ID   A0JNY3_MOUSE            Unreviewed;       772 AA.
AC   A0JNY3;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAR-2011, entry version 36.
DE   SubName: Full=Gphn protein;
GN   Name=Gphn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC127058; AAI27059.1; -; mRNA.
DR   IPI; IPI00816946; -.
DR   RefSeq; NP_666077.2; NM_145965.2.
DR   UniGene; Mm.341742; -.
DR   UniGene; Mm.363753; -.
DR   UniGene; Mm.453131; -.
DR   ProteinModelPortal; A0JNY3; -.
DR   SMR; A0JNY3; 13-181, 354-772.
DR   STRING; A0JNY3; -.
DR   PRIDE; A0JNY3; -.
DR   Ensembl; ENSMUST00000110388; ENSMUSP00000106018; ENSMUSG00000047454.
DR   GeneID; 268566; -.
DR   KEGG; mmu:268566; -.
DR   UCSC; uc007nzd.1; mouse.
DR   CTD; 268566; -.
DR   MGI; MGI:109602; Gphn.
DR   eggNOG; roNOG11629; -.
DR   HOGENOM; HBG731522; -.
DR   HOVERGEN; HBG005828; -.
DR   InParanoid; A0JNY3; -.
DR   OMA; SCPTPKX; -.
DR   PhylomeDB; A0JNY3; -.
DR   Bgee; A0JNY3; -.
DR   Genevestigator; A0JNY3; -.
DR   GO; GO:0019897; C:extrinsic to plasma membrane; TAS:MGI.
DR   GO; GO:0005622; C:intracellular; IDA:MGI.
DR   GO; GO:0008092; F:cytoskeletal protein binding; TAS:MGI.
DR   GO; GO:0007529; P:establishment of synaptic specificity at neuromuscular junction; IMP:MGI.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:InterPro.
DR   InterPro; IPR020817; Mo_cofactor_synthesis.
DR   InterPro; IPR008284; MoCF_biosynth_CS.
DR   InterPro; IPR005111; MoeA_C_domain_IV.
DR   InterPro; IPR005110; MoeA_linker/N.
DR   InterPro; IPR001453; Mopterin-bd.
DR   Gene3D; G3DSA:2.40.340.10; G3DSA:2.40.340.10; 1.
DR   Gene3D; G3DSA:3.40.980.10; MPT_bd; 2.
DR   Pfam; PF00994; MoCF_biosynth; 2.
DR   Pfam; PF03454; MoeA_C; 1.
DR   Pfam; PF03453; MoeA_N; 1.
DR   SMART; SM00852; MoCF_biosynth; 2.
DR   SUPFAM; SSF53218; MoCF_biosynth; 2.
DR   SUPFAM; SSF63867; MoeA_C; 1.
DR   SUPFAM; SSF63882; MoeA_N; 1.
DR   TIGRFAMs; TIGR00177; molyb_syn; 2.
DR   PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
DR   PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   772 AA;  83666 MW;  D8AA1208A84BE3D2 CRC64;
     MATEGMILTN HDHQIRVGVL TVSDSCFRNL AEDRSGINLK DLVQDPSLLG GTISAYKIVP
     DEIEEIKETL IDWCDEKELN LILTTGGTGF APRDVTPEAT KEVIEREAPG MALAMLMGSL
     NVTPLGMLSR PVCGIRGKTL IINLPGSKKG SQECFQFILP ALPHAIDLLR DAIVKVKEVH
     DELEDLPSPP PPLSPPPTTS PHKQTEDKGV QCEEEEEEKK DSGVASTEDS SSSHITAAAL
     AAKKHPFYTS PALFMANHGQ PIPGLISYSH HATGSADKRI PDSIISRGVQ VLPRDTASLS
     TTPSESPRAQ ATSRLSTASC PTPKVQSRCS SKENILRASH SAVDITKVAR RHRMSPFPLT
     SMDKAFITVL EMTPVLGTEI INYRDGMGRV LAQDVYAKDN LPPFPASVKD GYAVRAADGP
     GDRFIIGESQ AGEQPTQTVM PGQVMRVTTG APIPCGADAV VQVEDTELIR ESDDGTEELE
     VRILVQARPG QDIRPIGHDI KRGECVLAKG THMGPSEIGL LATVGVTEVE VNKFPVVAVM
     STGNELLNPE DDLLPGKIRD SNRSTLLATI QEHGYPTINL GIVGDNPDDL LNALNEGISR
     ADVIITSGGV SMGEKDYLKQ VLDIDLHAQI HFGRVFMKPG LPTTFATLDI DGVRKIIFAL
     PGNPVSAVVT CNLFVVPALR KMQGILDPRP TIIKARLSCD VKLDPRPEYH RCILTWHHQE
     PLPWAQSTGN QMSSRLMSMR SANGLLMLPP KTEQYVELHK GEVVDVMVIG RL
//
ID   A0T1J8_MOUSE            Unreviewed;      1699 AA.
AC   A0T1J8;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   SubName: Full=LIM domain only 7;
GN   Name=Lmo7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6;
RA   Ott E.B., te Velthuis A.J.W., Bagowski C.P.;
RT   "Gene expression patterns of LIM-only protein 7 (LMO7) during
RT   embryogenesis in Danio rerio, Gallus gallus and Mus musculus.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 LIM zinc-binding domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
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DR   EMBL; EF071857; ABK60217.1; -; mRNA.
DR   IPI; IPI00659447; -.
DR   RefSeq; NP_963287.2; NM_201529.2.
DR   UniGene; Mm.479274; -.
DR   ProteinModelPortal; A0T1J8; -.
DR   SMR; A0T1J8; 16-170, 1031-1119, 1615-1698.
DR   STRING; A0T1J8; -.
DR   PhosphoSite; A0T1J8; -.
DR   Ensembl; ENSMUST00000100337; ENSMUSP00000097910; ENSMUSG00000033060.
DR   GeneID; 380928; -.
DR   KEGG; mmu:380928; -.
DR   UCSC; uc007uvx.1; mouse.
DR   CTD; 380928; -.
DR   MGI; MGI:1353586; Lmo7.
DR   eggNOG; roNOG04616; -.
DR   HOGENOM; HBG505523; -.
DR   HOVERGEN; HBG049143; -.
DR   InParanoid; A0T1J8; -.
DR   OrthoDB; EOG49GKFQ; -.
DR   Bgee; A0T1J8; -.
DR   Genevestigator; A0T1J8; -.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR003096; SM22_calponin.
DR   InterPro; IPR001781; Znf_LIM.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 1.
DR   Gene3D; G3DSA:2.10.110.10; Znf_LIM; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF00412; LIM; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   PRINTS; PR00888; SM22CALPONIN.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00132; LIM; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   2: Evidence at transcript level;
KW   LIM domain; Metal-binding; Zinc.
SQ   SEQUENCE   1699 AA;  192560 MW;  B35C5A303632E7AD CRC64;
     MEGMEDAEAD CSVAFAEAQR WVEAVTEKNF ETTDFRASLE NGVLLCDLIN KLKPGVVKKI
     NRLSTPIAGL DNINVFLRAC EQIGLKEAQL FHPGDLQDLS NRVTVKQEET DRRLKNVLIT
     LYWLGRKAQS NPYYNGPYLN LKAFETLLGQ ALTKALEDSS CLKRSGRDSG YGDIWCPDRG
     EFPAPPGSHR REDSFESLDS LGSRSLTSCS SDFTLRVGKE GCESDIDWEF TFKMQDYNKD
     DMSYRRISAI EPKSALPFNR FLPNKSKQPS YVPAPFEKKR PDKHEDNRRS WASPVYTETD
     GTFSSTQRRT WGPKMETWHT VQETSTSSWC VEEEEEKLTR MPNIVKDDLY VRKLSPVMPS
     PGSSFDQFLP KCWTPEDMNW KKIKRETYKP WYKEFQGFSQ FLLLQALQTY SDDILSSETS
     VKLDPTSGPR LITRRKNRSP APGYRAHDLE LPALDPDLEN DDFFVRKTGA FHANPCVLRA
     FEDFRSFSEP DDAVERDIIL QCREGELVLP DLEKDDMIVR RIPAQKKEVP LSGAPDRYQP
     VPFPEPWTLP PEIQAKFLSV LERTRPPKEQ SSGCRVLVPS YRQKKDDMLA RKIQSWKLGT
     AVPPISFKPG PCSEADLQKW EAIWEASRLR HRKRLMVERL FQKIYGENGS KSMSDVSAED
     VQNLRQVRYE EMQKIKSQLK EQDQKWQDDL AKWKNRRKSY TSDLQKKKEE REEIEKQALE
     KSDRSSKTFR EMLQDRESRG STVTSWRRTY SSDDILDDGV LPPTVTLSET SYQSERLEDE
     ARAHPAEMPK EDSTTFANRE DSVVAETQLA SHSPEEQRLA PSPSEEPRQA SGSSAEPHQA
     PLLSTEPRRT PLPSEEPHQA SLSSTLQRPS SLSSQQSWST RAESTRISAS LPRSYQRTDT
     ARLTSVVTAR PFGTSSRGIS SLPRSYTMDD GWKYNGDVEV VKREQLDLGR ATGPKPDSSH
     FISGSASEKE VIATEDVASL SSPTLPSSSL SHDRAVSSKA TFSSMSGLDS VSDSGEGRGS
     PLREVSRSLD QFSDMRVSIN QTPGNKPVFG FTIKWDISGI FVASVEQGSP AEFSQLQVDD
     EILAINNTKF SYKDTKKWEE VMANAQETGN LVMDVRRYGK SGSSETKWID TTSGIYNSDK
     SSSLSVTTDF SESLQSPYTE SKEVNGIHEE SNPFDSKASE SISLKNLKRR SQFFEQGSSD
     SVAPDLPVPT LSAPSRWAWD QEEERRRQER WQKEQDRLLQ EKYQREQEKL REEWQRAQQE
     AERENSKYLD EELMVLNSNS ISLTSREPVA ATWEATWSEG SKSLDSEGTR AGEEDRGQLE
     DDAVYEDQSQ KLQELEQEKK RKEQEAQEEE RRKQREAQAW AEAEAKAWAE AQARAEAEAK
     ARAEAQARAE AEAQKRAEAQ KLQAERERET SVKIYQYRRP IDSYDLPKRE DDTSGMLPTD
     RSKSRSTTEL NDPLIEKNGS SKYSERIGAT SFSHRSSKKD QAPSEAELER QQILQEMRKR
     TSLHNDNSWI RQRSASVNKE PICLPGIMRR GESLDNLDSQ RPGSWRQSPW HSQPAGVYAS
     SSVQDFSRPP PQLLSTSNRA YMRNPSSAVP PPAGSVKTSP GSPSPRSHSP SMSQSGSQLR
     NRSVSGKRVC SYCNNILGKG AAMIIETLGL SYHLHCFKCV SCGCDLGGSS SGAEVRIRNH
     QLYCNDCYLR FKSGRPTAM
//
ID   TBC25_MOUSE             Reviewed;         742 AA.
AC   A1A5B6; Q8BIM6; Q8BIW8;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   RecName: Full=TBC1 domain family member 25;
GN   Name=Tbc1d25;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Aorta, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May act as a GTPase-activating protein for Rab family
CC       protein(s).
CC   -!- SIMILARITY: Contains 1 Rab-GAP TBC domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC30751.1; Type=Erroneous initiation;
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DR   EMBL; AK040932; BAC30751.1; ALT_INIT; mRNA.
DR   EMBL; AK078145; BAC37146.1; -; mRNA.
DR   EMBL; AL663032; CAM19502.1; -; Genomic_DNA.
DR   EMBL; BC128566; AAI28567.1; -; mRNA.
DR   IPI; IPI00222302; -.
DR   RefSeq; NP_001159909.1; NM_001166437.1.
DR   RefSeq; NP_766066.2; NM_172478.3.
DR   UniGene; Mm.122963; -.
DR   ProteinModelPortal; A1A5B6; -.
DR   SMR; A1A5B6; 257-487.
DR   STRING; A1A5B6; -.
DR   PhosphoSite; A1A5B6; -.
DR   PRIDE; A1A5B6; -.
DR   Ensembl; ENSMUST00000039892; ENSMUSP00000047838; ENSMUSG00000039201.
DR   GeneID; 209815; -.
DR   KEGG; mmu:209815; -.
DR   NMPDR; fig|10090.3.peg.21190; -.
DR   UCSC; uc009sog.1; mouse.
DR   CTD; 209815; -.
DR   MGI; MGI:2444862; Tbc1d25.
DR   eggNOG; roNOG04533; -.
DR   HOGENOM; HBG358390; -.
DR   HOVERGEN; HBG103222; -.
DR   InParanoid; A1A5B6; -.
DR   OMA; KALFADY; -.
DR   OrthoDB; EOG4255SM; -.
DR   PhylomeDB; A1A5B6; -.
DR   NextBio; 372806; -.
DR   Bgee; A1A5B6; -.
DR   CleanEx; MM_TBC1D25; -.
DR   Genevestigator; A1A5B6; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005097; F:Rab GTPase activator activity; IEA:InterPro.
DR   GO; GO:0032313; P:regulation of Rab GTPase activity; IEA:InterPro.
DR   InterPro; IPR000195; RabGAP/TBC_dom.
DR   Pfam; PF00566; TBC; 1.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; RabGAP_TBC; 2.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
PE   2: Evidence at transcript level;
KW   GTPase activation; Phosphoprotein.
FT   CHAIN         1    742       TBC1 domain family member 25.
FT                                /FTId=PRO_0000288509.
FT   DOMAIN      282    488       Rab-GAP TBC.
FT   COMPBIAS     76     81       Poly-Ala.
FT   COMPBIAS     83     88       Poly-Glu.
FT   COMPBIAS    529    533       Poly-Gly.
FT   COMPBIAS    596    662       Pro-rich.
FT   MOD_RES     194    194       Phosphoserine (By similarity).
FT   MOD_RES     560    560       Phosphoserine (By similarity).
FT   CONFLICT    115    115       T -> A (in Ref. 1; BAC37146).
FT   CONFLICT    626    626       S -> Y (in Ref. 1; BAC30751).
SQ   SEQUENCE   742 AA;  82575 MW;  F1CD1A40BDB46F47 CRC64;
     MRPPAQARWE GQGPTAPLRL RSGARWGRGR PHCWVYVRVR VTIGYHLDRD DSGGMATTSA
     ASDSACSAAP PPVGGAQAAA AVEEEEREVV RVRVKKCESF LSPEFRSFAV DPQITSLDVL
     QHILIRAFDL NGKKNFGISY LARDRLGQET FLSLLSDWDL STAFATASKP YLQLRVDIRP
     SEDSPLLEDW DIISPKDVIG SDVLLAEKRS SLTTAALPFT QSILSQVGRT LSKVQQVLSW
     SYGEDVKPFK PPLSDAEFHT YLNHEGQLSR PEELRLRIYH GGVEPSLRKV VWRYLLNVYP
     DGLTGRERMD YMKRKSREYE QLKSEWAQRV NPEDLEFIRS TVLKDVLRTD RAHPYYAGPE
     DGPHLRALHD LLTTYAVTHP QVSYCQGMSD LASPILAVMD HEGHAFVCFC GIMKRLAANF
     HPDGRAMATK FAHLKLLLRH ADPDFYQYLQ EAGADDLFFC YRWLLLELKR EFAFDDALRM
     LEVTWSSLPP DPPEHEVELV GPPSQVADTG FGSHRGRPVR QRHMLRPAGG GGGAFEDAVV
     HLAASSQGPS GGGRLLRQAS LDGLQQLRDN MGLRKDHLVQ LSHPATLISS KSLSEPLLNS
     PDPLLSTSSR PDSPSSSSPP STQEASPSGD IAVGSPLMQE VGSPRDPGKP VPPPPPMGLP
     PPQEFGRGNP FMLFLCLAIL LEHRDHIMRN GLDYNELAMH FDRLVRKHHL GRVLRRAKAL
     FADYLQSEVW DSEEGAEATA PS
//
ID   A1BN54_MOUSE            Unreviewed;       887 AA.
AC   A1BN54;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   05-OCT-2010, entry version 29.
DE   SubName: Full=Alpha actinin 1a;
GN   Name=Actn1; Synonyms=Actn1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c;
RX   PubMed=16751418;
RA   Zhao Z., Deocharan B., Scherer P.E., Ozelius L.J., Putterman C.;
RT   "Differential binding of cross-reactive anti-DNA antibodies to
RT   mesangial cells: the role of alpha-actinin.";
RL   J. Immunol. 176:7704-7714(2006).
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DR   EMBL; DQ288940; ABB88726.1; -; mRNA.
DR   IPI; IPI00380436; -.
DR   UniGene; Mm.253564; -.
DR   UniGene; Mm.403477; -.
DR   ProteinModelPortal; A1BN54; -.
DR   SMR; A1BN54; 30-254, 267-739, 742-814, 816-887.
DR   STRING; A1BN54; -.
DR   Ensembl; ENSMUST00000021554; ENSMUSP00000021554; ENSMUSG00000015143.
DR   UCSC; uc007oaq.1; mouse.
DR   MGI; MGI:2137706; Actn1.
DR   eggNOG; roNOG11088; -.
DR   HOVERGEN; HBG050453; -.
DR   InParanoid; A1BN54; -.
DR   Bgee; A1BN54; -.
DR   Genevestigator; A1BN54; -.
DR   GO; GO:0030018; C:Z disc; IDA:MGI.
DR   GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR014837; EF-hand_Ca_insen.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 2.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF08726; efhand_Ca_insen; 1.
DR   Pfam; PF00435; Spectrin; 4.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM00150; SPEC; 2.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   2: Evidence at transcript level;
KW   Actin-binding; Repeat.
SQ   SEQUENCE   887 AA;  102720 MW;  3DE9A4FB303F7F8A CRC64;
     MDHYDSQQTN DYMQPEEDWD RDLLLDPAWE KQQRKTFTAW CNSHLRKAGT QIENIEEDFR
     DGLKLMLLLE VISGERLAKP ERGKMRVHKI SNVNKALDFI ASKGVKLVSI GAEEIVDGNV
     KMTLGMIWTI ILRFAIQDIS VEETSAKEGL LLWCQRKTAP YKNVNIQNFH ISWKDGLGFC
     ALIHRHRPEL IDYGKLRKDD PLTNLNTAFD VAERFLDIPK MLDAEDIVGT ARPDEKAIMT
     YVSSFYHAFS GAQKAETAAN RICKVLAVNQ ENEQLMEDYE KLASDLLEWI RRTIPWLENR
     VPENTMHAMQ QKLEDFRDYR RLHKPPKVQE KCQLEINFNT LQTKLRLSNR PAFMPSEGRM
     VSDINNAWGC LEQAEKGYEE WLLNEIRRLE RLDHLAEKFR QKASIHEAWT DGKEAMLRQK
     DYETATLSEI KALLKKHEAF ESDLAAHQDR VEQIAAIAQE LNELDYYDSP SVNARCQKIC
     DQWDNLGALT QKRREALERT EKLLETIDQL YLEYAKRAAP FNNWMEGAME DLQDTFIVHT
     IEEIQGLTTA HEQFKATLPD ADKERLAILG IHNEVSKIVQ TYHVNMAGTN PYTTITPQEI
     NGKWDHVRQL VPRRDQALTE EHARQQHNER LRKQFGAQAN VIGPWIQTKM EEIGRISIEM
     HGTLEDQLSH LRQYEKSIVN YKPKIDQLEC DHQLIQEALI FDNKHTNYNM EHIRVGWEQL
     LTTIARTINE VENQILTRDA KGISQEQMNE FRASFNHFDR KKTGMMDTDD FRACLISMGY
     NMGEAEFARI MSIVDPNRLG VVTFQAFIDF MSRETADTDT ADQVMASFKI LAGDKNYITE
     DELRRELPPD QAEYCIARMA PYAGPDSVPG ALDYMSFSTA LYGESDL
//
ID   A1E2I3_MOUSE            Unreviewed;       128 AA.
AC   A1E2I3;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAR-2011, entry version 38.
DE   SubName: Full=Chemokine receptor 4;
DE   Flags: Fragment;
GN   Name=Cxcr4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c;
RA   Huysentruyt L.C., Banerjee D., Seyfried T.N.;
RT   "Novel metastatic mouse tumor cells express multiple properties of
RT   macrophages.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
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DR   EMBL; EF101560; ABK96809.1; -; mRNA.
DR   IPI; IPI00849797; -.
DR   UniGene; Mm.1401; -.
DR   STRING; A1E2I3; -.
DR   Ensembl; ENSMUST00000052172; ENSMUSP00000053489; ENSMUSG00000045382.
DR   Ensembl; ENSMUST00000142893; ENSMUSP00000120153; ENSMUSG00000045382.
DR   MGI; MGI:109563; Cxcr4.
DR   eggNOG; roNOG04388; -.
DR   GeneTree; ENSGT00590000082948; -.
DR   HOVERGEN; HBG106917; -.
DR   InParanoid; A1E2I3; -.
DR   Bgee; A1E2I3; -.
DR   Genevestigator; A1E2I3; -.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0030426; C:growth cone; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0016494; F:C-X-C chemokine receptor activity; IEA:InterPro.
DR   GO; GO:0001667; P:ameboidal cell migration; IMP:MGI.
DR   GO; GO:0007420; P:brain development; IMP:MGI.
DR   GO; GO:0007281; P:germ cell development; IMP:MGI.
DR   GO; GO:0008354; P:germ cell migration; IMP:MGI.
DR   GO; GO:0008045; P:motor axon guidance; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IDA:MGI.
DR   GO; GO:0001569; P:patterning of blood vessels; IMP:MGI.
DR   GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
DR   GO; GO:0042098; P:T cell proliferation; IMP:MGI.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR001277; Chemokine_CXCR4.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00645; CXCCHMKINER4.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   G-protein coupled receptor; Membrane; Receptor; Transducer;
KW   Transmembrane.
FT   NON_TER       1      1
FT   NON_TER     128    128
SQ   SEQUENCE   128 AA;  14449 MW;  688807EA7E5E9AAE CRC64;
     YSSVLILAFI SLDRYLAIVH ATNSQRPRKL LAEKAVYVGV WIPALLLTIP DFIFADVSQG
     DISQGDDRYI CDRLYPDSLW MVVFQFQHIM VGLVLPGIVI LSCYCIIISK LSHSKGHQKR
     KALKTTVI
//
ID   A1ILH2_MOUSE            Unreviewed;        75 AA.
AC   A1ILH2;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   05-OCT-2010, entry version 15.
DE   SubName: Full=Chorein;
DE   Flags: Fragment;
GN   Name=Vps13c; Synonyms=Vps13c 3' variant I;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=17196930; DOI=10.1016/j.bbrc.2006.12.122;
RA   Mizuno E., Nakamura M., Agemura A., Kusumoto A., Ichiba M., Kurano Y.,
RA   Muroya S., Sano A.;
RT   "Brain-specific transcript variants of 5' and 3' ends of mouse VPS13A
RT   and VPS13C.";
RL   Biochem. Biophys. Res. Commun. 353:902-907(2007).
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DR   EMBL; AB281685; BAF44199.1; -; mRNA.
DR   IPI; IPI00761666; -.
DR   UniGene; Mm.241454; -.
DR   Ensembl; ENSMUST00000098601; ENSMUSP00000096201; ENSMUSG00000035284.
DR   MGI; MGI:2444207; Vps13c.
DR   Bgee; A1ILH2; -.
DR   Genevestigator; A1ILH2; -.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   75 AA;  8068 MW;  205FE4C28E3D64A9 CRC64;
     GIGKGLVGAV ARPTGGIIDM ASSTFQGIQR VAESTEEVSS LRPPRLIHED GIIRPYDRQE
     SEGSDLLEQE MGTQE
//
ID   A1L332_MOUSE            Unreviewed;      1161 AA.
AC   A1L332;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   SubName: Full=Atp8a1 protein;
GN   Name=Atp8a1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + phospholipid(In) = ADP +
CC       phosphate + phospholipid(Out).
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DR   EMBL; BC129872; AAI29873.1; -; mRNA.
DR   IPI; IPI00466422; -.
DR   UniGene; Mm.153230; -.
DR   STRING; A1L332; -.
DR   PRIDE; A1L332; -.
DR   Ensembl; ENSMUST00000113656; ENSMUSP00000109286; ENSMUSG00000037685.
DR   Ensembl; ENSMUST00000135930; ENSMUSP00000118379; ENSMUSG00000037685.
DR   MGI; MGI:1330848; Atp8a1.
DR   eggNOG; roNOG15226; -.
DR   HOVERGEN; HBG050601; -.
DR   PhylomeDB; A1L332; -.
DR   Bgee; A1L332; -.
DR   Genevestigator; A1L332; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015662; F:ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004012; F:phospholipid-translocating ATPase activity; IEA:InterPro.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   InterPro; IPR023306; ATPase_cation_domN.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR023300; ATPase_P-typ_cyto_domA.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR006539; ATPase_P-typ_Plipid-transl.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Gene3D; G3DSA:2.70.150.10; ATPase_P-typ_cyto_domA; 2.
DR   Gene3D; G3DSA:3.40.1110.10; ATPase_P-typ_cyto_domN; 1.
DR   Gene3D; G3DSA:3.40.50.1000; HAD-like_dom; 2.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SUPFAM; SSF81660; ATPase_cation_domN; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 4.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Hydrolase; Magnesium; Membrane; Nucleotide-binding;
KW   Transmembrane; Transmembrane helix.
SQ   SEQUENCE   1161 AA;  131179 MW;  498C948DE2D65D87 CRC64;
     MRRTVSEIRS RAEGYEKTDD VSEKTSLADQ EEVRTIFINQ PQLTKFCNNH VSTAKYNVIT
     FLPRFLYSQF RRAANSFFLF IALLQQIPDV SPTGRYTTLV PLLFILAVAA IKEIIEDIKR
     HKADNAVNKK QTQVLRNGAW EIVHWEKVNV GDIVIIKGKE YIPADTVLLS SSEPQAMCYI
     ETSNLDGETN LKIRQGLPAT SDIKDIDSLM RISGRIECES PNRHLYDFVG NIRLDGHGTV
     PLGADQILLR GAQLRNTQWV HGIVVYTGHD TKLMQNSTSP PLKLSNVERI TNVQILILFC
     ILIAMSLVCS VGSAIWNRRH SGKDWYLHLH YGGASNFGLN FLTFIILFNN LIPISLLVTL
     EVVKFTQAYF INWDLDMHYE PTDTAAMART SNLNEELGQV KYIFSDKTGT LTCNVMQFKK
     CTIAGVAYGH VPEPEDYGCS PDEWQSSQFG DEKTFNDPSL LDNLQNNHPT APIICEFLTM
     MAVCHTAVPE REGDKIIYQA ASPDEGALVR AAKQLNFVFT GRTPDSVIID SLGQEERYEL
     LNVLEFTSAR KRMSVVVRTP SGKLRLYCKG ADTVIYERLA ETSKYKEITL KHLEQFATEG
     LRTLCFAVAE ISESDFEEWR AVYHRASTSV QNRLLKLEES YELIEKNLQL LGATAIEDKL
     QDQVPETIET LMKADIKIWI LTGDKQETAI NIGHSCRLLK RNMGMIVINE GSLDGTRETL
     SRHCTTLGDA LRKENDFALI IDGKTLKYAL TFGVRQYFLD LALSCKAVIC CRVSPLQKSE
     VVEMVKKQVK VITLAIGDGA NDVSMIQTAH VGVGISGNEG LQAANSSDYS IAQFKYLKNL
     LMVHGAWNYN RVSKCILYCF YKNIVLYIIE IWFAFVNGFS GQILFERWCI GLYNVMFTAM
     PPLTLGIFER SCRKENMLKY PELYKTSQNA LDFNTKVFWV HCLNGLFHSV ILFWFPLKAL
     QYGTVFGNGK TSDYLLLGNF VYTFVVITVC LKAGLETSYW TWFSHIAIWG SIALWVVFFG
     IYSSLWPAVP MAPDMSGEAA MLFSSGVFWV GLLSIPVASL LLDVLYKVIK RTAFKTLVDE
     VQELEAKSQD PGAVVLGKSL TERAQLLKNV FKKNHVNLYR SESLQQNLLH GYAFSQDENG
     IVSQSEVIRA YDTTKQRPDE W
//
ID   A1L338_MOUSE            Unreviewed;      1185 AA.
AC   A1L338;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 33.
DE   SubName: Full=Rapgef1 protein;
GN   Name=Rapgef1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 Ras-GEF domain.
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DR   EMBL; BC129881; AAI29882.1; -; mRNA.
DR   IPI; IPI00652147; -.
DR   UniGene; Mm.298274; -.
DR   ProteinModelPortal; A1L338; -.
DR   SMR; A1L338; 949-1172.
DR   STRING; A1L338; -.
DR   Ensembl; ENSMUST00000095087; ENSMUSP00000092703; ENSMUSG00000039844.
DR   MGI; MGI:104580; Rapgef1.
DR   eggNOG; roNOG10012; -.
DR   HOVERGEN; HBG058477; -.
DR   InParanoid; A1L338; -.
DR   Bgee; A1L338; -.
DR   Genevestigator; A1L338; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:MGI.
DR   GO; GO:0005070; F:SH3/SH2 adaptor activity; TAS:MGI.
DR   GO; GO:0004871; F:signal transducer activity; TAS:MGI.
DR   GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR   GO; GO:0016337; P:cell-cell adhesion; IMP:MGI.
DR   GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:MGI.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR   InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR   InterPro; IPR001895; RasGRF_CDC25.
DR   Gene3D; G3DSA:1.10.840.10; RasGRF_CDC25; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00229; RasGEFN; 1.
DR   PROSITE; PS00720; RASGEF; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50212; RASGEF_NTER; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1185 AA;  132020 MW;  5D43E67308849DC5 CRC64;
     MSSGLGLRRS PEMSGKIEKA DSQRSHLSSF TMKLMDKFHS PKIKRTPSKK GKPAEVSKIP
     EKPVSKNLCW LEEKEKEVVS ALRYFKTIVD KMAIDKKVLE MLPGSASKVL EAILPLVQTD
     PRIQHSSALS SCYSRVYQSL ANLIRWSDQV MLEGVNSEDK EMVTTVKGVI KAVLDGVKEL
     VRLTIEKQGR PSPTSPVKPS SPASKPDGQP ELPLTDREME ILNKTTSVSP SAELLPDSTS
     EEVAPPKPPL PGIRVVDNSP PALPPKKRQS APSPTRVAVV APMSRATSGS SLPVGINRQD
     FDVECYTQRR LSGGSRSCGG ESPRLSPCSS TGKLSRSDEQ LSSLDRDSGQ CSRNTSCETL
     DHYDPDYEFL QQDLSNADQI PPQAACNLSP LPESLGESGP PFLGHPFQLP LGSCLQQEGQ
     QTDTPPALPE KKRRSAVSQT TDSSGCRVSY ERHPSQYDNI SEGDLQNPVP VQPVPYPPFA
     AVLPFQQGAS SASAEFVGDF SVPELAGDTE KPPPLPEKKN KHMLAYMQLL EDYSEPQPSM
     FYQTPQSEHI YQQKNKMLME VYGFSESFCG SDSTQELAPP PALPPKQRQL ASYAASSFSV
     SYCVQQTKVA FTPEDGSAAQ GLSVSVSNSF LNRHGSLPVP SYKSVFRSYS QDFMPHHQAS
     VQPFLPPTSS SSPHFPPVHT SQSSDLAVPT VSSPPPSTVD GPLSSSQDSS FHGNPVRLPS
     ETSFTDSEPP SGKDGHPRDP SVSSASGKDS RENGERSPKS LDGLESAQSE EEVDELSLID
     HNEIMARLTL KQEGDDGPDV RGGSGDILLV HATETDRKDL VLYCEAFLTT YRTFISPEEL
     IKKLQYRYEK FSPFADTFKK RVSKNTFFVL VRVVDELCLV ELTEEILKLL MELVFRLVCS
     GELSLARVLR KNILDKVDQK KLLRCAHSDQ PLAARGVAAR PGTLHDFHSH EIAEQLTLLD
     AELFYKIEIP EVLLWAKEQN EEKSPNLTQF TEHFNNMSYW VRSIIMLQEK AQDRERLLLK
     FIKIMKHLRK LNNFNSYLAI LSALDSAPIR RLEWQRQTSE GLAEYCTLID SSSSFRAYRA
     ALSEVEPPCI PYLGLILQDL TFVHLGNPDY IDGKVNFSKR WQQFNILDSM RCFQQAHYEI
     RRNDDIINFF NDFSDHLAEE ALWELSLKIK PRNITRRKTD REEKT
//
ID   A1L3P4_MOUSE            Unreviewed;       702 AA.
AC   A1L3P4;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 36.
DE   RecName: Full=Sodium/hydrogen exchanger;
GN   Name=Slc9a6; ORFNames=RP23-105E2.4-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RA   Lawlor S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1
CC       (CPA1) transporter (TC 2.A.36) family.
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DR   EMBL; BC130221; AAI30222.1; -; mRNA.
DR   EMBL; AL672085; CAQ12098.1; -; Genomic_DNA.
DR   EMBL; AC048362; CAQ12098.1; JOINED; Genomic_DNA.
DR   IPI; IPI00225023; -.
DR   RefSeq; NP_766368.2; NM_172780.3.
DR   UniGene; Mm.17815; -.
DR   ProteinModelPortal; A1L3P4; -.
DR   PhosphoSite; A1L3P4; -.
DR   PRIDE; A1L3P4; -.
DR   Ensembl; ENSMUST00000077741; ENSMUSP00000076922; ENSMUSG00000060681.
DR   GeneID; 236794; -.
DR   KEGG; mmu:236794; -.
DR   CTD; 236794; -.
DR   MGI; MGI:2443511; Slc9a6.
DR   eggNOG; roNOG12965; -.
DR   HOGENOM; HBG443570; -.
DR   HOVERGEN; HBG055575; -.
DR   InParanoid; A1L3P4; -.
DR   OMA; CLHIRVG; -.
DR   OrthoDB; EOG418BMW; -.
DR   Bgee; A1L3P4; -.
DR   Genevestigator; A1L3P4; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0015385; F:sodium:hydrogen antiporter activity; IEA:InterPro.
DR   GO; GO:0006885; P:regulation of pH; IEA:InterPro.
DR   InterPro; IPR006153; Cation/H_exchanger.
DR   InterPro; IPR018422; Cation/H_exchanger_CPA1.
DR   InterPro; IPR002090; Na/H_exchanger_6.
DR   InterPro; IPR004709; NaH_exchanger.
DR   PANTHER; PTHR10110; Cation/H_exchanger_cons-reg; 1.
DR   Pfam; PF00999; Na_H_Exchanger; 1.
DR   PRINTS; PR01084; NAHEXCHNGR.
DR   PRINTS; PR01088; NAHEXCHNGR6.
DR   TIGRFAMs; TIGR00840; b_cpa1; 1.
PE   1: Evidence at protein level;
KW   Antiport; Ion transport; Membrane; Sodium; Sodium transport;
KW   Transmembrane; Transport.
SQ   SEQUENCE   702 AA;  77953 MW;  243F0126533B5547 CRC64;
     MAGARRGWRL APVRRGVCGP RARPLMRPLW LLFAVSFFGW TGALDGSGGT TRAMDEEIVS
     EKQAEESHRQ DSANLLIFIL LLTLTILTIW LFKHRRARFL HETGLAMIYG LLVGLVLRYG
     IHVPSDVNNV TLSCEVQSSP TTLLVNVSGK FYEYTLKGEI SSHELNNVQD NEMLRKVTFD
     PEVFFNILLP PIIFYAGYSL KRRHFFRNLG SILAYAFLGT AISCFVIGSI MYGCVTLMKV
     TGQLAGDFYF TDCLLFGAIV SATDPVTVLA IFHELQVDVE LYALLFGESV LNDAVAIVLS
     SSIVAYQPAG DNSHTFDVTA MFKSIGIFLG IFSGSFAMGA ATGVVTALVT KFTKLREFQL
     LETGLFFLMS WSTFLLAEAW GFTGVVAVLF CGITQAHYTY NNLSTESQHR TKQLFELLNF
     LAENFIFSYM GLTLFTFQNH VFNPTFVVGA FIAIFLGRAA NIYPLSLLLN LGRRSKIGSN
     FQHMMMFAGL RGAMAFALAI RDTATYARQM MFSTTLLIVF FTVWVFGGGT TAMLSCLHIR
     VGVDSDQEHL GVPDNERRTT KAESAWLFRM WYNFDHNYLK PLLTHSGPPL TTTLPACCGP
     IARCLTSPQA YENQEQLKDD DSDLILNDGD ISLTYGDSTV NTESATASAP RRFMGNSSED
     ALDRELTFGD HELVIRGTRL VLPMDDSEPA LNSLDDTRHS PA
//
ID   A1L3S9_MOUSE            Unreviewed;       567 AA.
AC   A1L3S9;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 24.
DE   SubName: Full=Phactr2 protein;
GN   Name=Phactr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC130264; AAI30265.1; -; mRNA.
DR   IPI; IPI00462897; -.
DR   RefSeq; NP_001182025.1; NM_001195096.1.
DR   UniGene; Mm.283359; -.
DR   UniGene; Mm.338311; -.
DR   Ensembl; ENSMUST00000105544; ENSMUSP00000101183; ENSMUSG00000062866.
DR   GeneID; 215789; -.
DR   KEGG; mmu:215789; -.
DR   CTD; 215789; -.
DR   MGI; MGI:2446138; Phactr2.
DR   eggNOG; roNOG05811; -.
DR   GeneTree; ENSGT00390000004420; -.
DR   HOVERGEN; HBG108246; -.
DR   Bgee; A1L3S9; -.
DR   Genevestigator; A1L3S9; -.
DR   InterPro; IPR004018; RPEL_repeat.
DR   Pfam; PF02755; RPEL; 3.
DR   SMART; SM00707; RPEL; 4.
DR   PROSITE; PS51073; RPEL; 4.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   567 AA;  62314 MW;  0E29A26A6DB4D010 CRC64;
     MGQTSVSALS PQPGSVDGLD KASIANSDGP PAGSQTPPFK RKGKLSTIGK IFKPWKWRKK
     KTSDKFRETS AVLERKISTR QSREELIRRG LLKELPDQDG DVTVNFENSN GHMIHIGEEA
     TQEENVGKPE EGSDSVCEKT PPREEQAEEK TAASRAGSSH PKKATGSKAS ASPSTSSTSS
     RPRAPKESLA GKAGLVGTTR GKKKISKQPV ASRLSPSTTT SDTPSLKGEL SDTGIESLTP
     EETVAGAEEQ ATSKSKAAIA LPPSTAPPSP PALLLPPEDQ CTIALDTPMV LVSDGPTLPV
     SALDTSQLLW TEEPSSRTSP YSSTGLGGSR EQAKCFTTKD ELGPQLLTPG QMGDSSESFS
     APEDEAPREY QANDSDSDGP ILYTDDDDEE DDDDDSSGES ALASKIRRRD TLAIKLGNRP
     SKKELEDKNI LQRTSEEERQ ELRQQIGTKL VRRLSQRPTT EELEQRNILK QKNEEEEQEA
     KMELKRRLSR KLSLRPTVAE LQARRILRFN EYVEVTDSPD YDRRADKPWA RLTPADKAAI
     RKELNEFKST EMEVHEESRQ FTRFHRP
//
ID   AK17B_MOUSE             Reviewed;         959 AA.
AC   A2A3V1; B0QZD2; Q0P534; Q8BR01; Q8C6P6;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 2.
DT   08-MAR-2011, entry version 29.
DE   RecName: Full=A-kinase anchor protein 17B;
DE            Short=AKAP-17B;
DE   AltName: Full=Protein Talia;
DE   AltName: Full=Protein kinase A-anchoring protein 17B;
DE            Short=PRKA17B;
DE   AltName: Full=Splicing factor, arginine/serine-rich 17B;
GN   Name=Akap17b; Synonyms=Sfrs17b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-304.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Oviduct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 508-959.
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=17302988; DOI=10.1186/1471-213X-7-8;
RA   Frankenberg S., Smith L., Greenfield A., Zernicka-Goetz M.;
RT   "Novel gene expression patterns along the proximo-distal axis of the
RT   mouse embryo before gastrulation.";
RL   BMC Dev. Biol. 7:8-8(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-673, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Splice factor regulating alternative splice site
CC       selection for certain mRNA precursors (By similarity).
CC   -!- SUBUNIT: Monomer. Component of the spliceosome (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle (By similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- DEVELOPMENTAL STAGE: Uniformally expressed in the extraembryonic
CC       ectoderm at E5.5. Restricted to the distal part of the
CC       extraembryonic ectoderm at E6.5-E7.5.
CC   -!- MISCELLANEOUS: 'Talia' means 'waistline' in Polish.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC35651.1; Type=Frameshift; Positions=126;
CC       Sequence=CAQ12496.1; Type=Erroneous gene model prediction;
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DR   EMBL; AL450397; CAM13291.2; -; Genomic_DNA.
DR   EMBL; AL450397; CAQ12496.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AK046007; BAC32570.2; -; mRNA.
DR   EMBL; AK054091; BAC35651.1; ALT_FRAME; mRNA.
DR   EMBL; BC120735; AAI20736.1; -; mRNA.
DR   EMBL; BC131917; AAI31918.1; -; mRNA.
DR   IPI; IPI00606284; -.
DR   RefSeq; NP_001075425.1; NM_001081956.1.
DR   UniGene; Mm.116704; -.
DR   STRING; A2A3V1; -.
DR   PRIDE; A2A3V1; -.
DR   Ensembl; ENSMUST00000051906; ENSMUSP00000052042; ENSMUSG00000059708.
DR   GeneID; 338351; -.
DR   KEGG; mmu:338351; -.
DR   CTD; 338351; -.
DR   MGI; MGI:2443758; Akap17b.
DR   eggNOG; maNOG10022; -.
DR   GeneTree; ENSGT00440000039314; -.
DR   InParanoid; A2A3V1; -.
DR   OrthoDB; EOG45HRWT; -.
DR   NextBio; 400117; -.
DR   Bgee; A2A3V1; -.
DR   Genevestigator; A2A3V1; -.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   RNA-binding; Spliceosome.
FT   CHAIN         1    959       A-kinase anchor protein 17B.
FT                                /FTId=PRO_0000343419.
FT   DOMAIN      145    253       RRM.
FT   COILED      261    334       Potential.
FT   COMPBIAS    425    428       Poly-Glu.
FT   COMPBIAS    742    745       Poly-Glu.
FT   COMPBIAS    846    849       Poly-Ser.
FT   MOD_RES     673    673       Phosphothreonine.
FT   CONFLICT    126    126       E -> K (in Ref. 2; BAC35651).
SQ   SEQUENCE   959 AA;  111066 MW;  B8663A72ECD8F434 CRC64;
     MTVTVVYDNS EATELCAAQH LYLKPIAKLM INVLLPECIE PVRPFSNWEV LDQLKSLICP
     DQFTTVRLSK STKDFIRFEG EAETRSLVQI LKAKLHGKII KLNGLKTDLK VVATDAQGEW
     EHFPKEKEAS VIEGAEEQDH DKGPDSIYFE GLPCKWFAPK GSSGEKPCEE ILRVVFESFG
     KIKNVDIPML DPYREVMTGG SFGGLNFGLQ TFEAFIQYQE STDFIKAMES LRGMKLMLKG
     DDGKALACNI KVMFDTTKHF SEGAIQRRNQ ERLKLQELEE ERKKEKKREE EVAERKRKDE
     VRKAQEKRKK ARDRRRALKE RDRHRQRKEK VKTKPEARQE LDSSGEWEER KYLLARRRVE
     ALRLLRVLLK KIAVWMRKEK NLKPCQTHIS LLLNCLGSTQ CNPQEVGVMK SEAHHTPGTA
     LKSPEEEELN TRHLLDWEEM PSYQASTLDL SQKAEKRCYQ ASKSDNKQKQ KGKKKTKAQL
     QKSSHTPGVK QMRHSARKEE TGKVLSDGCD YSLVSDQNSL QSTMIADQSL AKEDHASSNE
     SHSSRQAVIN RGRKQKIYET DEFIDYLLNY YQTPEYARFC LEASHLTSTC QWQRDVYAKG
     DGFQIYLRKQ GYHSNSLSEE ESLQGIEQDE EQDWPQVYIK DPESKSQKTG KINYAKEFTK
     KLKNHCKDIA SETDEHLSPT DGESYPVEKI HSHGVKDSQH IRKSPVSSSL RSVDVGLPLA
     DFLEEISSDS ECFSETLSMN QEEEERSMAV YNSSPEKRPL GTDKISTCKQ KTKSSQQTLC
     SEWKHDNEGK YSKHRVRAPG KRSKSELRYS WLEEEGDSIR VDKNISKTRG KLAPKHMLDE
     GQYHESSSSD ELESTTRKKR RLTSGMFDQN VKYRPLHMPS MPPKRARAFY LGYFSRKRQT
     PWKSEYNQDV RRFKRYENSE DYTLDSDNYY VSHDDNQEHI EYGSYLGDSY SSSLYFKMF
//
ID   CUL4B_MOUSE             Reviewed;         970 AA.
AC   A2A432; Q3TU30; Q8BSL3; Q8CHD6; Q91YZ7; Q99KS9; Q9CZM5;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 39.
DE   RecName: Full=Cullin-4B;
DE            Short=CUL-4B;
GN   Name=Cul4b; Synonyms=mKIAA0695;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=129/Sv; TISSUE=Embryonic carcinoma;
RX   PubMed=16052071; DOI=10.1007/BF02703670;
RA   Tripathi R., Sastry K.S., Kota S.K., Srinivas U.K.;
RT   "Cloning and characterization of mouse cullin4B/E3 ubiquitin ligase.";
RL   J. Biosci. 30:329-337(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic head, Head, and Wolffian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 204-970 (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
CC   -!- FUNCTION: Core component of multiple cullin-RING-based E3
CC       ubiquitin-protein ligase complexes which mediate the
CC       ubiquitination and subsequent proteasomal degradation of target
CC       proteins. The functional specificity of the E3 ubiquitin-protein
CC       ligase complex depends on the variable substrate recognition
CC       subunit. CUL4B may act within the complex as a scaffold protein,
CC       contributing to catalysis through positioning of the substrate and
CC       the ubiquitin-conjugating enzyme. Plays a role as part of the E3
CC       ubiquitin-protein ligase complex in polyubiquitination of CDT1,
CC       histone H2A, histone H3 and histone H4 in response to radiation-
CC       induced DNA damage. Targeted to UV damaged chromatin by DDB2 and
CC       may be important for DNA repair and DNA replication. Required for
CC       ubiquitination of cyclin E, and consequently, normal G1 cell cycle
CC       progression. Regulates the mammalian target-of-rapamycin (mTOR)
CC       pathway involved in control of cell growth, size and metabolism.
CC       Specific CUL4B regulation of the mTORC1-mediated pathway is
CC       dependent upon 26S proteasome function and requires interaction
CC       between CUL4B and MLST8 (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Component of multiple DCX (DDB1-CUL4-X-box) E3 ubiquitin-
CC       protein ligase complexes that seem to be formed of DDB1, CUL4A or
CC       CUL4B, RBX1 and a variable substrate recognition component which
CC       seems to belong to a protein family described as DCAF (Ddb1- and
CC       Cul4-associated factor) or CDW (CUL4-DDB1-associated WD40-repeat)
CC       proteins. Component of the DCX(DTL) complex with the putative
CC       substrate recognition component DTL. Component of the DCX(DDB2)
CC       complex with the putative substrate recognition component DDB2.
CC       Part of a complex with RBX1 and TIP120A/CAND1. Interacts with RBX1
CC       GRWD1, MLST8, SMU1, TLE2, TLE3, VPRBP, DDA1, DCAF6, DCAF17, DDB2,
CC       DCAF8, TIP120A/CAND1 and TMEM113. Interacts with cyclin E and with
CC       importins alpha-1 (KPNA2), alpha-3 (KPNA4), alpha-5 (KPNA1) and
CC       beta-1 (KPNB1). May interact with WDR26, WDR51B, SNRNP40, WDR61,
CC       WDR76 and WDR5 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A2A432-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2A432-2; Sequence=VSP_039242;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Neddylated. Deneddylated via its interaction with the COP9
CC       signalosome (CSN) complex (By similarity).
CC   -!- SIMILARITY: Belongs to the cullin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH04026.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=AAH10347.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAC41443.3; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; AY330868; AAP84984.1; -; mRNA.
DR   EMBL; AK012410; BAB28222.2; -; mRNA.
DR   EMBL; AK032701; BAC27992.1; -; mRNA.
DR   EMBL; AK160998; BAE36141.1; -; mRNA.
DR   EMBL; AL513356; CAM17145.1; -; Genomic_DNA.
DR   EMBL; CH466570; EDL29019.1; -; Genomic_DNA.
DR   EMBL; BC004026; AAH04026.1; ALT_INIT; mRNA.
DR   EMBL; BC010347; AAH10347.1; ALT_INIT; mRNA.
DR   EMBL; AB093259; BAC41443.3; ALT_INIT; Transcribed_RNA.
DR   IPI; IPI00224689; -.
DR   IPI; IPI00473987; -.
DR   RefSeq; NP_001103612.1; NM_001110142.1.
DR   RefSeq; NP_082564.3; NM_028288.5.
DR   UniGene; Mm.327675; -.
DR   ProteinModelPortal; A2A432; -.
DR   SMR; A2A432; 252-970.
DR   STRING; A2A432; -.
DR   PRIDE; A2A432; -.
DR   Ensembl; ENSMUST00000050083; ENSMUSP00000059276; ENSMUSG00000031095.
DR   Ensembl; ENSMUST00000115118; ENSMUSP00000110771; ENSMUSG00000031095.
DR   GeneID; 72584; -.
DR   KEGG; mmu:72584; -.
DR   CTD; 72584; -.
DR   MGI; MGI:1919834; Cul4b.
DR   eggNOG; roNOG06853; -.
DR   HOGENOM; HBG622322; -.
DR   HOVERGEN; HBG003619; -.
DR   InParanoid; A2A432; -.
DR   OMA; HANGLTK; -.
DR   OrthoDB; EOG42FSH0; -.
DR   NextBio; 336543; -.
DR   Bgee; A2A432; -.
DR   Genevestigator; A2A432; -.
DR   GO; GO:0031465; C:Cul4B-RING ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0071445; P:cellular response to protein stimulus; IMP:MGI.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:MGI.
DR   GO; GO:0045750; P:positive regulation of S phase of mitotic cell cycle; IMP:MGI.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR016157; Cullin_CS.
DR   InterPro; IPR016158; Cullin_homology.
DR   InterPro; IPR001373; Cullin_N.
DR   InterPro; IPR019559; Cullin_neddylation_domain.
DR   InterPro; IPR016159; Cullin_repeat-like_dom.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2.
DR   Pfam; PF00888; Cullin; 1.
DR   Pfam; PF10557; Cullin_Nedd8; 1.
DR   SMART; SM00182; CULLIN; 1.
DR   SMART; SM00884; Cullin_Nedd8; 1.
DR   SUPFAM; SSF75632; Cullin_homology; 1.
DR   SUPFAM; SSF74788; Cullin_repeat-like; 1.
DR   PROSITE; PS01256; CULLIN_1; 1.
DR   PROSITE; PS50069; CULLIN_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; DNA damage; DNA repair;
KW   Isopeptide bond; Nucleus; Phosphoprotein; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   CHAIN         1    970       Cullin-4B.
FT                                /FTId=PRO_0000394426.
FT   MOTIF       112    115       Nuclear localization signal (By
FT                                similarity).
FT   COMPBIAS     36     56       Pro-rich.
FT   COMPBIAS    118    250       Ser-rich.
FT   MOD_RES     105    105       Phosphothreonine (By similarity).
FT   MOD_RES     106    106       Phosphothreonine (By similarity).
FT   MOD_RES     109    109       Phosphothreonine (By similarity).
FT   MOD_RES     110    110       Phosphoserine (By similarity).
FT   MOD_RES     192    192       Phosphoserine (By similarity).
FT   MOD_RES     195    195       Phosphoserine (By similarity).
FT   MOD_RES     196    196       Phosphoserine (By similarity).
FT   MOD_RES     197    197       Phosphoserine (By similarity).
FT   MOD_RES     198    198       Phosphoserine (By similarity).
FT   MOD_RES     199    199       Phosphoserine (By similarity).
FT   MOD_RES     200    200       Phosphoserine (By similarity).
FT   MOD_RES     202    202       Phosphothreonine (By similarity).
FT   MOD_RES     206    206       Phosphoserine (By similarity).
FT   MOD_RES     250    250       Phosphoserine (By similarity).
FT   CROSSLNK    916    916       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in NEDD8) (By
FT                                similarity).
FT   VAR_SEQ     693    721       Missing (in isoform 2).
FT                                /FTId=VSP_039242.
FT   CONFLICT     56     56       P -> A (in Ref. 2; BAB28222).
FT   CONFLICT    209    209       Q -> E (in Ref. 6; BAC41443).
FT   CONFLICT    593    593       K -> E (in Ref. 2; BAB28222).
FT   CONFLICT    933    933       Q -> R (in Ref. 1; AAP84984 and 2;
FT                                BAC27992).
FT   CONFLICT    966    966       Y -> S (in Ref. 6; BAC41443).
SQ   SEQUENCE   970 AA;  110699 MW;  87D518B268A21849 CRC64;
     MSRSTRSKER RENDTDSEDN SSETSNQERR RCRQGPPRPP YPPLLPPVFP PPTPPPQVRR
     TRGLQDLGAM KSVCPGTSGF SSPNPSAASA AAQEVRSATD GNTSTTPPTS AKKRKLNSSS
     SSSNSSNERE DFDSTSSSST PPQPRDSASP STSSFCLGVP VATSSHVPIQ KKLRFEDTLE
     FVGIDTKMAE ESSSSSSSSS PTAATSQQQQ QQQLKTKSIL ISSVASVHHA NGLAKSSTAV
     SSFANSKPGS AKKLVIKNFK DKPKLPENYT DETWQKLKEA VEAIQNSTSI KYNLEELYQA
     VENLCSHKIS ANLYKQLRQI CEDHIKAQIH QFREDSLDSV LFLKKIDRCW QNHCRQMIMI
     RSIFLFLDRT YVLQNSMLPS IWDMGLELFR AHIISDQKVQ TKTIDGILLL IERERNGEAI
     DRSLLRSLLS MLSDLQIYQD SFEQQFLQET NRLYAAEGQK LMQEREVPEY LHHVNKRLEE
     EADRLITYLD QTTQKSLIAS VEKQLLGEHL TAILQKGLNS LLDENRIQDL SLLYQLFSRV
     RGGVQVLLQQ WIEYIKAFGS TIVINPEKDK TMVQELLDFK DKVDHIIDTC FLKNEKFINA
     MKEAFETFIN KRPNKPAELI AKYVDSKLRA GNKEATDEEL EKMLDKIMII FRFIYGKDVF
     EAFYKKDLAK RLLVGKSASV DAEKSMLSKL KHECGAAFTS KLEGMFKDME LSKDIMIQFK
     QYMQNQNVPG NIELTVNILT MGYWPTYVPM EVHLPPEMVK LQEIFKTFYL GKHSGRKLQW
     QSTLGHCVLK AEFKEGKKEL QVSLFQTMVL LMFNEGEEFS LEEIKHATGI EDGELRRTLQ
     SLACGKARVL AKNPKGKDIE DGDKFICNDD FKHKLFRIKI NQIQMKETVE EQASTTERVF
     QDRQYQIDAA IVRIMKMRKT LSHNLLVSEV YNQLKFPVKP ADLKKRIESL IDRDYMERDK
     ENPNQYNYIA
//
ID   A2A472_MOUSE            Unreviewed;       547 AA.
AC   A2A472;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 32.
DE   SubName: Full=TOX high mobility group box family member 2;
GN   Name=Tox2; ORFNames=RP23-117O11.2-003;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Pearce A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL589876; CAM13813.1; -; Genomic_DNA.
DR   IPI; IPI00755976; -.
DR   UniGene; Mm.207709; -.
DR   ProteinModelPortal; A2A472; -.
DR   SMR; A2A472; 284-368.
DR   PRIDE; A2A472; -.
DR   Ensembl; ENSMUST00000099110; ENSMUSP00000096710; ENSMUSG00000074607.
DR   MGI; MGI:3611233; Tox2.
DR   eggNOG; roNOG08286; -.
DR   GeneTree; ENSGT00560000076898; -.
DR   HOGENOM; HBG447268; -.
DR   HOVERGEN; HBG051183; -.
DR   InParanoid; A2A472; -.
DR   OMA; SGQLPTI; -.
DR   OrthoDB; EOG44J2JB; -.
DR   PhylomeDB; A2A472; -.
DR   Bgee; A2A472; -.
DR   Genevestigator; A2A472; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR000910; HMG_HMG1/HMG2.
DR   InterPro; IPR000135; HMG_HMG1/HMG2_subgr.
DR   InterPro; IPR009071; HMG_superfamily.
DR   Gene3D; G3DSA:1.10.30.10; HMG-box; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   PRINTS; PR00886; HIGHMOBLTY12.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   4: Predicted;
KW   DNA-binding; Nucleus.
SQ   SEQUENCE   547 AA;  57797 MW;  702A67F77F01D611 CRC64;
     MGGGGAGPPA NRGPRVVGRL IKLLFLAFFS LSVLIMQQHL TEAVAGAFSR CLGFRGMRLR
     LLTRHWCIAG ASLQKFDGDS AYVGMSDGNP ELLSTSQTYN SQGESNEDYE IPPITPPNLP
     EPSLLHLGDH EAGYHSLCHG LAPNGLLPAY SYQAMDLPAI MVSNMLAQDG HLLSGQLPTI
     QEMVHSEVAA YDSGRPGPLL GRPAMLASHM SALSQSQLIS QMGIRSGIAH GSPSPPGSKS
     ATPSPSSSTQ EEESDAHFKI SGEKRPSVDP GKKAKNPKKK KKKDPNEPQK PVSAYALFFR
     DTQAAIKGQN PSATFGDVSK IVASMWDSLG EEQKQAYKRK TEAAKKEYLK ALAAYRASLV
     SKSPPDQGEA KNTQANPPAK MLPPKQPMYA MPGLASFLTP SDLQAFRSGA SPASLARTLG
     SKALLPGLST SPPPPSFPLS PSLHQQLPLP PHAQGTLLSP PLSMSPAPQP PVLPASMALQ
     VQLAMSPSPP GPQDFPHISD FSSGSGSRSP GPSNPSSSGD WDGSYPSGER GLGTCSLLPR
     DKSLYLT
//
ID   A2A482_MOUSE            Unreviewed;      1206 AA.
AC   A2A482;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 39.
DE   SubName: Full=Protein kinase C binding protein 1;
GN   Name=Zmynd8; Synonyms=Prkcbp1; ORFNames=RP23-108D12.1-015;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Lovell J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Kay M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RA   Tracey A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL589902; CAM13521.1; -; Genomic_DNA.
DR   EMBL; AL591712; CAM13521.1; JOINED; Genomic_DNA.
DR   EMBL; AL928840; CAM13521.1; JOINED; Genomic_DNA.
DR   EMBL; AL591712; CAM14839.1; -; Genomic_DNA.
DR   EMBL; AL589902; CAM14839.1; JOINED; Genomic_DNA.
DR   EMBL; AL928840; CAM14839.1; JOINED; Genomic_DNA.
DR   EMBL; AL928840; CAM27730.1; -; Genomic_DNA.
DR   EMBL; AL589902; CAM27730.1; JOINED; Genomic_DNA.
DR   EMBL; AL591712; CAM27730.1; JOINED; Genomic_DNA.
DR   IPI; IPI00625016; -.
DR   ProteinModelPortal; A2A482; -.
DR   SMR; A2A482; 251-359, 1010-1053.
DR   Ensembl; ENSMUST00000099084; ENSMUSP00000096683; ENSMUSG00000039671.
DR   Ensembl; ENSMUST00000109266; ENSMUSP00000104889; ENSMUSG00000039671.
DR   MGI; MGI:1918025; Zmynd8.
DR   HOVERGEN; HBG031823; -.
DR   Bgee; A2A482; -.
DR   Genevestigator; A2A482; -.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR021931; DUF3544.
DR   InterPro; IPR000313; PWWP.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR002893; Znf_MYND.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:1.20.920.10; Bromodomain; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF12064; DUF3544; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   Pfam; PF01753; zf-MYND; 1.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS50812; PWWP; 1.
DR   PROSITE; PS01360; ZF_MYND_1; 1.
DR   PROSITE; PS50865; ZF_MYND_2; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   4: Predicted;
KW   Kinase; Metal-binding; Transferase; Zinc.
SQ   SEQUENCE   1206 AA;  133560 MW;  4B94150530360132 CRC64;
     MDISTRSKDP VSTEKTAPKR RFPSPPHSSN GHSPQDSSTS PIKKKKKPGL LNSSNKEQDG
     RNDFYCWVCH REGQVLCCEL CPRVYHAKCL RLTSEPEGDW FCPECEKITV AECIETQSKA
     MTMLTIEQLS YLLKFAIQKM KQPGTDAFQK PVPLEQHPDY AEYIFHPMDL CTLEKNAKKK
     MYGCTEAFLA DAKWILHNCI IYNGGNHKLT QIAKVVIKIC EHEMNEIEVC PECYLAACQK
     RDNWFCEPCS NPHPLVWAKL KGFPFWPAKA LRDKDGQVDA RFFGQHDRAW VPVNNCYLMS
     KEIPFSVKKT KSIFNSAMQE MEVYVENIRR KFGVFNYSPF RTPYTPNNQY QMLLDPSNPS
     AGTAKTDKQE KVKLNFDMTA SPKILLSKPL LSGGAGRRIS LSDMPRSPTS TNSSVHTGSD
     VEQDPEKKAP SSHFSASEES MDFLDKSTAS PASTKTGQAG SLSGSPKPFS PQAPTPIMTK
     PDKTSTSTTG SILNLNLDRS KAEMDLKELS ESVQQQSAPV PLISPKRQIR SRFQLNLDKT
     IESCKAQLGI NEISEDVYTA VEHSDSEDSE KSESSDSEYV SDEEQKPKNE PEDPEDKEGS
     RVDKEAPAIK RKPKPTNQVE VKEEAKSNSP VSEKPDPTPA KDKASPEPEK DFVEKAKPSP
     HPTKDKLKGK DETDSPTVHL GLDSDSESEL VIDLGEDPSG REGRKNKKDP KVPSPKQDAI
     GKPPPSSTSA GNQSPPETPV LTRSATQAPA AGVTVAAATT STMSTVTVTA PATAVTGSPV
     KKQRPLLPKE TVPAVQRVVW NASSKFQTSS QKWHMQKIQR QQQQQQQQQQ SQQQSQQQQP
     QSSQGTRYQT RQAVKAVQQK EVTQSPSTST ITLVTSTQPA ALVSSSGSAS TLASAINADL
     PIATASADVA ADIAKYTSKM MDAIKGTMTE IYNDLSKNTT GSTIAEIRRL RIEIEKLQWL
     HQQELAEMKH NLELTMAEMR QSLEQERDRL IAEVKKQLEL EKQQAVDETK KKQWCANCKK
     EAIFYCCWNT SYCDYPCQQA HWPEHMKSCT QSATAPQQEA DAEASTETGN KSSQGNSSNT
     QSAPSEPASA PKEKEAPAEK SKDSSNSTLD LSGSRETPSS MLLGSNQSSV SKRCDKQPAY
     TPTTTDHQPH PNYPAQKYHS RSSKAGLWSS SEEKRASSRS EHSGGTSTKN LMPKESRESR
     LDAFWD
//
ID   A2A543_MOUSE            Unreviewed;       597 AA.
AC   A2A543;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   11-JAN-2011, entry version 35.
DE   SubName: Full=Calcium channel, voltage-dependent, beta 1 subunit;
GN   Name=Cacnb1; ORFNames=RP23-309H19.4-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Matthews N.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; AL591209; CAM20416.1; -; Genomic_DNA.
DR   IPI; IPI00929798; -.
DR   RefSeq; NP_660099.2; NM_145121.2.
DR   UniGene; Mm.41252; -.
DR   ProteinModelPortal; A2A543; -.
DR   SMR; A2A543; 74-417.
DR   STRING; A2A543; -.
DR   Ensembl; ENSMUST00000017552; ENSMUSP00000017552; ENSMUSG00000020882.
DR   GeneID; 12295; -.
DR   KEGG; mmu:12295; -.
DR   CTD; 12295; -.
DR   MGI; MGI:102522; Cacnb1.
DR   HOVERGEN; HBG050765; -.
DR   Bgee; A2A543; -.
DR   Genevestigator; A2A543; -.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IDA:MGI.
DR   GO; GO:0030315; C:T-tubule; IDA:MGI.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:MGI.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IGI:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0006612; P:protein targeting to membrane; IMP:MGI.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR005443; VDCC_L_b1su.
DR   InterPro; IPR000584; VDCC_L_bsu.
DR   PANTHER; PTHR11824; Ca_channel_B; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF12052; VGCC_beta4Aa_N; 1.
DR   PRINTS; PR01626; LCACHANNELB.
DR   PRINTS; PR01627; LCACHANNELB1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
SQ   SEQUENCE   597 AA;  65482 MW;  C0567EB24A6BBAEC CRC64;
     MVQKSGMSRG PYPPSQEIPM EVFDPSPQGK YSKRKGRFKR SDGSTSSDTT SNSFVRQGSA
     ESYTSRPSDS DVSLEEDREA LRKEAERQAL AQLEKAKTKP VAFAVRTNVG YNPSPGDEVP
     VQGVAITFEP KDFLHIKEKY NNDWWIGRLV KEGCEVGFIP SPVKLDSLRL LQEQTLRQNR
     LSSSKSGDNS SSSLGDVVTG TRRPTPPASA KQKQKSTEHV PPYDVVPSMR PIILVGPSLK
     GYEVTDMMQK ALFDFLKHRF DGRISITRVT ADISLAKRSV LNNPSKHIII ERSNTRSSLA
     EVQSEIERIF ELARTLQLVA LDADTINHPA QLSKTSLAPI IVYIKITSPK VLQRLIKSRG
     KSQSKHLNVQ IAASEKLAQC PPEMFDIILD ENQLEDACEH LAEYLEAYWK ATHPPSSTPP
     NPLLNRTMAT AALAASPAPV SNLQGPYLAS GDQPLDRATG EHASVHEYPG ELGQPPGLYP
     SNHPPGRAGT LRALSRQDTF DADTPGSRNS AYTEPGDSCV DMETDPSEGP GPGDPAGGGT
     PPARQGSWED EEDYEEEMTD NRNRGRNKAR YCAEGGGPVL GRNKNELEGW GQGVYIR
//
ID   A2A5A0_MOUSE            Unreviewed;       838 AA.
AC   A2A5A0;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 33.
DE   SubName: Full=ATPase, H+ transporting, lysosomal V0 subunit A1, isoform CRA_j;
DE   SubName: Full=ATPase, H+ transporting, lysosomal V0 subunit a isoform 1;
GN   Name=Atp6v0a1; ORFNames=RP23-278K23.1-001, mCG_20226;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Matthews L.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL591425; CAM19436.1; -; Genomic_DNA.
DR   EMBL; CH466677; EDL03873.1; -; Genomic_DNA.
DR   IPI; IPI00228525; -.
DR   RefSeq; NP_058616.1; NM_016920.2.
DR   UniGene; Mm.340818; -.
DR   UniGene; Mm.475829; -.
DR   STRING; A2A5A0; -.
DR   PRIDE; A2A5A0; -.
DR   Ensembl; ENSMUST00000044721; ENSMUSP00000044838; ENSMUSG00000019302.
DR   GeneID; 11975; -.
DR   KEGG; mmu:11975; -.
DR   CTD; 11975; -.
DR   MGI; MGI:103286; Atp6v0a1.
DR   HOVERGEN; HBG014606; -.
DR   PhylomeDB; A2A5A0; -.
DR   NextBio; 280107; -.
DR   Bgee; A2A5A0; -.
DR   Genevestigator; A2A5A0; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0033177; C:proton-transporting two-sector ATPase complex, proton-transporting domain; IEA:InterPro.
DR   GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR002490; ATPase_V0/A0-cplx_116kDa_su.
DR   PANTHER; PTHR11629; ATPase_V0/A0_116; 1.
DR   Pfam; PF01496; V_ATPase_I; 1.
PE   4: Predicted;
SQ   SEQUENCE   838 AA;  96294 MW;  1A96E0FA5D521FE0 CRC64;
     MGELFRSEEM TLAQLFLQSE AAYCCVSELG ELGKVQFRDL NPDVNVFQRK FVNEVRRCEE
     MDRKLRFVEK EIRKANIPIM DTGENPEVPF PRDMIDLEAN FEKIENELKE INTNQEALKR
     NFLELTELKF ILRKTQQFFD EMADPDLLEE SSSLLEPNEM GRGAPLRLGF VAGVINRERI
     PTFERMLWRV CRGNVFLRQA EIENPLEDPV TGDYVHKSVF IIFFQGDQLK NRVKKICEGF
     RASLYPCPET PQERKEMASG VNTRIDDLQM VLNQTEDHRQ RVLQAAAKNI RVWFIKVRKM
     KAIYHTLNLC NIDVTQKCLI AEVWCPVTDL DSIQFALRRG TEHSGSTVPS ILNRMQTNQT
     PPTYNKTNKF THGFQNIVDA YGIGTYREIN PAPYTVITFP FLFAVMFGDF GHGILMTLFA
     VWMVLRESRI LSQKHENEMF SMVFSGRYII LLMGLFSIYT GLIYNDCFSK SLNIFGSSWS
     VRPMFTQGNW TEETLLGSSV LQLNPAIPGV FGGPYPFGID PIWNIATNKL TFLNSFKMKM
     SVILGIIHML FGVSLSLFNH IYFKKPLNIY FGFIPEIIFM SSLFGYLVIL IFYKWTAYDA
     HSSRNAPSLL IHFINMFLFS YPESGNAMLY SGQKGIQCFL IVVAMLCVPW MLLFKPLILR
     HQYLRKKHLG TLNFGGIRVG NGPTEEDAEI IQHDQLSTHS EDAEEPTEDE VFDFGDTMVH
     QAIHTIEYCL GCISNTASYL RLWALSLAHA QLSEVLWTMV IHIGLHVRSL AGGLGLFFIF
     AAFATLTVAI LLIMEGLSAF LHALRLHWVE FQNKFYTGTG FKFLPFSFEH IREGKFDE
//
ID   A2A5N1_MOUSE            Unreviewed;       159 AA.
AC   A2A5N1;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 30.
DE   SubName: Full=Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, beta;
DE   Flags: Fragment;
GN   Name=Ywhab; ORFNames=RP23-321M14.1-002;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Almeida-King J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL591542; CAM20760.1; -; Genomic_DNA.
DR   IPI; IPI00750790; -.
DR   STRING; A2A5N1; -.
DR   PRIDE; A2A5N1; -.
DR   Ensembl; ENSMUST00000018470; ENSMUSP00000018470; ENSMUSG00000018326.
DR   Ensembl; ENSMUST00000131288; ENSMUSP00000117125; ENSMUSG00000018326.
DR   MGI; MGI:1891917; Ywhab.
DR   eggNOG; roNOG14110; -.
DR   GeneTree; ENSGT00550000074221; -.
DR   HOVERGEN; HBG050423; -.
DR   InParanoid; A2A5N1; -.
DR   PhylomeDB; A2A5N1; -.
DR   Bgee; A2A5N1; -.
DR   Genevestigator; A2A5N1; -.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019904; F:protein domain specific binding; IDA:MGI.
DR   GO; GO:0006605; P:protein targeting; IDA:MGI.
DR   InterPro; IPR000308; 14-3-3.
DR   PANTHER; PTHR18860; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
PE   4: Predicted;
KW   Monooxygenase; Oxidoreductase.
FT   NON_TER     159    159
SQ   SEQUENCE   159 AA;  18349 MW;  BCE39E9E4E860D91 CRC64;
     MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY KNVVGARRSS
     WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICNDVL ELLDKYLILN ATQAESKVFY
     LKMKGDYFRY LSEVASGENK QTTVSNSQQA YQEAFEISK
//
ID   A2A5R2_MOUSE            Unreviewed;      1792 AA.
AC   A2A5R2;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 36.
DE   SubName: Full=ADP-ribosylation factor guanine nucleotide-exchange factor 2 (Brefeldin A-inhibited);
DE   SubName: Full=ADp-ribosylation factor guanine nucleotide-exchange factor 2 (Brefeldin A-inhibited);
DE   SubName: Full=MCG14609;
GN   Name=Arfgef2; ORFNames=RP23-216D20.2-001, mCG_14609;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Sycamore N.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC158012; AAI58013.1; -; mRNA.
DR   EMBL; AL591703; CAM24646.1; -; Genomic_DNA.
DR   EMBL; AL591911; CAM24646.1; JOINED; Genomic_DNA.
DR   EMBL; CH466551; EDL06489.1; -; Genomic_DNA.
DR   IPI; IPI00137087; -.
DR   RefSeq; NP_001078964.1; NM_001085495.2.
DR   UniGene; Mm.297192; -.
DR   ProteinModelPortal; A2A5R2; -.
DR   SMR; A2A5R2; 648-840.
DR   PhosphoSite; A2A5R2; -.
DR   PRIDE; A2A5R2; -.
DR   Ensembl; ENSMUST00000099078; ENSMUSP00000096677; ENSMUSG00000074582.
DR   GeneID; 99371; -.
DR   KEGG; mmu:99371; -.
DR   NMPDR; fig|10090.3.peg.7453; -.
DR   CTD; 99371; -.
DR   MGI; MGI:2139354; Arfgef2.
DR   HOGENOM; HBG355338; -.
DR   HOVERGEN; HBG004846; -.
DR   InParanoid; A2A5R2; -.
DR   OMA; NIVELAF; -.
DR   OrthoDB; EOG4V9TPR; -.
DR   PhylomeDB; A2A5R2; -.
DR   NextBio; 353893; -.
DR   Bgee; A2A5R2; -.
DR   Genevestigator; A2A5R2; -.
DR   GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR015403; DUF1981_SEC7_assoc.
DR   InterPro; IPR000904; Sec7.
DR   InterPro; IPR023394; SEC7_alpha_orthog.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 4.
DR   Gene3D; G3DSA:1.10.1000.11; G3DSA:1.10.1000.11; 1.
DR   Pfam; PF09324; DUF1981; 1.
DR   Pfam; PF01369; Sec7; 1.
DR   SMART; SM00222; Sec7; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF48425; Sec7; 1.
DR   PROSITE; PS50190; SEC7; 1.
PE   1: Evidence at protein level;
SQ   SEQUENCE   1792 AA;  202240 MW;  23DF06EA23A34A71 CRC64;
     MQESQTKSMF VSRALEKILA DKEVKRPQHS QLRRACQVAL DEIKAELEKQ RLGAAAPPKA
     NFIEADKYFL PFELACQSKS PRVVSTSLDC LQKLIAYGHI TGNAPDSGAP GKRLIDRIVE
     TICNCFQGPQ TDEGVQLQII KALLTAVTSP HIEIHEGTIL QTVRTCYNIY LASKNLINQT
     TAKATLTQML NVIFTRMENQ VLQEARELEK PMQSKPQSPV IQATAGSPKF SRLKQSQAQS
     KPTTPEKAEL PNGDHAQSGL GKVSLENGEA PRERGSPVSG RAEPSRGTDS GAQEVVKDIL
     EDVVTSAVKE AAEKHGLPEP DRALGALECQ ECAVPPGVDE NSQTNGIADD RQSLSSADNL
     EPDVQGHQVA ARFSHILQKD AFLVFRSLCK LSMKPLGEGP PDPKSHELRS KVVSLQLLLS
     VLQNAGPVFR SHEMFVTAIK QYLCVALSKN GVSSVPDVFE LSLAIFLTLL SNFKMHLKMQ
     IEVFFKEIFL NILETSTSSF EHRWMVIQTL TRICADAQCV VDIYVNYDCD LNAANIFERL
     VNDLSKIAQG RSGHELGMTP LQELSLRKKG LECLVSILKC MVEWSKDLYV NPNHQATLGQ
     ERLPDQEMGD GKGLDMARRC SVTSVESTVS SGTQTAIQDD PEQFEVIKQQ KEIIEHGIEL
     FNKKPKRGIQ FLQEQGMLGA AVEDIAQFLH QEERLDSTQV GEFLGDSTRF NKEVMYAYVD
     QLDFCEKEFV SALRTFLEGF RLPGEAQKID RLMEKFAARY IECNQGQTLF ASADTAYVLA
     YSIIMLTTDL HSPQVKNKMT KEQYIKMNRG INDSKDLPEE YLSSIYDEIE GKKIAMKETK
     EHTIATKSTK QSVASEKQRR LLYNVEMEQM AKTAKALMEA VSHAKAPFTS ATHLDHVRPM
     FKLVWTPLLA AYSIGLQNCD DTEVASLCLE GIRCAVRIAC IFGMQLERDA YVQALARFSL
     LTASSSITEM KQKNIDTIKT LITVAHTDGN YLGNSWHEIL KCISQLELAQ LIGTGVKTRY
     LSGSGREREG SLKGHSLAGE EFMGLGLGNL VSGGVDKRQM ASFQESVGET SSQSVVVAVD
     RIFTGSTRLD GNAIVDFVRW LCAVSMDELA SPHHPRMFSL QKIVEISYYN MNRIRLQWSR
     IWHVIGDHFN KVGCNPNEDV AIFAVDSLRQ LSMKFLEKGE LANFRFQKDF LRPFEHIMKK
     NRSPTIRDMV IRCIAQMVSS QAANIRSGWK NIFAVFHQAA SDHDGNIVEL AFQTTGHIVS
     TIFQHHFPAA IDSFQDAVKC LSEFACNAAF PDTSMEAIRL IRFCGKYVSE RPRVLQEYTS
     DDMNVAPGDR VWVRGWFPIL FELSCIINRC KLDVRTRGLT VMFEIMKSYG HTFAKHWWQD
     LFRIVFRIFD NMKLPEQQSE KSEWMTTTCN HALYAICDVF TQFYEALHEV LLSDVFAQLQ
     WCVKQDNEQL ARSGTNCLEN LVISNGEKFS PAVWDETCNC MLDIFKTTIP HVLLTWRPAG
     MEEEVSDRHL DVDLDRQSLS SIDRNASERG QSQLSNPTDD SWKGAPYAHQ KLLASLLIKC
     VVQLELIQTI DNIVFYPATS KKEDAEHMVA AQQDTLDAEI HIETENQGMY KFMSSQHLFK
     LLDCLQESHS FSKAFNSNYE QRTVLWRAGF KGKSKPNLLK QETSSLACCL RILFRMYVDE
     NRRDSWDEIQ QRLLRVCSEA LAYFITVNSE SHREAWTSLL LLLLTKTLKI SDEKFKAHAS
     MYYPYLCEIM QFDLIPELRA VLRKFFLRIG LVYKIWIPEE PSQVPAALSS TW
//
ID   A2A654_MOUSE            Unreviewed;      3036 AA.
AC   A2A654;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 38.
DE   SubName: Full=Bromodomain PHD finger transcription factor;
GN   Name=Bptf; ORFNames=RP23-317F9.3-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Beasley H.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL596116; CAM20631.1; -; Genomic_DNA.
DR   IPI; IPI00649138; -.
DR   UniGene; Mm.343986; -.
DR   ProteinModelPortal; A2A654; -.
DR   SMR; A2A654; 404-450, 2855-3022.
DR   STRING; A2A654; -.
DR   PRIDE; A2A654; -.
DR   Ensembl; ENSMUST00000106763; ENSMUSP00000102374; ENSMUSG00000040481.
DR   MGI; MGI:2444008; Bptf.
DR   HOGENOM; HBG505875; -.
DR   HOVERGEN; HBG080062; -.
DR   InParanoid; A2A654; -.
DR   OMA; FHLRTSY; -.
DR   OrthoDB; EOG466VK1; -.
DR   Bgee; A2A654; -.
DR   Genevestigator; A2A654; -.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009952; P:anterior/posterior pattern formation; IMP:MGI.
DR   GO; GO:0001892; P:embryonic placenta development; IMP:MGI.
DR   GO; GO:0007492; P:endoderm development; IMP:MGI.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR004022; DDT_dom.
DR   InterPro; IPR018500; DDT_dom_subgr.
DR   InterPro; IPR018501; DDT_dom_superfamily.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:1.20.920.10; Bromodomain; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 2.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF02791; DDT; 1.
DR   Pfam; PF00628; PHD; 2.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00571; DDT; 1.
DR   SMART; SM00249; PHD; 2.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 2.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS50827; DDT; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 2.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   4: Predicted;
KW   Bromodomain; Metal-binding; Zinc.
SQ   SEQUENCE   3036 AA;  333228 MW;  DB5E7A095A97E3AA CRC64;
     MRGRRGRPPK QPAAPAAERC APAPPPPPPP PPPPPPPPPP PPPASGPIGG LRSRHRGSSR
     GRWAAAQAEV APKTRLSSPR GGGRRKQPPP PPPASGSSAS GPGRGGRGGG GGRTGGGGGH
     LARTTPARRA VNKVVYDDHE SDDDDEEEDM VSEEDEEEEE DGDAEETQDS EDEEEDDMEE
     DDDDSDYPEE MEDDDDDASY CTESSFRSHS TYSSTPGRRK PRVHRPRSPI LEEKDIPPLE
     FPKSSEDLMV PNEHIMNVIA IYEVVRNFGN VLRLSPFCFE DFCAALVSQE QCTLMAEMHV
     ALLKAVLREE DTSNTTFGPA DLKDSVNSTL YFIDGMTWPE VLRVYCESDK EYHHVLPYQE
     AEDYPYGPVE NKIKVLQFLV DQFLTTNIAR EELMSEGVIQ YDDHCRVCHK LGDLLCCETC
     SAVYHLECVK PPLEEVPEDE WQCEVCVAHK VPGVTDCVAE VQKNKPYVRH EPIGYDRSRR
     KYWFLNRRLI IEEDTDNENE KKVWYYSTKV QLAELIDCLD KGYWEAELCR VLEDIREEMQ
     QHMDVTEDLT NKARGSNKSF LAAANEEILD SLRIKRGEDI DCDQSPEDPE KDKHEGENNS
     SKDAEKSREE AEDPSADKDA DSKGLEEEPG HGKPEEPTEV GDKGNSVPAN LGDNTTNASP
     EETSPCDGRS PEGCLSETHD SSSMAEKKVA SELPPDVPED SNRTCDSSNT SATTASSQPN
     LETCSSSELT SSQSDSAKAA DDPEIGERDS HTPVSVHEEI GDFRLEKSNG EVSESPGAGK
     GTSGSTRIIT RLRNPESKLS QLKSQQVAAA AHEANKLFKE GKEVLVVNSQ GEVSRLSTKK
     EVVMKGNINN YFKLGQEGKY RVYHNQYSTN SFALNKHQHR EDHDKRRHLA HKFCLTPAGE
     FKWNGSVHGS KVLTISTLRL TITQLESNIP SSFLHPNWAS HRANWIKAVQ MCSKPREFAL
     ALAILECAVK PVVMLPIWRE SLGHTRLHRM TSIEREEKEK VKKKEKKQEE EETMQQATWV
     KYTFPVKHQV TGYGGWSWIS KTHVYRFLPK LPGNTNVNYR KPLDGAKNNT DENKDESEKR
     KSPRSPKKMK TECDSEQGET RDADATAGAA AGAMELSKEP EKKDQDVKEL LDSDNDKSFK
     EEPMEIDDTI KTESHVSSLE STEVDVVNVS EGFHLRTSYK KKTKSSKLDG LLERRIRQFT
     LEEKQRLEKL KLESGVKGAG KPPMGALKSS SESPGSTKAS EGHQGDSLRQ EQSPSSSQAS
     TVDLGLGGSQ SDPLVLGISP PSLSTHKPDP KDQVLDDVSI QSPGPNCQRQ NSVESDLDAR
     ISEPAGKGLE LSQTKTEVTD SSSDDSKPTS ADDVGILICK SRKLHSQDDS STVVSSSKST
     LPASVPKSPR DRDARAFSKA VDFDGRLGGD SEYSSTLENS SDNMCIRDSA EEDMVVQNSS
     EATSKRFIAP EQGGESVEST KCQVVSKSTE NCEDKLQGKV TEANGKKLGQ HPPKPEERAV
     NRCTDQVSLR HSVDRKNSEP RESEKKGQKA NKFQINGKDS KAKGYLKGPG TKDGSDGKVV
     SSAVEPKVNN INKVIPGNTK SLAGKESAAK PFINGDIIME ELSEQNTSET NSYSLSSSDA
     KGNHQDGLHT LPSTKESAST QVITPRAPCP DRNSLSQVED METESPEVKR VIPSPVRTGE
     GSNLSKGFMD DNGLPSSKDE NVNGESQRKT VITEVTTMTS TVATESKTVI KVAKGDKQTV
     VSSTENCARS TVTTTTTTVT KLSTPSPDTG VDTISVKEQS KTVVTTTVTD SLTTAGSTLV
     TSMTVSKEYS TRDRVKLMKF SRPKKTRSGT ALPSYRKFVT KSSKKSIFVL PNDDLKKLAR
     KGGIREVPYF NYNAKPALDI WPYPSPRPTF GITWRYRLQT VKSLAGVSLM LRLLWASLRW
     DDMAAKAPPG GGSTRTETSE TEITTTEIIK RRDVGPYGIR SEYCIRKIIC PIGVPEAPKE
     TPTPQRKGLR SSALRPKRPE TPKQTGPVII ESWVAEEELE LWEIRAFAER VEKEKAQAAE
     QQTKKRLEQQ KPAVIAASTT SPANNTSSTV SPAQKVMVAP LSGSVTPGTK MVLATKVGSP
     ATVTFQQNKN FHQTFATWVK QGQSNSGMVQ VQQKVLGIIP STTGPSQQTF TSFQPRTATV
     TIRPNTSASA GTTTTSQVIT GPQIRPGMTV IRTPLQQPAL GKAIIRTPVV VQPGTPQQVV
     TQIIRGQPVS TAISAPSTAS SAPVQKGLTP GAAAGPLQPS APHSPRPQQG QVKLTMAQLT
     QLTQGHGGNQ GLTVVIQGQG QTTGQLQLIP QGMTVLPGPG QQLMQAAMPN GTVQRFLFTP
     LSTSATAASS SSNSSSTTTN ATAAGSGEQK QSKILPQTQV QPATTLAPTQ SSSVSPAEAQ
     PQPAQPAAQP QPQPQPPAQP EVQTQPAVSS HVPSETQPSQ AQTSKPLVAT QCQPQSSVQG
     QSPVRVQSPP LTRIRPSTPS QVTPGQQPQV QTTASQPIPI PPPTSLQAPS QGQPQSQPQV
     QSSTQTLSSG QTLNQVTVLS PSCPQPQPQV IAVPQLQQVQ VLSQIQSQVV AQIQAQQSGV
     PQQIKLQLPI QVQQNSAAQT QSVVTVQAAS VQEQLQRVQQ LRDQQQKKKQ QIETEREHTL
     QASNQSEIIQ KQVVMKHNAV IEHLKQKKTM TPAEREENQR MIVCNQVMKY ILDKIDKEEK
     QAAKKRKREE SVEQKRSKQN ASKLSALLFK HKEQLKAEIL RKRALLDKEL QIQVQEELKR
     DLKMKREREM AQAVQANAAS VPTPSVPAPV PAPAPAAPPA PPRSPPPSTH SLPPAGHPTA
     PLPVTSQKRK REEEKDSKSK KKKMISTTSK EAKKDTRLYC ICKTPYDESK FYIGCDRCQN
     WYHGRCVGIL QSEADLIDEY VCPQCQSTED AMTVLTPLTE KDYEGLKRVL RSLQAHKMAW
     PFLEPVDPND APDYYGVIKE PMDLATMEER IQKRYYEKLT EFVADMTKIF DNCRYYNPRD
     TPFYQCAEVL ESFFVQKLKG FKASRSHNNK LQSTAP
//
ID   TANC2_MOUSE             Reviewed;        1994 AA.
AC   A2A690; A2A683; Q3TRZ3; Q5EBP6; Q69ZQ7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   RecName: Full=Protein TANC2;
DE   AltName: Full=Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 2;
GN   Name=Tanc2; Synonyms=Kiaa1148;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 416-1994 (ISOFORM 2).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 575-1994 (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1484-1994 (ISOFORM 1/2).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1534, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1534 AND SER-1549, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A2A690-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2A690-2; Sequence=VSP_033551;
CC   -!- SIMILARITY: Belongs to the TANC family.
CC   -!- SIMILARITY: Contains 11 ANK repeats.
CC   -!- SIMILARITY: Contains 3 TPR repeats.
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DR   EMBL; AL596246; CAM16873.1; -; Genomic_DNA.
DR   EMBL; AL596246; CAM16880.1; -; Genomic_DNA.
DR   EMBL; AL627312; CAM16880.1; JOINED; Genomic_DNA.
DR   EMBL; AL645524; CAM16880.1; JOINED; Genomic_DNA.
DR   EMBL; AL627312; CAM19362.1; -; Genomic_DNA.
DR   EMBL; AL596246; CAM19362.1; JOINED; Genomic_DNA.
DR   EMBL; AL645524; CAM19362.1; JOINED; Genomic_DNA.
DR   EMBL; AL645524; CAM22186.1; -; Genomic_DNA.
DR   EMBL; AL596246; CAM22186.1; JOINED; Genomic_DNA.
DR   EMBL; AL627312; CAM22186.1; JOINED; Genomic_DNA.
DR   EMBL; AK173111; BAD32389.1; -; mRNA.
DR   EMBL; BC089352; AAH89352.1; -; mRNA.
DR   EMBL; AK162382; BAE36883.1; -; mRNA.
DR   IPI; IPI00551112; -.
DR   IPI; IPI00648438; -.
DR   RefSeq; NP_851416.2; NM_181071.3.
DR   UniGene; Mm.22501; -.
DR   ProteinModelPortal; A2A690; -.
DR   SMR; A2A690; 339-385, 859-1245.
DR   PhosphoSite; A2A690; -.
DR   PRIDE; A2A690; -.
DR   Ensembl; ENSMUST00000100330; ENSMUSP00000097904; ENSMUSG00000053580.
DR   GeneID; 77097; -.
DR   KEGG; mmu:77097; -.
DR   CTD; 77097; -.
DR   MGI; MGI:2444121; Tanc2.
DR   eggNOG; roNOG09495; -.
DR   GeneTree; ENSGT00600000084024; -.
DR   HOGENOM; HBG443929; -.
DR   HOVERGEN; HBG061464; -.
DR   InParanoid; A2A690; -.
DR   OMA; TQQDLRV; -.
DR   OrthoDB; EOG42FSGQ; -.
DR   NextBio; 346476; -.
DR   Bgee; A2A690; -.
DR   Genevestigator; A2A690; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 2.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
DR   Pfam; PF00023; Ank; 4.
DR   SMART; SM00248; ANK; 11.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 6.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ANK repeat; Phosphoprotein; Repeat; TPR repeat.
FT   CHAIN         1   1994       Protein TANC2.
FT                                /FTId=PRO_0000333812.
FT   REPEAT      846    878       ANK 1.
FT   REPEAT      884    913       ANK 2.
FT   REPEAT      917    946       ANK 3.
FT   REPEAT      950    979       ANK 4.
FT   REPEAT      990   1019       ANK 5.
FT   REPEAT     1033   1062       ANK 6.
FT   REPEAT     1066   1095       ANK 7.
FT   REPEAT     1099   1128       ANK 8.
FT   REPEAT     1132   1161       ANK 9.
FT   REPEAT     1165   1194       ANK 10.
FT   REPEAT     1198   1227       ANK 11.
FT   REPEAT     1244   1277       TPR 1.
FT   REPEAT     1291   1324       TPR 2.
FT   REPEAT     1325   1358       TPR 3.
FT   MOD_RES     169    169       Phosphoserine (By similarity).
FT   MOD_RES     171    171       Phosphothreonine (By similarity).
FT   MOD_RES    1446   1446       Phosphoserine (By similarity).
FT   MOD_RES    1450   1450       Phosphoserine (By similarity).
FT   MOD_RES    1461   1461       Phosphoserine (By similarity).
FT   MOD_RES    1534   1534       Phosphoserine.
FT   MOD_RES    1538   1538       Phosphoserine (By similarity).
FT   MOD_RES    1549   1549       Phosphoserine.
FT   MOD_RES    1831   1831       Phosphoserine (By similarity).
FT   VAR_SEQ    1225   1225       I -> IGCQTLPSRPR (in isoform 2).
FT                                /FTId=VSP_033551.
SQ   SEQUENCE   1994 AA;  220263 MW;  A6A3B4F264CE3341 CRC64;
     MFRNSLKMLL TGGKSSRKNR SSDGGSEEPP DRRQSSVDSR QSRSGQGGIS TESDCAFEPD
     YAVPPLPVSE GDVEQELGPP PSVDEAANTL MTRLGFLLGE KVTEVQPSDQ YSMEVQDENQ
     TSAITQRISP CSTLTSSTAS PPASSPCSTL PPVSTNAAAK DCSYGAVTSP TSTLESRDSG
     IIATLTNYSE NMERTKYVGE GSKELGSGGN LKPWQSQKSS MDSCLYRVDE NMAASTYSLN
     KIPERNLETV LSQSVQSIPL YLMPRPNSVA ATSSAHLEDL AYLDEQRHTP LRTSLRMPRQ
     SLSGARTQQD LRVRFAPYRP PDISLKPLLF EVPSITTESV FVGRDWVFHE IDAQLQSSNA
     SVNQGVVIVG NIGFGKTAII SRLVALSCHG TRMRQIASDS PHASPKHVDA NRELPLTQAP
     SAHSSITSGS CPGTPEMRRR QEEAMRRLAS QVVAYHYCQA DNAYTCLVPE FVHNVAALLC
     RSPQLTAYRE QLLREPHLQS MLSLRSCVQD PMASFRRGVL EPLENLHKER KIPDEDFIIL
     IDGLNEAEFH KPDYGDTIVS FLSKMIGNFP SWLKLIVTVR TSLQEITKLL PFHRIFLDRL
     EENEAIDQDL QAYILHRIHS SSEIQNNISL NGKMDNTTFG KLSSHLKTLS QGSYLYLKLT
     FDLIEKGYLV LKSSSYKVVP VSLSEVYLLQ CNMKFPTQSS FDRVMPLLNV AVASLHPLTD
     EHIFQAINAG SIEGTLEWED FQQRMENLSM FLIKRRDMTR MFVHPSFREW LIWREEGEKT
     KFLCDPRSGH TLLAFWFSRQ EGKLNRQQTI ELGHHILKAH IFKGLSKKVG VSSSILQGLW
     ISYSTEGLSM ALASLRNLYT PNIKVSRLLI LGGANINYRT EVLNNAPILC VQSHLGYTEM
     VALLLEFGAN VDASSESGLT PLGYAAAAGF LSIVVLLCKK RAKVDHLDKN GQCALVHAAL
     RGHLEVVKFL IQCDWTMAGQ QQGVFKKSHA IQQALIAAAS MGYTEIVSYL LDLPEKDEEE
     VERAQINSFD SLWGETALTA AAGRGKLDVC RLLLEQGAAV AQPNRRGAVP LFSTVRQGHW
     QIVDLLLTHG ADVNMADKQG RTPLMMAASE GHLGTVDFLL AQGASIALMD KEGLTALSWA
     CLKGHLSVVR SLVDNGAATD HADKNGRTPL DLAAFYGDAE VVQFLVDHGA MIEHVDYSGM
     RPLDRAVGCR NTSVVVTLLK KGAKIGPATW AMATSKPDIM IILLSKLMEE GDMFYKKGKV
     KEAAQRYQYA LKKFPREGFG EDLKTFRELK VSLLLNLSRC RRKMNDFGMA EEFATKALEL
     KPKSYEAYYA RARAKRSSRQ FAAALEDLKE AIKLCPNNRE IQRLLMRVEE ECRQMQQQQQ
     QQPPPPPQQP PQELPEEETE PEPQHEDIYS VQDIFEEEYL EQDVENVSIG LQTEARPSQG
     LPVIQSPPSS PAHRDSAYIS SSPLGSHQVF DFRSNSSVGS PTRQGYQSTS PALSPTHQNS
     HYRPSPPHTS PAHQGASYRF SPPPVGGQSK EYPSPPPSPL RRGPQYRASP PAESMSVYRS
     QSGSPVRYQQ ETNVSQLPGR PKSPLSKMAQ RPYQMPQLPV AVPQQGLRLQ PAKAQIVRSN
     QPSSAVHSST VIPTGAYGQV AHSMASKYQS SQGDMGVSQS RLVYQGSIGG IVGDGRPVQH
     VQASLSAGAI CQHGGLTKED LPQRPSSAYR GGMRYSQTPQ IGRSQSASYY PVCHSKLDLE
     RSSSQLGSPD VSHLIRRPIS VNPNEIKPHP PTPRPLLHSQ SVGLRFSPSS NSISSTSNLT
     PTFRPSSSIQ QMEIPLKPAY DRSCDELSPV SPTQGGYPSE PTRSRTTPFM GIIDKTARTQ
     QYPHLHQQNR TWAVSSVDTV LSPTSPGNLP QPESFSPPSS ISNIAFYNKT NNAQNGHLLE
     DDYYSPHGML ANGSRGDLLE RVSQASSYPD VKVARTLPVA QAYQDNLYRQ LSRDSRQGQT
     SPIKPKRPFV ESNV
//
ID   F1712_MOUSE             Reviewed;         822 AA.
AC   A2A699; B7ZC48; Q05CH6; Q6P2L1;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 36.
DE   RecName: Full=Protein FAM171A2;
DE   Flags: Precursor;
GN   Name=Fam171a2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-507 (ISOFORM 1).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A2A699-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2A699-2; Sequence=VSP_032783;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the FAM171 family.
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DR   EMBL; AL596258; CAX15548.1; -; Genomic_DNA.
DR   EMBL; BC025575; AAH25575.1; -; mRNA.
DR   EMBL; BC064455; AAH64455.1; -; mRNA.
DR   IPI; IPI00396753; -.
DR   IPI; IPI00890142; -.
DR   RefSeq; NP_954670.2; NM_199200.2.
DR   UniGene; Mm.259924; -.
DR   PhosphoSite; A2A699; -.
DR   PRIDE; A2A699; -.
DR   Ensembl; ENSMUST00000049057; ENSMUSP00000038486; ENSMUSG00000034685.
DR   GeneID; 217219; -.
DR   KEGG; mmu:217219; -.
DR   CTD; 217219; -.
DR   MGI; MGI:2448496; Fam171a2.
DR   eggNOG; roNOG11820; -.
DR   GeneTree; ENSGT00530000063318; -.
DR   HOGENOM; HBG715100; -.
DR   HOVERGEN; HBG057508; -.
DR   InParanoid; A2A699; -.
DR   OMA; RRDSMTS; -.
DR   OrthoDB; EOG447FSS; -.
DR   NextBio; 375687; -.
DR   Bgee; A2A699; -.
DR   Genevestigator; A2A699; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR018890; Uncharacterised_FAM171.
DR   Pfam; PF10577; UPF0560; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Membrane; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     29       Potential.
FT   CHAIN        30    822       Protein FAM171A2.
FT                                /FTId=PRO_0000328772.
FT   TOPO_DOM     30    315       Extracellular (Potential).
FT   TRANSMEM    316    336       Helical; (Potential).
FT   TOPO_DOM    337    822       Cytoplasmic (Potential).
FT   COMPBIAS    710    718       Poly-Pro.
FT   CARBOHYD     66     66       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    201    201       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    221    221       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    265    265       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1    184       Missing (in isoform 2).
FT                                /FTId=VSP_032783.
SQ   SEQUENCE   822 AA;  87487 MW;  AA4A1CA28B3E4516 CRC64;
     MPPPSGPGVL ARLLPLLGLL LGGASRAPGK SPPEPPSPQE ILIKVQVYVS GELVPLARAS
     VDVFGNRTLL AAGTTDSEGV ATLPLSYRLG TWVLVTAARP GFLTNSVPWR VDKLPLYASV
     SLYLLPERPA TLILYEDLVH ILLGSPGARS QPWVQFQRRA ARLPVSSTYS QLWASLTPAS
     TQQEMRAFPA FLGTEASSSG NGSWLELIPL AAVSVHLLTG NGTEVPLSGP IHLSLPVPSE
     PRALAVGTSI PAWRFDPKSG LWVRNGTGVI RKEGRQLYWT FVSPQLGYWV AAMASPTSGL
     VTITSGIQDI GTYHTIFLLT ILAALALLVL ILLCLLIYYC RRRCLKPRQQ HRKLQLSGPS
     DNKRDQATSM SQLHLICGGP LEPTSSGDPE APPPGSLHSA FSSSRDLASS RDDFFRAKPR
     SASRPAAEPP GARTVEGAGL KSARSVEGPG GLEPSLDEYR RGPAGAAAFL HEPPSPPPSF
     DHYLGHKGAA ESKTPDFLLS QSVDQLARPP SLSQPGQLIF CGSIDHLKDN VYRNVMPTLV
     IPAHYVRLGG EAGAAGVGDE ATPPEGSAAG PARPFPQPDP QRPLMQGHAG AGGDSGGGEG
     WGGGRSAPVS GSVTIPVLFN ESTMAQLNGE LQALTEKKLL ELGVKPHPRA WFVSLDGRSN
     SQVRHSYIDL QAGSGGRSTD ASLDSGVDVH EARPARRRLP REERERAQLP APPPPAPPRL
     ALSEDTEPSS SESRTGLCSP EDNSLTPLLD EVVAPEGRAA TVPRGRGRSR GDSSRSSASE
     LRRDSLTSPE DELGAEVGDE AGDKKSPWQR REERPLMVFN VK
//
ID   A2A6P4_MOUSE            Unreviewed;       185 AA.
AC   A2A6P4;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   08-MAR-2011, entry version 22.
DE   SubName: Full=Likely orthologue of family with sequence similarity 104, member A (FAM104A);
GN   Name=D11Wsu99e; Synonyms=RP23-407I21.2; ORFNames=RP23-407I21.2-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Clark G.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
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DR   EMBL; AL603706; CAM23538.2; -; Genomic_DNA.
DR   IPI; IPI00762255; -.
DR   RefSeq; NP_613064.2; NM_138598.5.
DR   UniGene; Mm.261620; -.
DR   UniGene; Mm.351688; -.
DR   PRIDE; A2A6P4; -.
DR   Ensembl; ENSMUST00000120194; ENSMUSP00000113652; ENSMUSG00000041629.
DR   GeneID; 28081; -.
DR   KEGG; mmu:28081; -.
DR   CTD; 28081; -.
DR   MGI; MGI:106351; D11Wsu99e.
DR   HOVERGEN; HBG059882; -.
DR   OrthoDB; EOG4CJVJD; -.
DR   NextBio; 306624; -.
DR   Bgee; A2A6P4; -.
DR   Genevestigator; A2A6P4; -.
PE   1: Evidence at protein level;
SQ   SEQUENCE   185 AA;  19618 MW;  3904EBE62A52E32D CRC64;
     MGRRGGDTGS GCGPGRPEGD SAPAATTRAA AVRAQTRAGG RGGRRDTAPT VRCRRGAAPR
     RSPSPAAMSE RLRPRKRRRN GSDDDNHPPP QTKRSSRNPI FQDSWDTESS SSDSGGSSSS
     SSINSPDRAS GPESSLSHTI PGSCPSTPQP MPEQSALCQG PYFHINQTLK EAHFHSLQHR
     GRPPT
//
ID   CDR2L_MOUSE             Reviewed;         465 AA.
AC   A2A6T1;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 27.
DE   RecName: Full=Cerebellar degeneration-related protein 2-like;
GN   Name=Cdr2l; Synonyms=Gm21;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Belongs to the CDR2 family.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AL603828; CAM13809.1; -; Genomic_DNA.
DR   IPI; IPI00353932; -.
DR   RefSeq; NP_001074398.1; NM_001080929.1.
DR   UniGene; Mm.102872; -.
DR   PhosphoSite; A2A6T1; -.
DR   PRIDE; A2A6T1; -.
DR   Ensembl; ENSMUST00000053288; ENSMUSP00000052096; ENSMUSG00000050910.
DR   GeneID; 237988; -.
DR   KEGG; mmu:237988; -.
DR   NMPDR; fig|10090.3.peg.25610; -.
DR   CTD; 237988; -.
DR   MGI; MGI:2684867; Cdr2l.
DR   eggNOG; roNOG16124; -.
DR   HOVERGEN; HBG006695; -.
DR   InParanoid; A2A6T1; -.
DR   OMA; WPKTQPA; -.
DR   OrthoDB; EOG4KPTB8; -.
DR   NextBio; 383628; -.
DR   Bgee; A2A6T1; -.
DR   CleanEx; MM_CDR2L; -.
DR   Genevestigator; A2A6T1; -.
PE   2: Evidence at transcript level;
KW   Coiled coil; Phosphoprotein.
FT   CHAIN         1    465       Cerebellar degeneration-related protein
FT                                2-like.
FT                                /FTId=PRO_0000307235.
FT   COILED       31     64       Potential.
FT   COILED       91    142       Potential.
FT   COILED      188    266       Potential.
FT   COILED      350    377       Potential.
FT   MOD_RES     178    178       Phosphoserine (By similarity).
FT   MOD_RES     179    179       Phosphoserine (By similarity).
FT   MOD_RES     304    304       Phosphoserine (By similarity).
FT   MOD_RES     308    308       Phosphoserine (By similarity).
SQ   SEQUENCE   465 AA;  53213 MW;  F63244370A51DDA9 CRC64;
     MRRAAGMEDY SAEEEESWYD HQDLEQDLHL AAELGKTLLE RNKELEESLQ QMYSTNEEQV
     HEIEYLTKQL DTLRLVNEQH AKVYEQLDLT ARDLELTNQR LVMESKAAQQ KIHGLTETIE
     RLQSQVEELQ AQVEQLRGLE QLRIRREKRE RRRTIHTFPC LKELCTSSRC EDAFRLHSSS
     LELGPRPLEQ ENERLQTLVG VLRSQVSQER QRKERAEREY TVVLQEYTEL ERQLCEMEGC
     RLRVQELEAE LLELQQMKQA KTYLLAREEH LAEALLAPLT QAPEADDPQP GSGDDSNAQD
     GVSSPAASPS HAVRKSCSDT ALNAIVAKDP ASRHAGNLTL HANSVRRRGM SILREVDEQY
     HALLEKYEEL LSKCRQHGAG VRHAGVQTSR PISRDSSWRD LLGGEESPGE GKAGEKSLSQ
     HVEAVDKRLE QSQPEYKALF KEIFARIQKT KADINATKVK THSSK
//
ID   ZMYM4_MOUSE             Reviewed;        1549 AA.
AC   A2A791; Q3UFQ2; Q6ZQB9; Q80X47; Q8K1H5;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 38.
DE   RecName: Full=Zinc finger MYM-type protein 4;
DE   AltName: Full=Zinc finger protein 262;
GN   Name=Zmym4; Synonyms=Kiaa0425, Zfp262, Znf262;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-218.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 253-1549 (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1540; SER-1543 AND
RP   SER-1548, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A2A791-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2A791-2; Sequence=VSP_027515;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 9 MYM-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97947.1; Type=Erroneous initiation;
CC       Sequence=CAM19273.1; Type=Erroneous gene model prediction;
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DR   EMBL; AK129137; BAC97947.1; ALT_INIT; mRNA.
DR   EMBL; AL606985; CAM15585.1; -; Genomic_DNA.
DR   EMBL; AL606908; CAM15585.1; JOINED; Genomic_DNA.
DR   EMBL; AL606908; CAM19271.1; -; Genomic_DNA.
DR   EMBL; AL606985; CAM19271.1; JOINED; Genomic_DNA.
DR   EMBL; AL606908; CAM19273.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AK148366; BAE28508.1; -; mRNA.
DR   EMBL; BC029670; AAH29670.1; -; mRNA.
DR   EMBL; BC050924; AAH50924.1; -; mRNA.
DR   IPI; IPI00453846; -.
DR   IPI; IPI00625993; -.
DR   RefSeq; NP_001107871.1; NM_001114399.1.
DR   UniGene; Mm.165401; -.
DR   ProteinModelPortal; A2A791; -.
DR   SMR; A2A791; 338-370.
DR   PhosphoSite; A2A791; -.
DR   PRIDE; A2A791; -.
DR   Ensembl; ENSMUST00000030630; ENSMUSP00000030630; ENSMUSG00000042446.
DR   Ensembl; ENSMUST00000106108; ENSMUSP00000101714; ENSMUSG00000042446.
DR   GeneID; 67785; -.
DR   KEGG; mmu:67785; -.
DR   CTD; 67785; -.
DR   MGI; MGI:1915035; Zmym4.
DR   eggNOG; roNOG09773; -.
DR   GeneTree; ENSGT00550000074408; -.
DR   HOGENOM; HBG716329; -.
DR   HOVERGEN; HBG106731; -.
DR   InParanoid; A2A791; -.
DR   OMA; HRDGFPQ; -.
DR   OrthoDB; EOG4KD6KF; -.
DR   PhylomeDB; A2A791; -.
DR   NextBio; 325557; -.
DR   Bgee; A2A791; -.
DR   CleanEx; MM_ZMYM4; -.
DR   Genevestigator; A2A791; -.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR021893; DUF3504.
DR   InterPro; IPR011017; TRASH.
DR   InterPro; IPR010507; Znf_MYM.
DR   Pfam; PF12012; DUF3504; 1.
DR   Pfam; PF06467; zf-FCS; 5.
DR   SMART; SM00746; TRASH; 10.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Metal-binding; Phosphoprotein;
KW   Repeat; Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1549       Zinc finger MYM-type protein 4.
FT                                /FTId=PRO_0000299018.
FT   ZN_FING     362    402       MYM-type 1.
FT   ZN_FING     414    457       MYM-type 2.
FT   ZN_FING     464    499       MYM-type 3.
FT   ZN_FING     510    544       MYM-type 4.
FT   ZN_FING     554    592       MYM-type 5.
FT   ZN_FING     600    631       MYM-type 6.
FT   ZN_FING     708    742       MYM-type 7.
FT   ZN_FING     749    788       MYM-type 8.
FT   ZN_FING     795    829       MYM-type 9.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     121    121       Phosphoserine.
FT   MOD_RES     161    161       Phosphoserine (By similarity).
FT   MOD_RES    1069   1069       Phosphoserine (By similarity).
FT   MOD_RES    1072   1072       Phosphoserine (By similarity).
FT   MOD_RES    1182   1182       Phosphoserine (By similarity).
FT   MOD_RES    1242   1242       Phosphoserine (By similarity).
FT   MOD_RES    1257   1257       Phosphoserine (By similarity).
FT   MOD_RES    1540   1540       Phosphoserine.
FT   MOD_RES    1543   1543       Phosphoserine.
FT   MOD_RES    1548   1548       Phosphoserine.
FT   VAR_SEQ     524    612       Missing (in isoform 2).
FT                                /FTId=VSP_027515.
FT   CONFLICT   1357   1357       M -> V (in Ref. 1; BAC97947).
SQ   SEQUENCE   1549 AA;  172438 MW;  644AF24B4FEB0A62 CRC64;
     MAEREVETGP RKRFEQKSDA VFDEIVENCG VMDTEMSEDT DHNLTPTLAS MSYGMPNQTG
     SENSLLDEDD YFLNSGDLAG IPVVSSDNED EQDCSSKDNL VSSVHTDGSL EVERRAAHQE
     SDNENEIQIQ NQLKKDFPKQ FDQVSVFKSI RKDFCLVREN SKETFSGKEK NRDLTYHERE
     KRLDKPHKGL DSRLKSSFFD KAANQVEETL HTHLPQNPET NFRDSSYPFA SKESIGSELG
     NSFASNIRIK EEPLDDEYDR AVAPQQGLLD RVKDEPDNAQ EYSHGQQQKT QEGELKISAV
     FSVSGSPLAP QLTTGFQPSL ASPGMNKMLP SVPATAVRVS CSGCKKILQK GQTAYQRKGS
     TQLFCSTLCL TGYTVPPARP PPPLTKKTCS SCSKDILNPK DVISAQFENS TTSKDFCSQS
     CLSTYELKKK PIVTINTNSI STKCSMCQKN AVIRHEVNYQ NVVHKLCSDA CFSKFRSANN
     LTMNCCENCG GYCYSGSGQC HVLQIEGQSK KFCSSMCVTS YKQKSAKITP CALCKSLRSS
     AEMIENTNSL GKTELFCSVN CLSAYRVKMV TSAGVQVQCN SCKTSAIPQY HLAMSDGSIR
     NFCSYSCVVA FQNLFNKPTG MNSSVVPLSQ GQVIVSIPTG SSASAGGGST PAVSPTSINS
     SAAAGLQRLA AQSQHVGFAR SVVKLRCQHC NRLFATKPEL LDYKGKMFQF CGKNCCDEYK
     KINNVMAMCE YCKIEKIIKE TVRFSGADKS FCSEGCKLLY KHDLGKRWGS HCKMCSYCLQ
     TSPKLIQNNL GGKVEDFCCE ECMSKYTVLF YQMAKCDGCK RQGKLSESLK WRGDIKHFCN
     LLCILMFCHQ QTVCDPPLQN NAVASISMVQ AASAGPPSLR KDSTPVIANV VSLASAPAAQ
     PTANTNSVLQ GAVPTVTAKI IGDASTQTDA LKLPPSQPPR LLKNKALLCK PITQTKATSC
     KPHTQNKECQ TDTPSEPQVM VVPVPVPVFV PIPLHLYTQY TPVPFGIPVP MPVPMFIPSS
     MDNDEKATEG IEDIKEKLAT HPFEADLLEM AEMIAEDEEK EKTLSQGESQ TSEQELFLDT
     KIFEKDQGST YSGDLESEAV STPHSWEEEL NHYALKSNAV QDADSELKPF SKGETEQDLE
     ADFPSESFDP LNKGQGIQAR SRTRRRHRDG FPQPRRRGRK KSVVPVEPRS LIQGALQGCS
     VSGMTLKYMY GVNAWKNWVQ WKNAKDEQGD LKCGGGELAS ASPCSDSLGS AQDHALSQES
     SEQGCKARSV KLKEDILSCT FSELSLGLCQ FIQEVRRPNG EKYDPDSILY LCLGIQQYLF
     ENGRIDNIFT EPYSRFMIEL TKLLKIWEPT ILPNGYMFSR IEEEHLWECK QLGAYSPIVL
     LNTLLFFNTK YFQLRNVTEH LKLSFAHVMR RTRTLKYSTK MTYLRFFPPL QKPESEPDKV
     TIGKRKRNED DEAPVGVEMA ENTDNPLRCP VRLYEFYLSK CSESVKQRSD VFYLQPERSC
     VPNSPMWYST FPIDPGTLDT MLTRILMVRE VHEELAKAKS EDSDAELSD
//
ID   K1522_MOUSE             Reviewed;        1013 AA.
AC   A2A7S8; A2A7S9; Q3U356; Q3U437; Q3V3N0; Q6ZPN9; Q8K0K8;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 27.
DE   RecName: Full=Uncharacterized protein KIAA1522;
GN   Name=Kiaa1522;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 817-1013.
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-108, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-402; SER-883;
RP   SER-952 AND SER-961, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445; SER-667; SER-838;
RP   SER-842; SER-909 AND SER-959, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667; SER-886 AND
RP   SER-909, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=A2A7S8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2A7S8-2; Sequence=VSP_029460;
CC       Name=3;
CC         IsoId=A2A7S8-3; Sequence=VSP_029459;
CC       Name=4;
CC         IsoId=A2A7S8-4; Sequence=VSP_029461;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98192.1; Type=Erroneous initiation;
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DR   EMBL; AK129382; BAC98192.1; ALT_INIT; mRNA.
DR   EMBL; AK038020; BAE20526.1; -; mRNA.
DR   EMBL; AK154456; BAE32598.1; -; mRNA.
DR   EMBL; AK154932; BAE32933.1; -; mRNA.
DR   EMBL; AL606977; CAM19726.1; -; Genomic_DNA.
DR   EMBL; AL606977; CAM19727.1; -; Genomic_DNA.
DR   EMBL; BC031163; AAH31163.1; -; mRNA.
DR   IPI; IPI00420527; -.
DR   IPI; IPI00650031; -.
DR   IPI; IPI00875022; -.
DR   IPI; IPI00875730; -.
DR   RefSeq; NP_001028361.1; NM_001033189.3.
DR   UniGene; Mm.331907; -.
DR   PhosphoSite; A2A7S8; -.
DR   PRIDE; A2A7S8; -.
DR   Ensembl; ENSMUST00000097873; ENSMUSP00000095483; ENSMUSG00000050390.
DR   Ensembl; ENSMUST00000106051; ENSMUSP00000101666; ENSMUSG00000050390.
DR   GeneID; 97130; -.
DR   KEGG; mmu:97130; -.
DR   CTD; 97130; -.
DR   MGI; MGI:2140651; C77080.
DR   GeneTree; ENSGT00440000038119; -.
DR   HOVERGEN; HBG108037; -.
DR   OMA; AEEPLQD; -.
DR   OrthoDB; EOG4CVG70; -.
DR   Bgee; A2A7S8; -.
DR   CleanEx; MM_C77080; -.
DR   Genevestigator; A2A7S8; -.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1   1013       Uncharacterized protein KIAA1522.
FT                                /FTId=PRO_0000311247.
FT   COMPBIAS    152    158       Poly-Arg.
FT   COMPBIAS    311    429       Ser-rich.
FT   COMPBIAS    436    963       Pro-rich.
FT   MOD_RES     108    108       Phosphotyrosine.
FT   MOD_RES     109    109       Phosphoserine.
FT   MOD_RES     183    183       Phosphothreonine (By similarity).
FT   MOD_RES     213    213       Phosphoserine (By similarity).
FT   MOD_RES     239    239       Phosphotyrosine (By similarity).
FT   MOD_RES     337    337       Phosphoserine (By similarity).
FT   MOD_RES     340    340       Phosphoserine (By similarity).
FT   MOD_RES     402    402       Phosphoserine.
FT   MOD_RES     445    445       Phosphoserine.
FT   MOD_RES     518    518       Phosphoserine (By similarity).
FT   MOD_RES     543    543       Phosphoserine (By similarity).
FT   MOD_RES     571    571       Phosphoserine (By similarity).
FT   MOD_RES     591    591       Phosphothreonine (By similarity).
FT   MOD_RES     667    667       Phosphoserine.
FT   MOD_RES     671    671       Phosphoserine (By similarity).
FT   MOD_RES     838    838       Phosphoserine.
FT   MOD_RES     842    842       Phosphoserine.
FT   MOD_RES     883    883       Phosphoserine.
FT   MOD_RES     886    886       Phosphoserine.
FT   MOD_RES     909    909       Phosphoserine.
FT   MOD_RES     952    952       Phosphoserine.
FT   MOD_RES     959    959       Phosphoserine.
FT   MOD_RES     961    961       Phosphoserine.
FT   VAR_SEQ       1    113       Missing (in isoform 3).
FT                                /FTId=VSP_029459.
FT   VAR_SEQ       1     18       MVVFLGRHLPALLEVFKK -> MAARAPPAAPAADEPGSPG
FT                                GPPRRKKSRSGLRRAFSWLRGKRRKKKAAGAEGAESTASRA
FT                                KKADDKAKRAKGKSR (in isoform 2).
FT                                /FTId=VSP_029460.
FT   VAR_SEQ       1     18       MVVFLGRHLPALLEVFKK -> MGNSHHKRKAPSGPRTRSF
FT                                WRFGRSAKRPA (in isoform 4).
FT                                /FTId=VSP_029461.
FT   CONFLICT    221    221       T -> P (in Ref. 2; BAE20526).
FT   CONFLICT    231    231       I -> L (in Ref. 2; BAE20526).
SQ   SEQUENCE   1013 AA;  104842 MW;  0E7A98C1A1D4382F CRC64;
     MVVFLGRHLP ALLEVFKKGS AKAESDNRQG AGPSQGPGSV GDELQDNVFF PSGRPPHLEE
     LHTQAQEGLR SLQHQERQKL SKGGWDHGDT QSIQSSQTGP DEDTISIYSQ KSYMTESSTA
     EDALSVRSEM IQRRGSTFRP HDSFPKSGKS GRRRRERRST VLGLPQHVQK ELGLRNNREA
     PGTPQPPGSR DAVRIPTVDG RPGLALGTGV RVSLQALEAE TEAGTDAEAV IQRHIDRVYH
     DDTLVGRSTG ARPPPLTRPM SLAVPGLTGG AGSPEPLSPA MSISPQATYL SKLIPHAVLP
     PTVDVVALGR SSLRTLSRCS LLSASPASVR SLGRFSSASS PRPRSRNASS SSDNWSHSQS
     SETIVSDGST LSSKGGSEGQ PEGSVASNNV APPPPGGSGR GSPSGGSTAE TSDTASIRSS
     GQLSGRSVSL RKMKRPPPPP RRTYSLHQRG SAVPDGPLGL PPKPERKQQP QLPRPPTAGG
     SSGVGAVSCP PSSAGTWGSG LSPGGSRRPP RSPERTLSPS SGYSSQSGTP TLPPKGLAVA
     PASPGKAQPP KPDRVTSLRS PGASVSSSLT SLCSSSSDPT PLDRSGPQMS TPLSDRFVIP
     PHPKVPAPFS PPPSKSKSSN QAAPVLAAPA VAPGQVSTID TSPASPSMPQ TTLTPAQESP
     VASKDESPPP SPPPSYHPPP PPTKKPEVLE EAPPPPEAAV EILPDPSWPP PPPPAPEEQD
     LSMADFPPPE EVFFNAGPEL GPLESCSSEA AVPPAASLSQ TPPPAPPPSS GSEPLARLPQ
     KDSVGKHSGA PREDSGTPLV TPSLLQMVRL RSVGASTGIP NPSPGSSAPQ KPLRRALSGR
     ASPVTAPSSG LHAAVRLKAS SLAASESPAS ALPTGIPEAE PRSPQSPASK ASFIFSKGTK
     KLQLERPVSP EAQADLQRNL VAELRSISEH RPPPQAQKKP SKAPPPVARK PSVGVPPPSP
     SLPRTESLTA PSTNGLPHAE DRTNGELAEN GGVQLAATEK MGSPGSDPQK KLV
//
ID   A2A7T0_MOUSE            Unreviewed;       257 AA.
AC   A2A7T0;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-FEB-2011, entry version 19.
DE   SubName: Full=Novel protein (C77080) containing Formin Homology Region 1 domains;
DE   Flags: Fragment;
GN   Name=C77080; Synonyms=RP23-284L6.7; ORFNames=RP23-284L6.7-005;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Clark G.;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL606977; CAM19728.1; -; Genomic_DNA.
DR   IPI; IPI00895020; -.
DR   UniGene; Mm.331907; -.
DR   Ensembl; ENSMUST00000052602; ENSMUSP00000062395; ENSMUSG00000050390.
DR   MGI; MGI:2140651; C77080.
DR   eggNOG; maNOG12766; -.
DR   GeneTree; ENSGT00440000038119; -.
DR   HOGENOM; HBG281823; -.
DR   InParanoid; A2A7T0; -.
DR   Bgee; A2A7T0; -.
DR   Genevestigator; A2A7T0; -.
PE   4: Predicted;
FT   NON_TER     257    257
SQ   SEQUENCE   257 AA;  27843 MW;  BE194EA3BE6D5C65 CRC64;
     MAARAPPAAP AADEPGSPGG PPRRKKSRSG LRRAFSWLRG KRRKKKAAGA EGAESTASRA
     KKADDKAKRA KGKSRGSAKA ESDNRQGAGP SQGPGSVGDE LQDNVFFPSG RPPHLEELHT
     QAQEGLRSLQ HQERQKLSKG GWDHGDTQSI QSSQTGPDED TISIYSQKSY MTESSTAEDA
     LSVRSEMIQR RGSTFRPHDS FPKSGKSGRR RRERRSTVLG LPQHVQKELG LRNNREAPGT
     PQPPGSRDAV RIPTVDG
//
ID   ZEP3_MOUSE              Reviewed;        2348 AA.
AC   A2A884; A2MZW0; Q69ZG6; Q6SNP9;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=Transcription factor HIVEP3;
DE   AltName: Full=Human immunodeficiency virus type I enhancer-binding protein 3 homolog;
DE   AltName: Full=KB-binding and regognition component;
DE   AltName: Full=Kappa-B and V(D)J recombination signal sequences-binding protein;
DE   AltName: Full=Kappa-binding protein 1;
DE            Short=KBP-1;
DE   AltName: Full=Recombinant component;
DE   AltName: Full=Schnurri-3;
DE   AltName: Full=Zinc finger protein ZAS3;
GN   Name=Hivep3; Synonyms=KBP1, Kiaa1555, Krc, Rc, shn3, Zas3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-2341, DOMAIN, FUNCTION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=97001141; PubMed=8812474; DOI=10.1006/geno.1996.0380;
RA   Wu L.-C., Liu Y., Strandtmann J., Mak C.-H., Lee B., Li Z., Yu C.Y.;
RT   "The mouse DNA binding protein Rc for the kappa B motif of
RT   transcription and for the V(D)J recombination signal sequences
RT   contains composite DNA-protein interaction domains and belongs to a
RT   new family of large transcriptional proteins.";
RL   Genomics 35:415-424(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1281-2348.
RC   TISSUE=Thymus;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1497-2295, FUNCTION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, DOMAIN, AND REPEAT.
RX   PubMed=8255760; DOI=10.1093/nar/21.22.5067;
RA   Wu L.-C., Mak C.-H., Dear N., Boehm T., Foroni L., Rabbitts T.H.;
RT   "Molecular cloning of a zinc finger protein which binds to the
RT   heptamer of the signal sequence for V(D)J recombination.";
RL   Nucleic Acids Res. 21:5067-5073(1993).
RN   [5]
RP   PHOSPHORYLATION.
RX   PubMed=9862992; DOI=10.1093/nar/27.2.643;
RA   Bachmeyer C., Mak C.H., Yu C.Y., Wu L.-C.;
RT   "Regulation by phosphorylation of the zinc finger protein KRC that
RT   binds the kappaB motif and V(D)J recombination signal sequences.";
RL   Nucleic Acids Res. 27:643-648(1999).
RN   [6]
RP   FUNCTION.
RX   PubMed=11035930; DOI=10.1006/excr.2000.5029;
RA   Allen C.E., Wu L.-C.;
RT   "Downregulation of KRC induces proliferation, anchorage independence,
RT   and mitotic cell death in HeLa cells.";
RL   Exp. Cell Res. 260:346-356(2000).
RN   [7]
RP   FUNCTION.
RX   PubMed=10625627; DOI=10.1074/jbc.275.2.913;
RA   Hjelmsoe I., Allen C.E., Cohn M.A., Tulchinsky E.M., Wu L.-C.;
RT   "The kappaB and V(D)J recombination signal sequence binding protein
RT   KRC regulates transcription of the mouse metastasis-associated gene
RT   S100A4/mts1.";
RL   J. Biol. Chem. 275:913-920(2000).
RN   [8]
RP   FUNCTION, AND DOMAIN ZAS.
RX   PubMed=12193271; DOI=10.1186/1471-2172-3-10;
RA   Allen C.E., Mak C.-H., Wu L.-C.;
RT   "The kappa B transcriptional enhancer motif and signal sequences of
RT   V(D)J recombination are targets for the zinc finger protein
RT   HIVEP3/KRC: a site selection amplification binding study.";
RL   BMC Immunol. 3:10-10(2002).
RN   [9]
RP   SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH TRAF1 AND TRAF2, AND
RP   REGION.
RX   PubMed=11804591; DOI=10.1016/S1097-2765(01)00434-8;
RA   Oukka M., Kim S.T., Lugo G., Sun J., Wu L.-C., Glimcher L.H.;
RT   "A mammalian homolog of Drosophila schnurri, KRC, regulates TNF
RT   receptor-driven responses and interacts with TRAF2.";
RL   Mol. Cell 9:121-131(2002).
RN   [10]
RP   FUNCTION, INDUCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=12001065; DOI=10.1002/gene.10084;
RA   Hicar M.D., Robinson M.L., Wu L.-C.;
RT   "Embryonic expression and regulation of the large zinc finger protein
RT   KRC.";
RL   Genesis 33:8-20(2002).
RN   [11]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=14530385; DOI=10.1073/pnas.2133048100;
RA   Hong J.W., Allen C.E., Wu L.-C.;
RT   "Inhibition of NF-kappaB by ZAS3, a zinc-finger protein that also
RT   binds to the kappaB motif.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12301-12306(2003).
RN   [12]
RP   FUNCTION, INTERACTION WITH JUN, AND INDUCTION.
RX   PubMed=14707112; DOI=10.1084/jem.20030421;
RA   Oukka M., Wein M.N., Glimcher L.H.;
RT   "Schnurri-3 (KRC) interacts with c-Jun to regulate the IL-2 gene in T
RT   cells.";
RL   J. Exp. Med. 199:15-24(2004).
RN   [13]
RP   ALTERNATIVE PROMOTERS.
RX   PubMed=15627499; DOI=10.1016/j.bbaexp.2004.10.004;
RA   Hong J.-W., Wu L.-C.;
RT   "Structural characterization of the gene encoding the large zinc
RT   finger protein ZAS3: implication to the origin of multiple promoters
RT   in eukaryotic genes.";
RL   Biochim. Biophys. Acta 1681:74-87(2005).
RN   [14]
RP   DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INTERACTION WITH RUNX2
RP   AND WWP1.
RX   PubMed=16728642; DOI=10.1126/science.1126313;
RA   Jones D.C., Wein M.N., Oukka M., Hofstaetter J.G., Glimcher M.J.,
RA   Glimcher L.H.;
RT   "Regulation of adult bone mass by the zinc finger adapter protein
RT   Schnurri-3.";
RL   Science 312:1223-1227(2006).
CC   -!- FUNCTION: Plays a role of transcription factor; binds to
CC       recognition signal sequences (Rss heptamer) for somatic
CC       recombination of immunoglobulin and T-cell receptor gene segments;
CC       Binds also to the kappa-B motif of gene such as S100A4, involved
CC       in cell progression and differentiation. Kappa-B motif is a gene
CC       regulatory element found in promoters and enhancers of genes
CC       involved in immunity, inflammation, and growth and that responds
CC       to viral antigens, mitogens, and cytokines. Involvement of HIVEP3
CC       in cell growth is strengthened by the fact that its down-
CC       regulation promotes cell cycle progression with ultimate formation
CC       of multinucleated giant cells. Strongly inhibits TNF-alpha-induced
CC       NF-kappa-B activation; Interferes with nuclear factor NF-kappa-B
CC       by several mechanisms: as transcription factor, by competing for
CC       Kappa-B motif and by repressing transcription in the nucleus;
CC       Trough non transcriptional process, by inhibiting nuclear
CC       translocation of RELA by association with TRAF2, an adapter
CC       molecule in the tumor necrosis factor signaling, which blocks the
CC       formation of IKK complex. Interaction with TRAF proteins inhibits
CC       both NF-Kappa-B-mediated and c-Jun N-terminal kinase/JNK-mediated
CC       responses that include apoptosis and proinflammatory cytokine gene
CC       expression. Positively regulates the expression of IL2 in T-cell.
CC       Essential regulator of adult bone formation.
CC   -!- SUBUNIT: Interacts with TRAF1 AND TRAF2 as well as with JUN. Forms
CC       a multimeric complex with RUNX2 and E3 ubiquitin ligase WWP1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed in macrophages, lymphocytes, brain,
CC       thymus, spleen and bone marrow. Expressed in osteoblasts, whole
CC       bone and, to a lesser extend, in osteoclasts.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the thymus with increasing
CC       level, approximately 4-fold, from E15.5 to E16.5, constant level
CC       from E16.5 to birth, then decrease to a low level by P30.
CC       Expressed at E13.5 in the dorsal root ganglia of the peripheral
CC       nervous system and the trigeminal ganglion of the metencephalon
CC       and at relatively low levels in the cerebral cortex; no
CC       significant expression was observed prior to E13.5. Expressed in
CC       the spinal cord at E19, but weakly detected in the lung and the
CC       liver.
CC   -!- INDUCTION: Upon CD3/CD28 stimulation in CD4 T-cells. Induced by
CC       LPS in pre-B-cells.
CC   -!- DOMAIN: ZAS2 domain binds DNA as dimers, tetramers, and multiple
CC       of tetramers and readily forms highly ordred DNA-protein
CC       structures.
CC   -!- PTM: Phosphorylated on threonine and serine residues.
CC       Phosphorylation by cyclin-dependent kinase CDK1 decreases HIVEP3
CC       DNA binding affinity, and by epidermal growth factor receptor
CC       kinase increases its DNA binding affinity.
CC   -!- DISRUPTION PHENOTYPE: Mice display adult-onset osteosclerosis with
CC       increased bone mass due to increased osteoblast activity; the
CC       osteoblasts contain elevated levels of Runx2.
CC   -!- MISCELLANEOUS: Hivep3 gene expression is probably controlled by a
CC       combination of differential promoter usage, alternative splicing,
CC       and possible intergenic splicing.
CC   -!- SIMILARITY: Contains 5 C2H2-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA40039.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=AAA40039.1; Type=Frameshift; Positions=1502, 2242;
CC       Sequence=AAR88090.1; Type=Frameshift; Positions=752, 781, 1045, 1054, 2242;
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DR   EMBL; AL607142; CAM27499.1; -; Genomic_DNA.
DR   EMBL; AY454345; AAR88090.1; ALT_FRAME; mRNA.
DR   EMBL; AK173200; BAD32478.1; -; mRNA.
DR   EMBL; L07911; AAA40039.1; ALT_SEQ; mRNA.
DR   IPI; IPI00121314; -.
DR   PIR; S41479; S41479.
DR   PIR; T42717; T42717.
DR   RefSeq; NP_034787.2; NM_010657.3.
DR   UniGene; Mm.302758; -.
DR   UniGene; Mm.394479; -.
DR   UniGene; Mm.422538; -.
DR   ProteinModelPortal; A2A884; -.
DR   SMR; A2A884; 184-240, 1719-1775.
DR   STRING; A2A884; -.
DR   PRIDE; A2A884; -.
DR   Ensembl; ENSMUST00000106307; ENSMUSP00000101914; ENSMUSG00000028634.
DR   GeneID; 16656; -.
DR   KEGG; mmu:16656; -.
DR   CTD; 16656; -.
DR   MGI; MGI:106589; Hivep3.
DR   HOGENOM; HBG283020; -.
DR   HOVERGEN; HBG095595; -.
DR   InParanoid; A2A884; -.
DR   OMA; MERIPGE; -.
DR   OrthoDB; EOG4F7NJ3; -.
DR   NextBio; 290349; -.
DR   Bgee; A2A884; -.
DR   Genevestigator; A2A884; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 4.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW   Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1   2348       Transcription factor HIVEP3.
FT                                /FTId=PRO_0000331628.
FT   REPEAT     1897   1900       1.
FT   REPEAT     1927   1930       2.
FT   REPEAT     1933   1936       3.
FT   REPEAT     1961   1964       4.
FT   REPEAT     2024   2027       5.
FT   ZN_FING     185    207       C2H2-type 1.
FT   ZN_FING     213    235       C2H2-type 2.
FT   ZN_FING     636    658       C2H2-type 3; degenerate.
FT   ZN_FING    1720   1742       C2H2-type 4.
FT   ZN_FING    1748   1772       C2H2-type 5.
FT   REGION      185    235       ZAS1.
FT   REGION      204   1055       No DNA binding activity or
FT                                transactivation activity, but complete
FT                                prevention of TRAF-dependent NF-Kappa-B
FT                                activation; associates with TRAF2 and
FT                                JUN.
FT   REGION      257    280       Acidic 1.
FT   REGION      844    865       Acidic 2.
FT   REGION     1720   1772       ZAS2.
FT   REGION     1783   1841       Acidic 3.
FT   REGION     2053   2148       5 X 4 AA tandem repeats of [ST]-P-X-[RK].
FT   COILED     1409   1433       Potential.
FT   MOTIF       885    891       Nuclear localization signal (Potential).
FT   COMPBIAS    301    327       Ser-rich.
FT   COMPBIAS    371    407       Ser-rich.
FT   COMPBIAS    780    802       Ser-rich.
FT   COMPBIAS    826    862       Glu/Pro-rich.
FT   COMPBIAS    898    930       Ser-rich.
FT   COMPBIAS   1873   1902       Ser-rich.
FT   MOD_RES    2000   2000       Phosphothreonine (By similarity).
FT   CONFLICT    131    131       L -> S (in Ref. 2; AAR88090).
FT   CONFLICT    583    584       QP -> HA (in Ref. 2; AAR88090).
FT   CONFLICT    721    722       GS -> AC (in Ref. 2; AAR88090).
FT   CONFLICT    872    872       S -> T (in Ref. 2; AAR88090).
FT   CONFLICT   1129   1129       E -> Q (in Ref. 2; AAR88090).
FT   CONFLICT   1507   1507       K -> F (in Ref. 4; AAA40039).
FT   CONFLICT   1660   1660       L -> V (in Ref. 2; AAR88090 and 4;
FT                                AAA40039).
FT   CONFLICT   1880   1880       Q -> E (in Ref. 2; AAR88090 and 4;
FT                                AAA40039).
FT   CONFLICT   1944   1944       L -> V (in Ref. 2; AAR88090 and 4;
FT                                AAA40039).
FT   CONFLICT   1994   1994       L -> P (in Ref. 2; AAR88090 and 4;
FT                                AAA40039).
FT   CONFLICT   1998   1998       C -> R (in Ref. 2; AAR88090 and 4;
FT                                AAA40039).
FT   CONFLICT   2014   2014       R -> P (in Ref. 4; AAA40039).
FT   CONFLICT   2105   2105       A -> G (in Ref. 2; AAR88090 and 4;
FT                                AAA40039).
SQ   SEQUENCE   2348 AA;  253413 MW;  E226133774AD50C8 CRC64;
     MDPDQSIKGT KKADGSPRKR LTKGEAIQTS VSSSAPYPGS GTTAPSESAT QELLATQPFS
     GPSQEKTGQQ QKPARRPSIE ASVHISQLPQ HPLTPAFMSP GKPEHLLEGS TWQLVDPMRP
     GPSGSFVAPG LHPQSQLLPS HASILPPEEL PGIPKVFVPR PSQVSLKPAE EAHKKERKPQ
     KPGKYICQYC SRPCAKPSVL QKHIRSHTGE RPYPCGPCGF SFKTKSNLYK HRKSHAHRIK
     AGLASGSSSE MYPPGLEMER IPGEEFEEPT EGESTDSEEE TGAASGPSTD VLPKPKHPLL
     SSSLYSSGSH GSSQERCSLS QSSTGPSLED PAPFAEASSE HPLSHKPEDT HTIKQKLALR
     LSERKKLIEE QTFLSPGSKG STESGYFSRS ESAEQQVSPP NTNAKSYAEI IFGKCGRIGQ
     RTSMLASTST QPLLPLSSED KPSLVPLSVP RTQVIEHITK LITINEAVVD TSEIDSVKPR
     RSSLTRRSSV ESPKSSLYRD SLSSHGEKTK QEQSLLSLQH PPSSTHPVPL LRSHSMPSAA
     CTISTHHHTF RGSYSFDDHV ADPEVPSRNT PVFTSHPRML KRQPAIELPL GGEYSSEEPG
     PSSKDPTSKP SDEPEPKESD LTKKTKKGFK TKGANYECTI CGARYKKRDN YEAHKKYYCS
     ELQITKAHSV GAHEVEKTQA EPEPWSQMMH YKLGATLELT PLRKRRKEKS LGDEEEPPAF
     GSPGPSETAH NRPLGSTKSP AEASKSAPSL EGPTSFQPRT PKPGAGSEPG KERRTMSKEI
     SVIQHTSSFE KSDPPEQPSG LEEDKPPAQF SSPPPAPHGR SAHSLQPRLV RQPNIQVPEI
     LVTEEPDRPD TEPEPPPKEP EKTEEFQWPQ RSQTLAQLPA EKLPPKKKRL RLAEMAQSSG
     ESSFESSVPL SRSPSQESSI SLSGSSRSAS FDREDHGKAE APGPFSDTRS KTLGSHMLTV
     PSHHPHAREM RRSASEQSPN VPHSSHMTET RSKSFDYGSL SPTGPSLAVP AAPPPPAAPP
     ERRKCFLVRQ ASLNRPPEAE LEAVPKGKQE SSEEPAASKP STKSSVPQIS VGTTQGGPSG
     GKSQMQDRPP LGSSPPYTEA LQVFQPLGTQ LPPPASLFSL QQLLPQEQEQ SSEFFPTQAM
     AGLLSSPYSM PPLPPSLFQA PPLPLQPTVL HPSQLHLPQL LPHAADIPFQ QPPSFLPMPC
     PAPSTLSGYF LPLQSQFALQ LPGEIESHLP PVKTSLPPLA TGPPGPSSST EYSSDIQLPP
     VTPQATSPAP TSAPPLALPA CPDAMVSLVV PVRIQTHMPS YGSAMYTTLS QILVTQSPGS
     PASTALTKYE EPSSKSMTVC EADVYEAEPG PSSISKEQNR GYQTPYLRVP ERKGTSLSSE
     GILSLEGCSS TASGSKRVLS PAGSLELTME TQQQKRVKEE EASKADEKLE LVSTCSVVLT
     STEDRKKTEK PHVGGQGRSR REAETLSSLS SDVSDPKELS PLSHSTLSHG TAPGSEALKE
     YAQPSSKAHR RGLPPMSVKK EDPKEQTDLP PLAPPSSLPL SDTSPKPAKL QEGTDSKKVL
     QFPSLHTTTN VSWCYLNYIK PNHIQHADRR SSVYAGWCIS LYNPNLPGVS TKAALSLLRS
     KQKVSKETYT MATAPHPEAG RLVPSNSRKP RMTEVHLPSL VSPESQKDPA RVEKEEKQGK
     AEEGTPTSKR GEPARVKIFE GGYKSNEEYI YVRGRGRGRY VCEECGIRCK KPSMLKKHIR
     THTDVRPYVC KHCHFAFKTK GNLTKHMKSK AHSKKCQETG VLEELEAEEG TSDDLHQDSE
     GQEGAEAVEE HQFSDLEDSD SDSDLDEDEE EEEEEEESQD ELSGPCSEAA PPCLPPTLQE
     NSSPVEGPQA PDSTSDEVPQ GSSISEATHL TASSCSTPSR GTQGLPRLGL APLEKDMSSA
     PSPKATSPRR PWSPSKEAGS RPSLTRKHSL TKNDSSPQQC SPAREAQASV TSTPGPQMGP
     GRDLGPHLCG SPRLELSCLT PYPIGREAPA GLERATDTGT PRYSPTRRWS LGQAESPPQT
     VLPGKWALAG PCSPSADKSG LGLGPVPRAL LQPVPLPHTL LSRSPETCTS AWRKTESRSP
     SAGPAPLFPR PFSAPHDFHG HLPSRSEENL FSHLPLHSQL LSRAPCPLIP IGGIQMVQAR
     PGAQPTVLPG PCAAWVSGFS GGGSDLTGAR EAQERSRWSP TESPSASVSP VAKVSKFTLS
     SELEEERTGR GPGRPPDWEP HRAEAPPGPM GTHSPCSPQL PQGHQVAPSW RGLLGSPHTL
     ANLKASSFPP LDRSSSMDCL AETSTYSPPR SRNLSGEPRT RQGSPELLGR GELRTPLFLP
     KGSGPPSI
//
ID   CMTA1_MOUSE             Reviewed;        1682 AA.
AC   A2A891; A2A892; A2A896; A2A897; A2A898; B2KGR3; B2KGR4; Q80TQ8;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   08-MAR-2011, entry version 36.
DE   RecName: Full=Calmodulin-binding transcription activator 1;
GN   Name=Camta1; Synonyms=Kiaa0833;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 160-1682 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
CC   -!- FUNCTION: Transcriptional activator (By similarity).
CC   -!- SUBUNIT: May interact with calmodulin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=A2A891-1; Sequence=Displayed;
CC         Note=Gene prediction based on EST data;
CC       Name=2;
CC         IsoId=A2A891-2; Sequence=VSP_052990;
CC       Name=3;
CC         IsoId=A2A891-3; Sequence=VSP_052987, VSP_052988;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=A2A891-4; Sequence=VSP_052987, VSP_052988, VSP_052990,
CC                                  VSP_052991;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=A2A891-5; Sequence=VSP_052989, VSP_052990, VSP_052991;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the CAMTA family.
CC   -!- SIMILARITY: Contains 3 ANK repeats.
CC   -!- SIMILARITY: Contains 1 CG-1 DNA-binding domain.
CC   -!- SIMILARITY: Contains 1 IPT/TIG domain.
CC   -!- SIMILARITY: Contains 3 IQ domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM24788.2; Type=Erroneous gene model prediction;
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DR   EMBL; AL606986; CAM18834.1; -; Genomic_DNA.
DR   EMBL; AL606967; CAM18834.1; JOINED; Genomic_DNA.
DR   EMBL; AL607143; CAM18834.1; JOINED; Genomic_DNA.
DR   EMBL; AL611931; CAM18834.1; JOINED; Genomic_DNA.
DR   EMBL; AL732550; CAM18834.1; JOINED; Genomic_DNA.
DR   EMBL; AL606986; CAM18835.1; -; Genomic_DNA.
DR   EMBL; AL606967; CAM18835.1; JOINED; Genomic_DNA.
DR   EMBL; AL607143; CAM18835.1; JOINED; Genomic_DNA.
DR   EMBL; AL611931; CAM18835.1; JOINED; Genomic_DNA.
DR   EMBL; AL732550; CAM18835.1; JOINED; Genomic_DNA.
DR   EMBL; AL606967; CAM20269.1; -; Genomic_DNA.
DR   EMBL; AL606986; CAM20269.1; JOINED; Genomic_DNA.
DR   EMBL; AL607143; CAM20269.1; JOINED; Genomic_DNA.
DR   EMBL; AL611931; CAM20269.1; JOINED; Genomic_DNA.
DR   EMBL; AL732550; CAM20269.1; JOINED; Genomic_DNA.
DR   EMBL; AL606967; CAM20270.1; -; Genomic_DNA.
DR   EMBL; AL606986; CAM20270.1; JOINED; Genomic_DNA.
DR   EMBL; AL607143; CAM20270.1; JOINED; Genomic_DNA.
DR   EMBL; AL611931; CAM20270.1; JOINED; Genomic_DNA.
DR   EMBL; AL732550; CAM20270.1; JOINED; Genomic_DNA.
DR   EMBL; AL732550; CAM24365.1; -; Genomic_DNA.
DR   EMBL; AL606967; CAM24365.1; JOINED; Genomic_DNA.
DR   EMBL; AL606986; CAM24365.1; JOINED; Genomic_DNA.
DR   EMBL; AL607143; CAM24365.1; JOINED; Genomic_DNA.
DR   EMBL; AL611931; CAM24365.1; JOINED; Genomic_DNA.
DR   EMBL; AL732550; CAM24366.1; -; Genomic_DNA.
DR   EMBL; AL606967; CAM24366.1; JOINED; Genomic_DNA.
DR   EMBL; AL606986; CAM24366.1; JOINED; Genomic_DNA.
DR   EMBL; AL607143; CAM24366.1; JOINED; Genomic_DNA.
DR   EMBL; AL611931; CAM24366.1; JOINED; Genomic_DNA.
DR   EMBL; AL607143; CAM24783.1; -; Genomic_DNA.
DR   EMBL; AL606967; CAM24783.1; JOINED; Genomic_DNA.
DR   EMBL; AL606986; CAM24783.1; JOINED; Genomic_DNA.
DR   EMBL; AL611931; CAM24783.1; JOINED; Genomic_DNA.
DR   EMBL; AL732550; CAM24783.1; JOINED; Genomic_DNA.
DR   EMBL; AL607143; CAM24784.1; -; Genomic_DNA.
DR   EMBL; AL606967; CAM24784.1; JOINED; Genomic_DNA.
DR   EMBL; AL606986; CAM24784.1; JOINED; Genomic_DNA.
DR   EMBL; AL611931; CAM24784.1; JOINED; Genomic_DNA.
DR   EMBL; AL732550; CAM24784.1; JOINED; Genomic_DNA.
DR   EMBL; AL607143; CAM24788.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL607143; CAM24789.1; -; Genomic_DNA.
DR   EMBL; AL607143; CAM24790.1; -; Genomic_DNA.
DR   EMBL; AL611931; CAM25054.1; -; Genomic_DNA.
DR   EMBL; AL606967; CAM25054.1; JOINED; Genomic_DNA.
DR   EMBL; AL606986; CAM25054.1; JOINED; Genomic_DNA.
DR   EMBL; AL607143; CAM25054.1; JOINED; Genomic_DNA.
DR   EMBL; AL732550; CAM25054.1; JOINED; Genomic_DNA.
DR   EMBL; AL611931; CAM25055.1; -; Genomic_DNA.
DR   EMBL; AL606967; CAM25055.1; JOINED; Genomic_DNA.
DR   EMBL; AL606986; CAM25055.1; JOINED; Genomic_DNA.
DR   EMBL; AL607143; CAM25055.1; JOINED; Genomic_DNA.
DR   EMBL; AL732550; CAM25055.1; JOINED; Genomic_DNA.
DR   EMBL; CU442759; CAQ51627.1; -; Genomic_DNA.
DR   EMBL; CU207342; CAQ51627.1; JOINED; Genomic_DNA.
DR   EMBL; CU407306; CAQ51627.1; JOINED; Genomic_DNA.
DR   EMBL; CU442759; CAQ51628.1; -; Genomic_DNA.
DR   EMBL; CU207342; CAQ51628.1; JOINED; Genomic_DNA.
DR   EMBL; CU407306; CAQ51628.1; JOINED; Genomic_DNA.
DR   EMBL; CU407306; CAQ51883.1; -; Genomic_DNA.
DR   EMBL; CU207342; CAQ51883.1; JOINED; Genomic_DNA.
DR   EMBL; CU442759; CAQ51883.1; JOINED; Genomic_DNA.
DR   EMBL; CU407306; CAQ51884.1; -; Genomic_DNA.
DR   EMBL; CU207342; CAQ51884.1; JOINED; Genomic_DNA.
DR   EMBL; CU442759; CAQ51884.1; JOINED; Genomic_DNA.
DR   EMBL; AK122383; BAC65665.1; -; mRNA.
DR   IPI; IPI00284435; -.
DR   IPI; IPI00378693; -.
DR   IPI; IPI00648671; -.
DR   IPI; IPI00831530; -.
DR   IPI; IPI00972897; -.
DR   RefSeq; NP_001075026.1; NM_001081557.3.
DR   UniGene; Mm.318846; -.
DR   ProteinModelPortal; A2A891; -.
DR   SMR; A2A891; 874-956, 1061-1166, 1547-1619.
DR   STRING; A2A891; -.
DR   PhosphoSite; A2A891; -.
DR   PRIDE; A2A891; -.
DR   Ensembl; ENSMUST00000049790; ENSMUSP00000054804; ENSMUSG00000014592.
DR   GeneID; 100072; -.
DR   KEGG; mmu:100072; -.
DR   CTD; 100072; -.
DR   MGI; MGI:2140230; Camta1.
DR   HOVERGEN; HBG080107; -.
DR   InParanoid; A2A891; -.
DR   OMA; RTHNCLC; -.
DR   OrthoDB; EOG4CC40F; -.
DR   NextBio; 354243; -.
DR   Bgee; A2A891; -.
DR   Genevestigator; A2A891; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR   GO; GO:0030528; F:transcription regulator activity; IEA:InterPro.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR005559; CG-1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002909; IPT_TIG_rcpt.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF03859; CG-1; 1.
DR   Pfam; PF00612; IQ; 1.
DR   Pfam; PF01833; TIG; 1.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00015; IQ; 2.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF81296; Ig_E-set; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS51437; CG_1; 1.
DR   PROSITE; PS50096; IQ; 1.
PE   2: Evidence at transcript level;
KW   Activator; Alternative splicing; ANK repeat; Cytoplasm; Nucleus;
KW   Phosphoprotein; Repeat; Transcription; Transcription regulation.
FT   CHAIN         1   1682       Calmodulin-binding transcription
FT                                activator 1.
FT                                /FTId=PRO_0000355043.
FT   DOMAIN      875    955       IPT/TIG.
FT   REPEAT     1066   1095       ANK 1.
FT   REPEAT     1111   1141       ANK 2.
FT   REPEAT     1145   1174       ANK 3.
FT   DOMAIN     1549   1585       IQ 1.
FT   DOMAIN     1586   1608       IQ 2.
FT   DOMAIN     1609   1631       IQ 3.
FT   DNA_BIND     63    188       CG-1.
FT   MOTIF       112    119       Nuclear localization signal (By
FT                                similarity).
FT   COMPBIAS   1006   1033       Gly-rich.
FT   MOD_RES     117    117       Phosphotyrosine (By similarity).
FT   VAR_SEQ       1    978       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_052987.
FT   VAR_SEQ    1222   1334       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_052988.
FT   VAR_SEQ    1459   1472       Missing (in isoform 5).
FT                                /FTId=VSP_052989.
FT   VAR_SEQ    1566   1572       Missing (in isoform 2, isoform 4 and
FT                                isoform 5).
FT                                /FTId=VSP_052990.
FT   VAR_SEQ    1662   1682       SPLVDHRLYKRSERIEKGQGT -> RVKELKKAKELEDIQQ
FT                                HPLAM (in isoform 4 and isoform 5).
FT                                /FTId=VSP_052991.
FT   CONFLICT   1394   1394       D -> G (in Ref. 1; CAQ51627/CAQ51628/
FT                                CAQ51883/CAQ51884).
FT   CONFLICT   1482   1482       S -> N (in Ref. 1; CAQ51627/CAQ51628/
FT                                CAQ51883/CAQ51884).
SQ   SEQUENCE   1682 AA;  184319 MW;  3F96253C6CF119C6 CRC64;
     MWRAEGKWLP KTSRKSVSQS VFCGTSTYCV LNTVPPIEDD HGNSNSSHVK IFLPKKLLEC
     LPKCSSLPKE RHRWNTNEEI AAYLITFEKH EEWLTTSPKT RPQNGSMILY NRKKVKYRKD
     GYCWKKRKDG KTTREDHMKL KVQGVECLYG CYVHSSIIPT FHRRCYWLLQ NPDIVLVHYL
     NVPAIEDCGK PCGPILCSIN TDKKEWAKWT KEELIGQLKP MFHGIKWTCS NGNSSSGFSV
     EQLVQQILDS HQTKPQPRTH NCLCTGSLGA GSSVHHKCNS AKHRIISPKV EPRAGGYGGH
     SEVQHNDVSE GKHEPSHGRS TSREKRNGKV AKPALLHQNS TEVSSTNQVE VPDTTQSSPV
     SISSGLNSDP DMVDSPVVTG VSSMAVASVM GGLSQSATVF MSEVTNEAVY TMSPTAGPNH
     HLLSPDASQG LVLAVSSDGH KFAFPTTGSS DSLSMLPANV SEELVLSTTL DGGRKIPETA
     MNFDPDCFLN NPKQGQTYGG GGLKAEMVST NIRHSPPAER SFGFTSVLTK EIKTEDTSFE
     QQMAKEAAYS SSAAAAASSS LTLTAAGSSL LPSGGGLSPS TTLEQMDFSA IDSNKDYASS
     FSQTGHSPHI HQTPSPSFFL QDASKPLPLE QNTHSSLSES GAAFVMPTVK TEASSQTSSC
     SGHVETRIES TSSLHLMQFQ ANFQAMAAEG EVTMETSQAA EGNEVLLKSG ELQACGSEHY
     LQPETNGVIR SAGGVPLLPS NVVQGLYPVA QPSLGNSSNM ELSLDHFDIS FSNQFSDLIN
     DFISVEGGSG TIYGHQLVSG DSAALSQSED GARAPFTQAE MCIPCCSPQQ GSLQLSSAEG
     GPSTMAYMHV AEVVSAASAQ GALGMLQQSG RVFMVTDYSP EWSYPEGGVK VLITGPWQEA
     SNNYSCLFDQ ISVPASLIQP GVLRCYCPAH DTGLVTLQVA FNNQIISNSV VFEYKARALP
     TLPSSQHDWL SLDDNQFRMS ILERLEQMER RMAEMTGSQQ HKQASGGGGS GSGSGSGAGG
     GQAQCASGAG TLGSCFESRV VVVCEKMMSR ACWAKSKHLI HSKTFRGMTL LHLAAAQGYA
     TLIQTLIKWR TKHADSIDLE LEVDPLNVDH FSCTPLMWAC ALGHLEAAVV LYKWDRRAIS
     IPDSLGRLPL GIARSRGHVK LAECLEHLQR DEQAQLGQAS RIHCAPSEEP TTDSWMAQWQ
     REAMSPPEIP KGVTVIASTN PELRRPRSEP SNYYSTEGHK DYPAPKKHKL NPESFQARQE
     KLLCTALSLE QPNIRKQSPR SKQPSPETIS PSEGVREYSR EAAPPTPETA ASQASASQPV
     VKWSAKDLYI GVSTVQVTGN PKGTSVVKDA APSQVRPREP MSVLMLANRE VVNTEMGAYR
     DRTEHEDCPQ PMDDIQVNMM TLAEHIIEAT PDRIKQENFV PMESSALERT DPATISSTMS
     WLASYLADAD RLPSAAHIRS AYTEPLTPSS NASLSPAGSP VSEVAFEKPS LPSAADWSEF
     LSASTSEKVE SELAQLTLSD HEQRELYEAA RLVQTAFRKY KGRPLREQQE VAAAVIQRCY
     RKYKQLTWIA LKYALYKKMT QAAILIQSKF RSYYEQKRFQ QSRRAAVLIQ NFYRSYKKCG
     RRRPARRTAV IVQQKLRSSL LTKKQDQAAR KIMRFLRRCR HSPLVDHRLY KRSERIEKGQ
     GT
//
ID   A2A8L1_MOUSE            Unreviewed;      1946 AA.
AC   A2A8L1;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   SubName: Full=Chromodomain helicase DNA binding protein 5;
GN   Name=Chd5; ORFNames=RP23-421E12.10-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Holt K.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL611985; CAM23902.1; -; Genomic_DNA.
DR   IPI; IPI00608001; -.
DR   UniGene; Mm.40192; -.
DR   ProteinModelPortal; A2A8L1; -.
DR   SMR; A2A8L1; 343-470, 590-646.
DR   PRIDE; A2A8L1; -.
DR   Ensembl; ENSMUST00000005175; ENSMUSP00000005175; ENSMUSG00000005045.
DR   MGI; MGI:3036258; Chd5.
DR   HOVERGEN; HBG005326; -.
DR   OrthoDB; EOG4WH8JX; -.
DR   PhylomeDB; A2A8L1; -.
DR   Bgee; A2A8L1; -.
DR   Genevestigator; A2A8L1; -.
DR   GO; GO:0000785; C:chromatin; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006333; P:chromatin assembly or disassembly; IEA:InterPro.
DR   GO; GO:0045449; P:regulation of transcription; IEA:InterPro.
DR   InterPro; IPR012957; CHD_C2.
DR   InterPro; IPR012958; CHD_N.
DR   InterPro; IPR000953; Chromodomain.
DR   InterPro; IPR016197; Chromodomain-like.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR009462; DUF1086.
DR   InterPro; IPR009463; DUF1087.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 2.
DR   Pfam; PF08074; CHDCT2; 1.
DR   Pfam; PF08073; CHDNT; 1.
DR   Pfam; PF00385; Chromo; 2.
DR   Pfam; PF06461; DUF1086; 1.
DR   Pfam; PF06465; DUF1087; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00628; PHD; 2.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00249; PHD; 2.
DR   SMART; SM00184; RING; 2.
DR   SUPFAM; SSF54160; Chromodomain-like; 2.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 2.
DR   PROSITE; PS50013; CHROMO_2; 2.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 2.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   4: Predicted;
KW   ATP-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding;
KW   Nucleus; Zinc.
SQ   SEQUENCE   1946 AA;  222515 MW;  5B94AB11A9C9BB03 CRC64;
     MRGPLGTEEE LPRLFAEEME NEEEMSEEED GGLEGFEDFF PAEPVSLPKK KPKKLKESKS
     SKGKRKKKEG SNDEMSDNEE DLEEKSESEG SDYSPTKKKK KKLKEKKEKK EKKEKRKKRG
     EDEDDNDDGG LKEPKSSGQL MAEWGLDDVD YLFSEDDYHT LTNYKAFSQF LRPLIAKKNP
     KIPMSKMMTV LGAKWREFSA NNPFKGSSAA AAAAAVAAAV ETVTIAPPLA ISPQQVPQTL
     PIRKAKTKEG KGPGVRKKNK GAKDSKKKGR GKRVAGLKFR FGGISKRKKG SSSEEDERED
     SDLDNASIHS SSVRSECSAA LGKKNKRRRK KKRIDDGDGY ETDHQDYCEV CQQGGEIILC
     DTCPRAYHLV CLDPELEKAP EGKWSCPHCE KEGIQWEPKD DDEEEEEGGC EEEEDDHMEF
     CRVCKDGGEL LCCDACPSSY HLHCLNPPLP EIPNGEWLCP RCTCPPLKGK VQRILHWRWT
     EPPAPFVVGL PGPEVEPGMP PPRPLEGIPE REFFVKWAGL SYWHCSWVKE LQLELYHTVM
     YRNYQRKNDM DEPPPFDYGS GDEDGKSEKR KNKDPLYAKM EERFYRYGIK PEWMMVHRIL
     NHSFDKKGDI HYLIKWKDLP YDQCTWEIDE IDIPYYDNLK QAYWGHRELM LGEDARLPKR
     LVKKGKKLKD DKQEKPPDTP IVDPTVKFDK QPWYIDATGG TLHPYQLEGL NWLRFSWAQG
     TDTILADEMG LGKTVQTIVF LYSLYKEGHS KGPYLVSAPL STIINWEREF EMWAPDFYVV
     TYTGDKESRS VIRENEFSFE DNAIRGGKKV FRMKKEVQIK FHVLLTSYEL ITIDQAILGS
     IEWACLVVDE AHRLKNNQSK FFRVLNSYKI DYKLLLTGTP LQNNLEELFH LLNFLTPERF
     NNLEGFLEEF ADISKEDQIK KLHDLLGPHM LRRLKADVFK NMPAKTELIV RVELSQMQKK
     YYKFILTRNF EALNSKGGGN QVSLLNIMMD LKKCCNHPYL FPVAAVEAPV LPNGSYDGSS
     LVKSSGKLML LQKMLKKLRD EGHRVLIFSQ MTKMLDLLED FLEYEGYKYE RIDGGITGGL
     RQEAIDRFNA PGAQQFCFLL STRAGGLGIN LATADTVIIY DSDWNPHNDI QAFSRAHRIG
     QNKKVMIYRF VTRASVEERI TQVAKRKMML THLVVRPGLG SKSGSMTKQE LDDILKFGTE
     ELFKDDVEGM MSQGQRPTTP IPDIQSTKGG SLTAGAKKKH GSTPPGDNKD VEDSSVIHYD
     DAAISKLLDR NQDATDDTEL QNMNEYLSSF KVAQYVVREE DGVEEVEREV IKQEENVDPD
     YWEKLLRHHY EQQQEDLARN LGKGKRIRKQ VNYNDASQED QEWQDELSDN QSEYSIGSED
     EDEDFEERPE GQSGRRQSRR QLKSDRDKPL PPLLARVGGN IEVLGFNARQ RKAFLNAIMR
     WGMPPQDAFN SHWLVRDLRG KSEKEFRAYV SLFMRHLCEP GADGAETFAD GVPREGLSRQ
     HVLTRIGVMS LVRKKVQEFE HVNGKYSTPD LVPEGAEGKK PGEVISSDPN TPVPASPAQL
     PPAPLGLTDK MEAQLGYTDE KESGMQKPKK SLEIQTLPTA LDRVEGEDKH QSSDSKDRAR
     EERTEEVEKA QGSPEQPLKE EVLPDKEPIP DKPELSLGHS GDFRPDDPKT EEKEPGETQQ
     NGDREEDEEG KKEDKNGKFK FMFNIADGGF TELHTLWQNE ERAAVSSGKI YEIWHRRHDY
     WLLAGIVTHG YARWQDIQND PRYMILNEPF KSEIHKGNYL EMKNKFLARR FKLLEQALVI
     EEQLRRAAYL NMTQDPNHPA MALNARLAEV ECLAESHQHL SKESLAGNKP ANAVLHKVLN
     QLEELLSDMK ADVTRLPSML SRIPPVAARL QMSERSILSR LTNRAGDPTI QQTSSRRRDF
     PLFQRSFPAE PSHLPNPRGR EKLQPF
//
ID   PTPRF_MOUSE             Reviewed;        1898 AA.
AC   A2A8L5; Q6PG86; Q9EQ17;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=Receptor-type tyrosine-protein phosphatase F;
DE            EC=3.1.3.48;
DE   AltName: Full=Leukocyte common antigen related;
DE            Short=LAR;
DE   Flags: Precursor;
GN   Name=Ptprf; Synonyms=Lar;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Thymus;
RX   MEDLINE=21135493; PubMed=11241288;
RX   DOI=10.1002/1521-4141(200103)31:3<832::AID-IMMU832>3.0.CO;2-D;
RA   Terszowski G., Jankowski A., Hendriks W.J.A.J., Rolink A.G.,
RA   Kisielow P.;
RT   "Within the hemopoietic system, LAR phosphatase is a T cell lineage-
RT   specific adhesion receptor-like protein whose phosphatase activity
RT   appears dispensable for T cell development, repertoire selection and
RT   function.";
RL   Eur. J. Immunol. 31:832-840(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 370-1898.
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-721; ASN-936; ASN-941 AND
RP   ASN-960, AND MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Possible cell adhesion receptor. It possesses an
CC       intrinsic protein tyrosine phosphatase activity (PTPase) (By
CC       similarity).
CC   -!- FUNCTION: The first PTPase domain has enzymatic activity, while
CC       the second one seems to affect the substrate specificity of the
CC       first one (By similarity).
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- SUBUNIT: Interacts with GRIP1 (By similarity). Interacts with
CC       PPFIA1, PPFIA2 and PPFIA3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- TISSUE SPECIFICITY: Expressed in the cell of the T lineage but not
CC       in cells of any other hemopoietic lineage.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 2A subfamily.
CC   -!- SIMILARITY: Contains 8 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 3 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SIMILARITY: Contains 2 tyrosine-protein phosphatase domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF300943; AAG40194.1; -; mRNA.
DR   EMBL; AL807774; CAM17264.1; -; Genomic_DNA.
DR   EMBL; AL626764; CAM17264.1; JOINED; Genomic_DNA.
DR   EMBL; AL626764; CAM27382.1; -; Genomic_DNA.
DR   EMBL; AL807774; CAM27382.1; JOINED; Genomic_DNA.
DR   EMBL; BC057166; AAH57166.1; -; mRNA.
DR   IPI; IPI00110264; -.
DR   RefSeq; NP_035343.2; NM_011213.2.
DR   UniGene; Mm.29855; -.
DR   ProteinModelPortal; A2A8L5; -.
DR   SMR; A2A8L5; 29-1083, 1325-1893.
DR   STRING; A2A8L5; -.
DR   PRIDE; A2A8L5; -.
DR   Ensembl; ENSMUST00000049074; ENSMUSP00000039368; ENSMUSG00000033295.
DR   GeneID; 19268; -.
DR   KEGG; mmu:19268; -.
DR   NMPDR; fig|10090.3.peg.10217; -.
DR   CTD; 19268; -.
DR   MGI; MGI:102695; Ptprf.
DR   eggNOG; roNOG04678; -.
DR   HOGENOM; HBG390264; -.
DR   InParanoid; A2A8L5; -.
DR   OMA; FTPTIEA; -.
DR   OrthoDB; EOG4BG8V3; -.
DR   PhylomeDB; A2A8L5; -.
DR   NextBio; 296150; -.
DR   Bgee; A2A8L5; -.
DR   Genevestigator; A2A8L5; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 11.
DR   Pfam; PF00041; fn3; 7.
DR   Pfam; PF07679; I-set; 3.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 8.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 2.
DR   SMART; SM00194; PTPc; 2.
DR   SUPFAM; SSF49265; FN_III-like; 8.
DR   PROSITE; PS50853; FN3; 8.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   1: Evidence at protein level;
KW   Cell adhesion; Disulfide bond; Glycoprotein; Hydrolase;
KW   Immunoglobulin domain; Membrane; Protein phosphatase; Receptor;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     29       Potential.
FT   CHAIN        30   1898       Receptor-type tyrosine-protein
FT                                phosphatase F.
FT                                /FTId=PRO_0000370193.
FT   TOPO_DOM     30   1254       Extracellular (Potential).
FT   TRANSMEM   1255   1275       Helical; (Potential).
FT   TOPO_DOM   1276   1898       Cytoplasmic (Potential).
FT   DOMAIN       33    123       Ig-like C2-type 1.
FT   DOMAIN      135    224       Ig-like C2-type 2.
FT   DOMAIN      232    314       Ig-like C2-type 3.
FT   DOMAIN      319    407       Fibronectin type-III 1.
FT   DOMAIN      413    506       Fibronectin type-III 2.
FT   DOMAIN      512    602       Fibronectin type-III 3.
FT   DOMAIN      606    703       Fibronectin type-III 4.
FT   DOMAIN      708    806       Fibronectin type-III 5.
FT   DOMAIN      808    901       Fibronectin type-III 6.
FT   DOMAIN      906    999       Fibronectin type-III 7.
FT   DOMAIN     1002   1086       Fibronectin type-III 8.
FT   DOMAIN     1343   1598       Tyrosine-protein phosphatase 1.
FT   DOMAIN     1630   1889       Tyrosine-protein phosphatase 2.
FT   REGION     1539   1545       Substrate binding (By similarity).
FT   ACT_SITE   1539   1539       Phosphocysteine intermediate (By
FT                                similarity).
FT   ACT_SITE   1830   1830       Phosphocysteine intermediate (By
FT                                similarity).
FT   BINDING    1507   1507       Substrate (By similarity).
FT   BINDING    1583   1583       Substrate (By similarity).
FT   CARBOHYD    117    117       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    250    250       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    295    295       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    721    721       N-linked (GlcNAc...).
FT   CARBOHYD    936    936       N-linked (GlcNAc...).
FT   CARBOHYD    941    941       N-linked (GlcNAc...).
FT   CARBOHYD    957    957       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    960    960       N-linked (GlcNAc...).
FT   DISULFID     54    107       By similarity.
FT   DISULFID    156    207       By similarity.
FT   DISULFID    253    298       By similarity.
FT   CONFLICT     47     47       G -> E (in Ref. 1; AAG40194).
FT   CONFLICT    482    482       I -> V (in Ref. 1; AAG40194).
FT   CONFLICT    514    515       QP -> RS (in Ref. 1; AAG40194).
FT   CONFLICT    579    579       H -> R (in Ref. 1; AAG40194).
FT   CONFLICT   1006   1006       A -> T (in Ref. 1; AAG40194).
FT   CONFLICT   1184   1184       V -> A (in Ref. 3; AAH57166).
FT   CONFLICT   1374   1374       N -> D (in Ref. 1; AAG40194).
SQ   SEQUENCE   1898 AA;  211489 MW;  903FF6814F0BC914 CRC64;
     MAPEPAPGRR MVPLVPALVM LGLMAGAHGD SKPVFVKVPE DQTGLSGGVA SFVCQATGEP
     KPRITWMKKG KKVSSQRFEV IEFDDGAGSV LRIQPLRVQR DEAIYECTAT NSLGEINTSA
     KLSVLEEDQL PSGFPTIDMG PQLKVVEKGR TATMLCAAGG NPDPEISWFK DFLPVDPAAS
     NGRIKQLRSG ALQIESSEES DQGKYECVAT NSAGTRYSAP ANLYVRVRRV APRFSIPPSS
     QEVMPGGSVN LTCVAVGAPM PYVKWMMGAE ELTKEDEMPV GRNVLELSNV MRSANYTCVA
     ISSLGMIEAT AQVTVKALPK PPIDLVVTET TATSVTLTWD SGNTEPVSFY GIQYRAAGTD
     GPFQEVDGVA STRYSIGGLS PFSEYAFRVL AVNSIGRGPP SEAVRARTGE QAPSSPPRRV
     QARMLSASTM LVQWEPPEEP NGLVRGYRVY YTPDSRRPLS AWHKHNTDAG LLTTVGSLLP
     GITYSLRVLA FTAVGDGPPS PTIQVKTQQG VPAQPADFQA NAESDTRIQL SWLLPPQERI
     VKYELVYWAA EDEGQQHKVT FDPTSSYTLE DLKPDTLYHF QLAARSDLGV GVFTPTVEAR
     TAQSTPSAPP QKVTCVSTGS TTVRVSWVPP PADSRNGIIT QYSVAYEAVD GEDRKRHVVD
     GISREHSSWD LLGLEKWTEY RVWVRAHTDV GPGPESSPVL VRTDEDVPSG PPRKVEVEPL
     NSTAVHVSWK LPVPNKQHGQ IRGYQVTYVR LENGEPRGQP IIQDVMLAEA QETTISGLTP
     ETTYSITVAA YTTKGDGARS KPKVVTTTGA VPGRPTMMVS TTAMHTALLQ WHPPKELPGE
     LLGYRLQYRR ADEARPNTID FGKDDQHFTV TGLHKGATYV FRLAAKNRAG PGEEFEKEIT
     TPEDVPSGFP QNLRVTGLTT STTELTWDPP VLAERNGHIT NYTVVYRDIN SQLELQNVTN
     DTHLTLLGLK PDTTYDIKVR AHTSKGAGPL SPSIQSRTMP VEQVFAKNFR VAAAMKTSVL
     LSWEVPDSYK SAVPFKILYN GQSVEVDGHS MRKLIADLQP NTEYSFVLMN RGSSAGGLQH
     LVSIRTAPDL LPQKPLPASA FIEDGRFSLS MPQVQDPSLV RWFYIVVVPI DRVGGNLLAP
     RWNTPEELEL DELLEAIEQG EEKQRRRRRQ AERLKPYVAA QVDVLPDTFT LGDKKSYRGF
     YNRPLSPDLS YQCFVLASLK EPMDQKRYAS SPYSDEIVVQ VTPAQQQEEP EMLWVTGPVL
     AVILIILIVI AILLFKRKRT HSPSSKDEQS IGLKDSLLAH SSDPVEMRRL NYQTPGMRDH
     PPIPITDLAD NIERLKANDG LKFSQEYESI DPGQQFTWEN SNSEVNKPKN RYANVIAYDH
     SRVLLTSIDG VPGSDYINAN YIDGYRKQNA YIATQGPLPE TMGDFWRMVW EQRTATVVMM
     TRLEEKSRVK CDQYWPVRGT ETYGLIQVTL VDTVELATYT MRTFALHKSG SSEKRELRQF
     QFMAWPDHGV PEYPTPILAF LRRVKACNPL DAGPMVVHCS AGVGRTGCFI VIDAMLERMK
     HEKTVDIYGH VTCMRSQRNY MVQTEDQYVF IHEALLEAAM CGHTEVLARN LYAHIQKLGQ
     VPPGESVTAM ELEFKLLANS KAHTSRFVSA NLPCNKFKNR LVNIMPYELT RVCLQPIRGV
     EGSDYINASF LDGYRQQKAY IATQGPLAES TEDFWRMLWE HNSTIIVMLT KLREMGREKC
     HQYWPAERSA RYQYFVVDPM AEYNMPQYIL REFKVTDARD GQSRTIRQFQ FTDWPEQGVP
     KTGEGFIDFI GQVHKTKEQF GQDGPITVHC SAGVGRTGVF ITLSIVLERM RYEGVVDMFQ
     TVKTLRTQRP AMVQTEDQYQ LCYRAALEYL GSFDHYAT
//
ID   A2A8M1_MOUSE            Unreviewed;      1331 AA.
AC   A2A8M1;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 35.
DE   SubName: Full=Protein tyrosine phosphatase, receptor type, F;
DE   Flags: Fragment;
GN   Name=Ptprf; ORFNames=RP23-94L18.2-003;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Brown J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AL626764; CAM27388.1; -; Genomic_DNA.
DR   IPI; IPI00648298; -.
DR   UniGene; Mm.29855; -.
DR   ProteinModelPortal; A2A8M1; -.
DR   STRING; A2A8M1; -.
DR   Ensembl; ENSMUST00000106394; ENSMUSP00000102002; ENSMUSG00000033295.
DR   Ensembl; ENSMUST00000124758; ENSMUSP00000119954; ENSMUSG00000033295.
DR   MGI; MGI:102695; Ptprf.
DR   HOVERGEN; HBG053758; -.
DR   PhylomeDB; A2A8M1; -.
DR   Bgee; A2A8M1; -.
DR   Genevestigator; A2A8M1; -.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 6.
DR   Pfam; PF00041; fn3; 4.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 5.
DR   SMART; SM00194; PTPc; 2.
DR   SUPFAM; SSF49265; FN_III-like; 5.
DR   PROSITE; PS50853; FN3; 6.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   4: Predicted;
KW   Hydrolase; Protein phosphatase; Receptor.
FT   NON_TER       1      1
SQ   SEQUENCE   1331 AA;  150105 MW;  632037BE4DFF873A CRC64;
     SLLPGITYSL RVLAFTAVGD GPPSPTIQVK TQQGVPAQPA DFQANAESDT RIQLSWLLPP
     QERIVKYELV YWAAEDEGQQ HKVTFDPTSS YTLEDLKPDT LYHFQLAARS DLGVGVFTPT
     VEARTAQSMP SGPPRKVEVE PLNSTAVHVS WKLPVPNKQH GQIRGYQVTY VRLENGEPRG
     QPIIQDVMLA EAQETTISGL TPETTYSITV AAYTTKGDGA RSKPKVVTTT GAVPGRPTMM
     VSTTAMHTAL LQWHPPKELP GELLGYRLQY RRADEARPNT IDFGKDDQHF TVTGLHKGAT
     YVFRLAAKNR AGPGEEFEKE ITTPEDVPSG FPQNLRVTGL TTSTTELTWD PPVLAERNGH
     ITNYTVVYRD INSQLELQNV TNDTHLTLLG LKPDTTYDIK VRAHTSKGAG PLSPSIQSRT
     MPVEQVFAKN FRVAAAMKTS VLLSWEVPDS YKSAVPFKIL YNGQSVEVDG HSMRKLIADL
     QPNTEYSFVL MNRGSSAGGL QHLVSIRTAP DLLPQKPLPA SAFIEDGRFS LSMPQVQDPS
     LVRWFYIVVV PIDRVGGNLL APRWNTPEEL ELDELLEAIE QGEEKQRRRR RQAERLKPYV
     AAQVDVLPDT FTLGDKKSYR GFYNRPLSPD LSYQCFVLAS LKEPMDQKRY ASSPYSDEIV
     VQVTPAQQQE EPEMLWVTGP VLAVILIILI VIAILLFKRK RTHSPSSKDE QSIGLKDSLL
     AHSSDPVEMR RLNYQTPGSS APSCPNISSM RDHPPIPITD LADNIERLKA NDGLKFSQEY
     ESIDPGQQFT WENSNSEVNK PKNRYANVIA YDHSRVLLTS IDGVPGSDYI NANYIDGYRK
     QNAYIATQGP LPETMGDFWR MVWEQRTATV VMMTRLEEKS RVKCDQYWPV RGTETYGLIQ
     VTLVDTVELA TYTMRTFALH KSGSSEKREL RQFQFMAWPD HGVPEYPTPI LAFLRRVKAC
     NPLDAGPMVV HCSAGVGRTG CFIVIDAMLE RMKHEKTVDI YGHVTCMRSQ RNYMVQTEDQ
     YVFIHEALLE AAMCGHTEVL ARNLYAHIQK LGQVPPGESV TAMELEFKLL ANSKAHTSRF
     VSANLPCNKF KNRLVNIMPY ELTRVCLQPI RGVEGSDYIN ASFLDGYRQQ KAYIATQGPL
     AESTEDFWRM LWEHNSTIIV MLTKLREMGR EKCHQYWPAE RSARYQYFVV DPMAEYNMPQ
     YILREFKVTD ARDGQSRTIR QFQFTDWPEQ GVPKTGEGFI DFIGQVHKTK EQFGQDGPIT
     VHCSAGVGRT GVFITLSIVL ERMRYEGVVD MFQTVKTLRT QRPAMVQTED QYQLCYRAAL
     EYLGSFDHYA T
//
ID   A2A8R0_MOUSE            Unreviewed;      1397 AA.
AC   A2A8R0;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 35.
DE   SubName: Full=MCG17975;
DE   SubName: Full=Zinc finger, FYVE domain containing 9;
GN   Name=Zfyve9; ORFNames=RP23-406B13.8-001, mCG_17975;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Griffiths C.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RA   Brown J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL626783; CAM23498.1; -; Genomic_DNA.
DR   EMBL; AL671909; CAM23498.1; JOINED; Genomic_DNA.
DR   EMBL; AL671909; CAM24599.1; -; Genomic_DNA.
DR   EMBL; AL626783; CAM24599.1; JOINED; Genomic_DNA.
DR   EMBL; CH466527; EDL30733.1; -; Genomic_DNA.
DR   IPI; IPI00136258; -.
DR   UniGene; Mm.196776; -.
DR   ProteinModelPortal; A2A8R0; -.
DR   SMR; A2A8R0; 612-734, 743-783.
DR   STRING; A2A8R0; -.
DR   PRIDE; A2A8R0; -.
DR   Ensembl; ENSMUST00000106657; ENSMUSP00000102268; ENSMUSG00000034557.
DR   Ensembl; ENSMUST00000106660; ENSMUSP00000102271; ENSMUSG00000034557.
DR   MGI; MGI:2652838; Zfyve9.
DR   HOGENOM; HBG283005; -.
DR   HOVERGEN; HBG079085; -.
DR   InParanoid; A2A8R0; -.
DR   OMA; KVFSLAH; -.
DR   OrthoDB; EOG4R23VG; -.
DR   Bgee; A2A8R0; -.
DR   Genevestigator; A2A8R0; -.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR022557; DUF3480.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR017165; Znf_FYVE_SARA/endofin.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF11979; DUF3480; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   PIRSF; PIRSF037289; SARA/endofin; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   4: Predicted;
KW   Metal-binding; Zinc.
SQ   SEQUENCE   1397 AA;  152417 MW;  E4A74480426CB240 CRC64;
     MENYFQAEAY NLDKVLDEFE QNEDETVSPT LLDTKWNKIL DPSSHPLSFN PALASVNEPT
     VSETGPQLKV FSLAGSAPLT KEDKDPCANG QDCSLNPETD TMWIDENAVT EDQLIKRNYN
     QDDQFSAVEV GEEKCGSLTC LPDEKNVLVV AVMHNCDKRT LQSDLQDCNN YNSQSLMNSF
     SCSLDNETRQ TDQFSFSMNG STEKGINSEK QMDALNKPKP ERDSVNHLCA ASSNSATSIS
     SPSQLKDGEN VGRDPSTSTV TSLAVNSSQG MDGGPAIKQQ GNYMPDEDLS GMNSSSRTDL
     GISNSFSHSS GELLIKTEPA EERTAEDSLP SDLSLNLKPD TPALSGRDNC EQSSDCLGSS
     ETRADEDEGN DSQMTNWKLT KLNEMSDSQV NEENQMALQS NQPEDTNSGG ECVGMADSDL
     DFKGTCMNES EGYDFSTVND APAANSLSNS CDSYGMQSPI VSFVPKTLPS KEDSVTEEKE
     IEESKSECYS NIYEQRGNEN AEGSGLLLNS TGNVMKKNYL HNFCSQIPSV LGQSSPKIAN
     LQSISVPFGG ARPKQPSNLK LQIPKPLSDH LQNDLPANNG NNSKNKNDVL GKAKLGENSA
     VNACSATLGN ISVTDTNGEH LETYEAEISS RPCLALAPDS PDNDLRASQF GISARKPFTT
     LGEVAPVWVP DSQAPNCMKC EARFTFTKRR HHCRACGKVF CASCCSLKCK LLYMDRKEAR
     VCVICHSVLM NAQAWENMMS ASSQSPNPNN PAEYCSTIPP LQQAQASGAL SSPPPTVMVP
     VGVLKHPGTE VPQPREQRRV WFADGILPNG EVADAAKLTM NGTSSAGTLA VSHDPVKPVA
     TSPLPTEADT SLFSGSITQV GSPVGSAMNL IPEDGLPPIL ISTGVKGDYA VEEKPSQISV
     MQQLEDGGPD PLVFVLNANL LSMVKIVNYV NRKCWCFTTK GMHAVGQSEI VILLQCLPDE
     KCLPKDIFNH FVQLYRDALA GNVVGSLGHS FFSQSFLGSK EHGGFLYVTS TYQSLQDLVL
     PTPPYLFGIL IQKWETPWAK VFPIRLLLRL GAEYRLYPCP LFSVRFRKPL FGETGHTIMN
     LLADFRNYQY TLPVVQGLVV DMEVRKTSIK IPSNRYNEMM KAMNKSNEHV LAGGACFNEK
     ADSHLVCVQN DDGNYQTQAI SIHNQPRKVT GASFFVFSGA LKSSSGYLAK SSIVEDGVMV
     QITAENMDSL RQALREMKDF TITCGKADAE DPQEQIHIQW VDDDKTVNKG VVSPIDGKSM
     ESITNVKIFH GSEYKANGKV IRWTEVFFLE NDDHHNCLSD PADHSRLTEH VAKAFCLALC
     PHLKLLKEDG MTKLGLRVTL DSDQVGYQAG SNGQPLPSQY MNDLDSALVP VIHGGACQLS
     EGPVVMELIF YILENIA
//
ID   SZT2_MOUSE              Reviewed;        3431 AA.
AC   A2A9C3; Q6PB77; Q7TSS6;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 26.
DE   RecName: Full=Protein SZT2;
DE   AltName: Full=Seizure threshold 2 protein;
DE   AltName: Full=Transcript increased in glutamate resistance;
DE            Short=TIGR;
GN   Name=Szt2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, MASS SPECTROMETRY,
RP   DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=19624305; DOI=10.1111/j.1601-183X.2009.00509.x;
RA   Frankel W.N., Yang Y., Mahaffey C.L., Beyer B.J., O'Brien T.P.;
RT   "Szt2, a novel gene for seizure threshold in mice.";
RL   Genes Brain Behav. 8:568-576(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INDUCTION, TISSUE
RP   SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=20045724; DOI=10.1016/j.freeradbiomed.2009.12.023;
RA   Toutzaris D., Lewerenz J., Albrecht P., Jensen L.T., Letz J.,
RA   Geerts A., Golz S., Methner A.;
RT   "A novel giant peroxisomal superoxide dismutase motif-containing
RT   protein.";
RL   Free Radic. Biol. Med. 48:811-820(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2675-3431.
RC   STRAIN=C57BL/6, and Czech II; TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Involved in oxidative stress. May be involved in
CC       superoxide dismutase activity and in neuroprotective effect of
CC       peroxisomes, but has no direct dismutase activity when tested in
CC       yeast. May enhance epileptogenesis and confer low seizure
CC       threshold.
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A2A9C3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2A9C3-2; Sequence=VSP_039917;
CC   -!- TISSUE SPECIFICITY: Mostly expressed in brain, spinal cord and
CC       lung.
CC   -!- INDUCTION: Induced in cells resistant to glutamate toxicity.
CC   -!- DISRUPTION PHENOTYPE: Mutant mice have a low seizure threshold;
CC       STZ2 expression is several fold increased in the brain. Mutations
CC       are induced by a chemical mutagen, ethylnitrosourea (ENU) that
CC       randomly induces point mutations in DNA. Mutagenesis screen of
CC       mice with low electroconvulsive threshold allows to identify STZ2
CC       as regulator of seizure threshold and neuronal excitation.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH52935.1; Type=Frameshift; Positions=Several;
CC       Sequence=AAH52935.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part;
CC       Sequence=GU433214; Type=Frameshift; Positions=Several;
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DR   EMBL; FJ998170; ACS91341.1; -; mRNA.
DR   EMBL; GU433214; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AL627212; CAM15198.1; -; Genomic_DNA.
DR   EMBL; BC059842; AAH59842.2; -; mRNA.
DR   EMBL; BC052935; AAH52935.1; ALT_SEQ; mRNA.
DR   IPI; IPI00420588; -.
DR   IPI; IPI00970666; -.
DR   RefSeq; NP_937813.3; NM_198170.3.
DR   UniGene; Mm.415218; -.
DR   PRIDE; A2A9C3; -.
DR   Ensembl; ENSMUST00000075406; ENSMUSP00000074862; ENSMUSG00000033253.
DR   GeneID; 230676; -.
DR   KEGG; mmu:230676; -.
DR   CTD; 230676; -.
DR   MGI; MGI:3033336; Szt2.
DR   eggNOG; roNOG09212; -.
DR   HOGENOM; HBG283014; -.
DR   HOVERGEN; HBG080139; -.
DR   InParanoid; A2A9C3; -.
DR   OMA; WRCYARL; -.
DR   OrthoDB; EOG4SJ5DR; -.
DR   Bgee; A2A9C3; -.
DR   Genevestigator; A2A9C3; -.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0007417; P:central nervous system development; IMP:MGI.
DR   GO; GO:0043473; P:pigmentation; IMP:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
PE   1: Evidence at protein level;
KW   Alternative splicing; Peroxisome.
FT   CHAIN         1   3431       Protein SZT2.
FT                                /FTId=PRO_0000399821.
FT   COMPBIAS   3040   3091       His-rich.
FT   VAR_SEQ    2131   2131       Missing (in isoform 2).
FT                                /FTId=VSP_039917.
FT   CONFLICT    275    275       C -> S (in Ref. 1; GU433214).
FT   CONFLICT    888    888       N -> K (in Ref. 1; GU433214).
FT   CONFLICT   1067   1067       L -> C (in Ref. 1; GU433214).
FT   CONFLICT   1192   1192       L -> H (in Ref. 1; GU433214).
FT   CONFLICT   1204   1204       S -> T (in Ref. 1; GU433214).
FT   CONFLICT   1308   1308       F -> S (in Ref. 1; GU433214).
SQ   SEQUENCE   3431 AA;  377627 MW;  2DADDD0F72FC38F7 CRC64;
     MASERPEPEV EEAGQVFLLM KKDYRISRNV RLAWFLNHLH QTVQATPQEL LLQSEQELEV
     LSVLPPGWQP DEPVVPRPFL LVPSTRVTFL AWQYRFVIEL DLSPSTGIVD DSTGEILFDE
     VFHALSRCLG GLLRPFRVPG SCINFQPEIY VTIQAYSSII GLQSHQVLVQ GCLLDPSQRE
     AFLQQVYEQL CLFEDKVATM LQQQYEPQGQ AEDQSPESGE SLGRKVGVSM VTADLGLVSM
     IRQGILALQL LPSNSSAGII VITDGVTSVP DVAVCETLLN QLRSGTVACS FVQVGGVYSY
     DCSFGHVPNV ELMKFIAMAT FGSYLSTCPE TEPGNLGLTV YHRAFLLYSF LRSGEALNPE
     YYCGSQHRLF NEHLVSASSN PALALRRKKH TEKEVPADLV STVSVRLREG YSVREVTLAK
     GGSQLEVKLV LLWKHNMRIE YVAVAPWPLE PEGPRGTRVE VTMEGGYDIL HDVSCALRQP
     IRSLYRTHVI RRFWNTLQSI NQTDQMLAHL QSFSSVPEHF TLPDSTKSGV PLFYIPPGSS
     TPVLSLQHSG SDSSHAQFAA YWKPVLSMDA NSWQRWLHMH RLVLILEHDT PLPKHLHTPG
     SNGRYSTIQC RISHSSLTSL LRDWSSFVLV EGYSYVKLLS SAPDQPPSSF YMVRIISKTP
     CMVLRLGFPI GTPAQARHKI VSGLKEEILR LRFPHRVQSK EPTPKVKRKG LGGVGGSSPS
     KSPPTLGPQQ ALSDRPCLVV LHKPLDKLLI RYEKLPLDYR APFLLTLEPP GPLPLVSGRS
     ASSSLASLSR YLYHRRWLWS VPSGLAPTLP LSATAQLLSV LTEVRLSEGF HFACSGEGII
     NMVLELPVQN EPLGQAAAEE KHTCVVQYIL FPPHSTSTKD SFSTDDDNDV EVEALEGDSE
     LNLVTEVWVE PQYGRVGPGP ENWKHLQDLT YSEIPQALHP RDAACIGSLL TFEYLIQLCQ
     SKEWGPLPPE PRLSDGLDQR GDTCVHEIPF HFDLLGLLPQ CQQLQMFFLL LSREPEGVPL
     AEGPCPTNDM VLCLLHSCLG QELSDREIPL TPADQAAFLN EVLRRSLRDP GPEGPPVGGH
     AVAKDRAGNS TQASGDSTLP SQSVVIPGVL RSSISAQPPQ WHCYARLLGP QHVFLTFLPA
     TFSDVQHLTA YGLESSFQEE TKPKLGDWSG APSLKDPGAT GTKATESQVP TLSVTLASDS
     AQDSGEPSTP SCQDLAANSG RQAPQTEGAD GPRTRCPVYI YSCSLEALRE QMVGLQPPQA
     PRDLIFRAQD LDHPSSSSAW MEPRCKEAAT HCALLQEHAQ RCFVRGLFRS LQQAQSVTCQ
     DLLTAVDACE ELLQEIDITS FLLALCGHTW GLPHAPPSPG PLSPGPFSSS IEEGPEPRER
     AILVSESSIE TEDLSEPEFQ SSRVSGNLDP GPEISLTDVC QLRGEAHDAL HSLIQEKFLE
     ISRLHFRTVP SNPHYFFYCP PSSRREDEGP RDTVDRKISD LEFSEAELVG EEGDTSACCV
     VTESDPELEV EYRESREPDL GPAGLDSASL SDADTVNPDE DSFSILGGDS PTGPDSLMHD
     LPPLFLHLTC SVRLRGQHSS VPVCSLPTCL GQVLSSLEGP PIGGRVPLRD LSITLDVFVL
     TLPLEVELPP ASDPQHHRST SESSASFPRS PGQPSSLRSD DGLGPPLPPP EEERHPGLSS
     LAMPHRLAIE STMNEIRWLL EDEMVGALRR GGIPQSPALH RAAAHIHSSS GRPTCLRQAP
     PLSFVFGPER SLTQFKEEFR RLHLPGHVLL EDPDSGFFFV AAGQQPGVLH GEPPSAAWAW
     HNHEDRAEDA EGEVLTASPQ VPGSLEDSEG TPLISLPSLS QGGSQPGPSR GLSLMSSQGS
     VDSDHLGYDG GSSGSDSEGP GETLGEKALF TLRTPPGPAP PQPSLPVLPG PSLPDFWLIV
     RILQDRVEVY AHARSLSRED GGPGAECRHL QQFLVRRVGE ICREVNQRLL LQDLHDSHVC
     NSLLVAESEE DLWRSETPFH SRQRAVLPSD DFAADESCAP RGYLAATMQF VPGHFSCDVV
     WGTVIRVHSR LKMGPSMGVS RAIQALRSVL NAFSVVNRKN MFVYQERATK AVYYLRLLET
     SCSDRPWEGD TLPPSLALSR SQEPISSEDS VAPRSPLDMA SSRSSDAVRP VGQVDRHIQL
     LVHGVGQAGP EITDELVRVL RRRLDEATLD IITVMLVRNC KLTPADVEFI QPPGSLPSEV
     LHLVLPPSCR PCLPALAWYL RQNLLTFLHS PKYTDSNSRN HFQHPLPAQG GLPDLDIYLY
     NKPGGQGTGG KGVACITLAF VEEGGTPISL ASWPPSSPGP PDPLREEEFE QLTQVIRCPN
     TLDSCSAQDG SPRLRLDVWE KGNISIVQLE EKLRAAARQA LADAIMELRL LPASLCTEDI
     PPGSLKSGPL DTKSPACRAN TFPCTPVSGE PVTPPSKAGR RSFWDMLSKT EAGDLGSPKT
     TDDIVLDRPE DTRGRRRHKT ENVRTPGGSE RAPGPDSGAQ RQRRRTTQLE EGEVGTLHPV
     FARVIQRWMG FMVQIGCASV SRSSTHMVSR FLLPSILSEF TTLVISMAGD TSVRVFEQHL
     GSEPDVFSPC SPGQLGPAPR PAAQRHLLLL GRNFAQWRRP TQQAAKAVQR FESGGDGSPG
     RSAPRQRLLL LEVTDKKLQL LTYNWAPDLG AALGRALIRL VQWQNARAHL ISCLLSQKLG
     LFHHCGQLDF PMRDGKEPNP FLLPTMEVET LIRNASPPLS REQGRLSGSS RGGGPLSLDT
     FPFDEALRDI TAARPSSTGG PAPRPPDPVT YHGQQFLEIK MTERKELERQ MKMENLFVTW
     QQRSAPASMP ISAGELETLK QSSRLVHYCA TALLFDPAAW LHGPPETCAP SEGQRRPCPE
     SGSGSREVPT SCESLDVPPP GAREEPWLKE LSLAFLQQYV QYLQSIGFVL VPLRPPSPAR
     STSRLRAMAI LGTEGRGSFS CPKAKAEGSP KSTSTPVTTY HLQRALPGGI ILMELTFQGC
     YFCVKQFALE CSRIPMGQAV NSQLSLLFTE ECDKVRDLMH VHSFSYDFHL RLVHQHVLGA
     HLALRHGYHL TTFLQHFLAH HPDGPHFGRN HIYQGTLELP TPLIAAHQLY NYVADHASSY
     HMKPLRMARP GGPEHNEYAL VSAWHSSGSY LDSEGLRHQD DFDVSLLVCH SAAPFEEQGE
     AERHVLRLQF FVVLTSQREL FPRLTADMRR FRKPSRLPLE PETPGSLVGS PREASGMMLA
     PGPAPLFPPL AAEVGMARAR LAQLVRLAGG HCRRDTLWKR LFLLEPPGPD RLRLGGRLAL
     AELEELLEAV HAKSIADIDP QLDCFLSMTV SWYQSLIKVL LSRFPQSCRH FQSPDLGTQY
     LVVLNQKFTD CFVLVFLDSH LGKTSLTVVF REPFPVQPQD SESPPAQLVS TYHHLESVIN
     TACFTLWTRL L
//
ID   K1109_MOUSE             Reviewed;        5005 AA.
AC   A2AAE1; A2AAD2; A2AAD4; Q05BP8; Q3UG08; Q3UYB7; Q571C4; Q69ZR8;
AC   Q6AXD9; Q8BWF1; Q8BY77; Q8CEA4; Q8R0A8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 3.
DT   08-MAR-2011, entry version 34.
DE   RecName: Full=Uncharacterized protein KIAA1109;
DE   AltName: Full=Fragile site-associated protein homolog;
GN   Name=Kiaa1109; Synonyms=Fsa, Kiaa1371;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 4183-4995 (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 3903-5005 (ISOFORM 6).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Kidney, Medulla oblongata, Skin, Testis, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1415 (ISOFORM 4).
RC   TISSUE=Pancreatic islet;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 261-1421 AND 4332-5005
RP   (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3442-5005
RP   (ISOFORM 2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3385-5005 (ISOFORM 3).
RC   TISSUE=Embryonic intestine;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [6]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=16545529; DOI=10.1016/j.gene.2005.12.024;
RA   Wei Y., Lin-Lee Y.-C., Yang X., Dai W., Zhao S., Rassool F.V.,
RA   Elgart G.W., Feun L., Savaraj N., Kuo M.T.;
RT   "Molecular cloning of Chinese hamster 1q31 chromosomal fragile site
RT   DNA that is important to mdr1 gene amplification reveals a novel gene
RT   whose expression is associated with spermatocyte and adipocyte
RT   differentiation.";
RL   Gene 372:44-52(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4613, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2931 AND SER-3653, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=A2AAE1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2AAE1-2; Sequence=VSP_031037;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=A2AAE1-3; Sequence=VSP_031036, VSP_031037, VSP_031038;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=A2AAE1-4; Sequence=VSP_031032, VSP_031033;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=A2AAE1-5; Sequence=VSP_031034, VSP_031035;
CC       Name=6;
CC         IsoId=A2AAE1-6; Sequence=VSP_031038;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis and ovary. Weakly
CC       or not expressed in other tissues.
CC   -!- DEVELOPMENTAL STAGE: Expressed during spermatogenesis and
CC       adipogenesis.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH27125.3; Type=Erroneous initiation;
CC       Sequence=AAH79623.1; Type=Erroneous initiation;
CC       Sequence=BAC31019.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAC31019.1; Type=Frameshift; Positions=4985;
CC       Sequence=BAC35104.1; Type=Erroneous initiation;
CC       Sequence=BAD90190.1; Type=Erroneous initiation;
CC       Sequence=CAM28060.1; Type=Erroneous gene model prediction;
CC       Sequence=CAM28069.1; Type=Erroneous gene model prediction;
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DR   EMBL; AK028716; BAC26080.1; -; mRNA.
DR   EMBL; AK041642; BAC31019.1; ALT_SEQ; mRNA.
DR   EMBL; AK052702; BAC35104.1; ALT_INIT; mRNA.
DR   EMBL; AK134811; BAE22295.1; -; mRNA.
DR   EMBL; AK148181; BAE28401.1; -; mRNA.
DR   EMBL; AL691425; CAM18175.4; -; Genomic_DNA.
DR   EMBL; AL645759; CAM18175.4; JOINED; Genomic_DNA.
DR   EMBL; AL662823; CAM18175.4; JOINED; Genomic_DNA.
DR   EMBL; AL662823; CAM18416.3; -; Genomic_DNA.
DR   EMBL; AL645759; CAM18416.3; JOINED; Genomic_DNA.
DR   EMBL; AL691425; CAM18416.3; JOINED; Genomic_DNA.
DR   EMBL; AL645759; CAM24476.3; -; Genomic_DNA.
DR   EMBL; AL662823; CAM24476.3; JOINED; Genomic_DNA.
DR   EMBL; AL691425; CAM24476.3; JOINED; Genomic_DNA.
DR   EMBL; AL645753; CAM28060.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL645806; CAM28060.1; JOINED; Genomic_DNA.
DR   EMBL; AL645753; CAM28062.1; -; Genomic_DNA.
DR   EMBL; AL645806; CAM28062.1; JOINED; Genomic_DNA.
DR   EMBL; AL645806; CAM28069.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL645753; CAM28069.1; JOINED; Genomic_DNA.
DR   EMBL; AL645806; CAM28070.1; -; Genomic_DNA.
DR   EMBL; AL645753; CAM28070.1; JOINED; Genomic_DNA.
DR   EMBL; AK220265; BAD90190.1; ALT_INIT; mRNA.
DR   EMBL; BC027125; AAH27125.3; ALT_INIT; mRNA.
DR   EMBL; BC034738; AAH34738.1; -; mRNA.
DR   EMBL; BC079623; AAH79623.1; ALT_INIT; mRNA.
DR   EMBL; AK173100; BAD32378.1; -; mRNA.
DR   IPI; IPI00755374; -.
DR   IPI; IPI00808103; -.
DR   IPI; IPI00850889; -.
DR   IPI; IPI00850947; -.
DR   IPI; IPI00884521; -.
DR   IPI; IPI00885934; -.
DR   RefSeq; NP_766267.2; NM_172679.2.
DR   UniGene; Mm.207907; -.
DR   PhosphoSite; A2AAE1; -.
DR   Ensembl; ENSMUST00000057272; ENSMUSP00000060199; ENSMUSG00000037270.
DR   GeneID; 229227; -.
DR   KEGG; mmu:229227; -.
DR   MGI; MGI:2444631; 4932438A13Rik.
DR   GeneTree; ENSGT00580000081590; -.
DR   HOVERGEN; HBG108027; -.
DR   InParanoid; A2AAE1; -.
DR   Bgee; A2AAE1; -.
DR   CleanEx; MM_4932438A13RIK; -.
DR   Genevestigator; A2AAE1; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR019362; DUF2246.
DR   InterPro; IPR018863; Fragile_site-assoc_C.
DR   Pfam; PF10229; DUF2246; 1.
DR   Pfam; PF10479; FSA_C; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   5005       Uncharacterized protein KIAA1109.
FT                                /FTId=PRO_0000317556.
FT   TRANSMEM     27     47       Helical; (Potential).
FT   COMPBIAS    772    779       Poly-Ser.
FT   COMPBIAS   1154   1157       Poly-Ser.
FT   COMPBIAS   1226   1391       Ser-rich.
FT   COMPBIAS   1417   1421       Poly-Lys.
FT   COMPBIAS   1544   1547       Poly-Ser.
FT   COMPBIAS   1991   1994       Poly-Pro.
FT   COMPBIAS   3838   3841       Poly-Lys.
FT   COMPBIAS   4110   4234       Ser-rich.
FT   MOD_RES    2931   2931       Phosphoserine.
FT   MOD_RES    3653   3653       Phosphoserine.
FT   MOD_RES    4613   4613       Phosphoserine.
FT   VAR_SEQ       1    386       Missing (in isoform 4).
FT                                /FTId=VSP_031032.
FT   VAR_SEQ     871    871       Missing (in isoform 4).
FT                                /FTId=VSP_031033.
FT   VAR_SEQ     872    877       QRPPVD -> VMSNDI (in isoform 5).
FT                                /FTId=VSP_031034.
FT   VAR_SEQ     878   5005       Missing (in isoform 5).
FT                                /FTId=VSP_031035.
FT   VAR_SEQ    3513   3513       T -> TSSDGSSVSGDGHKLTFGQRLVNHLLGLAPPNQRYS
FT                                VPAEYLCDSEMRGSPQSSQSHLKACRAHSWGN (in
FT                                isoform 3).
FT                                /FTId=VSP_031036.
FT   VAR_SEQ    3665   3665       T -> TLKNTVWGSSPQSRSPGEGYFQ (in isoform 2
FT                                and isoform 3).
FT                                /FTId=VSP_031037.
FT   VAR_SEQ    3915   3949       Missing (in isoform 3 and isoform 6).
FT                                /FTId=VSP_031038.
FT   CONFLICT    293    293       L -> I (in Ref. 1; BAE28401).
FT   CONFLICT    314    314       D -> E (in Ref. 1; BAE28401).
FT   CONFLICT    391    391       T -> A (in Ref. 1; BAE28401).
FT   CONFLICT    706    706       S -> C (in Ref. 1; BAE28401).
FT   CONFLICT    707    707       M -> T (in Ref. 1; BAE28401).
FT   CONFLICT    997    997       V -> I (in Ref. 3; BAD90190 and 4;
FT                                AAH34738).
FT   CONFLICT   4100   4100       S -> N (in Ref. 5; BAD32378).
FT   CONFLICT   4450   4450       S -> R (in Ref. 4; AAH27125).
FT   CONFLICT   4451   4451       M -> V (in Ref. 4; AAH27125).
FT   CONFLICT   4582   4582       Q -> K (in Ref. 1; BAC35104).
FT   CONFLICT   4606   4606       T -> A (in Ref. 5; BAD32378).
SQ   SEQUENCE   5005 AA;  555351 MW;  5D4263F6398A87AA CRC64;
     MDQRKNDSIV PSITQLEDFL TEHNSNVVWL LVATILSCGW IIYLTYYNSR NVGLILTLVL
     NRLYKHGYIH IGSFSFSVLS GKVMVREIYY ITEDMSIRIQ DGFIIFRWWK MYNPKQKQHD
     PKAETRLYIT VNDFEFHVYN RSDLYGRLQE LFGLEPTIIP PKKDDDKTRE NGRTRTQSKI
     ERVKVKTESQ DPTSSWRSLI PVIKVNVSTG RLAFGNHYQP QTLCINFDDA FLTYTTKPPS
     SHLDQFMHIV KGKLENVRVM LVPSPRYVGL QNDEPPRLMG EGFVVLQSND VDLYYYMDEP
     GLVPEETEES TEGDISSEDC KLQDLPPCWG LDIVCGKGTD FNYGPWADRQ RDCLWKFFFP
     PDYQVLKVSE IAQPGRPRQI LAFELRMNII TDATIDLLFT KNRETNAVHV NVGAGSYLEI
     NIPMTVDENG YTPAIKGQLL HVDATTSMQY RTLLEAEMLA FHINASYPRI WNMPQTWQCE
     LEVYKATYHF IFAQKNFFTD LIQDWSSDNA PDIFSFVPYT WNFKIMFHQF EMIWAANQHN
     WIDCSTKQQE NVYLAACGET LNIDFSLPFT DFVPATCNTR FSLRGEDVDL HLFLPDCHPS
     KYSLFMLVKN CHPNKMVPET GIPAECQSGQ KTVKPKWRNV TQEKAGWVEC WTVPSVMLTI
     DYTWHPIYPQ KADEQLKQSL SEMEETMLSV LRPAQKTSER VVSSPSMSPR PPVDPSELPP
     DKLHVEMELS PDSQITLYGP LLNAFLCIKE NYFGEDDMYM DFEEVISSPV LSLSTSSSSG
     WTAVGMDNDK RENESSAKSI HPLALRPWDI TVLVNLYKVH GRLPVHGTTD GPECPTAFLE
     RLCFEMKKGF RETMLQLVLS PLNVFVSDNY QQRPPVDEVL REGHINLSGL QLRAHAMFSA
     EGLPLGSDSL EYAWLIDVQA GSLTAKVTAP QLACLLEWGQ TFVFHVVCRE YELERPKSVI
     VCQHGIDRRF CESKLSCIPG PCPTSDDLKY TMTRLAVDGS DIYIVEHGCA TNIKMGAVRI
     ANCNLHNQSV GEGISAAIQD FQVRQYIEQL NNCRIGLQPA VLRRAYWLEA GSANLGLITV
     DIALAADHHS KHEAQRHFLE THDARTKRLW FLWPDDTLKN KRCRNKCGCL GGCRFFGGTV
     TGLDFFKLEE LTPSSSSAFS STSAESDMYY GQSLLQPGEW IITKEIPKTV DGNVNSMKRK
     EWENKSVGIE GERKTQHLSL QVPLRSHSSS SSSEENSSSS AAQPLLAGEK ESPSSAADDH
     SVQKDLLHSA RRDDGQASVP TEISGTSPVS PNTQDKSVGQ SPLRSPLKRQ ASVCSTRLGS
     TKSLTAAFYG DKQPVTVGVQ FSSDVSRSDE NVLDSPKQRR SFGSFPYTPS ADSNSFHQYR
     SMDSSMSMAD SEAYFSAAEE FEPISSDEGP GTYPGRKKKK KQMQQIDYSR GSIYHSVEGP
     LAVHGEGITD PRTLPFKTHP SQASFVSALG GEDEVIEHVY IVEGEKRGES EQVTSQQPVM
     SCYHTYLTQF QVINWSVKHP TNKRTSKSSL HRPLDLDTPT SEESSSSFEQ LCVPTFKVIK
     QGLTANSLLD RGMQLSGSTS NTPYTPLDKK IVDTTDDETL TEEWTLDQPV AQTKTTAIVE
     VKGTVDVVLT PLVAEALDRY IEAMVHRVST RHPAAIVDDL HTKVLREAVQ NSKTTFSENL
     SPKQDIRGTK TEHPMIGTTN QGQIQTNVTT KQDNVTIKGL QANVSIPKVN LCLLQASVEE
     SPATVPSRSV THVSLVALCF DRIATQVRMN RGVVEETANN VDAGKTSNFD RYVHASKMQP
     QSSGSLRSNA GAEKGKEIAA KLNIHRVHGQ LRGLDTTDIG TCAITAIPFE KSKVLFTLEE
     LDEFTFVDET DQQAIPDVTR IGPSQEKWGW IMFECGLENL TIKGGRQSGA VLYNSFGIMG
     KNSVTERGGV LTSNNSSDSP TGSGYNTDVS DDNLPCDRTS PSSDINGNSV SDEQDEGVES
     DDLKKDLPLM PPPPDSCSMK LTIKEIWFSF AAPTNVRSPA HAFSRQLNLL STATPAVGAW
     LVPIDQLKSS LNKLETEGTL RICAVMGCIM TEALENKSVH FPLRSKYNRL TKVARFLQEN
     PSCLLCNILH HYLHQANYSI IDDATMSDGL PALVTLKKGL VALARQWMKF IVVTPAFKGV
     SLHRPAQPLK PPATVDQEHE EGLGLDNGGG LQSDTSADGA EFEFDAATVS EHTMLLEGTA
     NRPPPGSSGP VTGAEIMRKL SKTHTHSDSA LKIKGIHPYH SLSYTSGDTA TDSPVHVGRA
     GMPVKESPRK ESLLSYLTGS FPSLHNLLEG TPQRSSAAVK SSSLTRTGNT VATDMLSEHP
     LLSEPSSVSF YNWMSNAVGN RGSVVQESPV TKSGHNSLPT GVAPNLPTIP SASDFNTVLS
     SDQNTLDGTH SQHSTSQDDV AGVEEANQGF PAVQLADAQV VFKPLLSHTG IQSQDTMPLC
     YRMYFGEHLS FSGTLDCLRA DIVDSDTAKD RKGKRARRQG HVNLPPLEFK PALMLETFSI
     SAVVMEKSVC TPQNSTSALS FHDLNKRYYN TFHCNFTISC QSISQHVDMA LVRLIHQFST
     MIDDIKATQT DIKLSRYTAG SASPTPTFKT RKHRDFRSSD FSRSSRGSLN GGNRVNNAKN
     KRANNENNKK ESRNKNSLGR SERRTSKVSR KGSKDVVDHM TIHMDDSDSI TVSEQSEPSA
     ECWQNMYKLL NFYSLISDPT GILEKSSETF GPAGVRSPTE PTCRVVFENE QDNNSLTKTQ
     RKRSLVTSEP QHVTLIVFGI GMVNRTHLEA DIGGLTMESE LKRIHGSFTL KEKMKDVLHQ
     KMTETCATAH IGGVNIVLLE GITPNIQLED FPTSPTSTAK QEFLTVVKCS IAKSQALYSA
     QRGLKTNNAA VFKVGAISIN IPQHPATLHS MMVRSSHQLS KQISDLIRQP STAPQPMKED
     IATPLPSEKT PTSVNQTPIE TNEFPQLPEG LEKKPIVLKF SAMLDGIAIG AALLPSLKAE
     YKMGRMRSHG MTGAQTRFTF ELPNHRLRFT SKVSATDMST IPPSASLNLP PVTMSGKYIM
     EEHDSYSDQV WSIDELPSKQ GYYLQGNYLR CVAEVGSFEH NLTTDLLNHL VFVQKVFMKE
     VNEVIQKVSG GEQPIPLWNE HDGTTDGDKP KILLYSLNLQ FKGIQVTATT PSMRAVRFET
     GLIELELSNR LQTKASPGSS SYLKLFGKCQ VDLNLALGQI VKHQVYEEAG SDFHQVAYFK
     TRIGLRNALR EEISGSSDRE AVLITLNRPI VYAQPVAFDR AVLFWLNYKA AYDNWNEQRM
     ALHKDIHMAT KEVVDMLPGI QQTSAQAFGT LFLQLTVNDL GICLPITNTA QSNHTGDLDT
     GSALVLTIES TLITACSSES LVSKGHFKNF CIRFADGFET SWDDWKPEIR GDLVMNACVV
     PDGTYEVCSR TTGQAAAESS SAGTWTLNVL WKMCGIDVHM DPNIGKRLNA LGNTLTTLTG
     EEDIDDIADL NSVNIADLSD EDEVDTMSPT IHTEAVDYRR QGTSSSQPGE LRGRKIMKRL
     VDIRELNEQA KVIDDLKKLG ASEGTINQEI QRYQQLESVA VNDIRRDVRK KLRRSSMRAA
     SLKDKWGLGY KPSYSRSKSI SASGRPPLKR MERASSRIGE TDELPEIRVD AASPGPRVTF
     NIQDTFPEET ELDLLSVTIE GPSHYSSNSE GSCSVFSSPK TTGGFSPSVP FQSEDGRRDD
     SLSSTSEDSE KDEKDEDRER ERFYIYRKPS HTSRKKATGF AAVHQLLTER WPTTPVNRSL
     SGTATERNID FELDIRVEID SGKCVLHPTT LLQEHDDISL RRSYDRSSRS LDQDSPSKKK
     KFQTNYASTT HLMTGKKVPS SLQTKPSDLE TTVFYIPGVD VKLHYNSKTL KTESPNASRG
     SSLPRTLSKE SKLYGMKDSA ASPSPSPLPC TVQSKTNTLL PPQPPPIPSA KGKGSGGVKT
     AKLYAWVALQ SLPEEMVISP CLLDFLEKAL ETIPITPIER NYTAVSSQDE DMGHFDIPDP
     MEESTTSLVS SSTSAYSSFP VDVVVYVRVQ PSQIKFSCLP VSRVECMLKL PSLDLVFSSN
     RGELETLGTT YPAETVSPGS NAPQTGAKTS ASKAGMPGSS GLGSPLGRSR HSSSQSDLTG
     SSSSSSGLSF TACMSDFSLY VFHPYGAGKQ KSTVSGLTSG SGGLGNVDEE PTSVTGRKDS
     LSINLEFVKV SLSRIRRSGG ASFFESQSVS KSTSKMDTTL INISAVCDIG SASFKYDMRR
     LSEILAFPRA WYRRSIARRL FLGDQTVNLP TSGPGTPDSI EGVSQHLSPE SSRKAYCRTW
     DQPSQSASFT HMPQSPNVFN EHMTNNTMSP GTAAQSLKSP ASIRSRSVSD SSVPRRDSIS
     KTSTPVNKSN KAASQQGTPW ETLVVFAINL KQLNVQMNMS NVMGNTTWTT SGLKSQGRLS
     VGSNRDREIS MSVGLGRSQL DSKGGVVGGT IDVNALEMVA HISEHPNQQP NHKIQITMGS
     TESRVDYMGS SILMGIFSNA DLKLQDEWKV NLYNALDSSM TDKSEIFVHG DLKWDIFQVM
     ISRSTTPDLI KIGMKLQEFF TQQFDTSKRA LSTWGPVPYL PPKTMTNNLE KNSQEQLLDA
     AHHRHWPGVL KVVSGCHISL FQVPLPEDGM QFGGSMSLHG NHMTLACFHG PNFRSKSWAL
     FHLEEPNIAF WTEAQKIWED GSSDHSTYIV QTLDFHLGHN TMVTKPCGAL ESPMATITKI
     TRRRHENPPH GVASVKEWFN YVTATRNEEL NLLRNVDANN TENSTTVKNS SLLSGFRGGS
     SYNHETETIF ALPRMQLEFK SIHVQEPQEP SLQDASLKPK VECSVVTEFT DHICVTMDAE
     LIMFLHDLVS AYLKEKEKAI FPPRILSTRP GQKCPLIIHD DSSSDRDRED SITYTTVDWR
     DFMCNTWHLE PTLRLISWTG RKIDPVGVDY ILQKLGFHHA RTTIPKWLQR GVMDPLDKVL
     SVLIKKLGTA LQDEKEKKGK DKEEH
//
ID   MED14_MOUSE             Reviewed;        1459 AA.
AC   A2ABV5; Q3TQU3; Q6P1H5; Q9R0T1; Q9WTN9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 39.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 14;
DE   AltName: Full=Cofactor required for Sp1 transcriptional activation subunit 2;
DE            Short=CRSP complex subunit 2;
DE   AltName: Full=Mediator complex subunit 14;
DE   AltName: Full=Thyroid hormone receptor-associated protein complex 170 kDa component;
DE            Short=Trap170;
GN   Name=Med14; Synonyms=Crsp2, Gm641, Trap170;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   MEDLINE=99443876; PubMed=10512684; DOI=10.1006/geno.1999.5944;
RA   Takada S., Kamiya M., Arima T., Kagebayashi H., Shibata H.,
RA   Muramatsu M., Chapman V.M., Wake N., Hayashizaki Y., Takagi N.;
RT   "Detection and cloning of an X-linked locus associated with a NotI
RT   site that is not methylated on mouse inactivated X chromosome by the
RT   RLGS-M method.";
RL   Genomics 61:92-100(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH GATA1.
RX   PubMed=17132730; DOI=10.1073/pnas.0604494103;
RA   Stumpf M., Waskow C., Kroetschel M., van Essen D., Rodriguez P.,
RA   Zhang X., Guyot B., Roeder R.G., Borggrefe T.;
RT   "The mediator complex functions as a coactivator for GATA-1 in
RT   erythropoiesis via subunit Med1/TRAP220.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18504-18509(2006).
RN   [6]
RP   ERRATUM.
RA   Stumpf M., Waskow C., Kroetschel M., van Essen D., Rodriguez P.,
RA   Zhang X., Guyot B., Roeder R.G., Borggrefe T.;
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1442-1442(2007).
CC   -!- FUNCTION: Component of the Mediator complex, a coactivator
CC       involved in the regulated transcription of nearly all RNA
CC       polymerase II-dependent genes. Mediator functions as a bridge to
CC       convey information from gene-specific regulatory proteins to the
CC       basal RNA polymerase II transcription machinery. Mediator is
CC       recruited to promoters by direct interactions with regulatory
CC       proteins and serves as a scaffold for the assembly of a functional
CC       preinitiation complex with RNA polymerase II and the general
CC       transcription factors (By similarity).
CC   -!- SUBUNIT: Component of the Mediator complex, which is composed of
CC       MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13,
CC       MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21,
CC       MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31,
CC       CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8
CC       subunits form a distinct module termed the CDK8 module. Mediator
CC       containing the CDK8 module is less active than Mediator lacking
CC       this module in supporting transcriptional activation. Individual
CC       preparations of the Mediator complex lacking one or more distinct
CC       subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and
CC       TRAP. Interacts with AR, ESR1, SREBF1 and STAT2 (By similarity).
CC       Interacts with GATA1.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=A2ABV5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2ABV5-2; Sequence=VSP_028037, VSP_028038;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=A2ABV5-3; Sequence=VSP_028035, VSP_028036;
CC       Name=4;
CC         IsoId=A2ABV5-4; Sequence=VSP_028033, VSP_028034;
CC         Note=No experimental confirmation avilable;
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 14 family.
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DR   EMBL; AB019028; BAA76610.1; -; mRNA.
DR   EMBL; AB019029; BAA76611.1; -; Genomic_DNA.
DR   EMBL; AK163306; BAE37289.1; -; mRNA.
DR   EMBL; AL662925; CAM17981.1; -; Genomic_DNA.
DR   EMBL; BX000537; CAM17981.1; JOINED; Genomic_DNA.
DR   EMBL; BX000537; CAM27890.1; -; Genomic_DNA.
DR   EMBL; AL662925; CAM27890.1; JOINED; Genomic_DNA.
DR   EMBL; BC065072; AAH65072.1; -; mRNA.
DR   IPI; IPI00417070; -.
DR   IPI; IPI00469443; -.
DR   IPI; IPI00788366; -.
DR   IPI; IPI00831273; -.
DR   RefSeq; NP_001041673.1; NM_001048208.1.
DR   RefSeq; NP_036135.3; NM_012005.3.
DR   UniGene; Mm.17616; -.
DR   STRING; A2ABV5; -.
DR   PhosphoSite; A2ABV5; -.
DR   PRIDE; A2ABV5; -.
DR   Ensembl; ENSMUST00000071680; ENSMUSP00000071603; ENSMUSG00000064127.
DR   Ensembl; ENSMUST00000096495; ENSMUSP00000094239; ENSMUSG00000064127.
DR   GeneID; 26896; -.
DR   KEGG; mmu:26896; -.
DR   CTD; 26896; -.
DR   MGI; MGI:1349442; Med14.
DR   GeneTree; ENSGT00390000001021; -.
DR   HOGENOM; HBG357410; -.
DR   HOVERGEN; HBG104308; -.
DR   InParanoid; A2ABV5; -.
DR   OMA; WANNAGK; -.
DR   NextBio; 304735; -.
DR   Bgee; A2ABV5; -.
DR   CleanEx; MM_MED14; -.
DR   Genevestigator; A2ABV5; -.
DR   InterPro; IPR013947; Mediator_Med14.
DR   Pfam; PF08638; MED14; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Nucleus; Phosphoprotein; Repeat;
KW   Transcription; Transcription regulation.
FT   CHAIN         1   1459       Mediator of RNA polymerase II
FT                                transcription subunit 14.
FT                                /FTId=PRO_0000304585.
FT   REGION      194    572       Interaction with STAT2 (By similarity).
FT   REGION      506    830       Interaction with SREBF1 (By similarity).
FT   MOTIF        75     79       LXXLL motif 1.
FT   MOTIF      1187   1191       LXXLL motif 2.
FT   COMPBIAS     31     51       Ala-rich.
FT   COMPBIAS   1008   1170       Pro-rich.
FT   MOD_RES     623    623       Phosphoserine (By similarity).
FT   MOD_RES     992    992       Phosphoserine (By similarity).
FT   MOD_RES    1117   1117       Phosphoserine (By similarity).
FT   MOD_RES    1124   1124       Phosphoserine (By similarity).
FT   MOD_RES    1133   1133       Phosphoserine (By similarity).
FT   MOD_RES    1138   1138       Phosphoserine (By similarity).
FT   MOD_RES    1141   1141       Phosphoserine (By similarity).
FT   MOD_RES    1147   1147       Phosphoserine (By similarity).
FT   MOD_RES    1149   1149       Phosphoserine (By similarity).
FT   VAR_SEQ       1     72       Missing (in isoform 4).
FT                                /FTId=VSP_028033.
FT   VAR_SEQ     435   1459       Missing (in isoform 4).
FT                                /FTId=VSP_028034.
FT   VAR_SEQ     436    471       SIETALPALIVPILEPCGNSECLHIFVDLHSGMFQL -> K
FT                                HSRAGEMAQQLRVPTALPKVLSSNPINHMVAHNHL (in
FT                                isoform 3).
FT                                /FTId=VSP_028035.
FT   VAR_SEQ     472   1459       Missing (in isoform 3).
FT                                /FTId=VSP_028036.
FT   VAR_SEQ     747    770       PSRHVYLTYENLLSEPVGGRKVVE -> KIFHTVFLLMSIF
FT                                LKVLVTISFFL (in isoform 2).
FT                                /FTId=VSP_028037.
FT   VAR_SEQ     771   1459       Missing (in isoform 2).
FT                                /FTId=VSP_028038.
FT   CONFLICT    158    158       F -> C (in Ref. 2; BAE37289).
FT   CONFLICT    346    347       WN -> C (in Ref. 1; BAA76611).
SQ   SEQUENCE   1459 AA;  160966 MW;  FE61E45E8E99E4E9 CRC64;
     MAPVQLDNHQ LIPPGGGGGS SGGGGSSSGS ASAPAPPPPA AAVAAAAAAA ASPGYRLSTL
     IEFLLHRAYS ELMVLTDLLP RKSDVERKIE IVQFASRTRQ LFVRLLALVK WANDAGKVEK
     CAMISSFLDQ QAILFVDTAD RLASLARDAL VHARLPSFAI PYAIDVLTTG SYPRLPTCIR
     DKIIPPDPIT KIEKQATLHQ LNQILRHRLV TTDLPPQLAN LTVANGRVKF RVEGEFEATL
     TVMGDDPEVP WRLLKLEILV EDKETGDGRA LVHSMQIDFI HQLVQSRLFA DEKPLQDMYN
     CLHCFCLSLQ LEVLHSQTLM LIRERWGDLV QVERYHAGKS LSLSVWNQQV LGRKTGTASV
     HKVTIKIDEN DVSKPLQIFH DPPLPASDSK LVERAMKIDH LSIEKLLIDS VHARAHQRLQ
     ELKAILRSFN ANESSSIETA LPALIVPILE PCGNSECLHI FVDLHSGMFQ LMLYGLDPAT
     LEDMEKSLND DMKRIIPWIQ QLKFWLGQQR CKQSIKHLPT ITTETLQLAN YSTHPIGSLS
     KNKLFIKLTR LPQYYIVVEM LEVPNKPTQL SYNYYFMSVS TADREDSPVM ALLLQQFKDN
     IQDLMSYTKT GKQTRTGTKH KLSDDPCPID SKKAKRSGEM CAFNKVLAHF VAMCDTNMPF
     VGLRLELSNL EIPHQGVQVE GDGFNHAIRL LKIPPCKGIS EETQKALDRS LLDCTFRLQG
     RNNRTWVAEL VFANCPLNGT STREQGPSRH VYLTYENLLS EPVGGRKVVE MFLNDWSSIA
     RLYECVLEFA RSLPEIPAHL NIFSEVRVYN YRKLILCYGT TKGSSISIQW NSIHQKFHIA
     LGTVGPNSGC SNCHNTILHQ LQEMFNKTPN VVQLLQVLFD TQAPLNAINK LPTVPMLGLT
     QRTNTAYQCF SILPQSSTHI RLAFRNMYCI DIYCRSRGVV AIRDGAYSLF DNSKLVEGFY
     PAPGLKTFLN MFVDSNQDAR RRSVNEDDNP PSPIGGDMMD SLISQLQPPQ QQPFPKQPGT
     SGAYPLTSPP TSYHSTVNQS PSMMHTQSPG NLHAASSPSG ALRAPSPASF VPTPPPSSHG
     ISIGPGASFA SPHGTLDPSS PYTMVSPSGR AGNWPGSPQV SGPSPATRLP GMSPANPSLH
     SPVPDVSHSP RAGTSSQTMP TNMPPPRKLP QRSWAASIPT ILTHSALNIL LLPSPTPGLV
     PGLAGSYLCS PLERFLGSVI MRRHLQRIIQ QETLQLINSN EPGVIMFKTD ALKCRVALSP
     KTNQTLQLKV TPENAGQWKP DELQVLEKFF ETRVAGPPFK ANTLIAFTKL LGAPTHILRD
     CVHIMKLELF PDQATQLKWN VQFCLTIPPS APPIAPPGTP AVVLKSKMLF FLQLTQKTSV
     PPQEPVSIIV PIIYDMASGT TQQADIPRQQ NSSVAAPMMV SNILKRFAEM NPPRQGECTI
     FAAVRDLMAN LTLPPGGRP
//
ID   A2AC03_MOUSE            Unreviewed;       178 AA.
AC   A2AC03;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-FEB-2011, entry version 22.
DE   SubName: Full=Alveolar soft part sarcoma chromosome region, candidate 1 (Human);
DE   Flags: Fragment;
GN   Name=Aspscr1; ORFNames=RP23-84C12.15-004;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Peck A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL663030; CAM27111.1; -; Genomic_DNA.
DR   IPI; IPI00649204; -.
DR   UniGene; Mm.294020; -.
DR   STRING; A2AC03; -.
DR   Ensembl; ENSMUST00000026135; ENSMUSP00000026135; ENSMUSG00000025142.
DR   Ensembl; ENSMUST00000103016; ENSMUSP00000099305; ENSMUSG00000025142.
DR   Ensembl; ENSMUST00000106158; ENSMUSP00000101764; ENSMUSG00000025142.
DR   Ensembl; ENSMUST00000106159; ENSMUSP00000101765; ENSMUSG00000025142.
DR   Ensembl; ENSMUST00000135346; ENSMUSP00000120072; ENSMUSG00000025142.
DR   Ensembl; ENSMUST00000147850; ENSMUSP00000116151; ENSMUSG00000025142.
DR   Ensembl; ENSMUST00000151160; ENSMUSP00000116447; ENSMUSG00000025142.
DR   MGI; MGI:1916188; Aspscr1.
DR   GeneTree; ENSGT00510000048362; -.
DR   InParanoid; A2AC03; -.
DR   Bgee; A2AC03; -.
DR   Genevestigator; A2AC03; -.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0019898; C:extrinsic to membrane; IDA:MGI.
DR   GO; GO:0009898; C:internal side of plasma membrane; IDA:MGI.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR   GO; GO:0000300; C:peripheral to membrane of membrane fraction; IDA:MGI.
DR   GO; GO:0012506; C:vesicle membrane; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; IDA:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; IDA:MGI.
DR   GO; GO:0046324; P:regulation of glucose import; IDA:MGI.
PE   4: Predicted;
FT   NON_TER     178    178
SQ   SEQUENCE   178 AA;  18951 MW;  E48FA8EC3BC523D6 CRC64;
     MVPVSRSREG PENIVRIAFQ LDDGSRLQDA FCSRQTLWEL LSHFAQTRER LQQLGEKTPV
     CVYMRNEVTG RAALQNTTLQ SLGLTGGSAT IRFVIKQCDT AGKQESIAVR SKAPGSPVSS
     LSADQASSST LLPLNSGEFS RGDLNHEGDA NTSGTGLEGG PKPTDAQTKQ STSEPASA
//
ID   A2AC46_MOUSE            Unreviewed;       752 AA.
AC   A2AC46;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 42.
DE   SubName: Full=ATP-binding cassette, sub-family B (MDR/TAP), member 7;
GN   Name=Abcb7; ORFNames=RP23-202N14.1-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Heath P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
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DR   EMBL; BC151037; AAI51038.1; -; mRNA.
DR   EMBL; AL663052; CAM17389.1; -; Genomic_DNA.
DR   IPI; IPI00761646; -.
DR   RefSeq; NP_033722.1; NM_009592.1.
DR   UniGene; Mm.426128; -.
DR   ProteinModelPortal; A2AC46; -.
DR   SMR; A2AC46; 120-709.
DR   STRING; A2AC46; -.
DR   Ensembl; ENSMUST00000033695; ENSMUSP00000033695; ENSMUSG00000031333.
DR   GeneID; 11306; -.
DR   KEGG; mmu:11306; -.
DR   CTD; 11306; -.
DR   MGI; MGI:109533; Abcb7.
DR   eggNOG; roNOG10658; -.
DR   HOVERGEN; HBG080194; -.
DR   InParanoid; A2AC46; -.
DR   OMA; FGQGVIF; -.
DR   PhylomeDB; A2AC46; -.
DR   NextBio; 278598; -.
DR   Bgee; A2AC46; -.
DR   Genevestigator; A2AC46; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IMP:MGI.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR017940; ABC_transporter_type1.
DR   InterPro; IPR001140; ABC_transptr_TM_dom.
DR   InterPro; IPR011527; ABC_transptrTM_dom_typ1.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF90123; ABC_TM_1; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding.
SQ   SEQUENCE   752 AA;  82581 MW;  79B2BC8A7A07555A CRC64;
     MALLAIHSWR WAAAAVAFEK HKHSAVLTRA LVSMCGSGPR WSSSQRGASG SARLSQTTES
     LRNTTQQRWG KDNSRQLLDA TKALQTWPLI EKRTCWHGHA GGGLHTDPKE GLKDVDTRKI
     IKAMLSYVWP EDRPDLRARV AISLGFLGGA KAMNIVVPFM FKYAVDSLNQ MSGNMLNLSD
     APNTVATMAT AVLIGYGVSR AGAAFFNEVR NAVFGKVAQN SIRRIAKNVF LHLHNLDLGF
     HLSRQTGALS KAIDRGTRGI SFVLSALVFN LLPIVFEMML VSSVLYYKCG AQFALVTLGT
     LGAYTAFTVA VTRWRTRFRI EMNKADNDAG NAAIDSLLNY ETVKYFNNEK YEAQRYDGFL
     KTYETASLKS TSTLAMLNFG QNAIFSVGLT AIMVLASQGI VAGALTVGDL VMVNGLLFQL
     SLPLNFLGTV YRETRQALID MNTLFTLLKV DTRIKDKVMA PPLQITPQTA TVAFDNVHFE
     YIEGQKVLNG VSFEVPAGKK VAIVGGSGSG KSTIVRLLFR FYEPQKGSIY LAGQNLQDVS
     LESLRRAVGV VPQDAVLFHN TIYYNLLYGN INASPEEVYA VAKLAGLHDA ILRMPHGYDT
     QVGERGLKLS GGEKQRVAIA RAILKNPPVI LYDEATSSLD SITEETILGA MRDVVKHRTS
     IFIAHRLSTV VDADEIIVLS QGKVAERGTH YGLLANSSSI YSEMWHTQSN RVQNQDSLGW
     DAKKESLSKE EERKKLQEEI VNSVKGCGNC SC
//
ID   A2ACV6_MOUSE            Unreviewed;      1654 AA.
AC   A2ACV6;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 27.
DE   SubName: Full=Novel protein;
GN   Name=9830001H06Rik; ORFNames=RP23-430P1.3-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Griffiths C.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL669932; CAM24113.1; -; Genomic_DNA.
DR   IPI; IPI00944761; -.
DR   RefSeq; NP_001158135.1; NM_001164663.1.
DR   UniGene; Mm.79466; -.
DR   Ensembl; ENSMUST00000069098; ENSMUSP00000066556; ENSMUSG00000055485.
DR   GeneID; 320706; -.
DR   KEGG; mmu:320706; -.
DR   MGI; MGI:2444575; 9830001H06Rik.
DR   eggNOG; roNOG09111; -.
DR   HOGENOM; HBG716993; -.
DR   HOVERGEN; HBG080205; -.
DR   InParanoid; A2ACV6; -.
DR   OMA; AVCDCST; -.
DR   OrthoDB; EOG4XSKP1; -.
DR   Bgee; A2ACV6; -.
DR   Genevestigator; A2ACV6; -.
DR   InterPro; IPR021507; DUF3166.
DR   Pfam; PF11365; DUF3166; 2.
PE   4: Predicted;
SQ   SEQUENCE   1654 AA;  183145 MW;  6B14B640F9022498 CRC64;
     METPAGESSA RGYGPPPAPA PAAERKKSHR APSPARPKDV AGWSLAKGRR GTGPGSATAC
     GTASSARPDK KGRAVAPGTR GTGPRVAGVR TGVRAKGRPR PGTGPRPPPP PPSLTDSSSE
     VSDCASEEAR QLGLELALSS DAESAAGGPA GTRTGQPPQP AQSGQQPPRP PASPDEPSVA
     ASSVGSSRLP LSASLAFSDL TEEMLDCGPG GLVRELEELR SENDYLKDEI EELRAEMLEM
     RDVYMEEDVY QLQELRQQLD QASKTCRILQ YRLRKAERRS LRAAQTGQVD GELIRGLEQD
     VKVSKDISMR LHKELEVVEK KRMRLEEENE GLRQRLIETE LAKQVLQTEL DRPREHSLKK
     RGTRSLGKTD KKPTAQEDSA DLKCQLHFAK EESALMCKKL TKLAKENDSM KEELLKYRSL
     YGDLDAALSA EELADAPHSR ETELKVHLKL VEEEANLLSR RIVELEVENR GLRAEMDDMK
     DHGGGGGPEA RLAFSSLGGE CGESLAELRR HLQFVEEEAE LLRRSSAELE DQNKLLLNEL
     AKYRSEHELD VTLSEDSCSV LSEPSQEELA AAKLQIGELS GKVKKLQYEN RVLLSNLQRC
     DLASCQSTRP MLETDAEAGD SAQCVPAPLG ETLEPHAARL CRAREAEALP GLREQAALVS
     KAIDVLVADA NGFSVGLRLC LDNECADLRL HEAPDNSEGP RDAKLIHAIL VRLSVLQQEL
     NAFTRKADVA LGSSGKEQPE PFPALPALGS QGPAKEIMLS KDLGSDFQPP DFRDLLEWEP
     RIREAFRTGD LESKPDPSRN FRPYRAEDND SYASEIKDLQ LVLAEAHDSL RGLQEQLSQE
     RQLRKEEADS FNQKMVQLKE DQQRALLRRE FELQSLSLQR RLEQKFWSQE KNILVQESQQ
     FKHNFLLLFM KLRWFLKRWR QGKVLPSEED DFLEVNSMKE LYLLMEEEEM NAQHSDNKAC
     TGESWTQNTP NECIKTLADM KVTLKELCWL LQDERRGLTE LQQQFAKAKA TWETERAELK
     GHASQMELKA GKGASERPGP DWKAALQRER EEQQHLLAES YSAVMELTRQ LQLSERHWSQ
     EKLQLVERLQ GEKQQVEQQV KELQNRLSQL QKAAEPWVLK HSDMEKQDNS WKEARSEKTH
     DKEGVSEAEL GGTGLKRTKS VSSMSEFESL LDCSPYLAGG DARNKKLPNG PAFAFVSTEP
     VEPEKDAKEK AGLSTRDCSH IGSLACQEPA GRQMQRSYTA PDKTGIRVYY SPPVARRLGV
     PVVHDKEGKI LIEPGFLFTT AKPKESAEAD GLAESSYSRW LCNFSRQRLD GGSGASTSGS
     GPAFPALHDF EMSGNMSDDM KEITNCVRQA MRSGSLERKV KNTSSQTVGV ATVGTQTIRT
     VSVGLQTDPP RSSLHSKSWS PRSSSLVSVR SKQISSSLDK VHSRIERPCC SPKYGSPKLQ
     RRSVSKLDST KDRSLWNLHQ GKQNGSAWAR STTTRDSPVL RNINDGLSSL FSVVEHSGST
     ESVWKLGMSE ARTKPEPPKY GIVQEFFRNV CGRAPSPTTA AGEESCKKPE PLSPASYHQP
     EGVSRILNKK AAKAGGSEEV RPTMLSQVGK DGILRDGDGS LILPSEDAVC DCSAQSLASC
     FIRPSRNTIR HSPSKCRLHP SESGWGGEER AAPQ
//
ID   A2AD03_MOUSE            Unreviewed;       662 AA.
AC   A2AD03;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   30-NOV-2010, entry version 34.
DE   SubName: Full=Choroidermia;
GN   Name=Chm; ORFNames=RP23-213K6.2-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Collins J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL669958; CAM17683.1; -; Genomic_DNA.
DR   IPI; IPI00828331; -.
DR   RefSeq; NP_061288.2; NM_018818.2.
DR   UniGene; Mm.257316; -.
DR   ProteinModelPortal; A2AD03; -.
DR   SMR; A2AD03; 2-626.
DR   STRING; A2AD03; -.
DR   PRIDE; A2AD03; -.
DR   Ensembl; ENSMUST00000026607; ENSMUSP00000026607; ENSMUSG00000025531.
DR   GeneID; 12662; -.
DR   KEGG; mmu:12662; -.
DR   CTD; 12662; -.
DR   MGI; MGI:892979; Chm.
DR   eggNOG; roNOG14744; -.
DR   HOVERGEN; HBG004961; -.
DR   InParanoid; A2AD03; -.
DR   OMA; IAMTSET; -.
DR   PhylomeDB; A2AD03; -.
DR   NextBio; 281894; -.
DR   Bgee; A2AD03; -.
DR   Genevestigator; A2AD03; -.
DR   GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IEA:InterPro.
DR   GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IEA:InterPro.
DR   GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR   InterPro; IPR018203; GDP_dissociation_inhibitor.
DR   InterPro; IPR001738; Rab_escort.
DR   InterPro; IPR002005; Rab_GDI_REP.
DR   InterPro; IPR016664; Rab_geranylTrfase_A_euk.
DR   PANTHER; PTHR11787; Rab_GDI_REP; 1.
DR   Pfam; PF00996; GDI; 2.
DR   PIRSF; PIRSF016550; Rab_ger_ger_transf_A_euk; 1.
DR   PRINTS; PR00893; RABESCORT.
DR   PRINTS; PR00891; RABGDIREP.
PE   4: Predicted;
SQ   SEQUENCE   662 AA;  73664 MW;  A5DFB31AEA6502C5 CRC64;
     MADNLPSDFD VIVIGTGLPE SIIAAACSRS GQRVLHVDSR SYYGGNWASF SFSGLLSWLK
     EYQENSDVVT ENSMWQEQIL ENEEAILLSS KDKTIQHVEV FCYASQDLHK DVEEAGALQK
     NPASVMSAQA TEAAEAAEAA EAAEATEAAE AACLPTAEES LSTRSCELPA EQSQCTGPES
     SPQVNDAEVG EKETQSDAKS STEQSSEILP KVQDNTETPK RNVITYSQII KEGRRFNIDL
     VSKLLYSRGL LIDLLIKSNV SRYAEFKNIT RILAFREGTV EQVPCSRADV FNSKQLTMVE
     KRMLMKFLTF CVEYEDHPDE YKAYEETTFS EYLKTQKLTP NLQYFVLHSI AMTSETTSST
     VDGLKATKKF LQCLGRYGNT PFLFPLYGQG ELPQCFCRMC AVFGGIYCLR HSVQCLVVDK
     ESRKCKAIVD QFGQRIISKH FVIEDSYLSE NTCSGVQYRQ ISRAVLITDG SVLKPDSDQQ
     VSILTVPAEE SGSFAVRVIE LCSSTMTCMK GTYLVHLTCM SSKTAREDLE RVVQKLFTPY
     TEIEAENEQV EKPRILWALY FNMRDSSDIS RDCYNDLPSN VYVCSGPDCN LGNDNAVQQA
     ETVFQKICPN EDFCPAPPNP EDIILDGDSS QQEVSESSVI PETNSETPKE STVLGDSEEP
     SE
//
ID   A2ADB2_MOUSE            Unreviewed;       273 AA.
AC   A2ADB2;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 31.
DE   SubName: Full=Family with sequence similarity 131, member C;
DE   SubName: Full=MCG10041;
DE   SubName: Full=Novel protein;
GN   Name=Fam131c; Synonyms=Gm693, RP23-308N2.4;
GN   ORFNames=RP23-308N2.4-001, mCG_10041;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Wood J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC147048; AAI47049.1; -; mRNA.
DR   EMBL; BC147049; AAI47050.1; -; mRNA.
DR   EMBL; AL670285; CAM20394.1; -; Genomic_DNA.
DR   EMBL; CH466615; EDL13363.1; -; Genomic_DNA.
DR   IPI; IPI00118611; -.
DR   RefSeq; NP_001078982.1; NM_001085513.1.
DR   UniGene; Mm.294614; -.
DR   PRIDE; A2ADB2; -.
DR   Ensembl; ENSMUST00000006380; ENSMUSP00000006380; ENSMUSG00000006218.
DR   GeneID; 277743; -.
DR   KEGG; mmu:277743; -.
DR   NMPDR; fig|10090.3.peg.10723; -.
DR   CTD; 277743; -.
DR   MGI; MGI:2685539; Fam131c.
DR   eggNOG; roNOG06334; -.
DR   GeneTree; ENSGT00390000015421; -.
DR   HOGENOM; HBG716984; -.
DR   HOVERGEN; HBG080216; -.
DR   InParanoid; A2ADB2; -.
DR   OMA; PWQRCFQ; -.
DR   OrthoDB; EOG4N5VXN; -.
DR   NextBio; 393815; -.
DR   Bgee; A2ADB2; -.
DR   Genevestigator; A2ADB2; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   273 AA;  29919 MW;  0EE72CE189EB3938 CRC64;
     MGSCVSRDLF TSAHKNSPRP QGTDLLNRDL PSSHSPAIVP DHVAGKDKQM DFCWDPWQRC
     FQTTNGYISD SRACPSNYSV AALATSSLVG VVQSIKDHIT KPTAMARGRV AHLIEWKGWS
     AQQSGWELSP AEDEHYCCLP DELREARFAA GVAEQFAITE ATLSAWSSLD DEELQPEDST
     QGAFQLQDLE SIYLQDSLLS GPSQDDSLLA CSPGLTLNDG WPSPEEPPSP TQQHHRQRLP
     GAQGLDDRAH LHGSLPSVDS GSLSEEEDEV FYN
//
ID   DDI2_MOUSE              Reviewed;         399 AA.
AC   A2ADY9;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   RecName: Full=Protein DDI1 homolog 2;
GN   Name=Ddi2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-121 AND
RP   SER-128, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SIMILARITY: Belongs to the DDI1 family.
CC   -!- SIMILARITY: Contains 1 ubiquitin-like domain.
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DR   EMBL; AL671733; CAM27072.1; -; Genomic_DNA.
DR   IPI; IPI00608021; -.
DR   RefSeq; NP_001017966.1; NM_001017966.2.
DR   UniGene; Mm.393721; -.
DR   UniGene; Mm.441022; -.
DR   UniGene; Mm.459121; -.
DR   ProteinModelPortal; A2ADY9; -.
DR   SMR; A2ADY9; 1-83, 231-360.
DR   STRING; A2ADY9; -.
DR   PhosphoSite; A2ADY9; -.
DR   PRIDE; A2ADY9; -.
DR   Ensembl; ENSMUST00000102484; ENSMUSP00000099542; ENSMUSG00000078515.
DR   GeneID; 68817; -.
DR   KEGG; mmu:68817; -.
DR   CTD; 68817; -.
DR   MGI; MGI:1917244; Ddi2.
DR   eggNOG; roNOG05279; -.
DR   GeneTree; ENSGT00510000047125; -.
DR   HOGENOM; HBG737457; -.
DR   HOVERGEN; HBG058638; -.
DR   InParanoid; A2ADY9; -.
DR   OMA; GTTGTET; -.
DR   OrthoDB; EOG4RFKSW; -.
DR   PhylomeDB; A2ADY9; -.
DR   NextBio; 327997; -.
DR   Bgee; A2ADY9; -.
DR   Genevestigator; A2ADY9; -.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR021109; Peptidase_aspartic.
DR   InterPro; IPR009007; Peptidase_aspartic_catalytic.
DR   InterPro; IPR019103; Peptidase_aspartic_euk-pred.
DR   InterPro; IPR000626; Ubiquitin.
DR   InterPro; IPR019955; Ubiquitin_supergroup.
DR   Gene3D; G3DSA:2.40.70.10; Pept_Aspartc_cat; 1.
DR   Pfam; PF09668; Asp_protease; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SUPFAM; SSF50630; Pept_Aspartic; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    399       Protein DDI1 homolog 2.
FT                                /FTId=PRO_0000287091.
FT   DOMAIN        1     81       Ubiquitin-like.
FT   MOD_RES     120    120       Phosphoserine.
FT   MOD_RES     121    121       Phosphoserine.
FT   MOD_RES     128    128       Phosphoserine.
FT   MOD_RES     194    194       Phosphoserine (By similarity).
SQ   SEQUENCE   399 AA;  44591 MW;  25FBCEB27CC886DA CRC64;
     MLLTVYCVRR DLSEVTFSLQ VDADFELHNF RALCELESGI PAAESQIVYA ERPLTDNHRS
     LASYGLKDGD VVILRQKENA DPRPAVQFSN LPRIDFSSIA VPGTSNPQQR QLPRTQAQHS
     SPGEMASSPQ GLDNPALLRD MLLANPHELS LLKERNPPLA EALLSGDLEK FSRVLVEQQQ
     DRARREQERI RLFSADPFDL EAQAKIEEDI RQQNIEENMT IAMEEAPESF GQVAMLYINC
     RVNGHPVKAF VDSGAQMTIM SQACAERCNI MRLVDRRWAG IAKGVGTQKI IGRVHLAQVQ
     IEGDFLACSF SILEEQPMDM LLGLDMLKRH QCSIDLKKNV LVIGTTGSQT TFLPEGELPE
     CARLAYGTGR EDIRPEEIAD QELAEAIQKS AEDAERQKP
//
ID   A2AEE7_MOUSE            Unreviewed;      2919 AA.
AC   A2AEE7;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 52.
DE   SubName: Full=Cadherin EGF LAG seven-pass G-type receptor 2;
GN   Name=Celsr2; ORFNames=RP23-27B23.1-001, mCG_4064;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Clark G.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Garner P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Contains 1 GPS domain.
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DR   EMBL; AL671899; CAM19472.1; -; Genomic_DNA.
DR   EMBL; AL672200; CAM19472.1; JOINED; Genomic_DNA.
DR   EMBL; AL672200; CAM22588.1; -; Genomic_DNA.
DR   EMBL; AL671899; CAM22588.1; JOINED; Genomic_DNA.
DR   EMBL; CH466607; EDL01967.1; -; Genomic_DNA.
DR   IPI; IPI00649043; -.
DR   RefSeq; NP_059088.2; NM_017392.3.
DR   UniGene; Mm.39728; -.
DR   ProteinModelPortal; A2AEE7; -.
DR   SMR; A2AEE7; 279-602, 758-919, 1269-1366, 1792-1970.
DR   STRING; A2AEE7; -.
DR   PRIDE; A2AEE7; -.
DR   Ensembl; ENSMUST00000090558; ENSMUSP00000088046; ENSMUSG00000068740.
DR   GeneID; 53883; -.
DR   KEGG; mmu:53883; -.
DR   CTD; 53883; -.
DR   MGI; MGI:1858235; Celsr2.
DR   HOVERGEN; HBG050887; -.
DR   InParanoid; A2AEE7; -.
DR   OMA; RSFPAHS; -.
DR   PhylomeDB; A2AEE7; -.
DR   NextBio; 310761; -.
DR   Bgee; A2AEE7; -.
DR   Genevestigator; A2AEE7; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   InterPro; IPR022624; DUF3497.
DR   InterPro; IPR006209; EGF.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR001881; EGF_Ca-bd.
DR   InterPro; IPR002049; EGF_laminin.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR001879; GPCR_2_extracellular_dom.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR000203; GPS_dom.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR012680; Laminin_G_2.
DR   InterPro; IPR001368; TNFR_Cys_rich_reg.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 9.
DR   Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 2.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF00028; Cadherin; 8.
DR   Pfam; PF12003; DUF3497; 1.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF00053; Laminin_EGF; 1.
DR   Pfam; PF02210; Laminin_G_2; 2.
DR   PRINTS; PR00205; CADHERIN.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   SMART; SM00112; CA; 9.
DR   SMART; SM00181; EGF; 5.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00180; EGF_Lam; 1.
DR   SMART; SM00303; GPS; 1.
DR   SMART; SM00008; HormR; 1.
DR   SMART; SM00282; LamG; 2.
DR   SMART; SM00208; TNFR; 1.
DR   SUPFAM; SSF49313; Cadherin; 9.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS00232; CADHERIN_1; 7.
DR   PROSITE; PS50268; CADHERIN_2; 9.
DR   PROSITE; PS00022; EGF_1; 6.
DR   PROSITE; PS01186; EGF_2; 4.
DR   PROSITE; PS50026; EGF_3; 6.
DR   PROSITE; PS01248; EGF_LAM_1; 1.
DR   PROSITE; PS50027; EGF_LAM_2; 1.
DR   PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE   3: Inferred from homology;
KW   Calcium; Cell membrane; EGF-like domain; G-protein coupled receptor;
KW   Membrane; Receptor; Repeat; Transducer; Transmembrane;
KW   Transmembrane helix.
SQ   SEQUENCE   2919 AA;  316986 MW;  A8F35C88C5808300 CRC64;
     MRSRAASAPL PTPLLPLLLL LLLLPPSPLL GDQVGPCRSL GSGGRSSSGA CAPVGWLCPA
     SASNLWLYTS RCRESGIELT GHLVPHHDGL RVWCPESGAH IPLPPSSEGC PWSCRLLGIG
     GHLSPQGTLT LPEEHPCLKA PRLRCQSCKL AQAPGLRAGE GSPEESLGGR RKRNVNTAPQ
     FQPPSYQATV PENQPAGTSV ASLRAIDPDE GEAGRLEYTM DALFDSRSNH FFSLDPITGV
     VTTAEELDRE TKSTHVFRVT AQDHGMPRRS ALATLTILVT DTNDHDPVFE QQEYKESLRE
     NLEVGYEVLT VRATDGDAPP NANILYRLLE GAGGSPSDAF EIDPRSGVIR TRGPVDREEV
     ESYKLTVEAS DQGRDPGPRS STAIVFLSVE DDNDNAPQFS EKRYVVQVRE DVTPGAPVLR
     VTASDRDKGS NALVHYSIMS GNARGQFYLD AQTGALDVVS PLDYETTKEY TLRIRAQDGG
     RPPLSNVSGL VTVQVLDIND NAPIFVSTPF QATVLESVPL GYLVLHVQAI DADAGDNARL
     EYSLAGVGHD FPFTINNGTG WISVAAELDR EEVDFYSFGV EARDHGTPAL TASASVSVTI
     LDVNDNNPTF TQPEYTVRLN EDAAVGTSVV TVSAVDRDAH SVITYQITSG NTRNRFSITS
     QSGGGLVSLA LPLDYKLERQ YVLAVTASDG TRQDTAQIVV NVTDANTHRP VFQSSHYTVN
     VNEDRPAGTT VVLISATDED TGENARITYF MEDSIPQFRI DADTGAVTTQ AELDYEDQVS
     YTLAITARDN GIPQKSDTTY LEILVNDVND NAPQFLRDSY QGSVYEDVPP FTSVLQISAT
     DRDSGLNGRV FYTFQGGDDG DGDFIVESTS GIVRTLRRLD RENVAQYVLR AYAVDKGMPP
     ARTPMEVTVT VLDVNDNPPV FEQDEFDVFV EENSPIGLAV ARVTATDPDE GTNAQIMYQI
     VEGNIPEVFQ LDIFSGELTA LVDLDYEDRP EYVLVIQATS APLVSRATVH VRLLDRNDNP
     PVLGNFEILF NNYVTNRSSS FPGGAIGRVP AHDPDISDSL TYSFERGNEL SLVLLNASTG
     ELRLSRALDN NRPLEAIMSV LVSDGVHSVT AQCSLRVTII TDEMLTHSIT LRLEDMSPER
     FLSPLLGLFI QAVAATLATP PDHVVVFNVQ RDTDAPGGHI LNVSLSVGQP PGPGGGPPFL
     PSEDLQERLY LNRSLLTAIS AQRVLPFDDN ICLREPCENY MRCVSVLRFD SSAPFIASSS
     VLFRPIHPVG GLRCRCPPGF TGDYCETEVD LCYSRPCGPH GRCRSREGGY TCLCLDGYTG
     EHCEASTHSG RCTPGVCKNG GTCVNLLVGG FKCDCPSGDF EKPFCQVTTR SFPARSFITF
     RGLRQRFHFT LALSFATKER NGLLLYNGRF NEKHDFVALE VIQEQVQLTF SAGESTTTVS
     PFVPGGVSDG QWHTVQLKYY NKPLLGQTGL PQGPSEQKVA VVSVDGCDTG VALRFGAMLG
     NYSCAAQGTQ GGSKKSLDLT GPLLLGGVPD LPESFPVRMR HFVGCMKDLQ VDSRHIDMAD
     FIANNGTVPG CPTKKIVCDS SICHNGGTCV NQWNAFSCEC PLGFGGKSCA QEMANPQRFL
     GSSLVAWHGL SLPISQPWHL SLMFRTRQAD GVLLQAVTRG RSTITLQLRA GHVVLSVEGT
     GLQASSLRLE PGRANDGDWH HAQLALGASG GPGHAILSFD YGQQKAEGNL GPRLHGLHLS
     NITVGGVPGP ASGVARGFRG CLQGVRVSET PEGISSLDPS RGESINVEPG CSWPDPCDSN
     PCPTNSYCSN DWDSYSCSCV LGYYGDNCTN VCDLNPCEHQ SVCTRKPNTP HGYICECLPN
     YLGPYCETRI DQPCPRGWWG HPTCGPCNCD VSKGFDPDCN KTSGECHCKE NHYRPPGSPT
     CLLCDCYPTG SLSRVCDPED GQCPCKPGVI GRQCDRCDNP FAEVTTNGCE VNYDSCPRAI
     EAGIWWPRTR FGLPAAAPCP KGSFGTAVRH CDEHRGWLPP NLFNCTSVTF SELKGFAERL
     QRNESGLDSG RSQRLALLLR NATQHTSGYF GSDVKVAYQL ATRLLAHESA QRGFGLSATQ
     DVHFTENLLR VGSALLDAAN KRHWELIQQT EGGTAWLLQH YEAYASALAQ NMRHTYLSPF
     TIVTPNIVIS VVRLDKGNFA GTKLPRYEAL RGERPPDLET TVILPESVFR EMPSMVRSAG
     PGEAQETEEL ARRQRRHPEL SQGEAVASVI IYHTLAGLLP HNYDPDKRSL RVPKRPVINT
     PVVSISVHDD EELLPRALDK PVTVQFRLLE TEERTKPICV FWNHSILVSG TGGWSARGCE
     VVFRNESHVS CQCNHMTSFA VLMDMSRREN GEILPLKTLT YVALGVTLAA LMLTFLFLTL
     LRALRSNQHG IRRNLTAALG LAQLVFLLGI NQADLPFACT VIAILLHFLY LCTFSWALLE
     ALHLYRALTE VRDVNASPMR FYYMLGWGVP AFITGLAVGL DPEGYGNPDF CWLSVYDTLI
     WSFAGPVAFA VSMSVFLYIL SARASCAAQR QGFEKKGPVS GLRSSFTVLL LLSATWLLAL
     LSVNSDTLLF HYLFAACNCV QGPFIFLSYV VLSKEVRKAL KFACSRKPSP DPALTTKSTL
     TSSYNCPSPY ADGRLYQPYG DSAGSLHSAS RSGKSQPSYI PFLLREESTL NPGQVPPGLG
     DPSGLFLEGQ AQQHDPDTDS DSDLSLEDDQ SGSYASTHSS DSEEEEEEAA FPGEQGWDSL
     LGPGAERLPL HSTPKDGGPG SGKVPWLGDF GTTTKENSGS GPLEERPREN GDALTREGSL
     GPLPGPSTQP HKGILKKKCL PTISEKSSLL RLPLEQGTGS SRGSSISEGS RHGPPPRPPP
     RQSLQEQLNG VMPVAMSIKA GTVDEDSSGS EFLFFNFLH
//
ID   A2AEG6_MOUSE            Unreviewed;       328 AA.
AC   A2AEG6;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 29.
DE   SubName: Full=Glycoprotein m6b;
DE   SubName: Full=Glycoprotein m6b, isoform CRA_g;
GN   Name=Gpm6b; ORFNames=RP23-239H22.1-006, mCG_7562;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Howden P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL671905; CAM18330.1; -; Genomic_DNA.
DR   EMBL; CH466571; EDL40740.1; -; Genomic_DNA.
DR   IPI; IPI00828221; -.
DR   RefSeq; NP_001171426.1; NM_001177955.1.
DR   UniGene; Mm.222320; -.
DR   STRING; A2AEG6; -.
DR   PRIDE; A2AEG6; -.
DR   Ensembl; ENSMUST00000112229; ENSMUSP00000107848; ENSMUSG00000031342.
DR   GeneID; 14758; -.
DR   KEGG; mmu:14758; -.
DR   CTD; 14758; -.
DR   MGI; MGI:107672; Gpm6b.
DR   HOVERGEN; HBG000096; -.
DR   InParanoid; A2AEG6; -.
DR   Bgee; A2AEG6; -.
DR   Genevestigator; A2AEG6; -.
DR   InterPro; IPR001614; Myelin_PLP.
DR   InterPro; IPR018237; Myelin_PLP_CS.
DR   PANTHER; PTHR11683; Myelin_PLP; 1.
DR   Pfam; PF01275; Myelin_PLP; 1.
DR   PRINTS; PR00214; MYELINPLP.
DR   SMART; SM00002; PLP; 1.
DR   PROSITE; PS00575; MYELIN_PLP_1; 1.
DR   PROSITE; PS01004; MYELIN_PLP_2; 1.
PE   4: Predicted;
SQ   SEQUENCE   328 AA;  36197 MW;  D5F7EE68C1F3AB37 CRC64;
     MKPAMETAAE ENTEQSQERK VNSRAEMEIG RYHWMYPGSK NHQYRPVPTL GDRAGPLSSP
     GCFECCIKCL GGVPYASLVA TILCFSGVAL FCGCGHVALA GTVAILEQHF STNTSDHALL
     SEVIQLMQYV IYGIASFFFL YGIILLAEGF YTTSAVKELH GEFKTTACGR CISGMFVFLT
     YVLGVAWLGV FGFSAVPVFM FYNIWSTCEV IKSPQSNGTS GVEQICVDVR QYGIIPWNAF
     PGKICGSALE NICNTNEFYM SYHLFIVACA GAGATVIALI HFLMILSSNW AYLKDASKMQ
     AYQDIKAKEE QELQDIQSRS KEQLNSYT
//
ID   A2AEV7_MOUSE            Unreviewed;       629 AA.
AC   A2AEV7;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 26.
DE   SubName: Full=Coiled-coil domain containing 120;
GN   Name=Ccdc120; ORFNames=RP23-109E24.5-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Grafham D.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testicle;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC139064; AAI39065.1; -; mRNA.
DR   EMBL; AL671995; CAM13591.1; -; Genomic_DNA.
DR   IPI; IPI00380690; -.
DR   RefSeq; NP_997085.2; NM_207202.2.
DR   UniGene; Mm.63342; -.
DR   PhosphoSite; A2AEV7; -.
DR   PRIDE; A2AEV7; -.
DR   Ensembl; ENSMUST00000033490; ENSMUSP00000033490; ENSMUSG00000031150.
DR   GeneID; 54648; -.
DR   KEGG; mmu:54648; -.
DR   CTD; 54648; -.
DR   MGI; MGI:1859619; Ccdc120.
DR   eggNOG; roNOG05362; -.
DR   HOGENOM; HBG507267; -.
DR   HOVERGEN; HBG080242; -.
DR   InParanoid; A2AEV7; -.
DR   OMA; RCYEVGQ; -.
DR   OrthoDB; EOG4CVG6P; -.
DR   PhylomeDB; A2AEV7; -.
DR   NextBio; 311500; -.
DR   Bgee; A2AEV7; -.
DR   Genevestigator; A2AEV7; -.
DR   InterPro; IPR021774; DUF3338.
DR   Pfam; PF11819; DUF3338; 1.
PE   1: Evidence at protein level;
SQ   SEQUENCE   629 AA;  67407 MW;  277CF22B3D090564 CRC64;
     MEVKGQLISS PTFTAPAALF GEAAPLVKSD RLRGLLDRQR ALQEALSVKL QELRKVCLQE
     AELTGQLPPE CPLEPGERPQ LVRRRPPAAR AYPPPHPNPA HHSLCPAEEL ALEALEREVS
     VQQQIAAAAR RLALAPDLNG EQRRRRRQVQ VDALRRLHEL EEQLRDFRAR LGLPVLQPLP
     LSAGALVNAQ GVCLGTRLAQ LSQEDVVLHS ESSSLSESGA SHDNEEPHSC FPLTERPSPP
     KAWDQFRAVS GGSPERRAPW KPPPSDIYGD LKSRRNSVAS PTSPTRSLPR SASSFEGRSV
     PATPVLTRGS GPRLCKPEGL HSRQWSGSQD SQMGFPRPDP ASDRASLFAA RTRRSNSSEA
     LLVDRAAAGG AGSPPAPLAP PAAGPPVCKS SEVLYERPQP VPSFSSRTTG PPDPPRAARP
     SSAAPASRGA PRLPTVCGDF LLDYPLDRGL PRGSGGAGWG ELLPAPEVPG PLSRRDGLLA
     MLPGPPPIYA ADGSSPLLRS KDPNTRAIRS KPSGLPPEAV EGLEVHPNPL LWMPPPTRIP
     PAGERGGHKN LALEGLRDWY IRNSGLAVGP QRRPMLPHVG PTHTPFLHAR CYEVGQSLYG
     PPSQAPLPHS RSFTAPPVSG RYGGAFTDG
//
ID   DOC11_MOUSE             Reviewed;        2073 AA.
AC   A2AF47; Q5KTP7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   RecName: Full=Dedicator of cytokinesis protein 11;
DE   AltName: Full=Activated Cdc42-associated guanine nucleotide exchange factor;
DE            Short=ACG;
DE   AltName: Full=Zizimin-2;
GN   Name=Dock11; Synonyms=Ziz2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CDC42, TISSUE
RP   SPECIFICITY, AND FUNCTION.
RC   TISSUE=Spleen;
RX   PubMed=15710388; DOI=10.1016/j.febslet.2005.01.006;
RA   Nishikimi A., Meller N., Uekawa N., Isobe K., Schwartz M.A.,
RA   Maruyama M.;
RT   "Zizimin2: a novel, DOCK180-related Cdc42 guanine nucleotide exchange
RT   factor expressed predominantly in lymphocytes.";
RL   FEBS Lett. 579:1039-1046(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CDC42, AND
RP   FUNCTION.
RX   PubMed=16968698; DOI=10.1074/jbc.M606248200;
RA   Lin Q., Yang W., Baird D., Feng Q., Cerione R.A.;
RT   "Identification of a DOCK180-related guanine nucleotide exchange
RT   factor that is capable of mediating a positive feedback activation of
RT   Cdc42.";
RL   J. Biol. Chem. 281:35253-35262(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1240, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Guanine nucleotide-exchange factor (GEF) that activates
CC       CDC42 by exchanging bound GDP for free GTP.
CC   -!- SUBUNIT: Interacts with CDC42.
CC   -!- TISSUE SPECIFICITY: Expressed in spleen, thymus, bone marrow and
CC       peripheral blood lymphocytes. Enriched in B-cells from germinal
CC       centers.
CC   -!- DOMAIN: The DHR-2 domain is necessary for the GEF activity.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- MISCELLANEOUS: 'Zizim' means 'spike' in Hebrew.
CC   -!- SIMILARITY: Belongs to the DOCK family.
CC   -!- SIMILARITY: Contains 1 DHR-1 (CZH-1) domain.
CC   -!- SIMILARITY: Contains 1 DHR-2 (CZH-2) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
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DR   EMBL; AB116935; BAD83670.1; -; mRNA.
DR   EMBL; AL672038; CAM20638.1; -; Genomic_DNA.
DR   EMBL; AL672023; CAM20638.1; JOINED; Genomic_DNA.
DR   EMBL; AL672023; CAM21480.1; -; Genomic_DNA.
DR   EMBL; AL672038; CAM21480.1; JOINED; Genomic_DNA.
DR   IPI; IPI00462949; -.
DR   RefSeq; NP_001009947.2; NM_001009947.3.
DR   UniGene; Mm.32873; -.
DR   ProteinModelPortal; A2AF47; -.
DR   SMR; A2AF47; 155-290, 640-820, 1613-2035.
DR   STRING; A2AF47; -.
DR   PhosphoSite; A2AF47; -.
DR   PRIDE; A2AF47; -.
DR   Ensembl; ENSMUST00000033419; ENSMUSP00000033419; ENSMUSG00000031093.
DR   GeneID; 75974; -.
DR   KEGG; mmu:75974; -.
DR   CTD; 75974; -.
DR   MGI; MGI:1923224; Dock11.
DR   GeneTree; ENSGT00600000084424; -.
DR   HOGENOM; HBG446568; -.
DR   HOVERGEN; HBG107819; -.
DR   InParanoid; A2AF47; -.
DR   OMA; YENVITQ; -.
DR   OrthoDB; EOG4SJ5CX; -.
DR   PhylomeDB; A2AF47; -.
DR   NextBio; 344361; -.
DR   Bgee; A2AF47; -.
DR   CleanEx; MM_DOCK11; -.
DR   Genevestigator; A2AF47; -.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0017048; F:Rho GTPase binding; IPI:MGI.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IDA:MGI.
DR   InterPro; IPR010703; DOCK.
DR   InterPro; IPR021816; DUF3398.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF06920; Ded_cyto; 1.
DR   Pfam; PF11878; DUF3398; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Guanine-nucleotide releasing factor; Phosphoprotein.
FT   CHAIN         1   2073       Dedicator of cytokinesis protein 11.
FT                                /FTId=PRO_0000299559.
FT   DOMAIN      165    272       PH.
FT   DOMAIN      641    879       DHR-1.
FT   DOMAIN     1509   2027       DHR-2.
FT   REGION       66    126       Interaction with activated CDC42.
FT   MOD_RES     158    158       Phosphoserine (By similarity).
FT   MOD_RES     161    161       Phosphoserine (By similarity).
FT   MOD_RES     248    248       Phosphotyrosine (By similarity).
FT   MOD_RES     329    329       Phosphoserine (By similarity).
FT   MOD_RES    1240   1240       Phosphoserine.
FT   CONFLICT   1608   1608       A -> T (in Ref. 1; BAD83670).
SQ   SEQUENCE   2073 AA;  237771 MW;  2907066969A6A8F8 CRC64;
     MAEVRKFTKR LSKPGTAAEL RQSVSEAVRG SVVLEKAKLV EPLDYENVIT QRKTQIYSDP
     LRDLLMFPME DISISVIGRQ RRTVQSTVPE DAEKRAQSLF VKECIKTYST DWHVVNYKYE
     DFSGDFRMLP CKSLRPEKIP NHVFEIDEDC EKDEDSSSLC SQKGGVIKQG WLHKANVNST
     ITVTMKVFKR RYFYLTQLPD GSYILNSYKD EKNSKESKGC IYLDACIDVV QCPKMRRHAF
     ELKMLDKYSH YLAAETEQEM EEWLIMLKKI IQINTDSLVQ EKKDTVEAIQ EEETSSQGKA
     ENIMASLERS MHPELMKYGR ETEQLNKLSR GDGRQNLFSF DSEVQRLDFS GIEPDVKPFE
     EKCNKRFMVN CHDLTFNILG HIGDNAKGPP TNVEPFFINL ALFDVKNNCK ISADFHVDLN
     PPSVREMLWG TSTQLSNDGN AKGFSPESLI HGIAESQLCY IKQGIFSVTN PHPEIFLVVR
     IEKVLQGNIT HCAEPYIKNS DPIKTAQKVH RTAKQVCSRL GQYRMPFAWA ARPIFKDVQG
     SLDLDGRFSP LYKQDSSKLS NEDILKLLSE YKKPEKTKLQ IIPGQLSITV ECVPVDLPNC
     ITSSYVPLKP FEKNCQNITV EVEEFVPEMT KYCYPFTIYK NHLYVYPLQL KYDSQKSFAK
     ARNIAVCVEF RDSDESDASA LKCIYGKPAG SVFTTNAYAV VSHHNQNPEF YDEIKIELPI
     HLHQKHHLLF TFYHVSCEIN TKGTTKKQDT VETPVGFAWV PLLKDGRVIT LEQQLPVSAN
     LPPGYLNVND AESRRQSNAD IKWVDGAKPL LKIKTHLEST IYTQDLHVHK FFHHCQLIQS
     GSKEVPGELI KYLKCLHAME IQVMIQFLPV ILMQLFRVLT NMTHEDDVPI NCTMVLLHIV
     SKCHEEGLES YLRSFIKYSF RPEKPSTLQA QLIHETLATT MIAILKQSAD FLAINKLLKY
     SWFFFEIIAK SMATYLLEEN KIKLPRGQRF PEAYHHVLHS LLLAIIPHVT IRYAEIPDES
     RNGNYSLASF LKRCLTLMDR GFVFNLINDY ISGFSPKDPK VLAEYKFEFL QTICNHEHYI
     PLNLPMAFAK PKLQRVQDSN LEYSLSDEYC KHHFLVGLLL RETSIALQDN YEIRYTAISV
     IKNLLIKHAF DTRYQHKNQQ AKIAQLYLPF VGLLLENIQR LAGRDTLYSC AAMPSSASRD
     EFPCGFVSPT NRGSLASDKD TAYGSFQNGH GIKREDSRGS LIPEGATGFP DPGSTSENTR
     QSSSRSSVSQ YNRLDQYEIR NLLMCYLYIV KMISEDTLLT YWNKVSPQEL INILVLLEVC
     LFHFRYMGKR NIARVHDAWL SKHFGIDRKS QTMPALRNRS GVMQARLQHL SSLESSFTLN
     HSSATTEADI FHQALLEGNT ATEVSLTVLD TISFFTQCFK NQLLNNDGHN PLMKKVFDIH
     LAFLKNGQSE VSLKHVFASL RSFISKFPSA FFKGRVNMCA AFCYEVLKCC TSKISSTRNE
     ASALLYLLMR NNFEYTKRKT FLRTHLQIII AVSQLIADVA LSGGSRFQES LFIINNFANS
     DRPMKATAFP TEVKDLTKRI RTVLMATAQM KEHEKDPEML IDLQYSLAKS YASTPELRKT
     WLDSMAKIHI KNGDFSEAAM CYVHVAALVA EFLHRKKLFP SGCSAFKKIT PNIDEEGAMK
     EDAGMMDVHY SEEVLLELLE QCVDGLWKAE RYEVISEISK LIIPIYEKRR EFEKLTQVYR
     TLHGAYTKIL EVMHTKKRLL GTFFRVAFYG QSFFEEEDGK EYIYKEPKLT GLSEISLRLV
     KLYGEKFGTE NVKIIQDSDK VNAKELDPKF AHIQVTYVKP YFDDKELTER KTEFERNHNI
     NRFVFEAPYT LSGKKQGCIE EQCKRRTILT TSNSFPYVKK RIPINCEQQV NLKPIDVATD
     EIKDKTAELH KLCSSVDVDM IQLQLKLQGC VSVQVNAGPL AYARAFLNES QANKYPPKKV
     NELKDMFRKF IQACSIALEL NERLIKEDQI EYHEGLKSNF RDMVKELSDI IHEQILQEDT
     MHSPWMNNTL HVFCAISGTS SNRGYGSPRY AEV
//
ID   A2AF53_MOUSE            Unreviewed;       350 AA.
AC   A2AF53;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-FEB-2011, entry version 26.
DE   SubName: Full=BC023829 protein;
DE   SubName: Full=Novel protein (Likely orthologe of human FAM11A family with sequence similarity 11, member A);
GN   Name=BC023829; Synonyms=RP23-403O11.9; ORFNames=RP23-403O11.9-002;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Whitehead S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC138670; AAI38671.1; -; mRNA.
DR   EMBL; BC145368; AAI45369.1; -; mRNA.
DR   EMBL; AL672026; CAM23469.1; -; Genomic_DNA.
DR   IPI; IPI00775778; -.
DR   UniGene; Mm.24569; -.
DR   Ensembl; ENSMUST00000114630; ENSMUSP00000110277; ENSMUSG00000073139.
DR   MGI; MGI:2448555; BC023829.
DR   GeneTree; ENSGT00390000008194; -.
DR   HOGENOM; HBG507246; -.
DR   HOVERGEN; HBG051528; -.
DR   InParanoid; A2AF53; -.
DR   OMA; TGVVITQ; -.
DR   PhylomeDB; A2AF53; -.
DR   Bgee; A2AF53; -.
DR   Genevestigator; A2AF53; -.
DR   InterPro; IPR019396; TM_Fragile-X-F-assoc.
DR   Pfam; PF10269; Tmemb_185A; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   350 AA;  40620 MW;  13FFC0BA9F8328B4 CRC64;
     MNLRGLFQDF NPSKFLIYAC LLLFSVLLAL RLDGIIQWSY WAVFAPIWLW KLMVIVGASV
     GTGVWARNPQ YRAEGETCVE FKAMLIAVGI HLLLLMFEVL VCDRIERGSH FWLLVFMPLF
     FVSPVSVAAC VWGFRHDRSL ELEILCSVNI LQFIFIALRL DKIIHWPWLV VCVPLWILMS
     FLCLVVLYYI VWSVLFLRSM DVIAEQRRTH ITMALSWMTI VVPLLTFEIL LVHKLDGHNA
     FSCIPIFVPL WLSLITLMAT TFGQKGGNHW WFGIRKDFCQ FLLEIFPFLR EYGNISYDLH
     HEDSEETEET PVPEPPKIAP MFRKKARVVI TQSPGKYVLP PPKLNIEMPD
//
ID   A2AFI8_MOUSE            Unreviewed;       647 AA.
AC   A2AFI8;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   08-MAR-2011, entry version 23.
DE   SubName: Full=RALBP1 associated Eps domain containing protein 2;
DE   SubName: Full=Reps2 protein;
GN   Name=Reps2; ORFNames=RP23-436I3.2-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Humphries M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Brown J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC145500; AAI45501.1; -; mRNA.
DR   EMBL; AL672039; CAM20008.1; -; Genomic_DNA.
DR   EMBL; AL672123; CAM20008.1; JOINED; Genomic_DNA.
DR   EMBL; AL672123; CAM24310.1; -; Genomic_DNA.
DR   EMBL; AL672039; CAM24310.1; JOINED; Genomic_DNA.
DR   IPI; IPI00265211; -.
DR   UniGene; Mm.442441; -.
DR   ProteinModelPortal; A2AFI8; -.
DR   SMR; A2AFI8; 20-126, 252-355.
DR   STRING; A2AFI8; -.
DR   Ensembl; ENSMUST00000112334; ENSMUSP00000107953; ENSMUSG00000040855.
DR   MGI; MGI:2663511; Reps2.
DR   HOVERGEN; HBG056372; -.
DR   OrthoDB; EOG45X7WG; -.
DR   Bgee; A2AFI8; -.
DR   Genevestigator; A2AFI8; -.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR000261; EPS15_homology.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   SMART; SM00027; EH; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS50031; EH; 2.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   647 AA;  70484 MW;  85303F400FEBD533 CRC64;
     MEVAAGGGCG AGPPLLLSDS EQQCYSELFA RCAGAASGGP GPGPPEATRV APGTATAAAG
     PVADLFRASQ LPPETLHQIT ELCGAKRVGY FGPTQFYVAL KLIAAAQAGL PVRTESIKCE
     LPLPRFVMSK NDGEIRFGNP AELHGPKVQI PYLTTEKNSF KRMDNEDKQE TQSPTMSPLA
     SPPSSPPHYQ RVSLSHGYSK LRSGTEQMHP APYERQPIGQ PEGPSSEGPG AKPFRRQASL
     IRSFSVEREP QENNSNYPDE PWRITEEQRE YYVNQFRSLQ PDPSSFISGS VAKNFFTKSK
     LSIPELSYIW ELSDADCDGA LTLSEFCAAF HLIVARKNGY PLPEGLPPTL QPEYLQAAFP
     KSKWECAIFD SYSESMPANQ QSCDLNRMEK TSVKDVADFP VPTQDVTTAD DKQALKSTVN
     ESLPKDVSED TATSKDYNSL KARPRSRSYS STSIEEAMKR GEDPPTPPPR PQKTHSRASS
     LDLNKVFLPS APAANSGLLP PPPALPPRPC PTQSEPVSEA DLHSQLNRAP SQAAESSPTK
     MDAPHAQPPS KPIRRKFRPE NQTTESQEPA AAVGGAVSAA MVKPHPTVQK QSSKQKKAIQ
     TAIRKNKEAN AVLARLNSEL QQQLKEVHQE RIALENQLEQ LRPVTVL
//
ID   FRPD4_MOUSE             Reviewed;        1320 AA.
AC   A2AFR3; B9EIG4; Q3UHE4; Q3UHI9; Q80U41;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   RecName: Full=FERM and PDZ domain-containing protein 4;
DE   AltName: Full=PDZ domain-containing protein 10;
DE   AltName: Full=PSD-95-interacting regulator of spine morphogenesis;
DE            Short=Preso;
GN   Name=Frmpd4; Synonyms=Gm196, Kiaa0316, Pdzd10, Pdzk10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 523-1320.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1250, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=19118189; DOI=10.1523/JNEUROSCI.3112-08.2008;
RA   Lee H.W., Choi J., Shin H., Kim K., Yang J., Na M., Choi S.Y.,
RA   Kang G.B., Eom S.H., Kim H., Kim E.;
RT   "Preso, a novel PSD-95-interacting FERM and PDZ domain protein that
RT   regulates dendritic spine morphogenesis.";
RL   J. Neurosci. 28:14546-14556(2008).
CC   -!- FUNCTION: Positive regulator of dendritic spine morphogenesis and
CC       density (By similarity). Required for the maintenance of
CC       excitatory synaptic transmission. Binds phosphatidylinositol-4,5-
CC       bisphosphate (By similarity).
CC   -!- SUBUNIT: Interacts (via C-terminus) with DLG1, DLG2, DLG3 and
CC       DLG4/PSD95 (By similarity). Interacts (via N-terminus) with
CC       ARHGEF7; the interaction is mediated by the PDZ domain (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=A2AFR3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2AFR3-2; Sequence=VSP_028581;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=A2AFR3-3; Sequence=VSP_028582;
CC   -!- TISSUE SPECIFICITY: Expressed in various regions of the brain,
CC       including cortex, hipppocampus, cerebellum, olfactory bulb and
CC       medial habenular nucleus.
CC   -!- DOMAIN: The FERM domain mediates the interaction with
CC       phosphatidylinositol-4,5-bisphosphate (By similarity).
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 WW domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65526.1; Type=Erroneous translation; Note=Wrong choice of CDS;
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DR   EMBL; AK147370; BAE27868.1; -; mRNA.
DR   EMBL; AK147440; BAE27913.1; -; mRNA.
DR   EMBL; AL807744; CAM16366.1; -; Genomic_DNA.
DR   EMBL; AL807773; CAM16366.1; JOINED; Genomic_DNA.
DR   EMBL; BX546498; CAM16366.1; JOINED; Genomic_DNA.
DR   EMBL; BX546498; CAM17768.1; -; Genomic_DNA.
DR   EMBL; AL807744; CAM17768.1; JOINED; Genomic_DNA.
DR   EMBL; AL807773; CAM17768.1; JOINED; Genomic_DNA.
DR   EMBL; BX546498; CAM17769.1; -; Genomic_DNA.
DR   EMBL; AL807773; CAM17769.1; JOINED; Genomic_DNA.
DR   EMBL; BX546498; CAM17770.1; -; Genomic_DNA.
DR   EMBL; AL672186; CAM17770.1; JOINED; Genomic_DNA.
DR   EMBL; AL807773; CAM17770.1; JOINED; Genomic_DNA.
DR   EMBL; AL807773; CAM18047.1; -; Genomic_DNA.
DR   EMBL; AL807744; CAM18047.1; JOINED; Genomic_DNA.
DR   EMBL; BX546498; CAM18047.1; JOINED; Genomic_DNA.
DR   EMBL; AL807773; CAM18048.1; -; Genomic_DNA.
DR   EMBL; BX546498; CAM18048.1; JOINED; Genomic_DNA.
DR   EMBL; AL807773; CAM18049.1; -; Genomic_DNA.
DR   EMBL; AL672186; CAM18049.1; JOINED; Genomic_DNA.
DR   EMBL; BX546498; CAM18049.1; JOINED; Genomic_DNA.
DR   EMBL; AL672186; CAM24062.1; -; Genomic_DNA.
DR   EMBL; AL807773; CAM24062.1; JOINED; Genomic_DNA.
DR   EMBL; BX546498; CAM24062.1; JOINED; Genomic_DNA.
DR   EMBL; BC139429; AAI39430.1; -; mRNA.
DR   EMBL; AK122244; BAC65526.1; ALT_SEQ; Transcribed_RNA.
DR   IPI; IPI00653851; -.
DR   IPI; IPI00831201; -.
DR   IPI; IPI00831313; -.
DR   RefSeq; NP_001028502.1; NM_001033330.2.
DR   UniGene; Mm.426168; -.
DR   ProteinModelPortal; A2AFR3; -.
DR   SMR; A2AFR3; 33-66, 74-160, 204-524.
DR   PhosphoSite; A2AFR3; -.
DR   PRIDE; A2AFR3; -.
DR   Ensembl; ENSMUST00000112149; ENSMUSP00000107777; ENSMUSG00000049176.
DR   GeneID; 333605; -.
DR   KEGG; mmu:333605; -.
DR   CTD; 333605; -.
DR   MGI; MGI:3042378; Frmpd4.
DR   eggNOG; roNOG07401; -.
DR   HOVERGEN; HBG106593; -.
DR   OrthoDB; EOG461438; -.
DR   Bgee; A2AFR3; -.
DR   CleanEx; MM_FRMPD4; -.
DR   Genevestigator; A2AFR3; -.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0051835; P:positive regulation of synapse structural plasticity; ISS:UniProtKB.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS00660; FERM_1; FALSE_NEG.
DR   PROSITE; PS00661; FERM_2; FALSE_NEG.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; FALSE_NEG.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell projection; Lipid-binding; Phosphoprotein.
FT   CHAIN         1   1320       FERM and PDZ domain-containing protein 4.
FT                                /FTId=PRO_0000307133.
FT   DOMAIN       33     66       WW.
FT   DOMAIN       78    155       PDZ.
FT   DOMAIN      204    519       FERM.
FT   MOD_RES    1250   1250       Phosphoserine.
FT   VAR_SEQ       1     40       Missing (in isoform 2).
FT                                /FTId=VSP_028581.
FT   VAR_SEQ       1     14       MDVFSFVKIPKLSS -> MRSHSC (in isoform 3).
FT                                /FTId=VSP_028582.
SQ   SEQUENCE   1320 AA;  144978 MW;  B8E9FE340BBF7475 CRC64;
     MDVFSFVKIP KLSSHRTKSS GWPPPSGTWG LNQVPPYGWE MMTNRDGRDY FINHMTQAIP
     FDDPRFDSCQ IIPPAPRKVE MRRDPVLGFG FVAGSEKPVV VRSVTPGGPS EGKLIPGDQI
     VMINDEAVSA APRERVIDLV RSCKESILLT VIQPYPSPKS AFISAAKKAR LKSNPVKVRF
     SEEVIINGQV SETVKDNSLL FMPNVLKVYL ENGQTKSFRF DCSTSIKDVI LTLQEKLSIK
     GIEHFSLMLE QRIEGAGTKL LLLHEQETLT QVTQRPSSHK MRCLFRISFV PKDPIDLLRR
     DPVAFEYLYV QSCNDVVQER FGPELKYDIA LRLAALQMYI ATVTTKQTQK ISLKYIEKEW
     GLETFLPSAV LQSMKEKNIK KALSHLVKAN QNLVPPGKKL SALQAKVHYL KFLSDLRLYG
     GRVFKATLVQ AEKRSEVTLL VGPRYGISHV INTKTNLVAL LADFSHVNRI EMFTEEESLV
     RVELHVLDVK PITLLMESSD AMNLACLTAG YYRLLVDSRR SIFNMANKKN AGTQDTGSEN
     KGKHNLLGPD WNCMPQMTTF IGEGEQEAQI TYIDSKQKTV EMTDSTLCPK EHRHLYIDNS
     YSSDELNQPL TQPGDAPCEA DYRSLAQRSL LTLSGPDTLK KAQESPRGAK VSFIFGDLAL
     DDGMSPPTIG YERMLEENPE MLEKQRNLYI SSANDMKNLD LTPDTDSIQF VANSVYANIG
     DVKNFEAPEG IEEPLLHDIC YAENTDDAED EDEVSCEEDL VVGEMNQPAI LDLSGSSDDI
     IDLTTLPPPE GDDNEDDFLL RSLNMAIAAP PPGFRDSSDE EDTQSQATSF HEDKEQGSSL
     QNEEIPVSLI DAVPTSAEGK CEKGLDPAVV STLEALEALS EEQQKSENSG VAILRAYSPE
     SSSDSGNETN SSEMTEGSEL AAAQKQSESL SRMFLATHEG YHPLAEEQTE FPTSKAPSVG
     LPPKSSHGLA ARPATDLPPK VVPSKQILHS DHMEMEPETM ETKSVTDYFS KLHMGSVAYS
     CTSKRKSKLP EGEGKSPLSG NIPGKKQQGT KIAEIEEDTK GKAGTVSSRD NPHLSTFNLE
     RTAFRKDSQR WYVASDGGVV EKSGMEAPAM KVFPRGPGLG NREAEGKEDG TVEGGADDAS
     VLGQGDRFLT DMACVASAKD LDNPEDTDSP SCDHATKLSE AEDNVARLCD YHLAKRMSSL
     QSEGHFSLQS SQGSSVDTGC GPGSSSSACA TPVESPLCPS MGKHMIPDAS GKGGRYISPE
     ERAPGHPNHG ATFEELHPQT EGMCPRMTVP ALHTAINADP LFGTLRDGCH RLPKIKETTV
//
ID   A2AG46_MOUSE            Unreviewed;       276 AA.
AC   A2AG46;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 22.
DE   SubName: Full=Melanoma antigen, family D, 2;
DE   Flags: Fragment;
GN   Name=Maged2; ORFNames=RP23-448K19.1-006;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Humphries M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL672282; CAM24640.1; -; Genomic_DNA.
DR   IPI; IPI00654377; -.
DR   UniGene; Mm.22575; -.
DR   STRING; A2AG46; -.
DR   Ensembl; ENSMUST00000026302; ENSMUSP00000026302; ENSMUSG00000025268.
DR   Ensembl; ENSMUST00000112699; ENSMUSP00000108319; ENSMUSG00000025268.
DR   Ensembl; ENSMUST00000112700; ENSMUSP00000108320; ENSMUSG00000025268.
DR   Ensembl; ENSMUST00000112702; ENSMUSP00000108322; ENSMUSG00000025268.
DR   Ensembl; ENSMUST00000143843; ENSMUSP00000119088; ENSMUSG00000025268.
DR   MGI; MGI:1933391; Maged2.
DR   eggNOG; roNOG06475; -.
DR   HOVERGEN; HBG102959; -.
DR   InParanoid; A2AG46; -.
DR   OrthoDB; EOG4R23V1; -.
DR   Bgee; A2AG46; -.
DR   Genevestigator; A2AG46; -.
DR   InterPro; IPR002190; MAGE.
DR   PANTHER; PTHR11736; MAGE; 1.
PE   4: Predicted;
FT   NON_TER     276    276
SQ   SEQUENCE   276 AA;  29208 MW;  622C6C31A4FFE432 CRC64;
     MSDTSESGAD PARSQGKASE KDSGSVMQDL LTVTQNLEVS ETPKAEKAPE VSEAAKAPKA
     SGNPKATEVS KAPEASEAAA TQASPTTQLS ETQVLATENK SPAADTKTQK SDLQAMTMPT
     TPTKKVSCGT DPKVNTKAPE TEAPASQAGT DEPEPEGTAV QVQENQDTRP KVKAKNTQKG
     KHPDGEEDGN SDQSQASEAT GGRRVSKALM ASMARRASRG PIAFWARRAS RTRLAAWARR
     ALLSLRSPRA RRGKARRRAA KLQSSQEPEA PPPRDV
//
ID   MA7D2_MOUSE             Reviewed;         781 AA.
AC   A2AG50; A2AG54; Q8BLE6; Q8BMQ4; Q9D2A4;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 29.
DE   RecName: Full=MAP7 domain-containing protein 2;
GN   Name=Map7d2; Synonyms=Mtap7d2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Pituitary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=A2AG50-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2AG50-2; Sequence=VSP_028494, VSP_028495;
CC       Name=3;
CC         IsoId=A2AG50-3; Sequence=VSP_028494, VSP_028495, VSP_028496,
CC                                  VSP_028497;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the MAP7 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC26896.1; Type=Frameshift; Positions=23, 92, 175;
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DR   EMBL; AK019929; BAB31923.1; -; mRNA.
DR   EMBL; AK030316; BAC26896.1; ALT_FRAME; mRNA.
DR   EMBL; AK045412; BAC32351.1; -; mRNA.
DR   EMBL; AL672284; CAM23334.1; -; Genomic_DNA.
DR   EMBL; AL672284; CAM23337.1; -; Genomic_DNA.
DR   EMBL; AL672284; CAM23338.1; -; Genomic_DNA.
DR   IPI; IPI00459177; -.
DR   IPI; IPI00808096; -.
DR   IPI; IPI00830556; -.
DR   RefSeq; NP_001074593.1; NM_001081124.1.
DR   UniGene; Mm.160079; -.
DR   PhosphoSite; A2AG50; -.
DR   PRIDE; A2AG50; -.
DR   Ensembl; ENSMUST00000058145; ENSMUSP00000053095; ENSMUSG00000041020.
DR   Ensembl; ENSMUST00000112471; ENSMUSP00000108090; ENSMUSG00000041020.
DR   GeneID; 78283; -.
DR   KEGG; mmu:78283; -.
DR   CTD; 78283; -.
DR   MGI; MGI:1917474; Mtap7d2.
DR   HOGENOM; HBG716315; -.
DR   HOVERGEN; HBG055348; -.
DR   InParanoid; A2AG50; -.
DR   OMA; KQTEPPM; -.
DR   OrthoDB; EOG4TF0MP; -.
DR   NextBio; 348613; -.
DR   Bgee; A2AG50; -.
DR   CleanEx; MM_MTAP7D2; -.
DR   Genevestigator; A2AG50; -.
DR   InterPro; IPR008604; E-MAP-115.
DR   PANTHER; PTHR15073; E-MAP-115; 1.
DR   Pfam; PF05672; MAP7; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Phosphoprotein.
FT   CHAIN         1    781       MAP7 domain-containing protein 2.
FT                                /FTId=PRO_0000306810.
FT   COILED       73    168       Potential.
FT   MOD_RES     248    248       Phosphoserine.
FT   MOD_RES     699    699       Phosphoserine (By similarity).
FT   MOD_RES     702    702       Phosphoserine (By similarity).
FT   MOD_RES     770    770       Phosphoserine (By similarity).
FT   VAR_SEQ       1    151       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_028494.
FT   VAR_SEQ     182    214       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_028495.
FT   VAR_SEQ     480    480       L -> M (in isoform 3).
FT                                /FTId=VSP_028496.
FT   VAR_SEQ     481    781       Missing (in isoform 3).
FT                                /FTId=VSP_028497.
SQ   SEQUENCE   781 AA;  86050 MW;  06BBD409721DE9B1 CRC64;
     MERSGGNGGG GGGGGGGGGG YGGSGGGGGG AGVPSEGAAK GLSLLLAKSA EAASGRASQS
     TPRSAGMDGF LKSDERQRLA KERREEREKC LAAREQQILE KQKRAKLQYE KQIEERWRKL
     EEQRQREDQK RAAVEEKRKQ KLREEEERLE AMMRRSLERT QQLELKKKCS WAGSPGPGGR
     DGESENTPPL PLTLATSTPP LDTGTTTAAA ESTNACDKLS TSTMNLPKQT ESPMSKHLSS
     STVAISYSPD RALGSPLKSS YKSSPTRTTE KKKNTPISAM GDAGKGAMAG GEPSQMEKMK
     KGRVATSAAS GGHGSPLRRC EPPEDISKRL SSPVKSKITS KTYPQSPKTA KPTYLGSPVK
     YYFPPIANEE TPKKKAEKEK RNKEKEGAPG QQSTVLPREE SLEKRMADKY ATEKYVADKH
     ATEKHSAPGG KAEHSAGKPT AGTTDAGEAA KILAEKRRQA RLQKEQEEQE RLEKEERERL
     EKEELKRKAE EERLRIEMAY KREQEKKRQE EEEKRKAEEK AKEKAEEELL SKEKQEKEKQ
     EQEKKEKAMI EKQKEAAEAK AQDAAKQMRL EREQIMLQIE QERLERKKRI DEIMKRTRKS
     DASLEVKKED PKVELQPPPD VENKANKAKP VVPNKIEINV LNTCQKVSGS ERAAPETFPQ
     DIFSTGLKPV GGPVHLDVLD GKSNSLDDST EDVQSMDVSP VSKEELISIP EFSPVSEMIP
     GMSLDQNGTG NARALQDILD FTGPPAFPKK SSENLSLDDC NKNLIEGFNS PGQETTLNTF
     C
//
ID   CX023_MOUSE             Reviewed;         752 AA.
AC   A2AG58; A2AG56; A2AG57; Q3UM32; Q8BRL2;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 29.
DE   RecName: Full=Uncharacterized protein CXorf23 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex, and Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A2AG58-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2AG58-2; Sequence=VSP_025460;
CC         Note=No experimental confirmation available. Ref.1 (BAE26266)
CC         sequence is in conflict in position: 657:Y->C;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM23340.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK044001; BAC31733.1; -; mRNA.
DR   EMBL; AK145159; BAE26266.1; -; mRNA.
DR   EMBL; AL672284; CAM23340.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL672284; CAM23341.1; -; Genomic_DNA.
DR   EMBL; AL672284; CAM23342.1; -; Genomic_DNA.
DR   IPI; IPI00381415; -.
DR   IPI; IPI00831175; -.
DR   RefSeq; NP_001028644.2; NM_001033472.2.
DR   UniGene; Mm.296254; -.
DR   PhosphoSite; A2AG58; -.
DR   PRIDE; A2AG58; -.
DR   Ensembl; ENSMUST00000057180; ENSMUSP00000051031; ENSMUSG00000044150.
DR   Ensembl; ENSMUST00000112464; ENSMUSP00000108083; ENSMUSG00000044150.
DR   GeneID; 382252; -.
DR   KEGG; mmu:382252; -.
DR   MGI; MGI:2685992; A830080D01Rik.
DR   GeneTree; ENSGT00530000063211; -.
DR   HOGENOM; HBG283604; -.
DR   HOVERGEN; HBG101041; -.
DR   InParanoid; A2AG58; -.
DR   OMA; PEDRDFR; -.
DR   OrthoDB; EOG4J117N; -.
DR   NextBio; 403185; -.
DR   Bgee; A2AG58; -.
DR   CleanEx; MM_A830080D01RIK; -.
DR   Genevestigator; A2AG58; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Mitochondrion; Phosphoprotein.
FT   CHAIN         1    752       Uncharacterized protein CXorf23 homolog.
FT                                /FTId=PRO_0000287435.
FT   MOD_RES      15     15       Phosphoserine (By similarity).
FT   MOD_RES      17     17       Phosphoserine (By similarity).
FT   MOD_RES      78     78       Phosphoserine (By similarity).
FT   MOD_RES      80     80       Phosphoserine (By similarity).
FT   VAR_SEQ     597    752       NHQSPSFSKVKTIRADGFQKPPHFIKSNFRKFIQKPYINYT
FT                                MQRKDAIDQKIFRVEENHQNRRGSKGSFKNFLGGRFQPHYK
FT                                SHLVQKSMYIQAKYQRLRFAGPRGFITNKFRNRFLRKKKEY
FT                                PVLPRTNNLELLQVEPTLYEDLTEHLIFVRNWN -> TILC
FT                                REKMPLIRRYLELRKIIRTEEALKDLLRTFWVADSSLIINH
FT                                TWYRRACIFRLNTSAYGLLDQEDLLPINSETDF (in
FT                                isoform 2).
FT                                /FTId=VSP_025460.
FT   CONFLICT    166    166       K -> Q (in Ref. 1; BAE26266).
FT   CONFLICT    392    392       S -> N (in Ref. 1; BAE26266).
FT   CONFLICT    591    591       A -> T (in Ref. 1; BAE26266).
SQ   SEQUENCE   752 AA;  90111 MW;  85DFCD631B080798 CRC64;
     MARSRSRSPR WKQRSLSPQS RNFEYHEERH FHGHYDPEYR HDQQRPFTWR MDDEKHGQNK
     PRIPPRVNSY HRSYVNRSPS PNVKPVEKFD TYKPHQEYFP GRGDDDRRSQ YMPTYTESAA
     TYMEHERDCY IPTVQGRYTP DDHRGRGRGS GRGEKPPQMS LGKPPKMSLG KPPQMSLADS
     LRFKEKWHED ELRHQRVQEE SYPQSPRRGS EDFGTRNPFQ KRYPEDHDFR KYGYTSKRPT
     DAARYENRDP ARIPKWKPEH SFLPFQEKKE EWSFGAQGHR YTEREYPERS STTRVSYDYR
     HKHHKLSESE QDFPDGRFHK HLKEEDRKYS SIKAPANREL DCFSTTRGRE IENEQINGPF
     YLYNKNSVSY NHTNIKDADL EPCNDKWKKK ISKEDCRKEN ASFSKQFDTS PKPEEKCYSL
     IKKKPLSVKV DRNKTDTFRS TSRYSAERQI SHDLVAIGKT SDNFHPVFQH LDSTQNPENK
     PTEEFAQEII TLIHKVKADS FVTPDITLNE RFSRIKNRQD ADFNQTKSNS DPEFHRRIDM
     SLDDFQNKYT MVYEPDKTLV KVIEPNDLRH DIERRRKERL QNEDENIFHM ASPTERNHQS
     PSFSKVKTIR ADGFQKPPHF IKSNFRKFIQ KPYINYTMQR KDAIDQKIFR VEENHQNRRG
     SKGSFKNFLG GRFQPHYKSH LVQKSMYIQA KYQRLRFAGP RGFITNKFRN RFLRKKKEYP
     VLPRTNNLEL LQVEPTLYED LTEHLIFVRN WN
//
ID   A2AGC7_MOUSE            Unreviewed;       920 AA.
AC   A2AGC7;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 39.
DE   SubName: Full=WD repeat domain 47;
GN   Name=Wdr47; ORFNames=RP23-128G10.4-001, mCG_4074;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Corby N.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 CTLH domain.
CC   -!- SIMILARITY: Contains 1 LisH domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AL683823; CAM14496.1; -; Genomic_DNA.
DR   EMBL; CH466607; EDL01977.1; -; Genomic_DNA.
DR   IPI; IPI00890345; -.
DR   RefSeq; NP_852065.2; NM_181400.3.
DR   UniGene; Mm.285968; -.
DR   ProteinModelPortal; A2AGC7; -.
DR   SMR; A2AGC7; 598-917.
DR   Ensembl; ENSMUST00000051145; ENSMUSP00000057482; ENSMUSG00000040389.
DR   GeneID; 99512; -.
DR   KEGG; mmu:99512; -.
DR   NMPDR; fig|10090.3.peg.8828; -.
DR   CTD; 99512; -.
DR   MGI; MGI:2139593; Wdr47.
DR   eggNOG; roNOG14515; -.
DR   HOVERGEN; HBG058798; -.
DR   InParanoid; A2AGC7; -.
DR   OMA; THDASNI; -.
DR   NextBio; 353995; -.
DR   Bgee; A2AGC7; -.
DR   Genevestigator; A2AGC7; -.
DR   InterPro; IPR006595; CTLH_C.
DR   InterPro; IPR006594; LisH_dimerisation.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 6.
DR   SMART; SM00668; CTLH; 1.
DR   SMART; SM00667; LisH; 1.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS50897; CTLH; 1.
DR   PROSITE; PS50896; LISH; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   4: Predicted;
KW   Repeat; WD repeat.
SQ   SEQUENCE   920 AA;  102312 MW;  401F22FFC00951AA CRC64;
     MTAEETVNVK EVEIIKLILD FLNSKKLHIS MLALEKESGV INGLFSDDML FLRQLILDGQ
     WDEVLQFIQP LECMEKFDKK RFRYIILKQK FLEALCVNNA MSAEDEPQHL EFTMQEAVQC
     LHALEEYCPS KDDYSKLCLL LTLPRLTNHA EFKDWNPSTA RVHCFEEVCV MVAEFIPADR
     KLSEAGFKAS NNRLFQLVMK GLLYECCVEF CQSKATGEEI TESEVLLGID LLCGNGCDDL
     DLSLLSWLQN LPSSVFSCAF EQKMLNIHVD KLLKPTKAAY ADLLTPLISK LSPYPSSPMR
     RPQSADAYMT RSLNPALDGL TCGLTSHDKR ISDLGNKTSP MSHSFANFHY PGVQNLSRSL
     MLENTECHSI YEESPERSDT PVEAQQPVSS EAMCQGSGLE KEPANGAQNP VPAKQEKNEL
     RDSTEQFQEY YRQRLRYQQH LEQKEQQRQM YQQMLLEGGV NQEDGPDQQQ NLTEQFLNRS
     IQKLGELNIG MDSLGNEVPV LNQQCSGSKN NGSNNSSVTS FSTPPQDSSQ RLIHDTANIH
     TSTPRNPGST NHIPFHEDSP CGSQNSSEHS VIKPSPGDSS GNLSRSKGEE DDKSKKQFVC
     INTLEDTQAV RAVAFHPSGS LYAVGSNSKT LRVCAYPEKM DASAHDNPKQ PVVRFKRNKH
     HKGSIYCVAW SPCGQLLATG SNDKYVKVLP FNAETCNATG PDLEFSMHDG TIRDLAFMEG
     PESGGAILIS AGAGDCNIYT TDCQRGQGLH ALSGHTGHIL ALYTWSGWMI ASGSQDKTVR
     FWDLRVPSCV RVVGTTFHGT GSAVASVAVD PSGRLLATGQ EDSSCMLYDI RGGRMVQSYH
     PHSSDVRSVR FSPGAHYLLT GSYDMKIKVT DLQGDLTKQL PLMVVGEHKD KVIQCRWHTQ
     DLSFLSSSAD RTVTLWTYSG
//
ID   MED12_MOUSE             Reviewed;        2190 AA.
AC   A2AGH6; A2AGH7; O88542; Q571H3; Q6PGB4; Q6PGD8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 12;
DE   AltName: Full=Mediator complex subunit 12;
DE   AltName: Full=OPA-containing protein;
DE   AltName: Full=Thyroid hormone receptor-associated protein complex 230 kDa component;
DE            Short=Trap230;
DE   AltName: Full=Trinucleotide repeat-containing gene 11 protein;
GN   Name=Med12; Synonyms=Kiaa0192, Mopa, Tnrc11, Trap230;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 33-2190 (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 33-2190 (ISOFORM 2).
RX   MEDLINE=98368120; PubMed=9702738; DOI=10.1038/sj.mp.4000442;
RA   Philibert R.A., King B.H., Cook E.H., Lee Y.-H., Stubblefield B.,
RA   Damschroder-Williams P., Dea C., Palotie A., Tengstrom C.,
RA   Martin B.M., Ginns E.I.;
RT   "Association of an X-chromosome dodecamer insertional variant allele
RT   with mental retardation.";
RL   Mol. Psychiatry 3:303-309(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1045-2190 (ISOFORM 1).
RC   TISSUE=Spleen;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the Mediator complex, a coactivator
CC       involved in the regulated transcription of nearly all RNA
CC       polymerase II-dependent genes. Mediator functions as a bridge to
CC       convey information from gene-specific regulatory proteins to the
CC       basal RNA polymerase II transcription machinery. Mediator is
CC       recruited to promoters by direct interactions with regulatory
CC       proteins and serves as a scaffold for the assembly of a functional
CC       preinitiation complex with RNA polymerase II and the general
CC       transcription factors. This subunit may specifically regulate
CC       transcription of targets of the Wnt signaling pathway and SHH
CC       signaling pathway (By similarity).
CC   -!- SUBUNIT: Component of the Mediator complex, which is composed of
CC       MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13,
CC       MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21,
CC       MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31,
CC       CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8
CC       subunits form a distinct module termed the CDK8 module. Mediator
CC       containing the CDK8 module is less active than Mediator lacking
CC       this module in supporting transcriptional activation. Individual
CC       preparations of the Mediator complex lacking one or more distinct
CC       subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and
CC       TRAP. Also interacts with CTNNB1 and GLI3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=A2AGH6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2AGH6-2; Sequence=VSP_029978, VSP_029979, VSP_029980;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=A2AGH6-3; Sequence=VSP_029977, VSP_029978;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 12 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC83164.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL683892; CAM24445.1; -; Genomic_DNA.
DR   EMBL; AL683892; CAM24446.1; -; Genomic_DNA.
DR   EMBL; BC057085; AAH57085.1; -; mRNA.
DR   EMBL; BC057119; AAH57119.1; -; mRNA.
DR   EMBL; AF071310; AAC83164.1; ALT_INIT; mRNA.
DR   EMBL; AK220216; BAD90141.1; -; mRNA.
DR   IPI; IPI00620781; -.
DR   IPI; IPI00625430; -.
DR   IPI; IPI00882323; -.
DR   RefSeq; NP_067496.2; NM_021521.2.
DR   UniGene; Mm.20873; -.
DR   STRING; A2AGH6; -.
DR   PhosphoSite; A2AGH6; -.
DR   PRIDE; A2AGH6; -.
DR   Ensembl; ENSMUST00000087948; ENSMUSP00000085260; ENSMUSG00000079487.
DR   Ensembl; ENSMUST00000087956; ENSMUSP00000085269; ENSMUSG00000079487.
DR   GeneID; 59024; -.
DR   KEGG; mmu:59024; -.
DR   CTD; 59024; -.
DR   MGI; MGI:1926212; Med12.
DR   HOGENOM; HBG357124; -.
DR   HOVERGEN; HBG052447; -.
DR   InParanoid; A2AGH6; -.
DR   OMA; TVDMQSN; -.
DR   OrthoDB; EOG4X3H0F; -.
DR   NextBio; 314592; -.
DR   Bgee; A2AGH6; -.
DR   Genevestigator; A2AGH6; -.
DR   GO; GO:0016592; C:mediator complex; IEA:InterPro.
DR   GO; GO:0016455; F:RNA polymerase II transcription mediator activity; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEA:InterPro.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR021990; Med12-LCEWAV.
DR   InterPro; IPR021989; Med12-PQL.
DR   InterPro; IPR019035; Mediator_Med12.
DR   Pfam; PF09497; Med12; 1.
DR   Pfam; PF12145; Med12-LCEWAV; 1.
DR   Pfam; PF12144; Med12-PQL; 1.
PE   2: Evidence at transcript level;
KW   Activator; Alternative splicing; Nucleus; Phosphoprotein; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN         1   2190       Mediator of RNA polymerase II
FT                                transcription subunit 12.
FT                                /FTId=PRO_0000312957.
FT   REGION     1617   2063       Interaction with CTNNB1 and GLI3 (By
FT                                similarity).
FT   MOD_RES     166    166       Phosphotyrosine (By similarity).
FT   MOD_RES     636    636       Phosphoserine (By similarity).
FT   MOD_RES     699    699       Phosphoserine (By similarity).
FT   MOD_RES     701    701       Phosphoserine (By similarity).
FT   MOD_RES    1259   1259       Phosphoserine (By similarity).
FT   MOD_RES    1270   1270       Phosphoserine (By similarity).
FT   VAR_SEQ       1   1321       Missing (in isoform 3).
FT                                /FTId=VSP_029977.
FT   VAR_SEQ    1919   1921       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_029978.
FT   VAR_SEQ    1946   1946       S -> SQLSSPSL (in isoform 2).
FT                                /FTId=VSP_029979.
FT   VAR_SEQ    1966   1990       Missing (in isoform 2).
FT                                /FTId=VSP_029980.
FT   CONFLICT    674    674       S -> T (in Ref. 2; AAC83164).
FT   CONFLICT   1597   1597       A -> T (in Ref. 4; BAD90141).
FT   CONFLICT   2171   2171       L -> I (in Ref. 2; AAC83164).
SQ   SEQUENCE   2190 AA;  244561 MW;  146E05DCCFF38DB4 CRC64;
     MAAFGILSYE HRPLKRLRLG PPDVYPQDPK QKEDELTALN VKQGFNNQPA VSGDEHGSAK
     NVNFNPAKIS SNFSSIIAEK LRCNTLSDTG RRKSLMNQKD NFWLVTARSQ SAINTWFTDL
     AGTKPLTHLA KKVPIFSKKE EVFGYLAKYT VPVMRAAWLI KMTCAYYAAM SETKVKKKNT
     ADPFTEWTQI ITKYLWEQLQ KMAEYYRPGP AGSGGCGSTI GPLPHDVEMA IRQWDYNEKL
     ALFMFQDGML DRHEFLTWVL ECFEKIRPGE DELLKLLLPL LLRYSGEFVQ SAYLSRRLAY
     FCTRRLALQL DGVSSHSSHV IAAQSTSSLP TTPAPQPPTS STPSTPFSDL LMCPQHRPLV
     FGLSCILQTI LLCCPSALVW HYSLTDSRIK TGSPLDHLPI APSNLPMPEG NSAFTQQVRA
     KLREIEQQIK ERGQAVEVRW SFDKCQEATA GFTIGRVLHT LEVLDSHSFE RSDFSNSLDS
     LCNRIFGLGP SKDGHEISSD DDAVVSLLCE WAVSCKRSGR HRAMVVAKLL EKRQAEIEAE
     RCGESEAADE KGSVASGSLS APSAPIFQDV LLQFLDTQAP MLTDPRSESE RVEFFNLVLL
     FCELIRHDVF SHNMYTCTLI SRGDLAFGAP GPRPPSPFDD PTDDPERKEA EGSSSSKLED
     PGLSESMDID PSSSVLFEDM EKPDFSLFSP TMPCEGKGSP SPEKPDVEKE VKPPAKEKIE
     GTLGILYDQP RHVQYATHFP IPQEESCSHE CNQRLVVLFG VGKQRDDARH AIKKITKDIL
     KVLNRKGTAE TDQLAPIVPL NPGDLTFLGG EDGQKRRRNR PEAFPTAEDI FAKFQHLSHY
     DQHQVTAQVS RNVLEQITSF ALGMSYHLPL VQHVQFIFDL MEYSLSISGL IDFAIQLLNE
     LSVVEAELLL KSSDLVGSYT TSLCLCIVAV LRHYHACLIL NQDQMAQVFE GLCGVVKHGM
     NRSDGSSAER CILAYLYDLY TSCSHLKSKF GELFSDFCSK VKNTIYCNVE PSESNMRWAP
     EFMIDTLENP AAHTFTYTGL GKSLSENPAN RYSFVCNALM HVCVGHHDPD RVNDIAILCA
     ELTGYCKSLS AEWLGVLKAL CCSSNNGTCG FNDLLCNVDV SDLSFHDSLA TFVAILIARQ
     CLLLEDLIRC AAIPSLLNAA CSEQDSEPGA RLTCRILLHL FKTPQLNPCQ SDGNKPTVGI
     RSSCDRHLLA ASQNRIVDGA VFAVLKAVFV LGDAELKGSG FTVPGGTEEL PEEEGGGGSS
     GRRQGGRNIS VETASLDVYA KYVLRSICQQ EWVGERCLKS LCEDSNDLQD PVLSSAQAQR
     LMQLICYPHR LLDNEDGENP QRQRIKRILK NLDQWTMRQS SLELQLMIKQ TPNTEMNSLL
     ENIAKATIEV FQQSAETGSS SGSTASNMPS SSKTKPVLSS LERSGVWLVA PLIAKLPTSV
     QGHVLKAAGE ELEKGQHLGS SSRKERDRQK QKSMSLLSQQ PFLSLVLTCL KGQDEQREGL
     LASLHSQVHQ IVINWRENQY LDDCKPKQLM HEALKLRLNL VGGMFDTVQR STQQTTEWAQ
     LLLEIIISGT VDMQSNNELF TTVLDMLSVL INGTLAADMS SISQGSMEEN KRAYMNLVKK
     LQKDLGERQS DSLEKVHQLL PLPKQNRDVI TCEPQGSLID TKGNKIAGFD SIFKKEGLQV
     STKQKISPWE LFEGLKPSTA PLSWAWFGTV RVDRRVARGE EQQRLLLYHT HLRPRPRAYY
     LEPLPLPPED EEPPAPALLE PEKKAPEPPK TDKPGAAPPS TEERKKKSTK GKKRSQPATK
     NEDYGMGPGR SGPYGVTVPP DLLHHANPGS ISHLSYRQSS MGLYTQNQPL PAGGPRVDPY
     RPVRLPMQKL PTRPTYPGVL PTTMSTVMGL EPSSYKTSVY RQQQPTVPQG QRLRQQLQAK
     IQSQGMLGQS SVHQMTPSSS YGLQTSQGYT SYVSHVGLQQ HTGPAGTMVP PSYSSQPYQS
     THPSTNPTLV DPTRHLQQRP SGYVHQQAPT YGHGLTSTQR FSHQTLQQTP MMGTMTPLSA
     QGVQAGVRST SILPEQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQYH IRQQQQQQQM
     LRQQQQQQQQ QQQQQQQQQQ QQQQQQQQQP HQQQQQAAPP QPQPQSQPQF QRQGLQQTQQ
     QQQTAALVRQ LQQQLSNTQP QPSTNIFGRY
//
ID   A2AGJ6_MOUSE            Unreviewed;      1099 AA.
AC   A2AGJ6;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   30-NOV-2010, entry version 32.
DE   SubName: Full=Solute carrier family 12, member 6;
DE   SubName: Full=Solute carrier family 12, member 6, isoform CRA_a;
GN   Name=Slc12a6; ORFNames=RP23-208E23.1-004, mCG_20782;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Almeida-King J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL683897; CAM17483.1; -; Genomic_DNA.
DR   EMBL; CH466519; EDL27837.1; -; Genomic_DNA.
DR   IPI; IPI00230064; -.
DR   RefSeq; NP_598409.2; NM_133648.2.
DR   UniGene; Mm.479575; -.
DR   ProteinModelPortal; A2AGJ6; -.
DR   STRING; A2AGJ6; -.
DR   PRIDE; A2AGJ6; -.
DR   Ensembl; ENSMUST00000053666; ENSMUSP00000051490; ENSMUSG00000027130.
DR   GeneID; 107723; -.
DR   KEGG; mmu:107723; -.
DR   CTD; 107723; -.
DR   MGI; MGI:2135960; Slc12a6.
DR   eggNOG; roNOG12599; -.
DR   HOVERGEN; HBG052852; -.
DR   NextBio; 359318; -.
DR   Bgee; A2AGJ6; -.
DR   Genevestigator; A2AGJ6; -.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0015377; F:cation:chloride symporter activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR   InterPro; IPR004841; AA-permease_dom.
DR   InterPro; IPR000622; K/Cl_cotranspt1.
DR   InterPro; IPR018491; K/Cl_cotranspt_1/3.
DR   InterPro; IPR000076; KCL_cotranspt.
DR   InterPro; IPR004842; Na/K/Cl_cotransptS.
DR   Pfam; PF00324; AA_permease; 2.
DR   Pfam; PF03522; KCl_Cotrans_1; 1.
DR   PRINTS; PR01081; KCLTRNSPORT.
DR   PRINTS; PR01082; KCLTRNSPORT1.
DR   TIGRFAMs; TIGR00930; 2a30; 1.
PE   4: Predicted;
SQ   SEQUENCE   1099 AA;  122040 MW;  8CEA6F2DC4103DB2 CRC64;
     MPHFTVTKVE DPEEGAAGPL SPEPSSAEVK ARIQDPQEPD PSQNSITGEH SQLLDDGHKK
     ARNAYLNNSN YEEGDEYFDK NLALFEEEMD TRPKVSSLLN RMANYTNLTQ GAKEHEEAEN
     ITEGKKKPTK SPQMGTFMGV YLPCLQNIFG VILFLRLTWV VGTAGILQAF AIVLICCCCT
     MLTAISMSAI ATNGVVPAGG SYFMISRALG PEFGGAVGLC FYLGTTFAAA MYILGAIEIF
     LVYIVPRAAI FRSDDALKES AAMLNNMRVY GTAFLVLMVL VVFIGVRYVN KFASLFLACV
     IVSILAIYAG AIKSSFAPPH FPVCMLGNRT LSSRHLDICS KTKEVDNMTV PSKLWGFFCN
     SSQFFNATCD EYFVHNNVIS IQGIPGLASG IITENLWSNY LPKGEIIEKP SAKSSDVLGN
     LNHEYVLADI TTSFTLLVGI FFPSVTGIMA GSNRSGDLKD AQKSIPIGTI LAILTTSFVY
     LSNVVLFGAC IEGVVLRDKF GDAVKGNLVV GTLSWPSPWV IVIGSFFSTC GAGLQSLTGA
     PRLLQAIAKD NIIPFLRVFG HSKANGEPTW ALLLTAAIAE LGILIASLDL VAPILSMFFL
     MCYLFVNLAC ALQTLLRTPN WRPRFRYYHW ALSFMGMSIC LALMFISSWY YAIVAMVIAG
     MIYKYIEYQG AEKEWGDGIR GLSLSAARFA LLRLEEGPPH TKNWRPQLLV LLKLDEDLHV
     KHPRLLTFAS QLKAGKGLTI VGSVIVGNFL ENYGDALAAE QTIKHLMEAE KVKGFCQLVV
     AAKLKEGISH LIQSCGLGGM KHNTVVMGWP NGWRQSEDAR AWKTFIGTVR VTTAAHLALL
     VAKNVSFFPS NVEQFSEGNI DVWWIVHDGG MLMLLPFLLK QHKVWRKCSI RIFTVAQLED
     NSIQMKKDLA TFLYHLRIEA EVEVVEMHDS DISAYTYERT LMMEQRSQML RHMRLSKTER
     DREAQLVKDR NSMLRLTSIG SDEDEETETY QEKVHMTWTK DKYMASRGQK VKSMEGFQDL
     LNMRPDQSNV RRMHTAVKLN EVIVNKSHEA KLVLLNMPGP PRNPEGDENY MEFLEVLTEG
     LERVLLVRGG GSEVITIYS
//
ID   A2AGQ4_MOUSE            Unreviewed;      1632 AA.
AC   A2AGQ4;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 32.
DE   SubName: Full=MAP-kinase activating death domain;
GN   Name=Madd; ORFNames=RP23-20F9.4-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Pelan S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL691450; CAM17570.1; -; Genomic_DNA.
DR   IPI; IPI00620097; -.
DR   RefSeq; NP_001171192.1; NM_001177721.1.
DR   UniGene; Mm.36410; -.
DR   STRING; A2AGQ4; -.
DR   Ensembl; ENSMUST00000077941; ENSMUSP00000077094; ENSMUSG00000040687.
DR   GeneID; 228355; -.
DR   KEGG; mmu:228355; -.
DR   CTD; 228355; -.
DR   MGI; MGI:2444672; Madd.
DR   HOGENOM; HBG715614; -.
DR   HOVERGEN; HBG079455; -.
DR   InParanoid; A2AGQ4; -.
DR   OMA; AFQRIHN; -.
DR   OrthoDB; EOG4CC40G; -.
DR   Bgee; A2AGQ4; -.
DR   Genevestigator; A2AGQ4; -.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR005112; dDENN.
DR   InterPro; IPR001194; DENN.
DR   InterPro; IPR005113; uDENN.
DR   Pfam; PF03455; dDENN; 1.
DR   Pfam; PF02141; DENN; 1.
DR   Pfam; PF03456; uDENN; 1.
DR   SMART; SM00801; dDENN; 1.
DR   SMART; SM00799; DENN; 1.
DR   SMART; SM00800; uDENN; 1.
DR   PROSITE; PS50947; DDENN; 1.
DR   PROSITE; PS50211; DENN; 1.
DR   PROSITE; PS50946; UDENN; 1.
PE   4: Predicted;
KW   Kinase; Transferase.
SQ   SEQUENCE   1632 AA;  181181 MW;  CB666B13F6CA6E2D CRC64;
     MVQKKFCPRL LDYLVIVGAR HPSSDSVAQT PELLRRYPLE DHPEFPLPPD VVFFCQPEGC
     LSVRQRRMSL RDDTSFVFTL TDKDTGVTRY GICVNFYRSF QKRMPKEKVE GGAGPRGKEG
     AHTSGASEEA AAGSSESGST LQPPSADSTP DVNQSPRGKR RAKAGSRSRN STLTSLCVLS
     HYPFFSTFRE CLYTLKRLVD CCSERLLGKK LGIPRGVQRD TMWRIFTGSL LVEEKSSALL
     QDLREIEAWI YRLLRSPVPV SGQKRVDIEV LPQELQQALT FALPDPSRFT LVDFPLHLPL
     ELLGVDACLQ VLTCILLEHK VVLQSRDYNA LSMSVMAFVA MIYPLEYMFP VIPLLPTCMA
     SAEQLLLAPT PYIIGVPASF FLYKLDFKMP DDVWLVDLDS NRVIAPTNAE VLPILPEPES
     LELKKHLKQA LASMSLNTQP ILNLEKFHEG QEIPLLLGRP SNDLQSTPST EFNPLIYGND
     VDSVDVATRV AMVRFFNSAN VLQGFQMHTR TLRLFPRPVV AFQAGSFLAS RPRQTPFAEK
     LARTQAVEYF GEWILNPSNY AFQRIHNNTF DPALIGDKPK WYAHQLQPIH YRVYDGNSQL
     AEALSVPPER DSDSDPTEDS GSDSQDYDDS SSSYSSLGDF VSEMMKCDIN GDTPNVDPLT
     HAALGDASEV EIDELQPQKE GEEPGPDSEN SQENPPLRSS SSTTASSSPS TVVHSAHSEA
     ADSTEMGDKA TAGISKPLPP VPPSICKSTV DRRQTETGEG SVCQRTYDNP YFEPQYGFPP
     EEDEEEQGES YTPRFSQHVS GSRAQKLLRP NSLKLASDSD AESDSRASSP NSTVSNNSTE
     GFGGIMSFAS SLYRNHSTSF SLSNLTLPTK GAREKTTPFP SLKVFGLNTL MEIVTEAGPG
     SGEGNRRALV DQKSSVIKHS PTVKREPSSP QGRSSNSSEN QQFLKEVVHS VLDGQGVGWL
     NMKKVRRLLE SEQLRVFVLS KLNRAVQSED DARQDVIQDV EISRKVYKGM LDLLKCTVLS
     LEQSYAHAGL GGMASIFGLL EIAQTHYYSK EPDKRKRSPT ENVNTPVGKD PGLAGRGDPK
     AMAQLRVPQL GPRAPSATGK GPKELDTRSL KEENFVASVE LWNKHQEVKK QKALEKQRPE
     GIKPVFDLGE TEEKKSQMSA DSGVSLTSAS QRTDQDSVIG VSPAVMIRSS SQDSEVSTVV
     SNSSGETLGA DSDLSSNAGD GPGGEGSAHL ASSRATLSDS EIETNSATSA IFGKAHSLKP
     KEKPAGSPIR SSEDVSQRVY LYEGLLGRDK GSMWDQLEDA AMETFSLSKE RSTLWDQMQF
     WEDAFLDAVM LEREGMGMDQ GPQEMIDRYL SLGEHDRKRL EDDEDRLLAT LLHNLISYML
     LMKVNKNDIR KKVRRLMGKS HIGLVYSQQV NEVLDQLNSL NGRDLSIRSS GSRHMKKQTF
     VVHAGTDTNG DIFFMEVCDD CVVLRSNIGT VYERWWYEKL INMTYCPKTK VLCLWRRNGS
     ETQLNKFYTK KVLRVCVWAG DWIGPELGGE FPVQDMKTGE GGLLQVTLEG INLKFMHNQV
     FIELNHIKKC NTVRGVFVLE EFVPEIKEVV SHKYKTPMAH EICYSVLCLF SYVAAVRSSE
     EDLRTPPRPV SS
//
ID   CKAP5_MOUSE             Reviewed;        2032 AA.
AC   A2AGT5; A0PJ77; A2AGT6; B2RRC4; Q0VGR0; Q3TML9; Q3UDY6; Q4VAE7;
AC   Q9CUN0;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 35.
DE   RecName: Full=Cytoskeleton-associated protein 5;
GN   Name=Ckap5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6; TISSUE=Head, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-980 (ISOFORMS 1/2/3).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow macrophage, Lung, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Plays a major role in organizing spindle poles (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with TACC1 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=A2AGT5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2AGT5-2; Sequence=VSP_053003;
CC         Note=No experimental confirmation available. Gene prediction
CC         based on similarity to human ortholog;
CC       Name=3;
CC         IsoId=A2AGT5-3; Sequence=VSP_053004;
CC   -!- SIMILARITY: Belongs to the TOG/XMAP215 family.
CC   -!- SIMILARITY: Contains 10 HEAT repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH17140.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC   -----------------------------------------------------------------------
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DR   EMBL; AL691489; CAM16482.1; -; Genomic_DNA.
DR   EMBL; AL691489; CAM16483.1; -; Genomic_DNA.
DR   EMBL; BC017140; AAH17140.1; ALT_SEQ; mRNA.
DR   EMBL; BC089032; AAH89032.1; -; mRNA.
DR   EMBL; BC096422; AAH96422.1; -; mRNA.
DR   EMBL; BC138334; AAI38335.1; -; mRNA.
DR   EMBL; AK015282; BAB29779.1; -; mRNA.
DR   EMBL; AK149854; BAE29125.1; -; mRNA.
DR   EMBL; AK165862; BAE38422.1; -; mRNA.
DR   IPI; IPI00317134; -.
DR   IPI; IPI00337930; -.
DR   IPI; IPI00874846; -.
DR   RefSeq; NP_001159461.1; NM_001165989.1.
DR   RefSeq; NP_083713.2; NM_029437.2.
DR   UniGene; Mm.168478; -.
DR   ProteinModelPortal; A2AGT5; -.
DR   SMR; A2AGT5; 4-222, 266-502, 602-628, 848-1079, 1160-1424.
DR   PRIDE; A2AGT5; -.
DR   Ensembl; ENSMUST00000111338; ENSMUSP00000106970; ENSMUSG00000040549.
DR   GeneID; 75786; -.
DR   KEGG; mmu:75786; -.
DR   NMPDR; fig|10090.3.peg.6404; -.
DR   CTD; 75786; -.
DR   MGI; MGI:1923036; Ckap5.
DR   HOVERGEN; HBG050955; -.
DR   InParanoid; A2AGT5; -.
DR   OMA; KHSTSGT; -.
DR   OrthoDB; EOG42Z4P9; -.
DR   Bgee; A2AGT5; -.
DR   Genevestigator; A2AGT5; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0050658; P:RNA transport; ISS:UniProtKB.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR021133; HEAT_type_2.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 7.
DR   SUPFAM; SSF48371; ARM-type_fold; 2.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Cell cycle; Cell division; Mitosis;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1   2032       Cytoskeleton-associated protein 5.
FT                                /FTId=PRO_0000364005.
FT   REPEAT      159    197       HEAT 1.
FT   REPEAT      356    394       HEAT 2.
FT   REPEAT      434    472       HEAT 3.
FT   REPEAT      750    788       HEAT 4.
FT   REPEAT      855    893       HEAT 5.
FT   REPEAT      936    974       HEAT 6.
FT   REPEAT     1013   1051       HEAT 7.
FT   REPEAT     1284   1322       HEAT 8.
FT   REPEAT     1324   1357       HEAT 9.
FT   REPEAT     1361   1399       HEAT 10.
FT   MOD_RES      48     48       N6-acetyllysine (By similarity).
FT   MOD_RES     816    816       Phosphoserine (By similarity).
FT   VAR_SEQ    1564   1623       Missing (in isoform 2).
FT                                /FTId=VSP_053003.
FT   VAR_SEQ    1903   1923       Missing (in isoform 3).
FT                                /FTId=VSP_053004.
FT   CONFLICT      5      5       S -> C (in Ref. 3; BAE38422).
FT   CONFLICT     19     19       K -> N (in Ref. 3; BAB29779).
FT   CONFLICT    111    111       E -> K (in Ref. 3; BAB29779).
FT   CONFLICT    174    174       E -> G (in Ref. 3; BAE38422).
FT   CONFLICT    227    227       K -> R (in Ref. 3; BAB29779).
FT   CONFLICT    522    522       A -> T (in Ref. 3; BAB29779).
FT   CONFLICT    581    581       E -> Q (in Ref. 3; BAB29779).
FT   CONFLICT    675    675       S -> F (in Ref. 3; BAB29779).
FT   CONFLICT    709    709       A -> G (in Ref. 3; BAB29779).
FT   CONFLICT    836    836       E -> V (in Ref. 3; BAE29125).
FT   CONFLICT    981    981       E -> A (in Ref. 2; AAH89032).
FT   CONFLICT   1028   1028       K -> E (in Ref. 2; AAH89032/AAH96422/
FT                                AAI38335).
FT   CONFLICT   1717   1717       V -> F (in Ref. 2; AAH96422).
SQ   SEQUENCE   2032 AA;  225635 MW;  28FD8628C6F678CB CRC64;
     MGDDSEWLKL PVDQKCEHKL WKARLSGYEE ALKIFQKIKD EKSPEWSKYL GLIKKFVTDS
     NAVVQLKGLE AALVYVENAH VAGKTTGEVV SGVVSKVFNQ PKAKAKELGI EICLMYVEIE
     KGESVQEELL KGLDNKNPKI IVACIETLRK ALSEFGSKII SLKPIIKVLP KLFESRDKAV
     RDEAKLFAIE IYRWNRDAVK HTLQNINSVQ LKELEEEWVK LPTGAPKPSR FLRSQQELEA
     KLEQQQSAGG DAEGGGDDGD EVPQVDAYEL LDAVEILSKL PKDFYDKIEA KKWQERKEAL
     EAVEVLVKNP KLEAGDYADL VKALKKVVGK DTNVMLVALA AKCLTGLAVG LRKKFGQYAG
     HVVPTILEKF KEKKPQVVQA LQEAIDAIFL TTTLQNISED VLAVMDNKNP TIKQQTSLFI
     ARSFRHCTSS TLPKSLLKPF CAALLKHIND SAPEVRDAAF EALGTALKVV GEKSVNPFLA
     DVDKLKLDRI KECSEKVELV HGKKSGLATE KKESKPLPGR AAASGAAGDK DTKDVSGPKP
     GPLKKTPTAK AGGPSKKGKT TAPGGSASAG TKNKKGLETK EIVEPELSIE VCEEKASAVL
     PPTCIQLLDS SNWKERLACM EEFQKAVELM ERTEMPCQAL VKMLAKKPGW KETNFQVMQM
     KLHIVALIAQ KGNFSKTSAQ IVLDGLVDKI GDVKCGNNAK EAMTAIAEAC MLPWTAEQVM
     SMAFSQKNPK NQSETLNWLS NAIKEFGFSE LNVKAFISNV KTALAATNPA VRTSAITLLG
     VMYLYVGPSL RMIFEDEKPA LLSQIDAEFQ KMQGQSPPAP TRGIAKHSTS ATDEGEDGEE
     PGEGGNDVVD LLPRIEISDK ITSELVSKIG DKNWKIRKEG LDEVAGIINE AKFIQPNIGE
     LPTALKGRLN DSNKILVQQT LNILQQLAVA MGANIRQHVK NLGIPVITVL GDSKNNVRAA
     ALATVNAWAE QTGMKEWLEG EDLSEELKKE NPFLRQELLG WLAEKLPTLR STPTDLILCV
     PHLYSCLKDR NGDVRKKAQD ALPFFMMHLG YEKMAKATGK LKPTSKDQVL AMLEKAKANM
     PSKPAAPAKA MSKPMGGSAP AKTQPIPAPV EDSVSSTIEA KPDLKKAKAP GVSSKAKSVQ
     GKKVPSKTTL KEDDDKSGPI FIVVPNGKEQ RMRDEKGLKV LKWNFTTPRD EYIEQLKTQM
     STCVAKWLQD EMFHSDFQHH NKALAVMVDH LESEKDGVIS CLDLILKWLT LRFFDTNTSV
     LMKALEYLKL LFTLLSEEEY HLTENEASSF IPYLILKVGE PKDVIRKDVR AILNRMCLVY
     PASKMFPFIM EGTKSKNSKQ RAECLEELGC LIESYGMNVC QPTPGKALKE IAIHIGDRDN
     AVRNAALNTI VTVYNVHGDQ VFKLIGNLSE KDMSMLEERI KRSAKRPSAA PVKQAEEKPQ
     RTQNINSNAN MLRKGPAEDM SSKLNQARSL SGHPEAAQMV RREFQLDLDE IENDNGTVRC
     EMPELVQHKL DDIFEPVLIP EPKIRAVSPH FDDMHSNTAS TINFIISQVA SGDINTSIQA
     LTQIDEVLRQ EDKAEAMSGH IDQFLIATFM QLRLIYSTHM ADEKLDKDEI IKLYSCIIGN
     MISLFQIESL AREASTGVLK DLMHGLITLM LDSRIEDLEE GQQVIRSVNL LVVKVLEKSD
     QTNILSALLV LLQDSLLATA SSPKFSELVM KCLWRMVRLL PDTINSINLD RILLDIHIFM
     KVFPKEKLKQ CKSEFPIRTL KTLLHTLCKL KGPKILDHLT MIDNKNESEL EAHLCRMMKH
     SMDQTGSKSD KETEKGASRI DEKSSKAKVN DFLAEIFKKI GSKENTKEGL AELYEYKKKY
     SDTDIEPFLK NSSQFFQSYV ERGLRVIEME RESKGRIPTS TGISPQMEVT CVPTPTSTVS
     SLGNTNGEEV GPSVYLERLK ILRQRCGLDN TKQDDRPPLT SLLSKPAIPP VASSTDMLHS
     KLSQLRESRE QHQHSDLDSN QTHSAGTMTS SSSTTNIDDL KKRLERIKSS RK
//
ID   CAMP1_MOUSE             Reviewed;        1581 AA.
AC   A2AHC3; Q7TQF8; Q8CBV3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 36.
DE   RecName: Full=Calmodulin-regulated spectrin-associated protein 1;
GN   Name=Camsap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 383-1581 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A2AHC3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2AHC3-2; Sequence=VSP_030802, VSP_030803, VSP_030804;
CC   -!- DOMAIN: The CKK domain binds microtubules (By similarity).
CC   -!- SIMILARITY: Belongs to the CAMSAP1 family.
CC   -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC   -!- SIMILARITY: Contains 1 CKK domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH54553.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AL731682; CAM14279.1; -; Genomic_DNA.
DR   EMBL; BC054553; AAH54553.1; ALT_INIT; mRNA.
DR   EMBL; AK035221; BAC28983.1; -; mRNA.
DR   IPI; IPI00673777; -.
DR   IPI; IPI00885251; -.
DR   RefSeq; NP_001108548.1; NM_001115076.1.
DR   UniGene; Mm.36834; -.
DR   ProteinModelPortal; A2AHC3; -.
DR   SMR; A2AHC3; 1442-1570.
DR   PhosphoSite; A2AHC3; -.
DR   PRIDE; A2AHC3; -.
DR   Ensembl; ENSMUST00000061377; ENSMUSP00000058690; ENSMUSG00000026933.
DR   Ensembl; ENSMUST00000091268; ENSMUSP00000088812; ENSMUSG00000026933.
DR   Ensembl; ENSMUST00000114167; ENSMUSP00000109804; ENSMUSG00000026933.
DR   GeneID; 227634; -.
DR   KEGG; mmu:227634; -.
DR   CTD; 227634; -.
DR   MGI; MGI:3036242; Camsap1.
DR   GeneTree; ENSGT00390000010026; -.
DR   HOGENOM; HBG446513; -.
DR   HOVERGEN; HBG107572; -.
DR   InParanoid; A2AHC3; -.
DR   OMA; KVRYRRE; -.
DR   OrthoDB; EOG4SF952; -.
DR   NextBio; 378706; -.
DR   Bgee; A2AHC3; -.
DR   Genevestigator; A2AHC3; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   InterPro; IPR014797; CAMSAP_C.
DR   InterPro; IPR022613; CAMSAP_CH.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR011033; PRC_barrell-like.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 1.
DR   Pfam; PF11971; CAMSAP_CH; 1.
DR   Pfam; PF08683; DUF1781; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   SUPFAM; SSF50346; PRCH_cytoplasmic; 1.
DR   PROSITE; PS50021; CH; FALSE_NEG.
DR   PROSITE; PS51508; CKK; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Cytoskeleton; Microtubule;
KW   Phosphoprotein.
FT   CHAIN         1   1581       Calmodulin-regulated spectrin-associated
FT                                protein 1.
FT                                /FTId=PRO_0000316829.
FT   DOMAIN      182    327       CH.
FT   DOMAIN     1443   1576       CKK.
FT   MOD_RES     370    370       Phosphoserine (By similarity).
FT   MOD_RES     374    374       Phosphoserine (By similarity).
FT   MOD_RES     511    511       Phosphothreonine (By similarity).
FT   MOD_RES     550    550       Phosphoserine.
FT   MOD_RES     553    553       Phosphoserine.
FT   MOD_RES     560    560       Phosphoserine (By similarity).
FT   MOD_RES     572    572       Phosphoserine (By similarity).
FT   MOD_RES     586    586       Phosphoserine (By similarity).
FT   MOD_RES     718    718       Phosphoserine (By similarity).
FT   MOD_RES     734    734       Phosphoserine (By similarity).
FT   MOD_RES     736    736       Phosphoserine (By similarity).
FT   MOD_RES    1069   1069       Phosphoserine (By similarity).
FT   MOD_RES    1516   1516       Phosphotyrosine (By similarity).
FT   VAR_SEQ     221    221       K -> KPGLEHAVMHCMLEPVDFARV (in isoform
FT                                2).
FT                                /FTId=VSP_030802.
FT   VAR_SEQ    1058   1062       IKAPV -> ASPRR (in isoform 2).
FT                                /FTId=VSP_030803.
FT   VAR_SEQ    1063   1581       Missing (in isoform 2).
FT                                /FTId=VSP_030804.
FT   CONFLICT    901    901       R -> L (in Ref. 2; BAC28983).
FT   CONFLICT   1482   1482       E -> EE (in Ref. 2; BAC28983).
SQ   SEQUENCE   1581 AA;  175887 MW;  4293DE86DE3A2585 CRC64;
     MVDAGGRCAA EGWRRMEAPP EGADLVPLDR YDAARAKIAA NLQWICAKAY GLDNIPEDLR
     DPFYIDQYEQ EHIKPPVIKL LLSSELYCRV CSLILKGDQV ATLQGHQSVI QALSRKGIYV
     MESDDTPVTD ADLSQAPIKM SGHMAMVDAL MMAYTVEMIS IEKVVASVKR FSTFSASKEL
     PYDLEDAMVF WINKVNLKMR EITEKEVKLK QQPLESPAHQ KVRYRREHLS ARQSPYFPLL
     EDLMRDGSDG AALLAVVHYY CPEQMKLDDI CLKEVPSMAD SLYNIRLLRE FSNEHLNKCF
     YLTLEDMLYA PLVLKPNVMV FIAELFWWFE NVKPDFVQPR DIQELKDAKT VLQQKSSRPP
     VPISNATKRS FLGSPAAMSP ADQPPSTQPL AEGSHRYHLH SEEPECLGKG ASTFSPSHPL
     LPLRQKQQKV SQTEEIPDQR HRSNSLTRVD GQPRGAIGAW PDKKNRPVSQ PTSFALHHAA
     SCDVDPSSGD SVSLARSISK DSLASNIIHL TPQNQPHPSA GKSNGKSLLS NVNIEDEDEE
     LVAIIRTDVS PPSPQMPRTS PQAPGLVASI RSPQRQADTL ESKPDSFYLE PLMPAVLRPA
     KEKQITTKED ERGEGRPRTI MAKRPSEGSQ PMVRKKVSGG HGSRDLNRTF TPIPCSEFAA
     SIDLAEVGPQ SAEATGEGQP LALGRFDTLP QGQAADGFFL HVGRAEEDEG RWYVGSQSPS
     SHDSEPWTIL RQDSDSDVVD VEDTEQDFIG EDHPVVIPRY AGEEESAKLQ EDMKVKEHED
     KDDASGRSSP CLSTTSQLSS MSMASGSVKM TSFAERKLQR LNSCETKSST SSSQKTTPDA
     SESCPAPLTT WRQKREQSPG RHSKDPASLL ASELVQLHMQ LEEKRRAIEA QKKKMEALSA
     RQRLKLGKAA FLHVVKKGKA DGAPQPLRPE HFTKEFTQHN GEDLDDGTCK TEGFLVKEEQ
     RDLSDAQDVA FVQLHKPRDP AALHDGEKHR MISTALLEDS VGEVDVNECD LSIEKLNETI
     STLQQAILKI SQQQEQLLMK SPTVPTPGTK NNCQDQKIKA PVHFVEPLSP TGVPGHRKPP
     RLGQGRNSRS GRPAELKVPK DRQQGCSRSK TPTPSVETLP QSRSLPPSTH PRSPSDPGGE
     LPEKCLFDSY RLHDESNHRT FVLSSCKDAN IVSEQVNFKE GLDTSVKEAG LSSSTITGKE
     HTPVEEPLRS KASLIEVDLS DLKAPDEDGE VVGHESSVEL GGDSDQKPGV GFFFKDEQKA
     EDELAKKRAA FLLKQQRKAE EARARKQQLE AEVELKRDEA RRKAEEDRLR KEEEKARREL
     IKQEYLRRKQ QQALEEQGLG KPKSKPKKPR PKSVHREESY SDSGTKCSST HNLSQTHSGS
     SLSLASAATT EPESVYSGGT PSHRVESLEA LPILSRNPSR STDRDWETAS AASSLASVAE
     YTGPKLFKEP SSKSNKPIIH NAISHCCLAG KVNEPHKNSI LELEKCDANH YIILFRDAGC
     QFRALYCYQP DTEEIYKLTG TGPKSITKKM IDKLYKYSSD RKQFNLIPAK TMSVSVDALT
     IHNHLWQPKR PTVPKKTQTR K
//
ID   PRIP1_MOUSE             Reviewed;         700 AA.
AC   A2AHG0; A2AHF9; Q3TSY0; Q6PE51;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   RecName: Full=ProSAP-interacting protein 1;
DE            Short=ProSAPiP1;
GN   Name=Prosapip1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-700 (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBUNIT: Interacts (via C-terminus) with SHANK3 (via PDZ domain).
CC       Interacts (via coiled coil) with SIPA1L1. Can form homooligomers
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane, postsynaptic density (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity). Note=Detected at synapses,
CC       postsynaptic density, synaptic spines and dendrites (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=A2AHG0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2AHG0-2; Sequence=VSP_039203;
CC       Name=3;
CC         IsoId=A2AHG0-3; Sequence=VSP_039204, VSP_039205;
CC   -!- SIMILARITY: Belongs to the PROSAPIP1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH58280.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; AL731707; CAM13272.1; -; Genomic_DNA.
DR   EMBL; AL731707; CAM13273.1; -; Genomic_DNA.
DR   EMBL; CH466519; EDL28282.1; -; Genomic_DNA.
DR   EMBL; CH466519; EDL28283.1; -; Genomic_DNA.
DR   EMBL; AK161711; BAE36545.1; -; mRNA.
DR   EMBL; BC058280; AAH58280.1; ALT_INIT; mRNA.
DR   IPI; IPI00378731; -.
DR   IPI; IPI00651935; -.
DR   IPI; IPI00968391; -.
DR   RefSeq; NP_922936.3; NM_197945.3.
DR   UniGene; Mm.440130; -.
DR   ProteinModelPortal; A2AHG0; -.
DR   PRIDE; A2AHG0; -.
DR   Ensembl; ENSMUST00000045761; ENSMUSP00000037109; ENSMUSG00000037703.
DR   Ensembl; ENSMUST00000089561; ENSMUSP00000086990; ENSMUSG00000037703.
DR   GeneID; 241638; -.
DR   KEGG; mmu:241638; -.
DR   CTD; 241638; -.
DR   MGI; MGI:2656976; Prosapip1.
DR   GeneTree; ENSGT00510000046769; -.
DR   HOGENOM; HBG713386; -.
DR   HOVERGEN; HBG052381; -.
DR   InParanoid; A2AHG0; -.
DR   OMA; KDSQADV; -.
DR   OrthoDB; EOG4G1MGH; -.
DR   NextBio; 385107; -.
DR   Bgee; A2AHG0; -.
DR   Genevestigator; A2AHG0; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR009638; Fez1.
DR   Pfam; PF06818; Fez1; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell junction; Cell membrane; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Membrane; Postsynaptic cell membrane;
KW   Synapse.
FT   CHAIN         1    700       ProSAP-interacting protein 1.
FT                                /FTId=PRO_0000394199.
FT   COILED      345    523       Potential.
FT   COILED      597    666       Potential.
FT   COMPBIAS    215    333       Gly/Ser-rich.
FT   VAR_SEQ      70    183       Missing (in isoform 2).
FT                                /FTId=VSP_039203.
FT   VAR_SEQ     589    591       VEA -> IAG (in isoform 3).
FT                                /FTId=VSP_039204.
FT   VAR_SEQ     592    700       Missing (in isoform 3).
FT                                /FTId=VSP_039205.
FT   CONFLICT     97     97       S -> G (in Ref. 1; BAE36545).
SQ   SEQUENCE   700 AA;  74986 MW;  2DD613B6F77BB6A2 CRC64;
     MAPADLASEG PKLEDPPAPH LFGKCPSGLI MAKLETLPVR ADPGRDPLLA FAPRPSELGP
     PDPRLTMGSV GSGVTHAQEF PMKSVGTRTG GGGNQGSFPG PRSGGSGANR ERPGRYPSED
     KVLANSLYLN GELRGSDHTD VCGNVVGSSG GSSSSGGSDK APPQYREPNH PPKLLTTSGK
     LDQCSEPLVR PSAFKPVVPK NFHSMQNLCP PQTNGTPEGR QGPAGLKGGL DKSRTMTPAG
     GSGGGLSDSG RNSLTSLPTY SSSYSQHLAP LSASTSHINR IGTAGYSSGS SGGGSGYQDL
     GTSDSGRASS KSGSSSSMGR SGHLGSGEGG NGGLPFAACS PPSPSALIQE LEERLWEKEQ
     EVAALRRSLE QSEAAVAQVL EERQKAWERE LAELRQGCSG KLQQVARRAQ RAQQGLQLQV
     LRLQQDKKQL QEEAAQLIRQ REELEDKVAV CQKEQADFLP RMEETKWEVC QKAGEISLLK
     QQLKDSQADV SQKLSEIVGL RSQLREGRAS LREKEEQLLS LRDSFGSKQA SLELSEGELP
     PACLKPALTP VDLVEPQEAL ASCESDEAKM RRQAGVAAAA SLVSVDGEVE AGGEGGTRAL
     RREVGRLQAE LAAERRARER QGASFAEERR VWLEEKEKVI EYQKQLQLSY VEMYQRNQQL
     ERRLRERGAA GGSSTPTPQH GEEKKAWTPS RLERIESTEI
//
ID   A2AHJ6_MOUSE            Unreviewed;       929 AA.
AC   A2AHJ6;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 40.
DE   SubName: Full=Diacylglycerol kinase zeta;
GN   Name=Dgkz; ORFNames=RP23-273F8.4-002;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Van Hellmond Z.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Humphries M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL731772; CAM19275.1; -; Genomic_DNA.
DR   EMBL; AL732484; CAM19275.1; JOINED; Genomic_DNA.
DR   EMBL; AL732484; CAM22583.1; -; Genomic_DNA.
DR   EMBL; AL731772; CAM22583.1; JOINED; Genomic_DNA.
DR   IPI; IPI00953737; -.
DR   RefSeq; NP_612179.2; NM_138306.2.
DR   UniGene; Mm.314923; -.
DR   ProteinModelPortal; A2AHJ6; -.
DR   SMR; A2AHJ6; 755-914.
DR   STRING; A2AHJ6; -.
DR   Ensembl; ENSMUST00000028667; ENSMUSP00000028667; ENSMUSG00000040479.
DR   GeneID; 104418; -.
DR   KEGG; mmu:104418; -.
DR   NMPDR; fig|10090.3.peg.6417; -.
DR   CTD; 104418; -.
DR   MGI; MGI:1278339; Dgkz.
DR   eggNOG; roNOG04094; -.
DR   HOVERGEN; HBG067303; -.
DR   PhylomeDB; A2AHJ6; -.
DR   Bgee; A2AHJ6; -.
DR   Genevestigator; A2AHJ6; -.
DR   GO; GO:0004143; F:diacylglycerol kinase activity; IEA:InterPro.
DR   GO; GO:0004857; F:enzyme inhibitor activity; IDA:MGI.
DR   GO; GO:0007205; P:activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway; IEA:InterPro.
DR   GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IMP:MGI.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 2.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00609; DAGK_acc; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00045; DAGKa; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS50146; DAGK; 1.
PE   4: Predicted;
KW   ANK repeat; Kinase; Repeat; Transferase.
SQ   SEQUENCE   929 AA;  104031 MW;  AC3E48790E3C3463 CRC64;
     MEPRDPSPEG RSSDSESASA SSSGSERDAG PEPDKAPRRL TKRRFPGLRL FGHRKAITKS
     GLQHLAPPPP TPGAPCGESE EQIQSTVDWS ESAVYGEHIW FETNVSGDFC YVGEQHCVAK
     MLPKSAPRKK CAACKIVVHT QCIKQLEKIN FRCKPSFRES GSRNVREPTF VRHHWVHRRR
     QDGKCRHCGK GFQQKFTFHS KEIVAISCSW CKQAYHSKVS CFMMQQIEEP CSLGVHAAVV
     IPPTWILRAR RPQNTLKASK KKKRASFKRR SSKKGPEEGR WRPFIIRPTP SPLMKPLLVF
     VNPKSGGNQG AKIIQSFLWY LNPRQVFDLS QGGPREALEM YRKVHNLRIL ACGGDGTVGW
     ILSTLDQLRL KPPPPVAILP LGTGNDLART LNWGGGYTDE PVSKILSHVE EGNVVQLDRW
     DLRAEPNPEA GPEERDDGAT DRLPLDVFNN YFSLGFDAHV TLEFHESREA NPEKFNSRFR
     NKMFYAGTAF SDFLMGSSKD LAKHIRVVCD GMDLTPKIQD LKPQCIVFLN IPRYCAGTMP
     WGHPGEHHDF EPQRHDDGYL EVIGFTMTSL AALQVGGHGE RLTQCREVLL TTAKAIPVQV
     DGEPCKLSAS RIRIALRNQA TMVQKAKRRS TAPLHSDQQP VPEQLRIQVS RVSMHDYEAL
     HYDKEQLKEA SVPLGTVVVP GDSDLELCRA HIERLQREPD GAGAKSPMCH QLSSKWCFLD
     ATTASRFYRI DRAQEHLNYV TEIAQDEIYI LDPELLGASA RPDLPTPTSP LPASPCSPTP
     GSMQGDTALP QGEELIEAAK RNDCCKLQEL HRAGGDLMHR DQKSRTLLHH AVSTGSKEVV
     RYLLDHAPPE ILDAVEENGE TCLHQAAALG QRTICHYIVE AGASLMKTDL QGDTPRQRAE
     KAQDTELAAY LENRQHYQMI QREDQETAV
//
ID   ANO3_MOUSE              Reviewed;         981 AA.
AC   A2AHL1; A2AHL0;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   08-MAR-2011, entry version 30.
DE   RecName: Full=Anoctamin-3;
DE   AltName: Full=Transmembrane protein 16C;
GN   Name=Ano3; Synonyms=Tmem16c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=18729231; DOI=10.1002/dvdy.21676;
RA   Rock J.R., Harfe B.D.;
RT   "Expression of TMEM16 paralogs during murine embryogenesis.";
RL   Dev. Dyn. 237:2566-2574(2008).
CC   -!- FUNCTION: May act as a calcium-activated chloride channel (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A2AHL1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2AHL1-2; Sequence=VSP_052958, VSP_052959;
CC         Note=Gene prediction based on EST data;
CC   -!- DEVELOPMENTAL STAGE: In the developing gastrointestinal tract,
CC       expressed in the intestinal epithelium at E14.5 and in an
CC       incomplete ring of cells in the mesenchyme of the esophagus,
CC       stomach and small intestine at E16.5. In the developing skeleton,
CC       expressed in the perichondria of the neural arch of developing
CC       vertebrae at E14.5 and E16.5. At E14.5, also expressed in
CC       perichondria of developing ribs. At E14.5 and E16.5, detected in
CC       dorsal root ganglia and neural tube. In developing skin,
CC       expression is detected in the most suprabasal layers at E16.5. Not
CC       detected in the lung at E14.5 or E16.5.
CC   -!- SIMILARITY: Belongs to the anoctamin family.
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DR   EMBL; AL731700; CAM18324.1; -; Genomic_DNA.
DR   EMBL; AL731779; CAM18324.1; JOINED; Genomic_DNA.
DR   EMBL; AL731700; CAM18325.1; -; Genomic_DNA.
DR   EMBL; AL731779; CAM18325.1; JOINED; Genomic_DNA.
DR   EMBL; BX005257; CAM18325.1; JOINED; Genomic_DNA.
DR   EMBL; AL731779; CAM25696.1; -; Genomic_DNA.
DR   EMBL; AL731700; CAM25696.1; JOINED; Genomic_DNA.
DR   EMBL; AL731779; CAM25697.1; -; Genomic_DNA.
DR   EMBL; AL731700; CAM25697.1; JOINED; Genomic_DNA.
DR   EMBL; BX005257; CAM25697.1; JOINED; Genomic_DNA.
DR   EMBL; BX005257; CAM27817.1; -; Genomic_DNA.
DR   EMBL; AL731700; CAM27817.1; JOINED; Genomic_DNA.
DR   EMBL; AL731779; CAM27817.1; JOINED; Genomic_DNA.
DR   IPI; IPI00756965; -.
DR   IPI; IPI00757601; -.
DR   RefSeq; NP_001075025.1; NM_001081556.1.
DR   RefSeq; NP_001121575.1; NM_001128103.1.
DR   UniGene; Mm.156043; -.
DR   STRING; A2AHL1; -.
DR   PRIDE; A2AHL1; -.
DR   Ensembl; ENSMUST00000099623; ENSMUSP00000097219; ENSMUSG00000074968.
DR   GeneID; 228432; -.
DR   KEGG; mmu:228432; -.
DR   CTD; 228432; -.
DR   MGI; MGI:3613666; Ano3.
DR   GeneTree; ENSGT00600000084125; -.
DR   HOGENOM; HBG357842; -.
DR   HOVERGEN; HBG069519; -.
DR   InParanoid; A2AHL1; -.
DR   OMA; ERVNPIT; -.
DR   PhylomeDB; A2AHL1; -.
DR   NextBio; 379004; -.
DR   Bgee; A2AHL1; -.
DR   Genevestigator; A2AHL1; -.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   InterPro; IPR007632; Anoctamin.
DR   PANTHER; PTHR12308; DUF590; 1.
DR   Pfam; PF04547; DUF590; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Calcium; Chloride; Chloride channel;
KW   Glycoprotein; Ion transport; Ionic channel; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    981       Anoctamin-3.
FT                                /FTId=PRO_0000353188.
FT   TOPO_DOM      1    403       Cytoplasmic (Potential).
FT   TRANSMEM    404    424       Helical; (Potential).
FT   TOPO_DOM    425    469       Extracellular (Potential).
FT   TRANSMEM    470    490       Helical; (Potential).
FT   TOPO_DOM    491    550       Cytoplasmic (Potential).
FT   TRANSMEM    551    571       Helical; (Potential).
FT   TOPO_DOM    572    592       Extracellular (Potential).
FT   TRANSMEM    593    613       Helical; (Potential).
FT   TOPO_DOM    614    640       Cytoplasmic (Potential).
FT   TRANSMEM    641    661       Helical; (Potential).
FT   TOPO_DOM    662    761       Extracellular (Potential).
FT   TRANSMEM    762    782       Helical; (Potential).
FT   TOPO_DOM    783    810       Cytoplasmic (Potential).
FT   TRANSMEM    811    831       Helical; (Potential).
FT   TOPO_DOM    832    914       Extracellular (Potential).
FT   TRANSMEM    915    935       Helical; (Potential).
FT   TOPO_DOM    936    981       Cytoplasmic (Potential).
FT   CARBOHYD    425    425       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    448    448       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    455    455       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    866    866       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     625    637       EYPRTESEWENSF -> GKFIFLILLVVSK (in
FT                                isoform 2).
FT                                /FTId=VSP_052958.
FT   VAR_SEQ     638    981       Missing (in isoform 2).
FT                                /FTId=VSP_052959.
SQ   SEQUENCE   981 AA;  114568 MW;  E851D80BC49F4977 CRC64;
     MVHHSGSIQS FKQQKGMNIS KSEITTEASL KPSRRSLPCL AQSYAHSKSL SQSASLFQST
     ESESQAPTSV TFLSADKPEH VTSEESRKDS TLKCSFADLS DFCLALGKDK DYLDESEHAN
     YDRSRLLNDF VTKDKPASKT KLSKNDMSYI ASSGLLFKDG KKRIDYILVY RKTNIQYDKR
     NTFEKNLRAE GLMLEKEPAI ANPDIMFIKI HIPWDTLCKY AERLNIRVPF RKKCYYTDQK
     NKSKSRVQNY FKRIKKWMSQ NPMVLDKSAF PELEESDCYT GPFSRARIHH FIINNKDTFF
     SNATRSRIVY HMLERTKYEN GISKVGIRKL ITNGSYIAAF PPHEGAYKSS LPIKTHGPQN
     NRHLLYERWA RWGMWYKHQP LDLIRMYFGE KIGLYFAWLG WYTGMLIPAA VVGLCVFFYG
     LVTMNESQVS QEICKATEVF MCPLCDKNCS LQRLNDSCIY AKVTYLFDNG GTVFFAIFMA
     IWATVFLEFW KRRRSILTYT WDLIEWEEEE ETLRPQFEAK YYRMEVINPI TGKPEPHQPS
     SDKVTRLLVS VSGIFFMISL VITAVFAVVV YRLVVMEQFA SFKWNFVKQH WQFATSGAAV
     CINFIIIMLL NLAYEKIAYL LTNLEYPRTE SEWENSFALK MFLFQFVNLN SSIFYIAFFL
     GRFVGHPGKY NKLFERWRLE ECHPSGCLID LCLQMGVIMF LKQIWNNFME LGYPLIQNWW
     SRHKIKRGIQ DASIPQWEND WNLQPMNIHG LMDEYLEMVL QFGFTTIFVA AFPLAPLLAL
     LNNIIEIRLD AYKFVTQWRR PLPARATDIG IWLGILEGIG ILAVITNAFV IAITSDYIPR
     FVYEYKYGPC ANHVKQNENC LKGYVNNSLS FFDLSELGMG KSGYCRYRDY RGPPWSSKPY
     EFTLQYWHIL AARLAFIIVF EHLVFGIKSF IAYLIPDIPK GLRERIRREK YLVQEMMYEA
     ELEHLQQQRR KSGQPIHHEW P
//
ID   TPRN_MOUSE              Reviewed;         749 AA.
AC   A2AI08; Q3TAJ8; Q3TMR8; Q5FWB3; Q7TNG3; Q8BNM5; Q8R1G4;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 32.
DE   RecName: Full=Taperin;
GN   Name=Tprn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 135-749.
RC   STRAIN=FVB/N; TISSUE=Brain, and Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184; SER-457 AND
RP   SER-501, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [5]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=20170899; DOI=10.1016/j.ajhg.2010.01.030;
RA   Rehman A.U., Morell R.J., Belyantseva I.A., Khan S.Y., Boger E.T.,
RA   Shahzad M., Ahmed Z.M., Riazuddin S., Khan S.N., Riazuddin S.,
RA   Friedman T.B.;
RT   "Targeted capture and next-generation sequencing identifies C9orf75,
RT   encoding taperin, as the mutated gene in nonsyndromic deafness
RT   DFNB79.";
RL   Am. J. Hum. Genet. 86:378-388(2010).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=20170898; DOI=10.1016/j.ajhg.2010.02.003;
RA   Li Y., Pohl E., Boulouiz R., Schraders M., Nurnberg G., Charif M.,
RA   Admiraal R.J., von Ameln S., Baessmann I., Kandil M., Veltman J.A.,
RA   Nurnberg P., Kubisch C., Barakat A., Kremer H., Wollnik B.;
RT   "Mutations in TPRN cause a progressive form of autosomal-recessive
RT   nonsyndromic hearing loss.";
RL   Am. J. Hum. Genet. 86:479-484(2010).
CC   -!- SUBCELLULAR LOCATION: Cell projection, stereocilium.
CC       Note=Localized prominently at the taper regions of hair cell
CC       stereocilia.
CC   -!- TISSUE SPECIFICITY: Expressed in the sensory epithelia of the
CC       organ of Corti and vestibular end organs and, to a lesser extent,
CC       in Reisner's membrane and the spiral ligament (at protein level).
CC       At postnatal day 2, expression is detected in cochlea, liver,
CC       brain, kidney, heart and lung.
CC   -!- SIMILARITY: Belongs to the taperin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH89508.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAC38669.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAC38669.1; Type=Frameshift; Positions=241;
CC       Sequence=BAE38373.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAE42670.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAE42670.1; Type=Frameshift; Positions=180;
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DR   EMBL; AK082888; BAC38669.1; ALT_SEQ; mRNA.
DR   EMBL; AK165772; BAE38373.1; ALT_INIT; mRNA.
DR   EMBL; AK171799; BAE42670.1; ALT_SEQ; mRNA.
DR   EMBL; AL732309; CAM14678.1; -; Genomic_DNA.
DR   EMBL; BC024573; AAH24573.1; -; mRNA.
DR   EMBL; BC055478; AAH55478.1; -; mRNA.
DR   EMBL; BC089508; AAH89508.1; ALT_INIT; mRNA.
DR   IPI; IPI00223286; -.
DR   RefSeq; NP_780495.2; NM_175286.4.
DR   UniGene; Mm.308539; -.
DR   PhosphoSite; A2AI08; -.
DR   PRIDE; A2AI08; -.
DR   Ensembl; ENSMUST00000114336; ENSMUSP00000109975; ENSMUSG00000048707.
DR   GeneID; 97031; -.
DR   KEGG; mmu:97031; -.
DR   CTD; 97031; -.
DR   MGI; MGI:2139535; Tprn.
DR   eggNOG; roNOG06079; -.
DR   GeneTree; ENSGT00530000064035; -.
DR   HOVERGEN; HBG107679; -.
DR   InParanoid; A2AI08; -.
DR   OMA; NDSFEIR; -.
DR   OrthoDB; EOG4TF0KS; -.
DR   NextBio; 352461; -.
DR   Bgee; A2AI08; -.
DR   Genevestigator; A2AI08; -.
DR   GO; GO:0032420; C:stereocilium; IDA:UniProtKB.
DR   GO; GO:0007605; P:sensory perception of sound; ISS:UniProtKB.
PE   1: Evidence at protein level;
KW   Cell projection; Hearing; Phosphoprotein.
FT   CHAIN         1    749       Taperin.
FT                                /FTId=PRO_0000330310.
FT   COMPBIAS    106    321       Pro-rich.
FT   COMPBIAS    637    665       Glu-rich.
FT   MOD_RES     184    184       Phosphoserine.
FT   MOD_RES     457    457       Phosphoserine.
FT   MOD_RES     501    501       Phosphoserine.
FT   CONFLICT    264    264       P -> T (in Ref. 1; BAE38373).
FT   CONFLICT    265    265       T -> A (in Ref. 1; BAE42670).
FT   CONFLICT    432    432       A -> V (in Ref. 1; BAE42670).
FT   CONFLICT    527    527       A -> D (in Ref. 1; BAE42670).
FT   CONFLICT    531    532       HT -> DN (in Ref. 1; BAE42670).
FT   CONFLICT    650    650       Missing (in Ref. 1; BAE42670).
FT   CONFLICT    671    671       E -> G (in Ref. 3; AAH89508).
SQ   SEQUENCE   749 AA;  80089 MW;  02E3D12D60051082 CRC64;
     MAGLGRLDPG PRTVMPAWKR EILERRRAKL AALSGGQGSG AAPDGPNERL VLAESLGPLS
     QNPFMRLESE RRRGTRPAQQ LLELYCRVPG VRTIRADNIL IIESAPGFPP AVPPAAGIRA
     AEVVVYEAPQ PGRVSRLLEK FDSPAAPCRR GSPERFRPAL PQLPVASASA ATRTPTNRSL
     APASPVRLSQ PAPPISPVPV AQRAGQRSAC CEPAHPDGTA GPGARRSDFL QKTGSNSFTV
     HPRGLPRSAV NRSLSNGPMT QESPTGPANG LSGSPPVPGK WKPKVESKEP SLHPPPSPGT
     PSATSVGPPA FPAPSPASAT PSQRQWVSSA TSANDSFEIR PSSKPDMETI PIGDLQARAL
     ANLRVNSRNS FVLIPKRKAP GNYPLAGRQF EEPKGEVGWA SQSQGLGSQL VSTVDGAPAL
     EKSPLAAEMQ WAVRKGACPR PAISDTDKCV RWQRPASPPP FLPATAEAEP AEGLGVPGLA
     KNGQEPVRPG LPVTFIDEVD SEEEAFQEAK LPSSAVGVPS QYHLHPARPG HTSELLNRGS
     NTFTVVPKRK PGTLQEPHLS QTNGQSQQGA EEQDAESLSG PHTTLENTLK KRYPTVHEIE
     VIGGYLALQK SCLIKAGSSR KKMKISFNDK SLHTTFEYPS ESSLAQEEAE EEEEEEGEED
     GEEEEVGPDS EKPFTVFLPR ATFVSSVGPE SSSGLSSYTP KHSMAFSKWQ EQTLVQTPTD
     VELPPKEVML TPASQNDLSD FRSEPALYF
//
ID   A2AI14_MOUSE            Unreviewed;       943 AA.
AC   A2AI14;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 39.
DE   SubName: Full=Glutamate receptor ionotropic NMDA1 (Zeta 1);
GN   Name=Grin1; ORFNames=RP23-132N23.20-006;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Leongamornlert D.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL732309; CAM14684.1; -; Genomic_DNA.
DR   IPI; IPI00753459; -.
DR   UniGene; Mm.278672; -.
DR   ProteinModelPortal; A2AI14; -.
DR   SMR; A2AI14; 417-821.
DR   STRING; A2AI14; -.
DR   PRIDE; A2AI14; -.
DR   Ensembl; ENSMUST00000114318; ENSMUSP00000109957; ENSMUSG00000026959.
DR   MGI; MGI:95819; Grin1.
DR   GeneTree; ENSGT00590000083017; -.
DR   HOVERGEN; HBG052638; -.
DR   Bgee; A2AI14; -.
DR   Genevestigator; A2AI14; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0043197; C:dendritic spine; IDA:MGI.
DR   GO; GO:0017146; C:N-methyl-D-aspartate selective glutamate receptor complex; IPI:MGI.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
DR   GO; GO:0005262; F:calcium channel activity; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR   GO; GO:0005516; F:calmodulin binding; IDA:MGI.
DR   GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0004972; F:N-methyl-D-aspartate selective glutamate receptor activity; IDA:MGI.
DR   GO; GO:0005102; F:receptor binding; IPI:MGI.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
DR   GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR   GO; GO:0001661; P:conditioned taste aversion; IMP:MGI.
DR   GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:MGI.
DR   GO; GO:0007616; P:long-term memory; IMP:MGI.
DR   GO; GO:0060179; P:male mating behavior; IMP:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptosis; IGI:MGI.
DR   GO; GO:0008355; P:olfactory learning; IMP:MGI.
DR   GO; GO:0021586; P:pons maturation; IMP:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptosis; IGI:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0060134; P:prepulse inhibition; IMP:MGI.
DR   GO; GO:0050770; P:regulation of axonogenesis; IMP:MGI.
DR   GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:MGI.
DR   GO; GO:0060079; P:regulation of excitatory postsynaptic membrane potential; IMP:MGI.
DR   GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:MGI.
DR   GO; GO:0043576; P:regulation of respiratory gaseous exchange; IMP:MGI.
DR   GO; GO:0051963; P:regulation of synaptogenesis; IMP:MGI.
DR   GO; GO:0007585; P:respiratory gaseous exchange; IMP:MGI.
DR   GO; GO:0001975; P:response to amphetamine; IMP:MGI.
DR   GO; GO:0043278; P:response to morphine; IMP:MGI.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR   GO; GO:0035176; P:social behavior; IMP:MGI.
DR   GO; GO:0001967; P:suckling behavior; IMP:MGI.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR018882; CaM-bd_C0_NMDA_rcpt_NR1.
DR   InterPro; IPR019594; Glu_rcpt_Glu/Gly-bd.
DR   InterPro; IPR001320; Iontro_glu_rcpt.
DR   InterPro; IPR001508; NMDA_rcpt.
DR   InterPro; IPR001638; SBP_bac_3.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF10562; CaM_bdg_C0; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   PRINTS; PR00177; NMDARECEPTOR.
DR   SMART; SM00918; Lig_chan-Glu_bd; 1.
DR   SMART; SM00079; PBPe; 1.
PE   4: Predicted;
KW   Cell junction; Cell membrane; Ion transport; Ionic channel;
KW   Ligand-gated ion channel; Membrane; Postsynaptic cell membrane;
KW   Receptor; Synapse; Transmembrane; Transmembrane helix; Transport.
SQ   SEQUENCE   943 AA;  106123 MW;  22A334C71B7DA487 CRC64;
     MSTMHLLTFA LLFSCSFARA ACDPKIVNIG AVLSTRKHEQ MFREAVNQAN KRHGSWKIQL
     NATSVTHKPN AIQMALSVCE DLISSQVYAI LVSHPPTPND HFTPTPVSYT AGFYRIPVLG
     LTTRMSIYSD KSIHLSFLRT VPPYSHQSSV WFEMMRVYNW NHIILLVSDD HEGRAAQKRL
     ETLLEERESK SKKRNYENLD QLSYDNKRGP KAEKVLQFDP GTKNVTALLM EARDLEARVI
     ILSASEDDAA TVYRAAAMLN MTGSGYVWLV GEREISGNAL RYAPDGIIGL QLINGKNESA
     HISDAVGVVA QAVHELLEKE NITDPPRGCV GNTNIWKTGP LFKRVLMSSK YADGVTGRVE
     FNEDGDRKFA NYSIMNLQNR KLVQVGIYNG THVIPNDRKI IWPGGETEKP RGYQMSTRLK
     IVTIHQEPFV YVKPTMSDGT CKEEFTVNGD PVKKVICTGP NDTSPGSPRH TVPQCCYGFC
     VDLLIKLART MNFTYEVHLV ADGKFGTQER VNNSNKKEWN GMMGELLSGQ ADMIVAPLTI
     NNERAQYIEF SKPFKYQGLT ILVKKEIPRS TLDSFMQPFQ STLWLLVGLS VHVVAVMLYL
     LDRFSPFGRF KVNSEEEEED ALTLSSAMWF SWGVLLNSGI GEGAPRSFSA RILGMVWAGF
     AMIIVASYTA NLAAFLVLDR PEERITGIND PRLRNPSDKF IYATVKQSSV DIYFRRQVEL
     STMYRHMEKH NYESAAEAIQ AVRDNKLHAF IWDSAVLEFE ASQKCDLVTT GELFFRSGFG
     IGMRKDSPWK QNVSLSILKS HENGFMEDLD KTWVRYQECD SRSNAPATLT FENMAGVFML
     VAGGIVAGIF LIFIEIAYKR HKDARRKQMQ LAFAAVNVWR KNLQDRKSGR AEPDPKKKAT
     FRAITSTLAS SFKRRRSSKD TQYHPTDITG PLNLSDPSVS TVV
//
ID   A2AI16_MOUSE            Unreviewed;       906 AA.
AC   A2AI16;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 39.
DE   SubName: Full=Glutamate receptor ionotropic NMDA1 (Zeta 1);
GN   Name=Grin1; ORFNames=RP23-132N23.20-010;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Leongamornlert D.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL732309; CAM14686.1; -; Genomic_DNA.
DR   IPI; IPI00755985; -.
DR   RefSeq; NP_001171127.1; NM_001177656.1.
DR   UniGene; Mm.278672; -.
DR   ProteinModelPortal; A2AI16; -.
DR   SMR; A2AI16; 417-821.
DR   STRING; A2AI16; -.
DR   Ensembl; ENSMUST00000114317; ENSMUSP00000109956; ENSMUSG00000026959.
DR   GeneID; 14810; -.
DR   KEGG; mmu:14810; -.
DR   CTD; 14810; -.
DR   MGI; MGI:95819; Grin1.
DR   GeneTree; ENSGT00590000083017; -.
DR   HOVERGEN; HBG052638; -.
DR   Bgee; A2AI16; -.
DR   Genevestigator; A2AI16; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0043197; C:dendritic spine; IDA:MGI.
DR   GO; GO:0017146; C:N-methyl-D-aspartate selective glutamate receptor complex; IPI:MGI.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
DR   GO; GO:0005262; F:calcium channel activity; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR   GO; GO:0005516; F:calmodulin binding; IDA:MGI.
DR   GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0004972; F:N-methyl-D-aspartate selective glutamate receptor activity; IDA:MGI.
DR   GO; GO:0005102; F:receptor binding; IPI:MGI.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
DR   GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR   GO; GO:0001661; P:conditioned taste aversion; IMP:MGI.
DR   GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:MGI.
DR   GO; GO:0007616; P:long-term memory; IMP:MGI.
DR   GO; GO:0060179; P:male mating behavior; IMP:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptosis; IGI:MGI.
DR   GO; GO:0008355; P:olfactory learning; IMP:MGI.
DR   GO; GO:0021586; P:pons maturation; IMP:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptosis; IGI:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0060134; P:prepulse inhibition; IMP:MGI.
DR   GO; GO:0050770; P:regulation of axonogenesis; IMP:MGI.
DR   GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:MGI.
DR   GO; GO:0060079; P:regulation of excitatory postsynaptic membrane potential; IMP:MGI.
DR   GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:MGI.
DR   GO; GO:0043576; P:regulation of respiratory gaseous exchange; IMP:MGI.
DR   GO; GO:0051963; P:regulation of synaptogenesis; IMP:MGI.
DR   GO; GO:0007585; P:respiratory gaseous exchange; IMP:MGI.
DR   GO; GO:0001975; P:response to amphetamine; IMP:MGI.
DR   GO; GO:0043278; P:response to morphine; IMP:MGI.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR   GO; GO:0035176; P:social behavior; IMP:MGI.
DR   GO; GO:0001967; P:suckling behavior; IMP:MGI.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR018882; CaM-bd_C0_NMDA_rcpt_NR1.
DR   InterPro; IPR019594; Glu_rcpt_Glu/Gly-bd.
DR   InterPro; IPR001320; Iontro_glu_rcpt.
DR   InterPro; IPR001508; NMDA_rcpt.
DR   InterPro; IPR001638; SBP_bac_3.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF10562; CaM_bdg_C0; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   PRINTS; PR00177; NMDARECEPTOR.
DR   SMART; SM00918; Lig_chan-Glu_bd; 1.
DR   SMART; SM00079; PBPe; 1.
PE   4: Predicted;
KW   Cell junction; Cell membrane; Ion transport; Ionic channel;
KW   Ligand-gated ion channel; Membrane; Postsynaptic cell membrane;
KW   Receptor; Synapse; Transmembrane; Transmembrane helix; Transport.
SQ   SEQUENCE   906 AA;  101959 MW;  5DE227FF6E93B57F CRC64;
     MSTMHLLTFA LLFSCSFARA ACDPKIVNIG AVLSTRKHEQ MFREAVNQAN KRHGSWKIQL
     NATSVTHKPN AIQMALSVCE DLISSQVYAI LVSHPPTPND HFTPTPVSYT AGFYRIPVLG
     LTTRMSIYSD KSIHLSFLRT VPPYSHQSSV WFEMMRVYNW NHIILLVSDD HEGRAAQKRL
     ETLLEERESK SKKRNYENLD QLSYDNKRGP KAEKVLQFDP GTKNVTALLM EARDLEARVI
     ILSASEDDAA TVYRAAAMLN MTGSGYVWLV GEREISGNAL RYAPDGIIGL QLINGKNESA
     HISDAVGVVA QAVHELLEKE NITDPPRGCV GNTNIWKTGP LFKRVLMSSK YADGVTGRVE
     FNEDGDRKFA NYSIMNLQNR KLVQVGIYNG THVIPNDRKI IWPGGETEKP RGYQMSTRLK
     IVTIHQEPFV YVKPTMSDGT CKEEFTVNGD PVKKVICTGP NDTSPGSPRH TVPQCCYGFC
     VDLLIKLART MNFTYEVHLV ADGKFGTQER VNNSNKKEWN GMMGELLSGQ ADMIVAPLTI
     NNERAQYIEF SKPFKYQGLT ILVKKEIPRS TLDSFMQPFQ STLWLLVGLS VHVVAVMLYL
     LDRFSPFGRF KVNSEEEEED ALTLSSAMWF SWGVLLNSGI GEGAPRSFSA RILGMVWAGF
     AMIIVASYTA NLAAFLVLDR PEERITGIND PRLRNPSDKF IYATVKQSSV DIYFRRQVEL
     STMYRHMEKH NYESAAEAIQ AVRDNKLHAF IWDSAVLEFE ASQKCDLVTT GELFFRSGFG
     IGMRKDSPWK QNVSLSILKS HENGFMEDLD KTWVRYQECD SRSNAPATLT FENMAGVFML
     VAGGIVAGIF LIFIEIAYKR HKDARRKQMQ LAFAAVNVWR KNLQQYHPTD ITGPLNLSDP
     SVSTVV
//
ID   1A1L1_MOUSE             Reviewed;         502 AA.
AC   A2AIG8; Q8CHS6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 35.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate synthase-like protein 1;
DE            Short=ACC synthase-like protein 1;
GN   Name=Accs;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Does not catalyze the synthesis of 1-aminocyclopropane-
CC       1-carboxylate but is capable of catalyzing the deamination of L-
CC       vinylglycine (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A2AIG8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2AIG8-2; Sequence=VSP_052669;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family.
CC   -!- CAUTION: Similar to plant 1-aminocyclopropane-1-carboxylate
CC       synthases but lacks a number of residues which are necessary for
CC       activity.
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DR   EMBL; AL732472; CAM23884.1; -; Genomic_DNA.
DR   EMBL; AL732472; CAM23885.1; -; Genomic_DNA.
DR   EMBL; BC039569; AAH39569.1; -; mRNA.
DR   IPI; IPI00229717; -.
DR   IPI; IPI00750758; -.
DR   RefSeq; NP_899043.1; NM_183220.2.
DR   UniGene; Mm.86901; -.
DR   ProteinModelPortal; A2AIG8; -.
DR   SMR; A2AIG8; 64-481.
DR   STRING; A2AIG8; -.
DR   PRIDE; A2AIG8; -.
DR   Ensembl; ENSMUST00000041593; ENSMUSP00000036268; ENSMUSG00000040272.
DR   Ensembl; ENSMUST00000111246; ENSMUSP00000106877; ENSMUSG00000040272.
DR   GeneID; 329470; -.
DR   KEGG; mmu:329470; -.
DR   CTD; 329470; -.
DR   MGI; MGI:1919717; Accs.
DR   HOGENOM; HBG713659; -.
DR   HOVERGEN; HBG055243; -.
DR   InParanoid; A2AIG8; -.
DR   OMA; RDRDWIN; -.
DR   OrthoDB; EOG4P8FJ0; -.
DR   Bgee; A2AIG8; -.
DR   Genevestigator; A2AIG8; -.
DR   GO; GO:0016847; F:1-aminocyclopropane-1-carboxylate synthase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016769; F:transferase activity, transferring nitrogenous groups; IEA:InterPro.
DR   InterPro; IPR001176; ACC_synthase.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase_major_dom.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 2.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00753; ACCSYNTHASE.
DR   SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Pyridoxal phosphate.
FT   CHAIN         1    502       1-aminocyclopropane-1-carboxylate
FT                                synthase-like protein 1.
FT                                /FTId=PRO_0000318072.
FT   BINDING     106    106       Substrate (By similarity).
FT   MOD_RES     324    324       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
FT   VAR_SEQ       1     23       Missing (in isoform 2).
FT                                /FTId=VSP_052669.
SQ   SEQUENCE   502 AA;  56879 MW;  9399891308FC91A0 CRC64;
     MFCLPQQEST APTTCTGSAS TQDMDSGYGD GLQGECLRKP DQTQPKLYGV GDPTATFSSD
     SSCLSSRGRV IKWFWDSAEE GYRTYHMDEY DEDKNPSGII NLGTSENKLC FDLLSWRLTQ
     GDMLHVEPSL LQYPDWRGHL FLREEVAKFL SFYCKSPAPL KPENVVVLNG CASLFSALAT
     VLCEAGEALL IPTPYYGAIT QHIYLYGNVR LAYVYLDSKV TGLNTRPFQL TVEKLEMVLQ
     GVSSEGVKVK GLILINPQNP LGDVYSPEEL QDFLRFAMRH KLHVIMDEVY MLSVFEESLG
     YRSVLSLERL PDPQRTHVMW ATSKDFGMSG LRFGVLYTEN QHVATAVASL CRYHGLSGLV
     QHQMAQLLRD HDWISQVYLP ENHARLKAAH TYVSEELRAL GIPFVSRGAG FFIWVDLRKY
     LCKGTFEEEA LLWRQFLDNK VLLSSGKTFE CKEPGWFRVV FSDKENRLRL GMQRMRQVLE
     GQSQVVEDAS PCHAQEPQSQ PR
//
ID   A2AIR4_MOUSE            Unreviewed;      1115 AA.
AC   A2AIR4;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 42.
DE   SubName: Full=Glutamate receptor ionotropic, NMDA3A;
GN   Name=Grin3a; ORFNames=RP23-134A17.2-002;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Wallis J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Lad H.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL807392; CAM13396.1; -; Genomic_DNA.
DR   EMBL; AL732521; CAM13396.1; JOINED; Genomic_DNA.
DR   EMBL; AL732521; CAM14733.1; -; Genomic_DNA.
DR   EMBL; AL807392; CAM14733.1; JOINED; Genomic_DNA.
DR   IPI; IPI00648365; -.
DR   RefSeq; NP_001028523.1; NM_001033351.1.
DR   UniGene; Mm.440095; -.
DR   ProteinModelPortal; A2AIR4; -.
DR   SMR; A2AIR4; 512-911.
DR   STRING; A2AIR4; -.
DR   PRIDE; A2AIR4; -.
DR   Ensembl; ENSMUST00000076674; ENSMUSP00000075970; ENSMUSG00000039579.
DR   GeneID; 242443; -.
DR   KEGG; mmu:242443; -.
DR   CTD; 242443; -.
DR   MGI; MGI:1933206; Grin3a.
DR   HOVERGEN; HBG052634; -.
DR   NextBio; 385347; -.
DR   Bgee; A2AIR4; -.
DR   Genevestigator; A2AIR4; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR   GO; GO:0005262; F:calcium channel activity; IDA:MGI.
DR   GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0004972; F:N-methyl-D-aspartate selective glutamate receptor activity; IMP:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0016358; P:dendrite development; IMP:MGI.
DR   GO; GO:0060134; P:prepulse inhibition; IMP:MGI.
DR   InterPro; IPR019594; Glu_rcpt_Glu/Gly-bd.
DR   InterPro; IPR001320; Iontro_glu_rcpt.
DR   InterPro; IPR001508; NMDA_rcpt.
DR   InterPro; IPR001638; SBP_bac_3.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   PRINTS; PR00177; NMDARECEPTOR.
DR   SMART; SM00918; Lig_chan-Glu_bd; 1.
DR   SMART; SM00079; PBPe; 1.
PE   4: Predicted;
KW   Cell junction; Cell membrane; Ion transport; Ionic channel;
KW   Ligand-gated ion channel; Membrane; Postsynaptic cell membrane;
KW   Receptor; Synapse; Transmembrane; Transmembrane helix; Transport.
SQ   SEQUENCE   1115 AA;  125105 MW;  C10145036DF07774 CRC64;
     MRRLSLWWLL SRVCLLLPPP CALVLAGVPS SSSHPQPCQI LKRIGHAVRV GAVHLQPWTT
     APRAASRAQD GGRAGAQRDE PESGTWRPPA PSQGARWLGS ALHGRGPPGS RKLGEGAGTE
     TLWPRDALLF AVENLNRVEG LLPYNLSLEV VMAIEAGLGD LPLMPFSSPS SPWSSDPFSF
     LQSVCHTVVV QGVSALLAFP QSQGEMMELD LVSSVLHIPV LSIVRHEFPR ESQNPLHLQL
     SLENSLSSDA DVTVSILTMN NWYNFSLLLC QEDWNITDFL LLTENNSKFH LESIINITAN
     LSSTKDLLSF LQVQLENIRN STPTMVMFGC DMGSIRQIFE MSTQFGLSPP DLHWVLGDSQ
     NVEELRTEGL PLGLIAHGKT TQSVFEYYVQ DAMELVARAV ATATMIQPEL ALLPSTMNCM
     DVKTTNLTSG QYLSRFLANT TFRGLSGSIK VKGSTIVSSE NNFFIWNLQY DPMGKPMWTR
     LGSWQGGRIV MDSGIWPEQA QRHKTHFHHP NKLHLRVVTL IEHPFVFTRE VDDEGLCPAG
     QLCLDPMTND SSILDSLFSS LHSSNDTVPI KFKKCCYGYC IDLLEQLAED MNFDFDLYIV
     GDGKYGAWKN GHWTGLVGDL LSGTANMAVT SFSINTARSQ VIDFTSPFFS TSLGILVRTR
     DTAAPIGAFM WPLHWTMWLG IFVALHITAI FLTLYEWKSP FGMTPKGRNR NKVFSFSSAL
     NVCYALLFGR TAAIKPPKCW TGRFLMNLWA IFCMFCLSTY TANLAAVMVG EKIYEELSGI
     HDPKLHHPSQ GFRFGTVRES SAEDYVRQSF PEMHEYMRRY NVPATPDGVQ YLKNDPEKLD
     AFIMDKALLD YEVSIDADCK LLTVGKPFAI EGYGIGLPPN SPLTSNISEL ISQYKSHGFM
     DVLHDKWYKV VPCGKRSFAV TETLQMGIKH FSGLFVLLCI GFGLSILTTI GEHIVYRLLL
     PRIKNKSKLQ YWLHTSQRFH RALNTSFVEE KQPCSKTKRV EKRSNMGPQQ LMVWNTSNLS
     HDNQRKYIFN DEEGQNQLGT QTHQDIPLPP RRRELPASLT TNGKADSLNV ARNSVMQELS
     ELEKQIQVIR QELQLAVSRK TELEEYQRTN RTCES
//
ID   A2AIR7_MOUSE            Unreviewed;      2328 AA.
AC   A2AIR7;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   SubName: Full=Calcium channel, voltage-dependent, N type, alpha 1B subunit;
GN   Name=Cacna1b; ORFNames=RP23-264D16.5-003;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Leongamornlert D.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Griffiths C.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RA   Howden P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family.
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DR   EMBL; AL732546; CAM19042.1; -; Genomic_DNA.
DR   EMBL; AL732525; CAM19042.1; JOINED; Genomic_DNA.
DR   EMBL; BX294112; CAM19042.1; JOINED; Genomic_DNA.
DR   EMBL; AL732525; CAM22107.1; -; Genomic_DNA.
DR   EMBL; AL732546; CAM22107.1; JOINED; Genomic_DNA.
DR   EMBL; BX294112; CAM22107.1; JOINED; Genomic_DNA.
DR   EMBL; BX294112; CAM27788.1; -; Genomic_DNA.
DR   EMBL; AL732525; CAM27788.1; JOINED; Genomic_DNA.
DR   EMBL; AL732546; CAM27788.1; JOINED; Genomic_DNA.
DR   IPI; IPI00466672; -.
DR   UniGene; Mm.4424; -.
DR   ProteinModelPortal; A2AIR7; -.
DR   STRING; A2AIR7; -.
DR   Ensembl; ENSMUST00000114447; ENSMUSP00000110090; ENSMUSG00000004113.
DR   MGI; MGI:88296; Cacna1b.
DR   eggNOG; roNOG13514; -.
DR   HOVERGEN; HBG050763; -.
DR   Bgee; A2AIR7; -.
DR   Genevestigator; A2AIR7; -.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0007269; P:neurotransmitter secretion; IMP:MGI.
DR   GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR   GO; GO:0008016; P:regulation of heart contraction; IMP:MGI.
DR   GO; GO:0048265; P:response to pain; IMP:MGI.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005447; VDCC_N_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01631; NVDCCALPHA1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   3: Inferred from homology;
KW   Calcium; Calcium channel; Calcium transport; Ion transport;
KW   Ionic channel; Membrane; Transmembrane; Transport;
KW   Voltage-gated channel.
SQ   SEQUENCE   2328 AA;  261552 MW;  CB9D5BCC9FEB8BBB CRC64;
     MVRFGDELGG RYGGTGGGER ARGGGAGGAG GPGQGGLPPG QRVLYKQSIA QRARTMALYN
     PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPPFEYM ILATIIANCI VLALEQHLPD
     GDKTPMSERL DDTEPYFIGI FCFEAGIKII ALGFVFHKGS YLRNGWNVMD FVVVLTGILA
     TAGTDFDLRT LRAVRVLRPL KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAILMFAII
     GLEFYMGKFH KACFPNSTDT EPVGDFPCGK DPPARQCDGD TECREYWPGP NFGITNFDNI
     LFAILTVFQC ITMEGWTDIL YNTNDAAGNT WNWLYFIPLI IIGSFFMLNL VLGVLSGEFA
     KERERVENRR AFLKLRRQQQ IERELNGYLE WIFKAEEVML AEEDKNAEEK SPLDAVLKRA
     ATKKSRNDLI HAEEGEDRFV DLCAVGSPFA RASLKSGKTE SSSYFRRKEK MFRFFIRRMV
     KAQSFYWVVL CVVALNTLCV AMVHYNQPQR LTTALYFAEF VFLGLFLTEM SLKMYGLGPR
     SYFRSSFNCF DFGVIVGSIF EVVWAAIKPG TSFGISVLRA LRLLRIFKVT KYWNSLRNLV
     VSLLNSMKSI ISLLFLLFLF IVVFALLGMQ LFGGQFNFQD ETPTTNFDTF PAAILTVFQI
     LTGEDWNAVM YHGIESQGGV SKGMFSSFYF IVLTLFGNYT LLNVFLAIAV DNLANAQELT
     KDEEEMEEAA NQKLALQKAK EVAEVSPMSA ANISIAARQQ NSAKARSVWE QRASQLRLQN
     LRASCEALYS EMDPEERLRY ASTRHVRPDM KTHMDRPLVV EPGRDGLRGP VGSKSKPEGT
     EATESADLPR RHHRHRDRDK TSATAPAGGE QDRTESTETG AREERARPRR SHSKETPGAD
     TQVRCERSRR HHRRGSPEEA TEREPRRHRA HRHAQDSSKE GTAPVLVPKG ERRARHRGPR
     TGPREAENNE EPTRRHRARH KVPPTLQPPE REAAEKESNA VEGDKETRNH QPKEPHCDLE
     AIAVTGVGPL HMLPSTCLQK VDEQPEDADN QRNVTRMGSQ PSDPSTTVHV PVTLTGPPGE
     TPVVPSGNMN LEGQAEGKKE AEADDVLRRG PRPIVPYSSM FCLSPTNLLR RFCHYIVTMR
     YFEMVILVVI ALSSIALAAE DPVRTDSFRN NALKYMDYIF TGVFTFEMVI KMIDLGLLLH
     PGAYFRDLWN ILDFIVVSGA LVAFAFSSFM GGSKGKDINT IKSLRVLRVL RPLKTIKRLP
     KLKAVFDCVV NSLKNVLNIL IVYMLFMFIF AVIAVQLFKG KFFYCTDESK ELERDCRGQY
     LDYEKEEVEA QPRQWKKYDF HYDNVLWALL TLFTVSTGEG WPMVLKHSVD ATYEEQGPSP
     GFRMELSIFY VVYFVVFPFF FVNIFVALII ITFQEQGDKV MSECSLEKNE RACIDFAISA
     KPLTRYMPQN KQSFQYKTWT FVVSPPFEYF IMAMIALNTV VLMMKFYDAP YEYELMLKCL
     NIVFTSMFSM ECILKIIAFG VLNYFRDAWN VFDFVTVLGS ITDILVTEIA NNFINLSFLR
     LFRAARLIKL LRQGYTIRIL LWTFVQSFKA LPYVCLLIAM LFFIYAIIGM QVFGNIALDD
     DTSINRHNNF RTFLQALMLL FRSATGEAWH EIMLSCLGNR ACDPHANASE CGSDFAYFYF
     VSFIFLCSFL MLNLFVAVIM DNFEYLTRDS SILGPHHLDE FIRVWAEYDP AACGRISYND
     MFEMLKHMSP PLGLGKKCPA RVAYKRLVRM NMPISNEDMT VHFTSTLMAL IRTALEIKLA
     PAGTKQHQCD AELRKEISSV WANLPQKTLD LLVPPHKPDE MTVGKVYAAL MIFDFYKQNK
     TTRDQTHQAP GGLSQMGPVS LFHPLKATLE QTQPAVLRGA RVFLRQKSAT SLSNGGAIQT
     QESGIKESLS WGTQRTQDAL YEARAPLERG HSAEIPVGQS GTLAVDVQMQ NMTLRGPDGE
     PQPGLESQGR AASMPRLAAE TQPAPNASPM KRSISTLAPR PHGTQLCSTV LDRPPPSQAS
     HHHHHRCHRR RDKKQRSLEK GPSLSVDPEG APSTAAGPGL PHGEGSTACR RDRKQERGRS
     QERRQPSSSS SEKQRFYSCD RFGSREPPQL MPSLSSHPTS PTAALEPAPH PQGSGSVNGS
     PLMSTSGAST PGRGGRRQLP QTPLTPRPSI TYKTANSSPV HFAEGQSGLP AFSPGRLSRG
     LSEHNALLQK EPLSQPLAPG SRIGSDPYLG QRLDSEASAH TLPEDTLTFE EAVATNSGRS
     SRTSYVSSLT SQSHPLRRVP NGYHCTLGLS TGVRARHSYH HPDQDHWC
//
ID   A2AIS0_MOUSE            Unreviewed;      2288 AA.
AC   A2AIS0;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   SubName: Full=Calcium channel, voltage-dependent, N type, alpha 1B subunit;
GN   Name=Cacna1b; ORFNames=RP23-264D16.5-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Leongamornlert D.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Griffiths C.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RA   Howden P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family.
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DR   EMBL; AL732546; CAM19043.1; -; Genomic_DNA.
DR   EMBL; AL732525; CAM19043.1; JOINED; Genomic_DNA.
DR   EMBL; BX294112; CAM19043.1; JOINED; Genomic_DNA.
DR   EMBL; AL732525; CAM22110.1; -; Genomic_DNA.
DR   EMBL; AL732546; CAM22110.1; JOINED; Genomic_DNA.
DR   EMBL; BX294112; CAM22110.1; JOINED; Genomic_DNA.
DR   EMBL; BX294112; CAM27786.1; -; Genomic_DNA.
DR   EMBL; AL732525; CAM27786.1; JOINED; Genomic_DNA.
DR   EMBL; AL732546; CAM27786.1; JOINED; Genomic_DNA.
DR   IPI; IPI00625414; -.
DR   RefSeq; NP_031605.2; NM_007579.2.
DR   UniGene; Mm.4424; -.
DR   ProteinModelPortal; A2AIS0; -.
DR   STRING; A2AIS0; -.
DR   PRIDE; A2AIS0; -.
DR   Ensembl; ENSMUST00000070864; ENSMUSP00000063236; ENSMUSG00000004113.
DR   GeneID; 12287; -.
DR   KEGG; mmu:12287; -.
DR   CTD; 12287; -.
DR   MGI; MGI:88296; Cacna1b.
DR   HOVERGEN; HBG050763; -.
DR   OrthoDB; EOG48KR9C; -.
DR   NextBio; 280760; -.
DR   Bgee; A2AIS0; -.
DR   Genevestigator; A2AIS0; -.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0007269; P:neurotransmitter secretion; IMP:MGI.
DR   GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR   GO; GO:0008016; P:regulation of heart contraction; IMP:MGI.
DR   GO; GO:0048265; P:response to pain; IMP:MGI.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005447; VDCC_N_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01631; NVDCCALPHA1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   3: Inferred from homology;
KW   Calcium; Calcium channel; Calcium transport; Ion transport;
KW   Ionic channel; Membrane; Transmembrane; Transport;
KW   Voltage-gated channel.
SQ   SEQUENCE   2288 AA;  257072 MW;  2847EB88FE600366 CRC64;
     MVRFGDELGG RYGGTGGGER ARGGGAGGAG GPGQGGLPPG QRVLYKQSIA QRARTMALYN
     PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPPFEYM ILATIIANCI VLALEQHLPD
     GDKTPMSERL DDTEPYFIGI FCFEAGIKII ALGFVFHKGS YLRNGWNVMD FVVVLTGILA
     TAGTDFDLRT LRAVRVLRPL KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAILMFAII
     GLEFYMGKFH KACFPNSTDT EPVGDFPCGK DPPARQCDGD TECREYWPGP NFGITNFDNI
     LFAILTVFQC ITMEGWTDIL YNTNDAAGNT WNWLYFIPLI IIGSFFMLNL VLGVLSGEFA
     KERERVENRR AFLKLRRQQQ IERELNGYLE WIFKAEEVML AEEDKNAEEK SPLDVLKRAA
     TKKSRNDLIH AEEGEDRFVD LCAVGSPFAR ASLKSGKTES SSYFRRKEKM FRFFIRRMVK
     AQSFYWVVLC VVALNTLCVA MVHYNQPQRL TTALYFAEFV FLGLFLTEMS LKMYGLGPRS
     YFRSSFNCFD FGVIVGSIFE VVWAAIKPGT SFGISVLRAL RLLRIFKVTK YWNSLRNLVV
     SLLNSMKSII SLLFLLFLFI VVFALLGMQL FGGQFNFQDE TPTTNFDTFP AAILTVFQIL
     TGEDWNAVMY HGIESQGGVS KGMFSSFYFI VLTLFGNYTL LNVFLAIAVD NLANAQELTK
     DEEEMEEAAN QKLALQKAKE VAEVSPMSAA NISIAAQQNS AKARSVWEQR ASQLRLQNLR
     ASCEALYSEM DPEERLRYAS TRHVRPDMKT HMDRPLVVEP GRDGLRGPVG SKSKPEGTEA
     TESADLPRRH HRHRDRDKTS ATAPAGGEQD RTESTETGAR EERARPRRSH SKETPGADTQ
     VRCERSRRHH RRGSPEEATE REPRRHRAHR HAQDSSKEGT APVLVPKGER RARHRGPRTG
     PREAENNEEP TRRHRARHKV PPTLQPPERE AAEKESNAVE GDKETRNHQP KEPHCDLEAI
     AVTGVGPLHM LPSTCLQKVD EQPEDADNQR NVTRMGSQPS DPSTTVHVPV TLTGPPGETP
     VVPSGNMNLE GQAEGKKEAE ADDVLRRGPR PIVPYSSMFC LSPTNLLRRF CHYIVTMRYF
     EMVILVVIAL SSIALAAEDP VRTDSFRNNA LKYMDYIFTG VFTFEMVIKM IDLGLLLHPG
     AYFRDLWNIL DFIVVSGALV AFAFSGSKGK DINTIKSLRV LRVLRPLKTI KRLPKLKAVF
     DCVVNSLKNV LNILIVYMLF MFIFAVIAVQ LFKGKFFYCT DESKELERDC RGQYLDYEKE
     EVEAQPRQWK KYDFHYDNVL WALLTLFTVS TGEGWPMVLK HSVDATYEEQ GPSPGFRMEL
     SIFYVVYFVV FPFFFVNIFV ALIIITFQEQ GDKVMSECSL EKNERACIDF AISAKPLTRY
     MPQNKQSFQY KTWTFVVSPP FEYFIMAMIA LNTVVLMMKF YDAPYEYELM LKCLNIVFTS
     MFSMECILKI IAFGVLNYFR DAWNVFDFVT VLGSITDILV TEIAETNNFI NLSFLRLFRA
     ARLIKLLRQG YTIRILLWTF VQSFKALPYV CLLIAMLFFI YAIIGMQVFG NIALDDDTSI
     NRHNNFRTFL QALMLLFRSA TGEAWHEIML SCLGNRACDP HANASECGSD FAYFYFVSFI
     FLCSFLMLNL FVAVIMDNFE YLTRDSSILG PHHLDEFIRV WAEYDPAACG RISYNDMFEM
     LKHMSPPLGL GKKCPARVAY KRLVRMNMPI SNEDMTVHFT STLMALIRTA LEIKLAPADE
     MTVGKVYAAL MIFDFYKQNK TTRDQTHQAP GGLSQMGPVS LFHPLKATLE QTQPAVLRGA
     RVFLRQKSAT SLSNGGAIQT QESGIKESLS WGTQRTQDAL YEARAPLERG HSAEIPVGQS
     GTLAVDVQMQ NMTLRGPDGE PQPGLESQGR AASMPRLAAE TQPAPNASPM KRSISTLAPR
     PHGTQLCSTV LDRPPPSQAS HHHHHRCHRR RDKKQRSLEK GPSLSVDPEG APSTAAGPGL
     PHGEGSTACR RDRKQERGRS QERRQPSSSS SEKQRFYSCD RFGSREPPQL MPSLSSHPTS
     PTAALEPAPH PQGSGSVNGS PLMSTSGAST PGRGGRRQLP QTPLTPRPSI TYKTANSSPV
     HFAEGQSGLP AFSPGRLSRG LSEHNALLQK EPLSQPLAPG SRIGSDPYLG QRLDSEASAH
     TLPEDTLTFE EAVATNSGRS SRTSYVSSLT SQSHPLRRVP NGYHCTLGLS TGVRARHSYH
     HPDQDHWC
//
ID   VIR_MOUSE               Reviewed;        1811 AA.
AC   A2AIV2; A2AIV1; Q3TDQ3; Q3TRR9; Q3U1Z2; Q80TD6; Q8C758; Q8K151;
AC   Q9CSI3;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 26.
DE   RecName: Full=Protein virilizer homolog;
GN   Name=Kiaa1429;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-1210 AND 1737-1811 (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Lung, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-1811 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1421-1811 (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May be involved in mRNA splicing regulation (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A2AIV2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2AIV2-2; Sequence=VSP_029022, VSP_029023;
CC   -!- SIMILARITY: Belongs to the vir family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH28830.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK012768; BAB28456.1; -; mRNA.
DR   EMBL; AK052499; BAC35017.2; -; mRNA.
DR   EMBL; AK155623; BAE33351.1; -; mRNA.
DR   EMBL; AK162531; BAE36958.1; -; mRNA.
DR   EMBL; AK170075; BAE41548.1; -; mRNA.
DR   EMBL; AL732538; CAM18405.1; -; Genomic_DNA.
DR   EMBL; AL772170; CAM18405.1; JOINED; Genomic_DNA.
DR   EMBL; AL732538; CAM18406.1; -; Genomic_DNA.
DR   EMBL; AL772170; CAM18406.1; JOINED; Genomic_DNA.
DR   EMBL; AL772170; CAM20819.1; -; Genomic_DNA.
DR   EMBL; AL732538; CAM20819.1; JOINED; Genomic_DNA.
DR   EMBL; AL772170; CAM20820.1; -; Genomic_DNA.
DR   EMBL; AL732538; CAM20820.1; JOINED; Genomic_DNA.
DR   EMBL; AK122509; BAC65791.1; -; mRNA.
DR   EMBL; BC028830; AAH28830.1; ALT_INIT; mRNA.
DR   IPI; IPI00348445; -.
DR   IPI; IPI00869461; -.
DR   UniGene; Mm.331487; -.
DR   ProteinModelPortal; A2AIV2; -.
DR   PhosphoSite; A2AIV2; -.
DR   PRIDE; A2AIV2; -.
DR   Ensembl; ENSMUST00000059914; ENSMUSP00000058078; ENSMUSG00000040720.
DR   MGI; MGI:1913435; 1110037F02Rik.
DR   GeneTree; ENSGT00390000002833; -.
DR   HOVERGEN; HBG094918; -.
DR   OrthoDB; EOG4D52WT; -.
DR   Bgee; A2AIV2; -.
DR   CleanEx; MM_1110037F02RIK; -.
DR   Genevestigator; A2AIV2; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; mRNA processing; mRNA splicing;
KW   Nucleus; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1811       Protein virilizer homolog.
FT                                /FTId=PRO_0000308606.
FT   COMPBIAS    139    202       Pro-rich.
FT   COMPBIAS    208    314       Glu-rich.
FT   COMPBIAS    942    945       Poly-Pro.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     138    138       Phosphoserine (By similarity).
FT   MOD_RES     173    173       Phosphoserine.
FT   MOD_RES     184    184       Phosphothreonine (By similarity).
FT   MOD_RES     222    222       Phosphoserine (By similarity).
FT   MOD_RES    1578   1578       Phosphoserine (By similarity).
FT   MOD_RES    1707   1707       Phosphothreonine (By similarity).
FT   VAR_SEQ    1131   1139       IEPHDISVA -> PLHITCILS (in isoform 2).
FT                                /FTId=VSP_029022.
FT   VAR_SEQ    1140   1811       Missing (in isoform 2).
FT                                /FTId=VSP_029023.
FT   CONFLICT     97     97       S -> Y (in Ref. 1; BAE41548).
FT   CONFLICT    373    373       K -> E (in Ref. 1; BAC35017).
FT   CONFLICT   1520   1520       A -> T (in Ref. 4; AAH28830).
FT   CONFLICT   1582   1582       S -> T (in Ref. 4; AAH28830).
SQ   SEQUENCE   1811 AA;  201439 MW;  5F505FADEC3211E3 CRC64;
     MAVDSSMELL FLDTFKHPSA EQSSHIDVVR FPCVVYINEV RVIPPGVRAH SGLPDNRAYG
     ETSPHTFQLD LFFNNVSKPS APVFDRLGSL EYDENTSIIF RPNSKVNTDG LVLRGWYNCL
     TLAIYGSVDR VISHDRDSPP PPPPPPPPPQ PQPTLKRNLK HADGEKEDQF NGSPPRPQPR
     GPRTPPGPPP PDDDEDDPMS LPVSGDKEED VPHREDYFEP ISPDRNSVPQ EGQYSDEGEV
     EEEPQEEGED DEDDVDVEEE EDEDEDDCHT VDSIPDDEEE DEEEEGEEDE EGEGDDGYEQ
     ISSDEDGIAD LERETFKYPN FDVEYTPEDL ASVPPMTYDP YDRELAPLLY FSCPYKTTFE
     IEISRMKDQG PDKENSGAVE ASVKLTELLD LYQEDRGAKW VTALEEIPSL IIKGLSYLQL
     KNTEQDSLGQ LVDWTMQALN LQVAFRQPIA LNVRQLKAGT KLVTSLAECG APGVTELLQA
     GVINVLFDLL FADHVSSSLK LNAFKALDSV ISMTEGMEAF LRSTQNEKSG YQRLLELILL
     DQTVRVVTAG SAILQKCHFY EILSEIKRLG DHIAEKTSAV PNHSEPDQDT DAVLERANPD
     YENEVEASMD MDLLESSIIS EGEIEKLTNL LEEVFHVMET APHTMTQPPV KSFPTIARIT
     GPPERDDPYP VLFRYLHSHH FLELVTLLLS IPITSAHQGV LQATKDVLKF LAQSQKGLLF
     FMSEYEATNL LIRALCHLYD QDEEEGLQSD GADDAFALWL QDSTQTLQCI TELFSHFQRC
     TASEETDHSD LLGTLHNLYL ITFNPVGRSA VGHVFSLDKN LQSLITLMEY YSKEALGDSK
     SKKSVAYNYA CVLTLVVAQS SSGVQMLEQH AASLLKLCKA DENNAKLQEL GKWLEPLKNL
     RFEINCIPNL IEYVKQNIDN LMTAEGVGLT TALRVLCNVA CPPPPVEGQQ KDLKWNLAVI
     QLFSAEGMDT FIRVLQKLNS ILTQPWRLHV NMGTTLHRVT TISMARCTLT LLKTMLTELL
     RGGSFEFKDM RVPSALVTLH MLLCSIPLSG RLDSDEQKIQ NDIIDILLTF TQGVNEKLTI
     SEETLANNTW SLMLKEVLSS ILKVPEGFFS GLILLSELLP LPLPMQTTQV IEPHDISVAL
     NTRKLWSMHL HVQAKLLQEI VRSFSGTTCQ PIQHMLRRIC VQLCDLASPT ALLIMRTVLD
     LIVEDLQSTS EDKEKQYTSQ TTRLLALLDA LASHKACKLA ILHLINGTIK GDERYAEIFQ
     DLLALVRSPG DSVTRQQCVE YVTSILQSLC DQDIALILPS PSEGPASELE QLSNSLPSKE
     LMTAICDCLL ATLANSESSY NCLLTCVRTM MFLAEHDYGL FHLKSSLRKN SSALHSLLKR
     VVSTFSKDTG ELASASLDFM RQILNADAMG CCGDDSGLME VEGAHPPRTM SLNAAELKQL
     LQSKEESPES LFLELEKLVL EHSKDDDSLE SLLDNVIGLK QMLESSGEPL PLSDQDVEPV
     LSAPESLQNL FNNRTAYVLA DVMDDQLKSM WFTPFQAEEI DTDLDLVKVD LIELSEKCCS
     DFDLHSELER SFLSEPSSPG RSKTTKGFKL GKHKHETFIT SSGKSEYIEP AKRAHVVPPP
     RGRGRGGFGQ GIRPHDIFRQ RKQNTSRPPS MHVDDFVAAE SKEVVPQDGI PPPKRPLKVS
     QKISSRGGFS GNRGGRGAFH SQNRFFTPPA SKGNYSRREG TRGSSWSAQN TPRGNYNESR
     GGQSNFNRGP LPPLRPLSST GYRPSPRDRA SRGRGGLGPS WASTNSGSGG SRGKFVSGGS
     GRGRHVRSFT R
//
ID   A2AIX1_MOUSE            Unreviewed;      2377 AA.
AC   A2AIX1;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 24.
DE   SubName: Full=SEC16 homolog A (S. cerevisiae);
GN   Name=Sec16a; ORFNames=RP23-306D20.10-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Peck A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
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DR   EMBL; AL732541; CAM20305.1; -; Genomic_DNA.
DR   IPI; IPI00755905; -.
DR   UniGene; Mm.206371; -.
DR   PhosphoSite; A2AIX1; -.
DR   PRIDE; A2AIX1; -.
DR   Ensembl; ENSMUST00000114082; ENSMUSP00000109716; ENSMUSG00000026924.
DR   MGI; MGI:2139207; Sec16a.
DR   HOGENOM; HBG715574; -.
DR   HOVERGEN; HBG079941; -.
DR   InParanoid; A2AIX1; -.
DR   OMA; IYSCRLA; -.
DR   OrthoDB; EOG4XD3Q5; -.
DR   Bgee; A2AIX1; -.
DR   Genevestigator; A2AIX1; -.
PE   1: Evidence at protein level;
SQ   SEQUENCE   2377 AA;  256473 MW;  3D97AFDDF97218BC CRC64;
     MQPPPQAVPS GVAGPPPAGN PRSMFWANSP YRKPANNAPV APITRPLQPV TDPFAFNRQT
     LQNTPVGSSS KSSLPNLPGP ALSVFSQWPG LPVTPTNAGD SSTGLHEPLS GTLSQPRADA
     SLFPPASTPS SLPGLEVSRN AEADPSSGHE VQMLPHSAHY IPGVGPEQPL GGQMNDSGSG
     PDQPMNRHAP HDGAVTHAAS PFLPQPQMPG QWGPAQGGPQ PSYQHHSPYL EGPVQNMGLQ
     AASLPHFPPP SSLHQGPGHE SHAPQTFTPA SLASGEGNEI VHQQSKNHPL SSFPPKHTFE
     QNSRIGNMWA SPELKQNPGV NKEHLLDPAH VNPFTQGNSP ENQAHHPPVA ATNHALQEAA
     SGALSMFFQG EETENEENLS SEKAGLDKRL NLDSFSSTSR LGHPPPPGAS GVYQAFPRGP
     SSEAAQEGDA QPYFSQSVGV RLDKQSTVPP ANDAWGDVPG TGTRCASGPQ CENVENLEFV
     QNQEVLPRET LSVDPFPLSD QIRYGPLPGP AASRPATVGL TRGGGLNLEA PDTPLHPTRP
     DSVSSSYSSH SHRSPPGSAR PQELVGTFIQ QEVGKLEDDT SGSFFKQIDS SPVGGETDEV
     TGSQNCCSSL SQPSTPSPPK PTGVFQTSAN SSFEPVKSHL VGVKPVEADR ANMVVEVRGT
     QYCPKKRRAA VAPPDATSGN LEQPPDNMET PCAPQACPLP LSTTGEAGQL VSNTAGTPLD
     TVRPVPDKRP SARAQGPVKC ESPATTLWAQ NELPDFGGNV LLAPAAPALY VPVKPKPSEV
     VHHPEKGMSG QKAWKQGSVP PLQNQDPPGA SENLENPPKV GEEEALPVQA SSGYASLLSS
     PPTESLHNQP VLIAQPDQSY NLAQPINFSV SLLNPNEKNQ SWGDAVVGER SIVSNNWALG
     GDPEERAALS GVPASAVTGA SLPSSIPQNC APQGSGSSEM IASQSASWLV QQLSPQTPQS
     PHPNAEKGPS EFVSSPAGNT SVMLVPPASS TLVPNSNKAK HSSNQEEAVG ALDFTLNRTL
     ENPVRMYSPS PSDGPASQQP LPNHPRQSGP GLHNQDHFYQ QVTKDAQDQH RLERAQPELV
     PPRPQNSPQV PQASCPEPSN PESPPTQGQS ESLAQPPASP ASVNTGQLLP QPPQASSASV
     TSTNSSQAAV RSEQLWLHPP PPNTFGPAPQ DLASYYYYRP LYDAYQSQYP SPYPSDPGTA
     SLYYQDMYGL YEPRYRPYDS SASAYAENHR YSEPERPSSR ASHYSDQLAP RQGYPEGYYN
     SKSGWSSHSD YYANYYSGQY DYGDPSRWDR YYGSRLRDPR TWDRRYWYDS EHDPYRKDHY
     AYSDRPEKCD DHWRYDPRFT GSFDDDAEIH RDPYGEEADR RSIHSEHSAR SLRSTHSLPS
     RRSSLSSHSH QSQIYRSHHV TGGSFEAPHA PGSFHGDYAY GTYASNFSGA HGFPEYSYPA
     DTSWPAVEQV PSRPTSPEKF TVPHVCARFG PGGQLLKVIP NLPSEGQPAL VEIHSLETLL
     QHTPEQEEMR SFPGPLGKDD THKVDVINFA QNKATKCLQN ESLIDKESAS LLWKFIILLC
     RQNGTVVGTD IAELLLRDHR TVWLPGKSPN EANLIDFTNE AVEQVEEEES GEAQLSFLTD
     SQTVTTSVLE KETERFRELL LYGRKKDALE SAMKNGLWGH ALLLASKMDS RTHARVMTRF
     ANSLPINDPL QTVYQLMSGR MPAASTCCGD EKWGDWRPHL AMVLSNLNNN MDVESRTMAT
     MGDTLASKGL LDAAHFCYLM AQVGFGVYTK KTTKLVLIGS NHSLPFLKFA TNEAIQRTEA
     YEYAQSLGAH TCSLPNFQVF KFIYLCRLAE MGLATQAFHY CEVIAKSVLT QPGAYSPVLI
     SQLTQMASQL RLFDPQLKEK PEEESFVEPA WLVQLQHVER QIQEGTVLWS QDGTEPQQCR
     ITSGSEVEQS DGPGLNQQAG PQADNPLLMP STEPLMHGVQ LLPTAPQTLP DGQPAHLSRV
     PMFPVPMSRG PLELSPAYGP PGSALGFPES SRSDPAVLHP GQALPPTTLS LQESGLPPQE
     AKSPDPEMVP RGSPVRHSPP ELSQEEFGES FADPGSSRTA QDLETSPVWD LGSSSLTRAP
     SLTSDSEGKK PAQAVKKEPK EPKKTESWFS RWLPGKKRTE AYLPDDKNKS IVWDEKKNQW
     VNLNEPEEEK KAPPPPPTSF PRVPQVAPTG PAGPPTASVN VFSRKAGGSR ARYVDVLNPS
     GTQRSEPALA PADFFAPLAP LPIPSNLFVP NPDAEEPQPA DGTGCRGQAP AGTQSKAEST
     LEPKVGSSTV SAPGPELLPS KPDGSQGGEL SRCSSLSSLS QEVSRHFHQA PGDHCPTGAP
     HGGSVPFYNP AQLVQASVTS GNSRPGRIGQ RKYAALN
//
ID   A2AIY8_MOUSE            Unreviewed;       826 AA.
AC   A2AIY8;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 24.
DE   SubName: Full=SH3-domain GRB2-like (Endophilin) interacting protein 1;
GN   Name=Sgip1; ORFNames=RP23-66O4.1-007;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Lovell J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Oliver K.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL732543; CAM14981.1; -; Genomic_DNA.
DR   EMBL; AL772290; CAM14981.1; JOINED; Genomic_DNA.
DR   EMBL; AL772290; CAM26591.1; -; Genomic_DNA.
DR   EMBL; AL732543; CAM26591.1; JOINED; Genomic_DNA.
DR   IPI; IPI00623241; -.
DR   UniGene; Mm.238094; -.
DR   UniGene; Mm.461880; -.
DR   STRING; A2AIY8; -.
DR   Ensembl; ENSMUST00000106882; ENSMUSP00000102495; ENSMUSG00000028524.
DR   MGI; MGI:1920344; Sgip1.
DR   HOVERGEN; HBG081524; -.
DR   Bgee; A2AIY8; -.
DR   Genevestigator; A2AIY8; -.
DR   GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR008968; Clathrin_mu_C.
DR   InterPro; IPR018808; SAFF_domain.
DR   Pfam; PF00928; Adap_comp_sub; 1.
DR   Pfam; PF10291; SAFF; 1.
PE   4: Predicted;
SQ   SEQUENCE   826 AA;  88551 MW;  706459A1A5A74CB5 CRC64;
     MMEGLKKRTR KAFGIRKKEK DTDSTGSPDR DGMQPSPHEP PYHSKAECAR EGGKKASKKS
     NGAPNGFYAE IDWERYNSPE LDEEGYSIRP EEPGSTKGKH FYSSSESEEE EESHKKFNIK
     IKPLQSKDVL KNAATVDELK ASIGNIALSP SPVRKSPRRS PGAIKRNLSS EEVARPRRST
     PTPELTSKKP LDDTLALAPL FGPPLESAFD EQKTEVLLDQ PEIWGSGQPM NPSTESPELA
     RPFPTGTPPP LPPKTVPATP PRTGSPLTVA TGNDQAATEA KIEKLPSISD LDSIFGPVLS
     PKSVAVNTEE KWVHFSDASP EHVTPELTPR EQVVTPPAAS DIPADSPAPA PPGPTGSAGP
     PGPPGPRHVP SPLNLEEVQK KVAEQTFIKD DYLETLSSPK ECGLGQRATP PPPPPPTYRT
     VVSSPGPGSG SGTGTTSGAS SPARPATPLV PCSTTPPPPP PRPPSRPKLP PGKPGVGDVS
     RPFSPPIHSS SPPPIAPLAR AESTSSISST NSLSAATTPT VENEQPSLVW FDRGKFYLTF
     EGSSRGPSPL TMGAQDTLPV AAAFTETVNA YFKGADPSKC IVKITGEMVL SFPAGITRHF
     ANNPSPAALT FRVVNSSRLE HVLPNPQLLC CDNTQNDANT KEFWVNMPNL MTHLKKVSEQ
     KPQATYYNVD MLKYQVSAQG IQSTPLNLAV NWRCEPASTD LRIDYKYNTD AMSTAVALNN
     VQFLVPIDGG VTKLQAVLPP AVWNAEQQRI LWKIPDISQK SENGGVGSLL ARFQLSEGPS
     KPSPLVVQFT SEGSTLSGCD IELVGAGYRF SLIKKRFAAG KYLADN
//
ID   A2AIY9_MOUSE            Unreviewed;       659 AA.
AC   A2AIY9;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 24.
DE   SubName: Full=SH3-domain GRB2-like (Endophilin) interacting protein 1;
GN   Name=Sgip1; ORFNames=RP23-66O4.1-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Lovell J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Oliver K.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL732543; CAM14982.1; -; Genomic_DNA.
DR   EMBL; AL772290; CAM14982.1; JOINED; Genomic_DNA.
DR   EMBL; AL772290; CAM26592.1; -; Genomic_DNA.
DR   EMBL; AL732543; CAM26592.1; JOINED; Genomic_DNA.
DR   IPI; IPI00311247; -.
DR   UniGene; Mm.238094; -.
DR   UniGene; Mm.461880; -.
DR   STRING; A2AIY9; -.
DR   PRIDE; A2AIY9; -.
DR   Ensembl; ENSMUST00000066824; ENSMUSP00000063712; ENSMUSG00000028524.
DR   MGI; MGI:1920344; Sgip1.
DR   HOVERGEN; HBG081524; -.
DR   Bgee; A2AIY9; -.
DR   Genevestigator; A2AIY9; -.
DR   GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR008968; Clathrin_mu_C.
DR   InterPro; IPR018808; SAFF_domain.
DR   Pfam; PF00928; Adap_comp_sub; 1.
DR   Pfam; PF10291; SAFF; 1.
PE   4: Predicted;
SQ   SEQUENCE   659 AA;  71361 MW;  4A2F2788CF03E9F7 CRC64;
     MMEGLKKRTR KAFGIRKKEK DTDSTGSPDR DGMPSPHEPP YHSKAECARE GGKKASKKSN
     GAPNGFYAEI DWERYNSPEL DEEGYSIRPE EPGSTKGKHF YSSSESEEEE ESHKKFNIKI
     KPLQSKDVLK NAATVDELKA SIGNIALSPS PVRKSPRRSP GAIKRNLSSE EVARPRRSTP
     TPELTSKKPL DDTLALAPLF GPPLESAFDE QKTEVLLDQP EIWGSGQPMN PSTESPELAR
     PFPTGTPPPL PPKTVPATPP RTGSPLTVAT GASSPARPAT PLVPCSTTPP PPPPRPPSRP
     KLPPGKPGVG DVSRPFSPPI HSSSPPPIAP LARAESTSSI SSTNSLSAAT TPTVENEQPS
     LVWFDRGKFY LTFEGSSRGP SPLTMGAQDT LPVAAAFTET VNAYFKGADP SKCIVKITGE
     MVLSFPAGIT RHFANNPSPA ALTFRVVNSS RLEHVLPNPQ LLCCDNTQND ANTKEFWVNM
     PNLMTHLKKV SEQKPQATYY NVDMLKYQVS AQGIQSTPLN LAVNWRCEPA STDLRIDYKY
     NTDAMSTAVA LNNVQFLVPI DGGVTKLQAV LPPAVWNAEQ QRILWKIPDI SQKSENGGVG
     SLLARFQLSE GPSKPSPLVV QFTSEGSTLS GCDIELVGAG YRFSLIKKRF AAGKYLADN
//
ID   MA1B1_MOUSE             Reviewed;         658 AA.
AC   A2AJ15;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   RecName: Full=Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase;
DE            EC=3.2.1.113;
DE   AltName: Full=ER alpha-1,2-mannosidase;
DE   AltName: Full=ER mannosidase 1;
DE            Short=ERMan1;
DE   AltName: Full=Man9GlcNAc2-specific-processing alpha-mannosidase;
DE   AltName: Full=Mannosidase alpha class 1B member 1;
GN   Name=Man1b1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Involved in glycoprotein quality control targeting of
CC       misfolded glycoproteins for degradation. It primarily trims a
CC       single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to
CC       produce Man(8)GlcNAc(2), but at high enzyme concentrations, as
CC       found in the ER quality control compartment (ERQC), it further
CC       trims the carbohydrates to Man(5-6)GlcNAc(2) (By similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of the terminal (1->2)-linked
CC       alpha-D-mannose residues in the oligo-mannose oligosaccharide
CC       Man(9)(GlcNAc)(2).
CC   -!- COFACTOR: Calcium (By similarity).
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       type II membrane protein.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 47 family.
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DR   EMBL; AL732557; CAM25606.1; -; Genomic_DNA.
DR   EMBL; CH466542; EDL08233.1; -; Genomic_DNA.
DR   EMBL; BC138550; AAI38551.1; -; mRNA.
DR   EMBL; BC138551; AAI38552.1; -; mRNA.
DR   IPI; IPI00124093; -.
DR   RefSeq; NP_001025154.1; NM_001029983.2.
DR   UniGene; Mm.270798; -.
DR   ProteinModelPortal; A2AJ15; -.
DR   SMR; A2AJ15; 206-655.
DR   STRING; A2AJ15; -.
DR   PhosphoSite; A2AJ15; -.
DR   PRIDE; A2AJ15; -.
DR   Ensembl; ENSMUST00000042390; ENSMUSP00000036996; ENSMUSG00000036646.
DR   GeneID; 227619; -.
DR   KEGG; mmu:227619; -.
DR   CTD; 227619; -.
DR   MGI; MGI:2684954; Man1b1.
DR   eggNOG; maNOG18798; -.
DR   HOGENOM; HBG559734; -.
DR   HOVERGEN; HBG052389; -.
DR   InParanoid; A2AJ15; -.
DR   OMA; KQWIQTG; -.
DR   OrthoDB; EOG4J9MZB; -.
DR   PhylomeDB; A2AJ15; -.
DR   NextBio; 378670; -.
DR   Bgee; A2AJ15; -.
DR   Genevestigator; A2AJ15; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004571; F:mannosyl-oligosaccharide 1,2-alpha-mannosidase activity; IMP:MGI.
DR   GO; GO:0030433; P:ER-associated protein catabolic process; IMP:MGI.
DR   InterPro; IPR001382; Glyco_hydro_47.
DR   Gene3D; G3DSA:1.50.10.50; Glyco_hydro_47; 1.
DR   PANTHER; PTHR11742; Glyco_hydro_47; 1.
DR   Pfam; PF01532; Glyco_hydro_47; 1.
DR   PRINTS; PR00747; GLYHDRLASE47.
DR   SUPFAM; SSF48225; Glyco_hydro_47; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Disulfide bond; Endoplasmic reticulum; Glycosidase;
KW   Hydrolase; Membrane; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    658       Endoplasmic reticulum mannosyl-
FT                                oligosaccharide 1,2-alpha-mannosidase.
FT                                /FTId=PRO_0000396622.
FT   TOPO_DOM      1     50       Cytoplasmic (Potential).
FT   TRANSMEM     51     71       Helical; Signal-anchor for type II
FT                                membrane protein; (Potential).
FT   TOPO_DOM     72    658       Lumenal (Potential).
FT   ACT_SITE    289    289       Proton donor (By similarity).
FT   ACT_SITE    422    422       By similarity.
FT   ACT_SITE    558    558       By similarity.
FT   DISULFID    486    515       By similarity.
SQ   SEQUENCE   658 AA;  75150 MW;  75BA990FA9B1470B CRC64;
     MYPPPAPPPA PHRDFISVTL SLGESYDNSK SRRRRSCWRK WKQLSRLQRN VILFVLGFLI
     LCGFLYSLHT ADQWKALSGR PAEVEKMKQE VLPVLPAPQK ESAEQEGFAD ILSQKRQRHF
     RRGPPHLQIR PPNTVSKDGM QDDAKEREAA LGKAQQEENT QRTVISWRGA VIEPEQATEL
     PYKRAEASIK PLVLASKIWK EPAPPNERQK GVIEAFLHAW KGYQKFAWGH DELKPVSKTF
     SEWFGLGLTL IDALDTMWIL GLKQEFKQAR KWVSENLDFQ KNVDVNLFES TIRILGGLLS
     TYHLSGDSLF LTKAEDFGKR LMPAFTTPSK IPYSDVNIGT GFAHSPQWTS DSTVAEVTSI
     QLEFRELSRL TGIKKFQEAV EEVTKHIHSL SGKKDGLVPM FINTNSGLFT HPGVFTLGAR
     ADSYYEYLLK QWIQGGKKET QLLEDYVKAI EGIKAHLLRQ SQPRKLTFVG ELAHGRFSAK
     MDHLVCFLPG TLALGVHHGL PADHMDLARA LMETCYQMNQ QMETGLSPEI AHFNMYPRAD
     HKDVEVKPAD RHNLLRPETV ESLFYLYRVT RDRKYQDWGW EILQSFNKYT RVPSGGYSSI
     NNVQNSHKPE PRDKMESFFV GETLKYLYLL FSDDLELLSL DSCVFNTEAH PLPIWAPA
//
ID   A2AJ40_MOUSE            Unreviewed;       267 AA.
AC   A2AJ40;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-FEB-2011, entry version 22.
DE   SubName: Full=Novel protein (4930430A15Rik);
DE   Flags: Fragment;
GN   Name=4930430A15Rik; Synonyms=RP23-9A5.2; ORFNames=RP23-9A5.2-002;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Pelan S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL732559; CAM27560.1; -; Genomic_DNA.
DR   IPI; IPI00758026; -.
DR   PRIDE; A2AJ40; -.
DR   Ensembl; ENSMUST00000111010; ENSMUSP00000106639; ENSMUSG00000027157.
DR   Ensembl; ENSMUST00000142636; ENSMUSP00000117759; ENSMUSG00000027157.
DR   MGI; MGI:1914825; 4930430A15Rik.
DR   GeneTree; ENSGT00560000076605; -.
DR   Bgee; A2AJ40; -.
DR   Genevestigator; A2AJ40; -.
PE   4: Predicted;
FT   NON_TER     267    267
SQ   SEQUENCE   267 AA;  30445 MW;  CCC679049A55794F CRC64;
     MTESHHFIKE SDLEIESLVE TFSYDNEDKQ SMSDDGHFSG TTPKWCQNDT NRKTTVQDCM
     YPNLKSPTEG KIPTRSKAGK MAESAHFIIE SDLEIESLEE TVSCDSEDKQ LLYLPQIDDS
     HFSEAANEEP ENNLERQMKE SAKKYPYLKI ANEMNDLSPN TYSESKDEET LTSELTISST
     SEEQKCPYAR GKAQSMQTGP MDIVYLVTVN NQREENMGIS QEKDSPEEKH EHQCSTEKTY
     SIAQEESDTN QEDSSHAEQV FELTSQE
//
ID   A2AJ72_MOUSE            Unreviewed;       569 AA.
AC   A2AJ72;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 27.
DE   SubName: Full=Far upstream element (FUSE) binding protein 3;
DE   SubName: Full=MCG130458;
GN   Name=Fubp3; ORFNames=RP23-442G9.4-001, mCG_130458;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Pearce A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 4 KH domains.
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DR   EMBL; AL732564; CAM24508.1; -; Genomic_DNA.
DR   EMBL; CH466542; EDL08510.1; -; Genomic_DNA.
DR   IPI; IPI00379513; -.
DR   UniGene; Mm.207261; -.
DR   ProteinModelPortal; A2AJ72; -.
DR   SMR; A2AJ72; 73-152, 162-425.
DR   STRING; A2AJ72; -.
DR   Ensembl; ENSMUST00000113482; ENSMUSP00000109110; ENSMUSG00000026843.
DR   MGI; MGI:2443699; Fubp3.
DR   GeneTree; ENSGT00530000063563; -.
DR   HOVERGEN; HBG000625; -.
DR   OrthoDB; EOG4X97H1; -.
DR   Bgee; A2AJ72; -.
DR   Genevestigator; A2AJ72; -.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR004088; KH_type_1.
DR   InterPro; IPR018111; KH_type_1_subgr.
DR   Pfam; PF00013; KH_1; 4.
DR   SMART; SM00322; KH; 4.
DR   PROSITE; PS50084; KH_TYPE_1; 4.
PE   4: Predicted;
SQ   SEQUENCE   569 AA;  61447 MW;  D78EE76A13C8E274 CRC64;
     MAELVQGQSA PVGMKAEGFV DALHRVRQIA AKIDSIPHLN NSTPLVDPSV YGYGVQKRAL
     DDGVGNQLGA LVHQRAVITE EFKVPDKMVG FIIGRGGEQI SRIQAESGCK IQIASESSGI
     PERPCVLTGT PESIEQAKRL LGQIVDRCRN GPGFHNDMDG NSTIQELLIP ASKVGLVIGK
     GGETIKQLQE RTGVKMVMIQ DGPLPTGADK PLRITGDPFK VQQAREMVLE IIREKDQADF
     RGVRSDFTSR AGGGSIEVSV PRFVVGIVIG RNGEMIKKIQ NDAGVRIQFK PDDGISPERA
     AQVMGPPDRC QHAARIINEL ILTAQEREIL GGLTVTRGRG RGRSDWSVGT PGGVQEITYT
     VPADKCGLVI GKGGENIKSI NQQSGAHVEL QRNPPPNTDP NLRIFTIRGA PQQMEVARHL
     IDEKVGGASL GAPAAFGQSP FSQPPAAPHQ NTFPPRGFPN IAAKVNGNPH STPVSGPPAF
     LTQGWGSTYQ AWQQPTQQVP SQQSQPQNSQ PDYSKAWEDY YKKQSHPTSA APQASSPPDY
     TMAWAEYYRQ QAAFYGQTLG QAQAHSQEQ
//
ID   PLPL7_MOUSE             Reviewed;        1352 AA.
AC   A2AJ88; Q3TD21; Q3UFP1; Q66JS2; Q6P3F9; Q8BTY7; Q8R064; Q8R3C5;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 33.
DE   RecName: Full=Patatin-like phospholipase domain-containing protein 7;
DE            EC=3.1.1.-;
GN   Name=Pnpla7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 113-1352 (ISOFORM 1).
RC   STRAIN=129, and FVB/N; TISSUE=Limb, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Serine hydrolase, whose specific chemical modification
CC       by certain organophosphorus (OP) compounds leads to distal
CC       axonopathy (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential). Nucleus membrane; Single-pass membrane protein (By
CC       similarity). Mitochondrion membrane; Single-pass membrane protein
CC       (By similarity). Lysosome membrane; Single-pass membrane protein
CC       (By similarity). Microsome membrane; Single-pass membrane protein
CC       (By similarity). Note=Found in the nuclear, mitochondrial,
CC       lysosomal, and microsomal fractions (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A2AJ88-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2AJ88-2; Sequence=VSP_026506, VSP_026507;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the NTE family.
CC   -!- SIMILARITY: Contains 3 cyclic nucleotide-binding domains.
CC   -!- SIMILARITY: Contains 1 patatin domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH27342.1; Type=Erroneous initiation;
CC       Sequence=BAC40302.1; Type=Erroneous initiation;
CC       Sequence=BAE28519.1; Type=Erroneous initiation;
CC       Sequence=BAE41783.1; Type=Erroneous initiation;
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DR   EMBL; AK088362; BAC40302.1; ALT_INIT; mRNA.
DR   EMBL; AK148380; BAE28519.1; ALT_INIT; mRNA.
DR   EMBL; AK170417; BAE41783.1; ALT_INIT; mRNA.
DR   EMBL; AL732585; CAM17985.1; -; Genomic_DNA.
DR   EMBL; BC025621; AAH25621.1; -; mRNA.
DR   EMBL; BC064003; AAH64003.1; -; mRNA.
DR   EMBL; BC080793; AAH80793.1; -; mRNA.
DR   EMBL; BC027342; AAH27342.1; ALT_INIT; mRNA.
DR   IPI; IPI00331610; -.
DR   IPI; IPI00853933; -.
DR   RefSeq; NP_666363.3; NM_146251.4.
DR   UniGene; Mm.389243; -.
DR   ProteinModelPortal; A2AJ88; -.
DR   SMR; A2AJ88; 156-300, 493-713.
DR   STRING; A2AJ88; -.
DR   PhosphoSite; A2AJ88; -.
DR   PRIDE; A2AJ88; -.
DR   Ensembl; ENSMUST00000045295; ENSMUSP00000044078; ENSMUSG00000036833.
DR   GeneID; 241274; -.
DR   KEGG; mmu:241274; -.
DR   CTD; 241274; -.
DR   MGI; MGI:2385325; Pnpla7.
DR   eggNOG; roNOG13327; -.
DR   HOVERGEN; HBG053067; -.
DR   InParanoid; A2AJ88; -.
DR   OMA; LHLCCPR; -.
DR   OrthoDB; EOG4P5K8B; -.
DR   PhylomeDB; A2AJ88; -.
DR   NextBio; 384953; -.
DR   Bgee; A2AJ88; -.
DR   CleanEx; MM_PNPLA7; -.
DR   Genevestigator; A2AJ88; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005792; C:microsome; IEA:UniProtKB-SubCell.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPlipase.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR002641; Patatin/PhospholipaseA2-rel.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 3.
DR   Pfam; PF00027; cNMP_binding; 3.
DR   Pfam; PF01734; Patatin; 1.
DR   SMART; SM00100; cNMP; 3.
DR   SUPFAM; SSF52151; Acyl_Trfase/lysoPlipase; 1.
DR   SUPFAM; SSF51206; cNMP_binding; 3.
DR   PROSITE; PS00888; CNMP_BINDING_1; FALSE_NEG.
DR   PROSITE; PS00889; CNMP_BINDING_2; FALSE_NEG.
DR   PROSITE; PS50042; CNMP_BINDING_3; 3.
DR   PROSITE; PS01237; UPF0028; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW   Lysosome; Membrane; Microsome; Mitochondrion; Nucleus; Phosphoprotein;
KW   Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN         1   1352       Patatin-like phospholipase domain-
FT                                containing protein 7.
FT                                /FTId=PRO_0000293490.
FT   TRANSMEM     37     57       Helical; (Potential).
FT   DOMAIN      950   1116       Patatin.
FT   NP_BIND     170    297       cNMP 1.
FT   NP_BIND     478    602       cNMP 2.
FT   NP_BIND     598    718       cNMP 3.
FT   MOTIF       981    985       GXSXG.
FT   ACT_SITE    983    983       By similarity.
FT   MOD_RES     379    379       Phosphoserine.
FT   CARBOHYD    102    102       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    401    401       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    750    750       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1036   1036       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1255   1255       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ    1313   1326       EYEPSMLQGPPSLT -> VRNMSLRCCKDPPA (in
FT                                isoform 2).
FT                                /FTId=VSP_026506.
FT   VAR_SEQ    1327   1352       Missing (in isoform 2).
FT                                /FTId=VSP_026507.
FT   CONFLICT    113    116       RTKV -> PRVR (in Ref. 3; AAH25621).
FT   CONFLICT    237    237       S -> R (in Ref. 1; BAE41783).
FT   CONFLICT    361    420       Missing (in Ref. 2).
FT   CONFLICT   1343   1343       D -> N (in Ref. 1; BAE28519).
SQ   SEQUENCE   1352 AA;  150494 MW;  ADF5362282EA1607 CRC64;
     MQNEEDACLE AGYCLGTTLS SWRLHFMEEQ SQSTMLMGIG IGALLTLAFV GITFFFVYRR
     VRRLRRAEPT PQYRFRKRDK VMFYGRKIMR KVTTLPHTLV GNTSAPRQRV RKRTKVLSLA
     KRILRFKKEY PTLQPKEPPP SLLEADLTEF DVKNSHLPSE VLYMLKNVRV LGHFEKPLFL
     ELCKHMVFVQ LQEGEHVFQP GEPDISIYVV QDGRLEVCIQ DADGTEVVVK EVLPGDSVHS
     LLSILDVITG HTAPYKTVSA RAAVSSTVLW LPAAAFQGVF EKYPETLVRV VQIIMVRLQR
     VTFLALHNYL GLTTELFNPE SQAIPLLSVA SVAGRAKRQM SYGPEEQLER SLRPSEFSSS
     DHGSSCVTVS GPLLKRSCSV PLPSNHGEVD ELRQSQGSGS NTSAFQESHE GATSDLGMAY
     NRARILPHSD EQLGNSLASK SKKSVVAETP SAIFHYSENF RDETGACGKT DAIFRAATKD
     LLTLMKLDDP SLLDGRVAFL HVPAGTLVSK QGDQDVNILF VVSGMLHVYQ QKIDSLEDTC
     LFLTHPGEMV GQLAVLTGEP LMFTIRANRD CSFLSISKAH FYEIMRKRPD VVLGVAHTVV
     KRMSSFVRQI DFALDWMEVE AGRAIYRQGD KSDCTYIVLS GRLRSVIRKD DGKKRLAGEY
     GRGDLVGVVE TLTHQARATT VHAVRDSELA KLPAGALTSI KRRYPQVVTR LIHLLGEKIL
     GSLQQGSATG HQLGFNTASS KWDLGNPPGN LSTVAALPAS EDVPLTAFAL ELQHALSAIG
     PVLLLTSDNI KQRLGSAALD SIHEYRLSSW LGQQEDIHRI VLYQADGTLT PWTQRCIRQA
     DCILIVGLGE QEPAVGELEQ MLESTAVRAQ KQLILLHKED GPVPSRTVEW LNMRSWCSGH
     LHLCCPRRVF SKRSLPKLVE MYTRVFQRPP DRHSDFSRLA RMLTGNAIAL VLGGGGARGC
     AQVGILRALA ECGVPVDIIG GTSIGAFMGA LFAEERSYSQ TRIRAKQWAE GMTSMMKTIL
     DLTYPITSMF SGTGFNSSIS NIFKDRQIED LWLPYFAITT DITASAMRVH TDGSLWRYVR
     ASMSLSGYMP PLCDPKDGHL LMDGGYINNL PADVARSMGA KVVIAIDVGS RDETDLTNYG
     DALSGWWLLW KRWNPLATKV KVLNMAEIQT RLAYVCCVRQ LEMVKNSDYC EYLRPPIDSY
     RTLDFGKFDE ICEVGYQHGR TVFDIWVRSG VLEKMLQDQQ GTSKRKDCGV FTCPNSSFTD
     LAEIVSRIEP AKVAAVDDES DYQTEYEEEL PAIPKETYAD FQSTGIELDS DSEYEPSMLQ
     GPPSLTSPEQ SQDSFPWLPN QDDQGPRLEH PS
//
ID   CI172_MOUSE             Reviewed;         974 AA.
AC   A2AJA9; Q6P0A3;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 31.
DE   RecName: Full=Uncharacterized protein C9orf172 homolog;
GN   Name=Gm996;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129 AND THR-498, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-105; SER-109; SER-448;
RP   THR-511 AND SER-593, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A2AJA9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2AJA9-2; Sequence=VSP_038820;
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DR   EMBL; AL732590; CAM25172.1; -; Genomic_DNA.
DR   EMBL; BC065698; AAH65698.1; -; mRNA.
DR   IPI; IPI00420221; -.
DR   IPI; IPI00955709; -.
DR   RefSeq; NP_001005424.2; NM_001005424.2.
DR   UniGene; Mm.379511; -.
DR   ProteinModelPortal; A2AJA9; -.
DR   SMR; A2AJA9; 654-713.
DR   PhosphoSite; A2AJA9; -.
DR   PRIDE; A2AJA9; -.
DR   Ensembl; ENSMUST00000114217; ENSMUSP00000109855; ENSMUSG00000029419.
DR   GeneID; 381353; -.
DR   KEGG; mmu:381353; -.
DR   MGI; MGI:2685842; Gm996.
DR   eggNOG; maNOG17646; -.
DR   GeneTree; ENSGT00390000016543; -.
DR   HOGENOM; HBG446961; -.
DR   HOVERGEN; HBG062328; -.
DR   InParanoid; A2AJA9; -.
DR   OMA; RSWDNIL; -.
DR   OrthoDB; EOG40S0DZ; -.
DR   NextBio; 401949; -.
DR   Bgee; A2AJA9; -.
DR   Genevestigator; A2AJA9; -.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    974       Uncharacterized protein C9orf172 homolog.
FT                                /FTId=PRO_0000392545.
FT   COMPBIAS     68    422       Pro-rich.
FT   MOD_RES     105    105       Phosphothreonine.
FT   MOD_RES     109    109       Phosphoserine.
FT   MOD_RES     129    129       Phosphoserine.
FT   MOD_RES     448    448       Phosphoserine.
FT   MOD_RES     498    498       Phosphothreonine.
FT   MOD_RES     511    511       Phosphothreonine.
FT   MOD_RES     593    593       Phosphoserine.
FT   VAR_SEQ     202    234       Missing (in isoform 2).
FT                                /FTId=VSP_038820.
SQ   SEQUENCE   974 AA;  107186 MW;  9C1D6C006770E3CC CRC64;
     MTRTDPPDLL VSTVYQDIKV VDPGLTSKRQ PCERSVARPA APTPFNKRHC RSFDFLEALD
     EPTMETHPEP PPPEPAPPRA RPRDSEPRRR TRSKSAPRAS QGLATAPASP PVLQRRGREA
     QRAVRVEGSP RREPSYPALR ALANELHPIK LQPQRGGPGR IAPLCATPGR CAPPEPPSGP
     VPHVRCRLDI KPDEAVLQHA ARSSRSCAPR ETTSWARTAP QFHGLTVPGP RHVALSRTPT
     PSDLYCTDPR TLYCDGPLPG PRDYLEHRSQ PFTTPPGPTQ FFYTEEPEGY AGSFTTSPGL
     PFDGYCSRPY LSEEPPRPSP RRGGSYYAGE VRTFPIQEPP SRSYYGETTR AYGMPFVPRY
     VPEEPRAHPG ARTFYTEDFG RYRERDVLAR TYPHPRSSPP WADWGPRPYR TLQVMPPPAP
     GPLLASWHGG TGTSPPRLAT DSRHYSRSWD NILAPGPRRE DPLGRGRSYE NLLGREVRDT
     RGSSPEGRRP PVVVNLSTSP RRYAALSLSE TSLTEKGRAG ESLGRNWYVT PEITITDNDL
     RSVDRPTAKG WELPGGRPRQ PVSTVPEGPA SSRQRSLEQL DELITDLVID SRSPAQAPEP
     AAEGLGRQLR RLLDSRAAGP GGATLLAPSR SPPASAGSTE EPTGSGEAAD ASPEPSADED
     DLMTCSNARC RRTETMFNAC LYFKSCHSCY TYYCSRLCRR EDWDAHKARC VYGRVGSVCR
     HVLQFCRDSS PVHRAFSRIA RVGFLSRGRG VLFLGFPSPG SADNFLRFGL EGLLLSPTYL
     SLRELATHAA PLGSYARELA AAGRLYEPAE CFLLSVSVAV GPSAAPPGAA ARPAPRTPGP
     TVRKFAKVAL AAGSPTRPPP ARGGEPDMET LILTPPPGTA GLDEEGEAGR RAREVAFIHI
     QRELRMRGVF LRHEFPRVYE QLCEFVEANR RFTPTTIYPT DRRTGRPFMC MIMAASEPRA
     LDWVASANLL DDIM
//
ID   MA7D1_MOUSE             Reviewed;         846 AA.
AC   A2AJI0; Q80TI3; Q8CIL3; Q8VCG2; Q91YQ4;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-FEB-2011, entry version 35.
DE   RecName: Full=MAP7 domain-containing protein 1;
GN   Name=Map7d1; Synonyms=Kiaa1187, Mtap7d1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 220-846 (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 291-846 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276; SER-544; SER-548
RP   AND SER-552, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401; SER-544 AND
RP   SER-548, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A2AJI0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2AJI0-2; Sequence=VSP_028489;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the MAP7 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH16081.1; Type=Erroneous initiation;
CC       Sequence=AAH19977.1; Type=Erroneous initiation;
CC       Sequence=BAC65744.3; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it is derived from pre-RNA;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL732624; CAM13850.1; -; Genomic_DNA.
DR   EMBL; BC016081; AAH16081.1; ALT_INIT; mRNA.
DR   EMBL; BC019977; AAH19977.1; ALT_INIT; mRNA.
DR   EMBL; BC023677; AAH23677.1; -; mRNA.
DR   EMBL; AK122462; BAC65744.3; ALT_SEQ; Transcribed_RNA.
DR   IPI; IPI00282957; -.
DR   IPI; IPI00867855; -.
DR   RefSeq; NP_659190.3; NM_144941.3.
DR   UniGene; Mm.266716; -.
DR   ProteinModelPortal; A2AJI0; -.
DR   PhosphoSite; A2AJI0; -.
DR   PRIDE; A2AJI0; -.
DR   Ensembl; ENSMUST00000061143; ENSMUSP00000054338; ENSMUSG00000028849.
DR   GeneID; 245877; -.
DR   KEGG; mmu:245877; -.
DR   CTD; 245877; -.
DR   MGI; MGI:2384297; Mtap7d1.
DR   GeneTree; ENSGT00530000063115; -.
DR   HOGENOM; HBG279032; -.
DR   HOVERGEN; HBG071099; -.
DR   InParanoid; A2AJI0; -.
DR   OMA; AMKNATS; -.
DR   PhylomeDB; A2AJI0; -.
DR   NextBio; 386980; -.
DR   Bgee; A2AJI0; -.
DR   Genevestigator; A2AJI0; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   InterPro; IPR008604; E-MAP-115.
DR   PANTHER; PTHR15073; E-MAP-115; 1.
DR   Pfam; PF05672; MAP7; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Isopeptide bond; Phosphoprotein; Ubl conjugation.
FT   CHAIN         1    846       MAP7 domain-containing protein 1.
FT                                /FTId=PRO_0000306808.
FT   COILED      130    224       Potential.
FT   COILED      414    443       Potential.
FT   COILED      599    740       Potential.
FT   COMPBIAS      5    129       Pro-rich.
FT   COMPBIAS    467    595       Pro-rich.
FT   MOD_RES      43     43       Phosphoserine (By similarity).
FT   MOD_RES      49     49       Phosphothreonine (By similarity).
FT   MOD_RES      53     53       Phosphothreonine (By similarity).
FT   MOD_RES      90     90       Phosphoserine (By similarity).
FT   MOD_RES      99     99       Phosphothreonine (By similarity).
FT   MOD_RES     115    115       Phosphoserine (By similarity).
FT   MOD_RES     118    118       Phosphoserine (By similarity).
FT   MOD_RES     120    120       Phosphothreonine (By similarity).
FT   MOD_RES     125    125       Phosphoserine (By similarity).
FT   MOD_RES     127    127       Phosphoserine (By similarity).
FT   MOD_RES     254    254       Phosphoserine (By similarity).
FT   MOD_RES     276    276       Phosphoserine.
FT   MOD_RES     304    304       Phosphothreonine (By similarity).
FT   MOD_RES     315    315       Phosphoserine (By similarity).
FT   MOD_RES     401    401       Phosphoserine.
FT   MOD_RES     444    444       Phosphoserine (By similarity).
FT   MOD_RES     448    448       Phosphoserine (By similarity).
FT   MOD_RES     460    460       Phosphoserine (By similarity).
FT   MOD_RES     544    544       Phosphoserine.
FT   MOD_RES     548    548       Phosphoserine.
FT   MOD_RES     552    552       Phosphoserine.
FT   MOD_RES     554    554       Phosphothreonine (By similarity).
FT   MOD_RES     591    591       Phosphothreonine (By similarity).
FT   MOD_RES     746    746       Phosphoserine (By similarity).
FT   CROSSLNK    441    441       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   VAR_SEQ     249    285       Missing (in isoform 2).
FT                                /FTId=VSP_028489.
FT   CONFLICT    123    125       PAS -> SAY (in Ref. 2; AAH23677).
SQ   SEQUENCE   846 AA;  93276 MW;  3B4EEDAFEAC93C56 CRC64;
     MESGPRVEPG PGAPAAVLAR IPQEPRPSPE GDPSPPPPPT PMSALVPDTP PDTPPALKTA
     TNPKQLPLEP GNPTGQISPQ PAPPQEECPS SEAKSRGPTP TATGPREAKP SRRSSQPSPT
     TVPASDSPPA KQDVKKAGER HKLAKERREE RAKYLAAKKA VWLEKEEKAK ALREKQLQER
     RRRLEEQRLK AEQRRAALEE RQRQKLEKNK ERYEAAIQRS VKKTWAEIRQ QRWSWAGALH
     HSSPGRKTSG SRCSVSAVNL PKHVDSIINK RLSKSSATLW NSPSRNRSLQ LSAWESSIVD
     RLMTPTLSFL ARSRSAVTLP RNGRDQGRGS GPGRRPTRAR AGASLAPGPH PDRTHPSAAV
     PVCPRSASAS PLTPCSAPRS AHRCTPSGER PERRKPGAGG SPALARRRLE ATPVQKKEKK
     DKERENEKEK SALARERNLK KRQSLPASIR PRLSTGSELS PKSKARPSSP STTWHRPASP
     CPSPGPGHAL PPKPPSPRGT TASPKGRVRR KEEAKESPSP SGPEDKNHRK SRAAEEKEPA
     APASPAPSPV PSPTPAQPQK EQSSTQIPAE TAVPAVPAAP TAPPTAAPSV TPSKPMAGTT
     DREEATRLLA EKRRQAREQR EREEQERKLQ AERDKRMREE QLAREAEARA EREAEARRRE
     EQEAREKAQA EQEEQERLQK QKEEAEARSR EEAERQRQER EKHFQKEEQE RQERRKRLEE
     IMKRTRKSEA AETKKQDAKE TAANNSGPDP VKAVETRPSG LQKDSMQKEE LAPQEPQWSL
     PSKEMPGSLV NGLQPLPAHQ ENGFSPKGTA GDKSLGRTAE GLLPFAEAEA FLKKAVVQPP
     QVTEVL
//
ID   SFR18_MOUSE             Reviewed;         805 AA.
AC   A2AJT4; Q9CS92;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 27.
DE   RecName: Full=Splicing factor, arginine/serine-rich 18;
DE   AltName: Full=Serine/arginine-rich-splicing regulatory protein 130;
DE            Short=SRrp130;
DE   AltName: Full=Splicing factor, arginine/serine-rich 130;
GN   Name=Sfrs18; Synonyms=Srrp130;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-695.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- SUBUNIT: Interacts with PNN (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the splicing factor SR family.
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DR   EMBL; AL772187; CAM22884.1; -; Genomic_DNA.
DR   EMBL; AK017507; BAB30779.3; -; mRNA.
DR   IPI; IPI00808191; -.
DR   UniGene; Mm.100117; -.
DR   STRING; A2AJT4; -.
DR   PhosphoSite; A2AJT4; -.
DR   PRIDE; A2AJT4; -.
DR   Ensembl; ENSMUST00000029911; ENSMUSP00000029911; ENSMUSG00000028248.
DR   Ensembl; ENSMUST00000098238; ENSMUSP00000095840; ENSMUSG00000028248.
DR   MGI; MGI:1913875; Sfrs18.
DR   HOVERGEN; HBG062408; -.
DR   InParanoid; A2AJT4; -.
DR   OrthoDB; EOG444KM4; -.
DR   Bgee; A2AJT4; -.
DR   CleanEx; MM_SFRS18; -.
DR   Genevestigator; A2AJT4; -.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Coiled coil; Nucleus; Phosphoprotein.
FT   CHAIN         1    805       Splicing factor, arginine/serine-rich 18.
FT                                /FTId=PRO_0000292655.
FT   COILED      237    276       Potential.
FT   COILED      427    461       Potential.
FT   COMPBIAS      4     56       Gln-rich.
FT   COMPBIAS    100    222       Pro-rich.
FT   COMPBIAS    508    636       Ser-rich.
FT   COMPBIAS    655    801       Lys/Ser-rich.
FT   MOD_RES     211    211       Phosphoserine.
FT   MOD_RES     290    290       Phosphoserine (By similarity).
FT   MOD_RES     311    311       Phosphoserine (By similarity).
FT   MOD_RES     313    313       Phosphoserine (By similarity).
FT   MOD_RES     321    321       Phosphoserine (By similarity).
FT   MOD_RES     410    410       Phosphothreonine (By similarity).
FT   MOD_RES     706    706       Phosphoserine (By similarity).
FT   CONFLICT    695    695       Q -> R (in Ref. 2; BAB30779).
SQ   SEQUENCE   805 AA;  92115 MW;  B73F082E7C486D39 CRC64;
     MWDQGGQPWQ QWPLNQQQWM QSFQHQQDPS QIDWAALAQA WIAQREASGQ QSIVEQPPGM
     MPNGQDMSAM ESGPNNHGNF QGDSNFNRMW QPEWGMHQQP PHPPPEQPWM PPAPGPMDIV
     PPSEDSNSQD SGEFAPDNRH IFNQNNHNFG GPPDNFAVGP VNQFDYQHGA AFGPPQGGFH
     PPYWQPGPPG PPAPTQNRRE RPPSFRDRQR SPIALPVKQE PPQIDAVKRR TLPAWIREGL
     EKMEREKQKK LEKERMEQQR SQLSKKEKKA TEDAEGGDGP RLPQRSKFDS DEEDEDAENL
     EAVSSGKVTR SPSPAPQEEH SEPEMTEEEK EYQMMLLTKM LLTEILLDVT DEEIYYVAKD
     AHRKATKAPA KQLAQSSALA SLTGLGGLGG YGSGDSEDER SDRGSESSDT DDEELRHRIR
     QKQEAFWRKE KEQQLLQDKQ IEEEKQQTER VTKEMNEFIH REQNSLSLLE ASEADRDAVN
     DKKRTPNEAP SVLEPKREHK GKEKERGSRS GSSSSGSSSS GSRTSSSSSS VSSSSYSSSS
     GSSCTSSRSS SPKRRKRPSR SRSPPAKARR SRSRSYSRRV KVDSSRTRGK LRDRRRSNRS
     SIERERRRNR SPSRDRRRSR SRSRDRRTNR SSRSRSRDRR KIEDPRGNLS GNSHKHKGEA
     KEQDRKKERS RSVDKDRRKK DKERDRELDK RKEKQKREEK DFKFSSQDDR LKRKRESERT
     FCRSGSISVK VIRHDSRQDS KKNATKDSKR HSGSDSSGRS SSESPGSSKE KKAKKPKHSR
     SRSLEKSQRS GKKASRKHKS KSRSR
//
ID   A2AJW4_MOUSE            Unreviewed;       279 AA.
AC   A2AJW4;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 33.
DE   SubName: Full=MCG51138;
DE   SubName: Full=Protein phosphatase 1 regulatory subunit 3D;
GN   Name=Ppp1r3d; ORFNames=RP23-160K5.3-001, mCG_51138;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Tromans A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL772217; CAM15812.1; -; Genomic_DNA.
DR   EMBL; CH466626; EDL07288.1; -; Genomic_DNA.
DR   IPI; IPI00134958; -.
DR   RefSeq; NP_001078970.1; NM_001085501.1.
DR   UniGene; Mm.472736; -.
DR   ProteinModelPortal; A2AJW4; -.
DR   SMR; A2AJW4; 133-262.
DR   STRING; A2AJW4; -.
DR   CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR   PhosphoSite; A2AJW4; -.
DR   PRIDE; A2AJW4; -.
DR   Ensembl; ENSMUST00000058678; ENSMUSP00000061402; ENSMUSG00000049999.
DR   GeneID; 228966; -.
DR   KEGG; mmu:228966; -.
DR   CTD; 228966; -.
DR   MGI; MGI:1917664; Ppp1r3d.
DR   eggNOG; maNOG08990; -.
DR   GeneTree; ENSGT00530000062978; -.
DR   HOGENOM; HBG715688; -.
DR   HOVERGEN; HBG053658; -.
DR   InParanoid; A2AJW4; -.
DR   OMA; VKVFNAG; -.
DR   OrthoDB; EOG43BMPR; -.
DR   NextBio; 379273; -.
DR   Bgee; A2AJW4; -.
DR   Genevestigator; A2AJW4; -.
DR   InterPro; IPR005036; CBM_21.
DR   InterPro; IPR017434; Pase-1_Glycogen_target-su_met.
DR   Pfam; PF03370; CBM_21; 1.
DR   PIRSF; PIRSF038207; PP1_GT_animal; 1.
DR   PROSITE; PS51159; CBM21; 1.
PE   1: Evidence at protein level;
SQ   SEQUENCE   279 AA;  30510 MW;  6E732E2F60C8F755 CRC64;
     MSKGSGSAPL PSTPGSRKLV PRSLSCLSDM DRRPCRPPGC DPRLRPIIQR RSRSLPTSPE
     RRAKAAGAPG AACGAGCNRQ VRVRFADALG LELAQVKVFN AGDDPSVPLH VLSRLAINSD
     LCCSSQDLEF TLQCLVPDFS PPIETPGFGE RLARQLVCLE RVTCSDLGIS GTVRVRNVAF
     EKQVTVRYTF SGWRSAHEAV ARWRGPAGAE GTEDIFAFGF PVPPFLLELG SQVHFALRYG
     VAGAEYWDNN DGRDYSLTCR SHALHMPRGE CEESWIHFI
//
ID   A2AJW5_MOUSE            Unreviewed;       387 AA.
AC   A2AJW5;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 32.
DE   SubName: Full=Novel protein (9030418K01Rik);
GN   Name=9030418K01Rik; Synonyms=RP23-160K5.4; ORFNames=RP23-160K5.4-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Tromans A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL772217; CAM15813.1; -; Genomic_DNA.
DR   IPI; IPI00661237; -.
DR   RefSeq; NP_001074758.1; NM_001081289.1.
DR   UniGene; Mm.220761; -.
DR   UniGene; Mm.40216; -.
DR   PhosphoSite; A2AJW5; -.
DR   PRIDE; A2AJW5; -.
DR   Ensembl; ENSMUST00000094251; ENSMUSP00000091805; ENSMUSG00000070476.
DR   GeneID; 71532; -.
DR   KEGG; mmu:71532; -.
DR   MGI; MGI:1918782; 9030418K01Rik.
DR   eggNOG; maNOG15225; -.
DR   GeneTree; ENSGT00510000049414; -.
DR   HOGENOM; HBG282865; -.
DR   HOVERGEN; HBG051210; -.
DR   InParanoid; A2AJW5; -.
DR   OMA; PPFNSWD; -.
DR   OrthoDB; EOG4GTKDH; -.
DR   NextBio; 333963; -.
DR   Bgee; A2AJW5; -.
DR   Genevestigator; A2AJW5; -.
PE   4: Predicted;
SQ   SEQUENCE   387 AA;  42134 MW;  724B5D5E801ACA65 CRC64;
     MRDCHQKSSI NAGSSWNQVQ HSKTTSGKRQ SGSQGPHVSS QLRSSLLGIS QPAAEKLMET
     VPTEGIQEQA ALSSRYQAAS GSKLFLDFHS MEIMKGADED SASDLSDSER VAIPPSPFTP
     PELNLRAEEI DPVSFSLHPE LSQAESRQTY PDFLPPPFNS WDLRDMAVVM NSECRSEALP
     RATGFLGKYI DRLLQLEWLQ VQTVQCEKAR AAKAKPPGAS GVLKSPGRGK LLTSALSKPL
     PSPEGISKSG PSRKKGFRHE EAHPSYYAFE TLPNSVDGPG RPRLCSQKQA PELRMEKKKK
     SSKGPKLQPR APPCAEGNPA MEANGNIRIP RQSAVLLDPV DSHRASRTQA HVDLKKKGSA
     NTCGYAPSSS EKKLKTNGAK QSTYKLK
//
ID   A2AJX5_MOUSE            Unreviewed;      1955 AA.
AC   A2AJX5;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 29.
DE   SubName: Full=DENN/MADD domain containing 4C;
GN   Name=Dennd4c; ORFNames=RP24-468M3.1-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Lovell J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RA   McLaren K.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL772228; CAM18278.1; -; Genomic_DNA.
DR   EMBL; BX005084; CAM18278.1; JOINED; Genomic_DNA.
DR   EMBL; BX005084; CAM27931.1; -; Genomic_DNA.
DR   EMBL; AL772228; CAM27931.1; JOINED; Genomic_DNA.
DR   IPI; IPI00348488; -.
DR   UniGene; Mm.273718; -.
DR   UniGene; Mm.472357; -.
DR   PRIDE; A2AJX5; -.
DR   Ensembl; ENSMUST00000082026; ENSMUSP00000080685; ENSMUSG00000038024.
DR   MGI; MGI:1914769; Dennd4c.
DR   eggNOG; roNOG08810; -.
DR   HOGENOM; HBG716720; -.
DR   HOVERGEN; HBG058313; -.
DR   InParanoid; A2AJX5; -.
DR   OMA; FDSAEDT; -.
DR   OrthoDB; EOG43BMMZ; -.
DR   Bgee; A2AJX5; -.
DR   Genevestigator; A2AJX5; -.
DR   InterPro; IPR005112; dDENN.
DR   InterPro; IPR001194; DENN.
DR   InterPro; IPR023341; MABP.
DR   InterPro; IPR005113; uDENN.
DR   Pfam; PF03455; dDENN; 1.
DR   Pfam; PF02141; DENN; 1.
DR   Pfam; PF03456; uDENN; 1.
DR   SMART; SM00801; dDENN; 1.
DR   SMART; SM00799; DENN; 1.
DR   SMART; SM00800; uDENN; 1.
DR   PROSITE; PS50947; DDENN; 1.
DR   PROSITE; PS50211; DENN; 1.
DR   PROSITE; PS51498; MABP; 1.
DR   PROSITE; PS50946; UDENN; 1.
PE   1: Evidence at protein level;
SQ   SEQUENCE   1955 AA;  216455 MW;  3D97B5B382949DFF CRC64;
     MIEDKGPRVT DYFVVAGLTD TSTLLDQEIN RTDTNSIGPK APITDIAVII KSAGETVPEG
     YTCVEATPSA LQANLNYGSL KSPELFLCYR RGRDKPPLTD IGVLYEGKER LMPGCEVIQA
     TPYGRCANVN NSSTTSQRIF ITYRRAPPVR SQNSLAVTDI CVIITSKGET PPHTFCKVDK
     NLNCGMWGSN VFLCYKKSVP ASNAIAYKAG LIFRYPEEDY ESFPLSPSVP LFCLPMGATI
     ECWDPQIKYP LPVFSTFVLT GSSAEKVYGA AIQFYEPYSQ ERLTEKQLTQ LGLLTLVEKR
     VVSKPINSNK CICLLSHWPF FEAFKNFLMF IYKVSVSGPH PLPIEKHISH FMQNIPFPSP
     QRPRILIQLS VHDAFILSQP VSTPLPLSGA NFSSLLMNLG PENCATLLLL VLLESKILLH
     SLRPAVLTGV AEAVVAMIFP FQWQCPYIPL CPLSLAGVLS APLPFIVGVD SRYFDLHDPP
     QDVVCIDLDT NTLYVADERK NINWKQLPKR PCKSLLGTLR RLYQQLCSVH RKPQESSAIE
     MTPIEADYSW QKKMTQLEME IQETFLRFMA SILKGYRSYL RPITEAPSNK ATAADSLFDR
     QGFLKSRDRA YTKFYTLLSK TQIFIRFIEE CSFVSDKDTG LAFFDDCIEK LFPDKGVERT
     EKVDLDSAED TRLIELDDSQ RSEHTVFIMP PEPPPDDGNN LSPQYSYTYF PRLDLKLFDS
     PQKLKLCFNR HPPGSSITNS PALMAKRTKQ EIKTAHKLAK RCYTNPPQWA KYLFSHCYSL
     WFICLPAYVR VSHPKVRALQ QAHDVLVKMR KTDVDPLDEV CYRVVMQLCG LWVNPVLAVR
     VLFEMKTARI KPNAITYGYY NKVVLESPWP SSTRSGIFLW TKVRNVVHGL AQFRQPLKKT
     GQKSQVFSIS APQNAACGSD GDTVSHGSVD SSNDANNGEH TVFVRDLISL DSIDNHSSTG
     GQSDQGYGSK DELVKEGADG HAPEEHTPPE LTTTELHIEE ECDISAIVSK HLQPTPEPQS
     PTEPPAWGSS IVKVPSGLFD TNNRTSTGST STVLFSTQAP VEDAVFSEVT NFKKNGDRGE
     KKQKHFPERS CSFSSESRAG MLLKKSSLDL NSSEMAIMMG ADAKILTAAL TCPKTSPPHV
     TRTHSFENVN CHLADSRTRM SEGTRDSEHR SSPVLEMLEE SQELLEPVVG DNVAETAAEM
     TCNSLQSNSH SDQSRDTQAG AQDPVNKRSS SYATRKAIER EDVETGLDPL SLLATECVEK
     TSDSEDKLFS PVISRNLADE IESYMNLKSP LGSKSCSMEL HGEGNQEPGS PAVFAHPLER
     SSSLPSDRGP PARDSTETEK SSPAVSSSKT LTGRFKPQSP YRAYKDRSTS LSALVRSSPN
     SSLGSVVNSL SGLKLDNILS GPKIDVLKSS MKQAATVASK MWVAVASAYS YSDDEEETNK
     DYSFPAGLED HHIVGETLSP NTSVSGLVPS ELTQSNTSLG SSSSSGDVGK LQCPAGEVPF
     SRNIKGQDFE KSDHGSSQNT SMSSIYQNCA MEVLMSSCSQ CRACGALVYD EEIMAGWTAD
     DSNLNTTCPF CKSNFLPLLN VEFKDLRGSA SFFLKPSTSG DSLQSGSIPS ASEPSEHKPT
     SSSAEPDLIS FMDFSKHSET ITEEASYTVE SSDEIKKTNG DVQSVKMSSV PNSLSKRNVS
     LTRSHSVGGP LQNIDFSQRP FHGVSTVSLP SSLQEDVDHL GKRPSPPPVS VPYLSPLVLR
     KELESLLENE GDQVIHTSSF INQHPIIFWN LVWYFRRLDL PSNLPGLILT SEHCNGGVQL
     PLSSLSQDSK LVYIQLLWDN INLHQEPGEP LYVSWRNLNS EKKPSLLSEQ QQAASALVET
     IRQSIQQNDV LKPINLLSQQ MKPGTKRQRS LYREILFLSL VSLGRENIDI EAFDNEYGLA
     YRSLPSESLE RLQRIDAPPS ISVEWCRKCF GAPLI
//
ID   DCA10_MOUSE             Reviewed;         566 AA.
AC   A2AKB9; A2AKV8; Q3TNI7; Q5U4G6; Q8BHQ2; Q8BHS1; Q8BHX4; Q8K3A5;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 40.
DE   RecName: Full=DDB1- and CUL4-associated factor 10;
DE   AltName: Full=WD repeat-containing protein 32;
GN   Name=Dcaf10; Synonyms=Wdr32;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 112-566 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Head, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
RP   SPLICING.
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3
CC       ubiquitin-protein ligase complex (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with DDB1 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=A2AKB9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2AKB9-2; Sequence=VSP_028516;
CC       Name=3;
CC         IsoId=A2AKB9-3; Sequence=VSP_028514;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=A2AKB9-4; Sequence=VSP_028515;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the WD repeat DCAF10 family.
CC   -!- SIMILARITY: Contains 7 WD repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH27317.1; Type=Erroneous initiation;
CC       Sequence=AAH85101.1; Type=Erroneous initiation;
CC       Sequence=BAC38912.1; Type=Erroneous initiation;
CC       Sequence=CAM20443.1; Type=Erroneous gene model prediction;
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DR   EMBL; AK045241; BAC32276.1; -; mRNA.
DR   EMBL; AK076417; BAC36330.1; -; mRNA.
DR   EMBL; AK083428; BAC38912.1; ALT_INIT; mRNA.
DR   EMBL; AK165246; BAE38101.1; -; mRNA.
DR   EMBL; AL772376; CAM20447.1; -; Genomic_DNA.
DR   EMBL; AL772285; CAM20447.1; JOINED; Genomic_DNA.
DR   EMBL; AL772285; CAM26867.1; -; Genomic_DNA.
DR   EMBL; AL772376; CAM26867.1; JOINED; Genomic_DNA.
DR   EMBL; AL772376; CAM20443.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC027317; AAH27317.1; ALT_INIT; mRNA.
DR   EMBL; BC085101; AAH85101.1; ALT_INIT; mRNA.
DR   IPI; IPI00170055; -.
DR   IPI; IPI00649982; -.
DR   IPI; IPI00867762; -.
DR   IPI; IPI00867908; -.
DR   RefSeq; NP_694807.2; NM_153167.2.
DR   UniGene; Mm.317668; -.
DR   ProteinModelPortal; A2AKB9; -.
DR   SMR; A2AKB9; 171-335, 524-565.
DR   PhosphoSite; A2AKB9; -.
DR   PRIDE; A2AKB9; -.
DR   Ensembl; ENSMUST00000044459; ENSMUSP00000044692; ENSMUSG00000035572.
DR   GeneID; 242418; -.
DR   KEGG; mmu:242418; -.
DR   CTD; 242418; -.
DR   MGI; MGI:2140179; Dcaf10.
DR   eggNOG; roNOG05556; -.
DR   GeneTree; ENSGT00390000012666; -.
DR   HOVERGEN; HBG055755; -.
DR   InParanoid; A2AKB9; -.
DR   OMA; DDEECTC; -.
DR   OrthoDB; EOG4Z36DS; -.
DR   NextBio; 385339; -.
DR   Bgee; A2AKB9; -.
DR   CleanEx; MM_WDR32; -.
DR   Genevestigator; A2AKB9; -.
DR   GO; GO:0080008; C:CUL4 RING ubiquitin ligase complex; ISS:UniProtKB.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Repeat; Ubl conjugation pathway; WD repeat.
FT   CHAIN         1    566       DDB1- and CUL4-associated factor 10.
FT                                /FTId=PRO_0000306834.
FT   REPEAT      173    212       WD 1.
FT   REPEAT      216    254       WD 2.
FT   REPEAT      258    297       WD 3.
FT   REPEAT      303    342       WD 4.
FT   REPEAT      415    455       WD 5.
FT   REPEAT      477    515       WD 6.
FT   REPEAT      533    566       WD 7.
FT   COMPBIAS      3     68       Pro-rich.
FT   VAR_SEQ       1    308       Missing (in isoform 3).
FT                                /FTId=VSP_028514.
FT   VAR_SEQ     226    566       Missing (in isoform 4).
FT                                /FTId=VSP_028515.
FT   VAR_SEQ     359    395       Missing (in isoform 2).
FT                                /FTId=VSP_028516.
FT   CONFLICT    202    202       F -> L (in Ref. 1; BAE38101).
FT   CONFLICT    235    235       C -> S (in Ref. 3; AAH27317).
FT   CONFLICT    323    323       S -> P (in Ref. 1; BAC38912).
SQ   SEQUENCE   566 AA;  61558 MW;  4923778CDA90E6F8 CRC64;
     MFPFGPHSPG GDETAGAEEP PPLGGPAAAS RPPSPAPRPA SPQRGADAAS PPPVAGSPRL
     PGGPAVSPAE RAGEFAAPGA LELSAATASA SQAKLSPSSS PRRRSRPDWR AGGRSRQGLG
     AGLGGPGARL FGWLRERSLG RGLFVDPARD NFRTMTNLYG SIHPADSVYL STRTHGAVFN
     LEYSPDGSVL TVACEQTEVL LFDPISSKHI KTLSEAHEDC VNNIRFLDNR LFATCSDDTT
     IALWDLRKLN TKVCTLHGHT SWVKNIEYDT NTRLLVTSGF DGNVIIWDTN RCTEDGCPHK
     KFFHTRFLMR MRLTPDCSKM LISTSSGYLL ILHELDLTKS LEVGSYPILR ARRTTSSSDL
     TTTSSSSGSR VSGSPCHHND SNSTEKHMSR ASQREGVSPR NSLEVLTPEV PGERDRGNCI
     TSLQLHPKGW ATLLRCSSNT DDQEWTCVYE FQEGAPVRPV SPRCSLRLTH YIEEANVGRG
     YIKELCFSPD GRMISSPHGY GIRLLGFDKQ CSELVDCLPK EASPLRVIRS LYSHNDVVLT
     TKFSPTHCQI ASGCLSGRVS LYQPKF
//
ID   A2ALF9_MOUSE            Unreviewed;       158 AA.
AC   A2ALF9;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-FEB-2011, entry version 24.
DE   SubName: Full=Phosphatase and actin regulator 4;
DE   Flags: Fragment;
GN   Name=Phactr4; ORFNames=RP23-63D8.1-004;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Tromans A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL805897; CAM26522.1; -; Genomic_DNA.
DR   IPI; IPI00648561; -.
DR   UniGene; Mm.158361; -.
DR   PRIDE; A2ALF9; -.
DR   Ensembl; ENSMUST00000136711; ENSMUSP00000122194; ENSMUSG00000066043.
DR   MGI; MGI:2140327; Phactr4.
DR   GeneTree; ENSGT00390000004420; -.
DR   Bgee; A2ALF9; -.
DR   Genevestigator; A2ALF9; -.
PE   4: Predicted;
FT   NON_TER     158    158
SQ   SEQUENCE   158 AA;  17038 MW;  FE6149524CB85A34 CRC64;
     MGQADVSRPV NPDAVEEAEQ PSGDPGMGMD SVEAGDTTPP TKRKSKFSAL GKIFKPWKWR
     KKKSSDKFKE TSEDGEDSGK LSHAALKNGH TTPIGSARSS SPVLVEEEPE RSLRNLTPEE
     ESKKRLGSTG SQPNSEAEPG PEHAPKQPLL PPKRPLSS
//
ID   AJAP1_MOUSE             Reviewed;         412 AA.
AC   A2ALI5; B2RVK0;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 35.
DE   RecName: Full=Adherens junction-associated protein 1;
GN   Name=Ajap1; Synonyms=Gm573;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Plays a role in cell adhesion and cell migration (By
CC       similarity).
CC   -!- SUBUNIT: Forms a complex with CDH1 and CTNNB1; interacts directly
CC       with CTNNB1. Interacts with AP1M2 and BSG/CD147 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Basolateral cell membrane; Single-pass type
CC       III membrane protein (By similarity). Apical cell membrane;
CC       Single-pass type III membrane protein (By similarity). Cell
CC       junction, adherens junction (By similarity). Note=Mainly
CC       basolateral. Localization is mediated by AP1M2 (By similarity).
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DR   EMBL; AL954390; CAM14993.1; -; Genomic_DNA.
DR   EMBL; AL805910; CAM14993.1; JOINED; Genomic_DNA.
DR   EMBL; AL805910; CAM15168.1; -; Genomic_DNA.
DR   EMBL; AL954390; CAM15168.1; JOINED; Genomic_DNA.
DR   EMBL; BC147229; AAI47230.1; -; mRNA.
DR   EMBL; BC147230; AAI47231.1; -; mRNA.
DR   EMBL; BC147654; AAI47655.1; -; mRNA.
DR   EMBL; BC147658; AAI47659.1; -; mRNA.
DR   IPI; IPI00125794; -.
DR   RefSeq; NP_001092769.1; NM_001099299.1.
DR   UniGene; Mm.318874; -.
DR   STRING; A2ALI5; -.
DR   PhosphoSite; A2ALI5; -.
DR   PRIDE; A2ALI5; -.
DR   Ensembl; ENSMUST00000047707; ENSMUSP00000037697; ENSMUSG00000039546.
DR   Ensembl; ENSMUST00000105646; ENSMUSP00000101271; ENSMUSG00000039546.
DR   GeneID; 230959; -.
DR   KEGG; mmu:230959; -.
DR   CTD; 230959; -.
DR   MGI; MGI:2685419; Ajap1.
DR   eggNOG; roNOG15381; -.
DR   GeneTree; ENSGT00510000048586; -.
DR   HOGENOM; HBG716989; -.
DR   HOVERGEN; HBG096853; -.
DR   InParanoid; A2ALI5; -.
DR   OMA; ESNTFPG; -.
DR   OrthoDB; EOG4KD6MS; -.
DR   NextBio; 380314; -.
DR   Bgee; A2ALI5; -.
DR   CleanEx; MM_AJAP1; -.
DR   Genevestigator; A2ALI5; -.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Cell junction; Cell membrane; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    412       Adherens junction-associated protein 1.
FT                                /FTId=PRO_0000284802.
FT   TOPO_DOM      1    284       Extracellular (Potential).
FT   TRANSMEM    285    305       Helical; (Potential).
FT   TOPO_DOM    306    412       Cytoplasmic (Potential).
FT   REGION      305    412       Targeting signals (By similarity).
FT   COMPBIAS    175    259       Thr-rich.
SQ   SEQUENCE   412 AA;  44772 MW;  FA54456D22247447 CRC64;
     MWIQQLLGLS SMSIRWPGRS LGSHAWILIA MLQLAVDFPS CDSLGPGPEF RLLSRPQRPQ
     RLWSLRSGPP TRLPTPAWSP RAARAERAHG PIQMQTPRAR RAHRPRDQVA TLGPKGGLTK
     PPAATRSSPS LASATASSSI VTAGAAEHQG LLRRGRRHTH DTEFNDFDFR GGRPTTETEF
     IAWGPTGDED ALESNTFPGG FGPTTVSILQ TRKTTVATTT TTTAASTATA MTLQTKGVTE
     SLDPWKRTPV GVSTTEPSTS PSSNGKDIQP PRILGETSGL AVHQIITITV SLIMVIAALI
     TTLVLKNCCA PSGHTRRNSH QRKMNQQEES CQNLTDFTPA RVPSSVDIFT AYNETLQCSH
     ECVRASVPVY ADETLHSTGE YKSTFNGNRT SSADRHLIPV AFVSEKWFEI SC
//
ID   A2ALK6_MOUSE            Unreviewed;       899 AA.
AC   A2ALK6;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   SubName: Full=Erythrocyte protein band 4.1-like 4b;
GN   Name=Epb4.1l4b; ORFNames=RP23-318H16.1-002;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Wood J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Andrew R.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 FERM domain.
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DR   EMBL; AL805921; CAM19969.1; -; Genomic_DNA.
DR   EMBL; AL831761; CAM19969.1; JOINED; Genomic_DNA.
DR   EMBL; AL831761; CAM20656.1; -; Genomic_DNA.
DR   EMBL; AL805921; CAM20656.1; JOINED; Genomic_DNA.
DR   IPI; IPI00649652; -.
DR   UniGene; Mm.28217; -.
DR   UniGene; Mm.381403; -.
DR   ProteinModelPortal; A2ALK6; -.
DR   SMR; A2ALK6; 84-416.
DR   PRIDE; A2ALK6; -.
DR   Ensembl; ENSMUST00000095076; ENSMUSP00000092687; ENSMUSG00000028434.
DR   CTD; 54357; -.
DR   MGI; MGI:1859149; Epb4.1l4b.
DR   eggNOG; roNOG10628; -.
DR   GeneTree; ENSGT00600000084386; -.
DR   HOGENOM; HBG447107; -.
DR   HOVERGEN; HBG051434; -.
DR   InParanoid; A2ALK6; -.
DR   OrthoDB; EOG444KKG; -.
DR   NextBio; 311146; -.
DR   Bgee; A2ALK6; -.
DR   Genevestigator; A2ALK6; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0019898; C:extrinsic to membrane; IEA:InterPro.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR000798; Ez/rad/moesin.
DR   InterPro; IPR014847; FERM-adjacent.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH_type.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   4: Predicted;
SQ   SEQUENCE   899 AA;  99783 MW;  D27E1913C67C483F CRC64;
     MLRFLRRTFG RRSMQRYARG AAGRGAAGLG DERDGGPRGG PAAAASSSVL PAAPGGSVFP
     AGGGPLLTGG AAVHISASGA AKATLYCRVF LLDGTEVSVD LPKHAKGQDL FDQIVYHLDL
     VETDYFGLQF LDSAQVTHWL DHAKPIKKQM KVGPAYALHF RVKYYSSEPN NLREEFTRYL
     FVLQLRHDIL SGKLKCPYET AVELAALCLQ AELGECELPE HTPELVSEFR FIPNQTEAME
     FDIFQRWKEY RGKSPAQAEL SYLNKAKWLE MYGVDMHVVR GRDGCEYSLG LTPTGILIFE
     GANKIGLFFW PKITKMDFKK SKLTLVVVED DDQGREQEHT FVFRLDSART CKHLWKCAVE
     HHAFFRLRTP SNSKSARSDF IRLGSRFRFS GRTEYQATHG SRLRRTSTFE RKPSKRYPSR
     RHSTFKASNP VIAAQLCSKA NPEVHNYQPQ YHPDVHPSQP RWRPHSPNVS YPLPSPALSP
     TERLPFSLEE NGGTPFAPKT SGRHHHQHQH QHHSNYGLSL TLENKEAPLR SPNASKALTK
     LSPGTPALYS EAAAHLKKLE LETVKAVAPW PALHININKA EEKKVSEKTL QTPLLPSPVA
     DHVKCNILKA QLENASRVNA QIGKEEPSFV NINKKSNLQD TNVRSPIPIR VEAAQPAVEK
     PEIKPPRVRR LTRQYSFDED DLPPDLAEAV GATTATTTTT TTTTMSATQV SVSLASPKIQ
     KVSSPQKSEV KSPLSPGAKS PSDHGGSLTL GPGDLLMDFT EATPLAEPAS SPHCAHSRCS
     PPLSLPMKEE TTGVCMYRPI KTRLIKTFPA EPVMNPFPDP FTTGPQFPAD FRENKLQCCP
     GQSSPLIPTV TLRPLTETVA TVQTIYTSRK PVSLATSAET LRQELEREKM MKRLLMTEL
//
ID   PTPN3_MOUSE             Reviewed;         913 AA.
AC   A2ALK8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type 3;
DE            EC=3.1.3.48;
GN   Name=Ptpn3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- FUNCTION: May act at junctions between the membrane and the
CC       cytoskeleton (By similarity).
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity). Cytoplasm, cytoskeleton (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class subfamily.
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
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DR   EMBL; AL805921; CAM19971.1; -; Genomic_DNA.
DR   IPI; IPI00621903; -.
DR   RefSeq; NP_035337.2; NM_011207.2.
DR   UniGene; Mm.246552; -.
DR   ProteinModelPortal; A2ALK8; -.
DR   SMR; A2ALK8; 28-311, 508-601, 607-904.
DR   STRING; A2ALK8; -.
DR   PhosphoSite; A2ALK8; -.
DR   PRIDE; A2ALK8; -.
DR   Ensembl; ENSMUST00000043585; ENSMUSP00000042412; ENSMUSG00000038764.
DR   Ensembl; ENSMUST00000075637; ENSMUSP00000075063; ENSMUSG00000038764.
DR   GeneID; 545622; -.
DR   KEGG; mmu:545622; -.
DR   CTD; 545622; -.
DR   MGI; MGI:105307; Ptpn3.
DR   HOGENOM; HBG382957; -.
DR   HOVERGEN; HBG008322; -.
DR   InParanoid; A2ALK8; -.
DR   OMA; RESHSRE; -.
DR   OrthoDB; EOG4RNB7S; -.
DR   PhylomeDB; A2ALK8; -.
DR   BRENDA; 3.1.3.48; 244.
DR   Bgee; A2ALK8; -.
DR   CleanEx; MM_PTPN3; -.
DR   Genevestigator; A2ALK8; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR012151; Tyr_Pase_non-rcpt_typ-3/4.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PIRSF; PIRSF000927; Tyr-Ptase_nr3; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00194; PTPc; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasm; Cytoskeleton; Hydrolase; Membrane;
KW   Protein phosphatase.
FT   CHAIN         1    913       Tyrosine-protein phosphatase non-receptor
FT                                type 3.
FT                                /FTId=PRO_0000320074.
FT   DOMAIN       29    312       FERM.
FT   DOMAIN      510    582       PDZ.
FT   DOMAIN      646    901       Tyrosine-protein phosphatase.
FT   REGION      842    848       Substrate binding (By similarity).
FT   ACT_SITE    842    842       Phosphocysteine intermediate (By
FT                                similarity).
FT   BINDING     811    811       Substrate (By similarity).
FT   BINDING     886    886       Substrate (By similarity).
SQ   SEQUENCE   913 AA;  103896 MW;  8D86101FA691142A CRC64;
     MTSRLRALGG RINNTRTSEL PKEKTRSEVI CSIRFLDGLV QTFKVNKQDL GQSLLDMAYG
     HLGVTEKEYF GLQHGDDPVD SPRWLEASKP LRKQLKGGFP CTLHFRVRYF IPDPNTLQQE
     QTRHLYFLQL KMDVCEGRLT CPLNSAVVLA SYAVQSHFGD FNSSIHHPGY LADSQFIPDQ
     NDDFLSKVES LHEQHSGLKQ SEAESCYINI ARTLDFYGVE LHGGRDLHNL DLMIGIASAG
     IAVYRKYICT SFYPWVNILK ISFKRKKFFI HQRQKQAESR EHIVAFNMLN YRSCKNLWKS
     CVEHHSFFQA KKLLPQEKNV LSQYWTLGSR NPKKSVNNQY CKKVIGGMVW NPVMRRSLSV
     ERLETKSLPS RSPPITPNWR SPRLRHEIRK PRHSSADNLA NEMTYITETE DVFYTYKGPL
     SPKDSDSEVS QNHSPHRESL SENNPAQSCL TQKSSSSVSP SSNAPGSCSP DGVDQRFLED
     YHKVTKGGFV EDASQYYCDK SDDGDGYLVL IRITPDEEGR FGFNLKGGVD QKMPLVVSRI
     NPESPADTCM PKLNEGDQIV LINGRDISEH THDQVVMFIK ASRESHSREL ALVIRRKAVR
     SLAEIRSEDE LSQLFPEAMF PACPEGGDSL EGSMELLKKG LESGTVLIQF EQLYRKKPGL
     AVSFAKLPQN LDKNRYKDVL PYDTTRVLLQ GNEDYINASY VNMEMPAANL VNKYIATQGP
     LPNTCAQFWQ VVWDQKLSLV VMLTTLTERG RTKCHQYWPD PPDIMDHGIF HIQCQTEDCT
     IAYVSREMLV TNTETGEEHT VTHLQYVAWP DHGVPDDSSD FLEFVKYVRS LRVDGEPALV
     HCSAGIGRTG VLVTMETAMC LIERNLPVYP LDIVRKMRDQ RAMMVQTSSQ YKFVCEAILR
     VYEEGLVQRL DPS
//
ID   A2ALL9_MOUSE            Unreviewed;      1173 AA.
AC   A2ALL9;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   SubName: Full=ATPase, Ca++ transporting, plasma membrane 3;
GN   Name=Atp2b3; ORFNames=RP23-329M9.1-002;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Whitehead S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       family.
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DR   EMBL; AL805924; CAM21052.1; -; Genomic_DNA.
DR   IPI; IPI00776035; -.
DR   UniGene; Mm.210095; -.
DR   ProteinModelPortal; A2ALL9; -.
DR   STRING; A2ALL9; -.
DR   PRIDE; A2ALL9; -.
DR   Ensembl; ENSMUST00000114479; ENSMUSP00000110123; ENSMUSG00000031376.
DR   MGI; MGI:1347353; Atp2b3.
DR   eggNOG; roNOG14596; -.
DR   GeneTree; ENSGT00510000046331; -.
DR   HOVERGEN; HBG061286; -.
DR   PhylomeDB; A2ALL9; -.
DR   Bgee; A2ALL9; -.
DR   Genevestigator; A2ALL9; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005388; F:calcium-transporting ATPase activity; IEA:InterPro.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   InterPro; IPR022141; ATP_Ca_trans_C.
DR   InterPro; IPR023306; ATPase_cation_domN.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR006408; ATPase_P-typ_Ca-transp_PMCA.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023300; ATPase_P-typ_cyto_domA.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Gene3D; G3DSA:2.70.150.10; ATPase_P-typ_cyto_domA; 1.
DR   Gene3D; G3DSA:3.40.1110.10; ATPase_P-typ_cyto_domN; 1.
DR   Gene3D; G3DSA:1.20.1110.10; ATPase_P-typ_TM_dom; 1.
DR   Pfam; PF12424; ATP_Ca_trans_C; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81660; ATPase_cation_domN; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01517; ATPase-IIB_Ca; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 4.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Hydrolase; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Transmembrane; Transmembrane helix; Transport.
SQ   SEQUENCE   1173 AA;  128739 MW;  1CE904EE3BD5D94C CRC64;
     MGDMANSSIE FHPKPQQQRE VPHVGGFGCT LAELRSLMEL RGAEALQKIQ EAYGDVSGLC
     RRLKTSPTEG LADNTNDLEK RRQIYGQNFI PPKQPKTFLQ LVWEALQDVT LIILEVAAIV
     SLGLSFYAPP GEESEACGNV SGGAEDEGEA EAGWIEGAAI LLSVICVVLV TAFNDWSKEK
     QFRGLQSRIE QEQKFTVIRN GQLLQVPVAA LVVGDIAQVK YGDLLPADGV LIQGNDLKID
     ESSLTGESDH VRKSADKDPM LLSGTHVMEG SGRMVVTAVG VNSQTGIIFT LLGAGGEEEE
     KKDKKGKQQD GAMDSSQTRA KKQDGAVAME MQPLKSAEGG EMEEREKKKA NVPKKEKSVL
     QGKLTKLAVQ IGKAGLVMSA ITVIILVLYF VIETFVVDGR VWLAECTPVY VQYFVKFFII
     GVTVLVVAVP EGLPLAVTIS LAYSVKKMMK DNNLVRHLDA CETMGNATAI CSDKTGTLTT
     NRMTVVQSYL GDTHYKEIPA PSALTPKILD LLVHAISINS AYTTKILPPE KEGALPRQVG
     NKTECALLGF VLDLKRDFQP VREQIPEDQL YKVYTFNSVR KSMSTVIRMP DGGFRLFSKG
     ASEILLKKCT NILNSNGELR GFRPRDRDDM VKKIIEPMAC DGLRTICIAY RDFSAIQEPD
     WDNENEVVGD LTCIAVVGIE DPVRPEVPEA IRKCQRAGIT VRMVTGDNIN TARAIAAKCG
     IIQPGEDFLC LEGKEFNRRI RNEKGEIEQE RLDKVWPKLR VLARSSPTDK HTLVKGIIDS
     TTGEQRQVVA VTGDGTNDGP ALKKADVGFA MGIAGTDVAK EASDIILTDD NFTSIVKAVM
     WGRNVYDSIS KFLQFQLTVN VVAVIVAFTG ACITQDSPLK AVQMLWVNLI MDTFASLALA
     TEPPTESLLL RKPYGRDKPL ISRTMMKNIL GHAVYQLTII FTLLFVGELF FDIDSGRNAP
     LHSPPSEHYT IIFNTFVMMQ LFNEINARKI HGERNVFDGI FSNPIFCTIV LGTFGIQIVI
     VQFGGKPFSC SPLSTEQWLW CLFVGVGELV WGQVIATIPT SQLKCLKEAG HGPGKDEMTD
     EELAEGEEEI DHAERELRRG QILWFRGLNR IQTQMEVVST FKRSGSFQGA VRRRSSVLSQ
     LHDVTNLSTP THVTLSAAKP PSAAGNPGGE SIP
//
ID   A2ALS5_MOUSE            Unreviewed;       694 AA.
AC   A2ALS5;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 28.
DE   SubName: Full=Rap1 GTPase-activating protein;
GN   Name=Rap1gap; ORFNames=RP23-277N22.1-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Tromans A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL805954; CAM19421.1; -; Genomic_DNA.
DR   IPI; IPI00674263; -.
DR   UniGene; Mm.180763; -.
DR   ProteinModelPortal; A2ALS5; -.
DR   SMR; A2ALS5; 109-445.
DR   STRING; A2ALS5; -.
DR   PRIDE; A2ALS5; -.
DR   Ensembl; ENSMUST00000097837; ENSMUSP00000095448; ENSMUSG00000041351.
DR   MGI; MGI:109338; Rap1gap.
DR   HOVERGEN; HBG016371; -.
DR   OrthoDB; EOG43FGWB; -.
DR   Bgee; A2ALS5; -.
DR   Genevestigator; A2ALS5; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR003109; GoLoco_motif.
DR   InterPro; IPR000331; Rap_GAP.
DR   Pfam; PF02188; GoLoco; 1.
DR   Pfam; PF02145; Rap_GAP; 1.
DR   SMART; SM00390; GoLoco; 1.
DR   PROSITE; PS50877; GOLOCO; 1.
DR   PROSITE; PS50085; RAPGAP; 1.
PE   4: Predicted;
SQ   SEQUENCE   694 AA;  76784 MW;  B4B5ED75448DB722 CRC64;
     MAQPRPPAPH GRPRRGSLPA GAGWQNTDLF EMIEKMQGSR MDEQRCSFPP PLKTEEDYIP
     YPSVHEVLGR EGPFPLILLP QFGGYWIEGT NHEISSLPET EPLQSPTTKV KLECNPTARI
     YRKHFLGKEH FNYYSLDTAL GHLVFSLKYD VIGDQEHLRL LLRTKCRTHH DVIPISCLTE
     FPNVVQMAKL VCEDVNVDRF YPVLYPKASR LIVTFDEHVI SNNFKFGVIY QKLGQTSEEE
     LFSTNEESPA FVEFLEFLGQ KVKLQDFKGF RGGLDVTHGQ TGTESVYCNF RNKEIMFHVS
     TKLPYTEGDA QQLQRKRHIG NDIVAVVFQD ENTPFVPDMI ASNFLHAYVV VQAEGGGPDG
     PLYKVSVTAR DDVPFFGPPL PDPAVFRKGP EFQEFLLTKL INAEYACYKA EKFAKLEERT
     RAALLETLYE ELHIHSQSMM GLGGDDDKME NGSGGGGFFE SFKRVIRSRS QSMDAMGLSN
     KKPNTVSTSH SGSFTPNNPD LAKAAGISLI VPGKSPTRKK SGPFGSRRSS AIGIENIQEV
     QEKRESPPAG QKTPDSGHVS QEPKSENSST QSSPEMPTTK NRVESAAQRT EVLQGFSRSS
     SSASSFTSVV EETEGVDGDD TGLESVSSSG TPHKRDSFLY STWLDDSVST TSGGSSPGLT
     RSPHPDVGKS GDPACPEIKI QLETSEQHTP QMGC
//
ID   A2ALU3_MOUSE            Unreviewed;       278 AA.
AC   A2ALU3;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-FEB-2011, entry version 23.
DE   SubName: Full=DENN/MADD domain containing 1A;
DE   Flags: Fragment;
GN   Name=Dennd1a; ORFNames=RP23-399K8.1-010;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Matthews L.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL805959; CAM22967.1; -; Genomic_DNA.
DR   IPI; IPI00757433; -.
DR   UniGene; Mm.314245; -.
DR   UniGene; Mm.461078; -.
DR   Ensembl; ENSMUST00000040406; ENSMUSP00000047498; ENSMUSG00000035392.
DR   Ensembl; ENSMUST00000136460; ENSMUSP00000115527; ENSMUSG00000035392.
DR   MGI; MGI:2442794; Dennd1a.
DR   GeneTree; ENSGT00550000074339; -.
DR   Bgee; A2ALU3; -.
DR   Genevestigator; A2ALU3; -.
DR   GO; GO:0030665; C:clathrin coated vesicle membrane; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0017124; F:SH3 domain binding; IPI:MGI.
DR   GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:MGI.
PE   4: Predicted;
FT   NON_TER       1      1
FT   NON_TER     278    278
SQ   SEQUENCE   278 AA;  30933 MW;  340BBEE031618062 CRC64;
     AKMGIKEVKN RLKQKDITEN GCVSSAEDPL PKTMPSPQAE TQDPRLREDR RPITVHFGQV
     RPPRPHVVRR PKSNITVEGR RTSVSSPEHL VKPLRHYAVF LSEDSSDEEC RREEAPSTGF
     TESLLFSAPF EWPQPYRTLK ESDSAEGDET ESPEQLVREP WGPTPAPPDR AASIDLLEDV
     FSSLDVEAPL QPLGQAKSLE DLRAPKDLRE QPGSFDYQRL DLCRSERGLS MAAALKLAHP
     YTKLWSLGQD DMAIPSKPSI TSPEKPSALL GTSPALPL
//
ID   SHRM2_MOUSE             Reviewed;        1481 AA.
AC   A2ALU4; Q2EY23; Q8C7N1; Q8CCR2; Q8CDZ0;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   RecName: Full=Protein Shroom2;
DE   AltName: Full=Protein Apxl;
GN   Name=Shroom2; Synonyms=Apxl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, TISSUE
RP   SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH F-ACTIN, AND
RP   FUNCTION.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   PubMed=16684770; DOI=10.1074/jbc.M512463200;
RA   Dietz M.L., Bernaciak T.M., Vendetti F., Kielec J.M., Hildebrand J.D.;
RT   "Differential actin-dependent localization modulates the
RT   evolutionarily conserved activity of Shroom family proteins.";
RL   J. Biol. Chem. 281:20542-20554(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Head, Hippocampus, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NOMENCLATURE.
RX   PubMed=16615870; DOI=10.1186/1471-2121-7-18;
RA   Hagens O., Ballabio A., Kalscheuer V., Kraehenbuhl J.-P.,
RA   Schiaffino M.V., Smith P., Staub O., Hildebrand J.D.,
RA   Wallingford J.B.;
RT   "A new standard nomenclature for proteins related to Apx and Shroom.";
RL   BMC Cell Biol. 7:18-18(2006).
RN   [5]
RP   FUNCTION.
RX   PubMed=16987870; DOI=10.1242/dev.02563;
RA   Fairbank P.D., Lee C., Ellis A., Hildebrand J.D., Gross J.M.,
RA   Wallingford J.B.;
RT   "Shroom2 (APXL) regulates melanosome biogenesis and localization in
RT   the retinal pigment epithelium.";
RL   Development 133:4109-4118(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1165, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-933; SER-960 AND
RP   SER-1165, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May be involved in endothelial cell morphology changes
CC       during cell spreading. In the retinal pigment epithelium, may
CC       regulate the biogenesis of melanosomes and promote their
CC       association with the apical cell surface by inducing gamma-tubulin
CC       redistribution.
CC   -!- SUBUNIT: Interacts with F-actin.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane. Cell junction, tight
CC       junction. Cytoplasm, cytoskeleton. Note=Associates with cortical
CC       F-actin.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A2ALU4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2ALU4-2; Sequence=VSP_024964;
CC   -!- TISSUE SPECIFICITY: Present in kidney tubules and in the
CC       vasculature of many tissues (at protein level).
CC   -!- DEVELOPMENTAL STAGE: Present in the vasculature and in multiple
CC       epithelial populations at E10.5. Present in the cell junctions of
CC       the retinal pigmented epithelium at E15.5 (at protein level).
CC   -!- DOMAIN: The ASD1 domain mediates F-actin binding.
CC   -!- SIMILARITY: Belongs to the shroom family.
CC   -!- SIMILARITY: Contains 1 ASD1 domain.
CC   -!- SIMILARITY: Contains 1 ASD2 domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABD19518.1; Type=Frameshift; Positions=1238, 1244, 1263;
CC       Sequence=BAC26404.1; Type=Erroneous initiation;
CC       Sequence=BAC27781.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; DQ358971; ABD19518.1; ALT_FRAME; mRNA.
DR   EMBL; AK029338; BAC26404.1; ALT_INIT; mRNA.
DR   EMBL; AK032256; BAC27781.1; ALT_INIT; mRNA.
DR   EMBL; AK049850; BAC33957.1; -; mRNA.
DR   EMBL; AL805960; CAM17589.1; -; Genomic_DNA.
DR   EMBL; AL807777; CAM17589.1; JOINED; Genomic_DNA.
DR   EMBL; AL807777; CAM22989.1; -; Genomic_DNA.
DR   EMBL; AL805960; CAM22989.1; JOINED; Genomic_DNA.
DR   IPI; IPI00463074; -.
DR   IPI; IPI00762712; -.
DR   RefSeq; NP_766029.2; NM_172441.2.
DR   UniGene; Mm.40796; -.
DR   ProteinModelPortal; A2ALU4; -.
DR   SMR; A2ALU4; 27-111.
DR   STRING; A2ALU4; -.
DR   PhosphoSite; A2ALU4; -.
DR   PRIDE; A2ALU4; -.
DR   Ensembl; ENSMUST00000062317; ENSMUSP00000057500; ENSMUSG00000045180.
DR   Ensembl; ENSMUST00000101141; ENSMUSP00000098701; ENSMUSG00000045180.
DR   GeneID; 110380; -.
DR   KEGG; mmu:110380; -.
DR   CTD; 110380; -.
DR   MGI; MGI:107194; Shroom2.
DR   eggNOG; roNOG04292; -.
DR   HOVERGEN; HBG096290; -.
DR   OrthoDB; EOG4FBHS5; -.
DR   NextBio; 363891; -.
DR   Bgee; A2ALU4; -.
DR   CleanEx; MM_SHROOM2; -.
DR   Genevestigator; A2ALU4; -.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005938; C:cell cortex; IDA:MGI.
DR   GO; GO:0005913; C:cell-cell adherens junction; IDA:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005923; C:tight junction; IDA:UniProtKB.
DR   GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR   GO; GO:0008013; F:beta-catenin binding; IDA:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR   GO; GO:0045176; P:apical protein localization; ISS:UniProtKB.
DR   GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR   GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR   GO; GO:0045217; P:cell-cell junction maintenance; IDA:MGI.
DR   GO; GO:0043482; P:cellular pigment accumulation; ISS:UniProtKB.
DR   GO; GO:0043583; P:ear development; ISS:UniProtKB.
DR   GO; GO:0032401; P:establishment of melanosome localization; ISS:UniProtKB.
DR   GO; GO:0008057; P:eye pigment granule organization; ISS:UniProtKB.
DR   GO; GO:0002089; P:lens morphogenesis in camera-type eye; ISS:UniProtKB.
DR   GO; GO:0032438; P:melanosome organization; IMP:UniProtKB.
DR   GO; GO:0030835; P:negative regulation of actin filament depolymerization; IDA:MGI.
DR   InterPro; IPR014800; ASD1.
DR   InterPro; IPR014799; ASD2.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF08688; ASD1; 1.
DR   Pfam; PF08687; ASD2; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS51306; ASD1; 1.
DR   PROSITE; PS51307; ASD2; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Alternative splicing; Cell junction;
KW   Cell membrane; Cytoplasm; Cytoskeleton; Developmental protein;
KW   Membrane; Microtubule; Phosphoprotein; Tight junction.
FT   CHAIN         1   1481       Protein Shroom2.
FT                                /FTId=PRO_0000286063.
FT   DOMAIN       26    108       PDZ.
FT   DOMAIN      705    807       ASD1.
FT   DOMAIN     1185   1476       ASD2.
FT   MOD_RES     285    285       Phosphoserine.
FT   MOD_RES     372    372       Phosphothreonine (By similarity).
FT   MOD_RES     933    933       Phosphotyrosine.
FT   MOD_RES     960    960       Phosphoserine.
FT   MOD_RES    1165   1165       Phosphoserine.
FT   MOD_RES    1209   1209       N6-acetyllysine (By similarity).
FT   MOD_RES    1308   1308       Phosphoserine (By similarity).
FT   VAR_SEQ       1   1035       Missing (in isoform 2).
FT                                /FTId=VSP_024964.
FT   CONFLICT    274    274       F -> S (in Ref. 2; ABD19518).
FT   CONFLICT    458    458       P -> S (in Ref. 2; ABD19518).
FT   CONFLICT    603    603       R -> C (in Ref. 2; ABD19518).
FT   CONFLICT   1012   1012       N -> K (in Ref. 2; BAC27781).
FT   CONFLICT   1100   1100       A -> S (in Ref. 2; ABD19518).
FT   CONFLICT   1227   1227       E -> K (in Ref. 2; ABD19518).
SQ   SEQUENCE   1481 AA;  164703 MW;  3C5C96100263E393 CRC64;
     MEGAEPRARP ERLAEAEAPA TDGVRLVEVQ LSGGAPWGFT LKGGREHGEP LVITKIEEGS
     KAAAVDKLLA GDEIVAINDV SLSGFRQEAI CLVKGSHKTL KLVVKRKSDP SWRPHSWHAT
     KYFDVHPEPA ASLFLNTSGS PSWKSQHQAS SSSHDLSGSW EHTSLQRTSD HFSSMGSIDS
     LDHSSQLYPS GHLSSAKSNS SIDHLGGHSK RDSAYGSFST CSSTPDHTLP KADASSTENI
     LYKVGLWEAS RPGSSRQSQS TGDPQGLQDR PSCFIPRVPG NSSKSPRPED NVEPKIATHG
     RSNFGPVWYV PDKKKAPSPP PLGLPLRSDS FSVAARGHEK ARGPPFSDLA SMQHFITLPH
     VQPRGDHRME TTDRQWKLTH LSSGKEIGNV GYQSEGHLDC RWLCSDDRAG RPSGPPGRLQ
     FSDVHFLKSY HGSQHQQQCS DESPRAPSSP RELLHITPGG GLQEPPEPSQ DDNPTQVRWP
     GSAHQKLDDR GRSHYFPGSL RQPVQGSAQV VIPRGDYWHS DTTPVDLEYP LLRPVGQRTY
     LQQHEETPAS HEKEGYHQLN AGIEGCCSGI QEPPRASRTV RTGLQCPSND FKLVDGESGR
     ISRQRTPMLH SLTQDGTWRP GNSKDCGNDK PPLFDAQVGK PTRRSDRFAT TLRNEIQMRR
     AKLQKSKSTV TLAGDSEAED CAGDWRADVG AVPEGSFPST YKEHLKEAQT RVLKATSFQR
     RDLDPTPADQ YSGPSEHRTF DHSASSSLSS FPGEPDSAPR FCETGLAKAP SSGVGVPHVL
     RIGGRKRFTA EQKLKSYSEP EKINEVGLSG DHRPHPTVRT PEDTVGTFAD RWKFFEETSK
     SLLQKAGHRQ VHCGLPREKA ERPQTGHHEC ESTEPWFQKR SLATSCGEIL SDRKVEKASE
     KLNPPRRLGT FAEYQASWKE QKKPLEARSS GRYHSADDIL DAGLDQQQRP QYIHERSRSS
     PSTDHYSQEV PVEPNRQAED SGDHKEAILC TLQAEEGCSA PSAQPQDSQH VNEDTTFPQP
     ETQLSSKCQH LQTSAMETSR SPSPQFAPQK LTDKPPLLIH EDNSARIERV MDNNTTVKMV
     PIKIVHSESQ PEKESRQSLA CPAELPPLPS GLERDQIKTL STSEQCYSRF CVYTRQEVEA
     PHRARPPEPR PPSTPAPPVR DSCSSPPSLN YGKAKEKTMD DLKSEELARE IVGKDKSLAD
     ILDPSVKIKT TMDLMEGIFP KDEYLLEEAQ QRRKLLPKVP LPRVTEDKKQ DPGMPGVVSL
     ATNSTYYSTS APKAELLIKM KDLQEPEEYS AGDLDHDLSV KKQELIDSIS RKLQVLREAR
     ESLLEDIQAN NALGDEVEAI VKDVCKPNEF DKFRMFIGDL DKVVNLLLSL SGRLARVENA
     LNNLDDNPSP GDRQSLLEKQ RVLTQQHEDA KELKENLDRR ERIVFDILAT YLSEENLADY
     EHFVKMKSAL IIEQRELEDK IHLGEEQLKC LFDSLQPERS K
//
ID   AF9_MOUSE               Reviewed;         569 AA.
AC   A2AM29; Q8VDR6; Q99MK4;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   RecName: Full=Protein AF-9;
DE   AltName: Full=Myeloid/lymphoid or mixed-lineage leukemia translocated to chromosome 3 protein homolog;
GN   Name=Mllt3; Synonyms=Af9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-569, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND INTERACTION WITH CBX8.
RC   STRAIN=Swiss Webster / NIH;
RX   PubMed=11439343; DOI=10.1038/sj.onc.1204478;
RA   Hemenway C.S., de Erkenez A.C., Gould G.C.D.;
RT   "The polycomb protein MPc3 interacts with AF9, an MLL fusion partner
RT   in t(9;11)(p22;q23) acute leukemias.";
RL   Oncogene 20:3798-3805(2001).
CC   -!- SUBUNIT: Interacts with BCOR (By similarity). Interacts with CBX8.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed. Strong expression in
CC       the spleen.
CC   -!- SIMILARITY: Contains 1 YEATS domain.
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DR   EMBL; AL831756; CAM20202.1; -; Genomic_DNA.
DR   EMBL; AL806533; CAM20202.1; JOINED; Genomic_DNA.
DR   EMBL; AL929524; CAM20202.1; JOINED; Genomic_DNA.
DR   EMBL; AL929524; CAM24441.1; -; Genomic_DNA.
DR   EMBL; AL806533; CAM24441.1; JOINED; Genomic_DNA.
DR   EMBL; AL831756; CAM24441.1; JOINED; Genomic_DNA.
DR   EMBL; AL806533; CAM25293.1; -; Genomic_DNA.
DR   EMBL; AL831756; CAM25293.1; JOINED; Genomic_DNA.
DR   EMBL; AL929524; CAM25293.1; JOINED; Genomic_DNA.
DR   EMBL; BC021420; AAH21420.1; -; mRNA.
DR   EMBL; AF333960; AAK28536.1; -; mRNA.
DR   IPI; IPI00473183; -.
DR   RefSeq; NP_081602.3; NM_027326.3.
DR   UniGene; Mm.288898; -.
DR   ProteinModelPortal; A2AM29; -.
DR   SMR; A2AM29; 5-137.
DR   STRING; A2AM29; -.
DR   PhosphoSite; A2AM29; -.
DR   PRIDE; A2AM29; -.
DR   Ensembl; ENSMUST00000078090; ENSMUSP00000077232; ENSMUSG00000028496.
DR   GeneID; 70122; -.
DR   KEGG; mmu:70122; -.
DR   NMPDR; fig|10090.3.peg.9860; -.
DR   CTD; 70122; -.
DR   MGI; MGI:1917372; Mllt3.
DR   HOGENOM; HBG283095; -.
DR   HOVERGEN; HBG004191; -.
DR   InParanoid; A2AM29; -.
DR   OrthoDB; EOG45756W; -.
DR   PhylomeDB; A2AM29; -.
DR   NextBio; 331032; -.
DR   Bgee; A2AM29; -.
DR   Genevestigator; A2AM29; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0009952; P:anterior/posterior pattern formation; IMP:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   GO; GO:0007379; P:segment specification; IMP:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR005033; YEATS.
DR   PANTHER; PTHR23195; YEATS; 1.
DR   Pfam; PF03366; YEATS; 1.
DR   PROSITE; PS51037; YEATS; 1.
PE   1: Evidence at protein level;
KW   Activator; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    569       Protein AF-9.
FT                                /FTId=PRO_0000305124.
FT   DOMAIN        8    112       YEATS.
FT   MOTIF       296    301       Nuclear localization signal (Potential).
FT   COMPBIAS    149    194       Poly-Ser.
FT   COMPBIAS    384    392       Poly-Ser.
FT   COMPBIAS    467    470       Poly-Pro.
FT   MOD_RES     289    289       Phosphoserine (By similarity).
FT   MOD_RES     295    295       Phosphoserine (By similarity).
FT   MOD_RES     413    413       Phosphoserine (By similarity).
FT   MOD_RES     420    420       Phosphoserine (By similarity).
FT   MOD_RES     430    430       Phosphoserine (By similarity).
FT   MOD_RES     484    484       Phosphoserine (By similarity).
FT   CONFLICT    157    157       S -> G (in Ref. 3; AAK28536).
FT   CONFLICT    164    164       S -> G (in Ref. 3; AAK28536).
FT   CONFLICT    172    172       S -> N (in Ref. 3; AAK28536).
FT   CONFLICT    176    176       S -> G (in Ref. 3; AAK28536).
FT   CONFLICT    179    190       Missing (in Ref. 2; AAH21420).
FT   CONFLICT    352    352       M -> T (in Ref. 2; AAH21420).
SQ   SEQUENCE   569 AA;  63375 MW;  120A0604B13675EC CRC64;
     MASSCAVQVK LELGHRAQVR KKPTVEGFTH DWMVFVRGPE HSNIQHFVEK VVFHLHESFP
     RPKRVCKDPP YKVEESGYAG FILPIEVYFK NKEEPKKVRF DYDLFLHLEG HPPVNHLRCE
     KLTFNNPTED FRRKLLKAGG DPNRSIHTSS SSSSSSSSSS SSSSSSSSSS SSSSSSSSSS
     SSSSSSSSSS TSFSKPHKLM KEHKEKPSKD SREHKSAFKE PSRDHNKSSK DSSKKPKENK
     PLKEEKIVPK MAFKEPKPMS KEPKADSNLL TVTSGQQDKK APSKRPPASD SEELSAKKRK
     KSSSEALFKS FSSAPPLILT CSADKKQIKD KSHVKMGKVK IESETSEKKK SMLPPFDDIV
     DPNDSDVEEN MSSKSDSEQP SPASSSSSSS SSFTPSQTRQ QGPLRSIMKD LHSDDNEEES
     DEAEDNDNDS EMERPVNRGG SRSRRVSLSD GSDSESSSAS SPLHHEPPPP LLKTNNNQIL
     EVKSPIKQSK SDKQIKNGEC DKAYLDELVE LHRRLMTLRE RHILQQIVNL IEETGHFHIT
     NTTFDFDLCS LDKTTVRKLQ SYLETSGTS
//
ID   A2AM62_MOUSE            Unreviewed;       165 AA.
AC   A2AM62;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 31.
DE   SubName: Full=Heterochromatin protein 1, binding protein 3;
DE   Flags: Fragment;
GN   Name=Hp1bp3; ORFNames=RP23-25C1.1-007;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Pelan S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the histone H1/H5 family.
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DR   EMBL; AL807249; CAM18861.1; -; Genomic_DNA.
DR   IPI; IPI00649203; -.
DR   UniGene; Mm.399941; -.
DR   STRING; A2AM62; -.
DR   Ensembl; ENSMUST00000124305; ENSMUSP00000120587; ENSMUSG00000028759.
DR   MGI; MGI:109369; Hp1bp3.
DR   GeneTree; ENSGT00510000047652; -.
DR   InParanoid; A2AM62; -.
DR   Bgee; A2AM62; -.
DR   Genevestigator; A2AM62; -.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   InterPro; IPR005818; Histone_H1/H5.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF00538; Linker_histone; 1.
DR   SMART; SM00526; H15; 1.
PE   3: Inferred from homology;
KW   Chromosome; DNA-binding; Nucleus.
FT   NON_TER     165    165
SQ   SEQUENCE   165 AA;  18480 MW;  A6C075C419CC046D CRC64;
     MPIRRAVNST RETPPKSKLA EGEEEKPEEQ ENETPPATSS EAEQPKGEPE SGEKEENNNK
     SAEEPKKDEK DQSKEKEKKV KKTIPAWATL SASQLARAQR QTPMASSPRP KMDAILTEAI
     KASFQKTGAS VVAIRKYIIH KYPSLGLERR GYLLKQALKR ELNRG
//
ID   A2AM66_MOUSE            Unreviewed;       195 AA.
AC   A2AM66;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-FEB-2011, entry version 22.
DE   SubName: Full=SH2 domain containing 5;
DE   Flags: Fragment;
GN   Name=Sh2d5; ORFNames=RP23-25C1.2-004;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Pelan S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL807249; CAM18865.1; -; Genomic_DNA.
DR   IPI; IPI00649840; -.
DR   UniGene; Mm.271936; -.
DR   PRIDE; A2AM66; -.
DR   Ensembl; ENSMUST00000105822; ENSMUSP00000101448; ENSMUSG00000045349.
DR   Ensembl; ENSMUST00000124239; ENSMUSP00000119052; ENSMUSG00000045349.
DR   MGI; MGI:2446215; Sh2d5.
DR   GeneTree; ENSGT00510000048936; -.
DR   Bgee; A2AM66; -.
DR   Genevestigator; A2AM66; -.
PE   4: Predicted;
FT   NON_TER     195    195
SQ   SEQUENCE   195 AA;  21420 MW;  4E0A899660C7B652 CRC64;
     MQRAGAGARR ASDCGPAPYR PRCIAKLAQY VGSFPVDDLD TQESVGLVQQ QLWALQVHIL
     YLLLCRSFQL AYLLQHPEER AQSEPCLAPV GDLSLKPLCS PGVPPALVRE PFSRDQLSQN
     VHALVSFRRL PAEGLLGSNG KELPESEGRG GTRHIRLGNP YCSPTLVRKK AIRSKVIRSG
     AYRGCTYETQ LQLSA
//
ID   UBR4_MOUSE              Reviewed;        5180 AA.
AC   A2AN08; A2AN07; A2AN09; A2AN10; A2AN11; Q52KI4; Q6PB49; Q6PFC7;
AC   Q80Y11; Q8BGB9; Q8C3E8; Q8C4W5; Q8C8X7; Q8CGE0; Q8CHF3;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 39.
DE   RecName: Full=E3 ubiquitin-protein ligase UBR4;
DE            EC=6.3.2.-;
DE   AltName: Full=N-recognin-4;
DE   AltName: Full=Zinc finger UBR1-type protein 1;
DE   AltName: Full=p600;
GN   Name=Ubr4; Synonyms=Kiaa0462, Zubr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-4461 (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 2599-5180 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, Head, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1290-3369 (ISOFORM 3).
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4020-5180.
RC   STRAIN=C57BL/6, and FVB/N-3; TISSUE=Brain, Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16055722; DOI=10.1128/MCB.25.16.7120-7136.2005;
RA   Tasaki T., Mulder L.C.F., Iwamatsu A., Lee M.J., Davydov I.V.,
RA   Varshavsky A., Muesing M., Kwon Y.T.;
RT   "A family of mammalian E3 ubiquitin ligases that contain the UBR box
RT   motif and recognize N-degrons.";
RL   Mol. Cell. Biol. 25:7120-7136(2005).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=16081543; DOI=10.1073/pnas.0505322102;
RA   DeMasi J., Huh K.-W., Nakatani Y., Muenger K., Howley P.M.;
RT   "Bovine papillomavirus E7 transformation function correlates with
RT   cellular p600 protein binding.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11486-11491(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-181; SER-365;
RP   THR-2712; SER-2716; SER-2719 AND THR-2721, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which is a component of the
CC       N-end rule pathway. Recognizes and binds to proteins bearing
CC       specific N-terminal residues that are destabilizing according to
CC       the N-end rule, leading to their ubiquitination and subsequent
CC       degradation. Together with clathrin, forms meshwork structures
CC       involved in membrane morphogenesis and cytoskeletal organization.
CC       Regulates integrin-mediated signaling. May play a role in
CC       activation of FAK in response to cell-matrix interactions.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with RB1 and calmodulin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential). Cytoplasm (By similarity). Cytoplasm, cytoskeleton
CC       (By similarity). Nucleus (By similarity). Note=Concentrates at the
CC       leading edge of membrane structures involved in actin motility (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=A2AN08-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2AN08-2; Sequence=VSP_025210;
CC       Name=3;
CC         IsoId=A2AN08-3; Sequence=VSP_025213, VSP_025215;
CC       Name=4;
CC         IsoId=A2AN08-4; Sequence=VSP_025211, VSP_025212;
CC       Name=5;
CC         IsoId=A2AN08-5; Sequence=VSP_025214;
CC   -!- TISSUE SPECIFICITY: Widely expressed in adult and embryonic stages
CC       with highest levels in testis and brain.
CC   -!- SIMILARITY: Belongs to the UBR4 family.
CC   -!- SIMILARITY: Contains 1 UBR-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC39609.1; Type=Erroneous initiation;
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DR   EMBL; AK044277; BAC31850.1; -; mRNA.
DR   EMBL; AK080556; BAC37944.1; -; mRNA.
DR   EMBL; AK082231; BAC38442.2; ALT_SEQ; mRNA.
DR   EMBL; AK083644; BAC38980.2; ALT_SEQ; mRNA.
DR   EMBL; AK086097; BAC39609.1; ALT_INIT; mRNA.
DR   EMBL; AL807833; CAM22428.1; -; Genomic_DNA.
DR   EMBL; AL807833; CAM22429.1; -; Genomic_DNA.
DR   EMBL; AL807833; CAM22430.1; -; Genomic_DNA.
DR   EMBL; AL807833; CAM22431.1; -; Genomic_DNA.
DR   EMBL; AB093242; BAC41426.2; -; mRNA.
DR   EMBL; BC040468; AAH40468.1; -; mRNA.
DR   EMBL; BC051096; AAH51096.1; -; mRNA.
DR   EMBL; BC057625; AAH57625.1; -; mRNA.
DR   EMBL; BC059890; AAH59890.1; -; mRNA.
DR   EMBL; BC094329; AAH94329.1; -; mRNA.
DR   IPI; IPI00378681; -.
DR   IPI; IPI00606977; -.
DR   IPI; IPI00648709; -.
DR   IPI; IPI00845523; -.
DR   IPI; IPI00845583; -.
DR   RefSeq; NP_001153791.1; NM_001160319.1.
DR   UniGene; Mm.271956; -.
DR   ProteinModelPortal; A2AN08; -.
DR   SMR; A2AN08; 1658-1724.
DR   PhosphoSite; A2AN08; -.
DR   PRIDE; A2AN08; -.
DR   Ensembl; ENSMUST00000097822; ENSMUSP00000095433; ENSMUSG00000066036.
DR   GeneID; 69116; -.
DR   KEGG; mmu:69116; -.
DR   CTD; 69116; -.
DR   MGI; MGI:1916366; Ubr4.
DR   HOVERGEN; HBG058328; -.
DR   InParanoid; A2AN08; -.
DR   OMA; HQGFGVL; -.
DR   OrthoDB; EOG49W2DG; -.
DR   NextBio; 328632; -.
DR   Bgee; A2AN08; -.
DR   Genevestigator; A2AN08; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR003126; Znf_N-recognin.
DR   Pfam; PF02207; zf-UBR; 1.
DR   PROSITE; PS51157; ZF_UBR; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Calmodulin-binding; Cytoplasm;
KW   Cytoskeleton; Ligase; Membrane; Metal-binding; Nucleus;
KW   Phosphoprotein; Transmembrane; Transmembrane helix;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1   5180       E3 ubiquitin-protein ligase UBR4.
FT                                /FTId=PRO_0000286862.
FT   TRANSMEM    329    349       Helical; (Potential).
FT   TRANSMEM    408    428       Helical; (Potential).
FT   ZN_FING    1655   1728       UBR-type.
FT   COMPBIAS      9     15       Poly-Ala.
FT   COMPBIAS    608    626       Pro-rich.
FT   COMPBIAS    811    816       Poly-Leu.
FT   COMPBIAS   2725   2735       Poly-Asp.
FT   MOD_RES     178    178       Phosphoserine.
FT   MOD_RES     181    181       Phosphoserine.
FT   MOD_RES     360    360       Phosphothreonine (By similarity).
FT   MOD_RES     365    365       Phosphoserine.
FT   MOD_RES     619    619       Phosphoserine (By similarity).
FT   MOD_RES     620    620       Phosphoserine (By similarity).
FT   MOD_RES    1083   1083       N6-acetyllysine (By similarity).
FT   MOD_RES    2712   2712       Phosphothreonine.
FT   MOD_RES    2715   2715       Phosphoserine (By similarity).
FT   MOD_RES    2716   2716       Phosphoserine.
FT   MOD_RES    2719   2719       Phosphoserine.
FT   MOD_RES    2721   2721       Phosphothreonine.
FT   VAR_SEQ       1   3159       Missing (in isoform 2).
FT                                /FTId=VSP_025210.
FT   VAR_SEQ     466    474       HQGFGVLSV -> CVSACKLHF (in isoform 4).
FT                                /FTId=VSP_025211.
FT   VAR_SEQ     475   5180       Missing (in isoform 4).
FT                                /FTId=VSP_025212.
FT   VAR_SEQ    2474   2474       E -> ESSETESLTKLD (in isoform 3).
FT                                /FTId=VSP_025213.
FT   VAR_SEQ    2599   2599       T -> TDCFSPRCACWNLGIVGILIGAPLETPSA (in
FT                                isoform 5).
FT                                /FTId=VSP_025214.
FT   VAR_SEQ    2827   2861       Missing (in isoform 3).
FT                                /FTId=VSP_025215.
FT   CONFLICT    445    445       R -> K (in Ref. 1; BAC39609).
SQ   SEQUENCE   5180 AA;  572290 MW;  5F4238194DF88EE0 CRC64;
     MATSGGEEAA AAAPAPGAPA TGQDTTPGWE VAVRPLLSAS YSAFEMKELP QLVASVIESE
     SEILHHEKQY EPFYSSFVAL STHYITTVCS LIPRNQLQSV AAACKVLIEF SLLRLENPDE
     ACAVSQKHLI LLIKGLCTGC SRLDRTEIIT FTAMMKSAKL PQTVKTLSDV EDQKELASPV
     SPELRQKEVQ MNFLNQLTSV FNPRTVPSPP ISPQALVEGE NDEQSSPDQV SAAKTKSVFI
     AQNVASLQEL GGSEKLLRVC LNLPYFLRYI NRFQDAVVAN SFFIMPATVA DATAVRNGFH
     SLVIDVTMAL DTLSLPVLEP LNPSRLQDVT VLSLSCLYAG VSVATCMAIL HVGSAQQVRT
     GSTSSKEDDY ESDAATIVQK CLEIYDMIGQ AISSSRRAGG EHFQNFQLLG AWCLLNSLFL
     ILNLSPTALA DKGKEKDPLA ALRVRDILSR TKEGVGSPKL GPGKGHQGFG VLSVILANHA
     IKLLASLFQD LQVEALHKGW ETDGPPAVLS IMAQSTSTQR IQRLIDSVPL TNLLLTLLST
     SYRKACVLQR QRKGSMSSDA SASTDSNTYY EDDFSSTEED SSQDDDSEPI LGQWFEETIS
     PSKEKAAPPP PPPPPPLESS PRVKSPNKQA SGEKGNILAS RKDPELFSGL ASNILNFITT
     SMLNSRNSFI RSYLSASLSE HHMATLASII KEVDKDGLKG SSDEDFAAAL YHFNHSLVTS
     DLQSPNLQNT LLQQLGVAPF SEGPWPLYIH PQGLSVLSRL LLIWQHKAGA QGDPDVPECL
     KVWDRFLTTM KQNALQGVVP SETEDLNVEH LQLLLLIFHS FSEKGRRAIL TMLVQSIQEL
     SVNMEVQMRT APLILARLLL IFDYLLHQYS KAPVYLFEQV QHNLLSPPFG WASGSQDSSS
     RRANTPLYHG FKEVEENWSK HFSSDAAPQP RFYCVLSTEA SEEDLNRLDS EACEVLFSKP
     VKYDELYSSL TTLLAAGSQL DTTRRKEKKN VTALEACALQ YYFLILWRIL GILPPSKTYM
     NQLAMNSPEM SECDILHTLR WSSRLRISSY VSWIKDHLIK QGMKPEHAGS LIELAASKCS
     SVKYDVEIVE EYFARQISSF CSIDCTAVLQ LHEIPSLQSI YTLDAAVSKV QVSLDEHFSK
     MAAETDPHKS SEITKNLLPA TLQLIDTYAS FTRAYLLQNL NEEGSTEKPS QEKLHGFAAV
     LAIGSSRCKA NTLGPTLVQN LPSSVQSVCE SWNNINTNEF PNIGSWRNAF ANDTIPSESY
     ISAVQAAHLG TLCGQSLPLA ASLKHTLLSL VRLTGDLIVW SDEMNPAQVI RTLLPLLLES
     STESAAEISS NSLERILGPA ESDEFLARVY EKLITGCYNI LANHADPNSG LDESILEECL
     QYLEKQLESS QARKAMEEFF SDGGELVQIM MATANEDLSA KFCNRVLKFF TKLFQLTEKS
     PNPSLLHLCG SLAQLACVEP VRLQAWLTRM TTSPPKDSDQ LEVIQENRQL LQLLTTYIVR
     ENSQVGEGVC AVLLGTLTPM ATDMLANGDG TGFPELMVVM ATLASAGQGA GHLQLHNAAV
     DWLGRCKKYL SQKNVVEKLN ANVMHGKHVM VLECTCHIMS YLADVTNALS QSNGQGPSHL
     SVDGEERAIE VDSDWVEELA VEEEDSQAED SDEDSLCNKL CTFTITQKEF MNQHWYHCHT
     CKMVDGVGVC TVCAKVCHKD HEISYAKYGS FFCDCGAKED GSCLALVKRT PSSGMSSTMK
     ESAFQSEPRV SESLVRHAST SPADKAKVTI SDGKVTDEEK PKKSSLCRTV EGCREELQNQ
     ANFSFAPLVL DMLSFLMDAI QTNFQQASAV GSSSRAQQAL SELHTVDKGV EMTDQLMVPT
     LGSQEGAFEN VRMNYSGDQG QTIRQLISAH VLRRVAMCVL SSPHGRRQHL AVSHEKGKIT
     VLQLSALLKQ ADSSKRKLTL TRLASAPVPF TVLSLTGNPC KEDYLAVCGL KDCHVLTFSS
     SGSVSDHLVL HPQLATGNFI IKAVWLPGSQ TELAIVTADF VKIYDLSIDA LSPTFYFLLP
     SSKIRDVTFL FNEEGKNIIV IMSSAGYMYT QLMEEASSAQ QGPFYVTNVL EINHEDLKDS
     NSQVAGGGVS VYYSHVLQML FFSYSQGRSF AATVSRSTLE VLQLFPINIK SSNGGSKTSP
     ALCQWSEVMN HPGLVCCVQQ TTGVPLVVMV KPGTFLIQEI KTLPAKAKIQ DMVAIRHTAC
     NEQQRTTMIL LCEDGSLRIY MANVENTSYW LQPSLQPSSV ISIMKPVRKR KTATITARTS
     SQVTFPIDFF EHNQQLTDVE FGGNDLLQVY NAQQIKHRLN STGMYVANTK PGGFTIEISN
     NSSTMVMTGM RIQIGTQAIE RAPSYIEIFG RTMQLNLSRS RWFDFPFTRE EALQADRKLS
     LFIGASVDPA GVTMIDAVKI YGKTKEQFGW PDEPPEDFPS ASVSNICPPN LNQSNGTGES
     DSAAPATTSG TVLERLVVSS LEALESCFAV GPIIEKERNK HAAQELATLL LSLPAPASVQ
     QQSKSLLASL HSSRSAYHSH KDQALLSKAV QCLNTSSKEG KDLDPEVFQR LVITARSIAV
     TRPNNLVHFT ESKLPQMETE GADEGKEPQK QEGDGCSFIT QLVNHFWKLH ASKPKNAFLA
     PACLPGLTHI EATVNALVDI IHGYCTCELD CINTASKIYM QMLLCPDPAV SFSCKQALIR
     VLRPRNKRRH VTLPSSPRSN TPMGDKDDDD DDDADEKMQS SGIPDGGHIR QESQEQSEVD
     HGDFEMVSES MVLETAENVN NGNPSPLEAL LAGAEGFPPM LDIPPDADDE TMVELAIALS
     LQQDQQGSSS SALGLQSLGL SGQAPSSSSL DAGTLSDTTA SAPASDDEGS TAATDGSTLR
     TSPADHGGSV GSESGGSAVD SVAGEHSVSG RSSAYGDATA EGHPAGPGSV SSSTGAISTA
     TGHQEGDGSE GEGEGEAEGD VHTSNRLHMV RLMLLERLLQ TLPQLRNVGG VRAIPYMQVI
     LMLTTDLDGE DEKDKGALDN LLAQLIAELG MDKKDVSKKN ERSALNEVHL VVMRLLSVFM
     SRTKSGSKSS ICESSSLISS ATAAALLSSG AVDYCLHVLK SLLEYWKSQQ SDEEPVAASQ
     LLKPHTTSSP PDMSPFFLRQ YVKGHAADVF EAYTQLLTEM VLRLPYQIKK IADTSSRIPP
     PVFDHSWFYF LSEYLMIQQT PFVRRQVRKL LLFICGSKEK YRQLRDLHTL DSHVRGIKKL
     LEEQGIFLRA SVVTASSGSA LQYDTLISLM EHLKACAEIA AQRTINWQKF CIKDDSVLYF
     LLQVSFLVDE GVSPVLLQLL SCALCGSKVL AALAASTGSS SVASSSAPPA ASSGQATTQS
     KSSTKKSKKE EKEKEKEGES SGSQEDQLCT ALVNQLNRFA DKETLIQFLR CFLLESNSSS
     VRWQAHCLTL HIYRNSNKAQ QELLLDLMWS IWPELPAYGR KAAQFVDLLG YFSLKTAQTE
     KKLKEYSQKA VEILRTQNHI LTNHPNSNIY NTLSGLVEFD GYYLESDPCL VCNNPEVPFC
     YIKLSSIKVD TRYTTTQQVV KLIGSHTISK VTVKIGDLKR TKMVRTINLY YNNRTVQAIV
     ELKNKPARWH KAKKVQLTPG QTEVKIDLPL PIVASNLMIE FADFYENYQA STETLQCPRC
     SASVPANPGV CGNCGENVYQ CHKCRSINYD EKDPFLCNAC GFCKYARFDF MLYAKPCCAV
     DPIENEEDRK KAVSNINTLL DKADRVYHQL MGHRPQLENL LCKVNEAAPE KPQEDSGTAG
     GISSTSASVN RYILQLAQEY CGDCKNSFDE LSKIIQKVFA SRKELLEYDL QQREAATKSS
     RTSVQPTFTA SQYRALSVLG CGHTSSTKCY GCASAVTEHC ITLLRALATN PALRHILVSQ
     GLIRELFDYN LRRGAAAIRE EVRQLMCLLT RDNPEATQQM NDLIIGKVST ALKGHWANPD
     LASSLQYEML LLTDSISKED SCWELRLRCA LSLFLMAVNI KTPVVVENIT LMCLRILQKL
     IKPPAPTSKK NKDVPVEALT TVKPYCNEIH AQAQLWLKRD PKASYEAWKK CLPIRGVDGN
     GKSPSKSELH RLYLTEKYVW RWKQFLSRRG KRTTPLDLKL GHNNWLRQVL FTPATQAARQ
     AACTIVEALA TVPSRKQQVL DLLTSYLDEL SVAGECAAEY LALYQKLIAS CHWKVYLAAR
     GVLPYVGNLI TKEIARLLAL EEATLSTDLQ QGYALKSLTG LLSSFVEVES IKRHFKSRLV
     GTVLNGYLCL RKLVLQRTKL IDETQDMLLE MLEDMTTGTE SETKAFMAVC IETAKRYNLD
     DYRTPVFIFE RLCSIIYPEE NEVTEFFVTL EKDPQQEDFL QGRMPGNPYS SNEPGIGPLM
     RDIKNKICQD CDLVALLEDD SGMELLVNNK IISLDLPVAE VYKKVWCATN EGEPMRIVYR
     MRGLLGDATE EFIESLDSTT DEEEDEEEVY RMAGVMAQCG GLQCMLNRLA GVKDFKQGRH
     LLTVLLKLFS YCVKVKVNRQ QLVKLETNTL NVMLGTLNLA LVAEQESKDS GGAAVAEQVL
     SIMEIILDES NAEPLSEDKG NLLLTGDKDQ LVMLLDQINS TFVRSNPSVL QGLLRIIPYL
     SFGEVEKMQI LVERFKPYCS FEKYDEDHSG DDKVFLDCFC KIAAGIKNNS NGHQLKDLIL
     QKGITQNALD YMKKHIPSAK NLDADIWKKF LSRPALPFIL RLLRGLAMQH PATQVLIGTD
     SITSLHKLEQ VSSDEGIGTL AENLLEALRE HPDVNKKIDA ARRETRAEKK RMAMAMRQKA
     LGTLGMTTNE KGQVVTKTAL LKQMEELIEE PGLTCCICRE GYKFQPTKVL GIYTFTKRVA
     LEEMENKPRK QQGYSTVSHF NIVHYDCHLA AVRLARGREE WESAALQNAN TKCNGLLPVW
     GPHVPESAFA TCLARHNTYL QECTGQREPT YQLNIHDIKL LFLRFAMEQS FSADTGGGGR
     ESNIHLIPYI IHTVLYVLNT TRATSREEKN LQGFLEQPKE KWTESAFDVD GPHYFTILAL
     HVLPPEQWKA IRVEILRRLL VASHARAVAP GGATRLTDKA VKDYSAYRSS LLFWALVDLI
     YNMFKKVPTS NTEGGWSCSL AEYIRHNDMP IYEAADKALK TFQEEFMPVE TFSEFLDAAG
     LLSEITDPES FLKDLLNSVP
//
ID   A2AN33_MOUSE            Unreviewed;      1558 AA.
AC   A2AN33;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 23.
DE   SubName: Full=Novel protein (5830434P21Rik);
DE   Flags: Fragment;
GN   Name=Prrc2b; Synonyms=Bat2l; ORFNames=RP23-161B9.1-003;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Dunn M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL808027; CAM15835.1; -; Genomic_DNA.
DR   IPI; IPI00754134; -.
DR   UniGene; Mm.25504; -.
DR   PRIDE; A2AN33; -.
DR   Ensembl; ENSMUST00000069817; ENSMUSP00000064892; ENSMUSG00000039262.
DR   Ensembl; ENSMUST00000137551; ENSMUSP00000114656; ENSMUSG00000039262.
DR   MGI; MGI:1923304; Prrc2b.
DR   HOGENOM; HBG715582; -.
DR   InParanoid; A2AN33; -.
DR   Bgee; A2AN33; -.
DR   Genevestigator; A2AN33; -.
PE   4: Predicted;
FT   NON_TER       1      1
SQ   SEQUENCE   1558 AA;  169049 MW;  86C35F1A221A4E60 CRC64;
     PQRTFYPHHP QMLGFDPRWM MMPSYMDPRI TPTRTPVDFY PSALHPSGLM KPMMPQESLS
     GTGCRSEDQN CVPSLQERKV TALDPAPVWS PEGYMALQNK GYSLPHPKSA DTLAMGMHVR
     NERSYCASPG RPGGISAQRD LFEERGEEFL SAFDKKAQAD FDSCISSQRI GQELLFPPQE
     NVQEVGAPGG CTPNLRCSPL EPDFVPAEKK PEYGSWDVGH QPKAADTANG VELEAPRQEP
     SFHVSSWEKE GSPKKQPNPE PEWTPEPRSS SGQHQEQPGR TRRSGPIKKP VLKALKVEEK
     EKALERGRQG LREESSQRAP EKEPVGRAEE DEENNPALAN ASSALEDKAA SRAGFAHEAS
     KLDEDEKADK TWESRPSREA SDIPPTKRNN WIFIDEEQAF GGRGQARSRG RGFREFTFRG
     GRPAGSSTSG LCGTGVLGSR GMYSSGQRSN RGRGLRDFPP PEDCPRAKPR RRIASETHSE
     GSEYEELPKR RRQRGSEHSH EGMLTERDEG ALKDSWRSNR TYTEDQGGID TRSRGSRTCG
     RALPPRLSNC SYGRRTFVAK EPPHWQSRSP GSSWQEYGSS DPCGPRRGTD RDYIPDSYRQ
     SDTFGSRLFE DSRTEDKRSF FQDDHGADSE NAENRPFRRR RPPRQDKPPR FRRLRQERES
     LGLWGPEEES HLLASQWPGR SKLCPGDKSG PGGHRSPELS YQNSSDHANE EWETASESSD
     FSERRERREG LVAEPEAQGD GGLSGSSLGE KKELAKRSFS SQRPLADRQS RKLEPGGFGE
     KPVRPGGGEP SPRCESQQSG TPLKVKRSPD EALPGGLGSH SPYALERTTH ASSDGPETPS
     KKSEREVSLP TQRASEQEEA RKQFDLGYGN ALIDNCASSP GEENEASSVV GEGFIEVLTK
     KQRRLLEEER RKKEQAAQVP VKGRGLSSRI PPRFAKKQNG LCLEQDVTVP GSSLGTEIWE
     NSSQALPVQG AASDSWRTAV TAFSSTEPGT SEGFKSSQGD SGVDLSAESR ESSATSSQRS
     SPYGTLKPEE ISGPGLAESK ADSHKDQAQK QAEHKDSEQG SAQSKEHRPG PIGNERSLKN
     RKGSEGAERL PGAVVPPVNG VEIHVDSVLP VPPIEFGVSP KDSDFSLPPG SVSGPVGNPV
     AKLQDVLASN AGLTQSIPIL RRDHHMQRAI GLSPMSFPTA DLTLKMESAR KAWENSPSLP
     EQSSPGGAGS GIQPPSSVGA SNGVNYSSFG GVSMPPMPVA SVAPSASIPG SHLPPLYLDG
     HVFASQPRLV PQTIPQQQSY QQAATAQQIP ISLHTSLQAQ AQLGLRGGLP VSQSQEIFSS
     LQPFRSQVYM HPSLSPPSTM ILSGGTALKP PYSAFPGIQP LEMVKPQSGS PYQPMSGNQA
     LVYEGQLGQA AGLGTSQMLD SQLPQLTMPL PRYGSGQQPL ILPQSIQLPP GQSLSVGAPR
     RVPPPGSQPP VLNTSRESAP MELKGFHFAD SKQNVPTGGS APSPQAYRPS SASPSGKPSG
     SAVNMGSVQG HYVQQAKRVD EKPGLGTVKL QEASSATSQM KRTGAIKPRA VKVEGSKA
//
ID   A2ANP1_MOUSE            Unreviewed;       168 AA.
AC   A2ANP1;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   30-NOV-2010, entry version 24.
DE   SubName: Full=2310028H24Rik protein;
DE   SubName: Full=Likely ortholog of H. sapiens chromosome 9 open reading frame 25 (C9orf25);
DE   SubName: Full=MCG9749, isoform CRA_a;
GN   Name=2310028H24Rik; ORFNames=RP23-100C7.5-003, mCG_9749;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Collins J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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DR   EMBL; BC147808; AAI47809.1; -; mRNA.
DR   EMBL; BC147810; AAI47811.1; -; mRNA.
DR   EMBL; BC147834; AAI47835.1; -; mRNA.
DR   EMBL; BC147836; AAI47837.1; -; mRNA.
DR   EMBL; AL831723; CAM13280.1; -; Genomic_DNA.
DR   EMBL; CH466538; EDL05396.1; -; Genomic_DNA.
DR   IPI; IPI00650017; -.
DR   RefSeq; NP_001153055.1; NM_001159583.1.
DR   UniGene; Mm.39215; -.
DR   Ensembl; ENSMUST00000108052; ENSMUSP00000103687; ENSMUSG00000028439.
DR   GeneID; 71901; -.
DR   KEGG; mmu:71901; -.
DR   MGI; MGI:1919151; 2310028H24Rik.
DR   eggNOG; roNOG17024; -.
DR   HOGENOM; HBG507176; -.
DR   HOVERGEN; HBG054822; -.
DR   InParanoid; A2ANP1; -.
DR   OMA; CDTREGE; -.
DR   Bgee; A2ANP1; -.
DR   Genevestigator; A2ANP1; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   168 AA;  18656 MW;  11F73B10DAD037EB CRC64;
     MMEEIDRFQV PTAHSEMQPL DPAAASISDR DCDAREEKQR ELARKGSLKN GSMGSPVNQQ
     PKKNNVMART RLVVPNKGYS SLDQSPDEKP LVALDTDSDD DFDMSRYSSS GYSSAEQINQ
     DLNIQLLKDG YRLDEIPDDE DLDLIPPKSV NPTCMCCQAT SSTACHIQ
//
ID   TM90B_MOUSE             Reviewed;         258 AA.
AC   A2ANU3;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 35.
DE   RecName: Full=Transmembrane protein 90B;
DE   AltName: Full=Synapse differentiation-induced protein 1;
DE            Short=SynDIG1;
GN   Name=Tmem90b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=12408845; DOI=10.1016/S0896-6273(02)01016-4;
RA   Diaz E., Ge Y., Yang Y.H., Loh K.C., Serafini T.A., Okazaki Y.,
RA   Hayashizaki Y., Speed T.P., Ngai J., Scheiffele P.;
RT   "Molecular analysis of gene expression in the developing
RT   pontocerebellar projection system.";
RL   Neuron 36:417-434(2002).
RN   [5]
RP   TOPOLOGY, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND INTERACTION WITH GRIA1 AND GRIA2.
RX   PubMed=20152115; DOI=10.1016/j.neuron.2009.12.021;
RA   Kalashnikova E., Lorca R.A., Kaur I., Barisone G.A., Li B.,
RA   Ishimaru T., Trimmer J.S., Mohapatra D.P., Diaz E.;
RT   "SynDIG1: an activity-regulated, AMPA- receptor-interacting
RT   transmembrane protein that regulates excitatory synapse development.";
RL   Neuron 65:80-93(2010).
CC   -!- FUNCTION: May regulate AMPA receptor content at nascent synapses,
CC       and have a role in postsynaptic development and maturation (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer. Interacts with GRIA1 and GRIA2.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC       Early endosome membrane; Single-pass membrane protein.
CC       Note=Shuttles between the cell surface and early endosome
CC       membrane.
CC   -!- TISSUE SPECIFICITY: Brain-specific. Expressed in Purkinje neurons
CC       in cerebellum. Also detected in the hippocampus. Found at
CC       excitatory synapses and postsynaptic cells.
CC   -!- DEVELOPMENTAL STAGE: Expressed during synaptogenesis. Found at the
CC       cell surface of excitatory synapses.
CC   -!- SIMILARITY: Belongs to the capucin family.
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DR   EMBL; AL831742; CAM13941.1; -; Genomic_DNA.
DR   EMBL; AL845436; CAM13941.1; JOINED; Genomic_DNA.
DR   EMBL; AL845436; CAM20081.1; -; Genomic_DNA.
DR   EMBL; AL831742; CAM20081.1; JOINED; Genomic_DNA.
DR   EMBL; CH466519; EDL28557.1; -; Genomic_DNA.
DR   EMBL; BC147352; AAI47353.1; -; mRNA.
DR   EMBL; BC147353; AAI47354.1; -; mRNA.
DR   EMBL; BC147660; AAI47661.1; -; mRNA.
DR   EMBL; BC147661; AAI47662.1; -; mRNA.
DR   IPI; IPI00457710; -.
DR   RefSeq; NP_001078990.1; NM_001085521.2.
DR   UniGene; Mm.330649; -.
DR   ProteinModelPortal; A2ANU3; -.
DR   PRIDE; A2ANU3; -.
DR   Ensembl; ENSMUST00000099263; ENSMUSP00000096869; ENSMUSG00000074736.
DR   Ensembl; ENSMUST00000109934; ENSMUSP00000105560; ENSMUSG00000074736.
DR   Ensembl; ENSMUST00000109935; ENSMUSP00000105561; ENSMUSG00000074736.
DR   GeneID; 433485; -.
DR   KEGG; mmu:433485; -.
DR   CTD; 433485; -.
DR   MGI; MGI:3702158; Tmem90b.
DR   eggNOG; roNOG12107; -.
DR   HOGENOM; HBG444108; -.
DR   HOVERGEN; HBG051163; -.
DR   InParanoid; A2ANU3; -.
DR   OMA; NFMAESR; -.
DR   OrthoDB; EOG4H464K; -.
DR   NextBio; 408730; -.
DR   Bgee; A2ANU3; -.
DR   Genevestigator; A2ANU3; -.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009607; P:response to biotic stimulus; IEA:InterPro.
DR   InterPro; IPR007593; Interferon-induced_TM_protein.
DR   Pfam; PF04505; CD225; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Endosome; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    258       Transmembrane protein 90B.
FT                                /FTId=PRO_0000394033.
FT   TOPO_DOM      1    181       Cytoplasmic (Potential).
FT   TRANSMEM    182    202       Helical; (Potential).
FT   TOPO_DOM    203    228       Extracellular (Potential).
FT   INTRAMEM    229    249       Helical; (Potential).
FT   TOPO_DOM    250    258       Extracellular (Potential).
FT   COMPBIAS    151    155       Poly-Glu.
SQ   SEQUENCE   258 AA;  28456 MW;  90580C01DD5C1267 CRC64;
     MDGIIEQKSV LVHSKISDAG KRNGLINTRN FMAESRDGLV SVYPAPQYQS HRLVASAAPG
     SLEGGRSEPV QQLLDPNTLQ QSVESHYRPN IILYSDGVLR SWGDGVATDC CETTFIEDRS
     PTKDSLEYPD GKFIDLSGDD IKIHTLSYDV EEEEELQELE SDYSSDTESE DNFLMMPPRD
     HLGLSVFSML CCFWPLGIAA FYLSHETNKA VAKGDFHQAS TSSRRALFLA VLSITIGTGI
     YVGVAVALIA YLSKNNHL
//
ID   A2AP20_MOUSE            Unreviewed;      1237 AA.
AC   A2AP20;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   SubName: Full=Phospholipase C, eta 2;
DE   Flags: Fragment;
GN   Name=Plch2; ORFNames=RP24-89N4.4-003;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Wallis J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Howden P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 PI-PLC X-box domain.
CC   -!- SIMILARITY: Contains 1 PI-PLC Y-box domain.
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DR   EMBL; AL831788; CAM16346.2; -; Genomic_DNA.
DR   EMBL; BX004788; CAM16346.2; JOINED; Genomic_DNA.
DR   EMBL; BX004788; CAM28039.2; -; Genomic_DNA.
DR   EMBL; AL831788; CAM28039.2; JOINED; Genomic_DNA.
DR   IPI; IPI00857083; -.
DR   RefSeq; NP_780765.2; NM_175556.4.
DR   UniGene; Mm.379458; -.
DR   Ensembl; ENSMUST00000105630; ENSMUSP00000101255; ENSMUSG00000029055.
DR   Ensembl; ENSMUST00000139976; ENSMUSP00000122704; ENSMUSG00000029055.
DR   GeneID; 269615; -.
DR   KEGG; mmu:269615; -.
DR   CTD; 269615; -.
DR   MGI; MGI:2443078; Plch2.
DR   GeneTree; ENSGT00600000084266; -.
DR   HOVERGEN; HBG107104; -.
DR   OMA; TEVASSW; -.
DR   OrthoDB; EOG41RPT8; -.
DR   NextBio; 392931; -.
DR   Bgee; A2AP20; -.
DR   Genevestigator; A2AP20; -.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:InterPro.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0030384; ?:?; IDA:MGI.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR015359; Phospholipase_C_EF-hand-like.
DR   InterPro; IPR001711; Phospholipase_C_Pinositol-sp_Y.
DR   InterPro; IPR001192; Pinositol_Phospholipase-C.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:3.20.20.190; PLC-like_Pdiesterase_TIM-brl; 2.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF09279; efhand_like; 1.
DR   Pfam; PF00388; PI-PLC-X; 1.
DR   Pfam; PF00387; PI-PLC-Y; 1.
DR   PRINTS; PR00390; PHPHLIPASEC.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00148; PLCXc; 1.
DR   SMART; SM00149; PLCYc; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF51695; PLC-like_Pdiesterase_TIM-brl; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   4: Predicted;
KW   Calcium; Transducer.
FT   NON_TER       1      1
SQ   SEQUENCE   1237 AA;  136162 MW;  63E2D82818D1166C CRC64;
     GGLAWGPSRA AGSSWVNASG TWEQPLRGFS GLQGGRRRGR GEKGIPEEPL CQLTPQLGLS
     LRVPFGLGDY GLDMPGPQPS AASQTTGAVA CLAEVLLWVG GSVVVSPRWQ LSLVVERCMS
     AMQEGTQMVK LRGSSKGLVR FYYLDEHRSC LRWRPSRKNE KAKISIDSIQ EVSEGRQSEI
     FQRYPDSSFD PNCCFSIYHG SHRESLDLVS PSSEEARTWV TGLRYLMAGI SDEDSLARRQ
     RTRDQWLKQT FDEADKNGDG SLSISEVLQL LHKLNVNLPR QRVKQMFREA DTDDHQGTLG
     FEEFCAFYKM MSTRRDLYLL MLTYSNHKDH LDASDLQRFL EVEQKMNGVT LESCQNIIEQ
     FEPCLENKSK GMLGIDGFTN YTRSPAGDIF NPEHNRVHQD MTQPLSHYFI TSSHNTYLVG
     DQLMSQSRVD MYAWVLQAGC RCVEVDCWDG PDGEPIVHHG YTLTSKILFK DVIETINKYA
     FIKNEYPVIL SIENHCSVVQ QKKMAQYLTD ILGDKLDLSS VSSEDATMLP SPQMLKGKIL
     VKGKKLPANI SEDAEEGEVS DEDSADEMED DCKLLNGDAS TNRKRVENIA KKKLDSLIKE
     SKIRDCEDPN DFSVSTLSPS GKLGRKAEAK KGQSKVEEDV EAGEDSGVSR QNSRLFMSSF
     SKRKKKGSKI KKVASVEEGD ETLDSPGSQS RGTARQKKTM KLSRALSDLV KYTKSVGTHD
     VEIEVVSSWQ VSSFSETKAH QILQQKPTQY LRFNQHQLSR IYPSSYRVDS SNYNPQPFWN
     AGCQMVALNY QSEGRMLQLN RAKFSANGDC GYVLKPQCMC QGVFNPNSED PLPGQLKKQL
     ALRIISGQQL PKPRDSVLGD RGEIIDPFVE VEVIGLPVDC SKEQTRVVDD NGFNPMWEET
     LVFTVHMPEI ALVRFLVWDH DPIGRDFIGQ RTLAFSSIMP GYRHVYLEGM EEASIFVHVA
     VSDISGKVKQ TLGLKGLFLR GTKPGSLDSH AAGQPLPRPS VSQRLLRRTA SAPTKSQKPS
     RKGFPELALG TQDAGSEGAA DDVAPSSPNP ALEAPTQERS GSSSPRGKAP GGEATEERTL
     AQVRSPNAPE GPGPAGMAAT CMKCVVGSCA GMDVEGLQRE QQPSPGPAGS HMAISHQPRA
     RVDSLGGPCC SPSPRATPGR SKEAPKGPRA RRQGPGGGSV SSDSSSPDSP GSPKVAPCQP
     EGAHRQQGAL QGEMNALFVQ KLEEIRSHSP MFSTVRD
//
ID   A2API6_MOUSE            Unreviewed;       797 AA.
AC   A2API6;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   SubName: Full=Low density lipoprotein-related protein 1B (Deleted in tumors);
DE   Flags: Fragment;
GN   Name=Lrp1b; ORFNames=RP23-151M8.2-002;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Tracey A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL840626; CAM15517.1; -; Genomic_DNA.
DR   IPI; IPI00652062; -.
DR   UniGene; Mm.441398; -.
DR   UniGene; Mm.477142; -.
DR   STRING; A2API6; -.
DR   Ensembl; ENSMUST00000142546; ENSMUSP00000117212; ENSMUSG00000049252.
DR   MGI; MGI:2151136; Lrp1b.
DR   eggNOG; roNOG14586; -.
DR   InParanoid; A2API6; -.
DR   Bgee; A2API6; -.
DR   Genevestigator; A2API6; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005041; F:low-density lipoprotein receptor activity; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR006209; EGF.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR001881; EGF_Ca-bd.
DR   InterPro; IPR013091; EGF_Ca-bd_2.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   Gene3D; G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 1.
DR   Gene3D; G3DSA:4.10.400.10; LDL_rcpt_classA_cys-rich; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   Pfam; PF00058; Ldl_recept_b; 1.
DR   SMART; SM00181; EGF; 7.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00192; LDLa; 1.
DR   SMART; SM00135; LY; 3.
DR   SUPFAM; SSF57184; Grow_fac_recept; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 5.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 7.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
DR   PROSITE; PS51120; LDLRB; 5.
PE   4: Predicted;
KW   EGF-like domain; Lipoprotein; Membrane; Repeat; Transmembrane;
KW   Transmembrane helix.
FT   NON_TER       1      1
SQ   SEQUENCE   797 AA;  88442 MW;  24A7EED6B1080437 CRC64;
     SNRNCIPMEL QCDSLDDCGD GSDEQGCLKT PIEHTCENNG NPCGDDAYCN QIKTSVFCRC
     KPGFQRNMKG RECADLNECL LFGICSHHCL NTRGSYKCVC DQNFQEKNNS CIAKGSEDQA
     LYIANDTDIL GFVYPFNYSG GHQQISHVEH NSRITGMDVH YQRNVIVWST QFNPGGIFYK
     MIDAREKRQA NSGLICPEFK RPRDIAVDWV AGNVYWTDHS RMHWFSYYTT HWTSLRYSIN
     VGQLNGPNCT RLLTNMAGEP YAIAVNPKRG MMYWTVIGDH SHIEEAAMDG TLRRVLVQKN
     LQRPTGLTVD HFGERIYWAD FELSIIGSVL YDGSSPVVSV SSKQGLLHPH RIDVFEDYIY
     GAGPKNGIFR VQKFGHGSVE VLALGVDKTK SILVSHRYKQ LNLPNPCLDL SCDFLCLLNP
     SGATCICPEG KYMMNGTCHD DSLLDDSCKL TCENGGRCIL NEKGDLRCHC WPSYSGGRCE
     VNHCSNYCQN GGTCIPSTLG RPTCICALGF TGPNCGKAVC EDSCHNGGSC VVTAGNQPYC
     HCQADYTGDR CQYYVCHHYC VNSESCTIGN DGSVECVCPT RYEGPKCEID KCVRCHGGHC
     IINKDNEDIF CNCTNGKIAS SCQLCDGYCY NGGTCQLDPE TSIPVCVCST NWSGTQCERP
     APKSSKSEHI STRSIAIIVP LVLLVTLVTT LVIGLVVCKR KRRTKTIRRQ PIINGGINVE
     IGNPSYNMYE VDHDHSDGGL LEPSFMIDPV KPTNYSNPVY AKLYMDGQNC RNSLASVDER
     KELLPKKIEI GIRETVA
//
ID   A2APJ0_MOUSE            Unreviewed;      1136 AA.
AC   A2APJ0;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   08-MAR-2011, entry version 27.
DE   SubName: Full=Palm2-Akap2 fusion protein;
DE   Flags: Fragment;
GN   Name=Palm2; Synonyms=Akap2, Palm2-Akap2; ORFNames=RP23-334A5.2-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Matthews N.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL840629; CAM21288.1; -; Genomic_DNA.
DR   EMBL; AL772312; CAM21288.1; JOINED; Genomic_DNA.
DR   UniGene; Mm.440076; -.
DR   STRING; A2APJ0; -.
DR   Ensembl; ENSMUST00000030049; ENSMUSP00000030049; ENSMUSG00000038729.
DR   Ensembl; ENSMUST00000150412; ENSMUSP00000117466; ENSMUSG00000089945.
DR   HOGENOM; HBG715482; -.
DR   HOVERGEN; HBG050477; -.
DR   InParanoid; A2APJ0; -.
DR   OMA; QYCVRKV; -.
DR   OrthoDB; EOG4MCWZX; -.
DR   Bgee; A2APJ0; -.
DR   Genevestigator; A2APJ0; -.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:InterPro.
DR   InterPro; IPR004965; Paralemmin.
DR   InterPro; IPR018459; RII_binding_1.
DR   Pfam; PF03285; Paralemmin; 1.
DR   Pfam; PF10522; RII_binding_1; 1.
PE   4: Predicted;
FT   NON_TER       1      1
SQ   SEQUENCE   1136 AA;  125977 MW;  C27F307F126AA0C8 CRC64;
     FAQPLWKCLH RCGPFPLPLL AFRFLEPTPT HSDSLSLSLS LSLSLSLSLS LSLSPLSLHF
     FKEKRKRQTE IEGKRRQLDE QVLLLQHSKS KVLREKWLLQ GVPAGTAEEE EARRRQSEED
     EFKVKQLEDN IQRLEQEIQA LESEESQISA KEQIILEKLK ETEKSFKDLQ KSFSTADGAS
     GWSTVLLQGD ELTADPIGTN ADMAIQKPPQ LSEDANQLRS KQDNCGDSRL EPAASSLSPD
     HKNMEIGVSV AECKSVPGVT STPHSKDHSS PFYSPSHNGL LADHHESLDN DVAREIQYLD
     EVLEANCCDS SVDGTYNGIS SPEPGAAILV SSLGSPAHSV TEAEPTEKAS GRQVPPHIEL
     SRSPSDRMAE GERANGHSTD QPQDLLGNSL QAPASPSSST SSHCSSRDGE FTLTTLKKEA
     KFELRAFHED KKPSKLFEED EREKEQFCVR KVRPSEEMIE LEKERRELIR SQAVKKNPGI
     AAKWWNPPQE KTIEEQLDEE HLESHRKYKE RKEKRAQQEQ LQLQQQQQQQ LQQQQLQQQQ
     LQQQQLQQQL QQQQLSTSQP CTAPAAHKHL DGIEHTKEDV VTEQIDFSAA RKQFQLMENS
     RQTLAKGQST PRLFSIKPYY KPLGSIHSDK PPTILRPATV GGTLEDGGTQ AAKEQKAPCV
     SESQSAGAGP ANAATQGKEG PYSEPSKRGP LSKLWAEDGE FTSARAVLTV VKDEDHGILD
     QFSRSVNVSL TQEELDSGLD ELSVRSQDTT VLETLSNDFS MDNISDSGAS NETPSALQEN
     SLADFSLPQT PQTDNPSEGR EGVSKSFSDH GFYSPSSTLG DSPSVDDPLE YQAGLLVQNA
     IQQAIAEQVD KAEAHTSKEG SEQQEPEATV EEAGSQTPGS EKPQGMFAPP QVSSPVQEKR
     DILPKNLPAE DRALREKGPS QPPTAAQPSG PVNMEETRPE GGYFSKYSEA AELRSTASLL
     ATQESDVMVG PFKLRSRKQR TLSMIEEEIR AAQEREEELK RQRQVRQSTP SPRAKNAPSL
     PSRTTCYKTA PGKIEKVKPP PSPTTEGPSL QPDLAPEEAA GTQRPKNLMQ TLMEDYETHK
     SKRRERMDDS SYTSKLLSCK VTSEVLEATR VNRRKSALAL RWEAGIYANQ EEEDNE
//
ID   KLD7A_MOUSE             Reviewed;         773 AA.
AC   A2APT9; Q80SV4; Q8C706;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 3.
DT   08-MAR-2011, entry version 30.
DE   RecName: Full=Kelch domain-containing protein 7A;
GN   Name=Klhdc7a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-759.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 358-773.
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Contains 5 Kelch repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC35129.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAC35129.1; Type=Frameshift; Positions=658;
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DR   EMBL; AL844480; CAM17006.1; -; Genomic_DNA.
DR   EMBL; AK052747; BAC35129.1; ALT_SEQ; mRNA.
DR   EMBL; BC043462; AAH43462.1; -; mRNA.
DR   EMBL; BC043672; AAH43672.1; -; mRNA.
DR   IPI; IPI00466814; -.
DR   RefSeq; NP_775603.2; NM_173427.2.
DR   UniGene; Mm.60400; -.
DR   ProteinModelPortal; A2APT9; -.
DR   SMR; A2APT9; 499-718.
DR   PhosphoSite; A2APT9; -.
DR   PRIDE; A2APT9; -.
DR   Ensembl; ENSMUST00000105031; ENSMUSP00000100648; ENSMUSG00000078234.
DR   GeneID; 242721; -.
DR   KEGG; mmu:242721; -.
DR   CTD; 242721; -.
DR   MGI; MGI:2444612; Klhdc7a.
DR   GeneTree; ENSGT00560000077013; -.
DR   HOGENOM; HBG403048; -.
DR   HOVERGEN; HBG095597; -.
DR   InParanoid; A2APT9; -.
DR   OMA; YECATYR; -.
DR   OrthoDB; EOG4M65H1; -.
DR   Bgee; A2APT9; -.
DR   CleanEx; MM_KLHDC7A; -.
DR   Genevestigator; A2APT9; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   Gene3D; G3DSA:2.120.10.80; Kelch-typ_b-propeller; 1.
DR   Pfam; PF01344; Kelch_1; 2.
DR   SMART; SM00612; Kelch; 2.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Kelch repeat; Membrane; Phosphoprotein; Repeat;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    773       Kelch domain-containing protein 7A.
FT                                /FTId=PRO_0000285086.
FT   TRANSMEM     23     40       Helical; (Potential).
FT   REPEAT      323    370       Kelch 1.
FT   REPEAT      488    534       Kelch 2.
FT   REPEAT      537    585       Kelch 3.
FT   REPEAT      586    628       Kelch 4.
FT   REPEAT      631    673       Kelch 5.
FT   COMPBIAS     81     86       Poly-Arg.
FT   MOD_RES     289    289       Phosphotyrosine (By similarity).
FT   CARBOHYD     61     61       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    256    256       N-linked (GlcNAc...) (Potential).
FT   CONFLICT     14     14       H -> I (in Ref. 2; BAC35129).
FT   CONFLICT    513    513       A -> V (in Ref. 2; BAC35129).
SQ   SEQUENCE   773 AA;  83590 MW;  200329BF358AB065 CRC64;
     MLPTGEGAEG QDWHLDMQLP SKVVLSAAAL LLVTAAYKLY KSRPAPVGQA GRNNKDHKAE
     NETEALGQLA FQEAPPGTLP RGRRRRKASK GAGTSLDYSL VDPEDPCILD ISRSEEATRK
     GSDESQGRQC PDSQQVPPPC GGQEAGTDVR GKPNPPHLPH SGCEPTSSSG RLIPGVGGSC
     VGDKLSPWPD SRPPEETGSG DLEAPNGWTD LTLVNGDMNQ SWIFTHMTGV SRGEAGVLQA
     AADMGLATQQ QEGATNASHT FSSVARIRME ENIIQKAEGP GLKGRVYDYF VESTSKADSR
     PVPCPAALAD APSPGPGPEP LVTGAASRDE AANTAGGGAS EAASPQPVAS PSAPGFSRKV
     SLLQIAENPE LQLQPEGFRM PLPAHLDQRA QLSSACSHGE PHVQLVAGTN FFHIPLTPAS
     ALDVRLDLGN CYEMLTLAKR QGLETLKEAA YKVLSDNYLQ VLRSPDIYGG LSGAERELIL
     QRRFRGHKRL VVADMCPQDD SGRLCCYDNV QDAWHPLAQL PPEAMSRGCA LCTLFNYLFV
     VSGCQEPGGQ PSNRVFCYNP LTAIWSEVCP LNQARPHCRL VALEGHLYAI GGECLNTVER
     YDPRLDRWTF APPLPNDTFA LAHTATVCAN EIFVTGGSLR YLLLRFSTQE QRWWAGPTGG
     SKDRTAEMVA VNGFLYRFDL NRSLGISVYR CSASTRLWYE CATYRLPYPD AFQCAVVDDH
     IYCVGRRRML CFLADHISPR FVSKELKGFP SARGTLLPAV LTLPVPDVPQ TPV
//
ID   FMNL2_MOUSE             Reviewed;        1086 AA.
AC   A2APV2; A2AQW1; Q69Z73; Q7TPA8; Q80VH6;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 38.
DE   RecName: Full=Formin-like protein 2;
DE   AltName: Full=Protein Man;
GN   Name=Fmnl2; Synonyms=Kiaa1902, Man;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
RP   SPLICING (ISOFORM 3).
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 409-1082 (ISOFORM 2).
RC   STRAIN=CD-1; TISSUE=Limb;
RA   Cui Y., Harland R.M.;
RT   "Cloning of Man, a formin homology domain containing gene, and its
RT   expression in the mouse limb.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 614-1086 (ISOFORM 1).
RC   STRAIN=129; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 794-1086 (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=A2APV2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2APV2-2; Sequence=VSP_025888, VSP_025890, VSP_025891;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=A2APV2-3; Sequence=VSP_025889;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the formin homology family.
CC   -!- SIMILARITY: Contains 1 DAD (diaphanous autoregulatory) domain.
CC   -!- SIMILARITY: Contains 1 FH2 (formin homology 2) domain.
CC   -!- SIMILARITY: Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology
CC       3) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP87551.1; Type=Erroneous initiation;
CC       Sequence=CAM19613.1; Type=Erroneous gene model prediction;
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DR   EMBL; AL844859; CAM19034.1; -; Genomic_DNA.
DR   EMBL; AL844510; CAM19034.1; JOINED; Genomic_DNA.
DR   EMBL; AL845170; CAM19034.1; JOINED; Genomic_DNA.
DR   EMBL; AL845170; CAM19616.1; -; Genomic_DNA.
DR   EMBL; AL844510; CAM19616.1; JOINED; Genomic_DNA.
DR   EMBL; AL844859; CAM19616.1; JOINED; Genomic_DNA.
DR   EMBL; AL844510; CAM25963.1; -; Genomic_DNA.
DR   EMBL; AL844859; CAM25963.1; JOINED; Genomic_DNA.
DR   EMBL; AL845170; CAM25963.1; JOINED; Genomic_DNA.
DR   EMBL; AL845170; CAM19613.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF513716; AAP87551.1; ALT_INIT; mRNA.
DR   EMBL; BC048004; AAH48004.1; -; mRNA.
DR   EMBL; AK173293; BAD32571.1; -; mRNA.
DR   IPI; IPI00345373; -.
DR   IPI; IPI00403559; -.
DR   IPI; IPI00849114; -.
DR   RefSeq; NP_765997.2; NM_172409.2.
DR   UniGene; Mm.394427; -.
DR   ProteinModelPortal; A2APV2; -.
DR   SMR; A2APV2; 612-1005.
DR   STRING; A2APV2; -.
DR   PhosphoSite; A2APV2; -.
DR   PRIDE; A2APV2; -.
DR   Ensembl; ENSMUST00000049483; ENSMUSP00000047260; ENSMUSG00000036053.
DR   Ensembl; ENSMUST00000090952; ENSMUSP00000088472; ENSMUSG00000036053.
DR   GeneID; 71409; -.
DR   KEGG; mmu:71409; -.
DR   CTD; 71409; -.
DR   MGI; MGI:1918659; Fmnl2.
DR   HOVERGEN; HBG053118; -.
DR   OMA; DIAILPV; -.
DR   OrthoDB; EOG4N8R43; -.
DR   NextBio; 333723; -.
DR   Bgee; A2APV2; -.
DR   CleanEx; MM_FMNL2; -.
DR   Genevestigator; A2APV2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   InterPro; IPR003104; Actin-bd_FH2/DRF_autoreg.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR010472; Drf_FH3.
DR   InterPro; IPR010473; Drf_GTPase-bd.
DR   InterPro; IPR015425; FH2_actin-bd.
DR   InterPro; IPR014768; GTPase-bd/formin_homology_3.
DR   Pfam; PF06367; Drf_FH3; 1.
DR   Pfam; PF06371; Drf_GBD; 2.
DR   Pfam; PF02181; FH2; 1.
DR   SMART; SM00498; FH2; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF101447; FH2_actin_bd; 1.
DR   PROSITE; PS51231; DAD; FALSE_NEG.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Phosphoprotein.
FT   CHAIN         1   1086       Formin-like protein 2.
FT                                /FTId=PRO_0000289094.
FT   DOMAIN       23    469       GBD/FH3.
FT   DOMAIN      615   1006       FH2.
FT   DOMAIN     1038   1077       DAD.
FT   COMPBIAS    525    602       Pro-rich.
FT   MOD_RES     171    171       Phosphoserine (By similarity).
FT   MOD_RES    1015   1015       Phosphoserine (By similarity).
FT   VAR_SEQ     554    588       Missing (in isoform 2).
FT                                /FTId=VSP_025888.
FT   VAR_SEQ    1056   1086       ALKKNNITKFPNVHSRVRISSSTPVVEDTQS -> DLRNQP
FT                                YRRADAVRRSVRRRFDDQNLRSVNGAEITM (in
FT                                isoform 3).
FT                                /FTId=VSP_025889.
FT   VAR_SEQ    1056   1067       ALKKNNITKFPN -> VLETNPTDEPMR (in isoform
FT                                2).
FT                                /FTId=VSP_025890.
FT   VAR_SEQ    1068   1086       Missing (in isoform 2).
FT                                /FTId=VSP_025891.
FT   CONFLICT    557    591       Missing (in Ref. 2; AAP87551).
SQ   SEQUENCE   1086 AA;  123101 MW;  0E5BBC192FCF8ACA CRC64;
     MGNAGSMDSQ QTDFKAHNVP LKLPMPEPGE LEERFAIVLN AMNLPPDKAR LLRQYDNEKK
     WELICDQERF QVKNPPHTYI QKLKGYLDPA VTRKKFRRRV QESTQVLREL EISLRTNHIG
     WVREFLNEEN KGLDVLVEYL SFAQYAVTFD FESVESTMES TVDKSKPWSR SIEDLHRGSN
     LPSPVGNSVS RSGRHSALRY NTLPSRRTLK NSRLVSKKDD VHVCIMCLRA IMNYQYGFNM
     VMSHPHAVNE IALSLNNKNP RTKALVLELL AAVCLVRGGH EIILSAFDNF KEVCGEKQRF
     EKLMEHFRNE DNNIDFMVAS MQFINIVVHS VEDMNFRVHL QYEFTKLGLD EYLDKLKHTE
     SDKLQVQIQA YLDNVFDVGA LLEDAETKNA ALERVEELEE NISHLSEKLQ DTENEAMSKI
     VELEKQLMQR NKELDVVREI YKDANTQVHT LRKMVKEKEE AIQRQSTLEK KIHELEKQGT
     IKIQKKGDGD IAILPVMASG TLSTGSELAV GNYVGSVPGA TTSGPSVPPP PPLPPSSDTS
     EAAQNGTASP PMSPPPPPPP PPPPPPPPPP PLPGPAAETS PAPPLPPPPP PSAPPLPGTS
     SPTVVFNSGL AAVKIKKPIK TKFRMPVFNW VALKPNQING TVFNEIDDER ILEDLNVDEF
     EEIFKTKAQG PAIDLSSSKQ KITQKASSKV TLLEANRAKN LAITLRKAGK SADEICKAIH
     VFDLKTLPVD FVECLMRFLP TENEVKVLRL YERERKPLEN LSDEDRFMMQ FSKIERLLQK
     MTIMAFIGNF TESIQMLTPQ LHAIIAASVS IKSSQKLKKI LEIILALGNY MNSSKRGAVY
     GFKLQSLDLL LDTKSTDRKQ TLLHYISNVV KEKYQQVTLF YNELHYVEKA AAVSLENVLL
     DVKELQRGMD LTKREYTMHD HNTLLKEFLL HNEGKLKKLQ EDAKIAQDAF DDVVKYFGEN
     PKTTPPSVFF PVFVRFVKAY KQAEEENELR KKQEQALMEK LLEQEALMEQ QDAKSPSHKS
     KRQQQELIAE LRRRQVKDNR HVYEGKDGAI EDIITALKKN NITKFPNVHS RVRISSSTPV
     VEDTQS
//
ID   A2APX6_MOUSE            Unreviewed;      1998 AA.
AC   A2APX6;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 38.
DE   SubName: Full=Sodium channel voltage-gated type I alpha;
GN   Name=Scn1a; ORFNames=RP23-201O18.1-004;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Tromans A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the sodium channel family.
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DR   EMBL; AL844526; CAM17349.1; -; Genomic_DNA.
DR   IPI; IPI00661236; -.
DR   RefSeq; NP_061203.2; NM_018733.2.
DR   UniGene; Mm.439704; -.
DR   ProteinModelPortal; A2APX6; -.
DR   STRING; A2APX6; -.
DR   PRIDE; A2APX6; -.
DR   Ensembl; ENSMUST00000077489; ENSMUSP00000076697; ENSMUSG00000064329.
DR   GeneID; 20265; -.
DR   KEGG; mmu:20265; -.
DR   CTD; 20265; -.
DR   MGI; MGI:98246; Scn1a.
DR   HOVERGEN; HBG053100; -.
DR   NextBio; 297935; -.
DR   Bgee; A2APX6; -.
DR   Genevestigator; A2APX6; -.
DR   GO; GO:0043194; C:initial segment; IDA:MGI.
DR   GO; GO:0014704; C:intercalated disc; IDA:MGI.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0033268; C:node of Ranvier; IDA:MGI.
DR   GO; GO:0030315; C:T-tubule; IDA:MGI.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:InterPro.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; IMP:MGI.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0050884; P:neuromuscular process controlling posture; IMP:MGI.
DR   GO; GO:0019227; P:neuronal action potential propagation; IMP:MGI.
DR   GO; GO:0019228; P:regulation of action potential in neuron; IMP:MGI.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR008051; Na_channel_a1su.
DR   InterPro; IPR001696; Na_channel_asu.
DR   InterPro; IPR010526; Na_trans_assoc.
DR   Pfam; PF00520; Ion_trans; 4.
DR   Pfam; PF06512; Na_trans_assoc; 1.
DR   PRINTS; PR00170; NACHANNEL.
DR   PRINTS; PR01664; NACHANNEL1.
DR   SMART; SM00015; IQ; 1.
PE   3: Inferred from homology;
KW   Ion transport; Ionic channel; Membrane; Sodium; Sodium channel;
KW   Sodium transport; Transmembrane; Transport; Voltage-gated channel.
SQ   SEQUENCE   1998 AA;  227617 MW;  32E3F58EDFE53787 CRC64;
     MEQTVLVPPG PDSFNFFTRE SLAAIERRIA EEKAKNPKPD KKDDDENGPK PNSDLEAGKN
     LPFIYGDIPP EMVSEPLEDL DPYYINKKTF IVLNKGKAIF RFSATSALYI LTPFNPLRKI
     AIKILVHSLF SMLIMCTILT NCVFMTMSNP PDWTKNVEYT FTGIYTFESL IKIIARGFCL
     EDFTFLRDPW NWLDFTVITF AYVTEFVDLG NVSALRTFRV LRALKTISVI PGLKTIVGAL
     IQSVKKLSDV MILTVFCLSV FALIGLQLFM GNLRNKCVQW PPTNASLEEH SIEKNITMDY
     NGTLVNETVF EFDWKSYIQD SRYHYFLEGV LDALLCGNSS DAGQCPEGYM CVKAGRNPNY
     GYTSFDTFSW AFLSLFRLMT QDFWENLYQL TLRAAGKTYM IFFVLVIFLG SFYLINLILA
     VVAMAYEEQN QATLEEAEQK EAEFQQMLEQ LKKQQEAAQQ AAATTASEHS REPSAAGRLS
     DSSSEASKLS SKSAKERRNR RKKRKQKEQS GGEEKDDDEF HKSESEDSIR RKGFRFSIEG
     NRLTYEKRYS SPHQSLLSIR GSLFSPRRNS RTSLFSFRGR AKDVGSENDF ADDEHSTFED
     NESRRDSLFV PRRHGERRNS NLSQTSRSSR MLAVFPANGK MHSTVDCNGV VSLVGGPSVP
     TSPVGQLLPE GTTTETEMRK RRSSSFHVSM DFLEDPSQRQ RAMSIASILT NTVEELEESR
     QKCPPCWYKF SNIFLIWDCS PYWLKVKHIV NLVVMDPFVD LAITICIVLN TLFMAMEHYP
     MTEHFNHVLT VGNLVFTGIF TAEMFLKIIA MDPYYYFQEG WNIFDGFIVT LSLVELGLAN
     VEGLSVLRSF RLLRVFKLAK SWPTLNMLIK IIGNSVGALG NLTLVLAIIV FIFAVVGMQL
     FGKSYKDCVC KIATDCKLPR WHMNDFFHSF LIVFRVLCGE WIETMWDCME VAGQAMCLTV
     FMMVMVIGNL VVLNLFLALL LSSFSADNLA ATDDDNEMNN LQIAVDRMHK GIAYVKRKIY
     EFIQQSFVKK QKILDEIKPL DDLNNRKDNC ISNHTTEIGK DLDCLKDVNG TTSGIGTGSS
     VEKYIIDESD YMSFINNPSL TVTVPIAVGE SDFENLNTED FSSESDLEES KEKLNESSSS
     SEGSTVDIGA PAEEQPVIEP EETLEPEACF TEGCVQRFKC CQISVEEGRG KQWWNLRRTC
     FRIVEHNWFE TFIVFMILLS SGALAFEDIY IDQRKTIKTM LEYADKVFTY IFILEMLLKW
     VAYGYQTYFT NAWCWLDFLI VDVSLVSLTA NALGYSELGA IKSLRTLRAL RPLRALSRFE
     GMRVVVNALL GAIPSIMNVL LVCLIFWLIF SIMGVNLFAG KFYHCVNTTT GDIFEISEVN
     NHSDCLKLIE RNETARWKNV KVNFDNVGFG YLSLLQVATF KGWMDIMYAA VDSRNVELQP
     KYEESLYMYL YFVIFIIFGS FFTLNLFIGV IIDNFNQQKK KFGGQDIFMT EEQKKYYNAM
     KKLGSKKPQK PIPRPGNKFQ GMVFDFVTRQ VFDISIMILI CLNMVTMMVE TDDQSDYVTS
     ILSRINLVFI VLFTGECVLK LISLRHYYFT IGWNIFDFVV VILSIVGMFL AELIEKYFVS
     PTLFRVIRLA RIGRILRLIK GAKGIRTLLF ALMMSLPALF NIGLLLFLVM FIYAIFGMSN
     FAYVKREVGI DDMFNFETFG NSMICLFQIT TSAGWDGLLA PILNSKPPDC DPNKVNPGSS
     VKGDCGNPSV GIFFFVSYII ISFLVVVNMY IAVILENFSV ATEESAEPLS EDDFEMFYEV
     WEKFDPDATQ FMEFEKLSQF AAALEPPLNL PQPNKLQLIA MDLPMVSGDR IHCLDILFAF
     TKRVLGESGE MDALRIQMEE RFMASNPSKV SYQPITTTLK RKQEEVSAVI IQRAYRRHLL
     KRTVKQASFT YNKNKLKGGA NLLVKEDMLI DRINENSITE KTDLTMSTAA CPPSYDRVTK
     PIVEKHEQEG KDEKAKGK
//
ID   SKT_MOUSE               Reviewed;        1946 AA.
AC   A2AQ25; A2AUE9; A2AUF0; A2AUF1; Q75UV8; Q75UV9; Q80VK2; Q8BHX8;
AC   Q8BHY1; Q8CHA8; Q8R0K6;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-FEB-2011, entry version 32.
DE   RecName: Full=Sickle tail protein;
DE   AltName: Full=Enhancer trap locus 4;
GN   Name=Skt; Synonyms=Etl4, Kiaa1217;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), FUNCTION, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=16204209; DOI=10.1534/genetics.105.048934;
RA   Semba K., Araki K., Li Z., Matsumoto K., Suzuki M., Nakagata N.,
RA   Takagi K., Takeya M., Yoshinobu K., Araki M., Imai K., Abe K.,
RA   Yamamura K.;
RT   "A novel murine gene, Sickle tail, linked to the Danforth's short tail
RT   locus, is required for normal development of the intervertebral
RT   disc.";
RL   Genetics 172:445-456(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 7 AND 9).
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Ovary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 874-1946 (ISOFORM 3).
RC   STRAIN=129/Sv X 129SvCp, and FVB/N;
RC   TISSUE=Colon, and Embryonic stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT SER-357, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452088; DOI=10.1074/mcp.T500040-MCP200;
RA   Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G.,
RA   Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F.,
RA   Maltby D.A., Schoepfer R., Burlingame A.L.;
RT   "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT   preparations using lectin weak affinity chromatography and mass
RT   spectrometry.";
RL   Mol. Cell. Proteomics 5:923-934(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-244 AND TYR-245, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1049; SER-1899 AND
RP   SER-1905, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-474; SER-1902 AND
RP   SER-1905, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359 AND SER-361, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Required for normal development of intervertebral disks.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=9;
CC       Name=1;
CC         IsoId=A2AQ25-1; Sequence=Displayed;
CC         Note=Gene prediction based on EST data;
CC       Name=2;
CC         IsoId=A2AQ25-2; Sequence=VSP_052416, VSP_052418;
CC         Note=Gene prediction based on EST data;
CC       Name=3; Synonyms=Skt-a;
CC         IsoId=A2AQ25-3; Sequence=VSP_052418, VSP_052421;
CC       Name=4; Synonyms=Skt-b;
CC         IsoId=A2AQ25-4; Sequence=VSP_052418, VSP_052420, VSP_052421;
CC       Name=5;
CC         IsoId=A2AQ25-5; Sequence=VSP_052416, VSP_052418, VSP_052424,
CC                                  VSP_052425, VSP_052426;
CC         Note=Gene prediction based on EST data;
CC       Name=6;
CC         IsoId=A2AQ25-6; Sequence=VSP_052416, VSP_052418, VSP_052421,
CC                                  VSP_052425, VSP_052426;
CC         Note=Gene prediction based on EST data;
CC       Name=7;
CC         IsoId=A2AQ25-7; Sequence=VSP_052417;
CC       Name=8;
CC         IsoId=A2AQ25-8; Sequence=VSP_052418, VSP_052419;
CC         Note=No experimental confirmation available;
CC       Name=9;
CC         IsoId=A2AQ25-9; Sequence=VSP_052416, VSP_052418, VSP_052420,
CC                                  VSP_052422, VSP_052423;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in the notochord and
CC       mesonephros during embryogenesis as well as in other areas such as
CC       the epithalamus sulcus, lens vesicle, inner retinal layer, heart,
CC       hepatic primordial surface, infundibulum, surface ectoderm, hind
CC       gut and limb bud mesenchyme. In adults, expressed in a range of
CC       tissues including the nucleus pulposus, corpus callosum, kidney,
CC       cardiac muscle, Sertoli cells and hair follicles.
CC   -!- DISRUPTION PHENOTYPE: Mice display a kinky-tail phenotype in about
CC       half of homozygotes with defects in the nucleus pulposus and
CC       annulus fibrosus of intertebral disks. Shortening and curving of
CC       caudal vertebrae 20-25 is apparent by the age of 2 weeks.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH26657.2; Type=Erroneous initiation;
CC       Sequence=BAC41473.2; Type=Erroneous initiation;
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DR   EMBL; AB125594; BAD14929.1; -; mRNA.
DR   EMBL; AB125595; BAD14930.1; -; mRNA.
DR   EMBL; AB093289; BAC41473.2; ALT_INIT; mRNA.
DR   EMBL; AK052733; BAC35121.1; -; mRNA.
DR   EMBL; AK054453; BAC35783.1; -; mRNA.
DR   EMBL; AL844538; CAM19813.1; -; Genomic_DNA.
DR   EMBL; AL929100; CAM19813.1; JOINED; Genomic_DNA.
DR   EMBL; AL844538; CAM19814.1; -; Genomic_DNA.
DR   EMBL; AL929100; CAM19814.1; JOINED; Genomic_DNA.
DR   EMBL; AL844538; CAM19815.1; -; Genomic_DNA.
DR   EMBL; AL929100; CAM19815.1; JOINED; Genomic_DNA.
DR   EMBL; AL929100; CAM24302.1; -; Genomic_DNA.
DR   EMBL; AL844538; CAM24302.1; JOINED; Genomic_DNA.
DR   EMBL; AL929100; CAM24303.1; -; Genomic_DNA.
DR   EMBL; AL844538; CAM24303.1; JOINED; Genomic_DNA.
DR   EMBL; AL929100; CAM24304.1; -; Genomic_DNA.
DR   EMBL; AL844538; CAM24304.1; JOINED; Genomic_DNA.
DR   EMBL; AL929100; CAM24306.1; -; Genomic_DNA.
DR   EMBL; AL929100; CAM24307.1; -; Genomic_DNA.
DR   EMBL; AL929100; CAM24308.1; -; Genomic_DNA.
DR   EMBL; BC026657; AAH26657.2; ALT_INIT; mRNA.
DR   EMBL; BC050016; AAH50016.1; -; mRNA.
DR   IPI; IPI00553590; -.
DR   IPI; IPI00752398; -.
DR   IPI; IPI00754456; -.
DR   IPI; IPI00754975; -.
DR   IPI; IPI00756087; -.
DR   IPI; IPI00849799; -.
DR   IPI; IPI00849959; -.
DR   IPI; IPI00851081; -.
DR   IPI; IPI00968353; -.
DR   RefSeq; NP_001074475.1; NM_001081006.1.
DR   RefSeq; NP_084171.2; NM_029895.4.
DR   RefSeq; NP_835160.2; NM_178059.5.
DR   UniGene; Mm.237935; -.
DR   STRING; A2AQ25; -.
DR   PhosphoSite; A2AQ25; -.
DR   PRIDE; A2AQ25; -.
DR   Ensembl; ENSMUST00000066509; ENSMUSP00000066170; ENSMUSG00000036617.
DR   Ensembl; ENSMUST00000114609; ENSMUSP00000110256; ENSMUSG00000036617.
DR   Ensembl; ENSMUST00000114619; ENSMUSP00000110266; ENSMUSG00000036617.
DR   Ensembl; ENSMUST00000114620; ENSMUSP00000110267; ENSMUSG00000036617.
DR   GeneID; 208618; -.
DR   KEGG; mmu:208618; -.
DR   CTD; 208618; -.
DR   MGI; MGI:95454; Etl4.
DR   eggNOG; roNOG09302; -.
DR   GeneTree; ENSGT00390000012399; -.
DR   HOVERGEN; HBG019587; -.
DR   Bgee; A2AQ25; -.
DR   CleanEx; MM_ETL4; -.
DR   Genevestigator; A2AQ25; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0048706; P:embryonic skeletal system development; IMP:UniProtKB.
DR   InterPro; IPR022782; AIP3_C.
DR   Pfam; PF03915; AIP3; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Developmental protein;
KW   Glycoprotein; Phosphoprotein.
FT   CHAIN         1   1946       Sickle tail protein.
FT                                /FTId=PRO_0000287898.
FT   COILED      557    581       Potential.
FT   COILED      644    685       Potential.
FT   COILED      962    990       Potential.
FT   COILED     1469   1495       Potential.
FT   COILED     1659   1688       Potential.
FT   COMPBIAS    298    364       Pro-rich.
FT   COMPBIAS   1050   1120       Pro-rich.
FT   COMPBIAS   1796   1908       Ser-rich.
FT   MOD_RES     244    244       Phosphotyrosine.
FT   MOD_RES     245    245       Phosphotyrosine.
FT   MOD_RES     359    359       Phosphoserine.
FT   MOD_RES     361    361       Phosphoserine.
FT   MOD_RES     393    393       Phosphotyrosine (By similarity).
FT   MOD_RES     474    474       Phosphoserine.
FT   MOD_RES     837    837       Phosphotyrosine (By similarity).
FT   MOD_RES    1049   1049       Phosphoserine.
FT   MOD_RES    1899   1899       Phosphoserine.
FT   MOD_RES    1902   1902       Phosphoserine.
FT   MOD_RES    1905   1905       Phosphoserine.
FT   CARBOHYD    357    357       O-linked (GlcNAc).
FT   VAR_SEQ       1    282       Missing (in isoform 2, isoform 5, isoform
FT                                6 and isoform 9).
FT                                /FTId=VSP_052416.
FT   VAR_SEQ     252   1946       Missing (in isoform 7).
FT                                /FTId=VSP_052417.
FT   VAR_SEQ     560    594       Missing (in isoform 2, isoform 3, isoform
FT                                4, isoform 5, isoform 6, isoform 8 and
FT                                isoform 9).
FT                                /FTId=VSP_052418.
FT   VAR_SEQ     885   1755       Missing (in isoform 8).
FT                                /FTId=VSP_052419.
FT   VAR_SEQ     961    971       Missing (in isoform 4 and isoform 9).
FT                                /FTId=VSP_052420.
FT   VAR_SEQ    1181   1739       Missing (in isoform 3, isoform 4 and
FT                                isoform 6).
FT                                /FTId=VSP_052421.
FT   VAR_SEQ    1181   1191       NLEFYHEDVRK -> VTCGSYTFTIQ (in isoform
FT                                9).
FT                                /FTId=VSP_052422.
FT   VAR_SEQ    1192   1946       Missing (in isoform 9).
FT                                /FTId=VSP_052423.
FT   VAR_SEQ    1207   1739       Missing (in isoform 5).
FT                                /FTId=VSP_052424.
FT   VAR_SEQ    1781   1784       ANGS -> VVLP (in isoform 5 and isoform
FT                                6).
FT                                /FTId=VSP_052425.
FT   VAR_SEQ    1785   1946       Missing (in isoform 5 and isoform 6).
FT                                /FTId=VSP_052426.
FT   CONFLICT     41     41       R -> H (in Ref. 5; AAH50016).
FT   CONFLICT    119    119       T -> R (in Ref. 2; BAC41473).
FT   CONFLICT    551    551       T -> A (in Ref. 2; BAC41473).
FT   CONFLICT    818    818       R -> Q (in Ref. 2; BAC41473).
SQ   SEQUENCE   1946 AA;  213037 MW;  E5D411BD044DC1CB CRC64;
     MEESEGQKCE PNLPPSGDSR QMPQQGRSNL HVTSQEDAAC RRPRERLSNG NARAQVSKPA
     RNIPRRHTLG GPRSSKEILG MQPSEMDRKR EAFLEHLKQK YPHHATAIMG HQERLRDQTK
     SPKLSHSPQP PNLGDPVEHL SETSGDSLEA MSEGEVPSPF ARGSRTRASL PVVRSANQTK
     ERSLGVLYLQ YGDETKQLRM PNEVTSTDTI RALFVSAFPQ QLTMKMLESP SVAIYIKDDS
     RNVYYELNDV RNIQDRSLLK VYNKDPSHAF NHMTKAVNGD MRMQREIVYA RGDGLVAPRP
     GSVAHPPHVI PNSPPSTPVP HSLPPSPSRI PYGGSRPMAI PGNATIPRDR LSSLPVSRSI
     SPSPSAILER RDVKPDEDMS SKNLVMFRNE GFYADPYLYH EGRMSIASSH GGHPLDVPDH
     VIAYHRTAIR SASAYCSPSL QAEMHMEQSL YRQKSRKYPD SHLPTLGSKT PPASPHRVGD
     LRMIDLHPHL NTHGPPHTLQ PDRASPSRQS FKKEPGTLVY IEKPRNTSGL SSLVDLGPPL
     VEKQGFAYST TTIPKDRETR ERMQAMEKQI ASLTGLVQSA LFKGPITSSS KEASSEKMVK
     ATANRNQADG AGTAHVSAGK VLGSVEFSLP PSQPLPAGTS PIHTSLLDMR RNVAELRLQL
     QQMRQLQLQN QEILRAMMKK AELEISNKVK ETMKRLEDPV QRQRTLVEQE RQKYLHEEER
     IVKKLCELED FVEDLKKDSS STGRVVTLKD VEDGAFLLRQ VGEAVATLKG EFPTLQNKMR
     AVLRIEVEAV RFLKEEPHKL DSLLKRVRSM TDVLTMLRRH VTDGLLKGTD ASQAAQYVAM
     EKATAAEVLK HQEETAHAPG QPLHCSTGSP GDVKSEVVPL STMTVHHVQS SPVVMQPSQH
     SSALMNPAQN LPGGTRPHTA SPPAITQEVT SAQSAPGPQS PQTPVNGSSM QSLFIEEIHS
     VSAKNRAVSI EKAEKKWEEK RQNLEHYNGK EFEKLLEEAQ ANIMKSIPNL EMPPASSPVS
     KGDAAGDKLE LSEDSPNSEQ ELDKIGGKSP PPPPPPPRRS YLPGSGLTTT RSGDVVYTGR
     SMSKVSSEDP GPTPQTRATK CPPEEPASAW APSPPPVPAP SSKEEEEEEE EGDKIMAELQ
     AFQKCSFMDV NPNSHAEQSR ANSHLKDTRA GATAPPKEKK NLEFYHEDVR KSDVECENGP
     QVESQKVTAG ALRPSGPPKW ERVMVDSISD TSRTSECRAD TFTEENATPN KSLFRDSRNY
     SQKNVPKVSF SSSGLNSLEG EINKGPNVSG LQCAIPDLEN QKLNFGKTKE IGQQGQENAD
     KSHIPLPTRS AEFSIHDVKT QDQDVPVTGY GQVVLRSKVG RHANMNMNED GESTPSSPSE
     EHTATDNIAF MITKTAVQVL SSGEVHDIVS QKGQDVQTVN IDGRKETASQ HEGTEGEEPV
     VCLDKKPVII IFDEPMDIRS AYKRLSTIFE ECDEELERML TEEKIEEEEE DENEDSGVRT
     SSQMSCEQVD SRSDRMGQKA ETQSQPHVLS AELLTPGVQG VRKAEQRKLS SADSPDSGNK
     CGMVDDQFES PKKKFKFKFP KKQLAALTQA IRTGTKTGKK TLQVVVYEEE EEDGTLKQHK
     EAKRFEITRS QPEDALKTMA RRQEQLSPEG TLPASRTDEI RKSTYRTLDS LEQTIKQLEN
     TISEMSPRAL VDTSCSSNRD CGASLPHMAQ EVSPRSLLVL DEVPPAPEPP TSISPASRKG
     SSTTPQTSRM PVPMTSKNRP GSLDKASKQS KLQDPRQYRQ ANGSAKKAGG DCKPTSPSLP
     ASKIPALSPS SGKSSSLPSA SGDSSNLPNA PATKPSIAST PLSPQAGRSA HSASLIPSVS
     NGSLKFQSPP HAGKGHHHLS FALQTQNGRA APTTSSSSSP PSPASPTSLN QGARGIRTIH
     TPSLASYKAQ NGSSSKATPS TAKETS
//
ID   A2AR26_MOUSE            Unreviewed;       443 AA.
AC   A2AR26;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 39.
DE   SubName: Full=Slc2a6 protein;
DE   SubName: Full=Solute carrier family 2 (Facilitated glucose transporter), member 6;
GN   Name=Slc2a6; ORFNames=RP23-449M10.2-006;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Tracey A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC       transporter (TC 2.A.1.1) family.
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DR   EMBL; BC141168; AAI41169.1; -; mRNA.
DR   EMBL; AL845266; CAM24658.1; -; Genomic_DNA.
DR   IPI; IPI00749532; -.
DR   RefSeq; NP_001171098.1; NM_001177627.1.
DR   UniGene; Mm.41203; -.
DR   PRIDE; A2AR26; -.
DR   Ensembl; ENSMUST00000102890; ENSMUSP00000099954; ENSMUSG00000036067.
DR   GeneID; 227659; -.
DR   KEGG; mmu:227659; -.
DR   CTD; 227659; -.
DR   MGI; MGI:2443286; Slc2a6.
DR   GeneTree; ENSGT00600000084007; -.
DR   HOVERGEN; HBG104335; -.
DR   Bgee; A2AR26; -.
DR   Genevestigator; A2AR26; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0022891; F:substrate-specific transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   InterPro; IPR020846; Major_facilitator_SF.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   InterPro; IPR005828; Sub_transporter.
DR   InterPro; IPR003663; Sugar/inositol_transpt.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   PRINTS; PR00171; SUGRTRNSPORT.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR   PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Sugar transport; Transmembrane; Transmembrane helix;
KW   Transport.
SQ   SEQUENCE   443 AA;  48547 MW;  C71F0A6599615863 CRC64;
     MQEPLLRTEG LDYDTFPEVP ATPGERERAG ALKNRRVFLA TFAAVLGNFS FGYALVYTSP
     VIPELKLSSD PALHLDKIQA SWFGSVFTLG AAAGGLSAML LNDLLGRKLS IMFSAVPSAI
     GYAIMAGARG LWMLLLGRML TGFAGGLTAA CIPVYVSEIA PPDVRGALGA TPQLMAVFGS
     LSLYALGLLL PWRWLAVAGE GPVLIMILLL SFMPNSPRFL LSKSRDEEAL QALTWLRADS
     EVHWEFEQIQ DNVRRQSSRV SWAEAREPRV YRPVLIAVLM RFLQQLTGIT PILVYLQTIF
     DNTSVVLPSQ QDAAIVGAVR LLSVLIAAVT MDLAGRKVLL YVSGYAMGWG PITWLLMSEV
     LPLRARGVAS GLCVLVSWLT AFVLTNYFLL AVNAFGLQVP FFFFSAICLL SLLFTGCCVP
     ETRGRSLEQI EAFFHTRRMS FRP
//
ID   RGPS1_MOUSE             Reviewed;         585 AA.
AC   A2AR50; A2AR51; A2AR52; Q6GQS4; Q6ZQD2; Q8BVR9; Q8C1I2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   08-MAR-2011, entry version 41.
DE   RecName: Full=Ras-specific guanine nucleotide-releasing factor RalGPS1;
DE   AltName: Full=Ral GEF with PH domain and SH3-binding motif 1;
DE   AltName: Full=Ral guanine nucleotide exchange factor 2;
DE            Short=RalGEF 2;
DE   AltName: Full=RalA exchange factor RalGPS1;
GN   Name=Ralgps1; Synonyms=Kiaa0351, Ralgef2, Ralgps1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Testis, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Guanine nucleotide exchange factor for the small GTPase
CC       RALA (By similarity). May be involved in cytoskeleton organization
CC       (By similarity). May also be involved in the stimulation of
CC       transcription in a Ras-independent fashion (By similarity). SRC
CC       (By similarity). Interacts with RALA (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By
CC       similarity). Note=Associates with membranes through the PH domain
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=A2AR50-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2AR50-2; Sequence=VSP_033482, VSP_033485;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=A2AR50-3; Sequence=VSP_033486;
CC       Name=4;
CC         IsoId=A2AR50-4; Sequence=VSP_033483, VSP_033484;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The PH domain mediates binding to membranes (Probable).
CC       The PH domain is also required for guanine nucleotide exchange of
CC       RALA (By similarity).
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 Ras-GEF domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC25535.1; Type=Erroneous termination; Positions=158; Note=Translated as Lys;
CC       Sequence=BAC25535.1; Type=Frameshift; Positions=84, 123;
CC       Sequence=BAC97933.1; Type=Erroneous initiation;
CC       Sequence=CAM22215.1; Type=Erroneous gene model prediction;
CC       Sequence=CAM25545.1; Type=Erroneous gene model prediction;
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DR   EMBL; AK129123; BAC97933.1; ALT_INIT; mRNA.
DR   EMBL; AK017939; BAC25535.1; ALT_SEQ; mRNA.
DR   EMBL; AK076767; BAC36473.1; -; mRNA.
DR   EMBL; AL845277; CAM22214.1; -; Genomic_DNA.
DR   EMBL; AL929197; CAM22214.1; JOINED; Genomic_DNA.
DR   EMBL; AL845277; CAM22215.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL929197; CAM22215.1; JOINED; Genomic_DNA.
DR   EMBL; AL845277; CAM22216.1; -; Genomic_DNA.
DR   EMBL; AL929197; CAM22216.1; JOINED; Genomic_DNA.
DR   EMBL; AL845277; CAM22217.1; -; Genomic_DNA.
DR   EMBL; AL929197; CAM25544.1; -; Genomic_DNA.
DR   EMBL; AL845277; CAM25544.1; JOINED; Genomic_DNA.
DR   EMBL; AL929197; CAM25545.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL845277; CAM25545.1; JOINED; Genomic_DNA.
DR   EMBL; AL929197; CAM25546.1; -; Genomic_DNA.
DR   EMBL; AL845277; CAM25546.1; JOINED; Genomic_DNA.
DR   EMBL; BC072656; AAH72656.1; -; mRNA.
DR   IPI; IPI00138321; -.
DR   IPI; IPI00460834; -.
DR   IPI; IPI00754130; -.
DR   IPI; IPI00755355; -.
DR   RefSeq; NP_780420.1; NM_175211.4.
DR   UniGene; Mm.274249; -.
DR   PDB; 2DTC; X-ray; 1.70 A; A/B=460-585.
DR   PDBsum; 2DTC; -.
DR   ProteinModelPortal; A2AR50; -.
DR   SMR; A2AR50; 49-289, 460-575.
DR   PRIDE; A2AR50; -.
DR   Ensembl; ENSMUST00000091039; ENSMUSP00000088563; ENSMUSG00000038831.
DR   Ensembl; ENSMUST00000113167; ENSMUSP00000108792; ENSMUSG00000038831.
DR   GeneID; 241308; -.
DR   KEGG; mmu:241308; -.
DR   CTD; 241308; -.
DR   MGI; MGI:1922008; Ralgps1.
DR   GeneTree; ENSGT00600000084163; -.
DR   HOVERGEN; HBG059258; -.
DR   InParanoid; A2AR50; -.
DR   OMA; TSKEENY; -.
DR   OrthoDB; EOG41C6W1; -.
DR   PhylomeDB; A2AR50; -.
DR   NextBio; 384973; -.
DR   Bgee; A2AR50; -.
DR   Genevestigator; A2AR50; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001895; RasGRF_CDC25.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.10.840.10; RasGRF_CDC25; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00720; RASGEF; FALSE_NEG.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Cytoplasm;
KW   Guanine-nucleotide releasing factor; Membrane.
FT   CHAIN         1    585       Ras-specific guanine nucleotide-releasing
FT                                factor RalGPS1.
FT                                /FTId=PRO_0000333193.
FT   DOMAIN       50    289       Ras-GEF.
FT   DOMAIN      459    571       PH.
FT   REGION      461    585       Required for stimulation of nucleotide
FT                                exchange by RALA (By similarity).
FT   MOTIF       330    333       PXXP.
FT   COMPBIAS     21     26       Poly-Ser.
FT   VAR_SEQ      56     72       Missing (in isoform 2).
FT                                /FTId=VSP_033482.
FT   VAR_SEQ     205    243       IYLLDLIYIDSAYPASGSIMENEQRSNQMNNILRIIADL
FT                                -> MSLSYFIINFPGNITCSGPNKMFLQFLVEMFPGSSRDH
FT                                G (in isoform 4).
FT                                /FTId=VSP_033483.
FT   VAR_SEQ     244    585       Missing (in isoform 4).
FT                                /FTId=VSP_033484.
FT   VAR_SEQ     346    417       NLMCQLSVVESKSATFPSEKARHLLDDSVLESRSPRRGLTH
FT                                TSSTAITNGLSLGSSESSEFSEEMSAGLESR -> K (in
FT                                isoform 2).
FT                                /FTId=VSP_033485.
FT   VAR_SEQ     347    416       Missing (in isoform 3).
FT                                /FTId=VSP_033486.
FT   CONFLICT     96     96       R -> L (in Ref. 2; BAC25535).
FT   CONFLICT    100    100       Q -> H (in Ref. 2; BAC25535).
FT   CONFLICT    108    108       E -> K (in Ref. 2; BAC25535).
FT   CONFLICT    118    118       R -> K (in Ref. 2; BAC25535).
FT   CONFLICT    123    134       SHFVKIAKKLLE -> TPCPVKNRPNKLSNN (in Ref.
FT                                2; BAC25535).
FT   CONFLICT    138    138       L -> H (in Ref. 2; BAC25535).
FT   CONFLICT    150    155       SAPIFR -> IATIFL (in Ref. 2; BAC25535).
FT   CONFLICT    162    162       L -> P (in Ref. 4; AAH72656).
FT   CONFLICT    165    165       R -> L (in Ref. 2; BAC25535).
FT   CONFLICT    168    168       K -> M (in Ref. 2; BAC25535).
FT   CONFLICT    174    174       L -> P (in Ref. 2; BAC25535).
FT   CONFLICT    183    183       N -> I (in Ref. 2; BAC25535).
FT   CONFLICT    204    204       G -> C (in Ref. 2; BAC25535).
FT   STRAND      466    472
FT   STRAND      484    490
FT   STRAND      494    498
FT   HELIX       508    510
FT   STRAND      518    520
FT   STRAND      525    527
FT   STRAND      537    541
FT   STRAND      548    552
FT   HELIX       556    570
SQ   SEQUENCE   585 AA;  65475 MW;  96579853188EC18F CRC64;
     MYKRNGLMAS VLVTSATPQG SSSSDSLEGQ SCDYASKSYD AVVFDVLKVT PEEFASQITL
     MDIPVFKAIQ PEELASCGWS KKEKHSLAPN VVAFTRRFNQ VSFWVVREIL TAQTLKIRAE
     ILSHFVKIAK KLLELNNLHS LMSVVSALQS APIFRLTKTW ALLNRKDKTT FEKLDYLMSK
     EDNYKRTRDY IRSLKMVPSI PYLGIYLLDL IYIDSAYPAS GSIMENEQRS NQMNNILRII
     ADLQVSCSYD HLTTLPHVQK YLKSVRYIEE LQKFVEDDNY KLSLRIEPGS SSPRLVSSKE
     DLAGPSAGSS SARFRRRPTC PDTSVAGSLP TPPVPRHRKS HSLGNNLMCQ LSVVESKSAT
     FPSEKARHLL DDSVLESRSP RRGLTHTSST AITNGLSLGS SESSEFSEEM SAGLESRGRL
     YATLGPNWRV PVRNSPRTRS CVYSPTSPCT CTVGSSATVP TMEGPLRRKT LLKEGRKPAL
     SSWTRYWVVL SGATLLYYGA KSLRGTDRKH YKSTPGKKVS IVGWMVQLPD DPEHPDIFQL
     NNPDKGNVYK FQTGSRFHAI LWHKHLDDAC KSSRPQVPAN LMSFE
//
ID   VIP1_MOUSE              Reviewed;        1436 AA.
AC   A2ARP1; A2ARP2; A2ARP3; A2ARP4; Q6P1C8; Q7TSP1; Q80U21; Q8BL16;
AC   Q8BUN6; Q8BVG9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 39.
DE   RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 1;
DE            EC=2.7.4.21;
DE            EC=2.7.4.24;
DE   AltName: Full=Diphosphoinositol pentakisphosphate kinase 1;
DE   AltName: Full=Histidine acid phosphatase domain-containing protein 2A;
DE   AltName: Full=InsP6 and PP-IP5 kinase 1;
DE   AltName: Full=VIP1 homolog;
GN   Name=Ppip5k1; Synonyms=Hisppd2a, Kiaa0377, Vip1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=Swiss Webster; TISSUE=Brain;
RA   Avidan N., Dgany O.D., Cattan D.C., Pariente A., Thulliez M.,
RA   Borot N., Moati L., Alain B., Krasnov T., Olender T., Shalmon L.,
RA   Ben-Asher E., Khen M., Shalev H., Fellous M., Delaunay J., Yaniv I.,
RA   Zaizov R., Beckmann J.S., Lancet D., Tamary H.;
RT   "A 60kb genomic deletion is associated with non-syndromic deafness and
RT   sperm motility disorder but not with congenital dyserythropoietic
RT   anemia type I.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 6).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Adipose tissue, Hippocampus, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
RP   SPLICING.
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Bifunctional inositol kinase that catalyzes the
CC       formation of diphosphoinositol pentakisphosphate (InsP7 or PP-
CC       InsP5) and bi-diphosphoinositol tetrakisphosphate (InsP8 or PP2-
CC       InsP4). Converts inositolitol hexakisphosphate (InsP6) to InsP7.
CC       Also able to convert InsP7 to InsP8. Probably specifically
CC       mediates the formation of 4PP-InsP5 and 6PP-InsP5 InsP7 isomers
CC       but not of 5PP-IP5 InsP7 isomer. Activated when cells are exposed
CC       to hyperosmotic stress (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol hexakisphosphate = ADP +
CC       5-diphospho-1D-myo-inositol (1,2,3,4,6)pentakisphosphate.
CC   -!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 1,3,4,5,6-
CC       pentakisphosphate = ADP + diphospho-1D-myo-inositol
CC       tetrakisphosphate (isomeric configuration unknown).
CC   -!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 5-diphosphate
CC       pentakisphosphate = ADP + 1D-myo-inositol bisdiphosphate
CC       tetrakisphosphate (isomeric configuration unknown).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=A2ARP1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2ARP1-2; Sequence=VSP_030631;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=A2ARP1-3; Sequence=VSP_030634;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=A2ARP1-5; Sequence=VSP_030625, VSP_030626;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=A2ARP1-6; Sequence=VSP_030627, VSP_030628;
CC         Note=No experimental confirmation available;
CC       Name=6;
CC         IsoId=A2ARP1-7; Sequence=VSP_030629, VSP_030630;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC       subfamily.
CC   -!- CAUTION: Although related to histidine acid phosphatases, it lacks
CC       the conserved active sites, suggesting that it has no phosphatase
CC       activity.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC32838.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC       Sequence=BAC37198.1; Type=Frameshift; Positions=42;
CC       Sequence=BAC65546.1; Type=Erroneous initiation;
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DR   EMBL; AF502585; AAP46293.1; -; mRNA.
DR   EMBL; AK122264; BAC65546.1; ALT_INIT; mRNA.
DR   EMBL; AK046696; BAC32838.1; ALT_SEQ; mRNA.
DR   EMBL; AK078268; BAC37198.1; ALT_FRAME; mRNA.
DR   EMBL; AK083140; BAC38780.1; -; mRNA.
DR   EMBL; AL845466; CAM24220.1; -; Genomic_DNA.
DR   EMBL; AL845466; CAM24221.1; -; Genomic_DNA.
DR   EMBL; AL845466; CAM24222.1; -; Genomic_DNA.
DR   EMBL; BC065138; AAH65138.1; -; mRNA.
DR   IPI; IPI00222662; -.
DR   IPI; IPI00330220; -.
DR   IPI; IPI00624662; -.
DR   IPI; IPI00750816; -.
DR   IPI; IPI00751331; -.
DR   IPI; IPI00880404; -.
DR   RefSeq; NP_848910.3; NM_178795.4.
DR   UniGene; Mm.386076; -.
DR   ProteinModelPortal; A2ARP1; -.
DR   SMR; A2ARP1; 525-597.
DR   PRIDE; A2ARP1; -.
DR   Ensembl; ENSMUST00000052029; ENSMUSP00000057632; ENSMUSG00000033526.
DR   Ensembl; ENSMUST00000089945; ENSMUSP00000087391; ENSMUSG00000033526.
DR   Ensembl; ENSMUST00000110622; ENSMUSP00000106252; ENSMUSG00000033526.
DR   Ensembl; ENSMUST00000110626; ENSMUSP00000106256; ENSMUSG00000033526.
DR   Ensembl; ENSMUST00000110629; ENSMUSP00000106259; ENSMUSG00000033526.
DR   GeneID; 327655; -.
DR   KEGG; mmu:327655; -.
DR   NMPDR; fig|10090.3.peg.6760; -.
DR   CTD; 327655; -.
DR   MGI; MGI:2443281; Ppip5k1.
DR   eggNOG; roNOG11112; -.
DR   HOVERGEN; HBG108657; -.
DR   InParanoid; A2ARP1; -.
DR   OMA; ESATAHF; -.
DR   OrthoDB; EOG41VK25; -.
DR   PhylomeDB; A2ARP1; -.
DR   BRENDA; 2.7.4.21; 244.
DR   BRENDA; 2.7.4.24; 244.
DR   NextBio; 397922; -.
DR   Bgee; A2ARP1; -.
DR   CleanEx; MM_HISPPD2A; -.
DR   Genevestigator; A2ARP1; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; ISS:UniProtKB.
DR   GO; GO:0000827; F:inositol 1,3,4,5,6-pentakisphosphate kinase activity; ISS:UniProtKB.
DR   GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; ISS:UniProtKB.
DR   GO; GO:0006020; P:inositol metabolic process; ISS:UniProtKB.
DR   InterPro; IPR000560; His_Pase_superF_clade-2.
DR   Pfam; PF00328; Acid_phosphat_A; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR   PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Transferase.
FT   CHAIN         1   1436       Inositol hexakisphosphate and
FT                                diphosphoinositol-pentakisphosphate
FT                                kinase 1.
FT                                /FTId=PRO_0000315689.
FT   MOD_RES     475    475       Phosphoserine (By similarity).
FT   MOD_RES     730    730       Phosphotyrosine (By similarity).
FT   MOD_RES     939    939       Phosphoserine (By similarity).
FT   MOD_RES    1147   1147       Phosphoserine (By similarity).
FT   VAR_SEQ     261    266       YTVGPD -> MVDAEI (in isoform 4).
FT                                /FTId=VSP_030625.
FT   VAR_SEQ     267   1436       Missing (in isoform 4).
FT                                /FTId=VSP_030626.
FT   VAR_SEQ     403    439       RTPKQKMKMEVTHPRFFALFEKHGGYKTGKLKLKRPE ->
FT                                HPSFVIEKLVPWRCCLKLHLQDLVATVCFHLHGHQQR (in
FT                                isoform 5).
FT                                /FTId=VSP_030627.
FT   VAR_SEQ     440   1436       Missing (in isoform 5).
FT                                /FTId=VSP_030628.
FT   VAR_SEQ     653    671       LAPTGSTSLLNSMSVIQNP -> VTLFSSPCSNYIATQFLK
FT                                F (in isoform 6).
FT                                /FTId=VSP_030629.
FT   VAR_SEQ     672   1436       Missing (in isoform 6).
FT                                /FTId=VSP_030630.
FT   VAR_SEQ     818    837       Missing (in isoform 2).
FT                                /FTId=VSP_030631.
FT   VAR_SEQ    1057   1077       Missing (in isoform 3).
FT                                /FTId=VSP_030634.
FT   CONFLICT    441    441       L -> I (in Ref. 3; BAC38780).
FT   CONFLICT    831    831       T -> A (in Ref. 3; BAC32838).
FT   CONFLICT   1049   1049       P -> S (in Ref. 2; BAC65546).
FT   CONFLICT   1180   1180       T -> A (in Ref. 1; AAP46293 and 2;
FT                                BAC65546).
SQ   SEQUENCE   1436 AA;  159923 MW;  D160DDDA7F34B4F2 CRC64;
     MWSLTANEDE STTAHFFLGA GDEGLGTCGI GMRTEESDSE LLEDEEDEVP PEPQIIVGIC
     AMTKKSKSKP MTQILERLCR FDYLTVVILG EDVILNEPVE NWPSCHCLIS FHSKGFPLDK
     AVAYSKLRNP FLINDLAMQY YIQDRREVYR ILQEEGIDLP RYAVLNRDPA CPEECSLIEG
     EDQVEVNGAV FPKPFVEKPV SAEDHNVYIY YPSSAGGGSQ RLFRKIGSRS SVYSPESSVR
     KTGSYIYEEF MPTDGTDVKV YTVGPDYAHA EARKSPALDG KVERDSEGKE VRYPVMLTAM
     EKLVARKVCV AFKQTVCGFD LLRANGHSFV CDVNGFSFVK NSMKYYDDCA KILGNTIMRE
     LAPQFQIPWS IPTEAEDIPI VPTTSGTMME LRCVIAIIRH GDRTPKQKMK MEVTHPRFFA
     LFEKHGGYKT GKLKLKRPEQ LQEVLDITRL LLAELEKEPE AEIEEKTGKL EQLKSVLEMY
     GHFSGINRKV QLTYYPHGVK ASNEGQDLQR EPLAPSLLLV LKWGGELTPD GRVQAEELGR
     AFRCMYPGGQ GDYAGFPGCG LLRLHSTFRH DLKIYASDEG RVQMTAAAFA KGLLALEGEL
     TPILVQMVKS ANMNGLLDSD SDSLSSCQHR VKARLHHILQ QDAPFGPEDY DQLAPTGSTS
     LLNSMSVIQN PVKVCDQVFA LIENLTHQIR ERMQDPSSVD LQLYHSETLE LMLQRWSKLE
     RDFRQKSGRY DISKIPDIYD CVKYDVQHNG SLGLQGTAEL LRLSKALADV VIPQEYGISR
     EEKVEIAVGF CLPLLRKILL DLQRTHEDES VNKLHPLYSR GVLSPGRHVR TRLYFTSESH
     VHSLLSVFRY GGLLDETQDA QWQRALAYLS AISELNYMTQ IVIMLYEDNT RDPLSEERFH
     VELHFSPGVK GVEEGSAPAG CGFRPASSEN EEMKTDPGSI ENLCPGKASD EPDRALQTSP
     QPVEGTGLPR RSPLIRNRKA GSMEVLSETS SSRPGGYRLF SSSRPPTEMK QSGLGSQCTG
     LFSTTVLGGS SSAPNLQDYA RTHGKKLPPA SLKHRDELLF VPAVKRFSVS FAKHPTNGFE
     GCSMVPTIYP LETLHNALSL RQVSEFLTKV CQRHTDAHAQ ASAALFDSMH NHQASDSPFS
     PPRTLHSPPL QLRHRSEKPP WYSSGPSSTV SSAGPSSPTT VDGNSHFGFS DQSSVNIHMT
     EEKQGFGLLQ ETPGDGTREL HIERQQELVE PAQSPQELPV EICPSGSQGV TKVSQTCQEV
     PDIVQPCHNI HEEIGQPQQE VPDISQLLLK DHDTTTNTCH LCQASQLSQK VCEEICQLCQ
     DNHEESNQLC QEVSVKLGRM VHGFPVNVDS TAQETLMEIG RPTQEIPEDP YQEFSVKVGV
     LAQKAPAISE LSQDIPEADK PSQELSEETE LQAQEVSEEI DQESEVVDEL PPEAIS
//
ID   A2ARS0_MOUSE            Unreviewed;       390 AA.
AC   A2ARS0;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   SubName: Full=Novel ankyrin repeat domain containing protein;
GN   Name=Gm1337; ORFNames=RP23-204G5.3-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Phillimore B.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL845470; CAM17417.1; -; Genomic_DNA.
DR   IPI; IPI00379202; -.
DR   RefSeq; NP_001075440.1; NM_001081971.1.
DR   UniGene; Mm.35758; -.
DR   ProteinModelPortal; A2ARS0; -.
DR   SMR; A2ARS0; 14-174.
DR   PhosphoSite; A2ARS0; -.
DR   PRIDE; A2ARS0; -.
DR   Ensembl; ENSMUST00000104937; ENSMUSP00000100542; ENSMUSG00000078137.
DR   GeneID; 383787; -.
DR   KEGG; mmu:383787; -.
DR   MGI; MGI:2686183; Gm1337.
DR   GeneTree; ENSGT00600000084433; -.
DR   HOGENOM; HBG505639; -.
DR   InParanoid; A2ARS0; -.
DR   OMA; HGAVLEF; -.
DR   OrthoDB; EOG4NGGN5; -.
DR   NextBio; 404179; -.
DR   Bgee; A2ARS0; -.
DR   Genevestigator; A2ARS0; -.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 2.
DR   SMART; SM00248; ANK; 3.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
PE   4: Predicted;
KW   ANK repeat; Repeat.
SQ   SEQUENCE   390 AA;  41068 MW;  8577D68BDFAE633B CRC64;
     MLKPKDLCPR AGTRTFLEAM QAGKVHLARF VLDALDRSII DCRAEQGRTP LMVAVGLPDP
     AMRSRFVRLL LEQGAAVNLR DERGRTALSL ACERGHLDAV QLLVQFSGDP EATDSAGNSP
     VMWAAACGHG AVLEFLVRSF RRLGLRLDRT NRAGLTALQL AASRGHGTCV QALTGPWGRA
     AAAAAARGSN SDSPPGHPAP APSPERRRPS PRRLPRPLLA RFARAAGGHG HGHGHGHGHG
     GELASAGKGS VRYRAQGNER PELGRSMSLA LGTMTEEETA RLRAGALMAR PNSPQSSGSG
     RWRSQEVLEG APLALMQAPV GLSPHPEGCP GSGRLGLRRR STAPDIPSLV GEASGPESGP
     ELENNALPFS VPGPKPWQAG TEAVVLQAQR
//
ID   A2ASB4_MOUSE            Unreviewed;      1122 AA.
AC   A2ASB4;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   SubName: Full=Adaptor-related protein complex AP-4, epsilon 1;
GN   Name=Ap4e1; ORFNames=RP23-26A12.1-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Brown J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Collins J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL928836; CAM18335.1; -; Genomic_DNA.
DR   EMBL; AL928590; CAM18335.1; JOINED; Genomic_DNA.
DR   EMBL; AL928590; CAM19126.1; -; Genomic_DNA.
DR   EMBL; AL928836; CAM19126.1; JOINED; Genomic_DNA.
DR   IPI; IPI00828779; -.
DR   RefSeq; NP_780759.2; NM_175550.3.
DR   UniGene; Mm.134045; -.
DR   ProteinModelPortal; A2ASB4; -.
DR   SMR; A2ASB4; 33-607.
DR   STRING; A2ASB4; -.
DR   PRIDE; A2ASB4; -.
DR   Ensembl; ENSMUST00000002063; ENSMUSP00000002063; ENSMUSG00000001998.
DR   GeneID; 108011; -.
DR   KEGG; mmu:108011; -.
DR   CTD; 108011; -.
DR   MGI; MGI:1336993; Ap4e1.
DR   eggNOG; roNOG12711; -.
DR   HOVERGEN; HBG050522; -.
DR   InParanoid; A2ASB4; -.
DR   OMA; VKQNVKM; -.
DR   PhylomeDB; A2ASB4; -.
DR   NextBio; 359873; -.
DR   Bgee; A2ASB4; -.
DR   Genevestigator; A2ASB4; -.
DR   GO; GO:0030126; C:COPI vesicle coat; IEA:InterPro.
DR   GO; GO:0005802; C:trans-Golgi network; TAS:MGI.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR   GO; GO:0016192; P:vesicle-mediated transport; TAS:MGI.
DR   InterPro; IPR017109; AP4_complex_esu.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   InterPro; IPR011710; Coatomer_bsu_C.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   Pfam; PF07718; Coatamer_beta_C; 1.
DR   PIRSF; PIRSF037097; AP4_complex_epsilon; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
PE   4: Predicted;
SQ   SEQUENCE   1122 AA;  124845 MW;  D5B4E518714DBA3D CRC64;
     MSDMVERTLT ALPGLFLQNQ LGGPAASRAP FFSRLGGLIR GVTALSSKHE EEKLIQQELS
     SLKATVSAPT TTLKTMKECM VRLIYCEMLG YDASFGYIHA IKLAQQGNLL EKRVGYLAVS
     LFLHESHELL LLLVNTVVKD LQSTNLVEVC MALTVVSQIF PREMIPAVLP LIEDKLQHSK
     EIIRRKAVLA LYKFYLIAPN QVQHIHTKFR KALCDRDVGV MAASLHIYLR MIKENASGYK
     DLTESFVTIL KQVVGGKLPV EFSYHSVPAP WLQIQLLRIL GLLGKDDERT SELMYDVLDE
     SLRRAELNHN VTYAILFECV HTIYSIYPKS ELLEKAAKCI GKFVLSPKIN LKYLGLKALT
     YVIQQDPSLA LQHQITIIEC LDHPDPIIKR ETLELLYRIT NAQNVVVIVQ KMLEYLHQSK
     EEHIIISLVG RIAELAEKYA PDNVWFIQTM NAVFSVGGDV MHPDILSNFL RLLAEGFDDE
     TEDQQLRLYA VQSYLTLLDM ENTFYPQRFL QVMSWVLGEY SYLLDKESPE EVITRLYKLL
     MSDSISSETK AWLFAAVTKL TPQAHSSPLV EKLIQEFTVS LNTCLRQHAF ELKHLHENTE
     LMKSLLQGAQ NCEDIVADAS LSFLDGFVAE GLSQGAAPYK PHHQRQEEQL SQEKVLNFEP
     YGLSFSSSGF TGRQSPAGIS LGSDISGNSA ETGLKETSSL KMEGIKKLWG KEGYLPKKES
     GTGDKPEASH VPAEGATVEN VDQATTRKDQ AQGHIPSTEE KEKQLLASSL FVGLGPENTV
     DLLGKADVVS HKFRRKSKLK VAQSDKTPSA PTAPCSALSL GSDVAGGDED GLSAVDRGDG
     ELSSELFRSE SLSGPPSAEK LESVSLPVPS LFADNNMEVF NPPSSSATST VKEETPECRH
     SGLVEICSNE AVSVSSYKVW RDDCLLVIWA VTSKTDSEFT DAQLEIFPVE NFKIIEQPEC
     SSPVIETERT KSFQYSVQME SPCIEGTLSG FIKYQMMDTH SVQLEFSMNL PLLDFIRPLK
     ISTEDFGKLW LSFANDVKQT IKISEPGVAL TSVLTELQQN LRLRVIDVIG NEGLLACKLL
     PSTPCVLHCR VHADAVALWF RSSSSVLSDY LSCHCQKVMQ TS
//
ID   A2ASI5_MOUSE            Unreviewed;      1947 AA.
AC   A2ASI5;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   08-MAR-2011, entry version 28.
DE   SubName: Full=Sodium channel voltage-gated type III alpha;
GN   Name=Scn3a; ORFNames=RP23-401G6.1-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Smith M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Tracey A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the sodium channel family.
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DR   EMBL; AL772235; CAM15655.1; -; Genomic_DNA.
DR   EMBL; AL928621; CAM15655.1; JOINED; Genomic_DNA.
DR   EMBL; AL928621; CAM23401.1; -; Genomic_DNA.
DR   EMBL; AL772235; CAM23401.1; JOINED; Genomic_DNA.
DR   IPI; IPI00831467; -.
DR   RefSeq; NP_061202.3; NM_018732.3.
DR   UniGene; Mm.330256; -.
DR   ProteinModelPortal; A2ASI5; -.
DR   STRING; A2ASI5; -.
DR   PhosphoSite; A2ASI5; -.
DR   Ensembl; ENSMUST00000100069; ENSMUSP00000097647; ENSMUSG00000057182.
DR   GeneID; 20269; -.
DR   KEGG; mmu:20269; -.
DR   CTD; 20269; -.
DR   MGI; MGI:98249; Scn3a.
DR   HOVERGEN; HBG053100; -.
DR   OrthoDB; EOG4Z36CT; -.
DR   NextBio; 297943; -.
DR   Bgee; A2ASI5; -.
DR   Genevestigator; A2ASI5; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:InterPro.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; IEA:InterPro.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001696; Na_channel_asu.
DR   InterPro; IPR010526; Na_trans_assoc.
DR   Pfam; PF00520; Ion_trans; 4.
DR   Pfam; PF06512; Na_trans_assoc; 1.
DR   PRINTS; PR00170; NACHANNEL.
DR   SMART; SM00015; IQ; 1.
PE   3: Inferred from homology;
KW   Ion transport; Ionic channel; Membrane; Sodium; Sodium channel;
KW   Sodium transport; Transmembrane; Transport; Voltage-gated channel.
SQ   SEQUENCE   1947 AA;  220880 MW;  B5E01EEC78004E15 CRC64;
     MAQALLVPPG PESFRLFTRE SLAAIEKRAA EEKAKKPKKE QDIDDENKPK PNSDLEAGKN
     LPFIYGDIPP EMVSEPLEDL DPYYVSKKTF VVLNKGKAIF RFSATSALYI LTPLNPVRKI
     AIKILVHSLF SMLIMCTILT NCVFMTLSNP PDWTKNVEYT FTGIYTFESL IKILARGFCL
     EDFTFLRDPW NWLDFSVIVM AYVTEFVDLG NVSALRTFRV LRALKTISVI PGLKTIVGAL
     IQSVKKLSDV MILTVFCLSV FALIGLQLFM GNLRNKCLQW PPSDSAFEIN TTSYFNGTMD
     SNGTFVNVTM STFNWKDYIA DDSHFYVLDG QKDPLLCGNG SDAGQCPEGY ICVKAGRNPN
     YGYTSFDTFS WAFLSLFRLM TQDYWENLYQ LTLRAAGKTY MIFFVLVIFL GSFYLVNLIL
     AVVAMAYEEQ NQATLEEAEQ KEAEFQQMLE QLKKQQEEAQ AVAAASAASR DFSGIGGLGE
     LLESSSEASK LSSKSAKEWR NRRKKRRQRE HLEGNHRPEG DRFPKSESED SVKRRSFLFS
     LDGNPLSGDK KLCSPHQSLL SIRGSLFSPR RNSKTSIFSF RGRAKDVGSE NDFADDEHST
     FEDSESRRDS LFVPHRPGER RNSNGTTTET EVRKRRLSSY QISMEMLEDS SGRQRAMSIA
     SILTNTMEEL EESRQKCPPC WYRFANVFLI WDCCDSWLKV KHLVNLIVMD PFVDLAITIC
     IVLNTLFMAM EHYPMTEQFS SVLTVGNLVF TGIFTAEMVL KIIAMDPYYY FQEGWNIFDG
     IIVSLSLMEL GLANVEGLSV LRSFRLLRVF KLAKSWPTLN MLIKIIGNSV GALGNLTLVL
     AIIVFIFAVV GMQLFGKSYK ECVCKINEDC KLPRWHMNDF FHSFLIVFRV LCGEWIETMW
     DCMEVAGQTM CLIVFMLVMV IGNLVVLNLF LALLLSSFSS DNLAATDDDN EMNNLQIAVG
     RMQKGIDYVK NKIRECFRKA FFRKPKVIEI HEGNKIDSCM SNNTGVVEIS KELNYLKDGN
     GTTSGVGTGS SVEKYVIDEN DYMSFINNPS LTVTVPIAVG ESDFENLNTE EFSSESELEE
     SKEKLNATSS SEGSTVDVAP PREGEQAEIE PEEDLKPEAC FTEGCIKKFP FCQVSTEEGK
     GKIWWNLRKT CYSIVEHNWF ETFIVFMILL SSGALAFEDI YIEQRKTIKT MLEYADKVFT
     YIFILEMLLK WVAYGFQTYF TNAWCWLDFL IVDVSLVSLV ANALGYSELG AIKSLRTLRA
     LRPLRALSRF EGMRVVVNAL VGAIPSIMNV LLVCLIFWLI FSIMGVNLFA GKFYHCVNMT
     TGSMFDMSEV NNFSDCQALG KQARWKNVKV NFDNVGAGYL ALLQVATFKG WMDIMYAAVD
     SRDVKLQPVY EENLYMYLYF VIFIIFGSFF TLNLFIGVII DNFNQQKKKF GGQDIFMTEE
     QKKYYNAMKK LGSKKPQKPI PRPANKFQGM VFDFVTRQVF DISIMILICL NMVTMMVETD
     DQSKYMTLVL SRINLVFIVL FTGEFLLKLI SLRYYYFTIG WNIFDFVVVI LSIVGMFLAE
     LIEKYFVSPT LFRVIRLARI GRILRLIKGA KGIRTLLFAL MMSLPALFNI GLLLFLVMFI
     YAIFGMSNFA YVKKEAGIDD MFNFETFGNS MICLFQITTS AGWDGLLAPI LNSAPPDCDP
     DAIHPGSSVK GDCGNPSVGI FFFVSYIIIS FLVVVNMYIA VILENFSVAT EESAEPLSED
     DFEMFYEVWE KFDPDATQFI EFCKLSDFAA ALDPPLLIAK PNKVQLIAMD LPMVSGDRIH
     CLDILFAFTK RVLGESGEMD ALRIQMEDRF MASNPSKVSY EPITTTLKRK QEEVSAAIIQ
     RNYRCYLLKQ RLKNISNTYD KETIKGRIVL PIKGDMVIDK LNGNSTPEKT DGSSSTTSPP
     SYDSVTKPDK EKFEKDKPEK ESKGKEV
//
ID   A2ATK9_MOUSE            Unreviewed;       892 AA.
AC   A2ATK9;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   30-NOV-2010, entry version 32.
DE   SubName: Full=Family with sequence similarity 171, member A1;
GN   Name=Fam171a1; ORFNames=RP23-60E18.1-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Ellwood M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC138175; AAI38176.1; -; mRNA.
DR   EMBL; AL928883; CAM26396.1; -; Genomic_DNA.
DR   IPI; IPI00352788; -.
DR   RefSeq; NP_001074630.1; NM_001081161.1.
DR   UniGene; Mm.478311; -.
DR   ProteinModelPortal; A2ATK9; -.
DR   STRING; A2ATK9; -.
DR   PhosphoSite; A2ATK9; -.
DR   PRIDE; A2ATK9; -.
DR   Ensembl; ENSMUST00000115099; ENSMUSP00000110751; ENSMUSG00000050530.
DR   GeneID; 269233; -.
DR   KEGG; mmu:269233; -.
DR   CTD; 269233; -.
DR   MGI; MGI:2442917; Fam171a1.
DR   HOGENOM; HBG715100; -.
DR   HOVERGEN; HBG057508; -.
DR   InParanoid; A2ATK9; -.
DR   OMA; VDHLERP; -.
DR   NextBio; 392750; -.
DR   Bgee; A2ATK9; -.
DR   Genevestigator; A2ATK9; -.
DR   InterPro; IPR018890; Uncharacterised_FAM171.
DR   Pfam; PF10577; UPF0560; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   892 AA;  97963 MW;  F6EEDACE93676E3F CRC64;
     MSKSAALLLC LLGCHVWKAV TKTLQEPGAG AQEVTLKVHI SDASTHQPIA DALIEIFASQ
     VSVASGTSGT DGVAFIKFPY KLGNQLIVTA TKQAYVPNSA PWKPIRLPVF SSLSLGLLPE
     RSATLMVYED VVQIVSGFQG ARPQPRVHFQ RRALRLPENT SYSDLTAFLT AASSPSEVDS
     FPYLRGLDGN GTGNSTRYDL TPVTAVSVHL LSGNGMPVLV DGPIYVTVPL ATQSSLRHNA
     YVAAWRFDQK LGTWLKSGLG LVHQEGSQLT WTYIAPQLGY WVAAMSPPIP GPVMTQDITT
     YHTVFLLAIL GGMAFILLVL LCLLLYYCRR KCLKPRQHHR KLQLPPALES SKRDQATSMS
     HINLLFSRRA SDYPGPLSVS SHSRPEAPGT KELMGGVHLE MMSPKGEGDL HTPMLKLSYS
     TSQEFSSREE LLSHKEEDKS QTSFDNLTPS GTLGKDYHKS VEIFPLKARK SMEKEDYEAP
     GNDDYRGSYN TVLSQSLFEK QDQEGLASAG SKLTIQEHMY HVPLSPEKEQ LLDRRPTECM
     MSRSVDHLER PTSFPRPGQL ICCSSVDQVN DSVYRKVLPA LVIPAHYMKL PGDHSYVSQP
     LVVPADQQLE IGRLQAELSN PHAGIFPHPS SQIQGQPLSS QAISQQHLQE AGAREWSSQS
     ASMSESLSIP ASLNDAALAQ MNSEVQLLTE KALMELGGGK PLPHPRAWFV SLDGRSNAHV
     RHSYIDLQRA GRNGSNDASL DSGVDMNEPK SARKGRGDPL SLQQSHTPLQ EHQQKDPRAP
     DSTACTQLLY LEDMDPSGSE CAATVCTPED SALRCLLEGS GRRSGGQLPS LQEETTKRTS
     DVPLEPLASP NQRRSANDED EDDDDDDDDQ GEDKKSPWQK REERPLMAFN IK
//
ID   A2ATZ5_MOUSE            Unreviewed;       473 AA.
AC   A2ATZ5;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   05-OCT-2010, entry version 25.
DE   SubName: Full=Calcium channel, voltage-dependent, beta 4 subunit;
GN   Name=Cacnb4; ORFNames=RP23-435G20.4-003;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Humphries M.;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Wood J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AL928960; CAM23660.1; -; Genomic_DNA.
DR   EMBL; AL845467; CAM23660.1; JOINED; Genomic_DNA.
DR   EMBL; AL845467; CAM24280.1; -; Genomic_DNA.
DR   EMBL; AL928960; CAM24280.1; JOINED; Genomic_DNA.
DR   IPI; IPI00473235; -.
DR   UniGene; Mm.330223; -.
DR   UniGene; Mm.472778; -.
DR   ProteinModelPortal; A2ATZ5; -.
DR   SMR; A2ATZ5; 2-356.
DR   STRING; A2ATZ5; -.
DR   PRIDE; A2ATZ5; -.
DR   Ensembl; ENSMUST00000102761; ENSMUSP00000099822; ENSMUSG00000017412.
DR   MGI; MGI:103301; Cacnb4.
DR   HOVERGEN; HBG050765; -.
DR   Bgee; A2ATZ5; -.
DR   Genevestigator; A2ATZ5; -.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:MGI.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; TAS:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0046058; P:cAMP metabolic process; IMP:MGI.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
DR   GO; GO:0014051; P:gamma-aminobutyric acid secretion; IMP:MGI.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IMP:MGI.
DR   GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
DR   GO; GO:0019227; P:neuronal action potential propagation; IMP:MGI.
DR   GO; GO:0048541; P:Peyer's patch development; IMP:MGI.
DR   GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR   GO; GO:0048536; P:spleen development; IMP:MGI.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IMP:MGI.
DR   GO; GO:0048538; P:thymus development; IMP:MGI.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR000584; VDCC_L_bsu.
DR   PANTHER; PTHR11824; Ca_channel_B; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF12052; VGCC_beta4Aa_N; 1.
DR   PRINTS; PR01626; LCACHANNELB.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
SQ   SEQUENCE   473 AA;  53084 MW;  1EA0EE1CA4264A65 CRC64;
     MAGSADSYTS RPSDSDVSLE EDREAIRQER EQQAAIQLER AKSKPVAFAV KTNVSYCGAL
     DEDVPVPSTA ISFDAKDFLH IKEKYNNDWW IGRLVKEGCE IGFIPSPLRL ENIRIQQEQK
     RGRFHGGKSS GNSSSSLGEM VSGTFRATPT TTAKQKQKVT EHIPPYDVVP SMRPVVLVGP
     SLKGYEVTDM MQKALFDFLK HRFDGRISIT RVTADISLAK RSVLNNPSKR AIIERSNTRS
     SLAEVQSEIE RIFELARSLQ LVVLDADTIN HPAQLIKTSL APIIVHVKVS SPKVLQRLIK
     SRGKSQSKHL NVQLVAADKL AQCPPEMFDV ILDENQLEDA CEHLGEYLEA YWRATHTSSS
     TPMTPLLGRN VGSTALSPYP TAISGLQSQR MRHSNHSTEN SPIERRSLMT SDENYHNERA
     RKSRNRLSSS SQHSRDHYPL VEEDYPDSYQ DTYKPHRNRG SPGGCSHDSR HRL
//
ID   A2ATZ6_MOUSE            Unreviewed;       486 AA.
AC   A2ATZ6;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   11-JAN-2011, entry version 31.
DE   SubName: Full=Calcium channel, voltage-dependent, beta 4 subunit;
DE   SubName: Full=Calcium channel, voltage-dependent, beta 4 subunit, isoform CRA_a;
GN   Name=Cacnb4; ORFNames=RP23-435G20.4-001, mCG_141879;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Humphries M.;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RA   Wood J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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CC   -----------------------------------------------------------------------
DR   EMBL; AL928960; CAM23661.1; -; Genomic_DNA.
DR   EMBL; AL845467; CAM23661.1; JOINED; Genomic_DNA.
DR   EMBL; AL845467; CAM24281.1; -; Genomic_DNA.
DR   EMBL; AL928960; CAM24281.1; JOINED; Genomic_DNA.
DR   EMBL; CH466519; EDL26909.1; -; Genomic_DNA.
DR   IPI; IPI00131720; -.
DR   RefSeq; NP_666235.1; NM_146123.2.
DR   UniGene; Mm.330223; -.
DR   UniGene; Mm.472778; -.
DR   ProteinModelPortal; A2ATZ6; -.
DR   SMR; A2ATZ6; 1-369.
DR   STRING; A2ATZ6; -.
DR   PRIDE; A2ATZ6; -.
DR   Ensembl; ENSMUST00000102760; ENSMUSP00000099821; ENSMUSG00000017412.
DR   GeneID; 12298; -.
DR   KEGG; mmu:12298; -.
DR   CTD; 12298; -.
DR   MGI; MGI:103301; Cacnb4.
DR   HOVERGEN; HBG050765; -.
DR   NextBio; 280812; -.
DR   Bgee; A2ATZ6; -.
DR   Genevestigator; A2ATZ6; -.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:MGI.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; TAS:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0046058; P:cAMP metabolic process; IMP:MGI.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
DR   GO; GO:0014051; P:gamma-aminobutyric acid secretion; IMP:MGI.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IMP:MGI.
DR   GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
DR   GO; GO:0019227; P:neuronal action potential propagation; IMP:MGI.
DR   GO; GO:0048541; P:Peyer's patch development; IMP:MGI.
DR   GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR   GO; GO:0048536; P:spleen development; IMP:MGI.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IMP:MGI.
DR   GO; GO:0048538; P:thymus development; IMP:MGI.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR008079; VDCC_L_b3su.
DR   InterPro; IPR000584; VDCC_L_bsu.
DR   PANTHER; PTHR11824; Ca_channel_B; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF12052; VGCC_beta4Aa_N; 1.
DR   PRINTS; PR01626; LCACHANNELB.
DR   PRINTS; PR01696; LCACHANNELB3.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
SQ   SEQUENCE   486 AA;  54619 MW;  F4FCDD8810D75696 CRC64;
     MYDNLYLHGV EDSEAGSADS YTSRPSDSDV SLEEDREAIR QEREQQAAIQ LERAKSKPVA
     FAVKTNVSYC GALDEDVPVP STAISFDAKD FLHIKEKYNN DWWIGRLVKE GCEIGFIPSP
     LRLENIRIQQ EQKRGRFHGG KSSGNSSSSL GEMVSGTFRA TPTTTAKQKQ KVTEHIPPYD
     VVPSMRPVVL VGPSLKGYEV TDMMQKALFD FLKHRFDGRI SITRVTADIS LAKRSVLNNP
     SKRAIIERSN TRSSLAEVQS EIERIFELAR SLQLVVLDAD TINHPAQLIK TSLAPIIVHV
     KVSSPKVLQR LIKSRGKSQS KHLNVQLVAA DKLAQCPPEM FDVILDENQL EDACEHLGEY
     LEAYWRATHT SSSTPMTPLL GRNVGSTALS PYPTAISGLQ SQRMRHSNHS TENSPIERRS
     LMTSDENYHN ERARKSRNRL SSSSQHSRDH YPLVEEDYPD SYQDTYKPHR NRGSPGGCSH
     DSRHRL
//
ID   A2AU34_MOUSE            Unreviewed;       232 AA.
AC   A2AU34;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 26.
DE   SubName: Full=Novel protein;
GN   Name=5430405G05Rik; Synonyms=RP23-402M7.3; ORFNames=RP23-402M7.3-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Wood J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL928988; CAM23445.1; -; Genomic_DNA.
DR   IPI; IPI00930825; -.
DR   RefSeq; NP_001153835.1; NM_001160363.1.
DR   UniGene; Mm.103494; -.
DR   Ensembl; ENSMUST00000060196; ENSMUSP00000060017; ENSMUSG00000044364.
DR   Ensembl; ENSMUST00000109872; ENSMUSP00000105498; ENSMUSG00000044364.
DR   GeneID; 108832; -.
DR   KEGG; mmu:108832; -.
DR   MGI; MGI:1918629; 5430405G05Rik.
DR   eggNOG; maNOG16195; -.
DR   HOVERGEN; HBG051165; -.
DR   InParanoid; A2AU34; -.
DR   OMA; GSINLRM; -.
DR   OrthoDB; EOG466VMV; -.
DR   Bgee; A2AU34; -.
DR   Genevestigator; A2AU34; -.
PE   4: Predicted;
SQ   SEQUENCE   232 AA;  24971 MW;  36AFDB58BD9B1C0A CRC64;
     MASPPGLELK TLSNGPQVPR RAASQGPVAP PRMGVENACF FSEEQETHFQ NPGDARLGNA
     PSPPGGVPSL SRSQRDDLSL HSEEGPGLEP VSRPVDYGFV SALVFLVSGI LLVVTAYAIP
     REARVNPDTV TAREMERLEM YYARLGSHLD KCIIAGLGLL TVGGMLLSVL LMVSLCKGEL
     YRRQTFVPGR GSRKTYGSIN LRMRQLTGDG GQVLVENEVV QVSETSYTTQ GS
//
ID   A2AU63_MOUSE            Unreviewed;       312 AA.
AC   A2AU63;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 32.
DE   SubName: Full=HnRNP-associated with lethal yellow;
GN   Name=C130057N11Rik; Synonyms=Raly; ORFNames=RP23-480H10.2-003;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Griffiths C.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL929024; CAM25655.1; -; Genomic_DNA.
DR   IPI; IPI00828741; -.
DR   RefSeq; NP_001132985.1; NM_001139513.1.
DR   UniGene; Mm.221440; -.
DR   UniGene; Mm.475494; -.
DR   ProteinModelPortal; A2AU63; -.
DR   SMR; A2AU63; 3-97, 187-213.
DR   STRING; A2AU63; -.
DR   PRIDE; A2AU63; -.
DR   Ensembl; ENSMUST00000029120; ENSMUSP00000029120; ENSMUSG00000027593.
DR   Ensembl; ENSMUST00000116389; ENSMUSP00000112090; ENSMUSG00000027593.
DR   GeneID; 19383; -.
DR   KEGG; mmu:19383; -.
DR   CTD; 19383; -.
DR   HOVERGEN; HBG002302; -.
DR   InParanoid; A2AU63; -.
DR   OMA; IYSGYSF; -.
DR   PhylomeDB; A2AU63; -.
DR   Bgee; A2AU63; -.
DR   Genevestigator; A2AU63; -.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   InterPro; IPR017347; hnRNP_C_Raly.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PIRSF; PIRSF037992; hnRNP-C_Raly; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   4: Predicted;
SQ   SEQUENCE   312 AA;  33188 MW;  A2A8FD35476BFC44 CRC64;
     MSLKIQTSNV TNKNDPKSIN SRVFIGNLNT AVVKKSDVET IFSKYGRVAG CSVHKGYAFV
     QYANERHARA AVLGENGRVL AGQTLDINMA GEPKPNRPKG LKRAATAIYS GYSFDYDYYQ
     DYFCARLFDY RGRLSPVPVP RAVPVKRPRV TVPLVRRVKT TIPVKLFARS TAVTTGSAKI
     KLKSSELQTI KTELTQIKSN IDALLGRLEQ IAEEQKANPD GKKKGDSSSG GGGGSSGGGG
     SSNVGGGSSG GSGSCSSSSR LPAPQEDTAS EAGTPQGEVQ TRDDGDEEGL LTHSEEELEH
     SQDTDAEDGA LQ
//
ID   A2AUD5_MOUSE            Unreviewed;       229 AA.
AC   A2AUD5;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-FEB-2011, entry version 29.
DE   SubName: Full=Tumor protein D52-like 2;
GN   Name=Tpd52l2; ORFNames=RP23-33L3.2-009;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Almeida-King J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL929094; CAM21499.1; -; Genomic_DNA.
DR   IPI; IPI00755183; -.
DR   UniGene; Mm.136648; -.
DR   STRING; A2AUD5; -.
DR   PRIDE; A2AUD5; -.
DR   Ensembl; ENSMUST00000108799; ENSMUSP00000104427; ENSMUSG00000000827.
DR   MGI; MGI:1913564; Tpd52l2.
DR   GeneTree; ENSGT00390000015988; -.
DR   HOGENOM; HBG717185; -.
DR   HOVERGEN; HBG058643; -.
DR   InParanoid; A2AUD5; -.
DR   OMA; VMRNSAT; -.
DR   Bgee; A2AUD5; -.
DR   Genevestigator; A2AUD5; -.
DR   InterPro; IPR007327; TPD52.
DR   PANTHER; PTHR19307; TPD52; 1.
DR   Pfam; PF04201; TPD52; 1.
PE   4: Predicted;
SQ   SEQUENCE   229 AA;  25067 MW;  99F4437F02CA962B CRC64;
     MDSASQDINL NSPNKGVLSD FMTDVPVDPG VVHRTPVVEG LTEGEEEELR AELAKVEEEI
     VTLRQVLAAK ERHCGELKRR LGLSTLGELK QNLSRSWHDV QVSTAYVKTS EKLGEWNEKV
     TQSDLYKKTQ ETLSQAGQKT SAALSTMGSA ISRKLGDMRA HPLSQSFSSY SIRHSISMPV
     MRNSATFKSF EDRVGTIKSK VVGGRENGSD NLPPSPGSGD QTLPDHAPF
//
ID   A2AUK4_MOUSE            Unreviewed;       880 AA.
AC   A2AUK4;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   05-OCT-2010, entry version 34.
DE   SubName: Full=Erythrocyte protein band 4.1-like 1;
DE   Flags: Fragment;
GN   Name=Epb4.1l1; ORFNames=RP23-55C8.1-003;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Wray P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 FERM domain.
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DR   EMBL; AL929153; CAM26030.1; -; Genomic_DNA.
DR   IPI; IPI00405986; -.
DR   UniGene; Mm.20852; -.
DR   STRING; A2AUK4; -.
DR   PRIDE; A2AUK4; -.
DR   Ensembl; ENSMUST00000069919; ENSMUSP00000065040; ENSMUSG00000027624.
DR   Ensembl; ENSMUST00000125153; ENSMUSP00000121161; ENSMUSG00000027624.
DR   MGI; MGI:103010; Epb4.1l1.
DR   eggNOG; maNOG05413; -.
DR   HOVERGEN; HBG070295; -.
DR   InParanoid; A2AUK4; -.
DR   Bgee; A2AUK4; -.
DR   Genevestigator; A2AUK4; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0019898; C:extrinsic to membrane; IEA:InterPro.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR021187; Band_41_protein.
DR   InterPro; IPR000798; Ez/rad/moesin.
DR   InterPro; IPR014847; FERM-adjacent.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR007477; SAB.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF04382; SAB; 1.
DR   PIRSF; PIRSF002304; Membrane_skeletal_4_1; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   4: Predicted;
FT   NON_TER     880    880
SQ   SEQUENCE   880 AA;  98495 MW;  8FD39B15148FFB45 CRC64;
     MTTETGPDSE VKKAQEETPQ QPEAAAAVTT PVTPAGHSHP ETNSNEKHLT QQDTRPAEQS
     LDMDDKDYSE ADGLSERTTP SKAQKSPQKI AKKFKSAICR VTLLDASEYE CEVEKHGRGQ
     VLFDLVCEHL NLLEKDYFGL TYCDADSQKN WLDPSKEIKK QIRSSPWNFA FTVKFYPPDP
     AQLTEDITRY YLCLQLRADI ITGRLPCSFV THALLGSYAV QAELGDYDAE EHVGNYVSEL
     RFAPNQTREL EERIMELHKT YRGMTPGEAE IHFLENAKKL SMYGVDLHHA KDSEGIDIML
     GVCANGLLIY RDRLRINRFA WPKILKISYK RSNFYIKIRP GEYEQFESTI GFKLPNHRSA
     KRLWKVCIEH HTFFRLVSPE PPPKGFLVMG SKFRYSGRTQ AQTRQASALI DRPAPFFERS
     SSKRYTMSRS LDGEFSRPAS VSENHDAGPD GDKREDDAES GGRRSEAEEG EVRTPTKIKE
     LKPEQETTPR HKQEFLDKPE DVLLKHQASI NELKRTLKEP NSKLIHRDRD WDRERRLPSS
     PASPSPKGTP EKASEGSEHW VLIERVYTRP EDLGLLTVPA TQREESGSSL TEILADGRLS
     KVDILVDKFK VEVATEETVR AQRTSTQQQG KMIASPEGSE TMREEDACLR GGPRDATRAA
     GYTSTDKLKL RNTRVSNGQT ESHVELNKGL ERPQTWGRLT AAGVGPVQGE VLSPASDKGG
     LQSFLLDPAQ TEARADSSDE TDTSFAERSF CLNYGKKDSE DSLLAPSLGD REEHLDAPPG
     DGTWLELAGA HTENWEPKSS DPRASAPGSS QNKDEAHMAS SAEEAWSPRD RGRPDDLQGS
     AVCQTLEEGW ENTQGLEGEL AYPVADVAED EAPTSIDWMG
//
ID   A2AUK5_MOUSE            Unreviewed;       879 AA.
AC   A2AUK5;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   11-JAN-2011, entry version 39.
DE   SubName: Full=Erythrocyte protein band 4.1-like 1;
DE   SubName: Full=Erythrocyte protein band 4.1-like 1, isoform CRA_c;
GN   Name=Epb4.1l1; ORFNames=RP23-55C8.1-001, mCG_5224;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Wray P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 FERM domain.
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DR   EMBL; AL929153; CAM26031.1; -; Genomic_DNA.
DR   EMBL; CH466551; EDL06197.1; -; Genomic_DNA.
DR   IPI; IPI00465812; -.
DR   RefSeq; NP_001006665.1; NM_001006664.2.
DR   RefSeq; NP_038538.1; NM_013510.3.
DR   UniGene; Mm.20852; -.
DR   ProteinModelPortal; A2AUK5; -.
DR   SMR; A2AUK5; 95-425.
DR   STRING; A2AUK5; -.
DR   PRIDE; A2AUK5; -.
DR   Ensembl; ENSMUST00000029155; ENSMUSP00000029155; ENSMUSG00000027624.
DR   Ensembl; ENSMUST00000088565; ENSMUSP00000085926; ENSMUSG00000027624.
DR   Ensembl; ENSMUST00000103135; ENSMUSP00000099424; ENSMUSG00000027624.
DR   Ensembl; ENSMUST00000103136; ENSMUSP00000099425; ENSMUSG00000027624.
DR   Ensembl; ENSMUST00000103137; ENSMUSP00000099426; ENSMUSG00000027624.
DR   Ensembl; ENSMUST00000109571; ENSMUSP00000105199; ENSMUSG00000027624.
DR   GeneID; 13821; -.
DR   KEGG; mmu:13821; -.
DR   CTD; 13821; -.
DR   MGI; MGI:103010; Epb4.1l1.
DR   HOVERGEN; HBG007777; -.
DR   OMA; APGGKEF; -.
DR   PhylomeDB; A2AUK5; -.
DR   NextBio; 284612; -.
DR   Bgee; A2AUK5; -.
DR   Genevestigator; A2AUK5; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0019898; C:extrinsic to membrane; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
DR   InterPro; IPR008379; Band_4.1_C.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR021187; Band_41_protein.
DR   InterPro; IPR000798; Ez/rad/moesin.
DR   InterPro; IPR014847; FERM-adjacent.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR007477; SAB.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF05902; 4_1_CTD; 1.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF04382; SAB; 1.
DR   PIRSF; PIRSF002304; Membrane_skeletal_4_1; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   4: Predicted;
SQ   SEQUENCE   879 AA;  98315 MW;  2EB501A4B4DCA325 CRC64;
     MTTETGPDSE VKKAQEETPQ QPEAAAAVTT PVTPAGHSHP ETNSNEKHLT QQDTRPAEQS
     LDMDDKDYSE ADGLSERTTP SKAQKSPQKI AKKFKSAICR VTLLDASEYE CEVEKHGRGQ
     VLFDLVCEHL NLLEKDYFGL TYCDADSQKN WLDPSKEIKK QIRSSPWNFA FTVKFYPPDP
     AQLTEDITRY YLCLQLRADI ITGRLPCSFV THALLGSYAV QAELGDYDAE EHVGNYVSEL
     RFAPNQTREL EERIMELHKT YRGMTPGEAE IHFLENAKKL SMYGVDLHHA KDSEGIDIML
     GVCANGLLIY RDRLRINRFA WPKILKISYK RSNFYIKIRP GEYEQFESTI GFKLPNHRSA
     KRLWKVCIEH HTFFRLVSPE PPPKGFLVMG SKFRYSGRTQ AQTRQASALI DRPAPFFERS
     SSKRYTMSRS LDGAEFSRPA SVSENHDAGP DGDKREDDAE SGGRRSEAEE GEVRTPTKIK
     ELKPEQETTP RHKQEFLDKP EDVLLKHQAS INELKRTLKE PNSKLIHRDR DWDRERRLPS
     SPASPSPKGT PEKASERAGL REGSEEKVKP PRPRAPESDT GDEDQDQERD AVFLKDNHLA
     IERKCSSITV SSTSSLEAEV DFTVIGDYHG GAFEDFSRSL PELDRDKSDS ETEGLVFARD
     LKGPSSQEDE SGGLEDSPDR GACSTPEMPQ FESVKAETMT VSSLAIRKKI EPEAMLQSRV
     SAADSTQVDG GTPMVKDFMT TPPCITTETI STTMENSLKS GKGAAAMIPG PQTVATEIRS
     LSPIIGKDVL TSTYGATAET LSTSTTTHVT KTVKGGFSET RIEKRIIITG DEDVDQDQAL
     ALAIKEAKLQ HPDMLVTKAV VYRETDPSPE ERDKKPQES
//
ID   A2AVX0_MOUSE            Unreviewed;       378 AA.
AC   A2AVX0;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   05-OCT-2010, entry version 17.
DE   SubName: Full=Breast carcinoma amplified sequence 1;
DE   Flags: Fragment;
GN   Name=Bcas1; ORFNames=RP23-321D1.1-005;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Humphries M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Heath P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL928812; CAM20734.1; -; Genomic_DNA.
DR   EMBL; AL935134; CAM20734.1; JOINED; Genomic_DNA.
DR   EMBL; AL935134; CAM20746.1; -; Genomic_DNA.
DR   EMBL; AL928812; CAM20746.1; JOINED; Genomic_DNA.
DR   IPI; IPI00404199; -.
DR   UniGene; Mm.240850; -.
DR   STRING; A2AVX0; -.
DR   Ensembl; ENSMUST00000154650; ENSMUSP00000122298; ENSMUSG00000013523.
DR   MGI; MGI:1924210; Bcas1.
DR   HOVERGEN; HBG082347; -.
DR   Bgee; A2AVX0; -.
DR   Genevestigator; A2AVX0; -.
PE   4: Predicted;
FT   NON_TER       1      1
SQ   SEQUENCE   378 AA;  40427 MW;  7FE7345180815624 CRC64;
     QTLPATGPLA PSPPESQAEA PAQDKDFGFL NRFFKLDKGR ESAPVNSQPK EAKGSEDPEQ
     ATEAPAVPGN PHGVSAGEDI VDSEQRGQDV DTLSYSVPGD PEVPGTTKED PQVVDTTENS
     SSIMSFFKTL VSPNKTETKK DPEDTKATKA DSVCDGHAAG QKMSETQAKS KKKRLDSPRL
     GLSFRKLFRH KDTENSPTTS ANLKSDKANF TPQETRGKTK ATKSCSPPPP PPEPTSEGRD
     SGKEKAGPTS LPLGKLFWKK TSNSVEKTPS PPEPEPAGTA QKNKETSSSK DKKSVDKKSA
     TENSKQKNGK QEVREPAPCV QPPTVEANAM QTGDKTPKKS EKRRQSLGGF LKGLGPKRMS
     DAQVQTDPVS IGPVGKSK
//
ID   A2AVX1_MOUSE            Unreviewed;       577 AA.
AC   A2AVX1;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   05-OCT-2010, entry version 19.
DE   SubName: Full=Breast carcinoma amplified sequence 1;
GN   Name=Bcas1; ORFNames=RP23-321D1.1-003;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Humphries M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Heath P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL928812; CAM20735.1; -; Genomic_DNA.
DR   EMBL; AL935134; CAM20735.1; JOINED; Genomic_DNA.
DR   EMBL; AL935134; CAM20747.1; -; Genomic_DNA.
DR   EMBL; AL928812; CAM20747.1; JOINED; Genomic_DNA.
DR   IPI; IPI00756676; -.
DR   UniGene; Mm.240850; -.
DR   STRING; A2AVX1; -.
DR   PRIDE; A2AVX1; -.
DR   Ensembl; ENSMUST00000068137; ENSMUSP00000069437; ENSMUSG00000013523.
DR   MGI; MGI:1924210; Bcas1.
DR   HOVERGEN; HBG082347; -.
DR   Bgee; A2AVX1; -.
DR   Genevestigator; A2AVX1; -.
PE   4: Predicted;
SQ   SEQUENCE   577 AA;  61162 MW;  25DC4592E3355DEE CRC64;
     MGNQMSVPLR PGDQEHDPGA DTCKGNPVVL STRVIQHYEE VDLGISSSKD NVATSSPKTM
     EAQAVGDASG KNLGKEAKTK APAARSHFFL TLSRPVPGRP GDQGTDSSAA SGRFDVSPSA
     APENKDPSEH GALPVAAAPG QAPDKTPGCP EAKQQTLPAT GPLAPSPPES QAEAPAQDKD
     FGFLNRFFKL DKGRESAPVN SQPKEAKGSE DPEQATEAPA VPGNPHGVSA GEDIVDSEQR
     GQDVDTLSYS VPGDPEVPGT TKEDPQVVDT TENSSSIMSF FKTLVSPNKT ETKKDPEDTD
     TENSPTTSAN LKSDKANFTP QETRGKTKAT KSCSPPPPPP EPTSEGRDSG KEKAGPTSLP
     LGKLFWKKSV KEDTLSTGAE ENAVCESPVE TVRLEEVESS LQTVDLSEET QPEPTDVKVK
     EESKPRKTPL MAFLRQMSVR SSEGIPRSEE SNVKDSSCQT SNSVEKTPSP PEPEPAGTAQ
     KNKETSSSKD KKSVDKKSAT ENSKQKNGKQ EVREPAPCVQ PPTVEANAMQ TGDKTPKKSE
     KRRQSLGGFL KGLGPKRMSD AQVQTDPVSI GPVGKSK
//
ID   A2AVX2_MOUSE            Unreviewed;       633 AA.
AC   A2AVX2;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   11-JAN-2011, entry version 26.
DE   SubName: Full=Breast carcinoma amplified sequence 1;
GN   Name=Bcas1; ORFNames=RP23-321D1.1-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Humphries M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Heath P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL928812; CAM20736.1; -; Genomic_DNA.
DR   EMBL; AL935134; CAM20736.1; JOINED; Genomic_DNA.
DR   EMBL; AL935134; CAM20748.1; -; Genomic_DNA.
DR   EMBL; AL928812; CAM20748.1; JOINED; Genomic_DNA.
DR   IPI; IPI00944706; -.
DR   RefSeq; NP_084091.2; NM_029815.2.
DR   UniGene; Mm.240850; -.
DR   ProteinModelPortal; A2AVX2; -.
DR   STRING; A2AVX2; -.
DR   Ensembl; ENSMUST00000013667; ENSMUSP00000013667; ENSMUSG00000013523.
DR   GeneID; 76960; -.
DR   KEGG; mmu:76960; -.
DR   CTD; 76960; -.
DR   MGI; MGI:1924210; Bcas1.
DR   HOVERGEN; HBG082347; -.
DR   InParanoid; A2AVX2; -.
DR   OMA; MEISAVA; -.
DR   PhylomeDB; A2AVX2; -.
DR   Bgee; A2AVX2; -.
DR   Genevestigator; A2AVX2; -.
PE   4: Predicted;
SQ   SEQUENCE   633 AA;  67378 MW;  53DBECB3581A245D CRC64;
     MGNQMSVPLR PGDQEHDPGA DTCKVTSDNE CVQNGNPVVL STRVIQHYEE VDLGISSSKD
     NVATSSPKTM EAQAVGDASG KNLGKEAKTK APAARSHFFL TLSRPVPGRP GDQGTDSSAA
     SGRFDVSPSA APENKDPSEH GALPVAAAPG QAPDKTPGCP EAKQQTLPAT GPLAPSPPES
     QAEAPAQDKD FGFLNRFFKL DKGRESAPVN SQPKEAKGSE DPEQATEAPA VPGNPHGVSA
     GEDIVDSEQR GQDVDTLSYS VPGDPEVPGT TKEDPQVVDT TENSSSIMSF FKTLVSPNKT
     ETKKDPEDTK ATKADSVCDG HAAGQKMSET QAKSKKKRLD SPRLGLSFRK LFRHKDTENS
     PTTSANLKSD KANFTPQETR GKTKATKSCS PPPPPPEPTS EGRDSGKEKA GPTSLPLGKL
     FWKKSVKEDT LSTGAEENAV CESPVETVRL EEVESSLQTV DLSEETQPEP TDVKVKEESK
     PRKTPLMAFL RQMSVRSSEG IPRSEESNVK DSSCQTSNSV EKTPSPPEPE PAGTAQKNKE
     TSSSKDKKSV DKKSATENSK QKNGKQEVRE PAPCVQPPTV EANAMQTGDK TPKKSEKRRQ
     SLGGFLKGLG PKRMSDAQVQ TDPVSIGPVG KSK
//
ID   RBGP1_MOUSE             Reviewed;        1064 AA.
AC   A2AWA9; Q5DTN1; Q8BQ32; Q8C8W3; Q8CD74; Q8R312;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 36.
DE   RecName: Full=Rab GTPase-activating protein 1;
DE   AltName: Full=GAP and centrosome-associated protein;
DE   AltName: Full=Rab6 GTPase-activating protein GAPCenA;
GN   Name=Rabgap1; Synonyms=Kiaa4104;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 646-1064 (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryonic spinal ganglion, Embryonic testis, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 733-1064 (ISOFORM 1).
RC   STRAIN=Czech II, and FVB/N; TISSUE=Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May act as a GTPase-activating protein of RAB6A. May
CC       play a role in microtubule nucleation by centrosome. May
CC       participate in a RAB6A-mediated pathway involved in the metaphase-
CC       anaphase transition (By similarity).
CC   -!- SUBUNIT: Interacts with RAB6A and tubulin gamma (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity).
CC       Cytoplasm, cytoskeleton, centrosome (By similarity).
CC       Note=Predominantly cytosolic but also associated with the
CC       centrosome (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=A2AWA9-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=A2AWA9-2; Sequence=VSP_052520, VSP_052521;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=A2AWA9-3; Sequence=VSP_052516, VSP_052517, VSP_052518,
CC                                  VSP_052519;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 PID domain.
CC   -!- SIMILARITY: Contains 1 Rab-GAP TBC domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH26862.1; Type=Erroneous initiation;
CC       Sequence=AAH31714.1; Type=Erroneous initiation;
CC       Sequence=BAC34703.1; Type=Erroneous initiation;
CC       Sequence=BAD90509.1; Type=Erroneous initiation;
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DR   EMBL; AK031315; BAC27344.1; -; mRNA.
DR   EMBL; AK044346; BAC31880.1; -; mRNA.
DR   EMBL; AK051644; BAC34703.1; ALT_INIT; mRNA.
DR   EMBL; AK220489; BAD90509.1; ALT_INIT; mRNA.
DR   EMBL; AL953890; CAM20742.1; -; Genomic_DNA.
DR   EMBL; AL953890; CAM20743.1; -; Genomic_DNA.
DR   EMBL; BC026862; AAH26862.1; ALT_INIT; mRNA.
DR   EMBL; BC031714; AAH31714.1; ALT_INIT; mRNA.
DR   IPI; IPI00227356; -.
DR   IPI; IPI00378156; -.
DR   IPI; IPI00856706; -.
DR   RefSeq; NP_001029132.1; NM_001033960.1.
DR   RefSeq; NP_666233.2; NM_146121.2.
DR   UniGene; Mm.383192; -.
DR   ProteinModelPortal; A2AWA9; -.
DR   SMR; A2AWA9; 533-820, 988-1039.
DR   STRING; A2AWA9; -.
DR   PhosphoSite; A2AWA9; -.
DR   PRIDE; A2AWA9; -.
DR   Ensembl; ENSMUST00000061179; ENSMUSP00000061624; ENSMUSG00000035437.
DR   Ensembl; ENSMUST00000066055; ENSMUSP00000068835; ENSMUSG00000035437.
DR   Ensembl; ENSMUST00000112919; ENSMUSP00000108541; ENSMUSG00000035437.
DR   Ensembl; ENSMUST00000112920; ENSMUSP00000108542; ENSMUSG00000035437.
DR   GeneID; 227800; -.
DR   KEGG; mmu:227800; -.
DR   CTD; 227800; -.
DR   MGI; MGI:2385139; Rabgap1.
DR   HOGENOM; HBG445383; -.
DR   HOVERGEN; HBG063892; -.
DR   InParanoid; A2AWA9; -.
DR   OMA; VVCLESE; -.
DR   OrthoDB; EOG4QC14X; -.
DR   NextBio; 378834; -.
DR   Bgee; A2AWA9; -.
DR   CleanEx; MM_RABGAP1; -.
DR   Genevestigator; A2AWA9; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0005097; F:Rab GTPase activator activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0032313; P:regulation of Rab GTPase activity; IEA:InterPro.
DR   InterPro; IPR022164; Kinesin-like.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   InterPro; IPR000195; RabGAP/TBC_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF12473; DUF3694; 1.
DR   Pfam; PF00640; PID; 1.
DR   Pfam; PF00566; TBC; 1.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; RabGAP_TBC; 2.
DR   PROSITE; PS01179; PID; 1.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell cycle; Coiled coil; Cytoplasm;
KW   Cytoskeleton; GTPase activation; Phosphoprotein.
FT   CHAIN         1   1064       Rab GTPase-activating protein 1.
FT                                /FTId=PRO_0000298780.
FT   DOMAIN      137    293       PID.
FT   DOMAIN      561    747       Rab-GAP TBC.
FT   COILED      805   1038       Potential.
FT   MOD_RES     991    991       Phosphothreonine (By similarity).
FT   VAR_SEQ       1     18       Missing (in isoform 3).
FT                                /FTId=VSP_052516.
FT   VAR_SEQ      19     30       TLNSEDFVLVSR -> MGLSSLSANKPW (in isoform
FT                                3).
FT                                /FTId=VSP_052517.
FT   VAR_SEQ     363    384       ESMGKSSDGKSYVITGSWNPKS -> VRFCCCCCCGLFWLW
FT                                LVFIRNL (in isoform 3).
FT                                /FTId=VSP_052518.
FT   VAR_SEQ     385   1064       Missing (in isoform 3).
FT                                /FTId=VSP_052519.
FT   VAR_SEQ     804    809       ISQKKL -> VQQRLL (in isoform 2).
FT                                /FTId=VSP_052520.
FT   VAR_SEQ     810   1064       Missing (in isoform 2).
FT                                /FTId=VSP_052521.
FT   CONFLICT    646    646       Q -> E (in Ref. 1; BAC34703).
SQ   SEQUENCE   1064 AA;  120798 MW;  8AFAB7C7827F0040 CRC64;
     MDDKASVGKI SVSSDSVSTL NSEDFVLVSR QGDETPSTNN GSDDEKTGLK IVGNGSEQQL
     QKELADVLMD PPMDDQPGER SQLDGEGDGP LSNQLSASST INPVPLVGLP KPEMSLPVKP
     GQGDSEVSSP FTPVADEDSV VFNKLTYLGC ASVNAPRSEV EALRMMSILR SQCQISLDVT
     LSVPNVSEGT VRLLDPQTNT EIANYPIYKI LFCVRGHDGT PESDCFAFTE SHYNAELFRI
     HVFRCEIQEA VSRILYSFAT AFRRSAKQTP LSATAAPQTP DSDIFTFSVS LEIKEDDGKG
     YFSAVPKDKD RQCFKLRQGI DKKIVICVQQ TANKELAIER CFGLLLSPGK DVRNSDMHLL
     DLESMGKSSD GKSYVITGSW NPKSPHFQVV NEETPKDKVL FMTTAVDLVI TEVQEPVRFL
     LETKVRVCSP NERLFWPFSK RSTTENFFLK LKQIKQKEKK NNADTLYEVV CLESESERER
     RKTTASPSVR LPQSGSQSSM IPSPPEDDEE EDNDEPLLSG FGDVSKECAE KILETWGELL
     SKWHLNLSVR PKQLSSLVRS GVPEALRGEV WQLLAGCHNN DHLVEKYRIL ITKESPQDSA
     ITRDINRTFP AHDYFKDTGG DGQDSLYKIC KAYSVYDEEI GYCQGQSFLA AVLLLHMPEE
     QAFSVLVKIM FDYGLRELFK QNFEDLHCKF YQLERLMQEY IPDLYNHFLD ISLEAHMYAS
     QWFLTLFTAK FPLYMVFHII DLLLCEGISV IFNVALGLLK TSKDDLLLTD FEGALKFFRV
     QLPKRYRSEE NAKRLMELAC NTKISQKKLK KFEKEYHTMR EQQAQQEDPI ERFERENRRL
     QEANMRLEQE NDDLAHELVT SKIALRKDLD NAEEKADALN KELLMTKQKL IDAEDEKRRL
     EEESAQLKEM CRRELDKAES EIKKNSSIIG DYKQICSQLS ERLEKQQTAN KVEIEKIRQK
     VDDCDRCRDF FNKEGRVKGI SSAKGVSDED TDEEKETLKN QLREMELELA QTKLQLVEAE
     CKIQDLEHHL GLALSEVQAA KKTWFNRTLS SIKTATGVQG KETC
//
ID   A2AWR2_MOUSE            Unreviewed;       840 AA.
AC   A2AWR2;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 29.
DE   SubName: Full=G protein-coupled receptor 155;
DE   SubName: Full=GPR155 variant 5;
GN   Name=Gpr155; Synonyms=Sp9; ORFNames=RP23-463K8.4-005;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Almeida-King J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=20537985; DOI=10.1016/j.bbrc.2010.05.162;
RA   Trifonov S., Houtani T., Shimizu J.I., Hamada S., Kase M.,
RA   Maruyama M., Sugimoto T.;
RT   "GPR155: Gene organization, multiple mRNA splice variants and
RT   expression in mouse central nervous system.";
RL   Biochem. Biophys. Res. Commun. 398:19-25(2010).
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DR   EMBL; HM161766; ADI43228.1; -; mRNA.
DR   EMBL; AL954713; CAM25137.1; -; Genomic_DNA.
DR   IPI; IPI00622285; -.
DR   UniGene; Mm.480380; -.
DR   ProteinModelPortal; A2AWR2; -.
DR   SMR; A2AWR2; 737-804.
DR   STRING; A2AWR2; -.
DR   Ensembl; ENSMUST00000112044; ENSMUSP00000107675; ENSMUSG00000041762.
DR   Ensembl; ENSMUST00000112045; ENSMUSP00000107676; ENSMUSG00000041762.
DR   MGI; MGI:1915776; Gpr155.
DR   HOVERGEN; HBG057276; -.
DR   Bgee; A2AWR2; -.
DR   Genevestigator; A2AWR2; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR004776; Auxin_eff.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF03547; Mem_trans; 1.
DR   SMART; SM00049; DEP; 1.
DR   PROSITE; PS50186; DEP; 1.
PE   2: Evidence at transcript level;
KW   Receptor.
SQ   SEQUENCE   840 AA;  93128 MW;  20DE5DF313E6B5F5 CRC64;
     MDSYFSAKNS TLAGDMNATW PASHGFNATG DPPSMSITRL FPALLECFGI VLCGYIAGRA
     NIITSTQAKG LGNFVSRFAL PALLFKNMVV LNFSNVDWAF LYSVLIGKAS VFFIVCVLTL
     LVASPESRFS KAGLFPIFAT QSNDFALGYP IVEALYQSTY PEYLQYIYLV APISLMMLNP
     IGFIFCEIQK SKDTQNASQN KAKIVGLGFL RVLQNPIVFM VFVGIAFNFI LDKKIPVYME
     NFLDGLANSF SGSALFYLGL TMVGKIRRLK KSAFVVLTLL ITAKLLVLPL LCREMVELLD
     KGDSVVNHTS LSNYAFLYGV FPVAPGVAIF ATQFNMEVEI ITSGMVISTF VSAPIMYVSA
     WLLTFPTMDA KPLAYAIQNV SFDISIISLV SLTIVCAGMM IWNFVKEKNF VGQILVFVLL
     YSSLYSTYLW TGLLAVSLFL LKKRESVQLP VGIIIISGWG IPALLVGVLL ITGKHNGDSI
     DSAFFYGKEQ MITTAVTLFC SILIAGVSLM CMNRTTQAGH YEGFGQSQNH KPVEPGSTAF
     EENPAPTNEP ELFPSSIPET SCCSCSLGNG ELRCPSIEPV TNSSASGPMP SSFEKTDHCV
     SRCDSQSCIL AQEEEQYLQS GDPQLTRHVL LCLLLIIGLF ANLSSCLWWL FNHETGRLYV
     ELQFFCAVFN FGQGFISFGI FGLDKHLIIL PFKRRLEFLW NNKEAAADRE SPVSEEIKMT
     CQQFVHYHRD LCIRNIVRER RCGAKTSAGT FCGCDLVNWL IEVGLASDRG EAVIYGDRLV
     QGGVIQHITN EYEFRDEYLF YRFLQKSPEQ SPPARTLRDH QEESYKEIGH SSPPSVSPKT
//
ID   A2BG94_MOUSE            Unreviewed;       208 AA.
AC   A2BG94;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 31.
DE   SubName: Full=Novel protein;
GN   Name=Gm6890; Synonyms=EG628518; ORFNames=RP23-459K15.14-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Collins J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BX465196; CAM24961.1; -; Genomic_DNA.
DR   IPI; IPI00828815; -.
DR   RefSeq; NP_001092776.1; NM_001099306.1.
DR   UniGene; Mm.465110; -.
DR   PRIDE; A2BG94; -.
DR   Ensembl; ENSMUST00000114117; ENSMUSP00000109752; ENSMUSG00000079532.
DR   GeneID; 628518; -.
DR   KEGG; mmu:628518; -.
DR   MGI; MGI:3645826; Gm6890.
DR   GeneTree; ENSGT00410000025802; -.
DR   HOGENOM; HBG283636; -.
DR   HOVERGEN; HBG076829; -.
DR   InParanoid; A2BG94; -.
DR   OMA; WTVENIA; -.
DR   OrthoDB; EOG473PT2; -.
DR   NextBio; 420527; -.
DR   Genevestigator; A2BG94; -.
DR   InterPro; IPR015419; EKC/KEOPS_Pcc1.
DR   Pfam; PF09341; Pcc1; 1.
PE   4: Predicted;
SQ   SEQUENCE   208 AA;  22010 MW;  B4C18B4C5E061496 CRC64;
     MQDPVEGLDG RAGLAEGEDS QLRPQAPDAQ ASSQNSATEG DHGNVPRSCP QDSGRPAAPG
     TLATPGSQAA PGSPSPGNTV GSGAAAEEAA VIPHSEQATL VPGRNGDTAS TRNRHLEFSV
     TVPFRTAMEA GMARRSLVAN ARPQQVMVQQ EFTANDSILA VRWTTDDPVL FRISINTFLD
     QLSLVMRNIQ RLEFVAVVKR GRGRSRES
//
ID   ARI1A_MOUSE             Reviewed;        2283 AA.
AC   A2BH40; Q640Q1; Q925Q1;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=AT-rich interactive domain-containing protein 1A;
DE            Short=ARID domain-containing protein 1A;
DE   AltName: Full=BRG1-associated factor 250;
DE            Short=BAF250;
DE   AltName: Full=BRG1-associated factor 250a;
DE            Short=BAF250A;
DE   AltName: Full=Osa homolog 1;
DE   AltName: Full=SWI-like protein;
DE   AltName: Full=SWI/SNF complex protein p270;
DE   AltName: Full=SWI/SNF-related, matrix-associated, actin-dependent regulator of chromatin subfamily F member 1;
GN   Name=Arid1a; Synonyms=Baf250, Baf250a, Osa1, Smarcf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING (ISOFORM
RP   3), TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=21218920; PubMed=11318604; DOI=10.1006/geno.2001.6477;
RA   Kozmik Z., Machon O., Kralova J., Kreslova J., Paces J., Vlcek C.;
RT   "Characterization of mammalian orthologues of the Drosophila osa gene:
RT   cDNA cloning, expression, chromosomal localization, and direct
RT   physical interaction with Brahma chromatin-remodeling complex.";
RL   Genomics 73:140-148(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION BY MASS
RP   SPECTROMETRY, IDENTIFICATION IN THE NBAF AND NPBAF COMPLEXES, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=17640523; DOI=10.1016/j.neuron.2007.06.019;
RA   Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T.,
RA   Wu H., Aebersold R., Graef I.A., Crabtree G.R.;
RT   "An essential switch in subunit composition of a chromatin remodeling
RT   complex during neural development.";
RL   Neuron 55:201-215(2007).
CC   -!- FUNCTION: Involved in transcriptional activation and repression of
CC       select genes by chromatin remodeling (alteration of DNA-nucleosome
CC       topology). Binds DNA non-specifically. Also involved in vitamin D-
CC       coupled transcription regulation via its association with the
CC       WINAC complex, a chromatin-remodeling complex recruited by vitamin
CC       D receptor (VDR), which is required for the ligand-bound VDR-
CC       mediated transrepression of the CYP27B1 gene (By similarity).
CC       Belongs to the neural progenitors-specific chromatin remodeling
CC       complex (npBAF complex) and the neuron-specific chromatin
CC       remodeling complex (nBAF complex). During neural development a
CC       switch from a stem/progenitor to a post-mitotic chromatin
CC       remodeling mechanism occurs as neurons exit the cell cycle and
CC       become committed to their adult state. The transition from
CC       proliferating neural stem/progenitor cells to post-mitotic neurons
CC       requires a switch in subunit composition of the npBAF and nBAF
CC       complexes. As neural progenitors exit mitosis and differentiate
CC       into neurons, npBAF complexes which contain ACTL6A/BAF53A and
CC       PHF10/BAF45A, are exchanged for homologous alternative
CC       ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-
CC       specific complexes (nBAF). The npBAF complex is essential for the
CC       self-renewal/proliferative capacity of the multipotent neural stem
CC       cells. The nBAF complex along with CREST plays a role regulating
CC       the activity of genes essential for dendrite growth.
CC   -!- SUBUNIT: Component of SWI/SNF chromatin remodeling complexes, in
CC       some of which it can be mutually exclusive with ARID1B/BAF250B.
CC       Component of the BAF (SWI/SNF-A) complex, which includes at least
CC       actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2,
CC       SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57,
CC       SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more
CC       of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle
CC       cells, the BAF complex also contains DPF3. Component of the
CC       SWI/SNF-B (PBAF) complex, at least composed of
CC       SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, ACTL6A/BAF53A or
CC       ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B,
CC       perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170,
CC       PB1/BAF180, ARID2/BAF200, ARID1A/BAF250A or ARID1B/BAF250B and
CC       actin. Component of the SWI/SNF Brm complex, at least composed of
CC       SMARCA2/BRM/BAF190B, SMARCB1/BAF47, ACTL6A/BAF53A or
CC       ACTL6B/BAF53B, SMARCE1/BAF57, BAF60 (one or more of
CC       SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C),
CC       SMARCC1/BAF155, SMARCC2/BAF170, ARID1A/BAF250A, SIN3A, HDAC1,
CC       HDAC2, and RBAP4. Component of the SWI/SNF complex Brg1(I), at
CC       least composed of SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
CC       ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, BAF60 (one or more
CC       of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C),
CC       SMARCC1/BAF155, SMARCC2/BAF170, ARID1A/BAF250A, SIN3A, and
CC       probably HDAC2 and RBAP4. Component of the SWI/SNF Brg1(II), at
CC       least composed of SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
CC       ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155,
CC       SMARCC2/BAF170, ARID1A/BAF250A and probably HDAC2 and RBAP4.
CC       Component of a SWI/SNF-like EPAFa complex, at least composed of
CC       SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, ACTL6A/BAF53A, SMARCE1/BAF57,
CC       SMARCD1/BAF60A, SMARCC1/BAF155, SMARCC2/BAF170, BAF250A and
CC       MLLT1/ENL. Component of a SWI/SNF-like complex containing
CC       ARID1A/BAF250A and ARID1B/BAF250B. Interacts through its C-
CC       terminus with SMARCA2/BRM/BAF190B and SMARCA4/BRG1/BAF190A.
CC       Component of the WINAC complex, at least composed of SMARCA2,
CC       SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A,
CC       BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. Interacts with
CC       SMARCC1/BAF155 (By similarity). Component of neural progenitors-
CC       specific chromatin remodeling complex (npBAF complex) composed of
CC       at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A,
CC       SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A,
CC       SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170,
CC       PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-
CC       specific chromatin remodeling complex (nBAF complex) composed of
CC       at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A,
CC       SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A,
CC       SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170,
CC       DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=A2BH40-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2BH40-2; Sequence=VSP_038737, VSP_038739;
CC       Name=3;
CC         IsoId=A2BH40-3; Sequence=VSP_038740;
CC       Name=4;
CC         IsoId=A2BH40-4; Sequence=VSP_038737, VSP_038738, VSP_038739;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in
CC       the testis.
CC   -!- DEVELOPMENTAL STAGE: Expressed ubiquitously throughout the
CC       developing spinal cord, brain and other embryonic tissues at
CC       E10.5-E16.5. In the earlier stages at E9.5 and E10.5, is fairly
CC       ubiquitous though with clearly elevated expression in the progress
CC       zone and lateral mesoderm of limb buds, optic and otic vesicle,
CC       neural tube, and brain. Later on at E11.5 and E12.5, expression
CC       becomes more restricted and is confined to the interdigital area
CC       of limbs, dorsal mes/metencephalon, neocortex, and neural tube.
CC       Expression is seen in the eye lens from E10.5 until E12.5.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 ARID domain.
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DR   EMBL; AF268912; AAK54504.1; -; mRNA.
DR   EMBL; CR751606; CAM20580.1; -; Genomic_DNA.
DR   EMBL; BX537327; CAM20580.1; JOINED; Genomic_DNA.
DR   EMBL; CR925752; CAM20580.1; JOINED; Genomic_DNA.
DR   EMBL; BX537327; CAM25151.1; -; Genomic_DNA.
DR   EMBL; CR751606; CAM25151.1; JOINED; Genomic_DNA.
DR   EMBL; CR925752; CAM25151.1; JOINED; Genomic_DNA.
DR   EMBL; CR925752; CAM27607.1; -; Genomic_DNA.
DR   EMBL; BX537327; CAM27607.1; JOINED; Genomic_DNA.
DR   EMBL; CR751606; CAM27607.1; JOINED; Genomic_DNA.
DR   EMBL; BC082554; AAH82554.1; -; mRNA.
DR   IPI; IPI00127131; -.
DR   IPI; IPI00648459; -.
DR   IPI; IPI00955140; -.
DR   IPI; IPI00955160; -.
DR   RefSeq; NP_001074288.1; NM_001080819.1.
DR   UniGene; Mm.22478; -.
DR   ProteinModelPortal; A2BH40; -.
DR   SMR; A2BH40; 1001-1120.
DR   STRING; A2BH40; -.
DR   PhosphoSite; A2BH40; -.
DR   PRIDE; A2BH40; -.
DR   Ensembl; ENSMUST00000105897; ENSMUSP00000101517; ENSMUSG00000007880.
DR   GeneID; 93760; -.
DR   KEGG; mmu:93760; -.
DR   CTD; 93760; -.
DR   MGI; MGI:1935147; Arid1a.
DR   HOGENOM; HBG403164; -.
DR   HOVERGEN; HBG058196; -.
DR   InParanoid; A2BH40; -.
DR   OMA; PDGSDPT; -.
DR   OrthoDB; EOG437RD2; -.
DR   NextBio; 351643; -.
DR   Bgee; A2BH40; -.
DR   Genevestigator; A2BH40; -.
DR   GO; GO:0071565; C:nBAF complex; IDA:UniProtKB.
DR   GO; GO:0071564; C:npBAF complex; IDA:UniProtKB.
DR   GO; GO:0005625; C:soluble fraction; IDA:MGI.
DR   GO; GO:0016514; C:SWI/SNF complex; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0016563; F:transcription activator activity; ISS:UniProtKB.
DR   GO; GO:0030521; P:androgen receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0030520; P:estrogen receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR001606; ARID/BRIGHT_DNA-bd.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR021906; DUF3518.
DR   Gene3D; G3DSA:1.10.150.60; ARID; 1.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF01388; ARID; 1.
DR   Pfam; PF12031; DUF3518; 1.
DR   SMART; SM00501; BRIGHT; 1.
DR   SUPFAM; SSF46774; ARID; 1.
DR   PROSITE; PS51011; ARID; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Chromatin regulator; DNA-binding;
KW   Neurogenesis; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   2283       AT-rich interactive domain-containing
FT                                protein 1A.
FT                                /FTId=PRO_0000391619.
FT   DOMAIN     1018   1109       ARID.
FT   MOTIF       296    300       LXXLL.
FT   MOTIF      1710   1714       LXXLL.
FT   MOTIF      1965   1969       LXXLL.
FT   MOTIF      2083   2087       LXXLL.
FT   COMPBIAS     16     20       Poly-Pro.
FT   COMPBIAS     38     43       Poly-Ala.
FT   COMPBIAS     53    425       Gly-rich.
FT   COMPBIAS    331    350       Ala-rich.
FT   COMPBIAS    405    612       Gln-rich.
FT   COMPBIAS    999   1002       Poly-Ser.
FT   COMPBIAS   1328   1500       Gln-rich.
FT   COMPBIAS   1545   1644       Pro-rich.
FT   COMPBIAS   1761   1766       Poly-Glu.
FT   COMPBIAS   1773   1778       Poly-Glu.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      77     77       Phosphoserine (By similarity).
FT   MOD_RES     234    234       Phosphoserine (By similarity).
FT   MOD_RES     287    287       Phosphothreonine (By similarity).
FT   MOD_RES     365    365       Phosphoserine (By similarity).
FT   MOD_RES     384    384       Phosphoserine (By similarity).
FT   MOD_RES     605    605       Phosphoserine (By similarity).
FT   MOD_RES     697    697       Phosphoserine (By similarity).
FT   MOD_RES     699    699       Phosphoserine (By similarity).
FT   MOD_RES     703    703       Phosphoserine (By similarity).
FT   MOD_RES     765    765       Phosphoserine (By similarity).
FT   MOD_RES     773    773       Phosphoserine (By similarity).
FT   MOD_RES    1185   1185       Phosphoserine (By similarity).
FT   MOD_RES    1613   1613       N6-acetyllysine (By similarity).
FT   MOD_RES    1756   1756       Phosphoserine (By similarity).
FT   MOD_RES    1903   1903       N6-acetyllysine (By similarity).
FT   MOD_RES    1942   1942       Phosphoserine (By similarity).
FT   VAR_SEQ       1    385       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_038737.
FT   VAR_SEQ    1181   1181       Missing (in isoform 4).
FT                                /FTId=VSP_038738.
FT   VAR_SEQ    1336   1336       Q -> QQQQQR (in isoform 2 and isoform 4).
FT                                /FTId=VSP_038739.
FT   VAR_SEQ    1367   1583       Missing (in isoform 3).
FT                                /FTId=VSP_038740.
FT   CONFLICT    697    697       S -> F (in Ref. 1; AAK54504).
FT   CONFLICT    750    750       D -> E (in Ref. 1; AAK54504).
FT   CONFLICT    758    758       P -> S (in Ref. 1; AAK54504).
FT   CONFLICT    833    833       M -> I (in Ref. 1; AAK54504).
FT   CONFLICT   1011   1011       K -> Q (in Ref. 1; AAK54504).
FT   CONFLICT   1148   1148       P -> H (in Ref. 1; AAK54504).
FT   CONFLICT   1181   1182       SR -> G (in Ref. 1; AAK54504).
FT   CONFLICT   1635   1635       M -> I (in Ref. 1; AAK54504).
FT   CONFLICT   1755   1755       Y -> S (in Ref. 1; AAK54504).
FT   CONFLICT   1795   1795       S -> P (in Ref. 1; AAK54504).
FT   CONFLICT   1799   1799       N -> S (in Ref. 1; AAK54504).
FT   CONFLICT   1929   1929       E -> D (in Ref. 1; AAK54504).
FT   CONFLICT   1956   1956       E -> D (in Ref. 1; AAK54504).
FT   CONFLICT   1974   1974       S -> P (in Ref. 1; AAK54504).
FT   CONFLICT   2233   2233       A -> P (in Ref. 1; AAK54504).
SQ   SEQUENCE   2283 AA;  242092 MW;  0F14BB1372CC4268 CRC64;
     MAAQVAPAAA SSLGNPPPPP SELKKAEQQQ REEAGGEAAA AAAERGEMKA AAGQESEGPA
     VGPPQPLGKE LQDGAESNGG GGGGGAGSGG GPGAEPDLKN SNGNAGPRPA LNNNLPEPPG
     GGGGGGSSSS DGVGAPPHSA AAALPPPAYG FGQAYGRSPS AVAAAAAAVF HQQHGGQQSP
     GLAALQSGGG GGLEPYAGPQ QNSHDHGFPN HQYNSYYPNR SAYPPPPQAY ALSSPRGGTP
     GSGAAAAAGS KPPPSSSASA SSSSSSFAQQ RFGAMGGGGP SAAGGGTPQP TATPTLNQLL
     TSPSSARGYQ GYPGGDYGGG PQDGGAGKGP ADMASQCWGA AAAAAAAAAA VSGGAQQRSH
     HAPMSPGSSG GGGQPLARTP QSSSPMDQMG KMRPQPYGGT NPYSQQQGPP SGPQQGHGYP
     GQPYGSQTPQ RYPMTMQGRA QSAMGSLSYA QQIPPYGQQG PSAYGQQGQT PYYNQQSPHP
     QQQPPYAQQP PSQTPHAQPS YQQQPQTQQP QLQSSQPPYS QQPSQPPHQQ SPTPYPSQQS
     TTQQHPQSQP PYSQPQAQSP YQQQQPQQPA SSSLSQQAAY PQPQPQQSQQ TAYSQQRFPP
     PQELSQDSFG SQASSAPSMT SSKGGQEDMN LSLQSRPSSL PDLSGSIDDL PMGTEGALSP
     GVSTSGISSS QGEQSNPAQS PFSPHTSPHL PGIRGPSPSP VGSPASVAQS RSGPLSPAAV
     PGNQMPPRPP SGQSDSIMHP SMNQSSIAQD RGYMQRNPQM PQYTSPQPGS ALSPRQPSGG
     QMHSGVGSYQ QNSMGSYGPQ GSQYGPQGGY PRQPNYNALP NANYPNAGMA GSMNPMGAGG
     QMHGQPGIPP YGTLPPGRMA HASMGNRPYG PNMANMPPQV GSGMCPPPGG MNRKTQESAV
     AMHVAANSIQ NRPPGYPNMN QGGMMGTGPP YGQGINSMAG MINPQGPPYP MGGTMANNSA
     GMAASPEMMG LGDVKLTPAT KMNNKADGTP KTESKSKKSS SSTTTNEKIT KLYELGGEPE
     RKMWVDRYLA FTEEKAMGMT NLPAVGRKPL DLYRLYVSVK EIGGLTQVNK NKKWRELATN
     LNVGTSSSAA SSLKKQYIQC LYAFECKIER GEDPPPDIFA AADSKKSQPK IQPPSPAGSG
     SMQGPQTPQS TSSSMAEGGD LKPPTPASTP HSQIPPLPGM SRSNSVGIQD AFPDGSDPTF
     QKRNSMTPNP GYQPSMNTSD MMGRMSYEPN KDPYGSMRKA PGSDPFMSSG QGPNGGMGDP
     YSRAAGPGLG SVAMGPRQHY PYGGPYDRVR TEPGIGPEGN MGTGAPQPNL MPSTPDSGMY
     SPSRYPPQQQ QQQQQQHDSY GNQFSTQGTP SSSPFPSQQT TMYQQQQQNY KRPMDGTYGP
     PAKRHEGEMY SVPYSAGQGQ PQQQQLPAAQ SQPASQPQAA QPSPQQDVYN QYSNAYPASA
     TAATDRRPAG GPQNQFPFQF GRDRVSAPPG SSAQQNMPPQ MMGGPIQASA EVAQQGTMWQ
     GRNDMTYNYA NRQNTGSATQ GPAYHGVNRT DEMLHTDQRA NHEGPWPSHG TRQPPYGPSA
     PVPPMTRPPP SNYQPPPSMP NHIPQVSSPA PLPRPMENRT SPSKSPFLHS GMKMQKAGPP
     VPASHIAPTP VQPPMIRRDI TFPPGSVEAT QPVLKQRRRL TMKDIGTPEA WRVMMSLKSG
     LLAESTWALD TINILLYDDN SIMTFNLSQL PGLLELLVEY FRRCLIEIFG ILKEYEVGDP
     GQRTLLDPGR FTKVYSPAHT EEEEEEHLDP KLEEEEEEGV GNDEEMAFLG KDKPSSENNE
     EKLVSKFDKL PVKIVQRNDP FVVDCSDKLG RVQEFDSGLL HWRIGGGDTT EHIQTHFESK
     IELLPSRPYV PCPTPPRKHL TTVEGTPGTT EQEGPPPDGL PEKRITATMD DMLSTRSSTL
     TDEGAKSAEA TKESSKFPFG ISPAQSHRNI KILEDEPHSK DETPLCTLLD WQDSLAKRCV
     CVSNTIRSLS FVPGNDFEMS KHPGLLLILG KLILLHHKHP ERKQAPLTYE KEEEQDQGVS
     CDKVEWWWDC LEMLRENTLV TLANISGQLD LSPYPESICL PVLDGLLHWA VCPSAEAQDP
     FSTLGPNAVL SPQRLVLETL SKLSIQDNNV DLILATPPFS RLEKLYSTMV RFLSDRKNPV
     CREMAVVLLA NLAQGDSLAA RAIAVQKGSI GNLLGFLEDS LAATQFQQSQ ASLLHMQNPP
     FEPTSVDMMR RAARALLALA KVDENHSEFT LYESRLLDIS VSPLMNSLVS QVICDVLFLI
     GQS
//
ID   A2BI30_MOUSE            Unreviewed;      1677 AA.
AC   A2BI30;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   08-MAR-2011, entry version 20.
DE   SubName: Full=Novel protein;
DE   Flags: Fragment;
GN   Name=D430041D05Rik; Synonyms=RP24-297H17.3;
GN   ORFNames=RP24-297H17.3-002;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Almeida-King J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   North P., Leaves N., Greystrong J., Coppola M., Manjunath S.,
RA   Russell E., Smith M., Strachan G., Tofts C., Boal E., Cobley V.,
RA   Hunter G., Kimberley C., Thomas D., Cave-Berry L., Weston P.,
RA   Botcherby M.R.M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL954370; CAM16661.1; -; Genomic_DNA.
DR   EMBL; BX813317; CAM16661.1; JOINED; Genomic_DNA.
DR   EMBL; BX813317; CAM27772.1; -; Genomic_DNA.
DR   EMBL; AL954370; CAM27772.1; JOINED; Genomic_DNA.
DR   IPI; IPI00751337; -.
DR   Ensembl; ENSMUST00000141159; ENSMUSP00000117041; ENSMUSG00000068373.
DR   MGI; MGI:2181743; D430041D05Rik.
DR   HOGENOM; HBG505318; -.
DR   HOVERGEN; HBG107700; -.
DR   InParanoid; A2BI30; -.
DR   OMA; TSWETHS; -.
DR   OrthoDB; EOG4SN1MV; -.
DR   Bgee; A2BI30; -.
DR   Genevestigator; A2BI30; -.
PE   4: Predicted;
FT   NON_TER       1      1
SQ   SEQUENCE   1677 AA;  181022 MW;  B51BBEAF514A755D CRC64;
     SSRKPTLSPE NKPSSLVPPP QPLTTLSQGQ MVHPEAAPGS PLKGTGTPLS LLTVRQPNKD
     HASPAPVPEA PLSREGAHDE YLPDAATQLL SSKLPNPPPT IWTFPQQKED RAAAIFWTNE
     KANGTTSLWA LPTKEAPSRR AVTGSTSDFN TGRLSPLIMT ALRTDLSPPG SPPSSALTTQ
     AASPRSSGTK LESLAAVTSQ SELPASASKQ VTELPSSTDV HGLPTMGGTR KPAATDVFWS
     FLSAETASLA TQSGISGSQQ QTNHDVNTHT INSTHRELRP ASVALPGGTT SAANALQSRN
     FKEIAGQLVA ADSFNFQDPV LSPRTSQPLQ PSEEAVVESH TDFPPTGKHA RDFDTEMVHY
     YSSTSQNPMS QLPIRPAHPF WPTWPSLASA ASLHQMLSDG TDAGSHISSD IYLSPGENGS
     PQFQSVLEYH SSTASPSVPT GAFSRTPSKV LRTSRRPKKW TGAATHTATA AATATTTLFL
     RRSSPAPLSA ALTAKGTGSS SSNLAKSSLT TALAKNVTNK AASGPKVTAG TIHTAFPFTP
     TYMLARTAHS LSTHTAMQGA TGSVSGLLST THLPKKPQAM HTGLPNPTRP DTPRASTPRP
     LTITAALTSM TASVKATRLP SLQTGNTDAA FPAVSTAMAT TGRMASNLDC QMSHKFLVKT
     VFFLTQRRIQ SSESLKLGVT KGLTQALRKA FHQNDVSAHV DILEYSHNVT VGYYATKGRL
     VYLPAVVMDV LGVYGVSNVT ADLKQHTPNL QSVAVLASPW KPQPAGAFQL KTVLQFVSQS
     DNIQSCRFAQ TMEQRLQKAF QDAERKVLST RSNLTVQIVS TSNASQAVTL VYAVGNQSSF
     LNGTVASSLL SQLSAELVGF YLTYPPLTIA EPLEYPNLDT SETTRDYWVI TVLQGVDNSL
     VGLHNQSFAR VMEQRLAQLF MMSQQQGRRF KRATTLGSYT VQMVKMQRVP GPKDPAELTY
     YTLYNGKPLL GTAAAKILST IDSQRMALTL HHVVLLQADP VVKNPPNNLW IIAAVLAPIA
     VVTIIIIIIT AVLCRKNKND FKPDTMINLP QRAKPVQGFD YAKQHLGQQG ADEEVIPVTQ
     ETVVLPIPVR DTPQERDTAQ DGSAIKTAKS TETRRSRSPS ENGSVISNES GKPSSGRRSP
     QNGMTQQKVT KEESRKRNVT ASDEEEGAGL FDSAGKAAAD PFDTSSGSVQ LIAIKPSALP
     VVHPASDRGQ ESSAALNGEV NKALKQKSDI EHYRNKLRLK AKRKGYYDFP PVEAGKGLAE
     RKMYEKAPKE VEHVLDADPE LCAPFAESKN RQQMKNSVYR SRQSLNSPSP GETEMDLLVT
     RERPRRGIRN SGYDTEPEII EETNVDRVHE PRGYGRARQA KGHSETSTLS SQPSIDEVRQ
     QMHMLLEEAF SLASAGHAGQ SRHQETYGST QHLPYSEVVT SAPGTMTRPR AGVQWVPTYR
     PEMYQYSLPR PAYRFSQLPE MVMGSPPPPV PPRTGPVAVA SLRRSTSDIG SKTRMAESTG
     PEPTQLHDSA SFAQVSRGPV SVTQLDQSAL NYSGNTVPAV FAIPAANRPG FTGYFIPTPP
     SSYRSQAWMS YAGENELPSQ WADSVPLPGY IEAYPRSRYQ QSSPSRLPRQ YSQPANLHPS
     LEQAPVPSAA ASQQSLTENE PPDTPLTNIS TAALVKAIRE EVAKLAKKQT DMFEFQV
//
ID   A2CEK3_MOUSE            Unreviewed;       580 AA.
AC   A2CEK3;
DT   20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 36.
DE   SubName: Full=Phosphoglucomutase 2;
GN   Name=Pgm2; ORFNames=RP24-156I23.2-002;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Wallis J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
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DR   EMBL; CR536609; CAM27652.1; -; Genomic_DNA.
DR   IPI; IPI00649253; -.
DR   UniGene; Mm.217764; -.
DR   ProteinModelPortal; A2CEK3; -.
DR   SMR; A2CEK3; 22-580.
DR   STRING; A2CEK3; -.
DR   PRIDE; A2CEK3; -.
DR   Ensembl; ENSMUST00000102783; ENSMUSP00000099844; ENSMUSG00000025791.
DR   MGI; MGI:97565; Pgm2.
DR   eggNOG; roNOG14098; -.
DR   HOGENOM; HBG286308; -.
DR   HOVERGEN; HBG001599; -.
DR   InParanoid; A2CEK3; -.
DR   OMA; HDQKPGT; -.
DR   PhylomeDB; A2CEK3; -.
DR   Bgee; A2CEK3; -.
DR   Genevestigator; A2CEK3; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IDA:MGI.
DR   GO; GO:0006006; P:glucose metabolic process; IDA:MGI.
DR   InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR   InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR   InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR   InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR   InterPro; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase.
DR   Gene3D; G3DSA:3.40.120.10; A-D-PHexomutase_a/b/a-I/II/III; 3.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   Pfam; PF00408; PGM_PMM_IV; 1.
DR   PRINTS; PR00509; PGMPMM.
DR   SUPFAM; SSF53738; A-D-PHexomutase_a/b/a-I/II/III; 2.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   3: Inferred from homology;
KW   Magnesium; Metal-binding.
SQ   SEQUENCE   580 AA;  63747 MW;  25748885AFB43752 CRC64;
     MSDFEEWISG TYRKTEEGPL PLLTFATAPY HDQKPGTSGL RKNTYYFEEK PCYLENFIQS
     IFFSIDLKDR QGSSLVVGGD GRYFNKSAIE TIVQMAAANG IGRLVIGQNG ILSTPAVSCI
     IRKIKAIGGI ILTASHNPGG PNGDFGIKFN ISNGGPAPEA ITDKIFQISK TIEEYAICPD
     LKVDLGVLGK QQFDLENKFK PFTVEIVDSV EAYATMLRNI FDFNALKELL SGPNRLKIRI
     DAMHGVVGPY VKKILCEELG APANSAVNCV PLEDFGGHHP DPNLTYAADL VETMKSGEHD
     FGAAFDGDGD RNMILGKHGF FVNPSDSVAV IAANIFSIPY FQQTGVRGFA RSMPTSGALD
     RVANATKIAL YETPTGWKFF GNLMDASKLS LCGEESFGTG SDHIREKDGL WAVLAWLSIL
     ATRKQSVEDI LKDHWQKFGR NFFTRYDYEE VEAEGANKMM KDLEALMLDR SFVGKQFSAN
     DKVYTVEKAD NFEYSDPVDG SISKNQGLRL IFADGSRIIF RLSGTGSAGA TIRLYIDSYE
     KDVAKINQDP QVMLAPLISI ALKVSQLQER TGRTAPTVIT
//
ID   KALRN_MOUSE             Reviewed;        2964 AA.
AC   A2CG49; A2CG50; A2CG51; A2CG52; A2CG53; B2RXR5; Q3TXY8; Q3TYL1;
AC   Q3UTA5; Q8BTT9; Q8C4Q2; Q9CVA9;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   08-MAR-2011, entry version 47.
DE   RecName: Full=Kalirin;
DE            EC=2.7.11.1;
DE   AltName: Full=Protein Duo;
DE   AltName: Full=Serine/threonine-protein kinase with Dbl- and pleckstrin homology domain;
GN   Name=Kalrn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4; 5 AND 6), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2108-2964 (ISOFORM 2).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Egg, Embryonic head, Stomach, Thymus, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 2034-2042, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1722 AND SER-1771, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1771, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Promotes the exchange of GDP by GTP. Activates specific
CC       Rho GTPase family members, thereby inducing various signaling
CC       mechanisms that regulate neuronal shape, growth, and plasticity,
CC       through their effects on the actin cytoskeleton. Induces
CC       lamellipodia independent of its GEF activity (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SUBUNIT: Interacts with the C-terminal of peptidylglycine alpha-
CC       amidating monooxygenase (PAM) and with the huntingtin-associated
CC       protein 1 (HAP1). Interacts with FASLG (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing, Alternative initiation; Named isoforms=9;
CC       Name=1;
CC         IsoId=A2CG49-1; Sequence=Displayed;
CC         Note=Produced by alternative splicing;
CC       Name=2;
CC         IsoId=A2CG49-2; Sequence=VSP_052576, VSP_052579;
CC         Note=Produced by alternative splicing. No experimental
CC         confirmation available;
CC       Name=3;
CC         IsoId=A2CG49-3; Sequence=VSP_052562;
CC         Note=Produced by alternative splicing. No experimental
CC         confirmation available;
CC       Name=4;
CC         IsoId=A2CG49-4; Sequence=VSP_052563, VSP_052570, VSP_052571,
CC                                  VSP_052573, VSP_052577, VSP_052578;
CC         Note=Produced by alternative splicing. No experimental
CC         confirmation available;
CC       Name=5;
CC         IsoId=A2CG49-5; Sequence=VSP_052564, VSP_052567, VSP_052568,
CC                                  VSP_052569;
CC         Note=Produced by alternative initiation at Met-624 of isoform 1.
CC         Inferred by similarity. Ref.1 (BAE34776) sequence is in conflict
CC         in position: 711:E->K;
CC       Name=6;
CC         IsoId=A2CG49-6; Sequence=VSP_052563, VSP_052570, VSP_052573,
CC                                  VSP_052574, VSP_052575;
CC         Note=Produced by alternative splicing. No experimental
CC         confirmation available;
CC       Name=7;
CC         IsoId=A2CG49-7; Sequence=VSP_052565, VSP_052572;
CC         Note=Produced by alternative splicing;
CC       Name=8;
CC         IsoId=A2CG49-8; Sequence=VSP_052566, VSP_052567, VSP_052568,
CC                                  VSP_052569;
CC         Note=Produced by alternative splicing. No experimental
CC         confirmation available;
CC       Name=9;
CC         IsoId=A2CG49-9; Sequence=VSP_052566, VSP_052568, VSP_052569;
CC         Note=Produced by alternative splicing;
CC   -!- DOMAIN: The two GEF domains catalyze nucleotide exchange for RAC1
CC       and RhoA which are bound by DH1 and DH2 respectively. The two GEF
CC       domains appear to play differing roles in neuronal development and
CC       axonal outgrowth. SH3 1 binds to the first GEF domain inhibiting
CC       GEF activity only when in the presence of a PXXP peptide,
CC       suggesting that the SH3 domain/peptide interaction mediates
CC       binding to GEF1. CRK1 SH3 domain binds to and inhibits GEF1
CC       activity (By similarity).
CC   -!- PTM: Autophosphorylated (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family.
CC   -!- SIMILARITY: Contains 1 CRAL-TRIO domain.
CC   -!- SIMILARITY: Contains 2 DH (DBL-homology) domains.
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 2 SH3 domains.
CC   -!- SIMILARITY: Contains 5 spectrin repeats.
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DR   EMBL; AK008844; BAB25925.1; -; mRNA.
DR   EMBL; AK081504; BAC38239.1; -; mRNA.
DR   EMBL; AK088732; BAC40535.1; -; mRNA.
DR   EMBL; AK139581; BAE24075.1; -; mRNA.
DR   EMBL; AK158544; BAE34552.1; -; mRNA.
DR   EMBL; AK159031; BAE34776.1; -; mRNA.
DR   EMBL; CT010573; CAM18305.1; -; Genomic_DNA.
DR   EMBL; AC154524; CAM18305.1; JOINED; Genomic_DNA.
DR   EMBL; AC155257; CAM18305.1; JOINED; Genomic_DNA.
DR   EMBL; AC165079; CAM18305.1; JOINED; Genomic_DNA.
DR   EMBL; CT010573; CAM18306.1; -; Genomic_DNA.
DR   EMBL; AC154524; CAM18306.1; JOINED; Genomic_DNA.
DR   EMBL; AC165079; CAM18306.1; JOINED; Genomic_DNA.
DR   EMBL; CT010573; CAM18307.1; -; Genomic_DNA.
DR   EMBL; AC154524; CAM18307.1; JOINED; Genomic_DNA.
DR   EMBL; AC154588; CAM18307.1; JOINED; Genomic_DNA.
DR   EMBL; CT010573; CAM18308.1; -; Genomic_DNA.
DR   EMBL; AC154524; CAM18308.1; JOINED; Genomic_DNA.
DR   EMBL; AC154588; CAM18308.1; JOINED; Genomic_DNA.
DR   EMBL; CT010573; CAM18309.1; -; Genomic_DNA.
DR   EMBL; AC154524; CAM18309.1; JOINED; Genomic_DNA.
DR   EMBL; AC154588; CAM18309.1; JOINED; Genomic_DNA.
DR   EMBL; BC157950; AAI57951.1; -; mRNA.
DR   EMBL; BC172101; AAI72101.1; -; mRNA.
DR   IPI; IPI00225550; -.
DR   IPI; IPI00620349; -.
DR   IPI; IPI00653391; -.
DR   IPI; IPI00660519; -.
DR   IPI; IPI00673239; -.
DR   IPI; IPI00762276; -.
DR   IPI; IPI00776346; -.
DR   IPI; IPI00848608; -.
DR   IPI; IPI00851092; -.
DR   RefSeq; NP_001157740.1; NM_001164268.1.
DR   UniGene; Mm.450612; -.
DR   UniGene; Mm.82274; -.
DR   PDB; 1WFW; NMR; -; A=2295-2354.
DR   PDBsum; 1WFW; -.
DR   ProteinModelPortal; A2CG49; -.
DR   SMR; A2CG49; 166-398, 719-977, 1252-1555, 1618-1684, 1890-2219, 2296-2361, 2439-2636, 2649-2943.
DR   PhosphoSite; A2CG49; -.
DR   PRIDE; A2CG49; -.
DR   Ensembl; ENSMUST00000023522; ENSMUSP00000023522; ENSMUSG00000061751.
DR   Ensembl; ENSMUST00000074924; ENSMUSP00000074459; ENSMUSG00000061751.
DR   Ensembl; ENSMUST00000076810; ENSMUSP00000076088; ENSMUSG00000061751.
DR   Ensembl; ENSMUST00000099959; ENSMUSP00000097542; ENSMUSG00000061751.
DR   Ensembl; ENSMUST00000114960; ENSMUSP00000110611; ENSMUSG00000061751.
DR   Ensembl; ENSMUST00000114968; ENSMUSP00000110619; ENSMUSG00000061751.
DR   GeneID; 545156; -.
DR   KEGG; mmu:545156; -.
DR   CTD; 545156; -.
DR   MGI; MGI:2685385; Kalrn.
DR   GeneTree; ENSGT00560000076675; -.
DR   HOVERGEN; HBG108598; -.
DR   OrthoDB; EOG4H462T; -.
DR   BRENDA; 2.7.11.1; 244.
DR   Bgee; A2CG49; -.
DR   CleanEx; MM_KALRN; -.
DR   Genevestigator; A2CG49; -.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR001251; CRAL-bd_TRIO_C.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:3.40.525.10; CRAL_bd_TRIO_C; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 2.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00621; RhoGEF; 2.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF00435; Spectrin; 4.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00325; RhoGEF; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SMART; SM00326; SH3; 2.
DR   SMART; SM00150; SPEC; 7.
DR   SUPFAM; SSF52087; CRAL_TRIO_C; 1.
DR   SUPFAM; SSF48065; DH-domain; 2.
DR   SUPFAM; SSF49265; FN_III-like; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50044; SH3; 2.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
DR   PROSITE; PS50010; DH_2; 2.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative initiation; Alternative splicing;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Disulfide bond; Guanine-nucleotide releasing factor;
KW   Immunoglobulin domain; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Repeat;
KW   Serine/threonine-protein kinase; SH3 domain; Transferase.
FT   CHAIN         1   2964       Kalirin.
FT                                /FTId=PRO_0000308173.
FT   DOMAIN       17    162       CRAL-TRIO.
FT   REPEAT      170    290       Spectrin 1.
FT   REPEAT      292    398       Spectrin 2.
FT   REPEAT      518    624       Spectrin 3.
FT   REPEAT      872    977       Spectrin 4.
FT   REPEAT     1103   1195       Spectrin 5.
FT   DOMAIN     1254   1429       DH 1.
FT   DOMAIN     1441   1553       PH 1.
FT   DOMAIN     1619   1684       SH3 1.
FT   DOMAIN     1900   2075       DH 2.
FT   DOMAIN     2087   2197       PH 2.
FT   DOMAIN     2292   2357       SH3 2.
FT   DOMAIN     2443   2536       Ig-like C2-type.
FT   DOMAIN     2541   2632       Fibronectin type-III.
FT   DOMAIN     2656   2910       Protein kinase.
FT   NP_BIND    2662   2670       ATP (By similarity).
FT   COMPBIAS    664    669       Poly-Gln.
FT   ACT_SITE   2775   2775       Proton acceptor (By similarity).
FT   BINDING    2685   2685       ATP (By similarity).
FT   MOD_RES    1722   1722       Phosphoserine.
FT   MOD_RES    1725   1725       Phosphoserine (By similarity).
FT   MOD_RES    1728   1728       Phosphoserine (By similarity).
FT   MOD_RES    1745   1745       Phosphoserine (By similarity).
FT   MOD_RES    1771   1771       Phosphoserine.
FT   MOD_RES    1789   1789       Phosphoserine (By similarity).
FT   MOD_RES    2208   2208       Phosphoserine (By similarity).
FT   MOD_RES    2233   2233       Phosphoserine (By similarity).
FT   DISULFID   2464   2520       By similarity.
FT   VAR_SEQ       1   2731       Missing (in isoform 3).
FT                                /FTId=VSP_052562.
FT   VAR_SEQ       1   1669       Missing (in isoform 4 and isoform 6).
FT                                /FTId=VSP_052563.
FT   VAR_SEQ       1    623       Missing (in isoform 5).
FT                                /FTId=VSP_052564.
FT   VAR_SEQ       1      4       MVLS -> MNPPEGASEEGGAADSDVDAFFRT (in
FT                                isoform 7).
FT                                /FTId=VSP_052565.
FT   VAR_SEQ       1      4       MVLS -> MTDRFWDQWYLWYLRLLRLLDR (in
FT                                isoform 8 and isoform 9).
FT                                /FTId=VSP_052566.
FT   VAR_SEQ     923    923       E -> ESLFHATSLQ (in isoform 5 and isoform
FT                                8).
FT                                /FTId=VSP_052567.
FT   VAR_SEQ    1617   1636       LSGGCELTVVLQDFSAGHSS -> DGNLVPRWHLGPGDPFS
FT                                TYV (in isoform 5, isoform 8 and isoform
FT                                9).
FT                                /FTId=VSP_052568.
FT   VAR_SEQ    1637   2964       Missing (in isoform 5, isoform 8 and
FT                                isoform 9).
FT                                /FTId=VSP_052569.
FT   VAR_SEQ    1670   1697       QEGLVPSSALCISHSRSSVEMDCFFPLK -> MKGGDQAYT
FT                                RGPSLGWLFAKCCCCFPCR (in isoform 4 and
FT                                isoform 6).
FT                                /FTId=VSP_052570.
FT   VAR_SEQ    1828   1858       Missing (in isoform 4).
FT                                /FTId=VSP_052571.
FT   VAR_SEQ    1859   1898       TLEGGSYRGSLKDPTGCLNEGMTPPTPPRNLEEEQKAKAL
FT                                -> VSGHAGGSSELPLTSVWLPGPQPGPRTGLPHPNFTNRN
FT                                CI (in isoform 7).
FT                                /FTId=VSP_052572.
FT   VAR_SEQ    2285   2285       Missing (in isoform 4 and isoform 6).
FT                                /FTId=VSP_052573.
FT   VAR_SEQ    2357   2364       KATAAAES -> QSQSRGRK (in isoform 6).
FT                                /FTId=VSP_052574.
FT   VAR_SEQ    2365   2964       Missing (in isoform 6).
FT                                /FTId=VSP_052575.
FT   VAR_SEQ    2371   2375       KSCSW -> TLLKP (in isoform 2).
FT                                /FTId=VSP_052576.
FT   VAR_SEQ    2372   2374       SCS -> EPY (in isoform 4).
FT                                /FTId=VSP_052577.
FT   VAR_SEQ    2375   2964       Missing (in isoform 4).
FT                                /FTId=VSP_052578.
FT   VAR_SEQ    2376   2964       Missing (in isoform 2).
FT                                /FTId=VSP_052579.
FT   CONFLICT   1824   1824       Q -> H (in Ref. 1; BAC40535).
FT   CONFLICT   2316   2316       G -> S (in Ref. 1; BAB25925).
FT   CONFLICT   2344   2344       E -> K (in Ref. 1; BAB25925).
FT   CONFLICT   2355   2355       L -> F (in Ref. 1; BAB25925).
FT   STRAND     2296   2298
FT   STRAND     2307   2309
FT   STRAND     2318   2324
FT   STRAND     2330   2334
FT   STRAND     2338   2343
SQ   SEQUENCE   2964 AA;  337000 MW;  76064FE06AA2BD9C CRC64;
     MVLSGSFRND GLKASDVLPI LKEKVAFVSG GRDKRGGPIL TFPARSNHDR IRQEDLRKLV
     TYLASVPSED VCKRGFTVII DMRGSKWDLI KPLLKTLQEA FPAEIHVALI IKPDNFWQKQ
     KTNFGSSKFI FETSMVSVEG LTKLVDPSQL TEEFDGSLDY NHEEWIELRL SLEEFFNSAV
     HLLSRLEDLQ EMLARKEFPV DVEGSRRLID EHTQLKKKVL KAPVEELDRE GQRLLQCIRC
     SDGFSGRNCI PGSADFQSLV PKITSLLDKL HSTRQHLHQM WHVRKLKLDQ CFQLRLFEQD
     AEKMFDWISH NKELFLQSHT EIGVSYQHAL DLQTQHNHFA MNSMNAYVNI NRIMSVASRL
     SEAGHYASQQ IKQISTQLDQ EWKSFAAALD ERSTILAMSA VFHQKAEQFL SGVDAWCKMC
     SEGGLPSEMQ DLELAIHHHQ SLYEQVTQAY TEVSQDGKAL LDVLQRPLSP GNSESLTATA
     NYSKAVHQVL DVVHEVLHHQ RRLESIWQHR KVRLHQRLQL CVFQQDVQQV LDWIENHGEA
     FLSKHTGVGK SLHRARALQK RHDDFEEVAQ NTYTNADKLL EAAEQLAQTG ECDPEEIYKA
     ARHLEVRIQD FVRRVEQRKL LLDMSVSFHT HTKELWTWME DLQKEVLEDV CADSVDAVQE
     LIKQFQQQQT ATLDATLNVI KEGEDLIQQL RSAPPSLGEP TEARDSAMSN NKTPHSSSIS
     HIESVLQQLD DAQVQMEELF HERKIKLDIF LQLRIFEQYT IEVTAELDAW NEDLLRQMND
     FNTEDLTLAE QRLQRHTERK LAMNNMTFEV IQQGQDLHQY IMEVQASGIE LICEKDLDLA
     AQVQELLEFL HEKQHELELN AEQTHKRLEQ CLQLRHLQAE VKQVLGWIRN GESMLNASLV
     NASSLSEAEQ LQREHEQFQL AIEKTHQSAL QVQQKAEALL QAGHYDADAI RECAEKVALH
     WQQLMLKMED RLKLVNASVA FYKTSEQVCS VLESLEQEYR RDEDWCGGRD KLGPAAEMDH
     VIPLLSKHLE QKEAFLKACT LARRNAEVFL KYIHRNNVSM PSVASHTRGP EQQVKAILSE
     LLQRENRVLH FWTLKKRRLD QCQQYVVFER SAKQALDWIQ ETGEYYLSTH TSTGETTEET
     QELLKEYGEF RVPAKQTKEK VKLLIQLADS FVEKGHIHAT EIRKWVTTVD KHYRDFSLRM
     GKYRYSLEKA LGVNTEDNKD LELDIIPASL SDREVKLRDA NHEINEEKRK SARKKEFIMA
     ELLQTEKAYV RDLHECLETY LWEMTSGVEE IPPGILNKEH IIFGNIQEIY DFHNNIFLKE
     LEKYEQLPED VGHCFVTWAD KFQMYVTYCK NKPDSNQLIL EHAGTFFDEI QQRHGLANSI
     SSYLIKPVQR VTKYQLLLKE LLTCCEEGKG ELKDGLEVML SVPKKANDAM HVSMLEGFDE
     NLDVQGELIL QDAFQVWDPK SLIRKGRERH LFLFEISLVF SKEIKDSSGH TKYVYKNKLL
     TSELGVTEHV EGDPCKFALW SGRTPSSDNK TVLKASNIET KQEWIKNIRE VIQERIIHLK
     GALKEPIQLP KTPAKLRNNS KRDGVEDGDS QGDGSSQPDT ISIASRTSQN TVESDKLSGG
     CELTVVLQDF SAGHSSELSI QVGQTVELLE RPSERPGWCL VRTTERSPPQ EGLVPSSALC
     ISHSRSSVEM DCFFPLKDSY SHSSSENGGK SESVAHLQSQ PSLNSIHSSP GPKRSTNTLK
     KWLTSPVRRL NSGKADGNIK KQKKVRDGRK SFDLGSPKPG DETTPQGDSA DEKSKKGWGE
     DEPDEESHTP LPPPMKIFDN DPTQDEMSSL LAARQAPPDV PTAADLVSAI EKLVKNKLTL
     EGGSYRGSLK DPTGCLNEGM TPPTPPRNLE EEQKAKALRG RMFVLNELVQ TEKDYVKDLG
     IVVEGFMKRI EEKGVPEDMR GKEKIVFGNI HQIYDWHKDF FLAELEKCIQ EQDRLAQLFI
     KHERKLHIYV WYCQNKPRSE YIVAEYDAYF EEVKQEINQR LTLSDFLIKP IQRITKYQLL
     LKDFLRYSEK AGLECSDIEK AVELMCLVPK RCNDMMNLGR LQGFEGTLTA QGKLLQQDTF
     YVIELDAGMQ SRTKERRVFL FEQIVIFSEL LRKGSLTPGY MFKRSIKMNY LVLEDNVDGD
     PCKFALMNRE TSERVILQAA NSDIQQAWVQ DINQVLETQR DFLNALQSPI EYQRKERSTA
     VIRSQPPRVP QASPRPYSSG PVGSEKPPKG SSYNPPLPPL KISTSNGSPG FDYHQPGDKF
     DASKQNDLGG CNGTSTMTVI KDYYALKENE ICVSQGEVVQ VLAVNQQNMC LVYQPASDHS
     PAAEGWVPGS ILAPLAKATA AAESSDGSIK KSCSWHTLRM RKRADVENSG KNEATGPRKP
     KDILGNKVSV KETNSSEESE CDDLDPNTSM EILNPNFIQE VAPEFLVPLV DVTCLLGDTV
     LLQCKACGRP KPSITWKGPD QNILDTDNSS ATYTISSCDS GESTLKICNL MPQDSGIYTC
     IAANDHGTAS TSATVKVQGV PAAPNRPIAQ ERSCTSVILR WLPPASTGNC TISGYTVEYR
     EEGSQVWQQS VASTLDTYLV IEDLSPGCPY QFRVSASNPW GISLPSEPSE FVRLPEYDAA
     ADGATISWKE NFDSAYTELN EIGRGRFSIV KKCIHKATRK DVAVKFVSKK MKKKEQAAHE
     AALLQHLQHP QYVTLHDTYE SPTSYILILE LMDDGRLLDY LMNHDELMEE KVAFYIRDIM
     EALQYLHNCR VAHLDIKPEN LLIDLRIPVP RVKLIDLEDA VQISGHFHIH HLLGNPEFAA
     PEVIQGIPVS LGTDIWSIGV LTYVMLSGVS PFLDESKEET CINVCRVDFS FPHEYFCGVS
     NAARDFINVI LQEDFRRRPT AATCLQHPWL QPHNGSYSKI PLDTSRLACF IERRKHQNDV
     RPIPNVKSYI VNRVNQGTSL SHNP
//
ID   A2RRJ6_MOUSE            Unreviewed;      1006 AA.
AC   A2RRJ6;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   SubName: Full=Mib1 protein;
GN   Name=Mib1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC131662; AAI31663.1; -; mRNA.
DR   IPI; IPI00330112; -.
DR   UniGene; Mm.21500; -.
DR   ProteinModelPortal; A2RRJ6; -.
DR   SMR; A2RRJ6; 14-218, 818-858, 865-909, 927-1006.
DR   STRING; A2RRJ6; -.
DR   Ensembl; ENSMUST00000052838; ENSMUSP00000054428; ENSMUSG00000024294.
DR   MGI; MGI:2443157; Mib1.
DR   eggNOG; roNOG08890; -.
DR   HOVERGEN; HBG068386; -.
DR   InParanoid; A2RRJ6; -.
DR   Bgee; A2RRJ6; -.
DR   Genevestigator; A2RRJ6; -.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR   GO; GO:0001947; P:heart looping; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:MGI.
DR   GO; GO:0001841; P:neural tube formation; IMP:MGI.
DR   GO; GO:0007219; P:Notch signaling pathway; IMP:MGI.
DR   GO; GO:0045807; P:positive regulation of endocytosis; IDA:MGI.
DR   GO; GO:0001756; P:somitogenesis; IMP:MGI.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR010606; Mib_Herc2.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR000433; Znf_ZZ.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 2.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00023; Ank; 5.
DR   Pfam; PF06701; MIB_HERC2; 2.
DR   Pfam; PF00569; ZZ; 1.
DR   SMART; SM00248; ANK; 9.
DR   SMART; SM00184; RING; 3.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF48403; ANK; 2.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 6.
DR   PROSITE; PS51416; MIB_HERC2; 2.
DR   PROSITE; PS50089; ZF_RING_2; 3.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   2: Evidence at transcript level;
KW   ANK repeat; Metal-binding; Repeat; Zinc; Zinc-finger.
SQ   SEQUENCE   1006 AA;  110088 MW;  918F9270BE96EE8A CRC64;
     MSNSRNNRVM VEGVGARVVR GPDWKWGKQD GGEGHVGTVR SFESPEEVVV VWDNGTAANY
     RCSGAYDLRI LDSAPTGIKH DGTMCDTCRQ QPIIGIRWKC AECTNYDLCT VCYHGDKHHL
     RHRFYRITTP GSERVLLESR RKSKKITARG IFAGARVVRG VDWQWEDQDG GNGRRGKVTE
     IQDWSASSPH SAAYVLWDNG AKNLYRVGFE GMSDLKCVQD AKGGSFYRDH CPVLGEQNGN
     RNPGGLQIGD LVNIDLDLEI VQSLQHGHGG WTDGMFETLT TTGTVCGIDE DHDIVVQYPS
     GNRWTFNPAV LTKANIVRSG DAAQGAEGGT SQFQVGDLVQ VCYDLERIKL LQRGHGEWAE
     AMLPTLGKVG RVQQIYSDSD LKVEVCGTSW TYNPAAVSKV APAGSAISNA SGERLSQLLK
     KLFETQESGD LNEELVKAAA NGDVAKVEDL LKRPDVDVNG QCAGHTAMQA ASQNGHVDIL
     KLLLKQNVDV EAEDKDGDRA VHHAAFGDEG AVIEVLHRGS ADLNARNKRR QTPLHIAVNK
     GHLQVVKTLL DFGCHPSLQD SEGDTPLHDA ISKKRDDILA VLLEAGADVT ITNNNGFNAL
     HHAALRGNPS AMRVLLSKLP RPWIVDEKKD DGYTALHLAA LNNHVEVAEL LVHQGNANLD
     IQNVNQQTAL HLAVERQHTQ IVRLLVRAGA KLDIQDKDGD TPLHEALRHH TLSQLRQLQD
     MQDVGKVDAA WEPSKNTLIM GLGTQGAEKK SAASIACFLA ANGADLSIRN KKGQSPLDLC
     PDPSLCKALA KCHKEKVSGK VGSRSPSMIS NDSETLEECM VCSDMKRDTL FGPCGHIATC
     SLCSPRVKKC LICKEQVQSR TKIEECVVCS DKKAAVLFQP CGHMCACENC ASLMKKCVQC
     RAVVERRVPF ITCCGGKSSE DPSDEISSGN IPVLQKDKDN TNVNADVQKL QQQLQDIKEQ
     TMCPVCLDRL KNMIFLCGHG TCQLCGDRMS ECPICRKAIE RRILLY
//
ID   A2RS43_MOUSE            Unreviewed;      1069 AA.
AC   A2RS43;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   08-MAR-2011, entry version 35.
DE   SubName: Full=Protocadherin 7;
DE   SubName: Full=Protocadherin 7, isoform CRA_d;
GN   Name=Pcdh7; ORFNames=mCG_9825;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC131967; AAI31968.1; -; mRNA.
DR   EMBL; CH466524; EDL37692.1; -; Genomic_DNA.
DR   IPI; IPI00128022; -.
DR   RefSeq; NP_061234.2; NM_018764.2.
DR   UniGene; Mm.332387; -.
DR   UniGene; Mm.397491; -.
DR   ProteinModelPortal; A2RS43; -.
DR   SMR; A2RS43; 28-146, 262-413, 544-734.
DR   STRING; A2RS43; -.
DR   PRIDE; A2RS43; -.
DR   Ensembl; ENSMUST00000068110; ENSMUSP00000066306; ENSMUSG00000029108.
DR   GeneID; 54216; -.
DR   KEGG; mmu:54216; -.
DR   NMPDR; fig|10090.3.peg.11616; -.
DR   CTD; 54216; -.
DR   MGI; MGI:1860487; Pcdh7.
DR   eggNOG; roNOG13895; -.
DR   HOGENOM; HBG403071; -.
DR   HOVERGEN; HBG053523; -.
DR   InParanoid; A2RS43; -.
DR   OMA; QLRFTVM; -.
DR   OrthoDB; EOG42820V; -.
DR   PhylomeDB; A2RS43; -.
DR   NextBio; 311082; -.
DR   Bgee; A2RS43; -.
DR   Genevestigator; A2RS43; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR013164; Cadherin_N.
DR   InterPro; IPR013585; Protocadherin.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 8.
DR   Pfam; PF00028; Cadherin; 6.
DR   Pfam; PF08266; Cadherin_2; 1.
DR   Pfam; PF08374; Protocadherin; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 7.
DR   SUPFAM; SSF49313; Cadherin; 6.
DR   PROSITE; PS00232; CADHERIN_1; 6.
DR   PROSITE; PS50268; CADHERIN_2; 7.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Membrane; Repeat; Transmembrane;
KW   Transmembrane helix.
SQ   SEQUENCE   1069 AA;  116258 MW;  299E221B3498B6A9 CRC64;
     MLRMRTTGWA RGWCLGCCLL LPLCFSLAAA KQLLRYRLAE EGPADVRIGN VASDLGIVTG
     SGEVTFSLES GSEYLKIDNL TGELSTSERR IDREKLPQCQ MIFDENECFL DFEVSVIGPS
     QSWVDLFEGR VIVLDINDNT PTFPSPVLTL TVEENRPVGT LYLLPTATDR DFGRNGIERY
     ELLQEPGGGG GSGEGRRLGP ADSAPYPGGG GNSASGGGSG GSKRRLDAPE GGGGTSPSGR
     SSVFELQVAD TPDGEKQPQL IVKGALDREQ RDSYELTLRV RDGGDPPRSS QAILRVLITD
     VNDNSPRFEK SVYEADLAEN SAPGTPILQL RATDLDVGVN GQIEYVFGAA TESVRRLLRL
     DETSGWLSVL HRIDREEVNQ LRFTVMARDR GQPPKTDKAT VVLNIKDEND NVPSIEIRKI
     GRIPLKDGVA NVAEDVLVDT PIALVQVSDR DQGENGVVTC TVVGDVPFQL KPASDTEGDQ
     NKKKYFLHTS APLDYETTRE FNVVIVAVDS GSPSLSSNNS LVVKVGDTND NPPVFGQSVV
     EVYFPENNIP GERVATVLAT DADSGKNAEI AYSLDSSVMG TFAIDPDSGD ILVNTVLDRE
     QTDRYEFKVN AKDKGIPVLQ GSTTVIVQVA DKNDNDPKFM QDVFTFYVKE NLQPNSPVGM
     VTVMDADKGR NAEMSLYIEE NSNIFSIEND TGTIYSTMSF DREHQTTYTF RVKAVDGGDP
     PRSATATVSL FVMDENDNAP TVTLPRNISY TLLPPSSNVR TVVATVLATD SDDGINADLN
     YSIVGGNPFK LFEIDSTSGV VSLVGKLTQK HYGLHRLVVQ VNDSGQPSQS TTTLVHVFVN
     ESVSNATVID SQIVRSLHTP LTQDIAGDPS YEISKQRLSI VIGVVAGIMT VILIILIVMM
     ARYCRSKNKN GYEAGKKDHE DFFTPQQHDK SKKPKKDKKN KKSKQPLYSS IVTVEASKPN
     GQRYDSVNEK LSDSPSMGRY RSVNGGPGSP DLARHYKSSS PLPTVQLHPQ SPTAGKKHQA
     VQDLPPANTF VGAGDNISIG SDHCSEYSCQ TSNKYSKQMR VHPYITVFG
//
ID   UH1BL_MOUSE             Reviewed;        1457 AA.
AC   A2RSJ4; B2RQV0; Q8CHD4;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   08-MAR-2011, entry version 26.
DE   RecName: Full=UHRF1-binding protein 1-like;
GN   Name=Uhrf1bp1l; Synonyms=Kiaa0701;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC41445.1; Type=Erroneous initiation;
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CC   -----------------------------------------------------------------------
DR   EMBL; AB093261; BAC41445.1; ALT_INIT; mRNA.
DR   EMBL; BC132134; AAI32135.1; -; mRNA.
DR   EMBL; BC138092; AAI38093.1; -; mRNA.
DR   IPI; IPI00762371; -.
DR   UniGene; Mm.268922; -.
DR   UniGene; Mm.446134; -.
DR   PhosphoSite; A2RSJ4; -.
DR   PRIDE; A2RSJ4; -.
DR   Ensembl; ENSMUST00000020112; ENSMUSP00000020112; ENSMUSG00000019951.
DR   MGI; MGI:2442888; Uhrf1bp1l.
DR   HOGENOM; HBG402959; -.
DR   HOVERGEN; HBG061128; -.
DR   InParanoid; A2RSJ4; -.
DR   OrthoDB; EOG4XD3Q8; -.
DR   NextBio; 342197; -.
DR   Bgee; A2RSJ4; -.
DR   CleanEx; MM_UHRF1BP1L; -.
DR   Genevestigator; A2RSJ4; -.
PE   2: Evidence at transcript level;
KW   Coiled coil; Phosphoprotein.
FT   CHAIN         1   1457       UHRF1-binding protein 1-like.
FT                                /FTId=PRO_0000295720.
FT   COILED     1410   1455       Potential.
FT   MOD_RES     414    414       Phosphoserine (By similarity).
FT   MOD_RES     418    418       Phosphoserine (By similarity).
SQ   SEQUENCE   1457 AA;  161900 MW;  6D58D829A3385209 CRC64;
     MAGIIKKQIL KHLSRFTKNL SPDKINLSTL KGEGELKNLE LDEEVLQNML DLPTWLAISK
     VFCNKASIRI PWTKLKTQPI CLSLDKVIME MSTCEEPRAP NGPSPIATAS GQSEYGFAEK
     VVEGITVSVN SIVIRIGAKA FNASFELSQL RIYSVNAQWE HGDLRFTRIQ DPQRGEVLTF
     KEINWQMIRI EADATQSSHL EIMCAPVRLI TNQSKIRVTL KRRLKDCNVI ATKLVLILDD
     LLWVLTDSQL KAMVQYAKSL SEAIEKSTEQ RKSMAPEPTQ SSTVTSSAQH VKTPQAANAP
     DLSDAIVKLF NDFDVKETSH HLVISHLDLH ICDDIHAKEK ESNRRVSGGA MQLSFTQLTI
     DYYPYHKAGD SCSHWMYFSD ATKTKNGWAN ELLHEFECNV EMLKQAMKDR NLGSPPKSPT
     HASPQHTQTE KDSTLKGTPK TPSVLPQPSK AKLMSSSVVV RLADFNIYQV STAEQCRSSP
     KSMISCNKKS LYLPQEMSAI YIEFTEYYYP DGKDFPIPSP NLYSQLNALQ FTVDERSILW
     LNQFLLDLKQ SLNQFMAVYK LNDSSKSDEH VDIRVDGLML KFVIPSEVKA GCHQDQPHTV
     SIQSSEMIAT NTRHCPNCRH SDLEALCQDF KECDFFSKTY TRFPKSCDSF NLLHPIFQRH
     AHEQDTKMHE VYKGNIIPKL NKNTLKTSAA TDVWAVYFSQ FWIDYEGMKS GKGRPVSFVD
     AFPLSIWICQ PTRYAELQKE FQTCDQVTLN TSQSESSDLA GRMKRKKLLK EYYSTESEPL
     TNGGQRPSSD TFLRFSSSSS DADVHVLVRV HKHVSMQINH YQYLLLLFIH ESLVLLSDTL
     RRDVEAVTGS PASQTSVCVG VLLRSAELAL LLHPVNPTSA LRSPASESGS PLLPDFLPAE
     NGGFLSSKRK QGGSGIHRIR NATLNHMSDN RSMSVDLSHA PLKDPLLFKS ASDTNLQKGT
     SFLDYLSDKH LGKISEDESS GLSHKSGSGE MTSEGSHTKD VASTDSDSVL NYRDGSTRLS
     LDDDGNHNPP SNPVTGKGID AIHSIFRAED FLPEAASLSE NPESSKEEAP PARAPKSQTS
     LSAKSKERCP PSPAPLSVSY KNMKRSASQV SLDTLSLDSM VLEEQAESDG SDSHVLLGKA
     MKRNSNTSCQ SPAESVNTSA NTQTCGEASP DAVSTNSEGT QENRDDLMSV VVFRITGVNG
     EIDIRGEDTE VCLQVNQVTP SQLGNVSLRH YLGNRPVGSD QKAIIHPKSS PEISLRFESG
     PGAVVHSLLA EKNGFLQCHI ENFTTEFLTS SLLNIQHFLE DETVATVMPM KIQVSNTKIN
     LKDDSPRGST VSLQPSPVTV HIDRLVVERS DDGSFHIRDS HLFNTGTDFK DGASSDSVVR
     TRGMCDVRMH SSVTQATQTS PEVPLPSQSA NFLDITREQL MEENECLRQR LAQAKMELAE
     AHSARDELLH QMKRMGL
//
ID   DEN5B_MOUSE             Reviewed;        1274 AA.
AC   A2RSQ0; Q8BII7; Q8BWK2;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 2.
DT   08-MAR-2011, entry version 41.
DE   RecName: Full=DENN domain-containing protein 5B;
DE   AltName: Full=Rab6IP1-like protein;
GN   Name=Dennd5b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-934.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-934.
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1076, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the RAB6IP1 family.
CC   -!- SIMILARITY: Contains 1 dDENN domain.
CC   -!- SIMILARITY: Contains 1 DENN domain.
CC   -!- SIMILARITY: Contains 1 PLAT domain.
CC   -!- SIMILARITY: Contains 2 RUN domains.
CC   -!- SIMILARITY: Contains 1 uDENN domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI32200.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
CC       Sequence=AAI32536.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
CC       Sequence=BAC34394.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
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DR   EMBL; AC132412; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC140327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK050728; BAC34394.1; ALT_SEQ; mRNA.
DR   EMBL; AK052296; BAC34923.1; -; mRNA.
DR   EMBL; BC132199; AAI32200.1; ALT_SEQ; mRNA.
DR   EMBL; BC132535; AAI32536.1; ALT_SEQ; mRNA.
DR   IPI; IPI00845620; -.
DR   RefSeq; NP_796166.2; NM_177192.3.
DR   UniGene; Mm.426874; -.
DR   ProteinModelPortal; A2RSQ0; -.
DR   SMR; A2RSQ0; 722-1050.
DR   PhosphoSite; A2RSQ0; -.
DR   PRIDE; A2RSQ0; -.
DR   Ensembl; ENSMUST00000032458; ENSMUSP00000032458; ENSMUSG00000089845.
DR   Ensembl; ENSMUST00000111557; ENSMUSP00000107182; ENSMUSG00000030313.
DR   GeneID; 320560; -.
DR   KEGG; mmu:320560; -.
DR   NMPDR; fig|10090.3.peg.15602; -.
DR   CTD; 320560; -.
DR   MGI; MGI:2444273; Dennd5b.
DR   eggNOG; roNOG07671; -.
DR   GeneTree; ENSGT00550000074509; -.
DR   HOGENOM; HBG381256; -.
DR   HOVERGEN; HBG059906; -.
DR   InParanoid; A2RSQ0; -.
DR   OMA; DCVMVRN; -.
DR   OrthoDB; EOG4M397P; -.
DR   NextBio; 396971; -.
DR   Bgee; A2RSQ0; -.
DR   Genevestigator; A2RSQ0; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR005112; dDENN.
DR   InterPro; IPR001194; DENN.
DR   InterPro; IPR008976; Lipase_LipOase.
DR   InterPro; IPR001024; LipOase_LH2.
DR   InterPro; IPR004012; Run.
DR   InterPro; IPR005113; uDENN.
DR   Gene3D; G3DSA:2.60.60.20; Lipase_LipOase; 1.
DR   Pfam; PF03455; dDENN; 1.
DR   Pfam; PF02141; DENN; 1.
DR   Pfam; PF01477; PLAT; 1.
DR   Pfam; PF02759; RUN; 2.
DR   Pfam; PF03456; uDENN; 1.
DR   SMART; SM00801; dDENN; 1.
DR   SMART; SM00799; DENN; 1.
DR   SMART; SM00593; RUN; 2.
DR   SMART; SM00800; uDENN; 1.
DR   SUPFAM; SSF49723; Lipase_LipOase; 1.
DR   PROSITE; PS50947; DDENN; 1.
DR   PROSITE; PS50211; DENN; 1.
DR   PROSITE; PS50095; PLAT; 1.
DR   PROSITE; PS50826; RUN; 2.
DR   PROSITE; PS50946; UDENN; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Phosphoprotein; Repeat; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   1274       DENN domain-containing protein 5B.
FT                                /FTId=PRO_0000326532.
FT   TRANSMEM    916    936       Helical; (Potential).
FT   DOMAIN       50    120       UDENN.
FT   DOMAIN      187    375       DENN.
FT   DOMAIN      498    574       dDENN.
FT   DOMAIN      772    932       RUN 1.
FT   DOMAIN      936   1044       PLAT.
FT   DOMAIN     1118   1267       RUN 2.
FT   MOD_RES    1076   1076       Phosphoserine.
FT   CARBOHYD    439    439       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    768    768       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    855    855       N-linked (GlcNAc...) (Potential).
FT   CONFLICT     37     37       E -> G (in Ref. 2; BAC34394).
FT   CONFLICT     83     83       P -> R (in Ref. 2; BAC34923).
FT   CONFLICT    153    153       C -> S (in Ref. 2; BAC34923).
FT   CONFLICT    221    221       P -> Q (in Ref. 2; BAC34923).
FT   CONFLICT    225    225       L -> H (in Ref. 2; BAC34394).
SQ   SEQUENCE   1274 AA;  144629 MW;  A29B06B3AB9FC946 CRC64;
     MSGSSAAPGP GSGSSPAACR FAHYFVLCGI DADSGLEPDE LAGENFDQSP LRRTFKSKVL
     AHYPQNIEWN PFDQDAVNML CMPKGLSFRT QADNKEPQFH SFIITREDGS RTYGFVLTFY
     EEVTSKQICT AMQTLYQMHN AEQYSSVYAS SSCSMDSLAS SIDEGDATSL LKLQRYNSYD
     INRDTLYVSK SICLITPLPF MQACKKFLFQ LHKAVTSQQP PPLPLESYIH NILYEVPLPP
     PGRSLKFYGV YEPVICQRPG PNELPLSDYP LREACELLGL ENLVQVFTCV LLEMQTLLYS
     QDYQRLMTVA EGITTLLFPF QWQHVYVPIL PASLLHFLDA PVPYLMGLQS KEGTDRSKLE
     LPQEANLCFV DIDNHFIELP EEFPQFPNKV DFIQELSEVL LQFGIPPEGS LHSSESATKL
     KNMVLKDLAN DKKNGNVPNN SVSVYELLKG SETIARLQAL AKRTGVTMEK IDLPASLSEK
     EKDLKLQCEE ADLRDSQLNV QLREVFANRF TQMFADYEAF VIQTAQDMES WLTNREQMQN
     FDKASFLSDQ PEPYLPFLSR FIETQMFATF IDNKIMSQWE EKDPLLRVFD SRIEKIRLYN
     VRAPTLRTSI YQKCSSLKEA AQSIEQRLMK MDHTAIHPHL LDMKIGQGKY EQGFFPKLQS
     DVLATGPANN NRWVSRSATA QRRKERLRQS SEHIGLDSDL REKYMQEARS LGKNLRQPKL
     SDLSPAVIAQ TNWKFVEGLL KECRMKTKRM LVEKMGHEAV ELGHGEANIT GLEENTLIAS
     LCDLLERIWS HGLLVKQGKS ALWSHLLQFQ DREEKQEHLT DSPVALGPER RKSDSGVMLP
     TLRVSLIQDM RHIQNMTEIK TDVGRARAWI RLSLEKKLLS QHLKQLLSNQ PLTKKLYKRY
     AFLRCEEERE QFLYHLLSLN AVDYFCFTSV FTTIMIPYRS VIIPIKKLSN AIITSNPWIC
     VSGELGDTGV MQIPKNLLEM TFECQNLGKL TTVQIGHDNS GLLAKWLVDC VMVRNEITGH
     TYRFPCGRWL GKGVDDGSLE RILIGELMTS ASDEDLGKQC RTPPQQKSPT TTRRLSITSL
     TGKPAKPNAG QIQEGIGEAV NNIVKHFHKP EKERGSLTVL LCGENGLVAA LEQVFHHGFK
     SARIFHKNVF IWDFVEKAVA YFETTDQILD NEGDVLIQKP SSKTFCHYVN AINTAPRNIG
     KDGKFQILVC LGTRDHLLPQ WIPLLAECPA ITRMYEENAL LRDHMTVNSL IRILQTIQDF
     TIVLEGSLIK GVDV
//
ID   A2RTH5_MOUSE            Unreviewed;       332 AA.
AC   A2RTH5;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   08-MAR-2011, entry version 31.
DE   SubName: Full=Leucine carboxyl methyltransferase 1;
DE   SubName: Full=Leucine carboxyl methyltransferase 1, isoform CRA_b;
GN   Name=Lcmt1; ORFNames=mCG_20988;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC132507; AAI32508.1; -; mRNA.
DR   EMBL; BC132509; AAI32510.1; -; mRNA.
DR   EMBL; CH466531; EDL17309.1; -; Genomic_DNA.
DR   IPI; IPI00283876; -.
DR   RefSeq; NP_079580.2; NM_025304.3.
DR   UniGene; Mm.260527; -.
DR   ProteinModelPortal; A2RTH5; -.
DR   SMR; A2RTH5; 21-320.
DR   STRING; A2RTH5; -.
DR   PhosphoSite; A2RTH5; -.
DR   PRIDE; A2RTH5; -.
DR   Ensembl; ENSMUST00000033025; ENSMUSP00000033025; ENSMUSG00000030763.
DR   GeneID; 30949; -.
DR   KEGG; mmu:30949; -.
DR   CTD; 30949; -.
DR   MGI; MGI:1353593; Lcmt1.
DR   eggNOG; roNOG08886; -.
DR   HOGENOM; HBG627438; -.
DR   HOVERGEN; HBG052313; -.
DR   InParanoid; A2RTH5; -.
DR   OMA; GCGFDTL; -.
DR   OrthoDB; EOG4TF0KQ; -.
DR   PhylomeDB; A2RTH5; -.
DR   NextBio; 307416; -.
DR   Bgee; A2RTH5; -.
DR   Genevestigator; A2RTH5; -.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR007213; LCM_MeTrfase.
DR   InterPro; IPR021121; LCM_MeTrfase_euk.
DR   InterPro; IPR016651; Leu_CO_MeTrfase_LCTM1.
DR   PANTHER; PTHR13600; LCM_mtfrase; 1.
DR   Pfam; PF04072; LCM; 1.
DR   PIRSF; PIRSF016305; LCM_mtfrase; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; Transferase.
SQ   SEQUENCE   332 AA;  38192 MW;  D638E98A47ECCED0 CRC64;
     MASSSRESSF SSCSSSCDLD DEGVRGTCED ASLCKRFAVS IGYWHDPYIE HLVRQSKERK
     APEINRGYFA RVHGVSQLIK AFLRKTECHC QILNLGAGMD TTFWKLKDEG LLPNKYFEVD
     FPMIVTRKLL TIKSKPLLFR PIMELHPEDT LQMDSHMLDS KRYAIIGADL RDLSELEEKL
     KKCNMNTQLP TLLITECVLV YMTPEQSANL LKWAASSFET AMFINYEQVN MDDRFGQIMI
     ENLRRRSCDL AGVETCKSLE SQKERLLLNG WETASAVNMM ELYSGLPRAE VNRIESLEFL
     DEMELLEQLM RHYCLCWATR GGQELGLKEI TY
//
ID   A2SW42_MOUSE            Unreviewed;      2500 AA.
AC   A2SW42;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   08-MAR-2011, entry version 26.
DE   SubName: Full=Zinc finger protein 462;
GN   Name=Zfp462;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CD-1; TISSUE=Brain;
RX   PubMed=17207666; DOI=10.1016/j.modgep.2006.11.009;
RA   Chang Y.S., Stoykova A., Chowdhury K., Gruss P.;
RT   "Graded expression of Zfp462 in the embryonic mouse cerebral cortex.";
RL   Gene Expr. Patterns 7:405-412(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CD-1; TISSUE=Brain;
RA   Chang Y.-S., Stoykova A., Chowdhury K., Gruss P.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; DQ355518; ABC79685.1; -; mRNA.
DR   IPI; IPI00467729; -.
DR   UniGene; Mm.102904; -.
DR   ProteinModelPortal; A2SW42; -.
DR   SMR; A2SW42; 1865-1942, 2018-2100, 2247-2342.
DR   STRING; A2SW42; -.
DR   PRIDE; A2SW42; -.
DR   Ensembl; ENSMUST00000098070; ENSMUSP00000095677; ENSMUSG00000060206.
DR   MGI; MGI:107690; Zfp462.
DR   eggNOG; roNOG10950; -.
DR   HOGENOM; HBG715580; -.
DR   HOVERGEN; HBG058189; -.
DR   InParanoid; A2SW42; -.
DR   OrthoDB; EOG444KJD; -.
DR   Bgee; A2SW42; -.
DR   Genevestigator; A2SW42; -.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0043392; P:negative regulation of DNA binding; IDA:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 1.
DR   SMART; SM00355; ZnF_C2H2; 34.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   2500 AA;  283373 MW;  AA6B3A2DE2937128 CRC64;
     MEVLQCDGCD FRAPSYEDLK AHIQDVHTAF LQPTDVAEDN DDEPLSGSMN ASNQTEVEFS
     SIKDEFVIAE DLPGQSATAL GSGGYYGHSP GYYGQHITPN PKPTNKFFQC KFCVRYFRSK
     NLLIEHTRKV HGAQAEESPT GPPVPGSLNY NIMMHEGFGK VFSCQFRTYK SPRRARIIKH
     QKMYHKNSLK ESTAPPPAPA PLPDPLVPPV SLQDPCKELP AEVVERSILE SMVKPLTKSR
     GNFCCEWCSY QTPRRERWCD HMMKKHRSMV KILSSIRQQE GPNVSEVQND NEPSPTSNST
     YLSMNAASRE MPNANVSNFR GSMGNSIMRP NSSSTSKFSS SMSYPQMKPK SPHNSGLVNL
     TERSRYGMSD MTNSSADLDT NSMLNDSSSD EDLNEVDSEN GLSVLDHQAS GLSAEQLMGS
     DGNKLLETKG IPFRRFMNRF QCPFCPFLTM HRRSISRHIE NIHLSGKTAV YKCDECPFTC
     KSSLKLGAHK QCHTGTSDWD TVNSQSESLS SSLNEGMVSY ESSSINGRKS GVMLDPLQQQ
     QPPQPPPPLP PPPPPPSQPL QQPPPPPLQS PHQVPPQPQP PPTQQPQPPT QAPPLHPYKC
     TMCSYSTMTL KGLRVHQQHK HSFCDNLPKF EGQPSSLPLE NETDSHPSSS NTVKKSQTSI
     LGLSSKNNFV AKANRKLASD FPLDLSPVKK RTRIDEIASN LQSKINQTKL QEDAIINVED
     DEEEEDDNEV EIEVELDREE EATDPIMEVP TAFSAQQIWA RDASEAQKEP NYRSITHDYT
     ATNGAEIELT LSEDEEDYYG SSASMKDQVS NAALLNTQPA IYGTEPSNEN TDFGDSGRLY
     YCKHCDFNNK SARSVSTHYQ RMHPYIKFSF RYILDPNDHS AVYRCLECYI DYTNFEDLQQ
     HYGEHHPEAM NVLNFDHSDL IYRCRFCSYT SPNVRSLMPH YQRMHPTVKI NNAMIFSSYV
     VEQQEGLNAE SQTLREILNS APKSMATSTP VARGGGLPAT FNKNTPPKTF TPECESQKDP
     SVNTVVVYDC DVCSFASPNM HSVLVHYQKK HPEEKASYFR IQKTMRMVSV DRGSALSQLS
     FEVGAPMSPK MSNMGSPPPP QPPPPDLSIE LYYCKHCSYS NRSVVGVLVH YQKRHPEIKV
     TAKYIRQAPP TAAMMRGAEG LQDSPRPPAP LQLNSSERDC PPVETEMFFC QHCDYGNRTV
     KGVLIHYQKK HRDFKANADV IRQHTATIRS LCDRNQKPAS CVLLPASGME RDKTKLRALK
     CRQCSYTSPY FYALRKHIKK DHPALKATVT SIMRWAFLDG LIEAGYHCEW CIYSHMEPSG
     LLLHYQRRHP EHYVDYTYMA TKLWAGPDPS SPTLTMSAEA KTYRCRDCVF EAVSIWDITN
     HYQAFHPWAM NGDESVLLDI IKEKDGVDKA LLAPEELIGP VNCENSIPNP LPEQEAECPE
     DARLSPEKSI HLASANPAIS STPYQCTVCQ SEYNNLHGLL THYGKKHPGM KVKAADFAQD
     IDINPGAVYK CRHCPYINTR IHGVLTHYQK RHPAIKVTAE DFVHDVEQSA DISQNDVEET
     SRIFKQGYGA YRCKLCPYTH GTLEKLKIHY EKYHNQPEFD VFSPPPPKLP VSLEPEITTE
     VSPSQVSVTE EEVGEDPMST AHFSTSHLVS HTVFRCQLCK YFCSTRKGIA RHYRIKHNNV
     RAQPEGKNNL FKCALCAYTN PIRKGLAAHY QKRHDIDAYY THCLAASRTI SDKPNKVIIP
     SPPKDDSPQL SEELRRAVEK KKCSLCSFQS FSKKGIVSHY MKRHPGVFPK KQHASKLGGY
     FTAVYADEHE KPPLMEEEER SSFERAEVEG EAQDIEWLPF RCIKCFKLSF STAELLCMHY
     TDHHSRDLKR DFVILGSGPR FQNSTFQCKH CDSKLQSIAE LTSHLNIHNE EFQKRAKRQE
     RRKQLLSKQK YADGAFADFK QERPFGHLEE VPKIKERKVV GYKCKFCVEV HPTLRAICNH
     LRKHVQYGSV PAVSAAVKGL RSHERSHLAL AMFTREDKYS CQYCSFVSAF RHNLDRHMQT
     HHGHHKPFRC KLCSFKSSYN SRLKTHILKA HAGEHAYKCS WCSFSTMTIS QLKEHSLKVH
     GKALTLPRPR IVSLLSSHAH PSSQKATPAE EVEDSNDSSY SEPPDVQQQL NHYQSAALAR
     NKSRVSPVPP SGTAAGTEQK AEAVLHCEFC EFSSGYIQSI RRHYRDKHGG KKLFKCKDCS
     FYTGFKSAFT MHVEAGHSAV PEEGPKDLRC PLCLYHTKYK RNMIDHIVLH REERVVPIEV
     CRSKLSKYLQ GVVFRCDKCT FTCSSDESLQ QHIEKHNELK PYKCQLCYYE TKHTEELDTH
     LRDEHKVSRN FELVGRVNLD QLEQMKEKIE SSSSEDEDKD DEMSSKAEDR ELMRFADRGP
     GVNTEKRFPC EFCGRAFSQG SEWERHVLRH GMSLHDTNQV SRNEIHTKEM VEESMQLPSI
     EAKEDDEPIG IDFPLKSETV TICVVAADKS LLEDAEAKNE
//
ID   PALM3_MOUSE             Reviewed;         734 AA.
AC   A2TJV2; Q9CRS0;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   08-MAR-2011, entry version 28.
DE   RecName: Full=Paralemmin-3;
GN   Name=Palm3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Hultqvist G., Neumann N.G., Kilimann M.W.;
RT   "Characterization of paralemmin-3, a new isoform of the paralemmin
RT   protein family implicated in membrane dynamics.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-442.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   IDENTIFICATION.
RX   MEDLINE=21371761; PubMed=11478809; DOI=10.1006/bbrc.2001.5329;
RA   Hu B., Copeland N.G., Gilbert D.J., Jenkins N.A., Kilimann M.W.;
RT   "The paralemmin protein family: identification of paralemmin-2, an
RT   isoform differentially spliced to AKAP2/AKAP-KL, and of palmdelphin, a
RT   more distant cytosolic relative.";
RL   Biochem. Biophys. Res. Commun. 285:1369-1376(2001).
CC   -!- FUNCTION: ATP-binding protein (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane;
CC       Lipid-anchor (By similarity).
CC   -!- PTM: Palmitoylated on Cys-728 and Cys-730 and prenylated on Cys-
CC       731; which is required for membrane association (By similarity).
CC   -!- SIMILARITY: Belongs to the paralemmin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB29393.3; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAB29393.3; Type=Miscellaneous discrepancy; Note=Intron retention;
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DR   EMBL; EF208034; ABM92364.1; -; mRNA.
DR   EMBL; AK014493; BAB29393.3; ALT_SEQ; mRNA.
DR   IPI; IPI00316088; -.
DR   RefSeq; NP_083153.1; NM_028877.1.
DR   UniGene; Mm.250943; -.
DR   PhosphoSite; A2TJV2; -.
DR   PRIDE; A2TJV2; -.
DR   Ensembl; ENSMUST00000055077; ENSMUSP00000051396; ENSMUSG00000047986.
DR   GeneID; 74337; -.
DR   KEGG; mmu:74337; -.
DR   CTD; 74337; -.
DR   MGI; MGI:1921587; Palm3.
DR   eggNOG; roNOG17239; -.
DR   GeneTree; ENSGT00390000009016; -.
DR   HOGENOM; HBG505945; -.
DR   HOVERGEN; HBG108232; -.
DR   InParanoid; A2TJV2; -.
DR   OMA; GQAQARI; -.
DR   OrthoDB; EOG45MN57; -.
DR   NextBio; 340479; -.
DR   Bgee; A2TJV2; -.
DR   Genevestigator; A2TJV2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell membrane; Coiled coil; Cytoplasm; Lipoprotein;
KW   Membrane; Methylation; Nucleotide-binding; Palmitate; Prenylation;
KW   Repeat.
FT   CHAIN         1    731       Paralemmin-3.
FT                                /FTId=PRO_0000332173.
FT   PROPEP      732    734       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000332174.
FT   COILED       19     64       Potential.
FT   COILED       90    116       Potential.
FT   COMPBIAS    318    663       Glu-rich.
FT   MOD_RES     731    731       Cysteine methyl ester (By similarity).
FT   LIPID       728    728       S-palmitoyl cysteine (By similarity).
FT   LIPID       730    730       S-palmitoyl cysteine (By similarity).
FT   LIPID       731    731       S-farnesyl cysteine (By similarity).
SQ   SEQUENCE   734 AA;  78788 MW;  AB071126A771653F CRC64;
     MALQTPVLSP ATPTVMAESA LYRQRLEVIA EKRRLQEEIG AARRELEEEK LRVERLKRKS
     LRERWLMDGA AEGPERPEEP ASKDPQSPEG QAQARIRNLE DSLFSLQSQL QLLQSASTGA
     QHRPAGRPAW RREGPRPLSQ SAMEAAPTAP TDVDKRTSLP DAPVGMSPES PSDPREESIA
     VLPASRPSTE AIGTSSEANG PCPGHSPLPE QLSLGVSSVT KAKGDGAVEV VWAGLRATEN
     SATGPTDVEL EAKVEEVVLE AIGARQGTSS PELPTWVKEG RGVVEVVWEG LGGRDLDVTG
     ESGRDAEATH TSSRRLQEQF EAETCRKEEG ASRDSLEGVG QGGPGVEEGS FIWVERVALS
     EDWEEILMEG LEAPQGAGSA GEPEALIGAQ PRGGEASWEV EKREVEKVEG IEEKGRAEKL
     GAEREDGVAV LPDETQGREE NEAEKVERKD SEGPFPAEIA TDEEKWEVKT TEGEESLEVE
     KGGEAEPVTT EKPLVTEKKP EGSLETERKG SEMPLDQEKD GEGSLDRESK TTEILLDGEI
     GDKSSLDETK GSKKLLDEKT GGEGSLDEEA EGSKKLLDRE ADGIEPFSEV DKTSGAKDDV
     SPEEQGKANE GAEFQAEDAS PPGATVCVQD EPRSEEQGQQ EPEKQEGLVE GAASKPEPCT
     EREGPPGDAT LLLAETPAPE QPVESQPLLH QEASSTNPGD HPAPTYAPAQ QLELAEAKEA
     SGPKQKTCQC CVVM
//
ID   A2VDF4_MOUSE            Unreviewed;       888 AA.
AC   A2VDF4;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   SubName: Full=Glutamate receptor, ionotropic, AMPA3 (Alpha 3);
DE   SubName: Full=Gria3 protein;
GN   Name=Gria3; ORFNames=RP23-471M13.1-001, mCG_51875;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RA   Corby N.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RA   Tracey A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC129855; AAI29856.1; -; mRNA.
DR   EMBL; AL672290; CAQ11290.1; -; Genomic_DNA.
DR   EMBL; AL672232; CAQ11290.1; JOINED; Genomic_DNA.
DR   EMBL; AL672232; CAQ12028.1; -; Genomic_DNA.
DR   EMBL; AL672290; CAQ12028.1; JOINED; Genomic_DNA.
DR   EMBL; CH466570; EDL29035.1; -; Genomic_DNA.
DR   IPI; IPI00131472; -.
DR   UniGene; Mm.327681; -.
DR   ProteinModelPortal; A2VDF4; -.
DR   SMR; A2VDF4; 415-530.
DR   STRING; A2VDF4; -.
DR   Ensembl; ENSMUST00000076349; ENSMUSP00000075687; ENSMUSG00000001986.
DR   NMPDR; fig|10090.3.peg.21465; -.
DR   MGI; MGI:95810; Gria3.
DR   eggNOG; roNOG11549; -.
DR   HOVERGEN; HBG051839; -.
DR   OMA; ASAENRT; -.
DR   PhylomeDB; A2VDF4; -.
DR   Bgee; A2VDF4; -.
DR   Genevestigator; A2VDF4; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0004970; F:ionotropic glutamate receptor activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR019594; Glu_rcpt_Glu/Gly-bd.
DR   InterPro; IPR001320; Iontro_glu_rcpt.
DR   InterPro; IPR001508; NMDA_rcpt.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR   PRINTS; PR00177; NMDARECEPTOR.
DR   SMART; SM00918; Lig_chan-Glu_bd; 1.
DR   SMART; SM00079; PBPe; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Ion transport; Ionic channel;
KW   Ligand-gated ion channel; Membrane; Postsynaptic cell membrane;
KW   Receptor; Synapse; Transmembrane; Transmembrane helix; Transport.
SQ   SEQUENCE   888 AA;  100527 MW;  9F68C5D80E81DC02 CRC64;
     MGQSVLRAVF FLVLGLLGHS HGGFPNTISI GGLFMRNTVQ EHSAFRFAVQ LYNTNQNTTE
     KPFHLNYHVD HLDSSNSFSV TNAFCSQFSR GVYAIFGFYD QMSMNTLTSF CGALHTSFVT
     PSFPTDADVQ FVIQMRPALK GAILSLLGYY KWEKFVYLYD TERGFSILQA IMEAAVQNNW
     QVTARSVGNI KDIQEFRRII EEMDRRQEKR YLIDCEVERI NTILEQVVIL GKHSRGYHYM
     LANLGFTDIV LERVMHGGAN ITGFQIVNNE NPMVQQFIQR WVRLDEREFP EAKNAPLKYT
     SALTHDAILV IAEAFRYLRR QRVDVSRRGS AGDCLANPAV PWSQGIDIER ALKMVQVQGM
     TGNIQFDTYG RRTNYTIDVY EMKVSGSRKA GYWNEYERFV PFSDQQISND SSSSENRTIV
     VTTILESPYV MYKKNHEQLE GNERYEGYCV DLAYEIAKHV RIKYKLSIVG DGKYGARDPE
     TKIWNGMVGE LVYGRADIAV APLTITLVRE EVIDFSKPFM SLGISIMIKK PQKSKPGVFS
     FLDPLAYEIW MCIVFAYIGV SVVLFLVSRF SPYEWHLEDN NEEPRDPQSP PDPPNEFGIF
     NSLWFSLGAF MQQGCDISPR SLSGRIVGGV WWFFTLIIIS SYTANLAAFL TVERMVSPIE
     SAEDLAKQTE IAYGTLDSGS TKEFFRRSKI AVYEKMWSYM KSAEPSVFTK TTADGVARVR
     KSKGKFAFLL ESTMNEYIEQ RKPCDTMKVG GNLDSKGYGV ATPKGSALRT PVNLAVLKLS
     EQGILDKLKN KWWYDKGECG AKDSGSKDKT SALSLSNVAG VFYILVGGLG LAMMVALIEF
     CYKSRAESKR MKLTKNTQNF KPAPATNTQN YATYREGYNV YGTESVKI
//
ID   A2VDF7_MOUSE            Unreviewed;      1057 AA.
AC   A2VDF7;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   08-FEB-2011, entry version 25.
DE   SubName: Full=Slc4a4 protein;
DE   Flags: Fragment;
GN   Name=Slc4a4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC129864; AAI29865.1; -; mRNA.
DR   IPI; IPI00857092; -.
DR   RefSeq; NP_001129732.1; NM_001136260.1.
DR   UniGene; Mm.41044; -.
DR   STRING; A2VDF7; -.
DR   Ensembl; ENSMUST00000156238; ENSMUSP00000121744; ENSMUSG00000060961.
DR   GeneID; 54403; -.
DR   KEGG; mmu:54403; -.
DR   CTD; 54403; -.
DR   MGI; MGI:1927555; Slc4a4.
DR   eggNOG; roNOG04387; -.
DR   GeneTree; ENSGT00560000076851; -.
DR   HOVERGEN; HBG004326; -.
DR   InParanoid; A2VDF7; -.
DR   Bgee; A2VDF7; -.
DR   Genevestigator; A2VDF7; -.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:MGI.
DR   GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
DR   GO; GO:0006885; P:regulation of pH; TAS:MGI.
DR   GO; GO:0006814; P:sodium ion transport; IDA:MGI.
DR   InterPro; IPR011531; HCO3_transpt_C.
DR   InterPro; IPR013769; HCO3_transpt_cyt.
DR   InterPro; IPR003020; HCO3_transpt_euk.
DR   InterPro; IPR003024; Na/HCO3_transpt.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   Gene3D; G3DSA:3.40.1100.10; HCO3_transpt_cyt; 1.
DR   PANTHER; PTHR11453; HCO3_transpt_euk; 1.
DR   Pfam; PF07565; Band_3_cyto; 1.
DR   Pfam; PF00955; HCO3_cotransp; 1.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   PRINTS; PR01232; NAHCO3TRSPRT.
DR   SUPFAM; SSF55804; PTrfase/Anion_transptr; 1.
DR   TIGRFAMs; TIGR00834; ae; 1.
PE   2: Evidence at transcript level;
FT   NON_TER    1057   1057
SQ   SEQUENCE   1057 AA;  118786 MW;  230A4BA9F47B3FB4 CRC64;
     MEDEAVLDRG ASFLKHVCDE EEVEGHHTIY IGVHVPKSYR RRRRHKRKAG HKEKKEKERI
     SENYSDKSDV ENADESSSSI LKPLISPAAE RIRFILGEED DSPAPPQLFT ELDELLAVDG
     QEMEWKETAR WIKFEEKVEQ GGERWSKPHV ATLSLHSLFE LRTCMEKGSI MLDREASSLP
     QLVEMIADHQ IETGLLKPDL KDKVTYTLLR KHRHQTKKSN LRSLADIGKT VSSASRMFSN
     PDNGSPAMTH RNLTSSSLND ISDKPEKDQL KNKFMKKLPR DAEASNVLVG EVDFLDTPFI
     AFVRLQQAVM LGALTEVPVP TRFLFILLGP KGKAKSYHEI GRAIATLMSD EVFHDIAYKA
     KDRHDLIAGI DEFLDEVIVL PPGEWDPTIR IEPPKSLPSS DKRKNMYSGG ENVQMNGDTP
     HDGGHGGGGH GDCEELQRTG RFCGGLIKDI KRKAPFFASD FYDALNIQAL SAILFIYLAT
     VTNAITFGGL LGDATDNMQG VLESFLGTAV SGAIFCLFAG QPLTILSSTG PVLVFERLLF
     NFSKDHNFDY LEFRLWIGLW SAFMCLVLVA TDASFLVQYF TRFTEEGFSS LISFIFIYDA
     FKKMIKLADY YPINSDFKVG YNTHFSCACL PPDPVNLSVS NDTTLAPEDL PTISSTDMYH
     NVTFDWAYLS KKECVKYGGK LVGNNCDFVP DITLMSFILF LGTYTSSMAM KKFKTSRYFP
     TTARKLISDF AIILSILIFC VIDALVGVDT PKLIVPSEFK PTSPNRGWFV PPFGGNPWWV
     CLAAAIPALL VTILIFMDQQ ITAVIVNRKE HKLKKGAGYH LDLFWVAILM VVCSFMALPW
     YVAATVISIA HIDSLKMETE TSAPGEQPKF LGVREQRVTG TLVFILTGLS VFMAPILKFI
     PMPVLYGVFL YMGVASLNGV QFMDRLKLLL MPLKHQPDFI YLRHVPLRRV HLFTFLQVLC
     LALLWILKST VAAIIFPVMI LALVAVRKGM DYLFSQHDLS FLDDVIPEKD KKKKEDEKKK
     KKKKGSLDSD NDDEKDPQHS SNATHHADKI PFLESLG
//
ID   TBC8B_MOUSE             Reviewed;        1114 AA.
AC   A3KGB4; B9EJW4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   08-MAR-2011, entry version 28.
DE   RecName: Full=TBC1 domain family member 8B;
GN   Name=Tbc1d8b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May act as a GTPase-activating protein for Rab family
CC       protein(s).
CC   -!- SIMILARITY: Contains 1 EF-hand domain.
CC   -!- SIMILARITY: Contains 2 GRAM domains.
CC   -!- SIMILARITY: Contains 1 Rab-GAP TBC domain.
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DR   EMBL; AL731648; CAM22209.1; -; Genomic_DNA.
DR   EMBL; AL672243; CAM22209.1; JOINED; Genomic_DNA.
DR   EMBL; AL672243; CAM46132.1; -; Genomic_DNA.
DR   EMBL; AL731648; CAM46132.1; JOINED; Genomic_DNA.
DR   EMBL; BC147581; AAI47582.1; -; mRNA.
DR   IPI; IPI00676513; -.
DR   RefSeq; NP_001074968.1; NM_001081499.2.
DR   UniGene; Mm.275869; -.
DR   ProteinModelPortal; A3KGB4; -.
DR   SMR; A3KGB4; 457-769, 781-905.
DR   PRIDE; A3KGB4; -.
DR   Ensembl; ENSMUST00000096313; ENSMUSP00000094036; ENSMUSG00000042473.
DR   GeneID; 245638; -.
DR   KEGG; mmu:245638; -.
DR   CTD; 245638; -.
DR   MGI; MGI:1918101; Tbc1d8b.
DR   eggNOG; maNOG10200; -.
DR   HOGENOM; HBG447190; -.
DR   HOVERGEN; HBG054142; -.
DR   InParanoid; A3KGB4; -.
DR   OMA; KELFLSC; -.
DR   OrthoDB; EOG4NP72Q; -.
DR   PhylomeDB; A3KGB4; -.
DR   NextBio; 386876; -.
DR   Bgee; A3KGB4; -.
DR   Genevestigator; A3KGB4; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005097; F:Rab GTPase activator activity; IEA:InterPro.
DR   GO; GO:0032313; P:regulation of Rab GTPase activity; IEA:InterPro.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR004182; GRAM.
DR   InterPro; IPR000195; RabGAP/TBC_dom.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF02893; GRAM; 2.
DR   Pfam; PF00566; TBC; 1.
DR   SMART; SM00568; GRAM; 2.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; RabGAP_TBC; 2.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
PE   2: Evidence at transcript level;
KW   GTPase activation; Repeat.
FT   CHAIN         1   1114       TBC1 domain family member 8B.
FT                                /FTId=PRO_0000337184.
FT   DOMAIN      145    212       GRAM 1.
FT   DOMAIN      285    353       GRAM 2.
FT   DOMAIN      486    673       Rab-GAP TBC.
FT   DOMAIN      857    892       EF-hand.
SQ   SEQUENCE   1114 AA;  127893 MW;  38EFAD9B55420628 CRC64;
     MWLKPEEVLL KNALKLWLME RSNEYFVLQR RRGYGEEGGG GLTGLLVGTL DSVLDSTAKV
     APFRILHQTP DSQVYLSIAC GANREEITKH WDWLEQNIMK TLSVFDSNED ITNFVQGKIR
     GLIAEEGKQS FAKEDDPEKF REALLKFEKS FGLPEQEKLV TYYSCSYWRG RVPCQGWLYL
     STNFLSFYSF LLGSEIKLII SWDAISKLEK TSTVILTESI HVCSQGENHY FSMFLHINET
     YLLMEQLANY AIKRLFDKET FDNDPVLDDP LQITKRGLEY RAHSEQFKAF FRLPKEETLK
     EVHECFLWVP FSHFSSHGKM CISENYICFA SQDGNLCSVI IPLREVLAID KTDDSNRSVI
     ISIKGKTAFR FSELKDFEQL VAKLRLKCRA ASTQDDVSTE VAVSSDSTGP SENFEEQPLT
     CPKECSKTVN TEALMTVFHP QNLENLDSKM LKEKMKEQSW NILFSECGRG VSMFRTKKTR
     DLVVRGIPET LRGELWMLFS GAVNDMATNP GYYAEVVEQS LGTSNLATEE IERDLRRSLP
     EHPAFQSDTG ISALRRVLTA YAYRNPKIGY CQAMNILTSV LLLYAKEEEA FWLLVAVCER
     MLPDYFNRRI IGALVDQAVF EELIRDHLPQ LTDHMTDMTF FSSVSLSWFL TLFISVLPIE
     SAVNVVDCFF YDGIKAILQL GLAILDYNLD KLLTCKDDAE AVTALNRFFD NVINKDSPLP
     SNVQQGSNIS NEKSDHTKVD ITDLIKESNE KYGSIRYEDI HSMRCRNRLY VIQTLEETTK
     QNVLRVVSQD VKMSLQELDE LYVIFKKELF ISCYWYLSCP GLKHHDPSLP YLEQYQIDCQ
     QFRVLYHLLS PWAHSANRDS LALWTFRLLD ENSDCLINFK EFSSAIDIMY NGSFTDKLKL
     LFKLHIPPAY TEVMSKTSSK GDELSTEELL YFSQLQVSKP ADEKETESGR NSPEKGKGKI
     DIQAYLSQWQ DELLKKEETI KDLPRMNQSQ FIQFSKTLYN LFHEDPEEES LYQAIAIVTN
     LLLRMEEVGR KLHSPASSAS TARDSGPSEG NAESSVKKDL PSPREEHQWS FAFEQILASL
     LNEPALVRFF ERPLDLKAKL ENAKSSQLRS RTKM
//
ID   A3KGR9_MOUSE            Unreviewed;       347 AA.
AC   A3KGR9;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   05-OCT-2010, entry version 23.
DE   SubName: Full=Histocompatibility 13;
DE   Flags: Fragment;
GN   Name=H13; ORFNames=RP23-35I8.11-003;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Kay M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL845162; CAM46158.1; -; Genomic_DNA.
DR   IPI; IPI00754923; -.
DR   UniGene; Mm.277327; -.
DR   Ensembl; ENSMUST00000079247; ENSMUSP00000078236; ENSMUSG00000019188.
DR   MGI; MGI:95886; H13.
DR   HOVERGEN; HBG024161; -.
DR   Bgee; A3KGR9; -.
DR   Genevestigator; A3KGR9; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   InterPro; IPR006639; Peptidase_A22.
DR   InterPro; IPR007369; Peptidase_A22B_SPP.
DR   PANTHER; PTHR12174; Peptidase_A22B; 1.
DR   Pfam; PF04258; Peptidase_A22B; 2.
DR   SMART; SM00730; PSN; 1.
PE   4: Predicted;
FT   NON_TER     347    347
SQ   SEQUENCE   347 AA;  38175 MW;  64DE9322DE37149C CRC64;
     MDSAVSDPHN GSAEAGTPAN GTTRPPSTPE GIALAYGSLL LMALLPIFFG ALRSVRCARG
     KSSSDMPETI TSRDAARFPI IASCTLLGLY LFFKIFSQEY INLLLSMYFF VLGILALSHT
     ISPFMNKFFP ANFPNRQYQL LFTQGSGENK EEIINYEFDT KDLVCLGLSS VVGVWYLLRK
     VFGTNVMVTV AKSFEAPIKL VFPQDLLEKG LEADNFAMLG LGDIVIPGIF IALLLRFDIS
     LKKNTHTYFY TSFAAYIFGL GLTIFIMHIF KHAQPALLYL VPACIGFPVL VALAKGEVAE
     MFSYESSAVI LPHTPRLTHF PTVSGSPASL ADSMQQKLAG PRRRRPQ
//
ID   RGPA2_MOUSE             Reviewed;        1872 AA.
AC   A3KGS3; A3KGS5; B7ZCU9; Q3TZD9; Q4VA60; Q69ZM8; Q7TQL4; Q8BYP2;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 33.
DE   RecName: Full=Ral GTPase-activating protein subunit alpha-2;
DE   AltName: Full=250 kDa substrate of Akt;
DE            Short=AS250;
DE   AltName: Full=P220;
GN   Name=Ralgapa2; Synonyms=Kiaa1272;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RALGAPB, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=16490346; DOI=10.1016/j.cellsig.2006.01.002;
RA   Gridley S., Chavez J.A., Lane W.S., Lienhard G.E.;
RT   "Adipocytes contain a novel complex similar to the tuberous sclerosis
RT   complex.";
RL   Cell. Signal. 18:1626-1632(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-734 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus, and Inner ear;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 975-1872 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1196-1872 (ISOFORM 1).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1406-1872 (ISOFORM 1).
RC   TISSUE=Pancreatic islet;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373; SER-376; SER-379;
RP   SER-819 AND SER-820, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-819 AND SER-820, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Catalytic subunit of the heterodimeric RalGAP2 complex
CC       which acts as a GTPase activator for the Ras-like small GTPases
CC       RALA and RALB (By similarity).
CC   -!- SUBUNIT: Component of the heterodimeric RalGAP2 complex with
CC       RALGAPB. Heterodimerization is required for activity (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A3KGS3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A3KGS3-2; Sequence=VSP_025251, VSP_025252;
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in testis, pancreas,
CC       lung, thymus, brown fat, and white fat.
CC   -!- SIMILARITY: Contains 1 Rap-GAP domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC30146.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC       Sequence=BAC30146.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact leading to erroneous C-terminus;
CC       Sequence=CAM46007.1; Type=Erroneous gene model prediction;
CC       Sequence=CAM46125.1; Type=Erroneous gene model prediction;
CC       Sequence=CAM46200.1; Type=Erroneous gene model prediction;
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DR   EMBL; AL845273; CAM46125.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL845430; CAM46125.1; JOINED; Genomic_DNA.
DR   EMBL; AL935056; CAM46125.1; JOINED; Genomic_DNA.
DR   EMBL; AL845273; CAX15311.1; -; Genomic_DNA.
DR   EMBL; AL845430; CAX15311.1; JOINED; Genomic_DNA.
DR   EMBL; AL935056; CAX15311.1; JOINED; Genomic_DNA.
DR   EMBL; AL845430; CAM46200.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL845273; CAM46200.1; JOINED; Genomic_DNA.
DR   EMBL; AL935056; CAM46200.1; JOINED; Genomic_DNA.
DR   EMBL; AL845430; CAX15398.1; -; Genomic_DNA.
DR   EMBL; AL845273; CAX15398.1; JOINED; Genomic_DNA.
DR   EMBL; AL935056; CAX15398.1; JOINED; Genomic_DNA.
DR   EMBL; AL935056; CAM46007.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL845273; CAM46007.1; JOINED; Genomic_DNA.
DR   EMBL; AL845430; CAM46007.1; JOINED; Genomic_DNA.
DR   EMBL; AL935056; CAX15696.1; -; Genomic_DNA.
DR   EMBL; AL845273; CAX15696.1; JOINED; Genomic_DNA.
DR   EMBL; AL845430; CAX15696.1; JOINED; Genomic_DNA.
DR   EMBL; AK038838; BAC30146.1; ALT_SEQ; mRNA.
DR   EMBL; AK157932; BAE34270.1; -; mRNA.
DR   EMBL; BC053994; AAH53994.1; -; mRNA.
DR   EMBL; BC096528; AAH96528.1; -; mRNA.
DR   EMBL; AK173140; BAD32418.1; -; mRNA.
DR   IPI; IPI00756343; -.
DR   IPI; IPI00845657; -.
DR   RefSeq; NP_001028520.2; NM_001033348.3.
DR   UniGene; Mm.222310; -.
DR   ProteinModelPortal; A3KGS3; -.
DR   SMR; A3KGS3; 1627-1848.
DR   STRING; A3KGS3; -.
DR   PhosphoSite; A3KGS3; -.
DR   PRIDE; A3KGS3; -.
DR   Ensembl; ENSMUST00000048623; ENSMUSP00000044509; ENSMUSG00000037110.
DR   GeneID; 241694; -.
DR   KEGG; mmu:241694; -.
DR   CTD; 241694; -.
DR   MGI; MGI:3036245; Ralgapa2.
DR   eggNOG; roNOG14655; -.
DR   HOVERGEN; HBG051842; -.
DR   NextBio; 385122; -.
DR   Bgee; A3KGS3; -.
DR   CleanEx; MM_A230067G21RIK; -.
DR   Genevestigator; A3KGS3; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0017123; F:Ral GTPase activator activity; ISS:UniProtKB.
DR   GO; GO:0032859; P:activation of Ral GTPase activity; ISS:UniProtKB.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000331; Rap_GAP.
DR   Pfam; PF02145; Rap_GAP; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50085; RAPGAP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; GTPase activation; Phosphoprotein.
FT   CHAIN         1   1872       Ral GTPase-activating protein subunit
FT                                alpha-2.
FT                                /FTId=PRO_0000286973.
FT   DOMAIN     1634   1842       Rap-GAP.
FT   MOD_RES     373    373       Phosphoserine.
FT   MOD_RES     376    376       Phosphoserine.
FT   MOD_RES     379    379       Phosphoserine.
FT   MOD_RES     486    486       Phosphoserine; by PKB (By similarity).
FT   MOD_RES     696    696       Phosphoserine; by PKB (By similarity).
FT   MOD_RES     715    715       Phosphothreonine; by PKB (By similarity).
FT   MOD_RES     819    819       Phosphoserine.
FT   MOD_RES     820    820       Phosphoserine.
FT   VAR_SEQ    1789   1807       VPFFGPLFDGAIVSGKLLP -> LLLKIEKFHSLGPCSMER
FT                                S (in isoform 2).
FT                                /FTId=VSP_025251.
FT   VAR_SEQ    1808   1872       Missing (in isoform 2).
FT                                /FTId=VSP_025252.
FT   CONFLICT    436    436       Q -> R (in Ref. 2; BAC30146).
FT   CONFLICT    447    447       K -> E (in Ref. 2; BAE34270).
FT   CONFLICT   1511   1511       N -> H (in Ref. 4; AAH53994).
FT   CONFLICT   1727   1727       D -> V (in Ref. 5; BAD32418).
SQ   SEQUENCE   1872 AA;  210288 MW;  CCB0AA23790D863A CRC64;
     MFSRRSHGDV KKSTQKVLDP KKDVLTRLKH LRALLDNVDA SDLKQFFETN YSQIYFIFYE
     NFITLENSLK LKGNNKSQRE ELDSILFLFE KILQFLPERI FFRWHYQSIG STLKKLLHTG
     NSIKIRCEGI RLFLLWLQAL QTNCAEEQVL IFACLVPGFP AVLSSRGPCT LETLINPSPS
     IVDAKIYPEE ITPLLPAISG EKIAEDQTCF FLQILLKYMV IQAASLEWKN KENQDTGFKF
     LFTLFRKYYL PHLFPSFTKL TNIYKPVLEI PHLRPKPVYV TVTRDNETIY STKIPYMAAR
     VVFIKWIVTF FLEKKYLTAT QNTKNGVDVL PKIIQTVGGG AIQEKVPELD GAGSTEQDKS
     HSNSSTLSDR RLSNSSLCSI EEEHRTVYEM VQRILLSTRG YVNFVNEVFR QAFLLPSCEI
     SVTRKVVQVY RKWILQNKPV FMEEPDKKDV AQEDADKLGL SETDSKEASS ESSGHKRSSS
     WGRTYSFTSA MSRGCVTEED NTNVKAGAQA MLQVFLTNAA NVFLLEPCAE VPMLLREQVD
     ASKAVLIIFR RMIMELTMNQ KTWEQMLQIL LRITEAVMQK PKDKHVKDLF AQSLAGLLFR
     TLIVAWIRAN LCVYISRELW DDFLRVLSSL TEWEELITEW SNIMDSLTAV LARTVYGVEM
     TNLPLDKLSE QKEKKQRGKG CILEPQKGTA VGRSFSLSWR SHPDVTEPMR FRSATTSGAP
     GVEKARNTVR QKATEVEEFQ QAESTAAADC DYLVVGQQQV PRSSSTSDIT ERLYSDSSQG
     QKVEHSQNLS SSEPKSVQES KGHVTHEHEG ITMLVRRSSS PAELELKDDL QQAHGRCRQR
     QTSESTGSDT VVGYSNEAEL PVSPWQACEE DPDLSTPTDA VADSDARHWL QLSPTDASNL
     TDSRECLADD CSIIAGGNLT GWHPDSAAVL WRRVLGILGD VNNIQSPKIH AKVFGYLYEL
     WYKLAKIRDN LAISLDNQSS PSPPLLIPPL RMFASWLFKA TTLPNEYKEG KLQAYKLICA
     MMTRRQDVLP NSDFLVHFYL VMHLGLTSED QDVLNTIIKN CSPRFFSLGL PGFSMLVGDF
     ITAAARVLST DMLAAPRSEA LTLLGSLVCF PNTYQEIPLL QSVPEVSDVV TGAEDVKHYL
     INILLKNATE EPNECARCIA ICSLGVWICE ELAQSASHPQ VKDAINVIGV TLKFPNKIVA
     QVACDVLQLL VSYWEKLQMF ETALPRKMAE ILVATIAFLL PSAEYSSVET DKKFIVSLLL
     CLLDWCMALP VSALLHPVST AVLEELHPSR APLLDYIYRV LHCCVCGSST YTQQSHYTLT
     LADLSSTDYD PFLPLANVRN SEPIQYHSSA DLGNLLTVEE EKKRRSVELI PLTARMVMAH
     LVNHLGHYPL SGGPAVLHSL VSENHDNAHV EGTELSSEVF RSPNLQLFVF NDSTLISYLQ
     TPAEGPAGGT SGGSLSDVRV IVRDISGKYS WDGKVLYGPL EGRLAPNGRN PSFQISGWHH
     HTCGPQKDLF NGEEGDDVLD KLLENIGHTS PECLLPSQLN LNEPSPTPCA MNWDQEKAIM
     EVILRQSAQE DEYVQRCNSD SSVTVTSQGQ PSPVEPRGPF YFCRLLLDDL GMNSWDRRKN
     FHLLKKNSKL LRELKNLDSR QCRETHKIAV FYIAEGQEDK CSILANERGS QAYEDFVAGL
     GWEVDLSTHC GFMGGLQRNG STGQTAPYYA TSTVEVIFHV STRMPSDSDD SLTKKLRHLG
     NDEVHIVWSE HSRDYRRGII PTAFGDVSII IYPMKNHMFF ITITKKPEVP FFGPLFDGAI
     VSGKLLPSLI CATCINASRA VKCLIPLYQS FYEERALYLE AIIQNHREVM TFEDFAAQVF
     SPSPSYSVSG TD
//
ID   A3KGU4_MOUSE            Unreviewed;       136 AA.
AC   A3KGU4;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-FEB-2011, entry version 21.
DE   SubName: Full=Spectrin alpha 2;
DE   Flags: Fragment;
GN   Name=Spna2; ORFNames=RP23-443G7.6-006;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Phillimore B.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL928926; CAM46234.1; -; Genomic_DNA.
DR   IPI; IPI00750020; -.
DR   UniGene; Mm.204969; -.
DR   ProteinModelPortal; A3KGU4; -.
DR   STRING; A3KGU4; -.
DR   PRIDE; A3KGU4; -.
DR   Ensembl; ENSMUST00000113741; ENSMUSP00000109370; ENSMUSG00000057738.
DR   MGI; MGI:98386; Spna2.
DR   eggNOG; roNOG13040; -.
DR   GeneTree; ENSGT00600000084396; -.
DR   Bgee; A3KGU4; -.
DR   Genevestigator; A3KGU4; -.
DR   GO; GO:0032437; C:cuticular plate; IDA:MGI.
DR   GO; GO:0005916; C:fascia adherens; IDA:MGI.
DR   GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR   GO; GO:0030018; C:Z disc; IDA:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; IDA:MGI.
DR   GO; GO:0030507; F:spectrin binding; IDA:MGI.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Pfam; PF00435; Spectrin; 1.
DR   SMART; SM00150; SPEC; 1.
PE   4: Predicted;
KW   Repeat.
FT   NON_TER     136    136
SQ   SEQUENCE   136 AA;  16090 MW;  A743318456570D44 CRC64;
     MLSSFRKRRA QKMDPSGVKV LETAEDIQER RQQVLDRYHR FKELSTLRRQ KLEDSYRFQF
     FQRDAEELEK WIQEKLQVAS DENYKDPTNL QGKLQKHQAF EAEVQANSGA IVKLDETGNL
     MISEGHFASE TIRTRL
//
ID   A3KGU7_MOUSE            Unreviewed;      2477 AA.
AC   A3KGU7;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAR-2011, entry version 35.
DE   SubName: Full=Spectrin alpha 2;
GN   Name=Spna2; ORFNames=RP23-443G7.6-004;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Phillimore B.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; AL928926; CAM46237.1; -; Genomic_DNA.
DR   IPI; IPI00757353; -.
DR   RefSeq; NP_001171138.1; NM_001177667.1.
DR   UniGene; Mm.204969; -.
DR   ProteinModelPortal; A3KGU7; -.
DR   SMR; A3KGU7; 2-147, 151-251, 364-571, 967-1025, 1342-1550, 1662-1979, 2092-2205.
DR   STRING; A3KGU7; -.
DR   Ensembl; ENSMUST00000100225; ENSMUSP00000097797; ENSMUSG00000057738.
DR   GeneID; 20740; -.
DR   KEGG; mmu:20740; -.
DR   CTD; 20740; -.
DR   MGI; MGI:98386; Spna2.
DR   HOVERGEN; HBG059266; -.
DR   Bgee; A3KGU7; -.
DR   Genevestigator; A3KGU7; -.
DR   GO; GO:0032437; C:cuticular plate; IDA:MGI.
DR   GO; GO:0005916; C:fascia adherens; IDA:MGI.
DR   GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR   GO; GO:0030018; C:Z disc; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0046982; F:protein heterodimerization activity; IDA:MGI.
DR   GO; GO:0030507; F:spectrin binding; IDA:MGI.
DR   InterPro; IPR018248; EF-hand.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR014837; EF-hand_Ca_insen.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR013315; Spectrin_alpha_SH3.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   Pfam; PF00036; efhand; 1.
DR   Pfam; PF08726; efhand_Ca_insen; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF00435; Spectrin; 20.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR01887; SPECTRNALPHA.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00150; SPEC; 20.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 3.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   Calcium; Repeat; SH3 domain.
SQ   SEQUENCE   2477 AA;  285152 MW;  B1EADFC5F2558FBC CRC64;
     MDPSGVKVLE TAEDIQERRQ QVLDRYHRFK ELSTLRRQKL EDSYRFQFFQ RDAEELEKWI
     QEKLQVASDE NYKDPTNLQG KLQKHQAFEA EVQANSGAIV KLDETGNLMI SEGHFASETI
     RTRLMELHRQ WELLLEKMRE KGIKLLQAQK LVQYLRECED VMDWINDKEA IVTSEELGQD
     LEHVEVLQKK FEEFQTDLAA HEERVNEVSQ FAAKLIQEQH PEEELIKTKQ DEVNAAWQRL
     KGLALQRQGK LFGAAEVQRF NRDVDETIGW IKEKEQLMAS DDFGRDLASV QALLRKHEGL
     ERDLAALEDK VKALCAEADR LQQSHPLSAS QIQVKREELI TNWEQIRTLA AERHARLDDS
     YRLQRFLADF RDLTSWVTEM KALINADELA NDVAGAEALL DRHQEHKGEI DAHEDSFKSA
     DESGQALLAA SHYASDEVRE KLSILSEERT ALLELWELRR QQYEQCMDLQ LFYRDTEQVD
     NWMSKQEAFL LNEDLGDSLD SVEALLKKHE DFEKSLSAQE EKITALDEFA TKLIQNNHYA
     MEDVATRRDA LLSRRNALHE RAMHRRAQLA DSFHLQQFFR DSDELKSWVN EKMKTATDEA
     YKDPSNLQGK VQKHQAFEAE LSANQSRIDA LEKAGQKLID VNHYAKEEVA ARMNEVISLW
     KKLLEATELK GIKLREANQQ QQFNRNVEDI ELWLYEVEGH LASDDYGKDL TNVQNLQKKH
     ALLEADVAAH QDRIDGITIQ ARQFQDAGHF DAENIKKKQE ALVARYEALK EPMVARKQKL
     ADSLRLQQLF RDVEDEETWI REKEPIAAST NRGKDLIGVQ NLLKKHQALQ AEIAGHEPRI
     KAVTQKGNAM VEEGHFAAED VKAKLSELNQ KWEALKAKAS QRRQDLEDSL QAQQYFADAN
     EAESWMREKE PIVGSTDYGK DEDSAEALLK KHEALMSDLS AYGSSIQALR EQAQSCRQQV
     APMDDETGKE LVLALYDYQE KSPREVTMKK GDILTLLNST NKDWWKVEVN DRQGFVPAAY
     VKKLDPAQSA SRENLLEEQG SIALRQGQID NQTRITKEAG SVSLRMKQVE ELYQSLLELG
     EKRKGMLEKS CKKFMLFREA NELQQWITEK EAALTNEEVG ADLEQVEVLQ KKFDDFQKDL
     KANESRLKDI NKVAEDLESE GLMAEEVQAV QQQEVYGAMP RDEADSKTAS PWKSARLMVH
     TVATFNSIKE LNERWRSLQQ LAEERSQLLG SAHEVQRFHR DADETKEWIE EKNQALNTDN
     YGHDLASVQA LQRKHEGFER DLAALGDKVN SLGETAQRLI QSHPESAEDL KEKCTELNQA
     WTSLGKRADQ RKAKLGDSHD LQRFLSDFRD LMSWINGIRG LVSSDELAKD VTGAEALLER
     HQEHRTEIDA RAGTFQAFEQ FGQQLLAHGH YASPEIKEKL DILDQERTDL EKAWVQRRMM
     LDHCLELQLF HRDCEQAENW MAAREAFLNT EDKGDSLDSV EALIKKHEDF DKAINVQEEK
     IAALQAFADQ LIAVDHYAKG DIANRRNEVL DRWRRLKAQM IEKRSKLGES QTLQQFSRDV
     DEIEAWISEK LQTASDESYK DPTNIQLSKL LSKHQKHQAF EAELHANADR IRGVIDMGNS
     LIERGACAGS EDAVKARLAA LADQWQFLVQ KSAEKSQKLK EANKQQNFNT GIKDFDFWLS
     EVEALLASED YGKDLASVNN LLKKHQLLEA DISAHEDRLK DLNSQADSLM TSSAFDTSQV
     KEKRDTINGR FQKIKSMATS RRAKLSESHR LHQFFRDMDD EESWIKEKKL LVSSEDYGRD
     LTGVQNLRKK HKRLEAELAA HEPAIQGVLD TGKKLSDDNT IGQEEIQQRL AQFVEHWKEL
     KQLAAARGQR LEESLEYQQF VANVEEEEAW INEKMTLVAS EDYGDTLAAI QGLLKKHEAF
     ETDFTVHKDR VNDVCTNGQD LIKKNNHHEE NISSKMKGLN GKVSDLEKAA AQRKAKLDEN
     SAFLQFNWKA DVVESWIGEK ENSLKTDDYG RDLSSVQTLL TKQETFDAGL QAFQQEGIAN
     ITALKDQLLA AKHIQSKAIE ARHASLMKRW TQLLANSATR KKKLLEAQSH FRKVEDLFLT
     FAKKASAFNS WFENAEEDLT DPVRCNSLEE IKALREAHDA FRSSLSSAQA DFNQLAELDR
     QIKSFRVASN PYTWFTMEAL EETWRNLQKI IKERELELQK EQRRQEENDK LRQEFAQHAN
     AFHQWIQETR TYLLDGSCMV EESGTLESQL EATKRKHQEI RAMRSQLKKI EDLGAAMEEA
     LILDNKYTEH STVGLAQQWD QLDQLGMRMQ HNLEQQIQAR NTTGVTEEAL KEFSMMFKHF
     DKDKSGRLNH QEFKSCLRSL GYDLPMVEEG EPDPEFEAIL DTVDPNRDGH VSLQEYMAFM
     ISRETENVKS SEEIESAFRA LSSEGKPYVT KEELYQNLTR EQADYCVSHM KPYVDGKGRE
     LPTAFDYVEF TRSLFVN
//
ID   ODFP2_MOUSE             Reviewed;         830 AA.
AC   A3KGV1; A3KGV5; A3KGV6; O35135; O35496; Q3TH68; Q3UP80; Q6PGI6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   30-NOV-2010, entry version 32.
DE   RecName: Full=Outer dense fiber protein 2;
DE   AltName: Full=84 kDa outer dense fiber protein;
DE   AltName: Full=Cenexin;
DE   AltName: Full=Outer dense fiber of sperm tails protein 2;
GN   Name=Odf2; Synonyms=Odf84;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 7), TISSUE SPECIFICITY, AND
RP   ALTERNATIVE SPLICING.
RC   TISSUE=Sperm;
RX   MEDLINE=98411040; PubMed=9740324;
RX   DOI=10.1002/(SICI)1098-2795(199810)51:2<167::AID-MRD6>3.0.CO;2-O;
RA   Hoyer-Fender S., Petersen C., Brohmann H., Rhee K., Wolgemuth D.J.;
RT   "Mouse Odf2 cDNAs consist of evolutionary conserved as well as highly
RT   variable sequences and encode outer dense fiber proteins of the sperm
RT   tail.";
RL   Mol. Reprod. Dev. 51:167-175(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   TISSUE SPECIFICITY, AND INTERACTION WITH ODF1.
RX   PubMed=9045620; DOI=10.1074/jbc.272.10.6105;
RA   Shao X., Tarnasky H.A., Schalles U., Oko R., van der Hoorn F.A.;
RT   "Interactional cloning of the 84-kDa major outer dense fiber protein
RT   Odf84. Leucine zippers mediate associations of Odf84 and Odf27.";
RL   J. Biol. Chem. 272:6105-6113(1997).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15852003; DOI=10.1038/ncb1251;
RA   Ishikawa H., Kubo A., Tsukita S., Tsukita S.;
RT   "Odf2-deficient mother centrioles lack distal/subdistal appendages and
RT   the ability to generate primary cilia.";
RL   Nat. Cell Biol. 7:517-524(2005).
CC   -!- FUNCTION: Seems to be a major component of sperm tail outer dense
CC       fibers (ODF). ODFs are filamentous structures located on the
CC       outside of the axoneme in the midpiece and principal piece of the
CC       mammalian sperm tail and may help to maintain the passive elastic
CC       structures and elastic recoil of the sperm tail. May have a
CC       modulating influence on sperm motility. Functions as a general
CC       scaffold protein that is specifically localized at the
CC       distal/subdistal appendages of mother centrioles. Component of the
CC       centrosome matrix required for the localization of PLK1 and NIN to
CC       the centrosomes. Required for the formation and/or maintenance of
CC       normal CETN1 assembly (By similarity).
CC   -!- SUBUNIT: Self-associates. Associates with microtubules and forms a
CC       fibrillar structure partially linked to the microtubule network.
CC       Interacts via its C-terminus with PLK1. Interacts with ODF1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome. Cell
CC       projection, cilium. Cytoplasm, cytoskeleton, centrosome,
CC       centriole. Cytoplasm, cytoskeleton, spindle pole. Note=Localized
CC       at the microtubule organizing centers in interphase and spindle
CC       poles in mitosis. Localized at the distal/subdistal appendages of
CC       mother centrioles.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=1;
CC         IsoId=A3KGV1-1; Sequence=Displayed;
CC         Note=Gene prediction based on EST data;
CC       Name=2;
CC         IsoId=A3KGV1-2; Sequence=VSP_027672, VSP_027673;
CC         Note=Gene prediction based on EST data;
CC       Name=3;
CC         IsoId=A3KGV1-3; Sequence=VSP_027672;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=A3KGV1-4; Sequence=VSP_027672, VSP_027674;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=A3KGV1-5; Sequence=VSP_027672, VSP_027675, VSP_027676;
CC         Note=No experimental confirmation available;
CC       Name=6; Synonyms=ODF2/2;
CC         IsoId=A3KGV1-6; Sequence=VSP_027673, VSP_027675, VSP_027676;
CC       Name=7; Synonyms=ODF2/1;
CC         IsoId=A3KGV1-7; Sequence=VSP_027671, VSP_027675, VSP_027676;
CC   -!- TISSUE SPECIFICITY: Testis-specific (at protein level). Expressed
CC       in spermatids at tubular stage V of the spermatogenic cycle.
CC       Highly expressed in the cytoplasm of elongating spermatids
CC       (tubular stages X/XI). In step 14/15 spermatids of tubular stage
CC       III/IV low expression detected. No expression detected in other
CC       testicular cells as well as the early round of spermatids.
CC   -!- PTM: Tyrosine phosphorylated (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Null mutations in F9 embryonic carcinoma
CC       cells eliminated distal/subdistal appendages and prevented primary
CC       cilium formation. Loss of ODF2 also disrupted two mother
CC       centriole-specific NIN dots, while leaving one dot on the proximal
CC       end of mother and daughter centrioles.
CC   -!- SIMILARITY: Belongs to the ODF2 family.
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DR   EMBL; AF000968; AAB65157.1; -; mRNA.
DR   EMBL; AF034105; AAB87525.1; -; mRNA.
DR   EMBL; AK143726; BAE25517.1; -; mRNA.
DR   EMBL; AK168415; BAE40330.1; -; mRNA.
DR   EMBL; AL928926; CAM46225.1; -; Genomic_DNA.
DR   EMBL; AL928926; CAM46226.1; -; Genomic_DNA.
DR   EMBL; AL928926; CAM46229.1; -; Genomic_DNA.
DR   EMBL; AL928926; CAM46230.1; -; Genomic_DNA.
DR   EMBL; AL928926; CAM46231.1; -; Genomic_DNA.
DR   EMBL; AL928926; CAM46232.1; -; Genomic_DNA.
DR   EMBL; BC057001; AAH57001.1; -; mRNA.
DR   IPI; IPI00130958; -.
DR   IPI; IPI00420925; -.
DR   IPI; IPI00750945; -.
DR   IPI; IPI00753993; -.
DR   IPI; IPI00756428; -.
DR   IPI; IPI00756984; -.
DR   IPI; IPI00856846; -.
DR   PIR; T02298; T02298.
DR   PIR; T09400; T09400.
DR   RefSeq; NP_001106684.1; NM_001113213.1.
DR   RefSeq; NP_001106685.1; NM_001113214.1.
DR   RefSeq; NP_001171130.1; NM_001177659.1.
DR   RefSeq; NP_001171132.1; NM_001177661.1.
DR   RefSeq; NP_001171133.1; NM_001177662.1.
DR   RefSeq; NP_038643.1; NM_013615.3.
DR   UniGene; Mm.330116; -.
DR   ProteinModelPortal; A3KGV1; -.
DR   STRING; A3KGV1; -.
DR   PhosphoSite; A3KGV1; -.
DR   REPRODUCTION-2DPAGE; A3KGV1; -.
DR   REPRODUCTION-2DPAGE; IPI00130958; -.
DR   PRIDE; A3KGV1; -.
DR   Ensembl; ENSMUST00000113759; ENSMUSP00000109388; ENSMUSG00000026790.
DR   Ensembl; ENSMUST00000113764; ENSMUSP00000109393; ENSMUSG00000026790.
DR   Ensembl; ENSMUST00000113765; ENSMUSP00000109394; ENSMUSG00000026790.
DR   Ensembl; ENSMUST00000113766; ENSMUSP00000109395; ENSMUSG00000026790.
DR   GeneID; 18286; -.
DR   KEGG; mmu:18286; -.
DR   CTD; 18286; -.
DR   MGI; MGI:1098824; Odf2.
DR   HOVERGEN; HBG052808; -.
DR   NextBio; 293720; -.
DR   Bgee; A3KGV1; -.
DR   CleanEx; MM_ODF2; -.
DR   Genevestigator; A3KGV1; -.
DR   GO; GO:0005814; C:centriole; IDA:MGI.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0019861; C:flagellum; IDA:MGI.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell projection; Cilium; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Developmental protein; Differentiation; Microtubule;
KW   Phosphoprotein; Spermatogenesis.
FT   CHAIN         1    830       Outer dense fiber protein 2.
FT                                /FTId=PRO_0000299458.
FT   COILED      144    217       Potential.
FT   COILED      245    423       Potential.
FT   COILED      461    798       Potential.
FT   VAR_SEQ       1     47       Missing (in isoform 7).
FT                                /FTId=VSP_027671.
FT   VAR_SEQ       1     41       MSASSSGGSPRFPSCGKNGVTSLTQKKVLRTPCGAPSVTVT
FT                                -> MKDRSSTPPLHVHVDENTPVHVHIKKLPKPSAASSQ
FT                                (in isoform 2, isoform 3, isoform 4 and
FT                                isoform 5).
FT                                /FTId=VSP_027672.
FT   VAR_SEQ      65     83       Missing (in isoform 2 and isoform 6).
FT                                /FTId=VSP_027673.
FT   VAR_SEQ     281    281       E -> EK (in isoform 4).
FT                                /FTId=VSP_027674.
FT   VAR_SEQ     638    657       IEHQGDKLEMAREKHQASQK -> VRDWQKGSHELARAGAR
FT                                LPR (in isoform 5, isoform 6 and isoform
FT                                7).
FT                                /FTId=VSP_027675.
FT   VAR_SEQ     658    830       Missing (in isoform 5, isoform 6 and
FT                                isoform 7).
FT                                /FTId=VSP_027676.
FT   CONFLICT    349    349       L -> W (in Ref. 2; AAH57001).
SQ   SEQUENCE   830 AA;  95541 MW;  C840B47EC10EF82A CRC64;
     MSASSSGGSP RFPSCGKNGV TSLTQKKVLR TPCGAPSVTV TKSHKRGMKG DTVNVRRSVR
     VKTKVPWMPP GKSSARHVGC KWENPPHCLE ITPPSSEKLV SVMRLSDLST EDDDSGHCKM
     NRYDKKIDSL MNAVGCLKSE VKMQKGERQM AKRFLEERKE ELEEVAHELA ETEHENTVLR
     HNIERIKEEK DFTMLQKKHL QQEKECLMSK LVEAEMDGAA AAKQVMALKD TIGKLKTEKQ
     MTCTDINTLT RQKELLLQKL STFEETNRTL RDLLREQHCK EDSERLMEQQ GTLLKRLAEA
     DSEKARLLLL LQDKDKEVEE LLQEIQCEKA QAKTASELSK SMESMRGHLQ AQLRCKEAEN
     SRLCMQIKNL ERSGNQHKAE VEAIMEQLKE LKQKGDRDKE TLKKAIRAQK ERAEKSEEYA
     EQLHVQLADK DLYVAEALST LESWRSRYNQ VVKDKGDLEL EIIVLNDRVT DLVNQQQSLE
     EKMREDRDSL VERLHRQTAE YSAFKLENER LKASFAPMED KLNQAHLEVQ QLKASVKNYE
     GMIDNYKSQV MKTRLEADEV AAQLERCDKE NKMLKDEMNK EIEAARRQFQ SQLADLQQLP
     DILKITEAKL AECQDQLQGY ERKNIDLTAI ISDLRSRIEH QGDKLEMARE KHQASQKENK
     QLSQKVDELE RKLEATSAQN VEFLQVIAKR EEAIHQAQLR LEEKTRECGS LARQLESAIE
     DARRQVEQTK EQALSKERAA QSKILDLETQ LSRTKTELGQ LRRTRDDADR RYQSRLQDLK
     DRLEQSESTN RSMQNYVQFL KASYANVFGD APYTSSYLTS SPIRSRSPPA
//
ID   A3KMN0_MOUSE            Unreviewed;       651 AA.
AC   A3KMN0;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   SubName: Full=Zbtb16 protein;
DE   Flags: Fragment;
GN   Name=Zbtb16;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
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DR   EMBL; BC132441; AAI32442.1; -; mRNA.
DR   EMBL; BC132443; AAI32444.1; -; mRNA.
DR   IPI; IPI00356328; -.
DR   UniGene; Mm.457803; -.
DR   STRING; A3KMN0; -.
DR   Ensembl; ENSMUST00000093852; ENSMUSP00000091374; ENSMUSG00000066687.
DR   MGI; MGI:103222; Zbtb16.
DR   eggNOG; roNOG06089; -.
DR   HOVERGEN; HBG057844; -.
DR   InParanoid; A3KMN0; -.
DR   OrthoDB; EOG4FFD1G; -.
DR   Bgee; A3KMN0; -.
DR   Genevestigator; A3KMN0; -.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009952; P:anterior/posterior pattern formation; IMP:MGI.
DR   GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
DR   GO; GO:0009880; P:embryonic pattern specification; IMP:MGI.
DR   GO; GO:0035136; P:forelimb morphogenesis; IMP:MGI.
DR   GO; GO:0035110; P:leg morphogenesis; IMP:MGI.
DR   GO; GO:0048133; P:male germ-line stem cell division; IMP:MGI.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptosis; IMP:MGI.
DR   GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR013069; BTB_POZ.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 8.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE   2: Evidence at transcript level;
KW   Metal-binding; Nucleus; Zinc.
FT   NON_TER       1      1
SQ   SEQUENCE   651 AA;  71792 MW;  FA780B23E87C395B CRC64;
     KANQMRLAGT LCDVVIMVDS QEFHAHRTVL ACTSKMFEIL FHRNSQHYTL DFLSPKTFQQ
     ILEYAYTATL QAKAEDLDDL LYAAEILEIE YLEEQCLKIL ETIQASDDND TEATMADGGG
     EEEEDRKARY LKNIFISKHS SEESGYASVA GQSLPGPMVD QSPSVSTSFG LSAMSPTKAA
     VDSLMSIGQS LLQGTLQPPA GPEEPTLAGG GRHPGVAEVK MEMMQVDEAP GQDSPGAAES
     SISGGMGDKL EERSKEGPGT PTRGSVITSA RELHYGREES GEQLSPPVEA GQGPPGRQEP
     LAPPVEKHLG IYSVLPNHKA DAVLSMPSSV TSGLHVQPAL AVSMDFSTYG GLLPQGFIQR
     ELFSKLGELA VGMKAESRPL GEQCSVCGVE LPDNEAVEQH RKLHSGMKTY GCELCGKRFL
     DSLRLRMHLL AHSAGAKAFV CDQCGAQFSK EDALETHRQT HTGTDMAVFC LLCGKRFQAQ
     SALQQHMEVH AGVRSYICSE CNRTFPSHTA LKRHLRSHTG DHPYECEFCG SCFRDESTLK
     SHKRIHTGEK PYECNGCGKK FSLKHQLETH YRVHTGEKPF ECKLCHQRSR DYSAMIKHLR
     THNGASPYQC TICTEYCPSL SSMQKHMKGH KPEEIPPDWR IEKTYLYLCY V
//
ID   A3KMN2_MOUSE            Unreviewed;      1157 AA.
AC   A3KMN2;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAR-2011, entry version 25.
DE   SubName: Full=Ercc6 protein;
DE   Flags: Fragment;
GN   Name=Ercc6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC132447; AAI32448.1; -; mRNA.
DR   IPI; IPI00606873; -.
DR   UniGene; Mm.318310; -.
DR   STRING; A3KMN2; -.
DR   Ensembl; ENSMUST00000066807; ENSMUSP00000066256; ENSMUSG00000054051.
DR   MGI; MGI:1100494; Ercc6.
DR   eggNOG; maNOG08275; -.
DR   HOGENOM; HBG590781; -.
DR   HOVERGEN; HBG103861; -.
DR   InParanoid; A3KMN2; -.
DR   OrthoDB; EOG476JZF; -.
DR   PhylomeDB; A3KMN2; -.
DR   Bgee; A3KMN2; -.
DR   Genevestigator; A3KMN2; -.
DR   GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR   GO; GO:0007256; P:activation of JNKK activity; IMP:MGI.
DR   GO; GO:0007257; P:activation of JUN kinase activity; IMP:MGI.
DR   GO; GO:0008630; P:DNA damage response, signal transduction resulting in induction of apoptosis; IMP:MGI.
DR   GO; GO:0045494; P:photoreceptor cell maintenance; IMP:MGI.
DR   GO; GO:0006290; P:pyrimidine dimer repair; IMP:MGI.
DR   GO; GO:0010332; P:response to gamma radiation; IMP:MGI.
DR   GO; GO:0000303; P:response to superoxide; IMP:MGI.
DR   GO; GO:0009636; P:response to toxin; IMP:MGI.
DR   GO; GO:0010224; P:response to UV-B; IMP:MGI.
DR   GO; GO:0010165; P:response to X-ray; IMP:MGI.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IMP:MGI.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   1157 AA;  130477 MW;  412E5314493B29F3 CRC64;
     DKRLKKHSRK LQRRALQFQG KVGLPSGKKP LEPEVRPEAE GDTEGEESGS SPTDGEEEEE
     QEEEEGVASL SSDDVSYELK PLRKRQKYQK KVPVQEIDDD FFPSSEEEDE AMEGRGGGRK
     VARRQDDGDE DYYKQRLRRW NRLRLQDKEK RLKLEDDSEE SDAEFDEGFK VPGFLFKKLF
     KYQQTGVRWL WELHCQQAGG ILGDEMGLGK TIQIIAFLAG LSYSKIRTRG SNYRFEGLGP
     TIIVCPTTVM HQWVKEFHTW WPPFRVAVLH ETGSYTHKKE RLIRDIVYCH GVLITSYSYI
     RLMQDDISRH DWHYVILDEG HKIRNPNAAV TLACKQFRTP HRIILSGSPM QNNLRELWSL
     FDFIFPGKLG TLPVFMEQFS VPITMGGYSN ASPVQVKTAY KCACVLRDTI NPYLLRRMKS
     DVKMSLSLPD KNEQVLFCRL TDEQHKVYQN FIDSKAVYRI LNGENQIFSG LVALRKICNH
     PDLFSGGPKN ASGPPEDELE EEQFGHWRRS GKMIVVESLL KIWHRQGQRV LLFSQSRQML
     HILEVFLRAH KYSYLKMDGT TTIASRQPLI TKYNEDTSIF VFLLTTRVGG LGVNLTGANR
     VIIYDPDWNP STDTQARERA WRIGQKKQVT VYRLLTAGTI EEKIYHRQIF KQFLTNRVLK
     DPKQRRFFKS NDLYELFTLT SPDASQGTET SAIFAGTGSS IQTPKCQLKK RTSTVLGTDP
     KCKKPPVSDT PANAATLIGE KPKAAGATGR SVTSGESGPF KGDHDTNGNR ASSVAFGEET
     DAGSTLEHLS VMSGDGKHSD SPTVDHTSRP PVEASTSEKQ GSSYAGARCQ AQTEPVPMSE
     QMEGQFSKYK SKRKHDASEE ETTEKRPQPK QKAKNSKHCR DAKFEGTRVP HLVKKRRYRQ
     QTSEQEGGAK DRSSDDYVLE KLFKKSVGVH SVVRHDAIID GSSPDYVLVE AEANRVAQDA
     LKALRLSRQQ CLGAASGVPT WTGHRGISGA PTGVKNRFGQ KRDSSLPVQH PSSLTEKTQN
     NMKKEGKAHT PEHFSGKEDG ASVSGAPSSS SLLARMRARN HMILPERLES DSEHLAEAAA
     VPPCGTEHDD LLVDMRNFIA FQAQVDGQAS TQEILQEFES KLSVAQSCVF RELLRNLCNF
     HRTPGGEGIW KLKPEYC
//
ID   A3KN70_MOUSE            Unreviewed;       740 AA.
AC   A3KN70;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   08-MAR-2011, entry version 40.
DE   SubName: Full=Dclk1 protein;
GN   Name=Dclk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC133685; AAI33686.1; -; mRNA.
DR   IPI; IPI00468380; -.
DR   RefSeq; NP_001182467.1; NM_001195538.1.
DR   UniGene; Mm.393242; -.
DR   UniGene; Mm.472264; -.
DR   ProteinModelPortal; A3KN70; -.
DR   SMR; A3KN70; 54-154, 180-284, 384-670.
DR   STRING; A3KN70; -.
DR   Ensembl; ENSMUST00000054237; ENSMUSP00000050034; ENSMUSG00000027797.
DR   GeneID; 13175; -.
DR   KEGG; mmu:13175; -.
DR   CTD; 13175; -.
DR   MGI; MGI:1330861; Dclk1.
DR   HOVERGEN; HBG003790; -.
DR   InParanoid; A3KN70; -.
DR   PhylomeDB; A3KN70; -.
DR   Bgee; A3KN70; -.
DR   Genevestigator; A3KN70; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0048675; P:axon extension; IGI:MGI.
DR   GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IGI:MGI.
DR   GO; GO:0048813; P:dendrite morphogenesis; IGI:MGI.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IGI:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR003533; Doublecortin_dom.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Gene3D; G3DSA:3.10.20.230; Doublecortin_dom; 2.
DR   Pfam; PF03607; DCX; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00537; DCX; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF89837; Doublecortin_dom; 2.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50309; DC; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding.
SQ   SEQUENCE   740 AA;  82192 MW;  4548A132FD30F7E3 CRC64;
     MSFGRDMELE HFDERDKAQR YSRGSRVNGL PSPTHSAHCS FYRTRTLQTL SSEKKAKKVR
     FYRNGDRYFK GIVYAISPDR FRSFEALLAD LTRTLSDNVN LPQGVRTIYT IDGLKKISSL
     DQLVEGESYV CGSIEPFKKL EYTKNVNPNW SVNVKTTSAS RAVSSLATAK GGPSEVRENK
     DFIRPKLVTI IRSGVKPRKA VRILLNKKTA HSFEQVLTDI TDAIKLDSGV VKRLYTLDGK
     QVMCLQDFFG DDDIFIACGP EKFRYQDDFL LDESECRVVK STSYTKIASA SRRGTTKSPG
     PSRRSKSPAS TSSVNGTPGS QLSTPRSGKS PSPSPTSPGS LRKQRISQHG GSSTSLSSTK
     VCSSMDENDG PGEEESEEGF QIPATITERY KVGRTIGDGN FAVVKECIER STAREYALKI
     IKKSKCRGKE HMIQNEVSIL RRVKHPNIVL LIEEMDVPTE LYLVMELVKG GDLFDAITST
     SKYTERDASG MLYNLASAIK YLHSLNIVHR DIKPENLLVY EHQDGSKSLK LGDFGLATIV
     DGPLYTVCGT PTYVAPEIIA ETGYGLKVDI WAAGVITYIL LCGFPPFRGS GDDQEVLFDQ
     ILMGQVDFPS PYWDNVSDSA KELINMMLLV NVDQRFSAVQ VLEHPWVNDD GLPENEHQLS
     VAGKIKKHFN TGPKPSSTAA GVSVIATTAL DKERQVFRRR RNQDVRSRYK AQPAPPELNS
     ESEDYSPSSS ETVRSPNSPF
//
ID   A4FU75_MOUSE            Unreviewed;      1043 AA.
AC   A4FU75;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   30-NOV-2010, entry version 28.
DE   SubName: Full=Dagla protein;
DE   Flags: Fragment;
GN   Name=Dagla;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC112414; AAI12415.1; -; mRNA.
DR   IPI; IPI00856692; -.
DR   RefSeq; NP_932782.2; NM_198114.2.
DR   UniGene; Mm.329718; -.
DR   STRING; A4FU75; -.
DR   Ensembl; ENSMUST00000039327; ENSMUSP00000046358; ENSMUSG00000035735.
DR   GeneID; 269060; -.
DR   KEGG; mmu:269060; -.
DR   NMPDR; fig|10090.3.peg.4657; -.
DR   CTD; 269060; -.
DR   MGI; MGI:2677061; Dagla.
DR   eggNOG; roNOG05404; -.
DR   HOVERGEN; HBG081435; -.
DR   InParanoid; A4FU75; -.
DR   OMA; SSSGELM; -.
DR   PhylomeDB; A4FU75; -.
DR   NextBio; 392664; -.
DR   Bgee; A4FU75; -.
DR   Genevestigator; A4FU75; -.
DR   GO; GO:0004806; F:triglyceride lipase activity; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   InterPro; IPR002921; Lipase_3.
DR   Pfam; PF01764; Lipase_3; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase.
FT   NON_TER       1      1
SQ   SEQUENCE   1043 AA;  115243 MW;  377E01A86338CCA8 CRC64;
     PGIVVFRRRW SVGSDDLVLP AIFLFLLHTT WFVILSVVLF GLVYNPHEAC SLNLVDHGRG
     YLGILLSCMI AEMAIIWLSM RGGILYTEPR DSMQYVLYVR LAILVIEFIY AIVGIVWLTQ
     YYTSCNDLTA KNVTLGMVVC NWVVILSVCI TVLCVFDPTG RTFVKLRATK RRQRNLRTYN
     LRHRLEEGQA TSWSRRLKVF LCCTRTKDSQ SDAYSEIAYL FAEFFRDLDI VPSDIIAGLV
     LLRQRQRAKR NAVLDEANND ILAFLSGMPV TRNTKYLDLK NSHEMLRYKE VCYYMLFALA
     AYGWPMYLMR KPTCGLCQLA RSCSCCLCPA RPRFAPGVTI EEDNCCGCNA IAIRRHFLDE
     NMTAVDIVYT SCHDAVYETP FYVAVDHDKK KVVISIRGTL SPKDALTDLT GDAERLPVEG
     HRGTWLGHKG MVLSAEYIKK KLEQEMVLSQ AFGRDLGRGT KHYGLIVVGH SLGAGTAAIL
     SFLLRPQYPT LKCFAYSPPG GLLSEDAMEY SKEFVTAVVL GKDLVPRIGL SQLEGFRRQL
     LDVLQRSTKP KWRIIVGATK CIPKSELPED QVEVTTLAST RLWTHPSDLT IALSASTPLY
     PPGRIIHVVH NHPAEQCCCC EQEEPTYFAI WGDNKAFNEV IISPAMLHEH LPYVVMEGLN
     KVLENYNKGK TALLSAAKVM VSPTEVDLTP ELIFQQQPLP TGPPLPTGLA LELPATEHRN
     SSVRSKSQSE MSLEGFSEGR LLSPVAAASA ARQDPVELLL LSTQERLAAE LQSRRAPLAT
     MESLSDTESL YSFDSRRSSG FRSIRGSPSL HAVLERDEGH LFYIDPAIPE ENPSLSSRTE
     LLAADSLSKH SQDTQPLEAA LGSGGVTPER PPSATIEEEE AAGGSEGGGV APRGELALHN
     GRLGDSPSPQ VLEFAEFIDS LFNLDSKSSS FQDLYCMMVP ESPTSDYTEG PKSPSQQEIL
     LRAQFEPNLV PKPPRLFAGS AEPSSGISLS PSFPLSSSGE LMDLTPTGLS SQECLATDKI
     RTSTPTGHGA SPTKQDDLVI SAR
//
ID   A4GZ26_MOUSE            Unreviewed;      1479 AA.
AC   A4GZ26;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   08-MAR-2011, entry version 30.
DE   SubName: Full=ARF6 guanine nucleotide exchange factor IQArfGEF;
GN   Name=Iqsec2; Synonyms=IQArfGEF;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Sakagami H., Kondo H.;
RT   "Expression of a novel GEF for ARF in mouse brain.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AB275281; BAF49453.1; -; mRNA.
DR   IPI; IPI00830728; -.
DR   RefSeq; NP_001108136.1; NM_001114664.1.
DR   UniGene; Mm.33027; -.
DR   ProteinModelPortal; A4GZ26; -.
DR   SMR; A4GZ26; 752-1095.
DR   STRING; A4GZ26; -.
DR   Ensembl; ENSMUST00000112605; ENSMUSP00000108224; ENSMUSG00000041115.
DR   GeneID; 245666; -.
DR   KEGG; mmu:245666; -.
DR   CTD; 245666; -.
DR   MGI; MGI:3528396; Iqsec2.
DR   GeneTree; ENSGT00590000083058; -.
DR   HOGENOM; HBG443726; -.
DR   HOVERGEN; HBG056324; -.
DR   InParanoid; A4GZ26; -.
DR   OrthoDB; EOG4DJJVR; -.
DR   NextBio; 386896; -.
DR   Bgee; A4GZ26; -.
DR   Genevestigator; A4GZ26; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR000904; Sec7.
DR   InterPro; IPR023394; SEC7_alpha_orthog.
DR   Gene3D; G3DSA:1.10.1000.11; G3DSA:1.10.1000.11; 1.
DR   Pfam; PF01369; Sec7; 1.
DR   SMART; SM00222; Sec7; 1.
DR   SUPFAM; SSF48425; Sec7; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS50190; SEC7; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1479 AA;  161772 MW;  2D43B4C065483CCB CRC64;
     MEAGSGPPGG PGSESPNRAV EYLLELNNII ESQQQLLETQ RRRIEELEGQ LDQLTQENRD
     LREESQLHRG ELHRDPLGAR DSPGRESQYQ NLRETQFHHR ELRESQFHQA SRDVGYPNRD
     GAYQNREAIY RDKEREASYQ LQDTTGYTAR ERDVAQCHLH HENPALGRER GGREAGPAHP
     GREKEAGYSA AVGVGQRPPR ERGQLSRGAS RSSSPGAGGG HSTSTSTSPA TTLQRKSDGE
     NSRTVSVEGD APGSDLSTAV DSPGSQPPYR LSQLPPTSSH MGGPPAGVGL PWAQRARLQP
     ASVALRKQEE EEIKRSKALS DSYELSTDLQ DKKVEMLERK YGGSFLSRRA ARTIQTAFRQ
     YRMNKNFERL RSSASESRMS RRIILSNMRM QFSFEEYEKA QNPAYFEGKP ASLDEGAMAG
     ARSHRLERGL PYGGSCGGGI DGGGSSVTTS GEFSNDITEL EDSFSKQVKS LAESIDEALN
     CHPSGPMSEE PGSAQLEKRE SKEQQEDSSA TSFSDLPLYL DDPVPPPSPE RLPSTEPPPQ
     GRPEFWAPAP LPPVPPPMPP GTREDGSREE GTRRGPGCLE CRDFRLRAAH LPLLTIEPPS
     DSSVDLSDRS DRGSVHRQLV YEADGCSPHG TLKHKGPPGR APIPHRHYPA PEGPAPAPPG
     PLPPAPNSGT GPSGVAGGRR LGKCEAAGEN SDGGDNESLE SSSNSNETIN CSSGSSSRDS
     LREPPATGLC KQTYQRETRH SWDSPAFNND VVQRRHYRIG LNLFNKKPEK GIQYLIERGF
     LSDTPVGVAH FILERKGLSR QMIGEFLGNR QKQFNRDVLD CVVDEMDFSS MDLDDALRKF
     QSHIRVQGEA QKVERLIEAF SQRYCVCNPA LVRQFRNPDT IFILAFAIIL LNTDMYSPSV
     KAERKMKLDD FIKNLRGVDN GEDIPRDLLV GIYQRIQGRE LRTNDDHVSQ VQAVERMIVG
     KKPVLSLPHR RLVCCCQLYE VPDPNRPQRL GLHQREVTKI FQKKKILVTY SFRQSFPLVE
     MHMQLFQNSY YQFGIKLLSA VPGGERKVLI IFNAPSLQDR LRFTSDLRES IAEVQEMEKY
     RVESELEKQK GMMRPNASQP GGAKDSVNGT LARSSLEDTY GAGDGLKRGA LSSSLRDLSD
     AGKRGRRNSV GSLDSTIEGS VISSPRPHQR MPPPPPPPPP EEYKSQRPVS NSSSFLGSLF
     GSKRGKGPFQ MPPPPTGQAS ASSSSASSTH HHHHHHHHGH SHGGLGVLPD GQSKLQALHA
     QYCQGPGPAP PPYLPPQQPP LPPPPQQPPP LPQLGSIPPP PASAPPVGPH RHFHAHGPVP
     GPQHYTLGRP GRAPRRGAGG HPQFAPHGRH PLHQPTSPLP LYSPAPQHPP AHKQGPKHFI
     FSHHPQMMPA AGAAGGPGSR PPGGSYSHPH HPQSPLSPHS PIPPHPSYPP LPPPSPHTPH
     SPLPPTSPHG PLHASGPPGT ANPPSANPKA KPSRISTVV
//
ID   A4PI81_MOUSE            Unreviewed;      1304 AA.
AC   A4PI81;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   SubName: Full=Ca2+-dependent activator protein for secretion 2 isoform b;
GN   Name=Cadps2; Synonyms=CAPS2b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=17428348; DOI=10.1186/1471-2202-8-25;
RA   Sadakata T., Washida M., Furuichi T.;
RT   "Alternative splicing variations in mouse CAPS2: differential
RT   expression and functional properties of splicing variants.";
RL   BMC Neurosci. 8:25-25(2007).
CC   -!- SIMILARITY: Contains 1 PH domain.
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DR   EMBL; AB291947; BAF56578.1; -; mRNA.
DR   IPI; IPI00227236; -.
DR   RefSeq; NP_694803.3; NM_153163.3.
DR   UniGene; Mm.259632; -.
DR   ProteinModelPortal; A4PI81; -.
DR   SMR; A4PI81; 492-605.
DR   STRING; A4PI81; -.
DR   PRIDE; A4PI81; -.
DR   Ensembl; ENSMUST00000018122; ENSMUSP00000018122; ENSMUSG00000017978.
DR   GeneID; 320405; -.
DR   KEGG; mmu:320405; -.
DR   CTD; 320405; -.
DR   MGI; MGI:2443963; Cadps2.
DR   HOGENOM; HBG358714; -.
DR   HOVERGEN; HBG080678; -.
DR   InParanoid; A4PI81; -.
DR   OMA; IGTVSVE; -.
DR   NextBio; 396664; -.
DR   Bgee; A4PI81; -.
DR   Genevestigator; A4PI81; -.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0045921; P:positive regulation of exocytosis; IDA:MGI.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR010439; Ca-dep_secretion_activator.
DR   InterPro; IPR014770; Munc13_1.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF06292; DUF1041; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   PROSITE; PS51258; MHD1; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1304 AA;  148553 MW;  1F0D3254F416E062 CRC64;
     MLDPSSSEEE SDEGLEEESR EVLVAPGVSQ RAPPAAAREG RRDAPGRSGG GSGGGAARPV
     SPSPSVLSEG RNEPELQLDE EQERRIRLQL YVFVVRCIAY PFNAKQPTDM ARRQQKLNKQ
     QLQLLKERFQ AFLNGETQIV ADEAFCNAVR SYYEVFLKSD RVARMVQSGG CSANDFREVF
     KKNIEKRVRS LPEIDGLSKE TVLSSWIAKY DAIYRGEEDL CKQPNRMTLS AVSELILSKE
     QLYEMFQQIL GIKKLEHQLL YNACQLDNAD EQAAQIRREL DGRLQLAEKM AKERRFPRFI
     SKEMESMYIE ELRASVNLLM ANLESLPVSK GGPEFKLQKL KRSQNSAFLD LGDENEIQLS
     KSDVVLSFTL EIVIMEVQGL KSVAPNRIVY CTMEVEGGEK LQTDQAEASR PQWGTQGDFN
     TTHPRPVVKV KLFTESTGVL ALEDKELGRV VLYPTSNSSK SAELHRMTVP KNSQDSDLKI
     KLAVRMDKPA HMKHSGYLYA LGQKVWKRWK KRYFVLVQVS QYTFAMCSYR EKKSEPQELM
     QLEGYTVDYT DPHPGLQGGQ VFFNAVKEGD TVIFASDDEQ DRILWVQAMY RATGQSYKPV
     PAVQSQKLNP KGGALHADAQ LYADRFQKHG MDEFISASPC KLDHAFLFRI LQRQTLDHRL
     NDSYSCLGWF SPGQVFVLDE YCARYGVRGC HRHLCYLTEL MEHSENGAVI DPTLLHYSFA
     FCASHVHGNR PDGIGTVSVE EKERFEEIKD RLSSLLENQI SHFRYCFPFG RPEGALKATL
     SLLERVLMKD IATPIPAEEV KKVVRKCLEK AALINYTRLT EYAKIEGPAE KETETMNQAT
     PARKLEEVLH LAELCIEVLQ QNEEHHAEGR EAFAWWPDLL AEHAEKFWAL FTVDMDTALE
     AQPQDSWDSF PLFQLLNNFL RNDTLLCNGK FHKHLQEIFV PLVVRYVDLM ESAIAQSIHR
     GFEQETWQPV KNIANSLPNV ALPKVPSLPL NLPQIPSFST PPWMASLYES TNGSTTSEDL
     FWKLDALQMF VFDLHWPEQE FAHHLEQRLK LMASDMIEAC VKRTRTAFEL KLQKANKTTD
     LRIPASVCTM FNVLVDAKKQ STKLCALDGG QEQQYHSKID DLIDNTVKEI IALLVSKFVS
     VLEGVLSKLS RYDEGTFFSS ILSFTVKAAA KYVDVPKPGM DLADTYIMFV RQNQDILREK
     VNEEMYIEKL FDQWYSNSMK VICVWLADRL DLQLHIYQLK TLIKIVKKTY RDFRLQGVLE
     GTLNSKTYDT LHRRLTVEEA TASVSEGGGL QGITMKDSDE EEEG
//
ID   TTLL7_MOUSE             Reviewed;         912 AA.
AC   A4Q9F0; A4Q9E9; Q8C417; Q9D5V3;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   08-MAR-2011, entry version 33.
DE   RecName: Full=Tubulin polyglutamylase TTLL7;
DE            EC=6.-.-.-;
DE   AltName: Full=Tubulin--tyrosine ligase-like protein 7;
GN   Name=Ttll7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Testis;
RX   PubMed=17499049; DOI=10.1016/j.molcel.2007.04.012;
RA   van Dijk J., Rogowski K., Miro J., Lacroix B., Edde B., Janke C.;
RT   "A targeted multienzyme mechanism for selective microtubule
RT   polyglutamylation.";
RL   Mol. Cell 26:437-448(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 636-912 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP   GLU-349.
RX   PubMed=16901895; DOI=10.1074/jbc.M603984200;
RA   Ikegami K., Mukai M., Tsuchida J., Heier R.L., Macgregor G.R.,
RA   Setou M.;
RT   "TTLL7 is a mammalian beta-tubulin polyglutamylase required for growth
RT   of MAP2-positive neurites.";
RL   J. Biol. Chem. 281:30707-30716(2006).
CC   -!- FUNCTION: Polyglutamylase which preferentially modifies beta-
CC       tubulin. Involved in the side-chain initiation step of the
CC       polyglutamylation reaction rather than in the elongation step.
CC       Required for neurite growth.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium. Cytoplasm,
CC       cytoskeleton, cilium basal body. Cell projection, dendrite.
CC       Perikaryon. Note=In cells with primary cilia, found in both cilia
CC       and basal bodies. In neuronal cells, found in dendrites and
CC       perikaryon.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=A4Q9F0-1; Sequence=Displayed;
CC       Name=2; Synonyms=TTLL7S;
CC         IsoId=A4Q9F0-2; Sequence=VSP_052730, VSP_052731;
CC   -!- TISSUE SPECIFICITY: Widely expressed with highest levels in brain,
CC       testis and trachea. In brain, highly expressed in hippocampus,
CC       thalamus, olfactory bulb and cerebellum.
CC   -!- SIMILARITY: Belongs to the tubulin--tyrosine ligase family.
CC   -!- SIMILARITY: Contains 1 TTL domain.
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DR   EMBL; AM690750; CAM84327.1; -; mRNA.
DR   EMBL; AM690751; CAM84328.1; -; mRNA.
DR   EMBL; AK014905; BAB29613.1; -; mRNA.
DR   EMBL; AK083236; BAC38821.1; -; mRNA.
DR   IPI; IPI00760054; -.
DR   IPI; IPI00857636; -.
DR   UniGene; Mm.187793; -.
DR   ProteinModelPortal; A4Q9F0; -.
DR   SMR; A4Q9F0; 155-209, 329-358.
DR   PRIDE; A4Q9F0; -.
DR   Ensembl; ENSMUST00000038090; ENSMUSP00000037875; ENSMUSG00000036745.
DR   MGI; MGI:1918142; Ttll7.
DR   eggNOG; roNOG12689; -.
DR   GeneTree; ENSGT00600000084067; -.
DR   HOVERGEN; HBG073374; -.
DR   OrthoDB; EOG4MSCXM; -.
DR   Bgee; A4Q9F0; -.
DR   CleanEx; MM_TTLL7; -.
DR   Genevestigator; A4Q9F0; -.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0005932; C:microtubule basal body; IEA:UniProtKB-SubCell.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0004835; F:tubulin-tyrosine ligase activity; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0006464; P:protein modification process; IEA:InterPro.
DR   InterPro; IPR004344; Tub_tyr_ligase.
DR   PANTHER; PTHR12241; Tub_tyr_ligase; 1.
DR   Pfam; PF03133; TTL; 1.
DR   PROSITE; PS51221; TTL; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell projection; Cilium; Cytoplasm;
KW   Cytoskeleton; Developmental protein; Differentiation; Ligase;
KW   Neurogenesis.
FT   CHAIN         1    912       Tubulin polyglutamylase TTLL7.
FT                                /FTId=PRO_0000326163.
FT   DOMAIN       38    390       TTL.
FT   VAR_SEQ     596    609       PSGSHNLIYSESPV -> SSKSISPTSLEEEL (in
FT                                isoform 2).
FT                                /FTId=VSP_052730.
FT   VAR_SEQ     610    912       Missing (in isoform 2).
FT                                /FTId=VSP_052731.
FT   MUTAGEN     349    349       E->V: Loss of activity.
FT   CONFLICT     98     98       F -> Y (in Ref. 2; BAB29613).
SQ   SEQUENCE   912 AA;  105501 MW;  ABCDD119BFF29336 CRC64;
     MPSLPQDGVI QGSSPVDLGT ELPYQCTMKR KVRKKKKKGI ITANVAGTKF EIVRLVIDEM
     GFMKTPDEDE TSNLIWCDAA VQQEKITDLQ NYQRINHFPG MGEICRKDFL ARNMTKMIKS
     RPMDYTFVPR TWIFPSEYTQ FQNYVKELKK KRKQKTFIVK PANGAMGHGI SLIRNGDKVP
     SQDHLIVQEY IEKPFLMEGY KFDLRIYILV TSCDPLKIFL YHDGLVRMGT EKYIPPNESN
     LTQLYMHLTN YSVNKHNERF ERNETEDKGS KRSIKWFTEF LQANQHDVTK FWSDISELVV
     KTLIVAEPHV LHAYRMCRPG QPPGSESVCF EVLGFDILLD RKLKPWLLEI NRAPSFGTDQ
     KIDYDVKRGV LLNALKLLNI RTSDKRKNLA KQKAEAQRRL YGQNPVRRLS PGSSDWEQQR
     HQLERRKEEL KERLLQVRKQ VSQEEHENRH MGNYRRIYPP EDKALLEKYE GLLAVAFQTF
     LSGRAASFQR EMNNPLKKMR EEDLLDLLEQ CEIDDEKLMG KTGRVRGPKP LCCMPECAEV
     TKKQKYYGSS DSSYDSSSSS SNSELDENEK ELCQKRLDQV PYSLKHTSHC KIIQQPSGSH
     NLIYSESPVY LTTLVFLSEF PDSMRRSVSC PRSISAHLPS RGDVRPFSSQ QVIPLARPTS
     ASRSHSLNRA SSYARHLPHG SDTGSTNTLN ESLRQLKTKE QEDDLTSQTL FVLKDMRIRF
     PGKSDAESEL LIEDIMDNWK HYKTKVASYW LIKLDSVKQR KVLDIVKSSI RTVLPRIWRV
     PDAEELSLYR IFNRVFNRLL WSHGQGLWSC FCDSGSSWES IFSKSPEVVT PLQLQCCQRL
     VELCKQCLLV VYKYTTETRG PISGIGPDWG NSRYLLPGST QFLMRSPLYN MKYNSPGMTR
     SNVLFTSRYG RL
//
ID   A5D6P2_MOUSE            Unreviewed;      1334 AA.
AC   A5D6P2;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAR-2011, entry version 32.
DE   SubName: Full=Par-3 (Partitioning defective 3) homolog (C. elegans);
GN   Name=Pard3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 3 PDZ (DHR) domains.
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DR   EMBL; BC090616; AAH90616.1; -; mRNA.
DR   IPI; IPI00970277; -.
DR   RefSeq; NP_001116322.1; NM_001122850.1.
DR   RefSeq; NP_296369.2; NM_033620.2.
DR   UniGene; Mm.299254; -.
DR   ProteinModelPortal; A5D6P2; -.
DR   SMR; A5D6P2; 2-83, 262-363, 454-550, 582-685.
DR   STRING; A5D6P2; -.
DR   PRIDE; A5D6P2; -.
DR   Ensembl; ENSMUST00000160272; ENSMUSP00000125453; ENSMUSG00000025812.
DR   GeneID; 93742; -.
DR   KEGG; mmu:93742; -.
DR   CTD; 93742; -.
DR   MGI; MGI:2135608; Pard3.
DR   eggNOG; roNOG04008; -.
DR   GeneTree; ENSGT00590000082971; -.
DR   HOGENOM; HBG715081; -.
DR   HOVERGEN; HBG053508; -.
DR   InParanoid; A5D6P2; -.
DR   NextBio; 351599; -.
DR   Bgee; A5D6P2; -.
DR   Genevestigator; A5D6P2; -.
DR   InterPro; IPR021922; DUF3534.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF12053; DUF3534; 1.
DR   Pfam; PF00595; PDZ; 3.
DR   SMART; SM00228; PDZ; 3.
DR   SUPFAM; SSF50156; PDZ; 3.
DR   PROSITE; PS50106; PDZ; 3.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1334 AA;  149086 MW;  8005FF1B1674D18B CRC64;
     MKVTVCFGRT RVVVPCGDGR MKVFSLIQQA VTRYRKAVAK DPNYWIQVHR LEHGDGGILD
     LDDILCDVAD DKDRLVAVFD EQDPHHGGDG TSASSTGTQS PEIFGSELGT NNVSAFQPYQ
     ATSEIEVTPS VLRANMPLHV RRSSDPALTG LSTSVSDNNF SSEEPSRKNP TRWSTTAGFL
     KQNTAGSPKT CDRKKDENYR SLPRDPSSWS NQFQRDNARS SLSASHPMVD RWLEKQEQDE
     EGTEEDSSRV EPVGHADTGL ENMPNFSLDD MVKLVQVPND GGPLGIHVVP FSARGGRTLG
     LLVKRLEKGG KAEQENLFHE NDCIVRINDG DLRNRRFEQA QHMFRQAMRA RVIWFHVVPA
     ANKEQYEQLS QREKNNYSPG RFSPDSHCVA NRSVANNAPQ ALPRAPRLSQ PPEQLDAHPR
     LPHSAHASTK PPAAPALAPP SVLSTNVGSV YNTKKVGKRL NIQLKKGTEG LGFSITSRDV
     TIGGSAPIYV KNILPRGAAI QDGRLKAGDR LIEVNGVDLA GKSQEEVVSL LRSTKMEGTV
     SLLVFRQEEA FHPREMNAEP SQMQTPKETK AEDEDVVLTP DGTREFLTFE VPLNDSGSAG
     LGVSVKGNRS KENHADLGIF VKSIINGGAA SKDGRLRVND QLIAVNGESL LGKANQEAME
     TLRRSMSTEG NKRGMIQLIV ARRISRCNEL RSPGSPAAPE LPIETELDDR ERRISHSLYS
     GIEGLDESPT RNAALSRIMG KCQLSPTVNM PHDDTVMIED DRLPVLPPHL SDQSSSSSHD
     DVGFIMTEAG TWAKATISDS ADCSLSPDVD PVLAFQREGF GRQSMSEKRT KQFSDASQLD
     FVKTRKSKSM DLGIADETKL NTVDDQRAGS PSRDVGPSLG LKKSSSLESL QTAVAEVTLN
     GNIPFHRPRP RIIRGRGCNE SFRAAIDKSY DKPMVDDDDE GMETLEEDTE ESSRSGRESV
     STSSDQPSYS LERQMNGDPE KRDKTERKKD KAGKDKKKDR EKEKDKLKAK KGMLKGLGDM
     FRFGKHRKDD KMEKMGRIKI QDSFTSEEDR VRMKEEQERI QAKTREFRER QARERDYAEI
     QDFHRTFGCD DELLYGGMSS YEGCLALNAR PQSPREGHLM DTLYAQVKKP RSSKPGDSNR
     STPSNHDRIQ RLRQEFQQAK QDEDVEDRRR TYSFEQSWSS SRPASQSGRH SVSVEVQVQR
     QRQEERESFQ QAQRQYSSLP RQSRKNASSI SQDSWEQNYA PGEGFQSAKE NPRYSSYQGS
     RNGYLGGHGF NARVMLETQE LLRQEQRRKE QQLKKQPPAD GVRGPFRQDV PPSPSQVARL
     NRLQTPEKGR PFYS
//
ID   A5D6Q5_MOUSE            Unreviewed;      1795 AA.
AC   A5D6Q5;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   11-JAN-2011, entry version 28.
DE   SubName: Full=Plxna3 protein;
GN   Name=Plxna3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 1170-1795.
RX   PubMed=19717441; DOI=10.1073/pnas.0906923106;
RA   He H., Yang T., Terman J.R., Zhang X.;
RT   "Crystal structure of the plexin A3 intracellular region reveals an
RT   autoinhibited conformation through active site sequestration.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:15610-15615(2009).
CC   -!- SIMILARITY: Contains 1 Sema domain.
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DR   EMBL; BC093482; AAH93482.1; -; mRNA.
DR   IPI; IPI00137314; -.
DR   UniGene; Mm.1685; -.
DR   PDB; 3IG3; X-ray; 1.99 A; A=1170-1795.
DR   PDBsum; 3IG3; -.
DR   ProteinModelPortal; A5D6Q5; -.
DR   SMR; A5D6Q5; 29-528, 838-936, 1394-1506.
DR   STRING; A5D6Q5; -.
DR   HOVERGEN; HBG105711; -.
DR   Genevestigator; A5D6Q5; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:InterPro.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:InterPro.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002909; IPT_TIG_rcpt.
DR   InterPro; IPR003659; Plexin-like.
DR   InterPro; IPR016201; Plexin-like_fold.
DR   InterPro; IPR013548; Plexin_cytoplasmic_RasGAP_dom.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR001627; Semaphorin/CD100_Ag.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF08337; Plexin_cytopl; 1.
DR   Pfam; PF01437; PSI; 3.
DR   Pfam; PF01403; Sema; 1.
DR   Pfam; PF01833; TIG; 3.
DR   SMART; SM00429; IPT; 3.
DR   SMART; SM00423; PSI; 3.
DR   SMART; SM00630; Sema; 1.
DR   SUPFAM; SSF81296; Ig_E-set; 4.
DR   SUPFAM; SSF103575; Plexin-like_fold; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   SUPFAM; SSF101912; Sema; 1.
DR   PROSITE; PS51004; SEMA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Membrane; Transmembrane; Transmembrane helix.
SQ   SEQUENCE   1795 AA;  199604 MW;  2E590AF8E22FEBA5 CRC64;
     MPTVCLLPLL FFTIGGCLGS SRPFRTFVVT DTTLTHLAVH RVTGEVFVGA VNRVFKLAPN
     LTELRAHVTG PIEDNARCYP PPSMRVCSHR LVPVDNVNKL LLIDYAARRL VACGSIWQGI
     CQFLRLDDLF KLGEPHHRKE HYLSGAQEPD SMAGVIVEQV QGPSKLFVGT AVDGKSEYFP
     TLSSRKLIDD EDSGDMFSLV YQDEFVSSQI KIPSDTLSLY PAFDIYYIYG FVSASFVYFL
     TLQLDTQQTL LDTAGEKFFT SKIVRMCAGD SEFYSYVEFP IGCSWRGVEY RLVQSAHLAK
     PGLLLAQALG VPADEDVLFT IFSQGQKNRA NPPRQTILCL FTLSSINAHI RRRIQSCYRG
     EGTLALPWLL NKELPCINTP LQINGNFCGL VLNQPLGGLH VIEGLPLLAD STDGMASVAA
     YTYHQHSVVF IGTRSGNLKK VRVDGSQDAQ LYETVSVVQG SPILRDLLFS PDHRHIYLLS
     EKQVSQLPVE TCEQYLSCAA CLGSGDPHCG WCVLQHRCCR EGACPGASAP HGFAEELSKC
     IQVRVRPNNV SVTSSGVQLT VAMRNVPDLS VGVSCSFEEV TESEAILLPS GELRCPSPSL
     QELQTLTRGH GATHTVRLQL LSMETGVRFA GVDFVFYNCS ALQSCMSCVG SPYPCHWCKY
     RHVCTSHPHE CSFQEGRVHS PEGCPEILPQ GDLLIPVGVM QPLTLRAKNL PQPQSGQKNY
     ECVVRVQGRQ HRVPAVRFNS SSVQCQNASY FYEGDEFGDT ELDFSVVWDG DFPIDKPPSF
     RALLYKCWAQ RPSCGLCLKA DPRFNCGWCI SEHRCQLRAH CPAPKSNWMH PSQKGARCSH
     PRITQIHPLT GPKEGGTRVT IVGENLGLTS REVGLRVAGV RCNSIPTEYV SAERIVCEME
     ESLVPSPPPG PAELCVGDCS ADFRTQSQQL YSFVTPTFDR VSPSRGPASG GTRLTISGIS
     LDAGSRVTVI IRDGECQFVR RDAEAIVCIS PVSTLGPSQS PITLAIDHAN ISNTGVIYTY
     TQDPTVTHLE PTWSIINGST SITVSGTHLL TVQEPRVRAK YRGIETTNTC QGKNLIPAAA
     GSSRLNYTVL IGGQPCALTV SDTQLLCDSP SQTGRQPVMV LVGGLEFWLG TLHITADRAL
     TLPAMVGLAA GGGLLLLAIT VVLVAYKRKT QDADRTLKRL QLQMDNLESR VALECKEAFA
     ELQTDINELT NHMDGVQIPF LDYRTYAVRV LFPGIEAHPV LKELDTPPNV EKALRLFGQL
     LHSRAFLLTF IHTLEAQSSF SMRDRGTVAS LTMVALQSRL DYATGLLKQL LADLIEKNLE
     SKNHPKLLLR RTESVAEKML TNWFTFLLHK FLKECAGEPL FLLYCAIKQQ MEKGPIDAIT
     GEARYSLSED KLIRQQIDYK TLTLHCVCPE SEGSAQVPVK VLNCDSITQA KDKLLDTVYK
     GIPYSQRPKA EDMDLEWRQG RMARIILQDE DITTKIECDW KRVNSLAHYQ VTDGSLVALV
     PKQVSAYNMA NSFTFTRSLS RYESLLRAAS SPDSLRSRAP MLTPDQEAGT KLWHLVRNHD
     HTDHREGDRG SKMVSEIYLT RLLATKGTLQ KFVDDLFETV FSTAHRGSAL PLAIKYMFDF
     LDEQADQRQI SDPDVRHTWK SNCLPLRFWV NVIKNPQFVF DIHKNSITDA CLSVVAQTFM
     DSCSTSEHRL GKDSPSNKLL YAKDIPNYKS WVERYYRDIA KMASISDQDM DAYLVEQSRL
     HANDFNVLSA LSELYFYVTK YRQEILTSLD RDASCRKHKL RQKLEQIITL VSSSS
//
ID   A5D6Q8_MOUSE            Unreviewed;      1460 AA.
AC   A5D6Q8;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAR-2011, entry version 26.
DE   SubName: Full=Clasp1 protein;
GN   Name=Clasp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Head;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC094432; AAH94432.1; -; mRNA.
DR   IPI; IPI00669522; -.
DR   RefSeq; NP_083985.2; NM_029709.2.
DR   UniGene; Mm.138740; -.
DR   ProteinModelPortal; A5D6Q8; -.
DR   STRING; A5D6Q8; -.
DR   GeneID; 76707; -.
DR   KEGG; mmu:76707; -.
DR   CTD; 76707; -.
DR   MGI; MGI:1923957; Clasp1.
DR   eggNOG; roNOG04905; -.
DR   HOVERGEN; HBG079692; -.
DR   NextBio; 345659; -.
DR   Genevestigator; A5D6Q8; -.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IDA:MGI.
DR   GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:MGI.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000357; HEAT.
DR   InterPro; IPR021133; HEAT_type_2.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 5.
DR   Pfam; PF02985; HEAT; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 2.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1460 AA;  161144 MW;  12B3D717DBB80A5B CRC64;
     MEPRMESCLA QVLQKDVGKR LQVGQELIDY FSDRQKSADL EHDQTLLDKL VDGLATSWVN
     SSNYKVVLLG MDILSALVTR LQDRFKAQIG TVLPSLIDRL GDAKDSVREQ DQTLLLKIMD
     QAANPQYVWD RMLGGFKHKN FRTREGICLC LIATLNASGA QTLTLSKIVP HICNLLGDPN
     SQVRDAAINS LVEIYRHVGE RVRADLSKKG LPQSRLNVIF TKFDEVQKSG NMIQSANEKN
     FDDEDSVDGN RPSSASSSSS KAPSSSRRNV NLGTTRRLMS SSLGSKSSAA KEGAGAVDEE
     DFIKAFDDVP VVQIYSSRDL EESINKIREI LSDDKHDWEQ RVNALKKIRS LLLAGAAEYD
     NFFQHLRLLD GAFKLSAKDL RSQVVREACI TLGHLSSVLG NKFDHGAEAI MPTIFNLIPN
     SAKIMATSGV VAVRLIIRHT HIPRLIPVIT SNCTSKSVAV RRRCFEFLDL LLQEWQTHSL
     ERHISVLAET IKKGIHDADS EARIEARKCY WGFHSHFSRE AEHLYHTLES SYQKALQSHL
     KNSDSIVSLP QSDRSSSSSQ ESLNRPLSAK RSPTGSTASR GSTVSTKSVS TTGSLQRSRS
     EIDVNAAASA KSKVSSSSGS PAFSSAAALP PGSYASLGRI RTRRQSSGST TNVASTPSDS
     RGRSRAKVVS QSQPGSRSSS PGKLLGSGLA GGSSRGPPVT PSSEKRSKIP RSQGCSRETS
     PNRIGLDRFG LGQSGRIPGS VNAMRVLSTS TDLEAAVADA LLLGDARSKK KPVRRRYEPY
     GMYSDDDANS DASSVRSERS YGSRNGGIPH YLRQTEDVAE VLNHCASSNW SERKEGLLGL
     QNLLKSQRTL SRVELKRLCE IFTRMFADPH SKRVFSMFLE TLVDFIIIHK DDLQDWLFVL
     LTQLLKKMGA DLLGSVQAKV QKALDVTRDS FPFDQQFNIL MRFIVDQTQT PNLKVKVAIL
     KYIESLARQM DPTDFVNSSE TRLAVSRIIT WTTEPKSSDV RKAAQIVLIS LFELNTPEFT
     MLLGALPKTF QDGATKLLHN HLKNSSNTGV GSPSNTIGRT PSRHPSSRTS PLTSPTNCSH
     GGLSPSMLDY DTENLNSEEI YSSLRGVTEA IEKFSFRSQE DLNEPIKRDG KKDCDIVSRD
     GGAASPATEG RGGSEIEGGR MALDNKTSLL NTQPPRAFPG PRAREYNPYP YSDTINTYDK
     TALKEAVFDD DMEQLRDVPI DHSDLVADLL KELSNHNERV EERKGALLEL LKITREDSLG
     VWEEHFKTIL LLLLETLGDK DHSIRALALR VLREILRNQP ARFKNYAELT IMKTLEAHKD
     SHKEVVRAAE EAASTLASSI HPEQCIKVLC PIIQTADYPI NLAAIKMQTK VVERITKESL
     LQLLVDIIPG LLQGYDNTES SVRKASVFCL VAIYSVIGED LKPHLAQLTG SKMKLLNLYI
     KRAQTTNSNS SSSSDVSTHS
//
ID   A5HLW0_MOUSE            Unreviewed;      1254 AA.
AC   A5HLW0;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   08-MAR-2011, entry version 17.
DE   SubName: Full=PCF11;
DE   Flags: Fragment;
GN   Name=Pcf11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c;
RA   Diano S., Diament A.L., Coppola A., Perroud B., Gao Q., Haus K.A.,
RA   Gao X.-B., Shariat-Madar Z., Mahdi F., Sun Y., Blake J.,
RA   Schmaier A.H., Warden C.H.;
RT   "Prolylcarboxypeptidase regulates food intake by promoting breakdown
RT   of alpha-MSH.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; EF537860; ABQ10834.1; -; mRNA.
DR   IPI; IPI00464318; -.
DR   UniGene; Mm.288645; -.
DR   STRING; A5HLW0; -.
DR   Ensembl; ENSMUST00000119954; ENSMUSP00000113717; ENSMUSG00000041328.
DR   MGI; MGI:1919579; Pcf11.
DR   eggNOG; roNOG05533; -.
DR   HOVERGEN; HBG058882; -.
DR   InParanoid; A5HLW0; -.
DR   OrthoDB; EOG4SJ5D3; -.
DR   Bgee; A5HLW0; -.
DR   Genevestigator; A5HLW0; -.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
FT   NON_TER    1254   1254
SQ   SEQUENCE   1254 AA;  139427 MW;  FC76396118379012 CRC64;
     LIRQQLLAKQ KQLLELQQKK LELELEQAKA QLAVSLSVQQ ETANLGPGSV PSKLHVPQIP
     TMAVKTPHQV PVQPDKSRAG PSLQMQDLKG TNRDPRLNRM SQHSSHGKEQ SHRKEFVMNT
     INQSDIKTSK NVPSEKLNSS KQEKSKSGER ITKKELDQLD SKSKSKSKSP SPLKNKLSHT
     KDLKNQDSES MRLSDMSKRD PRLKKHLQDK AEGKDEDVKE KRKTAEKKEK DEHVKSSEHR
     VIGSRSKIIN GIVQKQDMVT EELEKQGTKP GRSSTRKRSR SRSPKSRSPI IHSPKRRDRR
     SPKRRQRSMS PNLAPKAGKM RQSGLKQSHM EEFPPPSREE RNIKRSAKQD VRDPRRLKKM
     DEDRPQETAG QHSMKSGGDP KENIENWQSS KSAKRWKSGW EENKSLQQGD EHSKPPHLRH
     RESWSSTKGI LSPRAPKQQH RLSVDANLQI PKELTLASKR ELLQKTSERL ASGEITQDEF
     LVVVHQIRQL FQYQEGVREE QRSPFNDRFP LKRPRYEDSD KPFVDGPASR FAGLDTNQRL
     TALAEDRPLF DGPGRPSVTR DGPAKMIFEG PNKLSPRIDG PPTPGSLRFD GSPGQMGGGG
     PMRFEGPQGQ LGGGCPLRFE GPPGPVGTPL RFEGPIGQGG GGGFRFEGSP SLRFEGSTGG
     LRFEGPGGQP VGGLRFEGHR GQPVGGLRFE GPHGQPVGSL RFDNPRGQPV GGLRFEGGHG
     PSGAAIRFDG PHGQPGGGGG IRFEGPLLQQ GVGMRFEGPH GQSVAGLRFE GHNQLGGNLR
     FEGPHGQPGV GIRFEGPIVQ QGGGMRFEGP VPGGGLRIEG PLGQGGPRFE GCHSLRFDGQ
     PGQPSLLPRF DGLHGQPGPR FERTGQPGPQ RFDGPPGQQV QPRFDGVPQR FDGPQHQQAS
     RFDIPLGLQG TRFDNHPSQR IESFNHSGPY NDPPGNTFNV PSQGLQFQRH EQIFDTPQGP
     NFNGPHGPGN QNFPNPINRA SGHYFDEKNL QSSQFGNFGN LPTPISVGNI QASQQVLTGV
     AQPVAFGQGQ QFLPVHPQNP GAFIQNPSGG LPKAYPDNHL SQVDVNELFS KLLKTGILKL
     SQPDSATAQV TEAVAQPPPE EDEDQNEDQD VPDLTNFTIE ELKQRYDSVI NRLYTGIQCY
     SCGMRFTTSQ TDVYADHLDW HYRQNRTEKD VSRKVTHRRW YYSLTDWIEF EEIADLEERA
     KSQFFEKVHE EVVLKTQEAA KEKEFQSVPA GPAGAVESCE ICQEQFEQYW DEEE
//
ID   A6H5U5_MOUSE            Unreviewed;       663 AA.
AC   A6H5U5;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   11-JAN-2011, entry version 21.
DE   SubName: Full=Lrrfip1 protein;
GN   Name=Lrrfip1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC144956; AAI44957.1; -; mRNA.
DR   EMBL; BC145642; AAI45643.1; -; mRNA.
DR   IPI; IPI00855165; -.
DR   RefSeq; NP_001104782.1; NM_001111312.1.
DR   RefSeq; NP_032541.1; NM_008515.4.
DR   UniGene; Mm.395990; -.
DR   UniGene; Mm.45039; -.
DR   PRIDE; A6H5U5; -.
DR   Ensembl; ENSMUST00000097650; ENSMUSP00000095255; ENSMUSG00000026305.
DR   GeneID; 16978; -.
DR   KEGG; mmu:16978; -.
DR   CTD; 16978; -.
DR   MGI; MGI:1342770; Lrrfip1.
DR   HOVERGEN; HBG061558; -.
DR   Bgee; A6H5U5; -.
DR   Genevestigator; A6H5U5; -.
DR   InterPro; IPR019139; Leu-rich_rep_flightless-int_pr.
DR   PANTHER; PTHR19212; Leu-rich_rep_flightless-int_pr; 1.
DR   Pfam; PF09738; DUF2051; 3.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   663 AA;  75104 MW;  3F673C8AE94005EE CRC64;
     MTSPEGAQNK EIDCLSPEAQ RLAEARLAAK RAARAEAREI RMKELERQQK EIYQVQKKYY
     GLDTKWGDIE QWMEDSERYS RRFRRNTSAS DEDERLSVGS RGSLRAQPEL EYGSPYAWTN
     GYDGDYCGSQ SLSRRSGRNS SFSGGDGRVS TLSSCREEKL GLSCSNLGLP SSGLASKPLP
     TQNGSRASML DESSLYGARR GSACGSRAPS EYGSHLNSSS RASSRASSAR ASPVVEERPD
     KDFAEKGSRN MPSLSAATLA SLGGTSSRRG SGDTSISMDT EASIREIKEL NELKDQIQDV
     EGKYMQGLKE MKDSLAEVEE KYKKAMVSNA QLDNEKTNFM YQVDTLKDML LELEEQLAES
     QRQYEEKNKE FEREKHAHSI LQFQFAEVKE ALRQREEMLE EIRQLQQKQA GFIREISDLQ
     ETIEWKDKKI GALERQKEFF DSIRSERDDL REETVKLKEE LKKHGIILNS EIATNGETSD
     TVNDVGYQAP TKITKEELNA LKSAGEGTLD VRLKKLIDER ECLLEQIKKL KGQLEGRQKN
     NKLDLLRAED GILENGTDAH VMDLQRDANR QISDLKFKLA KSEQEITALE QNVIRLESQV
     TRYRSAAENA EKIEDELKAE KRKLQRELRS ALDKTEELEV SNGHLVKRLE KMKANRSALL
     SQQ
//
ID   A6H5Z3_MOUSE            Unreviewed;       810 AA.
AC   A6H5Z3;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   08-MAR-2011, entry version 26.
DE   SubName: Full=Exoc6b protein;
DE   SubName: Full=MCG141526;
GN   Name=Exoc6b; ORFNames=mCG_141526;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC144781; AAI44782.1; -; mRNA.
DR   EMBL; BC145693; AAI45694.1; -; mRNA.
DR   EMBL; CH466523; EDK99119.1; -; Genomic_DNA.
DR   IPI; IPI00662007; -.
DR   RefSeq; NP_796051.2; NM_177077.2.
DR   UniGene; Mm.159621; -.
DR   ProteinModelPortal; A6H5Z3; -.
DR   SMR; A6H5Z3; 419-737.
DR   Ensembl; ENSMUST00000160197; ENSMUSP00000125312; ENSMUSG00000033769.
DR   GeneID; 75914; -.
DR   KEGG; mmu:75914; -.
DR   CTD; 75914; -.
DR   MGI; MGI:1923164; Exoc6b.
DR   HOGENOM; HBG315398; -.
DR   HOVERGEN; HBG057543; -.
DR   InParanoid; A6H5Z3; -.
DR   OrthoDB; EOG4V4376; -.
DR   NextBio; 344249; -.
DR   Bgee; A6H5Z3; -.
DR   Genevestigator; A6H5Z3; -.
DR   GO; GO:0000145; C:exocyst; IEA:InterPro.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; IEA:InterPro.
DR   InterPro; IPR007225; Sec15.
DR   PANTHER; PTHR12702; Sec15; 1.
DR   Pfam; PF04091; Sec15; 1.
DR   PIRSF; PIRSF025007; Sec15; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   810 AA;  94130 MW;  9DC3AA54A4B36084 CRC64;
     MERAKMAEES LETAAEHERI LREIESTDTA CIGPTLRSVY DGEEHGRFME KLETRIRNHD
     REIEKMCNFH YQGFVDSITE LLKVRGEAQK LKNQVTDTNR KLQHEGKELV IAMEELKQCR
     LQQRNISATV DKLMLCLPVL EMYSKLRDQM KTKRHYPALK TLEHLEHTYL PQVSHYRFCK
     VMVDNIPKLR EEIKDVSMSD LKDFLESIRK HSDKIGETAM KQAQQQRNLD NIVLQQPRIG
     SKRKSKKDVY TIFDAEVEST SPKSEQDSGI LDVEDEEDDE EVPGAQDLVD FSPVYRCLHI
     YSVLGARETF ENYYRKQRRK QARLVLQPPS NMHETLDGYR KYFNQIVGFF VVEDHILHTT
     QGLVNRAYID ELWEMALSKT IAALRTHSSY CSDPNLVLDL KNLIVLFADT LQVYGFPVNQ
     LFDMLLEIRD QYSETLLKKW AGVFRNILDS DNYSPIPVTS EETYKKVVGQ FPFQDIELEK
     QPFPKKFPFS EFVPKVYNQI KEFIYACLKF SEDLHLSSTE VDDMIRKSTN LLLTRTLSNS
     LQNVIKRKNI GLTELVQIII NTTHLEKSCK YLEEFITNIT NVLPETVHTT KLYGTTTFKD
     ARHAAEEEIY TNLNQKIDQF LQLADYDWMT GDLDNKASDY LVDLIAFLRS TFAVFTHLPG
     KVAQTACMSA CKHLATSLMQ LLLEAEVRQL TLGALQQFNL DVRECEQFAR SGPVPGFQED
     TLQLAFIDLR QLLDLFIQWD WSTYLADYGQ PNCKYLRVNP VTALTLLEKM KDTSRKNNMF
     AQFRKNERDK QKLIDTVAKQ LRGLISSHHS
//
ID   A6H600_MOUSE            Unreviewed;       843 AA.
AC   A6H600;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   08-MAR-2011, entry version 27.
DE   SubName: Full=M-phase phosphoprotein 8;
GN   Name=Mphosph8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC145700; AAI45701.1; -; mRNA.
DR   IPI; IPI00121617; -.
DR   UniGene; Mm.152466; -.
DR   UniGene; Mm.474486; -.
DR   ProteinModelPortal; A6H600; -.
DR   SMR; A6H600; 34-101, 551-709.
DR   STRING; A6H600; -.
DR   Ensembl; ENSMUST00000022503; ENSMUSP00000022503; ENSMUSG00000079184.
DR   Ensembl; ENSMUST00000116468; ENSMUSP00000112170; ENSMUSG00000079184.
DR   MGI; MGI:1922589; Mphosph8.
DR   HOVERGEN; HBG052503; -.
DR   InParanoid; A6H600; -.
DR   OrthoDB; EOG44J2J7; -.
DR   PhylomeDB; A6H600; -.
DR   Bgee; A6H600; -.
DR   Genevestigator; A6H600; -.
DR   GO; GO:0000785; C:chromatin; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR   GO; GO:0006333; P:chromatin assembly or disassembly; IEA:InterPro.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR000953; Chromodomain.
DR   InterPro; IPR016197; Chromodomain-like.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF00385; Chromo; 1.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM00298; CHROMO; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF54160; Chromodomain-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
DR   PROSITE; PS00598; CHROMO_1; 1.
DR   PROSITE; PS50013; CHROMO_2; 1.
PE   2: Evidence at transcript level;
KW   ANK repeat; Repeat.
SQ   SEQUENCE   843 AA;  96093 MW;  A1FF3E67BFF7D518 CRC64;
     MSVPDSIGRS PESEGVGAGD EEKDAATKGT VAVGDSEEDG EDVFEVERIL DMKCEGGKNL
     YKVRWKGYTS EDDTWEPEVH LEDCKEVLLE FRKKLAENKA KAVRKDIQRL SLNNDIFEAD
     SDSDQQSDTK EDISPRKKKK KIKCKEETSP EDLRKKRTKM GKLKDKFKTE LESTSEIIGF
     DVKTKKRIWE VKEELKDSKK PKKDEIKETK ELKKANKRAE VRDLKIKIRE DVKENRKTKK
     ERYIESPLES ESPNDSLILE DDSEDFISDN REENQNVRSV RDKTAQETVQ EGIFEKHLDD
     LISIEEDAGT RVRRKKTKPR KFEEPKEIKK LESTNAFLER RAIPKKQRNQ DKGISNLELN
     KLPSPVFAQT LKSSRLSGEE KSLKSPDLAE EEKEKKNEPK GKYQKRYDLD KEEKARKEPK
     VLKSFKEIRN AFDLFKKTTE EKNDVLENNS KREEISLDSK IMNDNKTKDK CSLKEKRNTR
     DETDTWAYIA AEGDQEVSDS VCQTDETSDG RQPVLSLGMD LQLEWMKLED FQKHLDGEDE
     PFITTNRIPN NLLRDAVKNG DYIAVKVALN SNEEYNLDQE DSTGMTLVML AAAGGQDDLL
     RLLITKGAKV NGRQKNGTTA LIHAAEKNFL TTVAILLEAG AFVNVQQSNG ETALMKACKR
     GNSDIVRLVI ECGADCNILS KHQNSALYFA KQCNNVLVYE LLKSHLETLS RVAEETIRDY
     FESRLALLEP VFPIACHRLC EGPDFSTDFN YMPPQNMPEG SGVLLFIFHA NFLGKDVIAR
     LCGPCSVQAV VLNDKFQLPV FLDSHFVYSF SPVAGPNKLF IRLTEAPFAK VKLLIGAYRV
     QLQ
//
ID   RBG1L_MOUSE             Reviewed;         815 AA.
AC   A6H6A9; Q3UH20; Q80TZ4; Q8BZD2; Q8BZP0; Q8CFI6; Q9QY69;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   08-MAR-2011, entry version 32.
DE   RecName: Full=Rab GTPase-activating protein 1-like;
GN   Name=Rabgap1l; Synonyms=Hhl, Kiaa0471;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Brain, Cerebellum, and Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-386 (ISOFORMS 1/3), AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=CD-1 X 129/Sv; TISSUE=Embryonic stem cell;
RX   MEDLINE=20054088; PubMed=10585558; DOI=10.1016/S0925-4773(99)00234-8;
RA   Hidaka M., Caruana G., Stanford W.L., Sam M., Correll P.H.,
RA   Bernstein A.;
RT   "Gene trapping of two novel genes, Hzf and Hhl, expressed in
RT   hematopoietic cells.";
RL   Mech. Dev. 90:3-15(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 790-815 (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=A6H6A9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A6H6A9-2; Sequence=VSP_052927, VSP_052928, VSP_052929;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=A6H6A9-3; Sequence=VSP_052926, VSP_052930, VSP_052932;
CC       Name=4;
CC         IsoId=A6H6A9-4; Sequence=VSP_052925, VSP_052931;
CC   -!- TISSUE SPECIFICITY: Expressed in embryonic heart and liver, and in
CC       hemopoietic cells.
CC   -!- SIMILARITY: Contains 1 PID domain.
CC   -!- SIMILARITY: Contains 1 Rab-GAP TBC domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF24092.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=AAF24092.1; Type=Frameshift; Positions=145, 153, 156, 354;
CC       Sequence=AAF24092.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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DR   EMBL; AK034019; BAC28549.1; -; mRNA.
DR   EMBL; AK035796; BAC29189.1; -; mRNA.
DR   EMBL; AK147634; BAE28037.1; -; mRNA.
DR   EMBL; BC038651; AAH38651.1; -; mRNA.
DR   EMBL; BC145811; AAI45812.1; -; mRNA.
DR   EMBL; BC145813; AAI45814.1; -; mRNA.
DR   EMBL; AF118565; AAF24092.1; ALT_SEQ; mRNA.
DR   EMBL; AK122292; BAC65574.1; -; mRNA.
DR   IPI; IPI00227488; -.
DR   IPI; IPI00339535; -.
DR   IPI; IPI00461631; -.
DR   IPI; IPI00475284; -.
DR   RefSeq; NP_001033710.1; NM_001038621.2.
DR   RefSeq; NP_038890.3; NM_013862.5.
DR   UniGene; Mm.25833; -.
DR   UniGene; Mm.478325; -.
DR   ProteinModelPortal; A6H6A9; -.
DR   SMR; A6H6A9; 129-252, 510-797.
DR   STRING; A6H6A9; -.
DR   PRIDE; A6H6A9; -.
DR   Ensembl; ENSMUST00000028049; ENSMUSP00000028049; ENSMUSG00000026721.
DR   GeneID; 29809; -.
DR   KEGG; mmu:29809; -.
DR   CTD; 29809; -.
DR   MGI; MGI:1352507; Rabgap1l.
DR   GeneTree; ENSGT00550000074196; -.
DR   HOVERGEN; HBG063892; -.
DR   InParanoid; A6H6A9; -.
DR   OMA; EQLPDLY; -.
DR   OrthoDB; EOG4QC14X; -.
DR   PhylomeDB; A6H6A9; -.
DR   Bgee; A6H6A9; -.
DR   Genevestigator; A6H6A9; -.
DR   GO; GO:0032313; P:regulation of Rab GTPase activity; IEA:InterPro.
DR   InterPro; IPR022164; Kinesin-like.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   InterPro; IPR000195; RabGAP/TBC_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF12473; DUF3694; 1.
DR   Pfam; PF00640; PID; 1.
DR   Pfam; PF00566; TBC; 1.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; RabGAP_TBC; 2.
DR   PROSITE; PS01179; PID; 1.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; GTPase activation; Phosphoprotein.
FT   CHAIN         1    815       Rab GTPase-activating protein 1-like.
FT                                /FTId=PRO_0000348055.
FT   DOMAIN      126    282       PID.
FT   DOMAIN      538    724       Rab-GAP TBC.
FT   MOD_RES     118    118       Phosphoserine.
FT   MOD_RES     471    471       Phosphothreonine (By similarity).
FT   MOD_RES     480    480       Phosphoserine (By similarity).
FT   MOD_RES     490    490       Phosphoserine (By similarity).
FT   VAR_SEQ       1    743       Missing (in isoform 4).
FT                                /FTId=VSP_052925.
FT   VAR_SEQ       1    681       Missing (in isoform 3).
FT                                /FTId=VSP_052926.
FT   VAR_SEQ       1     30       MEVRASFQKVSGSSDSVATLNSEEFVLVSQ -> ME (in
FT                                isoform 2).
FT                                /FTId=VSP_052927.
FT   VAR_SEQ     489    505       ESDNELSSGTGDVSKDC -> DPGHASPDTVGFLTLFL
FT                                (in isoform 2).
FT                                /FTId=VSP_052928.
FT   VAR_SEQ     506    815       Missing (in isoform 2).
FT                                /FTId=VSP_052929.
FT   VAR_SEQ     682    737       YSHFCDLNLEAHMYASQWFLTLFTAKFPLCMVFHIIDLLLC
FT                                EGLNIIFHVALALLK -> MEEGVPCPAPAAKLTPPVKKSQ
FT                                DMHDERSKLVNEYACRVLELLGMGHRLFVPRLLA (in
FT                                isoform 3).
FT                                /FTId=VSP_052930.
FT   VAR_SEQ     744    780       LQADFEGALKFFRVQLPKRYRAEENARRLMEQACNIK ->
FT                                MMEEISIMVAYDAHVFSQLHDEDFLTSLVATSKPRSM (in
FT                                isoform 4).
FT                                /FTId=VSP_052931.
FT   VAR_SEQ     812    815       FVYL -> RENRRLQEASMRLEQENDDLAHELVTSKIALRN
FT                                DLDQAEDKADVLNKELLFTKQRLVETEEEKRKQEEETAQLK
FT                                EVFRKQLEKAEYEIKKTTAIIAEYKQICSQLSTRLEKQQAA
FT                                SKEELEAVKGKMMACKHCSDIFSKEGALKPVAVNREDQGLE
FT                                ADDEKDSLKKQLREMELELAQTKLQLVEAKCKIQELEHQRG
FT                                ALMNEIQAAKNSWFSKTLNSIKTATGTQPLQPPQAPQPPKE
FT                                ST (in isoform 3).
FT                                /FTId=VSP_052932.
FT   CONFLICT      4      4       R -> G (in Ref. 3; AAF24092).
FT   CONFLICT    108    108       S -> C (in Ref. 1; BAC29189).
FT   CONFLICT    208    208       G -> E (in Ref. 3; AAF24092).
FT   CONFLICT    303    303       F -> I (in Ref. 3; AAF24092).
FT   CONFLICT    384    386       PKD -> LSQ (in Ref. 3; AAF24092).
SQ   SEQUENCE   815 AA;  92404 MW;  28AA916BF9BA3F0E CRC64;
     MEVRASFQKV SGSSDSVATL NSEEFVLVSQ HTDATSIKDD GKPQLKIASN GDEQLEKAME
     EILRDSEKGQ SGLPVDCQGS SEISDCPFGD VPASQTTKPP LQLILDPSNT EISTPRPSSP
     SRFPEEDSVL FNKLTYLGCM KVSSPRSEVE ALRAMATMRA SSQYPFAVTL YVPNVPEGSV
     RIIDQSSNVE IASFPIYKVL FCARGHDGTA ESNCFAFTES SHGSEEFQIH VFSCEIKEAV
     SRILYSFCTA FKRSSRQVSD VKDSVIPTPD SDVFTFSVSL EVKEDDGKGN FSPVPKDRDK
     FYFKIKQGIE KKVVITVQQL SNKELAIERC FGMLLSPGRN VKNSDMHLLD MESMGKSYDG
     RAYVITGMWN PNAPIFLALN EETPKDKRVY MTVAVDMVVT EVVEPVRFLL ETVVRVYPAN
     ERFWYFSRKT FTETFFMRLK QSEGKGHSSA GDAIYEVVSL QRESDKEEPI TPTSAGGPMS
     PQEDEAEEES DNELSSGTGD VSKDCPEKIL YSWGELLGRW HNNLGGRPKG LFTLVKSGVP
     EALRAEVWQL LAGCHDNQEM LDKYRILITK DSAQESVITR DIHRTFPAHD YFKDTGGDGQ
     ESLYKICKAY SVFDEDIGYC QGQSFLAAVL LLHMPEEQAF CVLVTIMYGY KLRDLYRNNF
     EDLHCKFYQL EKLMQEQLPD LYSHFCDLNL EAHMYASQWF LTLFTAKFPL CMVFHIIDLL
     LCEGLNIIFH VALALLKTSK EDLLQADFEG ALKFFRVQLP KRYRAEENAR RLMEQACNIK
     VPTKKLKKYE KEYQAMRENQ LQQEDPMDRY KFVYL
//
ID   A6H6J9_MOUSE            Unreviewed;       467 AA.
AC   A6H6J9;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   08-MAR-2011, entry version 26.
DE   SubName: Full=Ankyrin repeat domain 50;
GN   Name=Ankrd50;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC145902; AAI45903.1; -; mRNA.
DR   IPI; IPI00468603; -.
DR   UniGene; Mm.290937; -.
DR   UniGene; Mm.415480; -.
DR   ProteinModelPortal; A6H6J9; -.
DR   SMR; A6H6J9; 1-141.
DR   PRIDE; A6H6J9; -.
DR   Ensembl; ENSMUST00000094300; ENSMUSP00000091858; ENSMUSG00000044864.
DR   Ensembl; ENSMUST00000156038; ENSMUSP00000122842; ENSMUSG00000044864.
DR   MGI; MGI:2139777; Ankrd50.
DR   HOVERGEN; HBG073337; -.
DR   InParanoid; A6H6J9; -.
DR   OMA; KSVANIA; -.
DR   OrthoDB; EOG4868C3; -.
DR   Bgee; A6H6J9; -.
DR   Genevestigator; A6H6J9; -.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 3.
DR   SMART; SM00248; ANK; 4.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
PE   2: Evidence at transcript level;
KW   ANK repeat; Repeat.
SQ   SEQUENCE   467 AA;  50265 MW;  1DD5F16107C405B5 CRC64;
     MAEYFLENGA NVEASDAEGR TALHVSCWQG HVEMVRVLIA CHADVNAADN EKRSALQSAA
     WQGHVKVVQL LIEHGAVVDH TCNQGATALC IAAQEGHVDV VQVLLEHGAD PNHADQFGRT
     AMRVAAKNGH SQIIKLLEKY GASSLNGCSP SPVHTMEQKP PQSAPSKMQS LTIRSNSSGG
     TGGGDLQPSL RGLPNGPAHA FSSPSESPDS TVDRQKSSLS NNSLKSSKNS SLRTTSSTAT
     AQTVPIDSFH SLSFTEQIQQ HSLPRSRSRQ SVVSPSSTTQ SLGHSHNSPS SEFEWSQVKP
     SLKSTKSNKG GKSDNSSKSG SAGKKAKQNS SSQPKVLEYE MTQFDKRGPV AKSGSSPPKQ
     TPAESQCKIV VPSSQDSSRA QPQFLIHQQS SEQKRRNGIM TNPNYHLQSN QVFLGRVSVP
     RTVQERGHQE VLEGFPPSET ELNLKQALKL QIEGSDPSFN YKKETPL
//
ID   KCNB2_MOUSE             Reviewed;         907 AA.
AC   A6H8H5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   08-MAR-2011, entry version 32.
DE   RecName: Full=Potassium voltage-gated channel subfamily B member 2;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv2.2;
GN   Name=Kcnb2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Mediates the voltage-dependent potassium ion
CC       permeability of excitable membranes. Channels open or close in
CC       response to the voltage difference across the membrane, letting
CC       potassium ions pass in accordance with their electrochemical
CC       gradient (By similarity).
CC   -!- SUBUNIT: Heteromultimer with KCNS1, KCNS2 and KCNS3 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position (By similarity).
CC   -!- DOMAIN: The tail may be important in modulation of channel
CC       activity and/or targeting of the channel to specific subcellular
CC       compartments (By similarity).
CC   -!- PTM: Phosphorylated (Potential).
CC   -!- SIMILARITY: Belongs to the potassium channel family. B (Shab)
CC       (TC 1.A.1.2) subfamily. Kv2.2/KCNB2 sub-subfamily.
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DR   EMBL; BC146609; AAI46610.1; -; mRNA.
DR   IPI; IPI00757780; -.
DR   RefSeq; NP_001091998.1; NM_001098528.2.
DR   UniGene; Mm.156081; -.
DR   ProteinModelPortal; A6H8H5; -.
DR   SMR; A6H8H5; 32-427.
DR   PRIDE; A6H8H5; -.
DR   GeneID; 98741; -.
DR   KEGG; mmu:98741; -.
DR   CTD; 98741; -.
DR   MGI; MGI:99632; Kcnb2.
DR   HOVERGEN; HBG052225; -.
DR   NextBio; 353617; -.
DR   Genevestigator; A6H8H5; -.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003973; K_chnl_volt-dep_Kv2.
DR   InterPro; IPR005826; K_chnl_volt-dep_Kv2.2.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   Pfam; PF03521; Kv2channel; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01515; KV22CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01495; SHABCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Ion transport; Ionic channel; Membrane; Phosphoprotein;
KW   Potassium; Potassium channel; Potassium transport; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    907       Potassium voltage-gated channel subfamily
FT                                B member 2.
FT                                /FTId=PRO_0000320104.
FT   TOPO_DOM      1    189       Cytoplasmic (Potential).
FT   TRANSMEM    190    210       Helical; Name=Segment S1; (Potential).
FT   TRANSMEM    233    253       Helical; Name=Segment S2; (Potential).
FT   TOPO_DOM    254    263       Cytoplasmic (Potential).
FT   TRANSMEM    264    284       Helical; Name=Segment S3; (Potential).
FT   TRANSMEM    299    320       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TOPO_DOM    321    334       Cytoplasmic (Potential).
FT   TRANSMEM    335    355       Helical; Name=Segment S5; (Potential).
FT   INTRAMEM    369    389       Pore-forming; Name=Segment H5;
FT                                (Potential).
FT   TRANSMEM    396    416       Helical; Name=Segment S6; (Potential).
FT   TOPO_DOM    417    907       Cytoplasmic (Potential).
FT   MOTIF       381    386       Selectivity filter (By similarity).
FT   CARBOHYD    287    287       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   907 AA;  102350 MW;  A926792CFE73431D CRC64;
     MAEKAPPGLN RKTSRSTLSL PPEPVDIIRS KTCSRRVKIN VGGLNHEVLW RTLDRLPRTR
     LGKLRDCNTH ESLLEVCDDY NLNENEYFFD RHPGAFTSIL NFYRTGKLHM MEEMCALSFG
     QELDYWGIDE IYLESCCQAR YHQKKEQMNE ELRREAETMR EREGEEFDNT CCPEKRKKLW
     DLLEKPNSSV AAKILAIVSI LFIVLSTIAL SLNTLPELQE NDEFGQPSDN RKLAHVEAVC
     IAWFTMEYLL RFLSSPNKWK FFKGPLNVID LLAILPYYVT IFLTESNKSV LQFQNVRRVV
     QIFRIMRILR ILKLARHSTG LQSLGFTLRR SYNELGLLIL FLAMGIMIFS SLVFFAEKDE
     DATKFTSIPA SFWWATITMT TVGYGDIYPK TLLGKIVGGL CCIAGVLVIA LPIPIIVNNF
     SEFYKEQKRQ EKAIKRREAL ERAKRNGSIV SMNLKDAFAR SMELIDVAVE KAGESANTKD
     SVDDNHLSPS RWKWARKALS ETSSNKSYEN KYQEVSQKDS HEHLNNTSSS SPQHLSAQKL
     EMLYNEITKT QPHSHPNPDC QEQPERPCVY EEEIEMEEVI CPQEQLAVAQ TEVIVDMKST
     SSIDSFTSCA TDFTETERSP LPPPSASHLQ MKFPTDLPGT DEHQRARAPP FLTLSRDKGP
     AAREAAVDYA PIDITVNLDA GASHGPLQPD SASDSPKSSL KGSNPLKSRS LKVNFQENRA
     SAPQTPPSTA RPLPVTTADF PLTTPQHMST ILLEEALPQG QPPLLEADDS AHCQGPSKGF
     SPRFPKQKLF PFSSRERRSF TEIDTGEDED FLDLQRSRPD KQADPSPNCL ADKPGDARDS
     LREEGCVGSS SPQNTDHNCR QDIYQAVGEV KKDSSQEGYK MENHLFAPEI HSNPGDTGHC
     PTRETSM
//
ID   RHG31_MOUSE             Reviewed;        1425 AA.
AC   A6X8Z5; Q3TL91; Q3U1T7; Q3UDE7; Q3UUH4; Q6ZPW0; Q9WV94;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   RecName: Full=Rho GTPase-activating protein 31;
DE   AltName: Full=Cdc42 GTPase-activating protein;
GN   Name=Arhgap31; Synonyms=Cdgap, Kiaa1204;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, and Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-820, FUNCTION, AND TISSUE SPECIFICITY.
RX   MEDLINE=99003274; PubMed=9786927; DOI=10.1074/jbc.273.44.29172;
RA   Lamarche-Vane N., Hall A.;
RT   "CdGAP, a novel proline-rich GTPase-activating protein for Cdc42 and
RT   Rac.";
RL   J. Biol. Chem. 273:29172-29177(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 406-1425.
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [5]
RP   INTERACTION WITH ITSN1, AND SUBCELLULAR LOCATION.
RX   PubMed=11744688; DOI=10.1074/jbc.M105516200;
RA   Jenna S., Hussain N.K., Danek E.I., Triki I., Wasiak S.,
RA   McPherson P.S., Lamarche-Vane N.;
RT   "The activity of the GTPase-activating protein CdGAP is regulated by
RT   the endocytic protein intersectin.";
RL   J. Biol. Chem. 277:6366-6373(2002).
RN   [6]
RP   IDENTIFICATION, AND PHOSPHORYLATION AT THR-776.
RX   PubMed=16024771; DOI=10.1128/MCB.25.15.6314-6329.2005;
RA   Tcherkezian J., Danek E.I., Jenna S., Triki I., Lamarche-Vane N.;
RT   "Extracellular signal-regulated kinase 1 interacts with and
RT   phosphorylates CdGAP at an important regulatory site.";
RL   Mol. Cell. Biol. 25:6314-6329(2005).
RN   [7]
RP   FUNCTION, INTERACTION WITH PARVA, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF ARG-56 AND ASN-169.
RX   PubMed=16860736; DOI=10.1016/j.cub.2006.05.057;
RA   LaLonde D.P., Grubinger M., Lamarche-Vane N., Turner C.E.;
RT   "CdGAP associates with actopaxin to regulate integrin-dependent
RT   changes in cell morphology and motility.";
RL   Curr. Biol. 16:1375-1385(2006).
RN   [8]
RP   PHOSPHORYLATION AT THR-776, AND INDUCTION BY SERUM.
RX   PubMed=17158447; DOI=10.1074/jbc.M610073200;
RA   Danek E.I., Tcherkezian J., Triki I., Meriane M., Lamarche-Vane N.;
RT   "Glycogen synthase kinase-3 phosphorylates CdGAP at a consensus ERK 1
RT   regulatory site.";
RL   J. Biol. Chem. 282:3624-3631(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1092 AND SER-1093, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1163, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Functions as a GTPase-activating protein (GAP) for RAC1
CC       and CDC42. Required for cell spreading, polarized lamellipodia
CC       formation and cell migration.
CC   -!- SUBUNIT: Interacts with ITSN1, which inhibits GAP activity.
CC       Interacts with PARVA.
CC   -!- SUBCELLULAR LOCATION: Cell projection, lamellipodium. Cell
CC       junction, focal adhesion.
CC   -!- TISSUE SPECIFICITY: Expressed at highest levels in heart and lung.
CC   -!- INDUCTION: By serum (at protein level).
CC   -!- PTM: Phosphorylated on Thr-776 by GSK3; which reduces GAP
CC       activity.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK138417; BAE23651.1; -; mRNA.
DR   EMBL; AK149975; BAE29205.1; -; mRNA.
DR   EMBL; AK150109; BAE29314.1; -; mRNA.
DR   EMBL; AK155729; BAE33406.1; -; mRNA.
DR   EMBL; AK166583; BAE38872.1; -; mRNA.
DR   EMBL; AK166622; BAE38901.1; -; mRNA.
DR   EMBL; CT009576; CAO77869.1; -; Genomic_DNA.
DR   EMBL; AC154425; CAO77869.1; JOINED; Genomic_DNA.
DR   EMBL; AF151363; AAD38043.1; -; mRNA.
DR   EMBL; AK129309; BAC98119.1; -; mRNA.
DR   IPI; IPI00125505; -.
DR   RefSeq; NP_064656.2; NM_020260.2.
DR   UniGene; Mm.370848; -.
DR   ProteinModelPortal; A6X8Z5; -.
DR   SMR; A6X8Z5; 19-218.
DR   STRING; A6X8Z5; -.
DR   PRIDE; A6X8Z5; -.
DR   Ensembl; ENSMUST00000023487; ENSMUSP00000023487; ENSMUSG00000022799.
DR   GeneID; 12549; -.
DR   KEGG; mmu:12549; -.
DR   CTD; 12549; -.
DR   MGI; MGI:1333857; Arhgap31.
DR   eggNOG; roNOG10148; -.
DR   HOVERGEN; HBG105825; -.
DR   InParanoid; A6X8Z5; -.
DR   OMA; PWEEPQW; -.
DR   OrthoDB; EOG4PRSPT; -.
DR   PhylomeDB; A6X8Z5; -.
DR   NextBio; 281594; -.
DR   Bgee; A6X8Z5; -.
DR   CleanEx; MM_CDGAP; -.
DR   Genevestigator; A6X8Z5; -.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR   GO; GO:0017124; F:SH3 domain binding; IDA:MGI.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:MGI.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell projection; GTPase activation; Phosphoprotein.
FT   CHAIN         1   1425       Rho GTPase-activating protein 31.
FT                                /FTId=PRO_0000320115.
FT   DOMAIN       21    216       Rho-GAP.
FT   COMPBIAS    770    777       Poly-Pro.
FT   MOD_RES     776    776       Phosphothreonine; by GSK3.
FT   MOD_RES    1092   1092       Phosphoserine.
FT   MOD_RES    1093   1093       Phosphoserine.
FT   MOD_RES    1163   1163       Phosphoserine.
FT   MUTAGEN      56     56       R->A: 70% reduction of GAP activity; when
FT                                associated with V-169.
FT   MUTAGEN     169    169       N->V: 70% reduction of GAP activity; when
FT                                associated with A-56.
FT   CONFLICT    292    292       R -> K (in Ref. 2; BAE33406).
FT   CONFLICT   1153   1153       V -> F (in Ref. 2; BAE38872/BAE38901).
FT   CONFLICT   1365   1365       S -> C (in Ref. 2; BAE38872/BAE38901).
SQ   SEQUENCE   1425 AA;  155276 MW;  00A39A0664D1A558 CRC64;
     MKNKGAKQKL KRKGAASAFG CDLTEYLESS GQDVPYVLKS CAEFIETHGI VDGIYRLSGI
     TSNIQRLRQE FGSDQCPDLT REVYLQDIHC VGSLCKLYFR ELPNPLLTYE LYEKFTEAVS
     HRPEEGQLAR IQNVILELPP PHYRTLEYLI RHLAHIASFS SKTNMHARNL ALVWAPNLLR
     SKKIEATICN GDAAFLAVRV QQVVIEFILN HADQIFNGGA PGALQQDESR TITKSLTLPA
     LSLPMKLVSL EEAQARSLAT NHPARKERRE NSLPEIVPPP FHTVLELPDN KRKLSSKSKK
     WKSIFNLGRS GSDSKSKLSR NGSVFVRGQR LSVEKATIRP AKSMDSLCSV PVEGKENKGN
     FSRTVTTGGF FIPATKMHAS STGSSCDLSK EGEWGQEGMP AGAEGGCEVG GQIRPLPEQL
     KVFRPIGDPE SEQSAPKLLG MFYTSSDSPG KSVFTSSLFQ MEPSPRHQRK ALNISEPFAV
     SVPLRVSAVI STNSTPCRTP PKELQSLSSL EEFSFQGSES GGWPEEEKPL GAESFPGSVT
     KKAATEDTKP EPEVPGRAEC SQSPPLDPGT QVEKKTLHVS LGSQVSKEAE KRPKAEKVME
     ESQGASQPKP STPQESLGAG TEPLILHEMD EEDLAQALIW PEIQQELKII ESEEEFSSLP
     PAAQKTSPIP ESSPAPFPFP EAPGSLPSSS APREVWTRDA ANQSIQEAAI LTDREKLEPV
     CSLLESESQQ ELSPDPASLA PLEMLLFEKV SSPARIEIGG PRNLSPPLTP APPPPTPLEE
     EPEVLLSKEG PDREDAARDS RTDVYTEQPT PKESPGIPTP CQREEAIASP NEKQNARHAV
     PENKGPGLPS PTKEVDIIPQ EEGGAPHSAQ EPSDCDEDDT VTDPAQHGLE MVEPWEEPQW
     VTSPLHSPTL KEVQESQTQG SQGHRLERRL CHRPSLRQSH SLDSKTTGNS HWTLEAPFSS
     SCANLETERN YEPLQPPAAR TKIAGLEEKA LKAFREFSGL KGLEVLPSQK GPSGIQPKPV
     ETNFMGLAEG KEQEPQLELS NRQMKHSDVP GPDSSKESSP RAQDSTLPGE HPLQLQLKNT
     ECGPSKGKHR PSSLNLDSAT PIADLFRLEN GAPFSSPGIE LSELGDTKVT WMSSSHCKAA
     PWNSQDTQDL DIVAHTLTGR RNSAPVSVSA VRTSFMVKMC QAKAVPVIPP KIQYTQIPQP
     LPSQSTGEGG AQPLERSQEE PGSTPEIPQK STKDDSPSSL GSPEEEQPKQ ETGASASRRQ
     ASITSCMYEG SSCSPEPSAS TLASTQDAVV QCRKRTSETE PSGDNLLSSK LERASGGPKA
     FHRSRPGRPQ SLILFPIMDH LPSSPTVIDS KVLLSPIRSP TQTVSPGLLC GELAENTWIT
     PEGVTLRNKM TIPKNGQRLE TSTSCFYQPQ RRSVILDGRS GRQIE
//
ID   D19L1_MOUSE             Reviewed;         746 AA.
AC   A6X919; Q3UP31; Q8CD79;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   RecName: Full=Protein dpy-19 homolog 1;
DE   AltName: Full=Dpy-19-like protein 1;
GN   Name=Dpy19l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Spleen, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-220 (ISOFORM 1).
RC   TISSUE=Brain, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=A6X919-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A6X919-2; Sequence=VSP_029630;
CC       Name=3;
CC         IsoId=A6X919-3; Sequence=VSP_029629, VSP_029631;
CC   -!- SIMILARITY: Belongs to the dpy-19 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CD352443; Type=Frameshift; Positions=14;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK031291; BAC27335.1; -; mRNA.
DR   EMBL; AK143845; BAE25566.1; -; mRNA.
DR   EMBL; CT010514; CAO77909.1; -; Genomic_DNA.
DR   EMBL; CT010514; CAO77910.1; -; Genomic_DNA.
DR   EMBL; AC102554; CAO77910.1; JOINED; Genomic_DNA.
DR   EMBL; BC116782; AAI16783.1; -; mRNA.
DR   EMBL; BC116784; AAI16785.1; -; mRNA.
DR   EMBL; CD352443; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00275318; -.
DR   IPI; IPI00857720; -.
DR   IPI; IPI00877183; -.
DR   RefSeq; NP_766508.3; NM_172920.4.
DR   UniGene; Mm.38526; -.
DR   PhosphoSite; A6X919; -.
DR   PRIDE; A6X919; -.
DR   Ensembl; ENSMUST00000034446; ENSMUSP00000034446; ENSMUSG00000043067.
DR   Ensembl; ENSMUST00000115277; ENSMUSP00000110932; ENSMUSG00000043067.
DR   GeneID; 244745; -.
DR   KEGG; mmu:244745; -.
DR   CTD; 244745; -.
DR   MGI; MGI:1915685; Dpy19l1.
DR   eggNOG; roNOG14654; -.
DR   GeneTree; ENSGT00530000063023; -.
DR   HOGENOM; HBG382512; -.
DR   HOVERGEN; HBG061402; -.
DR   InParanoid; A6X919; -.
DR   OMA; FDHGELV; -.
DR   OrthoDB; EOG4X3H0V; -.
DR   NextBio; 386420; -.
DR   Bgee; A6X919; -.
DR   CleanEx; MM_DPY19L1; -.
DR   Genevestigator; A6X919; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR018732; Dpy-19.
DR   Pfam; PF10034; DUF2211; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    746       Protein dpy-19 homolog 1.
FT                                /FTId=PRO_0000311878.
FT   TRANSMEM    137    159       Helical; (Potential).
FT   TRANSMEM    227    247       Helical; (Potential).
FT   TRANSMEM    257    279       Helical; (Potential).
FT   TRANSMEM    307    325       Helical; (Potential).
FT   TRANSMEM    331    350       Helical; (Potential).
FT   TRANSMEM    357    374       Helical; (Potential).
FT   TRANSMEM    380    396       Helical; (Potential).
FT   TRANSMEM    405    425       Helical; (Potential).
FT   TRANSMEM    481    501       Helical; (Potential).
FT   TRANSMEM    520    540       Helical; (Potential).
FT   TRANSMEM    562    582       Helical; (Potential).
FT   VAR_SEQ       1    551       Missing (in isoform 3).
FT                                /FTId=VSP_029629.
FT   VAR_SEQ       1    194       Missing (in isoform 2).
FT                                /FTId=VSP_029630.
FT   VAR_SEQ     552    560       VMASLICSR -> MVTRGFLEF (in isoform 3).
FT                                /FTId=VSP_029631.
FT   CONFLICT    208    208       V -> A (in Ref. 3; CD352443).
SQ   SEQUENCE   746 AA;  84187 MW;  C2C6007141CAE426 CRC64;
     MVLQARSKHR DAAPRPPRSA RSSPPPLSGA SEVDAGELGS ERTPPSPGRR GAAGRKGPRA
     GTAAPAPDGL AGRLAAGLHW ALGLRRGRGR TWSTLLLASF AALLHWSHIT HLFENDRHFS
     HLSTLEREMA FRTEMGLYYS YFKTIVEAPS FLNGVWMIMN DKLTEYPLVI NTLKRFNLYP
     EVILASWYRI YTKIMDLIGI QTKICWTVTR GEGLSPIESC EGLGDPACFY VAVIFMLNGL
     MMALFFIYGT YLSGSRLGGV VTVLCFFFNH GECTRVMWTP PLRESFSYPF LVLQMLLVTH
     ILRAPELCRG SLIALCISNV LFMLPWQFAQ FVLLTQIASL FAVYVVGYID THKLQKIIYM
     HMISLVLCFV LMFGNSMLLT SYYASSLVII WGMLAMKPQF LRMNVSELSL WVIQGCGWLF
     GTVILKSVTS RIFGIADDAH IGNLLTSKFF SYKDFDTLLY TCAAEFDFME KETPLRYTKT
     LLLPVVLVTV AAIVRKIFND MRGVVAKQRT HTRKQQFEHG ELVYHALQLL AYTALGVLIM
     RLKLFLTPHM CVMASLICSR QLFGWLFGKV HPGAVVFAIL AAMSIQGSAN LQTQWNIVGE
     FSNLPQEELI EWIRYSTKPD AVFAGAMPTM ASVKLSALRP VVNHPHYEDA GLRARTKIVY
     SMYSRKAPED VKKELMKLKV NYYILEESWC IRRSKPGCSM PEIWDVEDPD NAGKTPLCNI
     LVKDSKPHFT TVFQNSVYKV LEVLRQ
//
ID   A6XDA6_MOUSE            Unreviewed;       584 AA.
AC   A6XDA6;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   11-JAN-2011, entry version 29.
DE   SubName: Full=cAMP-specific phosphodiesterase 4D isoform 1;
GN   Name=Pde4d;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Swiss Webster;
RX   PubMed=18006274; DOI=10.1016/j.cellsig.2007.10.003;
RA   Chandrasekaran A., Toh K.Y., Low S.H., Tay S.K., Brenner S., Goh D.L.;
RT   "Identification and characterization of novel mouse PDE4D isoforms:
RT   molecular cloning, subcellular distribution and detection of isoform-
RT   specific intracellular localization signals.";
RL   Cell. Signal. 20:139-153(2008).
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DR   EMBL; DQ665891; ABG57272.1; -; mRNA.
DR   IPI; IPI00466648; -.
DR   UniGene; Mm.434429; -.
DR   ProteinModelPortal; A6XDA6; -.
DR   SMR; A6XDA6; 157-517.
DR   STRING; A6XDA6; -.
DR   PRIDE; A6XDA6; -.
DR   Ensembl; ENSMUST00000120664; ENSMUSP00000113024; ENSMUSG00000021699.
DR   MGI; MGI:99555; Pde4d.
DR   HOVERGEN; HBG108239; -.
DR   Bgee; A6XDA6; -.
DR   Genevestigator; A6XDA6; -.
DR   GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006198; P:cAMP catabolic process; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0006939; P:smooth muscle contraction; IMP:MGI.
DR   InterPro; IPR003607; Metal-dep_PHydrolase_HD_dom.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR023174; PDEase_CS.
DR   Gene3D; G3DSA:1.10.1300.10; PDEase_catalytic_dom; 1.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00471; HDc; 1.
DR   PROSITE; PS00126; PDEASE_I; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding.
SQ   SEQUENCE   584 AA;  66394 MW;  CEDFA3A57387798E CRC64;
     MKEQPSCAGT GHPSMAGYGR MAPFELAGGP VKRLRTESSF PCLFAEEAYQ KLASETLEEL
     DWCLDQLETL QTRHSVSEMA SNKFKRMLNR ELTHLSEMSR SGNQVSEYIS NTFLDKQHEV
     EIPSPTQKEK EKKKRPMSQI SGVKKLMHSS SLTNSCIPRF GVKTEQEDVL AKELEDVNKW
     GLHVFRIAEL SGNRPLTVIM HTIFQERDLL KTFKIPVDTL ITYLMTLEDH YHADVAYHNN
     IHAADVVQST HVLLSTPALE AVFTDLEILA AIFASAIHDV DHPGVSNQFL INTNSELALM
     YNDSSVLENH HLAVGFKLLQ EENCDIFQNL TKKQRQSLRK MVIDIVLATD MSKHMNLLAD
     LKTMVETKKV TSSGVLLLDN YSDRIQVLQN MVHCADLSNP TKPLQLYRQW TDRIMEEFFR
     QGDRERERGM EISPMCDKHN ASVEKSQVGF IDYIVHPLWE TWADLVHPDA QDILDTLEDN
     REWYQSTIPQ SPSPAPDDQE EGRQGQTEKF QFELTLEEDC ESDTEKDSGS QVEEDTSCSD
     SKTLCTQDSE STEIPLDEQV EEEAVAEEES QPETCVPDDC CPDT
//
ID   A6ZI46_MOUSE            Unreviewed;       419 AA.
AC   A6ZI46;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   08-MAR-2011, entry version 29.
DE   RecName: Full=Fructose-bisphosphate aldolase;
DE            EC=4.1.2.13;
GN   Name=Aldoa; Synonyms=Aldoart1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CD1; TISSUE=Testis;
RX   PubMed=17659271; DOI=10.1016/j.ydbio.2007.06.010;
RA   Vemuganti S.A., Bell T.A., Scarlett C.O., Parker C.E.,
RA   Pardo-Manuel de Villena F., O'Brien D.A.;
RT   "Three male germline-specific aldolase A isozymes are generated by
RT   alternative splicing and retrotransposition.";
RL   Dev. Biol. 309:18-31(2007).
CC   -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone
CC       phosphate + D-glyceraldehyde 3-phosphate.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC   -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC       family.
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DR   EMBL; EF662061; ABR88097.1; -; mRNA.
DR   IPI; IPI00856272; -.
DR   RefSeq; NP_001186199.1; NM_001199270.1.
DR   UniGene; Mm.317892; -.
DR   ProteinModelPortal; A6ZI46; -.
DR   SMR; A6ZI46; 60-400.
DR   STRING; A6ZI46; -.
DR   PRIDE; A6ZI46; -.
DR   Ensembl; ENSMUST00000087566; ENSMUSP00000084846; ENSMUSG00000030695.
DR   GeneID; 353204; -.
DR   KEGG; mmu:353204; -.
DR   HOGENOM; HBG559178; -.
DR   HOVERGEN; HBG002386; -.
DR   InParanoid; A6ZI46; -.
DR   Bgee; A6ZI46; -.
DR   Genevestigator; A6ZI46; -.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:InterPro.
DR   InterPro; IPR000741; Aldolase_I.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   PANTHER; PTHR11627; Aldolase_I; 1.
DR   Pfam; PF00274; Glycolytic; 1.
DR   PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE   2: Evidence at transcript level;
KW   Glycolysis; Lyase.
SQ   SEQUENCE   419 AA;  45344 MW;  65D7A46D320C26BB CRC64;
     MATHRQDVSI FNMTRLSLAM AFSFPPDANE QPHSGLDNTH QQTKELGKES TTTGTMPCPY
     PALTTEQKKE LSDIAHRIVA PGKGILAADE SIGSMGNRLQ SIGTENTEEN RRFFRQLLLT
     ADDRVNPCIG GVILFHETLY EKADDGRPFP QVIKSKGGVV GIKVDKGVVP LAGTNGETTT
     QGLDGLSERC AQYKKDGADF AKWRCVLKIG KHTPSPLAIM ENANVLARYA SICQQNGIVP
     IVEPEILPDG DHDLSCCQYV TEKVLAAVYK ALSDHHVYLE GTLLKPNMVT PGHACTQKFS
     NEEIAMATVT ALRRTVPPAV PGVTFLSGGQ SEEEASINLN AINKCPLLKP WALTFSYGRA
     LQASALKAWG GKEENLKAAQ EEYIKRALAN SLACQGKYTP SGKTGATASE SLFISNHAY
//
ID   A7BFW0_MOUSE            Unreviewed;       854 AA.
AC   A7BFW0;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   08-MAR-2011, entry version 20.
DE   SubName: Full=SH3-domain GRB2-like interacting protein 1 alpha;
GN   Name=Sgip1; Synonyms=SGIP1alpha;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=17626015; DOI=10.1074/jbc.M703815200;
RA   Uezu A., Horiuchi A., Kanda K., Kikuchi N., Umeda K., Tsujita K.,
RA   Suetsugu S., Araki N., Yamamoto H., Takenawa T., Nakanishi H.;
RT   "SGIP1alpha is an endocytic protein that directly interacts with
RT   phospholipids and Eps15.";
RL   J. Biol. Chem. 282:26481-26489(2007).
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DR   EMBL; AB262964; BAF74784.1; -; mRNA.
DR   IPI; IPI00623241; -.
DR   UniGene; Mm.238094; -.
DR   UniGene; Mm.461880; -.
DR   STRING; A7BFW0; -.
DR   PRIDE; A7BFW0; -.
DR   Ensembl; ENSMUST00000106882; ENSMUSP00000102495; ENSMUSG00000028524.
DR   MGI; MGI:1920344; Sgip1.
DR   GeneTree; ENSGT00510000046419; -.
DR   HOVERGEN; HBG081524; -.
DR   Bgee; A7BFW0; -.
DR   Genevestigator; A7BFW0; -.
DR   GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR008968; Clathrin_mu_C.
DR   InterPro; IPR018808; SAFF_domain.
DR   Pfam; PF00928; Adap_comp_sub; 1.
DR   Pfam; PF10291; SAFF; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   854 AA;  91721 MW;  6759A3924C6EB564 CRC64;
     MMEGLKKRTR KAFGIRKKEK DTDSTGSPDR DGMQGKKKAQ KTQLLLTSCF WLRALSLTLS
     QQPSPHEPPY HSKAECAREG GKKASKKSNG APNGFYAEID WERYNSPELD EEGYSIRPEE
     PGSTKGKHFY SSSESEEEEE SHKKFNIKIK PLQSKDVLKN AATVDELKAS IGNIALSPSP
     VRKSPRRSPG AIKRNLSSEE VARPRRSTPT PELTSKKPLD DTLALAPLFG PPLESAFDEQ
     KTEVLLDQPE IWGSGQPMNP STESPELARP FPTGTPPPLP PKTVPATPPR TGSPLTVATG
     NDQAATEAKI EKLPSISDLD SIFGPVLSPK SVAVNTEEKW VHFSDASPEH VTPELTPREQ
     VVTPPAASDI PADSPAPAPP GPPGSAGPPG PPGPRHVPSP LNLEEVQKKV AEQTFIKDDY
     LETLSSPKEC GLGQRATPPP PPPPTYRTVV SSPGPGSGSG TGTTSGASSP ARPATPLVPC
     STTPPPPPPR PPSRPKLPPG KPGVGDVSRP FSPPIHSSSP PPIAPLARAE STSSISSTNS
     LSAATTPTVE NEQPSLVWFD RGKFYLTFEG SSRGPSPLTM GAQDTLPVAA AFTETVNAYF
     KGADPSKCIV KITGEMVLSF PAGITRHFAN NPSPAALTFR VVNSSRLEHV LPNPQLLCCD
     NTQNDANTKE FWVNMPNLMT HLKKVSEQKP QATYYNVDML KYQVSAQGIQ STPLNLAVNW
     RCEPASTDLR IDYKYNTDAM STAVALNNVQ FLVPIDGGVT KLQAVLPPAV WNAEQQRILW
     KIPDISQKSE NGGVGSLLAR FQLSEGPSKP SPLVVQFTSE GSTLSGCDIE LVGAGYRFSL
     IKKRFAAGKY LADN
//
ID   TM215_MOUSE             Reviewed;         235 AA.
AC   A7E1Z1; Q8C8R5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   08-MAR-2011, entry version 27.
DE   RecName: Full=Transmembrane protein 215;
GN   Name=Tmem215;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
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DR   EMBL; AK044627; BAC32008.1; -; mRNA.
DR   EMBL; AL844182; CAM23301.1; -; Genomic_DNA.
DR   EMBL; BC148227; AAI48228.1; -; mRNA.
DR   EMBL; BC148284; AAI48285.1; -; mRNA.
DR   IPI; IPI00227237; -.
DR   RefSeq; NP_001159481.1; NM_001166009.1.
DR   RefSeq; NP_796149.2; NM_177175.4.
DR   UniGene; Mm.156365; -.
DR   ProteinModelPortal; A7E1Z1; -.
DR   PRIDE; A7E1Z1; -.
DR   Ensembl; ENSMUST00000049655; ENSMUSP00000052129; ENSMUSG00000046593.
DR   GeneID; 320500; -.
DR   KEGG; mmu:320500; -.
DR   CTD; 320500; -.
DR   MGI; MGI:2444167; Tmem215.
DR   eggNOG; maNOG10447; -.
DR   HOGENOM; HBG281100; -.
DR   HOVERGEN; HBG095177; -.
DR   InParanoid; A7E1Z1; -.
DR   OMA; CCYINQS; -.
DR   OrthoDB; EOG4F1X3X; -.
DR   PhylomeDB; A7E1Z1; -.
DR   NextBio; 396853; -.
DR   Bgee; A7E1Z1; -.
DR   Genevestigator; A7E1Z1; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    235       Transmembrane protein 215.
FT                                /FTId=PRO_0000319325.
FT   TRANSMEM     12     32       Helical; (Potential).
FT   TRANSMEM     40     60       Helical; (Potential).
FT   CONFLICT     79     79       K -> R (in Ref. 1; BAC32008).
SQ   SEQUENCE   235 AA;  25812 MW;  57D89C167B4339E5 CRC64;
     MRPDDINPRT GLVVALVSVF LVFGFMFTVS GMKGETLGNI PLLAIGPAIC LPGIAAIALA
     RKTEGCTKWP ENELLWVRKL PCFRKPKDKE VVELLRTPSD LESGKGSSDE LAKKAGLRGK
     QLPQGPGEVP MASSVTTPTP TEEGECQSLV QSGRQEETSR YLDGYCPSAS SLAYSALDAK
     CSAWDRSDRP EPEDSIFFVP QDSIIVCSYK QNSPYDRYCC YINQSQGRWD HETIV
//
ID   A7E1Z5_MOUSE            Unreviewed;      1070 AA.
AC   A7E1Z5;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   08-MAR-2011, entry version 22.
DE   SubName: Full=Electrogenic Na-bicarbonate cotransporter splice variant NBCe1-E;
DE   SubName: Full=Slc4a4 protein;
GN   Name=Slc4a4; Synonyms=slc4a4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Epididymis;
RA   Liu Y., Xu J.-Y., Wang D.-K., Chen L.-M.;
RT   "Cloning of a novel splice variant of electrogenic Na-bicarbonate
RT   cotransporter NBCe1 (slc4a4).";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC148292; AAI48293.2; -; mRNA.
DR   EMBL; HQ204220; ADN95183.1; -; mRNA.
DR   IPI; IPI00918179; -.
DR   RefSeq; NP_001184076.1; NM_001197147.1.
DR   UniGene; Mm.41044; -.
DR   ProteinModelPortal; A7E1Z5; -.
DR   SMR; A7E1Z5; 107-396, 444-485, 911-943.
DR   STRING; A7E1Z5; -.
DR   Ensembl; ENSMUST00000113218; ENSMUSP00000108844; ENSMUSG00000060961.
DR   GeneID; 54403; -.
DR   KEGG; mmu:54403; -.
DR   CTD; 54403; -.
DR   MGI; MGI:1927555; Slc4a4.
DR   HOVERGEN; HBG004326; -.
DR   InParanoid; A7E1Z5; -.
DR   PhylomeDB; A7E1Z5; -.
DR   Bgee; A7E1Z5; -.
DR   Genevestigator; A7E1Z5; -.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:MGI.
DR   GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
DR   GO; GO:0006885; P:regulation of pH; TAS:MGI.
DR   GO; GO:0006814; P:sodium ion transport; IDA:MGI.
DR   InterPro; IPR011531; HCO3_transpt_C.
DR   InterPro; IPR013769; HCO3_transpt_cyt.
DR   InterPro; IPR003020; HCO3_transpt_euk.
DR   InterPro; IPR003024; Na/HCO3_transpt.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   Gene3D; G3DSA:3.40.1100.10; HCO3_transpt_cyt; 1.
DR   PANTHER; PTHR11453; HCO3_transpt_euk; 1.
DR   Pfam; PF07565; Band_3_cyto; 1.
DR   Pfam; PF00955; HCO3_cotransp; 1.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   PRINTS; PR01232; NAHCO3TRSPRT.
DR   SUPFAM; SSF55804; PTrfase/Anion_transptr; 1.
DR   TIGRFAMs; TIGR00834; ae; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1070 AA;  120465 MW;  A17124475438F69A CRC64;
     MEDEAVLDRG ASFLKHVCDE EEVEGHHTIY IGVHVPKSYR RRRRHKRKAG HKEKKEKERI
     SENYSDKSDV ENADESSSSI LKPLISPAAE RIRFILGEED DSPAPPQLFT ELDELLAVDG
     QEMEWKETAR WIKFEEKVEQ GGERWSKPHV ATLSLHSLFE LRTCMEKGSI MLDREASSLP
     QLVEMIADHQ IETGLLKPDL KDKVTYTLLR KHRHQTKKSN LRSLADIGKT VSSASSPAMT
     HRNLTSSSLN DISDKPEKDQ LKNKFMKKLP RDAEASNVLV GEVDFLDTPF IAFVRLQQAV
     MLGALTEVPV PTRFLFILLG PKGKAKSYHE IGRAIATLMS DEVFHDIAYK AKDRHDLIAG
     IDEFLDEVIV LPPGEWDPTI RIEPPKSLPS SDKRKNMYSG GENVQMNGDT PHDGGHGGGG
     HGDCEELQRT GRFCGGLIKD IKRKAPFFAS DFYDALNIQA LSAILFIYLA TVTNAITFGG
     LLGDATDNMQ GVLESFLGTA VSGAIFCLFA GQPLTILSST GPVLVFERLL FNFSKDHNFD
     YLEFRLWIGL WSAFMCLVLV ATDASFLVQY FTRFTEEGFS SLISFIFIYD AFKKMIKLAD
     YYPINSDFKV GYNTHFSCAC LPPDPVNLSV SNDTTLAPED LPTISSTDMY HNVTFDWAYL
     SKKECVKYGG KLVGNNCDFV PDITLMSFIL FLGTYTSSMA MKKFKTSRYF PTTARKLISD
     FAIILSILIF CVIDALVGVD TPKLIVPSEF KPTSPNRGWF VPPFGGNPWW VCLAAAIPAL
     LVTILIFMDQ QITAVIVNRK EHKLKKGAGY HLDLFWVAIL MVVCSFMALP WYVAATVISI
     AHIDSLKMET ETSAPGEQPK FLGVREQRVT GTLVFILTGL SVFMAPILKF IPMPVLYGVF
     LYMGVASLNG VQFMDRLKLL LMPLKHQPDF IYLRHVPLRR VHLFTFLQVL CLALLWILKS
     TVAAIIFPVM ILALVAVRKG MDYLFSQHDL SFLDDVIPEK DKKKKEDEKK KKKKKGSLDS
     DNDDSDCPYS EKVPSIKIPM DIMEQQPFLS DNKPLDRERS STFLERHTSC
//
ID   A7LAI9_MOUSE            Unreviewed;       945 AA.
AC   A7LAI9;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   08-MAR-2011, entry version 20.
DE   SubName: Full=Neuroligin 4*;
GN   Name=Nlgn4l; Synonyms=Nlgn4, Nlgn4x;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   PubMed=18434543; DOI=10.1073/pnas.0801383105;
RA   Bolliger M.F., Pei J., Maxeiner S., Boucard A.A., Grishin N.V.,
RA   Sudhof T.C.;
RT   "Unusually rapid evolution of Neuroligin-4 in mice.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:6421-6426(2008).
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
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DR   EMBL; EF692521; ABS19580.1; -; mRNA.
DR   IPI; IPI00858277; -.
DR   UniGene; Mm.468446; -.
DR   ProteinModelPortal; A7LAI9; -.
DR   SMR; A7LAI9; 28-670.
DR   PRIDE; A7LAI9; -.
DR   HOVERGEN; HBG008839; -.
DR   Genevestigator; A7LAI9; -.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   PANTHER; PTHR11559; CarbesteraseB; 1.
DR   Pfam; PF00135; COesterase; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   945 AA;  97303 MW;  70DBD887284682A7 CRC64;
     MPAPAPALLC LALALASAQP SPPPPPPFPV VATNYGKLRG VRAALPGDVL GPVTQFLGVP
     YAAPPTGERR FQPPEPPSSW AGVRDATRFA PVCPQHLDER ALLRDRLPAW FAANLDAIAA
     YVQDQSEDCL YLNLYVPGGA NGKKMADDVT GNDHGDDQDS RDPGVGGAAA AAARKPVMVY
     IHGGSYMEGT ANIVDGSVLA SYGDVIVVTV NYRLGVLGFL STGDQAAKGN YGLLDQIQAL
     RWVEENAGAF GGDPDRVTVF GSGAGASCVS LLTLSHYSEG LFQKAIIQSG TALSSWAVNY
     QPARYARALG ERVGCATPDP GSPPGSPPGW DSASLVSCLR GKAAGELARA RVTPATYHVA
     FGPTVDGDVI PDDPQILMEQ GEFLNYDIML GVNQGEGARF VDGLGGGHDG GYGGYGGGYG
     GGVEDDEVQD GGPDGAAGGV SAGEFDLAVS GFINDLYGRP EGRGDALRET VKFMYTDWAD
     RDSPEARRKT LVALFTDHQW VAPAVATADL HARYGSPTYF YAFYHRCHGG GGGGGGVDGV
     AGGVAGGVGG EEARPAWADA AHGDEVPYVF GVPMAGPGDV FGCNFSRNDV MLSAVVMTYW
     TNFAKTGDPN QPVAQDTRFV HTRPNRFEEV AWAKYDPRGQ LYLHIGLRPR VRDHYRAAKV
     AFWLELVPHL HGLAADPGAY LSAAATRAAP SGDPDRDPGG GGGGRRRPRP ATRRPAVMTS
     SSMASGSGMT SSSGSGMTSS SGSSASAVLI ETRRDYSTEL SVTIAVGASL LFLNVLAFAA
     LYYKKDKRRH ETHRRPPPPR PPQAPPSAAA ADRNPRPDPG PAGRRGGECG AVVTAMAAEA
     SAGGLGHDGV GGVGVGGVIG GVAGLRLACP PDYALTLRRS PDDVPRAGAG PGAMTLIPGA
     LGGGGGGAVH GFNTFGSGVG VAGVAGVATS QAGPGLPHGH STTRV
//
ID   A7YY80_MOUSE            Unreviewed;       876 AA.
AC   A7YY80;
DT   23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   23-OCT-2007, sequence version 1.
DT   05-OCT-2010, entry version 28.
DE   SubName: Full=Epb4.1l3 protein;
GN   Name=Epb4.1l3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 FERM domain.
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DR   EMBL; BC152548; AAI52549.1; -; mRNA.
DR   IPI; IPI00229300; -.
DR   UniGene; Mm.131135; -.
DR   ProteinModelPortal; A7YY80; -.
DR   SMR; A7YY80; 115-446.
DR   STRING; A7YY80; -.
DR   PRIDE; A7YY80; -.
DR   Ensembl; ENSMUST00000112678; ENSMUSP00000108298; ENSMUSG00000024044.
DR   MGI; MGI:103008; Epb4.1l3.
DR   HOVERGEN; HBG007777; -.
DR   Bgee; A7YY80; -.
DR   Genevestigator; A7YY80; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0019898; C:extrinsic to membrane; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
DR   InterPro; IPR008379; Band_4.1_C.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR021187; Band_41_protein.
DR   InterPro; IPR000798; Ez/rad/moesin.
DR   InterPro; IPR014847; FERM-adjacent.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR007477; SAB.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF05902; 4_1_CTD; 1.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF04382; SAB; 1.
DR   PIRSF; PIRSF002304; Membrane_skeletal_4_1; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   876 AA;  97597 MW;  764B7C26EE8C99C9 CRC64;
     MTTESGSDSE SKPDQEAEPQ EAAGPQGQAG AQPGPEPAGG NGSLNGEKQQ PALEQFPEAA
     AHSTPVKREI GDKDRDFAAA AAKQLEYQQF EDDKLSQRSS SSKLSRSPLK IVKRPKSMQC
     KVTLLDGSEY GCDVDKRSRG QVLFDKVCEH LNLLEKDYFG LTYRDAENQK NWLDPAKEIK
     KQIRSGAWHF SFNVKFYPPD PAQLSEDITR YYLCLQLRDD IVSGRLPCSF VTLALLGSYT
     VQSELGDYDP DECGNDYISE FRFAPNHTKE LEDKVIELHK SHRGMTPAEA EMHFLENAKK
     LSMYGVDLHH AKDSEGVEIM LGVCASGLLI YRDRLRINRF AWPKVLKISY KRNNFYIKIR
     PGEFEQFEST IGFKLPNHRA AKRLWKVCVE HHTFFRLLLP EAPPKKFLTL GSKFRYSGRT
     QAQTRRASAL IDRPAPYFER SSSKRYTMSR SLDGASVSEN HEIYMKDSVS AAEVGTGQYA
     TTKGISQTNL ITTVTPEKKA EEERVEEEDR RKKAEEATPV TALRHEGKTD SERTDTAADG
     ETSATEDLDK TQDELMKHQT NISELKRTFL ETSTETALTN EWEKRLSTSP VRLAARQEDA
     PMIEPLVPEE KLETKTEPVE AEVESTPHPQ PLSTEKVLQE TILVEERHVM SVHASGDASH
     TARDEVDAAE STPTDRRHTG KGKEGSSVTE AAKEQRGEEV DQSAPEQEQP ATVSHEEEQA
     STIRTSEGLE QKSHFESSTV RVESTSVGSI SPGGAKLEIS TKEVPVVHTE TKTITYESSQ
     VDPGADLEPG VLMSAQTITS ETTSTTTTTH ITKTVKGGIS ETRIEKRIVI TGDADIDHDQ
     ALAQAIKEAK EQHPDMSVTK VVVHKETEIT PEDGED
//
ID   A8Y5K6_MOUSE            Unreviewed;       808 AA.
AC   A8Y5K6;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 2.
DT   08-FEB-2011, entry version 23.
DE   SubName: Full=Eukaryotic translation initiation factor 4E nuclear import factor 1;
GN   Name=Eif4enif1; ORFNames=RP23-191E3.3-012;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Dunn M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL671968; CAP19085.2; -; Genomic_DNA.
DR   IPI; IPI00880473; -.
DR   UniGene; Mm.255649; -.
DR   STRING; A8Y5K6; -.
DR   Ensembl; ENSMUST00000120721; ENSMUSP00000112550; ENSMUSG00000020454.
DR   MGI; MGI:1921453; Eif4enif1.
DR   GeneTree; ENSGT00390000012071; -.
DR   HOVERGEN; HBG023298; -.
DR   Bgee; A8Y5K6; -.
DR   Genevestigator; A8Y5K6; -.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR018862; eIF4E_transporter.
DR   Pfam; PF10477; EIF4E-T; 2.
PE   4: Predicted;
KW   Initiation factor; Protein biosynthesis.
SQ   SEQUENCE   808 AA;  87882 MW;  F9F027DFAE0C508E CRC64;
     MEKSVAETEN GDAFLELKKL PTSKSPHRYT KEELLDIKER PYSKQRPSCL SEKYDSDGVW
     DPEKWHASLY PASGRSSPVE SLKKESESDR PSLVRRIAGI VECNGGVAEE DEVEVILAQE
     PSADQEVPRD VILPEQSPGE FDFNEFFNLD KVPCLASMIE DVLGEGSVSA SRFSRWFSNP
     SRSGSRSSSL GSTPHEELER LAGLEQAVLS PGQNSGNYFA PIPSEDHAEN KVDILEMLQK
     AKVDLKPLLS SLSANKEKLK ESSHSGVVLS VEEVEAGLKG LKVDQQMKNS TPFMAEHLEE
     TLSAASSNRQ LKKDGDMTAF NKLVNTMKRN VESHLLAPAE IPGQPVSKNI LQELLGQPVQ
     RPASSNLLSG LMGSLEATAS LLSQRAPSPP MSQVFRTQAA SADYLHPRIP SPIGFPSGPQ
     QLLGDPFQGM RKPMSPVSAQ MSQLELQQAA LEGLALPHDL AVQTAPFYQP GFSKPQVDRT
     RDGLRNRQQR MSKSPAPMHG GNSSSPAPAA SITSMLSPSF TPTSVIRKMY ESREKTKEEM
     APGMVVPGDG KEDTQKTSEE NLLSSNPIPN TDQDSSTTNP KLSTLQRSSC STPLSQTSRY
     TKEQDYRPKT AGRKTPTLAS PVPGTPFLRP THQVPLVPHV PIVRPAHQLH PGLVQRLIAQ
     GVHPQHLPSL LQAGVLPPGI DMAPLQGLSG PLLGQPLYPL VSAASHPLLN PRPGTPLHLA
     VMQQQLQRSV LHPPGSSSQA AAISVQTPQN VPSRSGMPHM HSQLEHRTSQ RSSSPVGLAK
     WFGSDVLQQP LPSMPTKVIS VDELEYRQ
//
ID   A9C437_MOUSE            Unreviewed;       891 AA.
AC   A9C437;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   08-FEB-2011, entry version 23.
DE   SubName: Full=Chloride channel 2;
GN   Name=Clcn2; ORFNames=RP23-101H1.9-005;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Johnson C.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CT010490; CAP19213.1; -; Genomic_DNA.
DR   EMBL; AC087898; CAP19213.1; JOINED; Genomic_DNA.
DR   IPI; IPI00882352; -.
DR   UniGene; Mm.177761; -.
DR   ProteinModelPortal; A9C437; -.
DR   SMR; A9C437; 98-550, 559-834.
DR   STRING; A9C437; -.
DR   PRIDE; A9C437; -.
DR   Ensembl; ENSMUST00000120099; ENSMUSP00000112759; ENSMUSG00000022843.
DR   MGI; MGI:105061; Clcn2.
DR   GeneTree; ENSGT00550000074179; -.
DR   HOVERGEN; HBG005332; -.
DR   Bgee; A9C437; -.
DR   Genevestigator; A9C437; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005247; F:voltage-gated chloride channel activity; IMP:MGI.
DR   GO; GO:0060689; P:cell differentiation involved in salivary gland development; IMP:MGI.
DR   InterPro; IPR002244; Cl-channel-2.
DR   InterPro; IPR014743; Cl-channel_core.
DR   InterPro; IPR001807; Cl-channel_volt-gated.
DR   InterPro; IPR000644; Cysta_beta_synth_core.
DR   Gene3D; G3DSA:1.10.3080.10; Cl-channel_core; 1.
DR   PANTHER; PTHR11689; Cl-channel_volt; 1.
DR   Pfam; PF00571; CBS; 1.
DR   Pfam; PF00654; Voltage_CLC; 1.
DR   PRINTS; PR00762; CLCHANNEL.
DR   PRINTS; PR01113; CLCHANNEL2.
DR   SMART; SM00116; CBS; 1.
DR   SUPFAM; SSF81340; Cl-channel_core; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   4: Predicted;
KW   Membrane; Transmembrane; Transmembrane helix.
SQ   SEQUENCE   891 AA;  97698 MW;  B90815D3B718C083 CRC64;
     MAAATAAAAA AAAAGEGMEP RALQYEQTLM YGRYTQELGA FAKEEAARIR LGGPEPWKGS
     PSARATPELL EYGQSRCARC RICSVRCHKF LVSRVGEDWI FLVLLGLLMA LVSWAMDYAI
     AVCLQAQQWM SRGLNTNILL QYLAWVTYPV VLITFSAGFT QILAPQAVGS GIPEMKTILR
     GVVLKEYLTL KTFVAKVIGL TCALGSGMPL GKEGPFVHIA SMCAALLSKF LSLFGGIYEH
     ESRNTEMLAA ACAVGVGCCF AAPIGGVLFS IEVTSTFFAV RNYWRGFFAA TFSAFIFRVL
     AVWNRDEETI TALFKTRFRL DFPFDLQELP AFAVIGIASG FGGALFVYLN RKIVQVMRKQ
     KTINRFLMRK RLLFPALVTL LISTLTFPPG FGQFMAGQLS QKETLVTLFD NRTWVRQGLV
     EDLELPSTSQ AWSPPRANVF LTLVIFILMK FWMSALATTI PVPCGAFMPV FVIDGIHTDS
     STYRIVPGGY AVVGAAALAG AVTHTVSTAV IVFELTGQIA HILPVMIAVI LANAVAQSLQ
     PSLYDSIIRI KKLPYLPELG WGRHQQYRVR VEDIMVRDVP HVALSCTFRD LRLALHRTKG
     RMLALVESPE SMILLGSIER SQVVALLGAQ LSPARRRQHM QKLRKAQLSP PSDQESPPSS
     ETSIRFQVNT EDSGFSGAHG QTHKPLKPAL KRGPSNSTSL QEGTTGNMES AGIALRSLFC
     GSPPLEATSE LEKSESCDKR KLKRVRISLA SDSDPEAEMS PEEILEWEEQ QLDEPVNFSD
     CKIDPAPFQL VERTSLHKTH TIFSLLGVDH AYVTSIGRLI GIVTLKELRK AIEGSVTAQG
     VKVRPPLASF RDSATSSSDT ETTEVHALWG PRSRHGLPRE GTPSDSDDKC Q
//
ID   A9UGK3_MOUSE            Unreviewed;       620 AA.
AC   A9UGK3;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   08-FEB-2011, entry version 26.
DE   SubName: Full=RAN binding protein 10;
DE   SubName: Full=Ran binding protein 10;
GN   Name=Ranbp10; ORFNames=mCG_20477;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=18347012; DOI=10.1074/jbc.M709397200;
RA   Schulze H., Dose M., Korpal M., Meyer I., Italiano J.E.Jr.,
RA   Shivdasani R.A.;
RT   "RanBP10 Is a Cytoplasmic Guanine Nucleotide Exchange Factor That
RT   Modulates Noncentrosomal Microtubules.";
RL   J. Biol. Chem. 283:14109-14119(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 CTLH domain.
CC   -!- SIMILARITY: Contains 1 LisH domain.
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DR   EMBL; EU281316; ABX79150.1; -; mRNA.
DR   EMBL; CH466525; EDL11314.1; -; Genomic_DNA.
DR   IPI; IPI00320594; -.
DR   UniGene; Mm.4206; -.
DR   ProteinModelPortal; A9UGK3; -.
DR   SMR; A9UGK3; 64-220.
DR   STRING; A9UGK3; -.
DR   Ensembl; ENSMUST00000041400; ENSMUSP00000040045; ENSMUSG00000037415.
DR   MGI; MGI:1921584; Ranbp10.
DR   HOVERGEN; HBG053444; -.
DR   InParanoid; A9UGK3; -.
DR   Bgee; A9UGK3; -.
DR   Genevestigator; A9UGK3; -.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IDA:MGI.
DR   GO; GO:0048487; F:beta-tubulin binding; IDA:MGI.
DR   GO; GO:0008536; F:Ran GTPase binding; IPI:MGI.
DR   GO; GO:0005087; F:Ran guanyl-nucleotide exchange factor activity; IDA:MGI.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR   InterPro; IPR001870; B302/SPRY.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR006595; CTLH_C.
DR   InterPro; IPR006594; LisH_dimerisation.
DR   InterPro; IPR013720; LisH_dimerisation_sub.
DR   InterPro; IPR013144; Ran-bd_prot-like_CRA_domain.
DR   InterPro; IPR019589; Ran-bd_prot_CRA_domain.
DR   InterPro; IPR018355; SPla/RYanodine_receptor_sg.
DR   InterPro; IPR003877; SPRY_rcpt.
DR   Pfam; PF08513; LisH; 1.
DR   Pfam; PF10607; RanBPM_CRA; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   SMART; SM00757; CRA; 1.
DR   SMART; SM00668; CTLH; 1.
DR   SMART; SM00667; LisH; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50897; CTLH; 1.
DR   PROSITE; PS50896; LISH; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   620 AA;  67188 MW;  6A22ADAECC7B57F5 CRC64;
     MAAATADPGA GNPQAGDSSG GDSGGGLPSP GEQELSRRLQ RLYPAVNQHE TPLPRSWSPK
     DKYNYIGLSQ GNLRVHYKGH GKNHKDAASV RATHPIPAAC GIYYFEVKIV SKGRDGYMGI
     GLSAQGVNMN RLPGWDKHSY GYHGDDGHSF CSSGTGQPYG PTFTTGDVIG CCVNLINGTC
     FYTKNGHSLG IAFTDLPANL YPTVGLQTPG EIVDANFGQQ PFLFDIEDYM REWRAKVQGT
     VHGFPISARL GEWQAVLQNM VSSYLVHHGY CSTATAFARM TETPIQEEQA SIKNRQKIQK
     LVLEGRVGEA IETTQRFYPG LLEHNPNLLF MLKCRQFVEM VNGTDSEVRS LSSRSPKSQD
     SYPGSPSLSP RHGPSSSHIH NTGADSPSCS NGVASTKNKQ NHSKYPAPSS SSSSSSSSSS
     SSPSSVNYSE SNSTDSTKSQ PHSSTSNQET SDSEMEMEAE HYPNGVLESV STRIVNGAYK
     HDDLQTDESS MDDGHPRRQL CGGNQAATER IILFGRELQA LSEQLGREYG KNLAHTEMLQ
     DAFSLLAYSD PWSCPVGHQL DPIQREPVCA ALNSAILESQ NLPKQPPLML ALGQASECLR
     LMARAGLGSC SFARVDDYLH
//
ID   VW5B1_MOUSE             Reviewed;        1215 AA.
AC   A9Z1V5; Q6PFX4; Q9CUE8;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   08-MAR-2011, entry version 30.
DE   RecName: Full=von Willebrand factor A domain-containing protein 5B1;
DE   Flags: Precursor;
GN   Name=Vwa5b1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1209.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Secreted (Potential).
CC   -!- SIMILARITY: Contains 1 VIT domain.
CC   -!- SIMILARITY: Contains 1 VWFA domain.
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DR   EMBL; BC057376; AAH57376.1; -; mRNA.
DR   EMBL; BC132477; AAI32478.2; -; mRNA.
DR   EMBL; AK016425; BAB30227.1; -; mRNA.
DR   IPI; IPI00137148; -.
DR   RefSeq; NP_083677.1; NM_029401.1.
DR   UniGene; Mm.251530; -.
DR   ProteinModelPortal; A9Z1V5; -.
DR   PhosphoSite; A9Z1V5; -.
DR   PRIDE; A9Z1V5; -.
DR   Ensembl; ENSMUST00000030533; ENSMUSP00000030533; ENSMUSG00000028753.
DR   GeneID; 75718; -.
DR   KEGG; mmu:75718; -.
DR   CTD; 75718; -.
DR   MGI; MGI:1922968; Vwa5b1.
DR   eggNOG; roNOG05883; -.
DR   HOGENOM; HBG446040; -.
DR   HOVERGEN; HBG095596; -.
DR   InParanoid; A9Z1V5; -.
DR   OMA; PACLFNI; -.
DR   OrthoDB; EOG41RPT4; -.
DR   NextBio; 343770; -.
DR   Bgee; A9Z1V5; -.
DR   Genevestigator; A9Z1V5; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR013694; VIT.
DR   InterPro; IPR002035; VWF_A.
DR   Pfam; PF00092; VWA; 1.
DR   SMART; SM00327; VWA; 1.
DR   PROSITE; PS51468; VIT; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Phosphoprotein; Secreted; Signal.
FT   SIGNAL        1     18       Potential.
FT   CHAIN        19   1215       von Willebrand factor A domain-containing
FT                                protein 5B1.
FT                                /FTId=PRO_0000326174.
FT   DOMAIN       19    141       VIT.
FT   DOMAIN      353    532       VWFA.
FT   COMPBIAS    592    595       Poly-Ser.
FT   COMPBIAS    641    644       Poly-Arg.
FT   MOD_RES     879    879       Phosphotyrosine (By similarity).
FT   CARBOHYD    132    132       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    538    538       F -> L (in Ref. 2; BAB30227).
SQ   SEQUENCE   1215 AA;  133972 MW;  60DA7146EB08FDD6 CRC64;
     MPGLLNCLTG AALPLMESDV TSYVSGYALG LTASLTYGNL EAQPFQGLFV YPIDEYSTVV
     GFEAVIADRV VTIQLRDKAK LDRSHLDIQP ATVTGNFPEE ESPIAPGKVT LDEDLERVLF
     VVNLGTIAPM ENVTVFISTS SELPTLPSGA VRVLLPAICA PTVPPSCTHR FGSSSPQPQG
     KDPHCFGTQT KDSYNRLCLA TLLDTKVTNP MEYEFKFQLE IRGPCLLAGV ESPTHEIRAD
     AAPSAHSAKS IIITLAKKHT FDRPVEILLH PSEPHMPHVL VEKGDMTLGE YDQHLKGKAD
     FIRGTKKDNS AERKTEVIRK RLHKDIPHHS VIMLNFCPDL QSVQPNPRKA HGEFIFLIDR
     SNSMSKTNIQ CIKEAMLVAL KSLMPACFFN IIGFGSTFKA VFASSRIYNE ENLTMACDCI
     QRMQADMGGT NMLSPLKWVL RQPLRRGHPR LLFLITDGSV NNTGKVLELV RNHASSTRCY
     SFGIGPTVCY RLVKGLASVS KGSAEFLMEG ERLQPKMVKS LKKAMAPVLS DVTVEWVFPE
     TTEALISPVS TSSLFPGERL MGYGIVCDAS LYISNSRSDK RRKYGMLHTQ ESSSSVFYPS
     QDEGLSPGSG NCAKNVNQGQ TKDAHPCNGD SPTHHGLDVS RRRRAYSTNQ ISSHKTCPRA
     TTASDPTGTA RRYPLRKAKV QDLASESDWE SQKWQTDLQT LLNEGHNLSQ GPKLHGPGAR
     RPSLLPQGCQ LMRFFDQKPQ AWGPVRELDC GASRTSAPNS QSSEDLAIEP AHCPSTFERE
     TSLDLEPMAE SEEQANPCRT ATPSPVVGKA LVKGLCANQR MQWEVSFELE PPALKRGDTQ
     NADMWSETFH HLAARAIIRE FEHLAEREDE IELGSNRRYQ VNAVHTSKAC SVISKYTAFV
     PVDINKRQYL PTVVKYPNSG AMLSFRNLTR QWGGSSAGLG RPQSMLREHS SAAGDSKFQT
     LALQDSPTST FNKTPSPGHE KQTTAEGPPQ NLSASAPSSM KATETLFGSK LNLNKSRLLT
     RATKGFLSKS LPKASEATPG SQSSDYIPLV SLQLASGAFL LNEAFCTTIQ IPMEKLKWTS
     PFSCLRMSLV TRRQDLKTQS PQDCTSLSSS PPSCDGISLK SEESSDQESN AMLEHMGKLW
     ATVVALAWLE HSSANYIIEW ELVAAKASSW VEKQKVPEGR TLSTLKNTAR QLFVLLRHWD
     EKLEFNMLCY NPNYV
//
ID   B0EVI6_MOUSE            Unreviewed;       607 AA.
AC   B0EVI6;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   02-NOV-2010, entry version 17.
DE   SubName: Full=Ancient conserved domain protein 1;
GN   Name=Cnnm1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MF1; TISSUE=Brain;
RA   Alderton A., Davies P., Illman K., Brown D.R.;
RT   "Ancient conserved domain protein-1 (ACDP-1) is a copper binding
RT   protein that modifies cellular retention of copper.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; EF041508; ABM65697.1; -; mRNA.
DR   IPI; IPI00120943; -.
DR   UniGene; Mm.329864; -.
DR   ProteinModelPortal; B0EVI6; -.
DR   STRING; B0EVI6; -.
DR   Ensembl; ENSMUST00000026195; ENSMUSP00000026195; ENSMUSG00000025189.
DR   MGI; MGI:1891366; Cnnm1.
DR   HOVERGEN; HBG074775; -.
DR   InParanoid; B0EVI6; -.
DR   Bgee; B0EVI6; -.
DR   Genevestigator; B0EVI6; -.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   InterPro; IPR000644; Cysta_beta_synth_core.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 2.
DR   PROSITE; PS51371; CBS; 2.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   607 AA;  68517 MW;  B8ED1AF7F9FF9881 CRC64;
     MAAAFPVCYP LGRLLDWALR QEISTFYTRE KLLETLRAAD PYSDLVKEEL NIIQGALELR
     TKVVEEVLTP LGDCFMLRSD AVLDFATVSE ILRSGYTRIP VYEGDQRHNI VDILFVKDLA
     FVDPDDCTPL LTVTRFYNRP LHCVFNDTRL DTVLEEFKKG KSHLAIVQRV NNEGEGDPFY
     EVMGIATLED IIEEIIKSEI LDETDLYTDN RKKQRVPHRE RRRHDFSLFK LSDSEIRVKI
     SPQLLLATHR FMATEVEPFK SLYLSEKILL RLLKHPNVIQ ELKFDERNKK APEHYLYQRN
     RPVDYFVLLL QGKVEVEVGK EGLRFENGAF TYYGVPAIMT SACSDNDVRK VGSLAGSSVF
     LPVSVSRTFA FSRGDSLAGS PVNRSPSRCS GLNRSESPNR ERSDFGGSNT QLYSSSNNLY
     TPDYSVHILS DVQFVKITRQ QYQNALTACH MDSSPQSPDM EAFTDGDSTK APTTRGTPQT
     PKDDPVLTLL GNRTSLPCSR SDGLRSPGEV VYLRMEEMAF PQEEMPNFEE HRLQQVSLSP
     VAVPTTAASD PECCNIHLDP EASPCSSDSE ENMGKKLLRT LSGRKRKKSA DGERASEENS
     NLTPLIT
//
ID   B0QZJ2_MOUSE            Unreviewed;       136 AA.
AC   B0QZJ2;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 16.
DE   SubName: Full=Zinc finger and BTB domain containing 4;
DE   Flags: Fragment;
GN   Name=Zbtb4; ORFNames=RP23-422L16.16-007;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Pearce A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL603707; CAQ12835.1; -; Genomic_DNA.
DR   IPI; IPI00856656; -.
DR   UniGene; Mm.426361; -.
DR   STRING; B0QZJ2; -.
DR   Ensembl; ENSMUST00000156932; ENSMUSP00000115687; ENSMUSG00000018750.
DR   MGI; MGI:1922830; Zbtb4.
DR   GeneTree; ENSGT00530000063209; -.
DR   Bgee; B0QZJ2; -.
DR   Genevestigator; B0QZJ2; -.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR013069; BTB_POZ.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF00651; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
PE   4: Predicted;
FT   NON_TER     136    136
SQ   SEQUENCE   136 AA;  14552 MW;  E94C1203894E5673 CRC64;
     MPPPAEVTDP SHAPAVLHQL NEQRLRGLFC DVTLIAGDTK FPAHRSVLAK GRNLRAGRTL
     TYTAKPVGGL SGSGGSPTGT GRGSSQLQAP PPLCQITVRI GEEAIVKRRI SETDLRPGEL
     SGEEVEESEE EEEEEE
//
ID   B0QZW4_MOUSE            Unreviewed;       406 AA.
AC   B0QZW4;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-FEB-2011, entry version 19.
DE   SubName: Full=Suppressor of Ty 3 homolog (S. cerevisiae);
DE   Flags: Fragment;
GN   Name=Supt3h; ORFNames=AC164546.1-003;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Pearce A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Clark S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL672242; CAQ11504.1; -; Genomic_DNA.
DR   EMBL; AC154500; CAQ11504.1; JOINED; Genomic_DNA.
DR   EMBL; AC164546; CAQ11504.1; JOINED; Genomic_DNA.
DR   EMBL; CT573363; CAQ11504.1; JOINED; Genomic_DNA.
DR   EMBL; CT573363; CAQ11936.1; -; Genomic_DNA.
DR   EMBL; AC154500; CAQ11936.1; JOINED; Genomic_DNA.
DR   EMBL; AC164546; CAQ11936.1; JOINED; Genomic_DNA.
DR   EMBL; AL672242; CAQ11936.1; JOINED; Genomic_DNA.
DR   IPI; IPI00886094; -.
DR   STRING; B0QZW4; -.
DR   Ensembl; ENSMUST00000129416; ENSMUSP00000120197; ENSMUSG00000038954.
DR   MGI; MGI:1923723; Supt3h.
DR   GeneTree; ENSGT00390000010738; -.
DR   HOGENOM; HBG714135; -.
DR   HOVERGEN; HBG058560; -.
DR   InParanoid; B0QZW4; -.
DR   Bgee; B0QZW4; -.
DR   Genevestigator; B0QZW4; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003702; F:RNA polymerase II transcription factor activity; IEA:InterPro.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; IEA:InterPro.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR003195; TFIID-18.
DR   Gene3D; G3DSA:1.10.20.10; Histone-fold; 1.
DR   PANTHER; PTHR11380; TFIID-18; 1.
DR   Pfam; PF02269; TFIID-18kDa; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
PE   4: Predicted;
FT   NON_TER       1      1
FT   NON_TER     406    406
SQ   SEQUENCE   406 AA;  44926 MW;  76EDCEEED26BACA3 CRC64;
     PMSTTTSSSG RNAGKTISFA AELQSMMFSL GDARRPLHET AVLVEDVVHT QLINLLQQAA
     EVSQLRGARV ISAEDLLFLM RKDKKKLRRL LKYMFIRDYK SKIIKGIDED DLLEEKLSGS
     SGTNKRQKIA QDLINSIDQT GELLAMFEDN ELDDVKQERM ERAERQTRTM DSAQYAEFCE
     SRQLSFSKKA SKFRDWLDCS SMEIKPNVIA MEILAYLAYE TVAQLVDLAL LVRQDMVSKA
     GDPFSHAISA TFIQYHNSAE GSSCLKSSPD SPENTPPPTP TAPSSGSQHS GRAASGSLGN
     GNTGQDTAKT KQRKRKKSTA ACGVEAHSDA IQPCHIREAI RRYGHKIGPL SPFTISLSLT
     ECLPKEWDGF PGLLRGPWPC LPPRRGSGSP RSFLPVLPEN KIGFYV
//
ID   B0V2M3_MOUSE            Unreviewed;      2237 AA.
AC   B0V2M3;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 25.
DE   SubName: Full=Zinc finger protein 318;
GN   Name=Zfp318; ORFNames=RP24-201F8.1-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Phillimore B.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CT009572; CAQ11965.1; -; Genomic_DNA.
DR   EMBL; AC151275; CAQ11965.1; JOINED; Genomic_DNA.
DR   IPI; IPI00282808; -.
DR   RefSeq; NP_997554.2; NM_207671.3.
DR   UniGene; Mm.439916; -.
DR   ProteinModelPortal; B0V2M3; -.
DR   STRING; B0V2M3; -.
DR   PRIDE; B0V2M3; -.
DR   Ensembl; ENSMUST00000113481; ENSMUSP00000109109; ENSMUSG00000015597.
DR   GeneID; 57908; -.
DR   KEGG; mmu:57908; -.
DR   CTD; 57908; -.
DR   MGI; MGI:1889348; Zfp318.
DR   HOGENOM; HBG282587; -.
DR   HOVERGEN; HBG107139; -.
DR   InParanoid; B0V2M3; -.
DR   OMA; QPLTRLC; -.
DR   NextBio; 314073; -.
DR   Bgee; B0V2M3; -.
DR   Genevestigator; B0V2M3; -.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR003604; Znf_U1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SMART; SM00451; ZnF_U1; 2.
PE   4: Predicted;
SQ   SEQUENCE   2237 AA;  246324 MW;  97B600577866BA14 CRC64;
     MYRSGSRSSV SSHRSKDGSA SGPPPGRPVG ASSGPTRRPS SPPPPSCSSL RLPARRHRSP
     SGHRGRWASP SPPRGRRGSP SPPRGRRASP SPTRGRRASP SPPRGRRGSP SPPRARRGSP
     SPPRSRRHYP PGLGGFRGSI RGESRADFAR DGRGDHPGGG GGSRRRSPGL CSDSSLEESL
     RITVGNDHFC VSTPERRRLS DRLGSPVDGL QDMDRDDLTD DSVFTRSSQC SRGLERYISR
     EEGPLSPFLG QLDEDYRTRE TFLHRPEFSP QSSCHDELLR GTERNRDKLK SSSYSIRSEE
     RSREAKRPRY DDTEKVHSSG GDHSSFTSGT RNYRQRRSSP SPRFLDPEFR ELDLARRKRE
     EEEEQSRSLS QELVGVGDDQ IGCSIPGLAG VLTTSEPGYS LQRPEEVPMM PKKSILKKRI
     EADMKPSLQL ESFSSGASSG EDHPLYSEHS PLPLSGAIAA FTSEIENKGT TVEADLKEPQ
     SNLYQWGPLR EIPKDNSEKF DSFLGFKEKL DLKAEGLEQQ TDFLLPHERA SQDGSGFSRI
     LSMLADPTIT QEKRRRSFPD IEDEEKFLYG DEEEDIKSES PLKSLEDPES AGTRQKANSL
     PSTPAVKLES LEESNPEYAK IHNLLKTIGL DIGVAEIGKL AARTQERLHG KKPSSRPSAD
     RRLSADRHLS GDRHFSADRC SSVEHSFTAD WRSSDPHRPE SRETHHSNTQ SPEVSHPHPA
     SPVDPYLRTK NSPPFLKSDH PVCHVSGPEV VGSGFQSSVA VRCMLPSAPS TPIRLPHSAA
     LSQFHIPGAS QFAAARIPPN YQGSVIPSAS FDAYRHYMAY AASRWPMYPA SQPPSHPLSD
     PHRLLPVTKQ AARSRPNLRV IPTVTPAKPK QEIPVLGSIS VKRIPVRVSI PSLIKYNPKK
     ISDEKNRASQ KQKVIEEREK LKTEQEARQK KMFYLTTELE RLHKQQGEML RKKRREKDGH
     KDPLLMEVSR LQDSIMKDIA ELHKETEEAE KKQSELDKVA QILGIDIFDK SLKSSNDSKE
     STEKPEKEKS KSPEKELSPS NSSSSNKESK MNEKSCIKSP SSTESLQPTV KQSDQPVAAY
     EYYDAGSHWC KDCNTTCGTM FDFFTHMHNK KHTQTLDPYN RPWASKTQSE AKQDTVKRTD
     KITVPAKGSE FLIPVTGFYC QLCEEFLGDP ISGEQHVKGH QHNENYKKYV EENPLYEERR
     NLDRQAGLAV VLETERRRQN ELKRKLNEKP KEEKIEKKAR IVREVKEDDK APGELEEQLS
     EDGSAPEKGE VKGNASLRPQ VKEEVKKEPS VASIAASFGK FSWKKPEKEE EKGSVVTPGA
     PKEDTVETSK DRDDGKAEVG KAKPIKIKLS GKTVIAHTSP WTPVVTTSTQ TKIRPNLPIP
     STVLRKSGSA TVSKPAPLNT FLSIKSSGTS TKPLPVVKES SSDLLLPPDI ISKAFGGEEV
     VLKGSPEEKV ELAEKNEPSQ VPEQMLALLP PPPPPPPPPP PPPPPPPPQA VPQLSAPSPA
     QANVVLTPVK SNSVISQTFS LGFQGPNILN PGLPVAFMAS EQPTVIPSDE TAPGVSESDW
     DQTLISMLVR PPPPLSSVFS EQAKKLEKRN SCLATANAKD LYDIFYSSGG KGAHETKLSS
     STLANGESSS LPRTESSDFS STCTLNSSMS SEDLPQCSAL VTATEISNLE NPISKGMEST
     GKWSVVDQID PKSRDSTYSF LQPLTRLYQN KPYEIVSPKT DTLVMWTSGS SQNDTHKDRP
     PEGKIRFDLG EPGPPGTDST SHLSDTHCQT NGPQKLIEIN LIDNQNKNQE VYQSEGCRES
     EMKRKTELKG KVATEEEEEE EEEGANSIED SNSNHGNRNT WEGEIGQPKL STVDKKGEQS
     SKLMTGHENT SKVVIELSPS LPSKRTKIDL FPSLLQNPKS MPELLLLSPA GSGLCLKRQE
     IWERPEKPGL EDVELQGTRP ELTVTIESKV LENFDTTHLE VEGFASLRNL GDMHANFHNS
     QTEQTRRSPT ALSEKMSEEI SVSSVMCNPS SSSDIEPVPS FSGFPLESPK TLVLNFETEG
     AHSSSNSRNG RITSNSLETG HPVENVGHDL GGERTHQALD LLAGGMLSED VKETSPLQKD
     LLRMESTTVS PSGLGPSPCL PDLVDFVTRT PGVPKQKPCS PLSEPDAFLK CSSLEMGSPP
     PEILSVSVSE VAVPQVSEDN DSALNLVKTP PSGSPSRDQV VGGNVSPREM PEQEAAVDVI
     PDHTRSNVYN SQDYLNG
//
ID   PTPRS_MOUSE             Reviewed;        1907 AA.
AC   B0V2N1; Q3TEC3; Q3TXC9; Q4JFC7; Q5XJV4; Q64503; Q64699; Q7TT17;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 31.
DE   RecName: Full=Receptor-type tyrosine-protein phosphatase S;
DE            Short=R-PTP-S;
DE            EC=3.1.3.48;
DE   AltName: Full=PTPNU-3;
DE   AltName: Full=Receptor-type tyrosine-protein phosphatase sigma;
DE            Short=R-PTP-sigma;
DE   Flags: Precursor;
GN   Name=Ptprs;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 6), DEVELOPMENTAL STAGE,
RP   AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Embryonic kidney;
RX   MEDLINE=95112841; PubMed=7529177;
RX   DOI=10.1111/j.1432-1033.1994.00773.x;
RA   Wagner J., Boerboom D., Tremblay M.L.;
RT   "Molecular cloning and tissue-specific RNA processing of a murine
RT   receptor-type protein tyrosine phosphatase.";
RL   Eur. J. Biochem. 226:773-782(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Thymus;
RA   Ogata M., Sawada M., Hamaoka T.;
RT   "Expression of a novel murine receptor protein tyrosine phosphatase in
RT   the thymus.";
RL   Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1337-1907.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Interacts with LAR-interacting protein LIP.1 (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- SUBUNIT: Interacts with PPFIA1, PPFIA2 and PPFIA3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=B0V2N1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=B0V2N1-2; Sequence=VSP_036062;
CC       Name=3;
CC         IsoId=B0V2N1-3; Sequence=VSP_036058, VSP_036059;
CC       Name=4;
CC         IsoId=B0V2N1-4; Sequence=VSP_036058, VSP_036059, VSP_036061;
CC       Name=5;
CC         IsoId=B0V2N1-5; Sequence=VSP_036057;
CC       Name=6;
CC         IsoId=B0V2N1-6; Sequence=VSP_036060;
CC   -!- TISSUE SPECIFICITY: Isoform 1 and isoform 6 are predominantly
CC       expressed in the brain (cerebrum and cerebellum) and to a lesser
CC       extent in the heart and skeletal muscle. Also found in neuronal-
CC       derived cell lines.
CC   -!- DEVELOPMENTAL STAGE: Expression is seen in embryos between 8 dpc
CC       and 16 dpc and a peak expression is seen at 14 dpc.
CC   -!- PTM: A cleavage occurs, separating the extracellular domain from
CC       the transmembrane segment. This process called 'ectodomain
CC       shedding' is thought to be involved in receptor desensitization,
CC       signal transduction and/or membrane localization (By similarity).
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 2A subfamily.
CC   -!- SIMILARITY: Contains 8 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 3 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SIMILARITY: Contains 2 tyrosine-protein phosphatase domains.
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DR   EMBL; X82288; CAA57732.1; -; mRNA.
DR   EMBL; D28530; BAA05886.1; -; mRNA.
DR   EMBL; AK159320; BAE34987.1; -; mRNA.
DR   EMBL; AK169714; BAE41325.1; -; mRNA.
DR   EMBL; CT009637; CAQ12196.1; -; Genomic_DNA.
DR   EMBL; CT009637; CAQ12197.1; -; Genomic_DNA.
DR   EMBL; BC052462; AAH52462.1; -; mRNA.
DR   EMBL; BC083188; AAH83188.1; -; mRNA.
DR   IPI; IPI00230067; -.
DR   IPI; IPI00467688; -.
DR   IPI; IPI00754853; -.
DR   IPI; IPI00915502; -.
DR   IPI; IPI00915505; -.
DR   IPI; IPI00915512; -.
DR   RefSeq; NP_035348.2; NM_011218.2.
DR   UniGene; Mm.258771; -.
DR   ProteinModelPortal; B0V2N1; -.
DR   SMR; B0V2N1; 28-1086, 1326-1901.
DR   STRING; B0V2N1; -.
DR   PRIDE; B0V2N1; -.
DR   Ensembl; ENSMUST00000067538; ENSMUSP00000064048; ENSMUSG00000013236.
DR   GeneID; 19280; -.
DR   KEGG; mmu:19280; -.
DR   CTD; 19280; -.
DR   MGI; MGI:97815; Ptprs.
DR   HOVERGEN; HBG053758; -.
DR   InParanoid; B0V2N1; -.
DR   OMA; VPGQPMN; -.
DR   OrthoDB; EOG44J2H5; -.
DR   PhylomeDB; B0V2N1; -.
DR   NextBio; 296192; -.
DR   Bgee; B0V2N1; -.
DR   Genevestigator; B0V2N1; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 11.
DR   Pfam; PF00041; fn3; 6.
DR   Pfam; PF07679; I-set; 3.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 8.
DR   SMART; SM00408; IGc2; 3.
DR   SMART; SM00194; PTPc; 2.
DR   SUPFAM; SSF49265; FN_III-like; 8.
DR   PROSITE; PS50853; FN3; 8.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell adhesion; Disulfide bond; Glycoprotein;
KW   Hydrolase; Immunoglobulin domain; Membrane; Protein phosphatase;
KW   Receptor; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     29       Potential.
FT   CHAIN        30   1907       Receptor-type tyrosine-protein
FT                                phosphatase S.
FT                                /FTId=PRO_0000358321.
FT   TOPO_DOM     30   1257       Extracellular (Potential).
FT   TRANSMEM   1258   1278       Helical; (Potential).
FT   TOPO_DOM   1279   1907       Cytoplasmic (Potential).
FT   DOMAIN       33    123       Ig-like C2-type 1.
FT   DOMAIN      135    224       Ig-like C2-type 2.
FT   DOMAIN      232    314       Ig-like C2-type 3.
FT   DOMAIN      319    407       Fibronectin type-III 1.
FT   DOMAIN      413    507       Fibronectin type-III 2.
FT   DOMAIN      512    600       Fibronectin type-III 3.
FT   DOMAIN      605    702       Fibronectin type-III 4.
FT   DOMAIN      707    806       Fibronectin type-III 5.
FT   DOMAIN      814    899       Fibronectin type-III 6.
FT   DOMAIN      904   1007       Fibronectin type-III 7.
FT   DOMAIN     1009   1092       Fibronectin type-III 8.
FT   DOMAIN     1352   1607       Tyrosine-protein phosphatase 1.
FT   DOMAIN     1639   1898       Tyrosine-protein phosphatase 2.
FT   REGION     1548   1554       Substrate binding (By similarity).
FT   ACT_SITE   1548   1548       Phosphocysteine intermediate (By
FT                                similarity).
FT   ACT_SITE   1839   1839       Phosphocysteine intermediate (By
FT                                similarity).
FT   BINDING    1516   1516       Substrate (By similarity).
FT   BINDING    1592   1592       Substrate (By similarity).
FT   SITE       1197   1198       Cleavage (By similarity).
FT   CARBOHYD    250    250       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    295    295       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    720    720       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    916    916       N-linked (GlcNAc...) (Potential).
FT   DISULFID     54    107       By similarity.
FT   DISULFID    156    207       By similarity.
FT   DISULFID    253    298       By similarity.
FT   VAR_SEQ       1   1315       Missing (in isoform 5).
FT                                /FTId=VSP_036057.
FT   VAR_SEQ     604    604       K -> I (in isoform 3 and isoform 4).
FT                                /FTId=VSP_036058.
FT   VAR_SEQ     605   1010       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_036059.
FT   VAR_SEQ     624    669       Missing (in isoform 6).
FT                                /FTId=VSP_036060.
FT   VAR_SEQ    1284   1287       Missing (in isoform 4).
FT                                /FTId=VSP_036061.
FT   VAR_SEQ    1519   1521       Missing (in isoform 2).
FT                                /FTId=VSP_036062.
FT   CONFLICT    597    597       R -> H (in Ref. 1; CAA57732).
FT   CONFLICT    758    758       P -> A (in Ref. 1; CAA57732).
FT   CONFLICT    834    834       A -> G (in Ref. 1; CAA57732).
FT   CONFLICT    853    853       A -> R (in Ref. 1; CAA57732).
FT   CONFLICT    887    887       A -> G (in Ref. 1; CAA57732).
FT   CONFLICT    981    981       A -> G (in Ref. 1; CAA57732).
FT   CONFLICT   1169   1171       RSL -> QHV (in Ref. 1; CAA57732).
FT   CONFLICT   1502   1502       E -> G (in Ref. 1; CAA57732).
FT   CONFLICT   1609   1609       G -> S (in Ref. 1; CAA57732).
SQ   SEQUENCE   1907 AA;  211904 MW;  725C016196E22D1A CRC64;
     MAPTWSPSVV SVVGPVGLFL VLLARGCLAE EPPRFIREPK DQIGVSGGVA SFVCQATGDP
     KPRVTWNKKG KKVNSQRFET IDFDESSGAV LRIQPLRTPR DENVYECVAQ NSVGEITIHA
     KLTVLREDQL PPGFPNIDMG PQLKVVERTR TATMLCAASG NPDPEITWFK DFLPVDPSAS
     NGRIKQLRSG ALQIESSEET DQGKYECVAT NSAGVRYSSP ANLYVRVRRV APRFSILPMS
     HEIMPGGNVN ITCVAVGSPM PYVKWMQGAE DLTPEDDMPV GRNVLELTDV KDSANYTCVA
     MSSLGVIEAV AQITVKSLPK APGTPVVTEN TATSITVTWD SGNPDPVSYY VIEYKSKSQD
     GPYQIKEDIT TTRYSIGGLS PNSEYEIWVS AVNSIGQGPP SESVVTRTGE QAPASAPRNV
     QARMLSATTM IVQWEEPVEP NGLIRGYRVY YTMEPEHPVG NWQKHNVDDS LLTTVGSLLE
     DETYTVRVLA FTSVGDGPLS DPIQVKTQQG VPGQPMNLRA EAKSETSIGL SWSAPRQESV
     IKYELLFREG DRGREVGRTF DPTTAFVVED LKPNTEYAFR LAARSPQGLG AFTAVVRQRT
     LQAKPSAPPQ DVKCTSLRST AILVSWRPPP PETHNGALVG YSVRYRPLGS EDPDPKEVNN
     IPPTTTQILL EALEKWTEYR VTAVAYTEVG PGPESSPVVV RTDEDVPSAP PRKVEAEALN
     ATAIRVLWRS PTPGRQHGQI RGYQVHYVRM EGAEARGPPR IKDIMLADAQ EMVITNLQPE
     TAYSITVAAY TMKGDGARSK PKVVVTKGAV LGRPTLSVQQ TPEGSLLARW EPPADAAEDP
     VLGYRLQFGR EDAAPATLEL AAWERRFAAP AHKGATYVFR LAARGRAGLG EEAAAALSIP
     EDAPRGFPQI LGAAGNVSAG SVLLRWLPPV PAERNGAIIK YTVSVREAGA PGPATETELA
     AAAQPGAETA LTLRGLRPET AYELRVRAHT RRGPGPFSPP LRYRLARDPV SPKNFKVKMI
     MKTSVLLSWE FPDNYNSPTP YKIQYNGLTL DVDGRTTKKL ITHLKPHTFY NFVLTNRGSS
     LGGLQQTVTA RTAFNMLSGK PSVAPKPDND GFIVVYLPDG QSPVTVQNYF IVMVPLRKSR
     GGQFPVLLGS PEDMDLEELI QDISRLQRRS LRHSRQLEVP RPYIAARFSI LPAVFHPGNQ
     KQYGGFDNRG LEPGHRYVLF VLAVLQKNEP TFAASPFSDP FQLDNPDPQP IVDGEEGLIW
     VIGPVLAVVF IICIVIAILL YKNKPDSKRK DSEPRTKCLL NNADLAPHHP KDPVEMRRIN
     FQTPGMLSHP PIPITDMAEH MERLKANDSL KLSQEYESID PGQQFTWEHS NLEANKPKNR
     YANVIAYDHS RVILQPLEGI MGSDYINANY VDGYRRQNAY IATQGPLPET FGDFWRMVWE
     QRSATVVMMT RLEEKSRIKC DQYWPNRGTE TYGFIQVTLL DTMELATFCV RTFSLHKNGS
     SEKREVRHFQ FTAWPDHGVP EYPTPFLAFL RRVKTCNPPD AGPIVVHCSA GVGRTGCFIV
     IDAMLERIKT EKTVDVYGHV TLMRSQRNYM VQTEDQYGFI HEALLEAVGC GNTEVPARSL
     YTYIQKLAQV EPGEHVTGME LEFKRLASSK AHTSRFITAS LPCNKFKNRL VNILPYESSR
     VCLQPIRGVE GSDYINASFI DGYRQQKAYI ATQGPLAETT EDFWRALWEN NSTIVVMLTK
     LREMGREKCH QYWPAERSAR YQYFVVDPMA EYNMPQYILR EFKVTDARDG QSRTVRQFQF
     TDWPEQGAPK SGEGFIDFIG QVHKTKEQFG QDGPISVHCS AGVGRTGVFI TLSIVLERMR
     YEGVVDIFQT VKVLRTQRPA MVQTEDEYQF CFQAALEYLG SFDHYAT
//
ID   B0V2V8_MOUSE            Unreviewed;       745 AA.
AC   B0V2V8;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   11-JAN-2011, entry version 21.
DE   SubName: Full=Bromodomain containing 4;
GN   Name=Brd4; ORFNames=RP24-236O3.1-005;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Dunn M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CT033755; CAQ11933.1; -; Genomic_DNA.
DR   EMBL; CT033751; CAQ11933.1; JOINED; Genomic_DNA.
DR   EMBL; CT033751; CAQ12564.1; -; Genomic_DNA.
DR   EMBL; CT033755; CAQ12564.1; JOINED; Genomic_DNA.
DR   IPI; IPI00885355; -.
DR   ProteinModelPortal; B0V2V8; -.
DR   SMR; B0V2V8; 42-168, 347-460, 606-683.
DR   STRING; B0V2V8; -.
DR   PRIDE; B0V2V8; -.
DR   Ensembl; ENSMUST00000120276; ENSMUSP00000112474; ENSMUSG00000024002.
DR   MGI; MGI:1888520; Brd4.
DR   HOVERGEN; HBG004896; -.
DR   Bgee; B0V2V8; -.
DR   Genevestigator; B0V2V8; -.
DR   GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR   GO; GO:0000790; C:nuclear chromatin; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007059; P:chromosome segregation; IMP:MGI.
DR   GO; GO:0044154; P:histone H3-K14 acetylation; IMP:MGI.
DR   GO; GO:0043983; P:histone H4-K12 acetylation; IMP:MGI.
DR   GO; GO:0001833; P:inner cell mass cell proliferation; IMP:MGI.
DR   GO; GO:0043388; P:positive regulation of DNA binding; IDA:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IPI:MGI.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   Gene3D; G3DSA:1.20.920.10; Bromodomain; 2.
DR   Pfam; PF00439; Bromodomain; 2.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 2.
DR   SUPFAM; SSF47370; Bromodomain; 2.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 2.
PE   4: Predicted;
KW   Bromodomain.
SQ   SEQUENCE   745 AA;  83335 MW;  1E4EE4511AF0EBA0 CRC64;
     MSTESGPGTR LRNLPVMGDG LETSQMSTTQ AQAQPQPANA ASTNPPPPET SNPNKPKRQT
     NQLQYLLRVV LKTLWKHQFA WPFQQPVDAV KLNLPDYYKI IKTPMDMGTI KKRLENNYYW
     NAQECIQDFN TMFTNCYIYN KPGDDIVLMA EALEKLFLQK INELPTEETE IMIVQAKGRG
     RGRKETGAAK PGVSTVPNTT QASTSPQTQT PQQNPPPPVQ ATTHPFPAVT PDLIAQPPVM
     TMVPPQPLQT PSPVPPQPPP PPAPVPQPVQ SHPPIIATTP QPVKTKKGVK RKADTTTPTT
     IDPIHEPPSL APEPKTAKLG PRRESSRPVK PPKKDVPDSQ QHPGPEKSSK ISEQLKCCSG
     ILKEMFAKKH AAYAWPFYKP VDVEALGLHD YCDIIKHPMD MSTIKSKLES REYRDAQEFG
     ADVRLMFSNC YKYNPPDHEV VAMARKLQDV FEMRFAKMPD EPEEPVVTVS SPAVPPPTKV
     VAPPSSSDSS SDSSSDSDSS TDDSEEERAQ RLAELQEQLK AVHEQLAALS QPQQNKPKKK
     EKDKKEKKKE KHKKKEEVEE NKKSKTKELP PKKTKKNNSS NSNVSKKEPV PTKTKPPPTY
     ESEEEDKCKP MSYEEKRQLS LDINKLPGEK LGRVVHIIQS REPSLKNSNP DEIEIDFETL
     KPSTLRELER YVTSCLRKKR KPQAEKVDVI AGSSKMKGFS SSESESTSES SSSDSEDSET
     EVLPNHWTRT LNKTVFSSRF LPSEL
//
ID   B1APX2_MOUSE            Unreviewed;       447 AA.
AC   B1APX2;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   30-NOV-2010, entry version 23.
DE   SubName: Full=Novel protein;
GN   Name=5031439G07Rik; Synonyms=RP23-180L12.1;
GN   ORFNames=RP23-180L12.1-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Pearce A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL513352; CAP19270.1; -; Genomic_DNA.
DR   IPI; IPI00464302; -.
DR   RefSeq; NP_001028445.1; NM_001033273.2.
DR   UniGene; Mm.323925; -.
DR   ProteinModelPortal; B1APX2; -.
DR   PRIDE; B1APX2; -.
DR   Ensembl; ENSMUST00000047144; ENSMUSP00000037011; ENSMUSG00000036046.
DR   GeneID; 223739; -.
DR   KEGG; mmu:223739; -.
DR   MGI; MGI:2444899; 5031439G07Rik.
DR   HOGENOM; HBG716485; -.
DR   HOVERGEN; HBG061712; -.
DR   InParanoid; B1APX2; -.
DR   OMA; EFFREDD; -.
DR   NextBio; 376860; -.
DR   Bgee; B1APX2; -.
DR   Genevestigator; B1APX2; -.
DR   InterPro; IPR019141; DUF2045.
DR   Pfam; PF09741; DUF2045; 1.
PE   4: Predicted;
SQ   SEQUENCE   447 AA;  50236 MW;  4D65C2EA22094F47 CRC64;
     MASARPPGRA CASASAPAGL RAGPAASRES VDSSEAEERS LQHMLRAIAE ERGRLSLRRE
     VCGLGCFKDD RIVFWTWMFS TYFMEKLAPR QDDMLFYVRR KRAYPGNEGT IDGRKAEAEP
     EVEVEVYRRD SKKLPGLGDP DIDWEESVCL NLILQKLDYM VTCAVCTRAD GGDIHIHRKK
     SQQVFASPSK HPMDSKGEES KMSYPNIFFM IDSFEEVFSD MTVGEGEMVC VELVASDKTN
     TFQGVIFQGS IRYEALKKVY DNRVSVAARM AQKMSFGFYK YNNMEFVRMK GPQGKGHAEM
     AVSRVSTGDT SPCGTEDSSP ASPMHERVTS FSTPPTPERN NRPAFFSPSL KRKVPRNRIA
     EMKKSHSAND SEEFFREDDS GADLHNATNL RSRSLSGTGR SLVGSWLKLN RADGNFLLYA
     HLTYVTLPLH RILTDILEVR QKPILMT
//
ID   B1AQW2_MOUSE            Unreviewed;       390 AA.
AC   B1AQW2;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 25.
DE   RecName: Full=Microtubule-associated protein;
GN   Name=Mapt; ORFNames=RP23-136D4.1-006;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Peck A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 4 Tau/MAP repeats.
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DR   EMBL; AL593843; CAM14798.1; -; Genomic_DNA.
DR   IPI; IPI00648564; -.
DR   UniGene; Mm.1287; -.
DR   STRING; B1AQW2; -.
DR   PRIDE; B1AQW2; -.
DR   Ensembl; ENSMUST00000106993; ENSMUSP00000102606; ENSMUSG00000018411.
DR   MGI; MGI:97180; Mapt.
DR   HOVERGEN; HBG000991; -.
DR   Bgee; B1AQW2; -.
DR   Genevestigator; B1AQW2; -.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0035085; C:cilium axoneme; IDA:MGI.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:InterPro.
DR   InterPro; IPR002955; Tau_protein.
DR   InterPro; IPR001084; Tau_tubulin-bd.
DR   Pfam; PF00418; Tubulin-binding; 4.
DR   PRINTS; PR01261; TAUPROTEIN.
DR   PROSITE; PS00229; TAU_MAP_1; 4.
DR   PROSITE; PS51491; TAU_MAP_2; 4.
PE   4: Predicted;
KW   Microtubule; Repeat.
SQ   SEQUENCE   390 AA;  40892 MW;  58B27295306CDF3A CRC64;
     MADPRQEFDT MEDHAGDYTL LQDQEGDMDH GLKAEEAGIG DTPNQEDQAA GHVTQARVAS
     KDRTGNDEKK AKGADGKTGA KIATPRGAAS PAQKGTSNAT RIPAKTTPSP KTPPGSASKQ
     PQRKLPPAGA KSERGEPPKS GERSGYSSPG SPGTPGSRSR TPSLPTPPTR EPKKVAVVRT
     PPKSPSASKS RLQTAPVPMP DLKNVRSKIG STENLKHQPG GGKVQIINKK LDLSNVQSKC
     GSKDNIKHVP GGGSVQIVYK PVDLSKVTSK CGSLGNIHHK PGGGQVEVKS EKLDFKDRVQ
     SKIGSLDNIT HVPGGGNKKI ETHKLTFREN AKAKTDHGAE IVYKSPVVSG DTSPRHLSNV
     SSTGSIDMVD SPQLATLADE VSASLAKQGL
//
ID   B1AQX6_MOUSE            Unreviewed;      1174 AA.
AC   B1AQX6;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-FEB-2011, entry version 19.
DE   SubName: Full=P140 gene;
GN   Name=Srcin1; Synonyms=P140; ORFNames=RP23-157O10.7-004;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Tracey A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Harrison E.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL596088; CAM15696.1; -; Genomic_DNA.
DR   EMBL; AL596123; CAM15696.1; JOINED; Genomic_DNA.
DR   EMBL; AL596123; CAM27400.1; -; Genomic_DNA.
DR   EMBL; AL596088; CAM27400.1; JOINED; Genomic_DNA.
DR   IPI; IPI00890037; -.
DR   UniGene; Mm.342665; -.
DR   STRING; B1AQX6; -.
DR   PRIDE; B1AQX6; -.
DR   Ensembl; ENSMUST00000107590; ENSMUSP00000103216; ENSMUSG00000038453.
DR   Ensembl; ENSMUST00000107593; ENSMUSP00000103219; ENSMUSG00000038453.
DR   Ensembl; ENSMUST00000107594; ENSMUSP00000103220; ENSMUSG00000038453.
DR   MGI; MGI:1933179; Srcin1.
DR   GeneTree; ENSGT00390000012399; -.
DR   HOVERGEN; HBG019587; -.
DR   Bgee; B1AQX6; -.
DR   Genevestigator; B1AQX6; -.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007162; P:negative regulation of cell adhesion; IDA:MGI.
DR   InterPro; IPR022782; AIP3_C.
DR   Pfam; PF03915; AIP3; 1.
PE   4: Predicted;
SQ   SEQUENCE   1174 AA;  126990 MW;  F12ADAB9CD9133DF CRC64;
     MQPWQCLRRF ALAWWERTAE GRARSPREEV GPRDPGGRGE PDPERSSPPM LSADDAEYPR
     EYRTLGGGGG GGSGGRRFSN VGLVHTSERR HTVIAAQSLE ALSGLQKADA DRKRDAFMDH
     LKSKYPQHAL ALRGQQDRMR EQQPNYWSFK TRSSRHTQGA QPGLADQAAK LSYASAESLE
     TMSEAELPLG FSRMNRFRQS LPLSRSASQT KLRSPGVLFL QFGEETRRVH ITHEVSSLDT
     LHALIAHMFP QKLTMGMLKS PNTAILIKDE ARNVFYELED VRDIQDRSII KIYRKEPLYA
     AFPGSHLTNG DLRREMVYAS RESSPTRRLN NLSPASHLAS SSPPPGLPSG LPSGLPSGSP
     SRSRLSYAGG RPPSYAGSPV HHAAERLGGA PTGQGVSPSP SAILERRDVK PDEDLAGKAG
     GMVLVKGEGL YADPYGLLHE GRLSLAAAAG DPFAYPGAGG LYKRGSVRSL STYSAAALQS
     DLEDSLYKAG AGGPLYGDGY GFRLPPSSPQ KLADVSAPSG GPPPPHSPYS GPPSRGSPVR
     QSFRKDSGSS SVFAESPGGK ARSTGSASTA GAPPSELFPG PGERSLVGFG PPVPAKDTET
     RERMEAMEKQ IASLTGLVQS ALLRGSEPET PSEKVEGSNG AATPSAPVCG SGSKSSGATP
     VSGPPPPSAS STPAGQPTAV SRLQMQLHLR GLQNSASDLR GQLQQLRKLQ LQNQESVRAL
     LKRTEAELSM RVSEAARRQE DPLQRQRTLV EEERLRYLND EELITQQLND LEKSVEKIQR
     DVAHNHRLVP GPELEEKALV LKQLGETLTE LKAHFPGLQS KMRVVLRVEV EAVKFLKEEP
     QRLDGLLKRC RGVTDTLAQI RRQVDEGMWP PPNNLLNQSP KKVAAETDFS KGLDFEIPPP
     SPPLNLHELS GPAEGTPLTP KSTNPTKGLD ASSKRNTDKA VSVEAAERDW EEKRAALTQY
     SAKDINRLLE ETQAELLKAI PDLDCASKTH PGPAPTPDHK PPKAPHGQKA APRTEPSGRR
     GSDELTVPRY RTEKPSKSPP PPPPRRSFPS SHGLTTTRTG EVVVTSKKDS VFIKKAESEE
     LEVQKPQVKL RRAVSEVVRP ASTPPIMASA IKDEDDEERI IAELESGGSS VPPMKVVTPG
     ASRLKAAQGP AGSPDKGKHG KQRTEYMRIQ AQQQ
//
ID   B1AQX9_MOUSE            Unreviewed;      1217 AA.
AC   B1AQX9;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 24.
DE   SubName: Full=P140 gene;
GN   Name=Srcin1; Synonyms=P140; ORFNames=RP23-157O10.7-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Tracey A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Harrison E.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL596088; CAM15699.1; -; Genomic_DNA.
DR   EMBL; AL596123; CAM15699.1; JOINED; Genomic_DNA.
DR   EMBL; AL596123; CAM27403.1; -; Genomic_DNA.
DR   EMBL; AL596088; CAM27403.1; JOINED; Genomic_DNA.
DR   IPI; IPI00889824; -.
DR   RefSeq; NP_061361.2; NM_018873.2.
DR   UniGene; Mm.342665; -.
DR   STRING; B1AQX9; -.
DR   Ensembl; ENSMUST00000107596; ENSMUSP00000103222; ENSMUSG00000038453.
DR   GeneID; 56013; -.
DR   KEGG; mmu:56013; -.
DR   CTD; 56013; -.
DR   MGI; MGI:1933179; Srcin1.
DR   GeneTree; ENSGT00390000012399; -.
DR   HOVERGEN; HBG019587; -.
DR   OrthoDB; EOG418BMM; -.
DR   NextBio; 311742; -.
DR   Bgee; B1AQX9; -.
DR   Genevestigator; B1AQX9; -.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007162; P:negative regulation of cell adhesion; IDA:MGI.
DR   InterPro; IPR022782; AIP3_C.
DR   Pfam; PF03915; AIP3; 1.
PE   4: Predicted;
SQ   SEQUENCE   1217 AA;  130610 MW;  9CA4118C1AC71FEF CRC64;
     MGNAPSQDPE RSSPPMLSAD DAEYPREYRT LGGGGGGGSG GRRFSNVGLV HTSERRHTVI
     AAQSLEALSG LQKADADRKR DAFMDHLKSK YPQHALALRG QQDRMREQVG GWTVDPVCLL
     SSLCSHLHGD STPSGAGQPA QQPNYWSFKT RSSRHTQGAQ PGLADQAAKL SYASAESLET
     MSEAELPLGF SRMNRFRQSL PLSRSASQTK LRSPGVLFLQ FGEETRRVHI THEVSSLDTL
     HALIAHMFPQ KLTMGMLKSP NTAILIKDEA RNVFYELEDV RDIQDRSIIK IYRKEPLYAA
     FPGSHLTNGD LRREMVYASR ESSPTRRLNN LSPASHLASS SPPPGLPSGL PSGLPSGSPS
     RSRLSYAGGR PPSYAGSPVH HAAERLGGAP TGQGVSPSPS AILERRDVKP DEDLAGKAGG
     MVLVKGEGLY ADPYGLLHEG RLSLAAAAGD PFAYPGAGGL YKRGSVRSLS TYSAAALQSD
     LEDSLYKAGA GGPLYGDGYG FRLPPSSPQK LADVSAPSGG PPPPHSPYSG PPSRGSPVRQ
     SFRKDSGSSS VFAESPGGKA RSTGSASTAG APPSELFPGP GERSLVGFGP PVPAKDTETR
     ERMEAMEKQI ASLTGLVQSA LLRGSEPETP SEKVEGSNGA ATPSAPVCGS GSKSSGATPV
     SGPPPPSASS TPAGQPTAVS RLQMQLHLRG LQNSASDLRG QLQQLRKLQL QNQESVRALL
     KRTEAELSMR VSEAARRQED PLQRQRTLVE EERLRYLNDE ELITQQLNDL EKSVEKIQRD
     VAHNHRLVPG PELEEKALVL KQLGETLTEL KAHFPGLQSK MRVVLRVEVE AVKFLKEEPQ
     RLDGLLKRCR GVTDTLAQIR RQVDEGMWPP PNNLLNQSPK KVAAETDFSK GLDFEIPPPS
     PPLNLHELSG PAEGTPLTPK STNPTKGLDA SSKRNTDKAV SVEAAERDWE EKRAALTQYS
     AKDINRLLEE TQAELLKAIP DLDCASKTHP GPAPTPDHKP PKAPHGQKAA PRTEPSGRRG
     SDELTVPRYR TEKPSKSPPP PPPRRSFPSS HGLTTTRTGE VVVTSKKDSV FIKKAESEEL
     EVQKPQVKLR RAVSEVVRPA STPPIMASAI KDEDDEERII AELESGGSSV PPMKVVTPGA
     SRLKAAQGPA GSPDKGKHGK QRTEYMRIQA QQQATKPSKE VSGPNETSSP GSEKPSGSRT
     SIPVLTSFGA RNSSISF
//
ID   B1AQZ0_MOUSE            Unreviewed;       484 AA.
AC   B1AQZ0;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 22.
DE   SubName: Full=Septin 8;
GN   Name=Sept8; ORFNames=RP23-188H3.2-004;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Doggett S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the septin family.
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DR   EMBL; AL596095; CAP19147.1; -; Genomic_DNA.
DR   IPI; IPI00875717; -.
DR   ProteinModelPortal; B1AQZ0; -.
DR   SMR; B1AQZ0; 21-309.
DR   STRING; B1AQZ0; -.
DR   Ensembl; ENSMUST00000121334; ENSMUSP00000113038; ENSMUSG00000018398.
DR   MGI; MGI:894310; Sept8.
DR   HOGENOM; HBG715249; -.
DR   HOVERGEN; HBG065093; -.
DR   InParanoid; B1AQZ0; -.
DR   Bgee; B1AQZ0; -.
DR   Genevestigator; B1AQZ0; -.
DR   GO; GO:0031105; C:septin complex; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:InterPro.
DR   InterPro; IPR000038; Cell_Div_GTP-bd.
DR   InterPro; IPR016491; Septin.
DR   PANTHER; PTHR18884; Cell_Div_GTP_bd; 1.
DR   Pfam; PF00735; Septin; 1.
DR   PIRSF; PIRSF006698; Septin; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Nucleotide-binding.
SQ   SEQUENCE   484 AA;  55874 MW;  48FC85117B2D2BEF CRC64;
     MAATDLERVS NAEPEPRSLS LGGHVGFDSL PDQLVSKSVT QGFSFNILCV GETGIGKSTL
     MNTLFNTTFE TEEASHHEEC VRLRPQTYDL QESNVHLKLT IVDAVGFGDQ INKDDSYRPI
     VDYIDAQFEN YLQEELKIRR SLFDYHDTRI HVCLYFITPT GHSLKSLDLV TMKKLDSKVN
     IIPIIAKADT ISKSELHKFK IKIMGELVSN GVQIYQFPTD DEAVAEINAV MNAHLPFAVV
     GSTEEVKVGN KLVRARQYPW GVVQVENENH CDFVKLREML IRVNMEDLRE QTHSRHYELY
     RRCKLEEMGF QDSDGDSQPF SLQETYEAKR KEFLSELQRK EEEMRQMFVN KVKETELELK
     EKERELHEKF EHLKRIHQEE KRKVEEKRRE LEEETNAFNC RKAAMEALQS QALHATSQQP
     LRKDKDKKNR SDIAAAQQSG MSLSNSKVMM TKANVEPLNC SSWWPAIQCC SCLVRDATWR
     EGFL
//
ID   B1AR09_MOUSE            Unreviewed;      1079 AA.
AC   B1AR09;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 27.
DE   SubName: Full=Myeloid/lymphoid or mixed lineage-leukemia translocation to 6 homolog (Drosophila);
GN   Name=Mllt6; ORFNames=RP23-94N18.5-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Harrison E.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL596123; CAM27406.1; -; Genomic_DNA.
DR   IPI; IPI00128218; -.
DR   RefSeq; NP_647472.2; NM_139311.2.
DR   UniGene; Mm.23685; -.
DR   ProteinModelPortal; B1AR09; -.
DR   SMR; B1AR09; 7-58.
DR   STRING; B1AR09; -.
DR   PRIDE; B1AR09; -.
DR   Ensembl; ENSMUST00000044730; ENSMUSP00000045445; ENSMUSG00000038437.
DR   GeneID; 246198; -.
DR   KEGG; mmu:246198; -.
DR   CTD; 246198; -.
DR   MGI; MGI:1935145; Mllt6.
DR   HOVERGEN; HBG004186; -.
DR   OrthoDB; EOG4XD3QG; -.
DR   PhylomeDB; B1AR09; -.
DR   NextBio; 387169; -.
DR   Bgee; B1AR09; -.
DR   Genevestigator; B1AR09; -.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00249; PHD; 2.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   4: Predicted;
KW   Metal-binding; Zinc.
SQ   SEQUENCE   1079 AA;  110563 MW;  B198C36A8CF3BCBA CRC64;
     MKEMVGGCCV CSDERGWAEN PLVYCDGHAC SVAVHQACYG IVQVPTGPWF CRKCESQERA
     ARVRCELCPH KDGALKRTDN GGWAHVVCAL YIPEVQFANV LTMEPIVLQY VPHDRFNKTC
     YICEEQGRES KAASGACMTC NRHGCRQAFH VTCAQMAGLL CEEEVLEVDN VKYCGYCKYH
     FSKMKTSRHS SGGGGGAGGG SSGGGGGGSS SASGGGGGTG GGSGNSFLSG RRSRSASPST
     QPEKHPTHHE KGQKKSRKDK ERLKQKHKKR PESPPSVLAP PAVPTADKVS SATSSSHHEA
     STQETSESSR DSKGRKSSSH SLSHKDKKLG TGKGSSLQSS PDFAAFPKLE QPEEDKYPKP
     ADPTPPAPPS PTAPEPPKAD LFEQKVVFSG FGPIMRFTTT ASSSSRARAP SPGDYKSPHI
     TGAGASAGTH KRMPALSATL GPAEEAPETT LKEKKHKASK RSRHGPGRPK GSRGKEGASG
     PTASLPAAQL AGFTATAASP FSGGSLVSAG LGGLASRTFG PSGSLPSLSL ESSLLGAGIY
     TSNKDPISHG GGMLRAVCST PLSSSLLGPT GTSALPRLSR SPFTSTLASS SASISTTQVF
     SLAGSTFSLP SSHIFGTPMG TVNPLLTQAE SSHTEPDLED CSFRCHGTSP QESLSSMSPI
     SSLPALFDQT SAPCAGGQLD STAPGTTNME QLLEKQGDGE AGVNIVEMLK ALHALQKENQ
     RLQEQILSLT AKKERLQVLN VQLSVPFPAL PAALPATNGP IPGPYGLLPQ AGSSDSLSVS
     KSPPGKNSLG LDNSLSTSSE DPHSGCPSRS SSSLSFHSTP PPLPLLQQSP ATLPLALPGA
     PAPLPPQPQN GLGRAPGATG LGAMPMAEGL LGGLAGSGSL PLNGLLGGLN GAAAPNPAGL
     SQAGGAPTLQ LPGCLNSLTE QQRHLLQQQE QQLQQLQQLL ASPQLTPEHQ TVVYQMIQQM
     QQKRELQRLQ MAGGSQLPMA SLLAGSSTPL LSAGTPGLLP TASAPPLLPA GALVAPSLGS
     NTSLMAAAAA AAAVAAAGGP PVLTAQTNPF LSLPGADASG NGPKGGTADK GASTSQEKG
//
ID   CISD3_MOUSE             Reviewed;         137 AA.
AC   B1AR13; B1AR11; B1AR12;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 28.
DE   RecName: Full=CDGSH iron-sulfur domain-containing protein 3, mitochondrial;
DE   AltName: Full=Melanoma nuclear protein 13;
DE   Flags: Precursor;
GN   Name=Cisd3; Synonyms=Mel-13, Mel13;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=8597592; DOI=10.1016/0167-4781(95)00229-4;
RA   Tetsu O., Kanno R., Isono K., Taniguchi M., Kanno M.;
RT   "Cloning and characterization of two transcripts generated from the
RT   mel-13 gene positioned adjacent to the mammalian Polycomb group-
RT   related gene mel-18.";
RL   Biochim. Biophys. Acta 1305:109-112(1996).
CC   -!- COFACTOR: Binds 2 2Fe-2S clusters per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the CISD protein family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM27408.1; Type=Erroneous gene model prediction;
CC       Sequence=CAM27409.1; Type=Erroneous gene model prediction;
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DR   EMBL; AL596123; CAM27408.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL596123; CAM27409.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL596123; CAM27410.1; -; Genomic_DNA.
DR   IPI; IPI00649725; -.
DR   RefSeq; NP_001078969.2; NM_001085500.2.
DR   UniGene; Mm.29659; -.
DR   ProteinModelPortal; B1AR13; -.
DR   SMR; B1AR13; 49-137.
DR   PhosphoSite; B1AR13; -.
DR   Ensembl; ENSMUST00000107583; ENSMUSP00000103209; ENSMUSG00000078695.
DR   GeneID; 217149; -.
DR   KEGG; mmu:217149; -.
DR   CTD; 217149; -.
DR   MGI; MGI:101788; Cisd3.
DR   GeneTree; ENSGT00390000004574; -.
DR   HOGENOM; HBG524985; -.
DR   HOVERGEN; HBG107689; -.
DR   InParanoid; B1AR13; -.
DR   OrthoDB; EOG4CJVJG; -.
DR   PhylomeDB; B1AR13; -.
DR   NextBio; 375597; -.
DR   Genevestigator; B1AR13; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR018967; FeS-contain_CDGSH-typ.
DR   InterPro; IPR006622; FeS-contain_CDGSH-typ_subfam.
DR   Pfam; PF09360; zf-CDGSH; 2.
DR   SMART; SM00704; ZnF_CDGSH; 2.
PE   3: Inferred from homology;
KW   2Fe-2S; Acetylation; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW   Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    137       CDGSH iron-sulfur domain-containing
FT                                protein 3, mitochondrial.
FT                                /FTId=PRO_0000341406.
FT   METAL        70     70       Iron-sulfur 1 (2Fe-2S) (By similarity).
FT   METAL        72     72       Iron-sulfur 1 (2Fe-2S) (By similarity).
FT   METAL        81     81       Iron-sulfur 1 (2Fe-2S) (By similarity).
FT   METAL        85     85       Iron-sulfur 1 (2Fe-2S); via pros nitrogen
FT                                (By similarity).
FT   METAL       108    108       Iron-sulfur 2 (2Fe-2S) (By similarity).
FT   METAL       110    110       Iron-sulfur 2 (2Fe-2S) (By similarity).
FT   METAL       119    119       Iron-sulfur 2 (2Fe-2S) (By similarity).
FT   METAL       123    123       Iron-sulfur 2 (2Fe-2S); via pros nitrogen
FT                                (By similarity).
FT   MOD_RES      65     65       N6-acetyllysine (By similarity).
SQ   SEQUENCE   137 AA;  15676 MW;  526B8680019C135D CRC64;
     MGFRRLSFPT DFIFLFPNHI CLPALSKPYQ RREISSWLAR WFPKDPAKPV VAQKTPIRLE
     LVAGKTYRWC VCGRSKNQPF CDGSHFFQRT GLSPLKFKAQ ETRTVALCTC KATQRPPYCD
     GTHKSEQVQK AEVGSPL
//
ID   B1AR16_MOUSE            Unreviewed;      1885 AA.
AC   B1AR16;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 29.
DE   SubName: Full=Chromodomain helicase DNA binding protein 3;
DE   Flags: Fragment;
GN   Name=Chd3; ORFNames=RP23-26L6.13-004;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Wallis J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL596125; CAI35987.2; -; Genomic_DNA.
DR   IPI; IPI00551435; -.
DR   UniGene; Mm.178246; -.
DR   STRING; B1AR16; -.
DR   Ensembl; ENSMUST00000092971; ENSMUSP00000090649; ENSMUSG00000018474.
DR   Ensembl; ENSMUST00000128981; ENSMUSP00000122137; ENSMUSG00000018474.
DR   MGI; MGI:1344395; Chd3.
DR   GeneTree; ENSGT00560000076896; -.
DR   HOVERGEN; HBG005326; -.
DR   PhylomeDB; B1AR16; -.
DR   Bgee; B1AR16; -.
DR   Genevestigator; B1AR16; -.
DR   GO; GO:0000785; C:chromatin; IEA:InterPro.
DR   GO; GO:0016581; C:NuRD complex; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006333; P:chromatin assembly or disassembly; IDA:MGI.
DR   GO; GO:0045449; P:regulation of transcription; IEA:InterPro.
DR   InterPro; IPR012957; CHD_C2.
DR   InterPro; IPR012958; CHD_N.
DR   InterPro; IPR000953; Chromodomain.
DR   InterPro; IPR016197; Chromodomain-like.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR009462; DUF1086.
DR   InterPro; IPR009463; DUF1087.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR000910; HMG_HMG1/HMG2.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:1.10.30.10; HMG-box; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 2.
DR   Pfam; PF08074; CHDCT2; 1.
DR   Pfam; PF08073; CHDNT; 1.
DR   Pfam; PF00385; Chromo; 2.
DR   Pfam; PF06461; DUF1086; 1.
DR   Pfam; PF06465; DUF1087; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00628; PHD; 2.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00249; PHD; 2.
DR   SMART; SM00184; RING; 2.
DR   SUPFAM; SSF54160; Chromodomain-like; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 2.
DR   PROSITE; PS50013; CHROMO_2; 2.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 2.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   4: Predicted;
KW   ATP-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding;
KW   Nucleus; Zinc.
FT   NON_TER       1      1
FT   NON_TER    1885   1885
SQ   SEQUENCE   1885 AA;  213924 MW;  8D04869A0840CDF7 CRC64;
     SALGVKKRKR GPKKQKENKP GKPRKRKKLD SEEEFGSERD EYREKSESGG SEYGTGPGRK
     RRRKHREKKE KKTKRRKRGE GDGGHKQVEQ KSSATLLLTW GLEDVEHVFS EEDYHTLTNY
     KAFSQFMRPL IAKKNPKIPM SKMMTILGAK WREFSANNPF KGSAAAVAAA AAAAAAAVAE
     QVSAAVSSAT PIAPSGPPPA LPPPPAPEIQ PPPIRRAKTK EGKGPGHKRR NKSPRVPDGR
     KKLRGKKMAP LKIKLGLLGG KRKKAGSCAF QSEEGHEPEA EESDLDSGSV HSASGWPDGP
     VRAKKLKRGR PGRKKKKVLG CPAVTGEEEV DGYETDHQDY CEVCQQGGEI ILCDTCPRAY
     HLVCLDPELD RAPEGKWSCP HCEKEGVQWE AKEEEEEYEE EGEEGEKEEE DDHMEYCRVC
     KDGGELLCCD ACISSYHIHC LNPPLPDIPN GEWLCPRCTC PVLKGRVQKI LHWRWGEPPV
     AVPAPQQADG NPDVPPPRPL QGRSEREFFV KWVGLSYWHC SWAKELQLEI FHLVMYRNYQ
     RKNDMDEPPP LDYGSGEDDG KSDKRKVKDP HYAEMEEKYY RFGIKPEWMT VHRIINHSMD
     KKGNYHYLVK WKDLPYDQST WEEDEMNIPE YDDHKQSYWR HRELIMGEDP AQPRKYKKKK
     KELQGDGPPS SPTNDPTVKY ETQPRFITAT GGTLHMYQLE GLNWLRFSWA QGTDTILADE
     MGLGKTIQTI VFLYSLYKEG HTKGPFLVSA PLSTIINWER EFQMWAPKFY VVTYTGDKDS
     RAIIRENEFS FEDNAIKGGK KAFKMKREAQ VKFHVLLTSY ELITIDQAAL GSIRWACLVV
     DEAHRLKNNQ SKFFRVLNGY KIDHKLLLTG TPLQNNLEEL FHLLNFLTPE RFNNLEGFLE
     EFADISKEDQ IKKLHDLLGP HMLRRLKADV FKNMPAKTEL IVRVELSPMQ KKYYKYILTR
     NFEALNSRGG GNQVSLLNIM MDLKKCCNHP YLFPVAAMES PKLPSGAYEG GALIKSSGKL
     LLLQKMLRKL KEQGHRVLIF SQMTKMLDLL EDFLDYEGYK YERIDGGITG ALRQEAIDRF
     NAPGAQQFCF LLSTRAGGLG INLATADTVI IFDSDWNPHN DIQAFSRAHR IGQANKVMIY
     RFVTRASVEE RITQVAKRKM MLTHLVVRPG LGSKAGSMSK QELDDILKFG TEELFKDENE
     GENKEEDSSV IHYDNEAIAR LLDRNQDATE DTDVQNMNEY LSSFKVAQYV VREEDKIEEI
     EREIIKQEEN VDPDYWEKLL RHHYEQQQED LARNLGKGKR VRKQVNYNDA AQEDQDNQSE
     YSVGSEEEDE DFDERPEGRR QSKRQLRNEK DKPLPPLLAR VGGNIEVLGF NTRQRKAFLN
     AVMRWGMPPQ DAFTTQWLVR DLRGKTEKEF KAYVSLFMRH LCEPGADGSE TFADGVPREG
     LSRQQVLTRI GVMSLVKKKV QEFEHINGRW SMPELMPDPS AESKRSSRAS SPTKTSPTTP
     EASTTNSPCT SKPATPAPSE KGDGVRTPLD KDDTENQEEK PEKNSKVGEK MEAEVDSPSP
     APSLGERLEH RKILLEDEAP GVPGETEPEP GYRGDREKSE DVKADRELRL GPPRDEPRPN
     GRREEKVEKP RFMFNIADGG FTELHTLWQN EERAAISSGK LNEIWHRRHD YWLLAGIVLH
     GYARWQDIQN DAQFAIINEP FKTEANKGNF LEMKNKFLAR RFKLLEQALV IEEQLRRAAY
     LNLSQEPAHP AMALHARFAE AECLAESHQH LSKESLAGNK PANAVLHKVL NQLEELLSDM
     KADVTRLPAT LSRIPPIAAR LQMSERSILS RLASKGTEPH PTPAFPPGPY ATPPGYGAAF
     SAAPVGALAA AGANYSQMPA GSFIT
//
ID   B1ART1_MOUSE            Unreviewed;      4359 AA.
AC   B1ART1;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 23.
DE   SubName: Full=Vacuolar protein sorting 13D (Yeast);
GN   Name=Vps13d; ORFNames=RP23-133N19.2-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Pelan S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Beasley H.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL606909; CAM14728.1; -; Genomic_DNA.
DR   EMBL; AL627087; CAM14728.1; JOINED; Genomic_DNA.
DR   EMBL; AL627087; CAM18445.1; -; Genomic_DNA.
DR   EMBL; AL606909; CAM18445.1; JOINED; Genomic_DNA.
DR   IPI; IPI00649141; -.
DR   RefSeq; NP_001121670.1; NM_001128198.1.
DR   UniGene; Mm.240310; -.
DR   UniGene; Mm.476856; -.
DR   ProteinModelPortal; B1ART1; -.
DR   PRIDE; B1ART1; -.
DR   Ensembl; ENSMUST00000020441; ENSMUSP00000020441; ENSMUSG00000020220.
DR   GeneID; 230895; -.
DR   KEGG; mmu:230895; -.
DR   CTD; 230895; -.
DR   MGI; MGI:2448530; Vps13d.
DR   GeneTree; ENSGT00410000025397; -.
DR   HOVERGEN; HBG080098; -.
DR   OrthoDB; EOG4QZ7K0; -.
DR   NextBio; 380262; -.
DR   Bgee; B1ART1; -.
DR   Genevestigator; B1ART1; -.
DR   GO; GO:0008104; P:protein localization; IEA:InterPro.
DR   InterPro; IPR009060; UBA-like.
DR   InterPro; IPR000449; UBA/transl_elong_EF1B_N.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   InterPro; IPR009543; VPSAP.
DR   Pfam; PF06650; DUF1162; 1.
DR   Pfam; PF00627; UBA; 1.
DR   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF46934; UBA_like; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   4: Predicted;
SQ   SEQUENCE   4359 AA;  487329 MW;  EC033FCF3F755E06 CRC64;
     MLEGLVAWVL NTYLGKYVNN LNTDQLSVAL LKGAVELENL PLKKDALKEL ELPFEVKAGL
     IGKVTLQIPF YRPHVDPWVI SISGLHVIGG PEKIQDFNDE KEKLLERERK KALLQALEER
     WKKGEPYWYS VTASVVTRIV ENIELKIQDV HLRFEDGVTN PSRPFAFGIC IKNVSMQNAA
     NEPVQKLMRK KRLDVAEFSI YWDVNCTLLG DLPQAELQEA MARSMESRSH HYILEPVCAS
     ALLKRNCSKE PLRSRHSPRI ECDIQLETIP LKLSQLQYRQ IMAFLKELER KERQLKFRKW
     KPKVAVSKNC REWWYFALNA NLYEIREQRK CWTWDFLLHR ARDAVFYTDR YFNKLKGGVL
     SADDKEEMCR IEEEQSFEEL KILRELVHDR FYKQEELAES LREPQFDSPG TSPGDPDGSG
     GSGMLQYLQS WFPGWGGWYG QQSPEGKVVE GLTAESHEHW TPEEILGTEE FFDPTADASC
     MNTYTKRDHV FAKLNVQLQR GTVTLLHKEQ GTAHANESAF MQLEFSDVKL LAESLPRRNS
     SLLLVRLGGL FLRDLATEGT MFPLLVFPNP QKEVGRVSQS FGLQTASEDR SDQYSAADPD
     NPVFEMLYER NPVHSHFERR LHVSTRPLNI IYNPQAIKKV ADFFYKGKVH TSGFGYQSEL
     ELRVAEAARR QYDKLKVQTK AEIRQTLDRL LVGDFIEESK RWTVRLDISA PQVIFPDDFT
     FKNPVLVVVD LGRMLLTNTQ EDSRRKSGDG SASEENQFSD DEYKTPLATP PSTPPPETSS
     SNGEKTPPFS GVEFSEEQLQ AHLMSTQMYE RYSLTFMDLQ VMVGRVRDNW KRVQDIDVGP
     THVVEKFNVH LQLERRLIYT SDPKYPGAVL SGNLPDLKIH INEDKISALK NCFALLTTPE
     TKPSDTQIRE KIFPQEGPRG SLQDSVMNLT QSIVMLEQHT REVLVESQLL LAEFKVNCMQ
     LGVESSGRYI SVLKVFGTNA HFVKRPYDAE VSLTVHGLLL VDTMQTYGAD FDLLMASHKN
     LSFDIPTGSL RDSRAQSPVS GPNVAFQTDV TTLNDQSATS VSLEKILTKE QESLIKLEYQ
     FVSSECPSMN LDSTLQVISL QVNNLDIILN PETIVELIGF LQKSFPKEKD DVSPQPLMTD
     LERSIVEQGT IQSTYEQNTE VAVEIHRLNL LLLRTVGMAD GERHGRKIAT ASIGGTKVNV
     SMGSSFDMNG SLGCLQLMDL TQENVKSQYV VSIGNSVGYE NIVSDIGYFE SVFVRMEDAA
     LTEALSFTFA EKSKQECFLN LKMASLHYNH SAKFLKELTL SMDELEENFR SMLKSAATKV
     TTVLATKTAE YSEMVSLFET PKKTREPFVL EENEIYGFGL PSPRSDTVKL ILNINIESPV
     VSIPRRPGSP ELLVGHLGQI FIQNFVAGDD DSRSDRLQVE IKDIKLYSLN CTQLAGRDNA
     GPEVNRTFCP PSGLASVNSQ EEAHFTRHDF FESLHRGQAF HILNNTTIQF KLEKIPIERE
     SELTFSLSPD ELGTSSIMKI EGKFVNPVQV VLAKHVYEQV LQTMDNLVYS EDLNKFAASA
     PTSPCPNSPL PQLSSCGEPC VEKKENGLFS HSSFSSTSQK SLSVKEAKAF TQIQANFCIS
     ELQVQLSGDL TLGAQGLVSL KFQDFEVEFS KDHPQTLSIQ IALRSLLMED LLEKNPDSKY
     KSLMVSRGAP KPSSLAQKEY LSQSCPSVSS VEYPDMPRSL PSHMEEAPNV FQLYQRPIST
     CRKKPKEAQD KSYPQTPPPS PSVDEPNMLV GKSKFDDSLV HINIFLVDKK HPEFSSSYGR
     INRSIDVDFN CLDVLITLQT WVVILDFFGI GSTADNHAMK VPPEGLLQNV KAESSASMES
     EHQEPVNSKL DLKVHSLSLV LSKATSELAK ANVSKLMAHM EMIEGDLALQ GSIGSLSLSD
     LTPHGDFYRE RFTTSGEEAL IFQTFKYGQP DPLLQREHDI RVSLQMASVQ YVHTQRFQAE
     VVAFIQHFTQ LQDILGRQRA AIEGQTVRDQ AQRCSRILLD IEAGAPVLLI PESSRSNNLI
     VANLGKLKVK NKFLFAGFPG TFSLQDKESV PSASPAGTPK HSMRKMTTTE DPKGPQVQGL
     FMMPPAGVGL GSLKSDFVPS ASIKQRGQQA VPPVSQSSSS PEDHVCLLDC IVVDLQDMDI
     FAAERHPREG SKASEHSSGD LIFPSYFVRQ TGGSLLTEPC RLKLQVERNL DKEISHTVAD
     ISVHGSLSSV HCSLDLCKYK LIRGLLENNL GEPIEDFMRP YDLQDPRIHT VLSGEVYTCM
     CFLIDMVNVS LELKDPKGKE GTGSLARFDF KKCKLLYESF SNQTKSINLV SHSMMAFDTR
     YSGQKPSHGM TNVFNCIFQP SKSSSATQGS IQIELHFRST KDSSCFTVVL NNLRVFLIFD
     WLLLVHDFLH TPSDIKKQNV TPARHRNASS ESAVVPKTVK SGVVTKRSSL PVSNERHLEV
     KVNVTGTEFV VVEDVSCFDT NAIILKGTTV LTYKPRFVDR PFSGSLFGIE VFSCRLGNEQ
     DTALSIVDPV QIQVELVGNS SYQNSSGLMD AFNSEDFPPI LEIQLQALDI RLSYNDVQLF
     LAIAKSIPEQ ASAAAPDSSA LEVDSISCSL PGASRIGEDV REGSRHTLDP VLELQLARLQ
     ELGFSMDDCR KALLVCQGQL KKAASWLFKN AEPLKSLSLV SSSSRDNPGT MPAPRISGVE
     VKAESVCICF IDDCMDCDVP LAELTFSRLN FLQHIRTNPE GFAHFTLSGD YYNRALSGWE
     PFIEPWPCSV SWQQQASSRL HPPRLKLEAK AKRRLDINIT SVLIDQYIST KESWLADYCK
     EDKETESAKT EDWMGSSVDP PCFGQTEVKT PKRRQPFVPF ALRNHTGCTL WFATLTTTPT
     RAALSHSGSP GVVPEGNGAF LDDAHNVSEW REVLTGEEIP FEFEARGKLR HRHTHDLRIH
     QLQVRVNGWE QVSPVSVDKV GTFFRYAAPD KNSSSSTIGS PSSRTNIIHP QVYFSSLPPV
     RVVFAVTMEG SARKVITVRS ALIVKNRLET PMELRLDSPS APDKPVVLPA IMPGDSFAVP
     LHLTSWRLQA RPKGMGVFFC KVPIHWTNVV KTAEVSSSKR ECHSMDTEKS RFFRFCVAIK
     KENYPDYMPS NIFSDSAKQI FRQPGHTIYL LPTVVICNLL PCELDFYVKG MPINGTLKPG
     KEAALPTADT SQNIELGVSL ENFPLCKELL IPPGTQNYMV RMRLYDVNRR QLNLTIRIAC
     RAEGSLKIFI SAPYWLINKT GLPLIFRQDN AKTDAAGQFE EHELARSLSP LLFCYADKEQ
     PNLCTMRIGR GIHPEGMPGW CQGFSLDGGS GVRALKVIQQ GNRPGLIYNI GIDVKKGRGR
     YIDTCMVIFA PRYLLDNKSS HKLAFAQREF ARGQGTANPN GYISTLPGSS VVFHWPRNDY
     DQLLCVRLMD VPNCIWSGGF EVNKNNSFHI NMRDTLGKCF FLRVEITLRG ATYRISFSDT
     DQLPPPFRID NFSKVPVVFT QHGVAEPRLR TEVKPMMSLD YAWDEPTLPP FITLTVKGAG
     SSEINCNMND FQNNRQLYYE NFIYIAATYT FSGLQEGKGR PVASHKAITC AELVLDVSPK
     TQRVILKKKE PGKRSQLWRM TGTGMLAHEG SAVPHNPNKP SATRSIEGSA ILDIAGLAAV
     TDNRYEPLML RKPDRRRSTT QTWSFHEGKL TCGLHGLVVQ AKGGLSGLFD GAEVVLGPDS
     SMELLGPVPP EQQFANQKMR PGSGMLSIRV IPDGPTRALQ ITDFCQRKSE RSSYEVEELP
     VTEQELQKLR NPDTHQELEV LVRLEGGVGV SLINKVPEEL VFASLTGINI HYTQLAASHM
     LELSIQDVQV DNQLIGTTQP FMLYVTPLSN ENEVIETGPA VQVNAVKFPS KSALTNIYKH
     LMVTAQRFTV QIEEKLLLKL LSFFGYDQAE SEVEKYDENI HEKTAEQGGT PTRYYFENLK
     ISIPQIKLSV FTSNKLPLDL KALKSTLGFP LIRFEDAVIN LDPFTRVHPY ETKEFIINDI
     LKHFQEELLS QAARILGSVD FLGNPMGLLN DVSEGVTGLI KYGNVGGLIR NVTHGVSNSA
     AKFAGTLSDG LGKTMDNRHQ SEREYIRYHA ATSGEHLVAG IHGLAHGIIG GLTSVITSTV
     EGVKTEGGVS GFISGLGKGL VGTVTKPVAG ALDFASETAQ AVRDTATLSG PRTQAQRVRK
     PRCCTGPQGL LPRYSESQAE GQEQLFKLTD NIQDEFFIAV ENIDSYCVLI SSKAVYFLKS
     GDYVDREAIF LEVKYDDLYH CLVSKDHGKV YVQVTKKAAN SSSGVSIPGP SHQKPMVHVK
     SEVLAVKLSQ EINYAKSLYY EQQLMLRLSE NQEQLELDS
//
ID   B1ARU4_MOUSE            Unreviewed;      7353 AA.
AC   B1ARU4;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 28.
DE   SubName: Full=Microtubule-actin crosslinking factor 1;
GN   Name=Macf1; ORFNames=RP23-327O13.1-013;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Sehra H.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Hammond S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL606932; CAM18552.1; -; Genomic_DNA.
DR   EMBL; AL606918; CAM18552.1; JOINED; Genomic_DNA.
DR   EMBL; AL606918; CAM20970.1; -; Genomic_DNA.
DR   EMBL; AL606932; CAM20970.1; JOINED; Genomic_DNA.
DR   IPI; IPI00884482; -.
DR   UniGene; Mm.402299; -.
DR   UniGene; Mm.477352; -.
DR   ProteinModelPortal; B1ARU4; -.
DR   SMR; B1ARU4; 68-301, 565-775, 1542-1737, 1740-1918, 2350-2559, 7001-7067, 7076-7176.
DR   STRING; B1ARU4; -.
DR   PRIDE; B1ARU4; -.
DR   Ensembl; ENSMUST00000106224; ENSMUSP00000101831; ENSMUSG00000028649.
DR   MGI; MGI:108559; Macf1.
DR   HOVERGEN; HBG031127; -.
DR   OrthoDB; EOG4XKV61; -.
DR   Bgee; B1ARU4; -.
DR   Genevestigator; B1ARU4; -.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR   GO; GO:0007050; P:cell cycle arrest; IEA:InterPro.
DR   GO; GO:0006928; P:cellular component movement; IMP:MGI.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:MGI.
DR   GO; GO:0001707; P:mesoderm formation; IMP:MGI.
DR   GO; GO:0006620; P:posttranslational protein targeting to membrane; IMP:MGI.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IGI:MGI.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR003108; GAS2_dom.
DR   InterPro; IPR001101; Plectin_repeat.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 2.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Gene3D; G3DSA:3.30.920.20; GAS2_dom; 1.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF02187; GAS2; 1.
DR   Pfam; PF00681; Plectin; 10.
DR   Pfam; PF00435; Spectrin; 17.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM00243; GAS2; 1.
DR   SMART; SM00250; PLEC; 19.
DR   SMART; SM00150; SPEC; 34.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS51460; GAR; 1.
PE   4: Predicted;
KW   Actin-binding; Calcium; Repeat.
SQ   SEQUENCE   7353 AA;  831650 MW;  9D4B40945723B2C0 CRC64;
     MSSSDEETLS ERSCRSERSC RSERSYRSER SGSLSPCPPG DTLPWNLPLH EQKKRKSQDS
     VLDPAERAVV RVADERDRVQ KKTFTKWVNK HLMKVRKHIN DLYEDLRDGH NLISLLEVLS
     GIKLPREKGR MRFHRLQNVQ IALDFLKQRQ VKLVNIRNDD ITDGNPKLTL GLIWTIILHF
     QISDIYISGE SGDMSAKEKL LLWTQKVTAG YTGVKCTNFS SCWSDGKMFN ALIHRYRPDL
     VDMERVQVQS NRENLEQAFE VAERLGVTRL LDAEDVDVPS PDEKSVITYV SSIYDAFPKV
     PEGGEGISAT EVDSRWQEYQ SRVDSLIPWI RQHTILMSDK SFPQNPVELK ALYNQYIHFK
     ETEILAKERE KGRIKELYKL LEVWIEFGRI KLPQGYHPNH VEEEWGKLIV EMLEREKSLR
     PAVERLELLL QIANKIQNGA LNCEEKLTLA KNTLQADAAH LESGQPVQCE SDVIMYIQEC
     EGLIRQLQVD LQILRDEKYY QLEELAFRVM RLQDELVTLR LECTNLYRKG HFSSLELVPP
     STLTTTHLKA EPLNKTTHSS STSWFRKPMT RTELVSISSS EDEGNLRFVY ELLSWVEEMQ
     MKLERAEWGN DLPSVELQLE TQQHIHTSVE ELGSSVKEAR LYEGKMSQNF HTSYVETLGK
     LETQYCKLKE TSSFRMRHLQ SLHKFVSRAT AELIWLNGKE EEELACDWSD SNPNISAKKT
     YFSELTMELE GKQDVFRSLQ DTAEVLSLEN HPAKQTVEAY SAAVQSQLQW MKQLCLCVEQ
     HVKENAAYFQ FFSDARDLES FLRNLQDSIK RKYTCDRSTS LSRLEDLLQD SMDEKEQLIQ
     SKSSVASLVG RSKTIVQLKP RNPDHVLKST LSVKAICDYR QIEITICKND ECVLEDNSQR
     TKWKVISPTG NEAMVPSVCF LIPPPNKEAI EMASRVEQSY QKVMALWHQL HINTKSLISW
     NYLRKDLDTV QTWSLEKLRS LAPGECHQVM KNLQAHYEDF LQDSHDSALF SVADRLRIEE
     EVEACKAHFQ HLMKSLENED KEETLAKVYI SELKNIRLLL EECEQRLLKQ IQSPASSKTD
     RDARQDITLR IAEQEHTQED LQHLRSDLDA ISMKCNVFLQ QSPSGSSATT LRSELNLMVE
     KMDHVYGLST VYLNKLKTID VIVRSMQDAE LLVKGYEIKL SQEEAVPADL SALESHRTTL
     QHWLSDVKDK NSVFSVLDEE ITKAKKVAEQ LRHPASEPNL DLERYQEKGS QLQERWHRVI
     AQLETRQSEV ESIQEVLRDY RACHGTLIKW IEETTAQQEM MKPGQAEDSR VLSEQLSQQT
     ELFAEIERNQ TKLDQCQKFS QQYSTIVKDY ELQLMTYKAF VESQQKSPGK RRRMISSSDA
     ITQEFMDLRT RYTALVTLTT QHVKYISDAL RRLEEEEKVV EEEKQEHVEK VKDLLGWVST
     LARNTQGTTT SSHTSASADI EKAILEQQVL AEELTTKKEQ VSEAIKTSQI FLAKHGHKLS
     EGEKEQISEQ LRVLNKTYHD LCDGSANQLQ QLQSELAQQT EQKGCRAVAG VIDLGTVEIF
     PIFRAMQKGL IDQDTGLVLL ESQIIMSGLI DPENSEKLSL EEGLTRNFIN LPIYQQLLGL
     RDSLSLVSRL TGTLGSLSVV EAIEKKIISE RLGLKVLEVH LATGGFSLPP SENCINLEEA
     FHQGFIASSL HSELQSHLRS SKNLIDPNTA EKVGLLDLMQ RCIIHQESGL KLLPVKQLAG
     GMVSLKSGRK VSIFRAVQEG LIDRQVTVRL LEAQLFAGGI VDPRTGHRLT VEEAVRHNLI
     DQDMACAILI RQLQTGGIID TVTGDRMTID EAVTNNLVAA KIALVILESL WSFMGLLLPE
     SGEILPITDA LEQGIVSTEL AHKILHNRQQ IEALFLPTLT EIWSWEKATE SGILDKDLVN
     NLRSVCIPDM MPHIQLADSA EQSKVGFAAG KPPVSGPREE GSSHGEKLLF QLMTHSYIHA
     HTGQRLLLLD QELVEMLTSR DDCQVILPEV FEIQHQRLNT SEALQELYTG TISQISSAKH
     PRKPCESQFL SQNKDYPSQE NCTEAKGERS VVGIECSPAE SPERELFLKE QEAIIENVGS
     LKVINKVKLK LQRPLLGSRK EEQAETLREE NISGDPLLVE CPEESEGKDL STEKSKCQTP
     TKCSFTCHKE QVKTIKDIPS ETGTSLIKSQ NQMSQFQVDT SVGLRSEFKS EHDMNVNSLE
     KELKEELLVK DGHKQSQEGQ SVADGQTVAL EKTDTEDNAD EPALLHSSPF EDATLSTLSA
     QLQDGGIFNE ETGQKLLLNE AIAQGLVSSH TAVKLMGKLN MFRGFFDSQT CESLTTEEVI
     DEGLMDEKLL YNVLMSDKAI SGILDPRTHS LCSVKEAVAA GLLDKETATR ILEGQVITGG
     IVDLKRGKKL SVTLASNLGL VDTADQTELI NLEKATKGRG AEKAVKERLI ELQMETAGLM
     DPESKAPLTV LQSIDRGILE REAAVYLLTK QVLDGGIIHH ISGLRLSVDN AFKHGLIGED
     MARQLRKVEN FIHYQFFHPQ TKEALSFSEA IKLDLVSPDL KREIQEIQDF SGNLGDFIYG
     QKLTLAKTNK EESLANKTEL PSGVMHGVID PENCTIIPYS ELVKKCRIDT ESGWRYLEVI
     PFSDIKDEAG NNVLTPPEAI QLGKVDFASA LKVLEAQANT GGIIDMATGK RVTLASALEK
     KLLDENMARI IASHQMLSGG IIDIYSDQRV TLNDAVEKRL ISPELAAMIQ VDPLAEQGGT
     GVCELKGDFL RKELLSESSK TPRESYSKEK HEAVLQAGSL CAPEKAGIRG SNGEKAEKGR
     KISVEMEGQR QDEKASSDNK VSASILSPFG FEGESSYQVS VTHPCSESCD LKPREETRSC
     MKKCAVVERD KVVTQIKMVS HVKQSTSGLD AEEARERQGR MVSKEQGSHY ETAGNLLSER
     SVRVDRRVRR EMGGEQSVQM SREAAVLSEE ELDQEVTIGD EPDSFVKSQS MKMIGNDKGK
     EAGIEKDISV VCKIEGFPSQ MTSKDASLTN QDALPFYTEG ETKTVNLCSI LKPGEKLSQE
     TASTVQKEPL SSEIPRPERL NSQESDEEPQ ISDVPHISKG DMAAQITTRQ ETTDVQDLYI
     TSKSSETKDK IFPSKNYIEK LHQEIPMDPT RSHKLKEATI STLETEGISY LDSSDIKSLC
     EDSKADHKSC GHQKSKVTTT QAKKSLEVVD LLVRDTEEGS SEDRVGQRGP RVLASLLPEK
     LPTRTVQSEN IRQHDAVIPA ISEIREEMAL SLPCSVVKVD GKIPKEKHKE ILGDEQGPFM
     AIPSGKGIEG VNPEPCRATQ NVFTRRLCLE HDEKLVSYLS LLRDIEMRTK QIQPLELNVA
     ELQDLLGQAK ELDRELKDLS TVVSQELECV DRIVISQPQE VPAQLLKALE KDAKNLQKSL
     DSVSDSWSSR FLHLQSAVEV KKATVLNRHK ELQGKLQDLR AWVGRASLTL NSKGCDTETD
     ADSLSHTLQP YKDMKQSMAE RKSQLDALAL DIQLFISEHP QDLSLQQNQE MLQFLSELQR
     SFQGLVEHTA AQKDVVQGHL QQVQQEVQVK TLQKQQDTCH KKLEDLCNWV GQAERALERH
     QGGASRQELP ALQQNQSDLK DLQGDIQSHS TSFATAVKDI EGFLEENQTK LSPQELTALR
     EKLHQAKEQY EVLQERTRVA QKELEEAVTS ALQQETEKSK AATELAENKR KIDALLDWVA
     SVGSSERKPQ ASLPGMEQFS GACLEKQTLA ATDGHVDVNQ VPETLDRQYE LMKARHQELL
     SQQQNFIVAT QSVQSFLDQH SHNLTPEERQ KLQEKLGELK EQYAASLARS EAELKQTQAL
     RDELQKFLQD HKEFENWLQQ SENELDSMHK GGSSPEALNS LLKRQGSFSE DVISHKGDLR
     FVTISGQKVL ETENNFEEGQ EPSATRNLVN EKLKDATERY TTLHSKCIRL GSHLSMLLGQ
     YQQFQSSADS LQAWVLTCEA SVGKLLSDTV ASDPGVLQQQ LATTKQLQEE LAEHQVPVEK
     LQKAAHDLLD IEGEPALDCR PIQETTDSIS SRFQNLSCSL DERSALLQKA IAQSQSVQES
     MESLLQSIRE VEQNLERDQV ASLSSGVIQE ALANNMKLKQ DIARQKSSLE ATHDMVTRFM
     ETADSNSASV LQGKLAELSQ RFQQLQLQQQ EKESNLKKLL PQAEMFEQLS NKLQQFMENK
     SRLLASGNQP DQDIAHFSQQ IQELTLAMED QKENLDTLEH LVTTLGSCGF ALDLSQHQDK
     IQNLKKDFTE LQKTVQEREK DASTCQEQLD EFRKLIRTFQ KWLKETEGNV PPAKTFVSAK
     ELEKQIEHLK DLISDWESKG ALLGEINAKG TALESLIMDI TAPDSQAKTG SILPPVGSSV
     GSVNGYHTCK DLTEIQCDMF DVNSKYEKLW EVLRERQESL QTVFSRMEEV QKEASSVLQW
     LESKEEVLKA MDATLSPTKT ETVKAQAESN KAFLAELEQN SPKIQKVKEA LAGLLKTYPN
     SQEAENWKKM QEDLNSRWEK ATEVTVARQK QLEESASHLA CFQAAESQLR PWLMEKELMM
     GVLGPLSIDP NMLNAQKQQF MLKEFEARRQ QHEQLNEAAQ GILTGPGDMS PSASQVHKDL
     QSISQKWVEL TDKLNSRSSQ IDQAIVKSTQ YQDLLQDLSE KVKAIGQRLS GQSAISTQPE
     AVKQQLEETS EIRSDLGQLD NEIKEAQTLC QELSLLIGEQ YLKDELKKRL ETVALPLQGL
     EDLAADRMNR LQAALASTQQ FQQMFDELRT WLDEKQSQQA KNCPISAKLE RLQCQLQENE
     EFQKNLNQHS GSYEVIVAEG EALLLSVPPG EEKKTLQNQL VELRSHWEDL SKKTANRQSR
     LKDCMQKAQK YQGHVEDLVP WIDECKSKMS ELQVTLDPVQ LESSLLRSKA MLNEAEKRRS
     LLEILNSAAD ILINSSEIDE DEIRDEKAGL NQNMDAITEE LQAKTSSLEE MTQRLKEFQE
     SFKNIEKKVE GAKHQLEIFD ALGSQACSNK NLEKLKAQQE VLQALEPQVD YLRNFTQGLV
     EDAPDGSDAS PLVHQAEVAQ QEFLEVKQRV SSSCLTMENK LEGIGQFHCR VREMFSQLAD
     LDDELDGMGA IGRDTDSLQS QIEDVRLFLN KIQALRFDIE DSEAECRKML EEEGTLDLLG
     LKRELEALNK QCGKLTERGK VRQEQLELTL GRVEDFYRKL KALNDAATAA EEGEALQWIV
     GTEVDVINQQ LADFKLFQKD QVDPLQVKLQ QVNGLGQGLI QSAGKNCDVQ GLEHDMDEIN
     TRWNTLNKKV AQRIAQLQEA LLHCGKFQDA LEPLLSWLTD TEELIANQKP PSAEYKVVKA
     QIQEQKLLQR LLDDRKATVD MLQAEGGRIA QSAELADREK ITGQLESLER RWTDLLSKAA
     ARQKQLEDIL VLAKQFHETA EPISDFLSVT EKKLANSEPV GTQTAKIHQQ IIRHKALNEE
     IINRKKNVDQ AIKNGQALLK QTTGEEVLLI QEKLDGIKTR YADITLTSSK ALRTLEQARQ
     LATKFHSTYE ELTGWLREAE EELAASGGQS PTGEQIPQFQ QRQKELKKEV MEHRLVLDTV
     NEVSHALLEL VPWRAREGLD KLVSDANEQY KLISDTVGQR VDEIDAAIQR SQQYEQAADA
     ELAWVAETKR KLMALGPIRL EQDQTTAQLQ VQKAFSIDII RHKDSMDELF SHRGEIFSTC
     GEEQKAVLQE KTECLIQQYE AVSLLNSERY ARLERAQVLV NQFWETYEEL SPWAEETLAL
     IAQLPPPAVD HEQLRQQQEE MRQLRESIAE HKPHIDKILK IGPQLKELNP EEGKMVEEKY
     QKAENMYAQI KDEVRQRALA LDEAVSQSAQ FHDKIEPMLE TLENLSSRLR MPPLIPAEVD
     KIRECISDNK SATVELEKLQ PSFEALKRRG EELIGRSQGA DKDLAAKEIQ DKLDQMVFFW
     EDIKARSEER EIKFLDVLEL AEKFWYDMAA LLTTIKDTQD IVHDLESPGI DPSIIKQQVE
     AAETIKEETD GLHEELEFIR ILGADLIFAC GETEKPEVKK SIDEMNNAWE NLNKTWKERL
     EKLEDAMQAA VQYQDTLQAM FDWLDNTVIK LCTMPPVGTD LNTVKDQLNE MKEFKVEVYQ
     QQIEMEKLNH QGELMLKKAT DETDRDIIRE PLTELKHLWE NLGEKIAHRQ HKLEGALLAL
     GQFQHALEEL MSWLTHTEEL LDAQRPISGD PKVIEVELAK HHVLKNDVLA HQATVATVNK
     AGSELLESSA GDDASSLRSR LETMNQCWES VLQKTEEREQ QLQSTLQQAQ GFHSEIEDFL
     LELNRMENQL SASKPTGGLP ETAREQLDTH MELHSQLRAK EEIYNQLLDK GRLMLLSRGD
     SGSGSKTEQS VALLEQKWHA VSSKVEERKS KLEEALSLAT EFQNSLQEFI NWLTLAEQSL
     NIASPPSLIL NTVLSQIEEH KVFANEVNDH RDQIIELDQT GNQLKFLSQK QDVVLIKNLL
     VSVQSRWEKV VQRSIERGRS LDDARKRAKQ FHEAWKKLID WLEDAESHLD SELEISNDPD
     KIKLQLSKHK EFQKTLGGKQ PVYDTTIRTG RALKEKTLLA GDTQKLDNLL GEVRDKWDTV
     CGKSVERQHK LEEALLFSGQ FMDALQALVD WLYKVEPQLA EDQPVHGDLD LVMNLMDAHK
     VFQKELGKRT GTVQVLKRSG RELIEGSRDD TTWVKGQLQE LSTRWDTVCK LSVSKQSRLE
     QALKQAEEFR DTVHMLLEWL SEAEQTLRFR GALPDDTEAL QSLIDTHKEF MKKVEEKRVD
     VNTAVAMGEA ILAVCHPDCI TTIKHWITII RARFEEVLTW AKQHQQRLET ALSELVANAE
     LLEELLAWIQ WAETTLIQRD QEPIPQNIDR VKALITEHQS FMEEMTRKQP DVDRVTKTYK
     RKSVEPTHAP FMEKSRSGSR KSLNQPTPPP MPILSQSEAK NPRINQLSAR WQQVWLLALE
     RQRKLNDALD RLEELCPELK EFANFDFDVW RKKYMRWMNH KKSRVMDFFR RIDKDQDGKI
     TRQEFIDGIL ASKFPTTKLE MTAVADIFDR DGDGYIDYYE FVAALHPNKD AYRPTTDADK
     IEDEVTRQVA QCKCAKRFQV EQIGENKYRF FLGNQFGDSQ QLRLVRILRS TVMVRVGGGW
     MALDEFLVKN DPCRARGRTN IELREKFILP EGASQGMTPF RSRGRRSKPS SRAASPTRSS
     SSASQSNHSC TSMPSSPATP ASGTKVISSS GSKLKRPTPA FHSSRTSLAG DTSNSSSPAS
     TGAKANRADP KKSASRPGSR AGSRAGSRAS SRRGSDASDF DLLETQSACS DTSESSAAGG
     QGSSRRGLTK PSKIPTMSKK TTTASPRTPG PKR
//
ID   B1ARU6_MOUSE            Unreviewed;      2030 AA.
AC   B1ARU6;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-FEB-2011, entry version 19.
DE   SubName: Full=Microtubule-actin crosslinking factor 1;
DE   Flags: Fragment;
GN   Name=Macf1; ORFNames=RP23-327O13.1-007;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Sehra H.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL606918; CAM20972.1; -; Genomic_DNA.
DR   IPI; IPI00889893; -.
DR   UniGene; Mm.402299; -.
DR   UniGene; Mm.477352; -.
DR   ProteinModelPortal; B1ARU6; -.
DR   STRING; B1ARU6; -.
DR   Ensembl; ENSMUST00000147228; ENSMUSP00000115847; ENSMUSG00000028649.
DR   MGI; MGI:108559; Macf1.
DR   GeneTree; ENSGT00600000084106; -.
DR   Bgee; B1ARU6; -.
DR   Genevestigator; B1ARU6; -.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IDA:MGI.
DR   GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR   GO; GO:0006928; P:cellular component movement; IMP:MGI.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:MGI.
DR   GO; GO:0001707; P:mesoderm formation; IMP:MGI.
DR   GO; GO:0006620; P:posttranslational protein targeting to membrane; IMP:MGI.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IGI:MGI.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF00435; Spectrin; 1.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00150; SPEC; 6.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS50021; CH; 1.
PE   4: Predicted;
KW   Repeat.
FT   NON_TER    2030   2030
SQ   SEQUENCE   2030 AA;  230511 MW;  3D62379FD16AC4AB CRC64;
     MGNSLGCVKE PKESIAVPEK APISPKKRVR FKRKWRGKKI LTPEASHREE ALEGTGVIEE
     TETLTKLTAR LPKEPGVGGA EHPPSDIFLP GDSAPNSGVG DQGMIVQVKE SFQAEIQTAH
     LLLENESSVV GGAWDSLEEG MTVIAHLLDN PAERNCEKSV SQLVEFPRTA SCSSRAVLLP
     LQGETAVEQG GTLLRHRHRS STLPRTDYPS ETVDQDQPSE GWSVGGRTKS VPSAPPTGSW
     IAKCSVASSI PKQSGDPIHT EPTHVGLVSC KGPIMPASQS DLSVSGITVS ILPSSSGYGS
     DGLRLHGIRP EDTEPEKTST PFSEEDGTLS LEISDIYISG ESGDMSAKEK LLLWTQKVTA
     GYTGVKCTNF SSCWSDGKMF NALIHRYRPD LVDMERVQVQ SNRENLEQAF EVAERLGVTR
     LLDAEDVDVP SPDEKSVITY VSSIYDAFPK VPEGGEGISA TEVDSRWQEY QSRVDSLIPW
     IRQHTILMSD KSFPQNPVEL KALYNQYIHF KETEILAKER EKGRIKELYK LLEVWIEFGR
     IKLPQGYHPN HVEEEWGKLI VEMLEREKSL RPAVERLELL LQIANKIQNG ALNCEEKLTL
     AKNTLQADAA HLESGQPVQC ESDVIMYIQE CEGLIRQLQV DLQILRDEKY YQLEELAFRV
     MRLQDELVTL RLECTNLYRK GHFSSLELVP PSTLTTTHLK AEPLNKTTHS SSTSWFRKPM
     TRTELVSISS SEDEGNLRFV YELLSWVEEM QMKLERAEWG NDLPSVELQL ETQQHIHTSV
     EELGSSVKEA RLYEGKMSQN FHTSYVETLG KLETQYCKLK ETSSFRMRHL QSLHKFVSRA
     TAELIWLNGK EEEELACDWS DSNPNISAKK TYFSELTMEL EGKQDVFRSL QDTAEVLSLE
     NHPAKQTVEA YSAAVQSQLQ WMKQLCLCVE QHVKENAAYF QFFSDARDLE SFLRNLQDSI
     KRKYTCDRST SLSRLEDLLQ DSMDEKEQLI QSKSSVASLV GRSKTIVQLK PRNPDHVLKS
     TLSVKAICDY RQIEITICKN DECVLEDNSQ RTKWKVISPT GNEAMVPSVC FLIPPPNKEA
     IEMASRVEQS YQKVMALWHQ LHINTKSLIS WNYLRKDLDT VQTWSLEKLR SLAPGECHQV
     MKNLQAHYED FLQDSHDSAL FSVADRLRIE EEVEACKAHF QHLMKSLENE DKEETLAKVY
     ISELKNIRLL LEECEQRLLK QIQSPASSKT DRDARQDITL RIAEQEHTQE DLQHLRSDLD
     AISMKCNVFL QQSPSGSSAT TLRSELNLMV EKMDHVYGLS TVYLNKLKTI DVIVRSMQDA
     ELLVKGYEIK LSQEEAVPAD LSALESHRTT LQHWLSDVKD KNSVFSVLDE EITKAKKVAE
     QLRHPASEPN LDLERYQEKG SQLQERWHRV IAQLETRQSE VESIQEVLRD YRACHGTLIK
     WIEETTAQQE MMKPGQAEDS RVLSEQLSQQ TELFAEIERN QTKLDQCQKF SQQYSTIVKD
     YELQLMTYKA FVESQQKSPG KRRRMISSSD AITQEFMDLR TRYTALVTLT TQHVKYISDA
     LRRLEEEEKV VEEEKQEHVE KVKDLLGWVS TLARNTQGTT TSSHTSASAD IEKAILEQQV
     LAEELTTKKE QVSEAIKTSQ IFLAKHGHKL SEGEKEQISE QLRVLNKTYH DLCDGSANQL
     QQLQSELAQQ TEQKTLQKQQ DTCHKKLEDL CNWVGQAERA LERHQGGASR QELPALQQNQ
     SDLKDLQGDI QSHSTSFATA VKDIEGFLEE NQTKLSPQEL TALREKLHQA KEQYEVLQER
     TRVAQKELEE AVTSALQQET EKSKAATELA ENKRKIDALL DWVASVGSSE RKPQASLPGM
     EQFSGACLEK QTLAATDGHV DVNQVPETLD RQYELMKARH QELLSQQQNF IVATQSVQSF
     LDQHSHNLTP EERQKLQEKL GELKEQYAAS LARSEAELKQ TQALRDELQK FLQDHKEFEN
     WLQQSENELD SMHKGGSSPE ALNSLLKRQG SFSEDVISHK GDLRFVTISG
//
ID   B1ASU9_MOUSE            Unreviewed;       750 AA.
AC   B1ASU9;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 32.
DE   SubName: Full=Tousled-like kinase 2 (Arabidopsis);
GN   Name=Tlk2; ORFNames=RP23-456M3.2-006;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Tracey A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL645471; CAM24829.1; -; Genomic_DNA.
DR   IPI; IPI00648542; -.
DR   RefSeq; NP_001106176.1; NM_001112705.1.
DR   UniGene; Mm.126976; -.
DR   ProteinModelPortal; B1ASU9; -.
DR   SMR; B1ASU9; 434-719.
DR   STRING; B1ASU9; -.
DR   PRIDE; B1ASU9; -.
DR   Ensembl; ENSMUST00000106941; ENSMUSP00000102554; ENSMUSG00000020694.
DR   GeneID; 24086; -.
DR   KEGG; mmu:24086; -.
DR   CTD; 24086; -.
DR   MGI; MGI:1346023; Tlk2.
DR   HOGENOM; HBG607699; -.
DR   HOVERGEN; HBG007938; -.
DR   InParanoid; B1ASU9; -.
DR   OMA; GAENETP; -.
DR   NextBio; 304093; -.
DR   Bgee; B1ASU9; -.
DR   Genevestigator; B1ASU9; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding; Kinase; Nucleotide-binding; Transferase.
SQ   SEQUENCE   750 AA;  85342 MW;  A6FC0CF76E2C6DE9 CRC64;
     MMEELHSLDP RRQELLEARF TGVGVSKGPL NSESSNQSLC SVGSLSDKEV ETPEKKQNDQ
     RNRKRKAEPY DTSQGKGTPR GHKISDYFEF AGGSGPGTSP GRSVPPVARS SPQHSLSNPL
     PRRAEQPLYG LDGSAAKEAS EEQSALPTLM SVMLAKPRLD TEQLAPRGAG LCFTFVSAQQ
     NSPSSTGSGN TEHSCSSQKQ ISIQHRQTQS DLTIEKISAL ENSKNSDLEK KEGRIDDLLR
     ANCDLRRQID EQQKMLEKYK ERLNRCVTMS KKLLIEKSKQ EKMACRDKSM QDRLRLGHFT
     TVRHGASFTE QWTDGYAFQN LIKQQERINS QREEIERQRK MLAKRKPPAM GQAPPATNEQ
     KQRKSKTNGA ENETLTLAEY HEQEEIFKLR LGHLKKEEAE IQAELERLER VRNLHIRELK
     RIHNEDNSQF KDHPTLNDRY LLLHLLGRGG FSEVYKAFDL TEQRYVAVKI HQLNKNWRDE
     KKENYHKHAC REYRIHKELD HPRIVKLYDY FSLDTDSFCT VLEYCEGNDL DFYLKQHKLM
     SEKEARSIIM QIVNALKYLN EIKPPIIHYD LKPGNILLVN GTACGEIKIT DFGLSKIMDD
     DSYNSVDGME LTSQGAGTYW YLPPECFVVG KEPPKISNKV DVWSVGVIFY QCLYGRKPFG
     HNQSQQDILQ ENTILKATEV QFPPKPVVTP EAKAFIRRCL AYRKEDRIDV QQLACDPYLL
     PHIRKSVSTS SPAGAAIAST SGASNNSSSN
//
ID   B1ATI9_MOUSE            Unreviewed;       412 AA.
AC   B1ATI9;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 20.
DE   SubName: Full=Growth arrest specific 7;
GN   Name=Gas7; ORFNames=RP23-338M9.2-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Smith M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Lad H.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL662883; CAI24383.1; -; Genomic_DNA.
DR   EMBL; AL646097; CAI24383.1; JOINED; Genomic_DNA.
DR   EMBL; AL646097; CAI25246.1; -; Genomic_DNA.
DR   EMBL; AL662883; CAI25246.1; JOINED; Genomic_DNA.
DR   IPI; IPI00869375; -.
DR   UniGene; Mm.152121; -.
DR   UniGene; Mm.40338; -.
DR   ProteinModelPortal; B1ATI9; -.
DR   SMR; B1ATI9; 12-47, 135-411.
DR   STRING; B1ATI9; -.
DR   Ensembl; ENSMUST00000041611; ENSMUSP00000038420; ENSMUSG00000033066.
DR   Ensembl; ENSMUST00000108680; ENSMUSP00000104320; ENSMUSG00000033066.
DR   Ensembl; ENSMUST00000108681; ENSMUSP00000104321; ENSMUSG00000033066.
DR   Ensembl; ENSMUST00000108682; ENSMUSP00000104322; ENSMUSG00000033066.
DR   MGI; MGI:1202388; Gas7.
DR   HOVERGEN; HBG001320; -.
DR   InParanoid; B1ATI9; -.
DR   OrthoDB; EOG473PRG; -.
DR   PhylomeDB; B1ATI9; -.
DR   Bgee; B1ATI9; -.
DR   Genevestigator; B1ATI9; -.
DR   GO; GO:0005884; C:actin filament; IDA:MGI.
DR   GO; GO:0001726; C:ruffle; IDA:MGI.
DR   GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR   GO; GO:0051017; P:actin filament bundle assembly; IDA:MGI.
DR   GO; GO:0030041; P:actin filament polymerization; IDA:MGI.
DR   GO; GO:0048812; P:neuron projection morphogenesis; IMP:MGI.
DR   GO; GO:0008360; P:regulation of cell shape; IDA:MGI.
DR   InterPro; IPR001060; FCH.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF51045; WW_Rsp5_WWP; 1.
DR   PROSITE; PS50133; FCH; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   4: Predicted;
SQ   SEQUENCE   412 AA;  47261 MW;  C55B53CDB556395B CRC64;
     MVPPPPGEES QTVILPPGWH SYLSPQGRRY YVNTTTNETT WERPSSSPGI SASPGPHRSS
     LPTTVNGYHA SGTPAHPPET AHMSLRKSTG DSQNLGSSSP GRKQSKENTI TINCVTFPHP
     DTMPEQQLLK PTEWSYCDYF WADKKDPQGN GTVAGFELLL QKQLKGKQMQ KEMSEFIRER
     IKIEEEYAKN LAKLSQNSLA AQEEGSLGEA WAQVKKSLAD EAEVHLKFSA KLHSEVEKPL
     MNFRENFKKD MKKCDHHIAD LRKQLASRYA SVEKARKALT ERQKDLEMKT QQLEIKLSNK
     TEEDIKKARR KSTQAGDDLM RCVDLYNQAQ SKWFEEMVTT TLELERLEVE RVEMIRQHLC
     QYTQLRHETD MFNQSTVEPV DQLLRKVDPA KDRELWVREH KTGNIRPVDM EI
//
ID   B1ATV3_MOUSE            Unreviewed;       910 AA.
AC   B1ATV3;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 29.
DE   SubName: Full=Transient receptor potential cation channel, subfamily C, member 3;
GN   Name=Trpc3; ORFNames=CT7-314H19.1-001, mCG_14063;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Lloyd D.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL663106; CAM28054.1; -; Genomic_DNA.
DR   EMBL; CH466530; EDL35089.1; -; Genomic_DNA.
DR   IPI; IPI00137231; -.
DR   RefSeq; NP_062383.2; NM_019510.2.
DR   UniGene; Mm.74363; -.
DR   ProteinModelPortal; B1ATV3; -.
DR   SMR; B1ATV3; 102-253.
DR   STRING; B1ATV3; -.
DR   PRIDE; B1ATV3; -.
DR   Ensembl; ENSMUST00000029271; ENSMUSP00000029271; ENSMUSG00000027716.
DR   GeneID; 22065; -.
DR   KEGG; mmu:22065; -.
DR   CTD; 22065; -.
DR   MGI; MGI:109526; Trpc3.
DR   HOGENOM; HBG355804; -.
DR   HOVERGEN; HBG068337; -.
DR   InParanoid; B1ATV3; -.
DR   OMA; CTEKQRH; -.
DR   NextBio; 301880; -.
DR   Bgee; B1ATV3; -.
DR   Genevestigator; B1ATV3; -.
DR   GO; GO:0005262; F:calcium channel activity; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR013555; TRP_2.
DR   InterPro; IPR004729; TRP_channel.
DR   InterPro; IPR005459; TRPC3_channel.
DR   InterPro; IPR002153; TRPC_channel.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 2.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF08344; TRP_2; 1.
DR   PRINTS; PR01097; TRNSRECEPTRP.
DR   PRINTS; PR01644; TRPCHANNEL3.
DR   SMART; SM00248; ANK; 3.
DR   SUPFAM; SSF48403; ANK; 1.
DR   TIGRFAMs; TIGR00870; trp; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
PE   4: Predicted;
KW   Ion transport; Ionic channel; Membrane; Receptor; Transmembrane;
KW   Transport.
SQ   SEQUENCE   910 AA;  103620 MW;  3773375324F0E67C CRC64;
     MSTKVKKCRE PARVTLPAPE EEEDGEAEGG ESQRRRRGWR GVNGGLEPPC PRAPPSPGPD
     ASSEGSPSRW RTAGMRDKGR RQAVRGPAFM FGARGPSLTA EEERFLDAAE YGNIPVVRKM
     LEESRTLNVN CVDYMGQNAL QLAVGNEHLE VTELLLKKEN LARIGDALLL AISKGYVRIV
     EAILGHPGFA ASRRLTLSPC EQELRDDDFY AYDEDGTRFS PDITPIILAA HCHKYEVVHL
     LLLKGARIER PHDYFCRCSD CAEKQRLDAF SHSRSRINAY KGLASPAYLS LSSEDPVLTA
     LELSNELAKL ANIEKEFKND YRKLSMQCKD FVVGVLDLCR DSEEVEAILN GDLESAEPLE
     RHGHKASLSR VKLAIKYEVK KFVAHPNCQQ QLLTIWYENL SGLREQTIAI KCLVVLVVAL
     GLPFLAIGYW IAPCSRLGKI LRSPFMKFVA HAASFIIFLG LLVFNASDRF EGITTLPNIT
     VIDYPKQIFR VKTTQFTWTE MLIMVWVLGM MWSECKELWL EGPREYIVQL WNVLDFGMLS
     IFIAAFTARF LAFLQATKAQ QYVDSHVQES DLSEVTLPPE VQYFTYARDK WLPSDPQIIS
     EGLYAIAVVL SFSRIAYILP ANESFGPLQI SLGRTVKDIF KFMVLFIMVF LAFMIGMFIL
     YSYYLGAKVN PAFTTVEESF KTLFWSIFGL SEVTSVVLKY DHKFIENIGY VLYGIYNVTM
     VVVLLNMLIA MINSSYQEIE DDSDVEWKFA RSKLWLSYFD DGKTLPPPFS LVPSPKSFVY
     FIMRITNFSK CRRRRLQKDL ELGMGNSKSR LNLFTQSNSR VFESHSFNSI LNQPTRYQQI
     MKRLIKRYVL KAQVDKENDE VNEGELKEIK QDISSLRYEL LEDKSQATEE LAILIHKLSE
     KLNPSVLRCE
//
ID   B1AUH5_MOUSE            Unreviewed;       155 AA.
AC   B1AUH5;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-FEB-2011, entry version 20.
DE   SubName: Full=Calcium/calmodulin-dependent serine protein kinase (MAGUK family);
DE   Flags: Fragment;
GN   Name=Cask; ORFNames=RP23-278L4.1-006;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Clark S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Howden P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL671117; CAM19442.1; -; Genomic_DNA.
DR   EMBL; AL672204; CAM19442.1; JOINED; Genomic_DNA.
DR   EMBL; BX005215; CAM19442.1; JOINED; Genomic_DNA.
DR   EMBL; BX005215; CAM19530.1; -; Genomic_DNA.
DR   EMBL; AL671117; CAM19530.1; JOINED; Genomic_DNA.
DR   EMBL; AL672204; CAM19530.1; JOINED; Genomic_DNA.
DR   EMBL; AL672204; CAM20908.1; -; Genomic_DNA.
DR   EMBL; AL671117; CAM20908.1; JOINED; Genomic_DNA.
DR   EMBL; BX005215; CAM20908.1; JOINED; Genomic_DNA.
DR   IPI; IPI00775782; -.
DR   UniGene; Mm.327591; -.
DR   UniGene; Mm.474948; -.
DR   STRING; B1AUH5; -.
DR   Ensembl; ENSMUST00000124710; ENSMUSP00000119584; ENSMUSG00000031012.
DR   MGI; MGI:1309489; Cask.
DR   GeneTree; ENSGT00560000077048; -.
DR   HOVERGEN; HBG098089; -.
DR   InParanoid; B1AUH5; -.
DR   Bgee; B1AUH5; -.
DR   Genevestigator; B1AUH5; -.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   Kinase; Transferase.
FT   NON_TER     155    155
SQ   SEQUENCE   155 AA;  17734 MW;  9B1B4F0BB9BEAA9A CRC64;
     MADDDVLFED VYELCEVIGK GPFSVVRRCI NRETGQQFAV KIVDVAKFTS SPGLSTEGKR
     WISNLKREAS ICHMLKHPHI VELLETYSSD GMLYMVFEFM DGADLCFEIV KRADAGFVYS
     EAVASHYMRQ ILEALRYCHD NNIIHRDVKP HCVLL
//
ID   B1AUX1_MOUSE            Unreviewed;      2045 AA.
AC   B1AUX1;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 29.
DE   SubName: Full=Host cell factor C1;
GN   Name=Hcfc1; ORFNames=RP23-252M19.5-001, mCG_8083;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Johnson C.;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL672002; CAM18726.1; -; Genomic_DNA.
DR   EMBL; CH466650; EDL29851.1; -; Genomic_DNA.
DR   IPI; IPI00828543; -.
DR   RefSeq; NP_032250.2; NM_008224.3.
DR   UniGene; Mm.420572; -.
DR   UniGene; Mm.439140; -.
DR   UniGene; Mm.480587; -.
DR   ProteinModelPortal; B1AUX1; -.
DR   SMR; B1AUX1; 1899-2016.
DR   STRING; B1AUX1; -.
DR   PRIDE; B1AUX1; -.
DR   Ensembl; ENSMUST00000033761; ENSMUSP00000033761; ENSMUSG00000031386.
DR   GeneID; 15161; -.
DR   KEGG; mmu:15161; -.
DR   CTD; 15161; -.
DR   MGI; MGI:105942; Hcfc1.
DR   HOVERGEN; HBG051888; -.
DR   PhylomeDB; B1AUX1; -.
DR   NextBio; 287652; -.
DR   Bgee; B1AUX1; -.
DR   Genevestigator; B1AUX1; -.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR011498; Kelch_2.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Gene3D; G3DSA:2.120.10.80; Kelch-typ_b-propeller; 1.
DR   Pfam; PF01344; Kelch_1; 2.
DR   Pfam; PF07646; Kelch_2; 1.
DR   SMART; SM00060; FN3; 2.
DR   SUPFAM; SSF49265; FN_III-like; 2.
PE   4: Predicted;
SQ   SEQUENCE   2045 AA;  210437 MW;  AD0EC38C9DB19F22 CRC64;
     MASAVSPANL PAVLLQPRWK RVVGWSGPVP RPRHGHRAVA IKELIVVFGG GNEGIVDELH
     VYNTATNQWF IPAVRGDIPP GCAAYGFVCD GTRLLVFGGM VEYGKYSNDL YELQASRWEW
     KRLKAKTPKN GPPPCPRLGH SFSLVGNKCY LFGGLANDSE DPKNNIPRYL NDLYILELRP
     GSGVVAWDIP ITYGVLPPPR ESHTAVVYTE KDNKKSKLVI YGGMSGCRLG DLWTLDIETL
     TWNKPSLSGV APLPRSLHSA TTIGNKMYVF GGWVPLVMDD VKVATHEKEW KCTNTLACLN
     LDTMAWETIL MDTLEDNIPR ARAGHCAVAI NTRLYIWSGR DGYRKAWNNQ VCCKDLWYLE
     TEKPPPPARV QLVRANTNSL EVSWGAVATA DSYLLQLQKY DIPATAATAT SPTPNPVPSV
     PANPPKSPAP AAAAPAVQPL TQVGITLVPQ AATAPPSTTT IQVLPTVPGS SISVPTAART
     QGVPAVLKVT GPQATTGTPL VTMRPASQAG KAPVTVTSLP ASVRMVVPTQ SAQGTVIGSN
     PQMSGMAALA AAAAATQKIP PSSAPTVLSV PAGTTIVKTV AVTPGTTTLP ATVKVASSPV
     MVSNPATRML KTAAAQVGTS VSSAANTSTR PIITVHKSGT VTVAQQAQVV TTVVGGVTKT
     ITLVKSPISV PGGSALISNL GKVMSVVQTK PVQTSAVTGQ ASTGPVTQII QTKGPLPAGT
     ILKLVTSADG KPTTIITTTQ ASGAGTKPTI LGISSVSPST TKPGTTTIIK TIPMSAIITQ
     AGATGVTSSP GIKSPITIIT TKVMTSGTGA PAKIITAVPK IATGHGQQGV TQVVLKGAPG
     QPGTILRTVP MGGVRLVTPV TVSAVKPAVT TLVVKGTTGV TTLGTVTGTV STSLAGAGAH
     STSASLATPI TTLGTIATLS SQVINPTAIT VSAAQTTLTA AGGLTTPTIT MQPVSQPTQV
     TLITAPSGVE AQPVHDLPVS ILASPTTEQP TATVTIADSG QGDVQPGTVT LVCSNPPCET
     HETGTTNTAT TTVVANLGGH PQPTQVQFVC DRQETAASLV TSAVGQQNGN VVRVCSNPPC
     ETHETGTTNT ATTATSNMAG QHGCSNPPCE THETGTTSTA TTAMSSMGTG QQRDTRRTTN
     TPTVVRITVA PGALERVQGT VKPQCQTQQT NMTTTTMTVQ ATGAPCSAGP LLRPSVALES
     GSHSPAFVQL ALPSVRVGLS GPSSKDMPTG RQPETYHTYT TNTPTTTRSI MVAGELGAAR
     VVPTSTYESL QASSPSSTMT MTALEALLCP SATVTQVCSN PPCETHETGT TNTATTSNAG
     SAQRVCSNPP CETHETGTTH TATTATSNGG AGQPEGGQQP ASGHPCETHQ TTSTGTTMSV
     SVGTLIPDAT SSHGTLESGL EVVAVPTVTS QAGSTLLASF PTQRVCSNPP CETHETGTTH
     TATTVTSNMS SNQDPPPAAS DQGEVASTQG DSTNITSASA ITTSVSSTLP RAVTTVTQST
     PVPGPSVPPP EELQVSPGPR QQLPPRQLLQ SASTPLMGES TEVLSASQTP ELQAAVDLSS
     TGDPSSGQEP TTSAVVATVV VQPPPPTQSE VDQLSLPQEL MAEAQAGTTT LMVTGLTPEE
     LAVTAAAEAA AQAAATEEAQ ALAIQAVLQA AQQAVMGTGE PMDTSEAAAA VTQAELGHLS
     AEGQEGQATT IPIVLTQQEL AALVQQQQQL QEAQAQAQQQ HHLPTEALAP ADSLNDPSIE
     SNCLNELASA VPSTVALLPS TATESLAPSN TFVAPQPVVA SPAKMQAAAT LTEVANGIES
     LGVKPDLPPP PSKAPVKKEN QWFDVGVIKG TSVMVTHYFL PPDDAVQSDD DSGTVPDYNQ
     LKKQELQPGT AYKFRVAGIN ACGRGPFSEI SAFKTCLPGF PGAPCAIKIS KSPDGAHLTW
     EPPSVTSGKI IEYSVYLAIQ SSQASGEPKS STPAQLAFMR VYCGPSPSCL VQSSSLSNAH
     IDYTTKPAII FRIAARNEKG YGPATQVRWL QETSKDSSGT KPASKRPMSS PEMKSAPKKS
     KADGQ
//
ID   B1AV20_MOUSE            Unreviewed;       518 AA.
AC   B1AV20;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   05-OCT-2010, entry version 19.
DE   SubName: Full=RALBP1 associated Eps domain containing protein 2;
DE   Flags: Fragment;
GN   Name=Reps2; ORFNames=RP23-436I3.2-002;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Brown J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL672039; CAM20009.1; -; Genomic_DNA.
DR   IPI; IPI00652746; -.
DR   STRING; B1AV20; -.
DR   Ensembl; ENSMUST00000154424; ENSMUSP00000114744; ENSMUSG00000040855.
DR   MGI; MGI:2663511; Reps2.
DR   HOVERGEN; HBG056372; -.
DR   Bgee; B1AV20; -.
DR   Genevestigator; B1AV20; -.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR000261; EPS15_homology.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   SMART; SM00027; EH; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS50031; EH; 1.
PE   4: Predicted;
FT   NON_TER       1      1
SQ   SEQUENCE   518 AA;  57533 MW;  63C14AC4F5834019 CRC64;
     WRERPLNHCI HITELCGAKR VGYFGPTQFY VALKLIAAAQ AGLPVRTESI KCELPLPRFV
     MSKNDGEIRF GNPAELHGPK VQIPYLTTEK NSFKRMDNED KQETQSPTMS PLASPPSSPP
     HYQRVSLSHG YSKLRSGTEQ MHPAPYERQP IGQPEGPSSE GPGAKPFRRQ ASLIRSFSVE
     REPQENNSNY PDEPWRITEE QREYYVNQFR SLQPDPSSFI SGSVAKNFFT KSKLSIPELS
     YIWELSDADC DGALTLSEFC AAFHLIVARK NGYPLPEGLP PTLQPEYLQA AFPKSKWECA
     IFDSYSESMP ANQQSCDLNR METSVKDVAD FPVPTQDVTT ADDKQALKST VNESLPKDVS
     EDTAANSGLL PPPPALPPRP CPTQSEPVSE ADLHSQLNRA PSQAAESSPT KMDAPHAQPP
     SKPIRRKFRP ENQTTESQEP AAAVGGAVSA AMVKPHPTVQ KQSSKQKKAI QTAIRKNKEA
     NAVLARLNSE LQQQLKEVHQ ERIALENQLE QLRPVTVL
//
ID   B1AVE8_MOUSE            Unreviewed;       628 AA.
AC   B1AVE8;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   11-JAN-2011, entry version 27.
DE   SubName: Full=SH3-domain kinase binding protein 1;
GN   Name=Sh3kbp1; ORFNames=RP23-39I7.6-002;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Griffiths C.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Howden P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RA   Clark S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BX548017; CAM21339.1; -; Genomic_DNA.
DR   EMBL; AL683803; CAM21339.1; JOINED; Genomic_DNA.
DR   EMBL; AL929452; CAM21339.1; JOINED; Genomic_DNA.
DR   EMBL; AL929452; CAM21672.1; -; Genomic_DNA.
DR   EMBL; AL683803; CAM21672.1; JOINED; Genomic_DNA.
DR   EMBL; BX548017; CAM21672.1; JOINED; Genomic_DNA.
DR   EMBL; AL683803; CAM24636.1; -; Genomic_DNA.
DR   EMBL; AL929452; CAM24636.1; JOINED; Genomic_DNA.
DR   EMBL; BX548017; CAM24636.1; JOINED; Genomic_DNA.
DR   IPI; IPI00312101; -.
DR   RefSeq; NP_067364.2; NM_021389.5.
DR   UniGene; Mm.286495; -.
DR   ProteinModelPortal; B1AVE8; -.
DR   SMR; B1AVE8; 55-129, 230-290.
DR   STRING; B1AVE8; -.
DR   PRIDE; B1AVE8; -.
DR   Ensembl; ENSMUST00000080394; ENSMUSP00000079257; ENSMUSG00000040990.
DR   GeneID; 58194; -.
DR   KEGG; mmu:58194; -.
DR   CTD; 58194; -.
DR   MGI; MGI:1889583; Sh3kbp1.
DR   HOVERGEN; HBG057824; -.
DR   NextBio; 314169; -.
DR   Bgee; B1AVE8; -.
DR   Genevestigator; B1AVE8; -.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR013315; Spectrin_alpha_SH3.
DR   Pfam; PF07653; SH3_2; 2.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR01887; SPECTRNALPHA.
DR   SMART; SM00326; SH3; 2.
DR   SUPFAM; SSF50044; SH3; 2.
DR   PROSITE; PS50002; SH3; 2.
PE   4: Predicted;
KW   Kinase; Transferase.
SQ   SEQUENCE   628 AA;  68820 MW;  1C4AEC6BE48D5D17 CRC64;
     MELSAAKAPS PTDLPESEIK KDMKKDLLSN KAPEKPMHDV SSGNALLSSE TILRTNKRGE
     RRRRRCQVAF SYLPQNDDEL ELKVGDIIEV VGEVEEGWWE GVLNGKTGMF PSNFIKELSG
     ESDELGISQD EQLSKSSLRE TTGSESDGGD SSSTKSEGAN GTMATAAIQP KKVKGVGFGD
     IFKDKPIKLR PRSIEVENDF LPVEKTIGKK LPPATSTPDP SKTEMDSRTK TKDYCKVIFP
     YEAQNDDELT IKEGDIVTLI NKDCIDVGWW EGELNGRRGV FPDNFVKLLP SDFDKEGNRP
     KKPPPPSAPV VKQGAGTTER KHEIKKIPPE RPETLPNRTE EKERPEREPK LDLQKPSVPA
     IPPKKPRPPK TNSLNRPGAL PPRRPERPVG PLTHTRGDSP KIDLAGSALS GILDKDLSDR
     SNDIDLEGFD SVISSTEKLS HPTTSRPKAT GRRPPSQSLT SSSLSSPDIF DSPSPEEDKE
     EHISLAHRGI DVSKKTSKTV TISQVSDNKT SLPPKPGTMA AASSGPASLS SVASSPMSSS
     LGTAGQRASS PSLFSTEGKP KMEPAVSSQA AIEELKMQVR ELRTIIETMK DQQKREIKQL
     LSELDEEKKI RLRLQMEVND IKKALQSK
//
ID   B1AVZ0_MOUSE            Unreviewed;       310 AA.
AC   B1AVZ0;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 27.
DE   SubName: Full=Novel protein;
DE   SubName: Full=Uracil phosphoribosyltransferase (FUR1) homolog (S. cerevisiae);
GN   Name=Uprt; ORFNames=RP23-92C4.1-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Brown J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC147845; AAI47846.1; -; mRNA.
DR   EMBL; BC147853; AAI47854.1; -; mRNA.
DR   EMBL; AL731717; CAM27338.1; -; Genomic_DNA.
DR   IPI; IPI00111145; -.
DR   RefSeq; NP_001074658.1; NM_001081189.1.
DR   UniGene; Mm.438275; -.
DR   ProteinModelPortal; B1AVZ0; -.
DR   SMR; B1AVZ0; 109-309.
DR   STRING; B1AVZ0; -.
DR   PhosphoSite; B1AVZ0; -.
DR   PRIDE; B1AVZ0; -.
DR   Ensembl; ENSMUST00000087867; ENSMUSP00000085175; ENSMUSG00000073016.
DR   GeneID; 331487; -.
DR   KEGG; mmu:331487; -.
DR   CTD; 331487; -.
DR   MGI; MGI:2685620; Uprt.
DR   eggNOG; roNOG11186; -.
DR   GeneTree; ENSGT00510000047272; -.
DR   HOGENOM; HBG326432; -.
DR   HOVERGEN; HBG105296; -.
DR   InParanoid; B1AVZ0; -.
DR   OMA; LLMYPIM; -.
DR   OrthoDB; EOG44TP8D; -.
DR   PhylomeDB; B1AVZ0; -.
DR   NextBio; 399790; -.
DR   Bgee; B1AVZ0; -.
DR   Genevestigator; B1AVZ0; -.
DR   GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   InterPro; IPR000836; PRibTrfase.
DR   Pfam; PF00156; Pribosyltran; 1.
PE   2: Evidence at transcript level;
KW   Glycosyltransferase; Transferase.
SQ   SEQUENCE   310 AA;  34278 MW;  5EB768287D80B879 CRC64;
     MASELQRPDS MPCHNRQVNS TSSPSPEHLL AEDRVLDHAE ENNAAMAKLT LLPGHAHSSV
     LSERDSPACC STNLHSENHS DSSDSGNYDA PVGGDSLLGD CELSRQIGAQ LKLLPMNDQI
     RELQTIIRDK TASRGDFMFS ADRLIRLVVE EGLNQLPYKE CMVTTPTGHK YEGVKFEKGN
     CGVSIMRSGE AMEQGLRDCC RSIRIGKILI QSDEETQRAK VYYAKFPPDI HRRKVLLMYP
     ILSTGNTVIE AVKVLIEHGV QPSVIILLSL FSTPHGAKSI IQEFPEITIL TTEVHPVAPT
     HFGQKYFGTD
//
ID   B1AWE0_MOUSE            Unreviewed;       216 AA.
AC   B1AWE0;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 24.
DE   SubName: Full=Clathrin light polypeptide (Lca);
GN   Name=Clta; ORFNames=RP23-209M8.4-004;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Phillimore B.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL732563; CAM17521.1; -; Genomic_DNA.
DR   IPI; IPI00648658; -.
DR   RefSeq; NP_001073855.1; NM_001080386.1.
DR   UniGene; Mm.298875; -.
DR   PRIDE; B1AWE0; -.
DR   Ensembl; ENSMUST00000107845; ENSMUSP00000103477; ENSMUSG00000028478.
DR   GeneID; 12757; -.
DR   KEGG; mmu:12757; -.
DR   CTD; 12757; -.
DR   MGI; MGI:894297; Clta.
DR   GeneTree; ENSGT00390000010441; -.
DR   HOVERGEN; HBG003386; -.
DR   NextBio; 282098; -.
DR   Bgee; B1AWE0; -.
DR   Genevestigator; B1AWE0; -.
DR   GO; GO:0030132; C:clathrin coat of coated pit; IEA:InterPro.
DR   GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR000996; Clathrin_L-chain.
DR   PANTHER; PTHR10639; Clathrin_lg_ch; 1.
DR   Pfam; PF01086; Clathrin_lg_ch; 1.
DR   PROSITE; PS00224; CLATHRIN_LIGHT_CHN_1; 1.
DR   PROSITE; PS00581; CLATHRIN_LIGHT_CHN_2; 1.
PE   4: Predicted;
SQ   SEQUENCE   216 AA;  23479 MW;  7D299741BCF29AC3 CRC64;
     MAELDPFGAP AGAPGGPALG NGVAGAGEED PAAAFLAQQE SEIAGIENDE AFAILDGGAP
     GPQPHGEPPG DAVDGVMNGE YYQESNGPTD SYAAISEVDR LQSEPESIRK WREEQTERLE
     ALDANSRKQE AEWKEKAIKE LEEWYARQDE QLQKTKANNR AAEEAFVNDI DESSPGTEWE
     RVARLCDFNP KSSKQAKDVS RMRSVLISLK QAPLVH
//
ID   B1AWN6_MOUSE            Unreviewed;      2006 AA.
AC   B1AWN6;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 28.
DE   SubName: Full=Sodium channel voltage-gated type II alpha 1;
GN   Name=Scn2a1; ORFNames=RP23-300F1.1-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Tracey A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Mashreghi-Mohammadi M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the sodium channel family.
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DR   EMBL; AL772235; CAM15654.1; -; Genomic_DNA.
DR   EMBL; BX284648; CAM15654.1; JOINED; Genomic_DNA.
DR   EMBL; BX284648; CAM20181.1; -; Genomic_DNA.
DR   EMBL; AL772235; CAM20181.1; JOINED; Genomic_DNA.
DR   IPI; IPI00761641; -.
DR   RefSeq; NP_001092768.1; NM_001099298.2.
DR   UniGene; Mm.220329; -.
DR   ProteinModelPortal; B1AWN6; -.
DR   PRIDE; B1AWN6; -.
DR   Ensembl; ENSMUST00000028377; ENSMUSP00000028377; ENSMUSG00000075318.
DR   Ensembl; ENSMUST00000100067; ENSMUSP00000097645; ENSMUSG00000075318.
DR   GeneID; 110876; -.
DR   KEGG; mmu:110876; -.
DR   CTD; 110876; -.
DR   MGI; MGI:98248; Scn2a1.
DR   HOGENOM; HBG358468; -.
DR   HOVERGEN; HBG053100; -.
DR   InParanoid; B1AWN6; -.
DR   OMA; MSMASIL; -.
DR   NextBio; 364833; -.
DR   Bgee; B1AWN6; -.
DR   Genevestigator; B1AWN6; -.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0014704; C:intercalated disc; IDA:MGI.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0030315; C:T-tubule; IDA:MGI.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; TAS:MGI.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:MGI.
DR   GO; GO:0006915; P:apoptosis; IMP:MGI.
DR   GO; GO:0007399; P:nervous system development; IMP:MGI.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001696; Na_channel_asu.
DR   InterPro; IPR010526; Na_trans_assoc.
DR   Pfam; PF00520; Ion_trans; 4.
DR   Pfam; PF06512; Na_trans_assoc; 1.
DR   PRINTS; PR00170; NACHANNEL.
DR   SMART; SM00015; IQ; 1.
DR   PROSITE; PS50096; IQ; 1.
PE   3: Inferred from homology;
KW   Ion transport; Ionic channel; Membrane; Sodium; Sodium channel;
KW   Sodium transport; Transmembrane; Transport; Voltage-gated channel.
SQ   SEQUENCE   2006 AA;  227945 MW;  8A607C83C4E97F0D CRC64;
     MAQSVLVPPG PDSFRFFTRE SLAAIEQRIA EEKAKRPKQE RKDEDDENGP KPNSDLEAGK
     SLPFIYGDIP PEMVSEPLED LDPYYINKKT FIVLNKGKAI SRFSATSALY ILTPFNPIRK
     LAIKILVHSL FNVLIMCTIL TNCVFMTMSN PPDWTKNVEY TFTGIYTFES LIKILARGFC
     LEDFTFLRDP WNWLDFTVIT FAYVTEFVNL GNVSALRTFR VLRALKTISV IPGLKTIVGA
     LIQSVKKLSD VMILTVFCLS VFALIGLQLF MGNLRNKCLQ WPPDNSTFEI NITSFFNNSL
     DWNGTAFNRT MNMFNWDEYI EDKSHFYFLE GQNDALLCGN SSDAGQCPEG YICVKAGRNP
     NYGYTSFDTF SWAFLSLFRL MTQDFWENLY QLTLRAAGKT YMIFFVLVIF LGSFYLINLI
     LAVVAMAYEE QNQATLEEAE QKEAEFQQML EQLKKQQEEA QAAAAAASAE SRDFSGAGGI
     GVFSESSSVA SKLSSKSEKE LKNRRKKKKQ KEQAGEEEKE DAVRKSASED SIRKKGFRFS
     LEGSRLTYEK RFSSPHQSLL SIRGSLFSPR RNSRASLFSF KGRVKDIGSE NDFADDEHST
     FEDNDSRRDS LFVPHRHGER RPSNVSQASR ASRGIPTLPM NGKMHSAVDC NGVVSLVGGP
     SALTSPVGQL LPEGTTTETE IRKRRSSSYH VSMDLLEDPT SRQRAMSMAS ILTNTMEELE
     ESRQKCPPCW YKFANMCLIW DCCKPWLKVK HVVNLVVMDP FVDLAITICI VLNTLFMAME
     HYPMTEQFSS VLSVGNLVFT GIFTAEMFLK IIAMDPYYYF QEGWNIFDGF IVSLSLMELG
     LANVEGLSVL RSFRLLRVFK LAKSWPTLNM LIKIIGNSVG ALGNLTLVLA IIVFIFAVVG
     MQLFGKSYKE CVCKISNDCE LPRWHMHDFF HSFLIVFRVL CGEWIETMWD CMEVAGQTMC
     LTVFMMVMVI GNLVVLNLFL ALLLSSFSSD NLAATDDDNE MNNLQIAVGR MQKGIDFVKR
     KIREFIQKAF VRKQKALDEI KPLEDLNNKK DSCISNHTTI EIGKDLNYLK DGNGTTSGIG
     SSVEKYVVDE SDYMSFINNP SLTVTVPIAV GESDFENLNT EEFSSESDME ESKEKLNATS
     SSEGSTVDIG APAEGEQPEA EPEESLEPEA CFTEDCVRKF KCCQISIEEG KGKLWWNLRK
     TCYKIVEHNW FETFIVFMIL LSSGALAFED IYIEQRKTIK TMLEYADKVF TYIFILEMLL
     KWVAYGFQMY FTNAWCWLDF LIVDVSLVSL TANALGYSEL GAIKSLRTLR ALRPLRALSR
     FEGMRVVVNA LLGAIPSIMN VLLVCLIFWL IFSIMGVNLF AGKFYHCINY TTGEMFDVSV
     VNNYSECQAL IESNQTARWK NVKVNFDNVG LGYLSLLQVA TFKGWMDIMY AAVDSRNVEL
     QPKYEDNLYM YLYFVIFIIF GSFFTLNLFI GVIIDNFNQQ KKKFGGQDIF MTEEQKKYYN
     AMKKLGSKKP QKPIPRPANK FQGMVFDFVT KQVFDISIMI LICLNMVTMM VETDDQSQEM
     TNILYWINLV FIVLFTGECV LKLISLRHYY FTIGWNIFDF VVVILSIVGM FLAELIEKYF
     VSPTLFRVIR LARIGRILRL IKGAKGIRTL LFALMMSLPA LFNIGLLLFL VMFIYAIFGM
     SNFAYVKREV GIDDMFNFET FGNSMICLFQ ITTSAGWDGL LAPILNSGPP DCDPEKDHPG
     SSVKGDCGNP SVGIFFFVSY IIISFLVVVN MYIAVILENF SVATEESAEP LSEDDFEMFY
     EVWEKFDPDA TQFIEFCKLS DFAAALDPPL LIAKPNKVQL IAMDLPMVSG DRIHCLDILF
     AFTKRVLGES GEMDALRIQM EERFMASNPS KVSYEPITTT LKRKQEEVSA IVIQRAYRRY
     LLKQKVKKVS SIYKKDKGKE DEGTPIKEDI ITDKLNENST PEKTDVTPST TSPPSYDSVT
     KPEKEKFEKD KSEKEDKGKD IRESKK
//
ID   B1AWT2_MOUSE            Unreviewed;       399 AA.
AC   B1AWT2;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 24.
DE   SubName: Full=Ras-related GTP binding D;
DE   SubName: Full=Ras-related GTP binding D, isoform CRA_a;
GN   Name=Rragd; ORFNames=RP23-360H6.3-001, mCG_12768;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Dunn M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL772288; CAM22251.1; -; Genomic_DNA.
DR   EMBL; CH466538; EDL05495.1; -; Genomic_DNA.
DR   IPI; IPI00649297; -.
DR   RefSeq; NP_081767.2; NM_027491.2.
DR   UniGene; Mm.300814; -.
DR   UniGene; Mm.396693; -.
DR   ProteinModelPortal; B1AWT2; -.
DR   SMR; B1AWT2; 60-238.
DR   STRING; B1AWT2; -.
DR   Ensembl; ENSMUST00000098190; ENSMUSP00000095792; ENSMUSG00000028278.
DR   GeneID; 52187; -.
DR   KEGG; mmu:52187; -.
DR   CTD; 52187; -.
DR   MGI; MGI:1098604; Rragd.
DR   eggNOG; roNOG06920; -.
DR   GeneTree; ENSGT00550000074708; -.
DR   HOVERGEN; HBG059482; -.
DR   OrthoDB; EOG4CG08D; -.
DR   PhylomeDB; B1AWT2; -.
DR   NextBio; 308622; -.
DR   Bgee; B1AWT2; -.
DR   Genevestigator; B1AWT2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   InterPro; IPR006762; Gtr1_RagA.
DR   PANTHER; PTHR11259; Gtr1_RagA; 1.
DR   Pfam; PF04670; Gtr1_RagA; 1.
PE   4: Predicted;
SQ   SEQUENCE   399 AA;  45145 MW;  58010DD934BAB898 CRC64;
     MSQVLGKPQP QGEDGGEDEE EDELVGLAGY EDGPESSDAE LDSGPEEGVL DFSDPFSTEV
     KPRILLMGLR RSGKSSIQKV VFHKMSPSET LFLESTNRIC REDVSNSSFV NFQIWDFPGQ
     IDFFDPTFDY EMIFRGTGAL IFVIDSQDDY MEALARLHLT VTRAYKVNTD INFEVFIHKV
     DGLSDDHKIE TQRDIHQRAN DDLADAGLEK IHLSFYLTSI YDHSIFEAFS KVVQKLIPQL
     PTLENLLNIF ISNSGIEKAF LFDVVSKIYI ATDSTPVDMQ TYELCCDMID VVIDISCIYG
     LKEDGAGAPY DKDSTAIIKL NNTTVLYLKE VTKFLALVCF VREESFERKG LIDYNFHCFR
     KAIHEVFEVR MKMVKSRKAQ SRLPKKTGAT PNGTPRVLL
//
ID   B1AWV2_MOUSE            Unreviewed;      1136 AA.
AC   B1AWV2;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   05-OCT-2010, entry version 19.
DE   SubName: Full=Palm2-Akap2 fusion protein;
DE   Flags: Fragment;
GN   Name=Akap2; Synonyms=Palm2-Akap2; ORFNames=RP23-334A5.2-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Phillimore B.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL772312; CAM27309.1; -; Genomic_DNA.
DR   EMBL; AL840629; CAM27309.1; JOINED; Genomic_DNA.
DR   UniGene; Mm.331630; -.
DR   STRING; B1AWV2; -.
DR   Ensembl; ENSMUST00000030049; ENSMUSP00000030049; ENSMUSG00000038729.
DR   Ensembl; ENSMUST00000150412; ENSMUSP00000117466; ENSMUSG00000089945.
DR   HOVERGEN; HBG050477; -.
DR   InParanoid; B1AWV2; -.
DR   OMA; QYCVRKV; -.
DR   Bgee; B1AWV2; -.
DR   Genevestigator; B1AWV2; -.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:InterPro.
DR   InterPro; IPR004965; Paralemmin.
DR   InterPro; IPR018459; RII_binding_1.
DR   Pfam; PF03285; Paralemmin; 1.
DR   Pfam; PF10522; RII_binding_1; 1.
PE   4: Predicted;
FT   NON_TER       1      1
SQ   SEQUENCE   1136 AA;  125977 MW;  C27F307F126AA0C8 CRC64;
     FAQPLWKCLH RCGPFPLPLL AFRFLEPTPT HSDSLSLSLS LSLSLSLSLS LSLSPLSLHF
     FKEKRKRQTE IEGKRRQLDE QVLLLQHSKS KVLREKWLLQ GVPAGTAEEE EARRRQSEED
     EFKVKQLEDN IQRLEQEIQA LESEESQISA KEQIILEKLK ETEKSFKDLQ KSFSTADGAS
     GWSTVLLQGD ELTADPIGTN ADMAIQKPPQ LSEDANQLRS KQDNCGDSRL EPAASSLSPD
     HKNMEIGVSV AECKSVPGVT STPHSKDHSS PFYSPSHNGL LADHHESLDN DVAREIQYLD
     EVLEANCCDS SVDGTYNGIS SPEPGAAILV SSLGSPAHSV TEAEPTEKAS GRQVPPHIEL
     SRSPSDRMAE GERANGHSTD QPQDLLGNSL QAPASPSSST SSHCSSRDGE FTLTTLKKEA
     KFELRAFHED KKPSKLFEED EREKEQFCVR KVRPSEEMIE LEKERRELIR SQAVKKNPGI
     AAKWWNPPQE KTIEEQLDEE HLESHRKYKE RKEKRAQQEQ LQLQQQQQQQ LQQQQLQQQQ
     LQQQQLQQQL QQQQLSTSQP CTAPAAHKHL DGIEHTKEDV VTEQIDFSAA RKQFQLMENS
     RQTLAKGQST PRLFSIKPYY KPLGSIHSDK PPTILRPATV GGTLEDGGTQ AAKEQKAPCV
     SESQSAGAGP ANAATQGKEG PYSEPSKRGP LSKLWAEDGE FTSARAVLTV VKDEDHGILD
     QFSRSVNVSL TQEELDSGLD ELSVRSQDTT VLETLSNDFS MDNISDSGAS NETPSALQEN
     SLADFSLPQT PQTDNPSEGR EGVSKSFSDH GFYSPSSTLG DSPSVDDPLE YQAGLLVQNA
     IQQAIAEQVD KAEAHTSKEG SEQQEPEATV EEAGSQTPGS EKPQGMFAPP QVSSPVQEKR
     DILPKNLPAE DRALREKGPS QPPTAAQPSG PVNMEETRPE GGYFSKYSEA AELRSTASLL
     ATQESDVMVG PFKLRSRKQR TLSMIEEEIR AAQEREEELK RQRQVRQSTP SPRAKNAPSL
     PSRTTCYKTA PGKIEKVKPP PSPTTEGPSL QPDLAPEEAA GTQRPKNLMQ TLMEDYETHK
     SKRRERMDDS SYTSKLLSCK VTSEVLEATR VNRRKSALAL RWEAGIYANQ EEEDNE
//
ID   B1AX52_MOUSE            Unreviewed;       526 AA.
AC   B1AX52;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-FEB-2011, entry version 26.
DE   SubName: Full=Monoamine oxidase A;
DE   SubName: Full=Monoamine oxidase A, isoform CRA_b;
GN   Name=Maoa; ORFNames=RP23-68J21.1-001, mCG_3052;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Dunn M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RA   Kay M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL805907; CAM18994.1; -; Genomic_DNA.
DR   EMBL; AL831729; CAM18994.1; JOINED; Genomic_DNA.
DR   EMBL; AL831729; CAM26634.1; -; Genomic_DNA.
DR   EMBL; AL805907; CAM26634.1; JOINED; Genomic_DNA.
DR   EMBL; CH466584; EDL35717.1; -; Genomic_DNA.
DR   IPI; IPI00890076; -.
DR   RefSeq; NP_776101.3; NM_173740.3.
DR   UniGene; Mm.21108; -.
DR   ProteinModelPortal; B1AX52; -.
DR   SMR; B1AX52; 11-520.
DR   STRING; B1AX52; -.
DR   Ensembl; ENSMUST00000026013; ENSMUSP00000026013; ENSMUSG00000025037.
DR   GeneID; 17161; -.
DR   KEGG; mmu:17161; -.
DR   CTD; 17161; -.
DR   MGI; MGI:96915; Maoa.
DR   HOVERGEN; HBG004255; -.
DR   InParanoid; B1AX52; -.
DR   OMA; YLFVNIN; -.
DR   PhylomeDB; B1AX52; -.
DR   Bgee; B1AX52; -.
DR   Genevestigator; B1AX52; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0042420; P:dopamine catabolic process; IDA:MGI.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:InterPro.
DR   InterPro; IPR001613; Amineoxid_fl.
DR   InterPro; IPR002937; Amino_oxidase.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   PRINTS; PR00757; AMINEOXDASEF.
PE   4: Predicted;
SQ   SEQUENCE   526 AA;  59602 MW;  5375D1B0C4C5ACF9 CRC64;
     MTDLEKPSIT GHMFDVVVIG GGISGLAAAK LLSEYKINVL VLEARDRVGG RTYTVRNEHV
     KWVDVGGAYV GPTQNRILRL SKELGIETYK VNVNERLVQY VKGKTYPFRG AFPPVWNPLA
     YLDYNNLWRT MDDMGKEIPV DAPWQARHAE EWDKITMKDL IDKICWTKTA REFAYLFVNI
     NVTSEPHEVS ALWFLWYVRQ CGGTSRIFSV TNGGQERKFV GGSGQISEQI MVLLGDKVKL
     SSPVTYIDQT DDNIIIETLN HEHYECKYVI SAIPPVLTAK IHFKPELPPE RNQLIQRLPM
     GAVIKCMVYY KEAFWKKKDY CGCMIIEDEE APISITLDDT KPDGSMPAIM GFILARKAER
     LAKLHKDIRK RKICELYAKV LGSQEALSPV HYEEKNWCEE QYSGGCYTAY FPPGIMTLYG
     RVIRQPVGRI YFAGTETATQ WSGYMEGAVE AGERAAREVL NALGKVAKKD IWVQEPESKD
     VPALEITHTF LERNLPSVPG LLKITGFSTS VALLCFVLYK FKQPQS
//
ID   NHSL2_MOUSE             Reviewed;         854 AA.
AC   B1AXH1;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 20.
DE   RecName: Full=NHS-like protein 2;
GN   Name=Nhsl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 571-771.
RC   STRAIN=C57BL/6J;
RX   PubMed=14691545; DOI=10.1371/journal.pbio.0000074;
RA   Sharov A.A., Piao Y., Matoba R., Dudekula D.B., Qian Y., VanBuren V.,
RA   Falco G., Martin P.R., Stagg C.A., Bassey U.C., Wang Y., Carter M.G.,
RA   Hamatani T., Aiba K., Akutsu H., Sharova L., Tanaka T.S., Kimber W.L.,
RA   Yoshikawa T., Jaradat S.A., Pantano S., Nagaraja R., Boheler K.R.,
RA   Taub D., Hodes R.J., Longo D.L., Schlessinger D., Keller J., Klotz E.,
RA   Kelsoe G., Umezawa A., Vescovi A.L., Rossant J., Kunath T.,
RA   Hogan B.L.M., Curci A., D'Urso M., Kelso J., Hide W., Ko M.S.H.;
RT   "Transcriptome analysis of mouse stem cells and early embryos.";
RL   PLoS Biol. 1:410-419(2003).
CC   -!- SIMILARITY: Belongs to the NHS family.
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DR   EMBL; AL807784; CAM24630.1; -; Genomic_DNA.
DR   EMBL; CN666857; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00944145; -.
DR   UniGene; Mm.232; -.
DR   PhosphoSite; B1AXH1; -.
DR   Ensembl; ENSMUST00000113628; ENSMUSP00000109258; ENSMUSG00000079481.
DR   MGI; MGI:3645090; Nhsl2.
DR   GeneTree; ENSGT00530000063248; -.
DR   HOGENOM; HBG283574; -.
DR   HOVERGEN; HBG095614; -.
DR   InParanoid; B1AXH1; -.
DR   OMA; TTVIECT; -.
DR   OrthoDB; EOG4RV2RQ; -.
DR   Bgee; B1AXH1; -.
DR   Genevestigator; B1AXH1; -.
PE   2: Evidence at transcript level;
FT   CHAIN         1    854       NHS-like protein 2.
FT                                /FTId=PRO_0000341356.
SQ   SEQUENCE   854 AA;  91873 MW;  133330DC6700B46C CRC64;
     MESMAVVYSV PSSCNGPTES TFSTSWKGDA FTYMTPSASS QGNQVSENGK NPSSGNSWVP
     LNTLPPLVPK EAATLFVTRD NPAGCTGLPS YSEHPTLRRQ IPERPPKIGL LARGTSRLET
     GPGGTNRFRE RSLSVPTDSG VTSVDYDEEQ KTSETRILPY ASTSSEGSNS TDNIAALSTE
     QEARHRRQRS KSISLKKAKK KPSPPMRSVS LVKDEPALPP EGELVLPKDQ RPRSLCLSLE
     HQGHHPPHPD AQGHPAVPML KDPGSTQFSH HWYLTDWKSG DTYQSLSSSS TATGTTVIEC
     TQVQGSSESL ASPSTSRATT PSQLSIEVEA REVASPGRPT GLMSPSSGYS SQSETPTPTV
     SMSLTLGHLP PPSASVRVRP VVPERKSSLP PTSPMEKICK SRLSFDLPLT SSTTLDLSGM
     SISIRSKTKV SRHHSDTNFG VKLAQKTSPN QPIMPMVTQS DLRSVRLRSV SKSEPEDDIE
     SPDYIEEPGA EEVFTMPERK VKPPIAEKPP LARRPPSLVH RPPSLPGEYP LTSPTMAMAS
     RSSIPHMKQL PQDSYTVLRK PKSPSFPGES TASSSLVLSP LASSSGAFFS GTQQPPQASV
     EDGGPKVRAL PERIGLQSQE EAEKKMTKIP PPVPKKPSVL YLPLTSPVAQ MDACMAEPRL
     PFSPIITLEE DGKCPSTGDD QKSPGKGVTS PLHTDTEKEA ISPGRSVEPS AEEKSLISDK
     TAEWIAEEED DVFVASRTTE DLFTVIHRSK RKLLGWKETG EGFTGSKPSS HSPVKNTADS
     PTGEAAAAPG PSSSACLDAG RNDDFKALLQ KKGSKATPRT RPSAAELLKT TNPLARRIIA
     QFSKDYEPTD NPST
//
ID   NFX1_MOUSE              Reviewed;        1114 AA.
AC   B1AY10; Q3U2A7; Q3UK95; Q3UMW1; Q7TPT4; Q8CC59; Q9DBC8; Q9JKW7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 32.
DE   RecName: Full=Transcriptional repressor NF-X1;
DE            Short=m-Nfx.1;
DE            EC=6.3.2.-;
DE   AltName: Full=Nuclear transcription factor, X box-binding protein 1;
GN   Name=Nfx1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP   AND DEVELOPMENTAL STAGE.
RX   MEDLINE=22043268; PubMed=12047746;
RX   DOI=10.1046/j.1365-2567.2002.01416.x;
RA   Arlotta P., Miyazaki D., Copeland N.G., Gilbert D.J., Jenkins N.A.,
RA   Ono S.J.;
RT   "Murine NFX.1: isolation and characterization of its messenger RNA,
RT   mapping of its chromosomal location and assessment of its
RT   developmental expression.";
RL   Immunology 106:173-181(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Diencephalon, Liver, Lung, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Binds to the X-box motif of MHC class II genes and
CC       represses their expression. May play an important role in
CC       regulating the duration of an inflammatory response by limiting
CC       the period in which MHC class II molecules are induced by
CC       interferon-gamma. Together with PABPC1 or PABPC4, acts as a
CC       coactivator for TERT expression. Mediates E2-dependent
CC       ubiquitination.
CC   -!- SUBUNIT: Interacts with PABPC1 and PABPC4 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=B1AY10-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=B1AY10-2; Sequence=VSP_033694, VSP_033695;
CC       Name=3;
CC         IsoId=B1AY10-3; Sequence=VSP_033693, VSP_033696;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC       thymus.
CC   -!- DEVELOPMENTAL STAGE: Ubiquitously expressed at E12 and E14.
CC   -!- DOMAIN: The RING-type zinc finger domain interacts with an
CC       ubiquitin-conjugating enzyme (E2) and facilitates ubiquitination
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the NFX1 family.
CC   -!- SIMILARITY: Contains 8 NF-X1-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 R3H domain.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF34700.1; Type=Frameshift; Positions=200, 214, 242, 246;
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DR   EMBL; AF223576; AAF34700.1; ALT_FRAME; mRNA.
DR   EMBL; AK005038; BAB23765.1; -; mRNA.
DR   EMBL; AK033850; BAC28494.1; -; mRNA.
DR   EMBL; AK144647; BAE25987.1; -; mRNA.
DR   EMBL; AK146108; BAE26907.1; -; mRNA.
DR   EMBL; AK155387; BAE33235.1; -; mRNA.
DR   EMBL; AL837521; CAM19845.1; -; Genomic_DNA.
DR   EMBL; AL837521; CAM19846.1; -; Genomic_DNA.
DR   EMBL; AL837521; CAM19847.1; -; Genomic_DNA.
DR   EMBL; BC053709; AAH53709.1; -; mRNA.
DR   IPI; IPI00123537; -.
DR   IPI; IPI00648079; -.
DR   IPI; IPI00648908; -.
DR   RefSeq; NP_076228.2; NM_023739.3.
DR   UniGene; Mm.247456; -.
DR   UniGene; Mm.439181; -.
DR   ProteinModelPortal; B1AY10; -.
DR   SMR; B1AY10; 347-405, 990-1057.
DR   STRING; B1AY10; -.
DR   PRIDE; B1AY10; -.
DR   Ensembl; ENSMUST00000030133; ENSMUSP00000030133; ENSMUSG00000028423.
DR   Ensembl; ENSMUST00000091614; ENSMUSP00000089203; ENSMUSG00000028423.
DR   Ensembl; ENSMUST00000098143; ENSMUSP00000095747; ENSMUSG00000028423.
DR   GeneID; 74164; -.
DR   KEGG; mmu:74164; -.
DR   CTD; 74164; -.
DR   MGI; MGI:1921414; Nfx1.
DR   GeneTree; ENSGT00400000022083; -.
DR   HOVERGEN; HBG003827; -.
DR   InParanoid; B1AY10; -.
DR   OMA; PVIDYFD; -.
DR   OrthoDB; EOG4KSPHZ; -.
DR   NextBio; 339960; -.
DR   Bgee; B1AY10; -.
DR   Genevestigator; B1AY10; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045347; P:negative regulation of MHC class II biosynthetic process; IDA:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   InterPro; IPR001374; R3H_ss-bd.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR000967; Znf_NFX1.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR001841; Znf_RING.
DR   Pfam; PF01424; R3H; 1.
DR   Pfam; PF01422; zf-NF-X1; 4.
DR   SMART; SM00393; R3H; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00438; ZnF_NFX; 9.
DR   PROSITE; PS51061; R3H; 1.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; DNA-binding; Ligase; Metal-binding; Nucleus;
KW   Phosphoprotein; Repeat; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1   1114       Transcriptional repressor NF-X1.
FT                                /FTId=PRO_0000334614.
FT   DOMAIN      988   1056       R3H.
FT   ZN_FING     352    403       RING-type; atypical.
FT   ZN_FING     447    465       NF-X1-type 1.
FT   ZN_FING     500    519       NF-X1-type 2.
FT   ZN_FING     561    580       NF-X1-type 3.
FT   ZN_FING     626    649       NF-X1-type 4.
FT   ZN_FING     688    707       NF-X1-type 5.
FT   ZN_FING     715    734       NF-X1-type 6.
FT   ZN_FING     826    848       NF-X1-type 7.
FT   ZN_FING     857    878       NF-X1-type 8.
FT   REGION        9     26       Interaction with PABPC1 and PABC4 (By
FT                                similarity).
FT   COMPBIAS   1078   1083       Poly-Pro.
FT   MOD_RES      49     49       Phosphoserine (By similarity).
FT   MOD_RES      50     50       Phosphoserine (By similarity).
FT   MOD_RES      89     89       Phosphoserine (By similarity).
FT   MOD_RES    1035   1035       Phosphotyrosine (By similarity).
FT   VAR_SEQ     803    818       LRSNIPCHLVDISCGL -> ELTIKKLWTFKETLDF (in
FT                                isoform 3).
FT                                /FTId=VSP_033693.
FT   VAR_SEQ     803    804       LR -> RQ (in isoform 2).
FT                                /FTId=VSP_033694.
FT   VAR_SEQ     805   1114       Missing (in isoform 2).
FT                                /FTId=VSP_033695.
FT   VAR_SEQ     819   1114       Missing (in isoform 3).
FT                                /FTId=VSP_033696.
FT   CONFLICT     49     49       S -> N (in Ref. 2; BAC28494).
FT   CONFLICT    141    141       T -> A (in Ref. 2; BAE33235).
FT   CONFLICT    273    273       S -> P (in Ref. 4; AAH53709).
FT   CONFLICT    455    455       C -> Y (in Ref. 2; BAE33235).
FT   CONFLICT    590    590       C -> R (in Ref. 4; AAH53709).
SQ   SEQUENCE   1114 AA;  123811 MW;  A31013ACC6FB31F4 CRC64;
     MAEAPPVSGT FKFNTDAAEF IPQERKTSGL NCGTQRRLDS SRIGRRNYSS SPPCHLPRHI
     PYEDISAVHQ HSYASGSKPK SPQGFFQSSN KSLKNHGLQN QPWQKARNEK HQNRNKKAQG
     LSEQTSDTSS LESVARSESG TNPREHSPSE SEKEVVIADP RGAKPKKAAQ LTYNYGRGPK
     AKGRLRSEWG NRMSPKSEDE NTRPVAISHT DSSDASCRKP VVDPCVCRRN EQRRYPQKRP
     PWEVEGARPR PGRNPPKQES QRHINAGPKT NMSPIPKDNL RERPTKSACD TGNLAVVSKS
     SRRVNQEKTA VRRQDPQVLS PFPRGKQNHM LKNVETHTGS LIEQLTTEKY ECMVCCELVQ
     VTAPVWSCQS CFHVFHLNCI KKWARSPASH ADGQSGWRCP ACQNVSAHVP NTYTCFCGKV
     KNPEWSRNEI PHSCGEVCRK KQPGQDCPHS CNLLCHPGPC PPCPAFTTKT CECGRTRHTV
     RCGQPVSVHC SNACENILNC GQHHCAELCH GGQCQPCRII LNQVCYCGST SRDVLCGTDV
     GKSDGFGDFS CLKICGKDLK CGSHTCSQVC HPQPCQPCPR LPHLVRYCPC GQTPLSQLLE
     HGSNARKTCM DPVPSCGKVC GKPLACGSSD FIHTCEKLCH EGDCGPCSRT SVISCRCSFR
     TKELPCTSLK SEDATFMCDK RCNKKRLCGR HKCNEICCVD KEHKCPLICG RKLRCGLHRC
     EEPCHRGNCQ TCWQASFDEL TCHCGASVIY PPVPCGTRPP ECTQTCARIH ECDHPVYHSC
     HSEEKCPPCT FLTQKWCMGK HELRSNIPCH LVDISCGLPC SAMLPCGMHK CQRLCHKGEC
     LVDEACKQPC TTPRGDCGHP CMAPCHPSLP CPVTACKAKV ELQCECGRRK EMVICSEASG
     TYQRIVAISM ASKITDMQLG DSVEISKLIT KKEVQQARLQ CDEECAALER RKRLAEAFDI
     TDDSDPFNVR SSASKFSDSL KDDARKDLKF VSDVEKEMET LVEAVNKGKN NKKSHCFPPM
     NRDHRRIIHD LAQVYGLESI SYDSEPKRNV VVTAVRGKSV CPPTTLTSVI ERETQTRPPP
     PIPHHRHQAD KAPGSSTLQK IVKEAVIDYF DVQD
//
ID   UBP24_MOUSE             Reviewed;        2617 AA.
AC   B1AY13; Q8BLI7;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 28.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 24;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 24;
DE   AltName: Full=Ubiquitin thiolesterase 24;
DE   AltName: Full=Ubiquitin-specific-processing protease 24;
GN   Name=Usp24;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2384-2617 (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2044 AND THR-2556, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
CC   -!- FUNCTION: Involved in the ubiquitin-dependent proteolytic pathway
CC       in conjunction with the 26S proteasome (By similarity).
CC   -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=B1AY13-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=B1AY13-2; Sequence=VSP_035661, VSP_035662;
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC   -!- SIMILARITY: Contains 1 UBA domain.
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DR   EMBL; AK045043; BAC32195.1; -; mRNA.
DR   EMBL; AL954352; CAM15750.1; -; Genomic_DNA.
DR   EMBL; AL840623; CAM15750.1; JOINED; Genomic_DNA.
DR   EMBL; AL840623; CAM19818.1; -; Genomic_DNA.
DR   EMBL; AL954352; CAM19818.1; JOINED; Genomic_DNA.
DR   EMBL; AL840623; CAM19819.1; -; Genomic_DNA.
DR   EMBL; BC029165; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00123410; -.
DR   IPI; IPI00752867; -.
DR   RefSeq; NP_899048.2; NM_183225.2.
DR   UniGene; Mm.234544; -.
DR   ProteinModelPortal; B1AY13; -.
DR   SMR; B1AY13; 2-45, 957-1029, 1679-2041.
DR   PhosphoSite; B1AY13; -.
DR   PRIDE; B1AY13; -.
DR   Ensembl; ENSMUST00000094933; ENSMUSP00000092538; ENSMUSG00000028514.
DR   GeneID; 329908; -.
DR   KEGG; mmu:329908; -.
DR   CTD; 329908; -.
DR   MGI; MGI:1919936; Usp24.
DR   eggNOG; roNOG09231; -.
DR   GeneTree; ENSGT00600000084366; -.
DR   HOGENOM; HBG357761; -.
DR   HOVERGEN; HBG105784; -.
DR   InParanoid; B1AY13; -.
DR   OMA; HMISFLL; -.
DR   OrthoDB; EOG4T782B; -.
DR   PhylomeDB; B1AY13; -.
DR   Bgee; B1AY13; -.
DR   Genevestigator; B1AY13; -.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:EC.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19.
DR   InterPro; IPR009060; UBA-like.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF46934; UBA_like; 1.
DR   PROSITE; PS50030; UBA; 1.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; 1.
DR   PROSITE; PS50235; UCH_2_3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; Phosphoprotein; Protease;
KW   Thiol protease; Ubl conjugation pathway.
FT   CHAIN         1   2617       Ubiquitin carboxyl-terminal hydrolase 24.
FT                                /FTId=PRO_0000353213.
FT   DOMAIN        3     44       UBA.
FT   COMPBIAS     47     91       Gly-rich.
FT   COMPBIAS   1032   1059       Ser-rich.
FT   ACT_SITE   1695   1695       Nucleophile (By similarity).
FT   ACT_SITE   1967   1967       Proton acceptor (By similarity).
FT   MOD_RES    2044   2044       Phosphoserine.
FT   MOD_RES    2074   2074       Phosphoserine (By similarity).
FT   MOD_RES    2556   2556       Phosphothreonine.
FT   MOD_RES    2558   2558       Phosphoserine (By similarity).
FT   MOD_RES    2562   2562       Phosphothreonine (By similarity).
FT   VAR_SEQ     408    418       TKLIEDSTLSK -> SVHLSHMWPLM (in isoform
FT                                2).
FT                                /FTId=VSP_035661.
FT   VAR_SEQ     419   2617       Missing (in isoform 2).
FT                                /FTId=VSP_035662.
SQ   SEQUENCE   2617 AA;  294001 MW;  802DFE22143B2C94 CRC64;
     MESEEEQHMT TLLCMGFSDP ATIRKALRLA KNDINEAVAL LTNERPGLDY GGYEPMDSGG
     PSPGPGGGPR GDSGSDGSGP SRGGSTGGGG GFDPPPAYHE VVDAEKNDEN GNCSGEGIEF
     PTTNLYELES RVLTDHWSIP YKREESLGKC LLASTYLARL GLSESDENCK RFMERCMPEA
     FKKLLTSSAV HKWGTEIHEG IYNMLMLLIE LVAERMKQDP IPIGLLGVLT MAFNPDNEYH
     FKNRMKVSQR NWAEVFGEGN MFAISPVSTF QKEPHGWVVD LVNKFGELGG FAAIQAKLHS
     EDIELGAVSA LVQPLGVCAE YLNSSVVQPM LDPVILTTIQ DVRSVEEKDL KDKRLVSIPE
     LLSAIKLLCM RFQPALVTTV DALRLDILLR MLKSPHFSAK MNSLKEVTKL IEDSTLSKSV
     KNAIDTDRLL DWLVENSVLS IALEGNIDQA QYCDRIKGII ELLGSKLSLD ELTKIWKIQS
     GQSSTVIENI HTIIAAAAVK FNADQLNHLF VLIQKSWETE SDRVRQKLLS LIGRIGREAR
     FEATSGKVLD VLWELAHLPT LPSSLIQQAL EEHLTILSDA YAVKEAVKRS YIIKCIEDIK
     RPGEWSSLEK NKKDGFKSSQ LNNPQFVWVV PALRQLHEIT RSFIKQTYQK QDKSIIQDLK
     KNFEIVKLVT GSLLACHRLA AAVAGPGGLT GLTLVDGRYT YREYLEAHLK FLAFFLQEAT
     LYLGWNRAKE IWECLVTGQD VCELDREMCF EWFTKGQHDL ESDVQQQLFK EKILKLESYE
     ITMNGFNLFK TFFENVNLCD HRLKRQGAQL YVEKLELVGM DFIWKIAMES PDEEIANEAI
     QLIINYSYIN LNPRLKKDSV SLHKKFIADC YTRLEAASSA LGGPTLTHAV TRATKMLTAT
     AMPTVATSVQ SPYRSTKLVI IERLLLLAER YVITIEDFYS VPRTILPHGA SFHGHLLTLN
     VTYESTKDTF TVEAHSNETI GSVRWKIAKQ LCSPVDNIQI FTNDSLLTVN KDQKLLHQLG
     FSDEQVLTVK TSGSGTPSGS SADSSTSSSS SSSGAFSSSY AMEQEKSLPG VVMALVCNVF
     DMLYQLANLE EPRITLRVRK LLLLIPTDPA IQEALDQLDS LGRKKTLLSE TSSQSSKSPS
     LSSKQQHQPS ASSILESLFR SFAPGMSTFR VLYNLEVLSS KLMPTADDDM ARSCAKSFCE
     NFLKAGGLSL VVNVMQRDSI PSEVDYETRQ GVYSICLQLA RFLLVGQTMP TSLDEDLTKD
     GIEALSSRPF RNVSRQTSRQ MSLCGTPEKS SYRQLSVSDR SSIRVEEIIP AARVAIQTME
     ASDFTATVAC FMRLSWAAAA GRLDLVGSSQ PIKESNSLFP AGIRSRLSSS GSNCSSSSEG
     EPAALHAGIC VRQQSVSTKD ALIAGEALSL LVTCLQLRSQ QLASFYSLPC VADFIIDILL
     GSPSAEIRRV ACDQLYTLSQ TDTSAHPEVQ KPNQFLLGVI LTAQLPLWSP TSIMRGVNQR
     LLSQCMEYFD LRCQLLDDLT TSEMDQLRIS PATMLEDEIT WLDNFEPNRT ADCETSEADN
     ILLAGHLRLI KTLLSLCGAE KEMLGSSLIK PLLDDFLFRA SRIIVNSHSP ASSAAISQQD
     FHPKCSTVNS RLAAYEVLVM LADSSPSNLQ IITKELLSMH HQPDPALTKE FDYLPPVDSR
     SSSGFVGLRN GGATCYMNAV FQQLYMQPGL PESLLSVDDD TDNPDDSVFY QVQSLFGHLM
     ESKLQYYVPE NFWKIFKMWN KELYVREQQD AYEFFTSLID QMDEYLKKMG REQIFKNTFQ
     GIYSDQKICK DCPHRYEREE AFMALNLGVT SCQSLEISLD QFVRGEVLEG SNAYYCEKCK
     EKRITVKRTC IKSLPSVLVI HLMRFGFDWE SGRSIKYDEQ IRFPWMLNME PYTVAGMARQ
     DSSSEVGENG RNMDQGGGGS PRKKVALTEN YELVGVIVHS GQAHAGHYYS FIKDRRGCGK
     GKWYKFNDTV IEEFDLNDET LEYECFGGEY RPKVYDQTNP YTDVRRRYWN AYMLFYQRVS
     DQNSPVLPKK SRVSVVRQEA EDLSLSAPSS PEISPQSSPR PHRPNNDRLS ILTKLVKKGE
     KKGLFVEKMP ARIYQMVRDE NLKFMKNRDV YSSDYFSFVL SLASLNATKL KHPYYPCMAK
     VSLQLAIQFL FQTYLRTKKK LRVDTEEWIA TIEALLSKSL DACQWLVEYF ISSEGRELVK
     VFLLECSVRE VRVAVATILE KTLDSALFYQ DKLKSLHQLL EVLLALLDKD VPENCKNCAQ
     YFSLFNTFVQ KQGIRAGDLL LRHSALRHMI SFLLGVSRQN SQIRRWSSAQ AREFGNLHNT
     VALLVLHSDV SSQRNVAPGI FKQRPPISVA PSSPLLPLHE EVEALLFLSE GKPYLLEVMF
     ALRELTGSLL ALMEMVVYCC FCNEHFSFTM LHFIKNQLET APPHELKNTF QLLHEVLVIE
     DPIQVERVKF VFETENGLLA LMHHSNHVDS SRCYQCVKFL VTLAQKCPAA KEYFKENSHH
     WSWAVQWLQK KMSEHYWTPQ SNVSNETSTG KTFQRTISAQ DTLAYATALL NEKEQSGSSN
     GSESSPANEN GERHLQQGSE SPMMIGELRS DLDDVDP
//
ID   B1AYL1_MOUSE            Unreviewed;      1681 AA.
AC   B1AYL1;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 27.
DE   SubName: Full=Sodium channel voltage-gated type VII alpha;
GN   Name=Scn7a; ORFNames=RP23-276I21.3-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Tracey A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Tromans A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the sodium channel family.
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DR   EMBL; AL928623; CAM19366.1; -; Genomic_DNA.
DR   EMBL; AL928720; CAM19366.1; JOINED; Genomic_DNA.
DR   EMBL; AL928720; CAM27067.1; -; Genomic_DNA.
DR   EMBL; AL928623; CAM27067.1; JOINED; Genomic_DNA.
DR   IPI; IPI00341285; -.
DR   RefSeq; NP_033161.2; NM_009135.2.
DR   UniGene; Mm.38127; -.
DR   STRING; B1AYL1; -.
DR   PRIDE; B1AYL1; -.
DR   Ensembl; ENSMUST00000042792; ENSMUSP00000042405; ENSMUSG00000034810.
DR   GeneID; 20272; -.
DR   KEGG; mmu:20272; -.
DR   CTD; 20272; -.
DR   MGI; MGI:102965; Scn7a.
DR   HOGENOM; HBG358468; -.
DR   HOVERGEN; HBG053100; -.
DR   InParanoid; B1AYL1; -.
DR   OMA; TQVRGDC; -.
DR   OrthoDB; EOG4GF3D9; -.
DR   NextBio; 297951; -.
DR   Bgee; B1AYL1; -.
DR   Genevestigator; B1AYL1; -.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:InterPro.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; IEA:InterPro.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001696; Na_channel_asu.
DR   InterPro; IPR010526; Na_trans_assoc.
DR   Pfam; PF00520; Ion_trans; 4.
DR   Pfam; PF06512; Na_trans_assoc; 1.
DR   PRINTS; PR00170; NACHANNEL.
DR   SMART; SM00015; IQ; 1.
PE   3: Inferred from homology;
KW   Ion transport; Ionic channel; Membrane; Sodium; Sodium channel;
KW   Sodium transport; Transmembrane; Transport; Voltage-gated channel.
SQ   SEQUENCE   1681 AA;  192177 MW;  BD0E0A17FAFBC39C CRC64;
     MLTSPEPKGL VPFTTESLEL IENHIAKKCN EDPEEEEGLK PSRNLEAGKR LPIPYGTLPR
     GTVSEPLEDV DPYYYVKRNT FMVLNRSRVI FRFNAVSIFC TLSPLNSLRR AAIKALVHPL
     FRLLILISVL TDSILMCMSN LPEWILAIEN TLLGIYAFEI LVKVIARGIW AGSFSFLGDL
     WNWLDFSVTL FELITRFSPL SSFLMLKTIR TFRILKIIPL NHGLQSIVMT LAQCLKKLFG
     AIALALFFLA VFSLLGMGLF MGNLKHKCLR WPEENENETL HNRTGSLNYS PERINFYYME
     GAKYALLCGN RTDAGQCPEG YVCVKEGTNP DNGFTSFDNF GWSLLAMFRL MTQDYPELLY
     HQILYASGKV YMIFFVMISF WFAFYLTSLF LGILTMTYEK EKQRACEESG GLDPKCQQTV
     KELDEENDAA EMETTQIEMK KRSPTSINTT LDILEDTTLG HREEPETSRK KCPICWHKFI
     KTCFIWKCSP CWVKLNEFAD RVITHPLADL FLVICIVLNI CFLALEHFPM SEELRSLLHV
     GNLVFIGIYT IEMILKIIAM HPYGYFQISW NIFDSILVVL ELTEILLADV EGLAVLITVP
     LIFIKLGKYG PPFKSLMRIL GSSLMALKDL VLLLCIFVYF SAVFGMKLFG RSYKDCVCHI
     KEDCQPQRWH MSDFLHAYMT VFRILCGEWI ETLWECMEVA GQAWCIPFYM MVILIGNLLI
     LYLFVTLVSS FSYYDATSEV NKEAKNLQLA MARIKSGINS MLLKLMCTER SVPTEATDQI
     CDPSVKENIS GHTLSELSNT QTFLRYKDQS SSTEKTPVTE SESQSLIASP SASETVPIAS
     GESDIENLDN KETRSKSGNG GSKEKMKQSS SSECSTVDIA ISEEEEMVYE HEKSKLHKNG
     YERKSSTGQI SRESRNGKIW KNIRKTCCKI VENSWFECFI GLVTLLCTGT LALEDIYIDQ
     RKTTKILLEY ADMIFAYIFI LEMLLKWVAY GFKAFFSNNW YKLDFMVVIV FCLSLIGKTR
     EDLNPLTSIK FLRALRVLSQ FERMKVVLRA LIKTTLPTVS VFLVCLMIWL LFSVIGVQLF
     AGKFYECIDP TKGERFPVFE VMNKSQCEKL LFNESMPWEN AKLNFDNVGN GFLSLLQVAT
     FNGWISIMNS AIDSVGVNMQ PSFEYNLYMY SYFIIFVIFG LFLPLCMLIG VIIRNFNKQK
     IKQGGSNIFI TVKQKKQYRA LKKLLYADVQ KPTPRPRNKF QGFLFDLVTH RVFNVIIILL
     ICFQATTIMI QKDEQSPQME TAIFWMNSIF VMLFTLECIL KLTAFRCHYF TSAWNVHDFM
     VVIFSITGLL LPLTIGQYFV PPSLVQLILL SRVIHILRPG KGPKVFHDLM LPLILALPAL
     LNISLLIFLV MFIYAIFGMY NFAYVKKEAG INDVSNFETF GSSMLCLFQV TTFSGWDGML
     DAIFNSQWSD CDPDKINPGT QVKGDCGSPS VGISYFVSYI LISWLIIVNM YIVLIMEFLS
     IPSQKKSRTL SEDDFRRFFR VWNRFDPDRT QYIDSSKLSD FAAALDPPLF MAKPNKGQLV
     AMDLPMAAGD RIHCLDILLA FTKRVMGKDE RVEKILSEIE SGFMLANPFK ITYEPITTTL
     KRKQEAVSAT IIQRAYKSYR LRQNDKNVSD TPAIDDRRDD LTSKGAHSGK IEEKASIQTQ
     I
//
ID   B1AYU6_MOUSE            Unreviewed;       902 AA.
AC   B1AYU6;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 22.
DE   SubName: Full=Novel protein;
DE   SubName: Full=cDNA sequence BC003993, isoform CRA_c;
GN   Name=Cwc22; Synonyms=BC003993, RP23-65N20.1;
GN   ORFNames=RP23-65N20.1-005, mCG_12441;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Humphries M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RA   Whitehead S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL928915; CAM19371.1; -; Genomic_DNA.
DR   EMBL; AL928791; CAM19371.1; JOINED; Genomic_DNA.
DR   EMBL; AL928791; CAX15801.1; -; Genomic_DNA.
DR   EMBL; AL928915; CAX15801.1; JOINED; Genomic_DNA.
DR   EMBL; CH466519; EDL27235.1; -; Genomic_DNA.
DR   EMBL; CH466519; EDL27236.1; -; Genomic_DNA.
DR   IPI; IPI00757147; -.
DR   UniGene; Mm.288151; -.
DR   UniGene; Mm.314749; -.
DR   ProteinModelPortal; B1AYU6; -.
DR   STRING; B1AYU6; -.
DR   PRIDE; B1AYU6; -.
DR   Ensembl; ENSMUST00000111818; ENSMUSP00000107449; ENSMUSG00000027014.
DR   MGI; MGI:2136773; Cwc22.
DR   HOVERGEN; HBG054017; -.
DR   PhylomeDB; B1AYU6; -.
DR   Bgee; B1AYU6; -.
DR   Genevestigator; B1AYU6; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0016070; P:RNA metabolic process; IEA:InterPro.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR   InterPro; IPR016021; MIF4-like_typ_1/2/3.
DR   InterPro; IPR003890; MIF4G-like_typ-3.
DR   Gene3D; G3DSA:1.25.40.180; MIF4-like_typ_1/2/3; 1.
DR   Pfam; PF02847; MA3; 1.
DR   Pfam; PF02854; MIF4G; 1.
DR   SMART; SM00544; MA3; 1.
DR   SMART; SM00543; MIF4G; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS51366; MI; 1.
PE   4: Predicted;
SQ   SEQUENCE   902 AA;  104207 MW;  C2A305B558376B90 CRC64;
     MKSSVAHMKS SGHNRRETHS SYRRSSSPED RYTEQERSPR DRGYSDYSRS DYERSRRGYS
     YDDSMESRSR DREKRRERER DADHRKRSRK SPSPDRSPAR GGGQSSPQEE PTWKKKKDEL
     DPLLTRTGGA YIPPAKLRMM QEQITDKSSL AYQRMSWEAL KKSINGLINK VNISNISIII
     QELLQENIVR GRGLLSRSVL QAQSASPIFT HVYAALVAII NSKFPQIGEL ILKRLILNFR
     KGYRRNDKQL CLTASKFVAH LINQNVAHEV LCLEMLTLLL ERPTDDSVEV AIGFLKECGL
     KLTQVSPRGI NAIFERLRNI LHESEIDKRV QYMIEVMFAV RKDGFKDHPV ILEGLDLVEE
     DDQFTHMLPL EDDYNPEDVL NVFKMDPNFM ENEEKYKAIK KEILDEGDSD SNTDQGAGSS
     EDEEEEDEEE EGEDEEGGQK VTIHDKTEIN LVSFRRTIYL AIQSSLDFEE CAHKLLKMEF
     AESQTKELCN MILDCCAQQR TYEKFFGLLA GRFCMLKKEY MESFESIFKE QYDTIHRLET
     NKLRNVAKMF AHLLYTDSLP WSVLECIKLS EETTTSSSRI FVKIFFQELC EYMGLPKLNA
     RLKDETLQPF FEGLLPRDNP RNTRFAINFF TSIGLGGLTD ELREHLKNTP KVIVAQKPEA
     EQKKPALTSS SSESSSASDS SDSESDSSES SSESSSDASD SSSSSSTQSS TSAKGTRKKR
     QGKARGEEVD KLARGHQALE RRREGGREDQ RHQEGRTERA RSERRRAQNS RDADWRDPLA
     KHIDDRSHEN SHSRVGNGRE QGSHREPEDR HGEPKKRRER RDSFSENEKQ RSRNQDSDNV
     RRKDRSKSRE RSRRHSGHKG DDARCQNSAE RRWEKPGRRP EQSRESKRSQ DRRREKSPTT
     QK
//
ID   B1AZA5_MOUSE            Unreviewed;       876 AA.
AC   B1AZA5;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 19.
DE   SubName: Full=Likely ortholog of H. sapiens chromosome 9 open reading frame 5 (C9orf5);
GN   Name=D730040F13Rik; Synonyms=RP23-455B1.3; ORFNames=RP23-455B1.3-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Howden P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RA   Phillimore B.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL929577; CAM24765.1; -; Genomic_DNA.
DR   EMBL; BX470220; CAM24765.1; JOINED; Genomic_DNA.
DR   EMBL; BX470220; CAM27763.1; -; Genomic_DNA.
DR   EMBL; AL929577; CAM27763.1; JOINED; Genomic_DNA.
DR   IPI; IPI00876161; -.
DR   PhosphoSite; B1AZA5; -.
DR   Ensembl; ENSMUST00000068792; ENSMUSP00000067421; ENSMUSG00000055296.
DR   MGI; MGI:2445107; D730040F13Rik.
DR   eggNOG; roNOG10506; -.
DR   GeneTree; ENSGT00390000001667; -.
DR   HOVERGEN; HBG080525; -.
DR   OrthoDB; EOG4V6ZG5; -.
DR   Bgee; B1AZA5; -.
DR   Genevestigator; B1AZA5; -.
DR   InterPro; IPR002549; UPF0118.
DR   PANTHER; PTHR21716; UPF0118; 1.
DR   Pfam; PF01594; UPF0118; 1.
PE   1: Evidence at protein level;
SQ   SEQUENCE   876 AA;  97357 MW;  9CDC1AC21F01A7D6 CRC64;
     MADRGGPAEA PSPRGSPRPE SRAPRTVGPG ETPRTAALAL RFDKPIKQAF YNTGAVLFVC
     LCCGAAVLVY FILEAFLRPL LWAVLCGTFL HPFKSSLTRL GRLWLRRLHR AHTPIVLAAL
     LLPLCFADYG VEALGEQALR RRRLLLLLGA GGPLLYGLYC LGSYLGVQVL LAHAGALICR
     GLDYFSSLWI WTLVVGYVLM VSFKWNASTQ RYLRAVSIPV WMILLFHIAS LAGSWRIPVF
     LVIVFLMSVG TLYEKQNEKE SAGAELPGQV ISMAASTLAN LAISITGYES STEDQPSDPP
     TEPTDKGEPP PALSASSSSS SRSSPSSPSP TLGRQRPEMG TFLRKKKTSD IYFVSLVWAI
     IAVQLWLNLW IVQLLPVPVA VWIIKKLVIH FGVVGFLEKR CHAWWQVIEC FLKERQEALA
     PWPIIGLGKF LLKVDSKLWH WLNKKMIIWL EKMLDKIISI FIIFLLVIGT LLLALLLTAK
     VHQESVHMIE VTSSLINETL ANHPEWANWL PEAQVVQRAL NSAANNVYQY GREWITHKLH
     KILGDKVNNT AVIEKQVLEL WDRLYHSWFV KNVTHSGRHK GHKMHVSRQN SWLGDILDWQ
     DIASFVHENI ETFLSILESL WIVMSRNVSL LFTTVTTLLT ILFYSGTALL NFVLSLIIFL
     TTLFYLLSSS DEYYKPVKWV ISLTPLSQPG PSSNIIGQSV EEAIRGVFDA SLKMAGFYGL
     YTWLTHTIFG INIVFIPSAL AAILGAVPFL GTYWAAVPAV LDLWLTQGLG CKAILLLVFH
     LLPTYFVDTA IYSDISGGGH PYLTGLAVAG GAYYLGLEGA IIGPILLCIL VVASNIYSAM
     LVSPTNSMPT PNQTPWPAQT QRTFRDISED LKSSVD
//
ID   THOC2_MOUSE             Reviewed;        1594 AA.
AC   B1AZI6;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 26.
DE   RecName: Full=THO complex subunit 2;
DE            Short=Tho2;
GN   Name=Thoc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- FUNCTION: Component of the THO subcomplex of the TREX complex. The
CC       TREX complex specifically associates with spliced mRNA and not
CC       with unspliced pre-mRNA. It is recruited to spliced mRNAs by a
CC       transcription-independent mechanism. Binds to mRNA upstream of the
CC       exon-junction complex (EJC) and is recruited in a splicing- and
CC       cap-dependent manner to a region near the 5' end of the mRNA where
CC       it functions in mRNA export. The recruitment occurs via an
CC       interaction between THOC4 and the cap-binding protein NCBP1. UAP56
CC       functions as a bridge between THOC4 and the THO complex (By
CC       similarity).
CC   -!- SUBUNIT: Component of the THO complex, which is composed of THOC1,
CC       THOC2, THOC5, THOC6 and THOC7. Together with THOC3, THOC4 and
CC       UAP56, THO forms the transcription/export (TREX) complex.
CC       Interacts with THOC1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- SIMILARITY: Belongs to the THOC2 family.
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DR   EMBL; BX005253; CAM20174.1; -; Genomic_DNA.
DR   EMBL; AL954355; CAM20174.1; JOINED; Genomic_DNA.
DR   EMBL; AL954355; CAM27369.1; -; Genomic_DNA.
DR   EMBL; BX005253; CAM27369.1; JOINED; Genomic_DNA.
DR   IPI; IPI00664886; -.
DR   RefSeq; NP_001028594.1; NM_001033422.1.
DR   UniGene; Mm.259498; -.
DR   STRING; B1AZI6; -.
DR   PRIDE; B1AZI6; -.
DR   Ensembl; ENSMUST00000047037; ENSMUSP00000044677; ENSMUSG00000037475.
DR   GeneID; 331401; -.
DR   KEGG; mmu:331401; -.
DR   CTD; 331401; -.
DR   MGI; MGI:2442413; Thoc2.
DR   HOGENOM; HBG315902; -.
DR   InParanoid; B1AZI6; -.
DR   OMA; HAQSIMD; -.
DR   OrthoDB; EOG42BX7P; -.
DR   NextBio; 399751; -.
DR   Bgee; B1AZI6; -.
DR   Genevestigator; B1AZI6; -.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR021418; THO_THOC2_C.
DR   InterPro; IPR021726; THO_THOC2_N.
DR   Pfam; PF11262; Tho2; 1.
DR   Pfam; PF11732; Thoc2; 1.
PE   3: Inferred from homology;
KW   Coiled coil; mRNA processing; mRNA splicing; mRNA transport; Nucleus;
KW   Phosphoprotein; RNA-binding; Transport.
FT   CHAIN         1   1594       THO complex subunit 2.
FT                                /FTId=PRO_0000384399.
FT   COILED      896    965       Potential.
FT   COILED     1464   1491       Potential.
FT   MOTIF       923    928       Nuclear localization signal (Potential).
FT   MOD_RES    1222   1222       Phosphoserine (By similarity).
FT   MOD_RES    1289   1289       Phosphothreonine (By similarity).
FT   MOD_RES    1364   1364       Phosphoserine (By similarity).
FT   MOD_RES    1385   1385       Phosphothreonine (By similarity).
FT   MOD_RES    1390   1390       Phosphoserine (By similarity).
FT   MOD_RES    1393   1393       Phosphoserine (By similarity).
FT   MOD_RES    1417   1417       Phosphoserine (By similarity).
FT   MOD_RES    1448   1448       Phosphoserine (By similarity).
FT   MOD_RES    1486   1486       Phosphoserine (By similarity).
FT   MOD_RES    1516   1516       Phosphoserine (By similarity).
FT   MOD_RES    1520   1520       Phosphoserine (By similarity).
SQ   SEQUENCE   1594 AA;  182773 MW;  9732F53F9C506CC8 CRC64;
     MAAAAVVVPA EWIKNWEKSG RGEFLHLCRI LSENKSHDSS TYRDFQQALY ELSYHVIKGN
     LKHEQASSVL NDISEFREDM PSILADVFCI LDIETNCLEE KSKRDYFTQL VLACLYLVSD
     TVLKERLDPE TLESLGLIKQ SQQFNQKSVK IKTKLFYKQQ KFNLLREENE GYAKLIAELG
     QDLSGNITSD LILENIKSLI GCFNLDPNRV LDVILEVFEC RPEHDDFFIS LLESYMSMCE
     PQTLCHILGF KFKFYQEPSG ETPSSLYRVA AVLLQFNLID LDDLYVHLLP ADNCIMDEYK
     REIVEAKQIV RKLTMVVLSS EKLDERDKEK DKDDEKVEKP PDNQKLGLLE ALLKVGDWQH
     AQNIMDQMPP YYAASHKLIA LAICKLIHIT VEPLYRRVGV PKGAKGSPVS ALQNKRAPKQ
     VESFEDLRRD VFNMFCYLGP HLSHDPILFA KVVRIGKSFM KEFQSDGSKQ EDKEKTEVIL
     SCLLSITDQV LLPSLSLMDC NACMSEELWG MFKTFPYQHR YRLYGQWKNE TYNGHPLLVK
     VKAQTIDRAK YIMKRLTKEN VKPSGRQIGK LSHSNPTILF DYILSQIQKY DNLITPVVDS
     LKYLTSLNYD VLAYCIIEAL ANPEKERMKH DDTTISSWLQ SLASFCGAVF RKYPIDLAGL
     LQYVANQLKA GKSFDLLILK EVVQKMAGIE ITEEMTMEQL EAMTGGEQLK AEGGYFGQIR
     NTKKSSQRLK DALLDHDLAL PLCLLMAQQR NGVIFQEGGE KHLKLVGKLY DQCHDTLVQF
     GGFLASNLST EDYIKRVPSI DVLCNEFHTP HDAAFFLSRP MYAHHISSKY DELKKSEKGS
     KQQHKVHKYI TSCEMVMAPV HEAVVSLHVS KVWDDISPQF YATFWSLTMY DLAVPHTSYE
     REVNKLKVQM KAIDDNQEMP PNKKKKEKER CTALQDKLLE EEKKQMEHVQ RVLQRLKLEK
     DNWLLAKSTK NETITKFLQL CIFPRCIFSA IDAVYCARFV ELVHQQKTPN FSTLLCYDRV
     FSDIIYTVAS CTENEASRYG RFLCCMLETV TRWHSDRATY EKECGNYPGF LTILRATGFD
     GGNKADQLDY ENFRHVVHKW HYKLTKASVH CLETGEYTHI RNILIVLTKI LPWYPKVLNL
     GQALERRVNK ICQEEKEKRP DLYALAMGYS GQLKSRKSHM IPENEFHHKD PPPRNAVASV
     QNGPGGGTSS SSIGNASKSD ESGAEETDKS RERSQCGTKA VNKASSTTPK GNSSNGNSGS
     NSNKAVKEND KEKVKEKEKE KKEKTPATTP EARALGKDSK EKPKEERPNK EDKARETKER
     TPKSDKEKEK FKKEEKAKDE KFKTTVPIVE SKSTQERERE KEPSRERDVA KEMKSKENVK
     GGEKTPVSGS LKSPVPRSDI SEPDREQKRR KIDSHPSPSH SSTVKDSLID LKDSSAKLYI
     NHNPPPLSKS KEREMDKKDL DKSRERSRER EKKDEKDRKE RKRDHSNNDR EVPPDITKRR
     KEENGTMGVS KHKSESPCES QYPNEKDKEK NKSKSSGKEK SSSDSFKSEK MDKISSGGKK
     ESRHDKEKIE KKEKRDSSGG KEEKKHHKSS DKHR
//
ID   DLGP4_MOUSE             Reviewed;         992 AA.
AC   B1AZP2; B1AZP3; B7ZNS1; Q3KQQ8; Q6PD44; Q6XBF1; Q80TN3; Q8R3U9;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 30.
DE   RecName: Full=Disks large-associated protein 4;
DE            Short=DAP-4;
DE   AltName: Full=PSD-95/SAP90-binding protein 4;
DE   AltName: Full=SAP90/PSD-95-associated protein 4;
DE            Short=SAPAP-4;
GN   Name=Dlgap4; Synonyms=Kiaa0964, Sapap4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=ICR;
RX   PubMed=15024750; DOI=10.1002/cne.20060;
RA   Welch J.M., Wang D., Feng G.;
RT   "Differential mRNA expression and protein localization of the
RT   SAP90/PSD-95-associated proteins (SAPAPs) in the nervous system of the
RT   mouse.";
RL   J. Comp. Neurol. 472:24-39(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6, FVB/N, and FVB/N-3; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-973, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-377; SER-397
RP   AND SER-512, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND THR-915, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May play a role in the molecular organization of
CC       synapses and neuronal cell signaling. Could be an adapter protein
CC       linking ion channel to the subsynaptic cytoskeleton. May induce
CC       enrichment of PSD-95/SAP90 at the plasma membrane (By similarity).
CC   -!- SUBUNIT: Interacts with DLG1 and DLG4/PSD-95 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=B1AZP2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=B1AZP2-2; Sequence=VSP_034909;
CC       Name=3;
CC         IsoId=B1AZP2-3; Sequence=VSP_034907, VSP_034908;
CC   -!- SIMILARITY: Belongs to the SAPAP family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65690.2; Type=Miscellaneous discrepancy; Note=Intron retention;
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DR   EMBL; AK122408; BAC65690.2; ALT_SEQ; Transcribed_RNA.
DR   EMBL; AY243849; AAO89220.2; -; mRNA.
DR   EMBL; BX004793; CAM16917.1; -; Genomic_DNA.
DR   EMBL; BX571766; CAM16917.1; JOINED; Genomic_DNA.
DR   EMBL; BX571766; CAM22345.1; -; Genomic_DNA.
DR   EMBL; BX004793; CAM22345.1; JOINED; Genomic_DNA.
DR   EMBL; BX004793; CAM16918.1; -; Genomic_DNA.
DR   EMBL; BX571766; CAM16918.1; JOINED; Genomic_DNA.
DR   EMBL; BX571766; CAM22346.1; -; Genomic_DNA.
DR   EMBL; BX004793; CAM22346.1; JOINED; Genomic_DNA.
DR   EMBL; BX004793; CAM16919.1; -; Genomic_DNA.
DR   EMBL; BX571766; CAM16919.1; JOINED; Genomic_DNA.
DR   EMBL; BX571766; CAM22347.1; -; Genomic_DNA.
DR   EMBL; BX004793; CAM22347.1; JOINED; Genomic_DNA.
DR   EMBL; BC024558; AAH24558.1; -; mRNA.
DR   EMBL; BC058948; AAH58948.1; -; mRNA.
DR   EMBL; BC085475; AAH85475.1; -; mRNA.
DR   EMBL; BC106094; AAI06095.1; -; mRNA.
DR   EMBL; BC141110; AAI41111.1; -; mRNA.
DR   EMBL; BC145394; AAI45395.1; -; mRNA.
DR   IPI; IPI00330186; -.
DR   IPI; IPI00377469; -.
DR   IPI; IPI00752220; -.
DR   RefSeq; NP_001035952.1; NM_001042487.1.
DR   RefSeq; NP_001035953.1; NM_001042488.1.
DR   RefSeq; NP_666240.4; NM_146128.5.
DR   UniGene; Mm.22094; -.
DR   ProteinModelPortal; B1AZP2; -.
DR   STRING; B1AZP2; -.
DR   PhosphoSite; B1AZP2; -.
DR   PRIDE; B1AZP2; -.
DR   Ensembl; ENSMUST00000000094; ENSMUSP00000000094; ENSMUSG00000061689.
DR   Ensembl; ENSMUST00000099145; ENSMUSP00000096749; ENSMUSG00000061689.
DR   Ensembl; ENSMUST00000109567; ENSMUSP00000105195; ENSMUSG00000061689.
DR   Ensembl; ENSMUST00000109568; ENSMUSP00000105196; ENSMUSG00000061689.
DR   GeneID; 228836; -.
DR   KEGG; mmu:228836; -.
DR   CTD; 228836; -.
DR   MGI; MGI:2138865; Dlgap4.
DR   GeneTree; ENSGT00550000074473; -.
DR   HOVERGEN; HBG018957; -.
DR   InParanoid; B1AZP2; -.
DR   OMA; EGPIPCR; -.
DR   OrthoDB; EOG4ZCT3Z; -.
DR   PhylomeDB; B1AZP2; -.
DR   NextBio; 379186; -.
DR   Bgee; B1AZP2; -.
DR   Genevestigator; B1AZP2; -.
DR   GO; GO:0007267; P:cell-cell signaling; IEA:InterPro.
DR   InterPro; IPR005026; GKAP.
DR   Pfam; PF03359; GKAP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Membrane; Phosphoprotein.
FT   CHAIN         1    992       Disks large-associated protein 4.
FT                                /FTId=PRO_0000345018.
FT   MOD_RES     367    367       Phosphoserine.
FT   MOD_RES     368    368       Phosphotyrosine (By similarity).
FT   MOD_RES     377    377       Phosphoserine.
FT   MOD_RES     397    397       Phosphoserine.
FT   MOD_RES     421    421       Phosphoserine.
FT   MOD_RES     512    512       Phosphoserine.
FT   MOD_RES     665    665       Phosphoserine.
FT   MOD_RES     915    915       Phosphothreonine.
FT   MOD_RES     973    973       Phosphoserine.
FT   MOD_RES     984    984       Phosphotyrosine (By similarity).
FT   VAR_SEQ       1    539       Missing (in isoform 3).
FT                                /FTId=VSP_034907.
FT   VAR_SEQ     540    550       GSLSNSRTLPS -> MALCLELLKQC (in isoform
FT                                3).
FT                                /FTId=VSP_034908.
FT   VAR_SEQ     671    700       VDCIQPVPKEEPSPATKFQSIGIQVEDDWR -> ERTRRSG
FT                                SHLSEDNGPKAIDVMAPSSE (in isoform 2).
FT                                /FTId=VSP_034909.
FT   CONFLICT    614    614       S -> N (in Ref. 4; AAH24558).
FT   CONFLICT    676    676       Missing (in Ref. 1; AAO89220).
FT   CONFLICT    689    689       Q -> E (in Ref. 1; AAO89220).
FT   CONFLICT    693    693       I -> V (in Ref. 1; AAO89220 and 4;
FT                                AAH24558/AAI06095).
FT   CONFLICT    774    774       A -> V (in Ref. 4; AAH24558).
SQ   SEQUENCE   992 AA;  108037 MW;  A33016920922ABB9 CRC64;
     MKGLGDSRPR HLSDSLDPPH EPLFAGPDRN PYLLSPTEAF AREARFPGQN TLPGDGLFPL
     NNQLPPPSST FPRIHYNSHF EVPEESPFPS HAQATKINRL PANLLDQFEK QLPIHRDGFS
     TLQFPRGEAK ARGESPGRIR HLVHSVQRLF FTKAPSMEGT AGKVGGNGSK KGGLEDGKGR
     RAKSKERAKA GEPKRRSRSN ISGWWSSDDN LDGEGGAFRS GPASGLMTLG RQQERTQPRY
     FMHAYNTISG HMLKTTKNTT TELTAPPPPP APPATCPSLG VGTDTNYVKR GSWSTLTLSH
     AHEVCQKTSA TLDKSLLKSK SCHQGLAYHY LQVPGGGGEW STTLLSPRDM DSTAEGPIPC
     RRMRSGSYIK AMGDEDSDES GGGSPKPSPK TAARRQSYLR ATQQSLGEQS NPRRSLDRLD
     SVDMLLPSKC PSWEDDYNPI SDSLNDSSCI SQVFGQASLI PQLFGHDQQV READLSDQYE
     AACESACSEA ESTTAEALDL PLPSYFRSRS HSYLRAIQAG CSQEEDSVSL QSLSPPPSTG
     SLSNSRTLPS SSCLVAYKKT PPPVPPRTTS KPFISVTVQS STESAQDTYL DSQDHKSEVT
     SQSGLSNSSD SLDSSTRPPS VTRGGITPGP EAPEPPPKHA ALKSEQGTLT SSESHSEAIP
     KRKLSSIGIQ VDCIQPVPKE EPSPATKFQS IGIQVEDDWR SSAPSHSMSS RRDTDSDTQD
     ANDSSCKSSE RSLPDCTSHP NSISIDAGPR QAPKIAQIKR NLSYGDNSDP ALEASSLPPP
     DPWLETSSSS PAEPAQPGAC RRDGYWFLKL LQAETERLEG WCCQMDKETK ENNLSEEVLG
     KVLSAVGSAQ LLMSQKFQQF RGLCEQNLNP DANPRPTAQD LAGFWDLLQL SIEDISMKFD
     ELYHLKANSW QLVETPEKRK EEKKPPPPVP KKPAKSKAAV SRDKASDAGD KQRQEARKRL
     LAAKRAASVR QNSATESADS IEIYVPEAQT RL
//
ID   B1AZR7_MOUSE            Unreviewed;      1320 AA.
AC   B1AZR7;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 25.
DE   SubName: Full=Protocadherin 11 X-linked;
GN   Name=Pcdh11x; ORFNames=RP23-185M16.1-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Howden P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Heath P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BX005240; CAM16851.1; -; Genomic_DNA.
DR   EMBL; AC115298; CAM16851.1; JOINED; Genomic_DNA.
DR   EMBL; AC117258; CAM16851.1; JOINED; Genomic_DNA.
DR   EMBL; BX005446; CAM16851.1; JOINED; Genomic_DNA.
DR   EMBL; BX005446; CAM17585.1; -; Genomic_DNA.
DR   EMBL; AC115298; CAM17585.1; JOINED; Genomic_DNA.
DR   EMBL; AC117258; CAM17585.1; JOINED; Genomic_DNA.
DR   EMBL; BX005240; CAM17585.1; JOINED; Genomic_DNA.
DR   IPI; IPI00421107; -.
DR   UniGene; Mm.422941; -.
DR   UniGene; Mm.439552; -.
DR   ProteinModelPortal; B1AZR7; -.
DR   SMR; B1AZR7; 238-349, 473-665.
DR   Ensembl; ENSMUST00000113358; ENSMUSP00000108985; ENSMUSG00000034755.
DR   MGI; MGI:2442849; Pcdh11x.
DR   HOGENOM; HBG403071; -.
DR   HOVERGEN; HBG053523; -.
DR   InParanoid; B1AZR7; -.
DR   OMA; SECSYPV; -.
DR   OrthoDB; EOG43XV2N; -.
DR   Bgee; B1AZR7; -.
DR   Genevestigator; B1AZR7; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR013164; Cadherin_N.
DR   InterPro; IPR013585; Protocadherin.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 7.
DR   Pfam; PF00028; Cadherin; 6.
DR   Pfam; PF08266; Cadherin_2; 1.
DR   Pfam; PF08374; Protocadherin; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 7.
DR   SUPFAM; SSF49313; Cadherin; 6.
DR   PROSITE; PS00232; CADHERIN_1; 5.
DR   PROSITE; PS50268; CADHERIN_2; 7.
PE   4: Predicted;
KW   Calcium; Cell adhesion; Membrane; Repeat; Transmembrane;
KW   Transmembrane helix.
SQ   SEQUENCE   1320 AA;  145391 MW;  B378E39235DF1B9E CRC64;
     MDLLSGTYIF AVLLACVVFQ SGAQEKNYTV REEMPENVLI GDLLKDLNLS LIPDKSLTTP
     MQFKLVYKTG DVPLIRIEEG TGEIFTTGAR IDREKLCAGI VLDARCFYEV EVAVLPDEIF
     RLVKIRFLIE DINDNAPLFP TTVINISIPE NSAINSRYSL PAAIDPDIGI NGVQNYQLIK
     SQNIFGLDVI ETPEGDKMPQ LIVQKELDRE EKDTYVMKVK VEDGGFPQRS STAILQVSVA
     DTNDNHPIFI EKEIEVSIPE NAPIGSSVTQ LHATDADIGE NARIHFYFSN LVSNIAKRLF
     HLNTTTGLIT VKEPLDREES PSHKLLVLAT DGGSTPARAT VLVNVTDIND NVPSIDIRYI
     VNPTNGTVLL SENAPLNTKI ALITVMDKDS EHNGRVTCFT DHEVPFRLRP VFSNQFLLET
     AAFLDFESTR EYAIKLLAAD AGKPPLNQSS MLLIKVKDEN DNAPVFTQSF ISLSVPENNS
     PGAQLTKISA TDADSGQNAE ISYMLGFDAP PEFNLDQRTG ILTAVKKLDR EKQEKYYFTV
     LAQDNGIPPL MSNATVFVTV LDQNDNSPIF THNEYNFYVP ESLPKHGTVG LITVTDPDYG
     ENSAVTLSIL DVNDQFTIDP QSGVIRPNIS FDRERQESYT FYVKAEDGGR VSRSSTARVT
     INVVDVNDNK PIFIDPPSNY SFEWVLPSTN PGTVVFKVVA IDDDIGMNAE VLYSIVGGNT
     KGLFMIEQTS GNITLKEKCM VSDLGLHRVI VKANDLGQPD SLFNVVNVNF FINESVPNAT
     LIYELVRRSI DAPANQNTET TSASSPTTDY VKIMVAIVAG TITVVLVIFI TAVVRCRQPP
     HLKASQKNKQ NSEWVTPNPE NRQMIMMKKK KKKKKKHPPK NLLLNFVTIE EAKPDDGENE
     RNSVTLDLPI ELEEQTMGKY NWGTTPTTFK PDSPDLARHY KSASPQPAFQ IQPETPLNSK
     HHIIQELPLD NTFVGCDSIS KCSSSSSDPY SVSECSYPVT TFKAPVSVHI RPTMKEVVRS
     HTPMKEATTV EIWTHPHPQS QRRVTFHLPE GSQESISDGG LGDHDAGSLP STSHALPLGY
     PQEEYFDHAA PNNRTEGDGN SDPESTAEIT VQPTVEEASD TCTQECLILG HSDSCWMPAT
     LTNPSPSQIK TSAICHSPPR PRLSVRRYSP PVTQTVTICH SPPVTQAIAL CHSPPPVQVT
     VPRHSPPPAQ ASAVSYSPTL VQAVVIHHSP PLPQAATHHR TQAQPPMGLQ QGWVQGAGAD
     GLYPIDQGVQ GSTRAQFYTM AERFHPDDDS IKVIPLTTFT SGQQARSSRG DSPIIEEHPL
//
ID   B1B1E4_MOUSE            Unreviewed;       335 AA.
AC   B1B1E4;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   08-MAR-2011, entry version 26.
DE   SubName: Full=Regulator of G-protein signaling 6;
GN   Name=Rgs6; ORFNames=RP23-143E1.1-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Holt K.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CT033787; CAP19257.1; -; Genomic_DNA.
DR   EMBL; AC154684; CAP19257.1; JOINED; Genomic_DNA.
DR   EMBL; AC161055; CAP19257.1; JOINED; Genomic_DNA.
DR   IPI; IPI00970061; -.
DR   ProteinModelPortal; B1B1E4; -.
DR   SMR; B1B1E4; 255-310.
DR   STRING; B1B1E4; -.
DR   Ensembl; ENSMUST00000161801; ENSMUSP00000125256; ENSMUSG00000021219.
DR   MGI; MGI:1354730; Rgs6.
DR   GeneTree; ENSGT00560000076525; -.
DR   HOVERGEN; HBG007404; -.
DR   Bgee; B1B1E4; -.
DR   Genevestigator; B1B1E4; -.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; TAS:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; TAS:MGI.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR015898; G-protein_gamma_dom.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:4.10.260.10; G-protein_gamma_dom; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF00631; G-gamma; 1.
DR   SMART; SM00049; DEP; 1.
DR   SMART; SM00224; GGL; 1.
DR   SUPFAM; SSF48670; G-protein_gamma-like; 1.
DR   PROSITE; PS50186; DEP; 1.
PE   4: Predicted;
KW   Membrane; Transducer.
SQ   SEQUENCE   335 AA;  38501 MW;  9A89DB543EE854AA CRC64;
     MAQGSGDQRA VGIADPEESS PNMIVYCKIE DIITKMQDDK TGGVPIRTVK SFLSKIPSVV
     TGTDIVQWLM KNLSIEDPVE AIHLGSLIAA QGYIFPISDH VLTMKDDGTF YRFQAPYFWP
     SNCWEPENTD YAIYLCKRTM QNKARLELAD YEAENLARLQ RAFARKWEFI FMQAEAQVKI
     DRKKDKTERK ILDSQERAFW DVHRPVPGCV NTTEMDIRKC RRLKNPQKVK KSVYGVTDET
     QSQSPVHIPS QPIRKTTKDD IRKQITFLNA QIDRHCLKMS KVAESLIAYT EQYVEYDPFI
     TPAEPSNPWI SDDITLWDIE MTLTCTWLLC VSNGS
//
ID   B2FDI4_MOUSE            Unreviewed;        55 AA.
AC   B2FDI4;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   08-FEB-2011, entry version 21.
DE   SubName: Full=Meis homeobox 2;
DE   Flags: Fragment;
GN   Name=Meis2; ORFNames=RP23-230B1.1-017;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Phillimore B.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL929037; CAQ51575.1; -; Genomic_DNA.
DR   IPI; IPI00895428; -.
DR   UniGene; Mm.247566; -.
DR   UniGene; Mm.471935; -.
DR   STRING; B2FDI4; -.
DR   Ensembl; ENSMUST00000020367; ENSMUSP00000020367; ENSMUSG00000027210.
DR   Ensembl; ENSMUST00000110906; ENSMUSP00000106531; ENSMUSG00000027210.
DR   Ensembl; ENSMUST00000110907; ENSMUSP00000106532; ENSMUSG00000027210.
DR   Ensembl; ENSMUST00000150477; ENSMUSP00000121969; ENSMUSG00000027210.
DR   Ensembl; ENSMUST00000151279; ENSMUSP00000119867; ENSMUSG00000027210.
DR   MGI; MGI:108564; Meis2.
DR   GeneTree; ENSGT00550000074260; -.
DR   Bgee; B2FDI4; -.
DR   Genevestigator; B2FDI4; -.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0001654; P:eye development; IGI:MGI.
PE   4: Predicted;
KW   Homeobox.
FT   NON_TER      55     55
SQ   SEQUENCE   55 AA;  5757 MW;  6D1D20E3AC2AD6BA CRC64;
     MIDQSNRAGF LLDPSVSQGA AYSPEGQPMG SFVLDGQQHM GIRPAGPMSG MGMNM
//
ID   B2KF44_MOUSE            Unreviewed;       532 AA.
AC   B2KF44;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   08-MAR-2011, entry version 20.
DE   SubName: Full=Copine V;
DE   Flags: Fragment;
GN   Name=Cpne5; ORFNames=RP23-73B23.2-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Smith M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 2 C2 domains.
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DR   EMBL; CT009662; CAQ51804.1; -; Genomic_DNA.
DR   IPI; IPI00968982; -.
DR   Ensembl; ENSMUST00000024805; ENSMUSP00000024805; ENSMUSG00000024008.
DR   MGI; MGI:2385908; Cpne5.
DR   HOVERGEN; HBG066841; -.
DR   InParanoid; B2KF44; -.
DR   Bgee; B2KF44; -.
DR   Genevestigator; B2KF44; -.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR010734; Copine.
DR   InterPro; IPR002035; VWF_A.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF07002; Copine; 1.
DR   SMART; SM00239; C2; 2.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   4: Predicted;
FT   NON_TER       1      1
SQ   SEQUENCE   532 AA;  58677 MW;  39BDE12386EEC948 CRC64;
     FGRTEVIDNT LNPDFVRKFI VDYFFEEKQN LRFDLYDVDS KSPDLSKHDF LGQAFCTLGE
     IVGSSGSRLE KPLTIGTFSL NSRTGKPMPA VSNGGVPGKK CGTIILSAEE LSNCRDVATM
     QFCANKLDKK DFFGKSDPFL VFYRSNEDGT FTICHKTEVM KNTLNPVWQT FSIPVRALCN
     GDYDRTIKVE VYDWDRDGSH DFIGEFTTSY RELARGQSQF NIYEVINPKK KMKKKKYVNS
     GTVTLLSFAV ESESTFLDYI KGGTQINFTV AIDFTASNGN PSQSTSLHYM SPYQLNAYAL
     ALTAVGEIIQ HYDSDKMFPA LGFGAKLPPD GRVSHEFPLN GNQENPSCCG IDGILEAYHS
     SLRTVQLYGP TNFAPVVTHV ARNAAAVQDG SQYSVLLIIT DGVISDMAQT KEAIVNAAKL
     PMSIIIVGVG QAEFDAMVEL DGDDVRISSR GKLAERDIVQ FVPFRDYVDR TGNHVLSMAR
     LARDVLAEIP DQLVSYMKAQ GIRPRPPPAA PAQSPPQSPA HSPPGSPVHT HI
//
ID   B2KF50_MOUSE            Unreviewed;      1429 AA.
AC   B2KF50;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   08-MAR-2011, entry version 19.
DE   SubName: Full=UHRF1 (ICBP90) binding protein 1;
GN   Name=Uhrf1bp1; ORFNames=RP24-258K7.2-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Dunn M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CT009677; CAQ51768.1; -; Genomic_DNA.
DR   IPI; IPI00676350; -.
DR   RefSeq; NP_001074238.1; NM_001080769.1.
DR   UniGene; Mm.291291; -.
DR   PRIDE; B2KF50; -.
DR   Ensembl; ENSMUST00000114849; ENSMUSP00000110499; ENSMUSG00000039512.
DR   GeneID; 224648; -.
DR   KEGG; mmu:224648; -.
DR   CTD; 224648; -.
DR   MGI; MGI:3041238; Uhrf1bp1.
DR   HOVERGEN; HBG061128; -.
DR   InParanoid; B2KF50; -.
DR   OrthoDB; EOG4RXXZ9; -.
DR   NextBio; 377279; -.
DR   Bgee; B2KF50; -.
DR   Genevestigator; B2KF50; -.
PE   4: Predicted;
SQ   SEQUENCE   1429 AA;  157012 MW;  B0F9324749EBCE06 CRC64;
     MAGIIKKQIL KHLSRFTKNL SPDKINLSTL KGEGQLTHLE LDEEVLQNVL ELPTWLAITR
     VYCNRASIQI QWTKLKTHPI CLCLDKVEVE MQTCEDPRPP NGQSPIALAS GQSEYGFAEK
     VVEGMFIVVN SITIKIHSKA FHASFELWQL QGYSVNPNWQ QSDLRLTRIT DPRRGEVLTF
     KEITWQTLRV EADAIENGDQ DPVTTPLRLI TNQGRIQIAL KRRTKDCNVV ASKLTFLLDD
     LLWVLTDSQL KAMMKYAESL SEAMEKSAQQ RKSLAPESVQ TTPPAPSAQQ TWAQAFGGSQ
     GSSSSSRLSQ YFEKFDVKES SYHLLISRLD LHICDDSQSR EPGVSANRLT GGAMQLTFRR
     MAFDYYPFHR AGDSCKHWVR HCEAMETRGH WAQQLVTEFQ SRVEKQCEGG SVKPPWLLGV
     DPPFRRKADS FSSPGKTPLD KSPTQGRQAA FGAPAWNRLR SSCLVVRVDD LDIHQVSTAG
     QPSKKPSTLL SCSRKRHHLP PQVAAIHVQF TEYYFPDNQE LPVPCPNLYI QLNGLTFTVD
     PVSLLWGNLF CLDLYRSLEQ FKAIYKLEAS RGRDEHVDVR LDAFWLKVSF PLETRELAKL
     HRPQALVLST SSMIATNTRH APNCTRPDLQ SLFRGFAATE FFRCSYGHFP QVAGGFSLLH
     MLFLHHAFQM DSLPPQRLAA SQDLWSLHFT QISLDFEGTE NFRGHTLNFV APFPLSIWAC
     LPLRWQQAQA RRLLLASEGR LKQSASFGSP VHSEALAPES VSHQRSKTER DLKSLSGSTE
     GPAAAVREGD AGVDHKGRVA DLEDVADIHM LVHSTAHVRV RLDHYQYLAL LRLKEVLEGL
     QEQLTKDTEA MTGSPLQDQT VCIGVLFPSA EVALLMHPAP GTAHADSAGS DTTSLIDSEL
     SPSEDREPKS DASSDQGAVS PEKVLRDGSG ENLAASQERL PSDGELPDPG PCAQQPVGKS
     HEAVESLQAK KLSRAQSARS PATLKSPADR DAALNGQGEP VPLRSIEGDL SSAIHMTKDA
     TKEALHATVD LTKEAVSLTR DAFSLGRDRM TSTMHKMLSL PPAKEAMAKP DEGVVASVSG
     GAARLRFFSM KRTVSQQSFD GVSLDSGGPD DRISVDSDGS DSFVMLLESE SGPESVPPGS
     VTSVLDDSGI QGSPVTDSGG QGLPETNSSA SASGDLVMHS VSILVLKVNE VSLGIEVRGE
     DLAVALQAEE LALQQLGTVG LWQFLHGQCP GAGFQEPSNL KTNPIRPAVG LRFEVGPGAA
     VHSPLATQNG FLQFLLRGCD LELFTSVLNG LGPFLEDEEV PVVVPMQIEL LDCRVTLKDD
     IPPVYPTSPG PVPITLAMER LVLKRGDDGV FHLGAPAHDR PLTDVPEKLR LPKEQVLLVP
     LGQGLGCQEK ESPTLQQELM DTKQALAIAN QDKEKLLQEV RKYNPLFEL
//
ID   B2KF57_MOUSE            Unreviewed;       700 AA.
AC   B2KF57;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   08-FEB-2011, entry version 24.
DE   SubName: Full=Phosphodiesterase 4D, cAMP specific;
DE   Flags: Fragment;
GN   Name=Pde4d; ORFNames=RP24-383A20.1-008;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Glithero R.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CT025605; CAQ51655.1; -; Genomic_DNA.
DR   EMBL; AC161585; CAQ51655.1; JOINED; Genomic_DNA.
DR   EMBL; AC163650; CAQ51655.1; JOINED; Genomic_DNA.
DR   IPI; IPI00895058; -.
DR   STRING; B2KF57; -.
DR   PRIDE; B2KF57; -.
DR   Ensembl; ENSMUST00000135275; ENSMUSP00000119583; ENSMUSG00000021699.
DR   MGI; MGI:99555; Pde4d.
DR   GeneTree; ENSGT00550000074309; -.
DR   HOVERGEN; HBG108239; -.
DR   Bgee; B2KF57; -.
DR   Genevestigator; B2KF57; -.
DR   GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006198; P:cAMP catabolic process; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0006939; P:smooth muscle contraction; IMP:MGI.
DR   InterPro; IPR003607; Metal-dep_PHydrolase_HD_dom.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR023174; PDEase_CS.
DR   Gene3D; G3DSA:1.10.1300.10; PDEase_catalytic_dom; 1.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00471; HDc; 1.
DR   PROSITE; PS00126; PDEASE_I; 1.
PE   4: Predicted;
KW   Hydrolase; Metal-binding.
FT   NON_TER       1      1
SQ   SEQUENCE   700 AA;  79187 MW;  C2789BD2D6D8A4E0 CRC64;
     HSAVPVDLLA LSLQMAFVWD PLGVAVPGPS PRTRTRLRFS KSYSFDVDNG TSAGRSPLDP
     MTSPGSGLIL QANFVHSQRR ESFLYRSDSD YDLSPKSMSR NSSIASDIHG DDLIVTPFAQ
     VLASLRTVRN NFAALTNLQD RAPSKRSPMC NQPSINKATI TEEAYQKLAS ETLEELDWCL
     DQLETLQTRH SVSEMASNKF KRMLNRELTH LSEMSRSGNQ VSEYISNTFL DKQHEVEIPS
     PTQKEKEKKK RPMSQISGVK KLMHSSSLTN SCIPRFGVKT EQEDVLAKEL EDVNKWGLHV
     FRIAELSGNR PLTVIMHTIF QERDLLKTFK IPVDTLITYL MTLEDHYHAD VAYHNNIHAA
     DVVQSTHVLL STPALEAVFT DLEILAAIFA SAIHDVDHPG VSNQFLINTN SELALMYNDS
     SVLENHHLAV GFKLLQEENC DIFQNLTKKQ RQSLRKMVID IVLATDMSKH MNLLADLKTM
     VETKKVTSSG VLLLDNYSDR IQVLQNMVHC ADLSNPTKPL QLYRQWTDRI MEEFFRQGDR
     ERERGMEISP MCDKHNASVE KSQVGFIDYI VHPLWETWAD LVHPDAQDIL DTLEDNREWY
     QSTIPQSPSP APDDQEEGRQ GQTEKFQFEL TLEEDCESDT EKDSGSQVEE DTSCSDSKTL
     CTQDSESTEI PLDEQVEEEA VAEEESQPET CVPDDCCPDT
//
ID   B2KFM4_MOUSE            Unreviewed;       679 AA.
AC   B2KFM4;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   30-NOV-2010, entry version 18.
DE   SubName: Full=SRY-box containing gene 5;
GN   Name=Sox5; ORFNames=RP23-152D8.1-005;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Smith M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Kerry G.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RA   Heath P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CU207379; CAQ51609.1; -; Genomic_DNA.
DR   EMBL; CU210861; CAQ51609.1; JOINED; Genomic_DNA.
DR   EMBL; CU210928; CAQ51609.1; JOINED; Genomic_DNA.
DR   EMBL; CU210861; CAQ51616.1; -; Genomic_DNA.
DR   EMBL; CU207379; CAQ51616.1; JOINED; Genomic_DNA.
DR   EMBL; CU210928; CAQ51616.1; JOINED; Genomic_DNA.
DR   EMBL; CU210928; CAQ51825.1; -; Genomic_DNA.
DR   EMBL; CU207379; CAQ51825.1; JOINED; Genomic_DNA.
DR   EMBL; CU210861; CAQ51825.1; JOINED; Genomic_DNA.
DR   IPI; IPI00896030; -.
DR   UniGene; Mm.1752; -.
DR   ProteinModelPortal; B2KFM4; -.
DR   SMR; B2KFM4; 470-539.
DR   Ensembl; ENSMUST00000111749; ENSMUSP00000107378; ENSMUSG00000041540.
DR   MGI; MGI:98367; Sox5.
DR   HOVERGEN; HBG003915; -.
DR   Bgee; B2KFM4; -.
DR   Genevestigator; B2KFM4; -.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0010843; F:promoter binding; IDA:MGI.
DR   GO; GO:0021953; P:central nervous system neuron differentiation; IGI:MGI.
DR   GO; GO:0060164; P:regulation of timing of neuron differentiation; IMP:MGI.
DR   InterPro; IPR000910; HMG_HMG1/HMG2.
DR   InterPro; IPR009071; HMG_superfamily.
DR   Gene3D; G3DSA:1.10.30.10; HMG-box; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   4: Predicted;
SQ   SEQUENCE   679 AA;  75209 MW;  D638BF4CC26B842A CRC64;
     MLTDPDLPQE FERMSSKRPA SPYGETDGEV AMVTSRQKVE EEESERLPAF HLPLHEVDGN
     KVMSSLAPYN SSTSPQKAEE GGRQSGESVS SAALGTPERR KGSLADVVDT LKQRKMEELI
     KNEPEDTPSI EKLLSKDWKD KLLAMGSGNF GEIKGTPESL AEKERQLMGM INQLTSLREQ
     LLAAHDEQKK LAASQIEKQR QQMELAKQQQ EQIARQQQQL LQQQHKINLL QQQIQVQGQL
     PPLMIPVFPP DQRTLAAAAQ QGFLLPPGFS YKAGCSDPYP VQLIPTTMAA AAAATPGLGP
     LQLQDEVAQP LNLSAKPKTS DGKSPASPTS PHMPALRINS GAGPLKASVP AALASPSARV
     STIGYLNDHD AVTKAIQEAR QMKEQLRREQ QALDGKVAVV NSIGLSNCRT EKEKTTLESL
     TQQLAVKQNE EGKFSHGMMD FNMSGDSDGS AGVSESRIYR ESRGRGSNEP HIKRPMNAFM
     VWAKDERRKI LQAFPDMHNS NISKILGSRW KAMTNLEKQP YYEEQARLSK QHLEKYPDYK
     YKPRPKRTCL VDGKKLRIGE YKAIMRNRRQ EMRQYFNVGQ QAQIPIATAG VVYPSAIAMA
     GMPSPHLPSE HSSVSSSPEP GMPVIQSTYG AKGEEPHIKE EIQAEDINGE IYEEYDEEEE
     DPDVDYGSDS ENHIAGQAN
//
ID   B2KFV9_MOUSE            Unreviewed;       297 AA.
AC   B2KFV9;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   08-MAR-2011, entry version 20.
DE   SubName: Full=F-box only protein 2;
GN   Name=Fbxo2; ORFNames=RP23-139J21.11-001, mCG_16665;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Howden P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 F-box domain.
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DR   EMBL; CU207417; CAQ52212.1; -; Genomic_DNA.
DR   EMBL; CH466594; EDL14813.1; -; Genomic_DNA.
DR   IPI; IPI00894941; -.
DR   UniGene; Mm.262287; -.
DR   ProteinModelPortal; B2KFV9; -.
DR   SMR; B2KFV9; 47-297.
DR   STRING; B2KFV9; -.
DR   PRIDE; B2KFV9; -.
DR   Ensembl; ENSMUST00000047951; ENSMUSP00000037377; ENSMUSG00000041556.
DR   MGI; MGI:2446216; Fbxo2.
DR   HOVERGEN; HBG003593; -.
DR   InParanoid; B2KFV9; -.
DR   Bgee; B2KFV9; -.
DR   Genevestigator; B2KFV9; -.
DR   GO; GO:0005829; C:cytosol; TAS:MGI.
DR   GO; GO:0043197; C:dendritic spine; IDA:MGI.
DR   GO; GO:0001540; F:beta-amyloid binding; IDA:MGI.
DR   GO; GO:0030246; F:carbohydrate binding; IDA:MGI.
DR   GO; GO:0001948; F:glycoprotein binding; IDA:MGI.
DR   GO; GO:0030433; P:ER-associated protein catabolic process; IDA:MGI.
DR   GO; GO:0006516; P:glycoprotein catabolic process; IDA:MGI.
DR   GO; GO:0031396; P:regulation of protein ubiquitination; IDA:MGI.
DR   InterPro; IPR007397; F-box-assoc_dom.
DR   InterPro; IPR001810; F-box_dom_cyclin-like.
DR   InterPro; IPR022364; F-box_dom_Skp2-like.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   Pfam; PF00646; F-box; 1.
DR   Pfam; PF04300; FBA; 1.
DR   SUPFAM; SSF81383; F-box_dom_Skp2-like; 1.
DR   SUPFAM; SSF49785; Gal_bind_like; 1.
DR   PROSITE; PS51114; FBA; 1.
DR   PROSITE; PS50181; FBOX; 1.
PE   4: Predicted;
SQ   SEQUENCE   297 AA;  33648 MW;  F86926467752630C CRC64;
     MDGDGDPESV SHPEEASPEE QPEEAGAEAS AEEEQLREAE EEEEAEAVEY LAELPEPLLL
     RVLAELPATE LVQACRLVCL RWKELVDGAP LWLLKCQQEG LVPEGSADEE RDHWQQFYFL
     SKRRRNLLRN PCGEEDLEGW SDVEHGGDGW KVEELPGDNG VEFTQDDSVK KYFASSFEWC
     RKAQVIDLQA EGYWEELLDT TQPAIVVKDW YSGRTDAGSL YELTVRLLSE NEDVLAEFAT
     GQVAVPEDGS WMEISHTFID YGPGVRFVRF EHGGQDSVYW KGWFGARVTN SSVWVEP
//
ID   B2KGG3_MOUSE            Unreviewed;       403 AA.
AC   B2KGG3;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   08-MAR-2011, entry version 18.
DE   SubName: Full=4932411E22Rik protein;
DE   SubName: Full=Novel protein;
GN   Name=4932411E22Rik; Synonyms=RP23-205A9.2; ORFNames=RP23-205A9.2-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Sycamore N.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testicle;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC140961; AAI40962.1; -; mRNA.
DR   EMBL; CU392839; CAQ51539.1; -; Genomic_DNA.
DR   IPI; IPI00895087; -.
DR   UniGene; Mm.60997; -.
DR   Ensembl; ENSMUST00000050983; ENSMUSP00000049776; ENSMUSG00000047490.
DR   MGI; MGI:3045332; 4932411E22Rik.
DR   HOGENOM; HBG443874; -.
DR   HOVERGEN; HBG070855; -.
DR   InParanoid; B2KGG3; -.
DR   OrthoDB; EOG4C5CJG; -.
DR   Bgee; B2KGG3; -.
DR   Genevestigator; B2KGG3; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   403 AA;  44058 MW;  823C342942269D53 CRC64;
     MPLSVPLHTA AVHFCSYREK FISLYCRLSA VVELDSLNTQ QSLREAISDS EVAAAKQRHQ
     QVLDFIQQID EVWREMRWIM DALQYARYKQ PVSGLPITKL IDSSSEQNLK KISSTSSHID
     CLPSTSPSPE MHRRKAVSES QPCSDEEGCS EVFLPTDSDY DSSDALSPRD LDLVYLSSHD
     IAQQALSGLS GSAPDVLQVH DMKASMGPGQ DPQGPGQGPD TDHSCVEFLH SLTLTGLAPK
     NHAKMVPGTR PPLGFLGKRK PGKHQHYGGF SRHHHWLRMH SETQSLSLSE GVYTQHLSQA
     CGLAEDPGEA EGPGPVVDGP RGLPLAHAAS LPEERRSCLQ DPRRPLQRVY VEPYSDTLAG
     QDPKLWTSLS PTPAGRSSLP SSTSSEMSPD PTSPVSEILS SML
//
ID   B2RPU8_MOUSE            Unreviewed;       756 AA.
AC   B2RPU8;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 29.
DE   SubName: Full=MCG130675;
DE   SubName: Full=SCAN domain containing 3;
GN   Name=Scand3; ORFNames=mCG_130675;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC137610; AAI37611.1; -; mRNA.
DR   EMBL; CH466529; EDL19492.1; -; Genomic_DNA.
DR   IPI; IPI00407413; -.
DR   RefSeq; NP_898911.2; NM_183088.2.
DR   UniGene; Mm.422716; -.
DR   STRING; B2RPU8; -.
DR   PRIDE; B2RPU8; -.
DR   Ensembl; ENSMUST00000041466; ENSMUSP00000044533; ENSMUSG00000034173.
DR   GeneID; 71970; -.
DR   KEGG; mmu:71970; -.
DR   CTD; 71970; -.
DR   MGI; MGI:1919220; Scand3.
DR   HOGENOM; HBG446327; -.
DR   HOVERGEN; HBG067573; -.
DR   InParanoid; B2RPU8; -.
DR   OMA; CKPLERT; -.
DR   OrthoDB; EOG4XWFX9; -.
DR   NextBio; 335086; -.
DR   Bgee; B2RPU8; -.
DR   Genevestigator; B2RPU8; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   InterPro; IPR010625; CHCH.
DR   InterPro; IPR012337; RNaseH-like.
DR   Pfam; PF06747; CHCH; 1.
DR   SUPFAM; SSF53098; RNaseH_fold; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   756 AA;  84267 MW;  80ACE18DC80DCA78 CRC64;
     MPRGSRIRTS RVTLLAGRAP QMRAAPRRAP AAQPPAAAAP SAVGSPAAAP RQPGLMAQMA
     TTAAGVAVGS AVGHTLGHAI TGGFSGGGSA EPAKPDITYQ EPQGAQLQNQ QSFGPCSLEI
     KQFLECAQNQ SDVKLCEGFN EVLRQCRIAN VDHPRPVDHG ERNVKRRKYN EGFLQYGFTS
     TITVGIERPQ CVICGVVLSA ESMKPNKLKR HFESKHSSFA GKDTNYFRSK ADGLKKARPD
     TGSKSNKQNV AAVETSYLVA LRIARDMKPH TFAEHLLFPV AKDRVRVMIG DEFVTKLSAV
     SLSNDTVRRR IHDMSADILD QVVQEIKSAP LPICSIQLDE STDVANCLQL MVYVRYINDG
     DFKDEFLCCK PLERTATALD VFEAVDSFLR QHEISWKSIC GVCTDGAPAT LGCQSGFQRL
     VLNESPKAIG AHCMLHLQTL AMKTLPQDFQ EVMKSVLSSV NFVKASSLNS RLFLQLCSDL
     DEPSKTLLLH TEGRWLSRGK VLKRIFELRD ELKMFFNQKA IRQFEALFSD NSALQKVAYL
     VDIFTILNEL NLSLQGPNST CLDLSEKIHS FQMKLQLWQK KLDENKFYML PTLSAFFEEH
     DIEQHKRITV VISVKEHLDM LASEISWYFP NLPEIPFALA RSPFSVKAED VPETAQEDFT
     RLTNSDAARA DFSTMPVTQF WVKCLQSYPV LSEMVLRLLL PFPTTYLCET GFSSLLVIKS
     KYRSRLVVED DLRCALAKTT PRISDLVRKK QSQPSH
//
ID   B2RPZ8_MOUSE            Unreviewed;       286 AA.
AC   B2RPZ8;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   11-JAN-2011, entry version 18.
DE   SubName: Full=2810459M11Rik protein;
GN   Name=2810459M11Rik;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC137675; AAI37676.1; -; mRNA.
DR   IPI; IPI00921647; -.
DR   RefSeq; NP_001138465.1; NM_001144993.1.
DR   UniGene; Mm.54981; -.
DR   Ensembl; ENSMUST00000027429; ENSMUSP00000027429; ENSMUSG00000026227.
DR   GeneID; 72792; -.
DR   KEGG; mmu:72792; -.
DR   MGI; MGI:1920042; 2810459M11Rik.
DR   HOVERGEN; HBG106639; -.
DR   InParanoid; B2RPZ8; -.
DR   Bgee; B2RPZ8; -.
DR   Genevestigator; B2RPZ8; -.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   286 AA;  30320 MW;  7B9F6CAF39BFB4F6 CRC64;
     MESELEALAP RPASPAEPPF QALVEAAGGR GQVLLVGELW EREQSRALLR DFAGAVFPPE
     SAPGKPGCAE AESAGTAAAT ESHGAPGAKA ERAIRSPLVF VLCRVGSLTS RESRRRLREM
     LRDVRDRRCE GAALVGVLVA DTGADDARAP ELQLLETLLR TVFGRQVGGP VQAAAFRPGC
     PASSLAVQEA ACRALQAAGP GRPEGAWERP ARTGLLTCFS WGPRRQRKNR GVTSSQGPAQ
     EHLQFSEEEL ALTPVFPNGD CEDRGNGSRA QDGGVHIPPD PPEDTR
//
ID   B2RQ57_MOUSE            Unreviewed;      1078 AA.
AC   B2RQ57;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 29.
DE   SubName: Full=Abl2 protein;
GN   Name=Abl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; BC137771; AAI37772.1; -; mRNA.
DR   IPI; IPI00914726; -.
DR   RefSeq; NP_001129576.1; NM_001136104.1.
DR   RefSeq; NP_033725.2; NM_009595.3.
DR   UniGene; Mm.329515; -.
DR   ProteinModelPortal; B2RQ57; -.
DR   SMR; B2RQ57; 108-558, 978-1078.
DR   STRING; B2RQ57; -.
DR   GeneID; 11352; -.
DR   KEGG; mmu:11352; -.
DR   CTD; 11352; -.
DR   MGI; MGI:87860; Abl2.
DR   HOVERGEN; HBG004162; -.
DR   Genevestigator; B2RQ57; -.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; TAS:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:InterPro.
DR   GO; GO:0051017; P:actin filament bundle assembly; IDA:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR015015; F-actin_binding.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF08919; F_actin_bind; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00808; FABD; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; SH3 domain; Transferase.
SQ   SEQUENCE   1078 AA;  117766 MW;  7CF6AA48C100E1F4 CRC64;
     MGQQVGRVGE APGLQQPQPR GIRGSSAARP SGRRRDPAGR TADAGFNVFT QHDHFASCVE
     DGFEGDKTGG SSPEVLHRPF GCDAESQALN EAIRWSSKEN LLGATESDPN LFVALYDFVA
     SGDNTLSITK GEKLRVLGYN QNGEWSEVRS KNGQGWVPSN YITPVNSLEK HSWYHGPVSR
     SAAEYLLSSL INGSFLVRES ESSPGQLSIS LRYEGRVYHY RINTTTDSKV YVTAESRFST
     LAELVHHHST VADGLVTTLH YPAPKCNKPT VYGVSPIHDK WEMERTDITM KHKLGGGQYG
     EVYVGVWKKY SLTVAVKTLK EDTMEVEEFL KEAAVMKEIK HPNLVQLLGV CTLEPPFYIV
     TEYMPYGNLL DYLRECSREE VTAVVLLYMA TQISSAMEYL EKKNFIHRDL AARNCLVGEN
     HVVKVADFGL SRLMTGDTYT AHAGAKFPIK WTAPESLAYN TFSIKSDVWA FGVLLWEIAT
     YGMSPYPGID LSQVYDLLEK GYRMEQPEGC PPKVYELMRA CWKWSPADRP SFAETHQAFE
     TMFHDSSISE EVAEELGRTA SSSSVVPYLP RLPLLPSKTR TLRKQGENKE NLDGGLDAAE
     SLASSSAPAG FIRSTQASSG SPALPRKQRD KSPSSLLEDA KETCFTRDRK GGFFSSFMKK
     RNAPTPPKRS SSFREMENQP HKKYELTGLP EQDRMAMTLP RNCQRSKLQL ERTVSTSSQP
     EENVDRANDM LPKKSEEGAA PARERPKAKL LPRGATALPL RAPDPAITES DSPGVGVAGV
     AAAPKGKERN GGTRLGVAGV PEDGEQLGWS SPAKAVAVLP TTHNHKVPVL ISPTLKHTPA
     DVQLIGTDSQ GNKFKLLSEH QVTSSGDKDR PRRVKPKCAP PPPPVMRLLQ HPSTCSDPEE
     EPTAPPAGQH TPETQEGGKK AAPGPMPSSG KPGRPVMPPP QVPLPTSSIS PAKMANGTAG
     TKVALRKTKQ AAEKISADKI SKEALLECAD LLSSAITEPV PNSQLVDTGH QLLDYCSGYV
     DSIPQTRNKF AFREAVSKLE LSLQELQVSS TAAGVPGTNP VLNNLLSCVQ EISDVVQR
//
ID   B2RQ68_MOUSE            Unreviewed;      1067 AA.
AC   B2RQ68;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   11-JAN-2011, entry version 16.
DE   SubName: Full=Luzp1 protein;
GN   Name=Luzp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC137784; AAI37785.1; -; mRNA.
DR   EMBL; BC137786; AAI37787.1; -; mRNA.
DR   IPI; IPI00271985; -.
DR   UniGene; Mm.480631; -.
DR   PRIDE; B2RQ68; -.
DR   Ensembl; ENSMUST00000001116; ENSMUSP00000001116; ENSMUSG00000001089.
DR   Ensembl; ENSMUST00000105849; ENSMUSP00000101475; ENSMUSG00000001089.
DR   MGI; MGI:107629; Luzp1.
DR   HOVERGEN; HBG081939; -.
DR   InParanoid; B2RQ68; -.
DR   Bgee; B2RQ68; -.
DR   Genevestigator; B2RQ68; -.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1067 AA;  119262 MW;  A37BEF4B16E4113A CRC64;
     MAELTNYKDA ASNRHLRFKL QSLSRRLDEL EEATKNLQRA EDELLDLQDK VIQAEGSDSS
     TLAEIEVLRQ RVLKIEGKDE EIKRAEDLCH TMKEKLEEEE NLTRELKSEI ERLQKRMVDL
     EKLEEALSRS KNECSQLCLS LNEERNLTKK ISSELEMLRV KVKELESSED RLDKTEQSLV
     SELEKLKSLT LSFVNERKYL NEKEKENEKI IKELTQKLEQ NKKMNRDHMR NASTFLERND
     LRIEDGISST LSSKESKRKG SLDYLKQVEN ETRDKSENEK NRNQEDNKVK DLNQEIEKLK
     TQIKHFESLE EELKKMRAKN NDLQDNYLTE LNRNRSLASQ LEEIKLQVRK QKELGNGDIE
     GEDAFLLGRG RHERTKLKGH GSEASVSKHT SRELSPQHKR ERLRNREFAL SNEHYSLSSK
     QASSPVFTNK RAAKASNMGM GTDSGTQETK RTEDRFAPGS SHSEGKRGRE QPSVLSRYPP
     AAQEHTKVWK GAPKPGTESG LKGKVEKTTR TFSDSTHVSV PNDIVGKGDK TSDLSSEAHC
     GKRGQVPGHA SQGTQAVESS CSKAIGALSS SQKASSEGLS KGKKTANGLA ADANFSNSKA
     PILSKYPYSS RSQENILQGF SLPNKEGVDQ PVAVVMEDSS QHEALRCRVI KSSGREKPDS
     DDDLDIESFV TAKLVNTTIT PEPEPKPQPN SREKVKSRGG TRTALFENDK NAAIENDSVK
     PTRPSSNAIE FPDANCAGVK NQRPFSPREA LRSRAIIKPV IIDKDVKKIM GGSGTEVVLE
     KQKSTSKSVT SKVTSSITIY PSDSSGPRAV PSEAPRERHT STSNIQVGPP ELTAISNHVS
     SPLELSIHKH DITLQLTEAE RVGDGSPKNR AEMVVSRSSI LIKPSESVEK NSHVPPAETI
     RWKSHSASSE VASSDSRHIT VRNAWKSKRD PPTRIGRNME ATNAYTQRSP TDFLELEQPR
     SHPSEQGARK VGSSGDAPER SSRRTQSSLT ASEVLTRRDR MGGAITAASW NHSSSMEEGE
     DSTFVTSRRI HNPLEHSELP GKQGLPEPEP VWTEERLHPA KPYAEED
//
ID   B2RQ71_MOUSE            Unreviewed;      1556 AA.
AC   B2RQ71;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 19.
DE   SubName: Full=Dip2c protein;
GN   Name=Dip2c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC137787; AAI37788.1; -; mRNA.
DR   EMBL; BC144910; AAI44911.1; -; mRNA.
DR   IPI; IPI00875553; -.
DR   UniGene; Mm.217326; -.
DR   ProteinModelPortal; B2RQ71; -.
DR   STRING; B2RQ71; -.
DR   Ensembl; ENSMUST00000062376; ENSMUSP00000055231; ENSMUSG00000048264.
DR   MGI; MGI:1920179; Dip2c.
DR   eggNOG; roNOG07765; -.
DR   HOGENOM; HBG717784; -.
DR   HOVERGEN; HBG026594; -.
DR   InParanoid; B2RQ71; -.
DR   OrthoDB; EOG4KSPHX; -.
DR   Bgee; B2RQ71; -.
DR   Genevestigator; B2RQ71; -.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0008134; F:transcription factor binding; IEA:InterPro.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR010506; DMAP1-bd.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF06464; DMAP_binding; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1556 AA;  170922 MW;  196FCD14635BC27E CRC64;
     MADRSLEGMA LPLEVRARLA ELELELSEGD ITQKGYEKKR SKLIGAYLPQ PPRVDQALPQ
     ERRAPVTPSS ASRYHRRRSS GSRDERYRSD VHTEAVQAAL AKHKERKMAV PMPSKRRSLV
     VQTSMDAYTP PDTSSGSEDE GSVQGDSQGT PTSSQGSINM EHWISQAIHG STTSTTSSSS
     TQSGGSGAAH RLADVMAQTH IENHSAPPDV TTYTSEHSIQ VERPQGSTTS RTAPKYGNAE
     LMETGDGVPV SSRVSAKIQQ LVNTLKRPKR PPLREFFVDD FEELLEVQQP DPNQPKPEGA
     QMLATRGEQL GVVTNWPPSL EAALQRWGTI SPKAPCLTTM DTNGKPLYIL TYGKLWTRSM
     KVAYNILHKL GTKQEPMVRP GDRVALVFPN NDPAAFMVAF YGCLLAEVVP VPIEVPLTRK
     DAGSQQIGFL LGSCGVTVAL TSDACHKGLP KSPTGEIPQF KGWPKLLWFV TESKHLSKPP
     RDWFPHIKDA NNDTAYIEYK TCKDGSVLGV TVTRIALLTH CQALTQACGY TEAETIVNVL
     DFKKDVGLWH GILTSVMNMM HVISIPYSLM KVNPLSWIQK VCQYKAKVAC VKSRDMHWAL
     VAHRDQRDVN LSSLRMLIVA DGANPWSISS CDAFLNVFQS KGLRQEVICP CASSPEALTV
     AIRRPTDDSN QPPGRGVLSM HGLTYGVIRV DSEEKLSVLT VQDVGLVMPG AIMCSVKPDG
     IPQLCRTDEI GELCVCAVAT GTSYYGLSGM TKNTFEVFPM TSSGAPISEY PFIRTGLLGF
     VGPGGLVFVV GKMDGLMVVS GRRHNADDIV ATALAVEPMK FVYRGRIAVF SVTVLHDERI
     VIVAEQRPDS TEEDSFQWMS RVLQAIDSIH QVGVYCLALV PANTLPKTPL GGIHLSETKQ
     LFLEGSLHPC NVLMCPHTCV TNLPKPRQKQ PEIGPASVMV GNLVSGKRIA QASGRDLGQI
     EDNDQARKFL FLSEVLQWRA QTTPDHLLYT LLNCRGTIAN SLTCVQLHKR AEKIAVMLME
     RGHLQDGDHV ALVYPPGIDL IAAFYGCLYA GCVPITVRPP HPQNIATTLP TVKMIVEVSR
     SACLMTTQLI CKLLRSREAA AAVDVRTWPL ILDTDDLPKK RPAQIYKPSN PDTLAYLDFS
     VSTTGMLAGV KMSHAATSAF CRSIKLQCEL YPSREVAICL DPYCGLGFVL WCLCSVYSGH
     QSILIPPSEL ETNPALWLLA VSQYKVRDTF CSYSVMELCT KGLGSQTESL KARGLDLSRV
     RTCVVVAEER PRIALTQSFS KLFKDLGLHP RAVSTSFGCR VNLAICLQGT SGPDPTTVYV
     DMRALRHDRV RLVERGSPHS LPLMESGKIL PGVRIIIANP ETKGPLGDSH LGEIWVHSAH
     NASGYFTIYG DESLQSDHFN SRLSFGDTQT IWARTGYLGF LRRTELTDAN GERHDALYVV
     GALDEAMELR GMRYHPIDIE TSVIRAHKSV TECAVFTWTN LLVVVVELDG SEQEALDLVP
     LVTNVVLEEH YLIVGVVVVV DIGVIPINSR GEKQRMHLRD GFLADQLDPI YVAYNM
//
ID   B2RQC6_MOUSE            Unreviewed;      2225 AA.
AC   B2RQC6;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 32.
DE   SubName: Full=Carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase;
DE   SubName: Full=Carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase, isoform CRA_c;
GN   Name=Cad; ORFNames=mCG_23490;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC137856; AAI37857.1; -; mRNA.
DR   EMBL; CH466524; EDL37329.1; -; Genomic_DNA.
DR   IPI; IPI00380280; -.
DR   RefSeq; NP_076014.1; NM_023525.1.
DR   UniGene; Mm.305535; -.
DR   ProteinModelPortal; B2RQC6; -.
DR   SMR; B2RQC6; 2-603, 1921-2224.
DR   STRING; B2RQC6; -.
DR   PRIDE; B2RQC6; -.
DR   Ensembl; ENSMUST00000013773; ENSMUSP00000013773; ENSMUSG00000013629.
DR   GeneID; 69719; -.
DR   KEGG; mmu:69719; -.
DR   CTD; 69719; -.
DR   MGI; MGI:1916969; Cad.
DR   HOGENOM; HBG405439; -.
DR   HOVERGEN; HBG000279; -.
DR   InParanoid; B2RQC6; -.
DR   OMA; IVAHAER; -.
DR   OrthoDB; EOG46WZ7G; -.
DR   PhylomeDB; B2RQC6; -.
DR   NextBio; 330178; -.
DR   Bgee; B2RQC6; -.
DR   Genevestigator; B2RQC6; -.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004070; F:aspartate carbamoyltransferase activity; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004086; F:carbamoyl-phosphate synthase activity; IEA:InterPro.
DR   GO; GO:0016812; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides; IEA:InterPro.
DR   GO; GO:0006207; P:'de novo' pyrimidine base biosynthetic process; IEA:InterPro.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00001; Asp_carb_tr; 1; -.
DR   InterPro; IPR006680; Amidohydro_1.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR   InterPro; IPR002082; Asp_carbamoyltransf_euk.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR001317; CarbamoylP_synth_GATase_dom.
DR   InterPro; IPR006275; CarbamoylP_synth_lsu.
DR   InterPro; IPR005479; CarbamoylP_synth_lsu_ATP-bd.
DR   InterPro; IPR005483; CarbamoylP_synth_lsu_CPS-dom.
DR   InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR   InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR   InterPro; IPR006274; CarbamoylP_synth_ssu.
DR   InterPro; IPR002474; CarbamoylP_synth_ssu_N.
DR   InterPro; IPR004722; DHOase.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   InterPro; IPR017926; GATASE_1.
DR   InterPro; IPR000991; GATase_class1_C.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR013817; Pre-ATP_grasp.
DR   InterPro; IPR016185; PreATP-grasp-like.
DR   Gene3D; G3DSA:3.30.1490.20; ATP_grasp_subdomain_1; 2.
DR   Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 2.
DR   Gene3D; G3DSA:1.10.1030.10; CarbamoylP_synth_lsu_oligo; 1.
DR   Gene3D; G3DSA:3.50.30.20; G3DSA:3.50.30.20; 1.
DR   Gene3D; G3DSA:3.40.50.1380; MGS-like_dom; 1.
DR   Gene3D; G3DSA:3.40.50.20; Pre-ATP_grasp; 2.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   Pfam; PF00289; CPSase_L_chain; 2.
DR   Pfam; PF02786; CPSase_L_D2; 2.
DR   Pfam; PF02787; CPSase_L_D3; 1.
DR   Pfam; PF00988; CPSase_sm_chain; 1.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF02142; MGS; 1.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00101; ATCASE.
DR   PRINTS; PR00098; CPSASE.
DR   PRINTS; PR00099; CPSGATASE.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF53671; Asp/Orn_carbamoyltranf; 1.
DR   SUPFAM; SSF48108; CarbamoylP_synth_lsu_oligo; 1.
DR   SUPFAM; SSF52021; CP_synthsmall; 1.
DR   SUPFAM; SSF51338; Metalo_hydrolase; 1.
DR   SUPFAM; SSF52335; MGS-like_dom; 1.
DR   SUPFAM; SSF52440; PreATP-grasp-like; 2.
DR   TIGRFAMs; TIGR00670; asp_carb_tr; 1.
DR   TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR   TIGRFAMs; TIGR01368; CPSaseIIsmall; 1.
DR   TIGRFAMs; TIGR00857; pyrC_multi; 1.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
DR   PROSITE; PS00866; CPSASE_1; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
DR   PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR   PROSITE; PS00483; DIHYDROOROTASE_2; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   2225 AA;  243238 MW;  E7E606A0F650ABB4 CRC64;
     MAALVLEDGS VLQGRPFGAA VSTAGEVVFQ TGMVGYPEAL TDPSYKAQIL VLTYPLIGNY
     GIPSDEEDEF GLSKWFESSE IHVAGLVVGE CCPTPSHWSA NCTLHEWLQQ RGIPGLQGVD
     TRELTKKLRE QGSLLGKLVQ KGTEPSALPF VDPNARPLAP EVSIKTPRVF NAGGAPRICA
     LDCGLKYNQI RCLCQLGAEV TVVPWDHELD SQKYDGLFLS NGPGDPASYP GVVSTLSRVL
     SEPNPRPVFG ICLGHQLLAL AIGAKTYKMR YGNRGHNQPC LLVGTGRCFL TSQNHGFAVD
     ADSLPAGWAP LFTNANDCSN EGIVHDSLPF FSVQFHPEHR AGPSDMELLF DVFLETVREA
     AAGNIGGQTV RERLAQRLCP PELPIPGSGL PPPRKVLILG SGGLSIGQAG EFDYSGSQAI
     KALKEENIQT LLINPNIATV QTSQGLADKV YFLPITLHYV TQVIRNERPD GVLLTFGGQT
     ALNCGVELTK AGVLARYGVR VLGTPVETIE LTEDRRAFAA RMAEIGEHVA PSEAANSLEQ
     AQAAAERLGY PVLVRAAFAL GGLGSGFAST KEELSALVAP AFAHTSQVLI DKSLKGWKEI
     EYEVVRDAYG NCVTVCNMEN LDPLGIHTGE SIVVAPSQTL NDREYQLLRR TAIKVTQHLG
     IVGECNVQYA LNPESEQYYI IEVNARLSRS SALASKATGY PLAYVAAKLA LGIPLPELRN
     SVTGGTAAFE PSLDYCVVKI PRWDLSKFLR VSTKIGSCMK SVGEVMGIGR SFEEAFQKAL
     RMVDENCVGF DHTVKPVSDM ELETPTDKRI FVVAAALWAG YSVERLYELT RIDCWFLHRM
     KRIVTHAQLL EQHRGQALPQ DLLHQAKCLG FSDKQIALAV LSTELAVRKL RQELGICPAV
     KQIDTVAAEW PAQTNYLYLT YWGNTHDLDF RAPHVLVLGS GVYRIGSSVE FDWCAVGCIQ
     QLRKMGYKTI MVNYNPETVS TDYDMCDRLY FDEISFEVVM DIYELENPEG VILSMGGQLP
     NNMAMALHRQ QCRVLGTSPE AIDSAENRFK FSRLLDTIGI SQPQWRELSD LESARQFCHT
     VGYPCVVRPS YVLSGAAMNV AYTDGDLERF LSSAAAVSKE HPVVISKFIQ EAKEIDVDAV
     ACDGIVSAIA ISEHVENAGV HSGDATLVTP PQDITPKTLE RIKAIVHAVG QELQVTGPFN
     LQLIAKDDQL KVIECNVRVS RSFPFVSKTL GVDLVALATR IIMGEKVEPV GLMTGSGVVG
     VKVPQFSFSR LAGADVVLGV EMTSTGEVAG FGESRCEAYL KAMLSTGFKI PEKNILLTIG
     SYKNKSELLP TVRLLESLGY SLYASLGTAD FYTEHGVKVT AVDWHFEEAV DGECPPQRSI
     LDQLAENHFE LVINLSMRGA GGRRLSSFVT KGYRTRRLAA DFSVPLIIDI KCTKLFVEAL
     GQIGPAPPLK VHVDCMTSQK LVRLPGLIDV HVHLREPGGT HKEDFASGTA AALAGGVTMV
     CAMPNTRPPI IDAPALALAQ KLAEAGARCD FTLFLGASSE NAGTLGAVAG SAAGLKLYLN
     ETFSELRLDS VAQWMEHFET WPAHLPIVAH AERQSVAAVL MVAQLTQRPV HICHVARKEE
     ILLIKTAKAQ GLPVTCEVAP HHLFLNREDL ERLGPGKGEV RPELGSREDM EALWENMAVI
     DCFASDHAPH TLEEKCGPKP PPGFPGLETM LPLLLTAVSE GRLSLDDLLQ RLHHNPRRIF
     HLPLQEDTYV EVDLEHEWTV PSHMPFSKAR WTPFEGQKVK GTVRRVVLRG EVAYIDGQVL
     VPPGYGQDVR KWPQGVVPQP PPSTPATTEI TTTPERPRRV IPGLPDGRFH LPPRIHRASD
     PGLPAEEPKE KPPRKVVEPE LMGTPDGPCY PAPPVPRQAS PQNLGSSGLL HPQMSPLLHS
     LVGQHILSVK QFTKDQMSHL FNVAHTLRMM VQKERSLDIL KGKVMASMFY EVSTRTSSSF
     AAAMARLGGA VLSFSEATSS VQKGESLADS VQTMSCYADV IVLRHPQPGA VELAAKHCRR
     PVINAGDGVG EHPTQALLDI FTIREELGTV NGMTITMVGD LKHGRTVHSL ACLLTQYRVS
     LRYVAPPSLR MPPSVRDFVA SRGTKQEEFE SIEEALPDTD VLYMTRIQKE RFGSVQEYEA
     CFGQFILTPH IMTRAKKKMV VMHPMPRVNE ISVEVDSDPR AAYFRQAENG MYIRMALLAT
     VLGRF
//
ID   B2RQG2_MOUSE            Unreviewed;      2025 AA.
AC   B2RQG2;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 31.
DE   SubName: Full=PHD finger protein 3;
GN   Name=Phf3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
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DR   EMBL; BC137913; AAI37914.1; -; mRNA.
DR   IPI; IPI00377615; -.
DR   RefSeq; NP_001074549.1; NM_001081080.1.
DR   UniGene; Mm.194486; -.
DR   ProteinModelPortal; B2RQG2; -.
DR   SMR; B2RQG2; 683-749, 903-1008.
DR   STRING; B2RQG2; -.
DR   PRIDE; B2RQG2; -.
DR   Ensembl; ENSMUST00000088310; ENSMUSP00000085650; ENSMUSG00000048874.
DR   GeneID; 213109; -.
DR   KEGG; mmu:213109; -.
DR   CTD; 213109; -.
DR   MGI; MGI:2446126; Phf3.
DR   HOGENOM; HBG282737; -.
DR   HOVERGEN; HBG039623; -.
DR   InParanoid; B2RQG2; -.
DR   OMA; PRLMAQE; -.
DR   NextBio; 373859; -.
DR   Bgee; B2RQG2; -.
DR   Genevestigator; B2RQG2; -.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006350; P:transcription; IEA:InterPro.
DR   InterPro; IPR012921; SPOC_C.
DR   InterPro; IPR003618; TFIIS_cen_dom.
DR   InterPro; IPR017890; TFS2M.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:1.10.472.30; TFIIS_centre; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF07744; SPOC; 1.
DR   Pfam; PF07500; TFIIS_M; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00510; TFS2M; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   SUPFAM; SSF46942; TFIIS_centre; 1.
DR   PROSITE; PS51321; TFIIS_CENTRAL; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Zinc.
SQ   SEQUENCE   2025 AA;  225542 MW;  5B391558E582C215 CRC64;
     MDIVDTFNHL IPTEHLDDAL FLGSNLENEV CEDFSTSQNV LEDSLKNMLS DKDPMLGSAS
     NQFCLPVLDS NDPNFQMPCS TVVGLDDIMD EGVVKESGND TIDEEELILP NRSLRDRVED
     NSVRSPRKSP RLMAQEQVRS LRQSTIAKRS NAATLSTKKP SGKTLSTSKV GVKPAERCQG
     KEEVYASLKS EHPKESRRSG RHAEQMDVAP EVSASSVDSS VSSCAGMKEE AEFDPKHACN
     NQGEVNVPSP ELDCPLLSET SASVEEKNIE ALMECKAKTN SSPLFKFPVR EDEQSDLVSG
     ELNDTIEGKD AGGKPDQESE EVKFPCEGDQ TAEEPESSDV SSDSACANKN KAEKNEGAEC
     HLELKNTVDI VDKPENSPQR NELETLGYGE DTESNDARLQ STEFNKSDLE EVDACAFEPE
     ASTLENTICD VLDQNSKQLN ITQSIKMETA NLQDDRSGLE PKNIKPKHIK SVTHSKQSMT
     TETPRKTVAA KHEVGHSKTK SNVKAVKRNS GEPEPQPDSQ RPVKVRKKQG DKVWKSQSCN
     SGVKSVKSQA HSVLKRMPQD QNTMQISKPL THPHSDKLHG HSGFSKEPPH PVQTGHLVHS
     SQKQSQKPQQ QAAVGKGSSH VKDEHDHPVS EHLKEDDKLK PRKPDRNLQP RQRRSSRSFS
     LDEPPLFIPD NIATVKKEGS DQTTSIESKY MWTPSKQCGF CKKPHGNRFM VGCGRCDDWF
     HGDCVGLSLS QAQQMGEEDK EYVCVRCCAE EDKKTDILDT EIFEAQAPIE AHSEDKRMEC
     GKLTSSKHAV TDDKHRHSDD PGKHKVKILK RESGEGKTSS DSRDNEIKKW QLAPLRKLSQ
     PHLPRRSSEE KSEKIAKEST ALASTGERVA RSGTHEKQET KKKKMEKGGP NVHPPAATSK
     PSADQIRQSV RHSLKDILMK RLTDSNLKIP EEKAAKVATK IEKELFSFFR DTDAKYKNKY
     RSLMFNLKDP KNNILFKKVL KGEVTPDHLI RMSPEELASK ELAAWRRREN RHTIEMIEKE
     QREVERRPIT KITHKGEIEI ESDAPMKEQE AAIEIQEPSA NKSMEKPDVS EKQKEEVDST
     SKDTTSQHRQ HLFDLNCKIC IGRMAPPIDD LSPKTVKVVV GGARKHSDNE AESLADALSS
     TTNILTSDLF EEEKQESPKS TFSPTPRPEM PGTVEVESTF LARLNFIWKG FINMPSVAKF
     VTKAYPVSGS PEYLTEDLPD SIQVGGRISP QTVWDYVEKI KASGTKEICV VRFTPVTEED
     QISYTLLFAY FSSRKRYGVA ANNMKQVKDM YLIPLGAADK IPHPLVPFDG PGLELHRPNL
     LLGLIIRQKL KRPHSASAGP SHTGETPESA PIVLPPDKKG KMESCTEEAA EEESDFFNSF
     TTVLHKQRNK PSQPLQEDLP TAAEPLMEVT KQEPPKPLRF LPGVLIGWDN QPSTLELANK
     PLPVDDILQS LLGTTGQVYE QAQPLVEQST LKEIPFINDQ ANPKVEKIDK VEVTEGDAKE
     IKVKAENISV STSKNSGEET SSVGSSSISP GPLASLSLRG KPPDVSTEAF LTNLSIPSKQ
     EESVENKERT LKRLLLQDQE NSLQDNRTSS DSPCWPGTGK GGMDGDGSGS GSGSGSGSEG
     PVANTRAPQF INLKRDPRQA AGRSQQTASE SKDAESCRNG DKHAASAPPH NKEPLAEAVG
     GEGKLPSQEK SSCVEQNDDS EAAPNSSSVE NLNSSQAEQA NPSQEDVLTQ NIETVHPFRR
     GSAPTSSRFE GGNTCQSEFP SKSVSFTCRS SSPRASTNFS PMRPQQPNLQ HLKSSPPGFP
     FPGPQNFPPQ NMFGFPPHLS PPLLPPPGFG FPQNPPMVPW PPVHVPGQPQ RMMGPLSQAS
     RYMGPQNFYQ VKDIRRPERR HSDPWGRQDQ QQPDRPFNRG KGDRQRFYSD SHHLKRERHD
     KDWEQESERH RHRDRSQERD RDRKSKEEAA AHKDKERPRL SHGDRAPDGK ASRDGKSADK
     KPDRPKGEDH EKEKERDKSK HKEGEKDRER YHKDRDHTDR VKSKR
//
ID   B2RQL0_MOUSE            Unreviewed;      1170 AA.
AC   B2RQL0;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   05-OCT-2010, entry version 18.
DE   SubName: Full=Nup98 protein;
GN   Name=Nup98;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC137975; AAI37976.1; -; mRNA.
DR   IPI; IPI00464141; -.
DR   UniGene; Mm.439800; -.
DR   ProteinModelPortal; B2RQL0; -.
DR   SMR; B2RQL0; 712-863.
DR   STRING; B2RQL0; -.
DR   MEROPS; S59.001; -.
DR   PRIDE; B2RQL0; -.
DR   Ensembl; ENSMUST00000070165; ENSMUSP00000068530; ENSMUSG00000063550.
DR   MGI; MGI:109404; Nup98.
DR   HOVERGEN; HBG052702; -.
DR   PhylomeDB; B2RQL0; -.
DR   Bgee; B2RQL0; -.
DR   Genevestigator; B2RQL0; -.
DR   GO; GO:0005643; C:nuclear pore; IEA:InterPro.
DR   GO; GO:0006810; P:transport; IEA:InterPro.
DR   InterPro; IPR007230; Peptidase_S59.
DR   Gene3D; G3DSA:3.30.1610.10; Peptidase_S59; 1.
DR   Pfam; PF04096; Nucleoporin2; 1.
DR   SUPFAM; SSF82215; Peptidase_S59; 1.
DR   PROSITE; PS51434; NUP_C; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1170 AA;  123044 MW;  CE240A83D2E1E2AD CRC64;
     MFNKSFGTPF GGSTGGFGTT STFGQNTGFG TTSGGAFGTS AFGSSNNTGG LFGNSQTKPG
     GLFGTSSFSQ PATSTSTGFG FGTSTGTSNS LFGTASTGTS LFSSQNNAFA QNKPTGFGNF
     GTSTSSGGLF GTTNTTSNPF GSTSGSLFGP SSFTAAPTGT TIKFNPPTGT DTMVKAGVST
     NISTKHQCIT AMKEYESKSL EELRLEDYQA NRKGPQNQVG GGTTAGLFGS SPATSSATGL
     FSSSTTNSAF SYGQNKTAFG TSTTGFGTNP GGLFGQQNQQ TTSLFSKPFG QATTTPNTGF
     SFGNTSTLGQ PSTNTMGLFG VTQASQPGGL FGTATNTSTG TAFGTGTGLF GQPNTGFGAV
     GSTLFGNNKL TTFGTSTTSA PSFGTTSGGL FGFGTNNSGS SIFGSKPAAG TLGTGLGTGF
     GTALGAGQAS LFGNNQPKIG GPLGTGAFGA PGFNTSTAIL GFGAPQAPVA LTDPNASAAQ
     QAVLQQHLNS LTYSPFGDSP LFRNPMSDPK KKEERLKPTN PAAQKALTTP THYKLTPRPA
     TRVRPKALQT TGTAKSHLFD GLDDDEPSLA NGAFMPKKSI KKLVLKNLNN SNLFSPVNHD
     SEDLASPSEY PENGERFSFL SKPVDENNQQ DGEDDSLVSR FYTNPIAKPI PQTPESVGNK
     NNSSSNVEDT IVALNMRAAL RNGLEGSSEE TSFHDESLQD DREEIENNAY HIHPAGIVLT
     KVGYYTIPSM DDLAKITNEK GECIVSDFTI GRKGYGSIYF EGDVNLTNLN LDDIVHIRRK
     EVIVYVDDNQ KPPVGEGLNR KAEVTLDGVW PTDKTSRCLI KSPDRLADIN YEGRLEAVSR
     KQGAQFKEYR PETGSWVFKV SHFSKYGLQD SDEEEEEHPP KTTSKKLKTA PLPPAGQATT
     FQMTLNGKPA PPPQSQSPEV EQLGRVVELD SDMVDITQEP VPDSVLEESV PEDQEPVSAS
     THIASSLGIN PHVLQIMKAS LLVDEEDVDA MDQRFGHIPS KGETVQEICS PRLPISASHS
     SKSRSIVGGL LQSKFASGTF LSPSASVQEC RTPRTSSRMN IPSTSPWSVP LPLATVFTVP
     SPAPEVQLKT VGIRRQPGLV PLEKSITYGK GKLLMDMALF MGRSFRVGWG PNWTLANSGE
     QLHGSHELEN HQVADSMEYG FLPNPVAVKS
//
ID   B2RQQ5_MOUSE            Unreviewed;      2464 AA.
AC   B2RQQ5;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   05-OCT-2010, entry version 17.
DE   SubName: Full=Microtubule-associated protein 1B;
GN   Name=Mtap1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
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DR   EMBL; BC138033; AAI38034.1; -; mRNA.
DR   EMBL; BC138034; AAI38035.1; -; mRNA.
DR   IPI; IPI00896700; -.
DR   UniGene; Mm.4173; -.
DR   UniGene; Mm.474609; -.
DR   UniGene; Mm.474896; -.
DR   STRING; B2RQQ5; -.
DR   Ensembl; ENSMUST00000064762; ENSMUSP00000068374; ENSMUSG00000052727.
DR   MGI; MGI:1306778; Mtap1b.
DR   HOVERGEN; HBG052409; -.
DR   InParanoid; B2RQQ5; -.
DR   Bgee; B2RQQ5; -.
DR   Genevestigator; B2RQQ5; -.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005875; C:microtubule associated complex; TAS:MGI.
DR   GO; GO:0005519; F:cytoskeletal regulatory protein binding; TAS:MGI.
DR   GO; GO:0016358; P:dendrite development; IMP:MGI.
DR   GO; GO:0001578; P:microtubule bundle formation; IMP:MGI.
DR   InterPro; IPR000102; MAP1B_neuraxin.
DR   Pfam; PF00414; MAP1B_neuraxin; 6.
DR   PROSITE; PS00230; MAP1B_NEURAXIN; 8.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   2464 AA;  270307 MW;  F7D89A0C98CE3F43 CRC64;
     MATVVVEATE PEPSGSIGNP AASTSPSLSH RFLDSKFYLL VVVGETVTEE HLRRAIGNIE
     LGIRSWDTNL IECNLDQELK LFVSRHSARF SPEVPGQKIL HHRSDVLETV VLINPSDEAV
     STEVRLMITD AARHKLLVLT GQCFENTGEL ILQSGSFSFQ NFIEIFTDQE IGELLSTTHP
     ANKASLTLFC PEEGDWKNSN LDRHNLQDFI NIKLNSASIL PEMEGLSEFT EYLSESVEVP
     SPFDILEPPT SGGFLKLSKP CCYIFPGGRG DSALFAVNGF NMLINGGSER KSCFWKLIRH
     LDRVDSILLT HIGDDNLPGI NSMLQRKIAE LEEERSQGST SNSDWMKNLI SPDLGVVFLN
     VPENLKDPEP NIKMKRSIEE ACFTLQYLNK LSMKPEPLFR SVGNTIEPVI LFQKMGVGKL
     EMYVLNPVKS SKEMQYFMQQ WTGTNKDKAE LILPNGQEVD IPISYLTSVS SLIVWHPANP
     AEKIIRVLFP GNSTQYNILE GLEKLKHLDF LKQPLATQKD LTGQVPTPPV KQVKLKQRAD
     SRESLKPATK PVASKSVRKE SKEETPEVTK TSQVEKTPKV ESKEKVLVKK DKPVKTESKP
     SVTEKEVSSK EEQSPVKAEV AEKQATESKP KVTKDKVVKK EIKTKLEEKK EEKPKKEVVK
     KEDKTPLKKD EKPRKEEVKK EIKKEIKKEE RKELKKEVKK ETPLKDAKKE VKKEEKKEVK
     KEEKEPKKEI KKISKDIKKS TPLSDTKKPS ALKPKVAKKE ESTKKEPLAA GKLKDKGKVK
     VIKKEGKTTE AAATAVGTAA TTAAVVAAAG IAASGPVKEL EAERSLMSSP EDLTKDFEEL
     KAEEIDVAKD IKPQLELIED EEKLKETQPG EAYVIQKETE VSKGSAESPD EGITTTEGEG
     ECEQTPEELE PVEKQGVDDI EKFEDEGAGF EESSETGDYE EKAETEEAEE PEEDGEDNAS
     GSASKHSPTE DDESAKAEAD VHLKEKRESV VSGDDRAEED MDDVLEKGEA EQSEEEGEEE
     DKAEDAREEG YEPDKTEAED YVMAVADKAA EAGVTEEQYG YLGTSAKQPG IQSPSREPAS
     SIHDETLPGG SESEATASDE ENREDQPEEF TATSGYTQST IEISSEPTPM DEMSTPRDVM
     SDETNNEETE SPSQEFVNIT KYESSLYSQE YSKPAVASFN GLSEGSKTDA TDGKDYNASA
     STISPPSSME EDKFSKSALR DAYCSEEKEL KASAELDIKD VSDERLSPAK SPSLSPSPPS
     PIEKTPLGER SVNFSLTPNE IKVSAEGEAR SVSPGVTQAV VEEHCASPEE KTLEVVSPSQ
     SVTGSAGHTP YYQSPTDEKS SHLPTEVTEK PQAVPVSFEF SEAKDENERA SLSPMDEPVP
     DSESPVEKVL SPLRSPPLLG SESPYEDFLS ADSKVLGRRS ESPFEGKNGK QGFPDRESPV
     SDLTSTGLYQ DKQEEKSTGF IPIKEDFGPE KKTSDVETMS SQSALALDER KLGGDVSPTQ
     IDVSQFGSFK EDTKMSISEG TVSDKSATPV DEGVAEDTYS HMEGVASVST ASVATSSFPE
     PTTDDVSPSL HAEVGSPHST EVDDSLSVSV VQTPTTFQET EMSPSKEECP RPMSISPPDF
     SPKTAKSRTP VQDHRSEQSS MSIEFGQESP EHSFAMDFSR QSPDHPTLGA SVLHITENGP
     TEVDYSPSDI QDSSLSHKIP PTEEPSYTQD NDLSELISVS QVEASPSTSS AHTPSQIASP
     LQEDTLSDVV PPREMSLYAS LASEKVQSLE GEKLSPKSDI SPLTPRESSP LYSPGFSDST
     SAAKETAAAH QASSSPPIDA ATAEPYGFRS SMLFDTMQHH LALNRDLTTS SVEKDSGGKT
     PGDFNYAYQK PENAAGSPDE EDYDYESQEK TIRTHDVGGY YYEKTERTIK SPCDSGYSYE
     TIEKTTKTPE DGGYTCEITE KTTRTPEEGG YSYEISEKTT RTPEVSGYTY EKTERSRRLL
     DDISNGYDDT EDGGHTLGDC SYSYETTEKI TSFPESESYS YETSTKTTRS PDTSAYCYET
     MEKITKTPQA STYSYETSDR CYTTEKKSPS EARQDVDLCL VSSCEFKHPK TELSPSFINP
     NPLEWFAGEE PTEESEKPLT QSGGAPPPSG GKQQGRQCDE TPPTSVSESA PSQTDSDVPP
     ETEECPSITA DANIDSEDES ETIPTDKTVT YKHMDPPPAP MQDRSPSPRH PDVSMVDPDA
     LAVDQNLGKA LKKDLKEKTK TKKPGTKTKS SSPVKKGDGK SKPLAASPKP GALKESSDKV
     SRVASPKKKE SVEKATKTTT TPEVKATRGE EKDKETKNAA NASASKSAKT ATTGPGTTKT
     AKSSTVPPGL PVYLDLCYIP NHSNSKNVDV EFFKRVRSSY YVVSGNDPAA EEPSRAVLDA
     LLEGKAQWGS NMQVTLIPTH DSEVMREWYQ ETHEKQQDLN IMVLASSSTV VMQDESFPAC
     KIEL
//
ID   B2RQR5_MOUSE            Unreviewed;      1093 AA.
AC   B2RQR5;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   11-JAN-2011, entry version 21.
DE   SubName: Full=Small G protein signaling modulator 1;
GN   Name=Sgsm1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; BC138049; AAI38050.1; -; mRNA.
DR   EMBL; BC138050; AAI38051.1; -; mRNA.
DR   IPI; IPI00938490; -.
DR   RefSeq; NP_766306.2; NM_172718.3.
DR   UniGene; Mm.200203; -.
DR   ProteinModelPortal; B2RQR5; -.
DR   SMR; B2RQR5; 8-183, 880-1085.
DR   STRING; B2RQR5; -.
DR   Ensembl; ENSMUST00000048112; ENSMUSP00000046544; ENSMUSG00000042216.
DR   GeneID; 52850; -.
DR   KEGG; mmu:52850; -.
DR   CTD; 52850; -.
DR   MGI; MGI:107320; Sgsm1.
DR   HOVERGEN; HBG108483; -.
DR   InParanoid; B2RQR5; -.
DR   OMA; HRMLHRD; -.
DR   Bgee; B2RQR5; -.
DR   Genevestigator; B2RQR5; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005097; F:Rab GTPase activator activity; IEA:InterPro.
DR   GO; GO:0032313; P:regulation of Rab GTPase activity; IEA:InterPro.
DR   InterPro; IPR000195; RabGAP/TBC_dom.
DR   InterPro; IPR004012; Run.
DR   Pfam; PF02759; RUN; 1.
DR   Pfam; PF00566; TBC; 1.
DR   SMART; SM00593; RUN; 1.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; RabGAP_TBC; 2.
DR   PROSITE; PS50826; RUN; 1.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1093 AA;  123267 MW;  22E28FD26C703F51 CRC64;
     MASVPAEAET RQRLLRTVKK EVKQIMEEAV TRKFVHEDSS HIISFCAAVE ACVLHGLRRR
     AAGFLRSNKI AALFMKVGKG FPPAEELSRK VQELEQLIES ARNQIQGLQE NVRKLPKLPN
     LSPLAIKHLW IRTALFERVL DKIVHYLVEN SSKYYEKEAL LMDPVDGPIL ASLLVGPCAL
     EYTKMKTADH FWTDPSADEL VQRHRIHSSH LRQDSPTKRP ALCIQKRHSS GSMDDRPSIS
     ARDYVESLHQ NSRATLLYGK NNVLVQPRDD MEAVPGYLSL HQTADVMTLK WTPNQLMNGS
     VGDLDYEKSV YWDYAVTIRL EEIVYLHCHQ QVDSGGTVVL VSQDGIQRPP FRFPKGGHLL
     QFLSCLENGL LPHGQLDPPL WSQRGKGKVF PKLRKRSPQG SSESTSSDKE DDEATDYVFR
     IIYPGTQSEF VPQDLMDVSM NNLPPLWQPS PRKSSCSSCS QSGSADGGST NGCNHERAPL
     KLLCDNMKYQ ILSRAFYGWL AYCRHLSTVR THLSALVNHM IVSPDLPCDA GQGLTASIWE
     KYIQDSTTYP EQELLRLIYY GGVQPEIRRA VWPFLLGHYQ FGMTEMERKE VDEQIHACYA
     QTMSEWLGCE AIVRQRERES HAAALAKCSS GASLDSHLHR MLHRDSTISN ESSQSCSSGR
     QNLRLQSDSS SSTQVFESVD EVEQTEAEGR SEEKHPKIPN GNPANGTCSP DSGHPSSHNF
     SSGLSEHSEP SLSTEDSVLD AQRSLPAVFR PGDSSVEDGQ SSEATTSRDE APREELAVQD
     SLESDLLANE SLEEFMSIPG SLDVALPEKD GAVMDGWPGE ADKPSRADSE DNLSEEPEME
     SLFPALASLA VTSSANNEAS PVSSSGVTYS PELLDLYTVN LHRIEKDVQR CDRSYWYFTA
     ANLEKLRNIM CSYIWQHIEI GYVQGMCDLL APLLVILDDE ALAFSCFTEL MKRMNQNFPH
     GGAMDTHFAN MRSLIQILDS ELFELMHQNG DYTHFYFCYR WFLLDFKREL VYDDVFSVWE
     TIWAAKHVSS AHYVLFIALA LVEVYRDIIL ENNMDFTDII KFFNEMAERH NAKQILQLAR
     DLVHKVQILI ENK
//
ID   B2RQR8_MOUSE            Unreviewed;       763 AA.
AC   B2RQR8;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   11-JAN-2011, entry version 24.
DE   SubName: Full=Endothelin converting enzyme 2;
GN   Name=Ece2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
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DR   EMBL; BC138052; AAI38053.1; -; mRNA.
DR   EMBL; BC138053; AAI38054.1; -; mRNA.
DR   IPI; IPI00867751; -.
DR   RefSeq; NP_647454.2; NM_139293.2.
DR   UniGene; Mm.263319; -.
DR   ProteinModelPortal; B2RQR8; -.
DR   SMR; B2RQR8; 91-763.
DR   STRING; B2RQR8; -.
DR   MEROPS; M13.003; -.
DR   PRIDE; B2RQR8; -.
DR   Ensembl; ENSMUST00000003898; ENSMUSP00000003898; ENSMUSG00000022842.
DR   GeneID; 107522; -.
DR   KEGG; mmu:107522; -.
DR   CTD; 107522; -.
DR   MGI; MGI:1101356; Ece2.
DR   HOVERGEN; HBG005554; -.
DR   NextBio; 358964; -.
DR   Bgee; B2RQR8; -.
DR   Genevestigator; B2RQR8; -.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR000718; Peptidase_M13.
DR   InterPro; IPR018497; Peptidase_M13_C.
DR   InterPro; IPR008753; Peptidase_M13_N.
DR   PANTHER; PTHR11733; Peptidase_M13; 1.
DR   Pfam; PF01431; Peptidase_M13; 1.
DR   Pfam; PF05649; Peptidase_M13_N; 1.
DR   PRINTS; PR00786; NEPRILYSIN.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   763 AA;  86231 MW;  10FB30AFEF8AE9E2 CRC64;
     MNVALHELGG GGSMVEYKRA KLRDEESPEI TVEGRATRDS LEVGFQKRTR QLFGSHTQLE
     LVLAGLILVL AALLLGCLVA LWVHRDPAHS TCVTEACIRV AGKILESLDR GVSPCQDFYQ
     FSCGGWIRRN PLPNGRSRWN TFNSLWDQNQ AILKHLLENT TFNSSSEAER KTRSFYLSCL
     QSERIEKLGA KPLRDLIDKI GGWNITGPWD EDSFMDVLKA VAGTYRATPF FTVYVSADSK
     SSNSNIIQVD QSGLFLPSRD YYLNRTANEK VLTAYLDYMV ELGVLLGGQP TSTREQMQQV
     LELEIQLANI TVPQDQRRDE EKIYHKMSIS ELQALAPAVD WLEFLSFLLS PLELGDSEPV
     VVYGTEYLQQ VSELINRTEP SILNNYLIWN LVQKTTSSLD QRFETAQEKL LETLYGTKKS
     CTPRWQTCIS NTDDALGFAL GSLFVKATFD RQSKEIAEGM INEIRSAFEE TLGDLVWMDE
     KTRLAAKEKA DAIYDMIGFP DFILEPKELD DVYDGYEVSE DSFFQNMLNL YNFSAKVMAD
     QLRKPPSRDQ WSMTPQTVNA YYLPTKNEIV FPAGILQAPF YAHNHPKALN FGGIGVVMGH
     ELTHAFDDQG REYDKEGNLR PWWQNESLTA FQNHTACMEE QYSQYQVNGE RLNGLQTLGE
     NIADNGGLKA AYNAYKAWLR KHGEEQPLPA VGLTNHQLFF VGFAQVWCSV RTPESSHEGL
     VTDPHSPARF RVLGTLSNSR DFLRHFGCPV GSPMNPGQLC EVW
//
ID   B2RQX9_MOUSE            Unreviewed;       791 AA.
AC   B2RQX9;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 23.
DE   RecName: Full=Transporter;
GN   Name=Slc6a5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF)
CC       family.
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DR   EMBL; BC138125; AAI38126.1; -; mRNA.
DR   EMBL; BC138126; AAI38127.1; -; mRNA.
DR   IPI; IPI00928142; -.
DR   RefSeq; NP_001139485.1; NM_001146013.1.
DR   RefSeq; NP_683733.2; NM_148931.3.
DR   UniGene; Mm.207053; -.
DR   ProteinModelPortal; B2RQX9; -.
DR   SMR; B2RQX9; 185-725.
DR   STRING; B2RQX9; -.
DR   Ensembl; ENSMUST00000056442; ENSMUSP00000058699; ENSMUSG00000039728.
DR   Ensembl; ENSMUST00000107605; ENSMUSP00000103230; ENSMUSG00000039728.
DR   GeneID; 104245; -.
DR   KEGG; mmu:104245; -.
DR   CTD; 104245; -.
DR   MGI; MGI:105090; Slc6a5.
DR   HOVERGEN; HBG071421; -.
DR   InParanoid; B2RQX9; -.
DR   PhylomeDB; B2RQX9; -.
DR   Bgee; B2RQX9; -.
DR   Genevestigator; B2RQX9; -.
DR   GO; GO:0005887; C:integral to plasma membrane; IEA:InterPro.
DR   GO; GO:0005328; F:neurotransmitter:sodium symporter activity; IEA:InterPro.
DR   InterPro; IPR000175; Na/ntran_symport.
DR   PANTHER; PTHR11616; Na/ntran_symport; 1.
DR   Pfam; PF00209; SNF; 1.
DR   PRINTS; PR00176; NANEUSMPORT.
DR   PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR   PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
DR   PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Symport; Transmembrane; Transmembrane helix; Transport.
SQ   SEQUENCE   791 AA;  87029 MW;  3400501C93EC4421 CRC64;
     MNKQPANILE AAVPGHRDSP RAPRTSPEQD LPAEAPTATV QPPRVPRSAS TGAQTFQSAD
     ARACEAQQSG VGFCNLSSPR AQATSAALRD LSEGHSAQAN PPSGPAGAGN ALHCKIPALR
     GPEEDANVSV GKGTLEHNNT PAVGWVNMSQ STVVLGTDGI ASVLPGSVAT TTIPEDEQGD
     ENKARGNWSS KLDFILSMVG YAVGLGNVWR FPYLAFQNGG GAFLIPYLMM LALAGLPIFF
     LEVSLGQFAS QGPVSVWKAI PALQGCGIAM LIISVLIAIY YNVIICYTLF YLFASFVSVL
     PWGSCNNPWN TPECKDKTKL LLDSCVIGDH PKIQIKNSTF CMTAYPNLTM VNFTSQTNKT
     FVSGSEEYFK YFVLKISAGI EYPGEIRWPL AFCLFLAWVI VYASLAKGIK SSGKVVYFTA
     TFPYVVLVIL LIRGVTLPGA GAGIWYFITP KWEKLTDATV WKDAATQIFF SLSAAWGGLI
     TLSSYNKFHN NCYRDTLIVT CTNSATSIFA GFVIFSVIGF MANERKVNIE NVADQGPGIA
     FVVYPEALTR LPLSPFWAII FFLMLLTLGL DTMFATIETI VTSISDEFPK YLRTHKPVFT
     LGCCICFFIM GFPMITQGGI YMFQLVDTYA ASYALVIIAI FELVGISYVY GLQRFCEDIE
     MMIGFKPNIF WKVCWAFVTP TILTFILCFS FYQWEPMTYG SYRYPNWSMV LGWLMLACSV
     IWIPIMFVIK MYLAPGRFIE RLKLVCSPQP DWGPFLAQHR GERYKNMIDP LGTSSLGLKL
     PVKDLELGTQ C
//
ID   YTDC2_MOUSE             Reviewed;        1445 AA.
AC   B2RR83;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 27.
DE   RecName: Full=Probable ATP-dependent RNA helicase YTHDC2;
DE            EC=3.6.4.13;
GN   Name=Ythdc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily.
CC   -!- SIMILARITY: Contains 2 ANK repeats.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 R3H domain.
CC   -!- SIMILARITY: Contains 1 YTH domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; BC138263; AAI38264.1; -; mRNA.
DR   EMBL; BC171951; AAI71951.1; -; mRNA.
DR   IPI; IPI00343249; -.
DR   RefSeq; NP_001156485.1; NM_001163013.1.
DR   UniGene; Mm.244482; -.
DR   ProteinModelPortal; B2RR83; -.
DR   SMR; B2RR83; 63-121, 198-1081, 1303-1436.
DR   PRIDE; B2RR83; -.
DR   Ensembl; ENSMUST00000037763; ENSMUSP00000048340; ENSMUSG00000034653.
DR   GeneID; 240255; -.
DR   KEGG; mmu:240255; -.
DR   CTD; 240255; -.
DR   MGI; MGI:2448561; Ythdc2.
DR   HOGENOM; HBG444787; -.
DR   InParanoid; B2RR83; -.
DR   OrthoDB; EOG4JWVCN; -.
DR   NextBio; 384522; -.
DR   Bgee; B2RR83; -.
DR   Genevestigator; B2RR83; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR011709; DUF1605.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR001374; R3H_ss-bd.
DR   InterPro; IPR007275; YTH_domain.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF07717; DUF1605; 1.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF01424; R3H; 1.
DR   Pfam; PF04146; YTH; 1.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; FALSE_NEG.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51061; R3H; 1.
DR   PROSITE; PS50882; YTH; 1.
PE   2: Evidence at transcript level;
KW   ANK repeat; ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1   1445       Probable ATP-dependent RNA helicase
FT                                YTHDC2.
FT                                /FTId=PRO_0000378275.
FT   DOMAIN       53    121       R3H.
FT   DOMAIN      218    384       Helicase ATP-binding.
FT   REPEAT      521    553       ANK 1.
FT   REPEAT      554    586       ANK 2.
FT   DOMAIN      627    799       Helicase C-terminal.
FT   DOMAIN     1303   1433       YTH.
FT   NP_BIND     231    238       ATP (By similarity).
FT   MOTIF       331    334       DEAH box.
FT   COMPBIAS     16     50       Gly-rich.
FT   COMPBIAS   1263   1296       Ser-rich.
FT   MOD_RES    1104   1104       Phosphoserine (By similarity).
FT   MOD_RES    1278   1278       Phosphoserine (By similarity).
FT   MOD_RES    1282   1282       Phosphoserine (By similarity).
FT   MOD_RES    1284   1284       Phosphoserine (By similarity).
FT   MOD_RES    1288   1288       Phosphoserine (By similarity).
FT   MOD_RES    1294   1294       Phosphoserine (By similarity).
FT   MOD_RES    1296   1296       Phosphoserine (By similarity).
SQ   SEQUENCE   1445 AA;  161092 MW;  A693BF57FEAF7511 CRC64;
     MSRPSSVSPR PPAPSGGGTG GGGGGSGGGG GGGGGGPASC GPGGGGRAKG LKDIRIDEEV
     KIAVNIALER FRYGDQREME FPSSLTSTER AFIHRLSQSL GLVSKSKGKG ANRYLTVKKK
     DGSETAHAMM TCNLTHNTKH AVRSLIQRFP VTNKERTELL PKTERGNVFA VEAENREMSK
     TSGRLNNGIP QVPVKRGESE FDSFRQSLPV FEKQEEIVKI IKENKVVLIV GETGSGKTTQ
     IPQFLLDDCF KNGIPCRIFC TQPRRLAAIA VAERVAAERR ERIGQTIGYQ IRLESRVSPK
     TLLTFCTNGV LLRTLMAGDS TLSTVTHVIV DEVHERDRFS DFLLTKLRDL LQKHPTLKLI
     LSSAALDVNL FIRYFGSCPV IYIQGRPFEV KEMFLEDILR TTGYTNKEML KYKKEKQREE
     KQQTTLTEWY SAQENTFKPE SQRQRAVASV SEEYDLLDDG GDAVFSQLTE KDVNCLEPWL
     IKEMDACLSD IWLHKDVDAF AQVFHLILTE NVSVDYRHSE TSATALMVAA GRGFTSQVEQ
     LISMGANVHS KASNGWMALD WAKHFGQTEI VDLLESYSAS LEFGNLDESS LVQTNGNDLS
     AEDRELLKAY HHSFDDEKVD LDLIMHLLYN ICHSCDAGAI LIFLPGYDEI VGLRDRILFD
     DKRFADNTHR YQVFMLHSNM QTSDQKKVLK NPPAGVRKII LSTNIAETSI TVNDVVFVID
     SGKVKEKSFD ALNFVTMLKM VWISKASAIQ RKGRAGRCRP GICFRLFSRL RFQNMLEFQT
     PELLRMPLQE LCLHTKLLAP VNCTIADFLM KAPEPPPALI VRNAVQMLKT IDAMDAWEDL
     TELGYHLADL PVEPHLGKMV LCAVVLKCLD PILTIACTLA YRDPFVLPTQ ASQKRAAMLC
     RKRFTAGTFS DHMALLRAFQ AWQKARSDGW ERAFCEKNFL SQATMEIIIG MRTQLLGQLR
     ASGFVRARGG GDIRDVNTNS ENWAVVKAAL VAGMYPNLVH VDRENVILTG PKEKKVRFHP
     TSVLSQPQYK KIPPANGQAA AIQALPTDWL IYDEMTRAHR IANIRCCSAV TPVTVLVFCG
     PARLASNALQ EPSSFRADGI PNDSSDSEME DRTTANLAAL KLDEWLNFKL EPEAASLLLQ
     LRQKWHSLFL RRMRAPSKPW SQVDEATIRA IIAVLSTEEQ SAGLQQPSGI GQRPRPMSSE
     ELPLASSWRS NNSRKSTADT EFADGSTTGE RVLMKSPSPA LHPPQKYKDR GILHPKRSTD
     DRSDQSSVKS TDSSSYPSPC ASPSPPSSGK GSKSPSPRPN MPIRYFIMKS SNLRNLEISQ
     QKGIWSTTPS NERKLNRAFW ESSMVYLVFS VQGSGHFQGF SRMSSEIGRE KSQDWGSAGL
     GGVFKVEWIR KESLPFQFAH HLLNPWNDNK KVQISRDGQE LEPQVGEQLL QLWERLPLGE
     KTTSD
//
ID   B2RRD7_MOUSE            Unreviewed;      1212 AA.
AC   B2RRD7;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 25.
DE   SubName: Full=Bromodomain and PHD finger containing, 1;
DE   SubName: Full=Brpf1 protein;
GN   Name=Brpf1; ORFNames=mCG_132959;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC138361; AAI38362.1; -; mRNA.
DR   EMBL; CH466523; EDK99448.1; -; Genomic_DNA.
DR   IPI; IPI00856686; -.
DR   UniGene; Mm.356059; -.
DR   UniGene; Mm.449928; -.
DR   UniGene; Mm.474132; -.
DR   ProteinModelPortal; B2RRD7; -.
DR   SMR; B2RRD7; 269-327, 632-739, 1079-1195.
DR   STRING; B2RRD7; -.
DR   PRIDE; B2RRD7; -.
DR   Ensembl; ENSMUST00000113122; ENSMUSP00000108747; ENSMUSG00000001632.
DR   MGI; MGI:1926033; Brpf1.
DR   HOVERGEN; HBG004895; -.
DR   Bgee; B2RRD7; -.
DR   Genevestigator; B2RRD7; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR019542; Enhancer_of_polycomb-like_N.
DR   InterPro; IPR000313; PWWP.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:1.20.920.10; Bromodomain; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF10513; EPL1; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00249; PHD; 2.
DR   SMART; SM00293; PWWP; 1.
DR   SMART; SM00355; ZnF_C2H2; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS50812; PWWP; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Zinc.
SQ   SEQUENCE   1212 AA;  137310 MW;  2FC14ECF8FF5DECE CRC64;
     MGVDFDVKTF CHNLRATKPP YECPVETCRK VYKSYSGIEY HLYHYDHDSP PPPQQTPLRK
     HKKKGRQSRP ANKQSPSPSE VSQSPGREVM SYAQAQRMVE VDLHGRVHRI SIFDNLDVVS
     EDEEAPEEAP ENGSNKENTE TPAATPKSGK HKNKEKRKDS NHHHHSAPAS AAPKLPEVVY
     RELEQDTPDA PPRPTSYYRY IEKSAEELDE EVEYDMDEED YIWLDIMNER RKTEGVSPIP
     QEIFEYLMDR LEKESYFESH NKGDPNALVD EDAVCCICND GECQNSNVIL FCDMCNLAVH
     QECYGVPYIP EGQWLCRRCL QSPSRAVDCA LCPNKGGAFK QTDDGRWAHV VCALWIPEVC
     FANTVFLEPI DSIEHIPPAR WKLTCYICKQ RGSGACIQCH KANCYTAFHV TCAQQAGLYM
     KMEPVRETGA NGTSFSVRKT AYCDIHTPPG SARRLPALSH SEGEEEEDEE EDEGKSWSSE
     KVKKAKAKSR IKMKKARKIL AEKRAAAPVV SVPCIPPHRL SKITNRLTIQ RKSQFMQRLH
     SYWTLKRQSR NGVPLLRRLQ THLQSQRNCE QVGRDSDDKN WALKEQLKSW QRLRHDLERA
     RLLVELIRKR EKLKRETIKI QQIAMEMQLT PFLILLRKTL EQLQEKDTGN IFSEPVPLSE
     VPDYLDHIKK PMDFFTMKQN LEAYRYLNFD DFEEDFNLIV SNCLKYNAKD TIFYRAAVRL
     REQGGAVLRQ ARRQAEKMGI DFETGMHIPH NLAGDEVSHH TEDVEEERLV LLENQKHLPV
     EEQLKLLLER LDEVNASKQS VGRSRRAKMI KKEMTALRRK LAHQRETGRD GPERHGPSGR
     GNLTPHPAAC DKDGQTDSAA EESSSQETSK GLGPNMSSTP AHEVGRRTSV LFSKKNPKTA
     GPPKRPGRPP KNRESQMTPS HGGSPVGPPQ LPIMGSLRQR KRGRSPRPSS SSDSDSDKST
     EDPPMDLPAN GFSSGNQPVK KSFLVYRNDC NLPRSSSDSE SSSSSSSSAA SDRTSTTPSK
     QGRGKPSFSR GTFPEDSSED TSGTENEAYS VGTGRGVGHS MVRKSLGRGA GWLSEDEDSP
     LDALDLVWAK CRGYPSYPAL IIDPKMPREG MFHHGVPIPV PPLEVLKLGE QMTQEAREHL
     YLVLFFDNKR TWQWLPRTKL VPLGVNQDLD KEKMLEGRKS NIRKSVQIAY HRALQHRSKV
     QGEQSSETSD SD
//
ID   B2RRE2_MOUSE            Unreviewed;      2047 AA.
AC   B2RRE2;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 25.
DE   SubName: Full=Myo18a protein;
GN   Name=Myo18a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 myosin head-like domain.
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DR   EMBL; BC138366; AAI38367.1; -; mRNA.
DR   IPI; IPI00649326; -.
DR   UniGene; Mm.341248; -.
DR   UniGene; Mm.476162; -.
DR   ProteinModelPortal; B2RRE2; -.
DR   SMR; B2RRE2; 354-1222.
DR   STRING; B2RRE2; -.
DR   Ensembl; ENSMUST00000108376; ENSMUSP00000104013; ENSMUSG00000000631.
DR   MGI; MGI:2667185; Myo18a.
DR   HOGENOM; HBG402832; -.
DR   HOVERGEN; HBG052543; -.
DR   InParanoid; B2RRE2; -.
DR   Bgee; B2RRE2; -.
DR   Genevestigator; B2RRE2; -.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:motor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR002928; Myosin_tail.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF00063; Myosin_head; 2.
DR   Pfam; PF01576; Myosin_tail_1; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 1.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Coiled coil; Motor protein; Myosin; Nucleotide-binding.
SQ   SEQUENCE   2047 AA;  232138 MW;  BDB665AF95B5A54C CRC64;
     MFNLMKKDKD KDGGRKEKKE KKEKKERMSA AELRSLEEMS MRRGFFNLNR SSKRESKTRL
     EISNPIPIKV ASGSDLHLTD IDSDSNRGSI ILDSGHLSTA SSSDDLKGEE GSFRGSVLQR
     AAKFGSLAKQ NSQMIVKRFS FSQRSRDESA SETSTPSEHS AAPSPQVEVR TLEGQLMQHP
     GLGIPRPGPR SRVPELVTKR FPADLRLPAL VPPPPPALRE LELQRRPTGD FGFSLRRTTM
     LDRAPEGQAY RRVVHFAEPG AGTKDLALGL VPGDRLVEIN GQNVENKSRD EIVEMIRQSG
     DSVRLKVQPI PELSELSRSW LRTGEGHRRE PADLDPEAAS PAYSQAKTEE QIAAEEAWYE
     TEKVWLVHRD GFSLASQLKS EELSLPEGKA RVKLDHDGAI LDVDEDDIEK ANAPSCDRLE
     DLASLVYLNE SSVLHTLRQR YGASLLHTYA GPSLLVLSTR GAPAVYSEKV MHMFKGCRRE
     DMAPHIYAVA QTAYRAMLMS RQDQSIVLLG SSGSGKTTSF QHLVQYLATI AGTSGTKVFS
     VEKWQALSTL LEAFGNSPTI MNGSATRFSQ ILSLDFDQAG QVASASIQTM LLEKLRVARR
     PASEATFNVF YYLLACGDAT LRTELHLNHL AENNVFGIVP LSKPEEKQKA AQQFSKLQAA
     MKVLAISPEE QKTCWLILAS IYHLGAAGAT KEAAEAGRKQ FARHEWAQKA AYLLGCSLEE
     LSSAIFKHQL KGGTLQRSTS FRQGPEESGL GEGTKLSALE CLEGMASGLY SELFTLLISL
     VNRALKSSQH SLCSMMIVDT PGFQNPEWGG SARGASFEEL CHNYAQDRLQ RLFHERTFLQ
     ELERYKEDNI ELAFDDLEPV ADDSVAAVDQ ASHLVRSLAH ADEARGLLWL LEEEALVPGA
     TEDALLDRLF SYYGPQEGDK KGQSPLLRSS KPRHFLLGHS HGTNWVEYNV AGWLNYTKQN
     PATQNAPRLL QDSQKKIISN LFLGRAGSAT VLSGSIAGLE GGSQLALRRA TSMRKTFTTG
     MAAVKKKSLC IQIKLQVDAL IDTIKRSKMH FVHCFLPVAE GWPGEPRSAS SRRVSSSSEL
     DLPPGDPCEA GLLQLDVSLL RAQLRGSRLL DAMRMYRQGY PDHMVFSEFR RRFDVLAPHL
     TKKHGRNYIV VDEKRAVEEL LESLDLEKSS CCLGLSRVFF RAGTLARLEE QRDEQTSRHL
     TLFQAACRGY LARQHFKKRK IQDLAIRCVQ KNIKKNKGVK DWPWWKLFTT VRPLIQVQLS
     EEQIRNKDEE IQQLRSKLEK VEKERNELRL SSDRLETRIS ELTSELTDER NTGESASQLL
     DAETAERLRT EKEMKELQTQ YDALKKQMEV MEMEVMEARL IRAAEINGEV DDDDAGGEWR
     LKYERAVREV DFTKKRLQQE LEDKMEVEQQ SRRQLERRLG DLQADSDESQ RALQQLKKKC
     QRLTAELQDT KLHLEGQQVR NHELEKKQRR FDSELSQAHE ETQREKLQRE KLQREKDMLL
     AEAFSLKQQM EEKDLDIAGF TQKVVSLEAE LQDISSQESK DEASLAKVKK QLRDLEAKVK
     DQEEELDEQA GSIQMLEQAK LRLEMEMERM RQTHSKEMES RDEEVEEARQ SCQKKLKQME
     VQLEEEYEDK QKALREKREL ESKLSTLSDQ VNQRDFESEK RLRKDLKRTK ALLADAQIML
     DHLKNNAPSK REIAQLKNQL EESEFTCAAA VKARKAMEVE MEDLHLQIDD IAKAKTALEE
     QLSRLQREKN EIQNRLEEDQ EDMNELMKKH KAAVAQASRD MAQMNDLQAQ IEESNKEKQE
     LQEKLQALQS QVEFLEQSMV DKSLVSRQEA KIRELETRLE FEKTQVKRLE NLASRLKETM
     EKLTEERDQR AAAENREKEQ NKRLQRQLRD TKEEMSELAR KEAEASRKKH ELEMDLESLE
     AANQSLQADL KLAFKRIGDL QAAIEDEMES DENEDLINSE GDSDVDSELE DRVDGVKSWL
     SKNKGPSKAP SDDGSLKSSS PTSHWKPLAP DPSDDEHDPV DSISRPRFSH SYLSDSDTEA
     KLTETSA
//
ID   OTUD4_MOUSE             Reviewed;        1107 AA.
AC   B2RRE7; B7ZNI5; Q80TL3; Q9CUN2;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 24.
DE   RecName: Full=OTU domain-containing protein 4;
GN   Name=Otud4; Synonyms=Kiaa1046;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-1107.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 930-1107.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-438, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1000; SER-1005; SER-1016
RP   AND SER-1017, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1016 AND SER-1017, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1016 AND SER-1017, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SIMILARITY: Contains 1 OTU domain.
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CC   -----------------------------------------------------------------------
DR   EMBL; BC138373; AAI38374.1; -; mRNA.
DR   EMBL; BC145259; AAI45260.1; -; mRNA.
DR   EMBL; AK122429; BAC65711.1; -; mRNA.
DR   EMBL; AK015275; BAB29777.1; -; mRNA.
DR   IPI; IPI00137459; -.
DR   RefSeq; NP_001074633.1; NM_001081164.1.
DR   UniGene; Mm.34348; -.
DR   ProteinModelPortal; B2RRE7; -.
DR   SMR; B2RRE7; 25-153.
DR   MEROPS; C85.002; -.
DR   PRIDE; B2RRE7; -.
DR   Ensembl; ENSMUST00000048457; ENSMUSP00000035541; ENSMUSG00000036990.
DR   GeneID; 73945; -.
DR   KEGG; mmu:73945; -.
DR   CTD; 73945; -.
DR   MGI; MGI:1098801; Otud4.
DR   GeneTree; ENSGT00530000063508; -.
DR   HOGENOM; HBG283477; -.
DR   HOVERGEN; HBG082091; -.
DR   InParanoid; B2RRE7; -.
DR   OrthoDB; EOG4T4CTP; -.
DR   Bgee; B2RRE7; -.
DR   Genevestigator; B2RRE7; -.
DR   InterPro; IPR003323; OTU.
DR   Pfam; PF02338; OTU; 1.
DR   PROSITE; PS50802; OTU; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein.
FT   CHAIN         1   1107       OTU domain-containing protein 4.
FT                                /FTId=PRO_0000394458.
FT   DOMAIN       34    155       OTU.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     438    438       Phosphotyrosine.
FT   MOD_RES     442    442       Phosphoserine (By similarity).
FT   MOD_RES     554    554       Phosphoserine (By similarity).
FT   MOD_RES     935    935       Phosphoserine (By similarity).
FT   MOD_RES    1000   1000       Phosphoserine.
FT   MOD_RES    1005   1005       Phosphoserine.
FT   MOD_RES    1016   1016       Phosphoserine.
FT   MOD_RES    1017   1017       Phosphoserine.
FT   CONFLICT    290    290       Missing (in Ref. 1; AAI45260).
SQ   SEQUENCE   1107 AA;  123055 MW;  746B6BC8589FA672 CRC64;
     MEAAVGAPDG VDQGGVGPLE DETPMDAYLR KLGLYRKLVA KDGSCLFRAV AEQVLHSQSR
     HVEVRMACIR YLRENREKFE AFIEGSFEEY LKRLENPQEW VGQVEISALS LMYRKDFVIY
     QEPNVSPSHV TENNFPEKVL LCFSNGNHYD IVYPITYKDS SAMCQSLLYE LLYEKVFKTD
     VSKIMMGLEA SEVAEESNSE ISDSEDDSCK SKSTAATDVN GFKPSGSENP KNNGNSADLP
     LSRKVLKSLN PAVYRNVEYE IWLKSKQAQQ KRDYSIAAGL QYEVGDKCHQ VRLDHNGKLS
     NADIHGVHSE NGLVLSEELG KKHTPKNLKP PPPESWNTVS GKKMKKPNSG QNFHSDTDYR
     GPKNLNKPIK APSALPPRLQ HPSSGVRQHA FSSHSTGSQS QKSSSEHKNL SRMPSQITRK
     PDRERAEDFD HVSRESYYFG LSPEERREKQ AIEESRLLYE IQNRDEQAFP ALSSSSVSQS
     PSQNSNACVP RKSSHARDRK GSMRRADAEE RKDKDSLRGH THVDKKPEPS TLEISDDKCT
     RVSSPSKSKK ECPSPVEQKP AEHIPLSNPA PLLVSPEVHL TPAVPSLPAT VPAWPSEPTT
     FGPTGVPAQI PILSVTQTTG PDAAVSQAHL TPSPVPVSIQ AVNQPLMPLP QTMSLYQDPL
     YPGFPCSEKG DRAIAPPYSL CQTGEDLPKD KNILRFFFNL GVKAYSCPMW APHSYLYPLH
     QAYMAACRMY PKVPVPVYPQ NTWFQEAPPA QSESDCPCTD AHYSLHPEAS VNGQMPQAEM
     GPPAFASPLV IPPSQVSEGH GQLSYQPELE SENPGQLLHA EYEESLSGKN MYPQQSFGPN
     PFLGPVPIAP PFFPHVWYGY PFQGFVENPV MRQNIVLPPD DKGELDLPLE NLDLSKECDS
     VSAVDEFPDA RVEGAHSLSA ASVSSKHEGR VEQSSQTRKA DIDLASGSSA VEGKGHPPTQ
     ILNREREPGS AEPEPKRTIQ SLKEKPEKVK DPKTAADVVS PGANSVDRLQ RPKEESSEDE
     NEVSNILRSG RSKQFYNQTY GSRKYKSDWG SSGRGGYQHV RGEESWKGQP NRSRDEGYQY
     HRHVRGRPYR GDRRRSGMGD GHRGQHT
//
ID   B2RRI4_MOUSE            Unreviewed;       827 AA.
AC   B2RRI4;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   05-OCT-2010, entry version 22.
DE   SubName: Full=Adam17 protein;
GN   Name=Adam17;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 disintegrin domain.
CC   -!- SIMILARITY: Contains 1 peptidase M12B domain.
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DR   EMBL; BC138420; AAI38421.1; -; mRNA.
DR   IPI; IPI00381630; -.
DR   UniGene; Mm.27681; -.
DR   ProteinModelPortal; B2RRI4; -.
DR   SMR; B2RRI4; 216-642.
DR   STRING; B2RRI4; -.
DR   Ensembl; ENSMUST00000064536; ENSMUSP00000067953; ENSMUSG00000052593.
DR   MGI; MGI:1096335; Adam17.
DR   HOVERGEN; HBG050457; -.
DR   Bgee; B2RRI4; -.
DR   Genevestigator; B2RRI4; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR001762; Blood-coag_inhib_Disintegrin.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   Gene3D; G3DSA:4.10.70.10; Blood-coag_inhib_Disintegrin; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; Disintegrin; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease.
SQ   SEQUENCE   827 AA;  93045 MW;  0E751D0F026F6AC3 CRC64;
     MRRRLLILTT LVPFVLAPRP PEEAGSGAHP RLEKLDSLLS DYDILSLANI QQHSIRKRDL
     QSATHLETLL TFSALKRHFK LYLTSSTERF SQNLRVVVVD GKEESEYSVK WQDFFSGHVV
     GEPDSRVLAH IGDDDVTVRI NTDGAEYNIE PLWRFVNDTK DKRMLVYKSE DIKDFSRLQS
     PKVCGYLNAD SEELLPKGLI DREPSEEFVR RVKRRAEPNP LKNTCKLLVV ADHRFYKYMG
     RGEESTTTNY LIELIDRVDD IYRNTSWDNA GFKGYGVQIE QIRILKSPQE VKPGERHFNM
     AKSFPNEEKD AWDVKMLLEQ FSFDIAEEAS KVCLAHLFTY QDFDMGTLGL AYVGSPRANS
     HGGVCPKAYY NPTVKKNIYL NSGLTSTKNY GKTILTKEAD LVTTHELGHN FGAEHDPDGL
     AECAPNEDQG GKYVMYPIAV SGDHENNKMF SNCSKQSIYK TIESKAQECF QERSNKVCGN
     SRVDEGEECD PGIMYLNNDT CCNSDCTLKP GVQCSDRNSP CCKNCQFETA QKKCQEAINA
     TCKGVSYCTG NSSECPPPGD AEDDTVCLDL GKCKAGKCIP FCKREQELES CACVDTDNSC
     KVCCRNLSGP CVPYVDAEQK NLFLRKGKPC TVGFCDMNGK CEKRVQDVIE RFWDFIDQLS
     INTFGKFLAD NIVGSVLVFS LIFWIPFSIL VHCVDKKLDK QYESLSLFHH SNIEMLSSMD
     SASVRIIKPF PAPQTPGRLQ ALQPAAMMPP VSAAPKLDHQ RMDTIQEDPS TDSHADDDGF
     EKDPFPNSST AAKSFEDLTD HPVTRSEKAA SFKLQRQSRV DSKETEC
//
ID   B2RSH2_MOUSE            Unreviewed;       354 AA.
AC   B2RSH2;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 28.
DE   SubName: Full=Guanine nucleotide binding protein (G protein), alpha inhibiting 1;
GN   Name=Gnai1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC138862; AAI38863.1; -; mRNA.
DR   EMBL; BC138865; AAI38866.1; -; mRNA.
DR   IPI; IPI00467152; -.
DR   RefSeq; NP_034435.1; NM_010305.1.
DR   UniGene; Mm.254629; -.
DR   ProteinModelPortal; B2RSH2; -.
DR   SMR; B2RSH2; 5-348.
DR   STRING; B2RSH2; -.
DR   PRIDE; B2RSH2; -.
DR   Ensembl; ENSMUST00000074694; ENSMUSP00000074259; ENSMUSG00000057614.
DR   GeneID; 14677; -.
DR   KEGG; mmu:14677; -.
DR   CTD; 14677; -.
DR   MGI; MGI:95771; Gnai1.
DR   HOGENOM; HBG444960; -.
DR   HOVERGEN; HBG063184; -.
DR   InParanoid; B2RSH2; -.
DR   OMA; MTTELAG; -.
DR   OrthoDB; EOG4WDDC1; -.
DR   NextBio; 286574; -.
DR   Bgee; B2RSH2; -.
DR   Genevestigator; B2RSH2; -.
DR   GO; GO:0005622; C:intracellular; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; TAS:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; TAS:MGI.
DR   InterPro; IPR001408; Gprotein_alpha_I.
DR   InterPro; IPR001019; Gprotein_alpha_su.
DR   InterPro; IPR011025; GproteinA_insert.
DR   Gene3D; G3DSA:1.10.400.10; GproteinA_insert; 1.
DR   PANTHER; PTHR10218; Gprotein_alph_bd; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00441; GPROTEINAI.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF47895; Transducn_insert; 1.
PE   2: Evidence at transcript level;
KW   GTP-binding; Nucleotide-binding; Transducer.
SQ   SEQUENCE   354 AA;  40361 MW;  9F88311B46E62DE3 CRC64;
     MGCTLSAEDK AAVERSKMID RNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEAG
     YSEEECKQYK AVVYSNTIQS IIAIIRAMGR LKIDFGDSAR ADDARQLFVL AGAAEEGFMT
     AELAGVIKRL WKDSGVQACF NRSREYQLND SAAYYLNDLD RIAQPNYIPT QQDVLRTRVK
     TTGIVETHFT FKDLHFKMFD VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM
     NRMHESMKLF DSICNNKWFT DTSIILFLNK KDLFEEKIKK SPLTICYPEY AGSNTYEEAA
     AYIQCQFEDL NKRKDTKEIY THFTCATDTK NVQFVFDAVT DVIIKNNLKD CGLF
//
ID   B2RSI6_MOUSE            Unreviewed;       803 AA.
AC   B2RSI6;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 24.
DE   SubName: Full=Leucine rich repeat containing 8 family, member B;
GN   Name=Lrrc8b; ORFNames=mCG_52435;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC138877; AAI38878.1; -; mRNA.
DR   EMBL; BC138878; AAI38879.1; -; mRNA.
DR   EMBL; CH466529; EDL20199.1; -; Genomic_DNA.
DR   IPI; IPI00874916; -.
DR   RefSeq; NP_001028722.1; NM_001033550.2.
DR   UniGene; Mm.439781; -.
DR   UniGene; Mm.439828; -.
DR   ProteinModelPortal; B2RSI6; -.
DR   SMR; B2RSI6; 488-759.
DR   PRIDE; B2RSI6; -.
DR   Ensembl; ENSMUST00000112707; ENSMUSP00000108327; ENSMUSG00000070639.
DR   GeneID; 433926; -.
DR   KEGG; mmu:433926; -.
DR   CTD; 433926; -.
DR   MGI; MGI:2141353; Lrrc8b.
DR   HOGENOM; HBG445357; -.
DR   HOVERGEN; HBG052360; -.
DR   InParanoid; B2RSI6; -.
DR   OMA; MQLEGFQ; -.
DR   NextBio; 409111; -.
DR   Bgee; B2RSI6; -.
DR   Genevestigator; B2RSI6; -.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR021040; LRR_protein-8_N.
DR   Pfam; PF12534; DUF3733; 2.
DR   Pfam; PF00560; LRR_1; 2.
DR   SMART; SM00369; LRR_TYP; 2.
DR   PROSITE; PS51450; LRR; 10.
PE   2: Evidence at transcript level;
KW   Leucine-rich repeat; Repeat.
SQ   SEQUENCE   803 AA;  92186 MW;  5E6E4DE4A5136613 CRC64;
     MITLTELKCL ADAQSSYHIL KPWWDVFWYY ITLIMLLVAV LAGALQLTQS RVLCCLPCKV
     EFDNQCAVPW DLLKGSENAS SNSGLLLPLP LRIQNDLHRQ QYSYIDAVCY EKQLHWFAKF
     FPYLVLLHTL IFAACSNFWL HYPSTSSRLE HFVSILHKCF DSPWTTRALS ETVAEQSVRP
     LKLSKSKTLL STSGGSADID ASKQSLPYPQ PGLESPGIES PTSSVLDKKE GEQAKAIFEK
     VKRFRLHVEQ RDIIYRVYLK QIIVKVILFV LIITYVPYFL SYITLEIDCS IDVQAFTGYK
     RYQCVYSLAE IFKVLASFYV ILVMLYGLTS SYSLWWMLRS SLKQYSFEAL REKSNYSDIP
     DVKNDFAFIL HLADQYDPLY SKRFSIFLSE VSENKLKQIN LNNEWTVERL KSKLVKNSQD
     KVELHLFMLN GLPDNVFELT EMEVLSLELI PEVKLPAAVA QLVNLRELHV YHSSLVVDHP
     ALAFLEENLR ILRLKFTEMG KIPRWVFHLK NLKELYLSGC VLPEQLSSLH LEGFQDLKNL
     RTLYLKSSLS RIPQVVTDLL PSLQKLSLDN EGSKLVVLNN LKKMVNLKSL ELLSCDLERI
     PHSIFSLNNL HELDLKENNL KTVEEIISFQ HLPSLSCLKL WHNNIAYIPA QIGALSNLEQ
     LFLGHNNIES LPLQLFLCTK LHYLDLSYNH LTFIPEEIQY LTNLQYFAVT NNNIEMLPDG
     LFQCKKLQCL LLGRNSLTDL SPLVGELSNL THLELTGNYL ETLPVELEGC QSLKRSCLIV
     EDSLLNSLPL PVAERLQTCL DKC
//
ID   B2RT41_MOUSE            Unreviewed;      1992 AA.
AC   B2RT41;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 28.
DE   SubName: Full=Zinc finger, C3H1-type containing;
GN   Name=Zfc3h1; Synonyms=Ccdc131;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
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DR   EMBL; BC139124; AAI39125.1; -; mRNA.
DR   IPI; IPI00751628; -.
DR   RefSeq; NP_001028433.2; NM_001033261.2.
DR   UniGene; Mm.207621; -.
DR   ProteinModelPortal; B2RT41; -.
DR   SMR; B2RT41; 1610-1681.
DR   PRIDE; B2RT41; -.
DR   Ensembl; ENSMUST00000036044; ENSMUSP00000044069; ENSMUSG00000034163.
DR   GeneID; 216345; -.
DR   KEGG; mmu:216345; -.
DR   CTD; 216345; -.
DR   MGI; MGI:2446143; Zfc3h1.
DR   eggNOG; roNOG04005; -.
DR   HOGENOM; HBG282090; -.
DR   HOVERGEN; HBG095534; -.
DR   InParanoid; B2RT41; -.
DR   OMA; QSFWTFL; -.
DR   OrthoDB; EOG4CNQQ7; -.
DR   NextBio; 375115; -.
DR   Bgee; B2RT41; -.
DR   Genevestigator; B2RT41; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   InterPro; IPR003107; HAT.
DR   InterPro; IPR019607; Putative_zinc-finger_domain.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 4.
DR   Pfam; PF10650; zf-C3H1; 1.
DR   SMART; SM00386; HAT; 5.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 2.
PE   1: Evidence at protein level;
KW   Repeat.
SQ   SEQUENCE   1992 AA;  225054 MW;  4825958A88EB4892 CRC64;
     MAAAADPSTP ASSGLSPKEE GELEDGEISD DDNSRSRSSS SSSSGGGLLP YPRRRPPPPA
     RGGGSGGGGG GSSSSSSSSQ QQLRNFSRSR HPAERGQLRG PSSYRPKEPF RTHPPPGRMP
     SGSLSESSPR PSFWERSHIA LDRFRFRGSR PYRGGSRWSR GRGVGERGGK PGCRPPGGGG
     SGGAGSGFGS SQSWREPSPP RKSSKSFGRS PSRKQNHSSK SENCAEETFE DLLLKYKQIQ
     LELECINKDE KLALSSKEET AQEDPKTLHL EDQTSTDNAS ITKDPSKEVA PEEKTQVKTF
     QAFELKPLRQ KLTLPGDKNR VKRGKDGTRQ LSLKSSTTDA SQGLEDKEQN LTRRLSASDI
     VSEKKLGEEE EELSELQLRL LALQSASKKW QQKEQQVMKE SKEKLTKTKT AQQKAKTSTK
     AHSAKKVSAT AKQALRKQQT KAWKKLQQQK EQERQKEEDQ RKHAEEEERR KREEEIRKIR
     DLSNQEEQYN RFMKLVGGKR RARSKSSDPD LRRSLEKQSD SAGGIYQYDN YEEVAMDTDS
     ETSSPAPSPV QPPFFPECSL GYFSSAPSVS LPPPAQVSSV PSLNQPYGEG LCVSLDPLPP
     LPPLPPLPPE DPEQPPKPPF ADEEEEEEML LREELLKSLA SKRAFKPEET SSNSDPPSPP
     VLNNSQPLSR SNLSIVSINT VSQPRIQNPK FHRGPRLPRT VISLPKHKSV VVTLNDSDDS
     ESDGEASKST NSVFGGLESM IKEARRTAEQ ASKPKVPPKS EKENDPLRTP EALPEEKKME
     YRLLKEEIAN REKQRLIKSD QLKTSSSSPA NSDVEMDGIG RIAMVTKQVA DAEAKLKKHK
     ILLIKDESVL KNLVLQEAKK KESVRNAEAK ITKLTEQLQA AEKILSANRM FLKKLQEQIH
     RVQQRVTIKK ALTLKYGEEL ARAKAVASKE LGKRKLEQDR LGPNKMMRLD NSPISSPRKH
     SAELIAMEKR RLQKLEYEYA LKIQKLKEAR ALKAKEQQNL VPVVEEEPEF SVPQPSLHDL
     TQDKLTLDTE ENDVDDEVLS GASRERRRSF LESNSFTKPN LKHTDTPNKE CINKLSKSTV
     EKPELFLGLK IGELQKLYSR ADSLKQLILK TTTGTTEKVL HGQEISVDVD FVTAQSKTTE
     VKPCPFRPYQ SPLLVFKSYR FSPYYRTKEK LPLSSVSYSN MVEPDQCFCR FDLTGTCNDD
     DCQWQHVQDY TLSRKRLFQD ILSYNLSLIG CSEMSTDEEI ASAAEKYVEK LFGVNKDRMS
     MDQMAVLLVS NVNESKGHTP PFTTYKDKRK WKPKFCRKPV SENSCSSDDE QSTGPIKYAF
     RPEKQINVPA LDTVVTPDDV RYFTSETDDI ANLEASVLEN PSHVQLWLKL AYKYLNQNEG
     LCSESLDSAL NVLARALENN KDNPEIWCHY LRLFSKRGTK EEVQEMCETA VEYAPDYQSF
     WTFLHLESTF EEKDYVCERM VEFLMGAAKR EISDILSFQL LEALLFRVQL HIFTGRCQSA
     LAVLQNALKL ANDAIVAEYL KTDDRCLAWL AYIHLIEFNS LPSKLYDPSN ANPSRIVNTE
     PFVMPWQAAQ DVKTNPDLLL AVFEDAVKAC TDETLTSGER IEVCLPLYTN MIALHQLLER
     YEEAVELCTS LLESCPTNCQ LLETLAALYL KTDRYDKARR VWLTAFENNP QNAEIFYHLC
     KFFILQDGGD KLLPVLRQFV GSFFKPGFEK YSNVDLFRYL LNIPGPLDIP ACLCKGNFDD
     DAFNNQVPYL WLIYCLCHPL QSSIKETVEA YEAALGVAMR SDIVQKIWMD YLVFANNRAA
     GSRNKVQEFK LFTDLVNRCL VTVPARYPIP FSSADYWSNY EFHNRVIFFY LSCVPKTQHS
     KTLERFCSAM PANSRLALRL LQHEWEESNV QILKLQAKMF TYNIPTCLAT WKIAIAAEIA
     LKGQREVHRL YQRALQKLPL CASLWKDQLL FEASEGGKTD NLRKLVSKCQ EIGVSLNELL
     NLNSNKTESK NL
//
ID   B2RTI1_MOUSE            Unreviewed;       599 AA.
AC   B2RTI1;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 23.
DE   SubName: Full=Leucine zipper, putative tumor suppressor 1;
GN   Name=Lzts1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC139350; AAI39351.1; -; mRNA.
DR   EMBL; BC139352; AAI39353.1; -; mRNA.
DR   IPI; IPI00954671; -.
DR   RefSeq; NP_955396.2; NM_199364.2.
DR   UniGene; Mm.479807; -.
DR   ProteinModelPortal; B2RTI1; -.
DR   STRING; B2RTI1; -.
DR   Ensembl; ENSMUST00000037049; ENSMUSP00000039397; ENSMUSG00000036306.
DR   GeneID; 211134; -.
DR   KEGG; mmu:211134; -.
DR   CTD; 211134; -.
DR   MGI; MGI:2684762; Lzts1.
DR   HOVERGEN; HBG052381; -.
DR   InParanoid; B2RTI1; -.
DR   OMA; AMYQRNQ; -.
DR   PhylomeDB; B2RTI1; -.
DR   Bgee; B2RTI1; -.
DR   Genevestigator; B2RTI1; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   InterPro; IPR009638; Fez1.
DR   Pfam; PF06818; Fez1; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   599 AA;  67290 MW;  7B77A3BCF249E817 CRC64;
     MGSVSSLISG HSFHSKHCRA SQYKLRKSSH LKKLNRYSDG LLRFGFSQDS GRGKSSSKMG
     KSEDFFYIKV SQKARGSHRP DYTALSSGDI GGQTGVDFDP ATPPKLMPFS NQLEMSSDKG
     AVRPTAFKPV LPRSGAILHS SPESTSHQLH PMPPDKPKEQ ELKPGLCSGA LSDSGRNSMS
     SLPTHSTTSS YQLDPLVTPV GPTSRFGGSA HNITQGIILQ DSNMMSLKAL SFSDGGSKLA
     HPGKADKGAS CVRSPLSTDE CTIQELEQKL LQRETALQKL QRSFDEKEFA SGQTFEERPR
     RTRDELECLE PKSKLKPPSQ KSQRTQQVLQ LQVLQLQQEK RQLRQELESL MKEQDLLETK
     LRSYEREKTN FAPALEETQW EVCQKSGEIS LLKQQLKESQ LEVNTKASEI LSLKAQLKDT
     RGKLDGMELK TQDLESALRT KGLELEVCEN ELQRKKNEAE LLREKVNLLE QELMELRAQA
     ALHPAPLGPP GVGLTFSEDI PALQRELDRL RAELKEERQG HDQMSSGFQH ERLVWKEEKE
     KVIQYQRQLQ QSYLAMYQRN QRLEKALQQL ARGDGPGEPF EIDLEGADIP YEDIIATEI
//
ID   B2RTP7_MOUSE            Unreviewed;       707 AA.
AC   B2RTP7;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 21.
DE   SubName: Full=Krt2 protein;
GN   Name=Krt2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
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DR   EMBL; BC139485; AAI39486.1; -; mRNA.
DR   IPI; IPI00622240; -.
DR   UniGene; Mm.358616; -.
DR   ProteinModelPortal; B2RTP7; -.
DR   SMR; B2RTP7; 197-234, 430-507.
DR   STRING; B2RTP7; -.
DR   PRIDE; B2RTP7; -.
DR   Ensembl; ENSMUST00000023712; ENSMUSP00000023712; ENSMUSG00000064201.
DR   MGI; MGI:96699; Krt2.
DR   HOVERGEN; HBG013015; -.
DR   InParanoid; B2RTP7; -.
DR   Bgee; B2RTP7; -.
DR   Genevestigator; B2RTP7; -.
DR   GO; GO:0045095; C:keratin filament; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR016044; F.
DR   InterPro; IPR001664; IF.
DR   InterPro; IPR018039; Intermediate_filament_CS.
DR   InterPro; IPR003054; Keratin_II.
DR   PANTHER; PTHR23239; IF; 1.
DR   PANTHER; PTHR23239:SF18; Keratin_II; 1.
DR   Pfam; PF00038; Filament; 1.
DR   PRINTS; PR01276; TYPE2KERATIN.
DR   PROSITE; PS00226; IF; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Intermediate filament.
SQ   SEQUENCE   707 AA;  70923 MW;  AD90C9500FBE79DA CRC64;
     MSCQISCRSR RGGGGGGGGG FRGFSSGSAV VSGGSRRSNT SFSCISRHGG GRGGSGGGGF
     GSQSLVGLGG YKSISSSVAG NSGGYGGSSF GGSSGFGGGR GFGGGQGFGG SGGFGGGSGF
     GGGQGFGGGS RFGGGSGFGG GGFGGGSFGG GRFGGGPGGF GGPGGFPGGG IHEVSVNQSL
     LQPLDVKVDP EIQNVKSQER EQIKTLNNKF ASFIDKVRFL EQQNQVLRTK WELLQQLDVG
     SRTTNLDPIF QAYIGMLKKQ VDRLSAERTS QESELNNMQD LVEDFKKKYE DEINKRTSAE
     NDFVTIKKDV DSCYMDKTEL QARLDILAQE VNFLRTLYDA ELSQLQQDVT DTNVILSMDN
     NRNLDLDSII AEVQNQYEMI AHKSKAESEE LYHSKYEELQ VTAVKHGDSL KEIKMEISEL
     NRTIQRLQGE ISHVKKQCKG VQDSIADAEQ RGEHAIKDAR GKLTDLEEAL QQCREDLARL
     LRDYQELMNT KLSLDVEIAT YRKLLEGEEC RMSGDFSDNV SVSITSSTIS SSVASKTGFG
     SGGQSSGGRG SYGGRGGGGG GSTYGSGGRS SGSRGSGSGS GGGGYSSGGG SRGGSGGGYG
     SGGGSRGGSG GGYGSGGGSG SGGGGYSSGG GSRGGSGGGG VSSGGGSRGG SSSGGGSRGG
     SSSGGGGYSS GGGSRGGSSS GGAGSSSEKG GSGSGEGCGS GVTFSFR
//
ID   B2RUC1_MOUSE            Unreviewed;       209 AA.
AC   B2RUC1;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   05-OCT-2010, entry version 16.
DE   SubName: Full=Tpd52l1 protein;
GN   Name=Tpd52l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC141068; AAI41069.1; -; mRNA.
DR   EMBL; BC145321; AAI45322.1; -; mRNA.
DR   IPI; IPI00309878; -.
DR   UniGene; Mm.439966; -.
DR   STRING; B2RUC1; -.
DR   PRIDE; B2RUC1; -.
DR   Ensembl; ENSMUST00000000305; ENSMUSP00000000305; ENSMUSG00000000296.
DR   MGI; MGI:1298386; Tpd52l1.
DR   HOGENOM; HBG717185; -.
DR   HOVERGEN; HBG058643; -.
DR   InParanoid; B2RUC1; -.
DR   Bgee; B2RUC1; -.
DR   Genevestigator; B2RUC1; -.
DR   InterPro; IPR007327; TPD52.
DR   PANTHER; PTHR19307; TPD52; 1.
DR   Pfam; PF04201; TPD52; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   209 AA;  23031 MW;  51EABA926CB8A0D1 CRC64;
     MEAQAQGLLE TEPLQGRDGD AVGSADFSSM LSEEEKEELK AELIQLEDEI TTLRQVLSAK
     ERHLVEIKQK LGMNLMNELK QNFSRSWHDM QTTTAYKKTH ETLSHAGQKA TAAFNNVGTA
     ISKKFGDMRS HSFGYSIRHS ISMPAMRNSS TFKSFEERVE TTVASLKTKV GGTNHGGGSF
     EEVLNSTAHA SSQNASAGSR QTKDEELQC
//
ID   B2RUG6_MOUSE            Unreviewed;      1936 AA.
AC   B2RUG6;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   05-OCT-2010, entry version 20.
DE   SubName: Full=Dock4 protein;
GN   Name=Dock4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; BC141138; AAI41139.1; -; mRNA.
DR   IPI; IPI00223070; -.
DR   UniGene; Mm.341423; -.
DR   ProteinModelPortal; B2RUG6; -.
DR   STRING; B2RUG6; -.
DR   Ensembl; ENSMUST00000037488; ENSMUSP00000047387; ENSMUSG00000035954.
DR   MGI; MGI:1918006; Dock4.
DR   HOVERGEN; HBG051389; -.
DR   InParanoid; B2RUG6; -.
DR   Bgee; B2RUG6; -.
DR   Genevestigator; B2RUG6; -.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0051020; F:GTPase binding; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   InterPro; IPR010703; DOCK.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF06920; Ded_cyto; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1936 AA;  222197 MW;  8DAE09283FA3F6F7 CRC64;
     MWIPTEHEKY GVVIASFRGT VPYGLSLEIG DTVQILEKCD GWYRGFALKN PNIKGIFPSS
     YVHLKNACVK NKGQFEMVIP TEDSVITEMT STLRDWGTMW KQLYVRNEGD LFHRLWHIMN
     EILDLRRQVL VGHLTHDRMK DVKRHITARL DWGNEQLGLD LVPRKEYAMV DPEDISITEL
     YRLMEHRHRK KDTPVQASSH HLFVQMKSLM CSNLGEELEV IFSLFDSKEN RPISERFFLR
     LNRNGLPKAP DKPERHCSLF VDLGSSELRK DIYITVHIIR IGRMGAGEKK NACSVQYRRP
     FGCAVLSIAD LLTGETKDDL VLKVYMCNTE SEWYQIHENI IKKLNARYNL TGSNAGLAVS
     LQLLHGDIEQ IRREYSSVFS HGVSITRKLG FSDIIMPGEM RNDLYITVER GEFEKGGKSV
     ARNVEVTMFI VDSNGQPLKD FISFGSGEPP ASEYHSFVLY HNNSPRWSEL LKLPIPVDKF
     RGSHIRFEFR HCSTKEKGEK KLFGFSFVPL MQEDGRTLPD GTHELIVHKC EENTNLQDTT
     RYLKLPFSKV IFLGNNNQTM KATKESFWIT SFLCSTKLTQ NGDMLDLLKW RTHPDKITGC
     LSKLKEIDGS EIVKFLQDTL DTLFGILDEN SQKYGSKVFD SLVHIINLLQ DSKFHHFKPV
     MDTYIESHFA GALAYRDLIK VLKWYVDRIT EAERQEHIQE VLKAQEYIFK YIVQSRRLFS
     LATGGQNEEE FRCCIQELLM SVRFFLSQES KGTGALSQSQ AVFLSSFPAV YSELLKLFDV
     REVANLVQDT LGSLPTIMHV DDSLQAIKLQ CIGKTVESQL YTNPDSRYIL LPVVLHHLHI
     HLQEQKDLIM CARILSNVFC LIKKNSSEKS VLEEIDVIVA SLLDILLRTI LEITSRPQAS
     SSAMRLQFQD VTGEFVACLL SLLRQMTDRH YQQLLNSFST KEELRDFLLQ IFTVFRILIR
     PEMFPKDWTV MRLVANNVII TTVLYLSDAL RKNFLNENFD YKIWDSYFYL AVIFINQLCL
     QLEMFTPSKK KKVLEKYGDM RVTMGCEIFS MWQNLGEHKL HFIPALIGPF LEVTLIPQPD
     LRNVMIPIFH DMMDWEQRRS GNFKQVEAKL IDKLDSLMSE GKGDETYREL FNSIIPLFGP
     YPSLLKKIER ETWRESGVSL IATVTRLMER LLDYRDCMKI GEVDGKKIGC TVSLLNFYKT
     ELNKEEMYIR YIHKLYDLHL KAQNFTEAAY TLLLYDELLE WSDRPLREFL TYPMQTEWQR
     KEHLHLTIIQ NFDRGKCWEN GIILCRKIAE QYESYYDYRN LSKMRMMEAS LYDKIMDQQR
     LEPEFFRVGF YGKKFPFFLR NKEFVCRGHD YERLEAFQQR MLNEFPHAIA MQHANQPDET
     IFQAEAQYLQ IYAVTPIPES QEVLQREGVP DNIKSFYKVN HIWKFRYDRP FHKGAKDKEN
     EFKSLWVERT SLYLVQSLPG ISRWFEVEKR EVVEMSPLEN AIEVLENKNQ QLKTLISQCQ
     TRQMQNINPL TMCLNGVIDA AVNGGVSRYQ EAFFVKDYIL SHPEDGEKIA RLRELMLEQA
     QILEFGLAVH EKFVPQDMRP LHKKLVDQFF VMKSSFGIQE FPACIQASPV HFPNGSPRVC
     RNSAPASMSP DGTRVIPRRS PLSYPAVNRY SSSSLSSQAS AEVSNITGQS ESSDEVFNMQ
     PSPSTSSLSS THSASPNVTS SAPSSARASP LLSDKHKHSR ENSCLSPRDR PCSAIYPTPV
     EPSQRMLFNH IGDGALPRSD PNLSAPEKAS PARHTTSVSP SPAGRSPLKG SVQSFTPSPV
     EYNSPGLSSN SPVLSGSYSS GISSLSRCST SETSGFENQA NEQSVPVPVP VPVPSFSGSE
     EPVRKESKTP PPYSVYERTL RRPVPLPHSL SIPVTSEPPA LPPKPLAARS SHLENGTRRT
     EPGPRPRPLP RKVSQL
//
ID   B2RUG9_MOUSE            Unreviewed;      2842 AA.
AC   B2RUG9;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   11-JAN-2011, entry version 28.
DE   SubName: Full=Adenomatosis polyposis coli;
DE   SubName: Full=Adenomatosis polyposis coli, isoform CRA_a;
GN   Name=Apc; ORFNames=mCG_121500;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC141141; AAI41142.1; -; mRNA.
DR   EMBL; CH466557; EDK97078.1; -; Genomic_DNA.
DR   IPI; IPI00896736; -.
DR   RefSeq; NP_031488.2; NM_007462.3.
DR   UniGene; Mm.384171; -.
DR   ProteinModelPortal; B2RUG9; -.
DR   SMR; B2RUG9; 2-55, 128-237, 1467-1528.
DR   STRING; B2RUG9; -.
DR   Ensembl; ENSMUST00000079362; ENSMUSP00000078337; ENSMUSG00000005871.
DR   GeneID; 11789; -.
DR   KEGG; mmu:11789; -.
DR   CTD; 11789; -.
DR   MGI; MGI:88039; Apc.
DR   HOVERGEN; HBG004264; -.
DR   InParanoid; B2RUG9; -.
DR   OMA; FATESTP; -.
DR   PhylomeDB; B2RUG9; -.
DR   NextBio; 279609; -.
DR   Bgee; B2RUG9; -.
DR   Genevestigator; B2RUG9; -.
DR   GO; GO:0044295; C:axonal growth cone; IDA:MGI.
DR   GO; GO:0031253; C:cell projection membrane; IDA:MGI.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IDA:MGI.
DR   GO; GO:0035371; C:microtubule plus end; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0008013; F:beta-catenin binding; IDA:MGI.
DR   GO; GO:0051010; F:microtubule plus-end binding; IDA:MGI.
DR   GO; GO:0009952; P:anterior/posterior pattern formation; IMP:MGI.
DR   GO; GO:0009798; P:axis specification; IMP:MGI.
DR   GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR   GO; GO:0060070; P:canonical Wnt receptor signaling pathway; IMP:MGI.
DR   GO; GO:0016477; P:cell migration; IMP:MGI.
DR   GO; GO:0051276; P:chromosome organization; IGI:MGI.
DR   GO; GO:0000281; P:cytokinesis after mitosis; IMP:MGI.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IGI:MGI.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
DR   GO; GO:0001942; P:hair follicle development; IMP:MGI.
DR   GO; GO:0001822; P:kidney development; IMP:MGI.
DR   GO; GO:0007091; P:mitotic metaphase/anaphase transition; IMP:MGI.
DR   GO; GO:0046716; P:muscle cell homeostasis; IGI:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptosis; IMP:MGI.
DR   GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; IMP:MGI.
DR   GO; GO:0043409; P:negative regulation of MAPKKK cascade; IGI:MGI.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:MGI.
DR   GO; GO:0042483; P:negative regulation of odontogenesis; IMP:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptosis; IMP:MGI.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; IMP:MGI.
DR   GO; GO:0051781; P:positive regulation of cell division; IMP:MGI.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:MGI.
DR   GO; GO:0030858; P:positive regulation of epithelial cell differentiation; IGI:MGI.
DR   GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:MGI.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:MGI.
DR   GO; GO:0009954; P:proximal/distal pattern formation; IMP:MGI.
DR   GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; IMP:MGI.
DR   GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IMP:MGI.
DR   GO; GO:0045667; P:regulation of osteoblast differentiation; IMP:MGI.
DR   GO; GO:0045670; P:regulation of osteoclast differentiation; IMP:MGI.
DR   GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR   GO; GO:0043588; P:skin development; IMP:MGI.
DR   GO; GO:0035019; P:somatic stem cell maintenance; IGI:MGI.
DR   GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR   GO; GO:0048538; P:thymus development; IMP:MGI.
DR   InterPro; IPR009240; APC_15aa.
DR   InterPro; IPR009234; APC_basic.
DR   InterPro; IPR009223; APC_crr.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR009232; EB1-bd.
DR   InterPro; IPR009224; SAMP.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 3.
DR   Pfam; PF05972; APC_15aa; 4.
DR   Pfam; PF05956; APC_basic; 1.
DR   Pfam; PF05923; APC_crr; 7.
DR   Pfam; PF00514; Arm; 3.
DR   Pfam; PF05937; EB1_binding; 1.
DR   Pfam; PF05924; SAMP; 3.
DR   SMART; SM00185; ARM; 6.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   2842 AA;  310880 MW;  ED681AC077A9F7DB CRC64;
     MAAASYDQLL KQVEALKMEN SNLRQELEDN SNHLTKLETE ASNMKEVLKQ LQGSIEDETM
     TSGQIDLLER LKEFNLDSNF PGVKLRSKMS LRSYGSREGS VSSRSGECSP VPMGSFPRRT
     FVNGSRESTG YLEELEKERS LLLADLDKEE KEKDWYYAQL QNLTKRIDSL PLTENFSLQT
     DMTRRQLEYE ARQIRAAMEE QLGTCQDMEK RAQRRIARIQ QIEKDILRVR QLLQSQAAEA
     ERSSQSRHDA ASHEAGRQHE GHGVAESNTA ASSSGQSPAT RVDHETASVL SSSGTHSAPR
     RLTSHLGTKV EMVYSLLSML GTHDKDDMSR TLLAMSSSQD SCISMRQSGC LPLLIQLLHG
     NDKDSVLLGN SRGSKEARAR ASAALHNIIH SQPDDKRGRR EIRVLHLLEQ IRAYCETCWE
     WQEAHEQGMD QDKNPMPAPV EHQICPAVCV LMKLSFDEEH RHAMNELGGL QAIAELLQVD
     CEMYGLTNDH YSVTLRRYAG MALTNLTFGD VANKATLCSM KGCMRALVAQ LKSESEDLQQ
     VIASVLRNLS WRADVNSKKT LREVGSVKAL MECALEVKKE STLKSVLSAL WNLSAHCTEN
     KADICAVDGA LAFLVGTLTY RSQTNTLAII ESGGGILRNV SSLIATNEDH RQILRENNCL
     QTLLQHLKSH SLTIVSNACG TLWNLSARNP KDQEALWDMG AVSMLKNLIH SKHKMIAMGS
     AAALRNLMAN RPAKYKDANI MSPGSSLPSL HVRKQKALEA ELDAQHLSET FDNIDNLSPK
     ASHRSKQRHK QNLYGDYAFD ANRHDDSRSD NFNTGNMTVL SPYLNTTVLP SSSSSRGSLD
     SSRSEKDRSL ERERGIGLSA YHPTTENAGT SSKRGLQITT TAAQIAKVME EVSAIHTSQD
     DRSSASTTEF HCVADDRSAA RRSSASHTHS NTYNFTKSEN SNRTCSMPYA KVEYKRSSND
     SLNSVTSSDG YGKRGQMKPS VESYSEDDES KFCSYGQYPA DLAHKIHSAN HMDDNDGELD
     TPINYSLKYS DEQLNSGRQS PSQNERWARP KHVIEDEIKQ NEQRQARSQN TSYPVYSENT
     DDKHLKFQPH FGQQECVSPY RSRGTSGSET NRMGSSHAIN QNVNQSLCQE DDYEDDKPTN
     YSERYSEEEQ HEEEEERPTN YSIKYNEEKH HVDQPIDYSL KYATDISSSQ KPSFSFSKNS
     SAQSTKPEHL SPSSENTAVP PSNAKRQNQL RPSSAQRNGQ TQKGTTCKVP SINQETIQTY
     CVEDTPICFS RCSSLSSLSS ADDEIGCDQT TQEADSANTL QTAEVKENDV TRSAEDPATE
     VPAVSQNARA KPSRLQASGL SSESTRHNKA VEFSSGAKSP SKSGAQTPKS PPEHYVQETP
     LVFSRCTSVS SLDSFESRSI ASSVQSEPCS GMVSGIISPS DLPDSPGQTM PPSRSKTPPP
     PPQTVQAKRE VPKSKVPAAE KRESGPKQTA VNAAVQRVQV LPDVDTLLHF ATESTPDGFS
     CSSSLSALSL DEPFIQKDVE LRIMPPVQEN DNGNETESEQ PEESNENQDK EVEKPDSEKD
     LLDDSDDDDI EILEECIISA MPTKSSRKAK KLAQTASKLP PPVARKPSQL PVYKLLPAQN
     RLQAQKHVSF TPGDDVPRVY CVEGTPINFS TATSLSDLTI ESPPNELATG DGVRAGIQSG
     EFEKRDTIPT EGRSTDDAQR GKISSIVTPD LDDNKAEEGD ILAECINSAM PKGKSHKPFR
     VKKIMDQVQQ ASSTSSGANK NQVDTKKKKP TSPVKPMPQN TEYRTRVRKN TDSKVNVNTE
     ETFSDNKDSK KPSLQTNAKA FNEKLPNNED RVRGSFALDS PHHYTPIEGT PYCFSRNDSL
     SSLDFDDDDV DLSREKAELR KGKESKDSEA KVTCRPEPNS SQQAASKSQA SIKHPANRAQ
     SKPVLQKQPT FPQSSKDGPD RGAATDEKLQ NFAIENTPVC FSRNSSLSSL SDIDQENNNN
     KESEPIKEAE PANSQGEPSK PQASGYAPKS FHVEDTPVCF SRNSSLSSLS IDSEDDLLQE
     CISSAMPKKK RPSRLKSESE KQSPRKVGGI LAEDLTLDLK DLQRPDSEHA FSPDSENFDW
     KAIQEGANSI VSSLHQAAAA AACLSRQASS DSDSILSLKS GISLGSPFHL TPDQEEKPFT
     SNKGPRILKP GEKSTLEAKK IESENKGIKG GKKVYKSLIT GKIRSNSEIS SQMKQPLPTN
     MPSISRGRTM IHIPGLRNSS SSTSPVSKKG PPLKTPASKS PSEGPGATTS PRGTKPAGKS
     ELSPITRQTS QISGSNKGSS RSGSRDSTPS RPTQQPLSRP MQSPGRNSIS PGRNGISPPN
     KLSQLPRTSS PSTASTKSSG SGKMSYTSPG RQLSQQNLTK QASLSKNASS IPRSESASKG
     LNQMSNGNGS NKKVELSRMS STKSSGSESD RSERPALVRQ STFIKEAPSP TLRRKLEESA
     SFESLSPSSR PDSPTRSQAQ TPVLSPSLPD MSLSTHPSVQ AGGWRKLPPN LSPTIEYNDG
     RPTKRHDIAR SHSESPSRLP INRAGTWKRE HSKHSSSLPR VSTWRRTGSS SSILSASSES
     SEKAKSEDER HVSSMPAPRQ MKENQVPTKG TWRKIKESDI SPTGMASQSA SSGAASGAES
     KPLIYQMAPP VSKTEDVWVR IEDCPINNPR SGRSPTGNTP PVIDSVSEKG SSSIKDSKDT
     HGKQSVGSGS PVQTVGLETR LNSFVQVEAP EQKGTEAKPG QSNPVSIAET AETCIAERTP
     FSSSSSSKHS SPSGTVAARV TPFNYNPSPR KSSADSTSAR PSQIPTPVST NTKKRDSKTD
     STESSGAQSP KRHSGSYLVT SV
//
ID   B2RUJ5_MOUSE            Unreviewed;       842 AA.
AC   B2RUJ5;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 19.
DE   SubName: Full=Apba1 protein;
GN   Name=Apba1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 2 PDZ (DHR) domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC141181; AAI41182.1; -; mRNA.
DR   IPI; IPI00223019; -.
DR   UniGene; Mm.22879; -.
DR   ProteinModelPortal; B2RUJ5; -.
DR   SMR; B2RUJ5; 458-626, 660-842.
DR   STRING; B2RUJ5; -.
DR   Ensembl; ENSMUST00000025830; ENSMUSP00000025830; ENSMUSG00000024897.
DR   MGI; MGI:1860297; Apba1.
DR   HOVERGEN; HBG050523; -.
DR   InParanoid; B2RUJ5; -.
DR   OrthoDB; EOG43JC42; -.
DR   Bgee; B2RUJ5; -.
DR   Genevestigator; B2RUJ5; -.
DR   GO; GO:0014051; P:gamma-aminobutyric acid secretion; IMP:MGI.
DR   GO; GO:0014047; P:glutamate secretion; IGI:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; IPI:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IGI:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IGI:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IGI:MGI.
DR   GO; GO:0007268; P:synaptic transmission; IGI:MGI.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00595; PDZ; 2.
DR   Pfam; PF00640; PID; 1.
DR   SMART; SM00228; PDZ; 2.
DR   SMART; SM00462; PTB; 1.
DR   SUPFAM; SSF50156; PDZ; 2.
DR   PROSITE; PS50106; PDZ; 2.
DR   PROSITE; PS01179; PID; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   842 AA;  92881 MW;  1175E9F9C5A2CA2A CRC64;
     MNHLEGSAEV EVADEAPGGE VNESVEADLE HPEVVEGQQP SPSPPPPAGH EPEDHRGHPA
     PPPPPPPQEE EEEERGECLA RSASTESGFH NHTDTAEGDV LAAARDGYEA ERAQDADDES
     AYAVQYRPEA EEYTEQAEAE HAEAAQRRAL PNHLHFHSLE HEEAMNAAYS GYVYTHRLFH
     RAEDEPYAEP YADYGGLQEH VYEEIGDAPE LEARDGLRLY ERERDEAAAY RQEALGARLH
     HYDERSDGES DSPEKEAEFA PYPRMDSYEQ EEDIDQIVAE VKQSMSSQSL DKAAEDMPEA
     EQDLERAPTP GGGHPDSPGL PAPAGQQQRV VGTPGGSEVG QRYSKEKRDA ISLAIKDIKE
     AIEEVKTRTI RSPYTPDEPK EPIWVMRQDI SPTRDCDDQR PVDGDSPSPG SSSPLGAESS
     SIPLHPGDPT EASTNKESRK SLASFPTYVE VPGPCDPEDL IDGIIFAANY LGSTQLLSDK
     TPSKNVRMMQ AQEAVSRIKT AQKLAKSRKK APEGESQPMT EVDLFISTQR IKVLNADTQE
     PMMDHPLRTI SYIADIGNIV VLMARRRMPR SNSQENVEAS HPSQDGKRQY KMICHVFESE
     DAQLIAQSIG QAFSVAYQEF LRANGINPED LSQKEYSDLL NTQDMYNDDL IHFSKSENCK
     DVFIEKQKGE ILGVVIVESG WGSILPTVII ANMMHGGPAE KSGKLNIGDQ IMSINGTSLV
     GLPLSTCQSI IKGLKNQSRV KLNIVRCPPV TTVLIRRPDL RYQLGFSVQN GIICSLMRGG
     IAERGGVRVG HRIIEINGQS VVATPHEKIV HILSNAVGEI HMKTMPAAMY RLLTAQEQPV
     YI
//
ID   B2RUJ6_MOUSE            Unreviewed;      1606 AA.
AC   B2RUJ6;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 27.
DE   SubName: Full=Rapgef6 protein;
GN   Name=Rapgef6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 N-terminal Ras-GEF domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 Ras-GEF domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC141182; AAI41183.1; -; mRNA.
DR   IPI; IPI00551348; -.
DR   UniGene; Mm.254404; -.
DR   ProteinModelPortal; B2RUJ6; -.
DR   SMR; B2RUJ6; 11-386, 526-609, 864-1059.
DR   STRING; B2RUJ6; -.
DR   Ensembl; ENSMUST00000102743; ENSMUSP00000099804; ENSMUSG00000037533.
DR   MGI; MGI:2384761; Rapgef6.
DR   HOVERGEN; HBG056658; -.
DR   OrthoDB; EOG4JHCDT; -.
DR   Bgee; B2RUJ6; -.
DR   Genevestigator; B2RUJ6; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR000159; Ras-assoc.
DR   InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR   InterPro; IPR008937; Ras_GEF.
DR   InterPro; IPR001895; RasGRF_CDC25.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Gene3D; G3DSA:1.10.840.10; RasGRF_CDC25; 1.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 2.
DR   PANTHER; PTHR23113; Ras_GEF; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   SMART; SM00100; cNMP; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00314; RA; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00229; RasGEFN; 1.
DR   SUPFAM; SSF51206; cNMP_binding; 2.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50212; RASGEF_NTER; 1.
PE   2: Evidence at transcript level;
KW   Guanine-nucleotide releasing factor.
SQ   SEQUENCE   1606 AA;  179813 MW;  EE2B671210711D30 CRC64;
     MNSPVDPGAR QALRKKPPER TPEDLNIIYS YLHGMEILSN LREHQLRLMS TRARYERYSG
     NQMLFCSETI ARCWYILLSG SVLVKDSMVL PPCSFGKQFG GKRGCDCLVL EPSEMIVVEN
     SKDNEDSILQ REIPARQSRR RFRKINYKGE RQTIIDGVDI NNYLSLPADL TKMHLTDNPH
     PQVTHVSSSQ SGCSIASDSG SSSLSDIYQA TESEVGDVDL TRLPEGPVDS EDEEEEEEEI
     DRTDPLQGRD LVRECLEKEP ADKTDDDVEQ LLEFMHQLPA FANMTMSVRR ELCSVMVFEV
     VEQAGAVILE DGQELDSWYV ILNGTVEISH PDGKIENLFM GNSFGIVPTL DKQHMHGAVR
     TKVDDCQFVC IAQQDYWRIL NHVEKNTHKV EEEGEIVMVH EHRELDRSGT RKGHIVIKAT
     PERLIMHLIE EHSIVDPTYI EDFLLTYRTF LETPLDVGIK LLEWFKIDNL RDKVTRIVLL
     WVNNHFNDFE GDPAMTQFLE EFERNLEDTK MNGHLRLLNI ACAAKAKWRQ VVLQKASRES
     PLHFCLTGGS EKGFGVFVEE VESGSKAADA GLKRGDQVME VNGQNFENIT LAKALEILRN
     NTHLALTVKT NIFVFKELLS RTEQEKSGVP HIPKIAEKKS NRHSIQDVPG DMEQAPQEKG
     NKKIKANTVS GGRNKIRKIL DKTRFSILPP KLFSDGGLSQ SQDDSIVGTR HCRHSLAIMP
     IPGTLSSSSP DLLQPTTSML DFSNPSAVGF YYIPDQVIRV FKADQQSCYI IISKDTTAKE
     VVCQAVQEFG LTGASDTYSL CEVSVTPEGV IKQRRLPDQF SKLADRIQLN GRYYLKNNME
     TETLCSDEDA QELLKESQLS MLQLSTIEVA TQLSMRDFDL FRNIEPTEYI DDLFKLDSKT
     GNTHLKQFED IVNQETFWVA SEILSESNQL KRMKIIKHFI KIALHCRECK NFNSMFAIIS
     GLNLAPVARL RGTWEKLPSK YEKHLQDLQD LFDPSRNMAK YRNILSSQSM QPPIIPLFPV
     VKKDMTFLHE GNDSKVDGLV NFEKLRMIAK EIRHIIRMTS ANMDPAMMFR QRSLSQGSTN
     SNMLDVQGGA HKKRARRSSL LNAKKLYEDA QMARKVKQYL SSLDIDTDEE KFQMMSLQWE
     PAYGTLTKNL TEKRSAKSSE MSPVPLRSVG QTAKVHLHQP HRVSQVLQVP AVNLHPIRKK
     GQAKDHVLST SLPQKGLGPT EEVSVKKHTE DTISVASSLH SSPPASPQNS PRKGYTLTPS
     SKCDNLSDSS HSEISSRSSI VSNGSVDSMS AAGQDERCSS HSLAVPEPTG ALEKTDHPSG
     ISDHSQLAHG WMLSKPCLIK GVAVSSSLSS EEMSHEHVVL EAADSGRGSW TSCSSSSHDN
     FQSLQNQKSW DFLNSYRHMH LDDPIAEVEP TDCEPCACPK GCSRTCGQCK GSLETNQLRQ
     SWASSSSLSD TCEPNYGTVK RRVLESAPAE APDGLEPRDT TDPVYKTVTS STDKGLIVYC
     VTSPKKGDRY REPPPTPPGY LGISLADLKE GPHPHLKPPD YSVAVQRSKM MLNSLSRLPP
     APPSSHTSAW VPSKIGSQPQ RHSHPKLADV ADADSEADEN EQVSAV
//
ID   B2RUR8_MOUSE            Unreviewed;       840 AA.
AC   B2RUR8;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 28.
DE   SubName: Full=OTU domain containing 7B;
DE   SubName: Full=OTU domain containing 7B, isoform CRA_a;
GN   Name=Otud7b; ORFNames=mCG_122520;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 OTU domain.
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DR   EMBL; BC141397; AAI41398.1; -; mRNA.
DR   EMBL; BC141398; AAI41399.1; -; mRNA.
DR   EMBL; CH466620; EDL38862.1; -; Genomic_DNA.
DR   IPI; IPI00605489; -.
DR   RefSeq; NP_001020784.1; NM_001025613.1.
DR   RefSeq; NP_001020785.1; NM_001025614.1.
DR   UniGene; Mm.272336; -.
DR   ProteinModelPortal; B2RUR8; -.
DR   SMR; B2RUR8; 122-398, 798-827.
DR   MEROPS; C64.001; -.
DR   PRIDE; B2RUR8; -.
DR   Ensembl; ENSMUST00000035519; ENSMUSP00000046413; ENSMUSG00000038495.
DR   Ensembl; ENSMUST00000090785; ENSMUSP00000088291; ENSMUSG00000038495.
DR   Ensembl; ENSMUST00000098849; ENSMUSP00000096449; ENSMUSG00000038495.
DR   GeneID; 229603; -.
DR   KEGG; mmu:229603; -.
DR   CTD; 229603; -.
DR   MGI; MGI:2654703; Otud7b.
DR   HOGENOM; HBG444533; -.
DR   HOVERGEN; HBG050904; -.
DR   InParanoid; B2RUR8; -.
DR   OMA; ATFPRQC; -.
DR   OrthoDB; EOG4BRWK6; -.
DR   NextBio; 379553; -.
DR   Bgee; B2RUR8; -.
DR   Genevestigator; B2RUR8; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016579; P:protein deubiquitination; IDA:MGI.
DR   InterPro; IPR003323; OTU.
DR   InterPro; IPR009060; UBA-like.
DR   InterPro; IPR002653; Znf_A20.
DR   Pfam; PF02338; OTU; 1.
DR   SUPFAM; SSF46934; UBA_like; 1.
DR   PROSITE; PS50802; OTU; 1.
DR   PROSITE; PS51036; ZF_A20; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   840 AA;  91983 MW;  B63C06B656CC02EE CRC64;
     MTLDMDAVLS DFVRSTGAEP GLARDLLEGK NWDVSAALSD FEQLRQVHAG NLSPPFSGGS
     TCPKTPEKGG SDREPTRPSR PILQRQDDVI QEKRLSRGIS HASSSIVSLA RSHVSSNGGG
     GGSSEHPLEM PICAFQLPDL TVYKEDFRSF IERDLIEQSM LVALEQAGRL NWWVSMDSTC
     QRLLPLATTG DGNCLLHAAS LGMWGFHDRD LVLRKALYAL MEKGVEKEAL RRRWRWQQTQ
     QNKESGLVYT EDEWQKEWNE LIKLASSEPR MHLGSNGASG GGVESSEEPV YESLEEFHVF
     VLAHVLKRPI VVVADTMLRD SGGEAFAPIP FGGIYLPLEV PASQCHRSPL VLAYDQAHFS
     ALVSMEQKES AKEQAVIPLT DSEHKLLPLH FAVDPGKGWE WGKDDNDNVR LASIILSLEV
     KLHLLHSYMN VKWIPLSSDS QAPLAQPESP TASAGDEPRS TPESGESDKE SVGSSSLGNE
     GSRRKEKSKR DREKDKKRAD SVANKLGSFG KTLGSKLKKN MGGLMHSKGP KPGGLGSGSG
     ISSGTETLEK KKKNNTLKSW KGGKEEAAGD GPVSEKPPSE SVGNGGSKYS QEVMQSLSTM
     RIAMQGEGKY IFVGTLKMGH RHQYQEEMIQ RYLADAEERF LAEQKQKEVE RKIMNGGLVS
     GPPPAKKPEP DGGEDQPSDS PAEPKAMAFS TAYPGGFTIP RPSGGGVHCQ EPRRQLAGGP
     CVGGLPSYAT FPRQYPGRPY PHQDNIPALE PGKDGVHRGA LLPPQFRVAD SYSNGYREPP
     EPDGWAGAPR GLPPTQTKCK QPNCSFYGHP ETNNLCSCCY REELRRRERE PGGELLAHRF
//
ID   B2RUS0_MOUSE            Unreviewed;      1337 AA.
AC   B2RUS0;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 25.
DE   SubName: Full=Transient receptor potential cation channel, subfamily M, member 3;
GN   Name=Trpm3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC141400; AAI41401.1; -; mRNA.
DR   EMBL; BC141412; AAI41413.1; -; mRNA.
DR   IPI; IPI00654972; -.
DR   RefSeq; NP_796315.2; NM_177341.4.
DR   UniGene; Mm.131943; -.
DR   UniGene; Mm.397699; -.
DR   UniGene; Mm.440339; -.
DR   ProteinModelPortal; B2RUS0; -.
DR   STRING; B2RUS0; -.
DR   Ensembl; ENSMUST00000037901; ENSMUSP00000042184; ENSMUSG00000052387.
DR   GeneID; 226025; -.
DR   KEGG; mmu:226025; -.
DR   CTD; 226025; -.
DR   MGI; MGI:2443101; Trpm3.
DR   HOVERGEN; HBG055663; -.
DR   NextBio; 377921; -.
DR   Bgee; B2RUS0; -.
DR   Genevestigator; B2RUS0; -.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005216; F:ion channel activity; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR005821; Ion_trans.
DR   Pfam; PF00520; Ion_trans; 1.
PE   2: Evidence at transcript level;
KW   Ion transport; Ionic channel; Membrane; Receptor; Transmembrane;
KW   Transport.
SQ   SEQUENCE   1337 AA;  154069 MW;  1A164537E3885CEF CRC64;
     MPGPWGTVYF LGTAQICSFL SSRWNLEGVM NQTDASRPLN WTIRKLCHAA FLPSVRLLKA
     QKSWIERAFY KRECVHIIPS TKDPHRCCCG RLIGQHVGLT PSISVLQNEK NESRLSRNDI
     QSEKWSISKH TQLSPTDAFG TIEFQGGGHS NKAMYVRVSF DTKPDLLLHL MTKEWQLELP
     KLLISVHGGL QNFELQPKLK QVFGKGLIKA AMTTGAWIFT GGVNTGVIRH VGDALKDHAS
     KSRGKICTIG IAPWGIVENQ EDLIGRDVVR PYQTMSNPMS KLTVLNSMHS HFILADNGTT
     GKYGAEVKLR RQLEKHISLQ KINTRIGQGV PVVALIVEGG PNVISIVLEY LRDTPPVPVV
     VCDGSGRASD ILAFGHKYSE EGGLINESLR DQLLVTIQKT FTYTRTQAQH LFIILMECMK
     KKELITVFRM GSEGHQDIDL AILTALLKGA NASAPDQLSL ALAWNRVDIA RSQIFIYGQQ
     WPVGSLEQAM LDALVLDRVD FVKLLIENGV SMHRFLTISR LEELYNTRHG PSNTLYHLVR
     DVKKREYPGF GWIYFKGNLP PDYRISLIDI GLVIEYLMGG AYRCNYTRKR FRTLYHNLFG
     PKRPKALKLL GMEDDIPLRR GRKTTKKREE EVDIDLDDPE INHFPFPFHE LMVWAVLMKR
     QKMALFFWQH GEEAMAKALV ACKLCKAMAH EASENDMVDD ISQELNHNSR DFGQLAVELL
     DQSYKQDEQL AMKLLTYELK NWSNATCLQL AVAAKHRDFI AHTCSQMLLT DMWMGRLRMR
     KNSGLKVILG ILLPPSILSL EFKNKDDMPY MTQAQEIHLQ EKEPEEPEKP TKEKDEEDME
     LTAMLGRSNG ESSRKKDEEE VQSRHRLIPV GRKIYEFYNA PIVKFWFYTL AYIGYLMLFN
     YIVLVKMERW PSTQEWIVIS YIFTLGIEKM REILMSEPGK LLQKVKVWLQ EYWNVTDLIA
     ILLFSVGMIL RLQDQPFRSD GRVIYCVNII YWYIRLLDIF GVNKYLGPYV MMIGKMMIDM
     MYFVIIMLVV LMSFGVARQA ILFPNEEPSW KLAKNIFYMP YWMIYGEVFA DQIDPPCGQN
     ETREDGKTIQ LPPCKTGAWI VPAIMACYLL VANILLVNLL IAVFNNTFFE VKSISNQVWK
     FQRYQLIMTF HERPVLPPPL IIFSHMTMIF QHVCCRWRKH ESDQDERDYG LKLFITDDEL
     KKVHDFEEQC IEEYFREKDD RFNSSNDERI RVTSERVENM SMRLEEVNER EHSMKASLQT
     VDIRLAQLED LIGRMATALE RLTGLERAES NKIRSRTSSD CTDAAYIVRQ SSFNSQEGNT
     FKLQESIDPA EHPFYSV
//
ID   B2RUS7_MOUSE            Unreviewed;      1588 AA.
AC   B2RUS7;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 31.
DE   SubName: Full=ATP-binding cassette, sub-family C (CFTR/MRP), member 8;
GN   Name=Abcc8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
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DR   EMBL; BC141411; AAI41412.1; -; mRNA.
DR   IPI; IPI00624726; -.
DR   RefSeq; NP_035640.2; NM_011510.3.
DR   UniGene; Mm.259076; -.
DR   ProteinModelPortal; B2RUS7; -.
DR   SMR; B2RUS7; 1084-1585.
DR   STRING; B2RUS7; -.
DR   PRIDE; B2RUS7; -.
DR   Ensembl; ENSMUST00000033123; ENSMUSP00000033123; ENSMUSG00000040136.
DR   GeneID; 20927; -.
DR   KEGG; mmu:20927; -.
DR   CTD; 20927; -.
DR   MGI; MGI:1352629; Abcc8.
DR   HOGENOM; HBG758042; -.
DR   HOVERGEN; HBG101342; -.
DR   InParanoid; B2RUS7; -.
DR   OMA; ALYQHTN; -.
DR   OrthoDB; EOG4K6G3C; -.
DR   NextBio; 299841; -.
DR   Bgee; B2RUS7; -.
DR   Genevestigator; B2RUS7; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro.
DR   GO; GO:0008281; F:sulfonylurea receptor activity; IEA:InterPro.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR017940; ABC_transporter_type1.
DR   InterPro; IPR001140; ABC_transptr_TM_dom.
DR   InterPro; IPR011527; ABC_transptrTM_dom_typ1.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR000388; Sulphorea_rcpt.
DR   InterPro; IPR000844; Surea_rcpt-1.
DR   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   PRINTS; PR01093; SULFNYLUR1.
DR   PRINTS; PR01092; SULFNYLUREAR.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF90123; ABC_TM_1; 2.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding; Repeat.
SQ   SEQUENCE   1588 AA;  178071 MW;  661159D6319EFD53 CRC64;
     MPLAFCGTEN HSAAYRVDQG VLNNGCFVDA LNVVPHVFLL FITFPILFIG WGSQSSKVHI
     HHSTWLHFPG HNLRWILTFM LLFVLVCEIA EGILSDGVTE SRHLHLYMPA GMAFMAAITS
     VVYYHNIETS NFPKLLIALL IYWTLAFITK TIKFVKFYDH AIGFSQLRFC LTGLLVILYG
     MLLLVEINVI RVRRYIFFKT PREVKPPEDL QDLGVRFLQP FVNLLSKGTY WWMNAFIKTA
     HRKPIDLRAI GKLPIAMRAL TNYQRLCAAF DAQARKDTQS QQGARAIWRA LCHAFGRRLV
     LSSTFRILAD LLGFAGPLCI FGIVDHLGKE NHVFQPKTQF LGVYFVSSQE FLGNAYVLAV
     LLFLALLLQR TFLQASYYVA IETGINLRGA IQTKIYNKIM HLSTSNLSMG EMTAGQICNL
     VAIDTNQLMW FFFLCPNLWA MPVQIIVGVI LLYYILGVSA LIGAAVIILL APVQYFVATK
     LSQAQRSTLE YSNERLKQTN EMLRGIKLLK LYAWENIFCS RVEMTRRKEM TSLRAFAVYT
     SISIFMNTAI PIAAVLITFV GHVSFFKESD FSPSVAFASL SLFHILVTPL FLLSSVVRST
     VKALVSVQKL SEFLSSAEIR EEQCAPREPA PQGQAGKYQA VPLKVVNRKR PAREEVRDLL
     GPLQRLTPSM DGDADNFCVQ IIGGFFTWTP DGIPTLSNIT IRIPRGQLTM IVGQVGCGKS
     SLLLATLGEM QRVSGAVFWN SSLPDSEGED PRYCLRTSNP ERETAADSDA RSRGPVAYAS
     QKPWLLNATV EENITFESPF NKQRYKMVIE ACSLQPDIDI LPHGDQTQIG ERGINLSGGQ
     RQRISVARAL YQHTNVVFLD DPFSALDVHL SDHLMQAGIL ELLRDDKRTV VLVTHKLQYL
     PHADWIIAMK DGTIQREGTL KDFQRSECQL FEHWKTLMNR QDQELEKETV MERKAPEPSQ
     GLPRAMSSRD GLLLDEDEEE EEAAESEEDD NLSSVLHQRA KIPWRACTKY LSSAGVLLLS
     LLVFSQLLKH MVLVAIDYWL AKWTDSALVL SPAARNCSLS QECALDQSVY AMVFTVLCSL
     GIALCLVTSV TVEWTGLKVA KRLHRSLLNR IILAPMRFFE TTPLGSILNR FSSDCNTIDQ
     HIPSTLECLS RSTLLCVSAL TVISYVTPVF LVALLPLAVV CYFIQKYFRV ASRDLQQLDD
     TTQLPLLSHF AETVEGLTTI RAFRYEARFQ QKLLEYTDSN NIASLFLTAA NRWLEVRMEY
     IGACVVLIAA ATSISNSLHR ELSAGLVGLG LTYALMVSNY LNWMVRNLAD MEIQLGAVKR
     IHTLLKTEAE SYEGLLAPSL IPKNWPDQGK IQIQNLSVRY DSSLKPVLKH VNALIAPGQK
     IGICGRTGSG KSSFSLAFFR MVDMFEGRII IDGIDIAKLP LHTLRSRLSI ILQDPVLFSG
     TIRFNLDPEK KCSDSTLWEA LEIAQLKLVV KALPGGLDAI ITEGGENFSQ GQRQLFCLAR
     AFVRKTSIFI MDEATASIDM ATENILQKVV MTAFADRTVV TIAHRVHTIL SADLVMVLKR
     GAILEFDKPE KLLSQKDSVF ASFVRADK
//
ID   ZCH24_MOUSE             Reviewed;         241 AA.
AC   B2RVL6;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   30-NOV-2010, entry version 22.
DE   RecName: Full=Zinc finger CCHC domain-containing protein 24;
GN   Name=Zcchc24;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 CCHC-type zinc finger.
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DR   EMBL; CH466613; EDL01418.1; -; Genomic_DNA.
DR   EMBL; BC147263; AAI47264.1; -; mRNA.
DR   EMBL; BC147264; AAI47265.1; -; mRNA.
DR   IPI; IPI00660294; -.
DR   RefSeq; NP_001094903.1; NM_001101433.1.
DR   UniGene; Mm.41904; -.
DR   ProteinModelPortal; B2RVL6; -.
DR   SMR; B2RVL6; 126-151.
DR   PhosphoSite; B2RVL6; -.
DR   PRIDE; B2RVL6; -.
DR   GeneID; 71918; -.
DR   KEGG; mmu:71918; -.
DR   CTD; 71918; -.
DR   MGI; MGI:1919168; Zcchc24.
DR   eggNOG; roNOG16852; -.
DR   HOVERGEN; HBG089647; -.
DR   NextBio; 334948; -.
DR   Genevestigator; B2RVL6; -.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR013084; Znf_CCH_retrovir.
DR   InterPro; IPR001878; Znf_CCHC.
DR   Gene3D; G3DSA:4.10.60.10; Znf_CCH_retrovir; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Phosphoprotein; Zinc; Zinc-finger.
FT   CHAIN         1    241       Zinc finger CCHC domain-containing
FT                                protein 24.
FT                                /FTId=PRO_0000351149.
FT   ZN_FING     132    149       CCHC-type.
FT   MOD_RES      65     65       Phosphoserine (By similarity).
FT   MOD_RES      93     93       Phosphoserine (By similarity).
SQ   SEQUENCE   241 AA;  26961 MW;  04B29B3B6A73F306 CRC64;
     MSLLSAIDTS AASVYQPAQL LNWVYLSLQD THQASAFDAF RPEPPAGAAP PELAFGKGRP
     EQLGSPLHSS YLNSVFQLQR GEALSSSVYR NASPYGSLNN IADGLSSLTE HFSDLTLTSE
     ARKPSKRPPP NYLCHLCFNK GHYIKDCPQA RPKGEGLTPY QGKKRCFGEY KCPKCKRKWM
     SGNSWANMGQ ECIKCHINVY PHKQRPLEKP DGLDVSDQSK EHPQHLCEKC KVLGYYCRRV
     Q
//
ID   B2RW11_MOUSE            Unreviewed;       495 AA.
AC   B2RW11;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 24.
DE   SubName: Full=Ankyrin repeat domain 34A;
GN   Name=Ankrd34a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC147489; AAI47490.1; -; mRNA.
DR   EMBL; BC150865; AAI50866.1; -; mRNA.
DR   IPI; IPI00754546; -.
DR   RefSeq; NP_001020022.2; NM_001024851.3.
DR   UniGene; Mm.267664; -.
DR   ProteinModelPortal; B2RW11; -.
DR   PRIDE; B2RW11; -.
DR   Ensembl; ENSMUST00000058943; ENSMUSP00000102707; ENSMUSG00000049097.
DR   GeneID; 545554; -.
DR   KEGG; mmu:545554; -.
DR   CTD; 545554; -.
DR   MGI; MGI:3617846; Ankrd34a.
DR   GeneTree; ENSGT00390000012355; -.
DR   HOGENOM; HBG444529; -.
DR   HOVERGEN; HBG100441; -.
DR   InParanoid; B2RW11; -.
DR   OMA; YLNSPPS; -.
DR   OrthoDB; EOG42FSHR; -.
DR   NextBio; 412722; -.
DR   Bgee; B2RW11; -.
DR   Genevestigator; B2RW11; -.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 2.
DR   SMART; SM00248; ANK; 4.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
PE   2: Evidence at transcript level;
KW   ANK repeat; Repeat.
SQ   SEQUENCE   495 AA;  52450 MW;  9F9C5782ACC11237 CRC64;
     MLHTEGHALL RAVGQGKLRL ARLLLEGGAY VNEGDAQGET ALMAACRARY DDPQNKARMV
     RYLLEQGADP NIADRLGRTA LMHACAGGGG AAVASLLLAH GADPSVRDHA GASALVHALD
     RGDRETLATL LDACKAKGTE VIIITTDTSP SGTKKTRQYL NSPPSPGVED PAPAPPSPGV
     CTSPSEVQLQ TAGGGRGLLS PRAQEEEEKR DIFEFPLPKP PDDPSPSEPL PKPPRHPPKP
     LKRLNSEPWG LVAPPQPVPP AEGRPGLERL AAEFNGLTLT GRPRLSRRHS TEGPEDPPPW
     AEKVTGGGPL SRRNTAPEAQ ESGLPSGLRQ KLSRMEPVEL DTPGHFCPDS PESSRLSLER
     RRYSASPLTL PPAGSVSSPR QSQESLPGAV SPLSGRRRSP GLLERRGSGT LLLDHISQTR
     PGFLPPLNVS PHPPIPDIRP QPGGRAPSLP APPPSGAPGS PRTKRKLVRR HSMQTEQIRL
     LGGFQSLGGP GEPGR
//
ID   B2RWJ3_MOUSE            Unreviewed;       173 AA.
AC   B2RWJ3;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   30-NOV-2010, entry version 16.
DE   SubName: Full=EG381582 protein;
DE   SubName: Full=MCG23350;
GN   Name=Gm5151; Synonyms=EG381582; ORFNames=mCG_23350;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC147820; AAI47821.1; -; mRNA.
DR   EMBL; BC147826; AAI47827.1; -; mRNA.
DR   EMBL; CH466594; EDL15027.1; -; Genomic_DNA.
DR   IPI; IPI00855133; -.
DR   RefSeq; NP_001094976.1; NM_001101506.1.
DR   UniGene; Mm.379515; -.
DR   PRIDE; B2RWJ3; -.
DR   GeneID; 381582; -.
DR   KEGG; mmu:381582; -.
DR   MGI; MGI:3648074; Gm5151.
DR   HOVERGEN; HBG107552; -.
DR   NextBio; 402278; -.
DR   Genevestigator; B2RWJ3; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   173 AA;  20005 MW;  FA1980811EBB4D62 CRC64;
     MSMSANTMIF MILGASIVMA IACLMDMNAL LDRFHNYILP HLRGEDRVCH CNCGRHHIHY
     VIPYDGDQSV VDASENYFVT DNVTKQEIDL MLGLLLGFCI SWFLVWMDGV LHCAVRAWRA
     GRRYDGSWTW LPKLCSLREL GRRPHRPFEE PTGNMVHVKQ KLYHNGHPSP RHL
//
ID   B2RWR8_MOUSE            Unreviewed;      1262 AA.
AC   B2RWR8;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 19.
DE   SubName: Full=Myosin VI;
GN   Name=Myo6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC144917; AAI44918.1; -; mRNA.
DR   EMBL; BC150673; AAI50674.1; -; mRNA.
DR   IPI; IPI00623496; -.
DR   UniGene; Mm.4040; -.
DR   ProteinModelPortal; B2RWR8; -.
DR   SMR; B2RWR8; 2-825.
DR   STRING; B2RWR8; -.
DR   Ensembl; ENSMUST00000035889; ENSMUSP00000036181; ENSMUSG00000033577.
DR   MGI; MGI:104785; Myo6.
DR   HOVERGEN; HBG003523; -.
DR   OrthoDB; EOG46HG8W; -.
DR   Bgee; B2RWR8; -.
DR   Genevestigator; B2RWR8; -.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IPI:MGI.
DR   GO; GO:0012506; C:vesicle membrane; IPI:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:motor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0042491; P:auditory receptor cell differentiation; IMP:MGI.
DR   GO; GO:0016358; P:dendrite development; IMP:MGI.
DR   GO; GO:0006897; P:endocytosis; IMP:MGI.
DR   GO; GO:0014047; P:glutamate secretion; IMP:MGI.
DR   GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0006605; P:protein targeting; IPI:MGI.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR   GO; GO:0007416; P:synapse assembly; IMP:MGI.
DR   GO; GO:0007268; P:synaptic transmission; IMP:MGI.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 1.
DR   SMART; SM00242; MYSc; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Motor protein; Myosin; Nucleotide-binding.
SQ   SEQUENCE   1262 AA;  145848 MW;  07CCBC9BD7037230 CRC64;
     MEDGKPVWAP HPTDGFQMGN IVDIGPDSLT IEPLNQKGKT FLALINQVFP AEEDSKKDVE
     DNCSLMYLNE ATLLHNVKVR YSKDRIYTYV ANILIAVNPY FDIPKIYSSD TIKSYQGKSL
     GTMPPHVFAI ADKAFRDMKV LKMSQSIIVS GESGAGKTEN TKFVLRYLTE SYVTGQDIDD
     RIVEANPLLE AFGNAKTVRN NNSSRFGKFV EIHFNEKSSV VGGFVSHYLL EKSRICVQGK
     EERNYHIFYR LCAGASEDIR EKLHLSSPDN FRYLNRGCTR FFANKETDKQ ILQNRKSPEY
     VKAGSLKDPL LDDHGDFIRM CTAMKKIGLD DEEKLDLFRV VAGVLHLGNI DFEEAGSTSG
     GCNLKNKSAP SLEYCAELLG LDQDDLRVSL TTRVMLTTAG GTKGTVIKVP LKVEQANNAR
     DALAKTVYSH LFDHVVNRVN QCFPFETSSY FIGVLDIAGF EYFEHNSFEQ FCINYCNEKL
     QQFFNERILK EEQELYQKEG LGVNEVHYVD NQDCIDLIEV KLVGILDILD EENRLPQPSD
     QHFTSVVHQK HKDHFRLTIP RKSKLAVHRN LRDDEGFIIR HFAGAVCYET TQFVEKNNDA
     LHMSLESLIC ESRDKFIRAL FESSTNNNKD TKQKAGKLSF ISVGNKFKTQ LNLLLDKLRS
     TGASFIRCIK PNLKMTSHHF EGAQILSQLQ CSGMVSVLDL MQGGFPSRAS FHELYNMYKK
     YMPEKLARLD PRLFCKALFK ALGLNEVDYK FGLTKVFFRP GKFAEFDQIM KSDPDHLAEL
     VKRVNLWLVC SRWKKVQWCS LSVIKLKNKI KYRAEACIKM QKTIRMWLCK RRHKPRIDGL
     VKVGTLKKRL DKFNEVVSAL KDGKPEVNRQ IKNLEISIDA LMAKIKSTMM TREQIQKEYD
     ALVKSSEDLL SALQKKKQQE EEAERLRRIQ EEMEKERKRR EEDEERRRKE EEERRMKLEM
     EAKRKQEEEE RKKREDDEKR IQAEVEAQLA RQREEESQQQ AVLAQECRDR ELALRIAQNE
     SELISDEAQG DMALRRGPAV QATKAAAGTK KHDLSKWKYA ELRDTINTSC DIELLAACRE
     EFHRRLKVYH AWKSKNKKRN TETEQRAPKS VTDYDFAPFL NNSPQQNPAA QLPARQQEID
     MKRQQRFFRI PFIRPADQYK DPQNKKKGWW YAHFDGPWIA RQMELHPDKP PILLVAGKDD
     MEMCELNLEE TGLTRKRGAE ILPRQFEEIW ERCGGIQYLQ SAIESRQARP TYATAMLQNL
     LK
//
ID   B2RWR9_MOUSE            Unreviewed;      1081 AA.
AC   B2RWR9;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 23.
DE   SubName: Full=Teashirt zinc finger family member 3;
GN   Name=Tshz3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
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DR   EMBL; BC150674; AAI50675.1; -; mRNA.
DR   IPI; IPI00229585; -.
DR   UniGene; Mm.44141; -.
DR   ProteinModelPortal; B2RWR9; -.
DR   SMR; B2RWR9; 200-303.
DR   STRING; B2RWR9; -.
DR   Ensembl; ENSMUST00000021641; ENSMUSP00000021641; ENSMUSG00000021217.
DR   MGI; MGI:2442819; Tshz3.
DR   HOVERGEN; HBG079626; -.
DR   InParanoid; B2RWR9; -.
DR   Bgee; B2RWR9; -.
DR   Genevestigator; B2RWR9; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0060993; P:kidney morphogenesis; IMP:MGI.
DR   GO; GO:0050881; P:musculoskeletal movement; IMP:MGI.
DR   GO; GO:0051152; P:positive regulation of smooth muscle cell differentiation; IMP:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   GO; GO:0050975; P:sensory perception of touch; IMP:MGI.
DR   GO; GO:0048745; P:smooth muscle tissue development; IMP:MGI.
DR   GO; GO:0001657; P:ureteric bud development; IMP:MGI.
DR   InterPro; IPR001356; Homeobox.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   2: Evidence at transcript level;
KW   DNA-binding; Homeobox; Nucleus.
SQ   SEQUENCE   1081 AA;  118656 MW;  B4A323FE480BDDAF CRC64;
     MPRRKQQAPR RAAAYVSDEL KAAALVEDDV EPEEQAADGE PSAKYMCPEK ELSKACPSYQ
     NSPAAEFSSH EMDSESHISE TSDRMADFES SSIKNEEETK EVQVPLEDTT VSDSLEQMKA
     VYNNFLSNSY WSNLNLNLHQ PSSENNGGSS SSSSSSSSSC GSGSFDWHQS AMAKTLQQVS
     QNRMLPEPSL FSTVQLYRQS SKLYSSIFTG ASKFRCKDCS AAYDTLVELT VHMNETGHYR
     DDNHETDNNN PKRWSKPRKR SLLEMEGKED AQKVLKCMYC GHSFESLQDL SVHMIKTKHY
     QKVPLKEPVT PVAAKIIPAA RKKPSLELEL PSSPDSTGGT PKATLSDASD TLQKNSNPYI
     TPNNRYGHQN GASYAWHFEA RKSQILKCME CGSSHDTLQE LTAHMMVTGH FIKVTNSAMK
     KGKPIMETPV TPTITTLLDE KVQSVPLAAT TFTSPSNTPA SVSPKLAVEI KKEVDKEKAV
     PDEKPKEREK PSEEEEKYDI SSKYHYLTEN DLEESPKGGL DILKSLENTV TSAINKAQNG
     TPSWGGYPSI HAAYQLPNMM KLSLGSSGKS TPLKPMFGNS EIVSPTKTQT LVSPPSSQTS
     PMPKTNFHAM EELVKKVTEK VAKVEEKMKE PEGKLSPPKR ATPSPCSSEQ SEPIKMEASS
     DGGFKSQENS PSPPRDACKE ASPSAEPVEN GKELVKPLSG GLSGSTAIIT DHPPEQPFVN
     PLSALQSVMN IHLGKAAKPS LPALDPMSML FKMSNSLAEK AAVATPPPLQ AKKAEHLDRY
     FYHVNNDQPI DLTKGKSDKG CSLGSGLLSP TSTSPATSSS TVTTAKTSAV VSFMSNSPLR
     ENALSDISDM LKNLTESHTS KSSTPSSISE KSDIDGATLE EAEESTPAQK RKGRQSNWNP
     QHLLILQAQF AASLRQTSEG KYIMSDLSPQ ERMHISRFTG LSMTTISHWL ANVKYQLRRT
     GGTKFLKNLD TGHPVFFCND CASQIRTPST YISHLESHLG FRLRDLSKLS TEQINNQIAQ
     TKSPSEKLVT SSPEEDLGTT YQCKLCNRTF ASKHAVKLHL SKTHGKSPED HLLFVSELEK
     Q
//
ID   B2RWS6_MOUSE            Unreviewed;      2415 AA.
AC   B2RWS6;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 27.
DE   SubName: Full=Ep300 protein;
GN   Name=Ep300;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC144976; AAI44977.1; -; mRNA.
DR   EMBL; BC150681; AAI50682.1; -; mRNA.
DR   IPI; IPI00461822; -.
DR   UniGene; Mm.258397; -.
DR   UniGene; Mm.473354; -.
DR   ProteinModelPortal; B2RWS6; -.
DR   SMR; B2RWS6; 324-424, 567-653, 1044-1160, 1286-1712, 1725-1811, 2051-2093.
DR   STRING; B2RWS6; -.
DR   PRIDE; B2RWS6; -.
DR   Ensembl; ENSMUST00000068387; ENSMUSP00000066789; ENSMUSG00000055024.
DR   MGI; MGI:1276116; Ep300.
DR   HOGENOM; HBG402903; -.
DR   HOVERGEN; HBG000185; -.
DR   InParanoid; B2RWS6; -.
DR   OrthoDB; EOG4Z0B4S; -.
DR   Bgee; B2RWS6; -.
DR   Genevestigator; B2RWS6; -.
DR   GO; GO:0000123; C:histone acetyltransferase complex; IDA:MGI.
DR   GO; GO:0005667; C:transcription factor complex; IDA:MGI.
DR   GO; GO:0004402; F:histone acetyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0016563; F:transcription activator activity; IDA:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; ISS:UniProtKB.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR   GO; GO:0030324; P:lung development; IMP:MGI.
DR   GO; GO:0018076; P:N-terminal peptidyl-lysine acetylation; ISS:UniProtKB.
DR   GO; GO:0009887; P:organ morphogenesis; IMP:MGI.
DR   GO; GO:0051091; P:positive regulation of transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
DR   GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI.
DR   GO; GO:0001756; P:somitogenesis; IGI:MGI.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR010303; DUF902_CREBbp.
DR   InterPro; IPR013178; Histone_H3-K56_AcTrfase_RTT109.
DR   InterPro; IPR003101; KIX.
DR   InterPro; IPR009110; Nuc_rcpt_coact.
DR   InterPro; IPR014744; Nuc_rcpt_coact_CREBbp.
DR   InterPro; IPR000197; Znf_TAZ.
DR   InterPro; IPR000433; Znf_ZZ.
DR   Gene3D; G3DSA:1.20.920.10; Bromodomain; 1.
DR   Gene3D; G3DSA:1.10.246.20; KIX; 1.
DR   Gene3D; G3DSA:1.10.1630.10; Nuc_rcpt_coact_CREBbp; 1.
DR   Gene3D; G3DSA:1.20.1020.10; Znf_TAZ; 2.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF09030; Creb_binding; 1.
DR   Pfam; PF06001; DUF902; 1.
DR   Pfam; PF08214; KAT11; 1.
DR   Pfam; PF02172; KIX; 1.
DR   Pfam; PF02135; zf-TAZ; 2.
DR   Pfam; PF00569; ZZ; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00551; ZnF_TAZ; 2.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF47040; KIX; 1.
DR   SUPFAM; SSF69125; Nuc_recept_coact; 1.
DR   SUPFAM; SSF57933; TAZ_finger; 2.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS50952; KIX; 1.
DR   PROSITE; PS50134; ZF_TAZ; 2.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   2: Evidence at transcript level;
KW   Bromodomain.
SQ   SEQUENCE   2415 AA;  263762 MW;  FBCF19B91EE70A1C CRC64;
     MAENVVEPGP PSAKRPKLSS PALSASASDG TDFGSLFDLE HDLPDELINS TELGLTNGGD
     ISQLQTSLGI VQDAASKHKQ LSELLRSGSS PNLNMGVGGP GQAMASQAQQ NSPGLSLINS
     MVKSPMAQTG LTSPNMGIGS SGPNQGPTQS PAGMMNSPVN QPAMGMNTGM NAGMNPGMLA
     AGNGQGIMPN QVMNGSIGAG RGRPNMQYPN AGMGNAGSLL TEPLQQGSPQ MGGQPGLRGP
     QPLKMGMMNN PSPYGSPYTQ NSGQQIGASG LGLQIQTKTV LPNNLSPFAM DKKAVPGGGM
     PSMGQQPTPS VQQPGLVTPV AAGMGSGAHT ADPEKRKLIQ QQLVLLLHAH KCQRREQANG
     EVRQCNLPHC RTMKNVLNHM THCQSGKSCQ VAHCASSRQI ISHWKNCTRH DCPVCLPLKN
     AGDKRNQQSI LTGAPVGLGN PSSLGVGQQS TPSLSTVSQI DPSSIERAYA ALGLPYQVNQ
     IPPQPQVQAK NQQSQPSGQS PQGMRSVNNM SASPMGVNGG VGVQTPNLLS DSMLHSTINS
     QNPMMSENAG VASLGPLPTA AQPSSTGIRK QWHEDITQDL RNHLVHKLVQ AIFPTPDPAA
     LKDRRMENLV AYARKVEGDM YESANNRAEY YHLLAEKIYK IQKELEEKRR TRLQKQNMLP
     NAPGMGPVPM NTGSNMEQQP TGMTTNGPVP DPSMIRGSVP NHMMPRMTPQ PGLNQFGQMN
     MPQPPIGPRQ PSPLQHHGQL AQSGSLNPPM GYGPRMQQAS GQNQFLSQTQ FTSQGMNVTN
     MPLAPSSGQA PVSQAQMSSS SCPVNSPIMP PGSQGSHIHC PTLPQQAHQN SPSPVPSRTP
     TPHHTPPSIG NQPPPATAIP TPVPTPPAIP PGPQPPSLHP SSRQTPTPPT HLPPQVQPSL
     PAAPSADQSQ QQPRSQQSTA VSVPTPTAPL LPPQPSTPLS QPAVSIEGQV SNPPSTSSTE
     VNSQTIPEKQ PSQEVKMESK MEVDKPEPAD AQPEDTKEAK GEDVKVEPTE MEERGPELKT
     DGKEEEEQPS TSATQSSPAP GQSKKKIFKP EELRQALMPT LEALYRQDPE SLPFRQPVDP
     QLLGIPDYFD IVKSPMDLST IKRKLDTGQY QEPWQYIDDI WLMFNNAWLY NRKTSRVYKY
     CSKLSEVFEQ EIDPVMQSLG YCCGRKLEFS PQTLCCYGKQ LCTIPRDATY YSYQNRYHFC
     EKCFNEIQGE SVSLGDDPSQ PQTTINKEQF SKRKNDTLDP ELFVECTECG RKMHQICVLH
     HEIIWPSGFV CDGCLKKTAR TRKENKLSAK RLPSTRLGTF LENRVNDFLR RQNHPESGEV
     TVRVVHASDK TVEVKPGMKA RFVDSGEMAE SFPYRTKALF AFEEIDGVDL CFFGMHVQEY
     GSDCPPPNQR RVYISYLDSV HFFRPKCLRT AVYHEILIGY LEYVKKLGYT TGHIWACPPS
     EGDDYIFHCH PPDQKIPKPK RLQEWYKKML DKAVSERIVH DYKDILKQAT EDRLTSAKEL
     PYFEGDFWPN VLEESIKELE QEEEERKREE NTSNESTDVT KGDSKNAKKK NNKKTSKNKS
     SLSRGNKKKP GMPNVSNDLS QKLYATMEKH KEVFFVIRLI ACPAPNSLPP IVDPDPLIPC
     DLMDGRDAFL TLARDKHLEF SSLRRAQWST MCMLVELHTQ SQDRFVYTCN ECKHHVETRW
     HCTVCEDYDL CITCYNTKNH DHKMEKLGLG LDDESNNQQA AATQSPGDSR RLSIQRCIQS
     LVHACQCRNA NCSLPSCQKM KRVVQHTKGC KRKTNGGCPI CKQLIALCCY HAKHCQENKC
     PVPFCLNIKQ KLRQQQLQHR LQQAQMLRRR MASMQRTGVA GQQQGLPSPT PATPTTPTGQ
     QPATPQTPQP QPTSQPQPTP PNNMTPYLPR TQTTGPVSQG KAPGQVTPPT PPQTAQAPLP
     GPPPAAVEMA MQIQRAAETQ RQMAHVQIFQ RPIQHQMPQM SPMAPMGMNP PPMARGPGGH
     LDPGIGPAGM QQQPPWAQGG MPQPQQMQSG MPRPAMMSVA QHGQPLNMAP QPGLGQVGVS
     PLKPGTVSQQ ALQNLLRTLR SPSSPLQQQQ VLSILHANPQ LLAAFIKQRA AKYANPNPQP
     LPGQPGMTQG QPGLQPPTMP GQQGVHSNPA LQNMNPLQAG VQRAGLPQQQ PQQQLQPPMG
     AMSPQAQQMN MNHNTMPSQF RDILRRQMMQ QQGAGPGIGP GMANQFQQPQ GIGYPPQQQQ
     QQQQQRMQHH MQQMQQGNMG QMGQLPQALG AEAGASLQAY QQRLLQQQMG SPAQPNPMSP
     QQHMLPNQAQ SPHLQGQQIP NSLSNQVRSP QPVPSPRPQS QPPHSSPSPR MQPQPSPHHV
     SPQTSSPHPG LVAAQAANPM EQGHFASPDQ NSMLSQLASN PGMANLHGAS ATDLGLSSDN
     ADLNSNLSQS TLDIH
//
ID   B2RWU9_MOUSE            Unreviewed;       568 AA.
AC   B2RWU9;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 24.
DE   SubName: Full=CDK5 and Abl enzyme substrate 1;
GN   Name=Cables1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the cyclin family.
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DR   EMBL; BC145142; AAI45143.1; -; mRNA.
DR   EMBL; BC150714; AAI50715.1; -; mRNA.
DR   IPI; IPI00929838; -.
DR   UniGene; Mm.40717; -.
DR   ProteinModelPortal; B2RWU9; -.
DR   STRING; B2RWU9; -.
DR   Ensembl; ENSMUST00000046948; ENSMUSP00000040639; ENSMUSG00000040957.
DR   MGI; MGI:1927065; Cables1.
DR   HOVERGEN; HBG050759; -.
DR   InParanoid; B2RWU9; -.
DR   Bgee; B2RWU9; -.
DR   Genevestigator; B2RWU9; -.
DR   GO; GO:0016538; F:cyclin-dependent protein kinase regulator activity; IEA:InterPro.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:MGI.
DR   GO; GO:0007399; P:nervous system development; IMP:MGI.
DR   GO; GO:0051726; P:regulation of cell cycle; TAS:MGI.
DR   GO; GO:0051302; P:regulation of cell division; IEA:InterPro.
DR   InterPro; IPR012388; Cdk5/c-Abl_linker_prot_cables.
DR   InterPro; IPR006670; Cyclin.
DR   InterPro; IPR011028; Cyclin-like.
DR   InterPro; IPR013763; Cyclin-related.
DR   InterPro; IPR006671; Cyclin_N.
DR   Gene3D; G3DSA:1.10.472.10; Cyclin_related; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   PIRSF; PIRSF025798; Cables; 1.
DR   SMART; SM00385; CYCLIN; 1.
DR   SUPFAM; SSF47954; Cyclin_like; 1.
PE   2: Evidence at transcript level;
KW   Cyclin.
SQ   SEQUENCE   568 AA;  61441 MW;  3584EF1CFB55DF76 CRC64;
     MAAATATAGT AACSSSSSSR GGSTDAAATS GVQPPPPPPA TAPPEPLRKP RMDPRRRQAA
     LSFLTNISLD GRPPLQDHEW GGGEEGGGTK PGARARLSLL AAGCNAFSAP GTAAAPWTAG
     SGSSPCPLPP SLVPRVLGEP SQPPRSAPAV TGAQLQLPDG PGGAGQEELE EDDAFINVQV
     PSASFLGSGT PGSTSGSRGR LNSFTQGILP IAFSRQNSQN YCALEQSGQG GSTSALEQLQ
     RSRRRLISQR SSLETLEDIE ENAPLRRCRT LSGSPRPKNF KKIHFIKNMR QHDTKNGRDL
     KLDGGRQSAG AMSLKEIIGL EGVELGADGK TVSYTQFLLP TNAFGNRRNT IDSTASFSQF
     RSLSHRSLSM GRAGSTQGSL DAGSDLGDFM DYDPNLLDDP QWPCGKHKRV LTFPSYMTTV
     IDYVKPSDLK KDMNETFKEK FPHIKLTLSK IRSLKREMRK LAQEDCGFEE PTVAMAFVYF
     EKLALRGKLN KQNRKLCAGA CVLLAAKVGS DLRKHEVKHL IDKLEEKFRL NRRELIAFEF
     PVLVALEFAL HLPEHEVMPH YRRLIQSS
//
ID   B2RWW1_MOUSE            Unreviewed;       973 AA.
AC   B2RWW1;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   05-OCT-2010, entry version 14.
DE   SubName: Full=Microtubule-associated protein 1S;
GN   Name=Mtap1s;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
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DR   EMBL; BC150729; AAI50730.1; -; mRNA.
DR   IPI; IPI00223621; -.
DR   UniGene; Mm.248559; -.
DR   STRING; B2RWW1; -.
DR   Ensembl; ENSMUST00000019405; ENSMUSP00000019405; ENSMUSG00000019261.
DR   MGI; MGI:2443304; Mtap1s.
DR   HOVERGEN; HBG108117; -.
DR   InParanoid; B2RWW1; -.
DR   Bgee; B2RWW1; -.
DR   Genevestigator; B2RWW1; -.
DR   GO; GO:0005874; C:microtubule; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; IDA:MGI.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   973 AA;  103025 MW;  FCC29F69E1C2DA50 CRC64;
     MAAVMAAPEA VEAPSSLLLL VVGGECGCPG LLAYVMEELE RGVRSWEDVD PAVCSLDEQL
     KAFVSRHSAT FSSIVKGQRS LHHRGETLET LVLLNPSDKS LCDELRNLLM DPAPHKLLVL
     AGPCLEETGE LLLQTGGFSA HHFLQVLGDK EVQDALASAP AAPALTVSCP TFGDWALLGP
     VPGLQLRLNP PAQLPASEGL RAFLEYVAES LEPPSPFELL EPPAAGGFLR LARPCCYVFP
     GGLGDAAFFA VNGFTVLVNG GSNPKSSFWK LVRHLDRVDA VLVTHAGADS LPGLNSLLRR
     KLAEREAAAG PQGQHEERLR RLLSPALGVV FLNAREAASR LRGGEDEAVC ARSLLRSLGI
     APLPLQRGPQ PSCPTVLFEK LGVGRLELFV LHPPPGDPAA PACALLVWQP AAPGDKVVRV
     LFPGRTPPAR LLDGLQRLQH LPCLRRPVVT THDLEAPSRA NSQDSLASRD SARKEPVRGT
     VGSIANRSTV RREPALATRD QKKDTRSGPT RPTARDTRRS GPGVVNTKPR VSQNGPRAPV
     LAAPLTAPVA ECPGEAENIL ESERPPAPSP TLSPAQSPPP TAPGNSPERL SLSPLRPEPA
     PDASPSATTP TLTTPSLPAE LGSPHSTEVD ESLSVSFEQV LPAGDPGLSL PLRLARRSTS
     PHDVDLCLVS PCEFSHRKPP PPASPGSSDS SARSQERPPE TPPTSVSESL PTLSDSDPVP
     VADSDDDAGS ESAARDPPPT PRVPPPLPDV PGICMVDPEA LPPRARQPLN TTNPSRSRKA
     PARPSSASAT PRAATVAAKT KGPAGDRNRP LSARSEPADR PGRVPLTRKP SVPKTVPKMA
     SATRLSSGPS GRPAPLAAGS PVYLDLAYLP GGGAGHLDQN FFLRVRALCY VISGQGQRQE
     EGLRAVLDAL LAGKRQWDLD LQVTLIPTFD SAVMHRWYEE THAQHQALDI RVLGSGSLVS
     MQDEAFPACK VEF
//
ID   B2RWW2_MOUSE            Unreviewed;      3238 AA.
AC   B2RWW2;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   05-OCT-2010, entry version 17.
DE   SubName: Full=Golgb1 protein;
GN   Name=Golgb1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; BC150731; AAI50732.1; -; mRNA.
DR   IPI; IPI00929857; -.
DR   UniGene; Mm.244815; -.
DR   UniGene; Mm.475446; -.
DR   STRING; B2RWW2; -.
DR   PRIDE; B2RWW2; -.
DR   Ensembl; ENSMUST00000039855; ENSMUSP00000045239; ENSMUSG00000034243.
DR   MGI; MGI:1099447; Golgb1.
DR   HOGENOM; HBG506515; -.
DR   HOVERGEN; HBG051756; -.
DR   InParanoid; B2RWW2; -.
DR   Bgee; B2RWW2; -.
DR   Genevestigator; B2RWW2; -.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   3238 AA;  370111 MW;  4C51DE6C3536BBFE CRC64;
     MLSRLSGLAN NVLHELSGDY TDWNLMASSD ADSSQETAME SNNRIMESTQ EDALHRLAEA
     EKLVVELKDI ISQKDVQLQQ KDEALQEEKK AAENKIKKIK LHAKAKIMSL NKHMEEIKTQ
     GGAALPPEAQ AEELSKHNKS STEEEMEIEK IKHELQEKEK LISSLQAQLD QSEQASQLDK
     SSAEMEDFVL MKQQLQEKEE LISTLQTQLS QTQAEQAAQL SSMQQVVREK DARFETQVLL
     HEDELLQLVT QSDVETEMQQ KLRVMQRKLE EHEEALLGRA QVVDLLQKEL TSAEQRNQVL
     SQQLQLLEAE HNTLKNTMET ERQESKTLME KVELEVAERK LSFHNLQEEM HQLQGQLERA
     GQAQADLETQ YSALQQRHKT EMEEKTACIL SLQKNEQELQ SACAALKEEN SKLLQEKHDQ
     AAESAQAMRQ LEDQLQQKSK EISQFVNKPN LQKNETASQT SLPDVNNEGD QAVMEETVAS
     LQKRVVELEN EKGALLLSSG ELEELKAENE KLSSRITLLE AQNRAGEADG TVCEVSTAGT
     TLLNRSDSSP EENGQAVLEN TFSQKHKELS VLLVEMKEAQ EEIAFLKSQL QGKRPEGDYE
     VLDRREVQLM ESEGPPSVTA GDVLCAPSDE SSGPAAEEEQ AGMKDRHRAS EAGPLNDAGM
     ELSSPKLDGV DKSLAVSHVC QCHQGELERL KTQVLELETS LHTAEETYKR NLSEKVKEIS
     SLTQLSEEVK ESAEEARSTL AAVTEERDQL LYQVKELDVL AELRARVQEL ESSLAEAEKQ
     RGLDYESQRA QHNLLTEQIH SLSIEAKSKD VKIEALQREL DGVQLQFCEQ GTQMKTLQSQ
     LEAKEREVRE GTERLRDISQ EMEGLSQALS QKELEIAKMD QLLLEKQKDV ETLQQTIQEK
     DQQVTELSFS MTEKMVQLNE EKFSLGVEIK TLKEQLNLLS RTEEATKEQV EESGAGSSLK
     LGHDESGQEG LQQELELLRK ESEQRKRKLQ AALINRKELL QKVSQLEEEL AKVREDSRKE
     IPFGENERRK LEEDRENRDD PEEWGTSKWR EVEASLKQTI SEKEVELEGI RRDLKEKTAA
     EEELQAVVQR MTRDLQSKTK QIDLLQEEVT ENQATIQKLV TGTMDAGNGG SAAPVKETAA
     SSPPGAGGEE HWKPELEGRI LDLEKDKTQL QKKLQEALIA RKAILKKAQE KEKQLKEELR
     EQKDAYHHLQ GQFHEQNKEK ENIADQLRQL QCQARESIDR QLPGTGQQEP GPPAPSLEGI
     SLEDTEPASE SDLHAAQPSP PGETAALQAT VSVAQIQAQL KEMEVEKEEL ELKVSSIASE
     LAKKSEEVLL LQDQINEQGL EIQNLKAASV EAQAHTELLK QELESSQLKV AGLEHLKTLQ
     PELDALHKHM GQKEEEVNYL YGQLSEKEQT LTTVQTEMVE QERLIKALHT QLEMQAKEHE
     ERLKQAQVEI CELKKKPTEL EEETNAKQQL QRKLQAALIS RKEALKENKS LQEQLSSARD
     AVERLTKSLA DVESQVSVQN QEKDAVLGKL TILQEERDKL IAEMDRFLLE NQSLSGSCES
     LKLALGGLTE DKEKLMEELE SVRSSKMAES TEWQEKHKEL QKEYEVLLQS YENVSNEAER
     IQHVVESVRQ EKQELYAKLR STESDKRERE KQLQDAEQEM EEMKEKMRKF AKSKQQKILE
     LEEENDRLRA EAQPVGGTGE SMEALLSSNS SLKEELEKIT LEHKTLSKEF EALMAEKDAL
     SEETRNLKLQ VEAQVLKQAS LEATEKSDEP KDVIEEVTQA VVGKSQERDA LSDSAKLEDS
     EAILMGDGAK PGVSETFSSH DDIKNYLQQL DQLKGRIAEL EMEKQKDREL SQALENEKNA
     LLTQISAKDS ELKLLEEEVT KRTTLNQQIQ EELCRVTKLK ETAEEEKDDL EERLMNQLAE
     LNGSIGNYYQ DVTDAQIKNE QLESEMRNLQ RCVSELEEEK QQLVKEKTKV ESEIRKEYME
     KIQGAQKGPA NKSHAKELQE LLREKQQEVK QLQKDCIRYL ERISALEKTV KALEFVHTES
     QKDLDVTKGN LAQAVEHRKK AQAELSSFKI LLDDTQSEAA RVLADNLKLK KELQSNKESI
     KSQIKQKDED LLRRLEQAEE KHRKEKKNMQ EKLDALHREK AHVEETLAEI QVSLTRKDQE
     MKELQGSLDS TLAQLAAFTK SMSSLQDDRD RVIDEAKKWE RRFGDAIQTK EEEVRLKEEN
     CIALKDQLRQ MAIHMEELKI TVSRLEHDKE IWESKAQTEL QHHQKAYDKL QEENKELTSQ
     LEDARQLYHD SKNELTKLES ELKSLKDQTT DLNNSLEKCK EHENNLEGII KQQEADIQNC
     KFSCEQLETD LAASRELTSR LHDEINAKEQ KIISLLSGKE EAIQLAVEEL HQQHSKEIKE
     LENLLSQEEE ENVALEEENK RALEKTNQLT EALEAIKKES FEQKAQLDSF VKSMSSLQDD
     RDRIVSDYRQ LEERHLSAIL EKDQLIQDAA AENNKLKEEM RGLRSHMDDL NSENAKLDAE
     LVQYRRDLNE VIAIKDSQQK QLLDAQLQQN KELRNECTKL EERLKGLEAE KQSLQMSSDA
     LQKEKQGLSK EIKNLQTQLT ALQEEGTLGV YHAQLKAKEE ELQRLNMALS SSQKRTADLE
     EELVCVQKEA TRKVSEIEDQ LKKELKHLHH DAGIMRNETE TAEERVAELA RDLVEMEQKL
     LTVTKENKDL MAQIQAFGRS MSSLQDSRDH ATEELGDLKK KYDASLKELA QLKEWQDSSR
     EGDVLSQAAF PLSTSENVLS RLEKLNQQLT SKDEQLLHLS SELESSHNQV QSISKAMTSL
     QNERDRLWSE LEKFRKSEEG KQRAAAPSAA SSPAEVQSLK KAMSSLQNDR DRLLKELKNL
     QQQYLQMSQE MTELRPLKAQ LQESQDQTKA LQVMEEELRQ ENLSWQHELR QLRMEKNSWE
     LHERRMKEQF LMAISDKDQQ LGHLQSLLRE LRSSSQAQIL STQYQRQASP ETSASLDGSQ
     KLVYETELLR TQLNDSLKEI HQKELRIQQL NSKFSQLLEE KNVLSTQLSD ASQSLRENQH
     HYSNLFNHCA ILEKEVQKLQ AGPLNTDVAP GAPQEKNGMH RKSEPETTGE EQPSFSEVQQ
     QLCNTKQDLR ELKKLLEEER DQRLTAENAL SLAKEQIRRL EHSEWESART PIMGACGSQE
     QALLIDLPGH SCRRTRSGAG WKRVLRSLCH SRTRVPLLAA IYFLMIHVLL VLCFTGHL
//
ID   B2RWX1_MOUSE            Unreviewed;      1954 AA.
AC   B2RWX1;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 27.
DE   SubName: Full=Arhgap21 protein;
GN   Name=Arhgap21;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; BC150741; AAI50742.1; -; mRNA.
DR   IPI; IPI00918972; -.
DR   UniGene; Mm.28507; -.
DR   UniGene; Mm.465492; -.
DR   ProteinModelPortal; B2RWX1; -.
DR   SMR; B2RWX1; 53-164, 928-1045, 1145-1342.
DR   STRING; B2RWX1; -.
DR   Ensembl; ENSMUST00000154230; ENSMUSP00000122497; ENSMUSG00000036591.
DR   MGI; MGI:1918685; Arhgap21.
DR   HOVERGEN; HBG106694; -.
DR   InParanoid; B2RWX1; -.
DR   Bgee; B2RWX1; -.
DR   Genevestigator; B2RWX1; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   2: Evidence at transcript level;
KW   GTPase activation.
SQ   SEQUENCE   1954 AA;  216806 MW;  7B1DDF7BC1317500 CRC64;
     MATHWTGLPE EDGDKLKACG AASACEVSKN KDGKDQGEPV SPSEDEPFSW PGPKTVMLKR
     TSQGFGFTLR HFIVYPPESA IQFSYKDEEN GNRGGKQRNR LEPMDTIFVK QVKEGGPAFE
     AGLCTGDRII KVNGESVIGK TYSQVIALIQ NSDTTLELSV MPKDEDILQV LQFTKDVTAL
     AYSQDAYLKG NEAYSGNARN IPEPPPVCYP WLPSTPSATA QPVETCPPDS LPNKQQTSAP
     VLTQPGRAYR MEIQVPPSPT DVAKSNTAVC VCNESVRTVI VPSEKVVDLL ANRNNPSGPS
     HRTEEVRYGV NEQASTKAAS RTTSPASVPT AHLIHQTTGS RSLEPSGILL KSGNYSGHSE
     GISSSRSQAV DSPPVSVNHY SANSHQHIDW KNYKTYKEYI DNRRLHIGCR TIQERLDSLR
     AASQSAADYN QVVPTRTTLQ VRRRSTSHDR VPQSVQIRQR SVSQERLEDS VLMKYCPRSA
     SQGALTSPPV SFNNHRTRSW DYIEGQTEAT ATVNSESQIP DSNGERKQTY KWSGFTEQDD
     RRGIHERPRQ QEMHKPFRGS NLTVAPVVNS DNRRLVGRGV GPVSQFKKIP PDLRPPHSNR
     NFPTTTGVSL QRGIAQDRSP LVKVRSNSLK VPPPPVSKPS FSQHSLASMK DQRPVNHLHQ
     HSVLSQQTQF RSESTFEHQL ETEVSSCLPG TSAKTSPQLS ENLGTSDLEL PAIPRNGDIN
     LQEAEIQQPD VLDNKESVIL REKPQSGRQT PQPLRHQSYI LAVNDQETGS DTTCWLPNDA
     RREVHIKRME ERKASSTSPP GDSLASIPFI DEPTSPSIDH EIAHIPASAV ISASTAHVPS
     IATVPPSLTT SAPLIRRQLS HDQESVGPPS LDGQHSSKTE RSKSYDEGLD DYREDAKLSF
     KHVSSLKGIK ITDSQKSSED SGSRKGSSSE VFSDAAREGW LQFRPLVTDK GKRVGGSIRP
     WKQMYVVLRG HSLYLYKDRR EQTTPSEEEQ PISVNACLID ISYSETKRRN VFRLTTSDCE
     CLFQAEDRDD MLSWIKTIQE SSNLNEEDTG VTNRDLISRR IKEYNSLLSK TEQLPKTPRQ
     SLSIRQTLLG AKSEPKTQSP HSPKEESERK LLSKDDTSPP KDKGTWRRGI PSIVRKTFEK
     KPAATGTFGV RLDDCPPAHT NRYIPLIVDI CCKLVEERGL EYTGIYRVPG NNAAISSMQE
     ELNKGMADID IQDDKWRDLN VISSLLKSFF RKLPEPLFTN DKYADFIEAN RKEDPLDRLR
     TLKRLIHDLP EHHFETLKFL SAHLKTVAEN SEKNKMEPRN LAIVFGPTLV RTSEDNMTHM
     VTHMPDQYKI VETLIQHHDW FFTEEGAEEP LTAVQEENTV DSQPVPNIDH LLTNIGRTGV
     LPGDVSDSAT SDSAKSKGSW GSGKDQYSRE LLVSSIFAAA SRKRKKPKEK AQPSSSEDEL
     DSVFFKKENT EQSHSEIKEE SKRESETSGS KQRVVVAKES NTKKDSGTTK EEKKIPWEEP
     SPPHSSKRNR SPTLSCRLAM LKEGPRSLLT QKPHCEETGS DSGTLLSTSS QASLLRSSTK
     KSTSPETKHS EFLSIAGTTT SDYSTTSSTT YLTSLDSSRL SPEVQSVAES KGDEADDERS
     ELVSEGRPVE TDSESEFPVF PATLTSDRLF RGKFQDVARV SRRNSEGSEA SCTEGSLTPS
     LDSRRQQFSS HRLIECDTLS RKKSARFKSD SGSPGDTRTE KETPALAKMF DVMKKGKSTG
     SLLTPSRSES EKQEATWKTK IADRLKLRPR APADDMFGVG NQKPTAETAK RKNIKRRHTL
     GGHRDATEIS VLSFWKAHEQ SADKESELSA VNRLKPKCSA QDLSISDWLA RERVRTSASD
     LSRGEGLEPQ AESPSVLGTP ISTHSPPSQQ PEARVAATST LASTSQSPLF TPPQSPDQIN
     RESFQNMSQN ASSTANIHPH KQSESPDTKA ETPP
//
ID   B2RWX5_MOUSE            Unreviewed;      2414 AA.
AC   B2RWX5;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   05-OCT-2010, entry version 13.
DE   SubName: Full=Centrosomal protein 250;
GN   Name=Cep250;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC150746; AAI50747.1; -; mRNA.
DR   IPI; IPI00606583; -.
DR   UniGene; Mm.288729; -.
DR   STRING; B2RWX5; -.
DR   Ensembl; ENSMUST00000094421; ENSMUSP00000091988; ENSMUSG00000038241.
DR   MGI; MGI:108084; Cep250.
DR   HOVERGEN; HBG081320; -.
DR   Bgee; B2RWX5; -.
DR   Genevestigator; B2RWX5; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   2414 AA;  276851 MW;  FE8BB418C6776DE9 CRC64;
     METGSPGLNM KPQSLQLVLE GQVLALQQQM AENQAASWRK LKNSQEAQKR QATLVRKLQA
     KVLQYRSWCQ DLEKRLEATG GLIPQRWESV EEPNLEQLLI RLEEEQQRCE SLVEVNTELR
     LHMEKADVVN KALQEDVEKL TVDWSRARDE LVRKESQWRM EQEFFKGYLR GEHGRLLNLW
     REVVTFRRHF LKMKSATDRD LTELKAEHAR LSGSLLTCCL RLTLRAQSRE SSGSGRTEES
     EPARLLLLVA KTQALEKEAH EKSQELMQLK SHGDLEKAEL QDRVTELSAL LTQSQKQNED
     YEKMVKALRE TMEILETNHA ELMEHEASLS RNAQEEKLSL QQVIKAITQA LASVEEEDTV
     TQSSGHEDLL QSDCNGLSQF DPQDPDRALT LVQSVLTRRQ QAVQDLRQQL SGCQEAMSFL
     QQQRDQWEEE GRALRERLQK LTGERDALAG QTVDLQGEVD SLSRERELLQ KARGELQQQL
     EVLEQEAWRL RRMNMELQLQ GDSAQGERLE QQEELHLAVR ERERLQETLV GLEAKQSESL
     SELLTLREAL ESSRLEGELL KQERVEVAAA LARAEQSIVE LSGSENSLKA EVADLRAAAV
     KLGALNEALA LDKVGLNQQL LQLEQENQSL CSRVEAAEQL RSALRVDLAE AERRREALWE
     KKTQLETQLQ KAEEAGAELQ AELRGTREEK EELKDKLSEA HHQQETATAH LEQLHQDAER
     QEETLARAVQ EKEALVRERA ALEVRLQAVE RDRQDLTEHV LGLRSAKEQL ESNLFEAQQQ
     NSVIQVTKGQ LEVQIQTIIQ AKEVIQGEVK CLKLELDAER TRAEQERDAV ARQLAQAEQE
     GQASLERQKV AHEEEVNRLQ EKWEKERSWL QQELDKTLET LERERAELET KLREQQTEME
     AIRTQREEER SQADSALYQM QLETEKERVS LLETLLRTQK ELADASQQLE RLRQDMKIQK
     LKEQETTGML QAQLQETQQE LKEAAQQHRD DLAAFQKDKL DLQKQVEDLM SQLVAHDDSQ
     RLVKEEIEEK VKVAQECSRI QKELEKENAS LALSLVEKEK RLLILQEAYS VRQQELSSLR
     QDIQEAQEGQ RELGVQVELL RQEVKEKEAD FVAREAQLLE ELEASRVAEQ QLRASLWAQE
     AKATQLQLQL RSTESQLEAL VAEQQPENQA QAQLASLCSV LQQALGSACE SRPELRGGGD
     SAPTLWGPDP DQNGASRLFK RGSLPTALSP EAVALALQKL HQDVWKARQA RDDLRDQVQK
     LVQRLTDTEA QKSQVHSELQ DLQRQLSQSQ EEKSKWEGRQ NSLESELRDL HETAASLQSR
     LRQAELQKME AQNDRELLQA SKEKLSAQVE HLQACVAEAQ AQAGAAPVLE EDLRTARSAL
     KLKNEELESE RERAQALQEQ GELKVAQGKA LQENLALLAQ TLSNREREVE TLQAEVQELE
     KQREMQKAAL ELLSLDLKKR SREVDLQQEQ IQELEQCRSV LEHLPMAVQE REQKLSVQRD
     QIRELENDRE AQRSVLEHQL LDLEQKAQVI ESQRGQIQDL KKQLGTLECL ALELEESHHK
     VESQQKMITE LEGQREIQRV ALTHLTLDLE ERSQELQAQS SQLHELENHS THLAKELQER
     DQEVTSQRQQ IDELQKQQEQ LAQALERKGQ ELVLQKERIQ VLEDQRTLQT KILEEDLEQI
     KHSLRERSQE LASQRQLVHE RADDGKSPSK GQRGSLEHLK LILRDKEKEV ECQQERIQEL
     QGHMGQLEQQ LQGLHRKVGE TSLLLTHREQ ETATLQQHLQ EAKEQGELRE QVLQGQLEEA
     QRDLAQRDHE LETLRQEKQQ TQDQEESMKL KTSALQAALE QAHATLKERQ GELEEHREQV
     RRLQEELEVE GRQVRALEEV LGDLRAESRE HEKAVLALQQ RCAEQAQEHE AEARTLQDSW
     LQAQATLTEQ EQELAALRAE NQYSRRQEEA AVSQAEALQE ALSKAQAALQ EKEQSLLEQA
     ELSHTLEAST AALQATLDTC QARARQLEEA LRIREGEIQA QALQHHEVTQ HLQQELCQKE
     EELRQLLEKA GARRSQENGI QEKQSLEQER QEETRRLLES LKELQLTVAQ REEEILMLRE
     ASSPSHRALP AEKPALQPLP AQQELERLQT ALRQTEAREI EWREKAQDLA LSLAQSKASI
     SSLQEITMFL QASVLERESE QQRLQEELVL SRQALEEQQS GGPHSTSRAD QGPKVGQESQ
     PGEVETEPSP GVEEKERLTQ RLERLQQAVA ELEVDRSKLQ CHNAQLRTAL EQVERERRKL
     KRDSVRASRA GSLEARETMT SSPTQQDGRG SQRGSSDSVL VVELQREVAL LRAQLALERK
     QRQDYIARSV QTSRELAGLH HSLSHSLLTV AQAPEATVLE AETRKLDESL NQSLTSPGPC
     LLHPSLDTTQ NTHR
//
ID   B2RWX7_MOUSE            Unreviewed;      2273 AA.
AC   B2RWX7;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 21.
DE   SubName: Full=Calcium channel, voltage-dependent, R type, alpha 1E subunit;
GN   Name=Cacna1e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; BC150750; AAI50751.1; -; mRNA.
DR   IPI; IPI00331064; -.
DR   UniGene; Mm.267517; -.
DR   ProteinModelPortal; B2RWX7; -.
DR   STRING; B2RWX7; -.
DR   Ensembl; ENSMUST00000004214; ENSMUSP00000004214; ENSMUSG00000004110.
DR   MGI; MGI:106217; Cacna1e.
DR   HOGENOM; HBG713873; -.
DR   HOVERGEN; HBG050763; -.
DR   InParanoid; B2RWX7; -.
DR   Bgee; B2RWX7; -.
DR   Genevestigator; B2RWX7; -.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; TAS:MGI.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:MGI.
DR   GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR   GO; GO:0048266; P:behavioral response to pain; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0002027; P:regulation of heart rate; IMP:MGI.
DR   GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:MGI.
DR   GO; GO:0090273; P:regulation of somatostatin secretion; IMP:MGI.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR   GO; GO:0030317; P:sperm motility; IMP:MGI.
DR   GO; GO:0019226; P:transmission of nerve impulse; IMP:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005449; VDCC_R_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF57; RVDCCAlpha1; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01633; RVDCCALPHA1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Calcium channel; Calcium transport; Ion transport;
KW   Ionic channel; Membrane; Transmembrane; Transport;
KW   Voltage-gated channel.
SQ   SEQUENCE   2273 AA;  257240 MW;  4D6456A9E04ECFB4 CRC64;
     MARFGEAVVV GRPGSGDGDS DQSRNRQGTP VPASGPAAAY KQSKAQRART MALYNPIPVR
     QNCFTVNRSL FIFGEDNIVR KYAKKLIDWP PFEYMILATI IANCIVLALE QHLPEDDKTP
     MSRRLEKTEP YFIGIFCFEA GIKIVALGFI FHKGSYLRNG WNVMDFIVVL SGILATAGTH
     FNTHVDLRTL RAVRVLRPLK LVSGIPSLQI VLKSIMKAMV PLLQIGLLLF FAILMFAIIG
     LEFYSGKLHR ACFMNNSGIL EGFDPPHPCG VQGCPAGYEC KDWIGPNDGI TQFDNILFAV
     LTVFQCITME GWTTVLYNTN DALGATWNWL YFIPLIIIGS FFVLNLVLGV LSGEFAKERE
     RVENRRAFMK LRRQQQIERE LNGYRAWIDK AEEVMLAEEN KNSGTSALEV LRRATIKRSR
     TEAMTRDSSD EHCVDISSVG TPLARASIKS TKVDGASYFR HKERLLRISI RHMVKSQVFY
     WIVLSVVALN TACVAIVHHN QPQWLTHLLY YAEFLFLGLF LLEMSLKMYG MGPRLYFHSS
     FNCFDFGVTV GSIFEVVWAI FRPGTSFGIS VLRALRLLRI FKITKYWASL RNLVVSLMSS
     MKSIISLLFL LFLFIVVFAL LGMQLFGGRF NFNDGTPSAN FDTFPAAIMT VFQILTGEDW
     NEVMYNGIRS QGGVSSGMWS AIYFIVLTLF GNYTLLNVFL AIAVDNLANA QELTKDEQEE
     EEAFNQKHAL QKAKEVSPMS APNMPSIERD RRRRHHMSMW EPRSSHLRER RRRHHMSVWE
     QRTSQLRRHM QMSSQEALNK EEAPPMNPLN PLNPLSPLNP LNAHPSLYRR PRPIEGLALG
     LGLEKCEEER ISRGGSLKGD IGGLTSALDN QRSPLSLGKR EPPWLPRSCH GNCDPIQQEA
     GGGETVVTFE DRARHRQSQR RSRHRRVRTE GKDSASASRS RSASQERSLD EGVSVEGEKE
     HEPHSSHRSK EPTIHEEERT QDLRRTNSLM VPRGSGLVGA LDEAETPLVQ PQPELEVEKD
     AALTEQEAEG SSEQALLGDV QLDVGRGISQ SEPDLSCMTA NMDKATTEST SVTVAIPDVD
     PLVDSTVVNI SNKTDGEASP LKEAETKEEE EEVEKKKKQK KEKRETGKAM VPHSSMLIFS
     TTNPIRRACH YIVNLRYFEM CILLVIAASS IALAAEDPVL TNSERNKVLR YFDYVFTGVF
     TFEMVIKMID QGLILQDGSY FRDLWNILDF VVVVGALVAF ALANALGTNK GRDIKTIKSL
     RVLRVLRPLK TIKRLPKLKA VFDCVVTSLK NVFNILIVYK LFMFIFAVIA VQLFKGKFFY
     CTDSSKDTEK ECIGNYVDHE KNKMEVKGRE WKRHEFHYDN IIWALLTLFT VSTGEGWPQV
     LQHSVDVTEE DRGPSRSNRM EMSIFYVVYF VVFPFFFVNI FVALIIITFQ EQGDKMMEEC
     SLEKNERACI DFAISAKPLT RYMPQNRHTF QYRVWHFVVS PSFEYTIMAM IALNTVVLMM
     KYYSAPCTYE LALKYLNIAF TMVFSLECVL KVIAFGFLNY FRDTWNIFDF ITVIGSITEI
     ILTDSKLVNT SGFNMSFLKL FRAARLIKLL RQGYTIRILL WTFVQSFKAL PYVCLLIAML
     FFIYAIIGMQ VFGNIKLDEE SHINRHNNFR SFFGSLMLLF RSATGEAWQE IMLSCLGEKG
     CEPDTTAPSG QNESERCGTD LAYVYFVSFI FFCSFLMLNL FVAVIMDNFE YLTRDSSILG
     PHHLDEFVRV WAEYDRAACG RIHYTEMYEM LTLMSPPLGL GKRCPSKVAY KRLVLMNMPV
     AEDMTVHFTS TLMALIRTAL DIKIAKGGAD RQQLDSELQK ETLAIWPHLS QKMLDLLVPM
     PKASDLTVGK IYAAMMIMDY YKQSKVKKQR QQLEEQKNAP MFQRMEPSSL PQEIIANAKA
     LPYLQQDPVS GLSGRSGYPS MSPLSPQEIF QLACMDPADD GQFQEQQSLV VTDPSSMRRS
     FSTIRDKRSN SSWLEEFSME RSSENTYKSR RRSYHSSLRL SAHRLNSDSG HKSDTHRSGG
     RERGRSKERK HLLSPDVSRC NSEERGTQAD WESPERRQSR SPSEGRSQTP NRQGTGSLSE
     SSIPSISDTS TPRRSRRQLP PVPPKPRPLL SYSSLMRHTG GISPPPDGSE GGSPLASQAL
     ESNSACLTES SNSLHPQQGQ HPSPQHYISE PYLALHEDSH ASDCGEEETL TFEAAVATSL
     GRSNTIGSAP PLRHSWQMPN GHYRRRRRGG PGPGMMCGAV SDLLSDTEED DKC
//
ID   B2RWY1_MOUSE            Unreviewed;       682 AA.
AC   B2RWY1;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 25.
DE   SubName: Full=p21 (CDKN1A)-activated kinase 6;
GN   Name=Pak6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SIMILARITY: Contains 1 CRIB domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; BC150754; AAI50755.1; -; mRNA.
DR   IPI; IPI00119508; -.
DR   UniGene; Mm.241857; -.
DR   ProteinModelPortal; B2RWY1; -.
DR   SMR; B2RWY1; 4-66, 386-675.
DR   STRING; B2RWY1; -.
DR   Ensembl; ENSMUST00000099557; ENSMUSP00000097153; ENSMUSG00000074923.
DR   Ensembl; ENSMUST00000110853; ENSMUSP00000106477; ENSMUSG00000074923.
DR   MGI; MGI:2679420; Pak6.
DR   HOVERGEN; HBG108518; -.
DR   InParanoid; B2RWY1; -.
DR   Bgee; B2RWY1; -.
DR   Genevestigator; B2RWY1; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000095; PAK_box_Rho-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00786; PBD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00285; PBD; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding;
KW   Serine/threonine-protein kinase; Transferase.
SQ   SEQUENCE   682 AA;  74911 MW;  56CD9F3F168C31B6 CRC64;
     MFRKKKKKRP EISAPQNFQH RVHTSFDPKE GKFVGLPPQW QNILDTLRRP KPVVDPSRIT
     RVQLQPMKTV VRGSSVPTEG YISGLLNDIQ KLSVISSNTL RGRSPTSRRR AQSLGLLGDD
     QWAADPDMYL QSPQSEHTDP HGLYLSCNGG TPAGHRQVPW PEPQSPQALP NGMAAKAQSL
     GPAEFQGASQ RCLQQLGACL QSSPPGTSLP MATGRRGVKV AKHSSEEARP QSCLVGSAIG
     RPGGEGSPSP KNQESSLKHR LFRSMFLSTP ATGAASSSKP VPLPQNKPNS AFRPPQKDSS
     SNLVAKAQSL PSEQPMGTFS PLTTSDTSSP QKSLRTVPAA GPLPGRSSPA GSPRTRHAQI
     STSNLYLPQD PTVAKGALGG EDTGIVTHEQ FKAALRMVVD QGDPRLLLDS YVKIGEGSTG
     IVCLAREKHS GRQVAVKMMD LRKQQRRELL FNEVVIMRDY QHLNVVEMYK SYLVGEELWV
     LMEFLQGGAL TDIISQVRLN EEQIATVCEA VLQALAYLHA QGVIHRDIKS DSILLTLDGR
     VKLSDFGFCA QISKDVPKRK SLVGTPYWMA PEVISRSLYA TEVDIWSLGI MVIEMVDGEP
     PYFSDSPVQA MKRLRDSAPP KLKNSYKVSP VLRDFLDRML VREPQERATA QELLDHPFLL
     QTGLPECLVP LIQLYRKQTS TC
//
ID   B2RX08_MOUSE            Unreviewed;      2329 AA.
AC   B2RX08;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 21.
DE   SubName: Full=Spectrin beta 1;
GN   Name=Spnb1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC150783; AAI50784.1; -; mRNA.
DR   IPI; IPI00131376; -.
DR   UniGene; Mm.32881; -.
DR   ProteinModelPortal; B2RX08; -.
DR   SMR; B2RX08; 45-288, 1064-1273, 1869-2005, 2182-2287.
DR   STRING; B2RX08; -.
DR   Ensembl; ENSMUST00000021458; ENSMUSP00000021458; ENSMUSG00000021061.
DR   MGI; MGI:98387; Spnb1.
DR   HOGENOM; HBG357452; -.
DR   HOVERGEN; HBG057912; -.
DR   InParanoid; B2RX08; -.
DR   Bgee; B2RX08; -.
DR   Genevestigator; B2RX08; -.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0008091; C:spectrin; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0006779; P:porphyrin biosynthetic process; IMP:MGI.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR016343; Spectrin_bsu.
DR   InterPro; IPR001605; Spectrin_PH.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00435; Spectrin; 16.
DR   PIRSF; PIRSF002297; Spectrin_beta_subunit; 1.
DR   PRINTS; PR00683; SPECTRINPH.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00150; SPEC; 17.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Repeat.
SQ   SEQUENCE   2329 AA;  268105 MW;  C79A170471BA902F CRC64;
     MTSATEFENV GNQPPFSRIN ARWDAPDDEL DNDNSSARLF ERSRIKALAD EREVVQKKTF
     TKWVNSHLAR VSCRISDLYK DLRDGRMLIK LLEVLSGEML PRPTKGKMRI HCLENVDKAL
     QFLKEQRVHL ENMGSHDIVD GNHRLVLGLI WTIILRFQIQ DIVVQTQEGR ETRSAKDALL
     LWCQMKTAGY PHVNVTNFTS SWKDGLAFNA LIHKHRPDLI DFDKLKDSNA RHNLEHAFDV
     AERQLGIIPL LDPEDVFTEN PDEKSIITYV VAFYHYFSKM KVLAVEGKRV GKVIDHAIET
     EKMIEKYSGL ASDLLTWIEQ TISVLNSRKF ANSLSGVQQQ LQAFSTYRTV EKPPKFQEKG
     NLEVLLFTIQ SRMRANNQKV YTPHDGKLVS DINRAWESLE EAEYQRELAL RSELIRQEKL
     EQLARRFDRK AAMRETWLNE NQRLVTQDNF GYDLAAVEAA KKKHEAIETD TAAYEERVKA
     LEDLAQELEK ENYHDQKRII ARKDNILRLW SYLQELLRSR RQRLEATLAL QKLFQDMLHS
     IDWMDEIKAH ILSAEFGKHL LEVEDLLQKH KLMEADIAIQ GDKVKAITAA TLQFAEGKGY
     QPCDPQVIQD RVSHLEQCFS ELSNMAAGRK AQLEQSKRLW KFFWEMDEAE SWIKEKEQIY
     SSLDYGKDLT SVLILQRKHK AFEDELRGLD AHLKQIFQEA DDMVAQKQFG HPQIETRVKE
     VSAQWDHLKE LAAFRKKDLQ DAENFFQFQG DADDLKAWLQ DAHRLLSGED VGQDEGATRA
     LGKKHKEFLE ELEESRGVME HLEHQAQGFP EEFRDSPDVT NRLQALRKLY QQVLTQAELR
     GHKLQEALDL YTVFGESDAC ELWMTEKGKW LDQMDIPNTL EDLEVVQHRF DILDQEMKTL
     MAQIDGVNLA ANNLVESGHP RSGEVKQYQD RLNKRWQAFQ AVVSEQREAV DSALRVNNYC
     VDCEETSKWI MDKTKVVEST KDLGQDLAGV IAIQRKLSGL ERDVLAIRDR VSALERESQY
     LMESHPEQKE DIGQRQADVE KLWKGLQDAL QGQELSLGEA SKLQAFLQDL DDFKAWLSMA
     QKAVASEDMP ESLPEAEQLL QQHAAIKEEI DAHRDDYHRV KASGEKVIEG QTDPDYQLLG
     QRLEGLDTDW DALRRMWESR GNTLTQCLGF QEFQKDAKQA EAILSNQEYT LAHLEPPDSL
     AAAEAGIRKF EDFLVSMENN RDKILSPVDS GNKLVAEGNL YSNKIMEKVQ LIEDRHKKNN
     EKAQEATVLL KDNLELQNFL QNCKELTLWI NDKLLTSPDV SYDEARNLHN KWMKHQAFMA
     ELASHQGWLE NIDAEGRQLM AEKPQFKDVV SERLEALHKL WEELQSTAKA KAEQLSAARS
     SDLRLQTHAD LNKWIGAMED QLRSDDLGKD LTTVNRMLAK LKRVEEQVNL RKEELEELFA
     DAPSLGAEAG DTDMSIEKRF LDLLEPLGRR KKQLELSKAK LQISRDLEDE TLWVEERLPL
     AQSADYGTNL QTVQLFMKKN QTLQNEILGH APRVEDVLRR GQELVKAAEI DCQDIEERLG
     HLQSSWDTLR EAAAGRLQRL RDAHEAQQYY LDAGEAEAWI SEQELYVFSD EPPKDEEGAI
     VMLKRHLRQQ RTVEEYGRNI KQLAGRAQSL LSAGHPEGEQ IIRLQGQVDK QYAGLKDMAE
     ERRRRLENMY HLFQLKREAD DLEQWITEKE MVASSQEMGQ DFDHVTMLRD KFRDFARETG
     AIGQERVDNV NTIIERLIDA GHSEAATIAE WKDGLNDMWA DLLELIDTRM QLLAASYDLH
     RYFYTGTEIL GLIDEKHREL PEDVGLDAST AESFHRVHTA FERELHLLGV QVQQFQDVAT
     RLQTAYAGEK ADAIQSKEQE VSAAWQALLD ACAGRRAQLV DTADKFRFFS MVRDLLSWME
     SIIRQIETQE RPRDVSSVEL LLKYHQGIKA EINTRAKNFS TCLELGESLL QRQHQASEEI
     REKLQQVISR RQEMNDKWEA RSDRLHMLLE VCQFSRDASV AEAWLIAQEP YLASRDFGHT
     VDSVEKLIKR HEAFEKSTAS WAERFAALEK PTTLELKERQ TPERPTEEPG PQEEEGETAG
     EAPQVHHAAT ERTSPGEERG PWPQDLQPPP LPGHHKDEQE KSVGDERPAT EPLFKVLDTP
     LSEGDEPTTL PAQRDLGHTV QMEGYLGRKH DLEGPNKKAS NRSWNNLYCV LRNSQLTFYK
     DAKNLALGVP YHGEEPLALR HAICEIAVNY KKKKHVFKLR LSNGSEWLFH GKDEEEMLMW
     LQSMSTAINE SQSIRVKAQS LPLPSLAGPD ASVGKKEKEK RFSFFPKKK
//
ID   B2RX09_MOUSE            Unreviewed;      1503 AA.
AC   B2RX09;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 23.
DE   SubName: Full=Nrxn2 protein;
GN   Name=Nrxn2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC145496; AAI45497.1; -; mRNA.
DR   EMBL; BC150784; AAI50785.1; -; mRNA.
DR   IPI; IPI00467429; -.
DR   UniGene; Mm.329616; -.
DR   UniGene; Mm.414022; -.
DR   UniGene; Mm.440261; -.
DR   ProteinModelPortal; B2RX09; -.
DR   SMR; B2RX09; 285-663, 715-897, 1122-1325.
DR   STRING; B2RX09; -.
DR   Ensembl; ENSMUST00000113462; ENSMUSP00000109089; ENSMUSG00000033768.
DR   MGI; MGI:1096362; Nrxn2.
DR   HOVERGEN; HBG052670; -.
DR   InParanoid; B2RX09; -.
DR   OrthoDB; EOG41G339; -.
DR   Bgee; B2RX09; -.
DR   Genevestigator; B2RX09; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005246; F:calcium channel regulator activity; IGI:MGI.
DR   GO; GO:0007269; P:neurotransmitter secretion; IGI:MGI.
DR   GO; GO:0007416; P:synapse assembly; IGI:MGI.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR012680; Laminin_G_2.
DR   InterPro; IPR003585; Neurexin-like.
DR   Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 6.
DR   Pfam; PF02210; Laminin_G_2; 6.
DR   SMART; SM00294; 4.1m; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00282; LamG; 6.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 6.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 6.
PE   2: Evidence at transcript level;
KW   EGF-like domain; Membrane; Repeat; Transmembrane; Transmembrane helix.
SQ   SEQUENCE   1503 AA;  163087 MW;  1B395E966B58FA57 CRC64;
     MALGSRWQPP PQLPPLLLLL ALAAGVRGLE FGGGPGQWAR YARWAGAAST GELSFSLRTN
     ATRALLLYLD DGGDCDFLEL LLVDGRLRLR FTLSCAEPAT LQLDTPVADD RWHMVLLTRD
     ARRTALAVDG EARAAEVRSK RREMQVASDL FVGGIPPDVR LSALTLSTVK YEPPFRGLLA
     NLKLGERPPA LLGSQGLRGA AADPLCAPAR NPCANGGLCT VLAPGEVGCD CSHTGFGGKF
     CSEEEHPMEG PAHLTLNSEV GSLLFSEGGA GRGGAGDVHQ PTKGKEEFVA TFKGNEFFCY
     DLSHNPIQSS TDEITLAFRT LQRNGLMLHT GKSADYVNLS LKSGAVWLVI NLGSGAFEAL
     VEPVNGKFND NAWHDVRVTR NLRQVTISVD GILTTTGYTQ EDYTMLGSDD FFYIGGSPNT
     ADLPGSPVSN NFMGCLKDVV YKNNDFKLEL SRLAKEGDPK MKLQGDLSFR CEDVAALDPV
     TFESPEAFVA LPRWSAKRTG SISLDFRTTE PNGLLLFSQG RRAGAGVGSH SSTQRADYFA
     MELLDGYLYL LLDMGSGGIK LRASSRKVND GEWCHVDFQR DGRKGSISVN SRSTPFLATG
     ESEVLDLESE LYLGGLPEGG RVDLPLPPEV WTAALRAGYV GCVRDLFIDG RSRDLRGLAE
     AQGAVGVAPF CSRETLKQCA LAPCRNGGIC REGWNRFVCD CIGTGFLGRV CEREATVLSY
     DGSMYMKIML PTAMHTEAED VSLRFMSQRA YGLMMATTSR ESADTLRLEL DGGQMRLTVN
     LDCLRVGCAP SKGPETLFAG HKLNDNEWHT VRVVRRGKSL QLSVDNVTVE GQMAGAHTRL
     EFHNIETGIM TERRFISVVP SNFIGHLSGL VFNGQPYMDQ CKDGDITYCE LNARFGLRAI
     VADPVTFKSR SSYLALATLQ AYASMHLFFQ FKTTAPDGLL LFNSGNGNDF IVIELVKGYI
     HYVFDLGNGP SLMKGNSDKP VNDNQWHNVV VSRDPGNVHT LKIDSRTVTQ HSNGARNLDL
     KGELYIGGLS KNMFSNLPKL VASRDGFQGC LASVDLNGRL PDLIADALHR IGQVERGCDG
     PSTTCTEESC ANQGVCLQQW DGFTCDCTMT SYGGPVCNDP GTTYIFGKGG ALITYTWPPN
     DRPSTRMDRL AVGFSTHQRS AVLVRVDSAS GLGDYLQLHI DQGTVGVIFN VGTDDITIDE
     PNAIVSDGKY HVVRFTRSGG NATLQVDSWP VNERYPAGNF DNERLAIARQ RIPYRLGRVV
     DEWLLDKGRQ LTIFNSQAAI KIGGRDQGRP FQGQVSGLYY NGLKVLALAA ESDPNVRTEG
     HLRLVGEGPS VLLSAETTAT TLLADMATTI METTTTMATT TTRRGRSPTM RDSTTQNTDD
     LLVASAECPS DDEDLEECEP STANPTGPGE RGPPGAVEVI RESSSTTGMV VGIVAAAALC
     ILILLYAMYK YRNRDEGSYQ VDQSRNYISN SAQSNGAVVK EKAPAAPKTP SKAKKNKDKE
     YYV
//
ID   B2RX11_MOUSE            Unreviewed;      1742 AA.
AC   B2RX11;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 25.
DE   SubName: Full=Kinase non-catalytic C-lobe domain (KIND) containing 1;
GN   Name=Kndc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 Ras-GEF domain.
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CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC150787; AAI50788.1; -; mRNA.
DR   IPI; IPI00380321; -.
DR   UniGene; Mm.44442; -.
DR   ProteinModelPortal; B2RX11; -.
DR   STRING; B2RX11; -.
DR   Ensembl; ENSMUST00000053445; ENSMUSP00000050586; ENSMUSG00000066129.
DR   MGI; MGI:1923734; Kndc1.
DR   HOVERGEN; HBG108658; -.
DR   InParanoid; B2RX11; -.
DR   Bgee; B2RX11; -.
DR   Genevestigator; B2RX11; -.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
DR   GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; IDA:MGI.
DR   GO; GO:0021707; P:cerebellar granule cell differentiation; IMP:MGI.
DR   GO; GO:0048814; P:regulation of dendrite morphogenesis; IDA:MGI.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR011019; KIND.
DR   InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR   InterPro; IPR001895; RasGRF_CDC25.
DR   Gene3D; G3DSA:1.10.840.10; RasGRF_CDC25; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   SMART; SM00750; KIND; 2.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51377; KIND; 2.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50212; RASGEF_NTER; 1.
PE   2: Evidence at transcript level;
KW   Kinase; Transferase.
SQ   SEQUENCE   1742 AA;  191395 MW;  07C2C977ED7619B1 CRC64;
     MQAMDPASRG FYEEDGKDLD FYDFEPLPTL PEDEENVSLA DILSLRDRGL SEQEAWAVCL
     ECSLSMRSVA HAAIFQTLCI TPDTLAFNTS GNVCFMEQLS DDPEGAFVPP EFDLTGNTFE
     AHIYSLGATL KAALEYVPEP ELEPKLSTDL EGLLSQMQAE DPRERPDLAS IIALCEEKMQ
     PVSSCRLCRS LSAIGRRVLS IESFGAFQEL SENTWRGRPA PRNVGPKKMP GDLSTDPEAL
     FPSKGLLQPP ASRDAEQEAG QRPRAPSPKP LLSAPVRNGE NPGQEGLADL VLDARCPLGE
     LDRDNLRRSR LKKAQTFPRL LQESTETSTL CLSLNGSRNQ LAISEFFPPD PRKLFLEGKN
     GLSGFKTQSK SRLWPEQEPG VQLDKTPGAG RNPHRSPGAS GQLEASSPSQ GSVEYKPSPS
     PVDAGDLDHE GHIPRSEEKI PEESRQPGST ATEQSLSLKD LLSKLGRPFR EYELWALCLS
     CLSTLQTHKE HPAHLCLDNV LVAEDGTVFF GPPPANGAYN SLFLAPEVSE EKLVTEKASV
     YCVAAVLWTA AKFSVPRDHK LALPRRLKTL LLDMARRHAS ERPSAAEAIK VCSSYLLQRG
     MDSSKILAHL RASTCKVHPE EETIGLQNAF SVVELKSTTA PAPESSPGFL QVSNDTKLVA
     VPGPVPGLPP CCKEACELPA AFTSEATHFK PIVLAQDASV TRDQLALPSE SNEKPKEGSG
     HLDREGTRKQ AALELVEATD LKMSNQLSPG PELQGATPDP DGDSGSPSSA TECSCPHGPV
     LVTQQKGTSG TPSSPASSLP PEHRPDGEGP LDTTVLPGPT SASQGSRHPC KPPRGKAAAS
     PSSPRGSDGH PEKPRPADRK LCPSSVDTSS PPKMTACPSL QEAMRLIQEE FAFDGYMDNG
     LEALIMGEYI YALKDLTFAT FCGAISEKFC DLYWDEQLLK NLFKVVNGPA SPSESTSEEP
     GSQPEHSPSR CSLSSKRPSL HGLGKEKPAT TWGSGGPCSP TALSDIDSDT LSQGNFEVGF
     RSQKSIKVTR EQQPEAEVGG QPGPSQDSTS HASDTVARLA RSEDGGPAGS PGASDFQNCS
     PGWSSAFYEA DCFGADVYNY VKDLERQKAN GHTELEAQSP ELEQQLMIEK RNYRKTLKFY
     QKLLQKEKRN KGSEVRTMLS KLRGQLDEMK SKVQFLSLVK KYLQVMYAER WGLEPCALPV
     IVNIAAAPCD TLDFSPLDES SSLIFYNVNK HPGSGRQKKA RILQAGTPLG LMAYLYSSDA
     FLEGYVQQFL YTFRYFCTPH DFLHFLLDRI SSTLSRAHQD PTSTFTKIYR RSLCVLQAWV
     EDCYTVDFIR NAGLLGQLED FISSKILPLD GTAEHLLALL EVGTERRADS ASRGADLEDP
     KEAEEDTRPF NALCKRFSED GITRKSFSWR LPRGNGLVLP HHKERQYTIA SALPKPCFFE
     DFYGPYAKAS EKGPYFLTEY STNQLFTQLT LLQQELFQKC HPVHFLNSRA LGVMDKSAAI
     PKASSSESLS AKTCSLFLPN YVQDKYLLQL LRNADDVSTW VAAEIVTSHT SKLQVNLLSK
     FLLIAKSCYE QRNFATAMQI LGGLEHLAVR QSPAWRILPA KIAEVMEELK AVEVFLKSDS
     LCLMEGRRFR AQPTLPSAHL LAMHIQQLET GGFTMTNGAH RWSKLRNIAK VASQVHAFQE
     NPYTFSPDPK LQAHLKQRIA RFSGADVSIL AADNRANFHQ IPGEKHSRKI QDKLRRMKAT
     FQ
//
ID   CSPP1_MOUSE             Reviewed;        1205 AA.
AC   B2RX88; C7SBE3; C7SBE4; Q8CCQ4; Q8VE83; Q9CQD5;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   08-MAR-2011, entry version 24.
DE   RecName: Full=Centrosome and spindle pole associated protein 1;
GN   Name=Cspp1; Synonyms=Cspp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J;
RA   Asiedu M., Wu D., Matsumura F., Wei Q.;
RT   "Centrosome/spindle pole-associated protein (CSPP) regulates
RT   cytokinesis via promoting the recruitment of MyoGEF to the central
RT   spindle.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6).
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 6).
RC   STRAIN=Czech II; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in cell-cycle-dependent microtubule
CC       organization (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome (By
CC       similarity). Cytoplasm, cytoskeleton, spindle (By similarity).
CC       Note=Associated with mitotic spindles (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=B2RX88-1; Sequence=Displayed;
CC       Name=2; Synonyms=Cspp2;
CC         IsoId=B2RX88-2; Sequence=VSP_040073, VSP_040079;
CC       Name=3; Synonyms=Cspp3;
CC         IsoId=B2RX88-3; Sequence=VSP_040074, VSP_040077, VSP_040078;
CC       Name=4;
CC         IsoId=B2RX88-4; Sequence=VSP_040074;
CC       Name=5;
CC         IsoId=B2RX88-5; Sequence=VSP_040075, VSP_040076;
CC       Name=6;
CC         IsoId=B2RX88-6; Sequence=VSP_040074, VSP_040075, VSP_040076;
CC   -!- PTM: Phosphorylated. Phosphorylation increases in colcemide-
CC       treated cells (By similarity).
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; FJ008677; ACM46986.1; -; mRNA.
DR   EMBL; FJ008676; ACM46985.1; -; mRNA.
DR   EMBL; AK013065; BAB28630.1; -; mRNA.
DR   EMBL; AK015133; BAB29721.1; -; mRNA.
DR   EMBL; AK032310; BAC27806.1; -; mRNA.
DR   EMBL; AC102570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC159972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466536; EDL14300.1; -; Genomic_DNA.
DR   EMBL; CH466536; EDL14303.1; -; Genomic_DNA.
DR   EMBL; BC019581; AAH19581.1; -; mRNA.
DR   EMBL; BC151042; AAI51043.1; -; mRNA.
DR   IPI; IPI00357493; -.
DR   IPI; IPI00761285; -.
DR   IPI; IPI00785424; -.
DR   IPI; IPI00972872; -.
DR   IPI; IPI00972912; -.
DR   IPI; IPI00972917; -.
DR   RefSeq; NP_080769.3; NM_026493.3.
DR   UniGene; Mm.244046; -.
DR   STRING; B2RX88; -.
DR   PRIDE; B2RX88; -.
DR   Ensembl; ENSMUST00000071087; ENSMUSP00000068804; ENSMUSG00000056763.
DR   GeneID; 211660; -.
DR   KEGG; mmu:211660; -.
DR   CTD; 211660; -.
DR   MGI; MGI:2681832; Cspp1.
DR   HOGENOM; HBG507135; -.
DR   HOVERGEN; HBG107771; -.
DR   InParanoid; B2RX88; -.
DR   OMA; QNLATSN; -.
DR   OrthoDB; EOG4N04D6; -.
DR   NextBio; 373324; -.
DR   Bgee; B2RX88; -.
DR   Genevestigator; B2RX88; -.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Microtubule; Phosphoprotein.
FT   CHAIN         1   1205       Centrosome and spindle pole associated
FT                                protein 1.
FT                                /FTId=PRO_0000401192.
FT   COILED       12     34       Potential.
FT   COILED       87    108       Potential.
FT   COILED      357    391       Potential.
FT   COILED      574    618       Potential.
FT   COILED      724    813       Potential.
FT   COILED      874    911       Potential.
FT   COILED      993   1014       Potential.
FT   COMPBIAS    423    491       Pro-rich.
FT   COMPBIAS    621    626       Poly-Gly.
FT   COMPBIAS    728    804       Glu-rich.
FT   VAR_SEQ       1     33       MADSLDEFIEEQKAKLAKDKAELESDPPYMEMK -> MDLN
FT                                CYPHLVAGHAHSYLIWR (in isoform 2).
FT                                /FTId=VSP_040073.
FT   VAR_SEQ     103    110       Missing (in isoform 3, isoform 4 and
FT                                isoform 6).
FT                                /FTId=VSP_040074.
FT   VAR_SEQ     303    319       PHGSRRGYVDGDDVPEE -> YLHLHFSSLYLLNTGVL
FT                                (in isoform 5 and isoform 6).
FT                                /FTId=VSP_040075.
FT   VAR_SEQ     320   1205       Missing (in isoform 5 and isoform 6).
FT                                /FTId=VSP_040076.
FT   VAR_SEQ     406    424       PDRLKQFSLTPRHFEEMPP -> GSACASESTPASAPCPPS
FT                                SF (in isoform 3).
FT                                /FTId=VSP_040077.
FT   VAR_SEQ     425   1205       Missing (in isoform 3).
FT                                /FTId=VSP_040078.
FT   VAR_SEQ     638    689       TDLNRMHRQNIDAYHNPDARTYEDKRAVVSIDQNLATSNAE
FT                                NLEDSANKNSG -> S (in isoform 2).
FT                                /FTId=VSP_040079.
FT   CONFLICT    259    259       G -> E (in Ref. 5; AAH19581).
FT   CONFLICT    324    324       I -> V (in Ref. 1; ACM46986).
FT   CONFLICT    358    358       D -> G (in Ref. 1; ACM46985).
FT   CONFLICT    394    394       I -> V (in Ref. 1; ACM46985).
FT   CONFLICT    412    412       F -> S (in Ref. 1; ACM46985).
SQ   SEQUENCE   1205 AA;  138312 MW;  0668152BE28543CB CRC64;
     MADSLDEFIE EQKAKLAKDK AELESDPPYM EMKGKASEKL SENSKILISM AKENIPPSSQ
     QQPKGPLGIE YGLSLPLGED YEQKKHKLKE ELRQDYRRYL TQGITQAKRK KNFLSTGETD
     PSTLGVSLPI DERLSAKERL KLERNREYNQ FLRGKAESTE KVRQVEKNIE PKSQRNKNPI
     SQGKSDLPLQ IQTAYTHSEG PWLSRQEEGL YRQLDGEIEL RSRRPLKQTK EEVGISGAEH
     PSLSGSAGVP ERRARRANGE RVLDRQHCRA DRDPGVSEDM DERFRFESDF DRRLLRVYTN
     GRPHGSRRGY VDGDDVPEEP NTQISAAENK SVHCNGPPRS ADLDITSPFA GMLFGGEDRE
     LTKRRKEKYR QELLEQIAEQ QKKKRREKDL AFGITTSGVQ DPEKSPDRLK QFSLTPRHFE
     EMPPERPRVA FQTPPPPFSA PSSPSVPPVH SAPSHNEDLH SGLGSTLGEL AHPRVLPVPL
     NPPPPPLLAP PASNYRTPYD DAYYFYGARN TLDPNIVYYG SGMIGGQPAP HVSAPVTHQV
     APPAVNTVGQ NEQKVLSDGL RNSGLVFEDK PKPSTQSLQS YQEALQEQIR EREARRKKER
     LEKEEYEAKL EAEMRIYNPW GKGGGGAPLR DAKGNLITDL NRMHRQNIDA YHNPDARTYE
     DKRAVVSIDQ NLATSNAENL EDSANKNSGP LQTQSSPFAR GNTFGEPLSE LQIKQQELYK
     NFLRFQIEEK RQREEAEREK LRVAEEKEEK RLAEQRARIQ QEYEEEQERR REKEEEQRLK
     NEELIRLAEE RRKEAERKKK EEEEKHNLQL QHYYERENII GDETKHLRQP SPVVPALQNK
     IASKLQRPPS VDTIISSFIH ESSMSRAQSP PVPARKNQLR AEEEKKNVIM ELSEMRKQLR
     SEERRLQGRL LHLDSDDEIP MRKRERNPMD IFDMARHRVQ APVRRPSPKG LDATTFQNIH
     DFNELRERDS DTRVDLRLMY PDPPRDHHTL EIQQQALLRE QQKRLNRIKM RRDAGADLDT
     ICTDNAQGRR MPRDDTNDFL KNSLLESDSA FIGAYGETYP VIEDNAFPPP SQLPSARERR
     RNKLKGLDFD SSRLHTPQDG LSLKSISSVN VDQVRMRNED RMRRLTEQQK KPTNTDDEGS
     LVDPDDIMRH LSDDGRNSAA TEPWLRPGTS ESLKRFMAEH LNEEQHKGPG KPGTFTWQGL
     SAAHA
//
ID   B2RXC2_MOUSE            Unreviewed;       942 AA.
AC   B2RXC2;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 28.
DE   SubName: Full=Inositol 1,4,5-trisphosphate 3-kinase B;
DE   SubName: Full=MCG6217;
GN   Name=Itpkb; ORFNames=mCG_6217;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC151160; AAI51161.1; -; mRNA.
DR   EMBL; BC157986; AAI57987.1; -; mRNA.
DR   EMBL; BC158000; AAI58001.1; -; mRNA.
DR   EMBL; CH466555; EDL13155.1; -; Genomic_DNA.
DR   IPI; IPI00263265; -.
DR   RefSeq; NP_001074644.1; NM_001081175.1.
DR   UniGene; Mm.132535; -.
DR   UniGene; Mm.383297; -.
DR   ProteinModelPortal; B2RXC2; -.
DR   SMR; B2RXC2; 650-938.
DR   STRING; B2RXC2; -.
DR   PRIDE; B2RXC2; -.
DR   Ensembl; ENSMUST00000070181; ENSMUSP00000069851; ENSMUSG00000038855.
DR   GeneID; 320404; -.
DR   KEGG; mmu:320404; -.
DR   CTD; 320404; -.
DR   MGI; MGI:109235; Itpkb.
DR   HOGENOM; HBG282725; -.
DR   HOVERGEN; HBG052139; -.
DR   InParanoid; B2RXC2; -.
DR   OMA; VFSPGRG; -.
DR   OrthoDB; EOG4Q2DG1; -.
DR   NextBio; 396660; -.
DR   Bgee; B2RXC2; -.
DR   Genevestigator; B2RXC2; -.
DR   GO; GO:0008440; F:inositol trisphosphate 3-kinase activity; IDA:MGI.
DR   GO; GO:0007166; P:cell surface receptor linked signaling pathway; IMP:MGI.
DR   GO; GO:0000165; P:MAPKKK cascade; IMP:MGI.
DR   GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; IMP:MGI.
DR   GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IMP:MGI.
DR   GO; GO:0045059; P:positive thymic T cell selection; IMP:MGI.
DR   InterPro; IPR005522; IPK.
DR   PANTHER; PTHR12400; IPK; 1.
DR   Pfam; PF03770; IPK; 1.
PE   2: Evidence at transcript level;
KW   Kinase; Transferase.
SQ   SEQUENCE   942 AA;  102673 MW;  DABAEE912F737114 CRC64;
     MAVYCYALNS LVIMNSTNEL KSGGPRPSGS ETPQPSGRAA LSPGSVFSPG RGASFLFPPA
     ESLSLEEPGS PGGWRSGRRR LNSSSGSGGG SSSSNSSSSS GVGSPSWAGR LRGDAQQVVA
     ARILSPPGPE EAQRKLRILQ RELQNVQVNQ KVGMFEAQIQ AQSSAIQAPR SPRLGRARSP
     SPCPFRSSSQ PPERVLAPCS PSEERRTKSW GEQCTETPDT NSGRRSRLST HPSKDKEGVA
     PLLGPASPTR LGTQSPSTSV RMERGTPASP RCGSPTPMET DKRVAPSLER FGTSLTLATK
     VAASAASAGP HPGHDSALME TGCELGGMRP WEAQMERRGQ FLGKETGSTP EPVRTHMREP
     PGRVGRGIHS VGGQGSWTPE VIKRPEERAV TAQSSEPSED PRWSRLPVDL DSVGPEKGGN
     RIPGMRGPQQ TLDSEREGSP ALGLLGGSQA AQPGARGVEE DVHYGRMLEP LPPGEVTTKL
     KEPQCLPGDR MGMQPESSIV WPSALEEAPL IWTRDTGVQS KGTWGSQLPD GDAHPSCQEM
     PPDQKDKASL KEACSPSNIP AIPAVIITDM GAQEDGGLEE IQGSPRGPLP LRKLSSSSAS
     STGFSSSYDD SEEDISSDPE RTLDPNSAFL HTLDQQKPRV SKSWRKIKNM VQWSPFVMSF
     KKKYPWIQLA GHAGSFKAAA NGRILKKHCE SEQRCLDRLM ADVLRPFVPA YHGDVVKDGE
     RYNQMDDLLA DFDSPCVMDC KMGVRTYLEE ELTKARKKPS LRKDMYQKMV EVDPEAPTEE
     EKAQRAVTKP RYMQWRETIS STATLGFRIE GIKKEDGSVN RDFKKTKTRE QVTEAFREFT
     KGNQNILIAY RDRLKAIRAT LEISPFFKCH EVIGSSLLFI HDKKEQAKVW MIDFGKTTPL
     PEGQTLQHDV PWQEGNREDG YLSGLDNLID ILTEMSQGSP LT
//
ID   B2RXE2_MOUSE            Unreviewed;       898 AA.
AC   B2RXE2;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 29.
DE   RecName: Full=Sodium/hydrogen exchanger;
GN   Name=Slc9a5; ORFNames=mCG_23530;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1
CC       (CPA1) transporter (TC 2.A.36) family.
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DR   EMBL; BC151197; AAI51198.1; -; mRNA.
DR   EMBL; CH466525; EDL11276.1; -; Genomic_DNA.
DR   IPI; IPI00466275; -.
DR   RefSeq; NP_001074801.1; NM_001081332.1.
DR   UniGene; Mm.334766; -.
DR   ProteinModelPortal; B2RXE2; -.
DR   SMR; B2RXE2; 105-130, 200-225.
DR   STRING; B2RXE2; -.
DR   PRIDE; B2RXE2; -.
DR   Ensembl; ENSMUST00000073149; ENSMUSP00000072893; ENSMUSG00000014786.
DR   GeneID; 277973; -.
DR   KEGG; mmu:277973; -.
DR   CTD; 277973; -.
DR   MGI; MGI:2685542; Slc9a5.
DR   eggNOG; roNOG08148; -.
DR   GeneTree; ENSGT00560000076802; -.
DR   HOGENOM; HBG444842; -.
DR   HOVERGEN; HBG052615; -.
DR   InParanoid; B2RXE2; -.
DR   OMA; SHKSRTT; -.
DR   OrthoDB; EOG4HQDHQ; -.
DR   PhylomeDB; B2RXE2; -.
DR   NextBio; 393862; -.
DR   Bgee; B2RXE2; -.
DR   Genevestigator; B2RXE2; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0015385; F:sodium:hydrogen antiporter activity; IEA:InterPro.
DR   GO; GO:0006885; P:regulation of pH; IEA:InterPro.
DR   InterPro; IPR006153; Cation/H_exchanger.
DR   InterPro; IPR018422; Cation/H_exchanger_CPA1.
DR   InterPro; IPR018410; Na/H_exchanger_3/5.
DR   InterPro; IPR004709; NaH_exchanger.
DR   PANTHER; PTHR10110; Cation/H_exchanger_cons-reg; 1.
DR   PANTHER; PTHR10110:SF10; Na/H_exchanger_3/5_cons-reg; 1.
DR   Pfam; PF00999; Na_H_Exchanger; 1.
DR   PRINTS; PR01084; NAHEXCHNGR.
DR   PRINTS; PR01087; NAHEXCHNGR3.
DR   TIGRFAMs; TIGR00840; b_cpa1; 1.
PE   2: Evidence at transcript level;
KW   Antiport; Ion transport; Membrane; Sodium; Sodium transport;
KW   Transmembrane; Transport.
SQ   SEQUENCE   898 AA;  99009 MW;  AE5BBB8A4426BB42 CRC64;
     MLSAALLLLP GLPLAGAGAT EEPTQESGPL GEPPPGLALF RWQWHEVEAP YLVALWILVA
     SLAKIVFHLS RKVTSLVPES CLLILLGLVL GGIVLAVAKK AEYQLEPGTF FLFLLPPIVL
     DSGYFMPSRL FFDNLGAILT YAVVGTLWNA FTTGVALWGL QQAGLVAPRV QAGLLDFLLF
     GSLISAVDPV AVLAVFEEVH VNQTLFIIIF GESLLNDAVT VVLYKVCNSF VEMGSANVQA
     TDYLKGVASL FVVSLGGAAV GLVFAFLLAL TTRFTKRVRI IEPLLVFLLA YAAYLTAEMA
     SLSAILAVTM CGLGCKKYVE ANISHKSRTA VKYTMKTLAS CAETVIFMLL GISAVDSSKW
     AWDSGLVLGT LFFILFFRAL GVVLQTWALN QFRLVPLDKI DQVVMSYGGL RGAVAFALVI
     LLDRTKVPAK DYFVATTIVV VFFTVIVQGL TIKPLVKWLR VKRSDYHKPT LNQELHEHTF
     DHILAAVEDV VGHHGYHYWR DRWEQFDKKY LSQLLMRRSA YRIRDQIWDV YYRLNIRDAI
     SFVDQGGHVL SSTGLTLPSM PSRNSVAETS VTNLLRESGS GACLDLQVID TVRSGRDRED
     AVMHHLLCGG LYKPRRRYKA SCGRHFISED AQERQDKEIF QQNMKRRLES FKSTKHNICF
     TKSKPRPRKT SHKKKDGVAN PEATNGKPPR DLGFQDTAAV ILTVESEEEE ESDSSETEKE
     DDEGIIFVAR ATSEVLQEGK VSGSLEVCPS PRIIPPSPTC AEKELPWKSG QGDLAVYVSS
     ETTKIVPVDM QTGWNQSISS LESLASPPCT QPPTLTRLPP HPLVTEEPQV PIDLSSDPRS
     SFAFPPSLAK AGRSRSESSA DIPQQELQPL MGHKDHTHLS PGTANSHWCI QFNRGGRL
//
ID   B2RXL7_MOUSE            Unreviewed;      1672 AA.
AC   B2RXL7;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   02-NOV-2010, entry version 22.
DE   SubName: Full=Kidins220 protein;
GN   Name=Kidins220;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC157898; AAI57899.1; -; mRNA.
DR   IPI; IPI00624420; -.
DR   UniGene; Mm.250641; -.
DR   UniGene; Mm.475357; -.
DR   ProteinModelPortal; B2RXL7; -.
DR   SMR; B2RXL7; 1-371, 1109-1170.
DR   STRING; B2RXL7; -.
DR   PRIDE; B2RXL7; -.
DR   Ensembl; ENSMUST00000085537; ENSMUSP00000082672; ENSMUSG00000036333.
DR   MGI; MGI:1924730; Kidins220.
DR   HOVERGEN; HBG058824; -.
DR   Bgee; B2RXL7; -.
DR   Genevestigator; B2RXL7; -.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR011646; KAP_NTPase.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 4.
DR   Pfam; PF00023; Ank; 7.
DR   Pfam; PF07693; KAP_NTPase; 1.
DR   SMART; SM00248; ANK; 11.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 10.
PE   2: Evidence at transcript level;
KW   ANK repeat; Repeat.
SQ   SEQUENCE   1672 AA;  185556 MW;  F99D403560F07519 CRC64;
     MIAAEQGNVE IVKELIKNGA NCNLEDLDNW TALISASKEG HIHIVEELLK CGANLEHRDM
     GGWTALMWAC YKGRTDVVEL LLSHGANPSV TGLYSVYPII WAAGRGHADI VHLLLQNGAK
     VNCSDKYGTT PLVWAARKGH LECVKHLLAM GADVDQEGAN SMTALIVAVK GGYTQSVKEI
     LKRNPNVNLT DKDGNTALMI ASKEGHIEIV QDLLDAGTYV NIPDRSGDTV LIGAVRGGHV
     EIVRALLQKY ADIDIRGQDN KTALYWAVEK GNATMVRDIL QCNPDTEICT KDGETPLIKA
     TKMRNIEVVE LLLDKGARVS AVDKKGDTPL HVAIRGRSRR LAELLLRNPK DGRLLYRPNK
     AGETPYNIDC SHQKSILTQI FGARHLSPTE TDGDMLGYDL YSSALADILS EPTMQPPICV
     GLYAQWGSGK SFLLKKLEDE MKTFAGQQIE PLFQFSWLIV FLTLLLCGGL GLVFAFTVDT
     NLAIAVSLSF LALLYIFFIV IYFGGRQEGE SWNWAWALST RLARHIGYLE LLFKLMFVNP
     PELPEQTTKA LPVRFLFTDY NRLSSVGGET SLAEMIATLS DACEREFGFL ATRLFRVFKT
     EDSQGKKKWK KTCCLPSFII FLFIVGCIIA GITLLAIFRV DPKHLTVNAI LISIASIVGL
     AFVLNCRTWW QVLDSLLNSQ RKRLHSAASK LHKLKSEGFM KVLKCEVELM ARMAKTIDSF
     TQNQTRLVVI IDGLDACEQD KVLQMLDTVR VLFSKGPFIA IFASDPHIII KAINQNLNSV
     LRDSNINGHD YMRNIVHLPV FLNSRGLSNA RKFLVTSATN GDISCSEATG VQEDADRRVS
     QNSLGEMTKL GSKTALNRRD TYRRRQMQRT ITRQMSFDLT KLLVTEDWFS DISPQTMRRL
     LNIVSVTGRL LRANQITFNW DRLASWINLT EQWPYRTSWL ILYLEETEGL PDQMTLKTIY
     ERISKNIPTT KDVEPLLEID GDIRNFEVFL SSRTPVLVAR DVKTFLPCTV NLDPKLREII
     ADVRAAREQI NIGGLAYPPL PLHEAPPRPP SGYSQPASVC SSSASFNGPF PGGVVSPQPH
     SSYYSGLSGP QHPFYNRASV PATGTSLLLS SMTVDVVCEK LRQIEGLDQG MLPQYCTTIK
     KANINGRVLA QCNIDELKKE MAMNFGDWHL FRSMVLEMRS VENQVVPEDP RFLNENSSAP
     VAHGESARRT SHSELPHTEL SSQTPYTLNF SFEELNTLGL DEGAPRHSNL SWQSQTRRTP
     SLSSLNSQDS SIEISKLTDK VQAEYRDAYR EYIAQMSQLE GGTGSSTISG RSSPHSTYYI
     GQSSSGGSIH SNLEQERGKE SELKQEEGRK SFLMKRGDVL DYSSSGVSTN EASPLDPITE
     EDEKSDQSGS KLLPGKKSSE RPSLFQTDLK LKGSGLRYQK LPSDEDESGT EESDNTPLLK
     DDKDKKAEGK AERVAKSPEH SVEPIRTFIK AKEYLSDALL DKKDSSDSGV RSNESSPNHS
     LHNEAADDSQ LEKANLIELE DEGHSGKRGM PHSLSGLQDP VIARMSICSE DKKSPSECSL
     IASSPEESWP SCQKAYNLNR TPSTVTLNNN TAPTNRANQN FDEIEGVRET SQVILRPGPS
     PNPTAVQNEN LKSMAHKRSQ RSSYTRLSKD ASELHAASSD STGFGEERES IL
//
ID   B2RXQ2_MOUSE            Unreviewed;      1266 AA.
AC   B2RXQ2;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 20.
DE   SubName: Full=Ppfia1 protein;
GN   Name=Ppfia1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC157936; AAI57937.1; -; mRNA.
DR   EMBL; BC172096; AAI72096.1; -; mRNA.
DR   IPI; IPI00896602; -.
DR   RefSeq; NP_001182015.1; NM_001195086.1.
DR   UniGene; Mm.272809; -.
DR   ProteinModelPortal; B2RXQ2; -.
DR   SMR; B2RXQ2; 907-983, 1024-1091.
DR   STRING; B2RXQ2; -.
DR   PRIDE; B2RXQ2; -.
DR   GeneID; 233977; -.
DR   KEGG; mmu:233977; -.
DR   CTD; 233977; -.
DR   MGI; MGI:1924750; Ppfia1.
DR   HOVERGEN; HBG052330; -.
DR   Genevestigator; B2RXQ2; -.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR011510; SAM_2.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 3.
DR   Pfam; PF00536; SAM_1; 2.
DR   Pfam; PF07647; SAM_2; 1.
DR   SMART; SM00454; SAM; 3.
DR   SUPFAM; SSF47769; SAM_homology; 3.
DR   PROSITE; PS50105; SAM_DOMAIN; 3.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1266 AA;  142676 MW;  545C3EFBF1067EBC CRC64;
     MMCEVMPTIS EAEGPPGGGG SHGSGSPSQP DADSHFEQLM VSMLEERDRL LDTLRETQET
     LALTQGKLHE VGHERDSLQR QLNTALPQEF AALTKELNVC REQLLEREEE IAELKAERNN
     TRLLLEHLEC LVSRHERSLR MTVVKRQAQS PAGVSSEVEV LKALKSLFEH HKALDEKVRE
     RLRVALERCS LLEEELGATH KELMILKEQN NQKKTLTDGL LDGNHEQESA PSTNGKRSSD
     GSLSHEDLAK VLELQEVIDR QAREQSQMKE RLASLSSHAA ELEEDLDTAR KDLIKSEEMN
     TKLQREVREA MAQKEDMEER ITTLEKRYLA AQREATSVHD LNDKLENEIA NKDSMHRQTE
     DKNRQLQERL ELAEQKLQQT LRKAETLPEV EAELAQRVAA LSKSGPLSSG SSAAKEAKLL
     ELTSKLRKAE ERHGNIEERL RQMEAQLEEK NQELQRARQR EKMNEEHNKR LSDTVDKLLS
     ESNERLQLHL KERMAALEDK NSLLREVENA KKQLEETQHD KDQLVVTIEA LKAELEQMRL
     RGPSLHHGRP HLGSVPDFRF SVADGHVDAY STSAVLRRPQ KGRLAALRDE PSKVQTLNEQ
     DWERAQQASV LANVAQAFES DVDVSDGEDD RDTLLSSVDL LSPSGQADAQ TLAMMLQEQL
     DAINKEIRLI QEEKENTEQR AEEIESRVGS GSLDNLGRFR SMSSIPPYPA SSLAGSSPPG
     SGRSTPRRVP HSPAREVDRL GVMTLPSDLR KHRRQLPASR EEVRDDKTTI KCETSPPSSP
     RPLRLDRMHK GAPHTVSHED IRDLRNSTGS QDGPVSNPSS SNSSQDSLHK APKKKGIKSS
     IGRLFGKKEK GRPGPLGKES PGQVGVSETE NSSQDALGLS KLGGQAEKNR KLQKKHELLE
     EARRQGLPFA QWDGPTVVVW LELWVGMPAW YVAACRANVK SGAIMSALSD TEIQREIGIS
     NPLHRLKLRL AIQEIMSLTS PSAPPTSRTT TGNVWLTHEE METLTATPQT EDEEGSWAQT
     LAYGDMNHEW IGNEWLPSLG LPQYRSYFME CLVDARMLDH LTKKDLRGQL KMVDSFHRNS
     FQCGIMCLRR LNYDRKELER KREESQNETR DVLVWSNDRV IRWILSIGLK EYANNLIESG
     VHGALLALDE TFDFSALALL LQIPTQNTQA RAVLEREFNN LLITGTDRRF DEDDDKSFRR
     APSWRKKFRP KDIRGLASGS AETLPANFRV TSSMSSPSMQ PKKVQMDGSV SGAQRLDSAT
     VRTYSC
//
ID   B2RXQ9_MOUSE            Unreviewed;       652 AA.
AC   B2RXQ9;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 26.
DE   SubName: Full=Sorbs2 protein;
GN   Name=Sorbs2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 3 SH3 domains.
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DR   EMBL; BC157944; AAI57945.1; -; mRNA.
DR   IPI; IPI00177047; -.
DR   UniGene; Mm.211096; -.
DR   UniGene; Mm.447653; -.
DR   ProteinModelPortal; B2RXQ9; -.
DR   SMR; B2RXQ9; 419-475, 493-551, 595-649.
DR   STRING; B2RXQ9; -.
DR   PRIDE; B2RXQ9; -.
DR   Ensembl; ENSMUST00000130011; ENSMUSP00000121619; ENSMUSG00000031626.
DR   MGI; MGI:1924574; Sorbs2.
DR   HOVERGEN; HBG053053; -.
DR   Bgee; B2RXQ9; -.
DR   Genevestigator; B2RXQ9; -.
DR   InterPro; IPR000108; p67phox.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR003127; Sorb.
DR   Pfam; PF00018; SH3_1; 2.
DR   Pfam; PF07653; SH3_2; 1.
DR   Pfam; PF02208; Sorb; 1.
DR   PRINTS; PR00499; P67PHOX.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 3.
DR   SMART; SM00459; Sorb; 1.
DR   SUPFAM; SSF50044; SH3; 3.
DR   PROSITE; PS50002; SH3; 3.
DR   PROSITE; PS50831; SOHO; 1.
PE   2: Evidence at transcript level;
KW   SH3 domain.
SQ   SEQUENCE   652 AA;  72404 MW;  324FE95DD8373798 CRC64;
     MNTGRESQSP DSAKGFRSVR PNLQDKRSPT QSQITINGNS GGAVSPVSYY QRPFSPSAYS
     LPASLNSSII MQHGRSLDSA ETYSQHAQSL DGTMGSSIPL YRSSEEEKRV TVIKAPHYPG
     IGPVDESGIP TAIRTTVDRP KDWYKTMFKQ IHMVHKPGLY NSPYSAQSHP AAKTQTYRPL
     SKSHSDNGTD AFKEVPSPVP PPHVPPRPRD QSSTLKHDWD PPDRKVDTRK FRSEPRSIFE
     YEPGKSSILQ HERPPPLPPT PTPVPREPSR KPLSVSPSTD GLRSPSPPPR SCVPAPRPSA
     PDLSPTRVSI YQSSIDRSLE RPSSSASMAG DFRKRRKSEP AVGPLRGLGD QSSSRTSPGR
     ADLPGSSSTF TKSFISSSPS SPSRAQDHES PRSYSSTLTD LGRSASRERR GTPEKEKLPA
     KAVYDFKAQT SKELSFKKGD TVYILRKIDQ NWYEGEHHGR VGIFPISYVE KLTPPEKAQP
     ARPPPPVQPG EIGEAIAKYN FNADTNVELS LRKGDRIILL KRVDQNWYEG KIPGTNRQGI
     FPVSYVEVVK RNAKGAEDYP DPPLPHSYSS DRIYTLSSNK PQRPGFSHEN IQGGGEPFQA
     LYNYTPRNED ELELRESDVV DVMEKCDDGW FVGTSRRTKF FGTFPGNYVK RL
//
ID   B2RXR4_MOUSE            Unreviewed;      1272 AA.
AC   B2RXR4;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   30-NOV-2010, entry version 15.
DE   SubName: Full=2210408I21Rik protein;
GN   Name=2210408I21Rik;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC157949; AAI57950.1; -; mRNA.
DR   IPI; IPI00672647; -.
DR   UniGene; Mm.371098; -.
DR   UniGene; Mm.81475; -.
DR   Ensembl; ENSMUST00000095588; ENSMUSP00000093248; ENSMUSG00000071252.
DR   MGI; MGI:1919621; 2210408I21Rik.
DR   HOVERGEN; HBG108024; -.
DR   InParanoid; B2RXR4; -.
DR   Bgee; B2RXR4; -.
DR   Genevestigator; B2RXR4; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1272 AA;  145602 MW;  D5C81EF4B763F864 CRC64;
     MDALQDYSHN SFDLQCLLNS FPGDLEFKQI FSDIGEQMEQ NAASIEHCIE EIQSEVNKLC
     PDAQLQTTSD CFKWLTSYNY NLSKSPSISH GDLINFLKTM KDLLNNEDNH EEMILDLLWD
     LSCQSSISFL SSLGGTTFCH LSRTSIHSVE DFSSVDVKSV WDDVRLHLRR FLVNRLERYN
     EINNSQQKIE LKSQCMKQFL LLYSESEVLV KYQSIQKRLL DTFLQDSFPS CNRESDLERI
     VCGYQSTMLM LYSMIKEDFN VLCEILAPSS LVQFFNETYL DTVTEEMTKI LEYFCELQFK
     ENAVPVVKTS KSCNKRRGAV HALVSPECSQ KERRPSLSLE ELRFLSQLTE SFVKLENSIQ
     ELFAETLSLL QMPRSSPGIL EKSKKEVMVE KLIANENNKP PEALLPVKEA TLLEFGWRNA
     FKEVPLAIAH CISAAIEGFS TQVLQQEQTE RISSVSYTIN LVNVPQLCPE GHIFPEEEQP
     KRVAKFCSDI MEKLDTMLPL ALACRDDSPQ EIRENLVEAY SKVATAVLER LQERGKEVPS
     RAPLKNLHSI LSSAAYVSQR FTHYDNLMKE TTKKPIFLVP VQRYQEFINT VQFQVTDYCA
     RVCAMSILQD AESHHWDDYK AFYEGERCSF AIQMWHYFSL ALHHDLWTIL PPKLAQEILA
     EMLEKSLGLL ASRYARAHPS PKRTAQIRLD VMAILIFTEN MLWSICSSGQ EILNPHKFNN
     HKIFKIHTHC NNLFTTLAIL TSPLTELYKT FQHGVDESPS NSLTPLFNQP LHWISCMSQF
     YPSLLRPPSA GGLTAQGQLK LLLSQPCCKW NLLLDTLLHS GGLIPRILLK SSKQAAGMES
     KQSAGGSLVG AIFEVLYHCH LSPQTFGNVF MSHMEEEQLW DFLFNIPVSS FTESQPEVIH
     CLRLALMDSV KDTVQQIISI MRCRRNSETN LNKPRVPDHL LQSIPQGWNY IPRDSRRKES
     NKGITELAAQ AVSIVLSKLP TVIACLPPTI KYFFFLSERK MSKNLAELKK AGLLVWNLII
     IICRIFEDGN TVERLTGSSL DRWSKEKLGL ICLCLESILG KQSNPSQLTQ KVILSIERQK
     PNWMEQQLLK ARTLSIQCAF TRMEENSGSE GEAALELTEQ KTNAMVLDLC HKPGGSKYLQ
     QIYHIMQLNE EYLKEQLFAM NGSEEKPLLI RPLKVALRDE DQPPAFNPFH VHKVVSESML
     DQVATVTWCC DWSNLLPNYL GLNKMTFGAL LKNRWEMRKD ETLEEKEKMM LEHLKQNCTI
     QDFSTSDSKT EQ
//
ID   B2RXR7_MOUSE            Unreviewed;      1161 AA.
AC   B2RXR7;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 19.
DE   SubName: Full=Pcdh9 protein;
GN   Name=Pcdh9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; BC157952; AAI57953.1; -; mRNA.
DR   IPI; IPI00855176; -.
DR   UniGene; Mm.37126; -.
DR   UniGene; Mm.458162; -.
DR   ProteinModelPortal; B2RXR7; -.
DR   SMR; B2RXR7; 149-352, 476-667.
DR   HOVERGEN; HBG053523; -.
DR   Genevestigator; B2RXR7; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR013164; Cadherin_N.
DR   InterPro; IPR013585; Protocadherin.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 7.
DR   Pfam; PF00028; Cadherin; 6.
DR   Pfam; PF08266; Cadherin_2; 1.
DR   Pfam; PF08374; Protocadherin; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 7.
DR   SUPFAM; SSF49313; Cadherin; 6.
DR   PROSITE; PS00232; CADHERIN_1; 6.
DR   PROSITE; PS50268; CADHERIN_2; 7.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Membrane; Repeat; Transmembrane;
KW   Transmembrane helix.
SQ   SEQUENCE   1161 AA;  127877 MW;  960DFA454AC74C06 CRC64;
     MDLRDFYLLA ALIACLRLDS AIAQELIYTI REELPENVPI GNIPKDLNIS HINAATGTSA
     SLVYRLVSKA GDAPLVKVSS STGEIFTTSN RIDREKLCAG ASYAEENECF FELEVVILPN
     DFFRLIKIKI IVKDTNDNAP MFPSPVINIS IPENTLINSR FPIPSATDPD TGFNGVQHYE
     LLNGQSVFGL DIVETPEGEK WPQLIVQQNL DREQKDTYVM KIKVEDGGTP QKSSTAILQV
     TVSDVNDNRP VFKEGQIEVH IPENAPVGTS VIQLHATDAD IGSNAEIRYI FGAQVAPATK
     RLFALNNTTG LITVQRSLDR EETAIHKVTV LASDGSSTPA RATVTINVTD VNDNPPNIDL
     RYIISPINGT VYLSEKDPVN TKIALITVSD KDTDVNGKVI CFIEREVPFH LKAVYDNQYL
     LETSSLLDYE GTKEFSFKIV ASDSGKPSLN QTALVRVKLE DENDNPPIFN QPVIELSVSE
     NNRRGLYLTT ISATDEDSGK NADIVYQLGP NASFFDLDRK TGVLTASRVF NREEQERFIF
     TVTARDNGTP PLQSQAAVIV TVLDENDNSP KFTHNHFQFF VSENLPKYST VGVITVTDED
     AGENKAVTLS ILNDNENFVL DPYSGVIKSN VSFDREQQSS YTFDVKATDG GQPPRSSTAK
     VTINVMDVND NSPVVISPPS NTSFKLVPLS AIPGSVVAEV FAVDIDTGMN AELKYTIVSG
     NNKGLFRIDP VTGNITLEEK PAPTDVGLHR LVVNISDLGY PKALHTLVLV FLYVNDTAGN
     TSYIYDLIRR TMETPLDRNI GDSGQPYQNE DYLTIMIAIV AGAMVVIVVI FVTVLVRCRH
     ASRFKAAQRS KQGAEWMSPN QENKQNKKKK RKKRKSPKSS LLNFVTIEES KPDDAVHEPI
     NGTISLPAEL EEQGIGRFDW GPAPPTTFKP NSPDLAKHYK SASPQPAFHL KPDTPVSVKK
     HHVIQELPLD NTFVGGCDTL SKRSSTSSDH FSASECSSQG GFKTKGPLHT RQPQDEFYDQ
     ASPDKRTEAD GNSDPNSDGP LGPRGLAEAT EMCTQECLVL GHSDNCWMPP GLGPYQHPKS
     PLSTFAPQKE WIKKDKLVNG HTLTRAWKED TNRNQFNDRK QYGSNEGHFN NGGHMADIPL
     ANLKSYKQAG GTIESPKEHQ L
//
ID   B2RXT3_MOUSE            Unreviewed;      1010 AA.
AC   B2RXT3;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 20.
DE   SubName: Full=Ogdhl protein;
GN   Name=Ogdhl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC157970; AAI57971.1; -; mRNA.
DR   EMBL; BC157971; AAI57972.1; -; mRNA.
DR   IPI; IPI00342603; -.
DR   UniGene; Mm.318302; -.
DR   ProteinModelPortal; B2RXT3; -.
DR   SMR; B2RXT3; 113-1003.
DR   STRING; B2RXT3; -.
DR   Ensembl; ENSMUST00000022480; ENSMUSP00000022480; ENSMUSG00000021913.
DR   MGI; MGI:3616088; Ogdhl.
DR   eggNOG; roNOG11925; -.
DR   GeneTree; ENSGT00530000063092; -.
DR   HOVERGEN; HBG001892; -.
DR   OrthoDB; EOG4VQ9NH; -.
DR   Bgee; B2RXT3; -.
DR   Genevestigator; B2RXT3; -.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:InterPro.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   PANTHER; PTHR23152; 2oxoglutarate_DH_E1; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1010 AA;  114561 MW;  6598E55AB930E61D CRC64;
     MSQLRLLPFR LGPRATKLLA TRAIPVFSGC RRSSGPPTTI PRSRSGVSSS YVEEMYFAWL
     ENPQSVHKSW DSFFQRASKE ASVGPAQPQL PAVLQESRTS VSSCTKTSKL VEDHLAVQSL
     IRAYQIRGHH VAQLDPLGIL DADLDSFVPS DLITTIDKLA FYDLQEADLD KEFRLPTTTF
     IGGPENTLSL REIIRRLEST YCQHIGLEFM FINDVEQCQW IRQKFETPGV MQFSVEEKRT
     LLARLVRSMR FEDFLARKWS SEKRFGLEGC EVMIPALKTI IDKSSEMGIE NVILGMPHRG
     RLNVLANVIR KDLEQIFCQF DPKLEAADEG SGDVKYHLGM YHERINRVTN RNITLSLVAN
     PSHLEAVDPV VQGKTKAEQF YRGDAQGRKV MSILVHGDAA FAGQGVVYET FHLSDLPSYT
     TNGTVHVVVN NQIGFTTDPR MARSSPYPTD VARVVNAPIF HVNADDPEAV IYVCSVAAEW
     RNTFNKDVVV DLVCYRRRGH NEMDEPMFTQ PLMYKQIHKQ VPVLKKYADK LIAEGTVTLQ
     EFEEEIAKYD RICEEAYGRS KDKKILHIKH WLDSPWPGFF NVDGEPKSMT CPTTGIPEEM
     LTHIGSVASS VPLEDFKIHT GLSRILRGRA DMTKKRTVDW ALAEYMAFGS LLKEGIHVRL
     SGQDVERGTF SHRHHVLHDQ EVDRRTCVPM NHLWPDQAPY TVCNSSLSEY GVLGFELGYA
     MASPNALVLW EAQFGDFHNT AQCIIDQFIS TGQAKWVRHN GIVLLLPHGM EGMGPEHSSA
     RPERFLQMSN DDSDAYPVFT EDFEVSQLYD CNWIVVNCST PASYFHVLRR QILLPFRKPL
     IVFTPKSLLR HPDAKSSFDQ MVSGTSFQRL IPEDGPAAHS PEQVQRLIFC TGKVYYDLVK
     ERSSQGLEQQ VAITRLEQIS PFPFDLIMRE AEKYSGAELV WCQEEHKNMG YYDYISPRFM
     TLLGHSRPIW YVGRDPAAAP ATGNKNAHLV SLRRFLDTAF NLKAFEGKTF
//
ID   B2RXT8_MOUSE            Unreviewed;      1260 AA.
AC   B2RXT8;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 24.
DE   SubName: Full=Arid4a protein;
GN   Name=Arid4a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 ARID domain.
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DR   EMBL; BC157975; AAI57976.1; -; mRNA.
DR   IPI; IPI00654990; -.
DR   UniGene; Mm.241601; -.
DR   ProteinModelPortal; B2RXT8; -.
DR   SMR; B2RXT8; 10-111, 170-277, 308-419, 575-642.
DR   STRING; B2RXT8; -.
DR   Ensembl; ENSMUST00000046305; ENSMUSP00000035512; ENSMUSG00000048118.
DR   Ensembl; ENSMUST00000058026; ENSMUSP00000052271; ENSMUSG00000048118.
DR   MGI; MGI:2444354; Arid4a.
DR   HOVERGEN; HBG058247; -.
DR   InParanoid; B2RXT8; -.
DR   OrthoDB; EOG498V0C; -.
DR   Bgee; B2RXT8; -.
DR   Genevestigator; B2RXT8; -.
DR   GO; GO:0000785; C:chromatin; IEA:InterPro.
DR   GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR   GO; GO:0006333; P:chromatin assembly or disassembly; IEA:InterPro.
DR   InterPro; IPR001606; ARID/BRIGHT_DNA-bd.
DR   InterPro; IPR000953; Chromodomain.
DR   InterPro; IPR016197; Chromodomain-like.
DR   InterPro; IPR012603; RBB1NT.
DR   InterPro; IPR002999; Tudor.
DR   Gene3D; G3DSA:1.10.150.60; ARID; 1.
DR   Pfam; PF01388; ARID; 1.
DR   Pfam; PF08169; RBB1NT; 1.
DR   SMART; SM00501; BRIGHT; 1.
DR   SMART; SM00298; CHROMO; 1.
DR   SMART; SM00333; TUDOR; 1.
DR   SUPFAM; SSF46774; ARID; 1.
DR   SUPFAM; SSF54160; Chromodomain-like; 1.
DR   PROSITE; PS51011; ARID; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1260 AA;  141875 MW;  D15802BD797789DE CRC64;
     MKAADEPAYL TVGTDVSAKY RGAFCEAKIK TVKRLVKVKV LLKQDNTTQL VQDDQVKGPL
     RVGAIVETRT SDGSIQEAII SKLTDASWYT VVFDDGDERT LRRTSLCLKG ERHFAESETL
     DQLPLTNPEH FGTPVIAKKT NRGRRSSLPI TEDEKEEESS EEEDEDKRRL NDELLGKVVS
     VASTAESTGW YPALVVSPSC NDDVTVKKDQ CLVRSFIDSK FYSIARKDIK ELDILTLPES
     ELCARPGLRR ASVFLKGRIV PDNWKMDISE ILESSSSDDE ECPAEEHEEE KEKEAKKEEE
     ELPEEELDPE ERDNFLQQLY KFMEDRGTPI NKPPVLGYKD LNLFKLFRLV YHQGGCGNID
     SGAVWKQIYM DLGIPILNSA ASYNVKTAYR KYLYGFEEYC RSANIQFRTI HHHEPKVKEE
     KKDFEDSMDE ALKEAPEMPL LDVKSEPEEN TDSNSESDRE DTELKSPRGR RKIVRDANCI
     KKEIEEEKIE DKFLRDDLEN KDAGDDDDDG DPAAKREHEL LFGRKSTPKN KEKIKKPEDS
     ERDSDEEEEK SQEREETESR CDSEGEDEED DTEPCLTGTK VKVKYGRGKT QKIYEASIKS
     TEMDDGEILY LVHYYGWNVR YDEWVKADRI IWPLDKGGPK KKQKKKVKNK EDSEKDEKRD
     EERQKSKRGR PPLKSTFSPN MPYSLSKTSN SEGKSDSCSS DSEADDQLEK SSGGEDLSPD
     VKEELEKNEN GHDDKLDEEN PKIVHISKEN DRTQAQPSDT LTVEAGDSDQ IVHIFGDKVD
     QVEELKKQVE KSPKGKGRRS KTKDLSLELI KISPFGQEEA GSEAHGDVHS LEFSSLECKN
     FSSTEDDIDP YEKEKKLKRK ILGQQSPEKK LRLDNGMEMT TGVSQERSDD GAGAEGMKGA
     HVEQHFETEG EGMPSLTAEP DQGLQELTSE KSDSPAEEEP VHTPLKEEED AMPLIGPETL
     VCHEVDLDDL DEKDKTSIED VVVEGSESNS LASVPPALPP VAQHNFSVAS PLTLSQDESR
     SIKSESDITI EVDSIAEESQ EGLCERESAN GFEASVASGA CSIIAHERES REKGQKRPSD
     GNSGLIAKKQ KRTPKRTSAA AKTEKNGAGQ SSDSEDLPAM DSSSNCTPVK RLSLPKPQKL
     PRSPARTSPH IKDAEKEKHR EKHPNSSPRT YKWSFQLNEL DNMNSTERIS FLQEKLQEIR
     KYYMSLKSEV ATIDRRRKRL KKKDREVSHA GASMSSASSD TGMSPSSSSP PQNVLAVECR
//
ID   B2RXU5_MOUSE            Unreviewed;       408 AA.
AC   B2RXU5;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   05-OCT-2010, entry version 22.
DE   SubName: Full=Zfp365 protein;
DE   SubName: Full=Zinc finger protein 365;
GN   Name=Zfp365; ORFNames=mCG_10493;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC157983; AAI57984.1; -; mRNA.
DR   EMBL; BC157991; AAI57992.1; -; mRNA.
DR   EMBL; CH466553; EDL32018.1; -; Genomic_DNA.
DR   IPI; IPI00399502; -.
DR   UniGene; Mm.268346; -.
DR   ProteinModelPortal; B2RXU5; -.
DR   STRING; B2RXU5; -.
DR   Ensembl; ENSMUST00000064656; ENSMUSP00000067197; ENSMUSG00000037855.
DR   MGI; MGI:2143676; Zfp365.
DR   HOVERGEN; HBG094181; -.
DR   InParanoid; B2RXU5; -.
DR   NextBio; 437379; -.
DR   Bgee; B2RXU5; -.
DR   Genevestigator; B2RXU5; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   SMART; SM00355; ZnF_C2H2; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   408 AA;  46852 MW;  D56ACAEEB6A10FF7 CRC64;
     MQQTTFEESR YHWQDSLENV AVCLPFRCPR CGDHTRFRSL SSLRAHLEFS HSYEERTLLT
     KCSLLPSLKD TELLRSSELP KQGKVLRGHA KVTKQKPSYV NLYSISHGHS KDTKPFEMVA
     ERPVSYVQTY TAVDIRADSL DAPCASPGLP TQDTKAAFEA HVREKFNRMV EAVDRTIEKR
     IDKLTKELAQ KTAELLEVRA AFAQLTQKKQ EVQRRERALN KQVDVAVEMI AVLKQRLTES
     EEELLRKEEE VVTFNHFLEA AAEKEVQGKA RLQDFIENLL QRVELAEKQL EYYQSQQASG
     FSCDTSEHML TDIPSNRKPR CLSRGHQHSV CNHPELRAHF HLKGRSYLKK AKDERAGMQP
     AKAIHEPAES PREFFRPAKK GEHLGLSRKG NFRPKMAKKK PTAIVNII
//
ID   B2RY08_MOUSE            Unreviewed;      2042 AA.
AC   B2RY08;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 25.
DE   SubName: Full=Dock9 protein;
GN   Name=Dock9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; BC158050; AAI58051.1; -; mRNA.
DR   IPI; IPI00896689; -.
DR   UniGene; Mm.441054; -.
DR   ProteinModelPortal; B2RY08; -.
DR   SMR; B2RY08; 182-318.
DR   STRING; B2RY08; -.
DR   Ensembl; ENSMUST00000100299; ENSMUSP00000097872; ENSMUSG00000025558.
DR   MGI; MGI:106321; Dock9.
DR   HOVERGEN; HBG107819; -.
DR   Bgee; B2RY08; -.
DR   Genevestigator; B2RY08; -.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0017048; F:Rho GTPase binding; IPI:MGI.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IDA:MGI.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR010703; DOCK.
DR   InterPro; IPR021816; DUF3398.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF06920; Ded_cyto; 1.
DR   Pfam; PF11878; DUF3398; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   2042 AA;  233741 MW;  1B3D4D6AC4E20580 CRC64;
     MGCTTSVILF KGIRTVFERN CAYMCKQPGE SNALEYTAYN WSKEDSELSI AFCLAKPKLI
     EPLDYENVIV QKKTQILNDC LREMLLFPYD DFQTAILRRQ GRYLRSTVPA NAEEEAQSLF
     VTECIKTYNS DWHLVTYKYE DYSGEFRQLP NKVPKLDKLP VHVYEVDEEA DKDEDAASLG
     SQKGGITKHG WLYKGNMNSA ISVTMRSFKR RFFHLIQLGD GSYNLNFYKD EKISKEPKGS
     IFLDSCMGVI QNNRVRRFAF ELKMQDKSSY LLAADSEAEM EEWVTVLNKI LQLNFEAAMQ
     EKRNGDPHED DEQSKLEGSG SGLDSYLPEL AKSTREAEIK LKSESRVKLF YLDPDTQKLD
     FSSAEPEVKP FEEKFGKRIL VKCNDLSFNL QCCVAENEEG PTTNVEPFFV TLSLFDIKYN
     RKISADFHVD LNHFSVRQML APTSPALMNG GQSPPAFQDA LHTAMQYPKQ GIFSVTCPHP
     DIFLVARIEK VLQGSITHCA EPYMRSSDSS KVAQKVLKNA KQACQRLGQY RMPFAWAART
     LFKDTSGNLD KNARFSAIYR QDSNKLSNDD MLKLLADFRK PEKMAKLPVI LGNLDITIDS
     VSCDFPNYLN SSYIPMRQFE TCSKSPITFE VEEFVPCIPK HTQPYTVYSN HLYVYPKYLK
     YDSQKSFAKA RNIAICIEFK DSDEEDSQPL KCIYGRPGGP VFTRSALAAV LHHQQNPEFY
     DEIKIELPAQ LHERHHLLFT FFHVSCDNST KGSTKKKDAV ETQVGFSWLP LLKDGRVLTS
     EQHIPVSANL PSGYLGYQEL GMGRHYGPEV KWVEGGKPLL KISTHLVSTV YTQDQHLHNF
     FQYCQKTESG AQASGSELVK YLKSLHAMEG HVMIAFLPTI LNQLFRVLTR ATQEEVAVNV
     TRVIIHVVAQ CHEEGLESHL RSYVKFAYKA EPYVASEYKT VHEELTKSMT TILKPSADFL
     TSNKLLKYSW FFFDVLIKSM AQHLIENNKV KLLRNQRFPA SYHHAVETVV NMLMPHITQK
     FRDNPEASKN ANHSLAVFIK RCFTFMDRGF VFKQINNYIS CFAPGDPKTL FEYKFEFLRV
     VCNHEHYIPL NLPMPFGKGR IQRYQDLQLD YSLTDEFCRN HFLVGLLLRE VGTALQEFRE
     VRVIAISMLK NLLIKHSFDD RYNSRSHQAR IATLYLPLFG LLIENVQRIN VRDVSPFPVN
     PGSIVKDEAL AVPAGNPLMT PQKGNTLDHS LHKDLLGAIS GIASPYTAST PNINSVRNAD
     SRGSLISTDS GNSLPDRNPE KSNSLDKQQS GMLGNSVVRC DKLDQSEIKS LLMCFLYVLK
     SMSDDALFTY WNKASTAELM DFFTISEVCL HQFQYMGKRY IARTGMMHAR LQQLGSLDNS
     VTFNHSYGHS EADVVHQSLL EANIATEVCL TALDTLSLFT LAFKNQLLAD HGHNPLMKKV
     FDVYLCFLQK HQSEMALKNV FTALRSLIYK FPSAFYEGRA DMCASLCYEV LKCCNSKLSS
     IRTEASQLLY FLMRNNFDYT GKKSFVRTHL QVIISVSQLI ADVVGIGGTR FQQSLSIINN
     CANSDRIIKH TSFSSDVKDL TKRIRTVLMA TAQMKEHEND PEMLVDLQYS LAKSYASTPE
     LRKTWLDSMA RIHVKNGDLS EAAMCYVHVT ALVAEYLTRK GMFRQGCTAF RVITPNIDEE
     ASMMEDVGMQ DVHFNEDVLM ELLEQCADGL WKAERYELIA DIYKLIIPIY EKRRDFERLA
     HLYDTLHRAY SKVTEVMHSG RRLLGTYFRV AFFGQAAGFF EDEDGKEYIY KEPKLTPLSE
     ISQRLLKLYS DKFGSENVKM IQDSGKVNPK DLDSKFAYIQ VTHVTPFFDE KELQERRTEF
     ERCHNIRRFM FEMPFTQTGK RQGGVEEQCK RRTILTAIHC FPYVKKRIPV MYQHHTDLNP
     IEVAIDEMSK KVAELRQLCS SAEVDMIKLQ LKLQGSVSVQ VNAGPLAYAR AFLDDTNTKR
     YPDNKVKLLK EVFRQFVEAC GQALAVNERL IKEDQLEYQE EMKANYREMA KELSDIMREQ
     MG
//
ID   B2RY09_MOUSE            Unreviewed;      1347 AA.
AC   B2RY09;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   30-NOV-2010, entry version 15.
DE   SubName: Full=Etl4 protein;
GN   Name=Etl4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC158051; AAI58052.1; -; mRNA.
DR   IPI; IPI00876314; -.
DR   RefSeq; NP_001074475.1; NM_001081006.1.
DR   RefSeq; NP_001171101.1; NM_001177630.1.
DR   RefSeq; NP_001171102.1; NM_001177631.1.
DR   UniGene; Mm.237935; -.
DR   STRING; B2RY09; -.
DR   GeneID; 208618; -.
DR   KEGG; mmu:208618; -.
DR   CTD; 208618; -.
DR   MGI; MGI:95454; Etl4.
DR   HOVERGEN; HBG019587; -.
DR   Genevestigator; B2RY09; -.
DR   InterPro; IPR022782; AIP3_C.
DR   Pfam; PF03915; AIP3; 2.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1347 AA;  146607 MW;  F5D8D10E9AE5074C CRC64;
     MEESEGQKCE PNLPPSGDSR QMPQQGRSNL HVTSQEDAAC RRPRERLSNG NARAQVSKPA
     RNIPRRHTLG GPRSSKEILG MQPSEMDRKR EAFLEHLKQK YPHHATAIMG HQERLRDQRK
     SPKLSHSPQP PNLGDPVEHL SETSGDSLEA MSEGEVPSPF ARGSRTRASL PVVRSANQTK
     ERSLGVLYLQ YGDETKQLRM PNEVTSTDTI RALFVSAFPQ QLTMKMLESP SVAIYIKDDS
     RNVYYELNDV RNIQDRSLLK VYNKDPSHAF NHMTKAVNGD MRMQREIVYA RGDGLVAPRP
     GSVAHPPHVI PNSPPSTPVP HSLPPSPSRI PYGGSRPMAI PGNATIPRDR LSSLPVSRSI
     SPSPSAILER RDVKPDEDMS SKNLVMFRNE GFYADPYLYH EGRMSIASSH GGHPLDVPDH
     VIAYHRTAIR SASAYCSPSL QAEMHMEQSL YRQKSRKYPD SHLPTLGSKT PPASPHRVGD
     LRMIDLHPHL NTHGPPHTLQ PDRASPSRQS FKKEPGTLVY IEKPRNTSGL SSLVDLGPPL
     VEKQGFAYST ATIPKDRETR ERMQAMEKQI ASLTGLVQSA LFKGPITSSS KEASSEKMVK
     ATANRNQADG AGTAHVSAGK VLGSVEFSLP PSQPLPAGTS PIHTSLLDMR RNVAELRLQL
     QQMRQLQLQN QEILRAMMKK AELEISNKVK ETMKRLEDPV QRQRTLVEQE RQKYLHEEER
     IVKKLCELED FVEDLKKDSS STGRVVTLKD VEDGAFLLRQ VGEAVATLKG EFPTLQNKMR
     AVLRIEVEAV RFLKEEPHKL DSLLKRVRSM TDVLTMLQRH VTDGLLKGTD ASQAAQYVAM
     EKATAAEVLK HQEETAHAPG QPLHCSTGSP GDVKSEVVPL STMTVHHVQS SPVVMQPSQH
     SSALMNPAQN LPGGTRPHTA SPPAITQEVT SAQSAPGPQS PQTPVNGSSM QSLFIEEIHS
     VSAKNRAVSI EKAEKKWEEK RQNLEHYNGK EFEKLLEEAQ ANIMKSIPNL EMPPASSPVS
     KGDAAGDKLE LSEDSPNSEQ ELDKIGGKSP PPPPPPPRRS YLPGSGLTTT RSGDVVYTGR
     SMSKVSSEDP GPTPQTRATK CPPEEPASAW APSPPPVPAP SSKEEEEEEE EGDKIMAELQ
     GSSTTPQTSR MPVPMTSKNR PGSLDKASKQ SKLQDPRQYR QANGSAKKAG GDCKPTSPSL
     PASKIPALSP SSGKSSSLPS ASGDSSNLPN APATKPSIAS TPLSPQAGRS AHSASLIPSV
     SNGSLKFQSP PHAGKGHHHL SFALQTQNGR AAPTTSSSSS PPSPASPTSL NQGARGIRTI
     HTPSLASYKA QNGSSSKATP STAKETS
//
ID   B2RY15_MOUSE            Unreviewed;      2542 AA.
AC   B2RY15;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 25.
DE   SubName: Full=Tln2 protein;
GN   Name=Tln2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC158057; AAI58058.1; -; mRNA.
DR   IPI; IPI00229647; -.
DR   UniGene; Mm.33645; -.
DR   ProteinModelPortal; B2RY15; -.
DR   SMR; B2RY15; 198-403, 489-892, 1839-1974, 2297-2479, 2496-2529.
DR   STRING; B2RY15; -.
DR   Ensembl; ENSMUST00000040025; ENSMUSP00000039633; ENSMUSG00000052698.
DR   MGI; MGI:1917799; Tln2.
DR   HOGENOM; HBG314610; -.
DR   HOVERGEN; HBG023870; -.
DR   InParanoid; B2RY15; -.
DR   Bgee; B2RY15; -.
DR   Genevestigator; B2RY15; -.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR   GO; GO:0005925; C:focal adhesion; IEA:InterPro.
DR   GO; GO:0001726; C:ruffle; IEA:InterPro.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0005158; F:insulin receptor binding; IEA:InterPro.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0007016; P:cytoskeletal anchoring at plasma membrane; IEA:InterPro.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR002558; ILWEQ.
DR   InterPro; IPR002404; Insln_rcpt_S1.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR015711; Talin.
DR   InterPro; IPR015710; Talin-rel.
DR   InterPro; IPR015224; Talin_cent.
DR   InterPro; IPR015009; Vinculin-bd_dom.
DR   InterPro; IPR006077; Vinculin/catenin.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.1420.10; Talin_cent; 1.
DR   PANTHER; PTHR19981; Talin; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF01608; I_LWEQ; 1.
DR   Pfam; PF02174; IRS; 1.
DR   Pfam; PF09141; Talin_middle; 1.
DR   Pfam; PF08913; VBS; 1.
DR   ProDom; PD011820; ILWEQ; 1.
DR   SMART; SM00295; B41; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   SUPFAM; SSF109880; Talin_cent; 1.
DR   SUPFAM; SSF47220; Vinculin/catenin; 6.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS50945; I_LWEQ; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   2542 AA;  271646 MW;  585DCE0EA0434952 CRC64;
     MVALSLKICV RHCNVVKTMQ FEPSTAVYDA CRVIRERVPE AQTGQASDYG LFLSDEDPRK
     GIWLEAGRTL DYYMLRNGDI LEYKKKQRPQ KIRMLDGSVK TVMVDDSKTV GELLVTICSR
     IGITNYEEYS LIQETIEEKK EEGTGTLKKD RTLLRDERKM EKLKAKLHTD DDLNWLDHSR
     TFREQGVDEN ETLLLRRKFF YSDQNVDSRD PVQLNLLYVQ ARDDILNGSH PVSFEKACEF
     GGFQAQIQFG PHVEHKHKPG FLDLKEFLPK EYIKQRGAEK RIFQEHKNCG EMSEIEAKVK
     YVKLARSLRT YGVSFFLVKE KMKGKNKLVP RLLGITKDSV MRVDEKTKEV LQEWPLTTVK
     RWAASPKSFT LDFGEYQESY YSVQTTEGEQ ISQLIAGYID IILKKKQSKD RFGLEGDEES
     TMLEESVSPK KSTILQQQFN RTGKAEHGSV ALPAVMRSGS SGPETFNVGS MPSPQQQVMV
     GQMHRGHMPP LTSAQQALMG TINTSMHAVQ QAQDDLSELD SLPPLGQDMA SRVWVQNKVD
     ESKHEIHSQV DAITAGTASV VNLTAGDPAD TDYTAVGCAI TTISSNLTEM SKGVKLLAAL
     MDDDVGSGED LLRAARTLAG AVSDLLKAVQ PTSGEPRQTV LTAAGSIGQA SGDLLRQIGE
     NETDERFQDV LMSLAKAVAN AAAMLVLKAK NVAQVAEDTV LQNRVIAAAT QCALSTSQLV
     ACAKVVSPTI SSPVCQEQLI EAGKLVDRSV ENCVRACQAA TGDSELLKQV SAAASVVSQA
     LHDLLQHVRQ FASRGEPIGR YDQATDTIMC VTESIFSSMG DAGEMVRQAR VLAQATSDLV
     NAMRSDAEAE IDMENSKKLL AAAKLLADST ARMVEAAKGA AANPENEDQQ QRLREAAEGL
     RVATNAAAQN AIKKKIVNRL EVAAKQAAAA ATQTIAASQN AAISNKNPSA QQQLVQSCKA
     VADHIPQLVQ GVRGSQAQAE DLSAQLALII SSQNFLQPGS KMVSSAKAAV PTVSDQAAAM
     QLSQCAKNLA TSLAELRTAS QKAHEACGPM EIDSALNTVQ TLKNELQDAK MAAAESQLKP
     LPGETLEKCA QDLGSTSKGV GSSMAQLLTC AAQGNEHYTG VAARETAQAL KTLAQAARGV
     AASTNDPEAA HAMLDSARDV MEGSAMLIQE AKQALIAPGD TESQQRLAQV AKAVSHSLNN
     CVNCLPGQKD VDVALKSIGE ASKKLLVDSL PPSTKPFQEA QSELNQAAAD LNQSAGEVVH
     ATRGQSGELA AASGKFSDDF DEFLDAGIEM AGQAQTKEDQ MQVIGNLKNI SMASSKLLLA
     AKSLSVDPGA PNAKNLLAAA ARAVTESINQ LIMLCTQQAP GQKECDNALR ELETVKGMLE
     NPNEPVSDLS YFDCIESVME NSKVLGESMA GISQNAKTGD LPAFGECVGI ASKALCGLTE
     AAAQAAYLVG ISDPNSQAGH QGLVDPIQFA RANQAIQMAC QNLVDPGSSP SQVLSAATIV
     AKHTSALCNA CRIASSKTAN PVAKRHFVQS AKEVANSTAN LVKTIKALDG DFSEDNRNKC
     RIATTPLIEA VENLTAFASN PEFASIPAQI SSEGSQAQEP ILVSAKTMLE SSSYLIRTAR
     SLAINPKDPP TWSVLAGHSH TVSDSIKSLI TSIRDKAPGQ RECDYSIDGI NRCIRDIEQA
     SLAAVSQSLA TRDDISVEAL QEQLTSVVQE IGHLIDPIAT AARGEAAQLG HKVTQLASYF
     EPLILAAVGV ASKMLDHQQQ MTVLDQTKTL AESALQMLYA AKEGGGNPKA HHTHDAITEA
     AQLMKEAVDD IMVTLNEAAS EVGLVGGMVD AIAEAMSKLD EGTPPEPKGT FVDYQTTVVK
     YSKAIAVTAQ EMMTKSVTNP EELGGLASQM TTDYGHLALQ GQMAAATAEP EEIGFQIRTR
     VQDLGHGCIF LVQKAGALQV CPTDSYTKRE LIECARSVTE KVSLVLSALQ AGNKGTQACI
     TAATAVSGII ADLDTTIMFA TAGTLNAENG ETFADHRENI LKTAKALVED TKLLVSGAAS
     TPDKLAQAAQ SSAATITQLA EVVKLGAASL GSNDPETQVV LINAIKDVAK ALSDLIGATK
     GAASKPADDP SMYQLKGAAK VMVTNVTSLL KTVKAVEDEA TRGTRALEAT IEYIKQELTV
     FQSKDIPEKT SSPEESIRMT KGITMATAKA VAAGNSCRQE DVIATANLSR KAVSDMLIAC
     KQASFYPDVS EEVRTRALRY GTECTLGYLD LLEHVLVILQ KPTPELKHQL AAFSKRVAGA
     VTELIQAAEA MKGTEWVDPE DPTVIAETEL LGAAASIEAA AKKLEQLKPR AKPKQADETL
     DFEEQILEAA KSIAAATSAL VKSASAAQRE LVAQGKVGSI PANAADDGQW SQGLISAARM
     VAAATSSLCE AANASVQGHA SEEKLISSAK QVAASTAQLL VACKVKADQD SEAMKRLQAA
     GNAVKRASDN LVRAAQKAAF GKADDDDVVV KTKFVGGIAQ IIAAQEEMLK KERELEEARK
     KLAQIRQQQY KFLPTELRED EG
//
ID   B2RY51_MOUSE            Unreviewed;      1976 AA.
AC   B2RY51;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 19.
DE   SubName: Full=Thyroid hormone receptor interactor 11;
GN   Name=Trip11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC158098; AAI58099.1; -; mRNA.
DR   IPI; IPI00380829; -.
DR   UniGene; Mm.208618; -.
DR   ProteinModelPortal; B2RY51; -.
DR   STRING; B2RY51; -.
DR   PRIDE; B2RY51; -.
DR   Ensembl; ENSMUST00000021605; ENSMUSP00000021605; ENSMUSG00000021188.
DR   MGI; MGI:1924393; Trip11.
DR   HOGENOM; HBG713026; -.
DR   HOVERGEN; HBG079281; -.
DR   InParanoid; B2RY51; -.
DR   OrthoDB; EOG4229HV; -.
DR   Bgee; B2RY51; -.
DR   Genevestigator; B2RY51; -.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000237; GRIP.
DR   PROSITE; PS50913; GRIP; 1.
PE   2: Evidence at transcript level;
KW   Receptor.
SQ   SEQUENCE   1976 AA;  226445 MW;  2320BFA3728213B5 CRC64;
     MSSWLGGLGS GLGQSLGQVG GSLASLTGQI SNFTKDMLLE GTEDVPADFP NSGREENEAT
     HSVLRSENER LKKLYTDLEE KHEASELQIK QQSSSYRSQL QQKEEEINHL KARQLALQDE
     LLRLQSAAQS AHSGSGSAPA ASASSSFSYG VSHRVSAFHE DDMDFGDVIS SQQEINRLSN
     EVSRLESELG HWRHIAQTKV QGAQSSDQTE ICKLQNIIKE LKQNRSQDLD DHQHELSALQ
     NAHQQKLTEI SRRHREELSD YEERIEELEN LLQQGGSGVT VTDHSKVYEM QNTIQILQME
     KVESTKQIED LENKIKEIHK RLSSAEHDQE VWKKEQERLE VEKREMTEQC ERLKLELSEA
     QQSALRQSDA AVEEETILPH SSSVAEVLRL QQALTDAENE IMRLRSLNQD ISLAEDNQKL
     QMCVQTLEKE KSLLSQEKEE LQISLSKLSS EYEVIKSTAS RDLDLFSQVH DLKHNLEAKE
     QELNQSIHEN EILMAELEEL DKQNQEATKH VILIKDQLSK QQSEGDSVIK KLKEELAGEK
     QRTHQLEDDK MNIIKELTVQ KEKLTHSEQA LSDLQLTKQK LEDKVEDLVD QLSKSEKNNF
     DIQKENHELR EHIRQNEEEL STVRSELTQS QTQGSSRNVK DDLLKERETQ VQNLKQNLSE
     VEQLNEHLEQ VAFDLRTENE ELLEAYEEVR NQLEESVAGN KQISLEKTAM LEWEKAPLET
     ELCRAEKRVL EEERKYEQTV QELSSACSPD TSALQLEQER LIQLNQEKDF EIAELKKSIE
     QMDTDHKRTK ETLSSSLEEQ KQLTQLINEK EICIVKLKEK SSELQKELDK CAQTLRKNET
     LRQTIEEKDR SLGSMKEENN HLQEELERLR EQQSRVVPAP EPRTLDSTTE LESELSQLHR
     IKGHLEEEIK HHQKMIEDQN QSKLQLLQSL QEQKKELDEF KYQHEQMSIS HTRLFLEKDE
     EIKNLQKTIE QIKAQLHEER QDSQTENSDI FQETKVQSLS IEHGSEKHDL SKAETERLVK
     GIKERELEIK LLNEKNTSLT KQIDQLSKDE VGKLTQIIQQ KDLEIQALHA RISSASYSQD
     VVYLQQQLHA YAMEREKVMV ILNEKTRENS QLKTEYHKVI DIISAKEAAL IKLQDENKKM
     STRFESSGQD MFKETIQNLS RIIREKDIEI DALSQKCQTL LTVLQTSGTG SEAGGVNSNQ
     FEELLQERDK LKQQVKKMEE WKQQVMTTVQ NMQHESAQLQ EELHQLQAQV SVDSDNNSKL
     QVDYTGLIQS YEQNETKLKN FGQELAQVQH SIGQLCNTKD LLLGKLDIMS PQLSSGSSLT
     SQAAEPLRAS QSSEPHESSQ LLQQEVDDLR KSLQEKDATI RTLQENNHRL SDSVAASSEV
     ERKEHEQADS EIKQLKEKQE VLQNLLKEKD LLIKAKSDQL HSSNENLANK VNENELLRQA
     VTNLKERILI LEMDISKLKG ENEKIVDASK GKETEYQALQ ETNMKFSMML REKEFECHSM
     REKALAFEQL LKEKEQGKAG ELNQLLNAVK SMQEKTVTFQ QERDQVMLAL KQKQMETSTL
     QNEVQRLRDK ESRLNQELQR LRDHLLESED SHTREALAAE DREAKLRKKV SVLEEKLVSS
     SNAMENASHQ ASVQVESLQE QLNMVSKQRD ETALQLSVSQ EQVKQYALSL ANLQMVLEHF
     QQEEKAMYSA ELEKQNHLLA EWKKKAESLE GKVLSLQERL DEANAALDSA SRLTEQLDLK
     EEQIEELKKQ NELHQEMLDD AQKKLMSLVN STEGKVDKVL MRNLFIGHFH TPKHQRHEVL
     RLMGSILGVK REEMEQLFAE DQGGVTWWMA GWLGGGSKSV PNTPLRPNQQ SVFNSSFSEL
     FVKFLETESH PSVPPPKLSV HGLKPLDSPG RRKADTGIPE SFRDTAESRA GRRTDVNPFL
     APRSAAVPLI NPAGHGPGGP GHLLLKPISD VLPTFTPLPV SPDNSAGVVL KDLLKQ
//
ID   RBM25_MOUSE             Reviewed;         841 AA.
AC   B2RY56; Q3TPH6; Q3U976; Q3UQU7; Q6NWW2; Q8BVT8; Q91XE6; Q9CT27;
AC   Q9CT49;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   08-MAR-2011, entry version 29.
DE   RecName: Full=RNA-binding protein 25;
DE   AltName: Full=RNA-binding motif protein 25;
GN   Name=Rbm25;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryo, Embryonic eye, Embryonic spinal ganglion, Macrophage,
RC   and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 20-302 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Colon, and Embryonic germ cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-581 AND SER-701, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-701, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-581; SER-675 AND
RP   SER-701, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: RNA-binding protein that acts as a regulator of
CC       alternative pre-mRNA splicing. Involved in apoptotic cell death
CC       through the regulation of the apoptotic factor BCL2L1 isoform
CC       expression. Modulates the ratio of proapoptotic BCL2L1 isoform S
CC       to antiapoptotic BCL2L1 isoform L mRNA expression. When
CC       overexpressed, stimulates proapoptotic BCL2L1 isoform S 5'-splice
CC       site (5'-ss) selection, whereas its depletion caused the
CC       accumulation of antiapoptotic BCL2L1 isoform L. Promotes BCL2L1
CC       isoform S 5'-ss usage through the 5'-CGGGCA-3' RNA sequence. Its
CC       association with LUC7L3 promotes U1 snRNP binding to a weak 5' ss
CC       in a 5'-CGGGCA-3'-dependent manner. Binds to the exonic splicing
CC       enhancer 5'-CGGGCA-3' RNA sequence located within exon 2 of the
CC       BCL2L1 pre-mRNA (By similarity).
CC   -!- SUBUNIT: Interacts with LUC7L3 and SRRM1 (By similarity).
CC       Specifically associates with functional splicing complexes,
CC       including Sm proteins and U1, U2, U4, U5 and U6 snRNAs (By
CC       similarity). Associates with exon junction complex (EJC) proteins,
CC       including APEX1, BAT1, NCBP1, RBM8A and RNPS1. Interaction with
CC       NCBP1 is RNA-dependent (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle (By similarity). Cytoplasm
CC       (By similarity). Note=Colocalizes predominantly, with SFRS2 and
CC       LUC7L3 splicing factors, in nuclear speckles. Cytoplasmic
CC       localization is faint (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=B2RY56-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=B2RY56-2; Sequence=VSP_036795;
CC       Name=3;
CC         IsoId=B2RY56-3; Sequence=VSP_036795, VSP_036796, VSP_036797;
CC   -!- PTM: Sumoylated (By similarity).
CC   -!- SIMILARITY: Contains 1 PWI domain.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH10792.1; Type=Erroneous initiation;
CC       Sequence=AAH66150.1; Type=Erroneous initiation;
CC       Sequence=AAH67400.1; Type=Erroneous initiation;
CC       Sequence=BAB27451.2; Type=Erroneous initiation;
CC       Sequence=BAE24941.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK011184; BAB27451.2; ALT_INIT; mRNA.
DR   EMBL; AK011403; BAB27595.3; -; mRNA.
DR   EMBL; AK076553; BAC36389.1; -; mRNA.
DR   EMBL; AK142132; BAE24941.1; ALT_INIT; mRNA.
DR   EMBL; AK151910; BAE30791.1; -; mRNA.
DR   EMBL; AK164367; BAE37760.1; -; mRNA.
DR   EMBL; BC158104; AAI58105.1; -; mRNA.
DR   EMBL; BC010792; AAH10792.1; ALT_INIT; mRNA.
DR   EMBL; BC066150; AAH66150.1; ALT_INIT; mRNA.
DR   EMBL; BC067400; AAH67400.1; ALT_INIT; mRNA.
DR   IPI; IPI00421119; -.
DR   IPI; IPI00662049; -.
DR   IPI; IPI00928541; -.
DR   RefSeq; NP_081625.3; NM_027349.3.
DR   UniGene; Mm.46005; -.
DR   ProteinModelPortal; B2RY56; -.
DR   SMR; B2RY56; 84-163, 748-839.
DR   PhosphoSite; B2RY56; -.
DR   PRIDE; B2RY56; -.
DR   Ensembl; ENSMUST00000010752; ENSMUSP00000010752; ENSMUSG00000010608.
DR   GeneID; 67039; -.
DR   KEGG; mmu:67039; -.
DR   CTD; 67039; -.
DR   MGI; MGI:1914289; Rbm25.
DR   eggNOG; roNOG15063; -.
DR   InParanoid; B2RY56; -.
DR   OrthoDB; EOG498V0R; -.
DR   Bgee; B2RY56; -.
DR   Genevestigator; B2RY56; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; ISS:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0000381; P:regulation of alternative nuclear mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR002483; PWI.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Gene3D; G3DSA:1.20.1390.10; PWI; 1.
DR   Pfam; PF01480; PWI; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00311; PWI; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF101233; PWI; 1.
DR   PROSITE; PS51025; PWI; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Cytoplasm; Isopeptide bond;
KW   mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; RNA-binding;
KW   Ubl conjugation.
FT   CHAIN         1    841       RNA-binding protein 25.
FT                                /FTId=PRO_0000368187.
FT   DOMAIN       87    164       RRM.
FT   DOMAIN      748    841       PWI.
FT   REGION      287    642       Necessary for nuclear speckle
FT                                localization (By similarity).
FT   COMPBIAS    294    606       Glu-rich.
FT   COMPBIAS    311    547       Arg-rich.
FT   MOD_RES     581    581       Phosphoserine.
FT   MOD_RES     673    673       Phosphoserine (By similarity).
FT   MOD_RES     675    675       Phosphoserine.
FT   MOD_RES     681    681       Phosphoserine (By similarity).
FT   MOD_RES     701    701       Phosphoserine.
FT   CROSSLNK    475    475       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   VAR_SEQ     181    183       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_036795.
FT   VAR_SEQ     292    302       KLEEEKGKKEK -> VVFLIFHLIPI (in isoform
FT                                3).
FT                                /FTId=VSP_036796.
FT   VAR_SEQ     303    841       Missing (in isoform 3).
FT                                /FTId=VSP_036797.
FT   CONFLICT    490    490       E -> G (in Ref. 1; BAB27451).
FT   CONFLICT    581    581       S -> F (in Ref. 2; AAH66150/AAH67400).
FT   CONFLICT    621    621       A -> D (in Ref. 1; BAB27451).
FT   CONFLICT    669    669       K -> R (in Ref. 1; BAB27451).
SQ   SEQUENCE   841 AA;  99926 MW;  50B28DE4FC2B2411 CRC64;
     MSFPPHLNRP PMGIPALPPG IPPPQFPGFP PPVPPGTPMI PVPMSIMAPA PTVLVPTVSM
     VGKHLGARKD HPGLKLKEND ENCGPTTTVF VGNISEKASD MLIRQLLAKC GLVLSWKRVQ
     GASGKLQAFG FCEYKEPEST LRALRLLHDL QIGEKKLLVK VDAKTKAQLD EWKAKKKANG
     VFKNARPETV TNDDEEALDE ETKRRDQMIK GAIEVLIREY SSELNAPSQE SDSHPRKKKK
     EKKEDIFRRF PVAPLIPYPL ITKEDINAIE MEEDKRDLIS REISKFRDTH KKLEEEKGKK
     EKERQEIEKE RRERERERER ERERRERERE REREREREKE KERERERERD RDRDRTKERD
     RDRERDRDRD RERSSDRNKD RSRSREKSRD RERERERERE RERERERERE RERERERERE
     REREKDKKRD REEDEEDAYE RRKLERKLRE KEAAYQERLK NWEIRERKKT REYEKEAERE
     EERRREMAKE AKRLKEFLED YDDDRDDPKY YRGSALQKRL RDREKEMEAD ERDRKREKEE
     LEEIRQRLLA EGHPDPDAEL QRMEQEAERR RQPQIKQEPE SEEEEEEKQE KEEKREEPVE
     EEEEPEQKPC LKPTLRPISS APSVSSASGN ATPNTPGDES PCGIIIPHEN SPDQQQPEEH
     RPKIGLSLKL GASNSPGQPN SVKRKKLPVD SVFNKFEDED SDDVPRKRKL VPLDYGEDDK
     NATKGTVNTE EKRKHIKSLI EKIPTAKPEL FAYPLDWSIV DSILMERRIR PWINKKIIEY
     IGEEEATLVD FVCSKVMAHS SPQSILDDVA MVLDEEAEVF IVKMWRLLIY ETEAKKIGLV
     K
//
ID   B2RY58_MOUSE            Unreviewed;      1201 AA.
AC   B2RY58;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   11-JAN-2011, entry version 27.
DE   SubName: Full=Hyperpolarization-activated, cyclic nucleotide-gated K+ 4;
DE   SubName: Full=MCG22630;
GN   Name=Hcn4; ORFNames=mCG_22630;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 cyclic nucleotide-binding domain.
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DR   EMBL; BC158106; AAI58107.1; -; mRNA.
DR   EMBL; BC158108; AAI58109.1; -; mRNA.
DR   EMBL; CH466522; EDL25959.1; -; Genomic_DNA.
DR   IPI; IPI00353056; -.
DR   RefSeq; NP_001074661.1; NM_001081192.1.
DR   UniGene; Mm.151967; -.
DR   ProteinModelPortal; B2RY58; -.
DR   SMR; B2RY58; 521-721.
DR   PRIDE; B2RY58; -.
DR   Ensembl; ENSMUST00000034889; ENSMUSP00000034889; ENSMUSG00000032338.
DR   GeneID; 330953; -.
DR   KEGG; mmu:330953; -.
DR   CTD; 330953; -.
DR   MGI; MGI:1298209; Hcn4.
DR   HOGENOM; HBG447083; -.
DR   HOVERGEN; HBG039490; -.
DR   InParanoid; B2RY58; -.
DR   NextBio; 399644; -.
DR   Bgee; B2RY58; -.
DR   Genevestigator; B2RY58; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005222; F:intracellular cAMP activated cation channel activity; IMP:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0008016; P:regulation of heart contraction; IMP:MGI.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR013621; Ion_trans_N.
DR   InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF08412; Ion_trans_N; 1.
DR   PRINTS; PR01463; EAGCHANLFMLY.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; cNMP_binding; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
PE   2: Evidence at transcript level;
KW   Ion transport; Ionic channel; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
SQ   SEQUENCE   1201 AA;  129065 MW;  7D04EBDE4D258517 CRC64;
     MDKLPPSMRK RLYSLPQQVG AKAWIMDEEE DGEEEGAGGR QDPSRRSIRL RPLPSPSPSV
     AAGCSESRGA ALGATESEGP GRSAGKSSTN GDCRRFRGSL ASLGSRGGGS GGAGGGSSLG
     HLHDSAEERR LIAAEGDASP GEDRTPPGLA TEPERPATAA QPAASPPPQQ PPQPASASCE
     QPSADTAIKV EGGAAASDQI LPEAEVRLGQ SGFMQRQFGA MLQPGVNKFS LRMFGSQKAV
     EREQERVKSA GFWIIHPYSD FRFYWDLTML LLMVGNLIII PVGITFFKDE NTTPWIVFNV
     VSDTFFLIDL VLNFRTGIVV EDNTEIILDP QRIKMKYLKS WFVVDFISSI PVDYIFLIVE
     TRIDSEVYKT ARALRIVRFT KILSLLRLLR LSRLIRYIHQ WEEIFHMTYD LASAVVRIVN
     LIGMMLLLCH WDGCLQFLVP MLQDFPHDCW VSINGMVNNS WGKQYSYALF KAMSHMLCIG
     YGRQAPVGMS DVWLTMLSMI VGATCYAMFI GHATALIQSL DSSRRQYQEK YKQVEQYMSF
     HKLPPDTRQR IHDYYEHRYQ GKMFDEESIL GELSEPLREE IINFNCRKLV ASMPLFANAD
     PNFVTSMLTK LRFEVFQPGD YIIREGTIGK KMYFIQHGVV SVLTKGNKET KLADGSYFGE
     ICLLTRGRRT ASVRADTYCR LYSLSVDNFN EVLEEYPMMR RAFETVALDR LDRIGKKNSI
     LLHKVQHDLN SGVFNYQENE IIQQIVRHDR EMAHCAHRVQ AAASATPTPT PVIWTPLIQA
     PLQAAAATTS VAIALTHHPR LPAAIFRPPP GPGLGNLGAG QTPRHPRRLQ SLIPSALGSA
     SPASSPSQVD TPSSSSFHIQ QLAGFSAPPG LSPLLPSSSS SPPPGACGSP PAPTPSTSTA
     AAASTTGFGH FHKALGGSLS SSDSPLLTPL QPGARSPQAA QPPPPLPGAR GGLGLLEHFL
     PPPPSSRSPS SSPGQLGQPP GELSLGLAAG PSSTPETPPR PERPSFMAGA SGGASPVAFT
     PRGGLSPPGH SPGPPRTFPS APPRASGSHG SLLLPPASSP PPPQVPQRRG TPPLTPGRLT
     QDLKLISASQ PALPQDGAQT LRRASPHSSG ESVAAFSLYP RAGGGSGSSG GLGPPGRPYG
     AIPGQHVTLP RKTSSGSLPP PLSLFGARAA SSGGPPLTTA APQREPGARS EPVRSKLPSN
     L
//
ID   B2Z892_MOUSE            Unreviewed;       497 AA.
AC   B2Z892;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   11-JAN-2011, entry version 20.
DE   SubName: Full=6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase 2 variant 4;
DE            EC=2.7.1.105;
GN   Name=Pfkfb2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=14623077; DOI=10.1016/S0014-5793(03)01179-7;
RA   Minchenko O.H., Opentanova I.L., Caro J.;
RT   "Hypoxic regulation of the 6-phosphofructo-2-kinase/fructose-2,6-
RT   bisphosphatase gene family (PFKFB-1-4) expression in vivo.";
RL   FEBS Lett. 554:264-270(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Minchenko D., Tsuchihara K., Moenner M., Bikfalvi A., Komisarenko S.,
RA   Esumi H., Caro J., Minchenko O.;
RT   "Unique alternative splice variants of mouse 6-phosphofructo-2-
RT   kinase/fructose-2,6-bisphosphatase-2.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Minchenko D.O., Minchenko O.H., Tsuchihara K., Esumi H., Caro J.,
RA   Mykhalchenko V., Moenner M., Bikfalvi A., Komisarenko S.;
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; EU616667; ACC97555.1; -; mRNA.
DR   IPI; IPI00938511; -.
DR   RefSeq; NP_001155888.1; NM_001162416.1.
DR   UniGene; Mm.249861; -.
DR   ProteinModelPortal; B2Z892; -.
DR   SMR; B2Z892; 38-447.
DR   STRING; B2Z892; -.
DR   Ensembl; ENSMUST00000066863; ENSMUSP00000066426; ENSMUSG00000026409.
DR   GeneID; 18640; -.
DR   KEGG; mmu:18640; -.
DR   CTD; 18640; -.
DR   MGI; MGI:107815; Pfkfb2.
DR   HOVERGEN; HBG005628; -.
DR   InParanoid; B2Z892; -.
DR   Bgee; B2Z892; -.
DR   Genevestigator; B2Z892; -.
DR   GO; GO:0003873; F:6-phosphofructo-2-kinase activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IEA:InterPro.
DR   InterPro; IPR003094; 6Pfruct_kin.
DR   InterPro; IPR013079; 6Phosfructo_kin.
DR   InterPro; IPR016260; Bifunct_6PFK/fruc_bisP_Ptase.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR001345; PG/BPGM_mutase_AS.
DR   PANTHER; PTHR10606; 6Pfruct_kin; 1.
DR   Pfam; PF01591; 6PF2K; 1.
DR   Pfam; PF00300; PGAM; 1.
DR   PIRSF; PIRSF000709; 6PFK_2-Ptase; 1.
DR   PRINTS; PR00991; 6PFRUCTKNASE.
DR   SMART; SM00855; PGAM; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   2: Evidence at transcript level;
KW   Kinase; Transferase.
SQ   SEQUENCE   497 AA;  57332 MW;  AEA15C499C5EBB07 CRC64;
     MSENSTFSPE DCNSSYKPHA SNLRRAGKTC SWASYMTNSP TLIVMIGLPA RGKTYVSKKL
     TRYLNWIGVP TKVFNLGVYR REAVKSYQSY DFFRHDNEEA MKIRKQCALV ALEDVKAYFT
     EESGQIAVFD ATNTTRERRD MILNFAKQNA FKVFFVESVC DDPDVIAANI LEVKVSSPDY
     PERNRENVME DFLKRIECYK VTYQPLDPDN YDKDLSFIKV INVGQRFLVN RVQDYIQSKI
     VYYLMNIHVH PRTIYLCRHG ESEFNLLGKI GGDSGLSVRG KQFAHALKKF LEEQEIQDLK
     VWTSQLKRTI QTAESLGVTY EQWKILNEID AGVCEEMTYS EIEQRYPEEF ALRDQEKYLY
     RYPGGESYQD LVQRLEPVIM ELERQGNILV ISHQAVMRCL LAYFLDKGAG CKVETITLNV
     DAVDTHRDKP THNFPKSQTP VRMRRNSFTP LSSSNTIRRP RNYSVGSRPL KPLSPLRALD
     MQEGADQPKT QVSIPVV
//
ID   B3V097_MOUSE            Unreviewed;       630 AA.
AC   B3V097;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   30-NOV-2010, entry version 12.
DE   SubName: Full=BetaCstF-64 variant 3;
GN   Name=Cstf2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=19284619; DOI=10.1186/1471-2199-10-22;
RA   Shankarling G.S., Coates P.W., Dass B., Macdonald C.C.;
RT   "A family of splice variants of CstF-64 expressed in vertebrate
RT   nervous systems.";
RL   BMC Mol. Biol. 10:22-22(2009).
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DR   EMBL; EU616680; ACF05700.1; -; mRNA.
DR   IPI; IPI00903356; -.
DR   UniGene; Mm.67938; -.
DR   STRING; B3V097; -.
DR   HOVERGEN; HBG051145; -.
DR   Genevestigator; B3V097; -.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   630 AA;  66425 MW;  3B993DC78812310F CRC64;
     MAGLPVRDPA VDRSLRSVFV GNIPYEATEE QLKDIFSEVG PVVSFRLVYD RETGKPKGYG
     FCEYQDQETA LSAMRNLNGR EFSGRALRVD NAASEKNKEE LKSLGTGAPV IESPYGESIS
     PEDAPESISK AVASLPPEQM FELMKQMKLC VQNSPQEARN MLLQNPQLAY ALLQAQVVMR
     IVDPEIALKI LHRQTNIPTL ISGNPQPVHV AGPGSGPNVS MNQQNPQAPQ AQSLGGMHVN
     GAPPMMQASM PGGVPAPVQM AAAVGGPGPG SLAPAGVMQA QVGMQGAGPV PMERGQGTLQ
     HSPVGPAGPA SIERVQGQRT WMIWASVRGS TPSLLVSGGL DGIAVCVPMQ DPRAAMQRGA
     LPTNVPTPRG LLGDAPNDPR GGTLMTVTGD VEPRAYLGPP PPPHQGPPMH HVPGHEGRGP
     PPHDMRGGPL AEPRPLMAEP RGPMLDQRGP PLDARGGRDP RGLDARGMEA RAMEARGLDA
     RGLEARAMEA RAMEARAMEA RAMEARAMEA RAMEARGMDT RGPVPGPRGP MPSGIQGPNP
     MNMGAVVPQG SRQVPVMQGA GMQGASMQGG SQPGGFSPGQ SQVTPQDHEK AALIMQVLQL
     TADQIAMLPP EQRQSILILK EQIQKSTGAP
//
ID   B5TVM2_MOUSE            Unreviewed;       646 AA.
AC   B5TVM2;
DT   04-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 1.
DT   08-MAR-2011, entry version 18.
DE   SubName: Full=Lisch-like isoform 1;
GN   Name=Ildr2; Synonyms=D1Ertd471e, Ll;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   PubMed=18654634; DOI=10.1371/journal.pgen.1000137;
RA   Dokmanovic-Chouinard M., Chung W.K., Chevre J.C., Watson E., Yonan J.,
RA   Wiegand B., Bromberg Y., Wakae N., Wright C.V., Overton J., Ghosh S.,
RA   Sathe G.M., Ammala C.E., Brown K.K., Ito R., LeDuc C., Solomon K.,
RA   Fischer S.G., Leibel R.L.;
RT   "Positional cloning of 'Lisch-Like', a candidate modifier of
RT   susceptibility to type 2 diabetes in mice.";
RL   PLoS Genet. 4:E1000137-E1000137(2008).
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DR   EMBL; FJ024494; ACH90402.1; -; mRNA.
DR   IPI; IPI00944785; -.
DR   UniGene; Mm.101743; -.
DR   Ensembl; ENSMUST00000111416; ENSMUSP00000107047; ENSMUSG00000040612.
DR   MGI; MGI:1196370; Ildr2.
DR   eggNOG; roNOG15931; -.
DR   HOGENOM; HBG715011; -.
DR   HOVERGEN; HBG061576; -.
DR   InParanoid; B5TVM2; -.
DR   OrthoDB; EOG45QHD1; -.
DR   Bgee; B5TVM2; -.
DR   Genevestigator; B5TVM2; -.
DR   GO; GO:0030154; P:cell differentiation; IMP:MGI.
DR   GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
DR   GO; GO:0030073; P:insulin secretion; IMP:MGI.
DR   GO; GO:0031016; P:pancreas development; IMP:MGI.
DR   GO; GO:0009749; P:response to glucose stimulus; IMP:MGI.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR008664; LISCH7.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Pfam; PF05624; LSR; 1.
DR   SMART; SM00409; IG; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   646 AA;  71651 MW;  E9F81CDF5B5CEEF9 CRC64;
     MDRVVLGWTA VFWLTAMVEG LQVTVPDKKK VAMLFQPTVL RCHFSTSSHQ PAVVQWKFKS
     YCQDRMGESL GMSSPRAQAL SKRNLEWDPY LDCLDSRRTV RVVASKQGST VTLGDFYRGR
     EITIVHDADL QIGKLMWGDS GLYYCIITTP DDLEGKNEDS VELLVLGRTG LLADLLPSFA
     VEIMPEWVFV GLVILGIFLF FVLVGICWCQ CCPHSCCCYV RCPCCPDSCC CPQALYEAGK
     AAKAGYPPSV SGVPGPYSIP SVPLGGAPSS GMLMDKPHPP PLAPSDSTGG SHSVRKGYRI
     QADKERDSMK VLYYVEKELA QFDPARRMRG RYNNTISELS SLHDDDSNFR QSYHQMRNKQ
     FPMSGDLESN PDYWSGVMGG NSGTNRGPAL EYNKEDRESF RHSQQRSKSE MLSRKNFATG
     VPAVSMDELA AFADSYGQRS RRANGNSHEA RAGSRFERSE SRAHGAFYQD GSLDEYYGRG
     RSREPPGDGE RGWTYSPAPA RRRPPEDAPL PRLVSRTPGT APKYDHSYLS SVLERQARPE
     SSSRGGSLET PSKLGAQLGP RSASYYAWSP PTTYKAGASE GEDEDDAADE DALPPYSELE
     LSRGELSRGP SYRGRDLSFH SNSEKRRKKE PAKKPGDFPT RMSLVV
//
ID   B7ZBV3_MOUSE            Unreviewed;       726 AA.
AC   B7ZBV3;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   05-OCT-2010, entry version 16.
DE   SubName: Full=Potassium voltage-gated channel, subfamily Q, member 2;
DE   Flags: Fragment;
GN   Name=Kcnq2; ORFNames=RP23-401L17.2-015;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Wall M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL450341; CAX15856.1; -; Genomic_DNA.
DR   IPI; IPI00752451; -.
DR   UniGene; Mm.40615; -.
DR   UniGene; Mm.440175; -.
DR   ProteinModelPortal; B7ZBV3; -.
DR   PRIDE; B7ZBV3; -.
DR   Ensembl; ENSMUST00000129695; ENSMUSP00000123488; ENSMUSG00000016346.
DR   MGI; MGI:1309503; Kcnq2.
DR   HOVERGEN; HBG059014; -.
DR   Bgee; B7ZBV3; -.
DR   Genevestigator; B7ZBV3; -.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR020969; Ankyrin-G_BS.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003937; K_chnl_volt-dep_KCNQ.
DR   InterPro; IPR013821; K_chnl_volt-dep_KCNQ_C.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF03520; KCNQ_channel; 1.
DR   Pfam; PF11956; KCNQC3-Ank-G_bd; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01459; KCNQCHANNEL.
PE   4: Predicted;
KW   Ion transport; Ionic channel; Membrane; Potassium; Potassium channel;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport.
FT   NON_TER       1      1
SQ   SEQUENCE   726 AA;  80275 MW;  191B2F3578FFCF1B CRC64;
     IKEYEKSSEG ALYILEIVTI VVFGVEYFVR IWAAGCCCRY RGWRGRLKFA RKPFCVIDIM
     VLIASIAVLA AGSQGNVFAT SALRSLRFLQ ILRMIRMDRR GGTWKLLGSV VYAHSKELVT
     AWYIGFLCLI LASFLVYLAE KGENDHFDTY ADALWWGLIT LTTIGYGDKY PQTWNGRLLA
     ATFTLIGVSF FALPAGILGS GFALKVQEQH RQKHFEKRRN PAAGLIQSAW RFYATNLSRT
     DLHSTWQYYE RTVTVPMYSS QTQTYGASRL IPPLNQLELL RNLKSKSGLT FRKEPQPEPS
     PSPRGMAAKG KGSPQAQTVR RSPSADQSLD DSPSKVPKSW SFGDRSRTRQ AFRIKGAASR
     QNSEEASLPG EDIVEDNKSC NCEFVTEDLT PGLKVSIRAV CVMRFLVSKR KFKESLRPYD
     VMDVIEQYSA GHLDMLSRIK SLQSRVDQIV GRGPTITDKD RTKGPAETEL PEDPSMMGRL
     GKVEKQVLSM EKKLDFLVSI YTQRMGIPPA ETEAYFGAKE PEPAPPYHSP EDSRDHADKH
     GCIIKIVRST SSTGQRNYAA PPAIPPAQCP PSTSWQQSHQ RHGTSPVGDH GSLVRIPPPP
     AHERSLSAYG GGNRASTEFL RLEGTPACRP SEAALRDSDT SISIPSVDHE ELERSFSGFS
     ISQSKENLDA LGSCYAAVAP CAKVRPYIAE GESDTDSDLC TPCGPPPRSA TGEGPFGDVA
     WAGPRK
//
ID   B7ZBW1_MOUSE            Unreviewed;       852 AA.
AC   B7ZBW1;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-FEB-2011, entry version 16.
DE   SubName: Full=Potassium voltage-gated channel, subfamily Q, member 2;
GN   Name=Kcnq2; ORFNames=RP23-401L17.2-017;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Wall M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL450341; CAX15864.1; -; Genomic_DNA.
DR   IPI; IPI00922967; -.
DR   UniGene; Mm.40615; -.
DR   UniGene; Mm.440175; -.
DR   ProteinModelPortal; B7ZBW1; -.
DR   PRIDE; B7ZBW1; -.
DR   Ensembl; ENSMUST00000103051; ENSMUSP00000099340; ENSMUSG00000016346.
DR   MGI; MGI:1309503; Kcnq2.
DR   GeneTree; ENSGT00550000074513; -.
DR   HOVERGEN; HBG059014; -.
DR   Bgee; B7ZBW1; -.
DR   Genevestigator; B7ZBW1; -.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR020969; Ankyrin-G_BS.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003937; K_chnl_volt-dep_KCNQ.
DR   InterPro; IPR003947; K_chnl_volt-dep_KCNQ2.
DR   InterPro; IPR013821; K_chnl_volt-dep_KCNQ_C.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF03520; KCNQ_channel; 1.
DR   Pfam; PF11956; KCNQC3-Ank-G_bd; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01461; KCNQ2CHANNEL.
DR   PRINTS; PR01459; KCNQCHANNEL.
PE   4: Predicted;
KW   Ion transport; Ionic channel; Membrane; Potassium; Potassium channel;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport.
SQ   SEQUENCE   852 AA;  93939 MW;  454DCBB0FA3CF84C CRC64;
     MVQKSRNGGV YPGTSGEKKL KVGFVGLDPG APDSTRDGAL LIAGSEAPKR GSVLSKPRTG
     GAGAGKPPKR NAFYRKLQNF LYNVLERPRG WAFIYHAYVF LLVFSCLVLS VFSTIKEYEK
     SSEGALYILE IVTIVVFGVE YFVRIWAAGC CCRYRGWRGR LKFARKPFCV IDIMVLIASI
     AVLAAGSQGN VFATSALRSL RFLQILRMIR MDRRGGTWKL LGSVVYAHSK ELVTAWYIGF
     LCLILASFLV YLAEKGENDH FDTYADALWW GLITLTTIGY GDKYPQTWNG RLLAATFTLI
     GVSFFALPAG ILGSGFALKV QEQHRQKHFE KRRNPAAGLI QSAWRFYATN LSRTDLHSTW
     QYYERTVTVP MYSSQTQTYG ASRLIPPLNQ LELLRNLKSK SGLTFRKEPQ PEPSPSQKVS
     LKDRVFSSPR GMAAKGKGSP QAQTVRRSPS ADQSLDDSPS KVPKSWSFGD RSRTRQAFRI
     KGAASRQNSE EASLPGEDIV EDNKSCNCEF VTEDLTPGLK VSIRAVCVMR FLVSKRKFKE
     SLRPYDVMDV IEQYSAGHLD MLSRIKSLQS RVDQIVGRGP TITDKDRTKG PAETELPEDP
     SMMGRLGKVE KQVLSMEKKL DFLVSIYTQR MGIPPAETEA YFGAKEPEPA PPYHSPEDSR
     DHADKHGCII KIVRSTSSTG QRNYAAPPAI PPAQCPPSTS WQQSHQRHGT SPVGDHGSLV
     RIPPPPAHER SLSAYGGGNR ASTEFLRLEG TPACRPSEAA LRDSDTSISI PSVDHEELER
     SFSGFSISQS KENLDALGSC YAAVAPCAKV RPYIAEGESD TDSDLCTPCG PPPRSATGEG
     PFGDVAWAGP RK
//
ID   B7ZC24_MOUSE            Unreviewed;       406 AA.
AC   B7ZC24;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-FEB-2011, entry version 14.
DE   SubName: Full=Nuclear receptor coactivator 5;
GN   Name=Ncoa5; ORFNames=RP23-61O3.13-008;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Sycamore N.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL591495; CAX16082.1; -; Genomic_DNA.
DR   IPI; IPI00885273; -.
DR   UniGene; Mm.233080; -.
DR   PRIDE; B7ZC24; -.
DR   Ensembl; ENSMUST00000122070; ENSMUSP00000113166; ENSMUSG00000039804.
DR   MGI; MGI:2385165; Ncoa5.
DR   GeneTree; ENSGT00530000064134; -.
DR   HOVERGEN; HBG052585; -.
DR   Bgee; B7ZC24; -.
DR   Genevestigator; B7ZC24; -.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR004154; Anticodon-bd.
DR   Gene3D; G3DSA:3.40.50.800; Anticodon_bd; 1.
DR   SUPFAM; SSF52954; Anticodon_bd; 1.
PE   4: Predicted;
KW   Receptor.
SQ   SEQUENCE   406 AA;  48075 MW;  5D2E2B8A35CF48AD CRC64;
     MNTAPSRPSP TRRDPYSFGD SRDTRRDRSP IRGSPRREPR DGRNGRDARD SRDIRDPRDL
     RDRRDSRDIR DHRDSRSVRE ARDLRDFRDF RDLRDSRDFR DHRDPVYDRY RDIRDSRDPL
     YRREGSYDRY LRVDDYCRRK DDSYFDRYRD SFDGRGPPGP ESQSRAKERL KREERRREEL
     YRRYFEEIQR RFDAERPVDC SVIVVNKQTK DYAESVGRKV RDLGMVVDLI FLNTEVSLSQ
     ALEDVSRGGS PFAIVITQQH QIHRSCTVNI MFGTPQEHRN MPQADAMVLV ARNYERYKND
     CREKEREEIA RQAAKMANDA ILQERDRGGP EEGGRGGHPP AIQSLINLLA DNRYLTAEET
     DKIINYLRER KERLLRSSAD SLPGELRGRA EARFPASHSG RPRVPR
//
ID   B7ZCC0_MOUSE            Unreviewed;       257 AA.
AC   B7ZCC0;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 15.
DE   SubName: Full=Syntaxin 16;
DE   Flags: Fragment;
GN   Name=Stx16; ORFNames=RP23-477F4.3-005;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Pearce A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL669896; CAX15281.1; -; Genomic_DNA.
DR   IPI; IPI00918940; -.
DR   UniGene; Mm.277977; -.
DR   Ensembl; ENSMUST00000156054; ENSMUSP00000116618; ENSMUSG00000027522.
DR   MGI; MGI:1923396; Stx16.
DR   GeneTree; ENSGT00550000075126; -.
DR   HOVERGEN; HBG057612; -.
DR   Bgee; B7ZCC0; -.
DR   Genevestigator; B7ZCC0; -.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR006011; Syntaxin_N.
DR   InterPro; IPR010989; t-SNARE.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   Pfam; PF05739; SNARE; 1.
DR   Pfam; PF00804; Syntaxin; 1.
DR   SUPFAM; SSF47661; t-snare; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   4: Predicted;
FT   NON_TER       1      1
FT   NON_TER     257    257
SQ   SEQUENCE   257 AA;  29315 MW;  90216A90A5825DB3 CRC64;
     RRLTDAFLLL RNNSIQTRQL LAEQVSSHTT SSPLHSRSIA AELDELADDR MALVSGISLD
     PEAAIGVTKR SPPKWVDGVD EIQYDVGRIK QKMKELASLH DKHLNRPTLD DSSEEEHAIE
     ITTQEVTQLF HRCQRAVQAL PSRARRACSE QEERLLRNVV ASLAQALQEL STSFRHAQSD
     YLKRMKNREE RSQHFFDTPV PLMDDGDDAT LYGQGTVLDR IDYNVEQSCV KTEDGLKQLH
     KAEQYQKKNR KMLVIVI
//
ID   B7ZCF1_MOUSE            Unreviewed;       451 AA.
AC   B7ZCF1;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 19.
DE   SubName: Full=Proteasome (Prosome, macropain) 26S subunit ATPase 3;
GN   Name=Psmc3; ORFNames=RP23-263H8.1-009;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Smith M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
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DR   EMBL; AL691439; CAX15265.1; -; Genomic_DNA.
DR   IPI; IPI00405114; -.
DR   ProteinModelPortal; B7ZCF1; -.
DR   Ensembl; ENSMUST00000002171; ENSMUSP00000002171; ENSMUSG00000002102.
DR   MGI; MGI:1098754; Psmc3.
DR   HOGENOM; HBG724153; -.
DR   HOVERGEN; HBG000109; -.
DR   OMA; DNEIKIM; -.
DR   OrthoDB; EOG46143Z; -.
DR   PhylomeDB; B7ZCF1; -.
DR   Bgee; B7ZCF1; -.
DR   Genevestigator; B7ZCF1; -.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   GO; GO:0001824; P:blastocyst development; IMP:MGI.
DR   GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR   InterPro; IPR005937; 26S_Psome_P45.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   Pfam; PF00004; AAA; 1.
DR   SMART; SM00382; AAA; 1.
DR   TIGRFAMs; TIGR01242; 26Sp45; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding; Proteasome.
SQ   SEQUENCE   451 AA;  50396 MW;  8B6FEDA447AAE3B5 CRC64;
     MQEMNLLPTP ESPVTRQEKM ATVWDEAEQD GIGEEVLKMS TEEIVQRTRL LDSEIKIMKS
     EVLRVTHELQ AMKDKIKENS EKIKVNKTLP YLVSNVIELL DVDPNDQEED GANIDLDSQR
     KGKCAVIKTS TRQTYFLPVI GLVDAEKLKP GDLVGVNKDS YLILETLPTE YDSRVKAMEV
     DERPTEQYSD IGGLDKQIQE LVEAIVLPMN HKEKFENLGI QPPKGVLMYG PPGTGKTLLA
     RACAAQTKAT FLKLAGPQLV QMFIGDGAKL VRDAFALAKE KAPSIIFIDE LDAIGTKRFD
     SEKAGDREVQ RTMLELLNQL DGFQPNTQVK VIAATNRVDI LDPALLRSGR LDRKIEFPMP
     NEEARARIMQ IHSRKMNVSP DVNYEELARC TDDFNGAQCK AVCVEAMCWA AFTAHRDTCD
     PKLRVGHAWC RPTPPAAGAE TRCPGVHLRQ S
//
ID   B7ZCJ1_MOUSE            Unreviewed;      1955 AA.
AC   B7ZCJ1;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 20.
DE   SubName: Full=Rho GTPase activating protein 21;
GN   Name=Arhgap21; ORFNames=RP23-436G18.3-012;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Lovell J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Brown J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RA   Williams S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
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DR   EMBL; AL929100; CAX15605.1; -; Genomic_DNA.
DR   EMBL; AL773540; CAX15605.1; JOINED; Genomic_DNA.
DR   EMBL; BX649226; CAX15605.1; JOINED; Genomic_DNA.
DR   EMBL; BX649226; CAX15708.1; -; Genomic_DNA.
DR   EMBL; AL773540; CAX15708.1; JOINED; Genomic_DNA.
DR   EMBL; AL929100; CAX15708.1; JOINED; Genomic_DNA.
DR   EMBL; AL773540; CAX15782.1; -; Genomic_DNA.
DR   EMBL; AL929100; CAX15782.1; JOINED; Genomic_DNA.
DR   EMBL; BX649226; CAX15782.1; JOINED; Genomic_DNA.
DR   IPI; IPI00918972; -.
DR   RefSeq; NP_001121556.2; NM_001128084.2.
DR   UniGene; Mm.28507; -.
DR   UniGene; Mm.465492; -.
DR   Ensembl; ENSMUST00000154230; ENSMUSP00000122497; ENSMUSG00000036591.
DR   GeneID; 71435; -.
DR   KEGG; mmu:71435; -.
DR   CTD; 71435; -.
DR   MGI; MGI:1918685; Arhgap21.
DR   GeneTree; ENSGT00600000084250; -.
DR   HOGENOM; HBG505226; -.
DR   HOVERGEN; HBG106694; -.
DR   Bgee; B7ZCJ1; -.
DR   Genevestigator; B7ZCJ1; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   4: Predicted;
KW   GTPase activation.
SQ   SEQUENCE   1955 AA;  216981 MW;  1E5AF7E92BEA8231 CRC64;
     MMATHWTGLP EEDGDKLKAC GAASACEVSK NKDGKDQGEP VSPSEDEPFS WPGPKTVMLK
     RTSQGFGFTL RHFIVYPPES AIQFSYKDEE NGNRGGKQRN RLEPMDTIFV KQVKEGGPAF
     EAGLCTGDRI IKVNGESVIG KTYSQVIALI QNSDTTLELS VMPKDEDILQ VLQFTKDVTA
     LAYSQDAYLK GNEAYSGNAR NIPEPPPVCY PWLPSTPSAT AQPVETCPPD SLPNKQQTSA
     PVLTQPGRAY RMEIQVPPSP TDVAKSNTAV CVCNESVRTV IVPSEKVVDL LANRNNPSGP
     SHRTEEVRYG VNEQASTKAA SRTTSPASVP TAHLIHQTTG SRSLEPSGIL LKSGNYSGHS
     EGISSSRSQA VDSPPVSVNH YSANSHQHID WKNYKTYKEY IDNRRLHIGC RTIQERLDSL
     RAASQSAADY NQVVPTRTTL QVRRRSTSHD RVPQSVQIRQ RSVSQERLED SVLMKYCPRS
     ASQGALTSPP VSFNNHRTRS WDYIEGQTEA TATVNSESQI PDSNGERKQT YKWSGFTEQD
     DRRGIHERPR QQEMHKPFRG SNLTVAPVVN SDNRRLVGRG VGPVSQFKKI PPDLRPPHSN
     RNFPTTTGVS LQRGIAQDRS PLVKVRSNSL KVPPPPVSKP SFSQHSLASM KDQRPVNHLH
     QHSVLSQQTQ FRSESTFEHQ LETEVSSCLP GTSAKTSPQL SENLGTSDLE LPAIPRNGDI
     NLQEAEIQQP DVLDNKESVI LREKPQSGRQ TPQPLRHQSY ILAVNDQETG SDTTCWLPND
     ARREVHIKRM EERKASSTSP PGDSLASIPF IDEPTSPSID HEIAHIPASA VISASTAHVP
     SIATVPPSLT TSAPLIRRQL SHDQESVGPP SLDGQHSSKT ERSKSYDEGL DDYREDAKLS
     FKHVSSLKGI KITDSQKSSE DSGSRKGSSS EVFSDAAREG WLQFRPLVTD KGKRVGGSIR
     PWKQMYVVLR GHSLYLYKDR REQTTPSEEE QPISVNACLI DISYSETKRR NVFRLTTSDC
     ECLFQAEDRD DMLSWIKTIQ ESSNLNEEDT GVTNRDLISR RIKEYNSLLS KTEQLPKTPR
     QSLSIRQTLL GAKSEPKTQS PHSPKEESER KLLSKDDTSP PKDKGTWRRG IPSIVRKTFE
     KKPAATGTFG VRLDDCPPAH TNRYIPLIVD ICCKLVEERG LEYTGIYRVP GNNAAISSMQ
     EELNKGMADI DIQDDKWRDL NVISSLLKSF FRKLPEPLFT NDKYADFIEA NRKEDPLDRL
     RTLKRLIHDL PEHHFETLKF LSAHLKTVAE NSEKNKMEPR NLAIVFGPTL VRTSEDNMTH
     MVTHMPDQYK IVETLIQHHD WFFTEEGAEE PLTAVQEENT VDSQPVPNID HLLTNIGRTG
     VLPGDVSDSA TSDSAKSKGS WGSGKDQYSR ELLVSSIFAA ASRKRKKPKE KAQPSSSEDE
     LDSVFFKKEN TEQSHSEIKE ESKRESETSG SKQRVVVAKE SNTKKDSGTT KEEKKIPWEE
     PSPPHSSKRN RSPTLSCRLA MLKEGPRSLL TQKPHCEETG SDSGTLLSTS SQASLLRSST
     KKSTSPETKH SEFLSIAGTT TSDYSTTSST TYLTSLDSSR LSPEVQSVAE SKGDEADDER
     SELVSEGRPV ETDSESEFPV FPTTLTSDRL FRGKFQEVAR VSRRNSEGSE ASCTEGSLTP
     SLDSRRQQFS SHRLIECDTL SRKKSARFKS DSGSPGDTRT EKETPALAKM FDVMKKGKST
     GSLLTPSRSE SEKQEATWKT KIADRLKLRP RAPADDMFGV GNQKPTAETA KRKNIKRRHT
     LGGHRDATEI SVLSFWKAHE QSADKESELS AVNRLKPKCS AQDLSISDWL ARERVRTSAS
     DLSRGEGLEP QAESPSVLGT PISTHSPPSQ QPEARVAATS TLASTSQSPL FTPPQSPDQI
     NRESFQNMSQ NASSTANIHP HKQSESPDTK AETPP
//
ID   B7ZCU0_MOUSE            Unreviewed;       480 AA.
AC   B7ZCU0;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 17.
DE   SubName: Full=Abl-interactor 1;
GN   Name=Abi1; ORFNames=RP23-436J19.3-005;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Phillimore B.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Almeida-King J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; AL845257; CAX15302.1; -; Genomic_DNA.
DR   EMBL; CT030013; CAX15302.1; JOINED; Genomic_DNA.
DR   EMBL; CT030013; CAX15873.1; -; Genomic_DNA.
DR   EMBL; AL845257; CAX15873.1; JOINED; Genomic_DNA.
DR   IPI; IPI00918951; -.
DR   UniGene; Mm.205647; -.
DR   UniGene; Mm.249752; -.
DR   Ensembl; ENSMUST00000091394; ENSMUSP00000088957; ENSMUSG00000058835.
DR   MGI; MGI:104913; Abi1.
DR   HOVERGEN; HBG050446; -.
DR   Bgee; B7ZCU0; -.
DR   Genevestigator; B7ZCU0; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0030296; F:protein tyrosine kinase activator activity; IDA:MGI.
DR   GO; GO:0009987; P:cellular process; IDA:MGI.
DR   GO; GO:0001756; P:somitogenesis; IMP:MGI.
DR   InterPro; IPR012849; Abl-interactor_HHR_dom.
DR   InterPro; IPR000108; p67phox.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   Pfam; PF07815; Abi_HHR; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00499; P67PHOX.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   4: Predicted;
KW   SH3 domain.
SQ   SEQUENCE   480 AA;  52216 MW;  F78D5AD705520B2A CRC64;
     MAELQMLLEE EIPSGKRALI ESYQNLTRVA DYCENNYIQA TDKRKALEET KAYTTQSLAS
     VAYQINALAN NVLQLLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR
     THKIIAPANM ERPVRYIRKP IDYTVLDDVG HGVKWLKAKH GNNQPARTGT LSRTNPPTQK
     PPSPPVSGRG TLGRNTPYKT LEPVKPPTVP NDYMTSPARL GSQHSPGRTA SLNQRPRTHS
     GSSGGSGSRE NSGSSSIGIP IAVPTPSPPT AGPAPGAAPG SQYGTMTRQI SRHNSTTSST
     SSGGYRRTPS VAAQFSAQPH VNGGPLYSQN SISVAPPPPP MPQLTPQIPL TGFVARVQEN
     IADSPTPPPP PPPDDIPMFD DSPPPPPPPP VDYEDEEAAV VQYSDPYADG DPAWAPKNYI
     EKVVAIYDYT KDKDDELSFK EGAIIYVIKK NDDGWFEGVC NRVTGLFPGN YVESIMHYTD
//
ID   B7ZD29_MOUSE            Unreviewed;      1154 AA.
AC   B7ZD29;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   11-JAN-2011, entry version 20.
DE   SubName: Full=Disabled homolog 2 (Drosophila) interacting protein;
GN   Name=Dab2ip; ORFNames=RP23-4L24.1-009;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Almeida-King J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 PH domain.
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DR   EMBL; AL929241; CAX15341.1; -; Genomic_DNA.
DR   IPI; IPI00928038; -.
DR   Ensembl; ENSMUST00000135741; ENSMUSP00000122341; ENSMUSG00000026883.
DR   MGI; MGI:1916851; Dab2ip.
DR   HOVERGEN; HBG006492; -.
DR   Bgee; B7ZD29; -.
DR   Genevestigator; B7ZD29; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR021887; DUF3498.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001936; RasGAP.
DR   InterPro; IPR023152; RasGAP_CS.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.10.506.10; RasGAP; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF12004; DUF3498; 1.
DR   Pfam; PF00616; RasGAP; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00323; RasGAP; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE   4: Predicted;
KW   GTPase activation.
SQ   SEQUENCE   1154 AA;  127312 MW;  264FB2AA66FF3D7A CRC64;
     MSEKNPSMEP SASTPFRVTG FLSRRLKGSI KRTKSQPKLD RNHSFRHILP GFRSAAAAAA
     DNERSHLMPR LKESRSHESL LSPSSAVEAL DLSMEEEVII KPVHSSILGQ DYCFEVTTSS
     GSKCFSCRSA AERDKWMENL RRAVHPNKDN SRRVEHILKL WVIEAKDLPA KKKYLCELCL
     DDVLYARTTS KLKTDNVFWG EHFEFHNLPP LRTVTVHLYR ETDKKKKKER NSYLGLVSLP
     AASVAGRQFV EKWYPVVTPN PKGGKGPGPM IRIKARYQTV SILPMEMYKE FAEHITNHYL
     GLCAALEPIL SAKTKEEMAS ALVHILQSTG KVKDFLTDLM MSEVDRCGDN EHLIFRENTL
     ATKAIEEYLK LVGQKYLQDA LGEFIKALYE SDENCEVDPS KCSSADLPEH QGNLKMCCEL
     AFCKIINSYC VFPRELKEVF ASWRQECSSR GRPDISERLI SASLFLRFLC PAIMSPSLFN
     LLQEYPDDRT ARTLTLIAKV TQNLANFAKF GSKEEYMSFM NQFLEHEWTN MQRFLLEISN
     PETLSNTAGF EGYIDLGREL SSLHSLLWEA VSQLDQSVVS KLGPLPRILR DVHTALSTPG
     SGQLPGTNDL ASTPGSGSSS VSAGLQKMVI ENDLSGLIDF TRLPSPTPEN KDLFFVTRSS
     GVQPSPARSS SYSEANEPDL QMANGSKSLS MVDLQDARTL DGEAGSPVGP DALPADGQVP
     ATQLLAGWPA RAAPVSLAGL ATVRRAVPTP TTPGTSEGAP GRPQLLAPLS FQNPVYQMAA
     GLPLSPRGLG DSGSEGHSSL SSHSNSEELA AAAKLGSFST AAEELARRPG ELARRQMSLT
     EKGGQPTVPR QNSAGPQRRI DQPPPPPPPP PPAPRGRTPP TLLSTLQYPR PSSGTLASAS
     PDWAGPGTRL RQQSSSSKGD SPELKPRAMH KQGPSPVSPN ALDRTAAWLL TMNAQLLEDE
     GLGPDPPHRD RLRSKEELSQ AEKDLAVLQD KLRISTKKLE EYETLFKCQE ETTQKLVLEY
     QARLEEGEER LRRQQEDKDI QMKGIISRLM SVEEELKKDH AEMQAAVDSK QKIIDAQEKR
     IASLDAANAR LMSALTQLKE SNGLGRLSSA YSKGWSCQRP CSGKTLATDT QDLMERAAPP
     LPTQTPDLFV QLVC
//
ID   B7ZMP8_MOUSE            Unreviewed;       279 AA.
AC   B7ZMP8;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   11-JAN-2011, entry version 18.
DE   SubName: Full=2310046A06Rik protein;
GN   Name=2310046A06Rik;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC144730; AAI44731.1; -; mRNA.
DR   IPI; IPI00850743; -.
DR   UniGene; Mm.35008; -.
DR   Ensembl; ENSMUST00000093816; ENSMUSP00000091334; ENSMUSG00000032355.
DR   MGI; MGI:1916892; 2310046A06Rik.
DR   HOVERGEN; HBG055766; -.
DR   Bgee; B7ZMP8; -.
DR   Genevestigator; B7ZMP8; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   279 AA;  30814 MW;  211A5DFE7995B2E8 CRC64;
     MEFGKHEPGS SLKRNKNLEE GVTVSPGDPE AKPLIFTFVP TLRRLPTHIQ LADTSKFLVK
     IPEEPTDKSP ETVNRFEYSD HMTFSSESKQ ERVQRILDYP SEVSGRNSQQ KEFNTKEPQG
     MQKGDLFKAE YVFIVDSDGE DEATCRQGEQ GPPGGPGNIA TRPKSLAISS SLASDVVRPK
     VRGADLKTSS HPEIPHGIAP QQKHGLTPTT HPRAAGRETK YANLSSSSST ASESQLTKPG
     VIRPVPVKSK LLLRKDEEVY EPNPFSKYLE DNSGLFSEQ
//
ID   B7ZN48_MOUSE            Unreviewed;       999 AA.
AC   B7ZN48;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 16.
DE   SubName: Full=Stxbp5l protein;
GN   Name=Stxbp5l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC145007; AAI45008.1; -; mRNA.
DR   IPI; IPI00656258; -.
DR   UniGene; Mm.403226; -.
DR   UniGene; Mm.80170; -.
DR   HOVERGEN; HBG083064; -.
DR   Genevestigator; B7ZN48; -.
DR   InterPro; IPR000664; Lethal2_giant.
DR   InterPro; IPR013577; LLGL2.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 3.
DR   Pfam; PF08366; LLGL; 1.
DR   Pfam; PF00400; WD40; 3.
DR   PRINTS; PR00962; LETHAL2GIANT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 3.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Repeat; WD repeat.
SQ   SEQUENCE   999 AA;  111778 MW;  767B305063A63DE2 CRC64;
     MKKFNFRKVL DGLTASSPGS GSSSGSNSGG AGSGSVHPGG TAGLPREEIQ ESLTSDYFQI
     CKTVRHGFPY QPTALAFDPV QKILAIGTRT GAIRILGRPG VDCYCQHESG AAVLQLQFLI
     NEGALVSASS DDTLHLWNLR QKRPAILHSL KFNRERITYC HLPFQSKWLY VGTERGNTHI
     VNIESFILSG YVIMWNKAIE LSTKTHPGPV VHLSDSPRDE GKLLIGYENG TVVFWDLKSK
     RAELRVYYDE AIHSIDWHHE GKQFMCSHSD GSLTLWNLKS PSRPFQTTVP HGKSQREGRK
     SESCKPILKV EYKTCRNSEP FIIFSGGLSY DKACRRPSLT IMHGKAITVL EMDHPIVEFL
     TLCETPYPNE FQEPYAVAVL LEKDLIVVDL TQTNFPIFEN PYPMDIHESP VTCTAYFADC
     PPDLILVLYS IGVKHKKQGY SNKEWPVSGG AWNLGAQTYP EIIITGHADG TIKFWDASAM
     TLQMLYKLKT SKVFEKQKAG EGKQTCELVE EDPFAVQMIY WCPESRIFCV SGVSAYVIIY
     KFSRHEVTTE IVSLEVRLQC DVEDIITPEP ETSPPFPDLS SQLPPSRSLS GSTNTVSSEG
     VTKDSIPCLS VKTRPVRMPP GYQADLVIQL VWVDGEPPQQ ITSLSISSAY GIVAFGNCTG
     LVVVDFIQKT VLLSMGTIDL YRSSDLYQRQ PRSPRKNRQF IADNFCMRGL SNFYPDLTKR
     IRTSYQSLTE LNDSPVPLEL ERCKSPTSGL ATRTPEAAPG FYRNEMPAVK QRSQVHHLPE
     TRENSYNRSR SSSISSIDKD SKEAITALYF MESFARKNDS TVSPCLFVGT SLGMVVLISL
     NLPSSDEQRF TEPVVVLPSG TFLSLKGAVL TFSCMDRTGS LMQPPYEVWR DPNNTDENEK
     TWKRKLVMNY LSSSQEMGDH QYTIICSEKQ AKVFSLPSQT CLYVHNITET SFILQADVVV
     MCNSACLACF CANGHIMIMR YMVYLLLTDN HNNASKVKW
//
ID   B7ZN50_MOUSE            Unreviewed;      1032 AA.
AC   B7ZN50;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 16.
DE   SubName: Full=Stxbp5l protein;
GN   Name=Stxbp5l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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CC   -----------------------------------------------------------------------
DR   EMBL; BC145009; AAI45010.1; -; mRNA.
DR   IPI; IPI00555114; -.
DR   UniGene; Mm.403226; -.
DR   UniGene; Mm.80170; -.
DR   HOVERGEN; HBG083064; -.
DR   Genevestigator; B7ZN50; -.
DR   InterPro; IPR000664; Lethal2_giant.
DR   InterPro; IPR013577; LLGL2.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 3.
DR   Pfam; PF08366; LLGL; 1.
DR   Pfam; PF00400; WD40; 3.
DR   PRINTS; PR00962; LETHAL2GIANT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 3.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Repeat; WD repeat.
SQ   SEQUENCE   1032 AA;  114879 MW;  CD0C5C7AD0B8DA10 CRC64;
     MKKFNFRKVL DGLTASSPGS GSSSGSNSGG AGSGSVHPGG TAGLPREEIQ ESLTSDYFQI
     CKTVRHGFPY QPTALAFDPV QKILAIGTRT GAIRILGRPG VDCYCQHESG AAVLQLQFLI
     NEGALVSASS DDTLHLWNLR QKRPAILHSL KFNRERITYC HLPFQSKWLY VGTERGNTHI
     VNIESFILSG YVIMWNKAIE LSTKTHPGPV VHLSDSPRDE GKLLIGYENG TVVFWDLKSK
     RAELRVYYDE AIHSIDWHHE GKQFMCSHSD GSLTLWNLKS PSRPFQTTVP HGKSQREGRK
     SESCKPILKV EYKTCRNSEP FIIFSGGLSY DKACRRPSLT IMHGKAITVL EMDHPIVEFL
     TLCETPYPNE FQEPYAVAVL LEKDLIVVDL TQTNFPIFEN PYPMDIHESP VTCTAYFADC
     PPDLILVLYS IGVKHKKQGY SNKEWPVSGG AWNLGAQTYP EIIITGHADG TIKFWDASAM
     TLQMLYKLKT SKVFEKQKAG EGKQTCELVE EDPFAVQMIY WCPESRIFCV SGVSAYVIIY
     KFSRHEVTTE IVSLEVRLQC DVEDIITPEP ETSPPFPDLS SQLPPSRSLS GSTNTVSSEG
     VTKDSIPCLS VKTRPVRMPP GYQADLVIQL VWVDGEPPQQ ITSLSISSAY GIVAFGNCTG
     LVVVDFIQKT VLLSMGTIDL YRSSDLYQRQ PRSPRKNRQF IAGLTELNDS PVPLELERCK
     SPTSGLATRT PEAAPGFYRN EMPAVKQRSQ VHHLPDHVNG HCTSPTSQSC SSGKRLSSAD
     VSKVNRWGPG RPPFRKAQSA ACMEISLPVT TEETRENSYN RSRSSSISSI DKDSKEAITA
     LYFMESFARK NDSTVSPCLF VGTSLGMVVL ISLNLPSSDE QRFTEPVVVL PSGTFLSLKG
     AVLTFSCMDR TGSLMQPPYE VWRDPNNTDE NEKTWKRKLV MNYLSSSQEM GDHQYTIICS
     EKQAKVFSLP SQTCLYVHNI TETSFILQAD VVVMCNSACL ACFCANGHIM IMRYMVYLLL
     TDNHNNASKV KW
//
ID   B7ZNA3_MOUSE            Unreviewed;      2082 AA.
AC   B7ZNA3;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   11-JAN-2011, entry version 15.
DE   SubName: Full=Garnl1 protein;
GN   Name=Ralgapa1; Synonyms=Garnl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC145119; AAI45120.1; -; mRNA.
DR   EMBL; BC150707; AAI50708.1; -; mRNA.
DR   IPI; IPI00460042; -.
DR   UniGene; Mm.292180; -.
DR   HOVERGEN; HBG051842; -.
DR   Genevestigator; B7ZNA3; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR000331; Rap_GAP.
DR   Pfam; PF02145; Rap_GAP; 1.
DR   PROSITE; PS50085; RAPGAP; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   2082 AA;  234381 MW;  90B5373764C36828 CRC64;
     MFSKKPHGDV KKSTQKVLDT KKDALTRLKH LRIVIENAES IDLKQFFDQH FSHIYYVFFE
     NFVTIEASLK QKGHKSQREE LDAILFIFEK ILQLLPERIH QRWQFHSIGL ILKKLLHTGN
     SLKIRREGVR LFLLWLQALQ DNCSKEQLWM FSCLIPGFSA PQSEYGPRTL DNLINPPLSL
     QETQVTIEEV TPLVPPQSGD KGQEDLTSYF LEALLKYIVI QVKSLEWKNK ENQERGFSFL
     FSHFKKFYLP YIFPNICKEN SLYHPVLDIP QIRPKPHYVM IKKDAETNET IYCTKEPFIQ
     ARVIVIRWLV SFWLEPKPHS GPNIPGMEGE VLPKNIQRAA ASLVSREESK NDTVDKVDKS
     AEPEQSHSNT STLTEREPSS SSLCSIDEEH LTDIEIVRRV FSSKRSNVNF VTEIFRQAFL
     LPICEAAAMR KVVKVYQEWI QQEEKPLFMQ EPEDTAITCS DIPCSETVAD HDSAIEDGEK
     REEENGTSTS EHVRNSSWTK NGSYQEAFHV CEEATEQNIQ AGTQAVLQVF IINSSNIFLL
     EPANEIKNLL DEHTDMCKRI LNIYRYMVVQ VSMDKKTWEQ MLLVLLRVTE SVLKMSSQAF
     LQFQGKKSMT LAGRLAGPLF QTLIVAWIKA NLNVYISREL WDDLLSVLSS LTYWEELATE
     WSLTMETLTK VLARNLYSLD LSDLPLDKLS EQKQKKHKGK GVGHEFQKVS VDKSFSRGWS
     RDQPGQAPMR QRSATTTGSP GTEKARSIVR QKTVAMRSRS IGECALPSAY IRSAKSAPVL
     IHTSKPFLPD IVLTPLSDEL SDIDDAQILP RSTRVRHFSQ SEDTGNEVFG ALHEEQPLPR
     SSSTSDILEP FTVERAKVNK EDTSPKLPPL NSETGGNSAN VPDLMDEFIA ERLRSGNAST
     MTRRGSSPGS LEIPKDLPDI LNKQNQMRPV DDPGVPSEWT SPASAGSSDL MSSDSHSDSF
     SAFQCEGRKF DNFGFGTDIG IPSSADVDLG SGHHQSTEEQ EVASLTTLHL DSETSSLNQQ
     AFSAEVATVT GSESASPVHS ALGSRSQTPS PSTLSRAHIE QKDLQLDEKL HHSVLQTPDD
     LEISEFPSEC CSVMAGGTLT GWHADVATVM WRRMLGILGD VNAIMDPEIH AQVFDYLCEL
     WQNLAKIRDN LGISADNLTS PSPPVLIPPL RILTPWLFKA AMLTDKYKQG KLHAYKLICN
     TMKRRQDVSP NRDFLTHFYN IMHCGLLHID QDIVNTIIKH CSPQFFSLGL PGATMLIMDF
     IIAAGRVASS AFLNAPRVEA QVLLGSLVCF PNLYCELPAL HPNIPDIAVS QFTDVKELII
     KTVLSSARDE PSGPARCVAL CSLGIWICEE LVHESHHPQI KEALNVICVS LKFTNKTVAH
     VACNMLHMLV HYVPRLQIHQ PQSPLKIIQI LIATITHLLP STEASSYEMD KRLVVSLLLC
     LLDWIMALPL KTLLQPVHAT GAENDKTEKS VLNCIYKVLH GCVYGAQSFS NPKYFPISLS
     DLASVDYDPF MHLESLKEPE PLHSPDSERS SKLQPVTEVK TQMQQGLISI AARTVITHLV
     NHLGHYPMSG GPAMLTSQVC ENHDNHYSES TELSPELFES PNIQFFVLNN TTLVSCIQIR
     SEESMPGGGL AAGLVSANSN VRIIVRDLSG KYSWDSAILY GPPIVSGLPE PTSFILSMSD
     QEKPEEPPTS NECLEDIAVK DGLSLQLRRF RETVPTWSTI REEEDVLDEL LQYLGTTSPE
     CLQRTGISLN VPAPQPLCIS EKQENDVINA ILKQYTEEKE FVEKHFNDLN MKASEQDEPT
     PQKPQSAFYY CRLLLSILGM NSWDKRRSFH LLKKNEKLLR ELRNLDSRQC RETHKIAVFY
     VAEGQEDKYS ILTNIGGSQA YEDFVAGLGW EVNLTNHCGF MGGLQKNRST GLTTPYFATS
     TVEVIFHVST RMPSDSDDSL TKKLRHLGND EVHIVWSEHT RDYRRGIIPT EFGDVLIVIY
     PMKNHMFSIQ IMKKPEVPFF GPLFDGAIVN GKVLPIMVRS TAINASRALK SLIPLYQNFY
     EERARYLQTI VQHHLEPTTF EDFAAQVFSP APYHHFPADA DH
//
ID   B7ZNA5_MOUSE            Unreviewed;       951 AA.
AC   B7ZNA5;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   11-JAN-2011, entry version 15.
DE   SubName: Full=Phc3 protein;
GN   Name=Phc3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC145123; AAI45124.1; -; mRNA.
DR   IPI; IPI00857303; -.
DR   RefSeq; NP_001159428.1; NM_001165956.1.
DR   UniGene; Mm.233173; -.
DR   GeneID; 241915; -.
DR   KEGG; mmu:241915; -.
DR   CTD; 241915; -.
DR   MGI; MGI:2181434; Phc3.
DR   HOVERGEN; HBG106650; -.
DR   Genevestigator; B7ZNA5; -.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   InterPro; IPR012313; Znf_FCS.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
DR   PROSITE; PS51024; ZF_FCS; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   951 AA;  102436 MW;  92E2B0E1BB6C7F05 CRC64;
     MAEAEFKDHS TAMDSEPSSG TSVSTTASST TTTTITTSSS RMQQPQISVY SGSDRHAVQV
     IQQALHRPPS SAAQYLQQMY AAQQQHLMLH TAALQQQHLS SSQLQSLAAV QASLSSGRPS
     TSPTGSVTQQ SSMSQTSILS ASPAPAQLMN RSQTSSSTSG SITQQTMLLG STSPTLTASQ
     AQMYLRAQML IFTPATTVAA VQSDIPVVSS SPSPSCQSAA AQVQNLTLRS QKLGVLSSSQ
     NGSPKSAGQT QSLTICHNKT TVTSSKISQR DPSPESKKGG SPGLESRSTA VTRTSSIHQL
     IAPASYSPIQ PHSLIKHQQI PLHSPPPKVS HHQLLLQQQQ QQIQPITLQS PSQDPPPSQH
     CIPLPNHGLS PAPSNAQPQH CSPVQSHPPP LTVSPNQAQS AQQSVVVSPP PPHSPSQSPT
     IIIHPQALIQ PHPLVSSALQ TGPNLQQMVS PTSHQQYSAL QSSPIPIATP PQMSASPPAQ
     LPPLPLQSMQ SLQVQPEILS QGQVLVQNAL VSEEELPAAE ALVQLPFQTL PPPQTVAVNL
     QVQPPAPVDP PVVYQVEDVC EEEMPEESDE CARMDRTPPP PTLSPAAVTV GRGEDLTSEH
     PLLEQVELPA VASVSASVIK SPSDPTHASA PAPPLLIPAA STRSSSTSLA SSTPSLENKP
     PQAIVKPQIL THVIEGFVIQ EGLEPFPVSR SSLLIEQPVK KRPLLDNQVV NSVCVQPELQ
     NNTKHADNSS DTEIEDMMAE ETLEEMDSEL LKCEFCGKMG YPNEFLRSKR FCTMSCAKRY
     NVSCSKKFAL SRWNRKPDNQ SLGHRGRRPS GPEGAAREHI LRQLPITYPS AEEDVASHED
     PVPSAMTTRL RRQSERERER ELRDVRIRKM PENSDLLPVA QTEPSIWTVD DVWAFIHSLP
     GCQDVADEFR AQEIDGQALL LLKEDHLMSA MNMKLGPALK ICARINSLKD S
//
ID   B7ZNC5_MOUSE            Unreviewed;       376 AA.
AC   B7ZNC5;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   05-OCT-2010, entry version 11.
DE   SubName: Full=Sfrs11 protein;
GN   Name=Srsf11; Synonyms=Sfrs11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; BC145162; AAI45163.1; -; mRNA.
DR   IPI; IPI00923001; -.
DR   UniGene; Mm.223946; -.
DR   Ensembl; ENSMUST00000069025; ENSMUSP00000063916; ENSMUSG00000090195.
DR   MGI; MGI:1916457; Srsf11.
DR   HOVERGEN; HBG058422; -.
DR   Bgee; B7ZNC5; -.
DR   Genevestigator; B7ZNC5; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   376 AA;  42708 MW;  A2209588EFA93EDE CRC64;
     MINNHRDQTL YFSEHKYFQQ TQVVYQGDIF WVFLCVFCLQ RECVLMQGCF SAGVIPDETK
     ALSLLAPANA VAGLLPGGGL LPTPNPLTQI GAVPLAALGA PALDPALAAL GLPGTNLNSQ
     SLAADQLLKL MSTVDPKLNH VAAGLVSPSL KSDTSSKEIE EAMKRVREAQ SLISAAIEPD
     KKEEKRRHSR SRSRSRRRRT PSSSRHRRSR SRSRRRSHSK SRSRRRSKSP RRRRSHSRER
     GRRSRSTSKA RDKKKEDKEK KRSKTPPKSY STARRSRSAS RDERERSTSK KKRSKDKEKE
     RERKSESDKD VKQVTRDYDE EEQGYDSEKE KKEEKRPTEA VSPKTKECSV EKGVGDLRES
     KVNGDDHHEE DMDMSD
//
ID   B7ZNJ3_MOUSE            Unreviewed;      1360 AA.
AC   B7ZNJ3;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   11-JAN-2011, entry version 18.
DE   SubName: Full=Caskin1 protein;
GN   Name=Caskin1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC138443; AAI38444.1; -; mRNA.
DR   EMBL; BC145281; AAI45282.1; -; mRNA.
DR   IPI; IPI00553792; -.
DR   UniGene; Mm.480045; -.
DR   Ensembl; ENSMUST00000115347; ENSMUSP00000111004; ENSMUSG00000033597.
DR   MGI; MGI:2442952; Caskin1.
DR   HOVERGEN; HBG051133; -.
DR   Bgee; B7ZNJ3; -.
DR   Genevestigator; B7ZNJ3; -.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF00023; Ank; 4.
DR   Pfam; PF00536; SAM_1; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 6.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   ANK repeat; Repeat.
SQ   SEQUENCE   1360 AA;  142676 MW;  D79698466250FD9C CRC64;
     MGKEQELVQA VKAEDVGTAQ RLLQRPRPGK AKLLGSTKKI NVNFQDPDGF SALHHAALNG
     NTELISLLLE AQAAVDIKDN KGMRPLHYAA WQGRKEPMKL VLKAGSAVNV PSDEGHIPLH
     LAAQHGHYDV SEMLLQHQSN PCMVDNSGKT PLDLACEFGR VGVVQLLLSS NMCAALLEPR
     PGDTTDPNGT SPLHLAAKNG HIDIIRLLLQ AGIDINRQTK SGTALHEAAL CGKTEVVRLL
     LDSGINAQVR NTYSQTALDI VHQFTTSQAS KEIKQLLREA SAALQVRATK DYCNNYDLTS
     LNVKAGDIIT VLEQHPDGRW KGCIHDNRTG NDRVGYFPSS LGEAIVKRAG SRTGSEPSPP
     QGGGSLGPSA PPEEIWVLRK PFAGGDRSGS LSNVAGGRST GGHALHAGSE GVKLLATVLS
     QKSVSESSPG DSPVKPPEGS SGAARSQPPA AHAGQVYGEQ PPKKLESASA SASEGKANLA
     VWLSMIGLAQ YYKVLVDNGY ENIDFITDIT WEDLQEIGIT KLGHQKKLML AVRKLAELQK
     AEYSKYEGGP LRRKTPQSLE MMAIESPPPS EPAAAECQSP KMTTFQDSEL SGELQAALSG
     PAEAGAAAVE KSSNHLPPTP RTTSRESSLS GRARHISSSQ ELLGDGPPGP GSPMSRSQEY
     LLDEGMAPGT PPKEVRSSRH GHSVKRASVP PVPGKPRQVL PSGASHFTPP QTPTKAQPGS
     PQALGGPHGP ATAKVKPTPQ LLPPTDRPMS PRSLPQSPTH RGFAYVLPQP VEGEVGPPAP
     GPAPPPVPAA VPTLCLPPET DVEPGRPKKR AHSLNRYAAS DSEPERDELL VPAAAGPYAT
     VQRRVGRSHS VRAPAGTDKN VNRSQSFAVR PRKKGPPPPP PKRSSSAMAS ANLADEPAPD
     VEAEDGRLGV RAQRRRASDL AGSVDTGSAG SVKSIAAMLE LSSIGGGGRA IRRPPEGHPT
     PRPASPEPGR VATVLASVKH KEAIGPDGEV VNRRRTLSGP VTGLLATARR GSGEPAEQSH
     FMEDGTARQR LRGPAKGEAS AEGPPLARVE ASATLKRRIR AKQSQQENVK FILTESDTVK
     RRPKAKEPDT GPEPPPPLSV YQNGTATVRR RPTSEQAGPP ELPPPPPPAE PPPADLMQLP
     PLPLPDGNAR KPVKPPVSPK PILAQPVSKI QGSPTPASKK VPLPGPGSPE VKRAHGTPPP
     VSPKPPPPPT APKPAKALAG LQSSSATPSP VPSPARQPPA ALIKPASSPP SQSASPVKPP
     SPGTPALHVP AKPPRAAASV VSGPPVASDC ASPGDSARQK LEETSACLAA ALQAVEEKIR
     QEDGQGPRPS SIEEKSTGSI LEDIGSMFDD LADQLDAMLE
//
ID   B7ZNK9_MOUSE            Unreviewed;       893 AA.
AC   B7ZNK9;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 15.
DE   SubName: Full=Spata5 protein;
GN   Name=Spata5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
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DR   EMBL; BC145302; AAI45303.1; -; mRNA.
DR   IPI; IPI00111113; -.
DR   UniGene; Mm.172679; -.
DR   Ensembl; ENSMUST00000108112; ENSMUSP00000103747; ENSMUSG00000027722.
DR   MGI; MGI:1927170; Spata5.
DR   HOVERGEN; HBG108504; -.
DR   Bgee; B7ZNK9; -.
DR   Genevestigator; B7ZNK9; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   InterPro; IPR009010; Asp_de-COase-like_fold.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   Gene3D; G3DSA:2.40.40.20; Asp_decarboxylase-like_fold; 1.
DR   Pfam; PF00004; AAA; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF50692; Asp_decarb_fold; 1.
DR   PROSITE; PS00674; AAA; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding.
SQ   SEQUENCE   893 AA;  97268 MW;  F011B0FB02800754 CRC64;
     MSSKKNRKRQ KEGAEGASPS LSAAPSRSGT STPFAQPSPA APGMLVVTNF LEKVDGKVPK
     TFQNSLVHLG LNTMKSANIC IGRPVLLTSL DGKQEVYTAW PVAGFPGGKV GLSEMAQKNV
     GVRAGETIQV QPLLGAVLQA QEMDLALSDK DKEINEEELT GCILRKLDGK IVLPGNFLYC
     TFYGRLCKLQ VLQVKGTDGT TLGKPQSASG TDAQGMASEH SSMENSDVDL SFQLSQLDLK
     EPQSPSSQST PCKPTNDRTV NKAGEVLLDV TQSPRDGSGL GLEESTGLKC SFDSSKEGNT
     QPVSEEKLLK PASAGTKSNT DTFYFISSTT RINLRKICTN SKEQDSQFKV TYDMIGGLNS
     QLKAIREIIE LPLKQPELFK SYGIPAPRGL LLYGPPGTGK TMIARAVANE VGAYVSVING
     PEIISKFYGE TEARLRQIFA EATLRHPSII FIDELDALCP KREGAQSEVE KRVVASLLTL
     MDGIGSEGSE GRVLVLGATN RPQALDAALR RPGRFDKEIE IGIPNAQDRL DILQKLLRRV
     PHLLTKAELL RLANNAHGYV GADLKALCNE AGLHALRRVL RKQPNLPDSK VAGMVKITLN
     DFLQGMNDIR PSAMREVAID VPNVSWSDIG GLENIKLKLK QAVEWPLKHP KSFNRMGIQP
     PKGVLLYGPP GCSKTMIAKA LANESGLNFL AIKGPELMNK YVGESERAVR EIFRKARAVA
     PSIIFFDELD ALAVERGSSS GAGNVADRVL AQLLTEMDGI EQLKNVTVLA ATNRPDRIDK
     ALMRPGRIDR IIYVPLPDAA TRREILNLQF HSMPISNEVD LDELVLQTDT YSGAEIIAVC
     KEAALLALEE NIKADCIMKR HFTEALSIVT PRIPESLRRF YEDYQEKSGL HTV
//
ID   B7ZNR8_MOUSE            Unreviewed;      1288 AA.
AC   B7ZNR8;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 15.
DE   SubName: Full=Map4k4 protein;
GN   Name=Map4k4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC145390; AAI45391.1; -; mRNA.
DR   IPI; IPI00923108; -.
DR   UniGene; Mm.19073; -.
DR   HOVERGEN; HBG036506; -.
DR   Genevestigator; B7ZNR8; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0005083; F:small GTPase regulator activity; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR001180; Citron.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding.
SQ   SEQUENCE   1288 AA;  146730 MW;  D63FC51A41EA6399 CRC64;
     MANDSPAKSL VDIDLSSLRD PAGIFELVEV VGNGTYGQVY KGRHVKTGQL AAIKVMDVTE
     DEEEEIKLEI NMLKKYSHHR NIATYYGAFI KKSPPGHDDQ LWLVMEFCGA GSITDLVKNT
     KGNTLKEDWI AYISREILRG LAHLHIHHVI HRDIKGQNVL LTENAEVKLV DFGVSAQLDR
     TVGRRNTFIG TPYWMAPEVI ACDENPDATY DYRSDLWSCG ITAIEMAEGA PPLCDMHPMR
     ALFLIPRNPP PRLKSKKWSK KFFSFIEGCL VKNYMQRPST EQLLKHPFIR DQPNERQVRI
     QLKDHIDRTR KKRGEKDETE YEYSGSEEEE EEVPEQEGEP SSIVNVPGES TLRRDFLRLQ
     QENKERSEAL RRQQLLQEQQ LREQEEYKRQ LLAERQKRIE QQKEQRRRLE EQQRREREAR
     RQQEREQRRR EQEEKRRLEE LERRRKEEEE RRRAEEEKRR VEREQEYIRR QLEEEQRHLE
     ILQQQLLQEQ AMLLHDHRRP HAQQQPPPPQ QQERSKPSFH APEPKPHYDP ADRAREVEDR
     FRKTNHSSPE AQAKQTGRGL EPPVPSRSES FSNGNSESVH PALQRPAEPQ VQWSHLASLK
     NNVSPVSRSH SFSDPSPKFA HHHLRSQDPC PPSRSEGLSQ SSDSKSEVPE PTQKAWSRSD
     SDEVPPRVPV RTTSRSPVLS RRDSPLQGGG QQNSQAGQRN STSSIEPRLL WERVEKLVPR
     PGSGSSSGSS NSGSQPGSHP GSQSGSGERF RVRSSSKSEG SPSPRQESAA KKPDDKKEVF
     RPLKPAGEVD LTALAKELRA VEDVRPPHKV TDYSSSSEES GTTDEEEEDV EQEGADDSTS
     GPEDTRAASS PNLSNGETES VKTMIVHDDV ESEPAMTPSK EGTLIVRQTQ SASSTLQKHK
     SSSSFTPFID PRLLQISPSS GTTVTSVVGF SCDGLRPEAI RQDPTRKGSV VNVNPTNTRP
     QSDTPEIRKY KKRFNSEILC AALWGVNLLV GTESGLMLLD RSGQGKVYPL ISRRRFQQMD
     VLEGLNVLVT ISGKKDKLRV YYLSWLRNKI LHNDPEVEKK QGWTTVGDLE GCVHYKVVKY
     ERIKFLVIAL KSSVEVYAWA PKPYHKFMAF KSFGELLHKP LLVDLTVEEG QRLKVIYGSC
     AGFHAVDVDS GSVYDIYLPT HIQCSIKPHA IIILPNTDGM ELLVCYEDEG VYVNTYGRIT
     KDVVLQWGEM PTSVAYIRSN QTMGWGEKAI EIRSVETGHL DGVFMHKRAQ RLKFLCERND
     KVFFASVRSG GSSQVYFMTL GRTSLLSW
//
ID   B7ZW98_MOUSE            Unreviewed;      1852 AA.
AC   B7ZW98;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 17.
DE   SubName: Full=Ank1 protein;
GN   Name=Ank1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; BC138029; AAI38030.1; -; mRNA.
DR   EMBL; BC171944; AAI71944.1; -; mRNA.
DR   IPI; IPI00119871; -.
DR   UniGene; Mm.334444; -.
DR   UniGene; Mm.476804; -.
DR   Ensembl; ENSMUST00000084038; ENSMUSP00000081051; ENSMUSG00000031543.
DR   MGI; MGI:88024; Ank1.
DR   HOVERGEN; HBG004234; -.
DR   Bgee; B7ZW98; -.
DR   Genevestigator; B7ZW98; -.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0048821; P:erythrocyte development; IMP:MGI.
DR   GO; GO:0015672; P:monovalent inorganic cation transport; IMP:MGI.
DR   GO; GO:0006779; P:porphyrin biosynthetic process; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR000488; Death.
DR   InterPro; IPR011029; DEATH-like.
DR   InterPro; IPR000906; ZU5.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 3.
DR   Gene3D; G3DSA:1.10.533.10; DEATH_like; 1.
DR   Pfam; PF00023; Ank; 18.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF00791; ZU5; 1.
DR   SMART; SM00248; ANK; 23.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00218; ZU5; 1.
DR   SUPFAM; SSF48403; ANK; 2.
DR   SUPFAM; SSF47986; DEATH_like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 20.
DR   PROSITE; PS50017; DEATH_DOMAIN; 1.
DR   PROSITE; PS51145; ZU5; 1.
PE   2: Evidence at transcript level;
KW   ANK repeat; Repeat.
SQ   SEQUENCE   1852 AA;  202963 MW;  53FDAD2796CA6E5D CRC64;
     MAERPRRSGS DPAADAATSF LRAARSGNLD KALDHLRNGV DINTCNQNGL NGLHLASKEG
     HVKMVVELLH KEIILETTTK KGNTALHIAA LAGQDEVVRE LVNYGANVNA QSQKGFTPLY
     MAAQENHLEV VKFLLENGAN QNVATEDGFT PLAVALQQGH ENVVAHLINY GTKGKVRLPA
     LHIAARNDDT RTAAVLLQND PNPDVLSKTG FTPLHIAAHY ENLNVAQLLL NRGASVNFTP
     QNGITPLHIA SRRGNVIMVR LLLDRGAQIE TRTKDELTPL HCAARNGHVR ISEILLDHGA
     PIQAKTKNGL SPIHMAAQGD HLDCVRLLLQ YNAEIDDITL DHLTPLHVAA HCGHHRVAKV
     LLDKGAKPNS RALNGFTPLH IACKKNHIRV MELLLKTGAS IDAVTESGLT PLHVASFMGH
     LPIVKNLLQR GASPNVSNVK VETPLHMAAR AGHTEVAKYL LQNKAKANAK AKDDQTPLHC
     AARIGHTGMV KLLLENGASP NLATTAGHTP LHTAAREGHV DTALALLEKE ASQACMTKKG
     FTPLHVAAKY GKVRLAELLL EHDAHPNAAG KNGLTPLHVA VHHNNLDIVK LLLPRGGSPH
     SPAWNGYTPL HIAAKQNQIE VARSLLQYGG SANAESVQGV TPLHLAAQEG HTEMVALLLS
     KQANGNLGNK SGLTPLHLVS QEGHVPVADV LIKHGVTVDA TTRMGYTPLH VASHYGNIKL
     VKFLLQHQAD VNAKTKLGYS PLHQAAQQGH TDIVTLLLKN GASPNEVSSN GTTPLAIAKR
     LGYISVTDVL KVVTDETSVV LVSDKHRMSY PETVDEILDV SEDEGTAHIS IMGDELVGSK
     AERRDSRDVG EEKELLDFVP KLDQVVESPA IPRIPCVTPE TVVIRSEDQE QASKEYDEDS
     LIPSSPATET SDNISPVASP VHTGFLVSFM VDARGGSMRG SRHNGLRVVI PPRTCAAPTR
     ITCRLVKPQK LNTPPPLAEE EGLASRIIAL GPTGAQFLSP VIVEIPHFAS HGRGDRELVV
     LRSENGSVWK EHKSRYGESY LDQILNGMDE ELGSLEELEK KRVCRIITTD FPLYFVIMSR
     LCQDYDTIGP EGGSLRSKLV PLVQATFPEN AVTKKVKLAL QAQPVPDELV TKLLGNQATF
     SPIVTVEPRR RKFHRPIGLR IPLPPSWTDN PRDSGEGDTT SLRLLCSVIG GTDQAQWEDI
     TGTTKLIYAN ECANFTTNVS ARFWLSDCPR TAEAVHFATL LYKELTAVPY MAKFVIFAKM
     NDAREGRLRC YCMTDDKVDK TLEQHENFVE VARSRDIEVL EGMPLFAELS GNLVPVKKAA
     QQRSFHFQSF RENRLAIPVK VRDSSREPGG FLSFLRKTMK YEDTQHILCH LNITMPPCTK
     GSGAEDRRRT LTPLTLRYSI LSESRLGFTS DTDRVEMRMA VIREHLGLSW AELARELQFS
     VEDINRIRVE NPNSLLDQST ALLTLWVDRE GENAKMENLY TALRNIDRSE IVNMLEGSGR
     QSRNLKPERR HGDREYSLSP SQVNGYSSLQ DELLSPASLQ YALPSPLCAD QYWNEVAVID
     AIPLAATEHD TMLEMSDMQV WSAGLTPSLV TAEDSSLECS KAEDSDAIPE WKLEGAHSED
     TQGPELGSQD LVEDDTVDSD ATNGLADLLG QEEGQQRVHA RITDSPSVRQ VLDRSQARTL
     DWDKQGSTAV HPQEATQSSW QEEVTQGPHS FQRRITTIQG PEPGALQEYE QVLVSTREHV
     QRGPPETGSP KAGKEPSLWA PESAFSQEVQ GDELQNIPGE QVTEEQFTDE QGNIVTKKII
     RKVVRQVDSS GAIDTQQHEE VELRGSGLQP DLIEGRKGAQ IVKRASLKRG KQ
//
ID   B7ZWC5_MOUSE            Unreviewed;      1250 AA.
AC   B7ZWC5;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 18.
DE   SubName: Full=Abcc4 protein;
GN   Name=Abcc4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
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CC   -----------------------------------------------------------------------
DR   EMBL; BC171974; AAI71974.1; -; mRNA.
DR   IPI; IPI00923039; -.
DR   UniGene; Mm.40537; -.
DR   UniGene; Mm.478748; -.
DR   ProteinModelPortal; B7ZWC5; -.
DR   Ensembl; ENSMUST00000036554; ENSMUSP00000042186; ENSMUSG00000032849.
DR   MGI; MGI:2443111; Abcc4.
DR   HOVERGEN; HBG108314; -.
DR   OrthoDB; EOG476JZD; -.
DR   Bgee; B7ZWC5; -.
DR   Genevestigator; B7ZWC5; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro.
DR   GO; GO:0015238; F:drug transmembrane transporter activity; TAS:MGI.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR017940; ABC_transporter_type1.
DR   InterPro; IPR001140; ABC_transptr_TM_dom.
DR   InterPro; IPR011527; ABC_transptrTM_dom_typ1.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF90123; ABC_TM_1; 2.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding; Repeat.
SQ   SEQUENCE   1250 AA;  140270 MW;  1E539C3F3142DDFF CRC64;
     MLPVHTEVKP NPLQDANLCS RVFFWWLNPL FKTGHKRRLE EDDMFSVLPE DRSKHLGEEL
     QRYWDKELLR AKKDSRKPSL TKAIIKCYWK SYLILGIFTL IEALRLSNSA MGKTTTGQIV
     NLLSNDVNKF DQVTIFLHFL WAGPLQAIAV TVLLWVEIGI SCLAGLAVLV ILLPLQSCIG
     KLFSSLRSKT AAFTDARIRT MNEVITGMRI IKMYAWEKSF ADLIANLRKK EISKILGSSY
     LRGMNMASFF IANKVILFVT FTSYVLLGNE ITASHVFVAM TLYGAVRLTV TLFFPSAIER
     GSEAIVSIRR IKNFLLLDEL PQRKAHVPSD GKAIVHVQDF TAFWDKALDS PTLQGLSFIA
     RPGELLAVVG PVGAGKSSLL SAVLGELPPA SGLVSVHGRI AYVSQQPWVF SGTVRSNILF
     GKKYEKERYE KVIKACALKK DLQLLEDGDL TVIGDRGATL SGGQKARVNL ARAVYQDADI
     YLLDDPLSAV DAEVGKHLFQ LCICQALHEK ITILVTHQLQ YLKAASHILI LKDGEMVQKG
     TYTEFLKSGV DFGSLLKKEN EEAEPSTAPG TPTLRKRTFS EASIWSQQSS RPSLKDGAPE
     GQDAENMQAV QPEESRSEGR IGFKAYKNYF SAGASWFFII FLVLLNMVGQ VFYVLQDWWL
     SHWANKQGAL NNTRNANGNI TETLDLSWYL GIYTGLTAVT VLFGIARSLL VFYILVNASQ
     TLHNRMFESI LKAPVLFFDR NPIGRILNRF SKDIGHMDDL LPLTFLDFIQ TLLLVVSVIA
     VAAAVIPWIL IPLVPLSVVF LVLRRYFLET SRDVKRLEST TRSPVFSHLS SSLQGLWTIR
     AYKAEERCQE LFDAHQDLHS EAWFLFLTTS RWFAVRLDAI CAIFVIVVAF GSLVLAKTLN
     AGQVGLALSY ALTLMGMFQW SVRQSAEVEN MMISVERVIE YTDLEKEAPW ECKKRPPPGW
     PHEGVIVFDN VNFTYSLDGP LVLKHLTALI KSREKVGIVG RTGAGKSSLI SALFRLSEPE
     GKIWIDKILT TEIGLHDLRK KMSIIPQEPV LFTGTMRKNL DPFNEHTDEE LWRALEEVQL
     KEAIEDLPGK MDTELAESGS NFSVGQRQLV CLARAILKNN RILIIDEATA NVDPRTDELI
     QQKIREKFAQ CTVLTIAHRL NTIIDSDKIM VLDSGRLKEY DEPYVLLQNP ESLFYKMVQQ
     LGKGEAAALT ETAKQVYFRR NYPDITFTSP AVMNTSNGQP SALTIFETAL
//
ID   B8JK39_MOUSE            Unreviewed;      1036 AA.
AC   B8JK39;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 21.
DE   SubName: Full=Integrin alpha 9;
GN   Name=Itga9; ORFNames=RP23-366B23.1-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Howden P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Belongs to the integrin alpha chain family.
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DR   EMBL; CT486004; CAX15643.1; -; Genomic_DNA.
DR   EMBL; AC156800; CAX15643.1; JOINED; Genomic_DNA.
DR   EMBL; AC165257; CAX15643.1; JOINED; Genomic_DNA.
DR   IPI; IPI00130117; -.
DR   RefSeq; NP_598482.2; NM_133721.2.
DR   UniGene; Mm.335520; -.
DR   ProteinModelPortal; B8JK39; -.
DR   PRIDE; B8JK39; -.
DR   Ensembl; ENSMUST00000044165; ENSMUSP00000044227; ENSMUSG00000039115.
DR   GeneID; 104099; -.
DR   KEGG; mmu:104099; -.
DR   CTD; 104099; -.
DR   MGI; MGI:104756; Itga9.
DR   HOGENOM; HBG447158; -.
DR   HOVERGEN; HBG004538; -.
DR   OMA; GQEKGNC; -.
DR   OrthoDB; EOG4HHP1K; -.
DR   Bgee; B8JK39; -.
DR   Genevestigator; B8JK39; -.
DR   GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR013519; Int_alpha_beta-p.
DR   InterPro; IPR000413; Integrin_alpha.
DR   InterPro; IPR013649; Integrin_alpha-2.
DR   InterPro; IPR018184; Integrin_alpha_C_CS.
DR   Pfam; PF01839; FG-GAP; 2.
DR   Pfam; PF08441; Integrin_alpha2; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   SMART; SM00191; Int_alpha; 5.
DR   PROSITE; PS51470; FG_GAP; 7.
DR   PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE   3: Inferred from homology;
KW   Cell adhesion; Integrin; Membrane; Receptor; Transmembrane;
KW   Transmembrane helix.
SQ   SEQUENCE   1036 AA;  114416 MW;  F14BDEA82670FFCD CRC64;
     MGGPAAARTG AGGLRALLLA LVAAGVPAGA YNLDAQRPVR FQGPSGSFFG YAVLEHFHDN
     TRWVLVGAPK ADSKYSTSVK SPGAVFKCRV HTNPDRRCTE LDMARGRTRG APCGKTCRGD
     RDDEWMGVSL ARQPRADGRV LACAHRWKNI YYEADHILPH GFCYLIPSNL QAKGKVLIPC
     YEEYKKKYGE EHGSCQAGIA GFFTEELVVM GAPGSFYWAG TLKVLNLTDN TYFKLNDEAI
     MNRRYTYLGY AVTAGHFSHP SITDVVGGAP QDEGIGKVYI FRADRRSGTL IKIFQASGKK
     MGSYFGSSLC AVDLNMDGLS DLLVGAPMFS EIRDEGQVTV YLNQGHGALE EQLTLTGDAA
     YNAHFGESIA NLGDIDDDGF PDVAVGAPKE EDFAGAVYIY HGDANGIVPK YSMKLSGRRL
     NPTLRMFGQS ISGGIDMDGN GYPDVTIGAF LSDSVVLLRA RPVITVDVSI FLPGSINITA
     PQCHDGQQPV NCLNVTVCFR FHGKNVPGEI GLNYNLTADV AQKEKGQLPR VYFVLFGETA
     GQVSERLQLS HMDEVCHHYV AHVKRRVQDV ISPIVFEAAY SLDEHVMGEE DRELPDLTPV
     LRWKKGQRIS QKNQTVFERN CQSEDCAADL QLRGKLLLSS VDEKTPHLAL GAVKNISLNI
     SISNLGDDAY DANVSFNVSR ELFFINMWQK EEMGISCELL ESDFLKCSVG FPFMRSKSKY
     EFSVIFDTSH LSGEEEILSF IVTAQSGNLE RSEALHDNTL TLTVPLVHEV DTSITGIVSP
     TSFVYGESVD ASNFIQLDDQ ECHFQPVNIT LQVYNMGPST LPGSSVSISF PSRLSPGGAE
     MFQVQDMVVS QEKGNCSLQR NPTPCIIPQE QENIFHTIFA FFSKSGRKVL DCEKPGSFCL
     TLHCNLSALP KEESRTINLY MLLNTEILKK DSSSVIQFMA RAKVKVEPAL RVVEIANGNP
     EETLVVFEAL HNLEPRGYVV GWIIAISLLV GILIFLLLAV LLWKMGFFRR RYKEIIEAEK
     NRKENEDGWD WVQKNQ
//
ID   B8QI35_MOUSE            Unreviewed;      1194 AA.
AC   B8QI35;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 19.
DE   SubName: Full=Liprin-alpha 3;
GN   Name=Ppfia3; Synonyms=ppfia3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6;
RX   PubMed=19013515; DOI=10.1016/j.ygeno.2008.10.007;
RA   Zurner M., Schoch S.;
RT   "The mouse and human Liprin-alpha family of scaffolding proteins:
RT   Genomic organization, expression profiling and regulation by
RT   alternative splicing.";
RL   Genomics 93:243-253(2009).
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DR   EMBL; EU568871; ACE63189.1; -; mRNA.
DR   IPI; IPI00399905; -.
DR   RefSeq; NP_084017.2; NM_029741.2.
DR   UniGene; Mm.277235; -.
DR   ProteinModelPortal; B8QI35; -.
DR   Ensembl; ENSMUST00000107779; ENSMUSP00000103408; ENSMUSG00000003863.
DR   GeneID; 76787; -.
DR   KEGG; mmu:76787; -.
DR   CTD; 76787; -.
DR   MGI; MGI:1924037; Ppfia3.
DR   HOGENOM; HBG356868; -.
DR   HOVERGEN; HBG052330; -.
DR   OMA; PGGDSNR; -.
DR   OrthoDB; EOG4X6C7K; -.
DR   Bgee; B8QI35; -.
DR   Genevestigator; B8QI35; -.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR011510; SAM_2.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 2.
DR   Pfam; PF00536; SAM_1; 2.
DR   Pfam; PF07647; SAM_2; 1.
DR   SMART; SM00454; SAM; 3.
DR   SUPFAM; SSF47769; SAM_homology; 3.
DR   PROSITE; PS50105; SAM_DOMAIN; 3.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1194 AA;  133426 MW;  CA6386D6281470FA CRC64;
     MMCEVMPTIS EDGRRGSALG PDEAGGELER LMVTMLTERE RLLETLREAQ DGLATAQLRL
     RELGHEKDSL QRQLSIALPQ EFAALTKELN LCREQLLERE EEIAELKAER NNTRLLLEHL
     ECLVSRHERS LRMTVVKRQA QSPGGVSSEV EVLKALKSLF EHHKALDEKV RERLRMALER
     VAVLEEELEL SNQEALNLRD QLSRRRSGLE EPGKDGDGQT LANGLGPVGE SNRRTAELEE
     ALERQRAEVC QLRERLAVLC RQMSQLEEEL GTAHRELGKA EEANSKLQRD LKEALAQRED
     MEERITTLEK RYLSAQREAT SLHDANDKLE NELASKESLY RQSEEKSRQL AEWLDDAKQK
     LQQTLQKAET LPEIEAQLAQ RVAALNKAEE RHGNFEERLR QLEAQLEEKN QELQRARQRE
     KMNDDHNKRL SETVDKLLSE SNERLQLHLK ERMGALEEKN SLSEEIANMK KLQDELLLNK
     EQLLAEMERM QMEIDQLRGR PPSSYSRSLP GSALELRYSQ APTLPSGAPL DPYGAGSGRA
     GKRGRWSGAK DESSKDWDRS APAGSIPPPF PGELDGSDEE EAEGMFGAEL LSPSGQADVQ
     TLAIMLQEQL EAINKEIKLI QEEKETTEQR AEELESRVSS SGLDSLGRYR SSCSLPPSLT
     TSTLASPSPP SSGHSTPRLA PPSPAREGTD KTNHVSKEEA GVPRGEGPAV PGDTPPPTPR
     SARLERMAQA LALQAGSPED GAPPRGSEST PDSLHKAPKR KSIKSSIGRL FGKKEKGRMG
     PPGRESVSLA GTPSDETLAT DPLGLAKLTG PGDKDRRNKR KHELLEEACR QGLPFAAWDG
     PTVVSWLELW VGMPAWYVAA CRANVKSGAI MANLSDTEIQ REIGISNPLH RLKLRLAIQE
     MVSLTSPSAP ASSRTPTGNV WMTHEEMESL TAATKPETKE ISWEQILAYG DMNHEWVGND
     WLPSLGLPQY RSYFMESLVD ARMLDHLNKK ELRGQLKMVD SFHRVSLHYG IMCLKRLNYD
     RKDLERRREE SQTQIRDVMV WSNERVMGWV SGLGLKEFAT NLTESGVHGA LLALDETFDY
     SDLALLLQIP TQNAQARQLL EKEFSNLISL GTDRRLDEDS AKSFSRSPSW RKMFREKDLR
     GVTPDSAEML PPNFRSAAAG ALGSPGLPLR KLQPEGQTSG SSRADGVSVR TYSC
//
ID   B8QI36_MOUSE            Unreviewed;      1187 AA.
AC   B8QI36;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 17.
DE   SubName: Full=Liprin-alpha 4;
GN   Name=Ppfia4; Synonyms=ppfia4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6;
RX   PubMed=19013515; DOI=10.1016/j.ygeno.2008.10.007;
RA   Zurner M., Schoch S.;
RT   "The mouse and human Liprin-alpha family of scaffolding proteins:
RT   Genomic organization, expression profiling and regulation by
RT   alternative splicing.";
RL   Genomics 93:243-253(2009).
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DR   EMBL; EU568872; ACE63190.1; -; mRNA.
DR   IPI; IPI00921638; -.
DR   RefSeq; NP_001138327.1; NM_001144855.1.
DR   UniGene; Mm.295105; -.
DR   Ensembl; ENSMUST00000027729; ENSMUSP00000027729; ENSMUSG00000026458.
DR   GeneID; 68507; -.
DR   KEGG; mmu:68507; -.
DR   CTD; 68507; -.
DR   MGI; MGI:1915757; Ppfia4.
DR   HOGENOM; HBG356868; -.
DR   HOVERGEN; HBG052330; -.
DR   OrthoDB; EOG4PC9RB; -.
DR   Bgee; B8QI36; -.
DR   Genevestigator; B8QI36; -.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR011510; SAM_2.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 3.
DR   Pfam; PF00536; SAM_1; 2.
DR   Pfam; PF07647; SAM_2; 1.
DR   SMART; SM00454; SAM; 3.
DR   SUPFAM; SSF47769; SAM_homology; 3.
DR   PROSITE; PS50105; SAM_DOMAIN; 3.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1187 AA;  133713 MW;  44C94BE3611D62BC CRC64;
     MCEVMPTINE GDPLGPPHGA DAEANFEQLM VNMLDEREKL LESLRESQET LVATQSRLQD
     ALHERDQLQR HLNSALPQEF ATLTRELSMC REQLLEREEE ISELKAERNN TRLLLEHLEC
     LVSRHERSLR MTVVKRQAQS PSGVSSEVEV LKALKSLFEH HKALDEKVRE RLRAALERVT
     TLEEQLAGAH QQVSALQQGA GIRDGVAEEE GTVDLGPKRL WKDDTGRVEE LQGLLEKQNY
     ELSQARERLV TLSATVTELE EDLGTARRDL IKSEELSSKH QRDLREALAQ KEDMEERITT
     LEKRYLAAQR EATSIHDLND KLENELANKE SLHRQCEEKA RHLQELLEVA EQKLQQTMRK
     AETLPEVEAE LSQRIAALTK AEERHGNIEE HLRQLEGQLE EKNQELARVR QREKMNEDHN
     KRLSDTVDRL LSESNERLQL HLKERMAALE EKGRLSEEIE KLRQEVDQLK GRGGPFVDGI
     HSRSHVGSAA DVRFSLSTAT HAPPGLHRRY SALRDESAKD WKPSPLPGVL GATTPAFDSD
     PEISDVDEDE PGGLVGTQVD VISPGGHSDA QTLAMMLQEQ LDAINQEIRM IQEEKESTEL
     RAEEIETRVT SGSMEALNLT QLRKRGSIPT SLTALSLASA SPPLSGRSTP KLTSRSAAQD
     LDRMGVMTLP SDLRKHRRKL LSPVSREENR EDKATIKCET SPPSSPRTLR LEKLGHPGLS
     QEEGKSALEG QDSNPSSSNS SQDSLHKGAK RKGIKSSIGR LFGKKEKGRL IQLSRDATGH
     VLLTDSELSL QEPMVPAKLG TQAEKDRRLK KKHQLLEDAR RKGMPFAQWD GPTVVSWLEL
     WVGMPAWYVA ACRANVKSGA IMSALSDTEI QREIGISNAL HRLKLRLAIQ EMVSLTSPSA
     PPTSRTSSGN VWVTHEEMET LATSTKTDSE EGSWAQTLAY GDMNHEWIGN EWLPSLGLPQ
     YRSYFMECLV DARMLDHLTK KDLRVHLKMV DSFHRTSLQY GIMCLKRLNY DRKELEKRRE
     ESQHEIKDVL VWTNDQVVHW VQSIGLRDYA GNLHESGVHG ALLALDENFD HNTLALVLQI
     PTQSTQARQV MEREFNNLLA LGTDRKLDDG EEKVFRRAPS WRKRFRPRDH HSGGMLGTSA
     ETLPAGFRVS TLGPLQPPPA PPKKIMPEAG TAGAQRLEPS TVRTYSC
//
ID   B9EHE8_MOUSE            Unreviewed;      1101 AA.
AC   B9EHE8;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   05-OCT-2010, entry version 10.
DE   SubName: Full=R3hdm1 protein;
GN   Name=R3hdm1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC137772; AAI37773.1; -; mRNA.
DR   IPI; IPI00461460; -.
DR   UniGene; Mm.221041; -.
DR   HOVERGEN; HBG052192; -.
DR   PhylomeDB; B9EHE8; -.
DR   Genevestigator; B9EHE8; -.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   InterPro; IPR001374; R3H_ss-bd.
DR   Pfam; PF01424; R3H; 1.
DR   SMART; SM00393; R3H; 1.
DR   PROSITE; PS51061; R3H; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1101 AA;  120868 MW;  45081F71B218BC07 CRC64;
     MRMSDIVIIK DETETMKDLE AEMRDTTRVE NLIKSENYGK ISAEKNEHCI DNNIDLQRPP
     QSFGQTGKRS KSSSKLKLVR SLAVCEESPP PPAAEISQET QEKIQIQLTQ SFEKEEKPSK
     DETDKEKASD KLPRKMLSRD SSQEYTDSTG IDLHEFLVNT LKNNPRDRMM LLKLEQEILD
     FIGNNESPRK KFPPMTSYHR MLLHRVAAYF GLDHNVDQSG KSVIVNKTSN TRIPDQKFNE
     HIKDDRGEDF QKRYILKRDN SSFDKDDSQM RIRLKDDRRS KSIEEREEEY QRARDRIFSQ
     DSLCSQENYI IDKRIQDEDT IGTQQRRQIF RVNKDASGRS TNSHQSSTEN ELKYSEPRPW
     SSTDSDSSLR NLKPAVTKAS SFSGISVLTR GDSSGSSKSI GRLSKTGSES SGSVGSSTGS
     LSHTQQPLPG SALSQSSHGA PVIYPAASNH SSLSFDGGLS GQGASPSTSF LLLPLEATGI
     PPGSILINPQ TGQPFLNPDG SPVVYNPPMT QQPVRTQVPG PPQPPLPPPP PQQPAASHMF
     SQDNLGAQFS HMSLARQPSA DGSDPHATMF QSTVVLQSPQ QSGYIVTTAP PHPPPPPPPP
     PPPPSLPPGQ SVPTASFSAS GHPVSQPVLQ QQGFLPQPSP QMPACYCAPG HYHSSQPQYR
     PIPSVHHSSH LNQPLPQPAQ HTGYQVMPNQ QQNYQGIVGV QSPQSQSLMG GQPNSTGPHI
     QGVVIPYPSV PSYQVSLPQG SQGIAHQTYQ QPVVFPNQSN QGSLPTTGMP VYYSVIPPGQ
     QSNLSSAVGY LQHPGSEQVQ FPRTTSPCSS QQLQGHQCAA VPQQPPGGGM VMMQLNLPNN
     PQSRTHSPPQ WKQNKHYCDH QRGQKCMDFS NMDNIVQPSP QLSSPILSPV QSPAPAQLST
     LKTIRPSGPP LSIMSQFARP FVPGQGDARY PLLGQPLQYN PPTLLHGHIP HQQGQSGSRH
     GNRGRRQAKK AASTDLGAGE AVVGKVLEIT ELPDGITRVE AEKLFGELFK IGAKIRWLRD
     PQSQPQLRRH ALCCGSGDNT VNPEHSKPSD LASTYTVLAT FPSISAAQSA LKKQIHSVNK
     FKLRMSKKHY DFHILERASS Q
//
ID   B9EHJ3_MOUSE            Unreviewed;      1685 AA.
AC   B9EHJ3;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 19.
DE   SubName: Full=Tjp1 protein;
GN   Name=Tjp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC   -!- SIMILARITY: Contains 3 PDZ (DHR) domains.
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DR   EMBL; BC138028; AAI38029.1; -; mRNA.
DR   IPI; IPI00944062; -.
DR   RefSeq; NP_001157046.1; NM_001163574.1.
DR   UniGene; Mm.4342; -.
DR   GeneID; 21872; -.
DR   KEGG; mmu:21872; -.
DR   CTD; 21872; -.
DR   MGI; MGI:98759; Tjp1.
DR   HOVERGEN; HBG007849; -.
DR   Genevestigator; B9EHJ3; -.
DR   GO; GO:0005913; C:cell-cell adherens junction; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0046581; C:intercellular canaliculus; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005923; C:tight junction; IDA:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR   GO; GO:0001825; P:blastocyst formation; IMP:MGI.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR005417; ZonOcculdens.
DR   InterPro; IPR005418; ZonOcculS1.
DR   InterPro; IPR000906; ZU5.
DR   PANTHER; PTHR13865:SF9; ZonOcculS1; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF00595; PDZ; 3.
DR   Pfam; PF07653; SH3_2; 1.
DR   Pfam; PF00791; ZU5; 1.
DR   PRINTS; PR01597; ZONOCCLUDNS.
DR   PRINTS; PR01598; ZONOCCLUDNS1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 3.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00218; ZU5; 1.
DR   SUPFAM; SSF50156; PDZ; 3.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 3.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS51145; ZU5; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1685 AA;  188852 MW;  1D4F51FDA6ACFA20 CRC64;
     MSARAAAAKS TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG ETSIVISDVL
     KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK NAKITIRRKK KVQIPVSHPD
     PEPVSDNEDD SYDEEVHDPR AGRGALANRR SEKSWARDRS ASRERSLSPR SDRRSVASSQ
     PAKPTKVTLV KSRKNEEYGL RLASHIFVKE ISQDSLAARD GNIQEGDVVL KINGTVTENM
     SLTDAKTLIE RSKGKLKMVV QRDERATLLN VPDLSDSIHS ANASERDDIS EIQSLASDHS
     GRSHDRPPRR SQSRSPDQRS EPSDHSTQSP QQPSNGSLRS REEERMSKPG AISTPVKHVD
     DHPPKAVEEV TVEKNEKQTP TLPEPKPVYA QVGQPDVDLP VSPSDGALPN SAHEDGILRP
     SMKLVKFRKG DSVGLRLAGG NDVGIFVAGV LEDSPAAKEG LEEGDQILRV NNVDFTNIIR
     EEAVLFLLDL PKGEEVTILA QKKKDVYRRI VESDVGDSFY IRTHFEYEKE SPYGLSFNKG
     EVFRVVDTLY NGKLGSWLAI RIGKNHKEVE RGIIPNKNRA EQLASVQYTL PKTAGGDRAD
     FWRFRGLRSS KRNLRKSRED LSAQPVQTKF PAYERVVLRE AGFLRPVTIF GPIADVAREK
     LAREEPDIYQ IAKSEPRDAG TDHRSSGIIR LHTIKQIIDQ DKHALLDVTP NAVDRLNYAQ
     WYPIVVFLNP DSKQGVKTMR MRLCPESRKS ARKLYERSHK LRKNNHHLFT TTINLNSMND
     GWYGALKEAI QQQQNQLVWV SEGKADGATS DDLDLHDDRL SYLSAPGSEY SMYSTDSRHT
     SDYEDTDTEG GAYTDQELDE TLNDEVGTPP ESAITRSSEP VREDSSGMHH ENQTYPPYSP
     QAQPQAIHRI DSPGLKPASQ QVYRKEPYSE EMMRQNHILK QPALGHPGQR PDKEPNLAYE
     PQLPYIEKQA SRDLEQPSYR YEVSSYTDQF SRNYDHRLRF EDRIPTYEDQ WSYYDDKQPY
     QPRPFENQHP RDLDSRQHPE EASERGYFQR FEEPAPLSYD SRTRYEQLPR TSTLRHEEQP
     APAYEVHNRY RPEAQPYSST GPKSSEPKQY FDQYPRSYEQ VPPPGFTSKT GHYEPLHGAA
     VVPPLIPSSQ QKPEVLPSAT KPQPPPPTLT EEEEDPAMKP QSVLTRVKMF ENKRSASLEN
     KKDVNDTASF KPPEVASKPP GASLAGPKPV PQSQFSEHDK TLYRLPEPQK PQVKPPEDIV
     RSNHYDPEED EEYYRKQLSY FDRRSFESKP SAHLPAGHHS EPAKPVHSQS QPNFSSYSSK
     GKPETDAVDR SFSEKRYDPA QATPPPPPLP SQYSQPAPPL SSSSLHIHSK GAQGEGNSVS
     LDFQNSYMSK PDPPPSQSKP ATFRPPTRED PPQTFYPQKS FPDKAPVNGA EQTQKTITPV
     YNRFTPKPYT SSARPFERKF ESPKFNHNLL PSETVHKPEL SSKTPTSPKT LMKAHSSTQP
     PEFDSGVETF SVHTDKPKYQ MNNISTMPKA VPVSPSAVEE DEDEDGHTVV ATARGIFNSN
     GGVLSSIETG VSIIIPQGAI PEGIEQEIYF KVCRDNSILP PLDKEKGETL LSPLVMCGPH
     GLKFLKPVEL RLPHCASMTP DGWSFALKSS DSSSGDPKTW QNKCLPGDPN YLVGANCVSV
     LIDHF
//
ID   B9EHN9_MOUSE            Unreviewed;      1730 AA.
AC   B9EHN9;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 13.
DE   SubName: Full=Zinc finger CCCH type containing 13;
GN   Name=Zc3h13;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
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DR   EMBL; BC138264; AAI38265.1; -; mRNA.
DR   IPI; IPI00515528; -.
DR   UniGene; Mm.74704; -.
DR   Ensembl; ENSMUST00000022577; ENSMUSP00000022577; ENSMUSG00000022000.
DR   MGI; MGI:1914552; Zc3h13.
DR   HOGENOM; HBG281303; -.
DR   HOVERGEN; HBG107115; -.
DR   OrthoDB; EOG4KSPJC; -.
DR   Bgee; B9EHN9; -.
DR   Genevestigator; B9EHN9; -.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR000571; Znf_CCCH.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Zinc.
SQ   SEQUENCE   1730 AA;  203827 MW;  3E9D4A6ACED42874 CRC64;
     MSKIRRKVTV ENTKTISEST SRRPSVFERL GPSTGSTTET QCRNWLKTGS CLYGNTCRFI
     HGPSPRGKGY SSNYRRSPER PTGDLRERMK NKRQDVDSES QKRNTEEPSS PVRKESSRGR
     HRDKEDIKIV KERTPESEEE NVEWETNRDD SDNGDINYDY VHELSLEMKR QKIQRELMKL
     EQENMDKREE IIIQKEVSPE VVRSKLSPSP SLRKSSKSPK RKSSPKASSA GKKERKAAVV
     ASPLLDQQRN SKGNQSKKKG PRTPSPPPPI LEDIILGKKY KEKYKVKDRI EEKPRDGKDR
     GRDFEKQREK RDKPRSSSPG QHHSPLSSRH HSSSSQSGSS IQRHSPSPRR KRTPSPSYQR
     TLTPSLRRSA SPYPTHCLSS PQRKQSPPRH RSPMREKGRH DHERTSQSHD RRHERREETR
     GKRDREKDTR EERESEHDHR DDREPRDSRD RRDTRDRREL RDSRDMRDSR EMRDYSRDAK
     ESRDPRDSRS ARDVHDYRDR EARDAHARDV RDARDARDAR DARDIRDVRD VRDVRDVRDV
     RDVRDVRDVR DVRDARDVRD VRDARDVRDV RDVRDGHRKE DVYQEEARSY GRNHLREESS
     RVELRNDSRN ESRSEIRNDR MGRSRGRGPE LPEKGSRGTR GSQMDSHSSG SNYHDSWETR
     SSYPERDRYP ERDTRDPARD SSFERRHGER DRRDNRERDQ RPSSPIRHQG RSEELERDER
     REERRIDRVD ERRDDRVRDR DRDRERERER EREREREREK ERERELERER AREREREREK
     ERERERERER DQRDRDHDRE RERERERERE KEREREREER ERERERERER ERERERERER
     ERERERERER AREREKERER QREWEDKDKG RDDRREKRED IHVREDRIPR DSHEERKSKK
     RYRNEGSPSP RQSPKRRREH SPDSDTYHSG DDKNEKHRLL SQVVRPQESR SLSPSHLTED
     RQGRWKEEDR KSERKESSRR YEEQELKEKL SCGDRQREQA ESVDSSRVRA QDLLSHRQAE
     DRDRDGSDRA HDEKKKAKAP KKPVKKKKEE DVGVERGNLE THEDSQVFSP KKGQKKKNIE
     KKRKRSKGDS DVSDEEAAPQ NKKKRGPRTP PLAIKEELAD ISTDKDGVLE DPLKKENTAF
     SDWSDEDVPD RTEGLEAEHT AATATPGSTP SPLSSLLPPP PPVAAASTAA TALASSAVSA
     TTSATSSSSA ATSNTNGSED SHRKCHRARG EKVEVSHVTL EDTPHRKLVD QKRSSSLGSN
     RSHRSHTSGR LRSPSNDSAH RSGDDQGSRK RVLHSGSRDR EKTKSLEITG ERKSRIDQLK
     RGEPSRSTSS DRQDSRSHSS RRSSPESDRQ VHSRSGSFDS RDRLQERDRY EHDRERERDR
     RDPRQREWDR EAEKEWPRTR DRDRLRERDR DRDRRRDLDR ERERLISDPM ERDRERERTF
     ETSQLESGKR SEVKLESEHE RDLEGSSRDS VALDKERMDR DLGSVQGFED VSKAERTESL
     EAGDDESKLD DAHSLGSGAG EGYEPISDDE LDEILAGDAE KREDQQEEEK MPDPLDVIDV
     DWSGLMPKHP KEPREPGAAL LKFTPGAVLL RVGISKKLAG SELFTKVKET CQQLVEKPKD
     ADSLFEHELG ALNMAALLRK EERASLLSDL GPCCKALCFR RDSAIRKQLV KNEKGTVKQA
     YTNTPMVDNE LLRLSLRLFK KKATCHAPGQ EKTEDGKLGP CSIQQELCVS
//
ID   B9EHT4_MOUSE            Unreviewed;       547 AA.
AC   B9EHT4;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 18.
DE   SubName: Full=CAP-GLY domain containing linker protein 3;
DE   SubName: Full=MCG22809;
GN   Name=Clip3; ORFNames=mCG_22809;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC138413; AAI38414.1; -; mRNA.
DR   EMBL; CH466593; EDL24034.1; -; Genomic_DNA.
DR   IPI; IPI00265407; -.
DR   RefSeq; NP_001074583.1; NM_001081114.1.
DR   UniGene; Mm.159258; -.
DR   PRIDE; B9EHT4; -.
DR   Ensembl; ENSMUST00000014065; ENSMUSP00000014065; ENSMUSG00000013921.
DR   GeneID; 76686; -.
DR   KEGG; mmu:76686; -.
DR   CTD; 76686; -.
DR   MGI; MGI:1923936; Clip3.
DR   HOGENOM; HBG717788; -.
DR   HOVERGEN; HBG057079; -.
DR   OMA; FTCPPKH; -.
DR   OrthoDB; EOG4Z36DJ; -.
DR   Bgee; B9EHT4; -.
DR   Genevestigator; B9EHT4; -.
DR   GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR   GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR   GO; GO:0005792; C:microsome; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR   GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
DR   GO; GO:0035594; F:ganglioside binding; ISS:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0072321; P:chaperone-mediated protein transport; ISS:UniProtKB.
DR   GO; GO:0045444; P:fat cell differentiation; IEP:UniProtKB.
DR   GO; GO:0044091; P:membrane biogenesis; ISS:UniProtKB.
DR   GO; GO:0031115; P:negative regulation of microtubule polymerization; ISS:UniProtKB.
DR   GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; ISS:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptosis; ISS:UniProtKB.
DR   GO; GO:0045807; P:positive regulation of endocytosis; ISS:UniProtKB.
DR   GO; GO:0090004; P:positive regulation of establishment of protein localization in plasma membrane; IDA:UniProtKB.
DR   GO; GO:0010828; P:positive regulation of glucose transport; IMP:UniProtKB.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR023092; CAP-Gly_CS.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Gene3D; G3DSA:2.30.30.190; CAP-Gly_domain; 2.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF01302; CAP_GLY; 2.
DR   SMART; SM00248; ANK; 3.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF74924; CAP-Gly_domain; 2.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS00845; CAP_GLY_1; 2.
DR   PROSITE; PS50245; CAP_GLY_2; 2.
PE   2: Evidence at transcript level;
KW   ANK repeat; Repeat.
SQ   SEQUENCE   547 AA;  59587 MW;  851B8B94DA20A1AD CRC64;
     MTKTDPAPMA PPPRGEEEEE EEEDEPVPEA PSPTQERRQK PVVHPSAPAP LPKDYAFTFF
     DPNDPACQEI LFDPKTTIPE LFAIVRQWVP QVQHKIDVIG NEILRRGCHV NDRDGLTDMT
     LLHYACKAGA HGVGDPAAAV RLSQQLLALG ADVTLRSRWT NMNALHYAAY FDVPDLVRVL
     LKGARPRVVN STCSDFNHGS ALHIAASNLC LGAAKCLLEH GANPALRNRK GQVPAEVVPD
     PMDMSLDKAE AALVAKELRT LLEEAVPLSC TLPKVTLPNY DNVPGNLMLS ALGLRLGDRV
     LLDGQKTGTL RFCGTTEFAS GQWVGVELDE PEGKNDGSVG GVRYFICPPK QGLFASVSKV
     SKAVDAPPSS VTSTPRTPRM DFSRVTGKGR REHKGKKKSP SSPSLGSLQQ REGAKAEVGD
     QVLVAGQKQG IVRFYGKTDF APGYWYGIEL DQPTGKHDGS VFGVRYFTCA PRHGVFAPAS
     RIQRIGGSTD PPGDSVGAKK VHQVTMTQPK RTFTTVRTPK DIASENSISR LLFCCWFPWM
     LRAEMQS
//
ID   B9EHZ5_MOUSE            Unreviewed;       539 AA.
AC   B9EHZ5;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 21.
DE   SubName: Full=Membrane protein, palmitoylated 6 (MAGUK p55 subfamily member 6);
DE   SubName: Full=Membrane protein, palmitoylated 6 (MAGUK p55 subfamily member 6), isoform CRA_a;
GN   Name=Mpp6; ORFNames=mCG_119906;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
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DR   EMBL; BC138666; AAI38667.1; -; mRNA.
DR   EMBL; CH466597; EDK98615.1; -; Genomic_DNA.
DR   IPI; IPI00314316; -.
DR   RefSeq; NP_064323.2; NM_019939.2.
DR   UniGene; Mm.41288; -.
DR   UniGene; Mm.463873; -.
DR   UniGene; Mm.478422; -.
DR   ProteinModelPortal; B9EHZ5; -.
DR   PRIDE; B9EHZ5; -.
DR   Ensembl; ENSMUST00000036236; ENSMUSP00000039314; ENSMUSG00000038388.
DR   GeneID; 56524; -.
DR   KEGG; mmu:56524; -.
DR   CTD; 56524; -.
DR   MGI; MGI:1927340; Mpp6.
DR   HOVERGEN; HBG001858; -.
DR   PhylomeDB; B9EHZ5; -.
DR   Bgee; B9EHZ5; -.
DR   Genevestigator; B9EHZ5; -.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR004172; L27.
DR   InterPro; IPR014775; L27_C.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF02828; L27; 2.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00569; L27; 2.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS51022; L27; 2.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   539 AA;  60925 MW;  56409E4E57D25971 CRC64;
     MQQVLENLTE LPSSTGAEEI DLIFLKGIME NPIVKSLAKA HERLEDSKLE AVSDNNLELV
     NEILEDITPL ISVDENVAEL VGILKEPHFQ SLLEAHDIVA SKCYDSPPSS PEMNIPSLNN
     QLPVDAIRIL GIHKKAGEPL GVTFRVENND LVIARILHGG MIDRQGLLHV GDIIKEVNGH
     EVGNNPKELQ ELLKNISGSV TLKILPSYRD TITPQQVFVK CHFDYNPFND NLIPCKEAGL
     KFSKGEILQI VNREDPNWWQ ASHVKEGGSA GLIPSQFLEE KRKAFVRRDW DNSGPFCGTI
     SNKKKKKMMY LTTRNAEFDR HEIQIYEEVA KMPPFQRKTL VLIGAQGVGR RSLKNRFIVL
     NPARFGTTVP FTSRKPREDE KDGQAYKFVS RSEMEADIKA GKYLEHGEYE GNLYGTKIDS
     ILEVVQTGRT CILDVNPQAL KVLRTSEFMP YVVFIAAPEL ETLRAMHKAV VDAGITTKLL
     TDSDLKKTVD ESARIQRAYN HYFDLIIVND NLDKAFEKLQ TAIEKLRMEP QWVPISWVY
//
ID   B9EID4_MOUSE            Unreviewed;       529 AA.
AC   B9EID4;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 18.
DE   SubName: Full=RAB11 family interacting protein 2 (Class I);
GN   Name=Rab11fip2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 C2 domain.
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DR   EMBL; BC139380; AAI39381.1; -; mRNA.
DR   EMBL; BC139419; AAI39420.1; -; mRNA.
DR   IPI; IPI00281670; -.
DR   RefSeq; NP_001028344.2; NM_001033172.3.
DR   UniGene; Mm.24167; -.
DR   Ensembl; ENSMUST00000051996; ENSMUSP00000059978; ENSMUSG00000040022.
DR   GeneID; 74998; -.
DR   KEGG; mmu:74998; -.
DR   CTD; 74998; -.
DR   MGI; MGI:1922248; Rab11fip2.
DR   HOGENOM; HBG443975; -.
DR   HOVERGEN; HBG054920; -.
DR   OMA; SLKSPHR; -.
DR   OrthoDB; EOG4WQ12F; -.
DR   Bgee; B9EID4; -.
DR   Genevestigator; B9EID4; -.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR019018; Rab11-bd_FIP_dom_C.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF09457; RBD-FIP; 1.
DR   SMART; SM00239; C2; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   PROSITE; PS50004; C2; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   529 AA;  59989 MW;  B323D6B7E10F0DA0 CRC64;
     MMLSEQAQKW FPTHVQVTVL QAKDLKPKGK SGTNDTYTII QLGKEKYSTS VAEKTLEPVW
     KEEASFELPG LLMQGSPEKY ILFLIVMHRS LVGLDKFLGQ VAINLNDIFE DKQRRKTEWF
     RLESKQGKRI KNRGEIKVNI QFMRNNMTAS MFDLSMKDKT RSPFAKLKDK MKGRKSDGVF
     SDTSSAIVPS THMPDANPEF SSGEMQMKSK PKKPFLLGPQ RLSSAHSMSD LTGSHLSSEK
     LKSSTVGPTH LLSRQIDSFG VVPESGSLKS PHRRTLSFDT SKLNQPGSIV DEGEHSFGRQ
     SDPFTNVTAS LPQKFATLPR KKNPFEESSE PWDSSMNLFS KPIEVRKESK REKREKVSLF
     ERVTGKRDSR RPDKLNNGGS DSPCDLKSPS AFSENRQDYF EYESTNPFTA KFRASTIMPS
     SSFHVNPTSS EDLRKIPDNN PFDATAGYRS LTYEEVLQEL VKHKELLRRK DTHIRELEDY
     IDNLLVRVME ETPSILRVPY EPSRKAVYTQ DHLSPGPPHL CGEATSTHS
//
ID   B9EIV0_MOUSE            Unreviewed;       730 AA.
AC   B9EIV0;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 16.
DE   SubName: Full=Ablim1 protein;
GN   Name=Ablim1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 4 LIM zinc-binding domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC141083; AAI41084.1; -; mRNA.
DR   IPI; IPI00356147; -.
DR   UniGene; Mm.217161; -.
DR   UniGene; Mm.446592; -.
DR   Ensembl; ENSMUST00000099294; ENSMUSP00000096897; ENSMUSG00000025085.
DR   Ensembl; ENSMUST00000111538; ENSMUSP00000107163; ENSMUSG00000025085.
DR   MGI; MGI:1194500; Ablim1.
DR   HOVERGEN; HBG031499; -.
DR   OrthoDB; EOG44TP7D; -.
DR   Bgee; B9EIV0; -.
DR   Genevestigator; B9EIV0; -.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007411; P:axon guidance; IDA:MGI.
DR   GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:MGI.
DR   InterPro; IPR003128; Villin_headpiece.
DR   InterPro; IPR001781; Znf_LIM.
DR   Gene3D; G3DSA:1.10.950.10; VHP; 1.
DR   Gene3D; G3DSA:2.10.110.10; Znf_LIM; 4.
DR   Pfam; PF00412; LIM; 4.
DR   Pfam; PF02209; VHP; 1.
DR   SMART; SM00132; LIM; 4.
DR   SMART; SM00153; VHP; 1.
DR   SUPFAM; SSF47050; VHP; 1.
DR   PROSITE; PS51089; HP; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 4.
PE   2: Evidence at transcript level;
KW   LIM domain; Metal-binding; Zinc.
SQ   SEQUENCE   730 AA;  82362 MW;  244A6C0B5DD15698 CRC64;
     MPSLLGLKCL GKLCSSEKGK VPSPERASLR NSHRRLLIED LSVPETPDPA HRRRGTVIHL
     VYLYSAGCGP PELRFSSYDP SVAHPQDPHH SSEKPVIHCH KCGEPCKGEV LRVQTKHFHI
     KCFTCKVCGC DLAQGGFFIK NGDYLCTLDY QRMYGTRCHG CGEFVEGEVV TALGKTYHPN
     CFACTICKRP FPPGDRVTFN GRDCLCQLCA QPMSSSPKEA SCSSNCAGCG RDIKNGQALL
     ALDKQWHLGC FKCKSCGKVL TGEYISKDGS PYCEKDYQGL FGVKCEACHQ FITGKVLEAG
     DKHYHPSCAR CSRCNQMFTE GEEMYLQGST VWHPDCKQST KTEEKLRPTR TSSESIYSRP
     GSSIPGSPGH TIYAKVDNEI LDYKDLAAIP KVKAIYDIER PDLITYEPFY TSGYEDKQER
     QSLGESPRTL SPTPSAEGYQ DVRDRMIHRS TSQGSINSPV YSRHSYTPTT SRSPQHFHRP
     GNEPSSGRNS PLPYRPDSRP LTPTYAQAPK HFHVPDQGIN IYRKPPIYKQ HGTDPRRRSS
     GREEDEEELL RRRQLQEEQL MKLNSGLGQL ILKEEMEKES RERASLASRY DSPLHSASHA
     PSSKTSSLPG YGKNGLHRPV STDFAQYNSY GDISGGVRDY QTLPDGHMPA VRMDRGVSMP
     NMLEPKIFPY EMLMVTNRGR NKILRDVDRT RLERHLAPEV FWEIFGMSIQ EFDKLPLWRR
     NDMKKKAKLF
//
ID   B9EIW5_MOUSE            Unreviewed;       932 AA.
AC   B9EIW5;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   05-OCT-2010, entry version 11.
DE   SubName: Full=Ncoa7 protein;
GN   Name=Ncoa7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
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DR   EMBL; BC141150; AAI41151.1; -; mRNA.
DR   IPI; IPI00671462; -.
DR   UniGene; Mm.297903; -.
DR   Ensembl; ENSMUST00000068567; ENSMUSP00000066741; ENSMUSG00000039697.
DR   MGI; MGI:2444847; Ncoa7.
DR   HOVERGEN; HBG065488; -.
DR   PhylomeDB; B9EIW5; -.
DR   Bgee; B9EIW5; -.
DR   Genevestigator; B9EIW5; -.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   InterPro; IPR004182; GRAM.
DR   InterPro; IPR018392; Peptidoglycan-bd_lysin.
DR   InterPro; IPR002482; Peptidoglycan-bd_Lysin_sg.
DR   InterPro; IPR006571; TLDc.
DR   Pfam; PF02893; GRAM; 1.
DR   Pfam; PF01476; LysM; 1.
DR   SMART; SM00257; LysM; 1.
DR   SMART; SM00584; TLDc; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   932 AA;  105015 MW;  AB5AF2865D2B6545 CRC64;
     MDTKEEKKEQ KERKQSYFAR LKKKKQAKQN AEIVSAASSK SRSGKDDANS DILEQDKFNV
     TAEGDHSTDD KKKRKSNQLK EIRRTELKRY YSVDDNQNKT HDKKEKKMMV QKPQGTMEYT
     AGSQDTLNSV ALKFNVTPNK LVELNKLFTH TIVPGQVLFV PDANISSSTI QLSSSTPGAT
     VSPSSSDAEY DKLPDADLAR KALKPIERVL SSTSEEDEPG VVKFLKMNCR YFTDGKGVVG
     GVMIVTPNNI MFDPHKSDPL VIENGCEEYG LICPMEEVVS IALYSDISHM KIKDALPSPG
     EWEDLASEKD INPFSKFKSI NKEKRQQNGE RTLALDAKSV RSPEESTERT CTRIEPPDNS
     ELWKLKNLQS SRGTTSESPS VTQLSMRAAL EPTAKENCLL KGDEDFVDLE ELSSQPESGI
     NKGDATKECL SYDQKKDGPH TVMSAKKGHV QSAQEVMGPE SDTELKGALD LETAEKQDEA
     PEVDKHSGSP ENLGESTLNI HEDLDKIKLI EFYLNKNKEG SQLLENVQKS ELSDRKSIEP
     GGIDITLSSS LPQAGDSPPE DNKEPGTLWV KGGETLPLKL DPSAEETVIN NKEVLDSLGS
     SLDKMCHSAQ MDNKSEIQLW LLKRIQVPIE DILPSKEEKS KTPPMFLCIK VGKPMRKSFA
     SHTATMVQQY SKRRKQPEYW FAVPRERVDH LYTFFVQWSP DVYGKDAKEQ GFVVVEKEEL
     NMIDNFFSEP TTKSWEIITV EEAKRRKSTC SYYEEEEEEE EGLPILQPHS ALLENMHIEQ
     LARRLPARVQ GYPWRLAYST LEHGTSLKTL YRKSASLDSP VLLVIKDMDN QIFGAYATHP
     FKFSDHYYGT GETFLYTFSP NFKVFKWSGE NSYFINGDIS SLELGGGGGR FGLWLDADLY
     HGRSNSCSTF NNDILSKKED FIVQDLEVWT FE
//
ID   B9EJ54_MOUSE            Unreviewed;      2008 AA.
AC   B9EJ54;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   11-JAN-2011, entry version 13.
DE   SubName: Full=MCG21756, isoform CRA_b;
DE   SubName: Full=Nup205 protein;
GN   Name=Nup205; ORFNames=mCG_21756;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC141333; AAI41334.1; -; mRNA.
DR   EMBL; CH466533; EDL13669.1; -; Genomic_DNA.
DR   IPI; IPI00929832; -.
DR   RefSeq; NP_081789.1; NM_027513.1.
DR   UniGene; Mm.261208; -.
DR   UniGene; Mm.480993; -.
DR   Ensembl; ENSMUST00000043815; ENSMUSP00000039656; ENSMUSG00000038759.
DR   GeneID; 70699; -.
DR   KEGG; mmu:70699; -.
DR   CTD; 70699; -.
DR   MGI; MGI:2141625; Nup205.
DR   HOVERGEN; HBG052682; -.
DR   Bgee; B9EJ54; -.
DR   Genevestigator; B9EJ54; -.
DR   InterPro; IPR021827; DUF3414.
DR   Pfam; PF11894; DUF3414; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   2008 AA;  227465 MW;  C09B0207E36285B8 CRC64;
     MAALLAVNSA ASLWGPYKDI WQTVGSALWR RQPEAVHLLD MILKKHKPDF ISLFKNPPKN
     VQQHEKIQKA SSEGVAIQGQ QGTRLLPEQL IKEAFIISDL FDIGELSAVE LLLAGEHQQP
     HFPGLTRGLV AVLLYWDGKR CIANSLRTLI QSRRGKTWTL ELSPELVSMT TRFTDELMEQ
     GLTYKVLTLL SQIDVNNEFE KLQRERGLGS EKHRKEVSDL IKECRQSLAE SLFAWACQSP
     LPKDDTLLLI GHLERVTVEA NGSLDAVNLC LLMALLYCFD TSFIDQSTEE RDDMIHHLPL
     LTERQYVSTI HSRLQDSQPW KLPGLQATVR LAWALALRGI SQLPDVTALA EFTEADEAIA
     ELAIADNVFL FLSEAVVLAE NFYQEEFYIR RIHSLITDFL AFMPMKVKQL KNRADEDARM
     IHMSIQMGNE PPISLRRDLE HLMLLIGELY KKNPFHLELA LEYWCPSEPL QTPTVMGSYL
     GVAHQRPPQR QVVLSKFVRQ MGDLLPPTIY IPYLKMLQGL ANGPQCAHYC FSLLKVNGSS
     HVENIQGAGG SPVSWEHFFH SLLLYHEHLR KDLPSADSVQ YRHLPSRGIT QKEQDGLIAF
     LQLTSTIITW SENARLALCE HPQWTPVVVI LGLLQCSIPP VLKAELLKTL AAFGKSPEIA
     ASLWQSLEYT QILQTVRVPS QRQAIGIEVE LNEIESRCEE YPLTRAFCQL ISTLVESSFP
     SNLGAGLRPP GFDPYLQFLR DSVFLRFRTR AYRRAAEKWE VAEVVLEVFY KLLRDYEPQL
     EDFVDQFVEL QGEEIIAYKP PGFSLMYHLL NESPMLELAL SLLEEGVKQL DTYAPFPGKK
     HLEKAVQHCL ALLNLTLQKE NLFMDLLRES QLALIVSPLE QLLQGINPRT KKADNVVNIA
     RYLYHGNNNP ELAFESAKIL CCISCNSNIQ VKMVGDFTHD QSVSQKLMAG FVECLDYEDT
     EEFVRVEEGS ELEKKLAAIR HETRIHILNL LITSLERNPP NLALYLLGFE LKKPISTTNL
     QDPGVLGCPR TCLHAILNIL EKGTEGRDGP VAVREYPQLA DLCYQVIYQL CACSDTSGPT
     MRYLRTSQDF LFSQLQHLPF SNKEHEISML SQMSWLMKTA SIELRVTSLN RQRSHTQRLL
     HLLLDDMPVK PYSDGEGGME DENRSVSGFL HFDTATKVRR KILSILDSID FSQEIPEPLQ
     LDFFDRAQIE QVIANCEHKN LQGQTVCNVK LLHRVLVAEV NALQGMAAIG QRPLLMEEIS
     TILQYVVGRN KLLQCLHAKR HALESWRQLV EIILTACPQE LIQAEDRQLI IRDLLQDVHD
     KVLDDEAAQE LMPVVAGAVF TLTAHLSQAV RTEQRQPLVS GPGEAQYAFM LDSSLTSSPA
     AESRPVGFAS IGDSSLHIIL KKLLDFILKT GGGFQRVRTH LYGSLLYYLQ IAQRPDEPDT
     LEAAKKTMWE RLTAPEDVFS KLQRENMAII ESYGAALMEV VCRDACDGHE IGRMLALALL
     DRIVSVDKQH QWLLYLSNSG YLKVLVDSLV DDDRTLQSLL TPQPPLLKAL YTYESKMAFL
     TRVAKEQQGS AELLRSGVIV RLAQCQVYDM RPEMDSHGMF GMRDPPVFIP TPVDRYRQIL
     LPALQLCQVI LTSSMSQHLQ AAGQVLQFLV SHSDTIQAIL RCQDVSTGSL QELALLTGII
     SKAALPGMLS ELDVDVNEGS LMELHGHIAR FQRQCLGLLS RFGGADRLRQ FKFQDNNAEG
     DRVSKKDEIE LAMQQICANV MEYCQSFIQQ NSSNLQSAAM CLFTPSLSET VNRDGARQDT
     QVPVVPYWRL PGLGIIIYLL KQSATDFFSY YDSHRRSVNK LQNVEQLPPD EIKELCQSVM
     PAGIDKISTA QKCVLARRRL VKLINNRAKL LSLCSYIIET CLFILWRHLE YYLLHCTPMD
     SQDSLFASRT LFKSRRLQEP NLDFRSGLSQ VNQHDIDQLQ SDAVNAFGES LQKKLLDIEG
     LYSKVRSRYS FIQALIRRIR GLLRLSRN
//
ID   B9EJ80_MOUSE            Unreviewed;      1147 AA.
AC   B9EJ80;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 21.
DE   SubName: Full=PDZ domain containing 8;
GN   Name=Pdzd8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
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DR   EMBL; BC141370; AAI41371.1; -; mRNA.
DR   EMBL; BC141371; AAI41372.1; -; mRNA.
DR   IPI; IPI00273491; -.
DR   RefSeq; NP_001028394.2; NM_001033222.3.
DR   UniGene; Mm.268797; -.
DR   UniGene; Mm.361919; -.
DR   UniGene; Mm.480392; -.
DR   ProteinModelPortal; B9EJ80; -.
DR   PRIDE; B9EJ80; -.
DR   Ensembl; ENSMUST00000099274; ENSMUSP00000096880; ENSMUSG00000074746.
DR   GeneID; 107368; -.
DR   KEGG; mmu:107368; -.
DR   CTD; 107368; -.
DR   MGI; MGI:2677270; Pdzd8.
DR   HOGENOM; HBG717111; -.
DR   HOVERGEN; HBG082118; -.
DR   OMA; ENKHSFQ; -.
DR   OrthoDB; EOG4QVCBF; -.
DR   Bgee; B9EJ80; -.
DR   Genevestigator; B9EJ80; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Zinc.
SQ   SEQUENCE   1147 AA;  127739 MW;  70674471242ADD1B CRC64;
     MGLLLLILAS AVLGSFLTLL AQFLLLYRRQ PEPRADEAAR AGDGFRYLKP VPGLPLREYL
     YGGGAEELAA CSSEAGASST PTPDSPAPPT LETCYFLNAT ILFLFRELRD TALARRWVTK
     KIKVEFEELL QTKTAGRLLE GLSLRDVFLG DTVPFIKTIR LVRPVVASGT GEPDDPDGDA
     LPATCPEELA FEAEVEYNGG FHLAIDVDLV FGKSAYLFVK LSRVVGRLRF VLTRVPFTHW
     FFSFVEDPLI DFEVRSQFEG RPMPQLTSII VNQLKKIIKR KHTLPSYKIR FKPFFPYQAL
     QGFEEDEELI HIQQWALTEG RLKVTLLECS RLFIFGSYDR ETNVHCTLEL SSGVWEEKQR
     SSIKTVELIK GNLQSVGLTL RLVQSTDGYA GHVIIETVAP NSPAAMADLQ RGDRLIAIGG
     VKITSTLQVL KLIKQAGDRV LVYYQRPAGQ SSQDSLGQLE ESFLSSSCQA AYEEDAAGLS
     ADTENRDLDS EFEDLASDVR VQTELKEETQ PLSHSPKRTP TTLSIKPLGA ISPVLNRKLI
     SGIHPPPQKL PSKEGNKPST LKTSETTEAA QVSKPQGPTF KPPVPPRPQG RVPLPPTDTS
     AQADPEAPEK PDKVLLPPPP ADKPAEKQVK SVDQGEDVAA GKQSSAKQEG VKDLPSESSA
     PTKDSSDDPQ MWESSEVLYR NKVGKWSRTR ASCVFDIEAC HRYLNIALWC RDPFKLGGLI
     CLGHVSLKLE EVALGCLATS NMEYLTKFRL EPPTPKAMVT RTALRNLSMQ KGFNDKFCFG
     DITIHFKYLK EGEPDHHIVP NVEKEKELHL VEEVSTLPKE EHFVGQMSLS ENKHSFQDTQ
     FQNPTWCDYC KKKVWTKAAS QCMFCAYVCH KKCQEKCLAE TPLCGATERR IDRTLKNLRL
     EGQDPLLGLP PRVEIEANKS VNKTTGLTRH IINTSSRLLN LRQVSKTRLS EPGTDLVEPS
     PKHTPNTSDN EGSDTEVCGS NSPSKRGNSA GIKLMRKEGG LDDSVFIAVK EIGRDLYRGL
     PTEERIQKLE FMLDKLQNEI DQELEHNNSL VREEKETNDT RKKSVLSAAL AKSGERLQAL
     TLLMIHYRAG IEDIETLENL SLDQHSKKMN KYADDTEEDL DSEISQLIDS QPFSNISDDL
     FGPSESV
//
ID   B9EJ86_MOUSE            Unreviewed;       889 AA.
AC   B9EJ86;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 19.
DE   RecName: Full=Oxysterol-binding protein;
GN   Name=Osbpl8; ORFNames=mCG_21329;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the OSBP family.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; BC141383; AAI41384.1; -; mRNA.
DR   EMBL; CH466539; EDL21721.1; -; Genomic_DNA.
DR   IPI; IPI00461290; -.
DR   RefSeq; NP_780698.2; NM_175489.3.
DR   UniGene; Mm.220204; -.
DR   PRIDE; B9EJ86; -.
DR   Ensembl; ENSMUST00000105275; ENSMUSP00000100911; ENSMUSG00000020189.
DR   GeneID; 237542; -.
DR   KEGG; mmu:237542; -.
DR   CTD; 237542; -.
DR   MGI; MGI:2443807; Osbpl8.
DR   HOGENOM; HBG446335; -.
DR   HOVERGEN; HBG053375; -.
DR   OMA; VTGEWHY; -.
DR   OrthoDB; EOG45TCMJ; -.
DR   PhylomeDB; B9EJ86; -.
DR   Bgee; B9EJ86; -.
DR   Genevestigator; B9EJ86; -.
DR   GO; GO:0008202; P:steroid metabolic process; IEA:InterPro.
DR   InterPro; IPR000648; Oxysterol-bd.
DR   InterPro; IPR018494; Oxysterol-bd_CS.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   PANTHER; PTHR10972; Oxysterol_bd; 1.
DR   Pfam; PF01237; Oxysterol_BP; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS01013; OSBP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Lipid transport; Transport.
SQ   SEQUENCE   889 AA;  101269 MW;  01565BEBAD48553C CRC64;
     MEAALADGEP DRSSLLGDSK DVLGPSTVVA NSDEPQHLTP GKMSQRQGRD ANPTPTRDLP
     QPSLSPASLH SQGFERGKED ISQNKDDSSL SMSKSKSESK LYNGSEKDSS TSSKLTKKES
     LKVQKKNYRE EKKRATKELL STITDPSVIV MADWLKIRGT LKSWTKLWCV LKPGVLLIYK
     TQKNGQWVGT VLLNACEIIE RPSKKDGFCF KLFHPLEQSI WAVKGPKGEA VGSITQPLPS
     SYLIIRATSE SDGRCWMDAL ELALKCSSLL KRTMVREGKE HDLSISSDST HVTLYGLLRA
     NNLHSGDNFQ LNDSEIERQH FKDQDLYSDK SDKENDPEHD ESDNEVLGKS EESDTDTSER
     QDDSYIDPEP VEPLKETTYM EQSHEELGEA GEASQTETVS EENKSLIWTL LKQVRPGMDL
     SRVVLPTFIL EPRSFLDKLS DYYYHADFLS EAALEENPYF RLKKVVKWYL SGFYKKPKGL
     KKPYNPILGE TFRCLWIHPR TNSKTFYIAE QVSHHPPISA FYVSNRKDGF CLSGSILAKS
     KFYGNSLSAI LEGEARLTFL NRGEDYVMTM PYAHCKGILY GTMTLELGGT VNITCQKTGY
     SAILEFKLKP FLGSSDYVNQ ISGKLKLGKE VLATLEGHWD SEVFINDKKT DNSEIFWNPT
     PDIKQWRLIR HTVKFEEQDD FESEKLWQRV TKAINAKDQT EATQEKYVLE EAQRQAARDR
     KTKTQEWVCK LFELDPLTGE WHYKFSDTRP WDPLNDMIQF EKDGVIQTKV KHRTPMVSVP
     KMKHKPTRQQ KKVVKGYSSP EPDIQDSSGS EAQSVKPSTR RKKGIDLGDI QSSIESIKQT
     QEEIKRNIMA LRNHLLSSTP ATDYFLQQKD YFVIFLLILL QVIINFIFK
//
ID   B9EJA2_MOUSE            Unreviewed;      1650 AA.
AC   B9EJA2;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 17.
DE   SubName: Full=Cttnbp2 protein;
GN   Name=Cttnbp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; BC141407; AAI41408.1; -; mRNA.
DR   IPI; IPI00672924; -.
DR   UniGene; Mm.480377; -.
DR   Ensembl; ENSMUST00000090601; ENSMUSP00000088089; ENSMUSG00000000416.
DR   MGI; MGI:1353467; Cttnbp2.
DR   HOGENOM; HBG444762; -.
DR   HOVERGEN; HBG073485; -.
DR   Bgee; B9EJA2; -.
DR   Genevestigator; B9EJA2; -.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR019131; Cortactin-binding_p2_N.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 2.
DR   Pfam; PF00023; Ank; 3.
DR   Pfam; PF09727; CortBP2; 2.
DR   SMART; SM00248; ANK; 6.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
PE   2: Evidence at transcript level;
KW   ANK repeat; Repeat.
SQ   SEQUENCE   1650 AA;  178948 MW;  E9C4F367850E5DF6 CRC64;
     MATDSASCEP DLSRTPGDTE GATAEAAKKE FDVDTLSKSE LRMLLSVMEG ELEARDLVIE
     ALRARRKEVF IQERYGRFNL NDPFLALQRD YEAGPGDKEK PVCTNPLSIL EAVMAHCRKM
     QERMSAQLVA AESRQKKLEM EKLQLQALEQ EHKKLAAHLE EERGKNKHVV LMLVKECKQL
     SGKVVEEAQK LEEVMAQLEE EKKKTSELEE QLSAEKQRSS GMEAQLEKQL SEFDTEREQL
     RAKLSREEAH TTDLKEEIDK MKKMMEQMKK GSDGKPGLSL PRKTKDKRLA SISVATEGPV
     TRSVACQTDV VTESTDPVKK LPLTVPIKPS TGSPLVPTNT KGNVGPSALL IRPGIDRQSS
     HSDLGPSPPT ALPSSANRIE ENGPSTGNAP DLSNSTPSTP SSTAPAAAQT PGTAPQNHSQ
     APTVHSLHSP CANTHPGLNP RIQAARFRFQ GNANDPDQNG NNTQSPPSRD VSPTSRDNLV
     AKQLARNTVT QALSRFTSPQ AGASSRLGVS PGGDAGTCPP VGRTGLKTPG AARVDRGNPP
     PIPPKKPGLS QTPSPPHPQL RASNAGAKVD NKIVASPPST LPQGTKVVNE ENVPKSSSPQ
     LPPKPSIDLT VAPAGCPVSA LATSQVGAWP AGTPGLNQPA CSDSSLVIPA TVAFCSSINP
     VSASSRSPGA SDSLLVAASG WSPSLTPLLM SGGPAPLAGR PTLLQQAAAQ GNVTLLSMLL
     NEEGLDINYS CEDGHSALYS AAKNGHTDCV RLLLNAEARV DAADKNGFTP LCVAAAQGHF
     ECIELLTAYN ANINHSAAGG QTPLYLACKN GNKECIKLLL EAGTDRSIKT RDGWTPIHAA
     VDTGNVDSLK LLMYHRVRAH GNSLSSEEPK SGLFSLNGGE SPTGPSKPVV PADLINHADK
     EGWTAAHIAA SKGFKNCLEV LCRHGGLEPE RRDKCNRTVH DVATDDCKHL LENLNALKIP
     LRISVGEIQP SNDVSDDFEC EHTICTLNIR KQTSWEDFSK AVSQALTNHF QAISSDGWWS
     LEDGTFNNAT DSCIGLGTSS IRSIMLGSMP WSTGQSFSQS PWDFLKKKKV EQVLALLSGP
     QEGCLSSVTY ASMIPLQMLQ NYLRLVEQYH NVIFHGPEGS LQDYIANQLA LCMKYRQMAA
     GFPCEIVRAE VDSGFSKEQL VDVFIRNACL IPVKQFPVKK KIIVILENLE KSSLSELLGD
     FLAPLENRST ESPCTFQKGN GTSECYYFHE NCFLVGTIAK ACLQGSDLLV QQHFRWVQLR
     WDCEPIQGLL QRFLRRKVVS KFRGQLPAPC DPVCKIVDWA LSVWRQLNSC LARLGTPEAL
     LGPKYFLSCP VVPGHAQATV KWMSKLWNAV IAPRVQEAIL SRASMNKQPG TGQTASKKYP
     SQGQQAVVRA ALSILLNKAV LHGCPLPRAE LDQQIADFKG GSFPLSIVSS YSKKKVESGA
     WRKVNTSPRK KPGHFSSPTW NKPDPKREGM RNKTIPHLNT NRNSSLSKQQ SLENDLSVTL
     TLDHRLSLGS DDEADLVKEL QSMCSSKSES DISKIADSRD DLRKFDSSRT NPGTSAPLNL
     RTPVPQKEAS PPSSRQTAEC SNSKSKTEMG VSSVKSFLPV PRSKVAQCSQ NTKRNSSSSS
     SNTRQLEINN NSKEENWTLD KHEQVEKPNK
//
ID   B9EJA3_MOUSE            Unreviewed;      1508 AA.
AC   B9EJA3;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 22.
DE   SubName: Full=Protein tyrosine phosphatase, receptor type, D;
GN   Name=Ptprd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
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DR   EMBL; BC141409; AAI41410.1; -; mRNA.
DR   IPI; IPI00465836; -.
DR   RefSeq; NP_035341.2; NM_011211.2.
DR   UniGene; Mm.184021; -.
DR   UniGene; Mm.403663; -.
DR   ProteinModelPortal; B9EJA3; -.
DR   PRIDE; B9EJA3; -.
DR   Ensembl; ENSMUST00000072540; ENSMUSP00000072353; ENSMUSG00000028399.
DR   GeneID; 19266; -.
DR   KEGG; mmu:19266; -.
DR   CTD; 19266; -.
DR   MGI; MGI:97812; Ptprd.
DR   HOVERGEN; HBG053758; -.
DR   Bgee; B9EJA3; -.
DR   Genevestigator; B9EJA3; -.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 7.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF07679; I-set; 3.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00408; IGc2; 3.
DR   SMART; SM00194; PTPc; 2.
DR   SUPFAM; SSF49265; FN_III-like; 4.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   2: Evidence at transcript level;
KW   Hydrolase; Protein phosphatase; Receptor.
SQ   SEQUENCE   1508 AA;  169744 MW;  5D4D09C127769C79 CRC64;
     MPLTNCRMVP VARPLSLLLT FFLCACAETP PRFTRTPVDQ TGVSGGVASF ICQATGDPRP
     KIVWNKKGKK VSNQRFEVIE FDDGSGSVLR IQPLRTPRDE AIYECVASNN VGEISVSTRL
     TVLREDQIPR GFPTIDMGPQ LKVVERTRTA TMLCAASGNP DPEITWFKDF LPVDTSNNNG
     RIKQLRSESI GGTPIRGALQ IEQSEESDQG KYECVATNSA GTRYSAPANL YVRELREVRR
     VPPRFSIPPT NHEIMPGGSV NITCVAVGSP MPYVKWMLGA EDLTPEDDMP IGRNVLELND
     VRQSANYTCV AMSTLGVIEA IAQITVKALP KPPGTPVVTE STATSITLTW DSGNPEPVSY
     YIIQHKPKNS EEPYKEIDGI ATTRYSVAGL SPYSDYEFRV VAVNNIGRGP ASEPVLTQTS
     EQAPSSAPRD VQARMLSSTT ILVQWKEPEE PNGQIQGYRV YYTMDPTQHV NNWMKHNVAD
     SQITTIGNLV PQKTYSVKVL AFTSIGDGPL SSDIQVITQT GVPGQPLNFK AEPESETSIL
     LSWTPPRSDT IASYELVYRD GDQGEEQRIT IEPGTSYRLQ GLKPNSLYYF RLSARSPQGL
     GASTAEISAR TMQSMFAKNF HVKAVMKTSV LLSWEIPENY NSAMPFKILY DDGKMVEEVD
     GRATQKLIVN LKPEKSYSFV LTNRGNSAGG LQHRVTAKTA PDVLRTKPAF IGKTNLDGMI
     TVQLPDVPAN ENIKGYYIII VPLKKSRGKF IKPWESPDEM ELDELLKEIS RKRRSIRYGR
     EVELKPYIAA HFDVLPTEFT LGDDKHYGGF TNKQLQSGQE YVFFVLAVMD HAESKMYATS
     PYSDPVVSMD LDPQPITDEE EGLIWVVGPV LAVVFIICIV IAILLYKRKR AESESRKSSL
     PNSKEVPSHH PTDPVELRRL NFQTPGMASH PPIPILELAD HIERLKANDN LKFSQEYESI
     DPGQQFTWEH SNLEVNKPKN RYANVIAYDH SRVLLSAIEG IPGSDYVNAN YIDGYRKQNA
     YIATQGSLPE TFGDFWRMIW EQRSATVVMM TKLEERSRVK CDQYWPSRGT ETHGLVQVTL
     LDTVELATYC VRTFALYKNG SSEKREVRQF QFTAWPDHGV PEHPTPFLAF LRRVKTCNPP
     DAGPMVVHCS AGVGRTGCFI VIDAMLERIK HEKTVDIYGH VTLMRAQRNY MVQTEDQYIF
     IHDALLEAVT CGNTEVPARN LYAYIQKLTQ IETGENVTGM ELEFKRLASS KAHTSRFISA
     NLPCNKFKNR LVNIMPYEST RVCLQPIRGV EGSDYINASF LDGYRQQKAY IATQGPLAET
     TEDFWRMLWE HNSTIVVMLT KLREMGREKC HQYWPAERSA RYQYFVVDPM AEYNMPQYIL
     REFKVTDARD GQSRTVRQFQ FTDWPEQGVP KSGEGFIDFI GQVHKTKEQF GQDGPISVHC
     SAGVGRTGVF ITLSIVLERM RYEGVVDIFQ TVKMLRTQRP AMVQTEDQYQ FCYRAALEYL
     GSFDHYAT
//
ID   T229A_MOUSE             Reviewed;         371 AA.
AC   B9EJI9;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 14.
DE   RecName: Full=Transmembrane protein 229A;
GN   Name=Tmem229a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the TMEM229 family.
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DR   EMBL; BC147241; AAI47242.1; -; mRNA.
DR   EMBL; BC147242; AAI47243.1; -; mRNA.
DR   IPI; IPI00830492; -.
DR   RefSeq; NP_795987.2; NM_177013.3.
DR   UniGene; Mm.127446; -.
DR   PRIDE; B9EJI9; -.
DR   Ensembl; ENSMUST00000127247; ENSMUSP00000116234; ENSMUSG00000048022.
DR   GeneID; 319832; -.
DR   KEGG; mmu:319832; -.
DR   CTD; 319832; -.
DR   MGI; MGI:2442812; Tmem229a.
DR   GeneTree; ENSGT00390000010899; -.
DR   HOVERGEN; HBG087807; -.
DR   OrthoDB; EOG4Q84XZ; -.
DR   Bgee; B9EJI9; -.
DR   Genevestigator; B9EJI9; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    371       Transmembrane protein 229A.
FT                                /FTId=PRO_0000391849.
FT   TRANSMEM     51     71       Helical; (Potential).
FT   TRANSMEM    117    137       Helical; (Potential).
FT   TRANSMEM    235    255       Helical; (Potential).
FT   TRANSMEM    269    289       Helical; (Potential).
FT   TRANSMEM    301    321       Helical; (Potential).
FT   TRANSMEM    334    354       Helical; (Potential).
SQ   SEQUENCE   371 AA;  41526 MW;  AAF56AAD640AFAFA CRC64;
     MAGSDVASEG PSPRDGATRR PGATGGLRSQ AAASCPEPLS AAEAPAERGA LPAWMRLYFY
     GMHGITLDVL VSSARRFARS LDLRMLGFSS PYRCLLHSLT HFALEQLYLQ RPRCPSAFLF
     NFLLYPSAHV GLQTLAGQAL RLSLGGGPGG AAAPALGALD LALQYVLALY HGQVFLKRFL
     CLRYPRRRDQ HTRDTLPAAR DAQILWEAGG QRRGPGGARG TERSPTQGLP DLLRFLFFGM
     HGFLDEIFFT FFFNVLGQGD RASSGHTSLW SFFMYGSCSF VVEKLYFHLH YSRGWGTWKR
     VPIYVIFIYA WEFSWGLGLR MCGACSWDYS HYPLNFMGLI TLMYLPGWLF LSVYQDLLSN
     VLWRVQYVPT N
//
ID   B9EJW3_MOUSE            Unreviewed;      1321 AA.
AC   B9EJW3;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 17.
DE   SubName: Full=Insulin receptor substrate 2;
GN   Name=Irs2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 PH domain.
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DR   EMBL; BC147580; AAI47581.1; -; mRNA.
DR   IPI; IPI00923679; -.
DR   RefSeq; NP_001074681.1; NM_001081212.1.
DR   UniGene; Mm.407207; -.
DR   Ensembl; ENSMUST00000040514; ENSMUSP00000038514; ENSMUSG00000038894.
DR   GeneID; 384783; -.
DR   KEGG; mmu:384783; -.
DR   CTD; 384783; -.
DR   MGI; MGI:109334; Irs2.
DR   HOVERGEN; HBG000542; -.
DR   Bgee; B9EJW3; -.
DR   Genevestigator; B9EJW3; -.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0019901; F:protein kinase binding; IDA:MGI.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007420; P:brain development; IMP:MGI.
DR   GO; GO:0008283; P:cell proliferation; IMP:MGI.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IMP:MGI.
DR   GO; GO:0030879; P:mammary gland development; IGI:MGI.
DR   GO; GO:0030335; P:positive regulation of cell migration; IGI:MGI.
DR   GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IGI:MGI.
DR   InterPro; IPR002404; Insln_rcpt_S1.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Pfam; PF02174; IRS; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00628; INSULINRSI.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00310; PTBI; 1.
DR   PROSITE; PS51064; IRS_PTB; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Receptor.
SQ   SEQUENCE   1321 AA;  136763 MW;  823A5458DA21C9C7 CRC64;
     MASAPLPGPP ASAGGDGPNL NNNNNNNNHS VRKCGYLRKQ KHGHKRFFVL RGPGTGGDEA
     SAAGGSPPQP PRLEYYESEK KWRSKAGAPK RVIALDCCLN INKRADAKHK YLIALYTKDE
     YFAVAAENEQ EQEGWYRALT DLVSEGRSGE GGSGTTGGSC SASLPGVLGG SAGAAGCDDN
     YGLVTPATAV YREVWQVNLK PKGLGQSKNL TGVYRLCLSA RTIGFVKLNC EQPSVTLQLM
     NIRRCGHSDS FFFIEVGRSA VTGPGELWMQ ADDSVVAQNI HETILEAMKA LKELFEFRPR
     SKSQSSGSSA THPISVPGAR RHHHLVNLPP SQTGLVRRSR TDSLAATPPA AKCTSCRVRT
     ASEGDGGAAG GAGTAGGRPM SVAGSPLSPG PVRAPLSRSH TLSAGCGGRP SKVTLAPAGG
     ALQHSRSMSM PVAHSPPAAT SPGSLSSSSG HGSGSYPLPP GSHPHLPHPL HHPQGQRPSS
     GSASASGSPS DPGFMSLDEY GSSPGDLRAF SSHRSNTPES IAETPPARDG SGGELYGYMS
     MDRPLSHCGR PYRRVSGDGA QDLDRGLRKR TYSLTTPARQ RQVPQPSSAS LDEYTLMRAT
     FSGSSGRLCP SFPASSPKVA YNPYPEDYGD IEIGSHKSSS SNLGADDGYM PMTPGAALRS
     GGPNSCKSDD YMPMSPTSVS APKQILQPRL AAALPPSGAA VPAPPSGVGR TFPVNGGGYK
     ASSPAESSPE DSGYMRMWCG SKLSMENPDP KLLPNGDYLN MSPSEAGTAG TPPDFSAALR
     GGSEGLKGIP GHCYSSLPRS YKAPCSCSGD NDQYVLMSSP VGRILEEERL EPQATPGAGT
     FGAAGGSHTQ PHHSAVPSSM RPSAIGGRPE GFLGQRCRAV RPTRLSLEGL QTLPSMQEYP
     LPTEPKSPGE YINIDFGEAG TRLSPPAPPL LASAASSSSL LSASSPASSL GSGTPGTSSD
     SRQRSPLSDY MNLDFSSPKS PKPSTRSGDT VGSMDGLLSP EASSPYPPLP PRPSTSPSSL
     QQPLPPAPGD LYRLPPASAA TSQGPTAGSS MSSEPGDNGD YTEMAFGVAA TPPQPIVAPP
     KPEGARVASP TSGLKRLSLM DQVSGVEAFL QVSQPPDPHR GAKVIRADPQ GGRRRHSSET
     FSSTTTVTPV SPSFAHNSKR HNSASVENVS LRKSSEGSST LGGGDEPPTS PGQAQPLVAV
     PPVPQARPWN PGQPGALIGC PGGSSSPMRR ETSVGFQNGL NYIAIDVRGE QGSLAQSQPQ
     PGDKNSWSRT RSLGGLLGTV GGSGASGVCG GPGTGALPSA STYASIDFLS HHLKEATVVK
     E
//
ID   B9EKC3_MOUSE            Unreviewed;      1503 AA.
AC   B9EKC3;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 17.
DE   SubName: Full=Rho GTPase activating protein 5;
GN   Name=Arhgap5; ORFNames=mCG_14971;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC150823; AAI50824.1; -; mRNA.
DR   EMBL; CH466526; EDL36765.1; -; Genomic_DNA.
DR   IPI; IPI00124298; -.
DR   UniGene; Mm.35059; -.
DR   UniGene; Mm.474991; -.
DR   Ensembl; ENSMUST00000110725; ENSMUSP00000106353; ENSMUSG00000035133.
DR   MGI; MGI:1332637; Arhgap5.
DR   HOGENOM; HBG444653; -.
DR   HOVERGEN; HBG051844; -.
DR   OrthoDB; EOG4PK26Z; -.
DR   Bgee; B9EKC3; -.
DR   Genevestigator; B9EKC3; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:MGI.
DR   GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:MGI.
DR   GO; GO:0008361; P:regulation of cell size; IMP:MGI.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR002713; FF_domain.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF01846; FF; 1.
DR   Pfam; PF00071; Ras; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00441; FF; 4.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
SQ   SEQUENCE   1503 AA;  172444 MW;  392912ECF120E485 CRC64;
     MMAKNKEPRP PSYTVSVVGL SGTEKDKGNC GVGKSCLCNR FVRSKADEYY PEHTSVLSTI
     DFGGRVVNND HFLYWGDITQ NGEDGVECKI HVIEQTEFID DQTFLPHRST NLQPYIKRAA
     ASKLQSAEKL MYICTDQLGL EQDFEQKQMP EGKLNVDGFL LCIDVSQGCN RKFDDQLKFV
     NNLFVQLSKS KKPVIIAATK CDECVDHYLR EVQAFASNKK NLLVVETSAR FNVNIETCFT
     ALVQMLDKTR GKPKIIPYLD AYKTQRQLVV TATDKFEKLV QTVRDYHATW KTVSNKLKNH
     PDYEEYINLE GTRKARNTFS KHIEQLKQEH IRKRREEYIS TLPRAFNTLL PDLEEIEHLN
     WLEALKLMEK RADFQLCFVV LEKTPWDETD HIDKINDRRI PFDLLSTLEA EKVYQNHVQH
     LISEKRRIEM KEKFKKTLEK IQFISPGQPW EEVMCFVMED EAFKYITEAD SKEVYGRHQR
     EIVEKAKEEF QEMLFEHSEL FYDLDLNATP SSDKMSEIHT VLSEEPRYKA LQKLAPDRES
     LLLKHIGFVY HPTKETCLSG QYCTDIKVEN LLATSLLEMD HNRVRLYHDS TNIDKVNLFI
     LGKDGLAQEL ANEIRTQSTD DEYALDGKIY ELDLRPVDAK SPYILSQLWT AAFKPHGCFC
     VFNSIESLSF IGEFIGKIRT EASQIRKDKY MTNLPFTLIL ANQRDSISKN LPILRHQGQQ
     LANKLQCPFV DVPTGTYPRK FNESQIKQAL RGVLESVKHN LDVVSPVPIN KDVSEADLRI
     VMCAMCGDPF SVDLILSPFL DSHSCSAAQA GQNNSLMLDK IIGEKRRRIQ ITILSYHSSI
     GVRKDELVHG YILVYSAKRK ASMGMLRAFL SEVQDTIPVQ LVAVTDSQAD FFENEAIKEL
     MTEGEHIATE ITAKFTALYS LSQYHRQTEV FTLFFSDVLE KKNMIENSYL SDNTRESTHQ
     SEDVFLPSPR DCFPYNNYPD SDDDTEAPPP YSPIGDDVQL LPTPSDRSRY RLDLEGNEYP
     VHSTPNCHDH ERNHKVPPPI KPKPVVPKTN VKKLDPNLLK TIEAGIGKNP RKQTSRVPLA
     HPEDMDSSDN YAEPLDTIFK QKGYSDEIYV VPDDSQNRII KIRNSFVNNT QGDEENGFSD
     RTSKGHGERR PSKYKYKSKT LFSKAKSYYR RTHSDASDDE AFTTSKTKRK GRHRGSEEDP
     LLSPVETWKG GIDNPAITSD QEVDDKKIKK KTHKVKEDKK QKKKTKTFNP PTRRNWESNY
     FGMPLQDLVT AEKPIPLFVE KCVEFIEDTG LCTEGLYRVS GNKTDQDNIQ KQFDQDHNIN
     LASMEVTVNA VAGALKAFFA DLPDPLIPYS LHPELLEAAK IPDKTERFHA LKEIVKKFHP
     VNYDVFRYVI THLNRVSQQN KINLMTADNL SICFWPTLMR PDFENREFLS TTKIHQSVVE
     TFIQQCQFFF YNGEIVETAN TVAPPPTSNP GQLVESMVPL QLPPPLQPQL IQPQLQTDPL
     GII
//
ID   B9EKF4_MOUSE            Unreviewed;       885 AA.
AC   B9EKF4;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 17.
DE   SubName: Full=Zinc finger protein 777;
GN   Name=Zfp777;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC150871; AAI50872.1; -; mRNA.
DR   IPI; IPI00830326; -.
DR   RefSeq; NP_001074851.1; NM_001081382.1.
DR   UniGene; Mm.381553; -.
DR   PRIDE; B9EKF4; -.
DR   Ensembl; ENSMUST00000114583; ENSMUSP00000110230; ENSMUSG00000071477.
DR   GeneID; 72306; -.
DR   KEGG; mmu:72306; -.
DR   CTD; 72306; -.
DR   MGI; MGI:1919556; Zfp777.
DR   HOGENOM; HBG506952; -.
DR   HOVERGEN; HBG108774; -.
DR   OMA; METQRSS; -.
DR   Bgee; B9EKF4; -.
DR   Genevestigator; B9EKF4; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR022137; DUF3669_Znf.
DR   InterPro; IPR001909; Krueppel-associated_box.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 9.
DR   Pfam; PF12417; DUF3669; 1.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF00096; zf-C2H2; 5.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   SUPFAM; SSF109640; Krueppel-associated_box; 1.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE   2: Evidence at transcript level;
KW   Metal-binding; Zinc.
SQ   SEQUENCE   885 AA;  99478 MW;  A993F299F4B4404E CRC64;
     MAEAAPARGR AARARTDARP RGPGDSLRAP GSVARPGVSV QQLDMEDDRS SPLSFSSVPH
     EESVRQAPAR LPRETVFPSC ILPPKEVPPL SPTASRQGVL PQTDSTTKQE TSSQMSHVLQ
     KGPSLLYPAT SEQDTPHQVS LASQEETQCS PSAAAQGIPF LSHSAHRQEA PLHSPEVPEK
     DSLTLSPTVP ETDMDPLLQS PTLQKDTPFH TSSAAQKEQP LPTAEITRLA VWAAVQAVER
     KLEAQAMRLL TLEGRTGTNE KKIADCERTA VEFANHLESK WVVLGTLLQE YGLLQRRLEN
     MENLLKNRNF WILRLPPGSN GEVPKVPVTF DDVAVHFSEQ EWGNLSEWQK ELYKNVMRGN
     YESLVSMDYA ISKPDLMSQM ERGERPAMQE QEDSEEGETP TDPSAAHDGI VIKIEVQTND
     EGSEGLETPE PLMGQVEEHG FQDSELGDPC GEQPDLDMQE QENALEESTE GSSEFSELKQ
     MLVQQRNCTE GIVIKTEEQE EEEEEEEEDE LPQHLQSLGQ LSGRYEASMY QTPLPGEMSP
     EGEESPPPLQ LGNPAVKRLA PSIHGHTHGH GHGHGHSERH LGENRGNSSQ QQRNRRGERP
     FTCMECGKSF RLKINLIIHQ RNHIKEGPYE CAECEISFRH KQQLTLHQRI HRVRSGYASP
     ERGSAFNPKH SLKPRPKSPS SGSGGGPKPY KCPECDSSFS HKSSLTKHQI THTGERPYTC
     PECKKSFRLH ISLVIHQRVH AGKHEVSFIC SLCGKSFSRP SHLLRHQRTH TGERPFKCPE
     CEKSFSEKSK LTNHCRVHSR ERPHACPECG KSFIRKHHLL EHRRIHTGER PYHCAECGKR
     FTQKHHLLEH QRAHTGERPY PCTHCAKCFR YKQSLKYHLR THTGE
//
ID   TMF1_MOUSE              Reviewed;        1091 AA.
AC   B9EKI3; Q3UMH8; Q3UMR3;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 21.
DE   RecName: Full=TATA element modulatory factor;
DE            Short=TMF;
DE   AltName: Full=Androgen receptor coactivator 160 kDa protein;
DE   AltName: Full=Androgen receptor-associated protein of 160 kDa;
GN   Name=Tmf1; Synonyms=Ara160, Gm153;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-619.
RC   TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-413, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Potential coactivator of the androgen receptor. Mediates
CC       STAT3 degradation. May play critical roles in two RAB6-dependent
CC       retrograde transport processes: one from endosomes to the Golgi
CC       and the other from the Golgi to the ER (By similarity).
CC   -!- SUBUNIT: Componement of the SNF/SWI transcription factor complexes
CC       (By similarity). Interacts with RAB6A. Interacts with STAT3 and
CC       FER (By similarity). Interacts with TCEB1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Golgi apparatus membrane (By similarity).
CC       Note=Concentrated at the budding structures localized at the tips
CC       of cisternae (By similarity).
CC   -!- DOMAIN: The Elongin BC complex binding domain is also known as BC-
CC       box with the consensus [APST]-L-x(3)-C-x(3)-[AILV].
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE26035.1; Type=Frameshift; Positions=44;
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DR   EMBL; BC150931; AAI50932.1; -; mRNA.
DR   EMBL; AK144898; BAE26120.1; -; mRNA.
DR   EMBL; AK144729; BAE26035.1; ALT_FRAME; mRNA.
DR   IPI; IPI00668529; -.
DR   RefSeq; NP_001074580.1; NM_001081111.2.
DR   UniGene; Mm.30893; -.
DR   ProteinModelPortal; B9EKI3; -.
DR   PhosphoSite; B9EKI3; -.
DR   Ensembl; ENSMUST00000095664; ENSMUSP00000093325; ENSMUSG00000030059.
DR   GeneID; 232286; -.
DR   KEGG; mmu:232286; -.
DR   CTD; 232286; -.
DR   MGI; MGI:2684999; Tmf1.
DR   eggNOG; roNOG08603; -.
DR   GeneTree; ENSGT00390000010697; -.
DR   HOGENOM; HBG713215; -.
DR   OrthoDB; EOG47M1X4; -.
DR   Bgee; B9EKI3; -.
DR   Genevestigator; B9EKI3; -.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR022092; TMF_DNA-bd.
DR   InterPro; IPR022091; TMF_TATA-bd.
DR   Pfam; PF12329; TMF_DNA_bd; 1.
DR   Pfam; PF12325; TMF_TATA_bd; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Cytoplasm; DNA-binding; Golgi apparatus;
KW   Membrane; Nucleus; Phosphoprotein; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   1091       TATA element modulatory factor.
FT                                /FTId=PRO_0000376797.
FT   REGION      329    338       Interaction with Elongin BC complex (By
FT                                similarity).
FT   COILED      443    767       Potential.
FT   COILED      824    894       Potential.
FT   COILED      984   1090       Potential.
FT   COMPBIAS    235    340       Ser-rich.
FT   COMPBIAS    374    377       Poly-Glu.
FT   MOD_RES     112    112       Phosphoserine (By similarity).
FT   MOD_RES     324    324       Phosphoserine (By similarity).
FT   MOD_RES     334    334       Phosphoserine (By similarity).
FT   MOD_RES     340    340       Phosphoserine.
FT   MOD_RES     360    360       Phosphothreonine (By similarity).
FT   MOD_RES     413    413       Phosphothreonine.
FT   MOD_RES     517    517       N6-acetyllysine (By similarity).
FT   MOD_RES     540    540       Phosphoserine (By similarity).
FT   MOD_RES     864    864       Phosphotyrosine (By similarity).
FT   MOD_RES     875    875       Phosphotyrosine (By similarity).
FT   MOD_RES     923    923       Phosphoserine (By similarity).
FT   MOD_RES     927    927       Phosphothreonine (By similarity).
FT   MOD_RES     931    931       Phosphoserine (By similarity).
FT   CONFLICT    106    106       V -> A (in Ref. 2; BAE26120/BAE26035).
FT   CONFLICT    144    144       A -> V (in Ref. 2; BAE26120/BAE26035).
FT   CONFLICT    161    161       P -> S (in Ref. 2; BAE26120/BAE26035).
FT   CONFLICT    203    203       S -> T (in Ref. 2; BAE26120/BAE26035).
FT   CONFLICT    439    439       L -> P (in Ref. 2; BAE26120/BAE26035).
SQ   SEQUENCE   1091 AA;  121815 MW;  5E4CD79E24844623 CRC64;
     MSWFNASQLS SFAKQALSQA QKSIDRVLDI QEEEPSAWAE AIPYGEPGIS PPVSGGWDTS
     TWGLNSTSSE PQSPPTASQA ITKPVRRTVV DESENFFSAF LSPSDVHTIQ KSPVVSKPPS
     KSQRPEEEVK SSLQESSSPG QSRASETAEV RDSVCVSGET PAVGTPSPVP EDKHEETAGE
     ESEVKVPTVR LKASENVVNV NTSEDVSTTS TQSLTAETKD MALEPKEQKH EDRQSNTPSP
     PVSSFSSGTS TTSDIEVLDH ESVISESSAS SRQETSDAKS SLHLMQTSFQ LLSASACPEY
     SRLDDFQKLN ESCCSSDAFE RIDSFSVQSL DSRSVSEINS DDELPGKGYA LVPIIVSPST
     PKTKVVESTE ENAEEEEGNE TLVAPSEEAE LEESGRSATP VNCDQPDILA SPTAGSGGHS
     ASGPATEQCE AVENQPKALP EKEDVCKTVE FLNEKLEKRE TQLLSLSKEK ALLEEAYDNL
     KDEMFRVKEE SSSISSLKDE FTQRIAEAEK KVQLACKERD AAKKEMKTIK EELATRLNSS
     QTADLLKEKD EQIQGLMEEG EKLSKQQLHN SNIIKKLRAK DKDNENVIAK LNRKAKELEE
     ELQHLRQVLD GKEEVEKQHR ENIKKLNSVV ERQEKDLGRL QVDMDELEEK SRSTQAALDS
     AYRELTDLHK ANAAKDSEVQ EAALRREMKA KEELSGALEK AQEEARQQQE ALVLQVGDLR
     LALQRAEQAA ARKEDYLRHE ISELQQRLQE AENRNQELSQ SVSSTARPLL RQIENLQATL
     GSQTSSWETL EKSLSDRLGE SQTLLAAAVE RERAATEELL ANKIQMSSVE SQNTLLRQEN
     SRLQAQLESE KNKLRKLEDE NSRYQVELEN IKDEYVRTLE ESRKEKTLLS SQLEMERMKV
     EQERKKTIFT QEALKEKDHK LFSVCSTPTM SRSSSISGVD AAGLQASFLS QDESHDHSFG
     PMSTSASGSN LYEAVRMGAG SSIIENLQSQ LKLREGEISH LQLEISNLEK TRSIMSEELV
     KLTNQNDELE EKVKEIPKLR VQLRDLDQRY NTILQMYGEK AEEAEELRLD LEDVKNMYKT
     QIDELLRQRL S
//
ID   B9EKL9_MOUSE            Unreviewed;       801 AA.
AC   B9EKL9;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   02-NOV-2010, entry version 15.
DE   SubName: Full=Eml1 protein;
GN   Name=Eml1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
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DR   EMBL; BC150975; AAI50976.1; -; mRNA.
DR   IPI; IPI00785320; -.
DR   UniGene; Mm.236645; -.
DR   Ensembl; ENSMUST00000109860; ENSMUSP00000105486; ENSMUSG00000058070.
DR   MGI; MGI:1915769; Eml1.
DR   HOVERGEN; HBG051470; -.
DR   Bgee; B9EKL9; -.
DR   Genevestigator; B9EKL9; -.
DR   InterPro; IPR005108; HELP.
DR   InterPro; IPR011047; Quino_AlcDH-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 3.
DR   Pfam; PF03451; HELP; 1.
DR   Pfam; PF00400; WD40; 5.
DR   SMART; SM00320; WD40; 10.
DR   SUPFAM; SSF50998; Quin_alc_DH_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   2: Evidence at transcript level;
KW   Repeat; WD repeat.
SQ   SEQUENCE   801 AA;  88051 MW;  219FBA767AF57C51 CRC64;
     MSDGEGPSAD DSASAASSME VSDRIASLEQ RVQMQEDDIQ LLKSALADVV RRLNITEEQQ
     AVLNRKGPTK ARPLGQTLPL RTTVNNGTVL PKKPSASLPS PSGARKEVVV PVTKSINRTS
     SSERVSPGGR RESSGDSKGS RNRTGSTSSS SSGKKNSESK PKEPAFSPEE GYVKMFLRGR
     PVTMYMPKDQ VDSYSLEAKA ELPTKRLKLE WVYGYRGRDC RNNLYLLPTG ETVYFIASVV
     VLYNVEEQLQ RHYAGHNDDV KCLAVHPDRI TIATGQVAGT SKDGKQLPPH VRIWDSVTLN
     TLHVIGIGFF DRAVTCIAFS KSNGGGHLCA VDDSNDHVLS VWDWQKEERL ADVKCSNEAV
     FAADFHPTDT NIIVTCGKSH LYFWTLEGNS LNKKQGLFEK QEKPKFVLCV TFSENGDTIT
     GDSSGNILVW GKGTNRISYA VQGAHEGGIF ALCMLRDGTL VSGGGKDRRL ISWNGNYQKL
     HKAEIPEQFG PIRTVAEGKG NVILIGTTRN FVLQGTLSGD FTPITQGHTD ELWGLAIHAS
     KPQFLTCGHD KHATLWDAVG HRPVWDKIIE DPAQSSGFHP SGSVVAVGTL TGRWFVFDTE
     TKDLVTVHTD GNEQLSVMRY SPDGNFLAIG SHDNCIYIYG VTDNGRKYTR VGKCSGHSSF
     ITHLDWSVNS QFLVSNSGDY EILYWVPSAC KQVVSVETTR DIEWATYTCT LGFHVFGVWP
     EGSDGTDINA VCRAHERKLL CTGDDFGKVH LFSYPCSQFR APSHIYSGHS SHVTNVDFLC
     EDSHLISTGG KDTSIMQWRV I
//
ID   B9EKR1_MOUSE            Unreviewed;      2312 AA.
AC   B9EKR1;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   08-MAR-2011, entry version 21.
DE   SubName: Full=Protein tyrosine phosphatase, receptor type Z, polypeptide 1;
GN   Name=Ptprz1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
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DR   EMBL; BC151071; AAI51072.1; -; mRNA.
DR   IPI; IPI00627008; -.
DR   RefSeq; NP_001074775.1; NM_001081306.1.
DR   UniGene; Mm.41639; -.
DR   ProteinModelPortal; B9EKR1; -.
DR   PRIDE; B9EKR1; -.
DR   Ensembl; ENSMUST00000090568; ENSMUSP00000088056; ENSMUSG00000068748.
DR   GeneID; 19283; -.
DR   KEGG; mmu:19283; -.
DR   CTD; 19283; -.
DR   MGI; MGI:97816; Ptprz1.
DR   HOGENOM; HBG402895; -.
DR   HOVERGEN; HBG053760; -.
DR   OMA; LAVFCEV; -.
DR   OrthoDB; EOG4CZBDZ; -.
DR   Bgee; B9EKR1; -.
DR   Genevestigator; B9EKR1; -.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   InterPro; IPR001148; Carbonic_anhydrase_a-class_cat.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Gene3D; G3DSA:3.10.200.10; Euk_COanhd; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00194; PTPc; 2.
DR   SUPFAM; SSF51069; Euk_COanhd; 1.
DR   SUPFAM; SSF49265; FN_III-like; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   2: Evidence at transcript level;
KW   Hydrolase; Protein phosphatase; Receptor.
SQ   SEQUENCE   2312 AA;  254405 MW;  91C5D58F74BA999C CRC64;
     MRILQSFLAC VQLLCLCRLD WAYGYYRQQR KLVEEIGWSY TGALNQKNWG KKYPICNSPK
     QSPINIDEDL TQVNVNLKKL KFQGWEKASL ENTFIHNTGK TVEINLTNDY YLSGGLSEKV
     FKASKITFHW GKCNVSSEGS EHSLEGQKFP LEMQVYCFDA DRFSSFEEAV KGKGRLRALS
     ILFEVGVEEN LDYKAIIDGT ESVSRFGKQA ALDPFVLQNL LPNSTDKYYI YNGSLTSPPC
     TDTVEWIVFK DTVSISESQL AVFCEVLTMQ QSGYVMLMDY LQNNFREQQY KFSRQVFSSY
     TGKEEIHEVV CSSEPENVQA DPENYTSLLV TWERPRVVYD AMIEKFAVLY QPLAGNDQAK
     HEFLTDGYQD LGAILNNLLP NMSYVLQIVA VCSNGLYGKY SDQLIVDMPT EDAELDLFPE
     LIGTEEIIKE EEYGKDNEED TGLNPGRDSV TNQIRKKEPQ VSTTTHYNHM GTKYNEAKTN
     RSPTRGSEFS GKSDVPNTSP NSTSQHVAEF ETERGISLPS QTGTNLPPHN VEGTSASLNS
     GSKTLFIFPQ MNLSGTAESL NTVPITEYKE VSADVSEEEN FLTDFKLDTG ADDSSGSSPS
     TSTVPFSSDN LSHGYITSSD MPEAITYDVL KPGSTRNAPE DSAPSGSEES LKDPSLEGSV
     WFPGSTDLTT QSETGSGRES FLQVNSTDIQ IDESRETTES FSPDATVSQD PSVTDMGMPH
     YSTFAYLPTE VTPQAFTPSS RPLDLAPTIN ILHSQTTQPV YNGETPLQPS YSSEVFPLAT
     PLLLDNQTLN TTPAASSSDS ALHATPVSPS VGVSFESILS SYDDAPLLPF SSASFSSEMF
     RHLHTVSQTL PQVTSAAERD ELSLHASLLV ARGDLLLEPS LVQYSDVASH QATTRAASDT
     LGFGSESAVF YKTSMVSQIE SPRSDVVMHA YSSGPEPSYT VEGSHHVPTV SYSSAMPLHG
     SVDVSDQGSL LINPSHISMP ESSFITPTAS LLQPPPALSG DGEWSGASSD SELLLPDADG
     LRTLNISSPV SVAEFTYTTS VFADGIKPLS KSEMMYGNET ELKMSSFSDM AYPSKSTVVP
     KMSDVVHKWS ESLKETSVSI SSMKSVFPES LVYPTTKGFE QGVSHVPEII FPVQPTHTAS
     QASGDTWLKP GLSANSEAAF SDTASREVVH PSTQPLLYEA ATPFNTEALL QPSFQASDVD
     TLLKTALPSV PSDPILAGTP QVEQSSSSVS HPMASESGSS ESMLHFTSVP ILDISPSKVH
     STPLQGLTVP HSSKKFSEQG LLKSKSPQQV LPSLFSNDEF FQSAHLDVSQ AYPPKGRHAF
     VTPVLSIDEP QNTLINKLVY SEDIFSSTEI SITDKVLTGL PTLASDVLSS TDHSVPLGSG
     PISLTMVSPN RDDSVTTAKL LLPSTATSKL TQSARSDADL VGGGEDGDDY DDDDYDDIDR
     GRFPVNKCMS CLPYRESREK VMNDSDTQES SLVDQSDPIS PLLFENTEEE NGGTGVTRVD
     KSPPPSMLPQ NHNDGKEDSD IQMGSAVLPH TPGSKAWAVL TSDEESGSGQ GTSDSLNDNE
     TSTDFSFPDV NEKDTDGVLE TDDTGIAPGS PRSSTPSVTS GHSGVSNSSE AEASNSSHES
     RIGLAEGLES EKKAVIPLVI VSALTFICLV VLVGILIYWR KCFQTAHFYL EDNTSPRVIS
     TPPTPIFPIS DDIGAIPIKH FPKHVADLHA SNGFTEEFET LKEFYQEVQS CTADLGITAD
     SSNHPDNKHK NRYVNIVAYD HSRVKLTQLA EKDGKLTDYI NANYVDGYNR PKAYIAAQGP
     LKSTAEDFWR MIWEHNVEVI VMITNLVEKG RRKCDQYWPT DGSEEYGSFL VNQKSVQVLA
     YYTVRNFTLR NTKLKKGSQK GRSSGRLVTQ YHYTQWPDMG VPEYSLPVLA FVRKAAQAKR
     HAVGPVVVHC SAGVGRTGTY IVLDSMLQQI QHEGTVNIFG FLKHIRSQRN YLVQTEEQYV
     FIHDTLVEAI LSKETEVPDS HIHSYVNTLL IPGPTGKTKL EKQFQLLSQS NILQSDYSTA
     LKQCNREKNR TSSIIPVERS RVGISSLSGE GTDYINASYI MGYYQSNEFI ITQHPLLHTI
     KDFWRMIWDH NAQLVVMIPD GQNMAEDEFV YWPNKDEPIN CESFKVTLMS EEHKCLSNEE
     KLIVQDFILE ATQDDYVLEV RHFQCPKWPN PDSPISKTFE LISIIKEEAA NRDGPMIVHD
     EHGGVTAGTF CALTTLMHQL EKENAMDVYQ VAKMINLMRP GVFTDIEQYQ FLYKVVLSLV
     STRQEENPST SLDSNGAALP DGNIAESLES LV
//
ID   C0KJK2_MOUSE            Unreviewed;       910 AA.
AC   C0KJK2;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   02-NOV-2010, entry version 12.
DE   SubName: Full=Polycystin-2 delta7 variant;
GN   Name=Pkd2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Sv109;
RX   PubMed=16192288; DOI=10.1093/hmg/ddi356;
RA   Hackmann K., Markoff A., Qian F., Bogdanova N., Germino G.G.,
RA   Pennekamp P., Dworniczak B., Horst J., Gerke V.;
RT   "A splice form of polycystin-2, lacking exon 7, does not interact with
RT   polycystin-1.";
RL   Hum. Mol. Genet. 14:3249-3262(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Sv109;
RA   Hackmann K., Markoff A., Qian F., Bogdanova N., Germino G.G.,
RA   Pennekamp P., Dworniczak B., Horst J., Gerke V.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FJ609779; ACN11624.1; -; mRNA.
DR   IPI; IPI00884540; -.
DR   UniGene; Mm.6442; -.
DR   Genevestigator; C0KJK2; -.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR013122; PKD1_2_channel.
DR   InterPro; IPR003915; PKD_2.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF08016; PKD_channel; 1.
DR   PRINTS; PR01433; POLYCYSTIN2.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   910 AA;  102421 MW;  B0C78883A583AB11 CRC64;
     MVNSRRVQPQ PPGDAGRSPA PRASGPGRLV AGGAGLAVPG GLGEQRGLEI EMERIRQAAA
     RDPPAGASAS PSPPLSSCSR QAWSRDNPGF EAEEDDDDDE VEGEEGGMVV EMDVEWRPGS
     RRSASSSAVS SVGARGRGLG SYRGAAHLSG RRRRLEDQGA QCPSPAGGGD PLHRHLPLEG
     QPPRVAWAER LVRGLRGLWG TRLMEESNAN REKYLKSVLR ELVTYLFFLV VLCILTYGMM
     SSNVYYYTRT LSQLFIDTPV SKTEKTNFKT LSSMEDFWKF TEGSFLDGLY WKAQTSNHTQ
     ADNRSFIFYE NLLLGVPRLR QLRVRNGSCS IPQDLRDEIK ECYDVYSVSS EDRAPFGPRN
     GTAWMYTSEK ELNGSSHWGI IASYSGAGYY LDLSRTREET AAQLAGLRRN FWLDRGTRAA
     FIDFSVYNAN INLFCVVRLL AEFPATGGVV PSWQFQPVKL IRYVTAFDFF LAACEIIFCF
     FIIYYVVEEI LEIRIHRLSY FRSFWNCLDV VIVVLFKFIN FNRTMSQLST TMSRCAKDLF
     GFTIMFSIIF LAYAQLAYLV FGTQVDDFST FQECIFTQFR IILGDINFAE IEEANRVLGP
     LYFTTFVFFM FFILLNMFLA IINDSYSEVK SDLAQQKAEM ELSDLIRKGC QKALVKLKLK
     RNTVDAISES LRQGGGKLNF DELRQDLKGE GHTDAEIEAI FTKYDQDGDQ ELTEREHQQM
     RDDLEKERED LDLEHSSLPR PMSSRSFPRS LDDSEEEDDE DSGHSSRRRG SISSGVSYEE
     FQVLVRRVDR MEHSIGSIVS KIDAVIVKLE IMERAKLKRR EVLGRLLDGV AEDARLGRDS
     EIHREQMERL VREELERWES DDAASQTGHG VSTQVGLGGQ PHPRNPRPPS SQSAEGLEGG
     GGNGSANVHA
//
ID   C3VLD3_MOUSE            Unreviewed;      1195 AA.
AC   C3VLD3;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   30-NOV-2010, entry version 16.
DE   SubName: Full=Large conductance Ca2+-activated potassium channel DEC variant 1;
GN   Name=Kcnma1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBA/J; TISSUE=Cochlea;
RA   Kathiresan T., Harvey M., Orchard S., Sakai Y., Sokolowski B.;
RT   "A Protein Interaction Network for the Large Conductance Ca2+-
RT   activated Potassium Channel in the Mouse Cochlea.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FJ872117; ACP74150.1; -; mRNA.
DR   IPI; IPI00410905; -.
DR   UniGene; Mm.343607; -.
DR   UniGene; Mm.458374; -.
DR   Ensembl; ENSMUST00000074983; ENSMUSP00000074511; ENSMUSG00000063142.
DR   MGI; MGI:99923; Kcnma1.
DR   Bgee; C3VLD3; -.
DR   Genevestigator; C3VLD3; -.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0015269; F:calcium-activated potassium channel activity; IEA:InterPro.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003929; K_chnl_Ca-activ_BK_asu.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR003148; RCK_N.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF03493; BK_channel_a; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02254; TrkA_N; 1.
DR   PRINTS; PR01449; BKCHANNELA.
DR   PRINTS; PR00169; KCHANNEL.
PE   2: Evidence at transcript level;
KW   Ion transport; Ionic channel; Membrane; Potassium; Potassium channel;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport.
SQ   SEQUENCE   1195 AA;  134534 MW;  5BC29C3DE581277A CRC64;
     MDALIIPVTM EVPCDSRGQR MWWAFLASSM VTFFGGLFII LLWRTLKYLW TVCCHCGGKT
     KEAQKINNGS SQADGTLKPV DEKEEVVAAE VGWMTSVKDW AGVMISAQTL TGRVLVVLVF
     ALSIGALVIY FIDSSNPIES CQNFYKDFTL QIDMAFNVFF LLYFGLRFIA ANDKLWFWLE
     VNSVVDFFTV PPVFVSVYLN RSWLGLRFLR ALRLIQFSEI LQFLNILKTS NSIKLVNLLS
     IFISTWLTAA GFIHLVENSG DPWENFQNNQ ALTYWECVYL LMVTMSTVGY GDVYAKTTLG
     RLFMVFFILG GLAMFASYVP EIIELIGNRK KYGGSYSAVS GRKHIVVCGH ITLESVSNFL
     KDFLHKDRDD VNVEIVFLHN ISPNLELEAL FKRHFTQVEF YQGSVLNPHD LARVKIESAD
     ACLILANKYC ADPDAEDASN IMRVISIKNY HPKIRIITQM LQYHNKAHLL NIPSWNWKEG
     DDAICLAELK LGFIAQSCLA QGLSTMLANL FSMRSFIKIE EDTWQKYYLE GVSNEMYTEY
     LSSAFVGLSF PTVCELCFVK LKLLMIAIEY KSANRESRIL INPGNHLKIQ EGTLGFFIAS
     DAKEVKRAFF YCKACHDDVT DPKRIKKCGC RRLIYFEDEQ PPTLSPKKKQ RNGGMRNSPN
     TSPKLMRHDP LLIPGNDQID NMDSNVKKYD STGMFHWCAP KEIEKVILTR SEAAMTVLSG
     HVVVCIFGDV SSALIGLRNL VMPLRASNFH YHELKHIVFV GSIEYLKREW ETLHNFPKVS
     ILPGTPLSRA DLRAVNINLC DMCVILSANQ NNIDDTSLQD KECILASLNI KSMQFDDSIG
     VLQANSQGFT PPGMDRSSPD NSPVHGMLRQ PSITTGVNIP IITELAKPGK LPLVSVNQEK
     NSGTHILMIT ELVNDTNVQF LDQDDDDDPD TELYLTQPFA CGTAFAVSVL DSLMSATYFN
     DNILTLIRTL VTGGATPELE ALIAEENALR GGYSTPQTLA NRDRCRVAQL ALLDGPFADL
     GDGGCYGDLF CKALKTYNML CFGIYRLRDA HLSTPSQCTK RYVITNPPYE FELVPTDLIF
     CLMQFDHNAG QSRASLSHSS HSSQSSSKKS SSVHSIPSTA NRPNRPKSRE SRDKQNATRM
     TRMGQEKKWF TDEPDNAYPR NIQIKPMSTH MANQINQYKS TSSLIPPIRE VEDEC
//
ID   C4IXU2_MOUSE            Unreviewed;      1026 AA.
AC   C4IXU2;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   08-MAR-2011, entry version 18.
DE   SubName: Full=Farp1 protein;
DE   Flags: Fragment;
GN   Name=Farp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -!- SIMILARITY: Contains 2 PH domains.
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DR   EMBL; BC141229; AAI41230.1; -; mRNA.
DR   IPI; IPI00356904; -.
DR   UniGene; Mm.223980; -.
DR   Ensembl; ENSMUST00000026635; ENSMUSP00000026635; ENSMUSG00000025555.
DR   MGI; MGI:2446173; Farp1.
DR   OrthoDB; EOG4J3WG7; -.
DR   Bgee; C4IXU2; -.
DR   Genevestigator; C4IXU2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0019898; C:extrinsic to membrane; IEA:InterPro.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR000798; Ez/rad/moesin.
DR   InterPro; IPR014847; FERM-adjacent.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 3.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF00169; PH; 2.
DR   Pfam; PF00621; RhoGEF; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   1026 AA;  116623 MW;  1CB39514A28BE24B CRC64;
     STLERGQKPP PTPSGKLMTV KIQMLDDTQE AFEVPQRAPG KVLFDAVCNH LNLVEGDYFG
     LEFPDHRKIV VWLDLLKPIV KQIRRPKHVV VKFVVKFFPP DHTQLQEELT RYLFALQVKQ
     DLAQGRLTCN DTSAALLISH IVQSEIGDFD EALDREHLAK NKYVPQQDAL EDRIMEFHHS
     HVGQTPAESD FQLLEVARRL EMYGIRLHPA KDREGTKINL AVANTGILVF QGFTKINAFN
     WAKVRKLSFK RKRFLIKLRP DVNSSYQDTL EFLMAGRDFC KSFWKICVEH HAFFRLFEEP
     KPKPKPVLFS RGSSFRFSGR TQKQVLDYVK EGGHKKVQFE RKHSKIHSTR SLVSQPTAPN
     SEVPKQSPQS ASLTFGEGTE SPGGQSCQQA KETKACTLEL GPHQSPALPK SPPGSKAADG
     TTVVPPEEEE EEEGGKDGIR PSNPQPPQPS TGSLTGSPHL SELSINSQGG AAPANVTLSP
     NLSPDNKQAS PLISPLLNDQ ACPRTDDEEE GRRKRFPTDK AYYIAKEVST TERTYLKDLE
     VIASWFQSTV SKEDSMPEAL KSLIFPNFEP LHKFHTNFLK EIEQRLALWE GRSNAHIRGD
     YQRIGDVMLK NIQGMKHLAA HLWKHSEALE ALETSIKGSR RLEHFCRDFE LQKVCYLPLN
     TFLLRPLHRL MHYKHVLERL CKHHPPNHAD FRDCRAALAE ITEMVAQLHG TMIKMENFQK
     LHELKKDLVG IDNLVIPGRE FIRLGSLSKL SGKGLQQRMF FLFNDVLLYT SRGLTASNQF
     KVHGQLPLYG MTIEESEEEW GVPHCLTLRG QRQSIIVAAS SRSEMEKWME DIQMAIDLAE
     KSNGPTPELL ASSPPDNKSP DEATAADQES EDDLSASRTS LERQAPHRGN TMVHVCWHRS
     TSVSMVDFSI AVENQLSGNL LRKFKNSNGW QKLWVVFTNF CLFFYKSHQD SHPLASLPLL
     GYSLTIPSES ENIHKDYVFK LHFKSHVYYF RAESEYTFER WMEVIRSATS SASRAHILSH
     KESHLY
//
ID   C6EQG9_MOUSE            Unreviewed;       642 AA.
AC   C6EQG9;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   05-OCT-2010, entry version 11.
DE   SubName: Full=ASL1/Amph fusion protein;
GN   Name=Amph;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RA   Li J., Symer D.E.;
RT   "An active antisense promoter in mouse L1 retrotransposons has
RT   implications for fusion gene expression and epigenetic control.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; EU234004; ACD47033.1; -; mRNA.
DR   Ensembl; ENSMUST00000003345; ENSMUSP00000003345; ENSMUSG00000021314.
DR   MGI; MGI:103574; Amph.
DR   Bgee; C6EQG9; -.
DR   Genevestigator; C6EQG9; -.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR   GO; GO:0007612; P:learning; IMP:MGI.
DR   GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:MGI.
DR   InterPro; IPR003005; Amphiphysin.
DR   InterPro; IPR003017; Amphiphysin_1.
DR   InterPro; IPR004148; BAR.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF03114; BAR; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR01251; AMPHIPHYSIN.
DR   PRINTS; PR01252; AMPHIPHYSIN1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00721; BAR; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS51021; BAR; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   642 AA;  69677 MW;  0CCFFC03B84A75AE CRC64;
     MMAEGTRLQR ELRGYLAAIK GMQEASMKLT ESLHEVYEPD WYGREDVKMV GEKCDVLWED
     FHQKLVDGSL LTLDTYLGQF PDIKNRIAKR SRKLVDYDSA RHHLEALQSS KRKDESRISK
     AEEEFQKAQK VFEEFNVDLQ EELPSLWSSR VGFYVNTFKN VSSLEAKFHK EIAVLCHKLY
     EVMTKLGDQH ADKAFSIQGA PSDSGPLRIA KTPSPPEEPS PLPSPTASPN HTLAPASPAP
     VRPRSPSQTR KGPPVPPLPK VTPTKELKQE NIINFFEDNF VPEINVTTPS QNEVLEVKKE
     ETLLDLDFDP FKPDVAPAGS AAATHSPMSQ TLPWDLWTTS TDLVQPASGG SFNDFTQAQD
     TSLFTMQTDQ NMVGGLAETE QALPTEPQAE EPPATAAAPT AGLDLGLEME EPKEEAVIPP
     ATDTGETVET AVPTEGAPVE EAEAEKAALP AGEGGSPEGA KIDGESTELA ISESPQPVEP
     EAGAPQVIPS VVIEPASNHE GEGEHQETAT GTEPREAAED VAAQGSAGEK QEVATEPTPL
     DSQATLPASA GAVDASLSAG DATQELPPGF LYKVETLHDF EAANSDELNL QRGDVVLVVP
     SDSEADQDAG WLVGVKESDW LQYRDLATYK GLFPENFTRR LE
//
ID   C7TQ62_MOUSE            Unreviewed;      2222 AA.
AC   C7TQ62;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   08-MAR-2011, entry version 14.
DE   SubName: Full=Calcium channel voltage-dependent alpha1c subunit;
GN   Name=Cacna1c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6N; TISSUE=Heart;
RA   Link S., Meissner M., Held B., Beck A., Weissgerber P., Freichel M.,
RA   Flockerzi V.;
RT   "Diversity and developmental expression of L-type calcium channel ?2
RT   proteins and their influence on calcium current in murine heart.";
RL   J. Biol. Chem. 0:0-0(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6N; TISSUE=Heart;
RA   Link S.A.M.;
RL   Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family.
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DR   EMBL; FM872414; CAS06717.1; -; mRNA.
DR   IPI; IPI00947641; -.
DR   UniGene; Mm.436656; -.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005451; VDCC_L_a1csu.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF47; LVDCCAlpha1C; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
DR   PRINTS; PR01635; LVDCCALPHA1C.
PE   2: Evidence at transcript level;
KW   Calcium; Calcium channel; Calcium transport; Ion transport;
KW   Ionic channel; Membrane; Transmembrane; Transport;
KW   Voltage-gated channel.
SQ   SEQUENCE   2222 AA;  248927 MW;  7360C3613F776AAA CRC64;
     MVNENTRMYV PEENHQGSNY GSPRPAHANM NANAAAGLAP EHIPTPGAAL SWQAAIDAAR
     QAKLMGSAGN ATISTVSSTQ RKRQQYGKPK KQGGTTATRP PRALLCLTLK NPIRRACISI
     VEWKPFEIII LLTIFANCVA LAIYIPFPED DSNATNSNLE RVEYLFLIIF TVEAFLKVIA
     YGLLFHPNAY LRNGWNLLDF IIVVVGLFSA ILEQATKADG ANALGGKGAG FDVKALRAFR
     VLRPLRLVSG VPSLQVVLNS IIKAMVPLLH IALLVLFVII IYAIIGLELF MGKMHKTCYN
     QEGIIDVPAE EDPSPCALET GHGRQCQNGT VCKPGWDGPK HGITNFDNFA FAMLTVFQCI
     TMEGWTDVLY WVNDAVGRDW PWIYFVTLII IGSFFVLNLV LGVLSGEFSK EREKAKARGD
     FQKLREKQQL EEDLKGYLDW ITQAEDIDPE NEDEGMDEDK PRNRGAPAGL HDQKKGKFAW
     FSHSTETHMS MPTSETESVN TENVAGGDIE GENCGARLAH RISKSKFSRY WRRWNRFCRR
     KCRAAVKSNV FYWLVIFLVF LNTLTIASEH YNQPHWLTEV QDTANKALLA LFTAEMLLKM
     YSLGLQAYFV SLFNRFDCFI VCGGILETIL VETKIMSPLG ISVLRCVRLL RIFKITRYWN
     SLSNLVASLL NSVRSIASLL LLLFLFIIIF SLLGMQLFGG KFNFDEMQTR RSTFDNFPQS
     LLTVFQILTG EDWNSVMYDG IMAYGGPSFP GMLVCIYFII LFICGNYILL NVFLAIAVDN
     LADAESLTSA QKEEEEEKER KKLARTASPE KKQEVMEKPA VEESKEEKIE LKSITADGES
     PPTTKINMDD LQPSENEDKS PHSNPDTAGE EDEEEPEMPV GPRPRPLSEL HLKEKAVPMP
     EASAFFIFSP NNRFRLQCHR IVNDTIFTNL ILFFILLSSI SLAAEDPVQH TSFRNHILGN
     ADYVFTSIFT LEIILKMTAY GAFLHKGSFC RNYFNILDLL VVSVSLISFG IQSSAINVVK
     ILRVLRVLRP LRAINRAKGL KHVVQCVFVA IRTIGNIVIV TTLLQFMFAC IGVQLFKGKL
     YTCSDSSKQT EAECKGNYIT YKDGEVDHPI IQPRSWENSK FDFDNVLAAM MALFTVSTFE
     GWPELLYRSI DSHTEDKGPI YNYRVEISIF FIIYIIIIAF FMMNIFVGFV IVTFQEQGEQ
     EYKNCELDKN QRQCVEYALK ARPLRRYIPK NQHQYKVWYV VNSTYFEYLM FVLILLNTIC
     LAMQHYGQSC LFKIAMNILN MLFTGLFTVE MILKLIAFKP KHYFCDAWNT FDALIVVGSI
     VDIAITEVHP AEHTQCSPSM VRTTLQTTFP ASVAPPLATH VLSTLISRAL GTQPSSHCMW
     PPCPLCALTA CAHVSCARSA EENSRISITF FRLFRVMRLV KLLSRGEGIR TLLWTFIKSF
     QALPYVALLI VMLFFIYAVI GMQVFGKIAL NDTTEINRNN NFQTFPQAVL LLFRCATGEA
     WQDIMLACMP GKKCAPESEP SNSTEGETPC GSSFAVFYFI SFYMLCAFLI INLFVAVIMD
     NFDYLTRDWS ILGPHHLDEF KRIWAEYDPE AKGRIKHLDV VTLLRRIQPP LGFGKLCPHR
     VACKRLVSMN MPLNSDGTVM FNATLFALVR TALRIKTEGN LEQANEELRA IIKKIWKRTS
     MKLLDQVVPP AGDDEVTVGK FYATFLIQEY FRKFKKRKEQ GLVGKPSQRN ALSLQAGLRT
     LHDIGPEIRR AISGDLTAEE ELDKAMKEAV SAASEDDIFR RAGGLFGNHV TYYQSDSRGN
     FPQTFATQRP LHINKTGNNQ ADTESPSHEK LVDSTFTPSS YSSTGSNANI NNANNTALGR
     FPHPAGYSST VSTVEGHGPP LSPAVRVQEA AWKLSSKRCH SRESQGATVN QEIFPDETRS
     VRMSEEAEYC SEPSLLSTDM FSYQEDEHRQ LTCPEEDKRE IQPSPKRSFL RSASLGRRAS
     FHLECLKRQK DQGGDISQKT ALPLHLVHHQ ALAVAGLSPL LQRSHSPTTF PRPCPTPPVT
     PGSRGRPLRP IPTLRLEGAE SSEKLNSSFP SIHCSSWSEE TTACSGSSSM ARRARPVSLT
     VPSQAGAPGR QFHGSASSLV EAVLISEGLG QFAQDPKFIE VTTQELADAC DMTIEEMENA
     ADNILSGGAQ QSPNGTLLPF VNCRDPGQDR AVAPEDESCA YALGRGRSEE ALADSRSYVS
     NL
//
ID   C9K100_MOUSE            Unreviewed;       610 AA.
AC   C9K100;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   11-JAN-2011, entry version 11.
DE   SubName: Full=Phosphodiesterase 4A;
GN   Name=Pde4a; Synonyms=pde4a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DdY; TISSUE=Spinal cord;
RA   Nishizwa M., Ito S.;
RT   "Expression of mRNA in mouse spinal cord.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DdY; TISSUE=Spinal cord;
RA   Nishizawa M., Ito S.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AB154250; BAI44635.1; -; mRNA.
DR   IPI; IPI00228051; -.
DR   UniGene; Mm.191749; -.
DR   Ensembl; ENSMUST00000003395; ENSMUSP00000003395; ENSMUSG00000032177.
DR   MGI; MGI:99558; Pde4a.
DR   Bgee; C9K100; -.
DR   GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR003607; Metal-dep_PHydrolase_HD_dom.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR023174; PDEase_CS.
DR   Gene3D; G3DSA:1.10.1300.10; PDEase_catalytic_dom; 1.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00471; HDc; 1.
DR   PROSITE; PS00126; PDEASE_I; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding.
SQ   SEQUENCE   610 AA;  68130 MW;  207AED14C3D4F76E CRC64;
     MPLVDFFCET CSKPWLVGWW DQFKRMLNRE LTHLSEMSRS GNQVSEYISN TFLDKQHEVE
     IPSPAPRQRP FQQPPPAAVQ QAQPMSQITG LKKLVHTGSL NINVPRFGVK TDQEDLLAQE
     LENLSKWGLN IFCVSEYAGG RSLSCIMYTI FQERDLLKKF HIPVDTMMTY MLTLEDHYHA
     DVAYHNSLHA ADVLQSTHVL LATPALDAVF TDLEILAALF AAAIHDVDHP GVSNQFLINT
     NSELALMYND ESVLENHHLA VGFKLLQEEN CDIFQNLSKR QKQSLRKMVI DMVLATDMSK
     HMTLLADLKT MVETKKVTSS GVLLLDNYSD RIQVLRNMVH CADLSNPTKP LELYRQWTDR
     IMAEFFQQGD RERERGMEIS PMCDKHTASV EKSQVGFIDY IVHPLWETWA DLVHPDAQDI
     LDTLEDNRDW YHSAIRQSPS PTLEEEPGVL GDPALPDKFQ FELTLEEEDE EDSLEVPGLP
     CTEETLLAPH DTRAQAMEQS KVKGQSPAVV EVVESLKQET ASAHGAPEES AEAVGHSFSL
     ETSILPDLRT LSPSEEAQGL LGLPSMAAEV EAPRDHLAAM RACSACSGTS GDNSAVISAP
     GRWGSGGDPA
//
ID   D0VYV6_MOUSE            Unreviewed;       911 AA.
AC   D0VYV6;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   05-OCT-2010, entry version 10.
DE   SubName: Full=Erythrocyte protein band 4.1-like 3 isoform B;
GN   Name=Epb4.1l3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C3H/HeN; TISSUE=Cochlea;
RA   Okumura K., Mochizuki E., Yokohama M., Kikkawa Y.;
RT   "Protein 4.1 expression in the developing mouse hair cells of
RT   cochlea.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 FERM domain.
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DR   EMBL; AB523362; BAI50089.1; -; mRNA.
DR   IPI; IPI00125501; -.
DR   UniGene; Mm.131135; -.
DR   Ensembl; ENSMUST00000080208; ENSMUSP00000079098; ENSMUSG00000024044.
DR   MGI; MGI:103008; Epb4.1l3.
DR   Bgee; D0VYV6; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0019898; C:extrinsic to membrane; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
DR   InterPro; IPR008379; Band_4.1_C.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR021187; Band_41_protein.
DR   InterPro; IPR000798; Ez/rad/moesin.
DR   InterPro; IPR014847; FERM-adjacent.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR007477; SAB.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF05902; 4_1_CTD; 1.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF04382; SAB; 1.
DR   PIRSF; PIRSF002304; Membrane_skeletal_4_1; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   911 AA;  101418 MW;  7304BA5C978A41BC CRC64;
     MTTESGSDSE SKPDQEAEPQ EAAGPQGQAG AQPGPEPAGG NGSLNGEKQQ PALEQFPEAA
     AHSTPVKREI GDKDRDFAAA AAKQLEYQQF EDDKLSQRSS SSKLSRSPLK IVKRPKSMQC
     KVTLLDGSEY GCDVDKRSRG QVLFDKVCEH LNLLEKDYFG LTYRDAENQK NWLDPAKEIK
     KQIRSGAWHF SFNVKFYPPD PAQLSEDITR YYLCLQLRDD IVSGRLPCSF VTLALLGSYT
     VQSELGDYDP DECGNDYISE FRFAPNHTKE LEDKVIELHK SHRGMTPAEA EMHFLENAKK
     LSMYGVDLHH AKDSEGVEIM LGVCASGLLI YRDRLRINRF AWPKVLKISY KRNNFYIKIR
     PGEFEQFEST IGFKLPNHRA AKRLWKVCVE HHTFFRLLLP EAPPKKFLTL GSKFRYSGRT
     QAQTRRASAL IDRPAPYFER SSSKRYTMSR SLDGEVGTGQ YATTKGISQT NLITTVTPEK
     KAEEERVEEE DRRKKAEEAT PVTALRHEGK TDSERTDTAA DGETSATESD QEEDAEIKAQ
     DLDKTQDELM KHQTNISELK RTFLETSTET ALTNEWEKRL STSPVRLAAR QEDAPMIEPL
     VPEETKQSSG EKLMDGSEIL SLLESARKPT EFIGGVSSTT QSWVQKLETK TEPVEAEVES
     TPHPQPLSTE KVLQETILVE ERHVMSVHAS GDASHTARDE VDAAESTPTD RRHTGKGKEG
     SSVTEAAKEQ RGEEVDQSAP EQEQPATVSH EEEQASTIRT SEGLEQKSHF ESSTVRVEST
     SVGSISPGGA KLEISTKEVP VVHTETKTIT YESSQVDPGA DLEPGVLMSA QTITSETTST
     TTTTHITKTV KGGISETRIE KRIVITGDAD IDHDQALAQA IKEAKEQHPD MSVTKVVVHK
     ETEITPEDGE D
//
ID   D1FNM8_MOUSE            Unreviewed;      1166 AA.
AC   D1FNM8;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   08-MAR-2011, entry version 15.
DE   SubName: Full=Plasma membrane Ca++ transporting ATPase 4 variant x/e;
GN   Name=Atp2b4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Afroze T., Yang G., Khoshbin A., Tanwir M., Tabish T., Momen A.,
RA   Elias C., Backx P., Husain M.;
RT   "Regulated Alternative Splicing of a Novel and a Classical Exon-20 of
RT   PMCA4.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       family.
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DR   EMBL; EU493094; ACC91879.1; -; mRNA.
DR   IPI; IPI00463589; -.
DR   RefSeq; NP_001161421.1; NM_001167949.1.
DR   UniGene; Mm.440679; -.
DR   ProteinModelPortal; D1FNM8; -.
DR   Ensembl; ENSMUST00000125659; ENSMUSP00000116941; ENSMUSG00000026463.
DR   GeneID; 381290; -.
DR   KEGG; mmu:381290; -.
DR   CTD; 381290; -.
DR   MGI; MGI:88111; Atp2b4.
DR   Bgee; D1FNM8; -.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005388; F:calcium-transporting ATPase activity; IEA:InterPro.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   InterPro; IPR022141; ATP_Ca_trans_C.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR006408; ATPase_P-typ_Ca-transp_PMCA.
DR   InterPro; IPR006069; ATPase_P-typ_cation-exchng_asu.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023300; ATPase_P-typ_cyto_domA.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Gene3D; G3DSA:2.70.150.10; ATPase_P-typ_cyto_domA; 1.
DR   Gene3D; G3DSA:3.40.1110.10; ATPase_P-typ_cyto_domN; 1.
DR   Gene3D; G3DSA:1.20.1110.10; ATPase_P-typ_TM_dom; 1.
DR   Pfam; PF12424; ATP_Ca_trans_C; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00121; NAKATPASE.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01517; ATPase-IIB_Ca; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 4.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Hydrolase; Ion transport; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Transmembrane; Transmembrane helix; Transport.
SQ   SEQUENCE   1166 AA;  128562 MW;  6BA2DCC9725178AB CRC64;
     MTNPPGQSVS ANTVAESHEG EFGCTLMDLR KLMELRGADA VAQISAHYGG VQEICTRLKT
     SPIEGLSGNP ADLEKRRLVF GKNVIPPKRP KTFLELVWEA LQDVTLIILE IAAIISLVLS
     FYRPPGGDNE ICGHIASSPE EEEEGETGWI EGAAILASVI IVVLVTAFND WSKEKQFRGL
     QSRIELEQKF SIIRNGQLIQ LPVAEIVVGD IAQIKYGDLL PADGILIQGN DLKIDESSLT
     GESDHVKKTL DKDPMLLSGT HVMEGSGRMV VTAVGVNSQT GIIFTLLGAS EEEDDDDKKK
     KGKKQGAPEN RNKAKTQDGV ALEIQPLNSQ EGLDSEDKEK KIARIPKKEK SVLQGKLTRL
     AVQIGKAGLI MSVLTVVILI LYFVVDNFVI QRREWLPECT PVYIQYFVKF FIIGVTVLVV
     AVPEGLPLAV TISLAYSVKK MMKDNNLVRH LDACETMGNA TAICSDKTGT LTMNRMTVVQ
     AYIGGTHYRQ IPQPDVFPPK VLELIVNGIS INCAYTSKIQ PPEKEGGLPR QVGNKTECGL
     LGFVTDLKQD YQAVRNEVPE EKLFKVYTFN SVRKSMSTVI RKPEGGFRMF SKGASEIMLR
     RCDRILNKEG EIKSFRSKDR DNMVRNVIEP MASEGLRTIC LAYRDFDGTE PSWDIEGEIL
     TSLICIAVVG IEDPVRPEVP DAIAKCKRAG ITVRMVTGDN VNTARAIATK CGILTPKDDF
     LCLEGKEFNS LIRNEKGEVE QEKLDKIWPK LRVLARSSPT DKHTLVKGII DSTAGEQRQV
     VAVTGDGTND GPALKKADVG FAMGIAGTDV AKEASDIILT DDNFTSIVKA VMWGRNVYDS
     ISKFLQFQLT VNVVAVIVAF TGACITQDSP LKAVQMLWVN LIMDTFASLA LATEPPTESL
     LRRRPYGRNK PLISRTMMKN ILGHAVYQLL IVFLLVFAGD TLFDIDSGRK APLNSPPSQH
     YTIVFNTFVL MQLFNEINAR KIHGEKNVFA GVYRNIIFCT VVLGTFFCQI MIVELGGKPF
     SCTSLTMEQW MWCLFIGIGE LLWGQVISAI PTKSLKFLKE AGHGSDKEDI SRDTEGMDEI
     DLAEMELRRG QILWVRGLNR IQTQIDVINK FQTEAPLKRV RENMTQHLDV KLVPSSYSAA
     VASLRTCPSI SSAISSAVTS PPVGSE
//
ID   D3Y273_MOUSE            Unreviewed;      1095 AA.
AC   D3Y273;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 2.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Solute carrier family 4 sodium bicarbonate cotransporter member 7 variant NBCn1-E;
GN   Name=Slc4a7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Reproductive tract;
RA   Liu Y., Chen L.M.;
RT   "Cloning and identification of two novel mouse NBCn1 splice
RT   variants.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GU386353; ADC92005.2; -; mRNA.
DR   IPI; IPI00664442; -.
DR   UniGene; Mm.258893; -.
DR   Ensembl; ENSMUST00000057015; ENSMUSP00000058313; ENSMUSG00000021733.
DR   MGI; MGI:2443878; Slc4a7.
DR   Bgee; D3Y273; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
DR   InterPro; IPR011531; HCO3_transpt_C.
DR   InterPro; IPR013769; HCO3_transpt_cyt.
DR   InterPro; IPR003020; HCO3_transpt_euk.
DR   InterPro; IPR003024; Na/HCO3_transpt.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   Gene3D; G3DSA:3.40.1100.10; HCO3_transpt_cyt; 1.
DR   PANTHER; PTHR11453; HCO3_transpt_euk; 1.
DR   Pfam; PF07565; Band_3_cyto; 1.
DR   Pfam; PF00955; HCO3_cotransp; 1.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   PRINTS; PR01232; NAHCO3TRSPRT.
DR   SUPFAM; SSF55804; PTrfase/Anion_transptr; 1.
DR   TIGRFAMs; TIGR00834; ae; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1095 AA;  123291 MW;  B2DA68720CE38444 CRC64;
     MEADGAGEQM RPLLTRGPDE EAVVDLGKTS STVNTKFEKE ELESHRAVYV GVHVPFSKES
     RRRHKHRGHK HHHRRRKDKD SDKEDGRESP SYDTPSQRVQ FILGTEDDDE EHIPHDLFTE
     MDELCYRDGE EYEWKETARW LKFEEDVEDG GDRWSKPYVA TLSLHSLFEL RSCILNGTVM
     LDMRASTLDE IADMVLDNMI ASGQLDDSIR ENVREALLKR HHHQNEKRFT SRIPLVRSFA
     DIGKKHSDPH LLERNGILAS PQSAPGNLDN SKSGEMKGNG SGGSRENSTV DFSKVDMNFM
     RKIPTGAEAS NVLVGEVDFL ERPIIAFVRL APAVLLSGLT EVPVPTRFLF LLLGPAGKAP
     QYHEIGRSIA TLMTDEIFHD VAYKAKDRND LLSGIDEFLD QVTVLPPGEW DPSIRIEPPK
     SVPSQEKRKI PVFPNGSAAM SVDPPKEDDH HAGPELQRTG RLFGGLILDI KRKAPFFLSD
     FKDALSLQCL ASILFLYCAC MSPVITFGGL LGEATEGRIS AIESLFGASL TGIAYSLFAG
     QPLTILGSTG PVLVFEKILF KFCRDYHLSY LSLRTSIGLW TSFLCIVLVA TDASSLVCYI
     TRFTEEAFAA LICIIFIYEA LEKLFHLGEI YAFNMHNNLD ELTSYTCVCA EPSNPSNETL
     ELWKRKNITA YSVSWGNLTV SECKTFHGMF VGSACGPHGP YVPDVLFWCV VLFFTTFFLS
     SFLKQFKTKR YFPTKVRSTI SDFAVFLTIV IMVAIDYLVG IPSPKLHVPE KFEPTDPSRG
     WIISPLGDNP WWTLLIAAVP ALLCTILIFM DQQITAVIIN RKEHKLKKGA GYHLDLLMVG
     VMLGVCSIMG LPWFVAATVL SISHVNSLKV ESECSAPGEQ PKFLGIREQR VTGLMIFILM
     GLSVFMTSVL KFIPMPVLYG VFLYMGVSSL KGIQFFDRIK LFGMPAKHQP DLIYLRYVPL
     WKVHVFTVVQ LTCLVLLWVI KASAAAVVFP MMVLALVFVR KLMDLCFTKR ELSWLDDLMP
     ESKKKKEDDK KKKEKEEAER MLQDDEDTVH LPFERGSLLQ IPVKTLKYSP EKPVSVTINF
     EDEPSKKYMD AETSL
//
ID   D3YTL8_MOUSE            Unreviewed;       643 AA.
AC   D3YTL8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 11.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Spire1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
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DR   EMBL; AC120410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00956954; -.
DR   RefSeq; NP_919336.1; NM_194355.2.
DR   UniGene; Mm.208723; -.
DR   ProteinModelPortal; D3YTL8; -.
DR   Ensembl; ENSMUST00000045105; ENSMUSP00000049336; ENSMUSG00000024533.
DR   GeneID; 68166; -.
DR   KEGG; mmu:68166; -.
DR   CTD; 68166; -.
DR   MGI; MGI:1915416; Spire1.
DR   GeneTree; ENSGT00390000003058; -.
DR   Bgee; D3YTL8; -.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0048193; P:Golgi vesicle transport; IDA:MGI.
DR   InterPro; IPR011019; KIND.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS51377; KIND; 1.
PE   4: Predicted;
SQ   SEQUENCE   643 AA;  73582 MW;  FD183EC12AA36734 CRC64;
     MANTVEADGS KDEGYEAADE GPEDEDGEKR SISAIRSYQD VMKICAAHLP TESEAPNHYQ
     AVCRALFAET MELHTFLTKI KSAKENLKKI QEMEKGDESS TDLEDLKNAD WARFWVQVMR
     DLRNGVKLKK VQQRQYNPLP IEYQLTPYEM LMDDIRCKRY TLRKVMVNGD VPPRLKKSAH
     EVILDFIRSR PPLNPVSARK LKPTPPRPRS LHERILEEIK AERKLRPVSP EEIRRSRLDV
     TTPESPKNVG ESSMVNGGLT SQTKENGLSA AQQGSAQRKR LLKAPTLAEL DSSDSEEEKS
     LHKSTSSSSA SPSLYEDPVL EAMCSRKKPP KFLPISSTPQ PERRQPPQRR HSIEKETPTN
     VRQFLPPSRQ SSRSLVPRIT GVWPRTPFRP LFSTIQTASL LSSHPFEAAM FGVAGAMYYL
     FERAFTSRWK PSKEEFCYPV ECLALTVEEV MHIRQVLVKA ELEKYQQYKD VYTALKKGKL
     CFCCRTRRFS FFTWSYTCQF CKRPVCSQCC KKMRLPSKPY STLPIFSLGP SALQRGESCS
     RSEKPSTSHH RPLRSIARFS TKSRSVDKSD EELQFPKELM EDWSTMEVCV DCKKFISEII
     SSSRRSLVLA NKRARLKRKT QSFYMSSAGP SEYCPSERTI NEI
//
ID   D3YTR7_MOUSE            Unreviewed;       364 AA.
AC   D3YTR7;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 6.
DE   RecName: Full=Adenylyl cyclase-associated protein;
GN   Name=Cap2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Belongs to the CAP family.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
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DR   EMBL; AC124598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC138329; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00882316; -.
DR   Ensembl; ENSMUST00000119341; ENSMUSP00000112952; ENSMUSG00000021373.
DR   MGI; MGI:1914502; Cap2.
DR   GeneTree; ENSGT00390000017955; -.
DR   Bgee; D3YTR7; -.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR   InterPro; IPR001837; Adenylate_cyclase-assoc_CAP.
DR   InterPro; IPR013912; Adenylate_cyclase-assoc_CAP_C.
DR   InterPro; IPR013992; Adenylate_cyclase-assoc_CAP_N.
DR   InterPro; IPR017901; C-CAP_CF_C-like.
DR   InterPro; IPR016098; CAP/MinC_C.
DR   InterPro; IPR018106; CAP_CS.
DR   InterPro; IPR006599; CARP_motif.
DR   Gene3D; G3DSA:2.160.20.70; CAP/MinC_C; 1.
DR   PANTHER; PTHR10652; CAP; 1.
DR   Pfam; PF08603; CAP_C; 1.
DR   Pfam; PF01213; CAP_N; 2.
DR   SMART; SM00673; CARP; 2.
DR   SUPFAM; SSF101278; Adenylate_cyclase-assoc_CAP_N; 1.
DR   SUPFAM; SSF69340; CARP; 1.
DR   PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
DR   PROSITE; PS01088; CAP_1; 1.
DR   PROSITE; PS01089; CAP_2; 1.
PE   3: Inferred from homology;
SQ   SEQUENCE   364 AA;  39877 MW;  695EF948D64C2C47 CRC64;
     MTDMAGLMER LERAVIRLEQ LSAGLDGPPR GCGEVNGVNG GVAPSVEAFD KLINSMVAEF
     LKNSRVLAGD VETHAEMVHG AFQAQRAFLL MVSQYQQPQE GPVASTASAF SILSSGPGLP
     PPPPPPPPPG PPPPFENEDK KEEPSPSRSA LFAQLNQGEA ITKGLRHVTD DKKTYKNPSL
     RAQGQIRSPT KTHTPSPTSP KSNSPQKHTP VLELEGKKWR VEYQEDRNDL VISETELKQV
     AYIFKCDKST LQIKGKVNSI TVDNCKKFGL VFDHVVGIVE VINSKDIQIQ VMGRVPTISI
     NKTEGCHLYL SEDALDCEIV SAKSSEMNVL VPQDDDYREF PIPEQFKTIW DGSKLVTEPA
     EIMA
//
ID   D3YTT1_MOUSE            Unreviewed;       113 AA.
AC   D3YTT1;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Syn3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
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CC   -----------------------------------------------------------------------
DR   EMBL; AC122919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC124614; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC125060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC145076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC150899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00875940; -.
DR   Ensembl; ENSMUST00000077267; ENSMUSP00000076499; ENSMUSG00000059602.
DR   Ensembl; ENSMUST00000105303; ENSMUSP00000100940; ENSMUSG00000059602.
DR   Ensembl; ENSMUST00000120638; ENSMUSP00000113720; ENSMUSG00000059602.
DR   Ensembl; ENSMUST00000121789; ENSMUSP00000113408; ENSMUSG00000059602.
DR   MGI; MGI:1351334; Syn3.
DR   Bgee; D3YTT1; -.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   InterPro; IPR013817; Pre-ATP_grasp.
DR   InterPro; IPR016185; PreATP-grasp-like.
DR   InterPro; IPR019736; Synapsin_P_site.
DR   InterPro; IPR020897; Synapsin_pre-ATP-grasp_dom.
DR   Gene3D; G3DSA:3.40.50.20; Pre-ATP_grasp; 1.
DR   Pfam; PF02078; Synapsin; 1.
DR   Pfam; PF10581; Synapsin_N; 1.
DR   SUPFAM; SSF52440; PreATP-grasp-like; 1.
DR   PROSITE; PS00415; SYNAPSIN_1; 1.
PE   4: Predicted;
SQ   SEQUENCE   113 AA;  12368 MW;  C8D25CA1A69EB044 CRC64;
     MNFLRRRLSD SSFVANLPNG YMPDLQRPES SSSSPASPAT ERRHPQPLAA SFSSPGSSLF
     SSFSGAMKQT PQAPSGLMEP PTPVTPVVQR PRILLVIDDA HTDWSKYFHG KKV
//
ID   D3YTT6_MOUSE            Unreviewed;       886 AA.
AC   D3YTT6;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   RecName: Full=Oxysterol-binding protein;
GN   Name=Osbpl3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the OSBP family.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
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DR   EMBL; AC008160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC124689; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00462728; -.
DR   Ensembl; ENSMUST00000090019; ENSMUSP00000087473; ENSMUSG00000029822.
DR   MGI; MGI:1918970; Osbpl3.
DR   Bgee; D3YTT6; -.
DR   GO; GO:0008202; P:steroid metabolic process; IEA:InterPro.
DR   InterPro; IPR000648; Oxysterol-bd.
DR   InterPro; IPR018494; Oxysterol-bd_CS.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   PANTHER; PTHR10972; Oxysterol_bd; 1.
DR   Pfam; PF01237; Oxysterol_BP; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS01013; OSBP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Lipid transport; Transport.
SQ   SEQUENCE   886 AA;  100497 MW;  DA627C7115E544CA CRC64;
     MSDEKNLGVS QKLVSPSRST SSCSSKQGSR QDSWEVVEGL RGEMTYTQEP PVQKGFLLKK
     RKWPLKGWHK RFFCLEKGIL KYAKSQADIE REKLHGCIDV GLSVMSVKKS SKCIDLDTEE
     HIYHLKVKSE ELFDEWVSKL RHHRMYRQNE IAMFPRDVNH FFSGSSVTDS APGVFESVSS
     RKRSSLSKQN SFPPGSNLSF SCGGDTRVPF WLQSSEDMEK CSKDMAHCHA YLLEMSQLLE
     SMDVLHRTYS APAINAIQGG AFESPKKEKR PHRRWRSRAI GKDAKGTLQV PKPFSGPVRL
     HSSNPNLSTL DFGEEKSYSD GSEASSEFSK MQEDLCHVAH KVYFALRSAF NSISVEREKL
     KQLMELDTSP SPSAQVVGLK HALSSALAQN TDLKERLRRI HAESLLLDPP AVPKPGDNLA
     EENSRDEGRA LVHQLSNESR LSITDSLSEF FDAQEVLLSP SSSENEISDD DSYVSDISDN
     LSLDNLSNDL DNERQTLGPV LESSGEARSK RRTSLPAPGP NTSSVSLWSI LRNNIGKDLS
     KVAMPVELNE PLNTLQRLCE ELEYSELLDK ASRIPSPLER MVYVAAFAIS AYASSYFRAG
     SKPFNPVLGE TYECIRQDKG FQFFAEQVSH HPPISACHAE SGNFVFWQDV RWKNKFWGKS
     MEIVPIGTTH VTLPAFGDHF EWNKVTSCIH NILSGQRWIE HYGEIDIKNL NDDSCHCKVN
     FIKAKYWSTN AHEIEGTVFD RSGKAVHRLF GKWHESIYCG GASSSTCVWR ANPMPKGYEQ
     YYGFTQFALE LNEMDPLSRS LLPPTDTRFR PDQRLLEEGN IEEAEVQKQR IEKLQRERRR
     VLEENGVEHQ PRFFRKSSDD AWVSNGTYLE LRKDLGFSKL DHPVLW
//
ID   D3YTU0_MOUSE            Unreviewed;       171 AA.
AC   D3YTU0;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Vamp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- SIMILARITY: Contains 1 v-SNARE coiled-coil homology domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC140324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00918069; -.
DR   Ensembl; ENSMUST00000063588; ENSMUSP00000063466; ENSMUSG00000030337.
DR   MGI; MGI:1313276; Vamp1.
DR   GeneTree; ENSGT00550000074449; -.
DR   Bgee; D3YTU0; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR001388; Synaptobrevin.
DR   Pfam; PF00957; Synaptobrevin; 1.
DR   PRINTS; PR00219; SYNAPTOBREVN.
DR   PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR   PROSITE; PS50892; V_SNARE; 1.
PE   4: Predicted;
KW   Coiled coil.
SQ   SEQUENCE   171 AA;  18735 MW;  A7F2AFDCC868ACC8 CRC64;
     MSAPAQPPAE GTEGAAPGGG PPGPPPNMTS NRRLQQTQAQ VEEVVDIMRV NVDKVLERDQ
     KLSELDDRAD ALQAGASQFE SSAAKLKRKY WWKNCKMMIM LGAICAIIVV VIVRMKISFG
     YRNDCKNGPP RNWNFPRNLM LGERKGRSLC QPGGPCLSVL FTSVDHAGLK L
//
ID   D3YTU6_MOUSE            Unreviewed;      1111 AA.
AC   D3YTU6;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Kcnt2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC120400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC156607; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC156989; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00885635; -.
DR   Ensembl; ENSMUST00000120709; ENSMUSP00000112887; ENSMUSG00000052726.
DR   MGI; MGI:3036273; Kcnt2.
DR   GeneTree; ENSGT00530000063026; -.
DR   Bgee; D3YTU6; -.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0015269; F:calcium-activated potassium channel activity; IEA:InterPro.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   InterPro; IPR013099; Ion_trans_2.
DR   InterPro; IPR003929; K_chnl_Ca-activ_BK_asu.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF03493; BK_channel_a; 1.
DR   Pfam; PF07885; Ion_trans_2; 1.
PE   4: Predicted;
SQ   SEQUENCE   1111 AA;  127503 MW;  06429EFCCC19716E CRC64;
     MVDLESEVPP LPPRYRFRDL LLGDQGWQND DRVQVEFYMN ENTFKERLKL FFIKNQRSSL
     RIRLFNFSLK LLSCLLYIIR VLLEKPSQGS EWSHIFWVNR SLPLWGLQVS VALISLFETI
     LLGYLSYKGN IWEQILRIPF ILEIINAVPF IISIFWPTLR NLFVPVFLNC WLAKHALENM
     INDLHRAIQR TQSAMFNQVL ILISTLLCLI FTCICGIQHL ERIGKKLNLF DSLYFCIVTF
     STVGFGDVTP ETWSSKLFVV AMICVALVVL PIQFEQLAYL WMERQKSGGN YSRHRAQTEK
     HVVLCVSSLK IDLLMDFLNE FYAHPRLQDY YVVILCPTEM DVQVRRVLQI PMWSQRVIYL
     QGSALKDQDL LRAKMDNAEA CFILSSRCEV DRTSSDHQTI LRAWAVKDFA PNCPLYVQIL
     KPENKFHIKF ADHVVCEEEF KYAMLALNCI CPATSTLITL LVHTSRGQEG QQSPEQWQKT
     YGRCSGNEVY HIVLEESTFF AEYEGKSFTY ASFHAHKKFG VCLVGVRRED NKNILLNPGP
     RYIMNASDIC FYINITKEEN SAFKNQDQQR KSNVSRSFYH GPSRLPVHSI IASMGTVAID
     LQDTSCRATS GPTLALPSEG GKELRRPSIA PVLEVADTSS IQTCDLLSDQ SEDETTPDEE
     TSSNLEYAKG YPPYSPYIGS SPTFCHLLQE KVPFCCLRLD KSCQHNYYED AKAYGFKNKL
     IIVAAETAGN GLYNFIVPLR AYYRPKKELN PIVLLLDNPL DDLLRCGVTF AANMVVVDKE
     STMSAEEDYM ADAKTIVNVQ TLFRLFSSLS IITELTHPAN MRFMQFRAKD CYSLALSKLE
     KKERERGSNL AFMFRLPFAA GRVFSISMLD TLLYQSFVKD YMISITRLLL GLDTIPGSGF
     LCSMKITEDD LWIRTYARLY QKLCSSTGDV PIGIYRTESQ KLTTSESQIS ISVEEWEDTK
     DVKDPGHHRS LHRNSTSSDQ SDHPLLRRKS MQWARRLSRK GPKHSGKTAE KITQQRLNLY
     RRSERQELAE LVKNRMKHLG LSTVGYDEMN DHQSTLSYIL INPSPDTRLE LNDVVYLIRP
     DPLSYLPNSE PSRKNSICNA AVQDSREETQ L
//
ID   D3YTV8_MOUSE            Unreviewed;      1878 AA.
AC   D3YTV8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Ank1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC115361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC126445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00882025; -.
DR   Ensembl; ENSMUST00000118733; ENSMUSP00000112850; ENSMUSG00000031543.
DR   MGI; MGI:88024; Ank1.
DR   GeneTree; ENSGT00600000084024; -.
DR   OrthoDB; EOG418BMG; -.
DR   Bgee; D3YTV8; -.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0048821; P:erythrocyte development; IMP:MGI.
DR   GO; GO:0015672; P:monovalent inorganic cation transport; IMP:MGI.
DR   GO; GO:0006779; P:porphyrin biosynthetic process; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR000488; Death.
DR   InterPro; IPR011029; DEATH-like.
DR   InterPro; IPR000906; ZU5.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 3.
DR   Gene3D; G3DSA:1.10.533.10; DEATH_like; 1.
DR   Pfam; PF00023; Ank; 18.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF00791; ZU5; 1.
DR   SMART; SM00248; ANK; 23.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00218; ZU5; 1.
DR   SUPFAM; SSF48403; ANK; 2.
DR   SUPFAM; SSF47986; DEATH_like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 20.
DR   PROSITE; PS50017; DEATH_DOMAIN; 1.
DR   PROSITE; PS51145; ZU5; 1.
PE   4: Predicted;
KW   ANK repeat; Repeat.
SQ   SEQUENCE   1878 AA;  205853 MW;  2A004DEB7FEAAC46 CRC64;
     MAERPRRSGS DPAADAATSF LRAARSGNLD KALDHLRNGV DINTCNQNGL NGLHLASKEG
     HVKMVVELLH KEIILETTTK KGNTALHIAA LAGQDEVVRE LVNYGANVNA QSQKGFTPLY
     MAAQENHLEV VKFLLENGAN QNVATEDGFT PLAVALQQGH ENVVAHLINY GTKGKVRLPA
     LHIAARNDDT RTAAVLLQND PNPDVLSKTG FTPLHIAAHY ENLNVAQLLL NRGASVNFTP
     QNGITPLHIA SRRGNVIMVR LLLDRGAQIE TRTKDELTPL HCAARNGHVR ISEILLDHGA
     PIQAKTKNGL SPIHMAAQGD HLDCVRLLLQ YNAEIDDITL DHLTPLHVAA HCGHHRVAKV
     LLDKGAKPNS RALNGFTPLH IACKKNHIRV MELLLKTGAS IDAVTESGLT PLHVASFMGH
     LPIVKNLLQR GASPNVSNVK VETPLHMAAR AGHTEVAKYL LQNKAKANAK AKDDQTPLHC
     AARIGHTGMV KLLLENGASP NLATTAGHTP LHTAAREGHV DTALALLEKE ASQACMTKKG
     FTPLHVAAKY GKVRLAELLL EHDAHPNAAG KNGLTPLHVA VHHNNLDIVK LLLPRGGSPH
     SPAWNGYTPL HIAAKQNQIE VARSLLQYGG SANAESVQGV TPLHLAAQEG HTEMVALLLS
     KQANGNLGNK SGLTPLHLVS QEGHVPVADV LIKHGVTVDA TTRMGYTPLH VASHYGNIKL
     VKFLLQHQAD VNAKTKLGYS PLHQAAQQGH TDIVTLLLKN GASPNEVSSN GTTPLAIAKR
     LGYISVTDVL KVVTDETSVV LVSDKHRMSY PETVDEILDV SEDEGTAHIS IMGDELVGSK
     AERRDSRDVG EEKELLDFVP KLDQVVESPA IPRIPCVTPE TVVIRSEDQE QASKEYDEDS
     LIPSSPATET SDNISPVASP VHTGFLVSFM VDARGGSMRG SRHNGLRVVI PPRTCAAPTR
     ITCRLVKPQK LNTPPPLAEE EGLASRIIAL GPTGAQFLSP VIVEIPHFAS HGRGDRELVV
     LRSENGSVWK EHKSRYGESY LDQILNGMDE ELGSLEELEK KRVCRIITTD FPLYFVIMSR
     LCQDYDTIGP EGGSLRSKLV PLVQATFPEN AVTKKVKLAL QAQPVPDELV TKLLGNQATF
     SPIVTVEPRR RKFHRPIGLR IPLPPSWTDN PRDSGEGDTT SLRLLCSVIG GTDQAQWEDI
     TGTTKLIYAN ECANFTTNVS ARFWLSDCPR TAEAVHFATL LYKELTAVPY MAKFVIFAKM
     NDAREGRLRC YCMTDDKVDK TLEQHENFVE VARSRDIEVL EGMPLFAELS GNLVPVKKAA
     QQRSFHFQSF RENRLAIPVK VRDSSREPGG FLSFLRKTMK YEDTQHILCH LNITMPPCTK
     GSGAEDRRRT LTPLTLRYSI LSESRLGFTS DTDRVEMRMA VIREHLGLSW AELARELQFS
     VEDINRIRVE NPNSLLDQST ALLTLWVDRE GENAKMENLY TALRNIDRSE IVNMLEGSGR
     QSRNLKPERR HGDREYSLSP SQVNGYSSLQ DELLSPASLQ YALPSPLCAD QYWNEVAVID
     AIPLAATEHD TMLEMSDMQV WSAGLTPSLV TAEDSSLECS KAEDSDAIPE WKLEGAHSED
     TQGPELGSQD LVEDDTVDSD ATNGLADLLG QEEGQRSEKK RQEVSGTEQD TETEVSLVSG
     QQRVHARITD SPSVRQVLDR SQARTLDWDK QGSTAVHPQE ATQSSWQEEV TQGPHSFQRR
     ITTIQGPEPG ALQEYEQVLV STREHVQRGP PETGSPKAGK EPSLWAPESA FSQEVQGDEL
     QNIPGEQVTE EQFTDEQGNI VTKKIIRKVV RQVDSSGAID TQQHEEVELR GSGLQPDLIE
     GRKGAQIVKR ASLKRGKQ
//
ID   D3YU59_MOUSE            Unreviewed;      1083 AA.
AC   D3YU59;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Limch1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Contains 1 LIM zinc-binding domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC119834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC152416; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC158994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00881328; -.
DR   Ensembl; ENSMUST00000119854; ENSMUSP00000112651; ENSMUSG00000037736.
DR   MGI; MGI:1924819; Limch1.
DR   GeneTree; ENSGT00530000063559; -.
DR   Bgee; D3YU59; -.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0031032; P:actomyosin structure organization; IEA:InterPro.
DR   InterPro; IPR001997; Calponin.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR001781; Znf_LIM.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 1.
DR   Gene3D; G3DSA:2.10.110.10; Znf_LIM; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF00412; LIM; 1.
DR   PRINTS; PR00889; CALPONIN.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00132; LIM; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE   4: Predicted;
KW   LIM domain; Metal-binding; Zinc.
SQ   SEQUENCE   1083 AA;  120993 MW;  44293770E9917A00 CRC64;
     MACPALGLEV LQPLQPEPPP EPAFAEAQKW IEQVTGRSFG DKDFRTGLEN GILLCELLNA
     IKPGLVKKIN RLPTPIAGLD NTILFLRGCK ELGLKESQLF DPSDLQDTSN RVTVKNLDYS
     RKLKNVLVTI YWLGKAANSC ASYGGTTLNL KEFEGLLAQM RKETDDIDSP KRSIRDSGYI
     DCWDSERSDS LSPPRHGRDD SFDSLDSFGS RSRQTPSPDV VLRGSSDGRG SDSESDLPHR
     KLPDVKKDDM SARRTSHGEP KSAVPFNQYL PNKSNQTAYV PAPLRKKKAE REEFRKSWST
     ATSPLGGERP FRYGPRTPVS DDAESTSMFD MRCEEEAAVL PHSRARQEQL QLINNQLREE
     DDKWQDDLAR WKSRRRSASQ DLIKKEEERK KMEKLMSGED GTSERRKSIK TYREIVQEKE
     RRERELHEAY KNARSQEEAE GILQQYIERF TISEAVLERL EMPKILERSH STEPNVSSFP
     NDPSPMKYLR QQSLPPPKFT ATVETTIART SVPESIASAG TGSPSKIITP NTVPMLTPRP
     YSQPKNSQEV LKTFKVDGKV SMNGEMAPGD EEGKEKEGPA AAAPGPSLTK SQMFEGVATV
     HDSPVQVKQG SNSIEINIKK PNSAPQELTA ASEETESNGQ EDEDGEERPG TGDLEPDSAE
     PQHFTTTVTR CSPTVALVEF SSNPQLKNEV PEQGQKKPED EMSGKVELVL SQKVAKPKSP
     EPEATLTFPF LDKMPETNQL HLPNPSSQAD SPSSEKSPGS TPFKFWAWDP EEERRRQEKW
     QQEQERLLQE RYQKEQDKLK EEWEKAQKEV EEEERRYYEE ERKIIEDTVV PFTISSSSAD
     QLSTSLSVTE GSGTRNKMDL ENCPDKENER RQKTPFQEND GDSLLKTREG GLPEEQSLTP
     SPSANPEISV SKGIHQDPQL EAEAGAPHCG TNPQPAQDPP RNQQIPNPPT STSEDVKPKT
     LALEKTINHQ MESPGERRKK NPRENFRAGP LSPCPPTPPG QSPNRSISGK KLCSSCGLTL
     GKGAAMIIET LNLYFHIQCF RCGICKGQLG DAVSGTDVRI RNGLLNCTDC YMRSRSAGQP
     TTL
//
ID   D3YU90_MOUSE            Unreviewed;      1168 AA.
AC   D3YU90;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Ms4a14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC134839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00403035; -.
DR   ProteinModelPortal; D3YU90; -.
DR   Ensembl; ENSMUST00000067600; ENSMUSP00000063691; ENSMUSG00000024671.
DR   MGI; MGI:2686122; Ms4a14.
DR   GeneTree; ENSGT00590000083163; -.
DR   OrthoDB; EOG4V4374; -.
DR   Bgee; D3YU90; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   InterPro; IPR007237; CD20-like.
DR   Pfam; PF04103; CD20; 1.
PE   4: Predicted;
SQ   SEQUENCE   1168 AA;  130410 MW;  3501FE989F55FF4E CRC64;
     MESPSEEKRR NHVITIDPNE TVLTAYPYRP HSSLLDFLKG EPKLLGAIQI LLSLVIVGFG
     NILALNFTFS SKEFPLVILT GYPFWGAVIF LLTGLVTMSH DKPRRILKQG VTTMNVLSSL
     TALAGIALTL LSFTQQHRVC QTPSLEGPCV VGETLLLGIL SVLLIITIVE LSISVTVVSL
     RSRCWTSPRE AVFFFPSEGA QNTEHPAPEE NNTLQFEFQE KSSKDNTASS IKSVFLGGYA
     FFKLRVSRIS STPKTIQQKS DKGTSFMYVP EEQEATPPLS PEQEIKLNAL PPPLTPYPSE
     NIPSQKDSTT DHLNDADLSS IIHQTSDMQS NLLDYENASV TRFKTPSSHN SLHFSPANLS
     SQSLMASLST QVLQYKQPSF HISQSYDLIS EYFLSENIPF QDNQSQDTPS QYTPSQDIQF
     QDMLAQDISF QGTPYQDLPY QVLLIKDTSP QGTPYQYILT KEIPFQETPS QGTLSQESPS
     QWTLSKGTPS QGTSPKGTPS QVTPPQGTPS QGTPSEGTSL QVSPSEVTPP QGTPSEVTPS
     QGTPSEGTSL QVSPSEVTPP QGTPSEMTPP QGTPSEGTSP QGTPSEETPP QGTPSEGTLP
     QGTPSQGTPP QGTPSEGTPP QGTPSQGTPP QGTPPQGTPS EGTPSQETVP QETPPQKLSF
     QDILTKDRSS QETAYQETPF QDLVTQNRPS QDSQYKETPS QEIFFQDTPF QNTPSQNIQY
     QDILSQDKIS QGSQTQNSVS QEMASSDLQV LNTQVQIQQY PEVFYRDIRT EVMELTQEWK
     SNQGKKPTRR LSLSLPGKHG QVHPKRYSVD LQVKSEKPRR YSEDLQSKTS RRKSIDQQIK
     AWISPKKNTT EKQDAYTQTT DQQADDQQAK EEVPVQQSQD EQIKDQKSIE NLLPEEHPND
     REDEGQQSDK EQPPEEQAQV QPVEDQQPKE QKAPNTQLQN WQGGQVLVKR APRQLCDNWE
     TQSFQFTEKS CSFWSTPSWQ PISQRSQDWI SQGWRNKDWK AQEWQFEVKP SLDWESQELL
     ERESLRQRAL YQQIQPQTTI VHQTPGHQLQ NYIFQVGLCQ GSRQQDSESG VLIEDVNEDD
     VQSREREPEN TEETCQKPTD QQSEDMRPDN YPVSCQSLVP YTYVTCLSNI ASEQEVQNNT
     PCSGSSKDLN TTSSTSYQRD QQQSEDSD
//
ID   D3YUI4_MOUSE            Unreviewed;       189 AA.
AC   D3YUI4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 9.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Camk2a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC124431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00830424; -.
DR   Ensembl; ENSMUST00000039904; ENSMUSP00000048325; ENSMUSG00000024617.
DR   MGI; MGI:88256; Camk2a.
DR   GeneTree; ENSGT00550000074354; -.
DR   Bgee; D3YUI4; -.
DR   GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:InterPro.
DR   GO; GO:0035254; F:glutamate receptor binding; IPI:MGI.
DR   GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; IMP:MGI.
DR   GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:MGI.
DR   GO; GO:0046928; P:regulation of neurotransmitter secretion; IMP:MGI.
DR   InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
DR   Pfam; PF08332; CaMKII_AD; 1.
PE   4: Predicted;
SQ   SEQUENCE   189 AA;  21351 MW;  0C7607B4B01BA49C CRC64;
     MLLFLTLWAL VPCLVLLTLY FLSSTGGKSG GNKKNDGVKE SSESTNTTIE DEDTKVRKQE
     IIKVTEQLIE AISNGDFESY TKMCDPGMTA FEPEALGNLV EGLDFHRFYF ENLWSRNSKP
     VHTTILNPHI HLMGDESACI AYIRITQYLD AGGIPRTAQS EETRVWHRRD GKWQIVHFHR
     SGAPSVLPH
//
ID   D3YUJ3_MOUSE            Unreviewed;       367 AA.
AC   D3YUJ3;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Ccnyl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Belongs to the cyclin family.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC101915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00753875; -.
DR   Ensembl; ENSMUST00000114077; ENSMUSP00000109711; ENSMUSG00000070871.
DR   MGI; MGI:2138614; Ccnyl1.
DR   GeneTree; ENSGT00390000006626; -.
DR   OrthoDB; EOG4NS3BZ; -.
DR   Bgee; D3YUJ3; -.
DR   InterPro; IPR006670; Cyclin.
DR   InterPro; IPR011028; Cyclin-like.
DR   InterPro; IPR013763; Cyclin-related.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR012399; UCP_CG14939_cyclin-contain.
DR   Gene3D; G3DSA:1.10.472.10; Cyclin_related; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   PIRSF; PIRSF028934; Cyclin_CG14939; 1.
DR   SMART; SM00385; CYCLIN; 1.
DR   SUPFAM; SSF47954; Cyclin_like; 1.
PE   3: Inferred from homology;
KW   Cyclin.
SQ   SEQUENCE   367 AA;  41600 MW;  C161CD6B38BEE3F8 CRC64;
     METRIRAAQL KGRGGAFPKL GRRAGPAEPD YESEVYEAAA GDAVAVAPAP AAAVEPAELD
     FGAGEGHHLQ HISDREMPED LALESNPSDH PRASTIFLSK SQTDVREKRK SNHLNHVSPG
     QLTKKYSSCS TIFLDDSTVS QPNLRTTIKC VTLAIYYHIK NRDANRSLDI FDERSHPLTR
     EKVPEEYFKH DPEHKFIYRF VRTLFSAAQL TAECAIVTLV YLERLLTYAE IDICPTNWKR
     IVLGAILLAS KVWDDQAVWN VDYCQILKDI TVEDMNEMER HFLELLQFNI NVPASVYAKY
     YFDLRSLADD NNLNFLFAPL SKERAQNLEA ISRLCEDKYK DLCRAAMRRS LSADNFIGIQ
     RSNAILS
//
ID   D3YUJ4_MOUSE            Unreviewed;       529 AA.
AC   D3YUJ4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 9.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Cpeb2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC105174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00856695; -.
DR   Ensembl; ENSMUST00000114066; ENSMUSP00000109700; ENSMUSG00000039782.
DR   MGI; MGI:2442640; Cpeb2.
DR   GeneTree; ENSGT00390000012886; -.
DR   Bgee; D3YUJ4; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0008187; F:poly-pyrimidine tract binding; IDA:MGI.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   4: Predicted;
SQ   SEQUENCE   529 AA;  59573 MW;  1B254AE12E610363 CRC64;
     MNLPQQQPPA AAPQQPQSRR SPVSPQLQQQ HQAAAAAFLQ QRNSYNHHQP LLKQSPWSNH
     QNSGWGTASM SWGAMHGRDH RRSGNMGIPG TMNQISPLKK PFSGNVIAPP KFTRSTPSLT
     PKSWIEDNVF RTDNNSNTLL PLQDRSRMYD SLNMHSLENS LIDIMRAEHD PLKGRLSYPH
     PGTDNLLMLN AHIAFRVTDI WMCGLGFSSN ILQFVLCLHA ARSYGRRRGR SSLFPIDDSL
     LDDGHSDQVG VLNSPTCYSA HQNGERIERF SRKVFVGGLP PDIDEDEITA SFRRFGPLVV
     DWPHKAESKS YFPPKGYAFL LFQEESSVQA LIDACIEEDG KLYLCVSSPT IKDKPVQIRP
     WNLSDSDFVM DGSQPLDPRK TIFVGGVPRP LRAVELAMIM DRLYGGVCYA GIDTDPELKY
     PKGAGRVAFS NQQSYIAAIS ARFVQLQHGD IDKRVEVKPY VLDDQMCDEC QGARCGGKFA
     PFFCANVTCL QYYCEFCWAN IHSRAGREFH KPLVKEGADR PRQIHFRWN
//
ID   D3YUP9_MOUSE            Unreviewed;       897 AA.
AC   D3YUP9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 9.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Adam22;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Contains 1 disintegrin domain.
CC   -!- SIMILARITY: Contains 1 peptidase M12B domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC140364; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC152165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC156022; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00515396; -.
DR   Ensembl; ENSMUST00000115386; ENSMUSP00000111044; ENSMUSG00000040537.
DR   MGI; MGI:1340046; Adam22.
DR   GeneTree; ENSGT00590000083076; -.
DR   Bgee; D3YUP9; -.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR   GO; GO:0022011; P:myelination in peripheral nervous system; IMP:MGI.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR001762; Blood-coag_inhib_Disintegrin.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   Gene3D; G3DSA:4.10.70.10; Blood-coag_inhib_Disintegrin; 1.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SMART; SM00181; EGF; 1.
DR   SUPFAM; SSF57552; Disintegrin; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   4: Predicted;
SQ   SEQUENCE   897 AA;  99559 MW;  83B1F02FFCBFD8C2 CRC64;
     MQAAAAASFW LLCVLGTCPL ARCGRAGVAS LKGLERGKEN RFLERQSIIP LRLIYRLGGE
     DETQHNQLDT RVRGDPGGPQ LTHVDKASFR VDAFGTSFVL DVLLNHELLS SGYVERQIEH
     GGKVVENKGG EHCYYQGQIR GNPVSFVALS TCHGLHGMFY DGNHTYLIEP EENEKSQESS
     HCHSVYKSRQ FEFPLDDLPS EFQRVNITPP QFILKPRLKR RKRQLLRFPR NVEEETKYIE
     LMIVNDHLMF KKHRLSVVYT NTYAKSVVNM ADVIYKDQLK TRIVLVAMET WAADNKFAIS
     ENPLITLREF MKYRRDFIKE KADAVHLFSG SQFESSRSGA AYIGGICSLL RGGGVNEFGK
     TDLMAVTLAQ SLAHNVGIIS DKRKLASGEC KCEDTWSGCI MGDTGYYLPK KFTQCNVEEY
     HDFLNSGGGA CLFNKPSKLL DPPECGNGFI ETGEECDCGT PAECALEGAE CCKKCTLTQD
     SQCSDGLCCK KCKFQPLGTV CREAVNDCDI REICSGNSSQ CAPNVHKMDG YSCDGTQGIC
     FGGRCKTRDR QCKYIWGQKV TASDRYCYEK LNIEGTEKGN CGKDKDTWTQ CNKRDVLCGY
     LLCTNIGNIP RLGELDGEIT STLVVQQGRT LNCSGAHVKL EEDVDLGYVE DGTPCGPQMM
     CLEHRCLPVA SFNFSTCSSS KAGTVCSGNG VCSNELKCVC NRHWTGADCG THFPHNDDAK
     TGITLSGNGV AGTNIIIGII AGTILVLALI LGITAWGYKN YREQRSNGLS HSWSERIPDT
     KHISDICENG RPRSNSWQGN MGGNKKKIRG KRFRPRSNST EYLNPWFKRD YNVAKWVEDV
     NKNTEGPYFR TLSPAKSPSS STGSIASSRK YPYPMPPLPD EGKTAGRQSA RLWETSI
//
ID   D3YUS5_MOUSE            Unreviewed;      1261 AA.
AC   D3YUS5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 10.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Rasal2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC119220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC119897; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC138382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00919009; -.
DR   Ensembl; ENSMUST00000132699; ENSMUSP00000114964; ENSMUSG00000070565.
DR   MGI; MGI:2443881; Rasal2.
DR   GeneTree; ENSGT00600000084217; -.
DR   Bgee; D3YUS5; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR021887; DUF3498.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001936; RasGAP.
DR   InterPro; IPR023152; RasGAP_CS.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Gene3D; G3DSA:1.10.506.10; RasGAP; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF12004; DUF3498; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00616; RasGAP; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00323; RasGAP; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE   4: Predicted;
KW   GTPase activation.
SQ   SEQUENCE   1261 AA;  142011 MW;  9752F05E0C2202D1 CRC64;
     MFTGLESDSP LPPEDLDAVV PVSGAVAGGM LDRILLESVC QQQSWVRVFD VKGPPTHRLS
     CGQSPYTETT SWERKYCILT DSQLVLLNKE KEMPVEGQDQ QTDSTKGRCL RRTVSVPSEG
     QFPEYPQEGT TKLEVPAERS PRRRSISGTS TSEKPNSMDT ANTSPFKVPG FFSKRLKGSI
     KRTKSQSKLD RNTSFRLPSL RNADDRSRGL PKLKESRSHE SLLSPCSAVE CLDLGRGEPV
     SVKPLHSSIL GQDFCFEVTY LSGSKCFSCS SASERDKWME NLRRTVQPNK DNCRRAENVL
     RLWIIEAKDL APKKKYFCEL CLDDTLFART TSKTKADNIF WGEHFEFYSL PPLHSITVHI
     YKDVEKKKKK DKNNYVGLVN IPTASVTGRQ FVEKWYPVST PTPNKGKTGG PSIRIKSRFQ
     TITILPMEQY KEFAEFITSN YTMLCSVLEP VISVRNKEEL ACALVHILQS TGRAKDFLTD
     LVMSEVDRCG EHDVLIFREN TIATKSIEEY LKLVGQQYLH DALGEFIKAL YESDENCEVD
     PSKCSSSELM DHQSNLKMCC ELAFCKIINS YCVFPRELKE VFASWKQQCL NRGKQDISER
     LISASLFLRF LCPAIMSPSL FNLMQEYPDD RTSRTLTLIA KVIQNLANFA KFGNKEEYMA
     FMNDFLEHEW GGMKRFLLEI SNPDTISNTP GFDGYIDLGR ELSVLHSLLW EVVSQLDKAT
     VAKLGPLPRV LADITKSLTN PTPIQQQLRR FAEHSSSPNV SGSLSSGLQR ICEDPTDSDL
     HKLKSPSQDN TDSYFRGKTL LLVQQASSQS MTYSEKDEKE NSLPNGRSIS LMDLQDTHAA
     QAEHASVMLD VPMRLAGSQL SITQVASIKQ LRETQSTPQS APQVRRPLHP ALNQPGSLQP
     LSFQNPVYHL NNPVPAMPKA SADSSLENLS TASSRSQSNS EDFKLSGPSN SSMEDFTKRS
     SHSEDFSRRH TVPDRHIPLA LPRQNSTGQS QIRKLDHSGL GARAKAPPSL PHSASLRSTG
     SMSVASAALM AEPVQNGSRS RQQSSSSRES PVPKVRAIQR QQTQQVQSPV DSATMSPVER
     TAAWVLNNGQ YEEDVEETEQ NQDEAKHAEK YEQEITKLKE RLRVSSRRLE EYERRLLVQE
     QQMQKLLLEY KARLEDSEER LRRQQEEKDS QMKSIISRLM AVEEELKKDH AEMQAVIDAK
     QKIIDAQEKR IVSLDSANTR LMSALTQVKE RYSMQVRNGI SPTNPTKLSI TENGEFKNSS
     C
//
ID   D3YUY7_MOUSE            Unreviewed;       121 AA.
AC   D3YUY7;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 9.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Trim3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC125227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00775876; -.
DR   Ensembl; ENSMUST00000057525; ENSMUSP00000053384; ENSMUSG00000036989.
DR   Ensembl; ENSMUST00000106789; ENSMUSP00000102401; ENSMUSG00000036989.
DR   Ensembl; ENSMUST00000106791; ENSMUSP00000102403; ENSMUSG00000036989.
DR   Ensembl; ENSMUST00000106792; ENSMUSP00000102404; ENSMUSG00000036989.
DR   Ensembl; ENSMUST00000147044; ENSMUSP00000114822; ENSMUSG00000036989.
DR   Ensembl; ENSMUST00000153371; ENSMUSP00000119910; ENSMUSG00000036989.
DR   MGI; MGI:1860040; Trim3.
DR   GeneTree; ENSGT00550000074377; -.
DR   Bgee; D3YUY7; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding; Zinc; Zinc-finger.
SQ   SEQUENCE   121 AA;  13421 MW;  0037722F090F8A04 CRC64;
     MAKREDSPGP EVQPMDKQFL VCSICLDRYR CPKVLPCLHT FCERCLQNYI PPQSLTLSCP
     VCRQTSILPE QGVSALQNNF FISSLMEAMQ QAPEGAHDPE DPHPLSAVAG RPLSCPNHEG
     K
//
ID   D3YUZ8_MOUSE            Unreviewed;       755 AA.
AC   D3YUZ8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Dlg2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC   -!- SIMILARITY: Contains 3 PDZ (DHR) domains.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC108832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC109506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC118621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC119218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC121261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC127299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC127683; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC141890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC161490; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC162304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00775854; -.
DR   Ensembl; ENSMUST00000107193; ENSMUSP00000102811; ENSMUSG00000052572.
DR   MGI; MGI:1344351; Dlg2.
DR   GeneTree; ENSGT00560000076879; -.
DR   Bgee; D3YUZ8; -.
DR   GO; GO:0044224; C:juxtaparanode region of axon; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR   GO; GO:0007268; P:synaptic transmission; IMP:MGI.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR016313; M-assoc_guanylate_kinase.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR019583; PDZ_assoc.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF00595; PDZ; 3.
DR   Pfam; PF10600; PDZ_assoc; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   PIRSF; PIRSF001741; MAGUK_DLGH; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 3.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50156; PDZ; 3.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 3.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
SQ   SEQUENCE   755 AA;  83951 MW;  F4B8C83333CC0EE3 CRC64;
     MLPTFDMQRP SASRAENYQL LWDTIASLKQ CEEAMQHAFI PVNGTEIEYE FEEITLERGN
     SGLGFSIAGG TDNPHIGDDP GIFITKIIPG GAAAEDGRLR VNDCILRVNE VDVSEVSHSK
     AVEALKEAGS IVRLYVRRRR PILETVVEIK LFKGPKGLGF SIAGGVGNQH IPGDNSIYVT
     KIIDGGAAQK DGRLQVGDRL LMVNNYSLEE VTHEEAVAIL KNTSDVVYLK VGKPTTIYMT
     DPYGPPDITH SYSPPMENHL LSGNNGTLEY KTSLPPISPG RYSPIPKHML GEDDYTSHSQ
     HSTATRQPSV TLQRAISLEG EPRKVVLHKG STGLGFNIVG GEDGEGIFVS FILAGGPADL
     SGELQRGDQI LSVNGIDLRG ASHEQAAAAL KGAGQTVTII AQYQPEDYAR FEAKIHDLRE
     QMMNHSMSSG SGSLRTNQKR SLYVRAMFDY DKSKDSGLPS QGLSFKYGDI LHVINASDDE
     WWQARRVTLD GDSEEMGVIP SKRRVERKER ARLKTVKFNA KPGVIDSKGD IPGLGDDGYG
     TKTLRGQEDL ILSYEPVTRQ EINYTRPVII LGPMKDRIND DLISEFPDKF GSCVPHTTRP
     KRDYEVDGRD YHFVISREQM EKDIQEHKFI EAGQYNDNLY GTSVQSVRFV AERGKHCILD
     VSGNAIKRLQ VAQLYPIAIF IKPKSLEPLM EMNKRLTEEQ AKKTYDRAIK LEQEFGEYFT
     AIVQGDTLED IYNQCKLVIE EQSGPFIWIP SKEKL
//
ID   D3YV69_MOUSE            Unreviewed;       175 AA.
AC   D3YV69;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Rab6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC124531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00757748; -.
DR   Ensembl; ENSMUST00000098252; ENSMUSP00000095852; ENSMUSG00000030704.
DR   Ensembl; ENSMUST00000107048; ENSMUSP00000102663; ENSMUSG00000030704.
DR   MGI; MGI:894313; Rab6.
DR   GeneTree; ENSGT00600000084341; -.
DR   Bgee; D3YV69; -.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Nucleotide-binding.
SQ   SEQUENCE   175 AA;  19962 MW;  1667A3BFAE94E983 CRC64;
     MYDSFDNTYQ ATIGIDFLSK TMYLEDRTIR LQLWDTAGQE RFRSLIPSYI RDSAAAVVVY
     DITNVNSFQQ TTKWIDDVRT ERGSDVIIML VGNKTDLADK RQVSIEEGER KAKELNVMFI
     ETSAKAGYNV KQLFRRVAAA LPGMESTQDR SREDMIDIKL EKPQEQPVNE GGCSC
//
ID   D3YVA3_MOUSE            Unreviewed;        90 AA.
AC   D3YVA3;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Scrib;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC116487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00830262; -.
DR   Ensembl; ENSMUST00000148211; ENSMUSP00000114573; ENSMUSG00000022568.
DR   MGI; MGI:2145950; Scrib.
DR   GeneTree; ENSGT00600000084222; -.
DR   Bgee; D3YVA3; -.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0008105; P:asymmetric protein localization; IMP:MGI.
DR   GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR   GO; GO:0042060; P:wound healing; IGI:MGI.
PE   4: Predicted;
SQ   SEQUENCE   90 AA;  9225 MW;  170BA24EEF7485D1 CRC64;
     MLGDHCQNGP SATTGGKTTE APCSPGSQQT KPGVIQPLAQ AWPRNSPAPR GRGGPCSPPS
     PDELPANVKQ AYRAFAAVPT VHPPENSATQ
//
ID   D3YVE8_MOUSE            Unreviewed;       412 AA.
AC   D3YVE8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 10.
DE   SubName: Full=MCG51522;
DE   SubName: Full=Uncharacterized protein;
GN   Name=Tmem22; ORFNames=mCG_51522;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; AC129223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466560; EDL21032.1; -; Genomic_DNA.
DR   IPI; IPI00659583; -.
DR   RefSeq; NP_001094953.1; NM_001101483.1.
DR   UniGene; Mm.236289; -.
DR   ProteinModelPortal; D3YVE8; -.
DR   Ensembl; ENSMUST00000093792; ENSMUSP00000091308; ENSMUSG00000070287.
DR   GeneID; 245020; -.
DR   KEGG; mmu:245020; -.
DR   CTD; 245020; -.
DR   MGI; MGI:2685365; Tmem22.
DR   GeneTree; ENSGT00510000048315; -.
DR   OrthoDB; EOG40P46S; -.
DR   Bgee; D3YVE8; -.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   InterPro; IPR000620; DMT.
DR   Pfam; PF00892; DUF6; 2.
PE   4: Predicted;
SQ   SEQUENCE   412 AA;  46395 MW;  975066E4E68A7E4D CRC64;
     MDTSPSKKYP IKKRVKIHPN TVMVKYTSHY PQPGDDGYEE INEDYGRFME ENPKKSLLSE
     MRRKGRTLFG TMDTQPSSSE DPRASGMGQF QSFAEKNIFQ SRKMWLVLFG SALAHGCVAL
     ITRLISDRSK VPSLELIFIR SVLQVLSVIV VCYYQEAPFG PSGYRLRLFF YGVCNVISIT
     CAYTSFSIVP PSNGTTMWRA TTTVFSAILA FLLVDEKMAY VDMATVVCSI LGVCLVMIPN
     IADEDNSLLN AWKEAFGYTM TVMAGLTTAL SMIVYRSIRE KISMWTALFT FGWTGTIWGL
     STMFVLQEPI IPLDGATWSY LIAICLCSTA AFLGVYYALD KFHPALVSTV QHLEIVVAMV
     LQLLVLHIFP SVYDVFGGVI IMISVFVLAG YKLYWRNVRR EDYQEILDSP IK
//
ID   D3YVV2_MOUSE            Unreviewed;       517 AA.
AC   D3YVV2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Myo5b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC147992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC148001; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC148002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00881560; -.
DR   ProteinModelPortal; D3YVV2; -.
DR   Ensembl; ENSMUST00000120161; ENSMUSP00000114038; ENSMUSG00000025885.
DR   MGI; MGI:106598; Myo5b.
DR   GeneTree; ENSGT00590000082740; -.
DR   Bgee; D3YVV2; -.
DR   GO; GO:0016459; C:myosin complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003774; F:motor activity; IEA:InterPro.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00242; MYSc; 1.
PE   4: Predicted;
SQ   SEQUENCE   517 AA;  59071 MW;  5E8829E9B65C3CC3 CRC64;
     MSYSELYTRY TRVWIPDPDE VWRSAELTKD YKEGDKSLQL RLEDDTILEY PVDVQNNQVP
     FLRNPDILVG ENDLTALSHL HEPAVLHNLK VRFLESNHIY TYCGIVLVAI NPYEQLPIYG
     QDVIYAYSGQ NMGDMDPHIF AVAEEAYKQM ARDEKNQSII VSGESGAGKT VSAKYAMRYF
     ATVGGSASDT NIEEKVLASS PIMEAIGNAK TTRNDNSSRF GKFIEIGFDK KYHIIGANMR
     TYLLEKSRVV FQADDERNYH IFYQLCAAAS LPEFKELALT CAEDFFYTAH GGNTTIEGVN
     DADDFEKTRQ ALTLLGVRDS HQISIFKIIA SILHLGSVEI QSERDGDSCS ISPQDEHLSN
     FCSLLGIEHS QMEHWLCHRK LVTTSETYVK TMSLQQVVNA RDALAKHIYA QLFSWIVEHI
     NKALHTSLKQ HSFIGVLDIY GFETFEINSF EQFCINYANE KLQQQFNSHV FKLEQEEYMK
     EQIPWTLIDF YDNQPCIDLI EAKLGILDLL DEECKTL
//
ID   D3YWE6_MOUSE            Unreviewed;      1297 AA.
AC   D3YWE6;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 9.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Mn1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC122226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC124749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00458368; -.
DR   RefSeq; NP_001074704.1; NM_001081235.1.
DR   UniGene; Mm.332576; -.
DR   Ensembl; ENSMUST00000094463; ENSMUSP00000092034; ENSMUSG00000070576.
DR   GeneID; 433938; -.
DR   KEGG; mmu:433938; -.
DR   CTD; 433938; -.
DR   MGI; MGI:1261813; Mn1.
DR   GeneTree; ENSGT00390000001777; -.
DR   OrthoDB; EOG4R5020; -.
DR   Bgee; D3YWE6; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0001957; P:intramembranous ossification; IMP:MGI.
DR   InterPro; IPR011989; ARM-like.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
PE   4: Predicted;
SQ   SEQUENCE   1297 AA;  134072 MW;  41130654703FF053 CRC64;
     MFGLDQFEPQ INSRHAGQGE GNFNEAGLSM NAHFKAPAFH AGPPTGPVDP AISALGEPPI
     LGLNMEPYGF HARSHSELHA GGLQAQPVHG FFGGQQPHHS HPGGHHPHQH HPHFGGNFGG
     PDPGASCLHG GRLLGYGGAA GGLGSQPPFA ESYEHMAESQ GPEGFGPQRP GNLPDFHSSG
     TSGHAVPAPC LPLDQSPNRA ASFHGLSASS GSDSHSLEPR RVTNQGAVDS LEYNYPSEPP
     SGHFDMFSPS DSEGQLPHYA AGRQVPGGAF PGASAMPRAS GMVGLSKMHS QPPQPPPQQQ
     QPQHGVFFER FGGARKMPVG LEPAVGSRHP LMQPPQQAPP PPQQPPPQQQ PPPPGLLVRQ
     NSCPPALPRP QQGEAGTPSG GLQDGGPMLP SQHAQFEYPI HRLENRSMHP YSEPVFSMQH
     PPPQQAPNQR LQHFDAPPYM NVAKRPRFDF PGSAGVDRCA SWNGSMHNGT LDNQLSPSAY
     PGLPGEFTPP VPDSFSSGPP LQHPGPDHQS LQQQQQQQQQ QQQQQQQQQQ QQQQQQQRQN
     AALMIKQMAS RNQQQRLRQP NLAQLGHPGD VGQGGLVHGG SVGGLAQTNF EREGGSAGAG
     RLSGFEQQAP HLAQESAWFP GPHPPGDLLP RRMGGAGLPT DCGPHDPALA PPPAPGGSGV
     LFRGSLQEPL RMPGEGHVPA LASPGLQFGG SLAGLGQLQS PGAGVGLPNA PSERRPPPPD
     FPAPALGGQP GFPFGSGSRQ ATPHSAPGVN SPPSAGSGSS GAGGGAYPPQ PDFQPSQRNS
     ASKLGALSLG SFNKPSSKDN LFGQSCLAAL STACQNMIAS LGAPNLNVTF NKKNPPEGKR
     KLSQNEPDSA VAAGNPGSDY FPGGTTPGAP GPGGPSGTSG GGSKASGPPN PPIQGDSTSL
     SPNYTLESTS GNDGKPVPGG SGRGRGRRKR DSGHVSPGTF FDKYSTAPDS GGAPGVSPGQ
     QQAPGSAAGG SSVNEARGPT PHEKALTSPS WGKGAELLLG DQPDLMASLD STAKSDGSSP
     HVGEFASDEV STSYANEDEV SSSSDNTTAL AKASRSPLVT SSPKLPPRGV GAGEHTPKAS
     ALGLGILSTS TSTPDSYGGG VGTGHPGTPG LEQVRTPTSS SGAQPPDEIH PLEILQAQIQ
     LQRQQFSISE DQPLGLKGSK KAECAVGASG AQNGDSELGS CCSEAVKSAM STIDLDSLMA
     EHSTTWYMPP DKALVDGGDE DKTLAPWEKA KSQNPNNKEA HDHPTNKASA TQPGSHLQCL
     TVHCTDGDPK ARTSVPTWRS LHSDISNRFG TFVAALT
//
ID   D3YWG9_MOUSE            Unreviewed;        75 AA.
AC   D3YWG9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 6.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Wdfy1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC083910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC170750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00762262; -.
DR   Ensembl; ENSMUST00000048820; ENSMUSP00000040224; ENSMUSG00000073643.
DR   Ensembl; ENSMUST00000113510; ENSMUSP00000109138; ENSMUSG00000073643.
DR   Ensembl; ENSMUST00000113511; ENSMUSP00000109139; ENSMUSG00000073643.
DR   Ensembl; ENSMUST00000113512; ENSMUSP00000109140; ENSMUSG00000073643.
DR   Ensembl; ENSMUST00000113513; ENSMUSP00000109141; ENSMUSG00000073643.
DR   Ensembl; ENSMUST00000113514; ENSMUSP00000109142; ENSMUSG00000073643.
DR   Ensembl; ENSMUST00000113515; ENSMUSP00000109143; ENSMUSG00000073643.
DR   Ensembl; ENSMUST00000125641; ENSMUSP00000118431; ENSMUSG00000073643.
DR   Ensembl; ENSMUST00000143368; ENSMUSP00000123303; ENSMUSG00000073643.
DR   MGI; MGI:1916618; Wdfy1.
DR   GeneTree; ENSGT00550000074629; -.
DR   Bgee; D3YWG9; -.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00320; WD40; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   4: Predicted;
KW   Repeat; WD repeat.
SQ   SEQUENCE   75 AA;  8277 MW;  62E5E259A00D9FE3 CRC64;
     MAAEIHSRPQ SSRPVLLSKI EGHQDAVTAA LLIPKEDGVI TASEDRTIRV WLKRDSGQYW
     PSIYHTMASP CSAMA
//
ID   D3YWH6_MOUSE            Unreviewed;       235 AA.
AC   D3YWH6;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Mapk8ip3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC166102; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00886364; -.
DR   Ensembl; ENSMUST00000146706; ENSMUSP00000118422; ENSMUSG00000024163.
DR   MGI; MGI:1353598; Mapk8ip3.
DR   GeneTree; ENSGT00600000084097; -.
DR   Bgee; D3YWH6; -.
DR   GO; GO:0030673; C:axolemma; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0005625; C:soluble fraction; IDA:MGI.
DR   GO; GO:0007257; P:activation of JUN kinase activity; IDA:MGI.
DR   GO; GO:0007411; P:axon guidance; IMP:MGI.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0048286; P:lung alveolus development; IMP:MGI.
DR   GO; GO:0060425; P:lung morphogenesis; IMP:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0008104; P:protein localization; IMP:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
DR   GO; GO:0007585; P:respiratory gaseous exchange; IMP:MGI.
PE   4: Predicted;
SQ   SEQUENCE   235 AA;  25136 MW;  3FB687659CF6E606 CRC64;
     MQQVGGSGQT ESSLPGRSPR QSWRKSRKER PTSLNVFPLA DGMCPNDEMS ESGQSSAAAT
     PSTTGTKSNT PTSSVPSAAV TPLNESLQPL GDYVSVTKNN KQAREKRNSR NMEVQVTQEM
     RNVSIGMGSS DEWSDVQDII DSTPELDVCP ETRLERTGSS PTQGIVNKAF GINTDSLYHE
     LSTAGSEVIG DVDEGADLLG EFSGMGKEVG NLLLENSQLL ETKNALNVVK NDLIA
//
ID   D3YWQ8_MOUSE            Unreviewed;       601 AA.
AC   D3YWQ8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 10.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Prkch;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC123940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC124179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00882014; -.
DR   Ensembl; ENSMUST00000119092; ENSMUSP00000112499; ENSMUSG00000021108.
DR   MGI; MGI:97600; Prkch.
DR   GeneTree; ENSGT00590000082973; -.
DR   Bgee; D3YWQ8; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004697; F:protein kinase C activity; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR014376; Prot_kin_PKC_delta.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF000551; PKC_delta; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   4: Predicted;
KW   ATP-binding; Kinase; Metal-binding; Nucleotide-binding; Repeat;
KW   Serine/threonine-protein kinase; Transferase; Zinc.
SQ   SEQUENCE   601 AA;  67971 MW;  67C7DBFEFF2E826B CRC64;
     MSSGTMKFNG YLRVRIGEAV GLQPTRWSLR HSLFKKGHQL LDPYLTVSVD QVRVGQTSTK
     QKTNKPTYNE EFCANVTDGG HLELAVFHET PLGYDHFVAN CTLQFQELLR TAGTSDTFEG
     WVDLEPEGKV FVVITLTGSF TEATLQRDRI FKHFTRKRQR AMRRRVHQVN GHKFMATYLR
     QPTYCSHCRE FIWGVFGKQG YQCQVCTCVV HKRCHHLIVT ACTCQNNINK VDAKIAEQRF
     GINIPHKFNV HNYKVPTFCD HCGSLLWGIM RQGLQCKICK MNVHIRCQAN VAPNCGVNAV
     ELAKTLAGMG LQPGNISPTS KLISRSTLRR QGKEGSKEGN GIGVNSSSRF GIDNFEFIRV
     LGKGSFGKVM LARIKETGEL YAVKVLKKDV ILQDDDVECT MTEKRILSLA RNHPFLTQLF
     CCFQTPDRLF FVMEFVNGGD LMFHIQKSRR FDEARARFYA AEIISALMFL HEKGIIYRDL
     KLDNVLLDHE GHCKLADFGM CKEGICNGVT TATFCGTPDY IAPEILQEML YGPAVDWWAM
     GVLLYEMLCG HAPFEAENED DLFEAILNDE VVYPTWLHED ATGILKSGST TLFSPLLSAH
     L
//
ID   D3YWX2_MOUSE            Unreviewed;      1941 AA.
AC   D3YWX2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Ylpm1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC127582; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC155811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR974585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00621973; -.
DR   ProteinModelPortal; D3YWX2; -.
DR   Ensembl; ENSMUST00000021670; ENSMUSP00000021670; ENSMUSG00000021244.
DR   MGI; MGI:1926195; Ylpm1.
DR   GeneTree; ENSGT00440000039837; -.
DR   Bgee; D3YWX2; -.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
PE   4: Predicted;
SQ   SEQUENCE   1941 AA;  219215 MW;  CE27A19A46E35F61 CRC64;
     MYPNWGRYGG SSHYPPPPVP PPPPPVALPE ASPGPGYSSS TAPAAPSSSG FMSFREQHLA
     QLQQLQQMHQ KQMQCVLQPH HLPPPPLPPP PVMPGGGYGD WQPPPPPMPP PPGPALSYQK
     QQQYKHQMIH HQRDGPPGLV PMELESPPES PPVPPGSYMP PSQSYMPPPQ PPPSYYPPSS
     AQPYLPPAQP SPSQSPPSQS YLAPTPSYSS SSSSQSYLSH SQPYLPPSQA SPSRSSQGPS
     KPQLPPPPSI PSGNKTAIQQ EPLESGAKNK TAEQKQAAPE PDPSTMTPQE QQQYWYRQHL
     LSLQQRTKVH LPGHKKGLVT AKDVPEPIKE EAPGPAASQV AEPLAAEKPP LPPPNEEAPP
     PLSPEEPQSE DSEEDARFKQ LKAIAAHWQA AAAHWQQQQQ QRVGFQYQGI MQRHTQLQQI
     LQQYQQVIQH SPHIQVTTPP PGIPPPGAPQ GMPPQLTAPL PPASGSQNSQ IPEKPRQALL
     PTPVSFGSTP PSPYHPPPQS EQVNSKPLNK VFSSEQGLGE SSALSQSIIA AKDTPVKSGG
     LLADPPKGSF LEGPRGPRFD GPRRFEDLGS RCEGPRPKGP RFEGNRPDGP RPRYESHPAE
     GTKSKWGTIP RGPASQFYIT PNTSLSPRQS GPQWKGPKAT VGQQHQQQPK QQPKSQAEPL
     SGNKEPLADT SNNQQKNLKI QSAAFSISAD VKDTKAAQSN ENLSDSQQEP TKSQVSEGPV
     EPSNWNQNSQ SMETEMDKAE GVTQPVSLAN KPVPTQSTFP SKVGSMEGGA AAAALTADDF
     KPLGVGLSHS ENHQEKDLPQ PDSRENRLEG NKGSSSSYRG PGQNRVEESR DKGLVNRGRG
     QIINRGPGLV KQEDFHDKMM GRREDSREKM NRGEGNRDRV FVRPGSSRDK IPGGLQDSQD
     SRANSRERGP PRRAGSQERG PPRRAGSRER VPPQRAGSRE RVPPRGPGSR ERGLGRPDFG
     HDRVPFRSEL GDGGDKVYPY HRDEPSRASW NHGEERGHEE FPVDGRNAPI ERERLDDWDR
     KRYWRECERD YQDDTLDSYS REDRFSAPPS RSHDGDRRGP WWDDWERDQD MDEGYGREMD
     RDLDRDVDRI RRPLDIYDRN VDNEWDRDYG RPLDEQESQF RERDIPSLPP LPPLPPLPPL
     DRYRDDRWRE ERNRDHGYDR DFRDRGELRI REYPERGDTW REKRDYVPDR MDWERERLSD
     RWYPSDVDRH SPMAEHMPSS HHSSEMMGSD ANLDSDQGLG GVMVLSQRQH EIILKAAQEL
     KMLREQKEQL QKLKDFGSEP QMADHLPPPD SRLQNPSRPG MYPPPGSYRP PPPMGKPPGS
     IVRPSAPPAR SSIPMTRPPV PIPPPPPPPP PPPPPPPVIK SKTSSVKQER WDEDSFFGLW
     DTNDDQGLNS EFKRDTATIP SAPVLPPPPV HSSIPPPGPM PMGMPPMSKP PPVQHTVDYG
     HGRDMPTNKV EQIPYGERIT LRPDPLPERS TFDADHAGQR DRYDRDRDRE PYFDRPSNIT
     DHRDFKRDRE THRDRDRDRV LDYERDRFDR ERRPRDDRNQ SYRDKKDHSS SRRGGFDRPS
     YDRKSDRPPY EGPPMFGGER RTYPEERMPL PAPALGHQPP PVPRVEKKPE SKNVDDILKP
     PGRESRPERI VVIMRGLPGS GKTHVAKLIR DKEVEFGGPA PRVLSLDDYF IAEVEKEEKD
     PDSGKKVKKK VMEYEYEADM EETYRTSMFK TFKKTLDDGF FPFIILDAIN DRVRHFDQFW
     SAAKTKGFEV YLAEMSADNQ TCGKRNIHGR KLKEINKMAE HWEVAPRHMM RLDIRSLLQD
     AAIEEVEMED FDANIEDQKE EKKDAEEEES ELGYIPKSKW EMDTSEAKLD KLDGLRTGTK
     RKRDWEAIAS RMEDYLQLPD DYETRASEPG KKRVRWADLE EKKDADRKRA IGFVVGQTDW
     EKITDESGHL AERALNRTKY I
//
ID   D3YWY4_MOUSE            Unreviewed;      1075 AA.
AC   D3YWY4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Grip1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- SIMILARITY: Contains 7 PDZ (DHR) domains.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC134326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC153493; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC158686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC162467; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00918581; -.
DR   Ensembl; ENSMUST00000148954; ENSMUSP00000118397; ENSMUSG00000034813.
DR   MGI; MGI:1921303; Grip1.
DR   GeneTree; ENSGT00390000013494; -.
DR   Bgee; D3YWY4; -.
DR   GO; GO:0045121; C:membrane raft; IDA:MGI.
DR   GO; GO:0008104; P:protein localization; IMP:MGI.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF00595; PDZ; 7.
DR   SMART; SM00228; PDZ; 7.
DR   SUPFAM; SSF50156; PDZ; 7.
DR   PROSITE; PS50106; PDZ; 7.
PE   4: Predicted;
SQ   SEQUENCE   1075 AA;  116049 MW;  93A41B8DAAC94483 CRC64;
     MIAVSFKCRC QILRRLTKDE SPYTKSASQT KPPDGALAVR RQSIPEEFKG STVVELMKKE
     GTTLGLTVSG GIDKDGKPRV SNLRQGGIAA RSDQLDVGDY IKAVNGINLA KFRHDEIISL
     LKNVGERVVL EVEYELPPVS VQGSSVMFRT VEVTLHKEGN TFGFVIRGGA HDDRNKSRPV
     VITCVRPGGP ADREGTIKPG DRLLSVDGIR LLGTTHAEAM SILKQCGQEA TLLIEYDVSV
     MDSVATASGP LLVEVAKTPG ASLGVALTTS VCCNKQVIVI DKIKSASIAD RCGALHVGDH
     ILSIDGTSME YCTLAEATQF LANTTDQVKL EILPHHQTRL ALKGPDHAAM VPSSSPTSMS
     AYSLSSLNMG TLPRSLYSTS PRGTMMRRRL KKKDFKSSLS LASSTVGLAG QVVHTETTEV
     VLTADPVTGF GIQLQGSVFA TETLSSPPLI SYIEADSPAE RCGVLQIGDR VMAINGIPTE
     DSTFEEANQL LRDSSITSKV TLEIEFDVAE SVIPSSGTFH VKLPKKHSVE LGITISSPSS
     RKPGDPLVIS DIKKGSVAHR TGTLELGDKL LAIDNIRLDN CSMEDAVQIL QQCEDLVKLK
     IRKDEDNSDE QESSGAIIYT VELKRYGGPL GITISGTEEP FDPIIISSLT KGGLAERTGA
     IHIGDRILAI NSSSLKGKPL SEAIHLLQMA GETVTLKIKK QTDAQSASSP KKFPIPGHSG
     DLGDGEEDPS PIQKPGKLSD AYPSTVPSVD SAVDSWDGSG IDASYGSQGS TFQTSGYNYN
     TYDWRSPKQR TSLSPVPKPR SQTYPDVGLS NEDWDRSTAS GFVGASDSAD AEQEENFWSQ
     ALEDLETCGQ SGILRELEEK ADRRVSLRNM TLLATIMSGS TMSLNHEAPM ARSQLGRQAS
     FQERSSSRPH YSQTTRSNTL PSDVGRKSVT LRKMKQEIKE IMSPTPVELH KVTLYKDSGM
     EDFGFSVADG LLEKGVYVKN IRPAGPGDVG GLKPYDRLLQ VNHVRTRDFD CCLVVPLIAE
     SGNKLDLVIS RNPLASQKSI EQPALPSDWS EQNSAFFQQP SHGGNLETRE PTNTL
//
ID   D3YX63_MOUSE            Unreviewed;       135 AA.
AC   D3YX63;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Pclo;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC144480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00889854; -.
DR   ProteinModelPortal; D3YX63; -.
DR   Ensembl; ENSMUST00000116626; ENSMUSP00000112325; ENSMUSG00000080293.
DR   MGI; MGI:1349390; Pclo.
DR   GeneTree; ENSGT00550000074588; -.
DR   OrthoDB; EOG4Z62PW; -.
DR   Bgee; D3YX63; -.
DR   GO; GO:0005522; F:profilin binding; IDA:MGI.
DR   GO; GO:0019933; P:cAMP-mediated signaling; IDA:MGI.
DR   GO; GO:0007010; P:cytoskeleton organization; IDA:MGI.
DR   GO; GO:0030073; P:insulin secretion; IDA:MGI.
DR   GO; GO:0017157; P:regulation of exocytosis; IDA:MGI.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   Pfam; PF00168; C2; 1.
DR   SMART; SM00239; C2; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   PROSITE; PS50004; C2; 1.
PE   4: Predicted;
SQ   SEQUENCE   135 AA;  15769 MW;  CEA3291EF40A51FD CRC64;
     MGEIKLALKK EMKTDGEQLI VEILQCRNIT YKFKSPDHLP DLYVKIYVIN IATQKKVIKK
     KTRVCRHDRE PSFNETFRFS LSPAGHSLQI LLFSNGGKFM KKTLIGEACI WLDKVDLRKR
     IVNWHKLLMS PTQTH
//
ID   D3YXB5_MOUSE            Unreviewed;       413 AA.
AC   D3YXB5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 9.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Gucy1a2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC118473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC122444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC156642; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00874544; -.
DR   Ensembl; ENSMUST00000086620; ENSMUSP00000083814; ENSMUSG00000041624.
DR   MGI; MGI:2660877; Gucy1a2.
DR   GeneTree; ENSGT00560000076952; -.
DR   Bgee; D3YXB5; -.
DR   GO; GO:0004383; F:guanylate cyclase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0030828; P:positive regulation of cGMP biosynthetic process; IMP:MGI.
DR   InterPro; IPR011644; Haem_NO-bd.
DR   InterPro; IPR011645; Haem_no_assoc-bd.
DR   Pfam; PF07700; HNOB; 1.
DR   Pfam; PF07701; HNOBA; 1.
DR   SUPFAM; SSF111126; Haem_NO-bd; 1.
PE   4: Predicted;
SQ   SEQUENCE   413 AA;  46470 MW;  157CCA353C0DF6EC CRC64;
     MSRRKISSES FSSLSSDYLE TSPEEEGECP LSRLCWNGSR SPPGPPGSRE AAKAATSAPA
     ASAAAASAAV AAEYKRAQRR GRVNLDSLGE SISLLTAPLP QTIHMTLKRT LQYYEHQVIG
     YRDAEKNFHN ISKRCSYADH SNKEEIEDVS GILQCTANVL GLQFQEIQER FGEEFFKICF
     DENERVLRAV GSTLQDFFNG FDALLEHIRT SFGKQATLES SSFLCKELPE GTLMLHYFHP
     HHTVGFAMLG MIKAAGKRIY HLNVEVEQIE NEKLCFDGSN PSNCSCLTFL IKECETTQIT
     KDNPQGTSQV PADLRISINT FCRAFPFHLM FDSNMVVLQL GEGLRKQLRY DTHRALKFED
     CFEIVSPMIN ATFDRVLLRL STPFVIRTKP EASGTENEDK VRKIIKVQHL VFF
//
ID   D3YXI3_MOUSE            Unreviewed;       450 AA.
AC   D3YXI3;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 11.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Gm5620;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. It
CC       binds two moles of GTP, one at an exchangeable site on the beta
CC       chain and one at a non-exchangeable site on the alpha-chain (By
CC       similarity).
CC   -!- SUBUNIT: Dimer of alpha and beta chains (By similarity).
CC   -!- SIMILARITY: Belongs to the tubulin family.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC152825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00129028; -.
DR   RefSeq; XP_486246.1; XM_486246.5.
DR   RefSeq; XP_909750.1; XM_904657.4.
DR   UniGene; Mm.326103; -.
DR   ProteinModelPortal; D3YXI3; -.
DR   Ensembl; ENSMUST00000077991; ENSMUSP00000111700; ENSMUSG00000056904.
DR   GeneID; 434428; -.
DR   KEGG; mmu:434428; -.
DR   MGI; MGI:3647798; Gm5620.
DR   GeneTree; ENSGT00600000084100; -.
DR   OrthoDB; EOG44J2HZ; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR   InterPro; IPR002452; Alpha_tubulin.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR023123; Tubulin_C.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   Gene3D; G3DSA:3.30.1330.20; Tubulin/FtsZ_2-layer-sand-dom; 1.
DR   Gene3D; G3DSA:1.10.287.600; Tubulin_C; 1.
DR   Gene3D; G3DSA:3.40.50.1440; Tubulin_FtsZ; 1.
DR   PANTHER; PTHR11588; Tubulin; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01162; ALPHATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF55307; Tub_FtsZ_C; 1.
DR   SUPFAM; SSF52490; Tubulin_FtsZ; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Cytoskeleton; GTP-binding; Microtubule; Nucleotide-binding.
SQ   SEQUENCE   450 AA;  50037 MW;  B582D4DAA1767587 CRC64;
     MRECISIHVG QAGVQIGNAC WELYCLEHGI QADGQMPSGK TIRGGDDSFN TFSETGAGKH
     VPRAVFVDLE PTVIDEVRTG TYRQLFHPEQ LITGKEDAAN NYARGHYTIG KEIIDLVLDT
     IRKLADQCIG LQGFLVFHSF GGGTGSGFTS LLMERLSVDY GKKSKLEFSI YPAPQVSTAV
     VEPYNSILTT HTTLEHSDCA FMVDNEAIYD ICRRNLDIEH PTYTNLNRLI SQIVSSITAS
     LRFDGALNVD LTEFQTNLVP YPRIHFPLAT YAPVISAEKA YHEHLSVAEI TNACFEPANQ
     MVKCDPRHGK YMACCLLYRG DVIPKDVNAA IATIKTKRSI QFVDWCPTGF KVGINYQPPT
     VVPGGDLAKV QRAVCMLSNT TAIAEAWARL DHKFDLMYAK RAFVYWYVGE SMEEGEFSEA
     REDMAALEKD YEEVGVDSVE GEGEEEGEEY
//
ID   D3YXJ0_MOUSE            Unreviewed;      1156 AA.
AC   D3YXJ0;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 10.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Dgkh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC124715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC126251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC161608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00277362; -.
DR   RefSeq; NP_001074805.1; NM_001081336.1.
DR   UniGene; Mm.379505; -.
DR   UniGene; Mm.411737; -.
DR   Ensembl; ENSMUST00000074729; ENSMUSP00000074290; ENSMUSG00000034731.
DR   GeneID; 380921; -.
DR   KEGG; mmu:380921; -.
DR   CTD; 380921; -.
DR   MGI; MGI:2444188; Dgkh.
DR   GeneTree; ENSGT00600000084245; -.
DR   Bgee; D3YXJ0; -.
DR   InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00609; DAGK_acc; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00045; DAGKa; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS50146; DAGK; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   4: Predicted;
SQ   SEQUENCE   1156 AA;  127362 MW;  84962D1A01A72842 CRC64;
     MAGAGSQHHP QGVAGGAVAG ASAVSPTAAG PGEDSSDSEA EQEGPQKLIR KVSTSGQMRT
     KTSIKEGQLL KQTSSFQRWK KRYFKLRGRT LYYAKDSKSL IFDEVDLSDA SVAEASTKNA
     NNSFTIITPF RRLMLCAENR KEMEVWISSL KSVQSREPYE VAQFNVEHFS GMHNWYACSH
     ARPTFCNVCR ESLSGVTSHG LSCEVCKFKA HKRCAVRATN NCKWTTLASI GKDIIEDEDG
     VAMPHQWLEG NLPVSAKCAV CDKTCGSVLR LQDWKCLWCK TMVHTACKDV YHPVCPLGQC
     KVSIIPPIAL NSTDSDGFCR ATFSFCVSPL LVFVNSKSGD NQGVKFLRRF KQLLNPAQVF
     DLMNGGPYLG LRLFQKFDNF RILVCGGDGS VGWVLSEIDK LNLHKQCQLG VLPLGTGNDL
     ARVLGWGGSY DDDTQLPQIL EKLERASTKM LDRWSIMTYE LKLPAKSSLL PEPVAATEEF
     YMTIYEDSVA NHLTKIVNSD EHAVVISSAK ILCETVKDFV AKVEKAQDRT LENTVVAEAV
     ASKCSVLNEK LEQLLQALHA DSQASRVPPG IGPAIPEEDT VESASDESLG ESKDQLVNDI
     GKPSSQKAVK PREIMLRANS LKKAVRQVIE EAEKVMDEPA VQPSEPVSPS CDYDTETDEA
     KEDDAKESLS AKTTSQSPDA QASCGHPQTD SVAGPAMATT KENLPVLNTR IICPGLRAGL
     AASIAGSSII NKMLLANIDP FGATPFIDPD LDSLDGYSEK CVMNNYFGIG LDAKISLEFN
     NKREEHPEKC RSRTKNLMWY GVLGTRELLQ RSYKNLEQRV QLECDGQYIP LPSLQGIAVL
     NIPSYAGGTN FWGGTKEDDI FAAPSFDDKI LEVVAVFDSV QMAVSRVIKL QHHRIAQCRT
     VKITIFGDEG VPVQVDGEAW VQPPGIIKIV HKNRAQMLTR DRAFESTLKS WEDKQKCDSG
     KPVLRTNLYI HPAPDLATEE VSQMRLCSQA AEELITRICD AATIHCLLEQ ELAHAVNACS
     HALNKANPRF PESLTRDTAT EIAINVKALY NETEALLVGR VPLHLESPHE ERVSSALHSV
     EMELQKLTEI PWLYYILRPS EDEEPPLDCT KRNNKSTVFR IVPKFKKEKA QKQKTSSQPG
     PGDSESGSYE ANSPGN
//
ID   D3YXK0_MOUSE            Unreviewed;       839 AA.
AC   D3YXK0;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 6.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Jakmip2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC156546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC166643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC168308; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00474995; -.
DR   ProteinModelPortal; D3YXK0; -.
DR   Ensembl; ENSMUST00000082254; ENSMUSP00000080881; ENSMUSG00000024502.
DR   MGI; MGI:1923467; Jakmip2.
DR   GeneTree; ENSGT00390000002812; -.
DR   OrthoDB; EOG4BP1B5; -.
DR   Bgee; D3YXK0; -.
PE   4: Predicted;
SQ   SEQUENCE   839 AA;  98333 MW;  596B30B54E48F3FE CRC64;
     MSKKGRNKGE KPEALIVALQ AANEDLRTKL TDIQIELHQE KSKVSKLERE KTQEAKRIRE
     LEQRKHTVLV TELKAKLHEE KMKELQAVRE NLIKQHEQEM SRTVKVRDGE IQRLKSALCA
     LRDGSSDKVR TALTIEAREE ARKQFDAERL KLLQEITDLK TAKKQVDEAL SNMIQADKIK
     AGDLRSEHQS HQEAISKIKW ESERDIRRLM DEIKAKDRII FSLEKELETQ TGYVQKLQLQ
     KEALDEQLFL VKEAECNMSS PKREIPGRAG DGSEHCSSPV SPCDLRDLRR NQKRIAELNA
     TIRKLEDRNT LLGDERNELL KRVRETEKQC KPLLERNKCL AKRNDELMVS LQRMEEKLKA
     VTKENSEMRE KITSHPPLKK LKSLNDLDQA NEEQETEFLK LQVIEQQNII DELTRVGEPS
     GNTLFSRDRE KLIRRRKHRR SSKPIKRPVL DPFIGYDEDS MDSETSSMTS FRTDRTPATP
     DDDLDESLAA EESELRFRQL TKEYQALQRA YALLQEQTGG IIDAEREAKA QEQLQAEVLR
     YRAKIEDLEA TLAQKGQDSH WVEDKQLFIK RNQELLEKIE KQEAENHRLQ QELQDARDQN
     ELLEFRNLEL EERERRSPPF NLQIHPFSDG VSALQIYCMK EGVKDVNIPD LIKQLDILGD
     NGNLRNEEQV AIIQASTVLS LAEKWIQQIE GAEAALHQKM MELESDMEQF CKIKGYLEEE
     LDYRKQALDQ AYMRIQELEA TLYNALQQET VIKFGELLSD KQQEELRTAV EKLRRQMLRK
     SREYDCQILQ ERMELLQQAH QRIRDLEDKT DIQKRQIKDL EEKFLFLFLF FSLAFILWP
//
ID   D3YXK1_MOUSE            Unreviewed;       519 AA.
AC   D3YXK1;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 9.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Samd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC156028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00762209; -.
DR   RefSeq; NP_001074884.1; NM_001081415.1.
DR   UniGene; Mm.298091; -.
DR   Ensembl; ENSMUST00000095228; ENSMUSP00000092853; ENSMUSG00000079003.
DR   GeneID; 666704; -.
DR   KEGG; mmu:666704; -.
DR   CTD; 666704; -.
DR   MGI; MGI:2142433; Samd1.
DR   GeneTree; ENSGT00530000063936; -.
DR   Bgee; D3YXK1; -.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   4: Predicted;
SQ   SEQUENCE   519 AA;  54533 MW;  C8E43277C77636C1 CRC64;
     MAGPPALPPP ETAAAATTAA AASSSAASPH YQEWILDTID SLRSRKARPD LERICRMVRR
     RHGPEPERTR AELEKLIQQR AVLRVSYKGS ISYRNAARVQ PPRRGATPPA PPRVPRGGPA
     APPPTPAPPP APVAAPTRAP RAAAATAPPS PGPAQPGPRA QRAAPLAAPP PAPAAPPAAA
     PPAGPRRAPP PAVAAREPPA PPQQQQPPPP QPQPPPEGGA ARAGGPARPV SLREVVRYLG
     GSGGASGRLT RGRVQGLLEE EAARGRLERT RLGALALPRG DRPGRAPPAA SARAARSKRG
     GEERVFEKEE EDEDEDEEEE EEDNVSEGSE VPESDRPAGA QHHQINGERG PQSAKERVKE
     WSPCGPYQGQ DEGRGPAPGS CTRQVFPMTA VNKEGGSACV GAAPDSPSPV PLPPGKPALP
     GADGTPFGCP PGRKEKPTDP VEWTVMDVVE YFTEAGFPEQ ATAFQEQEID GKSLLLMQRT
     DVLTGLSIRL GPALKIYEHH IKVLQQGHFE DDDPDGLLG
//
ID   D3YXK2_MOUSE            Unreviewed;       917 AA.
AC   D3YXK2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 9.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Safb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- SIMILARITY: Contains 1 SAP domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CT485788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00944159; -.
DR   ProteinModelPortal; D3YXK2; -.
DR   Ensembl; ENSMUST00000095224; ENSMUSP00000092849; ENSMUSG00000071054.
DR   MGI; MGI:2146974; Safb.
DR   GeneTree; ENSGT00590000082875; -.
DR   OrthoDB; EOG4F4S9X; -.
DR   Bgee; D3YXK2; -.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0030520; P:estrogen receptor signaling pathway; IMP:MGI.
DR   GO; GO:0040007; P:growth; IMP:MGI.
DR   GO; GO:0042445; P:hormone metabolic process; IMP:MGI.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR003034; SAP_DNA-bd.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF02037; SAP; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00513; SAP; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50800; SAP; 1.
PE   4: Predicted;
SQ   SEQUENCE   917 AA;  102757 MW;  5C5E24CC1C672FA9 CRC64;
     MAETLSGLGD ASAAGAAAVS SAASETGTRR LSDLRVIDLR AELKKRNLDS SGNKSVLMER
     LKKAIEDEGG NPDEIEVTSE CNKKMPKRPS KGRKPEDEGV EDNGLEENSG DGQEDVETSL
     ENLQDMDMMD ISVLDEADID NGSVADCVEE EEEATLPEGL ADSTELVEGD LKGLPEQLQE
     HAIDDKDTVN NVDTSSSDFT MLQEMEEASL EPENEKILDI LGETCKSEPV KEEGSELEQP
     FAQATSSVGP DRKLAEEEDL FESCGHPEEE DSSKSESPST RCQWSEADAP LAVVKREPAD
     APGGGTGMDR EPVGLEEPVE QSSTAAQLPE ATSQELVRAP TAALSPEPQD SKEDVKKFAF
     DACNDVPAPP KESSASEGAD QKMSSVEEDS DTKRLSREEK GRSSCGRNFW VSGLSSTTRA
     TDLKNLFSRY GKVVGAKVVT NARSPGARCY GFVTMSTAEE ATKCISHLHK TELHGKMISV
     EKAKSEPTGK RVPDRRDGDS KKEKASTSDR SANLKREEKG ERKDDAKKTD DGSTEKSKDA
     DDQKPGPSER SRTTKSGSRG TERTVVMDKS KGVPVISVKT SGSKERASKS QDRKSASREK
     RSVVSFDKVK ESRKSRDSES RSRERERSER EQRLQAQWER EERERLEIAR ERLAFHRHRL
     ERERMERERL ERERMHVEQE RRREQERIHR EREELRRQQE LRYEQERRPA VRRPYEVDGR
     RDDAYWPEAK RAALDDRYHS DFSRQDRFHD FDHRDRGRYP NHSVDRREGS RSMMGDREGQ
     HYPERHGGPE RHGRDSRDGW GYGSNKRLSE GRGLPPPPRR DWGEHGRRLE DDRAWQGTAD
     GGMMERDHKR WQGGERSMSG HSGPGHMMNR GGMSGRGSFA PGGASRGHVI PRGGMQAGFG
     GQSRGSRPSD ARFTRRY
//
ID   D3YXR8_MOUSE            Unreviewed;      1079 AA.
AC   D3YXR8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 9.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Rimbp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC110566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC111089; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC116715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00874334; -.
DR   RefSeq; NP_001074857.1; NM_001081388.1.
DR   UniGene; Mm.233996; -.
DR   Ensembl; ENSMUST00000111346; ENSMUSP00000106978; ENSMUSG00000029420.
DR   GeneID; 231760; -.
DR   KEGG; mmu:231760; -.
DR   CTD; 231760; -.
DR   MGI; MGI:2443235; Rimbp2.
DR   GeneTree; ENSGT00390000017228; -.
DR   OrthoDB; EOG4WQ11S; -.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF07653; SH3_2; 3.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00326; SH3; 3.
DR   SUPFAM; SSF49265; FN_III-like; 3.
DR   SUPFAM; SSF50044; SH3; 3.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS50002; SH3; 3.
PE   4: Predicted;
SQ   SEQUENCE   1079 AA;  119148 MW;  560826C5504B5F98 CRC64;
     MREAAERRQQ LELEHEQALA FLNAKQQEIQ LLQQAQVEAK KEHEGAVQLL ENTLDCMQSK
     VRELEEKCRV QSEQFNLLSR DLEKFRQHTG SIDLLGSSSV ALLDVPLAPG KPFPQYMNGL
     ATSIHKGHEG PTGHYSVIGD YIPLSGDKLE SPCVKPSFLL RSSSPRCRFE SEMDNDRNSN
     NSKQSSSGKV HLCVARYSYN PFDGPNENPE AELPLTAGKY LYVYGDMDED GFYEGELLDG
     QRGLVPSNFV DFIQDNESRL AGTLGSEQDQ NFLNHSGISL ERDSILHLHS PTQVDSGITD
     NGGGTLDVNI DDIGEDTVPY PRKITLIKQL AKSVIVGWEP PAVPPGWGTV SSYNVLVDKE
     TRMSLALGRR TKALIEKLNT AACTYRISVQ CVTSRGNSDE LQCTLLVGKD VVVAPSQLRV
     DNITQISAQL SWLPTNSNYS HIIFLNEEEL DIVKAARYKY QFFNLRPNMA YKVKVLAQPH
     QMPWQLPLEQ REKKEACVEF STLPAGPPAP PQDVTVHAGA TAASVQVSWK PPALTPTGLS
     NGANVTGYGV YAKGQRVAEV IAPTADGTAV ELIRLRSLEA KAVSVRTLSV QGESMDSALA
     AIPPDLLVPP APHPRTAPPP KPLASDMDTK DQHLGPHVKV DESWEQSRSP GPAHGHMLEP
     PDMHSAGPGR RSPSPSRILP QPQGAPVSTT VAKAMAREAA QRVAESNRLE KRSLFLEQSS
     AGQYTNSDEE DGYASPEVKR RGTSVDDFLK GSELGKQPHC CHGDEYHTES SRGSDLSDIM
     EEDEEELYSE MQLEDGGRRR PSGTSHNALK ILGNSTLMGR ADRMEHVSRR YSHSGGGSHR
     HRPAMAPSID EYTGRDHLSP DFYDESETDP GAEELPARIF VALFDYDPLT MSPNPDAAEE
     ELPFKEGQII KVYGDKDADG FYRGETCARL GLIPCNMVSE IHADDEEMMD QLLRQGFLPL
     NTPVEKIERS RRSGRGHSVP TRRMVALYDY DPRESSPNVD VEAELPFCTG DIITVFGEID
     EDGFYYGELN GQKGLVPSNF LEEVPDDVEV HLSDAPPHYS HDPPMRSKAK RKKSVHFTP
//
ID   D3YXR9_MOUSE            Unreviewed;       270 AA.
AC   D3YXR9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 10.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Gm7694;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=22354682; PubMed=12466850; DOI=10.1038/nature01262;
RA   Waterston R.H., Lindblad-Toh K., Birney E., Rogers J., Abril J.F.,
RA   Agarwal P., Agarwala R., Ainscough R., Alexandersson M., An P.,
RA   Antonarakis S.E., Attwood J., Baertsch R., Bailey J., Barlow K.,
RA   Beck S., Berry E., Birren B., Bloom T., Bork P., Botcherby M.,
RA   Bray N., Brent M.R., Brown D.G., Brown S.D., Bult C., Burton J.,
RA   Butler J., Campbell R.D., Carninci P., Cawley S., Chiaromonte F.,
RA   Chinwalla A.T., Church D.M., Clamp M., Clee C., Collins F.S.,
RA   Cook L.L., Copley R.R., Coulson A., Couronne O., Cuff J., Curwen V.,
RA   Cutts T., Daly M., David R., Davies J., Delehaunty K.D., Deri J.,
RA   Dermitzakis E.T., Dewey C., Dickens N.J., Diekhans M., Dodge S.,
RA   Dubchak I., Dunn D.M., Eddy S.R., Elnitski L., Emes R.D., Eswara P.,
RA   Eyras E., Felsenfeld A., Fewell G.A., Flicek P., Foley K.,
RA   Frankel W.N., Fulton L.A., Fulton R.S., Furey T.S., Gage D.,
RA   Gibbs R.A., Glusman G., Gnerre S., Goldman N., Goodstadt L.,
RA   Grafham D., Graves T.A., Green E.D., Gregory S., Guigo R., Guyer M.,
RA   Hardison R.C., Haussler D., Hayashizaki Y., Hillier L.W., Hinrichs A.,
RA   Hlavina W., Holzer T., Hsu F., Hua A., Hubbard T., Hunt A.,
RA   Jackson I., Jaffe D.B., Johnson L.S., Jones M., Jones T.A., Joy A.,
RA   Kamal M., Karlsson E.K., Karolchik D., Kasprzyk A., Kawai J.,
RA   Keibler E., Kells C., Kent W.J., Kirby A., Kolbe D.L., Korf I.,
RA   Kucherlapati R.S., Kulbokas E.J., Kulp D., Landers T., Leger J.P.,
RA   Leonard S., Letunic I., Levine R., Li J., Li M., Lloyd C., Lucas S.,
RA   Ma B., Maglott D.R., Mardis E.R., Matthews L., Mauceli E., Mayer J.H.,
RA   McCarthy M., McCombie W.R., McLaren S., McLay K., McPherson J.D.,
RA   Meldrim J., Meredith B., Mesirov J.P., Miller W., Miner T.L.,
RA   Mongin E., Montgomery K.T., Morgan M., Mott R., Mullikin J.C.,
RA   Muzny D.M., Nash W.E., Nelson J.O., Nhan M.N., Nicol R., Ning Z.,
RA   Nusbaum C., O'Connor M.J., Okazaki Y., Oliver K., Overton-Larty E.,
RA   Pachter L., Parra G., Pepin K.H., Peterson J., Pevzner P., Plumb R.,
RA   Pohl C.S., Poliakov A., Ponce T.C., Ponting C.P., Potter S., Quail M.,
RA   Reymond A., Roe B.A., Roskin K.M., Rubin E.M., Rust A.G., Santos R.,
RA   Sapojnikov V., Schultz B., Schultz J., Schwartz M.S., Schwartz S.,
RA   Scott C., Seaman S., Searle S., Sharpe T., Sheridan A., Shownkeen R.,
RA   Sims S., Singer J.B., Slater G., Smit A., Smith D.R., Spencer B.,
RA   Stabenau A., Stange-Thomann N., Sugnet C., Suyama M., Tesler G.,
RA   Thompson J., Torrents D., Trevaskis E., Tromp J., Ucla C.,
RA   Ureta-Vidal A., Vinson J.P., Von Niederhausern A.C., Wade C.M.,
RA   Wall M., Weber R.J., Weiss R.B., Wendl M.C., West A.P.,
RA   Wetterstrand K., Wheeler R., Whelan S., Wierzbowski J., Willey D.,
RA   Williams S., Wilson R.K., Winter E., Worley K.C., Wyman D., Yang S.,
RA   Yang S.P., Zdobnov E.M., Zody M.C., Lander E.S.;
RT   "Initial sequencing and comparative analysis of the mouse genome.";
RL   Nature 420:520-562(2002).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC119431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC123650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00874832; -.
DR   RefSeq; NP_001185884.1; NM_001198955.1.
DR   UniGene; Mm.452793; -.
DR   Ensembl; ENSMUST00000111345; ENSMUSP00000106977; ENSMUSG00000079188.
DR   GeneID; 665574; -.
DR   MGI; MGI:3649135; Gm7694.
DR   GeneTree; ENSGT00510000049665; -.
DR   OrthoDB; EOG479F7S; -.
PE   4: Predicted;
SQ   SEQUENCE   270 AA;  28502 MW;  E5ECBA5C0B8854C4 CRC64;
     MFENLNTTLT PKLQSSHSFP HLSRPGAPGS IAPGSGEPGG PGLRVGSSQH LRNLGKAVGA
     KVNDLLRRKE SSSLGSVGVL EINKTAGAQL PGGEDAACGP WLEDERSVQE VFPLLDPPPP
     ITRKRTPRAL KTTQDMLISS QPVLSNLEYG TESPPGQAQD SPPAAQPISA DTSRPESTIE
     MGEKGEALPN GEVSLLVPDL IHKNTQEEAK LKATEGKKSS SPGPIERNGL KLSLSPISLA
     ESWENSSPPP QARTSSLDNE GLHPDLLSFE
//
ID   D3YXS7_MOUSE            Unreviewed;       273 AA.
AC   D3YXS7;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 6.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Fam98c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC164564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00918161; -.
DR   Ensembl; ENSMUST00000136256; ENSMUSP00000118932; ENSMUSG00000030590.
DR   MGI; MGI:1921083; Fam98c.
DR   GeneTree; ENSGT00440000037341; -.
DR   Bgee; D3YXS7; -.
DR   InterPro; IPR018797; Uncharacterised_FAM98.
DR   Pfam; PF10239; DUF2465; 1.
PE   4: Predicted;
SQ   SEQUENCE   273 AA;  29503 MW;  BD3FBA296DC72AD1 CRC64;
     MDGAMVAGDL LTLGYDALPE GASRGPACAD FRALCARLAA ELTALGALER REEGTAVLGA
     GHGPDTEEEF LRQLAGWLRA LHCPDRALCG GDCATVLREP GGGLRLLRFL CSELQAARLL
     HLRLQRDSSP VPSFGEGTKK ANGVVQELTL TLQALGLPRP LRGTLASQLL REFHDKISEL
     LPSLPPESMK PLLNSQLDAS RWEALESLSQ SLTEQYCCRR CLLLKRLDLT TSAFHWGDRA
     EAHGEVMKAV LSPIRGLLTP ESDVSIAHVL AAR
//
ID   D3YXX3_MOUSE            Unreviewed;       188 AA.
AC   D3YXX3;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 9.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Akt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC124373; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00831633; -.
DR   Ensembl; ENSMUST00000001780; ENSMUSP00000001780; ENSMUSG00000001729.
DR   Ensembl; ENSMUST00000109749; ENSMUSP00000105371; ENSMUSG00000001729.
DR   Ensembl; ENSMUST00000121171; ENSMUSP00000113658; ENSMUSG00000001729.
DR   Ensembl; ENSMUST00000128300; ENSMUSP00000122222; ENSMUSG00000001729.
DR   Ensembl; ENSMUST00000144550; ENSMUSP00000123689; ENSMUSG00000001729.
DR   MGI; MGI:87986; Akt1.
DR   Bgee; D3YXX3; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005819; C:spindle; IDA:MGI.
DR   GO; GO:0042640; P:anagen; IMP:MGI.
DR   GO; GO:0008637; P:apoptotic mitochondrial changes; IDA:MGI.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:MGI.
DR   GO; GO:0007281; P:germ cell development; IDA:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0060709; P:glycogen cell development involved in embryonic placenta development; IMP:MGI.
DR   GO; GO:0006954; P:inflammatory response; IDA:MGI.
DR   GO; GO:0060716; P:labyrinthine layer blood vessel development; IMP:MGI.
DR   GO; GO:0001893; P:maternal placenta development; IMP:MGI.
DR   GO; GO:0001649; P:osteoblast differentiation; IGI:MGI.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:MGI.
DR   GO; GO:0010765; P:positive regulation of sodium ion transport; IDA:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
DR   GO; GO:0030163; P:protein catabolic process; IDA:MGI.
DR   GO; GO:0043491; P:protein kinase B signaling cascade; IGI:MGI.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:MGI.
DR   GO; GO:0045884; P:regulation of survival gene product expression; IDA:MGI.
DR   GO; GO:0032094; P:response to food; IDA:MGI.
DR   GO; GO:0051146; P:striated muscle cell differentiation; IGI:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   ATP-binding; Nucleotide-binding.
SQ   SEQUENCE   188 AA;  21934 MW;  82DFB852D062775E CRC64;
     MNDVAIVKEG WLHKRGEYIK TWRPRYFLLK NDGTFIGYKE RPQDVDQRES PLNNFSVAQC
     QLMKTERPRP NTFIIRCLQW TTVIERTFHV ETPEEREEWA TAIQTVADGL KRQEEETMDF
     RSGSPSDNSG AEEMEVSLAK PKHRVTMNEF EYLKLLGKGT FGKVILVKEK ATGRYYAMKI
     LKKEVIVA
//
ID   D3YXZ3_MOUSE            Unreviewed;       617 AA.
AC   D3YXZ3;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Klc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC124502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00757585; -.
DR   Ensembl; ENSMUST00000025798; ENSMUSP00000025798; ENSMUSG00000024862.
DR   Ensembl; ENSMUST00000113727; ENSMUSP00000109356; ENSMUSG00000024862.
DR   Ensembl; ENSMUST00000113728; ENSMUSP00000109357; ENSMUSG00000024862.
DR   MGI; MGI:107953; Klc2.
DR   OrthoDB; EOG45MN52; -.
DR   Bgee; D3YXZ3; -.
DR   GO; GO:0035253; C:ciliary rootlet; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005871; C:kinesin complex; IEA:InterPro.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0008088; P:axon cargo transport; IMP:MGI.
DR   InterPro; IPR002151; Kinesin_light.
DR   InterPro; IPR015792; Kinesin_light_repeat.
DR   InterPro; IPR015390; Rabaptin_Rab5-bd.
DR   InterPro; IPR001440; TPR-1.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 2.
DR   Pfam; PF09311; Rab5-bind; 1.
DR   Pfam; PF00515; TPR_1; 2.
DR   PRINTS; PR00381; KINESINLIGHT.
DR   SMART; SM00028; TPR; 4.
DR   PROSITE; PS01160; KINESIN_LIGHT; 2.
DR   PROSITE; PS50005; TPR; 5.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   4: Predicted;
KW   Repeat; TPR repeat.
SQ   SEQUENCE   617 AA;  68177 MW;  EFE518F6763BB810 CRC64;
     MATMVLPREE KLSQDEIVLG TKAVIQGLET LRGEHRALLA PLASHEAGEA EPGSQERCLL
     LRRSLEAIEL GLGEAQVILA LSSHLGAVES EKQKLRAQVR RLVQENQWLR EELAGTQQKL
     QRSEQAVAQL EEEKQHLLFM SQIRKLDEDA SPNEEKGDVP KDSLDDLFPN EDEQSPAPSP
     GGGDVAAQHG GYEIPARLRT LHNLVIQYAS QGRYEVAVPL CKQALEDLEK TSGHDHPDVA
     TMLNILALVY RDQNKYKDAA HLLNDALAIR EKTLGKDHPA VAATLNNLAV LYGKRGKYKE
     AEPLCKRALE IREKVLGKFH PDVAKQLSNL ALLCQNQGKA EEVEYYYRRA LEIYATRLGP
     DDPNVAKTKN NLASCYLKQG KYQDAETLYK EILTRAHEKE FGSVNGENKP IWMHAEEREE
     SKRRDSAPYG EYGSWYKACK VDSPTVNTTL RSLGALYRRQ GKLEAAHTLE DCASRSRKQG
     LDPASQTKVV ELLKDGSGGR GHRRGSRDVA GPQSESDLEE SGPAAEWSGD GSGSLRRSGS
     FGKLRDALRR SSEMLVRKLQ GGGPQEPPNS RMKRASSLNF LNKSVEEPVQ PGGTGLSDSR
     TLSSSSMDLS RRSSLVG
//
ID   D3YY68_MOUSE            Unreviewed;       190 AA.
AC   D3YY68;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 9.
DE   SubName: Full=MCG22130, isoform CRA_c;
DE   SubName: Full=Uncharacterized protein;
GN   Name=Eef1d; ORFNames=mCG_22130;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC116520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466545; EDL29497.1; -; Genomic_DNA.
DR   IPI; IPI00928179; -.
DR   Ensembl; ENSMUST00000151066; ENSMUSP00000118889; ENSMUSG00000055762.
DR   MGI; MGI:1913906; Eef1d.
DR   GeneTree; ENSGT00390000011747; -.
DR   Bgee; D3YY68; -.
DR   GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro.
DR   InterPro; IPR018940; EF-1_beta_acid_region_euk.
DR   InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6.
DR   InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
DR   InterPro; IPR014038; Transl_elong_fac_EF1B_bsu/dsu.
DR   Gene3D; G3DSA:3.30.70.60; Transl_elong_EF1B/rib_con; 1.
DR   Pfam; PF10587; EF-1_beta_acid; 1.
DR   Pfam; PF00736; EF1_GNE; 1.
DR   SMART; SM00888; EF1_GNE; 1.
DR   SUPFAM; SSF54984; Transl_elong_EF1B_B/D_G_exch; 1.
DR   PROSITE; PS00824; EF1BD_1; 1.
DR   PROSITE; PS00825; EF1BD_2; 1.
PE   3: Inferred from homology;
KW   Elongation factor; Protein biosynthesis.
SQ   SEQUENCE   190 AA;  21763 MW;  94CABB49AD3F1D44 CRC64;
     MATNFLAHEK IWFDKFKYDD AERRFYEQMN GPVTSGSRQH VSPMRQVEPP TKKGATPAED
     DEDKDIDLFG SDEEEEDKEA ARLREERLRQ YAEKKAKKPT LVAKSSILLD VKPWDDETDM
     AQLETCVRSI QLDGLVWGAS KLVPVGYGIR KLQIQCVVED DKVGTDLLEE EITKFEEHVQ
     SVDIAAFNKI
//
ID   D3YYD4_MOUSE            Unreviewed;        50 AA.
AC   D3YYD4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 6.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Stag1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC115355; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC134825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC146297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC147565; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00928196; -.
DR   Ensembl; ENSMUST00000041418; ENSMUSP00000040724; ENSMUSG00000037286.
DR   Ensembl; ENSMUST00000041595; ENSMUSP00000036451; ENSMUSG00000037286.
DR   Ensembl; ENSMUST00000123302; ENSMUSP00000117879; ENSMUSG00000037286.
DR   Ensembl; ENSMUST00000124487; ENSMUSP00000123595; ENSMUSG00000037286.
DR   Ensembl; ENSMUST00000129269; ENSMUSP00000116205; ENSMUSG00000037286.
DR   Ensembl; ENSMUST00000133388; ENSMUSP00000119637; ENSMUSG00000037286.
DR   Ensembl; ENSMUST00000138405; ENSMUSP00000116322; ENSMUSG00000037286.
DR   Ensembl; ENSMUST00000146312; ENSMUSP00000116597; ENSMUSG00000037286.
DR   Ensembl; ENSMUST00000155108; ENSMUSP00000118952; ENSMUSG00000037286.
DR   MGI; MGI:1098658; Stag1.
DR   GeneTree; ENSGT00390000014094; -.
DR   Bgee; D3YYD4; -.
PE   4: Predicted;
SQ   SEQUENCE   50 AA;  5462 MW;  C7A4AFC46AA671C1 CRC64;
     MITSELPVLQ DSTNETTAHS DAGSELEETE VKGKRKRGRP GRPPSTNKKP
//
ID   D3YYG9_MOUSE            Unreviewed;       190 AA.
AC   D3YYG9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Dctn1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC160400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00857843; -.
DR   Ensembl; ENSMUST00000077407; ENSMUSP00000076623; ENSMUSG00000031865.
DR   Ensembl; ENSMUST00000130212; ENSMUSP00000115838; ENSMUSG00000031865.
DR   MGI; MGI:107745; Dctn1.
DR   GeneTree; ENSGT00550000074375; -.
DR   Bgee; D3YYG9; -.
DR   GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR023092; CAP-Gly_CS.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   Gene3D; G3DSA:2.30.30.190; CAP-Gly_domain; 1.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   SUPFAM; SSF74924; CAP-Gly_domain; 1.
DR   PROSITE; PS00845; CAP_GLY_1; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 1.
PE   4: Predicted;
SQ   SEQUENCE   190 AA;  19352 MW;  5C68E2F001EE7748 CRC64;
     MSTEASARPL RVGSRVEVIG KGHRGTVAYV GATLFATGKW VGVILDEAKG KNDGTVQGRK
     YFTCDEGHGI FVRQSQIQVF EDGADTTSPE TPDSSASKVL KREGADAAAK TSKLPTRPAS
     TGVAGPSSSL GPSGSASAGE LSSSEPSTPA QTPLAAPIIP TPALTSPGAA PPLPSPSKEE
     EGLRAQVRDL
//
ID   D3YYH0_MOUSE            Unreviewed;       591 AA.
AC   D3YYH0;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Pex5l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC116723; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC119877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00857176; -.
DR   Ensembl; ENSMUST00000108224; ENSMUSP00000103859; ENSMUSG00000027674.
DR   MGI; MGI:1916672; Pex5l.
DR   GeneTree; ENSGT00390000013941; -.
DR   Bgee; D3YYH0; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0045185; P:maintenance of protein location; IDA:MGI.
DR   GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
DR   InterPro; IPR001440; TPR-1.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 2.
DR   Pfam; PF00515; TPR_1; 1.
DR   SMART; SM00028; TPR; 4.
DR   PROSITE; PS50005; TPR; 5.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   4: Predicted;
KW   Repeat; TPR repeat.
SQ   SEQUENCE   591 AA;  65836 MW;  07A2CCC68B9AEB85 CRC64;
     MQMSYLKSKE QGYGKLSSDE DLEIIVDQKQ LVNEQQESRP LLSPSIDDFL CETKSEAIAK
     PVTSNTAVLT TGLDLLDLSE PVSQTQTKAK KSEPSSKSSS LKKKADGSDL ISADAEQRAQ
     ALRGPETSSL DLVDIQTQLE KWDDVKFHGD RTSKGHLMAE RKSCSSRTGS KELLWSAEHR
     SQPELSTGKS ALNSESASEL ELVAPAQARL TKEHRWGSAL LSRNHSLEEE FERAKAAVES
     DTEFWDKMQA EWEEMARRNW ISENQEAQNQ VTVSASEKGY YFHTENPFKD WPGAFEEGLK
     RLKEGDLPVT ILFMEAAILQ DPGDAEAWQF LGITQAENEN EQAAIVALQR CLELQPNNLK
     ALMALAVSYT NTSHQQDACE ALKNWIKQNP KYKYLVKNKK GSPGLTRRMS KSPVDSSVLE
     GVKELYLEAA HQNGDMIDPD LQTGLGVLFH LSGEFNRAID AFNAALTVRP EDYSLWNRLG
     ATLANGDRSE EAVEAYTRAL EIQPGFIRSR YNLGISCINL GAYREAVSNF LTALSLQRKS
     RNQQQVPHPA ISGNIWAALR IALSLMDQPE LFQAANLGDL DVLLRAFNLD P
//
ID   D3YYI5_MOUSE            Unreviewed;       336 AA.
AC   D3YYI5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 11.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE            EC=1.2.1.12;
GN   Name=Gm7293;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
CC       NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CT030181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00751677; -.
DR   UniGene; Mm.335154; -.
DR   Ensembl; ENSMUST00000089534; ENSMUSP00000092698; ENSMUSG00000078308.
DR   MGI; MGI:3779717; Gm7293.
DR   GeneTree; ENSGT00550000074301; -.
DR   OrthoDB; EOG4Q84XS; -.
DR   Bgee; D3YYI5; -.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity; IEA:EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:InterPro.
DR   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR   InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR   InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR10836; GAP_DH; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PIRSF; PIRSF000149; GAP_DH; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
DR   SMART; SM00846; Gp_dh_N; 1.
DR   TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   Glycolysis; NAD; Oxidoreductase.
SQ   SEQUENCE   336 AA;  36304 MW;  C76061F089171F00 CRC64;
     MVKVGVNGFG RIGRLVTRAA FCSPHGKVEI VAINDPFIDL NYMVYMFQYD STHGKFNGTV
     KAENGKLVIN GKPITVFQER DPTNIKCGEA GAEYVMESTG VFTTMEKAGA HLFVTGAKRV
     IISAPSADAP MFVMGVNHEK YDNSLKIVSN ASCTTNCLAP LAKVIHDNFG IVEGLMTTVH
     AITATQKTVD GPSGKLWRDS RGAAQNIIPA PTDAAKAVSK VIPELNGKLT GMAFRVPTHN
     VSVVDLACRL EKPAKYDDIK KVVKQASEGS LKGILGYTED QVVSCDFNSN SHSSTFDAGA
     GIALNDNFVK LISWYDNEYG YSNRVVDLMA YMASKE
//
ID   D3YYK9_MOUSE            Unreviewed;      1054 AA.
AC   D3YYK9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Arfgef1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC102462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC159972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00928561; -.
DR   Ensembl; ENSMUST00000131556; ENSMUSP00000118805; ENSMUSG00000067851.
DR   MGI; MGI:2442988; Arfgef1.
DR   GeneTree; ENSGT00560000076562; -.
DR   OrthoDB; EOG4QC14S; -.
DR   Bgee; D3YYK9; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000904; Sec7.
DR   InterPro; IPR023394; SEC7_alpha_orthog.
DR   Gene3D; G3DSA:1.10.1000.11; G3DSA:1.10.1000.11; 1.
DR   Pfam; PF01369; Sec7; 1.
DR   SMART; SM00222; Sec7; 1.
DR   SUPFAM; SSF48425; Sec7; 1.
DR   PROSITE; PS50190; SEC7; 1.
PE   4: Predicted;
SQ   SEQUENCE   1054 AA;  117872 MW;  6D498E36227F578F CRC64;
     MYEGKKTKNM FLTRALEKIL ADKEVKKAHH SQLRKACEVA LEEIKVETEK QSPPHGEAKA
     GSGTLPPVKS KTNFIEADKY FLPFELACQS KCPRIVSTSL DCLQKLIAYG HLTGRAPDST
     TPGKKLIDRI IETICGCFQG PQTDEGVQLQ IIKALLTAVT SQHIEIHEGT VLQAVRTCYN
     IYLASKNLIN QTTAKATLTQ MLNVIFARME NQALQEAKQM ERERHRQQQH LLQSPVSHHE
     PESPHLRYLP PQTVDHINQE HEGDLEPQTH DVDKSLQDDT EPENGSDISS AENEQTEADQ
     ATAAETLSKN DILYDGDYEE KPLDIVQSIV EEMVNIIVGD MGEGMAISAS TEGNTGTVED
     GSDSENIQAN GIPGTPISVA YTPSLPDDRL SVSSNDTQES GNSSGPSPGA KFSHILQKDA
     FLVFRSLCKL SMKPLSDGPP DPKSHELRSK ILSLQLLLSI LQNAGPVFRT NEMFINAIKQ
     YLCVALSKNG VSSVPEVFEL SLSIFLTLLS NFKTHLKMQI EVFFKEIFLY ILETSTSSFD
     HKWMVIQTLT RICADAQSVV DIYVNYDCDL NAANIFERLV NDLSKIAQGR GSQELGMSNV
     QELSLRKKGL ECLVSILKCM VEWSKDQYVN PNSQTTLGQE KPSEQEISEV KHPETINRYG
     SLNSLESTSS SGIGSYSTQM SGTDNPEQFE VLKQQKEIIE QGIDLFNKKP KRGIQYLQEQ
     GMLGTTPEDI AQFLHQEERL DSTQVGEFLG DNDKFNKEVM YAYVDQHDFS GKDFVSALRL
     FLEGFRLPGE AQKIDRLMEK FAARYLECNQ GQTLFASADT AYVLAYSIIM LTTDLHSPQV
     KNKMTKEQYI KMNRGINDSK DLPEEYLSAI YNEIAGKKIS MKETKELTIP TKSTKQNVAS
     EKQRRLLYNL EMEQMAKTAK ALMEAVSHVQ APFTSATHLE HVRPMFKLAW TPFLAAFSVG
     LQDCDDTEVA SLCLEGIRCA IRIACIFSIQ LERDAYVQAL ARFTLLTVSS GITEMKQKNI
     DTIKTLITVA HTDGNYLGNS WHEVETLLTL QLNF
//
ID   D3YYL2_MOUSE            Unreviewed;       443 AA.
AC   D3YYL2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 10.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Rgs7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Contains 1 RGS domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC102499; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC113050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC117693; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC117734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC159973; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00875257; -.
DR   Ensembl; ENSMUST00000027812; ENSMUSP00000027812; ENSMUSG00000026527.
DR   Ensembl; ENSMUST00000111184; ENSMUSP00000106815; ENSMUSG00000026527.
DR   MGI; MGI:1346089; Rgs7.
DR   GeneTree; ENSGT00560000076525; -.
DR   Bgee; D3YYL2; -.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005096; F:GTPase activator activity; TAS:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; IDA:MGI.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR015898; G-protein_gamma_dom.
DR   InterPro; IPR000342; Regulat_G_prot_signal.
DR   InterPro; IPR016137; Regulat_G_prot_signal_superfam.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:4.10.260.10; G-protein_gamma_dom; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF00631; G-gamma; 1.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00049; DEP; 1.
DR   SMART; SM00224; GGL; 1.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48670; G-protein_gamma-like; 1.
DR   SUPFAM; SSF48097; Regulat_G_prot_signal_superfam; 1.
DR   PROSITE; PS50186; DEP; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   4: Predicted;
SQ   SEQUENCE   443 AA;  51965 MW;  7C77FB2009424069 CRC64;
     MEDVIARMQD EKNGIPIRTV KSFLSKIPSV FSGSDIVQWL IKNLTIEDPV EALHLGTLMA
     AHGYFFPISD HVLTLKDDGT FYRFQTPYFW PSNCWEPENT DYAVYLCKRT MQNKARLELA
     DYEAESLARL QRAFARKWEF IFMQAEAQAK VDKKRDKIER KILDSQERAF WDVHRPVPGC
     VNTTEVDIKK SSRMRNPHKT RKSVYGLQND IRSHSPTHTP TPETKPPTED ELHQQIKYWQ
     IQLDRHRLKM SKVADSLLSY TEQYVEYDPF LVPPDPSNPW LSDDTTFWEL EASKEPSQQR
     VKRWGFGMDE ALKDPVGREQ FLKFLESEFS SENLRFWLAV EDLKRRPIRE VPSRVQEIWQ
     EFLAPGAPSA INLDSKSYDK TTQNVKEPGR YTFEDAQEHI YKLMKSDSYP RFIRSSAYQE
     LLQAKRKGKT LTSKRLTSLV QSY
//
ID   D3YYM7_MOUSE            Unreviewed;       238 AA.
AC   D3YYM7;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Ahcyl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
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CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; AC069469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC079216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00757274; -.
DR   Ensembl; ENSMUST00000134438; ENSMUSP00000118790; ENSMUSG00000029772.
DR   MGI; MGI:1921590; Ahcyl2.
DR   GeneTree; ENSGT00390000003626; -.
DR   Bgee; D3YYM7; -.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:InterPro.
DR   InterPro; IPR000043; Adenosylhomocysteinase.
DR   InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
DR   PANTHER; PTHR23420; Ad_hcy_hydrolase; 1.
DR   Pfam; PF05221; AdoHcyase; 1.
DR   PROSITE; PS00738; ADOHCYASE_1; 1.
PE   3: Inferred from homology;
SQ   SEQUENCE   238 AA;  26533 MW;  A8CAD3F3CD28CD8F CRC64;
     MLSSKKKYIV NSNSGIKAQV RLSSCLPVLL RRPLPPKIQF ADQKQEFNKR PTKIGRRSLS
     RSISQSSTDS YSSAASYTDS SDDETSPRDK QQKNSKGSSD FCVKNIKQAE FGRREIEIAE
     QEMPALMALR KRAQGEKPLA GAKIVGCTHI TAQTAVLMET LGALGAQCRW AACNIYSTLN
     EVAAALAESG FPVFAWKGES EDDFWWCIDR CVNVEGWQPN MILDDGGDLT HWIYKKYP
//
ID   D3YYN8_MOUSE            Unreviewed;      1691 AA.
AC   D3YYN8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 10.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Cdc42bpa;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC125380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC132436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00830871; -.
DR   Ensembl; ENSMUST00000097453; ENSMUSP00000095062; ENSMUSG00000026490.
DR   MGI; MGI:2441841; Cdc42bpa.
DR   GeneTree; ENSGT00600000084128; -.
DR   Bgee; D3YYN8; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005083; F:small GTPase regulator activity; IEA:InterPro.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR   GO; GO:0007097; P:nuclear migration; IMP:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR001180; Citron.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR014930; Myotonic_dystrophy_kinase_coil.
DR   InterPro; IPR000095; PAK_box_Rho-bd.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF08826; DMPK_coil; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   ProDom; PD011252; Myotonic_dystrophy_kinase_coil; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00285; PBD; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   4: Predicted;
KW   ATP-binding; Kinase; Metal-binding; Nucleotide-binding;
KW   Serine/threonine-protein kinase; Transferase; Zinc.
SQ   SEQUENCE   1691 AA;  192679 MW;  020AB3CE7DDCC3C5 CRC64;
     MSGEVRLRQL EQFILDGPAQ TNGQCFSVET LLDILICLYD ECNNSPLRRE KNILEYLEWA
     KPFTSKVKQM RLHREDFEIL KVIGRGAFGE VAVVKLKNAD KVFAMKILNK WEMLKRAETA
     CFREERDVLV NGDSKWITTL HYAFQDDNNL YLVMDYYVGG DLLTLLSKFE DRLPEEMARF
     YLAEMVIAID SVHQLHYVHR DIKPDNILMD MNGHIRLADF GSCLKLMEDG TVQSSVAVGT
     PDYISPEILQ AMEDGKGRYG PECDWWSLGV CMYEMLYGET PFYAESLVET YGKIMNHKER
     FQFPAQVTDV SENAKDLIRR LICSREHRLG QNGIEDFKKH PFFSGIDWDN IRNCEAPYIP
     EVSSPTDTSN FDVDDDCLKN SETMPPPTHT AFSGHHLPFV GFTYTSSCVL SDRSCLRVTA
     GPTSLDLDVS VQRTLDNNLA TEAYERRIKR LEQEKLELTR KLQESTQTVQ ALQYSTVDGP
     LTASKDLEIK SLKEEIEKLR KQVAEVNHLE QQLEEANSVR RELDDAFRQI KASEKQIKTL
     QQEREELNKE LVQASERLKN QSKELKDAHC QRKLAMQEFM EINERLTELH TQKQKLARHV
     RDKEEEVDLV MQKAESLRQE LRRAERAKKE LEVHTEALIA EASKDKKLRE QSEHYSKQLE
     NELEGLKQKQ ISYSPGICSI EHQQEITKLK TDLEKKSIFY EEEISKREGI HASEIKNLKK
     ELHDSEGQQL ALNKEILVLK DKLEKTRRES QSEREEFENE FKQQYEREKV LLTEENKKLT
     SELDKLTSLY ESLSLRNQHL EEEVKDLADK KESVAHWEAQ ITEIIQWVSD EKDARGYLQA
     LASKMTEELE ALRNSSLGTR ATDMPWKMRR FAKLDMSARL ELQSALDAEI RAKQAIQEEL
     NKVKASNILT ECKLKDSEKK NLELLSEIEQ LIKDTEELRS EKGIEHQDSQ HSFLAFLNTP
     TDALDQFERK THQFFVKSFT APTKCHQCTS LMVGLIRQGC SCEVCGFSCH ITCVNKAPTV
     CPVPPEQTKG PLGIDPQKGV GTAYEGHVRI PKPAGVKKGW QRALAVVCDF KLFLYDIAEG
     KASQPTSVIS QVIDMRDEEF SVSSVLASDV IHASRKDIPC IFRVTASQLS APSNKCSILM
     LADSENERSK WVGVLSELHK ILKKNKFRDR SVYVPKEAYD STLPLIKTTQ AAAIIDHERI
     ALGNEEGLFV VHVTKDEIVR VGDNKKIHQI ELIPSDQLVA VISGRNRHVR LFPMSALDGR
     ETDFYKLAET KGCQTIAAGK VRHGALSCLC VAMKRQVLCY ELFQSKTRHR KFKEIQVPCN
     VQWMAIFSEH LCVGFQSGFL RYPLNGEGGP CNMLHSNDHT LSFISHQPMD ALCAVEISNK
     EYLLCFNSIG IYTDCQGRRS RQQELMWPAN PSSCCYNAPY LSVYSENAVD IFDVNSMEWI
     QTLPLKKVRP LNTEGSLNLL GLETIRLIYF KNKMAEGDEL VVPETSDNSR KQMVRNINNK
     RRYSFRVPEE ERMQQRREML RDPEMRNKLI SNPTNFNHIA HMGPGDGIQI LKDLPMNPRP
     QESRTVFSGS VSIPSITKSR PEPGRSMSAS SGLSARSSAQ NGSALKREFS GGSYNTKRQP
     MPSPSEGSLS SGGMDQGSDA PARDYDGEDS DSPRHSTASN SSNLSSPPSP ISPQKTKSLS
     LESTDRGSWD P
//
ID   D3YYN9_MOUSE            Unreviewed;       438 AA.
AC   D3YYN9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Akt2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC074312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00830259; -.
DR   Ensembl; ENSMUST00000085917; ENSMUSP00000083081; ENSMUSG00000004056.
DR   MGI; MGI:104874; Akt2.
DR   Bgee; D3YYN9; -.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0046328; P:regulation of JNK cascade; IDA:MGI.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   ATP-binding; Kinase; Nucleotide-binding;
KW   Serine/threonine-protein kinase; Transferase.
SQ   SEQUENCE   438 AA;  51056 MW;  D596E57AFD158D53 CRC64;
     MNEVSVIKEG WLHKRGEYIK TWRPRYFLLK SDGSFIGYKE RPEAPDQTLP PLNNFSVAEC
     QLMKTERPRP NTFVIRCLQW TTVIERTFHV DSPDEREEWM RAIQMVANSL KQRGPGEDAM
     DYKCGSPSDS STSEMMEVAV NKARAKVTMN DFDYLKLLGK GTFGKVILVR EKATGRYYAM
     KILRKEVIIA KDEVAHTVTE SRVLQNTRHP FLTALKYAFQ THDRLCFVME YANGGELFFH
     LSRERVFTED RARFYGAEIV SALEYLHSRD VVYRDIKVLE DNDYGRAVDW WGLGVVMYEM
     MCGRLPFYNQ DHERLFELIL MEEIRFPRTL GPEAKSLLAG LLKKDPKQRL GGGPSDAKEV
     MEHRFFLSIN WQDVVQKKLL PPFKPQVTSE VDTRYFDDEF TAQSITITPP DRYDSLDPLE
     LDQRTHFPQF SYSASIRE
//
ID   D3YYY8_MOUSE            Unreviewed;       869 AA.
AC   D3YYY8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 10.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Arhgef26;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC114424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC122883; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00467492; -.
DR   RefSeq; NP_001074764.1; NM_001081295.1.
DR   UniGene; Mm.479530; -.
DR   Ensembl; ENSMUST00000079300; ENSMUSP00000078281; ENSMUSG00000036885.
DR   GeneID; 622434; -.
DR   KEGG; mmu:622434; -.
DR   CTD; 622434; -.
DR   MGI; MGI:1918053; Arhgef26.
DR   GeneTree; ENSGT00550000074493; -.
DR   OrthoDB; EOG46MBHX; -.
DR   Bgee; D3YYY8; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   SH3 domain.
SQ   SEQUENCE   869 AA;  97388 MW;  C4C618260E925DCE CRC64;
     MDGESEVDFS SNGVTPLWRR RSTPPLQLLS RSKPRPQSYQ SPSGLLITDF PVEELAALPT
     PQTPVRVPAD PDDRTVSRSP QLLSAHRRPV TNGRTVSPDY RAASPRLRRP KSPLVSYAAS
     GGSPKSTSNG TVASPAALLS RASRTPDTPA SCATDEDCTG VTASKVSSPI ANGLAHKTDS
     SGPVSQTGQP AGDLELAPSR LSPALPHKSS EQKLPLQRLP SQGNELPNPS VVLSTNSPAA
     LKMGKQQIIP KSLASEIKLS KSNSQNVESH RRLLKVRSMV EGLGAPLGHE GEEGEVDNDM
     DSPGSLRRGL RSTSYRRAVV SGFDFDSPTS SKKKNRMSQP VLKAVMEDKE KFSSLGRIKK
     KILKGQGTFD GEENAVLYQN YKEKALDIDS DEEPEAKEQK AEERIVIHHK PLRSTWSQLS
     AVKRNGLSQT VSQEERKRQE AIFEVISSEH SYLLSLEILI RMFKNSKELT DTMTKTERHH
     LFSNITDVWE ASKKFFTELE ARHQNNIFIE DISDIVEKHT ASTFDPYVKY CTNEVYQQRT
     LQKLLATNPS FKEVLSRIES HEDCRNLPMI SFLILPMQRV TRLPLLMDTI CQKTPKDSPK
     YEVCKRALKE VSKLVRLCNE GARKMERTEM MYTINSQLEF KIKPFPLVSS SRWLVKRGEL
     TAYVEDTVLF SKRMSKQQVY FFLFNDVLII TKKKSEESYN VNDYSLRDQL LVESCDNEEL
     NSSPGKNPST MLYSRQSSAT HLFTLTVLSN HASEKVDMLL GAETQSERAR WITALGHSSG
     KQPPDRTTLT QVEIIRSFTA KQPDELSLQV ADVVLIYQRV GDGWYEGERL RDGERGWFPM
     ECAKEITCQA TIDKNVERMG RLLGLETNV
//
ID   D3YZ39_MOUSE            Unreviewed;      1262 AA.
AC   D3YZ39;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Shank2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC124520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC127546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC140268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC152166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00889283; -.
DR   Ensembl; ENSMUST00000097929; ENSMUSP00000095542; ENSMUSG00000037541.
DR   MGI; MGI:2671987; Shank2.
DR   GeneTree; ENSGT00510000046474; -.
DR   Bgee; D3YZ39; -.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   4: Predicted;
SQ   SEQUENCE   1262 AA;  135412 MW;  BF3B96EFA165D7B9 CRC64;
     MMSVPGGGAA TVMMTGYNNG RYPRNSLYSD CIIEDKTVVL QKKDNEGFGF VLRGAKADTP
     IEEFTPTPAF PALQYLESVD EGGVAWQAGL RTGDFLIEVN NENVVKVGHR QVVNMIRQGG
     NHLILKVVTV TRNLDPDDTA RKKAPPPPKR APTTALTLRS KSMTAELEEL VDKASVRKKK
     DKPEEIVPAS KPSRTAENVA IESRVATIKQ RPTSRCFPAA SDVNSVYERQ GIAVMTPTVP
     GSPKGPFLGL PRGTMRRQKS IDSRIFLSGI TEEERQFLAP PMLKFTRSLS MPDTSEDIPP
     PPQSVPPSPP PPSPTTYNCP RSPTPRVYGT IKPAFNQNPV VAKVPPATRS DTVATMMREK
     GMFYRRELDR FSLDSEDVYS RSPAPQAAFR TKRGQMPENP YSEVGKIASK AVYVPAKPAR
     RKGVLVKQSN VEDSPEKTCS IPIPTIIVKE PSTSSSGKSS QGSSMEIDPQ ATEPGQLRPD
     DSLTVSSPFA AAIAGAVRDR EKRLEARRNS PAFLSTDLGD EDVGLGPPAP RMQASKFPEE
     GGFGDEDETE QPLLPTPGAA PRELENHFLG GGEAGAQGEA GGPLSSTSKA KGPESGPAAP
     LKSSSPAGPE NYVHPLTGRL LDPSSPLALA LSARDRAMQE SQQGHKGEAP KADLNKPLYI
     DTKMRPSVES GFPPVTRQNT RGPLRRQETE NKYETDLGKD RRADDKKNML INIVDTAQQK
     SAGLLMVHTV DVPMAGPPLE EEEDREDGDT KPDHSPSTVP EGVPKTEGAL QISAAPEPAV
     APGRTIVAAG SVEEAVILPF RIPPPPLASV DLDEDFLFTE PLPPPLEFAN SFDIPDDRAA
     SVPALADLVK QKKNDTSQPP TLNSSQPANS TDSKKPAGIS NCLPSSFLPP PESFDAVTDS
     GIEEVDSRSS SDHHLETTST ISTVSSISTL SSEGGESMDT CTVYADGQAF VVDKPPVPPK
     PKMKPIVHKS NALYQDTLPE EDTDGFVIPP PAPPPPPGSA QAGVAKVIQP RTSKLWGDVP
     EVKSPILSGP KANVISELNS ILQQMNRGKS VKPGEGLELP VGAKSANLAP RSPEVMSTVS
     GTRSTTVTFT VRPGTSQPIT LQSRPPDYES RTSGPRRAPS PVVSPTELSK EILPTPPPPS
     ATAASPSPTL SDVFSLPSQS PAGDLFGLNP AGRSRSPSPS ILQQPISNKP FTTKPVHLWT
     KPDVADWLES LNLGEHKETF MDNEIDGSHL PNLQKEDLID LGVTRVGHRM NIERALKQLL
     DR
//
ID   D3YZ57_MOUSE            Unreviewed;       482 AA.
AC   D3YZ57;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 9.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Fyn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC153422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC153537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00927961; -.
DR   ProteinModelPortal; D3YZ57; -.
DR   Ensembl; ENSMUST00000136659; ENSMUSP00000118131; ENSMUSG00000019843.
DR   MGI; MGI:95602; Fyn.
DR   Bgee; D3YZ57; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IDA:MGI.
DR   GO; GO:0015631; F:tubulin binding; IDA:MGI.
DR   GO; GO:0050798; P:activated T cell proliferation; IMP:MGI.
DR   GO; GO:0007166; P:cell surface receptor linked signaling pathway; IDA:MGI.
DR   GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IMP:MGI.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0042552; P:myelination; TAS:MGI.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR   GO; GO:0008360; P:regulation of cell shape; IDA:MGI.
DR   GO; GO:0045471; P:response to ethanol; IGI:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   ATP-binding; Kinase; Nucleotide-binding; SH3 domain; Transferase;
KW   Tyrosine-protein kinase.
SQ   SEQUENCE   482 AA;  54426 MW;  EC74A32C6D33F5FE CRC64;
     MGCVQCKDKE AAKLTEERDG SLNQSSGYRY GTDPTPQHYP SFGVTSIPNY NNFHAAGGQG
     LTVFGGVNSS SHTGTLRTRG GTGVTLFVAL YDYEARTEDD LSFHKGEKFQ ILNSSEGDWW
     EARSLTTGET GYIPSNYVAP VDSIQAEEWY FGKLGRKDAE RQLLSFGNPR GTFLIRESET
     TKGAYSLSIR DWDDMKGDHV KHYKIRKLDN GGYYITTRAQ FETLQQLVQH YSGTWNGNTK
     VAIKTLKPGT MSPESFLEEA QIMKKLKHDK LVQLYAVVSE EPIYIVTEYM SKGSLLDFLK
     DGEGRALKLP NLVDMAAQVA AGMAYIERMN YIHRDLRSAN ILVGNGLICK IADFGLARLI
     EDNEYTARQG AKFPIKWTAP EAALYGRFTI KSDVWSFGIL LTELVTKGRV PYPGMNNREV
     LEQVERGYRM PCPQDCPISL HELMIHCWKK DPEERPTFEY LQGFLEDYFT ATEPQYQPGE
     NL
//
ID   D3YZ62_MOUSE            Unreviewed;      1828 AA.
AC   D3YZ62;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 9.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Myo5a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC133947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CT033761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00928007; -.
DR   ProteinModelPortal; D3YZ62; -.
DR   Ensembl; ENSMUST00000136731; ENSMUSP00000120444; ENSMUSG00000034593.
DR   MGI; MGI:105976; Myo5a.
DR   GeneTree; ENSGT00590000082740; -.
DR   Bgee; D3YZ62; -.
DR   GO; GO:0042641; C:actomyosin; IDA:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0005882; C:intermediate filament; IDA:MGI.
DR   GO; GO:0042470; C:melanosome; IDA:MGI.
DR   GO; GO:0016459; C:myosin complex; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
DR   GO; GO:0030141; C:stored secretory granule; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR   GO; GO:0005516; F:calmodulin binding; IDA:MGI.
DR   GO; GO:0000146; F:microfilament motor activity; IDA:MGI.
DR   GO; GO:0051010; F:microtubule plus-end binding; IPI:MGI.
DR   GO; GO:0042640; P:anagen; IMP:MGI.
DR   GO; GO:0051643; P:endoplasmic reticulum localization; IMP:MGI.
DR   GO; GO:0006887; P:exocytosis; IMP:MGI.
DR   GO; GO:0030073; P:insulin secretion; IMP:MGI.
DR   GO; GO:0031987; P:locomotion involved in locomotory behavior; IMP:MGI.
DR   GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IMP:MGI.
DR   GO; GO:0042438; P:melanin biosynthetic process; IMP:MGI.
DR   GO; GO:0030318; P:melanocyte differentiation; IMP:MGI.
DR   GO; GO:0032402; P:melanosome transport; IDA:MGI.
DR   GO; GO:0042552; P:myelination; IMP:MGI.
DR   GO; GO:0042476; P:odontogenesis; IDA:MGI.
DR   GO; GO:0031585; P:regulation of inositol-1,4,5-triphosphate receptor activity; IMP:MGI.
DR   GO; GO:0032252; P:secretory granule localization; IMP:MGI.
DR   GO; GO:0050808; P:synapse organization; IMP:MGI.
DR   GO; GO:0007268; P:synaptic transmission; IMP:MGI.
DR   GO; GO:0030050; P:vesicle transport along actin filament; TAS:MGI.
DR   GO; GO:0007601; P:visual perception; IMP:MGI.
DR   InterPro; IPR018444; Dil_domain.
DR   InterPro; IPR002710; Dilute.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   Pfam; PF01843; DIL; 1.
DR   Pfam; PF00612; IQ; 6.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 6.
DR   SMART; SM00242; MYSc; 1.
DR   PROSITE; PS51126; DILUTE; 1.
DR   PROSITE; PS50096; IQ; 6.
PE   4: Predicted;
KW   ATP-binding; Motor protein; Myosin; Nucleotide-binding.
SQ   SEQUENCE   1828 AA;  212335 MW;  6672451E710C2428 CRC64;
     MAASELYTKF ARVWIPDPEE VWKSAELLKD YKPGDKVLLL HLEEGKDLEY RLDPKTGELP
     HLRNPDILVG ENDLTALSYL HEPAVLHNLR VRFIDSKLIY TYCGIVLVAI NPYEQLPIYG
     EDIINAYSGQ NMGDMDPHIF AVAEEAYKQM ARDERNQSII VSGESGAGKT VSAKYAMRYF
     ATVSGSASEA NVEEKVLASN PIMESIGNAK TTRNDNSSRF GKYIEIGFDK RYRIIGANMR
     TYLLEKSRVV FQAEEERNYH IFYQLCASAK LPEFKMLRLG NADSFHYTKQ GGSPMIEGVD
     DAKEMAHTRQ ACTLLGISES YQMGIFRILA GILHLGNVGF ASRDSDSCTI PPKHEPLTIF
     CDLMGVDYEE MCHWLCHRKL ATATETYIKP ISKLQATNAR DALAKHIYAK LFNWIVDHVN
     QALHSAVKQH SFIGVLDIYG FETFEINSFE QFCINYANEK LQQQFNMHVF KLEQEEYMKE
     QIPWTLIDFY DNQPCINLIE SKLGILDLLD EECKMPKGTD DTWAQKLYNT HLNKCALFEK
     PRMSNKAFII KHFADKVEYQ CEGFLEKNKD TVFEEQIKVL KSSKFKMLPE LFQDDEKAIS
     PTSATSSGRT PLTRVPVKPT KGRPGQTAKE HKKTVGHQFR NSLHLLMETL NATTPHYVRC
     IKPNDFKFPF TFDEKRAVQQ LRACGVLETI RISAAGFPSR WTYQEFFSRY RVLMKQKDVL
     GDRKQTCKNV LEKLILDKDK YQFGKTKIFF RAGQVAYLEK LRADKLRAAC IRIQKTIRGW
     LLRKRYLCMQ RAAITVQRYV RGYQARCYAK FLRRTKAATT IQKYWRMYVV RRRYKIRRAA
     TIVIQSYLRG YLTRNRYRKI LREYKAVIIQ KRVRGWLART HYKRTMKAIV YLQCCFRRMM
     AKRELKKLKI EARSVERYKK LHIGMENKIM QLQRKVDEQN KDYKCLMEKL TNLEGVYNSE
     TEKLRNDVER LQLSEEEAKV ATGRVLSLQE EIAKLRKDLE QTRSEKKSIE ERADKYKQET
     DQLVSNLKEE NTLLKQEKET LNHRIVEQAK EMTETMERKL VEETKQLELD LNDERLRYQN
     LLNEFSRLEE RYDDLKEEMT LMLNVPKPGH KRTDSTHSSN ESEYTFSSEF AETEDIAPRT
     EEPIEKKVPL DMSLFLKLQK RVTELEQEKQ LMQDELDRKE EQVFRSKAKE EERPQIRGAE
     LEYESLKRQE LESENKKLKN ELNELRKALS EKSAPEVTAP GAPAYRVLME QLTSVSEELD
     VRKEEVLILR SQLVSQKEAI QPKDDKNTMT DSTILLEDVQ KMKDKGEIAQ AYIGLKETNR
     LLESQLQSQK RSHENEAEAL RGEIQSLKEE NNRQQQLLAQ NLQLPPEARI EASLQHEITR
     LTNENLDLME QLEKQDKTVR KLKKQLKVFA KKIGELEVGQ MENISPGQII DEPIRPVNIP
     RKEKDFQGML EYKREDEQKL VKNLILELKP RGVAVNLIPG LPAYILFMCV RHADYLNDDQ
     KVRSLLTSTI NSIKKVLKKR GDDFETVSFW LSNTCRFLHC LKQYSGEEGF MKHNTSRQNE
     HCLTNFDLAE YRQVLSDLAI QIYQQLVRVL ENILQPMIVS GMLEHETIQG VSGVKPTGLR
     KRTSSIADEG TYTLDSILRQ LNSFHSVMCQ HGMDPELIKQ VVKQMFYIVG AITLNNLLLR
     KDMCSWSKGM QIRYNVSQLE EWLRDKNLMN SGAKETLEPL IQAAQLLQVK KKTDDDAEAI
     CSMCNALTTA QIVKVLNLYT PVNEFEERVS VSFIRTIQMR LRDRKDSPQL LMDAKHIFPV
     TFPFNPSSLA LETIQIPASL GLGFIARV
//
ID   D3YZI9_MOUSE            Unreviewed;       523 AA.
AC   D3YZI9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 5.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Pgbd5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC114005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC126930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00272854; -.
DR   Ensembl; ENSMUST00000140012; ENSMUSP00000120984; ENSMUSG00000050751.
DR   MGI; MGI:2429955; Pgbd5.
DR   OrthoDB; EOG41JZC3; -.
DR   Bgee; D3YZI9; -.
PE   4: Predicted;
SQ   SEQUENCE   523 AA;  58300 MW;  F6F419B2DFAF5FB8 CRC64;
     MAEGGGGSRR RAPALLEAAR ARYESLHISD DVFGESGPDS GGNPFYSTSA ASRSSSAASS
     DDERERPAPP GTAPPSYAAD PLELEEDETG GGWSAVLRDR PSPRFEDTGG PTRKMPPSAS
     AVDFFQLFVP DNVLKNMVVQ TNMYARKFQE RFGSDGAWVE VTLAEMKAFL GYVISTSVSH
     CESVLSIWSG GFYSNRSLAL VMSQARFEKI LKYFHVVAFR SSQTTHGLYK VQPFLDSLQS
     GFDAAFRPSQ TQVLHEPLID EDPVFIATCT ERELRKRKKR KFSLWVRQCS STGFIIQIYV
     HLKEGGGPDG LDALKNKPQL HSMVARSLCR NAAGKNYIIF TGPSITSLNL FEEFEKQGIY
     CCGLLSSRKS DCTGLPPSML TNPATPLARG QHQIRTKGNM SLICWYNKGH FRFLTNAYSP
     VQKGVIIKRR SGEIPCPLAV EAFAAHLSYI CRYDDKYSKY FISHKPNKTW QQVFWFAISI
     AVNNAYILYK MSDAYHVKKY SRAQFGERLV RELLGLEDSS PAH
//
ID   D3YZP9_MOUSE            Unreviewed;       469 AA.
AC   D3YZP9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 10.
DE   SubName: Full=MCG115019;
DE   SubName: Full=Uncharacterized protein;
GN   Name=Ccdc6; ORFNames=mCG_115019;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; AC132435; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466553; EDL31982.1; -; Genomic_DNA.
DR   IPI; IPI00381495; -.
DR   RefSeq; NP_001104591.1; NM_001111121.1.
DR   UniGene; Mm.281741; -.
DR   Ensembl; ENSMUST00000147545; ENSMUSP00000123374; ENSMUSG00000048701.
DR   GeneID; 76551; -.
DR   KEGG; mmu:76551; -.
DR   CTD; 76551; -.
DR   MGI; MGI:1923801; Ccdc6.
DR   GeneTree; ENSGT00390000013594; -.
DR   OrthoDB; EOG4868CT; -.
DR   Bgee; D3YZP9; -.
DR   InterPro; IPR019152; DUF2046.
DR   PANTHER; PTHR15276; DUF2046; 1.
DR   Pfam; PF09755; DUF2046; 1.
PE   4: Predicted;
SQ   SEQUENCE   469 AA;  52939 MW;  708882EB2F131354 CRC64;
     MADSASESDT DAAGGGPAAM QSSCSATSGG SGGGGGGKSG GIVISPFRLE ELTNRLASLQ
     QENKVLKIEL ETYKLKCKAL QEENRDLRKA SVTIQARAEQ EEEFISNTLF KKIQALQKEK
     ETLAVNYEKE EEFLTNELSR KLMQLQHEKA ELEQHLEQEQ EFQVNKLMKK IKKLENDTIS
     KQLTLEQLRR EKIDLENTLE QEQEALVNRL WKRMDKLEAE KRILQEKLDQ PVSAPPSPRD
     ISMEIDSPEN MMRHIRFLKN EVERLKKQLR AAQLQHSEKM AQYLEEERHM REENLRLQRK
     LQREMERREA LCRQLSESES SLEMDDERYF NEMSAQGLRP RTVSSPIPYT PSPSSSRPIS
     PGLSYASHTV GFTPPTSLTR AGMSYYNSPG LHVQHMGASH GITRPSPRRS SSPDKFKRPT
     PPPSPNTQSP VQPPPPPPPP PMQPAVPSAA PTQPAPTQPQ HPVHPSSQP
//
ID   D3YZR2_MOUSE            Unreviewed;       857 AA.
AC   D3YZR2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 11.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Nrg2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC127350; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC131191; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00407953; -.
DR   RefSeq; NP_001161363.1; NM_001167891.1.
DR   UniGene; Mm.380390; -.
DR   Ensembl; ENSMUST00000115713; ENSMUSP00000111378; ENSMUSG00000060275.
DR   GeneID; 100042150; -.
DR   KEGG; mmu:100042150; -.
DR   CTD; 100042150; -.
DR   MGI; MGI:1098246; Nrg2.
DR   GeneTree; ENSGT00390000017243; -.
DR   OrthoDB; EOG4J9MZF; -.
DR   Bgee; D3YZR2; -.
DR   GO; GO:0009790; P:embryo development; IEA:InterPro.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR002154; Neuregulin_1_C.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF02158; Neuregulin; 1.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00408; IGc2; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   4: Predicted;
KW   EGF-like domain.
SQ   SEQUENCE   857 AA;  92549 MW;  0FEB83F4944EC4C8 CRC64;
     MRQVCCSALP PPLEKARCSS YSYSYSDSSS STTSSSRSSS SSSSRNSSSS NSSSSESSGS
     NSGSSSIFRP AAPPEPRPQP QPQPRSPAAR RAAARSRAAA AGGMRRDPAP GFSMLLFGVS
     LACYSPSLKS VQDQAYKAPV VVEGKVQGLA PAGGSSSNST REPPASGRVA LVKVLDKWPL
     RSGGLQREQV ISVGSCAPLE RNQRYIFFLE PTEQPLVFKT AFAPVDPNGK NIKKEVGKIL
     CTDCATRPKL KKMKSQTGEV GEKQSLKCEA AAGNPQPSYR WFKDGKELNR SRDIRIKYGN
     GRKNSRLQFN KVRVEDAGEY VCEAENILGK DTVRGRLHVN SVSTTLSSWS GHARKCNETA
     KSYCVNGGVC YYIEGINQLS CKCPNGFFGQ RCLEKLPLRL YMPDPKQKAE ELYQKRVLTI
     TGICVALLVV GIVCVVAYCK TKKQRRQMHH HLRQNMCPAH QNRSLANGPS HPRLDPEEIQ
     MADYISKNVP ATDHVIRREA ETTFSGSHSC SPSHHCSTAT PTSSHRHESH TWSLERSESL
     TSDSQSGIML SSVGTSKCNS PACVEARARR AAAYSQEERR RAAMPPYHDS IDSLRDSPHS
     ERYVSALTTP ARLSPVDFHY SLATQVPTFE ITSPNSAHAV SLPPAAPISY RLAEQQPLLR
     HPAPPGPGPG SGPGADMQRS YDSYYYPAAG PGPRRSACAL GGSLGSLPAS PFRIPEDDEY
     ETTQECAPPP PPRPRTRGAS RRTSAGPRRW RRSRLNGLAA QRARAARDSL SLSSGSGCGS
     ASASDDDADD ADGALAAEST PFLGLRAAHD ALRSDSPPLC PAADSRTYYS LDSHSTRASS
     RHSRGPPTRA KQDSGPL
//
ID   D3YZT9_MOUSE            Unreviewed;       210 AA.
AC   D3YZT9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 9.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Eef1d;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC116520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00831082; -.
DR   Ensembl; ENSMUST00000141268; ENSMUSP00000115553; ENSMUSG00000055762.
DR   MGI; MGI:1913906; Eef1d.
DR   GeneTree; ENSGT00390000011747; -.
DR   Bgee; D3YZT9; -.
DR   GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro.
DR   InterPro; IPR018940; EF-1_beta_acid_region_euk.
DR   InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
DR   Pfam; PF10587; EF-1_beta_acid; 1.
DR   PROSITE; PS00824; EF1BD_1; 1.
PE   4: Predicted;
SQ   SEQUENCE   210 AA;  23172 MW;  6F6B6CE178B22DC6 CRC64;
     MATNFLAHEK IWFDKFKYDD AERRFYEQMN GPVTSGSRQE NGASVILRDI ARARENIQKS
     LAGLKVMLPN SPEALGQATP GTSSGPGASS GPGGDHSELI VRITSLEVEN QNLRGVVQDL
     QQAISKLEAR LSSLEKSSPT PRATAPQTQH VSPMRQVEPP TKKGATPAED DEDKDIDLFG
     SDEEEEDKEA ARLREERLRQ YAEKKAKKPT
//
ID   D3YZU1_MOUSE            Unreviewed;      2167 AA.
AC   D3YZU1;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 10.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Shank1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC152939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00465999; -.
DR   RefSeq; NP_001029287.1; NM_001034115.1.
DR   UniGene; Mm.360368; -.
DR   Ensembl; ENSMUST00000107938; ENSMUSP00000103571; ENSMUSG00000038738.
DR   GeneID; 243961; -.
DR   KEGG; mmu:243961; -.
DR   CTD; 243961; -.
DR   MGI; MGI:3613677; Shank1.
DR   GeneTree; ENSGT00510000046474; -.
DR   OrthoDB; EOG48PMJ9; -.
DR   Bgee; D3YZU1; -.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   ANK repeat; Repeat.
SQ   SEQUENCE   2167 AA;  226317 MW;  A732912793A975AE CRC64;
     MTHSPATSED EERHSASECP EGGSESDSSP DGPGRGPQGT RGRGSGAPGN LASTRGLQGR
     SMSVPDDAHF SMMVFRIGIP DLHQTKCLRF NPDATIWTAK QQVLCALSES LQDVLNYGLF
     QPATSGRDAN FLEEERLLRE YPQSFEKGVP YLEFRYKTRV YKQTNLDEKQ LAKLHTKTGL
     KKFLEYVQLG TSDKVARLLD KGLDPNYHDS DSGETPLTLA AQTEGSVEVI RTLCLGGAHI
     DFRARDGMTA LHKAACARHC LALTALLDLG GSPNYKDRRG LTPLFHTAMV GGDPRCCELL
     LYNRAQLGIA DENGWQEIHQ ACQRGHSQHL EHLLFYGAEP GAQNASGNTA LHICALYNKE
     TCARILLYRG ANKDVKNNNG QTPFQVAVIA GNFELGELIR NHREQDVVPF QESPKYAARR
     RGPPGAGLTV PPALLRANSD TSMALPDWMV FSAPGASSSG TPGPTSGSQG QSQPSAPSTK
     LSSGTLRSAS SPRGARARSP SRGRHPEDAK RQPRGRPSSS GTPRDGPAGG TGGSGGPGGS
     LGSRGRRRKL YSAVPGRSFM AVKSYQAQGE GEISLSKGEK IKVLSIGEGG FWEGQVKGRV
     GWFPSDCLEE VANRSQEGRQ ESRSDKAKRL FRHYTVGSYD SFDAPSLIDG IDSGSDYIIK
     EKTVLLQKKD SEGFGFVLRG AKAQTPIEEF TPTPAFPALQ YLESVDEGGV AWRAGLRMGD
     FLIEVNGQNV VKVGHRQVVN MIRQGGNTLM VKVVMVTRHP DMDEAVHKKA SQQAKRLPPP
     AISLRSKSMT SELEEMVSPW KKKIEYEQQP AAVPSMEKKR TVYQMALNKL DEILAAAQQT
     ISASESPGPG GLASLGKHRP KGFFATESSF DPHHRSQPSY DRPSFLPPGP GLMLRQKSIG
     AAEDDRPYLA PPAMKFSRSL SVPGSEDIPP PPTTSPPEPP YSTPPAPSSS GRLTPSPRGG
     PFNPGSGGPL PASSPSSFDG PSPPDPRSGG REKSLYHSGA LPPAHHHPPH HHHHHAPPPQ
     PHHHHAHPPH PPEMETGGSP DDPPPRLALG PQPSLRGWRG GGPSPTSGAP SPSHHSSSGG
     SSGPAQAPAL RYFQLPPRAA SAAMYVPARS GRGRKGPLVK QTKVEGEPQK GSLPPASSPT
     SPALPRSEPP PAGPSEKNSI PIPTIIIKAP STSSSGRSSQ GSSTEAEPPT QPDGAGGGGS
     SPSPAPATSP VPPSPSPVPT PASPSGPATL DFTSQFGAAL VGAARREGGW QNEARRRSTL
     FLSTDAGDED GGDSGLGPGA PPGPRLRHSK SIDEGMFSAE PYLRLESGGS SGGYGAYAAG
     SRAYGGSGSS SAFTSFLPPR PLVHPLTGKA LDPASPLGLA LAARERALKE SSEGGVTPQP
     PPRPPSPRYD APPPTLHHHS PHSPHSPHAR HEPVLRLWGD PARRELGYRA GLGSQEKALT
     ASPPAARRSL LHRLPPTAPG VGPLLLQLGP EPPTPHPGVS KAWRTAAPEE PERLPLHVRF
     LENCQARPPP AGTRGSSTED GPGVPPPSPR RVLPTSPTSP RGNEENGLPL LVLPPPAPSV
     DVDDGEFLFA EPLPPPLEFS NSFEKPESPL TPGPPHPLPD PPSPATPLPA APPPAVAAAP
     PTLDSTASSL TSYDSEVATL TQGAPAAPGD PPAPGPPAPA APAPPAPQPG PDPPPGTDSG
     IEEVDSRSSS DHPLETISSA STLSSLSAEG GGNTGGVAGG GAGVASGTEL LDTYVAYLDG
     QAFGGSGTPG PPYPPQLMTP SKLRGRALGT SGNLRPGPSG GLRDPVTPTS PTVSVTGAGT
     DGLLALSACS GPSTAGVAGG PVAVEPEVPP VPLPTASSLP RKLLPWEEGP GPPPPPLPGP
     LSQPQASALA TVKASIISEL SSKLQQFGGA STAGGALPWA RGGSGGSTDS HHGGASYIPE
     RTSSLQRQRL SEDSQTSLLS KPSSSIFQNW PKPPLPPLPT GSGVSSSTAA APGATSPSAS
     SASASTRHLQ GVEFEMRPPL LRRAPSPSLL PASDHKVSPA PRPSSLPILP SGPLYPGLFD
     IRSSPTGGAG GSADPFAPVF VPPHPGISGG LGGALSGASR SLSPTRLLSL PPDKPFGAKP
     LGFWTKFDVA DWLEWLGLSE HRAQFLDHEI DGSHLPALTK EDYVDLGVTR VGHRMNIDRA
     LKFFLER
//
ID   D3YZU4_MOUSE            Unreviewed;      2159 AA.
AC   D3YZU4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Shank1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC152939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00758339; -.
DR   Ensembl; ENSMUST00000107935; ENSMUSP00000103568; ENSMUSG00000038738.
DR   MGI; MGI:3613677; Shank1.
DR   GeneTree; ENSGT00510000046474; -.
DR   Bgee; D3YZU4; -.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   ANK repeat; Repeat.
SQ   SEQUENCE   2159 AA;  225350 MW;  78EA8FD9E436C06F CRC64;
     MTHSPATSED EERHSASECP EGGSESDSSP DGPGRGPQGT RGRGSGAPGN LASTRGLQGR
     SMSVPDDAHF SMMVFRIGIP DLHQTKCLRF NPDATIWTAK QQVLCALSES LQDVLNYGLF
     QPATSGRDAN FLEEERLLRE YPQSFEKGVP YLEFRYKTRV YKQTNLDEKQ LAKLHTKTGL
     KKFLEYVQLG TSDKVARLLD KGLDPNYHDS DSGETPLTLA AQTEGSVEVI RTLCLGGAHI
     DFRARDGMTA LHKAACARHC LALTALLDLG GSPNYKDRRG LTPLFHTAMV GGDPRCCELL
     LYNRAQLGIA DENGWQEIHQ ACQRGHSQHL EHLLFYGAEP GAQNASGNTA LHICALYNKE
     TCARILLYRG ANKDVKNNNG QTPFQVAVIA GNFELGELIR NHREQDVVPF QESPKYAARR
     RGPPGAGLTV PPALLRANSD TSMALPDWMV FSAPGASSSG TPGPTSGSQG QSQPSAPSTK
     LSSGTLRSAS SPRGARARSP SRGRHPEDAK RQPRGRPSSS GTPRDGPAGG TGGSGGPGGS
     LGSRGRRRKL YSAVPGRSFM AVKSYQAQGE GEISLSKGEK IKVLSIGEGG FWEGQVKGRV
     GWFPSDCLEE VANRSQEGRQ ESRSDKAKRL FRHYTVGSYD SFDAPSLIDG IDSGSDYIIK
     EKTVLLQKKD SEGFGFVLRG AKAQTPIEEF TPTPAFPALQ YLESVDEGGV AWRAGLRMGD
     FLIEVNGQNV VKVGHRQVVN MIRQGGNTLM VKVVMVTRHP DMDEAVHKKA SQQAKRLPPP
     AISLRSKSMT SELEEMEYEQ QPAAVPSMEK KRTVYQMALN KLDEILAAAQ QTISASESPG
     PGGLASLGKH RPKGFFATES SFDPHHRSQP SYDRPSFLPP GPGLMLRQKS IGAAEDDRPY
     LAPPAMKFSR SLSVPGSEDI PPPPTTSPPE PPYSTPPAPS SSGRLTPSPR GGPFNPGSGG
     PLPASSPSSF DGPSPPDPRS GGREKSLYHS GALPPAHHHP PHHHHHHAPP PQPHHHHAHP
     PHPPEMETGG SPDDPPPRLA LGPQPSLRGW RGGGPSPTSG APSPSHHSSS GGSSGPAQAP
     ALRYFQLPPR AASAAMYVPA RSGRGRKGPL VKQTKVEGEP QKGSLPPASS PTSPALPRSE
     PPPAGPSEKN SIPIPTIIIK APSTSSSGRS SQGSSTEAEP PTQPDGAGGG GSSPSPAPAT
     SPVPPSPSPV PTPASPSGPA TLDFTSQFGA ALVGAARREG GWQNEARRRS TLFLSTDAGD
     EDGGDSGLGP GAPPGPRLRH SKSIDEGMFS AEPYLRLESG GSSGGYGAYA AGSRAYGGSG
     SSSAFTSFLP PRPLVHPLTG KALDPASPLG LALAARERAL KESSEGGVTP QPPPRPPSPR
     YDAPPPTLHH HSPHSPHSPH ARHEPVLRLW GDPARRELGY RAGLGSQEKA LTASPPAARR
     SLLHRLPPTA PGVGPLLLQL GPEPPTPHPG VSKAWRTAAP EEPERLPLHV RFLENCQARP
     PPAGTRGSST EDGPGVPPPS PRRVLPTSPT SPRGNEENGL PLLVLPPPAP SVDVDDGEFL
     FAEPLPPPLE FSNSFEKPES PLTPGPPHPL PDPPSPATPL PAAPPPAVAA APPTLDSTAS
     SLTSYDSEVA TLTQGAPAAP GDPPAPGPPA PAAPAPPAPQ PGPDPPPGTD SGIEEVDSRS
     SSDHPLETIS SASTLSSLSA EGGGNTGGVA GGGAGVASGT ELLDTYVAYL DGQAFGGSGT
     PGPPYPPQLM TPSKLRGRAL GTSGNLRPGP SGGLRDPVTP TSPTVSVTGA GTDGLLALSA
     CSGPSTAGVA GGPVAVEPEV PPVPLPTASS LPRKLLPWEE GPGPPPPPLP GPLSQPQASA
     LATVKASIIS ELSSKLQQFG GASTAGGALP WARGGSGGST DSHHGGASYI PERTSSLQRQ
     RLSEDSQTSL LSKPSSSIFQ NWPKPPLPPL PTGSGVSSST AAAPGATSPS ASSASASTRH
     LQGVEFEMRP PLLRRAPSPS LLPASDHKVS PAPRPSSLPI LPSGPLYPGL FDIRSSPTGG
     AGGSADPFAP VFVPPHPGIS GGLGGALSGA SRSLSPTRLL SLPPDKPFGA KPLGFWTKFD
     VADWLEWLGL SEHRAQFLDH EIDGSHLPAL TKEDYVDLGV TRVGHRMNID RALKFFLER
//
ID   D3YZU5_MOUSE            Unreviewed;      2158 AA.
AC   D3YZU5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Shank1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC152939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00606039; -.
DR   Ensembl; ENSMUST00000107934; ENSMUSP00000103567; ENSMUSG00000038738.
DR   MGI; MGI:3613677; Shank1.
DR   GeneTree; ENSGT00510000046474; -.
DR   Bgee; D3YZU5; -.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   ANK repeat; Repeat.
SQ   SEQUENCE   2158 AA;  225459 MW;  AA1791F0B367E1EE CRC64;
     MTHSPATSED EERHSASECP EGGSESDSSP DGPGRGPQGT RGRGSGAPGN LASTRGLQGR
     SMSVPDDAHF SMMVFRIGIP DLHQTKCLRF NPDATIWTAK QQVLCALSES LQDVLNYGLF
     QPATSGRDAN FLEEERLLRE YPQSFEKGVP YLEFRYKTRV YKQTNLDEKQ LAKLHTKTGL
     KKFLEYVQLG TSDKVARLLD KGLDPNYHDS DSGETPLTLA AQTEGSVEVI RTLCLGGAHI
     DFRARDGMTA LHKAACARHC LALTALLDLG GSPNYKDRRG LTPLFHTAMV GGDPRCCELL
     LYNRAQLGIA DENGWQEIHQ ACQRGHSQHL EHLLFYGAEP GAQNASGNTA LHICALYNKE
     TCARILLYRG ANKDVKNNNG QTPFQVAVIA GNFELGELIR NHREQDVVPF QESPKYAARR
     RGPPGAGLTV PPALLRANSD TSMALPDWMV FSAPGASSSG TPGPTSGSQG QSQPSAPSTK
     LSSGTLRSAS SPRGARARSP SRGRHPEDAK RQPRGRPSSS GTPRDGPAGG TGGSGGPGGS
     LGSRGRRRKL YSAVPGRSFM AVKSYQAQGE GEISLSKGEK IKVLSIGEGG FWEGQVKGRV
     GWFPSDCLEE VANRSQEGRQ ESRSDKAKRL FRHYTVGSYD SFDAPSDYII KEKTVLLQKK
     DSEGFGFVLR GAKAQTPIEE FTPTPAFPAL QYLESVDEGG VAWRAGLRMG DFLIEVNGQN
     VVKVGHRQVV NMIRQGGNTL MVKVVMVTRH PDMDEAVHKK ASQQAKRLPP PAISLRSKSM
     TSELEEMVSP WKKKIEYEQQ PAAVPSMEKK RTVYQMALNK LDEILAAAQQ TISASESPGP
     GGLASLGKHR PKGFFATESS FDPHHRSQPS YDRPSFLPPG PGLMLRQKSI GAAEDDRPYL
     APPAMKFSRS LSVPGSEDIP PPPTTSPPEP PYSTPPAPSS SGRLTPSPRG GPFNPGSGGP
     LPASSPSSFD GPSPPDPRSG GREKSLYHSG ALPPAHHHPP HHHHHHAPPP QPHHHHAHPP
     HPPEMETGGS PDDPPPRLAL GPQPSLRGWR GGGPSPTSGA PSPSHHSSSG GSSGPAQAPA
     LRYFQLPPRA ASAAMYVPAR SGRGRKGPLV KQTKVEGEPQ KGSLPPASSP TSPALPRSEP
     PPAGPSEKNS IPIPTIIIKA PSTSSSGRSS QGSSTEAEPP TQPDGAGGGG SSPSPAPATS
     PVPPSPSPVP TPASPSGPAT LDFTSQFGAA LVGAARREGG WQNEARRRST LFLSTDAGDE
     DGGDSGLGPG APPGPRLRHS KSIDEGMFSA EPYLRLESGG SSGGYGAYAA GSRAYGGSGS
     SSAFTSFLPP RPLVHPLTGK ALDPASPLGL ALAARERALK ESSEGGVTPQ PPPRPPSPRY
     DAPPPTLHHH SPHSPHSPHA RHEPVLRLWG DPARRELGYR AGLGSQEKAL TASPPAARRS
     LLHRLPPTAP GVGPLLLQLG PEPPTPHPGV SKAWRTAAPE EPERLPLHVR FLENCQARPP
     PAGTRGSSTE DGPGVPPPSP RRVLPTSPTS PRGNEENGLP LLVLPPPAPS VDVDDGEFLF
     AEPLPPPLEF SNSFEKPESP LTPGPPHPLP DPPSPATPLP AAPPPAVAAA PPTLDSTASS
     LTSYDSEVAT LTQGAPAAPG DPPAPGPPAP AAPAPPAPQP GPDPPPGTDS GIEEVDSRSS
     SDHPLETISS ASTLSSLSAE GGGNTGGVAG GGAGVASGTE LLDTYVAYLD GQAFGGSGTP
     GPPYPPQLMT PSKLRGRALG TSGNLRPGPS GGLRDPVTPT SPTVSVTGAG TDGLLALSAC
     SGPSTAGVAG GPVAVEPEVP PVPLPTASSL PRKLLPWEEG PGPPPPPLPG PLSQPQASAL
     ATVKASIISE LSSKLQQFGG ASTAGGALPW ARGGSGGSTD SHHGGASYIP ERTSSLQRQR
     LSEDSQTSLL SKPSSSIFQN WPKPPLPPLP TGSGVSSSTA AAPGATSPSA SSASASTRHL
     QGVEFEMRPP LLRRAPSPSL LPASDHKVSP APRPSSLPIL PSGPLYPGLF DIRSSPTGGA
     GGSADPFAPV FVPPHPGISG GLGGALSGAS RSLSPTRLLS LPPDKPFGAK PLGFWTKFDV
     ADWLEWLGLS EHRAQFLDHE IDGSHLPALT KEDYVDLGVT RVGHRMNIDR ALKFFLER
//
ID   D3YZV2_MOUSE            Unreviewed;       769 AA.
AC   D3YZV2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 11.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Kcnc3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC157653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00831479; -.
DR   RefSeq; NP_032448.2; NM_008422.2.
DR   UniGene; Mm.40312; -.
DR   ProteinModelPortal; D3YZV2; -.
DR   Ensembl; ENSMUST00000107907; ENSMUSP00000103540; ENSMUSG00000062785.
DR   GeneID; 16504; -.
DR   KEGG; mmu:16504; -.
DR   CTD; 16504; -.
DR   MGI; MGI:96669; Kcnc3.
DR   GeneTree; ENSGT00580000081499; -.
DR   OrthoDB; EOG4W9J3M; -.
DR   Bgee; D3YZV2; -.
DR   GO; GO:0030673; C:axolemma; IDA:MGI.
DR   GO; GO:0043679; C:axon terminus; IDA:MGI.
DR   GO; GO:0032590; C:dendrite membrane; IDA:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0032809; C:neuronal cell body membrane; IDA:MGI.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0046928; P:regulation of neurotransmitter secretion; IMP:MGI.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003974; K_chnl_volt-dep_Kv3.
DR   InterPro; IPR005404; K_chnl_volt-dep_Kv3.3.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01582; KV33CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01498; SHAWCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
PE   4: Predicted;
KW   Ion transport; Ionic channel; Membrane; Potassium; Potassium channel;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
SQ   SEQUENCE   769 AA;  81946 MW;  E482F3B2216870F5 CRC64;
     MLSSVCVWSF RGRQGTGKQQ PQPVPTPQPP ESSPPPLPPP QQQQCSQPGT AASPAGAPLS
     CGPGGRRAEP CPGLPAVAMG RHGGGGGDSG KIVINVGGVR HETYRSTLRT LPGTRLAGLT
     EPEAAARFDY DPGTDEFFFD RHPGVFAYVL NYYRTGKLHC PADVCGPLFE EELGFWGIDE
     TDVEACCWMT YRQHRDAEEA LDSFEAPDSS ANANANAGGA HDAGLDDEAG AGGGGLDGAG
     GELKRLCFQD AGGGAGGPAG GAGGAGGTWW RRWQPRVWAL FEDPYSSRAA RYVAFASLFF
     ILISITTFCL ETHEGFIHIS NKTVTQASPI PGAPPENITN VEVETEPFLT YVEGVCVVWF
     TFEFLMRVTF CPDKVEFLKS SLNIIDCVAI LPFYLEVGLS GLSSKAAKDV LGFLRVVRFV
     RILRIFKLTR HFVGLRVLGH TLRASTNEFL LLIIFLALGV LIFATMIYYA ERIGADPDDI
     LGSNHTYFKN IPIGFWWAVV TMTTLGYGDM YPKTWSGMLV GALCALAGVL TIAMPVPVIV
     NNFGMYYSLA MAKQKLPKKK NKHIPRPPQP GSPNYCKPDP PPPPPPHPHH GSGGISPPPP
     ITPPSMGVNV AGAYPPGPHT HPGLLRGGAG GLGIMGLPPL PAPGEPCPLA QEEVIETNRA
     DPRPNGDPAA AALAHEDCPA IDQPAMSPED KSPITPGSRG RYSRDRACFL VTDYAPSPDG
     SIRKGYEKSR SLSSIVGLSG VSLRLAPLAT PPGSPRATRR APPTLPSIL
//
ID   D3YZV4_MOUSE            Unreviewed;       729 AA.
AC   D3YZV4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 9.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Kcnc3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC157653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00844657; -.
DR   Ensembl; ENSMUST00000107905; ENSMUSP00000103538; ENSMUSG00000062785.
DR   MGI; MGI:96669; Kcnc3.
DR   GeneTree; ENSGT00580000081499; -.
DR   Bgee; D3YZV4; -.
DR   GO; GO:0030673; C:axolemma; IDA:MGI.
DR   GO; GO:0043679; C:axon terminus; IDA:MGI.
DR   GO; GO:0032590; C:dendrite membrane; IDA:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0032809; C:neuronal cell body membrane; IDA:MGI.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0046928; P:regulation of neurotransmitter secretion; IMP:MGI.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003974; K_chnl_volt-dep_Kv3.
DR   InterPro; IPR005404; K_chnl_volt-dep_Kv3.3.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01582; KV33CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01498; SHAWCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
PE   4: Predicted;
KW   Ion transport; Ionic channel; Membrane; Potassium; Potassium channel;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
SQ   SEQUENCE   729 AA;  77791 MW;  00FF674A604AFEBC CRC64;
     MLSSVCVWSF RGRQGTGKQQ PQPVPTPQPP ESSPPPLPPP QQQQCSQPGT AASPAGAPLS
     CGPGGRRAEP CPGLPAVAMG RHGGGGGDSG KIVINVGGVR HETYRSTLRT LPGTRLAGLT
     EPEAAARFDY DPGTDEFFFD RHPGVFAYVL NYYRTGKLHC PADVCGPLFE EELGFWGIDE
     TDVEACCWMT YRQHRDAEEA LDSFEAPDSS ANANANAGGA HDAGLDDEAG AGGGGLDGAG
     GELKRLCFQD AGGGAGGPAG GAGGAGGTWW RRWQPRVWAL FEDPYSSRAA RYVAFASLFF
     ILISITTFCL ETHEGFIHIS NKTVTQASPI PGAPPENITN VEVETEPFLT YVEGVCVVWF
     TFEFLMRVTF CPDKVEFLKS SLNIIDCVAI LPFYLEVGLS GLSSKAAKDV LGFLRVVRFV
     RILRIFKLTR HFVGLRVLGH TLRASTNEFL LLIIFLALGV LIFATMIYYA ERIGADPDDI
     LGSNHTYFKN IPIGFWWAVV TMTTLGYGDM YPKTWSGMLV GALCALAGVL TIAMPVPVIV
     NNFGMYYSLA MAKQKLPKKK NKHIPRPPQP GSPNYCKPDP PPPPPPHPHH GSGGISPPPP
     ITPPSMGVNV AGAYPPGPHT HPGLLRGGAG GLGIMGLPPL PAPGEPCPLA QEEVIETNRA
     DPRPNGDPAA AALAHEDCPA IDQPAMSPED KSPITPGSRG RYSRDRACFL VTDYAPSPDG
     SIRKALVTA
//
ID   D3YZX3_MOUSE            Unreviewed;       296 AA.
AC   D3YZX3;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 9.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Gnb2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC148018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00758356; -.
DR   Ensembl; ENSMUST00000031726; ENSMUSP00000031726; ENSMUSG00000029713.
DR   Ensembl; ENSMUST00000111020; ENSMUSP00000106649; ENSMUSG00000029713.
DR   Ensembl; ENSMUST00000111023; ENSMUSP00000106652; ENSMUSG00000029713.
DR   Ensembl; ENSMUST00000111027; ENSMUSP00000106656; ENSMUSG00000029713.
DR   MGI; MGI:95784; Gnb2.
DR   GeneTree; ENSGT00550000074331; -.
DR   Bgee; D3YZX3; -.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; TAS:MGI.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR001632; Gprotein_B.
DR   InterPro; IPR016346; Guanine_nucleotide-bd_bsu.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 7.
DR   PIRSF; PIRSF002394; GN-bd_beta; 1.
DR   PRINTS; PR00319; GPROTEINB.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 3.
DR   PROSITE; PS50082; WD_REPEATS_2; 6.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   4: Predicted;
KW   Repeat; WD repeat.
SQ   SEQUENCE   296 AA;  32409 MW;  D08283822FEECED4 CRC64;
     MRTRRTLRGH LAKIYAMHWG TDSRLLVSAS QDGKLIIWDS YTTNKVHAIP LRSSWVMTCA
     YAPSGNFVAC GGLDNICSIY SLKTREGNVR VSRELPGHTG YLSCCRFLDD NQIITSSGDT
     TCALWDIETG QQTVGFAGHS GDVMSLSLAP DGRTFVSGAC DASIKLWDVR DSMCRQTFIG
     HESDINAVAF FPNGYAFTTG SDDATCRLFD LRADQELLMY SHDNIICGIT SVAFSRSGRL
     LLAGYDDFNC NIWDAMKGDR AGVLAGHDNR VSCLGVTDDG MAVATGSWDS FLKIWN
//
ID   D3YZY0_MOUSE            Unreviewed;       270 AA.
AC   D3YZY0;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Actg2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells (By similarity).
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC090648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC090649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00885994; -.
DR   Ensembl; ENSMUST00000141904; ENSMUSP00000120936; ENSMUSG00000059430.
DR   MGI; MGI:104589; Actg2.
DR   Bgee; D3YZY0; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004000; Actin-like.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding.
SQ   SEQUENCE   270 AA;  30065 MW;  219B13CA0DEE4CAF CRC64;
     MCEEETTALV CDNGSGLCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
     SKRGILTLKY PIEHGIITNW DDMEKIWHHS FYNELRVAPE EHPTLLTEAP LNPKANREKM
     TQIMFETFNV PAMYVAIQAV LSLYASGRTT GIVLDSGDGV THNVPIYEGY ALPHAIMRLD
     LAGRDLTDYL MKILTERGYS FVTTAEREIV RDIKEKLCYV ALDFENEMAT AASSSSLEKS
     YELPDGQVIT IGNERFRCPE TLFQPSFIGE
//
ID   D3YZZ4_MOUSE            Unreviewed;       168 AA.
AC   D3YZZ4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 9.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Tsc22d4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC125063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00857501; -.
DR   Ensembl; ENSMUST00000110985; ENSMUSP00000106613; ENSMUSG00000029723.
DR   MGI; MGI:1926079; Tsc22d4.
DR   GeneTree; ENSGT00530000063062; -.
DR   Bgee; D3YZZ4; -.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   GO; GO:0006970; P:response to osmotic stress; IDA:MGI.
DR   InterPro; IPR000580; TSC-22_Dip_Bun.
DR   PANTHER; PTHR12348; TSC-22_Dip_Bun; 1.
DR   Pfam; PF01166; TSC22; 1.
DR   ProDom; PD007152; TSC-22_Dip_Bun; 1.
DR   PROSITE; PS01289; TSC22; 1.
PE   4: Predicted;
SQ   SEQUENCE   168 AA;  17578 MW;  676FC7A0741F2ED4 CRC64;
     MSQPGVSVKS LVSSYEMRVV GMAPGAPRKR GCVSSPCSPR GSSPIRGVSG PPAHQGLGGP
     GHRPSSHCGM DKSLLPLILY CHSGSGSLVG IDNKIEQAMD LVKSHLMFAV REEVEVLKEQ
     IRDLAERNAA LEQENGLLRA LASPEQLAQL PSSGLPRLGP SAPNGPSI
//
ID   D3Z080_MOUSE            Unreviewed;       707 AA.
AC   D3Z080;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 6.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Sorbs2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Contains 3 SH3 domains.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC113469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC116747; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC116861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC158351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00956780; -.
DR   ProteinModelPortal; D3Z080; -.
DR   Ensembl; ENSMUST00000037085; ENSMUSP00000040790; ENSMUSG00000031626.
DR   Ensembl; ENSMUST00000132139; ENSMUSP00000123250; ENSMUSG00000031626.
DR   MGI; MGI:1924574; Sorbs2.
DR   OrthoDB; EOG4J117C; -.
DR   Bgee; D3Z080; -.
DR   InterPro; IPR000108; p67phox.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR003127; Sorb.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   Pfam; PF02208; Sorb; 1.
DR   PRINTS; PR00499; P67PHOX.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 3.
DR   SMART; SM00459; Sorb; 1.
DR   SUPFAM; SSF50044; SH3; 3.
DR   PROSITE; PS50002; SH3; 3.
DR   PROSITE; PS50831; SOHO; 1.
PE   4: Predicted;
KW   SH3 domain.
SQ   SEQUENCE   707 AA;  78155 MW;  38DFBAB1E08635F7 CRC64;
     MNTDSGGCAR KRAAMSVTLT SVKRVQSSPN LLAAGRESQS PDSAKGFRSV RPNLQDKRSP
     TQSQITINGN SGGAVSPVSY YQRPFSPSAY SLPASLNSSI IMQHGRSLDS AETYSQHAQS
     LDGTMGSSIP LYRSSEEEKR VTVIKAPHYP GIGPVDESGI PTAIRTTVDR PKDWYKTMFK
     QIHMVHKPDE DTDMYNTPYT YNAGLYNSPY SAQSHPAAKT QTYRPLSKSH SDNGTDAFKE
     VPSPVPPPHV PPRPRDQSST LKHDWDPPDR KVDTRKFRSE PRSIFEYEPG KSSILQHERP
     PPLPPTPTPV PREPSRKPLS VSPSTDGLRS PSPPPRSCVP APRPSAPDLS PTRPPKKALD
     YVQDHSSGVS NEVSIYQSSI DRSLERPSSS ASMAGDFRKR RKSEPAVGPL RGLGDQSSSR
     TSPGRADLPG SSSTFTKSFI SSSPSSPSRA QDHESPRSYS STLTDLGRSA SRERRGTPEK
     EKLPAKAVYD FKAQTSKELS FKKGDTVYIL RKIDQNWYEG EHHGRVGIFP ISYVEKLTPP
     EKAQPARPPP PVQPGEIGEA IAKYNFNADT NVELSLRKGD RIILLKRVDQ NWYEGKIPGT
     NRQGIFPVSY VEVVKRNAKG AEDYPDPPLP HSYSSDRIYT LSSNKPQRPG FSHENIQGGG
     EPNEDELELR ESDVVDVMEK CDDGWFVGTS RRTKFFGTFP GNYVKRL
//
ID   D3Z095_MOUSE            Unreviewed;        60 AA.
AC   D3Z095;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 6.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Atxn7l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC132312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC132354; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC160112; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00918461; -.
DR   Ensembl; ENSMUST00000155386; ENSMUSP00000115463; ENSMUSG00000020564.
DR   MGI; MGI:3584458; Atxn7l1.
DR   GeneTree; ENSGT00530000063215; -.
DR   Bgee; D3Z095; -.
PE   4: Predicted;
SQ   SEQUENCE   60 AA;  6217 MW;  0756A5C435760C71 CRC64;
     MGTAAASERE RRHSSMCRPS PSPASPASNS RTSLAQAKTK ACLSGHSAVS STSKPFKTPK
//
ID   D3Z0L4_MOUSE            Unreviewed;       192 AA.
AC   D3Z0L4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Chchd3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC152943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC156288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00751223; -.
DR   Ensembl; ENSMUST00000127666; ENSMUSP00000123220; ENSMUSG00000053768.
DR   MGI; MGI:1913325; Chchd3.
DR   GeneTree; ENSGT00390000000903; -.
DR   Bgee; D3Z0L4; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   InterPro; IPR007964; DUF737.
DR   Pfam; PF05300; DUF737; 1.
PE   4: Predicted;
SQ   SEQUENCE   192 AA;  22452 MW;  6C00C82B59D07D27 CRC64;
     MGGTASTRRV TFEADENENI TVVKGIRLSE NVIDRMKESS PSGSKSQRYS SVYGASVSDE
     DLKRRVAEEL ALEQAKKESE HQRRLKQARD LERERAAANE QLTRAVLRER ISSEEERMKA
     KHLDIEDKAR QLEEKDRVMR KQDAFYKEQL ARLEERSSEF YKVTTEEYQK AAEEVEAKFK
     RYEYHPVCAD LQ
//
ID   D3Z0P2_MOUSE            Unreviewed;       218 AA.
AC   D3Z0P2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 6.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Tmem63b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC165259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00895360; -.
DR   Ensembl; ENSMUST00000133741; ENSMUSP00000115408; ENSMUSG00000036026.
DR   Ensembl; ENSMUST00000145873; ENSMUSP00000121681; ENSMUSG00000036026.
DR   MGI; MGI:2387609; Tmem63b.
DR   GeneTree; ENSGT00390000011855; -.
DR   Bgee; D3Z0P2; -.
PE   4: Predicted;
SQ   SEQUENCE   218 AA;  24273 MW;  9998BAA0F33602B7 CRC64;
     MLPFLLATLG TAALNSSNPK DYCYSARIRS TVLQGLPFGG VPTVLALDFM CFLALLFLFS
     ILRKVAWDYG RLALVTDADS VASAMHGDSH DRYERLTSVS SSVDFDQRDN GFCSWLTAIF
     RIKDDEIRDK CGGDAVHYLS FQRHIIGLLV VVGVLSVGIV LPVNFSGDLL ENNAYSFGRT
     TIANLKSGNN LLWLHTSFAF LYLLLTVYSM RRHTSKMR
//
ID   D3Z0P8_MOUSE            Unreviewed;       284 AA.
AC   D3Z0P8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 10.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Tmem200b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL607088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00678807; -.
DR   RefSeq; NP_001188296.1; NM_001201367.1.
DR   ProteinModelPortal; D3Z0P8; -.
DR   Ensembl; ENSMUST00000094666; ENSMUSP00000092253; ENSMUSG00000070720.
DR   GeneID; 623230; -.
DR   KEGG; mmu:623230; -.
DR   CTD; 623230; -.
DR   MGI; MGI:3646343; Tmem200b.
DR   GeneTree; ENSGT00530000063698; -.
DR   OrthoDB; EOG41JZD6; -.
DR   InterPro; IPR018787; DUF2371_TMEM200.
DR   Pfam; PF10177; DUF2371; 2.
PE   4: Predicted;
SQ   SEQUENCE   284 AA;  30336 MW;  1001BBDC2022B365 CRC64;
     MTAGSPGDGG ARRSPEGRVS RLGRRLGRRR RPRSPPEPLR VRARLRLRSP SGAFAALGAL
     VVLVGMGIAV AGYWPGRASH THAPRTGRAH GPHERLRLLG PVIMGVGLFV FICANTLLYE
     NRDLETRRLR RGMLRAQALR PPDGPGWDAL LPSPAHGSPG AVAEPETWDL APRRGPSPVP
     SVRSLRSEPA NPRSGLPALL HSYPLKGPGL PPPWGPRTQT GHVIITVQPS GSCIEHSKSL
     DLGLGELLLG APATRDCAHR SWPRLDRLSL GGYAKLGGDL GARV
//
ID   D3Z0Y4_MOUSE            Unreviewed;       346 AA.
AC   D3Z0Y4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 9.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Ablim2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC141898; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00857493; -.
DR   Ensembl; ENSMUST00000114203; ENSMUSP00000109841; ENSMUSG00000029095.
DR   MGI; MGI:2385758; Ablim2.
DR   GeneTree; ENSGT00570000079028; -.
DR   Bgee; D3Z0Y4; -.
DR   GO; GO:0030016; C:myofibril; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:MGI.
DR   InterPro; IPR003128; Villin_headpiece.
DR   Gene3D; G3DSA:1.10.950.10; VHP; 1.
DR   Pfam; PF02209; VHP; 1.
DR   SMART; SM00153; VHP; 1.
DR   SUPFAM; SSF47050; VHP; 1.
DR   PROSITE; PS51089; HP; 1.
PE   4: Predicted;
SQ   SEQUENCE   346 AA;  38975 MW;  F465ABFB1D8DBBAA CRC64;
     MFSEGEEMYL QGSSIWHPAC RQAARTEDKS KETRTSSESI VSVPASSTSG SPSRVIYAKL
     GDEILDYRDL AALPKNKAIY NIDRPDMISY SPYISHSAVG DRQSYGESPQ LLSPTPTEGD
     QDDRSYKQCR TSSPSSAGSV SLGHYTPTSR SPQHYSRPDT GVKDNIYRKP PIYKQHAARR
     LDVEDSSFDQ DSRKKTTWLL LKGDADTRTN SPDLDSQSLS LSSGTDQEPL QRMAGDSLYS
     RFPYSKPDTL PGPRKDGLDL RNANLAPCGA DPDASWGTRE YKIYPYDSLI VTNRIRVKLP
     KDVDRTRLER HLSPEEFQEV FGMSIEEFDR LALWKRNDLK KKALLF
//
ID   D3Z105_MOUSE            Unreviewed;        80 AA.
AC   D3Z105;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Hk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the hexokinase family.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC126428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC145297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00928549; -.
DR   Ensembl; ENSMUST00000143179; ENSMUSP00000120151; ENSMUSG00000037012.
DR   MGI; MGI:96103; Hk1.
DR   GeneTree; ENSGT00390000017159; -.
DR   Bgee; D3Z105; -.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004396; F:hexokinase activity; IDA:MGI.
DR   GO; GO:0006096; P:glycolysis; TAS:MGI.
DR   InterPro; IPR001312; Hexokinase.
DR   InterPro; IPR019807; Hexokinase_CS.
DR   InterPro; IPR022672; Hexokinase_N.
DR   PANTHER; PTHR19443; Hexokinase; 1.
DR   Pfam; PF00349; Hexokinase_1; 1.
DR   PROSITE; PS00378; HEXOKINASES; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Glycolysis; Kinase; Nucleotide-binding; Transferase.
SQ   SEQUENCE   80 AA;  8877 MW;  B8DBADD58E0F5FC7 CRC64;
     MDSEHCPSVP CGGAGAWEAR LFDHVAECLG DFMEKRKIKD KKLPVGFTFS FPCRQSKIDE
     AVLITWTKRF KASGVEGADV
//
ID   D3Z165_MOUSE            Unreviewed;      1000 AA.
AC   D3Z165;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Ccdc136;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC044807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00124212; -.
DR   Ensembl; ENSMUST00000115275; ENSMUSP00000110930; ENSMUSG00000029769.
DR   MGI; MGI:1918128; Ccdc136.
DR   GeneTree; ENSGT00530000063197; -.
DR   OrthoDB; EOG48PMJK; -.
DR   Bgee; D3Z165; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
PE   4: Predicted;
SQ   SEQUENCE   1000 AA;  115704 MW;  F7180879EAEEFE5B CRC64;
     MEAGGGAGAG AAGWSCPGPG PTVTTLGSYE VSEGCERKKG QRWGSLERRG MQAMDGEVLL
     PALYEEEEEE EEEEEEVEEE QVEKGGSLGS LSMGKHRGLS LTETELEELR AQVLQLVAEL
     EETRELAGQH EDDSLELQGL LEDERLASAQ QAEVFTKQIQ QLQGELQHLR EEISLLEHEK
     ESELKEMEQE LHLAQAEIQN LRQAAADSAT EHESDIASLQ DDLCRLQNDL DDMERIRGDY
     EMEIASLRAE MELKTSEPSN LSISDFSGIQ DELHHLRERY NLLNEEYQAL RESNSSLTGQ
     LAELESDRTR RATERWLESH LLRSTMSSES QTSELDFPEP DPVMQLLRQQ LLGAEEQMQD
     MQDKCKNLYC ELEELQHHRR TSEEEQKRLQ RELKCAQNEV LRFQTSHSTQ HEELKSRLCT
     LQQKYDASQD EHSELLKVQM QLETELQQLR LLRCTPVESQ SEKELMCRLQ KLQAQHQCSV
     NEKEQLLEVQ HHLHDKLRCH ESEVHRLRSM VDCLREKNEK NSGIHLQLQE MKGLYQFSRD
     ELERQKHMYD QLEQDFLLCQ QELTELKSSQ SLCEENGNCS NKCDALLARL TELQDKFKAS
     QEEIGHLQME QCELLEDQRR LQEEQGQLQE ELHRLTFPQP KCGILQKSQE LLSKLQDLCE
     MQLLYQNMQE QQRKLTQNQE CVLKEQLEAH KHLRGFKESH FQEVLANPQD ARGPKSSSCE
     NKFKVLMDQL QALQVLYDTS QKQQEVLQRE HGRLMEERKR LQAELQLCME EMQVLQTQSP
     MIKRSFEYCG KNSGSRAPST ENFHRSYESS IDENEGYQKS YVSSQPSTET FLKSYDSSTS
     ANEAFEKSYC SSSTSVSYKK SYGSVSSGET LHRSYASSST DEDPAEPEDL EHFEETVAKV
     LTKLQAVKAL YQVSQEEHCQ LQQRMHRLLA KQKELTEELQ CCEKELRECM ESLGKPLPPQ
     SDKCENMFGM WKPMVFLAIA AVALYVLPNM RPQESEYYMK
//
ID   D3Z183_MOUSE            Unreviewed;       794 AA.
AC   D3Z183;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 10.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Mfsd6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC139299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC161876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00262303; -.
DR   RefSeq; NP_598590.2; NM_133829.2.
DR   UniGene; Mm.269793; -.
DR   ProteinModelPortal; D3Z183; -.
DR   Ensembl; ENSMUST00000156876; ENSMUSP00000122881; ENSMUSG00000041439.
DR   GeneID; 98682; -.
DR   KEGG; mmu:98682; -.
DR   CTD; 98682; -.
DR   MGI; MGI:1922925; Mfsd6.
DR   GeneTree; ENSGT00530000063599; -.
DR   Bgee; D3Z183; -.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR011701; MFS_1.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   Pfam; PF07690; MFS_1; 2.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
PE   4: Predicted;
SQ   SEQUENCE   794 AA;  87828 MW;  D88B7D543EAF61DE CRC64;
     MAADDKVAIL TDDEEEQKRK YVLADPFNGI CREPEPPSNE TPSSTETSAI PEEEIDWIEK
     HCVKVNNDLL ISKVFYFFFY SAYGSLYPLL PVYYKQLGMS PSQSGLLVGI RYFIEFCSAP
     FWGVVADRFR KGKIVLLFSL LCWVLFNLGI GFVKPATLRC LPKIPPTAHP TNVSHPVTVL
     PMNSSTVAFF STPPKLLQKR DVQLSETEPN ISDIDLVSTA LTLTSEPTRR PQTEAITHPV
     TGLILNTSTV TLPPTGNVTR ETTIAVVTTT KSLPSDQVTL VYDQQEVEAI FLIILVVVII
     GEFFSASSVT IVDTVTLQYL GKHRDRYGLQ RMWGSLGWGL AMLSVGIGID YTHIDVLIDG
     KGCKPPEYRN YQIVFIVFGV LMTMALIVAT QFRFRYNHFN NSDGKGKEVE IPQVERDNST
     ESSEETPTAA THSQAFNFWD LIKLLCSVQY GSVLFVAWFM GFGYGFVFTF LYWHLEDLNG
     TTTLFGVCSV LSHVSELTAY FFSHKLIELI GHIRVLYIGL ACNTARYIYI SYLENAWTVL
     PMEVLQGVTH AAIWAACISY LSAAVPPELR TSAQGILQGL HLGLGRGCGA MIGGVLVNYF
     GAAATFRGIG MACLVILLLF ALIQWLAVPD EEEDKTMLAE RIPVPSSPVP IATIDLVQQQ
     TEDVMPRVEA RLPPKKTKHQ EEQEDVNKPA WGVSSSPWVT FVYALYQVKE LIQLTRESRA
     SEIQPLQGTS ENREASPAGG AQRAPRETHS ASPRNQPSPD TAASQTQSSP AHPSATPHGQ
     ESGEKQAQPT VGEH
//
ID   D3Z1D7_MOUSE            Unreviewed;       455 AA.
AC   D3Z1D7;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 9.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Gprin2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC154738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00750996; -.
DR   RefSeq; NP_899032.2; NM_183209.2.
DR   UniGene; Mm.294643; -.
DR   ProteinModelPortal; D3Z1D7; -.
DR   Ensembl; ENSMUST00000096019; ENSMUSP00000093718; ENSMUSG00000071531.
DR   GeneID; 432839; -.
DR   KEGG; mmu:432839; -.
DR   CTD; 432839; -.
DR   MGI; MGI:2444560; Gprin2.
DR   GeneTree; ENSGT00570000079168; -.
DR   OrthoDB; EOG4BZN2Q; -.
PE   4: Predicted;
SQ   SEQUENCE   455 AA;  46997 MW;  DD70046FFB5C2955 CRC64;
     MSSSHPEPGA REPQSPRPQA LSQSSSSLLC EGREQKPELR KSASSTVWRA QQGEAGSSPR
     ILQEEACQTE IPEHAQTAST ASQAGAGGHW RSSTVGNVST MGIGDLCRLR APSVAAVQRS
     HSDLVHSTQT RGHGGVQKPS LSCSALGSSP VHRAQLQPGS VAGQGGQTPA PLQSDSAPED
     GTSKSACTLG ESQVWVPTVE LEDATGLLRG PQGEPKATGQ PPTTSCHALP PAALLCTLGE
     AVAGSCCHAL PARGILAFPK LVASVSESGL QAQCGMKFHC KLSGGISGHP HCCVHPWGPT
     GLATESGSRT KDVWTMTSAT DLALGVASAQ DAGVQAAPAA ACKAVATSPS LEAPETLNLF
     PEVMLESGLR QASSPVRDVR WDAEGMTWEV YGASVDPEVL GIAIQKHLEM QFEQLQQAPA
     SEDSLSAEGR RGPLRAVMQS LRRPSCCGCS GAAPE
//
ID   D3Z1M1_MOUSE            Unreviewed;       227 AA.
AC   D3Z1M1;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Gnb2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC148018; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00756766; -.
DR   Ensembl; ENSMUST00000031726; ENSMUSP00000031726; ENSMUSG00000029713.
DR   Ensembl; ENSMUST00000111027; ENSMUSP00000106656; ENSMUSG00000029713.
DR   Ensembl; ENSMUST00000132525; ENSMUSP00000119725; ENSMUSG00000029713.
DR   MGI; MGI:95784; Gnb2.
DR   Bgee; D3Z1M1; -.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; TAS:MGI.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR001632; Gprotein_B.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 4.
DR   PRINTS; PR00319; GPROTEINB.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   4: Predicted;
KW   Repeat; WD repeat.
SQ   SEQUENCE   227 AA;  25025 MW;  6FACB13F74BC22FA CRC64;
     MSELEQLRQE AEQLRNQIRD ARKACGDSTL TQITAGLDPV GRIQMRTRRT LRGHLAKIYA
     MHWGTDSRLL VSASQDGKLI IWDSYTTNKV HAIPLRSSWV MTCAYAPSGN FVACGGLDNI
     CSIYSLKTRE GNVRVSRELP GHTGYLSCCR FLDDNQIITS SGDTTCALWD IETGQQTVGF
     AGHSGDVMSL SLAPDGRTFV SGACDASIKL WDVRDSMCRQ TFIGHES
//
ID   D3Z1M4_MOUSE            Unreviewed;       350 AA.
AC   D3Z1M4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Cabp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC119205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC145070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00750955; -.
DR   Ensembl; ENSMUST00000112113; ENSMUSP00000107741; ENSMUSG00000029544.
DR   MGI; MGI:1352750; Cabp1.
DR   GeneTree; ENSGT00590000082834; -.
DR   Bgee; D3Z1M4; -.
DR   InterPro; IPR015754; Ca_binding_pro.
DR   InterPro; IPR018248; EF-hand.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   PANTHER; PTHR23050:SF21; Ca_binding_pro; 1.
DR   Pfam; PF00036; efhand; 3.
DR   SMART; SM00054; EFh; 3.
DR   PROSITE; PS00018; EF_HAND_1; 3.
DR   PROSITE; PS50222; EF_HAND_2; 4.
PE   4: Predicted;
KW   Calcium.
SQ   SEQUENCE   350 AA;  37917 MW;  5C7940BF8D3DD1A9 CRC64;
     MGGGDGAAFK RPGDGARLQR VLGLGSRRAP RSLPSGGPAP PPPGHASAGP AAMSSHIAKS
     ESKTSLLKAA AASGGSRAPR HSSARDPGLR GRRLPGPCPG SPPPCGDPSS RRPLCRPVPR
     DEGARGSRRG LPQAHCRPRE TLPPARGRDG EERGLAPALG LRGSLRSRGR GDPAPAGTPE
     ADPFLHRLRP MLSSAFGQDR SLRPEEIEEL REAFREFDKD KDGYINCRDL GNCMRTMGYM
     PTEMELIELS QQINMNLGGH VDFDDFVELM GPKLLAETAD MIGVKELRDA FREFDTNGDG
     EISTSELREA MRKLLGHQVG HRDIEEIIRD VDLNGDGRVD FEEFVRMMSR
//
ID   D3Z1W3_MOUSE            Unreviewed;       443 AA.
AC   D3Z1W3;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 9.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Nrg1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC127374; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC132407; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC136147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00875804; -.
DR   Ensembl; ENSMUST00000098838; ENSMUSP00000096437; ENSMUSG00000062991.
DR   MGI; MGI:96083; Nrg1.
DR   GeneTree; ENSGT00390000017243; -.
DR   Bgee; D3Z1W3; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005887; C:integral to plasma membrane; IDA:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0005176; F:ErbB-2 class receptor binding; IDA:MGI.
DR   GO; GO:0003161; P:cardiac conduction system development; IDA:MGI.
DR   GO; GO:0016477; P:cell migration; IGI:MGI.
DR   GO; GO:0000902; P:cell morphogenesis; IDA:MGI.
DR   GO; GO:0009790; P:embryo development; IEA:InterPro.
DR   GO; GO:0010001; P:glial cell differentiation; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0000165; P:MAPKKK cascade; IDA:MGI.
DR   GO; GO:0007517; P:muscle organ development; IMP:MGI.
DR   GO; GO:0048663; P:neuron fate commitment; IMP:MGI.
DR   GO; GO:0045213; P:neurotransmitter receptor metabolic process; IMP:MGI.
DR   GO; GO:0007422; P:peripheral nervous system development; IMP:MGI.
DR   GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:MGI.
DR   GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IDA:MGI.
DR   GO; GO:0045595; P:regulation of cell differentiation; IMP:MGI.
DR   GO; GO:0007416; P:synapse assembly; IMP:MGI.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR018250; Neuregulin.
DR   InterPro; IPR002154; Neuregulin_1_C.
DR   Pfam; PF02158; Neuregulin; 1.
DR   PRINTS; PR01089; NEUREGULIN.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   4: Predicted;
SQ   SEQUENCE   443 AA;  49365 MW;  D61D5E1C67336533 CRC64;
     MVKDLSNPSR YLCKCQPGFT GARCTENVPM KVQTQEKAEE LYQKRVLTIT GICIALLVVG
     IMCVVAYCKT KKQRQKLHDR LRQSLRSERN NMVNIANGPH HPNPPPENVQ LVNQYVSKNV
     ISSEHIVERE VETSFSTSHY TSTAHHSTTV TQTPSHSWSN GHTESIISES HSVIMMSSVE
     NSRHSSPAGG PRGRLHGLGG PRECNSFLRH ARETPDSYRD SPHSERYVSA MTTPARMSPV
     DFHTPSSPKS PPSEMSPPVS SMTVSMPSVA VSPFVEEERP LLLVTPPRLR EKKYDHHPQQ
     LNSFHHNPAH QSTSLPPSPL RIVEDEEYET TQEYEPIQEP IKKVTNSRRA KRTKPNGHIA
     NRLEMDSNPS SVSSNSESET EDERVGEDTP FLGIQNPLAA SLEVAPAFRL AESRTNPAGR
     FSTQEELQAR LSSVIANQDP IAV
//
ID   D3Z1Y7_MOUSE            Unreviewed;       184 AA.
AC   D3Z1Y7;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Zbtb38;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC121951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00928060; -.
DR   Ensembl; ENSMUST00000093798; ENSMUSP00000091315; ENSMUSG00000040433.
DR   Ensembl; ENSMUST00000126066; ENSMUSP00000114300; ENSMUSG00000040433.
DR   Ensembl; ENSMUST00000128269; ENSMUSP00000121871; ENSMUSG00000040433.
DR   Ensembl; ENSMUST00000140121; ENSMUSP00000120040; ENSMUSG00000040433.
DR   Ensembl; ENSMUST00000152594; ENSMUSP00000121753; ENSMUSG00000040433.
DR   MGI; MGI:2442866; Zbtb38.
DR   GeneTree; ENSGT00530000063209; -.
DR   Bgee; D3Z1Y7; -.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR013069; BTB_POZ.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF00651; BTB; 1.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   4: Predicted;
SQ   SEQUENCE   184 AA;  20675 MW;  CEBE7A16D42F6AE4 CRC64;
     MTVMSLSRDL KDDFHSDTVL SILNEQRIRG ILCDVTIIVE DTKFKAHSNV LAASSLYFKN
     IFWSHTICIS SHVLELDDLK AEVFTEILNY IYSSTVVVKR QETVTDLAAA GKKLGISFLE
     DLSDRNFSNS PGPYVVCITE KGVVKEEKNE KRHEEPAVTN GPRITNAFSI IETENSNNMF
     SPLD
//
ID   D3Z2R5_MOUSE            Unreviewed;       557 AA.
AC   D3Z2R5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 6.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Sepn1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL669982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00624792; -.
DR   Ensembl; ENSMUST00000060435; ENSMUSP00000060026; ENSMUSG00000050989.
DR   MGI; MGI:2151208; Sepn1.
DR   GeneTree; ENSGT00390000005972; -.
DR   OrthoDB; EOG4QZ7KP; -.
DR   Bgee; D3Z2R5; -.
DR   InterPro; IPR018249; EF_HAND_2.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   4: Predicted;
SQ   SEQUENCE   557 AA;  62445 MW;  3E88FC97C3DE8249 CRC64;
     MGQARPAARR PHSPDPGAQP APPRRRARAL ALLGALLAAA AAVAAARACA LLADAQAAAR
     QESALKVLGT DGLFLFSSLD TDQDMYISPE EFKPIAEKLT GSVPVANYEE EELPHDPSEE
     TLTIEARFQP LLMETMTKSK DGFLGVSRLA LSGLRNWTTA ASPSAAFAAR HFRPFLPPPG
     QELGQPWWII PGELSVFTGY LSNNRFYPPP PKGKEVIIHR LLSMFHPRPF VKTRFAPQGT
     VACLTAISDS YYTVMFRIHA EFQLSEPPDF PFWFSPGQFT GHIILSKDAT HIRDFRLFVP
     NHRSLNVDME WLYGASETSN MEVDIGYVPQ MELEAVGPSV PSVILDEDGN MIDSRLPSGE
     PLQFVFEEIK WHQELSWEEA ARRLEVAMYP FKKVNYLPFT EAFDRARAEK KLVHSILLWG
     ALDDQSCCGS GRTLRETVLE SPPILTLLNE SFISTWSLVK ELEDLQTQQE NPLHRQLAGL
     HLEKYSFPVE MMICLPNGTV VHHINANYFL DITSMKPEDM ENNNVFSFSS SFEDPSTATY
     MQFLREGLRR GLPLLQP
//
ID   D3Z2S4_MOUSE            Unreviewed;       162 AA.
AC   D3Z2S4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   RecName: Full=Enolase;
DE            EC=4.2.1.11;
GN   Name=Eno2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate +
CC       H(2)O.
CC   -!- COFACTOR: Magnesium. Required for catalysis and for stabilizing
CC       the dimer (By similarity).
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5.
CC   -!- SIMILARITY: Belongs to the enolase family.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC164157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00830694; -.
DR   ProteinModelPortal; D3Z2S4; -.
DR   Ensembl; ENSMUST00000004378; ENSMUSP00000004378; ENSMUSG00000004267.
DR   Ensembl; ENSMUST00000149652; ENSMUSP00000119112; ENSMUSG00000004267.
DR   MGI; MGI:95394; Eno2.
DR   GeneTree; ENSGT00550000074560; -.
DR   Bgee; D3Z2S4; -.
DR   GO; GO:0043204; C:perikaryon; IDA:MGI.
DR   GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR   GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:EC.
DR   InterPro; IPR000941; Enolase.
DR   InterPro; IPR020810; Enolase_C.
DR   InterPro; IPR020811; Enolase_N.
DR   Pfam; PF00113; Enolase_C; 1.
DR   Pfam; PF03952; Enolase_N; 1.
DR   PRINTS; PR00148; ENOLASE.
PE   3: Inferred from homology;
KW   Glycolysis; Lyase; Magnesium.
SQ   SEQUENCE   162 AA;  17239 MW;  FF04C56C9986DD0A CRC64;
     MSIEKIWARE ILDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR DGDKQRYLGK
     GVLKAVDHIN SRIAPALISS GISVVEQEKL DNLMLELDGT ENKSKFGANA ILGVSLAVCK
     AGAAERDLPL YRHIAQLAGN SDLILPVPAF NVINGGSHAG NK
//
ID   D3Z2V9_MOUSE            Unreviewed;       489 AA.
AC   D3Z2V9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 10.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Camk2a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC124431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00420725; -.
DR   Ensembl; ENSMUST00000025519; ENSMUSP00000025519; ENSMUSG00000024617.
DR   MGI; MGI:88256; Camk2a.
DR   GeneTree; ENSGT00550000074354; -.
DR   Bgee; D3Z2V9; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:InterPro.
DR   GO; GO:0035254; F:glutamate receptor binding; IPI:MGI.
DR   GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; IMP:MGI.
DR   GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:MGI.
DR   GO; GO:0046928; P:regulation of neurotransmitter secretion; IMP:MGI.
DR   InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF08332; CaMKII_AD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding; Nucleotide-binding.
SQ   SEQUENCE   489 AA;  55347 MW;  ABFEC3059FC8C91D CRC64;
     MATITCTRFT EEYQLFEELG KGAFSVVRRC VKVLAGQEYA AKIINTKKLS ARDHQKLERE
     ARICRLLKHP NIVRLHDSIS EEGHHYLIFD LVTGGELFED IVAREYYSEA DASHCIQQIL
     EAVLHCHQMG VVHRDLKPEN LLLASKLKGA AVKLADFGLA IEVEGEQQAW FGFAGTPGYL
     SPEVLRKDPY GKPVDLWACG VILYILLVGY PPFWDEDQHR LYQQIKAGAY DFPSPEWDTV
     TPEAKDLINK MLTINPSKRI TAAEALKHPW ISHRSTVASC MHRQETVDCL KKFNARRKLK
     GAILTTMLAT RNFSGGKSGG NKKNDGVKKR KSSSSVQLME SSESTNTTIE DEDTKVRKQE
     IIKVTEQLIE AISNGDFESY TKMCDPGMTA FEPEALGNLV EGLDFHRFYF ENLWSRNSKP
     VHTTILNPHI HLMGDESACI AYIRITQYLD AGGIPRTAQS EETRVWHRRD GKWQIVHFHR
     SGAPSVLPH
//
ID   D3Z2W1_MOUSE            Unreviewed;      1050 AA.
AC   D3Z2W1;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 9.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Dgki;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC114574; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC159480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC184160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC185507; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00751738; -.
DR   Ensembl; ENSMUST00000090314; ENSMUSP00000087788; ENSMUSG00000038665.
DR   MGI; MGI:2443430; Dgki.
DR   GeneTree; ENSGT00600000084185; -.
DR   Bgee; D3Z2W1; -.
DR   GO; GO:0032045; C:guanyl-nucleotide exchange factor complex; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR   GO; GO:0004143; F:diacylglycerol kinase activity; IDA:MGI.
DR   GO; GO:0005095; F:GTPase inhibitor activity; IDA:MGI.
DR   GO; GO:0017016; F:Ras GTPase binding; IPI:MGI.
DR   GO; GO:0007205; P:activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway; IEA:InterPro.
DR   GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IMP:MGI.
DR   GO; GO:0032317; P:regulation of Rap GTPase activity; IMP:MGI.
DR   GO; GO:0051789; P:response to protein stimulus; IMP:MGI.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00609; DAGK_acc; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00045; DAGKa; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50146; DAGK; 1.
PE   4: Predicted;
KW   ANK repeat; Repeat.
SQ   SEQUENCE   1050 AA;  115963 MW;  629C08C4362CE129 CRC64;
     MDAAGRGCHL LPLPAARGPA RAPAASSALS PTGLCSGTTS ASFAAAGAVA MNPSSSAGEE
     RGATGGSSSS GSGAGSCCLG AEGGADPRGA GAAAAAALEE PAAAGQKEKE EALEEKLRDL
     TFRKQVSYRK AISRTGLQHL APAHPLGLPV ANGPAKEPRA TLDWSENAVN GEHLWLETNV
     SGDLCYLGEE NCQVRFAKSA LRRKCAVCKI VVHTACIEQL EKINFRCKPT FREGGSRSPR
     ENFVRHHWVH RRRQEGKCKQ CGKGFQQKFS FHSKEIVAIS CSWCKQAFHN KVTCFMLHHI
     EEPCSLGAHA AVIVPPTWII KVKKPQNSLK ASNRKKKRTS FKRKASKRGT EQETKGRPFV
     IKPISSPLMK PLLVFVNPKS GGNQGTKVLQ MFMWYLNPRQ VFDLSQEGPK DALEMYRKVP
     NLRILACGGD GTVGWILSIL DELQLSPQPP VGVLPLGTGN DLARTLNWGG GYTDEPVSKI
     LCQVEDGTIV QLDRWNLHVE RNPDLPPEEL EDGVCKLPLN VFNNYFSLGF DAHVTLEFHE
     SREANPEKFN SRFRNKMFYA GAAFSDFLQR SSRDLSKHVK VVCDGTDLTP KIQDLKFQCI
     VFLNIPRYCA GTMPWGNPGD HHDFEPQRHD DGYIEVIGFT MASLAALQVG GHGERLHQCR
     EVMLLTYKSI PMQVDGEPCR LAPAMIRISL RNQANMVQKS KRRTSMPLLN DPQSVPDRLR
     IRVNKISLQD YEGLHYDKDK LREASIPLGI LVVRGDCDLE TCRMYIDRLQ EDLQSVSSGS
     QRVHYQDQET SFPRALSAQR LSPRWCFLDA TSADRFYRID RSQEHLHFVM EISHDEIFIL
     DPDMVVSQQA GTPPGMPDLV VEQASGLSDW WNPALRKRML SDSGMITPHY EDSDLKDFSH
     SRVLQSPVSS EDHAILQAVL TGDLMKLMES YKNGGSLLIQ GPGHCSLLHY AAKTGNGDIV
     KYILDHGPAE LLDMADSETG ETALHKAACQ RNRAVCQLLV DAGASLRQTD SKGKTPQERA
     QQAGDPDLAA YLESRQNYKI IGHEDLETAV
//
ID   D3Z384_MOUSE            Unreviewed;       819 AA.
AC   D3Z384;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Efr3a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC091276; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00874856; -.
DR   Ensembl; ENSMUST00000110107; ENSMUSP00000105734; ENSMUSG00000015002.
DR   MGI; MGI:1923990; Efr3a.
DR   GeneTree; ENSGT00390000002143; -.
DR   Bgee; D3Z384; -.
DR   GO; GO:0005622; C:intracellular; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 2.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
PE   4: Predicted;
SQ   SEQUENCE   819 AA;  92599 MW;  35C09BE5B1B5737D CRC64;
     MPSRVCCCCS ALRPRYKRLV DNIFPEDPKD GLVKADMEKL TFYAVSAPEK LDRIGAYLAE
     RLSRDVVRHR SGYVLIAMEA LDQLLMACHS QSIKPFVESF LHMVAKLLES GEPKLQVLGT
     NSFVKFANIE EDTPSYHRRY DFFVSRFSAM CHSCHSDPEI RTEIRIAGIR GIQGVVRKTV
     NDELRATIWE PQHMDKIVPS LLFNMQKIEE VDSRLGPPSS PSAADKEENP AVLAESCFRE
     LLGRATFGNM NNAVRPVFAH LDHHKLWDPN EFAVHCFKII MYSIQAQYSH HVIQEILGHL
     DARRKDSPRV RAGIIQVLLE AVAIAAKGSI GPTVLEVFNT LLKHLRLSVE LEANDSQKGS
     VGSVTVSSKD NDEKIVQNAV IQTIGFFGSN LPDYQRSEIM MFIMGKVPVF GTSTHTLDIS
     QLGDLGTRRI QIMLLRSLLM VTSGYKAKTI VTALPGSFLD PLLSPSLMED YELRQLVLEV
     MHNLMDRHDN RAKLRGIRII PDVADLKIKR EKICRQDTSF MKKNGQQLYR HIYLGCKEED
     NVQKNYELLY TSLALITIEL ANEEVVIDLI RLAIALQDSA IINEDNLSMF HRCGIMALVA
     AYLNFVSQMI AVPAFCQHVS KVIETRTMEA PYFLPEHIFR DKCMLPKSLE KHDKNLYFLT
     NKIAESLGGS GYSVERLTVP YVPQVTDEDR LSRRKSIVDT VSIQVDILSN SVPSDDVVSN
     TEEITFEALK KAIDTNGMEE QEKEKRRLVI EKFQKAPFEE IAAQCESKAN LLHDRLAQIL
     ELTIRPPPSP SGTLTVTSGH TQYQSVPVYE MKFPDLCVY
//
ID   D3Z395_MOUSE            Unreviewed;       369 AA.
AC   D3Z395;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Sept6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Belongs to the septin family.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL450399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00473707; -.
DR   Ensembl; ENSMUST00000053456; ENSMUSP00000054034; ENSMUSG00000050379.
DR   Ensembl; ENSMUST00000060474; ENSMUSP00000062014; ENSMUSG00000050379.
DR   Ensembl; ENSMUST00000115239; ENSMUSP00000110894; ENSMUSG00000050379.
DR   Ensembl; ENSMUST00000115240; ENSMUSP00000110895; ENSMUSG00000050379.
DR   Ensembl; ENSMUST00000115241; ENSMUSP00000110896; ENSMUSG00000050379.
DR   MGI; MGI:1888939; Sept6.
DR   GeneTree; ENSGT00590000082767; -.
DR   Bgee; D3Z395; -.
DR   GO; GO:0031105; C:septin complex; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:InterPro.
DR   InterPro; IPR000038; Cell_Div_GTP-bd.
DR   InterPro; IPR016491; Septin.
DR   PANTHER; PTHR18884; Cell_Div_GTP_bd; 1.
DR   Pfam; PF00735; Septin; 1.
DR   PIRSF; PIRSF006698; Septin; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Nucleotide-binding.
SQ   SEQUENCE   369 AA;  42744 MW;  F56BFE2B0B260C80 CRC64;
     MDTLFNTKFE GEPATHTQPG VQLQSNTYDL QESNVGLKLT IVSTVGFGDQ INKEDSYKPI
     VEFIDAQFEA YLQEELKIRR VLHSYHDSRI HVCLYFIAPT GHSLKSLDLV TMKKLDSKVN
     IIPVIAKSDA ISKSELAKFK IKITSELVSN GVQIYQFPTD DESVSEINGT MNAHLPFAVV
     GSTEEVKIGN KMMRARQYPW GTVQVENEAH CDFVKLREML IRVNMEDLRE QTHARHYELY
     RRCKLEEMGF KDTDPDSKPF SLQETYEAKR NEFLGELQKK EEEMRQMFVQ RVKEKEAELK
     EAEKELHEKF DRLKKLHQEE KKKLEDKKKC LDEEMNAFKQ RKAAAELLQS QGSQAGGSQT
     LKRDKEKKN
//
ID   D3Z3B8_MOUSE            Unreviewed;       834 AA.
AC   D3Z3B8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 11.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Dlg1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC   -!- SIMILARITY: Contains 3 PDZ (DHR) domains.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC126055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC129214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00672505; -.
DR   Ensembl; ENSMUST00000115196; ENSMUSP00000110850; ENSMUSG00000022770.
DR   MGI; MGI:107231; Dlg1.
DR   GeneTree; ENSGT00560000076879; -.
DR   Bgee; D3Z3B8; -.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0031253; C:cell projection membrane; IDA:MGI.
DR   GO; GO:0001772; C:immunological synapse; IDA:MGI.
DR   GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR   GO; GO:0045121; C:membrane raft; IDA:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0032947; F:protein complex scaffold; IMP:MGI.
DR   GO; GO:0032147; P:activation of protein kinase activity; IMP:MGI.
DR   GO; GO:0042982; P:amyloid precursor protein metabolic process; IGI:MGI.
DR   GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI.
DR   GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
DR   GO; GO:0060022; P:hard palate development; IMP:MGI.
DR   GO; GO:0001771; P:immunological synapse formation; IMP:MGI.
DR   GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI.
DR   GO; GO:0031579; P:membrane raft organization; IMP:MGI.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
DR   GO; GO:0042130; P:negative regulation of T cell proliferation; IMP:MGI.
DR   GO; GO:0030432; P:peristalsis; IMP:MGI.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0008104; P:protein localization; IMP:MGI.
DR   GO; GO:0042391; P:regulation of membrane potential; IGI:MGI.
DR   GO; GO:0048608; P:reproductive structure development; IMP:MGI.
DR   GO; GO:0048745; P:smooth muscle tissue development; IMP:MGI.
DR   GO; GO:0042110; P:T cell activation; IMP:MGI.
DR   GO; GO:0002369; P:T cell cytokine production; IMP:MGI.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR016313; M-assoc_guanylate_kinase.
DR   InterPro; IPR019590; MAGUK_PEST_N.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR019583; PDZ_assoc.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF10608; MAGUK_N_PEST; 1.
DR   Pfam; PF00595; PDZ; 3.
DR   Pfam; PF10600; PDZ_assoc; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   PIRSF; PIRSF001741; MAGUK_DLGH; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 3.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50156; PDZ; 3.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 3.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
SQ   SEQUENCE   834 AA;  91623 MW;  553E1EAF25E9FEC0 CRC64;
     MNYIFGNNTL LYSRASRGGN ASSSHGSVGP KQKHWAKKGS SDELQAEPEP SRWQQIVAFF
     TRRHSFIDCI SVATSSTQPT EAVPPSSPIV PVTPALPVPA ESTVVLPSAP QANPPPVLVN
     TDSLETPTYV NGTDADYEYE EITLERGNSG LGFSIAGGTD NPHIGDDSSI FITKIITGGA
     AAQDGRLRVN DCILRVNEAD VRDVTHSKAV EALKEAGSIV RLYVKRRKPA SEKIMEIKLI
     KGPKGLGFSI AGGVGNQHIP GDNSIYVTKI IEGGAAHKDG KLQIGDKLLA VNSVCLEEVT
     HEEAVTALKN TSDFVYLKVA KPTSMYINDG YAPPDITNSS SQSVDNHVSP SSCLGQTPTS
     PARYSPISKA VLGDDEITRE PRKVVLHRGS TGLGFNIVGG EDGEGIFISF ILAGGPADLS
     GELRKGDRII SVNSVDLRAA SHEQAAAALK NAGQAVTIVA QYRPEEYSRF EAKIHDLREQ
     MMNSSVSSGS GSLRTSQKRS LYVRALFDYD KTKDSGLPSQ GLNFRFGDIL HVINASDDEW
     WQARQVTPDG ESDEVGVIPS KRRVEKKERA RLKTVKFNSK TRGDKGEIPD DMGSKGLKHV
     TSNASDSESS YLILITDEYG CSKGGQEEYV LSYEPVNQQE VNYTRPVIIL GPMKDRVNDD
     LISEFPDKFG SCVPHTTRPK RDYEVDGRDY HFVTSREQME KDIQEHKFIE AGQYNNHLYG
     TSVQSVRAVA EKGKHCILDV SGNAIKRLQI AQLYPISIFI KPKSMENIME MNKRLTEEQA
     RKTFERAMKL EQEFTEHFTA IVQGDTLEDI YNQVKQIIEE QSGPYIWVPA KEKL
//
ID   D3Z3G6_MOUSE            Unreviewed;       380 AA.
AC   D3Z3G6;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 10.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Mapk3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC124505; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00750828; -.
DR   Ensembl; ENSMUST00000050201; ENSMUSP00000101969; ENSMUSG00000063065.
DR   MGI; MGI:1346859; Mapk3.
DR   GeneTree; ENSGT00550000074298; -.
DR   Bgee; D3Z3G6; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004707; F:MAP kinase activity; IDA:MGI.
DR   GO; GO:0001784; F:phosphotyrosine binding; IMP:MGI.
DR   GO; GO:0051216; P:cartilage development; IDA:MGI.
DR   GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:MGI.
DR   GO; GO:0009887; P:organ morphogenesis; IDA:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR   GO; GO:0006974; P:response to DNA damage stimulus; IDA:MGI.
DR   GO; GO:0043330; P:response to exogenous dsRNA; IDA:MGI.
DR   InterPro; IPR008349; Erk_1_2_MAPK.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR003527; MAP_kinase_CS.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01770; ERK1ERK2MAPK.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS01351; MAPK; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding; Kinase; Nucleotide-binding;
KW   Serine/threonine-protein kinase; Transferase.
SQ   SEQUENCE   380 AA;  42402 MW;  316AF49A2657007B CRC64;
     MAAAAAAPGG GGGEPRGTAG VVPVVPGEVE VVKGQPFDVG PRYTQLQYIG EGAYGMVSSA
     YDHVRKTRVA IKKISPFEHQ TYCQRTLREI QILLRFRHEN VIGIRDILRA PTLEAMRDVY
     IVQDLMETDL YKLLKSQQLS NDHICYFLYQ ILRGLKYIHS ANVLHRDLKP SNLLINTTCD
     LKICDFGLAR IADPEHDHTG FLTEYVATRW YRAPEIMLNS KGYTKSIDIW SVGCILAEML
     SNRPIFPGKH YLDQLNHILG ILGSPSQEDL NCIINMKARN YLQSLPSKTK VAWAKLFPKS
     DSKALDLLDR MLTFNPNKRI TVEEALAHPY LEQYYDPTDE VSRSPAAGRG ASIPSAQPGP
     HRLCPLASGR GAIHLRHGAG
//
ID   D3Z3N9_MOUSE            Unreviewed;       682 AA.
AC   D3Z3N9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 6.
DE   SubName: Full=Uncharacterized protein;
GN   Name=9430031J16Rik;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC116105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC131336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC163450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00956773; -.
DR   Ensembl; ENSMUST00000123720; ENSMUSP00000117661; ENSMUSG00000054976.
DR   MGI; MGI:2443135; 9430031J16Rik.
DR   GeneTree; ENSGT00450000040316; -.
DR   OrthoDB; EOG4H463G; -.
DR   Bgee; D3Z3N9; -.
PE   4: Predicted;
SQ   SEQUENCE   682 AA;  73882 MW;  73FDE7F67A579505 CRC64;
     MIPSKMMSAN PEEDPLDTFF QYIEDMGMKA YDGLVIQNAS DIARENDRLR NETNLAYLKE
     KNEKRRRQEE TIKRIGGEVG RGQDASYAGK HFRMGFMTMP APQDRLPHPC SSGFTVRSQS
     LHSVGGTEDD SSCGSRRQPP PKPKRDPSTK LSTSSETVNS TAASKSGRSL ERAEGKFTVP
     ASHSPPRAST SGHLFPSPGS QERNIKVSAK PRPHSDEYSK KIPPPKPKRN PNTQLSTSFD
     ETYIKKHVPR RTSLPRDSSL SQVCSPAADP EEEEPVYIEM VGNILRDFRK EEDDQSEAVY
     EEMKYPIFDD LGHDSKCDFD HHSCSSQCAT PTVPDLDFVK SSGPCTPKGL LCDIPPPFPN
     LLSHRPPLLV FPPAPVHCSP NSDESPLTPL EVTKLPVLEN VSYMKQPPGA CPSSLPSHGS
     SHAKDQTGAL GPAPGASILS SSPPPPSTLY RTQSPHGYPK SHSTSPSPVS MGRSLTPLSL
     KRPPPYDAVH SGSLSRSSSS VPHTTPRPVS QDGAKMVNAA VNTYSAAQSG SRSRTPTSPL
     EELTSLFTSG RSLLRKSSSG RRSKEPAEKS TEELKVRSHS TEPLPKLDSK ERGHYGSSSS
     REPVKAQEWD GTPGPPVVTS RMGRCSVSPT LLAGNHSSEP KVSCKLGRSA STSGVPPPSV
     TPLRQASDLQ QSQVPSSLAN RD
//
ID   D3Z3Z3_MOUSE            Unreviewed;       483 AA.
AC   D3Z3Z3;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 10.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Cacnb3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC156543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00788347; -.
DR   RefSeq; NP_001038206.1; NM_001044741.1.
DR   UniGene; Mm.3544; -.
DR   Ensembl; ENSMUST00000109150; ENSMUSP00000104778; ENSMUSG00000003352.
DR   GeneID; 12297; -.
DR   KEGG; mmu:12297; -.
DR   CTD; 12297; -.
DR   MGI; MGI:103307; Cacnb3.
DR   GeneTree; ENSGT00390000002740; -.
DR   OrthoDB; EOG469QTZ; -.
DR   Bgee; D3Z3Z3; -.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:MGI.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; TAS:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IMP:MGI.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR008079; VDCC_L_b3su.
DR   InterPro; IPR000584; VDCC_L_bsu.
DR   PANTHER; PTHR11824; Ca_channel_B; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF12052; VGCC_beta4Aa_N; 1.
DR   PRINTS; PR01626; LCACHANNELB.
DR   PRINTS; PR01696; LCACHANNELB3.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
PE   4: Predicted;
SQ   SEQUENCE   483 AA;  54396 MW;  86336C5ED592C1AB CRC64;
     MSFSDSSATF LLNEGSADSY TSRPSLDSDV SLEEDRESAR REVESQAQQQ LERAKHKPVA
     FAVRTNVSYC GVLDEECPVQ GSGVNFEAKD FLHIKEKYSN DWWIGRLVKE GGDIAFIPSP
     QRLESIRLKQ EQKARRSGNP SSLGDIGNRR SPPPSLAKQK QKQAEHVPPY DVVPSMRPVV
     LVGPSLKGYE VTDMMQKALF DFLKHRFDGR ISITRVTADL SLAKRSVLNN PGKRTIIERS
     SARSSIAEVQ SEIERIFELA KSLQLVVLDA DTINHPAQLA KTSLAPIIVF VKVSSPKVLQ
     RLIRSRGKSQ MKHLTVQMMA YDKLVQCPPE SFDVILDENQ LEDACEHLAE YLEVYWRATH
     HPAPGPGLLG PPSAIPGLQN QQLLGERVEE HSPLERDSLM PSDEASESSR QAWTGSSQRS
     SRHLEEDYAD AYQDLYQPHR QHTSGLPSAN GHDPQDRLLA QDSEHDHNDR NWQRNRPWPK
     DSY
//
ID   D3Z4U5_MOUSE            Unreviewed;       831 AA.
AC   D3Z4U5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 6.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Jakmip1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC110238; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC115722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00880630; -.
DR   Ensembl; ENSMUST00000121010; ENSMUSP00000113624; ENSMUSG00000063646.
DR   MGI; MGI:1923321; Jakmip1.
DR   Bgee; D3Z4U5; -.
DR   GO; GO:0019894; F:kinesin binding; IPI:MGI.
PE   4: Predicted;
SQ   SEQUENCE   831 AA;  97235 MW;  11CFD4F2506FF732 CRC64;
     MSKKGRSKGD KPEAETDSVQ MANEELRAKL TNIQIEFQQE KSKVGKLRER LQEAKLEREQ
     EQRRHTAYIS ELKAKLHEEK TKELQALREA LIRQHEQEAA RTAKIKEGEL QRLQATLNVL
     RDGAADKVKT ALLADAREEA RRTFDGERQR LQQEILELKA ARKQAEEALS NCMQADKAKA
     ADLRAAYQAH QDEVHRIKRE CERDIRRLMD EIKGKERVIL ALEKELGVQT GQTQRLLLQK
     EALDEQLVQV KEAERHHSSP KRELPPGIGD MAELMGGQDQ HMDERDVRRF QLKIAELNSV
     IRKLEDRNTL LADERNELLK RSRETEVQLK PLVEKNKRMN KKNEELLHSI QRMEEKLKSL
     TRENVEMKEK LSAQASLKRH TSLNDLSLTR DEQEIEFLRL QVLEQQHVID DLSLERERLL
     RSKRHRGKSL KPPKKHVVET FFGFDEESVD SETLSETSYN TDRTDRTPAT PEEDLDETTT
     REEADLRFCQ LTREYQALQR AYALLQEQVG GTLDAEREAR TREQLQADLL RCQAKIEDLE
     KLLVEKGQDA AWVEEKQVLM RTNQDLLEKI YRLEMEENQL KSEMQDAKDQ NELLEFRVLE
     LEERERRSPA FNLQITTFPE NNSSALQLFC HQEGVKGVNI SELMKNLDIL GDNGNLRNEE
     QVAVIQAGTV LALCEKWLKQ IEGTEAALTQ KMMDLEKEKD QFSRQKGYLE QELDYRKEAL
     DQAYLKIQDL EATLYNALQQ EPGRRASEAL SASQREDLQA AVEKVRRQLL RQSREFDSQI
     LRERMELLQQ AQQKIREMEG KLELQRRQLK ELEEKFLFLF LFFSLAFILW P
//
ID   D3Z508_MOUSE            Unreviewed;       692 AA.
AC   D3Z508;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Dlgap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC079441; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154604; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC163902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC165424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC168117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00918416; -.
DR   Ensembl; ENSMUST00000140728; ENSMUSP00000117358; ENSMUSG00000003279.
DR   MGI; MGI:1346065; Dlgap1.
DR   GeneTree; ENSGT00550000074473; -.
DR   Bgee; D3Z508; -.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0007268; P:synaptic transmission; TAS:MGI.
DR   InterPro; IPR005026; GKAP.
DR   Pfam; PF03359; GKAP; 1.
PE   4: Predicted;
SQ   SEQUENCE   692 AA;  76968 MW;  DB2CC3CBF1952A2A CRC64;
     MIDLFKAEWV SSVCVQVSRN GRTDQVPQDE WSGYTPRGKD DEIPCRRMRS GSYIKAMGDE
     DSGDSDTSPK PSPKVAARRE SYLKATQPSL TELTTLKISN EHSPKLQIRS HSYLRAVSEV
     SINRSLDSLD PAGLLTSPKF RSRNESYMRA MSTISQVSEM EVNGQFESVC ESVFSELESQ
     AVEALDLPLP GCFRMRSHSY VRAIEKGCSQ DDECVSLRSS SPPRTTTTVR TIQSSTGVIK
     LSSAVEVSSC ITTYKKTPPP VPPRTTTKPF ISITAQSSTE SAQDAYMDGQ GQRGDMISQS
     GLSNSTESLD SMKALTAAIE AANAQIHGPA SQHMGSNAAA VTTTTTIATV TTEDRKKDFK
     KNRCLSIGIQ VDDAEEPEKM AESKTSNKFQ SVGVQVEEEK CFRRFTRSNS VTTAVQADLD
     FHDNLENSLE SIEDNSCPGP MARQFSRDAS TSTVSIQGSG NHYHACAADD DFDTDFDPSI
     LPPPDPWIDS ITEDPLEAVQ RSVCHRDGHW FLKLLQAERD RMEGWCKLME REERENNLPE
     DILGKIRTAV GSAQLLMAQK FYQFRELCEE NLNPNAHPRP TSQDLAGFWD MLQLSIENIS
     MKFDELHQLK ANNWKQMDPL DKKERRAPPP VPKKPAKGPA PLIRERSLES SQRQEARKRL
     MAAKRAASVR QNSATESAES IEIYIPEAQT RL
//
ID   D3Z535_MOUSE            Unreviewed;       739 AA.
AC   D3Z535;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Kalrn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 2 SH3 domains.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC154524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC155257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC165079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CT010573; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00776326; -.
DR   Ensembl; ENSMUST00000114963; ENSMUSP00000110614; ENSMUSG00000061751.
DR   MGI; MGI:2685385; Kalrn.
DR   GeneTree; ENSGT00560000076675; -.
DR   Bgee; D3Z535; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00326; SH3; 2.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   SUPFAM; SSF50044; SH3; 2.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   SH3 domain.
SQ   SEQUENCE   739 AA;  82927 MW;  28F7A00C9D24D5A1 CRC64;
     MFKCISWRQT AANKTQLSGG CELTVVLQDF SAGHSSELSI QVGQTVELLE RPSERPGWCL
     VRTTERSPPQ EGLVPSSALC ISHSRSSVEM DCFFPLKDSY SHSSSENGGK SESVAHLQSQ
     PSLNSIHSSP GPKRSTNTLK KWLTSPVRRL NSGKADGNIK KQKKVRDGRK SFDLGSPKPG
     DETTPQGDSA DEKSKKGWGE DEPDEESHTP LPPPMKIFDN DPTQDEMTLE GGSYRGSLKD
     PTGCLNEGMT PPTPPRNLEE EQKAKALRGR MFVLNELVQT EKDYVKDLGI VVEGFMKRIE
     EKGVPEDMRG KEKIVFGNIH QIYDWHKDFF LAELEKCIQE QDRLAQLFIK HERKLHIYVW
     YCQNKPRSEY IVAEYDAYFE EVKQEINQRL TLSDFLIKPI QRITKYQLLL KDFLRYSEKA
     GLECSDIEKA VELMCLVPKR CNDMMNLGRL QGFEGTLTAQ GKLLQQDTFY VIELDAGMQS
     RTKERRVFLF EQIVIFSELL RKGSLTPGYM FKRSIKMNYL VLEDNVDGDP CKFALMNRET
     SERVILQAAN SDIQQAWVQD INQVLETQRD FLNALQSPIE YQRKERSTAV IRSQPPRVPQ
     ASPRPYSSGP VGSEKPPKGS SYNPPLPPLK ISTSNGSPGF DYHQPGDKFD ASKQNDLGGC
     NGTSTMTVIK DYYALKENEI CVSQGEVVQV LAVNQQNMCL VYQPASDHSP AAEGWVPGSI
     LAPLAKATAA AESSDGSIK
//
ID   D3Z559_MOUSE            Unreviewed;      1013 AA.
AC   D3Z559;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Kalrn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC154524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC155257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC165079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CT010573; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00776209; -.
DR   Ensembl; ENSMUST00000114949; ENSMUSP00000110599; ENSMUSG00000061751.
DR   Ensembl; ENSMUST00000114960; ENSMUSP00000110611; ENSMUSG00000061751.
DR   MGI; MGI:2685385; Kalrn.
DR   Bgee; D3Z559; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF00435; Spectrin; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00150; SPEC; 3.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   4: Predicted;
KW   Repeat.
SQ   SEQUENCE   1013 AA;  116985 MW;  B2F1DCB9A1E85B90 CRC64;
     MSVSFHTHTK ELWTWMEDLQ KEVLEDVCAD SVDAVQELIK QFQQQQTATL DATLNVIKEG
     EDLIQQLRSA PPSLGEPTEA RDSAMSNNKT PHSSSISHIE SVLQQLDDAQ VQMEELFHER
     KIKLDIFLQL RIFEQYTIEV TAELDAWNED LLRQMNDFNT EDLTLAEQRL QRHTERKLAM
     NNMTFEVIQQ GQDLHQYIME VQASGIELIC EKDLDLAAQV QELLEFLHEK QHELELNAEQ
     THKRLEQCLQ LRHLQAEVKQ VLGWIRNGES MLNASLVNAS SLSEAEQLQR EHEQFQLAIE
     KTHQSALQVQ QKAEALLQAG HYDADAIREC AEKVALHWQQ LMLKMEDRLK LVNASVAFYK
     TSEQVCSVLE SLEQEYRRDE DWCGGRDKLG PAAEMDHVIP LLSKHLEQKE AFLKACTLAR
     RNAEVFLKYI HRNNVSMPSV ASHTRGPEQQ VKAILSELLQ RENRVLHFWT LKKRRLDQCQ
     QYVVFERSAK QALDWIQETG EYYLSTHTST GETTEETQEL LKEYGEFRVP AKQTKEKVKL
     LIQLADSFVE KGHIHATEIR KWVTTVDKHY RDFSLRMGKY RYSLEKALGV NTEDNKDLEL
     DIIPASLSDR EVKLRDANHE INEEKRKSAR KKEFIMAELL QTEKAYVRDL HECLETYLWE
     MTSGVEEIPP GILNKEHIIF GNIQEIYDFH NNIFLKELEK YEQLPEDVGH CFVTWADKFQ
     MYVTYCKNKP DSNQLILEHA GTFFDEIQQR HGLANSISSY LIKPVQRVTK YQLLLKELLT
     CCEEGKGELK DGLEVMLSVP KKANDAMHVS MLEGFDENLD VQGELILQDA FQVWDPKSLI
     RKGRERHLFL FEISLVFSKE IKDSSGHTKY VYKNKLLTSE LGVTEHVEGD PCKFALWSGR
     TPSSDNKTVL KASNIETKQE WIKNIREVIQ ERIIHLKGAL KEPIQLPKTP AKLRNNSKRD
     GVEDGDSQGD GSSQPDTISI ASRTSQNTVE SDKDGNLVPR WHLGPGDPFS TYV
//
ID   D3Z560_MOUSE            Unreviewed;       823 AA.
AC   D3Z560;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Kalrn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC154524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154588; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC155257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC165079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CT010573; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00762436; -.
DR   Ensembl; ENSMUST00000114947; ENSMUSP00000110597; ENSMUSG00000061751.
DR   MGI; MGI:2685385; Kalrn.
DR   GeneTree; ENSGT00560000076675; -.
DR   Bgee; D3Z560; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF00435; Spectrin; 2.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00150; SPEC; 3.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   PROSITE; PS50010; DH_2; 1.
PE   4: Predicted;
KW   Repeat.
SQ   SEQUENCE   823 AA;  95643 MW;  4FC4276FC9B9A989 CRC64;
     MSVSFHTHTK ELWTWMEDLQ KEVLEDVCAD SVDAVQELIK QFQQQQTATL DATLNVIKEG
     EDLIQQLRDS AMSNNKTPHS SSISHIESVL QQLDDAQVQM EELFHERKIK LDIFLQLRIF
     EQYTIEVTAE LDAWNEDLLR QMNDFNTEDL TLAEQRLQRH TERKLAMNNM TFEVIQQGQD
     LHQYIMEVQA SGIELICEKD LDLAAQVQEL LEFLHEKQHE LELNAEQTHK RLEQCLQLRH
     LQAEVKQVLG WIRNGESMLN ASLVNASSLS EAEQLQREHE QFQLAIESLF HATSLQKTHQ
     SALQVQQKAE ALLQAGHYDA DAIRECAEKV ALHWQQLMLK MEDRLKLVNA SVAFYKTSEQ
     VCSVLESLEQ EYRRDEDWCG GRDKLGPAAE MDHVIPLLSK HLEQKEAFLK ACTLARRNAE
     VFLKYIHRNN VSMPSVASHT RGPEQQVKAI LSELLQRENR VLHFWTLKKR RLDQCQQYVV
     FERSAKQALD WIQETGEYYL STHTSTGETT EETQELLKEY GEFRVPAKQT KEKVKLLIQL
     ADSFVEKGHI HATEIRKWVT TVDKHYRDFS LRMGKYRYSL EKALGVNTED NKDLELDIIP
     ASLSDREVKL RDANHEINEE KRKSARKKEF IMAELLQTEK AYVRDLHECL ETYLWEMTSG
     VEEIPPGILN KEHIIFGNIQ EIYDFHNNIF LKELEKYEQL PEDVGHCFVT WADKFQMYVT
     YCKNKPDSNQ LILEHAGTFF DEIQQRHGLA NSISSYLIKP VQRVTKYQLL LKELLTCCEE
     GKGELKDGLE VMLSVPKKAN DAMHVSMLEG SCSPVFLGPR LHP
//
ID   D3Z574_MOUSE            Unreviewed;       566 AA.
AC   D3Z574;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 6.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Gm15800; Synonyms=EG545802;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC110037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC126938; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00831513; -.
DR   ProteinModelPortal; D3Z574; -.
DR   Ensembl; ENSMUST00000065641; ENSMUSP00000064180; ENSMUSG00000042744.
DR   MGI; MGI:2141089; EG545802.
DR   MGI; MGI:3647820; Gm15800.
DR   GeneTree; ENSGT00600000084546; -.
DR   Bgee; D3Z574; -.
PE   4: Predicted;
SQ   SEQUENCE   566 AA;  63133 MW;  AEB0A521E0B2C00E CRC64;
     MCIHQLNLLA TNPNLPITSV LGKQHPIEAR HLSSICDIME KAMVNGDTCI VRCILVVFQV
     VFKFFFSPQT ERNRDIIRRS GLLLWQLLMA PKDQICPEIQ KEVCLAISSG LNILYPGETE
     INNLLKLVLT EVSGERNSGL SQLRDVILTN LAEQLQNNRF GSDEDDHYRL NDELLHYILK
     IVVRESCILI TKCQTVSKDD FQKLLSTVPA ASSCLRYLMA VQNHLLSNTV LIKPDENEDS
     DSSLQGETLK ELKTSILALA TQILTGCDEV LEMLQQVTTA LINSDIPDRE QRLKGLEQVT
     KATMLGHLLP VLLTSLMHPN LQTLTMADAL MPQLVQLVLY TSQTALLLKT QCPAFAEMSC
     SPCGTSDQKC RLFPDERMLE EKEEPGFLTG LKIPAPWAAG KTVETVHPVR DNYKFKETVH
     IPGARCLYLR FDTRCSSQYD YDKLVIYAGP NTNSRKVAEY GGNTLGYGSR SVLGTGWPKD
     LVKVEGDTVT FSFEMRSGRE HNTPDKAMWG FACTVRAQES SEDVSGGLPF LVDLALGLSV
     LACSMLRILY NGPEITKEEE ACQDLL
//
ID   D3Z5C9_MOUSE            Unreviewed;       420 AA.
AC   D3Z5C9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Akap5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC120002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00753601; -.
DR   ProteinModelPortal; D3Z5C9; -.
DR   Ensembl; ENSMUST00000095610; ENSMUSP00000093270; ENSMUSG00000021057.
DR   MGI; MGI:2685104; Akap5.
DR   GeneTree; ENSGT00390000019941; -.
DR   Bgee; D3Z5C9; -.
DR   GO; GO:0006605; P:protein targeting; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR001573; Pkinase-A_anch_WSK-motif.
DR   Pfam; PF03832; WSK; 1.
PE   4: Predicted;
SQ   SEQUENCE   420 AA;  45995 MW;  3AE7CF71070E0EA5 CRC64;
     METSVSEIQV ETKDEKGPVA ASPQKERQER KTATLCFKRR KKANKTKPKA GSRTAEETKK
     HTPEAGGSGQ RQPAGAWASI KGLVTHRKRS EPAKKQKPPE AEVQPEDGAL PKKKAKSRLK
     FPCLRFSRGA KRSRHSKLTE DSGYVRVQGE ADDLEIKAQT QPDDQAIQAG STQGLQEGVL
     VRDGKKSQES HISNSVTSGE NVIAIELELE NKSSAIQMGT PELEKETKVI TEKPSVQTQR
     ASLLESSAAG SPRSVTSAAP PSPATTHQHS LEEPSNGIRE SAPSGKDDRR KTAAEEKKSG
     ETALGQAEDL KENGIDTEKP RSEESKRMEP IAIIITDTEI SEFDVKKSKN VPKQFLISME
     NEQVGVFAND SDFEGRTSEQ YETLLIETAS SLVKNAIELS VEQLVNEMVS EDNQINTLFQ
//
ID   D3Z5H5_MOUSE            Unreviewed;      1438 AA.
AC   D3Z5H5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 9.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Mll1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC061963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC142113; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00230024; -.
DR   Ensembl; ENSMUST00000128768; ENSMUSP00000122541; ENSMUSG00000002028.
DR   MGI; MGI:96995; Mll1.
DR   GeneTree; ENSGT00580000081416; -.
DR   Bgee; D3Z5H5; -.
DR   GO; GO:0044428; C:nuclear part; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009952; P:anterior/posterior pattern formation; IMP:MGI.
DR   GO; GO:0006306; P:DNA methylation; IMP:MGI.
DR   GO; GO:0035162; P:embryonic hemopoiesis; IMP:MGI.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
DR   GO; GO:0051569; P:regulation of histone H3-K4 methylation; IMP:MGI.
DR   InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR   InterPro; IPR002857; Znf_CXXC.
DR   Pfam; PF02008; zf-CXXC; 1.
DR   SMART; SM00384; AT_hook; 3.
DR   PROSITE; PS51058; ZF_CXXC; 1.
PE   4: Predicted;
SQ   SEQUENCE   1438 AA;  154682 MW;  B780BFD7034BDC56 CRC64;
     MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPQAGGGG PGAPPSPPAV
     AAAAAGSSGA GVPGGAAAAS AASSSSASSS SSSSSSASSG PALLRVGPGF DAALQVSAAI
     GTNLRRFRAV FGESGGGGGS GELTTQIPGS WRTKGLIHDI KAELVRLLAW SWCLNDEQFL
     GFGSDEEVRV RSPTRSPSVK ASPRKPRGRP RSGSDRNPAI LSDPSVFSPL NKSETKSADK
     IKKKDSKSIE KKRGRPPTFP GVKIKITHGK DIAELTQGSK EDSLKKVKRT PSAMFQQATK
     IKKLRAGKLS PLKSKFKTGK LQIGRKGVQI VRRRGRPPST ERIKTPSGLL INSELEKPQK
     VRKDKEGTPP LTKEDKTVVR QSPRRIKPVR IIPSCKRTDA TIAKQLLQRA KKGAQKKIEK
     EAAQLQGRKV KTQVKNIRQF IMPVVSAISS RIIKTPRRFI EDEDYDPPMK IARLESTPNS
     RFSATSCGSS EKSSAASQHS SQMSSDSSRS SSPSIDTTSD SQASEEIQAL PEERSNTPEV
     HTPLPISQSP ENESNDRRSR RYSMSERSFG SRATKKLPTL QSAPQQQTSS SPPPPLLTPP
     PPLQPASGIS DHTPWLMPPT IPLASPFLPA SAAPMQGKRK SILREPTFRW TSLKHSRSEP
     QYFSSAKYAK EGLIRKPIFD NFRPPPLTPE DVGFASGFSA SGTAASARLF SPLHSGTRFD
     IHKRSPILRA PRFTPSEAHS RIFESVTLPS NRTSSGASSS GVSNRKRKRK VFSPIRSEPR
     SPSHSMRTRS GRLSTSELSP LTPPSSVSSS LSIPVSPLAA SALNPTFTFP SHSLTQSGES
     TEKNQRARKQ TSALAEPFSS NSPALFPWFT PGSQTEKGRK KDTAPEELSK DRDADKSVEK
     DKSRERDRER EKENKRESRK EKRKKGSDIQ SSSALYPVGR VSKEKVAGED VGTSSSAKKA
     TGRKKSSSLD SGADVAPVTL GDTTAVKAKI LIKKGRGNLE KNNLDLGPAA PSLEKERTPC
     LSAPSSSTVK HSTSSIGSML AQADKLPMTD KRVASLLKKA KAQLCKIEKS KSLKQTDQPK
     AQGQESDSSE TSVRGPRIKH VCRRAAVALG RKRAVFPDDM PTLSALPWEE REKILSSMGN
     DDKSSVAGSE DAEPLAPPIK PIKPVTRNKA PQEPPVKKGR RSRRCGQCPG CQVPEDCGIC
     TNCLDKPKFG GRNIKKQCCK MRKCQNLQWM PSKASLQKQT KAVKKKEKKS KTTEKKESKE
     STAVKSPLEP AQKAAPPPRE EPAPKKSSSE PPPRKPVEEK SEEGGAPAPA PAPEPKQVSA
     PASRKSSKQV SQPAAVVPPQ PPSTAPQKKE APKAVPSEPK KKQPPPPEPG PEQSKQKKVA
     PRPSIPVKQK PKDKEKPPPV SKQENAGTLN ILNPLSNGIS SKQKIPADGV HRIRVDFK
//
ID   D3Z5J3_MOUSE            Unreviewed;       938 AA.
AC   D3Z5J3;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 10.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Sorbs1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Contains 3 SH3 domains.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC142101; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC144949; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC170187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00655029; -.
DR   RefSeq; NP_848139.1; NM_178362.1.
DR   UniGene; Mm.210815; -.
DR   UniGene; Mm.417719; -.
DR   UniGene; Mm.440351; -.
DR   Ensembl; ENSMUST00000099467; ENSMUSP00000097066; ENSMUSG00000025006.
DR   GeneID; 20411; -.
DR   KEGG; mmu:20411; -.
DR   CTD; 20411; -.
DR   MGI; MGI:700014; Sorbs1.
DR   GeneTree; ENSGT00550000074287; -.
DR   OrthoDB; EOG40K7Z2; -.
DR   Bgee; D3Z5J3; -.
DR   GO; GO:0001725; C:stress fiber; IDA:MGI.
DR   GO; GO:0019901; F:protein kinase binding; IDA:MGI.
DR   InterPro; IPR000108; p67phox.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR003127; Sorb.
DR   Pfam; PF00018; SH3_1; 2.
DR   Pfam; PF07653; SH3_2; 1.
DR   Pfam; PF02208; Sorb; 1.
DR   PRINTS; PR00499; P67PHOX.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 3.
DR   SMART; SM00459; Sorb; 1.
DR   SUPFAM; SSF50044; SH3; 3.
DR   PROSITE; PS50002; SH3; 3.
DR   PROSITE; PS50831; SOHO; 1.
PE   4: Predicted;
KW   SH3 domain.
SQ   SEQUENCE   938 AA;  103977 MW;  1D0AEEB5B7EB2F20 CRC64;
     MSSECDVGSS KAVVNGLASG NHGPDKDMDP TKICTGKGTV TLRASSSYRG TPSSSPVSPQ
     ESPKHESKSD EWKLSSSADT NGNAQPSPLA AKGYRSVHPS LSADKPQGAT SSSSAPSEVI
     VVPLYLVNTD RGQGQEGTAR TPASLGPLGC VHTVPATTPA ASPLTFPTLD DFIPPHLQRR
     PHHSQPASAC GSLSPASQTS PPSPPPPLVP PVPEDLHRGL EPDLPGAVSS TGSPLLNEVS
     SSHIETDSQD FPPTSRPSSA YPSTTIVNPT IVLLQHNREQ QKRLSSLSDP ASERRAGEQD
     PVPTPAELTS PGRASERRAK DASRRVVRST QDLSDVSTDE VGIPLRNTER SKDWYKTMFK
     QIHKLNRDTP EENPYFPTYK FPELPEILQN SEEDSSYTPT YQFPASTPSP KSEDDDSDVH
     SPRYSFSDDT KSPLSVPRSK SEMNYIEGEK VVKRSATLPL PARSSSLKSS PERNDWEPPD
     KKVDTRKYRA EPKSIYEYQP GKSSVLTNEK MSRDISPEEI DLKNEPWYKF FSELEFGRPP
     PKKIWDYTPG DCSILPREDR KTNLEKDLSF CQAELEADLE KVETVNKSPS ANSPQSSAVS
     PTPDITSEPP GYIYSSNFHA VKRESDGTPG GLASLENERQ IYKSVLEGGD IPLQGLSGLK
     RPSSSASTKD SESPRHFIPA DYLESTEEFI RRRHDDKEMR PARAKFDFKA QTLKELPLQK
     GDVVYIYRQI DQNWYEGEHH GRVGIFPRTY IELLPPAEKA QPRKLAPVQV LEYGEAIAKF
     NFNGDTQVEM SFRKGERITL LRQVDENWYE GRIPGTSRQG IFPITYVDVL KRPLVKTPVD
     YIDLPYSSSP SRSATVSPQQ PQAQQRRVTP DRSQPSLDLC SYQALYSYVP QNDDELELRD
     GDIVDVMEKC DDGWFVGTSR RTRQFGTFPG NYVKPLYL
//
ID   D3Z5K8_MOUSE            Unreviewed;      1841 AA.
AC   D3Z5K8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Shank2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC124520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC127546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC140268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC152166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00757097; -.
DR   Ensembl; ENSMUST00000105902; ENSMUSP00000101522; ENSMUSG00000037541.
DR   MGI; MGI:2671987; Shank2.
DR   GeneTree; ENSGT00510000046474; -.
DR   OrthoDB; EOG48PMJ9; -.
DR   Bgee; D3Z5K8; -.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
KW   ANK repeat; Repeat.
SQ   SEQUENCE   1841 AA;  200122 MW;  16FE35AC62563766 CRC64;
     MPRSPTSSED EMAQSFSDYS VGSESDSSKE ETIYDTIRAT TEKPGGVKME ELQGNTLVIR
     VVIQDLQQTK CIRFNPDATV WVAKQRILCT LNQGLKDVLN YGLFQPASNG RDGKFLDEER
     LLREYPQPMG PGVPSLEFRY KKRVYKQSNL DEKQLARLHT KTNLKKFMDH AQHRSVEKLA
     KLLDRGLDPN FHDLETGETP LTLAAQLDDS MEVIKALRNG GAHLDFRSRD GMTALHKAAR
     MRNQVALKTL LELGASPDYK DSYGLTPLYH TAIVGGDPYC CELLLHEHAS VCCKDENGWH
     EIHQACRYGH VQHLEHLLFY GADMSAQNAS GNTALHICAL YNQDSCARVL LFRGGNKELK
     NYNSQTPFQV AIIAGNFELA EYIKNHKETD IVPFREAPAY SNRRRRPPNT LAAPRVLLRS
     NSDNNLNAGA PEWAVCSAAT SHRSLSPQLL QQTPSKPDGA TKSLGSYTPG PRSRSPSLNR
     LGGTAEDGKR TQPHWHVGSP FTPGANKDSL STFEYPGPRR KLYSAVPGRL FVAVKPYQPQ
     VDGEIPLHRG DRVKVLSIGE GGFWEGSARG HIGWFPAECV EEVQCKPRDS QAETRADRSK
     KLFRHYTVGS YDSFDAASDC IIEDKTVVLQ KKDNEGFGFV LRGAKADTPI EEFTPTPAFP
     ALQYLESVDE GGVAWQAGLR TGDFLIEVNN ENVVKVGHRQ VVNMIRQGGN HLILKVVTVT
     RNLDPDDTAR KKAPPPPKRA PTTALTLRSK SMTAELEELD KPEEIVPASK PSRTAENVAI
     ESRVATIKQR PTSRCFPAAS DVNSVYERQG IAVMTPTVPG SPKGPFLGLP RGTMRRQKSI
     DSRIFLSGIT EEERQFLAPP MLKFTRSLSM PDTSEDIPPP PQSVPPSPPP PSPTTYNCPR
     SPTPRVYGTI KPAFNQNPVV AKVPPATRSD TVATMMREKG MFYRRELDRF SLDSEDVYSR
     SPAPQAAFRT KRGQMPENPY SEVGKIASKA VYVPAKPARR KGVLVKQSNV EDSPEKTCSI
     PIPTIIVKEP STSSSGKSSQ GSSMEIDPQA TEPGQLRPDD SLTVSSPFAA AIAGAVRDRE
     KRLEARRNSP AFLSTDLGDE DVGLGPPAPR MQASKFPEEG GFGDEDETEQ PLLPTPGAAP
     RELENHFLGG GEAGAQGEAG GPLSSTSKAK GPESGPAAPL KSSSPAGPEN YVHPLTGRLL
     DPSSPLALAL SARDRAMQES QQGHKGEAPK ADLNKPLYID TKMRPSVESG FPPVTRQNTR
     GPLRRQETEN KYETDLGKDR RADDKKNMLI NIVDTAQQKS AGLLMVHTVD VPMAGPPLEE
     EEDREDGDTK PDHSPSTVPE GVPKTEGALQ ISAAPEPAVA PGRTIVAAGS VEEAVILPFR
     IPPPPLASVD LDEDFLFTEP LPPPLEFANS FDIPDDRAAS VPALADLVKQ KKNDTSQPPT
     LNSSQPANST DSKKPAGISN CLPSSFLPPP ESFDAVTDSG IEEVDSRSSS DHHLETTSTI
     STVSSISTLS SEGGESMDTC TVYADGQAFV VDKPPVPPKP KMKPIVHKSN ALYQDTLPEE
     DTDGFVIPPP APPPPPGSAQ AGVAKVIQPR TSKLWGDVPE VKSPILSGPK ANVISELNSI
     LQQMNRGKSV KPGEGLELPV GAKSANLAPR SPEVMSTVSG TRSTTVTFTV RPGTSQPITL
     QSRPPDYESR TSGPRRAPSP VVSPTELSKE ILPTPPPPSA TAASPSPTLS DVFSLPSQSP
     AGDLFGLNPA GRSRSPSPSI LQQPISNKPF TTKPVHLWTK PDVADWLESL NLGEHKETFM
     DNEIDGSHLP NLQKEDLIDL GVTRVGHRMN IERALKQLLD R
//
ID   D3Z5K9_MOUSE            Unreviewed;      1472 AA.
AC   D3Z5K9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Shank2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC124520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC127546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC140268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC152166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00349908; -.
DR   Ensembl; ENSMUST00000105900; ENSMUSP00000101520; ENSMUSG00000037541.
DR   MGI; MGI:2671987; Shank2.
DR   GeneTree; ENSGT00510000046474; -.
DR   Bgee; D3Z5K9; -.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   4: Predicted;
SQ   SEQUENCE   1472 AA;  158543 MW;  84E5F0582BF7E16F CRC64;
     MKSLLNAFTK KEVPFREAPA YSNRRRRPPN TLAAPRVLLR SNSDNNLNAG APEWAVCSAA
     TSHRSLSPQL LQQTPSKPDG ATKSLGSYTP GPRSRSPSLN RLGGTAEDGK RTQPHWHVGS
     PFTPGANKDS LSTFEYPGPR RKLYSAVPGR LFVAVKPYQP QVDGEIPLHR GDRVKVLSIG
     EGGFWEGSAR GHIGWFPAEC VEEVQCKPRD SQAETRADRS KKLFRHYTVG SYDSFDAASD
     CIIEDKTVVL QKKDNEGFGF VLRGAKADTP IEEFTPTPAF PALQYLESVD EGGVAWQAGL
     RTGDFLIEVN NENVVKVGHR QVVNMIRQGG NHLILKVVTV TRNLDPDDTA RKKAPPPPKR
     APTTALTLRS KSMTAELEEL GKATSVRKKK DKPEEIVPAS KPSRTAENVA IESRVATIKQ
     RPTSRCFPAA SDVNSVYERQ GIAVMTPTVP GSPKGPFLGL PRGTMRRQKS IDSRIFLSGI
     TEEERQFLAP PMLKFTRSLS MPDTSEDIPP PPQSVPPSPP PPSPTTYNCP RSPTPRVYGT
     IKPAFNQNPV VAKVPPATRS DTVATMMREK GMFYRRELDR FSLDSEDVYS RSPAPQAAFR
     TKRGQMPENP YSEVGKIASK AVYVPAKPAR RKGVLVKQSN VEDSPEKTCS IPIPTIIVKE
     PSTSSSGKSS QGSSMEIDPQ ATEPGQLRPD DSLTVSSPFA AAIAGAVRDR EKRLEARRNS
     PAFLSTDLGD EDVGLGPPAP RMQASKFPEE GGFGDEDETE QPLLPTPGAA PRELENHFLG
     GGEAGAQGEA GGPLSSTSKA KGPESGPAAP LKSSSPAGPE NYVHPLTGRL LDPSSPLALA
     LSARDRAMQE SQQGHKGEAP KADLNKPLYI DTKMRPSVES GFPPVTRQNT RGPLRRQETE
     NKYETDLGKD RRADDKKNML INIVDTAQQK SAGLLMVHTV DVPMAGPPLE EEEDREDGDT
     KPDHSPSTVP EGVPKTEGAL QISAAPEPAV APGRTIVAAG SVEEAVILPF RIPPPPLASV
     DLDEDFLFTE PLPPPLEFAN SFDIPDDRAA SVPALADLVK QKKNDTSQPP TLNSSQPANS
     TDSKKPAGIS NCLPSSFLPP PESFDAVTDS GIEEVDSRSS SDHHLETTST ISTVSSISTL
     SSEGGESMDT CTVYADGQAF VVDKPPVPPK PKMKPIVHKS NALYQDTLPE EDTDGFVIPP
     PAPPPPPGSA QAGVAKVIQP RTSKLWGDVP EVKSPILSGP KANVISELNS ILQQMNRGKS
     VKPGEGLELP VGAKSANLAP RSPEVMSTVS GTRSTTVTFT VRPGTSQPIT LQSRPPDYES
     RTSGPRRAPS PVVSPTELSK EILPTPPPPS ATAASPSPTL SDVFSLPSQS PAGDLFGLNP
     AGRSRSPSPS ILQQPISNKP FTTKPVHLWT KPDVADWLES LNLGEHKETF MDNEIDGSHL
     PNLQKEDLID LGVTRVGHRM NIERALKQLL DR
//
ID   D3Z5M4_MOUSE            Unreviewed;      1883 AA.
AC   D3Z5M4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Ank1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC115361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC126445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00881427; -.
DR   Ensembl; ENSMUST00000117270; ENSMUSP00000113495; ENSMUSG00000031543.
DR   MGI; MGI:88024; Ank1.
DR   GeneTree; ENSGT00600000084024; -.
DR   Bgee; D3Z5M4; -.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0048821; P:erythrocyte development; IMP:MGI.
DR   GO; GO:0015672; P:monovalent inorganic cation transport; IMP:MGI.
DR   GO; GO:0006779; P:porphyrin biosynthetic process; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR000488; Death.
DR   InterPro; IPR011029; DEATH-like.
DR   InterPro; IPR000906; ZU5.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 3.
DR   Gene3D; G3DSA:1.10.533.10; DEATH_like; 1.
DR   Pfam; PF00023; Ank; 18.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF00791; ZU5; 1.
DR   SMART; SM00248; ANK; 23.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00218; ZU5; 1.
DR   SUPFAM; SSF48403; ANK; 2.
DR   SUPFAM; SSF47986; DEATH_like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 20.
DR   PROSITE; PS50017; DEATH_DOMAIN; 1.
DR   PROSITE; PS51145; ZU5; 1.
PE   4: Predicted;
KW   ANK repeat; Repeat.
SQ   SEQUENCE   1883 AA;  206911 MW;  677989B1DA154627 CRC64;
     MAQAAKQLKK IKDIEAQALQ EQKEKEESNR KRRNRSRDRK KKADAATSFL RAARSGNLDK
     ALDHLRNGVD INTCNQNGLN GLHLASKEGH VKMVVELLHK EIILETTTKK GNTALHIAAL
     AGQDEVVREL VNYGANVNAQ SQKGFTPLYM AAQENHLEVV KFLLENGANQ NVATEDGFTP
     LAVALQQGHE NVVAHLINYG TKGKVRLPAL HIAARNDDTR TAAVLLQNDP NPDVLSKTGF
     TPLHIAAHYE NLNVAQLLLN RGASVNFTPQ NGITPLHIAS RRGNVIMVRL LLDRGAQIET
     RTKDELTPLH CAARNGHVRI SEILLDHGAP IQAKTKNGLS PIHMAAQGDH LDCVRLLLQY
     NAEIDDITLD HLTPLHVAAH CGHHRVAKVL LDKGAKPNSR ALNGFTPLHI ACKKNHIRVM
     ELLLKTGASI DAVTESGLTP LHVASFMGHL PIVKNLLQRG ASPNVSNVKV ETPLHMAARA
     GHTEVAKYLL QNKAKANAKA KDDQTPLHCA ARIGHTGMVK LLLENGASPN LATTAGHTPL
     HTAAREGHVD TALALLEKEA SQACMTKKGF TPLHVAAKYG KVRLAELLLE HDAHPNAAGK
     NGLTPLHVAV HHNNLDIVKL LLPRGGSPHS PAWNGYTPLH IAAKQNQIEV ARSLLQYGGS
     ANAESVQGVT PLHLAAQEGH TEMVALLLSK QANGNLGNKS GLTPLHLVSQ EGHVPVADVL
     IKHGVTVDAT TRMGYTPLHV ASHYGNIKLV KFLLQHQADV NAKTKLGYSP LHQAAQQGHT
     DIVTLLLKNG ASPNEVSSNG TTPLAIAKRL GYISVTDVLK VVTDETSVVL VSDKHRMSYP
     ETVDEILDVS EDEGTAHISI MGDELVGSKA ERRDSRDVGE EKELLDFVPK LDQVVESPAI
     PRIPCVTPET VVIRSEDQEQ ASKEYDEDSL IPSSPATETS DNISPVASPV HTGFLVSFMV
     DARGGSMRGS RHNGLRVVIP PRTCAAPTRI TCRLVKPQKL NTPPPLAEEE GLASRIIALG
     PTGAQFLSPV IVEIPHFASH GRGDRELVVL RSENGSVWKE HKSRYGESYL DQILNGMDEE
     LGSLEELEKK RVCRIITTDF PLYFVIMSRL CQDYDTIGPE GGSLRSKLVP LVQATFPENA
     VTKKVKLALQ AQPVPDELVT KLLGNQATFS PIVTVEPRRR KFHRPIGLRI PLPPSWTDNP
     RDSGEGDTTS LRLLCSVIGG TDQAQWEDIT GTTKLIYANE CANFTTNVSA RFWLSDCPRT
     AEAVHFATLL YKELTAVPYM AKFVIFAKMN DAREGRLRCY CMTDDKVDKT LEQHENFVEV
     ARSRDIEVLE GMPLFAELSG NLVPVKKAAQ QRSFHFQSFR ENRLAIPVKV RDSSREPGGF
     LSFLRKTMKY EDTQHILCHL NITMPPCTKG SGAEDRRRTL TPLTLRYSIL SESRLGFTSD
     TDRVEMRMAV IREHLGLSWA ELARELQFSV EDINRIRVEN PNSLLDQSTA LLTLWVDREG
     ENAKMENLYT ALRNIDRSEI VNMLEGSGRQ SRNLKPERRH GDREYSLSPS QVNGYSSLQD
     ELLSPASLQY ALPSPLCADQ YWNEVAVIDA IPLAATEHDT MLEMSDMQVW SAGLTPSLVT
     AEDSSLECSK AEDSDAIPEW KLEGAHSEDT QGPELGSQDL VEDDTVDSDA TNGLADLLGQ
     EEGQRSEKKR QEVSGTEQDT ETEVSLVSGQ QRVHARITDS PSVRQVLDRS QARTLDWDKQ
     GSTAVHPQEA TQSSWQEEVT QGPHSFQRRI TTIQGPEPGA LQEYEQVLVS TREHVQRGPP
     ETGSPKAGKE PSLWAPESAF SQEVQGDELQ NIPGEQVTEE QFTDEQGNIV TKKIIRKVVR
     QVDSSGAIDT QQHEEDHTST PKP
//
ID   D3Z5P0_MOUSE            Unreviewed;       703 AA.
AC   D3Z5P0;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Brsk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC161197; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00881320; -.
DR   Ensembl; ENSMUST00000048248; ENSMUSP00000039517; ENSMUSG00000035390.
DR   Ensembl; ENSMUST00000120836; ENSMUSP00000113448; ENSMUSG00000035390.
DR   MGI; MGI:2685946; Brsk1.
DR   GeneTree; ENSGT00570000078909; -.
DR   Bgee; D3Z5P0; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0030010; P:establishment of cell polarity; IGI:MGI.
DR   GO; GO:0030182; P:neuron differentiation; IGI:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   4: Predicted;
SQ   SEQUENCE   703 AA;  77197 MW;  F129EFAB986686F4 CRC64;
     MKVEREIAIL KLIEHPHVLK LHDVYENKKY LYLVLEHVSG GELFDYLVKK GRLTPKEARK
     FFRQIVSALD FCHSYSICHR DLKPENLLLD EKNNIRIADF GMASLQVGDS LLETSCGSPH
     YACPEVIKGE KYDGRRADMW SCGVILFALL VGALPFDDDN LRQLLEKVKR GVFHMPHFIP
     PDCQSLLRGM IEVEPEKRLS LEQIQKHPWY LGGKHEPDPC LEPAPGRRVA MRSLPSNGEL
     DPDVLESMAS LGCFRDRERL HRELRSEEEN QEKMIYYLLL DRKERYPSCE DQDLPPRNDV
     DPPRKRVDSP MLSRHGKRRP ERKSMEVLSI TDAGSGGSPV PTRRALEMAQ HSQRSRSVSG
     ASTGLSSSPL SSPRSPVFSF SPEPGAGDEA RGGGSPTSKT QTLPSRGPRG GGAGEQPPPP
     SARSTPLPGP PGSPRSSGGT PLHSPLHTPR ASPTGTPGTT PPPSPGGGVG GAAWRSRLNS
     IRNSFLGSPR FHRRKMQVPT AEEMSSLTPE SSPELAKRSW FGNFISLDKE EQIFLVLKDK
     PLSSIKADIV HAFLSIPSLS HSVLSQTSFR AEYKASGGPS VFQKPVRFQV DISSSEGPEP
     SPRRDGSSGG GIYSVTFTLI SGPSRRFKRV VETIQAQLLS THDQPSVQAL ADEKNGAQTR
     PAGTPPRSLQ PPPGRSDPDL SSSPRRGPPK DKKLLATNGT PLP
//
ID   D3Z5R1_MOUSE            Unreviewed;        55 AA.
AC   D3Z5R1;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Hoxa3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC015583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC091106; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00880844; -.
DR   Ensembl; ENSMUST00000048882; ENSMUSP00000043008; ENSMUSG00000079560.
DR   Ensembl; ENSMUST00000114434; ENSMUSP00000110077; ENSMUSG00000079560.
DR   Ensembl; ENSMUST00000118397; ENSMUSP00000113224; ENSMUSG00000079560.
DR   Ensembl; ENSMUST00000125044; ENSMUSP00000116334; ENSMUSG00000079560.
DR   MGI; MGI:96175; Hoxa3.
DR   GeneTree; ENSGT00600000084019; -.
DR   Bgee; D3Z5R1; -.
DR   GO; GO:0009952; P:anterior/posterior pattern formation; IGI:MGI.
DR   GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
DR   GO; GO:0051216; P:cartilage development; IGI:MGI.
DR   GO; GO:0048704; P:embryonic skeletal system morphogenesis; IGI:MGI.
DR   GO; GO:0021615; P:glossopharyngeal nerve morphogenesis; IGI:MGI.
DR   GO; GO:0048645; P:organ formation; IMP:MGI.
DR   GO; GO:0060017; P:parathyroid gland development; IGI:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0010159; P:specification of organ position; IGI:MGI.
DR   GO; GO:0048538; P:thymus development; IMP:MGI.
DR   GO; GO:0030878; P:thyroid gland development; IMP:MGI.
PE   4: Predicted;
SQ   SEQUENCE   55 AA;  5902 MW;  44AA49C4694B2782 CRC64;
     MQKATYYDSS AIYGGYPYQA ANGFAYNASQ QPYAPSAALG TDGVEYHRPA CSLQS
//
ID   D3Z5T6_MOUSE            Unreviewed;       610 AA.
AC   D3Z5T6;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Klc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC152065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00874566; -.
DR   ProteinModelPortal; D3Z5T6; -.
DR   Ensembl; ENSMUST00000084942; ENSMUSP00000082005; ENSMUSG00000021288.
DR   MGI; MGI:107978; Klc1.
DR   GeneTree; ENSGT00390000006393; -.
DR   Bgee; D3Z5T6; -.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0035253; C:ciliary rootlet; IDA:MGI.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR   GO; GO:0005871; C:kinesin complex; IEA:InterPro.
DR   GO; GO:0043227; C:membrane-bounded organelle; IDA:MGI.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0008088; P:axon cargo transport; IMP:MGI.
DR   InterPro; IPR002151; Kinesin_light.
DR   InterPro; IPR015792; Kinesin_light_repeat.
DR   InterPro; IPR015390; Rabaptin_Rab5-bd.
DR   InterPro; IPR001440; TPR-1.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 2.
DR   Pfam; PF09311; Rab5-bind; 1.
DR   Pfam; PF00515; TPR_1; 3.
DR   PRINTS; PR00381; KINESINLIGHT.
DR   SMART; SM00028; TPR; 5.
DR   PROSITE; PS01160; KINESIN_LIGHT; 4.
DR   PROSITE; PS50005; TPR; 6.
DR   PROSITE; PS50293; TPR_REGION; 2.
PE   4: Predicted;
KW   Repeat; TPR repeat.
SQ   SEQUENCE   610 AA;  68715 MW;  D9F4B3E4C2A9E975 CRC64;
     MSTMVYIKEE KLEKLTQDEI ISKTKQVIQG LEALKNEHNS ILQSLLETLK CLKKDDESNL
     VEEKSSMIRK SLEMLELGLS EAQVMMALSN HLNAVESEKQ KLRAQVRRLC QENQWLRDEL
     ANTQQKLQKS EQSVAQLEEE KKHLEFMNQL KKYDDDISPS EDKDSDSSKE PLDDLFPNDE
     DEPGQGIQHS SAAAAAQQGG YEIPARLRTL HNLVIQYASQ GRYEVAVPLC KQALEDLEKT
     SGHDHPDVAT MLNILALVYR DQNKYKDAAN LLNDALAIRE KTLGRDHPAV AATLNNLAVL
     YGKRGKYKEA EPLCKRALEI REKVLGKDHP DVAKQLNNLA LLCQNQGKYE EVEYYYQRAL
     GIYQTKLGPD DPNVAKTKNN LASCYLKQGK FKQAETLYKE ILTRAHEREF GSVDDENKPI
     WMHAEEREEC KGKQKDGSAF GEYGGWYKAC KVDSPTVTTT LKNLGALYRR QGKFEAAETL
     EEAAMRSRKQ GLDNVHKQRV AEVLNDPESM EKRRSRESLN MDVVKYESGP DGGEEVSMSV
     EWNGDGTGSL KRSGSFSKLR ASIRRSSEKL VRKLKGGSSR DSEPRNPGAS PAEPLCVEND
     SSSLEDASTN
//
ID   D3Z5X6_MOUSE            Unreviewed;       468 AA.
AC   D3Z5X6;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Sept3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Belongs to the septin family.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC104325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00761331; -.
DR   Ensembl; ENSMUST00000077804; ENSMUSP00000076977; ENSMUSG00000022456.
DR   MGI; MGI:1345148; Sept3.
DR   GeneTree; ENSGT00590000082767; -.
DR   Bgee; D3Z5X6; -.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:InterPro.
DR   InterPro; IPR000038; Cell_Div_GTP-bd.
DR   InterPro; IPR008114; Septin3.
DR   PANTHER; PTHR18884; Cell_Div_GTP_bd; 1.
DR   Pfam; PF00735; Septin; 1.
DR   PRINTS; PR01741; SEPTIN3.
PE   3: Inferred from homology;
KW   GTP-binding; Nucleotide-binding.
SQ   SEQUENCE   468 AA;  53406 MW;  0293DEC529962DB9 CRC64;
     MSELVPEPRP KPAVPMKPVS INSNLLGYIG IDTIIEQMRK KTMKTGFDFN IMVVGQSGLG
     KSTLVNTLFK SQVSRKASSW NREEKIPKTV EIKAIGHVIE EGGVKMKLTV IDTPGFGDQI
     NNENCWEPIE KYINEQYEKF LKEEVNIARK KRIPDTRVHC CLYFISPTGH SLRPLDLEFM
     KHLSKVVNII PVIAKADTMT LEEKSEFKQR VRFYPQKEFD EDLEDKTEND KIRQESMPFA
     VVGSDKEYQV NGKRVLGRKT PWGIIEVENL NHCEFALLRD FVIRTHLQDL KEVTHNIHYE
     TYRAKRLNDN GGLPPVSVDT EETTVTRALL CVIIHIPLLQ THTHPRYHSH HLLSALSPRP
     VWYLCSILSS VCVCVCVCVC VCVCMYVCMC VMESACVYVC VMESACVCVC MCVYVCVYSG
     VRYFHCPLWK VLCKSAFSMT LHSVSFFLVL QNKKLCASLK RSGEGFNL
//
ID   D3Z613_MOUSE            Unreviewed;       388 AA.
AC   D3Z613;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Gm7324;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC140256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00474144; -.
DR   ProteinModelPortal; D3Z613; -.
DR   Ensembl; ENSMUST00000053965; ENSMUSP00000055939; ENSMUSG00000049235.
DR   MGI; MGI:3646999; Gm7324.
DR   GeneTree; ENSGT00550000074314; -.
DR   OrthoDB; EOG4CNQSK; -.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR012604; RBM1CTR.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF08081; RBM1CTR; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   4: Predicted;
SQ   SEQUENCE   388 AA;  42179 MW;  E0D5D92FA5E43DC3 CRC64;
     MVEADRPGKL FIGGLNTETN EKALEAVFGK YGRIVEILLM KDRETNKSRG FAFVTFESPA
     DAKDAARDMN GKSLDGKAIK VEQATKPSFE SGRRGPPPPP RSRGPPRGLR GGSGGTRGPP
     SRGGYMDDGG YSMNFNMSSS RGPLPVKRGP PPRSGGPPPK RSTPSGPVRS SSGMGGRTPV
     SRGRDSYGGP PRREPLPSRR DVYLSPRDDG YSTKDNYSSR DYPSSRDTRD YAPPPRDYTY
     RDYSHSSSRD DYPSRGYGDR DGYGRDRDYS DHPSGGSYRD SYESYGNSRS ASPTRGPPPS
     YGGSSRYDDY SSSRDGYGGS RDSYSSSRSD LYSSGRDRVG RQERGLPPSM ERGYPPPRDS
     YSSSSRGAPR GGGRGGSRSD RGGGRSRY
//
ID   D3Z656_MOUSE            Unreviewed;      1607 AA.
AC   D3Z656;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 11.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Synj1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC134560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC141885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00850983; -.
DR   RefSeq; NP_001157955.1; NM_001164483.1.
DR   UniGene; Mm.187079; -.
DR   Ensembl; ENSMUST00000121759; ENSMUSP00000113308; ENSMUSG00000022973.
DR   GeneID; 104015; -.
DR   KEGG; mmu:104015; -.
DR   CTD; 104015; -.
DR   MGI; MGI:1354961; Synj1.
DR   GeneTree; ENSGT00600000084387; -.
DR   OrthoDB; EOG4PNXG7; -.
DR   Bgee; D3Z656; -.
DR   GO; GO:0030118; C:clathrin coat; TAS:MGI.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IMP:MGI.
DR   GO; GO:0017120; F:polyphosphatidylinositol phosphatase activity; IMP:MGI.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0007612; P:learning; IMP:MGI.
DR   GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IMP:MGI.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:MGI.
DR   GO; GO:0016082; P:synaptic vesicle priming; IMP:MGI.
DR   GO; GO:0016191; P:synaptic vesicle uncoating; IMP:MGI.
DR   InterPro; IPR015047; DUF1866.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   InterPro; IPR000300; IPPc.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR002013; Syja_N.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF08952; DUF1866; 1.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   Pfam; PF02383; Syja_N; 1.
DR   SMART; SM00128; IPPc; 1.
DR   SUPFAM; SSF56219; Exo_endo_phos; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50275; SAC; 1.
PE   4: Predicted;
SQ   SEQUENCE   1607 AA;  176333 MW;  27C4E48E5E59E7F8 CRC64;
     MRKSWTCWSG SDASGGCSGG GCGRRRRRSR RKRAASEERR MAFSKGFRIY HKLDPPPFSL
     IVETRHKEEC LMFESGAVAV LSSAEKEAIK GTYAKVLDAY GLLGVLRLNL GDTMLHYLVL
     VTGCMSVGKI QESEVFRVTS TEFISLRVDA SDEDRISEVR KVLNSGNFYF AWSASGVSLD
     LSLNAHRSMQ EHTTDNRFFW NQSLHLHLKH YGVNCDDWLL RLMCGGVEIR TIYAAHKQAK
     ACLISRLSCE RAGTRFNVRG TNDDGHVANF VETEQVIYLD DCVSSFIQIR GSVPLFWEQP
     GLQVGSHRVR MSRGFEANAP AFDRHFRTLK DLYGKQIVVN LLGSKEGEHM LSKAFQSHLK
     ASEHASDIHM VSFDYHQMVK GGKAEKLHSI LKPQVQKFLD YGFFYFDGSE VQRCQSGTVR
     TNCLDCLDRT NSVQAFLGLE MLAKQLEALG LAEKPQLVTR FQEVFRSMWS VNGDSISKIY
     AGTGALEGKA KLKDGARSVT RTIQNNFFDS SKQEAIDVLL LGNTLNSDLA DKARALLTTG
     SLRVSEQTLQ SASSKVLKNM CENFYKYSKP KKIRVCVGTW NVNGGKQFRS IAFKNQTLTD
     WLLDAPKLAG IQEFQDKRSK PTDIFAIGFE EMVELNAGNI VNASTTNQKL WAVELQKTIS
     RDNKYVLLAS EQLVGVCLFV FIRPQHAPFI RDVAVDTVKT GMGGATGNKG AVAIRMLFHT
     TSLCFVCSHF AAGQSQVKER NEDFVEIARK LSFPMGRMLF SHDYVFWCGD FNYRIDLPNE
     EVKELIRQQN WDSLIAGDQL INQKNAGQIF RGFLEGKVTF APTYKYDLFS EDYDTSEKCR
     TPAWTDRVLW RRRKWPFDRS AEDLDLLNAS FQDESKILYT WTPGTLLHYG RAELKTSDHR
     PVVALIDIDI FEVEAEERQK IYKEVIAVQG PPDGTVLVSI KSSAQESTFF DDALIDELLR
     QFAHFGEVIL IRFVEDKMWV TFLEGSSALN ALSLNGKELL NRTITITLKS PDWIKHLEEE
     MSLEKISVTL PSSASSTLLG EDAEVAADFD MEGDVDDYSA EVEELLPQHL QPSSSSGLGT
     SPSSSPRTSP CQSPTVPEYS APSLPIRPSR APSRTPGPPS SQGSPVDTQP AAQKDSSQTL
     EPKRPPPPRP VAPPARPAPP QRPPPPSGAR SPAPARKEFG GVGAPPSPGV ARREIEAPKS
     PGTARKDNIG RNQPSPQAGL AGPGPAGYGA ARPTIPARAG VISAPQSQAR VCAGRPTPDS
     QSKPSETLKG PAVLPEPLKP QAAFPQQPSL PTPAQKLQDP LVPIAAPTMP PSGPQPNLET
     PPQPPPRSRS SQSLPSDSSP QLQVKINGIS GVKQEPTLKS DPFEDLSLSV LAVSKAQPSV
     QISPVLTPDP KMLIQLPSAS QSQVNPLSSV SCMPTRPPGP EESKSQESMG SSANPFPSLP
     CRNPFTDRTA APGNPFRVQS QESEATSWLS KEEPVPNSPF PPLMPLSHDT SKASSSLGGF
     EDNFDLQSQS TVKTSNPKGW VTFDEDDNFP TTGKSKSVCP DLVGNAPASF DDDWSKGASV
     SFCVLPARRP PPPPPPVPLL PPGTTSSAGP STTLPSKAPS TLDFTER
//
ID   D3Z6A2_MOUSE            Unreviewed;      1102 AA.
AC   D3Z6A2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 10.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Mical2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Contains 1 LIM zinc-binding domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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DR   EMBL; AC100153; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC132392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC166834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00555103; -.
DR   RefSeq; NP_001180234.1; NM_001193305.1.
DR   UniGene; Mm.52312; -.
DR   Ensembl; ENSMUST00000037991; ENSMUSP00000047639; ENSMUSG00000038244.
DR   Ensembl; ENSMUST00000106649; ENSMUSP00000102260; ENSMUSG00000038244.
DR   GeneID; 320878; -.
DR   KEGG; mmu:320878; -.
DR   CTD; 320878; -.
DR   MGI; MGI:2444947; Mical2.
DR   GeneTree; ENSGT00600000084263; -.
DR   Bgee; D3Z6A2; -.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:InterPro.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR002938; mOase_FAD-bd.
DR   InterPro; IPR003042; Rng_hydrolase-like.
DR   InterPro; IPR001781; Znf_LIM.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 1.
DR   Gene3D; G3DSA:2.10.110.10; Znf_LIM; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   Pfam; PF00412; LIM; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00132; LIM; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE   4: Predicted;
KW   LIM domain; Metal-binding; Zinc.
SQ   SEQUENCE   1102 AA;  124257 MW;  F87D341BF3BA9E46 CRC64;
     MGENEDEKQA QASQVFENFV QATTCKGTLQ AFNILTCLLD LDPLDHRNFY SQLKSKVNTW
     KAKALWHKLD KRGSHKEYKR GKACSNTKCL IVGGGPCGLR TAIELAYLGA KVVVVEKRDT
     FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGSIDHISIR QLQLILFKVA LMLGVEVHVN
     VEFVRVLEPP EDQENQKVGW RAEFLPADHA LSDFEFDVII GADGHRNTLE GFRRKEFRGK
     LAIAITANFI NRNSTAEAKV EEISGVAFIF NQKFFQDLKE ETGIDLENIV YYKDSTHYFV
     MTAKKQSLLD KGVILNDYID TEMLLCSENV NQDNLLSYAR EAADFATNYQ LPSLDFAINH
     NGQPDVAMFD FTSMYASENA ALMRERQAHQ LLVALVGDSL LEPFWPMGTG CARGFLAAFD
     TAWMVKSWDQ GTPPLEVLAE RESLYRLLPQ TTPENINKNF EQYTLDPATR YPNLNLHCVR
     PHQVKHLYIT KEMDRFPLER WGSVRRSVSL SRRESDIRPN KLLTWCQQQT KGYQHVRVTD
     LTTSWRSGLA LCAIIHSFRP ELINFDSLNE DDAVENNQLA FDVAKREFGI LPVTTGKEMA
     STQEPDKLSM VMYLSKFYEL FRGTPLRPMD SWRKNYGENA DFGLGKTFIQ NNYLNLTLPR
     KRTPRVDTQT EENDMNKRRR QGFNHLEELP SFSSRSLGSS QEYAKESGSQ NKVKHMANQL
     LAKFEENTRN PSVVKQDCRR VSGIGKPVLC SASRPPGTSC CPKLEESTPR LPPPLKRQFS
     STVATGQVLR ELNQVPASGE CPSRPWRARA KSDLQLGGVE NLATLPRTCQ GALALSGVLR
     RLQQVEEKVL QKRAQNLANR EFHTKNIKEK AAHLASMFGH GDLPQDKLLS KRVPHAHPPS
     PPSCLPSPHP AAASSPPAAD SVSPARKLTV GKVSSGIGAA AEVLVNLYLN DHRPKTQATS
     PDLESPRKAF PLSLGGRDTC YFCKKRVYMI ERLSAEGHFF HQECFRCSVC SATLRLAAYA
     FDCDEGKFYC KPHFVHCKTS SKQRKRRAEL NQQREEEGTW QEQEAPRRDV PTESSCAVAA
     ISTPEGSPPV RFSLPVLHPL LG
//
ID   D3Z6B9_MOUSE            Unreviewed;       810 AA.
AC   D3Z6B9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 10.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Aldh1l2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC113014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00858223; -.
DR   Ensembl; ENSMUST00000020497; ENSMUSP00000020497; ENSMUSG00000020256.
DR   Ensembl; ENSMUST00000146640; ENSMUSP00000117076; ENSMUSG00000020256.
DR   MGI; MGI:2444680; Aldh1l2.
DR   GeneTree; ENSGT00550000074289; -.
DR   Bgee; D3Z6B9; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0000036; F:acyl carrier activity; IEA:InterPro.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0016742; F:hydroxymethyl-, formyl- and related transferase activity; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:InterPro.
DR   InterPro; IPR009081; Acyl_carrier_prot-like.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR005793; Formyl_trans_C.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR011034; Formyl_transferase_C-like.
DR   InterPro; IPR001555; GART_AS.
DR   InterPro; IPR006163; Phsphopanteth-bd.
DR   InterPro; IPR006162; PPantetheine_attach_site.
DR   Gene3D; G3DSA:1.10.1200.10; ACP_like; 1.
DR   Gene3D; G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 1.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   Gene3D; G3DSA:3.10.25.10; Formyl_trans_C; 1.
DR   Gene3D; G3DSA:3.40.50.170; Formyl_transf_N; 1.
DR   PANTHER; PTHR11699; Aldehyde_dehyd; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   Pfam; PF02911; Formyl_trans_C; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF47336; ACP_like; 1.
DR   SUPFAM; SSF53720; Aldehyde_DH/Histidinol_DH; 1.
DR   SUPFAM; SSF50486; FMT_C_like; 1.
DR   SUPFAM; SSF53328; formyl_transf; 1.
DR   PROSITE; PS50075; ACP_DOMAIN; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
DR   PROSITE; PS00373; GART; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase; Phosphopantetheine.
SQ   SEQUENCE   810 AA;  88897 MW;  346A536ED236B549 CRC64;
     MDVIDSPKHG SIIYHPSLLP RHRGASAINW TLIMGDKKAG FSVFWADDGL DTGPILLQRS
     CDVKPNDTVD SLYNRFLFPE GIKAMVEAVQ LIADGKAPRT PQPEEGATYE GIQKKENAEV
     SWDQPAEGLH NWIRGHDKVP GAWAEINGQM VTFYGSSLLT SSVPSGEPLD IRGAKKPGLV
     TKNGLVLFGN DGKALMVRNL QFEDGKMIPA SQYFSAGETS VVELTAEELK VAETIKVIWA
     RILSNTPVIE DSTDFFKSGA SSMDVVRLVE EIRQSCGGLQ LQNEDVYMAT KFGDFIQKVV
     RRLRGEDEEA EMVVDYVSKE VNGMTVKIPY QCFINGQFVD AEDGETYATV NPTDGTTICR
     VSYASLADVD RAVAAAKDAF ENGEWGRMNA RDRGRLMYRL ADLMEENQEE LATIEALDSG
     AVYTLALKTH IGMSVQTFRY FAGWCDKIQG STIPINQARP NYNLTFTKKE PLGACAIIIP
     WNYPLMMLAW KSAACLAAGN TLVLKPAQVT PLTALKFAEL TVKAGFPKGV INIIPGSGGV
     AGQRLSQHPD IRKLGFTGST SVGKQIMKSC AVSNLKKVSL ELGGKSPLII FSDCDLEKAV
     RMGMGAVFFN KGENCIAAGR LFVEEAIHDE FVTRVVEEIK KMKIGDPLDR STDHGPQNHR
     AHLEKLLQYC ETGVQEGATL VYGGRQVQRP GFFMEPTVFT GVEDHMYLAK EESFGPIMVI
     SKFQNGDIDG VLQRANNTEY GLASGVFTRD INKAMYVSDK LEAGTVFINT YNKTDVAAPF
     GGMKQSGFGK DLGEEALNEY LKIKTVTLEY
//
ID   D3Z6E4_MOUSE            Unreviewed;       315 AA.
AC   D3Z6E4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   RecName: Full=Enolase;
DE            EC=4.2.1.11;
GN   Name=Eno2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate +
CC       H(2)O.
CC   -!- COFACTOR: Magnesium. Required for catalysis and for stabilizing
CC       the dimer (By similarity).
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5.
CC   -!- SIMILARITY: Belongs to the enolase family.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC164157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00122684; -.
DR   ProteinModelPortal; D3Z6E4; -.
DR   Ensembl; ENSMUST00000112476; ENSMUSP00000108095; ENSMUSG00000004267.
DR   MGI; MGI:95394; Eno2.
DR   Bgee; D3Z6E4; -.
DR   GO; GO:0043204; C:perikaryon; IDA:MGI.
DR   GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR   GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:InterPro.
DR   InterPro; IPR020810; Enolase_C.
DR   InterPro; IPR020809; Enolase_CS.
DR   InterPro; IPR020811; Enolase_N.
DR   Pfam; PF00113; Enolase_C; 1.
DR   Pfam; PF03952; Enolase_N; 1.
DR   PROSITE; PS00164; ENOLASE; 1.
PE   3: Inferred from homology;
KW   Glycolysis; Lyase; Magnesium.
SQ   SEQUENCE   315 AA;  34804 MW;  0574433E27EF74AB CRC64;
     MSIEKIWARE ILDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR DGDKQRYLGK
     GVLKAVDHIN SRIAPALISS GISVVEQEKL DNLMLELDGT ENKSLELVKE AIDKAGYTEK
     MVIGMDVAAS EFYRDGKYDL DFKSPADPSR YITGDQLGAL YQDFVRNYPV VSIEDPFDQD
     DWAAWSKFTA NVGIQIVGDD LTVTNPKRIE RAVEEKACNC LLLKVNQIGS VTEAIQACKL
     AQENGWGVMV SHRSGETEDT FIADLVVGLC TGQIKTGAPC RSERLAKYNQ LMRIEEELGD
     EARFAGHNFR NPSVL
//
ID   D3Z6G3_MOUSE            Unreviewed;       266 AA.
AC   D3Z6G3;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Mapre3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC109606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC109611; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00830432; -.
DR   Ensembl; ENSMUST00000114724; ENSMUSP00000110372; ENSMUSG00000029166.
DR   MGI; MGI:2140967; Mapre3.
DR   GeneTree; ENSGT00490000043329; -.
DR   Bgee; D3Z6G3; -.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR004953; EB1_C.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF03271; EB1; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS51230; EB1_C; 1.
PE   4: Predicted;
SQ   SEQUENCE   266 AA;  30364 MW;  8CDBB1C30A3F4D4A CRC64;
     MAVNVYSTSV TSENLSRHDM LAWVNDSLHL NYTKIEQLCS GAAYCQFMDM LFPGCVHLRK
     VKFQAKLEHE YIHNFKVLQA AFKKMGVDKI IPVEKLVKGK FQDNFEFIQW FKKFFDANYD
     GKDYNPLLAR QGQDVAPPPN PVPQRTSPTG PKNMQTSGRL SNVAPPCILR KNPPSARNGG
     HEADAQILEL NQQLLDLKLT VDGLEKERDF YFSKLRDIEL ICQEHESENS PVISGIIGIL
     YATEEGFAPP EDDEIEEHQQ EDQDEY
//
ID   D3Z6I8_MOUSE            Unreviewed;       247 AA.
AC   D3Z6I8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Tpm3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Belongs to the tropomyosin family.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC163616; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00880679; -.
DR   Ensembl; ENSMUST00000119158; ENSMUSP00000113219; ENSMUSG00000027940.
DR   MGI; MGI:1890149; Tpm3.
DR   GeneTree; ENSGT00550000074494; -.
DR   Bgee; D3Z6I8; -.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR   GO; GO:0030426; C:growth cone; IDA:MGI.
DR   GO; GO:0002102; C:podosome; IDA:MGI.
DR   InterPro; IPR000533; Tropomyosin.
DR   Pfam; PF00261; Tropomyosin; 1.
DR   PRINTS; PR00194; TROPOMYOSIN.
DR   PROSITE; PS00326; TROPOMYOSIN; 1.
PE   3: Inferred from homology;
KW   Coiled coil.
SQ   SEQUENCE   247 AA;  28723 MW;  839796CC5575BC35 CRC64;
     MAGTTTIEAV KRKIQVLQQQ ADDAEERAER LQREVEGERR AREQAEAEVA SLNRRIQLVE
     EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRALK DEEKMELQEI QLKEAKHIAE
     EADRKYEEVA RKLVIIEGDL ERTEERAELA ESKCSELEEE LKNVTNNLKS LEAQAEKYSQ
     KEDKYEEEIK ILTDKLKEAE TRAEFAERSV AKLEKTIDDL EERLYSQLER NRLLSNELKL
     TLHGLCD
//
ID   D3Z6K2_MOUSE            Unreviewed;       282 AA.
AC   D3Z6K2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Mctp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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DR   EMBL; AC112671; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC124362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC140345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC161266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CAAA01191699; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CAAA01210796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00652565; -.
DR   Ensembl; ENSMUST00000099361; ENSMUSP00000096962; ENSMUSG00000021596.
DR   Ensembl; ENSMUST00000126960; ENSMUSP00000120673; ENSMUSG00000021596.
DR   MGI; MGI:1926021; Mctp1.
DR   GeneTree; ENSGT00550000074417; -.
DR   Bgee; D3Z6K2; -.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   Pfam; PF00168; C2; 2.
DR   PRINTS; PR00360; C2DOMAIN.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 2.
PE   4: Predicted;
KW   Repeat.
SQ   SEQUENCE   282 AA;  32409 MW;  0CBD47FDE85AB4EF CRC64;
     MYQLDITLRR GQSLAARDRG GTSDPYVKFK IGRKEVFRSK IIHKNLNPVW EEKACVLIDH
     LREPLYIKVF DYDFGLQDDF MGSAFLDLTQ LELNRSTDVT LTLKDPHYPD HDLGIILLSV
     ILTPKEGEHR DVFQTQSLRL SDQHRKSHLW RGIVSITLIE GRDLKAMDSN GLSDPYVKFR
     LGHQKYKSKI MPKTLNPQWR EQFDFHLYEE RGGIMDITAW DKDAGKRDDF IGSSSPVFHP
     GCSHEPHFLK NLYVFLYHQG VRDPSAYGSL GVLISPVTAP PG
//
ID   D3Z6Q0_MOUSE            Unreviewed;       867 AA.
AC   D3Z6Q0;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Dnm1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the dynamin family.
CC   -!- SIMILARITY: Contains 1 GED domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; AL808027; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00890133; -.
DR   Ensembl; ENSMUST00000113354; ENSMUSP00000108981; ENSMUSG00000026825.
DR   MGI; MGI:107384; Dnm1.
DR   GeneTree; ENSGT00600000084144; -.
DR   Bgee; D3Z6Q0; -.
DR   GO; GO:0030117; C:membrane coat; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR022812; Dynamin.
DR   InterPro; IPR000375; Dynamin_central.
DR   InterPro; IPR001401; Dynamin_GTPase.
DR   InterPro; IPR019762; Dynamin_GTPase_CS.
DR   InterPro; IPR003130; GED.
DR   InterPro; IPR020850; GTPase_effector_domain_GED.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Pfam; PF01031; Dynamin_M; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   Pfam; PF02212; GED; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00195; DYNAMIN.
DR   SMART; SM00053; DYNc; 1.
DR   SMART; SM00302; GED; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS00410; DYNAMIN; 1.
DR   PROSITE; PS51388; GED; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Nucleotide-binding.
SQ   SEQUENCE   867 AA;  97673 MW;  659BFF5394E5BDF6 CRC64;
     MGNRGMEDLI PLVNRLQDAF SAIGQNADLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
     SGIVTRRPLV LQLVNSTTEY AEFLHCKGKK FTDFEEVRLE IEAETDRVTG TNKGISPVPI
     NLRVYSPHVL NLTLVDLPGM TKVPVGDQPP DIEFQIRDML MQFVTKENCL ILAVSPANSD
     LANSDALKIA KEVDPQGQRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK
     DIDGKKDITA ALAAERKFFL SHPSYRHLAD RMGTPYLQKV LNQQLTNHIR DTLPGLRNKL
     QSQLLSIEKE VDEYKNFRPD DPARKTKALL QMVQQFAVDF EKRIEGSGDQ IDTYELSGGA
     RINRIFHERF PFELVKMEFD EKELRREISY AIKNIHGIRT GLFTPDLAFE ATVKKQVQKL
     KEPSIKCVDM VVSELTSTIR KCSEKLQQYP RLREEMERIV TTHIREREGR TKEQVMLLID
     IELAYMNTNH EDFIGFANAQ QRSNQMNKKK TSGNQDEILV IRKGWLTINN IGIMKGGSKE
     YWFVLTAENL SWYKDDEEKE KKYMLSVDNL KLRDVEKGFM SSKHIFALFN TEQRNVYKDY
     RQLELACETQ EEVDSWKASF LRAGVYPERV GDKEKASETE ENGSDSFMHS MDPQLERQVE
     TIRNLVDSYM AIVNKTVRDL MPKTIMHLMI NNTKEFIFSE LLANLYSCGD QNTLMEESAE
     QAQRRDEMLR MYHALKEALS IIGDINTTTV STPMPPPVDD SWLQVQSVPA GRRSPTSSPT
     PQRRAPAVPP ARPGSRGPAP GPPPAGSALG GAPPVPSRPG ASPDPFGPPP QVPSRPNRAP
     PGVPSLGAWR LNSPQGKHEN RAGKARL
//
ID   D3Z6Q9_MOUSE            Unreviewed;       489 AA.
AC   D3Z6Q9;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Bin2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC123724; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00752684; -.
DR   ProteinModelPortal; D3Z6Q9; -.
DR   Ensembl; ENSMUST00000100198; ENSMUSP00000097772; ENSMUSG00000075411.
DR   MGI; MGI:3611448; Bin2.
DR   GeneTree; ENSGT00390000017588; -.
DR   OrthoDB; EOG45HRXJ; -.
DR   Bgee; D3Z6Q9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   InterPro; IPR003005; Amphiphysin.
DR   InterPro; IPR004148; BAR.
DR   Pfam; PF03114; BAR; 1.
DR   PRINTS; PR01251; AMPHIPHYSIN.
DR   SMART; SM00721; BAR; 1.
DR   PROSITE; PS51021; BAR; 1.
PE   4: Predicted;
SQ   SEQUENCE   489 AA;  52554 MW;  8E207C53B1D31A99 CRC64;
     MAEGKAGGAA GLFAKQMQKK FSRAQEKVLQ KLGKTVETKD ERFEQSASNF YQQQAEGHKL
     YKDLKNFLSA VKVMHESSKR VSETLQEVYS SDWDGHEDLK AIVGNNDLLW EDYEEKLADQ
     ALRTMENYVS QFSEIKERIA KRGRKLVDYD SARHHLEAVQ NAKKKDDAKM AKAEEDFSKA
     QIVFEDLNQE LLEELPILYN SRIGCYVTVF QNISNLRDVF YREMSKLNHN LYEVMSKLEK
     QHSNKVFVVK GLSSSSRRSL VISPPVQSCA ASSPVSPVSP VSPVTSPTSP SATSEPESVS
     ATGEELTSEA GGEDSCESQE SLKDEEADEA QSETSSSLPA CNGPTPAPAS PAAEVGSQEE
     ALSSSAQSPG RGQTGKDTPS PGDVVLRARA SSEGAEQSKR AASIQRTSAP PSRPPPPRAS
     GSGSCNAPGS PEGSSQLCSP RASPDASSNP EPAETREKEG AGSSGPEEPR AVSTKSATQA
     SGGLVGLFL
//
ID   D3Z6U8_MOUSE            Unreviewed;       591 AA.
AC   D3Z6U8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Fmr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Contains 2 KH domains.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC055766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00776121; -.
DR   Ensembl; ENSMUST00000114656; ENSMUSP00000110304; ENSMUSG00000000838.
DR   MGI; MGI:95564; Fmr1.
DR   GeneTree; ENSGT00390000017033; -.
DR   Bgee; D3Z6U8; -.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0007417; P:central nervous system development; IMP:MGI.
DR   InterPro; IPR008395; Agenet.
DR   InterPro; IPR022034; FXR1P_C.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR004088; KH_type_1.
DR   InterPro; IPR018111; KH_type_1_subgr.
DR   Pfam; PF05641; Agenet; 1.
DR   Pfam; PF12235; FXR1P_C; 1.
DR   Pfam; PF00013; KH_1; 1.
DR   SMART; SM00322; KH; 2.
DR   PROSITE; PS50084; KH_TYPE_1; 2.
PE   4: Predicted;
SQ   SEQUENCE   591 AA;  66532 MW;  2D9FB4BAE366B738 CRC64;
     MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPER QIPFHDVRFP PPVGYNKDIN
     ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD ATYNEIVTIE RLRSVNPNKP
     ATKDTFHKIK LEVPEDLRQM CAKESAHKDF KKAVGAFSVT YDPENYQLVI LSINEVTSKR
     AHMLIDMHFR SLRTKLSLIL RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN
     IQQARKVPGV TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVVIGKNGK
     LIQEIVDKSG VVRVRIEAEN EKSVPQEEEI MPPSSLPSNN SRVGPNSSEE KKHLDTKENT
     HFSQPNSTKV QRGMVPFVFV GTKDSIANAT VLLDYHLNYL KEVDQLRLER LQIDEQLRQI
     GASSRPPPNR TDKEKGYVTD DGQGMGRGSR PYRNRGHGRR GPGYTSGTNS EASNASETES
     DHRDELSDWS LAPTEEERES FLRRGDGRRR GGGGRGQGGR GRGGGFKGND DHSRTDNRPR
     NPREAKGRTA DGSLQSASSE GSRLRTGKDR NQKKEKPDSV DGLQPLVNGV P
//
ID   D3Z6Z0_MOUSE            Unreviewed;       140 AA.
AC   D3Z6Z0;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Snx3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC125267; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC168273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00857621; -.
DR   ProteinModelPortal; D3Z6Z0; -.
DR   Ensembl; ENSMUST00000105500; ENSMUSP00000101139; ENSMUSG00000019804.
DR   MGI; MGI:1860188; Snx3.
DR   GeneTree; ENSGT00600000084448; -.
DR   Bgee; D3Z6Z0; -.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   InterPro; IPR001683; Phox.
DR   Gene3D; G3DSA:3.30.1520.10; PX; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; PX; 1.
DR   PROSITE; PS50195; PX; 1.
PE   4: Predicted;
SQ   SEQUENCE   140 AA;  16316 MW;  01710ACF7D256DCA CRC64;
     MAETVADTRR LITKPQNLND AYGPPSNFLE IDTNLPIFKL KESTVRRRYS DFEWLRSELE
     RESKVVVPPL PGKAFLRQLP FRGDDGIFDD NFIEERKQGL EQFINKVAGH PLAQNERCLH
     MFLQDEIIDK SYTPSKIRHA
//
ID   D3Z709_MOUSE            Unreviewed;       944 AA.
AC   D3Z709;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Dlgap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; AC079441; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154604; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154769; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC163902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC165424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC168117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00473783; -.
DR   Ensembl; ENSMUST00000146730; ENSMUSP00000116072; ENSMUSG00000003279.
DR   MGI; MGI:1346065; Dlgap1.
DR   GeneTree; ENSGT00550000074473; -.
DR   Bgee; D3Z709; -.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0007268; P:synaptic transmission; TAS:MGI.
DR   InterPro; IPR005026; GKAP.
DR   Pfam; PF03359; GKAP; 1.
PE   4: Predicted;
SQ   SEQUENCE   944 AA;  105048 MW;  2AE01B7710B90D30 CRC64;
     MKGLSGSRSH HHGITCEAAC DSLSHHSDHK PYLLSPVDHH PADHPYYTQR NSFQAECVGP
     FSDPLASSTF PRRHYTSQQE LKDESALVPR TLATKANRLP TNLLDQFERQ LPLSRDGYHT
     LQYKRTAVEH RSDSPGRIRH LVHSVQKLFT KSHSLEGPSK GSVNGGKASP DESQTLRYGK
     RSKSKERRSE SKARSNASNA SPTSPSWWSS DDNLDGDMCL YHTPSGVMTM GRCPDRSASQ
     YFMEAYNTIS EQAVKASRSN NDIKCSTCAN LPVTLDAPLL KKSAWSSTLT VSRAREVYQK
     ASVNMDQAMV KSEACQQERS CQYLQVPQDE WSGYTPRGKD DEIPCRRMRS GSYIKAMGDE
     DSGDSDTSPK PSPKVAARRE SYLKATQPSL TELTTLKISN EHSPKLQIRS HSYLRAVSEV
     SINRSLDSLD PAGLLTSPKF RSRNESYMRA MSTISQVSEM EVNGQFESVC ESVFSELESQ
     AVEALDLPLP GCFRMRSHSY VRAIEKGCSQ DDECVSLRSS SPPRTTTTVR TIQSSTGVIK
     LSSAVEVSSC ITTYKKTPPP VPPRTTTKPF ISITAQSSTE SAQDAYMDGQ GQRGDMISQS
     GLSNSTESLD SMKALTAAIE AANAQIHGPA SQHMGSNAAA VTTTTTIATV TTEDRKKDFK
     KNRCLSIGIQ VDDAEEPEKM AESKTSNKFQ SVGVQVEEEK CFRRFTRSNS VTTAVQADLD
     FHDNLENSLE SIEDNSCPGP MARQFSRDAS TSTVSIQGSG NHYHACAADD DFDTDFDPSI
     LPPPDPWIDS ITEDPLEAVQ RSVCHRDGHW FLKLLQAERD RMEGWCKLME REERENNLPE
     DILGKIRTAV GSAQLLMAQK FYQFRELCEE NLNPNAHPRP TSQDLAGFWD MLQLSIENIS
     MKFDELHQLK ANNWKQMDPL DKKVEQCRFC MVHLKPCTNA GQSK
//
ID   D3Z749_MOUSE            Unreviewed;       324 AA.
AC   D3Z749;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Cd47;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC107830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC158166; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00875877; -.
DR   Ensembl; ENSMUST00000023320; ENSMUSP00000023320; ENSMUSG00000055447.
DR   MGI; MGI:96617; Cd47.
DR   GeneTree; ENSGT00390000007697; -.
DR   Bgee; D3Z749; -.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:MGI.
DR   GO; GO:0005887; C:integral to plasma membrane; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0008228; P:opsonization; IDA:MGI.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; IMP:MGI.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; IDA:MGI.
DR   GO; GO:0009617; P:response to bacterium; IMP:MGI.
DR   InterPro; IPR006704; CD47.
DR   InterPro; IPR013147; CD47_TM.
DR   InterPro; IPR013270; CD47_Vset.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   PANTHER; PTHR10613; CD47; 1.
DR   Pfam; PF04549; CD47; 1.
DR   Pfam; PF08204; V-set_CD47; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   4: Predicted;
SQ   SEQUENCE   324 AA;  35290 MW;  F6558B75543BBF17 CRC64;
     MWPLAAALLL GSCCCGSAQL LFSNVNSIEF TSCNETVVIP CIVRNVEAQS TEEMFVKWKL
     NKSYIFIYDG NKNSTTTDQN FTSAKISVSD LINGIASLKM DKRDAMVGNY TCEVTELSRE
     GKTVIELKNR TAFNTDQGSA CSYEEEKGGC KLVSWFSPNE KILIVIFPIL AILLFWGKFG
     ILTLKYKSSH TNKRIILLLV AGLVLTVIVV VGAILLIPGE KPVKNASGLG LIVISTGILI
     LLQYNVFMTA FGMTSFTIAI LITQVLGYVL ALVGLCLCIM ACEPVHGPLL ISGLGIIALA
     ELLGLVYMKF VASNQRTIQP PRSR
//
ID   D3Z7E5_MOUSE            Unreviewed;       486 AA.
AC   D3Z7E5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 10.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Gsk3a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC156992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00830754; -.
DR   Ensembl; ENSMUST00000108411; ENSMUSP00000104049; ENSMUSG00000057177.
DR   MGI; MGI:2152453; Gsk3a.
DR   GeneTree; ENSGT00520000055635; -.
DR   Bgee; D3Z7E5; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
DR   GO; GO:0016477; P:cell migration; IGI:MGI.
DR   GO; GO:0071285; P:cellular response to lithium ion; IDA:MGI.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:MGI.
DR   GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding; Nucleotide-binding.
SQ   SEQUENCE   486 AA;  51246 MW;  0B6BB07F3243C57C CRC64;
     MSGGGPSGGG PGGSGRARTS SFAEPGGGGG GGGGGPGGSA SGPGGTGGGK ASVGAMGGGV
     GASSSGGGPS GSGGGGSGGP GAGTSFPPPG VKLGRDSGKV TTVVATVGQG PERSQEVAYT
     DIKVIGNGSF GVVYQARLAE TRELVAIKKV LQDKRFKNRE LQIMRKLDHC NIVRLRYFFY
     SSGEKKDELY LNLVLEYVPE TVYRVARHFT KAKLITPIIY IKVYMYQLFR SLAYIHSQGV
     CHRDIKPQNL LVDPDTAVLK LCDFGSAKQL VRGEPNVSYI CSRYYRAPEL IFGATDYTSS
     IDVWSAGCVL AELLLGQPIF PGDSGVDQLV EIIKVLGTPT REQIREMNPN YTEFKFPQIK
     AHPWTKVFKS SKTPPEAIAL CSSLLEYTPS SRLSPLEACA HSFFDELRRL GAQLPNDRPL
     PPLFNFSPGE LSIQPSLNAI LIPPHLRSPA GPASPLTTSY NPSSQAQTGQ DWQPSDATTA
     TLASSS
//
ID   D3Z7H4_MOUSE            Unreviewed;       177 AA.
AC   D3Z7H4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Gsg1l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC012297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC150648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00622555; -.
DR   Ensembl; ENSMUST00000073935; ENSMUSP00000073591; ENSMUSG00000046182.
DR   MGI; MGI:2685483; Gsg1l.
DR   GeneTree; ENSGT00390000011933; -.
DR   OrthoDB; EOG42822J; -.
DR   Bgee; D3Z7H4; -.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   Pfam; PF00822; PMP22_Claudin; 1.
PE   4: Predicted;
KW   Membrane; Transmembrane.
SQ   SEQUENCE   177 AA;  20539 MW;  84A7425D91016043 CRC64;
     MCLELVHSSS VIDGLKLNAF AAVFTVLSGL LGMVAHMMYT QVFQVTVSLG PEDWRPHSWD
     YGWSFCLAWG SFTCCMAASV TTLNSYTKTV IEFRHKRKVF EQGYREEPTF IDPEAIKYFR
     ERIEKGDVSE EEDFRLACRH ERYPTRHQPH MGDSWPRSSA HEAAELNRQC WVLGHWV
//
ID   D3Z7I0_MOUSE            Unreviewed;       950 AA.
AC   D3Z7I0;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 6.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Gtf3c2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC109608; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC114619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00830153; -.
DR   Ensembl; ENSMUST00000043161; ENSMUSP00000047210; ENSMUSG00000029144.
DR   MGI; MGI:1919002; Gtf3c2.
DR   GeneTree; ENSGT00390000018632; -.
DR   Bgee; D3Z7I0; -.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
DR   Pfam; PF00400; WD40; 2.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   4: Predicted;
KW   Repeat; WD repeat.
SQ   SEQUENCE   950 AA;  104719 MW;  95D2788E6F4DD73D CRC64;
     MDTCGVGYVA LGEADPVGSM IVVDSPGQEE LSQLDVKASE TSGVEASIEM SLPPPLPGFE
     DSSDRRLPPD QESLTRLEQQ DLSSEMSKVS NTRASKPSGR RGGRTARGAK RPQQRKPPST
     PLVPGLLDQS NPLSTPMPKK RSQKSKGDLL LLKLSKGLDQ PESPHPKRPP EDFETPSGER
     PRRRAAQVVS LPNPGWPRTC DPPTSASRVL GLQACATTPG SPSHFSQTSP RALLYLQELA
     EELSTALPAP PLSGPKSPKV SSPTKPKKTR QASSQGEEDG SARDEDFVLQ VEGEDEEESE
     APSENSSDPE PVAPRSTPRG PAAGKQKPHC RGMAPNGLPN YIMAPVWKCL HLTKDLREQH
     HSFWEFAEWI PVAWKWQLLS ELEAAPYLPQ EEKSPLFSVQ REGIPEDGTI YRINRFSSIT
     AHPERWDVSF FTGGPLWALD WCPVPEGSAA SQYVALFSSP DMNETHPLSQ LHSGPGLLQL
     WGLGTLQQES CPGNRAHFVY GIACDSGCIW DLKFCPSGAW EHPETLRKAP LLPRLGLLAL
     ACSDGKVLLF SLPHPEALLA QQPPDAMKPA IYKVQCLATL QVGSVQASDP SECGQCLSLA
     WMPTRPHHHL AAGYYNGMVV FWNLPTNSPL QRIRLSDGSL KLYPFQCFLA HDQAVRTIQW
     CKANSHFLVS AGSDRKIKFW DLRRPYEPIN CIKRFLSTEL SWLLPYNGVT VAQDNCYASY
     GLCGIHYIDA GYLGFKAYFT APRKGTVWSL SGSDWLGTVA AGDISGELIA AILPDMASNP
     INVKKPAERR FPIYKADLIP YQDSPEDQDY SSTSSETPNP PKARTYTETI NHHYLLFQDT
     DLSSFHNLLR REPMLRMQEG EGHSQLCLDR LQLEAIHKVR FSPNLDSYGW LVSGGQSGLV
     RIHFVRGLTS PLAHRVQLES RANFNAMFQP SFPTEGPGFS PSSHCLLPNP
//
ID   D3Z7K6_MOUSE            Unreviewed;       716 AA.
AC   D3Z7K6;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Neuronal tyrosine phosphorylated adaptor for phosphoinositide 3-kinase adaptor 2;
DE   SubName: Full=Uncharacterized protein;
GN   Name=9430031J16Rik; Synonyms=NYAP2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RA   Yokoyama K., Yamamoto T.;
RT   "NYAP family proteins conect neuronal tyrosine kinases to
RT   phosphoinositide 3-kinase activation.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC116105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC131336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC163450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB429290; BAJ19139.1; -; mRNA.
DR   IPI; IPI00957079; -.
DR   Ensembl; ENSMUST00000123285; ENSMUSP00000122935; ENSMUSG00000054976.
DR   MGI; MGI:2443135; 9430031J16Rik.
DR   GeneTree; ENSGT00450000040316; -.
DR   Bgee; D3Z7K6; -.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Kinase; Transferase.
SQ   SEQUENCE   716 AA;  78311 MW;  9F4D64E148AED28C CRC64;
     MIPSKMMSAN PEEDPLDTFF QYIEDMGMKA YDGLVIQNAS DIARENDRLR NETNLAYLKE
     KNEKRRRQEE TIKRIGGEVG RGQDASYAGK HFRMGFMTMP APQDRLPHPC SSGFTVRSQS
     LHSVGGTEDD SSCGSRRQPP PKPKRDPSTK LSTSSETVNS TAASKSGRSL ERAEVSAKPR
     PHSDEYSKKI PPPKPKRNPN TQLSTSFDET YIKKHVPRRT SLPRDSSLSQ VCSPAADPEE
     EEPVYIEMVG NILRDFRKEE DDQSEAVYEE MKYPIFDDLG HDSKCDFDHH SCSSQCATPT
     VPDLDFVKSS GPCTPKGLLC DIPPPFPNLL SHRPPLLVFP PAPVHCSPNS DESPLTPLEV
     TKLPVLENVS YMKQPPGACP SSLPSHGSSH AKDQTGALGP APGASILSSS PPPPSTLYRT
     QSPHGYPKSH STSPSPVSMG RSLTPLSLKR PPPYDAVHSG SLSRSSSSVP HTTPRPVSQD
     GAKMVNAAVN TYSAAQSGSR SRTPTSPLEE LTSLFTSGRS LLRKSSSGRR SKEPAEKSTE
     ELKVRSHSTE PLPKLDSKER GHYGSSSSRE PVKAQEWDGT PGPPVVTSRM GRCSVSPTLL
     AGNHSSEPKV SCKLGRSAST SGVPPPSVTP LRQASDLQQS QVACMQWFHG DHTMLEMIEK
     KRCLCKEIKA RQKTEKGLCK QDSMPILPSW KKNAGAKKYS PPPYSKQQTV FWDTAI
//
ID   D3Z7L6_MOUSE            Unreviewed;       338 AA.
AC   D3Z7L6;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 7.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Prrt2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC122863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00281761; -.
DR   ProteinModelPortal; D3Z7L6; -.
DR   Ensembl; ENSMUST00000060178; ENSMUSP00000052727; ENSMUSG00000045114.
DR   MGI; MGI:1916267; Prrt2.
DR   GeneTree; ENSGT00530000063980; -.
DR   OrthoDB; EOG4HHP3X; -.
DR   Bgee; D3Z7L6; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0009607; P:response to biotic stimulus; IEA:InterPro.
DR   InterPro; IPR007593; Interferon-induced_TM_protein.
DR   Pfam; PF04505; CD225; 1.
PE   4: Predicted;
SQ   SEQUENCE   338 AA;  35155 MW;  2B8B3843B93522A5 CRC64;
     MAASSSQVSE MKGVEDSSKT QTEGPRHSEE GLGPVQVVAE IPDQPEALQP GPGITAAPVD
     SGPKAELAPE TTETPVETPE TVQATDLSLN PEEGSKARQE PASKPDVNRE TAAEEGSEPQ
     STAPPEPTSE PAFQINTQSD PQPTSQPPPK PPLQAEPPTQ EDPTTEVLTE STGEKQENGA
     VVPLQAGDGE EGPAPQPHSP PSTKTPPANG APPRVLQKLV EEDRIGRAHG GHPGSPRGSL
     SRHPSSQLAG PGVEGGEGTQ KPRDYIILAI LSCFCPMWPV NIVAFAYAVM SRNSLQQGDV
     DGAQRLGRVA KLLSIVALVG GVLIIIASCV INLGAVYK
//
ID   D3Z7N2_MOUSE            Unreviewed;       129 AA.
AC   D3Z7N2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 6.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Eef1d;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC116520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00831299; -.
DR   Ensembl; ENSMUST00000109972; ENSMUSP00000105599; ENSMUSG00000055762.
DR   Ensembl; ENSMUST00000116440; ENSMUSP00000112141; ENSMUSG00000055762.
DR   Ensembl; ENSMUST00000123712; ENSMUSP00000122155; ENSMUSG00000055762.
DR   Ensembl; ENSMUST00000137426; ENSMUSP00000114753; ENSMUSG00000055762.
DR   MGI; MGI:1913906; Eef1d.
DR   GeneTree; ENSGT00390000011747; -.
DR   Bgee; D3Z7N2; -.
PE   4: Predicted;
SQ   SEQUENCE   129 AA;  14182 MW;  309838C7DD07B0D1 CRC64;
     MATNFLAHEK IWFDKFKYDD AERRFYEQMN GPVTSGSRQS SGPGASSGPG GDHSELIVRI
     TSLEVENQNL RGVVQDLQQA ISKLEARLSS LEKSSPTPRA TAPQTQHVSP MRQVEPPTKK
     GATPAEDDE
//
ID   D3Z7P3_MOUSE            Unreviewed;       674 AA.
AC   D3Z7P3;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 11.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Gls;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC123752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00464317; -.
DR   RefSeq; NP_001074550.1; NM_001081081.2.
DR   UniGene; Mm.440465; -.
DR   Ensembl; ENSMUST00000114513; ENSMUSP00000110158; ENSMUSG00000026103.
DR   GeneID; 14660; -.
DR   KEGG; mmu:14660; -.
DR   CTD; 14660; -.
DR   MGI; MGI:95752; Gls.
DR   Bgee; D3Z7P3; -.
DR   GO; GO:0004359; F:glutaminase activity; IMP:MGI.
DR   GO; GO:0007610; P:behavior; IMP:MGI.
DR   GO; GO:0006543; P:glutamine catabolic process; IMP:MGI.
DR   GO; GO:0002087; P:regulation of respiratory gaseous exchange by neurological system process; IMP:MGI.
DR   GO; GO:0007268; P:synaptic transmission; IMP:MGI.
DR   HAMAP; MF_00313; Glutaminase; 1; -.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR012338; B-lactamase-typ_transpept_fold.
DR   InterPro; IPR015868; Glutaminase.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Gene3D; G3DSA:3.40.710.20; Glutaminase_core; 2.
DR   PANTHER; PTHR12544; Glutaminase; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF04960; Glutaminase; 1.
DR   SMART; SM00248; ANK; 2.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF56601; PBP_transp_fold; 1.
DR   TIGRFAMs; TIGR03814; Gln_ase; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
PE   3: Inferred from homology;
KW   ANK repeat; Repeat.
SQ   SEQUENCE   674 AA;  73964 MW;  C46824C83E1D9639 CRC64;
     MMRLRGSAML RELLLRPPAA VGAVLRRAQP LGTLCRRPRG GSRPTAGLVA AARLHPWWGG
     GGRAKGPGAG GLSSSPSEIL QELGKGGTPP QQQQQQQQQP GASPPAAPGP KDSPGETDAF
     GNSEGKEMVA AGDNKIKQGL LPSLEDLLFY TIAEGQEKIP VHKFITALKS TGLRTSDPRL
     KECMDMLRLT LQTTSDGVML DKDLFKKCVQ SNIVLLTQAF RRKFVIPDFM SFTSHIDELY
     ESAKKQSGGK VADYIPQLAK FSPDLWGVSV CTVDGQRHSI GDTKVPFCLQ SCVKPLKYAI
     AVNDLGTEYV HRYVGKEPSG LRFNKLFLNE DDKPHNPMVN AGAIVVTSLI KQGVNNAEKF
     DYVMQFLNKM AGNEYVGFSN ATFQSERESG DRNFAIGYYL KEKKCFPEGT DMVGILDFYF
     QLCSIEVTCE SASVMAATLA NGGFCPITGE RVLSPEAVRN TLSLMHSCGM YDFSGQFAFH
     VGLPAKSGVA GGILLVVPNV MGMMCWSPPL DKMGNSVKGI HFCHDLVSLC NFHNYDNLRH
     FAKKLDPRRE GGDQRVKSVI NLLFAAYTGD VSALRRFALS AMDMEQRDYD SRTALHVAAA
     EGHVEVVKFL LEACKVNPFP KDRWNNTPMD EALHFGHHDV FKILQEYQVQ YTPQGDSDDG
     KGNQTVHKNL DGLL
//
ID   D3Z7R4_MOUSE            Unreviewed;       236 AA.
AC   D3Z7R4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 8.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Syt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
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CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; AC117199; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC122472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC124436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC141899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC162908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC163645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00750142; -.
DR   Ensembl; ENSMUST00000156979; ENSMUSP00000116981; ENSMUSG00000035864.
DR   MGI; MGI:99667; Syt1.
DR   GeneTree; ENSGT00600000084008; -.
DR   Bgee; D3Z7R4; -.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:MGI.
DR   GO; GO:0030141; C:stored secretory granule; IDA:MGI.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; TAS:MGI.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   GO; GO:0007269; P:neurotransmitter secretion; IDA:MGI.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   InterPro; IPR001565; Synaptotagmin.
DR   Pfam; PF00168; C2; 1.
DR   PRINTS; PR00360; C2DOMAIN.
DR   PRINTS; PR00399; SYNAPTOTAGMN.
DR   SMART; SM00239; C2; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   PROSITE; PS50004; C2; 1.
PE   4: Predicted;
KW   Repeat.
SQ   SEQUENCE   236 AA;  26295 MW;  27F1757486424132 CRC64;
     MVSASRPEAL AAPVTTVATL VPHNATEPAS PGEGKEDAFS KLKQKFMNEL HKIPLPPWAL
     IAIAIVAVLL VVTCCFCVCK KCLFKKKNKK KGKEKGGKNA INMKDVKDLG KTMKDQDDDA
     ETGLTDGEEK EEPKEEEKLG KLQYSLDYDF QNNQLLVGII QAAELPALDM GGTSDPYVKV
     FLLPDKKKKF ETKVHRKTLN PVFNEQFTFK VPYSELGGKT LVMAVYDFDR FSKHDI
//
ID   D3Z7T0_MOUSE            Unreviewed;       301 AA.
AC   D3Z7T0;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 6.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Speg;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC114651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC161346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00856928; -.
DR   Ensembl; ENSMUST00000148515; ENSMUSP00000116953; ENSMUSG00000026207.
DR   MGI; MGI:109282; Speg.
DR   GeneTree; ENSGT00600000084221; -.
DR   Bgee; D3Z7T0; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR020675; Myosin_light_chain_kin-rel.
DR   InterPro; IPR015726; Ser/Thr_kin_striated_muscle-sp.
DR   PANTHER; PTHR22964; Myosin_light_chain_kin-rel; 1.
DR   PANTHER; PTHR22964:SF9; Ser/Thr_kinase_striated_musc; 1.
PE   4: Predicted;
SQ   SEQUENCE   301 AA;  32535 MW;  DE199A385304D946 CRC64;
     MKKLWVKKRF QKTGHSRRAF GRLTHVFRSC RKQSYDSETA EDDISDVPGT QRLELRDDRA
     FSTPTGGSDT LVGTSLDTPP TSVTGTSEEQ VSWWGSGQTV LEQEAGSGGG TRPLPGSPSS
     IPPSGLHREE PDLQPQPASD ALRPRPALPP PSKSALLPPP SPRVGKRALP GPSTQPPATP
     TSPHRRAQEP SLPEDITTTE EKRGKKPKSS GPSLAGTVES RPQTPLSEAS GRLSALGRSP
     RLVRAGSRIL DKLQFFEERR RSLERSDSPP APLRPWVPLR KARSLEQPKS EGGAAWGTPE
     A
//
ID   D3Z7U4_MOUSE            Unreviewed;       189 AA.
AC   D3Z7U4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAR-2011, entry version 10.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Mecp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL672002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00928332; -.
DR   Ensembl; ENSMUST00000140399; ENSMUSP00000119947; ENSMUSG00000031393.
DR   MGI; MGI:99918; Mecp2.
DR   GeneTree; ENSGT00530000063687; -.
DR   OrthoDB; EOG40VVQ3; -.
DR   Bgee; D3Z7U4; -.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
DR   InterPro; IPR016177; DNA-bd_integrase-typ.
DR   InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR   Gene3D; G3DSA:3.30.890.10; Methyl_CpG_DNA-bd; 1.
DR   Pfam; PF01429; MBD; 1.
DR   SMART; SM00391; MBD; 1.
DR   SUPFAM; SSF54171; DNA-binding_integrase-type; 1.
DR   PROSITE; PS50982; MBD; 1.
PE   4: Predicted;
SQ   SEQUENCE   189 AA;  20331 MW;  1AC530F7F43A8535 CRC64;
     MAAAAATAAA AAAPSGGGGG GEEERLEEKS EDQDLQGLRD KPLKFKKAKK DKKEDKEGKH
     EPLQPSAHHS AEPAEAGKAE TSESSGSAPA VPEASASPKQ RRSIIRDRGP MYDDPTLPEG
     WTRKLKQRKS GRSAGKYDVY LINPQGKAFR SKVELIAYFE KLQELAGVGD APKGAALGDQ
     RQQHQKVFR
//
ID   D4N6R6_MUSMC            Unreviewed;       147 AA.
AC   D4N6R6;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   08-MAR-2011, entry version 6.
DE   SubName: Full=Beta-globin;
GN   Name=Hbbt1;
OS   Mus musculus castaneus (Southeastern Asian house mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20100937; DOI=10.1534/genetics.109.113506;
RA   Runck A.M., Weber R.E., Fago A., Storz J.F.;
RT   "Evolutionary and Functional Properties of a Two-Locus {beta}-Globin
RT   Polymorphism in Indian House Mice.";
RL   Genetics 0:0-0(2010).
CC   -!- SIMILARITY: Belongs to the globin family.
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DR   EMBL; GU057210; ADD52650.1; -; Genomic_DNA.
DR   EMBL; GU057211; ADD52651.1; -; Genomic_DNA.
DR   EMBL; GU057212; ADD52652.1; -; Genomic_DNA.
DR   EMBL; GU057213; ADD52653.1; -; Genomic_DNA.
DR   EMBL; GU057219; ADD52659.1; -; Genomic_DNA.
DR   EMBL; GU057221; ADD52661.1; -; Genomic_DNA.
DR   EMBL; GU057225; ADD52665.1; -; Genomic_DNA.
DR   EMBL; GU057229; ADD52669.1; -; Genomic_DNA.
DR   EMBL; GU057230; ADD52670.1; -; Genomic_DNA.
DR   EMBL; GU057231; ADD52671.1; -; Genomic_DNA.
DR   EMBL; GU057232; ADD52672.1; -; Genomic_DNA.
DR   EMBL; GU057233; ADD52673.1; -; Genomic_DNA.
DR   EMBL; GU057234; ADD52674.1; -; Genomic_DNA.
DR   EMBL; GU057243; ADD52683.1; -; Genomic_DNA.
DR   EMBL; GU057244; ADD52684.1; -; Genomic_DNA.
DR   EMBL; GU057247; ADD52687.1; -; Genomic_DNA.
DR   EMBL; GU057248; ADD52688.1; -; Genomic_DNA.
DR   GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen transporter activity; IEA:UniProtKB-KW.
DR   InterPro; IPR012292; Globin.
DR   InterPro; IPR009050; Globin-like.
DR   InterPro; IPR000971; Globin_subset.
DR   InterPro; IPR002337; Haemoglobin_b.
DR   Gene3D; G3DSA:1.10.490.10; Globin_related; 1.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00814; BETAHAEM.
DR   SUPFAM; SSF46458; Globin_like; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Metal-binding; Oxygen transport; Transport.
SQ   SEQUENCE   147 AA;  15824 MW;  99F0EAEEE5F03CC3 CRC64;
     MVHLTDAEKA AVSCLWGKVN ADEVGGEALG RLLVVYPWTQ RYFDSFGDLS SASAIMGNAK
     VKAHGKKVIT AFNDGLNHLD SLKGTFASLS ELHCDKLHVD PENFRLLGNM IVIVLGHHLG
     KDFTPAAQAA FQKVVAGVAT ALAHKYH
//
ID   D5MR34_MOUSE            Unreviewed;       133 AA.
AC   D5MR34;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   08-MAR-2011, entry version 6.
DE   SubName: Full=Tubulin beta 3;
DE   Flags: Fragment;
GN   Name=Tubb3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Nunome M., Ishimori C., Aplin K.P., Tsuchiya K., Yonekawa H.,
RA   Moriwaki K., Suzuki H.;
RT   "Detection of recombinant haplotypes in wild mice (Mus musculus)
RT   provides new insights into the origin of Japanese mice.";
RL   Mol. Ecol. 19:2474-2489(2010).
CC   -!- SIMILARITY: Belongs to the tubulin family.
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DR   EMBL; AB504826; BAJ07155.1; -; Genomic_DNA.
DR   EMBL; AB504827; BAJ07156.1; -; Genomic_DNA.
DR   EMBL; AB504828; BAJ07157.1; -; Genomic_DNA.
DR   EMBL; AB504829; BAJ07158.1; -; Genomic_DNA.
DR   IPI; IPI00112251; -.
DR   Ensembl; ENSMUST00000071134; ENSMUSP00000071134; ENSMUSG00000062380.
DR   MGI; MGI:107813; Tubb3.
DR   Bgee; D5MR34; -.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005874; C:microtubule; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR   InterPro; IPR002453; Beta_tubulin.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   Gene3D; G3DSA:3.40.50.1440; Tubulin_FtsZ; 1.
DR   PANTHER; PTHR11588; Tubulin; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   PRINTS; PR01163; BETATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SUPFAM; SSF52490; Tubulin_FtsZ; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Microtubule; Nucleotide-binding.
FT   NON_TER       1      1
FT   NON_TER     133    133
SQ   SEQUENCE   133 AA;  14528 MW;  FE8BD3E63B99535D CRC64;
     CLQGFQLTHS LGGGTGSGMG TLLISKVREE YPDRIMNTFS VVPSPKVSDT VVEPYNATLS
     IHQLVENTDE TYCIDNEALY DICFRTLKLA TPTYGDLNHL VSATMSGVTT SLRFPGQLNA
     DLRKLAVNMV PFP
//
ID   D6RG95_MOUSE            Unreviewed;       545 AA.
AC   D6RG95;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   08-MAR-2011, entry version 6.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Ythdc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUN-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC102016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00881171; -.
DR   Ensembl; ENSMUST00000156363; ENSMUSP00000122491; ENSMUSG00000035851.
DR   MGI; MGI:2443713; Ythdc1.
DR   GeneTree; ENSGT00570000079050; -.
DR   Bgee; D6RG95; -.
DR   InterPro; IPR007275; YTH_domain.
DR   PANTHER; PTHR12357; YTH; 1.
DR   Pfam; PF04146; YTH; 1.
DR   PROSITE; PS50882; YTH; 1.
PE   4: Predicted;
SQ   SEQUENCE   545 AA;  61939 MW;  DF660244C3BA49A8 CRC64;
     MAADSREEKE DCQDCSSWLF SDGELNVLDD ILTEVPEQDD ELYNPESEQD KNEKKGSKRK
     SERMESTDTK RQKPSIHSRQ LISKPLSSSV SNNKRIVSTK GKSVTEYKNE EYQRSERNKR
     LDADRKIRLS SSSSREPYKS QPEKTCLRKR DSERRAKSPT PDGSERIGLE VDRRASRSSQ
     SSKEEVNSED YGSDHETGSS GSSEQGNNTE NEEEGGEEDV EEDEEVDEDA EDDEEVDEDA
     EEEEEEDEEE EEDEDEDEEE EEYEQDERDQ KEEGNDYDTR SEASDSGSES VSFTDGSVRS
     GSGTDGSDEK KKERKRARGI SPIVFDRSGS SASESYADQT SKLKYVLQDA RFFLIKSNNH
     ENVSLAKAKG VWSTLPVNEK KLNLAFRSAR SVILIFSVRE SGKFQGFARL SSESHHGGSP
     IHWVLPAGMS AKMLGGVFKI DWICRRELPF TKSAHLTNPW NEHKPVKIGR DGQEIELECG
     TQLCLLFPPD ESIDLYQLIH KMRHKRRMHS QPRSRGRPSR REPVRDVGRL ETFFGLIIGT
     CIGIT
//
ID   D6RH62_MOUSE            Unreviewed;       352 AA.
AC   D6RH62;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   08-MAR-2011, entry version 5.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Ddhd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUN-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC107711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00857930; -.
DR   Ensembl; ENSMUST00000149286; ENSMUSP00000118848; ENSMUSG00000037697.
DR   MGI; MGI:2150302; Ddhd1.
DR   GeneTree; ENSGT00530000063155; -.
DR   Bgee; D6RH62; -.
PE   4: Predicted;
SQ   SEQUENCE   352 AA;  37883 MW;  C6D8BE588B8A5E72 CRC64;
     MNYPGRGAPR SPERNGRGGG AWELGSDAAG VFGGGGCCFE HQPGDSVPLS LLRAEPLHLA
     PGADDLSHLA LDPCLSDETY DFSSAESGSS LRYYSEGESA GGGSSSSPPP PLVAQNSGGG
     GAAGGGPGDR KRARPGGAAA RHRYEVVTEL GPEEVRWFYK EDKKTWKPFI GYDSLRIELA
     FRTLLQTTGA QARAAGRDGD RVCGPSSSFG EEDEEDSACG FCPRAAGPEP EMEELVTIEP
     VCVRGGLYEV DVTQGECYPV YWNQADKIPV MRGQWFIDGT WQPLEEEESN LIEQEHLSCF
     RGQQMQENFD IEVSKSLDGK DGSGINYSED IRRAQMPQVL SESVPKLFTV SS
//
ID   D6RHQ8_MOUSE            Unreviewed;       211 AA.
AC   D6RHQ8;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   08-MAR-2011, entry version 5.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Iqsec3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC115799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC153982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00856510; -.
DR   Ensembl; ENSMUST00000129815; ENSMUSP00000120847; ENSMUSG00000040797.
DR   Ensembl; ENSMUST00000152103; ENSMUSP00000116317; ENSMUSG00000040797.
DR   MGI; MGI:2677208; Iqsec3.
DR   GeneTree; ENSGT00590000083058; -.
DR   Bgee; D6RHQ8; -.
PE   4: Predicted;
SQ   SEQUENCE   211 AA;  22678 MW;  8376946E10C93E39 CRC64;
     MESLLENPVR AVLYLKELTA IVQNQQSLIH TQRQRIDELE RRLDELSAEN RSLWEHQQLL
     QAQPPPGLVP PPPSAPLPAP AVTAPAAAAA QEPLQDHGQL IPASPEPPLQ HHGQLLAQPQ
     PAPSSRVQTP QSPHQHPVAP GAIADKEKER PSSCCAAAGA LLQHASPAAL GKGVLSRRPE
     NETVLHQFCC PAADTEQKPA CSDLASQRLK C
//
ID   D9HP81_MOUSE            Unreviewed;      1572 AA.
AC   D9HP81;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   08-MAR-2011, entry version 6.
DE   SubName: Full=Regulating synaptic membrane exocytosis 2;
GN   Name=Rims2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   PubMed=20452978; DOI=10.1074/jbc.M110.101311;
RA   Uriu Y., Kiyonaka S., Miki T., Yagi M., Akiyama S., Mori E., Nakao A.,
RA   Beedle A.M., Campbell K.P., Wakamori M., Mori Y.;
RT   "Rab3-interacting molecule gamma isoforms lacking the Rab3-binding
RT   domain induce long lasting currents but block neurotransmitter vesicle
RT   anchoring in voltage-dependent P/Q-type Ca2+ channels.";
RL   J. Biol. Chem. 285:21750-21767(2010).
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; HM015529; ADI78886.1; -; mRNA.
DR   IPI; IPI00970050; -.
DR   UniGene; Mm.309296; -.
DR   GO; GO:0017137; F:Rab GTPase binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR010911; Rab-bd_domain.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00239; C2; 2.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50916; RABBD; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Zinc.
SQ   SEQUENCE   1572 AA;  177622 MW;  5AC5BF907848F75D CRC64;
     MSAPLGPRGR PAPTPAASQP PPQPEMPDLS HLTEEERKII LAVMDRQKKE EEKEQSVLKK
     LHQQFEMYKE QVKKMGEESQ QQQEQKGDAP TCGICHKTKF ADGCGHNCSY CQTKFCARCG
     GRVSLRSNKV MWVCNLCRKQ QEILTKSGAW FYNSGSNTLQ QPDQKVPRGL RNEEAPQEKK
     AKLHEQPQFQ GAPGDLSVPA VEKGRAHGLT RQDTIKNGSG VKHQIASDMP SDRKRSPSVS
     RDQNRRYEQS EEREDYSQYV PSDGTMPRSP SDYADRRSQR EPQFYEEPGH LNYRDSNRRG
     HRHSKEYIVD DEDVESRDEY ERQRREEEYQ ARYRSDPNLA RYPVKPQPYE EQMRIHAEVS
     RARHERRHSD VSLANAELED SRISLLRMDR PSRQRSVSER RAAMENQRSY SMERTREAQG
     QSSYPQRTSN HSPPTPRRSP IPLDRPDMRR ADSLRKQHHL DPSSAVRKTK REKMETMLRN
     DSLSSDQSES VRPPPPRPHK SKKGGKMRQV SLSSSEEELA STPEYTSCDD VELESESVSE
     KGDSQKGKRK TSEQGVLSDS NTRSERQKKR MYYGGHSLEE DLEWSEPQIK DSGVDTCSST
     TLNEEHSHSD KHPVTWQPSK DGDRLIGRIL LNKRLKDGSV PRDSGAMLGL KVVGGKMTES
     GRLCAFITKV KKGSLADTVG HLRPGDEVLE WNGRLLQGAT FEEVYNIILE SKPEPQVELV
     VSRPIGDIPR IPDSTHAQLE SSSSSFESQK MDRPSISVTS PMSPGMLRDV PQFLSGQLSI
     KLWFDKVGHQ LIVTILGAKD LPSREDGRPR NPYVKIYFLP DRSDKNKRRT KTVKKTLEPK
     WNQTFIYSPV HRREFRERML EITLWDQARV REEESEFLGE ILIELETALL DDEPHWYKLQ
     THDVSSLPLP RPSPYLPRRQ LHGESPTRRL QRSKRISDSE VSDYDCEDGV GVVSDYRHNG
     RDLQSSTLSV PEQVMSSNHC SPSGSPHRVD VIGRTRSWSP SAPPPQRNVE QGHRGTRATG
     HYNTISRMDR HRVMDDHYSS DRDSHFLTLP RSRHSQTIDH HHRDGRDCEA ADRQPYHRSR
     STEQRPLLER TTTRSRSSER PDTNLMRSMP SLMTGRSAPP SPALSRSHPR TGSVQTSPSS
     TPGTGRRGRQ LPQLPPKGTL ERSAMDIEER NRQMKLNKYK QVAGSDPRLE QDYHSKYRSG
     WDPHRGADTV STKSSDSDVS DVSAVSRTSS ASRFSSTSYM SVQSERPRGN RKISVFTSKM
     QNRQMGVSGK NLTKSTSISG DMCSLEKNDG SQSDTAVGAL GTSGKKRRSS IGAKMVAIVG
     LSRKSRSASQ LSQTEGGGKK LRSTVQRSTE TGLAVEMRNW MTRQASREST DGSMNSYSSE
     GNLIFPGVRL ASDSQFSDFL DGLGPAQLVG RQTLATPAMG DIQVGMMDKK GQLEVEIIRA
     RGLVVKPGSK TLPAPYVKVY LLDNGVCIAK KKTKVARKTL EPLYQQLLSF EESPQGRVLQ
     IIVWGDYGRM DHKSFMGVAQ ILLDELELSN MVIGWFKLFP PSSLVDPTLA PLTRRASQSS
     LESSTGPSYS RS
//
ID   E0CX59_MOUSE            Unreviewed;       303 AA.
AC   E0CX59;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   08-FEB-2011, entry version 5.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Pkp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC112943; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00830600; -.
DR   Ensembl; ENSMUST00000162150; ENSMUSP00000124898; ENSMUSG00000041957.
DR   MGI; MGI:1914701; Pkp2.
DR   GO; GO:0005912; C:adherens junction; IMP:MGI.
DR   GO; GO:0016337; P:cell-cell adhesion; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
PE   4: Predicted;
SQ   SEQUENCE   303 AA;  32910 MW;  6906C83367E58730 CRC64;
     MAVPGSLAEC GYIRTVLGQQ ILGHLDSSSL ALPSEARLRL AGSSGRGDPA ARSQRIQEQV
     QQTLARRGRS SAVSGNLHRT SSVPEYVYKL HVVENDFVGR QSPVTRDYDM LKAGMTATYG
     SRWGRAAAQY SSQKSVEERS WRQPLRRLEI SPDSSPERAH YGHSEYQYAW RSHVVPGGRL
     TLPRYARSEI LGLRQAGTAR RPPGCGSFSD AVFDNGPLKP TMPTHPPGTS HSAGSLLEET
     TVRVSQARLQ STQSRTARSS WPRSSVRSSL REPGRMLTTA GQAAVGSGDA HGDRSVFADA
     QLG
//
ID   E0CX65_MOUSE            Unreviewed;       172 AA.
AC   E0CX65;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   08-FEB-2011, entry version 5.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Sirpa;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL808126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00970314; -.
DR   Ensembl; ENSMUST00000163034; ENSMUSP00000124888; ENSMUSG00000037902.
DR   MGI; MGI:108563; Sirpa.
DR   GO; GO:0005887; C:integral to plasma membrane; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007015; P:actin filament organization; IMP:MGI.
DR   GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
DR   GO; GO:0006928; P:cellular component movement; IMP:MGI.
DR   GO; GO:0006911; P:phagocytosis, engulfment; IDA:MGI.
DR   GO; GO:0006910; P:phagocytosis, recognition; IDA:MGI.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; IDA:MGI.
PE   4: Predicted;
SQ   SEQUENCE   172 AA;  18890 MW;  70A13D1AABD80352 CRC64;
     MEPAGPAPGR LGPLLLCLLL SASCFCTDNN ATHNWNVFIG VGVACALLVV LLMAALYLLR
     IKQKKAKGST SSTRLHEPEK NAREITQIQD TNDINDITYA DLNLPKEKKP APRAPEPNNH
     TEYASIETGK VPRPEDTLTY ADLDMVHLSR AQPAPKPEPS FSEYASVQVQ RK
//
ID   E0CXB9_MOUSE            Unreviewed;       966 AA.
AC   E0CXB9;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   08-FEB-2011, entry version 5.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Ctnna2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC116787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC118610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC121356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC130220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC152957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC153997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC155840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00970354; -.
DR   Ensembl; ENSMUST00000160894; ENSMUSP00000124764; ENSMUSG00000063063.
DR   MGI; MGI:88275; Ctnna2.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0005913; C:cell-cell adherens junction; IDA:MGI.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0045296; F:cadherin binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   InterPro; IPR001033; Alpha_catenin.
DR   InterPro; IPR006077; Vinculin/catenin.
DR   InterPro; IPR000633; Vinculin_CS.
DR   Pfam; PF01044; Vinculin; 2.
DR   PRINTS; PR00805; ALPHACATENIN.
DR   SUPFAM; SSF47220; Vinculin/catenin; 4.
DR   PROSITE; PS00663; VINCULIN_1; 1.
PE   4: Predicted;
SQ   SEQUENCE   966 AA;  106730 MW;  EA92DE182CAB1D6C CRC64;
     MTDIHSSYTY TGSMTSATSP IILKWDPKSL EIRTLTVERL LEPLVTQVTT LVNTSNKGPS
     GKKKGRSKKA HVLAASVEQA TQNFLEKGEQ IAKESQDLKE ELVAAVEDVR KQGETMRIAS
     SEFADDPCSS VKRGTMVRAA RALLSAVTRL LILADMADVM RLLSHLKIVE EALEAVKNAT
     NEQDLANRFK EFGKEMVKLN YVAARRQQEL KDPHCRDEMA AARGALKKNA TMLYTASQAF
     LRHPDVAATR ANRDYVFKQV QEAIAGISSA AQATSPTDEA KGHTGIGELA AALNEFDNKI
     ILDPMTFSEA RFRPSLEERL ESIISGAALM ADSSCTRDDR RERIVAECNA VRQALQDLLS
     EYMNNTGRKE KGDPLNIAID KMTKKTRDLR RQLRKAVMDH ISDSFLETNV PLLVLIEAAK
     SGNEKEVKEY AQVFREHANK LVEVANLACS ISNNEEGVKL VRMAATQIDS LCPQVINAAL
     TLAARPQSKV AQDNMDVFKD QWEKQVRVLT EAVDDITSVD DFLSVSENHI LEDVNKCVIA
     LQEGDVDTLD RTAGAIRGRA ARVIHIINAE MENYEAGVYT EKVLEATKLL SETVMPRFAE
     QVEVAIEALS ANVPQPFEEN EFIDASRLVY DGVRDIRKAV LMIRTPEELE DDSDFEQEDY
     DVRSRTSVQT EDDQLIAGQS ARAIMAQLPQ EEKAKIAEQV EIFHQEKSKL DAEVAKWDDS
     GNDIIVLAKQ MCMIMMEMTD FTRGKGPLKN TSDVINAAKK IAEAGSRMDK LARAVADQCP
     DSACKQDLLA YLQRIALYCH QLNICSKVKA EVQNLGGELI VSGTGVQSTF TTFYEVDCDV
     IDGGRASQLS THLPTCAEGA PIGSGSSDSS MLDSATSLIQ AAKNLMNAVV LTVKASYVAS
     TKYQKVYGTA AVNSPVVSWK MKAPEKKPLV KREKPEEFQT RVRRGSQKKH ISPVQALSEF
     KAMDSF
//
ID   E0CXD4_MOUSE            Unreviewed;       360 AA.
AC   E0CXD4;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   11-JAN-2011, entry version 4.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Pcdh1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Contains 6 cadherin domains.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC133646; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00918764; -.
DR   Ensembl; ENSMUST00000160721; ENSMUSP00000124732; ENSMUSG00000051375.
DR   MGI; MGI:104692; Pcdh1.
DR   GO; GO:0005911; C:cell-cell junction; TAS:MGI.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0016339; P:calcium-dependent cell-cell adhesion; TAS:MGI.
DR   GO; GO:0007156; P:homophilic cell adhesion; TAS:MGI.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR013164; Cadherin_N.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 1.
DR   Pfam; PF00028; Cadherin; 1.
DR   Pfam; PF08266; Cadherin_2; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 1.
DR   SUPFAM; SSF49313; Cadherin; 1.
DR   PROSITE; PS00232; CADHERIN_1; 2.
DR   PROSITE; PS50268; CADHERIN_2; 2.
PE   4: Predicted;
KW   Calcium; Cell adhesion; Cell membrane; Membrane; Repeat;
KW   Transmembrane; Transmembrane helix.
SQ   SEQUENCE   360 AA;  39089 MW;  15A76DE3F35B287E CRC64;
     MGPLRPSPGP GGQRLLLPPL LLALLLLLAP SASHTTQVVY KVPEEQPPNT LIGSLAADYG
     LPDVGHLYKL EVGAPYLRVD GKTGDIFTTE TSIDREGLRE CQNQIPGNPC ILEFEVSITD
     LVQNGSPRLL EGQIEVQDIN DNTPNFASPV ITLAIPENTN IGSLFPIPLA TDRDAGPNGV
     ASYELQAGPE AQELFGLQVA EDQEEKQPQL IVMGNLDRER WDSYDLTIKV QDGGNPPRAS
     SALLRVTVLD TNDNAPKFER PTYEAELSEN SPIGHSVIQL PHRRVTFSAT SQAQELQDPS
     QHSYYDSGLE ESETPSSKSS SGPRLGPLAL PEDHYERTTP DGSIGEMEHP ENEPAGRSRP
//
ID   E0CXD6_MOUSE            Unreviewed;      1297 AA.
AC   E0CXD6;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   08-MAR-2011, entry version 6.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Tnik;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC108428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC114825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC121268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC147186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC160933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00885459; -.
DR   Ensembl; ENSMUST00000162777; ENSMUSP00000124726; ENSMUSG00000027692.
DR   MGI; MGI:1916264; Tnik.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0005083; F:small GTPase regulator activity; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR001180; Citron.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding; Nucleotide-binding.
SQ   SEQUENCE   1297 AA;  147896 MW;  5825ED3F90334AC3 CRC64;
     MASDSPARSL DEIDLSALRD PAGIFELVEL VGNGTYGQVY KGRHVKTGQL AAIKVMDVTG
     DEEEEIKQEI NMLKKYSHHR NIATYYGAFI KKNPPGMDDQ LWLVMEFCGA GSVTDLIKNT
     KGNTLKEEWI AYICREILRG LSHLHQHKVI HRDIKGQNVL LTENAEVKLV DFGVSAQLDR
     TVGRRNTFIG TPYWMAPEVI ACDENPDATY DFKSDLWSLG ITAIEMAEGA PPLCDMHPMR
     ALFLIPRNPA PRLKSKKWSK KFQSFIESCL VKNHSQRPAT EQLMKHPFIR DQPNERQVRI
     QLKDHIDRTK KKRGEKDETE YEYSGSEEEE EENDSGEPSS ILNLPGESTL RRDFLRLQLA
     NKERSEALRR QQLEQQQREN EEHKRQLLAE RQKRIEEQKE QRRRLEEQQR REKELRKQQE
     REQRRHYEEQ MRREEERRRA EHEQEYIRRQ LEEEQRQLEI LQQQLLHEQA LLLEYKRKQL
     EEQRQAERLQ RQLKQERDYL VSLQHQRQEQ RPLEKKPLYH YKEGMSPSEK PAWAKEIPQL
     VAVKSQGPAL TASQSVHEQP TKGLSGFQEA LNVTSHRVEM PRQNSDPTSE NPPLPTRIEK
     FDRSSWLRQE EDIPPKVPQR TTSISPALAR KNSPGNGSAL GPRLGSQPIR ASNPDLRRTE
     PVLESSLQRT SSGSSSSSST PSSQPSSQGG SQPGSQAGSS ERSRVRANSK SEGSPVLPHE
     PSKVKPEESR DITRPSRPAD LTALAKELRE LRIEETNRPL KKVTDYSSSS EESESSEEEE
     EDGESETHDG TVAVSDIPRL IPTGAPGNNE QYNMGMVGTH GLETSHADTF GGSISREGTL
     MIRETAEEKK RSGHSDSNGF AGHINLPDLV QQSHSPAGTP TEGLGRVSTH SQEMDSGAEY
     GIGSSTKASF TPFVDPRVYQ TSPTDEDEED DESSAAALFT SELLRQEQAK LNEARKISVV
     NVNPTNIRPH SDTPEIRKYK KRFNSEILCA ALWGVNLLVG TENGLMLLDR SGQGKVYNLI
     NRRRFQQMDV LEGLNVLVTI SGKKNKLRVY YLSWLRNRIL HNDPEVEKKQ GWITVGDLEG
     CIHYKVVKYE RIKFLVIALK NAVEIYAWAP KPYHKFMAFK SFADLQHKPL LVDLTVEEGQ
     RLKVIFGSHT GFHVIDVDSG NSYDIYIPSH IQGNITPHAI VILPKTDGME MLVCYEDEGV
     YVNTYGRITK DVVLQWGEMP TSVAYIHSNQ IMGWGEKAIE IRSVETGHLD GVFMHKRAQR
     LKFLCERNDK VFFASVRSGG SSQVFFMTLN RNSMMNW
//
ID   E0CXE0_MOUSE            Unreviewed;       821 AA.
AC   E0CXE0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   08-MAR-2011, entry version 5.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Grip2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- SIMILARITY: Contains 6 PDZ (DHR) domains.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC118245; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC162914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00970270; -.
DR   Ensembl; ENSMUST00000162293; ENSMUSP00000124717; ENSMUSG00000030098.
DR   MGI; MGI:2681173; Grip2.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF00595; PDZ; 6.
DR   SMART; SM00228; PDZ; 6.
DR   SUPFAM; SSF50156; PDZ; 6.
DR   PROSITE; PS50106; PDZ; 6.
PE   4: Predicted;
SQ   SEQUENCE   821 AA;  88056 MW;  C71BD0B71D6B760C CRC64;
     MVELIKREGS TLGLTISGGT DKDGKPRVSN LRPGGLAARS DLLNVGDYIR SVNGIHLTRL
     RHDEIITLLK NVGERVVLEV EYELPPPAPE NNPRIISKTV DVSLYKEGNS FGFVLRGGAH
     EDLHKSRPLV LTYVRPGGPA DREGSLKVGD RLLSIDGIPL HGASHATAIA TLQQCSHEAL
     FQVEYDVATP DTVANASGPL VVEIAKTPGS ALGISLTTGS HRNKPAITID RIKPASVVDR
     SGALHAGDHI LAIDGTSTEH CSLVEATKLL ASVTEKVRLE ILPSPQSRRP LKPPEAVRIQ
     RSEQLHRWDP SAPSCHSPRP SHCRAPTWAA GGPDQSRSVS STPFSSPTMN PAFPCANAST
     LPRGPMSPRT TAGRRRQRRK EHRSSLSLAS STVGPGGQIV HTETTEVVLC GDPLSGFGLQ
     LQGGIFATET LSSPPLVRFI EPDSPAERCG LLQVGDRVLA INGIATEDGT MEEANQLLRD
     AALARKVVLE IEFDVAESVI PSSGTFHVKL PKRRGVELGI TISSASRKRG EPLIISDIKK
     GSVAHRTGTL EPGDKLLAID NIRLDHCPME DAVQILRQCE DLVKLKIRKD EDNSDEQESS
     GAVSYTVELK RYGGPLGITI SGTEEPFDPI IISGLTKRGL AERTGAIHVG DRILAINSVS
     LKGRPLSEAI HLLQVAGETV TLKIKKQLDR PLLPRQSGSL SEASDVDEDP PEALKGGLLA
     TRFSPAVPSV DSAVESWGSS ATDGGFGGTG SYTPQVAVRS VTPQEWRPSR LKSSPPPLEP
     RRTSYTPGPS DESFPEEEGD WEPPMRRPVS PLSTPSHLPL F
//
ID   E0CXJ1_MOUSE            Unreviewed;        88 AA.
AC   E0CXJ1;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   11-JAN-2011, entry version 4.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Phyhip;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC122268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00970194; -.
DR   Ensembl; ENSMUST00000159180; ENSMUSP00000125254; ENSMUSG00000003469.
DR   MGI; MGI:1860417; Phyhip.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
PE   4: Predicted;
SQ   SEQUENCE   88 AA;  10246 MW;  3F67A9379BF8E70F CRC64;
     MELLSTPHSI EINNITCDSF RISWAMEDSD LERVTHYFID LNKKENKNSN KFKHRDVPTK
     LVAKAVPLPM TVRGHWFLSP RTEYSVAV
//
ID   E0CXK2_MOUSE            Unreviewed;      1835 AA.
AC   E0CXK2;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   08-MAR-2011, entry version 5.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Cacna1i;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC155313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00970007; -.
DR   Ensembl; ENSMUST00000162155; ENSMUSP00000125229; ENSMUSG00000022416.
DR   MGI; MGI:2178051; Cacna1i.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IEA:InterPro.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR005445; VDCC_T_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01629; TVDCCALPHA1.
PE   3: Inferred from homology;
KW   Calcium; Calcium channel; Calcium transport; Ion transport;
KW   Ionic channel; Membrane; Transmembrane; Transport;
KW   Voltage-gated channel.
SQ   SEQUENCE   1835 AA;  205417 MW;  02A75351A1373D4B CRC64;
     MADSNLPPSS SAAPDPEPGI TEQPGPRSPP PSPPGLEEPL DGTNPDVPHP DLAPVAFFCL
     RQTTSPRNWC IKMVCNPWFE CVSMLVILLN CVTLGMYQPC DDMECLSDRC KILQVFDDFI
     FIFFAMEMVL KMVALGIFGK KCYLGDTWNR LDFFIVMAGM VEYSLDLQNI NLSAIRTVRV
     LRPLKAINRV PSMRILVNLL LDTLPMLGNV LLLCFFVFFI FGIIGVQLWA GLLRNRCFLE
     ENFTIQGDVA LPPYYQPEED DEMPFICSLS GDNGIMGCHE IPPLKEQGRE CCLSKDDMYD
     FGAGRQDLNA SGLCVNWNRY YNVCRTGNAN PHKGAINFDN IGYAWIVIFQ VITLEGWVEI
     MYYVMDAHSF YNFIYFILLI IVGSFFMINL CLVVIATQFS ETKQREHRLM LEQRQRYLSS
     STVASYAEPG DCYEEIFQYV CHILRKAKRR ALGLYQALQN RRQATGPGTP APAKPGPHAK
     EPSHCKLCPR HSPLDTTPHT LVQPISAILA SDPSSCPRCQ HEAGRRPSGL GSTDSGQEGS
     GSGGSAEAEA NGDGPQSSED GVSSGLGKEE EQEDGAARLC GDVWRETRAK LRGIVDSKYF
     NRGIMMAILV NTVSMGIEHH EQPEELTNIL EICNVVFTSM FALEMILKLA AFGLFDYLRN
     PYNIFDSIIV IISIWEIVGQ ADGGLSVLRT FRLLRVLKLV RFMPALRRQL VVLMKTMDNV
     ATFCMLLMLF IFIFSILGMH IFGCKFSLRT DTGDTVPDRK NFDSLLWAIV TVFQILTQED
     WNVVLYNGMA STTPWASLYF VALMTFGNYV LFNLLVAILV EGFQAEGDAN RSYSDEDQSS
     SNLEELDKLP EGLDSSRDLK LCPIPMTPNG HLDPSLPLGG HLGPAGAMGA APRLSLQPDP
     VLVALESRKS SVMSLGRMSY DQRSLSSSRS SYYGPWGRSG TWASRRSSWN SLKHKPPSAE
     HESLLSGERG GSCVRACEGA REDAPPRAAP LHAPHTHHAH HGPHLAHRHR HHRRTLSLDT
     RDSVDLAELV PVVGAHSRAA WRAAGQAPGH EDCNGRMPNI AKDVFTKMDD RRDRGEDEEE
     IDYTLCFRVR KMIDVYKPDW CEVREDWSVY LFSPENKFRI LCQTIIAHKL FDYVVLAFIF
     LNCITIALER PQIEAGSTER IFLTVSNYIF TAIFVGEMTL KVVSLGLYFG EQAYLRSSWN
     VLDGFLVFVS IIDIVVSVAS AGGAKILGVL RVLRLLRTLR PLRVISRAPG LKLVVETLIS
     SLKPIGNIVL ICCAFFIIFG ILGVQLFKGK FYHCLGVDTR NITNRSDCVA ANYRWVHHKY
     NFDNLGQALM SLFVLASKDG WVNIMYNGLD AVAVDQQPVT NHNPWMLLYF ISFLLIVSFF
     VLNMFVGVVV ENFHKCRQHQ EAEEARRREE KRLRRLEKKR RKAQRLPYYA TYCPTRLLIH
     SMCTSHYLDI FITFIICLNV VTMSLEHYNQ PTSLETALKY CNYMFTTVFV LEAVLKLVAF
     GLRRFFKDRW NQLDLAIVLL SVMGITLEEI EINAALPINP TIIRIMRVLR IARVLKLLKM
     ATGMRALLDT VVQALPQVGN LGLLFMLLFF IYAALGVELF GKLVCNDENP CEGMSRHATF
     ENFGMAFLTL FQVSTGDNWN GIMKDTLRDC THDERSCLSS LQFVSPLYFV SFVLTAQFVL
     INVVVAVLMK HLDDSNKEAQ EDAEMDAEIE LEMAHGLGPG PGPCPCPCPC PCPCPCPGPR
     MPTSSPGAPG RGSGGAGVGG DTESHLCRHC YSPAQETLWL DSVSLIIKDS LEGELTIIDN
     LSGSIFHHYS SPAGCDKCHH DKQETGPRPS CWGMT
//
ID   E0CXS4_MOUSE            Unreviewed;      1001 AA.
AC   E0CXS4;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   08-MAR-2011, entry version 5.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Grip2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- SIMILARITY: Contains 7 PDZ (DHR) domains.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC118245; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC162914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00970210; -.
DR   Ensembl; ENSMUST00000159684; ENSMUSP00000125047; ENSMUSG00000030098.
DR   MGI; MGI:2681173; Grip2.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF00595; PDZ; 7.
DR   SMART; SM00228; PDZ; 7.
DR   SUPFAM; SSF50156; PDZ; 7.
DR   PROSITE; PS50106; PDZ; 7.
PE   4: Predicted;
SQ   SEQUENCE   1001 AA;  107648 MW;  DFAFA727355F04CE CRC64;
     MLAVSLKWRL GVVRRRPKDD GPYSKGGKDT AGADGALVCR RQSIPEEFRG ITMVELIKRE
     GSTLGLTISG GTDKDGKPRV SNLRPGGLAA RSDLLNVGDY IRSVNGIHLT RLRHDEIITL
     LKNVGERVVL EVEYELPPPA PENNPRIISK TVDVSLYKEG NSFGFVLRGG AHEDLHKSRP
     LVLTYVRPGG PADREGSLKV GDRLLSIDGI PLHGASHATA IATLQQCSHE ALFQVEYDVA
     TPDTVANASG PLVVEIAKTP GSALGISLTT GSHRNKPAIT IDRIKPASVV DRSGALHAGD
     HILAIDGTST EHCSLVEATK LLASVTEKVR LEILPSPQSR RPLKPPEAAV SSTPFSSPTM
     NPAFPCANAS TLPRGPMSPR TTAGRRRQRR KEHRSSLSLA SSTVGPGGQI VHTETTEVVL
     CGDPLSGFGL QLQGGIFATE TLSSPPLVRF IEPDSPAERC GLLQVGDRVL AINGIATEDG
     TMEEANQLLR DAALARKVVL EIEFDVAESV IPSSGTFHVK LPKRRGVELG ITISSASRKR
     GEPLIISDIK KGSVAHRTGT LEPGDKLLAI DNIRLDHCPM EDAVQILRQC EDLVKLKIRK
     DEDNSDEQES SGAVSYTVEL KRYGGPLGIT ISGTEEPFDP IIISGLTKRG LAERTGAIHV
     GDRILAINSV SLKGRPLSEA IHLLQVAGET VTLKIKKQLD RPLLPRQSGS LSEASDVDED
     PPEALKGGLL ATRFSPAVPS VDSAVESWGS SATDGGFGGT GSYTPQVAVR SVTPQEWRPS
     RLKSSPPPLE PRRTSYTPGP SDESFPEEEG DWEPPMSPAP GPAREEGFWR VLGEALEDLE
     SCGQSELLRE LEASIMTGTV HSVAVDGRPG SRPWRRSREV RTSPEDLQEL LLPTPLEMHR
     VTLHKDPVRN DFGFSVSDGL LEKGVYVHTV RIDGPAQLGG LQPFDRLLQV NHVRTRDFDC
     CLAVPLLAEA GDILELVVSR NPLAQSRRTP GAPGPSSPQM L
//
ID   E0CXS8_MOUSE            Unreviewed;       587 AA.
AC   E0CXS8;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   30-NOV-2010, entry version 3.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Gm8113; Synonyms=Gm5057;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC173966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00807904; -.
DR   Ensembl; ENSMUST00000160298; ENSMUSP00000125038; ENSMUSG00000089901.
DR   MGI; MGI:3648791; Gm8113.
PE   4: Predicted;
SQ   SEQUENCE   587 AA;  66009 MW;  A2B1EF2B6D9DC36D CRC64;
     MTPGWIPWKL PLVLVLPLWI WVPSIFGEYR WAILSAFPKP MPVRHNTAVF PKFFTTNKTL
     GLRYLPFDPI WAPLGEKRSL RERGSLCFQI YELENCIRLT SRALGMFFKY RGGVVKITQD
     TSNRDITLTN RTFWQEAIWV NGTFLPPNFS DKERPNQPKM APHCSLEDEG LILPWSDCQS
     SVTRWADQSK TFSFSPNMID DPEQKYVMKK GLFIQDFRMH PFHKWVLCGI NGSCTDLNPL
     VFLQGGTAGK AIFNGISKFA QFHQVLLPDR TIYQNSTTKI TGFNKTLIKQ TNYLPTPICV
     YTPFLFILSN GSFESCTNET CWMSQCWSLK WASRAMLAKI PRWVPVPVEI PSTITLHRQK
     RDFGITAAVV MTMAASAAAA TAARIAMATS VQSSTTVQQL SSSVAEAIDQ HSVLSAQLKG
     GLMIVNQPID LVEERLEILL QLAQLGCDKK SGALCIASVQ YENWTHAANL SKELSLFLTG
     NWSEGFDEKL EALRTAVMTI NSMRVDPSLI YGIKGLSSWM SSAFSHFKEW VGVGLFGATL
     CCGLVFLLWL VCKLRSQQKR DKVVIAQALA AIEEGTSPEI WLSILKN
//
ID   E0CXZ8_MOUSE            Unreviewed;       319 AA.
AC   E0CXZ8;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   08-MAR-2011, entry version 6.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Dnm3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=22354682; PubMed=12466850; DOI=10.1038/nature01262;
RA   Waterston R.H., Lindblad-Toh K., Birney E., Rogers J., Abril J.F.,
RA   Agarwal P., Agarwala R., Ainscough R., Alexandersson M., An P.,
RA   Antonarakis S.E., Attwood J., Baertsch R., Bailey J., Barlow K.,
RA   Beck S., Berry E., Birren B., Bloom T., Bork P., Botcherby M.,
RA   Bray N., Brent M.R., Brown D.G., Brown S.D., Bult C., Burton J.,
RA   Butler J., Campbell R.D., Carninci P., Cawley S., Chiaromonte F.,
RA   Chinwalla A.T., Church D.M., Clamp M., Clee C., Collins F.S.,
RA   Cook L.L., Copley R.R., Coulson A., Couronne O., Cuff J., Curwen V.,
RA   Cutts T., Daly M., David R., Davies J., Delehaunty K.D., Deri J.,
RA   Dermitzakis E.T., Dewey C., Dickens N.J., Diekhans M., Dodge S.,
RA   Dubchak I., Dunn D.M., Eddy S.R., Elnitski L., Emes R.D., Eswara P.,
RA   Eyras E., Felsenfeld A., Fewell G.A., Flicek P., Foley K.,
RA   Frankel W.N., Fulton L.A., Fulton R.S., Furey T.S., Gage D.,
RA   Gibbs R.A., Glusman G., Gnerre S., Goldman N., Goodstadt L.,
RA   Grafham D., Graves T.A., Green E.D., Gregory S., Guigo R., Guyer M.,
RA   Hardison R.C., Haussler D., Hayashizaki Y., Hillier L.W., Hinrichs A.,
RA   Hlavina W., Holzer T., Hsu F., Hua A., Hubbard T., Hunt A.,
RA   Jackson I., Jaffe D.B., Johnson L.S., Jones M., Jones T.A., Joy A.,
RA   Kamal M., Karlsson E.K., Karolchik D., Kasprzyk A., Kawai J.,
RA   Keibler E., Kells C., Kent W.J., Kirby A., Kolbe D.L., Korf I.,
RA   Kucherlapati R.S., Kulbokas E.J., Kulp D., Landers T., Leger J.P.,
RA   Leonard S., Letunic I., Levine R., Li J., Li M., Lloyd C., Lucas S.,
RA   Ma B., Maglott D.R., Mardis E.R., Matthews L., Mauceli E., Mayer J.H.,
RA   McCarthy M., McCombie W.R., McLaren S., McLay K., McPherson J.D.,
RA   Meldrim J., Meredith B., Mesirov J.P., Miller W., Miner T.L.,
RA   Mongin E., Montgomery K.T., Morgan M., Mott R., Mullikin J.C.,
RA   Muzny D.M., Nash W.E., Nelson J.O., Nhan M.N., Nicol R., Ning Z.,
RA   Nusbaum C., O'Connor M.J., Okazaki Y., Oliver K., Overton-Larty E.,
RA   Pachter L., Parra G., Pepin K.H., Peterson J., Pevzner P., Plumb R.,
RA   Pohl C.S., Poliakov A., Ponce T.C., Ponting C.P., Potter S., Quail M.,
RA   Reymond A., Roe B.A., Roskin K.M., Rubin E.M., Rust A.G., Santos R.,
RA   Sapojnikov V., Schultz B., Schultz J., Schwartz M.S., Schwartz S.,
RA   Scott C., Seaman S., Searle S., Sharpe T., Sheridan A., Shownkeen R.,
RA   Sims S., Singer J.B., Slater G., Smit A., Smith D.R., Spencer B.,
RA   Stabenau A., Stange-Thomann N., Sugnet C., Suyama M., Tesler G.,
RA   Thompson J., Torrents D., Trevaskis E., Tromp J., Ucla C.,
RA   Ureta-Vidal A., Vinson J.P., Von Niederhausern A.C., Wade C.M.,
RA   Wall M., Weber R.J., Weiss R.B., Wendl M.C., West A.P.,
RA   Wetterstrand K., Wheeler R., Whelan S., Wierzbowski J., Willey D.,
RA   Williams S., Wilson R.K., Winter E., Worley K.C., Wyman D., Yang S.,
RA   Yang S.P., Zdobnov E.M., Zody M.C., Lander E.S.;
RT   "Initial sequencing and comparative analysis of the mouse genome.";
RL   Nature 420:520-562(2002).
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC113015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC120180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC121318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC138218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC157798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00881200; -.
DR   Ensembl; ENSMUST00000160665; ENSMUSP00000124593; ENSMUSG00000040265.
DR   MGI; MGI:1341299; Dnm3.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   InterPro; IPR003130; GED.
DR   InterPro; IPR020850; GTPase_effector_domain_GED.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF02212; GED; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00302; GED; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS51388; GED; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   4: Predicted;
SQ   SEQUENCE   319 AA;  35725 MW;  481FFCB052AA160D CRC64;
     MKGGSKGYWF VLTAESLSWY KDDEEKEKKY MLPLDNLKVR DVEKGFMSSK HVFALFNTEQ
     RNVYKDYRFL ELACDSQEDV DSWKASLLRA GVYPDKSVTE NDENGQAENF SMDPQLERQV
     ETIRNLVDSY MSIINKCIRD LIPKTIMHLM INNVKDFINS ELLAQLYSSE DQNTLMEESA
     EQAQRRDEML RMYQALKEAL AIIGDINTAT VSTPAPPPVD DSWLQHSRRS PPPSPTTQRR
     LTISAPLPRP TSGRGPAPAI PSPGPHSGAP PVPFRPGPLP PFPNSSDSFG APPQVPSRPT
     RAPPSVPRFG AVKEEAVEP
//
ID   E0CY16_MOUSE            Unreviewed;       390 AA.
AC   E0CY16;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   08-MAR-2011, entry version 6.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Cadm1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC121870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC122426; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC140183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC183268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00849722; -.
DR   Ensembl; ENSMUST00000143026; ENSMUSP00000124555; ENSMUSG00000032076.
DR   MGI; MGI:1889272; Cadm1.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0016338; P:calcium-independent cell-cell adhesion; IDA:MGI.
DR   GO; GO:0007416; P:synapse assembly; IDA:MGI.
DR   GO; GO:0009826; P:unidimensional cell growth; IMP:MGI.
DR   InterPro; IPR013162; CD80_C2-set.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Pfam; PF08205; C2-set_2; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   PROSITE; PS50835; IG_LIKE; 3.
PE   4: Predicted;
KW   Immunoglobulin domain; Membrane; Repeat; Transmembrane;
KW   Transmembrane helix.
SQ   SEQUENCE   390 AA;  42892 MW;  A000130AAB63B868 CRC64;
     MASAVLPSGS QCAAAAAVAA AAAPPGLRLR LLLLLLSAAA LIPTGDGQNL FTKDVTVIEG
     EVATISCQVN KSDDSVIQLL NPNRQTIYFR DFRPLKDSRF QLLNFSSSEL KVSLTNVSIS
     DEGRYFCQLY TDPPQESYTT ITVLVPPRNL MIDIQKDTAV EGEEIEVNCT AMASKPATTI
     RWFKGNKELK GKSEVEEWSD MYTVTSQLML KVHKEDDGVP VICQVEHPAV TGNLQTQRYL
     EVQYKPQVHI QMTYPLQGLT REGDAFELTC EAIGKPQPVM VTWVRVDDEM PQHAVLSGPN
     LFINNLNKTD NGTYRCEASN IVGKAHSDYM LYVYDSRAGE EGTIGAVDHA VIGGVVAVVV
     FAMLCLLIIL GRYFARHKGL FSLTSSPRIK
//
ID   E0CY23_MOUSE            Unreviewed;       571 AA.
AC   E0CY23;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   08-MAR-2011, entry version 5.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Hspa4l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC146980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00857988; -.
DR   Ensembl; ENSMUST00000159819; ENSMUSP00000124536; ENSMUSG00000025757.
DR   MGI; MGI:107422; Hspa4l.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR001023; Hsp70.
DR   InterPro; IPR013126; Hsp_70.
DR   PANTHER; PTHR19375; Hsp70; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Nucleotide-binding.
SQ   SEQUENCE   571 AA;  63555 MW;  5F62CEA2CB0C3A82 CRC64;
     MSVVGIDLGF LNCYIAVARS GGIETIANEY SDRCTPACIS LGSRTRAIGN AAKSQIVTNV
     RNTIHGFKKL HGRSFDDPIV QTERIRLPYE LQKMPNGSTG VKVRYLEEER PFAIEQVTGM
     LLAKLKETSE NALKKPVADC VISIPSFFTD AERRSVMAAA QVAGLNCLRL MNETTAVALA
     YGIYKQDLPS LDEKPRNVVF IDMGHSAYQV SVCAFNKGKL KVLATTFDPY LGGRNFDEAL
     VDYFCDEFKT KYKINVKENS RALLRLYQEC EKLKKLMSAN ASDLPLNIEC FMNDLDVSSK
     MNRAQFEQLC ASLLARVEPP LKSVMDQANL QREDINSIEI VGGATRIPAV KEQVTRFFLK
     DISTTLNADE AVARGCALQC AILSPAFKVR EFSITDLVPY SVTLRWKTSF EEGTGECEVF
     SKNHPAPFSK VITFHKKEPF ELEAFYTNLH EVPYPDPRIG NFTIQNVFPQ SDGDSSKVKV
     KVRINIHGIF SVASASVIEK QNLEGDHNDA AMETEAPKSE GKEDVDKMQV DQEEGGHQKC
     HAEHTPEEEI DHTGAKAKAP PSDKQDRINQ T
//
ID   E0CYT1_MOUSE            Unreviewed;      2137 AA.
AC   E0CYT1;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   11-JAN-2011, entry version 4.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Wnk2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC160126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CT010439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00970389; -.
DR   Ensembl; ENSMUST00000159559; ENSMUSP00000123915; ENSMUSG00000037989.
DR   MGI; MGI:1922857; Wnk2.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
SQ   SEQUENCE   2137 AA;  226168 MW;  FB2A831905D96526 CRC64;
     MDGDGGRRDA PGALMEAGRG TGSAGMAEPR ARAARLGPQR FLRRSVVESD QEEPPGLEAA
     ETPSAQPPQP LQRRVLLLCK TRRLIAERAR GRPAAPAPAA PAAPPGSPSV PSDPGPERAG
     TQEPSPDPTT ASAAAAQVPD GGPRQEEAPA PTQEDAGTTE AKPEPGRARK DEPEEEEDDE
     DDLKAVATSL DGRFLKFDIE LGRGSFKTVY KGLDTETWVE VAWCELQDRK LTKLERQRFK
     EEAEMLKGLQ HPNIVRFYDF WESSAKGKRC IVLVTELMTS GTLKTYLKRF KVMKPKVLRS
     WCRQILKGLL FLHTRTPPII HRDLKCDNIF ITGPTGSVKI GDLGLATLKR ASFAKSVIGT
     PEFMAPEMYE EHYDESVDVY AFGMCMLEMA TSEYPYSECQ NAAQIYRKVT CGIKPASFEK
     VHDPEIKEII GECICKNKEE RYEIKDLLSH AFFAEDTGVR VELAEEDHGR KSTIALRLWV
     EDPKKLKGKP KDNGAIEFTF DLEKETPDEV AQEMIDSGFF HESDVKIVAK SIRDRVALIQ
     WRRERIWPAL QSQEPKDSGS PDKARGLPAP LQVQVTYHAQ SGQPGQPEPE EPEADQHLLP
     PTLPASVTSL ASDSTFDSGQ GSTVYSDSQS SQQSMVLSSL VDTAPTPASC VCSPPVSEGP
     GLTHSLPTLG AFQQPATVPG LSVGPVPPPA RPPLLQQHFP ESSMSFTPVL PPPSTPVPTG
     PSQPAPPVQQ VLAPQPMGTV QPVPSHLPPY LAPTSQVVAP AQLKPLQMPQ PPLQPLAQVP
     PQMPQMPVVP PITPLTGLDG LPQTLTDLPA ANVAPVPPPQ YFSPAVILPS LTTPLPTSPA
     LPMQAVKLPH PPGTPLAVPC QTIVPNAPAA IPLLAVAPQG VAALSIHPAV AQIPAQPVYP
     AAFPQMVPGD IPPSPHHTVQ SLRATPPQLA SPVPPQPVQP SVIHLPEQAA PTAASGTQVL
     LGHPPSYTAD VAAPVSAVSL PPAVLSPPLP DTLLPTVPDL LPKVPSSLAP TVVAASQSAP
     AQTSSLLLPT NPPLPTGPAV AGPCPAVQLM VEVAQEEQVS QDKPPGPPQS SESFGGSDVT
     SGRDLSDSCE GTFGGGRLEG RTARKHHRRS TRARSRQERA SRPRLTILNV CNTGDKMVEC
     QLETHNHKMV TFKFDLDGDA PDEIATYMVE HDFILPAERE TFIEQMKDVM DKAEDMLSED
     TDADHGSDTG TSPPHLGTCG LATGEENRQS QANAPVYQQN VLHTGKRWFI ICPVAEHPAT
     DTSESSPPLP LSSLQPEASQ DPAPYPDQLS LTDKPSFPAA QQLLSQAGSS NPPGGASAPL
     APSSPPVTTV IPAAPATSTV PESAAGTAMQ AGGPGTHQGP ASVHETLQPL AETRSAQCTA
     QPLSTGQGPC TPALEASRCS TGLGEPISTR EVSTQGEPLP ASVPEPSPPT GATQSVPGQP
     PPPLPITVGA ISLAAPQLPS PPLGPTAPPP PPSALESDGE GPPPRVGFVD NTIKSLDEKL
     RTLLYQEHVP TSSASAGTPM EASDRDFTLE PLRGDLPSAL SDKTPSLTQQ TQPSLEKSET
     APAGWALAQR EQGASSPMTA ESSSSNTLGC DSDAGQVASD SSTAPSVPQD ASGSSVPTHM
     DPKDQNSSVP REALAAPMQS GPGSFTVGSP AQLRGARDSG SPHKRPGQQD NSSPAKTVGR
     FSVVSTQDEW TLASPHSLRY SAPPDVYLDE IPSSPEVKLA VRRVQTASSI EVGVEEPASS
     DSGDERPRRR SQVQKQSSLP GTGGVASDFV KKATAFLHRS SRAGSLGPET PSRAGVKVPT
     ISITSFHSQS SYISSDNDSE FEDADIKKEL RSLREKHLKE ISELQSQQKQ EIEALYRRLG
     KPLPPNVGFF HTAPPMGRRR KTSKSKLKAG KLLNPLVQQL KVVASSTGHL SDSSRGPPTK
     DPAHASTPPG TKAVQTQQPC SVRASLSTDI CSGLASDGGG ARGQGWTVYH PTSERGAYKS
     SSKPRARFLS GPVSVSIWSA LKRLCLGKEH SSRSSTSSLA PGPEPGPQPT LHVQAQVNNS
     NNKKGTFTDD LHKLVDEWTT KTVGAAQVKP TLNQLKQTQK LHDMEASGDA RATSVPRAAV
     GASCLAPAPG PLSTTATPGA TPALPVPIPD PESEKPD
//
ID   E0CZ27_MOUSE            Unreviewed;       119 AA.
AC   E0CZ27;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   08-MAR-2011, entry version 6.
DE   RecName: Full=Histone H3;
GN   Name=H3f3a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=22354682; PubMed=12466850; DOI=10.1038/nature01262;
RA   Waterston R.H., Lindblad-Toh K., Birney E., Rogers J., Abril J.F.,
RA   Agarwal P., Agarwala R., Ainscough R., Alexandersson M., An P.,
RA   Antonarakis S.E., Attwood J., Baertsch R., Bailey J., Barlow K.,
RA   Beck S., Berry E., Birren B., Bloom T., Bork P., Botcherby M.,
RA   Bray N., Brent M.R., Brown D.G., Brown S.D., Bult C., Burton J.,
RA   Butler J., Campbell R.D., Carninci P., Cawley S., Chiaromonte F.,
RA   Chinwalla A.T., Church D.M., Clamp M., Clee C., Collins F.S.,
RA   Cook L.L., Copley R.R., Coulson A., Couronne O., Cuff J., Curwen V.,
RA   Cutts T., Daly M., David R., Davies J., Delehaunty K.D., Deri J.,
RA   Dermitzakis E.T., Dewey C., Dickens N.J., Diekhans M., Dodge S.,
RA   Dubchak I., Dunn D.M., Eddy S.R., Elnitski L., Emes R.D., Eswara P.,
RA   Eyras E., Felsenfeld A., Fewell G.A., Flicek P., Foley K.,
RA   Frankel W.N., Fulton L.A., Fulton R.S., Furey T.S., Gage D.,
RA   Gibbs R.A., Glusman G., Gnerre S., Goldman N., Goodstadt L.,
RA   Grafham D., Graves T.A., Green E.D., Gregory S., Guigo R., Guyer M.,
RA   Hardison R.C., Haussler D., Hayashizaki Y., Hillier L.W., Hinrichs A.,
RA   Hlavina W., Holzer T., Hsu F., Hua A., Hubbard T., Hunt A.,
RA   Jackson I., Jaffe D.B., Johnson L.S., Jones M., Jones T.A., Joy A.,
RA   Kamal M., Karlsson E.K., Karolchik D., Kasprzyk A., Kawai J.,
RA   Keibler E., Kells C., Kent W.J., Kirby A., Kolbe D.L., Korf I.,
RA   Kucherlapati R.S., Kulbokas E.J., Kulp D., Landers T., Leger J.P.,
RA   Leonard S., Letunic I., Levine R., Li J., Li M., Lloyd C., Lucas S.,
RA   Ma B., Maglott D.R., Mardis E.R., Matthews L., Mauceli E., Mayer J.H.,
RA   McCarthy M., McCombie W.R., McLaren S., McLay K., McPherson J.D.,
RA   Meldrim J., Meredith B., Mesirov J.P., Miller W., Miner T.L.,
RA   Mongin E., Montgomery K.T., Morgan M., Mott R., Mullikin J.C.,
RA   Muzny D.M., Nash W.E., Nelson J.O., Nhan M.N., Nicol R., Ning Z.,
RA   Nusbaum C., O'Connor M.J., Okazaki Y., Oliver K., Overton-Larty E.,
RA   Pachter L., Parra G., Pepin K.H., Peterson J., Pevzner P., Plumb R.,
RA   Pohl C.S., Poliakov A., Ponce T.C., Ponting C.P., Potter S., Quail M.,
RA   Reymond A., Roe B.A., Roskin K.M., Rubin E.M., Rust A.G., Santos R.,
RA   Sapojnikov V., Schultz B., Schultz J., Schwartz M.S., Schwartz S.,
RA   Scott C., Seaman S., Searle S., Sharpe T., Sheridan A., Shownkeen R.,
RA   Sims S., Singer J.B., Slater G., Smit A., Smith D.R., Spencer B.,
RA   Stabenau A., Stange-Thomann N., Sugnet C., Suyama M., Tesler G.,
RA   Thompson J., Torrents D., Trevaskis E., Tromp J., Ucla C.,
RA   Ureta-Vidal A., Vinson J.P., Von Niederhausern A.C., Wade C.M.,
RA   Wall M., Weber R.J., Weiss R.B., Wendl M.C., West A.P.,
RA   Wetterstrand K., Wheeler R., Whelan S., Wierzbowski J., Willey D.,
RA   Williams S., Wilson R.K., Winter E., Worley K.C., Wyman D., Yang S.,
RA   Yang S.P., Zdobnov E.M., Zody M.C., Lander E.S.;
RT   "Initial sequencing and comparative analysis of the mouse genome.";
RL   Nature 420:520-562(2002).
CC   -!- SUBUNIT: The nucleosome is a histone octamer containing two
CC       molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
CC       heterotetramer and two H2A-H2B heterodimers. The octamer wraps
CC       approximately 147 bp of DNA (By similarity).
CC   -!- SIMILARITY: Belongs to the histone H3 family.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC121292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00886201; -.
DR   Ensembl; ENSMUST00000159789; ENSMUSP00000125754; ENSMUSG00000060743.
DR   MGI; MGI:1097686; H3f3a.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR007125; Histone_core_D.
DR   InterPro; IPR000164; Histone_H3.
DR   Gene3D; G3DSA:1.10.20.10; Histone-fold; 1.
DR   PANTHER; PTHR11426; Histone_H3; 1.
DR   Pfam; PF00125; Histone; 1.
DR   PRINTS; PR00622; HISTONEH3.
DR   SMART; SM00428; H3; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
DR   PROSITE; PS00322; HISTONE_H3_1; 1.
DR   PROSITE; PS00959; HISTONE_H3_2; 1.
PE   3: Inferred from homology;
KW   Chromosome; DNA-binding; Nucleosome core; Nucleus.
SQ   SEQUENCE   119 AA;  13322 MW;  41364CCF4131C1FB CRC64;
     MARTKQTARK STGGKAPRKQ LATKAARKSA PSTGGVKKPH RYRPGTVALR EIRRYQKSTE
     LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY LVGLFEDTNL CAIHAKRVT
//
ID   E0CZ55_MOUSE            Unreviewed;       169 AA.
AC   E0CZ55;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   30-NOV-2010, entry version 3.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Phkb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC116323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC117185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC122830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00918452; -.
DR   Ensembl; ENSMUST00000160611; ENSMUSP00000125690; ENSMUSG00000036879.
DR   MGI; MGI:97578; Phkb.
DR   GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR   GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA:InterPro.
DR   GO; GO:0005977; P:glycogen metabolic process; IEA:InterPro.
DR   InterPro; IPR011613; Glyco_hydro_15-rel.
DR   InterPro; IPR008734; PHK_AB.
DR   PANTHER; PTHR10749; PHK_AB; 1.
DR   Pfam; PF00723; Glyco_hydro_15; 1.
PE   4: Predicted;
SQ   SEQUENCE   169 AA;  19316 MW;  9A3FA73612E3AF2E CRC64;
     MANSPDAAFS SPALLRSGSV YEPLKSINLP RPDNETLWDK LDHYYRIVKS TMLMYQSPTT
     GLFPTKTCGG EEKSKVHESL YCAAGAWALA LAYRRIDDDK GRTHELEHSA IKCMRGILYC
     YMRQADKVQQ FKQDPRPTTC LHSVFSVHTG DELLSYEEYG HLQILYFLK
//
ID   E0CZ72_MOUSE            Unreviewed;       743 AA.
AC   E0CZ72;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   08-MAR-2011, entry version 5.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Kif2a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Belongs to the kinesin-like protein family.
CC   -!- SIMILARITY: Contains 1 kinesin-motor domain.
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC154257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00969981; -.
DR   Ensembl; ENSMUST00000159772; ENSMUSP00000125644; ENSMUSG00000021693.
DR   MGI; MGI:108390; Kif2a.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   Gene3D; G3DSA:3.40.850.10; kinesin_motor; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_DOMAIN1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_DOMAIN2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Microtubule; Motor protein; Nucleotide-binding.
SQ   SEQUENCE   743 AA;  83861 MW;  996E5A0834A9BE0A CRC64;
     MATANFGKIQ IGIYVEIKRS DGRIHQAMVT SLNEDNESVT VEWIENGDTK GKEIDLESIF
     SLNPDLVPDE DIEPSPELPP PSSSSKVNKI VKNRRTVAAV KNDPPPRDNR VVGSARARPS
     QLPEQSSSAQ QNGSVSDISP VQAAKKEFGP PSRRKSNCVK EVEKLQEKRE KRRLQQQELR
     EKRAQDVDAT NPNYEIMCMI RDFRGSLDYR PLTTADPIDE HRICVCVRKR PLNKKETQMK
     DLDVITIPSK DVVMVHEPKQ KVDLTRYLEN QTFRFDYAFD DSAPNEMVYR FTARPLVETI
     FERGMATCFA YGQTGSGKTH TMGGDFSGKN QDCSKGIYAL AARDVFLMLK KPNYKKLELQ
     VYATFFEIYS GKVFDLLNRK TKLRVLEDGK QQVQVVGLQE REVKCVEDVL KLIDIGNSCR
     TSGQTSANAH SSRSHAVFQI ILRRKGKLHG KFSLIDLAGN ERGADTSSAD RQTRLEGAEI
     NKSLLALKEC IRALGRNKPH TPFRASKLTQ VLRDSFIGEN SRTCMIATIS PGMASCENTL
     NTLRYANRVK EFGISPSDIP FSQGGGSRPD LSPSYDYDDF SPSITRVKEL TVNPAAAGDV
     HPIMHHPPSQ IDDLETQWGV GSSPQRDDLK LLCEQNEEEV SPQLFTFHEA VSQMVEMEEQ
     VVEDHRAVFQ ESIRWIEDEK ALLEMTEEVD YDVDSYATQL EAILEQKIDI LTELRDKVKS
     FRAALQEEEQ ASKQINPKRP RAL
//
ID   PIEZ1_MOUSE             Reviewed;        2547 AA.
AC   E2JF22;
DT   11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   08-MAR-2011, entry version 4.
DE   RecName: Full=Protein PIEZO1;
DE   AltName: Full=Protein FAM38A;
GN   Name=Fam38a; Synonyms=Piezo1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=20813920; DOI=10.1126/science.1193270;
RA   Coste B., Mathur J., Schmidt M., Earley T.J., Ranade S., Petrus M.J.,
RA   Dubin A.E., Patapoutian A.;
RT   "Piezo1 and Piezo2 are essential components of distinct mechanically
RT   activated cation channels.";
RL   Science 330:55-60(2010).
CC   -!- FUNCTION: Component of mechanosensitive channel required for the
CC       mechanosensitive currents. Plays a key role in epithelial cell
CC       adhesion by maintaining integrin activation through R-Ras
CC       recruitment to the ER, most probably in its activated state, and
CC       subsequent stimulation of calpain signaling. Overexpression in
CC       multiple cell lines generates robust mechanosensitive cation
CC       currents that are non-selective, exhibit a linear current voltage
CC       relationship, and are sensitive to ruthenium red and gadolinium.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein. Endoplasmic reticulum-Golgi intermediate
CC       compartment membrane. Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in bladder, colon, kidney, lung, and
CC       skin.
CC   -!- MISCELLANEOUS: Piezo comes from the Greek 'piesi' meaning pressure
CC       (PubMed:20813920).
CC   -!- SIMILARITY: Belongs to the PIEZO family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; HQ215520; ADN28064.1; -; mRNA.
DR   IPI; IPI00620800; -.
DR   MGI; MGI:3603204; Fam38a.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033116; C:ER-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR   InterPro; IPR021999; DUF3595.
DR   Pfam; PF12166; DUF3595; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell membrane; Coiled coil; Endoplasmic reticulum;
KW   Glycoprotein; Ion transport; Ionic channel; Membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1   2547       Protein PIEZO1.
FT                                /FTId=PRO_0000403959.
FT   TRANSMEM      5     25       Helical; (Potential).
FT   TRANSMEM     27     47       Helical; (Potential).
FT   TRANSMEM     62     82       Helical; (Potential).
FT   TRANSMEM    120    140       Helical; (Potential).
FT   TRANSMEM    217    237       Helical; (Potential).
FT   TRANSMEM    250    270       Helical; (Potential).
FT   TRANSMEM    317    337       Helical; (Potential).
FT   TRANSMEM    435    455       Helical; (Potential).
FT   TRANSMEM    467    487       Helical; (Potential).
FT   TRANSMEM    520    540       Helical; (Potential).
FT   TRANSMEM    577    597       Helical; (Potential).
FT   TRANSMEM    608    628       Helical; (Potential).
FT   TRANSMEM    635    655       Helical; (Potential).
FT   TRANSMEM    687    707       Helical; (Potential).
FT   TRANSMEM    818    838       Helical; (Potential).
FT   TRANSMEM    847    867       Helical; (Potential).
FT   TRANSMEM    921    941       Helical; (Potential).
FT   TRANSMEM    982   1002       Helical; (Potential).
FT   TRANSMEM   1006   1023       Helical; (Potential).
FT   TRANSMEM   1038   1058       Helical; (Potential).
FT   TRANSMEM   1155   1175       Helical; (Potential).
FT   TRANSMEM   1179   1199       Helical; (Potential).
FT   TRANSMEM   1207   1227       Helical; (Potential).
FT   TRANSMEM   1232   1252       Helical; (Potential).
FT   TRANSMEM   1272   1292       Helical; (Potential).
FT   TRANSMEM   1678   1698       Helical; (Potential).
FT   TRANSMEM   1700   1720       Helical; (Potential).
FT   TRANSMEM   1734   1754       Helical; (Potential).
FT   TRANSMEM   1978   1998       Helical; (Potential).
FT   TRANSMEM   2019   2039       Helical; (Potential).
FT   TRANSMEM   2048   2068       Helical; (Potential).
FT   TRANSMEM   2077   2097       Helical; (Potential).
FT   TRANSMEM   2145   2165       Helical; (Potential).
FT   TRANSMEM   2193   2213       Helical; (Potential).
FT   TRANSMEM   2458   2478       Helical; (Potential).
FT   COILED     1334   1365       Potential.
FT   COMPBIAS      6    142       Leu-rich.
FT   COMPBIAS    157    170       Asp-rich.
FT   MOD_RES    1262   1262       N6-acetyllysine (By similarity).
FT   MOD_RES    1385   1385       Phosphoserine (By similarity).
FT   MOD_RES    1390   1390       Phosphoserine (By similarity).
FT   MOD_RES    1646   1646       Phosphoserine (By similarity).
FT   CARBOHYD     94     94       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    389    389       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   2547 AA;  292002 MW;  0C24CF18BDF502E3 CRC64;
     MEPHVLGAGL YWLLLPCTLL AASLLRFNAL SLVYLLFLLL LPWLPGPSRH SIPGHTGRLL
     RALLCLSLLF LVAHLAFQIC LHTVPHLDQF LGQNGSLWVK VSQHIGVTRL DLKDIFNTTR
     LVAPDLGVLL ASSLCLGLCG RLTRKAGQSR RTQELQDDDD DDDDDDEDID AAPAVGLKGA
     PALATKRRLW LASRFRVTAH WLLMTSGRTL VIVLLALAGI AHPSAFSSIY LVVFLAICTW
     WSCHFPLSPL GFNTLCVMVS CFGAGHLICL YCYQTPFIQD MLPPGNIWAR LFGLKNFVDL
     PNYSSPNALV LNTKHAWPIY VSPGILLLLY YTATSLLKLH KSCPSELRKE TPREDEEHEL
     ELDHLEPEPQ ARDATQGEMP MTTEPDLDNC TVHVLTSQSP VRQRPVRPRL AELKEMSPLH
     GLGHLIMDQS YVCALIAMMV WSIMYHSWLT FVLLLWACLI WTVRSRHQLA MLCSPCILLY
     GLTLCCLRYV WAMELPELPT TLGPVSLHQL GLEHTRYPCL DLGAMLLYLL TFWLLLRQFV
     KEKLLKKQKV PAALLEVTVA DTEPTQTQTL LRSLGELVTG IYVKYWIYVC AGMFIVVSFA
     GRLVVYKIVY MFLFLLCLTL FQVYYTLWRK LLRVFWWLVV AYTMLVLIAV YTFQFQDFPT
     YWRNLTGFTD EQLGDLGLEQ FSVSELFSSI LIPGFFLLAC ILQLHYFHRP FMQLTDLEHV
     PPPGTRHPRW AHRQDAVSEA PLLEHQEEEE VFREDGQSMD GPHQATQVPE GTASKWGLVA
     DRLLDLAASF SAVLTRIQVF VRRLLELHVF KLVALYTVWV ALKEVSVMNL LLVVLWAFAL
     PYPRFRPMAS CLSTVWTCII IVCKMLYQLK IVNPHEYSSN CTEPFPNNTN LQPLEINQSL
     LYRGPVDPAN WFGVRKGYPN LGYIQNHLQI LLLLVFEAVV YRRQEHYRRQ HQQAPLPAQA
     VCADGTRQRL DQDLLSCLKY FINFFFYKFG LEICFLMAVN VIGQRMNFMV ILHGCWLVAI
     LTRRRREAIA RLWPNYCLFL TLFLLYQYLL CLGMPPALCI DYPWRWSKAI PMNSALIKWL
     YLPDFFRAPN STNLISDFLL LLCASQQWQV FSAERTEEWQ RMAGINTDHL EPLRGEPNPI
     PNFIHCRSYL DMLKVAVFRY LFWLVLVVVF VAGATRISIF GLGYLLACFY LLLFGTTLLQ
     KDTRAQLVLW DCLILYNVTV IISKNMLSLL SCVFVEQMQS NFCWVIQLFS LVCTVKGYYD
     PKEMMTRDRD CLLPVEEAGI IWDSICFFFL LLQRRIFLSH YFLHVSADLK ATALQASRGF
     ALYNAANLKS INFHRQIEEK SLAQLKRQMK RIRAKQEKYR QSQASRGQLQ SKDPQDPSQE
     PGPDSPGGSS PPRRQWWRPW LDHATVIHSG DYFLFESDSE EEEEALPEDP RPAAQSAFQM
     AYQAWVTNAQ TVLRQRRERA RQERAEQLAS GGDLNPDVEP VDVPEDEMAG RSHMMQRVLS
     TMQFLWVLGQ ATVDGLTRWL RAFTKHHRTM SDVLCAERYL LTQELLRVGE VRRGVLDQLY
     VGEDEATLSG PVETRDGPST ASSGLGAEEP LSSMTDDTSS PLSTGYNTRS GSEEIVTDAG
     DLQAGTSLHG SQELLANART RMRTASELLL DRRLHIPELE EAERFEAQQG RTLRLLRAGY
     QCVAAHSELL CYFIIILNHM VTASAASLVL PVLVFLWAML TIPRPSKRFW MTAIVFTEVM
     VVTKYLFQFG FFPWNSYVVL RRYENKPYFP PRILGLEKTD SYIKYDLVQL MALFFHRSQL
     LCYGLWDHEE DRYPKDHCRS SVKDREAKEE PEAKLESQSE TGTGHPKEPV LAGTPRDHIQ
     GKGSIRSKDV IQDPPEDLKP RHTRHISIRF RRRKETPGPK GTAVMETEHE EGEGKETTER
     KRPRHTQEKS KFRERMKAAG RRLQSFCVSL AQSFYQPLQR FFHDILHTKY RAATDVYALM
     FLADIVDIII IIFGFWAFGK HSAATDIASS LSDDQVPQAF LFMLLVQFGT MVIDRALYLR
     KTVLGKLAFQ VVLVVAIHIW MFFILPAVTE RMFSQNAVAQ LWYFVKCIYF ALSAYQIRCG
     YPTRILGNFL TKKYNHLNLF LFQGFRLVPF LVELRAVMDW VWTDTTLSLS NWMCVEDIYA
     NIFIIKCSRE TEKKYPQPKG QKKKKIVKYG MGGLIILFLI AIIWFPLLFM SLIRSVVGVV
     NQPIDVTVTL KLGGYEPLFT MSAQQPSIVP FTPQAYEELS QQFDPYPLAM QFISQYSPED
     IVTAQIEGSS GALWRISPPS RAQMKQELYN GTADITLRFT WNFQRDLAKG GTVEYTNEKH
     TLELAPNSTA RRQLAQLLEG RPDQSVVIPH LFPKYIRAPN GPEANPVKQL QPDEEEDYLG
     VRIQLRREQV GTGASGEQAG TKASDFLEWW VIELQDCKAD CNLLPMVIFS DKVSPPSLGF
     LAGYGIVGLY VSIVLVVGKF VRGFFSEISH SIMFEELPCV DRILKLCQDI FLVRETRELE
     LEEELYAKLI FLYRSPETMI KWTRERE
//
ID   E3UVT8_MOUSE            Unreviewed;      1126 AA.
AC   E3UVT8;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   08-MAR-2011, entry version 2.
DE   SubName: Full=Solute carrier family 4 sodium bicarbonate cotransporter member 7 variant NBCn1-J;
GN   Name=slc4a7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Ovary;
RA   Liu Y., Chen L.-M.;
RT   "Cloning and identification of two novel mouse NBCn1 splice
RT   variants.";
RL   Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; HM624050; ADO51787.1; -; mRNA.
DR   IPI; IPI00664442; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
DR   InterPro; IPR011531; HCO3_transpt_C.
DR   InterPro; IPR013769; HCO3_transpt_cyt.
DR   InterPro; IPR003020; HCO3_transpt_euk.
DR   InterPro; IPR003024; Na/HCO3_transpt.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   Gene3D; G3DSA:3.40.1100.10; HCO3_transpt_cyt; 1.
DR   PANTHER; PTHR11453; HCO3_transpt_euk; 1.
DR   Pfam; PF07565; Band_3_cyto; 1.
DR   Pfam; PF00955; HCO3_cotransp; 1.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   PRINTS; PR01232; NAHCO3TRSPRT.
DR   SUPFAM; SSF55804; PTrfase/Anion_transptr; 1.
DR   TIGRFAMs; TIGR00834; ae; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1126 AA;  126875 MW;  CAC77C43467F5A35 CRC64;
     MERFQLARKL HGPDEEAVVD LGKTSSTVNT KFEKEELESH RAVYVGVHVP FSKESRRRHK
     HRGHKHHHRR RKDKDSDKED GRESPSYDTP SQRVQFILGT EDDDEEHIPH DLFTEMDELC
     YRDGEEYEWK ETARWLKFEE DVEDGGDRWS KPYVATLSLH SLFELRSCIL NGTVMLDMRA
     STLDEIADMV LDNMIASGQL DDSIRENVRE ALLKRHHHQN EKRFTSRIPL VRSFADIGKK
     HSDPHLLERN GILASPQSAP GNLDNSKSGE MKGNGSGGSR ENSTVDFSKV DMNFMRKIPT
     GAEASNVLVG EVDFLERPII AFVRLAPAVL LSGLTEVPVP TRFLFLLLGP AGKAPQYHEI
     GRSIATLMTD EIFHDVAYKA KDRNDLLSGI DEFLDQVTVL PPGEWDPSIR IEPPKSVPSQ
     EKRKIPVFPN GSAAMSVDPP KEDDHHAGPE LQRTGRLFGG LILDIKRKAP FFLSDFKDAL
     SLQCLASILF LYCACMSPVI TFGGLLGEAT EGRISAIESL FGASLTGIAY SLFAGQPLTI
     LGSTGPVLVF EKILFKFCRD YHLSYLSLRT SIGLWTSFLC IVLVATDASS LVCYITRFTE
     EAFAALICII FIYEALEKLF HLGEIYAFNM HNNLDELTSY TCVCAEPSNP SNETLELWKR
     KNITAYSVSW GNLTVSECKT FHGMFVGSAC GPHGPYVPDV LFWCVVLFFT TFFLSSFLKQ
     FKTKRYFPTK VRSTISDFAV FLTIVIMVAI DYLVGIPSPK LHVPEKFEPT DPSRGWIISP
     LGDNPWWTLL IAAVPALLCT ILIFMDQQIT AVIINRKEHK LKKGAGYHLD LLMVGVMLGV
     CSIMGLPWFV AATVLSISHV NSLKVESECS APGEQPKFLG IREQRVTGLM IFILMGLSVF
     MTSVLKFIPM PVLYGVFLYM GVSSLKGIQF FDRIKLFGMP AKHQPDLIYL RYVPLWKVHV
     FTVVQLTCLV LLWVIKASAA AVVFPMMVLA LVFVRKLMDL CFTKRELSWL DDLMPESKKK
     KEDDKKKKEK EEAERMLQDD EDTVHLPFER GSLLQIPVKT LKYSIDPSVV NISDEMAKTA
     QWKALSMNTE NAKVTRPNTS PEKPVSVTIN FEDEPSKKYM DAETSL
//
ID   E3VRY9_MOUSE            Unreviewed;      1192 AA.
AC   E3VRY9;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   08-MAR-2011, entry version 2.
DE   SubName: Full=Large conductance Ca2+-activated potassium channel DEC variant 8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBA/J; TISSUE=Cochlea;
RA   Sakai Y., Sokolowski B.;
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; HQ221748; ADO63675.1; -; mRNA.
DR   IPI; IPI00410905; -.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0015269; F:calcium-activated potassium channel activity; IEA:InterPro.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003929; K_chnl_Ca-activ_BK_asu.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR003148; RCK_N.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 2.
DR   Pfam; PF03493; BK_channel_a; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02254; TrkA_N; 1.
DR   PRINTS; PR01449; BKCHANNELA.
DR   PRINTS; PR00169; KCHANNEL.
PE   2: Evidence at transcript level;
KW   Ion transport; Ionic channel; Membrane; Potassium; Potassium channel;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport.
SQ   SEQUENCE   1192 AA;  134110 MW;  DD013F152F70F9F1 CRC64;
     MDALIIPVTM EVPCDSRGQR MWWAFLASSM VTFFGGLFII LLWRTLKYLW TVCCHCGGKT
     KEAQKINNGS SQADGTLKPV DEKEEVVAAE VGWMTSVKDW AGVMISAQTL TGRVLVVLVF
     ALSIGALVIY FIDSSNPIES CQNFYKDFTL QIDMAFNVFF LLYFGLRFIA ANDKLWFWLE
     VNSVVDFFTV PPVFVSVYLN RSWLGLRFLR ALRLIQFSEI LQFLNILKTS NSIKLVNLLS
     IFISTWLTAA GFIHLVENSG DPWENFQNNQ ALTYWECVYL LMVTMSTVGY GDVYAKTTLG
     RLFMVFFILG GLAMFASYVP EIIELIGNRK KYGGSYSAVS GRKHIVVCGH ITLESVSNFL
     KDFLHKDRDD VNVEIVFLHN ISPNLELEAL FKRHFTQVEF YQGSVLNPHD LARVKIESAD
     ACLILANKYC ADPDAEDASN IMRVISIKNY HPKIRIITQM LQYHNKAHLL NIPSWNWKEG
     DDAICLAELK LGFIAQSCLA QGLSTMLANL FSMRSFIKIE EDTWQKYYLE GVSNEMYTEY
     LSSAFVGLSF PTVCELCFVK LKLLMIAIEY KSANRESRIL INPGNHLKIQ EGTLGFFIAS
     DAKEVKRAFF YCKACHDDVT DPKRIKKCGC RRLEDEQPPT LSPKKKQRNG GMRNSPNTSP
     KLMRHDPLLI PGNDQIDNMD SNVKKYDSTG MFHWCAPKEI EKVILTRSEA AMTVLSGHVV
     VCIFGDVSSA LIGLRNLVMP LRASNFHYHE LKHIVFVGSI EYLKREWETL HNFPKVSILP
     GTPLSRADLR AVNINLCDMC VILSANQNNI DDTSLQDKEC ILASLNIKSM QFDDSIGVLQ
     ANSQGFTPPG MDRSSPDNSP VHGMLRQPSI TTGVNIPIIT ELAKPGKLPL VSVNQEKNSG
     THILMITELV NDTNVQFLDQ DDDDDPDTEL YLTQPFACGT AFAVSVLDSL MSATYFNDNI
     LTLIRTLVTG GATPELEALI AEENALRGGY STPQTLANRD RCRVAQLALL DGPFADLGDG
     GCYGDLFCKA LKTYNMLCFG IYRLRDAHLS TPSQCTKRYV ITNPPYEFEL VPTDLIFCLM
     QFDHNAGQSR ASLSHSSHSS QSSSKKSSSV HSIPSTANRP NRPKSRESRD KQNATRMTRM
     GQEKKWFTDE PDNAYPRNIQ IKPMSTHMAN QINQYKSTSS LIPPIREVED EC
//
ID   E3VRZ6_MOUSE            Unreviewed;      1142 AA.
AC   E3VRZ6;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   08-MAR-2011, entry version 2.
DE   SubName: Full=Large conductance Ca2+-activated potassium channel ERL variant 16;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBA/J; TISSUE=Cochlea;
RA   Sakai Y., Sokolowski B.;
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; HQ221755; ADO63682.1; -; mRNA.
DR   IPI; IPI00973606; -.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0015269; F:calcium-activated potassium channel activity; IEA:InterPro.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003929; K_chnl_Ca-activ_BK_asu.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR003148; RCK_N.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 3.
DR   Pfam; PF03493; BK_channel_a; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02254; TrkA_N; 1.
DR   PRINTS; PR01449; BKCHANNELA.
DR   PRINTS; PR00169; KCHANNEL.
PE   2: Evidence at transcript level;
KW   Ion transport; Ionic channel; Membrane; Potassium; Potassium channel;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport.
SQ   SEQUENCE   1142 AA;  128553 MW;  FBEAB9C4D4E210C3 CRC64;
     MDALIIPVTM EVPCDSRGQR MWWAFLASSM VTFFGGLFIV LLWRTLKYLW TVCCHCGGKT
     KEAQKINNGS SQADGTLKPV DEKEEVVAAE VGWMTSVKDW AGVMISAQTL TGRVLVVLVF
     ALSIGALVIY FIDSSNPIES CQNFYKDFTL QIDMAFNVFF LLYFGLRFIA ANDKLWFWLE
     VNSVVDFFTV PPVFVSVYLN RSWLGLRFLR ALRLIQFSEI LQFLNILKTS NSIKLVNLLS
     IFISTWLTAA GFIHLVENSG DPWENFQNNQ ALTYWECVYL LMVTMSTVGY GDVYAKTTLG
     RLFMVFFILG GLAMFASYVP EIIELIGNRK KYGGSYSAVS GRKHIVVCGH ITLESVSNFL
     KDFLHKDRDD VNVEIVFLHN ISPNLELEAL FKRHFTQVEF YQGSVLNPHD LARVKIESAD
     ACLILANKYC ADPDAEDASN IMRVISIKNY HPKIRIITQM LQYHNKAHLL NIPSWNWKEG
     DDAICLAELK LGFIAQSCLA QGLSTMLANL FSMRSFIKIE EDTWQKYYLE GVSNEMYTEY
     LSSAFVGLSF PTVCELCFVK LKLLMIAIEY KSANRESRIL INPGNHLKIQ EGTLGFFIAS
     DAKEVKRAFF YCKACHDDVT DPKRIKKCGC RRLKVEARAR YHKDPFMHKN ATPNSPHVPK
     PVEDEQPPTL SPKKKQRNGG MRNSPNTSPK LMRHDPLLIP GNDQIDNMDS NVKKYDSTGM
     FHWCAPKEIE KVILTRSEAA MTVLSGHVVV CIFGDVSSAL IGLRNLVMPL RASNFHYHEL
     KHIVFVGSIE YLKREWETLH NFPKVSILPG TPLSRADLRA VNINLCDMCV ILSANQNNID
     DTSLQDKECI LASLNIKSMQ FDDSIGVLQA NSQGFTPPGM DRSSPDNSPV HGMLRQPSIT
     TGVNIPIITE LVNDTNVQFL DQDDDDDPDT ELYLTQPFAC GTAFAVSVLD SLMSATYFND
     NILTLIRTLV TGGATPELEA LIAEENALRG GYSTPQTLAN RDRCRVAQLA LLDGPFADLG
     DGGCYGDLFC KALKTYNMLC FGIYRLRDAH LSTPSQCTKR YVITNPPYEF ELVPTDLIFC
     LMQFDHNAGQ SRASLSHSSH SSQSSSKKSS SVHSIPSTAN RPNRPKSRES RDKQKYVQEE
     RL
//
ID   E3VRZ7_MOUSE            Unreviewed;      1175 AA.
AC   E3VRZ7;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   08-MAR-2011, entry version 2.
DE   SubName: Full=Large conductance Ca2+-activated potassium channel VYR variant 20;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBA/J; TISSUE=Cochlea;
RA   Sakai Y., Sokolowski B.;
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; HQ221756; ADO63683.1; -; mRNA.
DR   IPI; IPI00410904; -.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0015269; F:calcium-activated potassium channel activity; IEA:InterPro.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003929; K_chnl_Ca-activ_BK_asu.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR003148; RCK_N.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 3.
DR   Pfam; PF03493; BK_channel_a; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02254; TrkA_N; 1.
DR   PRINTS; PR01449; BKCHANNELA.
DR   PRINTS; PR00169; KCHANNEL.
PE   2: Evidence at transcript level;
KW   Ion transport; Ionic channel; Membrane; Potassium; Potassium channel;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport.
SQ   SEQUENCE   1175 AA;  132353 MW;  6BC5CCAB95B17056 CRC64;
     MDALIIPVTM EVPCDSRGQR MWWAFLASSM VTFFGGLFII LLWRTLKYLW TVCCHCGGKT
     KEAQKINNGS SQADGTLKPV DEKEEVVAAE VGWMTSVKDW AGVMISAQTL TGRVLVVLVF
     ALSIGALVIY FIDSSNPIES CQNFYKDFTL QIDMAFNVFF LLYFGLRFIA ANDKLWFWLE
     VNSVVDFFTV PPVFVSVYLN RSWLGLRFLR ALRLIQFSEI LQFLNILKTS NSIKLVNLLS
     IFISTWLTAA GFIHLVENSG DPWENFQNNQ ALTYWECVYL LMVTMSTVGY GDVYAKTTLG
     RLFMAFFILG GLAMFASYVP EIIELIGNRK KYGGSYSAVS GRKHIVVCGH ITLESVSNFL
     KDFLHKDRDD VNVEIVFLHN ISPNLELEAL FKRHFTQVEF YQGSVLNPHD LARVKIESAD
     ACLILANKYC ADPDAEDASN IMRVISIKNY HPKIRIITQM LQYHNKAHLL NIPSWNWKEG
     DDAICLAELK LGFIAQSCLA QGLSTMLANL FSMRSFIKIE EDTWQKYYLE GVSNEMYTEY
     LSSAFVGLSF PTVCELCFVK LKLLMIAIEY KSANRESRSR KRILINPGNH LKIQEGTLGF
     FIASDAKEVK RAFFYCKACH DDVTDPKRIK KCGCRRPKMS IYKRMRRACC FDCGRSERDC
     SCMSGRVRGN VDTLERTFPL SSVSVNDCST SFRAFEDEQP PTLSPKKKQR NGGMRNSPNT
     SPKLMRHDPL LIPGNDQIDN MDSNVKKYDS TGMFHWCAPK EIEKVILTRS EAAMTVLSGH
     VVVCIFGDVS SALIGLRNLV MPLRASNFHY HELKHIVFVG SIEYLKREWE TLHNFPKVSI
     LPGTPLSRAD LRAVNINLCD MCVILSANQN NIDDTSLQDK ECILASLNIK SMQFDDSIGV
     LQANSQGFTP PGMDRSSPDN SPVHGMLRQP SITTGVNIPI ITELVNDTNV QFLDQDDDDD
     PDTELYLTQP FACGTAFAVS VLDSLMSATY FNDNILTLIR TLVTGGATPE LEALIAEENA
     LRGGYSTPQT LANRDRCRVA QLALLDGPFA DLGDGGCYGD LFCKALKTYN MLCFGIYRLR
     DAHLSTPSQC TKRYVITNPP YEFELVPTDL IFCLMQFDHN AGQSRASLSH SSHSSQSSSK
     KSSSVHSIPS TANRPNRPKS RESRDKQNRK EMVYR
//
ID   E3VWA1_MOUSE            Unreviewed;      1026 AA.
AC   E3VWA1;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   08-MAR-2011, entry version 2.
DE   SubName: Full=Electrogenic sodium bicarbonate cotransporter NBCe1 variant D;
GN   Name=Slc4a4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL; TISSUE=Epididymis;
RA   Xu J.-Y., Liu Y., Wang D.-K., Chen L.-M.;
RT   "Cloning and identification of NBCe1 variant D from mouse reproductive
RT   tract tissue.";
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; HQ285250; ADP37962.1; -; mRNA.
DR   IPI; IPI00662028; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
DR   InterPro; IPR011531; HCO3_transpt_C.
DR   InterPro; IPR013769; HCO3_transpt_cyt.
DR   InterPro; IPR003020; HCO3_transpt_euk.
DR   InterPro; IPR003024; Na/HCO3_transpt.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   PANTHER; PTHR11453; HCO3_transpt_euk; 1.
DR   Pfam; PF07565; Band_3_cyto; 1.
DR   Pfam; PF00955; HCO3_cotransp; 1.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   PRINTS; PR01232; NAHCO3TRSPRT.
DR   SUPFAM; SSF55804; PTrfase/Anion_transptr; 1.
DR   TIGRFAMs; TIGR00834; ae; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1026 AA;  115163 MW;  CB78D1D11B3F945C CRC64;
     MSTENVEGKP NNLGERGRAR SSTFLRVFQP MFNHSIFTSA VSPAAERIRF ILGEEDDSPA
     PPQLFTELDE LLAVDGQEME WKETARWIKF EEKVEQGGER WSKPHVATLS LHSLFELRTC
     MEKGSIMLDR EASSLPQLVE MIADHQIETG LLKPDLKDKV TYTLLRKHRH QTKKSNLRSL
     ADIGKTVSSA SSPAMTHRNL TSSSLNDISD KPEKDQLKNK FMKKLPRDAE ASNVLVGEVD
     FLDTPFIAFV RLQQAVMLGA LTEVPVPTRF LFILLGPKGK AKSYHEIGRA IATLMSDEVF
     HDIAYKAKDR HDLIAGIDEF LDEVIVLPPG EWDPTIRIEP PKSLPSSDKR KNMYSGGENV
     QMNGDTPHDG GHGGGGHGDC EELQRTGRFC GGLIKDIKRK APFFASDFYD ALNIQALSAI
     LFIYLATVTN AITFGGLLGD ATDNMQGVLE SFLGTAVSGA IFCLFAGQPL TILSSTGPVL
     VFERLLFNFS KDHNFDYLEF RLWIGLWSAF MCLVLVATDA SFLVQYFTRF TEEGFSSLIS
     FIFIYDAFKK MIKLADYYPI NSDFKVGYNT HFSCACLPPD PVNLSVSNDT TLAPEDLPTI
     SSTDMYHNVT FDWAYLSKKE CVKYGGKLVG NNCDFVPDIT LMSFILFLGT YTSSMAMKKF
     KTSRYFPTTA RKLISDFAII LSILIFCVID ALVGVDTPKL IVPSEFKPTS PNRGWFVPPF
     GGNPWWVCLA AAIPALLVTI LIFMDQQITA VIVNRKEHKL KKGAGYHLDL FWVAILMVVC
     SFMALPWYVA ATVISIAHID SLKMETETSA PGEQPKFLGV REQRVTGTLV FILTGLSVFM
     APILKFIPMP VLYGVFLYMG VASLNGVQFM DRLKLLLMPL KHQPDFIYLR HVPLRRVHLF
     TFLQVLCLAL LWILKSTVAA IIFPVMILAL VAVRKGMDYL FSQHDLSFLD DVIPEKDKKK
     KEDEKKKKKK KGSLDSDNDD SDCPYSEKVP SIKIPMDIME QQPFLSDNKP LDRERSSTFL
     ERHTSC
//
ID   E3W999_MOUSE            Unreviewed;      2611 AA.
AC   E3W999;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   08-MAR-2011, entry version 3.
DE   SubName: Full=Uncharacterized protein;
GN   Name=Dst;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (DEC-2010) to UniProtKB.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=22354682; PubMed=12466850; DOI=10.1038/nature01262;
RA   Waterston R.H., Lindblad-Toh K., Birney E., Rogers J., Abril J.F.,
RA   Agarwal P., Agarwala R., Ainscough R., Alexandersson M., An P.,
RA   Antonarakis S.E., Attwood J., Baertsch R., Bailey J., Barlow K.,
RA   Beck S., Berry E., Birren B., Bloom T., Bork P., Botcherby M.,
RA   Bray N., Brent M.R., Brown D.G., Brown S.D., Bult C., Burton J.,
RA   Butler J., Campbell R.D., Carninci P., Cawley S., Chiaromonte F.,
RA   Chinwalla A.T., Church D.M., Clamp M., Clee C., Collins F.S.,
RA   Cook L.L., Copley R.R., Coulson A., Couronne O., Cuff J., Curwen V.,
RA   Cutts T., Daly M., David R., Davies J., Delehaunty K.D., Deri J.,
RA   Dermitzakis E.T., Dewey C., Dickens N.J., Diekhans M., Dodge S.,
RA   Dubchak I., Dunn D.M., Eddy S.R., Elnitski L., Emes R.D., Eswara P.,
RA   Eyras E., Felsenfeld A., Fewell G.A., Flicek P., Foley K.,
RA   Frankel W.N., Fulton L.A., Fulton R.S., Furey T.S., Gage D.,
RA   Gibbs R.A., Glusman G., Gnerre S., Goldman N., Goodstadt L.,
RA   Grafham D., Graves T.A., Green E.D., Gregory S., Guigo R., Guyer M.,
RA   Hardison R.C., Haussler D., Hayashizaki Y., Hillier L.W., Hinrichs A.,
RA   Hlavina W., Holzer T., Hsu F., Hua A., Hubbard T., Hunt A.,
RA   Jackson I., Jaffe D.B., Johnson L.S., Jones M., Jones T.A., Joy A.,
RA   Kamal M., Karlsson E.K., Karolchik D., Kasprzyk A., Kawai J.,
RA   Keibler E., Kells C., Kent W.J., Kirby A., Kolbe D.L., Korf I.,
RA   Kucherlapati R.S., Kulbokas E.J., Kulp D., Landers T., Leger J.P.,
RA   Leonard S., Letunic I., Levine R., Li J., Li M., Lloyd C., Lucas S.,
RA   Ma B., Maglott D.R., Mardis E.R., Matthews L., Mauceli E., Mayer J.H.,
RA   McCarthy M., McCombie W.R., McLaren S., McLay K., McPherson J.D.,
RA   Meldrim J., Meredith B., Mesirov J.P., Miller W., Miner T.L.,
RA   Mongin E., Montgomery K.T., Morgan M., Mott R., Mullikin J.C.,
RA   Muzny D.M., Nash W.E., Nelson J.O., Nhan M.N., Nicol R., Ning Z.,
RA   Nusbaum C., O'Connor M.J., Okazaki Y., Oliver K., Overton-Larty E.,
RA   Pachter L., Parra G., Pepin K.H., Peterson J., Pevzner P., Plumb R.,
RA   Pohl C.S., Poliakov A., Ponce T.C., Ponting C.P., Potter S., Quail M.,
RA   Reymond A., Roe B.A., Roskin K.M., Rubin E.M., Rust A.G., Santos R.,
RA   Sapojnikov V., Schultz B., Schultz J., Schwartz M.S., Schwartz S.,
RA   Scott C., Seaman S., Searle S., Sharpe T., Sheridan A., Shownkeen R.,
RA   Sims S., Singer J.B., Slater G., Smit A., Smith D.R., Spencer B.,
RA   Stabenau A., Stange-Thomann N., Sugnet C., Suyama M., Tesler G.,
RA   Thompson J., Torrents D., Trevaskis E., Tromp J., Ucla C.,
RA   Ureta-Vidal A., Vinson J.P., Von Niederhausern A.C., Wade C.M.,
RA   Wall M., Weber R.J., Weiss R.B., Wendl M.C., West A.P.,
RA   Wetterstrand K., Wheeler R., Whelan S., Wierzbowski J., Willey D.,
RA   Williams S., Wilson R.K., Winter E., Worley K.C., Wyman D., Yang S.,
RA   Yang S.P., Zdobnov E.M., Zody M.C., Lander E.S.;
RT   "Initial sequencing and comparative analysis of the mouse genome.";
RL   Nature 420:520-562(2002).
CC   -!- CAUTION: The sequence shown here is derived from an Ensembl
CC       automatic analysis pipeline and should be considered as
CC       preliminary data.
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DR   EMBL; AC123072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC124386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC127433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00973613; -.
DR   Ensembl; ENSMUST00000027309; ENSMUSP00000027309; ENSMUSG00000026131.
DR   MGI; MGI:104627; Dst.
DR   GO; GO:0060053; C:neurofilament cytoskeleton; IDA:MGI.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:MGI.
DR   GO; GO:0008090; P:retrograde axon cargo transport; IMP:MGI.
DR   InterPro; IPR001101; Plectin_repeat.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Pfam; PF00681; Plectin; 5.
DR   Pfam; PF00435; Spectrin; 1.
DR   SMART; SM00250; PLEC; 11.
DR   SMART; SM00150; SPEC; 3.
PE   4: Predicted;
KW   Repeat.
SQ   SEQUENCE   2611 AA;  301795 MW;  E52A3C528766F478 CRC64;
     MRISCPFIVV PLINSCISFS NESLDGHRLD MLQQIATRVQ RDSVSCEDKL ILARNALQSD
     SKRLESGVQF QNEAEIAGYI LECENLLRQH VIDVQILIDG KYYQADQLVQ RVAKLRDEIM
     ALRNECSSVY SKGRMLTTEQ TKLMISGITQ SLNSGFAQTL HPSLNSGLTQ SLTPSLTSSS
     VTSGLSSGMT SRLTPSVTPV YAPGFPSVVA PNFSLGVEPN SLQTLKLMQI RKPLLKSSLL
     DQNLTEEEVN MKFVQDLLNW VDEMQVQLDR TEWGSDLPSV ESHLENHKNV HRAIEEFESS
     LKEAKISEIQ MTAPLKLSYT DKLHRLESQY AKLLNTSRNQ ERHLDTLHNF VTRATNELIW
     LNEKEESEVA YDWSERNSSV ARKKSYHAEL MRELEQKEES IKAVQEIAEQ LLLENHPARL
     TIEAYRAAMQ TQWSWILQLC QCVEQHIQEN SAYFEFFNDA KEATDYLRNL KDAIQRKYSC
     DRSSSIHKLE DLVQESMEKE ELLQYRSVVA GLMGRAKTVV QLKPRNPDNP LKTSIPIKAI
     CDYRQIEITI YKDDECVLAN NSHRAKWKVI SPTGNEAMVP SVCFTVPPPN KEAVDFANRI
     EQQYQSVLTL WHESHINMKS VVSWHYLVNE IDRIRASNVA SIKTMLPGEH QQVLSNLQSR
     LEDFLEDSQE SQIFSGSDIS QLEKEVSVCR KYYQELLKSA EREEQEESVY NLYISEVRNI
     RLRLESCEDR LIRQIRTPLE RDDLHESMLR ITEQEKLKKE LDRLKDDLGT ITNKCEEFFS
     QAADSPSVPA LRSELSVVIQ SLSQIYSMSS TYIEKLKTVN LVLKNTQAAE ALVKLYETKL
     CEEEAVIADK NNIENLMSTL KQWRSEVDEK REVFHALEDE LQKAKAISDE MFKTHKERDL
     DFDWHKEKAD QLVERWQSVH VQIDNRLRDL EGIGKSLKHY RDSYHPLDDW IQHIETTQRK
     IQENQPENSK ALALQLNQQK MLVSEIEVKQ SKMDECQKYS EQYSAAVKDY ELQTMTYRAM
     VESQQKSPVK RRRIQSSADL VIQEFMDLRT RYTALVTLMT QYIKFAGDSL KRLEEEEMKR
     SKENSEHGAY SDLLQRQRAT MVENSKLTGK ISELETMVAE LKKQKSRVEE ELPKVKEAAE
     NELRKQQRNV EDIALQKLRA ESEAKQYRRE LETIVREKEA AERELERVRQ LTAEAEARRA
     AVEENLRNFR SQLQENTFTR QTLEDHLRRK DSSLSDLEQQ KRALVEELQR KRDHEEELLR
     LVKQMERDLA FQKQVAEKQL KEKQKVELEA RRKITEIQFS CRESAAVAQA RPQREQGRQK
     EEELKQQVDE LTLANRKAEK EMRELKYELS AVQLEKASSE EKARLLKDKL DETNNTLKCL
     KEDLERKDQA QERYSQQLRD LGRQLNQTTD KAEEVRQEAN DLKKIKHTYQ LELESLHQEK
     GKLQREVDRV TRAHALAERN IQCLNSQVHA SRDEKDLSEE RRRLCQRKSD HLKEEFERSH
     AQLLQNIQAE KENNDKIQKL NKELEKSNEC AETLKQKVDE LTRQNNETKL MMQRIQAESK
     NIVREKQAIQ QRCEVLRIQA DGFKDQLRNT NEHLHKQTKT EQDFHRKIKS LEDDLAQSQN
     LVSEFKQKCD QQSMIIQKTE KEVRSLSAEL SASKEEKRRE EQKAQLQRAQ VQELNDRLKR
     VQDELHLKTI EEQMTHRKMI LLQEESDKFK RSADEFRKKM EKLMESKVVT ETDLSGIKHD
     FVSLQRENFR AQENAKLWET NIRELERQLQ CYREKMQQGP PVEANHYQKC RRLEEELLAQ
     RREVENLKQK MDQQIKEHEH QLLRLQCEIQ KKSTTQDHTF ASAFDTAGRE CHHPAEISPG
     NSGHLNLKTR LPLSRWTQEP HQTEGKWPHR AAEQLPKEVQ FRQPGAPLDR ESSQPCYSEY
     FSQTSTELQI TFDDKNPITR LSELETMREQ ALHPSRPPVT YQDDKLEREL VKLLTPLEIA
     KNKQCGMHTE VTTLKQEKRL GSSAGGWMLE GCRTSGGLKG DFLKKSVEPE ASPSLDLNQA
     CSVRDEEFQF QGLRHTVTGR QLVEAKLLDM RTVEQLRLGL KTVEEVQRSL SKFLTKATSI
     AGLYLESSKE KMSFTSAAQK IIIDKMIALA FLEAQAATGF IIDPVSGQTY CVEDAVLHGI
     VDPEFRSRLL EAEKAVLGYS HASKTLSVFQ AMENRMLDRK KGKHILEAQI ASGGVIDPVR
     GVRVPPEMAV QQGLLNNAVL QFLHEPSSNT RVFPNPNNKQ ALYYSELLQI CVFDVDCQCF
     LLPFGEREIS NLNIEKTHKI AVVDTKTGAE LTAFEAFQRN LIDKGIYLEL SGQQYQWKEA
     TFFDSYGHPS HMLTDTKTGL QFNISEAVEQ GTLDKALVQK YQEGLTTLTE LADFLLSKVV
     PKKDLHSPIA GYWLTASGER ISLLKASRRN LVDRVTALRC LEAQICTGGI IDPLTGKKYR
     VAEALHRGLV DEGFAQQLRQ CELVITGISH PVSNKMMSVV EAVNANIISK EMGMRCLEFQ
     YLTGGLIEPK VFSRLTIEEA LHVGIIDVLI ATRLKDQKSY VRDIMCPQTK RKLTYKEALE
     KADFDFHTGL KLLEVSEPLG TGISNLYYSS Q
//
ID   S1PR1_MOUSE             Reviewed;         382 AA.
AC   O08530; Q9R235;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 2.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Sphingosine 1-phosphate receptor 1;
DE            Short=S1P receptor 1;
DE            Short=S1P1;
DE   AltName: Full=Endothelial differentiation G-protein coupled receptor 1;
DE   AltName: Full=Lysophospholipid receptor B1;
DE   AltName: Full=Sphingosine 1-phosphate receptor Edg-1;
DE            Short=S1P receptor Edg-1;
DE   AltName: CD_antigen=CD363;
GN   Name=S1pr1; Synonyms=Edg1, Lpb1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=97369927; PubMed=9226368; DOI=10.1006/geno.1997.4759;
RA   Liu C.H., Hla T.;
RT   "The mouse gene for the inducible G-protein-coupled receptor edg-1.";
RL   Genomics 43:15-24(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=129/SvJ;
RX   MEDLINE=99132320; PubMed=9931453; DOI=10.1016/S0378-1119(98)00589-7;
RA   Zhang G., Contos J.J.A., Weiner J.A., Fukushima N., Chun J.;
RT   "Comparative analysis of three murine G-protein coupled receptors
RT   activated by sphingosine-1-phosphate.";
RL   Gene 227:89-99(1999).
RN   [3]
RP   FUNCTION.
RX   PubMed=11230698; DOI=10.1126/science.1057559;
RA   Hobson J.P., Rosenfeldt H.M., Barak L.S., Olivera A., Poulton S.,
RA   Caron M.G., Milstien S., Spiegel S.;
RT   "Role of the sphingosine-1-phosphate receptor EDG-1 in PDGF-induced
RT   cell motility.";
RL   Science 291:1800-1803(2001).
CC   -!- FUNCTION: Receptor for the lysosphingolipid sphingosine 1-
CC       phosphate (S1P). S1P is a bioactive lysophospholipid that elicits
CC       diverse physiological effect on most types of cells and tissues.
CC       This inducible epithelial cell G-protein-coupled receptor may be
CC       involved in the processes that regulate the differentiation of
CC       endothelial cells. Seems to be coupled to the G(i) subclass of
CC       heteromeric G proteins (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues with
CC       highest levels in brain, heart and spleen. Lower levels found in
CC       kidney, liver, lung, muscle, placenta, thymus, and uterus. Very
CC       low levels in intestine, stomach and testis. According to
CC       PubMed:9931453, expressed modestly in apparent endothelial cells
CC       surrounding some blood vessels (e.g. aortic trunk).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
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DR   EMBL; U40811; AAC53294.1; -; Genomic_DNA.
DR   EMBL; AF108019; AAD16975.1; -; Genomic_DNA.
DR   IPI; IPI00308940; -.
DR   UniGene; Mm.982; -.
DR   ProteinModelPortal; O08530; -.
DR   SMR; O08530; 45-327.
DR   STRING; O08530; -.
DR   PhosphoSite; O08530; -.
DR   PRIDE; O08530; -.
DR   Ensembl; ENSMUST00000055676; ENSMUSP00000050897; ENSMUSG00000045092.
DR   MGI; MGI:1096355; S1pr1.
DR   HOGENOM; HBG714382; -.
DR   HOVERGEN; HBG103071; -.
DR   InParanoid; O08530; -.
DR   OrthoDB; EOG418BNR; -.
DR   ArrayExpress; O08530; -.
DR   Bgee; O08530; -.
DR   Genevestigator; O08530; -.
DR   GermOnline; ENSMUSG00000045092; Mus musculus.
DR   GO; GO:0009897; C:external side of plasma membrane; IMP:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0001619; F:lysosphingolipid and lysophosphatidic acid receptor activity; IEA:InterPro.
DR   GO; GO:0001525; P:angiogenesis; IDA:MGI.
DR   GO; GO:0007420; P:brain development; IMP:MGI.
DR   GO; GO:0007193; P:inhibition of adenylate cyclase activity by G-protein signaling pathway; IDA:MGI.
DR   GO; GO:0030155; P:regulation of cell adhesion; IDA:MGI.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR000987; EDG1_rcpt.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR004061; S1P_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00642; EDG1RECEPTOR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01523; S1PRECEPTOR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW   Membrane; Palmitate; Phosphoprotein; Receptor; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    382       Sphingosine 1-phosphate receptor 1.
FT                                /FTId=PRO_0000069413.
FT   TOPO_DOM      1     46       Extracellular (By similarity).
FT   TRANSMEM     47     71       Helical; Name=1; (By similarity).
FT   TOPO_DOM     72     78       Cytoplasmic (By similarity).
FT   TRANSMEM     79    107       Helical; Name=2; (By similarity).
FT   TOPO_DOM    108    121       Extracellular (By similarity).
FT   TRANSMEM    122    140       Helical; Name=3; (By similarity).
FT   TOPO_DOM    141    159       Cytoplasmic (By similarity).
FT   TRANSMEM    160    185       Helical; Name=4; (By similarity).
FT   TOPO_DOM    186    201       Extracellular (By similarity).
FT   TRANSMEM    202    222       Helical; Name=5; (By similarity).
FT   TOPO_DOM    223    256       Cytoplasmic (By similarity).
FT   TRANSMEM    257    278       Helical; Name=6; (By similarity).
FT   TOPO_DOM    279    294       Extracellular (By similarity).
FT   TRANSMEM    295    315       Helical; Name=7; (By similarity).
FT   TOPO_DOM    316    382       Cytoplasmic (By similarity).
FT   MOD_RES     353    353       Phosphoserine (Potential).
FT   LIPID       328    328       S-palmitoyl cysteine (By similarity).
FT   CARBOHYD     30     30       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    218    218       V -> A (in Ref. 1; AAC53294).
FT   CONFLICT    244    244       A -> G (in Ref. 1; AAC53294).
SQ   SEQUENCE   382 AA;  42613 MW;  2EE4B974E9FBF39C CRC64;
     MVSTSIPEVK ALRSSVSDYG NYDIIVRHYN YTGKLNIGAE KDHGIKLTSV VFILICCFII
     LENIFVLLTI WKTKKFHRPM YYFIGNLALS DLLAGVAYTA NLLLSGATTY KLTPAQWFLR
     EGSMFVALSA SVFSLLAIAI ERYITMLKMK LHNGSNSSRS FLLISACWVI SLILGGLPSM
     GWNCISSLSS CSTVLPLYHK HYILFCTTVF TLLLLSIVIL YCRIYSLVRT RSRRLTFRKN
     ISKASRSSEK SLALLKTVII VLSVFIACWA PLFILLLLDV GCKAKTCDIL YKAEYFLVLA
     VLNSGTNPII YTLTNKEMRR AFIRIVSCCK CPNGDSAGKF KRPIIPGMEF SRSKSDNSSH
     PQKDDGDNPE TIMSSGNVNS SS
//
ID   BIN1_MOUSE              Reviewed;         588 AA.
AC   O08539; Q62434;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   08-MAR-2011, entry version 113.
DE   RecName: Full=Myc box-dependent-interacting protein 1;
DE   AltName: Full=Amphiphysin II;
DE   AltName: Full=Amphiphysin-like protein;
DE   AltName: Full=Bridging integrator 1;
DE   AltName: Full=SH3 domain-containing protein 9;
GN   Name=Bin1; Synonyms=Amphl, Sh3p9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=97326078; PubMed=9182529; DOI=10.1074/jbc.272.24.15101;
RA   Leprince C., Romero F., Cussac D., Vayssiere B., Berger R.,
RA   Tavitian A., Camonis J.H.;
RT   "A new member of the amphiphysin family connecting endocytosis and
RT   signal transduction pathways.";
RL   J. Biol. Chem. 272:15101-15105(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Embryo;
RX   MEDLINE=98294438; PubMed=9630982; DOI=10.1038/nbt0696-741;
RA   Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.;
RT   "Cloning of ligand targets: systematic isolation of SH3 domain-
RT   containing proteins.";
RL   Nat. Biotechnol. 14:741-744(1996).
RN   [3]
RP   INTERACTION WITH SH3GLB1.
RX   PubMed=12456676; DOI=10.1074/jbc.M208568200;
RA   Modregger J., Schmidt A.A., Ritter B., Huttner W.B., Plomann M.;
RT   "Characterization of endophilin B1b, a brain-specific membrane-
RT   associated lysophosphatidic acid acyl transferase with properties
RT   distinct from endophilin A1.";
RL   J. Biol. Chem. 278:4160-4167(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-298 AND
RP   SER-304, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-298; SER-304
RP   AND THR-308, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-298 AND
RP   SER-324, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: May be involved in regulation of synaptic vesicle
CC       endocytosis. May act as a tumor suppressor and inhibits malignant
CC       cell transformation.
CC   -!- SUBUNIT: Heterodimer with AMPH (By similarity). Interacts (via SH3
CC       domain) with SYNJ1. Interacts (via SH3 domain) with DNM1.
CC       Interacts with CLTC. Interacts with AP2A2. Interacts with AP2B1.
CC       Interacts with MYC (via N-terminal transactivation domain); the
CC       interaction requires the integrity of the conserved MYC box
CC       regions 1 and 2. Binds SH3GLB1. Interacts with BIN2 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=BRAMP2;
CC         IsoId=O08539-1; Sequence=Displayed;
CC       Name=2; Synonyms=SH3P9;
CC         IsoId=O08539-2; Sequence=VSP_000254, VSP_000255;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is expressed mainly in the brain.
CC       Isoform 2 is widely expressed.
CC   -!- PTM: Phosphorylated by protein kinase C (By similarity).
CC   -!- SIMILARITY: Contains 1 BAR domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U86405; AAC53318.1; -; mRNA.
DR   EMBL; U60884; AAC52661.1; -; mRNA.
DR   IPI; IPI00114352; -.
DR   IPI; IPI00282748; -.
DR   RefSeq; NP_033798.1; NM_009668.2.
DR   UniGene; Mm.4383; -.
DR   ProteinModelPortal; O08539; -.
DR   SMR; O08539; 1-33, 40-271, 302-378, 456-588.
DR   MINT; MINT-263281; -.
DR   STRING; O08539; -.
DR   PhosphoSite; O08539; -.
DR   PRIDE; O08539; -.
DR   Ensembl; ENSMUST00000025239; ENSMUSP00000025239; ENSMUSG00000024381.
DR   Ensembl; ENSMUST00000115796; ENSMUSP00000111462; ENSMUSG00000024381.
DR   GeneID; 30948; -.
DR   KEGG; mmu:30948; -.
DR   UCSC; uc008ejh.1; mouse.
DR   UCSC; uc008ejj.1; mouse.
DR   CTD; 30948; -.
DR   MGI; MGI:108092; Bin1.
DR   eggNOG; roNOG14368; -.
DR   HOGENOM; HBG713912; -.
DR   HOVERGEN; HBG004224; -.
DR   InParanoid; O08539; -.
DR   OMA; HEPEPAS; -.
DR   OrthoDB; EOG4G4GQ2; -.
DR   PhylomeDB; O08539; -.
DR   NextBio; 307410; -.
DR   PMAP-CutDB; O08539; -.
DR   ArrayExpress; O08539; -.
DR   Bgee; O08539; -.
DR   CleanEx; MM_BIN1; -.
DR   Genevestigator; O08539; -.
DR   GermOnline; ENSMUSG00000024381; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0042692; P:muscle cell differentiation; IMP:MGI.
DR   GO; GO:0030100; P:regulation of endocytosis; IEA:InterPro.
DR   InterPro; IPR003005; Amphiphysin.
DR   InterPro; IPR003023; Amphiphysin_2.
DR   InterPro; IPR004148; BAR.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF03114; BAR; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR01251; AMPHIPHYSIN.
DR   PRINTS; PR01253; AMPHIPHYSIN2.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00721; BAR; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS51021; BAR; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Developmental protein;
KW   Differentiation; Endocytosis; Nucleus; Phosphoprotein; SH3 domain;
KW   Tumor suppressor.
FT   CHAIN         1    588       Myc box-dependent-interacting protein 1.
FT                                /FTId=PRO_0000192952.
FT   DOMAIN       29    276       BAR.
FT   DOMAIN      515    588       SH3.
FT   REGION        1    122       Interaction with BIN2 (By similarity).
FT   REGION      379    422       Clathrin-binding (By similarity).
FT   COILED       15     42       Potential.
FT   COILED      193    274       Potential.
FT   MOD_RES     296    296       Phosphoserine.
FT   MOD_RES     298    298       Phosphoserine.
FT   MOD_RES     304    304       Phosphoserine.
FT   MOD_RES     308    308       Phosphothreonine.
FT   MOD_RES     324    324       Phosphoserine.
FT   MOD_RES     332    332       Phosphoserine.
FT   VAR_SEQ     174    204       Missing (in isoform 2).
FT                                /FTId=VSP_000254.
FT   VAR_SEQ     335    457       Missing (in isoform 2).
FT                                /FTId=VSP_000255.
SQ   SEQUENCE   588 AA;  64470 MW;  63CA362461500F38 CRC64;
     MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR
     LQKDLRTYLA SVKAMHEASK KLSECLQEVY EPEWPGRDEA NKIAENNDLL WMDYHQKLVD
     QALLTMDTYL GQFPDIKSRI AKRGRKLVDY DSARHHYESL QTAKKKDEAK IAKPVSLLEK
     AAPQWCQGKL QAHLVAQTNL LRNQAEEELI KAQKVFEEMN VDLQEELPSL WNSRVGFYVN
     TFQSIAGLEE NFHKEMSKLN QNLNDVLVSL EKQHGSNTFT VKAQPSDNAP EKGNKSPSPP
     PDGSPAATPE IRVNHEPEPA SGASPGATIP KSPSQLRKGP PVPPPPKHTP SKEMKQEQIL
     SLFDDAFVPE ISVTTPSQFE APGPFSEQAS LLDLDFEPLP PVASPVKAPT PSGQSIPWDL
     WEPTESQAGI LPSGEPSSAE GSFAVAWPSQ TAEPGPAQPA EASEVVGGAQ EPGETAASEA
     TSSSLPAVVV ETFSATVNGA VEGSAGTGRL DLPPGFMFKV QAQHDYTATD TDELQLKAGD
     VVLVIPFQNP EEQDEGWLMG VKESDWNQHK ELEKCRGVFP ENFTERVQ
//
ID   SC22B_MOUSE             Reviewed;         215 AA.
AC   O08547; Q91VU3;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 103.
DE   RecName: Full=Vesicle-trafficking protein SEC22b;
DE   AltName: Full=ER-Golgi SNARE of 24 kDa;
DE            Short=ERS-24;
DE            Short=ERS24;
DE   AltName: Full=SEC22 vesicle-trafficking protein homolog B;
DE   AltName: Full=SEC22 vesicle-trafficking protein-like 1;
DE            Short=mSec22b;
GN   Name=Sec22b; Synonyms=Sec22l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   MEDLINE=97248495; PubMed=9094723; DOI=10.1016/S0092-8674(00)80191-9;
RA   Hay J.C., Chao D.S., Kuo C.S., Scheller R.H.;
RT   "Protein interactions regulating vesicle transport between the
RT   endoplasmic reticulum and Golgi apparatus in mammalian cells.";
RL   Cell 89:149-158(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Pituitary, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 29-38, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-130.
RX   MEDLINE=21316491; PubMed=11309394; DOI=10.1074/jbc.M101584200;
RA   Gonzalez L.C. Jr., Weis W.I., Scheller R.H.;
RT   "A novel SNARE N-terminal domain revealed by the crystal structure of
RT   Sec22b.";
RL   J. Biol. Chem. 276:24203-24211(2001).
CC   -!- FUNCTION: SNARE involved in targeting and fusion of ER-derived
CC       transport vesicles with the Golgi complex as well as Golgi-derived
CC       retrograde transport vesicles with the ER.
CC   -!- SUBUNIT: Component of two distinct SNARE complexes consisting of
CC       STX5, GOSR2/BOS1, BET1 and SEC22B or STX18, USE1L, BNIP1/SEC20L
CC       and SEC22B. YKT6 can probably replace SEC22B in either complex (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC       compartment membrane; Single-pass type IV membrane protein (By
CC       similarity). Golgi apparatus membrane; Single-pass type IV
CC       membrane protein (By similarity). Endoplasmic reticulum membrane;
CC       Single-pass type IV membrane protein (By similarity). Melanosome
CC       (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the synaptobrevin family.
CC   -!- SIMILARITY: Contains 1 longin domain.
CC   -!- SIMILARITY: Contains 1 v-SNARE coiled-coil homology domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; U91538; AAC53130.1; -; mRNA.
DR   EMBL; AK017237; BAB30646.1; -; mRNA.
DR   EMBL; AK034973; BAC28899.1; -; mRNA.
DR   EMBL; AK037918; BAC29901.1; -; mRNA.
DR   EMBL; AK088514; BAC40397.1; -; mRNA.
DR   EMBL; AK089928; BAC40999.1; -; mRNA.
DR   EMBL; BC009024; AAH09024.1; -; mRNA.
DR   IPI; IPI00114368; -.
DR   RefSeq; NP_035472.1; NM_011342.4.
DR   UniGene; Mm.2551; -.
DR   PDB; 1IFQ; X-ray; 2.40 A; A/B=2-127.
DR   PDBsum; 1IFQ; -.
DR   ProteinModelPortal; O08547; -.
DR   SMR; O08547; 1-214.
DR   STRING; O08547; -.
DR   PhosphoSite; O08547; -.
DR   PRIDE; O08547; -.
DR   Ensembl; ENSMUST00000029476; ENSMUSP00000029476; ENSMUSG00000027879.
DR   GeneID; 20333; -.
DR   KEGG; mmu:20333; -.
DR   UCSC; uc008qpk.1; mouse.
DR   CTD; 20333; -.
DR   MGI; MGI:1338759; Sec22b.
DR   eggNOG; maNOG18150; -.
DR   GeneTree; ENSGT00510000046833; -.
DR   HOGENOM; HBG327843; -.
DR   HOVERGEN; HBG052748; -.
DR   InParanoid; O08547; -.
DR   OMA; QRIMVQN; -.
DR   OrthoDB; EOG4XPQGX; -.
DR   PhylomeDB; O08547; -.
DR   NextBio; 298135; -.
DR   ArrayExpress; O08547; -.
DR   Bgee; O08547; -.
DR   Genevestigator; O08547; -.
DR   GermOnline; ENSMUSG00000027879; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR   GO; GO:0033116; C:ER-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR010908; Longin.
DR   InterPro; IPR011012; Longin-like.
DR   InterPro; IPR001388; Synaptobrevin.
DR   Gene3D; G3DSA:3.30.450.50; Longin; 1.
DR   Pfam; PF00957; Synaptobrevin; 1.
DR   PRINTS; PR00219; SYNAPTOBREVN.
DR   SUPFAM; SSF64356; Longin_like; 1.
DR   PROSITE; PS50859; LONGIN; 1.
DR   PROSITE; PS50892; V_SNARE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Coiled coil; Direct protein sequencing;
KW   Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
KW   Phosphoprotein; Protein transport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    215       Vesicle-trafficking protein SEC22b.
FT                                /FTId=PRO_0000206771.
FT   TOPO_DOM      2    194       Cytoplasmic (Potential).
FT   TRANSMEM    195    215       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   DOMAIN        6    119       Longin.
FT   DOMAIN      134    194       v-SNARE coiled-coil homology.
FT   MOD_RES      35     35       Phosphoserine (By similarity).
FT   MOD_RES      38     38       N6-acetyllysine (By similarity).
FT   MOD_RES      48     48       Phosphoserine (By similarity).
FT   MOD_RES     137    137       Phosphoserine.
FT   MOD_RES     168    168       Phosphoserine.
FT   CONFLICT    189    189       M -> I (in Ref. 3; AAH09024).
FT   STRAND        4      9
FT   TURN         10     12
FT   STRAND       15     19
FT   HELIX        27     41
FT   STRAND       50     56
FT   STRAND       59     66
FT   STRAND       69     76
FT   HELIX        81     99
FT   TURN        100    105
FT   TURN        109    112
FT   HELIX       113    115
FT   HELIX       116    126
SQ   SEQUENCE   215 AA;  24741 MW;  29B4C55961C5A044 CRC64;
     MVLLTMIARV ADGLPLAASM QEDEQSGRDL QQYQSQAKQL FRKLNEQSPT RCTLEAGAMT
     FHYIIEQGVC YLVLCEAAFP KKLAFAYLED LHSEFDEQHG KKVPTVSRPY SFIEFDTFIQ
     KTKKLYIDSR ARRNLGSINT ELQDVQRIMV ANIEEVLQRG EALSALDSKA NNLSSLSKKY
     RQDAKYLNMR STYAKLAAVA VFFIMLIVYV RFWWL
//
ID   DPYL2_MOUSE             Reviewed;         572 AA.
AC   O08553; Q6P5D0;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Dihydropyrimidinase-related protein 2;
DE            Short=DRP-2;
DE   AltName: Full=Unc-33-like phosphoprotein 2;
DE            Short=ULIP-2;
GN   Name=Dpysl2; Synonyms=Crmp2, Ulip2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=98314496; PubMed=9652388;
RX   DOI=10.1046/j.1432-1327.1998.2540014.x;
RA   Byk T., Ozon S., Sobel A.;
RT   "The Ulip family phosphoproteins -- common and specific properties.";
RL   Eur. J. Biochem. 254:14-24(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 44-56; 174-211; 239-254; 259-268; 391-397; 441-467
RP   AND 533-552, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   SUBUNIT.
RX   PubMed=9375656;
RA   Wang L.H., Strittmatter S.M.;
RT   "Brain CRMP forms heterotetramers similar to liver
RT   dihydropyrimidinase.";
RL   J. Neurochem. 69:2261-2269(1997).
RN   [5]
RP   SUBUNIT.
RX   MEDLINE=20545548; PubMed=10956643; DOI=10.1074/jbc.M003277200;
RA   Fukada M., Watakabe I., Yuasa-Kawada J., Kawachi H., Kuroiwa A.,
RA   Matsuda Y., Noda M.;
RT   "Molecular characterization of CRMP5, a novel member of the collapsin
RT   response mediator protein family.";
RL   J. Biol. Chem. 275:37957-37965(2000).
RN   [6]
RP   INTERACTION WITH HTR4.
RX   PubMed=15466885; DOI=10.1242/jcs.01379;
RA   Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W.,
RA   Marin P., Dumuis A., Bockaert J.;
RT   "New sorting nexin (SNX27) and NHERF specifically interact with the 5-
RT   HT4a receptor splice variant: roles in receptor targeting.";
RL   J. Cell Sci. 117:5367-5379(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15648052; DOI=10.1002/pmic.200401066;
RA   Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA   Hart G.W., Burlingame A.L.;
RT   "Quantitative analysis of both protein expression and serine /
RT   threonine post-translational modifications through stable isotope
RT   labeling with dithiothreitol.";
RL   Proteomics 5:388-398(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509 AND THR-514, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-32; TYR-431; TYR-499 AND
RP   THR-509, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-462, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RA   Lubec G., Kang S.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-542, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-514; SER-517; SER-518
RP   AND SER-522, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Necessary for signaling by class 3 semaphorins and
CC       subsequent remodeling of the cytoskeleton. Plays a role in axon
CC       guidance, neuronal growth cone collapse and cell migration (By
CC       similarity).
CC   -!- SUBUNIT: Homotetramer, and heterotetramer with CRMP1, DPYSL3,
CC       DPYSL4 or DPYSL5. Interacts through its C-terminus with the C-
CC       terminus of CYFIP1/SRA1 (By similarity). Interacts with HTR4.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the DHOase family.
CC       Hydantoinase/dihydropyrimidinase subfamily.
CC   -!- CAUTION: Lacks most of the conserved residues that are essential
CC       for binding the metal cofactor and hence for dihydropyrimidinase
CC       activity. Its enzyme activity is therefore unsure.
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DR   EMBL; Y10339; CAA71370.1; -; mRNA.
DR   EMBL; BC062955; AAH62955.1; -; mRNA.
DR   IPI; IPI00114375; -.
DR   RefSeq; NP_034085.2; NM_009955.3.
DR   UniGene; Mm.352648; -.
DR   UniGene; Mm.475100; -.
DR   ProteinModelPortal; O08553; -.
DR   SMR; O08553; 14-490.
DR   STRING; O08553; -.
DR   MEROPS; M38.975; -.
DR   PhosphoSite; O08553; -.
DR   REPRODUCTION-2DPAGE; IPI00114375; -.
DR   REPRODUCTION-2DPAGE; O08553; -.
DR   UCD-2DPAGE; O08553; -.
DR   PRIDE; O08553; -.
DR   Ensembl; ENSMUST00000022629; ENSMUSP00000022629; ENSMUSG00000022048.
DR   GeneID; 12934; -.
DR   KEGG; mmu:12934; -.
DR   UCSC; uc007uko.1; mouse.
DR   CTD; 12934; -.
DR   MGI; MGI:1349763; Dpysl2.
DR   eggNOG; maNOG14228; -.
DR   GeneTree; ENSGT00550000074371; -.
DR   HOGENOM; HBG724623; -.
DR   HOVERGEN; HBG000806; -.
DR   InParanoid; O08553; -.
DR   OMA; TEWHKGV; -.
DR   OrthoDB; EOG48PMJT; -.
DR   PhylomeDB; O08553; -.
DR   NextBio; 282608; -.
DR   ArrayExpress; O08553; -.
DR   Bgee; O08553; -.
DR   CleanEx; MM_DPYSL2; -.
DR   Genevestigator; O08553; -.
DR   GermOnline; ENSMUSG00000022048; Mus musculus.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   InterPro; IPR006680; Amidohydro_1.
DR   InterPro; IPR011778; D-hydantoinase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Metalo_hydrolase; 2.
DR   TIGRFAMs; TIGR02033; D-hydantoinase; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Developmental protein; Differentiation;
KW   Direct protein sequencing; Neurogenesis; Phosphoprotein.
FT   CHAIN         1    572       Dihydropyrimidinase-related protein 2.
FT                                /FTId=PRO_0000165914.
FT   MOD_RES      32     32       Phosphotyrosine.
FT   MOD_RES     431    431       Phosphotyrosine.
FT   MOD_RES     462    462       Phosphothreonine.
FT   MOD_RES     465    465       Phosphoserine.
FT   MOD_RES     499    499       Phosphotyrosine.
FT   MOD_RES     509    509       Phosphothreonine.
FT   MOD_RES     512    512       Phosphothreonine (By similarity).
FT   MOD_RES     514    514       Phosphothreonine.
FT   MOD_RES     517    517       Phosphoserine.
FT   MOD_RES     518    518       Phosphoserine.
FT   MOD_RES     521    521       Phosphothreonine (By similarity).
FT   MOD_RES     522    522       Phosphoserine.
FT   MOD_RES     542    542       Phosphoserine.
FT   CONFLICT     11     11       R -> P (in Ref. 1; CAA71370).
FT   CONFLICT    208    208       E -> A (in Ref. 1; CAA71370).
FT   CONFLICT    257    257       S -> P (in Ref. 1; CAA71370).
SQ   SEQUENCE   572 AA;  62278 MW;  C031F3BC038AA737 CRC64;
     MSYQGKKNIP RITSDRLLIK GGKIVNDDQS FYADIYMEDG LIKQIGENLI VPGGVKTIEA
     HSRMVIPGGI DVHTRFQMPD QGMTSADDFF QGTKAALAGG TTMIIDHVVP EPGTSLLAAF
     DQWREWADSK SCCDYSLHVD ITEWHKGIQE EMEALVKDHG VNSFLVYMAF KDRFQLTDSQ
     IYEVLSVIRD IGAIAQVHAE NGDIIAEEQQ RILDLGITGP EGHVLSRPEE VEAEAVNRSI
     TIANQTNCPL YVTKVMSKSA AEVIAQARKK GTVVYGEPIT ASLGTDGSHY WSKNWAKAAA
     FVTSPPLSPD PTTPDFLNSL LSCGDLQVTG SAHCTFNTAQ KAVGKDNFTL IPEGTNGTEE
     RMSVIWDKAV VTGKMDENQF VAVTSTNAAK VFNLYPRKGR ISVGSDADLV IWDPDSVKTI
     SAKTHNSALE YNIFEGMECR GSPLVVISQG KIVLEDGTLH VTEGSGRYIP RKPFPDFVYK
     RIKARSRLAE LRGVPRGLYD GPVCEVSVTP KTVTPASSAK TSPAKQQAPP VRNLHQSGFS
     LSGAQIDDNI PRRTTQRIVA PPGGRANITS LG
//
ID   RUN3A_MOUSE             Reviewed;         446 AA.
AC   O08576; A2A693; A2A694; Q80Y95;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=RUN domain-containing protein 3A;
DE   AltName: Full=Rap2-interacting protein 8;
DE            Short=RPIP-8;
GN   Name=Rundc3a; Synonyms=Rap2ip, Rpip8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION OF ISOFORM 2,
RP   FUNCTION, INTERACTION WITH RAP2A, AND TISSUE SPECIFICITY.
RX   PubMed=9523700; DOI=10.1046/j.1432-1327.1998.2520290.x;
RA   Janoueix-Lerosey I., Pasheva E., de Tand M.-F., Tavitian A.,
RA   de Gunzburg J.;
RT   "Identification of a specific effector of the small GTP-binding
RT   protein Rap2.";
RL   Eur. J. Biochem. 252:290-298(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
RP   SPLICING (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May act as an effector of RAP2A in neuronal cells.
CC   -!- SUBUNIT: Interacts with the GTP-bound form of RAP2A.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=O08576-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O08576-2; Sequence=VSP_032157, VSP_032159, VSP_032160;
CC       Name=3;
CC         IsoId=O08576-3; Sequence=VSP_032159, VSP_032160;
CC       Name=4;
CC         IsoId=O08576-4; Sequence=VSP_032158, VSP_032159, VSP_032160;
CC   -!- TISSUE SPECIFICITY: Brain.
CC   -!- SIMILARITY: Belongs to the RUNDC3 family.
CC   -!- SIMILARITY: Contains 1 RUN domain.
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DR   EMBL; U73941; AAB51123.1; -; mRNA.
DR   EMBL; AL596258; CAM18002.1; -; Genomic_DNA.
DR   EMBL; AL596258; CAM18003.1; -; Genomic_DNA.
DR   EMBL; AL596258; CAM18004.1; -; Genomic_DNA.
DR   EMBL; AL596258; CAM18005.1; -; Genomic_DNA.
DR   EMBL; BC046319; AAH46319.1; -; mRNA.
DR   IPI; IPI00114399; -.
DR   IPI; IPI00648220; -.
DR   IPI; IPI00649764; -.
DR   IPI; IPI00650050; -.
DR   RefSeq; NP_058039.1; NM_016759.3.
DR   UniGene; Mm.2560; -.
DR   HSSP; Q9D394; 1WUS.
DR   ProteinModelPortal; O08576; -.
DR   SMR; O08576; 24-193.
DR   STRING; O08576; -.
DR   PhosphoSite; O08576; -.
DR   PRIDE; O08576; -.
DR   Ensembl; ENSMUST00000006750; ENSMUSP00000006750; ENSMUSG00000006575.
DR   Ensembl; ENSMUST00000107105; ENSMUSP00000102722; ENSMUSG00000006575.
DR   GeneID; 51799; -.
DR   KEGG; mmu:51799; -.
DR   UCSC; uc007lrr.1; mouse.
DR   CTD; 51799; -.
DR   MGI; MGI:1858752; Rundc3a.
DR   eggNOG; roNOG15242; -.
DR   GeneTree; ENSGT00550000074558; -.
DR   HOGENOM; HBG505847; -.
DR   HOVERGEN; HBG052747; -.
DR   InParanoid; O08576; -.
DR   OMA; FRRRSFH; -.
DR   OrthoDB; EOG40GCR4; -.
DR   PhylomeDB; O08576; -.
DR   NextBio; 308048; -.
DR   ArrayExpress; O08576; -.
DR   Bgee; O08576; -.
DR   CleanEx; MM_RUNDC3A; -.
DR   Genevestigator; O08576; -.
DR   InterPro; IPR004012; Run.
DR   Pfam; PF02759; RUN; 1.
DR   SMART; SM00593; RUN; 1.
DR   PROSITE; PS50826; RUN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil.
FT   CHAIN         1    446       RUN domain-containing protein 3A.
FT                                /FTId=PRO_0000324156.
FT   DOMAIN       52    189       RUN.
FT   REGION        1    298       Interaction with RAP2A.
FT   COILED      267    322       Potential.
FT   VAR_SEQ      75     79       Missing (in isoform 2).
FT                                /FTId=VSP_032157.
FT   VAR_SEQ     318    318       L -> LPDPPPPPR (in isoform 4).
FT                                /FTId=VSP_032158.
FT   VAR_SEQ     401    405       KDPTP -> SSEPN (in isoform 2, isoform 3
FT                                and isoform 4).
FT                                /FTId=VSP_032159.
FT   VAR_SEQ     406    446       Missing (in isoform 2, isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_032160.
SQ   SEQUENCE   446 AA;  50018 MW;  5D9D73127A216483 CRC64;
     MEASFVQTTM ALGLPSKKAS SRNVIVERRN LITVCRFSVK TLLEKYTAEP IDDSSEEFVN
     FAAILEQILS HRFKACAPAG PASWFSSDGQ RGFWDYIRLA CSKVPNNCVS SIENMENIST
     ARAKGRAWIR VALMEKRMSE YITTALRDNR TTRRFYDSGA IMLREEATVL TGMLIGLSAI
     DFSFCLKGEV LDGKTPVVID YTPYLKFTQS YDYLTDEEER HSAESSTSED NSPEHPYLPL
     VTDEDSWYNK WHKMEQKFRI VYAQKGYLEE LVRLRESQLK DLEAENRRLQ LQLEEAAAQN
     QREKRELEGV ILELQEQLTG LIPGDHAPLA QGSKELTTSL VNQWPSLSTL HRPEGASNSK
     LYRRHSFMST EPLSAEASLS SDSQRLGEAK RDEEPWGPIG KDPTPSMLGL CGSLASIPSC
     KSLASFKSNE CLVSDSPEGS PALSPS
//
ID   EMD_MOUSE               Reviewed;         259 AA.
AC   O08579;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Emerin;
GN   Name=Emd; Synonyms=Sta;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129;
RX   MEDLINE=97262100; PubMed=9107678; DOI=10.1007/s003359900435;
RA   Small K., Wagener M., Warren S.T.;
RT   "Isolation and characterization of the complete mouse emerin gene.";
RL   Mamm. Genome 8:337-341(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR;
RA   Hawkes S.L.J., Neville L.A., Kennedy M.A.K., Love D.R.;
RT   "cDNA sequence and analysis of the murine Emery-Dreifuss muscular
RT   dystrophy gene.";
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INTERACTION WITH TMEM43, AND SUBCELLULAR LOCATION.
RX   PubMed=18230648; DOI=10.1242/jcs.019281;
RA   Bengtsson L., Otto H.;
RT   "LUMA interacts with emerin and influences its distribution at the
RT   inner nuclear membrane.";
RL   J. Cell Sci. 121:536-548(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-161, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [5]
RP   INTERACTION WITH SUN1 AND SUN2.
RX   PubMed=19933576; DOI=10.1074/jbc.M109.071910;
RA   Haque F., Mazzeo D., Patel J.T., Smallwood D.T., Ellis J.A.,
RA   Shanahan C.M., Shackleton S.;
RT   "Mammalian SUN protein interaction networks at the inner nuclear
RT   membrane and their role in laminopathy disease processes.";
RL   J. Biol. Chem. 285:3487-3498(2010).
CC   -!- FUNCTION: Stabilizes and promotes the formation of a nuclear actin
CC       cortical network. Stimulates actin polymerization in vitro by
CC       binding and stabilizing the pointed end of growing filaments.
CC       Inhibits beta-catenin activity by preventing its accumulation in
CC       the nucleus. Acts by influencing the nuclear accumulation of beta-
CC       catenin through a CRM1-dependent export pathway. Links centrosomes
CC       to the nuclear envelope via a microtubule association. Required
CC       for proper localization of non-farnesylated prelamin-A/C (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with lamins A and C, BANF1, GMCL, BCLAF1 and
CC       YTHDC1/YT521. Interacts with TMEM43; the interaction retains
CC       emerin in the inner nuclear membrane. Interacts with ACTB, SPTAN1,
CC       F-actin, CTNNB1 and beta-tubulin (By similarity). Interacts with
CC       SUN1 and SUN2.
CC   -!- SUBCELLULAR LOCATION: Nucleus inner membrane; Single-pass membrane
CC       protein; Nucleoplasmic side. Nucleus outer membrane.
CC       Note=Colocalized with BANF1 at the central region of the
CC       assembling nuclear rim, near spindle-attachment sites. The
CC       accumulation of different intermediates of prelamin-A/C (non-
CC       farnesylated or carboxymethylated farnesylated prelamin-A/C) in
CC       fibroblasts modify its localization in the nucleus (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- SIMILARITY: Contains 1 LEM domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; U79753; AAB51239.1; -; Genomic_DNA.
DR   EMBL; U73902; AAD00238.1; -; mRNA.
DR   IPI; IPI00114401; -.
DR   RefSeq; NP_031953.1; NM_007927.2.
DR   UniGene; Mm.18892; -.
DR   ProteinModelPortal; O08579; -.
DR   SMR; O08579; 2-47.
DR   STRING; O08579; -.
DR   PhosphoSite; O08579; -.
DR   PRIDE; O08579; -.
DR   Ensembl; ENSMUST00000002029; ENSMUSP00000002029; ENSMUSG00000001964.
DR   GeneID; 13726; -.
DR   KEGG; mmu:13726; -.
DR   UCSC; uc009toa.1; mouse.
DR   CTD; 13726; -.
DR   MGI; MGI:108117; Emd.
DR   eggNOG; roNOG10516; -.
DR   HOGENOM; HBG127512; -.
DR   HOVERGEN; HBG001099; -.
DR   InParanoid; O08579; -.
DR   OMA; GPVVGST; -.
DR   OrthoDB; EOG4Z62PK; -.
DR   PhylomeDB; O08579; -.
DR   NextBio; 284512; -.
DR   PMAP-CutDB; O08579; -.
DR   ArrayExpress; O08579; -.
DR   Bgee; O08579; -.
DR   CleanEx; MM_EMD; -.
DR   Genevestigator; O08579; -.
DR   GermOnline; ENSMUSG00000001964; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005637; C:nuclear inner membrane; TAS:MGI.
DR   GO; GO:0005652; C:nuclear lamina; TAS:MGI.
DR   GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR003887; LEM.
DR   InterPro; IPR011015; LEM-like_dom.
DR   Gene3D; G3DSA:1.10.720.40; LEM; 1.
DR   Pfam; PF03020; LEM; 1.
DR   SMART; SM00540; LEM; 1.
DR   SUPFAM; SSF63451; LEM_like; 1.
DR   PROSITE; PS50954; LEM; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Membrane; Microtubule; Nucleus;
KW   Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    259       Emerin.
FT                                /FTId=PRO_0000206141.
FT   TRANSMEM    224    244       Helical; (Potential).
FT   DOMAIN        1     45       LEM.
FT   REGION       46    223       Interaction with F-actin (By similarity).
FT   REGION      168    187       Interaction with CTNNB1 (By similarity).
FT   COMPBIAS     53     59       Poly-Ser.
FT   COMPBIAS    186    200       Poly-Ser.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES       8      8       Phosphoserine (By similarity).
FT   MOD_RES      29     29       Phosphoserine (By similarity).
FT   MOD_RES      54     54       Phosphoserine (By similarity).
FT   MOD_RES      60     60       Phosphotyrosine (By similarity).
FT   MOD_RES      67     67       Phosphoserine (By similarity).
FT   MOD_RES      75     75       Phosphotyrosine (By similarity).
FT   MOD_RES      86     86       Phosphotyrosine (By similarity).
FT   MOD_RES      88     88       Phosphoserine (By similarity).
FT   MOD_RES      96     96       Phosphotyrosine (By similarity).
FT   MOD_RES     100    100       Phosphotyrosine (By similarity).
FT   MOD_RES     106    106       Phosphotyrosine (By similarity).
FT   MOD_RES     161    161       Phosphotyrosine.
FT   MOD_RES     163    163       Phosphoserine (By similarity).
FT   MOD_RES     167    167       Phosphotyrosine (By similarity).
FT   MOD_RES     171    171       Phosphoserine (By similarity).
SQ   SEQUENCE   259 AA;  29436 MW;  645B021541063502 CRC64;
     MDDYAVLSDT ELAAVLRQYN IPHGPIVGST RKLYEKKIFE YETQRRRLLP PNSSSSSFSY
     QFSDLDSAAV DSDMYDLPKK EDALLYQSKD YNDDYYEESY LTTKTYGEPE SVGMSKSFRQ
     PGTSLVDADT FHHQVRDDIF SSLEEEGKDR ERLIYGQDSA YQSIAHYRPI SNVSRSSLGL
     SYYPTSSTSS VSSSSSSPSS WLTRRAIRPE KQAPAAALGQ DRQVPLWGQL LLFLVFAAFL
     LFVYYSIQAE EGNPFWMDP
//
ID   ERR1_MOUSE              Reviewed;         422 AA.
AC   O08580; Q3U110;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 3.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Steroid hormone receptor ERR1;
DE   AltName: Full=Estrogen receptor-like 1;
DE   AltName: Full=Estrogen-related receptor alpha;
DE            Short=ERR-alpha;
DE   AltName: Full=Nuclear receptor subfamily 3 group B member 1;
GN   Name=Esrra; Synonyms=Err1, Estrra, Nr3b1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=97415618; PubMed=9271417;
RA   Sladek R., Bader J.-A., Giguere V.;
RT   "The orphan nuclear receptor estrogen-related receptor alpha is a
RT   transcriptional regulator of the human medium-chain acyl coenzyme A
RT   dehydrogenase gene.";
RL   Mol. Cell. Biol. 17:5400-5409(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain, and Kidney;
RX   MEDLINE=98121983; PubMed=9460651; DOI=10.1677/jme.0.0190299;
RA   Shigeta H., Zuo W., Yang N., DiAugustine R., Teng C.T.;
RT   "The mouse estrogen receptor-related orphan receptor alpha 1:
RT   molecular cloning and estrogen responsiveness.";
RL   J. Mol. Endocrinol. 19:299-309(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=14585956; DOI=10.1128/MCB.23.22.7947-7956.2003;
RA   Luo J., Sladek R., Carrier J., Bader J.A., Richard D., Giguere V.;
RT   "Reduced fat mass in mice lacking orphan nuclear receptor estrogen-
RT   related receptor alpha.";
RL   Mol. Cell. Biol. 23:7947-7956(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   SUMOYLATION, AND PHOSPHORYLATION AT SER-19.
RX   PubMed=18063693; DOI=10.1210/me.2007-0357;
RA   Tremblay A.M., Wilson B.J., Yang X.-J., Giguere V.;
RT   "Phosphorylation-dependent sumoylation regulates estrogen-related
RT   receptor-alpha and -gamma transcriptional activity through a synergy
RT   control motif.";
RL   Mol. Endocrinol. 22:570-584(2008).
CC   -!- FUNCTION: Binds to an ERR-alpha response element (ERRE) containing
CC       a single consensus half-site, 5'-TNAAGGTCA-3'. Can bind to the
CC       medium-chain acyl coenzyme A dehydrogenase (MCAD) response element
CC       NRRE-1 and may act as an important regulator of MCAD promoter.
CC       Binds to the C1 region of the lactoferrin gene promoter. Requires
CC       dimerization and the coactivator, PGC-1A, for full activity. The
CC       ERRalpha/PGC1alpha complex is a regulator of energy metabolism (By
CC       similarity).
CC   -!- SUBUNIT: Binds DNA as a monomer or a homodimer. Interacts (via the
CC       AF2 domain) with coactivator PPARGC1A (via the L3 motif); the
CC       interaction greatly enhances transriptional activity of genes
CC       involved in energy metabolism. Interacts with PIAS4; the
CC       interaction enhances sumoylation (By similarity).
CC   -!- INTERACTION:
CC       Q6STE5-1:SMARCD3 (xeno); NbExp=1; IntAct=EBI-1008937, EBI-488506;
CC       Q6STE5-2:SMARCD3 (xeno); NbExp=1; IntAct=EBI-1008937, EBI-488511;
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- TISSUE SPECIFICITY: Most highly expressed in kidney, heart, and
CC       brown adipocytes. Also found in utERus, cervix and vagina.
CC   -!- DEVELOPMENTAL STAGE: Expressed in an organ specific mannER through
CC       mid-to late embryonic development with persistent high-level
CC       expression in brown adipose tissue and intestinal mucosa.
CC   -!- INDUCTION: Activated by diethylstilbestrol (DES) and estradiol in
CC       the uterus.
CC   -!- PTM: Phosphorylation on Ser-19 enhances sumoylation on Lys-14
CC       increasing repression of transcriptional activity (By similarity).
CC   -!- PTM: Sumoylated by SUMO2. Main site is Lys-14 which is enhanced by
CC       phosphorylation on Ser-19, cofactor activation, and by interaction
CC       with PIAS4. Sumoylation enhances repression of transcriptional
CC       activiy, but has no effect on subcellular location nor on DNA
CC       binding (By similarity).
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype; mice are viable,
CC       fertile and display no gross anatomical alterations, with the
CC       exception of reduced body weight and peripheral fat deposits. Mice
CC       are resistant to a high-fat diet-induced obesity.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 nuclear receptor DNA-binding domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; U85259; AAB51250.1; -; mRNA.
DR   EMBL; AK156371; BAE33690.1; -; mRNA.
DR   IPI; IPI00762735; -.
DR   RefSeq; NP_031979.2; NM_007953.2.
DR   UniGene; Mm.386776; -.
DR   ProteinModelPortal; O08580; -.
DR   SMR; O08580; 73-421.
DR   IntAct; O08580; 2.
DR   STRING; O08580; -.
DR   PhosphoSite; O08580; -.
DR   PRIDE; O08580; -.
DR   Ensembl; ENSMUST00000025906; ENSMUSP00000025906; ENSMUSG00000024955.
DR   Ensembl; ENSMUST00000113432; ENSMUSP00000109059; ENSMUSG00000024955.
DR   GeneID; 26379; -.
DR   KEGG; mmu:26379; -.
DR   CTD; 26379; -.
DR   MGI; MGI:1346831; Esrra.
DR   eggNOG; roNOG14482; -.
DR   GeneTree; ENSGT00600000084216; -.
DR   HOGENOM; HBG717845; -.
DR   HOVERGEN; HBG108344; -.
DR   InParanoid; O08580; -.
DR   OrthoDB; EOG48KRBN; -.
DR   ArrayExpress; O08580; -.
DR   Bgee; O08580; -.
DR   CleanEx; MM_ESRRA; -.
DR   Genevestigator; O08580; -.
DR   GermOnline; ENSMUSG00000024955; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0010552; P:positive regulation of gene-specific transcription from RNA polymerase II promoter; IMP:BHF-UCL.
DR   InterPro; IPR008946; Nucl_hormone_rcpt_ligand-bd.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd_core.
DR   InterPro; IPR001723; Str_hrmn_rcpt.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   Gene3D; G3DSA:1.10.565.10; Nucl_hrmn_rcpt_lig_bd; 1.
DR   Gene3D; G3DSA:3.30.50.10; Znf_NHR/GATA; 1.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   PRINTS; PR00398; STRDHORMONER.
DR   PRINTS; PR00047; STROIDFINGER.
DR   SMART; SM00430; HOLI; 1.
DR   SMART; SM00399; ZnF_C4; 1.
DR   SUPFAM; SSF48508; Str_ncl_receptor; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW   Receptor; Transcription; Transcription regulation; Ubl conjugation;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    422       Steroid hormone receptor ERR1.
FT                                /FTId=PRO_0000053661.
FT   DNA_BIND     76    151       Nuclear receptor.
FT   ZN_FING      79     99       NR C4-type.
FT   ZN_FING     115    134       NR C4-type.
FT   REGION        1     76       Repressor domain.
FT   REGION      205    401       Ligand binding domain (By similarity).
FT   REGION      402    422       AF-2 domain (By similarity).
FT   SITE        124    124       Required for DNA-dependent dimerization
FT                                (By similarity).
FT   MOD_RES      19     19       Phosphoserine.
FT   MOD_RES      22     22       Phosphoserine (By similarity).
FT   MOD_RES      26     26       Phosphoserine (By similarity).
FT   MOD_RES      27     27       Phosphoserine (By similarity).
FT   CROSSLNK     14     14       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    402    402       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
SQ   SEQUENCE   422 AA;  45438 MW;  2372C60F113B511D CRC64;
     MSSQVVGIEP LYIKAEPASP DSPKGSSETE TEPPVTLASG PAPARCLPGH KEEEDGEGAG
     SGEQGSGKLV LSSLPKRLCL VCGDVASGYH YGVASCEACK AFFKRTIQGS IEYSCPASNE
     CEITKRRRKA CQACRFTKCL RVGMLKEGVR LDRVRGGRQK YKRRPEVDPL PFPGPFPAGP
     LAVAGGPRKT APVNALVSHL LVVEPEKLYA MPDPASPDGH LPAVATLCDL FDREIVVTIS
     WAKSIPGFSS LSLSDQMSVL QSVWMEVLVL GVAQRSLPLQ DELAFAEDLV LDEEGARAAG
     LGDLGAALLQ LVRRLQALRL EREEYVLLKA LALANSDSVH IEDAEAVEQL REALHEALLE
     YEAGRAGPGG GAERRRAGRL PCTLPLLRQT AGKVLAHFYG VKLEGKVPMH KLFLEMLEAM
     MD
//
ID   KCNK1_MOUSE             Reviewed;         336 AA.
AC   O08581;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Potassium channel subfamily K member 1;
DE   AltName: Full=Inward rectifying potassium channel protein TWIK-1;
GN   Name=Kcnk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=97165959; PubMed=9013852; DOI=10.1016/S0014-5793(96)01491-3;
RA   Lesage F., Lauritzen I., Duprat F., Reyes R., Fink M., Heurteaux C.,
RA   Lazdunski M.;
RT   "The structure, function and distribution of the mouse TWIK-1 K+
RT   channel.";
RL   FEBS Lett. 402:28-32(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/SvJ; TISSUE=Liver;
RX   MEDLINE=98218573; PubMed=9559671; DOI=10.1016/S0014-5793(98)00260-9;
RA   Arrighi I., Lesage F., Scimeca J.-C., Carle G.F., Barhanin J.;
RT   "Structure, chromosome localization, and tissue distribution of the
RT   mouse twik K+ channel gene.";
RL   FEBS Lett. 425:310-316(1998).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Weak inwardly rectifying potassium channel.
CC   -!- SUBUNIT: Homodimer (Potential).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- TISSUE SPECIFICITY: Widely expressed. Highest expression in brain,
CC       kidney, thyroid, salivary gland, adrenal gland, prostate,
CC       epididymis, uterus, placenta, colon and jejunum. Moderate
CC       expression in eyes, pituitary, pancreas, smooth muscle, testis and
CC       ovary. Very low levels in lung, aorta, liver, heart, skeletal
CC       muscle, thymus and spleen. In the brain, highest expression in
CC       cerebellar granule cells, brainstem, hippocampus and cerebral
CC       cortex.
CC   -!- DEVELOPMENTAL STAGE: Expression detected as early as 7 days post
CC       conception. Expression increases from 2-8 days after birth and
CC       stabilizes after day 8.
CC   -!- MISCELLANEOUS: Inhibited by quinine, barium, and internal
CC       acidification. Activated by protein kinase C.
CC   -!- SIMILARITY: Belongs to the two pore domain potassium channel
CC       (TC 1.A.1.8) family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF033017; AAC16973.1; -; mRNA.
DR   IPI; IPI00114405; -.
DR   RefSeq; NP_032456.2; NM_008430.2.
DR   UniGene; Mm.10800; -.
DR   ProteinModelPortal; O08581; -.
DR   SMR; O08581; 67-160, 191-267.
DR   STRING; O08581; -.
DR   TCDB; 1.A.1.8.1; voltage-gated ion channel (VIC) superfamily.
DR   PhosphoSite; O08581; -.
DR   PRIDE; O08581; -.
DR   Ensembl; ENSMUST00000046765; ENSMUSP00000046103; ENSMUSG00000033998.
DR   GeneID; 16525; -.
DR   KEGG; mmu:16525; -.
DR   UCSC; uc009nyr.1; mouse.
DR   CTD; 16525; -.
DR   MGI; MGI:109322; Kcnk1.
DR   eggNOG; roNOG07191; -.
DR   HOGENOM; HBG446730; -.
DR   HOVERGEN; HBG052237; -.
DR   InParanoid; O08581; -.
DR   OrthoDB; EOG451DRF; -.
DR   NextBio; 289919; -.
DR   ArrayExpress; O08581; -.
DR   Bgee; O08581; -.
DR   CleanEx; MM_KCNK1; -.
DR   Genevestigator; O08581; -.
DR   GermOnline; ENSMUSG00000033998; Mus musculus.
DR   GO; GO:0005768; C:endosome; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005267; F:potassium channel activity; IDA:MGI.
DR   GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR   InterPro; IPR013099; Ion_trans_2.
DR   InterPro; IPR003280; K_chnl_2pore.
DR   InterPro; IPR022306; K_chnl_2pore_TASK/TWIK.
DR   InterPro; IPR005408; K_chnl_2pore_TWIK.
DR   InterPro; IPR001779; K_chnl_2pore_TWIK1.
DR   PANTHER; PTHR11003:SF27; TWIK1_channel; 1.
DR   Pfam; PF07885; Ion_trans_2; 2.
DR   PIRSF; PIRSF038061; K_channel_subfamily_K_type; 1.
DR   PRINTS; PR01333; 2POREKCHANEL.
DR   PRINTS; PR01096; TWIK1CHANNEL.
DR   PRINTS; PR01586; TWIKCHANNEL.
PE   1: Evidence at protein level;
KW   Glycoprotein; Ion transport; Ionic channel; Membrane; Phosphoprotein;
KW   Potassium; Potassium channel; Potassium transport; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    336       Potassium channel subfamily K member 1.
FT                                /FTId=PRO_0000101741.
FT   TOPO_DOM      1     20       Cytoplasmic (Potential).
FT   TRANSMEM     21     41       Helical; (Potential).
FT   INTRAMEM    104    130       Pore-forming; Name=Pore-forming 1;
FT                                (Potential).
FT   TRANSMEM    133    153       Helical; (Potential).
FT   TOPO_DOM    154    177       Cytoplasmic (Potential).
FT   TRANSMEM    178    198       Helical; (Potential).
FT   INTRAMEM    212    238       Pore-forming; Name=Pore-forming 2;
FT                                (Potential).
FT   TRANSMEM    247    267       Helical; (Potential).
FT   TOPO_DOM    268    336       Cytoplasmic (Potential).
FT   MOD_RES     326    326       Phosphoserine.
FT   CARBOHYD     95     95       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   336 AA;  38275 MW;  A996060A18266FD4 CRC64;
     MLQSLAGSSC VRLVERHRSA WCFGFLVLGY LLYLVFGAVV FSSEELPYED LLRQELRKLK
     RRFLEEHECL SEPQLEQFLG RVLEASNYGV SVLSNASGNW NWDFTSALFF ASTVLSTTGY
     GHTVPLSDGG KAFCIIYSVI GIPFTLLFLT ALVQRVTVHV TRRPVLYFHI RWGFSKQVVA
     IVHAVLLGFV TVSCFFFIPA AVFSVLEDDW NFLESFYFCF ISLSTIGLGD YVPGEGYNQK
     FRELYKIGIT CYLLLGLITM LVVLETFCEL HELKKFRKMF YVKKDKDEDL VHIMEHDQLS
     FSSVTEQVAG LKEEQKQSEP FVASQSPPYE DGSADH
//
ID   GTPB1_MOUSE             Reviewed;         668 AA.
AC   O08582; Q3UD96; Q3UGW6; Q545R1; Q80ZY5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=GTP-binding protein 1;
DE            Short=G-protein 1;
DE            Short=GP-1;
DE            Short=GP1;
GN   Name=Gtpbp1; Synonyms=Gtpbp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Dendritic cell, Lung, and Melanocyte;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 35-668, AND TISSUE SPECIFICITY.
RX   MEDLINE=97223458; PubMed=9070279; DOI=10.1006/bbrc.1997.6103;
RA   Senju S., Nishimura Y.;
RT   "Identification of human and mouse GP-1, a putative member of a novel
RT   G-protein family.";
RL   Biochem. Biophys. Res. Commun. 231:360-364(1997).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-8; SER-12; SER-44
RP   AND SER-47, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-47, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- TISSUE SPECIFICITY: Expressed in brain, thymus, lung, and kidney.
CC   -!- SIMILARITY: Belongs to the GTPBP1 GTP-binding protein family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB51274.1; Type=Erroneous initiation;
CC       Sequence=BAB23409.1; Type=Erroneous initiation;
CC       Sequence=BAE28091.1; Type=Frameshift; Positions=631;
CC       Sequence=BAE29280.1; Type=Frameshift; Positions=666;
CC       Sequence=BAE29365.1; Type=Frameshift; Positions=666;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK004612; BAB23409.1; ALT_INIT; mRNA.
DR   EMBL; AK147717; BAE28091.1; ALT_FRAME; mRNA.
DR   EMBL; AK150068; BAE29280.1; ALT_FRAME; mRNA.
DR   EMBL; AK150185; BAE29365.1; ALT_FRAME; mRNA.
DR   EMBL; AK170091; BAE41557.1; -; mRNA.
DR   EMBL; BC046228; AAH46228.1; -; mRNA.
DR   EMBL; U87965; AAB51274.1; ALT_INIT; mRNA.
DR   IPI; IPI00761677; -.
DR   PIR; JC5292; JC5292.
DR   RefSeq; NP_038846.2; NM_013818.2.
DR   UniGene; Mm.19080; -.
DR   PDB; 1KJ2; X-ray; 2.71 A; P/Q=246-253.
DR   PDB; 1KJ3; X-ray; 2.30 A; P/Q=246-253.
DR   PDBsum; 1KJ2; -.
DR   PDBsum; 1KJ3; -.
DR   ProteinModelPortal; O08582; -.
DR   SMR; O08582; 159-576.
DR   STRING; O08582; -.
DR   PhosphoSite; O08582; -.
DR   PRIDE; O08582; -.
DR   Ensembl; ENSMUST00000046463; ENSMUSP00000043575; ENSMUSG00000042535.
DR   GeneID; 14904; -.
DR   KEGG; mmu:14904; -.
DR   NMPDR; fig|10090.3.peg.30262; -.
DR   UCSC; uc007wuf.1; mouse.
DR   CTD; 14904; -.
DR   MGI; MGI:109443; Gtpbp1.
DR   eggNOG; roNOG05004; -.
DR   GeneTree; ENSGT00580000081563; -.
DR   HOGENOM; HBG512879; -.
DR   HOVERGEN; HBG004471; -.
DR   InParanoid; O08582; -.
DR   OMA; REHQEAG; -.
DR   OrthoDB; EOG4CJVGS; -.
DR   PhylomeDB; O08582; -.
DR   NextBio; 287191; -.
DR   ArrayExpress; O08582; -.
DR   Bgee; O08582; -.
DR   CleanEx; MM_GTPBP1; -.
DR   Genevestigator; O08582; -.
DR   GermOnline; ENSMUSG00000042535; Mus musculus.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   InterPro; IPR000795; ProtSyn_GTP-bd.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   InterPro; IPR009000; Transl_elong_init/rib_B-barrel.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   SUPFAM; SSF50465; Elong_init_C; 1.
DR   SUPFAM; SSF50447; Translat_factor; 1.
PE   1: Evidence at protein level;
KW   3D-structure; GTP-binding; Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1    668       GTP-binding protein 1.
FT                                /FTId=PRO_0000122470.
FT   NP_BIND     167    174       GTP (Potential).
FT   NP_BIND     252    256       GTP (Potential).
FT   NP_BIND     308    311       GTP (Potential).
FT   COMPBIAS     28     36       Poly-Ala.
FT   MOD_RES       6      6       Phosphoserine.
FT   MOD_RES       8      8       Phosphoserine.
FT   MOD_RES      12     12       Phosphoserine.
FT   MOD_RES      24     24       Phosphoserine (By similarity).
FT   MOD_RES      25     25       Phosphoserine.
FT   MOD_RES      44     44       Phosphoserine.
FT   MOD_RES      47     47       Phosphoserine.
FT   MOD_RES     580    580       Phosphoserine (By similarity).
FT   MOD_RES     584    584       Phosphoserine (By similarity).
FT   CONFLICT    121    121       K -> E (in Ref. 1; BAE28091).
SQ   SEQUENCE   668 AA;  72301 MW;  E77C2148D6B237F8 CRC64;
     MAAERSRSPV DSPVPASMFA PEPSSPGAAR AAAAAARLHG GFDSDCSEDG EALNGEPELD
     LTSKLVLVSP TSEQYDSLLR QMWERMDEGC GETIYVIGQG SDGTEYGLSE ADMEASYATV
     KSMAEQIEAD VILLRERQEA GGRVRDYLVR KRVGDNDFLE VRVAVVGNVD AGKSTLLGVL
     THGELDNGRG FARQKLFRHK HEIESGRTSS VGNDILGFDS EGNVVNKPDS HGGSLEWTKI
     CEKSSKVITF IDLAGHEKYL KTTVFGMTGH LPDFCMLMVG SNAGIVGMTK EHLGLALALN
     VPVFVVVTKI DMCPANILQE TLKLLQRLLK SPGCRKIPVL VQSKDDVIVT ASNFSSERMC
     PIFQISNVTG ENLDLLKMFL NLLSPRTSYR EEEPAEFQID DTYSVPGVGT VVSGTTLRGL
     IKLNDTLLLG PDPLGNFLSI AVKSIHRKRM PVKEVRGGQT ASFALKKIKR SSIRKGMVMV
     SPRLNPQASW EFEAEILVLH HPTTISPRYQ AMVHCGSIRQ TATILSMDKD CLRTGDKATV
     HFRFIKTPEY LHIDQRLVFR EGRTKAVGTI TKLLQTTNNS PMNSKPQQIK MQSTKKGPLS
     KREEGGPCGV PAAGGPPTGD EASSLGTAQA ASTSGLQPQP KPSSGGRRRG GQRHKVKSGA
     CVTPASGC
//
ID   STXB1_MOUSE             Reviewed;         594 AA.
AC   O08599; A2ARS2; A2ARS3; A2ARS4; Q5WAC6; Q8VD51;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 2.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Syntaxin-binding protein 1;
DE   AltName: Full=Protein unc-18 homolog 1;
DE            Short=Unc18-1;
DE   AltName: Full=Protein unc-18 homolog A;
DE            Short=Unc-18A;
GN   Name=Stxbp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=96421662; PubMed=8824310;
RA   Gengyo-Ando K., Kitayama H., Mukaida M., Ikawa Y.;
RT   "A murine neural-specific homolog corrects cholinergic defects in
RT   Caenorhabditis elegans unc-18 mutants.";
RL   J. Neurosci. 16:6695-6702(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=98370997; PubMed=9705297; DOI=10.1074/jbc.273.34.21642;
RA   Gotoh K., Yokota H., Kikuya E., Watanabe T., Oishi M.;
RT   "Genomic structure of MUNC18-1 protein, which is involved in docking
RT   and fusion of synaptic vesicles in brain.";
RL   J. Biol. Chem. 273:21642-21647(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and DBA/2J; TISSUE=Brain;
RA   Fehr C., Buck K.J.;
RT   "Characterization of candidate genes for multiple ethanol influenced
RT   traits on mouse chromosome 2.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 30-39; 47-98; 101-120; 162-184; 193-225; 228-235;
RP   266-275; 278-314; 326-332; 344-356; 368-382; 389-425; 468-518 AND
RP   537-594.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-107; SER-142; TYR-145;
RP   SER-146; SER-345 AND THR-346, AND MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-473, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May participate in the regulation of synaptic vesicle
CC       docking and fusion, possibly through interaction with GTP-binding
CC       proteins. Essential for neurotransmission and binds syntaxin, a
CC       component of the synaptic vesicle fusion machinery probably in a
CC       1:1 ratio. Can interact with syntaxins 1, 2, and 3 but not
CC       syntaxin 4. May play a role in determining the specificity of
CC       intracellular fusion reactions (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O08599-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O08599-2; Sequence=VSP_010496;
CC   -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM20726.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D45903; BAA19479.1; -; mRNA.
DR   EMBL; AB012697; BAA32486.1; -; Genomic_DNA.
DR   EMBL; AF326545; AAL37391.1; -; mRNA.
DR   EMBL; AF326563; AAL37409.1; -; mRNA.
DR   EMBL; AL845471; CAM20726.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL845471; CAM20727.1; -; Genomic_DNA.
DR   EMBL; AL845471; CAM20728.1; -; Genomic_DNA.
DR   EMBL; BC031728; AAH31728.1; -; mRNA.
DR   IPI; IPI00415402; -.
DR   IPI; IPI00415403; -.
DR   RefSeq; NP_001107041.1; NM_001113569.1.
DR   RefSeq; NP_033321.2; NM_009295.2.
DR   UniGene; Mm.278865; -.
DR   ProteinModelPortal; O08599; -.
DR   SMR; O08599; 4-592.
DR   DIP; DIP-31951N; -.
DR   STRING; O08599; -.
DR   PhosphoSite; O08599; -.
DR   PRIDE; O08599; -.
DR   Ensembl; ENSMUST00000050000; ENSMUSP00000052440; ENSMUSG00000026797.
DR   GeneID; 20910; -.
DR   KEGG; mmu:20910; -.
DR   UCSC; uc008jha.1; mouse.
DR   UCSC; uc008jhb.1; mouse.
DR   CTD; 20910; -.
DR   MGI; MGI:107363; Stxbp1.
DR   eggNOG; roNOG12948; -.
DR   GeneTree; ENSGT00390000005206; -.
DR   HOVERGEN; HBG052710; -.
DR   OMA; DDDLWIT; -.
DR   OrthoDB; EOG4K6G3W; -.
DR   PhylomeDB; O08599; -.
DR   NextBio; 299797; -.
DR   ArrayExpress; O08599; -.
DR   Bgee; O08599; -.
DR   CleanEx; MM_STXBP1; -.
DR   Genevestigator; O08599; -.
DR   GermOnline; ENSMUSG00000026797; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0017075; F:syntaxin-1 binding; IPI:MGI.
DR   GO; GO:0007412; P:axon target recognition; IMP:MGI.
DR   GO; GO:0060292; P:long term synaptic depression; IMP:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptosis; IMP:MGI.
DR   GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; IDA:MGI.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:MGI.
DR   GO; GO:0007269; P:neurotransmitter secretion; IMP:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0016188; P:synaptic vesicle maturation; IMP:MGI.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; IMP:MGI.
DR   InterPro; IPR001619; Sec1-like.
DR   PANTHER; PTHR11679; Sec1-like; 1.
DR   Pfam; PF00995; Sec1; 1.
DR   SUPFAM; SSF56815; Sec1-like; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing; Phosphoprotein;
KW   Protein transport; Transport.
FT   CHAIN         1    594       Syntaxin-binding protein 1.
FT                                /FTId=PRO_0000206278.
FT   MOD_RES     107    107       Phosphothreonine.
FT   MOD_RES     142    142       Phosphoserine.
FT   MOD_RES     145    145       Phosphotyrosine.
FT   MOD_RES     146    146       Phosphoserine.
FT   MOD_RES     345    345       Phosphoserine.
FT   MOD_RES     346    346       Phosphothreonine.
FT   MOD_RES     473    473       Phosphotyrosine.
FT   MOD_RES     507    507       Phosphoserine.
FT   MOD_RES     509    509       Phosphoserine.
FT   VAR_SEQ     576    594       QKLLDTLKKLNKTDEEISS -> TKFLMDLRHPDFRESSRV
FT                                SFEDQAPTME (in isoform 2).
FT                                /FTId=VSP_010496.
FT   VARIANT     216    216       D -> N (in strain: DBA/2J).
FT   CONFLICT    101    101       A -> R (in Ref. 1; BAA19479).
FT   CONFLICT    367    367       R -> H (in Ref. 2; BAA32486).
FT   CONFLICT    537    537       L -> F (in Ref. 1; BAA19479).
FT   CONFLICT    561    561       G -> A (in Ref. 1; BAA19479).
SQ   SEQUENCE   594 AA;  67569 MW;  2DD0715F875CE0F3 CRC64;
     MAPIGLKAVV GEKIMHDVIK KVKKKGEWKV LVVDQLSMRM LSSCCKMTDI MTEGITIVED
     INKRREPLPS LEAVYLITPS EKSVHSLISD FKDPPTAKYR AAHVFFTDSC PDALFNELVK
     SRAAKVIKTL TEINIAFLPY ESQVYSLDSA DSFQSFYSPH KAQMKNPILE RLAEQIATLC
     ATLKEYPAVR YRGEYKDNAL LAQLIQDKLD AYKADDPTMG EGPDKARSQL LILDRGFDPS
     SPVLHELTFQ AMSYDLLPIE NDVYKYETSG IGEARVKEVL LDEDDDLWIA LRHKHIAEVS
     QEVTRSLKDF SSSKRMNTGE KTTMRDLSQM LKKMPQYQKE LSKYSTHLHL AEDCMKHYQG
     TVDKLCRVEQ DLAMGTDAEG EKIKDPMRAI VPILLDANVS TYDKIRIILL YIFLKNGITE
     ENLNKLIQHA QIPPEDSEII TNMAHLGVPI VTDSTLRRRS KPERKERISE QTYQLSRWTP
     IIKDIMEDTI EDKLDTKHYP YISTRSSASF STTAVSARYG HWHKNKAPGE YRSGPRLIIF
     ILGGVSLNEM RCAYEVTQAN GKWEVLIGST HILTPQKLLD TLKKLNKTDE EISS
//
ID   M3K4_MOUSE              Reviewed;        1597 AA.
AC   O08648; O08649; O70124;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Mitogen-activated protein kinase kinase kinase 4;
DE            EC=2.7.11.25;
DE   AltName: Full=MAPK/ERK kinase kinase 4;
DE            Short=MEK kinase 4;
DE            Short=MEKK 4;
GN   Name=Map3k4; Synonyms=Mekk4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, INTERACTION
RP   WITH CDC42, AND MUTAGENESIS OF LYS-1361.
RC   TISSUE=Brain;
RX   MEDLINE=97236778; PubMed=9079650; DOI=10.1074/jbc.272.13.8288;
RA   Gerwins P., Blank J.L., Johnson G.L.;
RT   "Cloning of a novel mitogen-activated protein kinase kinase kinase,
RT   MEKK4, that selectively regulates the c-Jun amino terminal kinase
RT   pathway.";
RL   J. Biol. Chem. 272:8288-8295(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 363-1049.
RC   STRAIN=C57BL/6; TISSUE=Ectoplacental cone;
RX   MEDLINE=97422605; PubMed=9268631; DOI=10.1006/geno.1997.4816;
RA   Schweifer N., Valk P.J., Delwel R., Cox R., Francis F.,
RA   Meier-Ewert S., Lehrach H., Barlow D.P.;
RT   "Characterization of the C3 YAC contig from proximal mouse chromosome
RT   17 and analysis of allelic expression of genes flanking the imprinted
RT   Igf2r gene.";
RL   Genomics 43:285-297(1997).
RN   [3]
RP   INTERACTION WITH AXIN1 AND DIXDC1.
RX   PubMed=15262978; DOI=10.1074/jbc.M404598200;
RA   Wong C.K., Luo W., Deng Y., Zou H., Ye Z., Lin S.-C.;
RT   "The DIX domain protein coiled-coil-DIX1 inhibits c-Jun N-terminal
RT   kinase activation by Axin and dishevelled through distinct
RT   mechanisms.";
RL   J. Biol. Chem. 279:39366-39373(2004).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-1361, AND
RP   INTERACTION WITH TRAF4.
RX   PubMed=16157600; DOI=10.1074/jbc.C500260200;
RA   Abell A.N., Johnson G.L.;
RT   "MEKK4 is an effector of the embryonic TRAF4 for JNK activation.";
RL   J. Biol. Chem. 280:35793-35796(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Component of a protein kinase signal transduction
CC       cascade. Activates the CSBP2, P38 and JNK MAPK pathways, but not
CC       the ERK pathway. Specifically phosphorylates and activates MAP2K4
CC       and MAP2K6.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: N-terminal autoinhibitory domain interacts with
CC       the C-terminal kinase domain, inhibiting kinase activity, and
CC       prevening interaction with its substrate, MAP2K6. The GADD45
CC       proteins activate the kinase by binding to the N-terminal domain.
CC       Activated by phosphorylation on Thr-1494 (By similarity).
CC   -!- SUBUNIT: Monomer and homodimer. Homodimerization enhances kinase
CC       activity. Interacts with TRAF4; this promotes homodimerization.
CC       Binds both upstream activators and downstream substrates in
CC       multimolecular complexes. Interacts with AXIN1 and DIXDC1;
CC       interaction with DIXDC1 prevents interaction with AXIN1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region.
CC       Note=Localized in perinuclear vesicular-like structures, probably
CC       Golgi-associated vesicles.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=O08648-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=O08648-2; Sequence=VSP_004885;
CC   -!- TISSUE SPECIFICITY: Widely expressed. High expression was found in
CC       skeletal muscle, kidney, testis followed by heart brain and lung.
CC       Low expression was found in spleen.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; U85607; AAC53126.1; -; mRNA.
DR   EMBL; U85608; AAC53127.1; -; mRNA.
DR   EMBL; U66240; AAC08286.1; -; mRNA.
DR   IPI; IPI00623304; -.
DR   IPI; IPI00875136; -.
DR   UniGene; Mm.28587; -.
DR   ProteinModelPortal; O08648; -.
DR   SMR; O08648; 1332-1592.
DR   STRING; O08648; -.
DR   PhosphoSite; O08648; -.
DR   PRIDE; O08648; -.
DR   Ensembl; ENSMUST00000074585; ENSMUSP00000074170; ENSMUSG00000014426.
DR   Ensembl; ENSMUST00000089058; ENSMUSP00000086459; ENSMUSG00000014426.
DR   UCSC; uc008ako.1; mouse.
DR   MGI; MGI:1346875; Map3k4.
DR   eggNOG; roNOG07433; -.
DR   HOGENOM; HBG714205; -.
DR   HOVERGEN; HBG006304; -.
DR   InParanoid; O08648; -.
DR   OrthoDB; EOG46MBHQ; -.
DR   BRENDA; 2.7.11.25; 244.
DR   ArrayExpress; O08648; -.
DR   Bgee; O08648; -.
DR   CleanEx; MM_MAP3K4; -.
DR   Genevestigator; O08648; -.
DR   GermOnline; ENSMUSG00000014426; Mus musculus.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0007243; P:intracellular protein kinase cascade; IDA:UniProtKB.
DR   GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1   1597       Mitogen-activated protein kinase kinase
FT                                kinase 4.
FT                                /FTId=PRO_0000086248.
FT   DOMAIN     1332   1590       Protein kinase.
FT   NP_BIND    1338   1346       ATP (By similarity).
FT   COMPBIAS   1178   1182       Poly-Ala.
FT   ACT_SITE   1452   1452       Proton acceptor (By similarity).
FT   BINDING    1361   1361       ATP.
FT   MOD_RES     440    440       Phosphothreonine (By similarity).
FT   MOD_RES     492    492       Phosphoserine.
FT   MOD_RES    1494   1494       Phosphothreonine (By similarity).
FT   VAR_SEQ    1162   1213       Missing (in isoform B).
FT                                /FTId=VSP_004885.
FT   MUTAGEN    1361   1361       K->A,R: Loss of kinase activity.
FT   CONFLICT    363    364       SL -> NS (in Ref. 2; AAC08286).
FT   CONFLICT    473    473       T -> A (in Ref. 2; AAC08286).
SQ   SEQUENCE   1597 AA;  179949 MW;  E84AEAAE92D103A4 CRC64;
     MRDAIAEPVP PPALADTPAA AMEELRPAPP PQPEPDPECC PAARQECMLG ESARKSMESD
     PEDFSDETNT ETLYGTSPPS TPRQMKRLSA KHQRNSAGRP ASRSNLKEKM NTPSQSPHKD
     LGKGVETVEE YSYKQEKKIR ATLRTTERDH KKNAQCSFML DSVAGSLPKK SIPDVDLNKP
     YLSLGCSNAK LPVSMPMPIA RTARQTSRTD CPADRLKFFE TLRLLLKLTS VSKKKDREQR
     GQENTAAFWF NRSNELIWLE LQAWHAGRTI NDQDLFLYTA RQAIPDIINE ILTFKVNYGS
     IAFSSNGAGF NGPLVEGQCR TPQETNRVGC SSYHEHLQRQ RVSFEQVKRI MELLEYMEAL
     YPSLQALQKD YERYAAKDFE DRVQALCLWL NITKDLNQKL RIMGTVLGIK NLSDIGWPVF
     EIPSPRPSKG YEPEDEVEDT EVELRELESG TEESDEEPTP SPRVPELRLS TDTILDSRSQ
     GCVSRKLERL ESEEDSIGWG TADCGPEASR HCLTSIYRPF VDKALKQMGL RKLILRLHKL
     MNGSLQRARV ALVKDDRPVE FSDFPGPMWG SDYVQLSGTP PSSEQKCSAV SWEELRAMDL
     PSFEPAFLVL CRVLLNVIHE CLKLRLEQRP AGEPSLLSIK QLVRECKEVL KGGLLMKQYY
     QFMLQEVLGG LEKTDCNMDA FEEDLQKMLM VYFDYMRSWI QMLQQLPQAS HSLKNLLEEE
     WNFTKEITHY IRGGEAQAGK LFCDIAGMLL KSTGSFLESG LQESCAELWT SADDNGAADE
     LRRSVIEISR ALKELFHEAR ERASKALGFA KMLRKDLEIA AEFVLSASAR ELLDALKAKQ
     YVKVQIPGLE NLHVFVPDSL AEEKKIILQL LNAATGKDCS KDPDDVFMDA FLLLTKHGDR
     ARDSEDGWGT WEARAVKIVP QVETVDTLRS MQVDNLLLVV MESAHLVLQR KAFQQSIEGL
     MTVRHEQTSS QPIIAKGLQQ LKNDALELCN RISDAIDRVD HMFTLEFDAE VEESESATLQ
     QYYREAMIQG YNFGFEYHKE VVRLMSGEFR QKIGDKYISF AQKWMNYVLT KCESGRGTRP
     RWATQGFDFL QAIEPAFISA LPEDDFLSLQ ALMNECIGHV IGKPHSPVTA IHRNSPRPVK
     VPRCHSDPPN PHLIIPTPEG FSTRSVPSDA RTHGNSVAAA AAVRAAATTA AGRPGPGGGD
     SVPAKPVNTA PDTRGSSVPE NDRLASIAAE LQFRSLSRHS SPTEERDEPA YPRSDSSGST
     RRSWELRTLI SQTKDSASKQ GPIEAIQKSV RLFEERRYRE MRRKNIIGQV CDTPKSYDNV
     MHVGLRKVTF KWQRGNKIGE GQYGKVYTCI SVDTGELMAM KEIRFQPNDH KTIKETADEL
     KIFEGIKHPN LVRYFGVELH REEMYIFMEY CDEGTLEEVS RLGLQEHVIR LYTKQITVAI
     NVLHEHGIVH RDIKGANIFL TSSGLIKLGD FGCSVKLKNN AQTMPGEVNS TLGTAAYMAP
     EVITRAKGEG HGRAADIWSL GCVVIEMVTG KRPWHEYEHN FQIMYKVGMG HKPPIPERLS
     PEGKAFLSHC LESDPKIRWT ASQLLDHAFV KVCTDEE
//
ID   AMPM2_MOUSE             Reviewed;         478 AA.
AC   O08663;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Methionine aminopeptidase 2;
DE            Short=MAP 2;
DE            Short=MetAP 2;
DE            EC=3.4.11.18;
DE   AltName: Full=Initiation factor 2-associated 67 kDa glycoprotein;
DE   AltName: Full=Peptidase M 2;
DE   AltName: Full=p67eIF2;
DE            Short=p67;
GN   Name=Metap2; Synonyms=Mnpep, P67eif2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RA   Sekiguchi S., Suzuki E.;
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 260-281; 297-318; 355-371 AND 386-395, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: Removes the amino-terminal methionine from nascent
CC       proteins (By similarity).
CC   -!- FUNCTION: Protects eIF-2 alpha-subunit from inhibitory
CC       phosphorylation by eIF-2 kinases. Plays a critical role in the
CC       regulation of protein synthesis. It also interacts with the eIF-2
CC       gamma-subunit (By similarity).
CC   -!- CATALYTIC ACTIVITY: Release of N-terminal amino acids,
CC       preferentially methionine, from peptides and arylamides.
CC   -!- COFACTOR: Binds 2 cobalt ions per subunit. The true nature of the
CC       physiological cofactor is under debate. The enzyme is also active
CC       with zinc, manganese or divalent iron ions (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase M24A family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB003144; BAA19789.1; -; mRNA.
DR   EMBL; AK076804; BAC36488.1; -; mRNA.
DR   EMBL; BC002213; AAH02213.1; -; mRNA.
DR   IPI; IPI00272238; -.
DR   RefSeq; NP_062622.1; NM_019648.3.
DR   UniGene; Mm.289329; -.
DR   ProteinModelPortal; O08663; -.
DR   SMR; O08663; 110-478.
DR   STRING; O08663; -.
DR   MEROPS; M24.002; -.
DR   PhosphoSite; O08663; -.
DR   PRIDE; O08663; -.
DR   Ensembl; ENSMUST00000047910; ENSMUSP00000048285; ENSMUSG00000036112.
DR   GeneID; 56307; -.
DR   KEGG; mmu:56307; -.
DR   UCSC; uc007gve.1; mouse.
DR   CTD; 56307; -.
DR   MGI; MGI:1929701; Metap2.
DR   eggNOG; roNOG14581; -.
DR   HOVERGEN; HBG050495; -.
DR   InParanoid; O08663; -.
DR   OrthoDB; EOG46T31M; -.
DR   PhylomeDB; O08663; -.
DR   BRENDA; 3.4.11.18; 244.
DR   NextBio; 312244; -.
DR   ArrayExpress; O08663; -.
DR   Bgee; O08663; -.
DR   CleanEx; MM_METAP2; -.
DR   Genevestigator; O08663; -.
DR   GermOnline; ENSMUSG00000036112; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:HGNC.
DR   GO; GO:0004177; F:aminopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008235; F:metalloexopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0031365; P:N-terminal protein amino acid modification; ISS:HGNC.
DR   GO; GO:0018206; P:peptidyl-methionine modification; ISS:HGNC.
DR   GO; GO:0016485; P:protein processing; ISS:HGNC.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR001714; Pept_M24_MAP.
DR   InterPro; IPR000994; Pept_M24_structural-domain.
DR   InterPro; IPR002468; Pept_M24A_MAP2.
DR   InterPro; IPR018349; Pept_M24A_MAP2_BS.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:3.90.230.10; Peptidase_M24_cat_core; 2.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   PANTHER; PTHR10804:SF9; Pept_M24A_MAP2; 1.
DR   PANTHER; PTHR10804; Peptidase_M24_cat_core; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   PRINTS; PR00599; MAPEPTIDASE.
DR   SUPFAM; SSF55920; Peptidase_M24_cat_core; 1.
DR   TIGRFAMs; TIGR00501; met_pdase_II; 1.
DR   PROSITE; PS01202; MAP_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Aminopeptidase; Cobalt; Direct protein sequencing;
KW   Hydrolase; Metal-binding; Phosphoprotein; Protease.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    478       Methionine aminopeptidase 2.
FT                                /FTId=PRO_0000148983.
FT   COMPBIAS     36     46       Arg/Lys-rich (basic).
FT   COMPBIAS     82     93       Asp/Glu-rich (acidic).
FT   COMPBIAS     98    106       Poly-Lys.
FT   METAL       251    251       Cobalt 1 (By similarity).
FT   METAL       262    262       Cobalt 1 (By similarity).
FT   METAL       262    262       Cobalt 2 (By similarity).
FT   METAL       331    331       Cobalt 2 (By similarity).
FT   METAL       364    364       Cobalt 2 (By similarity).
FT   METAL       459    459       Cobalt 1 (By similarity).
FT   METAL       459    459       Cobalt 2 (By similarity).
FT   BINDING     231    231       Substrate (By similarity).
FT   BINDING     339    339       Substrate (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      60     60       Phosphoserine (By similarity).
FT   MOD_RES     427    427       N6-acetyllysine (By similarity).
SQ   SEQUENCE   478 AA;  52922 MW;  BBB9A2AFC19952E8 CRC64;
     MAGVEQAASF GGHLNGDLDP DDREEGTSST AEEAAKKKRR KKKKGKGAVS AVQQELDKES
     GALVDEVAKQ LESQALEEKE RDDDDEDGDG DADGATGKKK KKKKKKRGPK VQTDPPSVPI
     CDLYPNGVFP KGQECEYPPT QDGRTAAWRT TSEEKKALDQ ASEEIWNDFR EAAEAHRQVR
     KYVMSWIKPG MTMIEICEKL EDCSRKLIKE NGLNAGLAFP TGCSLNNCAA HYTPNAGDTT
     VLQYDDICKI DFGTHISGRI IDCAFTVTFN PKYDILLTAV KDATNTGIKC AGIDVRLCDV
     GEAIQEVMES YEVEIDGKTY QVKPIRNLNG HSIGPYRIHA GKTVPIVKGG EATRMEEGEV
     YAIETFGSTG KGVVHDDMEC SHYMKNFDVG HVPIRLPRTK HLLNVINENF GTLAFCRRWL
     DRLGESKYLM ALKNLCDLGI VDPYPPLCDI KGSYTAQFEH TILLRPTCKE VVSRGDDY
//
ID   CAN5_MOUSE              Reviewed;         640 AA.
AC   O08688; Q91YU0;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Calpain-5;
DE            EC=3.4.22.-;
DE   AltName: Full=New calpain 3;
DE            Short=nCL-3;
GN   Name=Capn5; Synonyms=Ncl3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=97480729; PubMed=9339374; DOI=10.1006/geno.1997.4870;
RA   Dear T.N., Matena K., Vingron M., Boehm T.;
RT   "A new subfamily of vertebrate calpains lacking a calmodulin-like
RT   domain: implications for calpain regulation and evolution.";
RL   Genomics 45:175-184(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-427.
RX   MEDLINE=98163754; PubMed=9503024; DOI=10.1006/geno.1997.5133;
RA   Matena K., Boehm T., Dear N.T.;
RT   "Genomic organization of mouse Capn5 and Capn6 genes confirms that
RT   they are a distinct calpain subfamily.";
RL   Genomics 48:117-120(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Algate P.A.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-427.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: Broad endopeptidase specificity.
CC   -!- SIMILARITY: Belongs to the peptidase C2 family.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 calpain catalytic domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; Y10656; CAA71666.1; -; mRNA.
DR   EMBL; U85020; AAD00559.1; -; mRNA.
DR   EMBL; BC014767; AAH14767.1; -; mRNA.
DR   IPI; IPI00114962; -.
DR   RefSeq; NP_031628.1; NM_007602.3.
DR   UniGene; Mm.326847; -.
DR   ProteinModelPortal; O08688; -.
DR   SMR; O08688; 3-501, 516-631.
DR   STRING; O08688; -.
DR   MEROPS; C02.011; -.
DR   PRIDE; O08688; -.
DR   Ensembl; ENSMUST00000040971; ENSMUSP00000048183; ENSMUSG00000035547.
DR   Ensembl; ENSMUST00000107112; ENSMUSP00000102729; ENSMUSG00000035547.
DR   GeneID; 12337; -.
DR   KEGG; mmu:12337; -.
DR   UCSC; uc009ikc.1; mouse.
DR   CTD; 12337; -.
DR   MGI; MGI:1100859; Capn5.
DR   eggNOG; roNOG11514; -.
DR   HOGENOM; HBG506448; -.
DR   HOVERGEN; HBG001095; -.
DR   InParanoid; O08688; -.
DR   OMA; EQEWDPE; -.
DR   OrthoDB; EOG4DV5KQ; -.
DR   PhylomeDB; O08688; -.
DR   NextBio; 280956; -.
DR   ArrayExpress; O08688; -.
DR   Bgee; O08688; -.
DR   CleanEx; MM_CAPN5; -.
DR   Genevestigator; O08688; -.
DR   GermOnline; ENSMUSG00000035547; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR022684; Calpain_cysteine_protease.
DR   InterPro; IPR022682; Calpain_domain_III.
DR   InterPro; IPR022683; Calpain_III.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF01067; Calpain_III; 1.
DR   Pfam; PF00648; Peptidase_C2; 1.
DR   PRINTS; PR00704; CALPAIN.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00720; calpain_III; 1.
DR   SMART; SM00230; CysPc; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF49758; Peptidase_C2; 1.
DR   PROSITE; PS50004; C2; FALSE_NEG.
DR   PROSITE; PS50203; CALPAIN_CAT; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; FALSE_NEG.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Hydrolase; Polymorphism; Protease; Thiol protease.
FT   CHAIN         1    640       Calpain-5.
FT                                /FTId=PRO_0000207714.
FT   DOMAIN       26    343       Calpain catalytic.
FT   DOMAIN      518    619       C2.
FT   REGION      344    496       Domain III.
FT   ACT_SITE     81     81       By similarity.
FT   ACT_SITE    252    252       By similarity.
FT   ACT_SITE    284    284       By similarity.
FT   VARIANT     427    427       D -> N.
SQ   SEQUENCE   640 AA;  72955 MW;  7F1DA3E299FEC02D CRC64;
     MFSCAKAYED QNYSALKRAC LRKKVLFEDP LFPATDDSLY YKGTPGPTVR WKRPKDICDD
     PRLFVDGISS HDLHQGQVGN CWFVAACSSL ASRESLWQKV IPDWKEQEWN PEKPDSYAGI
     FHFNFWRFGE WVDVIVDDRL PTVNNQLIYC HSNSKNEFWC ALVEKAYAKL AGCYQALDGG
     NTADALVDFT GGVSEPIDLT EGDLATDEAK RNQLFERVLK VHSRGGLISA SIKAVTAADM
     EARLACGLVK GHAYAVTDVR KVRLGHGLLA FFKSEKLDMI RLRNPWGERE WTGPWSDTSE
     EWQKVSKSER EKMGVTVQDD GEFWMTFEDM CRYFTDIIKC RLINTSYLSI HKTWEEARLH
     GAWTRHEDPQ QNRSGGCINH KDTFFQNPQY VFEVKKPEDE VLISIQQRPK RSTRREGKGE
     NLAIGFDIYK VEENRQYRMH SLQHKAASSI YINSRSVFLR TELPEGRYVI IPTTFEPGHT
     GEFLLRVFTD VPSNCRELRL DEPPRTCWSS LCGYPQQVAQ VHVLGAAGLK DSPTGANSYV
     IIKCEGEKVR SAVQRGTSTP EYNVKGIFYR KKLAQPITVQ VWNHRVLKDE FLGQVHLKTA
     PDDLQDLHTL HLQDRSSRQP SDLPGIVAVR VLCSASLTAV
//
ID   AKAP1_MOUSE             Reviewed;         857 AA.
AC   O08715; O08714; P97488;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 3.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=A-kinase anchor protein 1, mitochondrial;
DE   AltName: Full=Dual specificity A-kinase-anchoring protein 1;
DE            Short=D-AKAP-1;
DE   AltName: Full=Protein kinase A-anchoring protein 1;
DE            Short=PRKA1;
DE   AltName: Full=Spermatid A-kinase anchor protein;
DE            Short=S-AKAP;
DE   Flags: Precursor;
GN   Name=Akap1; Synonyms=Akap;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC   TISSUE=Embryo;
RX   MEDLINE=97218247; PubMed=9065479; DOI=10.1074/jbc.272.12.8057;
RA   Huang L.J.-S., Durick K., Weiner J.A., Chun J., Taylor S.S.;
RT   "Identification of a novel protein kinase A anchoring protein that
RT   binds both type I and type II regulatory subunits.";
RL   J. Biol. Chem. 272:8057-8064(1997).
RN   [2]
RP   SEQUENCE REVISION.
RA   Huang L.J.-S., Durick K., Taylor S.S.;
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 5 AND 6).
RC   STRAIN=BALB/c; TISSUE=Testis;
RX   MEDLINE=97326098; PubMed=9182549; DOI=10.1074/jbc.272.24.15247;
RA   Chen Q., Lin R.-Y., Rubin C.S.;
RT   "Organelle-specific targeting of protein kinase AII (PKAII). Molecular
RT   and in situ characterization of murine A kinase anchor proteins that
RT   recruit regulatory subunits of PKAII to the cytoplasmic surface of
RT   mitochondria.";
RL   J. Biol. Chem. 272:15247-15257(1997).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=99286244; PubMed=10352013; DOI=10.1083/jcb.145.5.951;
RA   Huang L.J.-S., Wang L., Ma Y., Durick K., Perkins G., Deerinck T.J.,
RA   Ellisman M.H., Taylor S.S.;
RT   "NH2-Terminal targeting motifs direct dual specificity A-kinase-
RT   anchoring protein 1 (D-AKAP1) to either mitochondria or endoplasmic
RT   reticulum.";
RL   J. Cell Biol. 145:951-959(1999).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; SER-101 AND SER-103,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Differentially targeted protein that binds to type I and
CC       II regulatory subunits of protein kinase A. Anchors them to the
CC       cytoplasmic face of the mitochondrial outer membrane or allows
CC       them to reside in the endoplasmic reticulum. Does not contain the
CC       classic KDEL endoplasmic reticulum-targeting sequence. This
CC       explains how it is able to switch its localization, either being
CC       in the endoplasmic reticulum or in the mitochondria depending on
CC       which N-terminal part begins the isoform. The longest N-terminal
CC       part only present in isoform 2 and isoform 4 acts as a suppressor
CC       of mitochondrial targeting and as an activator of recessive
CC       endoplasmic reticulum targeting motif.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Endoplasmic reticulum.
CC   -!- SUBCELLULAR LOCATION: Isoform 4: Endoplasmic reticulum.
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Mitochondrion outer membrane.
CC   -!- SUBCELLULAR LOCATION: Isoform 3: Mitochondrion outer membrane.
CC   -!- SUBCELLULAR LOCATION: Isoform 5: Mitochondrion outer membrane.
CC   -!- SUBCELLULAR LOCATION: Isoform 6: Mitochondrion outer membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=3; Synonyms=D-AKAP1C, AKAP121;
CC         IsoId=O08715-1; Sequence=Displayed;
CC       Name=1; Synonyms=D-AKAP1A;
CC         IsoId=O08715-2; Sequence=VSP_002848, VSP_002849;
CC       Name=2; Synonyms=D-AKAP1B;
CC         IsoId=O08715-3; Sequence=VSP_002847, VSP_002848, VSP_002849;
CC       Name=4; Synonyms=D-AKAP1D;
CC         IsoId=O08715-4; Sequence=VSP_002847;
CC       Name=5; Synonyms=S-AKAP84;
CC         IsoId=O08715-5; Sequence=VSP_002850, VSP_002851;
CC       Name=6; Synonyms=AKAP100;
CC         IsoId=O08715-6; Sequence=VSP_002852, VSP_002853;
CC   -!- TISSUE SPECIFICITY: Highest expression in testis, heart, liver,
CC       skeletal muscle, intestine and kidney, followed by brain and lung.
CC       No expression in spleen. Isoform 1/D-AKAP1A is expressed
CC       predominantly in testis whereas isoform 4/D-AKAP1D is expressed
CC       primarily in liver.
CC   -!- DOMAIN: RII-alpha binding site, predicted to form an amphipathic
CC       helix, could participate in protein-protein interactions with a
CC       complementary surface on the R-subunit dimer.
CC   -!- SIMILARITY: Contains 1 KH domain.
CC   -!- SIMILARITY: Contains 1 Tudor domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U84389; AAC27100.1; -; mRNA.
DR   EMBL; U95145; AAB53740.1; -; mRNA.
DR   EMBL; U95146; AAB53741.1; -; mRNA.
DR   IPI; IPI00115506; -.
DR   IPI; IPI00230589; -.
DR   IPI; IPI00230590; -.
DR   IPI; IPI00230591; -.
DR   IPI; IPI00230592; -.
DR   IPI; IPI00230593; -.
DR   UniGene; Mm.2969; -.
DR   ProteinModelPortal; O08715; -.
DR   SMR; O08715; 563-631, 663-850.
DR   MINT; MINT-4087417; -.
DR   STRING; O08715; -.
DR   PhosphoSite; O08715; -.
DR   PRIDE; O08715; -.
DR   Ensembl; ENSMUST00000018572; ENSMUSP00000018572; ENSMUSG00000018428.
DR   Ensembl; ENSMUST00000107902; ENSMUSP00000103535; ENSMUSG00000018428.
DR   Ensembl; ENSMUST00000107903; ENSMUSP00000103536; ENSMUSG00000018428.
DR   Ensembl; ENSMUST00000107904; ENSMUSP00000103537; ENSMUSG00000018428.
DR   MGI; MGI:104729; Akap1.
DR   eggNOG; roNOG04568; -.
DR   GeneTree; ENSGT00390000001360; -.
DR   HOGENOM; HBG505861; -.
DR   HOVERGEN; HBG057436; -.
DR   InParanoid; O08715; -.
DR   OrthoDB; EOG40GCR6; -.
DR   ArrayExpress; O08715; -.
DR   Bgee; O08715; -.
DR   CleanEx; MM_AKAP1; -.
DR   Genevestigator; O08715; -.
DR   GermOnline; ENSMUSG00000018428; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR004088; KH_type_1.
DR   InterPro; IPR018111; KH_type_1_subgr.
DR   InterPro; IPR008191; Maternal_tudor.
DR   InterPro; IPR002999; Tudor.
DR   InterPro; IPR018351; Tudor_subgroup.
DR   Pfam; PF00013; KH_1; 1.
DR   Pfam; PF00567; TUDOR; 1.
DR   SMART; SM00322; KH; 1.
DR   SMART; SM00333; TUDOR; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
DR   PROSITE; PS50304; TUDOR; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endoplasmic reticulum; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Phosphoprotein; RNA-binding;
KW   Transit peptide; Transmembrane.
FT   TRANSIT       1     29       Mitochondrion (By similarity).
FT   CHAIN        30    857       A-kinase anchor protein 1, mitochondrial.
FT                                /FTId=PRO_0000016660.
FT   DOMAIN      561    625       KH.
FT   DOMAIN      712    771       Tudor.
FT   REGION      306    319       PKA-RII subunit binding domain.
FT   MOD_RES      55     55       Phosphoserine.
FT   MOD_RES     101    101       Phosphoserine.
FT   MOD_RES     103    103       Phosphoserine.
FT   MOD_RES     164    164       Phosphoserine (By similarity).
FT   MOD_RES     487    487       Phosphothreonine (By similarity).
FT   VAR_SEQ       1      1       M -> MGCKTGPKPFGGGETIRPIRIRRCSYFTSTDSKM
FT                                (in isoform 2 and isoform 4).
FT                                /FTId=VSP_002847.
FT   VAR_SEQ     526    547       GSDGNSMDSVDSCCGLTKPDSP -> VAAPPQERGHFGNGG
FT                                CTGFFEC (in isoform 5).
FT                                /FTId=VSP_002850.
FT   VAR_SEQ     527    544       SDGNSMDSVDSCCGLTKP -> RKVLGCFLGESGRGPIIC
FT                                (in isoform 1 and isoform 2).
FT                                /FTId=VSP_002848.
FT   VAR_SEQ     545    857       Missing (in isoform 1 and isoform 2).
FT                                /FTId=VSP_002849.
FT   VAR_SEQ     548    857       Missing (in isoform 5).
FT                                /FTId=VSP_002851.
FT   VAR_SEQ     614    637       SQHHVDKALNLIGKKFKELNLTNI -> CVSVLTRRLSAPC
FT                                RQSSELDWEEV (in isoform 6).
FT                                /FTId=VSP_002852.
FT   VAR_SEQ     638    857       Missing (in isoform 6).
FT                                /FTId=VSP_002853.
FT   CONFLICT    220    220       S -> I (in Ref. 2; AAC27100).
FT   CONFLICT    327    327       P -> A (in Ref. 2; AAC27100).
SQ   SEQUENCE   857 AA;  92165 MW;  62442798BC8AED7D CRC64;
     MAIQLRSLFP LALPGMLALL GWWWFFSRKK DRLSSSDKQV ETLKVGPAIK DRRLSEEACP
     GVLSVAPTVT QPPGREEQRS VDKPSTEPLA LPRTRQVRRR SESSGNLPSV ADTRSQPGPC
     RDEIAKVELS LMGDKAKSIP LGCPLLPKDA SFPYEAVERC KQESALGKTP GRGWPSPYAA
     SGEKARETGG TEGTGDAVLG ENVSEEGLLS QECVSEVEKS EFPILAPGGG EGEEVSHGPP
     QVAELLKKEE YIVGKLPSSF VEPVHSEPVK DEDALEPQVK GSSNTSDRDL AGELDKDETV
     PENDQIKQAA FQLISQVILE ATEELRPTTV GKTVAQVHPI SATQPKGKEE SCVPASQETS
     LGQDTSDPAS TRTGATASPS AEALPPKTYV SCLSSPLSGP TKDQKPKNSA HHISLAPCPP
     PVTPQRQSLE GASNPRGDDN FVACMANNSQ SVLSVSSLGQ CSDPVSTSGL EDSCTETISS
     SGDKAITPPL PVSTQPFSNG VLKEELSDLG TEDGWTMDTE ADHSGGSDGN SMDSVDSCCG
     LTKPDSPQSV QAGSNPKKVD LIIWEIEVPK HLVGRLIGKQ GRYVSFLKQT SGAKIYISTL
     PYTQNIQICH IEGSQHHVDK ALNLIGKKFK ELNLTNIYAP PLPSLALPSL PMTSWLMLPD
     GITVEVIVVN QVNAGHLFVQ QHTHPTFHAL RSLDQQMYLC YSQPGIPTLP TPVEITVICA
     APGADGAWWR AQVVASYEET NEVEIRYVDY GGYKRVKVDV LRQIRSDFVT LPFQGAEVLL
     DSVVPLSDDD HFSPEADAAM SEMTGNTALL AQVTSYSATG LPLIQLWSVV GDEVVLINRS
     LVERGLAQWV DSYYASL
//
ID   O08744_MOUSE            Unreviewed;       304 AA.
AC   O08744;
DT   01-JUL-1997, integrated into UniProtKB/TrEMBL.
DT   01-JUL-1997, sequence version 1.
DT   08-FEB-2011, entry version 58.
DE   SubName: Full=Emr1;
DE   Flags: Fragment;
GN   Name=Emr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=97312684; PubMed=9169125; DOI=10.1006/geno.1997.4674;
RA   Lin H.H., Stubbs L.J., Mucenski M.L.;
RT   "Identification and characterization of a seven transmembrane hormone
RT   receptor using differential display.";
RL   Genomics 41:301-308(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Lin H.-H., Mucenski M.L.;
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; U66891; AAC53187.1; -; mRNA.
DR   IPI; IPI00115560; -.
DR   UniGene; Mm.2254; -.
DR   HSSP; P35555; 1EMN.
DR   ProteinModelPortal; O08744; -.
DR   STRING; O08744; -.
DR   Ensembl; ENSMUST00000086763; ENSMUSP00000083971; ENSMUSG00000004730.
DR   MGI; MGI:106912; Emr1.
DR   GeneTree; ENSGT00600000084176; -.
DR   ArrayExpress; O08744; -.
DR   Bgee; O08744; -.
DR   Genevestigator; O08744; -.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR001881; EGF_Ca-bd.
DR   InterPro; IPR013091; EGF_Ca-bd_2.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   Pfam; PF07645; EGF_CA; 5.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00179; EGF_CA; 4.
DR   PROSITE; PS00010; ASX_HYDROXYL; 5.
DR   PROSITE; PS50026; EGF_3; 5.
DR   PROSITE; PS01187; EGF_CA; 4.
PE   2: Evidence at transcript level;
KW   Calcium; EGF-like domain; Repeat.
FT   NON_TER     304    304
SQ   SEQUENCE   304 AA;  33014 MW;  ADF9284D0E647BC7 CRC64;
     MWGFWLLLFW GFSGMYRWGM TTLPTLGQTL GGVNECQDTT TCPAYATCTD TTDSYYCTCK
     RGFLSSNGQT NFQGPGVECQ DEDECVTRDV CPEHATCHNT LGSYYCTCNS GLESSGGGPM
     FQGLDESCED VDECSRNSTL CGPTFICINT LGSYSCSCPA GFSLPTFQIL GHPADGNCTD
     IDECDDTCPL NSSCTNTIGS YFCTCHPGFA SSNGQLNFKD LEVTCEDIDE CTQDPLQCGL
     NSVCTNVPGS YICGCLPDFQ MDPEGSQGYG NFNCKRILFK CKEDLILQSE QIQQCQAVQG
     RDLG
//
ID   UNC5C_MOUSE             Reviewed;         931 AA.
AC   O08747; Q8CD16;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Netrin receptor UNC5C;
DE   AltName: Full=Protein unc-5 homolog 3;
DE   AltName: Full=Protein unc-5 homolog C;
DE   AltName: Full=Rostral cerebellar malformation protein;
DE   Flags: Precursor;
GN   Name=Unc5c; Synonyms=Rcm, Unc5h3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DISEASE, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=C57B6/SJL;
RX   MEDLINE=97271898; PubMed=9126743; DOI=10.1038/386838a0;
RA   Ackerman S.L., Kozak L.P., Przyborski S.A., Rund L.A., Boyer B.B.,
RA   Knowles B.B.;
RT   "The mouse rostral cerebellar malformation gene encodes an UNC-5-like
RT   protein.";
RL   Nature 386:838-842(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   MEDLINE=98111186; PubMed=9389662;
RA   Przyborski S.A., Knowles B.B., Ackerman S.L.;
RT   "Embryonic phenotype of Unc5h3 mutant mice suggests chemorepulsion
RT   during the formation of the rostral cerebellar boundary.";
RL   Development 125:41-50(1998).
RN   [4]
RP   INTERACTION WITH DCC.
RX   MEDLINE=99325507; PubMed=10399920; DOI=10.1016/S0092-8674(00)80804-1;
RA   Hong K., Hinck L., Nishiyama M., Poo M.-M., Tessier-Lavigne M.,
RA   Stein E.;
RT   "A ligand-gated association between cytoplasmic domains of UNC5 and
RT   DCC family receptors converts netrin-induced growth cone attraction to
RT   repulsion.";
RL   Cell 97:927-941(1999).
RN   [5]
RP   PHOSPHORYLATION AT TYR-568, AND MUTAGENESIS OF TYR-568.
RX   MEDLINE=21538865; PubMed=11533026; DOI=10.1074/jbc.M103872200;
RA   Tong J., Killeen M., Steven R., Binns K.L., Culotti J., Pawson T.;
RT   "Netrin stimulates tyrosine phosphorylation of the UNC-5 family of
RT   netrin receptors and induces Shp2 binding to the RCM cytodomain.";
RL   J. Biol. Chem. 276:40917-40925(2001).
RN   [6]
RP   FUNCTION.
RX   MEDLINE=22338860; PubMed=12451134;
RA   Finger J.H., Bronson R.T., Harris B., Johnson K., Przyborski S.A.,
RA   Ackerman S.L.;
RT   "The netrin 1 receptors Unc5h3 and Dcc are necessary at multiple
RT   choice points for the guidance of corticospinal tract axons.";
RL   J. Neurosci. 22:10346-10356(2002).
CC   -!- FUNCTION: Receptor for netrin required for axon guidance. Mediates
CC       axon repulsion of neuronal growth cones in the developing nervous
CC       system upon ligand binding. Axon repulsion in growth cones may be
CC       caused by its association with DCC that may trigger signaling for
CC       repulsion. Also involved in corticospinal tract axon guidances
CC       independently of DCC. It also acts as a dependence receptor
CC       required for apoptosis induction when not associated with netrin
CC       ligand.
CC   -!- SUBUNIT: Interacts with the cytoplasmic part of DCC.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O08747-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O08747-2; Sequence=VSP_011702;
CC   -!- TISSUE SPECIFICITY: Mainly expressed in regions of differentiating
CC       neurons. Highly expressed in brain and lung. Weakly expressed in
CC       testis, ovary, spleen, thymus and bladder. Expressed at very low
CC       level in kidney, intestine and salivary gland.
CC   -!- PTM: Phosphorylated on different cytoplasmic tyrosine residues.
CC       Phosphorylation of Tyr-568 leads to an interaction with PTPN11
CC       phosphatase, suggesting that its activity is regulated by
CC       phosphorylation/dephosphorylation. Tyrosine phosphorylation is
CC       netrin-dependent.
CC   -!- PTM: Proteolytically cleaved by caspases during apoptosis. The
CC       cleavage does not take place when the receptor is associated with
CC       netrin ligand. Its cleavage by caspases is required to induce
CC       apoptosis (By similarity).
CC   -!- DISEASE: Note=Defects in Unc5c are the cause of rostral cerebellar
CC       malformation (Rcm). Rcm is characterized by cerebellar and
CC       midbrain defects, apparently as a result of abnormal neuronal
CC       migration.
CC   -!- SIMILARITY: Belongs to the unc-5 family.
CC   -!- SIMILARITY: Contains 1 death domain.
CC   -!- SIMILARITY: Contains 1 Ig-like (immunoglobulin-like) domain.
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 2 TSP type-1 domains.
CC   -!- SIMILARITY: Contains 1 ZU5 domain.
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DR   EMBL; U72634; AAB54103.1; -; mRNA.
DR   EMBL; AK031655; BAC27495.1; -; mRNA.
DR   IPI; IPI00309191; -.
DR   IPI; IPI00471275; -.
DR   RefSeq; NP_033498.1; NM_009472.3.
DR   UniGene; Mm.24430; -.
DR   ProteinModelPortal; O08747; -.
DR   SMR; O08747; 60-367, 528-928.
DR   STRING; O08747; -.
DR   PRIDE; O08747; -.
DR   Ensembl; ENSMUST00000075282; ENSMUSP00000074758; ENSMUSG00000059921.
DR   Ensembl; ENSMUST00000106236; ENSMUSP00000101843; ENSMUSG00000059921.
DR   GeneID; 22253; -.
DR   KEGG; mmu:22253; -.
DR   UCSC; uc008roe.1; mouse.
DR   CTD; 22253; -.
DR   MGI; MGI:1095412; Unc5c.
DR   eggNOG; roNOG13266; -.
DR   HOVERGEN; HBG056483; -.
DR   OMA; QKIACTT; -.
DR   OrthoDB; EOG45X7VD; -.
DR   NextBio; 302331; -.
DR   ArrayExpress; O08747; -.
DR   Bgee; O08747; -.
DR   CleanEx; MM_UNC5C; -.
DR   Genevestigator; O08747; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IC:MGI.
DR   GO; GO:0005042; F:netrin receptor activity; IDA:MGI.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0007420; P:brain development; IMP:MGI.
DR   GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
DR   InterPro; IPR000488; Death.
DR   InterPro; IPR011029; DEATH-like.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR000884; Thrombospondin_1_rpt.
DR   InterPro; IPR000906; ZU5.
DR   Gene3D; G3DSA:1.10.533.10; DEATH_like; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00090; TSP_1; 1.
DR   Pfam; PF00791; ZU5; 1.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00209; TSP1; 2.
DR   SMART; SM00218; ZU5; 1.
DR   SUPFAM; SSF47986; DEATH_like; 1.
DR   SUPFAM; SSF82895; TSP1; 2.
DR   PROSITE; PS50017; DEATH_DOMAIN; FALSE_NEG.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS50092; TSP1; 2.
DR   PROSITE; PS51145; ZU5; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Developmental protein;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW   Phosphoprotein; Receptor; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     40       Potential.
FT   CHAIN        41    931       Netrin receptor UNC5C.
FT                                /FTId=PRO_0000036076.
FT   TOPO_DOM     41    380       Extracellular (Potential).
FT   TRANSMEM    381    401       Helical; (Potential).
FT   TOPO_DOM    402    931       Cytoplasmic (Potential).
FT   DOMAIN       62    159       Ig-like.
FT   DOMAIN      161    256       Ig-like C2-type.
FT   DOMAIN      260    314       TSP type-1 1.
FT   DOMAIN      316    368       TSP type-1 2.
FT   DOMAIN      528    634       ZU5.
FT   DOMAIN      850    929       Death.
FT   REGION      694    712       Interaction with DCC (By similarity).
FT   SITE        415    416       Cleavage; by caspase-3 (By similarity).
FT   MOD_RES     568    568       Phosphotyrosine.
FT   CARBOHYD    236    236       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    361    361       N-linked (GlcNAc...) (Potential).
FT   DISULFID     83    142       By similarity.
FT   DISULFID    188    239       By similarity.
FT   DISULFID    272    309       By similarity.
FT   DISULFID    276    313       By similarity.
FT   DISULFID    287    299       By similarity.
FT   VAR_SEQ     370    370       A -> GFIYPISTEHRPQNEYGFSS (in isoform 2).
FT                                /FTId=VSP_011702.
FT   MUTAGEN     568    568       Y->F: Abolishes interaction with PTPN11,
FT                                leading to a increased level of
FT                                phosphorylation.
FT   CONFLICT     16     16       L -> I (in Ref. 2; BAC27495).
FT   CONFLICT    733    733       H -> R (in Ref. 2; BAC27495).
FT   CONFLICT    924    924       S -> Y (in Ref. 2; BAC27495).
SQ   SEQUENCE   931 AA;  103063 MW;  8A5D951A4EECA179 CRC64;
     MRKGLRATAA RCGLGLGYLL QMLVLPALAL LSASGTGSAA QDDEFFHELP ETFPSDPPEP
     LPHFLIEPEE AYIVKNKPVN LYCKASPATQ IYFKCNSEWV HQKDHVVDER VDETSGLIVR
     EVSIEISRQQ VEELFGPEDY WCQCVAWSSA GTTKSRKAYV RIAYLRKTFE QEPLGKEVSL
     EQEVLLQCRP PEGIPVAEVE WLKNEDIIDP AEDRNFYITI DHNLIIKQAR LSDTANYTCV
     AKNIVAKRKS TTATVIVYVN GGWSTWTEWS VCNSRCGRGY QKRTRTCTNP APLNGGAFCE
     GQSVQKIACT TLCPVDGRWT SWSKWSTCGT ECTHWRRREC TAPAPKNGGK DCDGLVLQSK
     NCTDGLCMQA APDSDDVALY VGIVIAVTVC LAITVVVALF VYRKNHRDFE SDIIDSSALN
     GGFQPVNIKA ARQDLLAVPP DLTSAAAMYR GPVYALHDVS DKIPMTNSPI LDPLPNLKIK
     VYNSSGAVTP QDDLAEFSSK LSPQMTQSLL ENEALNLKNQ SLARQTDPSC TAFGTFNSLG
     GHLIIPNSGV SLLIPAGAIP QGRVYEMYVT VHRKENMRPP MEDSQTLLTP VVSCGPPGAL
     LTRPVILTLH HCADPSTEDW KIQLKNQAVQ GQWEDVVVVG EENFTTPCYI QLDAEACHIL
     TENLSTYALV GQSTTKAAAK RLKLAIFGPL CCSSLEYSIR VYCLDDTQDA LKEVLQLERQ
     MGGQLLEEPK ALHFKGSIHN LRLSIHDIAH SLWKSKLLAK YQEIPFYHIW SGSQRNLHCT
     FTLERLSLNT VELVCKLCVR QVEGEGQIFQ LNCTVSEEPT GIDLPLLDPA STITTVTGPS
     AFSIPLPIRQ KLCSSLDAPQ TRGHDWRMLA HKLNLDRYLN YFATKSSPTG VILDLWEAQN
     FPDGNLSMLA AVLEEMGRHE TVVSLAAEGQ Y
//
ID   TCOF_MOUSE              Reviewed;        1320 AA.
AC   O08784; O08857;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Treacle protein;
DE   AltName: Full=Treacher Collins syndrome protein homolog;
GN   Name=Tcof1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=97445113; PubMed=9299440; DOI=10.1006/bbrc.1997.7229;
RA   Paznekas W.A., Zhang N., Gridley T., Jabs E.W.;
RT   "Mouse TCOF1 is expressed widely, has motifs conserved in nucleolar
RT   phosphoproteins, and maps to chromosome 18.";
RL   Biochem. Biophys. Res. Commun. 238:1-6(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX   MEDLINE=97301769; PubMed=9158147; DOI=10.1093/hmg/6.5.727;
RA   Dixon J., Hovanes K., Shiang R., Dixon M.J.;
RT   "Sequence analysis, identification of evolutionary conserved motifs
RT   and expression analysis of murine tcof1 provide further evidence for a
RT   potential function for the gene and its human homologue, TCOF1.";
RL   Hum. Mol. Genet. 6:727-737(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1314.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1191, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-171, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-84; SER-85;
RP   SER-87; SER-88; SER-344; THR-346; SER-347; SER-348; SER-352; SER-354;
RP   SER-413; SER-414; SER-417; SER-419; SER-421; SER-433; SER-485;
RP   SER-487; SER-488; SER-489; SER-494; SER-499; SER-529; SER-531;
RP   SER-532; SER-535; SER-536; SER-538; THR-600; SER-603; SER-607;
RP   SER-608; SER-609; THR-753; SER-757; SER-759; SER-760; SER-761;
RP   SER-765; SER-767; SER-993; SER-994; THR-996; SER-997 AND SER-998, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169 AND THR-171, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-757; SER-759; SER-760;
RP   SER-761; SER-765; SER-767; SER-794; SER-1191 AND SER-1242, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-908 AND SER-1191, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; THR-171; SER-593
RP   AND SER-1216, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: May be involved in nucleolar-cytoplasmic transport. May
CC       play a fundamental role in early embryonic development,
CC       particularly in development of the craniofacial complex.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (Potential).
CC   -!- TISSUE SPECIFICITY: Ubiquitous in adult and embryonic tissues.
CC   -!- DEVELOPMENTAL STAGE: Expression elevated at 11 dpc when the
CC       branchial arches and facial swellings are present.
CC   -!- SIMILARITY: Contains 1 LisH domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF001794; AAB71347.1; -; mRNA.
DR   EMBL; U81030; AAB60933.1; -; mRNA.
DR   EMBL; BC060105; AAH60105.1; -; mRNA.
DR   IPI; IPI00115660; -.
DR   PIR; JC5630; JC5630.
DR   RefSeq; NP_035682.1; NM_011552.3.
DR   UniGene; Mm.2215; -.
DR   STRING; O08784; -.
DR   PhosphoSite; O08784; -.
DR   PRIDE; O08784; -.
DR   Ensembl; ENSMUST00000078036; ENSMUSP00000077183; ENSMUSG00000024613.
DR   GeneID; 21453; -.
DR   KEGG; mmu:21453; -.
DR   UCSC; uc008fbb.1; mouse.
DR   CTD; 21453; -.
DR   MGI; MGI:892003; Tcof1.
DR   eggNOG; roNOG16231; -.
DR   GeneTree; ENSGT00550000074747; -.
DR   HOVERGEN; HBG006664; -.
DR   InParanoid; O08784; -.
DR   OMA; GMASANQ; -.
DR   PhylomeDB; O08784; -.
DR   NextBio; 300816; -.
DR   PMAP-CutDB; O08784; -.
DR   ArrayExpress; O08784; -.
DR   Bgee; O08784; -.
DR   Genevestigator; O08784; -.
DR   GermOnline; ENSMUSG00000024613; Mus musculus.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042790; P:transcription of nuclear rRNA large RNA polymerase I transcript; IMP:MGI.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR006594; LisH_dimerisation.
DR   InterPro; IPR003993; TCS_treacle.
DR   InterPro; IPR017859; Treacle-like_TCS.
DR   Pfam; PF03546; Treacle; 2.
DR   PRINTS; PR01503; TREACLE.
DR   SMART; SM00667; LisH; 1.
DR   PROSITE; PS50896; LISH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Nucleus; Phosphoprotein; Repeat; Transport.
FT   CHAIN         1   1320       Treacle protein.
FT                                /FTId=PRO_0000072460.
FT   DOMAIN        6     38       LisH.
FT   REPEAT      212    295       1.
FT   REPEAT      296    366       2.
FT   REPEAT      367    436       3.
FT   REPEAT      437    505       4.
FT   REPEAT      506    550       5.
FT   REPEAT      551    624       6.
FT   REPEAT      625    680       7.
FT   REPEAT      681    714       8.
FT   REPEAT      715    774       9.
FT   REPEAT      775    839       10.
FT   REGION      212    839       10 X approximate tandem repeats.
FT   COMPBIAS    195    198       Poly-Ser.
FT   COMPBIAS    216    272       Ala-rich.
FT   COMPBIAS    253    272       Poly-Ala.
FT   COMPBIAS    880    885       Poly-Ser.
FT   COMPBIAS   1179   1314       Lys-rich.
FT   COMPBIAS   1200   1205       Poly-Lys.
FT   COMPBIAS   1270   1277       Poly-Lys.
FT   COMPBIAS   1280   1288       Poly-Lys.
FT   COMPBIAS   1307   1314       Poly-Lys.
FT   MOD_RES      83     83       Phosphoserine.
FT   MOD_RES      84     84       Phosphoserine.
FT   MOD_RES      85     85       Phosphoserine.
FT   MOD_RES      87     87       Phosphoserine.
FT   MOD_RES      88     88       Phosphoserine.
FT   MOD_RES     136    136       Phosphoserine (By similarity).
FT   MOD_RES     151    151       Phosphoserine (By similarity).
FT   MOD_RES     153    153       N6-acetyllysine (By similarity).
FT   MOD_RES     154    154       Phosphoserine (By similarity).
FT   MOD_RES     158    158       Phosphoserine (By similarity).
FT   MOD_RES     169    169       Phosphoserine.
FT   MOD_RES     171    171       Phosphothreonine.
FT   MOD_RES     301    301       N6-acetyllysine (By similarity).
FT   MOD_RES     309    309       Phosphoserine (By similarity).
FT   MOD_RES     344    344       Phosphoserine.
FT   MOD_RES     346    346       Phosphothreonine.
FT   MOD_RES     347    347       Phosphoserine.
FT   MOD_RES     348    348       Phosphoserine.
FT   MOD_RES     352    352       Phosphoserine.
FT   MOD_RES     354    354       Phosphoserine.
FT   MOD_RES     380    380       Phosphoserine (By similarity).
FT   MOD_RES     386    386       Phosphoserine (By similarity).
FT   MOD_RES     413    413       Phosphoserine.
FT   MOD_RES     414    414       Phosphoserine.
FT   MOD_RES     417    417       Phosphoserine.
FT   MOD_RES     419    419       Phosphoserine.
FT   MOD_RES     421    421       Phosphoserine.
FT   MOD_RES     433    433       Phosphoserine.
FT   MOD_RES     443    443       Phosphoserine (By similarity).
FT   MOD_RES     485    485       Phosphoserine.
FT   MOD_RES     487    487       Phosphoserine.
FT   MOD_RES     488    488       Phosphoserine.
FT   MOD_RES     489    489       Phosphoserine.
FT   MOD_RES     494    494       Phosphoserine.
FT   MOD_RES     499    499       Phosphoserine.
FT   MOD_RES     521    521       N6-acetyllysine (By similarity).
FT   MOD_RES     529    529       Phosphoserine.
FT   MOD_RES     531    531       Phosphoserine.
FT   MOD_RES     532    532       Phosphoserine.
FT   MOD_RES     535    535       Phosphoserine.
FT   MOD_RES     536    536       Phosphoserine.
FT   MOD_RES     538    538       Phosphoserine.
FT   MOD_RES     593    593       Phosphoserine.
FT   MOD_RES     600    600       Phosphothreonine.
FT   MOD_RES     603    603       Phosphoserine.
FT   MOD_RES     607    607       Phosphoserine.
FT   MOD_RES     608    608       Phosphoserine.
FT   MOD_RES     609    609       Phosphoserine.
FT   MOD_RES     655    655       N6-acetyllysine (By similarity).
FT   MOD_RES     662    662       Phosphoserine (By similarity).
FT   MOD_RES     664    664       Phosphoserine (By similarity).
FT   MOD_RES     669    669       Phosphoserine (By similarity).
FT   MOD_RES     671    671       Phosphoserine (By similarity).
FT   MOD_RES     753    753       Phosphothreonine.
FT   MOD_RES     757    757       Phosphoserine.
FT   MOD_RES     759    759       Phosphoserine.
FT   MOD_RES     760    760       Phosphoserine.
FT   MOD_RES     761    761       Phosphoserine.
FT   MOD_RES     765    765       Phosphoserine.
FT   MOD_RES     767    767       Phosphoserine.
FT   MOD_RES     794    794       Phosphoserine.
FT   MOD_RES     822    822       Phosphoserine (By similarity).
FT   MOD_RES     824    824       Phosphoserine (By similarity).
FT   MOD_RES     825    825       Phosphoserine (By similarity).
FT   MOD_RES     826    826       Phosphoserine (By similarity).
FT   MOD_RES     829    829       Phosphoserine (By similarity).
FT   MOD_RES     831    831       Phosphoserine (By similarity).
FT   MOD_RES     853    853       Phosphoserine (By similarity).
FT   MOD_RES     869    869       Phosphothreonine (By similarity).
FT   MOD_RES     882    882       Phosphoserine (By similarity).
FT   MOD_RES     883    883       Phosphoserine (By similarity).
FT   MOD_RES     885    885       Phosphoserine (By similarity).
FT   MOD_RES     908    908       Phosphothreonine.
FT   MOD_RES     993    993       Phosphoserine.
FT   MOD_RES     994    994       Phosphoserine.
FT   MOD_RES     996    996       Phosphothreonine.
FT   MOD_RES     997    997       Phosphoserine.
FT   MOD_RES     998    998       Phosphoserine.
FT   MOD_RES    1034   1034       Phosphoserine (By similarity).
FT   MOD_RES    1035   1035       Phosphoserine (By similarity).
FT   MOD_RES    1066   1066       Phosphothreonine (By similarity).
FT   MOD_RES    1071   1071       Phosphoserine (By similarity).
FT   MOD_RES    1191   1191       Phosphoserine.
FT   MOD_RES    1216   1216       Phosphoserine.
FT   MOD_RES    1242   1242       Phosphoserine.
FT   MOD_RES    1249   1249       N6-acetyllysine (By similarity).
FT   MOD_RES    1303   1303       Phosphoserine (By similarity).
FT   CONFLICT     35     35       G -> A (in Ref. 2; AAB60933).
FT   CONFLICT    125    142       Missing (in Ref. 2; AAB60933).
SQ   SEQUENCE   1320 AA;  135001 MW;  34D87F5F5D300758 CRC64;
     MAEARKRREL LPLIYHHLLQ AGYVRAAREV KEQSGQKSFL TQPVTLLDIY THWQQTSELG
     QKQKAEDDET LQAKKSRVSD PVSSSESSDQ EKEEEAATER AKATPRPTPV NSATAALPSK
     VKEKGKTKTA NKTVNSVSHP GSGKTVVHLL SGKSPKKSAE PLANTVLASE TEEEGNAQAL
     GPTAKSGTVS AGQGSSSSED SSISSDETDV EVKSPAKPAQ AKASAAPAKD PPARTAPGPT
     KLGNVAPTPA KPARAAAAAA AAAVAAAAAA AAEESESSEE DSDSEDEAPA GLPSQVKASG
     KGPHVRADSV SAKGISGKGP ILATPGKTGP AATQAKAERP EKDSETSSED DSDSEDEMPV
     TVNTPQARTS GKSPRARGTS APAKESSQKG APAVTPGKAR PVAAQAGKPE AKSSEESESD
     SGETPAAATL TTSPAKVKPL GKSSQVRPVS TVTPGSSGKG ANLPCPGKVG SAALRVQMVK
     KEDVSESSSA ELDSDGPGSP AKAKASLALP QKVRPVATQV KTDRGKGHSG SSEESSDSEE
     EAAPAASAAQ AKPALEKQMK ASSRKGTPAS ATGASTSSHC KAGAVTSSAS LSSPALAKGT
     QRSDVDSSSE SESEGAAPST PRVQGKSGGK GLQGKAALGQ GVAPVHTQKT GPSVKAMAQE
     DSESLEEDSS SEEEDETPAQ ATPLGRLPQA KANPPPTKTP PASASGKAVA APTKGKPPVP
     NSTVSARGQR SVPAAGKAGA PATQAQKGPV AGTGEDSESS SKEESDSEEE TPAQIKPVGK
     TSQVRAASAP AKESPKKGAH PGTPGKTGSS ATQAQPGKTE DSDSSSEESD SDTEMPSAQA
     IKSPPVSVNR NSSPAVPAPT PEGVQAVNTT KKASGTTAQS SSSESEDGDE DLIPATQPST
     YALRTSVTTP AALSRAASQP SKSEQSSRMP KGKKAKAAAS AQTSSAVETL PMMPPQSAPI
     QPKATNKLGK SKLPEKQQLA PGYPKAPRSS EDSSDTSSED EEDAKRPQMP KSAHRLDPDP
     SQKETVVEET PTESSEDEMV APSQSLLSGY MTPGLTVANS QASKATPRPD SNSLASSAPA
     TKDNPDGKQK SKSQHAADTA LPKTGRKEAS SGSTPQKPKK LKKSTSSSPA PTQTLPNSIT
     QRLLEQAWPL SEAQVQASVV KVLTELLEQE RLKATEAIKE SGKKSQKRKL SGDLEAGAPK
     NKKKKEQPVP RASAVSPEKA PMTSKAKSKL DKGSAGGKGK GSPGPQGAKE KPDGELLGIK
     LESGEQSDPK SKSKKKKSLK KKKDKEKKEK KKGKKSLAKD SASPIQKKKK KKKKSAEPAV
//
ID   CLOCK_MOUSE             Reviewed;         855 AA.
AC   O08785;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   08-MAR-2011, entry version 111.
DE   RecName: Full=Circadian locomoter output cycles protein kaput;
DE            Short=mCLOCK;
DE            EC=2.3.1.48;
GN   Name=Clock;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC   STRAIN=129;
RX   MEDLINE=97304393; PubMed=9160756; DOI=10.1016/S0092-8674(00)80246-9;
RA   Antoch M.P., Song E.J., Chang A.M., Vitaterna M.H., Zhao Y.,
RA   Wilsbacher L.D., Sangoram A.M., King D.P., Pinto L.H., Takahashi J.S.;
RT   "Functional identification of the mouse circadian clock gene by
RT   transgenic BAC rescue.";
RL   Cell 89:655-667(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS LONG AND SHORT),
RP   TISSUE SPECIFICITY, AND IDENTIFICATION OF CLOCK VARIANT.
RC   STRAIN=C57BL/6 X BALB/c; TISSUE=Suprachiasmatic nucleus;
RX   MEDLINE=97304392; PubMed=9160755; DOI=10.1016/S0092-8674(00)80245-7;
RA   King D.P., Zhao Y., Sangoram A.M., Wilsbacher L.D., Tanaka M.,
RA   Antoch M.P., Steeves T.D.L., Vitaterna M.H., Kornhauser J.M.,
RA   Lowrey P.L., Turek F.W., Takahashi J.S.;
RT   "Positional cloning of the mouse circadian clock gene.";
RL   Cell 89:641-653(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=20568483; PubMed=11116088; DOI=10.1101/gr.10.12.1928;
RA   Wilsbacher L.D., Sangoram A.M., Antoch M.P., Takahashi J.S.;
RT   "The mouse Clock locus: sequence and comparative analysis of 204 kb
RT   from mouse chromosome 5.";
RL   Genome Res. 10:1928-1940(2000).
RN   [4]
RP   INTERACTION WITH ARNTL.
RX   MEDLINE=98279137; PubMed=9616112; DOI=10.1126/science.280.5369.1564;
RA   Gekakis N., Staknis D., Nguyen H.B., Davis F.C., Wilsbacher L.D.,
RA   King D.P., Takahashi J.S., Weitz C.J.;
RT   "Role of the CLOCK protein in the mammalian circadian mechanism.";
RL   Science 280:1564-1569(1998).
RN   [5]
RP   INTERACTION WITH ARNTL; PER1; PER2; CRY1; CRY2 AND CSNK1E,
RP   PHOSPHORYLATION, SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=11779462; DOI=10.1016/S0092-8674(01)00610-9;
RA   Lee C., Etchegaray J.-P., Cagampang F.R.A., Loudon A.S.I.,
RA   Reppert S.M.;
RT   "Posttranslational mechanisms regulate the mammalian circadian
RT   clock.";
RL   Cell 107:855-867(2001).
RN   [6]
RP   INTERACTION WITH ARNTL, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND
RP   INDUCTION.
RX   PubMed=12897057; DOI=10.1101/gad.1099503;
RA   Kondratov R.V., Chernov M.V., Kondratova A.A., Gorbacheva V.Y.,
RA   Gudkov A.V., Antoch M.P.;
RT   "BMAL1-dependent circadian oscillation of nuclear CLOCK:
RT   posttranslational events induced by dimerization of transcriptional
RT   activators of the mammalian clock system.";
RL   Genes Dev. 17:1921-1932(2003).
RN   [7]
RP   HISTONE ACETYLTRANSFERASE ACTIVITY, AND MUTAGENESIS OF PRO-656;
RP   TYR-658; ASN-659; GLY-669; SER-670 AND VAL-672.
RX   PubMed=16678094; DOI=10.1016/j.cell.2006.03.033;
RA   Doi M., Hirayama J., Sassone-Corsi P.;
RT   "Circadian regulator CLOCK is a histone acetyltransferase.";
RL   Cell 125:497-508(2006).
RN   [8]
RP   FUNCTION IN ACETYLATION OF ARNTL.
RX   PubMed=18075593; DOI=10.1038/nature06394;
RA   Hirayama J., Sahar S., Grimaldi B., Tamaru T., Takamatsu K.,
RA   Nakahata Y., Sassone-Corsi P.;
RT   "CLOCK-mediated acetylation of BMAL1 controls circadian function.";
RL   Nature 450:1086-1090(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: ARNTL/2-CLOCK heterodimers activate E-box element (3'-
CC       CACGTG-5') transcription of a number of proteins of the circadian
CC       clock. Activates transcription of PER1 and PER2. This
CC       transcription is inhibited in a feedback loop by PER and CRY
CC       proteins. Has intrinsic histone acetyltransferase activity and
CC       this enzymatic function contributes to chromatin-remodeling events
CC       implicated in circadian control of gene expression. Acetylates
CC       primarily histones H3 and H4. Acetylates also a non-histone
CC       substrate: its own partner, ARNTL.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + [histone] = CoA + acetyl-
CC       [histone].
CC   -!- SUBUNIT: Component of the circadian clock oscillator which
CC       includes the CRY proteins, CLOCK or NPAS2, ARNTL or ARNTL2, CSNK1D
CC       and/or CSNK1E, TIMELESS and the PER proteins. Efficient DNA
CC       binding requires dimerization with another bHLH protein.
CC       Heterodimerization with ARNTL is required for E-box-dependent
CC       transactivation, for CLOCK nuclear translocation and degradation,
CC       and, for phosphorylation of both CLOCK and ARNTL. Interaction with
CC       PER and CRY proteins requires translocation to the nucleus.
CC       Interaction of the CLOCK-ARNTL heterodimer with PER or CRY
CC       inhibits transcription activation. Binds weakly ARNTL and ARNTL2
CC       to form heterodimers which bind poorly to the E-box motif.
CC   -!- INTERACTION:
CC       Q9WTL8:Arntl; NbExp=1; IntAct=EBI-79859, EBI-644534;
CC       O54943:Per2; NbExp=3; IntAct=EBI-79859, EBI-1266779;
CC       Q923E4:Sirt1; NbExp=4; IntAct=EBI-79859, EBI-1802585;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuffling between
CC       the cytoplasm and the nucleus is under circadian regulation and is
CC       ARNTL-dependent. Phosphorylated form located in the nucleus
CC       predominantly between C12 and C21. Nonphosphorylated form found
CC       only in the cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=O08785-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=O08785-2; Sequence=VSP_002103;
CC   -!- TISSUE SPECIFICITY: Expressed equally in brain, eye, testes,
CC       ovaries, liver, heart, lung, kidney. In the brain, expression is
CC       abundant in the suprachiasmatic nuclei (SCN), in the pyriform
CC       cortex, and in the hippocampus. Low expression throughout the rest
CC       of the brain. Expression does not appear to undergo circadian
CC       oscillations.
CC   -!- INDUCTION: In the SCN, nuclear expression is lowest between CT7
CC       and CT13. Cytoplasmic expression is highest at these times. In
CC       liver, peak levels from CT21 to CT3. Expression of both
CC       phosphorylated and unphosphorylated forms of ARNTL with other
CC       circadian clock proteins occurs between CT15 and CT18.
CC   -!- DOMAIN: Contains a Gln-rich C-terminal domain which could
CC       correspond to the transactivation domain.
CC   -!- PTM: Phosphorylation is dependent on CLOCK-ARNTL heterodimer
CC       formation.
CC   -!- POLYMORPHISM: The naturally-occurring CLOCK variant, missing exon
CC       19 (deletion of AA 514-564) due to an A-->T nucleotide
CC       transversion in a splice donor site, forms a heterodimer with DNA,
CC       but fails to activate transcription. Homozygous CLOCK mutants have
CC       a circadian rhythm that is increased from 3 to 4 hours and usually
CC       the circadian rhythmicity is lost at constant darkness. Expression
CC       of CLOCK is also reduced. There also exists an alternative spliced
CC       CLOCK variant missing both exon 18 and exon 19 (AA 484-564).
CC   -!- SIMILARITY: Contains 1 basic helix-loop-helix (bHLH) domain.
CC   -!- SIMILARITY: Contains 1 PAC (PAS-associated C-terminal) domain.
CC   -!- SIMILARITY: Contains 2 PAS (PER-ARNT-SIM) domains.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF000998; AAC53200.1; -; mRNA.
DR   EMBL; AF146793; AAD30565.1; -; Genomic_DNA.
DR   IPI; IPI00230536; -.
DR   IPI; IPI00420596; -.
DR   RefSeq; NP_031741.1; NM_007715.5.
DR   UniGene; Mm.3552; -.
DR   UniGene; Mm.392894; -.
DR   ProteinModelPortal; O08785; -.
DR   SMR; O08785; 47-85, 114-171, 272-380.
DR   IntAct; O08785; 38.
DR   MINT; MINT-4654078; -.
DR   STRING; O08785; -.
DR   PhosphoSite; O08785; -.
DR   PRIDE; O08785; -.
DR   Ensembl; ENSMUST00000031148; ENSMUSP00000031148; ENSMUSG00000029238.
DR   Ensembl; ENSMUST00000075159; ENSMUSP00000074656; ENSMUSG00000029238.
DR   Ensembl; ENSMUST00000113497; ENSMUSP00000109125; ENSMUSG00000029238.
DR   Ensembl; ENSMUST00000113499; ENSMUSP00000109127; ENSMUSG00000029238.
DR   GeneID; 12753; -.
DR   KEGG; mmu:12753; -.
DR   UCSC; uc008xuq.1; mouse.
DR   CTD; 12753; -.
DR   MGI; MGI:99698; Clock.
DR   eggNOG; roNOG15370; -.
DR   HOVERGEN; HBG050997; -.
DR   InParanoid; O08785; -.
DR   OrthoDB; EOG476JZV; -.
DR   PhylomeDB; O08785; -.
DR   BRENDA; 2.3.1.48; 244.
DR   Reactome; REACT_24972; Circadian Clock (mouse).
DR   NextBio; 282092; -.
DR   ArrayExpress; O08785; -.
DR   Bgee; O08785; -.
DR   CleanEx; MM_CLOCK; -.
DR   Genevestigator; O08785; -.
DR   GermOnline; ENSMUSG00000029238; Mus musculus.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005667; C:transcription factor complex; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0030528; F:transcription regulator activity; IEA:InterPro.
DR   GO; GO:0007623; P:circadian rhythm; IDA:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   InterPro; IPR011598; HLH_DNA-bd.
DR   InterPro; IPR001092; HLH_DNA-bd_dom.
DR   InterPro; IPR001067; Nuc_translocat.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR013655; PAS_fold_3.
DR   Gene3D; G3DSA:4.10.280.10; HLH_DNA_bd; 1.
DR   Pfam; PF00010; HLH; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   PRINTS; PR00785; NCTRNSLOCATR.
DR   SMART; SM00353; HLH; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF47459; HLH_basic; 1.
DR   PROSITE; PS50888; HLH; 1.
DR   PROSITE; PS50113; PAC; FALSE_NEG.
DR   PROSITE; PS50112; PAS; 2.
PE   1: Evidence at protein level;
KW   Activator; Acyltransferase; Alternative splicing; Biological rhythms;
KW   Cytoplasm; DNA-binding; Nucleus; Phosphoprotein; Repeat;
KW   Transcription; Transcription regulation; Transferase.
FT   CHAIN         1    855       Circadian locomoter output cycles protein
FT                                kaput.
FT                                /FTId=PRO_0000127164.
FT   DOMAIN       48     85       Helix-loop-helix motif.
FT   DOMAIN      107    177       PAS 1.
FT   DOMAIN      262    332       PAS 2.
FT   DOMAIN      336    379       PAC.
FT   DNA_BIND     35     47       Basic motif.
FT   REGION      514    564       Implicated in the circadian rhythmicity.
FT   COMPBIAS    484    855       Gln-rich.
FT   COMPBIAS    740    745       Poly-Gln.
FT   COMPBIAS    751    759       Poly-Gln.
FT   COMPBIAS    762    769       Poly-Gln.
FT   COMPBIAS    828    837       Poly-Gln.
FT   MOD_RES     408    408       Phosphoserine.
FT   VAR_SEQ     484    513       Missing (in isoform Short).
FT                                /FTId=VSP_002103.
FT   MUTAGEN     656    656       P->A: Reduces histone acetyltransferase
FT                                activity; when associated with A-658 and
FT                                A-659.
FT   MUTAGEN     658    658       Y->A: Reduces histone acetyltransferase
FT                                activity; when associated with A-656 and
FT                                A-659.
FT   MUTAGEN     659    659       N->A: Reduces histone acetyltransferase
FT                                activity; when associated with A-656 and
FT                                A-658.
FT   MUTAGEN     669    669       G->A: Reduces histone acetyltransferase
FT                                activity; when associated with A-670 and
FT                                A-672.
FT   MUTAGEN     670    670       S->A: Reduces histone acetyltransferase
FT                                activity; when associated with A-669 and
FT                                A-672.
FT   MUTAGEN     672    672       V->A: Reduces histone acetyltransferase
FT                                activity; when associated with A-669 and
FT                                A-670.
SQ   SEQUENCE   855 AA;  96393 MW;  9864D947049742F4 CRC64;
     MVFTVSCSKM SSIVDRDDSS IFDGLVEEDD KDKAKRVSRN KSEKKRRDQF NVLIKELGSM
     LPGNARKMDK STVLQKSIDF LRKHKETTAQ SDASEIRQDW KPTFLSNEEF TQLMLEALDG
     FFLAIMTDGS IIYVSESVTS LLEHLPSDLV DQSIFNFIPE GEHSEVYKIL STHLLESDSL
     TPEYLKSKNQ LEFCCHMLRG TIDPKEPSTY EYVRFIGNFK SLTSVSTSTH NGFEGTIQRT
     HRPSYEDRVC FVATVRLATP QFIKEMCTVE EPNEEFTSRH SLEWKFLFLD HRAPPIIGYL
     PFEVLGTSGY DYYHVDDLEN LAKCHEHLMQ YGKGKSCYYR FLTKGQQWIW LQTHYYITYH
     QWNSRPEFIV CTHTVVSYAE VRAERRRELG IEESLPETAA DKSQDSGSDN RINTVSLKEA
     LERFDHSPTP SASSRSSRKS SHTAVSDPSS TPTKIPTDTS TPPRQHLPAH EKMTQRRSSF
     SSQSINSQSV GPSLTQPAMS QAANLPIPQG MSQFQFSAQL GAMQHLKDQL EQRTRMIEAN
     IHRQQEELRK IQEQLQMVHG QGLQMFLQQS NPGLNFGSVQ LSSGNSNIQQ LTPVNMQGQV
     VPANQVQSGH ISTGQHMIQQ QTLQSTSTQQ SQQSVMSGHS QQTSLPSQTP STLTAPLYNT
     MVISQPAAGS MVQIPSSMPQ NSTQSATVTT FTQDRQIRFS QGQQLVTKLV TAPVACGAVM
     VPSTMLMGQV VTAYPTFATQ QQQAQTLSVT QQQQQQQQQP PQQQQQQQQS SQEQQLPSVQ
     QPAQAQLGQP PQQFLQTSRL LHGNPSTQLI LSAAFPLQQS TFPPSHHQQH QPQQQQQLPR
     HRTDSLTDPS KVQPQ
//
ID   DCTN1_MOUSE             Reviewed;        1281 AA.
AC   O08788; Q3TZG7;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Dynactin subunit 1;
DE   AltName: Full=150 kDa dynein-associated polypeptide;
DE   AltName: Full=DAP-150;
DE            Short=DP-150;
DE   AltName: Full=p150-glued;
GN   Name=Dctn1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   MEDLINE=97223454; PubMed=9070275; DOI=10.1006/bbrc.1997.6095;
RA   Jang W., Weber J.S., Tokito M.K., Holzbaur E.L., Meisler M.H.;
RT   "Mouse p150Glued (dynactin 1) cDNA sequence and evaluation as a
RT   candidate for the neuromuscular disease mutation mnd2.";
RL   Biochem. Biophys. Res. Commun. 231:344-347(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   INTERACTION WITH SNX6.
RX   PubMed=19935774; DOI=10.1038/cr.2009.130;
RA   Hong Z., Yang Y., Zhang C., Niu Y., Li K., Zhao X., Liu J.J.;
RT   "The retromer component SNX6 interacts with dynactin p150(Glued) and
RT   mediates endosome-to-TGN transport.";
RL   Cell Res. 19:1334-1349(2009).
CC   -!- FUNCTION: Required for the cytoplasmic dynein-driven retrograde
CC       movement of vesicles and organelles along microtubules. Dynein-
CC       dynactin interaction is a key component of the mechanism of axonal
CC       transport of vesicles and organelles.
CC   -!- SUBUNIT: Large macromolecular complex of at least 10 components;
CC       p150(glued) binds directly to microtubules and to cytoplasmic
CC       dynein. Interacts with the C-terminus of MAPRE1, MAPRE2 and
CC       MAPRE3. Interacts with FBXL5 (By similarity). Interacts with ECM29
CC       (By similarity). Interacts with SNX6.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O08788-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O08788-2; Sequence=VSP_029584;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Ubiquitinated by a SCF complex containing FBXL5, leading to
CC       its degradation by the proteasome (By similarity).
CC   -!- SIMILARITY: Belongs to the dynactin 150 kDa subunit family.
CC   -!- SIMILARITY: Contains 1 CAP-Gly domain.
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DR   EMBL; U60312; AAB57773.1; -; mRNA.
DR   EMBL; AK157867; BAE34241.1; -; mRNA.
DR   IPI; IPI00115663; -.
DR   IPI; IPI00857569; -.
DR   PIR; JC5368; JC5368.
DR   RefSeq; NP_031861.2; NM_007835.2.
DR   UniGene; Mm.6919; -.
DR   ProteinModelPortal; O08788; -.
DR   SMR; O08788; 25-98.
DR   MINT; MINT-1847327; -.
DR   STRING; O08788; -.
DR   PhosphoSite; O08788; -.
DR   PRIDE; O08788; -.
DR   Ensembl; ENSMUST00000113919; ENSMUSP00000109552; ENSMUSG00000031865.
DR   GeneID; 13191; -.
DR   KEGG; mmu:13191; -.
DR   CTD; 13191; -.
DR   MGI; MGI:107745; Dctn1.
DR   eggNOG; roNOG12991; -.
DR   HOGENOM; HBG356030; -.
DR   HOVERGEN; HBG004956; -.
DR   InParanoid; O08788; -.
DR   ArrayExpress; O08788; -.
DR   Bgee; O08788; -.
DR   CleanEx; MM_DCTN1; -.
DR   Genevestigator; O08788; -.
DR   GermOnline; ENSMUSG00000031865; Mus musculus.
DR   GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:motor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR023092; CAP-Gly_CS.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   InterPro; IPR022157; Dynactin.
DR   Gene3D; G3DSA:2.30.30.190; CAP-Gly_domain; 1.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   Pfam; PF12455; Dynactin; 1.
DR   SUPFAM; SSF74924; CAP-Gly_domain; 1.
DR   PROSITE; PS00845; CAP_GLY_1; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Dynein; Microtubule; Phosphoprotein; Ubl conjugation.
FT   CHAIN         1   1281       Dynactin subunit 1.
FT                                /FTId=PRO_0000083519.
FT   DOMAIN       48     90       CAP-Gly.
FT   COILED      214    547       Potential.
FT   COILED      943   1049       Potential.
FT   COILED     1185   1214       Potential.
FT   COMPBIAS    157    184       Ser-rich.
FT   MOD_RES     105    105       Phosphoserine (By similarity).
FT   MOD_RES     108    108       Phosphothreonine (By similarity).
FT   MOD_RES     230    230       N6-acetyllysine (By similarity).
FT   MOD_RES     541    541       Phosphoserine.
FT   VAR_SEQ    1049   1086       Missing (in isoform 2).
FT                                /FTId=VSP_029584.
FT   CONFLICT    406    406       W -> R (in Ref. 1; AAB57773).
FT   CONFLICT    721    723       TKA -> NKG (in Ref. 1; AAB57773).
FT   CONFLICT    732    732       S -> R (in Ref. 1; AAB57773).
FT   CONFLICT   1202   1202       V -> I (in Ref. 1; AAB57773).
SQ   SEQUENCE   1281 AA;  141692 MW;  7DE78A105DE38C4C CRC64;
     MAQSRRHMSS RTPSGSRMST EASARPLRVG SRVEVIGKGH RGTVAYVGAT LFATGKWVGV
     ILDEAKGKND GTVQGRKYFT CDEGHGIFVR QSQIQVFEDG ADTTSPETPD SSASKVLKRE
     GADAAAKTSK LRGLKPKKAP TARKTTTRRP KPTRPASTGV AGPSSSLGPS GSASAGELSS
     SEPSTPAQTP LAAPIIPTPA LTSPGAAPPL PSPSKEEEGL RAQVRDLEEK LETLRLKRSE
     DKAKLKELEK HKIQLEQVQE WKSKMQEQQA DLQRRLKEAR KEAKEALEAK ERYMEEMADT
     ADAIEMATLD KEMAEERAES LQQEVEALKE RVDELTTDLE ILKAEIEEKG SDGAASSYQL
     KQLEEQNARL KDALVRMRDL SSSEKQEHVK LQKLMEKKNQ ELEVVWQQRE RLQEELSQAE
     STIDELKEQV DAALGAEEMV EMLTDRNLNL EEKVRELRET VGDLEAMNEM NDELQENARE
     TELELREQLD MAGARVREAQ KRVEAAQETV ADYQQTIKKY RQLTAHLQDV NRELTNQQEA
     SVERQQQPPP ETFDFKIKFA ETKAHAKAIE MELRQMEVAQ ANRHMSLLTA FMPDSFLRPG
     GDHDCVLVLL LMPRLICKAE LIRKQAQEKF DLSENCSERP GLRGAAGEQL SFAAGLVYSL
     SLLQATLHRY EHALSQCSVD VYKKVGSLYP EMSAHERSLD FLIELLHKDQ LDETVNVEPL
     TKAIKYYQHL YSIHLAEQPE DSTMQLADHI KFTQSALDCM GVEVGRLRAF LQGGQEATDI
     ALLLRDLETS CSDTRQFCKK IRRRMPGTDA PGIPAALAFG SQVSDTLLDC RKHLTWVVAV
     LQEVAAAAAQ LIAPLAENEG LPVAALEELA FKASEQIYGS PSSSPYECLR QSCTILISTM
     NKLATAMQEG EYDAERPPSK PPPVELRAAA LRAEITDAEG LGLKLEDRET VIKELKKSLK
     IKGEELSEAN VRLSLLEKKL DSAAKDADER IEKVQTRLDE TQTLLRKKEK DFEETMDALQ
     ADIDQLEAEK AELKQRLNSQ SKRTIEGLRG PPPSGIATLV SGIAGEEPQR GGAPGQAPGA
     LPGPGLVKDS PLLLQQISAM RLHISQLQHE NSILRGAQMK ASLAALPPLH VAKLSLPPHE
     GPGGNLVAGA LYRKTSQLLE KLNQLSTHTH VVDITRSSPA AKSPSAQLME QVAQLKSLSD
     TVEKLKDEVL KETVTQRPGA TVPTDFATFP SSAFLRAKEE QQDDTVYMGK VTFSCAAGLG
     QRHRLVLTQE QLHQLHSRLI S
//
ID   DIAP1_MOUSE             Reviewed;        1255 AA.
AC   O08808;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   08-MAR-2011, entry version 104.
DE   RecName: Full=Protein diaphanous homolog 1;
DE   AltName: Full=Diaphanous-related formin-1;
DE            Short=DRF1;
DE   AltName: Full=p140mDIA;
DE            Short=mDIA1;
GN   Name=Diaph1; Synonyms=Diap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RHOA, AND
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=97357293; PubMed=9214622; DOI=10.1093/emboj/16.11.3044;
RA   Watanabe N., Madaule P., Reid T., Ishizaki T., Watanabe G.,
RA   Kakizuka A., Saito Y., Nakao K., Jockusch B.M., Narumiya S.;
RT   "p140mDia, a mammalian homolog of Drosophila diaphanous, is a target
RT   protein for Rho small GTPase and is a ligand for profilin.";
RL   EMBO J. 16:3044-3056(1997).
RN   [2]
RP   INTERACTION WITH BAIAP2.
RX   PubMed=10814512; DOI=10.1006/bbrc.2000.2671;
RA   Fujiwara T., Mammoto A., Kim Y., Takai Y.;
RT   "Rho small G-protein-dependent binding of mDia to an Src homology 3
RT   domain-containing IRSp53/BAIAP2.";
RL   Biochem. Biophys. Res. Commun. 271:626-629(2000).
RN   [3]
RP   FUNCTION.
RX   MEDLINE=20142655; PubMed=10678165; DOI=10.1016/S1097-2765(00)80399-8;
RA   Tominaga T., Sahai E., Chardin P., McCormick F., Courtneidge S.A.,
RA   Alberts A.S.;
RT   "Diaphanous-related formins bridge Rho GTPase and Src tyrosine kinase
RT   signaling.";
RL   Mol. Cell 5:13-25(2000).
RN   [4]
RP   INTERACTION WITH APC AND MAPRE1.
RX   PubMed=15311282; DOI=10.1038/ncb1160;
RA   Wen Y., Eng C.H., Schmoranzer J., Cabrera-Poch N., Morris E.J.S.,
RA   Chen M., Wallar B.J., Alberts A.S., Gundersen G.G.;
RT   "EB1 and APC bind to mDia to stabilize microtubules downstream of Rho
RT   and promote cell migration.";
RL   Nat. Cell Biol. 6:820-830(2004).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH ACTIN.
RX   PubMed=15044801; DOI=10.1126/science.1093923;
RA   Higashida C., Miyoshi T., Fujita A., Oceguera-Yanez F., Monypenny J.,
RA   Andou Y., Narumiya S., Watanabe N.;
RT   "Actin polymerization-driven molecular movement of mDia1 in living
RT   cells.";
RL   Science 303:2007-2010(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1104, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH NCDN.
RX   PubMed=18572016; DOI=10.1016/j.bbrc.2008.06.042;
RA   Schwaibold E.M., Brandt D.T.;
RT   "Identification of Neurochondrin as a new interaction partner of the
RT   FH3 domain of the Diaphanous-related formin Dia1.";
RL   Biochem. Biophys. Res. Commun. 373:366-372(2008).
RN   [8]
RP   INTERACTION WITH SCAI.
RX   PubMed=19350017; DOI=10.1038/ncb1862;
RA   Brandt D.T., Baarlink C., Kitzing T.M., Kremmer E., Ivaska J.,
RA   Nollau P., Grosse R.;
RT   "SCAI acts as a suppressor of cancer cell invasion through the
RT   transcriptional control of beta1-integrin.";
RL   Nat. Cell Biol. 11:557-568(2009).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 826-1163, OLIGOMERIZATION,
RP   AND INTERACTION WITH ACTIN.
RX   PubMed=14992721; DOI=10.1016/S1097-2765(04)00059-0;
RA   Shimada A., Nyitrai M., Vetter I.R., Kuehlmann D., Bugyi B.,
RA   Narumiya S., Geeves M.A., Wittinghofer A.;
RT   "The core FH2 domain of diaphanous-related formins is an elongated
RT   actin binding protein that inhibits polymerization.";
RL   Mol. Cell 13:511-522(2004).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 69-451 IN COMPLEX WITH RHOC,
RP   AND HOMODIMERIZATION.
RX   PubMed=15864301; DOI=10.1038/nature03604;
RA   Rose R., Weyand M., Lammers M., Ishizaki T., Ahmadian M.R.,
RA   Wittinghofer A.;
RT   "Structural and mechanistic insights into the interaction between Rho
RT   and mammalian Dia.";
RL   Nature 435:513-518(2005).
CC   -!- FUNCTION: Acts in a Rho-dependent manner to recruit PFY1 to the
CC       membrane. Required for the assembly of F-actin structures, such as
CC       actin cables and stress fibers. Nucleates actin filaments. Binds
CC       to the barbed end of the actin filament and slows down actin
CC       polymerization and depolymerization. Required for cytokinesis, and
CC       transcriptional activation of the serum response factor. DFR
CC       proteins couple Rho and Src tyrosine kinase during signaling and
CC       the regulation of actin dynamics. Functions as a scaffold protein
CC       for MAPRE1 and APC to stabilize microtubules and promote cell
CC       migration. Has neurite outgrowth promoting activity.
CC   -!- SUBUNIT: Homodimer. Interacts with the GTP-bound form of RHOA.
CC       Interacts with RHOC, PFY1, MAPRE1, BAIAP2 and APC. Interacts with
CC       SCAI. Interacts with DCAF7 (By similarity). Interacts with NCDN.
CC   -!- SUBCELLULAR LOCATION: Cell membrane. Cell projection, ruffle
CC       membrane. Cytoplasm, cytoskeleton. Note=Membrane ruffles,
CC       especially at the tip of ruffles, of motile cells.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- DOMAIN: DRFs are regulated by intramolecular GBD-DAD binding where
CC       Rho-GTP activates the DRFs by disrupting the GBD-DAD interaction.
CC       DCAF7 binds to the FH2 (formin homology 2) domain.
CC   -!- SIMILARITY: Belongs to the formin homology family. Diaphanous
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 DAD (diaphanous autoregulatory) domain.
CC   -!- SIMILARITY: Contains 1 FH1 (formin homology 1) domain.
CC   -!- SIMILARITY: Contains 1 FH2 (formin homology 2) domain.
CC   -!- SIMILARITY: Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology
CC       3) domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; U96963; AAC53280.1; -; mRNA.
DR   IPI; IPI00808370; -.
DR   PIR; T31065; T31065.
DR   RefSeq; NP_031884.1; NM_007858.2.
DR   UniGene; Mm.195916; -.
DR   PDB; 1V9D; X-ray; 2.60 A; A/B/C/D=826-1163.
DR   PDB; 1Z2C; X-ray; 3.00 A; B/D=69-451.
DR   PDB; 2BAP; X-ray; 3.30 A; A/B=135-451, C/D=1145-1200.
DR   PDB; 2BNX; X-ray; 2.40 A; A/B=131-516.
DR   PDB; 2F31; X-ray; 2.10 A; A=135-367, B=1177-1196.
DR   PDB; 2V8F; X-ray; 1.10 A; C=635-655.
DR   PDB; 3EG5; X-ray; 2.70 A; B/D=69-451.
DR   PDB; 3O4X; X-ray; 3.20 A; A/B/C/D=131-458, E/F/G/H=736-1200.
DR   PDB; 3OBV; X-ray; 2.75 A; A/B/C/D=131-457, E/F/G/H=753-1209.
DR   PDBsum; 1V9D; -.
DR   PDBsum; 1Z2C; -.
DR   PDBsum; 2BAP; -.
DR   PDBsum; 2BNX; -.
DR   PDBsum; 2F31; -.
DR   PDBsum; 2V8F; -.
DR   PDBsum; 3EG5; -.
DR   PDBsum; 3O4X; -.
DR   PDBsum; 3OBV; -.
DR   ProteinModelPortal; O08808; -.
DR   SMR; O08808; 83-457, 745-1198.
DR   DIP; DIP-29028N; -.
DR   STRING; O08808; -.
DR   PhosphoSite; O08808; -.
DR   PRIDE; O08808; -.
DR   Ensembl; ENSMUST00000115634; ENSMUSP00000111297; ENSMUSG00000024456.
DR   GeneID; 13367; -.
DR   KEGG; mmu:13367; -.
DR   CTD; 13367; -.
DR   MGI; MGI:1194490; Diap1.
DR   eggNOG; maNOG12511; -.
DR   HOVERGEN; HBG051357; -.
DR   OrthoDB; EOG4VQ9NP; -.
DR   NextBio; 283706; -.
DR   ArrayExpress; O08808; -.
DR   Bgee; O08808; -.
DR   CleanEx; MM_DIAP1; -.
DR   Genevestigator; O08808; -.
DR   GermOnline; ENSMUSG00000024456; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IDA:MGI.
DR   GO; GO:0030041; P:actin filament polymerization; IDA:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
DR   InterPro; IPR003104; Actin-bd_FH2/DRF_autoreg.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR014767; Diaphanous_autoregulatory.
DR   InterPro; IPR010465; Drf_DAD.
DR   InterPro; IPR010472; Drf_FH3.
DR   InterPro; IPR010473; Drf_GTPase-bd.
DR   InterPro; IPR015425; FH2_actin-bd.
DR   InterPro; IPR009408; Formin_homology_1.
DR   InterPro; IPR014768; GTPase-bd/formin_homology_3.
DR   Pfam; PF06345; Drf_DAD; 1.
DR   Pfam; PF06346; Drf_FH1; 1.
DR   Pfam; PF06367; Drf_FH3; 1.
DR   Pfam; PF06371; Drf_GBD; 1.
DR   Pfam; PF02181; FH2; 1.
DR   SMART; SM00498; FH2; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF101447; FH2_actin_bd; 1.
DR   PROSITE; PS51231; DAD; 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Actin-binding; Cell membrane;
KW   Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Hearing;
KW   Isopeptide bond; Membrane; Phosphoprotein; Repeat; Ubl conjugation.
FT   CHAIN         1   1255       Protein diaphanous homolog 1.
FT                                /FTId=PRO_0000194894.
FT   DOMAIN       75    440       GBD/FH3.
FT   DOMAIN      586    747       FH1.
FT   DOMAIN      752   1154       FH2.
FT   DOMAIN     1177   1205       DAD.
FT   COILED      460    562       Potential.
FT   COILED     1027   1179       Potential.
FT   COMPBIAS   1196   1199       Arg/Lys-rich (basic).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      22     22       Phosphoserine (By similarity).
FT   MOD_RES    1040   1040       N6-acetyllysine (By similarity).
FT   MOD_RES    1086   1086       N6-acetyllysine (By similarity).
FT   MOD_RES    1104   1104       Phosphotyrosine.
FT   CROSSLNK    477    477       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   HELIX        84     92
FT   TURN         93     95
FT   HELIX        98    105
FT   HELIX       109    121
FT   HELIX       136    143
FT   HELIX       149    165
FT   HELIX       168    190
FT   TURN        194    196
FT   HELIX       201    215
FT   HELIX       219    227
FT   STRAND      228    230
FT   HELIX       231    237
FT   HELIX       244    258
FT   HELIX       266    281
FT   HELIX       287    292
FT   HELIX       299    313
FT   HELIX       319    331
FT   HELIX       334    341
FT   HELIX       347    377
FT   HELIX       381    392
FT   HELIX       397    408
FT   TURN        415    417
FT   HELIX       418    433
FT   HELIX       436    438
FT   TURN        453    455
FT   HELIX       464    469
FT   TURN        470    472
FT   STRAND      833    835
FT   HELIX       837    850
FT   HELIX       854    863
FT   TURN        866    868
FT   HELIX       871    880
FT   HELIX       884    891
FT   HELIX       894    899
FT   HELIX       902    911
FT   HELIX       916    934
FT   HELIX       937    951
FT   HELIX       954    958
FT   HELIX       987    992
FT   HELIX      1002   1012
FT   HELIX      1020   1023
FT   HELIX      1027   1032
FT   HELIX      1035   1057
FT   STRAND     1063   1066
FT   HELIX      1069   1104
FT   TURN       1109   1111
FT   HELIX      1114   1159
FT   HELIX      1184   1190
SQ   SEQUENCE   1255 AA;  139343 MW;  09404164873CA7C1 CRC64;
     MEPSGGGLGP GRGTRDKKKG RSPDELPATG GDGGKHKKFL ERFTSMRIKK EKEKPNSAHR
     NSSASYGDDP TAQSLQDISD EQVLVLFEQM LVDMNLNEEK QQPLREKDIV IKREMVSQYL
     HTSKAGMNQK ESSRSAMMYI QELRSGLRDM HLLSCLESLR VSLNNNPVSW VQTFGAEGLA
     SLLDILKRLH DEKEETSGNY DSRNQHEIIR CLKAFMNNKF GIKTMLETEE GILLLVRAMD
     PAVPNMMIDA AKLLSALCIL PQPEDMNERV LEAMTERAEM DEVERFQPLL DGLKSGTSIA
     LKVGCLQLIN ALITPAEELD FRVHIRSELM RLGLHQVLQE LREIENEDMK VQLCVFDEQG
     DEDFFDLKGR LDDIRMEMDD FGEVFQIILN TVKDSKAEPH FLSILQHLLL VRNDYEARPQ
     YYKLIEECVS QIVLHKNGTD PDFKCRHLQI DIERLVDQMI DKTKVEKSEA KATELEKKLD
     SELTARHELQ VEMKKMENDF EQKLQDLQGE KDALDSEKQQ ITAQKQDLEA EVSKLTGEVA
     KLSKELEDAK NEMASLSAVV VAPSVSSSAA VPPAPPLPGD SGTVIPPPPP PPPLPGGVVP
     PSPPLPPGTC IPPPPPLPGG ACIPPPPQLP GSAAIPPPPP LPGVASIPPP PPLPGATAIP
     PPPPLPGATA IPPPPPLPGG TGIPPPPPPL PGSVGVPPPP PLPGGPGLPP PPPPFPGAPG
     IPPPPPGMGV PPPPPFGFGV PAAPVLPFGL TPKKVYKPEV QLRRPNWSKF VAEDLSQDCF
     WTKVKEDRFE NNELFAKLTL AFSAQTKTSK AKKDQEGGEE KKSVQKKKVK ELKVLDSKTA
     QNLSIFLGSF RMPYQEIKNV ILEVNEAVLT ESMIQNLIKQ MPEPEQLKML SELKEEYDDL
     AESEQFGVVM GTVPRLRPRL NAILFKLQFS EQVENIKPEI VSVTAACEEL RKSENFSSLL
     ELTLLVGNYM NAGSRNAGAF GFNISFLCKL RDTKSADQKM TLLHFLAELC ENDHPEVLKF
     PDELAHVEKA SRVSAENLQK SLDQMKKQIA DVERDVQNFP AATDEKDKFV EKMTSFVKDA
     QEQYNKLRMM HSNMETLYKE LGDYFVFDPK KLSVEEFFMD LHNFRNMFLQ AVKENQKRRE
     TEEKMRRAKL AKEKAEKERL EKQQKREQLI DMNAEGDETG VMDSLLEALQ SGAAFRRKRG
     PRQVNRKAGC AVTSLLASEL TKDDAMAPGP VKVPKKSEGV PTILEEAKEL VGRAS
//
ID   U5S1_MOUSE              Reviewed;         971 AA.
AC   O08810;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=116 kDa U5 small nuclear ribonucleoprotein component;
DE   AltName: Full=Elongation factor Tu GTP-binding domain-containing protein 2;
DE   AltName: Full=U5 snRNP-specific protein, 116 kDa;
DE            Short=U5-116 kDa;
GN   Name=Eftud2; Synonyms=Snrp116;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=97377047; PubMed=9233818; DOI=10.1093/emboj/16.13.4092;
RA   Fabrizio P., Laggerbauer B., Lauber J., Lane W.S., Luehrmann R.;
RT   "An evolutionarily conserved U5 snRNP-specific protein is a GTP-
RT   binding factor closely related to the ribosomal translocase EF-2.";
RL   EMBO J. 16:4092-4106(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Component of the U5 snRNP complex required for pre-mRNA
CC       splicing (By similarity).
CC   -!- SUBUNIT: Identified in the spliceosome C complex, at least
CC       composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23,
CC       DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1,
CC       GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK,
CC       HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1,
CC       PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B,
CC       PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2,
CC       SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2,
CC       SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2,
CC       SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8. Binds
CC       GTP. Interacts with PRPF8 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC       EF-G/EF-2 subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH12636.1; Type=Erroneous initiation;
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DR   EMBL; U97079; AAC53299.1; -; mRNA.
DR   EMBL; BC012636; AAH12636.1; ALT_INIT; mRNA.
DR   EMBL; BC054778; AAH54778.1; -; mRNA.
DR   IPI; IPI00469260; -.
DR   RefSeq; NP_001103465.1; NM_001109995.1.
DR   RefSeq; NP_035561.1; NM_011431.3.
DR   UniGene; Mm.873; -.
DR   ProteinModelPortal; O08810; -.
DR   SMR; O08810; 111-954.
DR   STRING; O08810; -.
DR   PhosphoSite; O08810; -.
DR   PRIDE; O08810; -.
DR   Ensembl; ENSMUST00000107060; ENSMUSP00000102675; ENSMUSG00000020929.
DR   GeneID; 20624; -.
DR   KEGG; mmu:20624; -.
DR   UCSC; uc007lsp.1; mouse.
DR   CTD; 20624; -.
DR   MGI; MGI:1336880; Eftud2.
DR   HOVERGEN; HBG001838; -.
DR   OrthoDB; EOG4001HJ; -.
DR   PhylomeDB; O08810; -.
DR   NextBio; 299023; -.
DR   ArrayExpress; O08810; -.
DR   Bgee; O08810; -.
DR   Genevestigator; O08810; -.
DR   GermOnline; ENSMUSG00000020929; Mus musculus.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR009022; Elongation_fac_G/III/V.
DR   InterPro; IPR000795; ProtSyn_GTP-bd.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR000640; Transl_elong_EFG/EF2_C.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR   InterPro; IPR009000; Transl_elong_init/rib_B-barrel.
DR   Gene3D; G3DSA:3.30.230.10; Ribosomal_S5_D2-type_fold; 1.
DR   Gene3D; G3DSA:3.30.70.240; Transl_elong_EFG/EF2_C; 1.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF03764; EFG_IV; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 1.
DR   SUPFAM; SSF54980; EFG_III_V; 2.
DR   SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR   SUPFAM; SSF50447; Translat_factor; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; EFACTOR_GTP; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Acetylation; GTP-binding; mRNA processing; mRNA splicing;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Spliceosome.
FT   CHAIN         1    971       116 kDa U5 small nuclear
FT                                ribonucleoprotein component.
FT                                /FTId=PRO_0000091564.
FT   NP_BIND     135    142       GTP (Potential).
FT   NP_BIND     203    207       GTP (Potential).
FT   NP_BIND     257    260       GTP (Potential).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      19     19       Phosphoserine (By similarity).
FT   MOD_RES      30     30       Phosphothreonine (By similarity).
FT   MOD_RES      85     85       Phosphothreonine (By similarity).
FT   MOD_RES     943    943       Phosphoserine (By similarity).
SQ   SEQUENCE   971 AA;  109361 MW;  0ECF1661DEA3A7FC CRC64;
     MDTDLYDEFG NYIGPELDSD EDDDELGRET KDLDEDEDED EDDVGEHEDD HPGMEVVLHE
     DKKYYPTAEE VYGPEVETIV QEEDTQPLTE PIIKPVKTKK FTLMEQTLPV TVYEMDFLAD
     LMDNSELIRN VTLCGHLHHG KTCFVDCLIE QTHPEIRKRY DQDLCYTDIL FTEQERGVGI
     KSTPVTVVLP DTKGKSYLFN IMDTPGHVNF SDEVTAGLRI SDGVVLFIDA AEGVMLNTER
     LIKHAVQERL AVTVCINKID RLILELKLPP TDAYYKLRHI VDEVNGLISM YSTDENLILS
     PLLGNVCFSS SQYSICFTLG SFAKIYADTF GDINYQEFAK RLWGDIYFNP KTRKFTKKAP
     SSSSQRSFVE FILEPLYKIL AQVVGDVDTS LPRTLDELGI HLTKEELKLN IRPLLRLVCK
     KFFGEFTGFV DMCVQHIPSP KVGAKPKIEH TYTGGVDSDL GEAMSDCDPD GPLMCHTTKM
     YSTDDGVQFH AFGRVLSGTI HAGQPVKVLG ENYTLEDEED SQICTVGRLW ISVARYHIEV
     NRVPAGNWVL IEGVDQPIVK TATITEPRGN EEAQIFRPLK FNTTSVIKIA VEPVNPSELP
     KMLDGLRKVN KSYPSLTTKV EESGEHVILG TGELYLDCVM HDLRKMYSEI DIKVADPVVT
     FCETVVETSS LKCFAETPNK KNKITMIAEP LEKGLAEDIE NEVVQITWNR KKLGEFFQTK
     YDWDLLAARS IWAFGPDATG PNILVDDTLP SEVDKALLGS VKDSIVQGFQ WGTREGPLCD
     ELIRNVKFKI LDAVVAQEPL HRGGGQIIPT ARRVVYSAFL MATPRLMEPY YFVEVQAPAD
     CVSAVYTVLA RRRGHVTQDA PIPGSPLYTI KAFIPAIDSF GFETDLRTHT QGQAFSLSVF
     HHWQIVPGDP LDKSIVIRPL EPQPAPHLAR EFMIKTRRRK GLSEDVSISK FFDDPMLLEL
     AKQDVVLNYP M
//
ID   FLOT1_MOUSE             Reviewed;         428 AA.
AC   O08917;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Flotillin-1;
GN   Name=Flot1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 133-152; 220-240 AND
RP   302-311, AND CHARACTERIZATION.
RC   TISSUE=Adipocyte, and Lung;
RX   MEDLINE=97298087; PubMed=9153235; DOI=10.1074/jbc.272.21.13793;
RA   Bickel P.E., Scherer P.E., Schnitzer J.E., Oh P., Lisanti M.P.,
RA   Lodish H.F.;
RT   "Flotillin and epidermal surface antigen define a new family of
RT   caveolae-associated integral membrane proteins.";
RL   J. Biol. Chem. 272:13793-13802(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
RX   MEDLINE=99230295; PubMed=10212252; DOI=10.1074/jbc.274.18.12702;
RA   Volonte D., Galbiati F., Li S., Nishiyama K., Okamoto T.,
RA   Lisanti M.P.;
RT   "Flotillins/cavatellins are differentially expressed in cells and
RT   tissues and form a hetero-oligomeric complex with caveolins in vivo.
RT   Characterization and epitope-mapping of a novel flotillin-1 monoclonal
RT   antibody probe.";
RL   J. Biol. Chem. 274:12702-12709(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May act as a scaffolding protein within caveolar
CC       membranes, functionally participating in formation of caveolae or
CC       caveolae-like vesicles.
CC   -!- SUBUNIT: Heterooligomeric complex of flotillin-1 and flotillin-2
CC       and caveolin-1 and caveolin-2. Interacts with ECM29 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC       Membrane, caveola; Peripheral membrane protein. Melanosome (By
CC       similarity). Endosome (By similarity). Note=Membrane-associated
CC       protein of caveolae.
CC   -!- TISSUE SPECIFICITY: High expression in brain, white adipose
CC       tissue, heart muscle, skeletal muscle and lung. Low expression in
CC       spleen, liver and testis.
CC   -!- MISCELLANEOUS: Expression increases at least 10-fold as 3T3-L1
CC       cells differentiate into adipocytes.
CC   -!- SIMILARITY: Belongs to the band 7/mec-2 family. Flotillin
CC       subfamily.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; U90435; AAB58583.1; -; mRNA.
DR   EMBL; AF145044; AAD33945.1; -; mRNA.
DR   EMBL; BC004647; AAH04647.1; -; mRNA.
DR   IPI; IPI00117181; -.
DR   RefSeq; NP_032053.1; NM_008027.2.
DR   UniGene; Mm.2931; -.
DR   ProteinModelPortal; O08917; -.
DR   SMR; O08917; 36-173.
DR   MINT; MINT-4095176; -.
DR   STRING; O08917; -.
DR   PhosphoSite; O08917; -.
DR   PRIDE; O08917; -.
DR   Ensembl; ENSMUST00000001569; ENSMUSP00000001569; ENSMUSG00000059714.
DR   GeneID; 14251; -.
DR   KEGG; mmu:14251; -.
DR   UCSC; uc008cip.1; mouse.
DR   CTD; 14251; -.
DR   MGI; MGI:1100500; Flot1.
DR   eggNOG; roNOG06225; -.
DR   HOGENOM; HBG729052; -.
DR   HOVERGEN; HBG051628; -.
DR   InParanoid; O08917; -.
DR   OMA; NMFYTCG; -.
DR   OrthoDB; EOG473PRK; -.
DR   PhylomeDB; O08917; -.
DR   NextBio; 285569; -.
DR   ArrayExpress; O08917; -.
DR   Bgee; O08917; -.
DR   CleanEx; MM_FLOT1; -.
DR   Genevestigator; O08917; -.
DR   GermOnline; ENSMUSG00000059714; Mus musculus.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016600; C:flotillin complex; IDA:BHF-UCL.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:BHF-UCL.
DR   InterPro; IPR001107; Band_7.
DR   Pfam; PF01145; Band_7; 1.
DR   SMART; SM00244; PHB; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Endosome; Membrane;
KW   Phosphoprotein.
FT   CHAIN         1    428       Flotillin-1.
FT                                /FTId=PRO_0000094045.
FT   MOD_RES      19     19       Phosphoserine (By similarity).
FT   MOD_RES     385    385       Phosphoserine (By similarity).
FT   MOD_RES     387    387       Phosphothreonine (By similarity).
SQ   SEQUENCE   428 AA;  47513 MW;  4B17C7EA1263F52C CRC64;
     MFFTCGPNEA MVVSGFCRSP PVMVAGGRVF VLPCIQQIQR ISLNTLTLNV KSEKVYTRHG
     VPISVTGIAQ VKIQGQNKEM LAAACQMFLG KTEAEIAHIA LETLEGHQRA IMAHMTVEEI
     YKDRQKFSEQ VFKVASSDLV NMGISVVSYT LKDIHDDQDY LHSLGKARTA QVQKDARIGE
     AEAKRDAGIR EAKAKQEKVS AQCLSEIEMA KAQRDYELKK ATYDIEVNTR RAQADLAYQL
     QVAKTKQQIE EQRVQVQVVE RAQQVAVQEQ EIARREKELE ARVRKPAEAE RYRLERLAEA
     EKAQLIMQAE AEAESVRMRG EAEAFAIGAR ARAEAEQMAK KAEAFQMYQE AAQLDMLLEK
     LPQVAEEISG PLTSANKITL VSSGSGTMGA AKVTGEVLDI LSRLPESVER LTGVSISQVN
     HNKPLRTA
//
ID   NUMBL_MOUSE             Reviewed;         604 AA.
AC   O08919; Q6NVG8;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 2.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Numb-like protein;
GN   Name=Numbl; Synonyms=Nbl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   MEDLINE=97313232; PubMed=9169836;
RA   Zhong W., Jiang M.-M., Weinmaster G., Jan L.Y., Jan Y.N.;
RT   "Differential expression of mammalian Numb, Numblike and Notch1
RT   suggests distinct roles during mouse cortical neurogenesis.";
RL   Development 124:1887-1897(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX   PubMed=12410312; DOI=10.1038/nature01124;
RA   Petersen P.H., Zou K., Hwang J.K., Jan Y.N., Zhong W.;
RT   "Progenitor cell maintenance requires numb and numblike during mouse
RT   neurogenesis.";
RL   Nature 419:929-934(2002).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX   PubMed=15273690; DOI=10.1038/nn1289;
RA   Petersen P.H., Zou K., Krauss S., Zhong W.;
RT   "Continuing role for mouse Numb and Numbl in maintaining progenitor
RT   cells during cortical neurogenesis.";
RL   Nat. Neurosci. 7:803-811(2004).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17174898; DOI=10.1016/j.cell.2006.10.041;
RA   Kuo C.T., Mirzadeh Z., Soriano-Navarro M., Rasin M., Wang D., Shen J.,
RA   Sestan N., Garcia-Verdugo J., Alvarez-Buylla A., Jan L.Y., Jan Y.N.;
RT   "Postnatal deletion of Numb/Numblike reveals repair and remodeling
RT   capacity in the subventricular neurogenic niche.";
RL   Cell 127:1253-1264(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND THR-279, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Plays a role in the process of neurogenesis. Required
CC       throughout embryonic neurogenesis to maintain neural progenitor
CC       cells, also called radial glial cells (RGCs), by allowing their
CC       daughter cells to choose progenitor over neuronal cell fate. Not
CC       required for the proliferation of neural progenitor cells before
CC       the onset of embryonic neurogenesis. Also required postnatally in
CC       the subventricular zone (SVZ) neurogenesis by regulating SVZ
CC       neuroblasts survival and ependymal wall integrity. Negative
CC       regulator of NF-kappa-B signaling pathway. The inhibition of NF-
CC       kappa-B activation is mediated at least in part, by preventing
CC       MAP3K7IP2 to interact with polyubiquitin chains of TRAF6 and RIPK1
CC       and by stimulating the 'Lys-48'-linked polyubiquitination and
CC       degradation of TRAF6 in cortical neurons.
CC   -!- SUBUNIT: Interacts (via PTB domain) with MAP3K7IP2 (via C-
CC       terminal). Interacts (via C-terminal) with TRAF6 (via TRAF
CC       domains) (By similarity). Associates with EPS15 and NOTCH1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Symmetrically distributed
CC       throughout the cytoplasm in non dividing neuroblasts of the CNS.
CC   -!- TISSUE SPECIFICITY: Preferentially expressed in the nervous
CC       system. In the developing neocortex, expressed in postmitotic
CC       neurons in the cortical plate but not in progenitors within the
CC       ventricular zone.
CC   -!- DEVELOPMENTAL STAGE: Expressed in neural progenitor and neuron
CC       cells throughout the developing nervous system. Expressed in
CC       somites and throughout the neural tube from 8.5 dpc, onward.
CC   -!- DOMAIN: The PTB domain is necessary for the inhibition of
CC       MAP3K7IP2-mediated activation of NF-kappa-B (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Viable, fertile and exhibit no obvious
CC       phenotypes. Mice lacking both Numb and Numbl genes die around 9.5
CC       dpc, with severe defects in somite and vasculature formation,
CC       neuronal tube closure and axial turning. Conditional double-
CC       knockout (cdKO) mutants (Numb and Numbl genes), with expression
CC       abrogated in neural progenitor cells from 8.5 dpc (just before the
CC       onset of neurogenesis), display a loss of neural progenitor cells
CC       formation and an overexpression of neurons as neurogenesis
CC       progresses; cdKO mutants become necrotic at 12.5 dpc and die
CC       around this stage. Conditional double-knockout (cdKO) mutants
CC       (Numb and Numbl genes), with expression abrogated in neural
CC       progenitor cells from 10.5 dpc (just after the onset of
CC       neurogenesis), display a premature depletion of neural progenitor
CC       cells in the dorsal forebrain ventrical zone of the neocortex and
CC       in the hippocampal CA fields as neurogenesis progresses; cdKO
CC       mutants are viable and fertile, but showed a reduction in the
CC       thickness of the neocortex and the hippocampus and an enlargement
CC       of the lateral ventricles. Tamoxifene-inducible double-knockout
CC       (cdKO) mutants (Numb and Numbl genes), with expression abrogated
CC       postnatally in the subventricular zone (SVZ) neuroprogenitors and
CC       in ependymal cells, display a loss of SVZ neuroblasts and show a
CC       disorganized ependyma lacking both interdigitation junction
CC       between neighboring cells and increasing number of separated
CC       cells.
CC   -!- SIMILARITY: Contains 1 PID domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U96441; AAB58697.1; -; mRNA.
DR   EMBL; BC068116; AAH68116.1; -; mRNA.
DR   IPI; IPI00280984; -.
DR   UniGene; Mm.458153; -.
DR   ProteinModelPortal; O08919; -.
DR   SMR; O08919; 60-202.
DR   STRING; O08919; -.
DR   PhosphoSite; O08919; -.
DR   PRIDE; O08919; -.
DR   Ensembl; ENSMUST00000079258; ENSMUSP00000078245; ENSMUSG00000063160.
DR   MGI; MGI:894702; Numbl.
DR   eggNOG; roNOG08433; -.
DR   HOGENOM; HBG444693; -.
DR   HOVERGEN; HBG006672; -.
DR   InParanoid; O08919; -.
DR   OrthoDB; EOG4DR9D8; -.
DR   ArrayExpress; O08919; -.
DR   Bgee; O08919; -.
DR   CleanEx; MM_NUMBL; -.
DR   Genevestigator; O08919; -.
DR   GermOnline; ENSMUSG00000063160; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0034332; P:adherens junction organization; IGI:MGI.
DR   GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; ISS:UniProtKB.
DR   GO; GO:0021670; P:lateral ventricle development; IMP:UniProtKB.
DR   GO; GO:0021849; P:neuroblast division in subventricular zone; IMP:UniProtKB.
DR   GO; GO:0019538; P:protein metabolic process; ISS:UniProtKB.
DR   InterPro; IPR016698; Numb/numb-like.
DR   InterPro; IPR010449; Numb_domain.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF06311; NumbF; 1.
DR   Pfam; PF00640; PID; 1.
DR   PIRSF; PIRSF017607; Numb/numb-like; 1.
DR   SMART; SM00462; PTB; 1.
DR   PROSITE; PS01179; PID; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Developmental protein; Neurogenesis; Phosphoprotein;
KW   Ubl conjugation pathway.
FT   CHAIN         1    604       Numb-like protein.
FT                                /FTId=PRO_0000058000.
FT   DOMAIN       74    225       PID.
FT   COMPBIAS    422    441       Gln-rich.
FT   MOD_RES     263    263       Phosphoserine.
FT   MOD_RES     268    268       Phosphothreonine (By similarity).
FT   MOD_RES     279    279       Phosphothreonine.
FT   MOD_RES     411    411       Phosphoserine (By similarity).
FT   CONFLICT     28     28       P -> A (in Ref. 1; AAB58697).
FT   CONFLICT    244    244       Missing (in Ref. 1; AAB58697).
FT   CONFLICT    589    589       F -> S (in Ref. 1; AAB58697).
SQ   SEQUENCE   604 AA;  64191 MW;  3C6012B7BB30986E CRC64;
     MSRSAAASGG PRRPDQHLSP APCGASGPPE TFRTESDGAG TMNKLRQSLR RRKPAYVPEA
     SRPHQWQADE DAVRKGTCSF PVRYLGHVEV EESRGMHVCE DAVKKLKAMG RKSVKSVLWV
     SADGLRVVDD KTKDLLVDQT IEKVSFCAPD RNLDKAFSYI CRDGTTRRWI CHCFLALKDS
     GERLSHAVGC AFAACLERKQ RREKECGVTA AFDASRTSFA REGSFRLSGG GRPAEREAGD
     KKKAEAAAAP AVAPGPAQPG HVSPTPATTS PGEKGEAGTP VAAGTTAAAI PRRHAPLEQL
     VRQGSFRGFP ALSQKNSPFK RQLSLRLNEL PSTLQRRTDF QVKGTVPEME PPGTGDSDGI
     NALCTQISSS FASAGAPASG PPPATTGTSA WGEPSVPAAA AFQPGHKRTP SEAERWLEEV
     SQVAKAQQQQ QQQQQQQQQQ QATSVPPMPT MAPTLQPFSA PVGPFDTAAA QVAVFLPPTH
     MQPPFVPAYP GLGYPPMPRV PVVGITPSQM VANAFCSAAQ LQPQPATLLG KAGAFPPPAA
     PSAPGGQARP RPNGAPWPPE PAPAPAPELD PFEAQWAALE GKPAVEKPFN PFSGDLQKTF
     EIEL
//
ID   SDCB1_MOUSE             Reviewed;         299 AA.
AC   O08992; A2AKJ7; Q544P5;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Syntenin-1;
DE   AltName: Full=Scaffold protein Pbp1;
DE   AltName: Full=Syndecan-binding protein 1;
GN   Name=Sdcbp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Burbelo P.D.;
RT   "A new family of scaffold proteins.";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Hsu S.I.-H., Hentschel D.M., Bonventre J.V.;
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, DBA/2, and NOD;
RC   TISSUE=Amnion, Bone marrow, Heart, Kidney, Liver, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Seems to function as an adapter protein. In adherens
CC       junctions may function to couple syndecans to cytoskeletal
CC       proteins or signaling components. Seems to couple transcription
CC       factor SOX4 to the IL-5 receptor (IL5RA). May also play a role in
CC       vesicular trafficking. Seems to be required for the targeting of
CC       TGFA to the cell surface in the early secretory pathway.
CC   -!- SUBUNIT: Monomer and homodimer (By similarity). Interacts with
CC       SDC1, SDC2, SDC3, SDC4, NRXN2, EPHA7, EPHB1, NF2 isoform 1, TGFA,
CC       IL5RA, neurofascin, SDCBP2 and PTPRJ (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC       similarity). Melanosome (By similarity).
CC   -!- PTM: Phosphorylated on tyrosine residues (By similarity).
CC   -!- SIMILARITY: Contains 2 PDZ (DHR) domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF003693; AAB61293.1; -; mRNA.
DR   EMBL; AK028429; BAC25946.1; -; mRNA.
DR   EMBL; AK033412; BAC28275.1; -; mRNA.
DR   EMBL; AK146085; BAE26889.1; -; mRNA.
DR   EMBL; AK150278; BAE29434.1; -; mRNA.
DR   EMBL; AK150321; BAE29466.1; -; mRNA.
DR   EMBL; AK150623; BAE29713.1; -; mRNA.
DR   EMBL; AK150721; BAE29799.1; -; mRNA.
DR   EMBL; AK150801; BAE29864.1; -; mRNA.
DR   EMBL; AK152017; BAE30879.1; -; mRNA.
DR   EMBL; AK152434; BAE31216.1; -; mRNA.
DR   EMBL; AK152552; BAE31306.1; -; mRNA.
DR   EMBL; AK159677; BAE35280.1; -; mRNA.
DR   EMBL; AK167513; BAE39588.1; -; mRNA.
DR   EMBL; AK168004; BAE39992.1; -; mRNA.
DR   EMBL; AK168777; BAE40613.1; -; mRNA.
DR   EMBL; AK169219; BAE40990.1; -; mRNA.
DR   EMBL; AK169687; BAE41305.1; -; mRNA.
DR   EMBL; AK171162; BAE42284.1; -; mRNA.
DR   EMBL; AL772306; CAM27239.1; -; Genomic_DNA.
DR   EMBL; BC019400; AAH19400.1; -; mRNA.
DR   IPI; IPI00117375; -.
DR   RefSeq; NP_001091697.1; NM_001098227.1.
DR   RefSeq; NP_058087.2; NM_016807.2.
DR   UniGene; Mm.247473; -.
DR   UniGene; Mm.479881; -.
DR   ProteinModelPortal; O08992; -.
DR   SMR; O08992; 114-272.
DR   IntAct; O08992; 2.
DR   MINT; MINT-140766; -.
DR   STRING; O08992; -.
DR   PhosphoSite; O08992; -.
DR   PRIDE; O08992; -.
DR   Ensembl; ENSMUST00000029912; ENSMUSP00000029912; ENSMUSG00000028249.
DR   GeneID; 53378; -.
DR   KEGG; mmu:53378; -.
DR   UCSC; uc008rxn.1; mouse.
DR   CTD; 53378; -.
DR   MGI; MGI:1337026; Sdcbp.
DR   HOGENOM; HBG279356; -.
DR   HOVERGEN; HBG053211; -.
DR   InParanoid; O08992; -.
DR   OMA; KSVDNGI; -.
DR   OrthoDB; EOG47WNPB; -.
DR   PhylomeDB; O08992; -.
DR   NextBio; 310193; -.
DR   ArrayExpress; O08992; -.
DR   Bgee; O08992; -.
DR   CleanEx; MM_SDCBP; -.
DR   Genevestigator; O08992; -.
DR   GermOnline; ENSMUSG00000028249; Mus musculus.
DR   GO; GO:0005895; C:interleukin-5 receptor complex; IMP:UniProtKB.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005137; F:interleukin-5 receptor binding; IMP:UniProtKB.
DR   GO; GO:0007265; P:Ras protein signal transduction; IPI:MGI.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF00595; PDZ; 2.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; PDZ; 2.
DR   PROSITE; PS50106; PDZ; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; Membrane; Phosphoprotein; Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    299       Syntenin-1.
FT                                /FTId=PRO_0000184002.
FT   DOMAIN      115    194       PDZ 1.
FT   DOMAIN      199    273       PDZ 2.
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES       6      6       Phosphoserine (By similarity).
FT   MOD_RES      47     47       Phosphotyrosine (By similarity).
FT   MOD_RES      61     61       Phosphoserine (By similarity).
FT   MOD_RES      92     92       Phosphotyrosine (By similarity).
SQ   SEQUENCE   299 AA;  32379 MW;  04FFF7A33A7F0195 CRC64;
     MSLYPSLEDL KVDKVIQAQT AYSANPASQA FVLVDASAAL PPDGNLYPKL YPELSQYMGL
     SLNEAEICES MPMVSGAPAQ GQLVARPSSV NYMVAPVTGN DAGIRRAEIK QGIREVILCK
     DQDGKIGLRL KSIDNGIFVQ LVQANSPASL VGLRFGDQVL QINGENCAGW SSDKAHKVLK
     QAFGEKITMT IRDRPFERTV TMHKDSSGHV GFIFKSGKIT SIVKDSSAAR NGLLTDHHIC
     EINGQNVIGL KDAQIADILS TAGTVVTITI MPTFIFEHII KRMAPSIMKS LMDHTIPEV
//
ID   SH2B3_MOUSE             Reviewed;         548 AA.
AC   O09039;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 2.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=SH2B adapter protein 3;
DE   AltName: Full=Lymphocyte adapter protein;
DE   AltName: Full=Lymphocyte-specific adapter protein Lnk;
DE   AltName: Full=Signal transduction protein Lnk;
GN   Name=Sh2b3; Synonyms=Lnk;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=20567312; PubMed=11114373; DOI=10.1016/S1074-7613(00)00060-1;
RA   Takaki S., Sauer K., Iritani B.M., Chien S., Ebihara Y., Tsuji K.,
RA   Takatsu K., Perlmutter R.M.;
RT   "Control of B cell production by the adaptor protein lnk. Definition
RT   Of a conserved family of signal-modulating proteins.";
RL   Immunity 13:599-609(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Links T-cell receptor activation signal to phospholipase
CC       C-gamma-1, GRB2 and phosphatidylinositol 3-kinase (By similarity).
CC   -!- PTM: Tyrosine phosphorylated (By similarity).
CC   -!- SIMILARITY: Belongs to the SH2B adapter family.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; U89992; AAB58580.2; -; mRNA.
DR   EMBL; U89993; AAB58581.1; -; Genomic_DNA.
DR   EMBL; BC006759; AAH06759.1; -; mRNA.
DR   IPI; IPI00113783; -.
DR   RefSeq; NP_032533.1; NM_008507.3.
DR   UniGene; Mm.65493; -.
DR   ProteinModelPortal; O09039; -.
DR   SMR; O09039; 22-79, 162-284, 331-413.
DR   STRING; O09039; -.
DR   PhosphoSite; O09039; -.
DR   PRIDE; O09039; -.
DR   Ensembl; ENSMUST00000040308; ENSMUSP00000041611; ENSMUSG00000042594.
DR   Ensembl; ENSMUST00000086310; ENSMUSP00000083490; ENSMUSG00000042594.
DR   Ensembl; ENSMUST00000122426; ENSMUSP00000113926; ENSMUSG00000042594.
DR   GeneID; 16923; -.
DR   KEGG; mmu:16923; -.
DR   UCSC; uc008zkg.1; mouse.
DR   CTD; 16923; -.
DR   MGI; MGI:893598; Sh2b3.
DR   eggNOG; roNOG14954; -.
DR   GeneTree; ENSGT00530000063355; -.
DR   HOGENOM; HBG717575; -.
DR   HOVERGEN; HBG093951; -.
DR   InParanoid; O09039; -.
DR   OMA; RYSLADE; -.
DR   OrthoDB; EOG4S1T7G; -.
DR   PhylomeDB; O09039; -.
DR   NextBio; 461287; -.
DR   ArrayExpress; O09039; -.
DR   Bgee; O09039; -.
DR   CleanEx; MM_SH2B3; -.
DR   Genevestigator; O09039; -.
DR   GermOnline; ENSMUSG00000042594; Mus musculus.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IMP:MGI.
DR   GO; GO:0035162; P:embryonic hemopoiesis; IDA:MGI.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR015012; Phe_ZIP.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000980; SH2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF08916; Phe_ZIP; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00252; SH2; 1.
DR   SUPFAM; SSF109805; Phe_ZIP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
DR   PROSITE; PS50001; SH2; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; SH2 domain.
FT   CHAIN         1    548       SH2B adapter protein 3.
FT                                /FTId=PRO_0000084455.
FT   DOMAIN      168    279       PH.
FT   DOMAIN      336    434       SH2.
SQ   SEQUENCE   548 AA;  60487 MW;  D21DCE46185962B8 CRC64;
     MNEPTVQPSR TSSAPASPAS PRGWSDFCEQ HAAAAARELA RQYWLFARAH PQPPRADLVS
     LQFAELFQRH FCREVRESLA GPPGHDYRAT APPRPALPKA RSSEDLGPRP ACALQHLRRG
     LRQLFRRRSA GELPGATSDT NDIDTTAASR PGPARKLLPW GLREPPTEAL KEVVLRYSLA
     DEAAMDSGAR WQRGRLVLRS PGPGHSHFLQ LFDPPKSSKP KLQEACSSIR EVRPCTRLEM
     PDNLYTFVLK VQDQTDIIFE VGDEQQLNSW LAELRASTGL GLEHPDTELP LSLAAEPGPA
     RSPRGSTDSL DQGASPGVLL DPACQKTDHF LSCYPWFHGP ISRVRAAQLV QLQGPDAHGV
     FLVRQSESRR GEYVLTFNLQ GRAKHLRLVL TERGQCRVQH LHFPSVVDML RHFQRSPIPL
     ECGAACDVRL SGYVVVLSQA PGSSNTVLFP FSLPHWDSEL GHPHLSSVGC PPSHGAEALP
     GQVTPPEQIF HLVPSPEELA NSLRQLELES VSSARDSDYD MDSSSRGHLR AIDNQYTPLS
     QLCREADV
//
ID   SNP23_MOUSE             Reviewed;         210 AA.
AC   O09044; O35620;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Synaptosomal-associated protein 23;
DE            Short=SNAP-23;
DE   AltName: Full=Syndet;
DE   AltName: Full=Vesicle-membrane fusion protein SNAP-23;
GN   Name=Snap23; Synonyms=Sndt;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adipose tissue;
RX   MEDLINE=97312558; PubMed=9168999; DOI=10.1006/bbrc.1997.6560;
RA   Araki S., Tamori Y., Kawanishi M., Shinoda H., Masugi J., Mori H.,
RA   Niki T., Okazawa H., Kubota T., Kasuga M.;
RT   "Inhibition of the binding of SNAP-23 to syntaxin 4 by Munc18c.";
RL   Biochem. Biophys. Res. Commun. 234:257-262(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=97220227; PubMed=9067602;
RA   Wang G., Witkin J.W., Hao G., Bankaitis V.A., Scherer P.E.,
RA   Baldini G.;
RT   "Syndet is a novel SNAP-25 related protein expressed in many
RT   tissues.";
RL   J. Cell Sci. 110:505-513(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Olken S.K., Doerre S., Corley R.B.;
RT   "SNARE expression in mouse plasma cells.";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   PubMed=10773458; DOI=10.1016/S0378-1119(00)00100-1;
RA   Vaidyanathan V.V., Roche P.A.;
RT   "Structure and chromosomal localization of the mouse SNAP-23 gene.";
RL   Gene 247:181-189(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   IDENTIFICATION IN A COMPLEX WITH VAMP8 AND STX4.
RX   PubMed=15363411; DOI=10.1016/j.devcel.2004.08.002;
RA   Wang C.-C., Ng C.P., Lu L., Atlashkin V., Zhang W., Seet L.-F.,
RA   Hong W.;
RT   "A role of VAMP8/endobrevin in regulated exocytosis of pancreatic
RT   acinar cells.";
RL   Dev. Cell 7:359-371(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-34 AND SER-110,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Essential component of the high affinity receptor for
CC       the general membrane fusion machinery and an important regulator
CC       of transport vesicle docking and fusion (By similarity).
CC   -!- SUBUNIT: Binds simultaneously to SNAPIN and SYN4. Found in a
CC       complex with VAMP8 and STX1A (By similarity). Binds tightly to
CC       multiple syntaxins and synaptobrevins/VAMPs. Found in a complex
CC       with VAMP8 and STX4 in pancreas.
CC   -!- INTERACTION:
CC       O14920:IKBKB (xeno); NbExp=1; IntAct=EBI-1812522, EBI-81266;
CC       O88351:Ikbkb; NbExp=1; IntAct=EBI-1812522, EBI-447960;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC       Cell membrane; Lipid-anchor (By similarity). Cell junction,
CC       synapse, synaptosome. Note=Mainly localized to the plasma
CC       membrane.
CC   -!- TISSUE SPECIFICITY: Expressed in non-neuronal tissues.
CC   -!- SIMILARITY: Belongs to the SNAP-25 family.
CC   -!- SIMILARITY: Contains 2 t-SNARE coiled-coil homology domains.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AB000822; BAA20345.1; -; mRNA.
DR   EMBL; U73143; AAB53597.1; -; mRNA.
DR   EMBL; AF007169; AAB62932.1; -; mRNA.
DR   EMBL; AF213257; AAF23503.1; -; Genomic_DNA.
DR   EMBL; AF213251; AAF23503.1; JOINED; Genomic_DNA.
DR   EMBL; AF213252; AAF23503.1; JOINED; Genomic_DNA.
DR   EMBL; AF213253; AAF23503.1; JOINED; Genomic_DNA.
DR   EMBL; AF213254; AAF23503.1; JOINED; Genomic_DNA.
DR   EMBL; AF213255; AAF23503.1; JOINED; Genomic_DNA.
DR   EMBL; AF213256; AAF23503.1; JOINED; Genomic_DNA.
DR   EMBL; AK019162; BAB31577.1; -; mRNA.
DR   EMBL; BC070456; AAH70456.1; -; mRNA.
DR   IPI; IPI00622270; -.
DR   PIR; JC5512; JC5512.
DR   RefSeq; NP_001171263.1; NM_001177792.1.
DR   RefSeq; NP_001171264.1; NM_001177793.1.
DR   RefSeq; NP_033248.1; NM_009222.3.
DR   UniGene; Mm.245715; -.
DR   ProteinModelPortal; O09044; -.
DR   SMR; O09044; 23-76, 146-204.
DR   IntAct; O09044; 5.
DR   MINT; MINT-269238; -.
DR   STRING; O09044; -.
DR   PhosphoSite; O09044; -.
DR   PRIDE; O09044; -.
DR   Ensembl; ENSMUST00000028743; ENSMUSP00000028743; ENSMUSG00000027287.
DR   Ensembl; ENSMUST00000110711; ENSMUSP00000106339; ENSMUSG00000027287.
DR   GeneID; 20619; -.
DR   KEGG; mmu:20619; -.
DR   UCSC; uc008lwg.1; mouse.
DR   CTD; 20619; -.
DR   MGI; MGI:109356; Snap23.
DR   GeneTree; ENSGT00390000012186; -.
DR   HOVERGEN; HBG056971; -.
DR   OrthoDB; EOG4H9XMG; -.
DR   NextBio; 299005; -.
DR   ArrayExpress; O09044; -.
DR   Bgee; O09044; -.
DR   CleanEx; MM_SNAP23; -.
DR   Genevestigator; O09044; -.
DR   GermOnline; ENSMUSG00000027287; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR   GO; GO:0019717; C:synaptosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006887; P:exocytosis; IMP:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000928; SNAP-25.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   Pfam; PF00835; SNAP-25; 1.
DR   Pfam; PF05739; SNARE; 1.
DR   SMART; SM00397; t_SNARE; 2.
DR   PROSITE; PS50192; T_SNARE; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Cell junction; Cell membrane; Coiled coil; Lipoprotein;
KW   Membrane; Palmitate; Phosphoprotein; Protein transport; Repeat;
KW   Synapse; Synaptosome; Transport.
FT   CHAIN         1    210       Synaptosomal-associated protein 23.
FT                                /FTId=PRO_0000213599.
FT   DOMAIN       14     76       t-SNARE coiled-coil homology 1.
FT   DOMAIN      145    207       t-SNARE coiled-coil homology 2.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      20     20       Phosphoserine.
FT   MOD_RES      34     34       Phosphoserine.
FT   MOD_RES     102    102       Phosphothreonine (By similarity).
FT   MOD_RES     110    110       Phosphoserine.
FT   MOD_RES     112    112       Phosphoserine.
FT   LIPID        79     79       N-palmitoyl cysteine (By similarity).
FT   LIPID        80     80       N-palmitoyl cysteine (By similarity).
FT   LIPID        83     83       N-palmitoyl cysteine (By similarity).
FT   LIPID        85     85       N-palmitoyl cysteine (By similarity).
FT   LIPID        87     87       N-palmitoyl cysteine (By similarity).
FT   CONFLICT      6      6       P -> S (in Ref. 3; AAB62932).
FT   CONFLICT    204    204       A -> P (in Ref. 3; AAB62932).
SQ   SEQUENCE   210 AA;  23261 MW;  6919E127E16BA2C9 CRC64;
     MDNLSPEEVQ LRAHQVTDES LESTRRILGL AIESQDAGIK TITMLDEQGE QLNRIEEGMD
     QINKDMREAE KTLTELNKCC GLCICPCNRT KNFESGKNYK ATWGDGGDNS PSNVVSKQPS
     RITNGQPQQT TGAASGGYIK RITNDAREDE MEENLTQVGS ILGNLKNMAL DMGNEIDAQN
     QQIQKITEKA DTNKNRIDIA NTRAKKLIDS
//
ID   HDAC1_MOUSE             Reviewed;         482 AA.
AC   O09106; P97476;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   08-MAR-2011, entry version 114.
DE   RecName: Full=Histone deacetylase 1;
DE            Short=HD1;
DE            EC=3.5.1.98;
GN   Name=Hdac1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fibroblast;
RX   MEDLINE=97415582; PubMed=9271381;
RA   Bartl S., Taplick J., Lagger G., Khier H., Kuchler K., Seiser C.;
RT   "Identification of mouse histone deacetylase 1 as a growth factor-
RT   inducible gene.";
RL   Mol. Cell. Biol. 17:5033-5043(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Johnson C.A.;
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INTERACTION WITH SAP30.
RX   MEDLINE=98367545; PubMed=9702189; DOI=10.1016/S1097-2765(00)80111-2;
RA   Laherty C.D., Billin A.N., Lavinsky R.M., Yochum G.S., Bush A.C.,
RA   Sun J.-M., Mullen T.-M., Davie J.R., Rose D.W., Glass C.K.,
RA   Rosenfeld M.G., Ayer D.E., Eisenman R.N.;
RT   "SAP30, a component of the mSin3 corepressor complex involved in N-
RT   CoR-mediated repression by specific transcription factors.";
RL   Mol. Cell 2:33-42(1998).
RN   [4]
RP   INTERACTION WITH DNMT1.
RX   MEDLINE=20082816; PubMed=10615135; DOI=10.1038/71750;
RA   Fuks F., Burgers W.A., Brehm A., Hughes-Davies L., Kouzarides T.;
RT   "DNA methyltransferase Dnmt1 associates with histone deacetylase
RT   activity.";
RL   Nat. Genet. 24:88-91(2000).
RN   [5]
RP   INTERACTION WITH HDAC7.
RX   MEDLINE=20442375; PubMed=10984530; DOI=10.1073/pnas.97.19.10330;
RA   Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M.;
RT   "Identification of a nuclear domain with deacetylase activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000).
RN   [6]
RP   INTERACTION WITH HDAC9.
RX   PubMed=11022042; DOI=10.1074/jbc.M007364200;
RA   Zhang C.L., McKinsey T.A., Lu J.R., Olson E.N.;
RT   "Association of COOH-terminal-binding protein (CtBP) and MEF2-
RT   interacting transcription repressor (MITR) contributes to
RT   transcriptional repression of the MEF2 transcription factor.";
RL   J. Biol. Chem. 276:35-39(2001).
RN   [7]
RP   INTERACTION WITH CBFA2T3.
RX   PubMed=11533236; DOI=10.1128/MCB.21.19.6470-6483.2001;
RA   Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N.,
RA   Downing J.R., Meyers S., Hiebert S.W.;
RT   "ETO, a target of t(8;21) in acute leukemia, makes distinct contacts
RT   with multiple histone deacetylases and binds mSin3A through its
RT   oligomerization domain.";
RL   Mol. Cell. Biol. 21:6470-6483(2001).
RN   [8]
RP   INTERACTION WITH BAZ2A.
RX   PubMed=12198165; DOI=10.1093/emboj/cdf460;
RA   Zhou Y., Santoro R., Grummt I.;
RT   "The chromatin remodeling complex NoRC targets HDAC1 to the ribosomal
RT   gene promoter and represses RNA polymerase I transcription.";
RL   EMBO J. 21:4632-4640(2002).
RN   [9]
RP   INTERACTION WITH SIN3B.
RX   MEDLINE=21907235; PubMed=11909966;
RX   DOI=10.1128/MCB.22.8.2743-2750.2002;
RA   Alland L., David G., Shen-Li H., Potes J., Muhle R., Lee H.-C.,
RA   Hou H. Jr., Chen K., DePinho R.A.;
RT   "Identification of mammalian Sds3 as an integral component of the
RT   Sin3/histone deacetylase corepressor complex.";
RL   Mol. Cell. Biol. 22:2743-2750(2002).
RN   [10]
RP   INTERACTION WITH SUV39H1.
RX   MEDLINE=21648906; PubMed=11788710; DOI=10.1093/nar/30.2.475;
RA   Vaute O., Nicolas E., Vandel L., Trouche D.;
RT   "Functional and physical interaction between the histone methyl
RT   transferase Suv39H1 and histone deacetylases.";
RL   Nucleic Acids Res. 30:475-481(2002).
RN   [11]
RP   INTERACTION WITH SETDB1.
RX   PubMed=12398767; DOI=10.1042/BJ20020854;
RA   Yang L., Mei Q., Zielinska-Kwiatkowska A., Matsui Y., Blackburn M.L.,
RA   Benedetti D., Krumm A.A., Taborsky G.J. Jr., Chansky H.A.;
RT   "An ERG (ets-related gene)-associated histone methyltransferase
RT   interacts with histone deacetylases 1/2 and transcription co-
RT   repressors mSin3A/B.";
RL   Biochem. J. 369:651-657(2003).
RN   [12]
RP   IDENTIFICATION IN A COMPLEX WITH DNMT3A.
RX   MEDLINE=22502935; PubMed=12616525; DOI=10.1002/jcb.10457;
RA   Datta J., Ghoshal K., Sharma S.M., Tajima S., Jacob S.T.;
RT   "Biochemical fractionation reveals association of DNA
RT   methyltransferase (Dnmt) 3b with Dnmt1 and that of Dnmt 3a with a
RT   histone H3 methyltransferase and Hdac1.";
RL   J. Cell. Biochem. 88:855-864(2003).
RN   [13]
RP   INTERACTION WITH RERE.
RX   PubMed=14645126; DOI=10.1242/dev.00908;
RA   Zoltewicz J.S., Stewart N.J., Leung R., Peterson A.S.;
RT   "Atrophin 2 recruits histone deacetylase and is required for the
RT   function of multiple signaling centers during mouse embryogenesis.";
RL   Development 131:3-14(2004).
RN   [14]
RP   INTERACTION WITH PHB2.
RX   PubMed=15140878; DOI=10.1074/jbc.M312300200;
RA   Kurtev V., Margueron R., Kroboth K., Ogris E., Cavailles V.,
RA   Seiser C.;
RT   "Transcriptional regulation by the repressor of estrogen receptor
RT   activity via recruitment of histone deacetylases.";
RL   J. Biol. Chem. 279:24834-24843(2004).
RN   [15]
RP   INTERACTION WITH KLF1, AND FUNCTION.
RX   PubMed=15542849; DOI=10.1128/MCB.24.23.10416-10424.2004;
RA   Chen X., Bieker J.J.;
RT   "Stage-specific repression by the EKLF transcriptional activator.";
RL   Mol. Cell. Biol. 24:10416-10424(2004).
RN   [16]
RP   INTERACTION WITH NRIP1.
RX   PubMed=15060175; DOI=10.1093/nar/gkh524;
RA   Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P.,
RA   Vignon F., Khochbin S., Jalaguier S., Cavailles V.;
RT   "Multiple domains of the receptor-interacting protein 140 contribute
RT   to transcription inhibition.";
RL   Nucleic Acids Res. 32:1957-1966(2004).
RN   [17]
RP   INTERACTION WITH BAZ2A.
RX   PubMed=16085498; DOI=10.1016/j.cub.2005.06.057;
RA   Zhou Y., Grummt I.;
RT   "The PHD finger/bromodomain of NoRC interacts with acetylated histone
RT   H4K16 and is sufficient for rDNA silencing.";
RL   Curr. Biol. 15:1434-1438(2005).
RN   [18]
RP   INTERACTION WITH H2AFY.
RX   PubMed=16107708; DOI=10.1128/MCB.25.17.7616-7624.2005;
RA   Chakravarthy S., Gundimella S.K., Caron C., Perche P.-Y.,
RA   Pehrson J.R., Khochbin S., Luger K.;
RT   "Structural characterization of the histone variant macroH2A.";
RL   Mol. Cell. Biol. 25:7616-7624(2005).
RN   [19]
RP   INTERACTION WITH BANP.
RX   PubMed=16166625; DOI=10.1128/MCB.25.19.8415-8429.2005;
RA   Rampalli S., Pavithra L., Bhatt A., Kundu T.K., Chattopadhyay S.;
RT   "Tumor suppressor SMAR1 mediates cyclin D1 repression by recruitment
RT   of the SIN3/histone deacetylase 1 complex.";
RL   Mol. Cell. Biol. 25:8415-8429(2005).
RN   [20]
RP   INTERACTION WITH HDAC9, AND TISSUE SPECIFICITY.
RX   PubMed=15711539; DOI=10.1038/nn1408;
RA   Mejat A., Ramond F., Bassel-Duby R., Khochbin S., Olson E.N.,
RA   Schaeffer L.;
RT   "Histone deacetylase 9 couples neuronal activity to muscle chromatin
RT   acetylation and gene expression.";
RL   Nat. Neurosci. 8:313-321(2005).
RN   [21]
RP   INTERACTION WITH SMYD2.
RX   PubMed=16805913; DOI=10.1186/1476-4598-5-26;
RA   Brown M.A., Sims R.J. III, Gottlieb P.D., Tucker P.W.;
RT   "Identification and characterization of Smyd2: a split SET/MYND
RT   domain-containing histone H3 lysine 36-specific methyltransferase that
RT   interacts with the Sin3 histone deacetylase complex.";
RL   Mol. Cancer 5:26-26(2006).
RN   [22]
RP   INTERACTION WITH PRDM6.
RX   PubMed=16537907; DOI=10.1128/MCB.26.7.2626-2636.2006;
RA   Davis C.A., Haberland M., Arnold M.A., Sutherland L.B., McDonald O.G.,
RA   Richardson J.A., Childs G., Harris S., Owens G.K., Olson E.N.;
RT   "PRISM/PRDM6, a transcriptional repressor that promotes the
RT   proliferative gene program in smooth muscle cells.";
RL   Mol. Cell. Biol. 26:2626-2636(2006).
RN   [23]
RP   INTERACTION WITH HDAC9.
RX   PubMed=16611996; DOI=10.1128/MCB.26.9.3550-3564.2006;
RA   Morrison B.E., Majdzadeh N., Zhang X., Lyles A., Bassel-Duby R.,
RA   Olson E.N., D'Mello S.R.;
RT   "Neuroprotection by histone deacetylase-related protein.";
RL   Mol. Cell. Biol. 26:3550-3564(2006).
RN   [24]
RP   INTERACTION WITH ZNF541.
RX   PubMed=18849567; DOI=10.1074/jbc.M805590200;
RA   Choi E., Han C., Park I., Lee B., Jin S., Choi H., Kim do H.,
RA   Park Z.Y., Eddy E.M., Cho C.;
RT   "A novel germ cell-specific protein, SHIP1, forms a complex with
RT   chromatin remodeling activity during spermatogenesis.";
RL   J. Biol. Chem. 283:35283-35294(2008).
RN   [25]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND
RP   SER-423, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [26]
RP   INTERACTION WITH NR4A2.
RX   PubMed=19144721; DOI=10.1242/dev.029769;
RA   Jacobs F.M., van Erp S., van der Linden A.J., von Oerthel L.,
RA   Burbach J.P., Smidt M.P.;
RT   "Pitx3 potentiates Nurr1 in dopamine neuron terminal differentiation
RT   through release of SMRT-mediated repression.";
RL   Development 136:531-540(2009).
RN   [27]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND
RP   SER-423, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [28]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393; SER-421 AND
RP   SER-423, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on
CC       the N-terminal part of the core histones (H2A, H2B, H3 and H4).
CC       Histone deacetylation gives a tag for epigenetic repression and
CC       plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events. Histone deacetylases act via
CC       the formation of large multiprotein complexes. Deacetylates SP
CC       proteins, SP1 and SP3, and regulates their function. Component of
CC       the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-
CC       mediated transcription in resting neurons. Upon calcium
CC       stimulation, HDAC1 is released from the complex and CREBBP is
CC       recruited, which facilitates transcriptional activation.
CC       Deacetylates TSHZ3 and regulates its transcriptional repressor
CC       activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the
CC       transcriptional activity of NF-kappa-B (By similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC   -!- SUBUNIT: Part of the core histone deacetylase (HDAC) complex
CC       composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex
CC       associates with MTA2, MBD2, MBD3, MTA1L1, CHD3 and CHD4 to form
CC       the nucleosome remodeling and histone deacetylation (NuRD)
CC       complex, or with SIN3, SAP18 and SAP30 to form the SIN3 HDAC
CC       complex. Component of a BHC histone deacetylase complex that
CC       contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and
CC       PHF21A/BHC80. The BHC complex may also contain ZMYM2, ZNF217,
CC       ZMYM3, GSE1 and GTF2I. Associates with the 9-1-1 complex;
CC       interacts with HUS1. Found in a complex with DNMT3A and HDAC7.
CC       Interacts with BAZ2A/TIP5, BCOR, BRMS1L, DAXX, DNMT1, EP300,
CC       HCFC1, NFE4, PCAF, PHB2, MIER1, KDM4A, MINT, NRIP1, PRDM6, RERE,
CC       SETDB1, SMYD2, SUV39H1, TGIF, TGIF2, UHRF1, UHRF2 and ZNF541.
CC       Interacts with the non-histone region of H2AFY. Component of a
CC       mSin3A corepressor complex that contains SIN3A, SAP130,
CC       SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2. Interacts with KDM5B
CC       and BRMS1 (By similarity). Interacts with BANP and CBFA2T3.
CC       Interacts with SAP30L and KLF1. Interacts with E4F1. Interacts
CC       with CHFR, PRDM16, SP1, SP3, and SMAD3. Interacts with RB1 and
CC       SMARCA4/BRG1. Interacts with TRAF6. Interacts with TSHZ3 (via N-
CC       terminus); the interaction is direct. Found in a trimeric complex
CC       with APBB1 and TSHZ3; the interaction between HDAC1 and APBB1 is
CC       mediated by TSHZ3. Interacts with APEX1; the interaction is not
CC       dependent on the acetylated status of APEX1 (By similarity).
CC       Interacts with NR4A2/NURR1.
CC   -!- INTERACTION:
CC       P13864:Dnmt1; NbExp=2; IntAct=EBI-301912, EBI-301927;
CC       Q8BX46:Lbxcor1; NbExp=1; IntAct=EBI-301912, EBI-604451;
CC       P25799:Nfkb1; NbExp=1; IntAct=EBI-301912, EBI-643958;
CC       P62137:Ppp1ca; NbExp=1; IntAct=EBI-301912, EBI-357187;
CC       Q04207:Rela; NbExp=1; IntAct=EBI-301912, EBI-644400;
CC       Q80TZ9:Rere; NbExp=1; IntAct=EBI-301912, EBI-904076;
CC       O88574:Sap30; NbExp=1; IntAct=EBI-301912, EBI-593511;
CC       O88939:Zbtb7a; NbExp=2; IntAct=EBI-301912, EBI-595063;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Widely expressed with higher levels in thymus
CC       and testis and lower levels in liver. Present in muscle (at
CC       protein level).
CC   -!- INDUCTION: By interleukin-2.
CC   -!- PTM: Sumoylated on Lys-444 and Lys-476; which promotes enzymatic
CC       activity. Desumoylated by SENP1 (By similarity).
CC   -!- PTM: Phosphorylation on Ser-421 and Ser-423 promotes enzymatic
CC       activity and interactions with NuRD and SIN3 complexes (By
CC       similarity).
CC   -!- PTM: Ubiquitinated by CHFR, leading to its degradation by the
CC       proteasome (By similarity).
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; X98207; CAA66870.1; -; mRNA.
DR   EMBL; U80780; AAB68398.1; -; mRNA.
DR   IPI; IPI00114232; -.
DR   RefSeq; NP_032254.1; NM_008228.2.
DR   UniGene; Mm.202504; -.
DR   UniGene; Mm.391033; -.
DR   ProteinModelPortal; O09106; -.
DR   SMR; O09106; 8-373.
DR   DIP; DIP-31499N; -.
DR   IntAct; O09106; 18.
DR   MINT; MINT-2568222; -.
DR   STRING; O09106; -.
DR   PhosphoSite; O09106; -.
DR   PRIDE; O09106; -.
DR   Ensembl; ENSMUST00000102597; ENSMUSP00000099657; ENSMUSG00000028800.
DR   GeneID; 433759; -.
DR   KEGG; mmu:433759; -.
DR   UCSC; uc008uxg.1; mouse.
DR   CTD; 433759; -.
DR   MGI; MGI:108086; Hdac1.
DR   eggNOG; roNOG14641; -.
DR   HOGENOM; HBG396919; -.
DR   HOVERGEN; HBG057112; -.
DR   InParanoid; O09106; -.
DR   OMA; QHGCDTH; -.
DR   OrthoDB; EOG4868CH; -.
DR   PhylomeDB; O09106; -.
DR   NextBio; 408961; -.
DR   ArrayExpress; O09106; -.
DR   Bgee; O09106; -.
DR   CleanEx; MM_HDAC1; -.
DR   Genevestigator; O09106; -.
DR   GermOnline; ENSMUSG00000061062; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR   GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0016581; C:NuRD complex; IPI:MGI.
DR   GO; GO:0005667; C:transcription factor complex; IPI:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0004407; F:histone deacetylase activity; IDA:UniProtKB.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR   GO; GO:0008134; F:transcription factor binding; TAS:UniProtKB.
DR   GO; GO:0016564; F:transcription repressor activity; IDA:MGI.
DR   GO; GO:0007492; P:endoderm development; IDA:MGI.
DR   GO; GO:0021766; P:hippocampus development; IGI:MGI.
DR   GO; GO:0016575; P:histone deacetylation; IEA:InterPro.
DR   GO; GO:0010553; P:negative regulation of gene-specific transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0030182; P:neuron differentiation; IGI:MGI.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR003084; His_deacetylse_1.
DR   Gene3D; G3DSA:3.40.800.20; His_deacetylse; 1.
DR   PANTHER; PTHR10625; His_deacetylse; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   PRINTS; PR01271; HISDACETLASE.
PE   1: Evidence at protein level;
KW   Acetylation; Chromatin regulator; Hydrolase; Isopeptide bond;
KW   Methylation; Nucleus; Phosphoprotein; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN         1    482       Histone deacetylase 1.
FT                                /FTId=PRO_0000114688.
FT   REGION        9    321       Histone deacetylase.
FT   ACT_SITE    141    141       By similarity.
FT   MOD_RES      74     74       N6-acetyllysine (By similarity).
FT   MOD_RES     220    220       N6-acetyllysine (By similarity).
FT   MOD_RES     221    221       Phosphotyrosine (By similarity).
FT   MOD_RES     393    393       Phosphoserine.
FT   MOD_RES     406    406       Phosphoserine (By similarity).
FT   MOD_RES     421    421       Phosphoserine.
FT   MOD_RES     423    423       Phosphoserine.
FT   MOD_RES     432    432       N6-methylated lysine; by EHMT2 (By
FT                                similarity).
FT   CROSSLNK    444    444       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    476    476       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
SQ   SEQUENCE   482 AA;  55075 MW;  7F64D3C17F5E4844 CRC64;
     MAQTQGTKRK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK MEIYRPHKAN
     AEEMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC PVFDGLFEFC QLSTGGSVAS
     AVKLNKQQTD IAVNWAGGLH HAKKSEASGF CYVNDIVLAI LELLKYHQRV LYIDIDIHHG
     DGVEEAFYTT DRVMTVSFHK YGEYFPGTGD LRDIGAGKGK YYAVNYPLRD GIDDESYEAI
     FKPVMSKVME MFQPSAVVLQ CGSDSLSGDR LGCFNLTIKG HAKCVEFVKS FNLPMLMLGG
     GGYTIRNVAR CWTYETAVAL DTEIPNELPY NDYFEYFGPD FKLHISPSNM TNQNTNEYLE
     KIKQRLFENL RMLPHAPGVQ MQAIPEDAIP EESGDEDEED PDKRISICSS DKRIACEEEF
     SDSDEEGEGG RKNSSNFKKA KRVKTEDEKE KDPEEKKEVT EEEKTKEEKP EAKGVKEEVK
     LA
//
ID   SEM4D_MOUSE             Reviewed;         861 AA.
AC   O09126;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Semaphorin-4D;
DE   AltName: Full=M-Sema G;
DE   AltName: Full=Semaphorin-C-like 2;
DE   AltName: Full=Semaphorin-J;
DE            Short=Sema J;
DE   AltName: CD_antigen=CD100;
DE   Flags: Precursor;
GN   Name=Sema4d; Synonyms=Semacl2, Semaj;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=97125976; PubMed=8969198; DOI=10.1074/jbc.271.52.33376;
RA   Furuyama T., Inagaki S., Kosugi A., Noda S., Saitoh S., Ogata M.,
RA   Iwahashi Y., Miyazaki N., Hamaoka T., Tohyama M.;
RT   "Identification of a novel transmembrane semaphorin expressed on
RT   lymphocytes.";
RL   J. Biol. Chem. 271:33376-33381(1996).
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-77; ASN-379 AND ASN-419,
RP   AND MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: May play a functional role in the immune system, as well
CC       as in the nervous system.
CC   -!- SUBUNIT: Homodimer. Binds PLXNB1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in lymphoid tissues,
CC       especially in the thymus, as well as in the nervous tissues.
CC   -!- SIMILARITY: Belongs to the semaphorin family.
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 1 PSI domain.
CC   -!- SIMILARITY: Contains 1 Sema domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U69535; AAC52964.1; -; mRNA.
DR   IPI; IPI00114274; -.
DR   UniGene; Mm.33903; -.
DR   ProteinModelPortal; O09126; -.
DR   SMR; O09126; 24-648.
DR   STRING; O09126; -.
DR   PhosphoSite; O09126; -.
DR   PRIDE; O09126; -.
DR   Ensembl; ENSMUST00000021900; ENSMUSP00000021900; ENSMUSG00000021451.
DR   Ensembl; ENSMUST00000110039; ENSMUSP00000105666; ENSMUSG00000021451.
DR   Ensembl; ENSMUST00000110040; ENSMUSP00000105667; ENSMUSG00000021451.
DR   MGI; MGI:109244; Sema4d.
DR   eggNOG; roNOG12836; -.
DR   HOGENOM; HBG717343; -.
DR   HOVERGEN; HBG061627; -.
DR   InParanoid; O09126; -.
DR   OrthoDB; EOG43N7C4; -.
DR   ArrayExpress; O09126; -.
DR   Bgee; O09126; -.
DR   Genevestigator; O09126; -.
DR   GermOnline; ENSMUSG00000021451; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005102; F:receptor binding; IPI:MGI.
DR   GO; GO:0050772; P:positive regulation of axonogenesis; IDA:MGI.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003659; Plexin-like.
DR   InterPro; IPR016201; Plexin-like_fold.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR001627; Semaphorin/CD100_Ag.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF01437; PSI; 1.
DR   Pfam; PF01403; Sema; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00423; PSI; 1.
DR   SMART; SM00630; Sema; 1.
DR   SUPFAM; SSF103575; Plexin-like_fold; 1.
DR   SUPFAM; SSF101912; Sema; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51004; SEMA; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Neurogenesis; Phosphoprotein; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     23       Potential.
FT   CHAIN        24    861       Semaphorin-4D.
FT                                /FTId=PRO_0000032328.
FT   TOPO_DOM     24    733       Extracellular (Potential).
FT   TRANSMEM    734    754       Helical; (Potential).
FT   TOPO_DOM    755    861       Cytoplasmic (Potential).
FT   DOMAIN       24    500       Sema.
FT   DOMAIN      502    551       PSI.
FT   DOMAIN      555    636       Ig-like C2-type.
FT   MOD_RES     195    195       Phosphoserine (By similarity).
FT   CARBOHYD     49     49       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     77     77       N-linked (GlcNAc...).
FT   CARBOHYD    139    139       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    191    191       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    379    379       N-linked (GlcNAc...).
FT   CARBOHYD    419    419       N-linked (GlcNAc...).
FT   CARBOHYD    613    613       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    632    632       N-linked (GlcNAc...) (Potential).
FT   DISULFID     97    108       By similarity.
FT   DISULFID    126    135       By similarity.
FT   DISULFID    257    370       By similarity.
FT   DISULFID    281    326       By similarity.
FT   DISULFID    503    520       By similarity.
FT   DISULFID    509    553       By similarity.
FT   DISULFID    512    529       By similarity.
FT   DISULFID    576    624       By similarity.
SQ   SEQUENCE   861 AA;  95714 MW;  533CD6D271A6D79B CRC64;
     MRMCAPVRGL FLALVVVLRT AVAFAPVPRL TWEHGEVGLV QFHKPGIFNY SALLMSEDKD
     TLYVGAREAV FAVNALNISE KQHEVYWKVS EDKKSKCAEK GKSKQTECLN YIRVLQPLSS
     TSLYVCGTNA FQPTCDHLNL TSFKFLGKSE DGKGRCPFDP AHSYTSVMVG GELYSGTSYN
     FLGSEPIISR NSSHSPLRTE YAIPWLNEPS FVFADVIQKS PDGPEGEDDK VYFFFTEVSV
     EYEFVFKLMI PRVARVCKGD QGGLRTLQKK WTSFLKARLI CSKPDSGLVF NILQDVFVLR
     APGLKEPVFY AVFTPQLNNV GLSAVCAYTL ATVEAVFSRG KYMQSATVEQ SHTKWVRYNG
     PVPTPRPGAC IDSEARAANY TSSLNLPDKT LQFVKDHPLM DDSVTPIDNR PKLIKKDVNY
     TQIVVDRTQA LDGTFYDVMF ISTDRGALHK AVILTKEVHV IEETQLFRDF EPVLTLLLSS
     KKGRKFVYAG SNSGVVQAPL AFCEKHGSCE DCVLARDPYC AWSPAIKACV TLHQEEASSR
     GWIQDMSGDT SSCLDKSKES FNQHFFKHGG TAELKCFQKS NLARVVWKFQ NGELKAASPK
     YGFVGRKHLL IFNLSDGDSG VYQCLSEERV RNKTVSQLLA KHVLEVKMVP RTPPSPTSED
     VQTEGSKITS KMPVGSTQGS SPPTPALWAT SPRAATLPPK SSSGTSCEPK MVINTVPQLH
     SEKTVYLKSS DNRLLMSLLL FIFVLFLCLF SYNCYKGYLP GQCLKFRSAL LLGKKTPKSD
     FSDLEQSVKE TLVEPGSFSQ QNGDHPKPAL DTGYETEQDT ITSKVPTDRE DSQRIDELSA
     RDKPFDVKCE LKFADSDADG D
//
ID   KIF1C_MOUSE             Reviewed;        1100 AA.
AC   O35071; Q5SX62;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 2.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Kinesin-like protein KIF1C;
GN   Name=Kif1c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 94-253.
RC   STRAIN=ICR;
RX   MEDLINE=97420736; PubMed=9275178; DOI=10.1073/pnas.94.18.9654;
RA   Nakagawa T., Tanaka Y., Matsuoka E., Kondo S., Okada Y., Noda Y.,
RA   Kanai Y., Hirokawa N.;
RT   "Identification and classification of 16 new kinesin superfamily (KIF)
RT   proteins in mouse genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:9654-9659(1997).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674; SER-676 AND
RP   THR-1080, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674; SER-676 AND
RP   SER-1031, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Motor required for the retrograde transport of Golgi
CC       vesicles to the endoplasmic reticulum. Has a microtubule plus end-
CC       directed motility (By similarity).
CC   -!- SUBUNIT: Monomer (Potential).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (Probable).
CC   -!- SIMILARITY: Belongs to the kinesin-like protein family. Unc-104
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 FHA domain.
CC   -!- SIMILARITY: Contains 1 kinesin-motor domain.
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DR   EMBL; AL596117; CAI25184.1; -; Genomic_DNA.
DR   EMBL; AB001456; BAA22398.1; -; mRNA.
DR   IPI; IPI00462727; -.
DR   RefSeq; NP_694743.2; NM_153103.2.
DR   UniGene; Mm.99996; -.
DR   ProteinModelPortal; O35071; -.
DR   SMR; O35071; 4-347, 498-599.
DR   IntAct; O35071; 13.
DR   STRING; O35071; -.
DR   PhosphoSite; O35071; -.
DR   PRIDE; O35071; -.
DR   Ensembl; ENSMUST00000094499; ENSMUSP00000092075; ENSMUSG00000020821.
DR   Ensembl; ENSMUST00000102554; ENSMUSP00000099614; ENSMUSG00000020821.
DR   GeneID; 16562; -.
DR   KEGG; mmu:16562; -.
DR   NMPDR; fig|10090.3.peg.24583; -.
DR   UCSC; uc007jwl.1; mouse.
DR   CTD; 16562; -.
DR   MGI; MGI:1098260; Kif1c.
DR   HOVERGEN; HBG057158; -.
DR   InParanoid; O35071; -.
DR   OMA; QSAQLSY; -.
DR   OrthoDB; EOG4W3SM7; -.
DR   PhylomeDB; O35071; -.
DR   NextBio; 290057; -.
DR   ArrayExpress; O35071; -.
DR   Bgee; O35071; -.
DR   CleanEx; MM_KIF1C; -.
DR   Genevestigator; O35071; -.
DR   GermOnline; ENSMUSG00000020821; Mus musculus.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IDA:MGI.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR008984; SMAD_FHA_domain.
DR   Gene3D; G3DSA:2.60.200.20; FHA; 1.
DR   Gene3D; G3DSA:3.40.850.10; kinesin_motor; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00240; FHA; 1.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF49879; SMAD_FHA; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; FALSE_NEG.
DR   PROSITE; PS00411; KINESIN_MOTOR_DOMAIN1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_DOMAIN2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW   Motor protein; Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1   1100       Kinesin-like protein KIF1C.
FT                                /FTId=PRO_0000125411.
FT   DOMAIN        1    273       Kinesin-motor.
FT   DOMAIN      523    590       FHA.
FT   NP_BIND      97    104       ATP (By similarity).
FT   COILED      359    381       Potential.
FT   COILED      438    479       Potential.
FT   COILED      634    671       Potential.
FT   COILED      827    871       Potential.
FT   COMPBIAS    964   1082       Pro-rich.
FT   MOD_RES     494    494       Phosphoserine (By similarity).
FT   MOD_RES     674    674       Phosphoserine.
FT   MOD_RES     676    676       Phosphoserine.
FT   MOD_RES    1031   1031       Phosphoserine.
FT   MOD_RES    1079   1079       Phosphothreonine (By similarity).
FT   MOD_RES    1080   1080       Phosphothreonine.
FT   MOD_RES    1089   1089       Phosphoserine (By similarity).
SQ   SEQUENCE   1100 AA;  122434 MW;  E92CFFECE6D0F0DA CRC64;
     MAGASVKVAV RVRPFNARET SQDAKCVVSM QGNTTSIINP KQSKDAPKSF TFDYSYWSHT
     SVEDPQFASQ QQVYRDIGEE MLLHAFEGYN VCIFAYGQTG AGKSYTMMGR QEPGQQGIVP
     QLCEDLFSRV NVNQSAQLSY SVEVSYMEIY CERVRDLLNP KSRGSLRVRE HPILGPYVQD
     LSKLAVTSYA DIADLMDCGN KARTVAATNM NETSSRSHAV FTIVFTQRSH DQLTGLDSEK
     VSKISLVDLA GSERADSSGA RGMRLKEGAN INKSLTTLGK VISALADLQS KKRKSDFIPY
     RDSVLTWLLK ENLGGNSRTA MIAALSPADI NYEETLSTLR YADRTKQIRC NAVINEDPNA
     RLIRELQEEV ARLRDLLMAQ GLSASALGGL KVEEGSPGGV LPPASSPPAP ASPSSPPPHN
     GELEPSFSPS AEPQIGPEEA MERLQETEKI IAELNETWEE KLRKTEALRM EREALLAEMG
     VAVREDGGTV GVFSPKKTPH LVNLNEDPLM SECLLYHIKD GVTRVGQVDV DIKLTGQFIR
     EQHCLFRSIP QPDGEVMVTL EPCEGAETYV NGKLVTEPLV LKSGNRIVMG KNHVFRFNHP
     EQARLERERG VPPPPGPPSE PVDWNFAQKE LLEQQGIDIK LEMEKRLQDL ENQYRKEKEE
     ADLLLEQQRL YADSDSGEDS DKRSCEESWR LISSLREQLP PTTVQNIVKR CGLPSSGKRR
     APRRVYQIPQ RRRLQGKDPR WATMADLKMQ AVKEICYEVA LADFRHGRAE IEALAALKMR
     ELCRTYGKPE GPGDAWRAVA RDVWDTVGEE EGCGGGGGGS EEGARGAEVE DLRAHIDKLT
     GILQEVKLQN SSKDRELQAL RDRMLRMERV IPLTQDLEDD NDESGLVTWA PPEGPEAVEE
     TVPNDHSPAV RPTSPPLSSW ERVSRLMEED PAFRRGRLRW LKQEQLRLQG LQGAGGRGGG
     LRRPPARFVP PHDCKLRFPF KSNPQHRESW PGMGSGEAPA PQPPEEVTVP PAPPNRRPPS
     PRRPHRSRRN SLDGGSRSRG GGSTQPEPQH LRPQKHNGYP QQPQPSPAQR PGPRYPPYTT
     PPRMRRQRSA PDLKESGAAV
//
ID   DPYL4_MOUSE             Reviewed;         572 AA.
AC   O35098; O08886; Q3UL94;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Dihydropyrimidinase-related protein 4;
DE            Short=DRP-4;
DE   AltName: Full=Collapsin response mediator protein 3;
DE            Short=CRMP-3;
DE   AltName: Full=UNC33-like phosphoprotein 4;
DE            Short=ULIP-4;
GN   Name=Dpysl4; Synonyms=Crmp3, Ulip4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Embryo;
RA   Hamajima N., Kato Y., Kouwaki M., Wada Y., Sasaski M., Nonaka M.;
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=98314496; PubMed=9652388;
RX   DOI=10.1046/j.1432-1327.1998.2540014.x;
RA   Byk T., Ozon S., Sobel A.;
RT   "The Ulip family phosphoproteins -- common and specific properties.";
RL   Eur. J. Biochem. 254:14-24(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PROTEIN SEQUENCE OF 346-361, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [5]
RP   INTERACTION WITH DPYSL2.
RX   PubMed=9375656;
RA   Wang L.H., Strittmatter S.M.;
RT   "Brain CRMP forms heterotetramers similar to liver
RT   dihydropyrimidinase.";
RL   J. Neurochem. 69:2261-2269(1997).
RN   [6]
RP   SUBUNIT.
RX   MEDLINE=20545548; PubMed=10956643; DOI=10.1074/jbc.M003277200;
RA   Fukada M., Watakabe I., Yuasa-Kawada J., Kawachi H., Kuroiwa A.,
RA   Matsuda Y., Noda M.;
RT   "Molecular characterization of CRMP5, a novel member of the collapsin
RT   response mediator protein family.";
RL   J. Biol. Chem. 275:37957-37965(2000).
RN   [7]
RP   INTERACTION WITH PLEXA1, AND SUBUNIT.
RX   PubMed=14685275; DOI=10.1038/sj.emboj.7600021;
RA   Deo R.C., Schmidt E.F., Elhabazi A., Togashi H., Burley S.K.,
RA   Strittmatter S.M.;
RT   "Structural bases for CRMP function in plexin-dependent semaphorin3A
RT   signaling.";
RL   EMBO J. 23:9-22(2004).
CC   -!- FUNCTION: Necessary for signaling by class 3 semaphorins and
CC       subsequent remodeling of the cytoskeleton. Plays a role in axon
CC       guidance, neuronal growth cone collapse and cell migration (By
CC       similarity).
CC   -!- SUBUNIT: Homotetramer, and heterotetramer with CRMP1, DPYSL2,
CC       DPYSL3 or DPYSL5. Interacts with PLEXA1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O35098-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O35098-2; Sequence=VSP_024802;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the DHOase family.
CC       Hydantoinase/dihydropyrimidinase subfamily.
CC   -!- CAUTION: Lacks most of the conserved residues that are essential
CC       for binding the metal cofactor and hence for dihydropyrimidinase
CC       activity. Its enzyme activity is therefore unsure.
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DR   EMBL; AB006715; BAA21888.1; -; mRNA.
DR   EMBL; Y09079; CAA70299.1; -; mRNA.
DR   EMBL; AK145638; BAE26556.1; -; mRNA.
DR   IPI; IPI00313151; -.
DR   IPI; IPI00845581; -.
DR   UniGene; Mm.250414; -.
DR   ProteinModelPortal; O35098; -.
DR   SMR; O35098; 14-490.
DR   STRING; O35098; -.
DR   MEROPS; M38.977; -.
DR   PhosphoSite; O35098; -.
DR   REPRODUCTION-2DPAGE; O35098; -.
DR   PRIDE; O35098; -.
DR   Ensembl; ENSMUST00000026551; ENSMUSP00000026551; ENSMUSG00000025478.
DR   UCSC; uc009kfj.1; mouse.
DR   MGI; MGI:1349764; Dpysl4.
DR   eggNOG; roNOG06642; -.
DR   HOVERGEN; HBG000806; -.
DR   OrthoDB; EOG48PMJT; -.
DR   PhylomeDB; O35098; -.
DR   ArrayExpress; O35098; -.
DR   Bgee; O35098; -.
DR   CleanEx; MM_DPYSL4; -.
DR   Genevestigator; O35098; -.
DR   GermOnline; ENSMUSG00000025478; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR006680; Amidohydro_1.
DR   InterPro; IPR011778; D-hydantoinase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Metalo_hydrolase; 2.
DR   TIGRFAMs; TIGR02033; D-hydantoinase; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Direct protein sequencing;
KW   Phosphoprotein.
FT   CHAIN         1    572       Dihydropyrimidinase-related protein 4.
FT                                /FTId=PRO_0000165922.
FT   MOD_RES     544    544       Phosphoserine (By similarity).
FT   VAR_SEQ       1     13       MSFQGKKSIPRIT -> MAYKMSQSISVTLGKDIPSRLRCL
FT                                PQRPLFSLCQ (in isoform 2).
FT                                /FTId=VSP_024802.
FT   CONFLICT    125    126       ER -> DG (in Ref. 2; CAA70299).
FT   CONFLICT    354    354       G -> V (in Ref. 2; CAA70299).
FT   CONFLICT    420    420       F -> I (in Ref. 2; CAA70299 and 3;
FT                                BAE26556).
SQ   SEQUENCE   572 AA;  61962 MW;  37671129FC02C7AF CRC64;
     MSFQGKKSIP RITSDRLLIK GGKIVNDDQS FHADLYVEDG LIKQIGENLI VPGGIKTIDA
     HGLMVLPGGV DVHTRLQMPV MGMTPADDFC QGTKAALAGG TTMILDHVFP DAGVSLLAAY
     EQWRERADSA ACCDYSLHVD IPRWHESTKE ELEALVRDKG VNSFLVFMAY KDRCQCTDGQ
     IYEIFSLIRD LGAVAQVHAE NGDIVEEEQK RLLEQGITGP EGHVLSHPEE VEAEAVYRAV
     TIAKQANCPL YVTKVMSKGA ADMVAQAKRR GVVVFGEPIT ASLGTDGSHY WSKNWAKAAA
     FVTSPPINPD PTTADHLTSL LSSGDLQVTG SAHCTFTTAQ KAVGKDNFTL IPEGVNGIEE
     RMSVVWEKCV ASGKMDENEF VAVTSTNAAK IFNFYPRKGR VAVGSDADLV IWNPRATKVF
     SAKSHNLNVE YNIFEGVECR GVPTVVISQG RVVLEDGNLL VTPGAGRFIP RKTFPDFVYK
     RIKARNRLAE IHGVPRGLYD GPVHEVMLPA KPGSGTQARA SCSGKISVPP VRNLHQSGFS
     LSGSQADDHI ARRTAQKIMA PPGGRSNITS LS
//
ID   M3K5_MOUSE              Reviewed;        1380 AA.
AC   O35099;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   30-NOV-2010, entry version 94.
DE   RecName: Full=Mitogen-activated protein kinase kinase kinase 5;
DE            EC=2.7.11.25;
DE   AltName: Full=Apoptosis signal-regulating kinase 1;
DE            Short=ASK-1;
DE   AltName: Full=MAPK/ERK kinase kinase 5;
DE            Short=MEK kinase 5;
DE            Short=MEKK 5;
GN   Name=Map3k5; Synonyms=Ask1, Mekk5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=98042492; PubMed=9367868; DOI=10.1006/bbrc.1997.7580;
RA   Tobiume K., Inage T., Takeda K., Enomoto S., Miyazono K., Ichijo H.;
RT   "Molecular cloning and characterization of the mouse apoptosis signal-
RT   regulating kinase 1.";
RL   Biochem. Biophys. Res. Commun. 239:905-910(1997).
RN   [2]
RP   SEQUENCE REVISION TO 22-26; 123; 273; 755; 1001-1011; 1220-1222 AND
RP   1274-1280.
RA   Tobiume K., Inage T., Takeda K., Enomoto S., Miyazono K., Ichijo H.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INTERACTION WITH PPM1L.
RX   PubMed=17456047; DOI=10.1042/BJ20070231;
RA   Saito J., Toriumi S., Awano K., Ichijo H., Sasaki K., Kobayashi T.,
RA   Tamura S.;
RT   "Regulation of apoptosis signal-regulating kinase 1 by protein
RT   phosphatase 2Cepsilon.";
RL   Biochem. J. 405:591-596(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-965, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Component of a protein kinase signal transduction
CC       cascade. Phosphorylates and activates MAP2K4 and MAP2K6, which in
CC       turn activate the JNK and p38 MAP kinases, respectively.
CC       Overexpression induces apoptotic cell death (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Contains an N-terminal autoinhibitory domain.
CC       Activated by phosphorylation at Thr-845, inhibited by
CC       phosphorylation at Ser-973 and Ser-1040. Binds to, and stabilizes
CC       MAP3K6 and is activated by MAP3K6 by phosphorylation on Thr-845.
CC   -!- SUBUNIT: Homodimer when inactive. Binds both upstream activators
CC       and downstream substrates in multimolecular complexes. Interacts
CC       with DAB2IP (By similarity). Interacts with PPM1L. Interacts with
CC       ARRB2 (By similarity).
CC   -!- INTERACTION:
CC       P31750:Akt1; NbExp=1; IntAct=EBI-777493, EBI-298707;
CC       Q9WTR2:Map3k6; NbExp=1; IntAct=EBI-777493, EBI-1254790;
CC   -!- TISSUE SPECIFICITY: Expressed in various adult mouse tissues
CC       including heart, brain, lung, liver and kidney.
CC   -!- PTM: Dephosphorylated and activated by PGAM5 (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB006787; BAA23648.3; -; mRNA.
DR   IPI; IPI00126589; -.
DR   PIR; JC5778; JC5778.
DR   UniGene; Mm.6595; -.
DR   ProteinModelPortal; O35099; -.
DR   SMR; O35099; 617-947.
DR   IntAct; O35099; 3.
DR   MINT; MINT-151480; -.
DR   STRING; O35099; -.
DR   PhosphoSite; O35099; -.
DR   PRIDE; O35099; -.
DR   Ensembl; ENSMUST00000095806; ENSMUSP00000093485; ENSMUSG00000071369.
DR   UCSC; uc007enm.1; mouse.
DR   MGI; MGI:1346876; Map3k5.
DR   eggNOG; roNOG12766; -.
DR   HOGENOM; HBG380040; -.
DR   HOVERGEN; HBG006305; -.
DR   InParanoid; O35099; -.
DR   BRENDA; 2.7.11.25; 244.
DR   BRENDA; 2.7.12.2; 244.
DR   ArrayExpress; O35099; -.
DR   Bgee; O35099; -.
DR   CleanEx; MM_MAP3K5; -.
DR   Genevestigator; O35099; -.
DR   GermOnline; ENSMUSG00000071369; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0008656; F:caspase activator activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0000187; P:activation of MAPK activity; IDA:MGI.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; ATP-binding; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN         1   1380       Mitogen-activated protein kinase kinase
FT                                kinase 5.
FT                                /FTId=PRO_0000086250.
FT   DOMAIN      687    945       Protein kinase.
FT   NP_BIND     693    701       ATP (By similarity).
FT   ACT_SITE    810    810       Proton acceptor (By similarity).
FT   BINDING     716    716       ATP (By similarity).
FT   MOD_RES     843    843       Phosphothreonine (By similarity).
FT   MOD_RES     845    845       Phosphothreonine (By similarity).
FT   MOD_RES     965    965       Phosphoserine.
FT   MOD_RES     973    973       Phosphoserine (By similarity).
FT   MOD_RES     983    983       Phosphothreonine (By similarity).
FT   MOD_RES     984    984       Phosphoserine (By similarity).
FT   MOD_RES     985    985       Phosphoserine (By similarity).
FT   MOD_RES     986    986       Phosphoserine (By similarity).
FT   MOD_RES     991    991       Phosphoserine (By similarity).
FT   MOD_RES     993    993       Phosphoserine (By similarity).
FT   MOD_RES     996    996       Phosphothreonine (By similarity).
FT   MOD_RES    1036   1036       Phosphoserine (By similarity).
FT   MOD_RES    1040   1040       Phosphoserine (By similarity).
SQ   SEQUENCE   1380 AA;  154460 MW;  D2CB6DA32515740F CRC64;
     MGTEAGEGIT FSVPPFASVG FCTIPEGGSC RRGGGAATAA EGEPSLQPLL VPPPPPPPGS
     FWNVESAAAP GTSCPTTAPG SSATRGRGNS GSGGGRRTTV AYVINEASQG QLVVAESEAL
     QSLREACEAV GATLETLHFG KLDFGETAVL DRFYNADIAV VEMSDTFRQP SLFYHLGVRE
     SFSMANNIIL YCDTNSDSLQ SLKEIICQKN TVCTGNYTFI PYMVTPHNKV YCCDSSFMKG
     LTELMQPNFE LLLGPICLPL VDRFVQLLKV AQASSSQYFR ESILSDIRKA RNLYTGKELA
     AELARIRQRV DNIEVLTADI VINLLLSYRD IQDYDSIVKL VETLEKLPTF DLASHHHVKF
     HYAFALNTRT LPGDRAKALD IMIPMVQSEE QVASDMYCLV GRIYKDMFLD SNFTDTESRD
     HGASWFKKAF ESEPTLQSGI NYAVLLLAAG HQFESSFELR KVGVKLSSLL GKKGNLEKLQ
     SYWEVGFFLG ASVLANDHLR VIQASEKLFR LKTPAWYLKS IVETILIYKH FVKLTTEQPS
     AKQELVDFWM DFLVEATKTD VTVVRFPVLI LEPTKIYQPS YLSINNEVEE KTISIWHVLP
     DDKKGIHEWN FGASSVRGVS ISKFEERCCF LYVLHNSDDF QIYFCTELHC KRFFEMVNTI
     TEEKGRGAED GDCEGDSLEY DYEYDENGDR VVLGKGTYGI VYAGRDLSNQ VRIAIKEIPE
     RDSRYSQPLH EEIALHKHLK HKNIVQYLGS FSENGFIKIF MEQVPGGSLS ALLRSKWGPL
     KDNEQTIGFY TKQILEGLKY LHDNQIVHRD IKGDNVLINT YSGVLKISDF GTSKRLAGIN
     PCTETFTGTL QYMAPEIIDK GPRGYGKAAD IWSLGCTIIE MATGKPPFYE LGEPQAAMFK
     VGMFKVHPEI PESMSAEAKA FILKCFEPDP DKRACANDLL IDEFLKVSSK KKKTQPKLSA
     LSTGSNEYLR SISLPVPVLV EDTSSSSEYG SVSPDTELKA DPFSFKARAK SCGEKDGKGI
     RTLFLGIPDE NFEDHSAPPS PEEKDSGFFM LRKDSERRAT LHRILTEDQD KVVRNLMESL
     AQGAEEPKLN WEHITTLISS LREFVRSTDR KIIATTLSKL KLELDFDSHG ISQVQVVLFG
     FQDAVNKVLR NHNIKPHWMF ALDSIIRKAV QTAITILVPE LRPHFSLASE SDTADPEDLD
     VEDEHEELSS NQTVRRPQAI TEDAVATSGV STLSSTVSHD SQNAHRSLNV QLGRMKIETN
     RLLEELVRKE RELQALLHQA IEEKDQEIRH LKLKSQPIDI PGFPVCHLNS PGTTTEDSEL
     PGWLRENGAD EDTISRFLAE DYTLVDVLYY VTRDDLKCLR LRGGMLCTLW KAIIDFRNKC
//
ID   KCNK3_MOUSE             Reviewed;         409 AA.
AC   O35111; O35163;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 2.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Potassium channel subfamily K member 3;
DE   AltName: Full=Acid-sensitive potassium channel protein TASK-1;
DE   AltName: Full=Cardiac two pore background K(+) channel;
DE   AltName: Full=TWIK-related acid-sensitive K(+) channel 1;
DE   AltName: Full=Two pore potassium channel KT3.1;
DE            Short=Two pore K(+) channel KT3.1;
DE   AltName: Full=cTBAK-1;
GN   Name=Kcnk3; Synonyms=Ctbak, Task, Task1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RX   MEDLINE=98165556; PubMed=9506712;
RA   Kim D., Fujita A., Horio Y., Kurachi Y.;
RT   "Cloning and functional expression of a novel cardiac two-pore
RT   background K+ channel (cTBAK-1).";
RL   Circ. Res. 82:513-518(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Heart;
RX   MEDLINE=20287574; PubMed=10748056; DOI=10.1074/jbc.M001948200;
RA   Lopes C.M.B., Gallagher P.G., Buck M.E., Butler M.H.,
RA   Goldstein S.A.N.;
RT   "Proton block and voltage gating are potassium-dependent in the
RT   cardiac leak channel Kcnk3.";
RL   J. Biol. Chem. 275:16969-16978(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4-409.
RX   MEDLINE=97459932; PubMed=9312005; DOI=10.1093/emboj/16.17.5464;
RA   Duprat F., Lesage F., Fink M., Reyes R., Heurteaux C., Lazdunski M.;
RT   "TASK, a human background K+ channel to sense external pH variations
RT   near physiological pH.";
RL   EMBO J. 16:5464-5471(1997).
CC   -!- FUNCTION: pH-dependent, voltage-insensitive, background potassium
CC       channel protein. Rectification direction results from potassium
CC       ion concentration on either side of the membrane. Acts as an
CC       outward rectifier when external potassium concentration is low.
CC       When external potassium concentration is high, current is inward
CC       (By similarity).
CC   -!- SUBUNIT: Homodimer (Potential).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- TISSUE SPECIFICITY: Very strong expression in heart, also detected
CC       in kidney, brain, skin, testis, lung, skeletal muscle, small
CC       intestine and stomach. Not detected in liver, thymus or spleen.
CC   -!- MISCELLANEOUS: Inactivated by barium.
CC   -!- SIMILARITY: Belongs to the two pore domain potassium channel
CC       (TC 1.A.1.8) family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AB008537; BAA25436.1; -; mRNA.
DR   EMBL; AF241798; AAF81418.1; -; Genomic_DNA.
DR   EMBL; AF242508; AAF81418.1; JOINED; Genomic_DNA.
DR   EMBL; AF065162; AAG29339.1; -; mRNA.
DR   EMBL; AF006824; AAC53367.1; -; mRNA.
DR   EMBL; AB013345; BAA28349.1; -; mRNA.
DR   IPI; IPI00127445; -.
DR   RefSeq; NP_034738.1; NM_010608.2.
DR   UniGene; Mm.439936; -.
DR   ProteinModelPortal; O35111; -.
DR   SMR; O35111; 77-131, 161-243.
DR   STRING; O35111; -.
DR   PhosphoSite; O35111; -.
DR   PRIDE; O35111; -.
DR   Ensembl; ENSMUST00000066295; ENSMUSP00000098987; ENSMUSG00000049265.
DR   GeneID; 16527; -.
DR   KEGG; mmu:16527; -.
DR   UCSC; uc008wvr.1; mouse.
DR   CTD; 16527; -.
DR   MGI; MGI:1100509; Kcnk3.
DR   eggNOG; maNOG04166; -.
DR   HOGENOM; HBG445489; -.
DR   HOVERGEN; HBG052239; -.
DR   InParanoid; O35111; -.
DR   OMA; KYLLHRA; -.
DR   OrthoDB; EOG4VX25V; -.
DR   PhylomeDB; O35111; -.
DR   NextBio; 289927; -.
DR   ArrayExpress; O35111; -.
DR   Bgee; O35111; -.
DR   CleanEx; MM_KCNK3; -.
DR   Genevestigator; O35111; -.
DR   GermOnline; ENSMUSG00000049265; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR013099; Ion_trans_2.
DR   InterPro; IPR003280; K_chnl_2pore.
DR   InterPro; IPR003092; K_chnl_2pore_TASK.
DR   InterPro; IPR022306; K_chnl_2pore_TASK/TWIK.
DR   InterPro; IPR005406; K_chnl_2pore_TASK1.
DR   PANTHER; PTHR11003:SF16; TASK1_channel; 1.
DR   Pfam; PF07885; Ion_trans_2; 2.
DR   PIRSF; PIRSF038061; K_channel_subfamily_K_type; 1.
DR   PRINTS; PR01333; 2POREKCHANEL.
DR   PRINTS; PR01584; TASK1CHANNEL.
DR   PRINTS; PR01095; TASKCHANNEL.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Ion transport; Ionic channel; Membrane; Potassium;
KW   Potassium channel; Potassium transport; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    409       Potassium channel subfamily K member 3.
FT                                /FTId=PRO_0000101745.
FT   TOPO_DOM      1      8       Cytoplasmic (Potential).
FT   TRANSMEM      9     29       Helical; (Potential).
FT   INTRAMEM     78    101       Pore-forming; Name=Pore-forming 1;
FT                                (Potential).
FT   TRANSMEM    108    128       Helical; (Potential).
FT   TOPO_DOM    129    158       Cytoplasmic (Potential).
FT   TRANSMEM    159    179       Helical; (Potential).
FT   INTRAMEM    184    207       Pore-forming; Name=Pore-forming 2;
FT                                (Potential).
FT   TRANSMEM    223    243       Helical; (Potential).
FT   TOPO_DOM    244    409       Cytoplasmic (Potential).
FT   CARBOHYD     53     53       N-linked (GlcNAc...) (Potential).
FT   CONFLICT      4      4       Q -> E (in Ref. 3; AAC53367).
FT   CONFLICT    123    123       V -> I (in Ref. 3; AAC53367).
SQ   SEQUENCE   409 AA;  45068 MW;  35236E011AAC5687 CRC64;
     MKRQNVRTLA LIVCTFTYLL VGAAVFDALE SEPEMIERQR LELRQLELRA RYNLSEGGYE
     ELERVVLRLK PHKAGVQWRF AGSFYFAITV ITTIGYGHAA PSTDGGKVFC MFYALLGIPL
     TLVMFQSLGE RINTFVRYLL HRAKRGLGMR HAEVSMANMV LIGFVSCIST LCIGAAAFSY
     YERWTFFQAY YYCFITLTTI GFGDYVALQK DQALQTQPQY VAFSFVYILT GLTVIGAFLN
     LVVLRFMTMN AEDEKRDAEH RALLTHNGQA VGLGGLSCLS GSLGDGVRPR DPVTCAAAAG
     GVGVGVGGSG FRNVYAEVLH FQSMCSCLWY KSREKLQYSI PMIIPRDLST SDTCVEHSHS
     SPGGGGRYSD TPSHPCLCSG TQRSAISSVS TGLHSLAAFR GLMKRRSSV
//
ID   SCRB2_MOUSE             Reviewed;         478 AA.
AC   O35114; Q3UNF8;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Lysosome membrane protein 2;
DE   AltName: Full=85 kDa lysosomal membrane sialoglycoprotein;
DE            Short=LGP85;
DE   AltName: Full=Lysosome membrane protein II;
DE            Short=LIMP II;
DE   AltName: Full=Scavenger receptor class B member 2;
GN   Name=Scarb2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   TISSUE=Liver;
RX   MEDLINE=98060500; PubMed=9399579;
RA   Tabuchi N., Akasaki K., Sasaki T., Kanda N., Tsuji H.;
RT   "Identification and characterization of a major lysosomal membrane
RT   glycoprotein, LGP85/LIMP II in mouse liver.";
RL   J. Biochem. 122:756-763(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 276-294 AND 361-378, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-105, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: May act as a lysosomal receptor (By similarity).
CC   -!- INTERACTION:
CC       P04062:GBA (xeno); NbExp=1; IntAct=EBI-1564519, EBI-1564609;
CC       P17439:Gba; NbExp=1; IntAct=EBI-1564519, EBI-1564504;
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Detected in the extracts of brain, heart,
CC       lung, liver and kidney.
CC   -!- PTM: Acylated by palmitic acid group(s) (By similarity).
CC   -!- PTM: Heavily glycosylated.
CC   -!- SIMILARITY: Belongs to the CD36 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AB008553; BAA23372.1; -; mRNA.
DR   EMBL; AK011123; BAB27416.1; -; mRNA.
DR   EMBL; AK083038; BAC38740.1; -; mRNA.
DR   EMBL; AK144235; BAE25789.1; -; mRNA.
DR   EMBL; BC029073; AAH29073.1; -; mRNA.
DR   IPI; IPI00127447; -.
DR   PIR; JC5670; JC5670.
DR   RefSeq; NP_031670.1; NM_007644.3.
DR   UniGene; Mm.297964; -.
DR   ProteinModelPortal; O35114; -.
DR   IntAct; O35114; 5.
DR   STRING; O35114; -.
DR   PhosphoSite; O35114; -.
DR   PRIDE; O35114; -.
DR   Ensembl; ENSMUST00000031377; ENSMUSP00000031377; ENSMUSG00000029426.
DR   GeneID; 12492; -.
DR   KEGG; mmu:12492; -.
DR   UCSC; uc008ydm.1; mouse.
DR   CTD; 12492; -.
DR   MGI; MGI:1196458; Scarb2.
DR   eggNOG; roNOG04558; -.
DR   HOGENOM; HBG445256; -.
DR   HOVERGEN; HBG106707; -.
DR   InParanoid; O35114; -.
DR   OMA; IVEWNGK; -.
DR   OrthoDB; EOG4CJVHB; -.
DR   PhylomeDB; O35114; -.
DR   NextBio; 281416; -.
DR   ArrayExpress; O35114; -.
DR   Bgee; O35114; -.
DR   CleanEx; MM_SCARB2; -.
DR   Genevestigator; O35114; -.
DR   GermOnline; ENSMUSG00000029426; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   InterPro; IPR002159; CD36.
DR   InterPro; IPR005429; LimpII.
DR   PANTHER; PTHR11923; CD36; 1.
DR   Pfam; PF01130; CD36; 1.
DR   PRINTS; PR01609; CD36FAMILY.
DR   PRINTS; PR01611; LIMPII.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Lipoprotein; Lysosome;
KW   Membrane; Palmitate; Receptor; Transmembrane; Transmembrane helix.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    478       Lysosome membrane protein 2.
FT                                /FTId=PRO_0000144156.
FT   TOPO_DOM      2      4       Cytoplasmic (Potential).
FT   TRANSMEM      5     27       Helical; (Potential).
FT   TOPO_DOM     28    433       Lumenal (Potential).
FT   TRANSMEM    434    459       Helical; (Potential).
FT   TOPO_DOM    460    478       Cytoplasmic (Potential).
FT   CARBOHYD     45     45       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     68     68       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    105    105       N-linked (GlcNAc...).
FT   CARBOHYD    122    122       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    206    206       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    224    224       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    249    249       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    304    304       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    325    325       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    412    412       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    430    430       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   478 AA;  54044 MW;  55724B77855470DF CRC64;
     MGRCCFYTAG TLSLLLLVTS VTLLVARVFQ KAVDQTIEKN MVLQNGTKVF NSWEKPPLPV
     YIQFYFFNVT NPEEILQGEI PLLEEVGPYT YRELRNKANI QFGENGTTIS AVTNKAYVFE
     RNQSVGDPNV DLIRTINIPL LTVVDLAQLT LLRELIEAML KAYQQKLFVI HTVHELLWGY
     KDEILSLVHI FKPDVSPNFG LFYERNGTND GEYVFLTGED NYLNFSKIVE WNGKTSLDWW
     TTDTCNMING TDGDSFHPLI SKDEVLYLFP SDLCRSVHIT FSSFENVEGL PAFRYKVPAE
     ILANTSENAG FCIPEGNCMD SGVLNISICK NGAPIIMSFP HFYQADEKFV SAIKGMHPNK
     EEHESFVDIN PLTGIILRGA KRFQINTYVR KLDDFVETGD IRTMVFPVMY LNESVLIDKE
     TANQLKSVIN TTLVVTNIPY IIMALGVFFG LVFTWLACRG QGSMDEGTAD ERAPLIRT
//
ID   ATN1_MOUSE              Reviewed;        1175 AA.
AC   O35126; P70200; Q80YQ0;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Atrophin-1;
DE   AltName: Full=Dentatorubral-pallidoluysian atrophy protein homolog;
GN   Name=Atn1; Synonyms=Drpla;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND POLYMORPHISM OF POLY-GLN REGION.
RX   MEDLINE=97224514; PubMed=9070948; DOI=10.1006/geno.1996.4522;
RA   Oyake M., Onodera O., Shiroishi T., Takano H., Takahashi Y.,
RA   Komonami R., Moriwaki K., Ikeuchi T., Igarashi S., Tanaka H.,
RA   Tsuji S.;
RT   "Molecular cloning of murine homologue dentatorubral-pallidoluysian
RT   atrophy (DRPLA) cDNA: strong conservation of a polymorphic CAG repeat
RT   in the murine gene.";
RL   Genomics 40:205-207(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=98112780; PubMed=9445485;
RA   Ansari-Lari M.A., Oeltjen J.C., Schwartz S., Zhang Z., Muzny D.M.,
RA   Lu J., Gorrell J.H., Chinault A.C., Belmont J.W., Miller W.,
RA   Gibbs R.A.;
RT   "Comparative sequence analysis of a gene-rich cluster at human
RT   chromosome 12p13 and its syntenic region in mouse chromosome 6.";
RL   Genome Res. 8:29-40(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBUNIT: Interacts with BAIAP2, WWP1, WWP2, WWP3 and RERE (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed. Most abundant in the brain.
CC   -!- DEVELOPMENTAL STAGE: Expressed as early as 5 days and thereafter
CC       shows little variation throughout 17 days.
CC   -!- POLYMORPHISM: The poly-Gln region of Atn1 is polymorphic (3 to 8
CC       repeats).
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DR   EMBL; D87744; BAA13450.1; -; mRNA.
DR   EMBL; AC002397; AAC36003.1; -; Genomic_DNA.
DR   EMBL; CH466523; EDK99754.1; -; Genomic_DNA.
DR   EMBL; CH466523; EDK99755.1; -; Genomic_DNA.
DR   EMBL; BC050920; AAH50920.2; -; mRNA.
DR   EMBL; BC053051; AAH53051.1; -; mRNA.
DR   IPI; IPI00858102; -.
DR   RefSeq; NP_031907.2; NM_007881.4.
DR   UniGene; Mm.333380; -.
DR   ProteinModelPortal; O35126; -.
DR   STRING; O35126; -.
DR   PhosphoSite; O35126; -.
DR   PRIDE; O35126; -.
DR   Ensembl; ENSMUST00000088357; ENSMUSP00000085695; ENSMUSG00000004263.
DR   GeneID; 13498; -.
DR   KEGG; mmu:13498; -.
DR   UCSC; uc009drq.1; mouse.
DR   CTD; 13498; -.
DR   MGI; MGI:104725; Atn1.
DR   eggNOG; roNOG15198; -.
DR   GeneTree; ENSGT00580000081398; -.
DR   HOGENOM; HBG446647; -.
DR   HOVERGEN; HBG075369; -.
DR   InParanoid; O35126; -.
DR   OMA; ATFPHVT; -.
DR   OrthoDB; EOG4RFKT4; -.
DR   NextBio; 284033; -.
DR   ArrayExpress; O35126; -.
DR   Bgee; O35126; -.
DR   Genevestigator; O35126; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0050827; F:toxin receptor binding; IDA:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; IGI:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0009404; P:toxin metabolic process; IDA:MGI.
DR   InterPro; IPR017993; Atrophin-1.
DR   InterPro; IPR002951; Atrophin-like.
DR   Pfam; PF03154; Atrophin-1; 2.
DR   PRINTS; PR01222; ATROPHIN.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein; Polymorphism; Triplet repeat expansion.
FT   CHAIN         1   1175       Atrophin-1.
FT                                /FTId=PRO_0000356253.
FT   COMPBIAS    166    172       Poly-Pro.
FT   COMPBIAS    304    307       Poly-Pro.
FT   COMPBIAS    378    383       Poly-Ser.
FT   COMPBIAS    387    396       Poly-Ser.
FT   COMPBIAS    441    446       Poly-Pro.
FT   COMPBIAS    477    480       Poly-His.
FT   COMPBIAS    481    487       Poly-Gln.
FT   COMPBIAS    495    498       Poly-Pro.
FT   COMPBIAS    555    564       Poly-Ser.
FT   COMPBIAS    694    697       Poly-Pro.
FT   COMPBIAS    792    805       Ala/Arg-rich.
FT   COMPBIAS    806    817       Arg/Glu-rich (mixed charge).
FT   COMPBIAS    915    924       Arg/Glu-rich (mixed charge).
FT   COMPBIAS   1035   1062       His-rich.
FT   MOD_RES     101    101       Phosphoserine.
FT   MOD_RES     626    626       N6-acetyllysine (By similarity).
FT   CONFLICT    452    452       A -> G (in Ref. 1; BAA13450).
FT   CONFLICT    495    495       P -> A (in Ref. 1; BAA13450).
FT   CONFLICT    532    532       P -> A (in Ref. 1; BAA13450).
FT   CONFLICT    691    691       S -> L (in Ref. 1; BAA13450).
FT   CONFLICT    734    734       P -> A (in Ref. 1; BAA13450).
FT   CONFLICT    766    766       D -> T (in Ref. 1; BAA13450).
FT   CONFLICT    926    926       D -> N (in Ref. 1; BAA13450).
SQ   SEQUENCE   1175 AA;  123724 MW;  8BEFFAB75DDC0F36 CRC64;
     MKTRQNKDSM SMRSGRKKEA PGPREELRSR GRASPGGVST SSSDGKAEKS RQTAKKARIE
     EPSAPKASKQ GRSEEISESE SEETSAPKKT KTEQELPRPQ SPSDLDSLDG RSINDDGSSD
     PRDIDQDNRS TSPSIYSPGS VENDSDSSSG LSQGPARPYH PPPLFPPSPP PPDSTPRQPE
     SGFEPHPSVP PTGYHAPMEP PTSRLFQGPP PGAPPTHPQL YPGNASGGVL SGPPMGPKGG
     AAASSVGAPS GGKQHPPPTT PIPISSSGAS GAPPAKPPSA PVGGGSLPSA PPPASFPHVT
     PNLPPPPALR PLNNASASPP GMGAQPIPGH LPSPHAMGQG MSGLPPGPEK GPTLAPSPHP
     LPPASSSAPG PPMRYPYSSS SSSAAASSSS SSSSASQYPA SQALPSYPHS FPPPTSMSVS
     NQPPKYTQPS LPSQAVWSQG PPPPPPYGRL LANNNTHPGP FPPTGGQSTA HPAAPTHHHH
     QQQPQQQHHH GNSGPPPPGA YPHPLESSNS HHAHPYNMSP SLGSLRPYPP GPAHLPPPHG
     QVSYNQAGPN GPPVSSSNSS GSSSQASYSC SHPSSSQGPQ GASYPFPPVP PVTTSSATLS
     TVIATVASSP AGYKTASPPG PPQYSKRAPS PGSYKTATPP GYKPGSPPSF RTGTPPGYRG
     TSPPAGPGTF KPGSPTVGPG PLPPAGPSSL SSLPPPPAAP TTGPPLTATQ IKQEPAEEYE
     PPESPVPPAR SPSPPPKVVD VPSHASQSAR FNKHLDRGFN SCARSDLYFV PLEGSKLAKK
     RADLVEKVRR EAEQRAREEK EREREREREK EREREKEREL ERSVKLAQEG RAPVECPSLG
     PVPHRPPFEP GSAVATVPPY LGPDTPALRT LSEYARPHVM SPGNRNHPFY VPLGAVDPGL
     LGYNVPALYS SDPAARERER EARERDLRDR LKPGFEVKPS ELEPLHGVPG PGLDPFPRHG
     GLALQPGPPG LHPFPFHPSL GPLERERLAL AAGPALRPDM SYAERLAAER QHAERVAALG
     NDPLARLQML NVTPHHHQHS HIHSHLHLHQ QDAIHAASAS VHPLIDPLAS GSHLTRIPYP
     AGTLPNPLLP HPLHENEVLR HQLFAAPYRD LPASLSAPMS AAHQLQAMHA QSAELQRLAL
     EQQQWLHAHH PLHSVPLPAQ EDYYSHLKKE SDKPL
//
ID   PHB2_MOUSE              Reviewed;         299 AA.
AC   O35129; O89075; Q61336;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Prohibitin-2;
DE   AltName: Full=B-cell receptor-associated protein BAP37;
DE   AltName: Full=Repressor of estrogen receptor activity;
GN   Name=Phb2; Synonyms=Bap, Bcap37, Rea;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Lymphoid tissue;
RX   MEDLINE=94349926; PubMed=8070406;
RA   Terashima M., Kim K.-M., Adachi T., Nielsen P.J., Reth M., Koehler G.,
RA   Lamers M.C.;
RT   "The IgM antigen receptor of B lymphocytes is associated with
RT   prohibitin and a prohibitin-related protein.";
RL   EMBO J. 13:3782-3792(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH ESR1.
RC   STRAIN=129/SvJ; TISSUE=Pituitary;
RX   MEDLINE=22877119; PubMed=12878603; DOI=10.1074/jbc.M303882200;
RA   Lin V.Y., Resnick E.M., Shupnik M.A.;
RT   "Truncated estrogen receptor product-1 stimulates estrogen receptor
RT   alpha transcriptional activity by titration of repressor proteins.";
RL   J. Biol. Chem. 278:38125-38131(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ESR1; HDAC1 AND
RP   HDAC5, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   PubMed=15140878; DOI=10.1074/jbc.M312300200;
RA   Kurtev V., Margueron R., Kroboth K., Ogris E., Cavailles V.,
RA   Seiser C.;
RT   "Transcriptional regulation by the repressor of estrogen receptor
RT   activity via recruitment of histone deacetylases.";
RL   J. Biol. Chem. 279:24834-24843(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=98112780; PubMed=9445485;
RA   Ansari-Lari M.A., Oeltjen J.C., Schwartz S., Zhang Z., Muzny D.M.,
RA   Lu J., Gorrell J.H., Chinault A.C., Belmont J.W., Miller W.,
RA   Gibbs R.A.;
RT   "Comparative sequence analysis of a gene-rich cluster at human
RT   chromosome 12p13 and its syntenic region in mouse chromosome 6.";
RL   Genome Res. 8:29-40(1998).
RN   [5]
RP   PROTEIN SEQUENCE OF 25-48; 55-71; 98-142; 148-165; 335-346; 866-885
RP   AND 1051-1058, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 73-154.
RC   STRAIN=BALB/c; TISSUE=Spleen;
RX   MEDLINE=99012997; PubMed=9798653; DOI=10.1016/S0161-5890(98)00031-5;
RA   Chu C.C., Paul W.E.;
RT   "Expressed genes in interleukin-4 treated B cells identified by cDNA
RT   representational difference analysis.";
RL   Mol. Immunol. 35:487-502(1998).
RN   [7]
RP   INTERACTION WITH PHB, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=11302691; DOI=10.1006/excr.2001.5166;
RA   Coates P.J., Nenutil R., McGregor A., Picksley S.M., Crouch D.H.,
RA   Hall P.A., Wright E.G.;
RT   "Mammalian prohibitin proteins respond to mitochondrial stress and
RT   decrease during cellular senescence.";
RL   Exp. Cell Res. 265:262-273(2001).
CC   -!- FUNCTION: Acts as a mediator of transcriptional repression by
CC       nuclear hormone receptors via recruitment of histone deacetylases.
CC       Functions as an estrogen receptor (ER)-selective coregulator that
CC       potentiates the inhibitory activities of antiestrogens and
CC       represses the activity of estrogens. Competes with NCOA1 for
CC       modulation of ER transcriptional activity. Probably involved in
CC       regulating mitochondrial respiration activity and in aging.
CC   -!- SUBUNIT: Interacts with PHB, ESR1, HDAC1 and HDAC5.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane. Cytoplasm.
CC       Nucleus. Note=Also cytoplasmic and nuclear.
CC   -!- TISSUE SPECIFICITY: Widely expressed in different tissues.
CC   -!- DEVELOPMENTAL STAGE: Throughout gestation, highly expressed in
CC       brown fat, heart, liver, developing renal tubules and neurons, and
CC       detected at lower levels in tissues such as lung and exocrine
CC       pancreas.
CC   -!- SIMILARITY: Belongs to the prohibitin family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X78683; CAA55350.1; -; mRNA.
DR   EMBL; AY319418; AAP86652.1; -; mRNA.
DR   EMBL; AY211613; AAP47231.1; -; mRNA.
DR   EMBL; AC002397; AAC36005.1; -; Genomic_DNA.
DR   EMBL; U89422; AAC36528.1; -; mRNA.
DR   IPI; IPI00321718; -.
DR   PIR; S46996; S46996.
DR   RefSeq; NP_031557.2; NM_007531.2.
DR   UniGene; Mm.36241; -.
DR   ProteinModelPortal; O35129; -.
DR   STRING; O35129; -.
DR   PhosphoSite; O35129; -.
DR   REPRODUCTION-2DPAGE; O35129; -.
DR   PRIDE; O35129; -.
DR   Ensembl; ENSMUST00000004375; ENSMUSP00000004375; ENSMUSG00000004264.
DR   GeneID; 12034; -.
DR   KEGG; mmu:12034; -.
DR   CTD; 12034; -.
DR   MGI; MGI:102520; Phb2.
DR   eggNOG; maNOG18062; -.
DR   HOGENOM; HBG680510; -.
DR   HOVERGEN; HBG004457; -.
DR   InParanoid; O35129; -.
DR   OMA; FTVEAGH; -.
DR   OrthoDB; EOG4QFWDX; -.
DR   PhylomeDB; O35129; -.
DR   NextBio; 280279; -.
DR   ArrayExpress; O35129; -.
DR   Bgee; O35129; -.
DR   CleanEx; MM_PHB2; -.
DR   Genevestigator; O35129; -.
DR   GermOnline; ENSMUSG00000004264; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0016566; F:specific transcriptional repressor activity; IDA:UniProtKB.
DR   GO; GO:0060749; P:mammary gland alveolus development; IMP:MGI.
DR   GO; GO:0060744; P:mammary gland branching involved in thelarche; IMP:MGI.
DR   GO; GO:0033147; P:negative regulation of estrogen receptor signaling pathway; IMP:MGI.
DR   GO; GO:0033600; P:negative regulation of mammary gland epithelial cell proliferation; IMP:MGI.
DR   GO; GO:0060762; P:regulation of branching involved in mammary gland duct morphogenesis; IMP:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR001107; Band_7.
DR   InterPro; IPR000163; Prohibitin.
DR   PANTHER; PTHR23222; Prohibitin; 1.
DR   Pfam; PF01145; Band_7; 1.
DR   PRINTS; PR00679; PROHIBITIN.
DR   SMART; SM00244; PHB; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Cytoplasm; Direct protein sequencing;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleus;
KW   Phosphoprotein; Receptor; Repressor; Transcription;
KW   Transcription regulation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    299       Prohibitin-2.
FT                                /FTId=PRO_0000213885.
FT   REGION       19     49       Necessary for transcriptional repression
FT                                (By similarity).
FT   REGION      150    174       Necessary for transcriptional repression
FT                                (By similarity).
FT   COILED      190    238       Potential.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     128    128       Phosphotyrosine (By similarity).
FT   MOD_RES     248    248       Phosphotyrosine (By similarity).
FT   MOD_RES     250    250       N6-acetyllysine (By similarity).
FT   CONFLICT     67     68       GL -> F (in Ref. 1; CAA55350).
FT   CONFLICT     81     81       Y -> N (in Ref. 6; AAC36528).
FT   CONFLICT    112    112       P -> L (in Ref. 6; AAC36528).
FT   CONFLICT    120    120       M -> I (in Ref. 6; AAC36528).
FT   CONFLICT    127    127       D -> G (in Ref. 6; AAC36528).
FT   CONFLICT    138    138       N -> S (in Ref. 6; AAC36528).
FT   CONFLICT    148    148       F -> V (in Ref. 6; AAC36528).
SQ   SEQUENCE   299 AA;  33296 MW;  A887CC982BF85C80 CRC64;
     MAQNLKDLAG RLPAGPRGMG TALKLLLGAG AVAYGVRESV FTVEGGHRAI FFNRIGGVQQ
     DTILAEGLHF RIPWFQYPII YDIRARPRKI SSPTGSKDLQ MVNISLRVLS RPNAQELPSM
     YQRLGLDYEE RVLPSIVNEV LKSVVAKFNA SQLITQRAQV SLLIRRELTE RAKDFSLILD
     DVAITELSFS REYTAAVEAK QVAQQEAQRA QFLVEKAKQE QRQKIVQAEG EAEAAKMLGE
     ALSKNPGYIK LRKIRAAQNI SKTIATSQNR IYLTADNLVL NLQDESFTRG SDSLIKGKK
//
ID   NCAM2_MOUSE             Reviewed;         837 AA.
AC   O35136; O35962; Q0VF23;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 102.
DE   RecName: Full=Neural cell adhesion molecule 2;
DE            Short=N-CAM-2;
DE            Short=NCAM-2;
DE   AltName: Full=Neural cell adhesion molecule RB-8;
DE   AltName: Full=R4B12;
DE   Flags: Precursor;
GN   Name=Ncam2; Synonyms=Ocam, Rncam;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RC   STRAIN=BALB/c; TISSUE=Olfactory neuroepithelium;
RX   MEDLINE=97368238; PubMed=9221781;
RA   Yoshihara Y., Kawasaki M., Tamada A., Fujita H., Hayashi H.,
RA   Kagamiyama H., Mori K.;
RT   "OCAM: a new member of the neural cell adhesion molecule family
RT   related to zone-to-zone projection of olfactory and vomeronasal
RT   axons.";
RL   J. Neurosci. 17:5830-5842(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RC   STRAIN=C57BL/6J; TISSUE=Olfactory epithelium;
RX   MEDLINE=97476194; PubMed=9334170; DOI=10.1074/jbc.272.42.26083;
RA   Alenius M., Bohm S.;
RT   "Identification of a novel neural cell adhesion molecule-related gene
RT   with a potential role in selective axonal projection.";
RL   J. Biol. Chem. 272:26083-26086(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-780, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: May play important roles in selective fasciculation and
CC       zone-to-zone projection of the primary olfactory axons.
CC   -!- SUBCELLULAR LOCATION: Isoform Long: Cell membrane; Single-pass
CC       type I membrane protein.
CC   -!- SUBCELLULAR LOCATION: Isoform Short: Cell membrane; Lipid-anchor,
CC       GPI-anchor.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=O35136-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=O35136-2; Sequence=VSP_002590;
CC         Note=GPI-anchored form;
CC   -!- TISSUE SPECIFICITY: Expressed in subsets of both olfactory and
CC       vomeronasal neurons in a zone-specific manner.
CC   -!- PTM: The GPI-anchor may be located on 'Asn-703' of isoform Short.
CC   -!- SIMILARITY: Contains 2 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 5 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF001287; AAB69125.1; -; mRNA.
DR   EMBL; AF001286; AAB69124.1; -; mRNA.
DR   EMBL; AF016619; AAC53375.1; -; mRNA.
DR   EMBL; BC119027; AAI19028.1; -; mRNA.
DR   EMBL; BC119029; AAI19030.1; -; mRNA.
DR   IPI; IPI00127556; -.
DR   IPI; IPI00322617; -.
DR   RefSeq; NP_001106679.1; NM_001113208.1.
DR   RefSeq; NP_035084.1; NM_010954.4.
DR   UniGene; Mm.433941; -.
DR   ProteinModelPortal; O35136; -.
DR   SMR; O35136; 19-689.
DR   MINT; MINT-1177341; -.
DR   STRING; O35136; -.
DR   PhosphoSite; O35136; -.
DR   PRIDE; O35136; -.
DR   Ensembl; ENSMUST00000037785; ENSMUSP00000049390; ENSMUSG00000022762.
DR   Ensembl; ENSMUST00000067602; ENSMUSP00000063468; ENSMUSG00000022762.
DR   GeneID; 17968; -.
DR   KEGG; mmu:17968; -.
DR   UCSC; uc007ztb.1; mouse.
DR   CTD; 17968; -.
DR   MGI; MGI:97282; Ncam2.
DR   eggNOG; roNOG09804; -.
DR   GeneTree; ENSGT00600000084036; -.
DR   HOGENOM; HBG444274; -.
DR   HOVERGEN; HBG052579; -.
DR   InParanoid; O35136; -.
DR   OMA; TWKIVRS; -.
DR   OrthoDB; EOG4MGS6S; -.
DR   NextBio; 292909; -.
DR   ArrayExpress; O35136; -.
DR   Bgee; O35136; -.
DR   CleanEx; MM_NCAM2; -.
DR   Genevestigator; O35136; -.
DR   GermOnline; ENSMUSG00000022762; Mus musculus.
DR   GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR009138; Neural_cell_adh.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 7.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07679; I-set; 5.
DR   PRINTS; PR01838; NCAMFAMILY.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00408; IGc2; 5.
DR   SUPFAM; SSF49265; FN_III-like; 2.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS50835; IG_LIKE; 5.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW   Glycoprotein; GPI-anchor; Immunoglobulin domain; Lipoprotein;
KW   Membrane; Phosphoprotein; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     19       Potential.
FT   CHAIN        20    837       Neural cell adhesion molecule 2.
FT                                /FTId=PRO_0000042589.
FT   TOPO_DOM     20    697       Extracellular (Potential).
FT   TRANSMEM    698    718       Helical; (Potential).
FT   TOPO_DOM    719    837       Cytoplasmic (Potential).
FT   DOMAIN       21    108       Ig-like C2-type 1.
FT   DOMAIN      113    202       Ig-like C2-type 2.
FT   DOMAIN      208    297       Ig-like C2-type 3.
FT   DOMAIN      302    396       Ig-like C2-type 4.
FT   DOMAIN      401    491       Ig-like C2-type 5.
FT   DOMAIN      496    588       Fibronectin type-III 1.
FT   DOMAIN      590    684       Fibronectin type-III 2.
FT   MOD_RES     780    780       Phosphothreonine.
FT   CARBOHYD    177    177       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    219    219       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    309    309       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    406    406       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    419    419       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    445    445       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    474    474       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    562    562       N-linked (GlcNAc...) (Potential).
FT   DISULFID     42     93       Probable.
FT   DISULFID    136    186       Probable.
FT   DISULFID    232    281       Probable.
FT   DISULFID    322    380       Probable.
FT   DISULFID    422    475       Probable.
FT   VAR_SEQ     694    837       TLFNGLGLGAIIGLGVAALLLILVVTDVSCFFIRQCGLLMC
FT                                ITRRMCGKKSGSSGKSKELEEGKAAYLKDGSKEPIVEMRTE
FT                                DERITNHEDGSPVNEPNETTPLTEPEKLPLKEENGKEVLNA
FT                                ETIEIKVSNDIIQSKEDDIKA -> NCCEANKGENGGQSWH
FT                                LNAVGFTFVITMSLSCLF (in isoform Short).
FT                                /FTId=VSP_002590.
SQ   SEQUENCE   837 AA;  93204 MW;  70473B053A2D65A5 CRC64;
     MSLLLSFYLL GLLVRSGQAL LQVTISLSKV ELSVGESKFF TCTAIGEPES IDWYNPQGEK
     IISTQRVMLQ KEGVRSRLTI YNANIEDAGI YRCQATDAKG QTQEATVVLE IYQKLTFREV
     VSPQEFKQGE DAEVVCRVSS SPAPAVSWLY HNEEVTTIPD NRFAVLANNN LQILNINKSD
     EGIYRCEGRV EARGEIDFRD IIVIVNVPPA IMMPQKSFNA TAERGEEMTL TCKASGSPDP
     TISWFRNGKL IEENEKYILK GSNTELTVRN IINKDGGSYV CKATNKAGED QKQAFLQVFV
     QPHILQLKNE TTSENGHVTL VCEAEGEPVP EITWKRAIDG VMFSEGDKSP DGRIEVKGQH
     GRSSLHIRDV KLSDSGRYDC EAASRIGGHQ RSMHLDIEYA PKFVSNQTMY YSWEGNPINI
     SCDVTANPPA SIHWRREKLL LPAKNTTHLK THSVGRKMIL EIAPTSDNDF GRYNCTATNR
     IGTRFQEYIL ELADVPSSPH GVKIIELSQT TAKISFNKPE SHGGVPIHHY QVDVKEVASE
     TWKIVRSHGV QTMVVLSSLE PNTTYEIRVA AVNGKGQGDY SKIEIFQTLP VREPSPPSIH
     GQPSSGKSFK ISITKQDDGG APILEYIVKY RSKDKEDQWL EKKVQGNKDH IILEHLQWTM
     GYEVQITAAN RLGYSEPTVY EFSMPPKPNI IKDTLFNGLG LGAIIGLGVA ALLLILVVTD
     VSCFFIRQCG LLMCITRRMC GKKSGSSGKS KELEEGKAAY LKDGSKEPIV EMRTEDERIT
     NHEDGSPVNE PNETTPLTEP EKLPLKEENG KEVLNAETIE IKVSNDIIQS KEDDIKA
//
ID   KCNS2_MOUSE             Reviewed;         477 AA.
AC   O35174; Q543P3;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Potassium voltage-gated channel subfamily S member 2;
DE   AltName: Full=Delayed-rectifier K(+) channel alpha subunit 2;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv9.2;
GN   Name=Kcns2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   MEDLINE=97450962; PubMed=9305895; DOI=10.1074/jbc.272.39.24371;
RA   Salinas M., Duprat F., Heurteaux C., Hugnot J.-P., Lazdunski M.;
RT   "New modulatory alpha subunits for mammalian Shab K+ channels.";
RL   J. Biol. Chem. 272:24371-24379(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Potassium channel subunit. Modulates channel activity
CC       and reduces the ion flow.
CC   -!- SUBUNIT: Heteromultimer with KCNB1 and with KCNB2. Does not form
CC       homomultimers. Might also bind to other channel proteins.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Note=May not reach the plasma membrane but remain in an
CC       intracellular compartment in the absence of KCNB1.
CC   -!- TISSUE SPECIFICITY: Detected in brain, but not in the other
CC       tissues tested. Expression was highest in the olfactory bulb,
CC       cerebral cortex, hippocampus, habenula, basolateral amygdaloid
CC       nuclei and cerebellum.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position.
CC   -!- SIMILARITY: Belongs to the potassium channel family. S
CC       (TC 1.A.1.2) subfamily. Kv9.2/KCNS2 sub-subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF008574; AAB72051.1; -; mRNA.
DR   EMBL; AK048819; BAC33468.1; -; mRNA.
DR   EMBL; AK087481; BAC39892.1; -; mRNA.
DR   EMBL; BC059833; AAH59833.1; -; mRNA.
DR   IPI; IPI00469995; -.
DR   RefSeq; NP_851834.1; NM_181317.3.
DR   UniGene; Mm.71045; -.
DR   ProteinModelPortal; O35174; -.
DR   SMR; O35174; 15-420.
DR   PhosphoSite; O35174; -.
DR   PRIDE; O35174; -.
DR   Ensembl; ENSMUST00000049742; ENSMUSP00000058773; ENSMUSG00000050963.
DR   Ensembl; ENSMUST00000072868; ENSMUSP00000072645; ENSMUSG00000050963.
DR   GeneID; 16539; -.
DR   KEGG; mmu:16539; -.
DR   UCSC; uc007vly.1; mouse.
DR   CTD; 16539; -.
DR   MGI; MGI:1197011; Kcns2.
DR   eggNOG; maNOG06122; -.
DR   HOVERGEN; HBG052230; -.
DR   InParanoid; O35174; -.
DR   OrthoDB; EOG405S10; -.
DR   NextBio; 289995; -.
DR   ArrayExpress; O35174; -.
DR   Bgee; O35174; -.
DR   CleanEx; MM_KCNS2; -.
DR   Genevestigator; O35174; -.
DR   GermOnline; ENSMUSG00000050963; Mus musculus.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003971; K_chnl_volt-dep_Kv9.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01494; KV9CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Ion transport; Ionic channel; Membrane; Potassium;
KW   Potassium channel; Potassium transport; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    477       Potassium voltage-gated channel subfamily
FT                                S member 2.
FT                                /FTId=PRO_0000054085.
FT   TOPO_DOM      1    187       Cytoplasmic (Potential).
FT   TRANSMEM    188    208       Helical; Name=Segment S1; (Potential).
FT   TOPO_DOM    209    232       Extracellular (Potential).
FT   TRANSMEM    233    253       Helical; Name=Segment S2; (Potential).
FT   TOPO_DOM    254    261       Cytoplasmic (Potential).
FT   TRANSMEM    262    282       Helical; Name=Segment S3; (Potential).
FT   TOPO_DOM    283    292       Extracellular (Potential).
FT   TRANSMEM    293    313       Helical; Name=Segment S4; (Potential).
FT   TOPO_DOM    314    328       Cytoplasmic (Potential).
FT   TRANSMEM    329    349       Helical; Name=Segment S5; (Potential).
FT   TOPO_DOM    350    361       Extracellular (Potential).
FT   INTRAMEM    362    382       Pore-forming; Name=Segment H5;
FT                                (Potential).
FT   TOPO_DOM    383    389       Extracellular (Potential).
FT   TRANSMEM    390    410       Helical; Name=Segment S6; (Potential).
FT   TOPO_DOM    411    477       Cytoplasmic (Potential).
FT   MOTIF       374    379       Selectivity filter (By similarity).
SQ   SEQUENCE   477 AA;  54289 MW;  C7AD7AA3AE312B2C CRC64;
     MTRQSLWDVS DTDVEDGEIR INVGGFKRRL RSHTLLRFPE TRLGRLLLCH SREAILELCD
     DYDDVQREFY FDRNPELFPY VLHFYHTGKL HVMAELCVFS FSQEIEYWGI NEFFIDSCCS
     YSYHGRKVEP EQEKWDEQSD QESTTSSFDE ILAFYNDASK FDGQPLGNFR RQLWLALDNP
     GYSVLSRVFS VLSILVVLGS IITMCLNSLP DFQIPDSQGN PGEDPRFEIV EHFGIAWFTF
     ELVARFAVAP DFLKFFKNAL NLIDLMSIVP FYITLVVNLV VESSPTLANL GRVAQVLRLM
     RIFRILKLAR HSTGLRSLGA TLKYSYKEVG LLLLYLSVGI SIFSVVAYTI EKEENEGLAT
     IPACWWWATV SMTTVGYGDV VPGTTAGKLT ASACILAGIL VVVLPITLIF NKFSHFYRRQ
     KQLESAMRSC DFGDGMKEVP SVNLRDYYAH KVKSLMASLT NMSRSSPSEL SLDDSLH
//
ID   X3CL1_MOUSE             Reviewed;         395 AA.
AC   O35188; O35933;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Fractalkine;
DE   AltName: Full=C-X3-C motif chemokine 1;
DE   AltName: Full=CX3C membrane-anchored chemokine;
DE   AltName: Full=Neurotactin;
DE   AltName: Full=Small-inducible cytokine D1;
DE   Contains:
DE     RecName: Full=Processed fractalkine;
DE   Flags: Precursor;
GN   Name=Cx3cl1; Synonyms=Cx3c, Fkn, Scyd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=97320499; PubMed=9177350; DOI=10.1038/42491;
RA   Pan Y., Lloyd C., Zhou H., Dolich S., Deeds J., Gonzalo J.-A.,
RA   Vath J., Gosselin M., Ma J., Dussault B., Woolf E., Alperin G.,
RA   Culpepper J., Gutierrez-Ramos J.-C., Gearing D.P.;
RT   "Neurotactin, a membrane-anchored chemokine upregulated in brain
RT   inflammation.";
RL   Nature 387:611-617(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=98140115; PubMed=9479488; DOI=10.1006/geno.1997.5058;
RA   Rossi D.L., Hardiman G., Copeland N.G., Gilbert D.J., Jenkins N.,
RA   Zlotnik A., Bazan J.F.;
RT   "Cloning and characterization of a new type of mouse chemokine.";
RL   Genomics 47:163-170(1998).
RN   [3]
RP   INDUCTION.
RX   MEDLINE=99059456; PubMed=9845323; DOI=10.1016/S0014-5793(98)01384-2;
RA   Schwaeble W.J., Stover C.M., Schall T.J., Dairaghi D.J.,
RA   Trinder P.K.E., Linington C., Iglesias A., Schubart A., Lynch N.J.,
RA   Weihe E., Schaefer M.K.-H.;
RT   "Neuronal expression of fractalkine in the presence and absence of
RT   inflammation.";
RL   FEBS Lett. 439:203-207(1998).
CC   -!- FUNCTION: Chemotactic for neutrophils both in vitro and in vivo.
CC       Results of chemotaxis assays suggest differential activation in
CC       vivo. The membrane-bound form promotes adhesion of leukocytes to
CC       endothelial cells (By similarity). May play a role in regulating
CC       leukocyte adhesion and migration processes at the endothelium (By
CC       similarity). Binds to CX3CR1.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- SUBCELLULAR LOCATION: Processed fractalkine: Secreted.
CC   -!- TISSUE SPECIFICITY: Highest levels in brain. Lower levels in
CC       kidney, heart and lung. Also found in skeletal muscle and testis.
CC   -!- PTM: A soluble short 95 kDa form may be released by proteolytic
CC       cleavage from the long membrane-anchored form.
CC   -!- SIMILARITY: Belongs to the intercrine delta family.
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DR   EMBL; AF010586; AAB66331.1; -; mRNA.
DR   EMBL; U92565; AAB71763.1; -; mRNA.
DR   IPI; IPI00127811; -.
DR   RefSeq; NP_033168.2; NM_009142.3.
DR   UniGene; Mm.103711; -.
DR   ProteinModelPortal; O35188; -.
DR   SMR; O35188; 25-100.
DR   STRING; O35188; -.
DR   PhosphoSite; O35188; -.
DR   PRIDE; O35188; -.
DR   Ensembl; ENSMUST00000034230; ENSMUSP00000034230; ENSMUSG00000031778.
DR   GeneID; 20312; -.
DR   KEGG; mmu:20312; -.
DR   CTD; 20312; -.
DR   MGI; MGI:1097153; Cx3cl1.
DR   eggNOG; roNOG08426; -.
DR   HOGENOM; HBG127109; -.
DR   HOVERGEN; HBG057269; -.
DR   InParanoid; O35188; -.
DR   OrthoDB; EOG415GDN; -.
DR   ArrayExpress; O35188; -.
DR   Bgee; O35188; -.
DR   CleanEx; MM_CX3CL1; -.
DR   Genevestigator; O35188; -.
DR   GermOnline; ENSMUSG00000031778; Mus musculus.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008009; F:chemokine activity; IDA:MGI.
DR   GO; GO:0060055; P:angiogenesis involved in wound healing; IMP:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IMP:MGI.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0048247; P:lymphocyte chemotaxis; IDA:MGI.
DR   GO; GO:0048246; P:macrophage chemotaxis; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptosis; IDA:MGI.
DR   GO; GO:0030593; P:neutrophil chemotaxis; IDA:MGI.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IMP:MGI.
DR   GO; GO:0032914; P:positive regulation of transforming growth factor-beta1 production; IMP:MGI.
DR   InterPro; IPR008097; Chemokine_fractalkine_CX3CL1.
DR   InterPro; IPR001811; Chemokine_IL8-like_dom.
DR   Pfam; PF00048; IL8; 1.
DR   PRINTS; PR01721; FRACTALKINE.
DR   SMART; SM00199; SCY; 1.
DR   SUPFAM; SSF54117; Chemokine_IL8; 1.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Cell membrane; Cytokine; Disulfide bond; Membrane;
KW   Secreted; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25    395       Fractalkine.
FT                                /FTId=PRO_0000005253.
FT   CHAIN        25   ?337       Processed fractalkine.
FT                                /FTId=PRO_0000296225.
FT   TOPO_DOM     25    336       Extracellular (Potential).
FT   TRANSMEM    337    357       Helical; (Potential).
FT   TOPO_DOM    358    395       Cytoplasmic (Potential).
FT   REGION       25    100       Chemokine.
FT   REGION      101    336       Mucin-like stalk.
FT   SITE        337    338       Cleavage; to produce soluble form
FT                                (Potential).
FT   DISULFID     32     58       By similarity.
FT   DISULFID     36     74       By similarity.
FT   CONFLICT     37     37       G -> D (in Ref. 1; AAB66331).
SQ   SEQUENCE   395 AA;  42041 MW;  1076320E3DAFA27C CRC64;
     MAPSPLAWLL RLAAFFHLCT LLPGQHLGMT KCEIMCGKMT SRIPVALLIR YQLNQESCGK
     RAIVLETTQH RRFCADPKEK WVQDAMKHLD HQAAALTKNG GKFEKRVDNV TPGITLATRG
     LSPSALTKPE SATLEDLALE LTTISQEARG TMGTSQEPPA AVTGSSLSTS EAQDAGLTAK
     PQSIGSFEAA DISTTVWPSP AVYQSGSSSW AEEKATESPS TTAPSPQVST TSPSTPEENV
     GSEGQPPWVQ GQDLSPEKSL GSEEINPVHT DNFQERGPGN TVHPSVAPIS SEETPSPELV
     ASGSQAPKIE EPIHATADPQ KLSVLITPVP DTQAATRRQA VGLLAFLGLL FCLGVAMFAY
     QSLQGCPRKM AGEMVEGLRY VPRSCGSNSY VLVPV
//
ID   KCNH2_MOUSE             Reviewed;        1162 AA.
AC   O35219; O35220; O35221; O35989;
DT   28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2002, sequence version 2.
DT   08-MAR-2011, entry version 102.
DE   RecName: Full=Potassium voltage-gated channel subfamily H member 2;
DE   AltName: Full=Ether-a-go-go-related gene potassium channel 1;
DE            Short=ERG-1;
DE            Short=Eag-related protein 1;
DE            Short=Ether-a-go-go-related protein 1;
DE            Short=MERG;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv11.1;
GN   Name=Kcnh2; Synonyms=Erg, Merg1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3), AND
RP   VARIANTS ARG-186; THR-455; TYR-752 AND ASN-1006.
RC   STRAIN=129/Sv, and BALB/c; TISSUE=Heart;
RX   MEDLINE=98012815; PubMed=9351462;
RA   London B., Trudeau M.C., Newton K.P., Beyer A.K., Copeland N.G.,
RA   Gilbert D.J., Jenkins N.A., Satler C.A., Robertson G.A.;
RT   "Two isoforms of the mouse ether-a-go-go-related gene coassemble to
RT   form channels with properties similar to the rapidly activating
RT   component of the cardiac delayed rectifier K+ current.";
RL   Circ. Res. 81:870-878(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Atrial tumor;
RX   MEDLINE=98012799; PubMed=9351446;
RA   Lees-Miller J.P., Kondo C., Wang L., Duff H.J.;
RT   "Electrophysiological characterization of an alternatively processed
RT   ERG K+ channel in mouse and human hearts.";
RL   Circ. Res. 81:719-726(1997).
CC   -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated inwardly
CC       rectifying potassium channel. Channel properties are modulated by
CC       cAMP and subunit assembly. Mediates the rapidly activating
CC       component of the delayed rectifying potassium current in heart
CC       (IKr) (By similarity).
CC   -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC       heterotetrameric complex of pore-forming alpha subunits that can
CC       associate with modulating beta subunits. Heteromultimer with
CC       KCNH6/ERG2, KCNH7/ERG3, KCNE1 and KCNE2. Interacts with ALG10B (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Experimental confirmation may be lacking for some
CC         isoforms;
CC       Name=1; Synonyms=1A, A;
CC         IsoId=O35219-1; Sequence=Displayed;
CC       Name=2; Synonyms=1A';
CC         IsoId=O35219-2; Sequence=VSP_000969;
CC       Name=3; Synonyms=1B, B;
CC         IsoId=O35219-3; Sequence=VSP_000970;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is expressed in heart, brain and
CC       testis and at low levels in lung. Isoform 3 is expressed
CC       predominantly in heart. The expression of isoform 2 is low in all
CC       tissues tested.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position.
CC   -!- PTM: Phosphorylated on serine and threonine residues (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the potassium channel family. H (Eag)
CC       (TC 1.A.1.20) subfamily. Kv11.1/KCNH2 sub-subfamily.
CC   -!- SIMILARITY: Contains 1 cyclic nucleotide-binding domain.
CC   -!- SIMILARITY: Contains 1 PAC (PAS-associated C-terminal) domain.
CC   -!- SIMILARITY: Contains 1 PAS (PER-ARNT-SIM) domain.
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DR   EMBL; AF012868; AAC53418.1; -; mRNA.
DR   EMBL; AF012869; AAC53419.1; -; mRNA.
DR   EMBL; AF012871; AAC53420.1; -; Genomic_DNA.
DR   EMBL; AF012870; AAC53420.1; JOINED; Genomic_DNA.
DR   EMBL; AF012871; AAC53421.1; -; Genomic_DNA.
DR   EMBL; AF012871; AAC53422.1; -; Genomic_DNA.
DR   EMBL; AF012870; AAC53422.1; JOINED; Genomic_DNA.
DR   EMBL; AF034762; AAB87571.1; -; mRNA.
DR   IPI; IPI00227779; -.
DR   IPI; IPI00314573; -.
DR   IPI; IPI00853663; -.
DR   UniGene; Mm.6539; -.
DR   ProteinModelPortal; O35219; -.
DR   SMR; O35219; 26-135, 572-666, 669-869.
DR   STRING; O35219; -.
DR   PhosphoSite; O35219; -.
DR   PRIDE; O35219; -.
DR   Ensembl; ENSMUST00000036092; ENSMUSP00000047705; ENSMUSG00000038319.
DR   Ensembl; ENSMUST00000115098; ENSMUSP00000110750; ENSMUSG00000038319.
DR   UCSC; uc008wrb.1; mouse.
DR   UCSC; uc008wrc.1; mouse.
DR   MGI; MGI:1341722; Kcnh2.
DR   eggNOG; roNOG14985; -.
DR   HOGENOM; HBG717083; -.
DR   HOVERGEN; HBG052232; -.
DR   InParanoid; O35219; -.
DR   OrthoDB; EOG4RJG0T; -.
DR   ArrayExpress; O35219; -.
DR   Bgee; O35219; -.
DR   Genevestigator; O35219; -.
DR   GermOnline; ENSMUSG00000038319; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0000155; F:two-component sensor activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR   InterPro; IPR003967; K_chnl_volt-dep_ERG.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PRINTS; PR01463; EAGCHANLFMLY.
DR   PRINTS; PR01470; ERGCHANNEL.
DR   SMART; SM00100; cNMP; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF51206; cNMP_binding; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; FALSE_NEG.
DR   PROSITE; PS00889; CNMP_BINDING_2; FALSE_NEG.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Ion transport; Ionic channel;
KW   Membrane; Phosphoprotein; Polymorphism; Potassium; Potassium channel;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN         1   1162       Potassium voltage-gated channel subfamily
FT                                H member 2.
FT                                /FTId=PRO_0000054000.
FT   TOPO_DOM      1    405       Cytoplasmic (Potential).
FT   TRANSMEM    406    426       Helical; Name=Segment S1; (Potential).
FT   TOPO_DOM    427    452       Extracellular (Potential).
FT   TRANSMEM    453    473       Helical; Name=Segment S2; (Potential).
FT   TOPO_DOM    474    497       Cytoplasmic (Potential).
FT   TRANSMEM    498    518       Helical; Name=Segment S3; (Potential).
FT   TOPO_DOM    519    522       Extracellular (Potential).
FT   TRANSMEM    523    543       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TOPO_DOM    544    549       Cytoplasmic (Potential).
FT   TRANSMEM    550    570       Helical; Name=Segment S5; (Potential).
FT   TOPO_DOM    571    613       Extracellular (Potential).
FT   INTRAMEM    614    634       Pore-forming; Name=Segment H5;
FT                                (Potential).
FT   TOPO_DOM    635    640       Extracellular (Potential).
FT   TRANSMEM    641    661       Helical; Name=Segment S6; (Potential).
FT   TOPO_DOM    662   1162       Cytoplasmic (Potential).
FT   DOMAIN       17     88       PAS.
FT   DOMAIN       92    144       PAC.
FT   NP_BIND     744    861       cNMP.
FT   MOTIF       626    631       Selectivity filter (By similarity).
FT   COMPBIAS    299    302       Poly-Pro.
FT   MOD_RES     322    322       Phosphoserine (By similarity).
FT   CARBOHYD    600    600       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1    378       MPVRRGHVAPQNTFLDTIIRKFEGQSRKFIIANARVENCAV
FT                                IYCNDGFCELCGYSRAEVMQRPCTCDFLHGPRTQRRAAAQI
FT                                AQALLGAEERKVEIAFYRKDGSCFLCLVDVVPVKNEDGAVI
FT                                MFILNFEVVMEKDMVGSPAHDTNHRGPSTSWLASGRAKTFR
FT                                LKLPALLALTARESSVRTGSMHSAGAPGAVVVDVDLTPAAP
FT                                SSESLALDEVSAMDNHVAGLGPAEERRALVGPGSASPVASI
FT                                RGPHPSPRAQSLNPDASGSSCSLARTRSRESCASVRRASSA
FT                                DDIEAMRAGALPPPPRHASTGAMHPLRSGLLNSTSDSDLVR
FT                                YRTISKIPQITLNFVDLKGDPFLASPTSDREIIAPKIKERT
FT                                HNVTEKVTQ -> MAIPTGKESRTGALQPRAQKGRVRRAVR
FT                                ISSLVAQE (in isoform 3).
FT                                /FTId=VSP_000970.
FT   VAR_SEQ       1     59       Missing (in isoform 2).
FT                                /FTId=VSP_000969.
FT   VARIANT     186    186       H -> R (in strain: BALB/c).
FT   VARIANT     455    455       A -> T (in strain: BALB/c).
FT   VARIANT     752    752       C -> Y (in strain: BALB/c).
FT   VARIANT    1006   1006       D -> N (in strain: BALB/c).
SQ   SEQUENCE   1162 AA;  126886 MW;  A9455F7F10B61E46 CRC64;
     MPVRRGHVAP QNTFLDTIIR KFEGQSRKFI IANARVENCA VIYCNDGFCE LCGYSRAEVM
     QRPCTCDFLH GPRTQRRAAA QIAQALLGAE ERKVEIAFYR KDGSCFLCLV DVVPVKNEDG
     AVIMFILNFE VVMEKDMVGS PAHDTNHRGP STSWLASGRA KTFRLKLPAL LALTARESSV
     RTGSMHSAGA PGAVVVDVDL TPAAPSSESL ALDEVSAMDN HVAGLGPAEE RRALVGPGSA
     SPVASIRGPH PSPRAQSLNP DASGSSCSLA RTRSRESCAS VRRASSADDI EAMRAGALPP
     PPRHASTGAM HPLRSGLLNS TSDSDLVRYR TISKIPQITL NFVDLKGDPF LASPTSDREI
     IAPKIKERTH NVTEKVTQVL SLGADVLPEY KLQAPRIHRW TILHYSPFKA VWDWLILLLV
     IYTAVFTPYS AAFLLKETED GSQAPDCGYA CQPLAVVDLI VDIMFIVDIL INFRTTYVNA
     NEEVVSHPGR IAVHYFKGWF LIDMVAAIPF DLLIFGSGSE ELIGLLKTAR LLRLVRVARK
     LDRYSEYGAA VLFLLMCTFA LIAHWLACIW YAIGNMEQPH MDSHIGWLHN LGDQIGKPYN
     SSGLGGPSIK DKYVTALYFT FSSLTSVGFG NVSPNTNSEK IFSICVMLIG SLMYASIFGN
     VSAIIQRLYS GTARYHTQML RVREFIRFHQ IPNPLRQRLE EYFQHAWSYT NGIDMNAVLK
     GFPECLQADI CLHLNRSLLQ HCKPFRGATK GCLRALAMKF KTTHAPPGDT LVHAGDLLTA
     LYFISRGSIE ILRGDVVVAI LGKNDIFGEP LNLYARPGKS NGDVRALTYC DLHKIHRDDL
     LEVLDMYPEF SDHFWSSLEI TFNLRDTNMI PGSPGSAELE SGFNRQRKRK LSFRRRTDKD
     TEQPGEVSAL GQGPARVGPG PSCRGQPGGP WGESPSSGPS SPESSEDEGP GRSSSPLRLV
     PFSSPRPPGD PPGGEPLTED GEKSDTCNPL SGAFSGVSNI FSFWGDSRGR QYQELPRCPA
     PAPSLLNIPL SSPGRRSRGD VESRLDALQR QLNRLETRLS ADMATVLQLL QRQMTLVPPA
     YSAVTTPGPG PTSASPLLPV GPVPTLTLDS LSQVSQFVAF EELPAGAPEL PQDGPTRRLS
     LPGQLGALTS QPLHRHGSDP GS
//
ID   PSMD4_MOUSE             Reviewed;         376 AA.
AC   O35226; Q91V59; Q9JJM0; Q9JJM1; Q9JJM2; Q9JJM3;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 4;
DE   AltName: Full=26S proteasome regulatory subunit RPN10;
DE   AltName: Full=26S proteasome regulatory subunit S5A;
DE   AltName: Full=Multiubiquitin chain-binding protein;
GN   Name=Psmd4; Synonyms=Mcb1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98172730; PubMed=9511739; DOI=10.1016/S0378-1119(97)00599-4;
RA   Pusch W., Jaehner D., Ivell R.;
RT   "Molecular cloning and testicular expression of the gene transcripts
RT   encoding the murine multiubiquitin-chain-binding protein (Mcb1).";
RL   Gene 207:19-24(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=129/SvJ; TISSUE=Embryo, and Testis;
RX   MEDLINE=20380947; PubMed=10921894; DOI=10.1093/emboj/19.15.4144;
RA   Kawahara H., Kasahara M., Nishiyama A., Ohsumi K., Goto T.,
RA   Kishimoto T., Saeki Y., Yokosawa H., Shimbara N., Murata S., Chiba T.,
RA   Suzuki K., Tanaka K.;
RT   "Developmentally regulated, alternative splicing of the Rpn10 gene
RT   generates multiple forms of 26S proteasomes.";
RL   EMBO J. 19:4144-4153(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE (ISOFORM RPN10B).
RA   Masumoto H., Lee H.-J., Tomioka M., Saido T.C.;
RT   "Molecular cloning of a multiubiquitin chain binding subunit of mouse
RT   26S proteasome.";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM RPN10B).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-250, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-250; THR-253 AND
RP   SER-256, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Binds and presumably selects ubiquitin-conjugates for
CC       destruction.
CC   -!- SUBUNIT: The 26S proteasome is composed of a core protease, known
CC       as the 20S proteasome, capped at one or both ends by the 19S
CC       regulatory complex (RC). The RC is composed of at least 18
CC       different subunits in two subcomplexes, the base and the lid,
CC       which form the portions proximal and distal to the 20S proteolytic
CC       core, respectively. Directly interacts with NUB1. Interacts with
CC       SQSTM1 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=Rpn10A;
CC         IsoId=O35226-1; Sequence=Displayed;
CC       Name=Rpn10B;
CC         IsoId=O35226-2; Sequence=VSP_005293;
CC       Name=Rpn10C;
CC         IsoId=O35226-3; Sequence=VSP_005293, VSP_005294, VSP_005295;
CC       Name=Rpn10D;
CC         IsoId=O35226-4; Sequence=VSP_005296, VSP_005297;
CC       Name=Rpn10E;
CC         IsoId=O35226-5; Sequence=VSP_005298, VSP_005299;
CC   -!- TISSUE SPECIFICITY: Isoform Rpn10A is ubiquitous whereas isoform
CC       Rpn10E is mostly expressed in the embryonic brain.
CC   -!- DEVELOPMENTAL STAGE: Isoform Rpn10E is expressed only in the
CC       embryos.
CC   -!- DOMAIN: The 2 UIM motifs are involved in the binding to a multi-
CC       ubiquitin chain in a cooperative way (By similarity).
CC   -!- SIMILARITY: Belongs to the proteasome subunit S5A family.
CC   -!- SIMILARITY: Contains 2 UIM (ubiquitin-interacting motif) repeats.
CC   -!- SIMILARITY: Contains 1 VWFA domain.
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DR   EMBL; AF013099; AAC53547.1; -; mRNA.
DR   EMBL; AB029090; BAA97572.1; -; Genomic_DNA.
DR   EMBL; AB029142; BAA97573.1; -; mRNA.
DR   EMBL; AB029143; BAA97574.1; -; mRNA.
DR   EMBL; AB029144; BAA97575.1; -; mRNA.
DR   EMBL; AB029145; BAA97576.1; -; mRNA.
DR   EMBL; AB029146; BAA97577.1; -; mRNA.
DR   EMBL; AF175574; AAG09199.1; -; mRNA.
DR   EMBL; BC009005; AAH09005.1; -; mRNA.
DR   IPI; IPI00128564; -.
DR   IPI; IPI00230569; -.
DR   IPI; IPI00230570; -.
DR   IPI; IPI00345779; -.
DR   IPI; IPI00381291; -.
DR   PIR; JC6535; JC6535.
DR   RefSeq; NP_032977.1; NM_008951.1.
DR   UniGene; Mm.2261; -.
DR   ProteinModelPortal; O35226; -.
DR   SMR; O35226; 196-305.
DR   MINT; MINT-2841145; -.
DR   STRING; O35226; -.
DR   PhosphoSite; O35226; -.
DR   REPRODUCTION-2DPAGE; IPI00345779; -.
DR   PRIDE; O35226; -.
DR   Ensembl; ENSMUST00000071664; ENSMUSP00000071589; ENSMUSG00000005625.
DR   Ensembl; ENSMUST00000107237; ENSMUSP00000102857; ENSMUSG00000005625.
DR   GeneID; 19185; -.
DR   KEGG; mmu:19185; -.
DR   UCSC; uc008qhr.1; mouse.
DR   UCSC; uc008qht.1; mouse.
DR   UCSC; uc008qhu.1; mouse.
DR   UCSC; uc008qhv.1; mouse.
DR   CTD; 19185; -.
DR   MGI; MGI:1201670; Psmd4.
DR   eggNOG; roNOG14618; -.
DR   HOVERGEN; HBG000425; -.
DR   OMA; QCKLRAN; -.
DR   OrthoDB; EOG4JQ3Z0; -.
DR   PhylomeDB; O35226; -.
DR   NextBio; 295886; -.
DR   ArrayExpress; O35226; -.
DR   Bgee; O35226; -.
DR   Genevestigator; O35226; -.
DR   GermOnline; ENSMUSG00000005625; Mus musculus.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   InterPro; IPR007198; Ssl1-like.
DR   InterPro; IPR003903; Ubiquitin-int_motif.
DR   InterPro; IPR002035; VWF_A.
DR   Pfam; PF04056; Ssl1; 1.
DR   Pfam; PF02809; UIM; 2.
DR   SMART; SM00726; UIM; 2.
DR   SMART; SM00327; VWA; 1.
DR   PROSITE; PS50330; UIM; 2.
DR   PROSITE; PS50234; VWFA; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein; Proteasome; Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    376       26S proteasome non-ATPase regulatory
FT                                subunit 4.
FT                                /FTId=PRO_0000173829.
FT   DOMAIN        5    188       VWFA.
FT   REPEAT      211    230       UIM 1.
FT   REPEAT      282    301       UIM 2.
FT   COMPBIAS    238    246       Poly-Ala.
FT   MOD_RES     250    250       Phosphothreonine.
FT   MOD_RES     253    253       Phosphothreonine.
FT   MOD_RES     256    256       Phosphoserine.
FT   MOD_RES     360    360       Phosphoserine (By similarity).
FT   VAR_SEQ     254    254       E -> EGER (in isoform Rpn10B and isoform
FT                                Rpn10C).
FT                                /FTId=VSP_005293.
FT   VAR_SEQ     255    260       DSDDAL -> GERGGF (in isoform Rpn10E).
FT                                /FTId=VSP_005298.
FT   VAR_SEQ     261    376       Missing (in isoform Rpn10E).
FT                                /FTId=VSP_005299.
FT   VAR_SEQ     299    349       EFSQESADMDASSAMDTSDPVKEEDDYDVMQDPEFLQSVLE
FT                                NLPGVDPNNA -> GGPWLGWQGLDRVWGEELALSGLLLSF
FT                                PQSLAKNRLTWMPAQPWTHLIQSR (in isoform
FT                                Rpn10D).
FT                                /FTId=VSP_005296.
FT   VAR_SEQ     321    365       EEDDYDVMQDPEFLQSVLENLPGVDPNNAAIRSVMGALASQ
FT                                ATKD -> VRASSEALTQPSLTSPAFRSLSFWDQGLSSLAF
FT                                HKKGLGATEGNT (in isoform Rpn10C).
FT                                /FTId=VSP_005294.
FT   VAR_SEQ     350    376       Missing (in isoform Rpn10D).
FT                                /FTId=VSP_005297.
FT   VAR_SEQ     366    376       Missing (in isoform Rpn10C).
FT                                /FTId=VSP_005295.
SQ   SEQUENCE   376 AA;  40704 MW;  732AC02B56760EAA CRC64;
     MVLESTMVCV DNSEYMRNGD FLPTRLQAQQ DAVNIVCHSK TRSNPENNVG LITLANDCEV
     LTTLTPDTGR ILSKLHTVQP KGKITFCTGI RVAHLALKHR QGKNHKMRII AFVGSPVEDN
     EKDLVKLAKR LKKEKVNVDI INFGEEEVNT EKLTAFVNTL NGKDGTGSHL VTVPPGPSLA
     DALISSPILA GEGGAMLGLG ASDFEFGVDP SADPELALAL RVSMEEQRQR QEEEARRAAA
     ASAAEAGIAT PGTEDSDDAL LKMTINQQEF GRPGLPDLSS MTEEEQIAYA MQMSLQGTEF
     SQESADMDAS SAMDTSDPVK EEDDYDVMQD PEFLQSVLEN LPGVDPNNAA IRSVMGALAS
     QATKDGKNDK KEEEKK
//
ID   PTN9_MOUSE              Reviewed;         593 AA.
AC   O35239; Q7TSK0;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type 9;
DE            EC=3.1.3.48;
DE   AltName: Full=Protein-tyrosine phosphatase MEG2;
DE            Short=PTPase MEG2;
GN   Name=Ptpn9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Meng K., Gu M., Li F.N., Veile R.A., Donis-Keller H., Majerus P.W.;
RT   "MPTP-MEG2.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Protein-tyrosine phosphatase that could participate in
CC       the transfer of hydrophobic ligands or in functions of the Golgi
CC       apparatus (By similarity).
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class 3 subfamily.
CC   -!- SIMILARITY: Contains 1 CRAL-TRIO domain.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
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DR   EMBL; AF013490; AAB66898.1; -; mRNA.
DR   EMBL; BC053017; AAH53017.1; -; mRNA.
DR   IPI; IPI00128608; -.
DR   RefSeq; NP_062625.2; NM_019651.2.
DR   UniGene; Mm.325643; -.
DR   ProteinModelPortal; O35239; -.
DR   SMR; O35239; 7-583.
DR   PhosphoSite; O35239; -.
DR   PRIDE; O35239; -.
DR   Ensembl; ENSMUST00000034832; ENSMUSP00000034832; ENSMUSG00000032290.
DR   GeneID; 56294; -.
DR   KEGG; mmu:56294; -.
DR   UCSC; uc009ptt.1; mouse.
DR   CTD; 56294; -.
DR   MGI; MGI:1928376; Ptpn9.
DR   eggNOG; roNOG05060; -.
DR   HOGENOM; HBG445850; -.
DR   HOVERGEN; HBG006880; -.
DR   InParanoid; O35239; -.
DR   OMA; EGGRRKC; -.
DR   OrthoDB; EOG4DJJW7; -.
DR   PhylomeDB; O35239; -.
DR   BRENDA; 3.1.3.48; 244.
DR   NextBio; 312208; -.
DR   ArrayExpress; O35239; -.
DR   Bgee; O35239; -.
DR   CleanEx; MM_PTPN9; -.
DR   Genevestigator; O35239; -.
DR   GermOnline; ENSMUSG00000032290; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   InterPro; IPR001251; CRAL-bd_TRIO_C.
DR   InterPro; IPR011074; Sec14p-like_N.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Gene3D; G3DSA:3.40.525.10; CRAL_bd_TRIO_C; 1.
DR   Pfam; PF00650; CRAL_TRIO; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SUPFAM; SSF52087; CRAL_TRIO_C; 1.
DR   SUPFAM; SSF46938; Sec14p_like_N; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Hydrolase; Protein phosphatase.
FT   CHAIN         1    593       Tyrosine-protein phosphatase non-receptor
FT                                type 9.
FT                                /FTId=PRO_0000094765.
FT   DOMAIN       84    243       CRAL-TRIO.
FT   DOMAIN      303    574       Tyrosine-protein phosphatase.
FT   ACT_SITE    515    515       Phosphocysteine intermediate (By
FT                                similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   CONFLICT    190    190       G -> R (in Ref. 1; AAB66898).
FT   CONFLICT    215    215       Q -> P (in Ref. 1; AAB66898).
FT   CONFLICT    218    218       K -> T (in Ref. 1; AAB66898).
FT   CONFLICT    233    233       E -> K (in Ref. 1; AAB66898).
FT   CONFLICT    277    278       SV -> TL (in Ref. 1; AAB66898).
FT   CONFLICT    282    285       GPHA -> SPLS (in Ref. 1; AAB66898).
FT   CONFLICT    311    312       RR -> CL (in Ref. 1; AAB66898).
FT   CONFLICT    321    322       CS -> RT (in Ref. 1; AAB66898).
FT   CONFLICT    326    326       G -> R (in Ref. 1; AAB66898).
FT   CONFLICT    373    373       I -> N (in Ref. 1; AAB66898).
FT   CONFLICT    498    498       L -> M (in Ref. 1; AAB66898).
FT   CONFLICT    545    545       Q -> H (in Ref. 1; AAB66898).
FT   CONFLICT    576    579       EREG -> QKER (in Ref. 1; AAB66898).
SQ   SEQUENCE   593 AA;  67970 MW;  053451BCD9DC7C61 CRC64;
     MEPATAPRPD MAPELTPEEE QATKQFLEEI NKWTVQYNVS PLSWNVAVKF LMARKFDVLR
     AVELFHCYRE TRRKEGIVKL KPHEEPLRSE ILSGKFTILN VRDPTGASIA LFTARLHHPH
     KSAQHVVLQA LFYLLDRAVD SFETQRNGLV FIYDMCGSNY ANFELDLGKK VLNLLKGAFP
     ARLKKVLIVG APIWFRVPYS IISLLLKDKV RERIQILKTS EVTQHLPREC LPENLGGYVK
     IDLATWNFQF LPQVNGHPDP FDEIILSSLP PALDWDSVHV PGPHAMTIQE LVDYVNTRQK
     RGIYEEYEDI RRENPVGTFH CSMSPGNLEK NRYGDVPCLD QTRVKLTKRS GHTQTDYINA
     SFMDGYKQKN AYIGTQGPLE NTYRDFWLMV WEQKVLVIVM TTRFEEGGRR KCGQYWPLEK
     DSRIRFGFLT VTNLGVENMN HYKKTTLEIH NTEERQKRQV THFQFLSWPD YGVPSSAASL
     IDFLRVVRNQ QSMAVGNLGA RSKGQCPEPP IVVHCSAGIG RTGTFCSLDI CLAQLEELGT
     LNVFQTVSRM RTQRAFSIQT PEQYYFCYKA ILEFAEREGM VPSGHSLLAM DGQ
//
ID   O35243_MOUSE            Unreviewed;      1567 AA.
AC   O35243;
DT   01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 50.
DE   SubName: Full=Antigen containing epitope to monoclonal antibody MMS-85/12;
DE   Flags: Fragment;
GN   Name=Bod1l; Synonyms=AF013969;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=96115977; PubMed=8686505;
RA   Benayahu D., Efrati M., Wientroub S.;
RT   "Monoclonal antibodies recognize antigen expressed by osteoblasts.";
RL   J. Bone Miner. Res. 10:1496-1503(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Fisher L.W., Merrelli A., Benayahu D.;
RT   "Clone containing epitope to mouse osteoblast monoclonal antibody MMS-
RT   85/12.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AF013969; AAB69856.1; -; mRNA.
DR   IPI; IPI00753321; -.
DR   PIR; T03730; T03730.
DR   RefSeq; NP_001074891.1; NM_001081422.2.
DR   UniGene; Mm.158726; -.
DR   Ensembl; ENSMUST00000050556; ENSMUSP00000058618; ENSMUSG00000061755.
DR   GeneID; 665775; -.
DR   KEGG; mmu:665775; -.
DR   CTD; 665775; -.
DR   MGI; MGI:2444804; Bod1l.
DR   eggNOG; roNOG08381; -.
DR   InParanoid; O35243; -.
DR   OrthoDB; EOG40ZQWP; -.
DR   ArrayExpress; O35243; -.
DR   Bgee; O35243; -.
DR   Genevestigator; O35243; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR   SMART; SM00384; AT_hook; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   1567 AA;  164900 MW;  DF40D0365A151CB0 CRC64;
     PVNSRPPVPQ QRHGKMERGA AGSGRRDKAF IATSTEGTDK GIMLNTVKTG DATTTSSEVG
     EKGTALPCTS IEADEGFMMG ACPKKHPLQV GAEASECTVF AAAEEGKGVV TEGFAESEIL
     LTSSKEGESG ECAVAESEDR VAGPLAAHTV QAEANVNSIT TEEKDDAVTS AGSEEKCGGS
     ACTVEGTATF IGEVESDGAV TSAGTEIRAG SLSSEDVDGS QENRIQVGPK KETEGTVTCT
     ETKGRNDNFI CLVTRVETQE QRVVTGADVV QVNAAKPQEA NANQGDGSGT DGAEGESAVT
     STGITEEDGE ASANCTGSED NREGCAISSE TEESAESAMD STEAKALTNA PLVAAGPCDD
     EGIVTSTGAK EEDDEDEGVV TSTGRGNEPG HASACTGIEE SEGMMVCESG EGGAQIGPTI
     DHVNAEAGAA TVNTNDSNVD SMSGAEKEIK DTNICSSAKG IVESSVTSAL AGNSDRPPVL
     CGSEGPMASA SSHHSDSQLT RKETVEDTTI STGLVKGSDD VLVSGEVPEC EVGHMSPRKN
     EECDGLMAST AGCDVSNKDS LAGSKSQGNG LMISTSTNAC TPQISAVIDV RGGHLSTLST
     EEIRDGVRVH REGFEAPMPS AVSGENSQLT ASRSEEKDEC AMISTSIGEE FELPISSAVT
     VTCAERQQPV AAVEESTTGP ALVSTEDFEV PMPSAPTEAE SPLASTSKEE KDECALISTS
     IAEECEASVF GVSRNAPSVT DGNAVISTSS VEDCEGSVSS AVPQESVCPS VIPVEETGDT
     AMISTSTSEG REAVMVGTIP TDDDQATTVR GEDLSDAAII STSTAECVLT CTSLSRHEEN
     QQATHNPEGN GGHLATKQSK CELPMPSLVA ERNCKCPGPF RMGKGVGPLM AVGTRGEHDR
     LPVCEPSVGQ GQPGTALCLG EEESHGMDCP GQDLNAKERN TLLSSVQRES KSAEAEAAGD
     SSTARRTVRK DSERNANSLS ETNCLREPEQ KPAEDTSGST HCLTAVNPGA EADGMLPITH
     AALEYPDHQE PESNLKTTTK CITGQESQMP SSHTGVLSAV CHVAPCASEQ EGGLPTKSDH
     SGTWTSEGSP EKMGHVAGAR QSFHREGNLD VTLPPEDNGC GVGNEESPPK GIGGLELSTG
     LTTEISVSSE EDTSHGVVAA PENPCVGRRR GAAELQMEAL LMRESLNVEK SESRINEEIH
     FESQNKEEIC CGRKGSTEAL SGCSVEADPE EVEEEEKQIS QRNRKPDYSS SEEELDDSPD
     VLDSRIETAQ RQYSETEPHD TKEENSGDVE EFSSVTSKTN SSTGLEDRDE FSSSEGTGEK
     TEPNEDDGSI KSQEDDHPII IKRRRGRPRK YPAETAFKSK EDSKTETDIT TVEQSSPSGK
     LKVSQADESN KEIANLEEKS TSNDDSEEKT ASMRLRGRKP KRSLTSSDDA ESSEPERKRQ
     KSVSETSEDK KDEESDEEEE EEEEEEPLGA TTRSATRSEA QRKNHSKPST RATSKLGIPE
     TISPRNRQKL AKEKLSTSEK VSKSPPLGRS KAQLSPSVKR KREVSPPGAR TRGQQKVDEN
     PLKKAKR
//
ID   EXOC7_MOUSE             Reviewed;         697 AA.
AC   O35250; Q8K121;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2002, sequence version 2.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Exocyst complex component 7;
DE   AltName: Full=Exocyst complex component Exo70;
GN   Name=Exoc7; Synonyms=Exo70;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RA   Guo W., Roth D., De Camilli P., Novick P.;
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH ARHQ.
RX   MEDLINE=22573538; PubMed=12687004; DOI=10.1038/nature01533;
RA   Inoue M., Chang L., Hwang J., Chiang S.-H., Saltiel A.R.;
RT   "The exocyst complex is required for targeting of Glut4 to the plasma
RT   membrane by insulin.";
RL   Nature 422:629-633(2003).
CC   -!- FUNCTION: Component of the exocyst complex involved in the docking
CC       of exocystic vesicles with fusion sites on the plasma membrane. In
CC       adipocytes, plays a crucial role in targeting SLC2A4 vesicle to
CC       the plasma membrane in response to insulin, perhaps directing the
CC       vesicle to the precise site of fusion.
CC   -!- SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3,
CC       EXOC4, EXOC5, EXOC6, EXOC7 and EXOC8. Interacts with RAB11FIP3 (By
CC       similarity). Interacts with ARHQ in a GTP-dependent manner.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane;
CC       Peripheral membrane protein. Note=Translocates, as a preformed
CC       complex with SEC6 and SEC8, to the plasma membrane in response to
CC       insulin through the activation of ARHQ.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O35250-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O35250-2; Sequence=VSP_001484, VSP_001485;
CC   -!- DOMAIN: The C-terminus is required for translocation to the plasma
CC       membrane.
CC   -!- SIMILARITY: Belongs to the EXO70 family.
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DR   EMBL; AF014461; AAB69345.1; -; mRNA.
DR   EMBL; BC028927; AAH28927.1; -; mRNA.
DR   IPI; IPI00227970; -.
DR   IPI; IPI00316650; -.
DR   PIR; T03722; T03722.
DR   RefSeq; NP_001156344.1; NM_001162872.1.
DR   RefSeq; NP_058553.2; NM_016857.2.
DR   UniGene; Mm.22530; -.
DR   PDB; 2PFT; X-ray; 2.25 A; A=85-697.
DR   PDBsum; 2PFT; -.
DR   ProteinModelPortal; O35250; -.
DR   SMR; O35250; 85-696.
DR   MINT; MINT-1897779; -.
DR   STRING; O35250; -.
DR   PhosphoSite; O35250; -.
DR   PRIDE; O35250; -.
DR   Ensembl; ENSMUST00000021147; ENSMUSP00000021147; ENSMUSG00000020792.
DR   Ensembl; ENSMUST00000106411; ENSMUSP00000102019; ENSMUSG00000020792.
DR   GeneID; 53413; -.
DR   KEGG; mmu:53413; -.
DR   CTD; 53413; -.
DR   MGI; MGI:1859270; Exoc7.
DR   HOGENOM; HBG715163; -.
DR   HOVERGEN; HBG051515; -.
DR   InParanoid; O35250; -.
DR   OMA; PTKKPIK; -.
DR   OrthoDB; EOG4NGGM7; -.
DR   PhylomeDB; O35250; -.
DR   NextBio; 310225; -.
DR   ArrayExpress; O35250; -.
DR   Bgee; O35250; -.
DR   CleanEx; MM_EXOC7; -.
DR   Genevestigator; O35250; -.
DR   GermOnline; ENSMUSG00000020792; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0000145; C:exocyst; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR016159; Cullin_repeat-like_dom.
DR   InterPro; IPR004140; Exo70.
DR   PANTHER; PTHR12542; Exo70; 1.
DR   Pfam; PF03081; Exo70; 1.
DR   SUPFAM; SSF74788; Cullin_repeat-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Coiled coil;
KW   Cytoplasm; Exocytosis; Membrane; Phosphoprotein; Protein transport;
KW   Transport.
FT   CHAIN         1    697       Exocyst complex component 7.
FT                                /FTId=PRO_0000118961.
FT   REGION        1    384       SEC8 and ARHQ binding.
FT   COILED        5     42       Potential.
FT   COILED       63     85       Potential.
FT   MOD_RES     250    250       Phosphoserine (By similarity).
FT   VAR_SEQ     270    300       Missing (in isoform 2).
FT                                /FTId=VSP_001484.
FT   VAR_SEQ     477    489       Missing (in isoform 2).
FT                                /FTId=VSP_001485.
FT   CONFLICT     40     40       R -> K (in Ref. 1; AAB69345).
FT   CONFLICT    165    165       V -> I (in Ref. 1; AAB69345).
FT   CONFLICT    433    433       K -> E (in Ref. 1; AAB69345).
FT   CONFLICT    529    529       Y -> F (in Ref. 1; AAB69345).
FT   CONFLICT    610    611       ER -> DP (in Ref. 1; AAB69345).
FT   HELIX        89     91
FT   HELIX        93    103
FT   HELIX       109    129
FT   HELIX       134    161
FT   HELIX       167    176
FT   HELIX       193    209
FT   HELIX       214    240
FT   HELIX       307    334
FT   HELIX       337    339
FT   HELIX       340    371
FT   TURN        377    380
FT   HELIX       381    398
FT   TURN        399    401
FT   HELIX       404    407
FT   HELIX       409    434
FT   HELIX       439    441
FT   HELIX       450    464
FT   HELIX       466    474
FT   HELIX       500    526
FT   HELIX       532    547
FT   TURN        548    552
FT   HELIX       555    560
FT   HELIX       566    582
FT   HELIX       583    585
FT   HELIX       586    589
FT   TURN        590    592
FT   HELIX       594    596
FT   HELIX       608    632
FT   HELIX       640    666
FT   HELIX       674    677
FT   HELIX       682    690
FT   STRAND      692    694
SQ   SEQUENCE   697 AA;  79960 MW;  0A78F00E1D5D575A CRC64;
     MIPPQEASAR RREIEDKLKQ EEETLSFIRD SLEKSDQLTR NMVSILSSFE SRLMKLENSI
     IPVHKQTENL QRLQENVEKT LSCLDHVISY YHVASDTEKI IREGPTGRLE EYLGSMAKIQ
     KAVEYFQDNS PDSPELNKVK LLFERGKESL ESEFRSLMTR HSKVVSPVLL LDLISADDEL
     EVQEDVVLEH LPESVLRDVV RISRWLVEYG RNQDFMNVYY QIRSSQLDRS IKGLKEHFRK
     SSSSSGVPYS PAIPNKRKDT PTKKPIKRPG TIRKAQNLLK QYSQHGLDGK KGGSNLIPLE
     GRDDMLDVET DAYIHCVSAF VKLAQSEYRL LMEIIPEHHQ KKTFDSLIQD ALDGLMLEGE
     NIVSAARKAI IRHDFSTVLT VFPILRHLKQ TKPEFDQVLQ GTAASTKNKL PGLITSMETI
     GAKALEDFAD NIKNDPDKEY NMPKDGTVHE LTSNAILFLQ QLLDFQETAG AMLASQVLGD
     TYNIPLDPRE TSSSATSYSS EFSKRLLSTY ICKVLGNLQL NLLSKSKVYE DPALSAIFLH
     NNYNYILKSL EKSELIQLVA VTQKTAERSY REHIEQQIQT YQRSWLKVTD YIAEKNLPVF
     QPGVKLRDKE RQMIKERFKG FNDGLEELCK IQKVWAIPDT EQRDKIRQAQ KDIVKETYGA
     FLHRYGSVPF TKNPEKYIKY RVEQVGDMID RLFDTSA
//
ID   DHX15_MOUSE             Reviewed;         795 AA.
AC   O35286; Q99L91;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2003, sequence version 2.
DT   08-MAR-2011, entry version 103.
DE   RecName: Full=Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX15;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAH box protein 15;
GN   Name=Dhx15; Synonyms=Ddx15, Deah9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98004479; PubMed=9342318; DOI=10.1073/pnas.94.22.11803;
RA   Gee S., Krauss S.W., Miller E., Aoyagi K., Arenas J., Conboy J.G.;
RT   "Cloning of mDEAH9, a putative RNA helicase and mammalian homologue of
RT   Saccharomyces cerevisiae splicing factor Prp43.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:11803-11807(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Pre-mRNA processing factor involved in disassembly of
CC       spliceosomes after the release of mature mRNA (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Interacts with SSB/La. Component of the U11/U12 snRNPs
CC       that are part of the U12-type spliceosome (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily. DDX15/PRP43 sub-subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BC003745; Type=Frameshift; Positions=409;
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DR   EMBL; AF017153; AAC36129.1; -; mRNA.
DR   EMBL; BC003745; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00128818; -.
DR   RefSeq; NP_031865.2; NM_007839.2.
DR   UniGene; Mm.993; -.
DR   ProteinModelPortal; O35286; -.
DR   SMR; O35286; 115-787.
DR   STRING; O35286; -.
DR   PhosphoSite; O35286; -.
DR   PRIDE; O35286; -.
DR   Ensembl; ENSMUST00000031061; ENSMUSP00000031061; ENSMUSG00000029169.
DR   GeneID; 13204; -.
DR   KEGG; mmu:13204; -.
DR   UCSC; uc008xkf.1; mouse.
DR   CTD; 13204; -.
DR   MGI; MGI:1099786; Dhx15.
DR   eggNOG; roNOG05128; -.
DR   HOGENOM; HBG757997; -.
DR   HOVERGEN; HBG039428; -.
DR   InParanoid; O35286; -.
DR   OMA; VIYNEFV; -.
DR   OrthoDB; EOG4K6G3N; -.
DR   PhylomeDB; O35286; -.
DR   NextBio; 283358; -.
DR   ArrayExpress; O35286; -.
DR   Bgee; O35286; -.
DR   CleanEx; MM_DHX15; -.
DR   Genevestigator; O35286; -.
DR   GermOnline; ENSMUSG00000029169; Mus musculus.
DR   GO; GO:0005689; C:U12-type spliceosomal complex; ISS:HGNC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR011709; DUF1605.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF07717; DUF1605; 1.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Helicase; Hydrolase; mRNA processing;
KW   mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein.
FT   CHAIN         1    795       Putative pre-mRNA-splicing factor ATP-
FT                                dependent RNA helicase DHX15.
FT                                /FTId=PRO_0000055140.
FT   DOMAIN      147    313       Helicase ATP-binding.
FT   DOMAIN      338    518       Helicase C-terminal.
FT   NP_BIND     160    167       ATP (By similarity).
FT   MOTIF       260    263       DEAH box.
FT   COMPBIAS    346    349       Poly-Glu.
FT   COMPBIAS    395    398       Poly-Gln.
FT   COMPBIAS    403    406       Poly-Pro.
FT   MOD_RES      15     15       Phosphoserine (By similarity).
FT   MOD_RES     132    132       N6-acetyllysine (By similarity).
FT   MOD_RES     476    476       Phosphothreonine (By similarity).
FT   MOD_RES     488    488       N6-acetyllysine (By similarity).
FT   CONFLICT    388    389       LY -> FS (in Ref. 1).
FT   CONFLICT    391    393       TLP -> YTS (in Ref. 1).
FT   CONFLICT    757    758       WL -> CW (in Ref. 1).
FT   CONFLICT    759    795       Missing (in Ref. 1).
SQ   SEQUENCE   795 AA;  91007 MW;  25A97254318E497A CRC64;
     MSKRHRLDLG EDYPSGKKRA GTDGKDRERD RDREDRSKDR DRERDRGDRE REREKEKEKE
     LRASTNAMLI SAGLPPLKAS HSAHSTHSAH STHSTHSAHS THTGHTGHTS LPQCINPFTN
     LPHTPRYYDI LKKRLQLPVW EYKDRFTDIL VRHQSFVLVG ETGSGKTTQI PQWCVEYMRS
     LPGPKRGVAC TQPRRVAAMS VAQRVADEMD VMLGQEVGYS IRFEDCSSAK TILKYMTDGM
     LLREAMNDPL LERYGVIILD EAHERTLATD ILMGVLKEVV RQRSDLKVIV MSATLDAGKF
     QIYFDNCPLL TIPGRTHPVE IFYTPEPERD YLEAAIRTVI QIHMCEEEEG DLLLFLTGQE
     EIDEACKRIK REVDDLGPEV GDIKIIPLYS TLPPQQQQRI FEPPPPKKQN GAIGRKVVVS
     TNIAETSLTI DGVVFVIDPG FAKQKVYNPR IRVESLLVTA ISKASAQQRA GRAGRTRPGK
     CFRLYTEKAY KTEMQDNTYP EILRSNLGSV VLQLKKLGID DLVHFDFMDP PAPETLMRAL
     ELLNYLAALN DDGDLTELGS MMAEFPLDPQ LAKMVIASCD YNCSNEVLSI TAMLSVPQCF
     VRPTEAKKAA DEAKMRFAHI DGDHLTLLNV YHAFKQNHES VQWCYDNFIN YRSLMSADNV
     RQQLSRIMDR FNLPRRSTDF TSRDYYINIR KALVTGYFMQ VAHLERTGHY LTVKDNQVVQ
     LHPSTVLDHK PEWVLYNEFV LTTKNYIRTC TDIKPEWLVK IAPQYYDMSN FPQCEAKRQL
     DRIIAKLQSK EYSQY
//
ID   PURB_MOUSE              Reviewed;         324 AA.
AC   O35295;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Transcriptional activator protein Pur-beta;
DE   AltName: Full=Purine-rich element-binding protein B;
DE   AltName: Full=Vascular actin single-stranded DNA-binding factor 2 p44 component;
GN   Name=Purb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=C57BL/6 X CBA; TISSUE=Lung;
RX   MEDLINE=97476282; PubMed=9334258; DOI=10.1074/jbc.272.42.26727;
RA   Kelm R.J. Jr., Elder P.K., Strauch A.R., Getz M.J.;
RT   "Sequence of cDNAs encoding components of vascular actin single-
RT   stranded DNA-binding factor 2 establish identity to Puralpha and
RT   Purbeta.";
RL   J. Biol. Chem. 272:26727-26733(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   PROTEIN SEQUENCE OF 68-82, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   SUBUNIT.
RX   PubMed=10318844; DOI=10.1074/jbc.274.20.14238;
RA   Kelm R.J. Jr., Cogan J.G., Elder P.K., Strauch A.R., Getz M.J.;
RT   "Molecular interactions between single-stranded DNA-binding proteins
RT   associated with an essential MCAT element in the mouse smooth muscle
RT   alpha-actin promoter.";
RL   J. Biol. Chem. 274:14238-14245(1999).
RN   [5]
RP   FUNCTION.
RX   PubMed=11751932; DOI=10.1074/jbc.M109754200;
RA   Carlini L.E., Getz M.J., Strauch A.R., Kelm R.J. Jr.;
RT   "Cryptic MCAT enhancer regulation in fibroblasts and smooth muscle
RT   cells. Suppression of TEF-1 mediated activation by the single-stranded
RT   DNA-binding proteins, Pur alpha, Pur beta, and MSY1.";
RL   J. Biol. Chem. 277:8682-8692(2002).
RN   [6]
RP   REGION.
RX   PubMed=12874279; DOI=10.1074/jbc.M306163200;
RA   Kelm R.J. Jr., Wang S.X., Polikandriotis J.A., Strauch A.R.;
RT   "Structure/function analysis of mouse Purbeta, a single-stranded DNA-
RT   binding repressor of vascular smooth muscle alpha-actin gene
RT   transcription.";
RL   J. Biol. Chem. 278:38749-38757(2003).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION AT SER-6;
RP   SER-8 AND SER-316, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-8 AND SER-316,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Has capacity to bind repeated elements in single-
CC       stranded DNA such as the purine-rich single strand of the PUR
CC       element located upstream of the MYC gene. Participates in
CC       transcriptional and translational regulation of alpha-MHC
CC       expression in cardiac myocytes by binding to the purine-rich
CC       negative regulatory (PNR) element. Modulates constitutive liver
CC       galectin-3 gene transcription by binding to its promoter. May play
CC       a role in the dendritic transport of a subset of mRNAs (By
CC       similarity). Plays a role in the control of vascular smooth muscle
CC       (VSM) alpha-actin gene transcription as repressor in myoblasts and
CC       fibroblasts.
CC   -!- SUBUNIT: Homodimer, heterodimer with PURA and heterotrimer with
CC       PURA and YBX1/Y-box protein 1.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Belongs to the PUR DNA-binding protein family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF017630; AAB71859.1; -; mRNA.
DR   EMBL; AL646020; CAI26011.1; -; Genomic_DNA.
DR   IPI; IPI00128867; -.
DR   RefSeq; NP_035351.1; NM_011221.2.
DR   UniGene; Mm.296150; -.
DR   UniGene; Mm.390332; -.
DR   UniGene; Mm.474493; -.
DR   ProteinModelPortal; O35295; -.
DR   SMR; O35295; 43-294.
DR   IntAct; O35295; 2.
DR   STRING; O35295; -.
DR   PhosphoSite; O35295; -.
DR   PRIDE; O35295; -.
DR   Ensembl; ENSMUST00000059507; ENSMUSP00000055596; ENSMUSG00000049647.
DR   GeneID; 19291; -.
DR   KEGG; mmu:19291; -.
DR   UCSC; uc007hys.1; mouse.
DR   CTD; 19291; -.
DR   MGI; MGI:1338779; Purb.
DR   eggNOG; maNOG18881; -.
DR   HOGENOM; HBG383187; -.
DR   HOVERGEN; HBG006888; -.
DR   InParanoid; O35295; -.
DR   OMA; GGGEQET; -.
DR   OrthoDB; EOG4PRSRB; -.
DR   PhylomeDB; O35295; -.
DR   NextBio; 296226; -.
DR   ArrayExpress; O35295; -.
DR   Bgee; O35295; -.
DR   CleanEx; MM_PURB; -.
DR   Genevestigator; O35295; -.
DR   GermOnline; ENSMUSG00000049647; Mus musculus.
DR   GO; GO:0005662; C:DNA replication factor A complex; IDA:UniProtKB.
DR   GO; GO:0003691; F:double-stranded telomeric DNA binding; ISS:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR   GO; GO:0046332; F:SMAD binding; IDA:MGI.
DR   GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0006915; P:apoptosis; NAS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; NAS:UniProtKB.
DR   GO; GO:0008283; P:cell proliferation; NAS:UniProtKB.
DR   GO; GO:0006268; P:DNA unwinding involved in replication; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:MGI.
DR   InterPro; IPR006628; PUR_DNA_RNA-bd.
DR   PANTHER; PTHR12611; PUR_DNA_RNA_bd; 1.
DR   Pfam; PF04845; PurA; 1.
DR   SMART; SM00712; PUR; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; DNA-binding; Nucleus;
KW   Phosphoprotein; Repressor; Transcription; Transcription regulation.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    324       Transcriptional activator protein Pur-
FT                                beta.
FT                                /FTId=PRO_0000225616.
FT   DNA_BIND     37    263
FT   COMPBIAS     11     21       Poly-Gly.
FT   COMPBIAS     29     39       Poly-Gly.
FT   COMPBIAS    165    234       Gly-rich.
FT   MOD_RES       2      2       N-acetylalanine.
FT   MOD_RES       6      6       Phosphoserine.
FT   MOD_RES       8      8       Phosphoserine.
FT   MOD_RES      43     43       Phosphothreonine.
FT   MOD_RES     113    113       Phosphoserine (By similarity).
FT   MOD_RES     310    310       Phosphoserine (By similarity).
FT   MOD_RES     316    316       Phosphoserine.
SQ   SEQUENCE   324 AA;  33901 MW;  5CB70CCE3FDB7913 CRC64;
     MADGDSGSER GGGGGGGGGP GGFQPAPRGG GGGGGGPGGE QETQELASKR LDIQNKRFYL
     DVKQNAKGRF LKIAEVGAGG SKSRLTLSMA VAAEFRDSLG DFIEHYAQLG PSSPEQLAAG
     AEEGGGPRRA LKSEFLVREN RKYYLDLKEN QRGRFLRIRQ TVNRGGGGFG GGPGPGGLQS
     GQTIALPAQG LIEFRDALAK LIDDYGGDED ELAGGPGGGA GGPGGGLYGE LPEGTSITVD
     SKRFFFDVGC NKYGVFLRVS EVKPSYRNAI TVPFKAWGKF GGAFCRYADE MKEIQERQRD
     KLYERRGGGS GGGDESEGEE VDED
//
ID   VACHT_MOUSE             Reviewed;         530 AA.
AC   O35304;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   11-JAN-2011, entry version 73.
DE   RecName: Full=Vesicular acetylcholine transporter;
DE            Short=VAChT;
DE   AltName: Full=Solute carrier family 18 member 3;
GN   Name=Slc18a3; Synonyms=Vacht;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c;
RX   MEDLINE=98087181; PubMed=9427309;
RA   Naciff J.M., Misawa H., Dedman J.R.;
RT   "Molecular characterization of the mouse vesicular acetylcholine
RT   transporter gene.";
RL   NeuroReport 8:3467-3473(1997).
CC   -!- FUNCTION: Involved in acetylcholine transport into synaptic
CC       vesicles (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in the spinal cord, brain (excluding
CC       the cerebellum), brain stem and cholinergic tissues. Not expressed
CC       in peripheral tissues such as liver and kidney.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       Vesicular transporter family.
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DR   EMBL; AF019045; AAD09151.1; -; Genomic_DNA.
DR   IPI; IPI00129630; -.
DR   UniGene; Mm.190503; -.
DR   ProteinModelPortal; O35304; -.
DR   PhosphoSite; O35304; -.
DR   PRIDE; O35304; -.
DR   MGI; MGI:1101061; Slc18a3.
DR   HOVERGEN; HBG055082; -.
DR   Genevestigator; O35304; -.
DR   GO; GO:0060201; C:clathrin sculpted acetylcholine transport vesicle membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005277; F:acetylcholine transmembrane transporter activity; ISS:UniProtKB.
DR   InterPro; IPR020846; Major_facilitator_SF.
DR   InterPro; IPR011701; MFS_1.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Neurotransmitter transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    530       Vesicular acetylcholine transporter.
FT                                /FTId=PRO_0000127519.
FT   TOPO_DOM      1     33       Cytoplasmic (Potential).
FT   TRANSMEM     34     54       Helical; (Potential).
FT   TOPO_DOM     55    125       Lumenal, vesicle (Potential).
FT   TRANSMEM    126    146       Helical; (Potential).
FT   TOPO_DOM    147    152       Cytoplasmic (Potential).
FT   TRANSMEM    153    173       Helical; (Potential).
FT   TOPO_DOM    174    182       Lumenal, vesicle (Potential).
FT   TRANSMEM    183    203       Helical; (Potential).
FT   TOPO_DOM    204    213       Cytoplasmic (Potential).
FT   TRANSMEM    214    234       Helical; (Potential).
FT   TOPO_DOM    235    242       Lumenal, vesicle (Potential).
FT   TRANSMEM    243    263       Helical; (Potential).
FT   TOPO_DOM    264    288       Cytoplasmic (Potential).
FT   TRANSMEM    289    309       Helical; (Potential).
FT   TOPO_DOM    310    325       Lumenal, vesicle (Potential).
FT   TRANSMEM    326    346       Helical; (Potential).
FT   TOPO_DOM    347    356       Cytoplasmic (Potential).
FT   TRANSMEM    357    377       Helical; (Potential).
FT   TOPO_DOM    378    388       Lumenal, vesicle (Potential).
FT   TRANSMEM    389    409       Helical; (Potential).
FT   TOPO_DOM    410    422       Cytoplasmic (Potential).
FT   TRANSMEM    423    443       Helical; (Potential).
FT   TOPO_DOM    444    447       Lumenal, vesicle (Potential).
FT   TRANSMEM    448    468       Helical; (Potential).
FT   TOPO_DOM    469    530       Cytoplasmic (Potential).
FT   CARBOHYD     89     89       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     96     96       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   530 AA;  56615 MW;  08526F29B4E8EEDD CRC64;
     MEPTAPTGQA RAAATKLSEA VGAALQEPQR QRRLVLVIVC VALLLDNMLY MVIVPIVPDY
     IAHMRGGSES PTLISEVWEP TLPPPTLANA SAYLANTSAS PTAAGSARSI LRPRYPTESE
     DVKIGVLFAS KAILQLLVNP LSGPFIDRMS YDVPLLIGLG VMFASTVMFA FAEDYATFFA
     ARSLQGLGSA FADTSGIAMI ADKYPEEPER SRALGVALAF ISFGSLVAPP FGGILYEFAG
     KRVPFLVLAA VSLFDALLLL AVAKPFSAAA RARANLPVGT PIHRLMLDPY IAVVAGALTT
     CNIPLAFLEP TIATWMKHTM AASEWEMGMV WLPAFVPHVL GVYLTVRLAA RYPHLQWLYG
     ALGLAVIGVS SCVVPACRSF APLVVSLCGL CFGIALVDTA LLPTLAFLVD VRHVSVYGSV
     YAIADISYSV AYALGPIVAG HIVHSLGFEQ LSLGMGLANL LYAPVLLLLR NVGLLTRSRS
     ERDVLLDEPP QGLYDAVRLR EVQGKDGGEP CSPPGPFDGC EDDYNYYSRS
//
ID   SC6A6_MOUSE             Reviewed;         621 AA.
AC   O35316; P31642; Q91WI2;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2003, sequence version 2.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Sodium- and chloride-dependent taurine transporter;
DE   AltName: Full=Solute carrier family 6 member 6;
GN   Name=Slc6a6; Synonyms=Taut;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=93101684; PubMed=1465453; DOI=10.1073/pnas.89.24.12145;
RA   Liu Q.-R., Lopez-Corcuera B., Nelson H., Mandiyan S., Nelson N.;
RT   "Cloning and expression of a cDNA encoding the transporter of taurine
RT   and beta-alanine in mouse brain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:12145-12149(1992).
RN   [2]
RP   SEQUENCE REVISION.
RA   Liu Q.-R., Lopez-Corcuera B., Nelson H., Mandiyan S., Nelson N.;
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   MEDLINE=98041502; PubMed=9375654;
RA   Vinnakota S., Qian X., Egal H., Sarthy V., Sarkar H.K.;
RT   "Molecular characterization and in situ localization of a mouse
RT   retinal taurine transporter.";
RL   J. Neurochem. 69:2238-2250(1997).
RN   [4]
RP   SEQUENCE REVISION.
RA   Vinnakota S., Qian X., Egal H., Sarthy V., Sarkar H.K.;
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Required for the uptake of taurine. Transports both
CC       taurine and beta-alanine which requires sodium ions. Chloride ions
CC       are necessary for optimal uptake.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.5 uM for taurine;
CC         KM=56 uM for beta-alanine;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Brain, kidney and retina. Detectable amount in
CC       liver.
CC   -!- PTM: Down-regulated upon Ser-322 phosphorylation (By similarity).
CC   -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF)
CC       (TC 2.A.22) family. SLC6A6 subfamily.
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DR   EMBL; L03292; AAB54039.2; -; mRNA.
DR   EMBL; AF020194; AAB70922.2; -; mRNA.
DR   EMBL; BC015245; AAH15245.1; -; mRNA.
DR   IPI; IPI00314054; -.
DR   PIR; A47194; A47194.
DR   RefSeq; NP_033346.2; NM_009320.4.
DR   UniGene; Mm.395650; -.
DR   ProteinModelPortal; O35316; -.
DR   SMR; O35316; 40-558.
DR   STRING; O35316; -.
DR   PhosphoSite; O35316; -.
DR   PRIDE; O35316; -.
DR   Ensembl; ENSMUST00000032185; ENSMUSP00000032185; ENSMUSG00000030096.
DR   GeneID; 21366; -.
DR   KEGG; mmu:21366; -.
DR   UCSC; uc009cyh.1; mouse.
DR   CTD; 21366; -.
DR   MGI; MGI:98488; Slc6a6.
DR   eggNOG; roNOG04580; -.
DR   HOGENOM; HBG702834; -.
DR   HOVERGEN; HBG071421; -.
DR   InParanoid; O35316; -.
DR   OMA; PLPTFWA; -.
DR   OrthoDB; EOG4X3H0Z; -.
DR   PhylomeDB; O35316; -.
DR   NextBio; 300574; -.
DR   ArrayExpress; O35316; -.
DR   Bgee; O35316; -.
DR   Genevestigator; O35316; -.
DR   GermOnline; ENSMUSG00000030096; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; IC:MGI.
DR   GO; GO:0005328; F:neurotransmitter:sodium symporter activity; IEA:InterPro.
DR   InterPro; IPR000175; Na/ntran_symport.
DR   InterPro; IPR002434; Na/ntran_symport_taurine.
DR   PANTHER; PTHR11616; Na/ntran_symport; 1.
DR   PANTHER; PTHR11616:SF29; Tau_transporter; 1.
DR   Pfam; PF00209; SNF; 1.
DR   PRINTS; PR00176; NANEUSMPORT.
DR   PRINTS; PR01200; TAUTRANSPORT.
DR   PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR   PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
DR   PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Neurotransmitter transport; Phosphoprotein;
KW   Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    621       Sodium- and chloride-dependent taurine
FT                                transporter.
FT                                /FTId=PRO_0000214768.
FT   TOPO_DOM      1     49       Cytoplasmic (Potential).
FT   TRANSMEM     50     70       Helical; Name=1; (Potential).
FT   TRANSMEM     77     97       Helical; Name=2; (Potential).
FT   TRANSMEM    123    143       Helical; Name=3; (Potential).
FT   TOPO_DOM    144    215       Extracellular (Potential).
FT   TRANSMEM    216    236       Helical; Name=4; (Potential).
FT   TRANSMEM    245    265       Helical; Name=5; (Potential).
FT   TRANSMEM    290    310       Helical; Name=6; (Potential).
FT   TRANSMEM    332    352       Helical; Name=7; (Potential).
FT   TRANSMEM    380    400       Helical; Name=8; (Potential).
FT   TRANSMEM    430    450       Helical; Name=9; (Potential).
FT   TRANSMEM    465    485       Helical; Name=10; (Potential).
FT   TRANSMEM    508    528       Helical; Name=11; (Potential).
FT   TRANSMEM    545    565       Helical; Name=12; (Potential).
FT   TOPO_DOM    566    621       Cytoplasmic (Potential).
FT   MOD_RES      21     21       Phosphoserine.
FT   MOD_RES     322    322       Phosphoserine (By similarity).
FT   CARBOHYD    163    163       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    179    179       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    190    190       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    340    340       S -> L (in Ref. 3; AAB70922).
SQ   SEQUENCE   621 AA;  69856 MW;  4D3E4ACFDB7D7EA2 CRC64;
     MATKEKLQCL KDFHKDILKP SPGKSPGTRP EDEADGKPPQ REKWSSKIDF VLSVAGGFVG
     LGNVWRFPYL CYKNGGGAFL IPYFIFLFGS GLPVFFLEVI IGQYTSEGGI TCWEKICPLF
     SGIGYASIVI VSLLNVYYIV ILAWATYYLF HSFQKDLPWA HCNHSWNTPQ CMEDTLRRNE
     SHWVSLSTAN FTSPVIEFWE RNVLSLSSGI DNPGSLKWDL ALCLLLVWLV CFFCIWKGVR
     STGKVVYFTA TFPFAMLLVL LVRGLTLPGA GEGIKFYLYP DISRLGDPQV WIDAGTQIFF
     SYAICLGAMT SLGSYNKYKY NSYRDCMLLG CLNSGTSFVS GFAIFSILGF MAQEQGVDIA
     DVAESGPGLA FIAYPKAVTM MPLPTFWSIL FFIMLLLLGL DSQFVEVEGQ ITSLVDLYPS
     FLRKGYRREI FIAILCSISY LLGLTMVTEG GMYVFQLFDY YAASGVCLLW VAFFECFVIA
     WIYGGDNLYD GIEDMIGYRP GPWMKYSWAV ITPALCVGCF VFSLVKYVPL TYNKVYRYPD
     WAIGLGWGLA LSSMLCIPLV IVILLCRTEG PLRVRIKYLI TPREPNRWAV EREGATPFHS
     RVTLMNGALM KPSHVIVETM M
//
ID   IMA4_MOUSE              Reviewed;         521 AA.
AC   O35343;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Importin subunit alpha-4;
DE   AltName: Full=Importin alpha Q1;
DE            Short=Qip1;
DE   AltName: Full=Karyopherin subunit alpha-4;
GN   Name=Kpna4; Synonyms=Qip1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98034160; PubMed=9369227; DOI=10.1016/S0014-5793(97)01092-2;
RA   Tsuji L., Takumi T., Imamoto N., Yoneda Y.;
RT   "Identification of novel homologues of mouse importin alpha, the alpha
RT   subunit of the nuclear pore-targeting complex, and their tissue-
RT   specific expression.";
RL   FEBS Lett. 416:30-34(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Limb, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Functions in nuclear protein import as an adapter
CC       protein for nuclear receptor KPNB1. Binds specifically and
CC       directly to substrates containing either a simple or bipartite NLS
CC       motif. Docking of the importin/substrate complex to the nuclear
CC       pore complex (NPC) is mediated by KPNB1 through binding to
CC       nucleoporin FxFG repeats and the complex is subsequently
CC       translocated through the pore by an energy requiring, Ran-
CC       dependent mechanism. At the nucleoplasmic side of the NPC, Ran
CC       binds to importin-beta and the three components separate and
CC       importin-alpha and -beta are re-exported from the nucleus to the
CC       cytoplasm where GTP hydrolysis releases Ran from importin. The
CC       directionality of nuclear import is thought to be conferred by an
CC       asymmetric distribution of the GTP- and GDP-bound forms of Ran
CC       between the cytoplasm and nucleus.
CC   -!- SUBUNIT: Forms a complex with importin subunit beta-1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Detected more or less in all tissues examined
CC       (Ehrlich ascites tumor cells, testis, kidney, spleen, liver,
CC       heart, lung, thymus, skeletal muscle, cerebellum and brain
CC       (without cerebellum)). Multiple-sized transcripts were highly
CC       expressed, especially in testis.
CC   -!- DOMAIN: Consists of an N-terminal hydrophilic region, a
CC       hydrophobic central region composed of 10 repeats, and a short
CC       hydrophilic C-terminus. The N-terminal hydrophilic region contains
CC       the importin beta binding domain (IBB domain), which is sufficient
CC       for binding importin beta and essential for nuclear protein
CC       import.
CC   -!- DOMAIN: The IBB domain is thought to act as an intrasteric
CC       autoregulatory sequence by interacting with the internal
CC       autoinhibitory NLS. Binding of KPNB1 probably overlaps the
CC       internal NLS and contributes to a high affinity for cytoplasmic
CC       NLS-containing cargo substrates. After dissociation of the
CC       importin/substrate complex in the nucleus the internal
CC       autohibitory NLS contributes to a low affinity for nuclear NLS-
CC       containing proteins (By similarity).
CC   -!- DOMAIN: The major and minor NLS binding sites are mainly involved
CC       in recognition of simple or bipartite NLS motifs. Structurally
CC       located within in a helical surface groove they contain several
CC       conserved Trp and Asn residues of the corresponding third helices
CC       (H3) of ARM repeats which mainly contribute to binding (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the importin alpha family.
CC   -!- SIMILARITY: Contains 10 ARM repeats.
CC   -!- SIMILARITY: Contains 1 IBB domain.
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DR   EMBL; AF020771; AAC53371.1; -; mRNA.
DR   EMBL; BC026821; AAH26821.1; -; mRNA.
DR   EMBL; BC052162; AAH52162.1; -; mRNA.
DR   IPI; IPI00129792; -.
DR   RefSeq; NP_032493.1; NM_008467.4.
DR   UniGene; Mm.30601; -.
DR   ProteinModelPortal; O35343; -.
DR   SMR; O35343; 11-485.
DR   STRING; O35343; -.
DR   PhosphoSite; O35343; -.
DR   PRIDE; O35343; -.
DR   Ensembl; ENSMUST00000029353; ENSMUSP00000029353; ENSMUSG00000027782.
DR   GeneID; 16649; -.
DR   KEGG; mmu:16649; -.
DR   UCSC; uc008pme.1; mouse.
DR   CTD; 16649; -.
DR   MGI; MGI:1100848; Kpna4.
DR   eggNOG; roNOG09439; -.
DR   HOVERGEN; HBG001846; -.
DR   InParanoid; O35343; -.
DR   OMA; NATSDNQ; -.
DR   OrthoDB; EOG48GW2Z; -.
DR   PhylomeDB; O35343; -.
DR   NextBio; 290333; -.
DR   ArrayExpress; O35343; -.
DR   Bgee; O35343; -.
DR   CleanEx; MM_KPNA4; -.
DR   Genevestigator; O35343; -.
DR   GermOnline; ENSMUSG00000027782; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005643; C:nuclear pore; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0008565; F:protein transporter activity; IDA:MGI.
DR   GO; GO:0006606; P:protein import into nucleus; IDA:MGI.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR002652; Importin-a-like_IBB-bd_dom.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF00514; Arm; 8.
DR   Pfam; PF01749; IBB; 1.
DR   SMART; SM00185; ARM; 8.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 3.
DR   PROSITE; PS51214; IBB; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Protein transport;
KW   Repeat; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    521       Importin subunit alpha-4.
FT                                /FTId=PRO_0000120727.
FT   DOMAIN        2     58       IBB.
FT   REPEAT       66    106       ARM 1; truncated.
FT   REPEAT      107    149       ARM 2.
FT   REPEAT      150    194       ARM 3.
FT   REPEAT      195    233       ARM 4.
FT   REPEAT      234    278       ARM 5.
FT   REPEAT      279    318       ARM 6.
FT   REPEAT      319    360       ARM 7.
FT   REPEAT      361    400       ARM 8.
FT   REPEAT      401    443       ARM 9.
FT   REPEAT      447    485       ARM 10; atypical.
FT   REGION      137    229       NLS binding site (major) (By similarity).
FT   REGION      306    394       NLS binding site (minor) (By similarity).
FT   MOTIF        43     52       Nuclear localization signal (By
FT                                similarity).
FT   COMPBIAS    233    236       Poly-Pro.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      60     60       Phosphoserine (By similarity).
SQ   SEQUENCE   521 AA;  57923 MW;  A0578EC9D411E060 CRC64;
     MADNEKLDNQ RLKNFKNKGR DLETMRRQRN EVVVELRKNK RDEHLLKRRN VPQEDICEDS
     DIDGDYRVQN TSLEAIVQNA SSDNQGIQLS AVQAARKLLS SDRNPPIDDL IKSGILPILV
     HCLERDDNPS LQFEAAWALT NIASGTSEQT QAVVQSNAVP LFLRLLHSPH QNVCEQAVWA
     LGNIIGDGPQ CRDYVISLGV VKPLLSFISP SIPITFLRNV TWVMVNLCRH KDPPPPMETI
     QEILPALCVL IHHTDVNILV DTVWALSYLT DAGNEQIQMV IDSGIVPHLV PLLSHQEVKV
     QTAALRAVGN IVTGTDEQTQ VVLNCDALSH FPALLTHPKE KINKEAVWFL SNITAGNQQQ
     VQAVIDANLV PMIIHLLDKG DFGTQKEAAW AISNLTISGR KDQVAYLIQQ NVIPPFCNLL
     TVKDAQVVQV VLDGLSNILK MAEDQAETIA NLIEECGGLE KIEQLQNHEN EDIYKLAYEI
     IDQFFSSDDI DEDPSLVPES VQGGTFGFNS STNVPTEGFQ F
//
ID   IMA3_MOUSE              Reviewed;         521 AA.
AC   O35344;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Importin subunit alpha-3;
DE   AltName: Full=Importin alpha Q2;
DE            Short=Qip2;
DE   AltName: Full=Karyopherin subunit alpha-3;
GN   Name=Kpna3; Synonyms=Qip2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98034160; PubMed=9369227; DOI=10.1016/S0014-5793(97)01092-2;
RA   Tsuji L., Takumi T., Imamoto N., Yoneda Y.;
RT   "Identification of novel homologues of mouse importin alpha, the alpha
RT   subunit of the nuclear pore-targeting complex, and their tissue-
RT   specific expression.";
RL   FEBS Lett. 416:30-34(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Functions in nuclear protein import as an adapter
CC       protein for nuclear receptor KPNB1. Binds specifically and
CC       directly to substrates containing either a simple or bipartite NLS
CC       motif. Docking of the importin/substrate complex to the nuclear
CC       pore complex (NPC) is mediated by KPNB1 through binding to
CC       nucleoporin FxFG repeats and the complex is subsequently
CC       translocated through the pore by an energy requiring, Ran-
CC       dependent mechanism. At the nucleoplasmic side of the NPC, Ran
CC       binds to importin-beta and the three components separate and
CC       importin-alpha and -beta are re-exported from the nucleus to the
CC       cytoplasm where GTP hydrolysis releases Ran from importin. The
CC       directionality of nuclear import is thought to be conferred by an
CC       asymmetric distribution of the GTP- and GDP-bound forms of Ran
CC       between the cytoplasm and nucleus. In vitro, mediates the nuclear
CC       import of human cytomegalovirus UL84 by recognizing a non-
CC       classical NLS.
CC   -!- SUBUNIT: Forms a complex with importin subunit beta-1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Detected more or less in all tissues examined
CC       (Ehrlich ascites tumor cells, testis, kidney, spleen, liver,
CC       heart, lung, thymus, skeletal muscle, cerebellum and brain
CC       (without cerebellum)).
CC   -!- DOMAIN: Consists of an N-terminal hydrophilic region, a
CC       hydrophobic central region composed of 10 repeats, and a short
CC       hydrophilic C-terminus. The N-terminal hydrophilic region contains
CC       the importin beta binding domain (IBB domain), which is sufficient
CC       for binding importin beta and essential for nuclear protein
CC       import.
CC   -!- DOMAIN: The IBB domain is thought to act as an intrasteric
CC       autoregulatory sequence by interacting with the internal
CC       autoinhibitory NLS. Binding of KPNB1 probably overlaps the
CC       internal NLS and contributes to a high affinity for cytoplasmic
CC       NLS-containing cargo substrates. After dissociation of the
CC       importin/substrate complex in the nucleus the internal
CC       autohibitory NLS contributes to a low affinity for nuclear NLS-
CC       containing proteins (By similarity).
CC   -!- DOMAIN: The major and minor NLS binding sites are mainly involved
CC       in recognition of simple or bipartite NLS motifs. Structurally
CC       located within in a helical surface groove they contain several
CC       conserved Trp and Asn residues of the corresponding third helices
CC       (H3) of ARM repeats which mainly contribute to binding (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the importin alpha family.
CC   -!- SIMILARITY: Contains 8 ARM repeats.
CC   -!- SIMILARITY: Contains 1 IBB domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF020772; AAC53372.1; -; mRNA.
DR   EMBL; BC026885; AAH26885.1; -; mRNA.
DR   IPI; IPI00230429; -.
DR   RefSeq; NP_032492.1; NM_008466.5.
DR   UniGene; Mm.25548; -.
DR   ProteinModelPortal; O35344; -.
DR   SMR; O35344; 11-485.
DR   STRING; O35344; -.
DR   PhosphoSite; O35344; -.
DR   PRIDE; O35344; -.
DR   Ensembl; ENSMUST00000022496; ENSMUSP00000022496; ENSMUSG00000021929.
DR   GeneID; 16648; -.
DR   KEGG; mmu:16648; -.
DR   UCSC; uc007ufw.1; mouse.
DR   CTD; 16648; -.
DR   MGI; MGI:1100863; Kpna3.
DR   eggNOG; roNOG09439; -.
DR   HOGENOM; HBG590318; -.
DR   HOVERGEN; HBG001846; -.
DR   InParanoid; O35344; -.
DR   OMA; PNLLTHP; -.
DR   OrthoDB; EOG48GW2Z; -.
DR   PhylomeDB; O35344; -.
DR   NextBio; 290329; -.
DR   ArrayExpress; O35344; -.
DR   Bgee; O35344; -.
DR   CleanEx; MM_KPNA3; -.
DR   Genevestigator; O35344; -.
DR   GermOnline; ENSMUSG00000021929; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005643; C:nuclear pore; IEA:InterPro.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR   GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR   GO; GO:0006606; P:protein import into nucleus; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR002652; Importin-a-like_IBB-bd_dom.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF00514; Arm; 8.
DR   Pfam; PF01749; IBB; 1.
DR   SMART; SM00185; ARM; 8.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 3.
DR   PROSITE; PS51214; IBB; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Protein transport;
KW   Repeat; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    521       Importin subunit alpha-3.
FT                                /FTId=PRO_0000120725.
FT   DOMAIN        2     58       IBB.
FT   REPEAT       66    106       ARM 1; truncated.
FT   REPEAT      107    149       ARM 2.
FT   REPEAT      150    194       ARM 3.
FT   REPEAT      195    233       ARM 4.
FT   REPEAT      234    278       ARM 5.
FT   REPEAT      279    318       ARM 6.
FT   REPEAT      319    360       ARM 7.
FT   REPEAT      361    400       ARM 8.
FT   REPEAT      401    443       ARM 9.
FT   REPEAT      447    485       ARM 10; atypical.
FT   REGION      137    229       NLS binding site (major) (By similarity).
FT   REGION      306    394       NLS binding site (minor) (By similarity).
FT   MOTIF        43     52       Nuclear localization signal (By
FT                                similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      56     56       Phosphoserine.
FT   MOD_RES      60     60       Phosphoserine.
SQ   SEQUENCE   521 AA;  57773 MW;  78501CE1AAB3A260 CRC64;
     MAENPGLENH RIKSFKNKGR DVETMRRHRN EVTVELRKNK RDEHLLKKRN VPQEESLEDS
     DVDADFKAQN VTLEAILQNA TSDNPVVQLS AVQAARKLLS SDRNPPIDDL IKSGILPILV
     KCLERDDNPS LQFEAAWALT NIASGTSAQT QAVVQSNAVP LFLRLLHSPH QNVCEQAVWA
     LGNIIGDGPQ CRDYVISLGV VKPLLSFINP SIPITFLRNV TWVIVNLCRN KDPPPPMETV
     QEILPALCVL IYHTDINILV DTVWALSYLT DGGNEQIQMV IDSGVVPFLV PLLSHQEVKV
     QTAALRAVGN IVTGTDEQTQ VVLNCDVLSH FPNLLSHPKE KINKEAVWFL SNITAGNQQQ
     VQAVIDAGLI PMIIHQLAKG DFGTQKEAAW AISNLTISGR KDQVEYLVQQ NVIPPFCNLL
     SVKDSQVVQV VLDGLKNILI MAGDEASTIA EIIEECGGLE KIEVLQQHEN EDIYKLAFEI
     IDQYFSGDDI DEDPSLIPEA TQGGTYNFDP TANLQTKEFN F
//
ID   IMA7_MOUSE              Reviewed;         536 AA.
AC   O35345; Q3U388; Q9CVP9;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 2.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Importin subunit alpha-7;
DE   AltName: Full=Importin alpha-S2;
DE   AltName: Full=Karyopherin subunit alpha-6;
GN   Name=Kpna6; Synonyms=Kpna5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4-536.
RX   MEDLINE=98034160; PubMed=9369227; DOI=10.1016/S0014-5793(97)01092-2;
RA   Tsuji L., Takumi T., Imamoto N., Yoneda Y.;
RT   "Identification of novel homologues of mouse importin alpha, the alpha
RT   subunit of the nuclear pore-targeting complex, and their tissue-
RT   specific expression.";
RL   FEBS Lett. 416:30-34(1997).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Functions in nuclear protein import as an adapter
CC       protein for nuclear receptor KPNB1. Binds specifically and
CC       directly to substrates containing either a simple or bipartite NLS
CC       motif. Docking of the importin/substrate complex to the nuclear
CC       pore complex (NPC) is mediated by KPNB1 through binding to
CC       nucleoporin FxFG repeats and the complex is subsequently
CC       translocated through the pore by an energy requiring, Ran-
CC       dependent mechanism. At the nucleoplasmic side of the NPC, Ran
CC       binds to importin-beta and the three components separate and
CC       importin-alpha and -beta are re-exported from the nucleus to the
CC       cytoplasm where GTP hydrolysis releases Ran from importin. The
CC       directionality of nuclear import is thought to be conferred by an
CC       asymmetric distribution of the GTP- and GDP-bound forms of Ran
CC       between the cytoplasm and nucleus.
CC   -!- SUBUNIT: Forms a complex with importin subunit beta-1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Only slightly detected in Ehrlich ascites
CC       tumor cells, thymus and skeletal muscle, clearly detected in
CC       kidney, spleen, liver, heart, and lung. High expression in testis.
CC   -!- DOMAIN: Consists of an N-terminal hydrophilic region, a
CC       hydrophobic central region composed of 10 repeats, and a short
CC       hydrophilic C-terminus. The N-terminal hydrophilic region contains
CC       the importin beta binding domain (IBB domain), which is sufficient
CC       for binding importin beta and essential for nuclear protein
CC       import.
CC   -!- DOMAIN: The IBB domain is thought to act as an intrasteric
CC       autoregulatory sequence by interacting with the internal
CC       autoinhibitory NLS. Binding of KPNB1 probably overlaps the
CC       internal NLS and contributes to a high affinity for cytoplasmic
CC       NLS-containing cargo substrates. After dissociation of the
CC       importin/substrate complex in the nucleus the internal
CC       autohibitory NLS contributes to a low affinity for nuclear NLS-
CC       containing proteins (By similarity).
CC   -!- DOMAIN: The major and minor NLS binding sites are mainly involved
CC       in recognition of simple or bipartite NLS motifs. Structurally
CC       located within in a helical surface groove they contain several
CC       conserved Trp and Asn residues of the corresponding third helices
CC       (H3) of ARM repeats which mainly contribute to binding (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the importin alpha family.
CC   -!- SIMILARITY: Contains 10 ARM repeats.
CC   -!- SIMILARITY: Contains 1 IBB domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK007053; BAB24841.1; -; mRNA.
DR   EMBL; AK154882; BAE32900.1; -; mRNA.
DR   EMBL; BC004833; AAH04833.2; -; mRNA.
DR   EMBL; AF020773; AAC53373.1; -; mRNA.
DR   IPI; IPI00649329; -.
DR   RefSeq; NP_032494.3; NM_008468.4.
DR   UniGene; Mm.202358; -.
DR   ProteinModelPortal; O35345; -.
DR   SMR; O35345; 22-507.
DR   DIP; DIP-48616N; -.
DR   STRING; O35345; -.
DR   PhosphoSite; O35345; -.
DR   PRIDE; O35345; -.
DR   Ensembl; ENSMUST00000102590; ENSMUSP00000099650; ENSMUSG00000003731.
DR   GeneID; 16650; -.
DR   KEGG; mmu:16650; -.
DR   CTD; 16650; -.
DR   MGI; MGI:1100836; Kpna6.
DR   HOGENOM; HBG590318; -.
DR   HOVERGEN; HBG001846; -.
DR   InParanoid; O35345; -.
DR   OMA; NCAILPP; -.
DR   OrthoDB; EOG4NP739; -.
DR   PhylomeDB; O35345; -.
DR   NextBio; 290337; -.
DR   ArrayExpress; O35345; -.
DR   Bgee; O35345; -.
DR   CleanEx; MM_KPNA6; -.
DR   Genevestigator; O35345; -.
DR   GermOnline; ENSMUSG00000003731; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005643; C:nuclear pore; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0008565; F:protein transporter activity; IDA:MGI.
DR   GO; GO:0006606; P:protein import into nucleus; IDA:MGI.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR002652; Importin-a-like_IBB-bd_dom.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF00514; Arm; 8.
DR   Pfam; PF01749; IBB; 1.
DR   SMART; SM00185; ARM; 8.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 2.
DR   PROSITE; PS51214; IBB; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Phosphoprotein; Protein transport; Repeat;
KW   Transport.
FT   CHAIN         1    536       Importin subunit alpha-7.
FT                                /FTId=PRO_0000120730.
FT   DOMAIN        1     60       IBB.
FT   REPEAT       76    115       ARM 1; truncated.
FT   REPEAT      116    159       ARM 2.
FT   REPEAT      160    204       ARM 3.
FT   REPEAT      205    243       ARM 4.
FT   REPEAT      244    288       ARM 5.
FT   REPEAT      289    328       ARM 6.
FT   REPEAT      329    370       ARM 7.
FT   REPEAT      371    410       ARM 8.
FT   REPEAT      411    453       ARM 9.
FT   REPEAT      457    502       ARM 10; atypical.
FT   REGION      147    239       NLS binding site (major) (By similarity).
FT   REGION      316    404       NLS binding site (minor) (By similarity).
FT   MOTIF        45     54       Nuclear localization signal (By
FT                                similarity).
FT   COMPBIAS     28     31       Poly-Arg.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES       3      3       Phosphothreonine (By similarity).
FT   MOD_RES       6      6       Phosphoserine.
FT   CONFLICT     86     86       V -> E (in Ref. 1; BAE32900).
FT   CONFLICT    280    280       S -> A (in Ref. 1; BAE32900).
FT   CONFLICT    435    435       S -> T (in Ref. 1; BAB24841).
SQ   SEQUENCE   536 AA;  59964 MW;  553A6265023052AC CRC64;
     METMASPGKD NYRMKSYKNN ALNPEEMRRR REEEGIQLRK QKREQQLFKR RNVELINEEA
     AMFDSLLMDS YVSSTTGESV ITREMVEMLF SDDSDLQLAT TQKFRKLLSK EPSPPIDEVI
     NTPGVVDRFV EFLKRNENCT LQFEAAWALT NIASGTSQQT KIVIEAGAVP IFIELLNSDF
     EDVQEQAVWA LGNIAGDSSL CRDYVLNCSI LNPLLTLLTK STRLTMTRNA VWALSNLCRG
     KNPPPEFAKV SPCLPVLSRL LFSSDSDLLA DACWALSYLS DGPNEKIQAV IDSGVCRRLV
     ELLMHNDYKV ASPALRAVGN IVTGDDIQTQ VILNCSALPC LLHLLSSSKE SIRKEACWTI
     SNITAGNRAQ IQAVIDANIF PVLIEILQKA EFRTRKEAAW AITNATSGGT PEQIRYLVSL
     GCIKPLCDLL TVMDSKIVQV ALNGLENILR LGEQESKRSG SGVNPYCGLI EEAYGLDKIE
     FLQSHENQEI YQKAFDLIEH YFGVEDDDSS LAPQVDETQQ QFIFQQPEAP MEGFQL
//
ID   NRP2_MOUSE              Reviewed;         931 AA.
AC   O35375; O35373; O35374; O35376; O35377; O35378;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Neuropilin-2;
DE   AltName: Full=Vascular endothelial cell growth factor 165 receptor 2;
DE   Flags: Precursor;
GN   Name=Nrp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A0; A17; A22; A5; B0 AND B5).
RC   STRAIN=BALB/c;
RX   MEDLINE=97470888; PubMed=9331348; DOI=10.1016/S0896-6273(00)80371-2;
RA   Chen H., Chedotal A., He Z.-G., Goodman C.S., Tessier-Lavigne M.;
RT   "Neuropilin-2, a novel member of the neuropilin family, is a high
RT   affinity receptor for the semaphorins Sema E and Sema IV but not Sema
RT   III.";
RL   Neuron 19:547-559(1997).
CC   -!- FUNCTION: High affinity receptor for semaphorins 3C, 3F, VEGF-165
CC       and VEGF-145 isoforms of VEGF, and the PLGF-2 isoform of PGF.
CC   -!- SUBUNIT: Heterodimer with NRP1 (Probable). Binds PLXNB1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=A22;
CC         IsoId=O35375-1; Sequence=Displayed;
CC       Name=A0;
CC         IsoId=O35375-2; Sequence=VSP_004344;
CC       Name=A5;
CC         IsoId=O35375-3; Sequence=VSP_004345;
CC       Name=A17;
CC         IsoId=O35375-4; Sequence=VSP_004343;
CC       Name=B0;
CC         IsoId=O35375-5; Sequence=VSP_004346;
CC       Name=B5;
CC         IsoId=O35375-6; Sequence=VSP_004347;
CC   -!- TISSUE SPECIFICITY: Expressed in developing CNS, PNS and in some
CC       nonneural tissues including limb buds, developing bones, muscles,
CC       intestinal epithelium, kidney, lung and submandibular gland.
CC   -!- DEVELOPMENTAL STAGE: The expression pattern is very dynamic and is
CC       developmentally regulated.
CC   -!- SIMILARITY: Belongs to the neuropilin family.
CC   -!- SIMILARITY: Contains 2 CUB domains.
CC   -!- SIMILARITY: Contains 2 F5/8 type C domains.
CC   -!- SIMILARITY: Contains 1 MAM domain.
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DR   EMBL; AF022856; AAC53379.1; -; mRNA.
DR   EMBL; AF022854; AAC53377.1; -; mRNA.
DR   EMBL; AF022855; AAC53378.1; -; mRNA.
DR   EMBL; AF022857; AAC53380.1; -; mRNA.
DR   EMBL; AF022858; AAC53381.1; -; mRNA.
DR   EMBL; AF022861; AAC53382.1; -; mRNA.
DR   IPI; IPI00129911; -.
DR   IPI; IPI00227582; -.
DR   IPI; IPI00227583; -.
DR   IPI; IPI00227584; -.
DR   IPI; IPI00755777; -.
DR   IPI; IPI00876020; -.
DR   UniGene; Mm.266341; -.
DR   ProteinModelPortal; O35375; -.
DR   SMR; O35375; 26-595.
DR   STRING; O35375; -.
DR   PRIDE; O35375; -.
DR   Ensembl; ENSMUST00000027112; ENSMUSP00000027112; ENSMUSG00000025969.
DR   Ensembl; ENSMUST00000075144; ENSMUSP00000074642; ENSMUSG00000025969.
DR   Ensembl; ENSMUST00000114157; ENSMUSP00000109794; ENSMUSG00000025969.
DR   MGI; MGI:1100492; Nrp2.
DR   eggNOG; roNOG04879; -.
DR   HOGENOM; HBG714573; -.
DR   HOVERGEN; HBG000502; -.
DR   InParanoid; O35375; -.
DR   ArrayExpress; O35375; -.
DR   Bgee; O35375; -.
DR   CleanEx; MM_NRP2; -.
DR   Genevestigator; O35375; -.
DR   GermOnline; ENSMUSG00000025969; Mus musculus.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IC:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0017154; F:semaphorin receptor activity; IPI:MGI.
DR   GO; GO:0007411; P:axon guidance; IMP:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0071445; P:cellular response to protein stimulus; IDA:MGI.
DR   GO; GO:0007507; P:heart development; IGI:MGI.
DR   GO; GO:0050919; P:negative chemotaxis; IMP:MGI.
DR   GO; GO:0001755; P:neural crest cell migration; IMP:MGI.
DR   InterPro; IPR000421; Coagulation_factor_5/8-type_C.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR000859; CUB.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR000998; MAM_dom.
DR   InterPro; IPR014648; Neuropilin.
DR   InterPro; IPR022579; Neuropilin1_C.
DR   Gene3D; G3DSA:2.60.120.290; CUB; 2.
DR   Pfam; PF00431; CUB; 2.
DR   Pfam; PF11980; DUF3481; 1.
DR   Pfam; PF00754; F5_F8_type_C; 2.
DR   Pfam; PF00629; MAM; 1.
DR   PIRSF; PIRSF036960; Neuropilin; 1.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00231; FA58C; 2.
DR   SMART; SM00137; MAM; 1.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
DR   SUPFAM; SSF49854; CUB; 2.
DR   SUPFAM; SSF49785; Gal_bind_like; 2.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS01285; FA58C_1; 2.
DR   PROSITE; PS01286; FA58C_2; 2.
DR   PROSITE; PS50022; FA58C_3; 2.
DR   PROSITE; PS50060; MAM_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Developmental protein; Differentiation;
KW   Disulfide bond; Glycoprotein; Membrane; Neurogenesis; Receptor;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21    931       Neuropilin-2.
FT                                /FTId=PRO_0000021864.
FT   TOPO_DOM     21    864       Extracellular (Potential).
FT   TRANSMEM    865    889       Helical; (Potential).
FT   TOPO_DOM    890    931       Cytoplasmic (Potential).
FT   DOMAIN       28    142       CUB 1.
FT   DOMAIN      149    267       CUB 2.
FT   DOMAIN      277    427       F5/8 type C 1.
FT   DOMAIN      434    592       F5/8 type C 2.
FT   DOMAIN      642    802       MAM.
FT   COMPBIAS    838    845       Poly-Ser.
FT   CARBOHYD    152    152       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    157    157       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    629    629       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    839    839       N-linked (GlcNAc...) (Potential).
FT   DISULFID     28     55       By similarity.
FT   DISULFID     83    105       By similarity.
FT   DISULFID    149    175       By similarity.
FT   DISULFID    208    230       By similarity.
FT   DISULFID    277    427       By similarity.
FT   DISULFID    434    592       By similarity.
FT   VAR_SEQ     809    830       Missing (in isoform A0).
FT                                /FTId=VSP_004344.
FT   VAR_SEQ     809    813       Missing (in isoform A17).
FT                                /FTId=VSP_004343.
FT   VAR_SEQ     810    931       EDFKVDIPETHGGEGYEDEIDDEYEGDWSNSSSSTSGAGDP
FT                                SSGKEKSWLYTLDPILITIIAMSSLGVLLGATCAGLLLYCT
FT                                CSYSGLSSRSCTTLENYNFELYDGLKHKVKINHQKCCSEA
FT                                -> GTLPPGTEPTVDTVPVQPIPAYWYYVMAAGGAVLVLAS
FT                                VVLALVLHYHRFRYAAKKTDHSITYKTSHYTNGAPLAVEPT
FT                                LTIKLEQERGSHC (in isoform B0).
FT                                /FTId=VSP_004346.
FT   VAR_SEQ     814    931       VDIPETHGGEGYEDEIDDEYEGDWSNSSSSTSGAGDPSSGK
FT                                EKSWLYTLDPILITIIAMSSLGVLLGATCAGLLLYCTCSYS
FT                                GLSSRSCTTLENYNFELYDGLKHKVKINHQKCCSEA -> G
FT                                GTLPPGTEPTVDTVPVQPIPAYWYYVMAAGGAVLVLASVVL
FT                                ALVLHYHRFRYAAKKTDHSITYKTSHYTNGAPLAVEPTLTI
FT                                KLEQERGSHC (in isoform B5).
FT                                /FTId=VSP_004347.
FT   VAR_SEQ     814    830       Missing (in isoform A5).
FT                                /FTId=VSP_004345.
FT   CONFLICT    786    786       G -> I (in Ref. 1; AAC53380/AAC53381).
SQ   SEQUENCE   931 AA;  104559 MW;  76F2443F411D2F63 CRC64;
     MDMFPLTWVF LALYFSGHEV RSQQDPPCGG RPNSKDAGYI TSPGYPQDYP SHQNCEWIVY
     APEPNQKIVL NFNPHFEIEK HDCKYDFIEI RDGDSESADL LGKHCGNIAP PTIISSGSVL
     YIKFTSDYAR QGAGFSLRYE IFKTGSEDCS KNFTSPNGTI ESPGFPEKYP HNLDCTFTIL
     AKPRMEIILQ FLTFDLEHDP LQVGEGDCKY DWLDIWDGIP HVGPLIGKYC GTKTPSKLRS
     STGILSLTFH TDMAVAKDGF SARYYLIHQE PPENFQCNVP LGMESGRIAN EQISASSTFS
     DGRWTPQQSR LHGDDNGWTP NLDSNKEYLQ VDLRFLTMLT AIATQGAISR ETQKGYYVKS
     YKLEVSTNGE DWMVYRHGKN HKIFQANNDA TEVVLNKLHM PLLTRFIRIR PQTWHLGIAL
     RLELFGCRVT DAPCSNMLGM LSGLIADTQI SASSTREYLW SPSAARLVSS RSGWFPRNPQ
     AQPGEEWLQV DLGTPKTVKG VIIQGARGGD SITAVEARAF VRKFKVSYSL NGKDWEYIQD
     PRTQQTKLFE GNMHYDTPDI RRFDPVPAQY VRVYPERWSP AGIGMRLEVL GCDWTDSKPT
     VETLGPTVKS EETTTPYPMD EDATECGENC SFEDDKDLQL PSGFNCNFDF PEETCGWVYD
     HAKWLRSTWI SSANPNDRTF PDDKNFLKLQ SDGRREGQYG RLISPPVHLP RSPVCMEFQY
     QAMGGHGVAL QVVREASQES KLLWVIREDQ GSEWKHGRII LPSYDMEYQI VFEGVIGKGR
     SGEISGDDIR ISTDVPLENC MEPISAFAGE DFKVDIPETH GGEGYEDEID DEYEGDWSNS
     SSSTSGAGDP SSGKEKSWLY TLDPILITII AMSSLGVLLG ATCAGLLLYC TCSYSGLSSR
     SCTTLENYNF ELYDGLKHKV KINHQKCCSE A
//
ID   MRP1_MOUSE              Reviewed;        1528 AA.
AC   O35379;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Multidrug resistance-associated protein 1;
DE   AltName: Full=ATP-binding cassette sub-family C member 1;
DE   AltName: Full=Leukotriene C(4) transporter;
DE            Short=LTC4 transporter;
GN   Name=Abcc1; Synonyms=Abcc1a, Abcc1b, Mdrap, Mrp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RX   MEDLINE=96251691; PubMed=8649356;
RA   Stride B.D., Valdimarsson G., Gerlach J.H., Wilson G.M., Cole S.P.C.,
RA   Deeley R.G.;
RT   "Structure and expression of the messenger RNA encoding the murine
RT   multidrug resistance protein, an ATP-binding cassette transporter.";
RL   Mol. Pharmacol. 49:962-971(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   FUNCTION.
RX   PubMed=9281595;
RA   Stride B.D., Grant C.E., Loe D.W., Hipfner D.R., Cole S.P.C.,
RA   Deeley R.G.;
RT   "Pharmacological characterization of the murine and human orthologs of
RT   multidrug-resistance protein in transfected human embryonic kidney
RT   cells.";
RL   Mol. Pharmacol. 52:344-353(1997).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-878 AND SER-882, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Mediates export of organic anions and drugs from the
CC       cytoplasm. Mediates ATP-dependent transport of glutathione and
CC       glutathione conjugates, leukotriene C4, estradiol-17-beta-o-
CC       glucuronide, methotrexate, antiviral drugs and other xenobiotics.
CC       Confers resistance to anticancer drugs. Hydrolyzes ATP with low
CC       efficiency.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC
CC       family. Conjugate transporter (TC 3.A.1.208) subfamily.
CC   -!- SIMILARITY: Contains 2 ABC transmembrane type-1 domains.
CC   -!- SIMILARITY: Contains 2 ABC transporter domains.
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DR   EMBL; AF022908; AAB80938.1; -; mRNA.
DR   EMBL; AK029876; BAC26654.1; -; mRNA.
DR   IPI; IPI00129915; -.
DR   RefSeq; NP_032602.1; NM_008576.2.
DR   UniGene; Mm.196634; -.
DR   ProteinModelPortal; O35379; -.
DR   SMR; O35379; 611-871, 958-1525.
DR   STRING; O35379; -.
DR   PhosphoSite; O35379; -.
DR   PRIDE; O35379; -.
DR   Ensembl; ENSMUST00000100167; ENSMUSP00000097743; ENSMUSG00000023088.
DR   GeneID; 17250; -.
DR   KEGG; mmu:17250; -.
DR   UCSC; uc007yhj.1; mouse.
DR   CTD; 17250; -.
DR   MGI; MGI:102676; Abcc1.
DR   HOGENOM; HBG758042; -.
DR   HOVERGEN; HBG108314; -.
DR   InParanoid; O35379; -.
DR   OMA; YLATEVV; -.
DR   PhylomeDB; O35379; -.
DR   NextBio; 291714; -.
DR   ArrayExpress; O35379; -.
DR   Bgee; O35379; -.
DR   Genevestigator; O35379; -.
DR   GermOnline; ENSMUSG00000023088; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR017940; ABC_transporter_type1.
DR   InterPro; IPR001140; ABC_transptr_TM_dom.
DR   InterPro; IPR011527; ABC_transptrTM_dom_typ1.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR005292; Multidrug-R_assoc.
DR   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF90123; ABC_TM_1; 2.
DR   TIGRFAMs; TIGR00957; MRP_assoc_pro; 1.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Glycoprotein; Hydrolase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1   1528       Multidrug resistance-associated protein
FT                                1.
FT                                /FTId=PRO_0000093353.
FT   TOPO_DOM      1     33       Extracellular (By similarity).
FT   TRANSMEM     34     54       Helical; Name=1; (By similarity).
FT   TOPO_DOM     55     74       Cytoplasmic (By similarity).
FT   TRANSMEM     75     95       Helical; Name=2; (By similarity).
FT   TOPO_DOM     96    100       Extracellular (By similarity).
FT   TRANSMEM    101    121       Helical; Name=3; (By similarity).
FT   TOPO_DOM    122    133       Cytoplasmic (By similarity).
FT   TRANSMEM    134    154       Helical; Name=4; (By similarity).
FT   TOPO_DOM    155    172       Extracellular (By similarity).
FT   TRANSMEM    173    193       Helical; Name=5; (By similarity).
FT   TOPO_DOM    194    317       Cytoplasmic (By similarity).
FT   TRANSMEM    318    338       Helical; Name=6; (By similarity).
FT   TOPO_DOM    339    364       Extracellular (By similarity).
FT   TRANSMEM    365    385       Helical; Name=7; (By similarity).
FT   TOPO_DOM    386    441       Cytoplasmic (By similarity).
FT   TRANSMEM    442    462       Helical; Name=8; (By similarity).
FT   TOPO_DOM    463    465       Extracellular (By similarity).
FT   TRANSMEM    466    486       Helical; Name=9; (By similarity).
FT   TOPO_DOM    487    548       Cytoplasmic (By similarity).
FT   TRANSMEM    549    569       Helical; Name=10; (By similarity).
FT   TOPO_DOM    570    591       Extracellular (By similarity).
FT   TRANSMEM    592    612       Helical; Name=11; (By similarity).
FT   TOPO_DOM    613    963       Cytoplasmic (By similarity).
FT   TRANSMEM    964    984       Helical; Name=12; (By similarity).
FT   TOPO_DOM    985   1022       Extracellular (By similarity).
FT   TRANSMEM   1023   1043       Helical; Name=13; (By similarity).
FT   TOPO_DOM   1044   1086       Cytoplasmic (By similarity).
FT   TRANSMEM   1087   1107       Helical; Name=14; (By similarity).
FT   TOPO_DOM   1108   1108       Extracellular (By similarity).
FT   TRANSMEM   1109   1129       Helical; Name=15; (By similarity).
FT   TOPO_DOM   1130   1200       Cytoplasmic (By similarity).
FT   TRANSMEM   1201   1221       Helical; Name=16; (By similarity).
FT   TOPO_DOM   1222   1223       Extracellular (By similarity).
FT   TRANSMEM   1224   1244       Helical; Name=17; (By similarity).
FT   TOPO_DOM   1245   1528       Cytoplasmic (By similarity).
FT   DOMAIN      326    609       ABC transmembrane type-1 1.
FT   DOMAIN      644    868       ABC transporter 1.
FT   DOMAIN      971   1253       ABC transmembrane type-1 2.
FT   DOMAIN     1290   1524       ABC transporter 2.
FT   NP_BIND     678    685       ATP 1 (Potential).
FT   NP_BIND    1324   1331       ATP 2 (Potential).
FT   MOD_RES     878    878       Phosphoserine.
FT   MOD_RES     882    882       Phosphoserine.
FT   MOD_RES     912    912       Phosphoserine (By similarity).
FT   MOD_RES     914    914       Phosphoserine (By similarity).
FT   MOD_RES     927    927       Phosphoserine (By similarity).
FT   CARBOHYD     19     19       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1003   1003       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   1528 AA;  171185 MW;  68FD13667D61DBBB CRC64;
     MALRSFCSAD GSDPLWDWNV TWHTSNPDFT KCFQNTVLTW VPCFYLWSCF PLYFFYLSRH
     DRGYIQMTHL NKTKTALGFF LWIICWADLF YSFWERSQGV LRAPVLLVSP TLLGITMLLA
     TFLIQLERRK GVQSSGIMLT FWLVALLCAL AILRSKIISA LKKDAHVDVF RDSTFYLYFT
     LVLVQLVLSC FSDCSPLFSE TVHDRNPCPE SSASFLSRIT FWWITGMMVH GYRQPLESSD
     LWSLNKEDTS EEVVPVLVNN WKKECDKSRK QPVRIVYAPP KDPSKPKGSS QLDVNEEVEA
     LIVKSPHKDR EPSLFKVLYK TFGPYFLMSF LYKALHDLMM FAGPKILELI INFVNDREAP
     DWQGYFYTAL LFVSACLQTL ALHQYFHICF VSGMRIKTAV VGAVYRKALL ITNAARKSST
     VGEIVNLMSV DAQRFMDLAT YINMIWSAPL QVILALYFLW LSLGPSVLAG VAVMILMVPL
     NAVMAMKTKT YQVAHMKSKD NRIKLMNEIL NGIKVLKLYA WELAFQDKVM SIRQEELKVL
     KKSAYLAAVG TFTWVCTPFL VALSTFAVFV TVDERNILDA KKAFVSLALF NILRFPLNIL
     PMVISSIVQA SVSLKRLRIF LSHEELEPDS IERRSIKSGE GNSITVKNAT FTWARGEPPT
     LNGITFSIPE GALVAVVGQV GCGKSSLLSA LLAEMDKVEG HVTLKGSVAY VPQQAWIQND
     SLRENILFGH PLQENYYKAV MEACALLPDL EILPSGDRTE IGEKGVNLSG GQKQRVSLAR
     AVYSNSDIYL FDDPLSAVDA HVGKHIFEKV VGPMGLLKNK TRILVTHGIS YLPQVDVIIV
     MSGGKISEMG SYQELLDRDG AFAEFLRTYA NAEQDLASED DSVSGSGKES KPVENGMLVT
     DTVGKHLQRH LSNSSSHSGD TSQQHSSIAE LQKAGAKEET WKLMEADKAQ TGQVQLSVYW
     NYMKAIGLFI TFLSIFLFLC NHVSALASNY WLSLWTDDPP VVNGTQANRN FRLSVYGALG
     ILQGAAIFGY SMAVSIGGIF ASRRLHLDLL YNVLRSPMSF FERTPSGNLV NRFSKELDTV
     DSMIPQVIKM FMGSLFSVIG AVIIILLATP IAAVIIPPLG LVYFFVQRFY VASSRQLKRL
     ESVSRSPVYS HFNETLLGVS VIRAFEEQER FIHQSDLKVD ENQKAYYPSI VANRWLAVRL
     ECVGNCIVLF AALFAVISRH SLSAGLVGLS VSYSLQITAY LNWLVRMSSE METNIVAVER
     LKEYSETEKE APWQIQETAP PSTWPHSGRV EFRDYCLRYR EDLDLVLKHI NVTIEGGEKV
     GIVGRTGAGK SSLTLGLFRI NESAEGEIII DGVNIAKIGL HNLRFKITII PQDPVLFSGS
     LRMNLDPFSQ YSDEEVWMAL ELAHLKGFVS ALPDKLNHEC AEGGENLSVG QRQLVCLARA
     LLRKTKILVL DEATAAVDLE TDNLIQSTIR TQFEDCTVLT IAHRLNTIMD YTRVIVLDKG
     EVRECGAPSE LLQQRGIFYS MAKDAGLV
//
ID   EXOC4_MOUSE             Reviewed;         975 AA.
AC   O35382;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2002, sequence version 2.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Exocyst complex component 4;
DE   AltName: Full=Exocyst complex component Sec8;
GN   Name=Exoc4; Synonyms=Sec8, Sec8l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=98104241; PubMed=9441674; DOI=10.1006/dbio.1997.8727;
RA   Friedrich G.A., Hildebrand J.D., Soriano P.;
RT   "The secretory protein Sec8 is required for paraxial mesoderm
RT   formation in the mouse.";
RL   Dev. Biol. 192:364-374(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Component of the exocyst complex involved in the docking
CC       of exocystic vesicles with fusion sites on the plasma membrane.
CC   -!- SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3,
CC       EXOC4, EXOC5, EXOC6, EXOC7 and EXOC8 (By similarity).
CC   -!- SIMILARITY: Belongs to the SEC8 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF022962; AAB86537.1; -; mRNA.
DR   EMBL; BC034644; AAH34644.1; -; mRNA.
DR   IPI; IPI00129959; -.
DR   RefSeq; NP_033174.2; NM_009148.3.
DR   UniGene; Mm.265512; -.
DR   ProteinModelPortal; O35382; -.
DR   MINT; MINT-1897858; -.
DR   STRING; O35382; -.
DR   PhosphoSite; O35382; -.
DR   PRIDE; O35382; -.
DR   Ensembl; ENSMUST00000052266; ENSMUSP00000051965; ENSMUSG00000029763.
DR   GeneID; 20336; -.
DR   KEGG; mmu:20336; -.
DR   UCSC; uc009bgt.1; mouse.
DR   CTD; 20336; -.
DR   MGI; MGI:1096376; Exoc4.
DR   eggNOG; roNOG05456; -.
DR   HOVERGEN; HBG036151; -.
DR   InParanoid; O35382; -.
DR   OMA; TCLLVLH; -.
DR   OrthoDB; EOG4GB75C; -.
DR   PhylomeDB; O35382; -.
DR   NextBio; 298147; -.
DR   ArrayExpress; O35382; -.
DR   Bgee; O35382; -.
DR   CleanEx; MM_EXOC4; -.
DR   Genevestigator; O35382; -.
DR   GermOnline; ENSMUSG00000029763; Mus musculus.
DR   GO; GO:0000145; C:exocyst; IEA:InterPro.
DR   GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; IEA:InterPro.
DR   InterPro; IPR007191; Sec8_exocyst.
DR   Pfam; PF04048; Sec8_exocyst; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Coiled coil; Exocytosis; Phosphoprotein;
KW   Protein transport; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    975       Exocyst complex component 4.
FT                                /FTId=PRO_0000118935.
FT   COILED       32    114       Potential.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       9      9       N6-acetyllysine (By similarity).
FT   MOD_RES     226    226       Phosphoserine (By similarity).
FT   MOD_RES     238    238       Phosphothreonine (By similarity).
FT   CONFLICT    692    692       G -> A (in Ref. 1; AAB86537).
FT   CONFLICT    717    717       S -> R (in Ref. 1; AAB86537).
FT   CONFLICT    832    832       S -> T (in Ref. 1; AAB86537).
FT   CONFLICT    949    975       RLQRLKEIICEQAAIKQATKDKKITTV -> SCRDSRRSSV
FT                                SRLPSSKPPRTRK (in Ref. 1; AAB86537).
SQ   SEQUENCE   975 AA;  110545 MW;  8DB5E154FA44E52A CRC64;
     MAAEAAGGKY RSTVSKSKDP SGLLISVIRT LSTSDDVEDR ENEKGRLEEA YEKCDRDLDE
     LIVQHYTELT TAIRTYQSIT ERITNSRNKI KQVKENLLSC KMLLHCKRDE LRKLWIEGIE
     HKHVLNLLDE IENIKQVPQK LEQCMASKHY LSATDMLVSA VESLEGPLLQ VEGLSDLRLE
     LHSKKMNLHL VLIEELHRHL YIKSTSRVVQ RNKEKGKMSS HGKDPSPGPL IDVSNIPTPR
     KFLDASQYSA AGGSSVREMN LQDVKEDLEC DPEENSTLFM GILIQGLARL KKIPETVKAI
     KERLEQELKQ IVKRSTTQVA DSAYQRGESL TVDNQPRLLL ELLELLFDKF NAVATAHSVV
     LGYLQDSVGT QLTQQEEIKL YDMADVWVKI QDVLQMLLTE YLDMKNTRTA SEPSAQLSYA
     STGREFAAFF AKKKPQRPKN SLFKFESSSH AISMSAYLRE QRRELYSRSG ELQGGPDDNL
     IEGGGTKFVC KPGARNITVI FHPLLRFIQE IEHALGLGPA KQCPLREFLT VYIKSIFLNQ
     VLAEINKEIE GVTKTSDPLK ILANADTMKV LGVQRPLLQS TIIVEKTVQD LMNLMHDLSA
     YSDQFLNMVC VKLQEYKDTC STAYRGIVQS EEKLVISASW AKDDDISRLL KSLPNWTNMA
     QPKQLRPKRE EEEDFIRAAF GKESEVLIGN LGDKLIPPQD ILRDVSDLKA LANMHESLEW
     LAGRTKSAFS NLSTSQMLSP AQESHVNMDL PPVSEQIMQT LSELAKTFQD MADRCLLVLH
     LEVRVHCFHY LIPLAKEGNY AIVANVESMD YDPLVVKLNK DISAMEEAMS ASLQQHKFQY
     IFEGLGHLIS CILINGAQYF RRISESGIKK MCRNIFVLQQ NLTNITMSRE ADLDFARQYY
     EMLYNTADEL LNLVVDQGVK YTELEYIHAL TLLHRSQTGV GDQTTQNTRL QRLKEIICEQ
     AAIKQATKDK KITTV
//
ID   EFNB3_MOUSE             Reviewed;         340 AA.
AC   O35393;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Ephrin-B3;
DE   Flags: Precursor;
GN   Name=Efnb3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=98143367; PubMed=9484836; DOI=10.1038/sj.onc.1201557;
RA   Bergemann A.D., Zhang L., Chiang M.-K., Brambilla R., Klein R.,
RA   Flanagan J.G.;
RT   "Ephrin-B3, a ligand for the receptor EphB3, expressed at the midline
RT   of the developing neural tube.";
RL   Oncogene 16:471-480(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION.
RX   MEDLINE=20171264; PubMed=10704386;
RA   Imondi R., Wideman C., Kaprielian Z.;
RT   "Complementary expression of transmembrane ephrins and their receptors
RT   in the mouse spinal cord: a possible role in constraining the
RT   orientation of longitudinally projecting axons.";
RL   Development 127:1397-1410(2000).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-210, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: May play a pivotal role in forebrain function. Binds to,
CC       and induce the collapse of, commissural axons/growth cones in
CC       vitro. May play a role in constraining the orientation of
CC       longitudinally projecting axons.
CC   -!- SUBUNIT: Interacts with GRIP1 and GRIP2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Expressed on lateral floor plate cells,
CC       specifically on commissural axon segments that have passed through
CC       the floor plate. Expressed in cells of the retinal ganglion cell
CC       layer during retinal axon guidance to the optic disk.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the floor plate throughout the
CC       period of commissural axon pathfinding.
CC   -!- SIMILARITY: Belongs to the ephrin family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF025288; AAC53537.1; -; mRNA.
DR   EMBL; BC052001; AAH52001.1; -; mRNA.
DR   EMBL; BC058617; AAH58617.1; -; mRNA.
DR   IPI; IPI00130008; -.
DR   RefSeq; NP_031937.1; NM_007911.5.
DR   UniGene; Mm.249637; -.
DR   PDB; 3D12; X-ray; 3.00 A; B/E=29-169.
DR   PDBsum; 3D12; -.
DR   ProteinModelPortal; O35393; -.
DR   SMR; O35393; 29-169.
DR   DIP; DIP-44833N; -.
DR   STRING; O35393; -.
DR   PhosphoSite; O35393; -.
DR   PRIDE; O35393; -.
DR   Ensembl; ENSMUST00000004036; ENSMUSP00000004036; ENSMUSG00000003934.
DR   GeneID; 13643; -.
DR   KEGG; mmu:13643; -.
DR   UCSC; uc007jqi.1; mouse.
DR   CTD; 13643; -.
DR   MGI; MGI:109196; Efnb3.
DR   eggNOG; roNOG09064; -.
DR   HOGENOM; HBG443543; -.
DR   HOVERGEN; HBG051448; -.
DR   InParanoid; O35393; -.
DR   OMA; MGAPHSG; -.
DR   OrthoDB; EOG4ZW5BN; -.
DR   PhylomeDB; O35393; -.
DR   NextBio; 284350; -.
DR   ArrayExpress; O35393; -.
DR   Bgee; O35393; -.
DR   CleanEx; MM_EFNB3; -.
DR   Genevestigator; O35393; -.
DR   GermOnline; ENSMUSG00000003934; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0016198; P:axon choice point recognition; IMP:MGI.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR001799; Ephrin.
DR   InterPro; IPR019765; Ephrin_CS.
DR   Gene3D; G3DSA:2.60.40.420; Cupredoxin; 1.
DR   PANTHER; PTHR11304; Ephrin; 1.
DR   Pfam; PF00812; Ephrin; 1.
DR   PRINTS; PR01347; EPHRIN.
DR   ProDom; PD002533; Ephrin; 1.
DR   SUPFAM; SSF49503; Cupredoxin; 1.
DR   PROSITE; PS01299; EPHRIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Developmental protein; Differentiation; Disulfide bond;
KW   Glycoprotein; Membrane; Neurogenesis; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     27       Potential.
FT   CHAIN        28    340       Ephrin-B3.
FT                                /FTId=PRO_0000008396.
FT   TOPO_DOM     28    227       Extracellular (Potential).
FT   TRANSMEM    228    248       Helical; (Potential).
FT   TOPO_DOM    249    340       Cytoplasmic (Potential).
FT   MOTIF       338    340       PDZ-binding (Potential).
FT   CARBOHYD    210    210       N-linked (GlcNAc...).
FT   DISULFID     62    104       By similarity.
FT   DISULFID     92    156       By similarity.
FT   STRAND       57     62
FT   STRAND       80     84
FT   STRAND       99    103
FT   STRAND      107    109
FT   STRAND      111    119
FT   STRAND      134    139
FT   TURN        156    158
FT   STRAND      162    166
SQ   SEQUENCE   340 AA;  35885 MW;  52F3D58FD209A6B8 CRC64;
     MGAPHFGPGG VQVGALLLLG FAGLVSGLSL EPVYWNSANK RFQAEGGYVL YPQIGDRLDL
     LCPRARPPGP HSSPSYEFYK LYLVEGAQGR RCEAPPAPNL LLTCDRPDLD LRFTIKFQEY
     SPNLWGHEFR SHHDYYIIAT SDGTREGLES LQGGVCLTRG MKVLLRVGQS PRGGAVPRKP
     VSEMPMERDR GAAHSAEPGR DTIPGDPSSN ATSRGAEGPL PPPSMPAVAG AAGGMALLLL
     GVAGAGGAMC WRRRRAKPSE SRHPGPGSFG RGGSLGLGGG GGMGPREAEP GELGIALRGG
     GTADPPFCPH YEKVSGDYGH PVYIVQDGPP QSPPNIYYKV
//
ID   BOK_MOUSE               Reviewed;         213 AA.
AC   O35425;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Bcl-2-related ovarian killer protein;
DE   AltName: Full=Apoptosis activator Mtd;
DE   AltName: Full=Protein matador;
GN   Name=Bok; Synonyms=Mtd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP   AND MUTAGENESIS OF LEU-71; LEU-74 AND LEU-78.
RX   PubMed=9535847; DOI=10.1074/jbc.273.15.8705;
RA   Inohara N., Ekhterae D., Garcia I., Carrio R., Merino J., Merry A.,
RA   Chen S., Nunez G.;
RT   "Mtd, a novel Bcl-2 family member activates apoptosis in the absence
RT   of heterodimerization with Bcl-2 and Bcl-XL.";
RL   J. Biol. Chem. 273:8705-8710(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in apoptosis.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, liver, lymphoid tissues
CC       and in embryonic intestinal epithelium.
CC   -!- DEVELOPMENTAL STAGE: At E15.0, expressed in brain, liver, thymus,
CC       lung, intestinal epithelium and follicles of the whiskers.
CC   -!- MISCELLANEOUS: 'Matador' means killer in Spanish.
CC   -!- SIMILARITY: Belongs to the Bcl-2 family.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AF027707; AAC53582.1; -; mRNA.
DR   EMBL; BC030069; AAH30069.1; -; mRNA.
DR   IPI; IPI00130704; -.
DR   RefSeq; NP_058058.1; NM_016778.2.
DR   UniGene; Mm.3295; -.
DR   ProteinModelPortal; O35425; -.
DR   STRING; O35425; -.
DR   PhosphoSite; O35425; -.
DR   PRIDE; O35425; -.
DR   Ensembl; ENSMUST00000027499; ENSMUSP00000027499; ENSMUSG00000026278.
DR   GeneID; 51800; -.
DR   KEGG; mmu:51800; -.
DR   UCSC; uc007cee.1; mouse.
DR   CTD; 51800; -.
DR   MGI; MGI:1858494; Bok.
DR   eggNOG; maNOG06918; -.
DR   HOGENOM; HBG445898; -.
DR   HOVERGEN; HBG050709; -.
DR   InParanoid; O35425; -.
DR   OMA; ELEYIRP; -.
DR   OrthoDB; EOG476K15; -.
DR   PhylomeDB; O35425; -.
DR   NextBio; 308052; -.
DR   ArrayExpress; O35425; -.
DR   Bgee; O35425; -.
DR   CleanEx; MM_BOK; -.
DR   Genevestigator; O35425; -.
DR   GermOnline; ENSMUSG00000026278; Mus musculus.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0006917; P:induction of apoptosis; IDA:MGI.
DR   InterPro; IPR002475; Bcl2-like_apoptosis.
DR   InterPro; IPR000712; Bcl2_BH.
DR   Pfam; PF00452; Bcl-2; 1.
DR   PRINTS; PR01862; BCL2FAMILY.
DR   SMART; SM00337; BCL; 1.
DR   PROSITE; PS50062; BCL2_FAMILY; 1.
DR   PROSITE; PS01080; BH1; FALSE_NEG.
DR   PROSITE; PS01258; BH2; FALSE_NEG.
DR   PROSITE; PS01259; BH3; FALSE_NEG.
DR   PROSITE; PS01260; BH4_1; FALSE_NEG.
DR   PROSITE; PS50063; BH4_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Apoptosis.
FT   CHAIN         1    213       Bcl-2-related ovarian killer protein.
FT                                /FTId=PRO_0000143087.
FT   MOTIF        32     44       BH4.
FT   MOTIF        67     83       BH3.
FT   MOTIF       113    132       BH1.
FT   MOTIF       165    179       BH2.
FT   MUTAGEN      71     71       L->Q: No change in apoptosis induction;
FT                                when associated with Q-74 and Q-78.
FT   MUTAGEN      74     74       L->Q: No change in apoptosis induction;
FT                                when associated with Q-71 and Q-78.
FT   MUTAGEN      78     78       L->Q: No change in apoptosis induction;
FT                                when associated with Q-71 and Q-74.
SQ   SEQUENCE   213 AA;  23456 MW;  F8755C45CB05D626 CRC64;
     MEVLRRSSVF AAEIMDAFDR SPTDKELVAQ AKALGREYVH ARLLRAGLSW SAPERASPAP
     GGRLAEVCTV LLRLGDELEQ IRPSVYRNVA RQLHIPLQSE PVVTDAFLAV AGHIFSAGIT
     WGKVVSLYSV AAGLAVDCVR QAQPAMVHAL VDCLGEFVRK TLATWLRRRG GWTDVLKCVV
     STDPGFRSHW LVATLCSFGR FLKAAFFLLL PER
//
ID   CLCN6_MOUSE             Reviewed;         870 AA.
AC   O35454;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   30-NOV-2010, entry version 86.
DE   RecName: Full=Chloride transport protein 6;
DE   AltName: Full=Chloride channel protein 6;
DE            Short=ClC-6;
GN   Name=Clcn6; Synonyms=Clc6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kornak U., Boesl M.R., Jentsch T.J.;
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
RC   TISSUE=Chronic myeloid leukemia cell;
RX   MEDLINE=97344267; PubMed=9224655;
RA   Eggermont J., Buyse G., Voets T., Tytgat J., De Smedt H.,
RA   Droogmans G., Nilius B.;
RT   "Alternative splicing of ClC-6 (a member of the ClC chloride-channel
RT   family) transcripts generates three truncated isoforms one of which,
RT   ClC-6c, is kidney-specific.";
RL   Biochem. J. 325:269-276(1997).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=16950870; DOI=10.1073/pnas.0606137103;
RA   Poet M., Kornak U., Schweizer M., Zdebik A.A., Scheel O., Hoelter S.,
RA   Wurst W., Schmitt A., Fuhrmann J.C., Planells-Cases R., Mole S.E.,
RA   Huebner C.A., Jentsch T.J.;
RT   "Lysosomal storage disease upon disruption of the neuronal chloride
RT   transport protein ClC-6.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:13854-13859(2006).
CC   -!- FUNCTION: Chloride transport protein, initially identified as
CC       voltage-gated chloride channel. The presence of the conserved
CC       gating glutamate residues suggests that is functions as
CC       antiporter.
CC   -!- SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=ClC-6a;
CC         IsoId=O35454-1; Sequence=Displayed;
CC       Name=ClC-6c;
CC         IsoId=O35454-2; Sequence=Not described;
CC   -!- TISSUE SPECIFICITY: Detected in whole brain and in hippocampus
CC       neurons (at protein level). Detected in brain, trigeminus, dorsal
CC       root ganglion, spinal cord, eye, kidney, testis, skeletal muscle,
CC       thymus and pancreas. Isoform ClC-6c is expressed only in kidney.
CC   -!- PTM: N-glycosylated on several asparagine residues (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Reduced pain sensitivity and moderate
CC       behavorial abnormalities, but have normal fertility and are
CC       generally not very different from wild-type.
CC   -!- MISCELLANEOUS: The CLC channel family contains both chloride
CC       channels and proton-coupled anion transporters that exchange
CC       chloride or another anion for protons. The presence of conserved
CC       gating glutamate residues is typical for family members that
CC       function as antiporters (By similarity).
CC   -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family.
CC       ClC-6/CLCN6 subfamily.
CC   -!- SIMILARITY: Contains 2 CBS domains.
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DR   EMBL; AF030106; AAC17702.1; -; Genomic_DNA.
DR   EMBL; AF030101; AAC17702.1; JOINED; Genomic_DNA.
DR   EMBL; AF030102; AAC17702.1; JOINED; Genomic_DNA.
DR   EMBL; AF030103; AAC17702.1; JOINED; Genomic_DNA.
DR   EMBL; AF030104; AAC17702.1; JOINED; Genomic_DNA.
DR   EMBL; AF030105; AAC17702.1; JOINED; Genomic_DNA.
DR   IPI; IPI00875404; -.
DR   RefSeq; NP_036059.1; NM_011929.2.
DR   UniGene; Mm.89987; -.
DR   ProteinModelPortal; O35454; -.
DR   SMR; O35454; 82-295, 804-866.
DR   STRING; O35454; -.
DR   TCDB; 2.A.49.3.4; chloride carrier/channel (ClC) family.
DR   PRIDE; O35454; -.
DR   Ensembl; ENSMUST00000030879; ENSMUSP00000030879; ENSMUSG00000029016.
DR   GeneID; 26372; -.
DR   KEGG; mmu:26372; -.
DR   UCSC; uc008vts.1; mouse.
DR   CTD; 26372; -.
DR   MGI; MGI:1347049; Clcn6.
DR   HOVERGEN; HBG050985; -.
DR   PhylomeDB; O35454; -.
DR   NextBio; 304269; -.
DR   ArrayExpress; O35454; -.
DR   Bgee; O35454; -.
DR   CleanEx; MM_CLCN6; -.
DR   Genevestigator; O35454; -.
DR   GermOnline; ENSMUSG00000029016; Mus musculus.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
DR   InterPro; IPR014743; Cl-channel_core.
DR   InterPro; IPR001807; Cl-channel_volt-gated.
DR   InterPro; IPR002248; Cl_channel-6.
DR   InterPro; IPR000644; Cysta_beta_synth_core.
DR   Gene3D; G3DSA:1.10.3080.10; Cl-channel_core; 2.
DR   PANTHER; PTHR11689; Cl-channel_volt; 1.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF00654; Voltage_CLC; 1.
DR   PRINTS; PR00762; CLCHANNEL.
DR   PRINTS; PR01117; CLCHANNEL6.
DR   SMART; SM00116; CBS; 2.
DR   SUPFAM; SSF81340; Cl-channel_core; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Antiport; ATP-binding; CBS domain; Chloride;
KW   Endosome; Glycoprotein; Ion transport; Membrane; Nucleotide-binding;
KW   Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    870       Chloride transport protein 6.
FT                                /FTId=PRO_0000094450.
FT   TOPO_DOM      1     80       Cytoplasmic (By similarity).
FT   TRANSMEM     81    113       Helical; (By similarity).
FT   TRANSMEM    128    150       Helical; (By similarity).
FT   INTRAMEM    159    166       Helical; (By similarity).
FT   TRANSMEM    176    194       Helical; (By similarity).
FT   TRANSMEM    200    217       Helical; (By similarity).
FT   INTRAMEM    241    253       Helical; (By similarity).
FT   INTRAMEM    257    265       Helical; (By similarity).
FT   TRANSMEM    277    294       Helical; (By similarity).
FT   TRANSMEM    335    364       Helical; (By similarity).
FT   TRANSMEM    371    392       Helical; (By similarity).
FT   TRANSMEM    463    482       Helical; (By similarity).
FT   TRANSMEM    488    512       Helical; (By similarity).
FT   INTRAMEM    520    534       Helical; (By similarity).
FT   INTRAMEM    535    537       Note=Loop between two helices; (By
FT                                similarity).
FT   INTRAMEM    538    549       Helical; (By similarity).
FT   INTRAMEM    550    553       Note=Loop between two helices; (By
FT                                similarity).
FT   TRANSMEM    554    572       Helical; (By similarity).
FT   TOPO_DOM    573    870       Cytoplasmic (By similarity).
FT   DOMAIN      606    663       CBS 1.
FT   DOMAIN      808    869       CBS 2.
FT   NP_BIND     631    633       ATP (By similarity).
FT   NP_BIND     850    853       ATP (By similarity).
FT   MOTIF       156    160       Selectivity filter part_1 (By
FT                                similarity).
FT   MOTIF       198    202       Selectivity filter part_2 (By
FT                                similarity).
FT   MOTIF       488    492       Selectivity filter part_3 (By
FT                                similarity).
FT   BINDING     157    157       Chloride (By similarity).
FT   BINDING     490    490       Chloride; via amide nitrogen (By
FT                                similarity).
FT   BINDING     577    577       Chloride (By similarity).
FT   SITE        200    200       Mediates proton transfer from the outer
FT                                aqueous phase to the interior of the
FT                                protein; involved in linking H(+) and
FT                                Cl(-) transport (By similarity).
FT   SITE        267    267       Mediates proton transfer from the protein
FT                                to the inner aqueous phase (By
FT                                similarity).
FT   CARBOHYD    410    410       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    423    423       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    433    433       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   870 AA;  96980 MW;  872C090069188749 CRC64;
     MAGCRGSVCC CCRWCCCCGE RESRTPEELT ILGETQEEED EILPRKDYES LDYDRCINDP
     YLEVLETMDN KKGRRYEAVK WMVVFAIGVC TGLVGLFVDF SVRLFTQLKF GVVQTSVEEC
     SQKGCLALSL LELLGFNLTF VFLASLLVLI EPVAAGSGIP EIKCYLNGVK VPGIVRLRTL
     LCKVFGVLFS VSGGLFVGKE GPMIHSGAVV GAGLPQFQSI SLRKIQFNFP YFRSDRDKRD
     FVSAGAAAGV AAAFGAPIGG TLFSLEEGSS FWNQGLTWKV LFCSMSATFT LNFFRSGIQF
     GSWGSFQLPG LLNFGEFKCS DSDKKCHLWT AMDLGFFVVM GVIGGLLGAT FNCLNKRLAK
     YRMRNVHPKP KLVRVLESLL VSLVTTVVVF VASMVLGECR QMSSTSQTGN GSFQLQVTSE
     DVNSTIKAFF CPNDTYNDMA TLFFNSQESA ILQLFHQDGT FSPVTLALFF ILYFLLACWT
     FGTSVPSGLF VPSLLCGAAF GRLVANVLKS YIGLGHLYSG TFALIGAAAF LGGVVRMTIS
     LTVILIESTN EITYGLPIMV TLMVAKWTGD LFNKGIYDVH IGLRGVPLLE WETDVEMDKL
     RASDIMEPNL TYVYPHTRIQ SLVSILRTTV HHAFPVVTEN RGNEKEFMKG NQLISNNIKF
     KKSSILTRAG EQRKRGQSMK SYPSSELRNV CDEHVASEEP AEKEDLLQQM LERRYTPYPN
     LYPDQSPSED WTMEERFRPL TFHGLVLRSQ LVTLLVRGVC YSESQSSASQ PRLSYAEMAE
     DYPRYPDIHD LDLTLLNPRM IVDVTPYMNP SPFTVSPNTH VSQVFNLFRT MGLRHLPVVN
     AVGEIVGIIT RHNLTNEFLQ ARLRQHYQTL
//
ID   FKBP8_MOUSE             Reviewed;         402 AA.
AC   O35465; Q3UK86; Q6GTX9; Q811M7; Q811R4; Q8C2F0; Q99L93;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   08-MAR-2011, entry version 102.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP8;
DE            Short=PPIase FKBP8;
DE            EC=5.2.1.8;
DE   AltName: Full=38 kDa FK506-binding protein;
DE            Short=38 kDa FKBP;
DE            Short=FKBP-38;
DE            Short=mFKBP38;
DE   AltName: Full=FK506-binding protein 8;
DE            Short=FKBP-8;
DE   AltName: Full=FKBPR38;
DE   AltName: Full=Rotamase;
GN   Name=Fkbp8; Synonyms=Fkbp38, Sam11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH BCL2 AND
RP   BCL2L1/BCLXL.
RX   MEDLINE=22399853; PubMed=12510191; DOI=10.1038/ncb894;
RA   Shirane M., Nakayama K.I.;
RT   "Inherent calcineurin inhibitor FKBP38 targets Bcl-2 to mitochondria
RT   and inhibits apoptosis.";
RL   Nat. Cell Biol. 5:28-37(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=15105374; DOI=10.1242/dev.01122;
RA   Bulgakov O.V., Eggenschwiler J.T., Hong D.-H., Anderson K.V., Li T.;
RT   "FKBP8 is a negative regulator of mouse sonic hedgehog signaling in
RT   neural tissues.";
RL   Development 131:2149-2159(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=BALB/c, C57BL/6J, and NOD;
RC   TISSUE=Bone marrow macrophage, Placenta, Spleen, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 39-402 (ISOFORM 1), SUBUNIT, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=C57BL/6 X DBA/2;
RX   MEDLINE=99211287; PubMed=10197430;
RX   DOI=10.1002/(SICI)1522-2683(19990201)20:2<249::AID-ELPS249>3.0.CO;2-F;
RA   Pedersen K.M., Finsen B., Celis J.E., Jensen N.A.;
RT   "muFKBP38: a novel murine immunophilin homolog differentially
RT   expressed in Schwannoma cells and central nervous system neurons in
RT   vivo.";
RL   Electrophoresis 20:249-255(1999).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 48-402, SEQUENCE REVISION TO 100
RP   AND 400, ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RC   STRAIN=129/SvJ;
RX   PubMed=14667822; DOI=10.1016/j.ygeno.2003.07.001;
RA   Nielsen J.V., Mitchelmore C., Pedersen K.M., Kjaerulff K.M.,
RA   Finsen B., Jensen N.A.;
RT   "Fkbp8: novel isoforms, genomic organization, and characterization of
RT   a forebrain promoter in transgenic mice.";
RL   Genomics 83:181-192(2004).
CC   -!- FUNCTION: Constitutively inactive PPiase, which becomes active
CC       when bound to calmodulin and calcium. Seems to act as a chaperone
CC       for BCL2, targets it to the mitochondria and modulates its
CC       phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex
CC       probably interferes with the binding of BCL2 to its targets. The
CC       active form of FKBP8 may therefore play a role in the regulation
CC       of apoptosis (By similarity). Required for normal embryonic
CC       development.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- COFACTOR: Calcium (By similarity).
CC   -!- SUBUNIT: Homomultimers or heteromultimers (Potential). Forms
CC       heterodimer with calmodulin. When activated by calmodulin and
CC       calcium, interacts with the BH4 domain of BCL2 and weakly with
CC       BCLX isoform Bcl-X(L). Does not bind and inhibit calcineurin (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane
CC       protein; Cytoplasmic side.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O35465-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O35465-2; Sequence=VSP_034487;
CC   -!- TISSUE SPECIFICITY: Detected throughout the embryonic body, in
CC       caudal neural tube, limbs and head. Detected in adult retina,
CC       brain, heart, kidney, liver, pancreas, lung, testis and urinary
CC       bladder (at protein level). Detected in adult brain, kidney,
CC       liver, testis and trigeminal nerve, and in embryo. Detected at
CC       lower levels in lung, spleen, heart and ovary. Widely expressed in
CC       forebrain. Detected in the Purkinje cell layer in the cerebellum
CC       and in hippocampus neurons.
CC   -!- MISCELLANEOUS: Binds the immunosuppressant FK506 only in its
CC       calmodulin/calcium activated form (By similarity).
CC   -!- SIMILARITY: Contains 1 PPIase FKBP-type domain.
CC   -!- SIMILARITY: Contains 3 TPR repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB86422.1; Type=Erroneous initiation;
CC       Sequence=AAH03739.1; Type=Erroneous initiation;
CC       Sequence=AAH27808.1; Type=Erroneous initiation;
CC       Sequence=AAO27795.1; Type=Erroneous gene model prediction;
CC       Sequence=BAC40541.1; Type=Erroneous initiation;
CC       Sequence=BAE26916.1; Type=Erroneous initiation;
CC       Sequence=BAE31027.1; Type=Erroneous initiation;
CC       Sequence=BAE38118.1; Type=Erroneous initiation;
CC       Sequence=BAE39713.1; Type=Erroneous initiation;
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AY225340; AAO39021.1; -; mRNA.
DR   EMBL; AY278608; AAQ84562.1; -; mRNA.
DR   EMBL; AK088739; BAC40541.1; ALT_INIT; mRNA.
DR   EMBL; AK146122; BAE26916.1; ALT_INIT; mRNA.
DR   EMBL; AK152198; BAE31027.1; ALT_INIT; mRNA.
DR   EMBL; AK165281; BAE38118.1; ALT_INIT; mRNA.
DR   EMBL; AK167663; BAE39713.1; ALT_INIT; mRNA.
DR   EMBL; BC003739; AAH03739.1; ALT_INIT; mRNA.
DR   EMBL; BC027808; AAH27808.1; ALT_INIT; mRNA.
DR   EMBL; AF030635; AAB86422.1; ALT_INIT; mRNA.
DR   EMBL; AY187231; AAO27795.1; ALT_SEQ; Genomic_DNA.
DR   IPI; IPI00130833; -.
DR   IPI; IPI00881287; -.
DR   RefSeq; NP_001104536.1; NM_001111066.1.
DR   RefSeq; NP_001186560.1; NM_001199631.1.
DR   RefSeq; NP_034353.2; NM_010223.2.
DR   UniGene; Mm.141864; -.
DR   ProteinModelPortal; O35465; -.
DR   SMR; O35465; 48-362.
DR   STRING; O35465; -.
DR   PhosphoSite; O35465; -.
DR   PRIDE; O35465; -.
DR   Ensembl; ENSMUST00000075491; ENSMUSP00000074935; ENSMUSG00000019428.
DR   GeneID; 14232; -.
DR   KEGG; mmu:14232; -.
DR   UCSC; uc009mat.1; mouse.
DR   CTD; 14232; -.
DR   MGI; MGI:1341070; Fkbp8.
DR   eggNOG; roNOG16878; -.
DR   GeneTree; ENSGT00550000074272; -.
DR   HOVERGEN; HBG051626; -.
DR   OMA; PLEDFEV; -.
DR   PhylomeDB; O35465; -.
DR   BRENDA; 5.2.1.8; 244.
DR   NextBio; 285507; -.
DR   ArrayExpress; O35465; -.
DR   Bgee; O35465; -.
DR   CleanEx; MM_FKBP8; -.
DR   Genevestigator; O35465; -.
DR   GermOnline; ENSMUSG00000019428; Mus musculus.
DR   GO; GO:0030176; C:integral to endoplasmic reticulum membrane; IDA:MGI.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR   GO; GO:0001708; P:cell fate specification; IMP:MGI.
DR   GO; GO:0021904; P:dorsal/ventral neural tube patterning; IDA:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IGI:MGI.
DR   GO; GO:0030513; P:positive regulation of BMP signaling pathway; IMP:MGI.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR   GO; GO:0010468; P:regulation of gene expression; IGI:MGI.
DR   GO; GO:0007224; P:smoothened signaling pathway; IGI:MGI.
DR   InterPro; IPR023114; Elongated_TPR_rpt_dom.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR001440; TPR-1.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.10.150.160; Elongated_TPR_rpt_dom; 1.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   Pfam; PF00515; TPR_1; 2.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
DR   PROSITE; PS50005; TPR; 2.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Apoptosis; Calcium; Isomerase;
KW   Membrane; Mitochondrion; Phosphoprotein; Repeat; Rotamase; TPR repeat;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    402       Peptidyl-prolyl cis-trans isomerase
FT                                FKBP8.
FT                                /FTId=PRO_0000075332.
FT   TRANSMEM    380    400       Helical; (Potential).
FT   DOMAIN      110    194       PPIase FKBP-type.
FT   REPEAT      211    244       TPR 1.
FT   REPEAT      262    295       TPR 2.
FT   REPEAT      296    329       TPR 3.
FT   COMPBIAS    252    256       Poly-Glu.
FT   MOD_RES     312    312       Phosphotyrosine (By similarity).
FT   MOD_RES     338    338       N6-acetyllysine (By similarity).
FT   VAR_SEQ     173    173       G -> GS (in isoform 2).
FT                                /FTId=VSP_034487.
FT   CONFLICT    100    100       G -> C (in Ref. 1; AAO39021, 2; AAQ84562,
FT                                4; AAH03739 and 5; AAB86422).
FT   CONFLICT    163    163       A -> T (in Ref. 3; BAE26916).
FT   CONFLICT    170    170       G -> A (in Ref. 3; BAC40541).
FT   CONFLICT    400    400       A -> G (in Ref. 1; AAO39021, 2; AAQ84562,
FT                                4; AAH03739 and 5; AAB86422).
SQ   SEQUENCE   402 AA;  43529 MW;  609A954FAD3A76F8 CRC64;
     MASWAEPSEP AALRLPGAPL LEGFEVLDGV DDAEEEDDLS GLPPLEDMGQ PTVEEAEQPG
     ALAREFLAAT EPEPAPAPAP EEWLDILGNG LLRMKTLVPG PKGSSRPLKG QVVTVHLQMS
     LENGTRVQEE PELAFTLGDC DVIQALDLSV PLMDVGETAM VTADSKYCYG PQGRSPYIPP
     HAALCLEVTL KTAEDGPDLE MLSGQERVAL ANRKRECGNA HYQRADFVLA ANSYDLAIKA
     ITSNTKVDMT CEEEEELLQL KVKCLNNLAA SQLKLDHYRA ALRSCSQVLE HQPDNIKALF
     RKGKVLAQQG EYSEAIPILR AALKLEPSNK TIHAELSKLV KKRAAQRSTE TALYRKMLGN
     PSRLPAKCPG KGAWSIPWKW LFGATAVALG GVALSVVIAA RN
//
ID   CLK3_MOUSE              Reviewed;         638 AA.
AC   O35492; Q3TJU0; Q3UIF5; Q3V463; Q5U4I1; Q8C1V1;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 2.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Dual specificity protein kinase CLK3;
DE            EC=2.7.12.1;
DE   AltName: Full=CDC-like kinase 3;
GN   Name=Clk3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Brain, Kidney, Placenta, Thymus, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 139-638.
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 141-638.
RX   MEDLINE=97439710; PubMed=9307018;
RA   Nayler O., Stamm S., Ullrich A.;
RT   "Characterization and comparison of four serine- and arginine-rich
RT   (SR) protein kinases.";
RL   Biochem. J. 326:693-700(1997).
RN   [4]
RP   TISSUE SPECIFICITY, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX   PubMed=10585269; DOI=10.1006/excr.1999.4655;
RA   Menegay H., Moeslein F., Landreth G.;
RT   "The dual specificity protein kinase CLK3 is abundantly expressed in
RT   mature mouse spermatozoa.";
RL   Exp. Cell Res. 253:463-473(1999).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-155, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Phosphorylates serine- and arginine-rich (SR) proteins
CC       of the spliceosomal complex. May be a constituent of a network of
CC       regulatory mechanisms that enable SR proteins to control RNA
CC       splicing. Phosphorylates serines, threonines and tyrosines.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm.
CC       Cytoplasmic vesicle, secretory vesicle, acrosome.
CC   -!- TISSUE SPECIFICITY: Present at high levels in testis and ovary. In
CC       testis, expression is restricted to elongated, maturing
CC       spermatozoa. Also present in spleen, brain, lung and liver (at
CC       protein level).
CC   -!- PTM: Autophosphorylates on all three types of residues.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. Lammer subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB87509.1; Type=Erroneous initiation;
CC       Sequence=AAH85084.1; Type=Erroneous initiation;
CC       Sequence=BAC41138.1; Type=Erroneous initiation;
CC       Sequence=BAE21937.1; Type=Erroneous initiation;
CC       Sequence=BAE32308.1; Type=Erroneous initiation;
CC       Sequence=BAE39405.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAE39405.1; Type=Frameshift; Positions=15;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK090215; BAC41138.1; ALT_INIT; mRNA.
DR   EMBL; AK133936; BAE21937.1; ALT_INIT; mRNA.
DR   EMBL; AK146942; BAE27551.1; -; mRNA.
DR   EMBL; AK154003; BAE32308.1; ALT_INIT; mRNA.
DR   EMBL; AK167300; BAE39405.1; ALT_SEQ; mRNA.
DR   EMBL; AK009908; BAE43216.1; -; mRNA.
DR   EMBL; BC085084; AAH85084.1; ALT_INIT; mRNA.
DR   EMBL; AF033565; AAB87509.1; ALT_INIT; mRNA.
DR   IPI; IPI00314963; -.
DR   RefSeq; NP_031739.3; NM_007713.4.
DR   UniGene; Mm.25720; -.
DR   ProteinModelPortal; O35492; -.
DR   SMR; O35492; 284-629.
DR   STRING; O35492; -.
DR   PhosphoSite; O35492; -.
DR   PRIDE; O35492; -.
DR   Ensembl; ENSMUST00000065330; ENSMUSP00000067341; ENSMUSG00000032316.
DR   GeneID; 102414; -.
DR   KEGG; mmu:102414; -.
DR   CTD; 102414; -.
DR   MGI; MGI:1098670; Clk3.
DR   eggNOG; roNOG09009; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG107720; -.
DR   InParanoid; O35492; -.
DR   OMA; CRKRRTR; -.
DR   OrthoDB; EOG49ZXP2; -.
DR   PhylomeDB; O35492; -.
DR   BRENDA; 2.7.12.1; 244.
DR   NextBio; 355462; -.
DR   ArrayExpress; O35492; -.
DR   Bgee; O35492; -.
DR   CleanEx; MM_CLK3; -.
DR   Genevestigator; O35492; -.
DR   GermOnline; ENSMUSG00000032316; Mus musculus.
DR   GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IDA:MGI.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Cytoplasmic vesicle; Kinase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT   CHAIN         1    638       Dual specificity protein kinase CLK3.
FT                                /FTId=PRO_0000085871.
FT   DOMAIN      304    620       Protein kinase.
FT   NP_BIND     310    318       ATP (By similarity).
FT   COMPBIAS      7    264       Arg-rich.
FT   ACT_SITE    431    431       Proton acceptor (By similarity).
FT   BINDING     334    334       ATP (By similarity).
FT   MOD_RES     155    155       Phosphotyrosine.
FT   MOD_RES     157    157       Phosphoserine (By similarity).
FT   MOD_RES     197    197       Phosphoserine (By similarity).
FT   MOD_RES     199    199       Phosphoserine (By similarity).
FT   MOD_RES     215    215       Phosphoserine (By similarity).
FT   MOD_RES     224    224       Phosphoserine (By similarity).
FT   MOD_RES     226    226       Phosphoserine (By similarity).
FT   MOD_RES     283    283       Phosphoserine (By similarity).
FT   CONFLICT     68     68       P -> T (in Ref. 1; BAE39405).
FT   CONFLICT    165    165       S -> T (in Ref. 3; AAB87509).
FT   CONFLICT    314    314       T -> L (in Ref. 1; BAE43216).
FT   CONFLICT    428    428       T -> A (in Ref. 1; BAC41138).
SQ   SEQUENCE   638 AA;  73798 MW;  3CE7BFD35FB09A3C CRC64;
     MPVLSARRKR LASTAGPRRG SGPSLAVRWV PPLGPEPSSD RGRAPMRPRG PTCSTTRRGA
     GRGPRLLPGP PGRDLHRCRP DPGGAGQSPR VCEFGARAVR PLGRVEPGPP TAASREGAVL
     PRAEARAGSG RGARSGEWGL AAAGAWETMH HCKRYRSPEP DPYLSYRWKR RRSYSREHEG
     RLRYPSRREP PPRRSRSRSH DRIPYQRRYR EHRDSDTYRC EERSPSFGED CYGSSRSRHR
     RRSRERAPYR TRKHAHHCHK RRTRSCSSAS SRSQQSSKRS SRSVEDDKEG HLVCRIGDWL
     QERYEIVGNL GEGTFGKVVE CLDHARGKSQ VALKIIRNVG KYREAARLEI NVLKKIKEKD
     KENKFLCVLM SDWFNFHGHM CIAFELLGKN TFEFLKENNF QPYPLPHVRH MAYQLCHALR
     FLHENQLTHT DLKPENILFV NSEFETLYNE HKSCEEKSVK NTSIRVADFG SATFDHEHHT
     TIVATRHYRP PEVILELGWA QPCDVWSIGC ILFEYYRGFT LFQTHENREH LVMMEKILGP
     IPSHMIHRTR KQKYFYKGGL VWDENSSDGR YVKENCKPLK SYMLQDSLEH VQLFDLMRRM
     LEFDPAQRIT LAEALLHPFF AGLTPEERSF HSSRNPSR
//
ID   CLK4_MOUSE              Reviewed;         481 AA.
AC   O35493; O35721; Q8CEU9; Q99LU6;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   11-JAN-2011, entry version 84.
DE   RecName: Full=Dual specificity protein kinase CLK4;
DE            EC=2.7.12.1;
DE   AltName: Full=CDC-like kinase 4;
GN   Name=Clk4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=97439710; PubMed=9307018;
RA   Nayler O., Stamm S., Ullrich A.;
RT   "Characterization and comparison of four serine- and arginine-rich
RT   (SR) protein kinases.";
RL   Biochem. J. 326:693-700(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-219.
RX   MEDLINE=97480726; PubMed=9339371; DOI=10.1006/geno.1997.4931;
RA   Watkins-Chow D.E., Douglas K.R., Buckwalter M.S., Probst F.J.,
RA   Camper S.A.;
RT   "Construction of a 3-Mb contig and partial transcript map of the
RT   central region of mouse chromosome 11.";
RL   Genomics 45:147-157(1997).
RN   [5]
RP   FUNCTION.
RX   MEDLINE=21354768; PubMed=11461155; DOI=10.1006/mcne.2001.1000;
RA   Hartmann A.M., Rujescu D., Giannakouros T., Nikolakaki E., Goedert M.,
RA   Mandelkow E.-M., Gao Q.S., Andreadis A., Stamm S.;
RT   "Regulation of alternative splicing of human tau exon 10 by
RT   phosphorylation of splicing factors.";
RL   Mol. Cell. Neurosci. 18:80-90(2001).
RN   [6]
RP   TISSUE SPECIFICITY, AND MUTAGENESIS OF LYS-189.
RX   MEDLINE=22313485; PubMed=12169693; DOI=10.1074/jbc.M206504200;
RA   Katsu R., Onogi H., Wada K., Kawaguchi Y., Hagiwara M.;
RT   "Novel SR-rich-related protein Clasp specifically interacts with
RT   inactivated Clk4 and induces the exon EB inclusion of Clk.";
RL   J. Biol. Chem. 277:44220-44228(2002).
CC   -!- FUNCTION: Phosphorylates serine- and arginine-rich (SR) proteins
CC       of the spliceosomal complex may be a constituent of a network of
CC       regulatory mechanisms that enable SR proteins to control RNA
CC       splicing. Phosphorylates serines, threonines and tyrosines.
CC       Required for the regulation of alternative splicing of MAPT/TAU.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts with UBL5 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O35493-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O35493-2; Sequence=VSP_008205;
CC   -!- TISSUE SPECIFICITY: Expressed in the hippocampus, the cerebellum
CC       and the olfactory bulb.
CC   -!- PTM: Autophosphorylates on all three types of residues.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. Lammer subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF033566; AAB87510.1; -; mRNA.
DR   EMBL; AK013974; BAC25420.1; -; mRNA.
DR   EMBL; BC002220; AAH02220.1; -; mRNA.
DR   EMBL; BC012675; AAH12675.1; -; mRNA.
DR   EMBL; U94846; AAB62179.1; -; mRNA.
DR   IPI; IPI00130955; -.
DR   IPI; IPI00341291; -.
DR   RefSeq; NP_031740.1; NM_007714.5.
DR   UniGene; Mm.239354; -.
DR   ProteinModelPortal; O35493; -.
DR   SMR; O35493; 146-479.
DR   STRING; O35493; -.
DR   PhosphoSite; O35493; -.
DR   PRIDE; O35493; -.
DR   Ensembl; ENSMUST00000093132; ENSMUSP00000090820; ENSMUSG00000020385.
DR   GeneID; 12750; -.
DR   KEGG; mmu:12750; -.
DR   UCSC; uc007itr.1; mouse.
DR   CTD; 12750; -.
DR   MGI; MGI:1098551; Clk4.
DR   eggNOG; roNOG06585; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG107720; -.
DR   InParanoid; O35493; -.
DR   OMA; ECIDHDM; -.
DR   PhylomeDB; O35493; -.
DR   BRENDA; 2.7.12.1; 244.
DR   NextBio; 282080; -.
DR   ArrayExpress; O35493; -.
DR   Bgee; O35493; -.
DR   CleanEx; MM_CLK4; -.
DR   Genevestigator; O35493; -.
DR   GermOnline; ENSMUSG00000020385; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IDA:MGI.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Serine/threonine-protein kinase; Transferase;
KW   Tyrosine-protein kinase.
FT   CHAIN         1    481       Dual specificity protein kinase CLK4.
FT                                /FTId=PRO_0000085874.
FT   DOMAIN      159    475       Protein kinase.
FT   NP_BIND     165    173       ATP (By similarity).
FT   ACT_SITE    286    286       Proton acceptor (By similarity).
FT   BINDING     189    189       ATP (By similarity).
FT   MOD_RES     136    136       Phosphoserine (By similarity).
FT   MOD_RES     138    138       Phosphoserine (By similarity).
FT   VAR_SEQ       1    180       Missing (in isoform 2).
FT                                /FTId=VSP_008205.
FT   MUTAGEN     189    189       K->R: Loss of function.
FT   CONFLICT     58     58       E -> Q (in Ref. 4; AAB62179).
FT   CONFLICT    141    141       D -> N (in Ref. 4; AAB62179).
FT   CONFLICT    344    344       R -> K (in Ref. 2; BAC25420).
SQ   SEQUENCE   481 AA;  57345 MW;  F2C56965900C12AA CRC64;
     MRHSKRTHCP DWDSRESWGH ESYSGSHKRK RRSHSSTQEN RHCKPHHQFK DSDCHYLEAR
     CLNERDYRDR RYIDEYRNDY CEGYVPRHYH RDVESTYRIH CSKSSVRSRR SSPKRKRNRP
     CASHQSHSKS HRRKRSRSIE DDEEGHLICQ SGDVLRARYE IVDTLGEGAF GKVVECIDHG
     MDGLHVAVKI VKNVGRYREA ARSEIQVLEH LNSTDPNSVF RCVQMLEWFD HHGHVCIVFE
     LLGLSTYDFI KENSFLPFQI DHIRQMAYQI CQSINFLHHN KLTHTDLKPE NILFVKSDYV
     VKYNSKMKRD ERTLKNTDIK VVDFGSATYD DEHHSTLVST RHYRAPEVIL ALGWSQPCDV
     WSIGCILIEY YLGFTVFQTH DSKEHLAMME RILGPIPAHM IQKTRKRKYF HHNQLDWDEH
     SSAGRYVRRR CKPLKEFMLC HDEEHEKLFD LVRRMLEYDP ARRITLDEAL QHPFFDLLKR
     K
//
ID   STX1A_MOUSE             Reviewed;         288 AA.
AC   O35526;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   19-DEC-2001, sequence version 3.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Syntaxin-1A;
DE   AltName: Full=Neuron-specific antigen HPC-1;
GN   Name=Stx1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Fujiwara T., Genda M., Nagai A., Okazaki M., Watanabe T.,
RA   Nagamatsu S., Akagawa K.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 29-41; 47-56; 58-84; 95-108; 126-142; 152-158 AND
RP   233-246, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [3]
RP   INTERACTION WITH SYTL4.
RX   MEDLINE=22095988; PubMed=12101244;
RX   DOI=10.1128/MCB.22.15.5518-5526.2002;
RA   Torii S., Zhao S., Yi Z., Takeuchi T., Izumi T.;
RT   "Granuphilin modulates the exocytosis of secretory granules through
RT   interaction with syntaxin 1a.";
RL   Mol. Cell. Biol. 22:5518-5526(2002).
RN   [4]
RP   INTERACTION WITH OTOF.
RC   STRAIN=BALB/c; TISSUE=Cochlea;
RX   PubMed=17055430; DOI=10.1016/j.cell.2006.08.040;
RA   Roux I., Safieddine S., Nouvian R., Grati M., Simmler M.-C.,
RA   Bahloul A., Perfettini I., Le Gall M., Rostaing P., Hamard G.,
RA   Triller A., Avan P., Moser T., Petit C.;
RT   "Otoferlin, defective in a human deafness form, is essential for
RT   exocytosis at the auditory ribbon synapse.";
RL   Cell 127:277-289(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH LGI3.
RX   PubMed=18760330; DOI=10.1016/j.neulet.2008.08.044;
RA   Park W.-J., Lee S.E., Kwon N.S., Baek K.J., Kim D.-S., Yun H.-Y.;
RT   "Leucine-rich glioma inactivated 3 associates with syntaxin 1.";
RL   Neurosci. Lett. 444:240-244(2008).
CC   -!- FUNCTION: Potentially involved in docking of synaptic vesicles at
CC       presynaptic active zones. May play a critical role in
CC       neurotransmitter exocytosis.
CC   -!- SUBUNIT: Part of the SNARE core complex containing SNAP25, VAMP2
CC       and STX1A. This complex binds to CPLX1. Interacts with VAPA and
CC       SYBU. Binds STXBP6. Found in a complex with VAMP8 and SNAP23.
CC       Found in a ternary complex with STX1A and SNAP25 (By similarity).
CC       Interacts with SLC6A4 (By similarity). Binds SYTL4. Interacts with
CC       OTOF and LGI3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane; Single-pass type IV membrane protein.
CC       Cell junction, synapse, synaptosome.
CC   -!- SIMILARITY: Belongs to the syntaxin family.
CC   -!- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain.
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DR   EMBL; D45208; BAA28865.2; -; mRNA.
DR   IPI; IPI00131618; -.
DR   RefSeq; NP_058081.2; NM_016801.3.
DR   UniGene; Mm.6225; -.
DR   ProteinModelPortal; O35526; -.
DR   SMR; O35526; 2-286.
DR   MINT; MINT-2411610; -.
DR   STRING; O35526; -.
DR   PhosphoSite; O35526; -.
DR   PRIDE; O35526; -.
DR   Ensembl; ENSMUST00000005509; ENSMUSP00000005509; ENSMUSG00000007207.
DR   GeneID; 20907; -.
DR   KEGG; mmu:20907; -.
DR   UCSC; uc008zxk.1; mouse.
DR   CTD; 20907; -.
DR   MGI; MGI:109355; Stx1a.
DR   eggNOG; roNOG09503; -.
DR   HOGENOM; HBG717663; -.
DR   HOVERGEN; HBG000497; -.
DR   InParanoid; O35526; -.
DR   OMA; GIEQSIE; -.
DR   OrthoDB; EOG4PC9SV; -.
DR   PhylomeDB; O35526; -.
DR   NextBio; 299781; -.
DR   ArrayExpress; O35526; -.
DR   Bgee; O35526; -.
DR   CleanEx; MM_STX1A; -.
DR   Genevestigator; O35526; -.
DR   GermOnline; ENSMUSG00000007207; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR   GO; GO:0070044; C:synaptobrevin 2-SNAP-25-syntaxin-1a complex; IDA:MGI.
DR   GO; GO:0019717; C:synaptosome; IDA:UniProtKB.
DR   GO; GO:0019855; F:calcium channel inhibitor activity; IMP:MGI.
DR   GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR   GO; GO:0000149; F:SNARE binding; IDA:MGI.
DR   GO; GO:0017156; P:calcium ion-dependent exocytosis; IMP:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   InterPro; IPR015709; Syntaxin-1.
DR   InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR   InterPro; IPR006011; Syntaxin_N.
DR   InterPro; IPR010989; t-SNARE.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR19957:SF35; Syntaxin-1; 1.
DR   Pfam; PF05739; SNARE; 1.
DR   Pfam; PF00804; Syntaxin; 1.
DR   SMART; SM00503; SynN; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF47661; t-snare; 1.
DR   PROSITE; PS00914; SYNTAXIN; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Coiled coil; Cytoplasmic vesicle;
KW   Direct protein sequencing; Exocytosis; Membrane;
KW   Neurotransmitter transport; Phosphoprotein; Synapse; Synaptosome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    288       Syntaxin-1A.
FT                                /FTId=PRO_0000210187.
FT   TOPO_DOM      1    265       Cytoplasmic (Potential).
FT   TRANSMEM    266    286       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   TOPO_DOM    287    288       Extracellular (Potential).
FT   DOMAIN      192    254       t-SNARE coiled-coil homology.
FT   COILED       68    109       Potential.
FT   MOD_RES      14     14       Phosphoserine.
SQ   SEQUENCE   288 AA;  33054 MW;  8F8255F2EEF886CA CRC64;
     MKDRTQELRT AKDSDDDDDV TVTVDRDRFM DEFFEQVEEI RGFIDKIAEN VEEVKRKHSA
     ILASPNPDEK TKEELEELMS DIKKTANKVR SKLKSIEQSI EQEEGLNRSS ADLRIRKTQH
     STLSRKFVEV MSEYNATQSD YRERCKGRIQ RQLEITGRTT TSEELEDMLE SGNPAIFASG
     IIMDSSISKQ ALSEIETRHS EIIKLETSIR ELHDMFMDMA MLVESQGEMI DRIEYNVEHA
     VDYVERAVSD TKKAVKYQSK ARRKKIMIII CCVILGIIIA STIGGIFG
//
ID   EAA4_MOUSE              Reviewed;         561 AA.
AC   O35544;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Excitatory amino acid transporter 4;
DE   AltName: Full=High-affinity neuronal glutamate transporter;
DE   AltName: Full=Sodium-dependent glutamate/aspartate transporter;
DE   AltName: Full=Solute carrier family 1 member 6;
GN   Name=Slc1a6; Synonyms=Eaat4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Cerebellum;
RX   MEDLINE=98020668; PubMed=9379843; DOI=10.1016/S0169-328X(97)00169-1;
RA   Maeno-Hikichi Y., Tanaka K., Shibata T., Watanabe M., Inoue Y.,
RA   Mukainaka Y., Wada K.;
RT   "Structure and functional expression of the cloned mouse neuronal
RT   high-affinity glutamate transporter.";
RL   Brain Res. Mol. Brain Res. 48:176-180(1997).
CC   -!- FUNCTION: Transports L-glutamate and also L- and D-aspartate.
CC       Seems to act as a symport by cotransporting sodium (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Brain specific.
CC   -!- SIMILARITY: Belongs to the sodium:dicarboxylate (SDF) symporter
CC       (TC 2.A.23) family. SLC1A6 subfamily.
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DR   EMBL; D83262; BAA23640.1; -; mRNA.
DR   IPI; IPI00131666; -.
DR   RefSeq; NP_033226.1; NM_009200.3.
DR   UniGene; Mm.6257; -.
DR   ProteinModelPortal; O35544; -.
DR   SMR; O35544; 55-519.
DR   STRING; O35544; -.
DR   PhosphoSite; O35544; -.
DR   PRIDE; O35544; -.
DR   Ensembl; ENSMUST00000005490; ENSMUSP00000005490; ENSMUSG00000005357.
DR   GeneID; 20513; -.
DR   KEGG; mmu:20513; -.
DR   UCSC; uc007fyg.1; mouse.
DR   CTD; 20513; -.
DR   MGI; MGI:1096331; Slc1a6.
DR   eggNOG; roNOG15270; -.
DR   HOGENOM; HBG739804; -.
DR   HOVERGEN; HBG000080; -.
DR   InParanoid; O35544; -.
DR   OMA; MSSHANS; -.
DR   OrthoDB; EOG4WDDBJ; -.
DR   PhylomeDB; O35544; -.
DR   NextBio; 298715; -.
DR   ArrayExpress; O35544; -.
DR   Bgee; O35544; -.
DR   Genevestigator; O35544; -.
DR   GermOnline; ENSMUSG00000005357; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IMP:MGI.
DR   GO; GO:0017153; F:sodium:dicarboxylate symporter activity; IEA:InterPro.
DR   GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR   InterPro; IPR001991; Na-dicarboxylate_symporter.
DR   InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR   PANTHER; PTHR11958; Na/diCO_symport; 1.
DR   Pfam; PF00375; SDF; 1.
DR   PRINTS; PR00173; EDTRNSPORT.
DR   PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
DR   PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Symport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    561       Excitatory amino acid transporter 4.
FT                                /FTId=PRO_0000202071.
FT   TOPO_DOM      1     52       Cytoplasmic (Potential).
FT   TRANSMEM     53     73       Helical; (Potential).
FT   TRANSMEM     96    116       Helical; (Potential).
FT   TRANSMEM    130    150       Helical; (Potential).
FT   TOPO_DOM    151    261       Extracellular (Potential).
FT   TRANSMEM    262    282       Helical; (Potential).
FT   TRANSMEM    303    323       Helical; (Potential).
FT   TRANSMEM    342    362       Helical; (Potential).
FT   TRANSMEM    367    387       Helical; (Potential).
FT   TRANSMEM    415    435       Helical; (Potential).
FT   TRANSMEM    457    477       Helical; (Potential).
FT   TRANSMEM    478    498       Helical; (Potential).
FT   CARBOHYD    213    213       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    229    229       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    236    236       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   561 AA;  60784 MW;  CCFE3FD499D4CBBB CRC64;
     MSSHGNSLFL RESGAGGGCL QGLQDSLQQR ALRTRLRLQT MTREHVRRFL RRNAFILLTV
     SAVIIGVSLA FALRPYQLSY RQIKYFSFPG ELLMRMLQML VLPLIVSSLV TGMASLDNKA
     TGRMGMRAAV YYMVTTVIAV FIGILMVTII HPGKGSKEGL HREGRIETVP TADAFMDLVR
     NMFPPNLVEA CFKQFKTQYS TRVVTRTIVR TDNGSELGAS MSPTSSVENE TSILENVTRA
     LGTLQEVISF EETVPVPGSA NGINALGLVV FSVAFGLVIG GMKHKGRVLR DFFDSLNEAI
     MRLVGIIIWY APVGILFLIA GKILEMEDMA VLGGQLGMYT LTVIVGLFLH AGGVLPLIYF
     LVTHRNPFPF IGGMLQALIT AMGTSSSSAT LPITFRCLEE GLGVDRRITR FVLPVGATVN
     MDGTALYEAL AAIFIAQVNN YELNLGQITT ISITATAASV GAAGIPQAGL VTMVIVLTSV
     GLPTEDITLI IAVDWFLDRL RTMTNVLGDS IGAAVIEHLS QRELELQEAE LTLPSLGKPY
     KSLMAQEKGA SRGRGGNESV M
//
ID   RABE1_MOUSE             Reviewed;         862 AA.
AC   O35551; A1L322; Q99L08; Q9CRP3; Q9EQF9; Q9JI94;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Rab GTPase-binding effector protein 1;
DE   AltName: Full=Rabaptin-5;
DE   AltName: Full=Rabaptin-5alpha;
GN   Name=Rabep1; Synonyms=Rab5ep, Rabpt5, Rabpt5a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=ICR; TISSUE=Brain, and Muscle;
RX   MEDLINE=98087215; PubMed=9427343;
RA   Nishimune H., Uyeda A., Nogawa M., Fujimori K., Taguchi T.;
RT   "Neurocrescin: a novel neurite-outgrowth factor secreted by muscle
RT   after denervation.";
RL   NeuroReport 8:3649-3654(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=CBA; TISSUE=Embryo;
RX   PubMed=11977240;
RA   Korobko E.V., Smirnova E.V., Kiselev S.L., Georgiev G.P.,
RA   Korobko I.V.;
RT   "Identification of a new alternative-splicing transcript of rabaptin-5
RT   interacting with protein kinase MAK-V.";
RL   Dokl. Biochem. 370:1-3(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-316 (ISOFORMS 1/4/5).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Rab effector protein acting as linker between gamma-
CC       adaptin, RAB4A and RAB5A. Involved in endocytic membrane fusion
CC       and membrane trafficking of recycling endosomes. Stimulates
CC       RABGEF1 mediated nucleotide exchange on RAB5A (By similarity).
CC   -!- SUBUNIT: Heterodimer with RABGEF1. The heterodimer binds RAB4A and
CC       RAB5A that have been activated by GTP-binding. Binds TSC2, GGA1,
CC       GGA2, GGA3, AP1G1 and AP1G2 (By similarity). Interacts with ECM29
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Early endosome
CC       (By similarity). Recycling endosome (By similarity). Cytoplasmic
CC       vesicle (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1; Synonyms=Rabaptin-5;
CC         IsoId=O35551-1; Sequence=Displayed;
CC       Name=2; Synonyms=Rabaptin-5gamma;
CC         IsoId=O35551-2; Sequence=VSP_010452;
CC       Name=3; Synonyms=Rabaptin-5delta;
CC         IsoId=O35551-3; Sequence=VSP_010453;
CC       Name=4;
CC         IsoId=O35551-4; Sequence=VSP_010454, VSP_010455;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=O35551-5; Sequence=VSP_010456, VSP_010457;
CC         Note=May be due to an intron retention. No experimental
CC         confirmation available;
CC       Name=6;
CC         IsoId=O35551-6; Sequence=VSP_025444;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Proteolytic cleavage by caspases in apoptotic cells causes
CC       loss of endosome fusion activity (By similarity).
CC   -!- SIMILARITY: Belongs to the rabaptin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH03921.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; D86066; BAA21783.1; -; mRNA.
DR   EMBL; AB001750; BAA23818.1; -; mRNA.
DR   EMBL; AF248489; AAF78238.1; -; mRNA.
DR   EMBL; AF248490; AAG44544.1; -; mRNA.
DR   EMBL; BC003921; AAH03921.1; ALT_INIT; mRNA.
DR   EMBL; BC060166; AAH60166.1; -; mRNA.
DR   EMBL; BC129853; AAI29854.1; -; mRNA.
DR   EMBL; AK019413; BAB31710.3; -; mRNA.
DR   IPI; IPI00131692; -.
DR   IPI; IPI00310248; -.
DR   IPI; IPI00416396; -.
DR   IPI; IPI00416397; -.
DR   IPI; IPI00467555; -.
DR   IPI; IPI00845537; -.
DR   UniGene; Mm.7087; -.
DR   ProteinModelPortal; O35551; -.
DR   SMR; O35551; 553-640, 806-849.
DR   STRING; O35551; -.
DR   PhosphoSite; O35551; -.
DR   PRIDE; O35551; -.
DR   Ensembl; ENSMUST00000076270; ENSMUSP00000075619; ENSMUSG00000020817.
DR   Ensembl; ENSMUST00000081362; ENSMUSP00000080102; ENSMUSG00000020817.
DR   Ensembl; ENSMUST00000100928; ENSMUSP00000098488; ENSMUSG00000020817.
DR   Ensembl; ENSMUST00000108533; ENSMUSP00000104173; ENSMUSG00000020817.
DR   UCSC; uc007jwr.1; mouse.
DR   UCSC; uc007jwt.1; mouse.
DR   MGI; MGI:1860236; Rabep1.
DR   eggNOG; roNOG08030; -.
DR   GeneTree; ENSGT00530000063743; -.
DR   HOVERGEN; HBG055335; -.
DR   OrthoDB; EOG4XPQFF; -.
DR   NextBio; 311026; -.
DR   ArrayExpress; O35551; -.
DR   Bgee; O35551; -.
DR   CleanEx; MM_RABEP1; -.
DR   Genevestigator; O35551; -.
DR   GermOnline; ENSMUSG00000020817; Mus musculus.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0008083; F:growth factor activity; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR003914; Rabaptin.
DR   InterPro; IPR018514; Rabaptin_coiled-coil.
DR   InterPro; IPR015390; Rabaptin_Rab5-bd.
DR   Pfam; PF09311; Rab5-bind; 1.
DR   Pfam; PF03528; Rabaptin; 2.
DR   PRINTS; PR01432; RABAPTIN.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Apoptosis; Coiled coil; Cytoplasm;
KW   Cytoplasmic vesicle; Endocytosis; Endosome; Phosphoprotein;
KW   Protein transport; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    862       Rab GTPase-binding effector protein 1.
FT                                /FTId=PRO_0000187557.
FT   COILED       11    345       Potential.
FT   COILED      534    816       Potential.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     282    282       N6-acetyllysine (By similarity).
FT   MOD_RES     407    407       Phosphoserine (By similarity).
FT   MOD_RES     408    408       Phosphothreonine (By similarity).
FT   MOD_RES     410    410       Phosphoserine.
FT   VAR_SEQ       1     54       MAQPGPAPQPDVSLQQRVAELEKINAEFLRAQQQLEQEFNQ
FT                                KRAKFKELYLAKE -> MAQPGPAPQPD (in isoform
FT                                2).
FT                                /FTId=VSP_010452.
FT   VAR_SEQ     176    215       Missing (in isoform 3).
FT                                /FTId=VSP_010453.
FT   VAR_SEQ     366    367       EH -> VK (in isoform 4).
FT                                /FTId=VSP_010454.
FT   VAR_SEQ     368    862       Missing (in isoform 4).
FT                                /FTId=VSP_010455.
FT   VAR_SEQ     522    556       Missing (in isoform 5).
FT                                /FTId=VSP_010456.
FT   VAR_SEQ     738    738       I -> IVL (in isoform 6).
FT                                /FTId=VSP_025444.
FT   VAR_SEQ     831    862       QLERIRQADSLERIRAILNDTKLTDINQLPET -> RCLGN
FT                                HHGPSVGGGTNVAGGLGSPLSLPQIFA (in isoform
FT                                5).
FT                                /FTId=VSP_010457.
FT   CONFLICT     68     68       Q -> K (in Ref. 4; BAB31710).
FT   CONFLICT    805    805       R -> Q (in Ref. 3; AAI29854/AAH03921).
SQ   SEQUENCE   862 AA;  99552 MW;  5795524BBA4D7CE5 CRC64;
     MAQPGPAPQP DVSLQQRVAE LEKINAEFLR AQQQLEQEFN QKRAKFKELY LAKEEDLKRQ
     NAVLQAAQDD LGHLRTQLWE AQAEMENIKA IATVSENTKQ EAIDEVKRQW REEVASLQAI
     MKETVRDYEH QFHLRLEQER AQWAQYRESA EREIADLRRR LSEGQEEENL ENEMKKAQED
     AEKLRSVVMP MEKEIAALKD KLTEAEDKIK ELEASKVKEL NHYLEAEKSC RTDLEMYVAV
     LNTQKSVLQE DAEKLRKELH EVCHLLEQER QQHNQLKHTW QKANDQFLES QRLLMRDMQR
     MEIVLTSEQL RQVEELKKKD QEEDEQQRVN KRKDNKKTDT EEEVKIPVVC ALTQEESSTP
     LSNEEEHLDS THGSVHSLDA DLMLPSGDPF SKSDNDMFKD GLRRAQSTDS LGTSSSLQSK
     ALGYNYKAKS AGNLDESDFG PLVGADSVSE NFDTVSLGSL QMPSGFMLTK DQERAIKAMT
     PEQEETASLL SSVTQGMESA YVSPSGYRLV SETEWNLLQK EVHNAGNKLG RRCDMCSNYE
     KQLQGIQIQE AETRDQVKKL QLMLRQANDQ LEKTMKEKQE LEDFLKQSAE DSSHQISALV
     LRAQASEVLL EELQQSFSQA KRDVQEQMAV LMQSREQVSE ELVRLQKDND SLQGKHSLHV
     SLQLAEDFIL PDTVEVLREL VLKYRENIVH VRTAADHMEE KLKAEILFLK EQIQAEQCLK
     ENLEETLQLE IENCKEEIAS ISSLKAELER IKVEKGQLES TLREKSQQLE SLQEMKVNLE
     EQLKKETAAK ATVEQLMFEE KNKARRLQTE LDVSEQVQRD FVKLSQTLQV QLERIRQADS
     LERIRAILND TKLTDINQLP ET
//
ID   FYB_MOUSE               Reviewed;         819 AA.
AC   O35601; Q9Z2H3;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=FYN-binding protein;
DE   AltName: Full=Adhesion and degranulation promoting adaptor protein;
DE            Short=ADAP;
DE   AltName: Full=FYB-120/130;
DE            Short=p120/p130;
DE   AltName: Full=FYN-T-binding protein;
DE   AltName: Full=SLAP-130;
DE   AltName: Full=SLP-76-associated phosphoprotein;
GN   Name=Fyb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FYB-120), INTERACTION WITH FYN AND
RP   LCP2, AND FUNCTION.
RC   TISSUE=T-cell lymphoma;
RX   MEDLINE=97352826; PubMed=9207119; DOI=10.1073/pnas.94.14.7493;
RA   da Silva A.J., Li Z., de Vera C., Canto E., Findell P., Rudd C.E.;
RT   "Cloning of a novel T-cell protein FYB that binds FYN and SH2-domain-
RT   containing leukocyte protein 76 and modulates interleukin 2
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:7493-7498(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM FYB-130), INTERACTION WITH FYN AND
RP   LCP2, AND FUNCTION.
RC   TISSUE=Hybridoma;
RX   MEDLINE=99428514; PubMed=10497204; DOI=10.1074/jbc.274.40.28427;
RA   Veale M., Raab M., Li Z., da Silva A.J., Kraeft S.-K., Weremowicz S.,
RA   Morton C.C., Rudd C.E.;
RT   "Novel isoform of lymphoid adaptor FYN-T-binding protein (FYB-130)
RT   interacts with SLP-76 and up-regulates interleukin 2 production.";
RL   J. Biol. Chem. 274:28427-28435(1999).
RN   [3]
RP   INTERACTION WITH SKAP2, AND IDENTIFICATION IN A COMPLEX WITH SKAP2 AND
RP   PTPNS1.
RX   MEDLINE=99401000; PubMed=10469599; DOI=10.1016/S0960-9822(99)80401-1;
RA   Timms J.F., Swanson K.D., Marie-Cardine A., Raab M., Rudd C.E.,
RA   Schraven B., Neel B.G.;
RT   "SHPS-1 is a scaffold for assembling distinct adhesion-regulated
RT   multi-protein complexes in macrophages.";
RL   Curr. Biol. 9:927-930(1999).
RN   [4]
RP   INTERACTION WITH SKAP2, IDENTIFICATION IN A COMPLEX WITH SKAP2 AND
RP   PTPNS1, AND IDENTIFICATION IN A COMPLEX WITH SKAP2 AND LILRB3.
RX   PubMed=11207596; DOI=10.1046/j.1462-5822.2000.00061.x;
RA   Black D.S., Marie-Cardine A., Schraven B., Bliska J.B.;
RT   "The Yersinia tyrosine phosphatase YopH targets a novel adhesion-
RT   regulated signalling complex in macrophages.";
RL   Cell. Microbiol. 2:401-414(2000).
RN   [5]
RP   INTERACTION WITH SKAP2, FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17003372; DOI=10.1182/blood-2006-05-022301;
RA   Kasirer-Friede A., Moran B., Nagrampa-Orje J., Swanson K.,
RA   Ruggeri Z.M., Schraven B., Neel B.G., Koretzky G., Shattil S.J.;
RT   "ADAP is required for normal alphaIIb-beta3 activation by VWF/GP Ib-
RT   IX-V and other agonists.";
RL   Blood 109:1018-1025(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-559 AND SER-561, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-559 AND SER-561, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Acts as an adapter protein of the FYN and LCP2 signaling
CC       cascades in T cells. Modulates the expression of interleukin-2
CC       (IL-2). Involved in platelet activation. Prevents the degradation
CC       of SKAP1 and SKAP2.
CC   -!- SUBUNIT: Interacts with FYN, LCP2, SKAP1 and SKAP2. Part of a
CC       complex consisting of SKAP2, FYB and PTPNS1. Part of a complex
CC       consisting of SKAP2, FYB and LILRB3. Interacts with FASLG (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=FYB-130;
CC         IsoId=O35601-1; Sequence=Displayed;
CC       Name=FYB-120;
CC         IsoId=O35601-2; Sequence=VSP_004261;
CC   -!- TISSUE SPECIFICITY: Expressed in hematopoietic tissues such as
CC       myeloid and T-cells, spleen and thymus. Not expressed in B-cells,
CC       nor in non-lymphoid tissues. FYB-130 is preferentially expressed
CC       in mature T-cells compared to FYB-120, whereas thymocytes showed a
CC       greater relative amount of FYB-120.
CC   -!- PTM: T-cell receptor ligation leads to increased tyrosine
CC       phosphorylation.
CC   -!- DISRUPTION PHENOTYPE: Slight defects in platelet function.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF001863; AAB62227.1; -; mRNA.
DR   EMBL; AF061744; AAD03267.1; -; mRNA.
DR   IPI; IPI00226593; -.
DR   IPI; IPI00626627; -.
DR   RefSeq; NP_035945.1; NM_011815.4.
DR   UniGene; Mm.170905; -.
DR   ProteinModelPortal; O35601; -.
DR   SMR; O35601; 494-567, 725-801.
DR   MINT; MINT-244320; -.
DR   STRING; O35601; -.
DR   PhosphoSite; O35601; -.
DR   PRIDE; O35601; -.
DR   Ensembl; ENSMUST00000090461; ENSMUSP00000087947; ENSMUSG00000022148.
DR   Ensembl; ENSMUST00000110659; ENSMUSP00000106287; ENSMUSG00000022148.
DR   GeneID; 23880; -.
DR   KEGG; mmu:23880; -.
DR   UCSC; uc007vdj.1; mouse.
DR   UCSC; uc007vdk.1; mouse.
DR   CTD; 23880; -.
DR   MGI; MGI:1346327; Fyb.
DR   eggNOG; roNOG15289; -.
DR   HOGENOM; HBG506770; -.
DR   HOVERGEN; HBG005774; -.
DR   InParanoid; O35601; -.
DR   OMA; ACCDVKG; -.
DR   OrthoDB; EOG4VMFF3; -.
DR   NextBio; 303607; -.
DR   PMAP-CutDB; O35601; -.
DR   ArrayExpress; O35601; -.
DR   Bgee; O35601; -.
DR   CleanEx; MM_FYB; -.
DR   Genevestigator; O35601; -.
DR   GermOnline; ENSMUSG00000022148; Mus musculus.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 2.
DR   PROSITE; PS50002; SH3; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Nucleus;
KW   Phosphoprotein; SH3 domain.
FT   CHAIN         1    819       FYN-binding protein.
FT                                /FTId=PRO_0000087397.
FT   DOMAIN      699    756       SH3.
FT   COILED      448    495       Potential.
FT   MOTIF       479    493       Nuclear localization signal (Potential).
FT   MOTIF       584    587       SH2-binding; to LCP2.
FT   MOTIF       615    618       SH2-binding; to FYN.
FT   MOTIF       710    736       Nuclear localization signal (Potential).
FT   COMPBIAS    343    348       Poly-Pro.
FT   COMPBIAS    381    385       Poly-Pro.
FT   COMPBIAS    606    609       Poly-Pro.
FT   COMPBIAS    622    625       Poly-Asp.
FT   COMPBIAS    696    699       Poly-Pro.
FT   MOD_RES       3      3       N6-acetyllysine (By similarity).
FT   MOD_RES      28     28       Phosphoserine.
FT   MOD_RES      46     46       Phosphoserine (By similarity).
FT   MOD_RES     114    114       Phosphoserine.
FT   MOD_RES     147    147       N6-acetyllysine (By similarity).
FT   MOD_RES     260    260       N6-acetyllysine (By similarity).
FT   MOD_RES     413    413       N6-acetyllysine (By similarity).
FT   MOD_RES     445    445       Phosphoserine (By similarity).
FT   MOD_RES     559    559       Phosphotyrosine.
FT   MOD_RES     561    561       Phosphoserine.
FT   MOD_RES     687    687       Phosphotyrosine (By similarity).
FT   MOD_RES     747    747       Phosphothreonine (By similarity).
FT   VAR_SEQ     627    672       Missing (in isoform FYB-120).
FT                                /FTId=VSP_004261.
SQ   SEQUENCE   819 AA;  90055 MW;  6222CC7EF1CA2BBD CRC64;
     MAKFNTGSNP TEEAATSSRP FKVAGQSSPS GIQSRKNLFD NQGNASPPAG PSSMPKFGTT
     KPPLAAKPTY EEKPEKEPKP PFLKPTGGSP RFGTQPNSVS RDPEVKVGFL KPVSPKPTSL
     TKEDSKPVVL RPPGNKLHNL NQESDLKTPG PKPGPAPPVP ENELKPGFSK VAGAKSKFMP
     AAQDTDSKPR FPRHTFGQKP SLSTEDSQEE NTSKNVPVQK GSPVQLGAKS KGAPFKPPKE
     DPEDKDHGAP SSPFPGVVLK PAASRGSPGL SKNFEEKKED RKTDLAKNIF LNKLNQEEPA
     RFPKAPSKLT AGTPWGQSQE KEGDKNSATP KQKALPPLSV LGPPPPKPNR PPNVDLTRFR
     KADSANSATK SQTPYSTTSL PPPPPTHPAS QPPLPASHPA HPPVPSLPPR NIKPPLDLKH
     PINDENQDGV MHSDGTGNLE EEQESEGETY EDIDSSKERD KKREKEEKKR LELERKEQKE
     REKKEQELKK KFKLTGPIQV IHHAKACCDV KGGKNELSFK QGEDIEIIRI TDNPEGKWLG
     RTARGSYGYI KTTAVEIDYD SLKRKKNSLN AVPPRLVEDD QDVYDDVAEQ DAPNSHGQSG
     SGGMFPPPPT DDEIYDGIEE EDDDDGSVPQ VDEKTNAWSW GILKMLKGKD DRKKSIREKP
     KVSESDNNEG SSLPSQHKQL DVGEEVYDDV DASDFPPPPA EMSQGMSVGR AKTEEKDPKK
     LKKQEKEEKD LRKKFKYDGE IRVLYSTKVA SSLTSKKWGA RDLQIKPGES LEVIQSTDDT
     KVLCRNEEGK YGYVLRSYLV DNDGEIYDDI ADGCIYDND
//
ID   BMPR2_MOUSE             Reviewed;        1038 AA.
AC   O35607;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 104.
DE   RecName: Full=Bone morphogenetic protein receptor type-2;
DE            Short=BMP type-2 receptor;
DE            Short=BMPR-2;
DE            EC=2.7.11.30;
DE   AltName: Full=BRK-3;
DE   AltName: Full=Bone morphogenetic protein receptor type II;
DE            Short=BMP type II receptor;
DE            Short=BMPR-II;
DE   Flags: Precursor;
GN   Name=Bmpr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=97350808; PubMed=9207184; DOI=10.1006/bbrc.1997.6816;
RA   Beppu H., Minowa O., Miyazono K., Kawabata M.;
RT   "cDNA cloning and genomic organization of the mouse BMP type II
RT   receptor.";
RL   Biochem. Biophys. Res. Commun. 235:499-504(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Whitaker G.B., Koenig B.B., Ting J., Tiesman J.P., Limberg A.L.,
RA   Grant R.A., Begley K.B., Rosenbaum J.S.;
RT   "Identification of BMP receptor complexes with differential signaling
RT   properties and ligand binding profiles.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: On ligand binding, forms a receptor complex consisting
CC       of two type II and two type I transmembrane serine/threonine
CC       kinases. Type II receptors phosphorylate and activate type I
CC       receptors which autophosphorylate, then bind and activate SMAD
CC       transcriptional regulators. Binds to BMP-7, BMP-2 and, less
CC       efficiently, BMP-4. Binding is weak but enhanced by the presence
CC       of type I receptors for BMPs.
CC   -!- CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-
CC       protein] phosphate.
CC   -!- COFACTOR: Magnesium or manganese (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF003942; AAB63042.1; -; mRNA.
DR   EMBL; U78048; AAB87638.1; -; mRNA.
DR   IPI; IPI00338094; -.
DR   PIR; JC5527; JC5527.
DR   RefSeq; NP_031587.1; NM_007561.3.
DR   UniGene; Mm.391654; -.
DR   UniGene; Mm.7106; -.
DR   ProteinModelPortal; O35607; -.
DR   SMR; O35607; 33-131, 197-510.
DR   IntAct; O35607; 3.
DR   STRING; O35607; -.
DR   PhosphoSite; O35607; -.
DR   PRIDE; O35607; -.
DR   Ensembl; ENSMUST00000087435; ENSMUSP00000084701; ENSMUSG00000067336.
DR   GeneID; 12168; -.
DR   KEGG; mmu:12168; -.
DR   UCSC; uc007bdz.1; mouse.
DR   CTD; 12168; -.
DR   MGI; MGI:1095407; Bmpr2.
DR   eggNOG; roNOG13032; -.
DR   HOGENOM; HBG447050; -.
DR   HOVERGEN; HBG050705; -.
DR   InParanoid; O35607; -.
DR   OMA; GPTPVCL; -.
DR   OrthoDB; EOG470TGJ; -.
DR   PhylomeDB; O35607; -.
DR   BRENDA; 2.7.10.2; 244.
DR   BRENDA; 2.7.11.30; 244.
DR   NextBio; 280539; -.
DR   ArrayExpress; O35607; -.
DR   Bgee; O35607; -.
DR   Genevestigator; O35607; -.
DR   GermOnline; ENSMUSG00000067336; Mus musculus.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005024; F:transforming growth factor beta receptor activity; IEA:InterPro.
DR   GO; GO:0009952; P:anterior/posterior pattern formation; IMP:MGI.
DR   GO; GO:0030509; P:BMP signaling pathway; IMP:MGI.
DR   GO; GO:0048286; P:lung alveolus development; IMP:BHF-UCL.
DR   GO; GO:0001707; P:mesoderm formation; IMP:MGI.
DR   GO; GO:0045906; P:negative regulation of vasoconstriction; IMP:BHF-UCL.
DR   GO; GO:0014916; P:regulation of lung blood pressure; IMP:BHF-UCL.
DR   GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IMP:BHF-UCL.
DR   InterPro; IPR000472; Activin_rcpt.
DR   InterPro; IPR015770; BMPRII.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   PANTHER; PTHR23255:SF12; BMPRII; 1.
DR   Pfam; PF01064; Activin_recp; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   ATP-binding; Disulfide bond; Glycoprotein; Kinase; Magnesium;
KW   Manganese; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Receptor; Serine/threonine-protein kinase; Signal;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     26       Potential.
FT   CHAIN        27   1038       Bone morphogenetic protein receptor type-
FT                                2.
FT                                /FTId=PRO_0000024416.
FT   TOPO_DOM     27    150       Extracellular (Potential).
FT   TRANSMEM    151    171       Helical; (Potential).
FT   TOPO_DOM    172   1038       Cytoplasmic (Potential).
FT   DOMAIN      203    504       Protein kinase.
FT   NP_BIND     209    217       ATP (By similarity).
FT   NP_BIND     280    282       ATP (By similarity).
FT   NP_BIND     337    338       ATP (By similarity).
FT   COMPBIAS    191    194       Poly-Ala.
FT   COMPBIAS    547    550       Poly-Ser.
FT   COMPBIAS    610    618       Poly-Thr.
FT   COMPBIAS    901    908       Poly-Asn.
FT   ACT_SITE    333    333       Proton acceptor (By similarity).
FT   BINDING     230    230       ATP (By similarity).
FT   BINDING     351    351       ATP (By similarity).
FT   MOD_RES     375    375       Phosphoserine (By similarity).
FT   MOD_RES     379    379       Phosphothreonine (By similarity).
FT   MOD_RES     513    513       Phosphoserine (By similarity).
FT   MOD_RES     515    515       Phosphoserine (By similarity).
FT   MOD_RES     586    586       Phosphoserine (By similarity).
FT   MOD_RES     680    680       Phosphoserine (By similarity).
FT   MOD_RES     681    681       Phosphoserine (By similarity).
FT   MOD_RES     757    757       Phosphoserine (By similarity).
FT   MOD_RES     862    862       Phosphoserine (By similarity).
FT   MOD_RES     863    863       Phosphoserine (By similarity).
FT   CARBOHYD     55     55       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    110    110       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    126    126       N-linked (GlcNAc...) (Potential).
FT   DISULFID     34     66       By similarity.
FT   DISULFID     94    117       By similarity.
SQ   SEQUENCE   1038 AA;  115020 MW;  4106945DC63250E1 CRC64;
     MTSSLHRPFR VPWLLWAVLL VSTTAASQNQ ERLCAFKDPY QQDLGIGESR ISHENGTILC
     SKGSTCYGLW EKSKGDINLV KQGCWSHIGD PQECHYEECV VTTTPPSIQN GTYRFCCCST
     DLCNVNFTEN FPPPDTTPLS PPHSFNRDET IIIALASVSV LAVLIVALCF GYRMLTGDRK
     QGLHSMNMME AAAAEPSLDL DNLKLLELIG RGRYGAVYKG SLDERPVAVK VFSFANRQNF
     INEKNIYRVP LMEHDNIARF IVGDERLTAD GRMEYLLVME YYPNGSLCKY LSLHTSDWVS
     SCRLAHSVTR GLAYLHTELP RGDHYKPAIS HRDLNSRNVL VKNDGACVIS DFGLSMRLTG
     NRLVRPGEED NAAISEVGTI RYMAPEVLEG AVNLRDCESA LKQVDMYALG LIYWEVFMRC
     TDLFPGESVP DYQMAFQTEV GNHPTFEDMQ VLVSREKQRP KFPEAWKENS LAVRSLKETI
     EDCWDQDAEA RLTAQCAEER MAELMMIWER NKSVSPTVNP MSTAMQNERN LSHNRRVPKI
     GPYPDYSSSS YIEDSIHHTD SIVKNISSEH SMSSTPLTIG EKNRNSINYE RQQAQARIPS
     PETSVTSLST NTTTTNTTGL TPSTGMTTIS EMPYPDETHL HATNVAQSIG PTPVCLQLTE
     EDLETNKLDP KEVDKNLKES SDENLMEHSL KQFSGPDPLS STSSSLLYPL IKLAVEVTGQ
     QDFTQAANGQ ACLIPDVPPA QIYPLPKQQN LPKRPTSLPL NTKNSTKEPR LKFGNKHKSN
     LKQVETGVAK MNTINAAEPH VVTVTMNGVA GRSHNVNSHA ATTQYANGAV PAGQAANIVA
     HRSQEMLQNQ FIGEDTRLNI NSSPDEHEPL LRREQQAGHD EGVLDRLVDR RERPLEGGRT
     NSNNNNSNPC SEQDILTQGV TSTAADPGPS KPRRAQRPNS LDLSATNILD GSSIQIGEST
     QDGKSGSGEK IKRRVKTPYS LKRWRPSTWV ISTEPLDCEV NNNGSDRAVH SKSSTAVYLA
     EGGTATTTVS KDIGMNCL
//
ID   SCAM3_MOUSE             Reviewed;         349 AA.
AC   O35609; Q99M48; Q9ERM9;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Secretory carrier-associated membrane protein 3;
DE            Short=Secretory carrier membrane protein 3;
GN   Name=Scamp3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98017831; PubMed=9378760;
RA   Singleton D.R., Wu T.T., Castle J.D.;
RT   "Three mammalian SCAMPs (secretory carrier membrane proteins) are
RT   highly related products of distinct genes having similar subcellular
RT   distributions.";
RL   J. Cell Sci. 110:2099-2107(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20504667; PubMed=11050114;
RA   Fernandez-Chacon R., Suedhof T.C.;
RT   "Novel SCAMPs lacking NPF repeats: ubiquitous and synaptic vesicle-
RT   specific forms implicate SCAMPs in multiple membrane-trafficking
RT   functions.";
RL   J. Neurosci. 20:7941-7950(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Functions in post-Golgi recycling pathways. Acts as a
CC       recycling carrier to the cell surface.
CC   -!- SUBUNIT: Interacts with NEDD4 and NEDD4L and TSG101 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- PTM: Monoubiquitinated (By similarity).
CC   -!- SIMILARITY: Belongs to the SCAMP family.
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DR   EMBL; AF005036; AAB62721.1; -; mRNA.
DR   EMBL; AF295403; AAG22800.1; -; mRNA.
DR   EMBL; BC002021; AAH02021.1; -; mRNA.
DR   IPI; IPI00132604; -.
DR   UniGene; Mm.257052; -.
DR   STRING; O35609; -.
DR   PhosphoSite; O35609; -.
DR   PRIDE; O35609; -.
DR   Ensembl; ENSMUST00000029684; ENSMUSP00000029684; ENSMUSG00000028049.
DR   MGI; MGI:1346346; Scamp3.
DR   eggNOG; roNOG15416; -.
DR   HOVERGEN; HBG071938; -.
DR   OrthoDB; EOG44BB32; -.
DR   ArrayExpress; O35609; -.
DR   Bgee; O35609; -.
DR   CleanEx; MM_SCAMP3; -.
DR   Genevestigator; O35609; -.
DR   GermOnline; ENSMUSG00000028049; Mus musculus.
DR   GO; GO:0000139; C:Golgi membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR   GO; GO:0032526; P:response to retinoic acid; IDA:MGI.
DR   InterPro; IPR007273; SCAMP.
DR   PANTHER; PTHR10687; SCAMP; 1.
DR   Pfam; PF04144; SCAMP; 1.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Protein transport; Transmembrane;
KW   Transmembrane helix; Transport; Ubl conjugation.
FT   CHAIN         1    349       Secretory carrier-associated membrane
FT                                protein 3.
FT                                /FTId=PRO_0000191258.
FT   TOPO_DOM      1    168       Cytoplasmic (Potential).
FT   TRANSMEM    169    189       Helical; (Potential).
FT   TRANSMEM    200    220       Helical; (Potential).
FT   TRANSMEM    236    256       Helical; (Potential).
FT   TRANSMEM    277    297       Helical; (Potential).
FT   TOPO_DOM    298    349       Cytoplasmic (Potential).
FT   MOD_RES      32     32       Phosphoserine (By similarity).
FT   MOD_RES      35     35       Phosphotyrosine (By similarity).
FT   MOD_RES      53     53       Phosphotyrosine (By similarity).
FT   MOD_RES      78     78       Phosphoserine.
FT   MOD_RES      85     85       Phosphotyrosine (By similarity).
FT   MOD_RES      87     87       Phosphoserine (By similarity).
FT   CONFLICT     11     11       S -> F (in Ref. 3; AAH02021).
FT   CONFLICT     48     48       E -> EQ (in Ref. 3; AAH02021).
FT   CONFLICT     61     61       A -> S (in Ref. 3; AAH02021).
FT   CONFLICT    111    111       K -> T (in Ref. 1; AAB62721).
FT   CONFLICT    284    284       V -> D (in Ref. 1; AAB62721).
SQ   SEQUENCE   349 AA;  38398 MW;  B4953D4AC707988E CRC64;
     MAQSRDTGNP SPDSGELDNP FQDPAVIQHR PSQQYATLDV YNPFENREPP PAYEPPAPAP
     APLPPPSAPS VQSSRKLSPT EPRNYGSYST QASAAAATAE LLKKQEELNR KAEELDRRER
     ELQHVALGGA GTRQNNWPPL PSFCPVKPCF FQDISMEIPQ EFQKTVSTMY YLWMCSTLAL
     LLNFFACLAR FCVDTGSGSG FGLSMLWLLL FTPCSFVCWY RPMYKAFRSD SSFNFFVFFF
     IFFVQDVFFV LQAIGIPGWG FSGWVTALVV VGSKPAVAVL MLLVALLFTG IAVLGIVMLK
     RIHSLYRQTG ASFQKAQQEF AAGVFSNPAV RTAAANAAAG AAENAFRAP
//
ID   PMM1_MOUSE              Reviewed;         262 AA.
AC   O35621;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Phosphomannomutase 1;
DE            Short=PMM 1;
DE            EC=5.4.2.8;
GN   Name=Pmm1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Janoueix-Lerosey I., Goud B.;
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=16847318; DOI=10.1128/MCB.02357-05;
RA   Cromphout K., Vleugels W., Heykants L., Schollen E., Keldermans L.,
RA   Sciot R., D'Hooge R., De Deyn P.P., von Figura K., Hartmann D.,
RA   Korner C., Matthijs G.;
RT   "The normal phenotype of Pmm1-deficient mice suggests that Pmm1 is not
RT   essential for normal mouse development.";
RL   Mol. Cell. Biol. 26:5621-5635(2006).
RN   [3]
RP   FUNCTION, ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=18927083; DOI=10.1074/jbc.M805224200;
RA   Veiga-da-Cunha M., Vleugels W., Maliekal P., Matthijs G.,
RA   Van Schaftingen E.;
RT   "Mammalian phosphomannomutase PMM1 is the brain IMP-sensitive glucose-
RT   1,6-bisphosphatase.";
RL   J. Biol. Chem. 283:33988-33993(2008).
CC   -!- FUNCTION: Involved in the synthesis of the GDP-mannose and
CC       dolichol-phosphate-mannose required for a number of critical
CC       mannosyl transfer reactions. In addition, may be responsible for
CC       the degradation of glucose-1,6-bisphosphate in ischemic brain.
CC   -!- CATALYTIC ACTIVITY: Alpha-D-mannose 1-phosphate = D-mannose 6-
CC       phosphate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: IMP, a metabolite whose concentration is
CC       elevated in anoxia, inhibits phosphomannomutase and
CC       phosphoglucomutase activities and strongly enhances glucose-1,6-
CC       bisphosphatase activity.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=17 uM for glucose-1,6-bisphosphate in the presence of 1 uM
CC         IMP;
CC         KM=40 uM for glucose-1,6-bisphosphate in the presence of 20 uM
CC         IMP;
CC         Vmax=2.1 umol/min/mg enzyme with glucose-1,6-bisphosphate as
CC         substrate;
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose
CC       biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-
CC       phosphate: step 2/2.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Present in brain, where it is restricted to
CC       neuronal cell bodies. Present at lower levels in pancreas, liver,
CC       lung, gonads, uterus, adrenal glands and pituitary (at protein
CC       level). Undetectable in intestine.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed at E17 in most organs (at
CC       protein level).
CC   -!- DISRUPTION PHENOTYPE: Mice are viable and fertile and develop
CC       normally.
CC   -!- SIMILARITY: Belongs to the eukaryotic PMM family.
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DR   EMBL; AF007267; AAB62943.1; -; mRNA.
DR   IPI; IPI00132682; -.
DR   RefSeq; NP_038900.1; NM_013872.3.
DR   UniGene; Mm.18939; -.
DR   ProteinModelPortal; O35621; -.
DR   SMR; O35621; 13-258.
DR   STRING; O35621; -.
DR   PRIDE; O35621; -.
DR   Ensembl; ENSMUST00000023112; ENSMUSP00000023112; ENSMUSG00000022474.
DR   GeneID; 29858; -.
DR   KEGG; mmu:29858; -.
DR   UCSC; uc007wxt.1; mouse.
DR   CTD; 29858; -.
DR   MGI; MGI:1353418; Pmm1.
DR   eggNOG; roNOG12994; -.
DR   HOGENOM; HBG329388; -.
DR   HOVERGEN; HBG009971; -.
DR   InParanoid; O35621; -.
DR   OMA; NDYEIYD; -.
DR   OrthoDB; EOG4894NB; -.
DR   PhylomeDB; O35621; -.
DR   BRENDA; 5.4.2.8; 244.
DR   NextBio; 307058; -.
DR   ArrayExpress; O35621; -.
DR   Bgee; O35621; -.
DR   CleanEx; MM_PMM1; -.
DR   Genevestigator; O35621; -.
DR   GermOnline; ENSMUSG00000022474; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004615; F:phosphomannomutase activity; IEA:EC.
DR   GO; GO:0019307; P:mannose biosynthetic process; IEA:InterPro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR005002; PMM.
DR   Gene3D; G3DSA:3.40.50.1000; HAD-like_dom; 2.
DR   PANTHER; PTHR10466; PMM; 1.
DR   Pfam; PF03332; PMM; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Isomerase; Magnesium; Metal-binding.
FT   CHAIN         1    262       Phosphomannomutase 1.
FT                                /FTId=PRO_0000199693.
FT   ACT_SITE     19     19       Nucleophile (By similarity).
FT   ACT_SITE     21     21       By similarity.
FT   ACT_SITE     54     54       By similarity.
FT   ACT_SITE    198    198       By similarity.
FT   METAL       218    218       Magnesium (By similarity).
FT   BINDING      28     28       Substrate (By similarity).
FT   BINDING     132    132       Substrate (By similarity).
FT   BINDING     143    143       Substrate (By similarity).
FT   BINDING     150    150       Substrate (By similarity).
FT   BINDING     186    186       Substrate (By similarity).
FT   BINDING     188    188       Substrate (By similarity).
FT   BINDING     190    190       Substrate (By similarity).
SQ   SEQUENCE   262 AA;  29775 MW;  2967154C0FF292B0 CRC64;
     MAVAVEGARR KERILCLFDV DGTLTPARQK IDPEVSAFLQ KLRSRVQIGV VGGSDYSKIA
     EQLGEGDEVI EKFDYVFAEN GTVQYKHGRL LSKQTIQNHL GEELLQDLIN FCLSYMALLR
     LPKKRGTFIE FRNGMLNVSP IGRSCTLEER IEFSELDKKE KIREKFVEAL KTEFAGKGLR
     FSRGGMISFD VFPEGWDKRY CLDSLDEDSF DIIHFFGNET SPGGNDFEIY ADPRTVGHSV
     VSPQDTVQRC RELFFPETAH EA
//
ID   BET1_MOUSE              Reviewed;         118 AA.
AC   O35623;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=BET1 homolog;
DE            Short=mBET1;
DE   AltName: Full=Golgi vesicular membrane-trafficking protein p18;
GN   Name=Bet1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98044220; PubMed=9382863; DOI=10.1083/jcb.139.5.1157;
RA   Zhang T., Wong S.H., Tang B.L., Xu Y., Peter F., Subramaniam V.N.,
RA   Hong W.;
RT   "The mammalian protein (rbet1) homologous to yeast Bet1p is primarily
RT   associated with the pre-Golgi intermediate compartment and is involved
RT   in vesicular transport from the endoplasmic reticulum to the Golgi
RT   apparatus.";
RL   J. Cell Biol. 139:1157-1168(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Required for vesicular transport from the ER to the
CC       Golgi complex. Functions as a SNARE involved in the docking
CC       process of ER-derived vesicles with the cis-Golgi membrane (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type
CC       IV membrane protein (By similarity). Endoplasmic reticulum
CC       membrane; Single-pass type IV membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the BET1 family.
CC   -!- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain.
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DR   EMBL; AF007552; AAB62942.1; -; mRNA.
DR   EMBL; BC005572; AAH05572.1; -; mRNA.
DR   IPI; IPI00132685; -.
DR   RefSeq; NP_033878.1; NM_009748.2.
DR   UniGene; Mm.286457; -.
DR   ProteinModelPortal; O35623; -.
DR   SMR; O35623; 33-85.
DR   STRING; O35623; -.
DR   PhosphoSite; O35623; -.
DR   PRIDE; O35623; -.
DR   Ensembl; ENSMUST00000049166; ENSMUSP00000044877; ENSMUSG00000032757.
DR   GeneID; 12068; -.
DR   KEGG; mmu:12068; -.
DR   UCSC; uc009avk.1; mouse.
DR   CTD; 12068; -.
DR   MGI; MGI:1343104; Bet1.
DR   eggNOG; roNOG17504; -.
DR   HOGENOM; HBG714857; -.
DR   HOVERGEN; HBG029661; -.
DR   InParanoid; O35623; -.
DR   OMA; QTKLLCY; -.
DR   OrthoDB; EOG4NP753; -.
DR   PhylomeDB; O35623; -.
DR   NextBio; 280391; -.
DR   ArrayExpress; O35623; -.
DR   Bgee; O35623; -.
DR   Genevestigator; O35623; -.
DR   GermOnline; ENSMUSG00000032757; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   Pfam; PF05739; SNARE; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Endoplasmic reticulum; ER-Golgi transport;
KW   Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    118       BET1 homolog.
FT                                /FTId=PRO_0000206885.
FT   TOPO_DOM      1     94       Cytoplasmic (Potential).
FT   TRANSMEM     95    115       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   TOPO_DOM    116    118       Vesicular (Potential).
FT   DOMAIN       26     88       t-SNARE coiled-coil homology.
FT   MOD_RES      50     50       Phosphoserine (By similarity).
SQ   SEQUENCE   118 AA;  13274 MW;  CB81C325119BA152 CRC64;
     MRRAGLGDGA PPGSYGNYGY ANTGYNACEE ENDRLTESLR SKVTAIKSLS IEIGHEVKNQ
     NKLLAEMDSQ FDSTTGFLGK TMGRLKILSR GSQTKLLCYM MLFSLFVFFV IYWIIKLR
//
ID   AXN1_MOUSE              Reviewed;         863 AA.
AC   O35625;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2002, sequence version 2.
DT   08-MAR-2011, entry version 107.
DE   RecName: Full=Axin-1;
DE   AltName: Full=Axis inhibition protein 1;
DE   AltName: Full=Protein Fused;
GN   Name=Axin1; Synonyms=Axin, Fu;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX   MEDLINE=97373830; PubMed=9230313; DOI=10.1016/S0092-8674(00)80324-4;
RA   Zeng L., Fagotto F., Zhang T., Hsu W., Vasicek T.J., Perry W.L. III,
RA   Lee J.J., Tilghman S.M., Gumbiner B.M., Costantini F.;
RT   "The mouse Fused locus encodes Axin, an inhibitor of the Wnt signaling
RT   pathway that regulates embryonic axis formation.";
RL   Cell 90:181-192(1997).
RN   [2]
RP   PHOSPHORYLATION AT THR-480; SER-485 AND SER-492, INTERACTION WITH
RP   CTNNB1, AND MUTAGENESIS OF THR-480; SER-485; SER-492 AND SER-495.
RX   PubMed=10581160; DOI=10.1006/bbrc.1999.1760;
RA   Jho E., Lomvardas S., Costantini F.;
RT   "A GSK3beta phosphorylation site in axin modulates interaction with
RT   beta-catenin and Tcf-mediated gene expression.";
RL   Biochem. Biophys. Res. Commun. 266:28-35(1999).
RN   [3]
RP   INTERACTION WITH LRP5.
RX   PubMed=11336703; DOI=10.1016/S1097-2765(01)00224-6;
RA   Mao J., Wang J., Liu B., Pan W., Farr G.H. III, Flynn C., Yuan H.,
RA   Takada S., Kimelman D., Li L., Wu D.;
RT   "Low-density lipoprotein receptor-related protein-5 binds to Axin and
RT   regulates the canonical Wnt signaling pathway.";
RL   Mol. Cell 7:801-809(2001).
RN   [4]
RP   INTERACTION WITH ANKRD6.
RX   MEDLINE=22170692; PubMed=12183362; DOI=10.1101/gad.230402;
RA   Schwarz-Romond T., Asbrand C., Bakkers J., Kuehl M., Schaeffer H.J.,
RA   Huelsken J., Behrens J., Hammerschmidt M., Birchmeier W.;
RT   "The ankyrin repeat protein diversin recruits casein kinase Iepsilon
RT   to the beta-catenin degradation complex and acts in both canonical Wnt
RT   and Wnt/JNK signaling.";
RL   Genes Dev. 16:2073-2084(2002).
RN   [5]
RP   SUMOYLATION AT LYS-858 AND LYS-861, INTERACTION WITH MAP3K1; SUMO1;
RP   PIAS1; PIAS2 AND PIAS4, FUNCTION, HOMODIMERIZATION, AND MUTAGENESIS OF
RP   858-LYS--ASP-863.
RX   PubMed=12223491; DOI=10.1074/jbc.M208099200;
RA   Rui H.L., Fan E., Zhou H.M., Xu Z., Zhang Y., Lin S.C.;
RT   "SUMO-1 modification of the C-terminal KVEKVD of Axin is required for
RT   JNK activation but has no effect on Wnt signaling.";
RL   J. Biol. Chem. 277:42981-42986(2002).
RN   [6]
RP   PHOSPHORYLATION, AND INTERACTION WITH CTNNB1.
RX   PubMed=15063782; DOI=10.1016/j.bbrc.2004.03.065;
RA   Kim S.I., Park C.S., Lee M.S., Kwon M.S., Jho E.H., Song W.K.;
RT   "Cyclin-dependent kinase 2 regulates the interaction of Axin with
RT   beta-catenin.";
RL   Biochem. Biophys. Res. Commun. 317:478-483(2004).
RN   [7]
RP   FUNCTION, INTERACTION WITH TP53 AND HIPK2, AND IDENTIFICATION IN A
RP   COMPLEX WITH TP53 AND HIPK2.
RX   PubMed=15526030; DOI=10.1038/sj.emboj.7600475;
RA   Rui Y., Xu Z., Lin S., Li Q., Rui H., Luo W., Zhou H.-M.,
RA   Cheung P.-Y., Wu Z., Ye Z., Li P., Han J., Lin S.-C.;
RT   "Axin stimulates p53 functions by activation of HIPK2 kinase through
RT   multimeric complex formation.";
RL   EMBO J. 23:4583-4594(2004).
RN   [8]
RP   INTERACTION WITH DIXDC1; MAP3K1 AND MAP3K4.
RX   PubMed=15262978; DOI=10.1074/jbc.M404598200;
RA   Wong C.K., Luo W., Deng Y., Zou H., Ye Z., Lin S.-C.;
RT   "The DIX domain protein coiled-coil-DIX1 inhibits c-Jun N-terminal
RT   kinase activation by Axin and dishevelled through distinct
RT   mechanisms.";
RL   J. Biol. Chem. 279:39366-39373(2004).
RN   [9]
RP   FUNCTION, HOMODIMERIZATION, AND INTERACTION WITH AIDA.
RX   PubMed=17681137; DOI=10.1016/j.devcel.2007.07.006;
RA   Rui Y., Xu Z., Xiong B., Cao Y., Lin S., Zhang M., Chan S.-C., Luo W.,
RA   Han Y., Lu Z., Ye Z., Zhou H.-M., Han J., Meng A., Lin S.-C.;
RT   "A beta-catenin-independent dorsalization pathway activated by
RT   Axin/JNK signaling and antagonized by aida.";
RL   Dev. Cell 13:268-282(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Component of the beta-catenin destruction complex
CC       required for regulating CTNNB1 levels through phosphorylation and
CC       ubiquitination, and modulating Wnt-signaling (By similarity).
CC       Controls dorsoventral patterning via two opposing effects; down-
CC       regulates CTNNB1 to inhibit the Wnt signaling pathway and
CC       ventralize embryos, but also dorsalizes embryos by activating a
CC       Wnt-independent JNK signaling pathway. In Wnt signaling, probably
CC       facilitates the phosphorylation of CTNNB1 and APC by GSK3B. Likely
CC       to function as a tumor suppressor. Facilitates the phosphorylation
CC       of TP53 by HIPK2 upon ultraviolet irradiation. Enhances TGF-beta
CC       signaling by recruiting the RNF111 E3 ubiquitin ligase and
CC       promoting the degradation of inhibitory SMAD7 (By similarity).
CC       Also component of the AXIN1-HIPK2-TP53 complex which controls cell
CC       growth, apoptosis and development.
CC   -!- SUBUNIT: Homodimer. Component of the beta-catenin destruction
CC       complex, containing at least CTNNB1, an axin and GSK3B, that
CC       regulates CTNNB1 protein levels through phosphorylation and
CC       ubiquitination (By similarity). Interacts with GSK3B; the
CC       interaction hyperphosphorylates CTNNB1 leading to its
CC       ubiquitination and destruction. Interacts with DAXX; the
CC       interaction stimulates the interaction of DAXX with TP53,
CC       stimulates 'Ser-46' phosphorylation of TP53 and induces cell death
CC       on UV irradiation. Also interacts with APC, RNF111, SMAD6 and
CC       SMAD7. Interacts (via the C-terminal) with PPP1CA; the interaction
CC       dephosphorylates AXIN1 and regulates interaction with GSK3B.
CC       Interacts with PPP2CA; the interaction dephosphorylates AXIN1.
CC       Interacts with MDFI; the interaction decreases AXIN1-mediated JUN
CC       N-terminal kinase (JNK) activation. Interacts with MDFIC; the
CC       interaction inhibits beta-cateninin-mediated signaling and AXIN1-
CC       mediated JUN N-terminal kinase (JNK) activation (By similarity).
CC       Binds ANKRD6, PIAS1, PIAS2, PIAS4, SUMO1, MAP3K1 and MAP3K4.
CC       Component of the AXIN1-HIPK2-TP53 complex. Interacts directly in
CC       the complex with TP53 and HIPK2. Interacts with DIXDC1; the
CC       interaction prevents interaction with MAP3K1. Interacts with AIDA;
CC       the interaction blocks the AXIN1-mediated JNK activation through
CC       disrupting AXIN1 homodimerization and Wnt signaling. Interacts
CC       with LRP5 (via its phosphorylated PPPSP motifs); the interaction
CC       is stimulated by WNT1 and GSK3B and activates beta-catenin
CC       signaling. Interacts with CTNNB1 (via the armadillo repeats 2-7).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=On UV irradiation, translocates to the nucleus
CC       and colocalizes with DAAX (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O35625-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O35625-2; Sequence=VSP_000452;
CC   -!- TISSUE SPECIFICITY: Expressed in embryonic stem cells.
CC   -!- DEVELOPMENTAL STAGE: Widely expressed at E10.5 to E16.5 day.
CC   -!- PTM: Phosphorylation and dephosphorylation of AXIN1 regulates
CC       assembly and function of the beta-catenin complex. Phosphorylated
CC       by CK1 and GSK3B. Dephosphorylated by PPP1CA and PPP2CA.
CC       Phosphorylation by CK1 enhances binding of GSK3B to AXIN1 (By
CC       similarity). Also phosphorylated by CDK2 which regulates
CC       interaction with CTNBB1.
CC   -!- PTM: Sumoylation is required for AXIN1-mediated JNK activation.
CC   -!- SIMILARITY: Contains 1 DIX domain.
CC   -!- SIMILARITY: Contains 1 RGS domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC53285.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF009011; AAC53285.1; ALT_INIT; mRNA.
DR   IPI; IPI00845819; -.
DR   IPI; IPI00875849; -.
DR   RefSeq; NP_033863.2; NM_009733.2.
DR   UniGene; Mm.23684; -.
DR   ProteinModelPortal; O35625; -.
DR   SMR; O35625; 74-220, 780-863.
DR   DIP; DIP-42637N; -.
DR   IntAct; O35625; 2.
DR   MINT; MINT-1543084; -.
DR   STRING; O35625; -.
DR   PhosphoSite; O35625; -.
DR   PRIDE; O35625; -.
DR   Ensembl; ENSMUST00000074370; ENSMUSP00000073974; ENSMUSG00000024182.
DR   Ensembl; ENSMUST00000115005; ENSMUSP00000110657; ENSMUSG00000024182.
DR   GeneID; 12005; -.
DR   KEGG; mmu:12005; -.
DR   UCSC; uc008bdm.1; mouse.
DR   CTD; 12005; -.
DR   MGI; MGI:1096327; Axin1.
DR   eggNOG; roNOG11401; -.
DR   HOGENOM; HBG714290; -.
DR   HOVERGEN; HBG004324; -.
DR   InParanoid; O35625; -.
DR   OrthoDB; EOG47SSDB; -.
DR   NextBio; 280195; -.
DR   ArrayExpress; O35625; -.
DR   Bgee; O35625; -.
DR   CleanEx; MM_AXIN1; -.
DR   Genevestigator; O35625; -.
DR   GermOnline; ENSMUSG00000024182; Mus musculus.
DR   GO; GO:0034747; C:Axin-APC-beta-catenin-GSK3B complex; IDA:MGI.
DR   GO; GO:0005938; C:cell cortex; IDA:MGI.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:MGI.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0044459; C:plasma membrane part; IDA:MGI.
DR   GO; GO:0005625; C:soluble fraction; IDA:MGI.
DR   GO; GO:0008013; F:beta-catenin binding; IMP:MGI.
DR   GO; GO:0008013; F:beta-catenin binding; IPI:MGI.
DR   GO; GO:0070411; F:I-SMAD binding; IDA:BHF-UCL.
DR   GO; GO:0070411; F:I-SMAD binding; IPI:MGI.
DR   GO; GO:0008022; F:protein C-terminus binding; IDA:MGI.
DR   GO; GO:0032947; F:protein complex scaffold; IMP:BHF-UCL.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; IPI:MGI.
DR   GO; GO:0043621; F:protein self-association; IPI:MGI.
DR   GO; GO:0070412; F:R-SMAD binding; IPI:MGI.
DR   GO; GO:0016566; F:specific transcriptional repressor activity; IDA:MGI.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:MGI.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0048320; P:axial mesoderm formation; IMP:MGI.
DR   GO; GO:0060070; P:canonical Wnt receptor signaling pathway; IDA:MGI.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IGI:MGI.
DR   GO; GO:0009950; P:dorsal/ventral axis specification; IDA:MGI.
DR   GO; GO:0071514; P:genetic imprinting; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt receptor signaling pathway; IDA:MGI.
DR   GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:MGI.
DR   GO; GO:0090041; P:negative regulation of gene-specific transcription elongation from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0051248; P:negative regulation of protein metabolic process; IDA:MGI.
DR   GO; GO:0006913; P:nucleocytoplasmic transport; IDA:MGI.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; IMP:MGI.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; IMP:UniProtKB.
DR   GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:MGI.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:MGI.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:MGI.
DR   GO; GO:2000060; P:positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:MGI.
DR   GO; GO:0045941; P:positive regulation of transcription; IDA:BHF-UCL.
DR   GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IDA:MGI.
DR   GO; GO:0051443; P:positive regulation of ubiquitin-protein ligase activity; IMP:BHF-UCL.
DR   GO; GO:0030163; P:protein catabolic process; IDA:MGI.
DR   GO; GO:0051260; P:protein homooligomerization; IDA:MGI.
DR   GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
DR   GO; GO:0035412; P:regulation of catenin import into nucleus; IDA:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR   GO; GO:0035121; P:tail morphogenesis; IMP:MGI.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR014936; Axin_b-cat-bd.
DR   InterPro; IPR001158; DIX.
DR   InterPro; IPR000342; Regulat_G_prot_signal.
DR   InterPro; IPR016137; Regulat_G_prot_signal_superfam.
DR   Pfam; PF08833; Axin_b-cat_bind; 1.
DR   Pfam; PF00778; DIX; 1.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00021; DAX; 1.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48097; Regulat_G_prot_signal_superfam; 1.
DR   PROSITE; PS50841; DIX; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Cytoplasm; Developmental protein;
KW   Isopeptide bond; Nucleus; Phosphoprotein; Tumor suppressor;
KW   Ubl conjugation; Wnt signaling pathway.
FT   CHAIN         1    863       Axin-1.
FT                                /FTId=PRO_0000220889.
FT   DOMAIN       88    211       RGS.
FT   DOMAIN      781    863       DIX.
FT   REGION      209    338       Interaction with TP53.
FT   REGION      348    432       Interaction with GSK3B (By similarity).
FT   REGION      433    501       Interaction with beta-catenin (By
FT                                similarity).
FT   REGION      505    758       Interaction with RNF111 (By similarity).
FT   REGION      572    790       Interaction with PPP2CA (By similarity).
FT   REGION      678    753       Interaction with HIPK2.
FT   MOD_RES      75     75       Phosphoserine; by CK1 (By similarity).
FT   MOD_RES      77     77       Phosphoserine; by CK1 (By similarity).
FT   MOD_RES     217    217       Phosphoserine; by CK1 (By similarity).
FT   MOD_RES     468    468       Phosphoserine; by CK1 (By similarity).
FT   MOD_RES     480    480       Phosphothreonine; by GSK3-beta
FT                                (Probable).
FT   MOD_RES     485    485       Phosphoserine; by GSK3-beta.
FT   MOD_RES     492    492       Phosphoserine.
FT   CROSSLNK    858    858       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT   CROSSLNK    861    861       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT   VAR_SEQ     731    766       Missing (in isoform 2).
FT                                /FTId=VSP_000452.
FT   MUTAGEN     480    480       T->A: Greatly reduced GSK3B-mediated
FT                                phosphorylation; when associated with A-
FT                                485 and A-492.
FT   MUTAGEN     485    485       S->A: Greatly reduced GSK3B-mediated
FT                                phosphorylation and large effect on the
FT                                inhibitory activity in Wnt-signaling;
FT                                when associated with A-480 and A-492.
FT   MUTAGEN     492    492       S->A: Greatly reduced GSK3B-mediated
FT                                phosphorylation; when associated with A-
FT                                480 and A-485.
FT   MUTAGEN     492    492       S->I: Little effect on inhibitory
FT                                activity on Wnt-signaling.
FT   MUTAGEN     495    495       S->A: No effect on phosphorylation.
FT                                Little effect on inhibitory activity on
FT                                Wnt-signaling.
FT   MUTAGEN     858    863       Missing: Abolishes binding of PIAS1 and
FT                                PIAS2. Dramatically reduces sumoylation
FT                                and abolishes AXIN1-mediated JNK
FT                                activation. No effect on homodimerization
FT                                nor on Wnt-signaling.
SQ   SEQUENCE   863 AA;  96314 MW;  AD419D685411E9FB CRC64;
     MNVQEQGFPL DLGASFTEDA PRPPVPGEEG ELVSTDSRPV NHSFCSGKGT SIKSETSTAT
     PRRSDLDLGY EPEGSASPTP PYLRWAESLH SLLDDQDGIS LFRTFLKQEG CADLLDFWFA
     CSGFRKLEPC DSNEEKRLKL ARAIYRKYIL DSNGIVSRQT KPATKSFIKD CVMKQQIDPA
     MFDQAQTEIQ STMEENTYPS FLKSDIYLEY TRTGSESPKV CSDQSSGSGT GKGMSGYLPT
     LNEDEEWKCD QDADEDDGRD PLPPSRLTQK LLLETAAPRA PSSRRYNEGR ELRYGSWREP
     VNPYYVNSGY ALAPATSAND SEQQSLSSDA DTLSLTDSSV DGIPPYRIRK QHRREMQESI
     QVNGRVPLPH IPRTYRMPKE IRVEPQKFAE ELIHRLEAVQ RTREAEEKLE ERLKRVRMEE
     EGEDGEMPSG PMASHKLPSV PAWHHFPPRY VDMGCSGLRD AHEENPESIL DEHVQRVMRT
     PGCQSPGPGH RSPDSGHVAK TAVLGGTASG HGKHVPKLGL KLDTAGLHHH RHVHHHVHHN
     SARPKEQMEA EVARRVQSSF SWGPETHGHA KPRSYSENAG TTLSAGDLPF GGKTSAPSKR
     NTKKAESGKN ANAEVPSTTE DAEKNQKIMQ WIIEGEKEIS RHRKAGHGSS GLRKQQAHES
     SRPLSIERPG AVHPWVSAQL RNSVQPSHLF IQDPTMPPNP APNPLTQLEE ARRRLEEEEK
     RANKLPSKQR YVQAVMQRGR TCVRPACAPV LSVVPAVSDL ELSETETKSQ RKAGGGSAPP
     CDSIVVGYYF CGEPIPYRTL VRGRAVTLGQ FKELLTKKGS YRYYFKKVSD EFDCGVVFEE
     VREDEPVLPV FEEKIIGKVE KVD
//
ID   VIAAT_MOUSE             Reviewed;         525 AA.
AC   O35633;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2003, sequence version 3.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Vesicular inhibitory amino acid transporter;
DE   AltName: Full=GABA and glycine transporter;
DE   AltName: Full=Solute carrier family 32 member 1;
DE   AltName: Full=Vesicular GABA transporter;
DE            Short=mVGAT;
DE            Short=mVIAAT;
GN   Name=Slc32a1; Synonyms=Vgat, Viaat;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=98055669; PubMed=9395291; DOI=10.1016/S0014-5793(97)01279-9;
RA   Sagne C., El Mestikawy S., Isambert M.-F., Hamon M., Henry J.-P.,
RA   Giros B.P., Gasnier B.;
RT   "Cloning of a functional vesicular GABA and glycine transporter by
RT   screening of genome databases.";
RL   FEBS Lett. 417:177-183(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RX   MEDLINE=22461323; PubMed=12573541; DOI=10.1016/S0169-328X(02)00648-4;
RA   Ebihara S., Obata K., Yanagawa Y.;
RT   "Mouse vesicular GABA transporter gene: genomic organization,
RT   transcriptional regulation and chromosomal localization.";
RL   Brain Res. Mol. Brain Res. 110:126-139(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=22110478; PubMed=12115694; DOI=10.1002/cne.10272;
RA   Jellali A., Stussi-Garaud C., Gasnier B., Rendon A., Sahel J.-A.,
RA   Dreyfus H., Picaud S.;
RT   "Cellular localization of the vesicular inhibitory amino acid
RT   transporter in the mouse and human retina.";
RL   J. Comp. Neurol. 449:76-87(2002).
RN   [5]
RP   NITRATION [LARGE SCALE ANALYSIS] AT TYR-186, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16800626; DOI=10.1021/bi060474w;
RA   Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
RA   Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
RA   Squier T.C., Bigelow D.J.;
RT   "Endogenously nitrated proteins in mouse brain: links to
RT   neurodegenerative disease.";
RL   Biochemistry 45:8009-8022(2006).
CC   -!- FUNCTION: Involved in the uptake of GABA and glycine into the
CC       synaptic vesicles.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=b;
CC         IsoId=O35633-1; Sequence=Displayed;
CC       Name=2; Synonyms=a;
CC         IsoId=O35633-2; Sequence=VSP_007063;
CC   -!- TISSUE SPECIFICITY: Brain and retina. Localized in horizontal cell
CC       tips at both rod and cone terminals.
CC   -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2
CC       family.
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DR   EMBL; AB080232; BAC44888.1; -; Genomic_DNA.
DR   EMBL; AB080232; BAC44889.1; -; Genomic_DNA.
DR   EMBL; AJ001598; CAA04864.1; -; mRNA.
DR   EMBL; BC052020; AAH52020.1; -; mRNA.
DR   IPI; IPI00132720; -.
DR   IPI; IPI00221831; -.
DR   RefSeq; NP_033534.2; NM_009508.2.
DR   UniGene; Mm.143404; -.
DR   UniGene; Mm.413854; -.
DR   ProteinModelPortal; O35633; -.
DR   STRING; O35633; -.
DR   TCDB; 2.A.18.5.3; amino acid/auxin permease (AAAP) family.
DR   PRIDE; O35633; -.
DR   Ensembl; ENSMUST00000045738; ENSMUSP00000036299; ENSMUSG00000037771.
DR   Ensembl; ENSMUST00000109483; ENSMUSP00000105109; ENSMUSG00000037771.
DR   GeneID; 22348; -.
DR   KEGG; mmu:22348; -.
DR   UCSC; uc008nqk.1; mouse.
DR   CTD; 22348; -.
DR   MGI; MGI:1194488; Slc32a1.
DR   eggNOG; roNOG15425; -.
DR   GeneTree; ENSGT00490000043380; -.
DR   HOGENOM; HBG713804; -.
DR   HOVERGEN; HBG061364; -.
DR   InParanoid; O35633; -.
DR   OMA; GFIHSLE; -.
DR   OrthoDB; EOG4HMJ91; -.
DR   PhylomeDB; O35633; -.
DR   NextBio; 302627; -.
DR   ArrayExpress; O35633; -.
DR   Bgee; O35633; -.
DR   Genevestigator; O35633; -.
DR   GermOnline; ENSMUSG00000037771; Mus musculus.
DR   GO; GO:0051286; C:cell tip; IDA:MGI.
DR   GO; GO:0044316; C:cone cell pedicle; IDA:MGI.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044292; C:dendrite terminus; IDA:MGI.
DR   GO; GO:0060077; C:inhibitory synapse; IDA:MGI.
DR   GO; GO:0005887; C:integral to plasma membrane; IC:MGI.
DR   GO; GO:0015495; F:gamma-aminobutyric acid:hydrogen symporter activity; IDA:MGI.
DR   GO; GO:0015187; F:glycine transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR   InterPro; IPR013057; AA_transpt_TM.
DR   Pfam; PF01490; Aa_trans; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasmic vesicle; Glycoprotein; Membrane;
KW   Neurotransmitter transport; Nitration; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    525       Vesicular inhibitory amino acid
FT                                transporter.
FT                                /FTId=PRO_0000093822.
FT   TOPO_DOM      1    133       Cytoplasmic (Potential).
FT   TRANSMEM    134    154       Helical; (Potential).
FT   TOPO_DOM    155    204       Lumenal, vesicle (Potential).
FT   TRANSMEM    205    225       Helical; (Potential).
FT   TOPO_DOM    226    242       Cytoplasmic (Potential).
FT   TRANSMEM    243    263       Helical; (Potential).
FT   TOPO_DOM    264    265       Lumenal, vesicle (Potential).
FT   TRANSMEM    266    286       Helical; (Potential).
FT   TOPO_DOM    287    305       Cytoplasmic (Potential).
FT   TRANSMEM    306    326       Helical; (Potential).
FT   TOPO_DOM    327    341       Lumenal, vesicle (Potential).
FT   TRANSMEM    342    362       Helical; (Potential).
FT   TOPO_DOM    363    384       Cytoplasmic (Potential).
FT   TRANSMEM    385    405       Helical; (Potential).
FT   TOPO_DOM    406    438       Lumenal, vesicle (Potential).
FT   TRANSMEM    439    459       Helical; (Potential).
FT   TOPO_DOM    460    461       Cytoplasmic (Potential).
FT   TRANSMEM    462    482       Helical; (Potential).
FT   TOPO_DOM    483    489       Lumenal, vesicle (Potential).
FT   TRANSMEM    490    510       Helical; (Potential).
FT   TOPO_DOM    511    525       Cytoplasmic (Potential).
FT   MOD_RES     186    186       Nitrated tyrosine.
FT   CARBOHYD    341    341       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     515    525       LIEAYRTNAED -> KFAGLET (in isoform 2).
FT                                /FTId=VSP_007063.
FT   CONFLICT    432    432       G -> E (in Ref. 1; CAA04864).
SQ   SEQUENCE   525 AA;  57381 MW;  EBD63E01A4B54C07 CRC64;
     MATLLRSKLT NVATSVSNKS QAKVSGMFAR MGFQAATDEE AVGFAHCDDL DFEHRQGLQM
     DILKSEGEPC GDEGAEAPVE GDIHYQRGGA PLPPSGSKDQ AVGAGGEFGG HDKPKITAWE
     AGWNVTNAIQ GMFVLGLPYA ILHGGYLGLF LIIFAAVVCC YTGKILIACL YEENEDGEVV
     RVRDSYVAIA NACCAPRFPT LGGRVVNVAQ IIELVMTCIL YVVVSGNLMY NSFPGLPVSQ
     KSWSIIATAV LLPCAFLKNL KAVSKFSLLC TLAHFVINIL VIAYCLSRAR DWAWEKVKFY
     IDVKKFPISI GIIVFSYTSQ IFLPSLEGNM QQPSEFHCMM NWTHIAACVL KGLFALVAYL
     TWADETKEVI TDNLPGSIRA VVNLFLVAKA LLSYPLPFFA AVEVLEKSLF QEGSRAFFPA
     CYGGDGRLKS WGLTLRCALV VFTLLMAIYV PHFALLMGLT GSLTGAGLCF LLPSLFHLRL
     LWRKLLWHQV FFDVAIFVIG GICSVSGFVH SLEGLIEAYR TNAED
//
ID   STAG2_MOUSE             Reviewed;        1231 AA.
AC   O35638; Q6NZN7;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Cohesin subunit SA-2;
DE   AltName: Full=SCC3 homolog 2;
DE   AltName: Full=Stromal antigen 2;
GN   Name=Stag2; Synonyms=Sa2, Sap2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RA   Barbero J.L., Carreiro C.;
RT   "Homologue to human nuclear protein SA2.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1061 AND THR-1160, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Component of cohesin complex, a complex required for the
CC       cohesion of sister chromatids after DNA replication. The cohesin
CC       complex apparently forms a large proteinaceous ring within which
CC       sister chromatids can be trapped. At anaphase, the complex is
CC       cleaved and dissociates from chromatin, allowing sister chromatids
CC       to segregate. The cohesin complex may also play a role in spindle
CC       pole assembly during mitosis (By similarity).
CC   -!- SUBUNIT: Interacts directly with RAD21 in cohesin complex. Cohesin
CC       complexes are composed of a heterodimer between a SMC1 protein
CC       (SMC1A or SMC1B) and SMC3, which are attached via their hinge
CC       domain, and RAD21 which link them at their heads, and one STAG
CC       protein (STAG1, STAG2 or STAG3). In cohesin complexes, STAG2 is
CC       mutually exclusive with STAG1 and STAG3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome (By similarity).
CC       Chromosome, centromere (By similarity). Note=Associates with
CC       chromatin. Before prophase it is scattered along chromosome arms.
CC       During prophase, most of cohesin complexes dissociate from
CC       chromatin probably because of phosphorylation by PLK, except at
CC       centromeres, where cohesin complexes remain. At anaphase, the
CC       RAD21 subunit of cohesin is cleaved, leading to the dissociation
CC       of the complex from chromosomes, allowing chromosome separation.
CC       In germ cells, cohesin complex dissociates from chromatin at
CC       prophase I, and may be replaced by a meiosis-specific cohesin
CC       complex (By similarity).
CC   -!- PTM: Phosphorylated by PLK. The large dissociation of cohesin from
CC       chromosome arms during prophase is partly due to its
CC       phosphorylation (By similarity).
CC   -!- SIMILARITY: Belongs to the SCC3 family.
CC   -!- SIMILARITY: Contains 1 SCD (stromalin conservative) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BC066041; Type=Frameshift; Positions=53;
CC       Sequence=CAA05638.1; Type=Frameshift; Positions=23;
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DR   EMBL; AJ002636; CAA05638.1; ALT_FRAME; mRNA.
DR   EMBL; BC066041; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00776104; -.
DR   PIR; T30194; T30194.
DR   UniGene; Mm.290422; -.
DR   ProteinModelPortal; O35638; -.
DR   STRING; O35638; -.
DR   PhosphoSite; O35638; -.
DR   PRIDE; O35638; -.
DR   Ensembl; ENSMUST00000069619; ENSMUSP00000063250; ENSMUSG00000025862.
DR   Ensembl; ENSMUST00000115072; ENSMUSP00000110724; ENSMUSG00000025862.
DR   UCSC; uc009tax.1; mouse.
DR   MGI; MGI:1098583; Stag2.
DR   HOVERGEN; HBG057636; -.
DR   OrthoDB; EOG4GB759; -.
DR   ArrayExpress; O35638; -.
DR   Bgee; O35638; -.
DR   CleanEx; MM_STAG2; -.
DR   Genevestigator; O35638; -.
DR   GermOnline; ENSMUSG00000025862; Mus musculus.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR   GO; GO:0007126; P:meiosis; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR020839; SCD.
DR   InterPro; IPR013721; STAG.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 4.
DR   Pfam; PF08514; STAG; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS51425; SCD; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Centromere; Chromosome;
KW   Chromosome partition; Meiosis; Mitosis; Nucleus; Phosphoprotein.
FT   CHAIN         1   1231       Cohesin subunit SA-2.
FT                                /FTId=PRO_0000120186.
FT   DOMAIN      293    378       SCD.
FT   COMPBIAS   1096   1101       Poly-Ser.
FT   MOD_RES    1058   1058       Phosphoserine (By similarity).
FT   MOD_RES    1061   1061       Phosphoserine.
FT   MOD_RES    1065   1065       Phosphoserine (By similarity).
FT   MOD_RES    1112   1112       Phosphothreonine (By similarity).
FT   MOD_RES    1160   1160       Phosphothreonine.
FT   CONFLICT    299    299       Y -> D (in Ref. 2).
FT   CONFLICT    607    608       ND -> KH (in Ref. 2).
FT   CONFLICT    881    881       S -> T (in Ref. 2).
FT   CONFLICT    951    951       F -> L (in Ref. 2).
SQ   SEQUENCE   1231 AA;  141343 MW;  987BE5C39C2B4C98 CRC64;
     MIAAPEIQTD FNLLQESETH FSSDTDFEDI EGKIQKQGKG KTCKKGKKGP AEKGKSGNGG
     GKPPSGSNRM NGHHQQNGVE NMMLFEVVKM GKSAMQSVVD DWIESYKHDR DIALLDLINF
     FIQCSGCKGV VTAEMFRHMQ NSEIIRKMTE EFDEDSGDYP LTMAGPQWKK FKSSFCEFIG
     VLVRQCQYSI IYDEYMMDTV ISLLTGLSDS QVRAFRHTST LAAMKLMTAL VNVALNLSIN
     MDNTQRQYEA ERNKMIGKRA NERLELLLQK RKELQENQDE IENMMNAIFK GVFVHRYRYA
     IAEIRAICIE EIGIWMKMYS DAFLNDSYLK YVGWTMHDKQ GEVRLKCLTA LQGLYYNKEL
     NSKLELFTSR FKDRIVSMTL DKEYDVAVQA IKLLTLVLQS SEEVLTAEDC ENVYHLVYSA
     HRPVAVAAGE FLYKKLFSRR DPEEDGLMKR RGRQGPNANL VKTLVFFFLE SELHEHAAYL
     VDSMWDCATE LLKDWECMNS LLLEEPLSGE EALTDRQESA LIEIMLCTIR QAAECHPPVG
     RGTGKRVLTA KEKKTQLDDR TRITELFAVA LPQLLAKYSV DAEKVTNLLQ LPQYFDLEIY
     TTGRLENDLD ALLRQIRNIV EKHTDTDVLE ACSKTYHALC NEEFTIFNRV DISRSQLIDE
     LADKFNRLLE DFLQEGEEPD EDDAYQVLST LKRITAFHNA HDLSKWDLFA CNYKLLKTGI
     ENGDMPEQIV IHALQCAHYV ILWQLAKITE STSTKEDLLR LKKQMRVFCQ ICQHYLTNVN
     TTVKEQAFTI LCDILMIFSH QIMSGGRDML EPLVYTPDSS LQSELLSFIL DHVFIEQDDD
     SNSADGQQED EASKIEALHK RRNLLAAFCK LIVYTVVEMN SAADIFKQYM KYYNDYGDII
     KETMSKTRQI DKIQCAKTLI LSLQQLFNEM IQENGYNFDR SSSTFSGIKE FARRFALTFG
     LDQLKTREAI AMLHKDGIEF AFKEPNPQGE SHPPLNLAFL DILSEFSSKL LRQDKRTVYV
     YLEKFMTFQM SLRREDVWLP LMSYRNSLLA GGDDDTMSVI SGMSSRGSTV RSKKSKPSTG
     KRKVVEGMQL ALPEESSSSD SMWLSREQTL HTPVMMQTPQ LTSTIMREPK RLRPEDSFMS
     VYPMQAEHHQ TPLDYNRRGT SLMEDDEEPI VEDVMMSSEG RIEDLNEGMD FDTMDIDLPP
     SKNRRERTEL KPDFFDPASI MDESVLGVSM F
//
ID   AP1B1_MOUSE             Reviewed;         943 AA.
AC   O35643; Q922E2;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   30-NOV-2010, entry version 87.
DE   RecName: Full=AP-1 complex subunit beta-1;
DE   AltName: Full=Adapter-related protein complex 1 subunit beta-1;
DE   AltName: Full=Adaptor protein complex AP-1 subunit beta-1;
DE   AltName: Full=Beta-1-adaptin;
DE   AltName: Full=Beta-adaptin 1;
DE   AltName: Full=Clathrin assembly protein complex 1 beta large chain;
DE   AltName: Full=Golgi adaptor HA1/AP1 adaptin beta subunit;
GN   Name=Ap1b1; Synonyms=Adtb1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Embryonic brain;
RX   MEDLINE=97419266; PubMed=9271666; DOI=10.1007/s003359900531;
RA   Guilbaud C., Peyrard M., Fransson I., Clifton S.W., Roe B.A.,
RA   Carter N.P., Dumanski J.P.;
RT   "Characterization of the mouse beta-prime adaptin gene; cDNA sequence,
RT   genomic structure, and chromosomal localization.";
RL   Mamm. Genome 8:651-656(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NITRATION [LARGE SCALE ANALYSIS] AT TYR-574, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16800626; DOI=10.1021/bi060474w;
RA   Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
RA   Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
RA   Squier T.C., Bigelow D.J.;
RT   "Endogenously nitrated proteins in mouse brain: links to
RT   neurodegenerative disease.";
RL   Biochemistry 45:8009-8022(2006).
CC   -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1
CC       that plays a role in protein sorting in the late-Golgi/trans-Golgi
CC       network (TGN) and/or endosomes. The AP complexes mediate both the
CC       recruitment of clathrin to membranes and the recognition of
CC       sorting signals within the cytosolic tails of transmembrane cargo
CC       molecules.
CC   -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is an heterotetramer
CC       composed of two large adaptins (gamma-type subunit AP1G1 and beta-
CC       type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or
CC       AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or
CC       AP1S3).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle,
CC       clathrin-coated vesicle membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity). Golgi apparatus (By similarity).
CC       Note=Component of the coat surrounding the cytoplasmic face of
CC       coated vesicles located at the Golgi complex (By similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
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DR   EMBL; Y07919; CAA69224.1; -; mRNA.
DR   EMBL; BC008513; AAH08513.1; -; mRNA.
DR   IPI; IPI00648683; -.
DR   UniGene; Mm.274816; -.
DR   ProteinModelPortal; O35643; -.
DR   SMR; O35643; 2-583, 711-943.
DR   STRING; O35643; -.
DR   PhosphoSite; O35643; -.
DR   PRIDE; O35643; -.
DR   Ensembl; ENSMUST00000009234; ENSMUSP00000009234; ENSMUSG00000009090.
DR   MGI; MGI:1096368; Ap1b1.
DR   eggNOG; roNOG10896; -.
DR   HOVERGEN; HBG050515; -.
DR   PhylomeDB; O35643; -.
DR   ArrayExpress; O35643; -.
DR   Bgee; O35643; -.
DR   CleanEx; MM_AP1B1; -.
DR   Genevestigator; O35643; -.
DR   GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR   GO; GO:0030665; C:clathrin coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005802; C:trans-Golgi network; TAS:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR   InterPro; IPR016342; AP_complex_bsu.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR012295; Beta2_adaptin/TATA-box-bd_C.
DR   InterPro; IPR009028; Calthrin/coatomer_app_sub_C.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   InterPro; IPR013041; Clathrin/coatomer_app_Ig-like.
DR   InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR   InterPro; IPR013037; Clathrin_b-adaptin_app_Ig-like.
DR   InterPro; IPR015151; Clathrin_b-adaptin_app_sub_C.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Gene3D; G3DSA:3.30.310.10; b_Adaptin_TBP_C; 1.
DR   Gene3D; G3DSA:2.60.40.1150; Clathrin_b-adaptin_app_Ig-like; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   Pfam; PF02883; Alpha_adaptinC2; 1.
DR   Pfam; PF09066; B2-adapt-app_C; 1.
DR   PIRSF; PIRSF002291; AP_complex_beta; 1.
DR   SMART; SM00809; Alpha_adaptinC2; 1.
DR   SUPFAM; SSF55711; AP2_adap_app; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF49348; Clath_adapt; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasmic vesicle; Endocytosis; Golgi apparatus;
KW   Membrane; Nitration; Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1    943       AP-1 complex subunit beta-1.
FT                                /FTId=PRO_0000193739.
FT   COMPBIAS    576    722       Pro-rich (stalk region).
FT   MOD_RES     318    318       N6-acetyllysine (By similarity).
FT   MOD_RES     574    574       Nitrated tyrosine.
FT   MOD_RES     894    894       Phosphotyrosine (By similarity).
FT   CONFLICT    227    227       D -> A (in Ref. 2; AAH08513).
FT   CONFLICT    288    288       L -> P (in Ref. 2; AAH08513).
SQ   SEQUENCE   943 AA;  103979 MW;  7A67869C1CAAF973 CRC64;
     MTDSKYFTTT KKGEIFELKA ELNSDKKEKK KEAVKKVIAS MTVGKDVSAL FPDVVNCMQT
     DNLELKKLVY LYLMNYAKSQ PDMAIMAVNT FVKDCEDPNP LIRALAVRTM GCIRVDKITE
     YLCEPLRKCL KDEDPYVRKT AAVCVAKLHD INAQLVEDQG FLDTLKDLIS DSNPMVVANA
     VAALSEIAES HPSSNLLDLN PQSINKLLTA LNECTEWGQI FILDCLDNYM PKDDREAQSI
     CERVTPRLSH ANSAVVLSAV KVLMKFMEML SKDLDYYATL LKKLAPPLVT LLSAEPELQY
     VALRNINLIV QKRPEILKHE MKVFFVKYND PIYVKLEKLD IMIRLASQAN IAQVLAELKE
     YATEVDVDFV RKAVRAIGRC AIKVEQSAER CVSTLLDLIQ TKVNYVVQEA IVVIKDIFRK
     YPNKYESVIA TLCENLDSLD EPEARAAMIW IVGEYAERID NADELLESFL EGFHDESTQV
     QLQLLTAIVK LFLKKPTETQ ELVQQVLSLA TQDSDNPDLR DRGYIYWRLL STDPVAAKEV
     VLAEKPLISE ETDLIEPTLL DELICYIGTL ASVYHKPPNA FVEGGRGVVH KSLPPRTASS
     ESTESPETAP AGAPAGDQPD VIPAQGDLLG DLLNLDLGPP VSGPPLAASS VQMGAVDLLG
     GGLDSLIGDS NFGAPSASVA AAPAPARLGA PISSGLSDLF DLTSGVGTLS GSYVAPKAVW
     LPAMKAKGLE ISGTFTRQAG SISMDLQLTN KALQVMTDFA IQFNRNSFGL APAAPLQVHV
     PLSPNQTVEI SLPLNTVGSV LKMEPLNNLQ VAVKNNIDVF YFSTLYPLHV LFVEDGKMDR
     QMFLATWKDI ANENEAQFQI RDCPLNTEAA SNKLQSSNIF TVAKRNVEGQ DMLYQSLKLT
     NGIWVLAELR IQPGNPSFTL SLKCRAPEVS QHVYQAYETI LKN
//
ID   ITBP1_MOUSE             Reviewed;         200 AA.
AC   O35671; Q542A8;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Integrin beta-1-binding protein 1;
DE   AltName: Full=Bodenin;
GN   Name=Itgb1bp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=98289806; PubMed=9626504;
RX   DOI=10.1002/(SICI)1097-0177(199806)212:2<293::AID-AJA14>3.0.CO;2-5;
RA   Faisst A.M., Gruss P.;
RT   "Bodenin: a novel murine gene expressed in restricted areas of the
RT   brain.";
RL   Dev. Dyn. 212:293-303(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Kidney, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in the recruitment of beta-1 integrins
CC       to the focal contacts during integrin-dependent cell adhesion (By
CC       similarity).
CC   -!- SUBUNIT: Interacts specifically with the beta-1 integrin
CC       cytoplasmic domain-associated protein-1 (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in the brain.
CC   -!- DEVELOPMENTAL STAGE: First expressed in the heart primordium at
CC       E8.5.
CC   -!- SIMILARITY: Contains 1 PID domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AJ001373; CAA04706.1; -; mRNA.
DR   EMBL; AK002786; BAB22357.1; -; mRNA.
DR   EMBL; AK004172; BAB23206.1; -; mRNA.
DR   EMBL; AK007635; BAB25151.1; -; mRNA.
DR   EMBL; AK075577; BAC35832.1; -; mRNA.
DR   EMBL; AK089937; BAC41007.1; -; mRNA.
DR   EMBL; BC028772; AAH28772.1; -; mRNA.
DR   IPI; IPI00132866; -.
DR   RefSeq; NP_032429.1; NM_008403.4.
DR   UniGene; Mm.273333; -.
DR   ProteinModelPortal; O35671; -.
DR   STRING; O35671; -.
DR   PhosphoSite; O35671; -.
DR   PRIDE; O35671; -.
DR   Ensembl; ENSMUST00000076260; ENSMUSP00000075609; ENSMUSG00000062352.
DR   GeneID; 16413; -.
DR   KEGG; mmu:16413; -.
DR   UCSC; uc007ndl.1; mouse.
DR   CTD; 16413; -.
DR   MGI; MGI:1306802; Itgb1bp1.
DR   eggNOG; roNOG06435; -.
DR   HOGENOM; HBG713132; -.
DR   HOVERGEN; HBG052155; -.
DR   InParanoid; O35671; -.
DR   OMA; LDTCAEF; -.
DR   OrthoDB; EOG483D5W; -.
DR   PhylomeDB; O35671; -.
DR   NextBio; 289601; -.
DR   ArrayExpress; O35671; -.
DR   Bgee; O35671; -.
DR   CleanEx; MM_ITGB1BP1; -.
DR   Genevestigator; O35671; -.
DR   GermOnline; ENSMUSG00000062352; Mus musculus.
DR   GO; GO:0005829; C:cytosol; ISS:HGNC.
DR   GO; GO:0030027; C:lamellipodium; ISS:HGNC.
DR   GO; GO:0001726; C:ruffle; ISS:HGNC.
DR   GO; GO:0007160; P:cell-matrix adhesion; ISS:HGNC.
DR   InterPro; IPR019517; Integrin-bd_ICAP-1.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF10480; ICAP-1_inte_bdg; 1.
DR   SMART; SM00462; PTB; 1.
DR   PROSITE; PS01179; PID; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Phosphoprotein.
FT   CHAIN         1    200       Integrin beta-1-binding protein 1.
FT                                /FTId=PRO_0000084265.
FT   DOMAIN       58    200       PID.
FT   COMPBIAS     10     55       Ser/Thr-rich.
FT   MOD_RES      41     41       Phosphoserine (By similarity).
SQ   SEQUENCE   200 AA;  21644 MW;  F7F0EB09490AEA37 CRC64;
     MFRKGKKRHS SSSSQSSEIS TKSKSVDSSL GGLSRSSTVA SLDTDSTKSS GQSNSNLDTC
     AEFRIKYVGA IEKLAVSEGK SLEGPLDLIN YIDVAQQDGK LPFVPLEEEF ILGVSKYGIK
     VSTTDQHGVL HRHALYLIIR MVCYDDGLGA GKSLLALKTT DASNEEYSLW VYQCNSLEQA
     QAICKVLSTA FDSVLTSDKS
//
ID   MGLL_MOUSE              Reviewed;         303 AA.
AC   O35678; Q3V2R0; Q9D9G8;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Monoglyceride lipase;
DE            Short=MGL;
DE            EC=3.1.1.23;
DE   AltName: Full=Monoacylglycerol lipase;
DE            Short=MAGL;
GN   Name=Mgll;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ACTIVE SITE, AND
RP   MUTAGENESIS OF SER-122; ASP-239; ASP-243; HIS-269; HIS-272; HIS-284
RP   AND HIS-292.
RC   TISSUE=Adipose tissue;
RX   MEDLINE=98001701; PubMed=9341166; DOI=10.1074/jbc.272.43.27218;
RA   Karlsson M., Contreras J.A., Hellman U., Tornqvist H., Holm C.;
RT   "cDNA cloning, tissue distribution, and identification of the
RT   catalytic triad of monoglyceride lipase. Evolutionary relationship to
RT   esterases, lysophospholipases, and haloperoxidases.";
RL   J. Biol. Chem. 272:27218-27223(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Adipose tissue;
RX   MEDLINE=21363420; PubMed=11470505; DOI=10.1016/S0378-1119(01)00559-5;
RA   Karlsson M., Reue K., Xia Y.-R., Lusis A.J., Langin D., Tornqvist H.,
RA   Holm C.;
RT   "Exon-intron organization and chromosomal localization of the mouse
RT   monoglyceride lipase gene.";
RL   Gene 272:11-18(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NITRATION [LARGE SCALE ANALYSIS] AT TYR-58, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16800626; DOI=10.1021/bi060474w;
RA   Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
RA   Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
RA   Squier T.C., Bigelow D.J.;
RT   "Endogenously nitrated proteins in mouse brain: links to
RT   neurodegenerative disease.";
RL   Biochemistry 45:8009-8022(2006).
RN   [6]
RP   FUNCTION.
RX   PubMed=17700715; DOI=10.1038/sj.bjp.0707425;
RA   Comelli F., Giagnoni G., Bettoni I., Colleoni M., Costa B.;
RT   "The inhibition of monoacylglycerol lipase by URB602 showed an anti-
RT   inflammatory and anti-nociceptive effect in a murine model of acute
RT   inflammation.";
RL   Br. J. Pharmacol. 152:787-794(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   FUNCTION.
RX   PubMed=19029917; DOI=10.1038/nchembio.129;
RA   Long J.Z., Li W., Booker L., Burston J.J., Kinsey S.G.,
RA   Schlosburg J.E., Pavon F.J., Serrano A.M., Selley D.E., Parsons L.H.,
RA   Lichtman A.H., Cravatt B.F.;
RT   "Selective blockade of 2-arachidonoylglycerol hydrolysis produces
RT   cannabinoid behavioral effects.";
RL   Nat. Chem. Biol. 5:37-44(2009).
RN   [9]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20729846; DOI=10.1038/nn.2616;
RA   Schlosburg J.E., Blankman J.L., Long J.Z., Nomura D.K., Pan B.,
RA   Kinsey S.G., Nguyen P.T., Ramesh D., Booker L., Burston J.J.,
RA   Thomas E.A., Selley D.E., Sim-Selley L.J., Liu Q.S., Lichtman A.H.,
RA   Cravatt B.F.;
RT   "Chronic monoacylglycerol lipase blockade causes functional antagonism
RT   of the endocannabinoid system.";
RL   Nat. Neurosci. 13:1113-1119(2010).
CC   -!- FUNCTION: Converts monoacylglycerides to free fatty acids and
CC       glycerol. Hydrolyzes the endocannabinoid 2-arachidonoylglycerol,
CC       and thereby contributes to the regulation of endocannabinoid
CC       signaling, nociperception and perception of pain. Regulates the
CC       levels of fatty acids that serve as signaling molecules and
CC       promote cancer cell migration, invasion and tumor growth (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolyzes glycerol monoesters of long-chain
CC       fatty acids.
CC   -!- PATHWAY: Glycerolipid metabolism; triacylglycerol degradation.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O35678-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O35678-2; Sequence=VSP_010315;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- DISRUPTION PHENOTYPE: Ten-fold increase in brain 2-
CC       arachidonoylglycerol levels, combined with low levels of brain
CC       arachidonic acid.
CC   -!- MISCELLANEOUS: Short-term inhibition causes analgesia, while long-
CC       term inhibition causes tolerance to endocannabinoids acting on
CC       brain cannabinoid receptor CNR1, and a reduction in brain
CC       cannabinoid receptor CNR1 activity.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily.
CC       Monoacylglycerol lipase family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ001118; CAA04544.1; -; mRNA.
DR   EMBL; AJ316580; CAC69874.1; -; mRNA.
DR   EMBL; AK006949; BAB24800.1; -; mRNA.
DR   EMBL; AK131645; BAE20737.1; -; mRNA.
DR   EMBL; BC057965; AAH57965.1; -; mRNA.
DR   IPI; IPI00112675; -.
DR   IPI; IPI00953761; -.
DR   RefSeq; NP_001159721.1; NM_001166249.1.
DR   RefSeq; NP_001159722.1; NM_001166250.1.
DR   RefSeq; NP_001159723.1; NM_001166251.1.
DR   RefSeq; NP_035974.1; NM_011844.4.
DR   UniGene; Mm.272197; -.
DR   ProteinModelPortal; O35678; -.
DR   SMR; O35678; 6-295.
DR   STRING; O35678; -.
DR   MEROPS; S33.979; -.
DR   PhosphoSite; O35678; -.
DR   PRIDE; O35678; -.
DR   Ensembl; ENSMUST00000089449; ENSMUSP00000086872; ENSMUSG00000033174.
DR   Ensembl; ENSMUST00000113580; ENSMUSP00000109210; ENSMUSG00000033174.
DR   Ensembl; ENSMUST00000113585; ENSMUSP00000109215; ENSMUSG00000033174.
DR   GeneID; 23945; -.
DR   KEGG; mmu:23945; -.
DR   UCSC; uc009cvp.1; mouse.
DR   CTD; 23945; -.
DR   MGI; MGI:1346042; Mgll.
DR   eggNOG; roNOG15341; -.
DR   GeneTree; ENSGT00390000011364; -.
DR   HOVERGEN; HBG049220; -.
DR   OrthoDB; EOG4HMJ9X; -.
DR   PhylomeDB; O35678; -.
DR   BRENDA; 3.1.1.23; 244.
DR   NextBio; 303757; -.
DR   ArrayExpress; O35678; -.
DR   Bgee; O35678; -.
DR   CleanEx; MM_MGLL; -.
DR   Genevestigator; O35678; -.
DR   GermOnline; ENSMUSG00000033174; Mus musculus.
DR   GO; GO:0047372; F:acylglycerol lipase activity; IMP:UniProtKB.
DR   GO; GO:0046464; P:acylglycerol catabolic process; IMP:UniProtKB.
DR   GO; GO:0019369; P:arachidonic acid metabolic process; IMP:UniProtKB.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:2000124; P:regulation of endocannabinoid signaling pathway; IMP:UniProtKB.
DR   GO; GO:0050727; P:regulation of inflammatory response; IMP:UniProtKB.
DR   GO; GO:0051930; P:regulation of sensory perception of pain; IMP:UniProtKB.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR022742; AB_hydrolase_N.
DR   Pfam; PF12146; Hydrolase_4; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PROSITE; PS00120; LIPASE_SER; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Fatty acid biosynthesis; Hydrolase;
KW   Lipid degradation; Lipid metabolism; Lipid synthesis; Nitration;
KW   Phosphoprotein; Serine esterase.
FT   CHAIN         1    303       Monoglyceride lipase.
FT                                /FTId=PRO_0000191266.
FT   ACT_SITE    122    122       Nucleophile.
FT   ACT_SITE    239    239       Charge relay system.
FT   ACT_SITE    269    269       Charge relay system.
FT   MOD_RES      58     58       Nitrated tyrosine.
FT   MOD_RES     189    189       Phosphoserine.
FT   VAR_SEQ      78    303       VGHGQSEGERMVVSDFQVFVRDVLQHVDTIQKDYPDVPIFL
FT                                LGHSMGGAISILVAAERPTYFSGMVLISPLVLANPESASTL
FT                                KVLAAKLLNFVLPNMTLGRIDSSVLSRNKSEVDLYNSDPLV
FT                                CRAGLKVCFGIQLLNAVARVERAMPRLTLPFLLLQGSADRL
FT                                CDSKGAYLLMESSRSQDKTLKMYEGAYHVLHRELPEVTNSV
FT                                LHEVNSWVSHRIAAAGAGCPP -> AVMLSAALQSALVIFV
FT                                RLIWQIIFQGYPRGVCCGGRCHY (in isoform 2).
FT                                /FTId=VSP_010315.
FT   MUTAGEN     122    122       S->A: Abolishes activity.
FT   MUTAGEN     239    239       D->A: Abolishes activity.
FT   MUTAGEN     243    243       D->A: Slightly reduces activity.
FT   MUTAGEN     269    269       H->A: Abolishes activity.
FT   MUTAGEN     272    272       H->A: Reduces activity.
FT   MUTAGEN     284    284       H->A: Slightly reduces activity.
FT   MUTAGEN     292    292       H->A: Slightly reduces activity.
SQ   SEQUENCE   303 AA;  33388 MW;  CB753ECDE38EBEC1 CRC64;
     MPEASSPRRT PQNVPYQDLP HLVNADGQYL FCRYWKPSGT PKALIFVSHG AGEHCGRYDE
     LAHMLKGLDM LVFAHDHVGH GQSEGERMVV SDFQVFVRDV LQHVDTIQKD YPDVPIFLLG
     HSMGGAISIL VAAERPTYFS GMVLISPLVL ANPESASTLK VLAAKLLNFV LPNMTLGRID
     SSVLSRNKSE VDLYNSDPLV CRAGLKVCFG IQLLNAVARV ERAMPRLTLP FLLLQGSADR
     LCDSKGAYLL MESSRSQDKT LKMYEGAYHV LHRELPEVTN SVLHEVNSWV SHRIAAAGAG
     CPP
//
ID   SYT3_MOUSE              Reviewed;         587 AA.
AC   O35681; P97791; Q80WV1;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2003, sequence version 2.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Synaptotagmin-3;
DE   AltName: Full=Synaptotagmin III;
DE            Short=SytIII;
GN   Name=Syt3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RA   Kataoka M.;
RL   Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR;
RX   MEDLINE=20002669; PubMed=10531343; DOI=10.1074/jbc.274.44.31421;
RA   Fukuda M., Kanno E., Mikoshiba K.;
RT   "Conserved N-terminal cysteine motif is essential for homo- and
RT   heterodimer formation of synaptotagmins III, V, VI, and X.";
RL   J. Biol. Chem. 274:31421-31427(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in Ca(2+)-dependent exocytosis of
CC       secretory vesicles through Ca(2+) and phospholipid binding to the
CC       C2 domain or may serve as Ca(2+) sensors in the process of
CC       vesicular trafficking and exocytosis.
CC   -!- COFACTOR: Binds 3 calcium ions per subunit. The ions are bound to
CC       the C2 domains (By similarity).
CC   -!- SUBUNIT: Homodimer. Can also form heterodimers.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane; Single-pass membrane protein.
CC   -!- DOMAIN: The first C2 domain mediates Ca(2+)-dependent phospholipid
CC       binding.
CC   -!- SIMILARITY: Belongs to the synaptotagmin family.
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; D45858; BAA08292.1; -; mRNA.
DR   EMBL; AB000893; BAA19204.1; -; mRNA.
DR   EMBL; BC051969; AAH51969.1; -; mRNA.
DR   IPI; IPI00315620; -.
DR   RefSeq; NP_001107588.1; NM_001114116.1.
DR   RefSeq; NP_057872.3; NM_016663.3.
DR   UniGene; Mm.4824; -.
DR   ProteinModelPortal; O35681; -.
DR   SMR; O35681; 294-572.
DR   IntAct; O35681; 1.
DR   STRING; O35681; -.
DR   PhosphoSite; O35681; -.
DR   PRIDE; O35681; -.
DR   Ensembl; ENSMUST00000032980; ENSMUSP00000032980; ENSMUSG00000030731.
DR   Ensembl; ENSMUST00000118831; ENSMUSP00000112432; ENSMUSG00000030731.
DR   Ensembl; ENSMUST00000118962; ENSMUSP00000114070; ENSMUSG00000030731.
DR   Ensembl; ENSMUST00000120262; ENSMUSP00000112968; ENSMUSG00000030731.
DR   GeneID; 20981; -.
DR   KEGG; mmu:20981; -.
DR   UCSC; uc009gph.1; mouse.
DR   CTD; 20981; -.
DR   MGI; MGI:99665; Syt3.
DR   eggNOG; maNOG05389; -.
DR   HOGENOM; HBG716633; -.
DR   HOVERGEN; HBG005010; -.
DR   InParanoid; O35681; -.
DR   OrthoDB; EOG4SQWWQ; -.
DR   NextBio; 299972; -.
DR   ArrayExpress; O35681; -.
DR   Bgee; O35681; -.
DR   CleanEx; MM_SYT3; -.
DR   Genevestigator; O35681; -.
DR   GermOnline; ENSMUSG00000030731; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   InterPro; IPR001565; Synaptotagmin.
DR   Pfam; PF00168; C2; 2.
DR   PRINTS; PR00360; C2DOMAIN.
DR   PRINTS; PR00399; SYNAPTOTAGMN.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 2.
PE   2: Evidence at transcript level;
KW   Calcium; Cell junction; Cytoplasmic vesicle; Membrane; Metal-binding;
KW   Repeat; Synapse; Transmembrane; Transmembrane helix.
FT   CHAIN         1    587       Synaptotagmin-3.
FT                                /FTId=PRO_0000183946.
FT   TOPO_DOM      1     54       Vesicular (Potential).
FT   TRANSMEM     55     75       Helical; (Potential).
FT   TOPO_DOM     76    587       Cytoplasmic (Potential).
FT   DOMAIN      298    399       C2 1.
FT   DOMAIN      430    533       C2 2.
FT   METAL       327    327       Calcium 1 (By similarity).
FT   METAL       327    327       Calcium 2 (By similarity).
FT   METAL       333    333       Calcium 1 (By similarity).
FT   METAL       385    385       Calcium 1 (By similarity).
FT   METAL       385    385       Calcium 2 (By similarity).
FT   METAL       386    386       Calcium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       387    387       Calcium 1 (By similarity).
FT   METAL       387    387       Calcium 2 (By similarity).
FT   METAL       387    387       Calcium 3 (By similarity).
FT   METAL       390    390       Calcium 3 (By similarity).
FT   METAL       393    393       Calcium 2 (By similarity).
FT   METAL       393    393       Calcium 3 (By similarity).
FT   CONFLICT    111    111       V -> L (in Ref. 1; BAA08292).
FT   CONFLICT    232    232       P -> A (in Ref. 1; BAA08292).
FT   CONFLICT    312    312       H -> Q (in Ref. 1; BAA08292/BAA19204).
SQ   SEQUENCE   587 AA;  63254 MW;  87EAEAADF22D5A4C CRC64;
     MSGDYEDDLC RRALILVSDL CARVRDADTN DRCQEFNELR IRGYPRGPDA DISVSLLSVI
     VTFCGIVLLG VSLFVSWKLC WVPWRDKGGS AVGGGPLRKD LAPGVGLAGL VGGGGHHLGA
     SLGGHPLLGG PHHHGHTAHH PPFAELLEPG GLGGSEPPEP SYLDMDSYPE AAVASVVAAG
     VKPSQTSPEL PSEGGTGSGL LLLPPSGGGL PSAQSHQQVT SLAPTTRYPA LPRPLTQQTL
     TTQADPSTEE RPPALPLPLP GGEEKAKLIG QIKPELYQGT GPGGRRGGGS GEAGAPCGRI
     SFALRYLYGS DHLVVRILQA LDLPAKDSNG FSDPYVKIYL LPDRKKKFQT KVHRKTLNPI
     FNETFQFSVP LAELAQRKLH FSVYDFDRFS RHDLIGQVVL DNLLELAEQP PDRPLWRDIL
     EGGSEKADLG ELNFSLCYLP TAGRLTVTII KASNLKAMDL TGFSDPYVKA SLISEGRRLK
     KRKTSIKKNT LNPTYNEALV FDVAPESVEN VGLSIAVVDY DCIGHNEVIG VCRVGPEAAD
     PHGREHWAEM LANPRKPVEH WHQLVEEKTL SSFTKGGKGL SEKENSE
//
ID   MYADM_MOUSE             Reviewed;         320 AA.
AC   O35682; Q8BGS9; Q8BPS8;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Myeloid-associated differentiation marker;
DE   AltName: Full=Myeloid up-regulated protein;
GN   Name=Myadm; Synonyms=Mug;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20195242; PubMed=10733104;
RA   Pettersson M., Nilsson K., Jonsson J.I.;
RT   "Isolation of MYADM, a novel hematopoietic-associated marker gene
RT   expressed in multipotent progenitor cells and up-regulated during
RT   myeloid differentiation.";
RL   J. Leukoc. Biol. 67:423-431(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Dendritic cell, Embryonic heart, Eye, Macrophage, and
RC   Osteoclast;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Probable).
CC   -!- SIMILARITY: Belongs to the MAL family.
CC   -!- SIMILARITY: Contains 2 MARVEL domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA04870.1; Type=Frameshift; Positions=238;
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AJ001616; CAA04870.1; ALT_FRAME; mRNA.
DR   EMBL; AK052258; BAC34900.1; -; mRNA.
DR   EMBL; AK053414; BAC35377.1; -; mRNA.
DR   EMBL; AK089538; BAC40918.1; -; mRNA.
DR   EMBL; AK149962; BAE29196.1; -; mRNA.
DR   EMBL; AK159160; BAE34863.1; -; mRNA.
DR   IPI; IPI00132938; -.
DR   RefSeq; NP_001087233.1; NM_001093764.1.
DR   RefSeq; NP_001087234.1; NM_001093765.1.
DR   RefSeq; NP_001087235.1; NM_001093766.1.
DR   RefSeq; NP_058665.2; NM_016969.2.
DR   UniGene; Mm.29874; -.
DR   STRING; O35682; -.
DR   PhosphoSite; O35682; -.
DR   PRIDE; O35682; -.
DR   Ensembl; ENSMUST00000096744; ENSMUSP00000094505; ENSMUSG00000068566.
DR   GeneID; 50918; -.
DR   KEGG; mmu:50918; -.
DR   UCSC; uc009eup.1; mouse.
DR   CTD; 50918; -.
DR   MGI; MGI:1355332; Myadm.
DR   eggNOG; roNOG10999; -.
DR   HOGENOM; HBG444560; -.
DR   HOVERGEN; HBG052545; -.
DR   InParanoid; O35682; -.
DR   OMA; TIVGSPR; -.
DR   OrthoDB; EOG41G34V; -.
DR   NextBio; 307923; -.
DR   ArrayExpress; O35682; -.
DR   Bgee; O35682; -.
DR   CleanEx; MM_MYADM; -.
DR   Genevestigator; O35682; -.
DR   GermOnline; ENSMUSG00000068566; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR008253; Marvel.
DR   InterPro; IPR021128; MARVEL-like_dom.
DR   Pfam; PF01284; MARVEL; 2.
DR   PROSITE; PS51225; MARVEL; 2.
PE   2: Evidence at transcript level;
KW   Membrane; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN         1    320       Myeloid-associated differentiation
FT                                marker.
FT                                /FTId=PRO_0000156817.
FT   TRANSMEM     35     55       Helical; (Potential).
FT   TRANSMEM     61     81       Helical; (Potential).
FT   TRANSMEM     95    115       Helical; (Potential).
FT   TRANSMEM    131    151       Helical; (Potential).
FT   TRANSMEM    165    185       Helical; (Potential).
FT   TRANSMEM    197    217       Helical; (Potential).
FT   TRANSMEM    233    253       Helical; (Potential).
FT   TRANSMEM    292    312       Helical; (Potential).
FT   DOMAIN       25    157       MARVEL 1.
FT   DOMAIN      162    317       MARVEL 2.
FT   CONFLICT    186    186       S -> G (in Ref. 1; CAA04870).
SQ   SEQUENCE   320 AA;  35285 MW;  7404E588226E756E CRC64;
     MPVTVTRTTI TTTTSSSTTV GSARALTQPL GLLRLLQLIS TCVAFSLVAS VGAWTGPMGN
     WAMFTWCFCF AVTLIILIVE LGGLQAHFPL SWRNFPITFA CYAALFCLSS SIIYPTTYVQ
     FLAHGRTRDH AIAATTFSCV ACLAYATEVA WTRARPGEIT GYMATVPGLL KVFETFVACI
     IFAFISEPLL YNQKPALEWC VAVYAICFIL AGVTILLNLG DCTNVLPIPF PTFLSGLALL
     SVLFYATAIV LWPLYQFDQR YQGQPRRSMD PSCTRSISYI QPNTVCFWDR RLAVSILTGI
     NLLAYVSDLV YSTRLVFVKV
//
ID   PININ_MOUSE             Reviewed;         725 AA.
AC   O35691; Q8CD89; Q8CGU3;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Pinin;
GN   Name=Pnn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RX   MEDLINE=97473502; PubMed=9332356; DOI=10.1016/S0378-1119(97)00249-7;
RA   Ouyang P., Zhen Y.Y., Sugrue S.P.;
RT   "Cloning and analysis of cDNA encoding murine pinin.";
RL   Gene 197:115-120(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RA   Leu S., Ouyang P.;
RT   "Mouse pinin gene.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440 AND SER-442, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-100 AND SER-346,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-100; SER-380 AND
RP   SER-679, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-100 AND SER-380,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Transcriptional activator binding to the E-box 1 core
CC       sequence of the E-cadherin promoter gene; the core-binding
CC       sequence is 5'CAGGTG-3'. Capable of reversing CTBP1-mediated
CC       transcription repression. Component of a splicing-dependent
CC       multiprotein exon junction complex (EJC) deposited at splice
CC       junction on mRNAs. The EJC is a dynamic structure consisting of a
CC       few core proteins and several more peripheral nuclear and
CC       cytoplasmic associated factors that join the complex only
CC       transiently either during EJC assembly or during subsequent mRNA
CC       metabolism. Participates in the regulation of alternative pre-mRNA
CC       splicing. Associates to spliced mRNA within 60 nt upstream of the
CC       5'-splice sites. Involved in the establishment and maintenance of
CC       epithelia cell-cell adhesion (By similarity).
CC   -!- SUBUNIT: Found in a mRNA splicing-dependent exon junction complex
CC       (EJC), at least composed of ACIN1, CASC3, EIF4A3, MAGOH, PNN,
CC       RBM8A, RNPS1, SAP18 and THOC4. Found in a complex with SR
CC       proteins. Found in a mRNP complex with RNPS1. Interacts with
CC       C6orf111/SRRP130, CTBP1, CTBP2, KRT8, KRT18, KRT19, PS1D/PNO40,
CC       PPIG, RNPS1, SFRS4 and SRRM2. Identified in the spliceosome C
CC       complex, at least composed of AQR, ASCC3L1, C19orf29, CDC40,
CC       CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38,
CC       DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC,
CC       HNRPF, HNRPH1, HNRPK, HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604,
CC       LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3,
CC       PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX,
CC       SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2,
CC       SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF,
CC       SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1,
CC       WDR57, XAB2 and ZCCHC8 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle (By similarity). Cell
CC       junction, desmosome (By similarity). Note=Cell-cell contact area,
CC       predominantly desmosome of intercellular adherens junction. Not a
CC       nucleocytoplasmic shuttling protein (By similarity).
CC   -!- SIMILARITY: Belongs to the pinin family.
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DR   EMBL; Y08701; CAA69960.1; -; mRNA.
DR   EMBL; AY129403; AAN05017.1; -; Genomic_DNA.
DR   EMBL; AK030978; BAC27200.1; -; mRNA.
DR   IPI; IPI00317891; -.
DR   RefSeq; NP_032917.2; NM_008891.2.
DR   UniGene; Mm.22347; -.
DR   STRING; O35691; -.
DR   PhosphoSite; O35691; -.
DR   PRIDE; O35691; -.
DR   Ensembl; ENSMUST00000021381; ENSMUSP00000021381; ENSMUSG00000020994.
DR   GeneID; 18949; -.
DR   KEGG; mmu:18949; -.
DR   CTD; 18949; -.
DR   MGI; MGI:1100514; Pnn.
DR   eggNOG; roNOG15595; -.
DR   HOVERGEN; HBG053104; -.
DR   InParanoid; O35691; -.
DR   OrthoDB; EOG4K0QNP; -.
DR   NextBio; 295292; -.
DR   ArrayExpress; O35691; -.
DR   Bgee; O35691; -.
DR   CleanEx; MM_PNN; -.
DR   Genevestigator; O35691; -.
DR   GermOnline; ENSMUSG00000020994; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IDA:MGI.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR006786; Pinin_SDK_MemA.
DR   InterPro; IPR006787; Pinin_SDK_N.
DR   Pfam; PF04696; Pinin_SDK_memA; 1.
DR   Pfam; PF04697; Pinin_SDK_N; 1.
DR   ProDom; PD011048; Pinin_SDK_N; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Cell junction; Coiled coil; DNA-binding;
KW   mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Spliceosome;
KW   Transcription; Transcription regulation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    725       Pinin.
FT                                /FTId=PRO_0000190243.
FT   COILED        2     32       Potential.
FT   COILED      162    233       Potential.
FT   COILED      286    373       Potential.
FT   COILED      444    467       Potential.
FT   COMPBIAS    171    473       Glu-rich.
FT   COMPBIAS    468    522       Pro-rich.
FT   COMPBIAS    471    528       Gln-rich.
FT   COMPBIAS    579    712       Ser-rich.
FT   COMPBIAS    640    725       Arg-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      66     66       Phosphoserine.
FT   MOD_RES      96     96       Phosphoserine.
FT   MOD_RES     100    100       Phosphoserine.
FT   MOD_RES     114    114       Phosphoserine (By similarity).
FT   MOD_RES     237    237       N6-acetyllysine (By similarity).
FT   MOD_RES     346    346       Phosphoserine.
FT   MOD_RES     380    380       Phosphoserine.
FT   MOD_RES     440    440       Phosphoserine.
FT   MOD_RES     442    442       Phosphoserine.
FT   MOD_RES     657    657       Phosphoserine (By similarity).
FT   MOD_RES     666    666       Phosphoserine (By similarity).
FT   MOD_RES     671    671       Phosphoserine (By similarity).
FT   MOD_RES     674    674       Phosphoserine (By similarity).
FT   MOD_RES     675    675       Phosphoserine (By similarity).
FT   MOD_RES     679    679       Phosphoserine.
FT   MOD_RES     680    680       Phosphoserine (By similarity).
FT   MOD_RES     698    698       Phosphoserine (By similarity).
FT   MOD_RES     700    700       Phosphoserine (By similarity).
FT   MOD_RES     703    703       Phosphoserine (By similarity).
FT   CONFLICT     31     31       G -> A (in Ref. 2; AAN05017).
FT   CONFLICT     42     43       AR -> GT (in Ref. 1; CAA69960).
FT   CONFLICT    125    125       R -> RR (in Ref. 3; BAC27200).
FT   CONFLICT    216    217       QL -> HV (in Ref. 2; AAN05017).
FT   CONFLICT    287    287       Q -> P (in Ref. 1; CAA69960).
FT   CONFLICT    327    327       D -> H (in Ref. 2; AAN05017).
FT   CONFLICT    365    365       T -> I (in Ref. 1; CAA69960).
FT   CONFLICT    658    658       M -> V (in Ref. 3; BAC27200).
FT   CONFLICT    683    683       R -> T (in Ref. 3; BAC27200).
SQ   SEQUENCE   725 AA;  82436 MW;  DB99FF2DB17AAF5E CRC64;
     MAVAVRALQE QLEKAKESLK NVDENIRKLT GRDPNDVRPI QARLLALSGP GGGRGRGSLL
     LRRGFSDSGG GPPAKQRDLE GAVSRLGGER RTRRESRQES DPEDDDVKKP ALQSSVVATS
     KERTRDLIQD QNMDEKGKQR NRRIFGLLMG TLQKFKQEST VATERQKRRQ EIEQKLEVQA
     EEERKQVENE RRELFEERRA KQTELRLLEQ KVELAQLQEE WNEHNAKIIK YIRTKTKPHL
     FYIPGRMCPA TQKLIEESQR KMNALFEGRR IEFAEQINKM EARPRRQSMK EKEHQVVRNE
     EQKAEQEEGK VAQREEELEE TGNQHNDVEV EEAGEEEEKE AGIVHSDAEK EQEEEEQKQE
     MEVKTEEEAE VREGEKQQDS QPEEVMDVLE MVESVKHVIA EQEVMETNQV ESIEPSENET
     SKELEPEMEF DVEPDKECKS LSPGKENINS QEVEKESEEK EEKEEKEPEP QPEPVAQPQP
     PPQPLPQSQP HSQPHSQPQP VLQSQPLCQP ETLPLAVLQP PPQVIQEQGN LLPERKDFPL
     ESIKLPEVSV EPVLTVHSEN KSKNKTRSRS RGRARNKTSK SRSRSSSSSS SSSSSTSSSS
     GSSSSSGSSS SRSSSSSSSS TSGSSSRDSS SSTSSSSESR SRSRGRGHNR DRKHRRSMDR
     KRRDTSGLER SHKSSKGGSS RDRKGSKDKS SRPDRKRSIS ESSRSGKRSS RSERDRKSDR
     KDKRR
//
ID   ENC1_MOUSE              Reviewed;         589 AA.
AC   O35709;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Ectoderm-neural cortex protein 1;
DE            Short=ENC-1;
GN   Name=Enc1; Synonyms=Enc-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss albino; TISSUE=Brain;
RX   MEDLINE=97252647; PubMed=9096139;
RA   Hernandez M.-C., Andres-Barquin P.J., Martinez S., Bulfone A.,
RA   Rubenstein J.L.R., Israel M.A.;
RT   "ENC-1: a novel mammalian kelch-related gene specifically expressed in
RT   the nervous system encodes an actin-binding protein.";
RL   J. Neurosci. 17:3038-3051(1997).
CC   -!- FUNCTION: Actin-binding protein involved in the regulation of
CC       neuronal process formation and in differentiation of neural crest
CC       cells. Probable substrate-specific adapter of an E3 ubiquitin-
CC       protein ligase complex which mediates the ubiquitination and
CC       subsequent proteasomal degradation of target proteins (By
CC       similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Part of a complex that contains CUL3, RBX1 and ENC1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
CC       Note=Interacts with the actin cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Primarily expressed in the nervous system.
CC   -!- DEVELOPMENTAL STAGE: Expression is highly dynamic but mostly
CC       restricted to the nervous system. Outside the nervous system,
CC       expression is detected in the rostral-most somitomere of the
CC       presomitic mesoderm, at the times corresponding to the
CC       epithelialization that precedes somite formation. First detected
CC       in the brain and spinal chord of 12 PC embryos.
CC   -!- PTM: Ubiquitinated and probably targeted for proteasome-
CC       independent degradation.
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC   -!- SIMILARITY: Contains 6 Kelch repeats.
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DR   EMBL; U65079; AAB64206.1; -; mRNA.
DR   IPI; IPI00331234; -.
DR   UniGene; Mm.241073; -.
DR   UniGene; Mm.481214; -.
DR   ProteinModelPortal; O35709; -.
DR   SMR; O35709; 18-275, 294-584.
DR   STRING; O35709; -.
DR   PhosphoSite; O35709; -.
DR   PRIDE; O35709; -.
DR   Ensembl; ENSMUST00000041623; ENSMUSP00000038783; ENSMUSG00000041773.
DR   MGI; MGI:109610; Enc1.
DR   eggNOG; roNOG12338; -.
DR   HOGENOM; HBG445733; -.
DR   HOVERGEN; HBG000905; -.
DR   InParanoid; O35709; -.
DR   OrthoDB; EOG4DJJW1; -.
DR   ArrayExpress; O35709; -.
DR   Bgee; O35709; -.
DR   CleanEx; MM_ENC1; -.
DR   Genevestigator; O35709; -.
DR   GermOnline; ENSMUSG00000041773; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   InterPro; IPR011705; BACK.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR013069; BTB_POZ.
DR   InterPro; IPR017096; Kelch-like_gigaxonin.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Gene3D; G3DSA:2.120.10.80; Kelch-typ_b-propeller; 1.
DR   Pfam; PF07707; BACK; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF01344; Kelch_1; 4.
DR   PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
DR   SMART; SM00875; BACK; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00612; Kelch; 6.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Cytoplasm; Cytoskeleton; Developmental protein;
KW   Kelch repeat; Phosphoprotein; Repeat; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   CHAIN         1    589       Ectoderm-neural cortex protein 1.
FT                                /FTId=PRO_0000119069.
FT   DOMAIN       46    114       BTB.
FT   REPEAT      296    340       Kelch 1.
FT   REPEAT      341    388       Kelch 2.
FT   REPEAT      389    444       Kelch 3.
FT   REPEAT      446    492       Kelch 4.
FT   REPEAT      494    538       Kelch 5.
FT   REPEAT      539    585       Kelch 6.
FT   MOD_RES     435    435       Phosphoserine (By similarity).
FT   MOD_RES     441    441       Phosphoserine (By similarity).
SQ   SEQUENCE   589 AA;  66086 MW;  12E62354D508B6A2 CRC64;
     MSVSVHENRK SRASSGSINI YLFHKSSYAD SVLTHLNLLR QQRLFTDVLL HAGNRTFPCH
     RAVLAACSRY FEAMFSGGLK ESQDSEVNFD NSIHPEVLEL LLDYAYSSRV IINEENAESL
     LEAGDMLEFQ DIRDACAEFL EKNLHPTNCL GMLLLSDAHQ CTKLYELSWR MCLSNFQTIR
     KSEDFLQLPQ DMVVQLLSSE ELETEDERLV YESAMNWISY DLKKRYCYLP ELLQTVRLAL
     LPAIYLMENV AMEELITKQR KSKEIVEEAI RCKLKILQND GVVTSLCARP RKTGHALFLL
     GGQTFMCDKL YLVDQKAKEI IPKADIPSPR KEFSACAIGC KVYITGGRGS ENGVSKDVWV
     YDTLHEEWSK AAPMLVARFG HGSAELKHCL YVVGGHTAAT GCLPASPSVS LKQVEQYDPT
     TNKWTMVAPL REGVSNAAVV SAKLKLFAFG GTSVSHDKLP KVQCYDQCEN RWSVPATCPQ
     PWRYTAAAVL GNQIFIMGGD TEFSACSAYK FNSETYQWTK VGDVTAKRMS CHAVASGNKL
     YVVGGYFGIQ RCKTLDCYDP TLDVWNSITT VPYSLIPTAF VSTWKHLPS
//
ID   HNRH1_MOUSE             Reviewed;         449 AA.
AC   O35737;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Heterogeneous nuclear ribonucleoprotein H;
DE            Short=hnRNP H;
DE   Contains:
DE     RecName: Full=Heterogeneous nuclear ribonucleoprotein H, N-terminally processed;
GN   Name=Hnrnph1; Synonyms=Hnrph, Hnrph1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Neuroblastoma;
RA   Wolff A., Landon F., Portier M.M.;
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 99-114 AND 300-326, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: This protein is a component of the heterogeneous nuclear
CC       ribonucleoprotein (hnRNP) complexes which provide the substrate
CC       for the processing events that pre-mRNAs undergo before becoming
CC       functional, translatable mRNAs in the cytoplasm. Mediates pre-mRNA
CC       alternative splicing regulation. Inhibits, together with CUGBP1,
CC       insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast.
CC       Binds to the IR RNA. Binds poly(RG) (By similarity).
CC   -!- SUBUNIT: Part of a ternary complex containing FUBP2, PTBP1, PTBP2
CC       and HNRNPH1. Identified in the spliceosome C complex, at least
CC       composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23,
CC       DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1,
CC       GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRNPH1, HNRPK,
CC       HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1,
CC       PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B,
CC       PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2,
CC       SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2,
CC       SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2,
CC       SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8.
CC       Interacts with IGF2BP1. Interacts with CUGBP1; the interaction is
CC       RNA-dependent. Interacts with MBNL1; the interaction in RNA-
CC       independent (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm (By similarity).
CC   -!- DOMAIN: Each quasi-RRM repeat bound poly(RG), while only the N-
CC       terminal QRRM bound poly(RC) and poly(RU). None of the repeats
CC       bound detectable amounts of poly(RA).
CC   -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.
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DR   EMBL; Y14196; CAA74583.1; -; mRNA.
DR   EMBL; BC056224; AAH56224.1; -; mRNA.
DR   IPI; IPI00133916; -.
DR   RefSeq; NP_067485.1; NM_021510.2.
DR   UniGene; Mm.21740; -.
DR   ProteinModelPortal; O35737; -.
DR   SMR; O35737; 1-102, 105-193, 283-365.
DR   STRING; O35737; -.
DR   REPRODUCTION-2DPAGE; IPI00133916; -.
DR   REPRODUCTION-2DPAGE; O35737; -.
DR   PRIDE; O35737; -.
DR   Ensembl; ENSMUST00000069304; ENSMUSP00000070503; ENSMUSG00000007850.
DR   Ensembl; ENSMUST00000109142; ENSMUSP00000104770; ENSMUSG00000007850.
DR   GeneID; 59013; -.
DR   KEGG; mmu:59013; -.
DR   UCSC; uc007isj.1; mouse.
DR   CTD; 59013; -.
DR   MGI; MGI:1891925; Hnrnph1.
DR   eggNOG; roNOG06834; -.
DR   HOVERGEN; HBG055557; -.
DR   OrthoDB; EOG4CRM03; -.
DR   NextBio; 314564; -.
DR   ArrayExpress; O35737; -.
DR   Bgee; O35737; -.
DR   Genevestigator; O35737; -.
DR   GermOnline; ENSMUSG00000007850; Mus musculus.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR012996; Znf_CHHC.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 3.
DR   Pfam; PF00076; RRM_1; 3.
DR   Pfam; PF08080; zf-RNPHF; 1.
DR   SMART; SM00360; RRM; 3.
DR   PROSITE; PS50102; RRM; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Methylation; mRNA processing;
KW   mRNA splicing; Nucleus; Phosphoprotein; Repeat; Ribonucleoprotein;
KW   RNA-binding; Spliceosome.
FT   CHAIN         1    449       Heterogeneous nuclear ribonucleoprotein
FT                                H.
FT                                /FTId=PRO_0000367120.
FT   INIT_MET      1      1       Removed; alternate (By similarity).
FT   CHAIN         2    449       Heterogeneous nuclear ribonucleoprotein
FT                                H, N-terminally processed.
FT                                /FTId=PRO_0000081858.
FT   DOMAIN       11     90       RRM 1.
FT   DOMAIN      111    188       RRM 2.
FT   REPEAT      234    249       1-1.
FT   DOMAIN      289    364       RRM 3.
FT   REPEAT      354    372       2-1.
FT   REPEAT      374    392       2-2.
FT   REPEAT      418    433       1-2.
FT   REGION      234    433       2 X 16 AA Gly-rich approximate repeats.
FT   REGION      354    392       2 X 19 AA perfect repeats.
FT   MOD_RES       1      1       N-acetylmethionine; in Heterogeneous
FT                                nuclear ribonucleoprotein H; alternate
FT                                (By similarity).
FT   MOD_RES       2      2       N-acetylmethionine; in Heterogeneous
FT                                nuclear ribonucleoprotein H, N-terminally
FT                                processed (By similarity).
FT   MOD_RES      23     23       Phosphoserine (By similarity).
FT   MOD_RES      63     63       Phosphoserine (By similarity).
FT   MOD_RES     100    100       Phosphothreonine (By similarity).
FT   MOD_RES     104    104       Phosphoserine.
FT   MOD_RES     107    107       Phosphothreonine (By similarity).
FT   MOD_RES     217    217       Asymmetric dimethylarginine (By
FT                                similarity).
FT   MOD_RES     233    233       Dimethylated arginine; alternate (By
FT                                similarity).
FT   MOD_RES     233    233       Omega-N-methylarginine; alternate (By
FT                                similarity).
FT   MOD_RES     246    246       Phosphotyrosine (By similarity).
FT   MOD_RES     306    306       Phosphotyrosine (By similarity).
FT   MOD_RES     310    310       Phosphoserine (By similarity).
SQ   SEQUENCE   449 AA;  49199 MW;  BF6138CA982D5484 CRC64;
     MMLGAEGGEG FVVKVRGLPW SCSADEVQRF FSDCKIQNGA QGIRFIYTRE GRPSGEAFVE
     LESEDEVKLA LKKDRETMGH RYVEVFKSNN VEMDWVLKHT GPNSPDTAND GFVRLRGLPF
     GCSKEEIVQF FSGLEIVPNG ITLPVDFQGR STGEAFVQFA SQEIAEKALK KHKERIGHRY
     IEIFKSSRAE VRTHYDPPRK LMAMQRPGPY DRPGAGRGYN SIGRGAGFER MRRGAYGGGY
     GGYDDYNGYN DGYGFGSDRF GRDLNYCFSG MSDHRYGDGG STFQSTTGHC VHMRGLPYRA
     TENDIYNFFS PLNPVRVHIE IGPDGRVTGE ADVEFATHED AVAAMSKDKA NMQHRYVELF
     LNSTAGASGG AYEHRYVELF LNSTAGASGG AYGSQMMGGM GLSNQSSYGG PASQQLSGGY
     GGGYGGQSSM SGYDQVLQEN SSDFQSNIA
//
ID   CD5R2_MOUSE             Reviewed;         369 AA.
AC   O35926; O35277;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Cyclin-dependent kinase 5 activator 2;
DE            Short=CDK5 activator 2;
DE   AltName: Full=Cyclin-dependent kinase 5 regulatory subunit 2;
DE   AltName: Full=p39;
DE   AltName: Full=p39I;
DE   Flags: Precursor;
GN   Name=Cdk5r2; Synonyms=Nck5ai;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=98322126; PubMed=9655938;
RA   Nilden F., Baeckstroem A., Bark C.;
RT   "Molecular cloning and characterisation of a mouse gene encoding an
RT   isoform of the neuronal cyclin-dependent kinase 5 (CDK5) activator.";
RL   Biochim. Biophys. Acta 1398:371-376(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RA   Zheng M., Leung C.L., Liem R.K.H.;
RT   "Comparative analysis of gene expression of the cyclin-dependent
RT   kinase 5 (cdk5) activators p35 and p39 in the rat CNS and embryonic
RT   development revealed distinctive overlap with cdk5.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Activator of CDK5/TPKII.
CC   -!- SUBUNIT: Heterodimer of a catalytic subunit and a regulatory
CC       subunit.
CC   -!- SIMILARITY: Belongs to the cyclin-dependent kinase 5 activator
CC       family.
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CC   -----------------------------------------------------------------------
DR   EMBL; U90267; AAC53595.1; -; Genomic_DNA.
DR   EMBL; AF016393; AAB69709.1; -; Genomic_DNA.
DR   IPI; IPI00136133; -.
DR   UniGene; Mm.153833; -.
DR   UniGene; Mm.434459; -.
DR   ProteinModelPortal; O35926; -.
DR   SMR; O35926; 180-328.
DR   MINT; MINT-246909; -.
DR   PRIDE; O35926; -.
DR   Ensembl; ENSMUST00000160379; ENSMUSP00000125322; ENSMUSG00000090071.
DR   MGI; MGI:1330828; Cdk5r2.
DR   HOVERGEN; HBG050853; -.
DR   Bgee; O35926; -.
DR   Genevestigator; O35926; -.
DR   GO; GO:0016533; C:cyclin-dependent protein kinase 5 holoenzyme complex; IEA:InterPro.
DR   GO; GO:0016534; F:cyclin-dependent protein kinase 5 activator activity; TAS:MGI.
DR   GO; GO:0008092; F:cytoskeletal protein binding; TAS:MGI.
DR   InterPro; IPR004944; CDK5_activator.
DR   InterPro; IPR011028; Cyclin-like.
DR   InterPro; IPR013763; Cyclin-related.
DR   Gene3D; G3DSA:1.10.472.10; Cyclin_related; 1.
DR   PANTHER; PTHR23401; CDK5_activator; 1.
DR   Pfam; PF03261; CDK5_activator; 1.
DR   PIRSF; PIRSF009324; Cdk5_activator; 1.
DR   SUPFAM; SSF47954; Cyclin_like; 1.
PE   3: Inferred from homology;
FT   PROPEP        1      ?       Potential.
FT                                /FTId=PRO_0000004802.
FT   CHAIN         ?    369       Cyclin-dependent kinase 5 activator 2.
FT                                /FTId=PRO_0000004803.
FT   COMPBIAS     75     78       Poly-Lys.
FT   COMPBIAS    155    163       Poly-Pro.
FT   COMPBIAS    348    351       Poly-Ser.
FT   CONFLICT     91     91       G -> V (in Ref. 2; AAB69709).
FT   CONFLICT    172    172       S -> G (in Ref. 2; AAB69709).
FT   CONFLICT    191    191       R -> G (in Ref. 2; AAB69709).
FT   CONFLICT    197    197       S -> R (in Ref. 2; AAB69709).
FT   CONFLICT    220    220       L -> W (in Ref. 2; AAB69709).
FT   CONFLICT    248    248       S -> R (in Ref. 2; AAB69709).
FT   CONFLICT    253    253       A -> G (in Ref. 2; AAB69709).
SQ   SEQUENCE   369 AA;  38915 MW;  DA4EB1FD4D48CE66 CRC64;
     MGTVLSLSPA SSAKGRRPGG LPEEKKKAPP AGDEALGGYG APPAGKGGKG ESRLKRPSVL
     ISALTWKRLV AASAKKKKGS KKVTPKPAST GPDPLVQQRN RENLLRKGRD GPDGGGTAKP
     LAVPVPTVPT TAATCEPPSG GSAAAPPPGS GGGKPPPPPP PAPQAAPPAP GSSPRRVIVQ
     ASTGELLRCL RDFVCRSCYR LKELSPGELV GWFRGVDRSL LLQGWQDQAF ITPANLVFVY
     LLCRESLSGD ELASAAELQA AFLTCLYLAY SYMGNEISYP LKPFLVEPDK ERFWQRCLRL
     IQRLSPQMLR LNADPHFFTQ VFQDLKNEGE AAASTGGPPS GSSASTTSSS SARDSCATGA
     KHWTMNLDR
//
ID   CTND2_MOUSE             Reviewed;        1247 AA.
AC   O35927; B2RR80;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 100.
DE   RecName: Full=Catenin delta-2;
DE   AltName: Full=Neural plakophilin-related ARM-repeat protein;
DE            Short=NPRAP;
DE   AltName: Full=Neurojungin;
GN   Name=Ctnnd2; Synonyms=Catnd2, Nprap;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING.
RC   TISSUE=Fetal brain;
RX   MEDLINE=98002299; PubMed=9342840;
RX   DOI=10.1046/j.1432-0436.1997.6150293.x;
RA   Paffenholz R., Franke W.W.;
RT   "Identification and localization of a neurally expressed member of the
RT   plakoglobin/armadillo multigene family.";
RL   Differentiation 61:293-304(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH E-CADHERIN.
RC   TISSUE=Brain;
RX   MEDLINE=99268158; PubMed=9971746; DOI=10.1083/jcb.144.3.519;
RA   Lu Q., Paredes M., Medina M., Zhou J., Cavallo R., Peifer M.,
RA   Orecchio L., Kosik K.S.;
RT   "Delta-catenin, an adhesive junction-associated protein which promotes
RT   cell scattering.";
RL   J. Cell Biol. 144:519-532(1999).
RN   [4]
RP   ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), AND INDUCTION.
RX   MEDLINE=20090270; PubMed=10626844; DOI=10.1016/S0304-3940(99)00875-7;
RA   Kawamura Y., Fan Q.W., Hayashi H., Michikawa M., Yanagisawa K.,
RA   Komano H.;
RT   "Expression of the mRNA for two isoforms of neural plakophilin-related
RT   arm-repeat protein/delta-catenin in rodent neurons and glial cells.";
RL   Neurosci. Lett. 277:185-188(1999).
RN   [5]
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   MEDLINE=20216926; PubMed=10753311;
RX   DOI=10.1002/(SICI)1096-9861(20000501)420:2<261::AID-CNE8>3.3.CO;2-H;
RA   Ho C., Zhou J., Medina M., Goto T., Jacobson M., Bhide P.G.,
RA   Kosik K.S.;
RT   "Delta-catenin is a nervous system-specific adherens junction protein
RT   which undergoes dynamic relocalization during development.";
RL   J. Comp. Neurol. 420:261-276(2000).
RN   [6]
RP   FUNCTION, INTERACTION WITH ZBTB33, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=15282317; DOI=10.1128/MCB.24.16.7188-7196.2004;
RA   Rodova M., Kelly K.F., VanSaun M., Daniel J.M., Werle M.J.;
RT   "Regulation of the rapsyn promoter by kaiso and delta-catenin.";
RL   Mol. Cell. Biol. 24:7188-7196(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412; SER-531 AND
RP   SER-534, AND MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452088; DOI=10.1074/mcp.T500040-MCP200;
RA   Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G.,
RA   Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F.,
RA   Maltby D.A., Schoepfer R., Burlingame A.L.;
RT   "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT   preparations using lectin weak affinity chromatography and mass
RT   spectrometry.";
RL   Mol. Cell. Proteomics 5:923-934(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412; SER-1094 AND
RP   SER-1098, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-513, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264; SER-273; SER-471
RP   AND SER-1149, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [13]
RP   INTERACTION WITH RGNEF.
RX   PubMed=17993462; DOI=10.1074/jbc.M707158200;
RA   Kim H., Han J.-R., Park J., Oh M., James S.E., Chang S., Lu Q.,
RA   Lee K.Y., Ki H., Song W.-J., Kim K.;
RT   "Delta-catenin-induced dendritic morphogenesis. An essential role of
RT   p190RhoGEF interaction through Akt1-mediated phosphorylation.";
RL   J. Biol. Chem. 283:977-987(2008).
CC   -!- FUNCTION: May be involved in neuronal cell adhesion and tissue
CC       morphogenesis and integrity by regulating adhesion molecules.
CC       Functions as a transcriptional activator when bound to ZBTB33.
CC   -!- SUBUNIT: Binds to E-cadherin at a juxtamembrane site within the
CC       cytoplasmic domain. Binds to PSEN1. Interacts with PDZD2.
CC       Interacts (via the extreme C-terminus) with FRMPD2 (via the PDZ 2
CC       domain) (By similarity). Interacts with ZBTB33. Interacts with
CC       RGNEF.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cell junction, adherens junction.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=NPRAPa;
CC         IsoId=O35927-1; Sequence=Displayed;
CC       Name=2; Synonyms=NPRAPb;
CC         IsoId=O35927-2; Sequence=VSP_006747;
CC   -!- TISSUE SPECIFICITY: Expressed in neurons and glial cells. Isoform
CC       2 was found to be the most predominant isoform in various brain
CC       regions. Expressed at neuromuscular junctions.
CC   -!- DEVELOPMENTAL STAGE: Increasingly expressed by embryonic day E10.
CC       Expression peaks at postnatal day P7 and stays at lower levels in
CC       adulthood. First expressed within proliferating neuronal
CC       progenitor cells of the neuroepithelium, becomes down-regulated
CC       during neuronal migration, and is later reexpressed in the
CC       dendritic compartment of postmitotic neurons. In the developing
CC       neocortex, it is strongly expressed in the proliferative
CC       ventricular zone and the developing cortical plate, yet is
CC       conspicuously less prominent in the intermediate zone, which
CC       contains migrating cortical neurons, it forms a honeycomb pattern
CC       in the neuroepithelium by labeling the cell periphery in a typical
CC       adherens junction pattern. By E18, its expression shifts primarily
CC       to nascent apical dendrites, a pattern that continues through
CC       adulthood.
CC   -!- INDUCTION: By retinoic acid.
CC   -!- PTM: O-glycosylated.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the beta-catenin family.
CC   -!- SIMILARITY: Contains 9 ARM repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U90331; AAB82409.1; -; mRNA.
DR   EMBL; BC138260; AAI38261.1; -; mRNA.
DR   EMBL; BC138261; AAI38262.1; -; mRNA.
DR   IPI; IPI00136135; -.
DR   IPI; IPI00228632; -.
DR   PIR; T42209; T42209.
DR   RefSeq; NP_032755.2; NM_008729.2.
DR   UniGene; Mm.321648; -.
DR   ProteinModelPortal; O35927; -.
DR   SMR; O35927; 539-1060.
DR   STRING; O35927; -.
DR   PhosphoSite; O35927; -.
DR   PRIDE; O35927; -.
DR   Ensembl; ENSMUST00000081728; ENSMUSP00000080427; ENSMUSG00000022240.
DR   Ensembl; ENSMUST00000110414; ENSMUSP00000106044; ENSMUSG00000022240.
DR   GeneID; 18163; -.
DR   KEGG; mmu:18163; -.
DR   UCSC; uc007vjz.1; mouse.
DR   CTD; 18163; -.
DR   MGI; MGI:1195966; Ctnnd2.
DR   eggNOG; roNOG13058; -.
DR   HOVERGEN; HBG004284; -.
DR   OrthoDB; EOG4S4PFC; -.
DR   NextBio; 293442; -.
DR   ArrayExpress; O35927; -.
DR   Bgee; O35927; -.
DR   CleanEx; MM_CTNND2; -.
DR   Genevestigator; O35927; -.
DR   GermOnline; ENSMUSG00000022240; Mus musculus.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007612; P:learning; IMP:MGI.
DR   GO; GO:0001763; P:morphogenesis of a branching structure; IDA:MGI.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 2.
DR   Pfam; PF00514; Arm; 4.
DR   SMART; SM00185; ARM; 7.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Cell junction; Coiled coil;
KW   Developmental protein; Glycoprotein; Nucleus; Phosphoprotein; Repeat;
KW   Transcription; Transcription regulation.
FT   CHAIN         1   1247       Catenin delta-2.
FT                                /FTId=PRO_0000064300.
FT   REPEAT      391    433       ARM 1.
FT   REPEAT      537    576       ARM 2.
FT   REPEAT      579    618       ARM 3.
FT   REPEAT      623    663       ARM 4.
FT   REPEAT      679    721       ARM 5.
FT   REPEAT      725    770       ARM 6.
FT   REPEAT      832    872       ARM 7.
FT   REPEAT      904    943       ARM 8.
FT   REPEAT      997   1040       ARM 9.
FT   COILED       49     84       Potential.
FT   COMPBIAS    218    225       Poly-Pro.
FT   COMPBIAS    245    248       Poly-Ala.
FT   COMPBIAS    478    481       Poly-Ala.
FT   COMPBIAS    808    814       Poly-Lys.
FT   MOD_RES      32     32       Phosphoserine.
FT   MOD_RES     264    264       Phosphoserine.
FT   MOD_RES     273    273       Phosphoserine.
FT   MOD_RES     412    412       Phosphoserine.
FT   MOD_RES     471    471       Phosphoserine.
FT   MOD_RES     513    513       Phosphotyrosine.
FT   MOD_RES     531    531       Phosphoserine.
FT   MOD_RES     534    534       Phosphoserine.
FT   MOD_RES    1094   1094       Phosphoserine.
FT   MOD_RES    1098   1098       Phosphoserine.
FT   MOD_RES    1149   1149       Phosphoserine.
FT   VAR_SEQ     878    902       Missing (in isoform 2).
FT                                /FTId=VSP_006747.
SQ   SEQUENCE   1247 AA;  135000 MW;  D4A7A6B6A27D2919 CRC64;
     MFARKQSGAA PFGAMPVPDQ PPSASEKNSS LSPGLNTSNG DGSETETTSA ILASVKEQEL
     QFERLTRELE AERQIVASQL ERCKLGSETG SMSSISSAGE QFHWQTQDGQ KDIEDELTTG
     LELVDSCIRS LQESGILDPQ DYSTSERPSL LSQSALQLNS KPEGSFQYPA SYHSNQTLAL
     GDTAPSQLPA RSTQARAAGQ SFSQGTTGRA GHLAGSEPAP PPPPPREPFA PSLGSAFHLP
     DAPPAAAALY YSSSTLPAPP RGGSPLTTTQ GGSPTKLQRG GSAPEGAAYA APRGSSPKQS
     PSRLAKSYST SSPINIVVSS AGLSPIRVTS PPTVQSTISS SPIHQLSSTI GTYATLSPTK
     RLVHASEQYS KHSQELYATA TLQRPGSLAA GSRASYSSQH GHLAPELRAL QSPEHHIDPI
     YEDRVYQKPP MRSLSQSQGD PLPPAHTGTF RTSTAPSSPG VDSVPLQRTG SQHGPQNAAA
     ATFQRASYAA GPASNYADPY RQLQYCASVD SPYSKSGPAL PPEGTLARSP SIDSIQKDPR
     EFGWRDPELP EVIQMLQHQF PSVQSNAAAY LQHLCFGDNK IKAEIRRQGG IQLLVDLLDH
     RMTEVHRSAC GALRNLVYGK ANDDNKIALK NCGGIPALVR LLRKTTDLEI RELVTGVLWN
     LSSCDALKMP IIQDALAVLT NAVIIPHSGW ENSPLQDDRK IQLHSSQVLR NATGCLRNVS
     SAGEEARRRM RECDGLTDAL LYVIQSALGS SEIDSKTVEN CVCILRNLSY RLAAETSQGQ
     HMGTDELDGL LCGETNGKDT ESSGCWGKKK KKKKSQDQWD GVGPLPDCAE PPKGIQMLWH
     PSIVKPYLTL LSECSNPDTL EGAAGALQNL AAGSWKGWAE DVAGMAYALR SLPEGAPCLP
     QWSVYIRAAV RKEKGLPILV ELLRIDNDRV VCAVATALRN MALDVRNKEL IGKYAMRDLV
     HRLPGGNNSN NSGSKAMSDD TVTAVCCTLH EVITKNMENA KALRDAGGIE KLVGISKSKG
     DKHSPKVVKA ASQVLNSMWQ YRDLRSLYKK DGWSQYHFVA SSSTIERDRQ RPYSSSRTPS
     ISPVRVSPNN RSASAPASPR EMISLKERKT DYESAGNNAT YHGTKGEHTS RKDTMTAQNT
     GVSTLYRNSY GAPAEDIKQN QVSTQPVPQE PSRKDYETYQ PFPNSTRNYD ESFFEDQVHH
     RPPASEYTMH LGLKSTGNYV DFYSAARPYS ELNYETSHYP ASPDSWV
//
ID   PITM1_MOUSE             Reviewed;        1243 AA.
AC   O35954;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Membrane-associated phosphatidylinositol transfer protein 1;
DE   AltName: Full=Drosophila retinal degeneration B homolog 1;
DE            Short=RdgB1;
DE   AltName: Full=Mpt-1;
DE   AltName: Full=Phosphatidylinositol transfer protein, membrane-associated 1;
DE            Short=PITPnm 1;
DE   AltName: Full=Pyk2 N-terminal domain-interacting receptor 2;
DE            Short=NIR-2;
GN   Name=Pitpnm1; Synonyms=Dres9, Mpt1, Nir2, Pitpnm;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=97396134; PubMed=9245688; DOI=10.1006/bbrc.1997.7009;
RA   Aikawa Y., Hara H., Watanabe T.;
RT   "Molecular cloning and characterization of mammalian homologues of the
RT   Drosophila retinal degeneration B gene.";
RL   Biochem. Biophys. Res. Commun. 236:559-564(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Retina;
RX   MEDLINE=98343889; PubMed=9680295;
RA   Rubboli F., Bulfone A., Bogni S., Marchitiello A., Zollo M.,
RA   Borsani G., Ballabio A., Banfi S.;
RT   "A mammalian homologue of the Drosophila retinal degeneration B gene:
RT   implications for the evolution of phototransduction mechanisms.";
RL   Genes Funct. 1:205-213(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PIK4CA.
RX   PubMed=10400687; DOI=10.1074/jbc.274.29.20569;
RA   Aikawa Y., Kuraoka A., Kondo H., Kawabuchi M., Watanabe T.;
RT   "Involvement of PITPnm, a mammalian homologue of Drosophila rdgB, in
RT   phosphoinositide synthesis on Golgi membranes.";
RL   J. Biol. Chem. 274:20569-20577(1999).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Regulates RHOA activity, and plays a role in
CC       cytoskeleton remodeling. Necessary for normal completion of
CC       cytokinesis. Plays a role in maintaining normal diacylglycerol
CC       levels in the Golgi apparatus. Binds phosphatidyl inositol
CC       phosphates (in vitro). May catalyze the transfer of
CC       phosphatidylinositol and phosphatidylcholine between membranes (By
CC       similarity). Necessary for maintaining the normal structure of the
CC       endoplasmic reticulum and the Golgi apparatus. Required for
CC       protein export from the endoplasmic reticulum and the Golgi. Binds
CC       calcium ions (By similarity).
CC   -!- SUBUNIT: Interacts with PTK2B via its C-terminus. Interacts with
CC       RHOA. Has higher affinity for the inactive, GDP-bound form of
CC       RHOA. The CDK1-phosphorylated form interacts with PLK1. Interacts
CC       with VAPB and PIK4CA (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus,
CC       Golgi stack membrane; Peripheral membrane protein (By similarity).
CC       Endoplasmic reticulum membrane; Peripheral membrane protein (By
CC       similarity). Lipid droplet (By similarity). Cleavage furrow (By
CC       similarity). Midbody (By similarity). Note=Peripheral membrane
CC       protein associated with Golgi stacks in interphase cells. A minor
CC       proportion is associated with the endoplasmic reticulum.
CC       Associated with lipid droplets. Dissociates from the Golgi early
CC       on in mitosis and localizes to the cleavage furrow and midbody
CC       during cytokinesis (By similarity).
CC   -!- TISSUE SPECIFICITY: Detected at high levels in brain, and at lower
CC       levels in lung, kidney, spleen and liver (at protein level).
CC       Ubiquitous. Highly expressed in embryonic retina and the central
CC       nervous system.
CC   -!- DEVELOPMENTAL STAGE: Detected at low levels during fetal
CC       development up to day 15. Highly expressed at day 17.
CC   -!- PTM: Phosphorylated on multiple sites by CDK1 at the onset of
CC       mitosis. Phosphorylation facilitates dissociation from the Golgi
CC       complex and is required for interaction with PLK1 (By similarity).
CC   -!- PTM: Phosphorylated on threonine residues upon treatment with
CC       oleic acid (By similarity).
CC   -!- PTM: Phosphorylated on tyrosine residues by PTK2B (By similarity).
CC   -!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI
CC       transfer class IIA subfamily.
CC   -!- SIMILARITY: Contains 1 DDHD domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AF006467; AAB84393.1; -; mRNA.
DR   EMBL; Y08922; CAA70127.1; -; mRNA.
DR   EMBL; BC044893; AAH44893.1; -; mRNA.
DR   EMBL; BC048150; AAH48150.1; -; mRNA.
DR   IPI; IPI00136246; -.
DR   PIR; JC5615; JC5615.
DR   RefSeq; NP_001129550.1; NM_001136078.1.
DR   RefSeq; NP_032877.1; NM_008851.3.
DR   UniGene; Mm.1860; -.
DR   ProteinModelPortal; O35954; -.
DR   SMR; O35954; 1-256.
DR   STRING; O35954; -.
DR   PhosphoSite; O35954; -.
DR   PRIDE; O35954; -.
DR   Ensembl; ENSMUST00000049658; ENSMUSP00000054309; ENSMUSG00000024851.
DR   Ensembl; ENSMUST00000100022; ENSMUSP00000097599; ENSMUSG00000024851.
DR   GeneID; 18739; -.
DR   KEGG; mmu:18739; -.
DR   UCSC; uc008fyn.1; mouse.
DR   CTD; 18739; -.
DR   MGI; MGI:1197524; Pitpnm1.
DR   eggNOG; roNOG05053; -.
DR   GeneTree; ENSGT00550000074351; -.
DR   HOGENOM; HBG444305; -.
DR   HOVERGEN; HBG052733; -.
DR   InParanoid; O35954; -.
DR   OMA; GQQPNVF; -.
DR   OrthoDB; EOG49W2DK; -.
DR   NextBio; 294877; -.
DR   ArrayExpress; O35954; -.
DR   Bgee; O35954; -.
DR   CleanEx; MM_PITPNM1; -.
DR   Genevestigator; O35954; -.
DR   GermOnline; ENSMUSG00000024851; Mus musculus.
DR   GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005811; C:lipid particle; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR004177; DDHD.
DR   InterPro; IPR023214; HAD-like_dom.
DR   InterPro; IPR013209; LNS2.
DR   InterPro; IPR001666; PI_transfer.
DR   Gene3D; G3DSA:3.40.50.1000; HAD-like_dom; 1.
DR   PANTHER; PTHR10658; PI_transfer; 1.
DR   Pfam; PF02862; DDHD; 1.
DR   Pfam; PF02121; IP_trans; 1.
DR   Pfam; PF08235; LNS2; 1.
DR   PRINTS; PR00391; PITRANSFER.
DR   SMART; SM00775; LNS2; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   PROSITE; PS51043; DDHD; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cytoplasm; Endoplasmic reticulum; Golgi apparatus;
KW   Lipid droplet; Membrane; Metal-binding; Phosphoprotein;
KW   Protein transport; Transport.
FT   CHAIN         1   1243       Membrane-associated phosphatidylinositol
FT                                transfer protein 1.
FT                                /FTId=PRO_0000232739.
FT   DOMAIN      684    878       DDHD.
FT   COMPBIAS    310    319       Poly-Ser.
FT   MOD_RES     287    287       Phosphothreonine; by CDK1 (By
FT                                similarity).
FT   MOD_RES     300    300       Phosphoserine.
FT   MOD_RES     382    382       Phosphoserine; by CDK1 (By similarity).
FT   MOD_RES     593    593       Phosphoserine (By similarity).
FT   MOD_RES     600    600       Phosphoserine (By similarity).
FT   MOD_RES     621    621       Phosphoserine (By similarity).
FT   MOD_RES     895    895       Phosphoserine (By similarity).
SQ   SEQUENCE   1243 AA;  134940 MW;  98E247536527D83E CRC64;
     MLIKEYHILL PMSLDEYQVA QLYMIQKKSR EESSGEGSGV EILANRPYTD GPGGNGQYTH
     KVYHVGSHIP GWFRALLPKA ALQVEEESWN AYPYTRTRYT CPFVEKFSIE IETYYLPDGG
     QQPNVFNLSG AERRQRIVDT IDIVRDAVAP GEYKAEEDPR LYRSAKTGRG PLADDWARTA
     AQTGPLMCAY KLCKVEFRYW GMQAKIEQFI HDVGLRRVML RAHRQAWCWQ DEWIELSMAD
     IRALEEETAR MLAQRMAKCN TGSEGPEAQT PGKSSTEARP GTSTAGTPDG PEAPPGPDAS
     PDASFGKQWS SSSRSSYSSQ HGGGVSPQSL SEWRMQNIAR DSENSSEEEF FDAHEGFSDS
     DEVFPKEMTK WNSNDFIDAF ASPTEVEGVP DPTVMATKGI EDGARAPRDS EGLDGAGDLV
     VEACSVHALF LILHSGSILD SGPGDTNSKQ ADVQTLSTAF EAVTRVHFPE ALGHVALRLV
     PCPPICAAAY ALVSNLSPYS HDGDSLSRSQ DHIPLAALPL LATSSSRYQG AVATVIARTN
     QAYAAFLRSS EGTGFCGQVV LIGDGVGGIL GFDALCHSAS AGPGSRGSSR RGSMNNEMLS
     PEVGPVRDPL ADGVEVLGRA SPEPSALPAQ RTFSDMANPD PDGSQNSLQV ASTATSSGEP
     RRASTASCPP ASSEAPDGPT NAARLDFKVS GFFLFGSPLG LVLALRKTVM PALEVAQLRP
     ACEQIYNLFH AADPCASRLE PLLAPKFQAI APLAVPRYQK FPLGDGSSLL LADTLQTHSS
     LFLEELEMMV PSTPTSASGA FWKGSELGNE PASQTAAPST TSEVVKILDR WWGNKRIDYS
     LYCPEALTAF PTVTLPHLFH ASYWESADVV AFILRQVIEK ERPQLTECEE PSIYSPAFPR
     EKWQRKRTQV KIRNVTSNHR ASDTVVCEGR PQVLNGRFMY GPLDVVTLTG EKVDVYVMTQ
     PLSGKWIHFG TEVTNSSGRL TFPVPSERAL GIGVYPVRMV VRGDHTYAEC CLTVVSRGTE
     AVVFSIDGSF TASVSIMGSD PKVRAGAVDV VRHWQDSGYL IVYVTGRPDM QKHRVVAWLS
     QHNFPHGVVS FCDGLTHDPL RQKAMFLQSL VQEVELNIVA GYGSPKDVAV YAALGLSPSQ
     TYIVGRAVRK LQAQCQFLSD GYVAHLGQLE AGSHSHAPSG PPRAALAKSS YAVAAPVDFL
     RKQSQLLRSR GPSQVDREGP GTPPTTLARG KTRSISLKLD SEE
//
ID   RM23_MOUSE              Reviewed;         146 AA.
AC   O35972; Q78E46;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=39S ribosomal protein L23, mitochondrial;
DE            Short=L23mt;
DE            Short=MRP-L23;
DE   AltName: Full=L23 mitochondrial-related protein;
GN   Name=Mrpl23; Synonyms=L23mrp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=129/SvJ; TISSUE=Liver;
RX   MEDLINE=98008916; PubMed=9344651; DOI=10.1006/geno.1997.4961;
RA   Zubair M., Hilton K., Saam J.R., Surani M.A., Tilghman S.M.,
RA   Sasaki H.;
RT   "Structure and expression of the mouse L23mrp gene downstream of the
RT   imprinted H19 gene: biallelic expression and lack of interaction with
RT   the H19 enhancers.";
RL   Genomics 45:290-296(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=21293042; PubMed=11279069; DOI=10.1074/jbc.M100826200;
RA   Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A.,
RA   Watanabe K.;
RT   "Structural compensation for the deficit of rRNA with proteins in the
RT   mammalian mitochondrial ribosome. Systematic analysis of protein
RT   components of the large ribosomal subunit from mammalian
RT   mitochondria.";
RL   J. Biol. Chem. 276:21724-21736(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 8-44.
RC   STRAIN=C57BL/6;
RX   MEDLINE=98051897; PubMed=9337391; DOI=10.1007/s003359900583;
RA   Greally J.M., Guinness M.E., McGrath J., Zemel S.;
RT   "Matrix-attachment regions in the mouse chromosome 7F imprinted
RT   domain.";
RL   Mamm. Genome 8:805-810(1997).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the ribosomal protein L23P family.
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DR   EMBL; U84902; AAC53392.1; -; mRNA.
DR   EMBL; U84903; AAC53393.1; -; Genomic_DNA.
DR   EMBL; AB049646; BAB40851.1; -; mRNA.
DR   EMBL; AK086805; BAC39746.1; -; mRNA.
DR   EMBL; BC081460; AAH81460.1; -; mRNA.
DR   EMBL; U71209; AAB70459.1; -; Genomic_DNA.
DR   IPI; IPI00136310; -.
DR   RefSeq; NP_035418.1; NM_011288.1.
DR   UniGene; Mm.12144; -.
DR   UniGene; Mm.314652; -.
DR   ProteinModelPortal; O35972; -.
DR   SMR; O35972; 36-107.
DR   PRIDE; O35972; -.
DR   Ensembl; ENSMUST00000038675; ENSMUSP00000039784; ENSMUSG00000037772.
DR   Ensembl; ENSMUST00000100003; ENSMUSP00000097583; ENSMUSG00000075279.
DR   GeneID; 19935; -.
DR   KEGG; mmu:19935; -.
DR   NMPDR; fig|10090.3.peg.17998; -.
DR   UCSC; uc009kny.1; mouse.
DR   CTD; 100040519; -.
DR   CTD; 19935; -.
DR   MGI; MGI:1196612; Mrpl23.
DR   eggNOG; maNOG19792; -.
DR   HOGENOM; HBG315840; -.
DR   HOVERGEN; HBG052914; -.
DR   InParanoid; O35972; -.
DR   OMA; GQTFTFP; -.
DR   OrthoDB; EOG4N5VZ3; -.
DR   NextBio; 449051; -.
DR   Bgee; O35972; -.
DR   CleanEx; MM_MRPL23; -.
DR   Genevestigator; O35972; -.
DR   GermOnline; ENSMUSG00000037772; Mus musculus.
DR   GermOnline; ENSMUSG00000075279; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR012678; Ribosomal_L23/L15e.
DR   InterPro; IPR013025; Ribosomal_L25/23.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF00276; Ribosomal_L23; 1.
DR   SUPFAM; SSF54189; L23_L15e_core; 1.
PE   2: Evidence at transcript level;
KW   Mitochondrion; Ribonucleoprotein; Ribosomal protein.
FT   CHAIN         1    146       39S ribosomal protein L23, mitochondrial.
FT                                /FTId=PRO_0000129485.
SQ   SEQUENCE   146 AA;  17122 MW;  0116ADE56C9B1553 CRC64;
     MARNVLYPLY QLGGPQLRVF RTNFFIQLVR PGTAQPEDTV QFRIPMEMTR VDLRNYLEQI
     YNVPVAAVRT RVQHGSNRRR DHKNVRIKKP DYKVAYVQLA HGQTFTFPDL FPEKDPRSPE
     PLEEELPQQR QSSDLRCPGI PSWFGL
//
ID   PTRF_MOUSE              Reviewed;         392 AA.
AC   O54724; Q2TAW6;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Polymerase I and transcript release factor;
DE   AltName: Full=Cav-p60;
DE   AltName: Full=Cavin-1;
GN   Name=Ptrf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBUNIT.
RX   MEDLINE=98250657; PubMed=9582279; DOI=10.1093/emboj/17.10.2855;
RA   Jansa P., Mason S.W., Hoffmann-Rohrer U., Grummt I.;
RT   "Cloning and functional characterization of PTRF, a novel protein
RT   which induces dissociation of paused ternary transcription
RT   complexes.";
RL   EMBO J. 17:2855-2864(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=129/SvJ;
RX   MEDLINE=21100887; PubMed=11161808; DOI=10.1006/geno.2000.6433;
RA   Miyoshi K., Cui Y., Riedlinger G., Robinson P., Lehoczky J., Zon L.,
RA   Oka T., Dewar K., Hennighausen L.;
RT   "Structure of the mouse Stat 3/5 locus: evolution from Drosophila to
RT   zebrafish to mouse.";
RL   Genomics 71:150-155(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH ZNF148.
RX   MEDLINE=20193424; PubMed=10727401; DOI=10.1042/0264-6021:3470055;
RA   Hasegawa T., Takeuchi A., Miyaishi O., Xiao H., Mao J., Isobe K.;
RT   "PTRF (polymerase I and transcript-release factor) is tissue-specific
RT   and interacts with the BFCOL1 (binding factor of a type-I collagen
RT   promoter) zinc-finger transcription factor which binds to the two
RT   mouse type-I collagen gene promoters.";
RL   Biochem. J. 347:55-59(2000).
RN   [6]
RP   FUNCTION, AND PHOSPHORYLATION.
RX   MEDLINE=20580735; PubMed=11139612; DOI=10.1093/nar/29.2.423;
RA   Jansa P., Burek C., Sander E.E., Grummt I.;
RT   "The transcript release factor PTRF augments ribosomal gene
RT   transcription by facilitating reinitiation of RNA polymerase I.";
RL   Nucleic Acids Res. 29:423-429(2001).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION,
RP   AND TISSUE SPECIFICITY.
RX   PubMed=18191225; DOI=10.1016/j.cell.2007.11.042;
RA   Hill M.M., Bastiani M., Luetterforst R., Kirkham M., Kirkham A.,
RA   Nixon S.J., Walser P., Abankwa D., Oorschot V.M., Martin S.,
RA   Hancock J.F., Parton R.G.;
RT   "PTRF-Cavin, a conserved cytoplasmic protein required for caveola
RT   formation and function.";
RL   Cell 132:113-124(2008).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18840361; DOI=10.1016/j.cmet.2008.07.008;
RA   Liu L., Brown D., McKee M., Lebrasseur N.K., Yang D., Albrecht K.H.,
RA   Ravid K., Pilch P.F.;
RT   "Deletion of Cavin/PTRF causes global loss of caveolae, dyslipidemia,
RT   and glucose intolerance.";
RL   Cell Metab. 8:310-317(2008).
RN   [9]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18056712; DOI=10.1074/jbc.M707890200;
RA   Liu L., Pilch P.F.;
RT   "A critical role of cavin (polymerase I and transcript release factor)
RT   in caveolae formation and organization.";
RL   J. Biol. Chem. 283:4314-4322(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; THR-40; SER-42;
RP   SER-169; SER-177; SER-302; SER-367 AND SER-368, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169 AND SER-302, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Plays an important role in caveolae formation and
CC       organization. Required for the sequestration of mobile caveolin
CC       into immobile caveolae. Termination of transcription by RNA
CC       polymerase I involves pausing of transcription by TTF1, and the
CC       dissociation of the transcription complex, releasing pre-rRNA and
CC       RNA polymerase I from the template. PTRF is required for
CC       dissociation of the ternary transcription complex.
CC   -!- SUBUNIT: Interacts with LIPE in the adipocyte cytoplasm (By
CC       similarity). Interacts with RNA polymerase I and TTF1. Binds the
CC       3' end of pre-rRNA. Interacts with transcription factor ZNF148.
CC   -!- INTERACTION:
CC       P49817:Cav1; NbExp=2; IntAct=EBI-645496, EBI-1161338;
CC   -!- SUBCELLULAR LOCATION: Membrane, caveola. Cell membrane. Microsome
CC       (By similarity). Endoplasmic reticulum (By similarity). Cytoplasm,
CC       cytosol (By similarity). Mitochondrion (By similarity). Nucleus
CC       (By similarity). Note=Found at the surface of the caveolae. Also
CC       found in the plasma membrane, microsomal and cytosolic fractions
CC       and at a low level in the mitochondrial and nuclear fractions (By
CC       similarity). Translocates to the cytoplasm from caveolae upon
CC       insulin stimulation (By similarity). CAV1 is necessary to recruit
CC       it to the cell membrane. Co-localizes with CAV1 in lipid rafts in
CC       adipocytes.
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues tested (lung, heart,
CC       testis, kidney, muscle, liver, spleen and brain). Highest levels
CC       in lung and heart.
CC   -!- PTM: Phosphorylated. Present in active and inactive forms. Changes
CC       in phosphorylation pattern may alter activity.
CC   -!- DISRUPTION PHENOTYPE: Mice show a metabolic phenotype of
CC       significantly reduced adipose tissue mass, higher circulating
CC       triglyceride levels, glucose intolerance, and hyperinsulinemia,
CC       consistent with a lipodystrophy. Cells from various tissues,
CC       including lung epithelium, intestinal smooth muscle, skeletal
CC       muscle, and endothelial cells showed no detectable caveolae cells.
CC   -!- SIMILARITY: Belongs to the PTRF/SDPR family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF036249; AAC53588.1; -; mRNA.
DR   EMBL; AF458959; AAL60240.1; -; Genomic_DNA.
DR   EMBL; AL591466; CAM19459.1; -; Genomic_DNA.
DR   EMBL; BC110698; AAI10699.1; -; mRNA.
DR   EMBL; BC117527; AAI17528.1; -; mRNA.
DR   EMBL; BC116701; AAI16702.1; -; mRNA.
DR   IPI; IPI00117689; -.
DR   RefSeq; NP_033012.1; NM_008986.2.
DR   UniGene; Mm.21864; -.
DR   ProteinModelPortal; O54724; -.
DR   IntAct; O54724; 12.
DR   STRING; O54724; -.
DR   PhosphoSite; O54724; -.
DR   PRIDE; O54724; -.
DR   Ensembl; ENSMUST00000060792; ENSMUSP00000058321; ENSMUSG00000004044.
DR   GeneID; 19285; -.
DR   KEGG; mmu:19285; -.
DR   UCSC; uc007lmr.1; mouse.
DR   CTD; 19285; -.
DR   MGI; MGI:1277968; Ptrf.
DR   eggNOG; roNOG12917; -.
DR   GeneTree; ENSGT00530000063058; -.
DR   HOGENOM; HBG715099; -.
DR   HOVERGEN; HBG056807; -.
DR   InParanoid; O54724; -.
DR   OMA; TRHNLEK; -.
DR   OrthoDB; EOG49W2G9; -.
DR   PhylomeDB; O54724; -.
DR   NextBio; 296206; -.
DR   ArrayExpress; O54724; -.
DR   Bgee; O54724; -.
DR   CleanEx; MM_PTRF; -.
DR   Genevestigator; O54724; -.
DR   GermOnline; ENSMUSG00000004044; Mus musculus.
DR   GO; GO:0005901; C:caveola; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005792; C:microsome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003716; F:RNA polymerase I transcription termination factor activity; IDA:UniProtKB.
DR   GO; GO:0042134; F:rRNA primary transcript binding; IDA:UniProtKB.
DR   GO; GO:0006361; P:transcription initiation from RNA polymerase I promoter; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Coiled coil; Cytoplasm;
KW   Endoplasmic reticulum; Membrane; Microsome; Mitochondrion; Nucleus;
KW   Phosphoprotein; RNA-binding; rRNA-binding; Transcription;
KW   Transcription regulation; Transcription termination.
FT   CHAIN         1    392       Polymerase I and transcript release
FT                                factor.
FT                                /FTId=PRO_0000097095.
FT   COILED      201    284       Potential.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      38     38       Phosphoserine.
FT   MOD_RES      40     40       Phosphothreonine.
FT   MOD_RES      42     42       Phosphoserine.
FT   MOD_RES     111    111       N6-acetyllysine (By similarity).
FT   MOD_RES     120    120       Phosphoserine (By similarity).
FT   MOD_RES     158    158       Phosphotyrosine (By similarity).
FT   MOD_RES     169    169       Phosphoserine.
FT   MOD_RES     177    177       Phosphoserine.
FT   MOD_RES     204    204       Phosphoserine (By similarity).
FT   MOD_RES     205    205       Phosphoserine (By similarity).
FT   MOD_RES     302    302       Phosphoserine.
FT   MOD_RES     304    304       Phosphothreonine (By similarity).
FT   MOD_RES     310    310       Phosphotyrosine (By similarity).
FT   MOD_RES     367    367       Phosphoserine.
FT   MOD_RES     368    368       Phosphoserine.
FT   MOD_RES     378    378       Phosphothreonine (By similarity).
FT   MOD_RES     381    381       Phosphoserine (By similarity).
FT   MOD_RES     389    389       Phosphoserine (By similarity).
FT   MOD_RES     391    391       Phosphoserine (By similarity).
SQ   SEQUENCE   392 AA;  43954 MW;  6871CBC06DCF5C35 CRC64;
     MEDVTLHIVE RPYSGFPDAS SEGPEPTQGE ARATEEPSGT GSDELIKSDQ VNGVLVLSLL
     DKIIGAVDQI QLTQAQLEER QAEMEGAVQS IQGELSKLGK AHATTSNTVS KLLEKVRKVS
     VNVKTVRGSL ERQAGQIKKL EVNEAELLRR RNFKVMIYQD EVKLPAKLSV SKSLKESEAL
     PEKEGDELGE GERPEDDTAA IELSSDEAVE VEEVIEESRA ERIKRSGLRR VDDFKKAFSK
     EKMEKTKVRT RENLEKTRLK TKENLEKTRH TLEKRMNKLG TRLVPVERRE KLKTSRDKLR
     KSFTPDHVVY ARSKTAVYKV PPFTFHVKKI REGEVEVLKA TEMVEVGPED DEVGAERGEA
     TDLLRGSSPD VHTLLEITEE SDAVLVDKSD SD
//
ID   AP3D1_MOUSE             Reviewed;        1199 AA.
AC   O54774;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=AP-3 complex subunit delta-1;
DE   AltName: Full=AP-3 complex subunit delta;
DE   AltName: Full=Adapter-related protein complex 3 subunit delta-1;
DE   AltName: Full=Delta-adaptin;
DE            Short=mBLVR1;
GN   Name=Ap3d1; Synonyms=Ap3d;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Spleen;
RX   MEDLINE=98080452; PubMed=9420263;
RA   Suzuki T., Ikeda H.;
RT   "The mouse homolog of the bovine leukemia virus receptor is closely
RT   related to the delta subunit of adaptor-related protein complex AP-3,
RT   not associated with the cell surface.";
RL   J. Virol. 72:593-599(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-760 AND SER-825, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-760 AND SER-784, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-755; THR-758; SER-760
RP   AND SER-784, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-760, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-754; THR-758; SER-760
RP   AND SER-784, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632; SER-634; SER-636;
RP   SER-760 AND SER-784, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-758 AND SER-760, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Part of the AP-3 complex, an adaptor-related complex
CC       which is not clathrin-associated. The complex is associated with
CC       the Golgi region as well as more peripheral structures. It
CC       facilitates the budding of vesicles from the Golgi membrane and
CC       may be directly involved in trafficking to lysosomes (By
CC       similarity).
CC   -!- SUBUNIT: Adaptor protein complex 3 (AP-3) is an heterotetramer
CC       composed of two large adaptins (delta-type subunit AP3D1 and beta-
CC       type subunit AP3B1 or AP3B2), a medium adaptin (mu-type subunit
CC       AP3M1 or AP3M2) and a small adaptin (sigma-type subunit APS1 or
CC       AP3S2) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus
CC       membrane; Peripheral membrane protein; Cytoplasmic side (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC   -!- SIMILARITY: Contains 9 HEAT repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB004305; BAA24578.1; -; mRNA.
DR   EMBL; BC048786; AAH48786.1; -; mRNA.
DR   EMBL; BC053066; AAH53066.1; -; mRNA.
DR   IPI; IPI00117811; -.
DR   PIR; T13946; T13946.
DR   RefSeq; NP_031486.1; NM_007460.1.
DR   UniGene; Mm.209294; -.
DR   ProteinModelPortal; O54774; -.
DR   SMR; O54774; 11-614.
DR   DIP; DIP-32163N; -.
DR   STRING; O54774; -.
DR   PhosphoSite; O54774; -.
DR   PRIDE; O54774; -.
DR   Ensembl; ENSMUST00000020420; ENSMUSP00000020420; ENSMUSG00000020198.
DR   GeneID; 11776; -.
DR   KEGG; mmu:11776; -.
DR   UCSC; uc007gek.1; mouse.
DR   CTD; 11776; -.
DR   MGI; MGI:107734; Ap3d1.
DR   eggNOG; roNOG07709; -.
DR   HOGENOM; HBG739063; -.
DR   HOVERGEN; HBG050520; -.
DR   InParanoid; O54774; -.
DR   OMA; ITTPCYS; -.
DR   OrthoDB; EOG45TCMD; -.
DR   PhylomeDB; O54774; -.
DR   NextBio; 279571; -.
DR   ArrayExpress; O54774; -.
DR   Bgee; O54774; -.
DR   Genevestigator; O54774; -.
DR   GermOnline; ENSMUSG00000020198; Mus musculus.
DR   GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030117; C:membrane coat; IEA:InterPro.
DR   GO; GO:0005802; C:trans-Golgi network; TAS:MGI.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR   GO; GO:0048007; P:antigen processing and presentation, exogenous lipid antigen via MHC class Ib; IMP:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; IMP:MGI.
DR   GO; GO:0051138; P:positive regulation of NK T cell differentiation; IMP:MGI.
DR   GO; GO:0061088; P:regulation of sequestering of zinc ion; TAS:BHF-UCL.
DR   GO; GO:0016192; P:vesicle-mediated transport; TAS:MGI.
DR   GO; GO:0006829; P:zinc ion transport; TAS:BHF-UCL.
DR   InterPro; IPR017105; AP3_complex_dsu.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR010474; BLV_receptor.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   Pfam; PF06375; BLVR; 1.
DR   PIRSF; PIRSF037092; AP3_complex_delta; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Golgi apparatus; Membrane; Phosphoprotein;
KW   Protein transport; Repeat; Transport.
FT   CHAIN         1   1199       AP-3 complex subunit delta-1.
FT                                /FTId=PRO_0000193767.
FT   REPEAT       34     71       HEAT 1.
FT   REPEAT      142    179       HEAT 2.
FT   REPEAT      180    216       HEAT 3.
FT   REPEAT      218    254       HEAT 4.
FT   REPEAT      257    296       HEAT 5.
FT   REPEAT      298    336       HEAT 6.
FT   REPEAT      337    373       HEAT 7.
FT   REPEAT      375    409       HEAT 8.
FT   REPEAT      521    558       HEAT 9.
FT   COILED      659    679       Potential.
FT   COILED      722    750       Potential.
FT   COILED      843    863       Potential.
FT   COILED      911    934       Potential.
FT   COMPBIAS    836    944       Lys-rich.
FT   COMPBIAS    956    960       Poly-Glu.
FT   MOD_RES     632    632       Phosphoserine.
FT   MOD_RES     634    634       Phosphoserine.
FT   MOD_RES     636    636       Phosphoserine.
FT   MOD_RES     686    686       Phosphoserine (By similarity).
FT   MOD_RES     688    688       Phosphoserine (By similarity).
FT   MOD_RES     721    721       Phosphoserine (By similarity).
FT   MOD_RES     754    754       Phosphoserine.
FT   MOD_RES     755    755       Phosphoserine.
FT   MOD_RES     758    758       Phosphothreonine.
FT   MOD_RES     760    760       Phosphoserine.
FT   MOD_RES     784    784       Phosphoserine.
FT   MOD_RES     825    825       Phosphoserine.
SQ   SEQUENCE   1199 AA;  135081 MW;  29D2D036B36C3B05 CRC64;
     MALKMVKGSI DRMFDKNLQD LVRGIRNHKE DEAKYISQCI DEIKQELKQD NIAVKANAVC
     KLTYLQMLGY DISWAAFNII EVMSASKFTF KRVGYLAASQ CFHEGTDVIM LTTNQIRKDL
     SSPSQYDTGV ALTGLSCFVT PDLARDLAND IMTLMSHTKP YIRKKAVLIM YKVFLKYPES
     LRPAFPRLKE KLEDPDPGVQ SAAVNVICEL ARRNPKNYLS LAPLFFKLMT SSTNNWVLIK
     IIKLFGALTP LEPRLGKKLI EPLTNLIHST SAMSLLYECV NTVIAVLISL SSGMPNHSAS
     IQLCVQKLRI LIEDSDQNLK YLGLLAMSKI LKTHPKSVQS HKDLILQCLD DKDESIRLRA
     LDLLYGMVSK KNLMEIVKKL MTHVDKAEGT TYRDELLTKI IDICSQSNYQ HITNFEWYIS
     ILVELTRLEG TRHGHLIAAQ MLDVAIRVKA IRKFAVSQMS SLLDSAHLVA SSTQRNGICE
     VLYAAAWICG EFSEHLQGPQ QTLEAMLRPK VTTLPGHIQA VYVQNVVKLY ASILQQKEQA
     ADTEAAQEVT QLLVERLPQF VQSADLEVQE RASCILQLVK HVQKLQAKGV PVAEEVSALF
     AGELNPVAPK AQKKVPVPEG LDLDAWINEP PSDSESEDEK PKAIFHEEEP RHTRRRQPEE
     DEEELARRRE ARKQEQANNP FYIKSSPSPQ KRYQDAPGVE HIPVVQIDLS VPLKVPGMPM
     SDQYVKLEEQ RRHRQRLEKD KKRKKKEKGK RRHSSLPTES DEDIAPAQRV DIITEEMPEN
     ALPSDEDDKD PNDPYRALDI DLDKPLADSE KLPVQKHRNA EAVKSPEKEG VLGVEKKSKK
     PKKKEKKTKE REREKKDKKG EDLDFWLSTT PPPAAAPIPA PSTEELAAST ITSPKDECEV
     LKGEEEDHVD HDQERKSSRH KKKKHRKEKE KEERPRDKKK AKKKQVAPLE NGAAAEEEEE
     PIPPMSSYCL LAESPYIKVT YDIQASLQKD SQVTVSIILE NQSSSFLKNM ELNVLDSLNT
     KMTRPEGSSV HDGVPVPFQL PPGVSNEAQF VFTIQSIVMA QKLKGTLSFI AKDDEGATHE
     KLDFRLHFSC SSYLITTPCY SDAFAKLLES GDLSMNSIKV DGISMSFQNL LAKICFYHHF
     SVVERVDSCA SMYSRSIQGH HVCLLVKKGE SSVSVDGKCS DATLLSSLLE EMKTTLAQC
//
ID   SRPK2_MOUSE             Reviewed;         681 AA.
AC   O54781; Q8VCD9;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 2.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Serine/threonine-protein kinase SRPK2;
DE            EC=2.7.11.1;
DE   AltName: Full=SFRS protein kinase 2;
DE   AltName: Full=Serine/arginine-rich protein-specific kinase 2;
DE            Short=SR-protein-specific kinase 2;
GN   Name=Srpk2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Brain;
RX   MEDLINE=98113357; PubMed=9446799; DOI=10.1006/bbrc.1997.7913;
RA   Kuroyanagi N., Onogi H., Wakabayashi T., Hagiwara M.;
RT   "Novel SR-protein-specific kinase, SRPK2, disassembles nuclear
RT   speckles.";
RL   Biochem. Biophys. Res. Commun. 242:357-364(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Phosphorylates RS domain-containing proteins, such as
CC       SFRS1 and SFRS2 on serine residues. Role in spliceosome assembly
CC       and in mediating the trafficking of splicing factors.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: Activated by phosphorylation on Ser-50 and Ser-
CC       581 (By similarity).
CC   -!- INTERACTION:
CC       Q07955:SFRS1 (xeno); NbExp=2; IntAct=EBI-593325, EBI-398920;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed in testes, lung and brain.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AB006036; BAA24055.1; -; mRNA.
DR   EMBL; BC020178; AAH20178.1; -; mRNA.
DR   IPI; IPI00751009; -.
DR   PIR; JC5929; JC5929.
DR   RefSeq; NP_033300.2; NM_009274.2.
DR   UniGene; Mm.288728; -.
DR   ProteinModelPortal; O54781; -.
DR   SMR; O54781; 62-281, 501-681.
DR   IntAct; O54781; 3.
DR   STRING; O54781; -.
DR   PhosphoSite; O54781; -.
DR   PRIDE; O54781; -.
DR   Ensembl; ENSMUST00000088392; ENSMUSP00000085734; ENSMUSG00000062604.
DR   GeneID; 20817; -.
DR   KEGG; mmu:20817; -.
DR   UCSC; uc008wqe.1; mouse.
DR   CTD; 20817; -.
DR   MGI; MGI:1201408; Srpk2.
DR   eggNOG; roNOG04404; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108512; -.
DR   InParanoid; O54781; -.
DR   OrthoDB; EOG4SXNCR; -.
DR   PhylomeDB; O54781; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 299545; -.
DR   ArrayExpress; O54781; -.
DR   Bgee; O54781; -.
DR   CleanEx; MM_SRPK2; -.
DR   Genevestigator; O54781; -.
DR   GermOnline; ENSMUSG00000062604; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007243; P:intracellular protein kinase cascade; IDA:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0000245; P:spliceosome assembly; IDA:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   Pfam; PF00069; Pkinase; 2.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Differentiation; Kinase; mRNA processing;
KW   mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    681       Serine/threonine-protein kinase SRPK2.
FT                                /FTId=PRO_0000086678.
FT   DOMAIN       79    681       Protein kinase.
FT   NP_BIND      85     93       ATP (By similarity).
FT   ACT_SITE    212    212       Proton acceptor (By similarity).
FT   BINDING     108    108       ATP (By similarity).
FT   MOD_RES      50     50       Phosphoserine; by CK2 (By similarity).
FT   MOD_RES     317    317       Phosphotyrosine (By similarity).
FT   MOD_RES     378    378       Phosphoserine (By similarity).
FT   MOD_RES     487    487       Phosphoserine (By similarity).
FT   MOD_RES     490    490       Phosphoserine (By similarity).
FT   MOD_RES     491    491       Phosphothreonine (By similarity).
FT   MOD_RES     540    540       Phosphothreonine (By similarity).
FT   MOD_RES     581    581       Phosphoserine; by CK2 (By similarity).
FT   CONFLICT    313    313       Q -> QQ (in Ref. 2; AAH20178).
FT   CONFLICT    368    368       L -> P (in Ref. 1; BAA24055).
SQ   SEQUENCE   681 AA;  76757 MW;  1857EA955B2F9C0E CRC64;
     MSVNSEKSSS SERPEPQQKA PLVPPPPPPP PPPPLPDPAP PEPEEEILGS DDEEQEDPAD
     YCKGGYHPVK IGDLFNGRYH VIRKLGWGHF STVWLCWDMQ GKRFVAMKVV KSAQHYTETA
     LDEIKLLKCV RESDPSDPNK DMVVQLIDDF KISGMNGIHV CMVFEVLGHH LLKWIIKSNY
     QGLPVRCVKS IIRQVLQGLD YLHSKCKIIH TDIKPENILM CVDDAYVRRM AAEATEWQKA
     GAPPPSGSAV STAPQQKPIG KISKNKKKKL KKKQKRQAEL LEKRLQEIEE LEREAERKIL
     EENITSAEAS GEQDGEYQPE VTLKAADLED TTEEETAKDN GEVEDQEEKE DAEKENAEKD
     EDDVEQELAN LDPTWVESPK ANGHIENGPF SLEQQLEDEE DDEDDCANPE EYNLDEPNAE
     SDYTYSSSYE QFNGELPNGQ HKTSEFPTPL FSGPLEPVAC GSVISEGSPL TEQEESSPSH
     DRSRTVSASS TGDLPKTKTR AADLLVNPLD PRNADKIRVK IADLGNACWV HKHFTEDIQT
     RQYRSIEVLI GAGYSTPADI WSTACMAFEL ATGDYLFEPH SGEDYSRDED HIAHIIELLG
     SIPRHFALSG KYSREFFNRR GELRHITKLK PWSLFDVLVE KYGWPHEDAA QFTDFLIPML
     EMVPEKRASA GECLRHPWLN S
//
ID   NMBR_MOUSE              Reviewed;         390 AA.
AC   O54799;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Neuromedin-B receptor;
DE            Short=NMB-R;
DE   AltName: Full=Neuromedin-B-preferring bombesin receptor;
GN   Name=Nmbr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv; TISSUE=Liver;
RX   MEDLINE=97404084; PubMed=9262170; DOI=10.1016/S0006-8993(97)00380-6;
RA   Ohki-Hamazaki H., Wada E., Matsui K., Wada K.;
RT   "Cloning and expression of the neuromedin B receptor and the third
RT   subtype of bombesin receptor genes in the mouse.";
RL   Brain Res. 762:165-172(1997).
CC   -!- FUNCTION: Receptor for neuromedin-B.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB010281; BAA24405.1; -; Genomic_DNA.
DR   IPI; IPI00117887; -.
DR   RefSeq; NP_032729.1; NM_008703.2.
DR   UniGene; Mm.481215; -.
DR   ProteinModelPortal; O54799; -.
DR   SMR; O54799; 43-340.
DR   STRING; O54799; -.
DR   PhosphoSite; O54799; -.
DR   PRIDE; O54799; -.
DR   Ensembl; ENSMUST00000020015; ENSMUSP00000020015; ENSMUSG00000019865.
DR   GeneID; 18101; -.
DR   KEGG; mmu:18101; -.
DR   UCSC; uc007elp.1; mouse.
DR   CTD; 18101; -.
DR   MGI; MGI:1100525; Nmbr.
DR   eggNOG; roNOG10589; -.
DR   HOGENOM; HBG713709; -.
DR   HOVERGEN; HBG004898; -.
DR   InParanoid; O54799; -.
DR   OMA; IKSAHNL; -.
DR   OrthoDB; EOG4M398N; -.
DR   PhylomeDB; O54799; -.
DR   NextBio; 293267; -.
DR   ArrayExpress; O54799; -.
DR   Bgee; O54799; -.
DR   CleanEx; MM_NMBR; -.
DR   Genevestigator; O54799; -.
DR   GermOnline; ENSMUSG00000019865; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004946; F:bombesin receptor activity; IEA:InterPro.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR001556; Bombsn_rcpt.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR001642; NeuroB_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00358; BOMBESINR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00639; NEUROMEDINBR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Lipoprotein; Membrane; Palmitate; Receptor; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    390       Neuromedin-B receptor.
FT                                /FTId=PRO_0000069904.
FT   TOPO_DOM      1     41       Extracellular (Potential).
FT   TRANSMEM     42     65       Helical; Name=1; (Potential).
FT   TOPO_DOM     66     79       Cytoplasmic (Potential).
FT   TRANSMEM     80     99       Helical; Name=2; (Potential).
FT   TOPO_DOM    100    117       Extracellular (Potential).
FT   TRANSMEM    118    139       Helical; Name=3; (Potential).
FT   TOPO_DOM    140    156       Cytoplasmic (Potential).
FT   TRANSMEM    157    177       Helical; Name=4; (Potential).
FT   TOPO_DOM    178    211       Extracellular (Potential).
FT   TRANSMEM    212    235       Helical; Name=5; (Potential).
FT   TOPO_DOM    236    266       Cytoplasmic (Potential).
FT   TRANSMEM    267    287       Helical; Name=6; (Potential).
FT   TOPO_DOM    288    299       Extracellular (Potential).
FT   TRANSMEM    300    327       Helical; Name=7; (Potential).
FT   TOPO_DOM    328    390       Cytoplasmic (Potential).
FT   LIPID       341    341       S-palmitoyl cysteine (By similarity).
FT   CARBOHYD      8      8       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     16     16       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    192    192       N-linked (GlcNAc...) (Potential).
FT   DISULFID    116    198       By similarity.
SQ   SEQUENCE   390 AA;  43623 MW;  2EA733B1DF108B42 CRC64;
     MPPRSLSNLS FPTEANESEL VPEVWEKDFL PDSDGTTAEL VIRCVIPSLY LIIISVGLLG
     NIMLVKIFLT NSAMRNVPNI FISNLAAGDL LLLLTCVPVD ASRYFFDEWV FGKLGCKLIP
     AIQLTSVGVS VFTLTALSAD RYRAIVNPMD MQTSGVLLWT SLKAVGIWVV SVLLAVPEAV
     FSEVARIGSL DNSSFTACIP YPQTDELHPK IHSVLIFLVY FLIPLVIISI YYYHIAKTLI
     KSAHNLPGEY NEHTKKQMET RKRLAKIVLV FVGCFVFCWF PNHVLYLYRS FNYKEIDPSL
     GHMIVTLVAR VLSFSNSCVN PFALYLLSES FRKHFNSQLC CGRKSYPERS TSYLLSSSAV
     RMTSLKSNTK NVVTNSVLLN GHSTKQEIAL
//
ID   IL16_MOUSE              Reviewed;        1322 AA.
AC   O54824; O70236; Q3TEM4; Q5DTR5; Q8R0G5; Q9QZP6;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 3.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Pro-interleukin-16;
DE   Contains:
DE     RecName: Full=Interleukin-16;
DE              Short=IL-16;
DE     AltName: Full=Lymphocyte chemoattractant factor;
DE              Short=LCF;
GN   Name=Il16;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY
RP   (ISOFORM 2).
RC   STRAIN=NFS; TISSUE=Spleen;
RX   MEDLINE=98299621; PubMed=9637508;
RA   Keane J., Nicoll J., Kim S., Wu D.M.H., Cruikshank W.W., Brazer W.,
RA   Natke B., Zhang Y., Center D.M., Kornfeld H.;
RT   "Conservation of structure and function between human and murine IL-
RT   16.";
RL   J. Immunol. 160:5945-5954(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   MEDLINE=98179136; PubMed=9510557; DOI=10.1007/s002510050374;
RA   Bannert N., Adler H.S., Werner A., Baier M., Kurth R.;
RT   "Molecular cloning and sequence analysis of interleukin 16 from
RT   nonhuman primates and from the mouse.";
RL   Immunogenetics 47:390-397(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM
RP   1), TISSUE SPECIFICITY (ISOFORM 1), INTERACTION WITH GRIN2A; GRIN2D;
RP   KCNJ10; KCNJ15 AND CACNA1C, AND PROTEOLYTIC PROCESSING.
RX   MEDLINE=99410760; PubMed=10479680;
RA   Kurschner C., Yuzaki M.;
RT   "Neuronal interleukin-16 (NIL-16): a dual function PDZ domain
RT   protein.";
RL   J. Neurosci. 19:7770-7780(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-838, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-917, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Interleukin-16 stimulates a migratory response in CD4+
CC       lymphocytes, monocytes, and eosinophils. Primes CD4+ T-cells for
CC       IL-2 and IL-15 responsiveness. Also induces T-lymphocyte
CC       expression of interleukin 2 receptor. Ligand for CD4.
CC   -!- FUNCTION: Isoform 1 may act as a scaffolding protein that anchors
CC       ion channels in the membrane.
CC   -!- FUNCTION: Isoform 2 is involved in cell cycle progression in T-
CC       cells. Appears to be involved in transcriptional regulation of
CC       SKP2 and is probably part of a transcriptional repression complex
CC       on the core promoter of the SKP2 gene. May act as a scaffold for
CC       GABPB1 (the DNA-binding subunit the GABP transcription factor
CC       complex) and HDAC3 thus maintaining transcriptional repression and
CC       blocking cell cycle progression in resting T-cells.
CC   -!- SUBUNIT: Homotetramer (Probable). Isoform 2 interacts with GRIN2A.
CC       Isoform 1 interacts with GRIN2D, KCNJ10, KCNJ15 and CACNA1C.
CC       Isoform 2 interacts (via PDZ 3 domain) with PPP1R12A, PPP1R12B and
CC       PPP1R12C. Isoform 1 interacts with PPP1R12B. Isoform 3 interacts
CC       with GABPB1. Isoform 2 interacts (via PDZ 3 domain) with HDAC3 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Note=Colocalizes with
CC       GRIN2C in neuronal cell bodies and neurites.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage; Named isoforms=2;
CC       Name=1; Synonyms=NIL-16;
CC         IsoId=O54824-1; Sequence=Displayed;
CC         Note=Produced by alternative promoter usage. Is probably
CC         proteolytically processed to yield IL-16;
CC       Name=2; Synonyms=Pro-IL-16;
CC         IsoId=O54824-2; Sequence=VSP_037460;
CC         Note=Produced by alternative promoter usage. Is proteolytically
CC         processed to yield IL-16;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is expressed in neurons of the
CC       cerebellum and hippocampus. Isoform 2 is expressed in thymus,
CC       spleen and lung.
CC   -!- PTM: Synthesized as a chemo-attractant inactive precursor which is
CC       proteolytically cleaved by caspase-3 to yield IL-16.
CC   -!- SIMILARITY: Contains 4 PDZ (DHR) domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF006001; AAC04383.1; -; mRNA.
DR   EMBL; AF017111; AAC16039.1; -; mRNA.
DR   EMBL; AF175292; AAD55393.1; -; mRNA.
DR   EMBL; AK038319; BAC29967.1; -; mRNA.
DR   EMBL; AK169551; BAE41224.1; -; mRNA.
DR   EMBL; AK220455; BAD90484.1; -; mRNA.
DR   EMBL; CH466543; EDL06877.1; -; Genomic_DNA.
DR   EMBL; BC026894; AAH26894.1; -; mRNA.
DR   EMBL; BC058709; AAH58709.1; -; mRNA.
DR   IPI; IPI00137805; -.
DR   IPI; IPI00930865; -.
DR   RefSeq; NP_034681.2; NM_010551.3.
DR   UniGene; Mm.10137; -.
DR   ProteinModelPortal; O54824; -.
DR   SMR; O54824; 98-439, 1096-1322.
DR   IntAct; O54824; 3.
DR   MINT; MINT-103508; -.
DR   STRING; O54824; -.
DR   PhosphoSite; O54824; -.
DR   PRIDE; O54824; -.
DR   Ensembl; ENSMUST00000001792; ENSMUSP00000001792; ENSMUSG00000001741.
DR   GeneID; 16170; -.
DR   KEGG; mmu:16170; -.
DR   UCSC; uc009idr.1; mouse.
DR   CTD; 16170; -.
DR   MGI; MGI:1270855; Il16.
DR   eggNOG; roNOG07323; -.
DR   HOGENOM; HBG277834; -.
DR   HOVERGEN; HBG000100; -.
DR   InParanoid; O54824; -.
DR   OMA; HRVFPNG; -.
DR   OrthoDB; EOG4PNXG5; -.
DR   PhylomeDB; O54824; -.
DR   ArrayExpress; O54824; -.
DR   Bgee; O54824; -.
DR   CleanEx; MM_IL16; -.
DR   Genevestigator; O54824; -.
DR   GermOnline; ENSMUSG00000001741; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005125; F:cytokine activity; IDA:MGI.
DR   GO; GO:0050930; P:induction of positive chemotaxis; IDA:MGI.
DR   GO; GO:0030595; P:leukocyte chemotaxis; IDA:MGI.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR020450; Interleukin-16.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF00595; PDZ; 4.
DR   PRINTS; PR01931; INTRLEUKIN16.
DR   SMART; SM00228; PDZ; 4.
DR   SUPFAM; SSF50156; PDZ; 4.
DR   PROSITE; PS50106; PDZ; 4.
PE   1: Evidence at protein level;
KW   Alternative promoter usage; Chemotaxis; Cytokine; Cytoplasm; Nucleus;
KW   Phosphoprotein; Repeat; Secreted; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   1322       Pro-interleukin-16.
FT                                /FTId=PRO_0000377546.
FT   CHAIN      1205   1322       Interleukin-16 (By similarity).
FT                                /FTId=PRO_0000015418.
FT   DOMAIN      213    299       PDZ 1.
FT   DOMAIN      352    437       PDZ 2.
FT   DOMAIN     1105   1190       PDZ 3.
FT   DOMAIN     1226   1309       PDZ 4.
FT   REGION      183    449       Interaction with GRIN2A (By similarity).
FT   REGION     1099   1195       Interaction with PPP1R12A, PPP1R12B and
FT                                PPP1R12C (By similarity).
FT   MOD_RES     838    838       Phosphoserine.
FT   MOD_RES     917    917       Phosphoserine.
FT   VAR_SEQ       1    698       Missing (in isoform 2).
FT                                /FTId=VSP_037460.
FT   CONFLICT    264    264       I -> S (in Ref. 5; BAD90484).
FT   CONFLICT    733    733       T -> R (in Ref. 1; AAC04383).
FT   CONFLICT    921    921       G -> S (in Ref. 2; AAC16039).
FT   CONFLICT   1067   1067       S -> P (in Ref. 2; AAC16039).
FT   CONFLICT   1224   1224       V -> A (in Ref. 2; AAC16039).
FT   CONFLICT   1262   1264       TEQ -> DRT (in Ref. 1; AAC04383).
SQ   SEQUENCE   1322 AA;  141435 MW;  DDB94003A5DCB738 CRC64;
     MEPHGHSGKS RKSTKFRSIS RSLILCNAKT SDDGSSPDEK YPDPFETSLC QGKEGFFHSS
     MQLADTFEAG LSNIPDLALA SDSAQLAAAG SDRGKHCRKM FFMKESSSTS SKEKSGKPEA
     QSSSFLFPKA CHQRTRSNST SVNPYSAGEI DFPMTKKSAA PTDRQPYSLC SNRKSLSQQL
     DYPILGTARP TRSLSTAQLG QLSGGLQASV ISNIVLMKGQ AKGLGFSIVG GKDSIYGPIG
     IYVKSIFAGG AAAADGRLQE GDEILELNGE SMAGLTHQDA LQKFKQAKKG LLTLTVRTRL
     TTPPSLCSHL SPPLCRSLSS STCGAQDSSP FSLESPASPA STAKPNYRIM VEVSLKKEAG
     VGLGIGLCSI PYFQCISGIF VHTLSPGSVA HLDGRLRCGD EIVEINDSPV HCLTLNEVYT
     ILSHCDPGPV PIIVSRHPDP QVSEQQLKEA VAQAVEGVKF GKDRHQWSLE GVKRLESSWH
     GRPTLEKERE KHSAPPHRRA QKIMVRSSSD SSYMSGSPGG SPCSAGAEPQ PSEREGSTHS
     PSLSPGEEQE PCPGVPSRPQ QESPPLPESL ERESHPPLRL KKSFEILVRK PTSSKPKPPP
     RKYFKNDSEP QKKLEEKEKV TDPSGHTLPT CSQETRELLP LLLQEDTAGR APCTAACCPG
     PAASTQTSSS TEGESRRSAS PETPASPGKH PLLKRQARMD YSFDITAEDP WVRISDCIKN
     LFSPIMSENH SHTPLQPNTS LGEEDGTQGC PEGGLSKMDA ANGAPRVYKS ADGSTVKKGP
     PVAPKPAWFR QSLKGLRNRA PDPRRPPEVA SAIQPTPVSR DPPGPQPQAS SSIRQRISSF
     ENFGSSQLPD RGVQRLSLQP SSGETTKFPG KQDGGRFSGL LGQGATVTAK HRQTEVESMS
     TTFPNSSEVR DPGLPESPPP GQRPSTKALS PDPLLRLLTT QSEDTQGPGL KMPSQRARSF
     PLTRTQSCET KLLDEKASKL YSISSQLSSA VMKSLLCLPS SVSCGQITCI PKERVSPKSP
     CNNSSAAEGF GEAMASDTGF SLNLSELREY SEGLTEPGET EDRNHCSSQA GQSVISLLSA
     EELEKLIEEV RVLDEATLKQ LDSIHVTILH KEEGAGLGFS LAGGADLENK VITVHRVFPN
     GLASQEGTIQ KGNEVLSING KSLKGATHND ALAILRQARD PRQAVIVTRR TTVEATHDLN
     SSTDSAASAS AASDISVESK EATVCTVTLE KTSAGLGFSL EGGKGSLHGD KPLTINRIFK
     GTEQGEMVQP GDEILQLAGT AVQGLTRFEA WNVIKALPDG PVTIVIRRTS LQCKQTTASA
     DS
//
ID   BYST_MOUSE              Reviewed;         436 AA.
AC   O54825; Q3THF4; Q3UPY9; Q8VD68;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 3.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Bystin;
GN   Name=Bysl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, and C57BL/6J;
RC   TISSUE=Embryo, Embryonic spinal cord, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 151-436.
RA   Suzuki N., Fukuda M.N.;
RT   "Characterization of mouse bystin.";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17055491; DOI=10.1016/j.febslet.2006.09.072;
RA   Aoki R., Suzuki N., Paria B.C., Sugihara K., Akama T.O., Raab G.,
RA   Miyoshi M., Nadano D., Fukuda M.N.;
RT   "The Bysl gene product, bystin, is essential for survival of mouse
RT   embryos.";
RL   FEBS Lett. 580:6062-6068(2006).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=17242206; DOI=10.1128/MCB.01908-06;
RA   Adachi K., Soeta-Saneyoshi C., Sagara H., Iwakura Y.;
RT   "Crucial role of Bysl in mammalian preimplantation development as an
RT   integral factor for 40S ribosome biogenesis.";
RL   Mol. Cell. Biol. 27:2202-2214(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Required for processing of 20S pre-rRNA precursor and
CC       biogenesis of 40S ribosomal subunits.
CC   -!- SUBUNIT: Binds trophinin, tastin and cytokeratins (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus.
CC       Note=Associated with 40S ribosomal subunits.
CC   -!- TISSUE SPECIFICITY: High levels in preimplantation embryos, bone
CC       marrow, brain, testis and ovary.
CC   -!- DEVELOPMENTAL STAGE: High levels of maternal transcript in
CC       unfertilized eggs. High levels up to blastocyst stage.
CC   -!- DISRUPTION PHENOTYPE: Mice show embryonic lethality around stage
CC       E6.5 shortly after implantation. Mice lacking maternal Bysl
CC       transcript upon injection of siRNA into fertilized eggs are
CC       arrested at the 16-cell stage, fail to induce trophectoderm, and
CC       show altered morphology of developing nucleoli. Embryonic stem
CC       cells lacking Bysl show accumulation of pre-20S rRNA precursors
CC       and a reduction of 40S ribosomal subunits in the cytoplasm.
CC   -!- SIMILARITY: Belongs to the bystin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH17530.3; Type=Erroneous initiation;
CC       Sequence=BAB31619.2; Type=Erroneous initiation;
CC       Sequence=BAC38736.1; Type=Erroneous initiation;
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DR   EMBL; AK019239; BAB31619.2; ALT_INIT; mRNA.
DR   EMBL; AK083033; BAC38736.1; ALT_INIT; mRNA.
DR   EMBL; AK143027; BAE25255.1; -; mRNA.
DR   EMBL; AK168301; BAE40242.1; -; mRNA.
DR   EMBL; BC017530; AAH17530.3; ALT_INIT; mRNA.
DR   EMBL; AF007802; AAB94491.1; -; mRNA.
DR   IPI; IPI00118762; -.
DR   RefSeq; NP_058555.3; NM_016859.3.
DR   UniGene; Mm.472101; -.
DR   STRING; O54825; -.
DR   PhosphoSite; O54825; -.
DR   PRIDE; O54825; -.
DR   Ensembl; ENSMUST00000024783; ENSMUSP00000024783; ENSMUSG00000023988.
DR   GeneID; 53414; -.
DR   KEGG; mmu:53414; -.
DR   CTD; 53414; -.
DR   MGI; MGI:1858419; Bysl.
DR   eggNOG; roNOG13605; -.
DR   HOGENOM; HBG738986; -.
DR   HOVERGEN; HBG024425; -.
DR   InParanoid; O54825; -.
DR   OMA; MTGAGHH; -.
DR   OrthoDB; EOG4VHK6H; -.
DR   PhylomeDB; O54825; -.
DR   NextBio; 310229; -.
DR   ArrayExpress; O54825; -.
DR   Bgee; O54825; -.
DR   CleanEx; MM_BYSL; -.
DR   Genevestigator; O54825; -.
DR   GermOnline; ENSMUSG00000023988; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR007955; Bystin.
DR   PANTHER; PTHR12821; Bystin; 1.
DR   Pfam; PF05291; Bystin; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Ribosome biogenesis.
FT   CHAIN         1    436       Bystin.
FT                                /FTId=PRO_0000186115.
FT   MOD_RES      15     15       N6-acetyllysine (By similarity).
FT   MOD_RES      97     97       Phosphoserine.
FT   MOD_RES     166    166       Phosphoserine (By similarity).
FT   CONFLICT    284    284       A -> V (in Ref. 1; BAE40242).
SQ   SEQUENCE   436 AA;  49784 MW;  EFA148BED2072B72 CRC64;
     MPKFKVTRGA SNREKHAPLA EQILAGNAVR AGTREKRRGR EVEEEEEYVG PRLSRRILQQ
     ARQQQEELET DHGAGDRSAP PRERATRLGP GLPQDGSDEE DEEWPTLEKA AKMAGVDHQA
     EVIVDPEDER AIEMFMNKNP PVRRTLADII MEKLTEKQTE VETVMSEVSG FPMPQLDPRV
     LEVYRGVREV LCKYRSGKLP KAFKVIPALS NWEQILYVTE PEAWTAAAMY QATRIFASNL
     KERMAQRFYN LVLLPRVRDD IAEYKRLNFH LYMALKKALF KPGAWFKGIL IPLCESGTCT
     LREAIIVGSI ITKCSIPVLH SSAAMLKIAE MEYSGANSIF LRLLLDKKYA LPYRVLDALV
     FHFLAFRTEK RQLPVLWHQC LLTLAQRYKA DLATEQKEAL LELLRLQPHP QLSPEIRREL
     QSAVPRDVED GGVTME
//
ID   RGS9_MOUSE              Reviewed;         675 AA.
AC   O54828; Q9Z0S0;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Regulator of G-protein signaling 9;
DE            Short=RGS9;
GN   Name=Rgs9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=98119533; PubMed=9459445; DOI=10.1016/S0896-6273(00)80437-7;
RA   He W., Cowan C.W., Wensel T.G.;
RT   "RGS9, a GTPase accelerator for phototransduction.";
RL   Neuron 20:95-102(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Forebrain;
RX   MEDLINE=99165807; PubMed=10066255;
RA   Rahman Z., Gold S.J., Potenza M.N., Cowan C.W., Ni Y.G., He W.,
RA   Wensel T.G., Nestler E.J.;
RT   "Cloning and characterization of RGS9-2: a striatal-enriched
RT   alternatively spliced product of the RGS9 gene.";
RL   J. Neurosci. 19:2016-2026(1999).
RN   [3]
RP   PHOSPHORYLATION OF ISOFORM 1.
RX   MEDLINE=21303582; PubMed=11292825; DOI=10.1074/jbc.M011539200;
RA   Hu G., Jang G.F., Cowan C.W., Wensel T.G., Palczewski K.;
RT   "Phosphorylation of RGS9-1 by an endogenous protein kinase in rod
RT   outer segments.";
RL   J. Biol. Chem. 276:22287-22295(2001).
RN   [4]
RP   INTERACTION WITH RGS9BP.
RC   STRAIN=C57BL/6 X 129; TISSUE=Retina;
RX   MEDLINE=22133783; PubMed=12119397; DOI=10.1073/pnas.152094799;
RA   Hu G., Wensel T.G.;
RT   "R9AP, a membrane anchor for the photoreceptor GTPase accelerating
RT   protein, RGS9-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9755-9760(2002).
RN   [5]
RP   INTERACTION WITH RGS9BP.
RX   PubMed=12499365; DOI=10.1074/jbc.M211782200;
RA   Sokal I., Hu G., Liang Y., Mao M., Wensel T.G., Palczewski K.;
RT   "Identification of protein kinase C isozymes responsible for the
RT   phosphorylation of photoreceptor-specific RGS9-1 at Ser475.";
RL   J. Biol. Chem. 278:8316-8325(2003).
RN   [6]
RP   INTERACTION WITH RGS9BP.
RX   MEDLINE=22979145; PubMed=14614075;
RA   Martemyanov K.A., Lishko P.V., Calero N., Keresztes G., Sokolov M.,
RA   Strissel K.J., Leskov I.B., Hopp J.A., Kolesnikov A.V., Chen C.-K.,
RA   Lem J., Heller S., Burns M.E., Arshavsky V.Y.;
RT   "The DEP domain determines subcellular targeting of the GTPase
RT   activating protein RGS9 in vivo.";
RL   J. Neurosci. 23:10175-10181(2003).
RN   [7]
RP   INTERACTION WITH RGS7BP.
RX   PubMed=15632198; DOI=10.1074/jbc.C400596200;
RA   Martemyanov K.A., Yoo P.J., Skiba N.P., Arshavsky V.Y.;
RT   "R7BP, a novel neuronal protein interacting with RGS proteins of the
RT   R7 family.";
RL   J. Biol. Chem. 280:5133-5136(2005).
RN   [8]
RP   INTERACTION WITH RGS7BP.
RX   PubMed=15897264; DOI=10.1083/jcb.200502007;
RA   Drenan R.M., Doupnik C.A., Boyle M.P., Muglia L.J., Huettner J.E.,
RA   Linder M.E., Blumer K.J.;
RT   "Palmitoylation regulates plasma membrane-nuclear shuttling of R7BP, a
RT   novel membrane anchor for the RGS7 family.";
RL   J. Cell Biol. 169:623-633(2005).
RN   [9]
RP   INTERACTION WITH RGS9BP.
RX   PubMed=16908407; DOI=10.1016/j.neuron.2006.07.010;
RA   Krispel C.M., Chen D., Melling N., Chen Y.-J., Martemyanov K.A.,
RA   Quillinan N., Arshavsky V.Y., Wensel T.G., Chen C.-K., Burns M.E.;
RT   "RGS expression rate-limits recovery of rod photoresponses.";
RL   Neuron 51:409-416(2006).
CC   -!- FUNCTION: Inhibits signal transduction by increasing the GTPase
CC       activity of G protein alpha subunits thereby driving them into
CC       their inactive GDP-bound form. Binds to G(t)-alpha. Involved in
CC       phototransduction; key element in the recovery phase of visual
CC       transduction.
CC   -!- SUBUNIT: Heterodimer with Gbeta5. Interacts with RGS7BP, leading
CC       to regulate the subcellular location of the heterodimer formed
CC       with Gbeta5. Component of the RGS9-1-Gbeta5 complex composed of
CC       isoform 1 of RGS9 (RGS9-1), Gbeta5 (GNB5) and RGS9BP (Probable).
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Membrane; Peripheral membrane
CC       protein. Note=Isoform 1 is targeted to the membrane via its
CC       interaction with RGS9BP.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2; Synonyms=RGS9-2;
CC         IsoId=O54828-1; Sequence=Displayed;
CC       Name=1; Synonyms=RGS9-1;
CC         IsoId=O54828-2; Sequence=VSP_005678, VSP_005679;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is expressed in photoreceptor outer
CC       segments. Isoform 2 is expressed in brain striatum.
CC   -!- PTM: Retinal isoform 1 is light-dependent phosphorylated at 'Ser-
CC       475'. Phosphorylation is decreased by light exposition.
CC       Interaction with RGS9BP is decreased when isoform 1 is
CC       phosphorylated at 'Ser-475'.
CC   -!- SIMILARITY: Contains 1 DEP domain.
CC   -!- SIMILARITY: Contains 1 G protein gamma domain.
CC   -!- SIMILARITY: Contains 1 RGS domain.
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DR   EMBL; AF011358; AAC99481.1; -; mRNA.
DR   EMBL; AF125046; AAD20014.1; -; mRNA.
DR   IPI; IPI00118767; -.
DR   IPI; IPI00223466; -.
DR   UniGene; Mm.38548; -.
DR   PDB; 2PBI; X-ray; 1.95 A; A/C=1-422.
DR   PDBsum; 2PBI; -.
DR   ProteinModelPortal; O54828; -.
DR   SMR; O54828; 7-421.
DR   DIP; DIP-46389N; -.
DR   STRING; O54828; -.
DR   PRIDE; O54828; -.
DR   Ensembl; ENSMUST00000020920; ENSMUSP00000020920; ENSMUSG00000020599.
DR   UCSC; uc007mbx.1; mouse.
DR   MGI; MGI:1338824; Rgs9.
DR   GeneTree; ENSGT00560000076525; -.
DR   HOGENOM; HBG385421; -.
DR   HOVERGEN; HBG007404; -.
DR   InParanoid; O54828; -.
DR   OrthoDB; EOG44XJGT; -.
DR   ArrayExpress; O54828; -.
DR   Bgee; O54828; -.
DR   CleanEx; MM_RGS9; -.
DR   Genevestigator; O54828; -.
DR   GermOnline; ENSMUSG00000020599; Mus musculus.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; TAS:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR015898; G-protein_gamma_dom.
DR   InterPro; IPR000342; Regulat_G_prot_signal.
DR   InterPro; IPR016137; Regulat_G_prot_signal_superfam.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:4.10.260.10; G-protein_gamma_dom; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF00631; G-gamma; 1.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00049; DEP; 1.
DR   SMART; SM00224; GGL; 1.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48670; G-protein_gamma-like; 1.
DR   SUPFAM; SSF48097; Regulat_G_prot_signal_superfam; 1.
DR   PROSITE; PS50186; DEP; 1.
DR   PROSITE; PS50058; G_PROTEIN_GAMMA; FALSE_NEG.
DR   PROSITE; PS50132; RGS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Membrane; Phosphoprotein;
KW   Sensory transduction; Signal transduction inhibitor; Vision.
FT   CHAIN         1    675       Regulator of G-protein signaling 9.
FT                                /FTId=PRO_0000204204.
FT   DOMAIN       30    105       DEP.
FT   DOMAIN      222    283       G protein gamma.
FT   DOMAIN      299    414       RGS.
FT   VAR_SEQ     467    484       PGQHLAPSPHLAVYTGTC -> VMSKLDRRSQLKKELPPK
FT                                (in isoform 1).
FT                                /FTId=VSP_005678.
FT   VAR_SEQ     485    675       Missing (in isoform 1).
FT                                /FTId=VSP_005679.
FT   HELIX        16     27
FT   TURN         30     32
FT   HELIX        52     63
FT   HELIX        67     79
FT   STRAND       82     88
FT   STRAND       96     98
FT   STRAND      100    103
FT   HELIX       106    108
FT   HELIX       118    130
FT   STRAND      132    134
FT   HELIX       138    150
FT   HELIX       152    154
FT   HELIX       155    169
FT   HELIX       174    191
FT   STRAND      207    209
FT   HELIX       219    234
FT   HELIX       240    254
FT   HELIX       255    257
FT   HELIX       259    262
FT   HELIX       269    272
FT   HELIX       276    280
FT   HELIX       290    295
FT   TURN        296    298
FT   HELIX       300    305
FT   HELIX       307    319
FT   HELIX       325    337
FT   STRAND      340    342
FT   HELIX       343    354
FT   HELIX       367    376
FT   TURN        382    385
FT   HELIX       386    398
FT   HELIX       400    405
FT   HELIX       408    416
SQ   SEQUENCE   675 AA;  76972 MW;  0EC910D833FFD06D CRC64;
     MTIRHQGQQY RPRMAFLQKI EALVKDMQNP ETGVRMHNQR VLVTSVPHAM TGGDVLQWIT
     QRLWISNLEA QNLGNLIVKY GYIYPLQDPK NLILKPDSSL YRFQTPYFWP TQQWPAEDTD
     YAIYLAKRNI KKKGILEEYE KENYDFLNKK INYKWDFVIM RAKEQYRTGK ERNKADRYAL
     DCQEKAYWLV HRSPPGMNNV LDYGLDRVTN PNEVKKQTVT AVRKEIMYYQ QALMRSTVKS
     SVSLGGIVKY SEQFSSNDAI MSGCLPSNPW ITDDTQFWDL NAKLVEIPTK MRVERWAFNF
     SELIRDPKGR QSFQYFLKKE FSGENLGFWE ACEDLKYGDQ SKVKEKAEEI YKLFLAPGAR
     RWINIDGKTM DITVKGLRHP HRYVLDAAQT HIYMLMKKDS YARYLKSPIY KEMLAKAIEP
     QETTKRSSTL PFMRRHLRSS PSPVILRQLE EEEKAREAAN TVDITQPGQH LAPSPHLAVY
     TGTCVPPSPS SPFSPSCRSP RKPFASPSRF IRRPSIAICP SPSRVALEGS SGLEPKGEAS
     WSGANSGPSV TENREPSADH SRPQPRAPPK ARAALSLGRF LRRGCLASPV FARLSPKCPS
     VSHGKVQPLG DMGQQLPRLK PKKVANFFQI KMEMPTDSGT CLMDSDDPRA GESGDQTTEK
     EVICPWESLA EGKAG
//
ID   CSK22_MOUSE             Reviewed;         350 AA.
AC   O54833;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Casein kinase II subunit alpha';
DE            Short=CK II alpha';
DE            EC=2.7.11.1;
GN   Name=Csnk2a2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=98163749; PubMed=9503019; DOI=10.1006/geno.1997.5154;
RA   Xu X., Rich E.S. Jr., Seldin D.C.;
RT   "Murine protein kinase CK2 alpha': cDNA and genomic cloning and
RT   chromosomal mapping.";
RL   Genomics 48:79-86(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=98362010; PubMed=9694889; DOI=10.1074/jbc.273.33.21291;
RA   Orlandini M., Semplici F., Ferruzzi R., Meggio F., Pinna L.A.,
RA   Oliviero S.;
RT   "Protein kinase CK2alpha' is induced by serum as a delayed early gene
RT   and cooperates with Ha-ras in fibroblast transformation.";
RL   J. Biol. Chem. 273:21291-21297(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Casein kinases are operationally defined by their
CC       preferential utilization of acidic proteins such as caseins as
CC       substrates. The alpha and alpha' chains contain the catalytic
CC       site. Participates in Wnt signaling. CK2 phosphorylates 'Ser-389'
CC       of p53/TP53 following UV irradiation (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Tetramer composed of an alpha chain, an alpha' and two
CC       beta chains. Also component of a CK2-SPT16-SSRP1 complex composed
CC       of SSRP1, SUPT16H, CSNK2A1, CSNK2A2 and CSNK2B, the complex
CC       associating following UV irradiation (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. CK2 subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF012251; AAC53552.1; -; mRNA.
DR   EMBL; AJ001420; CAA04753.1; -; mRNA.
DR   EMBL; BC057862; AAH57862.1; -; mRNA.
DR   IPI; IPI00118795; -.
DR   RefSeq; NP_034104.1; NM_009974.3.
DR   UniGene; Mm.440348; -.
DR   ProteinModelPortal; O54833; -.
DR   SMR; O54833; 1-334.
DR   IntAct; O54833; 3.
DR   STRING; O54833; -.
DR   PhosphoSite; O54833; -.
DR   PRIDE; O54833; -.
DR   Ensembl; ENSMUST00000056919; ENSMUSP00000055919; ENSMUSG00000046707.
DR   GeneID; 13000; -.
DR   KEGG; mmu:13000; -.
DR   UCSC; uc009myk.1; mouse.
DR   CTD; 13000; -.
DR   MGI; MGI:88547; Csnk2a2.
DR   eggNOG; roNOG08248; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG107282; -.
DR   InParanoid; O54833; -.
DR   OMA; PSWGNQD; -.
DR   OrthoDB; EOG4J118H; -.
DR   PhylomeDB; O54833; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 282812; -.
DR   ArrayExpress; O54833; -.
DR   Bgee; O54833; -.
DR   CleanEx; MM_CSNK2A2; -.
DR   Genevestigator; O54833; -.
DR   GermOnline; ENSMUSG00000046707; Mus musculus.
DR   GO; GO:0005956; C:protein kinase CK2 complex; TAS:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR   GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.
FT   CHAIN         1    350       Casein kinase II subunit alpha'.
FT                                /FTId=PRO_0000085892.
FT   DOMAIN       40    325       Protein kinase.
FT   NP_BIND      46     54       ATP (By similarity).
FT   ACT_SITE    157    157       Proton acceptor (By similarity).
FT   BINDING      69     69       ATP (By similarity).
FT   MOD_RES      13     13       Phosphotyrosine (By similarity).
FT   MOD_RES      18     18       Phosphoserine (By similarity).
FT   MOD_RES      21     21       Phosphoserine (By similarity).
FT   MOD_RES      97     97       N6-acetyllysine (By similarity).
FT   MOD_RES     240    240       Phosphotyrosine (By similarity).
FT   MOD_RES     288    288       Phosphoserine (By similarity).
FT   MOD_RES     343    343       Phosphoserine (By similarity).
SQ   SEQUENCE   350 AA;  41215 MW;  C5FA314617627F5B CRC64;
     MPGPAAGSRA RVYAEVNSLR SREYWDYEAH VPSWGNQDDY QLVRKLGRGK YSEVFEAINI
     TNNERVVVKI LKPVKKKKIK REVKILENLR GGTNIIKLID TVKDPVSKTP ALVFEYINNT
     DFKQLYQILT DFDIRFYMYE LLKALDYCHS KGIMHRDVKP HNVMIDHQQK KLRLIDWGLA
     EFYHPAQEYN VRVASRYFKG PELLVDYQMY DYSLDMWSLG CMLASMIFRK EPFFHGQDNY
     DQLVRIAKVL GTDELYGYLK KYHIDLDPHF NDILGQHSRK RWENFIHSEN RHLVSPEALD
     LLDKLLRYDH QQRLTAKEAM EHPYFYPVVK EQSQPCAENT VLSSGLTAAR
//
ID   EOMES_MOUSE             Reviewed;         707 AA.
AC   O54839; Q3UPL1; Q52KJ1; Q8BN22; Q9JJL1; Q9QYG7;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 3.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Eomesodermin homolog;
DE   AltName: Full=T-box brain protein 2;
DE            Short=T-brain-2;
DE            Short=TBR-2;
GN   Name=Eomes; Synonyms=Tbr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=99337662; PubMed=10407135; DOI=10.1016/S0165-3806(99)00064-4;
RA   Kimura N., Nakashima K., Ueno M., Taga T.;
RT   "A novel mammalian T-box-containing gene, Tbr2, expressed in mouse
RT   developing brain.";
RL   Brain Res. Dev. Brain Res. 115:183-193(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
RP   2).
RC   STRAIN=129/Sv; TISSUE=Liver;
RX   MEDLINE=20432084; PubMed=10974533; DOI=10.1016/S0378-1119(00)00290-0;
RA   Ueno M., Kimura N., Nakashima K., Saito-Ohara F., Inazawa J., Taga T.;
RT   "Genomic organization, sequence and chromosomal localization of the
RT   mouse Tbr2 gene and a comparative study with Tbr1.";
RL   Gene 254:29-35(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Olfactory bulb, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 278-457.
RX   MEDLINE=98163742; PubMed=9503012; DOI=10.1006/geno.1997.5150;
RA   Wattler S., Russ A., Evans M., Nehls M.;
RT   "A combined analysis of genomic and primary protein structure defines
RT   the phylogenetic relationship of new members of the T-box family.";
RL   Genomics 48:24-33(1998).
RN   [7]
RP   FUNCTION IN TROPHOBLAST DIFFERENTIATION, FUNCTION IN GASTRULATION,
RP   DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX   PubMed=10716450; DOI=10.1038/35003601;
RA   Russ A.P., Wattler S., Colledge W.H., Aparicio S.A.J.R.,
RA   Carlton M.B.L., Pearce J.J., Barton S.C., Surani M.A., Ryan K.,
RA   Nehls M.C., Wilson V., Evans M.J.;
RT   "Eomesodermin is required for mouse trophoblast development and
RT   mesoderm formation.";
RL   Nature 404:95-99(2000).
RN   [8]
RP   FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=14605368; DOI=10.1126/science.1090148;
RA   Pearce E.L., Mullen A.C., Martins G.A., Krawczyk C.M., Hutchins A.S.,
RA   Zediak V.P., Banica M., DiCioccio C.B., Gross D.A., Mao C.-A.,
RA   Shen H., Cereb N., Yang S.Y., Lindsten T., Rossant J., Hunter C.A.,
RA   Reiner S.L.;
RT   "Control of effector CD8+ T cell function by the transcription factor
RT   Eomesodermin.";
RL   Science 302:1041-1043(2003).
RN   [9]
RP   FUNCTION IN GASTRULATION.
RX   PubMed=18171685; DOI=10.1242/dev.014357;
RA   Arnold S.J., Hofmann U.K., Bikoff E.K., Robertson E.J.;
RT   "Pivotal roles for eomesodermin during axis formation, epithelium-to-
RT   mesenchyme transition and endoderm specification in the mouse.";
RL   Development 135:501-511(2008).
RN   [10]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=18940588; DOI=10.1016/j.neuron.2008.09.028;
RA   Sessa A., Mao C.-A., Hadjantonakis A.-K., Klein W.H., Broccoli V.;
RT   "Tbr2 directs conversion of radial glia into basal precursors and
RT   guides neuronal amplification by indirect neurogenesis in the
RT   developing neocortex.";
RL   Neuron 60:56-69(2008).
CC   -!- FUNCTION: Functions as a transcriptional activator playing a
CC       crucial role during development. Functions in trophoblast
CC       differentiation and later in gastrulation, regulating both
CC       mesoderm delamination and endoderm specification. Plays a role in
CC       brain development being required for the specification and the
CC       proliferation of the intermediate progenitor cells and their
CC       progeny in the cerebral cortex. Also involved in the
CC       differentiation of CD8+ T-cells during immune response regulating
CC       the expression of lytic effector genes.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O54839-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O54839-2; Sequence=VSP_038806;
CC   -!- TISSUE SPECIFICITY: Expressed in CD8+ T-cells.
CC   -!- DEVELOPMENTAL STAGE: Originally expressed in the trophoectoderm of
CC       the blastocyst and later in the extra-embryonic ectoderm of the
CC       early post-implantation embryo. In the embryo proper, expressed in
CC       the posterior part of the epiblast. During gastrulation, extends
CC       distally into the primitive streak and nascent mesoderm. Also
CC       expressed in the developing forebrain and the olfactory lobes.
CC       Expressed at E12.5 and E14.5 in the forebrain.
CC   -!- INDUCTION: Up-regulated in CD8+ T-cells upon activation.
CC   -!- DISRUPTION PHENOTYPE: Embryonic lethal due to peri-implantation
CC       defects. Mutant embryos arrest soon after implantation and fail to
CC       form organized embryonic or extraembryonic structures. Conditional
CC       mutants, with expression abrogated in the inner cell mass of
CC       embryos from early implantation stages onward, display
CC       gastrulation defects.
CC   -!- SIMILARITY: Contains 1 T-box DNA-binding domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB031037; BAA83416.1; -; mRNA.
DR   EMBL; AB032373; BAB07808.1; -; Genomic_DNA.
DR   EMBL; AK089817; BAC40968.1; -; mRNA.
DR   EMBL; AK143454; BAE25384.1; -; mRNA.
DR   EMBL; AC173340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC094319; AAH94319.1; -; mRNA.
DR   EMBL; AF013281; AAC16233.1; -; mRNA.
DR   IPI; IPI00121983; -.
DR   IPI; IPI00830520; -.
DR   RefSeq; NP_001158261.1; NM_001164789.1.
DR   RefSeq; NP_034266.2; NM_010136.3.
DR   UniGene; Mm.200692; -.
DR   ProteinModelPortal; O54839; -.
DR   SMR; O54839; 269-458.
DR   STRING; O54839; -.
DR   PhosphoSite; O54839; -.
DR   PRIDE; O54839; -.
DR   Ensembl; ENSMUST00000111763; ENSMUSP00000107393; ENSMUSG00000032446.
DR   GeneID; 13813; -.
DR   KEGG; mmu:13813; -.
DR   CTD; 13813; -.
DR   MGI; MGI:1201683; Eomes.
DR   HOVERGEN; HBG000578; -.
DR   OMA; GFRAHVY; -.
DR   OrthoDB; EOG45QHD6; -.
DR   ArrayExpress; O54839; -.
DR   Bgee; O54839; -.
DR   CleanEx; MM_EOMES; -.
DR   Genevestigator; O54839; -.
DR   GermOnline; ENSMUSG00000032446; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0016563; F:transcription activator activity; ISS:UniProtKB.
DR   GO; GO:0002302; P:CD8-positive, alpha-beta T cell differentiation involved in immune response; IDA:UniProtKB.
DR   GO; GO:0060706; P:cell differentiation involved in embryonic placenta development; IMP:UniProtKB.
DR   GO; GO:0021895; P:cerebral cortex neuron differentiation; IDA:UniProtKB.
DR   GO; GO:0001706; P:endoderm formation; IMP:UniProtKB.
DR   GO; GO:0001707; P:mesoderm formation; IMP:UniProtKB.
DR   GO; GO:0060809; P:mesodermal to mesenchymal transition involved in gastrulation; IMP:UniProtKB.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; IDA:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   GO; GO:0001829; P:trophectodermal cell differentiation; IDA:MGI.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd.
DR   InterPro; IPR001699; TF_T-box.
DR   InterPro; IPR018186; TF_T-box_CS.
DR   Gene3D; G3DSA:2.60.40.820; TF_T-box; 1.
DR   PANTHER; PTHR11267; TF_T-box; 1.
DR   Pfam; PF00907; T-box; 1.
DR   PRINTS; PR00937; TBOX.
DR   SMART; SM00425; TBOX; 1.
DR   SUPFAM; SSF49417; P53_like_DNA_bnd; 1.
DR   PROSITE; PS01283; TBOX_1; 1.
DR   PROSITE; PS01264; TBOX_2; 1.
DR   PROSITE; PS50252; TBOX_3; 1.
PE   1: Evidence at protein level;
KW   Activator; Adaptive immunity; Alternative splicing;
KW   Developmental protein; Differentiation; DNA-binding; Gastrulation;
KW   Immunity; Nucleus; Transcription; Transcription regulation.
FT   CHAIN         1    707       Eomesodermin homolog.
FT                                /FTId=PRO_0000184460.
FT   DNA_BIND    278    458       T-box.
FT   REGION      592    707       Required for transcription activation (By
FT                                similarity).
FT   COMPBIAS     27    266       Gly-rich.
FT   VAR_SEQ     463    481       Missing (in isoform 2).
FT                                /FTId=VSP_038806.
FT   CONFLICT    144    144       E -> D (in Ref. 3; BAC40968).
FT   CONFLICT    159    159       A -> T (in Ref. 3; BAC40968).
FT   CONFLICT    178    178       V -> G (in Ref. 1; BAA83416).
SQ   SEQUENCE   707 AA;  74801 MW;  277AA462E214A927 CRC64;
     MQLGEQLLVS SVNLPGAHFY SLESARGGGG GGGGGGGGGG GSVSLLPGAA PSPQRLDLDK
     ASKKFPGSLP CQAGSAEPAG AGAGAPAAML SDADAGDTFG STSAVAKPGP PDGRKGSPCA
     EEELPSAATA AATARYSMDS LSSERYYLPS PGPQGSELAA PCSLFQYPAA AGAAHGPVYP
     ASNGARYPYG SMLPPGGFPA AVCPPARAQF GPAAGSGSGA GSSGGGAGGP GAYPYGQGSP
     LYGPYAGTSA AGSCGGLGGL GVPGSGFRAH VYLCNRPLWL KFHRHQTEMI ITKQGRRMFP
     FLSFNINGLN PTAHYNVFVE VVLADPNHWR FQGGKWVTCG KADNNMQGNK MYVHPESPNT
     GSHWMRQEIS FGKLKLTNNK GANNNNTQMI VLQSLHKYQP RLHIVEVTED GVEDLNEPSK
     TQTFTFSETQ FIAVTAYQNT DITQLKIDHN PFAKGFRDNY DSMYTASEND RLTPSPTDSP
     RSHQIVPGGR YGVQNFFPEP FVNTLPQARY YNGERTVPQT NGLLSPQQSE EVANPPQRWL
     VTPVQQPVTN KLDIGSYESE YTSSTLLPYG IKSLPLQTSH ALGYYPDPTF PAMAGWGGRG
     AYQRKMAAGL PWTSRMSPPV FPEDQLAKEK VKEEISSSWI ETPPSIKSLD SSDSGVYNSA
     CKRKRLSPST PSNGNSPPIK CEDINTEEYS KDTSKGMGAY YAFYTSP
//
ID   REPS1_MOUSE             Reviewed;         795 AA.
AC   O54916; Q3UAM3; Q5PPQ9; Q8C9J9; Q99LR8;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 2.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=RalBP1-associated Eps domain-containing protein 1;
DE   AltName: Full=RalBP1-interacting protein 1;
GN   Name=Reps1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND CHARACTERIZATION.
RC   TISSUE=Muscle;
RX   MEDLINE=98058900; PubMed=9395447; DOI=10.1074/jbc.272.50.31230;
RA   Yamaguchi A., Urano T., Goi T., Feig L.A.;
RT   "An eps homology (EH) domain protein that binds to the ral-GTPase
RT   target, RalBP1.";
RL   J. Biol. Chem. 272:31230-31234(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 39-795 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 499-795 (ISOFORM 1).
RC   TISSUE=Embryo, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186 AND SER-708, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-561 AND SER-708, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   STRUCTURE BY NMR OF 279-370.
RX   MEDLINE=21285759; PubMed=11389591; DOI=10.1021/bi002700m;
RA   Kim S., Cullis D.N., Feig L.A., Baleja J.D.;
RT   "Solution structure of the Reps1 EH domain and characterization of its
RT   binding to NPF target sequences.";
RL   Biochemistry 40:6776-6785(2001).
CC   -!- FUNCTION: May coordinate the cellular actions of activated EGF
CC       receptors and Ral-GTPases.
CC   -!- SUBUNIT: Homodimer (Potential). Interacts with RALBP1, CRK and
CC       GRB2. Binding to RALBP1 does not affect its Ral-binding activity.
CC       Forms a complex with the SH3 domains of CRK and GRB2 which may
CC       link it to an EGF-responsive tyrosine kinase. Interacts with
CC       RAB11FIP2 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=O54916-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O54916-2; Sequence=VSP_038337, VSP_007956, VSP_007957;
CC         Note=Due to intron retention. No experimental confirmation
CC         available;
CC       Name=3;
CC         IsoId=O54916-3; Sequence=VSP_038336, VSP_038338;
CC       Name=4;
CC         IsoId=O54916-4; Sequence=VSP_038336;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined. The highest
CC       level expression was found in the kidney and testis.
CC   -!- PTM: EGF stimulates phosphorylation on Tyr-residues.
CC   -!- SIMILARITY: Contains 1 EF-hand domain.
CC   -!- SIMILARITY: Contains 2 EH domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE29439.1; Type=Erroneous initiation;
CC       Sequence=BAE30291.1; Type=Erroneous initiation;
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DR   EMBL; AF031939; AAB94736.1; -; mRNA.
DR   EMBL; AK150284; BAE29439.1; ALT_INIT; mRNA.
DR   EMBL; AK151309; BAE30291.1; ALT_INIT; mRNA.
DR   EMBL; AK041967; BAC31117.1; -; mRNA.
DR   EMBL; AC153433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC002256; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC087547; AAH87547.1; -; mRNA.
DR   IPI; IPI00119795; -.
DR   IPI; IPI00338228; -.
DR   IPI; IPI00880345; -.
DR   IPI; IPI00918818; -.
DR   PIR; T09173; T09173.
DR   RefSeq; NP_001104535.1; NM_001111065.1.
DR   RefSeq; NP_033074.2; NM_009048.2.
DR   UniGene; Mm.4479; -.
DR   PDB; 1FI6; NMR; -; A=279-370.
DR   PDBsum; 1FI6; -.
DR   ProteinModelPortal; O54916; -.
DR   SMR; O54916; 3-88, 279-370.
DR   IntAct; O54916; 1.
DR   STRING; O54916; -.
DR   PhosphoSite; O54916; -.
DR   PRIDE; O54916; -.
DR   Ensembl; ENSMUST00000020001; ENSMUSP00000020001; ENSMUSG00000019854.
DR   GeneID; 19707; -.
DR   KEGG; mmu:19707; -.
DR   UCSC; uc007ema.1; mouse.
DR   CTD; 19707; -.
DR   MGI; MGI:1196373; Reps1.
DR   eggNOG; roNOG13234; -.
DR   GeneTree; ENSGT00530000063792; -.
DR   HOGENOM; HBG506816; -.
DR   HOVERGEN; HBG056372; -.
DR   InParanoid; O54916; -.
DR   OMA; PSLNQTW; -.
DR   OrthoDB; EOG4Z36D5; -.
DR   ArrayExpress; O54916; -.
DR   Bgee; O54916; -.
DR   CleanEx; MM_REPS1; -.
DR   Genevestigator; O54916; -.
DR   GermOnline; ENSMUSG00000019854; Mus musculus.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR000261; EPS15_homology.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   SMART; SM00027; EH; 2.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS50031; EH; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Coiled coil;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1    795       RalBP1-associated Eps domain-containing
FT                                protein 1.
FT                                /FTId=PRO_0000073830.
FT   DOMAIN       10    113       EH 1.
FT   DOMAIN      285    374       EH 2.
FT   DOMAIN      318    353       EF-hand.
FT   CA_BIND     331    342       Potential.
FT   REGION      651    795       Interaction with RALBP1.
FT   COILED      750    790       Potential.
FT   COMPBIAS    540    603       Pro-rich.
FT   MOD_RES     118    118       Phosphoserine (By similarity).
FT   MOD_RES     162    162       Phosphoserine (By similarity).
FT   MOD_RES     166    166       Phosphoserine (By similarity).
FT   MOD_RES     170    170       Phosphoserine (By similarity).
FT   MOD_RES     173    173       Phosphothreonine (By similarity).
FT   MOD_RES     174    174       Phosphoserine (By similarity).
FT   MOD_RES     186    186       Phosphoserine.
FT   MOD_RES     272    272       Phosphoserine.
FT   MOD_RES     288    288       Phosphotyrosine (Potential).
FT   MOD_RES     307    307       Phosphoserine (By similarity).
FT   MOD_RES     392    392       Phosphoserine (By similarity).
FT   MOD_RES     481    481       Phosphothreonine (By similarity).
FT   MOD_RES     489    489       Phosphoserine (By similarity).
FT   MOD_RES     534    534       Phosphoserine (By similarity).
FT   MOD_RES     536    536       Phosphoserine (By similarity).
FT   MOD_RES     538    538       Phosphothreonine (By similarity).
FT   MOD_RES     539    539       Phosphoserine (By similarity).
FT   MOD_RES     561    561       Phosphoserine.
FT   MOD_RES     708    708       Phosphoserine.
FT   MOD_RES     750    750       Phosphoserine (By similarity).
FT   VAR_SEQ       1    244       Missing (in isoform 2).
FT                                /FTId=VSP_038337.
FT   VAR_SEQ       1     52       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_038336.
FT   VAR_SEQ     420    454       QWETFSERSSSSQTLTQFDSNIAPADPDTAIVHPV -> VS
FT                                KTSLSLLEISLFTGRSFKQDRFTAGYLQYAHTP (in
FT                                isoform 2).
FT                                /FTId=VSP_007956.
FT   VAR_SEQ     420    446       Missing (in isoform 3).
FT                                /FTId=VSP_038338.
FT   VAR_SEQ     455    795       Missing (in isoform 2).
FT                                /FTId=VSP_007957.
FT   CONFLICT    161    161       V -> A (in Ref. 1; AAB94736).
FT   CONFLICT    605    605       D -> N (in Ref. 2; BAE29439).
FT   CONFLICT    701    701       P -> T (in Ref. 2; BAE29439).
FT   HELIX       283    293
FT   TURN        294    296
FT   STRAND      303    305
FT   HELIX       306    316
FT   HELIX       320    330
FT   STRAND      335    339
FT   HELIX       340    355
SQ   SEQUENCE   795 AA;  86519 MW;  98D788160F560509 CRC64;
     MEGLTLSDAE QKYYSDLFSY CDIESTKKVV VNGRVLELFR AAQLPNDVVL QIMELCGATR
     LGYFGRSQFY IALKLVAVAQ SGFPLRVESI NTVKDLPLPR FVASKNEQES RLAASYSSDS
     ENQGSYSGVI PPPPGRGQVK KGPGSHDAVQ PRPSAEQQEP VSPVVSPQQS PPTSPHTWRK
     HSRHPSGGNS ERPLTGPGPF WSPFGDAQAG SSAGDAVWSG QSPPPPQDNW VSFADTPPTS
     ALLTMHPASV QDQTTVRTVA SAATANEIRR QSSSYEDPWK ITDEQRQYYV NQFKTIQPDL
     NGFIPGSAAK EFFTKSKLPI LELSHIWELS DFDKDGALTL DEFCAAFHLV VARKNGYDLP
     EKLPESLMPK LIDLEDSADV GEQPGEVGYS GSPAEAPPSK SPSMPSLNQT WPELNQSSEQ
     WETFSERSSS SQTLTQFDSN IAPADPDTAI VHPVPIRMTP SKIHMQEMEL KRTSSDHTNP
     TSPLLVKPSD LSEENKINSS VKFPSGNTVD GYSSSDSFPS DPEQIGSSVT RQRSHSGTSP
     DNTAPPPPPP RPQPSHSRSS SLDMNRTFAV TTGQQQAGVV AHPPAVPPRP QPSQAPGPSV
     HRPVDADGLI THTSTSPQQI PEQPNFADFS QFEVFAASNV SEEQDSEAEK HPEVLPAEKA
     SDPSSSLRAA QADSKAEEKT ATNVPANVSK GTTPLAPPPK PVRRRLKSED ELRPDVDEHT
     QKTGVLAAVL TSQPSIPRSV GKDKKAIQAS IRRNKETNTV LARLNSELQQ QLKDVLEERI
     SLEVQLEQLR PFSHL
//
ID   NLK_MOUSE               Reviewed;         527 AA.
AC   O54949; Q5SYE6; Q6PF98;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 2.
DT   08-FEB-2011, entry version 94.
DE   RecName: Full=Serine/threonine-protein kinase NLK;
DE            EC=2.7.11.24;
DE   AltName: Full=Nemo-like kinase;
GN   Name=Nlk;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF
RP   LYS-167 AND THR-298.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=98115857; PubMed=9448268; DOI=10.1073/pnas.95.3.963;
RA   Brott B.K., Pinsky B.A., Erikson R.L.;
RT   "Nlk is a murine protein kinase related to Erk/MAP kinases and
RT   localized in the nucleus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:963-968(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION.
RX   PubMed=11745377;
RX   DOI=10.1002/1521-4141(200112)31:12<3580::AID-IMMU3580>3.0.CO;2-N;
RA   Kortenjann M., Nehls M., Smith A.J., Carsetti R., Schuler J.,
RA   Kohler G., Boehm T.;
RT   "Abnormal bone marrow stroma in mice deficient for nemo-like kinase,
RT   Nlk.";
RL   Eur. J. Immunol. 31:3580-3587(2001).
RN   [5]
RP   FUNCTION.
RX   PubMed=14720327; DOI=10.1111/j.1349-7006.2004.tb03170.x;
RA   Yasuda J., Yokoo H., Yamada T., Kitabayashi I., Sekiya T.,
RA   Ichikawa H.;
RT   "Nemo-like kinase suppresses a wide range of transcription factors,
RT   including nuclear factor-kappaB.";
RL   Cancer Sci. 95:52-57(2004).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH STAT3.
RX   PubMed=15004007; DOI=10.1101/gad.1166904;
RA   Ohkawara B., Shirakabe K., Hyodo-Miura J., Matsuo R., Ueno N.,
RA   Matsumoto K., Shibuya H.;
RT   "Role of the TAK1-NLK-STAT3 pathway in TGF-beta-mediated mesoderm
RT   induction.";
RL   Genes Dev. 18:381-386(2004).
RN   [7]
RP   FUNCTION, INTERACTION WITH MYB AND HIPK2, AND MUTAGENESIS OF LYS-167
RP   AND THR-298.
RX   PubMed=15082531; DOI=10.1101/gad.1170604;
RA   Kanei-Ishii C., Ninomiya-Tsuji J., Tanikawa J., Nomura T.,
RA   Ishitani T., Kishida S., Kokura K., Kurahashi T., Ichikawa-Iwata E.,
RA   Kim Y., Matsumoto K., Ishii S.;
RT   "Wnt-1 signal induces phosphorylation and degradation of c-Myb protein
RT   via TAK1, HIPK2, and NLK.";
RL   Genes Dev. 18:816-829(2004).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH MEF2A.
RX   PubMed=17785444; DOI=10.1128/MCB.01481-07;
RA   Satoh K., Ohnishi J., Sato A., Takeyama M., Iemura S., Natsume T.,
RA   Shibuya H.;
RT   "Nemo-like kinase-myocyte enhancer factor 2A signaling regulates
RT   anterior formation in Xenopus development.";
RL   Mol. Cell. Biol. 27:7623-7630(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-298, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Role in cell fate determination, required for
CC       differentiation of bone marrow stromal cells. Acts downstream of
CC       MAP3K7 and HIPK2 to negatively regulate the canonical Wnt/beta-
CC       catenin signaling pathway and the phosphorylation and destruction
CC       of the MYB transcription factor. May suppress a wide range of
CC       transcription factors by phosphorylation of the coactivator,
CC       CREBBP. Involved in TGFbeta-mediated mesoderm induction, acting
CC       downstream of MAP3K7/TAK1 to phosphorylate STAT3.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: Activated by tyrosine and threonine
CC       phosphorylation. Activated by activin (By similarity).
CC   -!- SUBUNIT: Interacts with RNF138/NARF and TCF7L2/TCF4 (By
CC       similarity). Interacts with STAT3. Interacts with HIPK2 and MYB.
CC   -!- INTERACTION:
CC       Q9QZR5:Hipk2; NbExp=1; IntAct=EBI-366894, EBI-366905;
CC       P06876:Myb; NbExp=1; IntAct=EBI-366894, EBI-366934;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly
CC       nuclear. A smaller fraction is cytoplasmic.
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in the brain, and at
CC       lower levels in heart, kidney, lung and liver.
CC   -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC       whose phosphorylation activates the MAP kinases.
CC   -!- PTM: Dually phosphorylated on Thr-303 and Tyr-305, which activates
CC       the enzyme (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. MAP kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC24499.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF036332; AAC24499.1; ALT_INIT; mRNA.
DR   EMBL; AL591177; CAI25549.2; -; Genomic_DNA.
DR   EMBL; AL591376; CAI25549.2; JOINED; Genomic_DNA.
DR   EMBL; AL591376; CAI25603.2; -; Genomic_DNA.
DR   EMBL; AL591177; CAI25603.2; JOINED; Genomic_DNA.
DR   EMBL; BC057667; AAH57667.2; -; mRNA.
DR   EMBL; BC058652; AAH58652.2; -; mRNA.
DR   IPI; IPI00556914; -.
DR   RefSeq; NP_032728.3; NM_008702.3.
DR   UniGene; Mm.9001; -.
DR   ProteinModelPortal; O54949; -.
DR   SMR; O54949; 135-486.
DR   IntAct; O54949; 3.
DR   STRING; O54949; -.
DR   PhosphoSite; O54949; -.
DR   PRIDE; O54949; -.
DR   Ensembl; ENSMUST00000017520; ENSMUSP00000017520; ENSMUSG00000017376.
DR   GeneID; 18099; -.
DR   KEGG; mmu:18099; -.
DR   CTD; 18099; -.
DR   MGI; MGI:1201387; Nlk.
DR   eggNOG; roNOG08587; -.
DR   HOVERGEN; HBG014652; -.
DR   InParanoid; O54949; -.
DR   PhylomeDB; O54949; -.
DR   BRENDA; 2.7.11.24; 244.
DR   ArrayExpress; O54949; -.
DR   Bgee; O54949; -.
DR   CleanEx; MM_NLK; -.
DR   Genevestigator; O54949; -.
DR   GermOnline; ENSMUSG00000017376; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0004707; F:MAP kinase activity; IDA:UniProtKB.
DR   GO; GO:0042169; F:SH2 domain binding; IPI:UniProtKB.
DR   GO; GO:0008134; F:transcription factor binding; ISS:UniProtKB.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:UniProtKB.
DR   GO; GO:0030178; P:negative regulation of Wnt receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR   GO; GO:0045449; P:regulation of transcription; IMP:UniProtKB.
DR   GO; GO:0033136; P:serine phosphorylation of STAT3 protein; IDA:UniProtKB.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR003527; MAP_kinase_CS.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS01351; MAPK; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transcription;
KW   Transcription regulation; Transferase; Wnt signaling pathway.
FT   CHAIN         1    527       Serine/threonine-protein kinase NLK.
FT                                /FTId=PRO_0000186337.
FT   DOMAIN      138    427       Protein kinase.
FT   NP_BIND     144    152       ATP (By similarity).
FT   MOTIF       303    305       TXY.
FT   COMPBIAS     22     25       Poly-Ala.
FT   COMPBIAS     27     34       Poly-His.
FT   COMPBIAS     42     48       Poly-His.
FT   COMPBIAS     71     83       Poly-Ala.
FT   COMPBIAS    106    111       Poly-Ala.
FT   COMPBIAS    115    119       Poly-Ala.
FT   ACT_SITE    264    264       Proton acceptor (By similarity).
FT   BINDING     167    167       ATP.
FT   MOD_RES     298    298       Phosphothreonine.
FT   MOD_RES     303    303       Phosphothreonine (By similarity).
FT   MOD_RES     305    305       Phosphotyrosine (By similarity).
FT   MOD_RES     522    522       Phosphoserine (By similarity).
FT   MUTAGEN     167    167       K->M: Loss of activity,
FT                                autophosphorylation and failed to induce
FT                                MYB degradation.
FT   MUTAGEN     298    298       T->D,E: Loss of autophosphorylation.
FT   MUTAGEN     298    298       T->V: Loss of autophosphorylation and
FT                                failed to induce MYB degradation.
FT   CONFLICT     69     69       S -> P (in Ref. 1; AAC24499).
SQ   SEQUENCE   527 AA;  58313 MW;  CE6D5DCCB9133989 CRC64;
     MSLCGTRANA KMMAAYNGGT SAAAAGHHHH HHHHLPHLPP PHLHHHHHPQ HHLHPGSAAA
     VHPVQQHTSS AAAAAAAAAA AAAMLNPGQQ QPYFPSPAPG QAPGPAAAAP AQVQAAAAAT
     VKAHHHQHSH HPQQQLDIEP DRPIGYGAFG VVWSVTDPRD GKRVALKKMP NVFQNLVSCK
     RVFRELKMLC FFKHDNVLSA LDILQPPHID YFEEIYVVTE LMQSDLHKII VSPQPLSSDH
     VKVFLYQILR GLKYLHSAGI LHRDIKPGNL LVNSNCVLKI CDFGLARVEE LDESRHMTQE
     VVTQYYRAPE ILMGSRHYSN AIDIWSVGCI FAELLGRRIL FQAQSPIQQL DLITDLLGTP
     SLEAMRTACE GAKAHILRGP HKQPSLPVLY TLSSQATHEA VHLLCRMLVF DPSKRISAKD
     ALAHPYLDEG RLRYHTCMCK CCFSTSTGRV YTSDFEPVTN PKFDDTFEKN LSSVRQVKEI
     IHQFILEQQK GNRVPLCINP QSAAFKSFIS STVAQPSEMP PSPLVWE
//
ID   AAKG1_MOUSE             Reviewed;         330 AA.
AC   O54950; Q5PRE8;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 2.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=5'-AMP-activated protein kinase subunit gamma-1;
DE            Short=AMPK gamma1;
DE            Short=AMPK subunit gamma-1;
DE            Short=AMPKg;
GN   Name=Prkag1; Synonyms=Prkaac;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   MEDLINE=21203559; PubMed=11306812;
RA   Shamsadin R., Jantsan K., Adham I.M., Engel W.;
RT   "Cloning, organisation, chromosomal localization and expression
RT   analysis of the mouse Prkag1 gene.";
RL   Cytogenet. Cell Genet. 92:134-138(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: AMPK is responsible for the regulation of fatty acid
CC       synthesis by phosphorylation of acetyl-CoA carboxylase. Also
CC       regulates cholesterol synthesis via phosphorylation and
CC       inactivation of hydroxymethylglutaryl-CoA reductase and hormone-
CC       sensitive lipase. This is a regulatory subunit.
CC   -!- SUBUNIT: Heterotrimer of an alpha catalytic subunit, a beta and a
CC       gamma non-catalytic regulatory subunits. Interacts with FNIP1 and
CC       FNIP2 (By similarity).
CC   -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase gamma
CC       subunit family.
CC   -!- SIMILARITY: Contains 4 CBS domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF036535; AAB95475.1; -; mRNA.
DR   EMBL; BC086660; AAH86660.1; -; mRNA.
DR   IPI; IPI00119930; -.
DR   RefSeq; NP_058061.2; NM_016781.2.
DR   UniGene; Mm.6670; -.
DR   ProteinModelPortal; O54950; -.
DR   SMR; O54950; 23-326.
DR   MINT; MINT-4583597; -.
DR   STRING; O54950; -.
DR   PhosphoSite; O54950; -.
DR   PRIDE; O54950; -.
DR   Ensembl; ENSMUST00000088285; ENSMUSP00000085623; ENSMUSG00000067713.
DR   GeneID; 19082; -.
DR   KEGG; mmu:19082; -.
DR   UCSC; uc007xoa.1; mouse.
DR   CTD; 19082; -.
DR   MGI; MGI:108411; Prkag1.
DR   eggNOG; roNOG13288; -.
DR   HOGENOM; HBG446629; -.
DR   HOVERGEN; HBG050431; -.
DR   InParanoid; O54950; -.
DR   OMA; KLFIAEF; -.
DR   OrthoDB; EOG45DWPQ; -.
DR   PhylomeDB; O54950; -.
DR   NextBio; 295618; -.
DR   ArrayExpress; O54950; -.
DR   Bgee; O54950; -.
DR   Genevestigator; O54950; -.
DR   GermOnline; ENSMUSG00000067713; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0004679; F:AMP-activated protein kinase activity; TAS:MGI.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006950; P:response to stress; TAS:MGI.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000644; Cysta_beta_synth_core.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 2.
DR   Pfam; PF00571; CBS; 3.
DR   SMART; SM00116; CBS; 4.
DR   PROSITE; PS51371; CBS; 4.
PE   2: Evidence at transcript level;
KW   Acetylation; CBS domain; Fatty acid biosynthesis; Lipid synthesis;
KW   Repeat.
FT   CHAIN         1    330       5'-AMP-activated protein kinase subunit
FT                                gamma-1.
FT                                /FTId=PRO_0000204378.
FT   DOMAIN       42    102       CBS 1.
FT   DOMAIN      124    186       CBS 2.
FT   DOMAIN      197    259       CBS 3.
FT   DOMAIN      271    328       CBS 4.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     263    263       N6-acetyllysine (By similarity).
FT   CONFLICT     80     80       S -> C (in Ref. 1; AAB95475).
FT   CONFLICT    137    137       L -> S (in Ref. 1; AAB95475).
FT   CONFLICT    180    180       T -> I (in Ref. 1; AAB95475).
FT   CONFLICT    320    320       A -> D (in Ref. 1; AAB95475).
SQ   SEQUENCE   330 AA;  37520 MW;  539F70EC8819C34D CRC64;
     MESVAAESSP ALENEHFQET PESNNSVYTS FMKSHRCYDL IPTSSKLVVF DTSLQVKKAF
     FALVTNGVRA APLWDSKKQS FVGMLTITDF INILHRYYKS ALVQIYELEE HKIETWREVY
     LQDSFKPLVC ISPNASLFDA VSSLIRNKIH RLPVIDPESG NTLYILTHKR ILKFLKLFIT
     EFPKPEFMSK SLQELQIGTY ANIAMVRTTT PVYVALGIFV QHRVSALPVV DEKGRVVDIY
     SKFDVINLAA EKTYNNLDVS VTKALQHRSH YFEGVLKCYL HETLETIINR LVEAEVHRLV
     VVDEHDVVKG IVSLSDILQA LVLTGGEKKP
//
ID   SEM6B_MOUSE             Reviewed;         886 AA.
AC   O54951;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Semaphorin-6B;
DE   AltName: Full=Semaphorin VIB;
DE            Short=Sema VIB;
DE   AltName: Full=Semaphorin-N;
DE            Short=Sema N;
DE   Flags: Precursor;
GN   Name=Sema6b; Synonyms=Seman;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98027184; PubMed=9361278; DOI=10.1006/mcne.1997.0644;
RA   Eckhardt F., Behar O., Calautti E., Yonezawa K., Nishimoto I.,
RA   Fishman M.C.;
RT   "A novel transmembrane semaphorin can bind c-src.";
RL   Mol. Cell. Neurosci. 9:409-419(1997).
CC   -!- SUBUNIT: Homodimer. Binds specifically the SH3 domain of the
CC       protooncogene C-SRC.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: During development it is expressed in
CC       subregions of the nervous system and is particularly prominent in
CC       muscle. In adulthood, it is expressed ubiquitously.
CC   -!- SIMILARITY: Belongs to the semaphorin family.
CC   -!- SIMILARITY: Contains 1 PSI domain.
CC   -!- SIMILARITY: Contains 1 Sema domain.
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DR   EMBL; AF036585; AAC00493.1; -; mRNA.
DR   IPI; IPI00119931; -.
DR   RefSeq; NP_001123928.1; NM_001130456.1.
DR   RefSeq; NP_038690.1; NM_013662.2.
DR   UniGene; Mm.8029; -.
DR   ProteinModelPortal; O54951; -.
DR   SMR; O54951; 28-576.
DR   STRING; O54951; -.
DR   PRIDE; O54951; -.
DR   Ensembl; ENSMUST00000001256; ENSMUSP00000001256; ENSMUSG00000001227.
DR   GeneID; 20359; -.
DR   KEGG; mmu:20359; -.
DR   UCSC; uc008dbc.1; mouse.
DR   CTD; 20359; -.
DR   MGI; MGI:1202889; Sema6b.
DR   eggNOG; roNOG08885; -.
DR   HOGENOM; HBG713978; -.
DR   HOVERGEN; HBG072910; -.
DR   InParanoid; O54951; -.
DR   OMA; KRLPTPH; -.
DR   OrthoDB; EOG4GTKCC; -.
DR   PhylomeDB; O54951; -.
DR   NextBio; 298241; -.
DR   ArrayExpress; O54951; -.
DR   Bgee; O54951; -.
DR   Genevestigator; O54951; -.
DR   GermOnline; ENSMUSG00000001227; Mus musculus.
DR   GermOnline; ENSMUSG00000073381; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004872; F:receptor activity; IEA:InterPro.
DR   GO; GO:0030215; F:semaphorin receptor binding; IPI:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   InterPro; IPR003659; Plexin-like.
DR   InterPro; IPR016201; Plexin-like_fold.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR001627; Semaphorin/CD100_Ag.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF01437; PSI; 1.
DR   Pfam; PF01403; Sema; 1.
DR   SMART; SM00423; PSI; 1.
DR   SMART; SM00630; Sema; 1.
DR   SUPFAM; SSF103575; Plexin-like_fold; 1.
DR   SUPFAM; SSF101912; Sema; 1.
DR   PROSITE; PS51004; SEMA; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW   Membrane; Neurogenesis; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     26       Potential.
FT   CHAIN        27    886       Semaphorin-6B.
FT                                /FTId=PRO_0000032342.
FT   TOPO_DOM     27    605       Extracellular (Potential).
FT   TRANSMEM    606    626       Helical; (Potential).
FT   TOPO_DOM    627    886       Cytoplasmic (Potential).
FT   DOMAIN       32    525       Sema.
FT   COMPBIAS    751    754       Poly-Leu.
FT   CARBOHYD     75     75       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    156    156       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    292    292       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    387    387       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    442    442       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    463    463       N-linked (GlcNAc...) (Potential).
FT   DISULFID    117    127       By similarity.
FT   DISULFID    145    154       By similarity.
FT   DISULFID    268    379       By similarity.
FT   DISULFID    293    338       By similarity.
SQ   SEQUENCE   886 AA;  95467 MW;  E5F56D125CDA574D CRC64;
     MWTPRVPPPR PALSFFLLLL LGVTYGLFPE EPPPLSVAPR DYLSHYPVFV GSGPGRLTAA
     EGAEDLNIQR VLRVNRTLFI GDRDNLYQVE LEPSTSTELR YQRKLTWRSN PSDIDVCRMK
     GKQEGECRNF VKVLLLRDES TLFVCGSNAF NPICANYSMD TLQLLGDSIS GMARCPYDPK
     HANVALFSDG MLFTATVTDF LAIDAVIYRS LGDRPTLRTV KHDSKWFKEP YFVHAVEWGS
     HVYFFFREIA MEFNYLEKVV VSRVARVCKN DVGGSPRVLE KQWTSFLKAR LNCSVPGDSH
     FYFNVLQAVT GVVSLGGRPV ILAVFSTPSN SIPGSAVCAF DMNQVAAVFE GRFREQKSPE
     SIWTPVPEDQ VPRPRPGCCA APGMQYNASS ALPDEILNFV KTHPLMDEAV PSLGHSPWIV
     RTLMRHQLTR VAVDVGAGPW GNQTIVFLGS EAGTVLKFLV KPNASVSGTT GPSIFLEEFE
     TYRPDRCGRP SSAGEWGQRL LSLELDAASG GLLAAFPRCV VRVPVARCQL YSGCMKNCIG
     SQDPYCGWAP DGSCIFLRPG TSATFEQDVS GASTSGLGDC TGLLRASLSD DRAGLVSVNL
     LVTSSVAAFV VGAVVSGFSV GWFVGLRERR ELARRKDKEA ILAHGGSEAV LSVSRLGERR
     GTGPGGRGGA GGGPGGPPEA LLAPLMQNGW TKAALLHGGP HDLDTGLLPT PEQTPLPQKR
     LPTPHPHAHA LGSRAWDHSH ALLSASASTS LLLLAPARAS EQPQVPAEPG PESRLCAPRS
     CRASHPGDFP LTPHASPDRR RVVSAPTGPL DPSVGDGLPG PWSPPATSSL RRPGPHGPPT
     AALRRTHTFN SGEARPGGHR PRRHPPADST HLLPCGTGER TAPPVP
//
ID   SLK_MOUSE               Reviewed;        1233 AA.
AC   O54988; A2RRK4; Q80U65; Q8CAU2; Q8CDW2; Q9WU41;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=STE20-like serine/threonine-protein kinase;
DE            Short=STE20-like kinase;
DE            Short=mSLK;
DE            EC=2.7.11.1;
DE   AltName: Full=Etk4;
DE   AltName: Full=STE20-related kinase SMAK;
DE   AltName: Full=STE20-related serine/threonine-protein kinase;
DE            Short=STE20-related kinase;
DE   AltName: Full=Serine/threonine-protein kinase 2;
GN   Name=Slk; Synonyms=Kiaa0204, Stk2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
RP   PHOSPHORYLATION, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX   PubMed=9808774; DOI=10.1006/abbi.1998.0907;
RA   Pytowski B., Hicklin D.J., Kornhaber G., Dellaratta D.V., Witte L.;
RT   "Identification and initial characterization of mSLK, a murine member
RT   of the STE20 family of kinases.";
RL   Arch. Biochem. Biophys. 359:310-319(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, CLEAVAGE
RP   BY CASPASE-3, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   ASP-436.
RC   STRAIN=BALB/c;
RX   MEDLINE=20079281; PubMed=10611247; DOI=10.1128/MCB.20.2.684-696.2000;
RA   Sabourin L.A., Seale P., Wagner J., Rudnicki M.A.;
RT   "Caspase 3 cleavage of the Ste20-related kinase SLK releases and
RT   activates an apoptosis-inducing kinase domain and an actin-
RT   disassembling region.";
RL   Mol. Cell. Biol. 20:684-696(2000).
RN   [3]
RP   ERRATUM.
RA   Sabourin L.A., Seale P., Wagner J., Rudnicki M.A.;
RL   Mol. Cell. Biol. 20:2949-2949(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-784 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J; TISSUE=Testis, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 157-201, AND TISSUE SPECIFICITY.
RX   PubMed=8346215; DOI=10.1073/pnas.90.15.7044;
RA   Biesecker L.G., Gottschalk L.R., Emerson S.G.;
RT   "Identification of four murine cDNAs encoding putative protein kinases
RT   from primitive embryonic stem cells differentiated in vitro.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:7044-7048(1993).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189; SER-543 AND
RP   SER-777, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND SER-348, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Mediates apoptosis and actin stress fiber dissolution.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O54988-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O54988-2; Sequence=VSP_018101;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- DEVELOPMENTAL STAGE: Ubiquitously expressed from day 7 to 17 dpc.
CC   -!- PTM: Proteolytically cleaved by caspase-3.
CC   -!- PTM: Autophosphorylated. Phosphorylated upon DNA damage, probably
CC       by ATM or ATR.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 UVR domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65500.1; Type=Erroneous initiation;
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DR   EMBL; AF039574; AAB96682.1; -; mRNA.
DR   EMBL; AF112855; AAD28717.1; -; mRNA.
DR   EMBL; AK037798; BAC29874.1; -; mRNA.
DR   EMBL; AK122218; BAC65500.1; ALT_INIT; mRNA.
DR   EMBL; BC131675; AAI31676.1; -; mRNA.
DR   EMBL; AK029491; BAC26474.1; -; mRNA.
DR   IPI; IPI00331076; -.
DR   IPI; IPI00749669; -.
DR   PIR; T14157; T14157.
DR   RefSeq; NP_001158111.1; NM_001164639.1.
DR   RefSeq; NP_033315.2; NM_009289.3.
DR   UniGene; Mm.281011; -.
DR   ProteinModelPortal; O54988; -.
DR   SMR; O54988; 21-308.
DR   STRING; O54988; -.
DR   PhosphoSite; O54988; -.
DR   PRIDE; O54988; -.
DR   Ensembl; ENSMUST00000026043; ENSMUSP00000026043; ENSMUSG00000025060.
DR   Ensembl; ENSMUST00000051691; ENSMUSP00000049977; ENSMUSG00000025060.
DR   GeneID; 20874; -.
DR   KEGG; mmu:20874; -.
DR   UCSC; uc008hvf.1; mouse.
DR   UCSC; uc008hvg.1; mouse.
DR   CTD; 20874; -.
DR   MGI; MGI:103241; Slk.
DR   GeneTree; ENSGT00600000084124; -.
DR   HOGENOM; HBG444013; -.
DR   HOVERGEN; HBG052712; -.
DR   InParanoid; O54988; -.
DR   OMA; NKLIKSE; -.
DR   OrthoDB; EOG40K7ZB; -.
DR   PhylomeDB; O54988; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 299723; -.
DR   PMAP-CutDB; O54988; -.
DR   ArrayExpress; O54988; -.
DR   Bgee; O54988; -.
DR   CleanEx; MM_SLK; -.
DR   Genevestigator; O54988; -.
DR   GermOnline; ENSMUSG00000025060; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004518; F:nuclease activity; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR022165; PKK.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   InterPro; IPR001943; UvrB/C.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF12474; PKK; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50151; UVR; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; ATP-binding; Coiled coil; Cytoplasm;
KW   Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1   1233       STE20-like serine/threonine-protein
FT                                kinase.
FT                                /FTId=PRO_0000233240.
FT   DOMAIN       34    292       Protein kinase.
FT   DOMAIN      873    908       UVR.
FT   NP_BIND      40     48       ATP (By similarity).
FT   COILED      824   1067       Potential.
FT   COILED     1107   1181       Potential.
FT   COMPBIAS     16     19       Poly-Lys.
FT   COMPBIAS    302    681       Glu-rich.
FT   ACT_SITE    155    155       Proton acceptor (By similarity).
FT   BINDING      63     63       ATP (By similarity).
FT   SITE        436    437       Cleavage; by caspase-3 (Probable).
FT   MOD_RES     181    181       Phosphothreonine (By similarity).
FT   MOD_RES     189    189       Phosphoserine.
FT   MOD_RES     340    340       Phosphoserine (By similarity).
FT   MOD_RES     341    341       Phosphoserine (By similarity).
FT   MOD_RES     344    344       Phosphoserine (By similarity).
FT   MOD_RES     347    347       Phosphoserine (By similarity).
FT   MOD_RES     348    348       Phosphoserine.
FT   MOD_RES     354    354       Phosphoserine.
FT   MOD_RES     370    370       Phosphoserine (By similarity).
FT   MOD_RES     542    542       Phosphoserine (By similarity).
FT   MOD_RES     543    543       Phosphoserine.
FT   MOD_RES     561    561       Phosphoserine (By similarity).
FT   MOD_RES     566    566       Phosphoserine (By similarity).
FT   MOD_RES     753    753       Phosphothreonine (By similarity).
FT   MOD_RES     770    770       Phosphoserine (By similarity).
FT   MOD_RES     775    775       Phosphoserine (By similarity).
FT   MOD_RES     777    777       Phosphoserine.
FT   MOD_RES     812    812       Phosphothreonine (By similarity).
FT   MOD_RES     816    816       Phosphoserine (By similarity).
FT   MOD_RES    1095   1095       Phosphothreonine (By similarity).
FT   MOD_RES    1233   1233       Phosphoserine (By similarity).
FT   VAR_SEQ     927    957       Missing (in isoform 2).
FT                                /FTId=VSP_018101.
FT   MUTAGEN     436    436       D->N: No change in caspase-3-induced
FT                                cleavage product.
FT   CONFLICT    164    164       T -> N (in Ref. 7).
FT   CONFLICT    574    574       A -> V (in Ref. 1; AAB96682).
FT   CONFLICT   1098   1098       Q -> K (in Ref. 2; BAC29874).
SQ   SEQUENCE   1233 AA;  141457 MW;  B1A5230666C58A73 CRC64;
     MSFFNFRKIF KLGSEKKKKQ YEHVKRDLNP EEFWEIIGEL GDGAFGKVYK AQNKETNVLA
     AAKVIDTKSE EELEDYMVEI DILASCDHPN IVKLLDAFYY ENNLWILIEF CAGGAVDAVM
     LELERPLTES QIQVVCKQTL EALNYLHDNK IIHRDLKAGN ILFTLDGDIK LADFGVSAKN
     TRTIQRRDSF IGTPYWMAPE VVMCETSKDR PYDYKADVWS LGITLIEMAE IEPPHHELNP
     MRVLLKIAKS EPPTLAQPSK WSSNFKDFLR KCLEKNVDAR WTTSQLLQHP FVTVDSNKPV
     RELIAEAKAE VTEEVEDGKE EDEEEEAENA LPIPANKRAS SDLSIASSEE DKLSQNACIL
     ESVSERTEQS TSEDKFSNKI LNEKPTTDGP EKAVDEHASD VNLETGAELN DQTVGIHENG
     REKKRPKLEN LPDTQDQQTV DVNSVSEENE NNRVTLETNT DCLKPEEDRN KENQETLESK
     LIQSEEINDT HIQTMDLVSQ ETGEKEADFQ AVDNEVGLTK EETQEKLGKD GTAQKVITSD
     RSSEVGTDEA LDDTQKAAEL SKAAQSGEGD EALAPTQTLA EKPTEGPEAG GAEEEPPGGE
     RVEDKQPEQQ PAVCEAEGQL TSTSETTRAT LEQPETDEVE QVSESNSIEE LERLVVTGAE
     ARALGSEGEA AATEVDLERK ENAQKVPVKA ESQAPAASQP SEPHPVLIPS ININSETTEN
     KEEMGALPKP ETILPPEPEH EKGNDTDSGT GSTVENSSGD LNLSISSFLS KAKDSGSVSL
     QETRRQKKTL KKTRKFIVDG VEVSVTTSKI VTDSDSKTEE LRFLRRQELR ELRLLQKEEQ
     RAQQQLNGKL QQQREQIFRR FEQEMLSKKR QYDQEIENLE KQQKQTIERL EQEHTNRLRD
     EAKRIKGEQE KELSKFQNVL KNRKKEVMNE VEKAPRELRR ELTKRRKEEL AQSQHAQEQE
     FVQKQQQELD GSLKKIIQQQ KAELANIERE CLNNKQQLMR AREAAIWELE ERHLQEKHQL
     LKQQLKDQYF MQRHQLLKRH EKETEQMQRY NQRLIEELKN RQTQERARLP KIQRSEAKTR
     MAMFKKSLRI NSTATPDQDR EKIKQFAAQE EKRQKNERMA QHQKHESQMR DLQLQCEANV
     RELHQLQNEK CHLLVEHETQ KLKELDEEHS QELKEWREKL RPRKKTLEEE FARKLQEQEV
     FFKMTGESEC LNPSAQSRIS KFYPIPTLHS TGS
//
ID   CNTP1_MOUSE             Reviewed;        1385 AA.
AC   O54991;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   08-MAR-2011, entry version 100.
DE   RecName: Full=Contactin-associated protein 1;
DE            Short=Caspr;
DE            Short=Caspr1;
DE   AltName: Full=MHDNIV;
DE   AltName: Full=NCP1;
DE   AltName: Full=Neurexin IV;
DE   AltName: Full=Neurexin-4;
DE   AltName: Full=Paranodin;
DE   Flags: Precursor;
GN   Name=Cntnap1; Synonyms=Nrxn4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND POSSIBLE FUNCTION.
RX   MEDLINE=21289247; PubMed=11395000; DOI=10.1016/S0896-6273(01)00294-X;
RA   Bhat M.A., Rios J.C., Lu Y., Garcia-Fresco G.P., Ching W.,
RA   St Martin M., Li J., Einheber S., Chesler M., Rosenbluth J.,
RA   Salzer J.L., Bellen H.J.;
RT   "Axon-glia interactions and the domain organization of myelinated
RT   axons requires neurexin IV/Caspr/Paranodin.";
RL   Neuron 30:369-383(2001).
RN   [2]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=21403569; PubMed=11512672; DOI=10.1007/s004410100403;
RA   Arroyo E.J., Xu T., Poliak S., Watson M., Peles E., Scherer S.S.;
RT   "Internodal specializations of myelinated axons in the central nervous
RT   system.";
RL   Cell Tissue Res. 305:53-66(2001).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1384, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Seems to play a role in the formation of functional
CC       distinct domains critical for saltatory conduction of nerve
CC       impulses in myelinated nerve fibers. Seems to demarcate the
CC       paranodal region of the axo-glial junction. In association with
CC       contactin may have a role in the signaling between axons and
CC       myelinating glial cells. Mice that lack CNTAP1 exhibit tremor,
CC       ataxia, and significant motor paresis. Normal paranodal junctions
CC       fail to form, and the organization of the paranodal loops is
CC       disrupted. Contactin is undetectable in the paranodes, and
CC       potassium channels are displaced from the juxtaparanodal into the
CC       paranodal domains. Also results in a severe decrease in peripheral
CC       nerve conduction velocity.
CC   -!- SUBUNIT: Interacts with contactin in cis form (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- TISSUE SPECIFICITY: Expressed in brain. In myelinated nerve fibers
CC       predominantly found in paranodal axoglial junctions. In the
CC       internodal region of myelinated axons in the CNS and the PNS also
CC       found as a thin line apposing the inner mesaxon of the myelin
CC       sheath. In PNS neurons this line forms a circumferential ring that
CC       apposes the innermost aspect of Schmidt-Lanterman incisures.
CC   -!- SIMILARITY: Belongs to the neurexin family.
CC   -!- SIMILARITY: Contains 2 EGF-like domains.
CC   -!- SIMILARITY: Contains 1 F5/8 type C domain.
CC   -!- SIMILARITY: Contains 1 fibrinogen C-terminal domain.
CC   -!- SIMILARITY: Contains 4 laminin G-like domains.
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DR   EMBL; AF039833; AAB96760.1; -; mRNA.
DR   IPI; IPI00338983; -.
DR   PIR; T14158; T14158.
DR   RefSeq; NP_058062.2; NM_016782.2.
DR   UniGene; Mm.474527; -.
DR   ProteinModelPortal; O54991; -.
DR   SMR; O54991; 22-522, 541-590, 787-945, 963-999, 1081-1219.
DR   STRING; O54991; -.
DR   PhosphoSite; O54991; -.
DR   PRIDE; O54991; -.
DR   Ensembl; ENSMUST00000103109; ENSMUSP00000099398; ENSMUSG00000017167.
DR   GeneID; 53321; -.
DR   KEGG; mmu:53321; -.
DR   UCSC; uc007lnt.1; mouse.
DR   CTD; 53321; -.
DR   MGI; MGI:1858201; Cntnap1.
DR   HOGENOM; HBG443585; -.
DR   HOVERGEN; HBG057718; -.
DR   InParanoid; O54991; -.
DR   OrthoDB; EOG40GCQ0; -.
DR   NextBio; 310125; -.
DR   ArrayExpress; O54991; -.
DR   Bgee; O54991; -.
DR   CleanEx; MM_CNTNAP1; -.
DR   Genevestigator; O54991; -.
DR   GermOnline; ENSMUSG00000017167; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0033270; C:paranode region of axon; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; EXP:Reactome.
DR   GO; GO:0005102; F:receptor binding; IEA:InterPro.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0031175; P:neuron projection development; IGI:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR000421; Coagulation_factor_5/8-type_C.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR002181; Fibrinogen_a/b/g_C.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR012680; Laminin_G_2.
DR   InterPro; IPR003585; Neurexin-like.
DR   Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 6.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF02210; Laminin_G_2; 4.
DR   SMART; SM00294; 4.1m; 1.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00231; FA58C; 1.
DR   SMART; SM00282; LamG; 4.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 4.
DR   SUPFAM; SSF56496; Fibrinogen_a/b/g_C; 1.
DR   SUPFAM; SSF49785; Gal_bind_like; 1.
DR   PROSITE; PS00022; EGF_1; FALSE_NEG.
DR   PROSITE; PS01186; EGF_2; FALSE_NEG.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01285; FA58C_1; 1.
DR   PROSITE; PS01286; FA58C_2; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
DR   PROSITE; PS00514; FIBRINOGEN_C_1; FALSE_NEG.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 4.
PE   1: Evidence at protein level;
KW   Cell adhesion; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Membrane; Phosphoprotein; Repeat; SH3-binding; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21   1385       Contactin-associated protein 1.
FT                                /FTId=PRO_0000019504.
FT   TOPO_DOM     21   1284       Extracellular (Potential).
FT   TRANSMEM   1285   1305       Helical; (Potential).
FT   TOPO_DOM   1306   1385       Cytoplasmic (Potential).
FT   DOMAIN       26    169       F5/8 type C.
FT   DOMAIN      204    356       Laminin G-like 1.
FT   DOMAIN      390    539       Laminin G-like 2.
FT   DOMAIN      545    577       EGF-like 1.
FT   DOMAIN      577    796       Fibrinogen C-terminal.
FT   DOMAIN      814    958       Laminin G-like 3.
FT   DOMAIN      962    996       EGF-like 2.
FT   DOMAIN     1089   1251       Laminin G-like 4.
FT   MOTIF      1334   1370       SH3-binding (Potential).
FT   MOD_RES    1384   1384       Phosphoserine.
FT   CARBOHYD    121    121       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    129    129       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    277    277       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    421    421       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    500    500       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    519    519       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    598    598       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    654    654       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    665    665       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    764    764       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    805    805       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    844    844       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    861    861       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    949    949       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    957    957       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1079   1079       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1148   1148       N-linked (GlcNAc...) (Potential).
FT   DISULFID     26    169       By similarity.
FT   DISULFID    324    356       By similarity.
FT   DISULFID    507    539       By similarity.
FT   DISULFID    545    556       By similarity.
FT   DISULFID    550    565       By similarity.
FT   DISULFID    567    577       By similarity.
FT   DISULFID    931    958       By similarity.
FT   DISULFID    962    975       By similarity.
FT   DISULFID    969    984       By similarity.
FT   DISULFID    986    996       By similarity.
FT   DISULFID   1210   1251       By similarity.
SQ   SEQUENCE   1385 AA;  156438 MW;  5F4FE33629E25D1D CRC64;
     MMSLRLFSIL LATVVSGAWG WGYYGCNEEL VGPLYARSLG ASSYYGLFTT ARFARLHGIS
     GWSPRIGDPN PWLQIDLMKK HRIRAVATQG AFNSWDWVTR YMLLYGDRVD SWTPFYQKGH
     NATFFGNVND SAVVRHDLHY HFTARYIRIV PLAWNPRGKI GLRLGIYGCP YTSSILYFDG
     DDAISYRFQR GASQSLWDVF AFSFKTEEKD GLLLHTEGSQ GDYVTLELQG AHLLLHMSLG
     SSPIQPRPGH TTVSLGGVLN DLSWHYVRVD RYGRDANFTL DGYAHHFVLN GDFERLNLEN
     EIFIGGLVGA ARKNLAYRHN FRGCIENVIY NRINIAEMAV MRHSRITFEG NVAFRCLDPV
     PHPINFGGPH NFVQVPGFPR RGRLAVSFRF RTWDLTGLLL FSHLGDGLGH VELMLSEGQV
     NVSIAQTGRK KLQFAAGYRL NDGFWHEVNF VAQENHAVIS IDDVEGAEVR VSYPLLIRTG
     TSYFFGGCPK PASRWGCHSN QTAFHGCMEL LKVDGQLVNL TLVEFRKLGY FAEVLFDTCG
     ITDRCSPNMC EHDGRCYQSW DDFICYCELT GYKGVTCHEP LYKESCEAYR LSGKYSGNYT
     IDPDGSGPLK PFVVYCDIRE NRAWTVVRHD RLWTTRVTGS SMDRPFLGAI QYWNASWEEV
     SALANASQHC EQWIEFSCYN SRLLNTAGSY PYSFWIGRNE EQHFYWGGSQ PGIQRCACGL
     DQSCVDPALH CNCDADQPQW RTDKGLLTFV DHLPVTQVVV GDTNRSNSEA QFFLRPLRCY
     GDRNSWNTIS FHTGAALRFP PIRANHSLDV SFYFRTSAPS GVFLENMGGP FCRWRRPYVR
     VELNTSRDVV FAFDIGNGDE NLTVHSDDFE FNDDEWHLVR AEINVKQARL RVDHRPWVLR
     PMPLQTYIWL VYDQPLYVGS AELKRRPFVG CLRAMRLNGV TLNLEGRANA SEGTFPNCTG
     HCTHPRFPCF HGGRCVERYS YYTCDCDLTA FDGPYCNHDI GGFFETGTWM RYNLQSALRS
     AAREFSHMLS RPVPGYEPGY VPGYDTPGYV PGYHGPGYRL PEYPRPGRPV PGYRGPVYNV
     TGEEVSFSFS TNSAPAVLLY VSSFVRDYMA VLIKEDGTLQ LRYQLGTSPY VYQVTRRPVT
     DGQPHSVNIT RVYRNLFIQV DYFPLTEQKF SLLVDSQLDS PKALYLGRVM ETGVIDPEIQ
     RYNTPGFSGC LSGVRFNNVA PLKTHFRTPR PMTAELAEAM RVQGELSESN CGAMPRLVSE
     VQPELDPWYL PPDFPYYHDD GWIAILLGFL VAFLLLGLVG MLVLFYLQNH RYQGSYHTNE
     PKATHHSHSG GKAPLPPSGP AQAPAPIPAP TQLPTPAPAP APAPASGPGP RDQNLPQILE
     ESRSE
//
ID   BNIP3_MOUSE             Reviewed;         187 AA.
AC   O55003; Q544Y4;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=BCL2/adenovirus E1B 19 kDa protein-interacting protein 3;
GN   Name=Bnip3; Synonyms=Nip3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99084982; PubMed=9867803; DOI=10.1074/jbc.274.1.7;
RA   Chen G., Cizeau J., Vande Velde C., Park J.H., Bozek G., Bolton J.,
RA   Shi L., Dubik D., Greenberg A.;
RT   "Nix and Nip3 form a subfamily of pro-apoptotic mitochondrial
RT   proteins.";
RL   J. Biol. Chem. 274:7-10(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-92, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-86 AND SER-88, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-85 AND SER-88,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Apoptosis-inducing protein that, which can overcome BCL2
CC       suppression. May play a role in repartitioning calcium between the
CC       two major intracellular calcium stores in association with BCL2.
CC   -!- SUBUNIT: Homodimer. Binds to BCL2. Interacts with BNIP3L and ACAA2
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). Mitochondrion
CC       membrane; Single-pass membrane protein (By similarity).
CC       Note=Colocalizes with ACAA2 in the mitochondria (By similarity).
CC   -!- SIMILARITY: Belongs to the NIP3 family.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF041054; AAD02922.1; -; mRNA.
DR   EMBL; AK014223; BAB29214.1; -; mRNA.
DR   EMBL; AK075943; BAC36072.1; -; mRNA.
DR   EMBL; AK152610; BAE31356.1; -; mRNA.
DR   EMBL; BC046603; AAH46603.1; -; mRNA.
DR   IPI; IPI00115040; -.
DR   RefSeq; NP_033890.1; NM_009760.4.
DR   UniGene; Mm.378890; -.
DR   ProteinModelPortal; O55003; -.
DR   SMR; O55003; 139-183.
DR   STRING; O55003; -.
DR   PhosphoSite; O55003; -.
DR   PRIDE; O55003; -.
DR   Ensembl; ENSMUST00000106112; ENSMUSP00000101718; ENSMUSG00000078566.
DR   GeneID; 12176; -.
DR   KEGG; mmu:12176; -.
DR   UCSC; uc009kfg.1; mouse.
DR   CTD; 12176; -.
DR   MGI; MGI:109326; Bnip3.
DR   eggNOG; roNOG16256; -.
DR   GeneTree; ENSGT00390000013415; -.
DR   HOGENOM; HBG443927; -.
DR   HOVERGEN; HBG050707; -.
DR   InParanoid; O55003; -.
DR   OMA; QTPQDIN; -.
DR   OrthoDB; EOG4T784H; -.
DR   PhylomeDB; O55003; -.
DR   NextBio; 280557; -.
DR   ArrayExpress; O55003; -.
DR   Bgee; O55003; -.
DR   CleanEx; MM_BNIP3; -.
DR   Genevestigator; O55003; -.
DR   GermOnline; ENSMUSG00000072594; Mus musculus.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0031307; C:integral to mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
DR   GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptotic nuclear change; ISS:UniProtKB.
DR   GO; GO:0006917; P:induction of apoptosis; ISS:UniProtKB.
DR   GO; GO:0045837; P:negative regulation of membrane potential; ISS:UniProtKB.
DR   GO; GO:0008634; P:negative regulation of survival gene product expression; ISS:UniProtKB.
DR   GO; GO:0051402; P:neuron apoptosis; ISS:UniProtKB.
DR   GO; GO:0006800; ?:oxygen and reactive oxygen species metabolic process; ISS:UniProtKB.
DR   GO; GO:0046902; P:regulation of mitochondrial membrane permeability; ISS:UniProtKB.
DR   GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR   InterPro; IPR010548; BNIP3.
DR   Pfam; PF06553; BNIP3; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Membrane; Mitochondrion; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    187       BCL2/adenovirus E1B 19 kDa protein-
FT                                interacting protein 3.
FT                                /FTId=PRO_0000064965.
FT   TRANSMEM    157    177       Helical; (Potential).
FT   MOD_RES      79     79       Phosphoserine.
FT   MOD_RES      85     85       Phosphoserine.
FT   MOD_RES      86     86       Phosphothreonine.
FT   MOD_RES      88     88       Phosphoserine.
FT   MOD_RES      92     92       Phosphotyrosine.
SQ   SEQUENCE   187 AA;  20978 MW;  901BCFACF43EE989 CRC64;
     MSQSGEENLQ GSWVELHFSN GNGSSVPASV SIYNGDMEKI LLDAQHESGR SSSKSSHCDS
     PPRSQTPQDT NRAEIDSHSF GEKNSTLSEE DYIERRREVE SILKKNSDWI WDWSSRPENI
     PPKEFLFKHP KRTATLSMRN TSVMKKGGIF SADFLKVFLP SLLLSHLLAI GLGIYIGRRL
     TTSTSTF
//
ID   CAC1B_MOUSE             Reviewed;        2327 AA.
AC   O55017; Q60609;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   08-MAR-2011, entry version 110.
DE   RecName: Full=Voltage-dependent N-type calcium channel subunit alpha-1B;
DE   AltName: Full=Brain calcium channel III;
DE            Short=BIII;
DE   AltName: Full=Calcium channel, L type, alpha-1 polypeptide isoform 5;
DE   AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.2;
GN   Name=Cacna1b; Synonyms=Cach5, Cacnl1a5, Cchn1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Hong T., Birnbaumer L.;
RT   "Nucleotide sequence polymorphism of mouse alpha1 B.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS NB1 AND NB2).
RC   TISSUE=Neuroblastoma;
RX   MEDLINE=94139884; PubMed=8307146; DOI=10.1016/0014-5793(94)80105-3;
RA   Coppola T., Waldmann R., Borsotto M., Heurteaux C., Romey G.,
RA   Mattei M.-G., Lazdunski M.;
RT   "Molecular cloning of a murine N-type calcium channel alpha 1 subunit.
RT   Evidence for isoforms, brain distribution, and chromosomal
RT   localization.";
RL   FEBS Lett. 338:1-5(1994).
RN   [3]
RP   INTERACTION WITH RIMS1.
RC   TISSUE=Brain;
RX   MEDLINE=21413925; PubMed=11438518; DOI=10.1074/jbc.M100929200;
RA   Coppola T., Magnin-Luethi S., Perret-Menoud V., Gattesco S.,
RA   Schiavo G., Regazzi R.;
RT   "Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-
RT   25, and synaptotagmin.";
RL   J. Biol. Chem. 276:32756-32762(2001).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-745; SER-783 AND
RP   SER-2244, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the
CC       entry of calcium ions into excitable cells and are also involved
CC       in a variety of calcium-dependent processes, including muscle
CC       contraction, hormone or neurotransmitter release, gene expression,
CC       cell motility, cell division and cell death. The isoform alpha-1B
CC       gives rise to N-type calcium currents. N-type calcium channels
CC       belong to the 'high-voltage activated' (HVA) group and are blocked
CC       by omega-conotoxin-GVIA (omega-CTx-GVIA) and by omega-agatoxin-
CC       IIIA (omega-Aga-IIIA). They are however insensitive to
CC       dihydropyridines (DHP), and omega-agatoxin-IVA (omega-Aga-IVA).
CC       Calcium channels containing alpha-1B subunit may play a role in
CC       directed migration of immature neurons.
CC   -!- SUBUNIT: Multisubunit complex consisting of alpha-1, alpha-2, beta
CC       and delta subunits in a 1:1:1:1 ratio. The channel activity is
CC       directed by the pore-forming and voltage-sensitive alpha-1
CC       subunit. In many cases, this subunit is sufficient to generate
CC       voltage-sensitive calcium channel activity. The auxiliary subunits
CC       beta and alpha-2/delta linked by a disulfide bridge regulate the
CC       channel activity. Interacts with RIMS1 and RIMBP2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=NB1;
CC         IsoId=O55017-1; Sequence=Displayed;
CC       Name=NB2;
CC         IsoId=O55017-2; Sequence=VSP_000883;
CC   -!- TISSUE SPECIFICITY: Widespread expression throughout the brain.
CC       Highest levels in pyramidal cell layers C1, C2 and C3 of the
CC       hippocampus, in the dentate gyrus, in the cortex layers 2 et 4, in
CC       the subiculum and the habenula.
CC   -!- DOMAIN: Each of the four internal repeats contains five
CC       hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one
CC       positively charged transmembrane segment (S4). S4 segments
CC       probably represent the voltage-sensor and are characterized by a
CC       series of positively charged amino acids at every third position.
CC   -!- PTM: Phosphorylated in vitro by CaM-kinase II, PKA, PKC and CGPK
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family. CACNA1B subfamily.
CC   -!- SIMILARITY: Contains 1 EF-hand domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB60437.1; Type=Frameshift; Positions=1924, 1934, 2121, 2127;
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DR   EMBL; AF042317; AAB97840.1; -; mRNA.
DR   EMBL; U04999; AAB60437.1; ALT_FRAME; mRNA.
DR   IPI; IPI00115062; -.
DR   IPI; IPI00466672; -.
DR   PIR; S41080; S41080.
DR   RefSeq; NP_001035993.1; NM_001042528.1.
DR   UniGene; Mm.4424; -.
DR   ProteinModelPortal; O55017; -.
DR   SMR; O55017; 1784-1861.
DR   STRING; O55017; -.
DR   TCDB; 1.A.1.11.9; voltage-gated ion channel (VIC) superfamily.
DR   PhosphoSite; O55017; -.
DR   PRIDE; O55017; -.
DR   Ensembl; ENSMUST00000041342; ENSMUSP00000037416; ENSMUSG00000004113.
DR   Ensembl; ENSMUST00000093372; ENSMUSP00000091064; ENSMUSG00000004113.
DR   GeneID; 12287; -.
DR   KEGG; mmu:12287; -.
DR   UCSC; uc008ipe.1; mouse.
DR   UCSC; uc008ipf.1; mouse.
DR   CTD; 12287; -.
DR   MGI; MGI:88296; Cacna1b.
DR   HOVERGEN; HBG050763; -.
DR   NextBio; 280760; -.
DR   ArrayExpress; O55017; -.
DR   Bgee; O55017; -.
DR   Genevestigator; O55017; -.
DR   GermOnline; ENSMUSG00000004113; Mus musculus.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0007269; P:neurotransmitter secretion; IMP:MGI.
DR   GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR   GO; GO:0008016; P:regulation of heart contraction; IMP:MGI.
DR   GO; GO:0048265; P:response to pain; IMP:MGI.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005447; VDCC_N_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01631; NVDCCALPHA1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Calcium; Calcium channel;
KW   Calcium transport; Disulfide bond; Glycoprotein; Ion transport;
KW   Ionic channel; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Polymorphism; Repeat; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN         1   2327       Voltage-dependent N-type calcium channel
FT                                subunit alpha-1B.
FT                                /FTId=PRO_0000053922.
FT   TOPO_DOM      1     95       Cytoplasmic (Potential).
FT   TRANSMEM     96    114       Helical; Name=S1 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    115    133       Extracellular (Potential).
FT   TRANSMEM    134    151       Helical; Name=S2 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    152    164       Cytoplasmic (Potential).
FT   TRANSMEM    165    179       Helical; Name=S3 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    180    186       Extracellular (Potential).
FT   TRANSMEM    187    205       Helical; Name=S4 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    206    225       Cytoplasmic (Potential).
FT   TRANSMEM    226    245       Helical; Name=S5 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    246    331       Extracellular (Potential).
FT   TRANSMEM    332    356       Helical; Name=S6 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    357    482       Cytoplasmic (Potential).
FT   TRANSMEM    483    502       Helical; Name=S1 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    503    516       Extracellular (Potential).
FT   TRANSMEM    517    536       Helical; Name=S2 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    537    544       Cytoplasmic (Potential).
FT   TRANSMEM    545    563       Helical; Name=S3 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    564    574       Extracellular (Potential).
FT   TRANSMEM    575    592       Helical; Name=S4 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    593    611       Cytoplasmic (Potential).
FT   TRANSMEM    612    631       Helical; Name=S5 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    632    684       Extracellular (Potential).
FT   TRANSMEM    685    709       Helical; Name=S6 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    710   1134       Cytoplasmic (Potential).
FT   TRANSMEM   1135   1158       Helical; Name=S1 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1159   1175       Extracellular (Potential).
FT   TRANSMEM   1176   1195       Helical; Name=S2 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1196   1203       Cytoplasmic (Potential).
FT   TRANSMEM   1204   1226       Helical; Name=S3 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1227   1241       Extracellular (Potential).
FT   TRANSMEM   1242   1256       Helical; Name=S4 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1257   1277       Cytoplasmic (Potential).
FT   TRANSMEM   1278   1297       Helical; Name=S5 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1298   1383       Extracellular (Potential).
FT   TRANSMEM   1384   1408       Helical; Name=S6 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1409   1465       Cytoplasmic (Potential).
FT   TRANSMEM   1466   1484       Helical; Name=S1 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1485   1498       Extracellular (Potential).
FT   TRANSMEM   1499   1518       Helical; Name=S2 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1519   1527       Cytoplasmic (Potential).
FT   TRANSMEM   1528   1546       Helical; Name=S3 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1547   1554       Extracellular (Potential).
FT   TRANSMEM   1555   1573       Helical; Name=S4 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1574   1592       Cytoplasmic (Potential).
FT   TRANSMEM   1593   1612       Helical; Name=S5 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1613   1674       Extracellular (Potential).
FT   TRANSMEM   1675   1694       Helical; Name=S6 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1695   2327       Cytoplasmic (Potential).
FT   REPEAT       82    359       I.
FT   REPEAT      468    712       II.
FT   REPEAT     1126   1412       III.
FT   REPEAT     1449   1702       IV.
FT   DOMAIN     1715   1750       EF-hand.
FT   NP_BIND     451    458       ATP (Potential).
FT   CA_BIND    1728   1739       By similarity.
FT   REGION      379    396       Binding to the beta subunit (By
FT                                similarity).
FT   COMPBIAS   2040   2044       Poly-His.
FT   COMPBIAS   2106   2110       Poly-Ser.
FT   SITE        314    314       Calcium ion selectivity and permeability
FT                                (By similarity).
FT   SITE        663    663       Calcium ion selectivity and permeability
FT                                (By similarity).
FT   SITE       1358   1358       Calcium ion selectivity and permeability
FT                                (By similarity).
FT   SITE       1646   1646       Calcium ion selectivity and permeability
FT                                (By similarity).
FT   MOD_RES     455    455       Phosphoserine (By similarity).
FT   MOD_RES     745    745       Phosphoserine.
FT   MOD_RES     783    783       Phosphoserine.
FT   MOD_RES    1710   1710       Phosphoserine; by PKA (Potential).
FT   MOD_RES    1959   1959       Phosphoserine (By similarity).
FT   MOD_RES    2244   2244       Phosphoserine.
FT   CARBOHYD    256    256       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1554   1554       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1666   1666       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     756    756       A -> AFVKQTRGTVSRSSSVSSVNSP (in isoform
FT                                NB2).
FT                                /FTId=VSP_000883.
FT   VARIANT     414    414       D -> DA.
FT   CONFLICT    238    238       A -> G (in Ref. 2; AAB60437).
FT   CONFLICT    645    645       N -> I (in Ref. 2; AAB60437).
FT   CONFLICT    757    759       RQQ -> QE (in Ref. 2; AAB60437).
FT   CONFLICT    880    880       A -> P (in Ref. 2; AAB60437).
FT   CONFLICT   1128   1128       L -> F (in Ref. 2; AAB60437).
FT   CONFLICT   1173   1173       K -> E (in Ref. 2; AAB60437).
FT   CONFLICT   1185   1185       F -> C (in Ref. 2; AAB60437).
FT   CONFLICT   1227   1230       Missing (in Ref. 2; AAB60437).
FT   CONFLICT   1388   1388       F -> L (in Ref. 2; AAB60437).
FT   CONFLICT   1549   1549       A -> AET (in Ref. 2; AAB60437).
FT   CONFLICT   1615   1615       I -> S (in Ref. 2; AAB60437).
FT   CONFLICT   1636   1636       L -> I (in Ref. 2; AAB60437).
FT   CONFLICT   1657   1657       G -> D (in Ref. 2; AAB60437).
FT   CONFLICT   1802   1837       Missing (in Ref. 2; AAB60437).
FT   CONFLICT   1942   1942       A -> G (in Ref. 2; AAB60437).
FT   CONFLICT   1949   1949       G -> D (in Ref. 2; AAB60437).
FT   CONFLICT   1963   1963       A -> L (in Ref. 2; AAB60437).
FT   CONFLICT   1979   1979       E -> D (in Ref. 2; AAB60437).
FT   CONFLICT   1994   1994       P -> L (in Ref. 2; AAB60437).
FT   CONFLICT   2021   2021       H -> D (in Ref. 2; AAB60437).
FT   CONFLICT   2075   2075       A -> AA (in Ref. 2; AAB60437).
FT   CONFLICT   2141   2141       T -> A (in Ref. 2; AAB60437).
FT   CONFLICT   2168   2168       S -> I (in Ref. 2; AAB60437).
FT   CONFLICT   2309   2309       S -> N (in Ref. 2; AAB60437).
FT   CONFLICT   2313   2313       R -> G (in Ref. 2; AAB60437).
FT   CONFLICT   2316   2316       H -> A (in Ref. 2; AAB60437).
SQ   SEQUENCE   2327 AA;  261481 MW;  AD42CDD38482895A CRC64;
     MVRFGDELGG RYGGTGGGER ARGGGAGGAG GPGQGGLPPG QRVLYKQSIA QRARTMALYN
     PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPPFEYM ILATIIANCI VLALEQHLPD
     GDKTPMSERL DDTEPYFIGI FCFEAGIKII ALGFVFHKGS YLRNGWNVMD FVVVLTGILA
     TAGTDFDLRT LRAVRVLRPL KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAILMFAII
     GLEFYMGKFH KACFPNSTDT EPVGDFPCGK DPPARQCDGD TECREYWPGP NFGITNFDNI
     LFAILTVFQC ITMEGWTDIL YNTNDAAGNT WNWLYFIPLI IIGSFFMLNL VLGVLSGEFA
     KERERVENRR AFLKLRRQQQ IERELNGYLE WIFKAEEVML AEEDKNAEEK SPLDVLKRAA
     TKKSRNDLIH AEEGEDRFVD LCAVGSPFAR ASLKSGKTES SSYFRRKEKM FRFFIRRMVK
     AQSFYWVVLC VVALNTLCVA MVHYNQPQRL TTALYFAEFV FLGLFLTEMS LKMYGLGPRS
     YFRSSFNCFD FGVIVGSIFE VVWAAIKPGT SFGISVLRAL RLLRIFKVTK YWNSLRNLVV
     SLLNSMKSII SLLFLLFLFI VVFALLGMQL FGGQFNFQDE TPTTNFDTFP AAILTVFQIL
     TGEDWNAVMY HGIESQGGVS KGMFSSFYFI VLTLFGNYTL LNVFLAIAVD NLANAQELTK
     DEEEMEEAAN QKLALQKAKE VAEVSPMSAA NISIAARQQN SAKARSVWEQ RASQLRLQNL
     RASCEALYSE MDPEERLRYA STRHVRPDMK THMDRPLVVE PGRDGLRGPV GSKSKPEGTE
     ATESADLPRR HHRHRDRDKT SATAPAGGEQ DRTESTETGA REERARPRRS HSKETPGADT
     QVRCERSRRH HRRGSPEEAT EREPRRHRAH RHAQDSSKEG TAPVLVPKGE RRARHRGPRT
     GPREAENNEE PTRRHRARHK VPPTLQPPER EAAEKESNAV EGDKETRNHQ PKEPHCDLEA
     IAVTGVGPLH MLPSTCLQKV DEQPEDADNQ RNVTRMGSQP SDPSTTVHVP VTLTGPPGET
     PVVPSGNMNL EGQAEGKKEA EADDVLRRGP RPIVPYSSMF CLSPTNLLRR FCHYIVTMRY
     FEMVILVVIA LSSIALAAED PVRTDSFRNN ALKYMDYIFT GVFTFEMVIK MIDLGLLLHP
     GAYFRDLWNI LDFIVVSGAL VAFAFSSFMG GSKGKDINTI KSLRVLRVLR PLKTIKRLPK
     LKAVFDCVVN SLKNVLNILI VYMLFMFIFA VIAVQLFKGK FFYCTDESKE LERDCRGQYL
     DYEKEEVEAQ PRQWKKYDFH YDNVLWALLT LFTVSTGEGW PMVLKHSVDA TYEEQGPSPG
     FRMELSIFYV VYFVVFPFFF VNIFVALIII TFQEQGDKVM SECSLEKNER ACIDFAISAK
     PLTRYMPQNK QSFQYKTWTF VVSPPFEYFI MAMIALNTVV LMMKFYDAPY EYELMLKCLN
     IVFTSMFSME CILKIIAFGV LNYFRDAWNV FDFVTVLGSI TDILVTEIAN NFINLSFLRL
     FRAARLIKLL RQGYTIRILL WTFVQSFKAL PYVCLLIAML FFIYAIIGMQ VFGNIALDDD
     TSINRHNNFR TFLQALMLLF RSATGEAWHE IMLSCLGNRA CDPHANASEC GSDFAYFYFV
     SFIFLCSFLM LNLFVAVIMD NFEYLTRDSS ILGPHHLDEF IRVWAEYDPA ACGRISYNDM
     FEMLKHMSPP LGLGKKCPAR VAYKRLVRMN MPISNEDMTV HFTSTLMALI RTALEIKLAP
     AGTKQHQCDA ELRKEISSVW ANLPQKTLDL LVPPHKPDEM TVGKVYAALM IFDFYKQNKT
     TRDQTHQAPG GLSQMGPVSL FHPLKATLEQ TQPAVLRGAR VFLRQKSATS LSNGGAIQTQ
     ESGIKESLSW GTQRTQDALY EARAPLERGH SAEIPVGQSG TLAVDVQMQN MTLRGPDGEP
     QPGLESQGRA ASMPRLAAET QPAPNASPMK RSISTLAPRP HGTQLCSTVL DRPPPSQASH
     HHHHRCHRRR DKKQRSLEKG PSLSVDPEGA PSTAAGPGLP HGEGSTACRR DRKQERGRSQ
     ERRQPSSSSS EKQRFYSCDR FGSREPPQLM PSLSSHPTSP TAALEPAPHP QGSGSVNGSP
     LMSTSGASTP GRGGRRQLPQ TPLTPRPSIT YKTANSSPVH FAEGQSGLPA FSPGRLSRGL
     SEHNALLQKE PLSQPLAPGS RIGSDPYLGQ RLDSEASAHT LPEDTLTFEE AVATNSGRSS
     RTSYVSSLTS QSHPLRRVPN GYHCTLGLST GVRARHSYHH PDQDHWC
//
ID   PGRC1_MOUSE             Reviewed;         195 AA.
AC   O55022; Q99JN0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Membrane-associated progesterone receptor component 1;
GN   Name=Pgrmc1; Synonyms=Pgrmc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Testis;
RA   Kwon S., Lunn R.M., O'Brien D.A., Bell D.A., Eddy E.M.;
RT   "The expression of a putative membrane associated progesterone
RT   receptor component in the mouse testis and epididymis.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 72-88 AND 106-119, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION AT SER-181.
RX   PubMed=15378723; DOI=10.1002/rcm.1604;
RA   Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.;
RT   "Phosphoproteome analysis of mouse liver using immobilized metal
RT   affinity purification and linear ion trap mass spectrometry.";
RL   Rapid Commun. Mass Spectrom. 18:2169-2176(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-180, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-180 AND SER-181, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Receptor for progesterone (By similarity).
CC   -!- SUBCELLULAR LOCATION: Microsome membrane; Single-pass membrane
CC       protein (By similarity). Endoplasmic reticulum membrane; Single-
CC       pass membrane protein (By similarity).
CC   -!- DOMAIN: The cytochrome b5 heme-binding domain lacks the conserved
CC       iron-binding His residues at positions 107 and 131 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome b5 family. MAPR subfamily.
CC   -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF042491; AAB97466.1; -; mRNA.
DR   EMBL; BC006016; AAH06016.1; -; mRNA.
DR   IPI; IPI00319973; -.
DR   RefSeq; NP_058063.2; NM_016783.3.
DR   UniGene; Mm.9052; -.
DR   ProteinModelPortal; O55022; -.
DR   SMR; O55022; 70-172.
DR   STRING; O55022; -.
DR   PhosphoSite; O55022; -.
DR   PRIDE; O55022; -.
DR   Ensembl; ENSMUST00000073339; ENSMUSP00000073061; ENSMUSG00000006373.
DR   GeneID; 53328; -.
DR   KEGG; mmu:53328; -.
DR   UCSC; uc009sxo.1; mouse.
DR   CTD; 53328; -.
DR   MGI; MGI:1858305; Pgrmc1.
DR   eggNOG; roNOG14725; -.
DR   HOGENOM; HBG715794; -.
DR   HOVERGEN; HBG059971; -.
DR   InParanoid; O55022; -.
DR   OMA; ESARKND; -.
DR   OrthoDB; EOG4SXNDQ; -.
DR   PhylomeDB; O55022; -.
DR   NextBio; 310145; -.
DR   ArrayExpress; O55022; -.
DR   Bgee; O55022; -.
DR   CleanEx; MM_PGRMC1; -.
DR   Genevestigator; O55022; -.
DR   GermOnline; ENSMUSG00000006373; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005792; C:microsome; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR   InterPro; IPR001199; Cyt_B5.
DR   Gene3D; G3DSA:3.10.120.10; Cyt_B5; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   SUPFAM; SSF55856; Cyt_B5; 1.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; FALSE_NEG.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Lipid-binding;
KW   Membrane; Microsome; Phosphoprotein; Receptor; Steroid-binding;
KW   Transmembrane; Transmembrane helix.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    195       Membrane-associated progesterone receptor
FT                                component 1.
FT                                /FTId=PRO_0000121740.
FT   TOPO_DOM      2     24       Lumenal (Potential).
FT   TRANSMEM     25     43       Helical; (Potential).
FT   TOPO_DOM     44    195       Cytoplasmic (Potential).
FT   DOMAIN       72    171       Cytochrome b5 heme-binding.
FT   MOD_RES      54     54       Phosphoserine (By similarity).
FT   MOD_RES      74     74       Phosphothreonine (By similarity).
FT   MOD_RES     178    178       Phosphothreonine (By similarity).
FT   MOD_RES     180    180       Phosphotyrosine.
FT   MOD_RES     181    181       Phosphoserine.
FT   CONFLICT     87     87       P -> S (in Ref. 1; AAB97466).
SQ   SEQUENCE   195 AA;  21694 MW;  1FFD17AFAE6C81FC CRC64;
     MAAEDVVATG ADPSELEGGG LLHEIFTSPL NLLLLGLCIF LLYKIVRGDQ PGASGDNDDD
     EPPPLPRLKR RDFTPAELRR FDGVQDPRIL MAINGKVFDV TKGRKFYGPE GPYGVFAGRD
     ASRGLATFCL DKEALKDEYD DLSDLTPAQQ ETLSDWDSQF TFKYHHVGKL LKEGEEPTVY
     SDDEEPKDET ARKNE
//
ID   IMPA1_MOUSE             Reviewed;         277 AA.
AC   O55023;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Inositol monophosphatase 1;
DE            Short=IMP 1;
DE            Short=IMPase 1;
DE            EC=3.1.3.25;
DE   AltName: Full=Inositol-1(or 4)-monophosphatase 1;
DE   AltName: Full=Lithium-sensitive myo-inositol monophosphatase A1;
GN   Name=Impa1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Parthasarathy L., Parthasarathy R., Vadnal R.E.;
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   INDUCTION.
RX   PubMed=12877981; DOI=10.1016/S0169-328X(03)00120-7;
RA   Shamir A., Shaltiel G., Greenberg M.L., Belmaker R.H., Agam G.;
RT   "The effect of lithium on expression of genes for inositol
RT   biosynthetic enzymes in mouse hippocampus; a comparison with the yeast
RT   model.";
RL   Brain Res. Mol. Brain Res. 115:104-110(2003).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=17068342; DOI=10.1074/jbc.M604474200;
RA   Ohnishi T., Ohba H., Seo K.-C., Im J., Sato Y., Iwayama Y.,
RA   Furuichi T., Chung S.-K., Yoshikawa T.;
RT   "Spatial expression patterns and biochemical properties distinguish a
RT   second myo-inositol monophosphatase IMPA2 from IMPA1.";
RL   J. Biol. Chem. 282:637-646(2007).
CC   -!- FUNCTION: Responsible for the provision of inositol required for
CC       synthesis of phosphatidylinositol and polyphosphoinositides and
CC       has been implicated as the pharmacological target for lithium
CC       action in brain. Can use myo-inositol monophosphates, myo-
CC       inositol-1,3-diphosphate, myo-inositol-1,4-diphosphate, scyllo-
CC       inositol-phosphate, glucose-1-phosphate, glucose-6-phosphate,
CC       fructose-1-phosphate, beta-glycerophosphate, and 2'-AMP as
CC       substrates (By similarity).
CC   -!- CATALYTIC ACTIVITY: Myo-inositol phosphate + H(2)O = myo-inositol
CC       + phosphate.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: Inhibited by Li(+).
CC   -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-
CC       inositol from D-glucose 6-phosphate: step 2/2.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Mostly expressed in brain, small intestine,
CC       testis, kidney, and spleen (at protein level).
CC   -!- INDUCTION: By lithium Li(+) in hippocamp.
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase family.
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DR   EMBL; AF042730; AAB97469.1; -; mRNA.
DR   IPI; IPI00115085; -.
DR   UniGene; Mm.183042; -.
DR   ProteinModelPortal; O55023; -.
DR   SMR; O55023; 5-276.
DR   STRING; O55023; -.
DR   PhosphoSite; O55023; -.
DR   PRIDE; O55023; -.
DR   Ensembl; ENSMUST00000065938; ENSMUSP00000068174; ENSMUSG00000027531.
DR   MGI; MGI:1933158; Impa1.
DR   eggNOG; roNOG09523; -.
DR   HOGENOM; HBG730251; -.
DR   HOVERGEN; HBG052123; -.
DR   InParanoid; O55023; -.
DR   OrthoDB; EOG42FSJ2; -.
DR   PhylomeDB; O55023; -.
DR   BRENDA; 3.1.3.25; 244.
DR   ArrayExpress; O55023; -.
DR   Bgee; O55023; -.
DR   CleanEx; MM_IMPA1; -.
DR   Genevestigator; O55023; -.
DR   GermOnline; ENSMUSG00000027531; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008934; F:inositol-1(or 4)-monophosphatase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR020583; Inositol_monoP_metal-BS.
DR   InterPro; IPR020552; Inositol_monoPase_Li-sen.
DR   InterPro; IPR000760; Inositol_monophosphatase.
DR   InterPro; IPR020550; Inositol_monophosphatase_CS.
DR   PANTHER; PTHR20854; Inositol_P; 1.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
DR   PRINTS; PR00378; LIIMPHPHTASE.
DR   PROSITE; PS00629; IMP_1; 1.
DR   PROSITE; PS00630; IMP_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Lithium; Magnesium; Metal-binding.
FT   CHAIN         1    277       Inositol monophosphatase 1.
FT                                /FTId=PRO_0000142514.
FT   REGION       92     95       Substrate binding (By similarity).
FT   REGION      194    196       Substrate binding (By similarity).
FT   METAL        70     70       Magnesium 1 (By similarity).
FT   METAL        90     90       Magnesium 1 (By similarity).
FT   METAL        90     90       Magnesium 2 (By similarity).
FT   METAL        92     92       Magnesium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        93     93       Magnesium 2 (By similarity).
FT   METAL       220    220       Magnesium 2 (By similarity).
FT   BINDING      70     70       Substrate (By similarity).
FT   BINDING     213    213       Substrate (By similarity).
FT   BINDING     220    220       Substrate (By similarity).
SQ   SEQUENCE   277 AA;  30436 MW;  EDBDB7BD24748E9D CRC64;
     MADPWQECMD YAVILARQAG EMIREALKNE MDVMIKSSPA DLVTVTDQKV EKMLMSSIKE
     KYPCHSFIGE ESVAAGEKTV FTESPTWFID PIDGTTNFVH RFPFVAVSIG FLVNKEMEFG
     IVYSCVEDKM YTGRKGKGAF CNGQKLQVSQ QEDITKSLLV TELGSSRKPE TLRIVLSNME
     KLCSIPIHGI RSVGTAAVNM CLVATGGADA YYEMGIHCWD MAGAGIIVTE AGGVLMDVTG
     GPFDLMSRRI IAANSITLAK RIAKEIEIIP LQRDDES
//
ID   BCKD_MOUSE              Reviewed;         412 AA.
AC   O55028;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=[3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial;
DE            EC=2.7.11.4;
DE   AltName: Full=Branched-chain alpha-ketoacid dehydrogenase kinase;
DE            Short=BCKD-kinase;
DE            Short=BCKDHKIN;
DE   Flags: Precursor;
GN   Name=Bckdk;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RX   MEDLINE=98278837; PubMed=9611264; DOI=10.1016/S0378-1119(98)00182-6;
RA   Doering C.B., Coursey C., Spangler W., Danner D.J.;
RT   "Murine branched chain alpha ketoacid dehydrogenase kinase; cDNA
RT   cloning, tissue distribution, and temporal expression during embryonic
RT   development.";
RL   Gene 212:213-219(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
CC   -!- FUNCTION: Catalyzes the phosphorylation and inactivation of the
CC       branched-chain alpha-ketoacid dehydrogenase complex, the key
CC       regulatory enzyme of the valine, leucine and isoleucine catabolic
CC       pathways. Key enzyme that regulate the activity state of the BCKD
CC       complex (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + [3-methyl-2-oxobutanoate dehydrogenase
CC       (acetyl-transferring)] = ADP + [3-methyl-2-oxobutanoate
CC       dehydrogenase (acetyl-transferring)] phosphate.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- INDUCTION: Expression in female liver is influenced by circadian
CC       rhythm.
CC   -!- PTM: Autophosphorylated (By similarity).
CC   -!- SIMILARITY: Belongs to the PDK/BCKDK protein kinase family.
CC   -!- SIMILARITY: Contains 1 histidine kinase domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF043070; AAB97689.1; -; mRNA.
DR   EMBL; BC046595; AAH46595.1; -; mRNA.
DR   IPI; IPI00115094; -.
DR   RefSeq; NP_033869.1; NM_009739.3.
DR   UniGene; Mm.425495; -.
DR   ProteinModelPortal; O55028; -.
DR   SMR; O55028; 68-408.
DR   STRING; O55028; -.
DR   PhosphoSite; O55028; -.
DR   PRIDE; O55028; -.
DR   Ensembl; ENSMUST00000071056; ENSMUSP00000070345; ENSMUSG00000030802.
DR   GeneID; 12041; -.
DR   KEGG; mmu:12041; -.
DR   UCSC; uc009jxf.1; mouse.
DR   CTD; 12041; -.
DR   MGI; MGI:1276121; Bckdk.
DR   eggNOG; roNOG09065; -.
DR   HOGENOM; HBG281443; -.
DR   HOVERGEN; HBG004829; -.
DR   InParanoid; O55028; -.
DR   OMA; NQSAIDV; -.
DR   OrthoDB; EOG49ZXPB; -.
DR   PhylomeDB; O55028; -.
DR   BRENDA; 2.7.11.4; 244.
DR   NextBio; 280305; -.
DR   ArrayExpress; O55028; -.
DR   Bgee; O55028; -.
DR   CleanEx; MM_BCKDK; -.
DR   Genevestigator; O55028; -.
DR   GermOnline; ENSMUSG00000030802; Mus musculus.
DR   GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; ISS:HGNC.
DR   GO; GO:0047323; F:[3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; ISS:HGNC.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:HGNC.
DR   GO; GO:0000155; F:two-component sensor activity; IEA:InterPro.
DR   GO; GO:0009083; P:branched chain family amino acid catabolic process; ISS:HGNC.
DR   GO; GO:0018106; P:peptidyl-histidine phosphorylation; IEA:InterPro.
DR   InterPro; IPR003594; ATPase-like_ATP-bd.
DR   InterPro; IPR018955; BCDHK/PDK_N.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR005467; Sig_transdc_His_kinase_core.
DR   Gene3D; G3DSA:3.30.565.10; ATP_bd_ATPase; 1.
DR   Gene3D; G3DSA:1.20.140.20; BCDHK/PDK_N; 1.
DR   Pfam; PF10436; BCDHK_Adom3; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATP_bd_ATPase; 1.
DR   SUPFAM; SSF69012; BCDHK/PDK_N; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Kinase; Mitochondrion; Nucleotide-binding;
KW   Phosphoprotein; Transferase; Transit peptide.
FT   TRANSIT       1     30       Mitochondrion (By similarity).
FT   CHAIN        31    412       [3-methyl-2-oxobutanoate dehydrogenase
FT                                [lipoamide]] kinase, mitochondrial.
FT                                /FTId=PRO_0000023453.
FT   DOMAIN      159    404       Histidine kinase.
FT   MOD_RES      31     31       Phosphoserine.
FT   MOD_RES      33     33       Phosphoserine (By similarity).
FT   MOD_RES      35     35       Phosphothreonine.
FT   MOD_RES      52     52       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     184    184       N6-acetyllysine (By similarity).
FT   MOD_RES     192    192       N6-acetyllysine (By similarity).
FT   MOD_RES     233    233       N6-acetyllysine (By similarity).
FT   MOD_RES     245    245       N6-acetyllysine (By similarity).
SQ   SEQUENCE   412 AA;  46588 MW;  80B3B173AAC8AAD3 CRC64;
     MILTSVLGSG PRSWSSLWPL LGSSLSLRAR STSATDTHHV ELARERSKTV TSFYNQSAID
     VAAEKPSVRL TPTMMLYSGR SQDGSHLLKS GRYLQQELPV RIAHRIKGFR SLPFIIGCNP
     TILHVHELYI RAFQKLTDFP PIKDQADEAQ YCQLVRQLLD DHKDVVTLLA EGLRESRKHI
     QDEKLVRYFL DKTLTSRLGI RMLATHHLAL HEDKPDFVGI ICTRLSPKKI IEKWVDFARR
     LCEHKYGNAP RVRINGHVAA RFPFIPMPLD YILPELLKNA MRATMESHLD TPYNVPDVVI
     TIANNDIDLI IRISDRGGGI AHKDLDRVMD YHFTTAEAST QDPRINPLFG HLDMHSGGQS
     GPMHGFGFGL PTSRAYAEYL GGSLQLQSLQ GIGTDVYLRL RHIDGREESF RI
//
ID   COPB2_MOUSE             Reviewed;         905 AA.
AC   O55029; Q3U5Z9;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 2.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Coatomer subunit beta';
DE   AltName: Full=Beta'-coat protein;
DE            Short=Beta'-COP;
DE   AltName: Full=p102;
GN   Name=Copb2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 456-905.
RC   TISSUE=Testis;
RA   Tarsounas M., Moens P.B., Pearlman R.E.;
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The coatomer is a cytosolic protein complex that binds
CC       to dilysine motifs and reversibly associates with Golgi non-
CC       clathrin-coated vesicles, which further mediate biosynthetic
CC       protein transport from the ER, via the Golgi up to the trans Golgi
CC       network. Coatomer complex is required for budding from Golgi
CC       membranes, and is essential for the retrograde Golgi-to-ER
CC       transport of dilysine-tagged proteins. In mammals, the coatomer
CC       can only be recruited by membranes associated to ADP-ribosylation
CC       factors (ARFs), which are small GTP-binding proteins; the complex
CC       also influences the Golgi structural integrity, as well as the
CC       processing, activity, and endocytic recycling of LDL receptors (By
CC       similarity).
CC   -!- FUNCTION: This coatomer complex protein, essential for Golgi
CC       budding and vesicular trafficking, is a selective binding protein
CC       (RACK) for protein kinase C, epsilon type. It binds to Golgi
CC       membranes in a GTP-dependent manner.
CC   -!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
CC       beta, beta', gamma, delta, epsilon and zeta subunits. Probably
CC       interacts with PEX11A. Interacts with SCYL1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus
CC       membrane; Peripheral membrane protein; Cytoplasmic side (By
CC       similarity). Cytoplasmic vesicle, COPI-coated vesicle membrane;
CC       Peripheral membrane protein; Cytoplasmic side (By similarity).
CC       Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic
CC       side of the Golgi, as well as on the vesicles/buds originating
CC       from it (By similarity).
CC   -!- SIMILARITY: Belongs to the WD repeat COPB2 family.
CC   -!- SIMILARITY: Contains 9 WD repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK088064; BAC40125.1; -; mRNA.
DR   EMBL; AK153352; BAE31926.1; -; mRNA.
DR   EMBL; AF043120; AAB97760.1; -; mRNA.
DR   EMBL; BC006675; AAH06675.1; -; mRNA.
DR   IPI; IPI00115097; -.
DR   RefSeq; NP_056642.1; NM_015827.2.
DR   UniGene; Mm.400464; -.
DR   ProteinModelPortal; O55029; -.
DR   SMR; O55029; 4-796.
DR   IntAct; O55029; 2.
DR   STRING; O55029; -.
DR   PhosphoSite; O55029; -.
DR   PRIDE; O55029; -.
DR   Ensembl; ENSMUST00000035033; ENSMUSP00000035033; ENSMUSG00000032458.
DR   GeneID; 50797; -.
DR   KEGG; mmu:50797; -.
DR   UCSC; uc009rdm.1; mouse.
DR   CTD; 50797; -.
DR   MGI; MGI:1354962; Copb2.
DR   eggNOG; roNOG07305; -.
DR   GeneTree; ENSGT00550000074859; -.
DR   HOGENOM; HBG330931; -.
DR   HOVERGEN; HBG051076; -.
DR   InParanoid; O55029; -.
DR   OMA; FYDWENT; -.
DR   OrthoDB; EOG43R3KZ; -.
DR   PhylomeDB; O55029; -.
DR   NextBio; 307805; -.
DR   ArrayExpress; O55029; -.
DR   Bgee; O55029; -.
DR   Genevestigator; O55029; -.
DR   GermOnline; ENSMUSG00000032458; Mus musculus.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   InterPro; IPR016453; Coatomer_beta'_subunit.
DR   InterPro; IPR006692; Coatomer_WD-assoc_reg.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF04053; Coatomer_WDAD; 1.
DR   Pfam; PF00400; WD40; 6.
DR   PIRSF; PIRSF005567; Coatomer_beta'_subunit; 1.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40_like; 2.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW   ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein;
KW   Protein transport; Repeat; Transport; WD repeat.
FT   CHAIN         1    905       Coatomer subunit beta'.
FT                                /FTId=PRO_0000050913.
FT   REPEAT       13     52       WD 1.
FT   REPEAT       55     94       WD 2.
FT   REPEAT       97    136       WD 3.
FT   REPEAT      140    180       WD 4.
FT   REPEAT      183    224       WD 5.
FT   REPEAT      227    266       WD 6.
FT   REPEAT      350    388       WD 7.
FT   REPEAT      390    425       WD 8.
FT   REPEAT      746    783       WD 9.
FT   COILED      867    891       Potential.
FT   MOD_RES     318    318       N6-acetyllysine (By similarity).
FT   MOD_RES     354    354       Phosphotyrosine (By similarity).
FT   MOD_RES     627    627       N6-acetyllysine (By similarity).
FT   MOD_RES     859    859       Phosphoserine (By similarity).
FT   CONFLICT    684    684       S -> H (in Ref. 3; AAB97760).
FT   CONFLICT    733    733       F -> L (in Ref. 3; AAB97760).
FT   CONFLICT    839    839       A -> P (in Ref. 3; AAB97760).
SQ   SEQUENCE   905 AA;  102449 MW;  5845082CAB10FD12 CRC64;
     MPLRLDIKRK LTARSDRVKS VDLHPTEPWM LASLYNGSVC VWNHETQTLV KTFEVCDLPV
     RAAKFVARKN WVVTGADDMQ IRVFNYNTLE RVHMFEAHSD YIRCIAVHPT QPFILTSSDD
     MLIKLWDWDK KWSCSQVFEG HTHYVMQIVI NPKDNNQFAS ASLDRTIKVW QLGSSSPNFT
     LEGHEKGVNC IDYYSGGDKP YLISGADDRL VKIWDYQNKT CVQTLEGHAQ NVSCASFHPE
     LPIIITGSED GTVRIWHSST YRLESTLNYG MERVWCVASL RGSNNVALGY DEGSIIVKLG
     REEPAMSMDA NGKIIWAKHS EVQQANLKAM GDTEIKDGER LPLAVKDMGS CEIYPQTIQH
     NPNGRFVVVC GDGEYIIYTA MALRNKSFGS AQEFAWAHDS SEYAIRESNS IVKIFKNFKE
     KKSFKPDFGA ESIYGGFLLG VRSVNGLAFY DWENTELIRR IEIQPKHIFW SDSGELVCIA
     TEESFFILKY LSEKVLAAQE THEGVTEDGI EDAFEVLGEI QEIVKTGLWV GDCFIYTSSV
     NRLNYYVGGE IVTIAHLDRT MYLLGYIPKD NRLYLGDKEL NIVSYSLLVS VLEYQTAVMR
     RDFSMADKVL PTIPKEQRTR VAHFLEKQGF KQQALTVSTD PEHRFELALQ LGELKIAYQL
     AVEAESEQKW KQLAELAISK CQFSLAQECL HHAQDYGGLL LLATASGNAS MVNKLAEGAE
     RDGKNNVAFM SYFLQGKLDA CLELLIRTGR LPEAAFLART YLPSQVSRVV KLWRENLSKV
     NQKAAESLAD PTEYENLFPG LKEAFVVEEW VKETHADLWP AKQYPLVTPN EERNVMEEAK
     GFQPSRPTAQ QEPDGKPASS PVIMASQTTH KEEKSLLELE VDLDNLELED IDTTDINLDE
     DILDD
//
ID   O55033_MOUSE            Unreviewed;       380 AA.
AC   O55033;
DT   01-JUN-1998, integrated into UniProtKB/TrEMBL.
DT   01-JUN-1998, sequence version 1.
DT   08-MAR-2011, entry version 87.
DE   SubName: Full=Non-catalytic region of tyrosine kinase adaptor protein 2;
DE   SubName: Full=SH2/SH3 adaptor protein;
GN   Name=Nck2; Synonyms=mNck-beta; ORFNames=mCG_113686;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   She H.Y., Chen M., Li W.;
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor. C3;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 3 SH3 domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF043260; AAC06353.1; -; mRNA.
DR   EMBL; BC011071; AAH11071.1; -; mRNA.
DR   EMBL; BC034255; AAH34255.1; -; mRNA.
DR   EMBL; CH466589; EDK96908.1; -; Genomic_DNA.
DR   IPI; IPI00309413; -.
DR   RefSeq; NP_035009.3; NM_010879.3.
DR   UniGene; Mm.389903; -.
DR   UniGene; Mm.476455; -.
DR   HSSP; P19174; 2HSP.
DR   ProteinModelPortal; O55033; -.
DR   SMR; O55033; 1-380.
DR   MINT; MINT-100584; -.
DR   STRING; O55033; -.
DR   PhosphoSite; O55033; -.
DR   PRIDE; O55033; -.
DR   Ensembl; ENSMUST00000086421; ENSMUSP00000083611; ENSMUSG00000066877.
DR   Ensembl; ENSMUST00000114744; ENSMUSP00000110392; ENSMUSG00000066877.
DR   GeneID; 17974; -.
DR   KEGG; mmu:17974; -.
DR   UCSC; uc007avo.1; mouse.
DR   CTD; 17974; -.
DR   MGI; MGI:1306821; Nck2.
DR   eggNOG; roNOG08387; -.
DR   HOGENOM; HBG387920; -.
DR   HOVERGEN; HBG000719; -.
DR   InParanoid; O55033; -.
DR   OMA; WKCKNSR; -.
DR   OrthoDB; EOG4DR9CN; -.
DR   PhylomeDB; O55033; -.
DR   NextBio; 457972; -.
DR   ArrayExpress; O55033; -.
DR   Bgee; O55033; -.
DR   Genevestigator; O55033; -.
DR   GO; GO:0012506; C:vesicle membrane; IDA:MGI.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007015; P:actin filament organization; IMP:MGI.
DR   GO; GO:0016477; P:cell migration; IMP:MGI.
DR   GO; GO:0030032; P:lamellipodium assembly; IMP:MGI.
DR   InterPro; IPR017304; Cytoplasmic_NCK.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF00018; SH3_1; 3.
DR   PIRSF; PIRSF037874; Cytoplasmic_NCK; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 3.
DR   SUPFAM; SSF50044; SH3; 3.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 3.
PE   1: Evidence at protein level;
KW   Kinase; SH3 domain; Transferase.
SQ   SEQUENCE   380 AA;  42879 MW;  7B3404B976F0A54D CRC64;
     MTEEVIVIAK WDYTAQQDQE LDIRKNERLW LLDDSKTWWR VRNAANRTGY VPSNYVERKN
     SLKKGSLVKN LKDTLGLGKT RRKPSARDAS PTPSTDAEYP ANGSGADRIY DLNIPAFVKF
     AYVAEREDEL SLVKGSRVTV MEKCSDGWWR GSFNGQIGWF PSNYVLEEAD EAAAEAPSFL
     SLRRGTALSN GQGARVLHVV QTLYPFSSVT EEELSFEKGE TMEVIEKPEN DPEWWKCKNA
     RGQVGLVPKN YVVVLSDGPA LHPAHTPQIS YTGPSASGRF AGREWYYGNV TRHQAECALN
     ERGVEGDFLI RDSESSPSDF SVSLKASGRN KHFKVQLVDS VYCIGQRRFH SMDELVEHYK
     KAPIFTSEHG EKLYLVRALQ
//
ID   SYUA_MOUSE              Reviewed;         140 AA.
AC   O55042; Q3U130; Q9CXF8; Q9EQC3; Q9QUR3;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Alpha-synuclein;
DE   AltName: Full=Non-A beta component of AD amyloid;
DE   AltName: Full=Non-A4 component of amyloid precursor;
DE            Short=NACP;
GN   Name=Snca; Synonyms=Syn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=98311217; PubMed=9648883;
RA   Hsu L.J., Mallory M., Xia Y., Veinbergs I., Hashimoto M.,
RA   Yoshimoto M., Thal L.J., Saitoh T., Masliah E.;
RT   "Expression pattern of synucleins (non-Abeta component of Alzheimer's
RT   disease amyloid precursor protein/alpha-synuclein) during murine brain
RT   development.";
RL   J. Neurochem. 71:338-344(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=ICR;
RX   MEDLINE=98264007; PubMed=9601701;
RA   Hong L., Ko H.W., Gwag B.J., Joe E., Lee S., Kim Y.T., Suh Y.-H.;
RT   "The cDNA cloning and ontogeny of mouse alpha-synuclein.";
RL   NeuroReport 9:1239-1243(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and Sv129/Ola; TISSUE=Brain;
RA   Fog J.U., Kallunki P.;
RT   "Genomic cloning of the mouse alpha-synuclein and analysis of the
RT   promoter.";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   PubMed=11156617; DOI=10.1101/gr.165801;
RA   Touchman J.W., Dehejia A., Chiba-Falek O., Cabin D.E., Schwartz J.R.,
RA   Orrison B.M., Polymeropoulos M.H., Nussbaum R.L.;
RT   "Human and mouse alpha-synuclein genes: comparative genomic sequence
RT   analysis and identification of a novel gene regulatory element.";
RL   Genome Res. 11:78-86(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Liver, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54.
RC   STRAIN=129/SvJ;
RX   MEDLINE=22618243; PubMed=12732244; DOI=10.1016/S0306-4522(03)00036-8;
RA   Schlueter O.M., Fornai F., Alessandri M.G., Takamori S., Geppert M.,
RA   Jahn R., Suedhof T.C.;
RT   "Role of alpha-synuclein in 1-methyl-4-phenyl-1,2,3,6-
RT   tetrahydropyridine-induced parkinsonism in mice.";
RL   Neuroscience 118:985-1002(2003).
RN   [8]
RP   PROTEIN SEQUENCE OF 61-96, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
CC   -!- FUNCTION: May be involved in the regulation of dopamine release
CC       and transport.
CC   -!- SUBUNIT: Interacts with UCHL1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O55042-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O55042-2; Sequence=VSP_025018, VSP_025019;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated, predominantly on serine residues.
CC       Phosphorylated on Tyr-125 upon osmotic stress (By similarity).
CC   -!- PTM: Ubiquitinated. The predominant conjugate is the
CC       diubiquitinated form (By similarity).
CC   -!- SIMILARITY: Belongs to the synuclein family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF044672; AAC00521.1; -; mRNA.
DR   EMBL; AF033261; AAD11254.1; -; mRNA.
DR   EMBL; AF179273; AAD56908.1; -; mRNA.
DR   EMBL; AF179272; AAD56907.1; -; Genomic_DNA.
DR   EMBL; AF179268; AAD56907.1; JOINED; Genomic_DNA.
DR   EMBL; AF179269; AAD56907.1; JOINED; Genomic_DNA.
DR   EMBL; AF179270; AAD56907.1; JOINED; Genomic_DNA.
DR   EMBL; AF179271; AAD56907.1; JOINED; Genomic_DNA.
DR   EMBL; AF163865; AAG30304.1; -; Genomic_DNA.
DR   EMBL; AK014472; BAB29375.1; -; mRNA.
DR   EMBL; AK156316; BAE33670.1; -; mRNA.
DR   EMBL; BC046764; AAH46764.1; -; mRNA.
DR   EMBL; AF277451; AAG44833.1; -; Genomic_DNA.
DR   IPI; IPI00115157; -.
DR   IPI; IPI00845803; -.
DR   RefSeq; NP_001035916.1; NM_001042451.1.
DR   RefSeq; NP_033247.1; NM_009221.2.
DR   UniGene; Mm.17484; -.
DR   ProteinModelPortal; O55042; -.
DR   SMR; O55042; 1-140.
DR   MINT; MINT-2736846; -.
DR   STRING; O55042; -.
DR   PhosphoSite; O55042; -.
DR   PRIDE; O55042; -.
DR   Ensembl; ENSMUST00000114268; ENSMUSP00000109907; ENSMUSG00000025889.
DR   GeneID; 20617; -.
DR   KEGG; mmu:20617; -.
DR   UCSC; uc009cdn.1; mouse.
DR   CTD; 20617; -.
DR   MGI; MGI:1277151; Snca.
DR   eggNOG; roNOG16930; -.
DR   GeneTree; ENSGT00390000016161; -.
DR   HOGENOM; HBG715579; -.
DR   HOVERGEN; HBG000481; -.
DR   InParanoid; O55042; -.
DR   OMA; PENEAYE; -.
DR   OrthoDB; EOG4FFD3B; -.
DR   PhylomeDB; O55042; -.
DR   NextBio; 298995; -.
DR   PMAP-CutDB; O55042; -.
DR   ArrayExpress; O55042; -.
DR   Bgee; O55042; -.
DR   CleanEx; MM_SNCA; -.
DR   Genevestigator; O55042; -.
DR   GermOnline; ENSMUSG00000025889; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
DR   GO; GO:0050544; F:arachidonic acid binding; IDA:MGI.
DR   GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR   GO; GO:0008344; P:adult locomotory behavior; IGI:MGI.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IMP:MGI.
DR   GO; GO:0042416; P:dopamine biosynthetic process; IMP:MGI.
DR   GO; GO:0006631; P:fatty acid metabolic process; IMP:MGI.
DR   GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
DR   GO; GO:0001774; P:microglial cell activation; IMP:MGI.
DR   GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; IMP:MGI.
DR   GO; GO:0007006; P:mitochondrial membrane organization; IMP:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptosis; IGI:MGI.
DR   GO; GO:0006638; P:neutral lipid metabolic process; IMP:MGI.
DR   GO; GO:0006644; P:phospholipid metabolic process; IMP:MGI.
DR   GO; GO:0001956; P:positive regulation of neurotransmitter secretion; IDA:MGI.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:BHF-UCL.
DR   GO; GO:0050812; P:regulation of acyl-CoA biosynthetic process; IDA:MGI.
DR   GO; GO:0014059; P:regulation of dopamine secretion; IGI:MGI.
DR   GO; GO:0060079; P:regulation of excitatory postsynaptic membrane potential; IMP:MGI.
DR   GO; GO:0014048; P:regulation of glutamate secretion; IMP:MGI.
DR   GO; GO:0040012; P:regulation of locomotion; IMP:MGI.
DR   GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:MGI.
DR   GO; GO:0043030; P:regulation of macrophage activation; IMP:MGI.
DR   GO; GO:0042493; P:response to drug; IMP:MGI.
DR   GO; GO:0001963; P:synaptic transmission, dopaminergic; IMP:MGI.
DR   GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:UniProtKB.
DR   InterPro; IPR001058; Synuclein.
DR   InterPro; IPR002460; Synuclein_alpha.
DR   Gene3D; G3DSA:1.10.287.700; Synuclein; 1.
DR   PANTHER; PTHR13820; Synuclein; 1.
DR   Pfam; PF01387; Synuclein; 1.
DR   PRINTS; PR01212; ASYNUCLEIN.
DR   PRINTS; PR01211; SYNUCLEIN.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Direct protein sequencing;
KW   Phosphoprotein; Repeat; Ubl conjugation.
FT   CHAIN         1    140       Alpha-synuclein.
FT                                /FTId=PRO_0000184026.
FT   REPEAT       20     30       1.
FT   REPEAT       31     41       2.
FT   REPEAT       42     56       3; approximate.
FT   REPEAT       57     67       4.
FT   REGION       20     67       4 X 11 AA tandem repeats of [EGS]-K-T-K-
FT                                [EQ]-[GQ]-V-X(4).
FT   MOD_RES     125    125       Phosphotyrosine (By similarity).
FT   VAR_SEQ     103    121       GEEGYPQEGILEDMPVDPG -> VWLPVLCSVITLDTMSLH
FT                                A (in isoform 2).
FT                                /FTId=VSP_025018.
FT   VAR_SEQ     122    140       Missing (in isoform 2).
FT                                /FTId=VSP_025019.
FT   CONFLICT     58     58       K -> T (in Ref. 1; AAC00521).
SQ   SEQUENCE   140 AA;  14485 MW;  1FFD19D7E15E636C CRC64;
     MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVTTVAEKTK
     EQVTNVGGAV VTGVTAVAQK TVEGAGNIAA ATGFVKKDQM GKGEEGYPQE GILEDMPVDP
     GSEAYEMPSE EGYQDYEPEA
//
ID   IMPCT_MOUSE             Reviewed;         318 AA.
AC   O55091; Q3UUR6; Q9EQH0;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1999, sequence version 2.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Protein IMPACT;
DE   AltName: Full=Imprinted and ancient gene protein;
GN   Name=Impact;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], IMPRINTING, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=97404381; PubMed=9256468; DOI=10.1073/pnas.94.17.9249;
RA   Hagiwara Y., Hirai M., Nishiyama K., Kanazawa I., Ueda T., Sakaki Y.,
RA   Ito T.;
RT   "Screening for imprinted genes by allelic message display:
RT   identification of a paternally expressed gene impact on mouse
RT   chromosome 18.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:9249-9254(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IMPRINTING.
RC   STRAIN=129/Sv;
RX   MEDLINE=20568479; PubMed=11116084; DOI=10.1101/gr.139200;
RA   Okamura K., Hagiwara-Takeuchi Y., Li T., Vu T.H., Hirai M.,
RA   Hattori M., Sakaki Y., Hoffman A.R., Ito T.;
RT   "Comparative genome analysis of the mouse imprinted gene impact and
RT   its nonimprinted human homolog IMPACT: toward the structural basis for
RT   species-specific imprinting.";
RL   Genome Res. 10:1878-1889(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-305.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   IMPRINTING.
RX   PubMed=15871461; DOI=10.1093/dnares/11.6.381;
RA   Okamura K., Yamada Y., Sakaki Y., Ito T.;
RT   "An evolutionary scenario for genomic imprinting of Impact lying
RT   between nonimprinted neighbors.";
RL   DNA Res. 11:381-390(2004).
RN   [6]
RP   FUNCTION, INTERACTION WITH GCN1L1, AND TISSUE SPECIFICITY.
RX   PubMed=15937339; DOI=10.1074/jbc.M408571200;
RA   Pereira C.M., Sattlegger E., Jiang H.-Y., Longo B.M., Jaqueta C.B.,
RA   Hinnebusch A.G., Wek R.C., Mello L.E.A.M., Castilho B.A.;
RT   "IMPACT, a protein preferentially expressed in the mouse brain, binds
RT   GCN1 and inhibits GCN2 activation.";
RL   J. Biol. Chem. 280:28316-28323(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=18260151; DOI=10.1002/cne.21652;
RA   Bittencourt S., Pereira C.M., Avedissian M., Delamano A.,
RA   Mello L.E.A.M., Castilho B.A.;
RT   "Distribution of the protein IMPACT, an inhibitor of GCN2, in the
RT   mouse, rat, and marmoset brain.";
RL   J. Comp. Neurol. 507:1811-1830(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Translational regulator that ensures constant high
CC       levels of translation under amino acid starvation. Acts by
CC       interacting with GCN1/GCN1L1, thereby preventing activation of
CC       GCN2 protein kinases (EIF2AK1 to 4) and subsequent down-regulation
CC       of protein synthesis. May be required to regulate tranlation in
CC       specific neuronal cells under amino acid starvation conditions by
CC       preventing GCN2 activation and therefore ATF4 synthesis.
CC   -!- SUBUNIT: Interacts with GCN1/GCN1L1.
CC   -!- TISSUE SPECIFICITY: Present in neurons in most areas of the brain.
CC       Present at high level in hypothalamus, particularly in the
CC       suprachiasmatic nucleus (at protein level). Preferentially
CC       expressed in brain, with a weaker expression in other tissues.
CC   -!- DEVELOPMENTAL STAGE: Detected in embryos at days 7, 11, 15, and
CC       17.
CC   -!- MISCELLANEOUS: The Impact locus is imprinted. Paternal inherited
CC       gene is expressed, while the maternal inherited gene is silenced.
CC       In contrast with most imprinted genes, neighboring genes are
CC       apparently not imprinted.
CC   -!- SIMILARITY: Belongs to the IMPACT family.
CC   -!- SIMILARITY: Contains 1 RWD domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; D87973; BAA35139.1; -; mRNA.
DR   EMBL; AF232228; AAG23916.1; -; Genomic_DNA.
DR   EMBL; BC020524; AAH20524.1; -; mRNA.
DR   EMBL; AK138136; BAE23558.1; -; mRNA.
DR   IPI; IPI00319956; -.
DR   RefSeq; NP_032404.1; NM_008378.2.
DR   UniGene; Mm.480369; -.
DR   HSSP; Q5SJF5; 2CVE.
DR   ProteinModelPortal; O55091; -.
DR   SMR; O55091; 6-115, 177-296.
DR   STRING; O55091; -.
DR   PhosphoSite; O55091; -.
DR   PRIDE; O55091; -.
DR   Ensembl; ENSMUST00000025290; ENSMUSP00000025290; ENSMUSG00000024423.
DR   GeneID; 16210; -.
DR   KEGG; mmu:16210; -.
DR   UCSC; uc008eda.1; mouse.
DR   CTD; 16210; -.
DR   MGI; MGI:1098233; Impact.
DR   eggNOG; roNOG10000; -.
DR   GeneTree; ENSGT00390000017571; -.
DR   HOGENOM; HBG407584; -.
DR   HOVERGEN; HBG108005; -.
DR   InParanoid; O55091; -.
DR   OMA; LEEIYIQ; -.
DR   OrthoDB; EOG4C87ST; -.
DR   PhylomeDB; O55091; -.
DR   NextBio; 289165; -.
DR   ArrayExpress; O55091; -.
DR   Bgee; O55091; -.
DR   Genevestigator; O55091; -.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:MGI.
DR   GO; GO:0006446; P:regulation of translational initiation; IDA:MGI.
DR   InterPro; IPR001498; Impact_N.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR006575; RWD-domain.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   InterPro; IPR020569; UPF0029_Impact_CS.
DR   Gene3D; G3DSA:3.30.230.30; G3DSA:3.30.230.30; 1.
DR   Gene3D; G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.
DR   Pfam; PF05773; RWD; 1.
DR   Pfam; PF01205; UPF0029; 1.
DR   SMART; SM00591; RWD; 1.
DR   SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR   SUPFAM; SSF54495; UBQ-conjugat/RWD-like; 1.
DR   PROSITE; PS50908; RWD; 1.
DR   PROSITE; PS00910; UPF0029; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Translation regulation.
FT   CHAIN         1    318       Protein IMPACT.
FT                                /FTId=PRO_0000330851.
FT   DOMAIN       14    116       RWD.
FT   MOD_RES     137    137       Phosphoserine.
FT   CONFLICT    303    303       N -> S (in Ref. 2; AAG23916).
SQ   SEQUENCE   318 AA;  36276 MW;  F3A3688D87C88A40 CRC64;
     MAEEEVGNSQ RQSEEIEAMA AIYGEEWCVI DENAKIFCIR VTDFMDDPKW TLCLQVMLPS
     EYPGTAPPSY QLNAPWLKGQ ERADLSNSLE EIYVHNMGES ILYQWVEKIR DALIQKSQIT
     EPDPDVKKKT EEVEVESEED PILEHPPENP VKTLDLKISE ETQPETEELP PVAHGVPITD
     RRSTFQAHVA PVVCPEQVKL VLAKLYENKK IASATHNIYA YRIFCEDKQT FLQDCEDDGE
     TAAGGRLLHL MEILNVKNVM VVVSRWYGGI LLGPDRFKHI NNCARNILVE KNFTNTPDES
     TKNLGKKKVK KDKKKNDH
//
ID   STRN_MOUSE              Reviewed;         780 AA.
AC   O55106; B2RWV9;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   30-NOV-2010, entry version 80.
DE   RecName: Full=Striatin;
GN   Name=Strn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster; TISSUE=Brain;
RA   Moqrich A., Mattei M.-G., Bartoli M., Rakitina T., Baillat G.,
RA   Monneron A., Castets F.;
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=20347911; PubMed=10748158; DOI=10.1074/jbc.M909782199;
RA   Castets F., Rakitina T., Gaillard S., Moqrich A., Mattei M.-G.,
RA   Monneron A.;
RT   "Zinedin, SG2NA, and striatin are calmodulin-binding, WD repeat
RT   proteins principally expressed in the brain.";
RL   J. Biol. Chem. 275:19970-19977(2000).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Binds calmodulin in a calcium dependent manner. May
CC       function as scaffolding or signaling protein.
CC   -!- SUBUNIT: Interacts with protein phosphatase 2A (PP2A) (Potential).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Mainly expressed in brain but is also
CC       expressed at low levels in various tissues such as kidney, spleen,
CC       skeletal muscle and lung.
CC   -!- SIMILARITY: Belongs to the WD repeat striatin family.
CC   -!- SIMILARITY: Contains 6 WD repeats.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ223777; CAA11545.1; -; mRNA.
DR   EMBL; BC150727; AAI50728.1; -; mRNA.
DR   IPI; IPI00352986; -.
DR   UniGene; Mm.311915; -.
DR   UniGene; Mm.391038; -.
DR   ProteinModelPortal; O55106; -.
DR   SMR; O55106; 435-779.
DR   STRING; O55106; -.
DR   PhosphoSite; O55106; -.
DR   PRIDE; O55106; -.
DR   Ensembl; ENSMUST00000024881; ENSMUSP00000024881; ENSMUSG00000024077.
DR   MGI; MGI:1333757; Strn.
DR   eggNOG; roNOG05976; -.
DR   HOGENOM; HBG385782; -.
DR   HOVERGEN; HBG007117; -.
DR   InParanoid; O55106; -.
DR   PMAP-CutDB; O55106; -.
DR   ArrayExpress; O55106; -.
DR   Bgee; O55106; -.
DR   CleanEx; MM_STRN; -.
DR   Genevestigator; O55106; -.
DR   GermOnline; ENSMUSG00000024077; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR013258; Striatin_N.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF08232; Striatin; 1.
DR   Pfam; PF00400; WD40; 5.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 3.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Calmodulin-binding; Coiled coil; Cytoplasm; Membrane;
KW   Phosphoprotein; Repeat; WD repeat.
FT   CHAIN         1    780       Striatin.
FT                                /FTId=PRO_0000051233.
FT   REPEAT      461    500       WD 1.
FT   REPEAT      514    553       WD 2.
FT   REPEAT      567    606       WD 3.
FT   REPEAT      662    701       WD 4.
FT   REPEAT      704    743       WD 5.
FT   REPEAT      750    779       WD 6.
FT   REGION       55     63       Caveolin-binding (Potential).
FT   REGION      149    166       Calmodulin-binding (Potential).
FT   COILED       53    120       Potential.
FT   COMPBIAS     37     45       Poly-Ala.
FT   MOD_RES     245    245       Phosphoserine.
FT   MOD_RES     264    264       Phosphoserine.
FT   MOD_RES     689    689       N6-acetyllysine (By similarity).
SQ   SEQUENCE   780 AA;  86014 MW;  DBD1104FF9E5BC08 CRC64;
     MDEQAGPGVF FSNNHPGAGG AKGLGPLAEA AAAGDGAAAA GAARAQYSLP GILHFLQHEW
     ARFEVERAQW EVERAELQAQ IAFLQGERKG QENLKKDLVR RIKMLEYALK QERAKYHKLK
     YGTELNQGDM KPPSYDSDEG NETEVQPQQN SQLMWKQGRQ LLRQYLQEVG YTDTILDVKS
     KRVRALLGFS SDVTDREDDK NQDSVINGTE AEVKETAMIG KSELTDSASV LDNFKFLESA
     AADFSDEDED EDTDGRAKSV IDTSTIVRKK ALPDTSEDRD TKEALKEFDF LVTSEEGDNE
     SRSAGDGTDW EKEDQCLTPE AWNVDQGVIS KLKEQYKKER KGKKGVKRPN RSKLQDMLAN
     LRDVDELPSL QPSVGSPSRP SSSRLPEQEL SRADEVEALT FPPSSGKSFI MGADEALESE
     LGLGELAGLT VANEADSLAY DIANNKDALR KTWNPKFTLR SHFDGIRALA FHPIEPVLIT
     ASEDHTLKMW NLQKTAPAKK STSLDVEPIY TFRAHKGPVL CVVMSSNGEQ CYSGGTDGRI
     QSWSTTNPNV DPYDAYDPSV LRGPLLGHTD AVWGLAYSAA HQRLLSCSAD GTLRLWNTTE
     VAPALSVFND NQELGIPASV DLVSSDPSHM VASFSKGYTS IFNMETQQRV LTLESNVDST
     SSSSCQINRV ISHPTLPISI TAHEDRHIKF YDNNTGKLIH SMVAHLEAVT SLAVDPNGLY
     LMSGSHDCSI RLWNLESKTC IQEFTAHRKK FEESIHDVAF HPSKCYIASA GADALAKVFV
//
ID   SEPT7_MOUSE             Reviewed;         436 AA.
AC   O55131;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Septin-7;
DE   AltName: Full=CDC10 protein homolog;
GN   Name=Sept7; Synonyms=Cdc10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=99023757; PubMed=9804986; DOI=10.1016/S0167-4781(98)00183-3;
RA   Soulier S., Vilotte J.-L.;
RT   "Sequence of murine CDC10 cDNA, gene organization and expression
RT   analysis.";
RL   Biochim. Biophys. Acta 1442:339-346(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 25-41; 63-95; 137-146; 186-207; 221-234; 298-309;
RP   333-342 AND 416-424, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   INTERACTION WITH SEPT2 AND SEPT5.
RX   PubMed=11739749; DOI=10.1128/MCB.22.1.378-387.2002;
RA   Peng X.-R., Jia Z., Zhang Y., Ware J., Trimble W.S.;
RT   "The septin CDCrel-1 is dispensable for normal development and
RT   neurotransmitter release.";
RL   Mol. Cell. Biol. 22:378-387(2002).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17546647; DOI=10.1002/humu.20554;
RA   Sudo K., Ito H., Iwamoto I., Morishita R., Asano T., Nagata K.;
RT   "SEPT9 sequence alternations causing hereditary neuralgic amyotrophy
RT   are associated with altered interactions with SEPT4/SEPT11 and
RT   resistance to Rho/Rhotekin-signaling.";
RL   Hum. Mutat. 28:1005-1013(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-227, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333 AND THR-425, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-425, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Filament-forming cytoskeletal GTPase. Required for
CC       normal organization of the actin cytoskeleton. Required for normal
CC       progress through mitosis. Involved in cytokinesis. Required for
CC       normal association of CENPE with the kinetochore (By similarity).
CC   -!- SUBUNIT: Septins polymerize into heterooligomeric protein
CC       complexes that form filaments, and associate with cellular
CC       membranes, actin filaments and microtubules. GTPase activity is
CC       required for filament formation. Filaments are assembled from
CC       asymmetrical heterotrimers, composed of SEPT2, SEPT6 and SEPT7
CC       that associate head-to-head to form a hexameric unit. Within the
CC       trimer, directly interacts with SEPT6, while interaction with
CC       SEPT2 seems indirect. In the absence of SEPT6, forms homodimers.
CC       Interacts directly with CENPE and links CENPE to septin filaments
CC       composed of SEPT2, SEPT6 and SEPT7. Interacts with SEPT5, SEPT8,
CC       SEPT9 and SEPT11 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Chromosome, centromere,
CC       kinetochore (By similarity). Cytoplasm, cytoskeleton, spindle (By
CC       similarity). Cleavage furrow (By similarity). Midbody (By
CC       similarity). Note=Distributed throughout the cytoplasm in
CC       prometaphase cells. Associated with the spindle during metaphase.
CC       Associated with the central spindle and at the cleavage furrow in
CC       anaphase cells. Detected at the midbody in telophase (By
CC       similarity). Associated with actin stress fibers (By similarity).
CC   -!- MISCELLANEOUS: Coordinated expression with SEPT2 and SEPT6 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the septin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ223782; CAA11547.1; -; Genomic_DNA.
DR   EMBL; AJ223783; CAA11547.1; JOINED; Genomic_DNA.
DR   EMBL; AJ223784; CAA11547.1; JOINED; Genomic_DNA.
DR   EMBL; AJ223785; CAA11547.1; JOINED; Genomic_DNA.
DR   EMBL; AJ223786; CAA11547.1; JOINED; Genomic_DNA.
DR   EMBL; AJ223787; CAA11547.1; JOINED; Genomic_DNA.
DR   EMBL; AJ223788; CAA11547.1; JOINED; Genomic_DNA.
DR   EMBL; AJ223789; CAA11547.1; JOINED; Genomic_DNA.
DR   EMBL; AJ223790; CAA11547.1; JOINED; Genomic_DNA.
DR   EMBL; AJ223791; CAA11547.1; JOINED; Genomic_DNA.
DR   EMBL; AJ223792; CAA11547.1; JOINED; Genomic_DNA.
DR   EMBL; AJ223793; CAA11547.1; JOINED; Genomic_DNA.
DR   EMBL; AJ223794; CAA11547.1; JOINED; Genomic_DNA.
DR   EMBL; BC058587; AAH58587.1; -; mRNA.
DR   IPI; IPI00874440; -.
DR   UniGene; Mm.270259; -.
DR   ProteinModelPortal; O55131; -.
DR   SMR; O55131; 33-314.
DR   STRING; O55131; -.
DR   PhosphoSite; O55131; -.
DR   PRIDE; O55131; -.
DR   Ensembl; ENSMUST00000060080; ENSMUSP00000052745; ENSMUSG00000001833.
DR   MGI; MGI:1335094; Sept7.
DR   eggNOG; roNOG10802; -.
DR   HOVERGEN; HBG065093; -.
DR   OrthoDB; EOG4894MJ; -.
DR   PhylomeDB; O55131; -.
DR   ArrayExpress; O55131; -.
DR   Bgee; O55131; -.
DR   CleanEx; MM_SEPT7; -.
DR   Genevestigator; O55131; -.
DR   GermOnline; ENSMUSG00000001833; Mus musculus.
DR   GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR   GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0031105; C:septin complex; IEA:InterPro.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   InterPro; IPR000038; Cell_Div_GTP-bd.
DR   InterPro; IPR016491; Septin.
DR   InterPro; IPR008115; Septin7.
DR   PANTHER; PTHR18884; Cell_Div_GTP_bd; 1.
DR   Pfam; PF00735; Septin; 1.
DR   PIRSF; PIRSF006698; Septin; 1.
DR   PRINTS; PR01742; SEPTIN7.
PE   1: Evidence at protein level;
KW   Acetylation; Cell cycle; Cell division; Centromere; Chromosome;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   GTP-binding; Kinetochore; Mitosis; Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1    436       Septin-7.
FT                                /FTId=PRO_0000173529.
FT   NP_BIND      56     63       GTP (By similarity).
FT   NP_BIND     194    202       GTP (By similarity).
FT   COILED      331    436       Potential.
FT   BINDING      89     89       GTP (By similarity).
FT   BINDING     115    115       GTP; via amide nitrogen (By similarity).
FT   BINDING     249    249       GTP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     264    264       GTP (By similarity).
FT   MOD_RES      29     29       Phosphotyrosine.
FT   MOD_RES     185    185       N6-acetyllysine (By similarity).
FT   MOD_RES     212    212       N6-acetyllysine (By similarity).
FT   MOD_RES     227    227       Phosphothreonine.
FT   MOD_RES     318    318       Phosphotyrosine (By similarity).
FT   MOD_RES     333    333       Phosphoserine.
FT   MOD_RES     422    422       Phosphoserine (By similarity).
FT   MOD_RES     423    423       Phosphoserine (By similarity).
FT   MOD_RES     425    425       Phosphothreonine.
SQ   SEQUENCE   436 AA;  50550 MW;  1028CCF14023059C CRC64;
     MSVSARSAAA EERSVNCGTM AQPKNLEGYV GFANLPNQVY RKSVKRGFEF TLMVVGESGL
     GKSTLINSLF LTDLYSPEYP GPSHRIKKTV QVEQSKVLIK EGGVQLLLTI VDTPGFGDAV
     DNSNCWQPVI DYIDSKFEDY LNAESRVNRR QMPDNRVQCC LYFIAPSGHG LKPLDIEFMK
     RLHEKVNIIP LIAKADTLTP EECQQFKKQI MKEIQEHKIK IYEFPETDDE EENKLVKKIK
     DRLPLAVVGS NTIIEVNGKR VRGRQYPWGV AEVENGEHCD FTILRNMLIR THMQDLKDVT
     NNVHYENYRS RKLAAVTYNG VDNNKNKGQL TKSPLAQMEE ERREHVAKMK KMEMEMEQVF
     EMKVKEKVQK LKDSEAELQR RHEQMKKNLE AQHKELEEKR RQFEEEKANW EAQQRILEQQ
     NSSRTLEKNK KKGKIF
//
ID   ACOT1_MOUSE             Reviewed;         419 AA.
AC   O55137; Q549A9;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Acyl-coenzyme A thioesterase 1;
DE            Short=Acyl-CoA thioesterase 1;
DE            EC=3.1.2.2;
DE   AltName: Full=CTE-I;
DE   AltName: Full=Inducible cytosolic acyl-coenzyme A thioester hydrolase;
DE   AltName: Full=Long chain acyl-CoA thioester hydrolase;
DE            Short=Long chain acyl-CoA hydrolase;
GN   Name=Acot1; Synonyms=Cte1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6;
RX   MEDLINE=20036578; PubMed=10567408; DOI=10.1074/jbc.274.48.34317;
RA   Hunt M.C., Nousiainen S.E.B., Huttunen M.K., Orii K.E., Svensson L.T.,
RA   Alexson S.E.H.;
RT   "Peroxisome proliferator-induced long chain acyl-CoA thioesterases
RT   comprise a highly conserved novel multi-gene family involved in lipid
RT   metabolism.";
RL   J. Biol. Chem. 274:34317-34326(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, INDUCTION, AND TISSUE
RP   SPECIFICITY.
RX   MEDLINE=21228826; PubMed=11330065; DOI=10.1385/CBB:32:1-3:317;
RA   Hunt M.C., Lindquist P.J.G., Nousiainen S.E.B., Huttunen M.K.,
RA   Orii K.E., Svensson L.T., Aoyama T., Hashimoto T., Diczfalusy U.,
RA   Alexson S.E.H.;
RT   "Acyl-CoA thioesterases belong to a novel gene family of peroxisome
RT   proliferator-regulated enzymes involved in lipid metabolism.";
RL   Cell Biochem. Biophys. 32:317-324(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Liver;
RX   MEDLINE=98149679; PubMed=9490035;
RX   DOI=10.1046/j.1432-1327.1998.2510631.x;
RA   Lindquist P.J.G., Svensson L.T., Alexson S.E.H.;
RT   "Molecular cloning of the peroxisome proliferator-induced 46-kDa
RT   cytosolic acyl-CoA thioesterase from mouse and rat liver --recombinant
RT   expression in Escherichia coli, tissue expression, and nutritional
RT   regulation.";
RL   Eur. J. Biochem. 251:631-640(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   ACTIVE SITES, MUTAGENESIS OF SER-232; ASP-324 AND HIS-358, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   MEDLINE=21671314; PubMed=11694534; DOI=10.1074/jbc.M109040200;
RA   Huhtinen K., O'Byrne J., Lindquist P.J.G., Contreras J.A.,
RA   Alexson S.E.H.;
RT   "The peroxisome proliferator-induced cytosolic type I acyl-CoA
RT   thioesterase (CTE-I) is a serine-histidine-aspartic acid alpha /beta
RT   hydrolase.";
RL   J. Biol. Chem. 277:3424-3432(2002).
CC   -!- FUNCTION: Acyl-CoA thioesterases are a group of enzymes that
CC       catalyze the hydrolysis of acyl-CoAs to the free fatty acid and
CC       coenzyme A (CoASH), providing the potential to regulate
CC       intracellular levels of acyl-CoAs, free fatty acids and CoASH.
CC       True acyl-CoA thioesterase being highly specific for saturated
CC       C12-C20 acyl-CoAs, with only a very low activity with decanoyl-CoA
CC       as substrate. Most active on myristoyl- and palmitoyl-CoA.
CC       Introduction of one or two double bonds decreases the activity to
CC       about half. No detectable activity with bile acid CoAs such as
CC       choloyl-CoA and chenodeoxycholoyl-CoA.
CC   -!- CATALYTIC ACTIVITY: Palmitoyl-CoA + H(2)O = CoA + palmitate.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.6 uM for palmitoyl-CoA;
CC         Vmax=1.2 umol/min/mg enzyme with palmitoyl-CoA as substrate;
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Expressed in heart, kidney, brown adipose
CC       tissue, white adipose tissue, adrenal gland and muscle.
CC   -!- INDUCTION: In the liver, by peroxisome proliferator (Clofibrate)
CC       treatment, via the peroxisome proliferator-activated receptors
CC       (PPARs) or fasting for 24 hours.
CC   -!- SIMILARITY: Belongs to the C/M/P thioester hydrolase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF180795; AAF13870.1; -; Genomic_DNA.
DR   EMBL; AF180793; AAF13870.1; JOINED; Genomic_DNA.
DR   EMBL; AF180794; AAF13870.1; JOINED; Genomic_DNA.
DR   EMBL; Y14004; CAA74327.1; -; mRNA.
DR   EMBL; BC028261; AAH28261.1; -; mRNA.
DR   IPI; IPI00115871; -.
DR   RefSeq; NP_036136.1; NM_012006.2.
DR   UniGene; Mm.1978; -.
DR   ProteinModelPortal; O55137; -.
DR   SMR; O55137; 1-408.
DR   STRING; O55137; -.
DR   PhosphoSite; O55137; -.
DR   UCD-2DPAGE; O55137; -.
DR   PRIDE; O55137; -.
DR   Ensembl; ENSMUST00000085210; ENSMUSP00000082306; ENSMUSG00000072949.
DR   GeneID; 26897; -.
DR   KEGG; mmu:26897; -.
DR   UCSC; uc007oeb.1; mouse.
DR   CTD; 26897; -.
DR   MGI; MGI:1349396; Acot1.
DR   eggNOG; roNOG10401; -.
DR   HOVERGEN; HBG000331; -.
DR   InParanoid; O55137; -.
DR   OMA; IPPVTIL; -.
DR   OrthoDB; EOG4QC15F; -.
DR   BRENDA; 3.1.2.2; 244.
DR   NextBio; 304741; -.
DR   ArrayExpress; O55137; -.
DR   Bgee; O55137; -.
DR   CleanEx; MM_ACOT1; -.
DR   Genevestigator; O55137; -.
DR   GermOnline; ENSMUSG00000021226; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0004091; F:carboxylesterase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:EC.
DR   GO; GO:0006637; P:acyl-CoA metabolic process; TAS:MGI.
DR   GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:MGI.
DR   InterPro; IPR016662; Acyl-CoA_thioEstase_long-chain.
DR   InterPro; IPR014940; BAAT_C.
DR   InterPro; IPR006862; Thio_Ohase/aa_AcTrfase.
DR   Pfam; PF08840; BAAT_C; 1.
DR   Pfam; PF04775; Bile_Hydr_Trans; 1.
DR   PIRSF; PIRSF016521; Acyl-CoA_hydro; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Serine esterase.
FT   CHAIN         1    419       Acyl-coenzyme A thioesterase 1.
FT                                /FTId=PRO_0000202156.
FT   ACT_SITE    232    232       Charge relay system.
FT   ACT_SITE    324    324       Charge relay system.
FT   ACT_SITE    358    358       Charge relay system.
FT   MUTAGEN     232    232       S->A: Abolishes activity.
FT   MUTAGEN     232    232       S->C: Retains 2% of the initial activity;
FT                                deacylation of the acyl-enzyme
FT                                intermediate becomes rate-limiting.
FT   MUTAGEN     324    324       D->A: Abolishes activity.
FT   MUTAGEN     358    358       H->Q: Abolishes activity.
SQ   SEQUENCE   419 AA;  46136 MW;  57346B6177471CFB CRC64;
     MEATLNLEPS GRSCWDEPLS IAVRGLAPEQ PVTLRSVLRD EKGALFRAHA RYRADSHGEL
     DLARTPALGG SFSGLEPMGL LWAMEPDRPF WRLVKRDVQT PFVVELEVLD GHEPDGGQRL
     AHAVHERHFL APGVRRVPVR EGRVRATLFL PPEPGPFPGI IDLFGVGGGL LEYRASLLAG
     KGFAVMALAY YNYDDLPKNM ETMHMEYFEE AVNYLRSHPE VKGPGIGLLG ISKGGELGLA
     MASFLKGITA AVVINGSVAA VGNTISYKDE TIPPVTILRN QVKMTKDGLK DVVDALQSPL
     VDKKSFIPVE RSDTTFLFLV GQDDHNWKSE FYADEISKRL QAHGKEKPQI ICYPAAGHYI
     EPPYFPLCSA GMHLLVGANI TFGGEPKPHA MAQLDAWQQL QTFFHKQLGS ECLHVSPKI
//
ID   AT2A2_MOUSE             Reviewed;        1044 AA.
AC   O55143; Q9R2A9; Q9WUT5;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   08-MAR-2011, entry version 120.
DE   RecName: Full=Sarcoplasmic/endoplasmic reticulum calcium ATPase 2;
DE            Short=SERCA2;
DE            Short=SR Ca(2+)-ATPase 2;
DE            EC=3.6.3.8;
DE   AltName: Full=Calcium pump 2;
DE   AltName: Full=Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform;
DE   AltName: Full=Endoplasmic reticulum class 1/2 Ca(2+) ATPase;
GN   Name=Atp2a2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS SERCA2A AND
RP   SERCA2B).
RC   STRAIN=129/SvJ;
RX   MEDLINE=20122169; PubMed=10656932; DOI=10.1007/s003350010030;
RA   Ver Heyen M., Reed T.D., Blough R.E., Zilberman A.L., Loukianov E.,
RA   Van Baelen K., Raeymaekers L., Periasamy M., Wutack F.;
RT   "Structure and organization of the mouse Atp2a2 gene encoding the
RT   sarco(endo)plasmic reticulum Ca(2+)-ATPase 2 (SERCA2) isoforms.";
RL   Mamm. Genome 11:159-163(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SERCA2B).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 604-611 AND 638-655, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   INTERACTION WITH TRAM2.
RX   PubMed=14749390; DOI=10.1128/MCB.24.4.1758-1768.2004;
RA   Stefanovic B., Stefanovic L., Schnabl B., Bataller R., Brenner D.A.;
RT   "TRAM2 protein interacts with endoplasmic reticulum Ca2+ pump Serca2b
RT   and is necessary for collagen type I synthesis.";
RL   Mol. Cell. Biol. 24:1758-1768(2004).
RN   [5]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-143, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Heart;
RX   PubMed=17451654; DOI=10.1016/j.bbrc.2007.04.015;
RA   Jeon H.B., Choi E.S., Yoon J.H., Hwang J.H., Chang J.W., Lee E.K.,
RA   Choi H.W., Park Z.-Y., Yoo Y.J.;
RT   "A proteomics approach to identify the ubiquitinated proteins in mouse
RT   heart.";
RL   Biochem. Biophys. Res. Commun. 357:731-736(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-537, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis
CC       of ATP coupled with the translocation of calcium from the cytosol
CC       to the sarcoplasmic reticulum lumen. Isoform SERCA2A is involved
CC       in the regulation of the contraction/relaxation cycle (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + Ca(2+)(Cis) = ADP + phosphate +
CC       Ca(2+)(Trans).
CC   -!- ENZYME REGULATION: Reversibly inhibited by phospholamban (PLN) at
CC       low calcium concentrations. Dephosphorylated PLN decreases the
CC       apparent affinity of the ATPase for calcium. This inhibition is
CC       regulated by the phosphorylation of PLN (By similarity).
CC   -!- SUBUNIT: Associated with phospholamban (PLN) (By similarity).
CC       Isoform SERCA2B interacts with TRAM2 (via C-terminus). Interacts
CC       with HAX1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein. Sarcoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=SERCA2B; Synonyms=ATP2A2B;
CC         IsoId=O55143-1; Sequence=Displayed;
CC       Name=SERCA2A; Synonyms=ATP2A2A;
CC         IsoId=O55143-2; Sequence=VSP_000359;
CC   -!- TISSUE SPECIFICITY: Isoform SERCA2A is highly expressed in heart
CC       and slow twitch skeletal muscle. Isoform SERCA2B is widely
CC       expressed.
CC   -!- PTM: Nitrated under oxidative stress. Nitration on the two
CC       tyrosine residues inhibits catalytic activity (By similarity).
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       (TC 3.A.3) family. Type IIA subfamily.
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DR   EMBL; AJ131821; CAB72436.1; -; mRNA.
DR   EMBL; AJ223584; CAA11450.1; -; mRNA.
DR   EMBL; AF029982; AAD01889.1; -; Genomic_DNA.
DR   EMBL; AJ131870; CAB41017.1; -; Genomic_DNA.
DR   EMBL; AJ131870; CAB41018.1; -; Genomic_DNA.
DR   EMBL; BC054531; AAH54531.1; -; mRNA.
DR   EMBL; BC054748; AAH54748.1; -; mRNA.
DR   IPI; IPI00338964; -.
DR   IPI; IPI00468900; -.
DR   RefSeq; NP_001103610.1; NM_001110140.3.
DR   RefSeq; NP_033852.1; NM_009722.3.
DR   UniGene; Mm.227583; -.
DR   ProteinModelPortal; O55143; -.
DR   SMR; O55143; 1-992.
DR   STRING; O55143; -.
DR   PhosphoSite; O55143; -.
DR   PRIDE; O55143; -.
DR   Ensembl; ENSMUST00000031423; ENSMUSP00000031423; ENSMUSG00000029467.
DR   Ensembl; ENSMUST00000100740; ENSMUSP00000098306; ENSMUSG00000029467.
DR   GeneID; 11938; -.
DR   KEGG; mmu:11938; -.
DR   UCSC; uc008zli.1; mouse.
DR   CTD; 11938; -.
DR   MGI; MGI:88110; Atp2a2.
DR   GeneTree; ENSGT00560000076887; -.
DR   HOVERGEN; HBG105648; -.
DR   InParanoid; O55143; -.
DR   OMA; PNKPSRT; -.
DR   OrthoDB; EOG4SXNBQ; -.
DR   PhylomeDB; O55143; -.
DR   BRENDA; 3.6.3.8; 244.
DR   NextBio; 280039; -.
DR   ArrayExpress; O55143; -.
DR   Bgee; O55143; -.
DR   Genevestigator; O55143; -.
DR   GermOnline; ENSMUSG00000029467; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005388; F:calcium-transporting ATPase activity; IDA:MGI.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:MGI.
DR   GO; GO:0006984; P:ER-nucleus signaling pathway; IMP:MGI.
DR   GO; GO:0045822; P:negative regulation of heart contraction; IGI:MGI.
DR   GO; GO:0006937; P:regulation of muscle contraction; TAS:MGI.
DR   GO; GO:0002026; P:regulation of the force of heart contraction; IGI:MGI.
DR   InterPro; IPR023306; ATPase_cation_domN.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR005782; ATPase_P-typ_Ca-transp.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023300; ATPase_P-typ_cyto_domA.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR000695; ATPase_P-typ_H-transp.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Gene3D; G3DSA:2.70.150.10; ATPase_P-typ_cyto_domA; 2.
DR   Gene3D; G3DSA:3.40.1110.10; ATPase_P-typ_cyto_domN; 1.
DR   Gene3D; G3DSA:1.20.1110.10; ATPase_P-typ_TM_dom; 2.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81660; ATPase_cation_domN; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01116; ATPase-IIA1_Ca; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 4.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Calcium;
KW   Calcium transport; Direct protein sequencing; Endoplasmic reticulum;
KW   Hydrolase; Ion transport; Isopeptide bond; Magnesium; Membrane;
KW   Metal-binding; Nitration; Nucleotide-binding; Phosphoprotein;
KW   Sarcoplasmic reticulum; Transmembrane; Transmembrane helix; Transport;
KW   Ubl conjugation.
FT   CHAIN         1   1044       Sarcoplasmic/endoplasmic reticulum
FT                                calcium ATPase 2.
FT                                /FTId=PRO_0000046197.
FT   TOPO_DOM      1     48       Cytoplasmic (By similarity).
FT   TRANSMEM     49     69       Helical; Name=1; (By similarity).
FT   TOPO_DOM     70     89       Lumenal (By similarity).
FT   TRANSMEM     90    110       Helical; Name=2; (By similarity).
FT   TOPO_DOM    111    253       Cytoplasmic (By similarity).
FT   TRANSMEM    254    273       Helical; Name=3; (By similarity).
FT   TOPO_DOM    274    295       Lumenal (By similarity).
FT   TRANSMEM    296    313       Helical; Name=4; (By similarity).
FT   TOPO_DOM    314    756       Cytoplasmic (By similarity).
FT   TRANSMEM    757    776       Helical; Name=5; (By similarity).
FT   TOPO_DOM    777    786       Lumenal (By similarity).
FT   TRANSMEM    787    807       Helical; Name=6; (By similarity).
FT   TOPO_DOM    808    827       Cytoplasmic (By similarity).
FT   TRANSMEM    828    850       Helical; Name=7; (By similarity).
FT   TOPO_DOM    851    896       Lumenal (By similarity).
FT   TRANSMEM    897    916       Helical; Name=8; (By similarity).
FT   TOPO_DOM    917    929       Cytoplasmic (By similarity).
FT   TRANSMEM    930    948       Helical; Name=9; (By similarity).
FT   TOPO_DOM    949    963       Lumenal (By similarity).
FT   TRANSMEM    964    984       Helical; Name=10; (By similarity).
FT   TOPO_DOM    985   1044       Cytoplasmic (By similarity).
FT   REGION      370    400       Interacts with phospholamban 1 (By
FT                                similarity).
FT   REGION      575    594       Interacts with HAX1 (By similarity).
FT   REGION      787    807       Interacts with phospholamban 2 (By
FT                                similarity).
FT   ACT_SITE    351    351       4-aspartylphosphate intermediate (By
FT                                similarity).
FT   METAL       304    304       Calcium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       305    305       Calcium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       307    307       Calcium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       309    309       Calcium 2 (By similarity).
FT   METAL       702    702       Magnesium (By similarity).
FT   METAL       706    706       Magnesium (By similarity).
FT   METAL       767    767       Calcium 1 (By similarity).
FT   METAL       770    770       Calcium 1 (By similarity).
FT   METAL       795    795       Calcium 2 (By similarity).
FT   METAL       798    798       Calcium 1 (By similarity).
FT   METAL       799    799       Calcium 1 (By similarity).
FT   METAL       799    799       Calcium 2 (By similarity).
FT   METAL       907    907       Calcium 1 (By similarity).
FT   MOD_RES     294    294       Nitrated tyrosine (By similarity).
FT   MOD_RES     295    295       Nitrated tyrosine (By similarity).
FT   MOD_RES     464    464       N6-acetyllysine (By similarity).
FT   MOD_RES     537    537       Phosphothreonine.
FT   MOD_RES     663    663       Phosphoserine.
FT   CROSSLNK    143    143       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   VAR_SEQ     995   1044       GKECVQPATKSSCSLSACTDGISWPFVLLIMPLVVWVYSTD
FT                                TNFSDMFWS -> AILE (in isoform SERCA2A).
FT                                /FTId=VSP_000359.
SQ   SEQUENCE   1044 AA;  114858 MW;  06A753982116C421 CRC64;
     MENAHTKTVE EVLGHFGVNE STGLSLEQVK KLKERWGSNE LPAEEGKTLL ELVIEQFEDL
     LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILVA NAIVGVWQER NAENAIEALK
     EYEPEMGKVY RQDRKSVQRI KAKDIVPGDI VEIAVGDKVP ADIRLTSIKS TTLRVDQSIL
     TGESVSVIKH TDPVPDPRAV NQDKKNMLFS GTNIAAGKAM GVVVATGVNT EIGKIRDEMV
     ATEQERTPLQ QKLDEFGEQL SKVISLICIA VWIINIGHFN DPVHGGSWIR GAIYYFKIAV
     ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ
     MSVCRMFILD KVEGDTCSLN EFSITGSTYA PIGEVQKDDK PVKCHQYDGL VELATICALC
     NDSALDYNEA KGVYEKVGEA TETALTCLVE KMNVFDTELK GLSKIERANA CNSVIKQLMK
     KEFTLEFSRD RKSMSVYCTP NKPSRTSMSK MFVKGAPEGV IDRCTHIRVG STKVPMTPGV
     KQKIMSVIRE WGSGSDTLRC LALATHDNPL KREEMHLEDS ANFIKYETNL TFVGCVGMLD
     PPRIEVASSV KLCRQAGIRV IMITGDNKGT AVAICRRIGI FGQDEDVTSK AFTGREFDEL
     SPSAQRDACL NARCFARVEP SHKSKIVEFL QSFDEITAMT GDGVNDAPAL KKSEIGIAMG
     SGTAVAKTAS EMVLADDNFS TIVAAVEEGR AIYNNMKQFI RYLISSNVGE VVCIFLTAAL
     GFPEALIPVQ LLWVNLVTDG LPATALGFNP PDLDIMNKPP RNPKEPLISG WLFFRYLAIG
     CYVGAATVGA AAWWFIAADG GPRVSFYQLS HFLQCKEDNP DFDGVDCAIF ESPYPMTMAL
     SVLVTIEMCN ALNSLSENQS LLRMPPWENI WLVGSICLSM SLHFLILYVE PLPLIFQITP
     LNLTQWLMVL KISLPVILMD ETLKFVARNY LEQPGKECVQ PATKSSCSLS ACTDGISWPF
     VLLIMPLVVW VYSTDTNFSD MFWS
//
ID   PJA1_MOUSE              Reviewed;         578 AA.
AC   O55176; Q8CFU2; Q99MJ1; Q99MJ2; Q99MJ3; Q9DB04;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 3.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=E3 ubiquitin-protein ligase Praja-1;
DE            Short=Praja1;
DE            EC=6.3.2.-;
GN   Name=Pja1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Embryo;
RX   MEDLINE=98054029; PubMed=9393880; DOI=10.1038/sj.onc.1201405;
RA   Mishra L., Tully R.E., Monga S.P.S., Yu P., Cai T., Makalowski W.,
RA   Mezey E., Pavan W.J., Mishra B.;
RT   "Praja1, a novel gene encoding a RING-H2 motif in mouse development.";
RL   Oncogene 15:2361-2368(1997).
RN   [2]
RP   SEQUENCE REVISION.
RA   Mishra L.;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4).
RC   STRAIN=C57BL/6; TISSUE=Amygdala;
RX   MEDLINE=21424589; PubMed=11533224; DOI=10.1101/lm.39401;
RA   Stork O., Stork S., Pape H.-C., Obata K.;
RT   "Identification of genes expressed in the amygdala during the
RT   formation of fear memory.";
RL   Learn. Memory 8:209-219(2001).
RN   [4]
RP   SEQUENCE REVISION TO C-TERMINUS (ISOFORMS 1 AND 3).
RA   Stork O., Stork S.;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   FUNCTION AS A UBIQUITATION LIGASE, AND MUTAGENESIS OF HIS-553.
RX   MEDLINE=99432238; PubMed=10500182; DOI=10.1073/pnas.96.20.11364;
RA   Lorick K.L., Jensen J.P., Fang S., Ong A.M., Hatakeyama S.,
RA   Weissman A.M.;
RT   "RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent
RT   ubiquitination.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:11364-11369(1999).
RN   [8]
RP   INTERACTION WITH MAGED1, AND MUTAGENESIS OF CYS-533.
RX   MEDLINE=22063353; PubMed=11959851; DOI=10.1074/jbc.M109728200;
RA   Sasaki A., Masuda Y., Iwai K., Ikeda K., Watanabe K.;
RT   "A RING finger protein Praja1 regulates Dlx5-dependent transcription
RT   through its ubiquitin ligase activity for the Dlx/Msx-interacting
RT   MAGE/Necdin family protein, Dlxin-1.";
RL   J. Biol. Chem. 277:22541-22546(2002).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-231, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Has E2-dependent E3 ubiquitin-protein ligase activity.
CC       Ubiquitinates MAGED1 antigen leading to its subsequent degradation
CC       by proteosome. May be involved in protein sorting.
CC   -!- SUBUNIT: Binds ubiquitin-conjugating enzymes (E2s). Binds, in
CC       vitro and in vivo, the MAGE conserved domain of MAGED1. Binds
CC       weakly Necdin, in vitro.
CC   -!- INTERACTION:
CC       Q9QYH6:Maged1; NbExp=1; IntAct=EBI-1801652, EBI-1801274;
CC       Q03358:Msx2; NbExp=1; IntAct=EBI-1801652, EBI-1801354;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Alternative splicing appears to be tissue-specific;
CC       Name=1; Synonyms=Praja1a;
CC         IsoId=O55176-3; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O55176-2; Sequence=VSP_007519;
CC       Name=3; Synonyms=Praja1c;
CC         IsoId=O55176-4; Sequence=VSP_007521;
CC       Name=4; Synonyms=Praja1d;
CC         IsoId=O55176-5; Sequence=VSP_022011, VSP_007520;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, liver, kidney. Highest
CC       levels in brain where it is found in many regions including
CC       cortical and subcortical areas and in neurons of the amygdala.
CC       Weak expression also found in testis. Also expressed in developing
CC       embryo.
CC   -!- INDUCTION: By fear memory. Differential induction of isoforms.
CC   -!- DOMAIN: The RING-type zinc finger domain interacts with an
CC       ubiquitin-conjugating enzyme (E2) and facilitates ubiquitination.
CC   -!- PTM: Substrate for E2-dependent ubiquitination.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -----------------------------------------------------------------------
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DR   EMBL; U06944; AAC00205.2; -; mRNA.
DR   EMBL; AF335250; AAK15764.2; -; mRNA.
DR   EMBL; AF335251; AAK15765.2; -; mRNA.
DR   EMBL; AF335252; AAK15766.1; -; mRNA.
DR   EMBL; AK005373; BAB23982.1; -; mRNA.
DR   EMBL; BC037616; AAH37616.1; -; mRNA.
DR   IPI; IPI00117765; -.
DR   IPI; IPI00309236; -.
DR   IPI; IPI00309237; -.
DR   IPI; IPI00309239; -.
DR   RefSeq; NP_001076579.1; NM_001083110.1.
DR   RefSeq; NP_032879.2; NM_008853.3.
DR   UniGene; Mm.8211; -.
DR   ProteinModelPortal; O55176; -.
DR   SMR; O55176; 491-574.
DR   IntAct; O55176; 10.
DR   PhosphoSite; O55176; -.
DR   PRIDE; O55176; -.
DR   Ensembl; ENSMUST00000036354; ENSMUSP00000109420; ENSMUSG00000034403.
DR   Ensembl; ENSMUST00000113792; ENSMUSP00000109423; ENSMUSG00000034403.
DR   Ensembl; ENSMUST00000113797; ENSMUSP00000109428; ENSMUSG00000034403.
DR   GeneID; 18744; -.
DR   KEGG; mmu:18744; -.
DR   UCSC; uc009tvk.1; mouse.
DR   UCSC; uc009tvl.1; mouse.
DR   CTD; 18744; -.
DR   MGI; MGI:1101765; Pja1.
DR   GeneTree; ENSGT00530000062967; -.
DR   HOGENOM; HBG283654; -.
DR   HOVERGEN; HBG003815; -.
DR   InParanoid; O55176; -.
DR   OMA; CGGGENT; -.
DR   OrthoDB; EOG4D52XB; -.
DR   PhylomeDB; O55176; -.
DR   NextBio; 294897; -.
DR   ArrayExpress; O55176; -.
DR   Bgee; O55176; -.
DR   CleanEx; MM_PJA1; -.
DR   Genevestigator; O55176; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030163; P:protein catabolic process; IDA:MGI.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Ligase; Metal-binding; Phosphoprotein;
KW   Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    578       E3 ubiquitin-protein ligase Praja-1.
FT                                /FTId=PRO_0000056000.
FT   ZN_FING     530    571       RING-type.
FT   COMPBIAS    230    236       Poly-Asp.
FT   COMPBIAS    292    295       Poly-Arg.
FT   MOD_RES     231    231       Phosphothreonine.
FT   VAR_SEQ      60    243       Missing (in isoform 2).
FT                                /FTId=VSP_007519.
FT   VAR_SEQ     185    187       ARP -> PLF (in isoform 4).
FT                                /FTId=VSP_022011.
FT   VAR_SEQ     188    578       Missing (in isoform 4).
FT                                /FTId=VSP_007520.
FT   VAR_SEQ     197    411       Missing (in isoform 3).
FT                                /FTId=VSP_007521.
FT   MUTAGEN     533    533       C->A: No effect on MAGED1 binding.
FT                                Decrease in ubiquitination of MAGED1. No
FT                                inhibition of DLX5-dependent
FT                                transcriptional activity.
FT   MUTAGEN     553    553       H->S: Loss of ubiquitination activity.
FT   CONFLICT    236    236       D -> DD (in Ref. 3; AAK15764).
FT   CONFLICT    515    515       I -> M (in Ref. 5; BAB23982).
FT   CONFLICT    523    523       A -> T (in Ref. 3; AAK15764/AAK15765).
SQ   SEQUENCE   578 AA;  63906 MW;  11B2D3C1F8982143 CRC64;
     MSHQERIASQ RRTTAEVPMH RSTANQSKRS RSPFASTRRR WDDSESSGAS LAVESEDYSR
     YPPREYRASG SRRGLAYGHI DTVVARDSEE EGAGPVDRLP VRGKAGKFKD DPEKGARSSR
     FTSVNHDAKE ECGKVESPPA ARCSARRAEL SKQNGSSASQ ISSAEGRAAA KGNNSLERER
     QNLPARPSRA PVSICGGGEN TPKSAEEPVV RPKVRNVATP NCMKPKVFFD TDDDDDVPHS
     TSRWRDAADA EEAHAEGLAR RGRGEAASSS EPRYAEDQDA RSEQAKADKV PRRRRTMADP
     DFWAYTDDYY RYYEEDSDSD KEWMAALRRK YRSREQPQSS SGESWELLPG KEELERQQAG
     AGSLASAGSN GSGYPEEVQD PSLQEEEQAS LEEGEIPWLR YNENESSSEG DNESTHELIQ
     PGMFMLDGNN NLEDDSSVSE DLEVDWSLFD GFADGLGVAE AISYVDPQFL TYMALEERLA
     QAMETALAHL ESLAVDVEVA NPPASKESID ALPEILVTED HGAVGQEMCC PICCSEYVKG
     EVATELPCHH YFHKPCVSIW LQKSGTCPVC RCMFPPPL
//
ID   DHX9_MOUSE              Reviewed;        1380 AA.
AC   O70133; O35931; O54703; Q5FWY1; Q6R5F7; Q9CSA2;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   08-MAR-2011, entry version 103.
DE   RecName: Full=ATP-dependent RNA helicase A;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAH box protein 9;
DE            Short=mHEL-5;
DE   AltName: Full=Nuclear DNA helicase II;
DE            Short=NDH II;
GN   Name=Dhx9; Synonyms=Ddx9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP   [GENOMIC DNA] OF 1-161.
RC   STRAIN=129/Sv;
RX   MEDLINE=98149984; PubMed=9480750; DOI=10.1006/geno.1997.5139;
RA   Lee C.-G., Eki T., Okumura K., da Costa Soares V., Hurwitz J.;
RT   "Molecular analysis of the cDNA and genomic DNA encoding mouse RNA
RT   helicase A.";
RL   Genomics 47:365-371(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-756 (ISOFORM 3).
RC   STRAIN=C57BL/6NCr;
RX   PubMed=14691545; DOI=10.1371/journal.pbio.0000074;
RA   Sharov A.A., Piao Y., Matoba R., Dudekula D.B., Qian Y., VanBuren V.,
RA   Falco G., Martin P.R., Stagg C.A., Bassey U.C., Wang Y., Carter M.G.,
RA   Hamatani T., Aiba K., Akutsu H., Sharova L., Tanaka T.S., Kimber W.L.,
RA   Yoshikawa T., Jaradat S.A., Pantano S., Nagaraja R., Boheler K.R.,
RA   Taub D., Hodes R.J., Longo D.L., Schlessinger D., Keller J., Klotz E.,
RA   Kelsoe G., Umezawa A., Vescovi A.L., Rossant J., Kunath T.,
RA   Hogan B.L.M., Curci A., D'Urso M., Kelso J., Hide W., Ko M.S.H.;
RT   "Transcriptome analysis of mouse stem cells and early embryos.";
RL   PLoS Biol. 1:410-419(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-756 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic germ cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-264 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE OF 386-919 (ISOFORMS 1/2/3).
RC   STRAIN=C57BL/6;
RA   Kisielow P., Miazek A.;
RT   "mHEL-5.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=10413677;
RA   Zhang S., Herrmann C., Grosse F.;
RT   "Nucleolar localization of murine nuclear DNA helicase II (RNA
RT   helicase A).";
RL   J. Cell Sci. 112:2693-2703(1999).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [8]
RP   STRUCTURE BY NMR OF 4-262.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of double-stranded RNA-binding motifs from
RT   hypothetical protein BAB28848.";
RL   Submitted (NOV-2004) to the PDB data bank.
CC   -!- FUNCTION: Component of the CRD-mediated complex that promotes MYC
CC       mRNA stability. Unwinds double-stranded DNA and RNA in a 3' to 5'
CC       direction. Alterations of secondary structure may subsequently
CC       influence interactions with proteins or other nucleic acids.
CC       Functions as a transcriptional activator (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Component of the coding region determinant (CRD)-mediated
CC       complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1.
CC       Identified in a mRNP complex, at least composed of DHX9, DDX3X,
CC       ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2,
CC       SYNCRIP and YBX1. Identified in a mRNP granule complex, at least
CC       composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB,
CC       HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3,
CC       NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X,
CC       RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs.
CC       Interacts with IGF2BP1. Binds MBD2, HRMT1L2/PRMT1, and RELA. May
CC       act to directly link BRCA1, CREBBP or SMN1 and the RNA polymerase
CC       II complex. Can also interact with XRCC5 and with TOP2A in an RNA
CC       dependent manner; these interactions may be indirect. Interaction
CC       with TOP2A is promoted by UBC9. Interacts with histone H2AFX and
CC       this requires phosphorylation of H2AFX on 'Ser-139' (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm (By
CC       similarity). Note=Localized in cytoplasmic mRNP granules
CC       containing untranslated mRNAs. Can shuttle between nucleus and
CC       cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O70133-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O70133-2; Sequence=VSP_014779;
CC       Name=3;
CC         IsoId=O70133-3; Sequence=VSP_014778;
CC   -!- DOMAIN: The MTAD domain mediates interaction with the RNA
CC       polymerase II holoenzyme (By similarity).
CC   -!- PTM: Methylated (By similarity).
CC   -!- PTM: May be phosphorylated by PRKDC/XRCC7 (By similarity).
CC       Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily.
CC   -!- SIMILARITY: Contains 2 DRBM (double-stranded RNA-binding) domains.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH89159.1; Type=Frameshift; Positions=447, 448;
CC       Sequence=AAR87796.1; Type=Miscellaneous discrepancy; Note=Intron retention;
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DR   EMBL; U91922; AAC05725.1; -; mRNA.
DR   EMBL; AF023530; AAC05301.1; -; Genomic_DNA.
DR   EMBL; AY512925; AAR87796.1; ALT_SEQ; mRNA.
DR   EMBL; BC089159; AAH89159.1; ALT_SEQ; mRNA.
DR   EMBL; AK013423; BAB28848.1; -; mRNA.
DR   EMBL; U92080; AAB72087.1; -; mRNA.
DR   IPI; IPI00339468; -.
DR   IPI; IPI00607914; -.
DR   IPI; IPI00875791; -.
DR   RefSeq; NP_031868.2; NM_007842.2.
DR   UniGene; Mm.20000; -.
DR   PDB; 1UIL; NMR; -; A=163-262.
DR   PDB; 1WHQ; NMR; -; A=4-89.
DR   PDBsum; 1UIL; -.
DR   PDBsum; 1WHQ; -.
DR   ProteinModelPortal; O70133; -.
DR   SMR; O70133; 4-89, 168-262, 331-1115.
DR   STRING; O70133; -.
DR   PhosphoSite; O70133; -.
DR   PRIDE; O70133; -.
DR   Ensembl; ENSMUST00000042141; ENSMUSP00000038135; ENSMUSG00000042699.
DR   GeneID; 13211; -.
DR   KEGG; mmu:13211; -.
DR   UCSC; uc007czy.1; mouse.
DR   CTD; 13211; -.
DR   MGI; MGI:108177; Dhx9.
DR   eggNOG; roNOG04266; -.
DR   HOGENOM; HBG444787; -.
DR   HOVERGEN; HBG039429; -.
DR   InParanoid; O70133; -.
DR   OrthoDB; EOG4HHP1J; -.
DR   ArrayExpress; O70133; -.
DR   Bgee; O70133; -.
DR   CleanEx; MM_DHX9; -.
DR   Genevestigator; O70133; -.
DR   GermOnline; ENSMUSG00000042699; Mus musculus.
DR   GO; GO:0070937; C:CRD-mediated mRNA stability complex; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:MGI.
DR   GO; GO:0030529; C:ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0034605; P:cellular response to heat; IDA:MGI.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR001159; Ds-RNA-bd.
DR   InterPro; IPR014720; dsRNA-bd-like.
DR   InterPro; IPR011709; DUF1605.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   Gene3D; G3DSA:3.30.160.20; dsRNA-bd-like; 2.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00035; dsrm; 2.
DR   Pfam; PF07717; DUF1605; 1.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00358; DSRM; 2.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS50137; DS_RBD; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Alternative splicing;
KW   ATP-binding; Cytoplasm; DNA-binding; Helicase; Hydrolase; Methylation;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Repeat; RNA-binding.
FT   CHAIN         1   1380       ATP-dependent RNA helicase A.
FT                                /FTId=PRO_0000055158.
FT   DOMAIN        3     71       DRBM 1.
FT   DOMAIN      182    254       DRBM 2.
FT   DOMAIN      400    566       Helicase ATP-binding.
FT   DOMAIN      638    811       Helicase C-terminal.
FT   NP_BIND     413    420       ATP (By similarity).
FT   REGION        1    253       Interaction with CREBBP (By similarity).
FT   REGION      233    328       Interaction with BRCA1 (By similarity).
FT   REGION      333    382       MTAD (By similarity).
FT   MOTIF       513    516       DEAH box.
FT   MOTIF       588    597       Nuclear localization signal (Potential).
FT   COMPBIAS   1171   1380       Arg/Gly/Ser/Tyr-rich.
FT   MOD_RES     193    193       N6-acetyllysine (By similarity).
FT   MOD_RES     201    201       N6-acetyllysine (By similarity).
FT   MOD_RES     323    323       Phosphoserine.
FT   MOD_RES    1026   1026       N6-acetyllysine (By similarity).
FT   MOD_RES    1338   1338       Phosphotyrosine (By similarity).
FT   MOD_RES    1345   1345       Phosphotyrosine (By similarity).
FT   VAR_SEQ       1    216       Missing (in isoform 3).
FT                                /FTId=VSP_014778.
FT   VAR_SEQ     123    123       E -> EA (in isoform 2).
FT                                /FTId=VSP_014779.
FT   CONFLICT     46     46       A -> R (in Ref. 1; AAC05725).
FT   CONFLICT    136    136       S -> A (in Ref. 1; AAC05725/AAC05301).
FT   CONFLICT    187    187       L -> V (in Ref. 2).
FT   CONFLICT    189    189       Q -> H (in Ref. 1; AAC05725).
FT   CONFLICT    211    211       R -> G (in Ref. 4; BAB28848).
FT   CONFLICT    235    235       S -> C (in Ref. 1; AAC05725).
FT   CONFLICT    257    257       V -> C (in Ref. 1; AAC05725).
FT   CONFLICT    281    281       S -> P (in Ref. 1; AAC05725).
FT   CONFLICT    674    674       N -> M (in Ref. 5; AAB72087).
FT   CONFLICT    748    748       T -> I (in Ref. 5; AAB72087).
FT   CONFLICT    831    831       I -> V (in Ref. 5; AAB72087).
FT   HELIX         5     14
FT   STRAND       20     27
FT   STRAND       29     39
FT   STRAND       47     53
FT   HELIX        54     72
FT   TURN         77     79
FT   HELIX       172    175
FT   HELIX       180    193
FT   STRAND      201    206
FT   STRAND      212    221
FT   TURN        222    225
FT   STRAND      226    231
FT   HELIX       237    255
SQ   SEQUENCE   1380 AA;  149475 MW;  005D641CD9A4F0C9 CRC64;
     MGDIKNFLYA WCGKRKMTPA YEIRAVGNKN RQKFMCEVRV EGFNYAGMGN STNKKDAQSN
     AARDFVNYLV RINEVKSEEV PAVGIVPPPP ILSDTSDSTA SAAEGLPAPM GGPLPPHLAL
     KAEENNSGVE SSGYGSPGPT WDRGANLKDY YSRKEEQEVQ ATLESEEVDL NAGLHGNWTL
     ENAKARLNQY FQKEKIQGEY KYTQVGPDHN RSFIAEMTIY IKQLGRRIFA REHGSNKKLA
     AQSCALSLVR QLYHLGVIEA YSGLTKKKEG ERVEPYKVFL SPDLELQLQN VVQELDLEIV
     PPPVDPSMPV ILNIGKLAHF EPSQRQNAVG VVPWSPPQSN WNPWTSSNID EGPLAYASTE
     QISMDLKNEL TYQMEQDHNL QSVLQERELL PVKKFEAEIL EAISSNSVVI IRGATGCGKT
     TQVPQYILDD FIQNDRAAEC NIVVTQPRRI SAVAVAERVA YERGEEPGKS CGYSVRFESI
     LPRPHASIMF CTVGVLLRKL EAGIRGISHV IVDEIHERDI NTDFLLVVLR DVVLAYPEVR
     IVLMSATIDT TMFCEYFFNC PIIEVYGRTF PVQEYFLEDC IQMTQFIPPP KDKKKKDKED
     DGGEDDDANC NLICGDEYGP ETKLSMSQLN EKETPFELIE ALLKYIETLN VPGAVLVFLP
     GWNLIYTMQK HLENNSHFGS HRYQILPLHS QIPREEQRKV FDPVPDGVTK VILSTNIAET
     SITINDVVYV IDSCKQKVKL FTAHNNMTNY ATVWASKTNL EQRKGRAGRV RPGFCFHLCS
     RARFDRLETH MTPEMFRTPL HEIALSIKLL RLGGIGQFLA KAIEPPPLDA IIEAEHTLRE
     LDALDANDEL TPLGRILAKL PIEPRFGKMM IMGCIFYVGD AVCTISAATC FPEPFISEGK
     RLGYIHRNFA GNRFSDHVAL LSVFQAWDDA RMSGEEAEIR FCEQKRLNMA TLRMTWEAKV
     QLKEILINSG FPEDCLLTQV FTNTGPDNNL DVVISLLAFG VYPNVCYHKE KRKILTTEGR
     NALIHKSSVN CPFSSQDMKY PSPFFVFGEK IRTRAISAKG MTLVTPLQLL LFASKKVQSD
     GQIVFIDDWI RLQISHEAAA CITIRAAMEA LVVEVSKQPN IISQLDPVNE HMLNTIRQIS
     RPSAAGINLM IGSVRYGDGP RPPKMARYDN GSGYRRGYGG GGYGGGGYGG GYGSGGFGGG
     FGSGGGFGGG FNSGGGGFGS GGGGFGSGGG GFGGGGGGFS GGGGGGFGGG RGGGGGGFGG
     SGGFGNGGGG YGVGGGGYGG GGGGGYGGGS GGYGGGGYGG GEGYSISPNS YRGNYGGGGG
     GYRGGSQGGY RNNFGGDYRG SSGDYRGSGG GYRGSGGFQR RGYGGGYFGQ GRGGGGGGGY
//
ID   PI51C_MOUSE             Reviewed;         661 AA.
AC   O70161; Q505A1; Q80TW9; Q8VCU5;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 2.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Phosphatidylinositol-4-phosphate 5-kinase type-1 gamma;
DE            Short=PIP5K1-gamma;
DE            Short=PtdIns(4)P-5-kinase 1 gamma;
DE            EC=2.7.1.68;
DE   AltName: Full=Phosphatidylinositol-4-phosphate 5-kinase type I gamma;
DE            Short=PIP5KIgamma;
GN   Name=Pip5k1c; Synonyms=Kiaa0589;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION,
RP   ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX   MEDLINE=98204859; PubMed=9535851; DOI=10.1074/jbc.273.15.8741;
RA   Ishihara H., Shibasaki Y., Kizuki N., Wada T., Yazaki Y., Asano T.,
RA   Oka Y.;
RT   "Type I phosphatidylinositol-4-phosphate 5-kinases. Cloning of the
RT   third isoform and deletion/substitution analysis of members of this
RT   novel lipid kinase family.";
RL   J. Biol. Chem. 273:8741-8748(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Fetal brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J, and NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=FVB/N; TISSUE=Brain, and Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYROSINE RESIDUES, AND
RP   INTERACTION WITH TLN1.
RX   PubMed=12422220; DOI=10.1038/nature01082;
RA   Ling K., Doughman R.L., Firestone A.J., Bunce M.W., Anderson R.A.;
RT   "Type I gamma phosphatidylinositol phosphate kinase targets and
RT   regulates focal adhesions.";
RL   Nature 420:89-93(2002).
RN   [7]
RP   PHOSPHORYLATION AT TYR-644, AND MUTAGENESIS OF TYR-644.
RX   PubMed=14691141; DOI=10.1083/jcb.200310067;
RA   Ling K., Doughman R.L., Iyer V.V., Firestone A.J., Bairstow S.F.,
RA   Mosher D.F., Schaller M.D., Anderson R.A.;
RT   "Tyrosine phosphorylation of type Igamma phosphatidylinositol
RT   phosphate kinase by Src regulates an integrin-talin switch.";
RL   J. Cell Biol. 163:1339-1349(2003).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=14741049; DOI=10.1042/BJ20031394;
RA   Giudici M.-L., Emson P.C., Irvine R.F.;
RT   "A novel neuronal-specific splice variant of Type I
RT   phosphatidylinositol 4-phosphate 5-kinase isoform gamma.";
RL   Biochem. J. 379:489-496(2004).
RN   [9]
RP   INTERACTION WITH AP2M1 AND TLN1, AND MUTAGENESIS OF TYR-644; PRO-646
RP   AND LEU-647.
RX   PubMed=16707488; DOI=10.1074/jbc.M601465200;
RA   Bairstow S.F., Ling K., Su X., Firestone A.J., Carbonara C.,
RA   Anderson R.A.;
RT   "Type Igamma661 phosphatidylinositol phosphate kinase directly
RT   interacts with AP2 and regulates endocytosis.";
RL   J. Biol. Chem. 281:20632-20642(2006).
RN   [10]
RP   INTERACTION WITH AP2B1, AND MUTAGENESIS OF PHE-635; TRP-642 AND
RP   TYR-644.
RX   PubMed=19287005; DOI=10.1074/jbc.M901017200;
RA   Thieman J.R., Mishra S.K., Ling K., Doray B., Anderson R.A.,
RA   Traub L.M.;
RT   "Clathrin regulates the association of PIPKIgamma661 with the AP-2
RT   adaptor beta2 appendage.";
RL   J. Biol. Chem. 284:13924-13939(2009).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 636-652 IN COMPLEX WITH TLN1.
RX   PubMed=15623515; DOI=10.1074/jbc.M413180200;
RA   de Pereda J.M., Wegener K.L., Santelli E., Bate N., Ginsberg M.H.,
RA   Critchley D.R., Campbell I.D., Liddington R.C.;
RT   "Structural basis for phosphatidylinositol phosphate kinase type
RT   Igamma binding to talin at focal adhesions.";
RL   J. Biol. Chem. 280:8381-8386(2005).
CC   -!- FUNCTION: Plays a role in membrane ruffling and assembly of
CC       clathrin-coated pits at the synapse (By similarity). Participates
CC       in the biosynthesis of phosphatidylinositol-4,5-bisphosphate.
CC       Mediates RAC1-dependent reorganization of actin filaments.
CC   -!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 4-
CC       phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
CC   -!- ENZYME REGULATION: Activated by phosphatidic acid.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=37 uM for PtdIns(4)P;
CC         KM=39 uM for ATP;
CC   -!- SUBUNIT: Interacts with ARF6 (By similarity). Interacts with TLN1,
CC       TLN2 and CSK. Interacts with AP2B1. Isoform 1 interacts with
CC       AP2M1; phosphorylation of PIP5K1C by CSK disrupts the interaction;
CC       clathrin competes with PIP5K1C.
CC   -!- SUBCELLULAR LOCATION: Endomembrane system. Cell junction, focal
CC       adhesion. Note=Associated with membranes. Detected at focal
CC       adhesions.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O70161-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O70161-2; Sequence=VSP_016013, VSP_016014;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=O70161-3; Sequence=VSP_016015;
CC   -!- TISSUE SPECIFICITY: Detected in brain, lung, thymus, heart,
CC       testicle, kidney and embryo. Highly expressed in forebrain, in
CC       particular in cerebellum, hippocampus and cerebral cortex.
CC   -!- PTM: Phosphorylation on Tyr-644 enhances binding to TLN2 and is
CC       necessary for targeting to focal adhesions.
CC   -!- SIMILARITY: Contains 1 PIPK domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65601.2; Type=Erroneous initiation;
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DR   EMBL; AB006916; BAA25664.1; -; mRNA.
DR   EMBL; AK122319; BAC65601.2; ALT_INIT; mRNA.
DR   EMBL; AK154816; BAE32849.1; -; mRNA.
DR   EMBL; AK171576; BAE42536.1; -; mRNA.
DR   EMBL; BC019138; AAH19138.1; -; mRNA.
DR   EMBL; BC094665; AAH94665.1; -; mRNA.
DR   IPI; IPI00403328; -.
DR   IPI; IPI00655177; -.
DR   IPI; IPI00655218; -.
DR   RefSeq; NP_001140159.1; NM_001146687.1.
DR   RefSeq; NP_032870.2; NM_008844.2.
DR   UniGene; Mm.29836; -.
DR   PDB; 1Y19; X-ray; 2.60 A; A/C/E/G/I/K=638-651.
DR   PDB; 2H7D; NMR; -; B=642-652.
DR   PDB; 2H7E; NMR; -; B=642-652.
DR   PDBsum; 1Y19; -.
DR   PDBsum; 2H7D; -.
DR   PDBsum; 2H7E; -.
DR   ProteinModelPortal; O70161; -.
DR   SMR; O70161; 74-443.
DR   MINT; MINT-4105231; -.
DR   STRING; O70161; -.
DR   PhosphoSite; O70161; -.
DR   PRIDE; O70161; -.
DR   Ensembl; ENSMUST00000045469; ENSMUSP00000038225; ENSMUSG00000034902.
DR   Ensembl; ENSMUST00000105326; ENSMUSP00000100963; ENSMUSG00000034902.
DR   Ensembl; ENSMUST00000105327; ENSMUSP00000100964; ENSMUSG00000034902.
DR   GeneID; 18717; -.
DR   KEGG; mmu:18717; -.
DR   UCSC; uc007ghc.1; mouse.
DR   UCSC; uc007ghd.1; mouse.
DR   CTD; 18717; -.
DR   MGI; MGI:1298224; Pip5k1c.
DR   eggNOG; maNOG07334; -.
DR   GeneTree; ENSGT00550000074279; -.
DR   HOGENOM; HBG588608; -.
DR   HOVERGEN; HBG052818; -.
DR   InParanoid; O70161; -.
DR   OMA; NIDQHER; -.
DR   OrthoDB; EOG4JQ3Z0; -.
DR   BRENDA; 2.7.1.68; 244.
DR   NextBio; 294809; -.
DR   ArrayExpress; O70161; -.
DR   Bgee; O70161; -.
DR   Genevestigator; O70161; -.
DR   GermOnline; ENSMUSG00000034902; Mus musculus.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; IDA:MGI.
DR   InterPro; IPR002498; PInositol-4-P-5-kinase_core.
DR   InterPro; IPR016034; PInositol-4P-5-kinase_core_sub.
DR   PANTHER; PTHR23086; PIP5K; 1.
DR   Pfam; PF01504; PIP5K; 1.
DR   SMART; SM00330; PIPKc; 1.
DR   PROSITE; PS51455; PIPK; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Cell junction;
KW   Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Transferase.
FT   CHAIN         1    661       Phosphatidylinositol-4-phosphate 5-kinase
FT                                type-1 gamma.
FT                                /FTId=PRO_0000185463.
FT   DOMAIN       75    443       PIPK.
FT   REGION      636    661       Mediates interaction with TLN2.
FT   MOD_RES     644    644       Phosphotyrosine; by CSK.
FT   VAR_SEQ     343    402       Missing (in isoform 2).
FT                                /FTId=VSP_016013.
FT   VAR_SEQ     635    635       F -> FFAHGRYWLFSPRRRQLRAVTPNHTGT (in
FT                                isoform 2).
FT                                /FTId=VSP_016014.
FT   VAR_SEQ     636    661       Missing (in isoform 3).
FT                                /FTId=VSP_016015.
FT   MUTAGEN     635    635       F->A: Abolishes interaction with AP2B1.
FT   MUTAGEN     642    642       W->A: Abolishes interaction with AP2B1.
FT   MUTAGEN     644    644       Y->F: Loss of phosphorylation by CSK.
FT                                Abolishes interaction with AP-2 complex.
FT   MUTAGEN     646    646       P->F: Abolishes interaction with AP-2
FT                                complex.
FT   MUTAGEN     647    647       L->V: Abolishes interaction with AP-2
FT                                complex.
FT   CONFLICT    110    110       V -> M (in Ref. 1; BAA25664).
FT   CONFLICT    122    122       L -> F (in Ref. 1; BAA25664).
FT   STRAND      642    644
FT   HELIX       646    648
SQ   SEQUENCE   661 AA;  72408 MW;  4A3B71E4465B83C3 CRC64;
     MELEVPDEAE SAEAGAVTAE AAWSAESGAA AGMTQKKAGL AEAPLVTGQP GPGHGKKLGH
     RGVDASGETT YKKTTSSTLK GAIQLGIGYT VGNLSSKPER DVLMQDFYVV ESIFFPSEGS
     NLTPAHHFQD FRFKTYAPVA FRYFRELFGI RPDDYLYSLC NEPLIELSNP GASGSVFYVT
     SDDEFIIKTV MHKEAEFLQK LLPGYYMNLN QNPRTLLPKF YGLYCVQSGG KNIRVVVMNN
     VLPRVVKMHL KFDLKGSTYK RRASKKEKEK SLPTYKDLDF MQDMPEGLLL DSDTFGALVK
     TLQRDCLVLE SFKIMDYSLL LGVHNIDQQE RERQAEGAQS KADEKRPVAQ KALYSTAMES
     IQGGAARGEA IETDDTMGGI PAVNGRGERL LLHIGIIDIL QSYRFIKKLE HTWKALVHDG
     DTVSVHRPSF YAERFFKFMS STVFRKSSSL KSSPSKKGRG ALLAVKPLGP TAAFSASQIP
     SEREDVQYDL RGARSYPTLE DEGRPDLLPC TPPSFEEATT ASIATTLSST SLSIPERSPS
     DTSEQPRYRR RTQSSGQDGR PQEEPHAEDL QKITVQVEPV CGVGVVPKEE GAGVEVPPCG
     ASAAASVEID AASQASEPAS QASDEEDAPS TDIYFPTDER SWVYSPLHYS ARPASDGESD
     T
//
ID   STMN3_MOUSE             Reviewed;         180 AA.
AC   O70166;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Stathmin-3;
DE   AltName: Full=Hippocampus abundant transcript 3;
DE   AltName: Full=SCG10-like protein;
DE   AltName: Full=SCG10-related protein HiAT3;
GN   Name=Stmn3; Synonyms=Sclip;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Hippocampus;
RX   MEDLINE=98382541; PubMed=9714847; DOI=10.1016/S0378-1119(98)00324-2;
RA   Matsuo N., Kawamoto S., Matsubara K., Okubo K.;
RT   "A novel SCG10-related gene uniquely expressed in the nervous
RT   system.";
RL   Gene 215:477-481(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98264342; PubMed=9603203;
RA   Ozon S., Byk T., Sobel A.;
RT   "SCLIP: a novel SCG10-like protein of the stathmin family expressed in
RT   the nervous system.";
RL   J. Neurochem. 70:2386-2396(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68 AND SER-73,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- TISSUE SPECIFICITY: Neuron specific.
CC   -!- SIMILARITY: Belongs to the stathmin family.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB007912; BAA28629.1; -; mRNA.
DR   EMBL; AF069708; AAC21575.1; -; mRNA.
DR   EMBL; BC057017; AAH57017.1; -; mRNA.
DR   IPI; IPI00309223; -.
DR   RefSeq; NP_033159.1; NM_009133.3.
DR   UniGene; Mm.2319; -.
DR   UniGene; Mm.447659; -.
DR   ProteinModelPortal; O70166; -.
DR   SMR; O70166; 38-173.
DR   STRING; O70166; -.
DR   PhosphoSite; O70166; -.
DR   PRIDE; O70166; -.
DR   Ensembl; ENSMUST00000103045; ENSMUSP00000099334; ENSMUSG00000027581.
DR   GeneID; 20262; -.
DR   KEGG; mmu:20262; -.
DR   UCSC; uc008olt.1; mouse.
DR   CTD; 20262; -.
DR   MGI; MGI:1277137; Stmn3.
DR   eggNOG; roNOG04799; -.
DR   HOGENOM; HBG444413; -.
DR   HOVERGEN; HBG054037; -.
DR   InParanoid; O70166; -.
DR   OMA; NFSRQAE; -.
DR   OrthoDB; EOG45MN6K; -.
DR   NextBio; 297927; -.
DR   ArrayExpress; O70166; -.
DR   Bgee; O70166; -.
DR   CleanEx; MM_STMN3; -.
DR   Genevestigator; O70166; -.
DR   GermOnline; ENSMUSG00000027581; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:HGNC.
DR   GO; GO:0005625; C:soluble fraction; IDA:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:HGNC.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IDA:HGNC.
DR   GO; GO:0035021; P:negative regulation of Rac protein signal transduction; IDA:HGNC.
DR   GO; GO:0031175; P:neuron projection development; IDA:HGNC.
DR   GO; GO:0051493; P:regulation of cytoskeleton organization; IDA:HGNC.
DR   GO; GO:0032314; P:regulation of Rac GTPase activity; IDA:HGNC.
DR   InterPro; IPR000956; Stathmin.
DR   PANTHER; PTHR10104; Stathmin; 1.
DR   Pfam; PF00836; Stathmin; 1.
DR   PIRSF; PIRSF002285; Stathmin; 1.
DR   PRINTS; PR00345; STATHMIN.
DR   SUPFAM; SSF101494; Stathmin; 1.
DR   PROSITE; PS00563; STATHMIN_1; 1.
DR   PROSITE; PS01041; STATHMIN_2; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Phosphoprotein.
FT   CHAIN         1    180       Stathmin-3.
FT                                /FTId=PRO_0000182403.
FT   COILED       75    179       Potential.
FT   MOD_RES      65     65       Phosphoserine.
FT   MOD_RES      68     68       Phosphoserine.
FT   MOD_RES      73     73       Phosphoserine.
SQ   SEQUENCE   180 AA;  20954 MW;  A7C0D35A6A684765 CRC64;
     MASTVSAYKE KMKELSVLSL ICSCFYSQPH PNTIYQYGDM EVKQLDKRAS GQSFEVILKS
     PSDLSPESPV LSSPPKRKDA SLEELQKRLE AAEERRKTQE AQVLKQLAER REHEREVLHK
     ALEENNNFSR LAEEKLNYKM ELSKEIREAH LAALRERLRE KELHAAEVRR NKEQREEMSG
//
ID   ACHA4_MOUSE             Reviewed;         629 AA.
AC   O70174; Q8BHE9; Q8VI10; Q9ET51;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2003, sequence version 2.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Neuronal acetylcholine receptor subunit alpha-4;
DE   Flags: Precursor;
GN   Name=Chrna4; Synonyms=Acra4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-529.
RC   STRAIN=Long sleep selected line;
RX   MEDLINE=21327370; PubMed=11434511;
RX   DOI=10.1097/00008571-200106000-00008;
RA   Stitzel J.A., Dobelis P., Jimenez M., Collins A.C.;
RT   "Long sleep and short sleep mice differ in nicotine-stimulated 86Rb+
RT   efflux and alpha4 nicotinic receptor subunit cDNA sequence.";
RL   Pharmacogenetics 11:331-339(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon, and Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RX   MEDLINE=98420182; PubMed=9749753;
RX   DOI=10.1046/j.1460-9568.1998.00235.x;
RA   Watanabe H., Zoli M., Changeux J.-P.;
RT   "Promoter analysis of the neuronal nicotinic acetylcholine receptor
RT   alpha4 gene: methylation and expression of the transgene.";
RL   Eur. J. Neurosci. 10:2244-2253(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 118-357.
RC   STRAIN=C57BL/6;
RA   Kuo Y.-P., Lukas R.J.;
RT   "Expression of mouse nicotinic acetylcholine receptor genes in the
RT   developing thymus.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: After binding acetylcholine, the AChR responds by an
CC       extensive change in conformation that affects all subunits and
CC       leads to opening of an ion-conducting channel across the plasma
CC       membrane.
CC   -!- SUBUNIT: Neuronal AChR is composed of two different types of
CC       subunits: alpha and beta. Alpha-4 subunit can be combined to beta-
CC       2 or beta-4 to give rise to functional receptors. Interacts with
CC       RIC3; which is required for proper folding and assembly (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane; Multi-pass membrane protein. Cell membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
CC       family. Acetylcholine receptor (TC 1.A.9.1) subfamily. Alpha-
CC       4/CHRNA4 sub-subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF225912; AAF34716.2; -; mRNA.
DR   EMBL; AK034228; BAC28638.1; -; mRNA.
DR   EMBL; AK083157; BAC38788.1; -; mRNA.
DR   EMBL; BC053013; AAH53013.1; -; mRNA.
DR   EMBL; AB010002; BAA25752.1; -; Genomic_DNA.
DR   EMBL; AF325347; AAL37363.1; -; mRNA.
DR   IPI; IPI00115712; -.
DR   RefSeq; NP_056545.3; NM_015730.5.
DR   UniGene; Mm.252369; -.
DR   ProteinModelPortal; O70174; -.
DR   SMR; O70174; 36-349.
DR   DIP; DIP-48731N; -.
DR   STRING; O70174; -.
DR   PhosphoSite; O70174; -.
DR   PRIDE; O70174; -.
DR   Ensembl; ENSMUST00000067120; ENSMUSP00000066338; ENSMUSG00000027577.
DR   GeneID; 11438; -.
DR   KEGG; mmu:11438; -.
DR   UCSC; uc008okq.1; mouse.
DR   CTD; 11438; -.
DR   MGI; MGI:87888; Chrna4.
DR   eggNOG; roNOG10402; -.
DR   HOVERGEN; HBG003756; -.
DR   OrthoDB; EOG480HWN; -.
DR   PhylomeDB; O70174; -.
DR   NextBio; 278736; -.
DR   ArrayExpress; O70174; -.
DR   Bgee; O70174; -.
DR   Genevestigator; O70174; -.
DR   GermOnline; ENSMUSG00000027577; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005892; C:nicotinic acetylcholine-gated receptor-channel complex; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004889; F:nicotinic acetylcholine-activated cation-selective channel activity; IMP:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0042113; P:B cell activation; IMP:MGI.
DR   GO; GO:0035095; P:behavioral response to nicotine; IMP:MGI.
DR   GO; GO:0006816; P:calcium ion transport; IGI:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0051899; P:membrane depolarization; IMP:MGI.
DR   GO; GO:0001508; P:regulation of action potential; IMP:MGI.
DR   GO; GO:0014059; P:regulation of dopamine secretion; IMP:MGI.
DR   GO; GO:0060080; P:regulation of inhibitory postsynaptic membrane potential; IMP:MGI.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; IDA:MGI.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   InterPro; IPR002394; Nicotinic_acetylcholine_rcpt.
DR   Gene3D; G3DSA:2.70.170.10; Neur_chan_lig_bd; 1.
DR   PANTHER; PTHR18945; Neur_channel; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR00254; NICOTINICR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF90112; Neu_channel_TM; 1.
DR   SUPFAM; SSF63712; Neur_chan_LBD; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Disulfide bond; Glycoprotein;
KW   Ion transport; Ionic channel; Ligand-gated ion channel; Membrane;
KW   Polymorphism; Postsynaptic cell membrane; Receptor; Signal; Synapse;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL        1     30       Potential.
FT   CHAIN        31    629       Neuronal acetylcholine receptor subunit
FT                                alpha-4.
FT                                /FTId=PRO_0000000352.
FT   TOPO_DOM     32    249       Extracellular (Potential).
FT   TRANSMEM    250    270       Helical; (Potential).
FT   TRANSMEM    279    299       Helical; (Potential).
FT   TRANSMEM    312    332       Helical; (Potential).
FT   TOPO_DOM    333    603       Cytoplasmic (Potential).
FT   TRANSMEM    604    624       Helical; (Potential).
FT   CARBOHYD     59     59       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    109    109       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    176    176       N-linked (GlcNAc...) (Potential).
FT   DISULFID    163    177       By similarity.
FT   DISULFID    227    228       Associated with receptor activation (By
FT                                similarity).
FT   VARIANT     529    529       T -> A.
FT   CONFLICT     16     16       P -> L (in Ref. 1; AAF34716).
FT   CONFLICT     24     24       G -> A (in Ref. 4; BAA25752).
FT   CONFLICT    134    134       D -> N (in Ref. 1; AAF34716).
SQ   SEQUENCE   629 AA;  70305 MW;  261455B6ED50B41C CRC64;
     MEIGGSGAPP PLLLLPLLLL LGTGLLPASS HIETRAHAEE RLLKRLFSGY NKWSRPVANI
     SDVVLVRFGL SIAQLIDVDE KNQMMTTNVW VKQEWHDYKL RWDPGDYENV TSIRIPSELI
     WRPDIVLYNN ADGDFAVTHL TKAHLFYDGR VQWTPPAIYK SSCSIDVTFF PFDQQNCTMK
     FGSWTYDKAK IDLVSMHSRV DQLDFWESGE WVIVDAVGTY NTRKYECCAE IYPDITYAFI
     IRRLPLFYTI NLIIPCLLIS CLTVLVFYLP SECGEKVTLC ISVLLSLTVF LLLITEIIPS
     TSLVIPLIGE YLLFTMIFVT LSIVITVFVL NVHHRSPRTH TMPAWVRRVF LDIVPRLLFM
     KRPSVVKDNC RRLIESMHKM ANAPRFWPEP ESEPGILGDI CNQGLSPAPT FCNRMDTAVE
     TQPTCRSPSH KVPDLKTSEV EKASPCPSPG SCHPPNSSGA PVLIKARSLS VQHVPSSQEA
     AEGSIRCRSR SIQYCVSQDG AASLTESKPT GSPASLKTRP SQLPVSDQTS PCKCTCKEPS
     PVSPITVLKA GGTKAPPQHL PLSPALTRAV EGVQYIADHL KAEDTDFSVK EDWKYVAMVI
     DRIFLWMFII VCLLGTVGLF LPPWLAGMI
//
ID   EF1B_MOUSE              Reviewed;         225 AA.
AC   O70251; Q3THP5; Q5SUH1; Q8CHS1; Q99L22; Q9CZD4;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 5.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Elongation factor 1-beta;
DE            Short=EF-1-beta;
GN   Name=Eef1b; Synonyms=Eef1b2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Tu Q., Yu L., Fu Q., Liu Q., Gong R., Zhao S.;
RT   "Cloning and expression analysis of a novel mouse gene homologous to
RT   human elongation factor 1-beta.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, and C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-10.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=10870971;
RX   DOI=10.1002/(SICI)1522-2683(20000501)21:9<1853::AID-ELPS1853>3.3.CO;2-P;
RA   Tsugita A., Kawakami T., Uchida T., Sakai T., Kamo M., Matsui T.,
RA   Watanabe Y., Morimasa T., Hosokawa K., Toda T.;
RT   "Proteome analysis of mouse brain: two-dimensional electrophoresis
RT   profiles of tissue proteins during the course of aging.";
RL   Electrophoresis 21:1853-1871(2000).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-106, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: EF-1-beta and EF-1-delta stimulate the exchange of GDP
CC       bound to EF-1-alpha to GTP (By similarity).
CC   -!- SUBUNIT: EF-1 is composed of 4 subunits: alpha, beta, delta, and
CC       gamma (By similarity).
CC   -!- PTM: Phosphorylation affects the GDP/GTP exchange rate (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family.
CC   -!- SIMILARITY: Contains 1 GST C-terminal domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH39635.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF029844; AAC13264.2; -; mRNA.
DR   EMBL; AK012756; BAB28447.1; -; mRNA.
DR   EMBL; AK027911; BAC25661.1; -; mRNA.
DR   EMBL; AK168191; BAE40151.1; -; mRNA.
DR   EMBL; AL645950; CAI24121.1; -; Genomic_DNA.
DR   EMBL; BC003899; AAH03899.1; -; mRNA.
DR   EMBL; BC023139; AAH23139.1; -; mRNA.
DR   EMBL; BC039635; AAH39635.1; ALT_INIT; mRNA.
DR   IPI; IPI00320208; -.
DR   PIR; PC7074; PC7074.
DR   RefSeq; NP_061266.2; NM_018796.3.
DR   UniGene; Mm.2718; -.
DR   ProteinModelPortal; O70251; -.
DR   SMR; O70251; 10-72, 136-225.
DR   STRING; O70251; -.
DR   PhosphoSite; O70251; -.
DR   PRIDE; O70251; -.
DR   Ensembl; ENSMUST00000129339; ENSMUSP00000116492; ENSMUSG00000025967.
DR   GeneID; 55949; -.
DR   KEGG; mmu:55949; -.
DR   NMPDR; fig|10090.3.peg.436; -.
DR   UCSC; uc007bfz.1; mouse.
DR   CTD; 55949; -.
DR   MGI; MGI:1929520; Eef1b2.
DR   eggNOG; roNOG07099; -.
DR   GeneTree; ENSGT00390000011747; -.
DR   HOGENOM; HBG714747; -.
DR   HOVERGEN; HBG000787; -.
DR   InParanoid; O70251; -.
DR   OMA; WYRHIAS; -.
DR   OrthoDB; EOG4Z8XXH; -.
DR   PhylomeDB; O70251; -.
DR   NextBio; 311646; -.
DR   ArrayExpress; O70251; -.
DR   Bgee; O70251; -.
DR   CleanEx; MM_EEF1B2; -.
DR   Genevestigator; O70251; -.
DR   GermOnline; ENSMUSG00000025967; Mus musculus.
DR   GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR018940; EF-1_beta_acid_region_euk.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6.
DR   InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
DR   InterPro; IPR014038; Transl_elong_fac_EF1B_bsu/dsu.
DR   Gene3D; G3DSA:1.20.1050.10; GST_C_like; 1.
DR   Gene3D; G3DSA:3.30.70.60; Transl_elong_EF1B/rib_con; 1.
DR   Pfam; PF10587; EF-1_beta_acid; 1.
DR   Pfam; PF00736; EF1_GNE; 1.
DR   SMART; SM00888; EF1_GNE; 1.
DR   SUPFAM; SSF47616; GST_C_like; 1.
DR   SUPFAM; SSF54984; Transl_elong_EF1B_B/D_G_exch; 1.
DR   PROSITE; PS00824; EF1BD_1; 1.
DR   PROSITE; PS00825; EF1BD_2; 1.
DR   PROSITE; PS50405; GST_CTER; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Elongation factor;
KW   Phosphoprotein; Protein biosynthesis.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    225       Elongation factor 1-beta.
FT                                /FTId=PRO_0000155022.
FT   DOMAIN        2     90       GST C-terminal.
FT   MOD_RES       7      7       N6-acetyllysine (By similarity).
FT   MOD_RES      60     60       N6-acetyllysine (By similarity).
FT   MOD_RES      83     83       Phosphoserine.
FT   MOD_RES      90     90       Phosphoserine (By similarity).
FT   MOD_RES     106    106       Phosphoserine.
FT   MOD_RES     112    112       Phosphoserine (By similarity).
FT   MOD_RES     126    126       Phosphotyrosine (By similarity).
FT   MOD_RES     128    128       Phosphoserine (By similarity).
FT   MOD_RES     141    141       Phosphoserine (By similarity).
FT   CONFLICT    113    113       E -> G (in Ref. 2; BAB28447).
FT   CONFLICT    116    116       K -> E (in Ref. 1; AAC13264).
FT   CONFLICT    136    136       V -> I (in Ref. 1; AAC13264).
SQ   SEQUENCE   225 AA;  24694 MW;  6E497150AD88F887 CRC64;
     MGFGDLKTPA GLQVLNDYLA DKSYIEGYVP SQADVAVFEA VSGPPPADLC HALRWYNHIK
     SYEKEKASLP GVKKSLGKYG PSSVEDTTGS GAADAKDDDD IDLFGSDDEE ESEEAKKLRE
     ERLAQYESKK AKKPAVVAKS SILLDVKPWD DETDMTKLEE CVRSIQADGL VWGSSKLVPV
     GYGIKKLQIQ CVVEDDKVGT DMLEEQITAF EDYVQSMDVA AFNKI
//
ID   TP4A2_MOUSE             Reviewed;         167 AA.
AC   O70274; Q3U1K7;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Protein tyrosine phosphatase type IVA 2;
DE            EC=3.1.3.48;
DE   AltName: Full=Protein-tyrosine phosphatase 4a2;
DE   AltName: Full=Protein-tyrosine phosphatase of regenerating liver 2;
DE            Short=PRL-2;
DE   Flags: Precursor;
GN   Name=Ptp4a2; Synonyms=Prl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=98189198; PubMed=9514946; DOI=10.1006/bbrc.1998.8291;
RA   Zeng Q., Hong W., Tan Y.H.;
RT   "Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine
RT   phosphatases homologous to PRL-1.";
RL   Biochem. Biophys. Res. Commun. 244:421-427(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   ISOPRENYLATION AT CYS-164, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   164-CYS--GLN-167.
RX   MEDLINE=20347263; PubMed=10747914; DOI=10.1074/jbc.M000453200;
RA   Zeng Q., Si X., Horstmann H., Xu Y., Hong W., Pallen C.J.;
RT   "Prenylation-dependent association of protein-tyrosine phosphatases
RT   PRL-1, -2, and -3 with the plasma membrane and the early endosome.";
RL   J. Biol. Chem. 275:21444-21452(2000).
CC   -!- FUNCTION: Protein tyrosine phosphatase which stimulates
CC       progression from G1 into S phase during mitosis. Inhibits
CC       geranylgeranyl transferase type II activity by blocking the
CC       association between RABGGTA and RABGGTB (By similarity).
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- ENZYME REGULATION: Inhibited by sodium orthovanadate and
CC       pentamidine (By similarity).
CC   -!- SUBUNIT: In contrast to PTP4A1 and PTP4A3, does not interact with
CC       tubulin. Interacts with RABGGTB (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane. Early endosome. Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, and at lower
CC       levels in liver, lung, heart, kidney, brain, testis and spleen.
CC   -!- PTM: Farnesylated. Farnesylation is required for membrane
CC       targeting and for interaction with RABGGTB (By similarity).
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF035644; AAC15874.1; -; mRNA.
DR   EMBL; AK033092; BAC28149.1; -; mRNA.
DR   EMBL; AK045093; BAC32217.1; -; mRNA.
DR   EMBL; AK155895; BAE33489.1; -; mRNA.
DR   EMBL; BC086794; AAH86794.1; -; mRNA.
DR   EMBL; BC087551; AAH87551.1; -; mRNA.
DR   IPI; IPI00116529; -.
DR   PIR; JC5981; JC5981.
DR   RefSeq; NP_001158217.1; NM_001164745.1.
DR   RefSeq; NP_033000.1; NM_008974.4.
DR   UniGene; Mm.193688; -.
DR   ProteinModelPortal; O70274; -.
DR   SMR; O70274; 6-157.
DR   STRING; O70274; -.
DR   PhosphoSite; O70274; -.
DR   PRIDE; O70274; -.
DR   Ensembl; ENSMUST00000030578; ENSMUSP00000030578; ENSMUSG00000028788.
DR   GeneID; 19244; -.
DR   KEGG; mmu:19244; -.
DR   UCSC; uc008uyf.1; mouse.
DR   CTD; 19244; -.
DR   MGI; MGI:1277117; Ptp4a2.
DR   HOGENOM; HBG314303; -.
DR   HOVERGEN; HBG071295; -.
DR   InParanoid; O70274; -.
DR   OMA; APIEKEG; -.
DR   OrthoDB; EOG4ZCT5N; -.
DR   PhylomeDB; O70274; -.
DR   BRENDA; 3.1.3.48; 244.
DR   NextBio; 296062; -.
DR   ArrayExpress; O70274; -.
DR   Bgee; O70274; -.
DR   CleanEx; MM_PTP4A2; -.
DR   Genevestigator; O70274; -.
DR   GermOnline; ENSMUSG00000028788; Mus musculus.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; FALSE_NEG.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; Disulfide bond; Endosome; Hydrolase;
KW   Lipoprotein; Membrane; Methylation; Prenylation; Protein phosphatase.
FT   CHAIN         1    164       Protein tyrosine phosphatase type IVA 2.
FT                                /FTId=PRO_0000094786.
FT   PROPEP      165    167       Removed in mature form (Probable).
FT                                /FTId=PRO_0000396732.
FT   DOMAIN       79    145       Tyrosine-protein phosphatase.
FT   REGION      102    107       Phosphate binding (By similarity).
FT   ACT_SITE     69     69       Proton donor (By similarity).
FT   ACT_SITE    101    101       Phosphocysteine intermediate (By
FT                                similarity).
FT   BINDING     107    107       Substrate (By similarity).
FT   MOD_RES     164    164       Cysteine methyl ester (Probable).
FT   LIPID       164    164       S-farnesyl cysteine.
FT   DISULFID     46    101       By similarity.
FT   MUTAGEN     164    167       Missing: Locates in the nucleus.
SQ   SEQUENCE   167 AA;  19127 MW;  E97B88BF87B87943 CRC64;
     MNRPAPVEIS YENMRFLITH NPTNATLNKF TEELKKYGVT TLVRVCDATY DKAPVEKEGI
     HVLDWPFDDG APPPNQIVDD WLNLLKTKFR EEPGCCVAVH CVAGLGRAPV LVALALIECG
     MKYEDAVQFI RQKRRGAFNS KQLLYLEKYR PKMRLRFRDT NGHCCVQ
//
ID   O70296_MOUSE            Unreviewed;       589 AA.
AC   O70296;
DT   01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT   01-AUG-1998, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   SubName: Full=G protein-coupled receptor kinase 6;
GN   Name=Grk6; Synonyms=GRK6, Gprk6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129SVJ;
RX   MEDLINE=99436149; PubMed=10506199; DOI=10.1074/jbc.274.41.29381;
RA   Premont R.T., Macrae A.D., Aparicio S.A., Kendall H.E., Welch J.E.,
RA   Lefkowitz R.J.;
RT   "The GRK4 subfamily of G protein-coupled receptor kinases. Alternative
RT   splicing, gene organization, and sequence conservation.";
RL   J. Biol. Chem. 274:29381-29389(1999).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. GPRK subfamily.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 RGS domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF040754; AAC09264.1; -; Genomic_DNA.
DR   IPI; IPI00230631; -.
DR   UniGene; Mm.10193; -.
DR   HSSP; P31751; 1GZK.
DR   ProteinModelPortal; O70296; -.
DR   SMR; O70296; 23-532.
DR   STRING; O70296; -.
DR   Ensembl; ENSMUST00000001115; ENSMUSP00000001115; ENSMUSG00000074886.
DR   MGI; MGI:1347078; Grk6.
DR   HOGENOM; HBG716704; -.
DR   HOVERGEN; HBG004532; -.
DR   InParanoid; O70296; -.
DR   ArrayExpress; O70296; -.
DR   Bgee; O70296; -.
DR   Genevestigator; O70296; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004703; F:G-protein coupled receptor kinase activity; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR000239; GPCR_kinase.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR000342; Regulat_G_prot_signal.
DR   InterPro; IPR016137; Regulat_G_prot_signal_superfam.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR00717; GPCRKINASE.
DR   SMART; SM00315; RGS; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF48097; Regulat_G_prot_signal_superfam; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Receptor;
KW   Serine/threonine-protein kinase; Transferase.
SQ   SEQUENCE   589 AA;  67087 MW;  B4160AC3FF79C466 CRC64;
     MELENIVANT VLLKAREGGG GNRKGKSKKW RQMLQFPHIS QCEELRLSLE RDYHSLCERQ
     PIGRLLFREF CATRPELTRC TAFLDGVSEY EVTPDEKQKA CGRRLMQNFL SHTGPDLIPE
     VPRQLVSNCA QRLEQGPCKD LFQELTRLTH EYLSTAPFAD YLDSIYFNRF LQWKWLERQP
     VTKNTFRQYR VLGKGGFGEV CACQVRATGK MYACKKLEKK RIKKRKGEAM ALNEKQILEK
     VNSRFVVSLA YAYETKDALC LVLTLMNGGD LKFHIYHMGQ AGFPEARAVF YAAEICCGLE
     DLHRERIVYR DLKPENILLD DHGHIRISDL GLAVHVPEGQ TIKGRVGTVG YMAPEVVRNE
     RYTFSPDWWA LGCLLYEMIA GQSPFQQRKK KIKREEVERL VKEVAEEYTD RFSSQARSLC
     SQLLSKDPAE RLGCRGGGAR EVKEHPLFKK LNFKRLGAGM LEPPFKPDPQ AIYCKDVLDI
     EQFSTVKGVD LEPTDQDFYQ KFATGSVSIP WQNEMVETEC FQELNVFGLD GSVPPDLDWK
     GQPTAPPKKG LLQRLFSRQR IAVGTAATVR KSSPPASSPQ AEAPTGGWR
//
ID   ATX2_MOUSE              Reviewed;        1285 AA.
AC   O70305; P97421;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Ataxin-2;
DE   AltName: Full=Spinocerebellar ataxia type 2 protein homolog;
GN   Name=Atxn2; Synonyms=Atx2, Sca2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBUNIT, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Brain;
RX   MEDLINE=98334550; PubMed=9668173; DOI=10.1093/hmg/7.8.1301;
RA   Nechiporuk T.T., Huynh D.P., Figueroa K., Sahba S., Nechiporuk A.V.,
RA   Pulst S.-M.;
RT   "The mouse SCA2 gene: cDNA sequence, alternative splicing and protein
RT   expression.";
RL   Hum. Mol. Genet. 7:1301-1309(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 145-563.
RX   MEDLINE=97051920; PubMed=8896555; DOI=10.1038/ng1196-269;
RA   Pulst S.-M., Nechiporuk A., Nechiporuk T., Gispert S., Chen X.-N.,
RA   Lopes-Cendes I., Pearlman S., Starkman S., Orozco-Diaz G., Lunkes A.,
RA   DeJong P., Rouleau G.A., Auburger G., Korenberg J.R., Figueroa C.,
RA   Sahba S.;
RT   "Moderate expansion of a normally biallelic trinucleotide repeat in
RT   spinocerebellar ataxia type 2.";
RL   Nat. Genet. 14:269-276(1996).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613; SER-653; SER-741;
RP   SER-832 AND SER-836, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBUNIT: Interacts with RBFOX1 (By similarity). Monomer. Can also
CC       form homodimers.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Type I;
CC         IsoId=O70305-1; Sequence=Displayed;
CC       Name=2; Synonyms=Type II;
CC         IsoId=O70305-2; Sequence=VSP_011583;
CC       Name=3; Synonyms=Type III;
CC         IsoId=O70305-3; Sequence=VSP_011583, VSP_011584;
CC   -!- TISSUE SPECIFICITY: Expressed in the heart, lung, liver, kidney,
CC       skeletal muscle, spleen and intestine. Predominant expression was
CC       seen in the brain where a high level expression was found in the
CC       pyramidal cortical neurons, large brain stem neurons and
CC       cerebellar Purkinje cells. All three isoforms were found in all
CC       the tissues except skeletal muscle where only isoform 1 was found.
CC   -!- DEVELOPMENTAL STAGE: Detectable at embryonic days E8-E16 and
CC       lowest expression was seen at E8.
CC   -!- SIMILARITY: Belongs to the ataxin-2 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF041472; AAC09275.1; -; mRNA.
DR   EMBL; U70670; AAB19202.1; -; mRNA.
DR   IPI; IPI00117229; -.
DR   IPI; IPI00461237; -.
DR   IPI; IPI00461238; -.
DR   PIR; T14171; T14171.
DR   RefSeq; NP_033151.2; NM_009125.2.
DR   UniGene; Mm.260900; -.
DR   STRING; O70305; -.
DR   PhosphoSite; O70305; -.
DR   PRIDE; O70305; -.
DR   Ensembl; ENSMUST00000051950; ENSMUSP00000056715; ENSMUSG00000042605.
DR   Ensembl; ENSMUST00000111761; ENSMUSP00000107391; ENSMUSG00000042605.
DR   Ensembl; ENSMUST00000111762; ENSMUSP00000107392; ENSMUSG00000042605.
DR   GeneID; 20239; -.
DR   KEGG; mmu:20239; -.
DR   UCSC; uc008zke.1; mouse.
DR   CTD; 20239; -.
DR   MGI; MGI:1277223; Atxn2.
DR   eggNOG; roNOG09325; -.
DR   GeneTree; ENSGT00530000063565; -.
DR   HOGENOM; HBG715226; -.
DR   HOVERGEN; HBG050623; -.
DR   InParanoid; O70305; -.
DR   OrthoDB; EOG4BP1B3; -.
DR   NextBio; 297885; -.
DR   ArrayExpress; O70305; -.
DR   Bgee; O70305; -.
DR   CleanEx; MM_ATXN2; -.
DR   Genevestigator; O70305; -.
DR   GermOnline; ENSMUSG00000042605; Mus musculus.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR   GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:MGI.
DR   InterPro; IPR009818; Ataxin-2_C.
DR   InterPro; IPR010920; LSM-related_domain.
DR   InterPro; IPR009604; LsmAD_domain.
DR   Pfam; PF06741; LsmAD; 1.
DR   Pfam; PF07145; PAM2; 1.
DR   SUPFAM; SSF50182; Sm_like_riboprot; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Phosphoprotein.
FT   CHAIN         1   1285       Ataxin-2.
FT                                /FTId=PRO_0000064757.
FT   COMPBIAS     46    197       Pro-rich.
FT   COMPBIAS    520    703       Pro-rich.
FT   COMPBIAS    808    841       Ser-rich.
FT   COMPBIAS    900    961       Pro-rich.
FT   MOD_RES     435    435       Phosphoserine (By similarity).
FT   MOD_RES     523    523       Phosphoserine (By similarity).
FT   MOD_RES     527    527       Phosphoserine (By similarity).
FT   MOD_RES     613    613       Phosphoserine.
FT   MOD_RES     636    636       Phosphoserine (By similarity).
FT   MOD_RES     653    653       Phosphoserine.
FT   MOD_RES     710    710       Phosphothreonine (By similarity).
FT   MOD_RES     718    718       Phosphoserine (By similarity).
FT   MOD_RES     740    740       Phosphothreonine (By similarity).
FT   MOD_RES     741    741       Phosphoserine.
FT   MOD_RES     745    745       Phosphoserine (By similarity).
FT   MOD_RES     753    753       Phosphoserine (By similarity).
FT   MOD_RES     797    797       Phosphoserine (By similarity).
FT   MOD_RES     808    808       Phosphoserine (By similarity).
FT   MOD_RES     820    820       Phosphoserine (By similarity).
FT   MOD_RES     828    828       Phosphoserine (By similarity).
FT   MOD_RES     832    832       Phosphoserine.
FT   MOD_RES     834    834       Phosphoserine (By similarity).
FT   MOD_RES     836    836       Phosphoserine.
FT   MOD_RES     859    859       Phosphoserine (By similarity).
FT   MOD_RES     860    860       Phosphoserine (By similarity).
FT   VAR_SEQ     519    588       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_011583.
FT   VAR_SEQ     589    649       Missing (in isoform 3).
FT                                /FTId=VSP_011584.
FT   CONFLICT    145    146       VY -> HE (in Ref. 2; AAB19202).
FT   CONFLICT    528    528       H -> P (in Ref. 2; AAB19202).
FT   CONFLICT    550    550       H -> P (in Ref. 2; AAB19202).
FT   CONFLICT    554    563       PSRPPSRPSR -> RAEFLQPGDP (in Ref. 2;
FT                                AAB19202).
SQ   SEQUENCE   1285 AA;  136485 MW;  2C72EF68A79F3793 CRC64;
     MRSSTAAVQR PAAGDPEPRR PAGWAARRSL PRTARRGGRG GAVAYPSAGP PPRGPGAPPR
     GPRSPPCASD CFGSNGHGAS RPGSRRLLGV CGPPRPFVVV LLALAPAATP ARACPPGVRA
     SPPRSGVSSS ARPAPGCPRP ACEPVYGPLT MSLKPQPQPP APATGRKPGG GLLSSPGAAP
     ASAAVTSASV VPAPAAPVAS SSAAAGGGRP GLGRGRNSSK GLPQPTISFD GIYANVRMVH
     ILTSVVGSKC EVQVKNGGIY EGVFKTYSPK CDLVLDAAHE KSTESSSGPK REEIMESVLF
     KCSDFVVVQF KDTDSSYARR DAFTDSALSA KVNGEHKEKD LEPWDAGELT ASEELELEND
     VSNGWDPNDM FRYNEENYGV VSTYDSSLSS YTVPLERDNS EEFLKREARA NQLAEEIESS
     AQYKARVALE NDDRSEEEKY TAVQRNCSDR EGHGPNTRDN KYIPPGQRNR EVLSWGSGRQ
     SSPRMGQPGP GSMPSRAASH TSDFNPNAGS DQRVVNGGVP WPSPCPSHSS RPPSRYQSGP
     NSLPPRAATH TRPPSRPPSR PSRPPSHPSA HGSPAPVSTM PKRMSSEGPP RMSPKAQRHP
     RNHRVSAGRG SMSSGLEFVS HNPPSEAAAP PVARTSPAGG TWSSVVSGVP RLSPKTHRPR
     SPRQSSIGNS PSGPVLASPQ AGIIPAEAVS MPVPAASPTP ASPASNRALT PSIEAKDSRL
     QDQRQNSPAG SKENVKASET SPSFSKADNK GMSPVVSEHR KQIDDLKKFK NDFRLQPSST
     SESMDQLLSK NREGEKSRDL IKDKTEASAK DSFIDSSSSS SNCTSGSSKT NSPSISPSML
     SNAEHKRGPE VTSQGVQTSS PACKQEKDDR EEKKDTTEQV RKSTLNPNAK EFNPRSFSQP
     KPSTTPTSPR PQAQPSPSMV GHQQPAPVYT QPVCFAPNMM YPVPVSPGVQ PLYPIPMTPM
     PVNQAKTYRA GKVPNMPQQR QDQHHQSTMM HPASAAGPPI VATPPAYSTQ YVAYSPQQFP
     NQPLVQHVPH YQSQHPHVYS PVIQGNARMM APPAHAQPGL VSSSAAQFGA HEQTHAMYAC
     PKLPYNKETS PSFYFAISTG SLAQQYAHPN AALHPHTPHP QPSATPTGQQ QSQHGGSHPA
     PSPVQHHQHQ AAQALHLASP QQQSAIYHAG LAPTPPSMTP ASNTQSPQSS FPAAQQTVFT
     IHPSHVQPAY TTPPHMAHVP QAHVQSGMVP SHPTAHAPMM LMTTQPPGPK AALAQSALQP
     IPVSTTAHFP YMTHPSVQAH HQQQL
//
ID   NMT1_MOUSE              Reviewed;         496 AA.
AC   O70310;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Glycylpeptide N-tetradecanoyltransferase 1;
DE            EC=2.3.1.97;
DE   AltName: Full=Myristoyl-CoA:protein N-myristoyltransferase 1;
DE            Short=NMT 1;
DE            Short=Type I N-myristoyltransferase;
DE   AltName: Full=Peptide N-myristoyltransferase 1;
GN   Name=Nmt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=98175914; PubMed=9506952; DOI=10.1074/jbc.273.12.6595;
RA   Giang D.K., Cravatt B.F.;
RT   "A second mammalian N-myristoyltransferase.";
RL   J. Biol. Chem. 273:6595-6598(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Adds a myristoyl group to the N-terminal glycine residue
CC       of certain cellular and viral proteins.
CC   -!- CATALYTIC ACTIVITY: Tetradecanoyl-CoA + glycylpeptide = CoA + N-
CC       tetradecanoylglycylpeptide.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the NMT family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF043326; AAC09296.1; -; mRNA.
DR   EMBL; BC016526; AAH16526.1; -; mRNA.
DR   EMBL; BC021635; AAH21635.1; -; mRNA.
DR   IPI; IPI00224128; -.
DR   RefSeq; NP_032733.1; NM_008707.3.
DR   UniGene; Mm.10265; -.
DR   ProteinModelPortal; O70310; -.
DR   SMR; O70310; 87-496.
DR   STRING; O70310; -.
DR   PhosphoSite; O70310; -.
DR   PRIDE; O70310; -.
DR   Ensembl; ENSMUST00000021314; ENSMUSP00000021314; ENSMUSG00000020936.
DR   GeneID; 18107; -.
DR   KEGG; mmu:18107; -.
DR   UCSC; uc007ltd.1; mouse.
DR   CTD; 18107; -.
DR   MGI; MGI:102579; Nmt1.
DR   eggNOG; roNOG05621; -.
DR   HOGENOM; HBG314670; -.
DR   HOVERGEN; HBG003404; -.
DR   InParanoid; O70310; -.
DR   OMA; YRLPETP; -.
DR   OrthoDB; EOG4C5CJ6; -.
DR   PhylomeDB; O70310; -.
DR   BRENDA; 2.3.1.97; 244.
DR   NextBio; 293293; -.
DR   ArrayExpress; O70310; -.
DR   Bgee; O70310; -.
DR   CleanEx; MM_NMT1; -.
DR   Genevestigator; O70310; -.
DR   GermOnline; ENSMUSG00000020936; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; TAS:MGI.
DR   GO; GO:0004379; F:glycylpeptide N-tetradecanoyltransferase activity; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0006499; P:N-terminal protein myristoylation; IMP:MGI.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000903; MyristoylCoA_TrFase.
DR   InterPro; IPR022677; MyristoylCoA_TrFase_C.
DR   InterPro; IPR022678; MyristoylCoA_TrFase_CS.
DR   InterPro; IPR022676; MyristoylCoA_TrFase_N.
DR   Gene3D; G3DSA:3.40.630.30; Acyl_CoA_acyltransferase; 2.
DR   PANTHER; PTHR11377; Myristoyl_trans; 1.
DR   Pfam; PF01233; NMT; 1.
DR   Pfam; PF02799; NMT_C; 1.
DR   PIRSF; PIRSF015892; N-myristl_transf; 1.
DR   SUPFAM; SSF55729; Acyl_CoA_acyltransferase; 2.
DR   PROSITE; PS00975; NMT_1; 1.
DR   PROSITE; PS00976; NMT_2; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Cytoplasm; Phosphoprotein; Transferase.
FT   CHAIN         1    496       Glycylpeptide N-tetradecanoyltransferase
FT                                1.
FT                                /FTId=PRO_0000064222.
FT   COMPBIAS     55     67       Poly-Lys.
FT   MOD_RES      31     31       Phosphoserine.
FT   MOD_RES      47     47       Phosphoserine (By similarity).
SQ   SEQUENCE   496 AA;  56888 MW;  61FA7B854A5CF3BC CRC64;
     MADESETAVK LPAPSLPLMM EGNGNGHEHC SDCENEEDNS HNRSGLSPAN DTGAKKKKKK
     QKKKKEKGSD MESTQDQPVK MTSLPAERIQ EIQKAIELFS VGQGPAKTME EASKRSYQFW
     DTQPVPKLGE VVNTHGPVEP DKDNIRQEPY TLPQGFTWDA LDLGDRGVLK ELYTLLNENY
     VEDDDNMFRF DYSPEFLLWA LRPPGWLPQW HCGVRVVSSR KLVGFISAIP ANIHIYDTEK
     KMVEINFLCV HKKLRSKRVA PVLIREITRR VHLEGIFQAV YTAGVVLPKP VGTCRYWHRS
     LNPRKLIEVK FSHLSRNMTM QRTMKLYRLP ETPKTAGLRP MEKKDIPVVH QLLSRYLKQF
     HLTPVMNQEE VEHWFYPQEN IIDTFVVENA NGEVTDFLSF YTLPSTIMNH PTHKSLKAAY
     SFYNVHTQTP LLDLMSDALV LAKMKGFDVF NALDLMENKT FLEKLKFGIG DGNLQYYLYN
     WKCPSMGAEK VGLVLQ
//
ID   MOT8_MOUSE              Reviewed;         545 AA.
AC   O70324; Q8K3S9;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Monocarboxylate transporter 8;
DE            Short=MCT 8;
DE   AltName: Full=Solute carrier family 16 member 2;
DE   AltName: Full=X-linked PEST-containing transporter;
GN   Name=Slc16a2; Synonyms=Mct8, Xpct;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=98207244; PubMed=9545634; DOI=10.1006/geno.1997.5173;
RA   Debrand E., Heard E., Avner P.;
RT   "Cloning and localization of the murine Xpct gene: evidence for
RT   complex rearrangements during the evolution of the region around the
RT   Xist gene.";
RL   Genomics 48:296-303(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=22040331; PubMed=12045143; DOI=10.1101/gr.152902;
RA   Chureau C., Prissette M., Bourdet A., Barbe V., Cattolico L.,
RA   Jones L., Eggen A., Avner P., Duret L.;
RT   "Comparative sequence analysis of the X-inactivation center region in
RT   mouse, human and bovine.";
RL   Genome Res. 12:894-908(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Very active and specific thyroid hormone transporter.
CC       Stimulates cellular uptake of thyroxine (T4), triiodothyronine
CC       (T3), reverse triiodothyronine (rT3) and diidothyronine. Does not
CC       transport Leu, Phe, Trp or Tyr (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in liver and kidney.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       Monocarboxylate porter (TC 2.A.1.13) family.
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DR   EMBL; AF045692; AAC40078.1; -; mRNA.
DR   EMBL; AJ421478; CAD33931.1; -; Genomic_DNA.
DR   EMBL; BC080678; AAH80678.1; -; mRNA.
DR   IPI; IPI00353962; -.
DR   RefSeq; NP_033223.2; NM_009197.2.
DR   UniGene; Mm.388973; -.
DR   ProteinModelPortal; O70324; -.
DR   SMR; O70324; 228-262.
DR   STRING; O70324; -.
DR   TCDB; 2.A.1.13.3; major facilitator superfamily (MFS).
DR   PhosphoSite; O70324; -.
DR   PRIDE; O70324; -.
DR   Ensembl; ENSMUST00000042664; ENSMUSP00000037629; ENSMUSG00000033965.
DR   GeneID; 20502; -.
DR   KEGG; mmu:20502; -.
DR   UCSC; uc009tzy.1; mouse.
DR   CTD; 20502; -.
DR   MGI; MGI:1203732; Slc16a2.
DR   HOGENOM; HBG717340; -.
DR   HOVERGEN; HBG006387; -.
DR   InParanoid; O70324; -.
DR   OMA; FPFLIRM; -.
DR   OrthoDB; EOG4H72BN; -.
DR   PhylomeDB; O70324; -.
DR   NextBio; 298675; -.
DR   ArrayExpress; O70324; -.
DR   Bgee; O70324; -.
DR   Genevestigator; O70324; -.
DR   GermOnline; ENSMUSG00000033965; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   InterPro; IPR020846; Major_facilitator_SF.
DR   InterPro; IPR011701; MFS_1.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell membrane; Membrane; Phosphoprotein; Repeat; Symport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    545       Monocarboxylate transporter 8.
FT                                /FTId=PRO_0000211402.
FT   TOPO_DOM      2    102       Cytoplasmic (Potential).
FT   TRANSMEM    103    123       Helical; (Potential).
FT   TOPO_DOM    124    149       Extracellular (Potential).
FT   TRANSMEM    150    170       Helical; (Potential).
FT   TOPO_DOM    171    177       Cytoplasmic (Potential).
FT   TRANSMEM    178    198       Helical; (Potential).
FT   TOPO_DOM    199    206       Extracellular (Potential).
FT   TRANSMEM    207    227       Helical; (Potential).
FT   TOPO_DOM    228    235       Cytoplasmic (Potential).
FT   TRANSMEM    236    256       Helical; (Potential).
FT   TOPO_DOM    257    264       Extracellular (Potential).
FT   TRANSMEM    265    285       Helical; (Potential).
FT   TOPO_DOM    286    328       Cytoplasmic (Potential).
FT   TRANSMEM    329    349       Helical; (Potential).
FT   TOPO_DOM    350    362       Extracellular (Potential).
FT   TRANSMEM    363    383       Helical; (Potential).
FT   TOPO_DOM    384    392       Cytoplasmic (Potential).
FT   TRANSMEM    393    413       Helical; (Potential).
FT   TOPO_DOM    414    415       Extracellular (Potential).
FT   TRANSMEM    416    436       Helical; (Potential).
FT   TOPO_DOM    437    453       Cytoplasmic (Potential).
FT   TRANSMEM    454    474       Helical; (Potential).
FT   TOPO_DOM    475    483       Extracellular (Potential).
FT   TRANSMEM    484    504       Helical; (Potential).
FT   TOPO_DOM    505    545       Cytoplasmic (Potential).
FT   REPEAT       29     50       1.
FT   REPEAT       51     72       2.
FT   REGION       29     72       2 X 22 AA approximate tandem repeats.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     199    199       Phosphoserine (By similarity).
FT   MOD_RES     201    201       Phosphoserine (By similarity).
FT   CONFLICT     62     62       Q -> QPLPDPAPLPELGFEAEPEPQ (in Ref. 1).
FT   CONFLICT    227    227       G -> D (in Ref. 1; AAC40078).
SQ   SEQUENCE   545 AA;  60025 MW;  ACCC7EC6B902A6DE CRC64;
     MALPSPASEE AEGPCQEANQ EYQEPVCSPV PEPEPEPEPE PEPDPEPVPV PPPEPQPEPE
     PQPLPDPAPL PELGFEAEPV QEPEPTPTVE TRGTARGFQP PEGGFGWIVV FAATWCNGSI
     FGIHNSVGIL YSMLLEEEKE KNRQVEFQAA WVGALAMGMI FFCSPIVSIF TDRLGCRITA
     TTGAAVAFIG LHTSSFTSSL SLRYFTYGIL FGCGCSFAFQ PSLVILGHYF QRRLGLANGV
     VSAGSSIFSM SFPFLIKMLG DKIKLAQTFQ VLSTFMFVLT LLSLTYRPLL PSSQDTPSKR
     GAHTLRQRFL VQFRKYFNMR VFRQRTYRIW AFGIAAAALG YFVPYVHLMK YVEDKFKEIK
     ETWVLLVCIG ATSGLGRLVS GHISDSIPGL KKIYLQVLSF LLLGLMSMMI PLCRDFGGLI
     VVCLFLGLCD GFFITIMAPI AFELVGPMQA SQAIGYLLGM MALPMIAGPP IAGLLRNCFG
     DYHVAFYFAG VPPIIGAVIL FFVPLMHQRM FKKEQRDSSK DKMLSHDPDP NGELLPGSPT
     PEEPI
//
ID   O70349_MOUSE            Unreviewed;      1236 AA.
AC   O70349;
DT   01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT   01-AUG-1998, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   SubName: Full=MCG15924, isoform CRA_a;
DE   SubName: Full=Putative uncharacterized protein SKI;
GN   Name=Skiv2l; Synonyms=SKI, Stk19; ORFNames=mCG_15924;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129;
RX   PubMed=14656967; DOI=10.1101/gr.1736803;
RA   Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
RA   Campbell R.D., Hood L.;
RT   "Analysis of the gene-dense major histocompatibility complex class III
RT   region and its comparison to mouse.";
RL   Genome Res. 13:2621-2636(2003).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AF049850; AAC05282.1; -; Genomic_DNA.
DR   EMBL; CH466666; EDL26752.1; -; Genomic_DNA.
DR   IPI; IPI00454140; -.
DR   UniGene; Mm.18845; -.
DR   ProteinModelPortal; O70349; -.
DR   SMR; O70349; 303-743.
DR   STRING; O70349; -.
DR   PRIDE; O70349; -.
DR   Ensembl; ENSMUST00000046022; ENSMUSP00000036265; ENSMUSG00000040356.
DR   MGI; MGI:1099835; Skiv2l.
DR   eggNOG; roNOG12634; -.
DR   HOVERGEN; HBG060025; -.
DR   InParanoid; O70349; -.
DR   OrthoDB; EOG47H5P5; -.
DR   ArrayExpress; O70349; -.
DR   Bgee; O70349; -.
DR   Genevestigator; O70349; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR012961; DSH_C.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR016438; RNA_helicase_ATP-dep_SK12/DOB1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF08148; DSHCT; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding.
SQ   SEQUENCE   1236 AA;  136655 MW;  7E8F8060896BE55E CRC64;
     MMETERLDPL NLPLRALEVG CTGRWELLNV PGPPESTLPH GLPPCAPDLC QEAEQLFLSS
     PAWLPLHGVE HSARKWQRKT DPWSLLAAVE TPVPSDLQAQ RHPTTGHILG YKEVLLENTN
     LSATTSLSLR RPPGPASQSL WGNPTQYPFW PGGMDEPSIT DLHTREEAEE EIDFEKDLLT
     VPPGFKKGVD FAPKAPVPGL LSLSRLLEPL DLSGGDEDEG EAAGGPRGDN ASPSPSGTPL
     VRASSLEDLV LKEAATVVST PEPPKPPPQE QWAVPVDVTS PVGDFYRLIP QPAFQWAFEP
     DVFQKQAILH LEQHDSVFVA AHTSAGKTVV AEYAIALAQK HMTRTIYTSP IKALSNQKFR
     DFRNTFGDVG LLTGDVQLHP EASCLIMTTE ILRSMLYSGS DVIRDLEWVI FDEVHYINDA
     ERGVVWEEVL IMLPEHVSII LLSATVPNAL EFADWIGRLK RRQIYVISTV ARPVPLEHYL
     FTGNSPKTQG ELFLLLDSRG AFHTQGYYAA VEAKKERMSK HAQTFGAKQP THQGGPAQDR
     GVYLSLLASL RTRAQLPVVV FTFSRGRCDE QASGLTSLDL TTSSEKSEIH LFLQRCLARL
     RGSDRQLPQV LHMSELLRRG LGVHHSGILP ILKEIVEMLF SRGLVKVLFA TETFAMGVNM
     PARTVVFDSM RKHDGSTFRD LLPGEYVQMA GRAGRRGLDP TGTVILLCKG RVPEMADLHR
     MMMGKPSQLQ SQFRLTYTMI LNLLRVDALR VEDMMKRSFS EFPSRKDSKA HEQALADLTK
     RLGALEEPDV TGQLADLPEY YSWAEELTET QNMIQRRIME SVNGLKSLSV GRVVVVKNEE
     HHNALGVILQ VSSNSTSRVF TTLVLCDKPV VSDNPRDKGP ATPDVPHPDD LIGFKLFLPE
     GPCEHTVAKL QPGDVAAIST KVLRVNGEKI SEDFSKRQQP KFRKDPPLAA VTTAVQELLR
     LAQSYPAGPP TLDPINDLQL KDVAVVEGGL RARKLEELIR GAQCVHSPRF PAQYVKLRER
     MQIQKEMERL RFLLSDQSLL LLPEYHQRVE VLRTLGYVDE AGTVKLAGRV ACAMSSHELL
     LTELMFDNAL SALRPEEIAA LLSGLVCQSP GDPGDQLPST LKQGVERVKA VAKRIGEVQV
     ACGLNQTVEE FVGELNFGLV EVVYEWARGM PFSELAGLSG TPEGLVVRCI QRLAEMCRSL
     RGAARLVGEP VLGAKMETAA TLLRRDIVFA ASLYTQ
//
ID   STX7_MOUSE              Reviewed;         261 AA.
AC   O70439;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Syntaxin-7;
GN   Name=Stx7; Synonyms=Syn7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adipocyte;
RA   Tellam J., Piper R.C., Smith C., James D.E.;
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION IN A COMPLEX WITH VAMP8 AND VTI1B.
RX   PubMed=15363411; DOI=10.1016/j.devcel.2004.08.002;
RA   Wang C.-C., Ng C.P., Lu L., Atlashkin V., Zhang W., Seet L.-F.,
RA   Hong W.;
RT   "A role of VAMP8/endobrevin in regulated exocytosis of pancreatic
RT   acinar cells.";
RL   Dev. Cell 7:359-371(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-79, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-79, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-126 AND
RP   SER-129, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-129 AND SER-205,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 169-229 IN COMPLEX WITH
RP   VAMP8; STX8 AND VTI1B.
RX   MEDLINE=21671743; PubMed=11786915; DOI=10.1038/nsb746;
RA   Antonin W., Fasshauer D., Becker S., Jahn R., Schneider T.R.;
RT   "Crystal structure of the endosomal SNARE complex reveals common
RT   structural principles of all SNAREs.";
RL   Nat. Struct. Biol. 9:107-111(2002).
CC   -!- FUNCTION: May be involved in protein trafficking from the plasma
CC       membrane to the early endosome (EE) as well as in homotypic fusion
CC       of endocytic organelles. Mediates the endocytic trafficking from
CC       early endosomes to late endosomes and lysosomes (By similarity).
CC   -!- SUBUNIT: Part of the SNARE core complex containing VAMP8, STX8 and
CC       VTI1B. Found in a complex with VAMP8 and VTI1B in the liver. Forms
CC       a SNARE complex with VTI1B, STX8 and VAMP8 which functions in the
CC       homotypic fusion of late endosomes. Interacts with VPS11, VPS16,
CC       VPS18 and VPS33A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane; Single-pass type IV
CC       membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the syntaxin family.
CC   -!- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain.
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DR   EMBL; AF056323; AAC15971.1; -; mRNA.
DR   IPI; IPI00118217; -.
DR   UniGene; Mm.248042; -.
DR   PDB; 1GL2; X-ray; 1.90 A; B=169-228.
DR   PDBsum; 1GL2; -.
DR   ProteinModelPortal; O70439; -.
DR   SMR; O70439; 2-259.
DR   IntAct; O70439; 2.
DR   STRING; O70439; -.
DR   PhosphoSite; O70439; -.
DR   PRIDE; O70439; -.
DR   Ensembl; ENSMUST00000020174; ENSMUSP00000020174; ENSMUSG00000019998.
DR   MGI; MGI:1858210; Stx7.
DR   eggNOG; roNOG10770; -.
DR   HOGENOM; HBG444570; -.
DR   HOVERGEN; HBG053083; -.
DR   InParanoid; O70439; -.
DR   OrthoDB; EOG41NTN3; -.
DR   PhylomeDB; O70439; -.
DR   ArrayExpress; O70439; -.
DR   Bgee; O70439; -.
DR   CleanEx; MM_STX7; -.
DR   Genevestigator; O70439; -.
DR   GermOnline; ENSMUSG00000019998; Mus musculus.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR   InterPro; IPR006011; Syntaxin_N.
DR   InterPro; IPR010989; t-SNARE.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   Pfam; PF05739; SNARE; 1.
DR   Pfam; PF00804; Syntaxin; 1.
DR   SMART; SM00503; SynN; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF47661; t-snare; 1.
DR   PROSITE; PS00914; SYNTAXIN; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Coiled coil; Endosome; Iron; Membrane;
KW   Phosphoprotein; Transmembrane; Transmembrane helix.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    261       Syntaxin-7.
FT                                /FTId=PRO_0000210214.
FT   TOPO_DOM      2    238       Cytoplasmic (Potential).
FT   TRANSMEM    239    259       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   TOPO_DOM    260    261       Vesicular (Potential).
FT   DOMAIN      165    227       t-SNARE coiled-coil homology.
FT   COILED       47     68       Potential.
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES       3      3       Phosphotyrosine (By similarity).
FT   MOD_RES      45     45       Phosphoserine.
FT   MOD_RES      79     79       Phosphothreonine.
FT   MOD_RES     125    125       Phosphoserine.
FT   MOD_RES     126    126       Phosphoserine.
FT   MOD_RES     129    129       Phosphoserine.
FT   MOD_RES     205    205       Phosphoserine.
FT   HELIX       170    226
SQ   SEQUENCE   261 AA;  29821 MW;  62F4E4B33F247ADB CRC64;
     MSYTPGIGGD SAQLAQRISS NIQKITQCSV EIQRTLNQLG TPQDSPELRQ LLQQKQQYTN
     QLAKETDKYI KEFGSLPTTP SEQRQRKIQK DRLVAEFTTS LTNFQKAQRQ AAEREKEFVA
     RVRASSRVSG GFPEDSSKEK NLVSWESQTQ PQVQVQDEEI TEDDLRLIHE RESSIRQLEA
     DIMDINEIFK DLGMMIHEQG DMIDSIEANV ESAEVHVQQA NQQLSRAADY QRKSRKTLCI
     IIFILVVRIV IICLIVWGLK G
//
ID   GNAZ_MOUSE              Reviewed;         355 AA.
AC   O70443; O70442; Q61637; Q91WM4;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   08-MAR-2011, entry version 102.
DE   RecName: Full=Guanine nucleotide-binding protein G(z) subunit alpha;
DE   AltName: Full=G(x) alpha chain;
DE   AltName: Full=Gz-alpha;
GN   Name=Gnaz;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 1-353.
RC   STRAIN=C57BL/6;
RA   Matthaei K.I., Mellick A.M., Hendry I.A.;
RT   "Partial genomic sequence of the mouse GTP binding protein Gz alpha.";
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 207-267.
RC   STRAIN=BALB/c; TISSUE=Pancreatic islet;
RX   MEDLINE=94283273; PubMed=8013366; DOI=10.1210/en.135.1.31;
RA   Zigman J.M., Westermark G.T., LaMendola J., Steiner D.F.;
RT   "Expression of cone transducin, Gz alpha, and other G-protein alpha-
RT   subunit messenger ribonucleic acids in pancreatic islets.";
RL   Endocrinology 135:31-37(1994).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC       involved as modulators or transducers in various transmembrane
CC       signaling systems.
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and
CC       gamma. The alpha chain contains the guanine nucleotide binding
CC       site.
CC   -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
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DR   EMBL; BC014702; AAH14702.1; -; mRNA.
DR   EMBL; AF056973; AAC13569.1; -; Genomic_DNA.
DR   EMBL; AF056972; AAC13568.1; -; mRNA.
DR   EMBL; L17074; AAC37651.1; -; mRNA.
DR   IPI; IPI00230193; -.
DR   RefSeq; NP_034441.1; NM_010311.3.
DR   UniGene; Mm.32595; -.
DR   UniGene; Mm.393508; -.
DR   ProteinModelPortal; O70443; -.
DR   SMR; O70443; 6-349.
DR   STRING; O70443; -.
DR   PhosphoSite; O70443; -.
DR   PRIDE; O70443; -.
DR   Ensembl; ENSMUST00000037813; ENSMUSP00000036087; ENSMUSG00000040009.
DR   GeneID; 14687; -.
DR   KEGG; mmu:14687; -.
DR   UCSC; uc007fpt.1; mouse.
DR   CTD; 14687; -.
DR   MGI; MGI:95780; Gnaz.
DR   eggNOG; roNOG07247; -.
DR   HOGENOM; HBG444960; -.
DR   HOVERGEN; HBG063184; -.
DR   InParanoid; O70443; -.
DR   OMA; IPLTVCF; -.
DR   OrthoDB; EOG4T4CVQ; -.
DR   PhylomeDB; O70443; -.
DR   NextBio; 286627; -.
DR   ArrayExpress; O70443; -.
DR   Bgee; O70443; -.
DR   Genevestigator; O70443; -.
DR   GermOnline; ENSMUSG00000040009; Mus musculus.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; TAS:MGI.
DR   GO; GO:0005624; C:membrane fraction; TAS:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; TAS:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   InterPro; IPR001408; Gprotein_alpha_I.
DR   InterPro; IPR001019; Gprotein_alpha_su.
DR   InterPro; IPR011025; GproteinA_insert.
DR   Gene3D; G3DSA:1.10.400.10; GproteinA_insert; 1.
DR   PANTHER; PTHR10218; Gprotein_alph_bd; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00441; GPROTEINAI.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF47895; Transducn_insert; 1.
PE   2: Evidence at transcript level;
KW   GTP-binding; Lipoprotein; Membrane; Myristate; Nucleotide-binding;
KW   Palmitate; Transducer.
FT   INIT_MET      1      1       Removed (Probable).
FT   CHAIN         2    355       Guanine nucleotide-binding protein G(z)
FT                                subunit alpha.
FT                                /FTId=PRO_0000203697.
FT   NP_BIND      40     47       GTP (By similarity).
FT   NP_BIND     201    205       GTP (By similarity).
FT   NP_BIND     270    273       GTP (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
FT   LIPID         3      3       S-palmitoyl cysteine (By similarity).
FT   CONFLICT    210    210       K -> R (in Ref. 3; AAC37651).
SQ   SEQUENCE   355 AA;  40850 MW;  24590AE5B1FE5D50 CRC64;
     MGCRQSSEEK EAARRSRRID RHLRSESQRQ RREIKLLLLG TSNSGKSTIV KQMKIIHSGG
     FNLDACKEYK PLIIYNAIDS LTRIIRALAA LKIDFHNPDR AYDAVQLFAL TGPAESKGEI
     TPELLGVMRR LWADPGAQAC FGRSSEYHLE DNAAYYLNDL ERIAAPDYIP TVEDILRSRD
     MTTGIVENKF TFKELTFKMV DVGGQRSERK KWIHCFEGVT AIIFCVELSG YDLKLYEDNQ
     TSRMAESLRL FDSICNNNWF INTSLILFLN KKDLLAEKIR RIPLSVCFPE YKGQNTYEEA
     AVYIQRQFED LNRNKETKEI YSHFTCATDT SNIQFVFDAV TDVIIQNNLK YIGLC
//
ID   1433S_MOUSE             Reviewed;         248 AA.
AC   O70456;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=14-3-3 protein sigma;
DE   AltName: Full=Stratifin;
GN   Name=Sfn; Synonyms=Mkrn3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=FVB/N;
RA   Karpitskiy V.V., Shaw A.S.;
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 1-12; 42-49; 61-68 AND 215-224, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND SER-216, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15648052; DOI=10.1002/pmic.200401066;
RA   Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA   Hart G.W., Burlingame A.L.;
RT   "Quantitative analysis of both protein expression and serine /
RT   threonine post-translational modifications through stable isotope
RT   labeling with dithiothreitol.";
RL   Proteomics 5:388-398(2005).
RN   [4]
RP   FUNCTION, INTERACTION WITH KRT17, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RX   PubMed=16710422; DOI=10.1038/nature04659;
RA   Kim S., Wong P., Coulombe P.A.;
RT   "A keratin cytoskeletal protein regulates protein synthesis and
RT   epithelial cell growth.";
RL   Nature 441:362-365(2006).
CC   -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC       spectrum of both general and specialized signaling pathway. Binds
CC       to a large number of partners, usually by recognition of a
CC       phosphoserine or phosphothreonine motif. Binding generally results
CC       in the modulation of the activity of the binding partner. When
CC       bound to KRT17, regulates protein synthesis and epithelial cell
CC       growth by stimulating Akt/mTOR pathway.
CC   -!- SUBUNIT: Homodimer. Found in a complex with XPO7, EIF4A1, ARHGAP1,
CC       VPS26A, VPS29, VPS35 and SFN. Interacts with GAB2 (By similarity).
CC       Interacts with KRT17.
CC   -!- INTERACTION:
CC       Q9QWL7:Krt17; NbExp=2; IntAct=EBI-1544118, EBI-309015;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Secreted (By
CC       similarity). Note=May be secreted by a non-classical secretory
CC       pathway (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in the basal layer of skin
CC       epithelium and in outer root sheath of hair follicle.
CC   -!- INDUCTION: Induced in damaged or stressed epidermis.
CC   -!- MISCELLANEOUS: 14-3-3 proteins have been shown to be PKC
CC       activators, but this effect could be non-specific and only due to
CC       the acidic nature of the protein.
CC   -!- SIMILARITY: Belongs to the 14-3-3 family.
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DR   EMBL; AF058798; AAC14344.1; -; mRNA.
DR   IPI; IPI00118286; -.
DR   UniGene; Mm.44482; -.
DR   ProteinModelPortal; O70456; -.
DR   SMR; O70456; 1-231.
DR   IntAct; O70456; 3.
DR   MINT; MINT-240814; -.
DR   STRING; O70456; -.
DR   PRIDE; O70456; -.
DR   Ensembl; ENSMUST00000057311; ENSMUSP00000050374; ENSMUSG00000047281.
DR   MGI; MGI:1891831; Sfn.
DR   eggNOG; roNOG05103; -.
DR   HOGENOM; HBG611720; -.
DR   HOVERGEN; HBG050423; -.
DR   InParanoid; O70456; -.
DR   OrthoDB; EOG4XH00X; -.
DR   PhylomeDB; O70456; -.
DR   ArrayExpress; O70456; -.
DR   Bgee; O70456; -.
DR   CleanEx; MM_MKRN3; -.
DR   CleanEx; MM_SFN; -.
DR   Genevestigator; O70456; -.
DR   GermOnline; ENSMUSG00000047281; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; IEA:InterPro.
DR   GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI.
DR   GO; GO:0043616; P:keratinocyte proliferation; IGI:MGI.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IGI:MGI.
DR   GO; GO:0030307; P:positive regulation of cell growth; IDA:UniProtKB.
DR   GO; GO:0000079; P:regulation of cyclin-dependent protein kinase activity; IDA:MGI.
DR   GO; GO:0043588; P:skin development; IMP:MGI.
DR   InterPro; IPR000308; 14-3-3.
DR   PANTHER; PTHR18860; 14-3-3; 1.
DR   PIRSF; PIRSF000868; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein;
KW   Secreted.
FT   CHAIN         1    248       14-3-3 protein sigma.
FT                                /FTId=PRO_0000058644.
FT   SITE         56     56       Interaction with phosphoserine on
FT                                interacting protein (By similarity).
FT   SITE        129    129       Interaction with phosphoserine on
FT                                interacting protein (By similarity).
FT   MOD_RES      64     64       Phosphoserine.
FT   MOD_RES     216    216       Phosphoserine.
SQ   SEQUENCE   248 AA;  27713 MW;  D433390433FB3F48 CRC64;
     MERASLIQKA KLAEQAERYE DMAAFMKSAV EKGEELSCEE RNLLSVAYKN VVGGQRAAWR
     VLSSIEQKSN EEGSEEKGPE VKEYREKVET ELRGVCDTVL GLLDSHLIKG AGDAESRVFY
     LKMKGDYYRY LAEVATGDDK KRIIDSARSA YQEAMDISKK EMPPTNPIRL GLALNFSVFH
     YEIANSPEEA ISLAKTTFDE AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADSAGEEGG
     EAPDDPHI
//
ID   VAMP4_MOUSE             Reviewed;         141 AA.
AC   O70480; Q9D095;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   08-FEB-2011, entry version 93.
DE   RecName: Full=Vesicle-associated membrane protein 4;
DE            Short=VAMP-4;
GN   Name=Vamp4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Zhang T., Wong S.H., Xu Y., Hong W.;
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-30, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 47-117 IN COMPLEX WITH
RP   STX13; VTI1A AND STX6, AND SUBUNIT.
RX   PubMed=17159904; DOI=10.1038/sj.emboj.7601467;
RA   Zwilling D., Cypionka A., Pohl W.H., Fasshauer D., Walla P.J.,
RA   Wahl M.C., Jahn R.;
RT   "Early endosomal SNAREs form a structurally conserved SNARE complex
RT   and fuse liposomes with multiple topologies.";
RL   EMBO J. 26:9-18(2007).
CC   -!- FUNCTION: Involved in the pathway that functions to remove an
CC       inhibitor (probably synaptotagmin-4) of calcium-triggered
CC       exocytosis during the maturation of secretory granules. May be a
CC       marker for this sorting pathway that is critical for remodeling
CC       the secretory response of granule (By similarity).
CC   -!- SUBUNIT: Identified in a complex containing STX6, STX13, VAMP4 and
CC       VTI1A.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC       membrane; Single-pass type IV membrane protein (Probable).
CC       Note=Associated with trans Golgi network (TGN) and newly formed
CC       immature secretory granules (ISG). Not found on the mature
CC       secretory organelles (By similarity).
CC   -!- SIMILARITY: Belongs to the synaptobrevin family.
CC   -!- SIMILARITY: Contains 1 v-SNARE coiled-coil homology domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF061516; AAC15776.1; -; mRNA.
DR   EMBL; AK011678; BAB27774.1; -; mRNA.
DR   EMBL; AK018344; BAB31171.1; -; mRNA.
DR   IPI; IPI00118372; -.
DR   UniGene; Mm.10699; -.
DR   PDB; 2NPS; X-ray; 2.50 A; A=47-117.
DR   PDBsum; 2NPS; -.
DR   ProteinModelPortal; O70480; -.
DR   SMR; O70480; 49-111.
DR   STRING; O70480; -.
DR   PhosphoSite; O70480; -.
DR   PRIDE; O70480; -.
DR   Ensembl; ENSMUST00000086068; ENSMUSP00000083236; ENSMUSG00000026696.
DR   UCSC; uc007dgk.1; mouse.
DR   MGI; MGI:1858730; Vamp4.
DR   eggNOG; roNOG16700; -.
DR   GeneTree; ENSGT00550000074449; -.
DR   HOVERGEN; HBG061695; -.
DR   OMA; RNDKIRH; -.
DR   PhylomeDB; O70480; -.
DR   ArrayExpress; O70480; -.
DR   Bgee; O70480; -.
DR   CleanEx; MM_VAMP4; -.
DR   Genevestigator; O70480; -.
DR   GermOnline; ENSMUSG00000026696; Mus musculus.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR001388; Synaptobrevin.
DR   InterPro; IPR016444; Synaptobrevin_met/fun.
DR   Pfam; PF00957; Synaptobrevin; 1.
DR   PIRSF; PIRSF005409; Synaptobrevin_euk; 1.
DR   PRINTS; PR00219; SYNAPTOBREVN.
DR   PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR   PROSITE; PS50892; V_SNARE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Golgi apparatus; Membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    141       Vesicle-associated membrane protein 4.
FT                                /FTId=PRO_0000206732.
FT   TOPO_DOM      1    118       Cytoplasmic (Potential).
FT   TRANSMEM    119    139       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   TOPO_DOM    140    141       Vesicular (Potential).
FT   DOMAIN       52    112       v-SNARE coiled-coil homology.
FT   MOD_RES      17     17       Phosphoserine.
FT   MOD_RES      30     30       Phosphoserine.
FT   CONFLICT    113    113       G -> V (in Ref. 2; BAB27774).
FT   STRAND       51     53
FT   HELIX        54     57
FT   HELIX        60    109
SQ   SEQUENCE   141 AA;  16353 MW;  556CCCB8213CF91E CRC64;
     MPPKFKRHLN DDDVTGSVKS ERRNLLEDDS DEEEDFFLRG PSGPRFGPRN DKIKHVQNQV
     DEVIDVMQEN ITKVIERGER LDELQDKSES LSDNATAFSN RSKQLRRQMW WRGCKIKAIM
     ALAAAILLLM IIILIVVKFR T
//
ID   UBR1_MOUSE              Reviewed;        1757 AA.
AC   O70481; Q5BKR8; Q792M3; Q8BN40; Q8C5K3;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=E3 ubiquitin-protein ligase UBR1;
DE            EC=6.3.2.-;
DE   AltName: Full=N-recognin-1;
DE   AltName: Full=Ubiquitin-protein ligase E3-alpha-1;
DE   AltName: Full=Ubiquitin-protein ligase E3-alpha-I;
GN   Name=Ubr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=129/SvJ;
RX   MEDLINE=98318583; PubMed=9653112; DOI=10.1073/pnas.95.14.7898;
RA   Kwon Y.T., Reiss Y., Fried V.A., Hershko A., Yoon J.K., Gonda D.K.,
RA   Sangan P., Copeland N.G., Jenkins N.A., Varshavsky A.;
RT   "The mouse and human genes encoding the recognition component of the
RT   N-end rule pathway.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:7898-7903(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-849 AND 1529-1757.
RC   STRAIN=NOD; TISSUE=Olfactory bulb, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-852.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=11689692; DOI=10.1128/MCB.21.23.8007-8021.2001;
RA   Kwon Y.T., Xia Z., Davydov I.V., Lecker S.H., Varshavsky A.;
RT   "Construction and analysis of mouse strains lacking the ubiquitin
RT   ligase UBR1 (E3alpha) of the N-end rule pathway.";
RL   Mol. Cell. Biol. 21:8007-8021(2001).
RN   [5]
RP   TISSUE SPECIFICITY, AND FUNCTION.
RX   MEDLINE=22948832; PubMed=14585983;
RX   DOI=10.1128/MCB.23.22.8255-8271.2003;
RA   Kwon Y.T., Xia Z., An J.Y., Tasaki T., Davydov I.V., Seo J.W.,
RA   Sheng J., Xie Y., Varshavsky A.;
RT   "Female lethality and apoptosis of spermatocytes in mice lacking the
RT   UBR2 ubiquitin ligase of the N-end rule pathway.";
RL   Mol. Cell. Biol. 23:8255-8271(2003).
RN   [6]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=15548684; DOI=10.1158/0008-5472.CAN-04-2102;
RA   Kwak K.S., Zhou X., Solomon V., Baracos V.E., Davis J., Bannon A.W.,
RA   Boyle W.J., Lacey D.L., Han H.Q.;
RT   "Regulation of protein catabolism by muscle-specific and cytokine-
RT   inducible ubiquitin ligase E3alpha-II during cancer cachexia.";
RL   Cancer Res. 64:8193-8198(2004).
RN   [7]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=16311597; DOI=10.1038/ng1681;
RA   Zenker M., Mayerle J., Lerch M.M., Tagariello A., Zerres K.,
RA   Durie P.R., Beier M., Hulskamp G., Guzman C., Rehder H., Beemer F.A.,
RA   Hamel B.C.J., Vanlieferinghen P., Gershoni-Baruch R., Vieira M.W.,
RA   Dumic M., Auslender R., Gil-da-Silva-Lopes V.L., Steinlicht S.,
RA   Rauh M., Shalev S.A., Thiel C., Winterpacht A., Kwon Y.T.,
RA   Varshavsky A., Reis A.;
RT   "Deficiency of UBR1, a ubiquitin ligase of the N-end rule pathway,
RT   causes pancreatic dysfunction, malformations and mental retardation
RT   (Johanson-Blizzard syndrome).";
RL   Nat. Genet. 37:1345-1350(2005).
RN   [8]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=16606826; DOI=10.1073/pnas.0601700103;
RA   An J.Y., Seo J.W., Tasaki T., Lee M.J., Varshavsky A., Kwon Y.T.;
RT   "Impaired neurogenesis and cardiovascular development in mice lacking
RT   the E3 ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6212-6217(2006).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which is a component of the
CC       N-end rule pathway. Recognizes and binds to proteins bearing
CC       specific N-terminal residues that are destabilizing according to
CC       the N-end rule, leading to their ubiquitination and subsequent
CC       degradation. May be involved in pancreatic homeostasis. Binds
CC       leucine and is a negative regulator of the leucine-mTOR signaling
CC       pathway, thereby controlling cell growth (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with RECQL4 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity).
CC   -!- TISSUE SPECIFICITY: Present in skeletal muscle and liver (at
CC       protein level). Broadly expressed, with highest levels in skeletal
CC       muscle and heart. Expressed in acinar cells of the pancreas. In
CC       testes, expressed primarily in spermatogonia.
CC   -!- DEVELOPMENTAL STAGE: Expressed in limb buds at E9.5-E11.5.
CC   -!- INDUCTION: In models of cancer cachexia, induced in muscle during
CC       the progression of wasting.
CC   -!- DOMAIN: The RING-H2 zinc finger is an atypical RING finger with a
CC       His ligand in place of the fourth Cys of the classical motif.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice are viable and fertile, but show a
CC       decreased mass of skeletal muscle and adipose tissue. They have
CC       exocrine pancreatic insufficiency with impaired stimulus-secretion
CC       coupling and increased susceptibiliy to pancreatic injury.
CC       UBR1/UBR2 double-knockout embryos die at midgestation, with
CC       defects in neurogenesis and cardiovascular development. These
CC       defects included reduced proliferation as well as precocious
CC       migration and differentiation of neural progenitor cells.
CC   -!- SIMILARITY: Belongs to the UBR1 family.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SIMILARITY: Contains 1 UBR-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH90969.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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DR   EMBL; AF061555; AAC40165.1; -; mRNA.
DR   EMBL; AF067379; AAC23678.1; -; Genomic_DNA.
DR   EMBL; AF067371; AAC23678.1; JOINED; Genomic_DNA.
DR   EMBL; AF067372; AAC23678.1; JOINED; Genomic_DNA.
DR   EMBL; AF067373; AAC23678.1; JOINED; Genomic_DNA.
DR   EMBL; AF067375; AAC23678.1; JOINED; Genomic_DNA.
DR   EMBL; AF067377; AAC23678.1; JOINED; Genomic_DNA.
DR   EMBL; AF067378; AAC23678.1; JOINED; Genomic_DNA.
DR   EMBL; AF067376; AAC23678.1; JOINED; Genomic_DNA.
DR   EMBL; AF067374; AAC23678.1; JOINED; Genomic_DNA.
DR   EMBL; AK078173; BAC37160.1; -; mRNA.
DR   EMBL; AK089616; BAC40933.1; -; mRNA.
DR   EMBL; BC090969; AAH90969.1; ALT_SEQ; mRNA.
DR   IPI; IPI00118376; -.
DR   PIR; T14318; T14318.
DR   UniGene; Mm.389330; -.
DR   ProteinModelPortal; O70481; -.
DR   SMR; O70481; 97-167, 222-302.
DR   IntAct; O70481; 1.
DR   STRING; O70481; -.
DR   PhosphoSite; O70481; -.
DR   PRIDE; O70481; -.
DR   Ensembl; ENSMUST00000028728; ENSMUSP00000028728; ENSMUSG00000027272.
DR   MGI; MGI:1277977; Ubr1.
DR   HOGENOM; HBG356075; -.
DR   HOVERGEN; HBG080426; -.
DR   InParanoid; O70481; -.
DR   OrthoDB; EOG41G338; -.
DR   PhylomeDB; O70481; -.
DR   ArrayExpress; O70481; -.
DR   Bgee; O70481; -.
DR   Genevestigator; O70481; -.
DR   GermOnline; ENSMUSG00000027272; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0000502; C:proteasome complex; IGI:MGI.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IGI:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:MGI.
DR   InterPro; IPR003769; ClpS_core.
DR   InterPro; IPR014719; Ribosomal_L7/12_C/ClpS-like.
DR   InterPro; IPR003126; Znf_N-recognin.
DR   InterPro; IPR013993; Znf_N-recognin_met.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.1390.10; Ribosomal_L7/12_C/ClpS-like; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF02617; ClpS; 1.
DR   Pfam; PF02207; zf-UBR; 1.
DR   SMART; SM00396; ZnF_UBR1; 1.
DR   SUPFAM; SSF54736; Ribosomal_L7/12_C/ClpS-like; 1.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; FALSE_NEG.
DR   PROSITE; PS51157; ZF_UBR; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Ligase; Metal-binding; Phosphoprotein;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1   1757       E3 ubiquitin-protein ligase UBR1.
FT                                /FTId=PRO_0000056137.
FT   ZN_FING      97    168       UBR-type.
FT   ZN_FING    1101   1204       RING-type; atypical.
FT   COMPBIAS    864    869       Poly-Pro.
FT   MOD_RES    1182   1182       Phosphoserine (By similarity).
FT   CONFLICT    639    639       S -> G (in Ref. 3; AAH90969).
SQ   SEQUENCE   1757 AA;  200217 MW;  689FC06148258BEF CRC64;
     MADEEMDGAE RMDVSPEPPL APQRPASWWD QQVDFYTAFL HHLAQLVPEI YFAEMDPDLE
     KQEESVQMSI LTPLEWYLFG EDPDICLEKL KHSGAFQLCG KVFKSGETTY SCRDCAIDPT
     CVLCMDCFQS SVHKNHRYKM HTSTGGGFCD CGDTEAWKTG PFCVDHEPGR AGTTKESLHC
     PLNEEVIAQA RRIFPSVIKY IVEMTIWEEE KELPPELQIR EKNERYYCVL FNDEHHSYDH
     VIYSLQRALD CELAEAQLHT TAIDKEGRRA VKAGVYATCQ EAKEDIKSHS ENVSQHPLHV
     EVLHSVVMAH QKFALRLGSW MNKIMSYSSD FRQIFCQACL VEEPGSENPC LISRLMLWDA
     KLYKGARKIL HELIFSSFFM EMEYKKLFAM EFVKYYKQLQ KEYISDDHER SISITALSVQ
     MLTVPTLARH LIEEQNVISV ITETLLEVLP EYLDRNNKFN FQGYSQDKLG RVYAVICDLK
     YILISKPVIW TERLRAQFLE GFRSFLKILT CMQGMEEIRR QVGQHIEVDP DWEAAIAIQM
     QLKNILLMFQ EWCACDEDLL LVAYKECHKA VMRCSTNFMS STKTVVQLCG HSLETKSYKV
     SEDLVSIHLP LSRTLAGLHV RLSRLGAISR LHEFVPFDSF QVEVLVEYPL RCLVLVAQVV
     AEMWRRNGLS LISQVFYYQD VKCREEMYDK DIIMLQIGAS IMDPNKFLLL VLQRYELTDA
     FNKTISTKDQ DLIKQYNTLI EEMLQVLIYI VGERYVPGVG NVTREEVIMR EITHLLCIEP
     MPHSAIARNL PENENNETGL ENVINKVATF KKPGVSGHGV YELKDESLKD FNMYFYHYSK
     TQHSKAEHMQ KKRRKQENKD EALPPPPPPE FCPAFSKVVN LLSCDVMIYI LRTIFERAVD
     TESNLWTEGM LQMAFHILAL GLLEEKQQLQ KAPEEEVAFD FYHKASRLGS SAMNAQNIQM
     LLERLKGIPQ LEGQKDMITW ILQMFDTVKR LREKSCLVVA TTSGLECIKS EEITHDKEKA
     ERKRKAEAAR LHRQKIMAQM SALQKNFIET HKLMYDNTSE VTGKEDSIME EESTSAVSEA
     SRIALGPKRG PAVTEKEVLT CILCQEEQEV KLENNAMVLS ACVQKSTALT QHRGKPVDHL
     GETLDPLFMD PDLAHGTYTG SCGHVMHAVC WQKYFEAVQL SSQQRIHVDL FDLESGEYLC
     PLCKSLCNTV IPIIPLQPQK INSENAEALA QLLTLARWIQ TVLARISGYN IKHAKGEAPA
     VPVLFNQGMG DSTFEFHSIL SFGVQSSVKY SNSIKEMVIL FATTIYRIGL KVPPDELDPR
     VPMMTWSTCA FTIQAIENLL GDEGKPLFGA LQNRQHSGLK ALMQFAVAQR ATCPQVLIHK
     HLARLLSVIL PNLQSENTPG LLSVDLFHVL VGAVLAFPSL YWDDTVDLQP SPLSSSYNHL
     YLFHLITMAH MLQILLTTDT DLSPGPPLAE GEEDSEEARC ASAFFVEVSQ HTDGLTGCGA
     PGWYLWLSLR NGITPYLRCA ALLFHYLLGV APPEELFANS AEGEFSALCS YLSLPTNLFL
     LFQEYWDTIR PLLQRWCGDP ALLKSLKQKS AVVRYPRKRN SLIELPEDYS CLLNQASHFR
     CPRSADDERK HPVLCLFCGA ILCSQNICCQ EIVNGEEVGA CVFHALHCGA GVCIFLKIRE
     CRVVLVEGKA RGCAYPAPYL DEYGETDPGL KRGNPLHLSR ERYRKLHLVW QQHCIIEEIA
     RSQETNQMLF GFNWQLL
//
ID   SNX12_MOUSE             Reviewed;         165 AA.
AC   O70493; Q9D0N3;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Sorting nexin-12;
DE   AltName: Full=SDP8 protein;
GN   Name=Snx12;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Xu Y., Wong S.H., Zhang T., Hong W.;
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: May be involved in several stages of intracellular
CC       trafficking (By similarity).
CC   -!- SIMILARITY: Belongs to the sorting nexin family.
CC   -!- SIMILARITY: Contains 1 PX (phox homology) domain.
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DR   EMBL; AF062484; AAC16019.1; -; mRNA.
DR   EMBL; AK011257; BAB27499.1; -; mRNA.
DR   IPI; IPI00762269; -.
DR   RefSeq; NP_061363.2; NM_018875.2.
DR   UniGene; Mm.206949; -.
DR   ProteinModelPortal; O70493; -.
DR   SMR; O70493; 28-158.
DR   PhosphoSite; O70493; -.
DR   REPRODUCTION-2DPAGE; O70493; -.
DR   PRIDE; O70493; -.
DR   Ensembl; ENSMUST00000077876; ENSMUSP00000077038; ENSMUSG00000046032.
DR   GeneID; 55988; -.
DR   KEGG; mmu:55988; -.
DR   UCSC; uc009twx.1; mouse.
DR   CTD; 55988; -.
DR   MGI; MGI:1919331; Snx12.
DR   eggNOG; roNOG15709; -.
DR   HOVERGEN; HBG055338; -.
DR   OrthoDB; EOG4C5CKP; -.
DR   PhylomeDB; O70493; -.
DR   ArrayExpress; O70493; -.
DR   Bgee; O70493; -.
DR   CleanEx; MM_SNX12; -.
DR   Genevestigator; O70493; -.
DR   GermOnline; ENSMUSG00000046032; Mus musculus.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001683; Phox.
DR   Gene3D; G3DSA:3.30.1520.10; PX; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; PX; 1.
DR   PROSITE; PS50195; PX; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1    165       Sorting nexin-12.
FT                                /FTId=PRO_0000213859.
FT   DOMAIN       28    151       PX.
FT   MOD_RES      23     23       Phosphotyrosine (By similarity).
FT   MOD_RES      73     73       Phosphoserine (By similarity).
FT   CONFLICT    101    101       H -> QL (in Ref. 2; BAB27499).
FT   CONFLICT    156    156       A -> P (in Ref. 2; BAB27499).
SQ   SEQUENCE   165 AA;  19116 MW;  AB80CFE513B0D08A CRC64;
     MSDTAVADTR RLNSKPQDLT DAYGPPSNFL EIDIFNPQTV GVGRARFTTY EVRMRTNLPI
     FKLKESCVRR RYSDFEWLKN ELERDSKIVV PPLPGKALKR HPFRGDEGIF EESFIEERRQ
     GLEQFINKIA GHPLAQNERC LHMFLQEEAI DRNYVAGKVL GEKDC
//
ID   CLCN7_MOUSE             Reviewed;         803 AA.
AC   O70496;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=H(+)/Cl(-) exchange transporter 7;
DE   AltName: Full=Chloride channel protein 7;
DE            Short=ClC-7;
GN   Name=Clcn7; Synonyms=Clc7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21124827; PubMed=11207362; DOI=10.1016/S0092-8674(01)00206-9;
RA   Kornak U., Kasper D., Boesl M.R., Kaiser E., Schweizer M., Schulz A.,
RA   Friedrich W., Delling G., Jentsch T.J.;
RT   "Loss of the ClC-7 chloride channel leads to osteopetrosis in mice and
RT   man.";
RL   Cell 104:205-215(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Mediates the exchange of chloride ions against protons.
CC       Functions as antiporter and contributes to the acidification of
CC       the lysosome lumen (By similarity).
CC   -!- INTERACTION:
CC       Q8BGT0:Ostm1; NbExp=2; IntAct=EBI-987482, EBI-987431;
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane
CC       protein (By similarity).
CC   -!- MISCELLANEOUS: The CLC channel family contains both chloride
CC       channels and proton-coupled anion transporters that exchange
CC       chloride or another anion for protons. The presence of conserved
CC       gating glutamate residues is typical for family members that
CC       function as antiporters (By similarity).
CC   -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family.
CC       ClC-7/CLCN7 subfamily.
CC   -!- SIMILARITY: Contains 2 CBS domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF063101; AAC18832.1; -; Genomic_DNA.
DR   EMBL; AF063098; AAC18832.1; JOINED; Genomic_DNA.
DR   EMBL; AF063099; AAC18832.1; JOINED; Genomic_DNA.
DR   EMBL; AF063100; AAC18832.1; JOINED; Genomic_DNA.
DR   EMBL; BC050907; AAH50907.1; -; mRNA.
DR   EMBL; BC053049; AAH53049.1; -; mRNA.
DR   EMBL; BC054799; AAH54799.1; -; mRNA.
DR   IPI; IPI00118440; -.
DR   RefSeq; NP_036060.1; NM_011930.3.
DR   UniGene; Mm.270587; -.
DR   ProteinModelPortal; O70496; -.
DR   SMR; O70496; 119-790.
DR   IntAct; O70496; 7.
DR   STRING; O70496; -.
DR   PhosphoSite; O70496; -.
DR   PRIDE; O70496; -.
DR   Ensembl; ENSMUST00000040729; ENSMUSP00000035964; ENSMUSG00000036636.
DR   GeneID; 26373; -.
DR   KEGG; mmu:26373; -.
DR   UCSC; uc008azv.1; mouse.
DR   CTD; 26373; -.
DR   MGI; MGI:1347048; Clcn7.
DR   eggNOG; roNOG07216; -.
DR   HOGENOM; HBG385491; -.
DR   HOVERGEN; HBG050985; -.
DR   InParanoid; O70496; -.
DR   OMA; RINHTAF; -.
DR   OrthoDB; EOG41C6VS; -.
DR   PhylomeDB; O70496; -.
DR   NextBio; 304273; -.
DR   ArrayExpress; O70496; -.
DR   Bgee; O70496; -.
DR   CleanEx; MM_CLCN7; -.
DR   Genevestigator; O70496; -.
DR   GermOnline; ENSMUSG00000036636; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
DR   InterPro; IPR014743; Cl-channel_core.
DR   InterPro; IPR001807; Cl-channel_volt-gated.
DR   InterPro; IPR002249; Cl_channel-7.
DR   InterPro; IPR000644; Cysta_beta_synth_core.
DR   InterPro; IPR006311; TAT_signal.
DR   Gene3D; G3DSA:1.10.3080.10; Cl-channel_core; 2.
DR   PANTHER; PTHR11689; Cl-channel_volt; 1.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF00654; Voltage_CLC; 1.
DR   PRINTS; PR00762; CLCHANNEL.
DR   PRINTS; PR01118; CLCHANNEL7.
DR   SMART; SM00116; CBS; 2.
DR   SUPFAM; SSF81340; Cl-channel_core; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   1: Evidence at protein level;
KW   Antiport; ATP-binding; CBS domain; Chloride; Ion transport; Lysosome;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    803       H(+)/Cl(-) exchange transporter 7.
FT                                /FTId=PRO_0000094453.
FT   TOPO_DOM      1    124       Cytoplasmic (By similarity).
FT   TRANSMEM    125    157       Helical; (By similarity).
FT   TRANSMEM    172    195       Helical; (By similarity).
FT   INTRAMEM    204    211       Helical; (By similarity).
FT   TRANSMEM    221    239       Helical; (By similarity).
FT   TRANSMEM    245    262       Helical; (By similarity).
FT   INTRAMEM    286    298       Helical; (By similarity).
FT   INTRAMEM    302    310       Helical; (By similarity).
FT   TRANSMEM    320    339       Helical; (By similarity).
FT   TRANSMEM    373    403       Helical; (By similarity).
FT   TRANSMEM    408    430       Helical; (By similarity).
FT   TRANSMEM    485    505       Helical; (By similarity).
FT   TRANSMEM    510    533       Helical; (By similarity).
FT   INTRAMEM    543    557       Helical; (By similarity).
FT   INTRAMEM    558    560       Note=Loop between two helices; (By
FT                                similarity).
FT   INTRAMEM    561    572       Helical; (By similarity).
FT   INTRAMEM    573    576       Note=Loop between two helices; (By
FT                                similarity).
FT   TRANSMEM    577    595       Helical; (By similarity).
FT   TOPO_DOM    596    803       Cytoplasmic (By similarity).
FT   DOMAIN      629    693       CBS 1.
FT   DOMAIN      739    797       CBS 2.
FT   NP_BIND     656    658       ATP (By similarity).
FT   NP_BIND     781    784       ATP (By similarity).
FT   MOTIF       201    205       Selectivity filter part_1 (By
FT                                similarity).
FT   MOTIF       243    247       Selectivity filter part_2 (By
FT                                similarity).
FT   MOTIF       510    514       Selectivity filter part_3 (By
FT                                similarity).
FT   BINDING     202    202       Chloride (By similarity).
FT   BINDING     512    512       Chloride; via amide nitrogen (By
FT                                similarity).
FT   BINDING     600    600       Chloride (By similarity).
FT   SITE        245    245       Mediates proton transfer from the outer
FT                                aqueous phase to the interior of the
FT                                protein; involved in linking H(+) and
FT                                Cl(-) transport (By similarity).
FT   SITE        312    312       Mediates proton transfer from the protein
FT                                to the inner aqueous phase (By
FT                                similarity).
FT   MOD_RES       9      9       Phosphoserine (By similarity).
SQ   SEQUENCE   803 AA;  88713 MW;  A7D6DA5791DAA48C CRC64;
     MANVSKKVSW SGRDRDDEEG APLLRRTGQP DEETPLLNGA GPGARQSHSA LFRIGQMNNV
     ELDDELLDPE VDPPHTFPKE IPHNEKLLSL KYESLDYDNS ENQLFLEEER RINHTAFRTV
     EIKRWVICAL IGILTGLVAC FIDIVVENLA GLKYRVIKDN IDKFTEKGGL SFSLLLWATL
     NSAFVLVGSV IVAFIEPVAA GSGIPQIKCF LNGVKIPHVV RLKTLVIKVS GVILSVVGGL
     AVGKEGPMIH SGSVIAAGIS QGRSTSLKRD FKIFEYFRRD TEKRDFVSAG AAAGVSAAFG
     APVGGVLFSL EEGASFWNQF LTWRIFFASM ISTFTLNFVL SIYHGNMWDL SSPGLINFGR
     FDSEKMAYTI HEIPVFIAMG VVGGILGAVF NALNYWLTMF RIRYIHRPCL QVIEAMLVAA
     VTATVAFVLI YSSRDCQPLQ GSSMSYPLQL FCADGEYNSM AAAFFNTPEK SVVSLFHDPP
     GSYNPMTLGL FTLVYFFLAC WTYGLTVSAG VFIPSLLIGA AWGRLFGISL SYLTGAAIWA
     DPGKYALMGA AAQLGGIVRM TLSLTVIMME ATSNVTYGFP IMLVLMTAKI VGDVFIEGLY
     DMHIQLQSVP FLHWEAPVTS HSLTAREVMS TPVTCLRRRE KVGIIVDVLS DTASNHNGFP
     VVEDVGDTQP ARLQGLILRS QLIVLLKHKV FVERSNMGLV QRRLRLKDFR DAYPRFPPIQ
     SIHVSQDERE CTMDLSEFMN PSPYTVPQEA SLPRVFKLFR ALGLRHLVVV DNHNQVVGLV
     TRKDLARYRL GKGGLEELSL AQT
//
ID   DHB12_MOUSE             Reviewed;         312 AA.
AC   O70503; Q3TID1; Q3U7V9; Q542N3; Q8CI39;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Estradiol 17-beta-dehydrogenase 12;
DE            EC=1.1.1.62;
DE   AltName: Full=17-beta-hydroxysteroid dehydrogenase 12;
DE            Short=17-beta-HSD 12;
DE   AltName: Full=3-ketoacyl-CoA reductase;
DE            Short=KAR;
DE            EC=1.3.1.-;
DE   AltName: Full=KIK-I;
GN   Name=Hsd17b12; Synonyms=Kik1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Liver;
RA   Gambotto A., Pagliano O., Robbins P., Deleo A.;
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c, C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Cerebellum, Colon, Head, Lung, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=12482854; DOI=10.1074/jbc.M211684200;
RA   Moon Y.-A., Horton J.D.;
RT   "Identification of two mammalian reductases involved in the two-carbon
RT   fatty acyl elongation cascade.";
RL   J. Biol. Chem. 278:7335-7343(2003).
CC   -!- FUNCTION: Catalyzes the transformation of estrone (E1) into
CC       estradiol (E2), suggesting a central role in estrogen formation.
CC       Its strong expression in ovary and mammary gland suggest that it
CC       may constitute the major enzyme responsible for the conversion of
CC       E1 to E2 in females. Also has 3-ketoacyl-CoA reductase activity,
CC       reducing both long chain 3-ketoacyl-CoAs and long chain fatty
CC       acyl-CoAs, suggesting a role in long fatty acid elongation (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Estradiol-17-beta + NAD(P)(+) = estrone +
CC       NAD(P)H.
CC   -!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O70503-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O70503-2; Sequence=VSP_020255;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in most tissues tested.
CC   -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum
CC       localization for type I membrane proteins (By similarity).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family. 17-beta-HSD 3 subfamily.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF064635; AAC16885.1; -; mRNA.
DR   EMBL; AK078841; BAC37418.1; -; mRNA.
DR   EMBL; AK081869; BAC38354.1; -; mRNA.
DR   EMBL; AK082715; BAC38583.1; -; mRNA.
DR   EMBL; AK088521; BAC40401.1; -; mRNA.
DR   EMBL; AK150849; BAE29906.1; -; mRNA.
DR   EMBL; AK152489; BAE31260.1; -; mRNA.
DR   EMBL; AK166027; BAE38530.1; -; mRNA.
DR   EMBL; AK167908; BAE39915.1; -; mRNA.
DR   EMBL; BC037620; AAH37620.1; -; mRNA.
DR   IPI; IPI00119219; -.
DR   IPI; IPI00785470; -.
DR   RefSeq; NP_062631.1; NM_019657.4.
DR   UniGene; Mm.480343; -.
DR   ProteinModelPortal; O70503; -.
DR   SMR; O70503; 49-261.
DR   STRING; O70503; -.
DR   PhosphoSite; O70503; -.
DR   PRIDE; O70503; -.
DR   Ensembl; ENSMUST00000028619; ENSMUSP00000028619; ENSMUSG00000027195.
DR   GeneID; 56348; -.
DR   KEGG; mmu:56348; -.
DR   UCSC; uc008lgp.1; mouse.
DR   CTD; 56348; -.
DR   MGI; MGI:1926967; Hsd17b12.
DR   eggNOG; roNOG06538; -.
DR   HOGENOM; HBG713750; -.
DR   HOVERGEN; HBG005478; -.
DR   InParanoid; O70503; -.
DR   OMA; YPEYFLD; -.
DR   OrthoDB; EOG4HMJB0; -.
DR   PhylomeDB; O70503; -.
DR   BRENDA; 1.1.1.62; 244.
DR   NextBio; 312340; -.
DR   ArrayExpress; O70503; -.
DR   Bgee; O70503; -.
DR   CleanEx; MM_HSD17B12; -.
DR   Genevestigator; O70503; -.
DR   GermOnline; ENSMUSG00000027195; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005518; F:collagen binding; IDA:MGI.
DR   GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; IEA:EC.
DR   GO; GO:0001968; F:fibronectin binding; IDA:MGI.
DR   GO; GO:0008201; F:heparin binding; IDA:MGI.
DR   GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Endoplasmic reticulum; Lipid synthesis;
KW   Membrane; NADP; Oxidoreductase; Steroid biosynthesis; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    312       Estradiol 17-beta-dehydrogenase 12.
FT                                /FTId=PRO_0000054576.
FT   TRANSMEM      4     24       Helical; (Potential).
FT   TRANSMEM    182    202       Helical; (Potential).
FT   TRANSMEM    269    285       Helical; (Potential).
FT   NP_BIND      50     79       NADP (By similarity).
FT   MOTIF       308    312       Di-lysine motif (By similarity).
FT   ACT_SITE    202    202       Proton acceptor (By similarity).
FT   BINDING     189    189       Substrate (By similarity).
FT   VAR_SEQ       1    135       Missing (in isoform 2).
FT                                /FTId=VSP_020255.
FT   CONFLICT      2      2       E -> V (in Ref. 2; BAE39915).
FT   CONFLICT    256    256       V -> M (in Ref. 2; BAE29906/BAE31260).
SQ   SEQUENCE   312 AA;  34742 MW;  7D255188FA1F8DDB CRC64;
     MECAPPAAGF LYWVGASTIA YLALRASYSL FRAFQVWCVG NEALVGPRLG EWAVVTGGTD
     GIGKAYAEEL AKRGMKIVLI SRSQDKLNQV SNNIKEKFNV ETRTIAVDFS LDDIYDKIKT
     GLSGLEIGVL VNNVGMSYEY PEYFLEIPDL DNTIKKLINI NVLSVCKVTR LVLPGMVERS
     KGVILNISSA SGMLPVPLLT IYSATKAFVD FFSQCLHEEY KSKGIFVQSV MPYLVATKLA
     KIQKPTLDKP SAETFVKSAI KTVGLQTRTT GYVIHSLMGS INSIMPRWMY FKIIMGFSKS
     LRNRYLKKRK KN
//
ID   SRPK1_MOUSE             Reviewed;         648 AA.
AC   O70551; O70193; Q99JT3;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Serine/threonine-protein kinase SRPK1;
DE            EC=2.7.11.1;
DE   AltName: Full=SFRS protein kinase 1;
DE   AltName: Full=Serine/arginine-rich protein-specific kinase 1;
DE            Short=SR-protein-specific kinase 1;
GN   Name=Srpk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=98113357; PubMed=9446799; DOI=10.1006/bbrc.1997.7913;
RA   Kuroyanagi N., Onogi H., Wakabayashi T., Hagiwara M.;
RT   "Novel SR-protein-specific kinase, SRPK2, disassembles nuclear
RT   speckles.";
RL   Biochem. Biophys. Res. Commun. 242:357-364(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Embryo;
RX   MEDLINE=99380486; PubMed=10390541; DOI=10.1093/nar/27.14.2972;
RA   Papoutsopoulou S., Nikolakaki E., Chalepakis G., Kruft V.,
RA   Chevaillier P., Giannakouros T.;
RT   "SR protein-specific kinase 1 is highly expressed in testis and
RT   phosphorylates protamine 1.";
RL   Nucleic Acids Res. 27:2972-2980(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 573-581, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-448 AND SER-450, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-448 AND SER-450, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309; SER-311; THR-448
RP   AND SER-450, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Plays a central role in the regulatory network for
CC       splicing, controlling the intranuclear distribution of splicing
CC       factors in interphase cells and the reorganization of nuclear
CC       speckles during mitosis. Hyperphosphorylates RS domain-containing
CC       proteins such as SFRS1, SFRS2 and ZRSR2 on serine residues during
CC       metaphase but at lower levels during interphase. Locks onto SFRS1
CC       to form a stable complex and processively phosphorylates the RS
CC       domain.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: Activated by phosphorylation on Ser-51 and Ser-
CC       548 (By similarity).
CC   -!- SUBUNIT: Present in a seven component complex, the toposome, which
CC       separates entangled circular chromatin DNA during chromosome
CC       segregation (By similarity).
CC   -!- INTERACTION:
CC       Q07955:SFRS1 (xeno); NbExp=4; IntAct=EBI-593343, EBI-398920;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in the testis but is
CC       also present at lower levels in heart, spleen, liver, brain,
CC       kidney, lung and skeletal muscle. Present in all germinal cells in
CC       the seminiferous tubules but not in mature spermatozoa.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AB012290; BAA25299.1; -; mRNA.
DR   EMBL; AJ224115; CAA11833.1; -; mRNA.
DR   EMBL; BC005707; AAH05707.1; -; mRNA.
DR   EMBL; BC050761; AAH50761.1; -; mRNA.
DR   IPI; IPI00387234; -.
DR   PIR; JC5930; JC5930.
DR   RefSeq; NP_058075.2; NM_016795.3.
DR   UniGene; Mm.15252; -.
DR   UniGene; Mm.479188; -.
DR   ProteinModelPortal; O70551; -.
DR   SMR; O70551; 63-648.
DR   IntAct; O70551; 5.
DR   STRING; O70551; -.
DR   PhosphoSite; O70551; -.
DR   PRIDE; O70551; -.
DR   Ensembl; ENSMUST00000004987; ENSMUSP00000004987; ENSMUSG00000004865.
DR   GeneID; 20815; -.
DR   KEGG; mmu:20815; -.
DR   UCSC; uc008bri.1; mouse.
DR   CTD; 20815; -.
DR   MGI; MGI:106908; Srpk1.
DR   eggNOG; roNOG04128; -.
DR   GeneTree; ENSGT00530000063566; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108512; -.
DR   InParanoid; O70551; -.
DR   OMA; HISQLQE; -.
DR   PhylomeDB; O70551; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 299541; -.
DR   ArrayExpress; O70551; -.
DR   Bgee; O70551; -.
DR   CleanEx; MM_SRPK1; -.
DR   Genevestigator; O70551; -.
DR   GermOnline; ENSMUSG00000004865; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR   GO; GO:0007243; P:intracellular protein kinase cascade; IDA:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0050684; P:regulation of mRNA processing; IDA:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   Pfam; PF00069; Pkinase; 2.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Chromosome partition; Cytoplasm;
KW   Differentiation; Direct protein sequencing; Kinase; mRNA processing;
KW   mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    648       Serine/threonine-protein kinase SRPK1.
FT                                /FTId=PRO_0000086675.
FT   DOMAIN       80    646       Protein kinase.
FT   NP_BIND      86     94       ATP (By similarity).
FT   ACT_SITE    213    213       Proton acceptor (By similarity).
FT   BINDING     109    109       ATP (By similarity).
FT   MOD_RES      37     37       Phosphoserine (By similarity).
FT   MOD_RES      51     51       Phosphoserine.
FT   MOD_RES     309    309       Phosphoserine.
FT   MOD_RES     311    311       Phosphoserine.
FT   MOD_RES     448    448       Phosphothreonine.
FT   MOD_RES     450    450       Phosphoserine.
FT   MOD_RES     548    548       Phosphoserine; by CK2 (By similarity).
FT   MOD_RES     578    578       N6-acetyllysine (By similarity).
FT   CONFLICT    113    113       S -> I (in Ref. 2; CAA11833).
FT   CONFLICT    155    155       G -> V (in Ref. 2; CAA11833).
FT   CONFLICT    256    256       Q -> T (in Ref. 2; CAA11833).
FT   CONFLICT    279    279       A -> P (in Ref. 1; BAA25299).
SQ   SEQUENCE   648 AA;  73088 MW;  CB779C163A11ECEB CRC64;
     MERKVLALQA RKKRTKAKKD KAQRKPETQH RGSAPHSESD IPEQEEEILG SDDDEQEDPN
     DYCKGGYHLV KIGDLFNGRY HVIRKLGWGH FSTVWLSWDI QGKKFVAMKV VKSAEHYTET
     ALDEIRLLKS VRNSDPNDPN GEMVVQLLDD FKISGVNGTH ICMVFEVLGH HLLKWIIKSN
     YQGLPLPCVK KIIQQVLQGL DYLHTKCRII HTDIKPENIL LSVNEQYIRR LAAEATEWQR
     SGAPPPSGSA VSTAPQPKPA DKMSKNKKKK LKKKQKRQAE LLEKRMQEIE EMEKESGPGQ
     KRPNKQEESE SPVDRPLTEN PPNKMTQEKL EESNSIGQDQ TLTERGGEGG APEINCNGVI
     GVVNYPENSN NETLRHKEDL HNANDCDVHT LKQEPSFLNS SNGDSSPSQD TDSCTPTASE
     TMVCQSSAEQ SLTRQDITQL EESIRADTPS GDEQEPNGAL DSKGKFSAGN FLINPLEPKN
     AEKLQVKIAD LGNACWVHKH FTEDIQTRQY RSLEVLIGSG YNTPADIWST ACMAFELATG
     DYLFEPHSGE DYTRDEDHIA LIIELLGKVP RKLIVAGKYS KEFFTKKGDL KHITKLKPWG
     LLEVLVEKYE WPQEEAAGFT DFLLPMLELM PEKRATAAEC LRHPWLNS
//
ID   DTNB_MOUSE              Reviewed;         700 AA.
AC   O70585; O70563; Q9CTZ1;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Dystrobrevin beta;
DE            Short=DTN-B;
DE            Short=mDTN-B;
DE   AltName: Full=Beta-dystrobrevin;
GN   Name=Dtnb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=98200066; PubMed=9540997; DOI=10.1016/S0014-5793(98)00097-0;
RA   Puca A.A., Piluso V.N.G., Belsito A., Sampaolo S., Quaderi N.,
RA   Rossi E., Di Iorio G., Ballabio A., Franco B.;
RT   "Identification and characterization of a novel member of the
RT   dystrobrevin gene family.";
RL   FEBS Lett. 425:7-13(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   MEDLINE=98081858; PubMed=9419360; DOI=10.1073/pnas.95.1.241;
RA   Blake D.J., Nawrotzki R., Loh N.Y., Gorecki D.C., Davies K.E.;
RT   "Beta-dystrobrevin, a member of the dystrophin-related protein
RT   family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:241-246(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
RX   MEDLINE=99018217; PubMed=9799833; DOI=10.1007/s003359900883;
RA   Loh N.Y., Ambrose H.J., Guay-Woodford L.M., Dasgupta S.,
RA   Nawrotzki R.A., Blake D.J., Davies K.E.;
RT   "Genomic organization and refined mapping of the mouse beta-
RT   dystrobrevin gene.";
RL   Mamm. Genome 9:857-862(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 590-608 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   INTERACTION WITH DYSTROBREVIN BINDING PROTEIN 1.
RX   MEDLINE=21316514; PubMed=11316798; DOI=10.1074/jbc.M010418200;
RA   Benson M.A., Newey S.E., Martin-Rendon E., Hawkes R., Blake D.J.;
RT   "Dysbindin, a novel coiled-coil-containing protein that interacts with
RT   the dystrobrevins in muscle and brain.";
RL   J. Biol. Chem. 276:24232-24241(2001).
CC   -!- SUBUNIT: Interacts with dystrophin short form DP71 and syntrophins
CC       SNTG1 and SNTG2 (By similarity). Binds dystrobrevin binding
CC       protein 1.
CC   -!- INTERACTION:
CC       P11532:DMD (xeno); NbExp=1; IntAct=EBI-349714, EBI-295827;
CC       Q91WZ8:Dtnbp1; NbExp=1; IntAct=EBI-349714, EBI-643186;
CC       Q91WZ8-1:Dtnbp1; NbExp=2; IntAct=EBI-349714, EBI-643199;
CC       P33175:Kif5a; NbExp=2; IntAct=EBI-349714, EBI-349710;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1;
CC         IsoId=O70585-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O70585-2; Sequence=VSP_004227, VSP_004228, VSP_004229;
CC   -!- TISSUE SPECIFICITY: Expressed mainly in brain, kidney, liver and
CC       lung. In brain expressed in neurons of the cortex and hippocampus.
CC   -!- DOMAIN: The coiled coil domain may mediate the interaction with
CC       dystrophin.
CC   -!- SIMILARITY: Belongs to the dystrophin family. Dystrobrevin
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 ZZ-type zinc finger.
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DR   EMBL; Y15742; CAA75752.1; -; mRNA.
DR   EMBL; AJ003007; CAA05796.1; -; mRNA.
DR   EMBL; AJ010204; CAA09038.1; -; Genomic_DNA.
DR   EMBL; AJ010205; CAA09038.1; JOINED; Genomic_DNA.
DR   EMBL; AJ010206; CAA09038.1; JOINED; Genomic_DNA.
DR   EMBL; AJ010207; CAA09038.1; JOINED; Genomic_DNA.
DR   EMBL; AJ010208; CAA09038.1; JOINED; Genomic_DNA.
DR   EMBL; AJ010209; CAA09038.1; JOINED; Genomic_DNA.
DR   EMBL; AJ010210; CAA09038.1; JOINED; Genomic_DNA.
DR   EMBL; AJ010211; CAA09038.1; JOINED; Genomic_DNA.
DR   EMBL; AJ010212; CAA09038.1; JOINED; Genomic_DNA.
DR   EMBL; AJ010213; CAA09038.1; JOINED; Genomic_DNA.
DR   EMBL; AJ010214; CAA09038.1; JOINED; Genomic_DNA.
DR   EMBL; AJ010215; CAA09038.1; JOINED; Genomic_DNA.
DR   EMBL; AJ010216; CAA09038.1; JOINED; Genomic_DNA.
DR   EMBL; AJ010217; CAA09038.1; JOINED; Genomic_DNA.
DR   EMBL; AJ010218; CAA09038.1; JOINED; Genomic_DNA.
DR   EMBL; AJ010219; CAA09038.1; JOINED; Genomic_DNA.
DR   EMBL; AJ010220; CAA09038.1; JOINED; Genomic_DNA.
DR   EMBL; AJ010221; CAA09038.1; JOINED; Genomic_DNA.
DR   EMBL; AK019068; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00119500; -.
DR   IPI; IPI00469658; -.
DR   UniGene; Mm.286202; -.
DR   ProteinModelPortal; O70585; -.
DR   SMR; O70585; 7-292.
DR   IntAct; O70585; 11.
DR   MINT; MINT-197260; -.
DR   STRING; O70585; -.
DR   PhosphoSite; O70585; -.
DR   PRIDE; O70585; -.
DR   Ensembl; ENSMUST00000077930; ENSMUSP00000077085; ENSMUSG00000071454.
DR   Ensembl; ENSMUST00000101637; ENSMUSP00000099161; ENSMUSG00000071454.
DR   UCSC; uc007mww.1; mouse.
DR   MGI; MGI:1203728; Dtnb.
DR   eggNOG; roNOG13280; -.
DR   HOGENOM; HBG378857; -.
DR   HOVERGEN; HBG005539; -.
DR   InParanoid; O70585; -.
DR   OrthoDB; EOG40GCQ7; -.
DR   NextBio; 284118; -.
DR   ArrayExpress; O70585; -.
DR   Bgee; O70585; -.
DR   CleanEx; MM_DTNB; -.
DR   Genevestigator; O70585; -.
DR   GermOnline; ENSMUSG00000071454; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR017432; Distrobrevin.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR015153; EF-hand_dom_typ1.
DR   InterPro; IPR015154; EF-hand_dom_typ2.
DR   InterPro; IPR000433; Znf_ZZ.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF09068; efhand_1; 1.
DR   Pfam; PF09069; efhand_2; 1.
DR   Pfam; PF00569; ZZ; 1.
DR   PIRSF; PIRSF038204; Distrobrevin; 1.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Metal-binding; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    700       Dystrobrevin beta.
FT                                /FTId=PRO_0000086879.
FT   ZN_FING     237    284       ZZ-type.
FT   REGION      369    418       Syntrophin-binding region.
FT   COILED      428    521       Potential.
FT   VAR_SEQ     518    518       K -> KEEEQKQA (in isoform 2).
FT                                /FTId=VSP_004227.
FT   VAR_SEQ     603    608       AEAEEQ -> EVTPVS (in isoform 2).
FT                                /FTId=VSP_004228.
FT   VAR_SEQ     609    700       Missing (in isoform 2).
FT                                /FTId=VSP_004229.
FT   CONFLICT    412    412       P -> L (in Ref. 2 and 3).
FT   CONFLICT    465    465       S -> F (in Ref. 2 and 3).
SQ   SEQUENCE   700 AA;  78356 MW;  6BE34EE861AFE46C CRC64;
     MIEEGGNKRK TMAEKRQLFI EMRAQNFDVI RLSTYRTACK LRFVQKRCNL HLVDIWNMIE
     AFRDNGLNTL DHSTEISVSR LETVISSIYY QLNKRLPSTH QISVEQSISL LLNFMVAAYD
     SEGRGKLTVF SVKAMLATMC GGKMLDKLRY IFSQMSDSNG LMMFGKLDQF LKEALKLPTA
     VFEGPSFGYT EHAVRTCFPQ QKKIMLNMFL DTMMADPPPQ CLVWLPLMHR LAHVENVFHP
     VECSYCHCES MMGFRYRCQQ CHNYQLCQNC FWRGHASGAH SNQHQMKEHS SWKSPAKKLS
     HAISKSLGCV PSREPPHPVF PEQPEKPLDL AHLVPPRPLT NMNDTVVSHM SSGVPTPTKR
     LQYSQDMPNL LADEHALIAS YVARLQHCTR VLDSPSRLDE EHRLIARYAA RPAAEAGNMT
     RPPTDASFNF DANKQQRQLI AELENKNREI LQEIQRLRLE HEQASQPTPE KAQQNPMLLA
     ELRLLRQRKD ELEQRMSALQ ESRRELMVQL EGLMKLLKAQ ATGSPHTSPT HGGGRPMPMP
     VRSTSAGSTP THGPQDSLSG VGGDVQEAFA QGTRRNLRND LLVAADSITN TMSSLVKELH
     SGAEAEEQAG TEKTREGLPP EAHSCPSFCC TPGPSLQAAR LTQPPERGAK PMGSGEGLPE
     AAAGGPPACT SIRIPPSWHG LISASGIYQE MEKNRKALKK
//
ID   CSKP_MOUSE              Reviewed;         926 AA.
AC   O70589; A2ADP8; A2ADP9; A2ADQ4; O70588; Q3UW92;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   08-MAR-2011, entry version 112.
DE   RecName: Full=Peripheral plasma membrane protein CASK;
DE            EC=2.7.11.1;
DE   AltName: Full=Calcium/calmodulin-dependent serine protein kinase;
GN   Name=Cask;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Embryo;
RX   MEDLINE=99005531; PubMed=9787075; DOI=10.1006/geno.1998.5479;
RA   Laverty H.G., Wilson J.B.;
RT   "Murine CASK is disrupted in a sex-linked cleft palate mouse mutant.";
RL   Genomics 53:29-41(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 273-926 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Cecum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH TBR1.
RX   PubMed=10749215; DOI=10.1038/35005118;
RA   Hsueh Y.P., Wang T.F., Yang F.C., Sheng M.;
RT   "Nuclear translocation and transcription regulation by the membrane-
RT   associated guanylate kinase CASK/LIN-2.";
RL   Nature 404:298-302(2000).
RN   [5]
RP   INTERACTION WITH TSPYL2, AND IDENTIFICATION IN COMPLEX WITH TSPYL2 AND
RP   TBR1.
RC   STRAIN=C57BL/6;
RX   PubMed=15066269; DOI=10.1016/S0896-6273(04)00139-4;
RA   Wang G.-S., Hong C.-J., Yen T.-Y., Huang H.-Y., Ou Y., Huang T.-N.,
RA   Jung W.-G., Kuo T.-Y., Sheng M., Wang T.-F., Hsueh Y.-P.;
RT   "Transcriptional modification by a CASK-interacting nucleosome
RT   assembly protein.";
RL   Neuron 42:113-128(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-571, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   STRUCTURE BY NMR OF 405-454, AND INTERACTION WITH LIN7B.
RX   PubMed=15863617; DOI=10.1073/pnas.0409346102;
RA   Feng W., Long J.-F., Zhang M.;
RT   "A unified assembly mode revealed by the structures of tetrameric L27
RT   domain complexes formed by mLin-2/mLin-7 and Patj/Pals1 scaffold
RT   proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:6861-6866(2005).
CC   -!- FUNCTION: Multidomain scaffolding protein with a role in synaptic
CC       transmembrane protein anchoring and ion channel trafficking.
CC       Contributes to neural development and regulation of gene
CC       expression via interaction with the transcription factor TRB1.
CC       Binds to cell-surface proteins, including amyloid precursor
CC       protein, neurexins, and syndecans. May mediate a link between the
CC       extracellular matrix and the actin cytoskeleton via its
CC       interaction with syndecan and with the actin/spectrin-binding
CC       protein 4.1.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Unlike other protein kinases, does not require a
CC       divalent cation such as magnesium for catalytic activity (By
CC       similarity).
CC   -!- ENZYME REGULATION: Differs from archetypal CaMK members in that
CC       the kinase domain exhibits a constitutively active conformation
CC       and the autoinhibitory region does not engage in direct contact
CC       with the ATP-binding cleft, although it still binds Ca(2+)/CAM (By
CC       similarity).
CC   -!- SUBUNIT: Binds WHRN and NRXN1 cytosolic tail. Interacts with
CC       CASKIN1, APBA1, LIN7(A/B/C), and L27 domain of DLG1 and isoform 2
CC       of DLG4 (By similarity). CASK and LIN7 form two mutually exclusive
CC       tripartite complexes with APBA1 or CASKIN1. Interacts with FCHSD2
CC       (By similarity). Interacts with KIRREL3 (By similarity). Forms a
CC       complex with ACTN4, IQGAP1, MAGI2, NPHS1, SPTAN1 and SPTBN1 (By
CC       similarity). Interacts with TSPYL2. Part of a complex containing
CC       CASK, TRB1 and TSPYL2.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity). Cell membrane; Peripheral membrane protein (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1; Synonyms=CASK-B;
CC         IsoId=O70589-1; Sequence=Displayed;
CC       Name=2; Synonyms=CASK-A;
CC         IsoId=O70589-2; Sequence=VSP_003152, VSP_003153;
CC       Name=3;
CC         IsoId=O70589-3; Sequence=VSP_024614, VSP_024615;
CC       Name=4;
CC         IsoId=O70589-4; Sequence=VSP_024614, VSP_024616;
CC       Name=5;
CC         IsoId=O70589-5; Sequence=VSP_024614;
CC   -!- DOMAIN: The first L27 domain binds DLG1 and the second L27 domain
CC       probably binds LIN7 (By similarity).
CC   -!- DOMAIN: The protein kinase domain mediates the interaction with
CC       FCHSD2 (By similarity).
CC   -!- SIMILARITY: In the N-terminal section; belongs to the protein
CC       kinase superfamily. CAMK Ser/Thr protein kinase family. CaMK
CC       subfamily.
CC   -!- SIMILARITY: Belongs to the MAGUK family.
CC   -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC   -!- SIMILARITY: Contains 2 L27 domains.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; Y17138; CAA76647.1; -; mRNA.
DR   EMBL; Y17137; CAA76646.1; -; mRNA.
DR   EMBL; AL671117; CAM19440.1; -; Genomic_DNA.
DR   EMBL; AL672204; CAM19440.1; JOINED; Genomic_DNA.
DR   EMBL; BX005215; CAM19440.1; JOINED; Genomic_DNA.
DR   EMBL; AL671117; CAM19441.1; -; Genomic_DNA.
DR   EMBL; AL672204; CAM19441.1; JOINED; Genomic_DNA.
DR   EMBL; BX005215; CAM19441.1; JOINED; Genomic_DNA.
DR   EMBL; AL671117; CAM19446.1; -; Genomic_DNA.
DR   EMBL; AL672204; CAM19446.1; JOINED; Genomic_DNA.
DR   EMBL; AL672204; CAM20906.1; -; Genomic_DNA.
DR   EMBL; AL671117; CAM20906.1; JOINED; Genomic_DNA.
DR   EMBL; BX005215; CAM20906.1; JOINED; Genomic_DNA.
DR   EMBL; AL672204; CAM20907.1; -; Genomic_DNA.
DR   EMBL; BX005215; CAM20907.1; JOINED; Genomic_DNA.
DR   EMBL; AL671117; CAM20907.1; JOINED; Genomic_DNA.
DR   EMBL; AL672204; CAM20909.1; -; Genomic_DNA.
DR   EMBL; AL671117; CAM20909.1; JOINED; Genomic_DNA.
DR   EMBL; BX005215; CAM19528.1; -; Genomic_DNA.
DR   EMBL; AL672204; CAM19528.1; JOINED; Genomic_DNA.
DR   EMBL; AL671117; CAM19528.1; JOINED; Genomic_DNA.
DR   EMBL; BX005215; CAM19529.1; -; Genomic_DNA.
DR   EMBL; AL672204; CAM19529.1; JOINED; Genomic_DNA.
DR   EMBL; AL671117; CAM19529.1; JOINED; Genomic_DNA.
DR   EMBL; AK136523; BAE23024.1; -; mRNA.
DR   IPI; IPI00119517; -.
DR   IPI; IPI00227910; -.
DR   IPI; IPI00776307; -.
DR   IPI; IPI00776341; -.
DR   IPI; IPI00844763; -.
DR   RefSeq; NP_033936.2; NM_009806.2.
DR   UniGene; Mm.327591; -.
DR   UniGene; Mm.474948; -.
DR   PDB; 1Y74; NMR; -; B/D=405-454.
DR   PDBsum; 1Y74; -.
DR   ProteinModelPortal; O70589; -.
DR   SMR; O70589; 5-324, 339-459, 487-572, 615-923.
DR   STRING; O70589; -.
DR   PhosphoSite; O70589; -.
DR   PRIDE; O70589; -.
DR   Ensembl; ENSMUST00000033321; ENSMUSP00000033321; ENSMUSG00000031012.
DR   Ensembl; ENSMUST00000115431; ENSMUSP00000111091; ENSMUSG00000031012.
DR   Ensembl; ENSMUST00000115438; ENSMUSP00000111098; ENSMUSG00000031012.
DR   Ensembl; ENSMUST00000115440; ENSMUSP00000111100; ENSMUSG00000031012.
DR   Ensembl; ENSMUST00000116623; ENSMUSP00000112322; ENSMUSG00000031012.
DR   GeneID; 12361; -.
DR   KEGG; mmu:12361; -.
DR   UCSC; uc009srp.1; mouse.
DR   CTD; 12361; -.
DR   MGI; MGI:1309489; Cask.
DR   eggNOG; roNOG12976; -.
DR   GeneTree; ENSGT00560000077048; -.
DR   HOGENOM; HBG446173; -.
DR   HOVERGEN; HBG001858; -.
DR   InParanoid; O70589; -.
DR   OMA; AIELVCT; -.
DR   OrthoDB; EOG4FBHS6; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 281028; -.
DR   ArrayExpress; O70589; -.
DR   Bgee; O70589; -.
DR   Genevestigator; O70589; -.
DR   GermOnline; ENSMUSG00000031012; Mus musculus.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR004172; L27.
DR   InterPro; IPR014775; L27_C.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF02828; L27; 2.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00569; L27; 2.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS51022; L27; 2.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Calmodulin-binding;
KW   Cell membrane; Cytoplasm; Kinase; Membrane; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Repeat; Serine/threonine-protein kinase;
KW   SH3 domain; Transferase.
FT   CHAIN         1    926       Peripheral plasma membrane protein CASK.
FT                                /FTId=PRO_0000094569.
FT   DOMAIN       12    276       Protein kinase.
FT   DOMAIN      343    398       L27 1.
FT   DOMAIN      402    455       L27 2.
FT   DOMAIN      490    571       PDZ.
FT   DOMAIN      612    682       SH3.
FT   DOMAIN      739    911       Guanylate kinase-like.
FT   NP_BIND      18     26       ATP (By similarity).
FT   REGION      305    315       Calmodulin-binding.
FT   ACT_SITE    141    141       By similarity.
FT   BINDING      41     41       ATP (By similarity).
FT   MOD_RES     151    151       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     155    155       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     571    571       Phosphotyrosine.
FT   VAR_SEQ     340    345       Missing (in isoform 3, isoform 4 and
FT                                isoform 5).
FT                                /FTId=VSP_024614.
FT   VAR_SEQ     580    664       RDSPSTSRQSPANGHSSTNNSVSDLPSTTQPKGRQIYVRAQ
FT                                FEYDPAKDDLIPCKEAGIRFRVGDIIQIISKDDHNWWQGKL
FT                                ENS -> VISLTSLSYPNLPISSEFLTNFLLMAECFCFLGN
FT                                CFCCAVTTLHTNFTTKITEQKEVPPTSSALLACRYLQPFCS
FT                                KIKAKYRKLQ (in isoform 2).
FT                                /FTId=VSP_003152.
FT   VAR_SEQ     580    602       Missing (in isoform 3).
FT                                /FTId=VSP_024615.
FT   VAR_SEQ     603    614       Missing (in isoform 4).
FT                                /FTId=VSP_024616.
FT   VAR_SEQ     665    926       Missing (in isoform 2).
FT                                /FTId=VSP_003153.
FT   CONFLICT    298    298       F -> L (in Ref. 1; CAA76646/CAA76647).
FT   CONFLICT    666    666       N -> K (in Ref. 1; CAA76646/CAA76647).
FT   CONFLICT    677    679       LQE -> IQG (in Ref. 1; CAA76646/
FT                                CAA76647).
FT   CONFLICT    720    723       FDQL -> LII (in Ref. 1; CAA76646/
FT                                CAA76647).
FT   CONFLICT    742    742       L -> S (in Ref. 1; CAA76646/CAA76647).
FT   CONFLICT    769    769       Y -> C (in Ref. 1; CAA76646/CAA76647).
FT   CONFLICT    798    798       Q -> R (in Ref. 1; CAA76646/CAA76647).
FT   CONFLICT    816    816       Y -> F (in Ref. 1; CAA76646/CAA76647).
FT   CONFLICT    821    823       ETI -> DH (in Ref. 1; CAA76646/CAA76647).
FT   CONFLICT    851    851       A -> P (in Ref. 1; CAA76646/CAA76647).
FT   HELIX       406    417
FT   HELIX       423    433
FT   HELIX       435    452
SQ   SEQUENCE   926 AA;  105109 MW;  ADD2008CE53E0018 CRC64;
     MADDDVLFED VYELCEVIGK GPFSVVRRCI NRETGQQFAV KIVDVAKFTS SPGLSTEDLK
     REASICHMLK HPHIVELLET YSSDGMLYMV FEFMDGADLC FEIVKRADAG FVYSEAVASH
     YMRQILEALR YCHDNNIIHR DVKPHCVLLA SKENSAPVKL GGFGVAIQLG ESGLVAGGRV
     GTPHFMAPEV VKREPYGKPV DVWGCGVILF ILLSGCLPFY GTKERLFEGI IKGKYKMNPR
     QWSHISESAK DLVRRMLMLD PAERITVYEA LNHPWLKERD RYAYKIHLPE TVEQLRKFNA
     RRKLKGAVLA AVSSHKFNSF YGDPPEELPD FSEDPTSSGL LAAERAVSQV LDSLEEIHAL
     TDCSEKDLDF LHSVFQDQHL HTLLDLYDKI NTKSSPQIRN PPSDAVQRAK EVLEEISCYP
     ENNDAKELKR ILTQPHFMAL LQTHDVVAHE VYSDEALRVT PPPTSPYLNG DSPESANGDM
     DMENVTRVRL VQFQKNTDEP MGITLKMNEL NHCIVARIMH GGMIHRQGTL HVGDEIREIN
     GISVANQTVE QLQKMLREMR GSITFKIVPS YRTQSSSCER DSPSTSRQSP ANGHSSTNNS
     VSDLPSTTQP KGRQIYVRAQ FEYDPAKDDL IPCKEAGIRF RVGDIIQIIS KDDHNWWQGK
     LENSKNGTAG LIPSPELQEW RVACIAMEKT KQEQQASCTW FGKKKKQYKD KYLAKHNAVF
     DQLDLVTYEE VVKLPAFKRK TLVLLGAHGV GRRHIKNTLI TKHPDRFAYP IPHTTRPPKK
     DEENGKNYYF VSHDQMMQDI SNNEYLEYGS HEDAMYGTKL ETIRKIHEQG LIAILDVEPQ
     ALKVLRTAEF APFVVFIAAP TITPGLNEDE SLQRLQKESD VLQRTYAHYF DLTIINNEID
     ETIRHLEEAV ELVCTAPQWV PVSWVY
//
ID   RTN2_MOUSE              Reviewed;         471 AA.
AC   O70622; O70620;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Reticulon-2;
DE   AltName: Full=Neuroendocrine-specific protein-like 1;
DE            Short=NSP-like protein 1;
DE   AltName: Full=Neuroendocrine-specific protein-like I;
DE            Short=NSP-like protein I;
DE            Short=NSPLI;
GN   Name=Rtn2; Synonyms=Nspl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=129/Sv, and FVB/N; TISSUE=Cerebellum, and Skeletal muscle;
RX   MEDLINE=98191726; PubMed=9530622; DOI=10.1007/s003359900748;
RA   Geisler J.G., Stubbs L.J., Wasserman W.W., Mucenski M.L.;
RT   "Molecular cloning of a novel mouse gene with predominant muscle and
RT   neural expression.";
RL   Mamm. Genome 9:274-282(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       membrane protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Brain;
CC         IsoId=O70622-1; Sequence=Displayed;
CC       Name=2; Synonyms=Muscle;
CC         IsoId=O70622-2; Sequence=VSP_005650, VSP_005651;
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in neural and muscular
CC       tissues.
CC   -!- SIMILARITY: Contains 1 reticulon domain.
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DR   EMBL; AF038537; AAC14906.1; -; Genomic_DNA.
DR   EMBL; AF038537; AAC14907.1; -; Genomic_DNA.
DR   EMBL; AF038538; AAC14908.1; -; mRNA.
DR   EMBL; AF038539; AAC14909.1; -; mRNA.
DR   EMBL; AF093624; AAD13195.1; -; Genomic_DNA.
DR   EMBL; BC031370; AAH31370.1; -; mRNA.
DR   IPI; IPI00120427; -.
DR   IPI; IPI00229453; -.
DR   RefSeq; NP_001020535.1; NM_001025364.2.
DR   RefSeq; NP_038676.1; NM_013648.5.
DR   UniGene; Mm.24142; -.
DR   ProteinModelPortal; O70622; -.
DR   SMR; O70622; 322-381.
DR   STRING; O70622; -.
DR   PhosphoSite; O70622; -.
DR   PRIDE; O70622; -.
DR   Ensembl; ENSMUST00000032559; ENSMUSP00000032559; ENSMUSG00000030401.
DR   Ensembl; ENSMUST00000108468; ENSMUSP00000104108; ENSMUSG00000030401.
DR   GeneID; 20167; -.
DR   KEGG; mmu:20167; -.
DR   UCSC; uc009fli.1; mouse.
DR   CTD; 20167; -.
DR   MGI; MGI:107612; Rtn2.
DR   eggNOG; roNOG12524; -.
DR   HOGENOM; HBG126840; -.
DR   HOVERGEN; HBG099866; -.
DR   InParanoid; O70622; -.
DR   OMA; REPITGQ; -.
DR   OrthoDB; EOG4FJ88W; -.
DR   PhylomeDB; O70622; -.
DR   NextBio; 297679; -.
DR   ArrayExpress; O70622; -.
DR   Bgee; O70622; -.
DR   CleanEx; MM_RTN2; -.
DR   Genevestigator; O70622; -.
DR   GermOnline; ENSMUSG00000030401; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR003388; Reticulon.
DR   PANTHER; PTHR10994; Reticulon; 1.
DR   Pfam; PF02453; Reticulon; 1.
DR   PROSITE; PS50845; RETICULON; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    471       Reticulon-2.
FT                                /FTId=PRO_0000168162.
FT   TRANSMEM    295    315       Helical; (Potential).
FT   DOMAIN      272    471       Reticulon.
FT   MOD_RES      44     44       Phosphoserine.
FT   VAR_SEQ       1    267       Missing (in isoform 2).
FT                                /FTId=VSP_005650.
FT   VAR_SEQ     268    271       PLLL -> MGSK (in isoform 2).
FT                                /FTId=VSP_005651.
SQ   SEQUENCE   471 AA;  51347 MW;  9BBD8F372CF63AD3 CRC64;
     MGQVLPVFAH CKEAPSTASS TPDSTEGGND DSDFRELHTA REFSEDEEEE TTSQDWGTPR
     ELTFSYIAFD GVVGSGGRRD SVVRRPRPQG RSVSEPRDPP QQSGLGDSLE SIPSLSQSPE
     PGRRGDPDPV PPAERPLEEL RLRLDQLGWV VRSAGSGEDS ATSSSTPLEN EEPDGLEASE
     AGEETNLELR LAQSLHLQLE VLTPQLSPSS GTPQAHTPSP QRSQDSNSGP DDEPLLNVVE
     EHWRLLEQEP ITAQCLDSTD QSEFMLEPLL LVADLLYWKD TRTSGAVFTG LMASLLCLLH
     FSIVSVAAHL ALLGLCATIS LRVYRKVLQA VHRGDGTNPF QAYLDMDLTL TREQTERLSQ
     QIASHVVSTA TQLRHFFLVE DLVDSLKLAL LFYILTFVGA IFNGLTLVIL GVVALFTVPL
     LYRQHQAQID QYVGLVTNQL SHIKAKIRAK IPGTGTLAPT ASVSGSKAKA E
//
ID   TTC3_MOUSE              Reviewed;        1979 AA.
AC   O88196; Q05D15; Q3TMM9; Q3TPC8; Q3TPV5; Q3TQL0; Q3TSK0; Q3UFH5;
AC   Q5DTM5; Q6PG61; Q8BPM4; Q8C2N6;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 2.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=E3 ubiquitin-protein ligase TTC3;
DE            EC=6.3.2.-;
DE   AltName: Full=TPR repeat protein D;
DE            Short=Mtprd;
GN   Name=Ttc3; Synonyms=Kiaa4119;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=9603993;
RA   Tsukahara F., Urakawa I., Hattori M., Hirai M., Ohba K., Yoshioka T.,
RA   Sakaki Y., Muraki T.;
RT   "Molecular characterization of the mouse mtprd gene, a homologue of
RT   human TPRD: unique gene expression suggesting its critical role in the
RT   pathophysiology of Down syndrome.";
RL   J. Biochem. 123:1055-1063(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1194 AND 1423-1979
RP   (ISOFORMS 4 AND 5), AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF
RP   1116-1874 (ISOFORM 6).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Corpora quadrigemina, Eye, Heart, Lung, Pancreas, Spinal cord,
RC   Thymus, and Wolffian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1178 (ISOFORM 1).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1181 (ISOFORMS 2 AND 3).
RC   STRAIN=FVB/N-3, and NMRI; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that mediates the
CC       ubiquitination and subsequent degradation of phosphorylated Akt
CC       (AKT1, AKT2 and AKT3) in the nucleus. Acts as a terminal regulator
CC       of Akt signaling after activation; its phosphorylation by Akt,
CC       which is a prerequisite for ubiquitin ligase activity, suggests
CC       the existence of a regulation mechanism required to control Akt
CC       levels after activation. Catalyzes the formation of 'Lys-48'-
CC       polyubiquitin chains. May play a role in neuronal differentiation
CC       inhibition via its interaction with CIT (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts (when phosphorylated on Ser-378) with AKT1,
CC       AKT2 and AKT3 (when phosphorylated). Interacts with CIT (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=O88196-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O88196-2; Sequence=VSP_038776;
CC       Name=3;
CC         IsoId=O88196-3; Sequence=VSP_038775;
CC       Name=4;
CC         IsoId=O88196-4; Sequence=VSP_038775, VSP_038776, VSP_038777;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=O88196-5; Sequence=VSP_038774;
CC         Note=No experimental confirmation available;
CC       Name=6;
CC         IsoId=O88196-6; Sequence=VSP_038778;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylation on Ser-378 by Akt is required for ubiquitin
CC       ligase activity (By similarity).
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SIMILARITY: Contains 4 TPR repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH19173.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAH57207.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=BAC35513.1; Type=Erroneous initiation;
CC       Sequence=BAD90293.1; Type=Erroneous initiation;
CC       Sequence=BAE28586.1; Type=Erroneous initiation;
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DR   EMBL; AB008516; BAA31563.1; -; mRNA.
DR   EMBL; AK053765; BAC35513.1; ALT_INIT; mRNA.
DR   EMBL; AK088273; BAC40250.1; -; mRNA.
DR   EMBL; AK162004; BAE36675.1; -; mRNA.
DR   EMBL; AK163496; BAE37372.1; -; mRNA.
DR   EMBL; AK164106; BAE37630.1; -; mRNA.
DR   EMBL; AK164492; BAE37809.1; -; mRNA.
DR   EMBL; AK165850; BAE38412.1; -; mRNA.
DR   EMBL; AK148494; BAE28586.1; ALT_INIT; mRNA.
DR   EMBL; AK220495; BAD90293.1; ALT_INIT; mRNA.
DR   EMBL; BC019173; AAH19173.1; ALT_SEQ; mRNA.
DR   EMBL; BC057207; AAH57207.1; ALT_SEQ; mRNA.
DR   IPI; IPI00314009; -.
DR   IPI; IPI00473525; -.
DR   IPI; IPI00885375; -.
DR   IPI; IPI00885420; -.
DR   IPI; IPI00886205; -.
DR   IPI; IPI00955373; -.
DR   PIR; JW0059; JW0059.
DR   UniGene; Mm.213408; -.
DR   HSSP; P31948; 1ELW.
DR   ProteinModelPortal; O88196; -.
DR   SMR; O88196; 227-340, 535-605, 1925-1974.
DR   IntAct; O88196; 1.
DR   STRING; O88196; -.
DR   PhosphoSite; O88196; -.
DR   Ensembl; ENSMUST00000036349; ENSMUSP00000046251; ENSMUSG00000040785.
DR   Ensembl; ENSMUST00000117648; ENSMUSP00000112801; ENSMUSG00000040785.
DR   UCSC; uc008aaz.1; mouse.
DR   MGI; MGI:1276539; Ttc3.
DR   eggNOG; roNOG11367; -.
DR   HOGENOM; HBG282532; -.
DR   HOVERGEN; HBG007494; -.
DR   InParanoid; O88196; -.
DR   OrthoDB; EOG4KKZ2P; -.
DR   ArrayExpress; O88196; -.
DR   Bgee; O88196; -.
DR   Genevestigator; O88196; -.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005773; C:vacuole; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0010771; P:negative regulation of cell morphogenesis involved in differentiation; IDA:MGI.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; IDA:MGI.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0051789; P:response to protein stimulus; IDA:MGI.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 2.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00028; TPR; 3.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 2.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Ligase; Metal-binding; Nucleus; Phosphoprotein;
KW   Repeat; TPR repeat; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1   1979       E3 ubiquitin-protein ligase TTC3.
FT                                /FTId=PRO_0000392034.
FT   REPEAT      231    264       TPR 1.
FT   REPEAT      266    298       TPR 2.
FT   REPEAT      536    572       TPR 3.
FT   REPEAT      576    609       TPR 4.
FT   ZN_FING    1931   1971       RING-type; atypical.
FT   COMPBIAS   1018   1029       Arg/Lys-rich (basic).
FT   COMPBIAS   1171   1184       Arg/Lys-rich (basic).
FT   COMPBIAS   1547   1563       Arg/Lys-rich (basic).
FT   MOD_RES     378    378       Phosphoserine (By similarity).
FT   VAR_SEQ       1    401       Missing (in isoform 5).
FT                                /FTId=VSP_038774.
FT   VAR_SEQ     143    160       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_038775.
FT   VAR_SEQ    1056   1056       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_038776.
FT   VAR_SEQ    1089   1110       Missing (in isoform 4).
FT                                /FTId=VSP_038777.
FT   VAR_SEQ    1593   1593       Missing (in isoform 6).
FT                                /FTId=VSP_038778.
FT   CONFLICT     94     94       L -> P (in Ref. 1; BAA31563).
FT   CONFLICT    454    454       F -> S (in Ref. 1; BAC35513/BAE38412).
FT   CONFLICT   1164   1164       I -> F (in Ref. 1; BAE37809).
FT   CONFLICT   1177   1177       L -> P (in Ref. 1; BAC40250).
FT   CONFLICT   1522   1522       N -> S (in Ref. 1; BAE36675).
FT   CONFLICT   1571   1571       S -> P (in Ref. 1; BAE36675/BAE37630/
FT                                BAE37809).
FT   CONFLICT   1603   1603       A -> V (in Ref. 1; BAE36675/BAE37630/
FT                                BAE37809).
FT   CONFLICT   1822   1822       N -> S (in Ref. 1; BAE36675).
FT   CONFLICT   1847   1847       V -> F (in Ref. 1; BAE36675).
SQ   SEQUENCE   1979 AA;  223931 MW;  63A93E3CA1CECF00 CRC64;
     MDDFAEGGLS LADDILLEDY PYEDDCICTP DFTTDDYVRV TQLYYEGVGM QYKDYAQSEK
     NLEYDICNIW CSKPLSILQD YCDAIKLYIF WPLLFQHQHS SIISRLHPCV EAIRSRAAEI
     SLKKLQHLEL MEDIVDLAKK VANDSFLIEG LLKIGYKIEN KILAMEDALN WIKYTGDVTI
     LPKLGSVDNC WPMLSIFFTE YKYHITRVVT ENCNLLEEFR RHSCMQCVKQ GELMKMRGNE
     EFSKEKFEIA VIYYTRAIEY RPENHLLYGN RALCFLRMGQ FRNALSDGKR AIVLKNTWPK
     GHYRYCDALC MLGEYDWALQ ANIKAQKLCK NDPEGIKDLI QQHVKLQKQI EDLQGRTSNK
     NPIKAFYESR AYIPRNSSAP AFRTSLNFVE TERGFRKTKY KMANGGDQNQ KVADEALKGD
     DCDCHPEFLP PPSQPPRHKG KQKSRNNESE KPSFNSEVSL QVDLKSILEK QFSKSSRAAH
     QDFANIMKML RSLIQDGYTA LLEQRCRSAA QAFTELLNGL DPQKIKQLNL AMINYVLVVY
     GLAVSLLGIG RPEELSEAEN QFKRIIEHYP NEGLDCLAYC GIGKVYLKKN RFLEALNHFE
     KAKTLISRLP GILTWPTSNV IIEESKPEKV KVMLEKFVEE CKFPPVPDAV CCYQKCRGYS
     KIQIYLTDPD FKGFIRISCC QYCKVEFHMN CWKKLKTTTF NDKIDKDFLQ GICLTPDCEG
     IISKIIIYSS GGQVKCEFEH KVIKEKVPSR PVLKQKCSSL EKLRLKEDKK LKRKIQKQEA
     KKLAQERMEE DLRESNPPKN EEPEETSDSA QRCQFLDDRI LQCIKQNADK IKSVVLNTST
     LLKELLSWKV LSTEDYTTCF SSKNFVHEAV DYVIGHLIQE KNRVKTRIFL HVLSELKELD
     PKLAPWIQRL NSFGLDAIGP FFTRYGASLK ELDFHVVTVL WDEKYGHKLG SIEGKQLDYF
     FEPASAMEAR CLIWLLEEHR DKFPALHSAL DEFFDIMDSR CTVLRKQDSD EMPFGCIKVK
     NKGKKKKPKD SKPMLVGSGA ASVAPSSEAV TPEDHSRRNS DSAGPFAVPD HLRQDVEEFE
     ALYDQHSSEY VVRNKKLWDI NPKQKCSTLY DYFSQLLEEH GPLDMSDRMF SEEYEFFPEE
     TRQILEKAGG LKSFLLGCPR FVVIDNCIAL KKVASRLKKK RKKKNMKAKV EDISKTGEYL
     RVKLPLNPTA REFQPDVKSE ALSEDVKSIP GPADSSTLAA EDLKAQLDSD SSSGSASEDS
     RLEVASPDSP TPLCEDASPS PTPAPEEAKP TYWAQSHLVT GFCTYLPFQG FGITQRPAYI
     NMVPSLSQFT SIYTPLANIS SEYPMQRSMP VVPSFVASNR ADENAAAYFE SPNLNTEHDS
     GDHMASETQI LEDTLGVCVR SQGSAADADP ALSEPEGNSE HSGSSDSLWE ASLENVSGTT
     DAPAAPSVAI QVSRSMVHQE VNTEPYEPFE TQQGDLSQKE KECHLLREQL KVACENCEQI
     ELRSSQEIKD LEEKLQRHTE ENKISKTELD WFLQDLDREI KKWQQEKKEI QERLKALKKK
     IKKVINTSEM SAQKNDGFDK ECEPHPDQSL GFSSALTDEK TKAEESVRKG KELYEESHQR
     AVAAEVSVLE NWKEREVCKL QGVASQSEAY LKSLKLMSSD SATYPDVEYD ILSWESFLST
     VREEIESKKS QFEEHIKAIK NGSRLSDLSS VQLSEVSFPG CSTIHPQFLS ESSGHEDPGL
     VACVDSMTGA VLNDPYMDSA SGCPEEVPEL SLGSPTHQPE VTQQLELKGA SQVSPSEQSP
     EADEKLSGQA TRSSQSPKKP SNSIIEHLSV IFPCYTSTEL AGFIKKVRNK TKNSFSGLTI
     EEIVEKVTEH IVDEQKKKKP NPGKDKKTSE AHSAASVAKS SQSPPLAAAG PSARTKGQKK
     DDVPAPDGNS CEICHEIFKS KNMRVLKCGH KFHKGCFKQW LKGQSTCPTC GSSDLLSEE
//
ID   GREM2_MOUSE             Reviewed;         168 AA.
AC   O88273;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Gremlin-2;
DE   AltName: Full=Cysteine knot superfamily 1, BMP antagonist 2;
DE   AltName: Full=Protein related to DAN and cerberus;
DE   Flags: Precursor;
GN   Name=Grem2; Synonyms=Cktsf1b2, Prdc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6; TISSUE=CNS;
RX   MEDLINE=98301233; PubMed=9639362;
RX   DOI=10.1046/j.1440-169X.1998.t01-1-00010.x;
RA   Minabe-Saegusa C., Saegusa H., Tsukahara M., Noguchi S.;
RT   "Sequence and expression of a novel mouse gene PRDC (protein related
RT   to DAN and cerberus) identified by a gene trap approach.";
RL   Dev. Growth Differ. 40:343-353(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Head;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, INTERACTION WITH BMP2 AND BMP4, TISSUE SPECIFICITY, AND
RP   INDUCTION.
RX   PubMed=15039429; DOI=10.1074/jbc.M402376200;
RA   Sudo S., Avsian-Kretchmer O., Wang L.S., Hsueh A.J.;
RT   "Protein related to DAN and cerberus is a bone morphogenetic protein
RT   antagonist that participates in ovarian paracrine regulation.";
RL   J. Biol. Chem. 279:23134-23141(2004).
CC   -!- FUNCTION: Cytokine that inhibits the activity of BMP2 and BMP4 in
CC       a dose-dependent manner. Antagonized BMP4-induced suppression of
CC       progesterone production in granulosa cells.
CC   -!- SUBUNIT: Interacts with BMP2 and BMP4.
CC   -!- SUBCELLULAR LOCATION: Secreted (Probable).
CC   -!- TISSUE SPECIFICITY: Highly expressed in the ovary, followed by
CC       brain, spleen, colon, kidney and uterus. In ovary expressed in
CC       granulosa cells of selective early antral follicles.
CC   -!- DEVELOPMENTAL STAGE: Expressed in commissural neurons in the
CC       developing spinal cord.
CC   -!- INDUCTION: Up-regulated by gonadotropin treatment.
CC   -!- SIMILARITY: Belongs to the DAN family.
CC   -!- SIMILARITY: Contains 1 CTCK (C-terminal cystine knot-like) domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB011030; BAA29038.1; -; mRNA.
DR   EMBL; BC079905; AAH79905.1; -; mRNA.
DR   IPI; IPI00128969; -.
DR   RefSeq; NP_035955.1; NM_011825.1.
DR   UniGene; Mm.25760; -.
DR   ProteinModelPortal; O88273; -.
DR   STRING; O88273; -.
DR   PhosphoSite; O88273; -.
DR   PRIDE; O88273; -.
DR   Ensembl; ENSMUST00000055294; ENSMUSP00000049640; ENSMUSG00000050069.
DR   GeneID; 23893; -.
DR   KEGG; mmu:23893; -.
DR   UCSC; uc007dtf.1; mouse.
DR   CTD; 23893; -.
DR   MGI; MGI:1344367; Grem2.
DR   eggNOG; maNOG17976; -.
DR   HOGENOM; HBG444607; -.
DR   HOVERGEN; HBG051837; -.
DR   InParanoid; O88273; -.
DR   OMA; CAFCKPH; -.
DR   OrthoDB; EOG4Z62PP; -.
DR   PhylomeDB; O88273; -.
DR   NextBio; 303653; -.
DR   ArrayExpress; O88273; -.
DR   Bgee; O88273; -.
DR   Genevestigator; O88273; -.
DR   GermOnline; ENSMUSG00000050069; Mus musculus.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   InterPro; IPR006207; Cys_knot_C.
DR   InterPro; IPR004133; DAN.
DR   InterPro; IPR017159; Gremlin_precursor.
DR   Pfam; PF03045; DAN; 1.
DR   PIRSF; PIRSF037254; Gremlin_precursor; 1.
DR   SMART; SM00041; CT; 1.
DR   PROSITE; PS01225; CTCK_2; 1.
PE   1: Evidence at protein level;
KW   Cytokine; Disulfide bond; Glycoprotein; Secreted; Signal.
FT   SIGNAL        1     21       Potential.
FT   CHAIN        22    168       Gremlin-2.
FT                                /FTId=PRO_0000006721.
FT   DOMAIN       73    163       CTCK.
FT   CARBOHYD     40     40       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    161    161       N-linked (GlcNAc...) (Potential).
FT   DISULFID     73    123       By similarity.
FT   DISULFID     87    137       By similarity.
FT   DISULFID     97    155       By similarity.
FT   DISULFID    101    157       By similarity.
SQ   SEQUENCE   168 AA;  19334 MW;  6361C1581D49C281 CRC64;
     MFWKLSLTLL LVAVLVKVAE TRKNRPAGAI PSPYKDGSSN NSERWHHQIK EVLASSQEAL
     VVTERKYLKS DWCKTQPLRQ TVSEEGCRSR TILNRFCYGQ CNSFYIPRHV KKEEDSFQSC
     AFCKPQRVTS VIVELECPGL DPPFRIKKIQ KVKHCRCMSV NLSDSDKQ
//
ID   WIZ_MOUSE               Reviewed;        1684 AA.
AC   O88286; O88287; Q1XG03; Q3UZX7; Q7TSJ4; Q9CT89;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Protein Wiz;
DE   AltName: Full=Widely-interspaced zinc finger-containing protein;
GN   Name=Wiz;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS L AND S), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Brain;
RX   PubMed=9795207; DOI=10.1016/S0169-328X(98)00216-2;
RA   Matsumoto K., Ishii N., Yoshida S., Shiosaka S., Wanaka A.,
RA   Tohyama M.;
RT   "Molecular cloning and distinct developmental expression pattern of
RT   spliced forms of a novel zinc finger gene wiz in the mouse
RT   cerebellum.";
RL   Brain Res. Mol. Brain Res. 61:179-189(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM S), FUNCTION, TISSUE SPECIFICITY,
RP   IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH EHMT1; EHMT2;
RP   CTBP1 AND CTBP2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-1631 AND
RP   HIS-1651.
RX   PubMed=16702210; DOI=10.1074/jbc.M603087200;
RA   Ueda J., Tachibana M., Ikura T., Shinkai Y.;
RT   "Zinc finger protein Wiz links G9a/GLP histone methyltransferases to
RT   the co-repressor molecule CtBP.";
RL   J. Biol. Chem. 281:20120-20128(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1525-1684 (ISOFORM L).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Pituitary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   POLYMORPHISM.
RX   PubMed=12226707; DOI=10.1007/s00335-002-2178-3;
RA   Baust C., Baillie G.J., Mager D.L.;
RT   "Insertional polymorphisms of ETn retrotransposons include a
RT   disruption of the wiz gene in C57BL/6 mice.";
RL   Mamm. Genome 13:423-428(2002).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1045; THR-1049 AND
RP   SER-1050, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1050, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: May link EHMT1 and EHMT2 histone methyltransferases to
CC       the CTBP corepressor machinery. May be involved in EHMT1-EHMT2
CC       heterodimer formation and stabilization.
CC   -!- SUBUNIT: Interacts with EHMT1, EHMT2, CTBP1 and CTBP2.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=L;
CC         IsoId=O88286-1; Sequence=Displayed;
CC       Name=S;
CC         IsoId=O88286-2; Sequence=VSP_024954;
CC       Name=2;
CC         IsoId=O88286-3; Sequence=VSP_024953, VSP_024956, VSP_024958;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=O88286-4; Sequence=VSP_024955, VSP_024957;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: According to PubMed:9795207, isoform L and
CC       isoform S are brain-specific. According to PubMed:16702210,
CC       isoform S is ubiquitously expressed.
CC   -!- DEVELOPMENTAL STAGE: Isoform L and isoform S are expressed in
CC       brain from E14 to adulthood, with highest levels in the perinatal
CC       period. At embryonic stages, isoform L seems to be excluded from
CC       cerebellum.
CC   -!- DOMAIN: The C2H2-type zinc finger 10 mediates interaction with
CC       EHMT1 and EHMT2.
CC   -!- POLYMORPHISM: C57BL/6J and C57BR/cdJ mice specifically present an
CC       insertion of a type II early transposon in the opposite
CC       orientation into exon 6. This results in a strong reduction in the
CC       protein levels of isoform L.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family.
CC   -!- SIMILARITY: Contains 10 C2H2-type zinc fingers.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB012265; BAA32790.1; -; mRNA.
DR   EMBL; AB012266; BAA32791.1; -; mRNA.
DR   EMBL; AB255388; BAE93139.1; -; mRNA.
DR   EMBL; AK004274; BAB23245.1; -; mRNA.
DR   EMBL; AK133564; BAE21728.1; -; mRNA.
DR   EMBL; BC053035; AAH53035.1; -; mRNA.
DR   IPI; IPI00129016; -.
DR   IPI; IPI00263016; -.
DR   IPI; IPI00408547; -.
DR   IPI; IPI00623297; -.
DR   PIR; T00247; T00247.
DR   PIR; T00248; T00248.
DR   RefSeq; NP_035847.2; NM_011717.4.
DR   RefSeq; NP_997603.3; NM_212438.3.
DR   UniGene; Mm.274948; -.
DR   ProteinModelPortal; O88286; -.
DR   SMR; O88286; 303-425, 446-485, 698-827, 897-928, 1071-1101.
DR   STRING; O88286; -.
DR   PhosphoSite; O88286; -.
DR   PRIDE; O88286; -.
DR   Ensembl; ENSMUST00000003725; ENSMUSP00000003725; ENSMUSG00000024050.
DR   Ensembl; ENSMUST00000064694; ENSMUSP00000069443; ENSMUSG00000024050.
DR   Ensembl; ENSMUST00000087699; ENSMUSP00000084989; ENSMUSG00000024050.
DR   Ensembl; ENSMUST00000087703; ENSMUSP00000084993; ENSMUSG00000024050.
DR   Ensembl; ENSMUST00000114463; ENSMUSP00000110107; ENSMUSG00000024050.
DR   GeneID; 22404; -.
DR   KEGG; mmu:22404; -.
DR   CTD; 22404; -.
DR   MGI; MGI:1332638; Wiz.
DR   eggNOG; roNOG04928; -.
DR   GeneTree; ENSGT00530000063587; -.
DR   HOGENOM; HBG505951; -.
DR   HOVERGEN; HBG108678; -.
DR   InParanoid; O88286; -.
DR   OrthoDB; EOG454909; -.
DR   NextBio; 302789; -.
DR   ArrayExpress; O88286; -.
DR   Bgee; O88286; -.
DR   CleanEx; MM_WIZ; -.
DR   Genevestigator; O88286; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 1.
DR   SMART; SM00355; ZnF_C2H2; 11.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE   1: Evidence at protein level;
KW   Alternative splicing; Metal-binding; Methylation; Nucleus;
KW   Phosphoprotein; Polymorphism; Repeat; Zinc; Zinc-finger.
FT   CHAIN         1   1684       Protein Wiz.
FT                                /FTId=PRO_0000286055.
FT   ZN_FING     308    330       C2H2-type 1.
FT   ZN_FING     345    367       C2H2-type 2.
FT   ZN_FING     454    477       C2H2-type 3.
FT   ZN_FING     734    756       C2H2-type 4.
FT   ZN_FING     802    824       C2H2-type 5.
FT   ZN_FING     903    925       C2H2-type 6.
FT   ZN_FING    1076   1098       C2H2-type 7.
FT   ZN_FING    1260   1282       C2H2-type 8.
FT   ZN_FING    1430   1452       C2H2-type 9.
FT   ZN_FING    1629   1655       C2H2-type 10.
FT   REGION     1063   1067       Interaction with CTBP1 and CTBP2 1.
FT   REGION     1247   1251       Interaction with CTBP1 and CTBP2 2.
FT   COMPBIAS    299    304       Poly-Glu.
FT   COMPBIAS    601    608       Poly-Glu.
FT   COMPBIAS    658    663       Poly-Gln.
FT   COMPBIAS    786    790       Poly-Lys.
FT   COMPBIAS   1174   1177       Poly-Pro.
FT   MOD_RES    1029   1029       Phosphoserine (By similarity).
FT   MOD_RES    1039   1039       Phosphoserine (By similarity).
FT   MOD_RES    1045   1045       Phosphoserine.
FT   MOD_RES    1049   1049       Phosphothreonine.
FT   MOD_RES    1050   1050       Phosphoserine.
FT   MOD_RES    1160   1160       Phosphoserine (By similarity).
FT   MOD_RES    1167   1167       Phosphoserine (By similarity).
FT   MOD_RES    1179   1179       Phosphoserine (By similarity).
FT   MOD_RES    1184   1184       Phosphoserine (By similarity).
FT   MOD_RES    1188   1188       Phosphoserine (By similarity).
FT   MOD_RES    1195   1195       N6,N6,N6-trimethyllysine; by EHMT2;
FT                                alternate (By similarity).
FT   MOD_RES    1195   1195       N6,N6-dimethyllysine; by EHMT2; alternate
FT                                (By similarity).
FT   MOD_RES    1550   1550       Phosphoserine (By similarity).
FT   VAR_SEQ       1    759       Missing (in isoform 2).
FT                                /FTId=VSP_024953.
FT   VAR_SEQ      63    790       Missing (in isoform S).
FT                                /FTId=VSP_024954.
FT   VAR_SEQ     745    798       YGIGLANHVRGHLNRVGVSYNVRHFISAEEVKAIERRFSFQ
FT                                KKKKKVANFDPGT -> NGIVLRPPAARNVNGSTEKAARAV
FT                                REESRRGKRRNVAKTVTLIKAQILLLRHQL (in
FT                                isoform 3).
FT                                /FTId=VSP_024955.
FT   VAR_SEQ     760    789       VGVSYNVRHFISAEEVKAIERRFSFQKKKK -> MAEVAFL
FT                                MGSPILASAKPSPVPPPPPIGSA (in isoform 2).
FT                                /FTId=VSP_024956.
FT   VAR_SEQ     799   1684       Missing (in isoform 3).
FT                                /FTId=VSP_024957.
FT   VAR_SEQ     898    898       D -> DGLCSEENTMVAMDLGSPLLPKKSLPVSGTLEQVAS
FT                                RLSSKVAAEVPHGSKQELPDLK (in isoform 2).
FT                                /FTId=VSP_024958.
FT   MUTAGEN    1631   1631       C->A: Impairs interaction with EHMT1 and
FT                                EHMT2.
FT   MUTAGEN    1651   1651       H->A: Impairs interaction with EHMT1 and
FT                                EHMT2.
FT   CONFLICT    492    492       D -> G (in Ref. 1; BAA32790).
FT   CONFLICT    868    868       R -> G (in Ref. 1; BAA32790/BAA32791).
FT   CONFLICT   1020   1020       K -> N (in Ref. 3; AAH53035).
FT   CONFLICT   1052   1052       K -> R (in Ref. 1; BAA32790/BAA32791).
FT   CONFLICT   1055   1055       W -> C (in Ref. 1; BAA32790/BAA32791).
FT   CONFLICT   1252   1252       Missing (in Ref. 1; BAA32790/BAA32791).
SQ   SEQUENCE   1684 AA;  184291 MW;  67BA8AC25A97DDEB CRC64;
     MEGLLAGGLA APDHPRGPAP REDIESGAEA AEGEGDIFPS SHYLPITKEG PRDILDGRSG
     ISDGQPHPGL SEALPRATSA THRISSCYWD GDSLDFQPGS PPPHLLGPFP ASLDVQGSWE
     HPMVQEAREG TPSEQRFKDS VIVRTMKPYA KLKGSRKFLH HQGEVKFLEK YSPSHHKFDW
     LQDTDEQGPL KDTGLHLDLP AQPPTVTSFR RVIVPVDNTP KTLDMEVMGT REDLEDFGQV
     AQPSEWGLHT SASEVATQTW TVNSEASVER LQPLLSPVQT GPYLCELLQE VAGGVDSNEE
     EEEEPAVFPC IECSIYFKHK EHLLEHMSQH RRAPGQEPPA DLAPLACSEC GWAFTEPTAL
     EQHWQLHQAS REKIIEEIQK LKQFPGDEGR EARLQCSKCV FGTNSSRAFM QHAKLHVRGS
     LPSRQATEPF RGGSPVLDVS TLVYPSYGDS SGLNTCVHCG FTAPSKSLLR EHTRLVHAHH
     AHWEEVGEAF EDLTSQPCTS QDAYTHSPDT ATVDYFSKSE PLLASVWQEN PSGYDPDLAF
     GPDYQQPGMR NFPLLNSGQQ SLGKLAFPSP MASASYSIQR NRNKSTVHLQ RMEDKSHLWS
     EEEEEEDEDV VLTSERDFTP ENGAFPPLAI PSLIPQPALE LKQTFQDALQ AVDASETQQQ
     QLQGMVPIVL MAKLRPQVIA ATTRASPQLP PEEPELRSTH PLDFLLLDAP LGGSLGLNTL
     LEGDPAMALK HEERKCPYCP DRFHYGIGLA NHVRGHLNRV GVSYNVRHFI SAEEVKAIER
     RFSFQKKKKK VANFDPGTFS LMRCDFCGAG FDTRAGLSSH ARAHLRDFGI TNWELTISPI
     NILQELLATS AAELPPSPLG REPGGPPRSF LTSRRPRLPL TMPFPPTWAE DPGPIYGDAQ
     SLTTCEVCGA CFETRKGLSS HARSHLRQLG VAESESSGAP IDLLYELVKQ KGLPDAPLGL
     TPSLTKKSNS PKEFLAGAAR PGLLTLAKPM DAPAVNKAIK SPPGFSAKGL THPSSSPLLK
     KAPLTLAGSP TPKNPEDKSP QLSLSPRPTS PKAQWPQSED EGPLNLTSGP EPTRDIRCEF
     CGEFFENRKG LSSHARSHLR QMGVTEWYVN GSPIDTLREI LKRRTQSRPG GHLHPPGPSP
     KALAKVLSTG GPGSSLEARS PSDLHISPLT KKLPPPPGSP LGHSPTASPP PTARKMFSGL
     ATPSLPKKLK PEHMRVEIKR EMLPGTLHGE PHPSEGPWGT PREDMAPLNL SARAEPVRDI
     RCEFCGEFFE NRKGLSSHAR SHLRQMGVTE WSVNGSPIDT LREILKKKSK LCLIKKEPPA
     GDLAPALTED GSPTAAPGAL HSPLPLSPLA SRPGKPGAGP TQVPRELSLS PITGSKPSAA
     SYLGPVATKR PLQEDRFLPA EVKAKTYIQT ELPFKAKTLH EKTSHSSTEA CCELCGLYFE
     NRKALASHAR AHLRQFGVTE WCVNGSPIET LSEWIKHRPQ KVGAYRSYIQ GGRPFTKKFR
     SAGHGRDSDK RPPLGLAPGG LSLVGRSAGG EPGLEAGRAA DSGERPLATS PPGTVKSEEH
     QRQNINKFER RQARPSDASA ARGGEEVNDL QQKLEEVRQP PPRVRPVPSL VPRPPQTSLV
     KFVGNIYTLK CRFCEVEFQG PLSIQEEWVR HLQRHILEMN FSKADPPPEE PQAPQAQTAA
     VEAP
//
ID   ZN326_MOUSE             Reviewed;         580 AA.
AC   O88291; Q8BSJ5; Q8K1X9; Q9CYG9;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Zinc finger protein 326;
DE   AltName: Full=Zinc finger protein-associated with nuclear matrix of 75 kDa;
GN   Name=Znf326; Synonyms=Zan75, Zfp326;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=99025618; PubMed=9809746;
RA   Lee J.-Y., Kambe M., Hayashi M., Takenaga K.;
RT   "Cloning and characterization of a novel zinc finger protein that
RT   associates with nuclear matrix.";
RL   DNA Cell Biol. 17:849-858(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Wolffian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, BIPARTITE NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=10798446; DOI=10.1089/104454900314492;
RA   Lee J.-Y., Nakane Y., Koshikawa N., Nakayama K., Hayashi M.,
RA   Takenaga K.;
RT   "Characterization of a zinc finger protein ZAN75: nuclear localization
RT   signal, transcriptional activator activity, and expression during
RT   neuronal differentiation of P19 cells.";
RL   DNA Cell Biol. 19:227-234(2000).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189 AND TYR-190, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Probable transcriptional activator which may play a role
CC       in neuronal differentiation. Able to bind DNA and activate
CC       expression in vitro.
CC   -!- SUBCELLULAR LOCATION: Nucleus matrix.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O88291-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O88291-2; Sequence=VSP_014957;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=O88291-3; Sequence=VSP_014958, VSP_014959;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed in adult tissues.
CC       Highly expressed in neuronal tissues such as brain and neural
CC       tube.
CC   -!- DEVELOPMENTAL STAGE: Weakly expressed during E9.5 and E10.5,
CC       expressed at highest level in E11.5 and gradually decreases
CC       thereafter. During the cell cycle, it is weakly expressed in G0
CC       and G1 phases. It increases during G1, S, G2 and M phases.
CC   -!- INDUCTION: Upon retinoic acid treatment.
CC   -!- SIMILARITY: Belongs to the AKAP95 family.
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DR   EMBL; AB012725; BAA31522.1; -; mRNA.
DR   EMBL; AK017693; BAB30878.1; -; mRNA.
DR   EMBL; AK032801; BAC28029.1; -; mRNA.
DR   EMBL; BC037055; AAH37055.1; -; mRNA.
DR   IPI; IPI00314507; -.
DR   IPI; IPI00458689; -.
DR   IPI; IPI00650041; -.
DR   RefSeq; NP_061229.2; NM_018759.2.
DR   UniGene; Mm.248876; -.
DR   STRING; O88291; -.
DR   PhosphoSite; O88291; -.
DR   PRIDE; O88291; -.
DR   Ensembl; ENSMUST00000031227; ENSMUSP00000031227; ENSMUSG00000029290.
DR   GeneID; 54367; -.
DR   KEGG; mmu:54367; -.
DR   UCSC; uc008ylj.1; mouse.
DR   UCSC; uc008ylk.1; mouse.
DR   CTD; 54367; -.
DR   MGI; MGI:1927246; Zfp326.
DR   eggNOG; roNOG05356; -.
DR   HOGENOM; HBG506188; -.
DR   HOVERGEN; HBG080752; -.
DR   InParanoid; O88291; -.
DR   OrthoDB; EOG4JHCFK; -.
DR   NextBio; 311162; -.
DR   ArrayExpress; O88291; -.
DR   Bgee; O88291; -.
DR   CleanEx; MM_ZFP326; -.
DR   Genevestigator; O88291; -.
DR   GermOnline; ENSMUSG00000029290; Mus musculus.
DR   GO; GO:0005626; C:insoluble fraction; IDA:MGI.
DR   GO; GO:0016363; C:nuclear matrix; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0016563; F:transcription activator activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IDA:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR007071; AKAP95.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   PANTHER; PTHR12190; AKAP95; 1.
DR   Pfam; PF04988; AKAP95; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Alternative splicing; DNA-binding;
KW   Metal-binding; Nucleus; Phosphoprotein; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    580       Zinc finger protein 326.
FT                                /FTId=PRO_0000075387.
FT   ZN_FING     312    336       C2H2 AKAP95-type 1.
FT   ZN_FING     405    430       C2H2 AKAP95-type 2.
FT   REGION        1    124       Mediates transcriptional activation.
FT   MOTIF       238    260       Bipartite nuclear localization signal.
FT   COMPBIAS     27    211       Gly-rich.
FT   COMPBIAS    484    564       Glu-rich.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     137    137       Phosphoserine (By similarity).
FT   MOD_RES     189    189       Phosphoserine.
FT   MOD_RES     190    190       Phosphotyrosine.
FT   MOD_RES     247    247       N6-acetyllysine (By similarity).
FT   MOD_RES     270    270       Phosphoserine (By similarity).
FT   MOD_RES     274    274       Phosphothreonine (By similarity).
FT   VAR_SEQ       1    206       Missing (in isoform 2).
FT                                /FTId=VSP_014957.
FT   VAR_SEQ      35     67       DRDYGHGSYGGQRSMDSYLNQSYGMDNHSGGGG -> AFKD
FT                                IYLKILLLSASKGEQHLIFFFLNSYRAGS (in isoform
FT                                3).
FT                                /FTId=VSP_014958.
FT   VAR_SEQ      68    580       Missing (in isoform 3).
FT                                /FTId=VSP_014959.
FT   CONFLICT    494    494       D -> G (in Ref. 2; BAB30878).
SQ   SEQUENCE   580 AA;  65225 MW;  EF9672513D0FFC70 CRC64;
     MDFEDDYVHS TCRGAYQDFN GMDRDYGPGS YGGLDRDYGH GSYGGQRSMD SYLNQSYGMD
     NHSGGGGGSR FGPYESYDSR SSLGGRDLYR SGYGFNEPEQ TRFGGSYGGR FESSYRNSLD
     SFGGRNQGGS SWEAPYSRSK LRPGFMEDRG RENYSSYSSF SSPHMKPAPV GSRGRGTPAY
     PESTFGSRSY DAFGGPSTGR GRGRGHMGDF GSFHRPGIIV DYQNKPANVT IATARGIKRK
     MMQIFIKPGG AFIKKPKLAK PMDKMNLSKS PTKTDPKNEE EEKRRIEARR EKQRRRREKN
     SEKYGDGYRM AFTCSFCKFR TFEEKDIELH LESSSHQETL DHIQKQTKFD KVVMEFLHEC
     MVNKFKKASI RKQQTLNHPE AYKIIEKDIM EGVTADDHMM KVETVHCSAC SVYIPALHSS
     VQLHLKSPDH SKGKQAYKEQ IKRESVLTAT SILNNPIVKA RYERFVKGEN PFEIQDHPQD
     QQIEGDEEDE EKIDEPIEEE EEEEEEEEEE GEEAGSVEEE GDVEGEEGTA EAAAAGEADA
     VGEAEGAGEA EEAEEEEEEE GTQEFAAQAC ATEQCEHRQM
//
ID   NTR1_MOUSE              Reviewed;         424 AA.
AC   O88319;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Neurotensin receptor type 1;
DE            Short=NT-R-1;
DE            Short=NTR1;
GN   Name=Ntsr1; Synonyms=Ntsr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Snider J., Sano H., Ohta M.;
RT   "Neurotensin receptor type 1.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for the tridecapeptide neurotensin. It is
CC       associated with G proteins that activate a phosphatidylinositol-
CC       calcium second messenger system.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Neurotensin receptor subfamily. NTSR1 sub-subfamily.
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DR   EMBL; AB017027; BAA33013.1; -; mRNA.
DR   IPI; IPI00129862; -.
DR   RefSeq; NP_061236.1; NM_018766.2.
DR   UniGene; Mm.301712; -.
DR   ProteinModelPortal; O88319; -.
DR   STRING; O88319; -.
DR   PhosphoSite; O88319; -.
DR   PRIDE; O88319; -.
DR   Ensembl; ENSMUST00000029084; ENSMUSP00000029084; ENSMUSG00000027568.
DR   GeneID; 18216; -.
DR   KEGG; mmu:18216; -.
DR   UCSC; uc008ojg.1; mouse.
DR   CTD; 18216; -.
DR   MGI; MGI:97386; Ntsr1.
DR   HOGENOM; HBG717152; -.
DR   HOVERGEN; HBG098285; -.
DR   InParanoid; O88319; -.
DR   OMA; TVMVRQA; -.
DR   OrthoDB; EOG4V438D; -.
DR   PhylomeDB; O88319; -.
DR   NextBio; 461229; -.
DR   ArrayExpress; O88319; -.
DR   Bgee; O88319; -.
DR   CleanEx; MM_NTSR1; -.
DR   Genevestigator; O88319; -.
DR   GermOnline; ENSMUSG00000027568; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016492; F:neurotensin receptor activity, G-protein coupled; IEA:InterPro.
DR   GO; GO:0008344; P:adult locomotory behavior; IGI:MGI.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR003985; NT1_rcpt.
DR   InterPro; IPR003984; NT_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01479; NEUROTENSINR.
DR   PRINTS; PR01480; NEUROTENSN1R.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Receptor; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN         1    424       Neurotensin receptor type 1.
FT                                /FTId=PRO_0000069947.
FT   TOPO_DOM      1     64       Extracellular (Potential).
FT   TRANSMEM     65     87       Helical; Name=1; (Potential).
FT   TOPO_DOM     88     96       Cytoplasmic (Potential).
FT   TRANSMEM     97    121       Helical; Name=2; (Potential).
FT   TOPO_DOM    122    143       Extracellular (Potential).
FT   TRANSMEM    144    165       Helical; Name=3; (Potential).
FT   TOPO_DOM    166    188       Cytoplasmic (Potential).
FT   TRANSMEM    189    210       Helical; Name=4; (Potential).
FT   TOPO_DOM    211    235       Extracellular (Potential).
FT   TRANSMEM    236    260       Helical; Name=5; (Potential).
FT   TOPO_DOM    261    308       Cytoplasmic (Potential).
FT   TRANSMEM    309    330       Helical; Name=6; (Potential).
FT   TOPO_DOM    331    348       Extracellular (Potential).
FT   TRANSMEM    349    372       Helical; Name=7; (Potential).
FT   TOPO_DOM    373    424       Cytoplasmic (Potential).
FT   LIPID       388    388       S-palmitoyl cysteine (Potential).
FT   CARBOHYD      4      4       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     38     38       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     42     42       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    211    211       N-linked (GlcNAc...) (Potential).
FT   DISULFID    141    224       By similarity.
SQ   SEQUENCE   424 AA;  47217 MW;  8E9A723171A48711 CRC64;
     MHLNSSVQQG APSEPGAQPF PHPQFGLETM LLALSLSNGS GNSSESILEP NSNLDVNTDI
     YSKVLVTAVY LALFVVGTVG NSVTAFTLAR KKSLQSLQST VHYHLGSLAL SDLLILLLAM
     PVELYNFIWV HHPWAFGDAG CRGYYFLRDA CTYATALNVA SLSVERYLAI CHPFKAKTLM
     SRSRTKKFIS AIWLASALLA VPMLFTMGLQ NRSADGQHPG GLVCTPTVDT ATVKVVIQVN
     TFMSFLFPML IISILNTVIA NKLTVMVHQA AEQGRGVCTV GTHNSLEHST FNMSIEPGRV
     QALRHGVLVL RAVVIAFVVC WLPYHVRRLM FCYISDEQWT TFLFDFYHYF YMLTNALFYV
     SSAINPILYN LVSANFRQVF LSTLACLCPG WRRRRKKRPT FSRKPNSMSS NHAFSTSATR
     ETLY
//
ID   CTNL1_MOUSE             Reviewed;         731 AA.
AC   O88327; Q810J3;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Alpha-catulin;
DE   AltName: Full=Alpha-catenin-related protein;
DE            Short=ACRP;
DE   AltName: Full=Catenin alpha-like protein 1;
GN   Name=Ctnnal1; Synonyms=Catnal1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kishi M., Nagafuchi A., Tsukita S.;
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May modulate the Rho pathway signaling by providing a
CC       scaffold for the Lbc Rho guanine nucleotide exchange factor
CC       (ARHGEF1) (By similarity).
CC   -!- SUBUNIT: Interacts with ARHGEF1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Cell membrane; Peripheral membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
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DR   EMBL; AF006071; AAC26012.1; -; mRNA.
DR   EMBL; BC050070; AAH50070.1; -; mRNA.
DR   IPI; IPI00129908; -.
DR   RefSeq; NP_061231.3; NM_018761.3.
DR   UniGene; Mm.218891; -.
DR   ProteinModelPortal; O88327; -.
DR   SMR; O88327; 67-277.
DR   STRING; O88327; -.
DR   PhosphoSite; O88327; -.
DR   PRIDE; O88327; -.
DR   Ensembl; ENSMUST00000045142; ENSMUSP00000036487; ENSMUSG00000038816.
DR   GeneID; 54366; -.
DR   KEGG; mmu:54366; -.
DR   UCSC; uc008sxu.1; mouse.
DR   CTD; 54366; -.
DR   MGI; MGI:1859649; Ctnnal1.
DR   eggNOG; roNOG14973; -.
DR   GeneTree; ENSGT00550000074411; -.
DR   HOGENOM; HBG444892; -.
DR   HOVERGEN; HBG051219; -.
DR   InParanoid; O88327; -.
DR   OMA; KVLATME; -.
DR   OrthoDB; EOG46HG98; -.
DR   PhylomeDB; O88327; -.
DR   NextBio; 311158; -.
DR   ArrayExpress; O88327; -.
DR   Bgee; O88327; -.
DR   Genevestigator; O88327; -.
DR   GermOnline; ENSMUSG00000038816; Mus musculus.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045296; F:cadherin binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   InterPro; IPR001033; Alpha_catenin.
DR   InterPro; IPR006077; Vinculin/catenin.
DR   Pfam; PF01044; Vinculin; 3.
DR   PRINTS; PR00805; ALPHACATENIN.
DR   SUPFAM; SSF47220; Vinculin/catenin; 3.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein.
FT   CHAIN         1    731       Alpha-catulin.
FT                                /FTId=PRO_0000064269.
FT   COMPBIAS      8     13       Poly-Gly.
FT   MOD_RES     537    537       Phosphoserine (By similarity).
FT   CONFLICT     62     62       K -> R (in Ref. 2; AAH50070).
FT   CONFLICT    135    135       T -> S (in Ref. 2; AAH50070).
FT   CONFLICT    728    728       D -> N (in Ref. 2; AAH50070).
SQ   SEQUENCE   731 AA;  81462 MW;  36CF25115E3EF1F3 CRC64;
     MAASPVPGGG GAGAVHSSNA AGFTFDSGLE IRTRSVEQTL LPLVSQITTL INHKDNTKKS
     DKTLQAIQRV GQAVNLAVGR FVKVGEAIAN ENWDLKEEIN IACIEAKQAG ETIASLTDVT
     KRSHLESDGQ VTILTDKTGV VQAARLLLSS VTKVLLLADR VVIKQIVTSR NKILATMERL
     EKVNSFQEFV QIFSQFGNEM VEFAHLTGDR QNDLKDEKKK ARMAVARAVL EKGTMMLLTA
     SKTCLRHPSC ESAHTNKEGV FDRMRVALEK VTEIVTDCRL SGETDSSSVS IFTGIKELKV
     NIEALRENVC FESKENLSAA LEAVLEHVED FTDSAYTSHE HRERILELSS QARTELQQLL
     SVWMQTQSRK TKSAAEELEL TVLKISHSLD ELRRELHCTA MQLAADLLKF HADHVVLKAL
     KVTGVEGNLE ALAEYACKLS EQKEQLVETC RLLRHISGTE PLEITCIHAE ETFQVTGQQI
     ISAAETLTLH PSSKIAKENL DVFCEAWESQ MSDMATLLRE ISDVFEGRRG ERCDHLSLPK
     PTKNSANLKS LKPDKPDSEE QAKIAKLGLK LGLLSSDADC EIEKWEDEEN EIVRHGRNMS
     RMAYSLYLFT RGEGPLKTSQ DLIHFLEVFA AEGLKLTSSV QSFSKQLKDD DKLMLLLEIN
     KLIPLCHQLQ TITKTSLQSK VFLKVDKCIT KIRSMMTLVV QLLSLCYKLL KKMENNRWGS
     ATNKDTMDGQ N
//
ID   S4A4_MOUSE              Reviewed;        1079 AA.
AC   O88343; Q3USE4; Q8BUG0; Q8QZR9; Q9R1C4;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Electrogenic sodium bicarbonate cotransporter 1;
DE            Short=Sodium bicarbonate cotransporter;
DE   AltName: Full=Na(+)/HCO3(-) cotransporter;
DE   AltName: Full=Solute carrier family 4 member 4;
GN   Name=Slc4a4; Synonyms=Nbc1, Nbce1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Pancreas;
RX   MEDLINE=98316338; PubMed=9651366; DOI=10.1074/jbc.273.28.17689;
RA   Abuladze N., Lee I., Newman D., Hwang J., Boorer K., Pushkin A.,
RA   Kurtz I.;
RT   "Molecular cloning, chromosomal localization, tissue distribution, and
RT   functional expression of the human pancreatic sodium bicarbonate
RT   cotransporter.";
RL   J. Biol. Chem. 273:17689-17695(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=C57BL/6; TISSUE=Duodenum;
RX   MEDLINE=21113639; PubMed=11171615;
RA   Praetorius J., Hager H., Nielsen S., Aalkjaer C., Friis U.G.,
RA   Ainsworth M.A., Johansen T.;
RT   "Molecular and functional evidence for electrogenic and electroneutral
RT   Na(+)-HCO(3)(-) cotransporters in murine duodenum.";
RL   Am. J. Physiol. 280:G332-G343(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-400 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-9; 60-67; 168-174; 323-331; 343-359; 607-618;
RP   753-766; 857-869 AND 935-943, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 382-1079.
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   GLYCOSYLATION.
RX   PubMed=12604466; DOI=10.1152/ajprenal.00131.2002;
RA   Choi I., Hu L., Rojas J.D., Schmitt B.M., Boron W.F.;
RT   "Role of glycosylation in the renal electrogenic Na+-HCO3-
RT   cotransporter (NBCe1).";
RL   Am. J. Physiol. 284:F1199-F1206(2003).
RN   [7]
RP   REGULATION BY CAMP, AND TISSUE SPECIFICITY.
RX   PubMed=12388213; DOI=10.1152/ajpgi.00209.2002;
RA   Bachmann O., Rossmann H., Berger U.V., Colledge W.H., Ratcliff R.,
RA   Evans M.J., Gregor M., Seidler U.;
RT   "cAMP-mediated regulation of murine intestinal/pancreatic Na+/HCO3-
RT   cotransporter subtype pNBC1.";
RL   Am. J. Physiol. 284:G37-G45(2003).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=22612361; PubMed=12727194; DOI=10.1016/S0006-291X(03)00632-6;
RA   Kim Y.-B., Yang B.H., Piao Z.G., Oh S.B., Kim J.S., Park K.;
RT   "Expression of Na+/HCO3- cotransporter and its role in pH regulation
RT   in mouse parotid acinar cells.";
RL   Biochem. Biophys. Res. Commun. 304:593-598(2003).
RN   [9]
RP   INTERACTION WITH CA4.
RX   PubMed=14567693; DOI=10.1021/bi0353124;
RA   Alvarez B.V., Loiselle F.B., Supuran C.T., Schwartz G.J., Casey J.R.;
RT   "Direct extracellular interaction between carbonic anhydrase IV and
RT   the human NBC1 sodium/bicarbonate co-transporter.";
RL   Biochemistry 42:12321-12329(2003).
RN   [10]
RP   INTERACTION WITH CA2.
RX   PubMed=15218065; DOI=10.1113/jphysiol.2004.065110;
RA   Pushkin A., Abuladze N., Gross E., Newman D., Tatishchev S., Lee I.,
RA   Fedotoff O., Bondar G., Azimov R., Ngyuen M., Kurtz I.;
RT   "Molecular mechanism of kNBC1-carbonic anhydrase II interaction in
RT   proximal tubule cells.";
RL   J. Physiol. (Lond.) 559:55-65(2004).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-254 AND SER-255, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-30, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1034, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-254; SER-257; SER-262;
RP   SER-1029 AND SER-1034, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Electrogenic sodium/bicarbonate cotransporter with a
CC       Na(+):HCO3(-) stoichiometry varying from 1:2 to 1:3. May regulate
CC       bicarbonate influx/efflux at the basolateral membrane of cells and
CC       regulate intracellular pH.
CC   -!- ENZYME REGULATION: Inhibited by stilbene derivatives and regulated
CC       by cyclic AMP.
CC   -!- SUBUNIT: Interacts with CA2/carbonic anhydrase 2 and CA4/carbonic
CC       anhydrase 4 which may regulate transporter activity.
CC   -!- SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass
CC       membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=pNBC;
CC         IsoId=O88343-1; Sequence=Displayed;
CC       Name=2; Synonyms=kNBC;
CC         IsoId=O88343-2; Sequence=VSP_016709, VSP_016710;
CC       Name=3;
CC         IsoId=O88343-3; Sequence=VSP_016709, VSP_016710, VSP_016711,
CC                                  VSP_016712;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is specifically expressed in
CC       pancreatic ducts and acini. Also expressed in parotid acinar cells
CC       and in the colonic crypts.
CC   -!- PTM: Phosphorylation of Ser-1026 by PKA increases the binding of
CC       CA2 and changes the Na(+):HCO3(-) stoichiometry of the transporter
CC       from 3:1 to 2:1 (By similarity).
CC   -!- PTM: N-glycosylated. May not be necessary for the transporter
CC       basic functions.
CC   -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
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DR   EMBL; AF020195; AAC40160.1; -; mRNA.
DR   EMBL; AF141934; AAD31036.3; -; mRNA.
DR   EMBL; AK085387; BAC39437.1; -; mRNA.
DR   EMBL; AK140443; BAE24389.1; -; mRNA.
DR   EMBL; BC026592; AAH26592.1; -; mRNA.
DR   IPI; IPI00314749; -.
DR   IPI; IPI00405057; -.
DR   IPI; IPI00662028; -.
DR   PIR; T14031; T14031.
DR   RefSeq; NP_001129732.1; NM_001136260.1.
DR   RefSeq; NP_061230.2; NM_018760.2.
DR   UniGene; Mm.41044; -.
DR   ProteinModelPortal; O88343; -.
DR   SMR; O88343; 106-411, 453-494, 920-952.
DR   STRING; O88343; -.
DR   PhosphoSite; O88343; -.
DR   PRIDE; O88343; -.
DR   Ensembl; ENSMUST00000066831; ENSMUSP00000071050; ENSMUSG00000060961.
DR   Ensembl; ENSMUST00000113216; ENSMUSP00000108842; ENSMUSG00000060961.
DR   Ensembl; ENSMUST00000113218; ENSMUSP00000108844; ENSMUSG00000060961.
DR   GeneID; 54403; -.
DR   KEGG; mmu:54403; -.
DR   UCSC; uc008yak.1; mouse.
DR   UCSC; uc008yal.1; mouse.
DR   CTD; 54403; -.
DR   MGI; MGI:1927555; Slc4a4.
DR   GeneTree; ENSGT00560000076851; -.
DR   HOGENOM; HBG355640; -.
DR   HOVERGEN; HBG004326; -.
DR   InParanoid; O88343; -.
DR   OrthoDB; EOG4320XB; -.
DR   PhylomeDB; O88343; -.
DR   NextBio; 311268; -.
DR   ArrayExpress; O88343; -.
DR   Bgee; O88343; -.
DR   Genevestigator; O88343; -.
DR   GermOnline; ENSMUSG00000060961; Mus musculus.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:MGI.
DR   GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0006885; P:regulation of pH; TAS:MGI.
DR   GO; GO:0006814; P:sodium ion transport; IDA:MGI.
DR   InterPro; IPR011531; HCO3_transpt_C.
DR   InterPro; IPR013769; HCO3_transpt_cyt.
DR   InterPro; IPR003020; HCO3_transpt_euk.
DR   InterPro; IPR003024; Na/HCO3_transpt.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   Gene3D; G3DSA:3.40.1100.10; HCO3_transpt_cyt; 1.
DR   PANTHER; PTHR11453; HCO3_transpt_euk; 1.
DR   Pfam; PF07565; Band_3_cyto; 1.
DR   Pfam; PF00955; HCO3_cotransp; 1.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   PRINTS; PR01232; NAHCO3TRSPRT.
DR   SUPFAM; SSF55804; PTrfase/Anion_transptr; 1.
DR   TIGRFAMs; TIGR00834; ae; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Direct protein sequencing;
KW   Glycoprotein; Ion transport; Membrane; Phosphoprotein; Sodium;
KW   Sodium transport; Symport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1   1079       Electrogenic sodium bicarbonate
FT                                cotransporter 1.
FT                                /FTId=PRO_0000079228.
FT   TOPO_DOM      1    468       Cytoplasmic (Potential).
FT   TRANSMEM    469    488       Helical; (Potential).
FT   TOPO_DOM    489    504       Extracellular (Potential).
FT   TRANSMEM    505    526       Helical; (Potential).
FT   TOPO_DOM    527    554       Cytoplasmic (Potential).
FT   TRANSMEM    555    580       Helical; (Potential).
FT   TOPO_DOM    581    691       Extracellular (Potential).
FT   TRANSMEM    692    710       Helical; (Potential).
FT   TOPO_DOM    711    725       Cytoplasmic (Potential).
FT   TRANSMEM    726    748       Helical; (Potential).
FT   TOPO_DOM    749    777       Extracellular (Potential).
FT   TRANSMEM    778    797       Helical; (Potential).
FT   TOPO_DOM    798    822       Cytoplasmic (Potential).
FT   TRANSMEM    823    847       Helical; (Potential).
FT   TOPO_DOM    848    881       Extracellular (Potential).
FT   TRANSMEM    882    901       Helical; (Potential).
FT   TOPO_DOM    902    949       Cytoplasmic (Potential).
FT   TRANSMEM    950    967       Helical; (Potential).
FT   TOPO_DOM    968    970       Extracellular (Potential).
FT   TRANSMEM    971    986       Helical; (Potential).
FT   TOPO_DOM    987   1079       Cytoplasmic (Potential).
FT   REGION      748    779       Interaction with CA4 (By similarity).
FT   REGION     1002   1004       CA2-binding (By similarity).
FT   REGION     1030   1033       CA2-binding (By similarity).
FT   REGION     1057   1059       Required for basolateral targeting (By
FT                                similarity).
FT   COMPBIAS   1009   1024       Lys-rich.
FT   MOD_RES      30     30       Phosphotyrosine.
FT   MOD_RES     254    254       Phosphothreonine.
FT   MOD_RES     255    255       Phosphoserine.
FT   MOD_RES     257    257       Phosphoserine.
FT   MOD_RES     262    262       Phosphoserine.
FT   MOD_RES    1026   1026       Phosphoserine; by PKA (By similarity).
FT   MOD_RES    1029   1029       Phosphoserine.
FT   MOD_RES    1034   1034       Phosphoserine.
FT   CARBOHYD    641    641       N-linked (GlcNAc...) (By similarity).
FT   CARBOHYD    661    661       N-linked (GlcNAc...) (By similarity).
FT   VAR_SEQ       1     44       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_016709.
FT   VAR_SEQ      45     85       HKRKAGHKEKKEKERISENYSDKSDVENADESSSSILKPLI
FT                                -> MSTENVEGKPNNLGERGRARSSTFLRVFQPMFNHSIFT
FT                                SAV (in isoform 2 and isoform 3).
FT                                /FTId=VSP_016710.
FT   VAR_SEQ     185    201       MIADHQIETGLLKPDLK -> LLGESRKVIRPAGFIRP
FT                                (in isoform 3).
FT                                /FTId=VSP_016711.
FT   VAR_SEQ     202   1079       Missing (in isoform 3).
FT                                /FTId=VSP_016712.
FT   CONFLICT    388    388       T -> A (in Ref. 1; AAC40160).
FT   CONFLICT    546    546       H -> N (in Ref. 1; AAC40160).
FT   CONFLICT    560    560       W -> R (in Ref. 1; AAC40160).
FT   CONFLICT    564    564       M -> L (in Ref. 1; AAC40160).
FT   CONFLICT    567    567       V -> I (in Ref. 1; AAC40160).
FT   CONFLICT    589    589       S -> P (in Ref. 1; AAC40160).
FT   CONFLICT    740    740       C -> G (in Ref. 1; AAC40160).
FT   CONFLICT    775    775       G -> E (in Ref. 1; AAC40160).
FT   CONFLICT    814    814       K -> Q (in Ref. 1; AAC40160).
FT   CONFLICT    832    832       V -> I (in Ref. 1; AAC40160).
FT   CONFLICT    835    835       F -> L (in Ref. 1; AAC40160).
FT   CONFLICT    848    848       S -> F (in Ref. 2; AAD31036).
FT   CONFLICT    876    876       Q -> P (in Ref. 2; AAD31036).
FT   CONFLICT    884    884       F -> L (in Ref. 1; AAC40160).
FT   CONFLICT    901    901       P -> R (in Ref. 2; AAD31036).
FT   CONFLICT    909    910       FL -> SW (in Ref. 2; AAD31036).
SQ   SEQUENCE   1079 AA;  121484 MW;  DBC7C3DEBE10BE97 CRC64;
     MEDEAVLDRG ASFLKHVCDE EEVEGHHTIY IGVHVPKSYR RRRRHKRKAG HKEKKEKERI
     SENYSDKSDV ENADESSSSI LKPLISPAAE RIRFILGEED DSPAPPQLFT ELDELLAVDG
     QEMEWKETAR WIKFEEKVEQ GGERWSKPHV ATLSLHSLFE LRTCMEKGSI MLDREASSLP
     QLVEMIADHQ IETGLLKPDL KDKVTYTLLR KHRHQTKKSN LRSLADIGKT VSSASRMFSN
     PDNGSPAMTH RNLTSSSLND ISDKPEKDQL KNKFMKKLPR DAEASNVLVG EVDFLDTPFI
     AFVRLQQAVM LGALTEVPVP TRFLFILLGP KGKAKSYHEI GRAIATLMSD EVFHDIAYKA
     KDRHDLIAGI DEFLDEVIVL PPGEWDPTIR IEPPKSLPSS DKRKNMYSGG ENVQMNGDTP
     HDGGHGGGGH GDCEELQRTG RFCGGLIKDI KRKAPFFASD FYDALNIQAL SAILFIYLAT
     VTNAITFGGL LGDATDNMQG VLESFLGTAV SGAIFCLFAG QPLTILSSTG PVLVFERLLF
     NFSKDHNFDY LEFRLWIGLW SAFMCLVLVA TDASFLVQYF TRFTEEGFSS LISFIFIYDA
     FKKMIKLADY YPINSDFKVG YNTHFSCACL PPDPVNLSVS NDTTLAPEDL PTISSTDMYH
     NVTFDWAYLS KKECVKYGGK LVGNNCDFVP DITLMSFILF LGTYTSSMAM KKFKTSRYFP
     TTARKLISDF AIILSILIFC VIDALVGVDT PKLIVPSEFK PTSPNRGWFV PPFGGNPWWV
     CLAAAIPALL VTILIFMDQQ ITAVIVNRKE HKLKKGAGYH LDLFWVAILM VVCSFMALPW
     YVAATVISIA HIDSLKMETE TSAPGEQPKF LGVREQRVTG TLVFILTGLS VFMAPILKFI
     PMPVLYGVFL YMGVASLNGV QFMDRLKLLL MPLKHQPDFI YLRHVPLRRV HLFTFLQVLC
     LALLWILKST VAAIIFPVMI LALVAVRKGM DYLFSQHDLS FLDDVIPEKD KKKKEDEKKK
     KKKKGSLDSD NDDSDCPYSE KVPSIKIPMD IMEQQPFLSD NKPLDRERSS TFLERHTSC
//
ID   IKKB_MOUSE              Reviewed;         757 AA.
AC   O88351; Q9R1J6;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 100.
DE   RecName: Full=Inhibitor of nuclear factor kappa-B kinase subunit beta;
DE            Short=I-kappa-B-kinase beta;
DE            Short=IKK-B;
DE            Short=IKK-beta;
DE            Short=IkBKB;
DE            EC=2.7.11.10;
DE   AltName: Full=I-kappa-B kinase 2;
DE            Short=IKK2;
DE   AltName: Full=Nuclear factor NF-kappa-B inhibitor kinase beta;
DE            Short=NFKBIKB;
GN   Name=Ikbkb; Synonyms=Ikkb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION BY MEKK1.
RC   STRAIN=C57BL/6; TISSUE=Spleen;
RX   MEDLINE=98188238; PubMed=9520401; DOI=10.1073/pnas.95.7.3537;
RA   Nakano H., Shindo M., Sakon S., Nishinaka S., Mihara M., Yagita H.,
RA   Okumura K.;
RT   "Differential regulation of IkappaB kinase alpha and beta by two
RT   upstream kinases, NF-kappaB-inducing kinase and mitogen-activated
RT   protein kinase/ERK kinase kinase-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:3537-3542(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Hu M.C.-T., Wang Y.-P., Mikhail A., Qiu W.R.;
RT   "Murine IkB kinase-B, a developmentally regulated protein kinase that
RT   constitutively phosphorylates serine residues of IkB.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   DEVELOPMENTAL STAGE.
RX   MEDLINE=99455228; PubMed=10523828; DOI=10.1038/sj.onc.1202740;
RA   Hu M.C.-T., Wang Y.-P., Qiu W.R., Mikhail A., Meyer C.F., Tan T.-H.;
RT   "Hematopoietic progenitor kinase-1 (HPK1) stress response signaling
RT   pathway activates IkappaB kinases (IKK-alpha/beta) and IKK-beta is a
RT   developmentally regulated protein kinase.";
RL   Oncogene 18:5514-5524(1999).
RN   [4]
RP   IKK PHOSPHORYLATION.
RX   MEDLINE=99038238; PubMed=9819420;
RA   Nemoto S., DiDonato J.A., Lin A.;
RT   "Coordinate regulation of IkappaB kinases by mitogen-activated protein
RT   kinase kinase kinase 1 and NF-kappaB-inducing kinase.";
RL   Mol. Cell. Biol. 18:7336-7343(1998).
RN   [5]
RP   REVIEW.
RX   MEDLINE=20178139; PubMed=10712233;
RA   Jobin C., Sartor R.B.;
RT   "The I kappa B/NF-kappa B system: a key determinant of mucosal
RT   inflammation and protection.";
RL   Am. J. Physiol. 278:C451-C462(2000).
RN   [6]
RP   INTERACTION WITH TERF2IP.
RX   PubMed=20622870; DOI=10.1038/ncb2080;
RA   Teo H., Ghosh S., Luesch H., Ghosh A., Wong E.T., Malik N., Orth A.,
RA   de Jesus P., Perry A.S., Oliver J.D., Tran N.L., Speiser L.J.,
RA   Wong M., Saez E., Schultz P., Chanda S.K., Verma I.M., Tergaonkar V.;
RT   "Telomere-independent Rap1 is an IKK adaptor and regulates NF-kappaB-
RT   dependent gene expression.";
RL   Nat. Cell Biol. 12:758-767(2010).
CC   -!- FUNCTION: Acts as part of the IKK complex in the conventional
CC       pathway of NF-kappa-B activation and phosphorylates inhibitors of
CC       NF-kappa-B thus leading to the dissociation of the inhibitor/NF-
CC       kappa-B complex and ultimately the degradation of the inhibitor.
CC       Also phosphorylates NCOA3 (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + [I-kappa-B protein] = ADP + [I-kappa-B
CC       phosphoprotein].
CC   -!- SUBUNIT: Component of the I-kappa-B-kinase (IKK) core complex
CC       consisting of CHUK, IKBKB and IKBKG; probably four alpha/CHUK-
CC       beta/IKBKB dimers are associated with four gamma/IKBKG subunits.
CC       The IKK core complex seems to associate with regulatory or adapter
CC       proteins to form a IKK-signalosome holo-complex. The IKK complex
CC       associates with TERF2IP/RAP1, leading to promote IKK-mediated
CC       phosphorylation of RELA/p65. Part of a complex composed of NCOA2,
CC       NCOA3, CHUK/IKKA, IKBKB, IKBKG and CREBBP. Part of a 70-90 kDa
CC       complex at least consisting of CHUK/IKKA, IKBKB, NFKBIA, RELA,
CC       IKBKAP and MAP3K14. Found in a membrane raft complex, at least
CC       composed of BCL10, CARD11, DPP4 and IKBKB. Interacts with SQSTM1
CC       through PRKCZ or PRKCI. Forms an NGF-induced complex with IKBKB,
CC       PRKCI and TRAF6. May interact with MAVS/IPS1. Interacts with
CC       NALP2. Interacts with TICAM1. Interacts with FAF1; the interaction
CC       disrupts the IKK complex formation. Interacts with ATM. Part of a
CC       ternary complex consisting of TANK, IKBKB and IKBKG. Interacts
CC       with NIBP; the interaction is direct. Interacts with ARRB1 and
CC       ARRB2. Interacts with TRIM21 (By similarity). Interacts with
CC       NLRC5; prevents IKBKB phosphorylation and kinase activity (By
CC       similarity).
CC   -!- INTERACTION:
CC       Self; NbExp=1; IntAct=EBI-447960, EBI-447960;
CC       Q91VK1:Bzw2; NbExp=2; IntAct=EBI-447960, EBI-646202;
CC       P68040:Gnb2l1; NbExp=3; IntAct=EBI-447960, EBI-296749;
CC       P70434:Irf7; NbExp=1; IntAct=EBI-447960, EBI-997907;
CC       P53349:Map3k1; NbExp=1; IntAct=EBI-447960, EBI-447913;
CC       P25963:NFKBIA (xeno); NbExp=1; IntAct=EBI-447960, EBI-307386;
CC       O09044:Snap23; NbExp=1; IntAct=EBI-447960, EBI-1812522;
CC       Q9WV80:Snx1; NbExp=2; IntAct=EBI-447960, EBI-646356;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane raft (By similarity).
CC       Note=Colocalized with DPP4 in membrane rafts (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in liver, kidney and spleen.
CC   -!- DEVELOPMENTAL STAGE: While it is expressed ubiquitously throughout
CC       the mouse embryo, at E9.5 day its expression begins to be
CC       localized to the brain, neural ganglia, neural tube, and in liver
CC       at E12.5 day. At E15.5 day, the expression is further restricted
CC       to specific tissues of the embryo.
CC   -!- PTM: Upon cytokine stimulation, phosphorylated on Ser-177 and Ser-
CC       181; which enhances activity. Once activated, autophosphorylates
CC       on the C-terminal serine cluster; which decreases activity and
CC       prevents prolonged activation of the inflammatory response (By
CC       similarity).
CC   -!- PTM: Acetylation of Thr-180 by Yersinia yopJ prevents
CC       phosphorylation and activation, thus blocking the I-kappa-B
CC       pathway (By similarity).
CC   -!- PTM: Ubiquitinated. Monoubiquitination involves TRIM21 that leads
CC       to inhibition of Tax-induced NF-kappa-B signaling. 'Ser-163' may
CC       not serve as a monoubiquitination site. Ubiquitination on 'Ser-
CC       163' may modulate phosphorylation on C-terminal serine residues.
CC       Monoubiquitination by TRIM21 is dirupted by Yersinia yopJ (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. I-kappa-B kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF026524; AAC23557.1; -; mRNA.
DR   EMBL; AF088910; AAD52095.1; -; mRNA.
DR   IPI; IPI00130038; -.
DR   RefSeq; NP_034676.1; NM_010546.2.
DR   UniGene; Mm.277886; -.
DR   ProteinModelPortal; O88351; -.
DR   SMR; O88351; 13-302, 703-743.
DR   DIP; DIP-29813N; -.
DR   IntAct; O88351; 30.
DR   MINT; MINT-135217; -.
DR   STRING; O88351; -.
DR   PhosphoSite; O88351; -.
DR   PRIDE; O88351; -.
DR   Ensembl; ENSMUST00000033939; ENSMUSP00000033939; ENSMUSG00000031537.
DR   GeneID; 16150; -.
DR   KEGG; mmu:16150; -.
DR   CTD; 16150; -.
DR   MGI; MGI:1338071; Ikbkb.
DR   eggNOG; roNOG10717; -.
DR   HOGENOM; HBG358635; -.
DR   HOVERGEN; HBG018241; -.
DR   InParanoid; O88351; -.
DR   OrthoDB; EOG4PK276; -.
DR   BRENDA; 2.7.11.10; 244.
DR   NextBio; 288941; -.
DR   ArrayExpress; O88351; -.
DR   Bgee; O88351; -.
DR   CleanEx; MM_IKBKB; -.
DR   Genevestigator; O88351; -.
DR   GermOnline; ENSMUSG00000031537; Mus musculus.
DR   GO; GO:0035631; C:CD40 receptor complex; IDA:BHF-UCL.
DR   GO; GO:0009898; C:internal side of plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0008384; F:IkappaB kinase activity; IEA:EC.
DR   GO; GO:0004702; F:receptor signaling protein serine/threonine kinase activity; TAS:MGI.
DR   GO; GO:0001782; P:B cell homeostasis; IMP:MGI.
DR   GO; GO:0007252; P:I-kappaB phosphorylation; TAS:MGI.
DR   InterPro; IPR022007; IKKbetaNEMObind.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   Pfam; PF12179; IKKbetaNEMObind; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase;
KW   Ubl conjugation.
FT   CHAIN         1    757       Inhibitor of nuclear factor kappa-B
FT                                kinase subunit beta.
FT                                /FTId=PRO_0000086014.
FT   DOMAIN       15    300       Protein kinase.
FT   DOMAIN      458    479       Leucine-zipper.
FT   NP_BIND      21     29       ATP (By similarity).
FT   REGION      737    742       NEMO-binding.
FT   ACT_SITE    145    145       Proton acceptor (By similarity).
FT   BINDING      44     44       ATP (By similarity).
FT   MOD_RES      23     23       Phosphothreonine (By similarity).
FT   MOD_RES     177    177       Phosphoserine (By similarity).
FT   MOD_RES     181    181       Phosphoserine (By similarity).
FT   MOD_RES     670    670       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     672    672       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     675    675       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     682    682       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     689    689       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     692    692       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     697    697       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     705    705       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     733    733       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     740    740       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   CONFLICT     56     56       N -> D (in Ref. 2; AAD52095).
FT   CONFLICT    343    343       N -> D (in Ref. 2; AAD52095).
FT   CONFLICT    356    356       K -> E (in Ref. 2; AAD52095).
FT   CONFLICT    390    390       L -> F (in Ref. 2; AAD52095).
FT   CONFLICT    406    406       P -> Q (in Ref. 2; AAD52095).
FT   CONFLICT    573    573       K -> R (in Ref. 2; AAD52095).
FT   CONFLICT    736    757       TLDWSWLQMEDEERCSLEQACD -> VTA (in Ref.
FT                                2).
SQ   SEQUENCE   757 AA;  86690 MW;  FED962F095449C5E CRC64;
     MSWSPSLPTQ TCGAWEMKER LGTGGFGNVI RWHNQATGEQ IAIKQCRQEL SPKNRNRWCL
     EIQIMRRLNH PNVVAARDVP EGMQNLAPND LPLLAMEYCQ GGDLRRYLNQ FENCCGLREG
     AVLTLLSDIA SALRYLHENR IIHRDLKPEN IVLQQGEKRL IHKIIDLGYA KELDQGSLCT
     SFVGTLQYLA PELLEQQKYT VTVDYWSFGT LAFECITGFR PFLPNWQPVQ WHSKVRQKSE
     VDIVVSEDLN GAVKFSSSLP FPNNLNSVLA ERLEKWLQLM LMWHPRQRGT DPQYGPNGCF
     RALDDILNLK LVHVLNMVTG TVHTYPVTED ESLQSLKTRI QENTGILETD QELLQKAGLV
     LLPDKPATQC ISDSKTNEGL TLDMDLVFLL DNSKINYETQ ITPRPPPESV SCILQEPKRN
     LSFFQLRKVW GQVWHSIQTL KEDCNRLQQG QRAAMMSLLR NNSCLSKMKN AMASTAQQLK
     AKLDFFKTSI QIDLEKYKEQ TEFGITSDKL LLAWREMEQA VEQCGRENDV KHLVERMMAL
     QTDIVDLQRS PMGRKQGGTL DDLEEQAREL YRKLREKPRD QRTEGDSQEM VRLLLQAIQS
     FEKKVRVIYT QLSKTVVCKQ KALELLPKVE EVVSLMNEDE RTVVRLQEKR QKELWNLLKI
     ACSKVRGPVS GSPDSMNVSR LSHPGQLMSQ PSSACDSLPE SDKKSEELVA EAHALCSRLE
     SALQDTVKEQ DRSFTTLDWS WLQMEDEERC SLEQACD
//
ID   CAC1H_MOUSE             Reviewed;        2365 AA.
AC   O88427; B2RQQ0; Q80TJ2; Q9JKU5;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2002, sequence version 2.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Voltage-dependent T-type calcium channel subunit alpha-1H;
DE   AltName: Full=Voltage-gated calcium channel subunit alpha Cav3.2;
GN   Name=Cacna1h; Synonyms=Kiaa1120;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/c;
RA   Mittman S.;
RT   "Exon organization of mouse Cacna1h.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 900-2365 (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1823-2365.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=98333998; PubMed=9670923;
RA   Cribbs L.L., Lee J.-H., Yang J., Satin J., Zhang Y., Daud A.N.,
RA   Barclay J., Wiliamson M.P., Fox M., Rees M., Perez-Reyes E.;
RT   "Cloning and characterization of alpha1H from human heart, a member of
RT   the T-type Ca2+ channel gene family.";
RL   Circ. Res. 83:103-109(1998).
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the
CC       entry of calcium ions into excitable cells and are also involved
CC       in a variety of calcium-dependent processes, including muscle
CC       contraction, hormone or neurotransmitter release, gene expression,
CC       cell motility, cell division and cell death. The isoform alpha-1H
CC       gives rise to T-type calcium currents. T-type calcium channels
CC       belong to the "low-voltage activated (LVA)" group and are strongly
CC       blocked by nickel and mibefradil. A particularity of this type of
CC       channels is an opening at quite negative potentials, and a
CC       voltage-dependent inactivation. T-type channels serve pacemaking
CC       functions in both central neurons and cardiac nodal cells and
CC       support calcium signaling in secretory cells and vascular smooth
CC       muscle. They may also be involved in the modulation of firing
CC       patterns of neurons which is important for information processing
CC       as well as in cell growth processes.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O88427-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=O88427-2; Sequence=VSP_013675;
CC   -!- DOMAIN: Each of the four internal repeats contains five
CC       hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one
CC       positively charged transmembrane segment (S4). S4 segments
CC       probably represent the voltage-sensor and are characterized by a
CC       series of positively charged amino acids at every third position.
CC   -!- PTM: In response to raising of intracellular calcium, the T-type
CC       channels are activated by CaM-kinase II.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family. CACNA1H subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF226868; AAK21607.2; -; Genomic_DNA.
DR   EMBL; AY026385; AAK21607.2; JOINED; Genomic_DNA.
DR   EMBL; BC138026; AAI38027.1; -; mRNA.
DR   EMBL; AK122452; BAC65734.1; -; mRNA.
DR   EMBL; AF051947; AAC67240.1; -; mRNA.
DR   IPI; IPI00130878; -.
DR   IPI; IPI00556756; -.
DR   UniGene; Mm.268378; -.
DR   UniGene; Mm.447208; -.
DR   ProteinModelPortal; O88427; -.
DR   STRING; O88427; -.
DR   PhosphoSite; O88427; -.
DR   PRIDE; O88427; -.
DR   Ensembl; ENSMUST00000078496; ENSMUSP00000077586; ENSMUSG00000024112.
DR   Ensembl; ENSMUST00000092775; ENSMUSP00000090450; ENSMUSG00000024112.
DR   UCSC; uc008bav.1; mouse.
DR   MGI; MGI:1928842; Cacna1h.
DR   eggNOG; roNOG07873; -.
DR   HOGENOM; HBG445131; -.
DR   HOVERGEN; HBG050764; -.
DR   InParanoid; O88427; -.
DR   OrthoDB; EOG4W3SM3; -.
DR   ArrayExpress; O88427; -.
DR   Bgee; O88427; -.
DR   Genevestigator; O88427; -.
DR   GermOnline; ENSMUSG00000024112; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; EXP:Reactome.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR005445; VDCC_T_a1su.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR01629; TVDCCALPHA1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW   Glycoprotein; Ion transport; Ionic channel; Membrane; Phosphoprotein;
KW   Repeat; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN         1   2365       Voltage-dependent T-type calcium channel
FT                                subunit alpha-1H.
FT                                /FTId=PRO_0000053955.
FT   TOPO_DOM      1    100       Cytoplasmic (Potential).
FT   TRANSMEM    101    119       Helical; Name=S1 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    120    139       Extracellular (Potential).
FT   TRANSMEM    140    160       Helical; Name=S2 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    161    169       Cytoplasmic (Potential).
FT   TRANSMEM    170    184       Helical; Name=S3 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    185    193       Extracellular (Potential).
FT   TRANSMEM    194    212       Helical; Name=S4 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    213    232       Cytoplasmic (Potential).
FT   TRANSMEM    233    253       Helical; Name=S5 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    254    394       Extracellular (Potential).
FT   TRANSMEM    395    419       Helical; Name=S6 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    420    790       Cytoplasmic (Potential).
FT   TRANSMEM    791    811       Helical; Name=S1 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    812    824       Extracellular (Potential).
FT   TRANSMEM    825    846       Helical; Name=S2 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    847    852       Cytoplasmic (Potential).
FT   TRANSMEM    853    871       Helical; Name=S3 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    872    879       Extracellular (Potential).
FT   TRANSMEM    880    903       Helical; Name=S4 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    904    914       Cytoplasmic (Potential).
FT   TRANSMEM    915    935       Helical; Name=S5 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    936    987       Extracellular (Potential).
FT   TRANSMEM    988   1012       Helical; Name=S6 of repeat II;
FT                                (Potential).
FT   TOPO_DOM   1013   1301       Cytoplasmic (Potential).
FT   TRANSMEM   1302   1324       Helical; Name=S1 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1325   1342       Extracellular (Potential).
FT   TRANSMEM   1343   1363       Helical; Name=S2 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1364   1373       Cytoplasmic (Potential).
FT   TRANSMEM   1374   1393       Helical; Name=S3 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1394   1407       Extracellular (Potential).
FT   TRANSMEM   1408   1429       Helical; Name=S4 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1430   1439       Cytoplasmic (Potential).
FT   TRANSMEM   1440   1463       Helical; Name=S5 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1464   1540       Extracellular (Potential).
FT   TRANSMEM   1541   1566       Helical; Name=S6 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1567   1627       Cytoplasmic (Potential).
FT   TRANSMEM   1628   1648       Helical; Name=S1 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1649   1662       Extracellular (Potential).
FT   TRANSMEM   1663   1684       Helical; Name=S2 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1685   1691       Cytoplasmic (Potential).
FT   TRANSMEM   1692   1710       Helical; Name=S3 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1711   1724       Extracellular (Potential).
FT   TRANSMEM   1725   1748       Helical; Name=S4 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1749   1762       Cytoplasmic (Potential).
FT   TRANSMEM   1763   1783       Helical; Name=S5 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1784   1846       Extracellular (Potential).
FT   TRANSMEM   1847   1874       Helical; Name=S6 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1875   2365       Cytoplasmic (Potential).
FT   REPEAT       87    422       I.
FT   REPEAT      776   1015       II.
FT   REPEAT     1292   1569       III.
FT   REPEAT     1613   1874       IV.
FT   COMPBIAS    521    531       Poly-His.
FT   COMPBIAS   1594   1597       Poly-Arg.
FT   SITE        378    378       Calcium ion selectivity and permeability
FT                                (By similarity).
FT   SITE        971    971       Calcium ion selectivity and permeability
FT                                (By similarity).
FT   SITE       1515   1515       Calcium ion selectivity and permeability
FT                                (By similarity).
FT   SITE       1819   1819       Calcium ion selectivity and permeability
FT                                (By similarity).
FT   MOD_RES     780    780       Phosphoserine (By similarity).
FT   MOD_RES    1196   1196       Phosphothreonine (By similarity).
FT   CARBOHYD    192    192       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    271    271       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1477   1477       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ    1598   1604       STFPNPE -> K (in isoform 2).
FT                                /FTId=VSP_013675.
FT   CONFLICT   1823   1825       GIM -> ARG (in Ref. 4; AAC67240).
FT   CONFLICT   1914   1914       D -> E (in Ref. 4; AAC67240).
FT   CONFLICT   1945   1947       APA -> LLQ (in Ref. 4; AAC67240).
FT   CONFLICT   1952   1952       S -> A (in Ref. 4; AAC67240).
FT   CONFLICT   1953   2351       Missing (in Ref. 4; AAC67240).
SQ   SEQUENCE   2365 AA;  261946 MW;  9A8A17570C210596 CRC64;
     MTEGTLAADE VRVPLGASPS APAAPVRASP ASPGVPGREE QRGSGSSVLA PESPGTECGA
     DLGADEEQPV PYPALAATVF FCLGQTTRPR SWCLRLVCNP WFEHISMLVI MLNCVTLGMF
     RPCEDVECRS ERCSILEAFD DFIFAFFAVE MVIKMVALGL FGQKCYLGDT WNRLDFFIVM
     AGMMEYSLDG HNVSLSAIRT VRVLRPLRAI NRVPSMRILV TLLLDTLPML GNVLLLCFFV
     FFIFGIVGVQ LWAGLLRNRC FLDSAFVRNN NLTFLRPYYQ TEEGEENPFI CSSRRDNGMQ
     KCSHIPSRRE LRVQCTLGWE AYGQPQAEDG GAGRNACINW NQYYNVCRSG EFNPHNGAIN
     FDNIGYAWIA IFQVITLEGW VDIMYYVMDA HSFYNFIYFI LLIIVGSFFM INLCLVVIAT
     QFSETKQREN QLMREQRARY LSNDSTLASF SEPGSCYEEL LKYVGHIFRK VKRRSLRLYA
     RWQSRWRKKV DPSSTLHGQG PRRRPRRAGR RTASVHHLVY HHHHHHHHHY HFSHGGPRRP
     SPEPGAGDTR LVRACVPPSP PSPGHGPPDS ESVHSIYHAD CHVEGPQERA RVAHTIATAA
     SLKLASGLGT MNYPTILPSG AVNSKGSTSS RPKGLRSAGT PGATAHSPLS LGSPSPYEKI
     QHVVGEQGLG RASSHLSGLS VPCPLPSPQA GTLTCELKSC PYCASALEDP EFEFSGSESG
     DSDAHGVYEF TQDVRHGDCR DPVQQPHEGG TPGHGNERWR PPLRTASQPG GLGRLWASFS
     SKLRRIVDSK YFNRGIMAAI LVNTLSMGVE YHEQPDELTN ALEISNIVFT SMFALEMLLK
     LLACGPLGYI RNPYNIFDGI VVVISVWEIV GQADGGLSVL RTFRLLRVLK LVRFLPALRR
     QLVVLMRTMD NVATFCMLLM LFIFIFSILG MHLFGCKFSL KTDSGDTVPD RKNFDSLLWA
     IVTVFQILTQ EDWNVVLYNG MASTSSWAAL YFVALMTFGN YVLFNLLVAI LVEGFQAEGD
     ATRSDTDEDK TSTHLEEDFD KLRDVRATEM KMYSLAVTPN GHLEGRGSLP PPLITHTAAT
     PMPTPKSSPH LDMAHTLLDS RRSSSGSVDP QLGDQKSLAS LRSSPCAPWG PNSAGSSRRS
     SWNSLGRAPS LKRRSQCGER ESLLSGEGKG STDDEAEDSR PNSGTHPGAS PGPRATPLRR
     AESLGHRSTM DLCPPRPATL LPTKFRDCNG QMVALPSEFF LRIDSHKEDA AEFDDDIEDS
     CCFRLHKVLE PYAPQWCSSR ESWALYLFPP QNRLRVSCQK VIAHKMFDHV VLVFIFLNCI
     TIALERPDID PGSTERAFLS VSNYIFTAIF VVEMMVKVVA LGLLWGEHAY LQSSWNVLDG
     LLVLVSLVDI IVAVASAGGA KILGVLRVLR LLRTLRPLRV ISRAPGLKLV VETLISSLRP
     IGNIVLICCA FFIIFGILGV QLFKGKFYYC EGTDTRNITT KAECHAAHYR WVRRKYNFDN
     LGQALMSLFV LSSKDGWVNI MYDGLDAVGI DQQPVQNHNP WMLLYFISFL LIVSFFVLNM
     FVGVVVENFH KCRQHQEAEE ARRREEKRLR RLERRRRSTF PNPEAQRRPY YADYSHTRRS
     IHSLCTSHYL DLFITFIICL NVITMSMEHY NQPKSLDEAL KYCNYVFTIV FVFEAALKLV
     AFGFRRFFKD RWNQLDLAIV LLSIMGIALE EIEMNAALPI NPTIIRIMRV LRIARVLKLL
     KMATGMRALL DTVVQALPQV GNLGLLFMLL FFIYAALGVE LFGRLECSED NPCEGLSRHA
     TFTNFGMAFL TLFRVSTGDN WNGIMKDTLR ECTREDKHCL SYLPALSPVY FVTFVLVAQF
     VLVNVVVAVL MKHLEESNKE AREDAEMDAE IELEIAQGST AQPPSTAQES QGTDPDTPNL
     LVVRKVSVSR MLSLPNDSYM FRPVAPAAAP HSHPLQEVEM ETYTGPVTSA HSPSLEPRTS
     FQVPSAASSP ARASDPLCAL SPRDTPRSLS LSRILYRQEA MHAESLEGQI DDAGEDGIPD
     YTEPAENISM SQAPLGTLRS PPCSPRPASV RTRKHTFGQH CISSRPPTLG GDDAEAADPA
     DEEVSHITSS AHPWPATEPH SPEASPTASP AKGTVGSGRD PHRFCSVDAQ SFLDKPGRPD
     AQRWSSVELD NGDGHLESGE VRARASELEP ALGARRKKKM SPPCISIDPP TEDEGSSRPP
     AAEGGNTTLR RRTPSCEAAL HRDCPESTEG PGTGGDPVAK GERWGQASCR AEHLTVPNFA
     FEPLDMGGPG GDCFLDSDQS VTPEPRVSSL GAIVPLILET ELSMPSGDPP EKEQGLYLTV
     PQTPLKKPGS PPATPAPDDS GDEPV
//
ID   MTX2_MOUSE              Reviewed;         263 AA.
AC   O88441; Q3TFR2;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Metaxin-2;
DE   AltName: Full=Mitochondrial outer membrane import complex protein 2;
GN   Name=Mtx2; ORFNames=MNCb-0780;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MTX1, SUBCELLULAR
RP   LOCATION, AND FUNCTION.
RX   MEDLINE=99308987; PubMed=10381257;
RX   DOI=10.1002/(SICI)1097-4644(19990701)74:1<11::AID-JCB2>3.3.CO;2-M;
RA   Armstrong L.C., Saenz A.J., Bornstein P.;
RT   "Metaxin 1 interacts with metaxin 2, a novel related protein
RT   associated with the mammalian mitochondrial outer membrane.";
RL   J. Cell. Biochem. 74:11-22(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S.,
RA   Hashimoto K.;
RT   "Isolation of full-length cDNA clones from mouse brain cDNA library
RT   made by oligo-capping method.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, C57BL/6J, and NOD; TISSUE=Kidney, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Involved in transport of proteins into the
CC       mitochondrion.
CC   -!- SUBUNIT: Interacts with MTX1/metaxin-1.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane.
CC   -!- SIMILARITY: Belongs to the metaxin family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF053550; AAC25104.1; -; mRNA.
DR   EMBL; AB041562; BAA95046.1; -; mRNA.
DR   EMBL; AK087933; BAC40046.1; -; mRNA.
DR   EMBL; AK168000; BAE39989.1; -; mRNA.
DR   EMBL; AK169048; BAE40836.1; -; mRNA.
DR   EMBL; BC006641; AAH06641.1; -; mRNA.
DR   IPI; IPI00225254; -.
DR   RefSeq; NP_058084.3; NM_016804.4.
DR   UniGene; Mm.292613; -.
DR   UniGene; Mm.478750; -.
DR   ProteinModelPortal; O88441; -.
DR   STRING; O88441; -.
DR   PRIDE; O88441; -.
DR   Ensembl; ENSMUST00000028511; ENSMUSP00000028511; ENSMUSG00000027099.
DR   Ensembl; ENSMUST00000111974; ENSMUSP00000107605; ENSMUSG00000027099.
DR   GeneID; 53375; -.
DR   KEGG; mmu:53375; -.
DR   NMPDR; fig|10090.3.peg.6172; -.
DR   UCSC; uc008kej.1; mouse.
DR   CTD; 53375; -.
DR   MGI; MGI:1859652; Mtx2.
DR   HOGENOM; HBG714138; -.
DR   HOVERGEN; HBG003471; -.
DR   InParanoid; O88441; -.
DR   OrthoDB; EOG408N8V; -.
DR   ArrayExpress; O88441; -.
DR   Bgee; O88441; -.
DR   CleanEx; MM_MTX2; -.
DR   Genevestigator; O88441; -.
DR   GermOnline; ENSMUSG00000027099; Mus musculus.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006626; P:protein targeting to mitochondrion; IEA:InterPro.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR019564; Mt-OM_transp_Tom37/Metaxin.
DR   Gene3D; G3DSA:1.20.1050.10; GST_C_like; 1.
DR   Pfam; PF10568; Tom37; 1.
DR   SUPFAM; SSF47616; GST_C_like; 1.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   Protein transport; Transport.
FT   CHAIN         1    263       Metaxin-2.
FT                                /FTId=PRO_0000220996.
SQ   SEQUENCE   263 AA;  29758 MW;  D77DE08F05DF7C11 CRC64;
     MSLVAEAFVS QIAATEPWPE NATLYQQLRG EQILLSDNAA SLAVQAFLQM CNLPVKVVCR
     ANAEYMSPSG KVPFIHVGNQ VVSELGPIVQ FVKAKGHSLS DGLDEVQKAE MKAYMELVNN
     MLLTAELYLQ WCDEATVGEI TIARYGSPYP WPLNHILAYQ KQWEVKRKMK AIGWGNKTLD
     QVLEDVDQCC QALSQRLGTQ PYFFNKQPTE LDALVFGHLY TILTTQLTSD ELSEKVKNYS
     NLLAFCRRIE QHYFEDWGKG RLS
//
ID   ADCY1_MOUSE             Reviewed;        1118 AA.
AC   O88444; Q5SS89;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 2.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Adenylate cyclase type 1;
DE            EC=4.6.1.1;
DE   AltName: Full=ATP pyrophosphate-lyase 1;
DE   AltName: Full=Adenylate cyclase type I;
DE   AltName: Full=Adenylyl cyclase 1;
DE   AltName: Full=Ca(2+)/calmodulin-activated adenylyl cyclase;
GN   Name=Adcy1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 100-1050.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   MEDLINE=98324784; PubMed=9662407; DOI=10.1038/980;
RA   Abdel-Majid R.M., Leong W.L., Schalkwyk L.C., Smallman D.S.,
RA   Wong S.T., Storm D.R., Fine A., Dobson M.J., Guernsey D.L.,
RA   Neumann P.E.;
RT   "Loss of adenylyl cyclase I activity disrupts patterning of mouse
RT   somatosensory cortex.";
RL   Nat. Genet. 19:289-291(1998).
CC   -!- FUNCTION: This is a calmodulin-sensitive adenylyl cyclase. May be
CC       involved in regulatory processes in the central nervous system. It
CC       may play a role in memory acquisition and learning (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
CC   -!- COFACTOR: Binds 2 magnesium ions per subunit (By similarity).
CC   -!- ENZYME REGULATION: Activated by calcium/calmodulin. Inhibited by
CC       the G protein beta and gamma subunit complex (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
CC       cyclase family.
CC   -!- SIMILARITY: Contains 2 guanylate cyclase domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL669838; CAI25155.1; -; Genomic_DNA.
DR   EMBL; AF053980; AAC29478.1; -; mRNA.
DR   IPI; IPI00130949; -.
DR   RefSeq; NP_033752.1; NM_009622.1.
DR   UniGene; Mm.259733; -.
DR   ProteinModelPortal; O88444; -.
DR   SMR; O88444; 289-476, 859-1053.
DR   STRING; O88444; -.
DR   PhosphoSite; O88444; -.
DR   PRIDE; O88444; -.
DR   Ensembl; ENSMUST00000020706; ENSMUSP00000020706; ENSMUSG00000020431.
DR   GeneID; 432530; -.
DR   KEGG; mmu:432530; -.
DR   UCSC; uc007hzf.1; mouse.
DR   CTD; 432530; -.
DR   MGI; MGI:99677; Adcy1.
DR   eggNOG; roNOG09082; -.
DR   HOGENOM; HBG445220; -.
DR   HOVERGEN; HBG050458; -.
DR   InParanoid; O88444; -.
DR   OMA; KCISSHL; -.
DR   OrthoDB; EOG4TQM8C; -.
DR   PhylomeDB; O88444; -.
DR   BRENDA; 4.6.1.1; 244.
DR   NextBio; 407738; -.
DR   ArrayExpress; O88444; -.
DR   Bgee; O88444; -.
DR   CleanEx; MM_ADCY1; -.
DR   Genevestigator; O88444; -.
DR   GermOnline; ENSMUSG00000020431; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; TAS:MGI.
DR   GO; GO:0004016; F:adenylate cyclase activity; IGI:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:MGI.
DR   GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR   GO; GO:0007616; P:long-term memory; IGI:MGI.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   Gene3D; G3DSA:3.30.70.1230; A/G_cyclase; 2.
DR   Pfam; PF00211; Guanylate_cyc; 2.
DR   SMART; SM00044; CYCc; 2.
DR   SUPFAM; SSF55073; A/G_cyclase; 2.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 2.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Calmodulin-binding; cAMP biosynthesis; Glycoprotein;
KW   Lyase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Repeat;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1   1118       Adenylate cyclase type 1.
FT                                /FTId=PRO_0000195683.
FT   TOPO_DOM      1     62       Cytoplasmic (Potential).
FT   TRANSMEM     63     83       Helical; (Potential).
FT   TRANSMEM     87    107       Helical; (Potential).
FT   TRANSMEM    124    144       Helical; (Potential).
FT   TRANSMEM    157    177       Helical; (Potential).
FT   TRANSMEM    182    202       Helical; (Potential).
FT   TRANSMEM    213    233       Helical; (Potential).
FT   TOPO_DOM    234    609       Cytoplasmic (Potential).
FT   TRANSMEM    610    630       Helical; (Potential).
FT   TRANSMEM    634    654       Helical; (Potential).
FT   TRANSMEM    673    693       Helical; (Potential).
FT   TRANSMEM    724    744       Helical; (Potential).
FT   TRANSMEM    752    772       Helical; (Potential).
FT   TRANSMEM    774    793       Helical; (Potential).
FT   TOPO_DOM    794   1118       Cytoplasmic (Potential).
FT   REGION      492    519       Interaction with calmodulin (By
FT                                similarity).
FT   REGION     1023   1046       Interaction with calmodulin (By
FT                                similarity).
FT   METAL       307    307       Magnesium 1 (By similarity).
FT   METAL       307    307       Magnesium 2 (By similarity).
FT   METAL       308    308       Magnesium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       351    351       Magnesium 1 (By similarity).
FT   METAL       351    351       Magnesium 2 (By similarity).
FT   CARBOHYD    703    703       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    147    155       SSAGGAMGS -> ALQEAQWAR (in Ref. 2;
FT                                AAC29478).
FT   CONFLICT    234    234       T -> A (in Ref. 2; AAC29478).
FT   CONFLICT    270    270       L -> M (in Ref. 2; AAC29478).
FT   CONFLICT    319    319       T -> K (in Ref. 2; AAC29478).
FT   CONFLICT    466    466       R -> K (in Ref. 2; AAC29478).
FT   CONFLICT    523    523       F -> I (in Ref. 2; AAC29478).
FT   CONFLICT    542    542       S -> T (in Ref. 2; AAC29478).
FT   CONFLICT    549    549       S -> T (in Ref. 2; AAC29478).
FT   CONFLICT    570    570       R -> L (in Ref. 2; AAC29478).
FT   CONFLICT    598    598       Q -> R (in Ref. 2; AAC29478).
FT   CONFLICT    692    692       G -> V (in Ref. 2; AAC29478).
FT   CONFLICT    697    697       A -> S (in Ref. 2; AAC29478).
FT   CONFLICT    707    707       V -> L (in Ref. 2; AAC29478).
FT   CONFLICT    713    713       G -> C (in Ref. 2; AAC29478).
FT   CONFLICT    720    721       AL -> GP (in Ref. 2; AAC29478).
FT   CONFLICT    774    776       VGG -> AMGA (in Ref. 2; AAC29478).
FT   CONFLICT    867    869       GVM -> AVL (in Ref. 2; AAC29478).
FT   CONFLICT    938    938       R -> K (in Ref. 2; AAC29478).
FT   CONFLICT    991    991       R -> C (in Ref. 2; AAC29478).
FT   CONFLICT   1020   1020       T -> I (in Ref. 2; AAC29478).
FT   CONFLICT   1030   1030       C -> S (in Ref. 2; AAC29478).
SQ   SEQUENCE   1118 AA;  123373 MW;  CEFAFF3940B22277 CRC64;
     MAGAPRGQGG GGGAGEPGGA ERAAGPGGRR GFRACGEEFA CPELEALFRG YTLRLEQAAT
     LKALAVLSLL AGALALAELL GAPGPAPGLA KGSHPVHCIL FLALFVVTNV RSLQVSQLQQ
     VGQLALFFSL TFALLCCPFA LGGPARSSAG GAMGSTVAEQ GVWQLLLVTF VSYALLPVRS
     LLAIGFGLVV AASHLLVTAA LVPAKRPRLW RTLGANALLF FGVNMYGVFV RILTERSQRK
     AFLQARNCIE DRLRLEDENE KQERLLMSLL PRNVAMEMKE DFLKPPERIF HKIYIQRHDN
     VSILFADIVG FTGLASQCTA QELVKLLNEL FGKFDELATE NHCRRIKILG DCYYCVSGLT
     QPKTDHAHCC VEMGLDMIDT ITSVAEATEV DLNMRVGLHT GRVLCGVLGL RKWQYDVWSN
     DVTLANVMEA AGLPGKVHIT KTTLACLNGD YEVEPGHGHE RNTFLRTHNI ETFFIVPSHR
     RKIFPGLILS DIKPAKRMKF KTVCYLLVQL MHCRKMFKAE IPFSNVMTCE DDDKRRALRT
     ASEKLRNRSS FSTNVVYTTP GTRVNRYISR LLEARQTELE MADLNFFTLK YKHVEREQKY
     HQLQDEYFTS AVVLALILAA LFGLIYLLVI PQSVAVLLLL VFSICFLVAC TLYLHITRVQ
     CFPGCLTIQI RTALCVFIVV LIYSVAQGCV VGCLPWAWSS QSNSSLVVLA AGGRRTVLPA
     LPCESAHHAL LCCLVGTLPL AIFLRVSSLP KMILLSGLTT SYILVLELSG YTKVGGGALS
     GRSYEPIMAI LLFSCTLALH ARQVDVRLRL DYLWAAQAEE ERDDMERVKL DNKRILFNLL
     PAHVAQHFLM SNPRNMDLYY QSYSQVGVMF ASIPNFNDFY IELDGNNMGV ECLRLLNEII
     ADFDELMDKD FYKDLEKIKT IGSTYMAAVG LAPTAGTRAK KSISSHLCTL ADFAIDMFDV
     LDEINYQSYN DFVLRVGINV GPVVAGVIGA RRPQYDIWGN TVNVASRMDS TGVQGRIQVT
     EEVHRLLKRC SYQFVCRGKV SVKGKGEMLT YFLEGRTDGN SSHGRTFRLE RRMCPYGRGG
     GQARRPPLCP AAGPPVRPGL PPAPTSQYLS STAAGKEA
//
ID   DC1I1_MOUSE             Reviewed;         628 AA.
AC   O88485; O88486;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-FEB-2011, entry version 86.
DE   RecName: Full=Cytoplasmic dynein 1 intermediate chain 1;
DE   AltName: Full=Cytoplasmic dynein intermediate chain 1;
DE   AltName: Full=Dynein intermediate chain 1, cytosolic;
DE            Short=DH IC-1;
GN   Name=Dync1i1; Synonyms=Dnci1, Dncic1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 1B).
RX   MEDLINE=99168894; PubMed=10049579; DOI=10.1006/geno.1998.5665;
RA   Crackower M.A., Sinasac D.S., Xia J., Motoyama J., Prochazka M.,
RA   Rommens J.M., Scherer S.W., Tsui L.-C.;
RT   "Cloning and characterization of two cytoplasmic dynein intermediate
RT   chain genes in mouse and human.";
RL   Genomics 55:257-267(1999).
RN   [2]
RP   INTERACTION WITH DYNLL2, AND MUTAGENESIS OF 151-LYS--THR-155.
RX   PubMed=11148209; DOI=10.1074/jbc.M010320200;
RA   Lo K.W., Naisbitt S., Fan J.S., Sheng M., Zhang M.;
RT   "The 8-kDa dynein light chain binds to its targets via a conserved
RT   (K/R)XTQT motif.";
RL   J. Biol. Chem. 276:14059-14066(2001).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-618, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
CC   -!- FUNCTION: Acts as one of several non-catalytic accessory
CC       components of the cytoplasmic dynein 1 complex that are thought to
CC       be involved in linking dynein to cargos and to adapter proteins
CC       that regulate dynein function. Cytoplasmic dynein 1 acts as a
CC       motor for the intracellular retrograde motility of vesicles and
CC       organelles along microtubules. The intermediate chains mediate the
CC       binding of dynein to dynactin via its 150 kDa component (p150-
CC       glued) DCNT1. May play a role in mediating the interaction of
CC       cytoplasmic dynein with membranous organelles and kinetochores.
CC   -!- SUBUNIT: Homodimer (By similarity). The cytoplasmic dynein 1
CC       complex consists of two catalytic heavy chains (HCs) and a number
CC       of non-catalytic subunits presented by intermediate chains (ICs),
CC       light intermediate chains (LICs) and light chains (LCs); the
CC       composition seems to vary in respect to the IC, LIC and LC
CC       composition. The heavy chain homodimer serves as a scaffold for
CC       the probable homodimeric assembly of the respective non-catalytic
CC       subunits. The ICs and LICs bind directly to the HC dimer and the
CC       LCs assemble on the IC dimer. Interacts with DYNC1H1. Interacts
CC       with DYNLT1 and DYNLT3. Interacts with DCNT1 (By similarity).
CC       Interacts with DYNLL2.
CC   -!- INTERACTION:
CC       P06537:Nr3c1; NbExp=2; IntAct=EBI-492834, EBI-492753;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Chromosome,
CC       centromere, kinetochore (By similarity). Cytoplasm, cytoskeleton,
CC       spindle pole (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1A;
CC         IsoId=O88485-1; Sequence=Displayed;
CC       Name=1B;
CC         IsoId=O88485-2; Sequence=VSP_001334;
CC   -!- SIMILARITY: Belongs to the dynein intermediate chain family.
CC   -!- SIMILARITY: Contains 7 WD repeats.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF063229; AAC33444.1; -; mRNA.
DR   EMBL; AF063230; AAC33445.1; -; mRNA.
DR   IPI; IPI00131084; -.
DR   IPI; IPI00226946; -.
DR   UniGene; Mm.20893; -.
DR   ProteinModelPortal; O88485; -.
DR   SMR; O88485; 130-156, 467-510.
DR   IntAct; O88485; 3.
DR   MINT; MINT-3088793; -.
DR   STRING; O88485; -.
DR   PhosphoSite; O88485; -.
DR   PRIDE; O88485; -.
DR   Ensembl; ENSMUST00000031771; ENSMUSP00000031771; ENSMUSG00000029757.
DR   Ensembl; ENSMUST00000115558; ENSMUSP00000111220; ENSMUSG00000029757.
DR   Ensembl; ENSMUST00000115559; ENSMUSP00000111221; ENSMUSG00000029757.
DR   UCSC; uc009awm.1; mouse.
DR   UCSC; uc009awn.1; mouse.
DR   MGI; MGI:107743; Dync1i1.
DR   eggNOG; roNOG08443; -.
DR   GeneTree; ENSGT00550000074241; -.
DR   HOVERGEN; HBG004083; -.
DR   ArrayExpress; O88485; -.
DR   Bgee; O88485; -.
DR   CleanEx; MM_DYNC1I1; -.
DR   Genevestigator; O88485; -.
DR   GermOnline; ENSMUSG00000029757; Mus musculus.
DR   GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
DR   GO; GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC.
DR   GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; ISS:HGNC.
DR   GO; GO:0003777; F:microtubule motor activity; ISS:HGNC.
DR   GO; GO:0047496; P:vesicle transport along microtubule; ISS:HGNC.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW   Dynein; Kinetochore; Microtubule; Motor protein; Phosphoprotein;
KW   Repeat; Transport; WD repeat.
FT   CHAIN         1    628       Cytoplasmic dynein 1 intermediate chain
FT                                1.
FT                                /FTId=PRO_0000114653.
FT   REPEAT      268    317       WD 1.
FT   REPEAT      321    361       WD 2.
FT   REPEAT      370    411       WD 3.
FT   REPEAT      420    460       WD 4.
FT   REPEAT      465    510       WD 5.
FT   REPEAT      513    553       WD 6.
FT   REPEAT      559    598       WD 7.
FT   MOD_RES     618    618       Phosphoserine.
FT   VAR_SEQ     106    125       Missing (in isoform 1B).
FT                                /FTId=VSP_001334.
FT   MUTAGEN     151    155       Missing: Abolishes interaction with
FT                                DYNLL2.
FT   MUTAGEN     153    153       T->A: Impairs interaction with DYNLL2.
FT   MUTAGEN     153    153       T->G: Abolishes interaction with DYNLL2.
FT   MUTAGEN     154    154       Q->A: Abolishes interaction with DYNLL2.
FT   MUTAGEN     155    155       T->G: Abolishes interaction with DYNLL2.
FT   MUTAGEN     155    155       T->S: Impairs interaction with DYNLL2.
SQ   SEQUENCE   628 AA;  70679 MW;  3C29AF6DA3467FD6 CRC64;
     MSDKSDLKAE LERKKQRLAQ IREEKKRKEE ERKKKEADMQ QKKEPVQDDS DLDRKRRETE
     ALLQSIGISP EPPLVPTPMS PSSKSVSTPS DAGSQDSGDL GPLTRTLQWD TDPSVLQLQS
     DSELGRRLHK LGVSKVTQVD FLPREVVSYS KETQTPLATH QSEEDEEDEE MVEPKIGHDS
     ELENQEKKQE TKEAPPRELT EEEKQQILHS EEFLIFFDRT IRVIERALAE DSDIFFDYSG
     RELEEKDGDV QAGANLSFNR QFYDEHWSKH RVVTCMDWSL QYPELMVASY SNNEDAPHEP
     DGVALVWNMK FKKTTPEYVF HCQSSVMSVC FARFHPNLVV GGTYSGQIVL WDNRSHRRTP
     VQRTPLSAAA HTHPVYCVNV VGTHNARNLI TVSTDGKMCS WSLDMLSTPQ ESMELVYNKS
     KPVAVTGMAF PTGDVNNFVV GSEEGTVYTA CRHGSKAGIG EVFEGHQGPV TGINCHMAVG
     PIDFSHLFVT SSFDWTVKLW TTKHNKPVYS SEDNADYVYD VMWSPVHPAL FACVDGMGRL
     DLWNLNSDTE VPTASVAIEG ASALNRVRWA QGGKEVAVGD SEGRIWIYDV GELAVPHNDE
     WTRFARTLVE IRANRADSEE EGAVELAA
//
ID   DC1I2_MOUSE             Reviewed;         612 AA.
AC   O88487; Q3TGH7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Cytoplasmic dynein 1 intermediate chain 2;
DE   AltName: Full=Cytoplasmic dynein intermediate chain 2;
DE   AltName: Full=Dynein intermediate chain 2, cytosolic;
DE            Short=DH IC-2;
GN   Name=Dync1i2; Synonyms=Dnci2, Dncic2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99168894; PubMed=10049579; DOI=10.1006/geno.1998.5665;
RA   Crackower M.A., Sinasac D.S., Xia J., Motoyama J., Prochazka M.,
RA   Rommens J.M., Scherer S.W., Tsui L.-C.;
RT   "Cloning and characterization of two cytoplasmic dynein intermediate
RT   chain genes in mouse and human.";
RL   Genomics 55:257-267(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Eye, Heart, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Acts as one of several non-catalytic accessory
CC       components of the cytoplasmic dynein 1 complex that are thought to
CC       be involved in linking dynein to cargos and to adapter proteins
CC       that regulate dynein function. Cytoplasmic dynein 1 acts as a
CC       motor for the intracellular retrograde motility of vesicles and
CC       organelles along microtubules. The intermediate chains mediate the
CC       binding of dynein to dynactin via its 150 kDa component (p150-
CC       glued) DCNT1. Involved in membrane-transport, such as Golgi
CC       apparatus, late endosomes and lysosomes (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity). The cytoplasmic dynein 1
CC       complex consists of two catalytic heavy chains (HCs) and a number
CC       of non-catalytic subunits presented by intermediate chains (ICs),
CC       light intermediate chains (LICs) and light chains (LCs); the
CC       composition seems to vary in respect to the IC, LIC and LC
CC       composition. The heavy chain homodimer serves as a scaffold for
CC       the probable homodimeric assembly of the respective non-catalytic
CC       subunits. The ICs and LICs bind directly to the HC dimer and the
CC       LCs assemble on the IC dimer. Interacts with DYNLT1 and DYNLT3.
CC       Interacts with DCNT1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. The
CC       phosphorylation status of Ser-84 appears to be involved in
CC       dynactin-dependent target binding (By similarity).
CC   -!- SIMILARITY: Belongs to the dynein intermediate chain family.
CC   -!- SIMILARITY: Contains 7 WD repeats.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF063231; AAC33446.1; -; mRNA.
DR   EMBL; AK088015; BAC40097.1; -; mRNA.
DR   EMBL; AK164437; BAE37788.1; -; mRNA.
DR   EMBL; AK168730; BAE40571.1; -; mRNA.
DR   IPI; IPI00131086; -.
DR   RefSeq; NP_001185805.1; NM_001198876.1.
DR   RefSeq; NP_034194.1; NM_010064.4.
DR   UniGene; Mm.249479; -.
DR   ProteinModelPortal; O88487; -.
DR   SMR; O88487; 110-138, 308-385, 442-576.
DR   STRING; O88487; -.
DR   PhosphoSite; O88487; -.
DR   REPRODUCTION-2DPAGE; O88487; -.
DR   PRIDE; O88487; -.
DR   Ensembl; ENSMUST00000081710; ENSMUSP00000080410; ENSMUSG00000027012.
DR   Ensembl; ENSMUST00000112138; ENSMUSP00000107766; ENSMUSG00000027012.
DR   GeneID; 13427; -.
DR   KEGG; mmu:13427; -.
DR   UCSC; uc008kai.1; mouse.
DR   CTD; 13427; -.
DR   MGI; MGI:107750; Dync1i2.
DR   HOVERGEN; HBG004083; -.
DR   OrthoDB; EOG4RBQJ5; -.
DR   PhylomeDB; O88487; -.
DR   NextBio; 283847; -.
DR   ArrayExpress; O88487; -.
DR   Bgee; O88487; -.
DR   CleanEx; MM_DYNC1I2; -.
DR   Genevestigator; O88487; -.
DR   GermOnline; ENSMUSG00000027012; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:motor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 2.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Dynein; Microtubule; Motor protein;
KW   Phosphoprotein; Repeat; Transport; WD repeat.
FT   CHAIN         1    612       Cytoplasmic dynein 1 intermediate chain
FT                                2.
FT                                /FTId=PRO_0000114656.
FT   REPEAT      251    300       WD 1.
FT   REPEAT      304    344       WD 2.
FT   REPEAT      353    394       WD 3.
FT   REPEAT      403    443       WD 4.
FT   REPEAT      448    493       WD 5.
FT   REPEAT      496    536       WD 6.
FT   REPEAT      542    581       WD 7.
FT   MOD_RES      81     81       Phosphoserine (By similarity).
FT   MOD_RES      84     84       Phosphoserine (By similarity).
FT   MOD_RES      86     86       Phosphoserine (By similarity).
FT   MOD_RES      88     88       Phosphoserine (By similarity).
FT   MOD_RES      89     89       Phosphothreonine (By similarity).
FT   MOD_RES      91     91       Phosphoserine (By similarity).
FT   MOD_RES      95     95       Phosphoserine (By similarity).
FT   MOD_RES      98     98       Phosphoserine (By similarity).
FT   MOD_RES     136    136       Phosphothreonine (By similarity).
SQ   SEQUENCE   612 AA;  68394 MW;  1D14CEECF62A5E33 CRC64;
     MSDKSDLKAE LERKKQRLAQ IREEKKRKEE ERKKKETDQK KEAAVSVQEE SDLEKKRREA
     EALLQSMGLT TDSPIVPPPM SPSSKSVSTP SEAGSQDSGD GAVGSRRGPI KLGMAKITQV
     DFPPREIVTY TKETQTPVTA QPKEDEEEED DVATPKPPVE PEEEKTLKKD EENDSKAPPH
     ELTEEEKQQI LHSEEFLSFF DHSTRIVERA LSEQINIFFD YSGRDLEDKE GEIQAGAKLS
     LNRQFFDERW SKHRVVSCLD WSSQYPELLV ASYNNNEEAP HEPDGVALVW NMKYKKTTPE
     YVFHCQSAVM SATFAKFHPN LVVGGTYSGQ IVLWDNRSNK RTPVQRTPLS AAAHTHPVYC
     VNVVGTQNAH NLISISTDGK ICSWSLDMLS HPQDSMELVH KQSKAVAVTS MSFPVGDVNN
     FVVGSEEGSV YTACRHGSKA GISEMFEGHQ GPITGIHCHA AVGAVDFSHL FVTSSFDWTV
     KLWTTKNNKP LYSFEDNSDY VYDVMWSPTH PALFACVDGM GRLDLWNLNN DTEVPTASIS
     VEGNPALNRV RWTHSGREIA VGDSEGQIVI YDVGEQIAVP RNDEWARFGR TLAEINANRA
     DAEEEAATRI PA
//
ID   NSD1_MOUSE              Reviewed;        2588 AA.
AC   O88491; Q8C480; Q9CT70;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific;
DE            EC=2.1.1.43;
DE   AltName: Full=H3-K36-HMTase;
DE   AltName: Full=H4-K20-HMTase;
DE   AltName: Full=Nuclear receptor-binding SET domain-containing protein 1;
DE            Short=NR-binding SET domain-containing protein;
GN   Name=Nsd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RARA; THRA;
RP   RXRA AND ESRRA, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-803;
RP   804-SER-THR-805 AND 806-LEU-LEU-807.
RC   TISSUE=Embryo;
RX   MEDLINE=98292459; PubMed=9628876; DOI=10.1093/emboj/17.12.3398;
RA   Huang N., vom Baur E., Garnier J.-M., Lerouge T., Vonesch J.-L.,
RA   Lutz Y., Chambon P., Losson R.;
RT   "Two distinct nuclear receptor interaction domains in NSD1, a novel
RT   SET protein that exhibits characteristics of both corepressors and
RT   coactivators.";
RL   EMBO J. 17:3398-3412(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2220-2588.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP   CYS-1920 AND THR-1950.
RX   MEDLINE=22688965; PubMed=12805229; DOI=10.1093/emboj/cdg288;
RA   Rayasam G.V., Wendling O., Angrand P.-O., Mark M., Niederreither K.,
RA   Song L., Lerouge T., Hager G.L., Chambon P., Losson R.;
RT   "NSD1 is essential for early post-implantation development and has a
RT   catalytically active SET domain.";
RL   EMBO J. 22:3153-3163(2003).
RN   [4]
RP   INTERACTION WITH ZNF496.
RX   PubMed=15169884; DOI=10.1128/MCB.24.12.5184-5196.2004;
RA   Nielsen A.L., Jorgensen P., Lerouge T., Cervino M., Chambon P.,
RA   Losson R.;
RT   "Nizp1, a novel multitype zinc finger protein that interacts with the
RT   NSD1 histone lysine methyltransferase through a unique C2HR motif.";
RL   Mol. Cell. Biol. 24:5184-5196(2004).
CC   -!- FUNCTION: Histone methyltransferase. Preferentially methylates
CC       'Lys-36' of histone H3 and 'Lys-20' of histone H4 (in vitro).
CC       Transcriptional intermediary factor capable of negatively
CC       influencing transcription. May also positively influence
CC       transcription. Essential for early post-implantation development.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC   -!- SUBUNIT: Interacts with AR DNA- and ligand-binding domains (By
CC       similarity). Interacts with the ligand-binding domains of RARA and
CC       THRA in the absence of ligand; in the presence of ligand the
CC       interaction is severely disrupted but some binding still occurs.
CC       Interacts with the ligand-binding domains of RXRA and ESRRA only
CC       in the presence of ligand. Interacts with ZNF496.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome (Probable).
CC   -!- TISSUE SPECIFICITY: Expressed in the embryo and the outer region
CC       of the uterine decidua at early post-implantation E5.5 stage.
CC       Uniformly expressed in embryonic and extraembryonic tissues during
CC       gastrulation stage E7.5. Expressed differentially after stage 14.5
CC       with highest expression in proliferating cells. Enriched in the
CC       telencephalic region of the brain, spinal cord, intestinal crypt,
CC       tooth buds, thymus and salivary glands at stage E16.5. Also
CC       expressed in the ossification region of developing bones and in
CC       the periosteum.
CC   -!- DOMAIN: Contains 2 adjacent but distinct nuclear receptor
CC       interaction domains (NID+L and NID-L) to which nuclear receptors
CC       bind differentially in the presence and absence of ligand
CC       respectively.
CC   -!- SIMILARITY: Belongs to the histone-lysine methyltransferase
CC       family.
CC   -!- SIMILARITY: Contains 1 AWS domain.
CC   -!- SIMILARITY: Contains 4 PHD-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 post-SET domain.
CC   -!- SIMILARITY: Contains 1 PWWP domain.
CC   -!- SIMILARITY: Contains 1 SET domain.
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DR   EMBL; AF064553; AAC40182.1; -; mRNA.
DR   EMBL; AK082820; BAC38635.1; -; mRNA.
DR   EMBL; AK004485; BAB23326.1; -; mRNA.
DR   IPI; IPI00876476; -.
DR   PIR; T14342; T14342.
DR   UniGene; Mm.12964; -.
DR   UniGene; Mm.168965; -.
DR   ProteinModelPortal; O88491; -.
DR   SMR; O88491; 1439-1486, 1555-1748, 1759-1981, 2014-2059.
DR   STRING; O88491; -.
DR   PhosphoSite; O88491; -.
DR   PRIDE; O88491; -.
DR   Ensembl; ENSMUST00000021944; ENSMUSP00000021944; ENSMUSG00000021488.
DR   UCSC; uc007qqd.1; mouse.
DR   MGI; MGI:1276545; Nsd1.
DR   eggNOG; roNOG06006; -.
DR   GeneTree; ENSGT00600000084164; -.
DR   HOVERGEN; HBG007518; -.
DR   OrthoDB; EOG49GKFN; -.
DR   BRENDA; 2.1.1.43; 244.
DR   ArrayExpress; O88491; -.
DR   Bgee; O88491; -.
DR   CleanEx; MM_NSD1; -.
DR   Genevestigator; O88491; -.
DR   GermOnline; ENSMUSG00000021488; Mus musculus.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0035097; C:histone methyltransferase complex; IC:UniProtKB.
DR   GO; GO:0050681; F:androgen receptor binding; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0030331; F:estrogen receptor binding; IPI:UniProtKB.
DR   GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IDA:UniProtKB.
DR   GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IDA:UniProtKB.
DR   GO; GO:0016922; F:ligand-dependent nuclear receptor binding; IPI:UniProtKB.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0046965; F:retinoid X receptor binding; IPI:UniProtKB.
DR   GO; GO:0046966; F:thyroid hormone receptor binding; IPI:UniProtKB.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; ISS:UniProtKB.
DR   InterPro; IPR006560; AWS.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR000313; PWWP.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 3.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00249; PHD; 5.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00293; PWWP; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 3.
DR   PROSITE; PS51215; AWS; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50812; PWWP; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 2.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   1: Evidence at protein level;
KW   Activator; Chromatin regulator; Chromosome; Developmental protein;
KW   Metal-binding; Methyltransferase; Nucleus; Phosphoprotein; Receptor;
KW   Repeat; Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1   2588       Histone-lysine N-methyltransferase, H3
FT                                lysine-36 and H4 lysine-20 specific.
FT                                /FTId=PRO_0000186071.
FT   DOMAIN     1654   1716       PWWP.
FT   DOMAIN     1788   1838       AWS.
FT   DOMAIN     1839   1961       SET.
FT   DOMAIN     1964   1980       Post-SET.
FT   ZN_FING    1441   1487       PHD-type 1.
FT   ZN_FING    1488   1544       PHD-type 2.
FT   ZN_FING    1605   1649       PHD-type 3.
FT   ZN_FING    2016   2063       PHD-type 4; atypical.
FT   COMPBIAS    841    896       Ser-rich.
FT   COMPBIAS   2213   2251       Pro-rich.
FT   MOD_RES     210    210       Phosphoserine (By similarity).
FT   MOD_RES     380    380       Phosphoserine (By similarity).
FT   MOD_RES     383    383       Phosphoserine (By similarity).
FT   MOD_RES    2369   2369       Phosphoserine (By similarity).
FT   MUTAGEN     803    803       F->A,Y: No effect on interaction with
FT                                nuclear receptors.
FT   MUTAGEN     804    805       ST->AA: Abolishes interaction with
FT                                nuclear receptors.
FT   MUTAGEN     806    807       LL->AA: Strongly decreases interaction
FT                                with liganded nuclear receptors. No
FT                                effect on interaction with non-liganded
FT                                nuclear receptors.
FT   MUTAGEN    1920   1920       C->S: Increases methyltransferase
FT                                activity towards H3 and H4. Increases
FT                                methyltransferase activity; when
FT                                associated with E-1950.
FT   MUTAGEN    1950   1950       T->E: Does not affect histone
FT                                methyltransferase activity. Increases
FT                                methyltransferase activity; when
FT                                associated with S-1920.
SQ   SEQUENCE   2588 AA;  284084 MW;  145DFCF2F285A959 CRC64;
     MDRTCELSRR NCLLSFSNPV NLDASEDKDS PFGNGQSNFS EPLNGCTMQL PTAASGTSQN
     AYGQDSPSCY IPLRRLQDLA SMINVEYLSG SADGSESFQD PAKSDSRAQS PIVCTSLSPG
     GPTALAMKQE PTCNNSPELQ LRVTKTTKNG FLHFENFTGV DDADVDSEMD PEQPVTEDES
     IEEIFEETQT NATCNYEPKS ENGVEVAMGS EQDSMPESRH GAVERPFLPL APQTEKQKNK
     QRSEVDGSNE KTALLPAPTS LGDTNVTVEE QFNSINLSFQ DDPDSSPSPL GNMLEIPGTS
     SPSTSQELPF VPQKILSKWE ASVGLAEQYD VPKGSKNQKC VSSSVKLDSE EDMPFEDCTN
     DPDSEHLLLN GCLKSLAFDS EHSADEKEKP CAKSRVRKSS DNIKRTSVKK DLVPFESRKE
     ERRGKIPDNL GLDFISGGVS DKQASNELSR IANSLTGSST APGSFLFSSS VQNTAKTDFE
     TPDCDSLSGL SESALISKHS GEKKKLHPGQ VCSSKVQLCY VGAGDEEKRS NSVSVSTTSD
     DGCSDLDPTE HNSGFQNSVL GITDAFDKTE NALSVHKNET QYSRYPVTNR IKEKQKSLIT
     NSHADHLMGS TKTMEPETAE LSQVNLSDLK ISSPIPKPQP EFRNDGLTTK FSAPPGIRNE
     NPLTKGGLAN QTLLPLKCRQ PKFRSIKCKH KESPAVAETS ATSEDLSLKC CSSDTNGSPL
     ANISKSGKGE GLKLLNNMHE KTRDSSDIET AVVKHVLSEL KELSYRSLSE DVSDSGTAKA
     SKPLLFSSAS SQNHIPIEPD YKFSTLLMML KDMHDSKTKE QRLMTAQNLA SYRTPDRGDC
     SSGSPVGTSK VLVLGSSTPN SEKPGDSTQD SVHQSPGGGD SALSGELSSS LSSLASDKRE
     LPACGKIRSN CIPRRNCGRA KPSSKLRETI SAQMVKPSVN PKALKTERKR KFSRLPAVTL
     AANRLGNKES GSVNGPSRGG AEDPGKEEPL QQMDLLRNED THFSDVHFDS KAKQSDPDKN
     LEKEPSFENR KGPELGSEMN TENDELHGVN QVVPKKRWQR LNQRRPKPGK RANRFREKEN
     SEGAFGVLLP ADAVQKARED YLEQRAPPTS KPEDSAADPN HGSHSESVAP RLNVCEKSSV
     GMGDVEKETG IPSLMPQTKL PEPAIRSEKK RLRKPSKWLL EYTEEYDQIF APKKKQKKVQ
     EQVHKVSSRC EDESLLARCQ PSAQNKQVDE NSLISTKEEP PVLEREAPFL EGPLAQSDLG
     VTHAELPQLT LSVPVAPEAS PRPALESEEL LVKTPGNYES KRQRKPTKKL LESNDLDPGF
     MPKKGDLGLS RKCFEASRSG NGIVESRATS HLKEFSGGTT KIFDKPRKRK RQRLVTARVH
     YKKVKKEDLT KDTPSSEGEL LIHRTAASPK EILEEGVEHD PGMSASKKLQ VERGGGAALK
     ENVCQNCEKL GELLLCEAQC CGAFHLECLG LPEMPRGKFI CNECHTGIHT CFVCKQSGED
     VKRCLLPLCG KFYHEECVQK YPPTVTQNKG FRCPLHICIT CHAANPANVS ASKGRLMRCV
     RCPVAYHAND FCLAAGSKIL ASNSIICPNH FTPRRGCRNH EHVNVSWCFV CSEGGSLLCC
     DSCPAAFHRE CLNIDIPEGN WYCNDCKAGK KPHYREIVWV KVGRYRWWPA EICHPRAVPS
     NIDKMRHDVG EFPVLFFGSN DYLWTHQARV FPYMEGDVSS KDKMGKGVDG TYKKALQEAA
     ARFEELKARK ELRQLQEDRK NDKKPPPYKH IKVNRPIGRV QIFTADLSEI PRCNCKATDE
     NPCGIDSECI NRMLLYECHP TVCPAGVRCQ NQCFSKRQYP DVEIFRTLQR GWGLRTKTDI
     KKGEFVNEYV GELIDEEECR ARIRYAQEHD ITNFYMLTLD KDRIIDAGPK GNYARFMNHC
     CQPNCETQKW SVNGDTRVGL FALSDIKAGT ELTFNYNLEC LGNGKTVCKC GAPNCSGFLG
     VRPKNQPIVT EEKSRKFKRK PHGKRRSQGE VTKEREDECF SCGDAGQLVS CKKPGCPKVY
     HADCLNLTKR PAGKWECPWH QCDVCGKEAA SFCEMCPSSF CKQHREGMLF ISKLDGRLSC
     TEHDPCGPNP LEPGEIREYV PPTATSPPSP GTQPKEQSSE MATQGPKKSD QPPTDATQLL
     PLSKKALTGS CQRPLLPERP PERTDSSSHL LDRIRDLAGS GTKSQSLVSS QRPQDRPPAK
     EGPRPQPPDR ASPMTRPSSS PSVSSLPLER PLRMTDSRLD KSIGAASPKS QAVEKTPAST
     GLRLSSPDRL LTTNSPKPQI SDRPPEKSHA SLTQRLPPPE KVLSAVVQSL VAKEKALRPV
     DQNTQSKHRP AVVMDLIDLT PRQKERAASP QEVTPQADEK TAMLESSSWP SSKGLGHIPR
     ATEKISVSES LQPSGKVAAP SEHPWQAVKS LTHARFLSPP SAKAFLYESA TQASGRTPVG
     AEQTPGPPSP APGLVKQVKQ LSRGLTAKSG QSFRSLGKIS ASLPNEEKKL TTTEQSPWGL
     GKASPGAGLW PIVAGQTLAQ ACWSAGGTQT LAQTCWSLGR GQDPKPENAI QALNQAPSSR
     KCADSEKK
//
ID   PDE8A_MOUSE             Reviewed;         823 AA.
AC   O88502; Q059P6;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=High affinity cAMP-specific and IBMX-insensitive 3',5'-cyclic phosphodiesterase 8A;
DE            Short=MmPDE8;
DE            EC=3.1.4.17;
GN   Name=Pde8a; Synonyms=Pde8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   MEDLINE=98338029; PubMed=9671792; DOI=10.1073/pnas.95.15.8991;
RA   Soderling S.H., Bayuga S.J., Beavo J.A.;
RT   "Cloning and characterization of a cAMP-specific cyclic nucleotide
RT   phosphodiesterase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:8991-8996(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Hydrolyzes the second messenger cAMP, which is a key
CC       regulator of many important physiological processes. May be
CC       involved in maintaining basal levels of the cyclic nucleotide
CC       and/or in the cAMP regulation of germ cell development (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Adenosine 3',5'-cyclic phosphate + H(2)O =
CC       adenosine 5'-phosphate.
CC   -!- COFACTOR: Binds 2 divalent metal cations per subunit. Site 1 may
CC       preferentially bind zinc ions, while site 2 has a preference for
CC       magnesium and/or manganese ions (By similarity).
CC   -!- ENZYME REGULATION: Inhibited by dipyridimole. Insensitive to
CC       selective PDE inhibitor rolipram and to the non-selective
CC       inhibitor, IBMX.
CC   -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC       3',5'-cyclic AMP: step 1/1.
CC   -!- TISSUE SPECIFICITY: Highest levels in testis > eye > liver >
CC       skeletal muscle > heart > 7-day embryo > kidney > ovary > brain.
CC       In the testis, expressed specifically in the seminiferous
CC       epithelium in a spatial and temporal manner.
CC   -!- DEVELOPMENTAL STAGE: Levels of expression decrease sometime
CC       between embryo day 7 and day 11. In the testis, expression
CC       restricted to middle and late pachytene spermatocytes.
CC   -!- DOMAIN: Composed of a C-terminal catalytic domain containing two
CC       putative divalent metal sites and an N-terminal regulatory domain.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
CC       family. PDE8 subfamily.
CC   -!- SIMILARITY: Contains 1 PAC (PAS-associated C-terminal) domain.
CC   -!- SIMILARITY: Contains 1 PAS (PER-ARNT-SIM) domain.
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DR   EMBL; AF067806; AAC40194.1; -; mRNA.
DR   EMBL; BC125578; AAI25579.1; -; mRNA.
DR   EMBL; BC132145; AAI32146.1; -; mRNA.
DR   IPI; IPI00131688; -.
DR   RefSeq; NP_032829.1; NM_008803.2.
DR   UniGene; Mm.458069; -.
DR   ProteinModelPortal; O88502; -.
DR   SMR; O88502; 224-331, 425-813.
DR   STRING; O88502; -.
DR   PhosphoSite; O88502; -.
DR   PRIDE; O88502; -.
DR   Ensembl; ENSMUST00000026672; ENSMUSP00000026672; ENSMUSG00000025584.
DR   GeneID; 18584; -.
DR   KEGG; mmu:18584; -.
DR   UCSC; uc009ibt.1; mouse.
DR   CTD; 18584; -.
DR   MGI; MGI:1277116; Pde8a.
DR   eggNOG; roNOG11318; -.
DR   HOVERGEN; HBG053544; -.
DR   InParanoid; O88502; -.
DR   OrthoDB; EOG4SBDX7; -.
DR   BRENDA; 3.1.4.17; 244.
DR   NextBio; 294456; -.
DR   ArrayExpress; O88502; -.
DR   Bgee; O88502; -.
DR   CleanEx; MM_PDE8A; -.
DR   Genevestigator; O88502; -.
DR   GermOnline; ENSMUSG00000025584; Mus musculus.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000156; F:two-component response regulator activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR003607; Metal-dep_PHydrolase_HD_dom.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR023174; PDEase_CS.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Gene3D; G3DSA:1.10.1300.10; PDEase_catalytic_dom; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF00233; PDEase_I; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00471; HDc; 1.
DR   SMART; SM00091; PAS; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 1.
DR   PROSITE; PS50113; PAC; FALSE_NEG.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS00126; PDEASE_I; 1.
PE   1: Evidence at protein level;
KW   cAMP; Hydrolase; Metal-binding; Phosphoprotein.
FT   CHAIN         1    823       High affinity cAMP-specific and IBMX-
FT                                insensitive 3',5'-cyclic
FT                                phosphodiesterase 8A.
FT                                /FTId=PRO_0000198839.
FT   DOMAIN      209    280       PAS.
FT   DOMAIN      283    325       PAC.
FT   REGION      526    807       Catalytic (By similarity).
FT   ACT_SITE    551    551       Proton donor (By similarity).
FT   METAL       555    555       Divalent metal cation 1 (By similarity).
FT   METAL       591    591       Divalent metal cation 1 (By similarity).
FT   METAL       592    592       Divalent metal cation 1 (By similarity).
FT   METAL       592    592       Divalent metal cation 2 (By similarity).
FT   METAL       720    720       Divalent metal cation 1 (By similarity).
FT   MOD_RES     382    382       Phosphoserine (By similarity).
FT   MOD_RES     403    403       Phosphoserine (By similarity).
FT   MOD_RES     452    452       Phosphoserine.
SQ   SEQUENCE   823 AA;  93171 MW;  7FD9BE4BAEB9BCF2 CRC64;
     MGCAPSIHTS ENRTFSHSDG EDEDVDVDVP GPAPRSIQRW STAPGLVEPQ PRDNGASKVS
     VADVQFGPMR FHQDQLQVLL VFTKEDSQCN GFHRACEKAG FKCTVTKEVQ TVLTCFQDKL
     HDIIIIDHRY PRQMDAETLC RSIRSSKFSE NTVIVGVVRR VDKEESSLMP FLAAGFTRRF
     IENPNVMACY NELLQLACGE VRSQLKLRAC NSVFTALEKS QEAIEITSED HIIQYANPAF
     ESTMGYQSGE LIGKELAQVP INEKKGDLLD AINSCVTVDK EWQGVYHTQK KNGDNIQQNV
     KIIPVIGQGG KIRHYVSIIR VCNGNNKVET TTECVQTDSQ TDNQAGKHKD RRKHSMDAKA
     VSSRTSDVSS QRRHSSLARI HSMMIEAPIT KVINIINAAQ ENSPVPVTEA LNRVLDILRT
     TELYSPQFNA QDDPHATDLV GGLMSDGLRR FSGNEYILAT KNLPPLSNNL ATPVSLHDVP
     PRIALAIENE EQWDFDIFEL EVATQNRPLI YLGLKTFARF GMCEFLQCSE TTLRSWFQMI
     ESNYHSSNPY HNSTHAADVL HATAYFLSRD KIKETLDRID EVAALIAATV HDVDHPGRTN
     SFLCNAGNQL AVLYNDTAVL ESHHVALAFQ LTLENDQCNI FKQMERNDYR TLRQSIIDMV
     LATEMTKHFE HVNKFINSIN KPLTAQESEE PDRSLEDIKA MLKTPESRAL IKRMMIKCAD
     VSNPCRPLEH CIEWAARISE EYFSQTDEEK QLDLPVVMPV FDRNTCSIPK SQISFIDYFI
     TDMFDAWDAF VDLPNLMQHL DDNFRYWKGL DEKKLRSLRP PPE
//
ID   DNM3A_MOUSE             Reviewed;         908 AA.
AC   O88508; Q3TZK8; Q3UH24; Q8CJ60; Q922J0; Q9CSE1;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 2.
DT   08-MAR-2011, entry version 110.
DE   RecName: Full=DNA (cytosine-5)-methyltransferase 3A;
DE            Short=Dnmt3a;
DE            EC=2.1.1.37;
DE   AltName: Full=DNA methyltransferase MmuIIIA;
DE            Short=DNA MTase MmuIIIA;
DE            Short=M.MmuIIIA;
GN   Name=Dnmt3a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=98324766; PubMed=9662389; DOI=10.1038/890;
RA   Okano M., Xie S., Li E.;
RT   "Cloning and characterization of a family of novel mammalian DNA
RT   (cytosine-5) methyltransferases.";
RL   Nat. Genet. 19:219-220(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and C57BL/6J; TISSUE=Brain, Embryo, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION,
RP   ALTERNATIVE PROMOTER USAGE, AND TISSUE SPECIFICITY.
RC   STRAIN=129/SvJ;
RX   MEDLINE=22254810; PubMed=12138111; DOI=10.1074/jbc.M205312200;
RA   Chen T., Ueda Y., Xie S., Li E.;
RT   "A novel Dnmt3a isoform produced from an alternative promoter
RT   localizes to euchromatin and its expression correlates with active de
RT   novo methylation.";
RL   J. Biol. Chem. 277:38746-38754(2002).
RN   [5]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=20021612; PubMed=10555141; DOI=10.1016/S0092-8674(00)81656-6;
RA   Okano M., Bell D.W., Haber D.A., Li E.;
RT   "DNA methyltransferases Dnmt3a and Dnmt3b are essential for de novo
RT   methylation and mammalian development.";
RL   Cell 99:247-257(1999).
RN   [6]
RP   FUNCTION.
RX   MEDLINE=21293216; PubMed=11399089; DOI=10.1006/jmbi.2001.4710;
RA   Gowher H., Jeltsch A.;
RT   "Enzymatic properties of recombinant Dnmt3a DNA methyltransferase from
RT   mouse: the enzyme modifies DNA in a non-processive manner and also
RT   methylates non-CpG correction sites.";
RL   J. Mol. Biol. 309:1201-1208(2001).
RN   [7]
RP   ERRATUM.
RA   Gowher H., Jeltsch A.;
RL   J. Mol. Biol. 310:951-951(2001).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH ZNF238 AND HDAC1.
RX   MEDLINE=21248589; PubMed=11350943; DOI=10.1093/emboj/20.10.2536;
RA   Fuks F., Burgers W.A., Godin N., Kasai M., Kouzarides T.;
RT   "Dnmt3a binds deacetylases and is recruited by a sequence-specific
RT   repressor to silence transcription.";
RL   EMBO J. 20:2536-2544(2001).
RN   [9]
RP   FUNCTION.
RX   PubMed=11919202; DOI=10.1074/jbc.M202148200;
RA   Gowher H., Jeltsch A.;
RT   "Molecular enzymology of the catalytic domains of the Dnmt3a and
RT   Dnmt3b DNA methyltransferases.";
RL   J. Biol. Chem. 277:20409-20414(2002).
RN   [10]
RP   IDENTIFICATION IN A COMPLEX WITH HDAC1.
RX   MEDLINE=22502935; PubMed=12616525; DOI=10.1002/jcb.10457;
RA   Datta J., Ghoshal K., Sharma S.M., Tajima S., Jacob S.T.;
RT   "Biochemical fractionation reveals association of DNA
RT   methyltransferase (Dnmt) 3b with Dnmt1 and that of Dnmt 3a with a
RT   histone H3 methyltransferase and Hdac1.";
RL   J. Cell. Biochem. 88:855-864(2003).
RN   [11]
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF 302-VAL-PRO-303 AND
RP   705-PRO-CYS-706.
RX   PubMed=15456878; DOI=10.1128/MCB.24.20.9048-9058.2004;
RA   Chen T., Tsujimoto N., Li E.;
RT   "The PWWP domain of Dnmt3a and Dnmt3b is required for directing DNA
RT   methylation to the major satellite repeats at pericentric
RT   heterochromatin.";
RL   Mol. Cell. Biol. 24:9048-9058(2004).
RN   [12]
RP   FUNCTION.
RX   PubMed=15215868; DOI=10.1038/nature02633;
RA   Kaneda M., Okano M., Hata K., Sado T., Tsujimoto N., Li E., Sasaki H.;
RT   "Essential role for de novo DNA methyltransferase Dnmt3a in paternal
RT   and maternal imprinting.";
RL   Nature 429:900-903(2004).
RN   [13]
RP   SUMOYLATION, AND INTERACTION WITH UBC9; PIAS1 AND PIAS2.
RX   PubMed=14752048; DOI=10.1093/nar/gkh195;
RA   Ling Y., Sankpal U.T., Robertson A.K., McNally J.G., Karpova T.,
RA   Robertson K.D.;
RT   "Modification of de novo DNA methyltransferase 3a (Dnmt3a) by SUMO-1
RT   modulates its interaction with histone deacetylases (HDACs) and its
RT   capacity to repress transcription.";
RL   Nucleic Acids Res. 32:598-610(2004).
RN   [14]
RP   ENZYME REGULATION.
RX   PubMed=15671018; DOI=10.1074/jbc.M413412200;
RA   Gowher H., Liebert K., Hermann A., Xu G., Jeltsch A.;
RT   "Mechanism of stimulation of catalytic activity of Dnmt3A and Dnmt3B
RT   DNA-(cytosine-C5)-methyltransferases by Dnmt3L.";
RL   J. Biol. Chem. 280:13341-13348(2005).
RN   [15]
RP   FUNCTION.
RX   PubMed=16567415; DOI=10.1093/jb/mvj044;
RA   Takeshima H., Suetake I., Shimahara H., Ura K., Tate S., Tajima S.;
RT   "Distinct DNA methylation activity of Dnmt3a and Dnmt3b towards naked
RT   and nucleosomal DNA.";
RL   J. Biochem. 139:503-515(2006).
RN   [16]
RP   MUTAGENESIS OF PHE-636; GLU-660; ASP-682; CYS-706; ASN-707; SER-710;
RP   ARG-716; LYS-717; GLU-752; ASN-753; ARG-788; ARG-827; ARG-832;
RP   ARG-878; ARG-881 AND ARG-883.
RX   PubMed=16472822; DOI=10.1016/j.jmb.2006.01.035;
RA   Gowher H., Loutchanwoot P., Vorobjeva O., Handa V., Jurkowska R.Z.,
RA   Jurkowski T.P., Jeltsch A.;
RT   "Mutational analysis of the catalytic domain of the murine Dnmt3a DNA-
RT   (cytosine C5)-methyltransferase.";
RL   J. Mol. Biol. 357:928-941(2006).
RN   [17]
RP   INTERACTION WITH THE PRC2/EED-EZH2 COMPLEX.
RX   PubMed=16357870; DOI=10.1038/nature04431;
RA   Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C.,
RA   Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M.,
RA   Esteller M., Di Croce L., de Launoit Y., Fuks F.;
RT   "The Polycomb group protein EZH2 directly controls DNA methylation.";
RL   Nature 439:871-874(2006).
RN   [18]
RP   ERRATUM.
RA   Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C.,
RA   Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M.,
RA   Esteller M., Di Croce L., de Launoit Y., Fuks F.;
RL   Nature 446:824-824(2006).
RN   [19]
RP   FUNCTION, ENZYME REGULATION, AND MUTAGENESIS OF PHE-728.
RX   PubMed=17713477; DOI=10.1038/nature06146;
RA   Jia D., Jurkowska R.Z., Zhang X., Jeltsch A., Cheng X.;
RT   "Structure of Dnmt3a bound to Dnmt3L suggests a model for de novo DNA
RT   methylation.";
RL   Nature 449:248-251(2007).
RN   [20]
RP   FUNCTION.
RX   PubMed=18823905; DOI=10.1016/j.jmb.2008.03.001;
RA   Takeshima H., Suetake I., Tajima S.;
RT   "Mouse Dnmt3a preferentially methylates linker DNA and is inhibited by
RT   histone H1.";
RL   J. Mol. Biol. 383:810-821(2008).
CC   -!- FUNCTION: Required for genome wide de novo methylation and is
CC       essential for the establishment of DNA methylation patterns during
CC       development. DNA methylation is coordinated with methylation of
CC       histones. It modifies DNA in a non-processive manner and also
CC       methylates non-CpG sites. May preferentially methylate DNA linker
CC       between 2 nucleosomal cores and is inhibited by histone H1. Plays
CC       a role in paternal and maternal imprinting. Required for
CC       methylation of most imprinted loci in germ cells. Acts as a
CC       transcriptional corepressor for ZNF238. Can actively repress
CC       transcription through the recruitment of HDAC activity.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L-
CC       homocysteine + DNA containing 5-methylcytosine.
CC   -!- ENZYME REGULATION: Activated by binding to the regulatory factor
CC       DNMT3L.
CC   -!- SUBUNIT: Heterotetramer composed of 1 DNMT3A homodimer and 2
CC       DNMT3L subunits (DNMT3L-DNMT3A-DNMT3A-DNMT3L). Interacts with
CC       DNMT1 and DNMT3B (By similarity). Binds the ZNF238 transcriptional
CC       repressor. Interacts with SETDB1. Associates with HDAC1 through
CC       its ADD-type zinc-finger. Interacts with the PRC2/EED-EZH2
CC       complex. Interacts with UBC9, PIAS1 and PIAS2.
CC   -!- INTERACTION:
CC       O88974:Setdb1; NbExp=1; IntAct=EBI-995154, EBI-79658;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm (By similarity).
CC       Note=Accumulates in the major satellite repeats at pericentric
CC       heterochromatin.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage; Named isoforms=2;
CC       Name=1;
CC         IsoId=O88508-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O88508-2; Sequence=VSP_009423;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is expressed ubiquitously at low
CC       levels. Expression of isoform 2 is restricted to tissues
CC       containing cells which are undergoing active de novo methylation,
CC       including spleen, testis and thymus.
CC   -!- DEVELOPMENTAL STAGE: At E7.5, the protein is moderately expressed
CC       in embryonic ectoderm and weakly in mesodermal cells. At E8.5 and
CC       E9.5, the expression become ubiquitous with an increase in the
CC       somites and in the ventral part of the embryo.
CC   -!- DOMAIN: The PWWP domain is essential for targeting to pericentric
CC       heterochromatin.
CC   -!- PTM: Sumoylated; sumoylation disrupts the ability to interact with
CC       histone deacetylases (HDAC1 and HDAC2) and repress transcription.
CC   -!- SIMILARITY: Belongs to the C5-methyltransferase family.
CC   -!- SIMILARITY: Contains 1 ADD-type zinc finger.
CC   -!- SIMILARITY: Contains 1 PWWP domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB28644.2; Type=Erroneous initiation;
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DR   EMBL; AF068625; AAC40177.2; -; mRNA.
DR   EMBL; AF480164; AAN40038.1; -; mRNA.
DR   EMBL; AK013096; BAB28644.2; ALT_INIT; mRNA.
DR   EMBL; AK090132; BAC41110.1; -; mRNA.
DR   EMBL; AK147263; BAE27806.1; -; mRNA.
DR   EMBL; AK147627; BAE28033.1; -; mRNA.
DR   EMBL; AK147642; BAE28043.1; -; mRNA.
DR   EMBL; AK147676; BAE28067.1; -; mRNA.
DR   EMBL; AK157792; BAE34200.1; -; mRNA.
DR   EMBL; BC007466; AAH07466.1; -; mRNA.
DR   IPI; IPI00131694; -.
DR   IPI; IPI00172129; -.
DR   RefSeq; NP_031898.1; NM_007872.4.
DR   RefSeq; NP_714965.1; NM_153743.3.
DR   UniGene; Mm.5001; -.
DR   ProteinModelPortal; O88508; -.
DR   SMR; O88508; 279-421, 469-908.
DR   DIP; DIP-38005N; -.
DR   DIP; DIP-46360N; -.
DR   IntAct; O88508; 2.
DR   MINT; MINT-2521021; -.
DR   STRING; O88508; -.
DR   REBASE; 3747; M.MmuDnmt3A.
DR   PhosphoSite; O88508; -.
DR   PRIDE; O88508; -.
DR   Ensembl; ENSMUST00000020991; ENSMUSP00000020991; ENSMUSG00000020661.
DR   Ensembl; ENSMUST00000085826; ENSMUSP00000082985; ENSMUSG00000020661.
DR   Ensembl; ENSMUST00000111186; ENSMUSP00000106817; ENSMUSG00000020661.
DR   GeneID; 13435; -.
DR   KEGG; mmu:13435; -.
DR   UCSC; uc007mxb.1; mouse.
DR   CTD; 13435; -.
DR   MGI; MGI:1261827; Dnmt3a.
DR   eggNOG; maNOG14167; -.
DR   HOGENOM; HBG445182; -.
DR   HOVERGEN; HBG051381; -.
DR   InParanoid; O88508; -.
DR   OMA; SSDTPKD; -.
DR   OrthoDB; EOG4T1HKX; -.
DR   BRENDA; 2.1.1.37; 244.
DR   NextBio; 283867; -.
DR   ArrayExpress; O88508; -.
DR   Bgee; O88508; -.
DR   CleanEx; MM_DNMT3A; -.
DR   Genevestigator; O88508; -.
DR   GermOnline; ENSMUSG00000020661; Mus musculus.
DR   GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
DR   GO; GO:0005720; C:nuclear heterochromatin; IDA:MGI.
DR   GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0043045; P:DNA methylation involved in embryo development; IMP:UniProtKB.
DR   GO; GO:0043046; P:DNA methylation involved in gamete generation; IMP:UniProtKB.
DR   GO; GO:0006346; P:methylation-dependent chromatin silencing; IDA:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0006349; P:regulation of gene expression by genetic imprinting; IMP:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR000313; PWWP.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   SMART; SM00293; PWWP; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS00095; C5_MTASE_2; FALSE_NEG.
DR   PROSITE; PS50812; PWWP; 1.
PE   1: Evidence at protein level;
KW   Alternative promoter usage; Chromatin regulator; Cytoplasm;
KW   DNA-binding; Metal-binding; Methyltransferase; Nucleus;
KW   Phosphoprotein; Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    908       DNA (cytosine-5)-methyltransferase 3A.
FT                                /FTId=PRO_0000088044.
FT   DOMAIN      288    346       PWWP.
FT   ZN_FING     490    582       ADD-type.
FT   REGION      195    399       Interaction with DNMT1 and DNMT3B (By
FT                                similarity).
FT   REGION      490    582       Interaction with the PRC2/EED-EZH2
FT                                complex.
FT   ACT_SITE    706    706       By similarity.
FT   MOD_RES     102    102       Phosphoserine (By similarity).
FT   VAR_SEQ       1    219       Missing (in isoform 2).
FT                                /FTId=VSP_009423.
FT   MUTAGEN     302    303       WP->ST: Prevents accumulation in
FT                                pericentric heterochromatin.
FT   MUTAGEN     636    636       F->A: Reduces activity about 20-fold.
FT                                Loss of substrate binding.
FT   MUTAGEN     660    660       E->A: Reduces activity about 15-fold.
FT                                Loss of substrate binding.
FT   MUTAGEN     682    682       D->A: Strongly reduces substrate binding.
FT                                No effect on activity.
FT   MUTAGEN     705    706       PC->VD: No effect on localization.
FT   MUTAGEN     706    706       C->A: Reduces activity about 5-fold.
FT                                Reduces DNA-binding capacity.
FT   MUTAGEN     707    707       N->Q: Reduces activity about 3-fold.
FT   MUTAGEN     710    710       S->A: No effect on activity.
FT   MUTAGEN     716    716       R->A: Reduces activity about 30-fold.
FT                                Reduces DNA-binding capacity.
FT   MUTAGEN     717    717       K->A: Reduces activity about 3-fold.
FT   MUTAGEN     728    728       F->A: Loss of activity du to the
FT                                incapacity to bind the regulatory subunit
FT                                DNMT3L.
FT   MUTAGEN     752    752       E->A: Reduces activity about 10-fold.
FT   MUTAGEN     753    753       N->A: Reduces activity about 10-fold.
FT   MUTAGEN     788    788       R->A: Reduces activity about 15-fold.
FT   MUTAGEN     827    827       R->A: Reduces activity about 2-fold.
FT                                Reduces DNA-binding capacity.
FT   MUTAGEN     832    832       R->A: Reduces DNA-binding capacity. No
FT                                effect on activity.
FT   MUTAGEN     878    878       R->A: Reduces activity about 6-fold.
FT                                Reduces DNA-binding capacity.
FT   MUTAGEN     881    881       R->A: Loss of activity. Strongly reduces
FT                                substrate binding.
FT   MUTAGEN     883    883       R->A: Reduces activity about 3-fold.
FT                                Reduces DNA-binding capacity.
FT   CONFLICT    151    151       Q -> P (in Ref. 4; AAH07466).
FT   CONFLICT    775    775       M -> T (in Ref. 3; BAB28644).
FT   CONFLICT    781    781       V -> G (in Ref. 3; BAB28644).
FT   CONFLICT    791    791       W -> R (in Ref. 3; BAB28644).
FT   CONFLICT    809    809       L -> P (in Ref. 3; BAB28644).
FT   CONFLICT    904    904       Y -> I (in Ref. 3; BAB28644).
SQ   SEQUENCE   908 AA;  101672 MW;  5F98D5A8092C84A5 CRC64;
     MPSSGPGDTS SSSLEREDDR KEGEEQEENR GKEERQEPSA TARKVGRPGR KRKHPPVESS
     DTPKDPAVTT KSQPMAQDSG PSDLLPNGDL EKRSEPQPEE GSPAAGQKGG APAEGEGTET
     PPEASRAVEN GCCVTKEGRG ASAGEGKEQK QTNIESMKME GSRGRLRGGL GWESSLRQRP
     MPRLTFQAGD PYYISKRKRD EWLARWKREA EKKAKVIAVM NAVEENQASG ESQKVEEASP
     PAVQQPTDPA SPTVATTPEP VGGDAGDKNA TKAADDEPEY EDGRGFGIGE LVWGKLRGFS
     WWPGRIVSWW MTGRSRAAEG TRWVMWFGDG KFSVVCVEKL MPLSSFCSAF HQATYNKQPM
     YRKAIYEVLQ VASSRAGKLF PACHDSDESD SGKAVEVQNK QMIEWALGGF QPSGPKGLEP
     PEEEKNPYKE VYTDMWVEPE AAAYAPPPPA KKPRKSTTEK PKVKEIIDER TRERLVYEVR
     QKCRNIEDIC ISCGSLNVTL EHPLFIGGMC QNCKNCFLEC AYQYDDDGYQ SYCTICCGGR
     EVLMCGNNNC CRCFCVECVD LLVGPGAAQA AIKEDPWNCY MCGHKGTYGL LRRREDWPSR
     LQMFFANNHD QEFDPPKVYP PVPAEKRKPI RVLSLFDGIA TGLLVLKDLG IQVDRYIASE
     VCEDSITVGM VRHQGKIMYV GDVRSVTQKH IQEWGPFDLV IGGSPCNDLS IVNPARKGLY
     EGTGRLFFEF YRLLHDARPK EGDDRPFFWL FENVVAMGVS DKRDISRFLE SNPVMIDAKE
     VSAAHRARYF WGNLPGMNRP LASTVNDKLE LQECLEHGRI AKFSKVRTIT TRSNSIKQGK
     DQHFPVFMNE KEDILWCTEM ERVFGFPVHY TDVSNMSRLA RQRLLGRSWS VPVIRHLFAP
     LKEYFACV
//
ID   NEMO_MOUSE              Reviewed;         412 AA.
AC   O88522;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=NF-kappa-B essential modulator;
DE            Short=NEMO;
DE   AltName: Full=IkB kinase-associated protein 1;
DE            Short=IKKAP1;
DE            Short=mFIP-3;
DE   AltName: Full=Inhibitor of nuclear factor kappa-B kinase subunit gamma;
DE            Short=I-kappa-B kinase subunit gamma;
DE            Short=IKK-gamma;
DE            Short=IKKG;
DE            Short=IkB kinase subunit gamma;
DE   AltName: Full=NF-kappa-B essential modifier;
GN   Name=Ikbkg; Synonyms=Nemo;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=T-cell;
RX   MEDLINE=98319237; PubMed=9657155; DOI=10.1016/S0092-8674(00)81466-X;
RA   Yamaoka S., Courtois G., Bessia C., Whiteside S.T., Weil R., Agou F.,
RA   Kirk H.E., Kay R.J., Israel A.;
RT   "Complementation cloning of NEMO, a component of the I-kappaB kinase
RT   complex essential for NF-kappaB activation.";
RL   Cell 93:1231-1240(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 85-412, AND PROTEIN SEQUENCE OF 144-159.
RC   TISSUE=Cervix carcinoma;
RX   MEDLINE=99108125; PubMed=9891086;
RA   Mercurio F., Murray B.W., Shevchenko A., Bennett B.L., Young D.B.,
RA   Li J.W., Pascual G., Motiwala A., Zhu H., Mann M., Manning A.M.;
RT   "IkappaB kinase (IKK)-associated protein 1, a common component of the
RT   heterogeneous IKK complex.";
RL   Mol. Cell. Biol. 19:1526-1538(1999).
RN   [3]
RP   FUNCTION.
RX   MEDLINE=99128359; PubMed=9927690; DOI=10.1073/pnas.96.3.1042;
RA   Li Y., Kang J., Friedman J., Tarassishin L., Ye J., Kovalenko A.,
RA   Wallach D., Horwitz M.S.;
RT   "Identification of a cell protein (FIP-3) as a modulator of NF-kappaB
RT   activity and as a target of an adenovirus inhibitor of tumor necrosis
RT   factor alpha-induced apoptosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:1042-1047(1999).
RN   [4]
RP   IKK COMPLEX.
RX   MEDLINE=21264955; PubMed=11080499; DOI=10.1074/jbc.M008353200;
RA   Li X.-H., Fang X., Gaynor R.B.;
RT   "Role of ikkgamma/nemo in assembly of the IkappaB kinase complex.";
RL   J. Biol. Chem. 276:4494-4500(2001).
RN   [5]
RP   PHOSPHORYLATION AT SER-369, AND MUTAGENESIS OF SER-369 AND SER-375.
RX   PubMed=11971901; DOI=10.1074/jbc.M201393200;
RA   Prajapati S., Gaynor R.B.;
RT   "Regulation of Ikappa B kinase (IKK)gamma /NEMO function by IKKbeta
RT   -mediated phosphorylation.";
RL   J. Biol. Chem. 277:24331-24339(2002).
RN   [6]
RP   INTERACTION WITH TANK AND IKBKB.
RX   PubMed=12133833; DOI=10.1074/jbc.M205069200;
RA   Chariot A., Leonardi A., Muller J., Bonif M., Brown K., Siebenlist U.;
RT   "Association of the adaptor TANK with the I kappa B kinase (IKK)
RT   regulator NEMO connects IKK complexes with IKK epsilon and TBK1
RT   kinases.";
RL   J. Biol. Chem. 277:37029-37036(2002).
RN   [7]
RP   UBIQUITINATION AT LYS-278; LYS-314; LYS-318; LYS-319 AND LYS-392, AND
RP   MUTAGENESIS OF LYS-278; LYS-314; VAL-316; LYS-318; LYS-319 AND
RP   LYS-392.
RX   PubMed=17728323; DOI=10.1093/hmg/ddm237;
RA   Sebban-Benin H., Pescatore A., Fusco F., Pascuale V., Gautheron J.,
RA   Yamaoka S., Moncla A., Ursini M.V., Courtois G.;
RT   "Identification of TRAF6-dependent NEMO polyubiquitination sites
RT   through analysis of a new NEMO mutation causing incontinentia
RT   pigmenti.";
RL   Hum. Mol. Genet. 16:2805-2815(2007).
RN   [8]
RP   INTERACTION WITH TERF2IP.
RX   PubMed=20622870; DOI=10.1038/ncb2080;
RA   Teo H., Ghosh S., Luesch H., Ghosh A., Wong E.T., Malik N., Orth A.,
RA   de Jesus P., Perry A.S., Oliver J.D., Tran N.L., Speiser L.J.,
RA   Wong M., Saez E., Schultz P., Chanda S.K., Verma I.M., Tergaonkar V.;
RT   "Telomere-independent Rap1 is an IKK adaptor and regulates NF-kappaB-
RT   dependent gene expression.";
RL   Nat. Cell Biol. 12:758-767(2010).
CC   -!- FUNCTION: Regulatory subunit of the IKK core complex which
CC       phosphorylates inhibitors of NF-kappa-B thus leading to the
CC       dissociation of the inhibitor/NF-kappa-B complex and ultimately
CC       the degradation of the inhibitor. Also considered to be a mediator
CC       for TAX activation of NF-kappa-B. Could be implicated in NF-kappa-
CC       B-mediated protection from cytokine toxicity (By similarity).
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Component of the I-kappa-B-
CC       kinase (IKK) core complex consisting of CHUK, IKBKB and IKBKG;
CC       probably four alpha/CHUK-beta/IKBKB dimers are associated with
CC       four gamma/IKBKG subunits. The IKK core complex seems to associate
CC       with regulatory or adapter proteins to form a IKK-signalosome
CC       holo-complex. The IKK complex associates with TERF2IP/RAP1,
CC       leading to promote IKK-mediated phosphorylation of RELA/p65. Part
CC       of a complex composed of NCOA2, NCOA3, CHUK/IKKA, IKBKB, IKBKG and
CC       CREBBP. Interacts with COPS3, CYLD, NALP2, TRPC4AP and LRDD.
CC       Interacts with ATM; the complex is exported from the nucleus.
CC       Interacts with TRAF6. Interacts with TANK; the interaction is
CC       enhanced by TBK1 and IKBKE. Part of a ternary complex consisting
CC       of TANK, IKBKB and IKBKG. Interacts with ZFAND5 (By similarity).
CC   -!- INTERACTION:
CC       P70434:Irf7; NbExp=1; IntAct=EBI-998011, EBI-997907;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- DOMAIN: The leucine-zipper domain and the C2HC-type zinc-finger
CC       are essential for polyubiquitin binding and for the activation of
CC       IRF3 (By similarity).
CC   -!- PTM: Phosphorylation at Ser-68 attenuates aminoterminal
CC       homodimerization (By similarity).
CC   -!- PTM: Polyubiquitinated on Lys-278 through 'Lys-63'; the
CC       ubiquitination is mediated by NOD2 and RIPK2 and probably plays a
CC       role in signaling by facilitating interactions with ubiquitin
CC       domain-containing proteins and activates the NF-kappa-B
CC       pathway.Polyubiquitinated on Lys-392 through 'Lys-63'; the
CC       ubiquitination is mediated by BCL10, MALT1 and TRAF6 and probably
CC       plays a role in signaling by facilitating interactions with
CC       ubiquitin domain-containing proteins and activates the NF-kappa-B
CC       pathway. Monoubiquitinated on Lys-270 and Lys-302; promotes
CC       nuclear export. Linear polyubiquitinated on Lys-278; the head-to-
CC       tail polyubiquitination is mediated by the LUBAC complex. Linear
CC       polyubiquitinated on Lys-302; the head-to-tail polyubiquitination
CC       is mediated by the LUBAC complex (By similarity).
CC   -!- PTM: Sumoylated on Lys-270 and Lys-302 by SUMO1; the modification
CC       results in phosphorylation of Ser-85 by ATM leading to a
CC       replacement of the sumoylation by mono-ubiquitination on these
CC       residues (By similarity).
CC   -!- SIMILARITY: Contains 1 C2HC-type zinc finger.
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DR   EMBL; AF069542; AAC40153.1; -; mRNA.
DR   IPI; IPI00831266; -.
DR   UniGene; Mm.12967; -.
DR   PDB; 2V4H; X-ray; 2.90 A; A/B=251-337.
DR   PDB; 2ZVN; X-ray; 3.00 A; B/D/F/H=253-337.
DR   PDB; 2ZVO; X-ray; 2.90 A; B/D=250-339.
DR   PDB; 3F89; X-ray; 2.80 A; A/B=250-339.
DR   PDB; 3JSV; X-ray; 2.70 A; C/D=250-343.
DR   PDBsum; 2V4H; -.
DR   PDBsum; 2ZVN; -.
DR   PDBsum; 2ZVO; -.
DR   PDBsum; 3F89; -.
DR   PDBsum; 3JSV; -.
DR   ProteinModelPortal; O88522; -.
DR   SMR; O88522; 49-109, 193-248, 256-341, 387-412.
DR   DIP; DIP-29811N; -.
DR   IntAct; O88522; 3.
DR   MINT; MINT-143245; -.
DR   STRING; O88522; -.
DR   PhosphoSite; O88522; -.
DR   PRIDE; O88522; -.
DR   Ensembl; ENSMUST00000004330; ENSMUSP00000004330; ENSMUSG00000004221.
DR   Ensembl; ENSMUST00000114127; ENSMUSP00000109762; ENSMUSG00000004221.
DR   Ensembl; ENSMUST00000114128; ENSMUSP00000109763; ENSMUSG00000004221.
DR   Ensembl; ENSMUST00000114133; ENSMUSP00000109768; ENSMUSG00000004221.
DR   UCSC; uc009tpe.1; mouse.
DR   MGI; MGI:1338074; Ikbkg.
DR   HOVERGEN; HBG000417; -.
DR   InParanoid; O88522; -.
DR   OrthoDB; EOG42BX8V; -.
DR   NextBio; 288945; -.
DR   ArrayExpress; O88522; -.
DR   Bgee; O88522; -.
DR   CleanEx; MM_IKBKG; -.
DR   Genevestigator; O88522; -.
DR   GermOnline; ENSMUSG00000004221; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IDA:MGI.
DR   GO; GO:0001782; P:B cell homeostasis; IMP:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR021063; NEMO_N.
DR   Pfam; PF11577; NEMO; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Cytoplasm; Direct protein sequencing;
KW   Disulfide bond; Isopeptide bond; Metal-binding; Nucleus;
KW   Phosphoprotein; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1    412       NF-kappa-B essential modulator.
FT                                /FTId=PRO_0000096783.
FT   DOMAIN      315    336       Leucine-zipper (Potential).
FT   ZN_FING     389    410       C2HC-type.
FT   REGION       44    111       Interaction with CHUK/IKBKB (By
FT                                similarity).
FT   REGION      150    250       Interaction with TANK.
FT   REGION      246    358       Self-association (By similarity).
FT   REGION      375    412       Interaction with CYLD (By similarity).
FT   COILED       49    345       Potential.
FT   MOD_RES      31     31       Phosphoserine; by IKKB (By similarity).
FT   MOD_RES      43     43       Phosphoserine; by IKKB (By similarity).
FT   MOD_RES      68     68       Phosphoserine (By similarity).
FT   MOD_RES      85     85       Phosphoserine; by ATM (By similarity).
FT   MOD_RES     369    369       Phosphoserine; by IKKB.
FT   MOD_RES     380    380       Phosphoserine (By similarity).
FT   DISULFID     54     54       Interchain (By similarity).
FT   DISULFID    340    340       Interchain (By similarity).
FT   CROSSLNK    270    270       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO);
FT                                alternate (By similarity).
FT   CROSSLNK    270    270       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin);
FT                                alternate (By similarity).
FT   CROSSLNK    278    278       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CROSSLNK    302    302       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    302    302       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin);
FT                                alternate (By similarity).
FT   CROSSLNK    314    314       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CROSSLNK    318    318       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CROSSLNK    319    319       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CROSSLNK    392    392       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   MUTAGEN     278    278       K->R: Slight decrease in TRAF6-induced
FT                                polyubiquitination.
FT   MUTAGEN     314    314       K->R: Slight decrease in TRAF6-induced
FT                                polyubiquitination. Important decrease in
FT                                TRAF6-induced polyubiquitination; when
FT                                associated with R-318 and R-319.
FT   MUTAGEN     316    316       V->P: Loss of interaction with TRAF6 and
FT                                TRAF6-induced polyubiquitination.
FT   MUTAGEN     318    318       K->R: Slight decrease in TRAF6-induced
FT                                polyubiquitination. Decrease in TRAF6-
FT                                induced polyubiquitination; when
FT                                associated with R-319. Important decrease
FT                                in TRAF6-induced polyubiquitination; when
FT                                associated with R-314 and R-319.
FT   MUTAGEN     319    319       K->R: Slight decrease in TRAF6-induced
FT                                polyubiquitination. Decrease in TRAF6-
FT                                induced polyubiquitination; when
FT                                associated with R-318. Important decrease
FT                                in TRAF6-induced polyubiquitination; when
FT                                associated with R-314 and R-318.
FT   MUTAGEN     369    369       S->A: Decreases phosphorylation and
FT                                increases NF-kappa-B activity.
FT   MUTAGEN     375    375       S->A: Decreases phosphorylation and
FT                                increases NF-kappa-B activity.
FT   MUTAGEN     392    392       K->R: 40% decrease in IL1-induced NF-
FT                                kappa-B activation.
FT   HELIX       260    278
FT   HELIX       280    287
FT   HELIX       290    321
FT   HELIX       323    328
FT   HELIX       330    333
SQ   SEQUENCE   412 AA;  47942 MW;  30ED68B5A2383608 CRC64;
     MNKHPWKNQL SETVQPSGGP AEDQDMLGEE SSLGKPAMLH LPSEQGTPET LQRCLEENQE
     LRDAIRQSNQ MLRERCEELL HFQVSQREEK EFLMCKFQEA RKLVERLSLE KLDLRSQREQ
     ALKELEQLKK CQQQMAEDKA SVKAQVTSLL GELQESQSRL EAATKDRQAL EGRIRAVSEQ
     VRQLESEREV LQQQHSVQVD QLRMQNQSVE AALRMERQAA SEEKRKLAQL QAAYHQLFQD
     YDSHIKSSKG MQLEDLRQQL QQAEEALVAK QELIDKLKEE AEQHKIVMET VPVLKAQADI
     YKADFQAERH AREKLVEKKE YLQEQLEQLQ REFNKLKVGC HESARIEDMR KRHVETPQPP
     LLPAPAHHSF HLALSNQRRS PPEEPPDFCC PKCQYQAPDM DTLQIHVMEC IE
//
ID   ZFR_MOUSE               Reviewed;        1074 AA.
AC   O88532; Q3TY30; Q8BS85; Q8CGG5; Q91VZ0; Q9CT34;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   08-FEB-2011, entry version 75.
DE   RecName: Full=Zinc finger RNA-binding protein;
GN   Name=Zfr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DNA-BINDING, RNA-BINDING, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Spermatocyte;
RX   MEDLINE=99173884; PubMed=10072773; DOI=10.1016/S0378-1119(98)00615-5;
RA   Meagher M.J., Schumacher J.M., Lee K., Holdcraft R.W., Edelhoff S.,
RA   Disteche C., Braun R.E.;
RT   "Identification of ZFR, an ancient and highly conserved murine
RT   chromosome-associated zinc finger protein.";
RL   Gene 228:197-211(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-357, AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 632-1074.
RC   STRAIN=129, C57BL/6J, and FVB/N; TISSUE=Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 458-1074.
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=11283266; DOI=10.1128/MCB.21.8.2880-2890.2001;
RA   Meagher M.J., Braun R.E.;
RT   "Requirement for the murine zinc finger protein ZFR in
RT   perigastrulation growth and survival.";
RL   Mol. Cell. Biol. 21:2880-2890(2001).
RN   [5]
RP   FUNCTION, INTERACTION WITH STAU2, AND SUBCELLULAR LOCATION.
RX   PubMed=16277607; DOI=10.1111/j.1471-4159.2005.03523.x;
RA   Elvira G., Massie B., DesGroseillers L.;
RT   "The zinc-finger protein ZFR is critical for Staufen 2 isoform
RT   specific nucleocytoplasmic shuttling in neurons.";
RL   J. Neurochem. 96:105-117(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Involved in postimplantation and gastrulation stages of
CC       development. Binds to DNA and RNA. Involved in the
CC       nucleocytoplasmic shuttling of STAU2 (By similarity).
CC   -!- SUBUNIT: Found in a cytoplasmic mRNP complex with STAU2. Does not
CC       interact with STAU1 (By similarity). Interacts with STAU2.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasmic granule (By
CC       similarity). Chromosome (By similarity). Note=Associated with
CC       chromosome foci in meiotic cells. Localizes in somatodendritic
CC       compartment of primary hippocampal neurons (By similarity).
CC       Colocalizes with STAU2 in several cytosolic RNA granules (By
CC       similarity). Associated with chromosomes.
CC   -!- TISSUE SPECIFICITY: Expressed in Sertoli cells, spermatocytes,
CC       primary and growing oocytes and granulosa cells (at protein
CC       level). Expressed in testis, ovary and brain.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryos at 5.5, 6.5 and 7 dpc
CC       (at protein level). Expressed in the trophoectoderm cells and
CC       inner cell mass of blastocysts (at protein level).
CC   -!- MISCELLANEOUS: Knockout mice form mesoderm but are delayed in
CC       their development and fail to form normal anterior embryonic
CC       structures. Show both an increase in programmed cell death and a
CC       decrease in mitotic index, especially in the region of the distal
CC       tip of the embryonic ectoderm. Show also a reduction in apical
CC       vacuoles in the columnar visceral endoderm cells in the
CC       extraembryonic region. Knockout mice die by 8 to 9 days of
CC       gestation.
CC   -!- SIMILARITY: Contains 1 DZF domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC25762.1; Type=Erroneous initiation;
CC       Sequence=AAH06962.1; Type=Erroneous initiation;
CC       Sequence=AAH38599.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=AAH38599.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAH58570.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=AAH58570.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=BAC28897.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF071059; AAC25762.1; ALT_INIT; mRNA.
DR   EMBL; BC006962; AAH06962.1; ALT_INIT; mRNA.
DR   EMBL; BC038599; AAH38599.1; ALT_SEQ; mRNA.
DR   EMBL; BC058570; AAH58570.1; ALT_SEQ; mRNA.
DR   EMBL; AK011329; BAB27548.1; -; mRNA.
DR   EMBL; AK034963; BAC28897.1; ALT_INIT; mRNA.
DR   EMBL; AK158938; BAE34733.1; -; mRNA.
DR   IPI; IPI00131810; -.
DR   PIR; T14343; T14343.
DR   RefSeq; NP_035897.2; NM_011767.2.
DR   UniGene; Mm.273496; -.
DR   ProteinModelPortal; O88532; -.
DR   IntAct; O88532; 1.
DR   STRING; O88532; -.
DR   PhosphoSite; O88532; -.
DR   PRIDE; O88532; -.
DR   Ensembl; ENSMUST00000022814; ENSMUSP00000022814; ENSMUSG00000022201.
DR   GeneID; 22763; -.
DR   KEGG; mmu:22763; -.
DR   UCSC; uc007vhk.1; mouse.
DR   CTD; 22763; -.
DR   MGI; MGI:1341890; Zfr.
DR   eggNOG; roNOG09140; -.
DR   GeneTree; ENSGT00550000074528; -.
DR   HOGENOM; HBG713351; -.
DR   HOVERGEN; HBG108765; -.
DR   InParanoid; O88532; -.
DR   NextBio; 303285; -.
DR   ArrayExpress; O88532; -.
DR   Bgee; O88532; -.
DR   CleanEx; MM_ZFR; -.
DR   Genevestigator; O88532; -.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   InterPro; IPR006561; DZF.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR022755; Znf_C2H2_jaz.
DR   InterPro; IPR003604; Znf_U1.
DR   Pfam; PF07528; DZF; 1.
DR   Pfam; PF12171; zf-C2H2_jaz; 1.
DR   SMART; SM00572; DZF; 1.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SMART; SM00451; ZnF_U1; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; UNKNOWN_3.
PE   1: Evidence at protein level;
KW   Acetylation; Chromosome; Cytoplasm; Developmental protein;
KW   DNA-binding; Nucleus; Phosphoprotein; Repeat; RNA-binding.
FT   CHAIN         1   1074       Zinc finger RNA-binding protein.
FT                                /FTId=PRO_0000312720.
FT   DOMAIN      790   1038       DZF.
FT   COMPBIAS     36    302       Ala-rich.
FT   MOD_RES     317    317       N6-acetyllysine (By similarity).
FT   MOD_RES     475    475       Phosphoserine (By similarity).
FT   MOD_RES     476    476       Phosphoserine (By similarity).
FT   MOD_RES     509    509       N6-acetyllysine (By similarity).
FT   MOD_RES     910    910       N6-acetyllysine (By similarity).
FT   MOD_RES    1054   1054       Phosphoserine.
FT   CONFLICT    355    355       H -> K (in Ref. 2; AAH58570/AAH38599).
FT   CONFLICT    458    458       T -> S (in Ref. 3; BAC28897).
FT   CONFLICT    877    877       M -> I (in Ref. 3; BAB27548).
FT   CONFLICT   1016   1016       F -> K (in Ref. 1; AAC25762).
SQ   SEQUENCE   1074 AA;  116859 MW;  F0CE7B9F84A79A07 CRC64;
     MIPICPVVSF TYVPSRLGED AKMATGNYFG FTHSGAAAAA AAAQYSQQPA SGVAYSHPTT
     VASYTVHQAP VAAHTVTAAY APAAATVAVA RPAPVAVAAA ATAAAYGGYP TAHTATDYGY
     TQRQQEAPPP PPPATTQNYQ DSYSYVRSTA PAVAYDSKQY YQQPTATAAA VAAAAQPQPS
     VAETYYQTAP KAGYSQGATQ YTQAQQARQV TAIKPATPSP ATTTFSIYPV SSTVQPVAAA
     ATVVPSYTQS ATYSTTAVTY SGTSYSGYEA AVYSAASSYY QQQQQQQKQA AAAAAAAAAT
     AAWTGTTFTK KTPFQNKQLK PKQPPKPPQI HYCDVCKISC AGPQTYKEHL EGQKHKKKEA
     ALKASQNTSS SNNSTRGTQN QLRCELCDVS CTGADAYAAH IRGAKHQKVV KLHTKLGKPI
     PSTEPNVVSQ ATSSTAASAS KPTASPSSIG ASNCTLNTSS IATSSVKGLS TTGNSSLNST
     SNTKVSAIPT NMAAKKTSTP KINFVGGNKL QSTGNKTEDL KGIDCVKNTP AASAVQIPEV
     KQDAGSEPVT PASLAALQSD VQPVGHDYVE EVRNDEGKVI RFHCKLCECS FNDPNAKEMH
     LKGRRHRLQY KKKVNPDLQV EVKPSIRARK IQEEKMRKQM QKEEYWRRRE EEERWRMEIR
     RYEEDMYWRR MEEEQHHWDD RRRMPDGGYP HGPPGPLGLL GVRPGMPPQP QGPAPLRRPD
     SSDDRYVMTK HATIYPTEEE LQAVQKIVSI TERALKLVSD SLSEHEKSKN KEGDDKKEGG
     KDRALKGVLR VGVLAKGLLL RGDRNVNLVL LCSEKPSKSL LSRIAENLPK QLAVISPEKY
     DIKCAVSEAA IILNSCVEPK MQVTITLTSP IIREENMREG DVTSGMVKDP PDVLDRQKCL
     DALAALRHAK WFQARANGLQ SCVIIIRILR DLCQRVPTWS DFPSWAMELL VEKAISSASS
     PQSPGDALRR VFECISSGII LKGSPGLLDP CEKDPFDTLA TMTDQQREDI TSSAQFALRL
     LAFRQIHKVL GMDPLPQMNQ RFNIHNNRKR RRDSDGVDGF EAEGKKDKKD YDNF
//
ID   CSN3_MOUSE              Reviewed;         423 AA.
AC   O88543;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=COP9 signalosome complex subunit 3;
DE            Short=SGN3;
DE            Short=Signalosome subunit 3;
DE   AltName: Full=JAB1-containing signalosome subunit 3;
GN   Name=Cops3; Synonyms=Csn3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION IN THE CSN COMPLEX.
RC   STRAIN=C57BL/6;
RX   MEDLINE=98372877; PubMed=9707402; DOI=10.1016/S0960-9822(07)00372-7;
RA   Wei N., Tsuge T., Serino G., Dohmae N., Takio K., Matsui M.,
RA   Deng X.-W.;
RT   "The COP9 complex is conserved between plants and mammals and is
RT   related to the 26S proteasome regulatory complex.";
RL   Curr. Biol. 8:919-922(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   MEDLINE=22853759; PubMed=12972600;
RX   DOI=10.1128/MCB.23.19.6798-6808.2003;
RA   Yan J., Walz K., Nakamura H., Carattini-Rivera S., Zhao Q., Vogel H.,
RA   Wei N., Justice M.J., Bradley A., Lupski J.R.;
RT   "COP9 signalosome subunit 3 is essential for maintenance of cell
RT   proliferation in the mouse embryonic epiblast.";
RL   Mol. Cell. Biol. 23:6798-6808(2003).
CC   -!- FUNCTION: Component of the COP9 signalosome complex (CSN), a
CC       complex involved in various cellular and developmental processes.
CC       The CSN complex is an essential regulator of the ubiquitin (Ubl)
CC       conjugation pathway by mediating the deneddylation of the cullin
CC       subunits of SCF-type E3 ligase complexes, leading to decrease the
CC       Ubl ligase activity of SCF-type complexes such as SCF, CSA or
CC       DDB2. The complex is also involved in phosphorylation of p53/TP53,
CC       c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via
CC       its association with CK2 and PKD kinases. CSN-dependent
CC       phosphorylation of TP53 and JUN promotes and protects degradation
CC       by the Ubl system, respectively. Essential to maintain the
CC       survival of epiblast cells and thus the development of the
CC       postimplantation embryo.
CC   -!- SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1,
CC       COPS2, COPS3, COPS4, COPS5, COP6, COPS7 (COPS7A or COPS7B) and
CC       COPS8. In the complex, it probably interacts directly with COPS1,
CC       COPS4 and COPS8. Interacts with CK2 and PKD. Interacts with the
CC       translation initiation factor EIF3S6 and IKBKG (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Embryos arrest after 5.5 dpc and resorb by
CC       8.5 dpc mainly due to increased cell death.
CC   -!- SIMILARITY: Belongs to the CSN3 family.
CC   -!- SIMILARITY: Contains 1 PCI domain.
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DR   EMBL; AF071313; AAC33900.1; -; mRNA.
DR   EMBL; BC068179; AAH68179.1; -; mRNA.
DR   IPI; IPI00131870; -.
DR   RefSeq; NP_036121.1; NM_011991.1.
DR   UniGene; Mm.40; -.
DR   ProteinModelPortal; O88543; -.
DR   STRING; O88543; -.
DR   PhosphoSite; O88543; -.
DR   PRIDE; O88543; -.
DR   Ensembl; ENSMUST00000019517; ENSMUSP00000019517; ENSMUSG00000019373.
DR   GeneID; 26572; -.
DR   KEGG; mmu:26572; -.
DR   UCSC; uc007jfa.1; mouse.
DR   CTD; 26572; -.
DR   MGI; MGI:1349409; Cops3.
DR   eggNOG; roNOG07719; -.
DR   HOGENOM; HBG412084; -.
DR   HOVERGEN; HBG051135; -.
DR   InParanoid; O88543; -.
DR   OMA; ALYFFEV; -.
DR   OrthoDB; EOG49KFQJ; -.
DR   PhylomeDB; O88543; -.
DR   NextBio; 304659; -.
DR   ArrayExpress; O88543; -.
DR   Bgee; O88543; -.
DR   CleanEx; MM_CSN3; -.
DR   Genevestigator; O88543; -.
DR   GermOnline; ENSMUSG00000019373; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008180; C:signalosome; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 2.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Signalosome.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    423       COP9 signalosome complex subunit 3.
FT                                /FTId=PRO_0000120979.
FT   DOMAIN      195    362       PCI.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     410    410       Phosphoserine (By similarity).
FT   MOD_RES     421    421       Phosphoserine (By similarity).
FT   MOD_RES     423    423       Phosphoserine (By similarity).
SQ   SEQUENCE   423 AA;  47832 MW;  2FDCCDB98A5168FB CRC64;
     MASALEQFVN SVRQLSAQGQ MTQLCELINK SGELLAKNLS HLDTVLGALD VQEHSLGVLA
     VLFVKFSMPS VPDFETLFSQ VQLFISTCNG EHIRYATDTF AGLCHQLTNA LVERKQPLRG
     IGILKQAIDK MQMNTNQLTS VHADLCQLCL LAKCFKPALP YLDVDMMDIC KENGAYDAKH
     FLCYYYYGGM IYTGLKNFER ALYFYEQAIT TPAMAVSHIM LESYKKYILV SLILLGKVQQ
     LPKYTSQIVG RFIKPLSNAY HELAQVYSTN NPSELRNLVS KHSETFTRDN NMGLVKQCLS
     SLYKKNIQRL TKTFLTLSLQ DMASRVQLSG PQEAEKYVLH MIEDGEIFAS INQKDGMVSF
     HDNPEKYNNP AMLHNIDQEM LKCIELDERL KAMDQEITVN PQFVQKSMGS QEDDSGNKPS
     SYS
//
ID   AXN2_MOUSE              Reviewed;         840 AA.
AC   O88566; Q9QXJ6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Axin-2;
DE   AltName: Full=Axin-like protein;
DE            Short=Axil;
DE   AltName: Full=Axis inhibition protein 2;
DE   AltName: Full=Conductin;
GN   Name=Axin2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98221239; PubMed=9554852; DOI=10.1126/science.280.5363.596;
RA   Behrens J., Jerchow B.-A., Wuertele M., Grimm J., Asbrand C.,
RA   Wirtz R., Kuehl M., Wedlich D., Birchmeier W.;
RT   "Functional interaction of an axin homolog, conductin, with beta-
RT   catenin, APC, and GSK3beta.";
RL   Science 280:596-599(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Zhang T., Fagotto F., Hsu W., Zeng L., Gilbert D., Copeland N.G.,
RA   Jenkins N.A., Warburton D., Costantini F.;
RT   "Properties of mouse Axin2 and human AXIN2: chromosomal location,
RT   expression pattern, interaction with Axin and effects on embryonic
RT   axis formation.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INTERACTION WITH ANKRD6.
RX   MEDLINE=22170692; PubMed=12183362; DOI=10.1101/gad.230402;
RA   Schwarz-Romond T., Asbrand C., Bakkers J., Kuehl M., Schaeffer H.J.,
RA   Huelsken J., Behrens J., Hammerschmidt M., Birchmeier W.;
RT   "The ankyrin repeat protein diversin recruits casein kinase Iepsilon
RT   to the beta-catenin degradation complex and acts in both canonical Wnt
RT   and Wnt/JNK signaling.";
RL   Genes Dev. 16:2073-2084(2002).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-460 AND SER-464, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Inhibitor of the Wnt signaling pathway. Down-regulates
CC       beta-catenin. Probably facilitate the phosphorylation of beta-
CC       catenin and APC by GSK3B (By similarity).
CC   -!- SUBUNIT: Interacts with glycogen synthase kinase-3 beta (GSK3B)
CC       and beta-catenin. The interaction between axin and beta-catenin
CC       occurs via the armadillo repeats contained in beta-catenin.
CC       Interacts with SMAD7 and RNF111 (By similarity). Interacts with
CC       ANKRD6.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- PTM: Probably phosphorylated by GSK3B and dephosphorylated by PP2A
CC       (By similarity).
CC   -!- SIMILARITY: Contains 1 DIX domain.
CC   -!- SIMILARITY: Contains 1 RGS domain.
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DR   EMBL; AF073788; AAC26047.1; -; mRNA.
DR   EMBL; AF205889; AAF22800.1; -; mRNA.
DR   IPI; IPI00131981; -.
DR   UniGene; Mm.71710; -.
DR   ProteinModelPortal; O88566; -.
DR   SMR; O88566; 47-203, 761-840.
DR   MINT; MINT-1951339; -.
DR   STRING; O88566; -.
DR   PhosphoSite; O88566; -.
DR   PRIDE; O88566; -.
DR   Ensembl; ENSMUST00000052915; ENSMUSP00000051331; ENSMUSG00000000142.
DR   MGI; MGI:1270862; Axin2.
DR   HOGENOM; HBG714290; -.
DR   HOVERGEN; HBG004324; -.
DR   InParanoid; O88566; -.
DR   OrthoDB; EOG4X3H11; -.
DR   ArrayExpress; O88566; -.
DR   Bgee; O88566; -.
DR   CleanEx; MM_AXIN2; -.
DR   Genevestigator; O88566; -.
DR   GermOnline; ENSMUSG00000000142; Mus musculus.
DR   GO; GO:0005813; C:centrosome; IDA:BHF-UCL.
DR   GO; GO:0070411; F:I-SMAD binding; IPI:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:MGI.
DR   GO; GO:0030282; P:bone mineralization; IMP:MGI.
DR   GO; GO:0008283; P:cell proliferation; IMP:MGI.
DR   GO; GO:0003413; P:chondrocyte differentiation involved in endochondral bone morphogenesis; IMP:MGI.
DR   GO; GO:0001957; P:intramembranous ossification; IMP:MGI.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:MGI.
DR   GO; GO:0070602; P:regulation of centromeric sister chromatid cohesion; IMP:BHF-UCL.
DR   GO; GO:0061181; P:regulation of chondrocyte development; IMP:MGI.
DR   GO; GO:0001756; P:somitogenesis; IDA:MGI.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR014936; Axin_b-cat-bd.
DR   InterPro; IPR001158; DIX.
DR   InterPro; IPR000342; Regulat_G_prot_signal.
DR   InterPro; IPR016137; Regulat_G_prot_signal_superfam.
DR   Pfam; PF08833; Axin_b-cat_bind; 1.
DR   Pfam; PF00778; DIX; 1.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00021; DAX; 1.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48097; Regulat_G_prot_signal_superfam; 1.
DR   PROSITE; PS50841; DIX; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; Tumor suppressor; Wnt signaling pathway.
FT   CHAIN         1    840       Axin-2.
FT                                /FTId=PRO_0000220896.
FT   DOMAIN       81    200       RGS.
FT   DOMAIN      758    840       DIX.
FT   REGION      327    413       Interaction with GSK3B (By similarity).
FT   REGION      413    478       Interaction with beta-catenin (By
FT                                similarity).
FT   COMPBIAS    469    476       Poly-His.
FT   MOD_RES     460    460       Phosphotyrosine.
FT   MOD_RES     464    464       Phosphoserine.
FT   MOD_RES     628    628       Phosphoserine (By similarity).
FT   MOD_RES     637    637       Phosphoserine (By similarity).
FT   CONFLICT    101    101       R -> K (in Ref. 2; AAF22800).
FT   CONFLICT    474    474       H -> Y (in Ref. 2; AAF22800).
FT   CONFLICT    484    484       S -> P (in Ref. 2; AAF22800).
FT   CONFLICT    503    503       F -> S (in Ref. 2; AAF22800).
FT   CONFLICT    603    603       G -> A (in Ref. 2; AAF22800).
SQ   SEQUENCE   840 AA;  92935 MW;  A07D5EFB25DE7277 CRC64;
     MSSAVLVTLL PDPSSSFRED APRPPVPGEE GETPPCQPSV GKVQSTKPMP VSSNARRNED
     GLGEPEGRAS PDSPLTRWTK SLHSLLGDQD GAYLFRTFLE REKCVDTLDF WFACNGFRQM
     NLKDTKTLRV AKAIYKRYIE NNSVVSKQLK PATKTYIRDG IKKQQIGSVM FDQAQTEIQA
     VMEENAYQVF LTSDIYLEYV RSGGENTAYM SNGGLGSLKV LCGYLPTLNE EEEWTCADLK
     CKLSPTVVGL SSKTLRATAS VRSTETAENG FRSFKRSDPV NPYHVGSGYV FAPATSANDS
     ELSSDALTDD SMSMTDSSVD GVPPYRMGSK KQLQREMHRS VKANGQVSLP HFPRTHRLPK
     EMTPVEPAAF AAELISRLEK LKLELESRHS LEERLQQIRE DEEKEGSEQA LSSRDGAPVQ
     HPLALLPSGS YEEDPQTILD DHLSRVLKTP GCQSPGVGRY SPRSRSPDHH HQHHHHQQCH
     TLLSTGGKLP PVAACPLLGG KSFLTKQTTK HVHHHYIHHH AVPKTKEEIE AEATQRVRCL
     CPGGTDYYCY SKCKSHPKAP EPLPGEQFCG SRGGTLPKRN AKGTEPGLAL SARDGGMSSA
     AGGPQLPGEE GDRSQDVWQW MLESERQSKS KPHSAQSIRK SYPLESARAA PGERVSRHHL
     LGASGHSRSV ARAHPFTQDP AMPPLTPPNT LAQLEEACRR LAEVSKPQKQ RCCVASQQRD
     RNHSAAGQAG ASPFANPSLA PEDHKEPKKL ASVHALQASE LVVTYFFCGE EIPYRRMLKA
     QSLTLGHFKE QLSKKGNYRY YFKKASDEFA CGAVFEEIWD DETVLPMYEG RILGKVERID
//
ID   O88568_MOUSE            Unreviewed;       798 AA.
AC   O88568;
DT   01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1998, sequence version 1.
DT   11-JAN-2011, entry version 66.
DE   SubName: Full=Heterogenous nuclear ribonucleoprotein U;
GN   Name=Hnrnpu; Synonyms=Hnrpu, hnRNP U;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Roshon M.J., DeGregori J., Ruley H.E.;
RT   "hnRNP U is required for early embryonic development.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SIMILARITY: Contains 1 SAP domain.
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DR   EMBL; AF073992; AAC26866.1; -; mRNA.
DR   IPI; IPI00458583; -.
DR   UniGene; Mm.86589; -.
DR   HSSP; P06855; 1LTQ.
DR   ProteinModelPortal; O88568; -.
DR   SMR; O88568; 1-48.
DR   STRING; O88568; -.
DR   PhosphoSite; O88568; -.
DR   Ensembl; ENSMUST00000037748; ENSMUSP00000047571; ENSMUSG00000039630.
DR   MGI; MGI:1858195; Hnrnpu.
DR   eggNOG; roNOG11975; -.
DR   HOVERGEN; HBG061101; -.
DR   InParanoid; O88568; -.
DR   ArrayExpress; O88568; -.
DR   Bgee; O88568; -.
DR   Genevestigator; O88568; -.
DR   GO; GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0001906; P:cell killing; IEA:InterPro.
DR   InterPro; IPR001870; B302/SPRY.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR003034; SAP_DNA-bd.
DR   InterPro; IPR018355; SPla/RYanodine_receptor_sg.
DR   InterPro; IPR003877; SPRY_rcpt.
DR   InterPro; IPR010488; Zeta_toxin_P-loop_hydrolase.
DR   Pfam; PF02037; SAP; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF06414; Zeta_toxin; 1.
DR   SMART; SM00513; SAP; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50800; SAP; 1.
PE   1: Evidence at protein level;
KW   Ribonucleoprotein; Viral nucleoprotein; Virion.
SQ   SEQUENCE   798 AA;  87892 MW;  09EC599AB352E27D CRC64;
     MSSSPVNVKK LKVSELKEEL KKRRLSDKGL KADLMDRLQA ALDNEAGGRP AMEPGNGSLD
     LGGDAAGRSG AGLEQEAAAG TEDDEEEEGI SALDGDQMEL GEENGAAGAA DAGAMEEEEA
     ASEDENGDDQ GFQEGEDELG DEEEGAGDEN GHGEQQSQPH SAQQQPSQQR GAGKEAAGKS
     SAPTSLFAVT VAPPGARQGQ QQAGGDGKTE QKGGDKKRGV KRPREDHGRG YFEYIEENKY
     SRAKSPQPPV EEEDEHFDDT VVCLDTYNCD LHFKISRDRL SASSLTMESF AFLWAGGRAS
     YGVSKGKVCF EMKVTEKIPV RHLYTKDIDI HEVRIGWSLT TSGMLLGEEE FSYGYSLKGI
     KTCNCETEDY GEKFDENDVI TCFANFETDE VELSYAKNGQ DLGVAFKISK EVLADRPLFP
     HVLCHNCAVE FNFGQKEKPY FPIPEDCTFI QNVPLEDRVR GPKGPEEKKD CEVVMMIGLP
     GAGKTTWVTK HAAENPGKYN ILGTNTIMDK MMVAGFKKQM ADTGKLNTLL QRAPQCLGKF
     IEIAARKKRN FILDQTNVSA AAQRRKMCLF AGFQRKAVVV CPKDEDYKQR TQKKAEVEGK
     DLPEHAVLKM KGNFTLPEVA ECFDEITYVE LQKEEAQKLL EQYKEESKKA LPPEKKQNTG
     SKKSNKNKSG KNQFNRGGGH RGRGGFNMRG GNFRGGAPGN RGGYNRRGNM PQRGGGGGSG
     GIGYPYPRGP VFPGRGGYSN RGNYNRGGMP NRGNYNQNFR GRGNNRGYKN QSQGYNQWQQ
     GQFWGQKPWS QHYHQGYY
//
ID   ROA2_MOUSE              Reviewed;         353 AA.
AC   O88569; B9EJ02; Q3UVJ5; Q6PCV9; Q8C2A0; Q8CJ71; Q91ZR9; Q9R204;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Heterogeneous nuclear ribonucleoproteins A2/B1;
DE            Short=hnRNP A2/B1;
GN   Name=Hnrnpa2b1; Synonyms=Hnrpa2b1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C3Heb/FeJ; TISSUE=Brain;
RX   MEDLINE=22229189; PubMed=12243756; DOI=10.1006/excr.2002.5604;
RA   Brumwell C., Antolik C., Carson J.H., Barbarese E.;
RT   "Intracellular trafficking of hnRNP A2 in oligodendrocytes.";
RL   Exp. Cell Res. 279:310-320(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=BALB/c;
RX   MEDLINE=22226624; PubMed=12242009; DOI=10.1016/S0378-1119(02)00800-4;
RA   Hatfield J.T., Rothnagel J.A., Smith R.;
RT   "Characterization of the mouse hnRNP A2/B1/B0 gene and identification
RT   of processed pseudogenes.";
RL   Gene 295:33-42(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2).
RX   MEDLINE=22730754; PubMed=12546712; DOI=10.1186/1471-2164-4-2;
RA   Roshon M., DeGregori J.V., Ruley H.E.;
RT   "Gene trap mutagenesis of hnRNP A2/B1: a cryptic 3' splice site in the
RT   neomycin resistance gene allows continued expression of the disrupted
RT   cellular gene.";
RL   BMC Genomics 4:2-2(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Thymus, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PROTEIN SEQUENCE OF 23-38; 47-54; 114-120; 138-147; 154-168; 174-185;
RP   191-200 AND 204-228, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Involved with pre-mRNA processing. Forms complexes
CC       (ribonucleosomes) with at least 20 other different hnRNP and
CC       heterogeneous nuclear RNA in the nucleous (By similarity).
CC   -!- SUBUNIT: Identified in the spliceosome C complex, at least
CC       composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23,
CC       DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1,
CC       GPATC1, HNRNPA1, HNRNPA2B1, HNRPA3, HNRNPC, HNRPF, HNRPH1, HNRPK,
CC       HNRPM, HNRNPR, HNRNPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH,
CC       MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19,
CC       PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1,
CC       SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB,
CC       SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1,
CC       SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and
CC       ZCCHC8. Identified in a mRNP granule complex, at least composed of
CC       ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD,
CC       HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1,
CC       NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8,
CC       RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with
CC       IGF2BP1 (By similarity).
CC   -!- INTERACTION:
CC       P04156:PRNP (xeno); NbExp=1; IntAct=EBI-299636, EBI-977302;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Cytoplasm (By
CC       similarity). Note=Localized in cytoplasmic mRNP granules
CC       containing untranslated mRNAs (By similarity). Component of
CC       ribonucleosomes. Predominantly nucleoplasmic, however isoform 2 is
CC       also found in the cytoplasm of cells in some tissues. Not found in
CC       the nucleolus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=B1;
CC         IsoId=O88569-1; Sequence=Displayed;
CC       Name=2; Synonyms=A2;
CC         IsoId=O88569-2; Sequence=VSP_022595;
CC       Name=3;
CC         IsoId=O88569-3; Sequence=VSP_022595, VSP_025012;
CC   -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF406651; AAK98601.2; -; mRNA.
DR   EMBL; AF452567; AAN16352.1; -; Genomic_DNA.
DR   EMBL; AF073990; AAD29846.1; -; Genomic_DNA.
DR   EMBL; AF073993; AAC26867.1; -; mRNA.
DR   EMBL; AK089012; BAC40700.1; -; mRNA.
DR   EMBL; AK137214; BAE23274.1; -; mRNA.
DR   EMBL; BC059107; AAH59107.1; -; mRNA.
DR   EMBL; BC141253; AAI41254.1; -; mRNA.
DR   IPI; IPI00405058; -.
DR   IPI; IPI00622847; -.
DR   IPI; IPI00828488; -.
DR   RefSeq; NP_058086.2; NM_016806.2.
DR   RefSeq; NP_872591.1; NM_182650.3.
DR   RefSeq; XP_001473875.2; XM_001473825.2.
DR   UniGene; Mm.155896; -.
DR   ProteinModelPortal; O88569; -.
DR   SMR; O88569; 1-193.
DR   IntAct; O88569; 7.
DR   STRING; O88569; -.
DR   PhosphoSite; O88569; -.
DR   SWISS-2DPAGE; O88569; -.
DR   REPRODUCTION-2DPAGE; IPI00405058; -.
DR   REPRODUCTION-2DPAGE; O88569; -.
DR   PRIDE; O88569; -.
DR   Ensembl; ENSMUST00000069949; ENSMUSP00000067491; ENSMUSG00000004980.
DR   Ensembl; ENSMUST00000090002; ENSMUSP00000087453; ENSMUSG00000004980.
DR   Ensembl; ENSMUST00000114459; ENSMUSP00000110103; ENSMUSG00000004980.
DR   Ensembl; ENSMUST00000116609; ENSMUSP00000112308; ENSMUSG00000004980.
DR   GeneID; 100045191; -.
DR   GeneID; 53379; -.
DR   KEGG; mmu:100045191; -.
DR   KEGG; mmu:53379; -.
DR   UCSC; uc009bxn.1; mouse.
DR   CTD; 53379; -.
DR   MGI; MGI:104819; Hnrnpa2b1.
DR   eggNOG; roNOG06874; -.
DR   GeneTree; ENSGT00540000069937; -.
DR   HOVERGEN; HBG002295; -.
DR   OrthoDB; EOG4HQDKF; -.
DR   NextBio; 310199; -.
DR   ArrayExpress; O88569; -.
DR   Bgee; O88569; -.
DR   CleanEx; MM_HNRNPA2B1; -.
DR   Genevestigator; O88569; -.
DR   GermOnline; ENSMUSG00000004980; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030530; C:heterogeneous nuclear ribonucleoprotein complex; ISS:HGNC.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; ISS:HGNC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003723; F:RNA binding; ISS:HGNC.
DR   GO; GO:0043047; F:single-stranded telomeric DNA binding; ISS:HGNC.
DR   GO; GO:0006397; P:mRNA processing; ISS:HGNC.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   GO; GO:0050658; P:RNA transport; ISS:HGNC.
DR   InterPro; IPR021662; HnRNPA1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF11627; HnRNPA1; 1.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm;
KW   Direct protein sequencing; Methylation; mRNA processing;
KW   mRNA splicing; Nucleus; Phosphoprotein; Repeat; Ribonucleoprotein;
KW   RNA-binding; Spliceosome.
FT   CHAIN         1    353       Heterogeneous nuclear ribonucleoproteins
FT                                A2/B1.
FT                                /FTId=PRO_0000081837.
FT   DOMAIN       21    104       RRM 1.
FT   DOMAIN      112    191       RRM 2.
FT   REGION      308    347       Nuclear targeting sequence (By
FT                                similarity).
FT   MOTIF         9     15       Nuclear localization signal (Potential).
FT   COMPBIAS    202    353       Gly-rich.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES       3      3       N6-acetyllysine (By similarity).
FT   MOD_RES      85     85       Phosphoserine.
FT   MOD_RES     104    104       N6,N6-dimethyllysine (By similarity).
FT   MOD_RES     168    168       N6-acetyllysine (By similarity).
FT   MOD_RES     173    173       N6-acetyllysine (By similarity).
FT   MOD_RES     176    176       Phosphothreonine (By similarity).
FT   MOD_RES     203    203       Dimethylated arginine; alternate (By
FT                                similarity).
FT   MOD_RES     203    203       Omega-N-methylarginine; alternate (By
FT                                similarity).
FT   MOD_RES     212    212       Phosphoserine (By similarity).
FT   MOD_RES     213    213       Dimethylated arginine; alternate (By
FT                                similarity).
FT   MOD_RES     213    213       Omega-N-methylarginine; alternate (By
FT                                similarity).
FT   MOD_RES     225    225       Phosphoserine (By similarity).
FT   MOD_RES     259    259       Phosphoserine.
FT   MOD_RES     324    324       Phosphoserine.
FT   MOD_RES     341    341       Phosphoserine (By similarity).
FT   MOD_RES     344    344       Phosphoserine (By similarity).
FT   MOD_RES     347    347       Phosphotyrosine (By similarity).
FT   VAR_SEQ       3     14       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_022595.
FT   VAR_SEQ     252    291       Missing (in isoform 3).
FT                                /FTId=VSP_025012.
FT   CONFLICT    173    173       K -> E (in Ref. 4; BAE23274).
FT   CONFLICT    214    214       G -> V (in Ref. 4; BAE23274).
FT   CONFLICT    299    299       S -> T (in Ref. 3; AAC26867).
SQ   SEQUENCE   353 AA;  37403 MW;  EC387DA3D8E989E4 CRC64;
     MEKTLETVPL ERKKREKEQF RKLFIGGLSF ETTEESLRNY YEQWGKLTDC VVMRDPASKR
     SRGFGFVTFS SMAEVDAAMA ARPHSIDGRV VEPKRAVARE ESGKPGAHVT VKKLFVGGIK
     EDTEEHHLRD YFEEYGKIDT IEIITDRQSG KKRGFGFVTF DDHDPVDKIV LQKYHTINGH
     NAEVRKALSR QEMQEVQSSR SGRGGNFGFG DSRGGGGNFG PGPGSNFRGG SDGYGSGRGF
     GDGYNGYGGG PGGGNFGGSP GYGGGRGGYG GGGPGYGNQG GGYGGGYDNY GGGNYGSGSY
     NDFGNYNQQP SNYGPMKSGN FGGSRNMGGP YGGGNYGPGG SGGSGGYGGR SRY
//
ID   COMT_MOUSE              Reviewed;         265 AA.
AC   O88587;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Catechol O-methyltransferase;
DE            EC=2.1.1.6;
GN   Name=Comt; Synonyms=Comt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98374293; PubMed=9707588; DOI=10.1073/pnas.95.17.9991;
RA   Gogos J.A., Morgan M., Luine V., Santha M., Ogawa S., Pfaff D.,
RA   Karayiorgou M.;
RT   "Catechol-O-methyltransferase-deficient mice exhibit sexually
RT   dimorphic changes in catecholamine levels and behavior.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:9991-9996(1998).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   MUTAGENESIS OF ARG-51.
RX   PubMed=18794526; DOI=10.1073/pnas.0807219105;
RA   Du X., Schwander M., Moresco E.M.Y., Viviani P., Haller C.,
RA   Hildebrand M.S., Pak K., Tarantino L., Roberts A., Richardson H.,
RA   Koob G., Najmabadi H., Ryan A.F., Smith R.J.H., Mueller U.,
RA   Beutler B.;
RT   "A catechol-O-methyltransferase that is essential for auditory
RT   function in mice and humans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:14609-14614(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Catalyzes the O-methylation, and thereby the
CC       inactivation, of catecholamine neurotransmitters and catechol
CC       hormones. Also shortens the biological half-lives of certain
CC       neuroactive drugs, like L-DOPA, alpha-methyl DOPA and
CC       isoproterenol.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + a catechol = S-
CC       adenosyl-L-homocysteine + a guaiacol.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform Soluble: Cytoplasm.
CC   -!- SUBCELLULAR LOCATION: Isoform Membrane-bound: Cell membrane;
CC       Single-pass type II membrane protein; Extracellular side.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Membrane-bound; Synonyms=MB-COMT;
CC         IsoId=O88587-1; Sequence=Displayed;
CC       Name=Soluble; Synonyms=S-COMT;
CC         IsoId=O88587-2; Sequence=VSP_018779;
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       Catechol-O-methyltransferase family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF076156; AAC33334.1; -; mRNA.
DR   IPI; IPI00132076; -.
DR   IPI; IPI00759876; -.
DR   UniGene; Mm.100940; -.
DR   ProteinModelPortal; O88587; -.
DR   SMR; O88587; 47-258.
DR   STRING; O88587; -.
DR   PhosphoSite; O88587; -.
DR   PRIDE; O88587; -.
DR   Ensembl; ENSMUST00000000335; ENSMUSP00000000335; ENSMUSG00000000326.
DR   Ensembl; ENSMUST00000115609; ENSMUSP00000111272; ENSMUSG00000000326.
DR   UCSC; uc007ynu.1; mouse.
DR   MGI; MGI:88470; Comt1.
DR   eggNOG; roNOG14769; -.
DR   HOGENOM; HBG565172; -.
DR   HOVERGEN; HBG005376; -.
DR   InParanoid; O88587; -.
DR   OrthoDB; EOG4G1MH8; -.
DR   BRENDA; 2.1.1.6; 244.
DR   ArrayExpress; O88587; -.
DR   Bgee; O88587; -.
DR   Genevestigator; O88587; -.
DR   GermOnline; ENSMUSG00000000326; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016206; F:catechol O-methyltransferase activity; IDA:MGI.
DR   GO; GO:0016206; F:catechol O-methyltransferase activity; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0009712; P:catechol metabolic process; IMP:MGI.
DR   GO; GO:0042420; P:dopamine catabolic process; IDA:MGI.
DR   GO; GO:0042417; P:dopamine metabolic process; IMP:MGI.
DR   GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR017128; Catechol_O-MeTrfase_euk.
DR   InterPro; IPR002935; O-MeTrfase_3.
DR   PANTHER; PTHR10509; Methyltransf_3; 1.
DR   Pfam; PF01596; Methyltransf_3; 1.
DR   PIRSF; PIRSF037177; Catechol_O-mtfrase_euk; 1.
PE   1: Evidence at protein level;
KW   Alternative initiation; Catecholamine metabolism; Cell membrane;
KW   Cytoplasm; Magnesium; Membrane; Metal-binding; Methyltransferase;
KW   Neurotransmitter degradation; Phosphoprotein; S-adenosyl-L-methionine;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN         1    265       Catechol O-methyltransferase.
FT                                /FTId=PRO_0000020973.
FT   TRANSMEM      3     19       Helical; Signal-anchor for type II
FT                                membrane protein; (Potential).
FT   REGION      160    163       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   METAL       184    184       Magnesium (By similarity).
FT   METAL       212    212       Magnesium (By similarity).
FT   METAL       213    213       Magnesium (By similarity).
FT   BINDING      85     85       S-adenosyl-L-methionine; via amide
FT                                nitrogen (By similarity).
FT   BINDING     115    115       S-adenosyl-L-methionine (By similarity).
FT   BINDING     133    133       S-adenosyl-L-methionine (By similarity).
FT   BINDING     184    184       S-adenosyl-L-methionine (By similarity).
FT   BINDING     187    187       Substrate (By similarity).
FT   BINDING     213    213       Substrate (By similarity).
FT   BINDING     242    242       Substrate (By similarity).
FT   MOD_RES     261    261       Phosphoserine.
FT   VAR_SEQ       1     43       Missing (in isoform Soluble).
FT                                /FTId=VSP_018779.
FT   MUTAGEN      51     51       R->L: Reduces methyltransferase activity
FT                                against norepinephrine.
SQ   SEQUENCE   265 AA;  29496 MW;  781260C8CA2899CD CRC64;
     MLLAAVSLGL LLLAFLLLLR HLGWGLVAIG WFEFVQQPVH NLLMGGTKEQ RILRHVQQHA
     KPGDPQSVLE AIDTYCSEKE WAMNVGDAKG QIMDAVIREY RPSLVLELGA YCGYSAVRMA
     RLLPPGARLL TMEINPDYAA ITQQMLDFAG LQDKVSILIG APQDLIPQLK KKYDVDTLDM
     VFLDHWKDRY LPDTLLLEEC GLLRKGTVLL ADNVIVPGTP DFLAYVRGSS SFECTHYSSY
     LEYMKVVDGL EKAVYQGPGS SPVKS
//
ID   CCG2_MOUSE              Reviewed;         323 AA.
AC   O88602;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Voltage-dependent calcium channel gamma-2 subunit;
DE   AltName: Full=Neuronal voltage-gated calcium channel gamma-2 subunit;
DE   AltName: Full=Stargazin;
GN   Name=Cacng2; Synonyms=Stg;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=98361159; PubMed=9697694; DOI=10.1038/1228;
RA   Letts V.A., Felix R., Biddlecome G.H., Arikkath J., Mahaffey C.L.,
RA   Valenzuela A., Bartlett F.S. II, Mori Y., Campbell K.P., Frankel W.N.;
RT   "The mouse stargazer gene encodes a neuronal Ca2+-channel gamma
RT   subunit.";
RL   Nat. Genet. 19:340-347(1998).
RN   [2]
RP   PHOSPHORYLATION AT THR-321, INTERACTION WITH DLG1 AND DLG4, AND
RP   MUTAGENESIS OF THR-321 AND VAL-323.
RX   MEDLINE=21922834; PubMed=11805122; DOI=10.1074/jbc.M200528200;
RA   Choi J., Ko J., Park E., Lee J.-R., Yoon J., Lim S., Kim E.;
RT   "Phosphorylation of stargazin by protein kinase A regulates its
RT   interaction with PSD-95.";
RL   J. Biol. Chem. 277:12359-12363(2002).
RN   [3]
RP   INTERACTION WITH GOPC.
RX   PubMed=15136571; DOI=10.1074/jbc.M402214200;
RA   Ives J.H., Fung S., Tiwari P., Payne H.L., Thompson C.L.;
RT   "Microtubule-associated protein light chain 2 is a stargazin-AMPA
RT   receptor complex-interacting protein in vivo.";
RL   J. Biol. Chem. 279:31002-31009(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-271, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Thought to stabilize the calcium channel in an
CC       inactivated (closed) state.
CC   -!- SUBUNIT: The L-type calcium channel is composed of five subunits:
CC       alpha-1, alpha-2/delta, beta and gamma. Interacts with the PDZ
CC       domains of DLG4/PSD-95 and DLG1/SAP97. May interact with GOPC.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Brain.
CC   -!- PTM: Phosphorylation of Thr-321 by PKA impairs interaction with
CC       DLG1 and DLG4.
CC   -!- DISEASE: Note=Defects in Cacng2 cause the stargazer (stg)
CC       phenotype. Stg mice have spike-wave seizures characteristic of
CC       absence epilepsy, with accompanying defects in the cerebellum and
CC       inner ear.
CC   -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG
CC       subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF077739; AAC40201.1; -; mRNA.
DR   IPI; IPI00132786; -.
DR   RefSeq; NP_031609.1; NM_007583.2.
DR   UniGene; Mm.277338; -.
DR   UniGene; Mm.400802; -.
DR   ProteinModelPortal; O88602; -.
DR   STRING; O88602; -.
DR   PhosphoSite; O88602; -.
DR   PRIDE; O88602; -.
DR   Ensembl; ENSMUST00000019290; ENSMUSP00000019290; ENSMUSG00000019146.
DR   GeneID; 12300; -.
DR   KEGG; mmu:12300; -.
DR   UCSC; uc007wop.1; mouse.
DR   CTD; 12300; -.
DR   MGI; MGI:1316660; Cacng2.
DR   eggNOG; roNOG06471; -.
DR   HOGENOM; HBG564649; -.
DR   HOVERGEN; HBG003682; -.
DR   InParanoid; O88602; -.
DR   OMA; ANARATD; -.
DR   OrthoDB; EOG4P5K9M; -.
DR   PhylomeDB; O88602; -.
DR   NextBio; 280822; -.
DR   ArrayExpress; O88602; -.
DR   Bgee; O88602; -.
DR   Genevestigator; O88602; -.
DR   GermOnline; ENSMUSG00000019146; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IMP:MGI.
DR   GO; GO:0051899; P:membrane depolarization; IMP:MGI.
DR   GO; GO:0060081; P:membrane hyperpolarization; IMP:MGI.
DR   GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
DR   GO; GO:0019226; P:transmission of nerve impulse; IGI:MGI.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   InterPro; IPR005422; VDCC_g2su.
DR   InterPro; IPR008368; VDCC_gsu.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01792; VDCCGAMMA.
DR   PRINTS; PR01602; VDCCGAMMA2.
PE   1: Evidence at protein level;
KW   Calcium; Calcium channel; Calcium transport; Ion transport;
KW   Ionic channel; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    323       Voltage-dependent calcium channel gamma-2
FT                                subunit.
FT                                /FTId=PRO_0000164674.
FT   TRANSMEM     10     30       Helical; (Potential).
FT   TRANSMEM    104    124       Helical; (Potential).
FT   TRANSMEM    134    154       Helical; (Potential).
FT   TRANSMEM    182    202       Helical; (Potential).
FT   MOD_RES     253    253       Phosphoserine.
FT   MOD_RES     271    271       Phosphotyrosine.
FT   MOD_RES     321    321       Phosphothreonine; by PKA.
FT   MUTAGEN     321    321       T->A: Abolishes phosphorylation.
FT   MUTAGEN     321    321       T->D,E: No interaction with DLG1 and
FT                                DLG4.
FT   MUTAGEN     323    323       V->A: No interaction with DLG1 and DLG4.
SQ   SEQUENCE   323 AA;  35895 MW;  AA9D475606A0FBA4 CRC64;
     MGLFDRGVQM LLTTVGAFAA FSLMTIAVGT DYWLYSRGVC KTKSVSENET SKKNEEVMTH
     SGLWRTCCLE GNFKGLCKQI DHFPEDADYE ADTAEYFLRA VRASSIFPIL SVILLFMGGL
     CIAASEFYKT RHNIILSAGI FFVSAGLSNI IGIIVYISAN AGDPSKSDSK KNSYSYGWSF
     YFGALSFIIA EMVGVLAVHM FIDRHKQLRA TARATDYLQA SAITRIPSYR YRYQRRSRSS
     SRSTEPSHSR DASPVGVKGF NTLPSTEISM YTLSRDPLKA ATTPTATYNS DRDNSFLQVH
     NCIQKDSKDS LHANTANRRT TPV
//
ID   PARG_MOUSE              Reviewed;         969 AA.
AC   O88622; Q80YQ6; Q8CB72;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 2.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Poly(ADP-ribose) glycohydrolase;
DE            EC=3.2.1.143;
GN   Name=Parg;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=99380098; PubMed=10449915;
RA   Ame J.-C., Apiou F., Jacobson E.L., Jacobson M.K.;
RT   "Assignment of the poly(ADP-ribose) glycohydrolase gene (PARG) to
RT   human chromosome 10q11.23 and mouse chromosome 14B by in situ
RT   hybridization.";
RL   Cytogenet. Cell Genet. 85:269-270(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Bone;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135; SER-256 AND
RP   SER-259, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Poly(ADP-ribose) synthesized after DNA damage is only
CC       present transiently and is rapidly degraded by poly(ADP-ribose)
CC       glycohydrolase. Poly(ADP-ribose) metabolism may be required for
CC       maintenance of the normal function of neuronal cells.
CC   -!- CATALYTIC ACTIVITY: Hydrolyzes poly(ADP-ribose) at glycosidic
CC       (1''-2') linkage of ribose-ribose bond to produce free ADP-ribose.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O88622-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O88622-2; Sequence=VSP_011771, VSP_011772;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the poly(ADP-ribose) glycohydrolase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BC050892; Type=Erroneous termination; Positions=962; Note=Translated as Met;
CC       Sequence=BC059827; Type=Erroneous termination; Positions=962; Note=Translated as Met;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF079557; AAC28735.1; -; mRNA.
DR   EMBL; AK036656; BAC29519.1; -; mRNA.
DR   EMBL; BC050892; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC059827; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00471055; -.
DR   IPI; IPI00471056; -.
DR   UniGene; Mm.15962; -.
DR   STRING; O88622; -.
DR   PhosphoSite; O88622; -.
DR   PRIDE; O88622; -.
DR   Ensembl; ENSMUST00000022470; ENSMUSP00000022470; ENSMUSG00000021911.
DR   UCSC; uc007syq.1; mouse.
DR   MGI; MGI:1347094; Parg.
DR   eggNOG; roNOG06680; -.
DR   HOGENOM; HBG282387; -.
DR   HOVERGEN; HBG053510; -.
DR   InParanoid; O88622; -.
DR   OrthoDB; EOG4KPT9V; -.
DR   BRENDA; 3.2.1.143; 244.
DR   ArrayExpress; O88622; -.
DR   Bgee; O88622; -.
DR   CleanEx; MM_PARG; -.
DR   Genevestigator; O88622; -.
DR   GermOnline; ENSMUSG00000021911; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IMP:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0004649; F:poly(ADP-ribose) glycohydrolase activity; IMP:MGI.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0016045; P:detection of bacterium; IMP:MGI.
DR   GO; GO:0006974; P:response to DNA damage stimulus; IMP:MGI.
DR   InterPro; IPR007724; Poly_GlycHdrlase.
DR   PANTHER; PTHR12837; Poly_glchydro; 1.
DR   Pfam; PF05028; PARG_cat; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Hydrolase; Nucleus; Phosphoprotein.
FT   CHAIN         1    969       Poly(ADP-ribose) glycohydrolase.
FT                                /FTId=PRO_0000066603.
FT   MOTIF        10     16       Nuclear localization signal (By
FT                                similarity).
FT   MOD_RES     135    135       Phosphoserine.
FT   MOD_RES     137    137       Phosphothreonine (By similarity).
FT   MOD_RES     195    195       Phosphoserine (By similarity).
FT   MOD_RES     197    197       Phosphothreonine (By similarity).
FT   MOD_RES     256    256       Phosphoserine.
FT   MOD_RES     259    259       Phosphoserine.
FT   MOD_RES     311    311       Phosphoserine (By similarity).
FT   MOD_RES     496    496       N6-acetyllysine (By similarity).
FT   VAR_SEQ     920    920       K -> E (in isoform 2).
FT                                /FTId=VSP_011771.
FT   VAR_SEQ     921    969       Missing (in isoform 2).
FT                                /FTId=VSP_011772.
FT   CONFLICT     13     14       RP -> A (in Ref. 1; AAC28735).
FT   CONFLICT    305    305       K -> R (in Ref. 1; AAC28735).
FT   CONFLICT    370    370       A -> V (in Ref. 3; BC050892/BC059827).
FT   CONFLICT    872    872       A -> V (in Ref. 2; BAC29519).
SQ   SEQUENCE   969 AA;  109324 MW;  2626996A53AC48ED CRC64;
     MSAGPGWEPC TKRPRWGAAG TSAPTASDSR SFPGRQRRVL DPKDAPVQFR VPPSSPACVS
     GRAGPHRGNA TSFVFKQKTI TTWMDTKGPK TAESESKENN NTRIDSMMSS VQKDNFYPHK
     VEKLENVPQL NLDKSPTEKS SQYLNQQQTA SVCKWQNEGK HAEQLLASEP PAGTPLPKQL
     SNANIGQSPH TDDHSDTDHE EDRDNQQFLT PIKLANTKPT VGDGQARSNC KCSGSRQSVK
     DCTGCQQEEV DVLPESPLSD VGAEDIGTGP KNDNKLTGQE SSLGDSPPFE KESEPESPMD
     VDNSKNSCQD SEADEETSPV FDEQDDRSSQ TANKLSSCQA READGDLRKR YLTKGSEVRL
     HFQFEGENNA GTSDLNAKPS GNSSSLNVEC RSSKQHGKRD SKITDHFMRI SKSEDRRKEQ
     CEVRHQRTER KIPKYIPPNL PPEKKWLGTP IEEMRKMPRC GIHLPSLRPS ASHTVTVRVD
     LLRAGEVPKP FPTHYKDLWD NKHVKMPCSE QNLYPVEDEN GERTAGSRWE LIQTALLNKF
     TRPQNLKDAI LKYNVAYSKK WDFTALVDFW DKVLEEAEAQ HLYQSILPDM VKIALCLPNI
     CTQPIPLLKQ KMNHSVTMSQ EQIASLLANA FFCTFPRRNA KMKSEYSSYP DINFNRLFEG
     RSSRKPEKLK TLFCYFRRVT EKKPTGLVTF TRQSLEDFPE WERCEKPLTR LHVTYEGTIE
     GNGRGMLQVD FANRFVGGGV TGAGLVQEEI RFLINPELIV SRLFTEVLDH NECLIITGTE
     QYSEYTGYAE TYRWARSHED GSEKDDWQRR CTEIVAIDAL HFRRYLDQFV PEKVRRELNK
     AYCGFLRPGV PSENLSAVAT GNWGCGAFGG DARLKALIQI LAAAAAERDV VYFTFGDSEL
     MRDIYSMHTF LTERKLDVGK VYKLLLRYYN EECRNCSTPG PDIKLYPFIY HAVESSAETT
     DMPGQKAGT
//
ID   PAK1_MOUSE              Reviewed;         545 AA.
AC   O88643;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 103.
DE   RecName: Full=Serine/threonine-protein kinase PAK 1;
DE            EC=2.7.11.1;
DE   AltName: Full=Alpha-PAK;
DE   AltName: Full=CDC42/RAC effector kinase PAK-A;
DE   AltName: Full=p21-activated kinase 1;
DE            Short=PAK-1;
DE   AltName: Full=p65-PAK;
GN   Name=Pak1; Synonyms=Paka;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99282526; PubMed=10352232; DOI=10.1016/S0378-1119(99)00110-9;
RA   Burbelo P.D., Kozak C.A., Finegold A.A., Hall A., Pirone D.M.;
RT   "Cloning, central nervous system expression and chromosomal mapping of
RT   the mouse PAK-1 and PAK-3 genes.";
RL   Gene 232:209-215(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 204-215; 276-299; 309-320; 372-388 AND 472-489,
RP   AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [3]
RP   INTERACTION WITH NISCH.
RX   PubMed=15229651; DOI=10.1038/sj.emboj.7600291;
RA   Alahari S.K., Reddig P.J., Juliano R.L.;
RT   "The integrin-binding protein Nischarin regulates cell migration by
RT   inhibiting PAK.";
RL   EMBO J. 23:2777-2788(2004).
RN   [4]
RP   INTERACTION WITH DSCAM.
RX   PubMed=15169762; DOI=10.1074/jbc.M401878200;
RA   Li W., Guan K.L.;
RT   "The Down syndrome cell adhesion molecule (DSCAM) interacts with and
RT   activates Pak.";
RL   J. Biol. Chem. 279:32824-32831(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-212; SER-223 AND
RP   THR-225, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-423, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   INTERACTION WITH SCRIB.
RX   PubMed=18716323; DOI=10.1093/hmg/ddn248;
RA   Nola S., Sebbagh M., Marchetto S., Osmani N., Nourry C., Audebert S.,
RA   Navarro C., Rachel R., Montcouquiol M., Sans N.,
RA   Etienne-Manneville S., Borg J.-P., Santoni M.-J.;
RT   "Scrib regulates PAK activity during the cell migration process.";
RL   Hum. Mol. Genet. 17:3552-3565(2008).
CC   -!- FUNCTION: The activated kinase acts on a variety of targets.
CC       Likely to be the GTPase effector that links the Rho-related
CC       GTPases to the JNK MAP kinase pathway. Activated by CDC42 and
CC       RAC1. Involved in dissolution of stress fibers and reorganization
CC       of focal complexes. Involved in regulation of microtubule
CC       biogenesis through phosphorylation of TBCB. Activity is inhibited
CC       in cells undergoing apoptosis, potentially due to binding of
CC       CDC2L1 and CDC2L2 (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activated by binding small G proteins. Binding
CC       of GTP-bound CDC42 or RAC1 to the autoregulatory region releases
CC       monomers from the autoinhibited dimer, enables phosphorylation of
CC       Thr-423 and allows the kinase domain to adopt an active structure.
CC       Also activated by binding to GTP-bound CDC42, independent of the
CC       phosphorylation state of Thr-423. Phosphorylation of Thr-84 by
CC       OXSR1 inhibits this activation (By similarity).
CC   -!- SUBUNIT: Homodimer in its autoinhibited state. Active as monomer.
CC       Interacts tightly with GTP-bound but not GDP-bound CDC42/P21 and
CC       RAC1. Binds to the caspase-cleaved p110 isoform of CDC2L1 and
CC       CDC2L2, p110C, but not the full-length proteins. Component of
CC       cytoplasmic complexes, which also contain PXN, ARHGEF6 and GIT1.
CC       Interacts with ARHGEF7. Also interacts with CRIPAK. Probably found
CC       in a ternary complex composed of DSCAM, PAK1 and RAC1. Interacts
CC       with DSCAM (via cytoplasmic domain); the interaction is direct and
CC       enhanced in presence of RAC1 (By similarity). Interacts with DSCAM
CC       and NISCH. Interacts with SCRIB.
CC   -!- INTERACTION:
CC       P60953:CDC42 (xeno); NbExp=1; IntAct=EBI-457240, EBI-81752;
CC       P60766-2:Cdc42; NbExp=2; IntAct=EBI-457240, EBI-287404;
CC       P63000:RAC1 (xeno); NbExp=1; IntAct=EBI-457240, EBI-413628;
CC   -!- PTM: Autophosphorylated when activated by CDC42/p21 and RAC1 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC   -!- SIMILARITY: Contains 1 CRIB domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF082077; AAC32375.1; -; mRNA.
DR   IPI; IPI00132993; -.
DR   UniGene; Mm.260227; -.
DR   ProteinModelPortal; O88643; -.
DR   SMR; O88643; 75-147, 249-541.
DR   DIP; DIP-32847N; -.
DR   IntAct; O88643; 11.
DR   MINT; MINT-193245; -.
DR   STRING; O88643; -.
DR   PhosphoSite; O88643; -.
DR   PRIDE; O88643; -.
DR   Ensembl; ENSMUST00000033040; ENSMUSP00000033040; ENSMUSG00000030774.
DR   UCSC; uc009ijv.1; mouse.
DR   MGI; MGI:1339975; Pak1.
DR   eggNOG; roNOG10184; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108518; -.
DR   InParanoid; O88643; -.
DR   OrthoDB; EOG45DWP5; -.
DR   PhylomeDB; O88643; -.
DR   BRENDA; 2.7.11.1; 244.
DR   ArrayExpress; O88643; -.
DR   Bgee; O88643; -.
DR   CleanEx; MM_PAK1; -.
DR   Genevestigator; O88643; -.
DR   GermOnline; ENSMUSG00000030774; Mus musculus.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0005925; C:focal adhesion; TAS:MGI.
DR   GO; GO:0030426; C:growth cone; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016358; P:dendrite development; IDA:MGI.
DR   GO; GO:0007528; P:neuromuscular junction development; IGI:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0043113; P:receptor clustering; IGI:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000095; PAK_box_Rho-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00786; PBD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00285; PBD; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Allosteric enzyme; ATP-binding;
KW   Direct protein sequencing; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    545       Serine/threonine-protein kinase PAK 1.
FT                                /FTId=PRO_0000086461.
FT   DOMAIN       75     88       CRIB.
FT   DOMAIN      270    521       Protein kinase.
FT   NP_BIND     276    284       ATP (By similarity).
FT   REGION       70    140       Autoregulatory region (By similarity).
FT   REGION       70    105       GTPase-binding (By similarity).
FT   REGION      132    270       Interaction with CRIPAK (By similarity).
FT   ACT_SITE    389    389       Proton acceptor (By similarity).
FT   BINDING     299    299       ATP (By similarity).
FT   MOD_RES      21     21       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES      57     57       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES      84     84       Phosphothreonine; by OXSR1 (By
FT                                similarity).
FT   MOD_RES     144    144       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     149    149       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     199    199       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     204    204       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     212    212       Phosphothreonine.
FT   MOD_RES     219    219       Phosphothreonine (By similarity).
FT   MOD_RES     220    220       Phosphoserine.
FT   MOD_RES     223    223       Phosphoserine.
FT   MOD_RES     225    225       Phosphothreonine.
FT   MOD_RES     229    229       Phosphothreonine (By similarity).
FT   MOD_RES     230    230       Phosphothreonine (By similarity).
FT   MOD_RES     256    256       N6-acetyllysine (By similarity).
FT   MOD_RES     423    423       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     474    474       Phosphotyrosine (By similarity).
SQ   SEQUENCE   545 AA;  60737 MW;  A4861289534C3819 CRC64;
     MSNNGVDIQD KPPAPPMRNT STMIGAGSKD TGTLNHGSKP LPPNPEEKKK KDRFYRSILP
     GDKTNKKREK ERPEISLPSD FEHTIHVGFD AVTGEFTGMP EQWARLLQTS NITKSEQKKN
     PQAVLDVLEF YNSKKTSNSK KYMSFTDKSA EDYNSSNTLN VKTVSETPAV PPVSEDDEDD
     DDDATPPPVI APRPEHTKSV YTRSVIEPLP VTPTRDVATS PISPTENNTT PPDALTRNTE
     KQKKKPKMSD EEILEKLRSI VSVGDPKKKY TPFEKIGQGA SGTVYTAMDV ATGQEVAIKQ
     MNLQQQPKKE LIINEILVMR ENKNPNIVNY LDSYLVGDEL WVVMEYLAGG SLTDVVTETC
     MDEGQIAAVC RECLQALEFL HSNQVIHRDI KSDNILLGMD GSVKLTDFGF CAQITPEQSK
     RSTMVGTPYW MAPEVVTRKA YGPKVDIWSL GIMAIEMIEG EPPYLNENPL RALYLIATNG
     TPELQNPEKL SAIFRDFLQC CLEMDVEKRG SAKELLQHQF LKIAKPLSSL TPLMHAAKEA
     TKNNH
//
ID   HCN2_MOUSE              Reviewed;         863 AA.
AC   O88703; O70506;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 103.
DE   RecName: Full=Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2;
DE   AltName: Full=Brain cyclic nucleotide-gated channel 2;
DE            Short=BCNG-2;
DE   AltName: Full=Hyperpolarization-activated cation channel 1;
DE            Short=HAC-1;
GN   Name=Hcn2; Synonyms=Bcng2, Hac1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   STRAIN=BALB/c;
RX   MEDLINE=98295993; PubMed=9634236; DOI=10.1038/31255;
RA   Ludwig A., Zong X., Jeglitsch M., Hofmann F., Biel M.;
RT   "A family of hyperpolarization-activated cation channels.";
RL   Nature 393:587-591(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 150-653, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=98292171; PubMed=9630217; DOI=10.1016/S0092-8674(00)81434-8;
RA   Santoro B., Liu D.T., Yao H., Bartsch D., Kandel E.R.,
RA   Siegelbaum S.A., Tibbs G.R.;
RT   "Identification of a gene encoding a hyperpolarization-activated
RT   'pacemaker' channel of brain.";
RL   Cell 93:717-729(1998).
RN   [3]
RP   MUTAGENESIS OF ASP-225; ASP-231; ASP-267; ASP-275; LYS-291; ARG-294;
RP   ARG-297; ARG-300; LYS-303; SER-306; ARG-309; ARG-312; ARG-315 AND
RP   ARG-318.
RX   MEDLINE=20549672; PubMed=10962006; DOI=10.1074/jbc.M007034200;
RA   Chen J., Mitcheson J.S., Lin M., Sanguinetti M.C.;
RT   "Functional roles of charged residues in the putative voltage sensor
RT   of the HCN2 pacemaker channel.";
RL   J. Biol. Chem. 275:36465-36471(2000).
RN   [4]
RP   INTERACTION WITH KCNE2.
RX   MEDLINE=21313430; PubMed=11420311;
RA   Yu H., Wu J., Potapova I., Wymore R.T., Holmes B., Zuckerman J.,
RA   Pan Z., Wang H., Shi W., Robinson R.B., El-Maghrabi M.R., Benjamin W.,
RA   Dixon J.E., McKinnon D., Cohen I.S., Wymore R.;
RT   "MinK-related peptide 1: a beta subunit for the HCN ion channel
RT   subunit family enhances expression and speeds activation.";
RL   Circ. Res. 88:E84-E87(2001).
RN   [5]
RP   REGULATION BY INTRACELLULAR PH, AND MUTAGENESIS OF HIS-321.
RX   MEDLINE=21125838; PubMed=11096117; DOI=10.1074/jbc.M010326200;
RA   Zong X., Stieber J., Ludwig A., Hofmann F., Biel M.;
RT   "A single histidine residue determines the pH sensitivity of the
RT   pacemaker channel HCN2.";
RL   J. Biol. Chem. 276:6313-6319(2001).
RN   [6]
RP   MUTAGENESIS OF ARG-318; GLU-324; TYR-331 AND ARG-339.
RX   MEDLINE=21457237; PubMed=11553787; DOI=10.1073/pnas.201250598;
RA   Chen J., Mitcheson J.S., Tristani-Firouzi M., Lin M.,
RA   Sanguinetti M.C.;
RT   "The S4-S5 linker couples voltage sensing and activation of pacemaker
RT   channels.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:11277-11282(2001).
RN   [7]
RP   FUNCTION, AND MUTAGENESIS OF SER-306.
RX   MEDLINE=21826463; PubMed=11741901; DOI=10.1074/jbc.M106974200;
RA   Proenza C., Angoli D., Agranovich E., Macri V., Accili E.A.;
RT   "Pacemaker channels produce an instantaneous current.";
RL   J. Biol. Chem. 277:5101-5109(2002).
RN   [8]
RP   OLIGOMERIZATION VIA THE N-TERMINAL DOMAIN.
RX   MEDLINE=22313494; PubMed=12193608; DOI=10.1074/jbc.M208477200;
RA   Tran N., Proenza C., Macri V., Petigara F., Sloan E., Samler S.,
RA   Accili E.A.;
RT   "A conserved domain in the NH2 terminus important for assembly and
RT   functional expression of pacemaker channels.";
RL   J. Biol. Chem. 277:43588-43592(2002).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; SER-750 AND
RP   SER-771, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 443-643 IN COMPLEX WITH CAMP
RP   AND CGMP, AND TETRAMERIZATION.
RX   MEDLINE=22848704; PubMed=12968185; DOI=10.1038/nature01922;
RA   Zagotta W.N., Olivier N.B., Black K.D., Young E.C., Olson R.,
RA   Gouaux E.;
RT   "Structural basis for modulation and agonist specificity of HCN
RT   pacemaker channels.";
RL   Nature 425:200-205(2003).
CC   -!- FUNCTION: Hyperpolarization-activated ion channel exhibiting weak
CC       selectivity for potassium over sodium ions. Contributes to the
CC       native pacemaker currents in heart (If) and in neurons (Ih).
CC       Produces a large instantaneous current. Activated by cAMP.
CC       Modulated by intracellular chloride ions and pH; acidic pH shifts
CC       the activation to more negative voltages.
CC   -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC       heterotetrameric complex of pore-forming subunits. Heteromultimer
CC       with HCN1. Interacts with KCNE2.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain. Detected at low
CC       levels in heart, in ventricle, atrium and in sinoatrial node
CC       (SAN).
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position.
CC   -!- SIMILARITY: Belongs to the potassium channel HCN family.
CC   -!- SIMILARITY: Contains 1 cyclic nucleotide-binding domain.
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DR   EMBL; AJ225122; CAA12406.1; -; mRNA.
DR   EMBL; AF064873; AAC40125.1; -; mRNA.
DR   IPI; IPI00133980; -.
DR   RefSeq; NP_032252.1; NM_008226.2.
DR   UniGene; Mm.12956; -.
DR   PDB; 1Q3E; X-ray; 1.90 A; A/B=443-645.
DR   PDB; 1Q43; X-ray; 2.00 A; A/B=443-645.
DR   PDB; 1Q5O; X-ray; 2.30 A; A=443-645.
DR   PDB; 2Q0A; X-ray; 2.25 A; A/B=443-640.
DR   PDB; 3BPZ; X-ray; 1.65 A; A/B/C/D=443-640.
DR   PDB; 3ETQ; X-ray; 1.90 A; A/B=443-640.
DR   PDB; 3FFQ; X-ray; 2.40 A; A/B=443-640.
DR   PDBsum; 1Q3E; -.
DR   PDBsum; 1Q43; -.
DR   PDBsum; 1Q5O; -.
DR   PDBsum; 2Q0A; -.
DR   PDBsum; 3BPZ; -.
DR   PDBsum; 3ETQ; -.
DR   PDBsum; 3FFQ; -.
DR   ProteinModelPortal; O88703; -.
DR   SMR; O88703; 443-635.
DR   DIP; DIP-29326N; -.
DR   STRING; O88703; -.
DR   PhosphoSite; O88703; -.
DR   PRIDE; O88703; -.
DR   Ensembl; ENSMUST00000020581; ENSMUSP00000020581; ENSMUSG00000020331.
DR   Ensembl; ENSMUST00000099513; ENSMUSP00000097113; ENSMUSG00000020331.
DR   GeneID; 15166; -.
DR   KEGG; mmu:15166; -.
DR   UCSC; uc007fzn.1; mouse.
DR   CTD; 15166; -.
DR   MGI; MGI:1298210; Hcn2.
DR   eggNOG; maNOG05978; -.
DR   GeneTree; ENSGT00600000084322; -.
DR   HOGENOM; HBG447083; -.
DR   HOVERGEN; HBG039489; -.
DR   InParanoid; O88703; -.
DR   OMA; PKVSFSC; -.
DR   OrthoDB; EOG46Q6S8; -.
DR   PhylomeDB; O88703; -.
DR   NextBio; 287670; -.
DR   ArrayExpress; O88703; -.
DR   Bgee; O88703; -.
DR   Genevestigator; O88703; -.
DR   GermOnline; ENSMUSG00000020331; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005272; F:sodium channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR013621; Ion_trans_N.
DR   InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF08412; Ion_trans_N; 1.
DR   PRINTS; PR01463; EAGCHANLFMLY.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; cNMP_binding; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 1.
DR   PROSITE; PS00889; CNMP_BINDING_2; FALSE_NEG.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; cAMP; cAMP-binding; Glycoprotein; Ion transport;
KW   Ionic channel; Ligand-gated ion channel; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Potassium; Potassium channel; Potassium transport;
KW   Sodium; Sodium channel; Sodium transport; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    863       Potassium/sodium hyperpolarization-
FT                                activated cyclic nucleotide-gated channel
FT                                2.
FT                                /FTId=PRO_0000054112.
FT   TOPO_DOM      1    188       Cytoplasmic (Potential).
FT   TRANSMEM    189    209       Helical; Name=Segment S1; (Potential).
FT   TOPO_DOM    210    213       Extracellular (Potential).
FT   TRANSMEM    214    234       Helical; Name=Segment S2; (Potential).
FT   TOPO_DOM    235    261       Cytoplasmic (Potential).
FT   TRANSMEM    262    282       Helical; Name=Segment S3; (Potential).
FT   TOPO_DOM    283    290       Extracellular (Potential).
FT   TRANSMEM    291    311       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TOPO_DOM    312    342       Cytoplasmic (Potential).
FT   TRANSMEM    343    363       Helical; Name=Segment S5; (Potential).
FT   TOPO_DOM    364    386       Extracellular (Potential).
FT   INTRAMEM    387    408       Pore-forming; Name=Segment H5;
FT                                (Potential).
FT   TOPO_DOM    409    413       Extracellular (Potential).
FT   TRANSMEM    414    434       Helical; Name=Segment S6; (Potential).
FT   TOPO_DOM    435    863       Cytoplasmic (Potential).
FT   NP_BIND     517    634       cAMP.
FT   REGION      131    182       Involved in subunit assembly.
FT   COMPBIAS     10     58       Pro-rich.
FT   COMPBIAS    688    835       Pro-rich.
FT   MOD_RES     119    119       Phosphoserine.
FT   MOD_RES     750    750       Phosphoserine.
FT   MOD_RES     771    771       Phosphoserine.
FT   CARBOHYD    380    380       N-linked (GlcNAc...) (Potential).
FT   MUTAGEN     225    225       D->N: Abolishes surface expression and
FT                                channel activity.
FT   MUTAGEN     231    231       D->N: Reduces surface expression and
FT                                abolishes channel activity.
FT   MUTAGEN     267    267       D->N: Reduces surface expression and
FT                                abolishes channel activity.
FT   MUTAGEN     275    275       D->N: Reduces surface expression and
FT                                abolishes channel activity.
FT   MUTAGEN     291    291       K->Q: Shifts voltage dependence of
FT                                activation to more negative values.
FT   MUTAGEN     294    294       R->Q: Shifts voltage dependence of
FT                                activation to more negative values.
FT   MUTAGEN     297    297       R->Q: Shifts voltage dependence of
FT                                activation to more negative values.
FT   MUTAGEN     300    300       R->Q: Shifts voltage dependence of
FT                                activation to more negative values.
FT   MUTAGEN     303    303       K->Q: Decreases current amplitude.
FT   MUTAGEN     306    306       S->Q: Decreases current amplitude.
FT   MUTAGEN     309    309       R->Q: Abolishes surface expression and
FT                                channel activity.
FT   MUTAGEN     312    312       R->Q: Reduces surface expression and
FT                                decreases current amplitude.
FT   MUTAGEN     315    315       R->Q: Reduces surface expression and
FT                                abolishes channel activity.
FT   MUTAGEN     318    318       R->Q: Reduces surface expression and
FT                                disrupts channel closure.
FT   MUTAGEN     321    321       H->E: Shifts voltage dependence of
FT                                activation to more positive values and
FT                                abolishes pH-sensitivity.
FT   MUTAGEN     321    321       H->Q: Abolishes pH-sensitivity.
FT   MUTAGEN     321    321       H->R: Abolishes pH-sensitivity.
FT   MUTAGEN     324    324       E->Q: Disrupts channel closure.
FT   MUTAGEN     331    331       Y->A: Disrupts channel closure.
FT   MUTAGEN     331    331       Y->S: Disrupts channel closure.
FT   MUTAGEN     339    339       R->Q: Disrupts channel closure.
FT   CONFLICT    486    486       F -> S (in Ref. 2; AAC40125).
FT   CONFLICT    642    642       I -> T (in Ref. 2; AAC40125).
FT   HELIX       444    462
FT   HELIX       467    481
FT   HELIX       488    494
FT   HELIX       497    507
FT   HELIX       509    514
FT   HELIX       516    519
FT   HELIX       523    530
FT   STRAND      534    538
FT   STRAND      543    545
FT   STRAND      553    559
FT   STRAND      562    565
FT   STRAND      571    574
FT   HELIX       582    587
FT   STRAND      592    599
FT   STRAND      601    607
FT   HELIX       608    617
FT   HELIX       619    621
FT   HELIX       622    633
SQ   SEQUENCE   863 AA;  94722 MW;  17CDC4DFF07AC039 CRC64;
     MDARGGGGRP GDSPGTTPAP GPPPPPPPPA PPQPQPPPAP PPNPTTPSHP ESADEPGPRA
     RLCSRDSACT PGAAKGGANG ECGRGEPQCS PEGPARGPKV SFSCRGAASG PSAAEEAGSE
     EAGPAGEPRG SQASFLQRQF GALLQPGVNK FSLRMFGSQK AVEREQERVK SAGAWIIHPY
     SDFRFYWDFT MLLFMVGNLI IIPVGITFFK DETTAPWIVF NVVSDTFFLM DLVLNFRTGI
     VIEDNTEIIL DPEKIKKKYL RTWFVVDFVS SIPVDYIFLI VEKGIDSEVY KTARALRIVR
     FTKILSLLRL LRLSRLIRYI HQWEEIFHMT YDLASAVMRI CNLISMMLLL CHWDGCLQFL
     VPMLQDFPSD CWVSINNMVN HSWSELYSFA LFKAMSHMLC IGYGRQAPES MTDIWLTMLS
     MIVGATCYAM FIGHATALIQ SLDSSRRQYQ EKYKQVEQYM SFHKLPADFR QKIHDYYEHR
     YQGKMFDEDS ILGELNGPLR EEIVNFNCRK LVASMPLFAN ADPNFVTAML TKLKFEVFQP
     GDYIIREGTI GKKMYFIQHG VVSVLTKGNK EMKLSDGSYF GEICLLTRGR RTASVRADTY
     CRLYSLSVDN FNEVLEEYPM MRRAFETVAI DRLDRIGKKN SILLHKVQHD LSSGVFNNQE
     NAIIQEIVKY DREMVQQAEL GQRVGLFPPP PPPQVTSAIA TLQQAVAMSF CPQVARPLVG
     PLALGSPRLV RRAPPGPLPP AASPGPPAAS PPAAPSSPRA PRTSPYGVPG SPATRVGPAL
     PARRLSRASR PLSASQPSLP HGVPAPSPAA SARPASSSTP RLGPAPTART AAPSPDRRDS
     ASPGAASGLD PLDSARSRLS SNL
//
ID   HCN1_MOUSE              Reviewed;         910 AA.
AC   O88704; O54899; Q9D613;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 102.
DE   RecName: Full=Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1;
DE   AltName: Full=Brain cyclic nucleotide-gated channel 1;
DE            Short=BCNG-1;
DE   AltName: Full=Hyperpolarization-activated cation channel 2;
DE            Short=HAC-2;
GN   Name=Hcn1; Synonyms=Bcng1, Hac2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND GLYCOSYLATION.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   MEDLINE=98070835; PubMed=9405696; DOI=10.1073/pnas.94.26.14815;
RA   Santoro B., Grant S.G.N., Bartsch D., Kandel E.R.;
RT   "Interactive cloning with the SH3 domain of N-src identifies a new
RT   brain specific ion channel protein, with homology to eag and cyclic
RT   nucleotide-gated channels.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:14815-14820(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=98295993; PubMed=9634236; DOI=10.1038/31255;
RA   Ludwig A., Zong X., Jeglitsch M., Hofmann F., Biel M.;
RT   "A family of hyperpolarization-activated cation channels.";
RL   Nature 393:587-591(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 377-910.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   FUNCTION, AND REGULATION BY CAMP.
RX   MEDLINE=98292171; PubMed=9630217; DOI=10.1016/S0092-8674(00)81434-8;
RA   Santoro B., Liu D.T., Yao H., Bartsch D., Kandel E.R.,
RA   Siegelbaum S.A., Tibbs G.R.;
RT   "Identification of a gene encoding a hyperpolarization-activated
RT   'pacemaker' channel of brain.";
RL   Cell 93:717-729(1998).
RN   [5]
RP   INTERACTION WITH KCNE2.
RX   MEDLINE=21313430; PubMed=11420311;
RA   Yu H., Wu J., Potapova I., Wymore R.T., Holmes B., Zuckerman J.,
RA   Pan Z., Wang H., Shi W., Robinson R.B., El-Maghrabi M.R., Benjamin W.,
RA   Dixon J.E., McKinnon D., Cohen I.S., Wymore R.;
RT   "MinK-related peptide 1: a beta subunit for the HCN ion channel
RT   subunit family enhances expression and speeds activation.";
RL   Circ. Res. 88:E84-E87(2001).
RN   [6]
RP   REGULATION BY CAMP.
RX   MEDLINE=21351681; PubMed=11459060; DOI=10.1038/35081088;
RA   Wainger B.J., DeGennaro M., Santoro B., Siegelbaum S.A., Tibbs G.R.;
RT   "Molecular mechanism of cAMP modulation of HCN pacemaker channels.";
RL   Nature 411:805-810(2001).
RN   [7]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   MEDLINE=21530492; PubMed=11675786; DOI=10.1038/35098087;
RA   Stevens D.R., Seifert R., Bufe B., Mueller F., Kremmer E., Gauss R.,
RA   Meyerhof W., Kaupp U.B., Lindemann B.;
RT   "Hyperpolarization-activated channels HCN1 and HCN4 mediate responses
RT   to sour stimuli.";
RL   Nature 413:631-635(2001).
RN   [8]
RP   INTERACTION WITH HCN2, AND MUTAGENESIS OF GLY-349; TYR-350 AND
RP   GLY-351.
RX   MEDLINE=22083667; PubMed=12089064;
RX   DOI=10.1161/01.RES.0000024390.97889.C6;
RA   Xue T., Marban E., Li R.A.;
RT   "Dominant-negative suppression of HCN1- and HCN2-encoded pacemaker
RT   currents by an engineered HCN1 construct: insights into structure-
RT   function relationships and multimerization.";
RL   Circ. Res. 90:1267-1273(2002).
RN   [9]
RP   OLIGOMERIZATION VIA N-TERMINAL DOMAIN.
RX   MEDLINE=22162449; PubMed=12034718; DOI=10.1074/jbc.M200504200;
RA   Proenza C., Tran N., Angoli D., Zahynacz K., Balcar P., Accili E.A.;
RT   "Different roles for the cyclic nucleotide binding domain and amino
RT   terminus in assembly and expression of hyperpolarization-activated,
RT   cyclic nucleotide-gated channels.";
RL   J. Biol. Chem. 277:29634-29642(2002).
RN   [10]
RP   MUTAGENESIS OF CYS-303 AND CYS-318.
RX   MEDLINE=22336443; PubMed=12351622; DOI=10.1074/jbc.M204915200;
RA   Xue T., Li R.A.;
RT   "An external determinant in the S5-P linker of the pacemaker (HCN)
RT   channel identified by sulfhydryl modification.";
RL   J. Biol. Chem. 277:46233-46242(2002).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-39 AND SER-69, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Hyperpolarization-activated ion channel exhibiting weak
CC       selectivity for potassium over sodium ions. Contributes to the
CC       native pacemaker currents in heart (If) and in neurons (Ih).
CC       Activated by cAMP, and at 10-100 times higher concentrations, also
CC       by cGMP. May mediate responses to sour stimuli.
CC   -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC       heterotetrameric complex of pore-forming subunits. Heteromultimer
CC       with HCN2. Interacts with KCNE2. Interacts with the SH3 domain of
CC       CSK.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in brain. Highly
CC       expressed in apical dendrites of pyramidal neurons in the cortex,
CC       in the layer corresponding to the stratum lacunosum-moleculare in
CC       the hippocampus and in axons of basket cells in the cerebellum.
CC       Expressed in a subset of elongated cells in taste buds.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position.
CC   -!- PTM: N-glycosylated.
CC   -!- MISCELLANEOUS: Inhibited by extracellular cesium ions.
CC   -!- SIMILARITY: Belongs to the potassium channel HCN family.
CC   -!- SIMILARITY: Contains 1 cyclic nucleotide-binding domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AK014722; Type=Frameshift; Positions=381;
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DR   EMBL; AF028737; AAC53518.1; -; mRNA.
DR   EMBL; AJ225123; CAA12407.1; -; mRNA.
DR   EMBL; AK014722; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00118978; -.
DR   RefSeq; NP_034538.2; NM_010408.3.
DR   UniGene; Mm.343429; -.
DR   ProteinModelPortal; O88704; -.
DR   SMR; O88704; 295-387, 390-582.
DR   STRING; O88704; -.
DR   TCDB; 1.A.1.5.2; voltage-gated ion channel (VIC) superfamily.
DR   PhosphoSite; O88704; -.
DR   PRIDE; O88704; -.
DR   Ensembl; ENSMUST00000006991; ENSMUSP00000006991; ENSMUSG00000021730.
DR   GeneID; 15165; -.
DR   KEGG; mmu:15165; -.
DR   UCSC; uc007ryo.1; mouse.
DR   CTD; 15165; -.
DR   MGI; MGI:1096392; Hcn1.
DR   eggNOG; roNOG13745; -.
DR   GeneTree; ENSGT00600000084322; -.
DR   HOGENOM; HBG447083; -.
DR   HOVERGEN; HBG039489; -.
DR   InParanoid; O88704; -.
DR   OMA; RTFHYSS; -.
DR   OrthoDB; EOG46Q6S8; -.
DR   PhylomeDB; O88704; -.
DR   NextBio; 287666; -.
DR   ArrayExpress; O88704; -.
DR   Bgee; O88704; -.
DR   Genevestigator; O88704; -.
DR   GermOnline; ENSMUSG00000021730; Mus musculus.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0005272; F:sodium channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0045176; P:apical protein localization; IMP:MGI.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR013621; Ion_trans_N.
DR   InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF08412; Ion_trans_N; 1.
DR   PRINTS; PR01463; EAGCHANLFMLY.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; cNMP_binding; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 1.
DR   PROSITE; PS00889; CNMP_BINDING_2; FALSE_NEG.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
PE   1: Evidence at protein level;
KW   cAMP; cAMP-binding; Glycoprotein; Ion transport; Ionic channel;
KW   Ligand-gated ion channel; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Potassium; Potassium channel; Potassium transport;
KW   Sodium; Sodium channel; Sodium transport; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    910       Potassium/sodium hyperpolarization-
FT                                activated cyclic nucleotide-gated channel
FT                                1.
FT                                /FTId=PRO_0000054108.
FT   TOPO_DOM      1    135       Cytoplasmic (Potential).
FT   TRANSMEM    136    156       Helical; Name=Segment S1; (Potential).
FT   TOPO_DOM    157    162       Extracellular (Potential).
FT   TRANSMEM    163    183       Helical; Name=Segment S2; (Potential).
FT   TOPO_DOM    184    208       Cytoplasmic (Potential).
FT   TRANSMEM    209    229       Helical; Name=Segment S3; (Potential).
FT   TOPO_DOM    230    237       Extracellular (Potential).
FT   TRANSMEM    238    258       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TOPO_DOM    259    289       Cytoplasmic (Potential).
FT   TRANSMEM    290    310       Helical; Name=Segment S5; (Potential).
FT   TOPO_DOM    311    333       Extracellular (Potential).
FT   INTRAMEM    334    355       Pore-forming; Name=Segment H5;
FT                                (Potential).
FT   TOPO_DOM    356    360       Extracellular (Potential).
FT   TRANSMEM    361    381       Helical; Name=Segment S6; (Potential).
FT   TOPO_DOM    382    910       Cytoplasmic (Potential).
FT   NP_BIND     464    581       cAMP.
FT   REGION       78    129       Involved in subunit assembly (By
FT                                similarity).
FT   COMPBIAS      1     81       Gly-rich.
FT   COMPBIAS    715    777       Gln-rich.
FT   COMPBIAS    878    884       Poly-Pro.
FT   MOD_RES      39     39       Phosphothreonine.
FT   MOD_RES      69     69       Phosphoserine.
FT   CARBOHYD    327    327       N-linked (GlcNAc...) (Probable).
FT   MUTAGEN     303    303       C->S: Abolishes conductivity.
FT   MUTAGEN     318    318       C->S: Abolishes sensitivity to sulfhydryl
FT                                modification.
FT   MUTAGEN     349    349       G->A: Abolishes conductivity; when
FT                                associated with A-350 and A-351.
FT   MUTAGEN     350    350       Y->A: Abolishes conductivity; when
FT                                associated with A-349 and A-351.
FT   MUTAGEN     351    351       G->A: Abolishes conductivity; when
FT                                associated with A-349 and A-350.
FT   CONFLICT     42     42       G -> R (in Ref. 1; AAC53518).
FT   CONFLICT    394    394       R -> S (in Ref. 3; AK014722).
SQ   SEQUENCE   910 AA;  102432 MW;  56FD5F328DD972E9 CRC64;
     MEGGGKPNSA SNSRDDGNSV FPSKAPATGP VAADKRLGTP PGGGAAGKEH GNSVCFKVDG
     GGGEEPAGSF EDAEGPRRQY GFMQRQFTSM LQPGVNKFSL RMFGSQKAVE KEQERVKTAG
     FWIIHPYSDF RFYWDLIMLI MMVGNLVIIP VGITFFTEQT TTPWIIFNVA SDTVFLLDLI
     MNFRTGTVNE DSSEIILDPK VIKMNYLKSW FVVDFISSIP VDYIFLIVEK GMDSEVYKTA
     RALRIVRFTK ILSLLRLLRL SRLIRYIHQW EEIFHMTYDL ASAVVRIFNL IGMMLLLCHW
     DGCLQFLVPL LQDFPPDCWV SLNEMVNDSW GKQYSYALFK AMSHMLCIGY GAQAPVSMSD
     LWITMLSMIV GATCYAMFVG HATALIQSLD SSRRQYQEKY KQVEQYMSFH KLPADMRQKI
     HDYYEHRYQG KIFDEENILS ELNDPLREEI VNFNCRKLVA TMPLFANADP NFVTAMLSKL
     RFEVFQPGDY IIREGAVGKK MYFIQHGVAG VITKSSKEMK LTDGSYFGEI CLLTKGRRTA
     SVRADTYCRL YSLSVDNFNE VLEEYPMMRR AFETVAIDRL DRIGKKNSIL LQKFQKDLNT
     GVFNNQENEI LKQIVKHDRE MVQAIPPINY PQMTALNCTS STTTPTSRMR TQSPPVYTAT
     SLSHSNLHSP SPSTQTPQPS AILSPCSYTT AVCSPPIQSP LATRTFHYAS PTASQLSLMQ
     QPQQQLPQSQ VQQTQTQTQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQPQTPG
     SSTPKNEVHK STQALHNTNL TKEVRPLSAS QPSLPHEVST LISRPHPTVG ESLASIPQPV
     AAVHSTGLQA GSRSTVPQRV TLFRQMSSGA IPPNRGVPPA PPPPAAVQRE SPSVLNTDPD
     AEKPRFASNL
//
ID   HCN3_MOUSE              Reviewed;         779 AA.
AC   O88705;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3;
DE   AltName: Full=Hyperpolarization-activated cation channel 3;
DE            Short=HAC-3;
GN   Name=Hcn3; Synonyms=Hac3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=98295993; PubMed=9634236; DOI=10.1038/31255;
RA   Ludwig A., Zong X., Jeglitsch M., Hofmann F., Biel M.;
RT   "A family of hyperpolarization-activated cation channels.";
RL   Nature 393:587-591(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=98292171; PubMed=9630217; DOI=10.1016/S0092-8674(00)81434-8;
RA   Santoro B., Liu D.T., Yao H., Bartsch D., Kandel E.R.,
RA   Siegelbaum S.A., Tibbs G.R.;
RT   "Identification of a gene encoding a hyperpolarization-activated
RT   'pacemaker' channel of brain.";
RL   Cell 93:717-729(1998).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-633, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Putative hyperpolarization-activated ion channel
CC       exhibiting weak selectivity for potassium over sodium ions.
CC   -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC       heterotetrameric complex of pore-forming subunits.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and heart, in
CC       particular in ventricle, atrium and in sinoatrial node (SAN).
CC       Detected at low levels in skeletal muscle and lung.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position.
CC   -!- SIMILARITY: Belongs to the potassium channel HCN family.
CC   -!- SIMILARITY: Contains 1 cyclic nucleotide-binding domain.
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DR   EMBL; AJ225124; CAA12408.1; -; mRNA.
DR   EMBL; AK032225; BAC27769.1; -; mRNA.
DR   EMBL; BC039156; AAH39156.1; -; mRNA.
DR   IPI; IPI00133981; -.
DR   RefSeq; NP_032253.1; NM_008227.1.
DR   UniGene; Mm.389461; -.
DR   ProteinModelPortal; O88705; -.
DR   SMR; O88705; 353-549.
DR   STRING; O88705; -.
DR   PhosphoSite; O88705; -.
DR   PRIDE; O88705; -.
DR   Ensembl; ENSMUST00000029686; ENSMUSP00000029686; ENSMUSG00000028051.
DR   GeneID; 15168; -.
DR   KEGG; mmu:15168; -.
DR   UCSC; uc008pxr.1; mouse.
DR   CTD; 15168; -.
DR   MGI; MGI:1298211; Hcn3.
DR   eggNOG; roNOG08921; -.
DR   GeneTree; ENSGT00600000084322; -.
DR   HOGENOM; HBG447083; -.
DR   HOVERGEN; HBG039489; -.
DR   InParanoid; O88705; -.
DR   OMA; ARGPWAS; -.
DR   OrthoDB; EOG46Q6S8; -.
DR   PhylomeDB; O88705; -.
DR   NextBio; 287674; -.
DR   ArrayExpress; O88705; -.
DR   Bgee; O88705; -.
DR   Genevestigator; O88705; -.
DR   GermOnline; ENSMUSG00000028051; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0005272; F:sodium channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR013621; Ion_trans_N.
DR   InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF08412; Ion_trans_N; 1.
DR   PRINTS; PR01463; EAGCHANLFMLY.
DR   SMART; SM00100; cNMP; 1.
DR   SUPFAM; SSF51206; cNMP_binding; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; FALSE_NEG.
DR   PROSITE; PS00889; CNMP_BINDING_2; FALSE_NEG.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
PE   1: Evidence at protein level;
KW   cAMP; cAMP-binding; Glycoprotein; Ion transport; Ionic channel;
KW   Ligand-gated ion channel; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Potassium; Potassium channel; Potassium transport;
KW   Sodium; Sodium channel; Sodium transport; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    779       Potassium/sodium hyperpolarization-
FT                                activated cyclic nucleotide-gated channel
FT                                3.
FT                                /FTId=PRO_0000054115.
FT   TOPO_DOM      1     96       Cytoplasmic (Potential).
FT   TRANSMEM     97    117       Helical; Name=Segment S1; (Potential).
FT   TOPO_DOM    118    123       Extracellular (Potential).
FT   TRANSMEM    124    144       Helical; Name=Segment S2; (Potential).
FT   TOPO_DOM    145    170       Cytoplasmic (Potential).
FT   TRANSMEM    171    191       Helical; Name=Segment S3; (Potential).
FT   TOPO_DOM    192    200       Extracellular (Potential).
FT   TRANSMEM    201    221       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TOPO_DOM    222    252       Cytoplasmic (Potential).
FT   TRANSMEM    253    273       Helical; Name=Segment S5; (Potential).
FT   TOPO_DOM    274    296       Extracellular (Potential).
FT   INTRAMEM    297    318       Pore-forming; Name=Segment H5;
FT                                (Potential).
FT   TOPO_DOM    319    328       Extracellular (Potential).
FT   TRANSMEM    329    349       Helical; Name=Segment S6; (Potential).
FT   TOPO_DOM    350    779       Cytoplasmic (Potential).
FT   NP_BIND     427    544       cAMP.
FT   REGION       45     90       Involved in subunit assembly (By
FT                                similarity).
FT   MOD_RES     633    633       Phosphoserine.
FT   CARBOHYD    290    290       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   779 AA;  86641 MW;  D4FF151F174DECAE CRC64;
     MEEEARPAAG AGEAATPARE TPPAAPAQAR AASGGVPESA PEPKRRQLGT LLQPTVNKFS
     LRVFGSHKAV EIEQERVKSA GAWIIHPYSD FRFYWDLIML LLMVGNLIVL PVGITFFKEE
     NSPPWIVFNV LSDTFFLLDL VLNFRTGIVV EEGAEILLAP RAIRTRYLRT WFLVDLISSI
     PVDYIFLVVE LEPRLDAEVY KTARALRIVR FTKILSLLRL LRLSRLIRYI HQWEEIFHMT
     YDLASAVVRI FNLIGMMLLL CHWDGCLQFL VPMLQDFPSD CWVSMNRMVN HSWGRQYSHA
     LFKAMSHMLC IGYGQQAPVG MPDVWLTMLS MIVGATCYAM FIGHATALIQ SLDSSRRQYQ
     EKYKQVEQYM SFHKLPADTR QRIHEYYEHR YQGKMFDEES ILGELSEPLR EEIINFTCRG
     LVAHMPLFAH ADPSFVTAVL TKLRFEVFQP GDLVVREGSV GRKMYFIQHG LLSVLARGAR
     DTRLTDGSYF GEICLLTRGR RTASVRADTY CRLYSLSVDH FNAVLEEFPM MRRAFETVAM
     DRLRRIGKKN SILQRKRSEP SPGSSGGVME QHLVQHDRDM ARGVRGLAPG TGARLSGKPV
     LWEPLVHAPL QAAAVTSNVA IALTHQRGPL PLSPDSPATL LARSARRSAG SPASPLVPVR
     AGPLLARGPW ASTSRLPAPP ARTLHASLSR TGRSQVSLLG PPPGGGARRL GPRGRPLSAS
     QPSLPQRATG DGSPRRKGSG SERLPPSGLL AKPPGTVQPP RSSVPEPVTP RGPQISANM
//
ID   MAP7_MOUSE              Reviewed;         730 AA.
AC   O88735; Q3V0B9; Q7TQL9; Q80V60;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Ensconsin;
DE   AltName: Full=Epithelial microtubule-associated protein of 115 kDa;
DE            Short=E-MAP-115;
DE   AltName: Full=Microtubule-associated protein 7;
DE            Short=MAP-7;
GN   Name=Map7; Synonyms=Mtap7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6 X CBA;
RX   MEDLINE=98418230; PubMed=9745708;
RX   DOI=10.1111/j.1432-0436.1998.00169.x;
RA   Fabre-Jonca N., Allaman J.-M., Radlgruber G., Meda P., Kiss J.Z.,
RA   French L.E., Masson D.;
RT   "The distribution of murine 115-kDa epithelial microtubule-associated
RT   protein (E-MAP-115) during embryogenesis and in adult organs suggests
RT   a role in epithelial polarization and differentiation.";
RL   Differentiation 63:169-180(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH TRPV4.
RC   TISSUE=Kidney;
RX   PubMed=14517216; DOI=10.1074/jbc.M308212200;
RA   Suzuki M., Hirao A., Mizuno A.;
RT   "Microtubule-associated protein 7 increases the membrane expression of
RT   transient receptor potential vanilloid 4 (TRPV4).";
RL   J. Biol. Chem. 278:51448-51453(2003).
RN   [3]
RP   ERRATUM.
RA   Suzuki M., Hirao A., Mizuno A.;
RL   J. Biol. Chem. 280:25948-25948(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-494 (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Eye, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=12755995; DOI=10.1046/j.1365-2605.2003.00406.x;
RA   Penttilae T.-L., Parvinen M., Paranko J.;
RT   "Microtubule-associated epithelial protein E-MAP-115 is localized in
RT   the spermatid manchette.";
RL   Int. J. Androl. 26:166-174(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Microtubule-stabilizing protein that may play an
CC       important role during reorganization of microtubules during
CC       polarization and differentiation of epithelial cells. Associates
CC       with microtubules in a dynamic manner. May play a role in the
CC       formation of intercellular contacts. Colocalization with TRPV4
CC       results in the redistribution of TRPV4 toward the membrane and may
CC       link cytoskeletal microfilaments.
CC   -!- SUBUNIT: Interacts with TRPV4.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Basolateral
CC       cell membrane. Cytoplasm, cytoskeleton. Note=Colocalized on
CC       microtubules. An intracellular redistribution is triggered during
CC       induction of keratinocyte terminal differentiation from
CC       microtubules with a perinuclear localization to cortical
CC       microtubules organized in spike-like bundles facing intercellular
CC       contacts.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O88735-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O88735-2; Sequence=VSP_021318;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in epithelial cells of kidney
CC       tubules, in absorptive cells of the intestine and is widely
CC       distributed in the testis. Expression correlates with the
CC       differentiation of certain epithelial cell types: in the adult
CC       intestine, abundantly expressed in the differentiating than in the
CC       proliferative cell compartment. Moreover the expression clearly
CC       correlates with the degree of cellular apicobasal polarity.
CC       Expressed in lung, kidney, brain and fat. Colocalized withTRPV4 in
CC       ependymal cells, in the choroid plexus, inbronchial and renal
CC       cortical tubular cells. Widely expressed in excitable neuronal or
CC       vascular cells as well as in epithelial cells. In seminiferous
CC       epithelium associated with the microtubule of the spermatid
CC       manchette.
CC   -!- DEVELOPMENTAL STAGE: Expressed in several epithelia from E9.5
CC       onwards and that its expression levels increase during
CC       development. From E14.5 days onwards, is found in some neuronal
CC       cells as well.
CC   -!- PTM: The association with microtubules is regulated by
CC       phosphorylation during the cell cycle. During interphase only
CC       phosphorylated on serine. Phosphorylated on threonine in mitosis
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the MAP7 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH42771.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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DR   EMBL; Y15197; CAA75495.1; -; mRNA.
DR   EMBL; AB098611; BAC53729.1; -; mRNA.
DR   EMBL; AK133267; BAE21585.1; -; mRNA.
DR   EMBL; BC042771; AAH42771.1; ALT_SEQ; mRNA.
DR   EMBL; BC052637; AAH52637.1; -; mRNA.
DR   IPI; IPI00380510; -.
DR   IPI; IPI00798490; -.
DR   RefSeq; NP_001185564.1; NM_001198635.1.
DR   RefSeq; NP_032661.2; NM_008635.2.
DR   UniGene; Mm.20928; -.
DR   ProteinModelPortal; O88735; -.
DR   STRING; O88735; -.
DR   PhosphoSite; O88735; -.
DR   PRIDE; O88735; -.
DR   Ensembl; ENSMUST00000020173; ENSMUSP00000020173; ENSMUSG00000019996.
DR   GeneID; 17761; -.
DR   KEGG; mmu:17761; -.
DR   UCSC; uc007eno.1; mouse.
DR   CTD; 17761; -.
DR   MGI; MGI:1328328; Mtap7.
DR   eggNOG; roNOG09070; -.
DR   GeneTree; ENSGT00530000063115; -.
DR   HOVERGEN; HBG081952; -.
DR   OrthoDB; EOG41NTN2; -.
DR   NextBio; 292449; -.
DR   ArrayExpress; O88735; -.
DR   Bgee; O88735; -.
DR   CleanEx; MM_MTAP7; -.
DR   Genevestigator; O88735; -.
DR   GermOnline; ENSMUSG00000019996; Mus musculus.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR   GO; GO:0008283; P:cell proliferation; IMP:MGI.
DR   GO; GO:0009566; P:fertilization; IMP:MGI.
DR   GO; GO:0007281; P:germ cell development; IMP:MGI.
DR   GO; GO:0006687; P:glycosphingolipid metabolic process; IMP:MGI.
DR   GO; GO:0048872; P:homeostasis of number of cells; IMP:MGI.
DR   GO; GO:0033327; P:Leydig cell differentiation; IMP:MGI.
DR   GO; GO:0001578; P:microtubule bundle formation; IMP:MGI.
DR   GO; GO:0006997; P:nucleus organization; IMP:MGI.
DR   GO; GO:0035265; P:organ growth; IMP:MGI.
DR   GO; GO:0006970; P:response to osmotic stress; IPI:MGI.
DR   GO; GO:0032526; P:response to retinoic acid; IMP:MGI.
DR   GO; GO:0060009; P:Sertoli cell development; IMP:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   InterPro; IPR008604; E-MAP-115.
DR   PANTHER; PTHR15073; E-MAP-115; 1.
DR   Pfam; PF05672; MAP7; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell membrane; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Membrane; Microtubule; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    730       Ensconsin.
FT                                /FTId=PRO_0000255950.
FT   COILED       89    152       Potential.
FT   COILED      460    589       Potential.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     169    169       Phosphoserine (By similarity).
FT   MOD_RES     181    181       Phosphoserine (By similarity).
FT   MOD_RES     200    200       Phosphoserine (By similarity).
FT   MOD_RES     201    201       Phosphoserine (By similarity).
FT   MOD_RES     202    202       Phosphoserine (By similarity).
FT   MOD_RES     203    203       Phosphoserine.
FT   MOD_RES     209    209       Phosphoserine (By similarity).
FT   MOD_RES     219    219       Phosphoserine (By similarity).
FT   MOD_RES     231    231       Phosphothreonine (By similarity).
FT   MOD_RES     243    243       Phosphothreonine (By similarity).
FT   MOD_RES     254    254       Phosphoserine (By similarity).
FT   MOD_RES     277    277       Phosphothreonine (By similarity).
FT   MOD_RES     316    316       Phosphoserine (By similarity).
FT   MOD_RES     366    366       Phosphoserine (By similarity).
FT   MOD_RES     654    654       Phosphoserine (By similarity).
FT   VAR_SEQ     250    250       T -> TVIPICPRS (in isoform 2).
FT                                /FTId=VSP_021318.
FT   CONFLICT      4      4       Q -> H (in Ref. 4; BAE21585).
FT   CONFLICT      8      8       G -> C (in Ref. 4; BAE21585).
FT   CONFLICT     16     16       G -> S (in Ref. 4; BAE21585).
FT   CONFLICT     35     35       A -> G (in Ref. 4; BAE21585).
FT   CONFLICT    360    360       A -> T (in Ref. 5; AAH42771).
FT   CONFLICT    373    373       F -> V (in Ref. 4; BAE21585 and 5;
FT                                AAH52637/AAH42771).
SQ   SEQUENCE   730 AA;  82022 MW;  F44B4201DE8F5A17 CRC64;
     MAEQGAGGDG HRGGDGATHS DPASDGYKVQ EKRTAPSRPT STVSGQTSNH SGNKPDPPPV
     LRVDDRQRLA RERREEREKQ LAARETVWLE REERARQHYE RHLEARKKKL EDQRLKEERR
     RAAVEEKRRQ RLEEDKERHE AVVRRTMERS QKPRQKSNRW SWGSPLHGSS SIHSGDPDRR
     SVSTMNLSKH VDPVISKRLS SSSATLLNSP DRARRLQLSP WESSVVSRLL TPTHSFLARS
     KSTAALSGDT ASCSPIIMPF KAAHSRNPVD RPKLFVTPPE GSARRRTIHG LASHKRERER
     EHVPFHVSPG ARRTLSPSNL KARSPAPARL WLPSKSMPHL PGTPRPASSL PPGSVRAASA
     QAPSSSPGNI RPFKREVKVE PEKKDPLPAV KSRVPLVKVE EVTVEEGTPV KPPEPAAPAS
     APIATPAPAP ATDPAPVPAP SSTVTVGVVP KTSAGTTDPE EATRLLAEKR RLAREQREKE
     ERERKEKEEL ERQKIEELAR RVAEERSRRE EEARRLEEEQ AREKEELALR LAEEERERWE
     REEVERVQKQ KEEEARAREE AERARQEREK HFQKEEQERL ERKKRLEEIM RRTRRTETAD
     KKTTEQRNGD IAKGVLTGEP EVPALPCMAS SGNGESAESP HGVALQQSEV TTESSPDLEK
     QPNENGMSIQ NENFEEVINL PVGSKASRLD VTNENPEIPL KPILAFNDEG TLGPLPQVDG
     VQTQQTAEVI
//
ID   BSN_MOUSE               Reviewed;        3942 AA.
AC   O88737; Q6ZQB5;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Protein bassoon;
GN   Name=Bsn; Synonyms=Kiaa0434;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC   STRAIN=129/SvJ;
RX   MEDLINE=98345363; PubMed=9679147; DOI=10.1083/jcb.142.2.499;
RA   tom Dieck S., Sanmarti-Vila L., Langnaese K., Richter K., Kindler S.,
RA   Soyke A., Wex H., Smalla K.-H., Kaempf U., Fraenzer J.-T., Stumm M.,
RA   Garner C.C., Gundelfinger E.D.;
RT   "Bassoon, a novel zinc-finger CAG/Glutamine-repeat protein selectively
RT   localized at the active zone of presynaptic nerve terminals.";
RL   J. Cell Biol. 142:499-509(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2714-3942 (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   MEDLINE=22516610; PubMed=12628168; DOI=10.1016/S0896-6273(03)00086-2;
RA   Dick O., tom Dieck S., Altrock W.D., Ammermueller J., Weiler R.,
RA   Garner C.C., Gundelfinger E.D., Brandstaetter J.H.;
RT   "The presynaptic active zone protein bassoon is essential for
RT   photoreceptor ribbon synapse formation in the retina.";
RL   Neuron 37:775-786(2003).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   MEDLINE=22516611; PubMed=12628169; DOI=10.1016/S0896-6273(03)00088-6;
RA   Altrock W.D., tom Dieck S., Sokolov M., Meyer A.C., Sigler A.,
RA   Brakebusch C., Faessler R., Richter K., Boeckers T.M., Potschka H.,
RA   Brandt C., Loescher W., Grimberg D., Dresbach T., Hempelmann A.,
RA   Hassan H., Balschun D., Frey J.U., Brandstaetter J.H., Garner C.C.,
RA   Rosenmund C., Gundelfinger E.D.;
RT   "Functional inactivation of a fraction of excitatory synapses in mice
RT   deficient for the active zone protein bassoon.";
RL   Neuron 37:787-800(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; THR-1102; SER-1105;
RP   SER-1108; SER-1114; SER-1481; SER-1482; SER-1486; SER-1493; THR-1495;
RP   SER-1497; SER-1510; SER-1553; SER-1554; SER-2029; SER-2122; SER-2124;
RP   SER-2808; SER-2811; SER-2822; SER-2858; SER-2860; SER-2866 AND
RP   SER-2908, AND MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1019; SER-1108;
RP   SER-1114; SER-1236; SER-2578; THR-2595; THR-2622; SER-2860; SER-2866;
RP   SER-3301 AND SER-3382, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-1395; SER-1707; THR-1934;
RP   THR-2318; THR-2524; THR-2700 AND THR-2945, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452088; DOI=10.1074/mcp.T500040-MCP200;
RA   Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G.,
RA   Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F.,
RA   Maltby D.A., Schoepfer R., Burlingame A.L.;
RT   "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT   preparations using lectin weak affinity chromatography and mass
RT   spectrometry.";
RL   Mol. Cell. Proteomics 5:923-934(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2073, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2694; THR-2703; TYR-3431
RP   AND TYR-3432, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105; SER-142; SER-980;
RP   THR-1116; TYR-1136; THR-1406; SER-1482; TYR-2044; THR-2595; SER-2811;
RP   SER-2858; SER-2860; SER-2866; SER-2908; SER-3022; SER-3301; SER-3382
RP   AND TYR-3459, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Is thought to be involved in the organization of the
CC       cytomatrix at the nerve terminals active zone (CAZ) which
CC       regulates neurotransmitter release. Seems to act through binding
CC       to ERC2/CAST1. Essential in regulated neurotransmitter release
CC       from a subset of brain glutamatergic synapses (By similarity).
CC       Involved in the formation of the retinal photoreceptor ribbon
CC       synapses.
CC   -!- SUBUNIT: Interacts with ERC2/CAST1, RIMS1 and UNC13A. Part of a
CC       complex consisting of ERC2, RIMS1 and BSN (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell junction, synapse,
CC       synaptosome. Cytoplasm, cytoskeleton. Note=Localized to the active
CC       zone of presynaptic density.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O88737-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O88737-2; Sequence=VSP_011375;
CC         Note=Incompl;
CC   -!- TISSUE SPECIFICITY: Expressed in brain and retina.
CC   -!- PTM: Myristoylated. The N-terminal myristoylation is not
CC       sufficient for presynaptic localization (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice show a reduced excitability attributed
CC       to inactivation of a fraction of brain glutamatergic synapses. At
CC       these synapses, vesicles are clustered and docked in normal
CC       numbers, but were unable to fuse. In retina, mutants lacking
CC       functional BSN showed normal retinal anatomy, but synapses lacked
CC       anchoring of the photoreceptor ribbon to the presynaptic active
CC       zone resulting in impaired photoreceptor synaptic transmission.
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DR   EMBL; Y17034; CAA76598.1; -; Genomic_DNA.
DR   EMBL; Y17035; CAA76598.1; JOINED; Genomic_DNA.
DR   EMBL; Y17036; CAA76598.1; JOINED; Genomic_DNA.
DR   EMBL; Y17037; CAA76598.1; JOINED; Genomic_DNA.
DR   EMBL; Y17038; CAA76598.1; JOINED; Genomic_DNA.
DR   EMBL; AK129141; BAC97951.1; -; mRNA.
DR   IPI; IPI00134093; -.
DR   IPI; IPI00461199; -.
DR   PIR; T42730; T42730.
DR   RefSeq; NP_031593.2; NM_007567.2.
DR   UniGene; Mm.20425; -.
DR   ProteinModelPortal; O88737; -.
DR   MINT; MINT-136785; -.
DR   STRING; O88737; -.
DR   PhosphoSite; O88737; -.
DR   PRIDE; O88737; -.
DR   Ensembl; ENSMUST00000035208; ENSMUSP00000035208; ENSMUSG00000032589.
DR   GeneID; 12217; -.
DR   KEGG; mmu:12217; -.
DR   UCSC; uc009rov.1; mouse.
DR   CTD; 12217; -.
DR   MGI; MGI:1277955; Bsn.
DR   eggNOG; roNOG04262; -.
DR   HOGENOM; HBG447034; -.
DR   HOVERGEN; HBG080934; -.
DR   InParanoid; O88737; -.
DR   OrthoDB; EOG4G4GPH; -.
DR   ArrayExpress; O88737; -.
DR   Bgee; O88737; -.
DR   CleanEx; MM_BSN; -.
DR   Genevestigator; O88737; -.
DR   GermOnline; ENSMUSG00000032589; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0044306; C:neuron projection terminus; IDA:MGI.
DR   GO; GO:0048786; C:presynaptic active zone; IDA:MGI.
DR   GO; GO:0019717; C:synaptosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR008899; Znf_piccolo.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 2.
DR   Pfam; PF05715; zf-piccolo; 2.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Glycoprotein; Lipoprotein; Metal-binding; Myristate;
KW   Phosphoprotein; Repeat; Synapse; Synaptosome; Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   3942       Protein bassoon.
FT                                /FTId=PRO_0000065003.
FT   REPEAT      570    576       1.
FT   REPEAT      577    583       2.
FT   REPEAT      584    590       3.
FT   REPEAT      591    597       4.
FT   REPEAT      598    604       5.
FT   ZN_FING     167    190       C4-type (Potential).
FT   ZN_FING     195    217       C4-type (Potential).
FT   ZN_FING     464    487       C4-type (Potential).
FT   ZN_FING     492    514       C4-type (Potential).
FT   REGION       62     71       5 X 2 AA tandem repeats of P-G.
FT   REGION      570    604       5 X 7 AA tandem repeats of K-A-S-P-Q-
FT                                [AT]-[AT].
FT   COMPBIAS   2608   2614       Poly-Arg.
FT   COMPBIAS   2635   2640       Poly-Arg.
FT   COMPBIAS   3784   3798       Poly-Gln.
FT   MOD_RES       6      6       Phosphoserine.
FT   MOD_RES     105    105       Phosphoserine.
FT   MOD_RES     135    135       Phosphoserine (By similarity).
FT   MOD_RES     140    140       Phosphoserine (By similarity).
FT   MOD_RES     142    142       Phosphoserine.
FT   MOD_RES     980    980       Phosphoserine.
FT   MOD_RES    1019   1019       Phosphoserine.
FT   MOD_RES    1102   1102       Phosphothreonine.
FT   MOD_RES    1105   1105       Phosphoserine.
FT   MOD_RES    1108   1108       Phosphoserine.
FT   MOD_RES    1114   1114       Phosphoserine.
FT   MOD_RES    1116   1116       Phosphothreonine.
FT   MOD_RES    1136   1136       Phosphotyrosine.
FT   MOD_RES    1236   1236       Phosphoserine.
FT   MOD_RES    1406   1406       Phosphothreonine.
FT   MOD_RES    1481   1481       Phosphoserine.
FT   MOD_RES    1482   1482       Phosphoserine.
FT   MOD_RES    1486   1486       Phosphoserine.
FT   MOD_RES    1493   1493       Phosphoserine.
FT   MOD_RES    1495   1495       Phosphothreonine.
FT   MOD_RES    1497   1497       Phosphoserine.
FT   MOD_RES    1510   1510       Phosphoserine.
FT   MOD_RES    1553   1553       Phosphoserine.
FT   MOD_RES    1554   1554       Phosphoserine.
FT   MOD_RES    2029   2029       Phosphoserine.
FT   MOD_RES    2044   2044       Phosphotyrosine.
FT   MOD_RES    2073   2073       Phosphotyrosine.
FT   MOD_RES    2122   2122       Phosphoserine.
FT   MOD_RES    2124   2124       Phosphoserine.
FT   MOD_RES    2578   2578       Phosphoserine.
FT   MOD_RES    2595   2595       Phosphothreonine.
FT   MOD_RES    2622   2622       Phosphothreonine.
FT   MOD_RES    2694   2694       Phosphoserine.
FT   MOD_RES    2703   2703       Phosphothreonine.
FT   MOD_RES    2808   2808       Phosphoserine.
FT   MOD_RES    2811   2811       Phosphoserine.
FT   MOD_RES    2822   2822       Phosphoserine.
FT   MOD_RES    2858   2858       Phosphoserine.
FT   MOD_RES    2860   2860       Phosphoserine.
FT   MOD_RES    2866   2866       Phosphoserine.
FT   MOD_RES    2908   2908       Phosphoserine.
FT   MOD_RES    3022   3022       Phosphoserine.
FT   MOD_RES    3301   3301       Phosphoserine.
FT   MOD_RES    3382   3382       Phosphoserine.
FT   MOD_RES    3431   3431       Phosphotyrosine.
FT   MOD_RES    3432   3432       Phosphotyrosine.
FT   MOD_RES    3459   3459       Phosphotyrosine.
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
FT   CARBOHYD   1354   1354       O-linked (GlcNAc) (By similarity).
FT   CARBOHYD   1395   1395       O-linked (GlcNAc).
FT   CARBOHYD   1707   1707       O-linked (GlcNAc).
FT   CARBOHYD   1934   1934       O-linked (GlcNAc).
FT   CARBOHYD   2318   2318       O-linked (GlcNAc).
FT   CARBOHYD   2524   2524       O-linked (GlcNAc).
FT   CARBOHYD   2700   2700       O-linked (GlcNAc).
FT   CARBOHYD   2945   2945       O-linked (GlcNAc).
FT   VAR_SEQ    2833   2889       Missing (in isoform 2).
FT                                /FTId=VSP_011375.
FT   CONFLICT   2892   2892       V -> A (in Ref. 2).
FT   CONFLICT   3902   3902       G -> S (in Ref. 2; BAC97951).
SQ   SEQUENCE   3942 AA;  418746 MW;  150267E636C4DACB CRC64;
     MGNEASLEGG AGEGPLPPGG SGLGPGPGAG KPPSALAGGG QLPVAGAARA AGPPTPGLGP
     VPGPGPGPGP GSVPRRLDPK EPLGSQRTTS PTPKQASATA PGRESPRETR AQGPSGQEAE
     SPRRTLQVDS RTQRSGRSPS VSPDRGSTPT SPYSVPQIAP LPSSTLCPIC KTSDLTSTPS
     QPNFNTCTQC HNKVCNQCGF NPNPHLTQVK EWLCLNCQMQ RALGMDMTTA PRSKSQQQLH
     SPALSPAHSP AKQPLGKPEQ ERSPRGPGAT QSGPRQAEAA RATSVPGPTQ ATAPPEVGRV
     SPQPPLSTKP STAEPRPPAG EAQGKSATTV PSGLGAGEQT QEGLTGKLFG LGASLLTQAS
     TLMSVQPEAD TQGQPSPSKG PPKIVFSDAS KEAGPRPPGS GPGPGPTPGA KTEPGARTGP
     GSGPGALAKT GGTASPKHGR AEHQAASKAA AKPKTMPKER AAACPLCQAE LNVGSRGPAN
     YNTCTACKLQ VCNLCGFNPT PHLVEKTEWL CLNCQTKRLL EGSLGEPAPL PLPTPQQPPA
     GVPHRAAGAA PLKQKGPQGL GQPSGSLPAK ASPQATKASP QATKASPQAT KASPQTTKAS
     PQAKPLRATE PSKTSSSAQE KKTATPAKAE PVPKPPPETT VPPGTPKAKS GVKRTDPATP
     VVKPVPEAPK GGEAEEPVPK PYSQDLSRSP QSLSDTGYSS DGVSSSQSEI TGVVQQEVEQ
     LDSAGVTGPR PPSPSELHKV GSSLRPSLEA QAVAPSAEWS KPPRSSSSAV EDQKRRPHSL
     SIMPEAFDSD EELGDILEED DSLAWGRQRE QQDTAESSDD FGSQLRHDYV EDSSEGGLSP
     LPPQPPARAD MTDEEFMRRQ ILEMSAEEDN LEEDDTAVSG RGLAKHSAQK ASARPRPESS
     QEPKRRLPHN ATTGYEELLS EAGPAEPTDS SGALQGGLRR FKTIELNSTG SYGHELDLGQ
     GPDPNLDREP ELEMESLTGS PEDRSRGEHS STLPASTPSY TSGTSPTSLS SLEEDSDSSP
     SRRQRLEEAK QQRKARHRSH GPLLPTIEDS SEEEELREEE ELLREQEKMR EVEQQRIRST
     ARKTRRDKEE LRAQRRRERS KTPPSNLSPI EDASPTEELR QAAEMEELHR SSCSEYSPSP
     SLDSEAETLD GGPTRLYKSG SEYNLPAFMS LYSPTETPSG SSTTPSSGRP LKSAEEAYED
     MMRKAEMLQR QQGQVAGARG PHGGPSQPTG PRSQGSFEYQ DTQDHDYGGR ASQPVAESTP
     AGLGAAVYEE ILQTSQSIAR MRQASSRDLG FTEDKKKEKQ FLNAESAYMD PMKQNGGPLT
     PGTSPTQLAA PVSFSTSTSS DSSGGRVIPD VRVTQHFAKE PQDPLKLHSS PVSSTLTSKE
     VGMTFSQGPG SPATTASPTR GYMTPTSPAG SERSPSTSST IHSYGQPPTT ANYGSQTEEL
     PHAPSGPPGS GRAPREKPLS GGDSEVGAPQ PSRGYSYFTG SSPPLSPSTP SESPTFSPGK
     LGPRATAEFS TQTPSLTLSS DIPRSPGPPS PMVAQGTQTP HRPSTPRLVW QQSSQEAPIM
     VITLASDASS QTRMVHASAS TSPLCSPTDS QPTSHSYSQT TPPSASQMPS EPAGPPGFPR
     APSAGTDGPL ALYGWGALPA ENISLCRISS VPGTSRVEPG PRPPGTAVVD LRTAVKPTPI
     ILTDQGMDLT SLAVEARKYG LALDPVSGRQ STAVQPLVIN LNAQEQTHTF LATATTVSIT
     MASSVLMAQQ KQPVVYGDPF QSRLDFGQGS GSPVCLAQVK QVEQAVQTAP YRGGPRGRPR
     EAKFARYNLP NQVTPLARRD ILITQMGTAQ GVGLKPGPVP EPGAEPHRAT PAELRSHAPP
     GTRKPHTVVV QMGEGTAGTV TTLLPEEPAG ALDLTGMRPE SQLACCDMVY KFPFGSSCTG
     TFHPAPSAPD KSVTDTALPG QSSGPFYSPR DPEPPEPLTF RTQGVVGPGP HEEQRPYPQG
     LPGRLYSSMS DTNLAEAGLN YHAQRLGQLF QGPGRDSAVD LSSLKHSYSL GFADGRYLGQ
     GLQYGSFTDL RHPTDLLSHP LPLRRYSSVS NIYSDHRYGP RGDAVGFQEA SLAQYSATTA
     REISRMCAAL NSMDQYGGRH GSGSGGPDLV QYQPQHGPGL SAPQGLAPLR SGLLGNPTYP
     EGQPSPGNLA QYGPAASQAT AVRQLLPSTA TVRAADGMIY STINTPIAAT LPITTQPASV
     LRPMVRGGMY RPYVSGGVTA VPLTSLTRVP MIAPRVPLGP AGLYRYPAPR FPIASSVPPA
     EGPVYLGKPA ATKASGAGGP PRPELPAGVA REEPFSTTAP AVIKEAPVAP APGPAPAPPP
     GQKPAGEAAA GSGSGVLSRP ASEKEEASQE DRQRKQQEQL LQLERERVEL EKLRQLRLQE
     ELERERVELQ RHREEEQLLV QRELQELQTI KQHVLQQQQE ERQAQFALQR EQLAQQRLQL
     EQIQQLQQQL QLQLEEQKQR QKAPFPATCE APSRGPPPAA TELAQNGQYW PPLTHAAFIA
     VAGTEGPGQP REPVLHRGLP SSASDMSLQT EEQWEAGRSG IKKRHSMPRL RDACEPESGP
     DPSTVRRIAD SSVQTDDEEG EGRYLVTRRR RTRRSADCSV QTDDEDNADW EQPVRRRRSR
     LSRHSDSGSD SKHDATASSS TTAAATARAM SSVGIQTISD CSVQTEPEQL PRVSPAIHIT
     AATDPKVEIV RYISAPEKTG RGESLACQTE PDGQAQGVAG PQLIGPTAIS PYLPGIQIVT
     PGALGRFEKK KPDPLEIGYQ AHLPPESLSQ LVSRQPPKSP QVLYSPVSPL SPHRLLDTSF
     ASSERLNKAH VSPQKQFIAD STLRQQTLPR PMKTLQRSLS DPKPLSPTAE ESAKERFSLY
     QHQGGLGSQV SVLPPNGLVR KVKRTLPSPP PEEAHLPLAG QVPSQLYAAS LLQRGLAGPT
     TVPATKASLL RELDRDLRLV EHESTKLRKK QAELDEEEKE IDAKLKYLEL GITQRKESLA
     KDRGGRDYPP LRGLGEHRDY LSDSELNQLR LQGCTTPAGQ YVDYPASAAV PATPSGPTAF
     QQPRFPPAAP QYTAGSSGPT QNGFPAHQAP TYTGPSTYPA PTYPPGTGYP AEPGLPSQPA
     FHPTGHYAAP TPMPTTQSAP FPVQADSRAA HQKPRQTSLA DLEQKVPTNY EVIGSPAVTM
     SSAPPETGYS GPAVSGSYEQ GKAPEHPRGS DRSSVSQSPA PTYPSDSHYT SLEQNVPRNY
     VMIDDISELT KDSTPTASES QRLEPLGPGG VSGRPGKDPG EPAVLEGPTL PCCYGRGEEE
     SEEDSYDPRG KSGHHRSMES NGRPSTHYYG DSDYRHGARA DKYGPGPMGP KHPSKSLAPA
     AISSKRSKHR KQGMEQKISK FSPIEEAKDV ESDLASYPPP TVSSSLTSRG RKFQDEITYG
     LKKNVYEQQR YYGVSSRDAA EEDERMYGSS SRSRMASAYS GEKLSSHDYS SRGKGYERER
     DTAERLQKAG SKPSSLSMAH GRARPPMRSQ ASEEESPVSP LGRPRPAGGA LPPGDTCPQF
     CSSHSMPDVQ EHVKDGPRAH AYKREEGYML DDSHCVVSDS EAYHLGQEET DWFDKPRDAR
     SDRFRHHGGH TVSSSQKRGP ARHSYHDYDE PPEEGLWPHD EGGPGRHTSA KEHRHHSDHG
     RHSGRHAGEE PGRRAAKPHA RDMGRHEARP HPQASPAPAM QKKGQPGYPS SADYSQSSRA
     PSAYHHASES KKGSRQAHTG PSALQPKADT QAQPQMQGRQ AAPGPQQSQP PSSRQTPSGT
     ASRQPQTQQQ QQQQQQQQGL GQQAPQQAPS QARLQPQSQP TTRGTAPAAS QPAGKPQPGP
     TTAPGPQPAG PPRAEQASSS KPPAAKAPQQ GRAPQAQTTP GPGPAGAKPG ARPGGTPGAP
     AGQPGAEGES VFSKILPGGA AEQAGKLTEA VSAFGKKFSS FW
//
ID   O88738_MOUSE            Unreviewed;      4845 AA.
AC   O88738;
DT   01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   SubName: Full=Ubiquitin-conjugating enzyme;
GN   Name=Birc6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=98292517; PubMed=9628897; DOI=10.1083/jcb.141.6.1415;
RA   Hauser H.P., Bardroff M., Pyrowolakis G., Jentsch S.;
RT   "A giant ubiquitin-conjugating enzyme related to IAP apoptosis
RT   inhibitors.";
RL   J. Cell Biol. 141:1415-1422(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Jentsch S.P.;
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- INTERACTION:
CC       O15392:BIRC5 (xeno); NbExp=1; IntAct=EBI-912068, EBI-518823;
CC       P06493:CDC2 (xeno); NbExp=1; IntAct=EBI-912068, EBI-444308;
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DR   EMBL; Y17267; CAA76720.1; -; mRNA.
DR   IPI; IPI00134095; -.
DR   PIR; T31067; T31067.
DR   RefSeq; NP_031592.2; NM_007566.2.
DR   UniGene; Mm.447926; -.
DR   UniGene; Mm.476864; -.
DR   HSSP; P98170; 1I3O.
DR   ProteinModelPortal; O88738; -.
DR   SMR; O88738; 258-358, 4509-4806.
DR   IntAct; O88738; 7.
DR   MINT; MINT-4105645; -.
DR   STRING; O88738; -.
DR   MEROPS; I32.006; -.
DR   PhosphoSite; O88738; -.
DR   PRIDE; O88738; -.
DR   Ensembl; ENSMUST00000024879; ENSMUSP00000024879; ENSMUSG00000024073.
DR   GeneID; 12211; -.
DR   KEGG; mmu:12211; -.
DR   UCSC; uc008doe.1; mouse.
DR   CTD; 12211; -.
DR   MGI; MGI:1276108; Birc6.
DR   eggNOG; roNOG04204; -.
DR   HOGENOM; HBG355747; -.
DR   HOVERGEN; HBG050691; -.
DR   InParanoid; O88738; -.
DR   OrthoDB; EOG4DJJVH; -.
DR   NextBio; 280605; -.
DR   ArrayExpress; O88738; -.
DR   Bgee; O88738; -.
DR   Genevestigator; O88738; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:MGI.
DR   GO; GO:0006916; P:anti-apoptosis; IMP:MGI.
DR   GO; GO:0060711; P:labyrinthine layer development; IMP:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0043687; P:post-translational protein modification; IEA:InterPro.
DR   GO; GO:0051246; P:regulation of protein metabolic process; IEA:InterPro.
DR   GO; GO:0060712; P:spongiotrophoblast layer development; IMP:MGI.
DR   InterPro; IPR001370; BIR.
DR   InterPro; IPR022103; DUF3643.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   Gene3D; G3DSA:1.10.1170.10; BIR; 1.
DR   Gene3D; G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 4.
DR   Pfam; PF00653; BIR; 1.
DR   Pfam; PF12356; DUF3643; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00238; BIR; 1.
DR   SUPFAM; SSF54495; UBQ-conjugat/RWD-like; 1.
DR   PROSITE; PS50143; BIR_REPEAT_2; 1.
DR   PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE   1: Evidence at protein level;
SQ   SEQUENCE   4845 AA;  528424 MW;  35C585F73B8CF84C CRC64;
     MAAAAAEASG PSCSSAAAAA GAGAAGVSEW LVLRDGCMRC DADGLHSLSY HPALNAILAV
     TSRGTIKVID GTSGATLQAS ALSAKPGGQV KCQYISAVDK VIFVDDYAVG CRKDLNGILL
     LDTALQTPVS KQDDVVQLEL PVTEAQQLLS ACIEKIDVSS TEGYDLFITQ LKDGLKNISH
     ETAANHKVAK WATVTFHLPH HVLKSIASAI VNELKKINQN VAALPVASSV MDRLSYLLPS
     ARPELGVGPG RSVDRALMYS EANRRETFTS WPHVGYRWAQ PDPMAQAGFY HQPASSGDDR
     AMCFTCSVCL VCWEPTDEPW SEHERHSPNC PFVKGEHTQN VPLSVTLATS PAQLPSADGA
     DRIACFGSGS CPQFLAAATK RGKICIWDVS KLMKVHLKFE INAYDPAIVQ QLILSGDPSS
     GVDSRRPTLA WLEDSSSCSD IPKLEGDSDD LLEDSDSEEH SRSDSVTGHT SQKEAMEVSL
     DITALSILQQ PEKLQWEIVA NVLEDTVKDL EELGANPSLT NSKSEKTKEK HQEQHNIPFP
     CLLAGGLLTY KSPATSPISS NSHRSLDGLS RTQGESISEQ GSTDNESCTN SELNSPLVRR
     TLPVLLLYSI KESDEKAGKI FSQMNNIMSK SLHDDGFTVP QIIEMELDNQ EQLLLQDPPV
     TYIQQFADAA ASLTSPDSEK WNSVFPKPGT LVQCLRLPKF AEEETLCIDS ITPCADGIHL
     LVGLRTCSVE SLSAINQVEA LNNLNKLNSA LCNRRKGDLE SNLAVVNGAN ISVIQHESPA
     DVPEHLLIRP EQRNVVSGGY LVLYKMNYTT RIVTLEEEPV KIQHIKDPQD TITSLILLPP
     DILDNREDDC EEPAEEMQLA SKNGIEREKK SDISTLGHLV VTTQGGYVKV LDLSNFEILA
     KVEPPKKEGT EEQDTFVSVI YCSGTDRLCA CTKGGELHFL QIGGTCDDID EADILVDGSL
     SKGIEPALEG SRPLSNPSSP GISGVELLVD QPFTLEILTS LVELTRFETL TPRFSATVPP
     CWVEVQQEQQ QRRHPQHLHQ QHHGDAAQHT RTWKLQTDSN SWDEHVFELV LPKACMVGHV
     DFKFVLNSNI TSVPQIQVTL LKNKAPGLGK ANALNIEVEH NGNPSLVDLN EEMHHMDVEE
     SQCLRLCPFL EDHKEDILCG PVWLASGLDL SGHAGMLTLT SPKLVKGMAG GKYRSFLIHV
     KAVSDRGAAD EMCSSGLRPV VRLPSLKQQG HKGYSLASLL AKVAAGKEKS SNVKNENAGG
     TRKSENLRGC DLLQEVSVTI RRFKKTSICK ERVQRCAMLQ FSEFHEKLLN TLCRRSDDGQ
     VTEHAQSLVL DALCWLAGVH SNGSGSSKEG NECLLSKTRK CLSDIVRVCF FEAGRSIAHK
     CARFLALCIS NGKCEPCQPG FGSVLLKALL DNMCFLPAAA TGGSVYWYFV LLNYVKDEDL
     AGCSTACAAL LTAVSRQLQD RLTPLEALLQ TRYGLYSSPF DPVLFDLEMS GSSWKTVYSS
     STAVQSDEID LSDVLSGNGR VSSCTAAEGS FTSLTGLLEV EPLHFTCVST SDGTRIERDD
     ASTFTVSSFG VPPAVGGLSS GTVGEASTAL SSAAQVALQS LSHAMASAEQ QLQVLQEKQQ
     QLLKLQQQKA KLEAKLHQTT AAAAAAASAA AAAAAGPVHN AVPSNPVAAP GFFIHPSDVI
     PPTPKTTPLF MTPPLTPPNE AVSVVINAEL AQLFPGSVID PPAVNLAAQN KNSSKSRMNP
     LGSGLALAIS HASHFLQPPP HQSIIIERMH SGARRFVTLD FGRPILLTDV LIPTCGDLAS
     LSIDIWTLGE EVDGRRLVVA TDISTHSLIL HDLIPPPVCR FMKITVIGRY GSTNARAKIP
     LGFYYGHSYI LPWESELKLM HDPLRGEGES ASQPEIDQHL AMMVALQEDI QCRYNLACHR
     LEALLQSIDL PPLNSANNAQ YFLRKPDKAV EEDSRVFSAY QDCIQLQLQL NLAHNAVQRL
     KVAIGASRKL LNETSGPEDL IQTSSTEQLR TIVRYLLDTL LSLLHSSNGH SVPAVLQSTF
     HAQACEELFK HLCISGTPKI RLHTGLLLVQ LCGGERWWRQ FLSNVLQELY NSEQLLIFPQ
     DRVFMLLSCI GQRSLSNSGV LESLLNLLDN LLSPLQPELS MHRRTEGVLD IPMISWVVML
     VSRLLDYVAT VEDEAAAAKK PLNGNQWSFI NNNLHTQNLN RSSKGGSSLD RLYSRKIRKQ
     LVHHKQQLNL LKAKQKALVE QMEKEKIQSN KGSSYKLLVE QAKLKQATSK HFKDLIRLRR
     TAEWSRSNLD TEVTTTKESP EIEPLPFTLA HDRCISVVQK LVLFLLSMDF TCHADLLLFV
     CKVLARIANA TRPTIHLCEI VNEPQLERLL LLLVGTDFNR GDISWGGAWA QYSLTCMLQD
     ILAGELLAPV AAEAMEEGTV SEDVGATAGD SDDSLQQSPA QLLETIDEPL THEIAGTPPL
     SSLEKDKEID LELLQDLMEV DIDPLDIDLE KDPLAAKVFK PISSTWYDYW GADYGTYNYN
     PYIGGLGMPV AKPPSNTEKN GSQTVSVSVS QALDARLEVG LEQQAELMLK MMSTLEADSI
     LQALTNTSPT FSQSPTGTDD SLLGNLQPAN QNSQLMIQLS SVPMLNVCFN KLFSMLQVHH
     VQLESLLQLW LTLSLNSSSS GNKENGADIF LYNANRIPVI SLNQASIASF LTVLAWYPNT
     LLRTWCLVLH SLTLMTNMQL NSGSSSSIGI QETTAHLLVS DPNLIHVLVK FLSGTSPHGT
     NQHSPQVGPT ATQAMQEFLT RLQVHLSSTC PQIFSELLLK LIHILSTERG AFQTGQGPLD
     AQVKLLEFTL EQNFEVVSVS TISAVIESVT FLVHHYITCS DKVMSRSGSD SSAGARACFG
     GLFANLIRPG DAKAVCGEMT RDQLMFDLLK LVNILVQLPL SSNREYSARV SVTTNTTDSV
     SDEEKVSGGK DVNGSSASIP GSPACVADLV LANQQIMSQI LSALGLCNSS AMAMIIGASG
     LHLTKHENFH GGLDAISVGD GLFTILTTLS KKASTVHMML QPILTYMACG YMGRQGSLAT
     CQLSEPLLWF ILRVLDTSDA LKAFHDMGGV QLICNNMVTS TRAIVNTARS MVSTIMKFLD
     SGPNKAVDST LKTRILASEP DNAEGIHNFA PLGTITSSSP TAQPAEVLLQ ATPPHRRARS
     AAWSYIFLPE EAWCDLTIHL PSAVLLKEIH IQPHLASLAT CPSSVTVEVS ADGVNMLPLS
     TPVVTSGLTY IKIQLVKAEV ASAVCLRLHR PRDASTLGLS QIKLLGLTAF GTTSSATVNN
     PFLPSEDQVS KTSIGWLRLL HHCLTHISDL EGMMASAAAP TANLLQTCAA LLMSPYCGMH
     SPNIEVVLVK IGLQSTRIGL KLIDILLRNC AASGSDPTDL NSPLLFGRLN GLSSDSTIDI
     LYQLGTTQDP GTKDRIQALL KWVSDSAKMA ALKRSGRMNY MCPSSSAVEY GLLMPSPSHL
     HCVAAILWHS YELLVEYDLP ALLDRELFEL LFNWSMSLPC NVVLKKAVDS LLCSMCHIHP
     NYFSLLMGWM GIIPPPVQCH HRLSMTDDSK KQDLSSSLTD DSKNAQAPLS LTESHLATLA
     SSSQSPEAIK QLLDSGLPSL LVRSLASFCF SHISYSESIA QSVDNSQDKL RRHHVPQHCN
     KMPITADLVA PILRFLTEVG NSHIMKDWLG GSEVNPLWTA LLFLLCHSGS TAGGHNLGAQ
     QSSTRSASHS SATTTVLTTQ QRTAIENATV AFFLQCISCH PNNQKLMAQV LCELFQTAPQ
     RGSLPTSGNI SGFVRRLFLQ LMLEDEKVTM FLQSPCPLYK GRINATSHVI QHPMFGAGHK
     FRTLHLPVST TLSDVLDRVS DTPSITAKLI SEQKDDKEKK NHEEKEKVKA ENGFQDNYSV
     VVASGLKSQS KRAVASTPPR PPSRRGRTVP DKIGSASSSA DAASKIITVP VFHLFHRLLA
     GQPLPAEMTL AQLLTLLYDR KLPQGYRSID LTVKLGSKVI TDPSLSKTDS FKRLHPEKDH
     GDLVGSCPED EALTPSDECM DGVLDESLLE TCPIQSPLQV FAGMGGLALI AERLPMLYPE
     VIQQVSAPVI ASTTQEKPKD SDQFEWVTIE QSGELVYEAP ETIAAEPPPV KSAVQATSPI
     PAHSLAAFGL FLRLPGYAEV LLKERKHAQC LLRLVLGVTD DGEGSHILQS PSANVLPTLP
     FHVLRSLFSA TPLTTDDGVL LRRMALEIGA LHLILVCLSA LSHHAPRVPN SSLSQTEPQV
     SNSHNPTSAE EQQLYWAKGT GFGTGSTASG WDVEQALTKQ RLEEEHVTCL LQVLASYINP
     MSGAVNGEAQ ASPESRAQNS SALPSMLLEL LSQSCLIPAM SSYLRNDSVL DMARHVPLYR
     ALLELLRAIA SCTSMVPLLL PLSTENGEEE EDEQSECQTS VGTLLAKMKT CVDTYTNRLR
     SKRENVKAGV KPDAPDQEPE GLALLVPDIQ RTAEIVHAAT ANLRQANQEK KLGEYSKKVV
     MKPKPLSVLK SLEEKYVAVM KKLQFDTFEM VSEDDDGKLG FKVNYHYMSQ VKNANDANSA
     ARARRLAQEA VTLSTSLPLS SSSSVFVRCD EERLDIMKVL ITGPADTPYA NGCFEFDVYF
     PQDYPSSPPL VNLETTGGHS VRFNPNLYND GKVCLSILNT WHGRPEEKWN PQTSSFLQVL
     VSVQSLILVA EPYFNEPGYE RSRGTPSGTQ SSREYDGNIR QATVKWAMLE QIRNPSPCFK
     EVIHKHFYLK RIELMAQCEE WIADIQQYSS DKRVGRTMSH HAAALKRHTA QLREELLKLP
     CPEGLDPDIE DASPVCRATA GAEDTLTHDH VNPSSSKDLP SDFQL
//
ID   TOM1_MOUSE              Reviewed;         492 AA.
AC   O88746; Q3V4C6; Q9D120;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Target of Myb protein 1;
GN   Name=Tom1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=99263500; PubMed=10329004; DOI=10.1006/geno.1998.5739;
RA   Seroussi E., Kedra D., Kost-Alimova M., Sandberg-Nordqvist A.-C.,
RA   Fransson I., Jacobs J.F.M., Fu Y., Pan H.-Q., Roe B.A., Imreh S.,
RA   Dumanski J.P.;
RT   "TOM1 genes map to human chromosome 22q13.1 and mouse chromosome 8C1
RT   and encode proteins similar to the endosomal proteins HGS and STAM.";
RL   Genomics 57:380-388(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174; SER-176 AND
RP   SER-180, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May be involved in intracellular trafficking. Probable
CC       association with membranes.
CC   -!- SUBUNIT: Interacts with ZFYVE16; interaction is required to target
CC       it to endosomes (By similarity).
CC   -!- INTERACTION:
CC       P51693:APLP1 (xeno); NbExp=1; IntAct=EBI-74264, EBI-74648;
CC       Q9QZ06:Tollip; NbExp=1; IntAct=EBI-74264, EBI-74272;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). Membrane; Peripheral
CC       membrane protein (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O88746-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O88746-2; Sequence=VSP_003991, VSP_003992;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. In adult brain, it is highly
CC       expressed at the mesencephalic level, in the hippocampal formation
CC       and medial lemniscus. In cerebellum, it is highly expressed in
CC       Purkinje cells and granular layers.
CC   -!- DEVELOPMENTAL STAGE: Ubiquitously expressed in the embryo, with a
CC       higher expression in the intestines.
CC   -!- SIMILARITY: Belongs to the TOM1 family.
CC   -!- SIMILARITY: Contains 1 GAT domain.
CC   -!- SIMILARITY: Contains 1 VHS domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ006972; CAA07361.1; -; mRNA.
DR   EMBL; AK004063; BAE43160.1; -; mRNA.
DR   EMBL; AK028398; BAC25932.1; -; mRNA.
DR   EMBL; BC021633; AAH21633.1; -; mRNA.
DR   IPI; IPI00222197; -.
DR   IPI; IPI00380814; -.
DR   RefSeq; NP_035752.1; NM_011622.3.
DR   UniGene; Mm.1967; -.
DR   UniGene; Mm.290868; -.
DR   ProteinModelPortal; O88746; -.
DR   SMR; O88746; 2-153, 183-307.
DR   IntAct; O88746; 4.
DR   PhosphoSite; O88746; -.
DR   PRIDE; O88746; -.
DR   Ensembl; ENSMUST00000036712; ENSMUSP00000036849; ENSMUSG00000037827.
DR   GeneID; 21968; -.
DR   KEGG; mmu:21968; -.
DR   UCSC; uc009mha.1; mouse.
DR   UCSC; uc009mhb.1; mouse.
DR   CTD; 21968; -.
DR   MGI; MGI:1338026; Tom1.
DR   eggNOG; roNOG08096; -.
DR   HOGENOM; HBG388010; -.
DR   HOVERGEN; HBG025068; -.
DR   InParanoid; O88746; -.
DR   OMA; GAIPVTQ; -.
DR   OrthoDB; EOG447FT4; -.
DR   PhylomeDB; O88746; -.
DR   NextBio; 301662; -.
DR   PMAP-CutDB; O88746; -.
DR   Bgee; O88746; -.
DR   CleanEx; MM_TOM1; -.
DR   Genevestigator; O88746; -.
DR   GermOnline; ENSMUSG00000037827; Mus musculus.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR004152; GAT.
DR   InterPro; IPR014645; TOM1.
DR   InterPro; IPR002014; VHS.
DR   InterPro; IPR018205; VHS_subgroup.
DR   Gene3D; G3DSA:1.25.40.90; ENTH_VHS; 1.
DR   Pfam; PF03127; GAT; 1.
DR   Pfam; PF00790; VHS; 1.
DR   PIRSF; PIRSF036948; TOM1; 1.
DR   SMART; SM00288; VHS; 1.
DR   SUPFAM; SSF48464; ENTH_VHS; 1.
DR   PROSITE; PS50909; GAT; 1.
DR   PROSITE; PS50179; VHS; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Membrane;
KW   Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1    492       Target of Myb protein 1.
FT                                /FTId=PRO_0000072629.
FT   DOMAIN       20    152       VHS.
FT   DOMAIN      215    303       GAT.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     130    130       Phosphoserine (By similarity).
FT   MOD_RES     131    131       Phosphoserine (By similarity).
FT   MOD_RES     160    160       Phosphoserine (By similarity).
FT   MOD_RES     164    164       Phosphothreonine (By similarity).
FT   MOD_RES     174    174       Phosphothreonine.
FT   MOD_RES     176    176       Phosphoserine.
FT   MOD_RES     180    180       Phosphoserine.
FT   MOD_RES     355    355       Phosphoserine (By similarity).
FT   MOD_RES     386    386       Phosphotyrosine (By similarity).
FT   MOD_RES     462    462       Phosphoserine (By similarity).
FT   MOD_RES     464    464       Phosphoserine (By similarity).
FT   VAR_SEQ       1    324       Missing (in isoform 2).
FT                                /FTId=VSP_003991.
FT   VAR_SEQ     325    343       MGPDPAATNNLSSQLAGMN -> MGRANGTAGLLPGPSVSA
FT                                D (in isoform 2).
FT                                /FTId=VSP_003992.
SQ   SEQUENCE   492 AA;  54325 MW;  A15F24FD9B4D31C3 CRC64;
     MDFLLGNPFS SPVGQRIEKA TDGSLQSEDW ALNMEICDII NETEEGPKDA FRAVKKRIMG
     NKNFHEVMLA LTVLETCVKN CGHRFHVLVA NQDFVENVLV RTILPKNNPP TIVHDKVLNL
     IQSWADAFRS SPDLTGVVAV YEDLRRKGLE FPMTDLDMLS PIHTPQRTVF NSETPSRQNS
     VSSNTSQRGD LSQHATPLPT PAVLPGDSPI TPTPEQIGKL RSELEMVSGN VRVMSEMLTE
     LVPTQVEPAD LELLQELNRT CRAMQQRILE LIPRISNEQL TEELLMINDN LNNVFLRHER
     FERFRTGQTA KASSEAELAT DLIDMGPDPA ATNNLSSQLA GMNLGSRSVR AGLQSLETSG
     HLEDDFDMFA LTRGSSLADQ RKGVKYEAPQ TTDGLAGALD ARQQSTGAIP ATQARIMEDI
     EQWLSTDVGN SAEEPSGVTS EEFDKFLEER AKAADRLPNL ASPSAEGPPR PSPGTAPRRK
     TQEKDDDMLF AL
//
ID   JAM1_MOUSE              Reviewed;         300 AA.
AC   O88792;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Junctional adhesion molecule A;
DE            Short=JAM-A;
DE   AltName: Full=Junctional adhesion molecule 1;
DE            Short=JAM-1;
DE   AltName: CD_antigen=CD321;
DE   Flags: Precursor;
GN   Name=F11r; Synonyms=Jam1, Jcam, Jcam1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98327120; PubMed=9660867; DOI=10.1083/jcb.142.1.117;
RA   Martin-Padura I., Lostaglio S., Schneemann M., Williams L., Romano M.,
RA   Fruscella P., Panzeri C., Stoppacciaro A., Ruco L., Villa A.,
RA   Simmons D., Dejana E.;
RT   "Junctional adhesion molecule, a novel member of the immunoglobulin
RT   superfamily that distributes at intercellular junctions and modulates
RT   monocyte transmigration.";
RL   J. Cell Biol. 142:117-127(1998).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=20489356; PubMed=11036763;
RA   Aurrand-Lions M.A., Duncan L., Du Pasquier L., Imhof B.A.;
RT   "Cloning of JAM-2 and JAM-3: an emerging junctional adhesion molecular
RT   family?";
RL   Curr. Top. Microbiol. Immunol. 251:91-98(2000).
RN   [3]
RP   INTERACTION WITH PARD3.
RX   MEDLINE=21340266; PubMed=11447115; DOI=10.1093/emboj/20.14.3738;
RA   Ebnet K., Suzuki A., Horikoshi Y., Hirose T.,
RA   Meyer zu Brickwedde M.-K., Ohno S., Vestweber D.;
RT   "The cell polarity protein ASIP/PAR-3 directly associates with
RT   junctional adhesion molecule (JAM).";
RL   EMBO J. 20:3738-3748(2001).
RN   [4]
RP   REVIEW, AND NOMENCLATURE.
RX   MEDLINE=22695901; PubMed=12810109; DOI=10.1016/S1471-4906(03)00117-0;
RA   Muller W.A.;
RT   "Leukocyte-endothelial-cell interactions in leukocyte transmigration
RT   and the inflammatory response.";
RL   Trends Immunol. 24:327-334(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285 AND SER-288, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-185, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-42 AND ASN-185, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 27-238.
RX   MEDLINE=21391702; PubMed=11500366; DOI=10.1093/emboj/20.16.4391;
RA   Kostrewa D., Brockhaus M., D'Arcy A., Dale G.E., Nelboeck P.,
RA   Schmid G., Mueller F., Bazzoni G., Dejana E., Bartfai T.,
RA   Winkler F.K., Hennig M.;
RT   "X-ray structure of junctional adhesion molecule: structural basis for
RT   homophilic adhesion via a novel dimerization motif.";
RL   EMBO J. 20:4391-4398(2001).
CC   -!- FUNCTION: Seems to plays a role in epithelial tight junction
CC       formation. Appears early in primordial forms of cell junctions and
CC       recruits PARD3. The association of the PARD6-PARD3 complex may
CC       prevent the interaction of PARD3 with JAM1, thereby preventing
CC       tight junction assembly. Plays a role in regulating monocyte
CC       transmigration involved in integrity of epithelial barrier.
CC       Involved in platelet activation. In case of orthoreovirus
CC       infection, serves as receptor for the virus (By similarity).
CC   -!- SUBUNIT: Interacts with the ninth PDZ domain of MPDZ. Interacts
CC       with the first PDZ domain of PARD3. The association between PARD3
CC       and PARD6B probably disrupts this interaction. Interacts with the
CC       orthoreovirus sigma-1 capsid protein (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction. Cell
CC       membrane; Single-pass type I membrane protein. Note=Localized at
CC       tight junctions of both epithelial and endothelial cells.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC   -!- SIMILARITY: Contains 2 Ig-like V-type (immunoglobulin-like)
CC       domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U89915; AAC32982.1; -; mRNA.
DR   IPI; IPI00316159; -.
DR   UniGene; Mm.294882; -.
DR   PDB; 1F97; X-ray; 2.50 A; A=27-238.
DR   PDBsum; 1F97; -.
DR   ProteinModelPortal; O88792; -.
DR   SMR; O88792; 27-238.
DR   MINT; MINT-247376; -.
DR   STRING; O88792; -.
DR   PhosphoSite; O88792; -.
DR   Ensembl; ENSMUST00000043839; ENSMUSP00000041907; ENSMUSG00000038235.
DR   MGI; MGI:1321398; F11r.
DR   eggNOG; roNOG16058; -.
DR   HOGENOM; HBG446408; -.
DR   HOVERGEN; HBG000518; -.
DR   InParanoid; O88792; -.
DR   OrthoDB; EOG4VT5XV; -.
DR   ArrayExpress; O88792; -.
DR   Bgee; O88792; -.
DR   CleanEx; MM_F11R; -.
DR   Genevestigator; O88792; -.
DR   GermOnline; ENSMUSG00000038235; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005923; C:tight junction; IMP:MGI.
DR   GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR   GO; GO:0030855; P:epithelial cell differentiation; IDA:MGI.
DR   GO; GO:0044419; P:interspecies interaction between organisms; IEA:UniProtKB-KW.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR003596; Ig_V-set_sub.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Pfam; PF07679; I-set; 2.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00406; IGv; 1.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Cell junction; Cell membrane; Disulfide bond;
KW   Glycoprotein; Host-virus interaction; Immunoglobulin domain; Membrane;
KW   Phosphoprotein; Repeat; Signal; Tight junction; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     26       Potential.
FT   CHAIN        27    300       Junctional adhesion molecule A.
FT                                /FTId=PRO_0000015067.
FT   TOPO_DOM     27    238       Extracellular (Potential).
FT   TRANSMEM    239    259       Helical; (Potential).
FT   TOPO_DOM    260    299       Cytoplasmic (Potential).
FT   DOMAIN       28    122       Ig-like V-type 1.
FT   DOMAIN      134    230       Ig-like V-type 2.
FT   MOD_RES     273    273       Phosphothreonine (By similarity).
FT   MOD_RES     281    281       Phosphotyrosine (By similarity).
FT   MOD_RES     282    282       Phosphoserine (By similarity).
FT   MOD_RES     285    285       Phosphoserine.
FT   MOD_RES     288    288       Phosphoserine.
FT   MOD_RES     297    297       Phosphoserine (By similarity).
FT   CARBOHYD     42     42       N-linked (GlcNAc...).
FT   CARBOHYD    185    185       N-linked (GlcNAc...).
FT   DISULFID     49    108
FT   DISULFID    152    212
FT   STRAND       29     31
FT   STRAND       35     40
FT   STRAND       45     48
FT   STRAND       50     53
FT   STRAND       55     65
FT   STRAND       68     74
FT   HELIX        80     82
FT   TURN         83     85
FT   STRAND       86     89
FT   STRAND       92     96
FT   HELIX       100    102
FT   STRAND      104    112
FT   STRAND      115    129
FT   STRAND      135    137
FT   STRAND      140    143
FT   STRAND      148    153
FT   STRAND      162    167
FT   STRAND      170    173
FT   STRAND      184    186
FT   STRAND      188    190
FT   TURN        192    194
FT   STRAND      197    201
FT   HELIX       204    206
FT   STRAND      208    215
FT   STRAND      217    219
FT   STRAND      227    234
SQ   SEQUENCE   300 AA;  32369 MW;  391F3E48FF3B97EC CRC64;
     MGTEGKAGRK LLFLFTSMIL GSLVQGKGSV YTAQSDVQVP ENESIKLTCT YSGFSSPRVE
     WKFVQGSTTA LVCYNSQITA PYADRVTFSS SGITFSSVTR KDNGEYTCMV SEEGGQNYGE
     VSIHLTVLVP PSKPTISVPS SVTIGNRAVL TCSEHDGSPP SEYSWFKDGI SMLTADAKKT
     RAFMNSSFTI DPKSGDLIFD PVTAFDSGEY YCQAQNGYGT AMRSEAAHMD AVELNVGGIV
     AAVLVTLILL GLLIFGVWFA YSRGYFETTK KGTAPGKKVI YSQPSTRSEG EFKQTSSFLV
//
ID   IDHC_MOUSE              Reviewed;         414 AA.
AC   O88844;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Isocitrate dehydrogenase [NADP] cytoplasmic;
DE            Short=IDH;
DE            EC=1.1.1.42;
DE   AltName: Full=Cytosolic NADP-isocitrate dehydrogenase;
DE   AltName: Full=IDP;
DE   AltName: Full=NADP(+)-specific ICDH;
DE   AltName: Full=Oxalosuccinate decarboxylase;
GN   Name=Idh1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99083434; PubMed=9866202;
RA   Nekrutenko A., Hillis D.M., Patton J.C., Bradley R.D., Baker R.J.;
RT   "Cytosolic isocitrate dehydrogenase in humans, mice, and voles and
RT   phylogenetic analysis of the enzyme family.";
RL   Mol. Biol. Evol. 15:1674-1684(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 30-49.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY: Isocitrate + NADP(+) = 2-oxoglutarate + CO(2)
CC       + NADPH.
CC   -!- CATALYTIC ACTIVITY: Oxalosuccinate + NADP(+) = 2-oxoglutarate +
CC       CO(2) + NADPH.
CC   -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF020039; AAD02919.1; -; mRNA.
DR   IPI; IPI00135231; -.
DR   UniGene; Mm.9925; -.
DR   PDB; 2CMJ; X-ray; 1.99 A; A/B=4-413.
DR   PDB; 2CMV; X-ray; 2.52 A; A/B=4-413.
DR   PDBsum; 2CMJ; -.
DR   PDBsum; 2CMV; -.
DR   ProteinModelPortal; O88844; -.
DR   SMR; O88844; 4-413.
DR   STRING; O88844; -.
DR   PhosphoSite; O88844; -.
DR   SWISS-2DPAGE; O88844; -.
DR   COMPLUYEAST-2DPAGE; O88844; -.
DR   REPRODUCTION-2DPAGE; O88844; -.
DR   PRIDE; O88844; -.
DR   Ensembl; ENSMUST00000097709; ENSMUSP00000095316; ENSMUSG00000025950.
DR   MGI; MGI:96413; Idh1.
DR   eggNOG; roNOG04762; -.
DR   HOVERGEN; HBG006119; -.
DR   OrthoDB; EOG47M1Z0; -.
DR   BRENDA; 1.1.1.42; 244.
DR   ArrayExpress; O88844; -.
DR   Bgee; O88844; -.
DR   CleanEx; MM_IDH1; -.
DR   Genevestigator; O88844; -.
DR   GermOnline; ENSMUSG00000025950; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0004450; F:isocitrate dehydrogenase (NADP+) activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006749; P:glutathione metabolic process; IMP:MGI.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006102; P:isocitrate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IDA:MGI.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR001804; Isocitrate/isopropylmalate_DH.
DR   InterPro; IPR004790; Isocitrate_DH_NADP-dep_euk.
DR   Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1.
DR   PANTHER; PTHR11822; IDH_NADP_euk; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   PIRSF; PIRSF000108; IDH_NADP; 1.
DR   TIGRFAMs; TIGR00127; nadp_idh_euk; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Glyoxylate bypass; Magnesium; Manganese; Metal-binding; NADP;
KW   Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN         1    414       Isocitrate dehydrogenase [NADP]
FT                                cytoplasmic.
FT                                /FTId=PRO_0000083578.
FT   NP_BIND      75     77       NADP (By similarity).
FT   NP_BIND     310    315       NADP (By similarity).
FT   REGION       94    100       Substrate binding (By similarity).
FT   METAL       252    252       Magnesium or manganese (By similarity).
FT   METAL       275    275       Magnesium or manganese (By similarity).
FT   BINDING      77     77       Substrate (By similarity).
FT   BINDING      82     82       NADP (By similarity).
FT   BINDING     109    109       Substrate (By similarity).
FT   BINDING     132    132       Substrate (By similarity).
FT   BINDING     260    260       NADP (By similarity).
FT   BINDING     328    328       NADP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   SITE        139    139       Critical for catalysis (By similarity).
FT   SITE        212    212       Critical for catalysis (By similarity).
FT   MOD_RES      81     81       N6-acetyllysine (By similarity).
FT   MOD_RES     224    224       N6-acetyllysine (By similarity).
FT   MOD_RES     321    321       N6-acetyllysine (By similarity).
FT   STRAND        5     14
FT   HELIX        17     30
FT   TURN         31     34
FT   STRAND       35     43
FT   HELIX        46     51
FT   TURN         52     54
FT   HELIX        55     67
FT   STRAND       68     72
FT   HELIX        80     86
FT   HELIX        95    103
FT   STRAND      106    111
FT   STRAND      128    133
FT   HELIX       137    140
FT   STRAND      142    146
FT   STRAND      148    162
FT   STRAND      165    172
FT   STRAND      177    185
FT   HELIX       186    203
FT   STRAND      207    211
FT   TURN        213    215
FT   HELIX       219    234
FT   HELIX       236    241
FT   STRAND      246    250
FT   HELIX       251    260
FT   STRAND      265    269
FT   HELIX       271    285
FT   STRAND      290    296
FT   STRAND      303    306
FT   HELIX       313    320
FT   HELIX       330    347
FT   HELIX       350    368
FT   HELIX       374    381
FT   HELIX       383    385
FT   HELIX       388    390
FT   HELIX       394    412
SQ   SEQUENCE   414 AA;  46660 MW;  AA482EA1C4114CAD CRC64;
     MSRKIQGGSV VEMQGDEMTR IIWELIKEKL ILPYVELDLH SYDLGIENRD ATNDQVTKDA
     AEAIKKYNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR NILGGTVFRE AIICKNIPRL
     VTGWVKPIII GRHAYGDQYR ATDFVVPGPG KVEITYTPKD GTQKVTYMVH DFEEGGGVAM
     GMYNQDKSIE DFAHSSFQMA LSKGWPLYLS TKNTILKKYD GRFKDIFQEI YDKKYKSQFE
     AQNICYEHRL IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLICPDG
     KTVEAEAAHG TVTRHYRMYQ KGQETSTNPI ASIFAWSRGL AHRAKLDNNT ELSFFAKALE
     DVCIETIEAG FMTKDLAACI KGLPNVQRSD YLNTFEFMDK LGENLKAKLA QAKL
//
ID   CCNK_MOUSE              Reviewed;         554 AA.
AC   O88874; Q8R068;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Cyclin-K;
GN   Name=Ccnk;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-222.
RC   TISSUE=Testis;
RX   MEDLINE=98298273; PubMed=9632813;
RA   Edwards M.C., Wong C., Elledge S.J.;
RT   "Human cyclin K, a novel RNA polymerase II-associated cyclin
RT   possessing both carboxy-terminal domain kinase and Cdk-activating
RT   kinase activity.";
RL   Mol. Cell. Biol. 18:4291-4300(1998).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325 AND SER-329, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325; SER-329 AND
RP   SER-341, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May play a role in transcriptional regulation. It is
CC       associated with an in vitro kinase activity toward both RNA
CC       polymerase II C-terminal domain and CDK2 (CAK) (By similarity).
CC   -!- SUBUNIT: Part of a cyclin-kinase pair in the RNA polymerase II
CC       holoenzyme. Binds to CDK9 (By similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highest levels in
CC       testis. Present throughout the seminiferous epithelium. Also
CC       highly expressed in the developing oocyte.
CC   -!- DEVELOPMENTAL STAGE: Found in 12.5 dpc embryo with abundant
CC       expression in eye (retinal pigment epithelium) and ear (cochlea,
CC       crista ampullaris of the semicircular canals).
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC027297; AAH27297.1; -; mRNA.
DR   EMBL; AF060517; AAD09979.1; -; mRNA.
DR   IPI; IPI00153134; -.
DR   UniGene; Mm.474441; -.
DR   ProteinModelPortal; O88874; -.
DR   SMR; O88874; 14-267.
DR   STRING; O88874; -.
DR   PhosphoSite; O88874; -.
DR   PRIDE; O88874; -.
DR   Ensembl; ENSMUST00000021683; ENSMUSP00000021683; ENSMUSG00000021258.
DR   UCSC; uc007ozm.1; mouse.
DR   MGI; MGI:1276106; Ccnk.
DR   eggNOG; roNOG09836; -.
DR   HOVERGEN; HBG050836; -.
DR   OrthoDB; EOG4KH2VJ; -.
DR   PhylomeDB; O88874; -.
DR   ArrayExpress; O88874; -.
DR   Bgee; O88874; -.
DR   CleanEx; MM_CCNK; -.
DR   Genevestigator; O88874; -.
DR   GermOnline; ENSMUSG00000021258; Mus musculus.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR006670; Cyclin.
DR   InterPro; IPR011028; Cyclin-like.
DR   InterPro; IPR013763; Cyclin-related.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR015429; Tscrpt_reg_cyclin.
DR   Gene3D; G3DSA:1.10.472.10; Cyclin_related; 1.
DR   PANTHER; PTHR10026; Trans_reg_cyclin; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   SMART; SM00385; CYCLIN; 2.
DR   SUPFAM; SSF47954; Cyclin_like; 2.
DR   PROSITE; PS00292; CYCLINS; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cyclin; Mitosis; Phosphoprotein;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    554       Cyclin-K.
FT                                /FTId=PRO_0000080479.
FT   MOD_RES       9      9       Phosphoserine (By similarity).
FT   MOD_RES     325    325       Phosphoserine.
FT   MOD_RES     329    329       Phosphoserine.
FT   MOD_RES     341    341       Phosphoserine.
FT   CONFLICT     73     73       N -> T (in Ref. 2; AAD09979).
FT   CONFLICT    202    202       E -> K (in Ref. 2; AAD09979).
SQ   SEQUENCE   554 AA;  61376 MW;  4C23FD1D2179E946 CRC64;
     MKENKENSSP SVTSANLDHT KPCWYWDKKD LAHTPSQLEG LDPATEARYR REGARFIFDV
     GTRLGLHYDT LANGIIYFHR FYMFHSFKQF PRYVTGACCL FLAGKVEETP KKCKDIIKTA
     RSLLNDVQFG QFGDDPKEEV MVLERILLQT IKFDLQVEHP YQFLLKYAKQ LKGDKNKIQK
     LVQMAWTFVN DSLCTTLSLQ WEPEIIAVAV MYLAGRLCKF EIQEWTSKPM YRRWWEQFVQ
     DVPVDVLEDI CHQILDLYSQ GKQQMPHHTP HQLQQPPSLQ PTPQVPQGPQ SQPSQGSEAA
     QPPQKDSQQS AQQQQQQAQQ PKKPSPQPSP PRQAKRAVVV SPKEENKATE PPPPPKIPKL
     EATHPPLPPA HPPPDRKPPL APALGEAEAT GPVETSDLPK VQIPPPAHPA PVHQPPPLPH
     RPPPPPPSSY MTGMSTTSSY MSGEGYQSLQ SMMKTEGPSY GALPPASFPP PTIPPPTPGY
     PPPPPTYNPN FPPPPPRLPP THAVPPHPPP GLGLPPASYP PPAVPPGGQP PVPPPIPPPG
     MPPVGGLGRA AWMR
//
ID   ZFAN5_MOUSE             Reviewed;         213 AA.
AC   O88878; Q3B7K8;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=AN1-type zinc finger protein 5;
DE   AltName: Full=Zinc finger A20 domain-containing protein 2;
DE   AltName: Full=Zinc finger protein 216;
GN   Name=Zfand5; Synonyms=Za20d2, Zfp216, Znf216;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=98428793; PubMed=9758550; DOI=10.1016/S0378-1119(98)00316-3;
RA   Scott D.A., Greinwald J.H. Jr., Marietta J.R., Drury S.,
RA   Swiderski R.E., Vinas A., DeAngelis M.M., Carmi R., Ramesh A.,
RA   Kraft M.L., Elbedour K., Skworak A.B., Friedman R.A.,
RA   Srikumari Srisailapathy C.R., Verhoeven K., Van Camp G., Lovett M.,
RA   Deininger P.L., Batzer M.A., Morton C.C., Keats B.J., Smith R.J.H.,
RA   Sheffield V.C.;
RT   "Identification and mutation analysis of a cochlear-expressed, zinc
RT   finger protein gene at the DFNB7/11 and dn hearing-loss loci on human
RT   chromosome 9q and mouse chromosome 19.";
RL   Gene 215:461-469(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=14754897; DOI=10.1074/jbc.M309491200;
RA   Huang J., Teng L., Li L., Liu T., Li L., Chen D., Xu L.-G., Zhai Z.,
RA   Shu H.-B.;
RT   "ZNF216 is an A20-like and IkappaB kinase gamma-interacting inhibitor
RT   of NFkappaB activation.";
RL   J. Biol. Chem. 279:16847-16853(2004).
RN   [5]
RP   INDUCTION, AND FUNCTION.
RX   PubMed=16194934; DOI=10.1080/10799890500240781;
RA   Hishiya A., Ikeda K., Watanabe K.;
RT   "A RANKL-inducible gene Znf216 in osteoclast differentiation.";
RL   J. Recept. Signal Transduct. 25:199-216(2005).
RN   [6]
RP   DISRUPTION PHENOTYPE, UBIQUITIN-BINDING, DOMAIN A20-TYPE ZINC FINGER,
RP   AND FUNCTION.
RX   PubMed=16424905; DOI=10.1038/sj.emboj.7600945;
RA   Hishiya A., Iemura S., Natsume T., Takayama S., Ikeda K., Watanabe K.;
RT   "A novel ubiquitin-binding protein ZNF216 functioning in muscle
RT   atrophy.";
RL   EMBO J. 25:554-564(2006).
RN   [7]
RP   STRUCTURE BY NMR OF 132-194.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the ZF-AN1 domain from mouse zinc finger
RT   protein 216.";
RL   Submitted (NOV-2004) to the PDB data bank.
CC   -!- FUNCTION: Inhibits NF-kappa-B activation triggered by
CC       overexpression of RIPK1 and TRAF6 but not of RELA. Inhibits also
CC       tumor necrosis (TNF), IL-1 and TLR4-induced NF-kappa-B activation
CC       in a dose-dependent manner. Overexpression sensitizes cells to
CC       TNF-induced apoptosis. Could be involved in regulating NF-kappa-B
CC       activation and apoptosis. Is a potent inhibitory factor for
CC       osteoclast differentiation. Involved in protein degradation via
CC       the ubiquitin-proteasome system and plays a critical role in
CC       muscle atrophy. May act by anchoring ubiquitinylated proteins to
CC       the proteasome, playing a critical role in protein degradation.
CC   -!- SUBUNIT: homooligomer and/or heterooligomer. Interacts (via A20-
CC       type domain) with IKBKG and RIPK1 and with TRAF6 (via AN1-type
CC       domain) (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in brain, muscle, eye, and heart,
CC       lower expression in lung, kidney, and spleen, and very low
CC       expression in liver. Expressed in myoblast C2C12 cells (at protein
CC       level).
CC   -!- INDUCTION: Up-regulated after TNFSF11 stimulation. Expression also
CC       induced by other cytokines such as TNF and IL1B. No significant
CC       inhibitory effect on the NF-kappa-B pathway is observed.
CC       Expression is increased in both denervation- and fasting-induced
CC       muscle atrophy.
CC   -!- DOMAIN: The A20-type zinc finger directly binds polyubiquitin
CC       chains and associates with the 26S proteasome. The zinc-finger
CC       A20-type domain is essential for inhibition of NF-kappa-B
CC       activation.
CC   -!- DISRUPTION PHENOTYPE: Resistance to muscle atrophy accompanied by
CC       abnormal accumulation of polyubiquitinylated proteins in skeletal
CC       muscle.
CC   -!- SIMILARITY: Contains 1 A20-type zinc finger.
CC   -!- SIMILARITY: Contains 1 AN1-type zinc finger.
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DR   EMBL; AF062071; AAC42600.1; -; mRNA.
DR   EMBL; AK076397; BAC36321.1; -; mRNA.
DR   EMBL; BC107566; AAI07567.1; -; mRNA.
DR   EMBL; BC119124; AAI19125.1; -; mRNA.
DR   EMBL; BC119126; AAI19127.1; -; mRNA.
DR   IPI; IPI00135365; -.
DR   RefSeq; NP_033577.1; NM_009551.4.
DR   UniGene; Mm.292405; -.
DR   UniGene; Mm.379919; -.
DR   PDB; 1WFL; NMR; -; A=134-194.
DR   PDBsum; 1WFL; -.
DR   ProteinModelPortal; O88878; -.
DR   SMR; O88878; 9-44, 140-196.
DR   STRING; O88878; -.
DR   PhosphoSite; O88878; -.
DR   PRIDE; O88878; -.
DR   Ensembl; ENSMUST00000025659; ENSMUSP00000025659; ENSMUSG00000024750.
DR   GeneID; 22682; -.
DR   KEGG; mmu:22682; -.
DR   UCSC; uc008gyw.1; mouse.
DR   CTD; 22682; -.
DR   MGI; MGI:1278334; Zfand5.
DR   eggNOG; roNOG04462; -.
DR   GeneTree; ENSGT00510000046525; -.
DR   HOGENOM; HBG747225; -.
DR   HOVERGEN; HBG053349; -.
DR   InParanoid; O88878; -.
DR   OMA; DASLNNC; -.
DR   OrthoDB; EOG44J2K0; -.
DR   PhylomeDB; O88878; -.
DR   NextBio; 461320; -.
DR   ArrayExpress; O88878; -.
DR   Bgee; O88878; -.
DR   CleanEx; MM_ZFAND5; -.
DR   Genevestigator; O88878; -.
DR   GermOnline; ENSMUSG00000024750; Mus musculus.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0060324; P:face development; IMP:MGI.
DR   GO; GO:0010761; P:fibroblast migration; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:MGI.
DR   GO; GO:0003016; P:respiratory system process; IMP:MGI.
DR   GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR   GO; GO:0048745; P:smooth muscle tissue development; IMP:MGI.
DR   GO; GO:0001944; P:vasculature development; IMP:MGI.
DR   InterPro; IPR002653; Znf_A20.
DR   InterPro; IPR000058; Znf_AN1.
DR   Gene3D; G3DSA:4.10.1110.10; Znf_AN1; 1.
DR   Pfam; PF01754; zf-A20; 1.
DR   Pfam; PF01428; zf-AN1; 1.
DR   SMART; SM00259; ZnF_A20; 1.
DR   SMART; SM00154; ZnF_AN1; 1.
DR   PROSITE; PS51036; ZF_A20; 1.
DR   PROSITE; PS51039; ZF_AN1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Metal-binding; Phosphoprotein; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    213       AN1-type zinc finger protein 5.
FT                                /FTId=PRO_0000066558.
FT   ZN_FING       8     42       A20-type.
FT   ZN_FING     151    194       AN1-type.
FT   MOD_RES      48     48       Phosphoserine (By similarity).
FT   STRAND      155    157
FT   HELIX       162    164
FT   STRAND      176    178
FT   TURN        181    185
FT   HELIX       190    192
SQ   SEQUENCE   213 AA;  23058 MW;  65B3B001DA6B8F59 CRC64;
     MAQETNQTPG PMLCSTGCGF YGNPRTNGMC SVCYKEHLQR QQNSGRMSPM GTASGSNSPT
     SDSASVQRAD AGLNNCEGAA GSTSEKSRNV PVAALPVTQQ MTEMSISRED KITTPKTEVS
     EPVVTQPSPS VSQPSSSQSE EKAPELPKPK KNRCFMCRKK VGLTGFDCRC GNLFCGLHRY
     SDKHNCPYDY KAEAAAKIRK ENPVVVAEKI QRI
//
ID   PIAS1_MOUSE             Reviewed;         651 AA.
AC   O88907; Q8C6H5;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 2.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=E3 SUMO-protein ligase PIAS1;
DE   AltName: Full=DEAD/H box-binding protein 1;
DE   AltName: Full=Protein inhibitor of activated STAT protein 1;
GN   Name=Pias1; Synonyms=Ddxbp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=B-cell;
RX   MEDLINE=98393695; PubMed=9724754; DOI=10.1073/pnas.95.18.10626;
RA   Liu B., Liao J., Rao X., Kushner S.A., Chung C.D., Chang D.D.,
RA   Shuai K.;
RT   "Inhibition of Stat1-mediated gene activation by PIAS1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:10626-10631(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=20311089; PubMed=10854042; DOI=10.1385/JMN:14:1-2:107;
RA   Sturm S., Koch M., White F.A.;
RT   "Cloning and analysis of a murine Pias family member, Pias-gamma, in
RT   developing skin and neurons.";
RL   J. Mol. Neurosci. 14:107-121(2000).
RN   [5]
RP   INTERACTION WITH AR.
RX   MEDLINE=21003591; PubMed=11117529; DOI=10.1210/me.14.12.1986;
RA   Kotaja N., Aittomaeki S., Silvennoinen O., Palvimo J.J., Jaenne O.A.;
RT   "ARIP3 (androgen receptor-interacting protein 3) and other PIAS
RT   (protein inhibitor of activated STAT) proteins differ in their ability
RT   to modulate steroid receptor-dependent transcriptional activation.";
RL   Mol. Endocrinol. 14:1986-2000(2000).
RN   [6]
RP   INTERACTION WITH SUMO1; UBE2I AND NCOA2, SUBCELLULAR LOCATION,
RP   SUMOYLATION OF AR AND NCOA2, AND MUTAGENESIS OF TRP-372.
RX   MEDLINE=22072593; PubMed=12077349;
RX   DOI=10.1128/MCB.22.14.5222-5234.2002;
RA   Kotaja N., Karvonen U., Jaenne O.A., Palvimo J.J.;
RT   "PIAS proteins modulate transcription factors by functioning as SUMO-1
RT   ligases.";
RL   Mol. Cell. Biol. 22:5222-5234(2002).
RN   [7]
RP   STAT1 SUMOYLATION.
RX   MEDLINE=22929837; PubMed=12855578; DOI=10.1182/blood-2002-12-3816;
RA   Ungureanu D., Vanhatupa S., Kotaja N., Yang J., Aittomaeki S.,
RA   Jaenne O.A., Palvimo J.J., Silvennoinen O.;
RT   "PIAS proteins promote SUMO-1 conjugation to STAT1.";
RL   Blood 102:3311-3313(2003).
RN   [8]
RP   SUMOYLATION OF KLF1, AND MUTAGENESIS OF CYS-346; CYS-351; CYS-356;
RP   ILE-363 AND 375-PRO-VAL-376.
RX   PubMed=17938210; DOI=10.1128/MCB.00589-07;
RA   Siatecka M., Xue L., Bieker J.J.;
RT   "Sumoylation of EKLF promotes transcriptional repression and is
RT   involved in inhibition of megakaryopoiesis.";
RL   Mol. Cell. Biol. 27:8547-8560(2007).
RN   [9]
RP   INTERACTION WITH NR2C1.
RX   PubMed=17187077; DOI=10.1038/nsmb1185;
RA   Park S.W., Hu X., Gupta P., Lin Y.P., Ha S.G., Wei L.N.;
RT   "SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4
RT   expression in stem cells.";
RL   Nat. Struct. Mol. Biol. 14:68-75(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483; SER-485 AND
RP   THR-487, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Functions as an E3-type small ubiquitin-like modifier
CC       (SUMO) ligase, stabilizing the interaction between UBE2I and the
CC       substrate, and as a SUMO-tethering factor. Plays a crucial role as
CC       a transcriptional coregulation in various cellular pathways,
CC       including the STAT pathway, the p53 pathway and the steroid
CC       hormone signaling pathway. In vitro, binds A/T-rich DNA (By
CC       similarity). The effects of this transcriptional coregulation,
CC       transactivation or silencing, may vary depending upon the
CC       biological context. Together with PRMT1, may repress STAT1
CC       transcriptional activity, in the late phase of interferon gamma
CC       (IFN-gamma) signaling.
CC   -!- PATHWAY: Protein modification; protein sumoylation.
CC   -!- SUBUNIT: Interacts with STAT1 (By similarity). Interacts with
CC       NR2C1; the interaction promotes its sumoylation. Interacts with
CC       DDX21, CSRP2, AXIN1, JUN, SATB2, PLAG1, TP53 and STAT1 (dimer),
CC       following IFNA1-stimulation. Interacts with SP3 (preferentially
CC       when SUMO-modified). Interacts with KLF8; the interaction results
CC       in SUMO ligation and repression of KLF8 transcriptional activity
CC       and of its cell cycle progression into G(1) phase (By similarity).
CC       Interacts with SUMO1, UBE2I, NCOA2 and AR. Interacts with NR2C1;
CC       the interaction promotes its sumoylation.
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle (By similarity).
CC       Note=Interaction with CSRP2 may induce a partial redistribution
CC       along the cytoskeleton (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in kidney, heart, spleen, brain and
CC       cerebellum; weak expression, if any, in liver and lung.
CC   -!- DEVELOPMENTAL STAGE: Expressed as early as 7.6 dpc. Expression
CC       remains high through 15.5 dpc.
CC   -!- DOMAIN: The LXXLL motif is a transcriptional coregulator
CC       signature.
CC   -!- DOMAIN: The SP-RING-type domain is required for promoting EKLF
CC       sumoylation.
CC   -!- PTM: Sumoylated (By similarity).
CC   -!- PTM: Dimethylated by PRMT1 at Arg-303 in the late phase of
CC       interferon gamma (IFN-gamma) signaling, leading to preferential
CC       interaction with STAT1 and thus resulting in release of STAT1 from
CC       its target gene (By similarity).
CC   -!- SIMILARITY: Belongs to the PIAS family.
CC   -!- SIMILARITY: Contains 1 PINIT domain.
CC   -!- SIMILARITY: Contains 1 SAP domain.
CC   -!- SIMILARITY: Contains 1 SP-RING-type zinc finger.
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DR   EMBL; AF077950; AAC36701.1; -; mRNA.
DR   EMBL; AK075708; BAC35902.1; -; mRNA.
DR   EMBL; BC051417; AAH51417.1; -; mRNA.
DR   IPI; IPI00268676; -.
DR   RefSeq; NP_062637.2; NM_019663.3.
DR   UniGene; Mm.431253; -.
DR   UniGene; Mm.479179; -.
DR   ProteinModelPortal; O88907; -.
DR   SMR; O88907; 1-65, 128-416.
DR   DIP; DIP-29277N; -.
DR   STRING; O88907; -.
DR   PhosphoSite; O88907; -.
DR   PRIDE; O88907; -.
DR   Ensembl; ENSMUST00000098651; ENSMUSP00000096248; ENSMUSG00000032405.
DR   GeneID; 56469; -.
DR   KEGG; mmu:56469; -.
DR   UCSC; uc009qas.1; mouse.
DR   CTD; 56469; -.
DR   MGI; MGI:1913125; Pias1.
DR   eggNOG; roNOG07102; -.
DR   HOGENOM; HBG315609; -.
DR   HOVERGEN; HBG053598; -.
DR   InParanoid; O88907; -.
DR   OMA; RFFPYAS; -.
DR   OrthoDB; EOG4G1MG3; -.
DR   NextBio; 312730; -.
DR   ArrayExpress; O88907; -.
DR   Bgee; O88907; -.
DR   CleanEx; MM_PIAS1; -.
DR   Genevestigator; O88907; -.
DR   GermOnline; ENSMUSG00000032405; Mus musculus.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
DR   GO; GO:0033235; P:positive regulation of protein sumoylation; ISS:UniProtKB.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR023321; PINIT.
DR   InterPro; IPR003034; SAP_DNA-bd.
DR   InterPro; IPR004181; Znf_MIZ.
DR   Pfam; PF02891; zf-MIZ; 1.
DR   SMART; SM00513; SAP; 1.
DR   PROSITE; PS51466; PINIT; 1.
DR   PROSITE; PS50800; SAP; 1.
DR   PROSITE; PS51044; ZF_SP_RING; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Methylation; Nucleus; Phosphoprotein;
KW   Repeat; Transcription; Transcription regulation; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    651       E3 SUMO-protein ligase PIAS1.
FT                                /FTId=PRO_0000218975.
FT   DOMAIN       11     45       SAP.
FT   DOMAIN      124    288       PINIT.
FT   REPEAT      520    523       1.
FT   REPEAT      557    560       2.
FT   REPEAT      598    601       3; approximate.
FT   REPEAT      612    615       4; approximate.
FT   ZN_FING     320    397       SP-RING-type.
FT   REGION      462    473       SUMO1-binding (By similarity).
FT   REGION      520    615       4 X 4 AA repeats of N-T-S-L.
FT   MOTIF        19     23       LXXLL motif.
FT   MOTIF        56     64       Nuclear localization signal (Potential).
FT   MOTIF       368    380       Nuclear localization signal (Potential).
FT   COMPBIAS    577    634       Ser-rich.
FT   MOD_RES     303    303       Asymmetric dimethylarginine; by PRMT1 (By
FT                                similarity).
FT   MOD_RES     466    466       Phosphoserine (By similarity).
FT   MOD_RES     467    467       Phosphoserine (By similarity).
FT   MOD_RES     468    468       Phosphoserine (By similarity).
FT   MOD_RES     483    483       Phosphoserine.
FT   MOD_RES     485    485       Phosphoserine.
FT   MOD_RES     487    487       Phosphothreonine.
FT   MOD_RES     503    503       Phosphoserine (By similarity).
FT   MOD_RES     510    510       Phosphoserine (By similarity).
FT   MOD_RES     522    522       Phosphoserine (By similarity).
FT   MUTAGEN     346    346       C->G: Loss of promotion of EKLF
FT                                sumoylation; when associated with G-351
FT                                and A-356.
FT   MUTAGEN     351    351       C->G: Loss of promotion of EKLF
FT                                sumoylation; when associated with G-346
FT                                and A-356.
FT   MUTAGEN     356    356       C->A: Loss of promotion of EKLF
FT                                sumoylation; when associated with G-346
FT                                and G-351.
FT   MUTAGEN     363    363       I->S: Loss of promotion of EKLF
FT                                sumoylation.
FT   MUTAGEN     372    372       W->A: Loss of promotion of NCOA2
FT                                sumoylation.
FT   MUTAGEN     375    376       PV->AA: Loss of promotion of EKLF
FT                                sumoylation.
FT   CONFLICT    320    320       P -> S (in Ref. 1; AAC36701).
SQ   SEQUENCE   651 AA;  71618 MW;  8844364E8FEE4F7F CRC64;
     MADSAELKQM VMSLRVSELQ VLLGYAGRNK HGRKHELLTK ALHLLKAGCS PAVQMKIKEL
     YRRRFPQKIM TPADLSIPNV HSSPMPPTLS PSTIPQLTYD GHPASSPLLP VSLLGPKHEL
     ELPHLTSALH PVHPDIKLQK LPFYDLLDEL IKPTSLASDN SQRFRETCFA FALTPQQVQQ
     ISSSMDISGT KCDFTVQVQL RFCLSETSCP QEDHFPPNLC VKVNTKPCSL PGYLPPTKNG
     VEPKRPSRPI NITSLVRLST TVPNTIVVSW TAEIGRTYSM AVYLVKQLSS TVLLQRLRAK
     GIRNPDHSRA LIKEKLTADP DSEIATTSLR VSLLCPLGKM RLTIPCRALT CSHLQCFDAT
     LYIQMNEKKP TWVCPVCDKK APYEHLIIDG LFMEILKYCT DCDEIQFKED GSWAPMRSKK
     EVQEVTASYN GVDGCLSSTL EHQVASHNQS SNKNKKVEVI DLTIDSSSDE EEEEPPAKRT
     CPSLSPTSPL SNKGILSLPH QASPVSRTPS LPAVDTSYIN TSLIQDYRHP FHMTPMPYDL
     QGLDFFPFLS GDNQHYNTSL LAAAAAAVSD DQDLLHSSRF FPYTSSQMFL DQLSAGGSTS
     LPATNGSSSG SNSSLVSSNS LRESHGHGVA SRSSADTASI FGIIPDIISL D
//
ID   MPP3_MOUSE              Reviewed;         568 AA.
AC   O88910;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=MAGUK p55 subfamily member 3;
DE   AltName: Full=Discs large homolog 3;
DE   AltName: Full=Protein MPP3;
GN   Name=Mpp3; Synonyms=Dlgh3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=99057599; PubMed=9838122; DOI=10.1016/S0167-4781(98)00209-7;
RA   Lin L., Peters L.L., Ciciotte S.L., Chishti A.H.;
RT   "cDNA sequence and chromosomal localization of mouse Dlgh3 gene
RT   adjacent to the BRCA1 tumor suppressor locus.";
RL   Biochim. Biophys. Acta 1443:211-216(1998).
RN   [2]
RP   INTERACTION WITH HTR2A.
RX   PubMed=14988405; DOI=10.1074/jbc.M312106200;
RA   Becamel C., Gavarini S., Chanrion B., Alonso G., Galeotti N.,
RA   Dumuis A., Bockaert J., Marin P.;
RT   "The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets
RT   of PDZ proteins.";
RL   J. Biol. Chem. 279:20257-20266(2004).
RN   [3]
RP   INTERACTION WITH HTR4.
RX   PubMed=15466885; DOI=10.1242/jcs.01379;
RA   Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W.,
RA   Marin P., Dumuis A., Bockaert J.;
RT   "New sorting nexin (SNX27) and NHERF specifically interact with the 5-
RT   HT4a receptor splice variant: roles in receptor targeting.";
RL   J. Cell Sci. 117:5367-5379(2004).
CC   -!- SUBUNIT: May interact with HTR2A. Interacts (via PDZ domain) with
CC       CADM1 (via C-terminus). Interacts with HTR4.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, skeletal muscle, testis,
CC       kidney, and lung.
CC   -!- SIMILARITY: Belongs to the MAGUK family.
CC   -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC   -!- SIMILARITY: Contains 2 L27 domains.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF079366; AAD12762.1; -; mRNA.
DR   IPI; IPI00351246; -.
DR   UniGene; Mm.20449; -.
DR   ProteinModelPortal; O88910; -.
DR   SMR; O88910; 5-118, 134-217, 229-566.
DR   STRING; O88910; -.
DR   PhosphoSite; O88910; -.
DR   PRIDE; O88910; -.
DR   Ensembl; ENSMUST00000062801; ENSMUSP00000055469; ENSMUSG00000052373.
DR   Ensembl; ENSMUST00000100400; ENSMUSP00000097969; ENSMUSG00000052373.
DR   Ensembl; ENSMUST00000107168; ENSMUSP00000102786; ENSMUSG00000052373.
DR   MGI; MGI:1328354; Mpp3.
DR   eggNOG; roNOG04141; -.
DR   HOVERGEN; HBG001858; -.
DR   InParanoid; O88910; -.
DR   OrthoDB; EOG4SQWW9; -.
DR   ArrayExpress; O88910; -.
DR   Bgee; O88910; -.
DR   Genevestigator; O88910; -.
DR   GermOnline; ENSMUSG00000052373; Mus musculus.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR004172; L27.
DR   InterPro; IPR014775; L27_C.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF02828; L27; 2.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00569; L27; 2.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS51022; L27; 2.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Repeat; SH3 domain.
FT   CHAIN         1    568       MAGUK p55 subfamily member 3.
FT                                /FTId=PRO_0000094576.
FT   DOMAIN        6     60       L27 1.
FT   DOMAIN       61    118       L27 2.
FT   DOMAIN      137    218       PDZ.
FT   DOMAIN      226    296       SH3.
FT   DOMAIN      385    568       Guanylate kinase-like.
SQ   SEQUENCE   568 AA;  64472 MW;  2AAF1635C00B09D9 CRC64;
     MPILSEDSGL HETLALLTSQ LRPDSNHREE MGFLRDVFSE KSLSYLMKIH EKLRYYERQS
     PTPVLHSAMA LAEDVMEELQ AASVHSDERE LLQLLSTPHL RAVLMVHDTV AQKNFDPVLP
     PLPDNIDEDF EEESVKIVRL VKNKEPLGAT IRRDEHSGAV VVARIMRGGA ADRSGLVHVG
     DELREVNGIA VLHKRPDEIS QILAQSQGSI TLKIIPATQE EDRFKDSKVF MRALFHYDPR
     EDRAIPCQEA GLPFQRRQVL EVVSQDDPTW WQAKRVGDTN LRAGLIPSKQ FQERRLSYRR
     TTGTLPSPQN FKKPPYDQPC DKETCDCDEY FKGHYVAGLR RSFRLGCRER LGGSQEAKVP
     TGAESQVLLT YEEVARYQHQ PGERPRLVVL IGSLGAHLHE LKQRVVAEDP QQFAVAVPHT
     TRPRKSHEID GVEYHFVSKQ AFEADVHHNR FLEHGEYKEN LYGTSLEAIQ AVMAKNKVCL
     VDVEPEALRH LRTPEFKPYV IFVKPAIQER RKTPPVSPDS EDIASSLDEQ QQEMAASAAF
     IDQHYGHLID TVLVRQDLQE PAASSELS
//
ID   SYN1_MOUSE              Reviewed;         706 AA.
AC   O88935; Q62279; Q8QZT8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   08-FEB-2011, entry version 98.
DE   RecName: Full=Synapsin-1;
DE   AltName: Full=Synapsin I;
GN   Name=Syn1; Synonyms=Syn-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IB).
RC   STRAIN=C57BL/6; TISSUE=Pancreatic islet;
RX   MEDLINE=99107854; PubMed=9890964; DOI=10.1074/jbc.274.4.2053;
RA   Matsumoto K., Ebihara K., Yamamoto H., Tabuchi H., Fukunaga K.,
RA   Yasunami M., Ohkubo H., Shichiri M., Miyamoto E.;
RT   "Cloning from insulinoma cells of synapsin I associated with insulin
RT   secretory granules.";
RL   J. Biol. Chem. 274:2053-2059(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125.
RX   MEDLINE=94308086; PubMed=8034599;
RA   Chin L.S., Li L., Greengard P.;
RT   "Neuron-specific expression of the synapsin II gene is directed by a
RT   specific core promoter and upstream regulatory elements.";
RL   J. Biol. Chem. 269:18507-18513(1994).
RN   [4]
RP   PROTEIN SEQUENCE OF 86-108; 115-128; 177-186; 257-269; 282-311;
RP   329-336; 414-420; 431-446 AND 566-576, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH PRNP.
RX   MEDLINE=21576182; PubMed=11571277; DOI=10.1074/jbc.M103289200;
RA   Spielhaupter C., Schaetzl H.M.;
RT   "PrPC directly interacts with proteins involved in signaling
RT   pathways.";
RL   J. Biol. Chem. 276:44604-44612(2001).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-510, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427 AND SER-568, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-87 AND THR-526, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452088; DOI=10.1074/mcp.T500040-MCP200;
RA   Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G.,
RA   Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F.,
RA   Maltby D.A., Schoepfer R., Burlingame A.L.;
RT   "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT   preparations using lectin weak affinity chromatography and mass
RT   spectrometry.";
RL   Mol. Cell. Proteomics 5:923-934(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-312, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-67; THR-337;
RP   SER-427; THR-512; SER-520; SER-553; SER-666 AND SER-705, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Neuronal phosphoprotein that coats synaptic vesicles,
CC       binds to the cytoskeleton, and is believed to function in the
CC       regulation of neurotransmitter release. Regulation of
CC       neurotransmitter release. The complex formed with NOS1 and CAPON
CC       proteins is necessary for specific nitric-oxide functions at a
CC       presynaptic level.
CC   -!- SUBUNIT: Homodimer. Interacts with CAPON. Forms a ternary complex
CC       with NOS1 (By similarity). Isoform Ib interacts with PRNP.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse. Golgi apparatus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=Ia;
CC         IsoId=O88935-2; Sequence=Displayed;
CC       Name=Ib;
CC         IsoId=O88935-1; Sequence=VSP_015206, VSP_015207;
CC       Name=3;
CC         IsoId=O88935-3; Sequence=VSP_015205;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Substrate of at least four different protein kinases. It is
CC       probable that phosphorylation plays a role in the regulation of
CC       synapsin-1 in the nerve terminal (By similarity).
CC   -!- SIMILARITY: Belongs to the synapsin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF085809; AAD09833.1; -; mRNA.
DR   EMBL; BC022954; AAH22954.1; -; mRNA.
DR   EMBL; L32025; AAA79963.1; -; Genomic_DNA.
DR   IPI; IPI00136372; -.
DR   IPI; IPI00649467; -.
DR   IPI; IPI00649886; -.
DR   PIR; A53692; A53692.
DR   RefSeq; NP_001104250.1; NM_001110780.1.
DR   RefSeq; NP_038708.3; NM_013680.4.
DR   UniGene; Mm.439844; -.
DR   ProteinModelPortal; O88935; -.
DR   SMR; O88935; 112-417.
DR   MINT; MINT-1531899; -.
DR   STRING; O88935; -.
DR   PhosphoSite; O88935; -.
DR   PRIDE; O88935; -.
DR   Ensembl; ENSMUST00000041344; ENSMUSP00000037545; ENSMUSG00000037217.
DR   Ensembl; ENSMUST00000081893; ENSMUSP00000080568; ENSMUSG00000037217.
DR   GeneID; 20964; -.
DR   KEGG; mmu:20964; -.
DR   UCSC; uc009stw.1; mouse.
DR   UCSC; uc009stx.1; mouse.
DR   CTD; 20964; -.
DR   MGI; MGI:98460; Syn1.
DR   GeneTree; ENSGT00530000063319; -.
DR   HOGENOM; HBG445598; -.
DR   HOVERGEN; HBG016354; -.
DR   InParanoid; O88935; -.
DR   OMA; QAGPVPR; -.
DR   NextBio; 299922; -.
DR   ArrayExpress; O88935; -.
DR   Bgee; O88935; -.
DR   CleanEx; MM_SYN1; -.
DR   Genevestigator; O88935; -.
DR   GermOnline; ENSMUSG00000037217; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048786; C:presynaptic active zone; IDA:MGI.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR   GO; GO:0000795; C:synaptonemal complex; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0046983; F:protein dimerization activity; TAS:MGI.
DR   GO; GO:0007269; P:neurotransmitter secretion; IGI:MGI.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR013817; Pre-ATP_grasp.
DR   InterPro; IPR016185; PreATP-grasp-like.
DR   InterPro; IPR001359; Synapsin.
DR   InterPro; IPR020898; Synapsin_ATP-bd_dom.
DR   InterPro; IPR019735; Synapsin_CS.
DR   InterPro; IPR019736; Synapsin_P_site.
DR   InterPro; IPR020897; Synapsin_pre-ATP-grasp_dom.
DR   Gene3D; G3DSA:3.30.1490.20; ATP_grasp_subdomain_1; 1.
DR   Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 2.
DR   Gene3D; G3DSA:3.40.50.20; Pre-ATP_grasp; 1.
DR   Pfam; PF02078; Synapsin; 1.
DR   Pfam; PF02750; Synapsin_C; 1.
DR   Pfam; PF10581; Synapsin_N; 1.
DR   PRINTS; PR01368; SYNAPSIN.
DR   SUPFAM; SSF52440; PreATP-grasp-like; 1.
DR   PROSITE; PS00415; SYNAPSIN_1; 1.
DR   PROSITE; PS00416; SYNAPSIN_2; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Cell junction;
KW   Direct protein sequencing; Glycoprotein; Golgi apparatus;
KW   Phosphoprotein; Repeat; Synapse.
FT   CHAIN         1    706       Synapsin-1.
FT                                /FTId=PRO_0000183019.
FT   REGION        1     28       A.
FT   REGION       29    112       B; linker.
FT   REGION      113    420       C; actin-binding and synaptic-vesicle
FT                                binding.
FT   REGION      421    657       D; Pro-rich linker.
FT   REGION      658    706       E.
FT   MOD_RES       9      9       Phosphoserine; by CaMK1 and PKA (By
FT                                similarity).
FT   MOD_RES      39     39       Phosphoserine (By similarity).
FT   MOD_RES      62     62       Phosphoserine.
FT   MOD_RES      67     67       Phosphoserine.
FT   MOD_RES     312    312       Phosphotyrosine.
FT   MOD_RES     337    337       Phosphothreonine.
FT   MOD_RES     427    427       Phosphoserine.
FT   MOD_RES     510    510       Phosphoserine.
FT   MOD_RES     512    512       Phosphothreonine.
FT   MOD_RES     520    520       Phosphoserine.
FT   MOD_RES     551    551       Phosphoserine (By similarity).
FT   MOD_RES     553    553       Phosphoserine.
FT   MOD_RES     568    568       Phosphoserine.
FT   MOD_RES     605    605       Phosphoserine; by CaMK2 (By similarity).
FT   MOD_RES     666    666       Phosphoserine.
FT   MOD_RES     705    705       Phosphoserine.
FT   CARBOHYD     55     55       O-linked (GlcNAc) (By similarity).
FT   CARBOHYD     56     56       O-linked (GlcNAc) (By similarity).
FT   CARBOHYD     87     87       O-linked (GlcNAc).
FT   CARBOHYD     96     96       O-linked (GlcNAc) (By similarity).
FT   CARBOHYD    103    103       O-linked (GlcNAc) (By similarity).
FT   CARBOHYD    261    261       O-linked (GlcNAc) (By similarity).
FT   CARBOHYD    432    432       O-linked (GlcNAc) (By similarity).
FT   CARBOHYD    518    518       O-linked (GlcNAc) (By similarity).
FT   CARBOHYD    526    526       O-linked (GlcNAc).
FT   CARBOHYD    564    564       O-linked (GlcNAc) (By similarity).
FT   CARBOHYD    578    578       O-linked (GlcNAc) (By similarity).
FT   VAR_SEQ     573    600       Missing (in isoform 3).
FT                                /FTId=VSP_015205.
FT   VAR_SEQ     662    670       NKSQSLTNA -> KASPSQAQP (in isoform Ib).
FT                                /FTId=VSP_015206.
FT   VAR_SEQ     671    706       Missing (in isoform Ib).
FT                                /FTId=VSP_015207.
FT   CONFLICT     44     44       P -> L (in Ref. 3; AAA79963).
SQ   SEQUENCE   706 AA;  74097 MW;  04C940E68547372B CRC64;
     MNYLRRRLSD SNFMANLPNG YMTDLQRPQP PPPPPSAASP GATPGSATAS AERASTAAPV
     ASPAAPSPGS SGGGGFFSSL SNAVKQTTAA AAATFSEQVG GGSGGAGRGG AAARVLLVID
     EPHTDWAKYF KGKKIHGEID IKVEQAEFSD LNLVAHANGG FSVDMEVLRN GVKVVRSLKP
     DFVLIRQHAF SMARNGDYRS LVIGLQYAGI PSVNSLHSVY NFCDKPWVFA QMVRLHKKLG
     TEEFPLIDQT FYPNHKEMLS STTYPVVVKM GHAHSGMGKV KVDNQHDFQD IASVVALTKT
     YATAEPFIDA KYDVRVQKIG QNYKAYMRTS VSGNWKTNTG SAMLEQIAMS DRYKLWVDTC
     SEIFGGLDIC AVEALHGKDG RDHIIEVVGS SMPLIGDHQD EDKQLIVELV VNKMTQALPR
     QPQRDASPGR GSHSQSSSPG ALTLGRQTSQ QPAGPPAQQR PPPQGGPPQP GPGPQRQGPP
     LQQRPPPQGQ QHLSGLGPPA GSPLPQRLPS PTAAPQQSAS QATPVTQGQG RQSRPVAGGP
     GAPPAARPPA SPSPQRQAGA PQATRQASIS GPAPTKASGA PPGGQQRQGP PQKPPGPAGP
     TRQASQAGPG PRTGPPTTQQ PRPSGPGPAG RPAKPQLAQK PSQDVPPPIT AAAGGPPHPQ
     LNKSQSLTNA FNLPEPAPPR PSLSQDEVKA ETIRSLRKSF ASLFSD
//
ID   LIN7B_MOUSE             Reviewed;         207 AA.
AC   O88951;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1999, sequence version 2.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Protein lin-7 homolog B;
DE            Short=Lin-7B;
DE   AltName: Full=Mammalian lin-seven protein 2;
DE            Short=MALS-2;
DE   AltName: Full=Vertebrate lin-7 homolog 2;
DE            Short=Veli-2;
GN   Name=Lin7b; Synonyms=Mals2, Veli2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH DLG2 AND DLG3.
RX   MEDLINE=98424246; PubMed=9753324; DOI=10.1016/S0092-8674(00)81736-5;
RA   Butz S., Okamoto M., Suedhof T.C.;
RT   "A tripartite protein complex with the potential to couple synaptic
RT   vesicle exocytosis to cell adhesion in brain.";
RL   Cell 94:773-782(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99274724; PubMed=10341223;
RA   Jo K., Derin R., Li M., Bredt D.S.;
RT   "Characterization of MALS/Velis-1, -2, and -3: a family of mammalian
RT   LIN-7 homologs enriched at brain synapses in association with the
RT   postsynaptic density-95/NMDA receptor postsynaptic complex.";
RL   J. Neurosci. 19:4189-4199(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=21607484; PubMed=11742811; DOI=10.1152/ajpcell.00249.2001;
RA   Olsen O., Liu H., Wade J.B., Merot J., Welling P.A.;
RT   "Basolateral membrane expression of the Kir 2.3 channel is coordinated
RT   by PDZ interaction with Lin-7/CASK complex.";
RL   Am. J. Physiol. 282:C183-C195(2002).
RN   [5]
RP   INTERACTION WITH ACCN3, AND FUNCTION.
RX   PubMed=15317815; DOI=10.1074/jbc.M405874200;
RA   Hruska-Hageman A.M., Benson C.J., Leonard A.S., Price M.P.,
RA   Welsh M.J.;
RT   "PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have
RT   opposite effects on H+- gated current.";
RL   J. Biol. Chem. 279:46962-46968(2004).
RN   [6]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15494546; DOI=10.1152/ajprenal.00235.2004;
RA   Olsen O., Wade J.B., Morin N., Bredt D.S., Welling P.A.;
RT   "Differential localization of the Mammalian Lin 7 (MALS/Veli) PDZ
RT   proteins in the kidney.";
RL   Am. J. Physiol. 288:F345-F352(2005).
RN   [7]
RP   STRUCTURE BY NMR OF 8-64, AND INTERACTION WITH CASK.
RX   PubMed=15863617; DOI=10.1073/pnas.0409346102;
RA   Feng W., Long J.-F., Zhang M.;
RT   "A unified assembly mode revealed by the structures of tetrameric L27
RT   domain complexes formed by mLin-2/mLin-7 and Patj/Pals1 scaffold
RT   proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:6861-6866(2005).
CC   -!- FUNCTION: Plays a role in establishing and maintaining the
CC       asymmetric distribution of channels and receptors at the plasma
CC       membrane of polarized cells. Forms membrane-associated
CC       multiprotein complexes that may regulate delivery and recycling of
CC       proteins to the correct membrane domains. The tripartite complex
CC       composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 may have
CC       the potential to couple synaptic vesicle exocytosis to cell
CC       adhesion in brain. Ensures the proper localization of GRIN2B
CC       (subunit 2B of the NMDA receptor) to neuronal postsynaptic density
CC       and may function in localizing synaptic vesicles at synapses where
CC       it is recruited by beta-catenin and cadherin. Required to localize
CC       Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2,
CC       ERBB3 and ERBB4 to the basolateral membrane of epithelial cells.
CC       May increase the amplitude of ACCN3 acid-evoked currents by
CC       stabilizing the channel at the cell surface.
CC   -!- SUBUNIT: Forms two exclusive ternary complexes with CASK and APBA1
CC       or CASKIN1. Can also interact with other modular proteins
CC       containing protein-protein interaction domains like MPP5, MPP6,
CC       MPP7, DLG1, DLG2 and DLG3 through its L27 domain. Interacts with
CC       DLG4 and GRIN2B as well as CDH1 and CTNNB1, the channels
CC       KCNJ12/Kir2.2, KCNJ4/Kir2.3 and probably KCNJ2/Kir2.1 and
CC       SLC6A12/BGT-1 via its PDZ domain. The association of LIN7A with
CC       cadherin and beta-catenin is calcium-dependent, occurs at synaptic
CC       junctions and requires the actin cytoskeleton. Interacts with
CC       EGFR, ERBB2, ERBB3 and ERBB4 with both PDZ and KID domains.
CC       Associates with KIF17 via APBA1. Interacts with ACCN3. Interacts
CC       with RTKN (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC       Basolateral cell membrane; Peripheral membrane protein. Cell
CC       junction. Cell junction, synapse, postsynaptic cell membrane,
CC       postsynaptic density; Peripheral membrane protein. Cell junction,
CC       tight junction. Cell junction, synapse, synaptosome. Note=Enriched
CC       in synaptosomes and at epithelial cell-cell junctions. Mainly
CC       basolateral in renal epithelial cells.
CC   -!- TISSUE SPECIFICITY: Expressed in the kidney; predominantly in the
CC       vasa recta.
CC   -!- DOMAIN: The kinase interacting site is required for proper
CC       delivery of ERBB2 to the basolateral membrane (By similarity).
CC   -!- DOMAIN: The PDZ domain regulates endocytosis and recycling of the
CC       receptor at the membrane (By similarity).
CC   -!- DOMAIN: The L27 domain mediates interaction with CASK and is
CC       involved in the formation of multimeric complexes and the
CC       association of LIN7 to membranes (By similarity).
CC   -!- SIMILARITY: Belongs to the lin-7 family.
CC   -!- SIMILARITY: Contains 1 L27 domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF087694; AAC78482.1; -; mRNA.
DR   EMBL; AF173082; AAD48501.1; -; mRNA.
DR   EMBL; BC031780; AAH31780.1; -; mRNA.
DR   IPI; IPI00136496; -.
DR   RefSeq; NP_035828.1; NM_011698.1.
DR   UniGene; Mm.20472; -.
DR   PDB; 1Y74; NMR; -; A/C=8-64.
DR   PDBsum; 1Y74; -.
DR   ProteinModelPortal; O88951; -.
DR   SMR; O88951; 8-64, 93-175.
DR   STRING; O88951; -.
DR   PRIDE; O88951; -.
DR   Ensembl; ENSMUST00000003971; ENSMUSP00000003971; ENSMUSG00000003872.
DR   GeneID; 22342; -.
DR   KEGG; mmu:22342; -.
DR   UCSC; uc009guv.1; mouse.
DR   CTD; 22342; -.
DR   MGI; MGI:1330858; Lin7b.
DR   eggNOG; maNOG18659; -.
DR   GeneTree; ENSGT00550000074582; -.
DR   HOGENOM; HBG315705; -.
DR   HOVERGEN; HBG052329; -.
DR   InParanoid; O88951; -.
DR   OMA; RQQHTSY; -.
DR   OrthoDB; EOG4BK556; -.
DR   NextBio; 302609; -.
DR   ArrayExpress; O88951; -.
DR   Bgee; O88951; -.
DR   CleanEx; MM_LIN7B; -.
DR   Genevestigator; O88951; -.
DR   GermOnline; ENSMUSG00000003872; Mus musculus.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019717; C:synaptosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0007269; P:neurotransmitter secretion; IGI:MGI.
DR   InterPro; IPR004172; L27.
DR   InterPro; IPR014775; L27_C.
DR   InterPro; IPR017365; Lin-7_homologue.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF02828; L27; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   PIRSF; PIRSF038039; Lin-7_homologue; 1.
DR   SMART; SM00569; L27; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS51022; L27; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell junction; Cell membrane; Exocytosis; Membrane;
KW   Postsynaptic cell membrane; Protein transport; Synapse; Synaptosome;
KW   Tight junction; Transport.
FT   CHAIN         1    207       Protein lin-7 homolog B.
FT                                /FTId=PRO_0000189627.
FT   DOMAIN       10     65       L27.
FT   DOMAIN       93    175       PDZ.
FT   MOTIF         1     13       Kinase interacting site (By similarity).
FT   HELIX        10     27
FT   HELIX        32     43
FT   HELIX        45     63
SQ   SEQUENCE   207 AA;  22914 MW;  BC6B6754B8C89F03 CRC64;
     MAALVEPLGL ERDVSRAVEL LERLQRSGEL PPQKLQALQR VLQSRFCSAI REVYEQLYDT
     LDITGSAEVR AHATAKATVA AFTASEGHAH PRVVELPKTD EGLGFNIMGG KEQNSPIYIS
     RVIPGGVADR HGGLKRGDQL LSVNGVSVEG EHHEKAVELL KAAQGSVKLV VRYTPRVLEE
     MEARFEKMRS ARRRQQHHSY TSLESRG
//
ID   LIN7C_MOUSE             Reviewed;         197 AA.
AC   O88952;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1999, sequence version 2.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Protein lin-7 homolog C;
DE            Short=Lin-7C;
DE            Short=mLin7C;
DE   AltName: Full=Mammalian lin-seven protein 3;
DE            Short=MALS-3;
DE   AltName: Full=Vertebrate lin-7 homolog 3;
DE            Short=Veli-3;
GN   Name=Lin7c; Synonyms=Mals3, Veli3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH DLG2 AND DLG3.
RC   TISSUE=Heart;
RX   MEDLINE=98424246; PubMed=9753324; DOI=10.1016/S0092-8674(00)81736-5;
RA   Butz S., Okamoto M., Suedhof T.C.;
RT   "A tripartite protein complex with the potential to couple synaptic
RT   vesicle exocytosis to cell adhesion in brain.";
RL   Cell 94:773-782(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99274724; PubMed=10341223;
RA   Jo K., Derin R., Li M., Bredt D.S.;
RT   "Characterization of MALS/Velis-1, -2, and -3: a family of mammalian
RT   LIN-7 homologs enriched at brain synapses in association with the
RT   postsynaptic density-95/NMDA receptor postsynaptic complex.";
RL   J. Neurosci. 19:4189-4199(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cecum, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 169-184, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH SLC6A12.
RX   MEDLINE=20178196; PubMed=10710551;
RA   Straight S.W., Karnak D., Borg J.-P., Kamberov E., Dare H.,
RA   Margolis B., Wade J.B.;
RT   "mLin-7 is localized to the basolateral surface of renal epithelia via
RT   its NH(2) terminus.";
RL   Am. J. Physiol. 278:F464-F475(2000).
RN   [7]
RP   INTERACTION WITH MPP5.
RX   MEDLINE=20219199; PubMed=10753959; DOI=10.1074/jbc.275.15.11425;
RA   Kamberov E., Makarova O., Roh M., Liu A., Karnak D., Straight S.,
RA   Margolis B.;
RT   "Molecular cloning and characterization of Pals, proteins associated
RT   with mLin-7.";
RL   J. Biol. Chem. 275:11425-11431(2000).
RN   [8]
RP   INTERACTION WITH HTR4.
RX   PubMed=15466885; DOI=10.1242/jcs.01379;
RA   Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W.,
RA   Marin P., Dumuis A., Bockaert J.;
RT   "New sorting nexin (SNX27) and NHERF specifically interact with the 5-
RT   HT4a receptor splice variant: roles in receptor targeting.";
RL   J. Cell Sci. 117:5367-5379(2004).
RN   [9]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15494546; DOI=10.1152/ajprenal.00235.2004;
RA   Olsen O., Wade J.B., Morin N., Bredt D.S., Welling P.A.;
RT   "Differential localization of the Mammalian Lin 7 (MALS/Veli) PDZ
RT   proteins in the kidney.";
RL   Am. J. Physiol. 288:F345-F352(2005).
CC   -!- FUNCTION: Plays a role in establishing and maintaining the
CC       asymmetric distribution of channels and receptors at the plasma
CC       membrane of polarized cells. Forms membrane-associated
CC       multiprotein complexes that may regulate delivery and recycling of
CC       proteins to the correct membrane domains. The tripartite complex
CC       composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 may have
CC       the potential to couple synaptic vesicle exocytosis to cell
CC       adhesion in brain. Ensures the proper localization of GRIN2B
CC       (subunit 2B of the NMDA receptor) to neuronal postsynaptic density
CC       and may function in localizing synaptic vesicles at synapses where
CC       it is recruited by beta-catenin and cadherin. Required to localize
CC       Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2,
CC       ERBB3 and ERBB4 to the basolateral membrane of epithelial cells.
CC   -!- SUBUNIT: Forms two exclusive ternary complexes with CASK and APBA1
CC       or CASKIN1 (By similarity). Can also interact with other modular
CC       proteins containing protein-protein interaction domains like MPP5,
CC       MPP6, MPP7, DLG1, DLG2 and DLG3 through its L27 domain. Interacts
CC       with DLG4 and GRIN2B as well as CDH1 and CTNNB1, the channels
CC       KCNJ12/Kir2.2, KCNJ4/Kir2.3 and probably KCNJ2/Kir2.1 and
CC       SLC6A12/BGT-1 via its PDZ domain. The association of LIN7A with
CC       cadherin and beta-catenin is calcium-dependent, occurs at synaptic
CC       junctions and requires the actin cytoskeleton. Interacts with
CC       EGFR, ERBB2, ERBB3 and ERBB4 with both PDZ and KID domains.
CC       Associates with KIF17 via APBA1. Interacts with HTR4. Forms a
CC       tripartite complex composed of DLG1, MPP7 and LIN7 (LIN7A or
CC       LIN7C) (By similarity).
CC   -!- INTERACTION:
CC       O95477:ABCA1 (xeno); NbExp=1; IntAct=EBI-821316, EBI-784112;
CC       Q08460:Kcnma1; NbExp=1; IntAct=EBI-821316, EBI-1633915;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC       Basolateral cell membrane; Peripheral membrane protein. Cell
CC       junction. Cell junction, synapse, postsynaptic cell membrane,
CC       postsynaptic density; Peripheral membrane protein. Cell junction,
CC       tight junction. Cell junction, synapse, synaptosome. Note=Enriched
CC       in synaptosomes and at epithelial cell-cell junctions. Mainly
CC       basolateral in renal epithelial cells.
CC   -!- TISSUE SPECIFICITY: Expressed in the kidney; particularly in the
CC       outer medullary collecting duct.
CC   -!- DOMAIN: The kinase interacting site is required for proper
CC       delivery of ERBB2 to the basolateral membrane (By similarity).
CC   -!- DOMAIN: The PDZ domain regulates endocytosis and recycling of the
CC       receptor at the membrane (By similarity).
CC   -!- DOMAIN: The L27 domain mediates interaction with CASK and is
CC       involved in the formation of multimeric complexes and the
CC       association of LIN7 to membranes.
CC   -!- SIMILARITY: Belongs to the lin-7 family.
CC   -!- SIMILARITY: Contains 1 L27 domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF087695; AAC78483.1; -; mRNA.
DR   EMBL; AF173083; AAD48502.1; -; mRNA.
DR   EMBL; AK015399; BAB29830.1; -; mRNA.
DR   EMBL; AK078923; BAC37462.1; -; mRNA.
DR   EMBL; BC046966; AAH46966.1; -; mRNA.
DR   IPI; IPI00136498; -.
DR   RefSeq; NP_035829.1; NM_011699.3.
DR   UniGene; Mm.235300; -.
DR   UniGene; Mm.478053; -.
DR   ProteinModelPortal; O88952; -.
DR   SMR; O88952; 3-64, 93-175.
DR   IntAct; O88952; 6.
DR   STRING; O88952; -.
DR   PRIDE; O88952; -.
DR   Ensembl; ENSMUST00000028583; ENSMUSP00000028583; ENSMUSG00000027162.
DR   GeneID; 22343; -.
DR   KEGG; mmu:22343; -.
DR   UCSC; uc008lmp.1; mouse.
DR   CTD; 22343; -.
DR   MGI; MGI:1330839; Lin7c.
DR   HOGENOM; HBG315705; -.
DR   HOVERGEN; HBG052329; -.
DR   InParanoid; O88952; -.
DR   OMA; VDINSSP; -.
DR   OrthoDB; EOG4J1198; -.
DR   PhylomeDB; O88952; -.
DR   NextBio; 302613; -.
DR   ArrayExpress; O88952; -.
DR   Bgee; O88952; -.
DR   CleanEx; MM_LIN7C; -.
DR   Genevestigator; O88952; -.
DR   GermOnline; ENSMUSG00000027162; Mus musculus.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
DR   GO; GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0007269; P:neurotransmitter secretion; IGI:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR004172; L27.
DR   InterPro; IPR014775; L27_C.
DR   InterPro; IPR017365; Lin-7_homologue.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF02828; L27; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   PIRSF; PIRSF038039; Lin-7_homologue; 1.
DR   SMART; SM00569; L27; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS51022; L27; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell junction; Cell membrane; Direct protein sequencing;
KW   Exocytosis; Membrane; Postsynaptic cell membrane; Protein transport;
KW   Synapse; Synaptosome; Tight junction; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    197       Protein lin-7 homolog C.
FT                                /FTId=PRO_0000189630.
FT   DOMAIN       10     65       L27.
FT   DOMAIN       93    175       PDZ.
FT   MOTIF         2     13       Kinase interacting site (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
SQ   SEQUENCE   197 AA;  21834 MW;  7410FBFA3BD24F45 CRC64;
     MAALGEPVRL ERDICRAIEL LEKLQRSGEV PPQKLQALQR VLQSEFCNAV REVYEHVYET
     VDISSSPEVR ANATAKATVA AFAASEGHSH PRVVELPKTE EGLGFNIMGG KEQNSPIYIS
     RIIPGGIADR HGGLKRGDQL LSVNGVSVEG EHHEKAVELL KAAQGKVKLV VRYTPKVLEE
     MESRFEKMRS AKRRQQT
//
ID   ACTN3_MOUSE             Reviewed;         900 AA.
AC   O88990; Q14DS8;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Alpha-actinin-3;
DE   AltName: Full=Alpha-actinin skeletal muscle isoform 3;
DE   AltName: Full=F-actin cross-linking protein;
GN   Name=Actn3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
RA   Birkenmeier C.S., Gifford E.J., Barker J.E.;
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: F-actin cross-linking protein which is thought to anchor
CC       actin to a variety of intracellular structures. This is a bundling
CC       protein (By similarity).
CC   -!- SUBUNIT: Homodimer; antiparallel. Also forms heterodimers with
CC       ACTN2. Interacts with MYOZ1 (By similarity).
CC   -!- SIMILARITY: Belongs to the alpha-actinin family.
CC   -!- SIMILARITY: Contains 1 actin-binding domain.
CC   -!- SIMILARITY: Contains 2 CH (calponin-homology) domains.
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
CC   -!- SIMILARITY: Contains 4 spectrin repeats.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AF093775; AAC62512.1; -; mRNA.
DR   EMBL; BC111890; AAI11891.1; -; mRNA.
DR   IPI; IPI00136701; -.
DR   RefSeq; NP_038484.1; NM_013456.1.
DR   UniGene; Mm.5316; -.
DR   ProteinModelPortal; O88990; -.
DR   SMR; O88990; 41-267, 280-752, 754-900.
DR   STRING; O88990; -.
DR   PhosphoSite; O88990; -.
DR   PRIDE; O88990; -.
DR   Ensembl; ENSMUST00000006626; ENSMUSP00000006626; ENSMUSG00000006457.
DR   GeneID; 11474; -.
DR   KEGG; mmu:11474; -.
DR   UCSC; uc008gbf.1; mouse.
DR   CTD; 11474; -.
DR   MGI; MGI:99678; Actn3.
DR   eggNOG; roNOG11088; -.
DR   HOGENOM; HBG314462; -.
DR   HOVERGEN; HBG050453; -.
DR   InParanoid; O88990; -.
DR   OMA; ASVNSRC; -.
DR   OrthoDB; EOG44F68D; -.
DR   PhylomeDB; O88990; -.
DR   NextBio; 278812; -.
DR   ArrayExpress; O88990; -.
DR   Bgee; O88990; -.
DR   CleanEx; MM_ACTN3; -.
DR   Genevestigator; O88990; -.
DR   GermOnline; ENSMUSG00000006457; Mus musculus.
DR   GO; GO:0005865; C:striated muscle thin filament; TAS:MGI.
DR   GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0030674; F:protein binding, bridging; TAS:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; TAS:UniProtKB.
DR   GO; GO:0006936; P:muscle contraction; IPI:MGI.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR014837; EF-hand_Ca_insen.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 2.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF08726; efhand_Ca_insen; 1.
DR   Pfam; PF00435; Spectrin; 4.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM00150; SPEC; 2.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   2: Evidence at transcript level;
KW   Actin-binding; Calcium; Repeat.
FT   CHAIN         1    900       Alpha-actinin-3.
FT                                /FTId=PRO_0000073439.
FT   DOMAIN        1    260       Actin-binding.
FT   DOMAIN       44    148       CH 1.
FT   DOMAIN      157    260       CH 2.
FT   REPEAT      287    397       Spectrin 1.
FT   REPEAT      407    512       Spectrin 2.
FT   REPEAT      522    633       Spectrin 3.
FT   REPEAT      643    746       Spectrin 4.
FT   DOMAIN      759    794       EF-hand 1.
FT   DOMAIN      795    830       EF-hand 2.
FT   CA_BIND     772    783       1; possibly ancestral.
FT   CA_BIND     808    819       2; possibly ancestral.
SQ   SEQUENCE   900 AA;  103043 MW;  7F795002CB2B7F8B CRC64;
     MMMVMQPEGL GAGEGPFSGG GGGEYMEQEE DWDRDLLLDP AWEKQQRKTF TAWCNSHLRK
     AGTQIENIEE DFRNGLKLML LLEVISGERL PRPDKGKMRF HKIANVNKAL DFIASKGVKL
     VSIGAEEIVD GNLKMTLGMI WTIILRFAIQ DISVEETSAK EGLLLWCQRK TAPYRNVNVQ
     NFHTSWKDGL ALCALIHRHR PDLIDYAKLR KDDPIGNLNT AFEVAEKYLD IPKMLDAEDI
     VNTPKPDEKA IMTYVSCFYH AFAGAEQAET AANRICKVLA VNQENEKLME EYEKLASELL
     EWIRRTVPWL ENRVGEPSMS AMQRKLEDFR DYRRLHKPPR VQEKCQLEIN FNTLQTKLRL
     SHRPAFMPSE GKLVSDIANA WRGLEQVEKG YEDWLLSEIR RLQRLQHLAE KFQQKASLHE
     AWTRGKEEML NQHDYESASL QEVRALLRRH EAFESDLAAH QDRVEHIAAL AQELNELDYH
     EAASVNSRCQ AICDQWDNLG TLTQKRRDAL ERMEKLLETI DQLQLEFARR AAPFNNWLDG
     AIEDLQDVWL VHSVEETQSL LTAHEQFKAT LPEADRERGA ILGIQGEIQK ICQTYGLRPK
     SGNPYITLSS QDINNKWDTV RKLVPSRDQT LQEELARQQV NERLRRQFAA QANAIGPWIQ
     GKVEEVGRLA AGLAGSLEEQ MAGLRQQEQN IINYKSNIDR LEGDHQLLQE SLVFDNKHTV
     YSMEHIRVGW EQLLTSIART INEVENQVLT RDAKGLSQEQ LNEFRASFNH FDRKRNGMME
     PDDFRACLIS MGYDLGEVEF ARIMTMVDPN AAGVVTFQAF IDFMTRETAE TDTAEQVVAS
     FKILAGDKNY ITPEELRREL PAEQAEYCIR RMAPYKGSGA PSGALDYVAF SSALYGESDL
//
ID   CBPD_MOUSE              Reviewed;        1377 AA.
AC   O89001;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Carboxypeptidase D;
DE            EC=3.4.17.22;
DE   AltName: Full=Metallocarboxypeptidase D;
DE   AltName: Full=gp180;
DE   Flags: Precursor;
GN   Name=Cpd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=98382529; PubMed=9714835; DOI=10.1016/S0378-1119(98)00270-4;
RA   Ishikawa T., Murakami K., Kido Y., Ohnishi S., Yazaki Y., Harada F.,
RA   Kuroki K.;
RT   "Cloning, functional expression, and chromosomal localization of the
RT   human and mouse gp180-carboxypeptidase D-like enzyme.";
RL   Gene 215:361-370(1998).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1365 AND THR-1367, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-398; ASN-409 AND ASN-521,
RP   AND MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- CATALYTIC ACTIVITY: Releases C-terminal Arg and Lys from
CC       polypeptides.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- DOMAIN: There are 3 carboxypeptidase-like domains. Only the first
CC       two domains seem to have kept a catalytic activity.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; D85391; BAA33371.1; -; mRNA.
DR   IPI; IPI00130573; -.
DR   UniGene; Mm.276736; -.
DR   ProteinModelPortal; O89001; -.
DR   SMR; O89001; 12-461, 493-872, 922-1286.
DR   STRING; O89001; -.
DR   MEROPS; M14.016; -.
DR   PhosphoSite; O89001; -.
DR   PRIDE; O89001; -.
DR   Ensembl; ENSMUST00000021201; ENSMUSP00000021201; ENSMUSG00000020841.
DR   MGI; MGI:107265; Cpd.
DR   eggNOG; roNOG06219; -.
DR   HOGENOM; HBG444298; -.
DR   HOVERGEN; HBG006932; -.
DR   InParanoid; O89001; -.
DR   OrthoDB; EOG44J2H6; -.
DR   BRENDA; 3.4.17.22; 244.
DR   ArrayExpress; O89001; -.
DR   Bgee; O89001; -.
DR   CleanEx; MM_CPD; -.
DR   Genevestigator; O89001; -.
DR   GermOnline; ENSMUSG00000020841; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR014766; CarboxyPept_regulatory_dom.
DR   InterPro; IPR015567; Pept_M14B_carboxypept_D2.
DR   InterPro; IPR000834; Peptidase_M14.
DR   Gene3D; G3DSA:2.60.40.1120; CarboxyPept_regulatory; 3.
DR   PANTHER; PTHR11532:SF8; C_peptidase_D; 1.
DR   Pfam; PF00246; Peptidase_M14; 3.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 3.
DR   SUPFAM; SSF49464; CarboxypepD_reg; 3.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; 2.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; 2.
PE   1: Evidence at protein level;
KW   Carboxypeptidase; Glycoprotein; Hydrolase; Lipoprotein; Membrane;
KW   Metal-binding; Metalloprotease; Palmitate; Phosphoprotein; Protease;
KW   Repeat; Signal; Transmembrane; Transmembrane helix; Zinc.
FT   SIGNAL        1     37       Potential.
FT   CHAIN        38   1377       Carboxypeptidase D.
FT                                /FTId=PRO_0000004402.
FT   TOPO_DOM     38   1296       Extracellular (Potential).
FT   TRANSMEM   1297   1317       Helical; (Potential).
FT   TOPO_DOM   1318   1377       Cytoplasmic (Potential).
FT   REGION       38    492       Carboxypeptidase-like 1.
FT   REGION      493    896       Carboxypeptidase-like 2.
FT   REGION      897   1296       Carboxypeptidase-like 3.
FT   MOTIF       161    163       Cell attachment site (Potential).
FT   ACT_SITE    349    349       Nucleophile 1 (By similarity).
FT   ACT_SITE    761    761       Nucleophile 2 (By similarity).
FT   METAL       138    138       Zinc 1 (By similarity).
FT   METAL       141    141       Zinc 1 (By similarity).
FT   METAL       256    256       Zinc 1 (By similarity).
FT   METAL       563    563       Zinc 2 (By similarity).
FT   METAL       566    566       Zinc 2 (By similarity).
FT   METAL       670    670       Zinc 2 (By similarity).
FT   MOD_RES    1341   1341       Phosphotyrosine (By similarity).
FT   MOD_RES    1355   1355       Phosphoserine (By similarity).
FT   MOD_RES    1358   1358       Phosphoserine (By similarity).
FT   MOD_RES    1365   1365       Phosphothreonine.
FT   MOD_RES    1367   1367       Phosphothreonine.
FT   MOD_RES    1373   1373       Phosphotyrosine (By similarity).
FT   LIPID      1314   1314       S-palmitoyl cysteine (By similarity).
FT   LIPID      1318   1318       S-palmitoyl cysteine (By similarity).
FT   LIPID      1320   1320       S-palmitoyl cysteine (By similarity).
FT   CARBOHYD    171    171       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    216    216       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    398    398       N-linked (GlcNAc...).
FT   CARBOHYD    409    409       N-linked (GlcNAc...).
FT   CARBOHYD    428    428       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    521    521       N-linked (GlcNAc...).
FT   CARBOHYD    625    625       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    810    810       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    854    854       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    866    866       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    878    878       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    952    952       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    975    975       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1067   1067       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1139   1139       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   1377 AA;  152306 MW;  77802F74267DE40F CRC64;
     MASGRDERPP WRLGRLRLLP PPPLLLLLLL LRSSAQAAHI KKAEATTTTV GGTEAAEGQF
     DHYYHEAALG EALEAAAAAG PPGLARLFSI GSSVEGRPLW VLRLTAGLGP PPTAAAGLDA
     AGPLLPGRPQ VKLVGNMHGD ETVSRQVLVY LARELASGYR RGDPRLVRLL NTTDVYLLPS
     LNPDGFERAR EGDCGLGDSG PPGTSGRDNS RGRDLNRSFP DQFSTGEPPS LDEVPEVRAL
     IDWIRRNKFV LSGNLHGGSV VASYPFDDSP EHKTTGLYSK TSDDEVFRYL AKAYASNHPI
     MKTGEPHCPG DEDETFKDGI TNGAHWYDVE GGMQDYNYVW ANCFEITLEL SCCKYPPASQ
     LRQEWENNRE SLITLIEKVH IGIKGFVKDS VTGSGLENAT ISVAGINHNI TTGRFGDFHR
     LLVPGTYNLT ALSTGYMPLT INNIMVKEGP ATEMDFSLRP TVMSVMPGST EAVTTPGTVA
     VPNIPPGTPS SHQPIQPKDF HHHHFPDMEI FLRRFANEYP NITRLYSLGK SVESRELYVM
     EISDNPGVHE PGEPEFKYIG NMHGNEVVGR ELLLNLIEYL CKNFGTDPEV TDLVRSTRIH
     LMPSMNPDGY EKSQEGDSIS VVGRNNSNNF DLNRNFPDQF VPITEPTQPE TIAVMSWVKA
     YPFVLSANLH GGSLVVNYPY DDNEQGVATY SKSPDDAVFQ QIALSYSKEN SQMFQGRPCK
     DMYLNEYFPH GITNGASWYN VPGGMQDWNY LQTNCFEVTI ELGCVKYPFE NELPKYWEQN
     RRSLIQFMKQ VHQGVKGFVL DATDGRGILN ATLSVAEINH PVTTYKAGDY WRLLVPGTYK
     ITASARGYNP VTKNVTVRSE GAVQVNFTLV RSSADANNES KKGRGHSTST DDTSDPTSKE
     FEALIKHLSA ENGLEGFMLS SSSDLALYRY HSYKDLSEFL RGLVMNYPHI TNLTTLGQSV
     EYRHIWSLEI SNKPNISEPE EPKIRFVAGI HGNAPVGTEL LLALAEFLCL NYKRNPVVTQ
     LVDRTRIVIV PSLNPDGRDG AQEKDCTSKT GHTNAHGKDL DTDFTSNASQ PETKAIIENL
     IQKQDFSLSI ALDGGSVLVT YPYDKPVQTV ENKETLKHLA SLYANNHPSM HMGQPSCPNN
     SDENIPGGVM RGAEWHSHLG SMKDYSVTYG HCPEITVYTS CCYFPSAAQL PALWAENKKS
     LLSMLVEVHK GVHGLVKDKA GKPISKAVIV LNEGIKVYTK EGGYFHVLLA PGVHNINAIA
     DGYQQQHTQV FVHHDAASSV VIVFDTDNRI FGLPRELVVT VSGATMSALI LTACIIWCIC
     SIKSNRHKDG FHRLRQHHDE YEDEIRMMST GSKKSLLSHE FQDETDTEEE TLYSSKH
//
ID   ROBO1_MOUSE             Reviewed;        1612 AA.
AC   O89026;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Roundabout homolog 1;
DE   Flags: Precursor;
GN   Name=Robo1; Synonyms=Dutt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Wu M.C., Lowe N., Fordham R., Rabbitts P.;
RT   "The mouse homologue of human DUTT1/H-robo1 gene: protein sequence and
RT   chromosomal location.";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   POSSIBLE FUNCTION, AND DISRUPTION PHENOTYPE.
RX   MEDLINE=21625015; PubMed=11734623; DOI=10.1073/pnas.251407098;
RA   Xian J., Clark K.J., Fordham R., Pannell R., Rabbitts T.H.,
RA   Rabbitts P.H.;
RT   "Inadequate lung development and bronchial hyperplasia in mice with a
RT   targeted deletion in the Dutt1/Robo1 gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:15062-15066(2001).
RN   [3]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15091338; DOI=10.1016/S0896-6273(04)00179-5;
RA   Long H., Sabatier C., Ma L., Plump A., Yuan W., Ornitz D.M.,
RA   Tamada A., Murakami F., Goodman C.S., Tessier-Lavigne M.;
RT   "Conserved roles for slit and robo proteins in midline commissural
RT   axon guidance.";
RL   Neuron 42:213-223(2004).
RN   [4]
RP   DEVELOPMENTAL STAGE.
RX   MEDLINE=98271458; PubMed=9608531; DOI=10.1006/mcne.1998.0672;
RA   Sundaresan V., Roberts I., Bateman A., Bankier A., Sheppard M.,
RA   Hobbs C., Xiong J., Minna J., Latif F., Lerman M., Rabbitts P.;
RT   "The DUTT1 gene, a novel NCAM family member is expressed in developing
RT   murine neural tissues and has an unusually broad pattern of
RT   expression.";
RL   Mol. Cell. Neurosci. 11:29-35(1998).
RN   [5]
RP   INTERACTION WITH SLIT1.
RX   MEDLINE=99365246; PubMed=10433822; DOI=10.1006/dbio.1999.9371;
RA   Yuan W., Zhou L., Chen J.H., Wu J.Y., Rao Y., Ornitz D.M.;
RT   "The mouse SLIT family: secreted ligands for ROBO expressed in
RT   patterns that suggest a role in morphogenesis and axon guidance.";
RL   Dev. Biol. 212:290-306(1999).
RN   [6]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=22119661; PubMed=12123796; DOI=10.1016/S0014-5793(02)02904-6;
RA   Clark K., Hammond E., Rabbitts P.;
RT   "Temporal and spatial expression of two isoforms of the Dutt1/Robo1
RT   gene in mouse development.";
RL   FEBS Lett. 523:12-16(2002).
RN   [7]
RP   UBIQUITINATION, AND INTERACTION WITH USP33.
RX   PubMed=19684588; DOI=10.1038/nn.2382;
RA   Yuasa-Kawada J., Kinoshita-Kawada M., Wu G., Rao Y., Wu J.Y.;
RT   "Midline crossing and Slit responsiveness of commissural axons require
RT   USP33.";
RL   Nat. Neurosci. 12:1087-1089(2009).
RN   [8]
RP   INTERACTION WITH USP33.
RX   PubMed=19706539; DOI=10.1073/pnas.0801262106;
RA   Yuasa-Kawada J., Kinoshita-Kawada M., Rao Y., Wu J.Y.;
RT   "Deubiquitinating enzyme USP33/VDU1 is required for Slit signaling in
RT   inhibiting breast cancer cell migration.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:14530-14535(2009).
CC   -!- FUNCTION: Receptor for SLIT1 and SLIT2 which are thought to act as
CC       molecular guidance cue in cellular migration, including axonal
CC       navigation at the ventral midline of the neural tube and
CC       projection of axons to different regions during neuronal
CC       development. In axon growth cones, the silencing of the attractive
CC       effect of NTN1 by SLIT2 may require the formation of a ROBO1-DCC
CC       complex (By similarity). May be required for lung development.
CC   -!- SUBUNIT: Interacts with SLIT1 and SLIT2.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- TISSUE SPECIFICITY: Expressed in embryonal spinal chord. Expressed
CC       in embryonal lung, and in adult lung bronchial epithelial cells of
CC       large proximal airways.
CC   -!- DEVELOPMENTAL STAGE: Earliest and highest expression at 11 dpc.
CC       Expression is detected in developing somits, brain, neural tube,
CC       and pericardiac mesenchyme. By in situ hybridization is detected
CC       in marginal zones bordering the mitotically active periventricular
CC       region, weakly extending to the ventral aspect impinging on motor
CC       neuron columns. Also detected in the ventral third of the
CC       developing neural tube, and in spinal chord throughout the full
CC       length of the neural tube. Also detected at 17.5 dpc in lung
CC       mesenchyme. Expressed at E11.5 in spinal chord, predominantly
CC       localized to postcrossing commissural axons.
CC   -!- PTM: Ubiquitinated. May be deubiquitinated by USP33.
CC   -!- DISRUPTION PHENOTYPE: Mice show defects in commissural axon
CC       guidance in spinal chord including midline recrossing and an
CC       altered lateral and ventral funiculi projection. The phenotype
CC       resembles that of a SLIT1;SLIT2;SLIT3 triple mutant. They also
CC       mimick a naturally occurring human homozygous deletion mutant
CC       detected in a small lung cancer cell line, frequently die at birth
CC       by respiratory failure with accompanying abnormal lung histology.
CC       Surviving mice develop bronchial hyperplasia.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ROBO
CC       family.
CC   -!- SIMILARITY: Contains 3 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 5 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Y17793; CAA76850.1; -; mRNA.
DR   IPI; IPI00130664; -.
DR   PIR; T30805; T30805.
DR   RefSeq; NP_062286.2; NM_019413.2.
DR   UniGene; Mm.310772; -.
DR   ProteinModelPortal; O89026; -.
DR   SMR; O89026; 4-834.
DR   STRING; O89026; -.
DR   PhosphoSite; O89026; -.
DR   PRIDE; O89026; -.
DR   Ensembl; ENSMUST00000023600; ENSMUSP00000023600; ENSMUSG00000022883.
DR   GeneID; 19876; -.
DR   KEGG; mmu:19876; -.
DR   UCSC; uc007zrb.1; mouse.
DR   CTD; 19876; -.
DR   MGI; MGI:1274781; Robo1.
DR   eggNOG; roNOG09567; -.
DR   HOGENOM; HBG506614; -.
DR   HOVERGEN; HBG073476; -.
DR   InParanoid; O89026; -.
DR   OrthoDB; EOG44QT01; -.
DR   ArrayExpress; O89026; -.
DR   Bgee; O89026; -.
DR   CleanEx; MM_ROBO1; -.
DR   Genevestigator; O89026; -.
DR   GO; GO:0030673; C:axolemma; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
DR   GO; GO:0016199; P:axon midline choice point recognition; IGI:UniProtKB.
DR   GO; GO:0060763; P:mammary duct terminal end bud growth; IMP:MGI.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR003596; Ig_V-set_sub.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 9.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF07679; I-set; 5.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00408; IGc2; 4.
DR   SMART; SM00406; IGv; 1.
DR   SUPFAM; SSF49265; FN_III-like; 3.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS50835; IG_LIKE; 5.
PE   1: Evidence at protein level;
KW   Chemotaxis; Developmental protein; Differentiation; Disulfide bond;
KW   Glycoprotein; Immunoglobulin domain; Membrane; Neurogenesis;
KW   Phosphoprotein; Receptor; Repeat; Signal; Transmembrane;
KW   Transmembrane helix; Ubl conjugation.
FT   SIGNAL        1     19       Potential.
FT   CHAIN        20   1612       Roundabout homolog 1.
FT                                /FTId=PRO_0000031034.
FT   TOPO_DOM     20    858       Extracellular (Potential).
FT   TRANSMEM    859    879       Helical; (Potential).
FT   TOPO_DOM    880   1612       Cytoplasmic (Potential).
FT   DOMAIN       29    125       Ig-like C2-type 1.
FT   DOMAIN      131    218       Ig-like C2-type 2.
FT   DOMAIN      223    307       Ig-like C2-type 3.
FT   DOMAIN      312    407       Ig-like C2-type 4.
FT   DOMAIN      416    502       Ig-like C2-type 5.
FT   DOMAIN      522    607       Fibronectin type-III 1.
FT   DOMAIN      634    724       Fibronectin type-III 2.
FT   DOMAIN      736    825       Fibronectin type-III 3.
FT   MOD_RES     901    901       Phosphoserine (By similarity).
FT   MOD_RES    1016   1016       Phosphoserine (By similarity).
FT   MOD_RES    1201   1201       Phosphothreonine (By similarity).
FT   CARBOHYD    121    121       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    424    424       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    751    751       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    781    781       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    788    788       N-linked (GlcNAc...) (Potential).
FT   DISULFID     50    108       Potential.
FT   DISULFID    152    201       Potential.
FT   DISULFID    244    291       Potential.
FT   DISULFID    333    389       Potential.
FT   DISULFID    437    486       Potential.
SQ   SEQUENCE   1612 AA;  176407 MW;  5F2988C544796B4B CRC64;
     MIAEPAHFYL FGLICLCSGS RLRQEDFPPR IVEHPSDLIV SKGEPATLNC KAEGRPTPTI
     EWYKGGERVE TDKDDPRSHR MLLPSGSLFF LRIVHGRKSR PDEGVYICVA RNYLGEAVSH
     NASLEVAILR DDFRQNPSDV MVAVGEPAVM ECQPPRGHPE PTISWKKDGS PLDDKDERIT
     IRGGKLMITY TRKSDAGKYV CVGTNMVGER ESEVAELTVL ERPSFVKRPS NLAVTVDDSA
     EFKCEARGDP VPTVRWRKDD GELPKSRYEI RDDHTLKIRK VTAGDMGSYT CVAENMVGKA
     EASATLTVQE PPHFVVKPRD QVVALGRTVT FQCEATGNPQ PAIFWRREGS QNLLFSYQPP
     QSSSRFSVSQ TGDLTITNVQ RSDVGYYICQ TLNVAGSIIT KAYLEVTDVI ADRPPPVIRQ
     GPVNQTVAVD GTLILSCVAT GSPAPTILWR KDGVLVSTQD SRIKQLESGV LQIRYAKLGD
     TGRYTCTAST PSGEATWSAY IEVQEFGVPV QPPRPTDPNL IPSAPSKPEV TDVSKNTVTL
     SWQPNLNSGA TPTSYIIEAF SHASGSSWQT AAENVKTETF AIKGLKPNAI YLFLVRAANA
     YGISDPSQIS DPVKTQDVPP TSQGVDHKQV QRELGNVVLH LHNPTILSSS SVEVHWTVDQ
     QSQYIQGYKI LYRPSGASHG ESEWLVFEVR TPTKNSVVIP DLRKGVNYEI KARPFFNEFQ
     GADSEIKFAK TLEEAPSAPP RSVTVSKNDG NGTAILVTWQ PPPEDTQNGM VQEYKVWCLG
     NETKYHINKT VDGSTFSVVI PSLVPGIRYS VEVAASTGAG PGVKSEPQFI QLDSHGNPVS
     PEDQVSLAQQ ISDVVRQPAF IAGIGAACWI ILMVFSIWLY RHRKKRNGLT STYAGIRKVP
     SFTFTPTVTY QRGGEAVSSG GRPGLLNISE PATQPWLADT WPNTGNNHND CSINCCTAGN
     GNSDSNLTTY SRPADCIANY NNQLDNKQTN LMLPESTVYG DVDLSNKINE MKTFNSPNLK
     DGRFVNPSGQ PTPYATTQLI QANLSNNMNN GAGDSSEKHW KPPGQQKPEV APIQYNIMEQ
     NKLNKDYRAN DTIPPTIPYN QSYDQNTGGS YNSSDRGSST SGSQGHKKGA RTPKAPKQGG
     MNWADLLPPP PAHPPPHSNS EEYNMSVDES YDQEMPCPVP PAPMYLQQDE LQEEEDERGP
     TPPVRGAASS PAAVSYSHQS TATLTPSPQE ELQPMLQDCP EDLGHMPHPP DRRRQPVSPP
     PPPRPISPPH TYGYISGPLV SDMDTDAPEE EEDEADMEVA KMQTRRLLLR GLEQTPASSV
     GDLESSVTGS MINGWGSASE EDNISSGRSS VSSSDGSFFT DADFAQAVAA AAEYAGLKVA
     RRQMQDAAGR RHFHASQCPR PTSPVSTDSN MSAVVIQKAR PAKKQKHQPG HLRREAYADD
     LPPPPVPPPA IKSPTVQSKA QLEVRPVMVP KLASIEARTD RSSDRKGGSY KGREALDGRQ
     VTDLRTNPSD PREAQEQPND GKGRGTRQPK RDLPPAKTHL GQEDILPYCR PTFPTSNNPR
     DPSSSSSMSS RGSGSRQREQ ANVGRRNMAE MQVLGGFERG DENNEELEET ES
//
ID   SPD2A_MOUSE             Reviewed;        1124 AA.
AC   O89032; Q148Q8;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=SH3 and PX domain-containing protein 2A;
DE   AltName: Full=Five SH3 domain-containing protein;
DE   AltName: Full=SH3 multiple domains protein 1;
DE   AltName: Full=Tyrosine kinase substrate with five SH3 domains;
GN   Name=Sh3pxd2a; Synonyms=Fish, Sh3md1, Tks5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM
RP   3), PTM, AND TISSUE SPECIFICITY.
RX   MEDLINE=98353460; PubMed=9687503; DOI=10.1093/emboj/17.15.4346;
RA   Lock P., Abram C.L., Gibson T., Courtneidge S.A.;
RT   "A new method for isolating tyrosine kinase substrates used to
RT   identify fish, an SH3 and PX domain-containing protein, and Src
RT   substrate.";
RL   EMBO J. 17:4346-4357(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18417249; DOI=10.1016/j.ejcb.2008.02.008;
RA   Blouw B., Seals D.F., Pass I., Diaz B., Courtneidge S.A.;
RT   "A role for the podosome/invadopodia scaffold protein Tks5 in tumor
RT   growth in vivo.";
RL   Eur. J. Cell Biol. 87:555-567(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-566 AND SER-993, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH CYBA.
RX   PubMed=19755709; DOI=10.1126/scisignal.2000368;
RA   Diaz B., Shani G., Pass I., Anderson D., Quintavalle M.,
RA   Courtneidge S.A.;
RT   "Tks5-dependent, nox-mediated generation of reactive oxygen species is
RT   necessary for invadopodia formation.";
RL   Sci. Signal. 2:RA53-RA53(2009).
CC   -!- FUNCTION: Adapter protein involved in invadopodia and podosome
CC       formation, extracellular matrix degradation and invasiveness of
CC       some cancer cells. Binds matrix metalloproteinases (ADAMs), NADPH
CC       oxidases (NOXs) and phosphoinositides. Acts as an organizer
CC       protein that allows NOX1- or NOX3-dependent reactive oxygen
CC       species (ROS) generation and ROS localization. In association with
CC       ADAM12, mediates the neurotoxic effect of beta-amyloid peptide (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with ADAM12, ADAM15 and ADAM19 (By similarity).
CC       Interacts with NOXO1 (By similarity). Interacts (via SH3 domains)
CC       with NOXA1; the interaction is direct (By similarity). Interacts
CC       (via N-terminus) with CYBA. Interacts with FASLG (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell projection, podosome (By
CC       similarity). Note=Cytoplasmic in normal cells and localizes to
CC       podosomes in Src-transformed cells (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1;
CC         IsoId=O89032-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O89032-2; Sequence=VSP_023315;
CC       Name=3;
CC         IsoId=O89032-3; Sequence=VSP_023314, VSP_023315;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Not found in the spleen and
CC       testis.
CC   -!- DOMAIN: The PX domain is required for podosome localization
CC       because of its ability to bind phosphatidylinositol 3-phosphate
CC       (PtdIns(3)P) and phosphatidylinositol 3,4-biphosphate
CC       (PtdIns(3,4)P2) and, to a lesser extent, phosphatidylinositol 4-
CC       phosphate (PtdIns(4)P), phosphatidylinositol 5-biphosphate
CC       (PtdIns(5)P), and phosphatidylinositol 3,5-biphosphate
CC       (PtdIns(3,5)P2). Binds to the third intramolecular SH3 domain (By
CC       similarity).
CC   -!- DOMAIN: The fifth SH3 domain mediates binding with ADAM12, ADAM15
CC       and ADAM19 (By similarity).
CC   -!- PTM: Tyrosine phosphorylated by SRC. Phosphorylation plays a
CC       regulatory role in the protein localization. The intramolecular
CC       interaction of the PX domain with the third SH3 domain maintains
CC       the protein in the cytoplasm and phosphorylation disrupts this
CC       interaction, resulting in the redistribution of the protein from
CC       cytoplasm to the perimembrane region. Phosphorylated on serine
CC       upon DNA damage, probably by ATM or ATR (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Shows significant decrease in total cellular
CC       reactive oxygen species (ROS) and in podosome formation.
CC   -!- SIMILARITY: Belongs to the SH3PXD2 family.
CC   -!- SIMILARITY: Contains 1 PX (phox homology) domain.
CC   -!- SIMILARITY: Contains 5 SH3 domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI18023.1; Type=Frameshift; Positions=788;
CC   -----------------------------------------------------------------------
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DR   EMBL; AJ007012; CAA07416.1; -; mRNA.
DR   EMBL; BC118022; AAI18023.1; ALT_FRAME; mRNA.
DR   IPI; IPI00280250; -.
DR   IPI; IPI00828487; -.
DR   IPI; IPI00828947; -.
DR   UniGene; Mm.127560; -.
DR   HSSP; P14598; 1OV3.
DR   ProteinModelPortal; O89032; -.
DR   SMR; O89032; 5-141, 167-329, 448-506, 835-901, 1063-1124.
DR   IntAct; O89032; 1.
DR   STRING; O89032; -.
DR   PhosphoSite; O89032; -.
DR   PRIDE; O89032; -.
DR   Ensembl; ENSMUST00000081619; ENSMUSP00000080325; ENSMUSG00000053617.
DR   Ensembl; ENSMUST00000111796; ENSMUSP00000107426; ENSMUSG00000053617.
DR   Ensembl; ENSMUST00000111800; ENSMUSP00000107430; ENSMUSG00000053617.
DR   UCSC; uc008huy.1; mouse.
DR   MGI; MGI:1298393; Sh3pxd2a.
DR   eggNOG; roNOG08950; -.
DR   GeneTree; ENSGT00530000063010; -.
DR   HOGENOM; HBG715788; -.
DR   HOVERGEN; HBG089589; -.
DR   InParanoid; O89032; -.
DR   OrthoDB; EOG4NKBTR; -.
DR   NextBio; 285465; -.
DR   ArrayExpress; O89032; -.
DR   Bgee; O89032; -.
DR   CleanEx; MM_SH3PXD2A; -.
DR   Genevestigator; O89032; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002102; C:podosome; ISS:UniProtKB.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   InterPro; IPR001683; Phox.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:3.30.1520.10; PX; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF00018; SH3_1; 4.
DR   SMART; SM00312; PX; 1.
DR   SMART; SM00326; SH3; 5.
DR   SUPFAM; SSF64268; PX; 1.
DR   SUPFAM; SSF50044; SH3; 5.
DR   PROSITE; PS50195; PX; 1.
DR   PROSITE; PS50002; SH3; 5.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell projection; Coiled coil;
KW   Cytoplasm; Phosphoprotein; Repeat; SH3 domain.
FT   CHAIN         1   1124       SH3 and PX domain-containing protein 2A.
FT                                /FTId=PRO_0000278489.
FT   DOMAIN        4    128       PX.
FT   DOMAIN      166    225       SH3 1.
FT   DOMAIN      266    325       SH3 2.
FT   DOMAIN      447    506       SH3 3.
FT   DOMAIN      833    892       SH3 4.
FT   DOMAIN     1062   1124       SH3 5.
FT   COILED      907    937       Potential.
FT   COMPBIAS    633    709       Ser-rich.
FT   MOD_RES     405    405       Phosphoserine (By similarity).
FT   MOD_RES     420    420       Phosphoserine (By similarity).
FT   MOD_RES     546    546       Phosphoserine.
FT   MOD_RES     566    566       Phosphoserine.
FT   MOD_RES     592    592       Phosphoserine (By similarity).
FT   MOD_RES     643    643       Phosphoserine (By similarity).
FT   MOD_RES     721    721       Phosphoserine (By similarity).
FT   MOD_RES     728    728       Phosphothreonine (By similarity).
FT   MOD_RES     766    766       Phosphoserine (By similarity).
FT   MOD_RES     993    993       Phosphoserine.
FT   MOD_RES    1007   1007       Phosphoserine (By similarity).
FT   MOD_RES    1008   1008       Phosphoserine (By similarity).
FT   MOD_RES    1029   1029       Phosphoserine (By similarity).
FT   VAR_SEQ     143    157       Missing (in isoform 3).
FT                                /FTId=VSP_023314.
FT   VAR_SEQ     240    267       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_023315.
SQ   SEQUENCE   1124 AA;  124171 MW;  2A001B1D1CE98A67 CRC64;
     MLAYCVQDAT VVDVEKRRSP SKHYVYIINV TWSDSTSQTI YRRYSKFFDL QMQLLDKFPI
     EGGQKDPKQR IIPFLPGKIL FRRSHIRDVA VKRLKPIDEY CRALVRLPPH ISQCDEVFRF
     FEARPEDVNP PKEDYGSSKR KSVWLSSWAE SPKKDVTGAD TNAEPMILEQ YVVVSNYKKQ
     ENSELSLQAG EVVDVIEKNE SGWWFVSTSE EQGWVPATYL EAQNGTRDDS DINTSKTGEV
     SKRRKAHLRR LDRRWTLGGM VNRQHSREEK YVTVQPYTSQ SKDEIGFEKG VTVEVIRKNL
     EGWWYIRYLG KEGWAPASYL KKAKDDLPTR KKNLAGPVEI IGNIMEISNL LNKKASGDKE
     APAEGEGSEA PITKKEISLP ILCNASNGSA LAIPERTTSK LAQGSPAVAR IAPQRAQISS
     PNLRTRPPPR RESSLGFQLP KPPEPPSVEV EYYTIAEFQS CISDGISFRG GQKAEVIDKN
     SGGWWYVQIG EKEGWAPASY IDKRKKPNLS RRTSTLTRPK VPPPAPPSKP KEAEENPVGA
     CESQGSPLKV KYEEPEYDVP AFGFDSEPEM NEEPSGDRGS GDKHPAQPRR ISPASSLQRA
     HFKVGESSED VALEEETIYE NEGFRPYTED TLSARGSSGD SDSPGSSSLS LAVKNSPKSD
     SPKSSSLLKL KAEKNAQAEL GKNQSNISFS SSVTISTTCS SSSSSSSLSK NNGDLKPRSA
     SDAGIRDTPK VGTKKDPDVK AGLASCARAK PSVRPKPVLN RAESQSQEKM DISSLRRQLR
     PTGQLRGGLK GSRSEDSELP PQMASEGSRR GSADIIPLTA TTPPCVPKKE WEGQGATYVT
     CSAYQKVQDS EISFPEGAEV HVLEKAVSGW WYVRFGELEG WAPSHYLVAE ENQQPDTASK
     EGDTGKSSQN EGKSDSLEKI EKRVQALNTV NQSKRATPPI PSKPPGGFGK TSGTVAVKMR
     NGVRQVAVRP QSVFVSPPPK DNNLSCALRR NESLTATDSL RGVRRNSSFS TARSAAAEAK
     GRLAERAASQ GSESPLLPTQ RKGIPVSPVR PKPIEKSQFI HNNLKDVYIS IADYEGDEET
     AGFQEGVSME VLEKNPNGWW YCQILDEVKP FKGWVPSNYL EKKN
//
ID   COR1A_MOUSE             Reviewed;         461 AA.
AC   O89053; Q7TMU0; Q9R1Y8; Q9R288;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 5.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Coronin-1A;
DE   AltName: Full=Coronin-like protein A;
DE            Short=Clipin-A;
DE   AltName: Full=Coronin-like protein p57;
DE   AltName: Full=Tryptophan aspartate-containing coat protein;
DE            Short=TACO;
GN   Name=Coro1a; Synonyms=Coro1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98449467; PubMed=9778037;
RA   Okumura M., Kung C., Wong S., Rodgers M., Thomas M.L.;
RT   "Definition of family of coronin-related proteins conserved between
RT   humans and mice: close genetic linkage between coronin-2 and CD45-
RT   associated protein.";
RL   DNA Cell Biol. 17:779-787(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 11-14, TISSUE
RP   SPECIFICITY, SUBCELLULAR LOCATION, AND ROLE IN PHAGOSOME TRAFFICKING.
RC   STRAIN=C57BL/6; TISSUE=Macrophage;
RX   MEDLINE=99268530; PubMed=10338208; DOI=10.1016/S0092-8674(00)80754-0;
RA   Ferrari G., Langen H., Naito M., Pieters J.;
RT   "A coat protein on phagosomes involved in the intracellular survival
RT   of mycobacteria.";
RL   Cell 97:435-447(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kohchi C., Inagawa H., Makino K., Terada H., Soma G.;
RT   "A new therapeutic strategy of mycobacterium infection by use of anti-
RT   TACO sequence.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Hematopoietic, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 156-276.
RC   STRAIN=BALB/c; TISSUE=Spleen;
RX   MEDLINE=99012997; PubMed=9798653; DOI=10.1016/S0161-5890(98)00031-5;
RA   Chu C.C., Paul W.E.;
RT   "Expressed genes in interleukin-4 treated B cells identified by cDNA
RT   representational difference analysis.";
RL   Mol. Immunol. 35:487-502(1998).
RN   [6]
RP   PROTEIN SEQUENCE OF 215-233, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-418, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-402, WD REPEATS, AND
RP   COILED-COIL DOMAIN.
RX   PubMed=16407068; DOI=10.1016/j.str.2005.09.013;
RA   Appleton B.A., Wu P., Wiesmann C.;
RT   "The crystal structure of murine coronin-1: a regulator of actin
RT   cytoskeletal dynamics in lymphocytes.";
RL   Structure 14:87-96(2006).
CC   -!- FUNCTION: May be a crucial component of the cytoskeleton of highly
CC       motile cells, functioning both in the invagination of large pieces
CC       of plasma membrane, as well as in forming protrusions of the
CC       plasma membrane involved in cell locomotion. In mycobacteria-
CC       infected cells, its retention on the phagosomal membrane prevents
CC       fusion between phagosomes and lysosomes.
CC   -!- SUBUNIT: Binds actin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell
CC       cortex. Cytoplasmic vesicle, phagosome membrane. Note=In non-
CC       infected macrophages, associated with the cortical microtubule
CC       network. In mycobacteria-infected macrophages, becomes
CC       progressively relocalized and retained around the mycobacterial
CC       phagosomes. Retention on the phagosomal membrane is strictly
CC       dependent on mycobacterial viability and not due to impaired
CC       acidification.
CC   -!- TISSUE SPECIFICITY: Expressed in spleen, lymph nodes, thymus,
CC       brain and at very lower levels in lung. Also expressed in cells of
CC       the lymphoid/myeloid lineage. Not expressed in Kuffper cells.
CC   -!- SIMILARITY: Belongs to the WD repeat coronin family.
CC   -!- SIMILARITY: Contains 7 WD repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF143955; AAD32703.1; -; mRNA.
DR   EMBL; AF047388; AAD31082.1; -; mRNA.
DR   EMBL; AF495468; AAM18514.1; -; mRNA.
DR   EMBL; BC002136; AAH02136.1; -; mRNA.
DR   EMBL; BC053398; AAH53398.1; -; mRNA.
DR   EMBL; U89399; AAC36506.1; -; mRNA.
DR   IPI; IPI00323600; -.
DR   RefSeq; NP_034028.1; NM_009898.2.
DR   UniGene; Mm.290482; -.
DR   PDB; 2AKF; X-ray; 1.20 A; A/B/C=430-461.
DR   PDB; 2AQ5; X-ray; 1.75 A; A=1-402.
DR   PDB; 2B4E; X-ray; 2.30 A; A=1-402.
DR   PDBsum; 2AKF; -.
DR   PDBsum; 2AQ5; -.
DR   PDBsum; 2B4E; -.
DR   ProteinModelPortal; O89053; -.
DR   SMR; O89053; 9-394, 430-461.
DR   STRING; O89053; -.
DR   PhosphoSite; O89053; -.
DR   PRIDE; O89053; -.
DR   Ensembl; ENSMUST00000032949; ENSMUSP00000032949; ENSMUSG00000030707.
DR   Ensembl; ENSMUST00000106364; ENSMUSP00000101972; ENSMUSG00000030707.
DR   GeneID; 12721; -.
DR   KEGG; mmu:12721; -.
DR   UCSC; uc009jsk.1; mouse.
DR   CTD; 12721; -.
DR   MGI; MGI:1345961; Coro1a.
DR   eggNOG; roNOG09484; -.
DR   HOGENOM; HBG735393; -.
DR   HOVERGEN; HBG059978; -.
DR   InParanoid; O89053; -.
DR   OMA; VPTVCGH; -.
DR   OrthoDB; EOG4RNB8C; -.
DR   PhylomeDB; O89053; -.
DR   NextBio; 282000; -.
DR   ArrayExpress; O89053; -.
DR   Bgee; O89053; -.
DR   CleanEx; MM_CORO1A; -.
DR   Genevestigator; O89053; -.
DR   GermOnline; ENSMUSG00000030707; Mus musculus.
DR   GO; GO:0001772; C:immunological synapse; IDA:MGI.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR   GO; GO:0007015; P:actin filament organization; IMP:MGI.
DR   GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR   GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
DR   GO; GO:0030595; P:leukocyte chemotaxis; IMP:MGI.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:MGI.
DR   GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:MGI.
DR   GO; GO:0030833; P:regulation of actin filament polymerization; IMP:MGI.
DR   GO; GO:0008360; P:regulation of cell shape; IMP:MGI.
DR   GO; GO:0034097; P:response to cytokine stimulus; IMP:MGI.
DR   GO; GO:0043029; P:T cell homeostasis; IMP:MGI.
DR   GO; GO:0032796; P:uropod organization; IMP:MGI.
DR   InterPro; IPR015505; Coronin.
DR   InterPro; IPR015048; DUF1899.
DR   InterPro; IPR015049; DUF1900.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   PANTHER; PTHR10856; Coronin; 1.
DR   Pfam; PF08953; DUF1899; 1.
DR   Pfam; PF08954; DUF1900; 1.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM00320; WD40; 3.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Actin-binding; Coiled coil; Cytoplasm;
KW   Cytoplasmic vesicle; Cytoskeleton; Direct protein sequencing;
KW   Membrane; Phosphoprotein; Repeat; WD repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    461       Coronin-1A.
FT                                /FTId=PRO_0000050921.
FT   REPEAT       13     63       WD 1.
FT   REPEAT       73    110       WD 2.
FT   REPEAT      123    160       WD 3.
FT   REPEAT      164    204       WD 4.
FT   REPEAT      207    251       WD 5.
FT   REPEAT      258    296       WD 6.
FT   REPEAT      302    349       WD 7.
FT   COILED      424    461
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES     356    356       Phosphoserine (By similarity).
FT   MOD_RES     418    418       Phosphothreonine.
FT   CONFLICT    125    125       I -> V (in Ref. 1; AAD32703 and 4;
FT                                AAH02136).
FT   CONFLICT    299    299       S -> F (in Ref. 4; AAH53398).
FT   TURN         10     13
FT   STRAND       15     18
FT   HELIX        21     23
FT   STRAND       24     27
FT   STRAND       39     42
FT   STRAND       44     51
FT   STRAND       54     56
FT   STRAND       59     63
FT   STRAND       84     89
FT   STRAND       96    101
FT   STRAND      104    110
FT   STRAND      124    128
FT   STRAND      134    139
FT   STRAND      141    143
FT   STRAND      146    151
FT   STRAND      156    160
FT   TURN        161    163
FT   STRAND      166    170
FT   TURN        172    174
FT   STRAND      179    184
FT   STRAND      191    195
FT   STRAND      198    204
FT   TURN        205    208
FT   STRAND      209    215
FT   STRAND      220    222
FT   STRAND      225    228
FT   STRAND      233    239
FT   STRAND      245    251
FT   STRAND      259    263
FT   STRAND      271    275
FT   TURN        277    279
FT   STRAND      281    286
FT   STRAND      292    297
FT   STRAND      304    310
FT   STRAND      317    321
FT   HELIX       324    326
FT   HELIX       329    331
FT   STRAND      333    341
FT   STRAND      344    351
FT   TURN        361    363
FT   HELIX       376    380
FT   HELIX       432    460
SQ   SEQUENCE   461 AA;  50989 MW;  9098F53757C5318D CRC64;
     MSRQVVRSSK FRHVFGQPAK ADQCYEDVRV SQTTWDSGFC AVNPKFMALI CEASGGGAFL
     VLPLGKTGRV DKNVPLVCGH TAPVLDIAWC PHNDNVIASG SEDCTVMVWE IPDGGLVLPL
     REPVITLEGH TKRVGIVAWH PTAQNVLLSA GCDNVILVWD VGTGAAVLTL GPDVHPDTIY
     SVDWSRDGAL ICTSCRDKRV RVIEPRKGTV VAEKDRPHEG TRPVHAVFVS EGKILTTGFS
     RMSERQVALW DTKHLEEPLS LQELDTSSGV LLPFFDPDTN IVYLCGKGDS SIRYFEITSE
     APFLHYLSMF SSKESQRGMG YMPKRGLEVN KCEIARFYKL HERKCEPIAM TVPRKSDLFQ
     EDLYPPTAGP DPALTAEEWL GGRDAGPLLI SLKDGYVPPK SRELRVNRGL DSARRRATPE
     PSGTPSSDTV SRLEEDVRNL NAIVQKLQER LDRLEETVQA K
//
ID   COPE_MOUSE              Reviewed;         308 AA.
AC   O89079; Q9JM65;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Coatomer subunit epsilon;
DE   AltName: Full=Epsilon-coat protein;
DE            Short=Epsilon-COP;
GN   Name=Cope; Synonyms=Cope1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Hahn Y., Chung J.H.;
RT   "Mouse Cope1 gene for nonclathrin coat protein epsilon-COP.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 155-298.
RC   STRAIN=BALB/c; TISSUE=Spleen;
RX   MEDLINE=99012997; PubMed=9798653; DOI=10.1016/S0161-5890(98)00031-5;
RA   Chu C.C., Paul W.E.;
RT   "Expressed genes in interleukin-4 treated B cells identified by cDNA
RT   representational difference analysis.";
RL   Mol. Immunol. 35:487-502(1998).
CC   -!- FUNCTION: The coatomer is a cytosolic protein complex that binds
CC       to dilysine motifs and reversibly associates with Golgi non-
CC       clathrin-coated vesicles, which further mediate biosynthetic
CC       protein transport from the ER, via the Golgi up to the trans Golgi
CC       network. Coatomer complex is required for budding from Golgi
CC       membranes, and is essential for the retrograde Golgi-to-ER
CC       transport of dilysine-tagged proteins. In mammals, the coatomer
CC       can only be recruited by membranes associated to ADP-ribosylation
CC       factors (ARFs), which are small GTP-binding proteins; the complex
CC       also influences the Golgi structural integrity, as well as the
CC       processing, activity, and endocytic recycling of LDL receptors (By
CC       similarity).
CC   -!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
CC       beta, beta', gamma, delta, epsilon and zeta subunits.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus
CC       membrane; Peripheral membrane protein; Cytoplasmic side (By
CC       similarity). Cytoplasmic vesicle, COPI-coated vesicle membrane;
CC       Peripheral membrane protein; Cytoplasmic side (By similarity).
CC       Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic
CC       side of the Golgi, as well as on the vesicles/buds originating
CC       from it (By similarity).
CC   -!- PTM: Phosphorylated by PKA (By similarity).
CC   -!- SIMILARITY: Belongs to the COPE family.
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DR   EMBL; AB039837; BAA92384.1; -; mRNA.
DR   EMBL; BC009170; AAH09170.1; -; mRNA.
DR   EMBL; BC083336; AAH83336.1; -; mRNA.
DR   EMBL; U89427; AAC36533.1; -; mRNA.
DR   IPI; IPI00130840; -.
DR   RefSeq; NP_067513.1; NM_021538.1.
DR   UniGene; Mm.28668; -.
DR   ProteinModelPortal; O89079; -.
DR   SMR; O89079; 17-307.
DR   STRING; O89079; -.
DR   PhosphoSite; O89079; -.
DR   REPRODUCTION-2DPAGE; O89079; -.
DR   PRIDE; O89079; -.
DR   Ensembl; ENSMUST00000066469; ENSMUSP00000071078; ENSMUSG00000055681.
DR   GeneID; 59042; -.
DR   KEGG; mmu:59042; -.
DR   UCSC; uc009lzx.1; mouse.
DR   CTD; 59042; -.
DR   MGI; MGI:1891702; Cope.
DR   eggNOG; roNOG14547; -.
DR   HOGENOM; HBG382235; -.
DR   HOVERGEN; HBG002201; -.
DR   InParanoid; O89079; -.
DR   OMA; CYMAQGK; -.
DR   OrthoDB; EOG43XV42; -.
DR   PhylomeDB; O89079; -.
DR   NextBio; 314654; -.
DR   ArrayExpress; O89079; -.
DR   Bgee; O89079; -.
DR   CleanEx; MM_COPE; -.
DR   Genevestigator; O89079; -.
DR   GermOnline; ENSMUSG00000055681; Mus musculus.
DR   GO; GO:0030126; C:COPI vesicle coat; IEA:InterPro.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; IEA:InterPro.
DR   InterPro; IPR006822; Coatomer_esu.
DR   InterPro; IPR011990; TPR-like_helical.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 2.
DR   PANTHER; PTHR10805; Coatomer_E; 1.
DR   Pfam; PF04733; Coatomer_E; 1.
DR   PIRSF; PIRSF016478; Coatomer_esu; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW   Membrane; Phosphoprotein; Protein transport; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    308       Coatomer subunit epsilon.
FT                                /FTId=PRO_0000193852.
FT   MOD_RES      45     45       Phosphoserine (By similarity).
FT   MOD_RES      99     99       Phosphoserine (By similarity).
FT   CONFLICT    291    291       Q -> R (in Ref. 3; AAC36533).
SQ   SEQUENCE   308 AA;  34567 MW;  81331BDDB1F99270 CRC64;
     MAPPVPGAVS GGSGEVDELF DVKNAFYIGS YQQCINEAQR VKLSSPEREV ERDVFLYRAY
     LAQRKYGVVL DEIKPSSAPE LQAVRMFAEY LASENQRDSI VLELDREMSR SVDVTNTTFL
     LMAASIYFHD QNPDAALRTL HQGDGLECMA MTIQILLKLD RLDLARKELK KMQDQDEDAT
     LTQLATAWVN LAVGGEKLQE AYYIFQELAD KCSPTLLLLN GQAACHSAQG RWETAEGVLQ
     EALDKDSGHP ETLINLIVLS QHLGKPPEVT NRYLSQLKDA HRAHPFIKEY QAKENDFDRL
     AMQYAPSA
//
ID   PDE4A_MOUSE             Reviewed;         844 AA.
AC   O89084; Q8R078; Q9JHQ4; Q9QX48; Q9QX49; Q9QXI8;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 2.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=cAMP-specific 3',5'-cyclic phosphodiesterase 4A;
DE            EC=3.1.4.17;
GN   Name=Pde4a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   TISSUE=Embryonic stem cell;
RX   MEDLINE=20069070; PubMed=10602991; DOI=10.1007/s003350010008;
RA   Olsen A.E., Bolger G.B.;
RT   "Physical mapping and promoter structure of the murine cAMP-specific
RT   phosphodiesterase pde4a gene.";
RL   Mamm. Genome 11:41-45(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ENZYME REGULATION.
RC   STRAIN=Swiss Webster; TISSUE=Brain;
RX   MEDLINE=21167368; PubMed=11267656; DOI=10.1016/S0167-4781(01)00164-6;
RA   Cherry J.A., Thompson B.E., Pho V.;
RT   "Diazepam and rolipram differentially inhibit cyclic AMP-specific
RT   phosphodiesterases PDE4A1 and PDE4B3 in the mouse.";
RL   Biochim. Biophys. Acta 1518:27-35(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 248-355 (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=98343959; PubMed=9677330;
RA   Sullivan M., Rena G., Begg F., Gordon L., Olsen A.S., Houslay M.D.;
RT   "Identification and characterization of the human homologue of the
RT   short PDE4A cAMP-specific phosphodiesterase 4A variant RD1 (PDE4A1) by
RT   analysis of the human HSPDE4A gene locus located at chromosome
RT   19p13.2.";
RL   Biochem. J. 333:693-703(1998).
CC   -!- FUNCTION: Hydrolyzes the second messenger cAMP, which is a key
CC       regulator of many important physiological processes (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Adenosine 3',5'-cyclic phosphate + H(2)O =
CC       adenosine 5'-phosphate.
CC   -!- COFACTOR: Binds 2 divalent metal cations per subunit. Site 1 may
CC       preferentially bind zinc ions, while site 2 has a preference for
CC       magnesium and/or manganese ions (By similarity).
CC   -!- ENZYME REGULATION: Inhibited by rolipram and diazepam.
CC   -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC       3',5'-cyclic AMP: step 1/1.
CC   -!- SUBUNIT: Interacts with LYN and ARRB2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1;
CC         IsoId=O89084-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O89084-2; Sequence=VSP_004563, VSP_004564;
CC       Name=3;
CC         IsoId=O89084-3; Sequence=VSP_004562;
CC   -!- PTM: Proteolytically cleaved by caspase-3 (By similarity).
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
CC       family. PDE4 subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH27224.2; Type=Erroneous initiation;
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DR   EMBL; AF142646; AAF14519.1; -; Genomic_DNA.
DR   EMBL; AF142643; AAF14519.1; JOINED; Genomic_DNA.
DR   EMBL; AF142644; AAF14519.1; JOINED; Genomic_DNA.
DR   EMBL; AF142645; AAF14519.1; JOINED; Genomic_DNA.
DR   EMBL; AF142646; AAF14520.1; -; Genomic_DNA.
DR   EMBL; AF142644; AAF14520.1; JOINED; Genomic_DNA.
DR   EMBL; AF142645; AAF14520.1; JOINED; Genomic_DNA.
DR   EMBL; AF208021; AAF19201.2; -; mRNA.
DR   EMBL; AJ297396; CAB96769.1; -; mRNA.
DR   EMBL; BC027224; AAH27224.2; ALT_INIT; mRNA.
DR   EMBL; U97586; AAC25681.1; -; mRNA.
DR   IPI; IPI00130881; -.
DR   IPI; IPI00228051; -.
DR   IPI; IPI00316902; -.
DR   RefSeq; NP_062772.3; NM_019798.5.
DR   RefSeq; NP_899668.1; NM_183408.3.
DR   UniGene; Mm.191749; -.
DR   ProteinModelPortal; O89084; -.
DR   SMR; O89084; 254-696.
DR   STRING; O89084; -.
DR   PhosphoSite; O89084; -.
DR   PRIDE; O89084; -.
DR   Ensembl; ENSMUST00000003395; ENSMUSP00000003395; ENSMUSG00000032177.
DR   Ensembl; ENSMUST00000039413; ENSMUSP00000037025; ENSMUSG00000032177.
DR   Ensembl; ENSMUST00000115458; ENSMUSP00000111118; ENSMUSG00000032177.
DR   GeneID; 18577; -.
DR   KEGG; mmu:18577; -.
DR   UCSC; uc009oki.1; mouse.
DR   UCSC; uc009okj.1; mouse.
DR   UCSC; uc009okl.1; mouse.
DR   CTD; 18577; -.
DR   MGI; MGI:99558; Pde4a.
DR   GeneTree; ENSGT00550000074309; -.
DR   HOGENOM; HBG315913; -.
DR   HOVERGEN; HBG108239; -.
DR   InParanoid; O89084; -.
DR   OMA; HIPVDTM; -.
DR   OrthoDB; EOG402WRM; -.
DR   BRENDA; 3.1.4.17; 244.
DR   NextBio; 294438; -.
DR   ArrayExpress; O89084; -.
DR   Bgee; O89084; -.
DR   CleanEx; MM_PDE4A; -.
DR   Genevestigator; O89084; -.
DR   GermOnline; ENSMUSG00000032177; Mus musculus.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR003607; Metal-dep_PHydrolase_HD_dom.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR023174; PDEase_CS.
DR   Gene3D; G3DSA:1.10.1300.10; PDEase_catalytic_dom; 1.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00471; HDc; 1.
DR   PROSITE; PS00126; PDEASE_I; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; cAMP; Cytoplasm; Hydrolase; Metal-binding;
KW   Phosphoprotein.
FT   CHAIN         1    844       cAMP-specific 3',5'-cyclic
FT                                phosphodiesterase 4A.
FT                                /FTId=PRO_0000198807.
FT   NP_BIND     419    423       cAMP (By similarity).
FT   REGION      317    710       Catalytic (By similarity).
FT   ACT_SITE    419    419       Proton donor (By similarity).
FT   METAL       423    423       Divalent metal cation 1 (By similarity).
FT   METAL       459    459       Divalent metal cation 1 (By similarity).
FT   METAL       460    460       Divalent metal cation 1 (By similarity).
FT   METAL       460    460       Divalent metal cation 2 (By similarity).
FT   METAL       577    577       Divalent metal cation 1 (By similarity).
FT   BINDING     460    460       cAMP (By similarity).
FT   BINDING     577    577       cAMP (By similarity).
FT   BINDING     628    628       cAMP (By similarity).
FT   SITE         69     70       Cleavage; by caspase-3 (By similarity).
FT   SITE        580    580       Binds AMP, but not cAMP (By similarity).
FT   MOD_RES     160    160       Phosphoserine (By similarity).
FT   MOD_RES     672    672       Phosphoserine (By similarity).
FT   MOD_RES     674    674       Phosphoserine (By similarity).
FT   VAR_SEQ       1    234       Missing (in isoform 2).
FT                                /FTId=VSP_004563.
FT   VAR_SEQ       1    102       MEPPAAPSERSLSLSLPGPREGQATLKPPPQHLWRQPRTPI
FT                                RIQQRGYSDSAERSEPERSPHRPIERADAVDTGDRPGLRTT
FT                                RMSWPSSFHGTGTGGGSSRR -> MRSSAAPRARPRPPALA
FT                                LPLGPESLTHFSFSEEDTLRHPPGRCVS (in isoform
FT                                3).
FT                                /FTId=VSP_004562.
FT   VAR_SEQ     235    256       WCLEQLETMQTYRSVSEMASHK -> MPLVDFFCETCSKPW
FT                                LVGWWDQ (in isoform 2).
FT                                /FTId=VSP_004564.
FT   CONFLICT    516    516       R -> K (in Ref. 2; AAF19201).
FT   CONFLICT    685    685       S -> G (in Ref. 3; AAH27224).
SQ   SEQUENCE   844 AA;  93558 MW;  632396C9F70E0F61 CRC64;
     MEPPAAPSER SLSLSLPGPR EGQATLKPPP QHLWRQPRTP IRIQQRGYSD SAERSEPERS
     PHRPIERADA VDTGDRPGLR TTRMSWPSSF HGTGTGGGSS RRLEAENGPT PSPGRSPLDS
     QASPGLMLHA GAATSQRRES FLYRSDSDYD MSPKTMSRNS SVASEAHGED LIVTPFAQVL
     ASLRNVRSNF SLLTNVPIPS NKRSPLGGPP SVCKATLSEE TCQQLARETL EELDWCLEQL
     ETMQTYRSVS EMASHKFKRM LNRELTHLSE MSRSGNQVSE YISNTFLDKQ HEVEIPSPTP
     RQRPFQQPPP AAVQQAQPMS QITGLKKLVH TGSLNINVPR FGVKTDQEDL LAQELENLSK
     WGLNIFCVSE YAGGRSLSCI MYTIFQERDL LKKFHIPVDT MMTYMLTLED HYHADVAYHN
     SLHAADVLQS THVLLATPAL DAVFTDLEIL AALFAAAIHD VDHPGVSNQF LINTNSELAL
     MYNDESVLEN HHLAVGFKLL QEENCDIFQN LSKRQRQSLR KMVIDMVLAT DMSKHMTLLA
     DLKTMVETKK VTSSGVLLLD NYSDRIQVLR NMVHCADLSN PTKPLELYRQ WTDRIMAEFF
     QQGDRERERG MEISPMCDKH TASVEKSQVG FIDYIVHPLW ETWADLVHPD AQDILDTLED
     NRDWYHSAIR QSPSPTLEEE PGVLSDPALP DKFQFELTLE EEDEEDSLEV PGLPCTEETL
     LAPHDTRAQA MEQSKVKGQS PAVVEVAESL KQETASAHGA PEESAEAVGH SFSLETSILP
     DLRTLSPSEE AQGLLGLPSM AAEVEAPRDH LAAMRACSAC SGTSGDNSAV ISAPGRWGSG
     GDPA
//
ID   VTI1A_MOUSE             Reviewed;         217 AA.
AC   O89116; Q545P9;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Vesicle transport through interaction with t-SNAREs homolog 1A;
DE   AltName: Full=Vesicle transport v-SNARE protein Vti1-like 2;
DE   AltName: Full=Vti1-rp2;
GN   Name=Vti1a; Synonyms=Vti1, Vti1l2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98371016; PubMed=9705316; DOI=10.1074/jbc.273.34.21783;
RA   Xu Y., Wong S.H., Tang B.L., Subramaniam V.N., Zhang T., Hong W.;
RT   "A 29-kilodalton Golgi soluble N-ethylmaleimide-sensitive factor
RT   attachment protein receptor (Vti1-rp2) implicated in protein
RT   trafficking in the secretory pathway.";
RL   J. Biol. Chem. 273:21783-21789(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98221163; PubMed=9553086; DOI=10.1074/jbc.273.17.10317;
RA   Advani R.J., Bae H.-R., Bock J.B., Chao D.S., Doung Y.-C.,
RA   Prekeris R., Yoo J.-S., Scheller R.H.;
RT   "Seven novel mammalian SNARE proteins localize to distinct membrane
RT   compartments.";
RL   J. Biol. Chem. 273:10317-10324(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Lung, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   STRUCTURE BY NMR OF 3-94.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of RSGI RUH-009, an N-terminal domain of VTI1A
RT   [Mus musculus].";
RL   Submitted (MAY-2005) to the PDB data bank.
CC   -!- FUNCTION: V-SNARE that mediates vesicle transport pathways through
CC       interactions with t-SNAREs on the target membrane. These
CC       interactions are proposed to mediate aspects of the specificity of
CC       vesicle trafficking and to promote fusion of the lipid bilayers.
CC       Involved in vesicular transport from the late endosomes to the
CC       trans-Golgi network. May be concerned with increased secretion of
CC       cytokines associated with cellular senescence.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type
CC       IV membrane protein. Note=Mainly associated with the Golgi
CC       apparatus.
CC   -!- TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung,
CC       liver, skeletal muscle, kidney and testis.
CC   -!- SIMILARITY: Belongs to the VTI1 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF035823; AAC32049.1; -; mRNA.
DR   EMBL; AF035209; AAC23482.1; -; mRNA.
DR   EMBL; AK004751; BAB23532.1; -; mRNA.
DR   EMBL; AK028646; BAC26046.1; -; mRNA.
DR   EMBL; BC019386; AAH19386.1; -; mRNA.
DR   IPI; IPI00131540; -.
DR   RefSeq; NP_058558.1; NM_016862.3.
DR   UniGene; Mm.258637; -.
DR   UniGene; Mm.451214; -.
DR   PDB; 1VCS; NMR; -; A=6-94.
DR   PDBsum; 1VCS; -.
DR   ProteinModelPortal; O89116; -.
DR   SMR; O89116; 8-94, 113-190.
DR   STRING; O89116; -.
DR   PhosphoSite; O89116; -.
DR   PRIDE; O89116; -.
DR   Ensembl; ENSMUST00000095950; ENSMUSP00000093644; ENSMUSG00000024983.
DR   GeneID; 53611; -.
DR   KEGG; mmu:53611; -.
DR   UCSC; uc008hxx.1; mouse.
DR   CTD; 53611; -.
DR   MGI; MGI:1855699; Vti1a.
DR   eggNOG; roNOG15861; -.
DR   GeneTree; ENSGT00530000063466; -.
DR   HOVERGEN; HBG104027; -.
DR   OrthoDB; EOG4V6ZHV; -.
DR   PhylomeDB; O89116; -.
DR   NextBio; 310323; -.
DR   ArrayExpress; O89116; -.
DR   Bgee; O89116; -.
DR   Genevestigator; O89116; -.
DR   GermOnline; ENSMUSG00000024983; Mus musculus.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR   InterPro; IPR010989; t-SNARE.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   InterPro; IPR007705; Vesicle_trsprt_v-SNARE_N.
DR   Pfam; PF05008; V-SNARE; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF47661; t-snare; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Golgi apparatus; Membrane;
KW   Protein transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    217       Vesicle transport through interaction
FT                                with t-SNAREs homolog 1A.
FT                                /FTId=PRO_0000218226.
FT   TOPO_DOM      1    192       Cytoplasmic (Potential).
FT   TRANSMEM    193    213       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   TOPO_DOM    214    217       Vesicular (Potential).
FT   COILED       31     92       Potential.
FT   COILED      112    178       Potential.
FT   HELIX         9     25
FT   HELIX        26     28
FT   TURN         31     33
FT   HELIX        34     59
FT   TURN         64     66
FT   HELIX        67     87
FT   HELIX        89     92
SQ   SEQUENCE   217 AA;  24986 MW;  3FD7B7A5A16E3522 CRC64;
     MSSDFEGYEQ DFAVLTAEIT SKIARVPRLP PDEKKQMVAN VEKQLEEARE LLEQMDLEVR
     EIPPQSRGMY SNRMRSYKQE MGKLETDFKR SRIAYSDEVR NELLGDAGNS SENQRAHLLD
     NTERLERSSR RLEAGYQIAV ETEQIGQEML ENLSHDREKI QRARDRLRDA DANLGKSSRI
     LTGMLRRIIQ NRILLVILGI IVVIAILTAI AFFVKGH
//
ID   COX2_MOUSE              Reviewed;         227 AA.
AC   P00405; Q85K21;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Cytochrome c oxidase subunit 2;
DE   AltName: Full=Cytochrome c oxidase polypeptide II;
GN   Name=Mtco2; Synonyms=COII, mt-Co2;
OS   Mus musculus (Mouse).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=82137051; PubMed=7332926; DOI=10.1016/0092-8674(81)90300-7;
RA   Bibb M.J., van Etten R.A., Wright C.T., Walberg M.W., Clayton D.A.;
RT   "Sequence and gene organization of mouse mitochondrial DNA.";
RL   Cell 26:167-180(1981).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 57-63.
RX   PubMed=8281018; DOI=10.1007/BF00360907;
RA   Nelson I., Gerasimov S., Marsac C., Lestienne P., Boursot P.;
RT   "Sequence analysis of a deleted mitochondrial DNA molecule in
RT   heteroplasmic mice.";
RL   Mamm. Genome 4:680-683(1993).
RN   [3]
RP   PROTEIN SEQUENCE OF 83-98; 135-171 AND 218-227, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory
CC       chain that catalyzes the reduction of oxygen to water. Subunits 1-
CC       3 form the functional core of the enzyme complex. Subunit 2
CC       transfers the electrons from cytochrome c via its binuclear copper
CC       A center to the bimetallic center of the catalytic subunit 1.
CC   -!- COFACTOR: Copper A.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; J01420; AAB48647.1; -; Genomic_DNA.
DR   EMBL; V00711; CAA24083.1; -; Genomic_DNA.
DR   EMBL; S68119; AAP15814.1; -; Genomic_DNA.
DR   IPI; IPI00131176; -.
DR   PIR; A00474; OBMS2.
DR   RefSeq; NP_904331.1; NC_005089.1.
DR   ProteinModelPortal; P00405; -.
DR   SMR; P00405; 2-227.
DR   STRING; P00405; -.
DR   PhosphoSite; P00405; -.
DR   SWISS-2DPAGE; P00405; -.
DR   PRIDE; P00405; -.
DR   Ensembl; ENSMUST00000082405; ENSMUSP00000080994; ENSMUSG00000064354.
DR   GeneID; 17709; -.
DR   KEGG; mmu:17709; -.
DR   CTD; 17709; -.
DR   MGI; MGI:102503; mt-Co2.
DR   eggNOG; roNOG08122; -.
DR   HOGENOM; HBG390534; -.
DR   HOVERGEN; HBG012727; -.
DR   InParanoid; P00405; -.
DR   OrthoDB; EOG4BZN3N; -.
DR   PhylomeDB; P00405; -.
DR   ProtClustDB; MTH00098; -.
DR   NextBio; 292315; -.
DR   Genevestigator; P00405; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR   InterPro; IPR001505; Copper_CuA.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR014222; Cyt_c_oxidase_su2.
DR   InterPro; IPR015964; Cyt_c_oxidase_su2-like_TM_dom.
DR   InterPro; IPR002429; Cyt_c_oxidase_su2_C.
DR   InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR   Gene3D; G3DSA:1.10.287.90; COX2_TM; 1.
DR   Gene3D; G3DSA:2.60.40.420; Cupredoxin; 1.
DR   PANTHER; PTHR22888; COX2_C; 1.
DR   Pfam; PF00116; COX2; 1.
DR   Pfam; PF02790; COX2_TM; 1.
DR   PRINTS; PR01166; CYCOXIDASEII.
DR   SUPFAM; SSF49503; Cupredoxin; 1.
DR   SUPFAM; SSF81464; Cyt_c_oxidase_II-like_TM; 1.
DR   TIGRFAMs; TIGR02866; CoxB; 1.
DR   PROSITE; PS00078; COX2; 1.
DR   PROSITE; PS50857; COX2_CUA; 1.
DR   PROSITE; PS50999; COX2_TM; 1.
PE   1: Evidence at protein level;
KW   Copper; Direct protein sequencing; Electron transport; Membrane;
KW   Metal-binding; Mitochondrion; Mitochondrion inner membrane;
KW   Respiratory chain; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    227       Cytochrome c oxidase subunit 2.
FT                                /FTId=PRO_0000183635.
FT   TOPO_DOM      1     26       Mitochondrial intermembrane (Potential).
FT   TRANSMEM     27     48       Helical; (Potential).
FT   TOPO_DOM     49     62       Mitochondrial matrix (Potential).
FT   TRANSMEM     63     82       Helical; (Potential).
FT   TOPO_DOM     83    227       Mitochondrial intermembrane (Potential).
FT   METAL       161    161       Copper A (Probable).
FT   METAL       196    196       Copper A (Probable).
FT   METAL       200    200       Copper A (Probable).
FT   METAL       204    204       Copper A (Probable).
SQ   SEQUENCE   227 AA;  25976 MW;  306C6EAD54802D11 CRC64;
     MAYPFQLGLQ DATSPIMEEL MNFHDHTLMI VFLISSLVLY IISLMLTTKL THTSTMDAQE
     VETIWTILPA VILIMIALPS LRILYMMDEI NNPVLTVKTM GHQWYWSYEY TDYEDLCFDS
     YMIPTNDLKP GELRLLEVDN RVVLPMELPI RMLISSEDVL HSWAVPSLGL KTDAIPGRLN
     QATVTSNRPG LFYGQCSEIC GSNHSFMPIV LEMVPLKYFE NWSASMI
//
ID   ABL1_MOUSE              Reviewed;        1123 AA.
AC   P00520; P97896; Q61252; Q61253; Q61254; Q61255; Q61256; Q61257;
AC   Q61258; Q61259; Q61260; Q61261; Q6PCM5; Q8C1X4;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 3.
DT   08-MAR-2011, entry version 153.
DE   RecName: Full=Tyrosine-protein kinase ABL1;
DE            EC=2.7.10.2;
DE   AltName: Full=Abelson murine leukemia viral oncogene homolog 1;
DE   AltName: Full=Proto-oncogene c-Abl;
DE   AltName: Full=p150;
GN   Name=Abl1; Synonyms=Abl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I).
RC   TISSUE=Testis;
RX   MEDLINE=88068561; PubMed=3317402; DOI=10.1073/pnas.84.23.8200;
RA   Oppi C., Shore S.K., Reddy E.P.;
RT   "Nucleotide sequence of testis-derived c-abl cDNAs: implications for
RT   testis-specific transcription and abl oncogene activation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:8200-8204(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
RC   STRAIN=ICR; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IV).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-187 (ISOFORMS I; II; III AND
RP   IV).
RX   MEDLINE=95394474; PubMed=7665185; DOI=10.1006/geno.1995.1008;
RA   Chissoe S.L., Bodenteich A., Wang Y.-F., Wang Y.-P., Burian D.,
RA   Clifton S.W., Crabtree J., Freeman A., Iyer K., Jian L., Ma Y.,
RA   McLaury H.-J., Pan H.-Q., Sarhan O.H., Toth S., Wang Z., Zhang G.,
RA   Heisterkamp N., Groffen J., Roe B.A.;
RT   "Sequence and analysis of the human ABL gene, the BCR gene, and
RT   regions involved in the Philadelphia chromosomal translocation.";
RL   Genomics 27:67-82(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE OF 85-182.
RX   MEDLINE=84106840; PubMed=6319018; DOI=10.1016/0092-8674(84)90228-9;
RA   Wang J.Y.J., Ledley F., Goff S., Lee R., Groner Y., Baltimore D.;
RT   "The mouse c-abl locus: molecular cloning and characterization.";
RL   Cell 36:349-356(1984).
RN   [6]
RP   ALTERNATIVE SPLICING.
RX   MEDLINE=88202920; PubMed=3283651;
RA   Bernards A., Paskind M., Baltimore D.;
RT   "Four murine c-abl mRNAs arise by usage of two transcriptional
RT   promoters and alternative splicing.";
RL   Oncogene 2:297-304(1988).
RN   [7]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=2065352; DOI=10.1016/0092-8674(91)90011-M;
RA   Tybulewicz V.L., Crawford C.E., Jackson P.K., Bronson R.T.,
RA   Mulligan R.C.;
RT   "Neonatal lethality and lymphopenia in mice with a homozygous
RT   disruption of the c-abl proto-oncogene.";
RL   Cell 65:1153-1163(1991).
RN   [8]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=2065353; DOI=10.1016/0092-8674(91)90012-N;
RA   Schwartzberg P.L., Stall A.M., Hardin J.D., Bowdish K.S., Humaran T.,
RA   Boast S., Harbison M.L., Robertson E.J., Goff S.P.;
RT   "Mice homozygous for the ablm1 mutation show poor viability and
RT   depletion of selected B and T cell populations.";
RL   Cell 65:1165-1175(1991).
RN   [9]
RP   FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
RP   SER-446, AND MUTAGENESIS OF SER-446.
RX   PubMed=9109492; DOI=10.1038/386732a0;
RA   Kharbanda S., Pandey P., Jin S., Inoue S., Bharti A., Yuan Z.-M.,
RA   Weichselbaum R., Weaver D., Kufe D.;
RT   "Functional interaction between DNA-PK and c-Abl in response to DNA
RT   damage.";
RL   Nature 386:732-735(1997).
RN   [10]
RP   SUBCELLULAR LOCATION.
RX   PubMed=9636171; DOI=10.1073/pnas.95.13.7457;
RA   Taagepera S., McDonald D., Loeb J.E., Whitaker L.L., McElroy A.K.,
RA   Wang J.Y., Hope T.J.;
RT   "Nuclear-cytoplasmic shuttling of C-ABL tyrosine kinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:7457-7462(1998).
RN   [11]
RP   IDENTIFICATION IN A TRIMOLECULAR COMPLEX WITH CDK5 AND CABLES1, AND
RP   INTERACTION WITH CABLES1.
RC   TISSUE=Brain;
RX   MEDLINE=20353055; PubMed=10896159; DOI=10.1016/S0896-6273(00)81200-3;
RA   Zukerberg L.R., Patrick G.N., Nikolic M., Humbert S., Wu C.-L.,
RA   Lanier L.M., Gertler F.B., Vidal M., Van Etten R.A., Tsai L.-H.;
RT   "Cables links Cdk5 and c-Abl and facilitates Cdk5 tyrosine
RT   phosphorylation, kinase upregulation, and neurite outgrowth.";
RL   Neuron 26:633-646(2000).
RN   [12]
RP   INTERACTION WITH PSTPIP1.
RX   PubMed=11163214; DOI=10.1016/S1097-2765(00)00138-6;
RA   Cong F., Spencer S., Cote J.F., Wu Y., Tremblay M.L., Lasky L.A.,
RA   Goff S.P.;
RT   "Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine
RT   phosphatase to the c-Abl kinase to mediate Abl dephosphorylation.";
RL   Mol. Cell 6:1413-1423(2000).
RN   [13]
RP   INTERACTION WITH CRK, AND FUNCTION.
RX   PubMed=11279004; DOI=10.1074/jbc.M100095200;
RA   Kain K.H., Klemke R.L.;
RT   "Inhibition of cell migration by Abl family tyrosine kinases through
RT   uncoupling of Crk-CAS complexes.";
RL   J. Biol. Chem. 276:16185-16192(2001).
RN   [14]
RP   INTERACTION WITH ZDHHC16.
RX   PubMed=12021275; DOI=10.1074/jbc.M202388200;
RA   Li B., Cong F., Tan C.P., Wang S.X., Goff S.P.;
RT   "Aph2, a protein with a zf-DHHC motif, interacts with c-Abl and has
RT   pro-apoptotic activity.";
RL   J. Biol. Chem. 277:28870-28876(2002).
RN   [15]
RP   FUNCTION, ENZYME REGULATION, INTERACTION WITH CRK, AUTOPHOSPHORYLATION
RP   AT TYR-226 AND TYR-393, AND MUTAGENESIS OF TYR-226; LYS-271 AND
RP   TYR-393.
RX   MEDLINE=22633749; PubMed=12748290;
RX   DOI=10.1128/MCB.23.11.3884-3896.2003;
RA   Tanis K.Q., Veach D., Duewel H.S., Bornmann W.G., Koleske A.J.;
RT   "Two distinct phosphorylation pathways have additive effects on Abl
RT   family kinase activation.";
RL   Mol. Cell. Biol. 23:3884-3896(2003).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 61-121.
RX   MEDLINE=95393198; PubMed=7664083; DOI=10.1038/nsb0894-546;
RA   Musacchio A., Saraste M., Wilmanns M.;
RT   "High-resolution crystal structures of tyrosine kinase SH3 domains
RT   complexed with proline-rich peptides.";
RL   Nat. Struct. Biol. 1:546-551(1994).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 229-515 IN COMPLEX WITH
RP   INHIBITOR STI-571, CATALYTIC ACTIVITY, ENZYME REGULATION,
RP   PHOSPHORYLATION AT TYR-393, AND ACTIVATION LOOP.
RX   MEDLINE=20446271; PubMed=10988075; DOI=10.1126/science.289.5486.1938;
RA   Schindler T., Bornmann W., Pellicena P., Miller W.T., Clarkson B.,
RA   Kuriyan J.;
RT   "Structural mechanism for STI-571 inhibition of Abelson tyrosine
RT   kinase.";
RL   Science 289:1938-1942(2000).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 229-515, MYRISTOYLATION
RP   (ISOFORM IV), AND ENZYME REGULATION.
RX   PubMed=12654251; DOI=10.1016/S0092-8674(03)00194-6;
RA   Nagar B., Hantschel O., Young M.A., Scheffzek K., Veach D.,
RA   Bornmann W., Clarkson B., Superti-Furga G., Kuriyan J.;
RT   "Structural basis for the autoinhibition of c-Abl tyrosine kinase.";
RL   Cell 112:859-871(2003).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 229-515 OF WILD-TYPE AND
RP   MUTANT ILE-315 IN COMPLEX WITH INHIBITOR PPY-A.
RX   PubMed=17718712; DOI=10.1111/j.1747-0285.2007.00556.x;
RA   Zhou T., Parillon L., Li F., Wang Y., Keats J., Lamore S., Xu Q.,
RA   Shakespeare W., Dalgarno D., Zhu X.;
RT   "Crystal structure of the T315I mutant of AbI kinase.";
RL   Chem. Biol. Drug Des. 70:171-181(2007).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 229-515 OF MUTANT ILE-315 IN
RP   COMPLEX WITH INHIBITOR AP24534, CATALYTIC ACTIVITY, AND FUNCTION.
RX   PubMed=19878872; DOI=10.1016/j.ccr.2009.09.028;
RA   O'Hare T., Shakespeare W.C., Zhu X., Eide C.A., Rivera V.M., Wang F.,
RA   Adrian L.T., Zhou T., Huang W.S., Xu Q., Metcalf C.A. III, Tyner J.W.,
RA   Loriaux M.M., Corbin A.S., Wardwell S., Ning Y., Keats J.A., Wang Y.,
RA   Sundaramoorthi R., Thomas M., Zhou D., Snodgrass J., Commodore L.,
RA   Sawyer T.K., Dalgarno D.C., Deininger M.W., Druker B.J., Clackson T.;
RT   "AP24534, a pan-BCR-ABL inhibitor for chronic myeloid leukemia,
RT   potently inhibits the T315I mutant and overcomes mutation-based
RT   resistance.";
RL   Cancer Cell 16:401-412(2009).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (1.22 ANGSTROMS) OF 115-401 IN COMPLEXES WITH
RP   INHIBITORS AP24283 AND AP24163.
RX   PubMed=19895503; DOI=10.1111/j.1747-0285.2009.00905.x;
RA   Zhou T., Commodore L., Huang W.S., Wang Y., Sawyer T.K.,
RA   Shakespeare W.C., Clackson T., Zhu X., Dalgarno D.C.;
RT   "Structural analysis of DFG-in and DFG-out dual Src-Abl inhibitors
RT   sharing a common vinyl purine template.";
RL   Chem. Biol. Drug Des. 75:18-28(2010).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 115-401 IN COMPLEX WITH
RP   INHIBITORS IMATINIB AND GNF-2, CATALYTIC ACTIVITY, ENZYME REGULATION,
RP   AUTOPHOSPHORYLATION, AND MUTAGENESIS OF PRO-112; TYR-128; TYR-139;
RP   SER-229; THR-315; CYS-464; PRO-465; PHE-497; GLU-505 AND VAL-506.
RX   PubMed=20072125; DOI=10.1038/nature08675;
RA   Zhang J., Adrian F.J., Jahnke W., Cowan-Jacob S.W., Li A.G.,
RA   Iacob R.E., Sim T., Powers J., Dierks C., Sun F., Guo G.R., Ding Q.,
RA   Okram B., Choi Y., Wojciechowski A., Deng X., Liu G., Fendrich G.,
RA   Strauss A., Vajpai N., Grzesiek S., Tuntland T., Liu Y., Bursulaya B.,
RA   Azam M., Manley P.W., Engen J.R., Daley G.Q., Warmuth M., Gray N.S.;
RT   "Targeting Bcr-Abl by combining allosteric with ATP-binding-site
RT   inhibitors.";
RL   Nature 463:501-506(2010).
CC   -!- FUNCTION: Protein kinase that regulates key processes linked to
CC       cell growth and survival. Regulates cytoskeleton remodeling during
CC       cell differentiation, cell division and cell adhesion. Localizes
CC       to dynamic actin structures, and phosphorylates CRK and CRKL,
CC       DOK1, and other proteins controlling cytoskeleton dynamics.
CC       Regulates DNA repair potentially by activating the proapoptotic
CC       pathway when the DNA damage is too severe to be repaired.
CC       Phosphorylates PSMA7 that leads to an inhibition of proteasomal
CC       activity and cell cycle transition blocks.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- COFACTOR: Magnesium or manganese.
CC   -!- ENZYME REGULATION: Stabilized in the inactive form by an
CC       association between the SH3 domain and the SH2-TK linker region,
CC       interactions of the amino-terminal cap, and contributions from an
CC       amino-terminal myristoyl group and phospholipids. Activated by
CC       autophosphorylation as well as by SRC-family kinase-mediated
CC       phosphorylation. Activated by RIN1 binding to the SH2 and SH3
CC       domains. Inhibited by imatinib mesylate (Gleevec).
CC   -!- SUBUNIT: Interacts with INPPL1/SHIP2. Interacts with SORBS1
CC       following insulin stimulation. Found in a trimolecular complex
CC       containing CDK5 and CABLES1. Interacts with CABLES1 and PSTPIP1.
CC       Interacts with ZDHHC16. Interacts with the 14-3-3 proteins, YWHAB,
CC       YWHAE, YWHAG, YWHAH, SFN AND YWHAZ; the interaction with 14-3-3
CC       proteins requires phosphorylation on Thr-734 and sequesters ABL1
CC       into the cytoplasm (By similarity). Interacts with PSMA7 (By
CC       similarity).
CC   -!- INTERACTION:
CC       P46527:CDKN1B (xeno); NbExp=1; IntAct=EBI-914519, EBI-519280;
CC       P97465:Dok1; NbExp=3; IntAct=EBI-914519, EBI-914917;
CC       Q07666:KHDRBS1 (xeno); NbExp=1; IntAct=EBI-914519, EBI-1364;
CC       Q99M51:Nck1; NbExp=1; IntAct=EBI-914519, EBI-642202;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus. Note=The
CC       myristoylated c-ABL protein is reported to be nuclear. Sequestered
CC       into the cytoplasm through interaction with 14-3-3 proteins (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=I;
CC         IsoId=P00520-1; Sequence=Displayed;
CC       Name=II;
CC         IsoId=P00520-2; Sequence=VSP_004959;
CC       Name=III;
CC         IsoId=P00520-3; Sequence=VSP_004958;
CC       Name=IV;
CC         IsoId=P00520-4; Sequence=VSP_004960;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- PTM: Phosphorylation on Thr-734 is required for binding 14-3-3
CC       proteins for cytoplasmic translocation (By similarity). DNA
CC       damage-induced activation of c-Abl requires the function of ATM
CC       and Ser-446 phosphorylation. Phosphorylated by PRKDC.
CC   -!- PTM: Isoform IV is myristoylated on Gly-2.
CC   -!- DISRUPTION PHENOTYPE: Mutants are born with the expected Mendelian
CC       frequency, but fail to thrive and most die within three weeks
CC       after birth. Most mutants are runted, and have atrophied thymuses
CC       with severe thymocyte deficiency. Mutants that survive to weaning
CC       age are most often runted, and about half of them show
CC       lymphopenia. They display a major reduction in the number of pre-B
CC       and immature B cell classes in bone marrow with a wide variation
CC       between individuals, but essentially normal mature B cell levels.
CC       Mutants are highly susceptible to infections.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. ABL subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; J02995; AAA88241.1; -; mRNA.
DR   EMBL; AK090095; BAC41088.1; -; mRNA.
DR   EMBL; BC059260; AAH59260.1; -; mRNA.
DR   EMBL; U14721; AAB60451.1; -; Genomic_DNA.
DR   EMBL; U14720; AAB60451.1; JOINED; Genomic_DNA.
DR   EMBL; U14721; AAB60450.1; -; Genomic_DNA.
DR   EMBL; U14720; AAB60450.1; JOINED; Genomic_DNA.
DR   EMBL; U14721; AAB60448.1; -; Genomic_DNA.
DR   EMBL; U13835; AAB60448.1; JOINED; Genomic_DNA.
DR   EMBL; U14721; AAB60449.1; -; Genomic_DNA.
DR   EMBL; U13835; AAB60449.1; JOINED; Genomic_DNA.
DR   EMBL; X07539; CAA30411.1; -; Genomic_DNA.
DR   EMBL; X07539; CAA30412.1; -; Genomic_DNA.
DR   EMBL; X07540; CAA30413.1; -; Genomic_DNA.
DR   EMBL; X07541; CAA30414.1; -; Genomic_DNA.
DR   EMBL; M12263; AAA37136.1; -; mRNA.
DR   EMBL; M12264; AAA37137.1; -; mRNA.
DR   EMBL; M12265; AAA37138.1; -; mRNA.
DR   EMBL; M12266; AAA37134.1; -; Genomic_DNA.
DR   EMBL; K03228; AAA37135.1; -; mRNA.
DR   IPI; IPI00227806; -.
DR   IPI; IPI00227807; -.
DR   IPI; IPI00314762; -.
DR   IPI; IPI00453940; -.
DR   PIR; A39962; A39962.
DR   PIR; S00774; S00774.
DR   RefSeq; NP_001106174.1; NM_001112703.1.
DR   RefSeq; NP_033724.2; NM_009594.3.
DR   UniGene; Mm.1318; -.
DR   PDB; 1ABO; X-ray; 2.00 A; A/B=61-121.
DR   PDB; 1ABQ; X-ray; 2.80 A; A=61-121.
DR   PDB; 1FPU; X-ray; 2.40 A; A/B=229-515.
DR   PDB; 1IEP; X-ray; 2.10 A; A/B=229-515.
DR   PDB; 1M52; X-ray; 2.60 A; A/B=229-515.
DR   PDB; 1OPJ; X-ray; 1.75 A; A/B=229-515.
DR   PDB; 1OPK; X-ray; 1.80 A; A=27-515.
DR   PDB; 2HZN; X-ray; 2.70 A; A=229-515.
DR   PDB; 2QOH; X-ray; 1.95 A; A/B=229-515.
DR   PDB; 2Z60; X-ray; 1.95 A; A=229-515.
DR   PDB; 3DK3; X-ray; 2.02 A; A/B=233-514.
DR   PDB; 3DK6; X-ray; 2.02 A; A/B=233-514.
DR   PDB; 3DK7; X-ray; 2.01 A; A/B=233-505.
DR   PDB; 3IK3; X-ray; 1.90 A; A/B=229-515.
DR   PDB; 3K5V; X-ray; 1.74 A; A/B=229-510.
DR   PDB; 3KF4; X-ray; 1.90 A; A/B=229-515.
DR   PDB; 3KFA; X-ray; 1.22 A; A/B=229-515.
DR   PDB; 3MS9; X-ray; 1.80 A; A/B=229-515.
DR   PDB; 3MSS; X-ray; 1.95 A; A/B/C/D=229-515.
DR   PDB; 3OXZ; X-ray; 2.20 A; A=229-511.
DR   PDB; 3OY3; X-ray; 1.95 A; A/B=229-511.
DR   PDBsum; 1ABO; -.
DR   PDBsum; 1ABQ; -.
DR   PDBsum; 1FPU; -.
DR   PDBsum; 1IEP; -.
DR   PDBsum; 1M52; -.
DR   PDBsum; 1OPJ; -.
DR   PDBsum; 1OPK; -.
DR   PDBsum; 2HZN; -.
DR   PDBsum; 2QOH; -.
DR   PDBsum; 2Z60; -.
DR   PDBsum; 3DK3; -.
DR   PDBsum; 3DK6; -.
DR   PDBsum; 3DK7; -.
DR   PDBsum; 3IK3; -.
DR   PDBsum; 3K5V; -.
DR   PDBsum; 3KF4; -.
DR   PDBsum; 3KFA; -.
DR   PDBsum; 3MS9; -.
DR   PDBsum; 3MSS; -.
DR   PDBsum; 3OXZ; -.
DR   PDBsum; 3OY3; -.
DR   ProteinModelPortal; P00520; -.
DR   SMR; P00520; 46-511, 1017-1123.
DR   IntAct; P00520; 11.
DR   MINT; MINT-85127; -.
DR   STRING; P00520; -.
DR   PhosphoSite; P00520; -.
DR   PRIDE; P00520; -.
DR   Ensembl; ENSMUST00000028190; ENSMUSP00000028190; ENSMUSG00000026842.
DR   Ensembl; ENSMUST00000075759; ENSMUSP00000075167; ENSMUSG00000026842.
DR   Ensembl; ENSMUST00000113454; ENSMUSP00000109081; ENSMUSG00000026842.
DR   Ensembl; ENSMUST00000113455; ENSMUSP00000109082; ENSMUSG00000026842.
DR   GeneID; 11350; -.
DR   KEGG; mmu:11350; -.
DR   UCSC; uc008jdz.1; mouse.
DR   UCSC; uc008jea.1; mouse.
DR   UCSC; uc008jec.1; mouse.
DR   CTD; 11350; -.
DR   MGI; MGI:87859; Abl1.
DR   HOVERGEN; HBG004162; -.
DR   OMA; GAFRESG; -.
DR   OrthoDB; EOG40P460; -.
DR   BRENDA; 2.7.10.2; 244.
DR   NextBio; 278620; -.
DR   ArrayExpress; P00520; -.
DR   Bgee; P00520; -.
DR   CleanEx; MM_ABL1; -.
DR   Genevestigator; P00520; -.
DR   GermOnline; ENSMUSG00000026842; Mus musculus.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:EC.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IDA:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR   GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
DR   InterPro; IPR015015; F-actin_binding.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF08919; F_actin_bind; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00808; FABD; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Cell adhesion;
KW   Chromosomal rearrangement; Cytoplasm; Cytoskeleton; Kinase;
KW   Lipoprotein; Magnesium; Manganese; Metal-binding; Myristate;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Proto-oncogene;
KW   SH2 domain; SH3 domain; Transferase.
FT   CHAIN         1   1123       Tyrosine-protein kinase ABL1.
FT                                /FTId=PRO_0000088051.
FT   DOMAIN       61    121       SH3.
FT   DOMAIN      127    217       SH2.
FT   DOMAIN      242    493       Protein kinase.
FT   NP_BIND     248    256       ATP (Probable).
FT   NP_BIND     316    322       ATP (Probable).
FT   REGION        1     60       CAP.
FT   MOTIF       381    405       Kinase activation loop.
FT   MOTIF       605    609       Nuclear localization signal (Potential).
FT   COMPBIAS     18     22       Poly-Ser.
FT   COMPBIAS    605    609       Poly-Lys.
FT   COMPBIAS    804   1012       Pro-rich.
FT   COMPBIAS    891    897       Poly-Pro.
FT   ACT_SITE    363    363       Proton acceptor (By similarity).
FT   BINDING     271    271       ATP (By similarity).
FT   MOD_RES      50     50       Phosphoserine (By similarity).
FT   MOD_RES     185    185       Phosphotyrosine (By similarity).
FT   MOD_RES     226    226       Phosphotyrosine (By similarity).
FT   MOD_RES     253    253       Phosphotyrosine (By similarity).
FT   MOD_RES     257    257       Phosphotyrosine (By similarity).
FT   MOD_RES     264    264       Phosphotyrosine (By similarity).
FT   MOD_RES     392    392       Phosphothreonine (By similarity).
FT   MOD_RES     393    393       Phosphotyrosine; by autocatalysis and
FT                                SRC-type Tyr-kinases.
FT   MOD_RES     394    394       Phosphothreonine (By similarity).
FT   MOD_RES     446    446       Phosphoserine.
FT   MOD_RES     469    469       Phosphotyrosine (By similarity).
FT   MOD_RES     569    569       Phosphoserine (By similarity).
FT   MOD_RES     613    613       Phosphothreonine (By similarity).
FT   MOD_RES     620    620       Phosphoserine (By similarity).
FT   MOD_RES     658    658       Phosphoserine (By similarity).
FT   MOD_RES     682    682       Phosphoserine (By similarity).
FT   MOD_RES     717    717       Phosphoserine (By similarity).
FT   MOD_RES     734    734       Phosphothreonine (By similarity).
FT   MOD_RES     803    803       Phosphoserine (By similarity).
FT   MOD_RES     807    807       Phosphoserine (By similarity).
FT   MOD_RES     812    812       Phosphothreonine (By similarity).
FT   MOD_RES     844    844       Phosphothreonine (By similarity).
FT   MOD_RES     909    909       Phosphoserine (By similarity).
FT   MOD_RES     911    911       Phosphoserine (By similarity).
FT   MOD_RES     927    927       Phosphoserine (By similarity).
FT   MOD_RES     970    970       Phosphoserine (By similarity).
FT   VAR_SEQ       1     26       MLEICLKLVGCKSKKGLSSSSSCYLE -> MISFDLLSDEL
FT                                HLKLLVLDV (in isoform II).
FT                                /FTId=VSP_004959.
FT   VAR_SEQ       1     26       MLEICLKLVGCKSKKGLSSSSSCYLE -> MSQRWTYTKCR
FT                                VQRDPALPFM (in isoform III).
FT                                /FTId=VSP_004958.
FT   VAR_SEQ       1     26       MLEICLKLVGCKSKKGLSSSSSCYLE -> MGQQPGKVLGD
FT                                QRRPSLPALHFIKGAGKRDSSRHGGPHCNVFVEH (in
FT                                isoform IV).
FT                                /FTId=VSP_004960.
FT   MUTAGEN     112    112       P->S: Strongly reduced inhibition by GNF-
FT                                2.
FT   MUTAGEN     128    128       Y->D: Strongly reduced inhibition by GNF-
FT                                2.
FT   MUTAGEN     139    139       Y->C: Strongly reduced inhibition by GNF-
FT                                2.
FT   MUTAGEN     226    226       Y->F: Minimal reduction in ability to
FT                                autophosphorylate.
FT   MUTAGEN     229    229       S->P: Strongly reduced inhibition by GNF-
FT                                2.
FT   MUTAGEN     271    271       K->M: Loss of kinase activity.
FT   MUTAGEN     315    315       T->I: Loss of inhibition by imatinib.
FT                                Loss of inhibition by GNF-2.
FT   MUTAGEN     393    393       Y->F: Minimal reduction in ability to
FT                                autophosphorylate.
FT   MUTAGEN     446    446       S->A: No effect on basal activity, but
FT                                abolishes ionizing radiation-induced
FT                                activation.
FT   MUTAGEN     464    464       C->Y: Loss of inhibition by GNF-2.
FT   MUTAGEN     465    465       P->S: Loss of inhibition by GNF-2.
FT   MUTAGEN     497    497       F->L: Strongly reduced inhibition by GNF-
FT                                2.
FT   MUTAGEN     505    505       E->K: Loss of inhibition by GNF-2.
FT   MUTAGEN     506    506       V->L: Strongly reduced inhibition by GNF-
FT                                2.
FT   MUTAGEN    1083   1083       L->A: Loss of nuclear export.
FT   CONFLICT    184    187       LYVS -> VGDW (in Ref. 4; AAB60451/
FT                                AAB60450).
FT   CONFLICT    782    786       PPRLV -> LPGWL (in Ref. 1; AAA88241).
FT   CONFLICT    987    987       D -> G (in Ref. 2; BAC41088).
FT   STRAND       65     70
FT   STRAND       87     93
FT   STRAND       97    104
FT   STRAND      107    112
FT   HELIX       113    115
FT   STRAND      116    118
FT   HELIX       122    124
FT   STRAND      128    131
FT   HELIX       134    140
FT   HELIX       141    143
FT   STRAND      148    153
FT   STRAND      155    157
FT   STRAND      161    167
FT   STRAND      170    175
FT   STRAND      184    187
FT   STRAND      192    194
FT   HELIX       195    202
FT   STRAND      209    211
FT   HELIX       239    241
FT   STRAND      242    247
FT   TURN        249    252
FT   STRAND      254    261
FT   HELIX       262    264
FT   STRAND      267    275
FT   TURN        277    279
FT   HELIX       280    291
FT   STRAND      301    305
FT   STRAND      307    316
FT   HELIX       323    329
FT   TURN        332    334
FT   HELIX       337    356
FT   HELIX       366    368
FT   STRAND      369    371
FT   HELIX       373    375
FT   STRAND      377    379
FT   HELIX       384    386
FT   STRAND      390    396
FT   STRAND      399    401
FT   HELIX       403    405
FT   HELIX       408    412
FT   HELIX       418    433
FT   HELIX       445    447
FT   HELIX       448    453
FT   HELIX       466    475
FT   HELIX       480    482
FT   HELIX       486    496
FT   HELIX       502    509
SQ   SEQUENCE   1123 AA;  122673 MW;  BD48ADE8557AE95C CRC64;
     MLEICLKLVG CKSKKGLSSS SSCYLEEALQ RPVASDFEPQ GLSEAARWNS KENLLAGPSE
     NDPNLFVALY DFVASGDNTL SITKGEKLRV LGYNHNGEWC EAQTKNGQGW VPSNYITPVN
     SLEKHSWYHG PVSRNAAEYL LSSGINGSFL VRESESSPGQ RSISLRYEGR VYHYRINTAS
     DGKLYVSSES RFNTLAELVH HHSTVADGLI TTLHYPAPKR NKPTIYGVSP NYDKWEMERT
     DITMKHKLGG GQYGEVYEGV WKKYSLTVAV KTLKEDTMEV EEFLKEAAVM KEIKHPNLVQ
     LLGVCTREPP FYIITEFMTY GNLLDYLREC NRQEVSAVVL LYMATQISSA MEYLEKKNFI
     HRDLAARNCL VGENHLVKVA DFGLSRLMTG DTYTAHAGAK FPIKWTAPES LAYNKFSIKS
     DVWAFGVLLW EIATYGMSPY PGIDLSQVYE LLEKDYRMER PEGCPEKVYE LMRACWQWNP
     SDRPSFAEIH QAFETMFQES SISDEVEKEL GKRGTRGGAG SMLQAPELPT KTRTCRRAAE
     QKDAPDTPEL LHTKGLGESD ALDSEPAVSP LLPRKERGPP DGSLNEDERL LPRDRKTNLF
     SALIKKKKKM APTPPKRSSS FREMDGQPDR RGASEDDSRE LCNGPPALTS DAAEPTKSPK
     ASNGAGVPNG AFREPGNSGF RSPHMWKKSS TLTGSRLAAA EEESGMSSSK RFLRSCSASC
     MPHGARDTEW RSVTLPRDLP SAGKQFDSST FGGHKSEKPA LPRKRTSESR SEQVAKSTAM
     PPPRLVKKNE EAAEEGFKDT ESSPGSSPPS LTPKLLRRQV TASPSSGLSH KEEATKGSAS
     GMGTPATAEP APPSNKVGLS KASSEEMRVR RHKHSSESPG RDKGRLAKLK PAPPPPPACT
     GKAGKPAQSP SQEAGEAGGP TKTKCTSLAM DAVNTDPTKA GPPGEGLRKP VPPSVPKPQS
     TAKPPGTPTS PVSTPSTAPA PSPLAGDQQP SSAAFIPLIS TRVSLRKTRQ PPERIASGTI
     TKGVVLDSTE ALCLAISRNS EQMASHSAVL EAGKNLYTFC VSYVDSIQQM RNKFAFREAI
     NKLESNLREL QICPATASSG PAATQDFSKL LSSVKEISDI VRR
//
ID   THY1_MOUSE              Reviewed;         162 AA.
AC   P01831;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   08-MAR-2011, entry version 108.
DE   RecName: Full=Thy-1 membrane glycoprotein;
DE   AltName: Full=Thy-1 antigen;
DE   AltName: CD_antigen=CD90;
DE   Flags: Precursor;
GN   Name=Thy1; Synonyms=Thy-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=85115360; PubMed=2857501; DOI=10.1126/science.2857501;
RA   Seki T., Chang H.-C., Moriuchi T., Denome R., Ploegh H., Silver J.;
RT   "A hydrophobic transmembrane segment at the carboxyl terminus of thy-
RT   1.";
RL   Science 227:649-651(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (THY-1.2 ALLOTYPE).
RC   STRAIN=BALB/c;
RX   MEDLINE=86055760; PubMed=2866091;
RA   Giguere V., Isobe K., Grosveld F.;
RT   "Structure of the murine Thy-1 gene.";
RL   EMBO J. 4:2017-2024(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (THY-1.2 ALLOTYPE).
RX   MEDLINE=85216583; PubMed=2582427; DOI=10.1073/pnas.82.11.3819;
RA   Chang H.-C., Seki T., Moriuchi T., Silver J.;
RT   "Isolation and characterization of mouse Thy-1 genomic clones.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:3819-3823(1985).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (THY-1.2 ALLOTYPE).
RX   MEDLINE=86113437; PubMed=2868059;
RA   Ingraham H.A., Lawless G.M., Evans G.A.;
RT   "The mouse Thy-1.2 glycoprotein gene: complete sequence and
RT   identification of an unusual promoter.";
RL   J. Immunol. 136:1482-1489(1986).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 20-131, PYROGLUTAMATE FORMATION AT GLN-20, AND
RP   GPI-ANCHOR AT CYS-131.
RX   MEDLINE=82199396; PubMed=6177036; DOI=10.1126/science.6177036;
RA   Williams A.F., Gagnon J.;
RT   "Neuronal cell Thy-1 glycoprotein: homology with immunoglobulin.";
RL   Science 216:696-703(1982).
CC   -!- FUNCTION: May play a role in cell-cell or cell-ligand interactions
CC       during synaptogenesis and other events in the brain.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC   -!- POLYMORPHISM: There are two major alleles; Thy-1.1 (CD90.1) and
CC       Thy-1.2 (CD90.2).
CC   -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC       domain.
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DR   EMBL; X03151; CAA26930.1; -; Genomic_DNA.
DR   EMBL; X02771; CAA26548.1; -; Genomic_DNA.
DR   EMBL; X02772; CAA26549.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X02773; CAA26550.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; M10246; AAA40440.1; -; Genomic_DNA.
DR   EMBL; M11160; AAA40441.1; -; Genomic_DNA.
DR   EMBL; M12379; AAA40443.1; -; Genomic_DNA.
DR   EMBL; BC054436; AAH54436.1; -; mRNA.
DR   IPI; IPI00109727; -.
DR   PIR; A94278; TDMS.
DR   RefSeq; NP_033408.1; NM_009382.3.
DR   UniGene; Mm.3951; -.
DR   ProteinModelPortal; P01831; -.
DR   SMR; P01831; 28-111.
DR   STRING; P01831; -.
DR   PRIDE; P01831; -.
DR   Ensembl; ENSMUST00000034509; ENSMUSP00000034509; ENSMUSG00000032011.
DR   Ensembl; ENSMUST00000114840; ENSMUSP00000110489; ENSMUSG00000032011.
DR   GeneID; 21838; -.
DR   KEGG; mmu:21838; -.
DR   UCSC; uc009pbl.1; mouse.
DR   CTD; 21838; -.
DR   MGI; MGI:98747; Thy1.
DR   eggNOG; roNOG17327; -.
DR   HOGENOM; HBG279081; -.
DR   HOVERGEN; HBG002958; -.
DR   InParanoid; P01831; -.
DR   OMA; TCELRLS; -.
DR   OrthoDB; EOG4SF977; -.
DR   PhylomeDB; P01831; -.
DR   NextBio; 301298; -.
DR   ArrayExpress; P01831; -.
DR   Bgee; P01831; -.
DR   CleanEx; MM_THY1; -.
DR   Genevestigator; P01831; -.
DR   GermOnline; ENSMUSG00000032011; Mus musculus.
DR   GO; GO:0031362; C:anchored to external side of plasma membrane; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR   GO; GO:0045121; C:membrane raft; IDA:MGI.
DR   GO; GO:0034235; F:GPI anchor binding; ISS:UniProtKB.
DR   GO; GO:0005100; F:Rho GTPase activator activity; ISS:UniProtKB.
DR   GO; GO:0001525; P:angiogenesis; IDA:UniProtKB.
DR   GO; GO:0016337; P:cell-cell adhesion; ISS:UniProtKB.
DR   GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0048041; P:focal adhesion assembly; ISS:UniProtKB.
DR   GO; GO:0050771; P:negative regulation of axonogenesis; ISS:UniProtKB.
DR   GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR   GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISS:UniProtKB.
DR   GO; GO:0050870; P:positive regulation of T cell activation; ISS:UniProtKB.
DR   GO; GO:0046549; P:retinal cone cell development; IMP:UniProtKB.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003596; Ig_V-set_sub.
DR   InterPro; IPR013151; Immunoglobulin.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF00047; ig; 1.
DR   SMART; SM00406; IGv; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; GPI-anchor; Immunoglobulin domain; Lipoprotein;
KW   Membrane; Polymorphism; Pyrrolidone carboxylic acid; Signal.
FT   SIGNAL        1     19
FT   CHAIN        20    131       Thy-1 membrane glycoprotein.
FT                                /FTId=PRO_0000014977.
FT   PROPEP      132    162       Removed in mature form.
FT                                /FTId=PRO_0000014978.
FT   DOMAIN       20    127       Ig-like V-type.
FT   MOD_RES      20     20       Pyrrolidone carboxylic acid.
FT   LIPID       131    131       GPI-anchor amidated cysteine.
FT   CARBOHYD     42     42       N-linked (GlcNAc...).
FT   CARBOHYD     94     94       N-linked (GlcNAc...).
FT   CARBOHYD    118    118       N-linked (GlcNAc...).
FT   DISULFID     28    131
FT   DISULFID     38    105
FT   VARIANT     108    108       Q -> R (in allele Thy-1.1).
SQ   SEQUENCE   162 AA;  18080 MW;  397BF7D3A9F2C77B CRC64;
     MNPAISVALL LSVLQVSRGQ KVTSLTACLV NQNLRLDCRH ENNTKDNSIQ HEFSLTREKR
     KHVLSGTLGI PEHTYRSRVT LSNQPYIKVL TLANFTTKDE GDYFCELQVS GANPMSSNKS
     ISVYRDKLVK CGGISLLVQN TSWMLLLLLS LSLLQALDFI SL
//
ID   HBB1_MOUSE              Reviewed;         147 AA.
AC   P02088; Q54AI0; Q91V86; Q9CRZ2; Q9CXH5; Q9CY12; Q9CY54; Q9R0S6;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 120.
DE   RecName: Full=Hemoglobin subunit beta-1;
DE   AltName: Full=Beta-1-globin;
DE   AltName: Full=Hemoglobin beta-1 chain;
DE   AltName: Full=Hemoglobin beta-major chain;
GN   Name=Hbb-b1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=89178643; PubMed=2926808; DOI=10.1016/0022-2836(89)90363-X;
RA   Shehee W.R., Loeb D.D., Adey N.B., Burton F.H., Casavant N.C.,
RA   Cole P., Davies C.J., McGraw R.A., Schichman S.A., Severynse D.M.,
RA   Voliva C.F., Weyter F.W., Wisely G.B., Edgell M.H.,
RA   Hutchison C.A. III;
RT   "Nucleotide sequence of the BALB/c mouse beta-globin complex.";
RL   J. Mol. Biol. 205:41-62(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=80090038; PubMed=519759; DOI=10.1016/0092-8674(79)90138-7;
RA   Konkel D.A., Maizel J.V. Jr., Leder P.;
RT   "The evolution and sequence comparison of two recently diverged mouse
RT   chromosomal beta-globin genes.";
RL   Cell 18:865-873(1979).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=80014491; PubMed=482942; DOI=10.1126/science.482942;
RA   van Ooyen A., van den Berg J., Mantei N., Weissmann C.;
RT   "Comparison of total sequence of a cloned rabbit beta-globin gene and
RT   its flanking regions with a homologous mouse sequence.";
RL   Science 206:337-344(1979).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE S).
RC   STRAIN=C57BL/10;
RX   MEDLINE=88216120; PubMed=3870864;
RA   Erhart M.A., Simons K.S., Weaver S.;
RT   "Evolution of the mouse beta-globin genes: a recent gene conversion in
RT   the Hbbs haplotype.";
RL   Mol. Biol. Evol. 2:304-320(1985).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ALLELES P AND W1).
RX   MEDLINE=99373250; PubMed=10441738; DOI=10.1007/s003359901107;
RA   Ueda Y., Miyashita N., Imai K., Yamaguchi Y., Takamura K.,
RA   Notohara M., Shiroishi T., Kawashima T., Ning L., Wang C., Wu X.,
RA   Moriwaki K.;
RT   "Nucleotide sequences of the mouse globin beta gene cDNAs in a wild
RT   derived new haplotype Hbb(w1).";
RL   Mamm. Genome 10:879-882(1999).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Head, Heart, Kidney, Liver, Placenta, Spleen, Stomach, and
RC   Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [7]
RP   PROTEIN SEQUENCE OF 19-41; 32-60 AND 67-145, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 86-109.
RX   MEDLINE=78237863; PubMed=277329;
RA   Curtis P.J., Mantei N., Weissmann C.;
RT   "Characterization and kinetics of synthesis of 15S beta-globin RNA, a
RT   putative precursor of beta-globin mRNA.";
RL   Cold Spring Harb. Symp. Quant. Biol. 42:971-984(1978).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 28-44 AND 100-115.
RX   MEDLINE=79114395; PubMed=264241; DOI=10.1038/276037a0;
RA   van den Berg J., van Ooyen A., Mantei N., Schamboeck A., Grosveld G.,
RA   Flavell R.A., Weissmann C.;
RT   "Comparison of cloned rabbit and mouse beta-globin genes showing
RT   strong evolutionary divergence of two homologous pairs of introns.";
RL   Nature 276:37-44(1978).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 94-105.
RX   MEDLINE=78137024; PubMed=273235; DOI=10.1073/pnas.75.2.725;
RA   Tilghman S.M., Tiemeier D.C., Seidman J.G., Peterlin B.M.,
RA   Sullivan M., Maizel J.V. Jr., Leder P.;
RT   "Intervening sequence of DNA identified in the structural portion of a
RT   mouse beta-globin gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 75:725-729(1978).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-81, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX   PubMed=11747442; DOI=10.1021/bi011329f;
RA   Kidd R.D., Russell J.E., Watmough N.J., Baker E.N., Brittain T.;
RT   "The role of beta chains in the control of the hemoglobin oxygen
RT   binding function: chimeric human/mouse proteins, structure, and
RT   function.";
RL   Biochemistry 40:15669-15675(2001).
RN   [15]
RP   VARIANTS ALLELIC.
RX   MEDLINE=77065139; PubMed=999642;
RA   Gilman J.G.;
RT   "Mouse haemoglobin beta chains. Comparative sequence data on adult
RT   major and minor beta chains from two species, Mus musculus and Mus
RT   cervicolor.";
RL   Biochem. J. 159:43-53(1976).
CC   -!- FUNCTION: Involved in oxygen transport from the lung to the
CC       various peripheral tissues.
CC   -!- SUBUNIT: Heterotetramer of two alpha chains and two beta chains.
CC   -!- TISSUE SPECIFICITY: Red blood cells.
CC   -!- POLYMORPHISM: Inbred mouse strains possess 1 of 4 alleles at the
CC       HBB locus: D (diffuse), S (single), P and W1. The D and P alleles
CC       are actually closely linked doublets that coordinately express a
CC       major and a minor chain, the minor chain being slightly different
CC       in the two alleles. The S allele produces only 1 chain, it is
CC       characteristic of North American wild mice. The W1 allele is
CC       observed mainly in Northwestern China.
CC   -!- MISCELLANEOUS: The D-major sequence is shown. See also the entry
CC       for the beta D and P-minor chain.
CC   -!- SIMILARITY: Belongs to the globin family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; X14061; CAA32224.1; -; Genomic_DNA.
DR   EMBL; J00413; AAA37791.1; -; Genomic_DNA.
DR   EMBL; AB020013; BAA77353.1; -; mRNA.
DR   EMBL; AB020015; BAA77355.1; -; mRNA.
DR   EMBL; AK002258; BAB21971.1; -; mRNA.
DR   EMBL; AK002394; BAB22067.1; -; mRNA.
DR   EMBL; AK003096; BAB22562.1; -; mRNA.
DR   EMBL; AK003472; BAB22806.1; -; mRNA.
DR   EMBL; AK005442; BAB24036.1; -; mRNA.
DR   EMBL; AK005490; BAB24075.1; -; mRNA.
DR   EMBL; AK005496; BAB24080.1; -; mRNA.
DR   EMBL; AK010873; BAB27237.1; -; mRNA.
DR   EMBL; AK010902; BAB27255.1; -; mRNA.
DR   EMBL; AK010980; BAB27302.1; -; mRNA.
DR   EMBL; AK010981; BAB27303.1; -; mRNA.
DR   EMBL; AK010991; BAB27310.1; -; mRNA.
DR   EMBL; AK010993; BAB27312.1; -; mRNA.
DR   EMBL; AK011006; BAB27325.1; -; mRNA.
DR   EMBL; AK011013; BAB27331.1; -; mRNA.
DR   EMBL; AK011016; BAB27334.1; -; mRNA.
DR   EMBL; AK011027; BAB27343.1; -; mRNA.
DR   EMBL; AK011033; BAB27347.1; -; mRNA.
DR   EMBL; AK011050; BAB27360.1; -; mRNA.
DR   EMBL; AK011052; BAB27361.1; -; mRNA.
DR   EMBL; AK011053; BAB27362.1; -; mRNA.
DR   EMBL; AK011057; BAB27365.1; -; mRNA.
DR   EMBL; AK011067; BAB27374.1; -; mRNA.
DR   EMBL; AK011069; BAB27376.1; -; mRNA.
DR   EMBL; AK011075; BAB27380.1; -; mRNA.
DR   EMBL; AK011077; BAB27382.1; -; mRNA.
DR   EMBL; AK011083; BAB27387.1; -; mRNA.
DR   EMBL; AK011102; BAB27399.1; -; mRNA.
DR   EMBL; AK012551; BAB28311.1; -; mRNA.
DR   EMBL; AK014364; BAB29299.1; -; mRNA.
DR   EMBL; AK027903; BAC25655.1; -; mRNA.
DR   EMBL; AK027904; BAC25656.1; -; mRNA.
DR   EMBL; AK028067; BAC25734.1; -; mRNA.
DR   EMBL; AK088149; BAC40173.1; -; mRNA.
DR   EMBL; AK133714; BAE21794.1; -; mRNA.
DR   EMBL; AK147001; BAE27598.1; -; mRNA.
DR   EMBL; AK160629; BAE35926.1; -; mRNA.
DR   EMBL; AK161021; BAE36152.1; -; mRNA.
DR   EMBL; AK165490; BAE38217.1; -; mRNA.
DR   EMBL; AK167615; BAE39668.1; -; mRNA.
DR   EMBL; AK168412; BAE40327.1; -; mRNA.
DR   EMBL; AK168477; BAE40366.1; -; mRNA.
DR   EMBL; AK168562; BAE40435.1; -; mRNA.
DR   EMBL; AK168584; BAE40453.1; -; mRNA.
DR   EMBL; AK168819; BAE40646.1; -; mRNA.
DR   EMBL; AK168826; BAE40653.1; -; mRNA.
DR   EMBL; AK168846; BAE40669.1; -; mRNA.
DR   EMBL; M19236; AAA37788.1; -; mRNA.
DR   EMBL; M10828; AAA37786.1; -; Genomic_DNA.
DR   EMBL; M10830; AAA37787.1; -; Genomic_DNA.
DR   EMBL; M10829; AAA37787.1; JOINED; Genomic_DNA.
DR   EMBL; M10688; AAA37790.1; -; Genomic_DNA.
DR   IPI; IPI00553333; -.
DR   PIR; A90790; HBMS.
DR   RefSeq; NP_032246.2; NM_008220.4.
DR   RefSeq; XP_003084761.1; XM_003084713.1.
DR   RefSeq; XP_003084762.1; XM_003084714.1.
DR   RefSeq; XP_003084763.1; XM_003084715.1.
DR   RefSeq; XP_003084764.1; XM_003084716.1.
DR   RefSeq; XP_003085430.1; XM_003085382.1.
DR   RefSeq; XP_003085431.1; XM_003085383.1.
DR   RefSeq; XP_003085432.1; XM_003085384.1.
DR   RefSeq; XP_003085433.1; XM_003085385.1.
DR   RefSeq; XP_003086668.1; XM_003086620.1.
DR   RefSeq; XP_003086669.1; XM_003086621.1.
DR   RefSeq; XP_003086670.1; XM_003086622.1.
DR   RefSeq; XP_003086671.1; XM_003086623.1.
DR   UniGene; Mm.288567; -.
DR   PDB; 1JEB; X-ray; 2.10 A; B/D=2-147.
DR   PDB; 3HRW; X-ray; 2.80 A; B/D=2-147.
DR   PDBsum; 1JEB; -.
DR   PDBsum; 3HRW; -.
DR   ProteinModelPortal; P02088; -.
DR   SMR; P02088; 2-147.
DR   STRING; P02088; -.
DR   PhosphoSite; P02088; -.
DR   SWISS-2DPAGE; P02088; -.
DR   REPRODUCTION-2DPAGE; IPI00553333; -.
DR   REPRODUCTION-2DPAGE; P02088; -.
DR   PRIDE; P02088; -.
DR   Ensembl; ENSMUST00000023934; ENSMUSP00000023934; ENSMUSG00000052305.
DR   Ensembl; ENSMUST00000098192; ENSMUSP00000095794; ENSMUSG00000073940.
DR   GeneID; 100503164; -.
DR   GeneID; 100503605; -.
DR   GeneID; 15129; -.
DR   KEGG; mmu:100503164; -.
DR   KEGG; mmu:100503605; -.
DR   KEGG; mmu:15129; -.
DR   CTD; 15129; -.
DR   MGI; MGI:96021; Hbb-b1.
DR   eggNOG; roNOG15646; -.
DR   HOVERGEN; HBG009709; -.
DR   InParanoid; P02088; -.
DR   OrthoDB; EOG4THVVF; -.
DR   NextBio; 287582; -.
DR   Bgee; P02088; -.
DR   CleanEx; MM_HBB-B1; -.
DR   Genevestigator; P02088; -.
DR   GermOnline; ENSMUSG00000052305; Mus musculus.
DR   GO; GO:0005833; C:hemoglobin complex; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0005344; F:oxygen transporter activity; IEA:UniProtKB-KW.
DR   InterPro; IPR012292; Globin.
DR   InterPro; IPR009050; Globin-like.
DR   InterPro; IPR000971; Globin_subset.
DR   InterPro; IPR002337; Haemoglobin_b.
DR   Gene3D; G3DSA:1.10.490.10; Globin_related; 1.
DR   Pfam; PF00042; Globin; 1.
DR   PRINTS; PR00814; BETAHAEM.
DR   SUPFAM; SSF46458; Globin_like; 1.
DR   PROSITE; PS01033; GLOBIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Heme; Iron; Metal-binding;
KW   Oxygen transport; Phosphoprotein; Polymorphism; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    147       Hemoglobin subunit beta-1.
FT                                /FTId=PRO_0000053024.
FT   METAL        64     64       Iron (heme distal ligand).
FT   METAL        93     93       Iron (heme proximal ligand).
FT   MOD_RES      45     45       Phosphoserine.
FT   MOD_RES      81     81       Phosphoserine.
FT   VARIANT      14     14       C -> G (in allele S and allele W1).
FT   VARIANT      21     21       S -> A (in allele S).
FT   VARIANT      74     74       D -> E (in allele W1).
FT   VARIANT     135    135       V -> M (in allele W1).
FT   VARIANT     140    140       T -> A (in allele S).
FT   CONFLICT     15     15       L -> Q (in Ref. 6; BAB27362).
FT   CONFLICT     39     39       T -> A (in Ref. 6; BAB29299).
FT   CONFLICT     63     63       A -> T (in Ref. 6; BAB27237).
FT   CONFLICT     91     91       E -> Q (in Ref. 3).
FT   CONFLICT    109    109       N -> S (in Ref. 6; BAB29299).
FT   HELIX         6     18
FT   HELIX        21     35
FT   HELIX        37     42
FT   HELIX        52     56
FT   HELIX        59     77
FT   HELIX        82     94
FT   TURN         95     97
FT   HELIX       102    119
FT   HELIX       120    122
FT   HELIX       125    143
SQ   SEQUENCE   147 AA;  15840 MW;  8190EAEEFD9036A3 CRC64;
     MVHLTDAEKA AVSCLWGKVN SDEVGGEALG RLLVVYPWTQ RYFDSFGDLS SASAIMGNAK
     VKAHGKKVIT AFNDGLNHLD SLKGTFASLS ELHCDKLHVD PENFRLLGNM IVIVLGHHLG
     KDFTPAAQAA FQKVVAGVAT ALAHKYH
//
ID   LAMC1_MOUSE             Reviewed;        1607 AA.
AC   P02468;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 2.
DT   08-MAR-2011, entry version 121.
DE   RecName: Full=Laminin subunit gamma-1;
DE   AltName: Full=Laminin B2 chain;
DE   AltName: Full=Laminin-1 subunit gamma;
DE   AltName: Full=Laminin-10 subunit gamma;
DE   AltName: Full=Laminin-11 subunit gamma;
DE   AltName: Full=Laminin-2 subunit gamma;
DE   AltName: Full=Laminin-3 subunit gamma;
DE   AltName: Full=Laminin-4 subunit gamma;
DE   AltName: Full=Laminin-6 subunit gamma;
DE   AltName: Full=Laminin-7 subunit gamma;
DE   AltName: Full=Laminin-8 subunit gamma;
DE   AltName: Full=Laminin-9 subunit gamma;
DE   AltName: Full=S-laminin subunit gamma;
DE            Short=S-LAM gamma;
DE   Flags: Precursor;
GN   Name=Lamc1; Synonyms=Lamb-2, Lamc-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=88059118; PubMed=3680290;
RA   Sasaki M., Yamada Y.;
RT   "The laminin B2 chain has a multidomain structure homologous to the B1
RT   chain.";
RL   J. Biol. Chem. 262:17111-17117(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=89000737; PubMed=3167041; DOI=10.1021/bi00414a038;
RA   Durkin M.E., Bartos B.B., Liu S.-H., Phillips S.L., Chung A.E.;
RT   "Primary structure of the mouse laminin B2 chain and comparison with
RT   laminin B1.";
RL   Biochemistry 27:5198-5204(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-239.
RX   MEDLINE=88228071; PubMed=2836421;
RA   Ogawa K., Burbelo P.D., Sasaki M., Yamada Y.;
RT   "The laminin B2 chain promoter contains unique repeat sequences and is
RT   active in transient transfection.";
RL   J. Biol. Chem. 263:8384-8389(1988).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1391-1607.
RX   MEDLINE=85051302; PubMed=6209134;
RA   Barlow D.P., Green N.M., Kurkinen M., Hogan B.L.M.;
RT   "Sequencing of laminin B chain cDNAs reveals C-terminal regions of
RT   coiled-coil alpha-helix.";
RL   EMBO J. 3:2355-2362(1984).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-648; ASN-1105; ASN-1203;
RP   ASN-1221 AND ASN-1393, AND MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 771-932.
RX   MEDLINE=96196434; PubMed=8648630; DOI=10.1006/jmbi.1996.0191;
RA   Stetefeld J., Mayer U., Timpl R., Huber R.;
RT   "Crystal structure of three consecutive laminin-type epidermal growth
RT   factor-like (LE) modules of laminin gamma1 chain harboring the nidogen
RT   binding site.";
RL   J. Mol. Biol. 257:644-657(1996).
RN   [7]
RP   STRUCTURE BY NMR OF 824-881.
RX   MEDLINE=96196435; PubMed=8648631; DOI=10.1006/jmbi.1996.0192;
RA   Baumgartner R., Czisch M., Mayer U., Poeschl E., Huber R., Timpl R.,
RA   Holak T.A.;
RT   "Structure of the nidogen binding LE module of the laminin gamma1
RT   chain in solution.";
RL   J. Mol. Biol. 257:658-668(1996).
CC   -!- FUNCTION: Binding to cells via a high affinity receptor, laminin
CC       is thought to mediate the attachment, migration and organization
CC       of cells into tissues during embryonic development by interacting
CC       with other extracellular matrix components.
CC   -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC       different polypeptide chains (alpha, beta, gamma), which are bound
CC       to each other by disulfide bonds into a cross-shaped molecule
CC       comprising one long and three short arms with globules at each
CC       end. Gamma-1 is a subunit of laminin-1 (laminin-111 or EHS
CC       laminin), laminin-2 (laminin-211 or merosin), laminin-3 (laminin-
CC       121 or S-laminin), laminin-4 (laminin-221 or S-merosin), laminin-6
CC       (laminin-311 or K-laminin), laminin-7 (laminin-321 or KS-laminin),
CC       laminin-8 (laminin-411), laminin-9 (laminin-421), laminin-10
CC       (laminin-511) and laminin-11 (laminin-521).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane.
CC   -!- TISSUE SPECIFICITY: Found in the basement membranes (major
CC       component).
CC   -!- DOMAIN: The alpha-helical domains I and II are thought to interact
CC       with other laminin chains to form a coiled coil structure.
CC   -!- DOMAIN: Domains VI and IV are globular.
CC   -!- SIMILARITY: Contains 11 laminin EGF-like domains.
CC   -!- SIMILARITY: Contains 1 laminin IV type A domain.
CC   -!- SIMILARITY: Contains 1 laminin N-terminal domain.
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DR   EMBL; X05211; CAA28838.1; -; mRNA.
DR   EMBL; J03484; AAA39405.1; -; mRNA.
DR   EMBL; J02930; AAA39408.1; -; mRNA.
DR   EMBL; J03749; AAA39409.1; -; Genomic_DNA.
DR   IPI; IPI00400016; -.
DR   PIR; A28469; MMMSB2.
DR   PIR; S55783; S55783.
DR   UniGene; Mm.1249; -.
DR   PDB; 1KLO; X-ray; 2.10 A; A=771-932.
DR   PDB; 1NPE; X-ray; 2.30 A; B=769-932.
DR   PDB; 1TLE; NMR; -; A=824-881.
DR   PDBsum; 1KLO; -.
DR   PDBsum; 1NPE; -.
DR   PDBsum; 1TLE; -.
DR   ProteinModelPortal; P02468; -.
DR   SMR; P02468; 284-491, 682-1027.
DR   MINT; MINT-1031545; -.
DR   STRING; P02468; -.
DR   PRIDE; P02468; -.
DR   Ensembl; ENSMUST00000027752; ENSMUSP00000027752; ENSMUSG00000026478.
DR   UCSC; uc007czu.1; mouse.
DR   MGI; MGI:99914; Lamc1.
DR   eggNOG; roNOG05600; -.
DR   HOGENOM; HBG358231; -.
DR   HOVERGEN; HBG100808; -.
DR   InParanoid; P02468; -.
DR   OrthoDB; EOG49GKFS; -.
DR   ArrayExpress; P02468; -.
DR   Bgee; P02468; -.
DR   CleanEx; MM_LAMC1; -.
DR   Genevestigator; P02468; -.
DR   GermOnline; ENSMUSG00000026478; Mus musculus.
DR   GO; GO:0043259; C:laminin-10 complex; IPI:MGI.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; ISS:HGNC.
DR   GO; GO:0043208; F:glycosphingolipid binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0016477; P:cell migration; ISS:HGNC.
DR   GO; GO:0022617; P:extracellular matrix disassembly; ISS:HGNC.
DR   GO; GO:0031581; P:hemidesmosome assembly; ISS:HGNC.
DR   GO; GO:0031175; P:neuron projection development; IDA:MGI.
DR   GO; GO:0006461; P:protein complex assembly; ISS:HGNC.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR002049; EGF_laminin.
DR   InterPro; IPR018031; Laminin_B_subgr.
DR   InterPro; IPR000034; Laminin_B_type_IV.
DR   InterPro; IPR008211; Laminin_N.
DR   Pfam; PF00052; Laminin_B; 1.
DR   Pfam; PF00053; Laminin_EGF; 10.
DR   Pfam; PF00055; Laminin_N; 1.
DR   SMART; SM00180; EGF_Lam; 10.
DR   SMART; SM00281; LamB; 1.
DR   SMART; SM00136; LamNT; 1.
DR   PROSITE; PS00022; EGF_1; 8.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS01248; EGF_LAM_1; 10.
DR   PROSITE; PS50027; EGF_LAM_2; 10.
DR   PROSITE; PS51115; LAMININ_IVA; 1.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Basement membrane; Cell adhesion; Coiled coil;
KW   Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Laminin EGF-like domain; Repeat; Secreted; Signal.
FT   SIGNAL        1     33
FT   CHAIN        34   1607       Laminin subunit gamma-1.
FT                                /FTId=PRO_0000017075.
FT   DOMAIN       44    283       Laminin N-terminal.
FT   DOMAIN      284    339       Laminin EGF-like 1.
FT   DOMAIN      340    395       Laminin EGF-like 2.
FT   DOMAIN      396    442       Laminin EGF-like 3.
FT   DOMAIN      443    492       Laminin EGF-like 4.
FT   DOMAIN      493    502       Laminin EGF-like 5; first part.
FT   DOMAIN      512    687       Laminin IV type A.
FT   DOMAIN      688    721       Laminin EGF-like 5; second part.
FT   DOMAIN      722    770       Laminin EGF-like 6.
FT   DOMAIN      771    825       Laminin EGF-like 7.
FT   DOMAIN      826    881       Laminin EGF-like 8; nidogen-binding.
FT   DOMAIN      882    932       Laminin EGF-like 9.
FT   DOMAIN      933    980       Laminin EGF-like 10.
FT   DOMAIN      981   1028       Laminin EGF-like 11.
FT   REGION     1029   1607       Domain II and I.
FT   COILED     1034   1594       Potential.
FT   CARBOHYD     58     58       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    132    132       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    574    574       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    648    648       N-linked (GlcNAc...).
FT   CARBOHYD   1020   1020       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1105   1105       N-linked (GlcNAc...).
FT   CARBOHYD   1159   1159       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1173   1173       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1203   1203       N-linked (GlcNAc...).
FT   CARBOHYD   1221   1221       N-linked (GlcNAc...).
FT   CARBOHYD   1239   1239       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1378   1378       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1393   1393       N-linked (GlcNAc...).
FT   CARBOHYD   1437   1437       N-linked (GlcNAc...) (Potential).
FT   DISULFID    284    293       By similarity.
FT   DISULFID    286    303       By similarity.
FT   DISULFID    305    314       By similarity.
FT   DISULFID    340    349       By similarity.
FT   DISULFID    342    365       By similarity.
FT   DISULFID    368    377       By similarity.
FT   DISULFID    380    393       By similarity.
FT   DISULFID    396    408       By similarity.
FT   DISULFID    398    414       By similarity.
FT   DISULFID    416    425       By similarity.
FT   DISULFID    428    440       By similarity.
FT   DISULFID    443    454       By similarity.
FT   DISULFID    445    461       By similarity.
FT   DISULFID    463    472       By similarity.
FT   DISULFID    475    490       By similarity.
FT   DISULFID    722    731       By similarity.
FT   DISULFID    724    738       By similarity.
FT   DISULFID    740    749       By similarity.
FT   DISULFID    752    768       By similarity.
FT   DISULFID    771    779
FT   DISULFID    773    790
FT   DISULFID    793    802
FT   DISULFID    805    823
FT   DISULFID    826    840
FT   DISULFID    828    847
FT   DISULFID    850    859
FT   DISULFID    862    879
FT   DISULFID    882    896
FT   DISULFID    884    903
FT   DISULFID    905    914
FT   DISULFID    917    930
FT   DISULFID    933    945       By similarity.
FT   DISULFID    935    952       By similarity.
FT   DISULFID    954    963       By similarity.
FT   DISULFID    966    978       By similarity.
FT   DISULFID    981    993       By similarity.
FT   DISULFID    983    999       By similarity.
FT   DISULFID   1001   1010       By similarity.
FT   DISULFID   1013   1026       By similarity.
FT   DISULFID   1029   1029       Interchain (Probable).
FT   DISULFID   1032   1032       Interchain (Probable).
FT   DISULFID   1598   1598       Interchain (with beta-1 chain).
FT   CONFLICT    216    216       G -> A (in Ref. 3; AAA39409).
FT   CONFLICT    260    260       E -> D (in Ref. 2).
FT   CONFLICT    337    337       S -> C (in Ref. 2; AAA39408).
FT   CONFLICT    447    448       LR -> PS (in Ref. 2; AAA39408).
FT   CONFLICT    544    544       D -> Y (in Ref. 2; AAA39408).
FT   CONFLICT    662    662       T -> S (in Ref. 2; AAA39408).
FT   CONFLICT    886    886       Missing (in Ref. 2; AAA39408).
FT   CONFLICT   1158   1158       Missing (in Ref. 2; AAA39408).
FT   CONFLICT   1434   1434       V -> A (in Ref. 2; AAA39408).
FT   CONFLICT   1475   1475       R -> K (in Ref. 4; CAA28838).
FT   CONFLICT   1576   1576       D -> N (in Ref. 4; CAA28838).
FT   STRAND      779    781
FT   STRAND      783    785
FT   STRAND      788    790
FT   STRAND      797    799
FT   STRAND      809    812
FT   STRAND      821    825
FT   TURN        842    844
FT   TURN        856    859
FT   STRAND      866    868
FT   HELIX       875    877
FT   STRAND      878    881
FT   TURN        886    888
FT   HELIX       890    892
FT   TURN        898    900
FT   STRAND      909    911
FT   HELIX       924    926
SQ   SEQUENCE   1607 AA;  177298 MW;  81B7B08E4869F242 CRC64;
     MTGGGRAALA LQPRGRLWPL LAVLAAVAGC VRAAMDECAD EGGRPQRCMP EFVNAAFNVT
     VVATNTCGTP PEEYCVQTGV TGVTKSCHLC DAGQQHLQHG AAFLTDYNNQ ADTTWWQSQT
     MLAGVQYPNS INLTLHLGKA FDITYVRLKF HTSRPESFAI YKRTREDGPW IPYQYYSGSC
     ENTYSKANRG FIRTGGDEQQ ALCTDEFSDI SPLTGGNVAF STLEGRPSAY NFDNSPVLQE
     WVTATDIRVT LNRLNTFGDE VFNEPKVLKS YYYAISDFAV GGRCKCNGHA SECVKNEFDK
     LMCNCKHNTY GVDCEKCLPF FNDRPWRRAT AESASESLPC DCNGRSQECY FDPELYRSTG
     HGGHCTNCRD NTDGAKCERC RENFFRLGNT EACSPCHCSP VGSLSTQCDS YGRCSCKPGV
     MGDKCDRCQP GFHSLTEAGC RPCSCDLRGS TDECNVETGR CVCKDNVEGF NCERCKPGFF
     NLESSNPKGC TPCFCFGHSS VCTNAVGYSV YDISSTFQID EDGWRVEQRD GSEASLEWSS
     DRQDIAVISD SYFPRYFIAP VKFLGNQVLS YGQNLSFSFR VDRRDTRLSA EDLVLEGAGL
     RVSVPLIAQG NSYPSETTVK YIFRLHEATD YPWRPALSPF EFQKLLNNLT SIKIRGTYSE
     RTAGYLDDVT LQSARPGPGV PATWVESCTC PVGYGGQFCE TCLPGYRRET PSLGPYSPCV
     LCTCNGHSET CDPETGVCDC RDNTAGPHCE KCSDGYYGDS TLGTSSDCQP CPCPGGSSCA
     IVPKTKEVVC THCPTGTAGK RCELCDDGYF GDPLGSNGPV RLCRPCQCND NIDPNAVGNC
     NRLTGECLKC IYNTAGFYCD RCKEGFFGNP LAPNPADKCK ACACNPYGTV QQQSSCNPVT
     GQCQCLPHVS GRDCGTCDPG YYNLQSGQGC ERCDCHALGS TNGQCDIRTG QCECQPGITG
     QHCERCETNH FGFGPEGCKP CDCHHEGSLS LQCKDDGRCE CREGFVGNRC DQCEENYFYN
     RSWPGCQECP ACYRLVKDKA AEHRVKLQEL ESLIANLGTG DDMVTDQAFE DRLKEAEREV
     TDLLREAQEV KDVDQNLMDR LQRVNSSLHS QISRLQNIRN TIEETGILAE RARSRVESTE
     QLIEIASREL EKAKMAAANV SITQPESTGE PNNMTLLAEE ARRLAERHKQ EADDIVRVAK
     TANETSAEAY NLLLRTLAGE NQTALEIEEL NRKYEQAKNI SQDLEKQAAR VHEEAKRAGD
     KAVEIYASVA QLTPVDSEAL ENEANKIKKE AADLDRLIDQ KLKDYEDLRE DMRGKEHEVK
     NLLEKGKAEQ QTADQLLARA DAAKALAEEA AKKGRSTLQE ANDILNNLKD FDRRVNDNKT
     AAEEALRRIP AINRTIAEAN EKTREAQLAL GNAAADATEA KNKAHEAERI ASAVQKNATS
     TKADAERTFG EVTDLDNEVN GMLRQLEEAE NELKRKQDDA DQDMMMAGMA SQAAQEAELN
     ARKAKNSVSS LLSQLNNLLD QLGQLDTVDL NKLNEIEGSL NKAKDEMKAS DLDRKVSDLE
     SEARKQEAAI MDYNRDIAEI IKDIHNLEDI KKTLPTGCFN TPSIEKP
//
ID   CASA1_BOVIN             Reviewed;         214 AA.
AC   P02662; A5YK80; A8WCP1; A8WCP2; A8WCP3; A8WCP4; A8WCP5; A8WCP6;
AC   A8WCP7; A8WCP8; A8WCP9; A8WCQ0; A8WCQ1; A8WCQ2; A8WCQ3; A8WCQ4;
AC   A8WCQ5; A8WCQ6; A8WCQ7; A8WCQ8; A8WCQ9; A8WCR0; A8WCR1; A8WCR2;
AC   A8WCR3; A8WCR4; A8WCR5; A8WCR6; A8WCR7; A8WCR8; A8WCR9; A8WCS0;
AC   A8WCS1; Q28048; Q28069; Q32LE8; Q7M2U6; Q9TRH5;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 2.
DT   08-MAR-2011, entry version 101.
DE   RecName: Full=Alpha-S1-casein;
DE   AltName: Allergen=Bos d 8;
DE   Contains:
DE     RecName: Full=Antioxidant peptide;
DE   Flags: Precursor;
GN   Name=CSN1S1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=84221403; PubMed=6328443; DOI=10.1093/nar/12.9.3895;
RA   Stewart A.F., Willis I.M., Mackinlay A.G.;
RT   "Nucleotide sequences of bovine alpha S1- and kappa-casein cDNAs.";
RL   Nucleic Acids Res. 12:3895-3907(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Nagao M., Maki M., Sasaki R., Chiba R.;
RT   "Isolation and sequence analysis of bovine alpha-S1-casein cDNA
RT   clone.";
RL   Agric. Biol. Chem. 48:1663-1667(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Mammary gland;
RX   MEDLINE=87049835; PubMed=3022833;
RA   Gorodetskii S.I., Zakhar'ev V.M., Kyarshulite D.R., Kapelinskaya T.V.,
RA   Skryabin K.G.;
RT   "cDNA of cattle alpha S1-casein: cloning and nucleotide sequence.";
RL   Biokhimiia 51:1641-1648(1986).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92051301; PubMed=1658736; DOI=10.1093/nar/19.20.5591;
RA   Koczan D., Hobom G., Seyfert H.-M.;
RT   "Genomic organization of the bovine alpha-S1 casein gene.";
RL   Nucleic Acids Res. 19:5591-5596(1991).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALLERGEN.
RX   PubMed=19454699; DOI=10.4049/jimmunol.0712366;
RA   Schulmeister U., Hochwallner H., Swoboda I., Focke-Tejkl M.,
RA   Geller B., Nystrand M., Harlin A., Thalhamer J., Scheiblhofer S.,
RA   Keller W., Niggemann B., Quirce S., Ebner C., Mari A., Pauli G.,
RA   Herz U., Valenta R., Spitzauer S.;
RT   "Cloning, expression, and mapping of allergenic determinants of
RT   alphaS1-casein, a major cow's milk allergen.";
RL   J. Immunol. 182:7019-7029(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   PROTEIN SEQUENCE OF 16-214 (VARIANT B).
RX   MEDLINE=72063417; PubMed=4331376;
RX   DOI=10.1111/j.1432-1033.1971.tb01590.x;
RA   Mercier J.-C., Grosclaude F., Ribadeau-Dumas B.;
RT   "Primary structure of bovine alpha-s1 casein. Complete sequence.";
RL   Eur. J. Biochem. 23:41-51(1971).
RN   [8]
RP   SEQUENCE REVISION TO 74 AND 92-93 (VARIANTS A; B; C AND D).
RX   MEDLINE=74082545; PubMed=4797901;
RX   DOI=10.1111/j.1432-1033.1973.tb03199.x;
RA   Mercier J.-C., Grosclaude F., Ribadeau-Dumas B.;
RT   "Primary structure of alpha casein and of bovine beta casein.
RT   Correction.";
RL   Eur. J. Biochem. 40:323-323(1973).
RN   [9]
RP   PROTEIN SEQUENCE OF 16-214 (VARIANT D).
RX   MEDLINE=72214259; PubMed=5064450;
RX   DOI=10.1111/j.1432-1033.1972.tb01771.x;
RA   Grosclaude F., Mahe M.-F., Mercier J.-C., Ribadeau-Dumas B.;
RT   "Characterization of genetic variants of alpha-S1 and beta bovine
RT   caseins.";
RL   Eur. J. Biochem. 26:328-337(1972).
RN   [10]
RP   PROTEIN SEQUENCE OF 23-49 (VARIANT A).
RX   PubMed=11945462; DOI=10.1016/0014-5793(70)80504-X;
RA   Grosclaude F., Mahe M.-F., Mercier J.-C., Ribadeau-Dumas B.;
RT   "Localization in the N-terminal part of bovine casein alpha-s1 of a 13
RT   amino-acid deletion that differentiates variant A from variants B and
RT   C.";
RL   FEBS Lett. 11:109-112(1970).
RN   [11]
RP   PROTEIN SEQUENCE OF 39-55.
RC   TISSUE=Mammary gland;
RX   MEDLINE=93231344; PubMed=1299613; DOI=10.1016/0014-5793(92)80664-3;
RA   Neuteboom B., Giuffrida M.G., Conti A.;
RT   "Isolation of a new ligand-carrying casein fragment from bovine
RT   mammary gland microsomes.";
RL   FEBS Lett. 305:189-191(1992).
RN   [12]
RP   PROTEIN SEQUENCE OF 39-47 AND 166-188.
RX   MEDLINE=96439049; PubMed=8841384; DOI=10.1016/0167-4838(96)00103-3;
RA   Ramalho-Santos M., Verissimo P., Faro C., Pires E.;
RT   "Action on bovine alpha s1-casein of cardosins A and B, aspartic
RT   proteinases from the flowers of the cardoon Cynara cardunculus L.";
RL   Biochim. Biophys. Acta 1297:83-89(1996).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 55-130.
RX   MEDLINE=83182023; PubMed=6897774;
RA   Willis I.M., Stewart A.F., Caputo A., Thompson A.R., McKinlay A.G.;
RT   "Construction and identification by partial nucleotide sequence
RT   analysis of bovine casein and beta-lactoglobulin cDNA clones.";
RL   DNA 1:375-386(1982).
RN   [14]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 85-110.
RA   Shahla M.N., Farooq M.S., Naeem M.K., Riazuddin S.;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [15]
RP   PROTEIN SEQUENCE OF 95-105, AND FUNCTION.
RA   Gupta A., Mann B., Kumar R., Sangwan R.B.;
RT   "Antioxidant peptides isolated from cheddar cheese made with adjunct
RT   culture L.casei ssp. casei 300.";
RL   Submitted (MAR-2008) to UniProtKB.
RN   [16]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 122-214.
RX   MEDLINE=85178933; PubMed=3838718;
RA   Kiarshulite D.R., Zakhar'ev V.M., Gorodetskii S.I.;
RT   "Nucleotide sequence of the 3'-nontranslated region of the mRNA of
RT   alpha S1-casein in cows.";
RL   Dokl. Akad. Nauk SSSR 280:1433-1437(1985).
RN   [17]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 164-214.
RX   MEDLINE=94154154; PubMed=1343827;
RA   Chen R., Wang B., Zhang Y., Liu W., Zhang J., Lao W.;
RT   "Cloning, mapping, and sequencing of 3' and its flanking region of
RT   bovine alpha-s1 casein gene.";
RL   Chin. J. Biotechnol. 8:235-245(1992).
RN   [18]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 185-202.
RC   TISSUE=Mammary gland;
RA   Maki M., Nagao M., Hirose M., Chiba H.;
RT   "Cloning of cDNA sequence coding for bovine alpha-s1-casein.";
RL   Agric. Biol. Chem. 47:441-444(1983).
RN   [19]
RP   PROTEIN SEQUENCE OF 205-214 (VARIANT C).
RA   Grosclaude F., Mercier J.-C., Ribadeau-Dumas B.;
RT   "On the localization in the C-terminal sequence of bovine casein
RT   alpha-s1 of a Glu/Gly substitution that differentiates the genetic
RT   variants B and C.";
RL   C. R. Hebd. Seances Acad. Sci., D, Sci. Nat. 268:3133-3136(1970).
RN   [20]
RP   ERRATUM, AND SEQUENCE REVISION.
RA   Grosclaude F., Mercier J.-C., Ribadeau-Dumas B.;
RL   C. R. Hebd. Seances Acad. Sci., D, Sci. Nat. 271:563-563(1970).
RN   [21]
RP   ALLERGEN.
RX   PubMed=11174208; DOI=10.1067/mai.2001.112372;
RA   Chatchatee P., Jaervinen K.M., Bardina L., Beyer K., Sampson H.A.;
RT   "Identification of IgE- and IgG-binding epitopes on alpha(s1)-casein:
RT   differences in patients with persistent and transient cow's milk
RT   allergy.";
RL   J. Allergy Clin. Immunol. 107:379-383(2001).
RN   [22]
RP   PHOSPHORYLATION AT SER-56.
RA   Bai F., Liu S., Witzmann F.A.;
RL   Submitted (SEP-2005) to UniProtKB.
RN   [23]
RP   PHOSPHORYLATION AT SER-56; SER-61; SER-63; SER-79; SER-81; SER-82;
RP   SER-83; SER-90 AND SER-130, AND MASS SPECTROMETRY.
RX   PubMed=17510049; DOI=10.1074/mcp.M600480-MCP200;
RA   Imanishi S.Y., Kochin V., Ferraris S.E., de Thonel A., Pallari H.M.,
RA   Corthals G.L., Eriksson J.E.;
RT   "Reference-facilitated phosphoproteomics: fast and reliable
RT   phosphopeptide validation by micro LC-ESI-Q-TOF MS/MS.";
RL   Mol. Cell. Proteomics 6:1380-1391(2007).
CC   -!- FUNCTION: Important role in the capacity of milk to transport
CC       calcium phosphate.
CC   -!- FUNCTION: Antioxidant peptide has 2,2-diphenyl-1-picrylhydrazyl
CC       (DPPH) radical scavenging activity.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Mammary gland specific. Secreted in milk.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Has six major and
CC       3 minor IgE-binding regions and 5 major and 1 minor IgG-binding
CC       regions. Is a cause of cow's milk allergy (CMA).
CC   -!- MISCELLANEOUS: The B variant sequence is shown.
CC   -!- SIMILARITY: Belongs to the alpha-casein family.
CC   -!- WEB RESOURCE: Name=Worthington enzyme manual;
CC       URL="http://www.worthington-biochem.com/CASA/";
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Of buttons, digestion
CC       and glue - Issue 16 of November 2001;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt016.shtml";
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DR   EMBL; X00564; CAB57792.1; -; mRNA.
DR   EMBL; M33123; AAA30428.1; -; mRNA.
DR   EMBL; M38641; AAA30429.1; -; mRNA.
DR   EMBL; X59856; CAA42516.1; -; Genomic_DNA.
DR   EMBL; EU221551; ABW98936.1; -; Genomic_DNA.
DR   EMBL; EU221552; ABW98937.1; -; Genomic_DNA.
DR   EMBL; EU221553; ABW98938.1; -; Genomic_DNA.
DR   EMBL; EU221554; ABW98939.1; -; Genomic_DNA.
DR   EMBL; EU221555; ABW98940.1; -; Genomic_DNA.
DR   EMBL; EU221556; ABW98941.1; -; Genomic_DNA.
DR   EMBL; EU221557; ABW98942.1; -; Genomic_DNA.
DR   EMBL; EU221558; ABW98943.1; -; Genomic_DNA.
DR   EMBL; EU221559; ABW98944.1; -; Genomic_DNA.
DR   EMBL; EU221560; ABW98945.1; -; Genomic_DNA.
DR   EMBL; EU221561; ABW98946.1; -; Genomic_DNA.
DR   EMBL; EU221562; ABW98947.1; -; Genomic_DNA.
DR   EMBL; EU221563; ABW98948.1; -; Genomic_DNA.
DR   EMBL; EU221564; ABW98949.1; -; Genomic_DNA.
DR   EMBL; EU221565; ABW98950.1; -; Genomic_DNA.
DR   EMBL; EU221566; ABW98951.1; -; Genomic_DNA.
DR   EMBL; EU221567; ABW98952.1; -; Genomic_DNA.
DR   EMBL; EU221568; ABW98953.1; -; Genomic_DNA.
DR   EMBL; EU221569; ABW98954.1; -; Genomic_DNA.
DR   EMBL; EU221570; ABW98955.1; -; Genomic_DNA.
DR   EMBL; EU221571; ABW98956.1; -; Genomic_DNA.
DR   EMBL; EU221572; ABW98957.1; -; Genomic_DNA.
DR   EMBL; EU221573; ABW98958.1; -; Genomic_DNA.
DR   EMBL; EU221574; ABW98959.1; -; Genomic_DNA.
DR   EMBL; EU221575; ABW98960.1; -; Genomic_DNA.
DR   EMBL; EU221576; ABW98961.1; -; Genomic_DNA.
DR   EMBL; EU221577; ABW98962.1; -; Genomic_DNA.
DR   EMBL; EU221578; ABW98963.1; -; Genomic_DNA.
DR   EMBL; EU221579; ABW98964.1; -; Genomic_DNA.
DR   EMBL; EU221580; ABW98965.1; -; Genomic_DNA.
DR   EMBL; EU221581; ABW98966.1; -; Genomic_DNA.
DR   EMBL; BC109618; AAI09619.1; -; mRNA.
DR   EMBL; K01084; AAA30478.1; -; mRNA.
DR   EMBL; EF538766; ABQ88318.1; -; Genomic_DNA.
DR   EMBL; M38658; AAA62707.1; -; mRNA.
DR   EMBL; S72388; AAD14099.1; -; Genomic_DNA.
DR   EMBL; D00412; BAA00313.1; -; mRNA.
DR   IPI; IPI00706094; -.
DR   PIR; S22575; KABOSB.
DR   PIR; S72220; S72220.
DR   RefSeq; NP_851372.1; NM_181029.2.
DR   UniGene; Bt.59369; -.
DR   DisProt; DP00330; -.
DR   DIP; DIP-29917N; -.
DR   STRING; P02662; -.
DR   Allergome; 167; Bos d 8.
DR   Allergome; 2734; Bos d 8 alphaS1.
DR   PRIDE; P02662; -.
DR   Ensembl; ENSBTAT00000010119; ENSBTAP00000010119; ENSBTAG00000007695.
DR   GeneID; 282208; -.
DR   KEGG; bta:282208; -.
DR   CTD; 282208; -.
DR   eggNOG; maNOG21672; -.
DR   GeneTree; ENSGT00390000017378; -.
DR   HOVERGEN; HBG005242; -.
DR   InParanoid; P02662; -.
DR   OrthoDB; EOG4M0F39; -.
DR   PhylomeDB; P02662; -.
DR   PMAP-CutDB; P02662; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016209; F:antioxidant activity; IEA:UniProtKB-KW.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   InterPro; IPR001588; Casein.
DR   Pfam; PF00363; Casein; 1.
DR   PROSITE; PS00306; CASEIN_ALPHA_BETA; 1.
PE   1: Evidence at protein level;
KW   Allergen; Antioxidant; Direct protein sequencing; Milk protein;
KW   Phosphoprotein; Polymorphism; Repeat; Secreted; Signal.
FT   SIGNAL        1     15
FT   CHAIN        16    214       Alpha-S1-casein.
FT                                /FTId=PRO_0000004446.
FT   PEPTIDE      95    105       Antioxidant peptide.
FT                                /FTId=PRO_0000331578.
FT   REPEAT       85     99
FT   REPEAT      125    140
FT   MOD_RES      56     56       Phosphoserine.
FT   MOD_RES      61     61       Phosphoserine.
FT   MOD_RES      63     63       Phosphoserine.
FT   MOD_RES      68     68       Phosphothreonine; in variant D.
FT   MOD_RES      79     79       Phosphoserine.
FT   MOD_RES      81     81       Phosphoserine.
FT   MOD_RES      82     82       Phosphoserine.
FT   MOD_RES      83     83       Phosphoserine.
FT   MOD_RES      90     90       Phosphoserine.
FT   MOD_RES     130    130       Phosphoserine.
FT   VARIANT      29     41       Missing (in variant A).
FT   VARIANT      68     68       A -> T (in variant D).
FT   VARIANT     207    207       E -> G (in variant C).
FT   CONFLICT     11     12       AV -> SA (in Ref. 5; ABW98943).
FT   CONFLICT     42     42       P -> L (in Ref. 3; AAA30429).
FT   CONFLICT     44     44       P -> S (in Ref. 5; ABW98945).
FT   CONFLICT     95     95       H -> Q (in Ref. 13; AAA30478).
FT   CONFLICT     99     99       E -> D (in Ref. 14; ABQ88318).
FT   CONFLICT    143    143       H -> D (in Ref. 3; AAA30429).
FT   CONFLICT    171    171       L -> P (in Ref. 5; ABW98953).
FT   CONFLICT    203    203       S -> L (in Ref. 16; AAA62707).
FT   CONFLICT    211    212       MP -> IS (in Ref. 3; AAA30429).
SQ   SEQUENCE   214 AA;  24529 MW;  F066B5C8AE55828B CRC64;
     MKLLILTCLV AVALARPKHP IKHQGLPQEV LNENLLRFFV APFPEVFGKE KVNELSKDIG
     SESTEDQAME DIKQMEAESI SSSEEIVPNS VEQKHIQKED VPSERYLGYL EQLLRLKKYK
     VPQLEIVPNS AEERLHSMKE GIHAQQKEPM IGVNQELAYF YPELFRQFYQ LDAYPSGAWY
     YVPLGTQYTD APSFSDIPNP IGSENSEKTT MPLW
//
ID   GFAP_MOUSE              Reviewed;         430 AA.
AC   P03995; A1E2H7; A2AH87; B2RTI7; Q09J71; Q3USS4; Q496R4; Q496S3;
AC   Q7TQ30; Q80VX6; Q925K2; Q925K3;
DT   23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 4.
DT   08-MAR-2011, entry version 102.
DE   RecName: Full=Glial fibrillary acidic protein;
DE            Short=GFAP;
GN   Name=Gfap;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=85297756; PubMed=2994002; DOI=10.1093/nar/13.15.5527;
RA   Balcarek J.M., Cowan N.J.;
RT   "Structure of the mouse glial fibrillary acidic protein gene:
RT   implications for the evolution of the intermediate filament multigene
RT   family.";
RL   Nucleic Acids Res. 13:5527-5543(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-150.
RC   STRAIN=129/Sv;
RA   Sheng J., Wu X., Lin F., Yang X., Deng J.;
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RC   TISSUE=Embryo;
RX   MEDLINE=95074269; PubMed=7983160;
RA   Ralton J.E., Lu X., Hutcheson A.M., Quinlan R.A.;
RT   "Identification of two N-terminal non-alpha-helical domain motifs
RT   important in the assembly of glial fibrillary acidic protein.";
RL   J. Cell Sci. 107:1935-1948(1994).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 28-430 (ISOFORM 1).
RX   MEDLINE=84194082; PubMed=6585825; DOI=10.1073/pnas.81.9.2743;
RA   Lewis S.A., Balcarek J.M., Krek V., Shelanski M., Cowan N.J.;
RT   "Sequence of a cDNA clone encoding mouse glial fibrillary acidic
RT   protein: structural conservation of intermediate filaments.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:2743-2746(1984).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 28-430 (ISOFORM 1).
RX   MEDLINE=86101618; PubMed=3866511;
RX   DOI=10.1111/j.1749-6632.1985.tb50437.x;
RA   Cowan N.J., Lewis S.A., Balcarek J.M., Krek V., Shelanski M.L.;
RT   "Structural implications of a cDNA clone encoding mouse glial
RT   fibrillary acidic protein.";
RL   Ann. N. Y. Acad. Sci. 455:575-582(1985).
RN   [9]
RP   SEQUENCE REVISION TO N-TERMINUS.
RX   MEDLINE=90294716; PubMed=2163003; DOI=10.1016/0169-328X(90)90078-R;
RA   Brenner M., Lampel K., Nakatani Y., Mill J., Banner C., Mearow K.,
RA   Dohadwala M., Lipsky R., Freese E.;
RT   "Characterization of human cDNA and genomic clones for glial
RT   fibrillary acidic protein.";
RL   Brain Res. Mol. Brain Res. 7:277-286(1990).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 31-430 (ISOFORM 1).
RC   STRAIN=ISS;
RX   MEDLINE=21363810; PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 92-275 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6;
RA   Huysentruyt L.C., Banerjee D., Seyfried T.N.;
RT   "Novel metastatic mouse tumor cells express multiple properties of
RT   macrophages.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   PROTEIN SEQUENCE OF 47-63; 139-149; 187-198; 210-233; 285-297 AND
RP   374-387, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [13]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 169-237 (ISOFORMS 1/2).
RC   STRAIN=SJL/JHanHsd; TISSUE=Brain;
RA   Ulrich R., Alldinger S., Baumgaertner W.;
RT   "Progressive demyelination despite a temporary increased number of NG-
RT   2 positive putative oligodendroglial progenitor cells in Theiler`s
RT   murine encephalomyelitis.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [14]
RP   PROTEIN SEQUENCE OF 354-364, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [15]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 388-430 (ISOFORM 2).
RC   TISSUE=Blood;
RX   MEDLINE=22721693; PubMed=12837269; DOI=10.1016/S0888-7543(03)00106-X;
RA   Singh R., Nielsen A.L., Johansen M.G., Jorgensen A.L.;
RT   "Genetic polymorphism and sequence evolution of an alternatively
RT   spliced exon of the glial fibrillary acidic protein gene, GFAP.";
RL   Genomics 82:185-193(2003).
RN   [16]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=22162526; PubMed=12058025; DOI=10.1074/jbc.M112121200;
RA   Nielsen A.L., Holm I.E., Johansen M., Bonven B., Jorgensen P.,
RA   Jorgensen A.L.;
RT   "A new splice variant of glial fibrillary acidic protein GFAPepsilon,
RT   interacts with the presenilin proteins.";
RL   J. Biol. Chem. 277:29983-29991(2002).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-40, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [18]
RP   INTERACTION WITH SYNM.
RX   PubMed=17356066; DOI=10.1242/jcs.03423;
RA   Jing R., Wilhelmsson U., Goodwill W., Li L., Pan Y., Pekny M.,
RA   Skalli O.;
RT   "Synemin is expressed in reactive astrocytes in neurotrauma and
RT   interacts differentially with vimentin and GFAP intermediate filament
RT   networks.";
RL   J. Cell Sci. 120:1267-1277(2007).
CC   -!- FUNCTION: GFAP, a class-III intermediate filament, is a cell-
CC       specific marker that, during the development of the central
CC       nervous system, distinguishes astrocytes from other glial cells.
CC   -!- SUBUNIT: Interacts with SYNM.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=Associated
CC       with intermediate filaments (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=GFAP alpha;
CC         IsoId=P03995-1; Sequence=Displayed;
CC       Name=2; Synonyms=GFAP epsilon;
CC         IsoId=P03995-2; Sequence=VSP_017053;
CC   -!- TISSUE SPECIFICITY: Brain; isoform 2 expressed at 20-fold lower
CC       level than isoform 1.
CC   -!- PTM: Phosphorylated by PKN1 (By similarity).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA26571.1; Type=Erroneous initiation;
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DR   EMBL; X02801; CAA26571.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AK140151; BAE24257.1; -; mRNA.
DR   EMBL; AL731670; CAM25115.1; -; Genomic_DNA.
DR   EMBL; AY279974; AAP33501.1; -; Genomic_DNA.
DR   EMBL; X78141; CAA55020.1; -; Genomic_DNA.
DR   EMBL; BC100728; AAI00729.1; -; mRNA.
DR   EMBL; BC100737; AAI00738.1; -; mRNA.
DR   EMBL; BC101968; AAI01969.1; -; mRNA.
DR   EMBL; BC103571; AAI03572.1; -; mRNA.
DR   EMBL; BC139357; AAI39358.1; -; mRNA.
DR   EMBL; BC139358; AAI39359.1; -; mRNA.
DR   EMBL; K01347; AAA37678.1; -; mRNA.
DR   EMBL; M25937; AAA37679.1; -; mRNA.
DR   EMBL; AF332061; AAK56090.1; -; mRNA.
DR   EMBL; AF332062; AAK56091.1; -; mRNA.
DR   EMBL; EF101554; ABK96803.1; -; mRNA.
DR   EMBL; DQ887822; ABI54133.1; -; mRNA.
DR   EMBL; AY142200; AAN87913.1; -; Genomic_DNA.
DR   IPI; IPI00117042; -.
DR   IPI; IPI00649033; -.
DR   PIR; B60052; VEMSGF.
DR   RefSeq; NP_001124492.1; NM_001131020.1.
DR   RefSeq; NP_034407.2; NM_010277.3.
DR   UniGene; Mm.1239; -.
DR   ProteinModelPortal; P03995; -.
DR   SMR; P03995; 64-101, 104-211, 226-296, 300-369.
DR   DIP; DIP-1084N; -.
DR   STRING; P03995; -.
DR   PhosphoSite; P03995; -.
DR   UCD-2DPAGE; P03995; -.
DR   PRIDE; P03995; -.
DR   Ensembl; ENSMUST00000067444; ENSMUSP00000064691; ENSMUSG00000020932.
DR   Ensembl; ENSMUST00000077902; ENSMUSP00000077061; ENSMUSG00000020932.
DR   GeneID; 14580; -.
DR   KEGG; mmu:14580; -.
DR   CTD; 14580; -.
DR   MGI; MGI:95697; Gfap.
DR   GeneTree; ENSGT00560000076592; -.
DR   HOVERGEN; HBG013015; -.
DR   InParanoid; P03995; -.
DR   OMA; NLATYRQ; -.
DR   OrthoDB; EOG48WC24; -.
DR   PhylomeDB; P03995; -.
DR   NextBio; 286306; -.
DR   ArrayExpress; P03995; -.
DR   Bgee; P03995; -.
DR   CleanEx; MM_GFAP; -.
DR   Genevestigator; P03995; -.
DR   GermOnline; ENSMUSG00000020932; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005882; C:intermediate filament; IDA:MGI.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0045103; P:intermediate filament-based process; IMP:MGI.
DR   InterPro; IPR016044; F.
DR   InterPro; IPR001664; IF.
DR   InterPro; IPR006821; Intermed_filament_DNA-bd.
DR   InterPro; IPR018039; Intermediate_filament_CS.
DR   PANTHER; PTHR23239; IF; 1.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF04732; Filament_head; 1.
DR   PROSITE; PS00226; IF; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm;
KW   Direct protein sequencing; Intermediate filament; Phosphoprotein.
FT   CHAIN         1    430       Glial fibrillary acidic protein.
FT                                /FTId=PRO_0000063806.
FT   REGION        1     69       Head.
FT   REGION       70    374       Rod.
FT   REGION       70    101       Coil 1A.
FT   REGION      102    112       Linker 1.
FT   REGION      113    211       Coil 1B.
FT   REGION      212    227       Linker 12.
FT   REGION      228    249       Coil 2A.
FT   REGION      250    253       Linker 2.
FT   REGION      254    374       Coil 2B.
FT   REGION      375    430       Tail.
FT   MOD_RES      40     40       Phosphothreonine.
FT   MOD_RES     107    107       Phosphothreonine (By similarity).
FT   MOD_RES     380    380       Phosphothreonine (By similarity).
FT   VAR_SEQ     388    430       ETSLDTKSVSEGHLKRNIVVKTVEMRDGEVIKDSKQEHKDV
FT                                VM -> GGKSTKEGEGQKVTRPLKRLTIQVVPIQAHQIENG
FT                                ALPALP (in isoform 2).
FT                                /FTId=VSP_017053.
FT   CONFLICT    141    141       F -> L (in Ref. 5; AAP33501 and 10;
FT                                AAK56091).
FT   CONFLICT    174    174       D -> H (in Ref. 1; CAA26571, 7; AAA37678,
FT                                8; AAA37679 and 13; ABI54133).
FT   CONFLICT    180    180       R -> S (in Ref. 2; BAE24257).
FT   CONFLICT    207    207       E -> D (in Ref. 1; CAA26571, 7; AAA37678
FT                                and 8; AAA37679).
FT   CONFLICT    347    347       Q -> H (in Ref. 1; CAA26571).
SQ   SEQUENCE   430 AA;  49900 MW;  C0FB500AE1588377 CRC64;
     MERRRITSAR RSYASETVVR GLGPSRQLGT MPRFSLSRMT PPLPARVDFS LAGALNAGFK
     ETRASERAEM MELNDRFASY IEKVRFLEQQ NKALAAELNQ LRAKEPTKLA DVYQAELREL
     RLRLDQLTAN SARLEVERDN FAQDLGTLRQ KLQDETNLRL EAENNLAAYR QEADEATLAR
     VDLERKVESL EEEIQFLRKI YEEEVRELRE QLAQQQVHVE MDVAKPDLTA ALREIRTQYE
     AVATSNMQET EEWYRSKFAD LTDAASRNAE LLRQAKHEAN DYRRQLQALT CDLESLRGTN
     ESLERQMREQ EERHARESAS YQEALARLEE EGQSLKEEMA RHLQEYQDLL NVKLALDIEI
     ATYRKLLEGE ENRITIPVQT FSNLQIRETS LDTKSVSEGH LKRNIVVKTV EMRDGEVIKD
     SKQEHKDVVM
//
ID   K2C1_MOUSE              Reviewed;         637 AA.
AC   P04104; Q149E0; Q9D2K8;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 4.
DT   08-MAR-2011, entry version 100.
DE   RecName: Full=Keratin, type II cytoskeletal 1;
DE   AltName: Full=67 kDa cytokeratin;
DE   AltName: Full=Cytokeratin-1;
DE            Short=CK-1;
DE   AltName: Full=Keratin-1;
DE            Short=K1;
DE   AltName: Full=Type-II keratin Kb1;
GN   Name=Krt1; Synonyms=Krt2-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=85207740; PubMed=2581964;
RA   Steinert P.M., Parry D.A.D., Idler W.W., Johnson L.D., Steven A.C.,
RA   Roop D.R.;
RT   "Amino acid sequences of mouse and human epidermal type II keratins of
RT   Mr 67,000 provide a systematic basis for the structural and functional
RT   diversity of the end domains of keratin intermediate filament
RT   subunits.";
RL   J. Biol. Chem. 260:7142-7149(1985).
RN   [2]
RP   SEQUENCE REVISION.
RA   Roop D.R.;
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 199-205; 208-219 AND 286-296, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   CITRULLINATION.
RX   PubMed=11841545; DOI=10.1046/j.0022-202x.2001.01671.x;
RA   Ishida-Yamamoto A., Senshu T., Eady R.A.J., Takahashi H., Shimizu H.,
RA   Akiyama M., Iizuka H.;
RT   "Sequential reorganization of cornified cell keratin filaments
RT   involving filaggrin-mediated compaction and keratin 1 deimination.";
RL   J. Invest. Dermatol. 118:282-287(2002).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-352, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   VARIANT EHK PRO-194.
RX   PubMed=16528356; DOI=10.1038/sj.jid.5700241;
RA   McGowan K.A., Aradhya S., Fuchs H., de Angelis M.H., Barsh G.S.;
RT   "A mouse keratin 1 mutation causes dark skin and epidermolytic
RT   hyperkeratosis.";
RL   J. Invest. Dermatol. 126:1013-1016(2006).
CC   -!- FUNCTION: May regulate the activity of kinases such as PKC and SRC
CC       via binding to integrin beta-1 (ITB1) and the receptor of
CC       activated protein kinase C (RACK1/GNB2L1) (By similarity).
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC       Keratin-1 is generally associated with keratin-10. Interacts with
CC       ITB1 in the presence of GNB2L1 and SRC, and with GNB2L1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane (By similarity).
CC   -!- PTM: Undergoes deimination of some arginine residues
CC       (citrullination).
CC   -!- DISEASE: Note=Defects in Krt1 are a cause of epidermolytic
CC       hyperkeratosis (EHK); also known as bullous congenital
CC       ichthyosiform erythroderma (BIE). EHK is a hereditary skin
CC       disorder characterized by intraepidermal blistering, a marked
CC       thickening of the stratum corneum, pigmentation of the skin and
CC       erosions at sites of trauma which are all present from birth.
CC   -!- MISCELLANEOUS: There are two types of cytoskeletal and
CC       microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to
CC       basic; 56-70 kDa).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
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DR   EMBL; M10937; AAD05191.1; -; mRNA.
DR   EMBL; AK019521; BAB31776.1; -; mRNA.
DR   EMBL; BC117842; AAI17843.1; -; mRNA.
DR   EMBL; BC117843; AAI17844.1; -; mRNA.
DR   IPI; IPI00625729; -.
DR   PIR; A02951; KRMS2.
DR   RefSeq; NP_032499.2; NM_008473.2.
DR   UniGene; Mm.183137; -.
DR   ProteinModelPortal; P04104; -.
DR   SMR; P04104; 186-223, 231-336, 354-499.
DR   IntAct; P04104; 1.
DR   STRING; P04104; -.
DR   PhosphoSite; P04104; -.
DR   SWISS-2DPAGE; P04104; -.
DR   PRIDE; P04104; -.
DR   Ensembl; ENSMUST00000023790; ENSMUSP00000023790; ENSMUSG00000046834.
DR   GeneID; 16678; -.
DR   KEGG; mmu:16678; -.
DR   NMPDR; fig|10090.3.peg.30683; -.
DR   CTD; 16678; -.
DR   MGI; MGI:96698; Krt1.
DR   eggNOG; roNOG07569; -.
DR   GeneTree; ENSGT00550000074491; -.
DR   HOGENOM; HBG715391; -.
DR   HOVERGEN; HBG013015; -.
DR   InParanoid; P04104; -.
DR   OMA; INYQRRT; -.
DR   OrthoDB; EOG48GW3H; -.
DR   PhylomeDB; P04104; -.
DR   NextBio; 290417; -.
DR   ArrayExpress; P04104; -.
DR   Bgee; P04104; -.
DR   CleanEx; MM_KRT1; -.
DR   Genevestigator; P04104; -.
DR   GermOnline; ENSMUSG00000046834; Mus musculus.
DR   GO; GO:0045095; C:keratin filament; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR016044; F.
DR   InterPro; IPR001664; IF.
DR   InterPro; IPR018039; Intermediate_filament_CS.
DR   InterPro; IPR003054; Keratin_II.
DR   PANTHER; PTHR23239; IF; 1.
DR   PANTHER; PTHR23239:SF18; Keratin_II; 1.
DR   Pfam; PF00038; Filament; 1.
DR   PRINTS; PR01276; TYPE2KERATIN.
DR   PROSITE; PS00226; IF; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Citrullination; Coiled coil; Direct protein sequencing;
KW   Disease mutation; Intermediate filament; Keratin; Membrane;
KW   Methylation; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    637       Keratin, type II cytoskeletal 1.
FT                                /FTId=PRO_0000063710.
FT   REGION        2    187       Head.
FT   REGION      188    497       Rod.
FT   REGION      188    223       Coil 1A.
FT   REGION      224    243       Linker 1.
FT   REGION      244    334       Coil 1B.
FT   REGION      335    358       Linker 12.
FT   REGION      359    497       Coil 2.
FT   REGION      498    637       Tail.
FT   COILED      180    328       Potential.
FT   COILED      397    483       Potential.
FT   COMPBIAS     13    159       Gly-rich.
FT   COMPBIAS    522    621       Gly-rich.
FT   SITE        452    452       Stutter.
FT   MOD_RES      24     24       Phosphoserine.
FT   MOD_RES      67     67       Phosphoserine (By similarity).
FT   MOD_RES     284    284       N6,N6-dimethyllysine (By similarity).
FT   MOD_RES     303    303       Phosphotyrosine (By similarity).
FT   MOD_RES     305    305       Phosphothreonine (By similarity).
FT   MOD_RES     352    352       Phosphoserine.
FT   VARIANT     194    194       S -> P (in EHK).
FT   CONFLICT     99     99       G -> R (in Ref. 1; AAD05191).
FT   CONFLICT    131    131       L -> S (in Ref. 1; AAD05191).
FT   CONFLICT    147    147       R -> T (in Ref. 3; BAB31776).
FT   CONFLICT    150    151       SM -> GY (in Ref. 1; AAD05191).
FT   CONFLICT    156    158       PPG -> SPS (in Ref. 1; AAD05191).
FT   CONFLICT    165    165       I -> L (in Ref. 1; AAD05191).
FT   CONFLICT    176    176       E -> K (in Ref. 1; AAD05191).
FT   CONFLICT    214    214       Q -> K (in Ref. 1; AAD05191).
FT   CONFLICT    261    261       D -> E (in Ref. 1; AAD05191).
FT   CONFLICT    313    313       A -> R (in Ref. 1; AAD05191).
FT   CONFLICT    321    321       D -> N (in Ref. 1; AAD05191).
FT   CONFLICT    325    325       A -> T (in Ref. 1; AAD05191).
FT   CONFLICT    352    353       SL -> QF (in Ref. 1; AAD05191).
FT   CONFLICT    428    428       S -> Y (in Ref. 3; BAB31776).
FT   CONFLICT    572    580       Missing (in Ref. 1; AAD05191).
SQ   SEQUENCE   637 AA;  65606 MW;  D2016D15066FD0A5 CRC64;
     MSLQCSSRSL CRGGGGSRNF SSGSAGLVSF QRRSTSSSMR RSGGGGGGRF SGGGFCGSSG
     SGFGSKSLMN LGGGRSISKS VAGGGGSFCG GFGGGSYGGG GFGGGSYGGG GFGGGSFGGG
     GFGGSGFGGG LGGGGGFGSG GGFGGGRFGS MGPVCPPGGI QEVTINQSLL QPLNVEVDPQ
     IQKVKSQERE QIKSLNDKFA SFIDKVRFLE QQNQVLQTKW ELLQQVDTTT RTQNLDPFFE
     NYISILRRKV DSLKSDQSRM DSELKNMQDL VEEYRTKYED EINKRTNAEN EFVTIKKDVD
     SAYMTKVELQ AKADALQQDI DFFSALYQME MSQMQTQISE TNVVLSMDNN RSLDLDGIIS
     EVKAQYDSIC QRSKAEAETF YQSKYEELQI TAGKHGDSVR NTKMEISELN RMIQRLRSEI
     DGCKKQISQI QQNINDAEQR GEKALKDAQN KLNEIEDALS QCKEDLARLL RDFQELMNTK
     LALDMEIATY KKLLEGEEIR MSGECTPNVS VSVSTSHTSM SGSSSRGGGS GGGRYGGGGS
     YGGGSGGGSY GGSSGGGGSG GSYGGGSGGG SYGGGSGGGS SGSHRGGSGG GGGSSGGSYG
     GSSGGGRGGS SSGGGGVKSS GSSTVKFVST SYSRGTK
//
ID   MBP_MOUSE               Reviewed;         250 AA.
AC   P04370; Q01585; Q03139; Q03176; Q61836; Q61837; Q99KE4; Q9QWP1;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   18-OCT-2001, sequence version 2.
DT   08-MAR-2011, entry version 127.
DE   RecName: Full=Myelin basic protein;
DE            Short=MBP;
DE   AltName: Full=Myelin A1 protein;
GN   Name=Mbp; Synonyms=Shi;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=85254913; PubMed=2410136; DOI=10.1016/S0092-8674(85)80109-4;
RA   Takahashi N., Roach A., Teplow D.B., Prusiner S.B., Hood L.E.;
RT   "Cloning and characterization of the myelin basic protein gene from
RT   mouse: one gene can encode both 14 kd and 18.5 kd MBPs by alternate
RT   use of exons.";
RL   Cell 42:139-148(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=86079555; PubMed=2416470; DOI=10.1016/0092-8674(85)90245-4;
RA   de Ferra F., Engh H., Hudson L., Kamholz J., Puckett C., Molineaux S.,
RA   Lazzarini R.A.;
RT   "Alternative splicing accounts for the four forms of myelin basic
RT   protein.";
RL   Cell 43:721-727(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6 AND 7), AND NUCLEOTIDE SEQUENCE
RP   [MRNA] OF 9-194.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   MEDLINE=87118269; PubMed=2433693; DOI=10.1073/pnas.84.3.886;
RA   Newman S., Kitamura K., Campagnoni A.T.;
RT   "Identification of a cDNA coding for a fifth form of myelin basic
RT   protein in mouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:886-890(1987).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
RX   MEDLINE=90250449; PubMed=1692584;
RX   DOI=10.1111/j.1471-4159.1990.tb04908.x;
RA   Kitamura K., Newman S.L., Campagnoni C.W., Verdi J.M., Mohandas T.,
RA   Handley V.W., Campagnoni A.T.;
RT   "Expression of a novel transcript of the myelin basic protein gene.";
RL   J. Neurochem. 54:2032-2041(1990).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Bone marrow;
RX   MEDLINE=93057537; PubMed=1279125;
RA   Grima B., Zelenika D., Pessac B.;
RT   "A novel transcript overlapping the myelin basic protein gene.";
RL   J. Neurochem. 59:2318-2323(1992).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=93186801; PubMed=7680345;
RA   Campagnoni A.T., Pribyl T.M., Campagnoni C.W., Kampf K.,
RA   Amur-Umarjee S., Landry C.F., Handley V.W., Newman S., Garbay B.,
RA   Kitamura K.;
RT   "Structure and developmental regulation of Golli-mbp, a 105-kilobase
RT   gene that encompasses the myelin basic protein gene and is expressed
RT   in cells in the oligodendrocyte lineage in the brain.";
RL   J. Biol. Chem. 268:4930-4938(1993).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 135-157.
RX   MEDLINE=89252919; PubMed=2470651; DOI=10.1016/0378-1119(89)90380-6;
RA   Miura M., Tamura T.A., Aoyama A., Mikoshiba K.;
RT   "The promoter elements of the mouse myelin basic protein gene function
RT   efficiently in NG108-15 neuronal/glial cells.";
RL   Gene 75:31-38(1989).
RN   [10]
RP   PROTEIN SEQUENCE OF 146-157; 164-175; 196-205 AND 211-222, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-224.
RX   MEDLINE=88196094; PubMed=2452084;
RA   Okano H., Tamura T., Miura M., Aoyama A., Ikenaka K., Oshimura M.,
RA   Mikoshiba K.;
RT   "Gene organization and transcription of duplicated MBP genes of myelin
RT   deficient (shi(mld)) mutant mouse.";
RL   EMBO J. 7:77-83(1988).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 193-222.
RX   MEDLINE=84119431; PubMed=6198644; DOI=10.1073/pnas.81.1.18;
RA   Zeller N.K., Hunkeler M.J., Campagnoni A.T., Sprague J.,
RA   Lazzarini R.A.;
RT   "Characterization of mouse myelin basic protein messenger RNAs with a
RT   myelin basic protein cDNA clone.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:18-22(1984).
RN   [13]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 6 AND 9).
RX   MEDLINE=86259714; PubMed=2425357; DOI=10.1073/pnas.83.13.4962;
RA   Kamholz J., de Ferra F., Puckett C., Lazzarini R.A.;
RT   "Identification of three forms of human myelin basic protein by cDNA
RT   cloning.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:4962-4966(1986).
RN   [14]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 10 AND 11).
RC   TISSUE=Spinal cord;
RX   MEDLINE=91162193; PubMed=1705957;
RX   DOI=10.1111/j.1471-4159.1991.tb11414.x;
RA   Aruga J., Okano H., Mikoshiba K.;
RT   "Identification of the new isoforms of mouse myelin basic protein: the
RT   existence of exon 5a.";
RL   J. Neurochem. 56:1222-1226(1991).
RN   [15]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 12 AND 13).
RC   TISSUE=Embryonic brain;
RX   MEDLINE=93203893; PubMed=7681106;
RX   DOI=10.1111/j.1471-4159.1993.tb03321.x;
RA   Nakajima K., Ikenaka K., Kagawa T., Aruga J., Nakao J., Nakahira K.,
RA   Shiota C., Kim S.U., Mikoshiba K.;
RT   "Novel isoforms of mouse myelin basic protein predominantly expressed
RT   in embryonic stage.";
RL   J. Neurochem. 60:1554-1563(1993).
RN   [16]
RP   DEVELOPMENTAL STAGE.
RX   MEDLINE=98409779; PubMed=9736652;
RA   Landry C.F., Pribyl T.M., Ellison J.A., Givogri M.I., Kampf K.,
RA   Campagnoni C.W., Campagnoni A.T.;
RT   "Embryonic expression of the myelin basic protein gene: identification
RT   of a promoter region that targets transgene expression to pioneer
RT   neurons.";
RL   J. Neurosci. 18:7315-7327(1998).
RN   [17]
RP   FUNCTION.
RX   MEDLINE=21018209; PubMed=11145205;
RA   Campagnoni A.T., Skoff R.P.;
RT   "The pathobiology of myelin mutants reveal novel biological functions
RT   of the MBP and PLP genes.";
RL   Brain Pathol. 11:74-91(2001).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144; SER-201 AND
RP   THR-229, AND MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172 AND SER-178, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15648052; DOI=10.1002/pmic.200401066;
RA   Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA   Hart G.W., Burlingame A.L.;
RT   "Quantitative analysis of both protein expression and serine /
RT   threonine post-translational modifications through stable isotope
RT   labeling with dithiothreitol.";
RL   Proteomics 5:388-398(2005).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-199, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [22]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-167, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RA   Lubec G., Kang S.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [24]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: The classic group of MBP isoforms (isoform 4-isoform 13)
CC       are with PLP the most abundant protein components of the myelin
CC       membrane in the CNS, AND MASS SPECTROMETRY. They have a role in
CC       both its formation and stabilization. The non-classic group of MBP
CC       isoforms (isoform 1-isoform 3/Golli-MBPs) may preferentially have
CC       a role in the early developing brain long before myelination,
CC       maybe as components of transcriptional complexes, and may also be
CC       involved in signaling pathways in T-cells and neural cells.
CC       Differential splicing events combined to optional post-
CC       translational modifications give a wide spectrum of isomers, with
CC       each of them potentially having a specialized function.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 13: Myelin membrane; Peripheral
CC       membrane protein; Cytoplasmic side.
CC   -!- SUBCELLULAR LOCATION: Isoform 12: Myelin membrane; Peripheral
CC       membrane protein; Cytoplasmic side.
CC   -!- SUBCELLULAR LOCATION: Isoform 11: Myelin membrane; Peripheral
CC       membrane protein; Cytoplasmic side.
CC   -!- SUBCELLULAR LOCATION: Isoform 10: Myelin membrane; Peripheral
CC       membrane protein; Cytoplasmic side.
CC   -!- SUBCELLULAR LOCATION: Isoform 9: Myelin membrane; Peripheral
CC       membrane protein; Cytoplasmic side.
CC   -!- SUBCELLULAR LOCATION: Isoform 8: Myelin membrane; Peripheral
CC       membrane protein; Cytoplasmic side.
CC   -!- SUBCELLULAR LOCATION: Isoform 7: Myelin membrane; Peripheral
CC       membrane protein; Cytoplasmic side.
CC   -!- SUBCELLULAR LOCATION: Isoform 6: Myelin membrane; Peripheral
CC       membrane protein; Cytoplasmic side.
CC   -!- SUBCELLULAR LOCATION: Isoform 5: Myelin membrane; Peripheral
CC       membrane protein; Cytoplasmic side.
CC   -!- SUBCELLULAR LOCATION: Isoform 4: Myelin membrane; Peripheral
CC       membrane protein; Cytoplasmic side.
CC   -!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Nucleus.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus.
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=13;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1; Synonyms=Golli-MBP1, J37;
CC         IsoId=P04370-1; Sequence=Displayed;
CC       Name=2; Synonyms=Golli-MBP2, BG21, HMBPR;
CC         IsoId=P04370-2; Sequence=VSP_003314;
CC       Name=3; Synonyms=Golli-MBP3, TP8;
CC         IsoId=P04370-3; Sequence=VSP_003313;
CC       Name=4; Synonyms=21.5-kDa;
CC         IsoId=P04370-4; Sequence=VSP_003312, VSP_003315, VSP_003319;
CC         Note=Met-1 is removed. Contains N-acetylalanine at position 2;
CC       Name=5; Synonyms=18.5-kDa;
CC         IsoId=P04370-5; Sequence=VSP_003312, VSP_003319;
CC         Note=Met-1 is removed. Contains N-acetylalanine at position 2;
CC       Name=6; Synonyms=17-kDa-a;
CC         IsoId=P04370-6; Sequence=VSP_003312, VSP_003315, VSP_003318;
CC         Note=Met-1 is removed. Contains N-acetylalanine at position 2;
CC       Name=7; Synonyms=17-kDa-b;
CC         IsoId=P04370-7; Sequence=VSP_003312, VSP_003320;
CC         Note=Met-1 is removed. Contains N-acetylalanine at position 2;
CC       Name=8; Synonyms=14-kDa;
CC         IsoId=P04370-8; Sequence=VSP_003312, VSP_003318;
CC         Note=Met-1 is removed. Contains N-acetylalanine at position 2;
CC       Name=9;
CC         IsoId=P04370-9; Sequence=VSP_003312, VSP_003315, VSP_003320;
CC         Note=Met-1 is removed. Contains N-acetylalanine at position 2;
CC       Name=10; Synonyms=21-kDa;
CC         IsoId=P04370-10; Sequence=VSP_003312, VSP_003317;
CC       Name=11; Synonyms=19.7-kDa;
CC         IsoId=P04370-11; Sequence=VSP_003312, VSP_003315, VSP_003316;
CC       Name=12; Synonyms=15.6-kDa;
CC         IsoId=P04370-13; Sequence=VSP_003312, VSP_003315;
CC       Name=13; Synonyms=13-kDa;
CC         IsoId=P04370-14; Sequence=VSP_003312;
CC   -!- TISSUE SPECIFICITY: In the embryo, isoform 1-isoform 3 are found
CC       in neurons within the central nervous system (primarily in pioneer
CC       neurons important in the formation of the cortex) and the
CC       peripheral nervous system. They are also expressed in the thymus,
CC       gut, lung and kidney. In the adult, isoform 1-isoform 3 are highly
CC       expressed in the brain (mainly in brain regions rich in
CC       oligodendrocytes) and spleen. Lower levels are seen in the heart,
CC       kidney and lung. Isoform 2 is also found in cells of the immune
CC       system. The isoforms missing the 134 first amino acids (isoform 4-
CC       isoform 13) are almost exclusively produced in the myelin-forming
CC       cells, the mature oligodendrocytes.
CC   -!- DEVELOPMENTAL STAGE: The differential expression of MBP isoforms
CC       is developmentally regulated. Isoform 2 and isoform 3 are first
CC       expressed during embryonic stages (as early as at embryonic day
CC       11.5), expression of isoform 1 is turned on shortly after birth.
CC       Expression of the isoforms missing the 134 first amino acids
CC       occurs later, presumably as the oligodendrocytes approach their
CC       terminally differentiated state.
CC   -!- PTM: As in other animals, several charge isomers may be produced
CC       as a result of optional post-translatonial modifications, such as
CC       phosphorylation of serine or threonine residues, deamidation of
CC       glutamine or asparagine residues, citrullination and methylation
CC       of arginine residues.
CC   -!- PTM: Methylated on arginine residues; decreases with the age of
CC       the animal, making MBP more cationic.
CC   -!- DISEASE: Note=Defects in Mbp are a cause of dysmyelinating
CC       diseases such as the shiverer (SHI) and myelin deficient (MLD)
CC       diseases characterized by decreased myelination in the CNS,
CC       tremors, and convulsions of progressively increasing severity
CC       leading to early death. The shiverer mice only express isoform 2,
CC       the MLD mice have a reduced amount of Mbp.
CC   -!- SIMILARITY: Belongs to the myelin basic protein family.
CC   -----------------------------------------------------------------------
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DR   EMBL; M11533; AAA39496.1; -; Genomic_DNA.
DR   EMBL; M11291; AAA39496.1; JOINED; Genomic_DNA.
DR   EMBL; M11529; AAA39496.1; JOINED; Genomic_DNA.
DR   EMBL; M11530; AAA39496.1; JOINED; Genomic_DNA.
DR   EMBL; M11531; AAA39496.1; JOINED; Genomic_DNA.
DR   EMBL; M11532; AAA39496.1; JOINED; Genomic_DNA.
DR   EMBL; M11533; AAA39497.1; -; Genomic_DNA.
DR   EMBL; M11291; AAA39497.1; JOINED; Genomic_DNA.
DR   EMBL; M11529; AAA39497.1; JOINED; Genomic_DNA.
DR   EMBL; M11530; AAA39497.1; JOINED; Genomic_DNA.
DR   EMBL; M11531; AAA39497.1; JOINED; Genomic_DNA.
DR   EMBL; L00404; AAA39499.1; -; Genomic_DNA.
DR   EMBL; L00398; AAA39499.1; JOINED; Genomic_DNA.
DR   EMBL; L00400; AAA39499.1; JOINED; Genomic_DNA.
DR   EMBL; L00401; AAA39499.1; JOINED; Genomic_DNA.
DR   EMBL; L00402; AAA39499.1; JOINED; Genomic_DNA.
DR   EMBL; L00404; AAA39500.1; -; Genomic_DNA.
DR   EMBL; L00398; AAA39500.1; JOINED; Genomic_DNA.
DR   EMBL; L00399; AAA39500.1; JOINED; Genomic_DNA.
DR   EMBL; L00400; AAA39500.1; JOINED; Genomic_DNA.
DR   EMBL; L00401; AAA39500.1; JOINED; Genomic_DNA.
DR   EMBL; L00402; AAA39500.1; JOINED; Genomic_DNA.
DR   EMBL; L00404; AAA39501.1; -; Genomic_DNA.
DR   EMBL; L00398; AAA39501.1; JOINED; Genomic_DNA.
DR   EMBL; L00400; AAA39501.1; JOINED; Genomic_DNA.
DR   EMBL; L00401; AAA39501.1; JOINED; Genomic_DNA.
DR   EMBL; L00402; AAA39501.1; JOINED; Genomic_DNA.
DR   EMBL; L00403; AAA39501.1; JOINED; Genomic_DNA.
DR   EMBL; L00404; AAA39502.1; -; Genomic_DNA.
DR   EMBL; L00398; AAA39502.1; JOINED; Genomic_DNA.
DR   EMBL; L00399; AAA39502.1; JOINED; Genomic_DNA.
DR   EMBL; L00400; AAA39502.1; JOINED; Genomic_DNA.
DR   EMBL; L00401; AAA39502.1; JOINED; Genomic_DNA.
DR   EMBL; L00402; AAA39502.1; JOINED; Genomic_DNA.
DR   EMBL; L00403; AAA39502.1; JOINED; Genomic_DNA.
DR   EMBL; M15060; AAB59711.1; -; mRNA.
DR   EMBL; M15062; AAB59712.1; -; mRNA.
DR   EMBL; X67319; CAA47733.1; -; mRNA.
DR   EMBL; L07507; AAA37720.1; -; mRNA.
DR   EMBL; L07508; AAA37721.1; -; mRNA.
DR   EMBL; L07509; AAA37722.1; -; mRNA.
DR   EMBL; L07505; AAA37719.1; -; Genomic_DNA.
DR   EMBL; L07504; AAA37719.1; JOINED; Genomic_DNA.
DR   EMBL; AK005129; BAB23830.1; -; mRNA.
DR   EMBL; BC004704; AAH04704.1; -; mRNA.
DR   EMBL; M24410; AAA39498.1; -; Genomic_DNA.
DR   EMBL; M36275; AAA39504.1; -; Genomic_DNA.
DR   EMBL; K00989; AAA39495.1; -; mRNA.
DR   EMBL; M20010; AAA39503.1; -; mRNA.
DR   IPI; IPI00115240; -.
DR   IPI; IPI00223375; -.
DR   IPI; IPI00223376; -.
DR   IPI; IPI00223377; -.
DR   IPI; IPI00223378; -.
DR   IPI; IPI00223379; -.
DR   IPI; IPI00223380; -.
DR   IPI; IPI00223381; -.
DR   IPI; IPI00223382; -.
DR   IPI; IPI00223593; -.
DR   IPI; IPI00223594; -.
DR   IPI; IPI00223595; -.
DR   IPI; IPI00223596; -.
DR   PIR; A45421; MBMSB.
DR   RefSeq; NP_001020416.1; NM_001025245.1.
DR   RefSeq; NP_001020422.1; NM_001025251.2.
DR   RefSeq; NP_001020425.1; NM_001025254.2.
DR   RefSeq; NP_001020426.1; NM_001025255.2.
DR   RefSeq; NP_001020427.1; NM_001025256.2.
DR   RefSeq; NP_001020429.1; NM_001025258.2.
DR   RefSeq; NP_001020430.1; NM_001025259.2.
DR   RefSeq; NP_034907.1; NM_010777.3.
DR   UniGene; Mm.252063; -.
DR   UniGene; Mm.454459; -.
DR   ProteinModelPortal; P04370; -.
DR   DisProt; DP00237; -.
DR   STRING; P04370; -.
DR   PhosphoSite; P04370; -.
DR   PRIDE; P04370; -.
DR   Ensembl; ENSMUST00000047865; ENSMUSP00000046185; ENSMUSG00000041607.
DR   Ensembl; ENSMUST00000062446; ENSMUSP00000053495; ENSMUSG00000041607.
DR   Ensembl; ENSMUST00000075372; ENSMUSP00000074836; ENSMUSG00000041607.
DR   Ensembl; ENSMUST00000080658; ENSMUSP00000079488; ENSMUSG00000041607.
DR   Ensembl; ENSMUST00000091789; ENSMUSP00000089393; ENSMUSG00000041607.
DR   Ensembl; ENSMUST00000102812; ENSMUSP00000099876; ENSMUSG00000041607.
DR   Ensembl; ENSMUST00000114673; ENSMUSP00000110321; ENSMUSG00000041607.
DR   Ensembl; ENSMUST00000114674; ENSMUSP00000110322; ENSMUSG00000041607.
DR   Ensembl; ENSMUST00000114678; ENSMUSP00000110326; ENSMUSG00000041607.
DR   Ensembl; ENSMUST00000114681; ENSMUSP00000110329; ENSMUSG00000041607.
DR   GeneID; 17196; -.
DR   KEGG; mmu:17196; -.
DR   UCSC; uc008fts.1; mouse.
DR   UCSC; uc008ftu.1; mouse.
DR   UCSC; uc008ftv.1; mouse.
DR   UCSC; uc008ftw.1; mouse.
DR   UCSC; uc008fty.1; mouse.
DR   CTD; 17196; -.
DR   MGI; MGI:96925; Mbp.
DR   eggNOG; roNOG05523; -.
DR   GeneTree; ENSGT00390000014772; -.
DR   HOVERGEN; HBG008347; -.
DR   InParanoid; P04370; -.
DR   OMA; DAHREGH; -.
DR   OrthoDB; EOG4S1T86; -.
DR   PhylomeDB; P04370; -.
DR   NextBio; 291554; -.
DR   PMAP-CutDB; P04370; -.
DR   ArrayExpress; P04370; -.
DR   Bgee; P04370; -.
DR   CleanEx; MM_MBP; -.
DR   Genevestigator; P04370; -.
DR   GermOnline; ENSMUSG00000041607; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033269; C:internode region of axon; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042552; P:myelination; IDA:MGI.
DR   InterPro; IPR000548; Myelin_BP.
DR   PANTHER; PTHR11429; Myelin_BP; 1.
DR   Pfam; PF01669; Myelin_MBP; 1.
DR   PRINTS; PR00212; MYELINMBP.
DR   PROSITE; PS00569; MYELIN_MBP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Autoimmune encephalomyelitis;
KW   Cell membrane; Citrullination; Cytoplasm; Direct protein sequencing;
KW   Membrane; Methylation; Nucleus; Phosphoprotein.
FT   CHAIN         1    250       Myelin basic protein.
FT                                /FTId=PRO_0000158991.
FT   MOD_RES      96     96       Phosphoserine.
FT   MOD_RES     141    141       Phosphoserine (By similarity).
FT   MOD_RES     144    144       Phosphoserine.
FT   MOD_RES     157    157       Citrulline (By similarity).
FT   MOD_RES     163    163       Citrulline (By similarity).
FT   MOD_RES     167    167       Phosphothreonine.
FT   MOD_RES     172    172       Phosphoserine.
FT   MOD_RES     178    178       Phosphoserine.
FT   MOD_RES     188    188       Phosphoserine (By similarity).
FT   MOD_RES     199    199       Phosphotyrosine.
FT   MOD_RES     201    201       Phosphoserine.
FT   MOD_RES     226    226       Phosphothreonine (By similarity).
FT   MOD_RES     229    229       Phosphothreonine.
FT   MOD_RES     234    234       Deamidated glutamine (By similarity).
FT   MOD_RES     239    239       Citrulline (By similarity).
FT   MOD_RES     241    241       Phosphoserine (By similarity).
FT   MOD_RES     245    245       Phosphoserine.
FT   MOD_RES     250    250       Citrulline (By similarity).
FT   VAR_SEQ       1    133       Missing (in isoform 4, isoform 5, isoform
FT                                6, isoform 7, isoform 8, isoform 9,
FT                                isoform 10, isoform 11, isoform 12 and
FT                                isoform 13).
FT                                /FTId=VSP_003312.
FT   VAR_SEQ      48    250       EADAIQNNGTSAEDTAVTDSKHTADPKNNWQGAHPADPGNR
FT                                PHLIRLFSRDAPGREDNTFKDRPSESDELQTIQEDPTAASG
FT                                GLDVMASQKRPSQRSKYLATASTMDHARHGFLPRHRDTGIL
FT                                DSIGRFFSGDRGAPKRGSGKDSHTRTTHYGSLPQKSQHGRT
FT                                QDENPVVHFFKNIVTPRTPPPSQGKGGRDSRSGSPMARR
FT                                -> LTHENYPLWLPAPEVAARPDPR (in isoform 3).
FT                                /FTId=VSP_003313.
FT   VAR_SEQ     190    190       K -> KVPWLKQSRSPLPSHARSRPGLCHMYK (in
FT                                isoform 4, isoform 6, isoform 9, isoform
FT                                11 and isoform 12).
FT                                /FTId=VSP_003315.
FT   VAR_SEQ     191    250       DSHTRTTHYGSLPQKSQHGRTQDENPVVHFFKNIVTPRTPP
FT                                PSQGKGGRDSRSGSPMARR -> VSSEP (in isoform
FT                                2).
FT                                /FTId=VSP_003314.
FT   VAR_SEQ     236    236       K -> KDFVPGDHHVNVSVVTVSFSSSQGRGLSLSRFSWGA
FT                                EGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTLSKIFKL
FT                                (in isoform 10).
FT                                /FTId=VSP_003317.
FT   VAR_SEQ     236    236       K -> KDFVPGDHHVNVSVVTVSFSSSQGRGLSLSRFSW
FT                                (in isoform 11).
FT                                /FTId=VSP_003316.
FT   VAR_SEQ     236    236       K -> KGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKG
FT                                FKGAYDAQGTLSKIFKL (in isoform 4 and
FT                                isoform 5).
FT                                /FTId=VSP_003319.
FT   VAR_SEQ     236    236       K -> KGRGLSLSRFSW (in isoform 6 and
FT                                isoform 8).
FT                                /FTId=VSP_003318.
FT   VAR_SEQ     236    236       K -> KGAEGQKPGFGYGGRASDYKSAHKGFKGAYDAQGTL
FT                                SKIFKL (in isoform 7 and isoform 9).
FT                                /FTId=VSP_003320.
FT   CONFLICT    204    205       QK -> HN (in Ref. 15).
SQ   SEQUENCE   250 AA;  27168 MW;  B418ED11C27B0C43 CRC64;
     MGNHSGKREL SAEKASKDGE IHRGEAGKKR SVGKLSQTAS EDSDVFGEAD AIQNNGTSAE
     DTAVTDSKHT ADPKNNWQGA HPADPGNRPH LIRLFSRDAP GREDNTFKDR PSESDELQTI
     QEDPTAASGG LDVMASQKRP SQRSKYLATA STMDHARHGF LPRHRDTGIL DSIGRFFSGD
     RGAPKRGSGK DSHTRTTHYG SLPQKSQHGR TQDENPVVHF FKNIVTPRTP PPSQGKGGRD
     SRSGSPMARR
//
ID   ARAF_MOUSE              Reviewed;         604 AA.
AC   P04627; B1AUN9; Q99J44; Q9CTT5; Q9D6R6; Q9DBU7;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2002, sequence version 2.
DT   08-MAR-2011, entry version 131.
DE   RecName: Full=Serine/threonine-protein kinase A-Raf;
DE            EC=2.7.11.1;
DE   AltName: Full=Proto-oncogene A-Raf;
GN   Name=Araf; Synonyms=A-raf, Araf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-283.
RC   STRAIN=C57BL/6J; TISSUE=Lung, Tongue, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 168-604.
RX   MEDLINE=87064566; PubMed=3491291;
RA   Huleihel M., Goldsborough M., Cleveland J., Gunnell M., Bonner T.,
RA   Rapp U.R.;
RT   "Characterization of murine A-raf, a new oncogene related to the v-raf
RT   oncogene.";
RL   Mol. Cell. Biol. 6:2655-2662(1986).
CC   -!- FUNCTION: Involved in the transduction of mitogenic signals from
CC       the cell membrane to the nucleus.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
CC   -!- SUBUNIT: Interacts with TH1L/NELFD (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. RAF subfamily.
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 RBD (Ras-binding) domain.
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DR   EMBL; AL671885; CAM14589.1; -; Genomic_DNA.
DR   EMBL; BC004757; AAH04757.1; -; mRNA.
DR   EMBL; AK004741; BAB23522.1; -; mRNA.
DR   EMBL; AK010060; BAB26674.1; -; mRNA.
DR   EMBL; AK020547; BAB32131.3; -; mRNA.
DR   EMBL; D00024; BAA00018.1; -; mRNA.
DR   IPI; IPI00320608; -.
DR   PIR; A25382; TVMSRF.
DR   RefSeq; NP_001153117.1; NM_001159645.1.
DR   RefSeq; NP_033833.1; NM_009703.2.
DR   UniGene; Mm.220946; -.
DR   ProteinModelPortal; P04627; -.
DR   SMR; P04627; 20-91, 96-146, 299-604.
DR   DIP; DIP-1070N; -.
DR   IntAct; P04627; 2.
DR   MINT; MINT-1582260; -.
DR   STRING; P04627; -.
DR   PhosphoSite; P04627; -.
DR   PRIDE; P04627; -.
DR   Ensembl; ENSMUST00000001155; ENSMUSP00000001155; ENSMUSG00000001127.
DR   GeneID; 11836; -.
DR   KEGG; mmu:11836; -.
DR   UCSC; uc009stu.1; mouse.
DR   CTD; 11836; -.
DR   MGI; MGI:88065; Araf.
DR   eggNOG; roNOG10943; -.
DR   HOGENOM; HBG506535; -.
DR   HOVERGEN; HBG001886; -.
DR   InParanoid; P04627; -.
DR   OMA; HVSETKF; -.
DR   OrthoDB; EOG4CRKZT; -.
DR   BRENDA; 2.7.10.2; 244.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 279767; -.
DR   ArrayExpress; P04627; -.
DR   Bgee; P04627; -.
DR   CleanEx; MM_ARAF; -.
DR   Genevestigator; P04627; -.
DR   GermOnline; ENSMUSG00000001127; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005057; F:receptor signaling protein activity; IEA:InterPro.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR003116; Raf-like_ras-bd.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF02196; RBD; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00455; RBD; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50898; RBD; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Proto-oncogene; Serine/threonine-protein kinase;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    604       Serine/threonine-protein kinase A-Raf.
FT                                /FTId=PRO_0000085623.
FT   DOMAIN       19     91       RBD.
FT   DOMAIN      308    568       Protein kinase.
FT   ZN_FING      98    144       Phorbol-ester/DAG-type.
FT   NP_BIND     314    322       ATP (By similarity).
FT   ACT_SITE    427    427       Proton acceptor (By similarity).
FT   METAL        99     99       Zinc 1 (By similarity).
FT   METAL       112    112       Zinc 2 (By similarity).
FT   METAL       115    115       Zinc 2 (By similarity).
FT   METAL       125    125       Zinc 1 (By similarity).
FT   METAL       128    128       Zinc 1 (By similarity).
FT   METAL       133    133       Zinc 2 (By similarity).
FT   METAL       136    136       Zinc 2 (By similarity).
FT   METAL       144    144       Zinc 1 (By similarity).
FT   BINDING     334    334       ATP (By similarity).
FT   MOD_RES     186    186       Phosphoserine (By similarity).
FT   MOD_RES     213    213       Phosphothreonine (By similarity).
FT   MOD_RES     215    215       Phosphothreonine (By similarity).
FT   MOD_RES     255    255       Phosphoserine (By similarity).
FT   MOD_RES     316    316       Phosphothreonine (By similarity).
FT   MOD_RES     578    578       Phosphoserine (By similarity).
FT   MOD_RES     580    580       Phosphoserine (By similarity).
FT   CONFLICT    169    169       E -> K (in Ref. 4; BAA00018).
FT   CONFLICT    186    186       S -> R (in Ref. 3; BAB23522/BAB26674).
FT   CONFLICT    326    326       R -> L (in Ref. 4; BAA00018).
SQ   SEQUENCE   604 AA;  67581 MW;  05F8262F99DDD087 CRC64;
     MEPPRGPPVS GAEPSRAVGT VKVYLPNKQR TVVTVREGMS VYDSLDKALK VRGLNQDCCV
     VYRLIKGRKT VTAWDTAIAP LDGEELIVEV LEDVPLTMHN FVRKTFFSLA FCDFCLKFLF
     HGFRCQTCGY KFHQHCSSKV PTVCVDMSTN RRQFYHSIQD LSGGSRQQEA PSNLSVNELL
     TPQGPSPFTQ QRDQEHFSFP APANPPLQRI RSTSTPNVHM VSTTAPMDSS LMQFTAQSFS
     TDAAGRGGDG APRGSPSPAS VSSGRKSPHS KLPSEQRERK SLADEKKKVK NLGYRDSGYY
     WEVPPSEVQL LKRIGTGSFG TVFRGRWHGD VAVKVLKVAQ PTAEQAQAFK NEMQVLRKTR
     HVNILLFMGF MTRPGFAIIT QWCEGSSLYH HLHVADTRFD MVQLIDVARQ TAQGMDYLHA
     KNIIHRDLKS NNIFLHEGLT VKIGDFGLAT VKTRWSGAQP LEQPSGSVLW MAAEVIRMQD
     PNPYSFQSDV YAYGVVLYEL MTGSLPYSHI GSRDQIIFMV GRGYLSPDLS KIFSNCPKAM
     RRLLTDCLKF QREERPLFPQ ILATIELLQR SLPKIERSAS EPSLHRTQAD ELPACLLSAA
     RLVP
//
ID   B3AT_MOUSE              Reviewed;         929 AA.
AC   P04919;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   08-MAR-2011, entry version 116.
DE   RecName: Full=Band 3 anion transport protein;
DE   AltName: Full=Anion exchange protein 1;
DE            Short=AE 1;
DE            Short=Anion exchanger 1;
DE   AltName: Full=MEB3;
DE   AltName: Full=Solute carrier family 4 member 1;
DE   AltName: CD_antigen=CD233;
GN   Name=Slc4a1; Synonyms=Ae1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=85268011; PubMed=2410791; DOI=10.1038/316234a0;
RA   Kopito R.R., Lodish H.F.;
RT   "Primary structure and transmembrane orientation of the murine anion
RT   exchange protein.";
RL   Nature 316:234-238(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=86034211; PubMed=3840489; DOI=10.1002/jcb.240290102;
RA   Kopito R.R., Lodish H.F.;
RT   "Structure of the murine anion exchange protein.";
RL   J. Cell. Biochem. 29:1-17(1985).
RN   [3]
RP   PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=87250387; PubMed=3036795;
RA   Kopito R.R., Andersson M., Lodish H.F.;
RT   "Structure and organization of the murine band 3 gene.";
RL   J. Biol. Chem. 262:8035-8040(1987).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RA   Kopito R.R.;
RL   Submitted (JUL-1987) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ERYTHROCYTE).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 11-929.
RX   MEDLINE=86274622; PubMed=3015590;
RA   Demuth D.R., Showe L.C., Ballantine M., Palumbo A., Fraser P.J.,
RA   Cioe L., Rovera G., Curtis P.J.;
RT   "Cloning and structural characterization of a human non-erythroid band
RT   3-like protein.";
RL   EMBO J. 5:1205-1214(1986).
RN   [7]
RP   PROTEIN SEQUENCE OF 33-47; 360-375; 382-395 AND 578-590.
RX   MEDLINE=89229233; PubMed=2713407; DOI=10.1016/0005-2736(89)90315-5;
RA   Raida M., Wendel J., Kojro E., Fahrenholz F., Fasold H., Legrum B.,
RA   Passow H.;
RT   "Major proteolytic fragments of the murine band 3 protein as obtained
RT   after in situ proteolysis.";
RL   Biochim. Biophys. Acta 980:291-298(1989).
RN   [8]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=9490702;
RA   Hassoun H., Hanada T., Lutchman M., Sahr K.E., Palek J., Hanspal M.,
RA   Chishti A.H.;
RT   "Complete deficiency of glycophorin A in red blood cells from mice
RT   with targeted inactivation of the band 3 (AE1) gene.";
RL   Blood 91:2146-2151(1998).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Band 3 is the major integral glycoprotein of the
CC       erythrocyte membrane. Band 3 has two functional domains. Its
CC       integral domain mediates a 1:1 exchange of inorganic anions across
CC       the membrane, whereas its cytoplasmic domain provides binding
CC       sites for cytoskeletal proteins, glycolytic enzymes, and
CC       hemoglobin.
CC   -!- SUBUNIT: A dimer in solution, it spans the membrane asymmetrically
CC       and appears to be tetrameric.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Erythrocyte;
CC         IsoId=P04919-1; Sequence=Displayed;
CC       Name=Kidney;
CC         IsoId=P04919-2; Sequence=VSP_000454;
CC   -!- TISSUE SPECIFICITY: Erythrocytes.
CC   -!- DISRUPTION PHENOTYPE: Gypa is not incorporated in the erythrocyte
CC       membrane.
CC   -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
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DR   EMBL; X02677; CAA26506.1; -; mRNA.
DR   EMBL; M29379; AAA37187.1; -; mRNA.
DR   EMBL; J02756; AAA37278.1; -; Genomic_DNA.
DR   EMBL; BC052419; AAH52419.1; -; mRNA.
DR   EMBL; BC053429; AAH53429.1; -; mRNA.
DR   EMBL; X03917; CAA27555.1; -; mRNA.
DR   IPI; IPI00120761; -.
DR   IPI; IPI00230594; -.
DR   PIR; A25314; A25314.
DR   RefSeq; NP_035533.1; NM_011403.2.
DR   UniGene; Mm.7248; -.
DR   ProteinModelPortal; P04919; -.
DR   SMR; P04919; 70-368, 408-449, 821-853.
DR   STRING; P04919; -.
DR   PhosphoSite; P04919; -.
DR   PRIDE; P04919; -.
DR   Ensembl; ENSMUST00000006749; ENSMUSP00000006749; ENSMUSG00000006574.
DR   GeneID; 20533; -.
DR   KEGG; mmu:20533; -.
DR   UCSC; uc007lrp.1; mouse.
DR   CTD; 20533; -.
DR   MGI; MGI:109393; Slc4a1.
DR   eggNOG; roNOG14874; -.
DR   HOGENOM; HBG355640; -.
DR   HOVERGEN; HBG004326; -.
DR   InParanoid; P04919; -.
DR   OMA; WSLLELQ; -.
DR   OrthoDB; EOG4W0XCF; -.
DR   PhylomeDB; P04919; -.
DR   NextBio; 298795; -.
DR   ArrayExpress; P04919; -.
DR   Bgee; P04919; -.
DR   Genevestigator; P04919; -.
DR   GermOnline; ENSMUSG00000006574; Mus musculus.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR   GO; GO:0015108; F:chloride transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
DR   InterPro; IPR001717; Anion_exchange.
DR   InterPro; IPR002977; Anion_exchange_1.
DR   InterPro; IPR018241; Anion_exchange_CS.
DR   InterPro; IPR011531; HCO3_transpt_C.
DR   InterPro; IPR013769; HCO3_transpt_cyt.
DR   InterPro; IPR003020; HCO3_transpt_euk.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   Gene3D; G3DSA:3.40.1100.10; HCO3_transpt_cyt; 1.
DR   PANTHER; PTHR11453; HCO3_transpt_euk; 1.
DR   Pfam; PF07565; Band_3_cyto; 1.
DR   Pfam; PF00955; HCO3_cotransp; 2.
DR   PRINTS; PR00165; ANIONEXCHNGR.
DR   PRINTS; PR01187; ANIONEXHNGR1.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   SUPFAM; SSF55804; PTrfase/Anion_transptr; 1.
DR   TIGRFAMs; TIGR00834; ae; 1.
DR   PROSITE; PS00219; ANION_EXCHANGER_1; 1.
DR   PROSITE; PS00220; ANION_EXCHANGER_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Anion exchange; Direct protein sequencing;
KW   Glycoprotein; Ion transport; Lipoprotein; Membrane; Palmitate;
KW   Phosphoprotein; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    929       Band 3 anion transport protein.
FT                                /FTId=PRO_0000079210.
FT   TOPO_DOM      1    422       Cytoplasmic (Potential).
FT   TRANSMEM    423    443       Helical; (Potential).
FT   TRANSMEM    456    475       Helical; (Potential).
FT   TRANSMEM    479    498       Helical; (Potential).
FT   TRANSMEM    510    529       Helical; (Potential).
FT   TRANSMEM    542    560       Helical; (Potential).
FT   TOPO_DOM    561    586       Extracellular (Potential).
FT   TRANSMEM    587    606       Helical; (Potential).
FT   TOPO_DOM    607    621       Cytoplasmic (Potential).
FT   TRANSMEM    622    642       Helical; (Potential).
FT   TOPO_DOM    643    678       Extracellular (Potential).
FT   TRANSMEM    679    698       Helical; (Potential).
FT   TRANSMEM    717    737       Helical; (Potential).
FT   TRANSMEM    781    798       Helical; (Potential).
FT   TRANSMEM    803    824       Helical; (Potential).
FT   TRANSMEM    862    883       Helical; (Potential).
FT   REGION      423    929       Membrane (anion exchange).
FT   MOD_RES      18     18       Phosphoserine.
FT   MOD_RES     363    363       Phosphoserine.
FT   LIPID       861    861       S-palmitoyl cysteine (By similarity).
FT   CARBOHYD    660    660       N-linked (GlcNAc...) (Probable).
FT   VAR_SEQ       1     79       Missing (in isoform Kidney).
FT                                /FTId=VSP_000454.
FT   CONFLICT    467    467       G -> S (in Ref. 6; CAA27555).
SQ   SEQUENCE   929 AA;  103136 MW;  5C0E281C394FB614 CRC64;
     MGDMRDHEEV LEIPDRDSEE ELENIIGQIA YRDLTIPVTE MQDPEALPTE QTATDYVPSS
     TSTPHPSSGQ VYVELQELMM DQRNQELQWV EAAHWIGLEE NLREDGVWGR PHLSYLTFWS
     LLELQKVFSK GTFLLGLAET SLAGVANHLL DCFIYEDQIR PQDREELLRA LLLKRSHAED
     LGNLEGVKPA VLTRSGGASE PLLPHQPSLE TQLYCGQAEG GSEGPSTSGT LKIPPDSETT
     LVLVGRANFL EKPVLGFVRL KEAVPLEDLV LPEPVGFLLV LLGPEAPHVD YTQLGRAAAT
     LMTERVFRIT ASMAHNREEL LRSLESFLDC SLVLPPTDAP SEKALLNLVP VQKELLRRRY
     LPSPAKPDPN LYNTLDLNGG KGGPGDEDDP LRRTGRIFGG LIRDIRRRYP YYLSDITDAL
     SPQVLAAVIF IYFAALSPAV TFGGLLGEKT RNLMGVSELL ISTAVQGILF ALLGAQPLLV
     LGFSGPLLVF EEAFFSFCES NNLEYIVGRA WIGFWLILLV MLVVAFEGSF LVQYISRYTQ
     EIFSFLISLI FIYETFSKLI KIFQDYPLQQ TYAPVVMKPK PQGPVPNTAL FSLVLMAGTF
     LLAMTLRKFK NSTYFPGKLR RVIGDFGVPI SILIMVLVDS FIKGTYTQKL SVPDGLKVSN
     SSARGWVIHP LGLYRLFPTW MMFASVLPAL LVFILIFLES QITTLIVSKP ERKMIKGSGF
     HLDLLLVVGM GGVAALFGMP WLSATTVRSV THANALTVMG KASGPGAAAQ IQEVKEQRIS
     GLLVSVLVGL SILMEPILSR IPLAVLFGIF LYMGVTSLSG IQLFDRILLL FKPPKYHPDV
     PFVKRVKTWR MHLFTGIQII CLAVLWVVKS TPASLALPFV LILTVPLRRL ILPLIFRELE
     LQCLDGDDAK VTFDEENGLD EYDEVPMPV
//
ID   ALDOC_MOUSE             Reviewed;         363 AA.
AC   P05063; Q64011; Q8CA91; Q99K96; Q9DBA4; Q9JK32;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   08-MAR-2011, entry version 117.
DE   RecName: Full=Fructose-bisphosphate aldolase C;
DE            EC=4.1.2.13;
DE   AltName: Full=Aldolase 3;
DE   AltName: Full=Brain-type aldolase;
DE   AltName: Full=Scrapie-responsive protein 2;
DE   AltName: Full=Zebrin II;
GN   Name=Aldoc; Synonyms=Aldo3, Scrg2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=95009537; PubMed=7925012;
RA   Ahn A.H., Dziennis S., Hawkes R., Herrup K.;
RT   "The cloning of zebrin II reveals its identity with aldolase C.";
RL   Development 120:2081-2090(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-227.
RX   MEDLINE=86192445; PubMed=3009179;
RX   DOI=10.1111/j.1432-1033.1986.tb09572.x;
RA   Paolella G., Buono P., Mancini P., Izzo P., Salvatore F.;
RT   "Structure and expression of mouse aldolase genes. Brain-specific
RT   aldolase C amino acid sequence is closely related to aldolase A.";
RL   Eur. J. Biochem. 156:229-235(1986).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-13; 29-57; 61-69; 73-96; 102-108; 112-134;
RP   154-215; 244-258; 260-289; 305-315; 319-330 AND 332-363, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 281-363, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=20185656; PubMed=10719228; DOI=10.1016/S0169-328X(00)00028-0;
RA   Dandoy-Dron F.C., Benboudjema L., Guillo F., Jaegly A., Jasmin C.,
RA   Dormont D., Tovey M.G., Dron M.;
RT   "Enhanced levels of scrapie responsive gene mRNA in BSE-infected mouse
RT   brain.";
RL   Brain Res. Mol. Brain Res. 76:173-179(2000).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-119, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RA   Lubec G., Kang S.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone
CC       phosphate + D-glyceraldehyde 3-phosphate.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC   -!- SUBUNIT: Homotetramer. Interacts with ATP6V1E1 (By similarity).
CC   -!- INTERACTION:
CC       P04156:PRNP (xeno); NbExp=1; IntAct=EBI-444845, EBI-977302;
CC   -!- TISSUE SPECIFICITY: Expressed exclusively in Purkinje cells in
CC       bands running from anterior to posterior across most of the
CC       cerebellum. Expressed at higher levels in the brains of BSE-
CC       infected animals.
CC   -!- DEVELOPMENTAL STAGE: Expression begins in the first week of
CC       postnatal life.
CC   -!- MISCELLANEOUS: In vertebrates, three forms of this ubiquitous
CC       glycolytic enzyme are found, aldolase A in muscle, aldolase B in
CC       liver and aldolase C in brain.
CC   -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; S72537; AAB32064.1; -; mRNA.
DR   EMBL; AK005077; BAB23801.1; -; mRNA.
DR   EMBL; AK039267; BAC30300.1; -; mRNA.
DR   EMBL; BC004802; AAH04802.1; -; mRNA.
DR   EMBL; BC008184; AAH08184.1; -; mRNA.
DR   EMBL; X03796; CAA27422.1; -; mRNA.
DR   EMBL; AJ132391; CAB77178.1; -; mRNA.
DR   IPI; IPI00119458; -.
DR   PIR; A25388; ADMSC.
DR   PIR; I53145; I53145.
DR   RefSeq; NP_033787.2; NM_009657.3.
DR   UniGene; Mm.7729; -.
DR   ProteinModelPortal; P05063; -.
DR   SMR; P05063; 3-344.
DR   IntAct; P05063; 5.
DR   STRING; P05063; -.
DR   PhosphoSite; P05063; -.
DR   REPRODUCTION-2DPAGE; IPI00119458; -.
DR   UCD-2DPAGE; P05063; -.
DR   PRIDE; P05063; -.
DR   Ensembl; ENSMUST00000017534; ENSMUSP00000017534; ENSMUSG00000017390.
DR   Ensembl; ENSMUST00000102478; ENSMUSP00000099536; ENSMUSG00000017390.
DR   GeneID; 11676; -.
DR   KEGG; mmu:11676; -.
DR   UCSC; uc007kiw.1; mouse.
DR   CTD; 11676; -.
DR   MGI; MGI:101863; Aldoc.
DR   eggNOG; roNOG15213; -.
DR   GeneTree; ENSGT00390000010235; -.
DR   HOGENOM; HBG559178; -.
DR   HOVERGEN; HBG002386; -.
DR   InParanoid; P05063; -.
DR   OMA; ACPIKYT; -.
DR   OrthoDB; EOG4X3H1J; -.
DR   BRENDA; 4.1.2.13; 244.
DR   NextBio; 279307; -.
DR   ArrayExpress; P05063; -.
DR   Bgee; P05063; -.
DR   CleanEx; MM_ALDOC; -.
DR   Genevestigator; P05063; -.
DR   GermOnline; ENSMUSG00000017390; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; ISS:UniProtKB.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR000741; Aldolase_I.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   PANTHER; PTHR11627; Aldolase_I; 1.
DR   Pfam; PF00274; Glycolytic; 1.
DR   PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Glycolysis; Lyase;
KW   Phosphoprotein; Schiff base.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    363       Fructose-bisphosphate aldolase C.
FT                                /FTId=PRO_0000216949.
FT   ACT_SITE    188    188       Proton acceptor (By similarity).
FT   ACT_SITE    230    230       Schiff-base intermediate with
FT                                dihydroxyacetone-P.
FT   BINDING      56     56       Substrate.
FT   BINDING     147    147       Substrate.
FT   SITE        363    363       Necessary for preference for fructose
FT                                1,6-bisphosphate over fructose 1-
FT                                phosphate.
FT   MOD_RES      39     39       Phosphoserine.
FT   MOD_RES     119    119       Phosphothreonine.
FT   MOD_RES     147    147       N6-acetyllysine (By similarity).
FT   CONFLICT     25     25       T -> A (in Ref. 3; AAH04802/AAH08184).
FT   CONFLICT     46     46       Q -> E (in Ref. 2; BAC30300).
FT   CONFLICT     62     62       V -> A (in Ref. 4; CAA27422).
FT   CONFLICT    113    113       V -> L (in Ref. 4; CAA27422).
FT   CONFLICT    201    201       R -> H (in Ref. 3; AAH04802/AAH08184).
FT   CONFLICT    280    280       A -> V (in Ref. 1; AAB32064).
FT   CONFLICT    358    358       I -> V (in Ref. 3; AAH04802/AAH08184).
SQ   SEQUENCE   363 AA;  39395 MW;  085C58AF163581C6 CRC64;
     MPHSYPALSA EQKKELSDIA LRIVTPGKGI LAADESVGSM AKRLSQIGVE NTEENRRLYR
     QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQD KGILVGIKVD KGVVPLAGTD
     GETTTQGLDG LLERCAQYKK DGADFAKWRC VLKISDRTPS ALAILENANV LARYASICQQ
     NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC
     PIKYSPEEIA MATVTALRRT VPPAVPGVTF LSGGQSEEEA SLNLNAINRC PLPRPWALTF
     SYGRALQASA LNAWRGQRDN AGAATEEFIK RAEMNGLAAQ GRYEGSGDGG AAAQSLYIAN
     HAY
//
ID   ALDOA_MOUSE             Reviewed;         364 AA.
AC   P05064;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 118.
DE   RecName: Full=Fructose-bisphosphate aldolase A;
DE            EC=4.1.2.13;
DE   AltName: Full=Aldolase 1;
DE   AltName: Full=Muscle-type aldolase;
GN   Name=Aldoa; Synonyms=Aldo1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129;
RX   MEDLINE=88096598; PubMed=3697100; DOI=10.1093/nar/15.24.10595;
RA   Mestek A., Stauffer J., Tolan D.R., Ciejek-Baez E.;
RT   "Sequence of a mouse brain aldolase A cDNA.";
RL   Nucleic Acids Res. 15:10595-10595(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-266 AND 295-364.
RX   MEDLINE=90307699; PubMed=2365699;
RA   Stauffer J.K., Colbert M.C., Ciejek-Baez E.;
RT   "Nonconservative utilization of aldolase A alternative promoters.";
RL   J. Biol. Chem. 265:11773-11782(1990).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-22; 29-57; 61-109; 112-134; 154-258; 260-312 AND
RP   323-364, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B.,
RA   Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 99-355.
RX   MEDLINE=86192445; PubMed=3009179;
RX   DOI=10.1111/j.1432-1033.1986.tb09572.x;
RA   Paolella G., Buono P., Mancini P., Izzo P., Salvatore F.;
RT   "Structure and expression of mouse aldolase genes. Brain-specific
RT   aldolase C amino acid sequence is closely related to aldolase A.";
RL   Eur. J. Biochem. 156:229-235(1986).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15648052; DOI=10.1002/pmic.200401066;
RA   Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA   Hart G.W., Burlingame A.L.;
RT   "Quantitative analysis of both protein expression and serine /
RT   threonine post-translational modifications through stable isotope
RT   labeling with dithiothreitol.";
RL   Proteomics 5:388-398(2005).
RN   [7]
RP   NITRATION [LARGE SCALE ANALYSIS] AT TYR-174, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16800626; DOI=10.1021/bi060474w;
RA   Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
RA   Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
RA   Squier T.C., Bigelow D.J.;
RT   "Endogenously nitrated proteins in mouse brain: links to
RT   neurodegenerative disease.";
RL   Biochemistry 45:8009-8022(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-39, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone
CC       phosphate + D-glyceraldehyde 3-phosphate.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- MISCELLANEOUS: In vertebrates, three forms of this ubiquitous
CC       glycolytic enzyme are found, aldolase A in muscle, aldolase B in
CC       liver and aldolase C in brain.
CC   -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X03797; CAA27423.1; -; mRNA.
DR   EMBL; BC043026; AAH43026.1; -; mRNA.
DR   EMBL; BC050896; AAH50896.1; -; mRNA.
DR   EMBL; J05517; AAA37210.2; -; Genomic_DNA.
DR   EMBL; Y00516; CAA68571.1; -; mRNA.
DR   IPI; IPI00221402; -.
DR   PIR; S06323; ADMSA.
DR   RefSeq; NP_001170779.1; NM_001177308.1.
DR   RefSeq; NP_031464.1; NM_007438.4.
DR   UniGene; Mm.275831; -.
DR   ProteinModelPortal; P05064; -.
DR   SMR; P05064; 5-344.
DR   IntAct; P05064; 8.
DR   STRING; P05064; -.
DR   PhosphoSite; P05064; -.
DR   SWISS-2DPAGE; P05064; -.
DR   COMPLUYEAST-2DPAGE; P05064; -.
DR   REPRODUCTION-2DPAGE; IPI00221402; -.
DR   REPRODUCTION-2DPAGE; P05064; -.
DR   PRIDE; P05064; -.
DR   Ensembl; ENSMUST00000032934; ENSMUSP00000032934; ENSMUSG00000030695.
DR   Ensembl; ENSMUST00000087566; ENSMUSP00000084846; ENSMUSG00000030695.
DR   Ensembl; ENSMUST00000106348; ENSMUSP00000101955; ENSMUSG00000030695.
DR   GeneID; 11674; -.
DR   KEGG; mmu:11674; -.
DR   UCSC; uc009jsu.1; mouse.
DR   CTD; 11674; -.
DR   MGI; MGI:87994; Aldoa.
DR   eggNOG; roNOG08752; -.
DR   HOVERGEN; HBG002386; -.
DR   InParanoid; P05064; -.
DR   OrthoDB; EOG4X3H1J; -.
DR   PhylomeDB; P05064; -.
DR   BRENDA; 4.1.2.13; 244.
DR   NextBio; 279303; -.
DR   ArrayExpress; P05064; -.
DR   Bgee; P05064; -.
DR   CleanEx; MM_ALDOA; -.
DR   Genevestigator; P05064; -.
DR   GermOnline; ENSMUSG00000030695; Mus musculus.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR000741; Aldolase_I.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   PANTHER; PTHR11627; Aldolase_I; 1.
DR   Pfam; PF00274; Glycolytic; 1.
DR   PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Glycolysis; Lyase; Nitration;
KW   Phosphoprotein; Schiff base.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    364       Fructose-bisphosphate aldolase A.
FT                                /FTId=PRO_0000216937.
FT   ACT_SITE    188    188       Proton acceptor (By similarity).
FT   ACT_SITE    230    230       Schiff-base intermediate with
FT                                dihydroxyacetone-P.
FT   BINDING      56     56       Substrate.
FT   BINDING     147    147       Substrate.
FT   SITE        364    364       Necessary for preference for fructose
FT                                1,6-bisphosphate over fructose 1-
FT                                phosphate.
FT   MOD_RES       5      5       Phosphotyrosine (By similarity).
FT   MOD_RES       9      9       Phosphothreonine (By similarity).
FT   MOD_RES      13     13       N6-acetyllysine (By similarity).
FT   MOD_RES      36     36       Phosphoserine.
FT   MOD_RES      37     37       Phosphothreonine (By similarity).
FT   MOD_RES      39     39       Phosphoserine.
FT   MOD_RES      42     42       N6-acetyllysine (By similarity).
FT   MOD_RES      46     46       Phosphoserine.
FT   MOD_RES      65     65       Phosphothreonine (By similarity).
FT   MOD_RES     108    108       N6-acetyllysine (By similarity).
FT   MOD_RES     174    174       Nitrated tyrosine.
FT   MOD_RES     204    204       Phosphotyrosine (By similarity).
FT   MOD_RES     223    223       Phosphotyrosine (By similarity).
FT   MOD_RES     235    235       Phosphothreonine (By similarity).
FT   MOD_RES     241    241       Phosphothreonine (By similarity).
FT   MOD_RES     330    330       N6-acetyllysine (By similarity).
FT   MOD_RES     354    354       Phosphoserine (By similarity).
FT   MOD_RES     356    356       Phosphoserine (By similarity).
FT   MOD_RES     364    364       Phosphotyrosine (By similarity).
FT   CONFLICT    281    281       S -> C (in Ref. 5; CAA27423).
SQ   SEQUENCE   364 AA;  39356 MW;  0D067F7E4C63E216 CRC64;
     MPHPYPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE NTEENRRFYR
     QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS KGGVVGIKVD KGVVPLAGTN
     GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKIGEHTPS ALAIMENANV LARYASICQQ
     NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC
     TQKFSNEEIA MATVTALRRT VPPAVTGVTF LSGGQSEEEA SINLNAINKC PLLKPWALTF
     SYGRALQASA LKAWGGKKEN LKAAQEEYIK RALANSLACQ GKYTPSGQSG AAASESLFIS
     NHAY
//
ID   KAPCA_MOUSE             Reviewed;         351 AA.
AC   P05132; Q9JID0;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 146.
DE   RecName: Full=cAMP-dependent protein kinase catalytic subunit alpha;
DE            Short=PKA C-alpha;
DE            EC=2.7.11.11;
GN   Name=Prkaca; Synonyms=Pkaca;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   MEDLINE=88186891; PubMed=2833513;
RA   Chrivia J.C., Uhler M.D., McKnight G.S.;
RT   "Characterization of genomic clones coding for the C alpha and C beta
RT   subunits of mouse cAMP-dependent protein kinase.";
RL   J. Biol. Chem. 263:5739-5744(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=86149293; PubMed=3456589; DOI=10.1073/pnas.83.5.1300;
RA   Uhler M.D., Carmichael D.F., Lee D.C., Chrivia J.C., Krebs E.G.,
RA   McKnight G.S.;
RT   "Isolation of cDNA clones coding for the catalytic subunit of mouse
RT   cAMP-dependent protein kinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:1300-1304(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-153 (ISOFORM 2).
RC   TISSUE=Testis;
RX   MEDLINE=20437760; PubMed=10982398;
RA   San Agustin J.T., Wilkerson C.G., Witman G.B.;
RT   "The unique catalytic subunit of sperm cAMP-dependent protein kinase
RT   is the product of an alternative C-alpha mRNA expressed specifically
RT   in spermatogenic cells.";
RL   Mol. Biol. Cell 11:3031-3044(2000).
RN   [5]
RP   MYRISTOYLATION AT GLY-2, PHOSPHORYLATION AT SER-11, AND DEAMIDATION AT
RP   ASN-3.
RX   MEDLINE=20580202; PubMed=11141074; DOI=10.1021/bi0021277;
RA   Tholey A., Pipkorn R., Bossemeyer D., Kinzel V., Reed J.;
RT   "Influence of myristoylation, phosphorylation, and deamidation on the
RT   structural behavior of the N-terminus of the catalytic subunit of
RT   cAMP-dependent protein kinase.";
RL   Biochemistry 40:225-231(2001).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-196, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX   MEDLINE=91320112; PubMed=1862342; DOI=10.1126/science.1862342;
RA   Knighton D.R., Zheng J., ten Eyck L.F., Ashford V.A., Xuong N.-H.,
RA   Taylor S.S., Sowadski J.M.;
RT   "Crystal structure of the catalytic subunit of cyclic adenosine
RT   monophosphate-dependent protein kinase.";
RL   Science 253:407-414(1991).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
RX   MEDLINE=93183878; PubMed=8443157; DOI=10.1021/bi00060a005;
RA   Zheng J., Knighton D.R., ten Eyck L.F., Karlsson R., Xuong N.-H.,
RA   Taylor S.S., Sowadski J.M.;
RT   "Crystal structure of the catalytic subunit of cAMP-dependent protein
RT   kinase complexed with MgATP and peptide inhibitor.";
RL   Biochemistry 32:2154-2161(1993).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF COMPLEX WITH INHIBITOR.
RX   MEDLINE=97263736; PubMed=9109651; DOI=10.1021/bi961947+;
RA   Narayana N., Cox S., Shaltiel S., Taylor S.S., Xuong N.;
RT   "Crystal structure of a polyhistidine-tagged recombinant catalytic
RT   subunit of cAMP-dependent protein kinase complexed with the peptide
RT   inhibitor PKI(5-24) and adenosine.";
RL   Biochemistry 36:4438-4448(1997).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX   MEDLINE=97411697; PubMed=9261084; DOI=10.1016/S0969-2126(97)00246-3;
RA   Narayana N., Cox S., Nguyen-Huu X., ten Eyck L.F., Taylor S.S.;
RT   "A binary complex of the catalytic subunit of cAMP-dependent protein
RT   kinase and adenosine further defines conformational flexibility.";
RL   Structure 5:921-935(1997).
CC   -!- FUNCTION: Phosphorylates a large number of substrates in the
CC       cytoplasm and the nucleus.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Activated by cAMP.
CC   -!- SUBUNIT: A number of inactive tetrameric holoenzymes are produced
CC       by the combination of homo- or heterodimers of the different
CC       regulatory subunits associated with two catalytic subunits. cAMP
CC       causes the dissociation of the inactive holoenzyme into a dimer of
CC       regulatory subunits bound to four cAMP and two free monomeric
CC       catalytic subunits.
CC   -!- INTERACTION:
CC       P00514:PRKAR1A (xeno); NbExp=1; IntAct=EBI-400564, EBI-1041635;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Translocates into the nucleus (monomeric
CC       catalytic subunit) (By similarity). The inactive holoenzyme is
CC       found in the cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=C-alpha-1;
CC         IsoId=P05132-1; Sequence=Displayed;
CC       Name=2; Synonyms=C-alpha-2, C-alpha-S, C(s);
CC         IsoId=P05132-2; Sequence=VSP_004760;
CC   -!- TISSUE SPECIFICITY: Isoform 2 is sperm specific.
CC   -!- PTM: Phosphorylated on threonine and serine residues.
CC       Phosphorylation on Thr-198 is required for full activity.
CC   -!- PTM: Asn-3 is partially deaminated to Asp-3 giving rise to 2 major
CC       isoelectric variants, called CB and CA respectively.
CC   -!- PTM: When myristoylated, Ser-11 is autophosphorylated probably in
CC       conjunction with deamidation of Asn-3.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. cAMP subfamily.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; M19960; AAA39937.1; -; Genomic_DNA.
DR   EMBL; M18240; AAA39937.1; JOINED; Genomic_DNA.
DR   EMBL; M18241; AAA39937.1; JOINED; Genomic_DNA.
DR   EMBL; M19953; AAA39937.1; JOINED; Genomic_DNA.
DR   EMBL; M19954; AAA39937.1; JOINED; Genomic_DNA.
DR   EMBL; M19955; AAA39937.1; JOINED; Genomic_DNA.
DR   EMBL; M19956; AAA39937.1; JOINED; Genomic_DNA.
DR   EMBL; M19957; AAA39937.1; JOINED; Genomic_DNA.
DR   EMBL; M19958; AAA39937.1; JOINED; Genomic_DNA.
DR   EMBL; M19959; AAA39937.1; JOINED; Genomic_DNA.
DR   EMBL; M12303; AAA39936.1; -; mRNA.
DR   EMBL; BC003238; AAH03238.1; -; mRNA.
DR   EMBL; BC054834; AAH54834.1; -; mRNA.
DR   EMBL; AF239743; AAF76425.1; -; mRNA.
DR   IPI; IPI00227900; -.
DR   IPI; IPI00230005; -.
DR   PIR; A28619; OKMSCA.
DR   RefSeq; NP_032880.1; NM_008854.4.
DR   UniGene; Mm.19111; -.
DR   PDB; 1APM; X-ray; 2.00 A; E=2-350.
DR   PDB; 1ATP; X-ray; 2.20 A; E=2-350.
DR   PDB; 1BKX; X-ray; 2.60 A; A=2-351.
DR   PDB; 1BX6; X-ray; 2.10 A; A=2-350.
DR   PDB; 1FMO; X-ray; 2.20 A; E=2-351.
DR   PDB; 1J3H; X-ray; 2.90 A; A/B=2-350.
DR   PDB; 1JBP; X-ray; 2.20 A; E=2-350.
DR   PDB; 1JLU; X-ray; 2.25 A; E=2-350.
DR   PDB; 1L3R; X-ray; 2.00 A; E=2-350.
DR   PDB; 1PVK; Model; -; B=16-351.
DR   PDB; 1RDQ; X-ray; 1.26 A; E=2-350.
DR   PDB; 1RE8; X-ray; 2.10 A; A=2-350.
DR   PDB; 1REJ; X-ray; 2.20 A; A=2-350.
DR   PDB; 1REK; X-ray; 2.30 A; A=2-350.
DR   PDB; 1SYK; X-ray; 2.80 A; A/B=2-351.
DR   PDB; 2CPK; X-ray; 2.70 A; E=2-351.
DR   PDB; 2ERZ; X-ray; 2.20 A; E=1-351.
DR   PDB; 2QCS; X-ray; 2.20 A; A=2-351.
DR   PDB; 2QUR; X-ray; 2.50 A; A=2-351.
DR   PDB; 2QVS; X-ray; 2.50 A; E=2-351.
DR   PDB; 3FHI; X-ray; 2.00 A; A=2-351.
DR   PDB; 3FJQ; X-ray; 1.60 A; E=2-351.
DR   PDB; 3IDB; X-ray; 1.62 A; A=2-351.
DR   PDB; 3IDC; X-ray; 2.70 A; A=2-351.
DR   PDB; 3O7L; X-ray; 2.80 A; B/D=2-351.
DR   PDB; 3OW3; X-ray; 1.90 A; A=2-351.
DR   PDBsum; 1APM; -.
DR   PDBsum; 1ATP; -.
DR   PDBsum; 1BKX; -.
DR   PDBsum; 1BX6; -.
DR   PDBsum; 1FMO; -.
DR   PDBsum; 1J3H; -.
DR   PDBsum; 1JBP; -.
DR   PDBsum; 1JLU; -.
DR   PDBsum; 1L3R; -.
DR   PDBsum; 1PVK; -.
DR   PDBsum; 1RDQ; -.
DR   PDBsum; 1RE8; -.
DR   PDBsum; 1REJ; -.
DR   PDBsum; 1REK; -.
DR   PDBsum; 1SYK; -.
DR   PDBsum; 2CPK; -.
DR   PDBsum; 2ERZ; -.
DR   PDBsum; 2QCS; -.
DR   PDBsum; 2QUR; -.
DR   PDBsum; 2QVS; -.
DR   PDBsum; 3FHI; -.
DR   PDBsum; 3FJQ; -.
DR   PDBsum; 3IDB; -.
DR   PDBsum; 3IDC; -.
DR   PDBsum; 3O7L; -.
DR   PDBsum; 3OW3; -.
DR   ProteinModelPortal; P05132; -.
DR   SMR; P05132; 16-351.
DR   DIP; DIP-6086N; -.
DR   IntAct; P05132; 5.
DR   MINT; MINT-4051347; -.
DR   STRING; P05132; -.
DR   PhosphoSite; P05132; -.
DR   PRIDE; P05132; -.
DR   Ensembl; ENSMUST00000005606; ENSMUSP00000005606; ENSMUSG00000005469.
DR   Ensembl; ENSMUST00000059266; ENSMUSP00000105424; ENSMUSG00000005469.
DR   GeneID; 18747; -.
DR   KEGG; mmu:18747; -.
DR   UCSC; uc009mll.1; mouse.
DR   CTD; 18747; -.
DR   MGI; MGI:97592; Prkaca.
DR   eggNOG; roNOG14656; -.
DR   GeneTree; ENSGT00550000074358; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108317; -.
DR   InParanoid; P05132; -.
DR   OMA; GKEFTEF; -.
DR   OrthoDB; EOG4RXZ0C; -.
DR   PhylomeDB; P05132; -.
DR   BRENDA; 2.7.11.11; 244.
DR   BindingDB; P05132; -.
DR   NextBio; 294909; -.
DR   ArrayExpress; P05132; -.
DR   Bgee; P05132; -.
DR   CleanEx; MM_PRKACA; -.
DR   Genevestigator; P05132; -.
DR   GermOnline; ENSMUSG00000005469; Mus musculus.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; EXP:Reactome.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004691; F:cAMP-dependent protein kinase activity; EXP:Reactome.
DR   GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IMP:MGI.
DR   GO; GO:0001707; P:mesoderm formation; IGI:MGI.
DR   GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; cAMP; Cytoplasm;
KW   Kinase; Lipoprotein; Myristate; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    351       cAMP-dependent protein kinase catalytic
FT                                subunit alpha.
FT                                /FTId=PRO_0000086053.
FT   DOMAIN       44    298       Protein kinase.
FT   DOMAIN      299    351       AGC-kinase C-terminal.
FT   NP_BIND      50     58       ATP.
FT   ACT_SITE    167    167       Proton acceptor.
FT   BINDING      73     73       ATP.
FT   MOD_RES       3      3       Deamidated asparagine; partial.
FT   MOD_RES      11     11       Phosphoserine; by autocatalysis.
FT   MOD_RES      35     35       Phosphoserine.
FT   MOD_RES      49     49       Phosphothreonine (By similarity).
FT   MOD_RES     140    140       Phosphoserine.
FT   MOD_RES     196    196       Phosphothreonine.
FT   MOD_RES     198    198       Phosphothreonine.
FT   MOD_RES     202    202       Phosphothreonine (By similarity).
FT   MOD_RES     339    339       Phosphoserine.
FT   LIPID         2      2       N-myristoyl glycine.
FT   VAR_SEQ       1     15       MGNAAAAKKGSEQES -> MASSSND (in isoform
FT                                2).
FT                                /FTId=VSP_004760.
FT   MUTAGEN     198    198       T->D: No phosphorylation by PDPK1.
FT   CONFLICT     33     33       T -> D (in Ref. 2; AAA39936).
FT   CONFLICT    287    287       N -> D (in Ref. 2; AAA39936).
FT   HELIX        16     32
FT   HELIX        41     43
FT   STRAND       44     52
FT   STRAND       57     63
FT   TURN         64     66
FT   STRAND       69     76
FT   HELIX        77     82
FT   HELIX        86     96
FT   STRAND      107    112
FT   STRAND      114    122
FT   HELIX       129    136
FT   HELIX       141    160
FT   HELIX       170    172
FT   STRAND      173    175
FT   STRAND      181    183
FT   HELIX       203    205
FT   HELIX       208    211
FT   HELIX       219    234
FT   HELIX       244    253
FT   HELIX       264    273
FT   TURN        278    280
FT   TURN        286    289
FT   HELIX       290    293
FT   HELIX       296    298
FT   HELIX       303    307
FT   TURN        345    350
SQ   SEQUENCE   351 AA;  40571 MW;  02F85D66EB21A1FA CRC64;
     MGNAAAAKKG SEQESVKEFL AKAKEDFLKK WETPSQNTAQ LDQFDRIKTL GTGSFGRVML
     VKHKESGNHY AMKILDKQKV VKLKQIEHTL NEKRILQAVN FPFLVKLEFS FKDNSNLYMV
     MEYVAGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDQQGY
     IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF
     ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVN DIKNHKWFAT
     TDWIAIYQRK VEAPFIPKFK GPGDTSNFDD YEEEEIRVSI NEKCGKEFTE F
//
ID   AATM_MOUSE              Reviewed;         430 AA.
AC   P05202; O09188; Q3TIP6; Q3UD91; Q5HZH5;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   08-MAR-2011, entry version 108.
DE   RecName: Full=Aspartate aminotransferase, mitochondrial;
DE            Short=mAspAT;
DE            EC=2.6.1.1;
DE   AltName: Full=Fatty acid-binding protein;
DE            Short=FABP-1;
DE   AltName: Full=Glutamate oxaloacetate transaminase 2;
DE   AltName: Full=Plasma membrane-associated fatty acid-binding protein;
DE            Short=FABPpm;
DE   AltName: Full=Transaminase A;
DE   Flags: Precursor;
GN   Name=Got2; Synonyms=Got-2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=87057413; PubMed=3782150;
RA   Obaru K., Nomiyama H., Shimada K., Nagashima F., Morino Y.;
RT   "Cloning and sequence analysis of mRNA for mouse aspartate
RT   aminotransferase isoenzymes.";
RL   J. Biol. Chem. 261:16976-16983(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C3H/He; TISSUE=Liver;
RX   MEDLINE=88118911; PubMed=2828632; DOI=10.1016/0022-2836(87)90454-2;
RA   Tsuzuki T., Obaru K., Setoyama C., Shimada K.;
RT   "Structural organization of the mouse mitochondrial aspartate
RT   aminotransferase gene.";
RL   J. Mol. Biol. 198:21-31(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=FVB; TISSUE=Liver;
RX   PubMed=10642497; DOI=10.1042/0264-6021:3450423;
RA   Bradbury M.W., Berk P.D.;
RT   "Mitochondrial aspartate aminotransferase: direction of a single
RT   protein with two distinct functions to two subcellular sites does not
RT   require alternative splicing of the mRNA.";
RL   Biochem. J. 345:423-427(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, C57BL/6J, and NOD;
RC   TISSUE=Bone marrow macrophage, Cecum, Dendritic cell, and Melanocyte;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 60-81; 91-122; 126-139; 171-180; 186-200; 280-296;
RP   310-345; 356-363 AND 397-404, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=7878064;
RA   Zhou S.-L., Stump D., Kiang C.L., Isola L.M., Berk P.D.;
RT   "Mitochondrial aspartate aminotransferase expressed on the surface of
RT   3T3-L1 adipocytes mediates saturable fatty acid uptake.";
RL   Proc. Soc. Exp. Biol. Med. 208:263-270(1995).
RN   [8]
RP   NITRATION [LARGE SCALE ANALYSIS] AT TYR-96, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16800626; DOI=10.1021/bi060474w;
RA   Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
RA   Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
RA   Squier T.C., Bigelow D.J.;
RT   "Endogenously nitrated proteins in mouse brain: links to
RT   neurodegenerative disease.";
RL   Biochemistry 45:8009-8022(2006).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-94; LYS-159; LYS-185;
RP   LYS-296; LYS-345 AND LYS-363, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- FUNCTION: Plays a key role in amino acid metabolism. Important for
CC       metabolite exchange between mitochondria and cytosol. Facilitates
CC       cellular uptake of long-chain free fatty acids.
CC   -!- CATALYTIC ACTIVITY: L-aspartate + 2-oxoglutarate = oxaloacetate +
CC       L-glutamate.
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix. Cell membrane.
CC   -!- PTM: Acetylation of Lys-296, Lys-345 and Lys-363 is observed in
CC       liver mitochondria from fasted mice but not from fed mice.
CC   -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial
CC       and chloroplastic isozymes.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; J02622; AAA37264.1; -; mRNA.
DR   EMBL; X06917; CAA30015.1; -; Genomic_DNA.
DR   EMBL; X06918; CAA30015.1; JOINED; Genomic_DNA.
DR   EMBL; X06919; CAA30015.1; JOINED; Genomic_DNA.
DR   EMBL; X06920; CAA30015.1; JOINED; Genomic_DNA.
DR   EMBL; X06921; CAA30015.1; JOINED; Genomic_DNA.
DR   EMBL; X06922; CAA30015.1; JOINED; Genomic_DNA.
DR   EMBL; X06923; CAA30015.1; JOINED; Genomic_DNA.
DR   EMBL; X06924; CAA30015.1; JOINED; Genomic_DNA.
DR   EMBL; X06925; CAA30015.1; JOINED; Genomic_DNA.
DR   EMBL; X06926; CAA30015.1; JOINED; Genomic_DNA.
DR   EMBL; M37259; AAA37265.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; M37250; AAA37265.1; JOINED; Genomic_DNA.
DR   EMBL; M37251; AAA37265.1; JOINED; Genomic_DNA.
DR   EMBL; M37252; AAA37265.1; JOINED; Genomic_DNA.
DR   EMBL; M37253; AAA37265.1; JOINED; Genomic_DNA.
DR   EMBL; M37254; AAA37265.1; JOINED; Genomic_DNA.
DR   EMBL; M37255; AAA37265.1; JOINED; Genomic_DNA.
DR   EMBL; M37256; AAA37265.1; JOINED; Genomic_DNA.
DR   EMBL; M37258; AAA37265.1; JOINED; Genomic_DNA.
DR   EMBL; U82470; AAB91426.1; -; mRNA.
DR   EMBL; AK136556; BAE23042.1; -; mRNA.
DR   EMBL; AK147953; BAE28248.1; -; mRNA.
DR   EMBL; AK149886; BAE29146.1; -; mRNA.
DR   EMBL; AK149926; BAE29171.1; -; mRNA.
DR   EMBL; AK150194; BAE29370.1; -; mRNA.
DR   EMBL; AK152921; BAE31596.1; -; mRNA.
DR   EMBL; AK155075; BAE33029.1; -; mRNA.
DR   EMBL; AK167767; BAE39800.1; -; mRNA.
DR   EMBL; BC089015; AAH89015.1; -; mRNA.
DR   EMBL; BC089341; AAH89341.1; -; mRNA.
DR   IPI; IPI00117312; -.
DR   PIR; S01174; S01174.
DR   RefSeq; NP_034455.1; NM_010325.2.
DR   UniGene; Mm.230169; -.
DR   PDB; 3HLM; X-ray; 2.50 A; A/B/C/D=30-430.
DR   PDB; 3PD6; X-ray; 2.40 A; A/B/C/D=30-430.
DR   PDB; 3PDB; X-ray; 2.40 A; A/B/C/D=30-430.
DR   PDBsum; 3HLM; -.
DR   PDBsum; 3PD6; -.
DR   PDBsum; 3PDB; -.
DR   ProteinModelPortal; P05202; -.
DR   SMR; P05202; 30-430.
DR   STRING; P05202; -.
DR   PhosphoSite; P05202; -.
DR   PRIDE; P05202; -.
DR   Ensembl; ENSMUST00000034097; ENSMUSP00000034097; ENSMUSG00000031672.
DR   GeneID; 14719; -.
DR   KEGG; mmu:14719; -.
DR   UCSC; uc009mzi.1; mouse.
DR   CTD; 14719; -.
DR   MGI; MGI:95792; Got2.
DR   eggNOG; roNOG10163; -.
DR   GeneTree; ENSGT00390000014081; -.
DR   HOGENOM; HBG446828; -.
DR   HOVERGEN; HBG000951; -.
DR   InParanoid; P05202; -.
DR   OMA; IASSYSK; -.
DR   OrthoDB; EOG4RXZ07; -.
DR   PhylomeDB; P05202; -.
DR   BRENDA; 2.6.1.1; 244.
DR   NextBio; 286731; -.
DR   ArrayExpress; P05202; -.
DR   Bgee; P05202; -.
DR   Genevestigator; P05202; -.
DR   GermOnline; ENSMUSG00000031672; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006532; P:aspartate biosynthetic process; IDA:MGI.
DR   GO; GO:0019551; P:glutamate catabolic process to 2-oxoglutarate; IDA:MGI.
DR   GO; GO:0019550; P:glutamate catabolic process to aspartate; IDA:MGI.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IDA:MGI.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR000796; Asp_trans.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase_major_dom.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   PANTHER; PTHR11879; Asp_trans; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00799; TRANSAMINASE.
DR   SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Aminotransferase; Cell membrane;
KW   Direct protein sequencing; Lipid transport; Membrane; Mitochondrion;
KW   Nitration; Phosphoprotein; Pyridoxal phosphate; Transferase;
KW   Transit peptide; Transport.
FT   TRANSIT       1     29       Mitochondrion.
FT   CHAIN        30    430       Aspartate aminotransferase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000001216.
FT   BINDING      65     65       Aspartate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     162    162       Aspartate (By similarity).
FT   BINDING     215    215       Aspartate (By similarity).
FT   BINDING     407    407       Aspartate (By similarity).
FT   MOD_RES      73     73       N6-acetyllysine (By similarity).
FT   MOD_RES      90     90       N6-acetyllysine (By similarity).
FT   MOD_RES      94     94       N6-acetyllysine.
FT   MOD_RES      96     96       Nitrated tyrosine.
FT   MOD_RES      96     96       Phosphotyrosine (By similarity).
FT   MOD_RES     150    150       N6-acetyllysine (By similarity).
FT   MOD_RES     159    159       N6-acetyllysine.
FT   MOD_RES     185    185       N6-acetyllysine.
FT   MOD_RES     234    234       N6-acetyllysine (By similarity).
FT   MOD_RES     279    279       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
FT   MOD_RES     296    296       N6-acetyllysine.
FT   MOD_RES     345    345       N6-acetyllysine.
FT   MOD_RES     363    363       N6-acetyllysine.
FT   MOD_RES     396    396       N6-acetyllysine (By similarity).
FT   MOD_RES     401    401       Phosphotyrosine (By similarity).
FT   MOD_RES     404    404       N6-acetyllysine (By similarity).
FT   CONFLICT     68     68       R -> G (in Ref. 4; BAE39800).
FT   CONFLICT    146    146       Q -> E (in Ref. 3; AAB91426).
FT   CONFLICT    153    153       R -> G (in Ref. 4; BAE39800).
FT   CONFLICT    377    377       Q -> K (in Ref. 4; BAE39800).
FT   CONFLICT    421    421       L -> I (in Ref. 4; BAE39800).
FT   TURN         32     35
FT   HELIX        48     52
FT   HELIX        78     88
FT   TURN         89     91
FT   HELIX       103    113
FT   HELIX       119    122
FT   STRAND      126    129
FT   HELIX       143    148
FT   STRAND      153    160
FT   HELIX       165    171
FT   STRAND      175    177
FT   TURN        184    186
FT   HELIX       195    200
FT   STRAND      206    213
FT   HELIX       223    236
FT   STRAND      239    245
FT   HELIX       259    266
FT   STRAND      272    275
FT   TURN        278    280
FT   STRAND      291    294
FT   HELIX       298    316
FT   HELIX       325    332
FT   HELIX       334    344
FT   HELIX       348    364
FT   HELIX       373    376
FT   HELIX       388    398
FT   HELIX       421    429
SQ   SEQUENCE   430 AA;  47411 MW;  D590524CA7FFB885 CRC64;
     MALLHSSRIL SGMAAAFHPG LAAAASARAS SWWTHVEMGP PDPILGVTEA FKRDTNSKKM
     NLGVGAYRDD NGKPYVLPSV RKAEAQIAAK NLDKEYLPIG GLAEFCKASA ELALGENNEV
     LKSGRFVTVQ TISGTGALRV GASFLQRFFK FSRDVFLPKP SWGNHTPIFR DAGMQLQGYR
     YYDPKTCGFD FSGALEDISK IPEQSVLLLH ACAHNPTGVD PRPEQWKEIA SVVKKKNLFA
     FFDMAYQGFA SGDGDKDAWA VRHFIEQGIN VCLCQSYAKN MGLYGERVGA FTVVCKDAEE
     AKRVESQLKI LIRPLYSNPP LNGARIAATI LTSPDLRKQW LQEVKGMADR IISMRTQLVS
     NLKKEGSSHN WQHITDQIGM FCFTGLKPEQ VERLTKEFSV YMTKDGRISV AGVTSGNVGY
     LAHAIHQVTK
//
ID   TBA1B_MOUSE             Reviewed;         451 AA.
AC   P05213; Q3TY23; Q3U8B1; Q3UAW8; Q4KMW2;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   08-MAR-2011, entry version 112.
DE   RecName: Full=Tubulin alpha-1B chain;
DE   AltName: Full=Alpha-tubulin 2;
DE   AltName: Full=Alpha-tubulin isotype M-alpha-2;
DE   AltName: Full=Tubulin alpha-2 chain;
GN   Name=Tuba1b; Synonyms=Tuba2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=87064538; PubMed=3785200;
RA   Villasante A., Wang D., Dobner P., Dolph P., Lewis S.A., Cowan N.J.;
RT   "Six mouse alpha-tubulin mRNAs encode five distinct isotypes: testis-
RT   specific expression of two sister genes.";
RL   Mol. Cell. Biol. 6:2409-2419(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Amnion, Bone marrow, Eye, Kidney, Liver, Thymus, and
RC   Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, Czech II, and FVB/N;
RC   TISSUE=Limb, Mammary tumor, Olfactory epithelium, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 41-60; 65-79; 85-121; 157-163; 216-304; 312-320;
RP   327-336; 340-370; 374-390; 395-401 AND 403-432, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 100-451.
RX   MEDLINE=85289512; PubMed=3839797; DOI=10.1083/jcb.101.3.852;
RA   Lewis S.A., Lee M.G.-S., Cowan N.J.;
RT   "Five mouse tubulin isotypes and their regulated expression during
RT   development.";
RL   J. Cell Biol. 101:852-861(1985).
RN   [6]
RP   POLYGLUTAMYLATION.
RX   PubMed=15890843; DOI=10.1126/science.1113010;
RA   Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M.,
RA   Temurak N., van Dijk J., Boucher D., van Dorsselaer A.,
RA   Suryavanshi S., Gaertig J., Edde B.;
RT   "Tubulin polyglutamylase enzymes are members of the TTL domain protein
RT   family.";
RL   Science 308:1758-1762(2005).
RN   [7]
RP   POLYGLYCYLATION.
RX   PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA   Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M.,
RA   Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J.,
RA   Janke C.;
RT   "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT   polyglycylation.";
RL   Cell 137:1076-1087(2009).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. It
CC       binds two moles of GTP, one at an exchangeable site on the beta
CC       chain and one at a non-exchangeable site on the alpha-chain.
CC   -!- SUBUNIT: Dimer of alpha and beta chains.
CC   -!- INTERACTION:
CC       P31689:DNAJA1 (xeno); NbExp=1; IntAct=EBI-2311600, EBI-347834;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in
CC       spleen, thymus and immature brain.
CC   -!- PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic
CC       removal and re-addition of a C-terminal tyrosine residue by the
CC       enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin
CC       tyrosine ligase (TTL), respectively (By similarity).
CC   -!- PTM: Some glutamate residues at the C-terminus are either
CC       polyglutamylated or polyglycylated. These 2 modifications occur
CC       exclusively on glutamate residues and result in either
CC       polyglutamate or polyglycine chains on the gamma-carboxyl group.
CC       Glycylation is mainly limited to tubulin incorporated into
CC       axonemes (cilia and flagella) whereas glutamylation is prevalent
CC       in neuronal cells, centrioles, axonemes, and the mitotic spindle.
CC       Both modifications can coexist on the same protein on adjacent
CC       residues, and lowering polyglycylation levels increases
CC       polyglutamylation, and reciprocally. The precise function of such
CC       modifications is still unclear but they are regulate the assembly
CC       and dynamics of axonemal microtubules.
CC   -!- PTM: Acetylation of alpha-tubulins at Lys-40 stabilizes
CC       microtubules and affects affinity and processivity of microtubule
CC       motors. This modification has a role in multiple cellular
CC       functions, ranging from cell motility, cell cycle progression or
CC       cell differentiation to intracellular trafficking and signaling
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the tubulin family.
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DR   EMBL; M13446; AAA40500.1; -; mRNA.
DR   EMBL; AK075955; BAC36080.1; -; mRNA.
DR   EMBL; AK137885; BAE23512.1; -; mRNA.
DR   EMBL; AK150128; BAE29327.1; -; mRNA.
DR   EMBL; AK150179; BAE29362.1; -; mRNA.
DR   EMBL; AK150968; BAE29999.1; -; mRNA.
DR   EMBL; AK151199; BAE30196.1; -; mRNA.
DR   EMBL; AK151809; BAE30708.1; -; mRNA.
DR   EMBL; AK152298; BAE31107.1; -; mRNA.
DR   EMBL; AK153064; BAE31690.1; -; mRNA.
DR   EMBL; AK153254; BAE31845.1; -; mRNA.
DR   EMBL; AK158958; BAE34741.1; -; mRNA.
DR   EMBL; AK164428; BAE37783.1; -; mRNA.
DR   EMBL; AK168770; BAE40606.1; -; mRNA.
DR   EMBL; AK169075; BAE40860.1; -; mRNA.
DR   EMBL; AK169092; BAE40875.1; -; mRNA.
DR   EMBL; AK169130; BAE40909.1; -; mRNA.
DR   EMBL; AK169665; BAE41287.1; -; mRNA.
DR   EMBL; BC002219; AAH02219.1; -; mRNA.
DR   EMBL; BC008117; AAH08117.1; -; mRNA.
DR   EMBL; BC063777; AAH63777.1; -; mRNA.
DR   EMBL; BC083120; AAH83120.1; -; mRNA.
DR   EMBL; BC098321; AAH98321.1; -; mRNA.
DR   EMBL; BC108337; AAI08338.1; -; mRNA.
DR   EMBL; BC108394; AAI08395.1; -; mRNA.
DR   EMBL; M28727; AAA40507.1; -; mRNA.
DR   IPI; IPI00117348; -.
DR   PIR; I77425; I77425.
DR   PIR; S29013; A61275.
DR   RefSeq; NP_035784.1; NM_011654.2.
DR   UniGene; Mm.392113; -.
DR   UniGene; Mm.481178; -.
DR   ProteinModelPortal; P05213; -.
DR   SMR; P05213; 1-440.
DR   IntAct; P05213; 4.
DR   STRING; P05213; -.
DR   PhosphoSite; P05213; -.
DR   REPRODUCTION-2DPAGE; P05213; -.
DR   PRIDE; P05213; -.
DR   Ensembl; ENSMUST00000077577; ENSMUSP00000076777; ENSMUSG00000023004.
DR   GeneID; 22143; -.
DR   KEGG; mmu:22143; -.
DR   UCSC; uc007xoj.1; mouse.
DR   CTD; 22143; -.
DR   MGI; MGI:107804; Tuba1b.
DR   eggNOG; roNOG14794; -.
DR   HOGENOM; HBG750007; -.
DR   HOVERGEN; HBG000089; -.
DR   InParanoid; P05213; -.
DR   OMA; IEPDGTM; -.
DR   OrthoDB; EOG44J2HZ; -.
DR   PhylomeDB; P05213; -.
DR   Reactome; REACT_17056; Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding.
DR   NextBio; 302042; -.
DR   Bgee; P05213; -.
DR   CleanEx; MM_TUBA1B; -.
DR   Genevestigator; P05213; -.
DR   GermOnline; ENSMUSG00000023004; Mus musculus.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005874; C:microtubule; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:MGI.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:MGI.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; TAS:Reactome.
DR   GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR   InterPro; IPR002452; Alpha_tubulin.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR023123; Tubulin_C.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   Gene3D; G3DSA:3.30.1330.20; Tubulin/FtsZ_2-layer-sand-dom; 1.
DR   Gene3D; G3DSA:1.10.287.600; Tubulin_C; 1.
DR   Gene3D; G3DSA:3.40.50.1440; Tubulin_FtsZ; 1.
DR   PANTHER; PTHR11588; Tubulin; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01162; ALPHATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF55307; Tub_FtsZ_C; 1.
DR   SUPFAM; SSF52490; Tubulin_FtsZ; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   GTP-binding; Isopeptide bond; Methylation; Microtubule;
KW   Nucleotide-binding; Phosphoprotein; Ubl conjugation.
FT   CHAIN         1    451       Tubulin alpha-1B chain.
FT                                /FTId=PRO_0000048121.
FT   NP_BIND     142    148       GTP (Potential).
FT   SITE        451    451       Involved in polymerization.
FT   MOD_RES      40     40       N6-acetyllysine (By similarity).
FT   MOD_RES      41     41       Phosphothreonine (By similarity).
FT   MOD_RES      48     48       Phosphoserine (By similarity).
FT   MOD_RES     232    232       Phosphoserine (By similarity).
FT   MOD_RES     334    334       Phosphothreonine (By similarity).
FT   MOD_RES     339    339       Omega-N-methylarginine (By similarity).
FT   MOD_RES     340    340       Phosphoserine (By similarity).
FT   MOD_RES     432    432       Phosphotyrosine (By similarity).
FT   MOD_RES     439    439       Phosphoserine (By similarity).
FT   MOD_RES     451    451       Phosphotyrosine (By similarity).
FT   CROSSLNK    326    326       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK    370    370       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CONFLICT     55     55       E -> G (in Ref. 2; BAE30708/BAE31107).
FT   CONFLICT    114    114       I -> T (in Ref. 2; BAE34741).
FT   CONFLICT    119    119       L -> P (in Ref. 2; BAE29999/BAE30196).
FT   CONFLICT    135    136       FL -> LF (in Ref. 5; AAA40507).
FT   CONFLICT    340    340       S -> T (in Ref. 1 and 5; AAA40507).
SQ   SEQUENCE   451 AA;  50152 MW;  94355B4EC2086429 CRC64;
     MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK
     HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD
     RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA
     VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA
     SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
     QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRS IQFVDWCPTG FKVGINYQPP
     TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
     AREDMAALEK DYEEVGVDSV EGEGEEEGEE Y
//
ID   SRC_MOUSE               Reviewed;         541 AA.
AC   P05480;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 125.
DE   RecName: Full=Neuronal proto-oncogene tyrosine-protein kinase Src;
DE            EC=2.7.10.2;
DE   AltName: Full=Proto-oncogene c-Src;
DE   AltName: Full=pp60c-src;
DE            Short=p60-Src;
GN   Name=Src;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=87263406; PubMed=2440106; DOI=10.1126/science.2440106;
RA   Martinez R., Mathey-Prevot B., Bernards A., Baltimore D.;
RT   "Neuronal pp60c-src contains a six-amino acid insertion relative to
RT   its non-neuronal counterpart.";
RL   Science 237:411-415(1987).
RN   [2]
RP   INTERACTION WITH DDEF1/ASAP1.
RX   MEDLINE=99038209; PubMed=9819391;
RA   Brown M.T., Andrade J., Radhakrishna H., Donaldson J.G., Cooper J.A.,
RA   Randazzo P.A.;
RT   "ASAP1, a phospholipid-dependent arf GTPase-activating protein that
RT   associates with and is phosphorylated by Src.";
RL   Mol. Cell. Biol. 18:7038-7051(1998).
RN   [3]
RP   INTERACTION WITH CCPG1.
RX   PubMed=17000758; DOI=10.1128/MCB.00670-06;
RA   Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P.;
RT   "Ccpg1, a novel scaffold protein that regulates the activity of the
RT   Rho guanine nucleotide exchange factor Dbs.";
RL   Mol. Cell. Biol. 26:8964-8975(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-192, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   INTERACTION WITH ARRB2.
RX   PubMed=19122674; DOI=10.1038/nature07617;
RA   Luan B., Zhao J., Wu H., Duan B., Shu G., Wang X., Li D., Jia W.,
RA   Kang J., Pei G.;
RT   "Deficiency of a beta-arrestin-2 signal complex contributes to insulin
RT   resistance.";
RL   Nature 457:1146-1149(2009).
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBUNIT: Interacts with CDCP1, PELP1, TGFB1I1 and TOM1L2 (By
CC       similarity). Interacts with DDEF1/ASAP1 via its SH3 domain.
CC       Interacts with CCPG1. Interacts with the cytoplasmic domain of
CC       MUC1, phosphorylates it and increases binding of MUC1 with beta-
CC       catenin (By similarity). Interacts with RALGPS1 via its SH3 domain
CC       (By similarity). Interacts with CAV2 (tyrosine phosphorylated
CC       form) (By similarity). Interacts (via the SH3 domain and the
CC       protein kinase domain) with ARRB1; the interaction is independent
CC       of the phosphorylation state of SRC C-terminus (By similarity).
CC       Interacts with ARRB2. Interacts with ARRB1. Interacts with SRCIN1
CC       (By similarity). Interacts with SRCIN1. Interacts with NDFIP2 and
CC       more weakly with NDFIP1. Interacts with PI3K (alpha and/or beta),
CC       PTK2, ESR1 (dimethylated on arginine) and FAK (By similarity).
CC   -!- INTERACTION:
CC       P07141:Csf1; NbExp=2; IntAct=EBI-298680, EBI-777188;
CC       Q8T4F7:ena (xeno); NbExp=2; IntAct=EBI-298680, EBI-466810;
CC       P54763:Ephb2; NbExp=1; IntAct=EBI-298680, EBI-537711;
CC       P70315:Was; NbExp=2; IntAct=EBI-298680, EBI-644195;
CC   -!- PTM: Dephosphorylated at Tyr-535 by PTPRJ (By similarity).
CC       Phosphorylated on Tyr-535 by c-Src kinase (CSK). The
CC       phosphorylated form is termed pp60c-src. Dephosphorylated at Tyr-
CC       424 by PTPRJ. The phosphorylated tail interacts with the SH2
CC       domain thereby repressing kinase activity (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. SRC subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; M17031; AAA40135.1; -; mRNA.
DR   IPI; IPI00222801; -.
DR   PIR; A43610; A43610.
DR   RefSeq; NP_001020566.1; NM_001025395.2.
DR   RefSeq; NP_033297.2; NM_009271.3.
DR   UniGene; Mm.22845; -.
DR   ProteinModelPortal; P05480; -.
DR   SMR; P05480; 85-541.
DR   DIP; DIP-31071N; -.
DR   IntAct; P05480; 17.
DR   MINT; MINT-85032; -.
DR   STRING; P05480; -.
DR   PhosphoSite; P05480; -.
DR   PRIDE; P05480; -.
DR   Ensembl; ENSMUST00000092576; ENSMUSP00000090237; ENSMUSG00000027646.
DR   Ensembl; ENSMUST00000109529; ENSMUSP00000105155; ENSMUSG00000027646.
DR   GeneID; 20779; -.
DR   KEGG; mmu:20779; -.
DR   CTD; 20779; -.
DR   MGI; MGI:98397; Src.
DR   eggNOG; roNOG11676; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG008761; -.
DR   InParanoid; P05480; -.
DR   OrthoDB; EOG4KKZ2S; -.
DR   BRENDA; 2.7.10.2; 244.
DR   Reactome; REACT_23985; Src is activated.
DR   NextBio; 299503; -.
DR   ArrayExpress; P05480; -.
DR   Bgee; P05480; -.
DR   CleanEx; MM_SRC; -.
DR   Genevestigator; P05480; -.
DR   GermOnline; ENSMUSG00000027646; Mus musculus.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:EC.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR   GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IMP:MGI.
DR   GO; GO:0016477; P:cell migration; IMP:MGI.
DR   GO; GO:0030900; P:forebrain development; IGI:MGI.
DR   GO; GO:0048477; P:oogenesis; IMP:MGI.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt receptor signaling pathway; IGI:MGI.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:BHF-UCL.
DR   GO; GO:0033146; P:regulation of estrogen receptor signaling pathway; IMP:MGI.
DR   GO; GO:0060065; P:uterus development; IMP:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Lipoprotein; Myristate; Nucleotide-binding;
KW   Phosphoprotein; Proto-oncogene; SH2 domain; SH3 domain; Transferase;
KW   Tyrosine-protein kinase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    541       Neuronal proto-oncogene tyrosine-protein
FT                                kinase Src.
FT                                /FTId=PRO_0000088142.
FT   DOMAIN       83    150       SH3.
FT   DOMAIN      156    253       SH2.
FT   DOMAIN      275    528       Protein kinase.
FT   NP_BIND     281    289       ATP (By similarity).
FT   ACT_SITE    394    394       Proton acceptor (By similarity).
FT   BINDING     303    303       ATP (By similarity).
FT   MOD_RES      17     17       Phosphoserine.
FT   MOD_RES      34     34       Phosphoserine (By similarity).
FT   MOD_RES      68     68       Phosphoserine (By similarity).
FT   MOD_RES      73     73       Phosphothreonine (By similarity).
FT   MOD_RES      74     74       Phosphoserine.
FT   MOD_RES     192    192       Phosphotyrosine.
FT   MOD_RES     424    424       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     444    444       Phosphotyrosine (By similarity).
FT   MOD_RES     516    516       Phosphothreonine (By similarity).
FT   MOD_RES     527    527       Phosphotyrosine (By similarity).
FT   MOD_RES     535    535       Phosphotyrosine; by CSK (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
SQ   SEQUENCE   541 AA;  60619 MW;  09BBA0EEF88A70B5 CRC64;
     MGSNKSKPKD ASQRRRSLEP SENVHGAGGA FPASQTPSKP ASADGHRGPS AAFVPPAAEP
     KLFGGFNSSD TVTSPQRAGA LAGGVTTFVA LYDYESRTET DLSFKKGERL QIVNNTRKVD
     VREGDWWLAH SLSTGQTGYI PSNYVAPSDS IQAEEWYFGK ITRRESERLL LNAENPRGTF
     LVRESETTKG AYCLSVSDFD NAKGLNVKHY KIRKLDSGGF YITSRTQFNS LQQLVAYYSK
     HADGLCHRLT TVCPTSKPQT QGLAKDAWEI PRESLRLEVK LGQGCFGEVW MGTWNGTTRV
     AIKTLKPGTM SPEAFLQEAQ VMKKLRHEKL VQLYAVVSEE PIYIVTEYMN KGSLLDFLKG
     ETGKYLRLPQ LVDMSAQIAS GMAYVERMNY VHRDLRAANI LVGENLVCKV ADFGLARLIE
     DNEYTARQGA KFPIKWTAPE AALYGRFTIK SDVWSFGILL TELTTKGRVP YPGMVNREVL
     DQVERGYRMP CPPECPESLH DLMCQCWRKE PEERPTFEYL QAFLEDYFTS TEPQYQPGEN
     L
//
ID   G6PI_MOUSE              Reviewed;         558 AA.
AC   P06745; O89062; Q3TEE7; Q3TW50; Q3UUX1; Q3UY84; Q3UZJ1; Q5RJI3;
AC   Q8C675; Q9JM07;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 4.
DT   08-MAR-2011, entry version 105.
DE   RecName: Full=Glucose-6-phosphate isomerase;
DE            Short=GPI;
DE            EC=5.3.1.9;
DE   AltName: Full=Autocrine motility factor;
DE            Short=AMF;
DE   AltName: Full=Neuroleukin;
DE            Short=NLK;
DE   AltName: Full=Phosphoglucose isomerase;
DE            Short=PGI;
DE   AltName: Full=Phosphohexose isomerase;
DE            Short=PHI;
GN   Name=Gpi; Synonyms=Gpi1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Salivary gland;
RX   MEDLINE=87018838; PubMed=3764429; DOI=10.1126/science.3764429;
RA   Gurney M.E., Heinrich S.P., Lee M.R., Yin H.-S.;
RT   "Molecular cloning and expression of neuroleukin, a neurotrophic
RT   factor for spinal and sensory neurons.";
RL   Science 234:566-574(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Head, Heart, Olfactory bulb, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 28-36; 63-73; 97-104; 107-124; 148-176; 181-234;
RP   242-252; 255-273; 424-438; 455-461 AND 467-481, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 235-393.
RC   STRAIN=BALB/c; TISSUE=Spleen;
RX   MEDLINE=99012997; PubMed=9798653; DOI=10.1016/S0161-5890(98)00031-5;
RA   Chu C.C., Paul W.E.;
RT   "Expressed genes in interleukin-4 treated B cells identified by cDNA
RT   representational difference analysis.";
RL   Mol. Immunol. 35:487-502(1998).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 269-558.
RX   MEDLINE=94375004; PubMed=7545951; DOI=10.1006/geno.1994.1233;
RA   Faik P., Walker J.I., Morgan M.J.;
RT   "Identification of a novel tandemly repeated sequence present in an
RT   intron of the glucose phosphate isomerase (GPI) gene in mouse and
RT   man.";
RL   Genomics 21:122-127(1994).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 417-543.
RC   STRAIN=129;
RA   Bauchwitz R.P., Tyagi S., Marras S.A.E.;
RT   "Quantitative allelic discrimination of GPI-c and GPI-a using
RT   molecular beacons.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   IDENTITY OF NEUROLEUKIN AS PGI.
RX   MEDLINE=88175071; PubMed=3352745; DOI=10.1038/332455a0;
RA   Faik P., Walker J.I.H., Redmill A.A.M., Morgan M.J.;
RT   "Mouse glucose-6-phosphate isomerase and neuroleukin have identical 3'
RT   sequences.";
RL   Nature 332:455-456(1988).
RN   [10]
RP   ISGYLATION.
RX   PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA   Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA   Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT   "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT   human cells.";
RL   Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH G6P, AND ACTIVE
RP   SITE.
RX   PubMed=15342241; DOI=10.1016/j.jmb.2004.07.085;
RA   Solomons J.T.G., Zimmerly E.M., Burns S., Krishnamurthy N., Swan M.K.,
RA   Krings S., Muirhead H., Chirgwin J., Davies C.;
RT   "The crystal structure of mouse phosphoglucose isomerase at 1.6A
RT   resolution and its complex with glucose 6-phosphate reveals the
RT   catalytic mechanism of sugar ring opening.";
RL   J. Mol. Biol. 342:847-860(2004).
RN   [12]
RP   IDENTITY OF AMF AS PGI.
RX   PubMed=8674049;
RA   Watanabe H., Takehana K., Date M., Shinozaki T., Raz A.;
RT   "Tumor cell autocrine motility factor is the neuroleukin/phosphohexose
RT   isomerase polypeptide.";
RL   Cancer Res. 56:2960-2963(1996).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 1-557 IN COMPLEX WITH
RP   INHIBITORS.
RX   PubMed=16375918; DOI=10.1016/j.jmb.2005.11.076;
RA   Tanaka N., Haga A., Naba N., Shiraiwa K., Kusakabe Y., Hashimoto K.,
RA   Funasaka T., Nagase H., Raz A., Nakamura K.T.;
RT   "Crystal structures of mouse autocrine motility factor in complex with
RT   carbohydrate phosphate inhibitors provide insight into structure-
RT   activity relationship of the inhibitors.";
RL   J. Mol. Biol. 356:312-324(2006).
CC   -!- FUNCTION: Besides it's role as a glycolytic enzyme, mammalian GPI
CC       can function as a tumor-secreted cytokine and an angiogenic factor
CC       (AMF) that stimulates endothelial cell motility. GPI is also a
CC       neurotrophic factor (Neuroleukin) for spinal and sensory neurons.
CC   -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate = D-fructose 6-
CC       phosphate.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 2/4.
CC   -!- SUBUNIT: Homodimer in the catalytically active form, monomer in
CC       the secreted form.
CC   -!- INTERACTION:
CC       Q2EMV9:Parp14; NbExp=3; IntAct=EBI-1534927, EBI-1534943;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Secreted.
CC   -!- PTM: ISGylated.
CC   -!- SIMILARITY: Belongs to the GPI family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC36335.1; Type=Erroneous initiation;
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DR   EMBL; M14220; AAA39825.1; -; mRNA.
DR   EMBL; AK076424; BAC36335.1; ALT_INIT; mRNA.
DR   EMBL; AK133827; BAE21866.1; -; mRNA.
DR   EMBL; AK134890; BAE22329.1; -; mRNA.
DR   EMBL; AK137805; BAE23502.1; -; mRNA.
DR   EMBL; AK147124; BAE27695.1; -; mRNA.
DR   EMBL; AK150341; BAE29481.1; -; mRNA.
DR   EMBL; AK159838; BAE35416.1; -; mRNA.
DR   EMBL; AK169681; BAE41301.1; -; mRNA.
DR   EMBL; BX537302; CAM21756.1; -; Genomic_DNA.
DR   EMBL; BC086640; AAH86640.1; -; mRNA.
DR   EMBL; BC088995; AAH88995.1; -; mRNA.
DR   EMBL; U89408; AAC36515.1; -; mRNA.
DR   EMBL; L09104; AAA65641.1; -; mRNA.
DR   EMBL; AF108354; AAF28799.1; -; mRNA.
DR   IPI; IPI00228633; -.
DR   PIR; A24439; NUMS.
DR   RefSeq; NP_032181.2; NM_008155.3.
DR   UniGene; Mm.390025; -.
DR   UniGene; Mm.471409; -.
DR   UniGene; Mm.589; -.
DR   PDB; 1U0E; X-ray; 1.60 A; A/B=1-558.
DR   PDB; 1U0F; X-ray; 1.60 A; A/B=1-558.
DR   PDB; 1U0G; X-ray; 1.70 A; A/B=1-558.
DR   PDB; 2CVP; X-ray; 1.80 A; A/B=1-557.
DR   PDB; 2CXN; X-ray; 1.40 A; A/B=1-557.
DR   PDB; 2CXO; X-ray; 1.80 A; A/B=1-557.
DR   PDB; 2CXP; X-ray; 1.70 A; A/B=1-557.
DR   PDB; 2CXQ; X-ray; 1.50 A; A/B=1-557.
DR   PDB; 2CXR; X-ray; 1.70 A; A/B=1-557.
DR   PDB; 2CXS; X-ray; 1.50 A; A/B=1-557.
DR   PDB; 2CXT; X-ray; 1.50 A; A/B=1-557.
DR   PDB; 2CXU; X-ray; 1.65 A; A/B=1-557.
DR   PDBsum; 1U0E; -.
DR   PDBsum; 1U0F; -.
DR   PDBsum; 1U0G; -.
DR   PDBsum; 2CVP; -.
DR   PDBsum; 2CXN; -.
DR   PDBsum; 2CXO; -.
DR   PDBsum; 2CXP; -.
DR   PDBsum; 2CXQ; -.
DR   PDBsum; 2CXR; -.
DR   PDBsum; 2CXS; -.
DR   PDBsum; 2CXT; -.
DR   PDBsum; 2CXU; -.
DR   ProteinModelPortal; P06745; -.
DR   SMR; P06745; 1-557.
DR   IntAct; P06745; 5.
DR   STRING; P06745; -.
DR   PhosphoSite; P06745; -.
DR   PRIDE; P06745; -.
DR   Ensembl; ENSMUST00000038027; ENSMUSP00000049355; ENSMUSG00000036427.
DR   GeneID; 14751; -.
DR   KEGG; mmu:14751; -.
DR   NMPDR; fig|10090.3.peg.16221; -.
DR   UCSC; uc009gix.1; mouse.
DR   CTD; 14751; -.
DR   MGI; MGI:95797; Gpi1.
DR   eggNOG; roNOG05642; -.
DR   GeneTree; ENSGT00390000000707; -.
DR   HOVERGEN; HBG002877; -.
DR   InParanoid; P06745; -.
DR   OMA; GPKIVSQ; -.
DR   OrthoDB; EOG44MXRS; -.
DR   PhylomeDB; P06745; -.
DR   BRENDA; 5.3.1.9; 244.
DR   NextBio; 286815; -.
DR   ArrayExpress; P06745; -.
DR   Bgee; P06745; -.
DR   CleanEx; MM_GPI1; -.
DR   Genevestigator; P06745; -.
DR   GermOnline; ENSMUSG00000036427; Mus musculus.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IDA:MGI.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR001672; G6P_Isomerase.
DR   InterPro; IPR023096; G6P_Isomerase_C.
DR   InterPro; IPR018189; Phosphoglucose_isomerase_CS.
DR   Gene3D; G3DSA:1.10.1390.10; G6P_Isomerase_C; 1.
DR   PANTHER; PTHR11469; G6P_Isomerase; 1.
DR   Pfam; PF00342; PGI; 1.
DR   PRINTS; PR00662; G6PISOMERASE.
DR   PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1.
DR   PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
DR   PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Angiogenesis; Cytokine; Cytoplasm;
KW   Direct protein sequencing; Gluconeogenesis; Glycolysis; Growth factor;
KW   Isomerase; Phosphoprotein; Secreted; Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    558       Glucose-6-phosphate isomerase.
FT                                /FTId=PRO_0000180538.
FT   ACT_SITE    358    358       Proton donor.
FT   ACT_SITE    389    389
FT   ACT_SITE    519    519
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      12     12       N6-acetyllysine (By similarity).
FT   MOD_RES     109    109       Phosphothreonine (By similarity).
FT   MOD_RES     142    142       N6-acetyllysine (By similarity).
FT   MOD_RES     185    185       Phosphoserine; by CK2 (By similarity).
FT   CONFLICT     95     95       N -> D (in Ref. 1; AAA39825/BAE41301).
FT   CONFLICT    119    119       M -> K (in Ref. 2; BAE21866).
FT   CONFLICT    191    191       H -> R (in Ref. 2; BAE22329).
FT   CONFLICT    238    238       A -> E (in Ref. 6; AAC36515).
FT   CONFLICT    264    266       FEF -> LEL (in Ref. 6; AAC36515).
FT   CONFLICT    285    285       A -> V (in Ref. 6; AAC36515).
FT   CONFLICT    303    303       M -> T (in Ref. 6; AAC36515).
FT   CONFLICT    313    313       E -> G (in Ref. 2; BAE35416).
FT   CONFLICT    357    357       M -> V (in Ref. 6; AAC36515).
FT   CONFLICT    372    372       D -> N (in Ref. 6; AAC36515).
FT   CONFLICT    380    380       W -> L (in Ref. 6; AAC36515).
FT   CONFLICT    499    499       F -> L (in Ref. 2; BAE23502).
FT   HELIX         3      6
FT   HELIX         8     20
FT   HELIX        21     23
FT   HELIX        26     32
FT   HELIX        36     39
FT   STRAND       41     45
FT   STRAND       50     54
FT   HELIX        62     74
FT   HELIX        77     85
FT   TURN         92     95
FT   HELIX       100    103
FT   STRAND      116    118
FT   HELIX       119    137
FT   STRAND      151    155
FT   HELIX       158    160
FT   HELIX       162    170
FT   HELIX       172    175
FT   STRAND      180    184
FT   HELIX       189    196
FT   TURN        201    203
FT   STRAND      204    209
FT   STRAND      211    213
FT   HELIX       216    233
FT   HELIX       236    241
FT   STRAND      243    248
FT   HELIX       250    256
FT   HELIX       260    262
FT   STRAND      263    265
FT   HELIX       272    274
FT   TURN        276    278
FT   HELIX       279    281
FT   HELIX       282    288
FT   HELIX       290    309
FT   HELIX       312    314
FT   HELIX       316    329
FT   STRAND      335    341
FT   HELIX       343    345
FT   HELIX       348    360
FT   STRAND      378    380
FT   TURN        384    387
FT   HELIX       388    397
FT   STRAND      404    411
FT   HELIX       417    419
FT   HELIX       420    438
FT   HELIX       442    451
FT   HELIX       456    462
FT   HELIX       463    466
FT   STRAND      474    481
FT   HELIX       484    505
FT   HELIX       513    515
FT   HELIX       516    525
FT   HELIX       526    529
FT   STRAND      530    533
FT   HELIX       540    552
SQ   SEQUENCE   558 AA;  62767 MW;  7299E98B12B4C375 CRC64;
     MAALTRNPQF QKLLEWHRAN SANLKLRELF EADPERFNNF SLNLNTNHGH ILVDYSKNLV
     NKEVMQMLVE LAKSRGVEAA RDNMFSGSKI NYTENRAVLH VALRNRSNTP IKVDGKDVMP
     EVNRVLDKMK SFCQRVRSGD WKGYTGKSIT DIINIGIGGS DLGPLMVTEA LKPYSKGGPR
     VWFVSNIDGT HIAKTLASLS PETSLFIIAS KTFTTQETIT NAETAKEWFL EAAKDPSAVA
     KHFVALSTNT AKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DHFEQLLSGA
     HWMDQHFLKT PLEKNAPVLL ALLGIWYINC YGCETHALLP YDQYMHRFAA YFQQGDMESN
     GKYITKSGAR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK MIPCDFLIPV QTQHPIRKGL
     HHKILLANFL AQTEALMKGK LPEEARKELQ AAGKSPEDLE KLLPHKVFEG NRPTNSIVFT
     KLTPFILGAL IAMYEHKIFV QGIMWDINSF DQWGVELGKQ LAKKIEPELE GSSAVTSHDS
     STNGLISFIK QQRDTKLE
//
ID   ENPP1_MOUSE             Reviewed;         906 AA.
AC   P06802; Q542E9; Q924C4;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2002, sequence version 4.
DT   08-FEB-2011, entry version 116.
DE   RecName: Full=Ectonucleotide pyrophosphatase/phosphodiesterase family member 1;
DE            Short=E-NPP 1;
DE   AltName: Full=Lymphocyte antigen 41;
DE            Short=Ly-41;
DE   AltName: Full=Phosphodiesterase I/nucleotide pyrophosphatase 1;
DE   AltName: Full=Plasma-cell membrane glycoprotein PC-1;
DE   Includes:
DE     RecName: Full=Alkaline phosphodiesterase I;
DE              EC=3.1.4.1;
DE   Includes:
DE     RecName: Full=Nucleotide pyrophosphatase;
DE              Short=NPPase;
DE              EC=3.6.1.9;
GN   Name=Enpp1; Synonyms=Npps, Pc1, Pdnp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c;
RX   MEDLINE=87165906; PubMed=3104326;
RA   van Driel I.R., Goding J.W.;
RT   "Plasma cell membrane glycoprotein PC-1. Primary structure deduced
RT   from cDNA clones.";
RL   J. Biol. Chem. 262:4882-4887(1987).
RN   [2]
RP   SEQUENCE REVISION TO 24; 46-47; 642 AND 693.
RA   Goding J.W.;
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION, AND FUNCTION.
RC   STRAIN=BALB/c; TISSUE=Plasmacytoma;
RX   MEDLINE=91271356; PubMed=1647027; DOI=10.1073/pnas.88.12.5192;
RA   Rebbe N.F., Tong B.D., Finley E.M., Hickman S.;
RT   "Identification of nucleotide pyrophosphatase/alkaline
RT   phosphodiesterase I activity associated with the mouse plasma cell
RT   differentiation antigen PC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:5192-5196(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS ARG-651 AND SER-680,
RP   AND ALTERNATIVE SPLICING.
RX   MEDLINE=22117315; PubMed=12121276;
RX   DOI=10.1046/j.1365-2370.2002.00330.x;
RA   Banakh I., Sali A., Dubljevic V., Grobben B., Slegers H., Goding J.W.;
RT   "Structural basis of allotypes of ecto-nucleotide
RT   pyrophosphatase/phosphodiesterase (plasma cell membrane glycoprotein
RT   PC-1) in the mouse and rat, and analysis of allele-specific xenogeneic
RT   antibodies.";
RL   Eur. J. Immunogenet. 29:307-313(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 168-188.
RX   MEDLINE=94039066; PubMed=8223581;
RX   DOI=10.1111/j.1432-1033.1993.tb18261.x;
RA   Belli S.I., van Driel I.R., Goding J.W.;
RT   "Identification and characterization of a soluble form of the plasma
RT   cell membrane glycoprotein PC-1 (5'-nucleotide phosphodiesterase).";
RL   Eur. J. Biochem. 217:421-428(1993).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 203-219.
RX   MEDLINE=86094275; PubMed=3001713; DOI=10.1073/pnas.82.24.8619;
RA   van Driel I.R., Wilks A.F., Pietersz G.A., Goding J.W.;
RT   "Murine plasma cell membrane antigen PC-1: molecular cloning of cDNA
RT   and analysis of expression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:8619-8623(1985).
RN   [8]
RP   PROTEIN SEQUENCE OF 204-219; 332-351; 486-509; 716-725; 803-818 AND
RP   855-867.
RX   MEDLINE=85056299; PubMed=3917281;
RA   Stearne P.A., van Driel I.R., Grego B., Simpson R.J., Goding J.W.;
RT   "The murine plasma cell antigen PC-1: purification and partial amino
RT   acid sequence.";
RL   J. Immunol. 134:443-448(1985).
RN   [9]
RP   IDENTIFICATION OF POSSIBLE INITIATION SITE.
RX   MEDLINE=91009202; PubMed=2211644;
RA   Buckley M.F., Loveland K.A., McKinstry W.J., Garson O.M., Goding J.W.;
RT   "Plasma cell membrane glycoprotein PC-1. cDNA cloning of the human
RT   molecule, amino acid sequence, and chromosomal location.";
RL   J. Biol. Chem. 265:17506-17511(1990).
RN   [10]
RP   DISEASE.
RX   MEDLINE=98324779; PubMed=9662402; DOI=10.1038/956;
RA   Okawa A., Nakamura I., Goto S., Moriya H., Nakamura Y., Ikegawa S.;
RT   "Mutation in Npps in a mouse model of ossification of the posterior
RT   longitudinal ligament of the spine.";
RL   Nat. Genet. 19:271-273(1998).
RN   [11]
RP   ACTIVE SITE, METAL-BINDING, AND MUTAGENESIS OF ASP-200; LYS-237;
RP   THR-238; PHE-239; ASP-358; HIS-362; ASP-405; HIS-406 AND HIS-517.
RX   PubMed=11027689; DOI=10.1074/jbc.M007552200;
RA   Gijsbers R., Ceulemans H., Stalmans W., Bollen M.;
RT   "Structural and catalytic similarities between nucleotide
RT   pyrophosphatases/phosphodiesterases and alkaline phosphatases.";
RL   J. Biol. Chem. 276:1361-1368(2001).
RN   [12]
RP   DI-LEUCINE MOTIF, MUTAGENESIS OF ALA-28; SER-30; LEU-31 AND LEU-32,
RP   AND SUBCELLULAR LOCATION.
RX   PubMed=11598187;
RA   Bello V., Goding J.W., Greengrass V., Sali A., Dubljevic V.,
RA   Lenoir C., Trugnan G., Maurice M.;
RT   "Characterization of a di-leucine-based signal in the cytoplasmic tail
RT   of the nucleotide-pyrophosphatase NPP1 that mediates basolateral
RT   targeting but not endocytosis.";
RL   Mol. Biol. Cell 12:3004-3015(2001).
RN   [13]
RP   DI-LEUCINE MOTIF, MUTAGENESIS OF LEU-31; LEU-32; LEU-42 AND TYR-57,
RP   AND SUBCELLULAR LOCATION.
RX   PubMed=15075217; DOI=10.1152/ajpcell.00320.2003;
RA   Vaingankar S.M., Fitzpatrick T.A., Johnson K., Goding J.W.,
RA   Maurice M., Terkeltaub R.;
RT   "Subcellular targeting and function of osteoblast nucleotide
RT   pyrophosphatase phosphodiesterase 1.";
RL   Am. J. Physiol. 286:C1177-C1187(2004).
RN   [14]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-267; ASN-323 AND ASN-624,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
CC   -!- FUNCTION: Involved primarily in ATP hydrolysis at the plasma
CC       membrane. Plays a role in regulating pyrophosphate levels, and
CC       functions in bone mineralization and soft tissue calcification. In
CC       vitro, has a broad specificity, hydrolyzing other nucleoside 5'
CC       triphosphates such as GTP, CTP, TTP and UTP to their corresponding
CC       monophosphates with release of pyrophosphate and diadenosine
CC       polyphosphates, and also 3',5'-cAMP to AMP. May also be involved
CC       in the regulation of the availability of nucleotide sugars in the
CC       endoplasmic reticulum and Golgi, and the regulation of purinergic
CC       signaling. Appears to modulate insulin sensitivity (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolytically removes 5'-nucleotides
CC       successively from the 3'-hydroxy termini of 3'-hydroxy-terminated
CC       oligonucleotides.
CC   -!- CATALYTIC ACTIVITY: A dinucleotide + H(2)O = 2 mononucleotides.
CC   -!- COFACTOR: Binds 2 divalent metal cations per subunit (Probable).
CC   -!- ENZYME REGULATION: At low concentrations of ATP, a phosphorylated
CC       intermediate is formed which inhibits further hydrolysis.
CC   -!- SUBUNIT: Homodimer; disulfide-linked.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane
CC       protein. Basolateral cell membrane; Single-pass type II membrane
CC       protein (By similarity). Note=Targeted to the basolateral membrane
CC       in polarized epithelial cells and in hepatocytes, and to matrix
CC       vesicles in osteoblasts. In bile duct cells and cancer cells,
CC       located to the apical cytoplasmic side (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2;
CC         IsoId=P06802-1; Sequence=Displayed;
CC       Name=1;
CC         IsoId=P06802-2; Sequence=VSP_006748;
CC   -!- TISSUE SPECIFICITY: Selectively expressed on the surface of
CC       antibody-secreting cells.
CC   -!- DOMAIN: The di-leucine motif is required for basolateral targeting
CC       in polarized epithelial cells, and for targeting to matrix
CC       vesicles derived from mineralizing cells.
CC   -!- PTM: The N-terminal is blocked.
CC   -!- PTM: N-glycosylated.
CC   -!- PTM: It has been suggested that the active SMB domain may be
CC       permitted considerable disulfide bond heterogeneity or
CC       variability, thus two alternate disulfide patterns based on 3D
CC       structures are described with 1 disulfide bond conserved in both.
CC   -!- DISEASE: Note=Defects in Enpp1 are the cause of the tiptoe walking
CC       (ttw) phenotype. Ttw mice exhibit ossification of the spinal
CC       ligaments.
CC   -!- SIMILARITY: Belongs to the nucleotide
CC       pyrophosphatase/phosphodiesterase family.
CC   -!- SIMILARITY: Contains 2 SMB (somatomedin-B) domains.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-35 is the initiator.
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DR   EMBL; J02700; AAA39893.2; -; mRNA.
DR   EMBL; AF339910; AAK84174.1; -; mRNA.
DR   EMBL; AK088857; BAC40616.1; -; mRNA.
DR   EMBL; L04516; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR   EMBL; M12552; AAA39892.1; -; mRNA.
DR   IPI; IPI00128859; -.
DR   IPI; IPI00265291; -.
DR   PIR; A27410; A27410.
DR   UniGene; Mm.478860; -.
DR   ProteinModelPortal; P06802; -.
DR   SMR; P06802; 85-126, 129-171, 190-579.
DR   STRING; P06802; -.
DR   PhosphoSite; P06802; -.
DR   PRIDE; P06802; -.
DR   Ensembl; ENSMUST00000039882; ENSMUSP00000046090; ENSMUSG00000037370.
DR   MGI; MGI:97370; Enpp1.
DR   eggNOG; roNOG12236; -.
DR   GeneTree; ENSGT00550000074244; -.
DR   HOGENOM; HBG357577; -.
DR   HOVERGEN; HBG051484; -.
DR   InParanoid; P06802; -.
DR   PhylomeDB; P06802; -.
DR   BRENDA; 3.1.4.1; 244.
DR   BRENDA; 3.6.1.9; 244.
DR   ArrayExpress; P06802; -.
DR   Bgee; P06802; -.
DR   Genevestigator; P06802; -.
DR   GermOnline; ENSMUSG00000037370; Mus musculus.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004551; F:nucleotide diphosphatase activity; IEA:EC.
DR   GO; GO:0004528; F:phosphodiesterase I activity; IEA:EC.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR   GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR   GO; GO:0046849; P:bone remodeling; IMP:MGI.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:BHF-UCL.
DR   GO; GO:0030279; P:negative regulation of ossification; IMP:MGI.
DR   InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
DR   InterPro; IPR017850; Alkaline_phosphatase_core.
DR   InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR   InterPro; IPR020821; Extracellular_endonuc_su_A.
DR   InterPro; IPR002591; Phosphodiest/P_Trfase.
DR   InterPro; IPR020436; Somatomedin_B_chordata.
DR   InterPro; IPR001212; Somatomedin_B_dom.
DR   Gene3D; G3DSA:3.40.720.10; Alk_phosphtse; 2.
DR   Gene3D; G3DSA:3.40.570.10; Endonuclease; 1.
DR   Pfam; PF01223; Endonuclease_NS; 1.
DR   Pfam; PF01663; Phosphodiest; 1.
DR   Pfam; PF01033; Somatomedin_B; 2.
DR   PRINTS; PR00022; SOMATOMEDINB.
DR   SMART; SM00892; Endonuclease_NS; 1.
DR   SMART; SM00477; NUC; 1.
DR   SMART; SM00201; SO; 2.
DR   SUPFAM; SSF53649; Alkaline_phosphatase_core; 1.
DR   PROSITE; PS00524; SMB_1; 2.
DR   PROSITE; PS50958; SMB_2; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Biomineralization; Cell membrane;
KW   Direct protein sequencing; Disease mutation; Disulfide bond;
KW   Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW   Multifunctional enzyme; Phosphoprotein; Polymorphism; Repeat;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN         1    906       Ectonucleotide
FT                                pyrophosphatase/phosphodiesterase family
FT                                member 1.
FT                                /FTId=PRO_0000188565.
FT   TOPO_DOM      1     58       Cytoplasmic (Potential).
FT   TRANSMEM     59     79       Helical; Signal-anchor for type II
FT                                membrane protein; (Potential).
FT   TOPO_DOM     80    906       Extracellular (Potential).
FT   DOMAIN       86    126       SMB 1.
FT   DOMAIN      127    171       SMB 2.
FT   REGION      173    573       Phosphodiesterase.
FT   REGION      635    906       Nuclease.
FT   MOTIF        27     34       Di-leucine motif.
FT   ACT_SITE    238    238       AMP-threonine intermediate.
FT   METAL       200    200       Divalent metal cation 2 (Probable).
FT   METAL       358    358       Divalent metal cation 1 (Probable).
FT   METAL       362    362       Divalent metal cation 1 (Probable).
FT   METAL       405    405       Divalent metal cation 2 (Probable).
FT   METAL       406    406       Divalent metal cation 2 (Probable).
FT   METAL       517    517       Divalent metal cation 1 (Probable).
FT   SITE        896    896       Essential for catalytic activity (By
FT                                similarity).
FT   CARBOHYD    161    161       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    267    267       N-linked (GlcNAc...).
FT   CARBOHYD    323    323       N-linked (GlcNAc...).
FT   CARBOHYD    459    459       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    567    567       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    624    624       N-linked (GlcNAc...).
FT   DISULFID     90    104       Alternate (By similarity).
FT   DISULFID     90     94       Alternate (By similarity).
FT   DISULFID     94    122       Alternate (By similarity).
FT   DISULFID    102    115       Alternate (By similarity).
FT   DISULFID    102    104       Alternate (By similarity).
FT   DISULFID    108    114       By similarity.
FT   DISULFID    115    122       Alternate (By similarity).
FT   DISULFID    131    148       Alternate (By similarity).
FT   DISULFID    131    136       Alternate (By similarity).
FT   DISULFID    136    166       Alternate (By similarity).
FT   DISULFID    146    159       Alternate (By similarity).
FT   DISULFID    146    148       Alternate (By similarity).
FT   DISULFID    152    158       By similarity.
FT   DISULFID    159    166       Alternate (By similarity).
FT   DISULFID    462    849       By similarity.
FT   VAR_SEQ     630    630       Missing (in isoform 1).
FT                                /FTId=VSP_006748.
FT   VARIANT     651    651       H -> R (in allele ENPP1b).
FT   VARIANT     680    680       R -> S (in allele ENPP1b).
FT   MUTAGEN      28     28       A->G: No effect on basolateral sorting in
FT                                epithelial cells.
FT   MUTAGEN      30     30       S->A,D: Little change in baolateral
FT                                sorting in epithelial cells.
FT   MUTAGEN      31     31       L->A: 60% of ENPP1 redirected to apical
FT                                surface in epithelial cells. 75% of ENPP1
FT                                redirected to apical surface in
FT                                epithelial cells; abrogation of increased
FT                                NPP activity in oestoblastic matrix
FT                                vesicles; when associated with A-32.
FT   MUTAGEN      32     32       L->A: 70% of ENPP1 redirected to apical
FT                                surface in epithelial cells; abrogation
FT                                of increased NPP activity in oestoblastic
FT                                matrix vesicles. 75% of ENPP1 redirected
FT                                to apical surface in epithelial cells;
FT                                abrogation of increased NPP activity in
FT                                oestoblastic matrix vesicles; when
FT                                associated with A-31.
FT   MUTAGEN      42     42       L->A: No change in increased NPP activity
FT                                in oestoblastic matrix vesicles.
FT   MUTAGEN      57     57       Y->G: No change in increased NPP activity
FT                                in oestoblastic matrix vesicles.
FT   MUTAGEN     200    200       D->N: Decreases phosphodiesterase
FT                                activity by 95%. Abolishes formation of
FT                                nucleotidylated intermediate.
FT   MUTAGEN     237    237       K->A: Decreases phosphodiesterase
FT                                activity by 40%. Decreased formation of
FT                                nucleotidylated intermediate.
FT   MUTAGEN     238    238       T->A: Abolishes all phosphodiesterase
FT                                activity. Abolishes formation of
FT                                nucleotidylated intermediate.
FT   MUTAGEN     238    238       T->S: Decreases phosphodiesterase
FT                                activity by 95%. Accumulates
FT                                nucleotidylated intermediate.
FT   MUTAGEN     239    239       F->A: Decreases phosphodiesterase
FT                                activity by 50%. Decreased formation of
FT                                nucleotidylated intermediate.
FT   MUTAGEN     358    358       D->Q: Decreases phosphodiesterase
FT                                activity by 90%. Accumulates
FT                                nucleotidylated intermediate.
FT   MUTAGEN     362    362       H->Q: Decreases phosphodiesterase
FT                                activity by 95%. 65% activity can be
FT                                restored by addition of Zn(2+) ions.
FT                                Accumulates nucleotidylated intermediate.
FT   MUTAGEN     405    405       D->N: Abolishes all phosphodiesterase
FT                                activity. 10% activity can be restored by
FT                                addition of Zn(2+) ions. Abolishes
FT                                formation of nucleotidylated
FT                                intermediate.
FT   MUTAGEN     406    406       H->Q: Abolishes all phosphodiesterase
FT                                activity. 15% activity can be restored by
FT                                addition of Zn(2+) ions. Abolishes
FT                                formation of nucleotidylated
FT                                intermediate.
FT   MUTAGEN     517    517       H->Q: Abolishes all phosphodiesterase
FT                                activity. 60% activity can be restored by
FT                                addition of Zn(2+) ions. Abolishes
FT                                formation of nucleotidylated
FT                                intermediate.
SQ   SEQUENCE   906 AA;  103176 MW;  068D45B0ED0F224D CRC64;
     MERDGDQAGH GPRHGSAGNG RELESPAAAS LLAPMDLGEE PLEKAERARP AKDPNTYKVL
     SLVLSVCVLT TILGCIFGLK PSCAKEVKSC KGRCFERTFS NCRCDAACVS LGNCCLDFQE
     TCVEPTHIWT CNKFRCGEKR LSRFVCSCAD DCKTHNDCCI NYSSVCQDKK SWVEETCESI
     DTPECPAEFE SPPTLLFSLD GFRAEYLHTW GGLLPVISKL KNCGTYTKNM RPMYPTKTFP
     NHYSIVTGLY PESHGIIDNK MYDPKMNASF SLKSKEKFNP LWYKGQPIWV TANHQEVKSG
     TYFWPGSDVE IDGILPDIYK VYNGSVPFEE RILAVLEWLQ LPSHERPHFY TLYLEEPDSS
     GHSHGPVSSE VIKALQKVDR LVGMLMDGLK DLGLDKCLNL ILISDHGMEQ GSCKKYVYLN
     KYLGDVNNVK VVYGPAARLR PTDVPETYYS FNYEALAKNL SCREPNQHFR PYLKPFLPKR
     LHFAKSDRIE PLTFYLDPQW QLALNPSERK YCGSGFHGSD NLFSNMQALF IGYGPAFKHG
     AEVDSFENIE VYNLMCDLLG LIPAPNNGSH GSLNHLLKKP IYNPSHPKEE GFLSQCPIKS
     TSNDLGCTCD PWIVPIKDFE KQLNLTTEDV DDIYHMTVPY GRPRILLKQH HVCLLQQQQF
     LTGYSLDLLM PLWASYTFLR NDQFSRDDFS NCLYQDLRIP LSPVHKCSYY KSNSKLSYGF
     LTPPRLNRVS NHIYSEALLT SNIVPMYQSF QVIWHYLHDT LLQRYAHERN GINVVSGPVF
     DFDYDGRYDS LEILKQNSRV IRSQEILIPT HFFIVLTSCK QLSETPLECS ALESSAYILP
     HRPDNIESCT HGKRESSWVE ELLTLHRARV TDVELITGLS FYQDRQESVS ELLRLKTHLP
     IFSQED
//
ID   NEUM_MOUSE              Reviewed;         227 AA.
AC   P06837;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   08-MAR-2011, entry version 109.
DE   RecName: Full=Neuromodulin;
DE   AltName: Full=Axonal membrane protein GAP-43;
DE   AltName: Full=Calmodulin-binding protein P-57;
DE   AltName: Full=Growth-associated protein 43;
GN   Name=Gap43; Synonyms=Basp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=87308218; PubMed=2442159;
RA   Cimler B.M., Giebelhaus D.H., Wakim B.T., Storm D.R., Moon R.T.;
RT   "Characterization of murine cDNAs encoding P-57, a neural-specific
RT   calmodulin-binding protein.";
RL   J. Biol. Chem. 262:12158-12163(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 84-104, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND THR-172, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15648052; DOI=10.1002/pmic.200401066;
RA   Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA   Hart G.W., Burlingame A.L.;
RT   "Quantitative analysis of both protein expression and serine /
RT   threonine post-translational modifications through stable isotope
RT   labeling with dithiothreitol.";
RL   Proteomics 5:388-398(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-172, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-95; SER-103 AND THR-172,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: This protein is associated with nerve growth. It is a
CC       major component of the motile "growth cones" that form the tips of
CC       elongating axons.
CC   -!- SUBUNIT: Binds calmodulin with a greater affinity in the absence
CC       of Ca(2+) than in its presence (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Cell projection, growth cone membrane;
CC       Peripheral membrane protein; Cytoplasmic side. Cell junction,
CC       synapse. Note=Cytoplasmic surface of growth cone and synaptic
CC       plasma membranes.
CC   -!- PTM: Phosphorylation of this protein by a protein kinase C is
CC       specifically correlated with certain forms of synaptic plasticity.
CC   -!- SIMILARITY: Belongs to the neuromodulin family.
CC   -!- SIMILARITY: Contains 1 IQ domain.
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DR   EMBL; J02809; AAA37377.1; -; mRNA.
DR   EMBL; BC028288; AAH28288.1; -; mRNA.
DR   EMBL; BC080758; AAH80758.1; -; mRNA.
DR   IPI; IPI00128973; -.
DR   PIR; A29800; A29800.
DR   RefSeq; NP_032109.1; NM_008083.2.
DR   UniGene; Mm.1222; -.
DR   STRING; P06837; -.
DR   PhosphoSite; P06837; -.
DR   PRIDE; P06837; -.
DR   Ensembl; ENSMUST00000102817; ENSMUSP00000099881; ENSMUSG00000047261.
DR   GeneID; 14432; -.
DR   KEGG; mmu:14432; -.
DR   UCSC; uc007zfv.1; mouse.
DR   CTD; 14432; -.
DR   MGI; MGI:95639; Gap43.
DR   eggNOG; roNOG16581; -.
DR   GeneTree; ENSGT00530000063966; -.
DR   HOGENOM; HBG282505; -.
DR   HOVERGEN; HBG006468; -.
DR   InParanoid; P06837; -.
DR   OMA; READQEH; -.
DR   NextBio; 286053; -.
DR   ArrayExpress; P06837; -.
DR   Bgee; P06837; -.
DR   CleanEx; MM_GAP43; -.
DR   Genevestigator; P06837; -.
DR   GermOnline; ENSMUSG00000047261; Mus musculus.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0032584; C:growth cone membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0016198; P:axon choice point recognition; IMP:MGI.
DR   GO; GO:0045165; P:cell fate commitment; IMP:MGI.
DR   GO; GO:0010001; P:glial cell differentiation; IMP:MGI.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001422; Neuromodulin.
DR   InterPro; IPR017454; Neuromodulin_C.
DR   InterPro; IPR018947; Neuromodulin_gap-junction_N.
DR   InterPro; IPR018243; Neuromodulin_palmitoyl/P_site.
DR   Pfam; PF00612; IQ; 1.
DR   Pfam; PF06614; Neuromodulin; 1.
DR   Pfam; PF10580; Neuromodulin_N; 1.
DR   PRINTS; PR00215; NEUROMODULIN.
DR   SMART; SM00015; IQ; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS00412; NEUROMODULIN_1; 1.
DR   PROSITE; PS00413; NEUROMODULIN_2; 1.
PE   1: Evidence at protein level;
KW   Calmodulin-binding; Cell junction; Cell membrane; Cell projection;
KW   Developmental protein; Differentiation; Direct protein sequencing;
KW   Growth regulation; Lipoprotein; Membrane; Neurogenesis; Palmitate;
KW   Phosphoprotein; Synapse.
FT   CHAIN         1    227       Neuromodulin.
FT                                /FTId=PRO_0000159597.
FT   DOMAIN       31     60       IQ.
FT   REGION        1      4       Important for membrane binding.
FT   MOD_RES      41     41       Phosphoserine.
FT   MOD_RES      95     95       Phosphothreonine.
FT   MOD_RES      96     96       Phosphoserine.
FT   MOD_RES     103    103       Phosphoserine.
FT   MOD_RES     172    172       Phosphothreonine.
FT   MOD_RES     192    192       Phosphoserine; by CK2 (By similarity).
FT   MOD_RES     193    193       Phosphoserine; by CK2 (By similarity).
FT   LIPID         3      3       S-palmitoyl cysteine (By similarity).
FT   LIPID         4      4       S-palmitoyl cysteine (By similarity).
SQ   SEQUENCE   227 AA;  23632 MW;  14803B2F8F0649F7 CRC64;
     MLCCMRRTKQ VEKNDEDQKI EQDGVKPEDK AHKAATKIQA SFRGHITRKK LKGEKKGDAP
     AAEAEAKEKD DAPVADGVEK KEGDGSATTD AAPATSPKAE EPSKAGDAPS EEKKGEGDAA
     PSEEKAGSAE TESAAKATTD NSPSSKAEDG PAKEEPKQAD VPAAVTDAAA TTPAAEDAAT
     KAAQPPTETA ESSQAEEEKD AVDEAKPKES ARQDEGKEDP EADQEHA
//
ID   HS90A_MOUSE             Reviewed;         733 AA.
AC   P07901;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   08-MAR-2011, entry version 129.
DE   RecName: Full=Heat shock protein HSP 90-alpha;
DE   AltName: Full=Heat shock 86 kDa;
DE            Short=HSP 86;
DE            Short=HSP86;
DE   AltName: Full=Tumor-specific transplantation 86 kDa antigen;
DE            Short=TSTA;
GN   Name=Hsp90aa1; Synonyms=Hsp86, Hsp86-1, Hspca;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=89174568; PubMed=2925609;
RA   Moore S.K., Kozak C., Robinson E.A., Ullrich S.J., Appella E.;
RT   "Murine 86- and 84-kDa heat shock proteins, cDNA sequences, chromosome
RT   assignments, and evolutionary origins.";
RL   J. Biol. Chem. 264:5343-5351(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=92009901; PubMed=1916807; DOI=10.1016/0888-7543(91)90193-I;
RA   Moore S.K., Appella E., Villar C.J., Kozak C.A.;
RT   "Mapping of the mouse 86-kDa heat-shock protein expressed gene (Hsp86-
RT   1) on chromosome 12 and related genes on chromosomes 3, 4, 9, and
RT   11.";
RL   Genomics 10:1019-1029(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-31.
RX   MEDLINE=86205848; PubMed=3458168; DOI=10.1073/pnas.83.10.3121;
RA   Ullrich S.J., Robinson E.A., Law L.W., Willingham M., Appella E.;
RT   "A mouse tumor-specific transplantation antigen is a heat shock-
RT   related protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:3121-3125(1986).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-356.
RX   MEDLINE=89232740; PubMed=2469626; DOI=10.1016/0378-1119(88)90182-5;
RA   Hoffmann T., Hovemann B.;
RT   "Heat-shock proteins, Hsp84 and Hsp86, of mice and men: two related
RT   genes encode formerly identified tumour-specific transplantation
RT   antigens.";
RL   Gene 74:491-501(1988).
RN   [6]
RP   PROTEIN SEQUENCE OF 47-58; 61-69; 75-84; 88-112; 154-173; 186-201;
RP   210-224; 285-356; 369-401; 448-457; 491-511; 515-535; 548-561;
RP   569-574; 593-632 AND 634-648.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 460-733.
RX   MEDLINE=90033873; PubMed=2806771;
RX   DOI=10.1111/j.1432-0436.1989.tb00730.x;
RA   Legagneux V., Mezger V., Quelard C., Barnier J.V., Bensaude O.,
RA   Morange M.;
RT   "High constitutive transcription of HSP86 gene in murine embryonal
RT   carcinoma cells.";
RL   Differentiation 41:42-48(1989).
RN   [8]
RP   PHOSPHORYLATION BY DS-DNA KINASE.
RX   MEDLINE=90008887; PubMed=2507541;
RA   Lees-Miller S.P., Anderson C.W.;
RT   "The human double-stranded DNA-activated protein kinase phosphorylates
RT   the 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminal
RT   threonine residues.";
RL   J. Biol. Chem. 264:17275-17280(1989).
RN   [9]
RP   ISGYLATION.
RX   PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA   Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA   Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT   "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT   human cells.";
RL   Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-493, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-263, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-314, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-263, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Molecular chaperone. Has ATPase activity (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with AHSA1, FNIP1,
CC       HSF1, SMYD3 and TOM34. Interacts with TERT; the interaction,
CC       together with PTGES3/P23, is required for correct assembly and
CC       stabilization of the TERT holoenzyme complex. Interacts with
CC       CHORDC1 and DNAJC7 (By similarity).
CC   -!- INTERACTION:
CC       P30561:Ahr; NbExp=1; IntAct=EBI-78930, EBI-78863;
CC       P07900:HSP90AA1 (xeno); NbExp=1; IntAct=EBI-78930, EBI-296047;
CC       Q61045:Sim1; NbExp=1; IntAct=EBI-78930, EBI-78890;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome (By similarity).
CC   -!- PTM: ISGylated.
CC   -!- SIMILARITY: Belongs to the heat shock protein 90 family.
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DR   EMBL; J04633; AAA53068.1; -; mRNA.
DR   EMBL; M57673; AAA37867.1; -; Genomic_DNA.
DR   EMBL; BC046614; AAH46614.1; -; mRNA.
DR   EMBL; M36830; AAA37868.1; -; mRNA.
DR   EMBL; X16857; CAA34748.1; -; mRNA.
DR   IPI; IPI00330804; -.
DR   PIR; B32848; HHMS86.
DR   RefSeq; NP_034610.1; NM_010480.5.
DR   UniGene; Mm.1843; -.
DR   UniGene; Mm.341186; -.
DR   ProteinModelPortal; P07901; -.
DR   SMR; P07901; 11-698.
DR   IntAct; P07901; 5.
DR   MINT; MINT-152660; -.
DR   STRING; P07901; -.
DR   PhosphoSite; P07901; -.
DR   REPRODUCTION-2DPAGE; P07901; -.
DR   PRIDE; P07901; -.
DR   Ensembl; ENSMUST00000021698; ENSMUSP00000021698; ENSMUSG00000021270.
DR   Ensembl; ENSMUST00000094361; ENSMUSP00000091921; ENSMUSG00000021270.
DR   GeneID; 15519; -.
DR   KEGG; mmu:15519; -.
DR   UCSC; uc007pbr.1; mouse.
DR   CTD; 15519; -.
DR   MGI; MGI:96250; Hsp90aa1.
DR   HOGENOM; HBG631012; -.
DR   HOVERGEN; HBG007374; -.
DR   InParanoid; P07901; -.
DR   OMA; TEGYWKV; -.
DR   OrthoDB; EOG42V8FM; -.
DR   PhylomeDB; P07901; -.
DR   NextBio; 288436; -.
DR   ArrayExpress; P07901; -.
DR   Bgee; P07901; -.
DR   Genevestigator; P07901; -.
DR   GermOnline; ENSMUSG00000021270; Mus musculus.
DR   GO; GO:0005829; C:cytosol; TAS:UniProtKB.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030235; F:nitric-oxide synthase regulator activity; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
DR   GO; GO:0030911; F:TPR domain binding; ISS:UniProtKB.
DR   GO; GO:0051082; F:unfolded protein binding; TAS:UniProtKB.
DR   GO; GO:0006809; P:nitric oxide biosynthetic process; TAS:UniProtKB.
DR   GO; GO:0045585; P:positive regulation of cytotoxic T cell differentiation; TAS:UniProtKB.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0042026; P:protein refolding; TAS:UniProtKB.
DR   GO; GO:0006986; P:response to unfolded protein; TAS:UniProtKB.
DR   InterPro; IPR003594; ATPase-like_ATP-bd.
DR   InterPro; IPR019805; Heat_shock_protein_90_CS.
DR   InterPro; IPR001404; Hsp90.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   Gene3D; G3DSA:3.30.565.10; ATP_bd_ATPase; 2.
DR   PANTHER; PTHR11528; Hsp90; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATP_bd_ATPase; 1.
DR   SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Chaperone; Cytoplasm;
KW   Direct protein sequencing; Nucleotide-binding; Phosphoprotein;
KW   Stress response; Ubl conjugation.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    733       Heat shock protein HSP 90-alpha.
FT                                /FTId=PRO_0000062912.
FT   MOD_RES       5      5       Phosphothreonine; by PRKDC.
FT   MOD_RES       7      7       Phosphothreonine; by PRKDC.
FT   MOD_RES     224    224       N6-acetyllysine (By similarity).
FT   MOD_RES     231    231       Phosphoserine.
FT   MOD_RES     252    252       Phosphoserine (By similarity).
FT   MOD_RES     263    263       Phosphoserine.
FT   MOD_RES     314    314       Phosphotyrosine.
FT   MOD_RES     400    400       Phosphoserine (By similarity).
FT   MOD_RES     411    411       N6-acetyllysine (By similarity).
FT   MOD_RES     444    444       N6-acetyllysine (By similarity).
FT   MOD_RES     459    459       N6-acetyllysine (By similarity).
FT   MOD_RES     490    490       N6-acetyllysine (By similarity).
FT   MOD_RES     493    493       Phosphotyrosine.
FT   MOD_RES     577    577       N6-acetyllysine (By similarity).
FT   MOD_RES     586    586       N6-acetyllysine (By similarity).
FT   CONFLICT      7      7       T -> A (in Ref. 5; AAA37868).
FT   CONFLICT    242    245       Missing (in Ref. 5; AAA37868).
FT   CONFLICT    356    356       R -> K (in Ref. 5; AAA37868).
SQ   SEQUENCE   733 AA;  84788 MW;  D92B8FD38A463B4E CRC64;
     MPEETQTQDQ PMEEEEVETF AFQAEIAQLM SLIINTFYSN KEIFLRELIS NSSDALDKIR
     YESLTDPSKL DSGKELHINL IPSKQDRTLT IVDTGIGMTK ADLINNLGTI AKSGTKAFME
     ALQAGADISM IGQFGVGFYS AYLVAEKVTV ITKHNDDEQY AWESSAGGSF TVRTDTGEPM
     GRGTKVILHL KEDQTEYLEE RRIKEIVKKH SQFIGYPITL FVEKERDKEV SDDEAEEKEE
     KEEEKEKEEK ESDDKPEIED VGSDEEEEEK KDGDKKKKKK IKEKYIDQEE LNKTKPIWTR
     NPDDITNEEY GEFYKSLTND WEEHLAVKHF SVEGQLEFRA LLFVPRRAPF DLFENRKKKN
     NIKLYVRRVF IMDNCEELIP EYLNFIRGVV DSEDLPLNIS REMLQQSKIL KVIRKNLVKK
     CLELFTELAE DKENYKKFYE QFSKNIKLGI HEDSQNRKKL SELLRYYTSA SGDEMVSLKD
     YCTRMKENQK HIYFITGETK DQVANSAFVE RLRKHGLEVI YMIEPIDEYC VQQLKEFEGK
     TLVSVTKEGL ELPEDEEEKK KQEEKKTKFE NLCKIMKDIL EKKVEKVVVS NRLVTSPCCI
     VTSTYGWTAN MERIMKAQAL RDNSTMGYMA AKKHLEINPD HSIIETLRQK AEADKNDKSV
     KDLVILLYET ALLSSGFSLE DPQTHANRIY RMIKLGLGID EDDPTVDDTS AAVTEEMPPL
     EGDDDTSRME EVD
//
ID   SPTA1_MOUSE             Reviewed;        2415 AA.
AC   P08032; B2RWX6; P97502;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 3.
DT   08-MAR-2011, entry version 105.
DE   RecName: Full=Spectrin alpha chain, erythrocyte;
DE   AltName: Full=Erythroid alpha-spectrin;
GN   Name=Spta1; Synonyms=Spna1, Spta;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ;
RA   Burnett R.C., Avery A.C., Swardson C.J.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Birkenmeier C.S., Gifford E.J., Barker J.E.;
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1567-1819.
RX   MEDLINE=86083178; PubMed=3000887; DOI=10.1016/0378-1119(85)90191-X;
RA   Curtis P.J., Palumbo A., Ming J., Fraser P.J., Cioe L., Meo P.,
RA   Shane S., Rovera G.;
RT   "Sequence comparison of human and murine erythrocyte alpha-spectrin
RT   cDNA.";
RL   Gene 36:357-362(1985).
CC   -!- FUNCTION: Spectrin is the major constituent of the cytoskeletal
CC       network underlying the erythrocyte plasma membrane. It associates
CC       with band 4.1 and actin to form the cytoskeletal superstructure of
CC       the erythrocyte plasma membrane.
CC   -!- SUBUNIT: Composed of non-homologous chains, alpha and beta, which
CC       aggregate to form dimers, tetramers, and higher polymers.
CC       Interacts with FASLG (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell
CC       cortex.
CC   -!- MISCELLANEOUS: This complex is anchored to the cytoplasmic face of
CC       the plasma membrane via another protein, ankyrin, which binds to
CC       beta-spectrin and mediates the binding of the whole complex to a
CC       transmembrane protein band 3. The interaction of erythrocyte
CC       spectrin with other proteins through specific binding domains lead
CC       to the formation of an extensive subplasmalemmal meshwork which is
CC       thought to be responsible for the maintenance of the biconcave
CC       shape of human erythrocytes, for the regulation of plasma membrane
CC       components and for the maintenance of the lipid asymmetry of the
CC       plasma membrane.
CC   -!- SIMILARITY: Belongs to the spectrin family.
CC   -!- SIMILARITY: Contains 3 EF-hand domains.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SIMILARITY: Contains 21 spectrin repeats.
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DR   EMBL; U87455; AAB47540.1; -; mRNA.
DR   EMBL; AF093576; AAC61874.1; -; mRNA.
DR   EMBL; AC113483; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC156549; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC150747; AAI50748.1; -; mRNA.
DR   EMBL; M10276; AAA40123.1; -; mRNA.
DR   IPI; IPI00323230; -.
DR   PIR; A05283; A05283.
DR   RefSeq; NP_035595.2; NM_011465.4.
DR   UniGene; Mm.200611; -.
DR   ProteinModelPortal; P08032; -.
DR   SMR; P08032; 4-2260, 2264-2342, 2345-2415.
DR   STRING; P08032; -.
DR   PhosphoSite; P08032; -.
DR   PRIDE; P08032; -.
DR   Ensembl; ENSMUST00000027817; ENSMUSP00000027817; ENSMUSG00000026532.
DR   GeneID; 20739; -.
DR   KEGG; mmu:20739; -.
DR   UCSC; uc007dsw.1; mouse.
DR   CTD; 20739; -.
DR   MGI; MGI:98385; Spna1.
DR   eggNOG; roNOG10130; -.
DR   HOGENOM; HBG315379; -.
DR   HOVERGEN; HBG059266; -.
DR   InParanoid; P08032; -.
DR   OMA; YLADLHE; -.
DR   OrthoDB; EOG4PC9R6; -.
DR   ArrayExpress; P08032; -.
DR   Bgee; P08032; -.
DR   CleanEx; MM_SPNA1; -.
DR   Genevestigator; P08032; -.
DR   GermOnline; ENSMUSG00000026532; Mus musculus.
DR   GO; GO:0032437; C:cuticular plate; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0008091; C:spectrin; TAS:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR   GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR   GO; GO:0006779; P:porphyrin biosynthetic process; IMP:MGI.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR014837; EF-hand_Ca_insen.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR013315; Spectrin_alpha_SH3.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   Pfam; PF08726; efhand_Ca_insen; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF00435; Spectrin; 20.
DR   PRINTS; PR01887; SPECTRNALPHA.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00150; SPEC; 20.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50222; EF_HAND_2; 3.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   Actin capping; Actin-binding; Calcium; Cell shape; Cytoplasm;
KW   Cytoskeleton; Repeat; SH3 domain.
FT   CHAIN         1   2415       Spectrin alpha chain, erythrocyte.
FT                                /FTId=PRO_0000073453.
FT   REPEAT       18     50       Spectrin 1.
FT   REPEAT       52    154       Spectrin 2.
FT   REPEAT      156    260       Spectrin 3.
FT   REPEAT      262    366       Spectrin 4.
FT   REPEAT      368    472       Spectrin 5.
FT   REPEAT      474    578       Spectrin 6.
FT   REPEAT      580    683       Spectrin 7.
FT   REPEAT      685    789       Spectrin 8.
FT   REPEAT      791    895       Spectrin 9.
FT   REPEAT      897    966       Spectrin 10.
FT   DOMAIN      975   1034       SH3.
FT   REPEAT     1080   1179       Spectrin 11.
FT   REPEAT     1181   1285       Spectrin 12.
FT   REPEAT     1287   1391       Spectrin 13.
FT   REPEAT     1393   1496       Spectrin 14.
FT   REPEAT     1498   1603       Spectrin 15.
FT   REPEAT     1605   1709       Spectrin 16.
FT   REPEAT     1711   1815       Spectrin 17.
FT   REPEAT     1817   1922       Spectrin 18.
FT   REPEAT     1924   2029       Spectrin 19.
FT   REPEAT     2039   2143       Spectrin 20.
FT   REPEAT     2153   2254       Spectrin 21.
FT   DOMAIN     2267   2302       EF-hand 1.
FT   DOMAIN     2310   2345       EF-hand 2.
FT   DOMAIN     2347   2382       EF-hand 3.
FT   CA_BIND    2280   2291       1 (Potential).
FT   CA_BIND    2323   2334       2 (Potential).
FT   CONFLICT    337    337       P -> L (in Ref. 1; AAB47540).
FT   CONFLICT    501    501       D -> Y (in Ref. 4; AAI50748).
FT   CONFLICT    716    716       G -> V (in Ref. 1; AAB47540).
FT   CONFLICT    741    741       V -> M (in Ref. 1; AAB47540 and 4;
FT                                AAI50748).
FT   CONFLICT   1044   1045       RQ -> QR (in Ref. 1; AAB47540 and 4;
FT                                AAI50748).
FT   CONFLICT   1225   1225       V -> C (in Ref. 1; AAB47540).
FT   CONFLICT   1238   1238       T -> N (in Ref. 1; AAB47540).
FT   CONFLICT   1425   1425       N -> D (in Ref. 1; AAB47540).
FT   CONFLICT   1582   1582       K -> M (in Ref. 1; AAB47540).
FT   CONFLICT   2062   2062       L -> M (in Ref. 1; AAB47540 and 4;
FT                                AAI50748).
SQ   SEQUENCE   2415 AA;  279865 MW;  510B61CDEC4FAD13 CRC64;
     METPKETAVE SSGPKVLETA EEIQHRRAEV LNQYQRFKDR VAERGQKLEE SYHYQVFRRD
     ADDLEKWIME KLEIAKDKTY EPTNIQGKYQ KHESFVSEVQ AKSRVLPELE EIREARFAED
     HFAHEATKTH LKQLRLLWDL LLELTQEKSD VLLRALKFYQ YSQECEDILE WVKEKEAIVT
     LVELGDDWER TEVLHKKFEE FQEELTARKG KVDRVNQYAN ECAQEKHPKL PEIKAKQDEV
     NAAWDRLWSL ALKRRESLSN AADLQRFKRD VNEAIQWMEE KEPQLTSEDY GKDLVSSEAL
     FHNHKRLERN LAVMDDKVKE LCAKADKLMI SHSADAPQIQ QMKLDLVSNW ERIRALATNR
     YAKLKASYGY HRFLSDYDEL SGWMKEKTAL INADELPTDV ASGEALLARH QQHKHEIDSY
     DDRFQSADAT GQELLDGNHE ASEEIREKMT ILANDWAALL ELWDKCQHQY RQCLDFHLFY
     RDSEQVDSWM SRQEAFLENE DLGNSVGSVE ALLQKHDDFE EAFTAQEEKI ITLDETATKL
     IDNDHYDSEN IAAIRDGLLA RRDALRERAA TRRKLLVDSQ LLQQLYQDSD DLKTWINKKK
     KLADDDDYKD VQNLKSRVQK QQDFEEELAV NEIMLNNLEK TGQEMIEDGH YASEAVAARL
     SEVANLWKEL LEATAQKGTQ LYEANQLLQF ENNAEDLKRW LEEVEWQVTS EDYGKGLADV
     QNLLRKHGLL ESDVTARQNQ VDTLTDMAAH FEEIGHPDSG DIRARQESLL SRFEALKEPL
     AIRKKKLIDL LKLQQICRDS EDEEAWIQET EPSAASTHLG KDLVAAKNLL NRHEVILADI
     ASHEPRIQVI TERGNKMVEE GHFAAEDIAS RVESLNKNME SLHARAIRRE NDLKANVQLQ
     QYLADLHEAE AWIKEKEPIV DNKNYGADEE AAGALLKKHE AFLVDLNAFE NSIKALRDQA
     EVCQQQQAAP VDEAGREARV IALYDFEARS RREVSMKKND VLTLLSSINK DWWKVEADDH
     QGFVPAVYVR KLAPDELPGF PQHRQEEPVN IPQLQQQVET LYHSLLDRAE ERRRRLLQRY
     NEFLLAYEAG DMLEWIQEKK TENTGVELDD VWELQKKFDE FQRDLKSNEP RLKDINKVAD
     ELLFEELLTP EGAHIRQELN TRWNSLKRLA DEQYQLLSSA HAVEMFHREA DDVKEQIDKK
     CRALNAADPG SDLLSVQALQ RQHEVFERDI IPLGEKVTTL GETAERLCES HPDATEDLQK
     QRTELNEAWD TLQGLTSDRK ESLNEAHKFF LFLSKASDLE NWIKTIGGVI SSPELAEDLT
     GTEILLERHQ EHHDDIKRED PTFQALEDFG TELIDSGHRN RREIDNTLQN INSKRDNLEK
     SWENRKKMLD QCLELQLFRG KCDQVESWMV ARENSLRSDD RDHLNSLQAL MKKRDDLDKA
     ITAQEGKISD LENVATRLID NDHYAKEEIA ARLQRVLDRW KALKEQLLTE LGKLGDYADL
     KQFYRDLEDL EEWINEMLPI ACDESYKDPT NIQRKYLKHQ AFENEVNGRA EQVDGVINLG
     NSLIERRVCD GDEENMQEQL DKLKENWDYL LERTTDKGQK LNEASRQQRF NTSIRDFEFW
     LSEAEGLLAM KDQARDLTSA GNLLKKHQLL EAEMLAREDP LKDLNDLAQE LISSGTFNID
     QIEEKMNGVN ERFENVQSLA AAHHEKLKET YALFQFFQDL DDEEAWIEEK LLRVSSQDYG
     RDLQSVQNLL KKHKRLEGEL VAHEPAVQNV LDTAESLRDK AAVGKEEIQE RLAQFVQHWE
     KLKELAKTRG VNLEESLEYL QFMENAEEEE AWLGEKCALV SRGDSGDTLA ATQSLLKKHE
     ALENDFAVHK NRVQDVCAQG EDILNKEETQ NKDKISTKIQ VLNEKTASLA KALAAWKSQL
     DDVHAFQQFN WKADVVESWI GEKEASLKTK SNGADLTAFL TLLAKHDTLD ASLQSFQQER
     LSEIAELKDQ LVAGEHSQAK AIEEQHAALL RHWEQLLEAS RVHRQKLLEK QLPLQKAEEL
     FMEFAHKASA FNNWCENAEE DLSEPVHCVS LNEIRQLQKE HEAFLASLAG AQEDFNYLLE
     LDKQIKALNV PSSPYTWLTV DVLGRIWNHL PDIIKEREQE LQKEEARQIK NFEMCQEFEQ
     NASAFLQWIQ ETRAYFLDGS LLKETGTLES QLEANKRKQK EIQAMKRHLT KIEDLGDSME
     EALILDIKYS TIGLAQQWDQ LHQLGMRMQH NLEQQIQAKD TIGVSEETLK EFSTTYKHFD
     ENLTGRLTHK EFRSCLRGLN YYLPMVEEGE PEPKFEKFLN AVDPGRKGYV SLEDYTSFLI
     DKESENIKTS DDIESAFQAL AEGKAYITKE DMKQALTPEQ VSFCTIHMQQ YMDPRGRSQP
     AGYDYVGFTN SFFGN
//
ID   APOE_MOUSE              Reviewed;         311 AA.
AC   P08226;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 2.
DT   08-MAR-2011, entry version 105.
DE   RecName: Full=Apolipoprotein E;
DE            Short=Apo-E;
DE   Flags: Precursor;
GN   Name=Apoe;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=89380144; PubMed=2550421;
RA   Horiuchi K., Tajima S., Menju M., Yamamoto A.;
RT   "Structure and expression of mouse apolipoprotein E gene.";
RL   J. Biochem. 106:98-103(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=86068046; PubMed=3865219; DOI=10.1073/pnas.82.23.8085;
RA   Rajavashisth T.B., Kaptein J.S., Reue K.L., Lusis A.J.;
RT   "Evolution of apolipoprotein E: mouse sequence and evidence for an 11-
RT   nucleotide ancestral unit.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:8085-8089(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 26-311.
RX   MEDLINE=91333018; PubMed=1870200;
RA   Diedrich J.F., Minnigan M., Carp R.I., Whitaker J.N., Race R.,
RA   Frey W. II, Haase A.T.;
RT   "Neuropathological changes in scrapie and Alzheimer's disease are
RT   associated with increased expression of apolipoprotein E and cathepsin
RT   D in astrocytes.";
RL   J. Virol. 65:4759-4768(1991).
RN   [5]
RP   PROTEIN SEQUENCE OF 114-122, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Mediates the binding, internalization, and catabolism of
CC       lipoprotein particles. It can serve as a ligand for the LDL (apo
CC       B/E) receptor and for the specific apo-E receptor (chylomicron
CC       remnant) of hepatic tissues.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Secreted in plasma.
CC   -!- PTM: Phosphorylation sites are present in the extracelllular
CC       medium (By similarity).
CC   -!- SIMILARITY: Belongs to the apolipoprotein A1/A4/E family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D00466; BAA00361.1; -; Genomic_DNA.
DR   EMBL; M12414; AAA37251.1; -; mRNA.
DR   EMBL; BC083351; AAH83351.1; -; mRNA.
DR   EMBL; M73490; AAA37252.1; -; mRNA.
DR   IPI; IPI00323571; -.
DR   PIR; JU0036; JU0036.
DR   RefSeq; NP_033826.2; NM_009696.3.
DR   UniGene; Mm.305152; -.
DR   PDB; 1YA9; X-ray; 2.09 A; A=20-200.
DR   PDBsum; 1YA9; -.
DR   ProteinModelPortal; P08226; -.
DR   SMR; P08226; 22-195.
DR   MINT; MINT-242645; -.
DR   STRING; P08226; -.
DR   PhosphoSite; P08226; -.
DR   PRIDE; P08226; -.
DR   Ensembl; ENSMUST00000003066; ENSMUSP00000003066; ENSMUSG00000002985.
DR   GeneID; 11816; -.
DR   KEGG; mmu:11816; -.
DR   CTD; 11816; -.
DR   MGI; MGI:88057; Apoe.
DR   eggNOG; roNOG10307; -.
DR   HOGENOM; HBG126848; -.
DR   HOVERGEN; HBG010582; -.
DR   InParanoid; P08226; -.
DR   OMA; EMGSRTR; -.
DR   OrthoDB; EOG4GB76S; -.
DR   PhylomeDB; P08226; -.
DR   NextBio; 279703; -.
DR   ArrayExpress; P08226; -.
DR   Bgee; P08226; -.
DR   CleanEx; MM_APOE; -.
DR   Genevestigator; P08226; -.
DR   GermOnline; ENSMUSG00000002985; Mus musculus.
DR   GO; GO:0042627; C:chylomicron; IEA:UniProtKB-KW.
DR   GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0034362; C:low-density lipoprotein particle; IDA:BHF-UCL.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0001540; F:beta-amyloid binding; ISS:UniProtKB.
DR   GO; GO:0017127; F:cholesterol transporter activity; IDA:MGI.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0071813; F:lipoprotein particle binding; IDA:MGI.
DR   GO; GO:0060228; F:phosphatidylcholine-sterol O-acyltransferase activator activity; IMP:BHF-UCL.
DR   GO; GO:0048844; P:artery morphogenesis; IGI:MGI.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:MGI.
DR   GO; GO:0006707; P:cholesterol catabolic process; IMP:MGI.
DR   GO; GO:0033344; P:cholesterol efflux; IDA:MGI.
DR   GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
DR   GO; GO:0006917; P:induction of apoptosis; ISS:UniProtKB.
DR   GO; GO:0042158; P:lipoprotein biosynthetic process; IGI:MGI.
DR   GO; GO:0042159; P:lipoprotein catabolic process; IMP:MGI.
DR   GO; GO:0034374; P:low-density lipoprotein particle remodeling; IMP:BHF-UCL.
DR   GO; GO:0051651; P:maintenance of location in cell; IMP:MGI.
DR   GO; GO:0010873; P:positive regulation of cholesterol esterification; IMP:BHF-UCL.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR   GO; GO:0002021; P:response to dietary excess; IMP:MGI.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
DR   GO; GO:0042311; P:vasodilation; IMP:MGI.
DR   GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IMP:BHF-UCL.
DR   InterPro; IPR013326; ApoA/E_ApoLp.
DR   InterPro; IPR000074; ApoA1_A4_E.
DR   Gene3D; G3DSA:1.20.120.20; ApoA/E_ApoLp; 2.
DR   Pfam; PF01442; Apolipoprotein; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chylomicron; Direct protein sequencing; HDL;
KW   Heparin-binding; Lipid transport; Phosphoprotein; Repeat; Secreted;
KW   Signal; Transport; VLDL.
FT   SIGNAL        1     18
FT   CHAIN        19    311       Apolipoprotein E.
FT                                /FTId=PRO_0000001990.
FT   REPEAT       72     93       1.
FT   REPEAT       94    115       2.
FT   REPEAT      116    137       3.
FT   REPEAT      138    159       4.
FT   REPEAT      160    181       5.
FT   REPEAT      182    203       6.
FT   REPEAT      204    225       7.
FT   REPEAT      226    247       8.
FT   REGION       72    247       8 X 22 AA approximate tandem repeats.
FT   REGION      150    160       LDL receptor binding (Potential).
FT   REGION      154    157       Heparin-binding (By similarity).
FT   REGION      221    228       Heparin-binding (By similarity).
FT   MOD_RES     139    139       Phosphoserine (By similarity).
FT   CONFLICT    163    163       E -> D (in Ref. 2; AAA37251).
FT   HELIX        29     31
FT   HELIX        34     50
FT   HELIX        55     62
FT   HELIX        65     90
FT   HELIX        97    134
FT   TURN        135    137
FT   HELIX       141    172
FT   HELIX       184    191
SQ   SEQUENCE   311 AA;  35867 MW;  3B36FA897CC34170 CRC64;
     MKALWAVLLV TLLTGCLAEG EPEVTDQLEW QSNQPWEQAL NRFWDYLRWV QTLSDQVQEE
     LQSSQVTQEL TALMEDTMTE VKAYKKELEE QLGPVAEETR ARLGKEVQAA QARLGADMED
     LRNRLGQYRN EVHTMLGQST EEIRARLSTH LRKMRKRLMR DAEDLQKRLA VYKAGAREGA
     ERGVSAIRER LGPLVEQGRQ RTANLGAGAA QPLRDRAQAF GDRIRGRLEE VGNQARDRLE
     EVREHMEEVR SKMEEQTQQI RLQAEIFQAR LKGWFEPIVE DMHRQWANLM EKIQASVATN
     PIITPVAQEN Q
//
ID   SODC_MOUSE              Reviewed;         154 AA.
AC   P08228;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 131.
DE   RecName: Full=Superoxide dismutase [Cu-Zn];
DE            EC=1.15.1.1;
GN   Name=Sod1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=SWR/J; TISSUE=Liver;
RX   MEDLINE=88203220; PubMed=3362683; DOI=10.1093/nar/16.6.2728;
RA   Bewley G.C.;
RT   "cDNA and deduced amino acid sequence of murine Cu-Zn superoxide
RT   dismutase.";
RL   Nucleic Acids Res. 16:2728-2728(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=91216458; PubMed=2022332; DOI=10.1016/0378-1119(91)90126-V;
RA   Benedetto M.T., Anzai Y., Gordon J.W.;
RT   "Isolation and analysis of the mouse genomic sequence encoding Cu(2+)-
RT   Zn2+ superoxide dismutase.";
RL   Gene 99:191-195(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Ovary, Urinary bladder, and Uterus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver, Mammary gland, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 4-23.
RX   MEDLINE=90361747; PubMed=2391363; DOI=10.1083/jcb.111.3.1217;
RA   Pluthero F.G., Shreeve M., Eskinazi D., van der Gaag H., Huang K.S.,
RA   Hulmes J.D., Blum M., Axelrad A.A.;
RT   "Purification of an inhibitor of erythroid progenitor cell cycling and
RT   antagonist to interleukin 3 from mouse marrow cell supernatants and
RT   its identification as cytosolic superoxide dismutase.";
RL   J. Cell Biol. 111:1217-1223(1990).
RN   [6]
RP   PROTEIN SEQUENCE OF 11-24 AND 104-116, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Klug S., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-71, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- FUNCTION: Destroys radicals which are normally produced within the
CC       cells and which are toxic to biological systems.
CC   -!- CATALYTIC ACTIVITY: 2 superoxide + 2 H(+) = O(2) + H(2)O(2).
CC   -!- COFACTOR: Binds 1 copper ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X06683; CAA29880.1; -; mRNA.
DR   EMBL; M60798; AAA40121.1; -; Genomic_DNA.
DR   EMBL; M60794; AAA40121.1; JOINED; Genomic_DNA.
DR   EMBL; M60795; AAA40121.1; JOINED; Genomic_DNA.
DR   EMBL; M60796; AAA40121.1; JOINED; Genomic_DNA.
DR   EMBL; M60797; AAA40121.1; JOINED; Genomic_DNA.
DR   EMBL; M35725; AAA37518.1; -; mRNA.
DR   EMBL; AK020624; BAB32154.1; -; mRNA.
DR   EMBL; AK077284; BAC36730.1; -; mRNA.
DR   EMBL; BC002066; AAH02066.1; -; mRNA.
DR   EMBL; BC048874; AAH48874.1; -; mRNA.
DR   EMBL; BC086886; AAH86886.1; -; mRNA.
DR   IPI; IPI00130589; -.
DR   PIR; JQ0915; JQ0915.
DR   RefSeq; NP_035564.1; NM_011434.1.
DR   UniGene; Mm.276325; -.
DR   UniGene; Mm.466779; -.
DR   PDB; 3GTT; X-ray; 2.40 A; A/B/C/D/E/F=2-154.
DR   PDB; 3GTV; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L=82-154.
DR   PDBsum; 3GTT; -.
DR   PDBsum; 3GTV; -.
DR   ProteinModelPortal; P08228; -.
DR   SMR; P08228; 2-154.
DR   DIP; DIP-48691N; -.
DR   STRING; P08228; -.
DR   PhosphoSite; P08228; -.
DR   SWISS-2DPAGE; P08228; -.
DR   DOSAC-COBS-2DPAGE; P08228; -.
DR   REPRODUCTION-2DPAGE; IPI00130589; -.
DR   REPRODUCTION-2DPAGE; P08228; -.
DR   UCD-2DPAGE; P08228; -.
DR   PRIDE; P08228; -.
DR   Ensembl; ENSMUST00000023707; ENSMUSP00000023707; ENSMUSG00000022982.
DR   GeneID; 20655; -.
DR   KEGG; mmu:20655; -.
DR   NMPDR; fig|10090.3.peg.1866; -.
DR   UCSC; uc007zvz.1; mouse.
DR   CTD; 20655; -.
DR   MGI; MGI:98351; Sod1.
DR   eggNOG; roNOG15892; -.
DR   GeneTree; ENSGT00530000063226; -.
DR   HOGENOM; HBG609879; -.
DR   HOVERGEN; HBG000062; -.
DR   InParanoid; P08228; -.
DR   OMA; KAVCVIN; -.
DR   OrthoDB; EOG45HRZM; -.
DR   PhylomeDB; P08228; -.
DR   BRENDA; 1.15.1.1; 244.
DR   NextBio; 299081; -.
DR   ArrayExpress; P08228; -.
DR   Bgee; P08228; -.
DR   CleanEx; MM_SOD1; -.
DR   Genevestigator; P08228; -.
DR   GermOnline; ENSMUSG00000047905; Mus musculus.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0032839; C:dendrite cytoplasm; ISS:UniProtKB.
DR   GO; GO:0031012; C:extracellular matrix; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0043234; C:protein complex; ISS:UniProtKB.
DR   GO; GO:0051087; F:chaperone binding; ISS:UniProtKB.
DR   GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR   GO; GO:0030346; F:protein phosphatase 2B binding; ISS:UniProtKB.
DR   GO; GO:0004784; F:superoxide dismutase activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0000187; P:activation of MAPK activity; IDA:MGI.
DR   GO; GO:0060088; P:auditory receptor cell stereocilium organization; IMP:MGI.
DR   GO; GO:0007569; P:cell aging; ISS:UniProtKB.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IMP:MGI.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptotic nuclear change; IDA:MGI.
DR   GO; GO:0006302; P:double-strand break repair; IMP:MGI.
DR   GO; GO:0007566; P:embryo implantation; IMP:MGI.
DR   GO; GO:0006749; P:glutathione metabolic process; IMP:MGI.
DR   GO; GO:0060047; P:heart contraction; IMP:MGI.
DR   GO; GO:0050665; P:hydrogen peroxide biosynthetic process; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0046716; P:muscle cell homeostasis; IMP:MGI.
DR   GO; GO:0002262; P:myeloid cell homeostasis; IGI:MGI.
DR   GO; GO:0045541; P:negative regulation of cholesterol biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0043524; P:negative regulation of neuron apoptosis; IMP:MGI.
DR   GO; GO:0060052; P:neurofilament cytoskeleton organization; IGI:MGI.
DR   GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0032287; P:peripheral nervous system myelin maintenance; IMP:MGI.
DR   GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR   GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:UniProtKB.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
DR   GO; GO:0060087; P:relaxation of vascular smooth muscle; IMP:MGI.
DR   GO; GO:0019430; P:removal of superoxide radicals; IMP:MGI.
DR   GO; GO:0048678; P:response to axon injury; IMP:MGI.
DR   GO; GO:0042493; P:response to drug; IMP:MGI.
DR   GO; GO:0045471; P:response to ethanol; IMP:MGI.
DR   GO; GO:0009408; P:response to heat; IMP:MGI.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IMP:MGI.
DR   GO; GO:0001895; P:retina homeostasis; IMP:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   GO; GO:0042554; P:superoxide anion generation; IDA:MGI.
DR   InterPro; IPR018152; SOD_Cu/Zn_BS.
DR   InterPro; IPR001424; SOD_Cu_Zn.
DR   Gene3D; G3DSA:2.60.40.200; SOD_Cu_Zn; 1.
DR   PANTHER; PTHR10003; SOD_Cu_Zn; 1.
DR   Pfam; PF00080; Sod_Cu; 1.
DR   PRINTS; PR00068; CUZNDISMTASE.
DR   SUPFAM; SSF49329; SOD_Cu_Zn; 1.
DR   PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR   PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Antioxidant; Copper; Cytoplasm;
KW   Direct protein sequencing; Disulfide bond; Metal-binding;
KW   Oxidoreductase; Phosphoprotein; Zinc.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    154       Superoxide dismutase [Cu-Zn].
FT                                /FTId=PRO_0000164062.
FT   METAL        47     47       Copper; catalytic (By similarity).
FT   METAL        49     49       Copper; catalytic (By similarity).
FT   METAL        64     64       Copper; catalytic (By similarity).
FT   METAL        64     64       Zinc; structural (By similarity).
FT   METAL        72     72       Zinc; structural (By similarity).
FT   METAL        81     81       Zinc; structural (By similarity).
FT   METAL        84     84       Zinc; structural (By similarity).
FT   METAL       121    121       Copper; catalytic (By similarity).
FT   MOD_RES      71     71       N6-acetyllysine.
FT   MOD_RES      99     99       Phosphoserine (By similarity).
FT   MOD_RES     123    123       N6-acetyllysine (By similarity).
FT   DISULFID     58    147       By similarity.
FT   CONFLICT    102    102       D -> H (in Ref. 2; AAA40121).
SQ   SEQUENCE   154 AA;  15943 MW;  CAE548C66043BAC4 CRC64;
     MAMKAVCVLK GDGPVQGTIH FEQKASGEPV VLSGQITGLT EGQHGFHVHQ YGDNTQGCTS
     AGPHFNPHSK KHGGPADEER HVGDLGNVTA GKDGVANVSI EDRVISLSGE HSIIGRTMVV
     HEKQDDLGKG GNEESTKTGN AGSRLACGVI GIAQ
//
ID   MDHM_MOUSE              Reviewed;         338 AA.
AC   P08249; Q0QF44; Q8CF79; Q8R1P0;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 3.
DT   08-MAR-2011, entry version 120.
DE   RecName: Full=Malate dehydrogenase, mitochondrial;
DE            EC=1.1.1.37;
DE   Flags: Precursor;
GN   Name=Mdh2; Synonyms=Mor1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=87271646; PubMed=3038184; DOI=10.1021/bi00383a017;
RA   Joh T., Takeshima H., Tsuzuki T., Shimada K., Tanase S., Morino Y.;
RT   "Cloning and sequence analysis of cDNAs encoding mammalian
RT   mitochondrial malate dehydrogenase.";
RL   Biochemistry 26:2515-2520(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=88245174; PubMed=3379635; DOI=10.1016/0022-2836(88)90328-2;
RA   Takeshima H., Joh T., Tsuzuki T., Shimada K., Matsukado Y.;
RT   "Structural organization of the mouse mitochondrial malate
RT   dehydrogenase gene.";
RL   J. Mol. Biol. 200:1-11(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, and C57BL/6J; TISSUE=Cerebellum, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 22-322.
RC   TISSUE=Liver;
RX   PubMed=16751257; DOI=10.1093/molbev/msl027;
RA   Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.;
RT   "Housekeeping genes for phylogenetic analysis of eutherian
RT   relationships.";
RL   Mol. Biol. Evol. 23:1493-1503(2006).
RN   [6]
RP   PROTEIN SEQUENCE OF 27-45; 53-74; 79-104; 166-185; 192-239; 242-257;
RP   282-296 AND 308-324, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B.,
RA   Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-157; LYS-239 AND LYS-314,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC   -!- ENZYME REGULATION: Enzyme activity is enhanced by acetylation (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Acetylation is enhanced by up to 67% after treatment either
CC       with trichostin A (TCA) or with nicotinamide (NAM) with the
CC       appearance of tri-and tetraacetylations. Glucose also increases
CC       acetylation by about 60% (By similarity). Acetylation of Lys-239
CC       and Lys-314 is observed in liver mitochondria from fasted mice but
CC       not from fed mice.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC24986.1; Type=Frameshift; Positions=39;
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DR   EMBL; M16229; AAA39509.1; -; mRNA.
DR   EMBL; X07295; CAA30274.1; -; Genomic_DNA.
DR   EMBL; X07296; CAA30274.1; JOINED; Genomic_DNA.
DR   EMBL; X07297; CAA30274.1; JOINED; Genomic_DNA.
DR   EMBL; X07298; CAA30274.1; JOINED; Genomic_DNA.
DR   EMBL; X07299; CAA30274.1; JOINED; Genomic_DNA.
DR   EMBL; X07300; CAA30274.1; JOINED; Genomic_DNA.
DR   EMBL; X07301; CAA30274.1; JOINED; Genomic_DNA.
DR   EMBL; AK002305; BAC24986.1; ALT_FRAME; mRNA.
DR   EMBL; AK167809; BAE39836.1; -; mRNA.
DR   EMBL; AK160553; BAE35869.1; -; mRNA.
DR   EMBL; AK135162; BAE22447.1; -; mRNA.
DR   EMBL; BC023482; AAH23482.1; -; mRNA.
DR   EMBL; DQ402950; ABD77283.1; -; mRNA.
DR   IPI; IPI00323592; -.
DR   PIR; S01350; DEMSMM.
DR   RefSeq; NP_032643.2; NM_008617.2.
DR   UniGene; Mm.297096; -.
DR   ProteinModelPortal; P08249; -.
DR   SMR; P08249; 25-337.
DR   STRING; P08249; -.
DR   PhosphoSite; P08249; -.
DR   SWISS-2DPAGE; P08249; -.
DR   REPRODUCTION-2DPAGE; P08249; -.
DR   UCD-2DPAGE; P08249; -.
DR   PRIDE; P08249; -.
DR   Ensembl; ENSMUST00000019323; ENSMUSP00000019323; ENSMUSG00000019179.
DR   GeneID; 17448; -.
DR   KEGG; mmu:17448; -.
DR   NMPDR; fig|10090.3.peg.12582; -.
DR   CTD; 17448; -.
DR   MGI; MGI:97050; Mdh2.
DR   eggNOG; roNOG11242; -.
DR   GeneTree; ENSGT00390000016686; -.
DR   HOGENOM; HBG566126; -.
DR   HOVERGEN; HBG001662; -.
DR   InParanoid; P08249; -.
DR   OMA; FVRSEET; -.
DR   OrthoDB; EOG4MKNGM; -.
DR   PhylomeDB; P08249; -.
DR   BRENDA; 1.1.1.37; 244.
DR   NextBio; 292084; -.
DR   ArrayExpress; P08249; -.
DR   Bgee; P08249; -.
DR   CleanEx; MM_MDH2; -.
DR   Genevestigator; P08249; -.
DR   GermOnline; ENSMUSG00000019179; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IDA:MGI.
DR   GO; GO:0006096; P:glycolysis; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR001252; Malate_DH_AS.
DR   InterPro; IPR010097; Malate_DH_type1.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.90.110.10; lact_mal_DH; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR11540:SF1; MDH_euk_g_bac; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF56327; Lactate_DH/Glyco_hydro_4_C; 1.
DR   TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Mitochondrion; NAD;
KW   Oxidoreductase; Phosphoprotein; Transit peptide;
KW   Tricarboxylic acid cycle.
FT   TRANSIT       1     24       Mitochondrion.
FT   CHAIN        25    338       Malate dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000018629.
FT   NP_BIND      31     37       NAD (By similarity).
FT   NP_BIND     140    142       NAD (By similarity).
FT   ACT_SITE    200    200       Proton acceptor (By similarity).
FT   BINDING      57     57       NAD (By similarity).
FT   BINDING     104    104       Substrate.
FT   BINDING     110    110       Substrate.
FT   BINDING     117    117       NAD (By similarity).
FT   BINDING     142    142       Substrate.
FT   BINDING     176    176       Substrate.
FT   BINDING     251    251       NAD (By similarity).
FT   MOD_RES      56     56       Phosphotyrosine (By similarity).
FT   MOD_RES     157    157       N6-acetyllysine.
FT   MOD_RES     165    165       N6-acetyllysine (By similarity).
FT   MOD_RES     185    185       N6-acetyllysine (By similarity).
FT   MOD_RES     239    239       N6-acetyllysine.
FT   MOD_RES     301    301       N6-acetyllysine (By similarity).
FT   MOD_RES     314    314       N6-acetyllysine.
FT   MOD_RES     329    329       N6-acetyllysine (By similarity).
FT   MOD_RES     335    335       N6-acetyllysine (By similarity).
FT   CONFLICT     76     76       N -> K (in Ref. 1; AAA39509).
FT   CONFLICT    269    269       K -> L (in Ref. 1; AAA39509 and 2;
FT                                CAA30274).
SQ   SEQUENCE   338 AA;  35611 MW;  99D13BB2099C19F1 CRC64;
     MLSALARPAG AALRRSFSTS AQNNAKVAVL GASGGIGQPL SLLLKNSPLV SRLTLYDIAH
     TPGVAADLSH IETRANVKGY LGPEQLPDCL KGCDVVVIPA GVPRKPGMTR DDLFNTNATI
     VATLTAACAQ HCPEAMVCII ANPVNSTIPI TAEVFKKHGV YNPNKIFGVT TLDIVRANTF
     VAELKGLDPA RVNVPVIGGH AGKTIIPLIS QCTPKVDFPQ DQLATLTGRI QEAGTEVVKA
     KAGAGSATLS MAYAGARFVF SLVDAMNGKE GVVECSFVQS KETECTYFST PLLLGKKGLE
     KNLGIGKITP FEEKMIAEAI PELKASIKKG EDFVKNMK
//
ID   KCC4_MOUSE              Reviewed;         469 AA.
AC   P08414; Q61381;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 2.
DT   08-MAR-2011, entry version 112.
DE   RecName: Full=Calcium/calmodulin-dependent protein kinase type IV;
DE            Short=CaMK IV;
DE            EC=2.7.11.17;
DE   AltName: Full=CaM kinase-GR;
GN   Name=Camk4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=91372388; PubMed=1893997; DOI=10.1016/0014-5793(91)80919-T;
RA   Jones D.A., Glod J., Wilson-Shaw D., Hahn W.E., Sikela J.M.;
RT   "cDNA sequence and differential expression of the mouse
RT   Ca2+/calmodulin-dependent protein kinase IV gene.";
RL   FEBS Lett. 289:105-109(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 240-469.
RX   MEDLINE=89122027; PubMed=2536634; DOI=10.1016/0888-7543(89)90309-1;
RA   Sikela J.M., Law M.L., Kao F.-T., Hartz J.A., Wei Q., Hahn W.E.;
RT   "Chromosomal localization of the human gene for brain Ca2+/calmodulin-
RT   dependent protein kinase type IV.";
RL   Genomics 4:21-27(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 315-469.
RC   TISSUE=Brain;
RX   MEDLINE=87204263; PubMed=3033675; DOI=10.1073/pnas.84.9.3038;
RA   Sikela J.M., Hahn W.E.;
RT   "Screening an expression library with a ligand probe: isolation and
RT   sequence of a cDNA corresponding to a brain calmodulin-binding
RT   protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:3038-3042(1987).
RN   [4]
RP   FUNCTION IN PHOSPHORYLATION OF CREB1.
RX   MEDLINE=94253131; PubMed=8195196;
RA   Enslen H., Sun P., Brickey D., Soderling S.H., Klamo E.,
RA   Soderling T.R.;
RT   "Characterization of Ca2+/calmodulin-dependent protein kinase IV. Role
RT   in transcriptional regulation.";
RL   J. Biol. Chem. 269:15520-15527(1994).
RN   [5]
RP   FUNCTION IN PHOSPHORYLATION OF CREBBP.
RX   MEDLINE=98397322; PubMed=9727976; DOI=10.1126/science.281.5382.1505;
RA   Chawla S., Hardingham G.E., Quinn D.R., Bading H.;
RT   "CBP: a signal-regulated transcriptional coactivator controlled by
RT   nuclear calcium and CaM kinase IV.";
RL   Science 281:1505-1509(1998).
RN   [6]
RP   FUNCTION IN PHOSPHORYLATION OF PRM2, TISSUE SPECIFICITY, AND
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=20392401; PubMed=10932193; DOI=10.1038/78153;
RA   Wu J.Y., Ribar T.J., Cummings D.E., Burton K.A., McKnight G.S.,
RA   Means A.R.;
RT   "Spermiogenesis and exchange of basic nuclear proteins are impaired in
RT   male germ cells lacking AC:.";
RL   Nat. Genet. 25:448-452(2000).
RN   [7]
RP   FUNCTION.
RX   MEDLINE=21456836; PubMed=11572782; DOI=10.1016/S0092-8674(01)00497-4;
RA   Kang H., Sun L.D., Atkins C.M., Soderling T.R., Wilson M.A.,
RA   Tonegawa S.;
RT   "An important role of neural activity-dependent CaMKIV signaling in
RT   the consolidation of long-term memory.";
RL   Cell 106:771-783(2001).
CC   -!- FUNCTION: Calcium/calmodulin-dependent protein kinase belonging to
CC       a proposed calcium-triggered signaling cascade. May be involved in
CC       transcriptional regulation. May be involved in regulation of
CC       microtubule dynamics. In vitro, phosphorylates CREB1, CREBBP,
CC       PRM2, MEF2A, MEF2D and STMN1/OP18. May be involved in
CC       spermatogenesis. May play a role in the consolidation/retention of
CC       hippocampus-dependent long-term memory.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Activated by Ca(2+)/calmodulin. Binding of
CC       calmodulin may releave intrasteric autoinhibition. Must be
CC       phosphorylated to be maximally active. Phosphorylated by CAMKK1 or
CC       CAMKK2. Autophosphorylation of the N-terminus is required for full
CC       activation. In part, activity is independent on Ca(2+)/calmodulin
CC       and autophosphorylation of Ser-332 allows to switch to a
CC       Ca(2+)/calmodulin-independent state. Probably inactivated by
CC       serine/threonine protein phosphatase 2A (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity). Interacts with serine/threonine
CC       protein phosphatase 2A catalytic subunit, PPP2CA or PPP2CB. The
CC       interaction with PP2CA or PP2CB is mutually exclusive with binding
CC       to Ca(2+)/calmodulin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Substantial
CC       localization in certain neuronal nuclei (By similarity). In
CC       spermatids associated with chromatin and nuclear matrix.
CC   -!- PTM: Autophosphorylated and phosphorylated by CAMKK1 and CAMKK2.
CC       Dephosphorylated by serine/threonine protein phosphatase 2A,
CC       probably on Thr-196 (By similarity).
CC   -!- MISCELLANEOUS: Camk4 deficient male mice are infertile with
CC       impairment of spermiogenesis in late elongating spermatids. The
CC       sequential deposition of sperm basic nuclear proteins on chromatin
CC       is disrupted, with a specific loss of protamine-2 and prolonged
CC       retention of Tnp2 in step-15 spermatids.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. CaMK subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M16206; AAA39933.1; -; mRNA.
DR   EMBL; M64266; AAA37364.1; -; mRNA.
DR   EMBL; J03057; AAA37366.1; -; mRNA.
DR   EMBL; X58995; CAA41741.1; -; mRNA.
DR   IPI; IPI00132526; -.
DR   PIR; S17656; S17656.
DR   UniGene; Mm.222329; -.
DR   ProteinModelPortal; P08414; -.
DR   SMR; P08414; 30-333.
DR   STRING; P08414; -.
DR   PhosphoSite; P08414; -.
DR   PRIDE; P08414; -.
DR   Ensembl; ENSMUST00000042868; ENSMUSP00000046539; ENSMUSG00000038128.
DR   UCSC; uc008ejq.1; mouse.
DR   MGI; MGI:88258; Camk4.
DR   eggNOG; roNOG13085; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108055; -.
DR   InParanoid; P08414; -.
DR   PhylomeDB; P08414; -.
DR   BRENDA; 2.7.11.17; 244.
DR   ArrayExpress; P08414; -.
DR   Bgee; P08414; -.
DR   CleanEx; MM_CAMK4; -.
DR   Genevestigator; P08414; -.
DR   GermOnline; ENSMUSG00000038128; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; TAS:MGI.
DR   GO; GO:0016563; F:transcription activator activity; IMP:MGI.
DR   GO; GO:0007270; P:nerve-nerve synaptic transmission; IMP:MGI.
DR   GO; GO:0006913; P:nucleocytoplasmic transport; IDA:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IDA:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Calcium; Calmodulin-binding; Cytoplasm;
KW   Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    469       Calcium/calmodulin-dependent protein
FT                                kinase type IV.
FT                                /FTId=PRO_0000086107.
FT   DOMAIN       42    296       Protein kinase.
FT   NP_BIND      48     56       ATP (By similarity).
FT   REGION      297    336       Autoinhibitory domain (By similarity).
FT   REGION      318    337       Calmodulin-binding (Potential).
FT   ACT_SITE    160    160       Proton acceptor (By similarity).
FT   BINDING      71     71       ATP (By similarity).
FT   MOD_RES      11     11       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES      12     12       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     186    186       N6-acetyllysine (By similarity).
FT   MOD_RES     196    196       Phosphothreonine (By similarity).
FT   MOD_RES     332    332       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     337    337       Phosphoserine (By similarity).
FT   MOD_RES     352    352       Phosphoserine (By similarity).
FT   CONFLICT    278    280       VLD -> CFGI (in Ref. 2; AAA37366).
FT   CONFLICT    302    302       N -> T (in Ref. 2; AAA37366).
SQ   SEQUENCE   469 AA;  52628 MW;  CE1F98670822F975 CRC64;
     MLKVTVPSCP SSPCSSVTAS TENLVPDYWI DGSNRDPLGD FFEVESELGR GATSIVYRCK
     QKGTQKPYAL KVLKKTVDKK IVRTEIGVLL RLSHPNIIKL KEIFETPTEI SLVLELVTGG
     ELFDRIVEKG YYSERDARDA VKQILEAVAY LHENGIVHRD LKPENLLYAT PAPDAPLKIA
     DFGLSKIVEH QVLMKTVCGT PGYCAPEILR GCAYGPEVDM WSVGIITYIL LCGFEPFYDE
     RGDQFMFRRI LNCEYYFISP WWDEVSLNAK DLVKKLIVLD PKKRLTTFQA LQHPWVTGKA
     ANFVHMDTAQ KKLQEFNARR KLKAAVKAVV ASSRLGSASS SHTSIQENHK ASSDPPSTQD
     AKDSTDLLGK KMQEEDQEED QVEAEASADE MRKLQSEEVE KDAGVKEEET SSMVPQDPED
     ELETDDPEMK RDSEEKLKSV EEEMDPMTEE EAPDAGLGVP QQDAIQPEY
//
ID   NFL_MOUSE               Reviewed;         543 AA.
AC   P08551; Q8K0Z0;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 5.
DT   08-MAR-2011, entry version 112.
DE   RecName: Full=Neurofilament light polypeptide;
DE            Short=NF-L;
DE   AltName: Full=68 kDa neurofilament protein;
DE   AltName: Full=Neurofilament triplet L protein;
GN   Name=Nefl; Synonyms=Nf68, Nfl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=87158637; PubMed=3103856;
RA   Julien J.-P., Meyer D., Flavell D., Hurst J., Grosveld F.;
RT   "Cloning and developmental expression of the murine neurofilament gene
RT   family.";
RL   Brain Res. 387:243-250(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Brain;
RX   MEDLINE=87064433; PubMed=3785173;
RA   Lewis S.A., Cowan N.J.;
RT   "Anomalous placement of introns in a member of the intermediate
RT   filament multigene family: an evolutionary conundrum.";
RL   Mol. Cell. Biol. 6:1529-1534(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Cerebellum;
RA   Jensen K.H., Brown A.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RX   MEDLINE=91060592; PubMed=2246261;
RA   Nakahira K., Ikenaka K., Wada K., Tamura T.A., Furuichi T.,
RA   Mikoshiba K.;
RT   "Structure of the 68-kDa neurofilament gene and regulation of its
RT   expression.";
RL   J. Biol. Chem. 265:19786-19791(1990).
RN   [6]
RP   PROTEIN SEQUENCE OF 38-54; 117-126 AND 381-391, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [7]
RP   PROTEIN SEQUENCE OF 52-57, AND PHOSPHORYLATION AT SER-56.
RX   MEDLINE=92011653; PubMed=1717455;
RA   Sihag R.K., Nixon R.A.;
RT   "Identification of Ser-55 as a major protein kinase A phosphorylation
RT   site on the 70-kDa subunit of neurofilaments. Early turnover during
RT   axonal transport.";
RL   J. Biol. Chem. 266:18861-18867(1991).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 242-543.
RC   TISSUE=Brain;
RX   MEDLINE=85131334; PubMed=3919033; DOI=10.1083/jcb.100.3.843;
RA   Lewis S.A., Cowan N.J.;
RT   "Genetics, evolution, and expression of the 68,000-mol-wt
RT   neurofilament protein: isolation of a cloned cDNA probe.";
RL   J. Cell Biol. 100:843-850(1985).
RN   [9]
RP   INTERACTION WITH RGNEF.
RX   PubMed=16236762; DOI=10.1093/hmg/ddi392;
RA   Lin H., Zhai J., Schlaepfer W.W.;
RT   "RNA-binding protein is involved in aggregation of light neurofilament
RT   protein and is implicated in the pathogenesis of motor neuron
RT   degeneration.";
RL   Hum. Mol. Genet. 14:3643-3659(2005).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473 AND SER-532, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [11]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452088; DOI=10.1074/mcp.T500040-MCP200;
RA   Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G.,
RA   Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F.,
RA   Maltby D.A., Schoepfer R., Burlingame A.L.;
RT   "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT   preparations using lectin weak affinity chromatography and mass
RT   spectrometry.";
RL   Mol. Cell. Proteomics 5:923-934(2006).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-43; TYR-425 AND TYR-433,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-532, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Neurofilaments usually contain three intermediate
CC       filament proteins: L, M, and H which are involved in the
CC       maintenance of neuronal caliber.
CC   -!- SUBUNIT: Interacts with RGNEF.
CC   -!- DOMAIN: The extra mass and high charge density that distinguish
CC       the neurofilament proteins from all other intermediate filament
CC       proteins are due to the tailpiece extensions. This region may form
CC       a charged scaffolding structure suitable for interaction with
CC       other neuronal components or ions.
CC   -!- PTM: O-glycosylated.
CC   -!- PTM: Phosphorylated in the Head and Rod regions by the PKC kinase
CC       PKN1, leading to inhibit polymerization (By similarity).
CC   -!- MISCELLANEOUS: NF-L is the most abundant of the three
CC       neurofilament proteins and, as the other nonepithelial
CC       intermediate filament proteins, it can form homopolymeric 10-nm
CC       filaments.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; M20480; AAA39814.1; -; mRNA.
DR   EMBL; M13016; AAA39810.1; -; Genomic_DNA.
DR   EMBL; DQ201635; ABA46748.1; -; mRNA.
DR   EMBL; BC029203; AAH29203.1; -; mRNA.
DR   EMBL; M55423; AAA39812.1; -; Genomic_DNA.
DR   EMBL; X02165; CAB51616.1; -; mRNA.
DR   IPI; IPI00554928; -.
DR   PIR; A25227; QFMSL.
DR   RefSeq; NP_035040.1; NM_010910.1.
DR   UniGene; Mm.1956; -.
DR   ProteinModelPortal; P08551; -.
DR   SMR; P08551; 88-125, 130-237, 253-323, 327-396.
DR   DIP; DIP-31944N; -.
DR   STRING; P08551; -.
DR   PhosphoSite; P08551; -.
DR   UCD-2DPAGE; P08551; -.
DR   PRIDE; P08551; -.
DR   Ensembl; ENSMUST00000022639; ENSMUSP00000022639; ENSMUSG00000022055.
DR   GeneID; 18039; -.
DR   KEGG; mmu:18039; -.
DR   UCSC; uc007uln.1; mouse.
DR   CTD; 18039; -.
DR   MGI; MGI:97313; Nefl.
DR   eggNOG; maNOG09227; -.
DR   HOGENOM; HBG715391; -.
DR   HOVERGEN; HBG013015; -.
DR   InParanoid; P08551; -.
DR   OMA; EMDVSTK; -.
DR   OrthoDB; EOG42Z4QC; -.
DR   PhylomeDB; P08551; -.
DR   NextBio; 293145; -.
DR   ArrayExpress; P08551; -.
DR   Bgee; P08551; -.
DR   CleanEx; MM_NEFL; -.
DR   Genevestigator; P08551; -.
DR   GermOnline; ENSMUSG00000022055; Mus musculus.
DR   GO; GO:0005883; C:neurofilament; IDA:MGI.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0045110; P:intermediate filament bundle assembly; IGI:MGI.
DR   GO; GO:0040011; P:locomotion; IMP:MGI.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptosis; IMP:MGI.
DR   GO; GO:0060052; P:neurofilament cytoskeleton organization; IMP:MGI.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR   GO; GO:0014012; P:peripheral nervous system axon regeneration; IMP:MGI.
DR   GO; GO:0050772; P:positive regulation of axonogenesis; IMP:MGI.
DR   GO; GO:0031133; P:regulation of axon diameter; IMP:MGI.
DR   InterPro; IPR016044; F.
DR   InterPro; IPR001664; IF.
DR   InterPro; IPR006821; Intermed_filament_DNA-bd.
DR   InterPro; IPR018039; Intermediate_filament_CS.
DR   PANTHER; PTHR23239; IF; 1.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF04732; Filament_head; 1.
DR   PROSITE; PS00226; IF; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Direct protein sequencing; Glycoprotein;
KW   Intermediate filament; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    543       Neurofilament light polypeptide.
FT                                /FTId=PRO_0000063788.
FT   REGION        2     93       Head.
FT   REGION       94    397       Rod.
FT   REGION       94    125       Coil 1A.
FT   REGION      126    138       Linker 1.
FT   REGION      139    234       Coil 1B.
FT   REGION      235    253       Linker 12.
FT   REGION      254    272       Coil 2A.
FT   REGION      273    281       Linker 2.
FT   REGION      282    397       Coil 2B.
FT   REGION      382    392       Epitope; recognized by IF-specific
FT                                monoclonal antibody.
FT   REGION      398    543       Tail.
FT   REGION      398    444       Tail, subdomain A.
FT   REGION      445    543       Tail, subdomain B (acidic).
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES      43     43       Phosphotyrosine.
FT   MOD_RES      56     56       Phosphoserine.
FT   MOD_RES      67     67       Phosphoserine (By similarity).
FT   MOD_RES     425    425       Phosphotyrosine.
FT   MOD_RES     433    433       Phosphotyrosine.
FT   MOD_RES     473    473       Phosphoserine.
FT   MOD_RES     532    532       Phosphoserine.
FT   CARBOHYD     21     21       O-linked (GlcNAc) (By similarity).
FT   CARBOHYD     27     27       O-linked (GlcNAc) (By similarity).
FT   CONFLICT      6      6       Y -> S (in Ref. 2; AAA39810).
FT   CONFLICT      9      9       Y -> I (in Ref. 2; AAA39810).
FT   CONFLICT     65     65       M -> K (in Ref. 2; AAA39810).
FT   CONFLICT     73     73       L -> V (in Ref. 2; AAA39810).
FT   CONFLICT     99     99       D -> H (in Ref. 2; AAA39810).
FT   CONFLICT    195    195       A -> R (in Ref. 1; AAA39814).
FT   CONFLICT    203    203       Missing (in Ref. 1; AAA39814).
FT   CONFLICT    240    240       Y -> I (in Ref. 2; AAA39810).
SQ   SEQUENCE   543 AA;  61508 MW;  BC40F8A8A536CFF5 CRC64;
     MSSFGYDPYF STSYKRRYVE TPRVHISSVR SGYSTARSAY SSYSAPVSSS LSVRRSYSSS
     SGSLMPSLEN LDLSQVAAIS NDLKSIRTQE KAQLQDLNDR FASFIERVHE LEQQNKVLEA
     ELLVLRQKHS EPSRFRALYE QEIRDLRLAA EDATNEKQAL QGEREGLEET LRNLQARYEE
     EVLSREDAEG RLMEARKGAD EAALARAELE KRIDSLMDEI AFLKKVHEEE IAELQAQIQY
     AQISVEMDVS SKPDLSAALK DIRAQYEKLA AKNMQNAEEW FKSRFTVLTE SAAKNTDAVR
     AAKDEVSESR RLLKAKTLEI EACRGMNEAL EKQLQELEDK QNADISAMQD TINKLENELR
     STKSEMARYL KEYQDLLNVK MALDIEIAAY RKLLEGEETR LSFTSVGSIT SGYSQSSQVF
     GRSAYSGLQS SSYLMSARSF PAYYTSHVQE EQTEVEETIE ATKAEEAKDE PPSEGEAEEE
     EKEKEEGEEE EGAEEEEAAK DESEDTKEEE EGGEGEEEDT KESEEEEKKE ESAGEEQVAK
     KKD
//
ID   NFM_MOUSE               Reviewed;         848 AA.
AC   P08553; A2VCT5; Q0VDM8; Q3HRJ6; Q3TNS4; Q3TPK2; Q61961; Q8BQ20;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 4.
DT   08-MAR-2011, entry version 113.
DE   RecName: Full=Neurofilament medium polypeptide;
DE            Short=NF-M;
DE   AltName: Full=160 kDa neurofilament protein;
DE   AltName: Full=Neurofilament 3;
DE   AltName: Full=Neurofilament triplet M protein;
GN   Name=Nefm; Synonyms=Nef3, Nfm;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=87246694; PubMed=3036526;
RX   DOI=10.1111/j.1432-1033.1987.tb13485.x;
RA   Levy E., Liem R.K.H., D'Eustachio P., Cowan N.J.;
RT   "Structure and evolutionary origin of the gene encoding mouse NF-M,
RT   the middle-molecular-mass neurofilament protein.";
RL   Eur. J. Biochem. 166:71-77(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Cerebellum;
RA   Jensen K.H., Brown A.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-848.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 167-182; 222-233 AND 410-425, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 322-540.
RX   MEDLINE=87158637; PubMed=3103856;
RA   Julien J.-P., Meyer D., Flavell D., Hurst J., Grosveld F.;
RT   "Cloning and developmental expression of the murine neurofilament gene
RT   family.";
RL   Brain Res. 387:243-250(1986).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502 AND SER-506, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605; SER-610; THR-642;
RP   SER-669 AND SER-715, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-47 AND THR-430, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452088; DOI=10.1074/mcp.T500040-MCP200;
RA   Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G.,
RA   Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F.,
RA   Maltby D.A., Schoepfer R., Burlingame A.L.;
RT   "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT   preparations using lectin weak affinity chromatography and mass
RT   spectrometry.";
RL   Mol. Cell. Proteomics 5:923-934(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-318, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-769, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502; SER-610 AND
RP   SER-645, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Neurofilaments usually contain three intermediate
CC       filament proteins: L, M, and H which are involved in the
CC       maintenance of neuronal caliber.
CC   -!- PTM: There are a number of repeats of the tripeptide K-S-P, NFM is
CC       phosphorylated on a number of the serines in this motif. It is
CC       thought that phosphorylation of NFM results in the formation of
CC       interfilament cross bridges that are important in the maintenance
CC       of axonal caliber.
CC   -!- PTM: Phosphorylation seems to play a major role in the functioning
CC       of the larger neurofilament polypeptides (NF-M and NF-H), the
CC       levels of phosphorylation being altered developmentally and
CC       coincident with a change in the neurofilament function.
CC   -!- PTM: Phosphorylated in the Head and Rod regions by the PKC kinase
CC       PKN1, leading to inhibit polymerization (By similarity).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC   -----------------------------------------------------------------------
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DR   EMBL; X05640; CAA29127.1; -; Genomic_DNA.
DR   EMBL; DQ201636; ABA46749.1; -; mRNA.
DR   EMBL; AK051696; BAC34724.1; -; mRNA.
DR   EMBL; AK164318; BAE37734.1; -; mRNA.
DR   EMBL; AK165041; BAE38014.1; -; mRNA.
DR   EMBL; BC119602; AAI19603.1; -; mRNA.
DR   EMBL; BC128564; AAI28565.1; -; mRNA.
DR   EMBL; M20481; AAA39815.1; -; mRNA.
DR   IPI; IPI00323800; -.
DR   PIR; B43772; B43772.
DR   PIR; S00030; S00030.
DR   RefSeq; NP_032717.2; NM_008691.2.
DR   UniGene; Mm.390700; -.
DR   ProteinModelPortal; P08553; -.
DR   SMR; P08553; 97-134, 138-246, 263-333, 337-405.
DR   STRING; P08553; -.
DR   PhosphoSite; P08553; -.
DR   UCD-2DPAGE; P08553; -.
DR   PRIDE; P08553; -.
DR   Ensembl; ENSMUST00000022638; ENSMUSP00000022638; ENSMUSG00000022054.
DR   GeneID; 18040; -.
DR   KEGG; mmu:18040; -.
DR   CTD; 18040; -.
DR   MGI; MGI:97314; Nefm.
DR   eggNOG; roNOG11778; -.
DR   GeneTree; ENSGT00560000076592; -.
DR   HOVERGEN; HBG013015; -.
DR   InParanoid; P08553; -.
DR   OrthoDB; EOG4VMFFD; -.
DR   NextBio; 293149; -.
DR   ArrayExpress; P08553; -.
DR   Bgee; P08553; -.
DR   CleanEx; MM_NEFM; -.
DR   Genevestigator; P08553; -.
DR   GermOnline; ENSMUSG00000022054; Mus musculus.
DR   GO; GO:0005883; C:neurofilament; IDA:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0008088; P:axon cargo transport; IMP:MGI.
DR   GO; GO:0045110; P:intermediate filament bundle assembly; IGI:MGI.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IGI:MGI.
DR   GO; GO:0060052; P:neurofilament cytoskeleton organization; IMP:MGI.
DR   GO; GO:0031133; P:regulation of axon diameter; IMP:MGI.
DR   InterPro; IPR016044; F.
DR   InterPro; IPR001664; IF.
DR   InterPro; IPR006821; Intermed_filament_DNA-bd.
DR   InterPro; IPR018039; Intermediate_filament_CS.
DR   InterPro; IPR002957; Keratin_I.
DR   PANTHER; PTHR23239; IF; 1.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF04732; Filament_head; 1.
DR   PRINTS; PR01248; TYPE1KERATIN.
DR   PROSITE; PS00226; IF; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Direct protein sequencing; Glycoprotein;
KW   Intermediate filament; Phosphoprotein.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    848       Neurofilament medium polypeptide.
FT                                /FTId=PRO_0000063795.
FT   REGION        2    102       Head.
FT   REGION      103    410       Rod.
FT   REGION      103    134       Coil 1A.
FT   REGION      135    147       Linker 1.
FT   REGION      148    246       Coil 1B.
FT   REGION      247    263       Linker 12.
FT   REGION      264    285       Coil 2A.
FT   REGION      286    289       Linker 2.
FT   REGION      290    410       Coil 2B.
FT   REGION      411    848       Tail.
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES     318    318       Phosphotyrosine.
FT   MOD_RES     502    502       Phosphoserine.
FT   MOD_RES     506    506       Phosphoserine.
FT   MOD_RES     537    537       Phosphoserine (By similarity).
FT   MOD_RES     545    545       Phosphoserine (By similarity).
FT   MOD_RES     551    551       Phosphoserine (By similarity).
FT   MOD_RES     605    605       Phosphoserine.
FT   MOD_RES     610    610       Phosphoserine.
FT   MOD_RES     642    642       Phosphothreonine.
FT   MOD_RES     645    645       Phosphoserine.
FT   MOD_RES     669    669       Phosphoserine.
FT   MOD_RES     715    715       Phosphoserine.
FT   MOD_RES     720    720       Phosphoserine (By similarity).
FT   MOD_RES     769    769       Phosphoserine.
FT   CARBOHYD     47     47       O-linked (GlcNAc) (Probable).
FT   CARBOHYD    430    430       O-linked (GlcNAc) (Probable).
FT   CONFLICT     17     17       V -> VP (in Ref. 1; CAA29127).
FT   CONFLICT     53     53       K -> T (in Ref. 1; CAA29127).
FT   CONFLICT     57     57       L -> V (in Ref. 1; CAA29127).
FT   CONFLICT    234    234       S -> R (in Ref. 1; CAA29127).
FT   CONFLICT    432    432       S -> F (in Ref. 6; AAA39815).
FT   CONFLICT    539    540       QA -> RR (in Ref. 6; AAA39815).
FT   CONFLICT    628    628       Q -> H (in Ref. 2; ABA46749 and 3;
FT                                BAC34724/BAE37734).
FT   CONFLICT    696    696       E -> K (in Ref. 3; BAC34724).
FT   CONFLICT    699    699       P -> L (in Ref. 2; ABA46749 and 3;
FT                                BAC34724).
SQ   SEQUENCE   848 AA;  95916 MW;  0783F50558A7D4C3 CRC64;
     MSYTLDSLGN PSAYRRVTET RSSFSRVSGS PSSGFRSQSW SRGSPSTVSS SYKRSALAPR
     LAYSSAMLSS AESSLDFSQS SSLLNGGSGG DYKLSRSNEK EQLQGLNDRF AGYIEKVHYL
     EQQNKEIEAE IQALRQKQAS HAQLGDAYDQ EIRELRATLE MVNHEKAQVQ LDSDHLEEDI
     HRLKERFEEE ARLRDDTEAA IRALRKDIEE SSMVKVELDK KVQSLQDEVA FLRSNHEEEV
     ADLLAQIQAS HITVERKDYL KTDISTALKE IRSQLECHSD QNMHQAEEWF KCRYAKLTEA
     AEQNKEAIRS AKEEIAEYRR QLQSKSIELE SVRGTKESLE RQLSDIEERH NHDLSSYQDT
     IQQLENELRG TKWEMARHLR EYQDLLNVKM ALDIEIAAYR KLLEGEETRF STFSGSITGP
     LYTHRQPSVT ISSKIQKTKV EAPKLKVQHK FVEEIIEETK VEDEKSEMEE TLTAIAEELA
     ASAKEEKEEA EEKEEEPEAE KSPVKSPEAK EEEEEGEKEE EEEGQEEEEE EDEGVKSDQA
     EEGGSEKEGS SEKDEGEQEE EEGETEAEGE GEEAEAKEEK KIEGKVEEVA VKEEIKVEKP
     EKAKSPMPKS PVEEVKPKPE AKAGKGEQKE EEKVEEEKKE VTKESPKEEK VEKKEEKPKD
     VADKKKAESP VKEKAVEEVI TISKSVKVSL EKDTKEEKPQ PQEKVKEKAE EEGGSEEEGS
     DRSPQESKKE DIAINGEVEG KEEEEQETQE KGSGREEEKG VVTNGLDVSP AEEKKGEDSS
     DDKVVVTKKV EKITSEGGDG ATKYITKSVT VTQKVEEHEE TFEEKLVSTK KVEKVTSHAI
     VKEVTQGD
//
ID   RPB1_MOUSE              Reviewed;        1970 AA.
AC   P08775; Q5F298;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 3.
DT   08-MAR-2011, entry version 116.
DE   RecName: Full=DNA-directed RNA polymerase II subunit RPB1;
DE            Short=RNA polymerase II subunit B1;
DE            EC=2.7.7.6;
DE   AltName: Full=DNA-directed RNA polymerase II subunit A;
DE   AltName: Full=DNA-directed RNA polymerase III largest subunit;
GN   Name=Polr2a; Synonyms=Rpii215, Rpo2-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=87280135; PubMed=3038894;
RA   Ahearn J.M. Jr., Bartolomei M.S., West M.L., Cisek L.J., Corden J.L.;
RT   "Cloning and sequence analysis of the mouse genomic locus encoding the
RT   largest subunit of RNA polymerase II.";
RL   J. Biol. Chem. 262:10695-10705(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1587-1970.
RX   MEDLINE=86068017; PubMed=2999785; DOI=10.1073/pnas.82.23.7934;
RA   Corden J.L., Cadena D.L., Ahearn J.M. Jr., Dahmus M.E.;
RT   "A unique structure at the carboxyl terminus of the largest subunit of
RT   eukaryotic RNA polymerase II.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:7934-7938(1985).
RN   [4]
RP   SEQUENCE REVISION, AND PRESENCE OF AN ADDITIONAL EXON.
RX   MEDLINE=92178992; PubMed=1542581; DOI=10.1093/nar/20.4.910;
RA   Wintzerith M., Acker J., Vicaire S., Vigneron M., Kedinger C.;
RT   "Complete sequence of the human RNA polymerase II largest subunit.";
RL   Nucleic Acids Res. 20:910-910(1992).
RN   [5]
RP   INTERACTION WITH SCAF8.
RX   MEDLINE=96293459; PubMed=8692929; DOI=10.1073/pnas.93.14.6975;
RA   Yuryev A., Patturajan M., Litingtung Y., Joshi R.V., Gentile C.,
RA   Gebara M., Corden J.L.;
RT   "The C-terminal domain of the largest subunit of RNA polymerase II
RT   interacts with a novel set of serine/arginine-rich proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:6975-6980(1996).
RN   [6]
RP   INTERACTION WITH MYO1C.
RX   MEDLINE=20485639; PubMed=11030652; DOI=10.1126/science.290.5490.337;
RA   Pestic-Dragovich L., Stojiljkovic L., Philimonenko A.A., Nowak G.,
RA   Ke Y., Settlage R.E., Shabanowitz J., Hunt D.F., Hozak P.,
RA   de Lanerolle P.;
RT   "A myosin I isoform in the nucleus.";
RL   Science 290:337-341(2000).
RN   [7]
RP   UBIQUITINATION AT LYS-1859; LYS-1866; LYS-1873; LYS-1887; LYS-1908 AND
RP   LYS-1922, MASS SPECTROMETRY, INTERACTION WITH WWP2, AND MUTAGENESIS OF
RP   LYS-1859; LYS-1866; LYS-1873; LYS-1887; LYS-1908 AND LYS-1922.
RX   PubMed=17526739; DOI=10.1128/MCB.01667-06;
RA   Li H., Zhang Z., Wang B., Zhang J., Zhao Y., Jin Y.;
RT   "Wwp2-mediated ubiquitination of the RNA polymerase II large subunit
RT   in mouse embryonic pluripotent stem cells.";
RL   Mol. Cell. Biol. 27:5296-5305(2007).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC       of DNA into RNA using the four ribonucleoside triphosphates as
CC       substrates. Largest and catalytic component of RNA polymerase II
CC       which synthesizes mRNA precursors and many functional non-coding
CC       RNAs. Forms the polymerase active center together with the second
CC       largest subunit. Pol II is the central component of the basal RNA
CC       polymerase II transcription machinery. It is composed of mobile
CC       elements that move relative to each other. RPB1 is part of the
CC       core element with the central large cleft, the clamp element that
CC       moves to open and close the cleft and the jaws that are thought to
CC       grab the incoming DNA template. At the start of transcription, a
CC       single stranded DNA template strand of the promoter is positioned
CC       within the central active site cleft of Pol II. A bridging helix
CC       emanates from RPB1 and crosses the cleft near the catalytic site
CC       and is thought to promote translocation of Pol II by acting as a
CC       ratchet that moves the RNA-DNA hybrid through the active site by
CC       switching from straight to bent conformations at each step of
CC       nucleotide addition. During transcription elongation, Pol II moves
CC       on the template as the transcript elongates. Elongation is
CC       influenced by the phosphorylation status of the C-terminal domain
CC       (CTD) of Pol II largest subunit (RPB1), which serves as a platform
CC       for assembly of factors that regulate transcription initiation,
CC       elongation, termination and mRNA processing (By similarity).
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1).
CC   -!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex
CC       consisting of 12 subunits. The phosphorylated C-terminal domain
CC       interacts with FNBP3 and SYNCRIP. Interacts with SAFB/SAFB1.
CC       Interacts with CCNL1, CCNL2 and SFRS19. Component of a complex
CC       which is at least composed of HTATSF1/Tat-SF1, the P-TEFb complex
CC       components CDK9 and CCNT1, RNA polymerase II, SUPT5H, and
CC       NCL/nucleolin. Hyperphosphorylated form on tandem 7 residues
CC       repeats specifically interacts with SETD2 (By similarity).
CC       Interacts with PAF1. Interacts (via C-terminus) with FTSJD2 and
CC       CTDSP1 (By similarity). Interacts with MYO1C. Interacts (via C-
CC       terminus) with SCAF8. Interacts via the phosphorylated C-terminal
CC       domain with WDR82 and with SETD1A and SETD1B only in the presence
CC       of WDR82 (By similarity). Interacts with ATF7IP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- PTM: The tandem 7 residues repeats in the C-terminal domain (CTD)
CC       can be highly phosphorylated. The phosphorylation activates Pol
CC       II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5'
CC       of the heptapepdtide repeat. The phosphorylation state is believed
CC       to result from the balanced action of site-specific CTD kinases
CC       and phosphataes, and a "CTD code" that specifies the position of
CC       Pol II within the transcription cycle has been proposed (By
CC       similarity).
CC   -!- PTM: Dephosphorylated by the protein phosphatase CTDSP1 (By
CC       similarity).
CC   -!- PTM: Ubiquitinated by WWP2 leading to proteasomal degradation.
CC   -!- MISCELLANEOUS: The binding of ribonucleoside triphosphate to the
CC       RNA polymerase II transcribing complex probably involves a two-
CC       step mechanism. The initial binding seems to occur at the entry
CC       (E) site and involves a magnesium ion temporarily coordinated by
CC       three conserved aspartate residues of the two largest RNA Pol II
CC       subunits. The ribonucleoside triphosphate is transferred by a
CC       rotation to the nucelotide addition (A) site for pairing with the
CC       template DNA. The catalytic A site involves three conserved
CC       aspartate residues of the RNA Pol II largest subunit which
CC       permanently coordinate a second magnesium ion.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC   -----------------------------------------------------------------------
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DR   EMBL; M12130; AAA40071.1; -; Genomic_DNA.
DR   EMBL; M14101; AAA40071.1; JOINED; Genomic_DNA.
DR   EMBL; AL603707; CAI51953.1; -; Genomic_DNA.
DR   IPI; IPI00136207; -.
DR   PIR; A28490; A28490.
DR   RefSeq; NP_033115.1; NM_009089.2.
DR   UniGene; Mm.16533; -.
DR   ProteinModelPortal; P08775; -.
DR   SMR; P08775; 16-904, 1054-1477.
DR   DisProt; DP00181; -.
DR   DIP; DIP-46369N; -.
DR   STRING; P08775; -.
DR   PhosphoSite; P08775; -.
DR   PRIDE; P08775; -.
DR   Ensembl; ENSMUST00000058470; ENSMUSP00000050771; ENSMUSG00000005198.
DR   GeneID; 20020; -.
DR   KEGG; mmu:20020; -.
DR   UCSC; uc007jrk.1; mouse.
DR   CTD; 20020; -.
DR   MGI; MGI:98086; Polr2a.
DR   HOGENOM; HBG499785; -.
DR   HOVERGEN; HBG004339; -.
DR   InParanoid; P08775; -.
DR   OMA; IVQDTLC; -.
DR   OrthoDB; EOG4JWVCM; -.
DR   PhylomeDB; P08775; -.
DR   BRENDA; 2.7.7.6; 244.
DR   ArrayExpress; P08775; -.
DR   Bgee; P08775; -.
DR   CleanEx; MM_POLR2A; -.
DR   Genevestigator; P08775; -.
DR   GermOnline; ENSMUSG00000005198; Mus musculus.
DR   GO; GO:0005665; C:DNA-directed RNA polymerase II, core complex; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR   InterPro; IPR000722; RNA_pol_asu.
DR   InterPro; IPR000684; RNA_pol_II_repeat_euk.
DR   InterPro; IPR006592; RNA_pol_N.
DR   InterPro; IPR007080; RNA_pol_Rpb1_1.
DR   InterPro; IPR007066; RNA_pol_Rpb1_3.
DR   InterPro; IPR007083; RNA_pol_Rpb1_4.
DR   InterPro; IPR007081; RNA_pol_Rpb1_5.
DR   InterPro; IPR007075; RNA_pol_Rpb1_6.
DR   InterPro; IPR007073; RNA_pol_Rpb1_7.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR   Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR   Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR   Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR   Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR   Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR   Pfam; PF05001; RNA_pol_Rpb1_R; 25.
DR   SMART; SM00663; RPOLA_N; 1.
DR   PROSITE; PS00115; RNA_POL_II_REPEAT; 42.
PE   1: Evidence at protein level;
KW   Acetylation; DNA-binding; DNA-directed RNA polymerase; Magnesium;
KW   Metal-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW   Repeat; Transcription; Transferase; Ubl conjugation; Zinc.
FT   CHAIN         1   1970       DNA-directed RNA polymerase II subunit
FT                                RPB1.
FT                                /FTId=PRO_0000073941.
FT   REPEAT     1593   1599       1.
FT   REPEAT     1600   1606       2; approximate.
FT   REPEAT     1608   1614       3.
FT   REPEAT     1615   1621       4.
FT   REPEAT     1622   1628       5.
FT   REPEAT     1629   1635       6.
FT   REPEAT     1636   1642       7.
FT   REPEAT     1643   1649       8.
FT   REPEAT     1650   1656       9.
FT   REPEAT     1657   1663       10.
FT   REPEAT     1664   1670       11.
FT   REPEAT     1671   1677       12.
FT   REPEAT     1678   1684       13.
FT   REPEAT     1685   1691       14.
FT   REPEAT     1692   1698       15.
FT   REPEAT     1699   1705       16.
FT   REPEAT     1706   1712       17.
FT   REPEAT     1713   1719       18.
FT   REPEAT     1720   1726       19.
FT   REPEAT     1727   1733       20.
FT   REPEAT     1734   1740       21.
FT   REPEAT     1741   1747       22.
FT   REPEAT     1748   1754       23.
FT   REPEAT     1755   1761       24.
FT   REPEAT     1762   1768       25.
FT   REPEAT     1769   1775       26.
FT   REPEAT     1776   1782       27.
FT   REPEAT     1783   1789       28.
FT   REPEAT     1790   1796       29.
FT   REPEAT     1797   1803       30.
FT   REPEAT     1804   1810       31.
FT   REPEAT     1811   1817       32.
FT   REPEAT     1818   1824       33.
FT   REPEAT     1825   1831       34.
FT   REPEAT     1832   1838       35.
FT   REPEAT     1839   1845       36.
FT   REPEAT     1846   1852       37.
FT   REPEAT     1853   1859       38.
FT   REPEAT     1860   1866       39.
FT   REPEAT     1867   1873       40.
FT   REPEAT     1874   1880       41.
FT   REPEAT     1881   1887       42.
FT   REPEAT     1888   1894       43.
FT   REPEAT     1895   1901       44.
FT   REPEAT     1902   1908       45.
FT   REPEAT     1909   1915       46.
FT   REPEAT     1916   1922       47.
FT   REPEAT     1923   1929       48.
FT   REPEAT     1930   1936       49.
FT   REPEAT     1940   1946       50.
FT   REPEAT     1947   1953       51; approximate.
FT   REPEAT     1954   1960       52; approximate.
FT   REGION      833    845       Bridging helix.
FT   REGION     1593   1960       52 X 7 AA approximate tandem repeats of
FT                                Y-[ST]-P-[STQ]-[ST]-P-[SRNTEVKGN].
FT   METAL        71     71       Zinc 1 (By similarity).
FT   METAL        74     74       Zinc 1 (By similarity).
FT   METAL        81     81       Zinc 1 (By similarity).
FT   METAL        84     84       Zinc 1 (By similarity).
FT   METAL       111    111       Zinc 2 (By similarity).
FT   METAL       114    114       Zinc 2 (By similarity).
FT   METAL       154    154       Zinc 2 (By similarity).
FT   METAL       184    184       Zinc 2 (By similarity).
FT   METAL       495    495       Magnesium 1; catalytic (By similarity).
FT   METAL       495    495       Magnesium 2; shared with RPB2 (By
FT                                similarity).
FT   METAL       497    497       Magnesium 1; catalytic (By similarity).
FT   METAL       497    497       Magnesium 2; shared with RPB2 (By
FT                                similarity).
FT   METAL       499    499       Magnesium 1; catalytic (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     145    145       Phosphotyrosine (By similarity).
FT   MOD_RES     772    772       Phosphoserine (By similarity).
FT   MOD_RES     777    777       Phosphoserine (By similarity).
FT   MOD_RES    1815   1815       Phosphoserine (By similarity).
FT   MOD_RES    1839   1839       Phosphotyrosine (By similarity).
FT   MOD_RES    1840   1840       Phosphothreonine (By similarity).
FT   MOD_RES    1842   1842       Phosphothreonine (By similarity).
FT   MOD_RES    1843   1843       Phosphoserine (By similarity).
FT   MOD_RES    1845   1845       Phosphoserine (By similarity).
FT   MOD_RES    1847   1847       Phosphoserine (By similarity).
FT   MOD_RES    1849   1849       Phosphoserine (By similarity).
FT   MOD_RES    1850   1850       Phosphoserine (By similarity).
FT   MOD_RES    1853   1853       Phosphotyrosine (By similarity).
FT   MOD_RES    1854   1854       Phosphothreonine (By similarity).
FT   MOD_RES    1857   1857       Phosphoserine (By similarity).
FT   MOD_RES    1871   1871       Phosphoserine (By similarity).
FT   MOD_RES    1874   1874       Phosphotyrosine (By similarity).
FT   MOD_RES    1875   1875       Phosphoserine (By similarity).
FT   MOD_RES    1877   1877       Phosphothreonine (By similarity).
FT   MOD_RES    1878   1878       Phosphoserine.
FT   MOD_RES    1881   1881       Phosphotyrosine (By similarity).
FT   MOD_RES    1882   1882       Phosphoserine (By similarity).
FT   MOD_RES    1884   1884       Phosphothreonine (By similarity).
FT   MOD_RES    1888   1888       Phosphotyrosine (By similarity).
FT   MOD_RES    1889   1889       Phosphoserine (By similarity).
FT   MOD_RES    1891   1891       Phosphothreonine (By similarity).
FT   MOD_RES    1892   1892       Phosphoserine (By similarity).
FT   MOD_RES    1894   1894       Phosphothreonine (By similarity).
FT   MOD_RES    1895   1895       Phosphotyrosine (By similarity).
FT   MOD_RES    1896   1896       Phosphoserine (By similarity).
FT   MOD_RES    1898   1898       Phosphothreonine (By similarity).
FT   MOD_RES    1899   1899       Phosphoserine (By similarity).
FT   MOD_RES    1902   1902       Phosphotyrosine (By similarity).
FT   MOD_RES    1903   1903       Phosphothreonine (By similarity).
FT   MOD_RES    1906   1906       Phosphoserine (By similarity).
FT   MOD_RES    1909   1909       Phosphotyrosine (By similarity).
FT   MOD_RES    1913   1913       Phosphoserine (By similarity).
FT   MOD_RES    1917   1917       Phosphoserine (By similarity).
FT   MOD_RES    1919   1919       Phosphothreonine (By similarity).
FT   MOD_RES    1920   1920       Phosphoserine (By similarity).
FT   MOD_RES    1923   1923       Phosphotyrosine.
FT   MOD_RES    1924   1924       Phosphoserine (By similarity).
FT   MOD_RES    1926   1926       Phosphothreonine (By similarity).
FT   MOD_RES    1927   1927       Phosphoserine.
FT   MOD_RES    1929   1929       Phosphothreonine (By similarity).
FT   MOD_RES    1930   1930       Phosphotyrosine (By similarity).
FT   MOD_RES    1931   1931       Phosphoserine (By similarity).
FT   MOD_RES    1933   1933       Phosphothreonine.
FT   MOD_RES    1934   1934       Phosphoserine (By similarity).
FT   MOD_RES    1962   1962       Phosphoserine (By similarity).
FT   MOD_RES    1966   1966       Phosphoserine (By similarity).
FT   MUTAGEN    1859   1859       K->R: Loss of ubiquitination, no effect
FT                                on interaction with WWP2; when associated
FT                                with R-1866; R-1873; R-1887; R-1908 and
FT                                R-1922.
FT   MUTAGEN    1866   1866       K->R: Loss of ubiquitination, no effect
FT                                on interaction with WWP2; when associated
FT                                with R-1859; R-1873; R-1887; R-1908 and
FT                                R-1922.
FT   MUTAGEN    1873   1873       K->R: Loss of ubiquitination, no effect
FT                                on interaction with WWP2; when associated
FT                                with R-1859; R-1866; R-1887; R-1908 and
FT                                R-1922.
FT   MUTAGEN    1887   1887       K->R: Loss of ubiquitination, no effect
FT                                on interaction with WWP2; when associated
FT                                with R-1859; R-1866; R-1873; R-1908 and
FT                                R-1922.
FT   MUTAGEN    1908   1908       K->R: Loss of ubiquitination, no effect
FT                                on interaction with WWP2; when associated
FT                                with R-1859; R-1866; R-1873; R-1887 and
FT                                R-1922.
FT   MUTAGEN    1922   1922       K->R: Loss of ubiquitination, no effect
FT                                on interaction with WWP2; when associated
FT                                with R-1859; R-1866; R-1873; R-1887 and
FT                                R-1908.
FT   CONFLICT   1498   1498       P -> R (in Ref. 1; AAA40071).
FT   CONFLICT   1499   1536       Missing (in Ref. 1; AAA40071).
SQ   SEQUENCE   1970 AA;  217176 MW;  7D76F38FD92A657E CRC64;
     MHGGGPPSGD SACPLRTIKR VQFGVLSPDE LKRMSVTEGG IKYPETTEGG RPKLGGLMDP
     RQGVIERTGR CQTCAGNMTE CPGHFGHIEL AKPVFHVGFL VKTMKVLRCV CFFCSKLLVD
     SNNPKIKDIL AKSKGQPKKR LTHVYDLCKG KNICEGGEEM DNKFGVEQPE GDEDLTKEKG
     HGGCGRYQPR IRRSGLELYA EWKHVNEDSQ EKKILLSPER VHEIFKRISD EECFVLGMEP
     RYARPEWMIV TVLPVPPLSV RPAVVMQGSA RNQDDLTHKL ADIVKINNQL RRNEQNGAAA
     HVIAEDVKLL QFHVATMVDN ELPGLPRAMQ KSGRPLKSLK QRLKGKEGRV RGNLMGKRVD
     FSARTVITPD PNLSIDQVGV PRSIAANMTF AEIVTPFNID RLQELVRRGN SQYPGAKYII
     RDNGDRIDLR FHPKPSDLHL QTGYKVERHM CDGDIVIFNR QPTLHKMSMM GHRVRILPWS
     TFRLNLSVTT PYNADFDGDE MNLHLPQSLE TRAEIQELAM VPRMIVTPQS NRPVMGIVQD
     TLTAVRKFTK RDVFLERGEV MNLLMFLSTW DGKVPQPAIL KPRPLWTGKQ IFSLIIPGHI
     NCIRTHSTHP DDEDSGPYKH ISPGDTKVVV ENGELIMGIL CKKSLGTSAG SLVHISYLEM
     GHDITRLFYS NIQTVINNWL LIEGHTIGIG DSIADSKTYQ DIQNTIKKAK QDVIEVIEKA
     HNNELEPTPG NTLRQTFENQ VNRILNDARD KTGSSAQKSL SEYNNFKSMV VSGAKGSKIN
     ISQVIAVVGQ QNVEGKRIPF GFKHRTLPHF IKDDYGPESR GFVENSYLAG LTPTEFFFHA
     MGGREGLIDT AVKTAETGYI QRRLIKSMES VMVKYDATVR NSINQVVQLR YGEDGLAGES
     VEFQNLATLK PSNKAFEKKF RFDYTNERAL RRTLQEDLVK DVLSNAHIQN ELEREFERMR
     EDREVLRVIF PTGDSKVVLP CNLLRMIWNA QKIFHINPRL PSDLHPIKVV EGVKELSKKL
     VIVNGDDPLS RQAQENATLL FNIHLRSTLC SRRMAEEFRL SGEAFDWLLG EIESKFNQAI
     AHPGEMVGAL AAQSLGEPAT QMTLNTFHYA GVSAKNVTLG VPRLKELINI SKKPKTPSLT
     VFLLGQSARD AERAKDILCR LEHTTLRKVT ANTAIYYDPN PQSTVVAEDQ EWVNVYYEMP
     DFDVARISPW LLRVELDRKH MTDRKLTMEQ IAEKINAGFG DDLNCIFNDD NAEKLVLRIR
     IMNSDENKMQ EEEEVVDKMD DDVFLRCIES NMLTDMTLQG IEQISKVYMH LPQTDNKKKI
     IITEDGEFKA LQEWILETDG VSLMRVLSEK DVDPVRTTSN DIVEIFTVLG IEAVRKALER
     ELYHVISFDG SYVNYRHLAL LCDTMTCRGH LMAITRHGVN RQDTGPLMKC SFEETVDVLM
     EAAAHGESDP MKGVSENIML GQLAPAGTGC FDLLLDAEKC KYGMEIPTNI PGLGAAGPTG
     MFFGSAPSPM GGISPAMTPW NQGATPAYGA WSPSVGSGMT PGAAGFSPSA ASDASGFSPG
     YSPAWSPTPG SPGSPGPSSP YIPSPGGAMS PSYSPTSPAY EPRSPGGYTP QSPSYSPTSP
     SYSPTSPSYS PTSPNYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP
     TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS
     YSPTSPNYSP TSPNYTPTSP SYSPTSPSYS PTSPNYTPTS PNYSPTSPSY SPTSPSYSPT
     SPSYSPSSPR YTPQSPTYTP SSPSYSPSSP SYSPTSPKYT PTSPSYSPSS PEYTPASPKY
     SPTSPKYSPT SPKYSPTSPT YSPTTPKYSP TSPTYSPTSP VYTPTSPKYS PTSPTYSPTS
     PKYSPTSPTY SPTSPKGSTY SPTSPGYSPT SPTYSLTSPA ISPDDSDEEN
//
ID   NUCL_MOUSE              Reviewed;         707 AA.
AC   P09405; Q548M9; Q61991; Q8BQD8; Q99K50;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 122.
DE   RecName: Full=Nucleolin;
DE   AltName: Full=Protein C23;
GN   Name=Ncl; Synonyms=Nuc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=88316930; PubMed=3137346; DOI=10.1016/0022-2836(88)90476-7;
RA   Bourbon H.-M., Lapeyre B., Amalric F.;
RT   "Structure of the mouse nucleolin gene. The complete sequence reveals
RT   that each RNA binding domain is encoded by two independent exons.";
RL   J. Mol. Biol. 200:627-638(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Egg, Lung, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
RX   MEDLINE=89121496; PubMed=2906027; DOI=10.1016/0378-1119(88)90600-2;
RA   Bourbon H.-M., Prudhomme M., Amalric F.;
RT   "Sequence and structure of the nucleolin promoter in rodents:
RT   characterization of a strikingly conserved CpG island.";
RL   Gene 68:73-84(1988).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-24.
RX   MEDLINE=91317840; PubMed=1860869;
RA   Pasternack M.S., Bleier K.J., McInerney T.N.;
RT   "Granzyme A binding to target cell proteins. Granzyme A binds to and
RT   cleaves nucleolin in vitro.";
RL   J. Biol. Chem. 266:14703-14708(1991).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-19 AND 558-567, AND FUNCTION.
RX   MEDLINE=94344117; PubMed=8065340;
RA   Yang T.-H., Tsai W.-H., Lee Y.-M., Lei H.-Y., Lai M.-Y., Chen D.-S.,
RA   Yeh N.-H., Lee S.-C.;
RT   "Purification and characterization of nucleolin and its identification
RT   as a transcription repressor.";
RL   Mol. Cell. Biol. 14:6068-6074(1994).
RN   [7]
RP   PROTEIN SEQUENCE OF 327-344; 351-364; 401-412; 432-439; 460-469;
RP   488-500; 525-538; 575-586 AND 608-621, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [8]
RP   IDENTIFICATION IN SWAP COMPLEX, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Spleen;
RX   MEDLINE=98307943; PubMed=9642267; DOI=10.1074/jbc.273.27.17025;
RA   Borggrefe T., Wabl M., Akhmedov A.T., Jessberger R.;
RT   "A B-cell-specific DNA recombination complex.";
RL   J. Biol. Chem. 273:17025-17035(1998).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145 AND SER-157, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145 AND SER-157, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-34; SER-40 AND
RP   SER-41, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [12]
RP   GLYCYLATION.
RX   PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA   Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M.,
RA   Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J.,
RA   Janke C.;
RT   "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT   polyglycylation.";
RL   Cell 137:1076-1087(2009).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-34; SER-40 AND
RP   SER-41, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Nucleolin is the major nucleolar protein of growing
CC       eukaryotic cells. It is found associated with intranucleolar
CC       chromatin and pre-ribosomal particles. It induces chromatin
CC       decondensation by binding to histone H1. It is thought to play a
CC       role in pre-rRNA transcription and ribosome assembly. May play a
CC       role in the process of transcriptional elongation. Binds RNA
CC       oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the
CC       telomeric single-stranded DNA 5'-TTAGGG-3' repeats (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with APTX and NSUN2. Component of the SWAP
CC       complex that consists of NPM1, NCL/nucleolin, PARP1 and SWAP70.
CC       Identified in a mRNP granule complex, at least composed of ACTB,
CC       ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL,
CC       HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL,
CC       PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9,
CC       SYNCRIP, TROVE2, YBX1 and untranslated mRNAs (By similarity).
CC       Component of a complex which is at least composed of HTATSF1/Tat-
CC       SF1, the P-TEFb complex components CDK9 and CCNT1, RNA polymerase
CC       II, SUPT5H, and NCL/nucleolin. Interacts (via RRM1 and C-terminal
CC       RRM4/Arg/Gly-rich domains) with TERT; the interaction is important
CC       for nucleolar localization of TERT (By similarity).
CC   -!- INTERACTION:
CC       Q9DC51:Gnai3; NbExp=2; IntAct=EBI-641864, EBI-641852;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm (By
CC       similarity). Note=Localized in cytoplasmic mRNP granules
CC       containing untranslated mRNAs (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in B-cells that have been induced to
CC       switch to various Ig isotypes.
CC   -!- PTM: Some glutamate residues are glycylated by TTLL8. This
CC       modification occurs exclusively on glutamate residues and results
CC       in a glycine chain on the gamma-carboxyl group.
CC   -!- SIMILARITY: Contains 4 RRM (RNA recognition motif) domains.
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DR   EMBL; X07699; CAA30538.1; -; Genomic_DNA.
DR   EMBL; AF318184; AAK07920.1; -; mRNA.
DR   EMBL; AK050958; BAC34476.1; -; mRNA.
DR   EMBL; AK083307; BAC38858.1; -; mRNA.
DR   EMBL; AK144894; BAE26119.1; -; mRNA.
DR   EMBL; AK161706; BAE36542.1; -; mRNA.
DR   EMBL; AK163275; BAE37270.1; -; mRNA.
DR   EMBL; BC005460; AAH05460.1; -; mRNA.
DR   EMBL; M22089; AAA39841.1; -; Genomic_DNA.
DR   IPI; IPI00317794; -.
DR   PIR; A29958; DNMS.
DR   RefSeq; NP_035010.3; NM_010880.3.
DR   UniGene; Mm.154378; -.
DR   UniGene; Mm.474153; -.
DR   ProteinModelPortal; P09405; -.
DR   SMR; P09405; 300-645.
DR   IntAct; P09405; 5.
DR   STRING; P09405; -.
DR   PhosphoSite; P09405; -.
DR   REPRODUCTION-2DPAGE; P09405; -.
DR   PRIDE; P09405; -.
DR   Ensembl; ENSMUST00000027438; ENSMUSP00000027438; ENSMUSG00000026234.
DR   GeneID; 17975; -.
DR   KEGG; mmu:17975; -.
DR   UCSC; uc007bvl.1; mouse.
DR   CTD; 17975; -.
DR   MGI; MGI:97286; Ncl.
DR   eggNOG; roNOG05125; -.
DR   HOVERGEN; HBG002295; -.
DR   InParanoid; P09405; -.
DR   OMA; GTEPTTA; -.
DR   OrthoDB; EOG45MN5J; -.
DR   PhylomeDB; P09405; -.
DR   NextBio; 292933; -.
DR   PMAP-CutDB; P09405; -.
DR   ArrayExpress; P09405; -.
DR   Bgee; P09405; -.
DR   CleanEx; MM_NCL; -.
DR   Genevestigator; P09405; -.
DR   GermOnline; ENSMUSG00000026234; Mus musculus.
DR   GO; GO:0005730; C:nucleolus; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR   GO; GO:0030529; C:ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0042162; F:telomeric DNA binding; ISS:UniProtKB.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 4.
DR   Pfam; PF00076; RRM_1; 4.
DR   SMART; SM00360; RRM; 4.
DR   PROSITE; PS50102; RRM; 4.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; DNA-binding;
KW   Methylation; Nucleus; Phosphoprotein; Repeat; RNA-binding.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    707       Nucleolin.
FT                                /FTId=PRO_0000081693.
FT   REPEAT       58     65       1.
FT   REPEAT       75     82       2.
FT   REPEAT       83     90       3.
FT   REPEAT       91     98       4.
FT   REPEAT       99    104       5; truncated.
FT   REPEAT      105    112       6.
FT   REPEAT      120    127       7.
FT   REPEAT      128    135       8.
FT   DOMAIN      309    385       RRM 1.
FT   DOMAIN      395    468       RRM 2.
FT   DOMAIN      487    561       RRM 3.
FT   DOMAIN      569    644       RRM 4.
FT   REGION       58    135       8 X 8 AA tandem repeats of X-T-P-X-K-K-X-
FT                                X.
FT   COMPBIAS    143    170       Asp/Glu-rich (acidic).
FT   COMPBIAS    190    215       Asp/Glu-rich (acidic).
FT   COMPBIAS    241    273       Asp/Glu-rich (acidic).
FT   COMPBIAS    646    697       Arg/Gly/Phe-rich.
FT   MOD_RES       9      9       N6-acetyllysine (By similarity).
FT   MOD_RES      28     28       Phosphoserine.
FT   MOD_RES      34     34       Phosphoserine.
FT   MOD_RES      40     40       Phosphoserine.
FT   MOD_RES      41     41       Phosphoserine.
FT   MOD_RES      67     67       Phosphoserine (By similarity).
FT   MOD_RES      69     69       Phosphothreonine (By similarity).
FT   MOD_RES      76     76       Phosphothreonine (By similarity).
FT   MOD_RES      99     99       Phosphothreonine (By similarity).
FT   MOD_RES     102    102       N6-acetyllysine (By similarity).
FT   MOD_RES     106    106       Phosphothreonine (By similarity).
FT   MOD_RES     116    116       N6-acetyllysine (By similarity).
FT   MOD_RES     121    121       Phosphothreonine (By similarity).
FT   MOD_RES     124    124       N6-acetyllysine (By similarity).
FT   MOD_RES     132    132       N6-acetyllysine (By similarity).
FT   MOD_RES     145    145       Phosphoserine.
FT   MOD_RES     157    157       Phosphoserine.
FT   MOD_RES     189    189       Phosphoserine (By similarity).
FT   MOD_RES     212    212       Phosphoserine (By similarity).
FT   MOD_RES     220    220       Phosphothreonine (By similarity).
FT   MOD_RES     320    320       N6-acetyllysine (By similarity).
FT   MOD_RES     335    335       N6-acetyllysine (By similarity).
FT   MOD_RES     369    369       Phosphothreonine (By similarity).
FT   MOD_RES     379    379       N6-acetyllysine (By similarity).
FT   MOD_RES     400    400       N6-acetyllysine (By similarity).
FT   MOD_RES     462    462       Phosphoserine (By similarity).
FT   MOD_RES     514    514       N6-acetyllysine (By similarity).
FT   MOD_RES     569    569       N6-acetyllysine (By similarity).
FT   MOD_RES     574    574       N6-acetyllysine (By similarity).
FT   MOD_RES     577    577       Phosphoserine (By similarity).
FT   MOD_RES     616    616       Phosphoserine (By similarity).
FT   MOD_RES     643    643       N6-acetyllysine (By similarity).
FT   CONFLICT    155    155       D -> E (in Ref. 3; AAH05460).
FT   CONFLICT    203    204       DD -> EE (in Ref. 3; AAH05460).
FT   CONFLICT    245    245       D -> E (in Ref. 3; AAH05460).
SQ   SEQUENCE   707 AA;  76723 MW;  EE2CE2ACDBF54CD4 CRC64;
     MVKLAKAGKT HGEAKKMAPP PKEVEEDSED EEMSEDEDDS SGEEEVVIPQ KKGKKATTTP
     AKKVVVSQTK KAAVPTPAKK AAVTPGKKAV ATPAKKNITP AKVIPTPGKK GAAQAKALVP
     TPGKKGAATP AKGAKNGKNA KKEDSDEDED EEDEDDSDED EDDEEEDEFE PPIVKGVKPA
     KAAPAAPASE DEEDDEDEDD EEDDDEEEED DSEEEVMEIT TAKGKKTPAK VVPMKAKSVA
     EEEDDEEEDE DDEDEDDEEE DDEDDDEEEE EEEPVKAAPG KRKKEMTKQK EAPEAKKQKV
     EGSEPTTPFN LFIGNLNPNK SVNELKFAIS ELFAKNDLAV VDVRTGTNRK FGYVDFESAE
     DLEKALELTG LKVFGNEIKL EKPKGRDSKK VRAARTLLAK NLSFNITEDE LKEVFEDAME
     IRLVSQDGKS KGIAYIEFKS EADAEKNLEE KQGAEIDGRS VSLYYTGEKG QRQERTGKTS
     TWSGESKTLV LSNLSYSATK ETLEEVFEKA TFIKVPQNPH GKPKGYAFIE FASFEDAKEA
     LNSCNKMEIE GRTIRLELQG SNSRSQPSKT LFVKGLSEDT TEETLKESFE GSVRARIVTD
     RETGSSKGFG FVDFNSEEDA KAAKEAMEDG EIDGNKVTLD WAKPKGEGGF GGRGGGRGGF
     GGRGGGRGGR GGFGGRGRGG FGGRGGFRGG RGGGGDFKPQ GKKTKFE
//
ID   PGK1_MOUSE              Reviewed;         417 AA.
AC   P09411; Q3TPE6; Q3UKV8; Q5XJE7;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 4.
DT   08-MAR-2011, entry version 104.
DE   RecName: Full=Phosphoglycerate kinase 1;
DE            EC=2.7.2.3;
GN   Name=Pgk1; Synonyms=Pgk-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=87106824; PubMed=3542714; DOI=10.1016/0378-1119(86)90025-9;
RA   Mori N., Singer-Sam J., Lee C.-Y., Riggs A.D.;
RT   "The nucleotide sequence of a cDNA clone containing the entire coding
RT   region for mouse X-chromosome-linked phosphoglycerate kinase.";
RL   Gene 45:275-280(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129, and C57BL/6; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX   MEDLINE=88152503; PubMed=3440520; DOI=10.1016/0378-1119(87)90214-9;
RA   Adra C.N., Boer P.H., McBurney M.W.;
RT   "Cloning and expression of the mouse pgk-1 gene and the nucleotide
RT   sequence of its promoter.";
RL   Gene 60:65-74(1987).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX   MEDLINE=90344879; PubMed=2166582; DOI=10.1016/0167-4781(90)90106-C;
RA   Tamaru M., Nagao Y., Taira M., Tatibana M., Masamune Y., Nakanishi Y.;
RT   "Selective activation of testis-specific genes in cultured rat
RT   spermatogenic cells.";
RL   Biochim. Biophys. Acta 1049:331-338(1990).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX   MEDLINE=90365677; PubMed=1975492; DOI=10.1007/BF02401419;
RA   Boer P.H., Potten H., Adra C.N., Jardine K., Mullhofer G.,
RA   McBurney M.W.;
RT   "Polymorphisms in the coding and noncoding regions of murine Pgk-1
RT   alleles.";
RL   Biochem. Genet. 28:299-308(1990).
RN   [8]
RP   PROTEIN SEQUENCE OF 23-30; 76-86; 98-123; 157-184; 193-216; 247-264;
RP   280-297; 333-350 AND 389-417, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [9]
RP   DISCUSSION OF SEQUENCE.
RX   MEDLINE=86275275; PubMed=3525226; DOI=10.1016/0014-5793(86)80835-3;
RA   Mori N., Singer-Sam J., Riggs A.D.;
RT   "Evolutionary conservation of the substrate-binding cleft of
RT   phosphoglycerate kinases.";
RL   FEBS Lett. 204:313-317(1986).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15648052; DOI=10.1002/pmic.200401066;
RA   Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA   Hart G.W., Burlingame A.L.;
RT   "Quantitative analysis of both protein expression and serine /
RT   threonine post-translational modifications through stable isotope
RT   labeling with dithiothreitol.";
RL   Proteomics 5:388-398(2005).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-76 AND TYR-196, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- CATALYTIC ACTIVITY: ATP + 3-phospho-D-glycerate = ADP + 3-phospho-
CC       D-glyceroyl phosphate.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 2/5.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the phosphoglycerate kinase family.
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DR   EMBL; M15668; AAA70267.1; -; mRNA.
DR   EMBL; AK145846; BAE26693.1; -; mRNA.
DR   EMBL; AK167710; BAE39754.1; -; mRNA.
DR   EMBL; AK167459; BAE39544.1; -; mRNA.
DR   EMBL; AK167441; BAE39527.1; -; mRNA.
DR   EMBL; AK133877; BAE21906.1; -; mRNA.
DR   EMBL; AK164440; BAE37790.1; -; mRNA.
DR   EMBL; BX469914; CAM17784.1; -; Genomic_DNA.
DR   EMBL; BC083355; AAH83355.1; -; mRNA.
DR   EMBL; BC108372; AAI08373.1; -; mRNA.
DR   EMBL; M18735; AAA39919.1; -; Genomic_DNA.
DR   EMBL; X55309; CAA39013.1; -; Genomic_DNA.
DR   EMBL; X15339; CAA33391.1; -; Genomic_DNA.
DR   IPI; IPI00555069; -.
DR   PIR; A25567; A25567.
DR   RefSeq; NP_032854.2; NM_008828.2.
DR   UniGene; Mm.336204; -.
DR   UniGene; Mm.336205; -.
DR   ProteinModelPortal; P09411; -.
DR   SMR; P09411; 2-417.
DR   STRING; P09411; -.
DR   PhosphoSite; P09411; -.
DR   SWISS-2DPAGE; P09411; -.
DR   COMPLUYEAST-2DPAGE; P09411; -.
DR   REPRODUCTION-2DPAGE; IPI00555069; -.
DR   REPRODUCTION-2DPAGE; P09411; -.
DR   PRIDE; P09411; -.
DR   Ensembl; ENSMUST00000081593; ENSMUSP00000080302; ENSMUSG00000062070.
DR   GeneID; 18655; -.
DR   KEGG; mmu:18655; -.
DR   CTD; 18655; -.
DR   MGI; MGI:97555; Pgk1.
DR   eggNOG; roNOG09572; -.
DR   GeneTree; ENSGT00390000008820; -.
DR   HOGENOM; HBG453500; -.
DR   HOVERGEN; HBG008177; -.
DR   InParanoid; P09411; -.
DR   OMA; NFANGTK; -.
DR   OrthoDB; EOG44MXS6; -.
DR   PhylomeDB; P09411; -.
DR   BRENDA; 2.7.2.3; 244.
DR   NextBio; 294662; -.
DR   Bgee; P09411; -.
DR   CleanEx; MM_PGK1; -.
DR   Genevestigator; P09411; -.
DR   GermOnline; ENSMUSG00000062070; Mus musculus.
DR   GermOnline; ENSMUSG00000066632; Mus musculus.
DR   GermOnline; ENSMUSG00000069008; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0004618; F:phosphoglycerate kinase activity; ISS:UniProtKB.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR001576; Phosphoglycerate_kinase.
DR   InterPro; IPR015901; Phosphoglycerate_kinase_C.
DR   InterPro; IPR015911; Phosphoglycerate_kinase_CS.
DR   InterPro; IPR015824; Phosphoglycerate_kinase_N.
DR   Gene3D; G3DSA:3.40.50.1270; Phosphoglycerate_kinase_C; 1.
DR   Gene3D; G3DSA:3.40.50.1260; Phosphoglycerate_kinase_N; 1.
DR   PANTHER; PTHR11406; PGK; 1.
DR   Pfam; PF00162; PGK; 1.
DR   PIRSF; PIRSF000724; Pgk; 1.
DR   PRINTS; PR00477; PHGLYCKINASE.
DR   SUPFAM; SSF53748; PGK; 1.
DR   PROSITE; PS00111; PGLYCERATE_KINASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing;
KW   Glycolysis; Kinase; Nucleotide-binding; Phosphoprotein; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    417       Phosphoglycerate kinase 1.
FT                                /FTId=PRO_0000145835.
FT   NP_BIND     373    376       ATP (By similarity).
FT   REGION       24     26       Substrate binding (By similarity).
FT   REGION       63     66       Substrate binding (By similarity).
FT   BINDING      39     39       Substrate (By similarity).
FT   BINDING     123    123       Substrate (By similarity).
FT   BINDING     171    171       Substrate (By similarity).
FT   BINDING     220    220       ATP (By similarity).
FT   BINDING     313    313       ATP; via carbonyl oxygen (By similarity).
FT   BINDING     344    344       ATP (By similarity).
FT   MOD_RES      11     11       N6-acetyllysine (By similarity).
FT   MOD_RES      30     30       N6-acetyllysine (By similarity).
FT   MOD_RES      48     48       N6-acetyllysine (By similarity).
FT   MOD_RES      75     75       N6-acetyllysine (By similarity).
FT   MOD_RES      76     76       Phosphotyrosine.
FT   MOD_RES      86     86       N6-acetyllysine (By similarity).
FT   MOD_RES      97     97       N6-acetyllysine (By similarity).
FT   MOD_RES     131    131       N6-acetyllysine (By similarity).
FT   MOD_RES     136    136       Phosphoserine (By similarity).
FT   MOD_RES     146    146       N6-acetyllysine (By similarity).
FT   MOD_RES     196    196       Phosphotyrosine.
FT   MOD_RES     199    199       N6-acetyllysine (By similarity).
FT   MOD_RES     203    203       Phosphoserine.
FT   MOD_RES     243    243       Phosphothreonine (By similarity).
FT   MOD_RES     267    267       N6-acetyllysine (By similarity).
FT   MOD_RES     291    291       N6-acetyllysine (By similarity).
FT   MOD_RES     323    323       N6-acetyllysine (By similarity).
FT   MOD_RES     390    390       Phosphoserine.
FT   MOD_RES     406    406       N6-acetyllysine (By similarity).
FT   CONFLICT     56     56       K -> N (in Ref. 1; AAA70267).
FT   CONFLICT    184    184       K -> R (in Ref. 2; BAE26693).
FT   CONFLICT    265    265       I -> V (in Ref. 2; BAE37790).
SQ   SEQUENCE   417 AA;  44550 MW;  5E2EE194FF9D8CEE CRC64;
     MSLSNKLTLD KLDVKGKRVV MRVDFNVPMK NNQITNNQRI KAAVPSIKFC LDNGAKSVVL
     MSHLGRPDGV PMPDKYSLEP VAAELKSLLG KDVLFLKDCV GPEVENACAN PAAGTVILLE
     NLRFHVEEEG KGKDASGNKV KAEPAKIDAF RASLSKLGDV YVNDAFGTAH RAHSSMVGVN
     LPQKAGGFLM KKELNYFAKA LESPERPFLA ILGGAKVADK IQLINNMLDK VNEMIIGGGM
     AFTFLKVLNN MEIGTSLYDE EGAKIVKDLM SKAEKNGVKI TLPVDFVTAD KFDENAKTGQ
     ATVASGIPAG WMGLDCGTES SKKYAEAVGR AKQIVWNGPV GVFEWEAFAR GTKSLMDEVV
     KATSRGCITI IGGGDTATCC AKWNTEDKVS HVSTGGGASL ELLEGKVLPG VDALSNV
//
ID   JUNB_MOUSE              Reviewed;         344 AA.
AC   P09450; Q8C2G9;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   08-MAR-2011, entry version 110.
DE   RecName: Full=Transcription factor jun-B;
DE   AltName: Full=MyD21;
GN   Name=Junb; Synonyms=Jun-b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=88144462; PubMed=3422745; DOI=10.1073/pnas.85.5.1487;
RA   Ryder K., Lau L.F., Nathans D.;
RT   "A gene activated by growth factors is related to the oncogene v-
RT   jun.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:1487-1491(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=96015051; PubMed=8530030; DOI=10.1006/geno.1995.1135;
RA   Phinney D.G., Tseng S.W., Ryder K.;
RT   "Complex genetic organization of junB: multiple blocks of flanking
RT   evolutionarily conserved sequence at the murine and human junB loci.";
RL   Genomics 28:228-234(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-30.
RX   MEDLINE=90191725; PubMed=1690380;
RA   Lord K.A., Hoffman-Liebermann B., Liebermann D.A.;
RT   "Complexity of the immediate early response of myeloid cells to
RT   terminal differentiation and growth arrest includes ICAM-1, Jun-B and
RT   histone variants.";
RL   Oncogene 5:387-396(1990).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248; THR-252 AND
RP   SER-256, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Transcription factor involved in regulating gene
CC       activity following the primary growth factor response. Binds to
CC       the DNA sequence 5'-TGA[CG]TCA-3'.
CC   -!- SUBUNIT: Binds DNA as an homodimer or as an heterodimer with
CC       another member of the Jun/Fos family (By similarity). Interacts
CC       with NFE2 (via its WW domains) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- INDUCTION: By growth factors.
CC   -!- PTM: Ubiquitinated by ITCH, leading to its degradation (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the bZIP family. Jun subfamily.
CC   -!- SIMILARITY: Contains 1 bZIP domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; J03236; AAA39343.1; -; mRNA.
DR   EMBL; U20735; AAA74916.1; -; Genomic_DNA.
DR   EMBL; AK088643; BAC40473.1; -; mRNA.
DR   EMBL; BC003790; AAH03790.1; -; mRNA.
DR   EMBL; X54332; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00137166; -.
DR   PIR; A28963; TVMSJB.
DR   RefSeq; NP_032442.1; NM_008416.2.
DR   UniGene; Mm.1167; -.
DR   UniGene; Mm.470093; -.
DR   ProteinModelPortal; P09450; -.
DR   SMR; P09450; 269-326.
DR   DIP; DIP-1069N; -.
DR   STRING; P09450; -.
DR   PhosphoSite; P09450; -.
DR   PRIDE; P09450; -.
DR   Ensembl; ENSMUST00000064922; ENSMUSP00000064680; ENSMUSG00000052837.
DR   GeneID; 16477; -.
DR   KEGG; mmu:16477; -.
DR   CTD; 16477; -.
DR   MGI; MGI:96647; Junb.
DR   eggNOG; maNOG08011; -.
DR   HOGENOM; HBG446073; -.
DR   HOVERGEN; HBG001722; -.
DR   InParanoid; P09450; -.
DR   OMA; NGCQLLL; -.
DR   OrthoDB; EOG4RV2RS; -.
DR   PhylomeDB; P09450; -.
DR   NextBio; 289767; -.
DR   ArrayExpress; P09450; -.
DR   Bgee; P09450; -.
DR   CleanEx; MM_JUNB; -.
DR   Genevestigator; P09450; -.
DR   GermOnline; ENSMUSG00000052837; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0071277; P:cellular response to calcium ion; IDA:MGI.
DR   GO; GO:0046697; P:decidualization; IMP:MGI.
DR   GO; GO:0060136; P:embryonic process involved in female pregnancy; IMP:MGI.
DR   GO; GO:0060716; P:labyrinthine layer blood vessel development; IMP:MGI.
DR   GO; GO:0001649; P:osteoblast differentiation; IMP:MGI.
DR   GO; GO:0033687; P:osteoblast proliferation; IMP:MGI.
DR   GO; GO:0030316; P:osteoclast differentiation; IMP:MGI.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; IDA:MGI.
DR   GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
DR   GO; GO:0001829; P:trophectodermal cell differentiation; IDA:MGI.
DR   GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR   InterPro; IPR011616; bZIP_1.
DR   InterPro; IPR008917; Euk_TF_DNA-bd.
DR   InterPro; IPR005643; JNK.
DR   InterPro; IPR002112; Leuzip_Jun.
DR   InterPro; IPR004827; TF_bZIP.
DR   Pfam; PF00170; bZIP_1; 1.
DR   Pfam; PF03957; Jun; 1.
DR   PRINTS; PR00043; LEUZIPPRJUN.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF47454; Euk_transcr_DNA; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN         1    344       Transcription factor jun-B.
FT                                /FTId=PRO_0000076439.
FT   DOMAIN      293    321       Leucine-zipper.
FT   DNA_BIND    270    289       Basic motif.
FT   MOD_RES     102    102       Phosphothreonine (By similarity).
FT   MOD_RES     104    104       Phosphothreonine (By similarity).
FT   MOD_RES     117    117       Phosphoserine (By similarity).
FT   MOD_RES     248    248       Phosphoserine.
FT   MOD_RES     252    252       Phosphothreonine.
FT   MOD_RES     256    256       Phosphoserine.
FT   CONFLICT     53     53       P -> S (in Ref. 3; BAC40473).
FT   CONFLICT    200    200       G -> R (in Ref. 2; AAA74916).
SQ   SEQUENCE   344 AA;  35765 MW;  6F52D4FECC32E234 CRC64;
     MCTKMEQPFY HDDSYAAAGY GRSPGSLSLH DYKLLKPTLA LNLADPYRGL KGPGARGPGP
     EGSGAGSYFS GQGSDTGASL KLASTELERL IVPNSNGVIT TTPTPPGQYF YPRGGGSGGG
     TGGGVTEEQE GFADGFVKAL DDLHKMNHVT PPNVSLGASG GPQAGPGGVY AGPEPPPVYT
     NLSSYSPASA PSGGSGTAVG TGSSYPTATI SYLPHAPPFA GGHPAQLGLS RGASAFKEEP
     QTVPEARSRD ATPPVSPINM EDQERIKVER KRLRNRLAAT KCRKRKLERI ARLEDKVKTL
     KAENAGLSSA AGLLREQVAQ LKQKVMTHVS NGCQLLLGVK GHAF
//
ID   ACE_MOUSE               Reviewed;        1312 AA.
AC   P09470; P22967; Q6GTS2;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 3.
DT   08-MAR-2011, entry version 114.
DE   RecName: Full=Angiotensin-converting enzyme;
DE            Short=ACE;
DE            EC=3.2.1.-;
DE            EC=3.4.15.1;
DE   AltName: Full=Dipeptidyl carboxypeptidase I;
DE   AltName: Full=Kininase II;
DE   AltName: CD_antigen=CD143;
DE   Contains:
DE     RecName: Full=Angiotensin-converting enzyme, soluble form;
DE   Flags: Precursor;
GN   Name=Ace; Synonyms=Dcp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SOMATIC).
RX   MEDLINE=89308599; PubMed=2545691;
RA   Bernstein K.E., Martin B.M., Edwards A.S., Bernstein E.A.;
RT   "Mouse angiotensin-converting enzyme is a protein composed of two
RT   homologous domains.";
RL   J. Biol. Chem. 264:11945-11951(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TESTIS-SPECIFIC), AND PARTIAL
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=90318396; PubMed=2164636;
RA   Howard T.E., Shai S.-Y., Langford K.G., Martin B.M., Bernstein K.E.;
RT   "Transcription of testicular angiotensin-converting enzyme (ACE) is
RT   initiated within the 12th intron of the somatic ACE gene.";
RL   Mol. Cell. Biol. 10:4294-4302(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SOMATIC).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-332 (ISOFORM SOMATIC), AND PARTIAL
RP   PROTEIN SEQUENCE.
RX   MEDLINE=88298730; PubMed=2841312;
RA   Bernstein K.E., Martin B.M., Bernstein E.A., Linton J., Striker L.,
RA   Striker G.;
RT   "The isolation of angiotensin-converting enzyme cDNA.";
RL   J. Biol. Chem. 263:11021-11024(1988).
RN   [5]
RP   PROTEIN SEQUENCE OF 35-54.
RC   TISSUE=Kidney;
RX   MEDLINE=88215372; PubMed=2835538; DOI=10.1038/ki.1988.48;
RA   Bernstein K.E., Martin B.M., Striker L., Striker G.;
RT   "Partial protein sequence of mouse and bovine kidney angiotensin
RT   converting enzyme.";
RL   Kidney Int. 33:652-655(1988).
RN   [6]
RP   FUNCTION.
RX   PubMed=7753170; DOI=10.1038/375146a0;
RA   Krege J.H., John S.W., Langenbach L.L., Hodgin J.B., Hagaman J.R.,
RA   Bachman E.S., Jennette J.C., O'Brien D.A., Smithies O.;
RT   "Male-female differences in fertility and blood pressure in ACE-
RT   deficient mice.";
RL   Nature 375:146-148(1995).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=8642790;
RA   Esther C.R. Jr., Howard T.E., Marino E.M., Goddard J.M.,
RA   Capecchi M.R., Bernstein K.E.;
RT   "Mice lacking angiotensin-converting enzyme have low blood pressure,
RT   renal pathology, and reduced male fertility.";
RL   Lab. Invest. 74:953-965(1996).
RN   [8]
RP   FUNCTION, ENZYME REGULATION, AND MUTAGENESIS OF HIS-993; GLU-994 AND
RP   HIS-997.
RX   PubMed=15665832; DOI=10.1038/nm1179;
RA   Kondoh G., Tojo H., Nakatani Y., Komazawa N., Murata C., Yamagata K.,
RA   Maeda Y., Kinoshita T., Okabe M., Taguchi R., Takeda J.;
RT   "Angiotensin-converting enzyme is a GPI-anchored protein releasing
RT   factor crucial for fertilization.";
RL   Nat. Med. 11:160-166(2005).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-151, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Plasma;
RX   PubMed=16944957; DOI=10.1021/pr060186m;
RA   Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
RA   Gevaert K.;
RT   "Proteome-wide characterization of N-glycosylation events by diagonal
RT   chromatography.";
RL   J. Proteome Res. 5:2438-2447(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1305, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Converts angiotensin I to angiotensin II by release of
CC       the terminal His-Leu, this results in an increase of the
CC       vasoconstrictor activity of angiotensin. Also able to inactivate
CC       bradykinin, a potent vasodilator. Has also a glycosidase activity
CC       which releases GPI-anchored proteins from the membrane by cleaving
CC       the mannose linkage in the GPI moiety. This GPIase activity seems
CC       to be crucial for the egg-binding ability of the sperm.
CC   -!- CATALYTIC ACTIVITY: Release of a C-terminal dipeptide,
CC       oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither
CC       Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II,
CC       with increase in vasoconstrictor activity, but no action on
CC       angiotensin II.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit. Isoform Testis-specific
CC       only binds 1 zinc ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 3 chloride ions per subunit (By similarity).
CC   -!- ENZYME REGULATION: Peptidase activity is specifically inhibited by
CC       lisinopril, captopril and enalaprilat. In contrast, GPIase
CC       activity is nearly insensitive to captopril.
CC   -!- SUBCELLULAR LOCATION: Angiotensin-converting enzyme, soluble form:
CC       Secreted (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Somatic;
CC         IsoId=P09470-1; Sequence=Displayed;
CC       Name=Testis-specific; Synonyms=ACE-T;
CC         IsoId=P09470-2, P22967-1;
CC         Sequence=VSP_037638, VSP_037639;
CC   -!- TISSUE SPECIFICITY: Testis-specific isoform is expressed in
CC       spermatocytes, adult testis.
CC   -!- INDUCTION: Expression is thought to be subject to hormonal
CC       regulation by androgens.
CC   -!- PTM: Phosphorylated by CK2 on Ser-1305; which allows membrane
CC       retention (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Low blood pressure, elevated serum
CC       potassium, anemia, and renal defects. Male mice have reduced
CC       fertility.
CC   -!- SIMILARITY: Belongs to the peptidase M2 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; J04946; AAA37147.1; -; mRNA.
DR   EMBL; J04947; AAA37148.1; -; mRNA.
DR   EMBL; M55333; AAA37149.1; -; mRNA.
DR   EMBL; M61094; AAA37150.1; -; Genomic_DNA.
DR   EMBL; BC040404; AAH40404.1; -; mRNA.
DR   EMBL; J03940; AAA37146.1; -; mRNA.
DR   IPI; IPI00272690; -.
DR   IPI; IPI00284824; -.
DR   PIR; A34171; A34171.
DR   PIR; A35655; A35655.
DR   RefSeq; NP_033728.1; NM_009598.1.
DR   RefSeq; NP_997507.1; NM_207624.4.
DR   UniGene; Mm.754; -.
DR   ProteinModelPortal; P09470; -.
DR   SMR; P09470; 35-646, 650-1227.
DR   STRING; P09470; -.
DR   MEROPS; M02.001; -.
DR   MEROPS; M02.004; -.
DR   PhosphoSite; P09470; -.
DR   PRIDE; P09470; -.
DR   Ensembl; ENSMUST00000001963; ENSMUSP00000001963; ENSMUSG00000020681.
DR   GeneID; 11421; -.
DR   KEGG; mmu:11421; -.
DR   UCSC; uc007lxu.1; mouse.
DR   CTD; 11421; -.
DR   MGI; MGI:87874; Ace.
DR   HOGENOM; HBG356536; -.
DR   HOVERGEN; HBG000264; -.
DR   InParanoid; P09470; -.
DR   OMA; EFWDKSM; -.
DR   OrthoDB; EOG495ZQZ; -.
DR   PhylomeDB; P09470; -.
DR   BRENDA; 3.4.15.1; 244.
DR   NextBio; 278668; -.
DR   ArrayExpress; P09470; -.
DR   Bgee; P09470; -.
DR   Genevestigator; P09470; -.
DR   GermOnline; ENSMUSG00000020681; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0008241; F:peptidyl-dipeptidase activity; IDA:UniProtKB.
DR   GO; GO:0042447; P:hormone catabolic process; IDA:BHF-UCL.
DR   GO; GO:0002446; P:neutrophil mediated immunity; IMP:MGI.
DR   GO; GO:0008217; P:regulation of blood pressure; IDA:BHF-UCL.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; Peptidase_M2; 1.
DR   Pfam; PF01401; Peptidase_M2; 2.
DR   PRINTS; PR00791; PEPDIPTASEA.
DR   PROSITE; PS00142; ZINC_PROTEASE; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Carboxypeptidase; Cell membrane;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Membrane; Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW   Repeat; Secreted; Signal; Transmembrane; Transmembrane helix; Zinc.
FT   SIGNAL        1     34
FT   CHAIN        35   1312       Angiotensin-converting enzyme.
FT                                /FTId=PRO_0000028539.
FT   CHAIN        35   1237       Angiotensin-converting enzyme, soluble
FT                                form.
FT                                /FTId=PRO_0000028540.
FT   PROPEP     1238   1312       Removed in secreted form (By similarity).
FT                                /FTId=PRO_0000028541.
FT   TOPO_DOM     35   1264       Extracellular (Potential).
FT   TRANSMEM   1265   1281       Helical; (Potential).
FT   TOPO_DOM   1282   1312       Cytoplasmic (Potential).
FT   REGION       35    635       Peptidase M2 1.
FT   REGION      636   1237       Peptidase M2 2.
FT   ACT_SITE    396    396       1 (By similarity).
FT   ACT_SITE    994    994       2.
FT   METAL       395    395       Zinc 1; catalytic (By similarity).
FT   METAL       399    399       Zinc 1; catalytic (By similarity).
FT   METAL       423    423       Zinc 1; catalytic (By similarity).
FT   METAL       993    993       Zinc 2; catalytic.
FT   METAL       997    997       Zinc 2; catalytic.
FT   METAL      1021   1021       Zinc 2; catalytic (By similarity).
FT   BINDING     236    236       Chloride 1 (By similarity).
FT   BINDING     534    534       Chloride 1 (By similarity).
FT   BINDING     796    796       Chloride 2 (By similarity).
FT   BINDING     834    834       Chloride 3 (By similarity).
FT   BINDING    1095   1095       Chloride 2 (By similarity).
FT   BINDING    1099   1099       Chloride 2 (By similarity).
FT   BINDING    1132   1132       Chloride 3 (By similarity).
FT   MOD_RES    1305   1305       Phosphoserine.
FT   CARBOHYD     59     59       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     79     79       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    116    116       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    151    151       N-linked (GlcNAc...).
FT   CARBOHYD    165    165       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    323    323       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    514    514       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    682    682       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    700    700       N-linked (GlcNAc...) (complex) (By
FT                                similarity).
FT   CARBOHYD    719    719       N-linked (GlcNAc...) (complex) (By
FT                                similarity).
FT   CARBOHYD    765    765       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    947    947       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1196   1196       N-linked (GlcNAc...) (Potential).
FT   DISULFID    162    170       By similarity.
FT   DISULFID    762    768       By similarity.
FT   DISULFID    962    980       By similarity.
FT   DISULFID   1148   1160       By similarity.
FT   VAR_SEQ       1    580       Missing (in isoform Testis-specific).
FT                                /FTId=VSP_037638.
FT   VAR_SEQ     581    646       GCSRPWQEVLKDLVGSDALDAKALLEYFQPVSQWLEEQNQR
FT                                NGEVLGWPENQWRPPLPDNYPEGID -> MGQGWATPGLPS
FT                                FLFLLLCCGHHLLVLSQVATDHVTANQGITNQATTRSQTTT
FT                                HQATIDQTTQIPN (in isoform Testis-
FT                                specific).
FT                                /FTId=VSP_037639.
FT   MUTAGEN     993    993       H->K: Abolishes peptidase activity but no
FT                                effect on GPIase activity; when
FT                                associated to K-997.
FT   MUTAGEN     994    994       E->D: Abolishes peptidase activity but no
FT                                effect on GPIase activity.
FT   MUTAGEN     997    997       H->K: Abolishes peptidase activity but no
FT                                effect on GPIase activity; when
FT                                associated to K-993.
FT   CONFLICT    568    568       A -> T (in Ref. 1; AAA37147).
SQ   SEQUENCE   1312 AA;  150918 MW;  7DF9F5BE91762DFF CRC64;
     MGAASGQRGR WPLSPPLLML SLLVLLLQPS PAPALDPGLQ PGNFSPDEAG AQLFAESYNS
     SAEVVMFQST VASWAHDTNI TEENARRQEE AALVSQEFAE VWGKKAKELY ESIWQNFTDS
     KLRRIIGSIR TLGPANLPLA QRQQYNSLLS NMSRIYSTGK VCFPNKTATC WSLDPELTNI
     LASSRSYAKL LFAWEGWHDA VGIPLKPLYQ DFTAISNEAY RQDDFSDTGA FWRSWYESPS
     FEESLEHIYH QLEPLYLNLH AYVRRALHRR YGDKYVNLRG PIPAHLLGDM WAQSWENIYD
     MVVPFPDKPN LDVTSTMVQK GWNATHMFRV SEEFFTSLGL SPMPPEFWAE SMLEKPTDGR
     EVVCHASAWD FYNRKDFRIK QCTRVTMEQL ATVHHEMGHV QYYLQYKDLH VSLRRGANPG
     FHEAIGDVLA LSVSTPAHLH KIGLLDHVTN DIESDINYLL KMALEKIAFL PFGYLVDQWR
     WGVFSGRTPP SRYNFDWWYL RTKYQGICPP VARNETHFDA GAKFHIPNVT PYIRYFVSFV
     LQFQFHQALC KEAGHQGPLH QCDIYQSAQA GAKLKQVLQA GCSRPWQEVL KDLVGSDALD
     AKALLEYFQP VSQWLEEQNQ RNGEVLGWPE NQWRPPLPDN YPEGIDLETD EAKADRFVEE
     YDRTAQVLLN EYAEANWQYN TNITIEGSKI LLEKSTEVSN HTLKYGTRAK TFDVSNFQNS
     SIKRIIKKLQ NLDRAVLPPK ELEEYNQILL DMETTYSLSN ICYTNGTCMP LEPDLTNMMA
     TSRKYEELLW AWKSWRDKVG RAILPFFPKY VEFSNKIAKL NGYTDAGDSW RSLYESDNLE
     QDLEKLYQEL QPLYLNLHAY VRRSLHRHYG SEYINLDGPI PAHLLGNMWA QTWSNIYDLV
     APFPSAPNID ATEAMIKQGW TPRRIFKEAD NFFTSLGLLP VPPEFWNKSM LEKPTDGREV
     VCHPSAWDFY NGKDFRIKQC TSVNMEDLVI AHHEMGHIQY FMQYKDLPVT FREGANPGFH
     EAIGDIMALS VSTPKHLYSL NLLSTEGSGY EYDINFLMKM ALDKIAFIPF SYLIDQWRWR
     VFDGSITKEN YNQEWWSLRL KYQGLCPPVP RSQGDFDPGS KFHVPANVPY VRYFVSFIIQ
     FQFHEALCRA AGHTGPLHKC DIYQSKEAGK LLADAMKLGY SKPWPEAMKL ITGQPNMSAS
     AMMNYFKPLT EWLVTENRRH GETLGWPEYN WAPNTARAEG STAESNRVNF LGLYLEPQQA
     RVGQWVLLFL GVALLVATVG LAHRLYNIRN HHSLRRPHRG PQFGSEVELR HS
//
ID   FRIH_MOUSE              Reviewed;         182 AA.
AC   P09528; Q3UI44;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 110.
DE   RecName: Full=Ferritin heavy chain;
DE            Short=Ferritin H subunit;
DE            EC=1.16.3.1;
GN   Name=Fth1; Synonyms=Fth;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c;
RX   MEDLINE=90016900; PubMed=2798146; DOI=10.1093/nar/17.19.8005;
RA   Yachaou A., Renaudie F., Grandchamp B., Beaumont C.;
RT   "Nucleotide sequence of the mouse ferritin H chain gene.";
RL   Nucleic Acids Res. 17:8005-8005(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Macrophage;
RX   MEDLINE=89057487; PubMed=3194211; DOI=10.1093/nar/16.21.10373;
RA   Miyazaki Y., Setoguchi M., Higuchi Y., Yoshida S., Akizuki S.,
RA   Yamamoto S.;
RT   "Nucleotide sequence of cDNA encoding the heavy subunit of mouse
RT   macrophage ferritin.";
RL   Nucleic Acids Res. 16:10373-10373(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=88315064; PubMed=3410854;
RA   Torti S.V., Kwak E.L., Miller S.C., Miller L.L., Ringold G.M.,
RA   Myambo K.B., Young A.P., Torti F.M.;
RT   "The molecular cloning and characterization of murine ferritin heavy
RT   chain, a tumor necrosis factor-inducible gene.";
RL   J. Biol. Chem. 263:12638-12644(1988).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=91078648; PubMed=2258056; DOI=10.1016/0378-1119(90)90396-9;
RA   Kwak E.L., Torti S.V., Torti F.M.;
RT   "Murine ferritin heavy chain: isolation and characterization of a
RT   functional gene.";
RL   Gene 94:255-261(1990).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=89214195; PubMed=2708374;
RA   Beaumont C., Dugast I., Renaudie F., Souroujon M., Grandchamp B.;
RT   "Transcriptional regulation of ferritin H and L subunits in adult
RT   erythroid and liver cells from the mouse. Unambiguous identification
RT   of mouse ferritin subunits and in vitro formation of the ferritin
RT   shells.";
RL   J. Biol. Chem. 264:7498-7504(1989).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Amnion, Heart, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   PROTEIN SEQUENCE OF 11-23 AND 55-64, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [9]
RP   FUNCTION.
RX   PubMed=19154717; DOI=10.1016/j.devcel.2008.12.002;
RA   Li J.Y., Paragas N., Ned R.M., Qiu A., Viltard M., Leete T.,
RA   Drexler I.R., Chen X., Sanna-Cherchi S., Mohammed F., Williams D.,
RA   Lin C.S., Schmidt-Ott K.M., Andrews N.C., Barasch J.;
RT   "Scara5 is a ferritin receptor mediating non-transferrin iron
RT   delivery.";
RL   Dev. Cell 16:35-46(2009).
CC   -!- FUNCTION: Stores iron in a soluble, non-toxic, readily available
CC       form. Important for iron homeostasis. Has ferroxidase activity.
CC       Iron is taken up in the ferrous form and deposited as ferric
CC       hydroxides after oxidation. Also plays a role in delivery of iron
CC       to cells. Mediates iron uptake in capsule cells of the developing
CC       kidney.
CC   -!- CATALYTIC ACTIVITY: 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O.
CC   -!- SUBUNIT: Oligomer of 24 subunits. There are two types of subunits:
CC       L (light) chain and H (heavy) chain. The major chain can be light
CC       or heavy, depending on the species and tissue type. The functional
CC       molecule forms a roughly spherical shell with a diameter of 12 nm
CC       and contains a central cavity into which the insoluble mineral
CC       iron core is deposited.
CC   -!- SIMILARITY: Belongs to the ferritin family.
CC   -!- SIMILARITY: Contains 1 ferritin-like diiron domain.
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DR   EMBL; X52561; CAA36795.1; -; Genomic_DNA.
DR   EMBL; X12812; CAA31300.1; -; mRNA.
DR   EMBL; J03941; AAA37611.1; -; mRNA.
DR   EMBL; M60170; AAA37613.1; -; Genomic_DNA.
DR   EMBL; M24509; AAA37612.1; -; mRNA.
DR   EMBL; AK027998; BAC25694.1; -; mRNA.
DR   EMBL; AK139622; BAE24084.1; -; mRNA.
DR   EMBL; AK147082; BAE27662.1; -; mRNA.
DR   EMBL; AK150262; BAE29419.1; -; mRNA.
DR   EMBL; AK150508; BAE29621.1; -; mRNA.
DR   EMBL; AK150628; BAE29718.1; -; mRNA.
DR   EMBL; AK150679; BAE29759.1; -; mRNA.
DR   EMBL; AK150693; BAE29772.1; -; mRNA.
DR   EMBL; AK151192; BAE30189.1; -; mRNA.
DR   EMBL; AK151241; BAE30233.1; -; mRNA.
DR   EMBL; AK151399; BAE30367.1; -; mRNA.
DR   EMBL; AK151609; BAE30548.1; -; mRNA.
DR   EMBL; AK151675; BAE30600.1; -; mRNA.
DR   EMBL; AK152071; BAE30924.1; -; mRNA.
DR   EMBL; AK152542; BAE31297.1; -; mRNA.
DR   EMBL; AK152702; BAE31431.1; -; mRNA.
DR   EMBL; AK153017; BAE31651.1; -; mRNA.
DR   EMBL; AK153195; BAE31795.1; -; mRNA.
DR   EMBL; AK153199; BAE31799.1; -; mRNA.
DR   EMBL; AK159243; BAE34925.1; -; mRNA.
DR   EMBL; AK168601; BAE40468.1; -; mRNA.
DR   EMBL; AK169004; BAE40803.1; -; mRNA.
DR   EMBL; BC012314; AAH12314.1; -; mRNA.
DR   IPI; IPI00230145; -.
DR   PIR; S06070; S06070.
DR   RefSeq; NP_034369.1; NM_010239.1.
DR   UniGene; Mm.1776; -.
DR   ProteinModelPortal; P09528; -.
DR   SMR; P09528; 7-177.
DR   IntAct; P09528; 3.
DR   STRING; P09528; -.
DR   PhosphoSite; P09528; -.
DR   REPRODUCTION-2DPAGE; P09528; -.
DR   PRIDE; P09528; -.
DR   Ensembl; ENSMUST00000025563; ENSMUSP00000025563; ENSMUSG00000024661.
DR   GeneID; 14319; -.
DR   KEGG; mmu:14319; -.
DR   UCSC; uc008got.1; mouse.
DR   CTD; 14319; -.
DR   MGI; MGI:95588; Fth1.
DR   eggNOG; roNOG16109; -.
DR   GeneTree; ENSGT00560000076974; -.
DR   HOGENOM; HBG750128; -.
DR   HOVERGEN; HBG000410; -.
DR   InParanoid; P09528; -.
DR   OMA; HQDCEAA; -.
DR   OrthoDB; EOG47PX78; -.
DR   PhylomeDB; P09528; -.
DR   BRENDA; 1.16.3.1; 244.
DR   NextBio; 285759; -.
DR   ArrayExpress; P09528; -.
DR   Bgee; P09528; -.
DR   CleanEx; MM_FTH1; -.
DR   Genevestigator; P09528; -.
DR   GermOnline; ENSMUSG00000024661; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0004322; F:ferroxidase activity; IEA:EC.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:UniProtKB-KW.
DR   GO; GO:0006955; P:immune response; ISS:UniProtKB.
DR   GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR009040; Ferritin-like.
DR   InterPro; IPR012347; Ferritin-rel.
DR   InterPro; IPR009078; Ferritin/RR-like.
DR   InterPro; IPR014034; Ferritin_CS.
DR   InterPro; IPR008331; Ferritin_Dps.
DR   InterPro; IPR001519; Ferritin_N.
DR   Gene3D; G3DSA:1.20.1260.10; Ferritin_rel; 1.
DR   PANTHER; PTHR11431; Ferritin_N; 1.
DR   Pfam; PF00210; Ferritin; 1.
DR   SUPFAM; SSF47240; Ferritin/RR_like; 1.
DR   PROSITE; PS00540; FERRITIN_1; 1.
DR   PROSITE; PS00204; FERRITIN_2; 1.
DR   PROSITE; PS50905; FERRITIN_LIKE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Iron; Iron storage; Metal-binding;
KW   Oxidoreductase; Phosphoprotein.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    182       Ferritin heavy chain.
FT                                /FTId=PRO_0000201049.
FT   DOMAIN       11    160       Ferritin-like diiron.
FT   METAL        28     28       Iron 1 (By similarity).
FT   METAL        63     63       Iron 1 (By similarity).
FT   METAL        63     63       Iron 2 (By similarity).
FT   METAL        66     66       Iron 1 (By similarity).
FT   METAL       108    108       Iron 2 (By similarity).
FT   METAL       142    142       Iron 2 (By similarity).
FT   MOD_RES     175    175       Phosphothreonine (By similarity).
FT   CONFLICT     17     17       A -> S (in Ref. 5; AAA37612).
FT   CONFLICT    137    137       Y -> H (in Ref. 5; AAA37612).
FT   CONFLICT    140    140       S -> N (in Ref. 5; AAA37612).
FT   CONFLICT    164    164       A -> S (in Ref. 5; AAA37612).
SQ   SEQUENCE   182 AA;  21067 MW;  129A8887A2BC650B CRC64;
     MTTASPSQVR QNYHQDAEAA INRQINLELY ASYVYLSMSC YFDRDDVALK NFAKYFLHQS
     HEEREHAEKL MKLQNQRGGR IFLQDIKKPD RDDWESGLNA MECALHLEKS VNQSLLELHK
     LATDKNDPHL CDFIETYYLS EQVKSIKELG DHVTNLRKMG APEAGMAEYL FDKHTLGHGD
     ES
//
ID   SURF1_MOUSE             Reviewed;         306 AA.
AC   P09925; Q99KB4; Q9DCU5;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 3.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Surfeit locus protein 1;
GN   Name=Surf1; Synonyms=Surf-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=87089816; PubMed=3025660;
RA   Williams T.J., Fried M.;
RT   "The MES-1 murine enhancer element is closely associated with the
RT   heterogeneous 5' ends of two divergent transcription units.";
RL   Mol. Cell. Biol. 6:4558-4569(1986).
RN   [2]
RP   SEQUENCE REVISION.
RA   Fried M.;
RL   Submitted (SEP-1988) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Probably involved in the biogenesis of the COX complex
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the SURF1 family.
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DR   EMBL; M14689; AAA40153.1; -; Genomic_DNA.
DR   EMBL; AK002469; BAB22123.1; -; mRNA.
DR   EMBL; BC004755; AAH04755.1; -; mRNA.
DR   IPI; IPI00319135; -.
DR   PIR; B25394; B25394.
DR   RefSeq; NP_038705.2; NM_013677.2.
DR   UniGene; Mm.347512; -.
DR   STRING; P09925; -.
DR   PRIDE; P09925; -.
DR   Ensembl; ENSMUST00000015934; ENSMUSP00000015934; ENSMUSG00000015790.
DR   GeneID; 20930; -.
DR   KEGG; mmu:20930; -.
DR   UCSC; uc008iwg.1; mouse.
DR   CTD; 20930; -.
DR   MGI; MGI:98443; Surf1.
DR   HOVERGEN; HBG058486; -.
DR   InParanoid; P09925; -.
DR   OrthoDB; EOG4BZN3D; -.
DR   PhylomeDB; P09925; -.
DR   NextBio; 299855; -.
DR   ArrayExpress; P09925; -.
DR   Bgee; P09925; -.
DR   CleanEx; MM_SURF1; -.
DR   Genevestigator; P09925; -.
DR   GermOnline; ENSMUSG00000015790; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IMP:MGI.
DR   InterPro; IPR002994; Surf1.
DR   Pfam; PF02104; SURF1; 1.
DR   PROSITE; PS50895; SURF1; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    306       Surfeit locus protein 1.
FT                                /FTId=PRO_0000215653.
FT   TRANSMEM     68     86       Helical; (Potential).
FT   TRANSMEM    280    300       Helical; (Potential).
FT   CONFLICT      9      9       V -> G (in Ref. 1; AAA40153).
FT   CONFLICT     14     14       M -> I (in Ref. 3; BAB22123).
FT   CONFLICT    284    284       W -> CR (in Ref. 1; AAA40153).
SQ   SEQUENCE   306 AA;  34798 MW;  8D9ECE9FB726AEB7 CRC64;
     MAAVMALAVL PRRMTRWSQW AYAGRAQFCA VRRSVFGFSV RSGMVCRPRR CCSSTAETAA
     AKAEDDSFLQ WFLLLIPATA FGLGTWQVQR RKWKLKLIAE LESRVMAEPI PLPADPMELK
     NLEYRPVKVR GHFDHSKELY IMPRTMVDPV REARDAGRLS STESGAHVVT PFHCSDLGVT
     ILVNRGFVPR KKVNPETRQK GQVLGEVDLV GIVRLTENRK PFVPENSPER NHWYYRDLEA
     MAKITGADPI FIDADFHSTA PGGPIGGQTR VTLRNEHMQY ILTWYGLCAA TSYLWFQKFV
     RRTPIM
//
ID   NUD10_MOUSE             Reviewed;         164 AA.
AC   P0C027; Q8BKF4;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Diphosphoinositol polyphosphate phosphohydrolase 3-alpha;
DE            Short=DIPP-3-alpha;
DE            Short=DIPP3-alpha;
DE            EC=3.6.1.52;
DE   AltName: Full=Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-alpha;
DE            EC=3.6.1.-;
DE   AltName: Full=Nucleoside diphosphate-linked moiety X motif 10;
DE            Short=Nudix motif 10;
GN   Name=Nudt10; Synonyms=Dipp3a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
RX   MEDLINE=22698698; PubMed=12689335; DOI=10.1042/BJ20030142;
RA   Hua L.V., Hidaka K., Pesesse X., Barnes L.D., Shears S.B.;
RT   "Paralogous murine Nudt10 and Nudt11 genes have differential
RT   expression patterns but encode identical proteins that are
RT   physiologically competent diphosphoinositol polyphosphate
RT   phosphohydrolases.";
RL   Biochem. J. 373:81-89(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in
CC       PP-InsP5 (diphosphoinositol pentakisphosphate), suggesting that it
CC       may play a role in signal transduction. Also able to catalyze the
CC       hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A
CC       being the preferred substrates. The major reaction products are
CC       ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to
CC       hydrolyze 5-phosphoribose 1-diphosphate; however, the relevance of
CC       such activity in vivo remains unclear.
CC   -!- CATALYTIC ACTIVITY: Diphospho-myo-inositol polyphosphate + H(2)O =
CC       myo-inositol polyphosphate + phosphate.
CC   -!- COFACTOR: Binds 3 magnesium or manganese ions per subunit.
CC       Manganese may be the true cofactor in vivo (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: Mainly expressed in testis, liver kidney and,
CC       at lower level, in heart, brain, spleen, lung and skeletal muscle.
CC   -!- MISCELLANEOUS: Nudt10 and Nudt11 code for identical proteins,
CC       which gives their indidual characterization difficult. Thus, most
CC       experiments do not discriminate between the 2 proteins.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. DIPP subfamily.
CC   -!- SIMILARITY: Contains 1 nudix hydrolase domain.
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DR   EMBL; BC055771; AAH55771.1; -; mRNA.
DR   IPI; IPI00121707; -.
DR   RefSeq; NP_001026834.1; NM_001031664.1.
DR   RefSeq; NP_067406.2; NM_021431.2.
DR   UniGene; Mm.41198; -.
DR   UniGene; Mm.426101; -.
DR   ProteinModelPortal; P0C027; -.
DR   SMR; P0C027; 17-144.
DR   PRIDE; P0C027; -.
DR   Ensembl; ENSMUST00000103006; ENSMUSP00000100071; ENSMUSG00000073293.
DR   Ensembl; ENSMUST00000103007; ENSMUSP00000100072; ENSMUSG00000073295.
DR   GeneID; 102954; -.
DR   GeneID; 58242; -.
DR   KEGG; mmu:102954; -.
DR   KEGG; mmu:58242; -.
DR   CTD; 102954; -.
DR   CTD; 58242; -.
DR   MGI; MGI:2147931; Nudt10.
DR   eggNOG; roNOG16536; -.
DR   HOGENOM; HBG713158; -.
DR   HOVERGEN; HBG053341; -.
DR   InParanoid; P0C027; -.
DR   OrthoDB; EOG479F89; -.
DR   PhylomeDB; P0C027; -.
DR   BRENDA; 3.6.1.52; 244.
DR   NextBio; 355731; -.
DR   ArrayExpress; P0C027; -.
DR   Bgee; P0C027; -.
DR   Genevestigator; P0C027; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008486; F:diphosphoinositol-polyphosphate diphosphatase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR020476; Nudix_hydrolase.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR015797; NUDIX_hydrolase_dom-like.
DR   Gene3D; G3DSA:3.90.79.10; NUDIX_hydrolase; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   PRINTS; PR00502; NUDIXFAMILY.
DR   SUPFAM; SSF55811; NUDIX_hydrolase; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Phosphoprotein.
FT   CHAIN         1    164       Diphosphoinositol polyphosphate
FT                                phosphohydrolase 3-alpha.
FT                                /FTId=PRO_0000057063.
FT   DOMAIN       17    144       Nudix hydrolase.
FT   REGION       17     19       Substrate binding (By similarity).
FT   REGION       89     91       Substrate binding (By similarity).
FT   MOTIF        50     71       Nudix box.
FT   ACT_SITE     68     68       Proton acceptor (By similarity).
FT   METAL        49     49       Magnesium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        65     65       Magnesium 2 (By similarity).
FT   METAL        65     65       Magnesium 3 (By similarity).
FT   METAL        69     69       Magnesium 1 (By similarity).
FT   BINDING       9      9       Substrate (By similarity).
FT   BINDING      40     40       Substrate (By similarity).
FT   MOD_RES     148    148       Phosphoserine (By similarity).
FT   MOD_RES     150    150       Phosphothreonine (By similarity).
FT   MOD_RES     154    154       Phosphoserine (By similarity).
FT   MOD_RES     158    158       Phosphoserine (By similarity).
FT   MOD_RES     162    162       Phosphoserine (By similarity).
SQ   SEQUENCE   164 AA;  18593 MW;  7141513979E4FBCD CRC64;
     MKCKPNQTRT YDPEGFKKRA ACLCFRSERE DEVLLVSSSR YPDRWIVPGG GMEPEEEPDG
     AAVREVYEEA GVKGKLGRLL GVFEQNQDRK HRTYVFVLTV TELLEDWEDS VSIGRKREWF
     KIEDAIKVLQ CHKPVHAEYL EKLKLGGSPT NGNSAAPSPP ESEP
//
ID   RC3H2_MOUSE             Reviewed;        1187 AA.
AC   P0C090; A2AVP5;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 1.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=RING finger and CCCH-type zinc finger domain-containing protein 2;
DE   AltName: Full=Membrane-associated nucleic acid-binding protein;
GN   Name=Rc3h2; Synonyms=Mnab;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SUBUNIT: Binds DNA (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region (By
CC       similarity). Endomembrane system (By similarity). Note=Membrane-
CC       associated. Primarily localizes to the perinuclear space, probably
CC       to the endoplasmic reticulum or trans-Golgi network (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 C3H1-type zinc finger.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
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DR   EMBL; AL929572; CAM25192.1; -; Genomic_DNA.
DR   IPI; IPI00349293; -.
DR   RefSeq; NP_001094061.1; NM_001100591.1.
DR   UniGene; Mm.288785; -.
DR   UniGene; Mm.477223; -.
DR   ProteinModelPortal; P0C090; -.
DR   SMR; P0C090; 8-76, 408-441.
DR   PhosphoSite; P0C090; -.
DR   PRIDE; P0C090; -.
DR   Ensembl; ENSMUST00000100143; ENSMUSP00000097721; ENSMUSG00000075376.
DR   Ensembl; ENSMUST00000112936; ENSMUSP00000108558; ENSMUSG00000075376.
DR   GeneID; 319817; -.
DR   KEGG; mmu:319817; -.
DR   UCSC; uc008jmq.1; mouse.
DR   CTD; 319817; -.
DR   MGI; MGI:2442789; Rc3h2.
DR   HOGENOM; HBG715492; -.
DR   HOVERGEN; HBG080524; -.
DR   InParanoid; P0C090; -.
DR   OMA; PQTGYYP; -.
DR   NextBio; 395454; -.
DR   ArrayExpress; P0C090; -.
DR   Bgee; P0C090; -.
DR   CleanEx; MM_RC3H2; -.
DR   Genevestigator; P0C090; -.
DR   GermOnline; ENSMUSG00000075376; Mus musculus.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; DNA-binding; Membrane; Metal-binding; Phosphoprotein; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1187       RING finger and CCCH-type zinc finger
FT                                domain-containing protein 2.
FT                                /FTId=PRO_0000055969.
FT   ZN_FING      14     54       RING-type; degenerate.
FT   ZN_FING     410    438       C3H1-type.
FT   COMPBIAS    575    686       Pro-rich.
FT   MOD_RES     548    548       Phosphoserine (By similarity).
SQ   SEQUENCE   1187 AA;  131295 MW;  2C73E8F430649669 CRC64;
     MPVQAAQWTE FLSCPICYNE FDENVHKPIS LGCSHTVCKT CLNKLHRKAC PFDQTAINTD
     IDVLPVNFAL LQLVGAQVPD HQSIKLSNLG ENKHYEVAKK CVEDLALYLK PLSGGKGVAS
     LNQSALSRPM QRKLVTLVNC QLVEEEGRVR AMRAARSLGE RTVTELILQH QNPQQLSANL
     WAAVRARGCQ FLGPAMQEEA LKLVLLALED GSALSRKVLV LFVVQRLEPR FPQASKTSIG
     HVVQLLYRAS CFKVTKRDED SSLMQLKEEF RSYEALRREH DAQIVHIAME AGLRISPEQW
     SSLLYGDLAH KSHMQSIIDK LQSPESFAKS VQELTIVLQR TGDPANLNRL RPHLELLANI
     DPNPDAVSPT WEQLENAMVA VKTVVHGLVD FIQNYSRKGH ETPQPQPNSK YKTSMCRDLR
     QQGGCPRGTN CTFAHSQEEL EKYRLRNKKM SATVRTFPLL NKVGVNSTVT TTAGNVISVI
     GSTETTGKIV ASTNGISNTE SSVSQLIPRG TDSAVRTLET VKKVGKVGTN AQNAGPSAES
     VSENKIGSPP KTPVSNAAAT SAGPSNFGTE LNSLPPKSSP FLTRVPVYPQ HSESIQYFQD
     PRTQIPFEVP QYPQTGYYPP PPTVPAGVTP CVPRFVRSSN VPESSLPPAS MPYADHYSTF
     SPRDRMNSSP YQPPPPQQYG PVPPVPSGMY APVYDSRRIW RPAMYQRDDI IRSNSLPPMD
     VMHSSVYQTS LRERYNSLDG YYSVACQPPN DPRTTVPLPR EPCGHLKTSC EEQLRRKPDQ
     WTQYHTQKTP VSSTLPVATQ SPTPPSPLFS VDFRSDFSES VSGAKFEEDH LSHYSPWSCG
     TIGSCINAID SEPKDVIANS NAVLMDLDSG DVKRRVHLFE AQRRTKEEDP IIPFSDGPII
     SKWGAISRSS RTGYHTTDPV QATASQGSAT KPISVSDYVP YVNAVDSRWS SYGNDATSSA
     HYIERDRFIV TDLSGHRKHS STGDLLSIEL QQAKSNSLLL QREANALAMQ QKWNSLDEGR
     HLTLNLLSKE IELRNGENDY TEDTVDTKPD RDIELELSAL DTDEPDGQSE QIEEILDIQL
     GISSQNDQLL NGTAVENGHP AQQHQKDPGK PKRQSLGEDH VILEEQKPIL PVTSCFSQPR
     PMSISSASCL PITTSVSVGN LILKTHVMSE DKNDFLKPIA NGKMVNS
//
ID   CHMP6_MOUSE             Reviewed;         200 AA.
AC   P0C0A3;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Charged multivesicular body protein 6;
DE   AltName: Full=Chromatin-modifying protein 6;
GN   Name=Chmp6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RG   The MGC Project Team;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable core component of the endosomal sorting
CC       required for transport complex III (ESCRT-III) which is involved
CC       in multivesicular bodies (MVBs) formation and sorting of endosomal
CC       cargo proteins into MVBs. MVBs contain intraluminal vesicles
CC       (ILVs) that are generated by invagination and scission from the
CC       limiting membrane of the endosome and mostly are delivered to
CC       lysosomes enabling degradation of membrane proteins, such as
CC       stimulated growth factor receptors, lysosomal enzymes and lipids.
CC       The MVB pathway appears to require the sequential function of
CC       ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly
CC       dissociate from the invaginating membrane before the ILV is
CC       released. The ESCRT machinery also functions in topologically
CC       equivalent membrane fission events, such as the terminal stages of
CC       cytokinesis. ESCRT-III proteins are believed to mediate the
CC       necessary vesicle extrusion and/or membrane fission activities,
CC       possibly in conjunction with the AAA ATPase VPS4. In the ESCRT-III
CC       complex, it probably serves as an acceptor for the ESCRT-II
CC       complex on endosomal membranes (By similarity).
CC   -!- SUBUNIT: Probable core component of the endosomal sorting required
CC       for transport complex III (ESCRT-III). ESCRT-III components are
CC       thought to multimerize to form a flat lattice on the perimeter
CC       membrane of the endosome. Several assembly forms of ESCRT-III may
CC       exist that interact and act sequentally. Interacts with VPS4A; the
CC       interaction is direct. Interacts with VPS4B; the interaction is
CC       direct. Interacts with CHMP4A, CHMP4B and CHMP4C. Interacts with
CC       SNF8, VPS25 and VPS36 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endomembrane system (By similarity).
CC       Endosome membrane; Lipid-anchor (By similarity). Late endosome
CC       membrane (By similarity). Note=Localizes to endosomal membranes
CC       (By similarity).
CC   -!- DOMAIN: The acidic C-terminus and the basic N-termminus are
CC       thought to render the protein in a closed, soluble and inactive
CC       conformation through an autoinhibitory intramolecular interaction.
CC       The open and active conformation, which enables membrane binding
CC       and oligomerization, is achieved by interaction with other
CC       cellular binding partners, probably including other ESCRT
CC       components (By similarity).
CC   -!- SIMILARITY: Belongs to the SNF7 family.
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DR   EMBL; BI157958; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00110956; -.
DR   RefSeq; NP_001078967.1; NM_001085498.2.
DR   UniGene; Mm.306673; -.
DR   ProteinModelPortal; P0C0A3; -.
DR   STRING; P0C0A3; -.
DR   PhosphoSite; P0C0A3; -.
DR   PRIDE; P0C0A3; -.
DR   Ensembl; ENSMUST00000026434; ENSMUSP00000026434; ENSMUSG00000025371.
DR   GeneID; 208092; -.
DR   KEGG; mmu:208092; -.
DR   UCSC; uc007mrd.1; mouse.
DR   CTD; 208092; -.
DR   MGI; MGI:3583942; Chmp6.
DR   eggNOG; roNOG16815; -.
DR   HOGENOM; HBG592869; -.
DR   HOVERGEN; HBG080510; -.
DR   InParanoid; P0C0A3; -.
DR   OMA; KIGNECL; -.
DR   OrthoDB; EOG4DBTG6; -.
DR   PhylomeDB; P0C0A3; -.
DR   NextBio; 372136; -.
DR   ArrayExpress; P0C0A3; -.
DR   Bgee; P0C0A3; -.
DR   CleanEx; MM_CHMP6; -.
DR   Genevestigator; P0C0A3; -.
DR   GermOnline; ENSMUSG00000025371; Mus musculus.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR005024; Snf7.
DR   Pfam; PF03357; Snf7; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Endosome; Lipoprotein; Membrane; Myristate;
KW   Protein transport; Transport.
FT   INIT_MET      1      1       Removed (Potential).
FT   CHAIN         2    200       Charged multivesicular body protein 6.
FT                                /FTId=PRO_0000211509.
FT   COILED       10    145       Potential.
FT   MOTIF       168    179       Type-2 MIT-interacting motif (By
FT                                similarity).
FT   LIPID         2      2       N-myristoyl glycine (Potential).
SQ   SEQUENCE   200 AA;  23416 MW;  13EE6683997D46C6 CRC64;
     MGNLFGRKKQ SRVTEQDRAI LQLKQQRDKL RQYQKRVTQQ LERERALARQ LLRDGRKERA
     KLLLKKKRYR EQLLDRTENQ ISSLEAMVQS IEFTQIEMKV MEGLQVGNEC LNKMHQVMSI
     EEVERILDET QEAVEYQRQI DELLAGNFTQ EDEDAILEEL NAITQEQMEL PEVPSEPLPD
     RNPEAPAKAR SRQAELVAAS
//
ID   LRC4B_MOUSE             Reviewed;         709 AA.
AC   P0C192;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   08-MAR-2011, entry version 47.
DE   RecName: Full=Leucine-rich repeat-containing protein 4B;
DE   AltName: Full=Netrin-G3 ligand;
DE            Short=NGL-3;
DE   Flags: Precursor;
GN   Name=Lrrc4b; Synonyms=Lrig4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Embryonic brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 63-709.
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   INTERACTION WITH DLG4.
RX   PubMed=16980967; DOI=10.1038/nn1763;
RA   Kim S., Burette A., Chung H.S., Kwon S.-K., Woo J., Lee H.W., Kim K.,
RA   Kim H., Weinberg R.J., Kim E.;
RT   "NGL family PSD-95-interacting adhesion molecules regulate excitatory
RT   synapse formation.";
RL   Nat. Neurosci. 9:1294-1301(2006).
CC   -!- FUNCTION: Synaptic adhesion protein. Regulates the formation of
CC       excitatory synapses. The trans-synaptic adhesion between LRRC4B
CC       and PTPRF regulates the formation of excitatory synapses in a
CC       bidirectional manner (By similarity).
CC   -!- SUBUNIT: Interacts with PTPRF (By similarity). Interacts with
CC       DLG4.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. Cell
CC       junction, synapse, presynaptic cell membrane (By similarity).
CC   -!- DOMAIN: The extreme C-terminus binds to the first 2 PDZ domains of
CC       DLG4.
CC   -!- PTM: N-glycosylated (By similarity). O-glycosylated; contains
CC       sialic acid (By similarity).
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 10 LRR (leucine-rich) repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC060263; AAH60263.1; -; mRNA.
DR   EMBL; AK140418; BAE24378.1; -; mRNA.
DR   IPI; IPI00381059; -.
DR   RefSeq; NP_937893.1; NM_198250.1.
DR   UniGene; Mm.44173; -.
DR   ProteinModelPortal; P0C192; -.
DR   SMR; P0C192; 57-457.
DR   STRING; P0C192; -.
DR   PhosphoSite; P0C192; -.
DR   PRIDE; P0C192; -.
DR   Ensembl; ENSMUST00000058667; ENSMUSP00000053123; ENSMUSG00000047085.
DR   GeneID; 272381; -.
DR   KEGG; mmu:272381; -.
DR   UCSC; uc009gpj.1; mouse.
DR   CTD; 272381; -.
DR   MGI; MGI:3027390; Lrrc4b.
DR   eggNOG; maNOG18524; -.
DR   GeneTree; ENSGT00600000084155; -.
DR   HOGENOM; HBG444724; -.
DR   HOVERGEN; HBG052359; -.
DR   InParanoid; P0C192; -.
DR   OMA; ERDHLNH; -.
DR   OrthoDB; EOG4W9J3K; -.
DR   NextBio; 393574; -.
DR   ArrayExpress; P0C192; -.
DR   Bgee; P0C192; -.
DR   CleanEx; MM_LRRC4B; -.
DR   Genevestigator; P0C192; -.
DR   GermOnline; ENSMUSG00000047085; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR000372; LRR-contain_N.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00560; LRR_1; 4.
DR   Pfam; PF01462; LRRNT; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00369; LRR_TYP; 4.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00013; LRRNT; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51450; LRR; 7.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Leucine-rich repeat; Membrane; Phosphoprotein;
KW   Repeat; Signal; Synapse; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     38       Potential.
FT   CHAIN        39    709       Leucine-rich repeat-containing protein
FT                                4B.
FT                                /FTId=PRO_0000232387.
FT   TRANSMEM    575    595       Helical; (Potential).
FT   REPEAT       87    110       LRR 1.
FT   REPEAT      111    134       LRR 2.
FT   REPEAT      135    158       LRR 3.
FT   REPEAT      160    182       LRR 4.
FT   REPEAT      184    207       LRR 5.
FT   REPEAT      208    229       LRR 6.
FT   REPEAT      230    253       LRR 7.
FT   REPEAT      255    277       LRR 8.
FT   REPEAT      278    301       LRR 9.
FT   DOMAIN      366    454       Ig-like C2-type.
FT   COMPBIAS     39     42       Poly-Gly.
FT   COMPBIAS    464    482       Gly-rich.
FT   COMPBIAS    631    637       Poly-Ala.
FT   MOD_RES     700    700       Phosphoserine (By similarity).
FT   CARBOHYD    226    226       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    285    285       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    335    335       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    376    376       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    402    402       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    424    424       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    427    427       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    446    446       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    454    454       N-linked (GlcNAc...) (Potential).
FT   DISULFID    387    438       By similarity.
FT   CONFLICT    574    574       K -> R (in Ref. 2; BAE24378).
SQ   SEQUENCE   709 AA;  76156 MW;  0C39148F9A8E3586 CRC64;
     MAQAHIRGSP CPLLPPGRMS WPHGALLLLW LFSPPLRAGG GGVAVTSAAG GGSPPATSCP
     AACSCSNQAS RVICTRRELA EVPASIPVNT RYLNLQENSI QVIRTDTFKH LRHLEILQLS
     KNLVRKIEVG AFNGLPSLNT LELFDNRLTT VPTQAFEYLS KLRELWLRNN PIESIPSYAF
     NRVPSLRRLD LGELKRLEYI SEAAFEGLVN LRYLNLGMCN LKDIPNLTAL VRLEELELSG
     NRLDLIRPGS FQGLTSLRKL WLMHAQVATI ERNAFDDLKS LEELNLSHNN LMSLPHDLFT
     PLHRLERVHL NHNPWHCNCD VLWLSWWLKE TVPSNTTCCA RCHAPAGLKG RYIGELDQSH
     FTCYAPVIVE PPTDLNVTEG MAAELKCRTG TSMTSVNWLT PNGTLMTHGS YRVRISVLHD
     GTLNFTNVTV QDTGQYTCMV TNSAGNTTAS ATLNVSAVDP VAAGGPGGGG PGGGGGAGGA
     GGYTYFTTVT VETLETQPGE EAQQPRGTEK EPPGPTTDGA WGGGRPDAAA PASASTTAPA
     PRSSRPTEKA FTVPITDVTE NALKDLDDVM KTTKIIIGCF VAITFMAAVM LVAFYKLRKQ
     HQLHKHHGPT RTVEIINVED ELPAASAVSV AAAAAVAGGA GVGGDSHLAL PALERDHLNH
     HHYVAAAFKA HYGGNPGGGC GAKGPGLNSI HEPLLFKSGS KENVQETQI
//
ID   KGP1_MOUSE              Reviewed;         671 AA.
AC   P0C605; Q14DK6; Q9Z0Z0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   RecName: Full=cGMP-dependent protein kinase 1;
DE            Short=cGK 1;
DE            Short=cGK1;
DE            EC=2.7.11.12;
DE   AltName: Full=cGMP-dependent protein kinase I;
DE            Short=cGKI;
GN   Name=Prkg1; Synonyms=Prkg1b, Prkgr1a, Prkgr1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=99185054; PubMed=10085070; DOI=10.1074/jbc.274.13.8391;
RA   Collins S.P., Uhler M.D.;
RT   "Cyclic AMP- and cyclic GMP-dependent protein kinases differ in their
RT   regulation of cyclic AMP response element-dependent gene
RT   transcription.";
RL   J. Biol. Chem. 274:8391-8404(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH MRVI1.
RX   PubMed=16990611; DOI=10.1182/blood-2005-10-026294;
RA   Antl M., von Bruehl M.-L., Eiglsperger C., Werner M., Konrad I.,
RA   Kocher T., Wilm M., Hofmann F., Massberg S., Schlossmann J.;
RT   "IRAG mediates NO/cGMP-dependent inhibition of platelet aggregation
RT   and thrombus formation.";
RL   Blood 109:552-559(2007).
CC   -!- FUNCTION: Phosphorylates PPP1R12A (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Binding of cGMP results in enzyme activation
CC       (By similarity).
CC   -!- SUBUNIT: Isoform alpha: parallel homodimer or heterodimer and also
CC       heterotetramer. Interacts directly with PPP1R12A. Non-covalent
CC       dimer of dimer of PRKG1-PRKG1 and PPP1R12A-PPP1R12A. This
CC       interaction targets PRKG1 to stress fibers to mediate smooth
CC       muscle cell relaxation and vasodilation in responses to rises in
CC       cGMP (By similarity). Isoform beta: antiparallel homodimer. Part
CC       of cGMP kinase signaling complex at least composed of ACTA2/alpha-
CC       actin, CNN1/calponin H1, PLN/phospholamban, PRKG1 and ITPR1 (By
CC       similarity). Interacts with MRVI1.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Alpha; Synonyms=CGK1-alpha;
CC         IsoId=P0C605-1; Sequence=Displayed;
CC       Name=Beta; Synonyms=CGK1-beta;
CC         IsoId=P0C605-2, Q9Z0Z0-1;
CC         Sequence=VSP_038715;
CC   -!- DOMAIN: Heterotetramerization is mediated by the interaction
CC       between a coiled-coil of PRKG1 and the leucine/isoleucine zipper
CC       of PPP1R12A/MBS, the myosin-binding subunit of the myosin
CC       phosphatase (By similarity).
CC   -!- PTM: 65 kDa monomer is produced by proteolytic cleavage (By
CC       similarity).
CC   -!- MISCELLANEOUS: Exhibit a substrate specificity similar but not
CC       identical to that of CAK (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. cGMP subfamily.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 2 cyclic nucleotide-binding domains.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF084547; AAD16044.1; -; mRNA.
DR   EMBL; AC102751; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC103405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC108399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC116507; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC119158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC122548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC113162; AAI13163.1; -; mRNA.
DR   IPI; IPI00129693; -.
DR   IPI; IPI00458024; -.
DR   RefSeq; NP_001013855.1; NM_001013833.2.
DR   RefSeq; NP_035290.1; NM_011160.2.
DR   UniGene; Mm.381170; -.
DR   UniGene; Mm.381172; -.
DR   ProteinModelPortal; P0C605; -.
DR   SMR; P0C605; 9-44, 57-658.
DR   DIP; DIP-29981N; -.
DR   STRING; P0C605; -.
DR   PRIDE; P0C605; -.
DR   Ensembl; ENSMUST00000065067; ENSMUSP00000067576; ENSMUSG00000052920.
DR   GeneID; 19091; -.
DR   KEGG; mmu:19091; -.
DR   CTD; 19091; -.
DR   MGI; MGI:108174; Prkg1.
DR   HOVERGEN; HBG006211; -.
DR   OMA; IGPRTRR; -.
DR   OrthoDB; EOG4V9TQ7; -.
DR   PhylomeDB; P0C605; -.
DR   BRENDA; 2.7.11.12; 244.
DR   NextBio; 295648; -.
DR   ArrayExpress; P0C605; -.
DR   Bgee; P0C605; -.
DR   CleanEx; MM_PRKG1; -.
DR   Genevestigator; P0C605; -.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030553; F:cGMP binding; IDA:UniProtKB.
DR   GO; GO:0004692; F:cGMP-dependent protein kinase activity; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0016358; P:dendrite development; IMP:MGI.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR016232; cGMP-dependent_protein_kinase.
DR   InterPro; IPR002374; cGMP_dep__kinase.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 2.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF000559; cGMP-dep_kinase; 1.
DR   PRINTS; PR00104; CGMPKINASE.
DR   SMART; SM00100; cNMP; 2.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF51206; cNMP_binding; 2.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 2.
DR   PROSITE; PS00889; CNMP_BINDING_2; 2.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; cGMP; cGMP-binding;
KW   Coiled coil; Disulfide bond; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    671       cGMP-dependent protein kinase 1.
FT                                /FTId=PRO_0000314022.
FT   DOMAIN      360    619       Protein kinase.
FT   DOMAIN      620    671       AGC-kinase C-terminal.
FT   NP_BIND     103    218       cNMP 1.
FT   NP_BIND     221    342       cNMP 2.
FT   NP_BIND     366    374       ATP (By similarity).
FT   REGION        2    102       Dimerization (By similarity).
FT   COILED        9     44       By similarity.
FT   ACT_SITE    484    484       Proton acceptor (By similarity).
FT   BINDING     390    390       ATP (By similarity).
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES      59     59       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     515    515       Phosphothreonine (By similarity).
FT   DISULFID     43     43       Interchain (By similarity).
FT   VAR_SEQ       1     89       MSELEEDFAKILMLKEERIKELEKRLSEKEEEIQELKRKLH
FT                                KCQSVLPVPSTHIGPRTTRAQGISAEPQTYRSFHDLRQAFR
FT                                KFTKSER -> MGTLRDLQYALQEKIEELRQRDALIDELEL
FT                                ELDQKDELIQKLQNELDKYRSVIRPATQQAQKQSASTLQGE
FT                                PRTKRQAISAEPTAFDIQDLSHVTLPFYPKSPQ (in
FT                                isoform Beta).
FT                                /FTId=VSP_038715.
SQ   SEQUENCE   671 AA;  76350 MW;  51878E2D27F26A22 CRC64;
     MSELEEDFAK ILMLKEERIK ELEKRLSEKE EEIQELKRKL HKCQSVLPVP STHIGPRTTR
     AQGISAEPQT YRSFHDLRQA FRKFTKSERS KDLIKEAILD NDFMKNLELS QIQEIVDCMY
     PVEYGKDSCI IKEGDVGSLV YVMEDGKVEV TKEGVKLCTM GPGKVFGELA ILYNCTRTAT
     VKTLVNVKLW AIDRQCFQTI MMRTGLIKHT EYMEFLKSVP TFQSLPDEIL SKLADVLEET
     HYENGEYIIR QGARGDTFFI ISKGQVNVTR EDSPSEDPVF LRTLGKGDWF GEKALQGEDV
     RTANVIAAEA VTCLVIDRDS FKHLIGGLDD VSNKAYEDAE AKAKYEAEAA FFANLKLSDF
     NIIDTLGVGG FGRVELVQLK SEESKTFAMK ILKKRHIVDT RQQEHIRSEK QIMQGAHSDF
     IVRLYRTFKD SKYLYMLMEA CLGGELWTIL RDRGSFEDST TRFYTACVVE AFAYLHSKGI
     IYRDLKPENL ILDHRGYAKL VDFGFAKKIG FGKKTWTFCG TPEYVAPEII LNKGHDISAD
     YWSLGILMYE LLTGSPPFSG PDPMKTYNII LRGIDMIEFP KKIAKNAANL IKKLCRDNPS
     ERLGNLKNGV KDIQKHKWFE GFNWEGLRKG TLTPPIIPSV ASPTDTSNFD SFPEDSDEPP
     PDDNSGWDID F
//
ID   IGS11_MOUSE             Reviewed;         428 AA.
AC   P0C673;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   08-MAR-2011, entry version 35.
DE   RecName: Full=Immunoglobulin superfamily member 11;
DE            Short=IgSF11;
DE   AltName: Full=Brain and testis-specific immunoglobulin superfamily protein;
DE            Short=Bt-IGSF;
DE   Flags: Precursor;
GN   Name=Igsf11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], GLYCOSYLATION, TOPOLOGY, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=12207903; DOI=10.1016/S0006-291X(02)02025-9;
RA   Suzu S., Hayashi Y., Harumi T., Nomaguchi K., Yamada M., Hayasawa H.,
RA   Motoyoshi K.;
RT   "Molecular cloning of a novel immunoglobulin superfamily gene
RT   preferentially expressed by brain and testis.";
RL   Biochem. Biophys. Res. Commun. 296:1215-1221(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Functions as a cell adhesion molecule through homophilic
CC       interaction. Stimulates cell growth (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis and detected in
CC       kidney and adrenal gland. In brain, expressed in commisure fibers
CC       of the corpus callosum and pyramidal cell layers of the dentate
CC       gyrus and hippocampus where it is probably expressed by both
CC       neurons and glial cells.
CC   -!- PTM: N-glycosylated.
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC       domain.
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DR   EMBL; AB079880; BAC07547.1; -; mRNA.
DR   EMBL; BC057555; AAH57555.1; -; mRNA.
DR   IPI; IPI00172354; -.
DR   RefSeq; NP_733548.2; NM_170599.2.
DR   UniGene; Mm.245564; -.
DR   ProteinModelPortal; P0C673; -.
DR   SMR; P0C673; 28-235.
DR   STRING; P0C673; -.
DR   PhosphoSite; P0C673; -.
DR   PRIDE; P0C673; -.
DR   Ensembl; ENSMUST00000023478; ENSMUSP00000023478; ENSMUSG00000022790.
DR   GeneID; 207683; -.
DR   KEGG; mmu:207683; -.
DR   CTD; 207683; -.
DR   MGI; MGI:2388477; Igsf11.
DR   eggNOG; roNOG09473; -.
DR   GeneTree; ENSGT00600000084033; -.
DR   HOGENOM; HBG506514; -.
DR   HOVERGEN; HBG107996; -.
DR   InParanoid; P0C673; -.
DR   OMA; TYNSRYW; -.
DR   OrthoDB; EOG4ZGPCD; -.
DR   NextBio; 372001; -.
DR   ArrayExpress; P0C673; -.
DR   Bgee; P0C673; -.
DR   CleanEx; MM_IGSF11; -.
DR   Genevestigator; P0C673; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   1: Evidence at protein level;
KW   Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW   Growth regulation; Immunoglobulin domain; Membrane; Phosphoprotein;
KW   Receptor; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     22       Potential.
FT   CHAIN        23    428       Immunoglobulin superfamily member 11.
FT                                /FTId=PRO_0000317371.
FT   TOPO_DOM     23    240       Extracellular (Potential).
FT   TRANSMEM    241    261       Helical; (Potential).
FT   TOPO_DOM    262    428       Cytoplasmic (Potential).
FT   DOMAIN       23    136       Ig-like V-type.
FT   DOMAIN      144    234       Ig-like C2-type.
FT   MOD_RES     334    334       Phosphoserine.
FT   CARBOHYD    102    102       N-linked (GlcNAc...) (Potential).
FT   DISULFID     44    120       By similarity.
FT   DISULFID    165    215       By similarity.
FT   CONFLICT    349    349       A -> P (in Ref. 1; BAC07547).
SQ   SEQUENCE   428 AA;  46067 MW;  64A45D8C6A0258CE CRC64;
     MTRRRSAPAS WLLVSLLGVA TSLEVSESPG SVQVARGQTA VLPCAFSTSA ALLNLNVIWM
     VIPLSNANQP EQVILYQGGQ MFDGALRFHG RVGFTGTMPA TNVSIFINNT QLSDTGTYQC
     LVNNLPDRGG RNIGVTGLTV LVPPSAPQCQ IQGSQDLGSD VILLCSSEEG IPRPTYLWEK
     LDNTLKLPPT ATQDQVQGTV TIRNISALSS GLYQCVASNA IGTSTCLLDL QVISPQPRSV
     GVIAGAVGTG AVLIVICLAL ISGAFFYWRS KNKEEEEEEI PNEIREDDLP PKCSSAKAFH
     TEISSSENNT LTSSNTYNSR YWNNNPKPHR NTESFNHFSD LRQSFSGNAV IPSIYANGNH
     LVLGPHKTLV VTANRGSSPQ VLPRNNGSVS RKPWPQHTHS YTVSQMTLER IGAVPVMVPA
     QSRAGSLV
//
ID   WIPF3_MOUSE             Reviewed;         485 AA.
AC   P0C7L0;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   08-MAR-2011, entry version 18.
DE   RecName: Full=WAS/WASL-interacting protein family member 3;
DE   AltName: Full=Corticosteroids and regional expression protein 16 homolog;
GN   Name=Wipf3; Synonyms=Cr16;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP   LOCATION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=17573773; DOI=10.1111/j.1365-2443.2007.01088.x;
RA   Suetsugu S., Banzai Y., Kato M., Fukami K., Kataoka Y., Takai Y.,
RA   Yoshida N., Takenawa T.;
RT   "Male-specific sterility caused by the loss of CR16.";
RL   Genes Cells 12:721-733(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-68 AND 203-485.
RC   TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be a regulator of cytoskeletal organization
CC       (Potential). May have a role in spermatogenesis.
CC   -!- SUBUNIT: Interacts with WASL, and monomeric and filamentous actin
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=In hippocampal neurons
CC       colocalizes with WASL in the cell body, axons and the growth cone
CC       (By similarity). Localizes to the actin filaments at the Sertoli
CC       cell-spermatid junctions.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P0C7L0-1; Sequence=Displayed;
CC       Name=2; Synonyms=deltains;
CC         IsoId=P0C7L0-2; Sequence=VSP_034030;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is expressed in brain and testis and
CC       isoform 2 is expressed only in brain (at protein level).
CC   -!- DOMAIN: The WH2 domain is found in a number of putative actin-
CC       binding proteins (By similarity).
CC   -!- DOMAIN: The profilin-binding motif has been implicated in the
CC       interaction with profilin and SH3 domains (By similarity).
CC   -!- DOMAIN: The KLKR motif is essential for G-actin binding and for
CC       actin polymerization (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice are normal but males are sterile due to
CC       defects in spermatogenesis.
CC   -!- SIMILARITY: Contains 1 WH2 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CB723002; Type=Frameshift; Positions=621;
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DR   EMBL; AC087841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BQ952480; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; CB723002; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00606892; -.
DR   IPI; IPI00849730; -.
DR   UniGene; Mm.434326; -.
DR   ProteinModelPortal; P0C7L0; -.
DR   SMR; P0C7L0; 419-458.
DR   PRIDE; P0C7L0; -.
DR   Ensembl; ENSMUST00000132855; ENSMUSP00000120240; ENSMUSG00000086040.
DR   MGI; MGI:3044681; Wipf3.
DR   eggNOG; roNOG17025; -.
DR   GeneTree; ENSGT00580000081291; -.
DR   HOVERGEN; HBG108677; -.
DR   OrthoDB; EOG4DZ1WB; -.
DR   Bgee; P0C7L0; -.
DR   Genevestigator; P0C7L0; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR003124; WH2_actin-bd.
DR   Pfam; PF02205; WH2; 1.
DR   SMART; SM00246; WH2; 1.
DR   PROSITE; PS51082; WH2; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Cytoplasm; Developmental protein;
KW   Differentiation; Spermatogenesis.
FT   CHAIN         1    485       WAS/WASL-interacting protein family
FT                                member 3.
FT                                /FTId=PRO_0000337998.
FT   DOMAIN       56     73       WH2.
FT   MOTIF         3      8       Profilin-binding motif.
FT   MOTIF        11     16       Profilin-binding motif.
FT   MOTIF        31     36       Profilin-binding motif.
FT   MOTIF        69     72       RLRK.
FT   MOTIF       424    448       WASP-binding motif.
FT   COMPBIAS    184    201       Poly-Pro.
FT   COMPBIAS    232    246       Poly-Pro.
FT   COMPBIAS    296    312       Poly-Pro.
FT   VAR_SEQ     417    451       DDFESKFTFHSMEDFPPPDEYKPCQKIYPSKVPRS -> G
FT                                (in isoform 2).
FT                                /FTId=VSP_034030.
FT   CONFLICT    482    482       L -> LPV (in Ref. 1).
SQ   SEQUENCE   485 AA;  49453 MW;  1ACA37E855D40447 CRC64;
     MPVPPPPPPP PPPPPPPPPP LGAPPPPPLG APPPPPPPGP PVSTDTPSLR KPDLKGRSAL
     LADIQQGTRL RKVTQINDRS APQIEGSKGT SKEGGAAGSN ARGGNTPPAL GDLFAGGFPV
     LRPAGQRDVS GGKSGQGPGS RAPSPRLPIK AISGPLPAPA SPRLGNASET HSSARPVPPR
     PSVPAPPPPT PPPPPPPPLP PASPIKAQLV SPPAPPTKVN PSVVPPPLPC APPLPPPPPT
     PPPLPPASAL SDKAVRPQLA PLHLPPIPPP LPLLPPCGYP GLHSEPNSPA QEVREPPAPP
     PPPPPPPPPP LPTYASCSSR TAVAPPPLPG ANNSGSETPP PLPPKSPSFQ TQKALPTPPG
     APGPQAILQK KRRGPGTSGG KLNPPPAPPA RSPTTELSSK SQQPGGQLRN GGQHAIDDFE
     SKFTFHSMED FPPPDEYKPC QKIYPSKVPR SRTPGSWLQA EAAGQSSDDI KSRNSQLSLK
     ALPVR
//
ID   CLC2L_MOUSE             Reviewed;         211 AA.
AC   P0C7M9;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   08-MAR-2011, entry version 22.
DE   RecName: Full=C-type lectin domain family 2 member L;
GN   Name=Clec2l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Contains 1 C-type lectin domain.
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DR   EMBL; AC161147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00666094; -.
DR   RefSeq; NP_001094977.1; NM_001101507.1.
DR   UniGene; Mm.349066; -.
DR   ProteinModelPortal; P0C7M9; -.
DR   SMR; P0C7M9; 95-209.
DR   PRIDE; P0C7M9; -.
DR   Ensembl; ENSMUST00000114874; ENSMUSP00000110524; ENSMUSG00000079598.
DR   GeneID; 665180; -.
DR   KEGG; mmu:665180; -.
DR   CTD; 665180; -.
DR   MGI; MGI:2141402; Clec2l.
DR   GeneTree; ENSGT00550000074413; -.
DR   HOGENOM; HBG403165; -.
DR   HOVERGEN; HBG107719; -.
DR   InParanoid; P0C7M9; -.
DR   OrthoDB; EOG44QT20; -.
DR   NextBio; 426842; -.
DR   ArrayExpress; P0C7M9; -.
DR   Bgee; P0C7M9; -.
DR   Genevestigator; P0C7M9; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005529; F:sugar binding; IEA:UniProtKB-KW.
DR   InterPro; IPR001304; C-type_lectin.
DR   InterPro; IPR016186; C-type_lectin-like.
DR   InterPro; IPR016187; C-type_lectin_fold.
DR   Gene3D; G3DSA:3.10.100.10; C-type_lectin-like; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; C-type_lectin_fold; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Lectin; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    211       C-type lectin domain family 2 member L.
FT                                /FTId=PRO_0000339386.
FT   TRANSMEM     66     86       Helical; (Potential).
FT   DOMAIN      104    206       C-type lectin.
FT   COMPBIAS      3     30       Pro-rich.
FT   DISULFID    125    205       By similarity.
FT   DISULFID    184    197       By similarity.
SQ   SEQUENCE   211 AA;  23653 MW;  147B5192E87612DA CRC64;
     MEPAREPPAR ARPPPPAARP APAAPRPRSP AEAEARGPEG LLRRSGSGYE GSTSWKAALE
     DTTTRLLLGA IAVLLFAILV VMSILASKGC IKCETPCPED WLLYGRKCYY FSEEPRDWNT
     GRQYCHTHEA ALAVIQSQKE LEFMFKFTRR EPWIGLRRVG DDFHWVNGDP FDPDTFTISG
     MGECVFVEPT RLVSTECLTT RPWVCSKMAY T
//
ID   EF1A1_MOUSE             Reviewed;         462 AA.
AC   P10126; Q61511; Q6ZWN2; Q8BMB8; Q8BVS8; Q99KU5;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 3.
DT   08-MAR-2011, entry version 125.
DE   RecName: Full=Elongation factor 1-alpha 1;
DE            Short=EF-1-alpha-1;
DE   AltName: Full=Elongation factor Tu;
DE            Short=EF-Tu;
DE   AltName: Full=Eukaryotic elongation factor 1 A-1;
DE            Short=eEF1A-1;
GN   Name=Eef1a1; Synonyms=Eef1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=89108007; PubMed=3215517; DOI=10.1016/0378-1119(88)90195-3;
RA   Reddy N.S., Roth W.W., Bragg P.W., Wahba A.J.;
RT   "Isolation and mapping of a gene for protein synthesis initiation
RT   factor 4A and its expression during differentiation of murine
RT   erythroleukemia cells.";
RL   Gene 70:231-243(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=89098401; PubMed=2911475; DOI=10.1093/nar/17.1.442;
RA   Lu X., Werner D.;
RT   "The complete cDNA sequence of mouse elongation factor 1 alpha (EF 1
RT   alpha) mRNA.";
RL   Nucleic Acids Res. 17:442-442(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, Testis, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-108.
RX   MEDLINE=88122115; PubMed=3481036;
RA   Roth W.W., Bragg P.W., Corrias M.V., Reddy N.S., Dholakia J.N.,
RA   Wahba A.J.;
RT   "Expression of a gene for mouse eucaryotic elongation factor Tu during
RT   murine erythroleukemic cell differentiation.";
RL   Mol. Cell. Biol. 7:3929-3936(1987).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-94.
RX   MEDLINE=86176739; PubMed=3960725; DOI=10.1093/nar/14.5.2409;
RA   Rao T.R., Slobin L.I.;
RT   "Structure of the amino-terminal end of mammalian elongation factor
RT   Tu.";
RL   Nucleic Acids Res. 14:2409-2409(1986).
RN   [7]
RP   PROTEIN SEQUENCE OF 6-30; 85-96; 135-146; 155-165; 248-290 AND
RP   431-439, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [8]
RP   PROTEIN SEQUENCE OF 291-313 AND 372-376, AND ETHANOLAMINYLATION AT
RP   GLU-301 AND GLU-374.
RX   MEDLINE=89340549; PubMed=2569467;
RA   Whiteheart S.W., Shenbagarmurthi P., Chen L., Cotter R.J., Hart G.W.;
RT   "Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally
RT   modified by novel amide-linked ethanolamine-phosphoglycerol moieties.
RT   Addition of ethanolamine-phosphoglycerol to specific glutamic acid
RT   residues on EF-1 alpha.";
RL   J. Biol. Chem. 264:14334-14341(1989).
RN   [9]
RP   ISGYLATION.
RX   PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA   Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA   Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT   "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT   human cells.";
RL   Biochem. Biophys. Res. Commun. 336:496-506(2005).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC       aminoacyl-tRNA to the A-site of ribosomes during protein
CC       biosynthesis.
CC   -!- SUBUNIT: Found in a nuclear export complex with XPO5, EEF1A1, Ran
CC       and aminoacylated tRNA. Interacts with XPO5 and KARS (By
CC       similarity). May interact with ERGIC2 (By similarity).
CC   -!- INTERACTION:
CC       Q01105:SET (xeno); NbExp=1; IntAct=EBI-773865, EBI-1053182;
CC       Q01534:TSPY1 (xeno); NbExp=4; IntAct=EBI-773865, EBI-1973142;
CC       Q9H2G4:TSPYL2 (xeno); NbExp=1; IntAct=EBI-773865, EBI-947459;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: ISGylated.
CC   -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC       EF-Tu/EF-1A subfamily.
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DR   EMBL; M22432; AAA50406.1; -; mRNA.
DR   EMBL; X13661; CAA31957.1; -; mRNA.
DR   EMBL; AK032914; BAC28085.1; -; mRNA.
DR   EMBL; AK076696; BAC36446.1; -; mRNA.
DR   EMBL; AK081725; BAC38311.1; -; mRNA.
DR   EMBL; AK083361; BAC38884.1; -; mRNA.
DR   EMBL; BC004005; AAH04005.1; -; mRNA.
DR   EMBL; BC004067; AAH04067.1; -; mRNA.
DR   EMBL; BC005660; AAH05660.1; -; mRNA.
DR   EMBL; BC018223; AAH18223.1; -; mRNA.
DR   EMBL; BC018485; AAH18485.1; -; mRNA.
DR   EMBL; BC083069; AAH83069.1; -; mRNA.
DR   EMBL; M17878; AAA37538.1; -; Genomic_DNA.
DR   EMBL; X03688; CAA27324.1; -; mRNA.
DR   IPI; IPI00307837; -.
DR   PIR; S02114; EFMS1.
DR   RefSeq; NP_034236.2; NM_010106.2.
DR   UniGene; Mm.138471; -.
DR   UniGene; Mm.335315; -.
DR   UniGene; Mm.360075; -.
DR   UniGene; Mm.391071; -.
DR   UniGene; Mm.468942; -.
DR   UniGene; Mm.478264; -.
DR   ProteinModelPortal; P10126; -.
DR   SMR; P10126; 2-443.
DR   IntAct; P10126; 14.
DR   STRING; P10126; -.
DR   PhosphoSite; P10126; -.
DR   SWISS-2DPAGE; P10126; -.
DR   PRIDE; P10126; -.
DR   Ensembl; ENSMUST00000042235; ENSMUSP00000042457; ENSMUSG00000037742.
DR   GeneID; 13627; -.
DR   KEGG; mmu:13627; -.
DR   UCSC; uc009qun.1; mouse.
DR   CTD; 13627; -.
DR   MGI; MGI:1096881; Eef1a1.
DR   eggNOG; roNOG10172; -.
DR   HOGENOM; HBG307581; -.
DR   HOVERGEN; HBG000179; -.
DR   InParanoid; P10126; -.
DR   OMA; SIETHHM; -.
DR   OrthoDB; EOG40K7ZP; -.
DR   PhylomeDB; P10126; -.
DR   NextBio; 284304; -.
DR   Bgee; P10126; -.
DR   Genevestigator; P10126; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000795; ProtSyn_GTP-bd.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR   InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   InterPro; IPR009000; Transl_elong_init/rib_B-barrel.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50465; Elong_init_C; 1.
DR   SUPFAM; SSF50447; Translat_factor; 1.
DR   TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR   PROSITE; PS00301; EFACTOR_GTP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Elongation factor;
KW   GTP-binding; Methylation; Nucleotide-binding; Phosphoprotein;
KW   Protein biosynthesis; Ubl conjugation.
FT   CHAIN         1    462       Elongation factor 1-alpha 1.
FT                                /FTId=PRO_0000090886.
FT   NP_BIND      14     21       GTP (By similarity).
FT   NP_BIND      91     95       GTP (By similarity).
FT   NP_BIND     153    156       GTP (By similarity).
FT   MOD_RES      29     29       Phosphotyrosine (By similarity).
FT   MOD_RES      36     36       N6,N6,N6-trimethyllysine (By similarity).
FT   MOD_RES      41     41       N6-acetyllysine (By similarity).
FT   MOD_RES      44     44       N6-acetyllysine (By similarity).
FT   MOD_RES      55     55       N6,N6-dimethyllysine (By similarity).
FT   MOD_RES      55     55       N6-acetyllysine (By similarity).
FT   MOD_RES      79     79       N6,N6,N6-trimethyllysine (By similarity).
FT   MOD_RES      86     86       Phosphotyrosine (By similarity).
FT   MOD_RES     141    141       Phosphotyrosine (By similarity).
FT   MOD_RES     146    146       N6-acetyllysine (By similarity).
FT   MOD_RES     162    162       Phosphotyrosine (By similarity).
FT   MOD_RES     165    165       N6,N6-dimethyllysine (By similarity).
FT   MOD_RES     172    172       N6-acetyllysine (By similarity).
FT   MOD_RES     179    179       N6-acetyllysine (By similarity).
FT   MOD_RES     255    255       N6-acetyllysine (By similarity).
FT   MOD_RES     301    301       5-glutamyl
FT                                glycerylphosphorylethanolamine.
FT   MOD_RES     318    318       N6,N6,N6-trimethyllysine; alternate (By
FT                                similarity).
FT   MOD_RES     318    318       N6-acetyllysine; alternate (By
FT                                similarity).
FT   MOD_RES     374    374       5-glutamyl
FT                                glycerylphosphorylethanolamine.
FT   MOD_RES     392    392       N6-acetyllysine (By similarity).
FT   MOD_RES     395    395       N6-acetyllysine (By similarity).
FT   MOD_RES     439    439       N6-acetyllysine (By similarity).
FT   CONFLICT      7      7       H -> R (in Ref. 5; AAA37538).
FT   CONFLICT     15     15       H -> L (in Ref. 5; AAA37538).
FT   CONFLICT     23     23       T -> S (in Ref. 5; AAA37538).
FT   CONFLICT     77     78       LW -> QR (in Ref. 2; CAA31957).
FT   CONFLICT     83     83       S -> A (in Ref. 6; CAA27324).
FT   CONFLICT     91     92       DA -> ES (in Ref. 2; CAA31957).
FT   CONFLICT    108    108       Q -> R (in Ref. 5; AAA37538).
FT   CONFLICT    156    156       D -> G (in Ref. 3; BAC28085).
FT   CONFLICT    222    222       S -> H (in Ref. 1; AAA50406).
FT   CONFLICT    224    226       SGT -> VAP (in Ref. 2; CAA31957).
FT   CONFLICT    225    225       G -> D (in Ref. 4; AAH04005).
FT   CONFLICT    239    239       Missing (in Ref. 2; CAA31957).
FT   CONFLICT    350    350       P -> T (in Ref. 3; BAC36446).
SQ   SEQUENCE   462 AA;  50114 MW;  71072871DE7405DC CRC64;
     MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL
     DKLKAERERG ITIDISLWKF ETSKYYVTII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV
     GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP PYSQKRYEEI VKEVSTYIKK
     IGYNPDTVAF VPISGWNGDN MLEPSANMPW FKGWKVTRKD GSASGTTLLE ALDCILPPTR
     PTDKPLRLPL QDVYKIGGIG TVPVGRVETG VLKPGMVVTF APVNVTTEVK SVEMHHEALS
     EALPGDNVGF NVKNVSVKDV RRGNVAGDSK NDPPMEAAGF TAQVIILNHP GQISAGYAPV
     LDCHTAHIAC KFAELKEKID RRSGKKLEDG PKFLKSGDAA IVDMVPGKPM CVESFSDYPP
     LGRFAVRDMR QTVAVGVIKA VDKKAAGAGK VTKSAQKAQK AK
//
ID   ENV1_MOUSE              Reviewed;         641 AA.
AC   P10404; Q78N71; Q78N73; Q78N94; Q80SW7; Q80SW8; Q80SY0; Q80SY1;
AC   Q811M9; Q811N4;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 3.
DT   08-FEB-2011, entry version 78.
DE   RecName: Full=MLV-related proviral Env polyprotein;
DE   Contains:
DE     RecName: Full=Surface protein;
DE              Short=SU;
DE   Contains:
DE     RecName: Full=Transmembrane protein;
DE              Short=TM;
DE   Flags: Precursor;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NFS;
RX   MEDLINE=22850800; PubMed=12970417;
RX   DOI=10.1128/JVI.77.19.10327-10338.2003;
RA   Evans L.H., Lavignon M., Taylor M., Alamgir A.S.;
RT   "Antigenic subclasses of polytropic murine leukemia virus (MLV)
RT   isolates reflect three distinct groups of endogenous polytropic MLV-
RT   related sequences in NFS/N mice.";
RL   J. Virol. 77:10327-10338(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-313.
RC   STRAIN=129;
RX   MEDLINE=86062897; PubMed=2415714;
RA   Levy D.E., Lerner R.A., Wilson M.C.;
RT   "Normal expression of polymorphic endogenous retroviral RNA containing
RT   segments identical to mink cell focus-forming virus.";
RL   J. Virol. 56:691-700(1985).
CC   -!- FUNCTION: The surface protein (SU) attaches the virus to the host
CC       cell by binding to its receptor. This interaction triggers the
CC       refolding of the transmembrane protein (TM) and is thought to
CC       activate its fusogenic potential by unmasking its fusion peptide.
CC       Fusion occurs at the host cell plasma membrane (By similarity).
CC   -!- FUNCTION: The transmembrane protein (TM) acts as a class I viral
CC       fusion protein. Under the current model, the protein has at least
CC       3 conformational states: pre-fusion native state, pre-hairpin
CC       intermediate state, and post-fusion hairpin state. During viral
CC       and target cell membrane fusion, the coiled coil regions (heptad
CC       repeats) assume a trimer-of-hairpins structure, positioning the
CC       fusion peptide in close proximity to the C-terminal region of the
CC       ectodomain. The formation of this structure appears to drive
CC       apposition and subsequent fusion of viral and target cell
CC       membranes. Membranes fusion leads to delivery of the nucleocapsid
CC       into the cytoplasm (By similarity).
CC   -!- SUBUNIT: The mature envelope protein (Env) consists of a trimer of
CC       SU-TM heterodimers attached by a labile interchain disulfide bond
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Transmembrane protein: Virion membrane;
CC       Single-pass type I membrane protein. Cell membrane; Single-pass
CC       type I membrane protein. Note=The surface protein is not anchored
CC       to the viral envelope, but associates with the extravirion surface
CC       through its binding to TM. Both proteins are thought to be
CC       concentrated at the site of budding and incorporated into the
CC       virions possibly by contacts between the cytoplasmic tail of Env
CC       and the N-terminus of Gag. R-peptide: Cell membrane; peripheral
CC       membrane protein. The R-peptide is membrane-associated through its
CC       palmitate (By similarity).
CC   -!- SUBCELLULAR LOCATION: Surface protein: Virion membrane; Peripheral
CC       membrane protein. Cell membrane; Peripheral membrane protein.
CC       Note=The surface protein is not anchored to the viral envelope,
CC       but associates with the extravirion surface through its binding to
CC       TM. Both proteins are thought to be concentrated at the site of
CC       budding and incorporated into the virions possibly by contacts
CC       between the cytoplasmic tail of Env and the N-terminus of Gag. R-
CC       peptide: Cell membrane; peripheral membrane protein. The R-peptide
CC       is membrane-associated through its palmitate (By similarity).
CC   -!- DOMAIN: The YXXL motif is involved in determining the exact site
CC       of viral release at the surface of infected mononuclear cells and
CC       promotes endocytosis.
CC   -!- DOMAIN: The 17 amino acids long immunosuppressive region is
CC       present in many retroviral envelope proteins. Synthetic peptides
CC       derived from this relatively conserved sequence inhibit immune
CC       function in vitro and in vivo (By similarity).
CC   -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
CC       Envelope glycoproteins are synthesized as a inactive precursor
CC       that is N-glycosylated and processed likely by host cell furin or
CC       by a furin-like protease in the Golgi to yield the mature SU and
CC       TM proteins. The cleavage site between SU and TM requires the
CC       minimal sequence [KR]-X-[KR]-R. The R-peptide is released from the
CC       C-terminus of the cytoplasmic tail of the TM protein upon particle
CC       formation as a result of proteolytic cleavage by the viral
CC       protease. Cleavage of this peptide is required for TM to become
CC       fusogenic (By similarity).
CC   -!- PTM: The CXXC motif is highly conserved across a broad range of
CC       retroviral envelope proteins. It is thought to participate in the
CC       formation of a labile disulfide bond possibly with the CX6CC motif
CC       present in the transmembrane protein. Isomerization of the
CC       intersubunit disulfide bond to an SU intrachain disulfide bond is
CC       thought to occur upon receptor recognition in order to allow
CC       membrane fusion (By similarity).
CC   -!- PTM: The transmembrane protein is palmitoylated (By similarity).
CC   -!- PTM: The R-peptide is palmitoylated (By similarity).
CC   -!- CAUTION: This polyprotein is encoded by an endogenous retrovirus
CC       expressed in some mouse strains. Multiple sequences are present in
CC       different regions of the genome, probably reflecting the different
CC       sites of integration of the exogenous retrovirus.
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DR   EMBL; AY219544; AAO37244.2; -; Genomic_DNA.
DR   EMBL; AY219545; AAO37246.2; -; Genomic_DNA.
DR   EMBL; AY219546; AAO37248.2; -; Genomic_DNA.
DR   EMBL; AY219547; AAO37250.2; -; Genomic_DNA.
DR   EMBL; AY219548; AAO37252.2; -; Genomic_DNA.
DR   EMBL; AY219550; AAO37255.2; -; Genomic_DNA.
DR   EMBL; AY219551; AAO37257.2; -; Genomic_DNA.
DR   EMBL; AY219554; AAO37261.2; -; Genomic_DNA.
DR   EMBL; AY219557; AAO37265.2; -; Genomic_DNA.
DR   EMBL; AY219558; AAO37267.2; -; Genomic_DNA.
DR   EMBL; AY219564; AAO37279.2; -; Genomic_DNA.
DR   EMBL; AY219566; AAO37283.2; -; Genomic_DNA.
DR   EMBL; AY219567; AAO37285.2; -; Genomic_DNA.
DR   EMBL; M11301; AAA37561.1; -; mRNA.
DR   IPI; IPI00420148; -.
DR   ProteinModelPortal; P10404; -.
DR   SMR; P10404; 38-230, 486-538.
DR   PRIDE; P10404; -.
DR   MGI; MGI:3642579; ENSMUSG00000075231.
DR   HOVERGEN; HBG008112; -.
DR   Genevestigator; P10404; -.
DR   GermOnline; ENSMUSG00000075231; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019028; C:viral capsid; IEA:InterPro.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0019058; P:viral infectious cycle; IEA:InterPro.
DR   InterPro; IPR008981; FMuLV_rcpt-bd.
DR   InterPro; IPR018154; TLV/ENV_coat_polyprotein.
DR   Gene3D; G3DSA:3.90.310.10; FMuLV_rcpt_bd; 1.
DR   Pfam; PF00429; TLV_coat; 2.
DR   SUPFAM; SSF49830; FMuLVrecept-bind; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cleavage on pair of basic residues; Coiled coil;
KW   Disulfide bond; Glycoprotein; Lipoprotein; Membrane; Metal-binding;
KW   Palmitate; Polymorphism; Signal; Transmembrane; Transmembrane helix;
KW   Viral envelope protein; Virion; Zinc.
FT   SIGNAL        1     32       Potential.
FT   CHAIN        33    440       Surface protein (By similarity).
FT                                /FTId=PRO_0000021186.
FT   CHAIN       441    641       Transmembrane protein (By similarity).
FT                                /FTId=PRO_0000295257.
FT   TOPO_DOM     33    581       Extracellular (Potential).
FT   TRANSMEM    582    602       Helical; (Potential).
FT   TOPO_DOM    603    641       Cytoplasmic (Potential).
FT   REGION      443    463       Fusion peptide (By similarity).
FT   REGION      509    525       Immunosuppression (By similarity).
FT   COILED      471    520       Potential.
FT   COILED      530    566       Potential.
FT   MOTIF       307    310       CXXC (By similarity).
FT   MOTIF       526    534       CX6CC (By similarity).
FT   MOTIF       626    629       YXXL motif; contains endocytosis signal
FT                                (By similarity).
FT   COMPBIAS    230    279       Pro-rich.
FT   SITE        440    441       Cleavage (By similarity).
FT   LIPID       601    601       S-palmitoyl cysteine (By similarity).
FT   CARBOHYD     43     43       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     58     58       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    297    297       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    336    336       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    369    369       N-linked (GlcNAc...) (Potential).
FT   DISULFID    109    126       By similarity.
FT   DISULFID    118    131       By similarity.
FT   DISULFID    307    534       Interchain (between SU and TM chains, or
FT                                C-337 with C-558); alternate (By
FT                                similarity).
FT   DISULFID    307    310       Alternate (By similarity).
FT   DISULFID    337    391       By similarity.
FT   DISULFID    356    368       By similarity.
FT   DISULFID    398    411       By similarity.
FT   DISULFID    526    533       By similarity.
FT   VARIANT      22     22       V -> I.
FT   VARIANT      24     24       G -> R.
FT   VARIANT     153    153       R -> G.
FT   VARIANT     157    157       Q -> R.
FT   VARIANT     268    268       I -> T.
FT   VARIANT     280    280       G -> E.
FT   VARIANT     339    339       V -> A.
FT   VARIANT     349    349       E -> K.
FT   VARIANT     358    358       G -> R.
FT   VARIANT     434    434       R -> K.
FT   VARIANT     458    458       G -> D.
FT   VARIANT     491    491       E -> K.
FT   VARIANT     514    514       G -> R.
FT   VARIANT     524    524       G -> R.
FT   VARIANT     531    531       E -> K.
FT   VARIANT     546    546       S -> N.
FT   VARIANT     548    548       A -> T.
FT   VARIANT     552    552       E -> K.
FT   VARIANT     636    636       E -> K.
SQ   SEQUENCE   641 AA;  69613 MW;  C39BF1C2F7B4063F CRC64;
     MEGPAFSKPL KDKINPWGPL IVLGILIRAG VSVQHDSPHQ VFNVTWRVTN LMTGQTANAT
     SLLGTMTDAF PKLYFDLCDL IGDDWDETGL GCRTPGGRKR ARTFDFYVCP GHTVPTGCGG
     PREGYCGKWG CETTGQAYWK PSSSWDLISL KRRNTPQNQG PCYDSSAVSS DIKGATPGGR
     CNPLVLEFTD AGKKASWDGP KVWGLRLYRS TGTDPVTRFS LTRQVLNIGP RVPIGPNPVI
     TDQLPPSRPV QIMLPRPPQP PPPGAASIVP ETAPPSQQPG TGDRLLNLVD GAYQALNLTS
     PDKTQECWLC LVAGPPYYEG VAVLGTYSNH TSAPANCSVA SQHKLTLSEV TGQGLCVGAV
     PKTHQALCNT TQKTSDGSYY LAAPAGTIWA CNTGLTPCLS TTVLDLTTDY CVLVELWPKV
     TYHSPGYVYG QFERKTKYKR EPVSLTLALL LGGLTMGGIA AGVGTGTTAL VATKQFEQLQ
     AAIHTDLGAL EKSVSALEKS LTSLSEVVLQ NRRGLDLLFL KEGGLCAALK EECCFYADHT
     GVVRDSMAKL RERLNQRQKL FESGQGWFEG LFNRSPWFTT LISTIMGPLI ILLLILLFGP
     CILNRLVQFV KDRISVVQAL VLTQQYHQLK SIDPEEVESR E
//
ID   HEM2_MOUSE              Reviewed;         330 AA.
AC   P10518; Q3THV6;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Delta-aminolevulinic acid dehydratase;
DE            Short=ALADH;
DE            EC=4.2.1.24;
DE   AltName: Full=Porphobilinogen synthase;
GN   Name=Alad; Synonyms=Lv;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=89160346; PubMed=2922298; DOI=10.1093/nar/17.4.1775;
RA   Bishop T.R., Hodes Z.I., Frelin L.P., Boyer S.H.;
RT   "Cloning and sequence of mouse erythroid delta-aminolevulinate
RT   dehydratase cDNA.";
RL   Nucleic Acids Res. 17:1775-1775(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, C57BL/6J, and DBA/2; TISSUE=Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
RG   RIKEN structural genomics initiative (RSGI);
RT   "Crystal structure of 5-aminolevulinic acid dehydratase (ALAD) from
RT   Mus musculus.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- FUNCTION: Catalyzes an early step in the biosynthesis of
CC       tetrapyrroles. Binds two molecules of 5-aminolevulinate per
CC       subunit, each at a distinct site, and catalyzes their condensation
CC       to form porphobilinogen (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2 5-aminolevulinate = porphobilinogen + 2
CC       H(2)O.
CC   -!- COFACTOR: Binds 8 zinc ions per octamer. Only four zinc ions per
CC       octamer are required for full catalytic activity. Only four zinc
CC       ions per octamer are tightly bound. Can bind 2 zinc ions per
CC       subunit. The first zinc ion is important for catalysis (By
CC       similarity).
CC   -!- ENZYME REGULATION: Can alternate between a fully active
CC       homooctamer and a low-activity homohexamer. A bound magnesium ion
CC       may promote the assembly of the fully active homooctamer. The
CC       magnesium-binding site is absent in the low-activity homohexamer.
CC       Inhibited by compounds that favor the hexameric state. Inhibited
CC       by divalent lead ions. The lead ions partially displace the zinc
CC       cofactor (By similarity).
CC   -!- PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis;
CC       coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
CC   -!- SUBUNIT: Homooctamer; active form. Homohexamer; low activity form
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the ALADH family.
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DR   EMBL; X13752; CAA32015.1; -; mRNA.
DR   EMBL; AK032908; BAC28080.1; -; mRNA.
DR   EMBL; AK167673; BAE39722.1; -; mRNA.
DR   EMBL; AK168119; BAE40090.1; -; mRNA.
DR   EMBL; AK168132; BAE40101.1; -; mRNA.
DR   EMBL; BC055930; AAH55930.1; -; mRNA.
DR   IPI; IPI00112719; -.
DR   PIR; S03187; S03187.
DR   RefSeq; NP_032551.3; NM_008525.3.
DR   UniGene; Mm.6988; -.
DR   PDB; 2Z0I; X-ray; 3.20 A; A/B=1-330.
DR   PDB; 2Z1B; X-ray; 3.30 A; A/B/C/D=1-330.
DR   PDBsum; 2Z0I; -.
DR   PDBsum; 2Z1B; -.
DR   ProteinModelPortal; P10518; -.
DR   SMR; P10518; 5-328.
DR   STRING; P10518; -.
DR   PhosphoSite; P10518; -.
DR   SWISS-2DPAGE; P10518; -.
DR   REPRODUCTION-2DPAGE; P10518; -.
DR   PRIDE; P10518; -.
DR   Ensembl; ENSMUST00000030090; ENSMUSP00000030090; ENSMUSG00000028393.
DR   Ensembl; ENSMUST00000107444; ENSMUSP00000103068; ENSMUSG00000028393.
DR   GeneID; 17025; -.
DR   KEGG; mmu:17025; -.
DR   NMPDR; fig|10090.3.peg.9704; -.
DR   UCSC; uc008tez.1; mouse.
DR   CTD; 17025; -.
DR   MGI; MGI:96853; Alad.
DR   HOGENOM; HBG285270; -.
DR   HOVERGEN; HBG001222; -.
DR   InParanoid; P10518; -.
DR   OMA; PIFVTDV; -.
DR   OrthoDB; EOG4BRWM1; -.
DR   PhylomeDB; P10518; -.
DR   BRENDA; 4.2.1.24; 244.
DR   NextBio; 291138; -.
DR   ArrayExpress; P10518; -.
DR   Bgee; P10518; -.
DR   CleanEx; MM_ALAD; -.
DR   Genevestigator; P10518; -.
DR   GermOnline; ENSMUSG00000028393; Mus musculus.
DR   GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR   GO; GO:0032791; F:lead ion binding; ISS:UniProtKB.
DR   GO; GO:0004655; F:porphobilinogen synthase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0006783; P:heme biosynthetic process; ISS:UniProtKB.
DR   InterPro; IPR001731; 4pyrrol_synth_porphobiln_synth.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   PANTHER; PTHR11458; AlaD_dehydratase; 1.
DR   Pfam; PF00490; ALAD; 1.
DR   PIRSF; PIRSF001415; Porphbilin_synth; 1.
DR   PRINTS; PR00144; DALDHYDRTASE.
DR   PROSITE; PS00169; D_ALA_DEHYDRATASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Allosteric enzyme; Heme biosynthesis; Lyase;
KW   Metal-binding; Porphyrin biosynthesis; Zinc.
FT   CHAIN         1    330       Delta-aminolevulinic acid dehydratase.
FT                                /FTId=PRO_0000140528.
FT   ACT_SITE    199    199       Schiff-base intermediate with substrate
FT                                (By similarity).
FT   ACT_SITE    252    252       Schiff-base intermediate with substrate
FT                                (By similarity).
FT   METAL       122    122       Zinc 1; catalytic (By similarity).
FT   METAL       124    124       Zinc 1; catalytic (By similarity).
FT   METAL       131    131       Zinc 2 (By similarity).
FT   METAL       132    132       Zinc 1; catalytic (By similarity).
FT   METAL       223    223       Zinc 2 (By similarity).
FT   BINDING     209    209       Substrate 1 (By similarity).
FT   BINDING     221    221       Substrate 1 (By similarity).
FT   BINDING     279    279       Substrate 2 (By similarity).
FT   BINDING     318    318       Substrate 2 (By similarity).
FT   HELIX         8     10
FT   HELIX        14     20
FT   HELIX        28     30
FT   STRAND       31     42
FT   STRAND       44     46
FT   STRAND       54     57
FT   HELIX        58     60
FT   HELIX        61     64
FT   HELIX        66     69
FT   TURN         70     72
FT   STRAND       75     81
FT   HELIX       100    111
FT   STRAND      113    119
FT   HELIX       144    160
FT   STRAND      163    165
FT   HELIX       174    183
FT   STRAND      192    194
FT   HELIX       206    211
FT   HELIX       231    241
FT   HELIX       242    244
FT   STRAND      247    254
FT   HELIX       255    257
FT   HELIX       258    267
FT   STRAND      273    276
FT   HELIX       279    290
FT   HELIX       296    309
FT   STRAND      313    316
FT   HELIX       320    326
SQ   SEQUENCE   330 AA;  36024 MW;  84052DC911C153EB CRC64;
     MHHQSVLHSG YFHPLLRSWQ TAASTVSASN LIYPIFVTDV PDDVQPIASL PGVARYGVNQ
     LEEMLRPLVE AGLRCVLIFG VPSRVPKDEQ GSAADSEDSP TIEAVRLLRK TFPSLLVACD
     VCLCPYTSHG HCGLLSENGA FLAEESRQRL AEVALAYAKA GCQVVAPSDM MDGRVEAIKA
     ALLKHGLGNR VSVMSYSAKF ASCFYGPFRD AAQSSPAFGD RRCYQLPPGA RGLALRAVAR
     DIQEGADMLM VKPGLPYLDM VREVKDKHPE LPLAVYQVSG EFAMLWHGAQ AGAFDLRTAV
     LETMTAFRRA GADIIITYFA PQLLKWLKEE
//
ID   TAU_MOUSE               Reviewed;         733 AA.
AC   P10637; A2A5Y9; P10638; Q60684; Q60685; Q60686; Q62286; Q91WK4;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 129.
DE   RecName: Full=Microtubule-associated protein tau;
DE   AltName: Full=Neurofibrillary tangle protein;
DE   AltName: Full=Paired helical filament-tau;
DE            Short=PHF-tau;
GN   Name=Mapt; Synonyms=Mtapt, Tau;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PNS-TAU).
RC   TISSUE=Neuroblastoma;
RX   MEDLINE=92262443; PubMed=1374898; DOI=10.1073/pnas.89.10.4378;
RA   Couchie D., Mavilia C., Georgieff I.S., Liem R.K.H., Shelanski M.L.,
RA   Nunez J.;
RT   "Primary structure of high molecular weight tau present in the
RT   peripheral nervous system.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:4378-4381(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-A; TAU-D AND TAU-E).
RC   STRAIN=Him OF1; TISSUE=Brain, Kidney, and Liver;
RX   MEDLINE=95012085; PubMed=7927211; DOI=10.1002/hep.1840200442;
RA   Kenner L., el-Shabrawi Y., Hutter H., Forstner M., Zatloukal K.,
RA   Hoefler G., Preisegger K.-H., Kurzbauer R., Denk H.;
RT   "Expression of three- and four-repeat tau isoforms in mouse liver.";
RL   Hepatology 20:1086-1089(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS TAU-B AND TAU-C).
RC   TISSUE=Brain;
RX   MEDLINE=88099510; PubMed=3122323; DOI=10.1126/science.3122323;
RA   Lee G., Cowan N.J., Kirschner M.;
RT   "The primary structure and heterogeneity of tau protein from mouse
RT   brain.";
RL   Science 239:285-288(1988).
RN   [4]
RP   PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING
RP   (ISOFORM TAU-B).
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=95182802; PubMed=7877441; DOI=10.1016/0169-328X(94)90191-0;
RA   Sawa A., Oyama F., Matsushita M., Ihara Y.;
RT   "Molecular diversity at the carboxyl terminus of human and rat tau.";
RL   Brain Res. Mol. Brain Res. 27:111-117(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM TAU-D).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 504-513; 535-546; 591-609 AND 646-661, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [8]
RP   CHARACTERIZATION.
RX   MEDLINE=94005827; PubMed=8402267;
RA   Couchie D., Gache Y., Mavilia C., Guilleminot J., Bridoux A.-M.,
RA   Nivez M.-P., Nunez J.;
RT   "High molecular weight tau proteins and acquisition of neuronal
RT   polarity in peripheral nervous system.";
RL   C. R. Acad. Sci. III, Sci. Vie 316:404-409(1993).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696; SER-701; THR-706
RP   AND SER-708, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-490; SER-491; SER-494;
RP   SER-688; SER-692; THR-695; SER-696; SER-704 AND THR-706, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [11]
RP   INTERACTION WITH PSMC2.
RX   PubMed=15953362; DOI=10.1111/j.1471-4159.2005.03181.x;
RA   Babu J.R., Geetha T., Wooten M.W.;
RT   "Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal
RT   degradation.";
RL   J. Neurochem. 94:192-203(2005).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-523 AND SER-527, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-457; SER-490; SER-491;
RP   SER-494; THR-497; SER-688; SER-692; THR-695 AND SER-696, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100; SER-470; THR-473;
RP   TYR-489; SER-494; THR-497; SER-688; SER-692 AND THR-695, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491; SER-688; SER-692
RP   AND SER-696, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-523; SER-688; SER-692
RP   AND SER-701, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Promotes microtubule assembly and stability, and might
CC       be involved in the establishment and maintenance of neuronal
CC       polarity. The C-terminus binds axonal microtubules while the N-
CC       terminus binds neural plasma membrane components, suggesting that
CC       tau functions as a linker protein between both. Axonal polarity is
CC       predetermined by tau localization (in the neuronal cell) in the
CC       domain of the cell body defined by the centrosome. The short
CC       isoforms allow plasticity of the cytoskeleton whereas the longer
CC       isoforms may preferentially play a role in its stabilization.
CC   -!- SUBUNIT: Interacts with SQSTM1 when polyubiquitinated (By
CC       similarity). Interacts with PSMC2 through SQSTM1. Interacts with
CC       FKBP4 (By similarity).
CC   -!- INTERACTION:
CC       P62137:Ppp1ca; NbExp=1; IntAct=EBI-774043, EBI-357187;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane;
CC       Peripheral membrane protein; Cytoplasmic side. Cytoplasm,
CC       cytoskeleton. Cell projection, axon. Note=Mostly found in the
CC       axons of neurons, in the cytosol and in association with plasma
CC       membrane components.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC         Comment=Additional isoforms seem to exist. Isoforms differ from
CC         each other by the presence or absence of up to 5 of the 14
CC         exons. One of these optional exons contains the additional
CC         tau/MAP repeat. Two different C-termini are obtained either by
CC         the retention or the splicing of intron 13/14;
CC       Name=PNS-Tau;
CC         IsoId=P10637-1; Sequence=Displayed;
CC       Name=Tau-A;
CC         IsoId=P10637-2; Sequence=VSP_003187, VSP_003188;
CC       Name=Tau-B;
CC         IsoId=P10637-3; Sequence=VSP_003185, VSP_003187, VSP_003188,
CC                                  VSP_003189, VSP_003190;
CC       Name=Tau-C;
CC         IsoId=P10637-4; Sequence=VSP_003185, VSP_003187, VSP_003188,
CC                                  VSP_003189;
CC       Name=Tau-D;
CC         IsoId=P10637-5; Sequence=VSP_003185, VSP_003187, VSP_003188;
CC       Name=Tau-E;
CC         IsoId=P10637-6; Sequence=VSP_003185, VSP_003186, VSP_003187,
CC                                  VSP_003188;
CC   -!- TISSUE SPECIFICITY: Expressed in neurons and at a lower level in
CC       the liver and kidney. Isoform PNS-tau is expressed in the
CC       peripheral nervous system while the others are expressed in the
CC       central nervous system.
CC   -!- DEVELOPMENTAL STAGE: Shorter forms or low molecular weight tau
CC       (lMW-tau) are generally expressed at early development stages and
CC       longer forms or high molecular weight tau (hMW-tau) in the adult
CC       brain.
CC   -!- DOMAIN: The tau/MAP repeat binds to tubulin. Type I isoforms
CC       contain 3 repeats while type II isoforms contain 4 repeats.
CC   -!- PTM: Polyubiquitinated. Requires functional TRAF6 and may provoke
CC       SQSTM1-dependent degradation by the proteasome (By similarity).
CC   -!- PTM: Phosphorylation at various serine and threonine residues in
CC       S-P or T-P motifs by proline-directed protein kinases (PDPK: CDK1,
CC       CDK5, GSK3, MAPK) (a few sites per protein in interphase, more in
CC       mitosis), and at serine residues in K-X-G-S motifs by
CC       MAP/microtubule affinity-regulating kinase (MARK) (By similarity).
CC   -!- DISEASE: Note=May be involved in the pathogenesis of cytoplasmic
CC       inclusions (as Mallory bodies) in livers of mice chronically
CC       intoxicated with Griseofulvin or DDC (3,5-diethoxycarbonyl-2,4-
CC       dihydrocollidine), a model for human alcoholic hepatitis.
CC       Alteration of Tau (abnormal phosphorylation and cross-linking)
CC       could contribute to Mallory bodies formation and disturbance of
CC       microtubule function in alcoholic liver disease.
CC   -!- SIMILARITY: Contains 4 Tau/MAP repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; U12914; AAA58343.1; -; mRNA.
DR   EMBL; U12915; AAA58344.1; -; mRNA.
DR   EMBL; U12916; AAA58345.1; -; mRNA.
DR   EMBL; Z12133; CAA78121.1; -; mRNA.
DR   EMBL; M93266; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; M18775; AAA40165.1; -; mRNA.
DR   EMBL; M18776; AAA40166.1; -; mRNA.
DR   EMBL; D30627; BAA18878.1; -; Genomic_DNA.
DR   EMBL; AL593843; CAM14797.1; -; Genomic_DNA.
DR   EMBL; BC014748; AAH14748.1; -; mRNA.
DR   IPI; IPI00230408; -.
DR   IPI; IPI00331265; -.
DR   IPI; IPI00407807; -.
DR   IPI; IPI00465469; -.
DR   IPI; IPI00468678; -.
DR   IPI; IPI00649104; -.
DR   PIR; A28820; A28820.
DR   PIR; A45301; A45301.
DR   PIR; B28820; B28820.
DR   RefSeq; NP_001033698.1; NM_001038609.1.
DR   RefSeq; NP_034968.3; NM_010838.3.
DR   UniGene; Mm.1287; -.
DR   IntAct; P10637; 2.
DR   MINT; MINT-3974107; -.
DR   STRING; P10637; -.
DR   PhosphoSite; P10637; -.
DR   PRIDE; P10637; -.
DR   Ensembl; ENSMUST00000100347; ENSMUSP00000097919; ENSMUSG00000018411.
DR   Ensembl; ENSMUST00000106988; ENSMUSP00000102601; ENSMUSG00000018411.
DR   Ensembl; ENSMUST00000106991; ENSMUSP00000102604; ENSMUSG00000018411.
DR   Ensembl; ENSMUST00000106992; ENSMUSP00000102605; ENSMUSG00000018411.
DR   Ensembl; ENSMUST00000106995; ENSMUSP00000102608; ENSMUSG00000018411.
DR   GeneID; 17762; -.
DR   KEGG; mmu:17762; -.
DR   UCSC; uc007lwf.1; mouse.
DR   UCSC; uc007lwg.1; mouse.
DR   UCSC; uc007lwi.1; mouse.
DR   CTD; 17762; -.
DR   MGI; MGI:97180; Mapt.
DR   eggNOG; roNOG13096; -.
DR   GeneTree; ENSGT00530000063491; -.
DR   HOVERGEN; HBG000991; -.
DR   OrthoDB; EOG4B8JDC; -.
DR   NextBio; 292453; -.
DR   ArrayExpress; P10637; -.
DR   Bgee; P10637; -.
DR   CleanEx; MM_MAPT; -.
DR   Genevestigator; P10637; -.
DR   GermOnline; ENSMUSG00000018411; Mus musculus.
DR   GO; GO:0030424; C:axon; ISS:UniProtKB.
DR   GO; GO:0035085; C:cilium axoneme; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0045298; C:tubulin complex; ISS:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:InterPro.
DR   GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB.
DR   GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:UniProtKB.
DR   InterPro; IPR002955; Tau_protein.
DR   InterPro; IPR001084; Tau_tubulin-bd.
DR   Pfam; PF00418; Tubulin-binding; 4.
DR   PRINTS; PR01261; TAUPROTEIN.
DR   PROSITE; PS00229; TAU_MAP_1; 4.
DR   PROSITE; PS51491; TAU_MAP_2; 4.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell membrane; Cell projection;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; Disulfide bond;
KW   Membrane; Microtubule; Phosphoprotein; Repeat; Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    733       Microtubule-associated protein tau.
FT                                /FTId=PRO_0000072742.
FT   REPEAT      536    566       Tau/MAP 1.
FT   REPEAT      567    597       Tau/MAP 2.
FT   REPEAT      598    628       Tau/MAP 3.
FT   REPEAT      629    660       Tau/MAP 4.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      35     35       Phosphoserine (By similarity).
FT   MOD_RES     100    100       Phosphothreonine.
FT   MOD_RES     445    445       Phosphothreonine (By similarity).
FT   MOD_RES     457    457       Phosphothreonine.
FT   MOD_RES     467    467       Phosphothreonine (By similarity).
FT   MOD_RES     470    470       Phosphoserine.
FT   MOD_RES     473    473       Phosphothreonine.
FT   MOD_RES     489    489       Phosphotyrosine.
FT   MOD_RES     490    490       Phosphoserine.
FT   MOD_RES     491    491       Phosphoserine.
FT   MOD_RES     494    494       Phosphoserine.
FT   MOD_RES     497    497       Phosphothreonine.
FT   MOD_RES     504    504       Phosphothreonine (By similarity).
FT   MOD_RES     506    506       Phosphoserine (By similarity).
FT   MOD_RES     509    509       Phosphothreonine (By similarity).
FT   MOD_RES     523    523       Phosphothreonine.
FT   MOD_RES     527    527       Phosphoserine.
FT   MOD_RES     554    554       Phosphoserine (By similarity).
FT   MOD_RES     688    688       Phosphoserine.
FT   MOD_RES     692    692       Phosphoserine.
FT   MOD_RES     695    695       Phosphothreonine.
FT   MOD_RES     696    696       Phosphoserine.
FT   MOD_RES     701    701       Phosphoserine.
FT   MOD_RES     704    704       Phosphoserine.
FT   MOD_RES     706    706       Phosphothreonine.
FT   MOD_RES     708    708       Phosphoserine.
FT   MOD_RES     714    714       Phosphoserine (By similarity).
FT   MOD_RES     719    719       Phosphothreonine (By similarity).
FT   DISULFID    583    614       By similarity.
FT   VAR_SEQ      34     91       Missing (in isoform Tau-B, isoform Tau-C,
FT                                isoform Tau-D and isoform Tau-E).
FT                                /FTId=VSP_003185.
FT   VAR_SEQ      92    113       Missing (in isoform Tau-E).
FT                                /FTId=VSP_003186.
FT   VAR_SEQ     114    350       Missing (in isoform Tau-A, isoform Tau-B,
FT                                isoform Tau-C, isoform Tau-D and isoform
FT                                Tau-E).
FT                                /FTId=VSP_003187.
FT   VAR_SEQ     368    433       Missing (in isoform Tau-A, isoform Tau-B,
FT                                isoform Tau-C, isoform Tau-D and isoform
FT                                Tau-E).
FT                                /FTId=VSP_003188.
FT   VAR_SEQ     567    597       Missing (in isoform Tau-B and isoform
FT                                Tau-C).
FT                                /FTId=VSP_003189.
FT   VAR_SEQ     733    733       L -> KAALLSSQVWNYSHDLATITDLGL (in isoform
FT                                Tau-B).
FT                                /FTId=VSP_003190.
FT   CONFLICT      3      3       D -> N (in Ref. 1).
FT   CONFLICT      9      9       D -> N (in Ref. 1).
FT   CONFLICT    405    405       S -> C (in Ref. 5; CAM14797).
FT   CONFLICT    528    528       P -> T (in Ref. 2; CAA78121).
FT   CONFLICT    549    549       R -> G (in Ref. 6; AAH14748).
FT   CONFLICT    672    672       E -> Q (in Ref. 1).
SQ   SEQUENCE   733 AA;  76243 MW;  80C0D50AC5F64E6F CRC64;
     MADPRQEFDT MEDHAGDYTL LQDQEGDMDH GLKESPPQPP ADDGAEEPGS ETSDAKSTPT
     AEDVTAPLVD ERAPDKQAAA QPHTEIPEGI TAEEAGIGDT PNQEDQAAGH VTQGRREGQA
     PDLGTSDWTR QQVSSMSGAP LLPQGLREAT CQPSGTRPED IEKSHPASEL LRRGPPQKEG
     WGQDRLGSEE EVDEDLTVDE SSQDSPPSQA SLTPGRAAPQ AGSGSVCGET ASVPGLPTEG
     SVPLPADFFS KVSAETQASQ PEGPGTGPME EGHEAAPEFT FHVEIKASTP KEQDLEGATV
     VGVPGEEQKA QTQGPSVGKG TKEASLQEPP GKQPAAGLPG RPVSRVPQLK ARVASKDRTG
     NDEKKAKTST PSCAKAPSHR PCLSPTRPTL GSSDPLIKPS SPAVSPEPAT SPKHVSSVTP
     RNGSPGTKQM KLKGADGKTG AKIATPRGAA SPAQKGTSNA TRIPAKTTPS PKTPPGSGEP
     PKSGERSGYS SPGSPGTPGS RSRTPSLPTP PTREPKKVAV VRTPPKSPSA SKSRLQTAPV
     PMPDLKNVRS KIGSTENLKH QPGGGKVQII NKKLDLSNVQ SKCGSKDNIK HVPGGGSVQI
     VYKPVDLSKV TSKCGSLGNI HHKPGGGQVE VKSEKLDFKD RVQSKIGSLD NITHVPGGGN
     KKIETHKLTF RENAKAKTDH GAEIVYKSPV VSGDTSPRHL SNVSSTGSID MVDSPQLATL
     ADEVSASLAK QGL
//
ID   TCEA1_MOUSE             Reviewed;         301 AA.
AC   P10711; P10712; P23713;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   12-FEB-2003, sequence version 2.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Transcription elongation factor A protein 1;
DE   AltName: Full=Transcription elongation factor S-II protein 1;
DE   AltName: Full=Transcription elongation factor TFIIS.o;
GN   Name=Tcea1; Synonyms=Tceat;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND PARTIAL PROTEIN
RP   SEQUENCE.
RX   MEDLINE=88153686; PubMed=3346229;
RA   Hirashima S., Hirai H., Nakanishi Y., Natori S.;
RT   "Molecular cloning and characterization of cDNA for eukaryotic
RT   transcription factor S-II.";
RL   J. Biol. Chem. 263:3858-3863(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver, and Mammary gland;
RX   MEDLINE=92011448; PubMed=1917889;
RA   Kanai A., Kuzuhara T., Sekimizu K., Natori S.;
RT   "Heterogeneity and tissue-specific expression of eukaryotic
RT   transcription factor S-II-related protein mRNA.";
RL   J. Biochem. 109:674-677(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=Czech II, and FVB/N;
RC   TISSUE=Mammary gland, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH EAF2.
RX   MEDLINE=22646236; PubMed=12761297; DOI=10.1093/jb/mvg065;
RA   Saso K., Ito T., Natori S., Sekimizu K.;
RT   "Identification of a novel tissue-specific transcriptional activator
RT   FESTA as a protein that interacts with the transcription elongation
RT   factor S-II.";
RL   J. Biochem. 133:493-500(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-100, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-100, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Necessary for efficient RNA polymerase II transcription
CC       elongation past template-encoded arresting sites. The arresting
CC       sites in DNA have the property of trapping a certain fraction of
CC       elongating RNA polymerases that pass through, resulting in locked
CC       ternary complexes. Cleavage of the nascent transcript by S-II
CC       allows the resumption of elongation from the new 3'-terminus.
CC   -!- SUBUNIT: Interacts with EAF2.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2; Synonyms=PSII-3;
CC         IsoId=P10711-1; Sequence=Displayed;
CC       Name=1; Synonyms=PSII-2;
CC         IsoId=P10711-2; Sequence=VSP_006410;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- MISCELLANEOUS: S-II binds to RNA-polymerase II in the absence of
CC       transcription.
CC   -!- SIMILARITY: Belongs to the TFS-II family.
CC   -!- SIMILARITY: Contains 1 TFIIS central domain.
CC   -!- SIMILARITY: Contains 1 TFIIS N-terminal domain.
CC   -!- SIMILARITY: Contains 1 TFIIS-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA00768.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA;
CC   -----------------------------------------------------------------------
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DR   EMBL; M18209; AAA40418.1; -; mRNA.
DR   EMBL; M18210; AAA40419.1; -; mRNA.
DR   EMBL; D00925; BAA00768.1; ALT_SEQ; mRNA.
DR   EMBL; BC006022; AAH06022.1; -; mRNA.
DR   EMBL; BC061490; AAH61490.1; -; mRNA.
DR   EMBL; BC083127; AAH83127.1; -; mRNA.
DR   IPI; IPI00121887; -.
DR   IPI; IPI00224168; -.
DR   PIR; A29950; A29950.
DR   RefSeq; NP_001153222.1; NM_001159750.1.
DR   RefSeq; NP_001153223.1; NM_001159751.1.
DR   RefSeq; NP_035671.1; NM_011541.4.
DR   UniGene; Mm.207263; -.
DR   ProteinModelPortal; P10711; -.
DR   SMR; P10711; 1-84, 135-301.
DR   STRING; P10711; -.
DR   PhosphoSite; P10711; -.
DR   PRIDE; P10711; -.
DR   Ensembl; ENSMUST00000081551; ENSMUSP00000080266; ENSMUSG00000033813.
DR   GeneID; 21399; -.
DR   KEGG; mmu:21399; -.
DR   UCSC; uc007afi.1; mouse.
DR   CTD; 21399; -.
DR   MGI; MGI:1196624; Tcea1.
DR   eggNOG; maNOG07851; -.
DR   HOGENOM; HBG716813; -.
DR   HOVERGEN; HBG055022; -.
DR   InParanoid; P10711; -.
DR   OMA; TTFVFCN; -.
DR   OrthoDB; EOG4SN1PH; -.
DR   PhylomeDB; P10711; -.
DR   NextBio; 300656; -.
DR   ArrayExpress; P10711; -.
DR   Bgee; P10711; -.
DR   CleanEx; MM_TCEA1; -.
DR   Genevestigator; P10711; -.
DR   GermOnline; ENSMUSG00000067869; Mus musculus.
DR   GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0003702; F:RNA polymerase II transcription factor activity; IEA:InterPro.
DR   GO; GO:0003711; F:transcription elongation regulator activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030218; P:erythrocyte differentiation; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0006354; P:transcription elongation, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR016492; TF_IIS.
DR   InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR   InterPro; IPR003618; TFIIS_cen_dom.
DR   InterPro; IPR017923; TFIIS_N.
DR   InterPro; IPR017890; TFS2M.
DR   InterPro; IPR006289; TFSII.
DR   InterPro; IPR001222; Znf_TFIIS.
DR   Gene3D; G3DSA:1.10.472.30; TFIIS_centre; 1.
DR   Gene3D; G3DSA:1.20.930.10; TFIIS_N_fun-typ; 1.
DR   Pfam; PF08711; TFIIS; 1.
DR   Pfam; PF01096; TFIIS_C; 1.
DR   Pfam; PF07500; TFIIS_M; 1.
DR   PIRSF; PIRSF006704; TF_IIS; 1.
DR   SMART; SM00510; TFS2M; 1.
DR   SMART; SM00509; TFS2N; 1.
DR   SMART; SM00440; ZnF_C2C2; 1.
DR   SUPFAM; SSF46942; TFIIS_centre; 1.
DR   SUPFAM; SSF47676; TFIIS_conserved; 1.
DR   TIGRFAMs; TIGR01385; TFSII; 1.
DR   PROSITE; PS51321; TFIIS_CENTRAL; 1.
DR   PROSITE; PS51319; TFIIS_N; 1.
DR   PROSITE; PS00466; ZF_TFIIS_1; 1.
DR   PROSITE; PS51133; ZF_TFIIS_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Direct protein sequencing;
KW   DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    301       Transcription elongation factor A protein
FT                                1.
FT                                /FTId=PRO_0000121447.
FT   DOMAIN        3     80       TFIIS N-terminal.
FT   DOMAIN      140    256       TFIIS central.
FT   ZN_FING     259    299       TFIIS-type.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      81     81       Phosphoserine (By similarity).
FT   MOD_RES      84     84       N6-acetyllysine (By similarity).
FT   MOD_RES      97     97       Phosphoserine.
FT   MOD_RES     100    100       Phosphoserine.
FT   MOD_RES     110    110       Phosphoserine (By similarity).
FT   MOD_RES     126    126       Phosphotyrosine (By similarity).
FT   VAR_SEQ       1     35       Missing (in isoform 1).
FT                                /FTId=VSP_006410.
SQ   SEQUENCE   301 AA;  33880 MW;  14B5105F8D77DA87 CRC64;
     MEDEVVRIAK KMDKMVQKKN AAGALDLLKE LKNIPMTLEL LQSTRIGMSV NALRKQSTDE
     EVTSLAKSLI KSWKKLLDGP STDKDPEEKK KEPAISSQNS PEAREESSSS SNVSSRKDET
     NARDTYVSSF PRAPSTSDSV RLKCREMLAA ALRTGDDYVA IGADEEELGS QIEEAIYQEI
     RNTDMKYKNR VRSRISNLKD AKNPNLRKNV LCGNIPPDLF ARMTAEEMAS DELKEMRKNL
     TKEAIREHQM AKTGGTQTDL FTCGKCKKKN CTYTQVQTRS ADEPMTTFVV CNECGNRWKF
     C
//
ID   RRAS_MOUSE              Reviewed;         218 AA.
AC   P10833;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   08-MAR-2011, entry version 100.
DE   RecName: Full=Ras-related protein R-Ras;
DE   AltName: Full=p23;
DE   Flags: Precursor;
GN   Name=Rras;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=87078390; PubMed=3098437; DOI=10.1016/0092-8674(87)90364-3;
RA   Lowe D.G., Capon D.J., Delwart E., Sakaguchi A.Y., Naylor S.L.,
RA   Goeddel D.V.;
RT   "Structure of the human and murine R-ras genes, novel genes closely
RT   related to ras proto-oncogenes.";
RL   Cell 48:137-146(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Regulates the organization of the actin cytoskeleton (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with PLCE1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (By similarity). Note=Inner surface of plasma membrane
CC       possibly with attachment requiring acylation of the C-terminal
CC       cysteine (By similarity with RAS).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; M21019; AAA40038.1; -; mRNA.
DR   EMBL; BC009105; AAH09105.1; -; mRNA.
DR   IPI; IPI00114594; -.
DR   RefSeq; NP_033127.1; NM_009101.2.
DR   UniGene; Mm.389894; -.
DR   ProteinModelPortal; P10833; -.
DR   SMR; P10833; 24-196.
DR   STRING; P10833; -.
DR   PhosphoSite; P10833; -.
DR   PRIDE; P10833; -.
DR   Ensembl; ENSMUST00000044111; ENSMUSP00000042150; ENSMUSG00000038387.
DR   GeneID; 20130; -.
DR   KEGG; mmu:20130; -.
DR   UCSC; uc009gss.1; mouse.
DR   CTD; 20130; -.
DR   MGI; MGI:98179; Rras.
DR   eggNOG; roNOG06144; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; P10833; -.
DR   OMA; FGASHHV; -.
DR   OrthoDB; EOG4P5KB6; -.
DR   PhylomeDB; P10833; -.
DR   NextBio; 297635; -.
DR   ArrayExpress; P10833; -.
DR   Bgee; P10833; -.
DR   CleanEx; MM_RRAS; -.
DR   Genevestigator; P10833; -.
DR   GermOnline; ENSMUSG00000038387; Mus musculus.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0030336; P:negative regulation of cell migration; IGI:MGI.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003577; GTPase_Ras.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR020849; Ras_small_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00173; RAS; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation.
FT   CHAIN         1    215       Ras-related protein R-Ras.
FT                                /FTId=PRO_0000082651.
FT   PROPEP      216    218       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000281301.
FT   NP_BIND      36     44       GTP (By similarity).
FT   NP_BIND      83     87       GTP (By similarity).
FT   NP_BIND     142    145       GTP (By similarity).
FT   NP_BIND     172    174       GTP (By similarity).
FT   MOTIF        58     66       Effector region (By similarity).
FT   MOD_RES     215    215       Cysteine methyl ester (By similarity).
FT   LIPID       215    215       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   218 AA;  23764 MW;  C1D32CE7904322E5 CRC64;
     MSSGAASGTG RGRPRGGGPG PRDPPPGETH KLVVVGGGGV GKSALTIQFI QSYFVSDYDP
     TIEDSYTKIC TVDGIPARLD ILDTAGQEEF GAMREQYMRA GNGFLLVFAI NDRQSFNEVG
     KLFTQILRVK DRDDFPIVLV GNKADLENQR QVLRSEASSF SASHHMTYFE ASAKLRLNVD
     EAFEQLVRAV RKYQEQELPP SPPSAPRKKD GGCPCVLL
//
ID   TCP4_MOUSE              Reviewed;         127 AA.
AC   P11031; Q3UJR5; Q543N2;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Activated RNA polymerase II transcriptional coactivator p15;
DE   AltName: Full=Positive cofactor 4;
DE            Short=PC4;
DE   AltName: Full=SUB1 homolog;
DE   AltName: Full=Single-stranded DNA-binding protein p9;
DE   AltName: Full=p14;
GN   Name=Sub1; Synonyms=Pc4, Rpo2tc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 51-81 AND 108-127,
RP   PROTEOLYTIC PROCESSING, AND DNA BINDING.
RX   MEDLINE=88228080; PubMed=3372536;
RA   Ballard D.W., Philbrick W.M., Bothwell A.L.M.;
RT   "Identification of a novel 9-kDa polypeptide from nuclear extracts.
RT   DNA binding properties, primary structure, and in vitro expression.";
RL   J. Biol. Chem. 263:8450-8457(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, DBA/2, and NOD; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-10; SER-11;
RP   SER-12; SER-13; SER-15; SER-17 AND SER-19, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
CC   -!- FUNCTION: General coactivator that functions cooperatively with
CC       TAFs and mediates functional interactions between upstream
CC       activators and the general transcriptional machinery. May be
CC       involved in stabilizing the multiprotein transcription complex.
CC       Binds single-stranded DNA. Also binds, in vitro, non-specifically
CC       to double-stranded DNA (ds DNA).
CC   -!- SUBUNIT: Homodimer. Interacts with CSTF2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- PTM: Activity is controlled by protein kinases that target the
CC       regulatory region. Phosphorylation inactivates both ds DNA-binding
CC       and cofactor function, but does not affect binding to ssDNA (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the transcriptional coactivator PC4 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; J03750; AAA37317.1; -; mRNA.
DR   EMBL; AK048371; BAC33314.1; -; mRNA.
DR   EMBL; AK049260; BAC33642.1; -; mRNA.
DR   EMBL; AK132021; BAE20946.1; -; mRNA.
DR   EMBL; AK146335; BAE27090.1; -; mRNA.
DR   EMBL; AK151734; BAE30649.1; -; mRNA.
DR   EMBL; AK154114; BAE32384.1; -; mRNA.
DR   EMBL; BC010967; AAH10967.1; -; mRNA.
DR   IPI; IPI00225633; -.
DR   PIR; A28084; A28084.
DR   RefSeq; NP_035424.1; NM_011294.3.
DR   UniGene; Mm.41746; -.
DR   ProteinModelPortal; P11031; -.
DR   SMR; P11031; 63-127.
DR   STRING; P11031; -.
DR   PhosphoSite; P11031; -.
DR   PRIDE; P11031; -.
DR   Ensembl; ENSMUST00000022816; ENSMUSP00000022816; ENSMUSG00000022205.
DR   Ensembl; ENSMUST00000110504; ENSMUSP00000106130; ENSMUSG00000022205.
DR   GeneID; 20024; -.
DR   KEGG; mmu:20024; -.
DR   UCSC; uc007vhj.1; mouse.
DR   CTD; 20024; -.
DR   MGI; MGI:104811; Sub1.
DR   eggNOG; roNOG17180; -.
DR   GeneTree; ENSGT00390000008802; -.
DR   HOGENOM; HBG383565; -.
DR   HOVERGEN; HBG028243; -.
DR   InParanoid; P11031; -.
DR   OMA; QWNQLKD; -.
DR   OrthoDB; EOG4NS3D2; -.
DR   PhylomeDB; P11031; -.
DR   NextBio; 297547; -.
DR   ArrayExpress; P11031; -.
DR   Bgee; P11031; -.
DR   CleanEx; MM_SUB1; -.
DR   Genevestigator; P11031; -.
DR   GermOnline; ENSMUSG00000022205; Mus musculus.
DR   InterPro; IPR003173; PC4.
DR   InterPro; IPR009044; ssDNA-bd_transcriptional_reg.
DR   Gene3D; G3DSA:2.30.31.10; ssDNA-bd_transcriptional_reg; 1.
DR   PANTHER; PTHR13215; PC4; 1.
DR   Pfam; PF02229; PC4; 1.
DR   SUPFAM; SSF54447; ssDNA_bind_regul; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Direct protein sequencing; DNA-binding;
KW   Nucleus; Phosphoprotein; Transcription; Transcription regulation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    127       Activated RNA polymerase II
FT                                transcriptional coactivator p15.
FT                                /FTId=PRO_0000023286.
FT   REGION        2     50       Regulatory.
FT   REGION       77    101       Interaction with ssDNA (By similarity).
FT   COMPBIAS      4     19       Ser-rich.
FT   COMPBIAS     23     53       Lys-rich.
FT   COMPBIAS     51     58       Ser-rich.
FT   SITE         50     51       Cleavage.
FT   MOD_RES       9      9       Phosphoserine.
FT   MOD_RES      10     10       Phosphoserine.
FT   MOD_RES      11     11       Phosphoserine.
FT   MOD_RES      12     12       Phosphoserine.
FT   MOD_RES      13     13       Phosphoserine.
FT   MOD_RES      15     15       Phosphoserine.
FT   MOD_RES      17     17       Phosphoserine.
FT   MOD_RES      19     19       Phosphoserine.
FT   MOD_RES      35     35       N6-acetyllysine (By similarity).
FT   MOD_RES      52     52       Phosphoserine (By similarity).
FT   MOD_RES      56     56       Phosphoserine (By similarity).
FT   MOD_RES      58     58       Phosphoserine (By similarity).
FT   MOD_RES      68     68       N6-acetyllysine (By similarity).
FT   MOD_RES     104    104       Phosphoserine (By similarity).
FT   MOD_RES     118    118       Phosphoserine (By similarity).
FT   CONFLICT     46     46       S -> P (in Ref. 2; BAE27090).
SQ   SEQUENCE   127 AA;  14427 MW;  12D58716F40FEB1C CRC64;
     MPKSKELVSS SSSGSDSDSE VEKKLKRKKQ AVPEKPVKKQ KPGETSRALA SSKQSSSSRD
     DNMFQIGKMR YVSVRDFKGK ILIDIREYWM DSEGEMKPGR KGISLNMEQW SQLKEQISDI
     DDAVRKL
//
ID   FINC_MOUSE              Reviewed;        2477 AA.
AC   P11276; Q61567; Q61568; Q61569; Q64233; Q80UI4;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2003, sequence version 3.
DT   08-MAR-2011, entry version 132.
DE   RecName: Full=Fibronectin;
DE            Short=FN;
DE   Contains:
DE     RecName: Full=Anastellin;
DE   Flags: Precursor;
GN   Name=Fn1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-920.
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RC   TISSUE=Liver;
RX   MEDLINE=94131313; PubMed=8299972; DOI=10.1016/0378-1119(93)90036-3;
RA   Polly P., Nicholson R.C.;
RT   "Sequence of the mouse fibronectin-encoding gene promoter region.";
RL   Gene 137:353-354(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 562-834.
RC   STRAIN=NMRI;
RX   MEDLINE=95403556; PubMed=7673336;
RA   Talts J.F., Weller A., Timpl R., Ekblom M., Ekblom P.;
RT   "Regulation of mesenchymal extracellular matrix protein synthesis by
RT   transforming growth factor-beta and glucocorticoids in tumor stroma.";
RL   J. Cell Sci. 108:2153-2162(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 899-2376.
RA   Gorski G., Aros M., Norton P.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2375-2477.
RX   MEDLINE=88124987; PubMed=3124113; DOI=10.1073/pnas.85.4.1119;
RA   Blatti S.P., Foster D.N., Ranganthan G., Moses H.L., Getz M.J.;
RT   "Induction of fibronectin gene transcription and mRNA is a primary
RT   response to growth-factor stimulation of AKR-2B cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:1119-1123(1988).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2375-2477.
RX   MEDLINE=89121031; PubMed=2521606; DOI=10.1016/0014-4827(89)90080-3;
RA   Ryseck R.P., MacDonald-Bravo H., Zerial M., Bravo R.;
RT   "Coordinate induction of fibronectin, fibronectin receptor,
RT   tropomyosin, and actin genes in serum-stimulated fibroblasts.";
RL   Exp. Cell Res. 180:537-545(1989).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2375-2477.
RC   TISSUE=Kidney;
RX   MEDLINE=93011702; PubMed=1327855; DOI=10.1016/0014-4827(92)90100-M;
RA   Khandjian E.W., Salomon C., Leonard N., Tremblay S., Turler H.;
RT   "Fibronectin gene expression in proliferating, quiescent, and SV40-
RT   infected mouse kidney cells.";
RL   Exp. Cell Res. 202:464-470(1992).
RN   [8]
RP   TRANSGLUTAMINATION AT GLN-35; GLN-36 AND GLN-48, AND MUTAGENESIS OF
RP   GLN-35; GLN-36 AND GLN-48.
RX   PubMed=9312106; DOI=10.1074/jbc.272.40.24999;
RA   Corbett S.A., Lee L., Wilson C.L., Schwarzbauer J.E.;
RT   "Covalent cross-linking of fibronectin to fibrin is required for
RT   maximal cell adhesion to a fibronectin-fibrin matrix.";
RL   J. Biol. Chem. 272:24999-25005(1997).
RN   [9]
RP   DOWN-REGULATION BY GLUCOCORTICOIDS.
RX   MEDLINE=21600963; PubMed=11737251;
RX   DOI=10.1034/j.1600-0609.2001.5790528.x;
RA   Gu Y.-C., Talts J.F., Gullberg D., Timpl R., Ekblom M.;
RT   "Glucocorticoids down-regulate the extracellular matrix proteins
RT   fibronectin, fibulin-1 and fibulin-2 in bone marrow stroma.";
RL   Eur. J. Haematol. 67:176-184(2001).
RN   [10]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1006, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Plasma;
RX   PubMed=16944957; DOI=10.1021/pr060186m;
RA   Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
RA   Gevaert K.;
RT   "Proteome-wide characterization of N-glycosylation events by diagonal
RT   chromatography.";
RL   J. Proteome Res. 5:2438-2447(2006).
RN   [11]
RP   INTERACTION WITH FBLN7.
RX   PubMed=17699513; DOI=10.1074/jbc.M705847200;
RA   de Vega S., Iwamoto T., Nakamura T., Hozumi K., McKnight D.A.,
RA   Fisher L.W., Fukumoto S., Yamada Y.;
RT   "TM14 is a new member of the fibulin family (fibulin-7) that interacts
RT   with extracellular matrix molecules and is active for cell binding.";
RL   J. Biol. Chem. 282:30878-30888(2007).
RN   [12]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-528, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Plasma;
RX   PubMed=17330941; DOI=10.1021/pr0604559;
RA   Bernhard O.K., Kapp E.A., Simpson R.J.;
RT   "Enhanced analysis of the mouse plasma proteome using cysteine-
RT   containing tryptic glycopeptides.";
RL   J. Proteome Res. 6:987-995(2007).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2475, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2475, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [15]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-528; ASN-1001; ASN-1006;
RP   ASN-1290 AND ASN-2198, AND MASS SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2475, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [17]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1006 AND ASN-1290, AND
RP   MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [18]
RP   STRUCTURE BY NMR OF 1447-1630.
RX   MEDLINE=98202578; PubMed=9533887; DOI=10.1006/jmbi.1998.1616;
RA   Copie V., Tomita Y., Akiyama S.K., Aota S., Yamada K.M., Venable R.M.,
RA   Pastor R.W., Krueger S., Torchia D.A.;
RT   "Solution structure and dynamics of linked cell attachment modules of
RT   mouse fibronectin containing the RGD and synergy regions: comparison
RT   with the human fibronectin crystal structure.";
RL   J. Mol. Biol. 277:663-682(1998).
CC   -!- FUNCTION: Fibronectins bind cell surfaces and various compounds
CC       including collagen, fibrin, heparin, DNA, and actin. Fibronectins
CC       are involved in cell adhesion, cell motility, opsonization, wound
CC       healing, and maintenance of cell shape.
CC   -!- FUNCTION: Anastellin binds fibronectin and induces fibril
CC       formation. This fibronectin polymer, named superfibronectin,
CC       exhibits enhanced adhesive properties. Both anastellin and
CC       superfibronectin inhibit tumor growth, angiogenesis and
CC       metastasis. Anastellin activates p38 MAPK and inhibits
CC       lysophospholipid signaling (By similarity).
CC   -!- SUBUNIT: Mostly heterodimers or multimers of alternatively spliced
CC       variants, connected by 2 disulfide bonds near the carboxyl ends;
CC       to a lesser extent homodimers. Interacts with FBLN1, AMBP,
CC       LGALS3BP and COL13A1 and COMP (By similarity). Interacts with TNR;
CC       interaction mediates inhibition of cell adhesion and neurite
CC       outgrowth. Interacts with FBLN7. Interacts with FST3 (By
CC       similarity).
CC   -!- INTERACTION:
CC       Q8CIH5:Plcg2; NbExp=2; IntAct=EBI-641955, EBI-617954;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. Each of the "extra
CC         domain" and the connecting strand 3 are present in some forms of
CC         fibronectin and absent in others;
CC       Name=1;
CC         IsoId=P11276-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Plasma FN (soluble dimeric form) is secreted
CC       by hepatocytes. Cellular FN (dimeric or cross-linked multimeric
CC       forms), made by fibroblasts, epithelial and other cell types, is
CC       deposited as fibrils in the extracellular matrix.
CC   -!- INDUCTION: Glucocorticoids suppressed mRNA expression and protein
CC       synthesis.
CC   -!- PTM: Sulfated (By similarity).
CC   -!- PTM: Forms covalent cross-links mediated by a transglutaminase,
CC       such as F13A or TGM2, between a glutamine and the epsilon-amino
CC       group of a lysine residue, forming homopolymers and heteropolymers
CC       (e.g. fibrinogen-fibronectin, collagen-fibronectin
CC       heteropolymers).
CC   -!- PTM: Phosphorylation sites are present in the extracelllular
CC       medium (By similarity).
CC   -!- PTM: Proteolytic processing produces the C-terminal NC1 peptide,
CC       anastellin (By similarity).
CC   -!- SIMILARITY: Contains 12 fibronectin type-I domains.
CC   -!- SIMILARITY: Contains 2 fibronectin type-II domains.
CC   -!- SIMILARITY: Contains 17 fibronectin type-III domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC051082; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; Z22729; CAA80422.1; -; Genomic_DNA.
DR   EMBL; X82402; CAA57796.1; -; mRNA.
DR   EMBL; X93167; CAA63654.1; -; mRNA.
DR   EMBL; M18194; AAA37636.1; -; mRNA.
DR   EMBL; S45680; AAB23491.1; -; mRNA.
DR   IPI; IPI00113539; -.
DR   PIR; A49173; A49173.
DR   PIR; I48349; I48349.
DR   UniGene; Mm.193099; -.
DR   PDB; 1MFN; NMR; -; A=1447-1630.
DR   PDB; 2MFN; NMR; -; A=1447-1630.
DR   PDBsum; 1MFN; -.
DR   PDBsum; 2MFN; -.
DR   ProteinModelPortal; P11276; -.
DR   SMR; P11276; 43-2422.
DR   IntAct; P11276; 6.
DR   MINT; MINT-202764; -.
DR   STRING; P11276; -.
DR   PhosphoSite; P11276; -.
DR   PRIDE; P11276; -.
DR   Ensembl; ENSMUST00000055226; ENSMUSP00000054499; ENSMUSG00000026193.
DR   UCSC; uc007bju.1; mouse.
DR   MGI; MGI:95566; Fn1.
DR   eggNOG; roNOG06867; -.
DR   HOGENOM; HBG447052; -.
DR   HOVERGEN; HBG005731; -.
DR   InParanoid; P11276; -.
DR   ArrayExpress; P11276; -.
DR   Bgee; P11276; -.
DR   CleanEx; MM_FN1; -.
DR   Genevestigator; P11276; -.
DR   GermOnline; ENSMUSG00000026193; Mus musculus.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0016504; F:peptidase activator activity; IDA:MGI.
DR   GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0007160; P:cell-matrix adhesion; IDA:MGI.
DR   GO; GO:0007044; P:cell-substrate junction assembly; IDA:MGI.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0042060; P:wound healing; IMP:MGI.
DR   InterPro; IPR016060; Complement_control_module.
DR   InterPro; IPR000083; Fibrnctn1.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR000562; FN_type2_col-bd.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013806; Kringle-like.
DR   Gene3D; G3DSA:2.10.70.10; Complement_control_module; 12.
DR   Gene3D; G3DSA:2.10.10.10; FN2; 2.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 17.
DR   Pfam; PF00039; fn1; 12.
DR   Pfam; PF00040; fn2; 2.
DR   Pfam; PF00041; fn3; 17.
DR   SMART; SM00058; FN1; 12.
DR   SMART; SM00059; FN2; 2.
DR   SMART; SM00060; FN3; 17.
DR   SUPFAM; SSF49265; FN_III-like; 17.
DR   SUPFAM; SSF57440; Kringle-like; 2.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01253; FN1_1; 12.
DR   PROSITE; PS51091; FN1_2; 12.
DR   PROSITE; PS00023; FN2_1; 2.
DR   PROSITE; PS51092; FN2_2; 2.
DR   PROSITE; PS50853; FN3; 17.
PE   1: Evidence at protein level;
KW   3D-structure; Acute phase; Alternative splicing; Angiogenesis;
KW   Cell adhesion; Cell shape; Disulfide bond; Extracellular matrix;
KW   Glycoprotein; Heparin-binding; Isopeptide bond; Phosphoprotein;
KW   Pyrrolidone carboxylic acid; Repeat; Secreted; Signal; Sulfation.
FT   SIGNAL        1     32       By similarity.
FT   CHAIN        33   2477       Fibronectin.
FT                                /FTId=PRO_0000019236.
FT   CHAIN       627    701       Anastellin (By similarity).
FT                                /FTId=PRO_0000390480.
FT   DOMAIN       51     91       Fibronectin type-I 1.
FT   DOMAIN       96    139       Fibronectin type-I 2.
FT   DOMAIN      140    183       Fibronectin type-I 3.
FT   DOMAIN      185    229       Fibronectin type-I 4.
FT   DOMAIN      230    274       Fibronectin type-I 5.
FT   DOMAIN      306    343       Fibronectin type-I 6.
FT   DOMAIN      355    403       Fibronectin type-II 1.
FT   DOMAIN      415    463       Fibronectin type-II 2.
FT   DOMAIN      468    516       Fibronectin type-I 7.
FT   DOMAIN      516    558       Fibronectin type-I 8.
FT   DOMAIN      559    602       Fibronectin type-I 9.
FT   DOMAIN      607    699       Fibronectin type-III 1.
FT   DOMAIN      719    808       Fibronectin type-III 2.
FT   DOMAIN      810    897       Fibronectin type-III 3.
FT   DOMAIN      905    994       Fibronectin type-III 4.
FT   DOMAIN      995   1083       Fibronectin type-III 5.
FT   DOMAIN     1091   1171       Fibronectin type-III 6.
FT   DOMAIN     1172   1264       Fibronectin type-III 7.
FT   DOMAIN     1265   1355       Fibronectin type-III 8; extra domain 1.
FT   DOMAIN     1356   1446       Fibronectin type-III 9.
FT   DOMAIN     1447   1536       Fibronectin type-III 10.
FT   DOMAIN     1537   1626       Fibronectin type-III 11.
FT   DOMAIN     1631   1720       Fibronectin type-III 12.
FT   DOMAIN     1721   1810       Fibronectin type-III 13; extra domain 2.
FT   DOMAIN     1813   1900       Fibronectin type-III 14.
FT   DOMAIN     1903   1991       Fibronectin type-III 15.
FT   DOMAIN     1992   2081       Fibronectin type-III 16.
FT   DOMAIN     2190   2280       Fibronectin type-III 17.
FT   DOMAIN     2294   2338       Fibronectin type-I 10.
FT   DOMAIN     2339   2381       Fibronectin type-I 11.
FT   DOMAIN     2383   2426       Fibronectin type-I 12.
FT   DNA_BIND    906   1171
FT   REGION       53    273       Fibrin- and heparin-binding 1.
FT   REGION      308    608       Collagen-binding.
FT   REGION     1357   1630       Cell-attachment.
FT   REGION     1811   2081       Heparin-binding 2.
FT   REGION     2082   2201       Connecting strand 3 (CS-3) (V region).
FT   REGION     2296   2427       Fibrin-binding 2.
FT   MOTIF      1614   1616       Cell attachment site.
FT   MOTIF      2181   2183       Cell attachment site.
FT   MOD_RES      33     33       Pyrrolidone carboxylic acid (By
FT                                similarity).
FT   MOD_RES     875    875       Sulfotyrosine (Potential).
FT   MOD_RES     880    880       Sulfotyrosine (Potential).
FT   MOD_RES     903    903       Phosphoserine (By similarity).
FT   MOD_RES    2392   2392       Sulfotyrosine (Potential).
FT   MOD_RES    2432   2432       Phosphoserine (By similarity).
FT   MOD_RES    2475   2475       Phosphoserine.
FT   CARBOHYD    430    430       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    528    528       N-linked (GlcNAc...).
FT   CARBOHYD    542    542       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    876    876       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1001   1001       N-linked (GlcNAc...).
FT   CARBOHYD   1006   1006       N-linked (GlcNAc...).
FT   CARBOHYD   1243   1243       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1290   1290       N-linked (GlcNAc...).
FT   CARBOHYD   2198   2198       N-linked (GlcNAc...).
FT   DISULFID     53     79       By similarity.
FT   DISULFID     77     88       By similarity.
FT   DISULFID     98    126       By similarity.
FT   DISULFID    124    136       By similarity.
FT   DISULFID    142    170       By similarity.
FT   DISULFID    168    180       By similarity.
FT   DISULFID    187    216       By similarity.
FT   DISULFID    214    226       By similarity.
FT   DISULFID    232    261       By similarity.
FT   DISULFID    259    271       By similarity.
FT   DISULFID    308    335       By similarity.
FT   DISULFID    333    342       By similarity.
FT   DISULFID    360    386       By similarity.
FT   DISULFID    374    401       By similarity.
FT   DISULFID    420    446       By similarity.
FT   DISULFID    434    461       By similarity.
FT   DISULFID    470    498       By similarity.
FT   DISULFID    496    508       By similarity.
FT   DISULFID    518    545       By similarity.
FT   DISULFID    543    555       By similarity.
FT   DISULFID    561    589       By similarity.
FT   DISULFID    587    599       By similarity.
FT   DISULFID   2296   2325       By similarity.
FT   DISULFID   2323   2335       By similarity.
FT   DISULFID   2341   2368       By similarity.
FT   DISULFID   2366   2378       By similarity.
FT   DISULFID   2385   2411       By similarity.
FT   DISULFID   2409   2420       By similarity.
FT   DISULFID   2458   2458       Interchain (with C-2462).
FT   DISULFID   2462   2462       Interchain (with C-2458).
FT   CROSSLNK     35     35       Isoglutamyl lysine isopeptide (Gln-Lys)
FT                                (interchain with K-?).
FT   CROSSLNK     36     36       Isoglutamyl lysine isopeptide (Gln-Lys)
FT                                (interchain with K-?).
FT   CROSSLNK     48     48       Isoglutamyl lysine isopeptide (Gln-Lys)
FT                                (interchain with K-?).
FT   MUTAGEN      35     35       Q->A: 99% decrease in cross-linking
FT                                efficiency; when associated with A-36 and
FT                                A-48.
FT   MUTAGEN      35     35       Q->L: 65% decrease in cross-linking
FT                                efficiency; when associated with L-36.
FT   MUTAGEN      36     36       Q->A: 99% decrease in cross-linking
FT                                efficiency; when associated with A-35 and
FT                                A-48.
FT   MUTAGEN      36     36       Q->L: 65% decrease in cross-linking
FT                                efficiency; when associated with L-35.
FT   MUTAGEN      48     48       Q->A: 99% decrease in cross-linking
FT                                efficiency; when associated with A-35 and
FT                                A-36.
FT   CONFLICT    918    920       TDV -> DIE (in Ref. 1; BC051082).
FT   CONFLICT   2440   2440       N -> T (in Ref. 6).
FT   STRAND     1455   1459
FT   STRAND     1461   1467
FT   STRAND     1476   1484
FT   STRAND     1492   1496
FT   STRAND     1501   1507
FT   STRAND     1510   1521
FT   STRAND     1530   1536
FT   STRAND     1545   1550
FT   STRAND     1553   1557
FT   STRAND     1567   1580
FT   STRAND     1582   1586
FT   STRAND     1591   1594
FT   STRAND     1600   1612
FT   STRAND     1615   1617
FT   STRAND     1624   1630
SQ   SEQUENCE   2477 AA;  272489 MW;  CC03BAF77A08CA9E CRC64;
     MLRGPGPGRL LLLAVLCLGT SVRCTEAGKS KRQAQQIVQP QSPVAVSQSK PGCFDNGKHY
     QINQQWERTY LGNALVCTCY GGSRGFNCES KPEPEETCFD KYTGNTYKVG DTYERPKDSM
     IWDCTCIGAG RGRISCTIAN RCHEGGQSYK IGDKWRRPHE TGGYMLECLC LGNGKGEWTC
     KPIAEKCFDH AAGTSYVVGE TWEKPYQGWM MVDCTCLGEG NGRITCTSRN RCNDQDTRTS
     YRIGDTWSKK DNRGNLLQCV CTGNGRGEWK CERHALQSAS AGSGSFTDVR TAIYQPQTHP
     QPAPYGHCVT DSGVVYSVGM QWLKSQGNKQ MLCTCLGNGV SCQETAVTQT YGGNSNGEPC
     VLPFTYNGRT FYSCTTEGRQ DGHLWCSTTS NYEQDQKYSF CTDHAVLVQT RGGNSNGALC
     HFPFLYNNRN YTDCTSEGRR DNMKWCGTTQ NYDADQKFGF CPMAAHEEIC TTNEGVMYRI
     GDQWDKQHDL GHMMRCTCVG NGRGEWACIP YSQLRDQCIV DDITYNVNDT FHKRHEEGHM
     LNCTCFGQGR GRWKCDPIDQ CQDSETRTFY QIGDSWEKFV HGVRYQCYCY GRGIGEWHCQ
     PLQTYPGTTG PVQVIITETP SQPNSHPIQW NAPEPSHITK YILRWRPKTS TGRWKEATIP
     GHLNSYTIKG LTPGVIYEGQ LISIQQYGHR EVTRFDFTTS ASTPVTSNTV TGETAPYSPV
     VATSESVTEI TASSFVVSWV SASDTVSGFR VEYELSEEGD EPQYLDLPST ATSVNIPDLL
     PGRKYIVNVY QISEEGKQSL ILSTSQTTAP DAPPDPTVDQ VDDTSIVVRW SRPQAPITGY
     RIVYSPSVEG SSTELNLPET ANSVTLSDLQ PGVQYNITIY AVEENQESTP VFIQQETTGT
     PRSDNVPPPT DLQFVELTDV KVTIMWTPPD SVVSGYRVEV LPVSLPGEHG QRLPVNRNTF
     AEITGLSPGV TYLFKVFAVH QGRESNPLTA QQTTKLDAPT NLQFVNETDR TVLVTWTPPR
     ARIAGYRLTA GLTRGGQPKQ YNVGPLASKY PLRNLQPGSE YTATLVAVKG NQQSPKATGV
     FTTLQPLRSI PPYNTEVTET TIVITWTPAP RIGFKLGVRP SQGGEAPREV TSDSGSIVVS
     GLTPGVEYTY TIQVLRDGQE RDAPIVNRVV TPLSPPTNLH LEANPDTGVL TVSWERSTTP
     DITGYRITTT PTNGQQGTSL EEVVHADQSS CTFENLNPGL EYNVSVYTVK DDKESAPISD
     TVVPEVPQLT DLSFVDITDS SIGLRWTPLN SSTIIGYRIT VVAAGEGIPI FEDFVDSSVG
     YYTVTGLEPG IDYDISVITL INGGESAPTT LTQQTAVPPP TDLRFTNIGP DTMRVTWAPP
     PSIELTNLLV RYSPVKNEED VAELSISPSD NAVVLTNLLP GTEYLVSVSS VYEQHESIPL
     RGRQKTGLDS PTGFDSSDIT ANSFTVHWVA PRAPITGYII RHHAEHSVGR PRQDRVPPSR
     NSITLTNLNP GTEYVVSIIA VNGREESPPL IGQQATVSDI PRDLEVIAST PTSLLISWEP
     PAVSVRYYRI TYGETGGNSP VQEFTVPGSK STATINNIKP GADYTITLYA VTGRGDSPAS
     SKPVSINYKT EIDKPSQMQV TDVQDNSISV RWLPSTSPVT GYRVTTTPKN GLGPSKTKTA
     SPDQTEMTIE GLQPTVEYVV SVYAQNRNGE SQPLVQTAVT NIDRPKGLAF TDVDVDSIKI
     AWESPQGQVS RYRVTYSSPE DGIRELFPAP DGEDDTAELQ GLRPGSEYTV SVVALHDDME
     SQPLIGIQST AIPAPTNLKL SQVTPTSFTA QWIAPSVQLT GYRVRVNPKE KTGPMKEINL
     SPDSSSVIVS GLMVATKYEV SVYALKDTLT SRPAQGVITT LENVSPPRRA RVTDATETTI
     TISWRTKTET ITGFQVDAIP ANGQTPVQRS ISPDVRSYTI TGLQPGTDYK IHLYTLNDNA
     RSSPVIIDAS TAIDAPSNLR FLTTTPNSLL VSWQAPRARI TGYIIKYEKP GSPPREVVPR
     PRPGVTEATI TGLEPGTEYT IYVIALKNNQ KSEPLIGRKK TDELPQLVTL PHPNLHGPEI
     LDVPSTVQKT PFITNPGYDT ENGIQLPGTT HQQPSVGQQM IFEEHGFRRT TPPTAATPVR
     LRPRPYLPNV DEEVQIGHVP RGDVDYHLYP HVPGLNPNAS TGQEALSQTT ISWTPFQESS
     EYIISCQPVG TDEEPLQFQV PGTSTSATLT GLTRGVTYNI IVEALQNQRR HKVREEVVTV
     GNAVSEGLNQ PTDDSCFDPY TVSHYAIGEE WERLSDAGFK LTCQCLGFGS GHFRCDSSKW
     CHDNGVNYKI GEKWDRQGEN GQRMSCTCLG NGKGEFKCDP HEATCYDDGK TYHVGEQWQK
     EYLGAICSCT CFGGQRGWRC DNCRRPGAAE PSPDGTTGHN YNQYTQRYNQ RTNTNVNCPI
     ECFMPLDVQA DRDDSRE
//
ID   LAMP1_MOUSE             Reviewed;         406 AA.
AC   P11438; Q62020;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 2.
DT   08-MAR-2011, entry version 102.
DE   RecName: Full=Lysosome-associated membrane glycoprotein 1;
DE            Short=LAMP-1;
DE            Short=Lysosome-associated membrane protein 1;
DE   AltName: Full=120 kDa lysosomal membrane glycoprotein;
DE   AltName: Full=CD107 antigen-like family member A;
DE   AltName: Full=LGP-120;
DE   AltName: Full=Lysosomal membrane glycoprotein A;
DE            Short=LGP-A;
DE   AltName: Full=P2B;
DE   AltName: CD_antigen=CD107a;
DE   Flags: Precursor;
GN   Name=Lamp1; Synonyms=Lamp-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90307738; PubMed=2142158;
RA   Granger B.L., Green S.A., Gabel C.A., Howe C.L., Mellman I.,
RA   Helenius A.;
RT   "Characterization and cloning of lgp110, a lysosomal membrane
RT   glycoprotein from mouse and rat cells.";
RL   J. Biol. Chem. 265:12036-12043(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90002989; PubMed=2676155;
RA   Heffernan M., Yousefi S., Dennis J.W.;
RT   "Molecular characterization of P2B/LAMP-1, a major protein target of a
RT   metastasis-associated oligosaccharide structure.";
RL   Cancer Res. 49:6077-6084(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 25-406, AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=88243732; PubMed=3379044;
RA   Chen J.W., Cha Y., Yuksel K.U., Gracy R.W., August J.T.;
RT   "Isolation and sequencing of a cDNA clone encoding lysosomal membrane
RT   glycoprotein mouse LAMP-1. Sequence similarity to proteins bearing
RT   onco-differentiation antigens.";
RL   J. Biol. Chem. 263:8754-8758(1988).
RN   [5]
RP   DISULFIDE BONDS.
RX   MEDLINE=90237040; PubMed=2332434;
RA   Arterburn L.M., Earles B.J., August J.T.;
RT   "The disulfide structure of mouse lysosome-associated membrane protein
RT   1.";
RL   J. Biol. Chem. 265:7419-7423(1990).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-252, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Epidermis;
RX   PubMed=16170054; DOI=10.1074/mcp.M500203-MCP200;
RA   Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K.,
RA   Monde K., Nishimura S.;
RT   "High throughput quantitative glycomics and glycoform-focused
RT   proteomics of murine dermis and epidermis.";
RL   Mol. Cell. Proteomics 4:1977-1989(2005).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-97, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Plasma;
RX   PubMed=16944957; DOI=10.1021/pr060186m;
RA   Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
RA   Gevaert K.;
RT   "Proteome-wide characterization of N-glycosylation events by diagonal
RT   chromatography.";
RL   J. Proteome Res. 5:2438-2447(2006).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-177, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-97; ASN-101; ASN-159 AND
RP   ASN-177, AND MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Presents carbohydrate ligands to selectins. Also
CC       implicated in tumor cell metastasis.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Endosome membrane; Single-pass type I membrane protein.
CC       Lysosome membrane; Single-pass type I membrane protein. Note=This
CC       protein shuttles between lysosomes, endosomes, and the plasma
CC       membrane.
CC   -!- PTM: O- and N-glycosylated; some of the N-glycans attached to
CC       LAMP-1 are polylactosaminoglycans (By similarity).
CC   -!- SIMILARITY: Belongs to the LAMP family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; M32015; AAA39428.1; -; mRNA.
DR   EMBL; M25244; AAA39869.1; -; mRNA.
DR   EMBL; BC049097; AAH49097.1; -; mRNA.
DR   EMBL; J03881; AAA39411.1; -; mRNA.
DR   IPI; IPI00876139; -.
DR   PIR; A28067; A28067.
DR   PIR; A60534; A60534.
DR   RefSeq; NP_034814.2; NM_010684.2.
DR   UniGene; Mm.16716; -.
DR   UniGene; Mm.463967; -.
DR   ProteinModelPortal; P11438; -.
DR   IntAct; P11438; 3.
DR   MINT; MINT-1858576; -.
DR   STRING; P11438; -.
DR   PhosphoSite; P11438; -.
DR   PRIDE; P11438; -.
DR   Ensembl; ENSMUST00000033824; ENSMUSP00000033824; ENSMUSG00000031447.
DR   GeneID; 16783; -.
DR   KEGG; mmu:16783; -.
DR   UCSC; uc009kxa.1; mouse.
DR   CTD; 16783; -.
DR   MGI; MGI:96745; Lamp1.
DR   eggNOG; roNOG05865; -.
DR   HOVERGEN; HBG052303; -.
DR   OrthoDB; EOG4MPHQD; -.
DR   PhylomeDB; P11438; -.
DR   NextBio; 290640; -.
DR   ArrayExpress; P11438; -.
DR   Bgee; P11438; -.
DR   CleanEx; MM_LAMP1; -.
DR   Genevestigator; P11438; -.
DR   GermOnline; ENSMUSG00000031447; Mus musculus.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042470; C:melanosome; IDA:MGI.
DR   GO; GO:0005771; C:multivesicular body; IDA:MGI.
DR   GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:BHF-UCL.
DR   InterPro; IPR018134; LAMP_CS.
DR   InterPro; IPR002000; Lysosome-assoc_membr_glycop.
DR   PANTHER; PTHR11506; Lamp; 1.
DR   Pfam; PF01299; Lamp; 1.
DR   PRINTS; PR00336; LYSASSOCTDMP.
DR   PROSITE; PS00310; LAMP_1; 2.
DR   PROSITE; PS00311; LAMP_2; 1.
DR   PROSITE; PS51407; LAMP_3; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Disulfide bond; Endosome;
KW   Glycoprotein; Lysosome; Membrane; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     24
FT   CHAIN        25    406       Lysosome-associated membrane glycoprotein
FT                                1.
FT                                /FTId=PRO_0000017105.
FT   TOPO_DOM     25    370       Lumenal (Potential).
FT   TRANSMEM    371    394       Helical; (Potential).
FT   TOPO_DOM    395    406       Cytoplasmic (Potential).
FT   REGION       25    188       First lumenal domain.
FT   REGION      189    218       Hinge.
FT   REGION      219    370       Second lumenal domain.
FT   CARBOHYD     31     31       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     52     52       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     58     58       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     70     70       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     78     78       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     97     97       N-linked (GlcNAc...).
FT   CARBOHYD    101    101       N-linked (GlcNAc...).
FT   CARBOHYD    115    115       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    159    159       N-linked (GlcNAc...).
FT   CARBOHYD    177    177       N-linked (GlcNAc...).
FT   CARBOHYD    214    214       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    219    219       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    232    232       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    240    240       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    252    252       N-linked (GlcNAc...) (high mannose).
FT   CARBOHYD    282    282       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    296    296       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    311    311       N-linked (GlcNAc...) (Potential).
FT   DISULFID     35     74
FT   DISULFID    149    185
FT   DISULFID    222    259
FT   DISULFID    327    364
FT   CONFLICT      1     10       MAAPGARRPL -> MRPPRAAAV (in Ref. 2).
FT   CONFLICT     25     26       LF -> IP (in Ref. 4; AAA39411).
FT   CONFLICT    385    385       V -> I (in Ref. 2 and 4).
SQ   SEQUENCE   406 AA;  43865 MW;  C1BD373548BB9655 CRC64;
     MAAPGARRPL LLLLLAGLAH GASALFEVKN NGTTCIMASF SASFLTTYET ANGSQIVNIS
     LPASAEVLKN GSSCGKENVS DPSLTITFGR GYLLTLNFTK NTTRYSVQHM YFTYNLSDTE
     HFPNAISKEI YTMDSTTDIK ADINKAYRCV SDIRVYMKNV TVVLRDATIQ AYLSSGNFSK
     EETHCTQDGP SPTTGPPSPS PPLVPTNPTV SKYNVTGNNG TCLLASMALQ LNITYLKKDN
     KTVTRAFNIS PNDTSSGSCG INLVTLKVEN KNRALELQFG MNASSSLFFL QGVRLNMTLP
     DALVPTFSIS NHSLKALQAT VGNSYKCNTE EHIFVSKMLS LNVFSVQVQA FKVDSDRFGS
     VEECVQDGNN MLIPIAVGGA LAGLVLIVLI AYLIGRKRSH AGYQTI
//
ID   DMD_MOUSE               Reviewed;        3678 AA.
AC   P11531; O35653; Q60703;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   08-MAR-2011, entry version 116.
DE   RecName: Full=Dystrophin;
GN   Name=Dmd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/10; TISSUE=Skeletal muscle;
RX   MEDLINE=92253376; PubMed=1579466; DOI=10.1093/nar/20.7.1725;
RA   Bies R.D., Phelps S.F., Cortez M.D., Roberts R., Caskey C.T.,
RA   Chamberlain J.S.;
RT   "Human and murine dystrophin mRNA transcripts are differentially
RT   expressed during skeletal muscle, heart, and brain development.";
RL   Nucleic Acids Res. 20:1725-1731(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-201.
RX   MEDLINE=87273512; PubMed=3607877; DOI=10.1016/0092-8674(87)90504-6;
RA   Koenig M., Hoffman E.P., Bertelson C.J., Monaco A.P., Feener C.,
RA   Kunkel L.M.;
RT   "Complete cloning of the Duchenne muscular dystrophy (DMD) cDNA and
RT   preliminary genomic organization of the DMD gene in normal and
RT   affected individuals.";
RL   Cell 50:509-517(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-176.
RC   STRAIN=129/J;
RX   MEDLINE=92182520; PubMed=1543903; DOI=10.1007/BF00570441;
RA   Maconochie M.K., Brown S.D.M., Greenfield A.J.;
RT   "Sequence analysis of two exons from the murine dystrophin locus.";
RL   Mamm. Genome 2:64-68(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 300-1390.
RX   MEDLINE=88018015; PubMed=3659917; DOI=10.1126/science.3659917;
RA   Hoffman E.P., Monaco A.P., Feener C.C., Kunkel L.M.;
RT   "Conservation of the Duchenne muscular dystrophy gene in mice and
RT   humans.";
RL   Science 238:347-350(1987).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 986-1056.
RC   STRAIN=C57BL/10; TISSUE=Skeletal muscle;
RX   MEDLINE=94154933; PubMed=8111539;
RA   Chamberlain J.S., Phelps S.F., Cox G.A., Maichele A.J.,
RA   Greenwood A.D.;
RT   "PCR analysis of muscular dystrophy in mdx mice.";
RL   Mol. Cell Biol. Hum. Dis. Ser. 3:167-189(1993).
RN   [6]
RP   PROTEIN SEQUENCE OF 1129-1134, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3069-3181.
RX   PubMed=1377655; DOI=10.1111/j.1432-0436.1992.tb00666.x;
RA   Rapaport D., Lederfein D., den Dunnen J.T., Grootscholten P.M.,
RA   van Ommen G.J.B., Fuchs O., Nudel U., Yaffe D.;
RT   "Characterization and cell type distribution of a novel, major
RT   transcript of the Duchenne muscular dystrophy gene.";
RL   Differentiation 49:187-193(1992).
RN   [8]
RP   ALTERNATIVE SPLICING, FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/10; TISSUE=Retina;
RX   MEDLINE=95360002; PubMed=7633443; DOI=10.1093/hmg/4.5.837;
RA   D'Souza V.N., Nguyen T.M., Morris G.E., Karges W., Pillers D.-A.M.,
RA   Ray P.N.;
RT   "A novel dystrophin isoform is required for normal retinal
RT   electrophysiology.";
RL   Hum. Mol. Genet. 4:837-842(1995).
RN   [9]
RP   INTERACTION WITH SNTA1 IN THE DYSTROPHIN-ASSOCIATED GLYCOPROTEIN
RP   COMPLEX.
RX   MEDLINE=96032613; PubMed=7547961; DOI=10.1021/bi00038a014;
RA   Madhavan R., Jarrett H.W.;
RT   "Interactions between dystrophin glycoprotein complex proteins.";
RL   Biochemistry 34:12204-12209(1995).
RN   [10]
RP   INTERACTION WITH SNTB1 IN THE DYSTROPHIN-ASSOCIATED GLYCOPROTEIN
RP   COMPLEX.
RX   MEDLINE=97362062; PubMed=9214383; DOI=10.1083/jcb.138.1.81;
RA   Peters M.F., Adams M.E., Froehner S.C.;
RT   "Differential association of syntrophin pairs with the dystrophin
RT   complex.";
RL   J. Cell Biol. 138:81-93(1997).
RN   [11]
RP   INTERACTION WITH DAG1 IN THE DYSTROPHIN-ASSOCIATED GLYCOPROTEIN
RP   COMPLEX.
RX   PubMed=11520903; DOI=10.1046/j.1471-4159.2001.00466.x;
RA   Moukhles H., Carbonetto S.;
RT   "Dystroglycan contributes to the formation of multiple dystrophin-like
RT   complexes in brain.";
RL   J. Neurochem. 78:824-834(2001).
RN   [12]
RP   INTERACTION WITH SYNM.
RX   PubMed=16777071; DOI=10.1016/j.bbrc.2006.05.192;
RA   Bhosle R.C., Michele D.E., Campbell K.P., Li Z., Robson R.M.;
RT   "Interactions of intermediate filament protein synemin with dystrophin
RT   and utrophin.";
RL   Biochem. Biophys. Res. Commun. 346:768-777(2006).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3617, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Anchors the extracellular matrix to the cytoskeleton via
CC       F-actin. Ligand for dystroglycan. Component of the dystrophin-
CC       associated glycoprotein complex which accumulates at the
CC       neuromuscular junction (NMJ) and at a variety of synapses in the
CC       peripheral and central nervous systems and has a structural
CC       function in stabilizing the sarcolemma. Also implicated in
CC       signaling events and synaptic transmission.
CC   -!- SUBUNIT: Interacts with SYNM. Interacts with the syntrophins SNTG1
CC       and SNTG2. Interacts with KRT19. Component of the dystrophin-
CC       associated glycoprotein complex which is composed of three
CC       subcomplexes: a cytoplasmic complex comprised of DMD (or UTRN),
CC       DTNA and a number of syntrophins, such as SNTB1, SNTB2, SNTG1 and
CC       SNTG2, the transmembrane dystroglycan complex, and the
CC       sarcoglycan-sarcospan complex. Interacts with DAG1 (betaDAG1) with
CC       DMD; the interaction is inhibited by phosphorylation on the PPXY
CC       motif of DAG1 (By similarity). Interacts with SYNM; SNTA1 and
CC       SNTB1.
CC   -!- INTERACTION:
CC       Q61234:Snta1; NbExp=1; IntAct=EBI-295928, EBI-295952;
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Peripheral
CC       membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=At least 11 isoforms are produced;
CC       Name=1;
CC         IsoId=P11531-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Differentially expressed during skeletal
CC       muscle, heart, and brain development. Also expressed in retina.
CC   -!- SIMILARITY: Contains 2 CH (calponin-homology) domains.
CC   -!- SIMILARITY: Contains 22 spectrin repeats.
CC   -!- SIMILARITY: Contains 1 WW domain.
CC   -!- SIMILARITY: Contains 1 ZZ-type zinc finger.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; M68859; AAB02797.1; -; mRNA.
DR   EMBL; X58153; CAA41157.1; -; Genomic_DNA.
DR   EMBL; M18025; AAA37530.1; -; mRNA.
DR   EMBL; U56724; AAB01216.1; -; Genomic_DNA.
DR   EMBL; U15218; AAA87068.1; -; mRNA.
DR   IPI; IPI00474450; -.
DR   PIR; S28916; S28916.
DR   RefSeq; NP_031894.1; NM_007868.5.
DR   UniGene; Mm.275608; -.
DR   UniGene; Mm.416750; -.
DR   ProteinModelPortal; P11531; -.
DR   SMR; P11531; 9-246, 3040-3354.
DR   IntAct; P11531; 7.
DR   MINT; MINT-85369; -.
DR   STRING; P11531; -.
DR   PhosphoSite; P11531; -.
DR   PRIDE; P11531; -.
DR   Ensembl; ENSMUST00000114000; ENSMUSP00000109633; ENSMUSG00000045103.
DR   GeneID; 13405; -.
DR   KEGG; mmu:13405; -.
DR   UCSC; uc009tri.1; mouse.
DR   CTD; 13405; -.
DR   MGI; MGI:94909; Dmd.
DR   HOGENOM; HBG403029; -.
DR   HOVERGEN; HBG005495; -.
DR   InParanoid; P11531; -.
DR   OrthoDB; EOG480HW7; -.
DR   NextBio; 283803; -.
DR   ArrayExpress; P11531; -.
DR   Bgee; P11531; -.
DR   CleanEx; MM_DMD; -.
DR   Genevestigator; P11531; -.
DR   GO; GO:0030055; C:cell-substrate junction; IDA:MGI.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0016010; C:dystrophin-associated glycoprotein complex; IDA:MGI.
DR   GO; GO:0045121; C:membrane raft; IDA:MGI.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0044306; C:neuron projection terminus; IDA:MGI.
DR   GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0030018; C:Z disc; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0050998; F:nitric-oxide synthase binding; IPI:BHF-UCL.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0046716; P:muscle cell homeostasis; IMP:MGI.
DR   GO; GO:0045213; P:neurotransmitter receptor metabolic process; IMP:MGI.
DR   GO; GO:0021629; P:olfactory nerve structural organization; IMP:MGI.
DR   GO; GO:0045449; P:regulation of transcription; IMP:MGI.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR016344; Dystrophin/utrophin.
DR   InterPro; IPR015153; EF-hand_dom_typ1.
DR   InterPro; IPR015154; EF-hand_dom_typ2.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   InterPro; IPR000433; Znf_ZZ.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 2.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF09068; efhand_1; 1.
DR   Pfam; PF09069; efhand_2; 1.
DR   Pfam; PF00435; Spectrin; 15.
DR   Pfam; PF00397; WW; 1.
DR   Pfam; PF00569; ZZ; 1.
DR   PIRSF; PIRSF002341; Dystrophin/utrophin; 1.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00150; SPEC; 22.
DR   SMART; SM00456; WW; 1.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   SUPFAM; SSF51045; WW_Rsp5_WWP; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Calcium; Cell membrane;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane;
KW   Metal-binding; Phosphoprotein; Repeat; Zinc; Zinc-finger.
FT   CHAIN         1   3678       Dystrophin.
FT                                /FTId=PRO_0000076076.
FT   DOMAIN        1    240       Actin-binding.
FT   DOMAIN       15    119       CH 1.
FT   DOMAIN      134    237       CH 2.
FT   REPEAT      341    449       Spectrin 1.
FT   REPEAT      450    558       Spectrin 2.
FT   REPEAT      561    669       Spectrin 3.
FT   REPEAT      721    830       Spectrin 4.
FT   REPEAT      832    936       Spectrin 5.
FT   REPEAT      945   1047       Spectrin 6.
FT   REPEAT     1050   1156       Spectrin 7.
FT   REPEAT     1159   1265       Spectrin 8.
FT   REPEAT     1268   1369       Spectrin 9.
FT   REPEAT     1470   1570       Spectrin 10.
FT   REPEAT     1573   1678       Spectrin 11.
FT   REPEAT     1681   1782       Spectrin 12.
FT   REPEAT     1879   1981       Spectrin 13.
FT   REPEAT     2013   2103       Spectrin 14.
FT   REPEAT     2106   2210       Spectrin 15.
FT   REPEAT     2213   2318       Spectrin 16.
FT   REPEAT     2468   2570       Spectrin 17.
FT   REPEAT     2573   2679       Spectrin 18.
FT   REPEAT     2682   2795       Spectrin 19.
FT   REPEAT     2798   2900       Spectrin 20.
FT   REPEAT     2902   2924       Spectrin 21.
FT   REPEAT     2927   3033       Spectrin 22.
FT   DOMAIN     3048   3081       WW.
FT   ZN_FING    3300   3347       ZZ-type.
FT   REGION     1417   1915       Interaction with SYNM.
FT   REGION     3051   3401       Interaction with SYNM.
FT   REGION     3459   3511       Binds to SNTB1 (By similarity).
FT   MOD_RES    1592   1592       Phosphothreonine (By similarity).
FT   MOD_RES    3476   3476       Phosphoserine (By similarity).
FT   MOD_RES    3606   3606       Phosphoserine (By similarity).
FT   MOD_RES    3609   3609       Phosphothreonine (By similarity).
FT   MOD_RES    3610   3610       Phosphoserine (By similarity).
FT   MOD_RES    3614   3614       Phosphoserine (By similarity).
FT   MOD_RES    3616   3616       Phosphoserine (By similarity).
FT   MOD_RES    3617   3617       Phosphoserine.
FT   MOD_RES    3645   3645       Phosphothreonine (By similarity).
FT   MOD_RES    3659   3659       Phosphoserine (By similarity).
FT   CONFLICT    463    463       D -> H (in Ref. 4; AAA37530).
FT   CONFLICT    677    677       S -> F (in Ref. 4; AAA37530).
FT   CONFLICT   2337   2337       V -> L (in Ref. 1; AAB02797).
SQ   SEQUENCE   3678 AA;  425817 MW;  1D2E74CF7DB035EE CRC64;
     MLWWEEVEDC YEREDVQKKT FTKWINAQFS KFGKQHIDNL FSDLQDGKRL LDLLEGLTGQ
     KLPKEKGSTR VHALNNVNKA LRVLQKNNVD LVNIGSTDIV DGNHKLTLGL IWNIILHWQV
     KNVMKTIMAG LQQTNSEKIL LSWVRQSTRN YPQVNVINFT SSWSDGLALN ALIHSHRPDL
     FDWNSVVSQH SATQRLEHAF NIAKCQLGIE KLLDPEDVAT TYPDKKSILM YITSLFQVLP
     QQVSIEAIQE VEMLPRTSSK VTREEHFQLH HQMHYSQQIT VSLAQGYEQT SSSPKPRFKS
     YAFTQAAYVA TSDSTQSPYP SQHLEAPRDK SLDSSLMETE VNLDSYQTAL EEVLSWLLSA
     EDTLRAQGEI SNDVEEVKEQ FHAHEGFMMD LTSHQGLVGN VLQLGSQLVG KGKLSEDEEA
     EVQEQMNLLN SRWECLRVAS MEKQSKLHKV LMDLQNQKLK ELDDWLTKTE ERTKKMEEEP
     FGPDLEDLKC QVQQHKVLQE DLEQEQVRVN SLTHMVVVVD ESSGDHATAA LEEQLKVLGD
     RWANICRWTE DRWIVLQDIL LKWQHFTEEQ CLFSTWLSEK EDAMKNIQTS GFKDQNEMMS
     SLHKISTLKI DLEKKKPTME KLSSLNQDLL SALKNKSVTQ KMEIWMENFA QRWDNLTQKL
     EKSSAQISQA VTTTQPSLTQ TTVMETVTMV TTREQIMVKH AQEELPPPPP QKKRQITVDS
     ELRKRLDVDI TELHSWITRS EAVLQSSEFA VYRKEGNISD LQEKVNAIAR EKAEKFRKLQ
     DASRSAQALV EQMANEGVNA ESIRQASEQL NSRWTEFCQL LSERVNWLEY QTNIITFYNQ
     LQQLEQMTTT AENLLKTQST TLSEPTAIKS QLKICKDEVN RLSALQPQIE QLKIQSLQLK
     EKGQGPMFLD ADFVAFTNHF NHIFDGVRAK EKELQTIFDT LPPMRYQETM SSIRTWIQQS
     ESKLSVPYLS VTEYEIMEER LGKLQALQSS LKEQQNGFNY LSDTVKEMAK KAPSEICQKY
     LSEFEEIEGH WKKLSSQLVE SCQKLEEHMN KLRKFQNHIK TLQKWMAEVD VFLKEEWPAL
     GDAEILKKQL KQCRLLVGDI QTIQPSLNSV NEGGQKIKSE AELEFASRLE TELRELNTQW
     DHICRQVYTR KEALKAGLDK TVSLQKDLSE MHEWMTQAEE EYLERDFEYK TPDELQTAVE
     EMKRAKEEAL QKETKVKLLT ETVNSVIAHA PPSAQEALKK ELETLTTNYQ WLCTRLNGKC
     KTLEEVWACW HELLSYLEKA NKWLNEVELK LKTMENVPAG PEEITEVLES LENLMHHSEE
     NPNQIRLLAQ TLTDGGVMDE LINEELETFN SRWRELHEEA VRKQKLLEQS IQSAQEIEKS
     LHLIQESLEF IDKQLAAYIT DKVDAAQMPQ EAQKIQSDLT SHEISLEEMK KHNQGKDANQ
     RVLSQIDVAQ KKLQDVSMKF RLFQKPANFE QRLEESKMIL DEVKMHLPAL ETKSVEQEVI
     QSQLSHCVNL YKSLSEVKSE VEMVIKTGRQ IVQKKQTENP KELDERVTAL KLHYNELGAK
     VTERKQQLEK CLKLSRKMRK EMNVLTEWLA ATDTELTKRS AVEGMPSNLD SEVAWGKATQ
     KEIEKQKAHL KSVTELGESL KMVLGKKETL VEDKLSLLNS NWIAVTSRVE EWLNLLLEYQ
     KHMETFDQNI EQITKWIIHA DELLDESEKK KPQQKEDILK RLKAEMNDMR PKVDSTRDQA
     AKLMANRGDH CRKVVEPQIS ELNRRFAAIS HRIKTGKASI PLKELEQFNS DIQKLLEPLE
     AEIQQGVNLK EEDFNKDMSE DNEGTVNELL QRGDNLQQRI TDERKREEIK IKQQLLQTKH
     NALKDLRSQR RKKALEISHQ WYQYKRQADD LLKCLDEIEK KLASLPEPRD ERKLKEIDRE
     LQKKKEELNA VRRQAEGLSE NGAAMAVEPT QIQLSKRWRQ IESNFAQFRR LNFAQIHTLH
     EETMVVTTED MPLDVSYVPS TYLTEISHIL QALSEVDHLL NTPELCAKDF EDLFKQEESL
     KNIKDNLQQI SGRIDIIHKK KTAALQSATS MEKVKVQEAV AQMDFQGEKL HRMYKERQGR
     FDRSVEKWRH FHYDMKVFNQ WLNEVEQFFK KTQNPENWEH AKYKWYLKEL QDGIGQRQAV
     VRTLNATGEE IIQQSSKTDV NILQEKLGSL SLRWHDICKE LAERRKRIEE QKNVLSEFQR
     DLNEFVLWLE EADNIAITPL GDEQQLKEQL EQVKLLAEEL PLRQGILKQL NETGGAVLVS
     APIRPEEQDK LEKKLKQTNL QWIKVSRALP EKQGELEVHL KDFRQLEEQL DHLLLWVSPI
     RNQLEIYNQP SQAGPFDIKE IEVTVHGKQA DVERLLSKGQ HLYKEKPSTQ PVKRKLEDLR
     SEWEAVNHLL RELRTKQPDR APGLSTTGAS ASQTVTLVTQ SVVTKETVIS KLEMPSSLLL
     EVPALADFNR AWTELTDWLS LLDRVIKSQR VMVGDLEDIN EMIIKQKATL QDLEQRRPQL
     EELITAAQNL KNKTSNQEAR TIITDRIERI QIQWDEVQEQ LQNRRQQLNE MLKDSTQWLE
     AKEEAEQVIG QVRGKLDSWK EGPHTVDAIQ KKITETKQLA KDLRQRQISV DVANDLALKL
     LRDYSADDTR KVHMITENIN TSWGNIHKRV SEQEAALEET HRLLQQFPLD LEKFLSWITE
     AETTANVLQD ASRKEKLLED SRGVRELMKP WQDLQGEIET HTDIYHNLDE NGQKILRSLE
     GSDEAPLLQR RLDNMNFKWS ELQKKSLNIR SHLEASSDQW KRLHLSLQEL LVWLQLKDDE
     LSRQAPIGGD FPAVQKQNDI HRAFKRELKT KEPVIMSTLE TVRIFLTEQP LEGLEKLYQE
     PRELPPEERA QNVTRLLRKQ AEEVNAEWDK LNLRSADWQR KIDEALERLQ ELQEAADELD
     LKLRQAEVIK GSWQPVGDLL IDSLQDHLEK VKALRGEIAP LKENVNRVND LAHQLTTLGI
     QLSPYNLSTL EDLNTRWRLL QVAVEDRVRQ LHEAHRDFGP ASQHFLSTSV QGPWERAISP
     NKVPYYINHE TQTTCWDHPK MTELYQSLAD LNNVRFSAYR TAMKLRRLQK ALCLDLLSLS
     AACDALDQHN LKQNDQPMDI LQIINCLTTI YDRLEQEHNN LVNVPLCVDM CLNWLLNVYD
     TGRTGRIRVL SFKTGIISLC KAHLEDKYRY LFKQVASSTG FCDQRRLGLL LHDSIQIPRQ
     LGEVASFGGS NIEPSVRSCF QFANNKPEIE AALFLDWMRL EPQSMVWLPV LHRVAAAETA
     KHQAKCNICK ECPIIGFRYR SLKHFNYDIC QSCFFSGRVA KGHKMHYPMV EYCTPTTSGE
     DVRDFAKVLK NKFRTKRYFA KHPRMGYLPV QTVLEGDNME TPVTLINFWP VDSAPASSPQ
     LSHDDTHSRI EHYASRLAEM ENSNGSYLND SISPNESIDD EHLLIQHYCQ SLNQDSPLSQ
     PRSPAQILIS LESEERGELE RILADLEEEN RNLQAEYDRL KQQHEHKGLS PLPSPPEMMP
     TSPQSPRDAE LIAEAKLLRQ HKGRLEARMQ ILEDHNKQLE SQLHRLRQLL EQPQAEAKVN
     GTTVSSPSTS LQRSDSSQPM LLRVVGSQTS ESMGEEDLLS PPQDTSTGLE EVMEQLNNSF
     PSSRGRNAPG KPMREDTM
//
ID   KCC2A_MOUSE             Reviewed;         478 AA.
AC   P11798; Q61284; Q6ZWN4;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 126.
DE   RecName: Full=Calcium/calmodulin-dependent protein kinase type II subunit alpha;
DE            Short=CaM kinase II subunit alpha;
DE            Short=CaMK-II subunit alpha;
DE            EC=2.7.11.17;
GN   Name=Camk2a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=89282416; PubMed=2543961; DOI=10.1093/nar/17.10.3992;
RA   Hanley R.M., Payne M.E., Cruzalegui F., Christenson M.A., Means A.R.;
RT   "Sequence of the cDNA for the alpha subunit of calmodulin kinase II
RT   from mouse brain.";
RL   Nucleic Acids Res. 17:3992-3992(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA KAP).
RC   STRAIN=BALB/c; TISSUE=Skeletal muscle;
RX   MEDLINE=96104551; PubMed=8524307;
RA   Bayer K.-U., Loehler J., Harbers K.;
RT   "An alternative, nonkinase product of the brain-specifically expressed
RT   Ca2+/calmodulin-dependent kinase II alpha isoform gene in skeletal
RT   muscle.";
RL   Mol. Cell. Biol. 16:29-36(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 9-21; 33-42; 135-146; 260-267; 301-311; 329-344;
RP   353-371; 397-405; 434-445 AND 470-478, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15648052; DOI=10.1002/pmic.200401066;
RA   Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA   Hart G.W., Burlingame A.L.;
RT   "Quantitative analysis of both protein expression and serine /
RT   threonine post-translational modifications through stable isotope
RT   labeling with dithiothreitol.";
RL   Proteomics 5:388-398(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-13, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275; THR-286; SER-333;
RP   THR-334 AND THR-337, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: CaM-kinase II (CAMK2) is a prominent kinase in the
CC       central nervous system that may function in long-term potentiation
CC       and neurotransmitter release. Member of the NMDAR signaling
CC       complex in excitatory synapses it may regulate NMDAR-dependent
CC       potentiation of the AMPAR and synaptic plasticity (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Autophosphorylation of Thr-286 allows the
CC       kinase to switch from a calmodulin-dependent to a calmodulin-
CC       independent state (By similarity).
CC   -!- SUBUNIT: CAMK2 is composed of four different chains: alpha, beta,
CC       gamma, and delta. The different isoforms assemble into homo- or
CC       heteromultimeric holoenzymes composed of 8 to 12 subunits.
CC       Interacts with BAALC, MPDZ, SYN1, CAMK2N2 and SYNGAP1 (By
CC       similarity).
CC   -!- INTERACTION:
CC       Q62108:Dlg4; NbExp=1; IntAct=EBI-400384, EBI-300895;
CC   -!- SUBCELLULAR LOCATION: Isoform Alpha KAP: Cytoplasm (Probable).
CC       Cell junction, synapse, presynaptic cell membrane (By similarity).
CC       Cell junction, synapse (By similarity). Note=Postsynaptic lipid
CC       rafts (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Alpha CaMKII;
CC         IsoId=P11798-1; Sequence=Displayed;
CC       Name=Alpha KAP;
CC         IsoId=P11798-2; Sequence=VSP_004767, VSP_004768, VSP_004769;
CC         Note=Has no kinase activity;
CC   -!- TISSUE SPECIFICITY: Isoform Alpha CaMKII is expressed in brain
CC       while isoform Alpha KAP is expressed in skeletal muscle.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. CaMK subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; X14836; CAA32946.1; -; mRNA.
DR   EMBL; X87142; CAA60620.1; -; mRNA.
DR   EMBL; AK083245; BAC38829.1; -; mRNA.
DR   EMBL; BC031745; AAH31745.1; -; mRNA.
DR   IPI; IPI00230096; -.
DR   IPI; IPI00621806; -.
DR   PIR; JC6083; JC6083.
DR   PIR; S04365; S04365.
DR   RefSeq; NP_033922.1; NM_009792.3.
DR   RefSeq; NP_803126.1; NM_177407.4.
DR   UniGene; Mm.131530; -.
DR   PDB; 1HKX; X-ray; 2.65 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=336-478.
DR   PDBsum; 1HKX; -.
DR   ProteinModelPortal; P11798; -.
DR   SMR; P11798; 9-300, 336-474.
DR   DIP; DIP-31593N; -.
DR   IntAct; P11798; 51.
DR   MINT; MINT-136541; -.
DR   STRING; P11798; -.
DR   PhosphoSite; P11798; -.
DR   PRIDE; P11798; -.
DR   Ensembl; ENSMUST00000102887; ENSMUSP00000099951; ENSMUSG00000024617.
DR   Ensembl; ENSMUST00000102888; ENSMUSP00000099952; ENSMUSG00000024617.
DR   Ensembl; ENSMUST00000115295; ENSMUSP00000110950; ENSMUSG00000024617.
DR   GeneID; 12322; -.
DR   KEGG; mmu:12322; -.
DR   UCSC; uc008fbg.1; mouse.
DR   UCSC; uc008fbh.1; mouse.
DR   CTD; 12322; -.
DR   MGI; MGI:88256; Camk2a.
DR   eggNOG; roNOG13785; -.
DR   GeneTree; ENSGT00550000074354; -.
DR   HOVERGEN; HBG108055; -.
DR   OrthoDB; EOG42JNR7; -.
DR   PhylomeDB; P11798; -.
DR   BRENDA; 2.7.11.17; 244.
DR   NextBio; 280898; -.
DR   ArrayExpress; P11798; -.
DR   Bgee; P11798; -.
DR   Genevestigator; P11798; -.
DR   GermOnline; ENSMUSG00000024617; Mus musculus.
DR   GO; GO:0005954; C:calcium- and calmodulin-dependent protein kinase complex; TAS:UniProtKB.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:EC.
DR   GO; GO:0035254; F:glutamate receptor binding; IPI:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; IMP:MGI.
DR   GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:MGI.
DR   GO; GO:0046928; P:regulation of neurotransmitter secretion; IMP:MGI.
DR   InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF08332; CaMKII_AD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Calmodulin-binding;
KW   Cell junction; Cell membrane; Cytoplasm; Direct protein sequencing;
KW   Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Synapse; Transferase.
FT   CHAIN         1    478       Calcium/calmodulin-dependent protein
FT                                kinase type II subunit alpha.
FT                                /FTId=PRO_0000086092.
FT   DOMAIN       13    271       Protein kinase.
FT   NP_BIND      19     27       ATP (By similarity).
FT   REGION      290    300       Calmodulin-binding.
FT   REGION      310    320       Interaction with BAALC (By similarity).
FT   ACT_SITE    135    135       Proton acceptor.
FT   BINDING      42     42       ATP (By similarity).
FT   MOD_RES      13     13       Phosphotyrosine.
FT   MOD_RES      25     25       Phosphoserine.
FT   MOD_RES     275    275       Phosphoserine.
FT   MOD_RES     286    286       Phosphothreonine; by autocatalysis.
FT   MOD_RES     333    333       Phosphoserine.
FT   MOD_RES     334    334       Phosphothreonine.
FT   MOD_RES     337    337       Phosphothreonine.
FT   VAR_SEQ       1    289       Missing (in isoform Alpha KAP).
FT                                /FTId=VSP_004767.
FT   VAR_SEQ     290    314       LKKFNARRKLKGAILTTMLATRNFS -> MLLFLTLWALVP
FT                                CLVLLTLYFLSST (in isoform Alpha KAP).
FT                                /FTId=VSP_004768.
FT   VAR_SEQ     328    328       K -> KKRKSSSSVQLM (in isoform Alpha KAP).
FT                                /FTId=VSP_004769.
FT   CONFLICT     40     40       A -> P (in Ref. 1; CAA32946).
FT   CONFLICT    169    169       A -> R (in Ref. 1; CAA32946).
FT   CONFLICT    228    228       G -> R (in Ref. 1; CAA32946).
FT   TURN        338    340
FT   HELIX       341    362
FT   HELIX       366    372
FT   STRAND      373    380
FT   HELIX       382    384
FT   STRAND      389    392
FT   HELIX       393    400
FT   HELIX       404    406
FT   STRAND      410    421
FT   STRAND      423    437
FT   STRAND      445    458
FT   STRAND      461    472
SQ   SEQUENCE   478 AA;  54115 MW;  306F416CCE9B5F62 CRC64;
     MATITCTRFT EEYQLFEELG KGAFSVVRRC VKVLAGQEYA AKIINTKKLS ARDHQKLERE
     ARICRLLKHP NIVRLHDSIS EEGHHYLIFD LVTGGELFED IVAREYYSEA DASHCIQQIL
     EAVLHCHQMG VVHRDLKPEN LLLASKLKGA AVKLADFGLA IEVEGEQQAW FGFAGTPGYL
     SPEVLRKDPY GKPVDLWACG VILYILLVGY PPFWDEDQHR LYQQIKAGAY DFPSPEWDTV
     TPEAKDLINK MLTINPSKRI TAAEALKHPW ISHRSTVASC MHRQETVDCL KKFNARRKLK
     GAILTTMLAT RNFSGGKSGG NKKNDGVKES SESTNTTIED EDTKVRKQEI IKVTEQLIEA
     ISNGDFESYT KMCDPGMTAF EPEALGNLVE GLDFHRFYFE NLWSRNSKPV HTTILNPHIH
     LMGDESACIA YIRITQYLDA GGIPRTAQSE ETRVWHRRDG KWQIVHFHRS GAPSVLPH
//
ID   ITPR1_MOUSE             Reviewed;        2749 AA.
AC   P11881; P20943; Q99LG5;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   08-MAR-2011, entry version 136.
DE   RecName: Full=Inositol 1,4,5-trisphosphate receptor type 1;
DE   AltName: Full=IP3 receptor isoform 1;
DE            Short=IP3R 1;
DE            Short=InsP3R1;
DE   AltName: Full=Inositol 1,4,5-trisphosphate-binding protein P400;
DE   AltName: Full=Protein PCD-6;
DE   AltName: Full=Purkinje cell protein 1;
DE   AltName: Full=Type 1 inositol 1,4,5-trisphosphate receptor;
DE            Short=Type 1 InsP3 receptor;
GN   Name=Itpr1; Synonyms=Insp3r, Pcd6, Pcp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Purkinje cell;
RX   MEDLINE=90044039; PubMed=2554142; DOI=10.1038/342032a0;
RA   Furuichi T., Yoshikawa S., Miyawaki A., Wada K., Maeda N.,
RA   Mikoshiba K.;
RT   "Primary structure and functional expression of the inositol 1,4,5-
RT   trisphosphate-binding protein P400.";
RL   Nature 342:32-38(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=ICR; TISSUE=Cerebellum;
RX   MEDLINE=89345101; PubMed=2762133; DOI=10.1093/nar/17.13.5385;
RA   Furuichi T., Yoshikawa S., Mikoshiba K.;
RT   "Nucleotide sequence of cDNA encoding P400 protein in the mouse
RT   cerebellum.";
RL   Nucleic Acids Res. 17:5385-5386(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 318-332 AND 1692-1731, AND
RP   ALTERNATIVE SPLICING.
RC   STRAIN=ICR;
RX   MEDLINE=91296797; PubMed=1648733; DOI=10.1073/pnas.88.14.6244;
RA   Nakagawa T., Okano H., Furuichi T., Aruga J., Mikoshiba K.;
RT   "The subtypes of the mouse inositol 1,4,5-trisphosphate receptor are
RT   expressed in a tissue-specific and developmentally specific manner.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:6244-6248(1991).
RN   [5]
RP   PROTEIN SEQUENCE OF 862-871, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2098-2749.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2250-2749.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=89068131; PubMed=3199205;
RA   Nordquist D.T., Kozak C.A., Orr H.T.;
RT   "cDNA cloning and characterization of three genes uniquely expressed
RT   in cerebellum by Purkinje neurons.";
RL   J. Neurosci. 8:4780-4789(1988).
RN   [8]
RP   INTERACTION WITH AHCYL1.
RX   MEDLINE=22526701; PubMed=12525476; DOI=10.1074/jbc.M210119200;
RA   Ando H., Mizutani A., Matsu-ura T., Mikoshiba K.;
RT   "IRBIT, a novel inositol 1,4,5-trisphosphate (IP3) receptor-binding
RT   protein, is released from the IP3 receptor upon IP3 binding to the
RT   receptor.";
RL   J. Biol. Chem. 278:10602-10612(2003).
RN   [9]
RP   INTERACTION WITH ERP44, AND MUTAGENESIS OF CYS-2496; CYS-2504 AND
RP   CYS-2527.
RX   PubMed=15652484; DOI=10.1016/j.cell.2004.11.048;
RA   Higo T., Hattori M., Nakamura T., Natsume T., Michikawa T.,
RA   Mikoshiba K.;
RT   "Subtype-specific and ER lumenal environment-dependent regulation of
RT   inositol 1,4,5-trisphosphate receptor type 1 by ERp44.";
RL   Cell 120:85-98(2005).
RN   [10]
RP   INTERACTION WITH AHCYL1.
RX   PubMed=16527252; DOI=10.1016/j.bbrc.2006.02.119;
RA   Devogelaere B., Nadif Kasri N., Derua R., Waelkens E., Callewaert G.,
RA   Missiaen L., Parys J.B., De Smedt H.;
RT   "Binding of IRBIT to the IP3 receptor: determinants and functional
RT   effects.";
RL   Biochem. Biophys. Res. Commun. 343:49-56(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1588, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1588, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1588, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1588, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-223.
RX   PubMed=15664189; DOI=10.1016/j.molcel.2004.11.047;
RA   Bosanac I., Yamazaki H., Matsu-Ura T., Michikawa T., Mikoshiba K.,
RA   Ikura M.;
RT   "Crystal structure of the ligand binding suppressor domain of type 1
RT   inositol 1,4,5-trisphosphate receptor.";
RL   Mol. Cell 17:193-203(2005).
RN   [16]
RP   INTERACTION WITH MRVI1.
RX   PubMed=16990611; DOI=10.1182/blood-2005-10-026294;
RA   Antl M., von Bruehl M.-L., Eiglsperger C., Werner M., Konrad I.,
RA   Kocher T., Wilm M., Hofmann F., Massberg S., Schlossmann J.;
RT   "IRAG mediates NO/cGMP-dependent inhibition of platelet aggregation
RT   and thrombus formation.";
RL   Blood 109:552-559(2007).
CC   -!- FUNCTION: Intracellular channel that mediates calcium release from
CC       the endoplasmic reticulum following stimulation by inositol 1,4,5-
CC       trisphosphate.
CC   -!- SUBUNIT: Homotetramer. Interacts with TRPC4. The PPXXF motif binds
CC       HOM1, HOM2 and HOM3. Interacts with RYR1, RYR2, ITPR1, SHANK1 and
CC       SHANK3. Part of cGMP kinase signaling complex at least composed of
CC       ACTA2/alpha-actin, CNN1/calponin H1, PLN/phospholamban, PRKG1 and
CC       ITPR1 (By similarity). Interacts with ERP44 in a pH-, redox state-
CC       and calcium-dependent manner which results in the inhibition the
CC       calcium channel activity. The strength of this interaction
CC       inversely correlates with calcium concentration. Interacts with
CC       AHCYL1 and MRVI1. Interacts with CABP1 (By similarity).
CC   -!- INTERACTION:
CC       Q9D1Q6:Erp44; NbExp=2; IntAct=EBI-541478, EBI-541567;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC         Comment=There is a combination of two alternatively spliced
CC         domains at site SI and site SII (A, B and C). Experimental
CC         confirmation may be lacking for some isoforms;
CC       Name=1; Synonyms=SISIIABC;
CC         IsoId=P11881-1; Sequence=Displayed;
CC       Name=2; Synonyms=SI-SIIABC;
CC         IsoId=P11881-2; Sequence=VSP_002691;
CC       Name=3; Synonyms=SISIIAC;
CC         IsoId=P11881-3; Sequence=VSP_002693;
CC       Name=4; Synonyms=SI-SIIAC;
CC         IsoId=P11881-4; Sequence=VSP_002691, VSP_002693;
CC       Name=5; Synonyms=SISIIA;
CC         IsoId=P11881-5; Sequence=VSP_002693, VSP_002694;
CC       Name=6; Synonyms=SI-SIIA;
CC         IsoId=P11881-6; Sequence=VSP_002691, VSP_002693, VSP_002694;
CC       Name=7; Synonyms=SISII;
CC         IsoId=P11881-7; Sequence=VSP_002692, VSP_002693, VSP_002694;
CC       Name=8; Synonyms=SI-SII;
CC         IsoId=P11881-8; Sequence=VSP_002691, VSP_002692, VSP_002693,
CC                                  VSP_002694;
CC   -!- DOMAIN: The receptor contains a calcium channel in its C-terminal
CC       extremity. Its large N-terminal cytoplasmic region has the ligand-
CC       binding site in the N-terminus and modulatory sites in the middle
CC       portion immediately upstream of the channel region.
CC   -!- PTM: Phosphorylated by cAMP kinase. Phosphorylation prevents the
CC       ligand-induced opening of the calcium channels.
CC   -!- PTM: Phosphorylated on tyrosine residues (By similarity).
CC   -!- MISCELLANEOUS: Calcium appears to inhibit ligand binding to the
CC       receptor, most probably by interacting with a distinct calcium-
CC       binding protein which then inhibits the receptor.
CC   -!- SIMILARITY: Belongs to the InsP3 receptor family.
CC   -!- SIMILARITY: Contains 5 MIR domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA88319.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=AAH03271.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; X15373; CAA33433.1; -; mRNA.
DR   EMBL; AC120411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC153986; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC156506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M75986; AAA39316.1; -; Genomic_DNA.
DR   EMBL; M75987; AAA39317.1; -; Genomic_DNA.
DR   EMBL; BC003271; AAH03271.1; ALT_INIT; mRNA.
DR   EMBL; M21530; AAA88319.1; ALT_INIT; mRNA.
DR   IPI; IPI00117630; -.
DR   IPI; IPI00230018; -.
DR   IPI; IPI00230019; -.
DR   IPI; IPI00230020; -.
DR   IPI; IPI00230021; -.
DR   IPI; IPI00230023; -.
DR   IPI; IPI00469221; -.
DR   IPI; IPI00474081; -.
DR   PIR; S04844; ACMSIT.
DR   RefSeq; NP_034715.3; NM_010585.4.
DR   UniGene; Mm.227912; -.
DR   PDB; 1N4K; X-ray; 2.20 A; A=224-604.
DR   PDB; 1XZZ; X-ray; 1.80 A; A=2-223.
DR   PDBsum; 1N4K; -.
DR   PDBsum; 1XZZ; -.
DR   ProteinModelPortal; P11881; -.
DR   DIP; DIP-32243N; -.
DR   IntAct; P11881; 9.
DR   STRING; P11881; -.
DR   PhosphoSite; P11881; -.
DR   PRIDE; P11881; -.
DR   Ensembl; ENSMUST00000032192; ENSMUSP00000032192; ENSMUSG00000030102.
DR   Ensembl; ENSMUST00000113204; ENSMUSP00000108830; ENSMUSG00000030102.
DR   Ensembl; ENSMUST00000113207; ENSMUSP00000108833; ENSMUSG00000030102.
DR   Ensembl; ENSMUST00000113208; ENSMUSP00000108834; ENSMUSG00000030102.
DR   GeneID; 16438; -.
DR   KEGG; mmu:16438; -.
DR   UCSC; uc009ddh.1; mouse.
DR   MGI; MGI:96623; Itpr1.
DR   eggNOG; roNOG05144; -.
DR   HOGENOM; HBG315164; -.
DR   HOVERGEN; HBG052158; -.
DR   InParanoid; P11881; -.
DR   OrthoDB; EOG4Z62MP; -.
DR   ArrayExpress; P11881; -.
DR   Bgee; P11881; -.
DR   CleanEx; MM_ITPR1; -.
DR   Genevestigator; P11881; -.
DR   GermOnline; ENSMUSG00000030102; Mus musculus.
DR   GO; GO:0005955; C:calcineurin complex; IDA:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0005637; C:nuclear inner membrane; IDA:MGI.
DR   GO; GO:0005730; C:nucleolus; IDA:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IDA:MGI.
DR   GO; GO:0005220; F:inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IEA:InterPro.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IGI:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0001666; P:response to hypoxia; IDA:BHF-UCL.
DR   GO; GO:0050882; P:voluntary musculoskeletal movement; IMP:MGI.
DR   InterPro; IPR000699; Ca-rel_channel.
DR   InterPro; IPR014821; Ins145_P3_rcpt.
DR   InterPro; IPR000493; InsP3_rcpt-bd.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003608; MIR.
DR   InterPro; IPR016093; MIR_motif.
DR   InterPro; IPR013662; RIH_assoc-dom.
DR   InterPro; IPR015925; Ryanodine_recept-rel.
DR   PANTHER; PTHR13715; Ryanodine_recept-rel; 1.
DR   Pfam; PF08709; Ins145_P3_rec; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02815; MIR; 1.
DR   Pfam; PF08454; RIH_assoc; 1.
DR   Pfam; PF01365; RYDR_ITPR; 2.
DR   PRINTS; PR00779; INSP3RECEPTR.
DR   SMART; SM00472; MIR; 4.
DR   SUPFAM; SSF82109; MIR; 2.
DR   PROSITE; PS50919; MIR; 5.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Calcium channel;
KW   Calcium transport; Direct protein sequencing; Endoplasmic reticulum;
KW   Ion transport; Ionic channel; Ligand-gated ion channel; Membrane;
KW   Phosphoprotein; Receptor; Repeat; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1   2749       Inositol 1,4,5-trisphosphate receptor
FT                                type 1.
FT                                /FTId=PRO_0000153921.
FT   TOPO_DOM      1   2273       Cytoplasmic (Potential).
FT   TRANSMEM   2274   2294       Helical; (Potential).
FT   TOPO_DOM   2295   2305       Lumenal (Potential).
FT   TRANSMEM   2306   2326       Helical; (Potential).
FT   TOPO_DOM   2327   2352       Cytoplasmic (Potential).
FT   TRANSMEM   2353   2373       Helical; (Potential).
FT   TOPO_DOM   2374   2396       Lumenal (Potential).
FT   TRANSMEM   2397   2417       Helical; (Potential).
FT   TOPO_DOM   2418   2439       Cytoplasmic (Potential).
FT   TRANSMEM   2440   2460       Helical; (Potential).
FT   TOPO_DOM   2461   2569       Lumenal (Potential).
FT   TRANSMEM   2570   2590       Helical; (Potential).
FT   TOPO_DOM   2591   2749       Cytoplasmic (Potential).
FT   DOMAIN      112    166       MIR 1.
FT   DOMAIN      173    223       MIR 2.
FT   DOMAIN      231    287       MIR 3.
FT   DOMAIN      294    373       MIR 4.
FT   DOMAIN      379    435       MIR 5.
FT   REGION     2463   2528       Interaction with ERP44.
FT   MOD_RES     482    482       Phosphotyrosine (Potential).
FT   MOD_RES     703    703       Phosphoserine (By similarity).
FT   MOD_RES    1588   1588       Phosphoserine.
FT   MOD_RES    1755   1755       Phosphoserine; by PKA (Potential).
FT   MOD_RES    2655   2655       Phosphotyrosine (Potential).
FT   VAR_SEQ     318    332       Missing (in isoform 2, isoform 4, isoform
FT                                6 and isoform 8).
FT                                /FTId=VSP_002691.
FT   VAR_SEQ    1692   1714       Missing (in isoform 7 and isoform 8).
FT                                /FTId=VSP_002692.
FT   VAR_SEQ    1715   1715       Missing (in isoform 3, isoform 4, isoform
FT                                5, isoform 6, isoform 7 and isoform 8).
FT                                /FTId=VSP_002693.
FT   VAR_SEQ    1716   1731       Missing (in isoform 5, isoform 6, isoform
FT                                7 and isoform 8).
FT                                /FTId=VSP_002694.
FT   MUTAGEN    2496   2496       C->S: No effect on channel activity.
FT                                Significant decrease of interaction with
FT                                ERP44. Complete loss of channel
FT                                inhibition by ERP44.
FT   MUTAGEN    2504   2504       C->S: No effect on channel activity.
FT                                Significant decrease of interaction with
FT                                ERP44. Complete loss of channel
FT                                inhibition by ERP44.
FT   MUTAGEN    2527   2527       C->S: Complete loss of channel activity.
FT                                Significant decrease of interaction with
FT                                ERP44.
FT   CONFLICT   1264   1264       N -> K (in Ref. 1; CAA33433).
FT   CONFLICT   2675   2675       P -> L (in Ref. 1; CAA33433).
FT   STRAND       14     23
FT   STRAND       25     30
FT   STRAND       36     39
FT   HELIX        41     43
FT   STRAND       46     48
FT   HELIX        53     56
FT   STRAND       58     61
FT   HELIX        67     74
FT   HELIX        86    109
FT   TURN        110    112
FT   STRAND      120    125
FT   TURN        126    129
FT   STRAND      130    139
FT   STRAND      141    143
FT   STRAND      146    154
FT   HELIX       157    159
FT   STRAND      161    167
FT   STRAND      181    189
FT   STRAND      193    199
FT   STRAND      201    205
FT   STRAND      207    213
FT   STRAND      239    244
FT   TURN        245    248
FT   STRAND      249    255
FT   STRAND      257    265
FT   STRAND      269    271
FT   HELIX       272    274
FT   HELIX       278    280
FT   STRAND      282    286
FT   STRAND      303    307
FT   TURN        308    310
FT   STRAND      313    318
FT   STRAND      353    359
FT   HELIX       364    366
FT   STRAND      368    371
FT   STRAND      388    392
FT   TURN        393    396
FT   STRAND      397    406
FT   STRAND      409    412
FT   STRAND      415    423
FT   STRAND      430    434
FT   HELIX       437    461
FT   HELIX       467    484
FT   TURN        485    487
FT   HELIX       495    499
FT   HELIX       504    512
FT   HELIX       515    524
FT   HELIX       525    527
FT   HELIX       547    564
FT   HELIX       568    585
FT   HELIX       589    599
SQ   SEQUENCE   2749 AA;  313167 MW;  FC4CF3ABB85EB82B CRC64;
     MSDKMSSFLH IGDICSLYAE GSTNGFISTL GLVDDRCVVQ PEAGDLNNPP KKFRDCLFKL
     CPMNRYSAQK QFWKAAKPGA NSTTDAVLLN KLHHAADLEK KQNETENRKL LGTVIQYGNV
     IQLLHLKSNK YLTVNKRLPA LLEKNAMRVT LDEAGNEGSW FYIQPFYKLR SIGDSVVIGD
     KVVLNPVNAG QPLHASSHQL VDNPGCNEVN SVNCNTSWKI VLFMKWSDNK DDILKGGDVV
     RLFHAEQEKF LTCDEHRKKQ HVFLRTTGRQ SATSATSSKA LWEVEVVQHD PCRGGAGYWN
     SLFRFKHLAT GHYLAAEVDP DFEEECLEFQ PSVDPDQDAS RSRLRNAQEK MVYSLVSVPE
     GNDISSIFEL DPTTLRGGDS LVPRNSYVRL RHLCTNTWVH STNIPIDKEE EKPVMLKIGT
     SPLKEDKEAF AIVPVSPAEV RDLDFANDAS KVLGSIAGKL EKGTITQNER RSVTKLLEDL
     VYFVTGGTNS GQDVLEVVFS KPNRERQKLM REQNILKQIF KLLQAPFTDC GDGPMLRLEE
     LGDQRHAPFR HICRLCYRVL RHSQQDYRKN QEYIAKQFGF MQKQIGYDVL AEDTITALLH
     NNRKLLEKHI TAAEIDTFVS LVRKNREPRF LDYLSDLCVS MNKSIPVTQE LICKAVLNPT
     NADILIETKL VLSRFEFEGV STGENALEAG EDEEEVWLFW RDSNKEIRSK SVRELAQDAK
     EGQKEDRDIL SYYRYQLNLF ARMCLDRQYL AINEISGQLD VDLILRCMSD ENLPYDLRAS
     FCRLMLHMHV DRDPQEQVTP VKYARLWSEI PSEIAIDDYD SSGTSKDEIK ERFAQTMEFV
     EEYLRDVVCQ RFPFSDKEKN KLTFEVVNLA RNLIYFGFYN FSDLLRLTKI LLAILDCVHV
     TTIFPISKMT KGEENKGSNV MRSIHGVGEL MTQVVLRGGG FLPMTPMAAA PEGNVKQAEP
     EKEDIMVMDT KLKIIEILQF ILNVRLDYRI SCLLCIFKRE FDESNSQSSE TSSGNSSQEG
     PSNVPGALDF EHIEEQAEGI FGGSEENTPL DLDDHGGRTF LRVLLHLTMH DYPPLVSGAL
     QLLFRHFSQR QEVLQAFKQV QLLVTSQDVD NYKQIKQDLD QLRSIVEKSE LWVYKGQGPD
     EPMDGASGEN EHKKTEEGTS KPLKHESTSS YNYRVVKEIL IRLSKLCVQE SASVRKSRKQ
     QQRLLRNMGA HAVVLELLQI PYEKAEDTKM QEIMRLAHEF LQNFCAGNQQ NQALLHKHIN
     LFLNPGILEA VTMQHIFMNN FQLCSEINER VVQHFVHCIE THGRNVQYIK FLQTIVKAEG
     KFIKKCQDMV MAELVNSGED VLVFYNDRAS FQTLIQMMRS ERDRMDENSP LMYHIHLVEL
     LAVCTEGKNV YTEIKCNSLL PLDDIVRVVT HEDCIPEVKI AYINFLNHCY VDTEVEMKEI
     YTSNHMWKLF ENFLVDICRA CNNTSDRKHA DSILEKYVTE IVMSIVTTFF SSPFSDQSTT
     LQTRQPVFVQ LLQGVFRVYH CNWLMPSQKA SVESCIRVLS DVAKSRAIAI PVDLDSQVNN
     LFLKSHNIVQ KTALNWRLSA RNAARRDSVL AASRDYRNII ERLQDIVSAL EDRLRPLVQA
     ELSVLVDVLH RPELLFPENT DARRKCESGG FICKLIKHTK QLLEENEEKL CIKVLQTLRE
     MMTKDRGYGE KQISIDESEN AELPQAPEAE NSTEQELEPS PPLRQLEDHK RGEALRQILV
     NRYYGNIRPS GRRESLTSFG NGPLSPGGPS KPGGGGGGPG SSSTSRGEMS LAEVQCHLDK
     EGASNLVIDL IMNASSDRVF HESILLAIAL LEGGNTTIQH SFFCRLTEDK KSEKFFKVFY
     DRMKVAQQEI KATVTVNTSD LGNKKKDDEV DRDAPSRKKA KEPTTQITEE VRDQLLEASA
     ATRKAFTTFR READPDDHYQ SGEGTQATTD KAKDDLEMSA VITIMQPILR FLQLLCENHN
     RDLQNFLRCQ NNKTNYNLVC ETLQFLDCIC GSTTGGLGLL GLYINEKNVA LINQTLESLT
     EYCQGPCHEN QNCIATHESN GIDIITALIL NDINPLGKKR MDLVLELKNN ASKLLLAIME
     SRHDSENAER ILYNMRPKEL VEVIKKAYMQ GEVEFEDGEN GEDGAASPRN VGHNIYILAH
     QLARHNKELQ TMLKPGGQVD GDEALEFYAK HTAQIEIVRL DRTMEQIVFP VPSICEFLTK
     ESKLRIYYTT ERDEQGSKIN DFFLRSEDLF NEMNWQKKLR AQPVLYWCAR NMSFWSSISF
     NLAVLMNLLV AFFYPFKGVR GGTLEPHWSG LLWTAMLISL AIVIALPKPH GIRALIASTI
     LRLIFSVGLQ PTLFLLGAFN VCNKIIFLMS FVGNCGTFTR GYRAMVLDVE FLYHLLYLLI
     CAMGLFVHEF FYSLLLFDLV YREETLLNVI KSVTRNGRSI ILTAVLALIL VYLFSIVGYL
     FFKDDFILEV DRLPNETAVP ETGESLANDF LYSDVCRVET GENCTSPAPK EELLPAEETE
     QDKEHTCETL LMCIVTVLSH GLRSGGGVGD VLRKPSKEEP LFAARVIYDL LFFFMVIIIV
     LNLIFGVIID TFADLRSEKQ KKEEILKTTC FICGLERDKF DNKTVTFEEH IKEEHNMWHY
     LCFIVLVKVK DSTEYTGPES YVAEMIRERN LDWFPRMRAM SLVSSDSEGE QNELRNLQEK
     LESTMKLVTN LSGQLSELKD QMTEQRKQKQ RIGLLGHPPH MNVNPQQPA
//
ID   TCPA_MOUSE              Reviewed;         556 AA.
AC   P11983; P11984; Q3TJ96; Q3TKU1; Q3U5T8; Q3U7I8; Q3UAA8; Q3UB80;
AC   Q3UE48;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 3.
DT   08-MAR-2011, entry version 111.
DE   RecName: Full=T-complex protein 1 subunit alpha;
DE            Short=TCP-1-alpha;
DE   AltName: Full=CCT-alpha;
DE   AltName: Full=Tailless complex polypeptide 1A;
DE            Short=TCP-1-A;
DE   AltName: Full=Tailless complex polypeptide 1B;
DE            Short=TCP-1-B;
GN   Name=Tcp1; Synonyms=Cct1, Ccta;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RX   MEDLINE=86133566; PubMed=3753900; DOI=10.1016/0092-8674(86)90839-1;
RA   Willison K.R., Dudley K., Potter J.;
RT   "Molecular cloning and sequence analysis of a haploid expressed gene
RT   encoding t complex polypeptide 1.";
RL   Cell 44:727-738(1986).
RN   [2]
RP   SEQUENCE REVISION.
RX   MEDLINE=90332422; PubMed=2377466; DOI=10.1093/nar/18.14.4247;
RA   Kirchhoff C., Willison K.R.;
RT   "Nucleotide and amino-acid sequence of human testis-derived TCP1.";
RL   Nucleic Acids Res. 18:4247-4247(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=92039043; PubMed=1937024; DOI=10.1016/0378-1119(91)90162-5;
RA   Kubota H., Morita T., Nagata T., Takemoto Y., Nozaki M., Gachelin G.,
RA   Matsushiro A.;
RT   "Nucleotide sequence of mouse Tcp-1a cDNA.";
RL   Gene 105:269-273(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=93013036; PubMed=1383093; DOI=10.1016/0378-1119(92)90095-7;
RA   Kubota H., Willison K., Ashworth A., Nozaki M., Miyamoto H.,
RA   Yamamoto H., Matsushiro A., Morita T.;
RT   "Structure and expression of the gene encoding mouse T-complex
RT   polypeptide (Tcp-1).";
RL   Gene 120:207-215(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 1-11; 34-43; 64-73; 190-199; 234-243; 371-378;
RP   434-466 AND 485-496, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RA   Bienvenut W.V., Sandilands E., Serrels B., Brunton V.G., Frame M.C.;
RL   Submitted (FEB-2008) to UniProtKB.
RN   [8]
RP   PROTEIN SEQUENCE OF 19-63; 112-122; 131-145; 190-199; 234-243;
RP   248-259; 299-309; 434-443; 469-480; 500-510 AND 516-526, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [9]
RP   PROTEIN SEQUENCE OF 485-496.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-551, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Molecular chaperone; assists the folding of proteins
CC       upon ATP hydrolysis. As part of the BBS/CCT complex may play a
CC       role in the assembly of BBSome, a complex involved in ciliogenesis
CC       regulating transports vesicles to the cilia. Known to play a role,
CC       in vitro, in the folding of actin and tubulin (By similarity).
CC   -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that
CC       forms two stacked rings, 12 to 16 nm in diameter. Interacts with
CC       PACRG. Component of the BBS/CCT complex composed at least of MKKS,
CC       BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8 (By
CC       similarity).
CC   -!- INTERACTION:
CC       Q9CZA6:Nde1; NbExp=2; IntAct=EBI-772338, EBI-309934;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton,
CC       centrosome (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P11983-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P11983-2; Sequence=VSP_024734, VSP_024735;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA40337.1; Type=Frameshift; Positions=528;
CC       Sequence=AAA40338.1; Type=Frameshift; Positions=528;
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DR   EMBL; M20130; AAA40337.1; ALT_FRAME; mRNA.
DR   EMBL; M12899; AAA40338.1; ALT_FRAME; mRNA.
DR   EMBL; D90344; BAA14356.1; -; mRNA.
DR   EMBL; D10606; BAA01461.1; -; Genomic_DNA.
DR   EMBL; S46763; AAB23855.1; -; Genomic_DNA.
DR   EMBL; AK149611; BAE28989.1; -; mRNA.
DR   EMBL; AK149755; BAE29063.1; -; mRNA.
DR   EMBL; AK151068; BAE30084.1; -; mRNA.
DR   EMBL; AK151445; BAE30407.1; -; mRNA.
DR   EMBL; AK152641; BAE31381.1; -; mRNA.
DR   EMBL; AK153430; BAE31988.1; -; mRNA.
DR   EMBL; AK165665; BAE38327.1; -; mRNA.
DR   EMBL; AK166828; BAE39052.1; -; mRNA.
DR   EMBL; AK166966; BAE39149.1; -; mRNA.
DR   EMBL; AK167529; BAE39599.1; -; mRNA.
DR   EMBL; BC003809; AAH03809.1; -; mRNA.
DR   IPI; IPI00459493; -.
DR   IPI; IPI00845611; -.
DR   PIR; B24059; B24059.
DR   PIR; JC1443; JC1443.
DR   RefSeq; NP_038714.2; NM_013686.3.
DR   UniGene; Mm.439645; -.
DR   ProteinModelPortal; P11983; -.
DR   SMR; P11983; 15-532.
DR   IntAct; P11983; 4.
DR   STRING; P11983; -.
DR   REPRODUCTION-2DPAGE; IPI00459493; -.
DR   REPRODUCTION-2DPAGE; P11983; -.
DR   PRIDE; P11983; -.
DR   Ensembl; ENSMUST00000089024; ENSMUSP00000086418; ENSMUSG00000068039.
DR   GeneID; 21454; -.
DR   KEGG; mmu:21454; -.
DR   UCSC; uc008all.1; mouse.
DR   CTD; 21454; -.
DR   MGI; MGI:98535; Tcp1.
DR   eggNOG; roNOG13011; -.
DR   HOVERGEN; HBG001052; -.
DR   InParanoid; P11983; -.
DR   OMA; RTQNVMA; -.
DR   PhylomeDB; P11983; -.
DR   NextBio; 300820; -.
DR   ArrayExpress; P11983; -.
DR   Bgee; P11983; -.
DR   CleanEx; MM_TCP1; -.
DR   Genevestigator; P11983; -.
DR   GermOnline; ENSMUSG00000068039; Mus musculus.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IDA:MGI.
DR   GO; GO:0005720; C:nuclear heterochromatin; IDA:MGI.
DR   GO; GO:0000242; C:pericentriolar material; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   InterPro; IPR012715; Chap_CCT_alpha.
DR   InterPro; IPR017998; Chaperone_TCP-1.
DR   InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR   InterPro; IPR002423; Cpn60/TCP-1.
DR   PANTHER; PTHR11353:SF20; Chap_CCT_alpha; 1.
DR   PANTHER; PTHR11353; Cpn60/TCP-1; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00304; TCOMPLEXTCP1.
DR   SUPFAM; SSF48592; GroEL-ATPase; 1.
DR   TIGRFAMs; TIGR02340; chap_CCT_alpha; 1.
DR   PROSITE; PS00750; TCP1_1; 1.
DR   PROSITE; PS00751; TCP1_2; 1.
DR   PROSITE; PS00995; TCP1_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Chaperone; Cytoplasm;
KW   Cytoskeleton; Direct protein sequencing; Nucleotide-binding;
KW   Phosphoprotein.
FT   CHAIN         1    556       T-complex protein 1 subunit alpha.
FT                                /FTId=PRO_0000128305.
FT   MOD_RES       1      1       N-acetylmethionine.
FT   MOD_RES     544    544       Phosphoserine.
FT   MOD_RES     551    551       Phosphoserine.
FT   VAR_SEQ       1     49       Missing (in isoform 2).
FT                                /FTId=VSP_024734.
FT   VAR_SEQ      50     50       G -> M (in isoform 2).
FT                                /FTId=VSP_024735.
FT   CONFLICT     17     17       V -> I (in Ref. 1; AAA40337, 3; BAA14356
FT                                and 5; BAE30084).
FT   CONFLICT     36     36       F -> L (in Ref. 1; AAA40337 and 3;
FT                                BAA14356).
FT   CONFLICT    140    140       T -> A (in Ref. 1; AAA40337 and 3;
FT                                BAA14356).
FT   CONFLICT    149    151       INA -> TNT (in Ref. 1; AAA40337 and 3;
FT                                BAA14356).
FT   CONFLICT    151    151       A -> T (in Ref. 1; AAA40338).
FT   CONFLICT    177    177       L -> H (in Ref. 5; BAE31381).
FT   CONFLICT    192    192       V -> I (in Ref. 1; AAA40337 and 3;
FT                                BAA14356).
FT   CONFLICT    217    217       N -> D (in Ref. 5; BAE39599).
FT   CONFLICT    259    259       K -> E (in Ref. 5; BAE31381).
FT   CONFLICT    296    296       Y -> C (in Ref. 1; AAA40337 and 3;
FT                                BAA14356).
FT   CONFLICT    318    318       H -> C (in Ref. 1; AAA40337 and 3;
FT                                BAA14356).
FT   CONFLICT    326    326       S -> T (in Ref. 1; AAA40337 and 3;
FT                                BAA14356).
FT   CONFLICT    378    378       R -> Q (in Ref. 5; BAE30084).
FT   CONFLICT    402    402       V -> I (in Ref. 5; BAE30407/BAE31988).
FT   CONFLICT    405    405       L -> S (in Ref. 1; AAA40337 and 3;
FT                                BAA14356).
FT   CONFLICT    429    429       S -> N (in Ref. 1; AAA40338).
FT   CONFLICT    439    439       A -> V (in Ref. 5; BAE31381).
FT   CONFLICT    454    454       V -> M (in Ref. 5; BAE39052).
FT   CONFLICT    494    494       K -> N (in Ref. 5; BAE30407).
FT   CONFLICT    537    537       S -> C (in Ref. 1; AAA40337 and 3;
FT                                BAA14356).
SQ   SEQUENCE   556 AA;  60449 MW;  48F2387BE0F909A4 CRC64;
     MEGPLSVFGD RSTGEAVRSQ NVMAAASIAN IVKSSFGPVG LDKMLVDDIG DVTITNDGAT
     ILKLLEVEHP AAKVLCELAD LQDKEVGDGT TSVVIIAAEL LKNADELVKQ KIHPTSVISG
     YRLACKEAVR YINENLIINT DELGRDCLIN AAKTSMSSKI IGINGDYFAN MVVDAVLAVK
     YTDARGQPRY PVNSVNILKA HGRSQIESML INGYALNCVV GSQGMPKRIV NAKIACLDFS
     LQKTKMKLGV QVVITDPEKL DQIRQRESDI TKERIQKILA TGANVILTTG GIDDMYLKYF
     VEAGAMAVRR VLKRDLKHVA KASGASILST LANLEGEETF EVTMLGQAEE VVQERICDDE
     LILIKNTKAR TSASIILRGA NDFMCDEMER SLHDALCVVK RVLELKSVVP GGGAVEAALS
     IYLENYATSM GSREQLAIAE FARSLLVIPN TLAVNAAQDS TDLVAKLRAF HNEAQVNPER
     KNLKWIGLDL VHGKPRDNKQ AGVFEPTIVK VKSLKFATEA AITILRIDDL IKLHPESKDD
     KHGSYENAVH SGALDD
//
ID   A4_MOUSE                Reviewed;         770 AA.
AC   P12023; P97487; P97942; Q99K32;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   09-MAY-2003, sequence version 3.
DT   08-MAR-2011, entry version 149.
DE   RecName: Full=Amyloid beta A4 protein;
DE   AltName: Full=ABPP;
DE            Short=APP;
DE   AltName: Full=Alzheimer disease amyloid A4 protein homolog;
DE   AltName: Full=Amyloidogenic glycoprotein;
DE            Short=AG;
DE   Contains:
DE     RecName: Full=N-APP;
DE   Contains:
DE     RecName: Full=Soluble APP-alpha;
DE              Short=S-APP-alpha;
DE   Contains:
DE     RecName: Full=Soluble APP-beta;
DE              Short=S-APP-beta;
DE   Contains:
DE     RecName: Full=C99;
DE     AltName: Full=APP-C99;
DE   Contains:
DE     RecName: Full=Beta-amyloid protein 42;
DE     AltName: Full=Beta-APP42;
DE   Contains:
DE     RecName: Full=Beta-amyloid protein 40;
DE     AltName: Full=Beta-APP40;
DE   Contains:
DE     RecName: Full=C83;
DE   Contains:
DE     RecName: Full=P3(42);
DE   Contains:
DE     RecName: Full=P3(40);
DE   Contains:
DE     RecName: Full=C80;
DE   Contains:
DE     RecName: Full=Gamma-secretase C-terminal fragment 59;
DE     AltName: Full=APP-C59;
DE     AltName: Full=Amyloid intracellular domain 59;
DE              Short=AID(59);
DE     AltName: Full=Gamma-CTF(59);
DE   Contains:
DE     RecName: Full=Gamma-secretase C-terminal fragment 57;
DE     AltName: Full=APP-C57;
DE     AltName: Full=Amyloid intracellular domain 57;
DE              Short=AID(57);
DE     AltName: Full=Gamma-CTF(57);
DE   Contains:
DE     RecName: Full=Gamma-secretase C-terminal fragment 50;
DE     AltName: Full=Amyloid intracellular domain 50;
DE              Short=AID(50);
DE     AltName: Full=Gamma-CTF(50);
DE   Contains:
DE     RecName: Full=C31;
DE   Flags: Precursor;
GN   Name=App;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP695).
RC   TISSUE=Brain;
RX   MEDLINE=88106489; PubMed=3322280; DOI=10.1016/0006-291X(87)90419-0;
RA   Yamada T., Sasaki H., Furuya H., Miyata T., Goto I., Sakaki Y.;
RT   "Complementary DNA for the mouse homolog of the human amyloid beta
RT   protein precursor.";
RL   Biochem. Biophys. Res. Commun. 149:665-671(1987).
RN   [2]
RP   SEQUENCE REVISION.
RA   Yamada T.;
RL   Submitted (MAR-1988) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP695).
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=92096458; PubMed=1756177; DOI=10.1016/0167-4781(91)90231-A;
RA   de Strooper B., van Leuven F., van den Berghe H.;
RT   "The amyloid beta protein precursor or proteinase nexin II from mouse
RT   is closer related to its human homolog than previously reported.";
RL   Biochim. Biophys. Acta 1129:141-143(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP695).
RC   STRAIN=SAMP8; TISSUE=Hippocampus;
RX   MEDLINE=21130647; PubMed=11235921; DOI=10.1139/bcb-79-1-57;
RA   Kumar V.B., Vyas K., Franko M., Choudhary V., Buddhiraju C.,
RA   Alvarez J., Morley J.E.;
RT   "Molecular cloning, expression, and regulation of hippocampal amyloid
RT   precursor protein of senescence accelerated mouse (SAMP8).";
RL   Biochem. Cell Biol. 79:57-67(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
RX   MEDLINE=92209998; PubMed=1555768; DOI=10.1016/0378-1119(92)90375-Y;
RA   Izumi R., Yamada T., Yoshikai S., Sasaki H., Hattori M., Sakai Y.;
RT   "Positive and negative regulatory elements for the expression of the
RT   Alzheimer's disease amyloid precursor-encoding gene in mouse.";
RL   Gene 112:189-195(1992).
RN   [6]
RP   PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM APP770).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 281-380, AND ALTERNATIVE SPLICING.
RC   TISSUE=Brain, and Kidney;
RX   MEDLINE=89149813; PubMed=2493250; DOI=10.1016/0006-291X(89)92808-8;
RA   Yamada T., Sasaki H., Dohura K., Goto I., Sakaki Y.;
RT   "Structure and expression of the alternatively-spliced forms of mRNA
RT   for the mouse homolog of Alzheimer's disease amyloid beta protein
RT   precursor.";
RL   Biochem. Biophys. Res. Commun. 158:906-912(1989).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 289-364.
RC   STRAIN=CD-1; TISSUE=Placenta;
RX   MEDLINE=89345111; PubMed=2569710; DOI=10.1093/nar/17.13.5396;
RA   Fukuchi K., Martin G.M., Deeb S.S.;
RT   "Sequence of the protease inhibitor domain of the A4 amyloid protein
RT   precursor of Mus domesticus.";
RL   Nucleic Acids Res. 17:5396-5396(1989).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 656-737.
RC   STRAIN=129/Sv;
RA   Wragg M.A., Busfield F., Duff K., Korenblat K., Capecchi M.,
RA   Loring J.F., Goate A.M.;
RT   "Introduction of six mutations into the mouse genome using 'Hit and
RT   Run' gene-targeting: introduction of familial Alzheimer's disease
RT   mutations into the mouse amyloid precursor protein gene and
RT   humanization of the A-beta fragment.";
RL   Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   TISSUE SPECIFICITY OF ALTERNATIVE SPLICED FORMS.
RX   MEDLINE=93287808; PubMed=8510506; DOI=10.1016/0169-328X(93)90020-P;
RA   Sola C., Mengod G., Ghetti B., Palacios J.M., Triarhou L.C.;
RT   "Regional distribution of the alternatively spliced isoforms of beta
RT   APP RNA transcript in the brain of normal, heterozygous and homozygous
RT   weaver mutant mice as revealed by in situ hybridization
RT   histochemistry.";
RL   Brain Res. Mol. Brain Res. 17:340-346(1993).
RN   [11]
RP   INTERACTION WITH KNS2.
RX   MEDLINE=21010507; PubMed=11144355; DOI=10.1016/S0896-6273(00)00124-0;
RA   Kamal A., Stokin G.B., Yang Z., Xia C.-H., Goldstein L.S.;
RT   "Axonal transport of amyloid precursor protein is mediated by direct
RT   binding to the kinesin light chain subunit of kinesin-I.";
RL   Neuron 28:449-459(2000).
RN   [12]
RP   C-TERMINAL PROTEIN-PROTEIN INTERACTION, AND MUTAGENESIS OF TYR-728;
RP   THR-743; TYR-757; ASN-759 AND TYR-762.
RX   MEDLINE=21408156; PubMed=11517249;
RA   Matsuda S., Yasukawa T., Homma Y., Ito Y., Niikura T., Hiraki T.,
RA   Hirai S., Ohno S., Kita Y., Kawasumi M., Kouyama K., Yamamoto T.,
RA   Kyriakis J.M., Nishimoto I.;
RT   "C-jun N-terminal kinase (JNK)-interacting protein-1b/islet-brain-1
RT   scaffolds Alzheimer's amyloid precursor protein with JNK.";
RL   J. Neurosci. 21:6597-6607(2001).
RN   [13]
RP   INTERACTION WITH MAPK8IP1, AND PHOSPHORYLATION.
RX   MEDLINE=22028091; PubMed=11912189; DOI=10.1074/jbc.M108372200;
RA   Taru H., Iijima K., Hase M., Kirino Y., Yagi Y., Suzuki T.;
RT   "Interaction of Alzheimer's beta-amyloid precursor family proteins
RT   with scaffold proteins of the JNK signaling cascade.";
RL   J. Biol. Chem. 277:20070-20078(2002).
RN   [14]
RP   INTERACTION OF CTF PEPTIDES WITH NUMB.
RX   MEDLINE=22008109; PubMed=12011466; DOI=10.1073/pnas.102192599;
RA   Roncarati R., Sestan N., Scheinfeld M.H., Berechid B.E., Lopez P.A.,
RA   Meucci O., McGlade J.C., Rakic P., D'Adamio L.;
RT   "The gamma-secretase-generated intracellular domain of beta-amyloid
RT   precursor protein binds Numb and inhibits Notch signaling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:7102-7107(2002).
RN   [15]
RP   PROTEOLYTIC PROCESSING BY GAMMA SECRETASE, AND INTERACTION WITH APBB1.
RX   MEDLINE=21437805; PubMed=11553691;
RX   DOI=10.1046/j.1471-4159.2001.00516.x;
RA   Cupers P., Orlans I., Craessaerts K., Annaert W., De Strooper B.;
RT   "The amyloid precursor protein (APP)-cytoplasmic fragment generated by
RT   gamma-secretase is rapidly degraded but distributes partially in a
RT   nuclear fraction of neurons in culture.";
RL   J. Neurochem. 78:1168-1178(2001).
RN   [16]
RP   INTERACTION WITH CPEB1.
RX   PubMed=16314516; DOI=10.1128/MCB.25.24.10930-10939.2005;
RA   Cao Q., Huang Y.-S., Kan M.-C., Richter J.D.;
RT   "Amyloid precursor proteins anchor CPEB to membranes and promote
RT   polyadenylation-induced translation.";
RL   Mol. Cell. Biol. 25:10930-10939(2005).
CC   -!- FUNCTION: Functions as a cell surface receptor and performs
CC       physiological functions on the surface of neurons relevant to
CC       neurite growth, neuronal adhesion and axonogenesis. Involved in
CC       cell mobility and transcription regulation through protein-protein
CC       interactions. Can promote transcription activation through binding
CC       to APBB1-KAT5 and inhibit Notch signaling through interaction with
CC       Numb. Couples to apoptosis-inducing pathways such as those
CC       mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity (By
CC       similarity). Acts as a kinesin I membrane receptor, mediating the
CC       axonal transport of beta-secretase and presenilin 1. May be
CC       involved in copper homeostasis/oxidative stress through copper ion
CC       reduction. Can regulate neurite outgrowth through binding to
CC       components of the extracellular matrix such as heparin and
CC       collagen I and IV (By similarity). The splice isoforms that
CC       contain the BPTI domain possess protease inhibitor activity.
CC       Induces a AGER-dependent pathway that involves activation of p38
CC       MAPK, resulting in internalization of amyloid-beta peptide and
CC       leading to mitochondrial dysfunction in cultured cortical neurons
CC       (By similarity).
CC   -!- FUNCTION: Beta-amyloid peptides are lipophilic metal chelators
CC       with metal-reducing activity. Bind transient metals such as
CC       copper, zinc and iron. Rat and mouse beta-amyloid peptides bind
CC       only weakly transient metals and have little reducing activity due
CC       to substitutions of transient metal chelating residues. Beta-APP42
CC       may activate mononuclear phagocytes in the brain and elicit
CC       inflammatory responses. Promotes both tau aggregation and TPK II-
CC       mediated phosphorylation (By similarity).
CC   -!- FUNCTION: The gamma-CTF peptides as well as the caspase-cleaved
CC       peptides, including C31, are potent enhancers of neuronal
CC       apoptosis.
CC   -!- FUNCTION: N-APP binds TNFRSF21 triggering caspase activation and
CC       degeneration of both neuronal cell bodies (via caspase-3) and
CC       axons (via caspase-6) (By similarity).
CC   -!- SUBUNIT: Binds, via its C-terminus, to the PID domain of several
CC       cytoplasmic proteins, including APBB family members, the APBA
CC       family, MAPK8IP1, SHC1, NUMB and DAB1. Binding to DAB1 inhibits
CC       its serine phosphorylation. Also interacts with GPCR-like protein
CC       BPP, FPRL1, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via
CC       BaSS) and DDB1 (By similarity). In vitro, it binds MAPT via the
CC       MT-binding domains (By similarity). Associates with microtubules
CC       in the presence of ATP and in a kinesin-dependent manner (By
CC       similarity). Interacts, through a C-terminal domain, with GNAO1
CC       (By similarity). Amyloid beta-42 binds CHRNA7 in hippocampal
CC       neurons (By similarity). Beta-amyloid associates with HADH2 (By
CC       similarity). Interacts with ANKS1B, TNFRSF21 and AGER (By
CC       similarity). Interacts with CPEB1. Interacts with ITM2B. Interacts
CC       with ITM2C. Interacts with IDE. Can form homodimers; this is
CC       promoted by heparin binding (By similarity).
CC   -!- INTERACTION:
CC       P98084:Apba2; NbExp=1; IntAct=EBI-78814, EBI-81669;
CC       Q9QXJ1:Apbb1; NbExp=1; IntAct=EBI-78814, EBI-81338;
CC       Q03157:Aplp1; NbExp=2; IntAct=EBI-78814, EBI-399929;
CC       Q06335:Aplp2; NbExp=1; IntAct=EBI-78814, EBI-446708;
CC       P97318:Dab1; NbExp=1; IntAct=EBI-78814, EBI-81680;
CC       Q9D1T0:Lingo1; NbExp=1; IntAct=EBI-78814, EBI-2012981;
CC       Q9UQF2:MAPK8IP1 (xeno); NbExp=1; IntAct=EBI-78814, EBI-78404;
CC       Q9WVI9:Mapk8ip1; NbExp=2; IntAct=EBI-78814, EBI-74515;
CC       Q9WVI9-1:Mapk8ip1; NbExp=2; IntAct=EBI-78814, EBI-288461;
CC       Q13526:PIN1 (xeno); NbExp=1; IntAct=EBI-78814, EBI-714158;
CC       Q61120:Shc3; NbExp=1; IntAct=EBI-78814, EBI-79107;
CC       Q9JHI9:Slc40a1; NbExp=1; IntAct=EBI-78814, EBI-2931424;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein. Membrane, clathrin-coated pit. Note=Cell surface protein
CC       that rapidly becomes internalized via clathrin-coated pits. During
CC       maturation, the immature APP (N-glycosylated in the endoplasmic
CC       reticulum) moves to the Golgi complex where complete maturation
CC       occurs (O-glycosylated and sulfated). After alpha-secretase
CC       cleavage, soluble APP is released into the extracellular space and
CC       the C-terminal is internalized to endosomes and lysosomes. Some
CC       APP accumulates in secretory transport vesicles leaving the late
CC       Golgi compartment and returns to the cell surface. Gamma-CTF(59)
CC       peptide is located to both the cytoplasm and nuclei of neurons. It
CC       can be translocated to the nucleus through association with APBB1
CC       (Fe65). Beta-APP42 associates with FPRL1 at the cell surface and
CC       the complex is then rapidly internalized (By similarity). APP
CC       sorts to the basolateral surface in epithelial cells (By
CC       similarity). During neuronal differentiation, the Thr-743
CC       phosphorylated form is located mainly in growth cones, moderately
CC       in neurites and sparingly in the cell body. Casein kinase
CC       phosphorylation can occur either at the cell surface or within a
CC       post-Golgi compartment (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Additional isoforms seem to exist;
CC       Name=APP770;
CC         IsoId=P12023-1; Sequence=Displayed;
CC       Name=APP695;
CC         IsoId=P12023-2; Sequence=VSP_000012, VSP_000013;
CC       Name=APP751;
CC         IsoId=P12023-3; Sequence=VSP_000014;
CC       Name=APP714;
CC         IsoId=P12023-4; Sequence=Not described;
CC   -!- TISSUE SPECIFICITY: Isoform APP770 is expressed in kidney. Isoform
CC       APP751 is widely expressed. Isoform APP695 is expressed in brain,
CC       kidney and liver. Isoform APP695, isoform APP714 and isoform
CC       APP751 are expressed in several different brain regions including
CC       hippocampus, substania nigra pars compacta and cerebellum. In the
CC       cerebellum, these isoforms are abundantly expressed in Purkinje
CC       cells.
CC   -!- DOMAIN: The basolateral sorting signal (BaSS) is required for
CC       sorting of membrane proteins to the basolateral surface of
CC       epithelial cells.
CC   -!- DOMAIN: The NPXY sequence motif found in many tyrosine-
CC       phosphorylated proteins is required for the specific binding of
CC       the PID domain. However, additional amino acids either N- or C-
CC       terminal to the NPXY motif are often required for complete
CC       interaction. The PID domain-containing proteins which bind APP
CC       require the YENPTY motif for full interaction. These interactions
CC       are independent of phosphorylation on the terminal tyrosine
CC       residue. The NPXY site is also involved in clathrin-mediated
CC       endocytosis (By similarity).
CC   -!- PTM: Proteolytically processed under normal cellular conditions.
CC       Cleavage either by alpha-secretase, beta-secretase or theta-
CC       secretase leads to generation and extracellular release of soluble
CC       APP peptides, S-APP-alpha and S-APP-beta, and the retention of
CC       corresponding membrane-anchored C-terminal fragments, C80, C83 and
CC       C99. Subsequent processing of C80 and C83 by gamma-secretase
CC       yields P3 peptides. This is the major secretory pathway and is
CC       non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated
CC       gamma-secretase processing of C99 releases the amyloid beta
CC       proteins, amyloid-beta 40 (Abeta40) and amyloid-beta 42 (Abeta42),
CC       major components of amyloid plaques, and the cytotoxic C-terminal
CC       fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59) (By
CC       similarity).
CC   -!- PTM: Proteolytically cleaved by caspases during neuronal
CC       apoptosis. Cleavage at Asp-739 by either caspase-3, -8 or -9
CC       results in the production of the neurotoxic C31 peptide and the
CC       increased production of beta-amyloid peptides (By similarity).
CC   -!- PTM: N- and O-glycosylated (By similarity).
CC   -!- PTM: Phosphorylation in the C-terminal on tyrosine, threonine and
CC       serine residues is neuron-specific. Phosphorylation can affect APP
CC       processing, neuronal differentiation and interaction with other
CC       proteins. The Thr-743 phosphorylated form causes a conformational
CC       change which reduces binding of Fe65 family members (By
CC       similarity). Phosphorylation on Tyr-757 is required for SHC
CC       binding (By similarity).
CC   -!- PTM: Extracellular binding and reduction of copper, results in a
CC       corresponding oxidation of Cys-144 and Cys-158, and the formation
CC       of a disulfide bond (By similarity).
CC   -!- PTM: Trophic-factor deprivation triggers the cleavage of surface
CC       APP by beta-secretase to release sAPP-beta which is further
CC       cleaved to release an N-terminal fragment of APP (N-APP) (By
CC       similarity).
CC   -!- PTM: Beta-amyloid peptides are degraded by IDE (By similarity).
CC   -!- MISCELLANEOUS: Chelation of metal ions, notably copper, iron and
CC       zinc, can induce histidine-bridging between beta-amyloid molecules
CC       resulting in beta-amyloid-metal aggregates. Rat and mouse beta-
CC       amyloid peptides have an arginine residue substituted for the
CC       bridging histidine residue and are thus less capable of forming
CC       amyloid aggegates. Extracellular zinc-binding increases binding of
CC       heparin to APP and inhibits collagen-binding (By similarity).
CC   -!- SIMILARITY: Belongs to the APP family.
CC   -!- SIMILARITY: Contains 1 BPTI/Kunitz inhibitor domain.
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DR   EMBL; M18373; AAA37139.1; -; mRNA.
DR   EMBL; X59379; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; U84012; AAB41502.1; -; mRNA.
DR   EMBL; D10603; BAA01456.1; -; Genomic_DNA.
DR   EMBL; BC005490; AAH05490.1; -; mRNA.
DR   EMBL; M24397; AAA39929.1; -; mRNA.
DR   EMBL; X15210; CAA33280.1; -; mRNA.
DR   EMBL; U82624; AAB40919.1; -; Genomic_DNA.
DR   IPI; IPI00114389; -.
DR   IPI; IPI00230494; -.
DR   IPI; IPI00323079; -.
DR   PIR; A27485; A27485.
DR   PIR; A32282; A32282.
DR   PIR; S04855; S04855.
DR   RefSeq; NP_001185752.1; NM_001198823.1.
DR   UniGene; Mm.277585; -.
DR   PDB; 2ROZ; NMR; -; A=739-770.
DR   PDB; 2YSZ; NMR; -; A=739-770.
DR   PDB; 2YT0; NMR; -; A=739-770.
DR   PDB; 2YT1; NMR; -; A=739-770.
DR   PDBsum; 2ROZ; -.
DR   PDBsum; 2YSZ; -.
DR   PDBsum; 2YT0; -.
DR   PDBsum; 2YT1; -.
DR   ProteinModelPortal; P12023; -.
DR   SMR; P12023; 26-192, 287-342, 374-565, 672-770.
DR   IntAct; P12023; 97.
DR   MINT; MINT-208509; -.
DR   STRING; P12023; -.
DR   MEROPS; I02.015; -.
DR   PhosphoSite; P12023; -.
DR   PRIDE; P12023; -.
DR   Ensembl; ENSMUST00000005406; ENSMUSP00000005406; ENSMUSG00000022892.
DR   Ensembl; ENSMUST00000074271; ENSMUSP00000073883; ENSMUSG00000022892.
DR   Ensembl; ENSMUST00000114177; ENSMUSP00000109814; ENSMUSG00000022892.
DR   GeneID; 11820; -.
DR   UCSC; uc007ztn.1; mouse.
DR   MGI; MGI:88059; App.
DR   eggNOG; roNOG06213; -.
DR   HOGENOM; HBG402865; -.
DR   HOVERGEN; HBG000051; -.
DR   InParanoid; P12023; -.
DR   OMA; RKQCKTH; -.
DR   OrthoDB; EOG45B1F4; -.
DR   PhylomeDB; P12023; -.
DR   ArrayExpress; P12023; -.
DR   Bgee; P12023; -.
DR   CleanEx; MM_APP; -.
DR   Genevestigator; P12023; -.
DR   GermOnline; ENSMUSG00000022892; Mus musculus.
DR   GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0035253; C:ciliary rootlet; IDA:MGI.
DR   GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IDA:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR   GO; GO:0051233; C:spindle midzone; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR   GO; GO:0008088; P:axon cargo transport; IMP:MGI.
DR   GO; GO:0016199; P:axon midline choice point recognition; IMP:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0006878; P:cellular copper ion homeostasis; IMP:MGI.
DR   GO; GO:0048669; P:collateral sprouting in absence of injury; IGI:MGI.
DR   GO; GO:0016358; P:dendrite development; IMP:MGI.
DR   GO; GO:0006897; P:endocytosis; IMP:MGI.
DR   GO; GO:0030198; P:extracellular matrix organization; IGI:MGI.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0000085; P:G2 phase of mitotic cell cycle; IMP:MGI.
DR   GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IMP:MGI.
DR   GO; GO:0007617; P:mating behavior; IGI:MGI.
DR   GO; GO:0006378; P:mRNA polyadenylation; IDA:MGI.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; IDA:MGI.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IGI:MGI.
DR   GO; GO:0016322; P:neuron remodeling; IMP:MGI.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IMP:MGI.
DR   GO; GO:0007176; P:regulation of epidermal growth factor receptor activity; IGI:MGI.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
DR   GO; GO:0050803; P:regulation of synapse structure and activity; IMP:MGI.
DR   GO; GO:0006417; P:regulation of translation; IDA:MGI.
DR   GO; GO:0051563; P:smooth endoplasmic reticulum calcium ion homeostasis; IGI:MGI.
DR   GO; GO:0001967; P:suckling behavior; IGI:MGI.
DR   GO; GO:0051124; P:synaptic growth at neuromuscular junction; IGI:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   InterPro; IPR008155; Amyloid_glyco.
DR   InterPro; IPR013803; Amyloid_glyco_Abeta.
DR   InterPro; IPR011178; Amyloid_glyco_Cu-bd.
DR   InterPro; IPR008154; Amyloid_glyco_extra.
DR   InterPro; IPR019744; Amyloid_glyco_extracell_CS.
DR   InterPro; IPR015849; Amyloid_glyco_heparin-bd.
DR   InterPro; IPR019745; Amyloid_glyco_intracell_CS.
DR   InterPro; IPR019543; APP_amyloid_C.
DR   InterPro; IPR002223; Prot_inh_Kunz-m.
DR   InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR   Gene3D; G3DSA:4.10.230.10; Amyloid_glyco_Abeta; 1.
DR   Gene3D; G3DSA:3.30.1490.140; Amyloid_glyco_Cu-bd; 1.
DR   Gene3D; G3DSA:3.90.570.10; Amyloid_glyco_heparin-bd; 1.
DR   Gene3D; G3DSA:4.10.410.10; Prot_inh_Kunz-m; 1.
DR   Pfam; PF02177; A4_EXTRA; 1.
DR   Pfam; PF10515; APP_amyloid; 1.
DR   Pfam; PF03494; Beta-APP; 1.
DR   Pfam; PF00014; Kunitz_BPTI; 1.
DR   PRINTS; PR00203; AMYLOIDA4.
DR   PRINTS; PR00759; BASICPTASE.
DR   PRINTS; PR00204; BETAAMYLOID.
DR   SMART; SM00006; A4_EXTRA; 1.
DR   SMART; SM00131; KU; 1.
DR   SUPFAM; SSF56491; A4_extra; 1.
DR   SUPFAM; SSF89811; Amyloid_glyco_Cu-bd; 1.
DR   SUPFAM; SSF57362; Prot_inh_Kunz-m; 1.
DR   PROSITE; PS00319; A4_EXTRA; 1.
DR   PROSITE; PS00320; A4_INTRA; 1.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Amyloid; Apoptosis; Cell adhesion;
KW   Coated pit; Copper; Disulfide bond; Endocytosis; Glycoprotein;
KW   Heparin-binding; Iron; Membrane; Metal-binding;
KW   Notch signaling pathway; Phosphoprotein; Protease inhibitor;
KW   Serine protease inhibitor; Signal; Transmembrane; Transmembrane helix;
KW   Zinc.
FT   SIGNAL        1     17       By similarity.
FT   CHAIN        18    770       Amyloid beta A4 protein.
FT                                /FTId=PRO_0000000114.
FT   CHAIN        18    687       Soluble APP-alpha (Potential).
FT                                /FTId=PRO_0000000115.
FT   CHAIN        18    671       Soluble APP-beta (Potential).
FT                                /FTId=PRO_0000000116.
FT   CHAIN        18    286       N-APP (By similarity).
FT                                /FTId=PRO_0000381968.
FT   CHAIN       672    770       C99 (By similarity).
FT                                /FTId=PRO_0000000117.
FT   CHAIN       672    713       Beta-amyloid protein 42 (By similarity).
FT                                /FTId=PRO_0000000118.
FT   CHAIN       672    711       Beta-amyloid protein 40 (By similarity).
FT                                /FTId=PRO_0000000119.
FT   CHAIN       688    770       C83 (By similarity).
FT                                /FTId=PRO_0000000120.
FT   PEPTIDE     688    713       P3(42) (By similarity).
FT                                /FTId=PRO_0000000121.
FT   PEPTIDE     688    711       P3(40) (By similarity).
FT                                /FTId=PRO_0000000122.
FT   CHAIN       691    770       C80.
FT                                /FTId=PRO_0000384576.
FT   CHAIN       712    770       Gamma-secretase C-terminal fragment 59.
FT                                /FTId=PRO_0000000123.
FT   CHAIN       714    770       Gamma-secretase C-terminal fragment 57.
FT                                /FTId=PRO_0000000124.
FT   CHAIN       721    770       Gamma-secretase C-terminal fragment 50.
FT                                /FTId=PRO_0000000125.
FT   CHAIN       740    770       C31 (By similarity).
FT                                /FTId=PRO_0000000126.
FT   TOPO_DOM     18    699       Extracellular (Potential).
FT   TRANSMEM    700    723       Helical; (Potential).
FT   TOPO_DOM    724    770       Cytoplasmic (Potential).
FT   DOMAIN      291    341       BPTI/Kunitz inhibitor.
FT   REGION       96    110       Heparin-binding (By similarity).
FT   REGION      181    188       Zinc-binding (By similarity).
FT   REGION      391    423       Heparin-binding (By similarity).
FT   REGION      491    522       Heparin-binding (By similarity).
FT   REGION      523    540       Collagen-binding (By similarity).
FT   REGION      732    751       Interaction with G(o)-alpha (By
FT                                similarity).
FT   MOTIF       724    734       Basolateral sorting signal.
FT   MOTIF       759    762       NPXY motif; contains endocytosis signal.
FT   COMPBIAS    230    260       Asp/Glu-rich (acidic).
FT   COMPBIAS    274    280       Poly-Thr.
FT   METAL       147    147       Copper 1 (By similarity).
FT   METAL       151    151       Copper 1 (By similarity).
FT   METAL       168    168       Copper 1 (By similarity).
FT   METAL       677    677       Copper or zinc 2 (By similarity).
FT   METAL       685    685       Copper or zinc 2 (By similarity).
FT   SITE        144    144       Required for Cu(2+) reduction (By
FT                                similarity).
FT   SITE        301    302       Reactive bond (By similarity).
FT   SITE        671    672       Cleavage; by beta-secretase (By
FT                                similarity).
FT   SITE        672    673       Cleavage; by caspase-6 (By similarity).
FT   SITE        687    688       Cleavage; by alpha-secretase (By
FT                                similarity).
FT   SITE        690    691       Cleavage; by theta-secretase (By
FT                                similarity).
FT   SITE        704    704       Implicated in free radical propagation
FT                                (By similarity).
FT   SITE        706    706       Susceptible to oxidation (By similarity).
FT   SITE        711    712       Cleavage; by gamma-secretase; site 1 (By
FT                                similarity).
FT   SITE        713    714       Cleavage; by gamma-secretase; site 2 (By
FT                                similarity).
FT   SITE        720    721       Cleavage; by gamma-secretase; site 3 (By
FT                                similarity).
FT   SITE        739    740       Cleavage; by caspase-6, caspase-8 or
FT                                caspase-9 (By similarity).
FT   MOD_RES     198    198       Phosphoserine; by CK2 (By similarity).
FT   MOD_RES     206    206       Phosphoserine; by CK1 (By similarity).
FT   MOD_RES     729    729       Phosphothreonine (By similarity).
FT   MOD_RES     730    730       Phosphoserine; by APP-kinase I (By
FT                                similarity).
FT   MOD_RES     743    743       Phosphothreonine; by CDK5 and MAPK10.
FT   MOD_RES     757    757       Phosphotyrosine (By similarity).
FT   MOD_RES     762    762       Phosphotyrosine (By similarity).
FT   CARBOHYD    542    542       N-linked (GlcNAc...) (Probable).
FT   CARBOHYD    571    571       N-linked (GlcNAc...) (Probable).
FT   DISULFID     38     62       By similarity.
FT   DISULFID     73    117       By similarity.
FT   DISULFID     98    105       By similarity.
FT   DISULFID    133    187       By similarity.
FT   DISULFID    144    174       By similarity.
FT   DISULFID    158    186       By similarity.
FT   DISULFID    291    341       By similarity.
FT   DISULFID    300    324       By similarity.
FT   DISULFID    316    337       By similarity.
FT   VAR_SEQ     289    289       E -> V (in isoform APP695).
FT                                /FTId=VSP_000012.
FT   VAR_SEQ     290    364       Missing (in isoform APP695).
FT                                /FTId=VSP_000013.
FT   VAR_SEQ     346    380       Missing (in isoform APP751).
FT                                /FTId=VSP_000014.
FT   MUTAGEN     728    728       Y->A: No effect on MAPK8IP1 binding.
FT   MUTAGEN     732    733       HH->GL,GP: Almost complete loss of
FT                                binding to G(o) alpha subunit. No
FT                                inhibition of GTPase activity.
FT   MUTAGEN     743    743       T->E: No effect on MAPK8IP1 binding.
FT   MUTAGEN     757    757       Y->G: No MAPK8IP1 nor APBA1 nor APBB1 nor
FT                                DAB1 binding.
FT   MUTAGEN     759    759       N->A: No MAPK8IP1 nor APBA1 nor Dab1
FT                                binding. No effect on APBB1 binding.
FT   MUTAGEN     762    762       Y->A: No MAPK8IP1 nor APBA1 nor Dab1
FT                                binding. No effect on APBB1 binding.
FT   CONFLICT    211    211       G -> V (in Ref. 1; AAA37139).
FT   CONFLICT    375    375       V -> A (in Ref. 4; AAB41502).
FT   HELIX       744    754
SQ   SEQUENCE   770 AA;  86722 MW;  988D89E089092A3E CRC64;
     MLPSLALLLL AAWTVRALEV PTDGNAGLLA EPQIAMFCGK LNMHMNVQNG KWESDPSGTK
     TCIGTKEGIL QYCQEVYPEL QITNVVEANQ PVTIQNWCKR GRKQCKTHTH IVIPYRCLVG
     EFVSDALLVP DKCKFLHQER MDVCETHLHW HTVAKETCSE KSTNLHDYGM LLPCGIDKFR
     GVEFVCCPLA EESDSVDSAD AEEDDSDVWW GGADTDYADG GEDKVVEVAE EEEVADVEEE
     EADDDEDVED GDEVEEEAEE PYEEATERTT STATTTTTTT ESVEEVVREV CSEQAETGPC
     RAMISRWYFD VTEGKCVPFF YGGCGGNRNN FDTEEYCMAV CGSVSTQSLL KTTSEPLPQD
     PDKLPTTAAS TPDAVDKYLE TPGDENEHAH FQKAKERLEA KHRERMSQVM REWEEAERQA
     KNLPKADKKA VIQHFQEKVE SLEQEAANER QQLVETHMAR VEAMLNDRRR LALENYITAL
     QAVPPRPHHV FNMLKKYVRA EQKDRQHTLK HFEHVRMVDP KKAAQIRSQV MTHLRVIYER
     MNQSLSLLYN VPAVAEEIQD EVDELLQKEQ NYSDDVLANM ISEPRISYGN DALMPSLTET
     KTTVELLPVN GEFSLDDLQP WHPFGVDSVP ANTENEVEPV DARPAADRGL TTRPGSGLTN
     IKTEEISEVK MDAEFGHDSG FEVRHQKLVF FAEDVGSNKG AIIGLMVGGV VIATVIVITL
     VMLKKKQYTS IHHGVVEVDA AVTPEERHLS KMQQNGYENP TYKFFEQMQN
//
ID   K6PL_MOUSE              Reviewed;         780 AA.
AC   P12382;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 108.
DE   RecName: Full=6-phosphofructokinase, liver type;
DE            EC=2.7.1.11;
DE   AltName: Full=Phosphofructo-1-kinase isozyme B;
DE            Short=PFK-B;
DE   AltName: Full=Phosphofructokinase 1;
DE   AltName: Full=Phosphohexokinase;
GN   Name=Pfkl; Synonyms=Pfk-l, Pfkb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=88298847; PubMed=2969893;
RA   Gehnrich S.C., Gekakis N., Sul H.S.;
RT   "Liver (B-type) phosphofructokinase mRNA. Cloning, structure, and
RT   expression.";
RL   J. Biol. Chem. 263:11755-11759(1988).
RN   [2]
RP   PROTEIN SEQUENCE OF 130-141; 257-269; 367-374; 655-672 AND 716-726,
RP   AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-640, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-775, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
CC       fructose 1,6-bisphosphate.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: Allosteric enzyme activated by ADP, AMP, or
CC       fructose bisphosphate and inhibited by ATP or citrate.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase family. Two domains
CC       subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; J03928; AAA20076.1; -; mRNA.
DR   IPI; IPI00554862; -.
DR   PIR; A31070; A31070.
DR   UniGene; Mm.269649; -.
DR   ProteinModelPortal; P12382; -.
DR   SMR; P12382; 16-372, 400-747.
DR   MINT; MINT-135975; -.
DR   STRING; P12382; -.
DR   PhosphoSite; P12382; -.
DR   PRIDE; P12382; -.
DR   Ensembl; ENSMUST00000020522; ENSMUSP00000020522; ENSMUSG00000020277.
DR   MGI; MGI:97547; Pfkl.
DR   eggNOG; maNOG12237; -.
DR   HOGENOM; HBG324640; -.
DR   HOVERGEN; HBG000976; -.
DR   InParanoid; P12382; -.
DR   OrthoDB; EOG4RJG0W; -.
DR   PhylomeDB; P12382; -.
DR   BRENDA; 2.7.1.11; 244.
DR   ArrayExpress; P12382; -.
DR   Bgee; P12382; -.
DR   CleanEx; MM_PFKL; -.
DR   Genevestigator; P12382; -.
DR   GermOnline; ENSMUSG00000020277; Mus musculus.
DR   GO; GO:0005945; C:6-phosphofructokinase complex; IEA:InterPro.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IDA:MGI.
DR   GO; GO:0006096; P:glycolysis; IDA:MGI.
DR   GO; GO:0046676; P:negative regulation of insulin secretion; IDA:MGI.
DR   GO; GO:0009749; P:response to glucose stimulus; IDA:MGI.
DR   InterPro; IPR009161; 6-phosphofructokinase_euk.
DR   InterPro; IPR022953; Phosphofructokinase.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   Pfam; PF00365; PFK; 2.
DR   PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Ppfruckinase; 2.
DR   TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Allosteric enzyme; ATP-binding;
KW   Direct protein sequencing; Glycolysis; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Repeat;
KW   Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    780       6-phosphofructokinase, liver type.
FT                                /FTId=PRO_0000112022.
FT   NP_BIND      35     39       ATP (By similarity).
FT   NP_BIND     193    197       ATP (By similarity).
FT   NP_BIND     210    226       ATP (By similarity).
FT   ACT_SITE    166    166       Proton acceptor (By similarity).
FT   METAL       224    224       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     201    201       Substrate (By similarity).
FT   BINDING     292    292       Substrate (By similarity).
FT   BINDING     298    298       Substrate (By similarity).
FT   BINDING     301    301       Substrate (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     640    640       Phosphotyrosine.
FT   MOD_RES     775    775       Phosphoserine.
SQ   SEQUENCE   780 AA;  85301 MW;  8947F984B86B0DCE CRC64;
     MATVDLEKLR MSGAGKAIGV LTSGGDAQGM NAAVRAVTRM GIYVGAKVFL IYEGYEGLVE
     GGENIKPANW LSVSNIIQLG GTIIGSARCK AFTTREGRLA AAYNLLQHGI TNLCVIGGDG
     SLTGANIFRN EWGSLLEELV KEGKISESTA QNYAHLTIAG LVGSIDNDFC GTDMTIGTDS
     ALHRIMEVID AITTTAQSHQ RTFVLEVMGR HCGYLALVSA LASGADWLFI PEAPPEDGWE
     NFMCERLGET RSRGSRLNII IIAEGAIDRH GKPISSSYVK DLVVQRLGFD TRVTVLGHVQ
     RGGTPSAFDR ILSSKMGMEA VMALLEATPD TPACVVSLSG NQSVRLPLME CVQVTKDVQK
     AMDEERFDEA IQLRGRSFEN NWKIYKLLAH QKVSKEKSNF SLAILNVGAP AAGMNAAVPS
     AVRTGISEGH TVYIVHDGFE GLAKGQVQEV GWHDVAGWLG RGGSMLGTKR TLPKPHLEAI
     VENLRTYNIH ALLVIGGFEA YEGVLQLVEA RGRYEELCIV MCVIPATISN NVPGTDFSLG
     SDTAVNAAME SCDRIKQSAS GTKRRVFIVE TMGGYCGYLA TVTGIAVGAD AAYVFEDPFN
     IHDLKANVEH MTEKMKTDIQ RGLVLRNEKC HEHYTTEFLY NLYSSEGRGV FDCRTNVLGH
     LQQGGAPTPF DRNYGTKLGV KAMLWVSEKL RDVYRKGRVF ANAPDSACVI GLRKKVVAFS
     PVTELKKETD FEHRMPREQW WLNLRLMLKM LAHYRISMAD YVSGELEHVT RRTLSIDKGF
//
ID   ACM1_MOUSE              Reviewed;         460 AA.
AC   P12657; Q8BJN3;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Muscarinic acetylcholine receptor M1;
GN   Name=Chrm1; Synonyms=Chrm-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=89054021; PubMed=2848036;
RA   Shapiro R.A., Scherer N.M., Habecker B.A., Subers E.M.,
RA   Nathanson N.M.;
RT   "Isolation, sequence, and functional expression of the mouse M1
RT   muscarinic acetylcholine receptor gene.";
RL   J. Biol. Chem. 263:18397-18403(1988).
RN   [2]
RP   ERRATUM.
RA   Shapiro R.A., Scherer N.M., Habecker B.A., Subers E.M.,
RA   Nathanson N.M.;
RL   J. Biol. Chem. 264:6596-6596(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Corpus striatum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: The muscarinic acetylcholine receptor mediates various
CC       cellular responses, including inhibition of adenylate cyclase,
CC       breakdown of phosphoinositides and modulation of potassium
CC       channels through the action of G proteins. Primary transducing
CC       effect is Pi turnover.
CC   -!- SUBUNIT: Interacts with GPRASP2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Cell junction, synapse, postsynaptic cell membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Muscarinic acetylcholine receptor subfamily. CHRM1 sub-subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; J04192; AAA37158.1; -; Genomic_DNA.
DR   EMBL; AK081248; BAC38175.1; -; mRNA.
DR   IPI; IPI00119416; -.
DR   PIR; A31897; A31897.
DR   RefSeq; NP_001106167.1; NM_001112697.1.
DR   RefSeq; NP_031724.2; NM_007698.3.
DR   UniGene; Mm.240607; -.
DR   ProteinModelPortal; P12657; -.
DR   SMR; P12657; 25-433.
DR   STRING; P12657; -.
DR   TCDB; 9.A.40.3.3; HlyC/CorC (HCC) family.
DR   PRIDE; P12657; -.
DR   Ensembl; ENSMUST00000035444; ENSMUSP00000042632; ENSMUSG00000032773.
DR   GeneID; 12669; -.
DR   KEGG; mmu:12669; -.
DR   CTD; 12669; -.
DR   MGI; MGI:88396; Chrm1.
DR   eggNOG; roNOG04436; -.
DR   HOGENOM; HBG713567; -.
DR   HOVERGEN; HBG105720; -.
DR   InParanoid; P12657; -.
DR   OrthoDB; EOG4NVZK1; -.
DR   ArrayExpress; P12657; -.
DR   Bgee; P12657; -.
DR   CleanEx; MM_CHRM1; -.
DR   Genevestigator; P12657; -.
DR   GermOnline; ENSMUSG00000032773; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0040012; P:regulation of locomotion; IMP:MGI.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR002228; Musac_M1_rcpt.
DR   InterPro; IPR000995; Musac_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00243; MUSCARINICR.
DR   PRINTS; PR00538; MUSCRINICM1R.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Receptor; Synapse; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    460       Muscarinic acetylcholine receptor M1.
FT                                /FTId=PRO_0000069017.
FT   TOPO_DOM      1     24       Extracellular (Potential).
FT   TRANSMEM     25     47       Helical; Name=1; (By similarity).
FT   TOPO_DOM     48     61       Cytoplasmic (Potential).
FT   TRANSMEM     62     82       Helical; Name=2; (By similarity).
FT   TOPO_DOM     83     99       Extracellular (Potential).
FT   TRANSMEM    100    121       Helical; Name=3; (By similarity).
FT   TOPO_DOM    122    141       Cytoplasmic (Potential).
FT   TRANSMEM    142    164       Helical; Name=4; (By similarity).
FT   TOPO_DOM    165    186       Extracellular (Potential).
FT   TRANSMEM    187    209       Helical; Name=5; (By similarity).
FT   TOPO_DOM    210    366       Cytoplasmic (Potential).
FT   TRANSMEM    367    387       Helical; Name=6; (By similarity).
FT   TOPO_DOM    388    401       Extracellular (Potential).
FT   TRANSMEM    402    421       Helical; Name=7; (By similarity).
FT   TOPO_DOM    422    460       Cytoplasmic (Potential).
FT   MOD_RES     428    428       Phosphohistidine (Potential).
FT   MOD_RES     451    451       Phosphoserine (Potential).
FT   MOD_RES     455    455       Phosphothreonine (Potential).
FT   MOD_RES     457    457       Phosphoserine (Potential).
FT   CARBOHYD      2      2       N-linked (GlcNAc...) (Probable).
FT   CARBOHYD     12     12       N-linked (GlcNAc...) (Probable).
FT   DISULFID     98    178       By similarity.
FT   CONFLICT     30     30       S -> I (in Ref. 3; BAC38175).
FT   CONFLICT     50     50       I -> F (in Ref. 3; BAC38175).
FT   CONFLICT    420    420       S -> L (in Ref. 3; BAC38175).
FT   CONFLICT    428    428       H -> T (in Ref. 3; BAC38175).
SQ   SEQUENCE   460 AA;  51329 MW;  121A625C50BE3993 CRC64;
     MNTSVPPAVS PNITVLAPGK GPWQVAFIGS TTGLLSLATV TGNLLVLISI KVNTELKTVN
     NYFLLSLACA DLIIGTFSMN LYTTYLLMGH WALGTLACDL WLALDYVASN ASVMNLLLIS
     FDRYFSVTRP LSYRAKRTPR RAALMIGLAW LVSFVLWAPA ILFWQYLVGE RTVLAGQCYI
     QFLSQPIITF GTAMAAFYLP VTVMCTLYWR IYRETENRAR ELAALQGSET PGKGGGSSSS
     SERSQPGAEG SPESPPGRCC RCCRAPRLLQ AYSWKEEEEE DEGSMESLTS SEGEEPGSEV
     VIKMPMVDPE AQAPTKQPPK SSPNTVKRPT KKGRDRGGKG QKPRGKEQLA KRKTFSLVKE
     KKAARTLSAI LLAFILTWTP YNIMVLVSTF CKDCVPETLW ELGYWLCYVN STVNPMCYAS
     CNKAFRDHFR LLLLCRWDKR RWRKIPKRPG SVHRTPSRQC
//
ID   PCP2_MOUSE              Reviewed;         120 AA.
AC   P12660; P22941; Q3TV53;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   08-FEB-2011, entry version 82.
DE   RecName: Full=Purkinje cell protein 2;
DE   AltName: Full=Protein PCD-5;
DE   AltName: Full=Purkinje cell-specific protein L7;
GN   Name=Pcp2; Synonyms=Pcp-2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RX   MEDLINE=89068131; PubMed=3199205;
RA   Nordquist D.T., Kozak C.A., Orr H.T.;
RT   "cDNA cloning and characterization of three genes uniquely expressed
RT   in cerebellum by Purkinje neurons.";
RL   J. Neurosci. 8:4780-4789(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Purkinje cell;
RX   MEDLINE=90166517; PubMed=2483097; DOI=10.1016/0896-6273(88)90186-9;
RA   Oberdick J., Levinthal F., Levinthal C.;
RT   "A Purkinje cell differentiation marker shows a partial DNA sequence
RT   homology to the cellular sis/PDGF2 gene.";
RL   Neuron 1:367-376(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=91293575; PubMed=2065970;
RA   Vandaele S., Nordquist D.T., Feddersen R.M., Tretjakoff I.,
RA   Peterson A.C., Orr H.T.;
RT   "Purkinje cell protein-2 regulatory regions and transgene expression
RT   in cerebellar compartments.";
RL   Genes Dev. 5:1136-1148(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: May function as a cell-type specific modulator for G
CC       protein-mediated cell signaling.
CC   -!- TISSUE SPECIFICITY: Cerebellum (Purkinje cells) and retinal
CC       bipolar neurons.
CC   -!- SIMILARITY: Contains 2 GoLoco domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA02989.1; Type=Erroneous initiation;
CC       Sequence=AAB19316.1; Type=Erroneous gene model prediction;
CC       Sequence=BAC25015.1; Type=Erroneous initiation;
CC       Sequence=BAE35767.1; Type=Erroneous initiation;
CC       Sequence=Ref.2; Type=Frameshift; Positions=77;
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DR   EMBL; M21532; AAA02989.1; ALT_INIT; mRNA.
DR   EMBL; S40022; AAB19316.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AK003002; BAC25015.1; ALT_INIT; mRNA.
DR   EMBL; AK160398; BAE35767.1; ALT_INIT; mRNA.
DR   IPI; IPI00119474; -.
DR   PIR; A40322; B34955.
DR   RefSeq; NP_001123276.1; NM_001129804.1.
DR   RefSeq; NP_032816.1; NM_008790.2.
DR   UniGene; Mm.440882; -.
DR   STRING; P12660; -.
DR   PRIDE; P12660; -.
DR   Ensembl; ENSMUST00000111056; ENSMUSP00000106685; ENSMUSG00000004630.
DR   GeneID; 18545; -.
DR   KEGG; mmu:18545; -.
DR   UCSC; uc009ksa.1; mouse.
DR   CTD; 18545; -.
DR   MGI; MGI:97508; Pcp2.
DR   eggNOG; maNOG19860; -.
DR   GeneTree; ENSGT00500000045061; -.
DR   HOVERGEN; HBG008159; -.
DR   OMA; KDGVQKR; -.
DR   NextBio; 294330; -.
DR   ArrayExpress; P12660; -.
DR   Bgee; P12660; -.
DR   CleanEx; MM_PCP2; -.
DR   Genevestigator; P12660; -.
DR   GermOnline; ENSMUSG00000004630; Mus musculus.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IPI:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR003109; GoLoco_motif.
DR   Pfam; PF02188; GoLoco; 2.
DR   SMART; SM00390; GoLoco; 2.
DR   PROSITE; PS50877; GOLOCO; 2.
PE   2: Evidence at transcript level;
KW   Repeat.
FT   CHAIN         1    120       Purkinje cell protein 2.
FT                                /FTId=PRO_0000058261.
FT   DOMAIN        7     29       GoLoco 1.
FT   DOMAIN       47     69       GoLoco 2.
SQ   SEQUENCE   120 AA;  13054 MW;  D186BF2710DCA03E CRC64;
     MAGSPDQEGF FNLLTHVQGD RMEEQRCSLQ AGPGQNPESQ GGPAPEMDNL MDMLVNTQGR
     RMDDQRVTVN SLPGFQPIGP KDGMQKRPGT LSPQPLLTPQ DPAALSFRRN SSPQPQTQAP
//
ID   KAP1_MOUSE              Reviewed;         381 AA.
AC   P12849;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=cAMP-dependent protein kinase type I-beta regulatory subunit;
GN   Name=Prkar1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=88234494; PubMed=3375237; DOI=10.1073/pnas.85.11.3703;
RA   Clegg C.H., Cadd G.G., McKnight G.S.;
RT   "Genetic characterization of a brain-specific form of the type I
RT   regulatory subunit of cAMP-dependent protein kinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:3703-3707(1988).
CC   -!- SUBUNIT: The inactive form of the enzyme is composed of two
CC       regulatory chains and two catalytic chains. Activation by cAMP
CC       produces two active catalytic monomers and a regulatory dimer that
CC       binds four cAMP molecules.
CC   -!- TISSUE SPECIFICITY: Four types of regulatory chains are found: I-
CC       alpha, I-beta, II-alpha, and II-beta. Their expression varies
CC       among tissues and is in some cases constitutive and in others
CC       inducible.
CC   -!- PTM: The pseudophosphorylation site binds to the substrate-binding
CC       region of the catalytic chain, resulting in the inhibition of its
CC       activity.
CC   -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC       family.
CC   -!- SIMILARITY: Contains 2 cyclic nucleotide-binding domains.
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CC   -----------------------------------------------------------------------
DR   EMBL; M20473; AAA39935.1; -; mRNA.
DR   IPI; IPI00310841; -.
DR   PIR; A30205; OKMSR1.
DR   RefSeq; NP_032949.3; NM_008923.3.
DR   UniGene; Mm.306163; -.
DR   ProteinModelPortal; P12849; -.
DR   SMR; P12849; 14-61, 112-378.
DR   IntAct; P12849; 6.
DR   STRING; P12849; -.
DR   PhosphoSite; P12849; -.
DR   PRIDE; P12849; -.
DR   Ensembl; ENSMUST00000026973; ENSMUSP00000026973; ENSMUSG00000025855.
DR   Ensembl; ENSMUST00000110890; ENSMUSP00000106515; ENSMUSG00000025855.
DR   GeneID; 19085; -.
DR   KEGG; mmu:19085; -.
DR   UCSC; uc009afy.1; mouse.
DR   CTD; 19085; -.
DR   MGI; MGI:97759; Prkar1b.
DR   eggNOG; roNOG07923; -.
DR   HOGENOM; HBG736470; -.
DR   HOVERGEN; HBG002025; -.
DR   InParanoid; P12849; -.
DR   OMA; QSDSHDD; -.
DR   OrthoDB; EOG4JQ3XP; -.
DR   PhylomeDB; P12849; -.
DR   ArrayExpress; P12849; -.
DR   Bgee; P12849; -.
DR   Genevestigator; P12849; -.
DR   GermOnline; ENSMUSG00000025855; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; TAS:MGI.
DR   GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008283; P:cell proliferation; TAS:MGI.
DR   GO; GO:0007611; P:learning or memory; IMP:MGI.
DR   GO; GO:0009887; P:organ morphogenesis; TAS:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; TAS:MGI.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR002373; cAMP/cGMP_kin.
DR   InterPro; IPR012198; cAMP_dep_PK_reg_su.
DR   InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 2.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF02197; RIIa; 1.
DR   PIRSF; PIRSF000548; PK_regulatory; 1.
DR   PRINTS; PR00103; CAMPKINASE.
DR   SMART; SM00100; cNMP; 2.
DR   SMART; SM00394; RIIa; 1.
DR   SUPFAM; SSF47391; cAMP-dep_prot_kin_reg_I/II_a/b; 1.
DR   SUPFAM; SSF51206; cNMP_binding; 2.
DR   PROSITE; PS00888; CNMP_BINDING_1; 2.
DR   PROSITE; PS00889; CNMP_BINDING_2; 2.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; cAMP; cAMP-binding; Disulfide bond; Nucleotide-binding;
KW   Phosphoprotein; Repeat.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    381       cAMP-dependent protein kinase type I-beta
FT                                regulatory subunit.
FT                                /FTId=PRO_0000205382.
FT   NP_BIND     137    254       cAMP 1.
FT   NP_BIND     255    381       cAMP 2.
FT   REGION        2    136       Dimerization and phosphorylation.
FT   MOTIF        96    100       Pseudophosphorylation motif.
FT   BINDING     202    202       cAMP 1.
FT   BINDING     211    211       cAMP 1.
FT   BINDING     326    326       cAMP 2.
FT   BINDING     335    335       cAMP 2.
FT   MOD_RES       2      2       N-acetylalanine (Probable).
FT   MOD_RES       3      3       Phosphoserine (By similarity).
FT   MOD_RES      77     77       Phosphoserine (By similarity).
FT   MOD_RES      83     83       Phosphoserine (By similarity).
FT   DISULFID     18     18       Interchain (with C-39) (By similarity).
FT   DISULFID     39     39       Interchain (with C-18) (By similarity).
SQ   SEQUENCE   381 AA;  43224 MW;  42287E553FA16023 CRC64;
     MASPSCFHSE DEDSLKGCEM YVQKHGIQQV LKECIVHLCV AKPDRPLRFL REHFEKLEKE
     ENRQILARQK SNSQCDSHDE EISPTPPNPV VKARRRRGGV SAEVYTEEDA VSYVRKVIPK
     DYKTMTALAK AISKNVLFSH LDDNERSDIF DAMFPVTHIG GETVIQQGNE GDNFYVIDQG
     EVDVYVNGEW VTNISEGGSF GELALIYGTP RAATVKAKTD LKLWGIDRDS YRRILMGSTL
     RKRKMYEEFL SKVSILESLE KWERLTVADA LEPVQFEDGE KIVVQGEPGD DFYIITEGTA
     SVLQRRSPNE EYVEVGRLGP SDYFGEIALL LNRPRAATVV ARGPLKCVKL DRPRFERVLG
     PCSEILKRNI QRYNSFISLT V
//
ID   CNTN1_MOUSE             Reviewed;        1020 AA.
AC   P12960; Q6NXV7; Q8BR42; Q8C6A0;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   08-MAR-2011, entry version 114.
DE   RecName: Full=Contactin-1;
DE   AltName: Full=Neural cell surface protein F3;
DE   Flags: Precursor;
GN   Name=Cntn1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=89340657; PubMed=2474555; DOI=10.1083/jcb.109.2.775;
RA   Gennarini G., Cibelli G., Rougon G., Mattei M.-G., Goridis C.;
RT   "The mouse neuronal cell surface protein F3: a phosphatidylinositol-
RT   anchored member of the immunoglobulin superfamily related to chicken
RT   contactin.";
RL   J. Cell Biol. 109:775-788(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CD-1; TISSUE=Neural stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 79-90; 226-249; 604-613; 619-628; 759-768 AND
RP   859-869, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 574-1020.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   INTERACTION WITH TNR, AND FUNCTION.
RX   MEDLINE=93152173; PubMed=7678967; DOI=10.1016/0896-6273(93)90243-K;
RA   Pesheva P., Gennarini G., Goridis C., Schachner M.;
RT   "The F3/11 cell adhesion molecule mediates the repulsion of neurons by
RT   the extracellular matrix glycoprotein J1-160/180.";
RL   Neuron 10:69-82(1993).
RN   [6]
RP   FUNCTION.
RX   MEDLINE=21289248; PubMed=11395001; DOI=10.1016/S0896-6273(01)00296-3;
RA   Boyle M.E., Berglund E.O., Murai K.K., Weber L., Peles E., Ranscht B.;
RT   "Contactin orchestrates assembly of the septate-like junctions at the
RT   paranode in myelinated peripheral nerve.";
RL   Neuron 30:385-397(2001).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH NOTCH1.
RX   MEDLINE=22929945; PubMed=14567914; DOI=10.1016/S0092-8674(03)00810-9;
RA   Hu Q.-D., Ang B.-T., Karsak M., Hu W.-P., Cui X.-Y., Duka T.,
RA   Takeda Y., Chia W., Sankar N., Ng Y.-K., Ling E.-A., Maciag T.,
RA   Small D., Trifonova R., Kopan R., Okano H., Nakafuku M., Chiba S.,
RA   Hirai H., Aster J.C., Schachner M., Pallen C.J., Watanabe K.,
RA   Xiao Z.-C.;
RT   "F3/contactin acts as a functional ligand for Notch during
RT   oligodendrocyte maturation.";
RL   Cell 115:163-175(2003).
CC   -!- FUNCTION: Contactins mediate cell surface interactions during
CC       nervous system development. Involved in the formation of paranodal
CC       axo-glial junctions in myelinated peripheral nerves and in the
CC       signaling between axons and myelinating glial cells via its
CC       association with CNTNAP1. Participates in oligodendrocytes
CC       generation by acting as a ligand of NOTCH1. Its association with
CC       NOTCH1 promotes NOTCH1 activation through the released notch
CC       intracellular domain (NICD) and subsequent translocation to the
CC       nucleus. Interaction with TNR induces a repulsion of neurons and
CC       an inhibition of neurite outgrowth.
CC   -!- SUBUNIT: Monomer. Interacts with CNTNAP1 in cis form. Binds to the
CC       carbonic-anhydrase like domain of protein-tyrosine phosphatase
CC       zeta (By similarity). Interacts with NOTCH1 and TNR.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC   -!- MISCELLANEOUS: F3 shares with L1, N-CAM, MAG, and other cell
CC       adhesion molecules from nervous tissue the L2/HNK-1 carbohydrate
CC       epitope.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. Contactin
CC       family.
CC   -!- SIMILARITY: Contains 4 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 6 Ig-like C2-type (immunoglobulin-like)
CC       domains.
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DR   EMBL; X14943; CAA33075.1; -; mRNA.
DR   EMBL; BC066864; AAH66864.1; -; mRNA.
DR   EMBL; AK045710; BAC32466.1; -; mRNA.
DR   EMBL; AK076273; BAC36282.1; -; mRNA.
DR   IPI; IPI00123058; -.
DR   PIR; S05944; S05944.
DR   RefSeq; NP_001153119.1; NM_001159647.1.
DR   RefSeq; NP_001153120.1; NM_001159648.1.
DR   RefSeq; NP_031753.1; NM_007727.2.
DR   UniGene; Mm.470343; -.
DR   UniGene; Mm.4911; -.
DR   ProteinModelPortal; P12960; -.
DR   SMR; P12960; 15-995.
DR   MINT; MINT-1177246; -.
DR   STRING; P12960; -.
DR   PRIDE; P12960; -.
DR   Ensembl; ENSMUST00000000109; ENSMUSP00000000109; ENSMUSG00000055022.
DR   Ensembl; ENSMUST00000068378; ENSMUSP00000067842; ENSMUSG00000055022.
DR   GeneID; 12805; -.
DR   KEGG; mmu:12805; -.
DR   UCSC; uc007xik.1; mouse.
DR   CTD; 12805; -.
DR   MGI; MGI:105980; Cntn1.
DR   eggNOG; roNOG11834; -.
DR   GeneTree; ENSGT00550000074380; -.
DR   HOGENOM; HBG444805; -.
DR   HOVERGEN; HBG051047; -.
DR   InParanoid; P12960; -.
DR   OMA; IDLIPWM; -.
DR   OrthoDB; EOG4DZ1TH; -.
DR   PhylomeDB; P12960; -.
DR   NextBio; 282242; -.
DR   ArrayExpress; P12960; -.
DR   Bgee; P12960; -.
DR   CleanEx; MM_CNTN1; -.
DR   Genevestigator; P12960; -.
DR   GermOnline; ENSMUSG00000055022; Mus musculus.
DR   GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; EXP:Reactome.
DR   GO; GO:0030246; F:carbohydrate binding; IDA:MGI.
DR   GO; GO:0001948; F:glycoprotein binding; IDA:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0031175; P:neuron projection development; IGI:MGI.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR   GO; GO:0090072; P:positive regulation of sodium ion transport via voltage-gated sodium channel activity; IMP:MGI.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 10.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF07679; I-set; 4.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 4.
DR   SUPFAM; SSF49265; FN_III-like; 4.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS50835; IG_LIKE; 6.
PE   1: Evidence at protein level;
KW   Cell adhesion; Cell membrane; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; GPI-anchor; Immunoglobulin domain;
KW   Lipoprotein; Membrane; Notch signaling pathway; Repeat; Signal.
FT   SIGNAL        1     20
FT   CHAIN        21   1001       Contactin-1.
FT                                /FTId=PRO_0000014687.
FT   PROPEP     1002   1020       Removed in mature form.
FT                                /FTId=PRO_0000014688.
FT   DOMAIN       41    131       Ig-like C2-type 1.
FT   DOMAIN      137    223       Ig-like C2-type 2.
FT   DOMAIN      241    326       Ig-like C2-type 3.
FT   DOMAIN      331    407       Ig-like C2-type 4.
FT   DOMAIN      413    500       Ig-like C2-type 5.
FT   DOMAIN      504    603       Ig-like C2-type 6.
FT   DOMAIN      605    701       Fibronectin type-III 1.
FT   DOMAIN      708    805       Fibronectin type-III 2.
FT   DOMAIN      810    901       Fibronectin type-III 3.
FT   DOMAIN      906    998       Fibronectin type-III 4.
FT   COMPBIAS    604    611       Gly/Pro-rich.
FT   LIPID      1001   1001       GPI-anchor amidated serine (Potential).
FT   CARBOHYD    208    208       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    258    258       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    338    338       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    457    457       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    473    473       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    494    494       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    521    521       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    593    593       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    935    935       N-linked (GlcNAc...) (Potential).
FT   DISULFID     65    114       By similarity.
FT   DISULFID    158    211       By similarity.
FT   DISULFID    263    310       By similarity.
FT   DISULFID    352    391       By similarity.
FT   DISULFID    436    484       By similarity.
FT   DISULFID    526    585       By similarity.
FT   CONFLICT    433    433       I -> V (in Ref. 2; AAH66864).
SQ   SEQUENCE   1020 AA;  113388 MW;  9DCDAA40EAA4CBC7 CRC64;
     MKMPLLVSHL LLISLTSCLG DFTWHRRYGH GVSEEDKGFG PIFEEQPINT IYPEESLEGK
     VSLNCRARAS PFPVYKWRMN NGDVDLTNDR YSMVGGNLVI NNPDKQKDAG VYYCLASNNY
     GMVRSTEATL SFGYLDPFPP EERPEVKVKE GKGMVLLCDP PYHFPDDLSY RWLLNEFPVF
     ITMDKRRFVS QTNGNLYIAN VESSDRGNYS CFVSSPSITK SVFSKFIPLI PIPERTTKPY
     PADIVVQFKD IYTMMGQNVT LECFALGNPV PDIRWRKVLE PMPSTAEIST SGAVLKIFNI
     QLEDEGLYEC EAENIRGKDK HQARIYVQAF PEWVEHINDT EVDIGSDLYW PCIATGKPIP
     TIRWLKNGYS YHKGELRLYD VTFENAGMYQ CIAENAYGSI YANAELKILA LAPTFEMNPM
     KKKILAAKGG RVIIECKPKA APKPKFSWSK GTEWLVNSSR ILIWEDGSLE INNITRNDGG
     IYTCFAENNR GKANSTGTLV ITNPTRIILA PINADITVGE NATMQCAASF DPALDLTFVW
     SFNGYVIDFN KEITHIHYQR NFMLDANGEL LIRNAQLKHA GRYTCTAQTI VDNSSASADL
     VVRGPPGPPG GLRIEDIRAT SVALTWSRGS DNHSPISKYT IQTKTILSDD WKDAKTDPPI
     IEGNMESAKA VDLIPWMEYE FRVVATNTLG TGEPSIPSNR IKTDGAAPNV APSDVGGGGG
     TNRELTITWA PLSREYHYGN NFGYIVAFKP FDGEEWKKVT VTNPDTGRYV HKDETMTPST
     AFQVKVKAFN NKGDGPYSLV AVINSAQDAP SEAPTEVGVK VLSSSEISVH WKHVLEKIVE
     SYQIRYWAGH DKEAAAHRVQ VTSQEYSARL ENLLPDTQYF IEVGACNSAG CGPSSDVIET
     FTRKAPPSQP PRIISSVRSG SRYIITWDHV VALSNESTVT GYKILYRPDG QHDGKLFSTH
     KHSIEVPIPR DGEYVVEVRA HSDGGDGVVS QVKISGVSTL SSSLLSLLLP SLGFLVYSEF
//
ID   7B2_MOUSE               Reviewed;         212 AA.
AC   P12961; Q8CCZ3; Q9CYP0; Q9D2P6; Q9DB14;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Neuroendocrine protein 7B2;
DE   AltName: Full=Secretogranin V;
DE   AltName: Full=Secretogranin-5;
DE   AltName: Full=Secretory granule endocrine protein I;
DE   Contains:
DE     RecName: Full=N-terminal peptide;
DE   Contains:
DE     RecName: Full=C-terminal peptide;
DE   Flags: Precursor;
GN   Name=Scg5; Synonyms=Sgne-1, Sgne1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=BALB/c; TISSUE=Pancreas;
RX   MEDLINE=89254271; PubMed=2542174;
RA   Mbikay M., Grant S.G.N., Sirois F., Tadros H., Skowronski J.,
RA   Lazure C., Seidah N.G., Hanahan D., Chretien M.;
RT   "cDNA sequence of neuroendocrine protein 7B2 expressed in beta cell
RT   tumors of transgenic mice.";
RL   Int. J. Pept. Protein Res. 33:39-45(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Embryo, Hippocampus, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   MEDLINE=98012196; PubMed=9348280; DOI=10.1083/jcb.139.3.625;
RA   Muller L., Zhu X., Lindberg I.;
RT   "Mechanism of the facilitation of PC2 maturation by 7B2: involvement
RT   in ProPC2 transport and activation but not folding.";
RL   J. Cell Biol. 139:625-638(1997).
RN   [5]
RP   FUNCTION.
RX   MEDLINE=99189754; PubMed=10089884; DOI=10.1016/S0092-8674(00)80579-6;
RA   Westphal C.H., Muller L., Zhou A., Zhu X., Bonner-Weir S.,
RA   Schambelan M., Steiner D.F., Lindberg I., Leder P.;
RT   "The neuroendocrine protein 7B2 is required for peptide hormone
RT   processing in vivo and provides a novel mechanism for pituitary
RT   Cushing's disease.";
RL   Cell 96:689-700(1999).
RN   [6]
RP   INHIBITION OF PCSK2 BY C-TERMINAL PEPTIDE.
RX   MEDLINE=94286522; PubMed=8016065; DOI=10.1073/pnas.91.13.5784;
RA   Martens G.J.M., Braks J.A., Eib D.W., Zhou Y., Lindberg I.;
RT   "The neuroendocrine polypeptide 7B2 is an endogenous inhibitor of
RT   prohormone convertase PC2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:5784-5787(1994).
RN   [7]
RP   SULFATION, CLEAVAGE BY FURIN-LIKE CONVERTASE, AND MUTAGENESIS OF
RP   ARG-177 AND ARG-178.
RX   MEDLINE=94308204; PubMed=8034690;
RA   Paquet L., Bergeron F., Boudreault A., Seidah N.G., Chretien M.,
RA   Mbikay M., Lazure C.;
RT   "The neuroendocrine precursor 7B2 is a sulfated protein
RT   proteolytically processed by a ubiquitous furin-like convertase.";
RL   J. Biol. Chem. 269:19279-19285(1994).
RN   [8]
RP   REVIEW.
RX   MEDLINE=21332545; PubMed=11439082; DOI=10.1042/0264-6021:3570329;
RA   Mbikay M., Seidah N.G., Chretien M.;
RT   "Neuroendocrine secretory protein 7B2: structure, expression and
RT   functions.";
RL   Biochem. J. 357:329-342(2001).
CC   -!- FUNCTION: Acts as a molecular chaperone for PCSK2/PC2, preventing
CC       its premature activation in the regulated secretory pathway. Binds
CC       to inactive PCSK2 in the endoplasmic reticulum and facilitates its
CC       transport from there to later compartments of the secretory
CC       pathway where it is proteolytically matured and activated. Also
CC       required for cleavage of PCSK2 but does not appear to be involved
CC       in its folding. Plays a role in regulating pituitary hormone
CC       secretion. The C-terminal peptide inhibits PCSK2 in vitro.
CC   -!- SUBUNIT: Interacts with PCSK2/PC2 early in the secretory pathway.
CC       Dissociation occurs at later stages (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Neuroendocrine and endocrine
CC       secretory granules.
CC   -!- PTM: Proteolytically cleaved in the Golgi by a furin-like
CC       convertase to generate bioactive peptides.
CC   -!- PTM: Sulfated on tyrosine residues.
CC   -!- DISRUPTION PHENOTYPE: Mice have no demonstrable Pcsk2/Pc2
CC       activity, are deficient in processing islet hormones, and display
CC       hypoglycemia, hyperproinsulinemia and hypoglucagonemia, similar to
CC       Pcsk2 null mice. In contrast to Pcsk2 null mice, they develop
CC       Cushing's disease due to excessive secretion of corticotropin from
CC       the pituitary and die before 9 weeks, indicating a role for Sgne1
CC       in control of peptide secretion from the pituitary.
CC   -!- SIMILARITY: Belongs to the 7B2 family.
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DR   EMBL; X15830; CAA33835.1; -; mRNA.
DR   EMBL; AK005331; BAB23956.1; -; mRNA.
DR   EMBL; AK011938; BAB27927.1; -; mRNA.
DR   EMBL; AK017481; BAB30765.1; -; mRNA.
DR   EMBL; AK019337; BAB31669.1; -; mRNA.
DR   EMBL; AK031856; BAC27581.1; -; mRNA.
DR   EMBL; BC029021; AAH29021.1; -; mRNA.
DR   IPI; IPI00123059; -.
DR   PIR; S12477; S12477.
DR   RefSeq; NP_033188.3; NM_009162.3.
DR   UniGene; Mm.4836; -.
DR   ProteinModelPortal; P12961; -.
DR   STRING; P12961; -.
DR   MEROPS; I21.001; -.
DR   PhosphoSite; P12961; -.
DR   PRIDE; P12961; -.
DR   Ensembl; ENSMUST00000024005; ENSMUSP00000024005; ENSMUSG00000023236.
DR   GeneID; 20394; -.
DR   KEGG; mmu:20394; -.
DR   UCSC; uc008lpq.1; mouse.
DR   CTD; 20394; -.
DR   MGI; MGI:98289; Scg5.
DR   eggNOG; roNOG09812; -.
DR   HOGENOM; HBG713767; -.
DR   HOVERGEN; HBG000031; -.
DR   InParanoid; P12961; -.
DR   OMA; GPYGNIP; -.
DR   OrthoDB; EOG44MXSZ; -.
DR   PhylomeDB; P12961; -.
DR   NextBio; 298342; -.
DR   ArrayExpress; P12961; -.
DR   Bgee; P12961; -.
DR   CleanEx; MM_SCG5; -.
DR   Genevestigator; P12961; -.
DR   GermOnline; ENSMUSG00000023236; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030141; C:stored secretory granule; ISS:UniProtKB.
DR   GO; GO:0004857; F:enzyme inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0051082; F:unfolded protein binding; ISS:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; IDA:UniProtKB.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0016486; P:peptide hormone processing; IDA:UniProtKB.
DR   GO; GO:0046883; P:regulation of hormone secretion; IDA:UniProtKB.
DR   InterPro; IPR007945; Secretogranin_V.
DR   PANTHER; PTHR12738; Secretogranin_V; 1.
DR   Pfam; PF05281; Secretogranin_V; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; Neuropeptide;
KW   Phosphoprotein; Secreted; Signal; Sulfation; Transport.
FT   SIGNAL        1     26
FT   CHAIN        27    212       Neuroendocrine protein 7B2.
FT                                /FTId=PRO_0000000044.
FT   CHAIN        27    176       N-terminal peptide (By similarity).
FT                                /FTId=PRO_0000000045.
FT   PEPTIDE     200    212       C-terminal peptide (By similarity).
FT                                /FTId=PRO_0000000046.
FT   MOD_RES     205    205       Phosphoserine (By similarity).
FT   DISULFID    120    130       By similarity.
FT   MUTAGEN     177    177       R->A: No effect on proteolytic
FT                                processing. Abolishes proteolytic
FT                                processing; when associated with G-178.
FT   MUTAGEN     178    178       R->G: Abolishes proteolytic processing;
FT                                when associated with A-177.
FT   CONFLICT      6      6       V -> G (in Ref. 2; BAB23956).
FT   CONFLICT    119    119       P -> H (in Ref. 2; BAB30765).
FT   CONFLICT    145    145       Q -> R (in Ref. 2; BAB31669).
FT   CONFLICT    153    153       P -> T (in Ref. 2; BAC27581).
SQ   SEQUENCE   212 AA;  23866 MW;  6D8CD046532F9609 CRC64;
     MASRLVSAML SGLLFWLMFE WNPAFAYSPR TPDRVSETDI QRLLHGVMEQ LGIARPRVEY
     PAHQAMNLVG PQSIEGGAHE GLQHLGPFGN IPNIVAELTG DNIPKDFSED QGYPDPPNPC
     PLGKTADDGC LENAPDTAEF SREFQLDQHL FDPEHDYPGL GKWNKKLLYE KMKGGQRRKR
     RSVNPYLQGK RLDNVVAKKS VPHFSEEEKE AE
//
ID   GELS_MOUSE              Reviewed;         780 AA.
AC   P13020; Q3UPB1; Q8R590;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   12-FEB-2003, sequence version 3.
DT   08-MAR-2011, entry version 117.
DE   RecName: Full=Gelsolin;
DE   AltName: Full=Actin-depolymerizing factor;
DE            Short=ADF;
DE   AltName: Full=Brevin;
DE   Flags: Precursor;
GN   Name=Gsn; Synonyms=Gsb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   MEDLINE=89327303; PubMed=2546951;
RA   Dieffenbach C.W., Sengupta D.N., Krause D., Sawzak D., Silverman R.H.;
RT   "Cloning of murine gelsolin and its regulation during differentiation
RT   of embryonal carcinoma cells.";
RL   J. Biol. Chem. 264:13281-13288(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 50-70 (ISOFORM 2), PROTEIN SEQUENCE OF 74-97;
RP   146-160; 167-186; 254-293; 301-336; 359-366; 372-388; 396-445;
RP   456-479; 529-546; 552-562; 583-621; 625-646; 667-673; 712-736 AND
RP   739-746 (ISOFORMS 1/2), CLEAVAGE OF INITIATOR METHIONINE (ISOFORM 2),
RP   ACETYLATION AT MET-1 (ISOFORM 2), AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RA   Sumpton D.P., Sandilands E., Frame M.C., Bienvenut W.V.;
RL   Submitted (MAR-2008) to UniProtKB.
RN   [5]
RP   PROTEIN SEQUENCE OF 51-73.
RC   TISSUE=Fibroblast;
RX   MEDLINE=95009907; PubMed=7523108; DOI=10.1002/elps.11501501101;
RA   Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.;
RT   "Separation and sequencing of familiar and novel murine proteins using
RT   preparative two-dimensional gel electrophoresis.";
RL   Electrophoresis 15:735-745(1994).
CC   -!- FUNCTION: Calcium-regulated, actin-modulating protein that binds
CC       to the plus (or barbed) ends of actin monomers or filaments,
CC       preventing monomer exchange (end-blocking or capping). It can
CC       promote the assembly of monomers into filaments (nucleation) as
CC       well as sever filaments already formed.
CC   -!- SUBUNIT: Binds to actin and to fibronectin.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytoskeleton.
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=1; Synonyms=Secreted, Plasma;
CC         IsoId=P13020-1; Sequence=Displayed;
CC       Name=2; Synonyms=Cytoplasmic;
CC         IsoId=P13020-2; Sequence=VSP_018960;
CC         Note=Initiator Met-1 is either removed, or N-acetylated;
CC   -!- PTM: Phosphorylated on tyrosine residues in vitro (By similarity).
CC   -!- SIMILARITY: Belongs to the villin/gelsolin family.
CC   -!- SIMILARITY: Contains 6 gelsolin-like repeats.
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DR   EMBL; J04953; AAA37677.1; -; mRNA.
DR   EMBL; AK076156; BAC36223.1; -; mRNA.
DR   EMBL; AK089934; BAC41004.1; -; mRNA.
DR   EMBL; AK143664; BAE25485.1; -; mRNA.
DR   EMBL; BC023143; AAH23143.2; -; mRNA.
DR   IPI; IPI00117167; -.
DR   IPI; IPI00759948; -.
DR   RefSeq; NP_666232.2; NM_146120.3.
DR   UniGene; Mm.21109; -.
DR   PDB; 1NPH; X-ray; 3.00 A; A=439-767.
DR   PDBsum; 1NPH; -.
DR   ProteinModelPortal; P13020; -.
DR   SMR; P13020; 48-780.
DR   IntAct; P13020; 5.
DR   STRING; P13020; -.
DR   PhosphoSite; P13020; -.
DR   REPRODUCTION-2DPAGE; P13020; -.
DR   PRIDE; P13020; -.
DR   Ensembl; ENSMUST00000028239; ENSMUSP00000028239; ENSMUSG00000026879.
DR   Ensembl; ENSMUST00000113016; ENSMUSP00000108639; ENSMUSG00000026879.
DR   GeneID; 227753; -.
DR   KEGG; mmu:227753; -.
DR   UCSC; uc008jkg.1; mouse.
DR   CTD; 227753; -.
DR   MGI; MGI:95851; Gsn.
DR   HOGENOM; HBG357198; -.
DR   HOVERGEN; HBG004183; -.
DR   InParanoid; P13020; -.
DR   OMA; KGKQANM; -.
DR   OrthoDB; EOG4Q58P0; -.
DR   PhylomeDB; P13020; -.
DR   NextBio; 378824; -.
DR   ArrayExpress; P13020; -.
DR   Bgee; P13020; -.
DR   CleanEx; MM_GSN; -.
DR   Genevestigator; P13020; -.
DR   GermOnline; ENSMUSG00000026879; Mus musculus.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR   GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR   GO; GO:0051014; P:actin filament severing; ISS:UniProtKB.
DR   GO; GO:0016192; P:vesicle-mediated transport; IMP:MGI.
DR   InterPro; IPR007122; Gelsolin.
DR   InterPro; IPR007123; Gelsolin_dom.
DR   PANTHER; PTHR11977; Gelsolin; 1.
DR   Pfam; PF00626; Gelsolin; 6.
DR   PRINTS; PR00597; GELSOLIN.
DR   SMART; SM00262; GEL; 6.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Actin capping; Actin-binding;
KW   Alternative initiation; Calcium; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Disulfide bond; Phosphoprotein; Repeat;
KW   Secreted; Signal.
FT   SIGNAL        1     25       Potential.
FT   CHAIN        26    780       Gelsolin.
FT                                /FTId=PRO_0000036387.
FT   REPEAT       74    124       Gelsolin-like 1.
FT   REPEAT      196    236       Gelsolin-like 2.
FT   REPEAT      312    354       Gelsolin-like 3.
FT   REPEAT      451    502       Gelsolin-like 4.
FT   REPEAT      574    614       Gelsolin-like 5.
FT   REPEAT      677    719       Gelsolin-like 6.
FT   REGION       51    174       Actin-severing (Potential).
FT   REGION      121    124       Actin-actin interfilament contact point.
FT   REGION      160    167       Polyphosphoinositide binding (By
FT                                similarity).
FT   REGION      186    194       Polyphosphoinositide binding (By
FT                                similarity).
FT   REGION      432    780       Actin-binding, Ca-sensitive (Potential).
FT   DISULFID    213    226       In isoform 1 (By similarity).
FT   VAR_SEQ       1     49       Missing (in isoform 2).
FT                                /FTId=VSP_018960.
FT   CONFLICT    262    263       GG -> ET (in Ref. 1; AAA37677).
FT   CONFLICT    274    274       P -> H (in Ref. 2; BAC41004).
FT   CONFLICT    294    294       R -> K (in Ref. 1; AAA37677).
FT   CONFLICT    316    316       E -> K (in Ref. 2; BAC41004).
FT   CONFLICT    323    323       A -> P (in Ref. 1; AAA37677).
FT   CONFLICT    423    423       A -> G (in Ref. 1; AAA37677).
FT   CONFLICT    615    615       G -> A (in Ref. 1; AAA37677).
FT   CONFLICT    638    638       A -> G (in Ref. 1; AAA37677).
FT   CONFLICT    648    648       A -> S (in Ref. 1; AAA37677).
FT   CONFLICT    763    763       D -> N (in Ref. 1; AAA37677).
FT   STRAND      445    451
FT   STRAND      454    457
FT   HELIX       460    462
FT   STRAND      465    467
FT   STRAND      470    477
FT   STRAND      486    492
FT   HELIX       498    514
FT   TURN        515    517
FT   STRAND      519    525
FT   HELIX       531    535
FT   TURN        536    539
FT   STRAND      542    546
FT   STRAND      551    553
FT   STRAND      560    568
FT   STRAND      570    572
FT   STRAND      574    579
FT   HELIX       583    585
FT   STRAND      590    595
FT   STRAND      600    604
FT   HELIX       610    623
FT   STRAND      627    631
FT   HELIX       637    643
FT   HELIX       653    656
FT   HELIX       660    662
FT   STRAND      666    671
FT   STRAND      674    676
FT   STRAND      678    681
FT   HELIX       688    690
FT   STRAND      695    700
FT   STRAND      705    709
FT   HELIX       715    729
FT   TURN        733    735
FT   STRAND      742    746
FT   HELIX       752    755
SQ   SEQUENCE   780 AA;  85942 MW;  AE94297BE457FF2D CRC64;
     MAPYRSSLLC ALLLLALCAL SPSHAATTSR GRAQERAPQS RVSEARPSTM VVEHPEFLKA
     GKEPGLQIWR VEKFDLVPVP PNLYGDFFTG DAYVILKTVQ LRNGNLQYDL HYWLGNECSQ
     DESGAAAIFT VQLDDYLNGR AVQHREVQGF ESSTFSGYFK SGLKYKKGGV ASGFKHVVPN
     EVVVQRLFQV KGRRVVRATE VPVSWDSFNN GDCFILDLGN NIYQWCGSGS NKFERLKATQ
     VSKGIRDNER SGRAQVHVSE EGGEPEAMLQ VLGPKPALPE GTEDTAKEDA ANRRLAKLYK
     VSNGAGSMSV SLVADENPFA QGALRSEDCF ILDHGRDGKI FVWKGKQANM EERKAALKTA
     SDFISKMQYP RQTQVSVLPE GGETPLFKQF FKNWRDPDQT DGPGLGYLSS HIANVERVPF
     DAATLHTSTA MAAQHGMDDD GTGQKQIWRI EGSNKVPVDP ATYGQFYGGD SYIILYNYRH
     GGRQGQIIYN WQGAQSTQDE VAASAILTAQ LDEELGGTPV QSRVVQGKEP AHLMSLFGGK
     PMIIYKGGTS RDGGQTAPAS IRLFQVRASS SGATRAVEVM PKSGALNSND AFVLKTPSAA
     YLWVGAGASE AEKTGAQELL KVLRSQHVQV EEGSEPDAFW EALGGKTAYR TSPRLKDKKM
     DAHPPRLFAC SNRIGRFVIE EVPGELMQED LATDDVMLLD TWDQVFVWVG KDSQEEEKTE
     ALTSAKRYIE TDPANRDRRT PITVVRQGFE PPSFVGWFLG WDDNYWSVDP LDRALAELAA
//
ID   RB_MOUSE                Reviewed;         921 AA.
AC   P13405;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   08-MAR-2011, entry version 122.
DE   RecName: Full=Retinoblastoma-associated protein;
DE   AltName: Full=pRb;
DE            Short=Rb;
DE   AltName: Full=pp105;
GN   Name=Rb1; Synonyms=Rb-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=89367271; PubMed=2671991; DOI=10.1073/pnas.86.17.6474;
RA   Bernards R., Schackleford G.M., Gerber M.R., Horowitz J.M.,
RA   Friend S.H., Schartl M., Bogenmann E., Rapaport J., McGee T.,
RA   Dryja T.P., Weinberg R.A.;
RT   "Structure and expression of the murine retinoblastoma gene and
RT   characterization of its encoded protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:6474-6478(1989).
RN   [2]
RP   INTERACTION WITH DNMT1.
RX   MEDLINE=20347723; PubMed=10888886; DOI=10.1038/77124;
RA   Robertson K.D., Ait-Si-Ali S., Yokochi T., Wade P.A., Jones P.L.,
RA   Wolffe A.P.;
RT   "DNMT1 forms a complex with Rb, E2F1 and HDAC1 and represses
RT   transcription from E2F-responsive promoters.";
RL   Nat. Genet. 25:338-342(2000).
RN   [3]
RP   INTERACTION WITH E4F1.
RX   PubMed=10869426; DOI=10.1073/pnas.130198397;
RA   Fajas L., Paul C., Zugasti O., Le Cam L., Polanowska J., Fabbrizio E.,
RA   Medema R., Vignais M.-L., Sardet C.;
RT   "pRB binds to and modulates the transrepressing activity of the E1A-
RT   regulated transcription factor p120E4F.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:7738-7743(2000).
RN   [4]
RP   INTERACTION WITH USP4.
RX   PubMed=11571651; DOI=10.1038/sj.onc.1204823;
RA   Blanchette P., Gilchrist C.A., Baker R.T., Gray D.A.;
RT   "Association of UNP, a ubiquitin-specific protease, with the pocket
RT   proteins pRb, p107 and p130.";
RL   Oncogene 20:5533-5537(2001).
RN   [5]
RP   TISSUE SPECIFICITY, AND CO-LOCALIZATION WITH RB1CC1.
RC   STRAIN=C57BL/6; TISSUE=Skeletal muscle;
RX   MEDLINE=22090535; PubMed=12095676; DOI=10.1016/S0378-1119(02)00585-1;
RA   Chano T., Ikegawa S., Saito-Ohara F., Inazawa J., Mabuchi A.,
RA   Saeki Y., Okabe H.;
RT   "Isolation, characterization and mapping of the mouse and human RB1CC1
RT   genes.";
RL   Gene 291:29-34(2002).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH SUV420H1 AND SUV420H2.
RX   PubMed=15750587; DOI=10.1038/ncb1235;
RA   Gonzalo S., Garcia-Cao M., Fraga M.F., Schotta G., Peters A.H.F.M.,
RA   Cotter S.E., Eguia R., Dean D.C., Esteller M., Jenuwein T.,
RA   Blasco M.A.;
RT   "Role of the RB1 family in stabilizing histone methylation at
RT   constitutive heterochromatin.";
RL   Nat. Cell Biol. 7:420-428(2005).
RN   [7]
RP   INTERACTION WITH ATAD5.
RX   PubMed=15983387; DOI=10.1073/pnas.0504222102;
RA   Ishii H., Inageta T., Mimori K., Saito T., Sasaki H., Isobe M.,
RA   Mori M., Croce C.M., Huebner K., Ozawa K., Furukawa Y.;
RT   "Frag1, a homolog of alternative replication factor C subunits, links
RT   replication stress surveillance with apoptosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:9655-9660(2005).
RN   [8]
RP   INTERACTION WITH PRMT2.
RX   PubMed=16616919; DOI=10.1016/j.yexcr.2006.03.001;
RA   Yoshimoto T., Boehm M., Olive M., Crook M.F., San H., Langenickel T.,
RA   Nabel E.G.;
RT   "The arginine methyltransferase PRMT2 binds RB and regulates E2F
RT   function.";
RL   Exp. Cell Res. 312:2040-2053(2006).
RN   [9]
RP   FUNCTION, INTERACTION WITH SUV420H1 AND SUV420H2, AND MUTAGENESIS OF
RP   ILE-746; ASN-750 AND MET-754.
RX   PubMed=16612004; DOI=10.1128/MCB.26.9.3659-3671.2006;
RA   Isaac C.E., Francis S.M., Martens A.L., Julian L.M., Seifried L.A.,
RA   Erdmann N., Binne U.K., Harrington L., Sicinski P., Berube N.G.,
RA   Dyson N.J., Dick F.A.;
RT   "The retinoblastoma protein regulates pericentric heterochromatin.";
RL   Mol. Cell. Biol. 26:3659-3671(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-819, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [11]
RP   CLEAVAGE OF INITIATOR METHIONINE, AND METHYLATION AT PRO-2.
RX   PubMed=20668449; DOI=10.1038/nature09343;
RA   Tooley C.E., Petkowski J.J., Muratore-Schroeder T.L., Balsbaugh J.L.,
RA   Shabanowitz J., Sabat M., Minor W., Hunt D.F., Macara I.G.;
RT   "NRMT is an alpha-N-methyltransferase that methylates RCC1 and
RT   retinoblastoma protein.";
RL   Nature 466:1125-1128(2010).
CC   -!- FUNCTION: Key regulator of entry into cell division that acts as a
CC       tumor suppressor. Acts as a transcription repressor of E2F1 target
CC       genes. The underphosphorylated, active form of RB1 interacts with
CC       E2F1 and represses its transcription activity, leading to cell
CC       cycle arrest. Directly involved in heterochromatin formation by
CC       maintaining overall chromatin structure and, in particular, that
CC       of constitutive heterochromatin by stabilizing histone
CC       methylation. Recruits and targets histone methyltransferases
CC       SUV39H1, SUV420H1 and SUV420H2, leading to epigenetic
CC       transcriptional repression. Controls histone H4 'Lys-20'
CC       trimethylation. Inhibits the intrinsic kinase activity of TAF1.
CC       Mediates transcriptional repression by SMARCA4/BRG1 by recruiting
CC       a histone deacetylase (HDAC) complex to the c-FOS promoter. In
CC       resting neurons, transcription of the c-FOS promoter is inhibited
CC       by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor
CC       complex. Upon calcium influx, RB1 is dephosphorylated by
CC       calcineurin, which leads to release of the repressor complex (By
CC       similarity).
CC   -!- SUBUNIT: The hypophosphorylated form interacts with and sequesters
CC       the E2F1 transcription factor. Interacts with heterodimeric E2F/DP
CC       transcription factor complexes containing TFDP1 and either E2F1,
CC       E2F3, E2F4 or E2F5, or TFDP2 and E2F4. The unphosphorylated form
CC       interacts with EID1, ARID3B, KDM5A, SUV39H1, MJD2A/JHDM3A and
CC       THOC1. Interacts with the N-terminal domain of TAF1. Interacts
CC       with ATAD5, AATF, DNMT1, LIN9, LMNA, SUV420H1, SUV420H2, PELP1,
CC       TMPO-alpha and USP4. May interact with NDC80. Interacts with GRIP1
CC       and UBR4. Interacts with ARID4A and KDM5B. Interacts with E4F1 and
CC       LIMD1. Interacts with SMARCA4/BRG1 and HDAC1. Interacts with USP4.
CC       Interacts (when methylated at Lys-853) with L3MBTL1 (By
CC       similarity). Interacts with PRMT2.
CC   -!- INTERACTION:
CC       P12534:- (xeno); NbExp=1; IntAct=EBI-971782, EBI-1213075;
CC       Q155P7:Cenpf; NbExp=3; IntAct=EBI-971782, EBI-2211248;
CC       Q80UP3:Dgkz; NbExp=1; IntAct=EBI-971782, EBI-971774;
CC       P52927:Hmga2; NbExp=1; IntAct=EBI-971782, EBI-912574;
CC       P24610:Pax3; NbExp=3; IntAct=EBI-971782, EBI-1208116;
CC       P62137:Ppp1ca; NbExp=1; IntAct=EBI-971782, EBI-357187;
CC       P62141:Ppp1cb; NbExp=1; IntAct=EBI-971782, EBI-352338;
CC       P63087:Ppp1cc; NbExp=1; IntAct=EBI-971782, EBI-80040;
CC       P63087-1:Ppp1cc; NbExp=1; IntAct=EBI-971782, EBI-450267;
CC       Q9R144:Prmt2; NbExp=1; IntAct=EBI-971782, EBI-1212945;
CC       Q3TKT4:Smarca4; NbExp=1; IntAct=EBI-971782, EBI-1210244;
CC       Q61412:Vsx2; NbExp=2; IntAct=EBI-971782, EBI-1208174;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed in the cell nuclei of renal tubules,
CC       hepathocytes and skeletal muscles. Co-localizes with RB1CC1 in
CC       various tissues.
CC   -!- PTM: Phosphorylated in G1, thereby releasing E2F1 which is then
CC       able to activate cell growth. Dephosphorylated at the late M
CC       phase. Phosphorylation of threonine residues in domain C promotes
CC       interaction between the C-terminal domain C and the Pocket domain,
CC       and thereby inhibits interactions with heterodimeric E2F/DP
CC       transcription factor complexes. Dephosphorylated at Ser-788 by
CC       calcineruin upon calcium stimulation (By similarity).
CC   -!- PTM: Monomethylated at Lys-853 by SMYD2, promoting interaction
CC       with L3MBTL1 (By similarity). N-terminus is methylated by
CC       METTL11A/NTM1.
CC   -!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=Retinoblastoma protein entry;
CC       URL="http://en.wikipedia.org/wiki/Retinoblastoma_protein";
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DR   EMBL; M26391; AAA39964.1; -; mRNA.
DR   IPI; IPI00121418; -.
DR   PIR; A33718; A33718.
DR   UniGene; Mm.273862; -.
DR   ProteinModelPortal; P13405; -.
DR   SMR; P13405; 47-349, 372-778, 822-865.
DR   DIP; DIP-37637N; -.
DR   IntAct; P13405; 23.
DR   MINT; MINT-225292; -.
DR   STRING; P13405; -.
DR   PhosphoSite; P13405; -.
DR   PRIDE; P13405; -.
DR   Ensembl; ENSMUST00000022701; ENSMUSP00000022701; ENSMUSG00000022105.
DR   UCSC; uc007upp.1; mouse.
DR   MGI; MGI:97874; Rb1.
DR   eggNOG; roNOG13978; -.
DR   HOGENOM; HBG445287; -.
DR   HOVERGEN; HBG008967; -.
DR   InParanoid; P13405; -.
DR   OrthoDB; EOG4TXBRB; -.
DR   ArrayExpress; P13405; -.
DR   Bgee; P13405; -.
DR   CleanEx; MM_RB1; -.
DR   Genevestigator; P13405; -.
DR   GermOnline; ENSMUSG00000022105; Mus musculus.
DR   GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR   GO; GO:0005819; C:spindle; IDA:MGI.
DR   GO; GO:0005667; C:transcription factor complex; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0019900; F:kinase binding; ISS:UniProtKB.
DR   GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0016564; F:transcription repressor activity; IDA:MGI.
DR   GO; GO:0007050; P:cell cycle arrest; IMP:MGI.
DR   GO; GO:0051301; P:cell division; IMP:MGI.
DR   GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IMP:MGI.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0048565; P:digestive tract development; IMP:MGI.
DR   GO; GO:0043353; P:enucleate erythrocyte differentiation; IGI:MGI.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI.
DR   GO; GO:0045445; P:myoblast differentiation; ISS:UniProtKB.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0051402; P:neuron apoptosis; IMP:MGI.
DR   GO; GO:0042551; P:neuron maturation; IMP:MGI.
DR   GO; GO:0031175; P:neuron projection development; IMP:MGI.
DR   GO; GO:0045651; P:positive regulation of macrophage differentiation; IGI:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0043550; P:regulation of lipid kinase activity; ISS:UniProtKB.
DR   GO; GO:0007090; P:regulation of S phase of mitotic cell cycle; IMP:MGI.
DR   GO; GO:0051146; P:striated muscle cell differentiation; IGI:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR006670; Cyclin.
DR   InterPro; IPR011028; Cyclin-like.
DR   InterPro; IPR013763; Cyclin-related.
DR   InterPro; IPR002720; RB_A.
DR   InterPro; IPR015652; Rb_associated.
DR   InterPro; IPR002719; RB_B.
DR   InterPro; IPR015030; Rb_C.
DR   Gene3D; G3DSA:1.10.472.10; Cyclin_related; 2.
DR   PANTHER; PTHR13742:SF10; Rb_associated; 1.
DR   Pfam; PF01858; RB_A; 1.
DR   Pfam; PF01857; RB_B; 1.
DR   Pfam; PF08934; Rb_C; 1.
DR   SMART; SM00385; CYCLIN; 1.
DR   SUPFAM; SSF47954; Cyclin_like; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Cell cycle; Chromatin regulator; DNA-binding;
KW   Methylation; Nucleus; Phosphoprotein; Repressor; Transcription;
KW   Transcription regulation; Tumor suppressor.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    921       Retinoblastoma-associated protein.
FT                                /FTId=PRO_0000167837.
FT   REGION      367    764       Pocket; binds T and E1A (By similarity).
FT   REGION      367    573       Domain A (By similarity).
FT   REGION      574    632       Spacer (By similarity).
FT   REGION      633    764       Domain B (By similarity).
FT   REGION      756    921       Interaction with LIMD1 (By similarity).
FT   REGION      764    921       Domain; mediates interaction with E4F1
FT                                (By similarity).
FT   MOTIF       863    869       Nuclear localization signal (By
FT                                similarity).
FT   COMPBIAS      9     12       Poly-Ala.
FT   COMPBIAS     14     22       Poly-Pro.
FT   MOD_RES       2      2       N,N-dimethylproline; by NTM1.
FT   MOD_RES      31     31       Phosphoserine (By similarity).
FT   MOD_RES     243    243       Phosphoserine; by CDK1 (By similarity).
FT   MOD_RES     246    246       Phosphothreonine; by CDK1 (By
FT                                similarity).
FT   MOD_RES     350    350       Phosphothreonine (By similarity).
FT   MOD_RES     367    367       Phosphothreonine; by CDK1 (By
FT                                similarity).
FT   MOD_RES     542    542       N6-acetyllysine (By similarity).
FT   MOD_RES     788    788       Phosphoserine (By similarity).
FT   MOD_RES     800    800       Phosphoserine; by CDK1 (By similarity).
FT   MOD_RES     804    804       Phosphoserine; by CDK1 (By similarity).
FT   MOD_RES     814    814       Phosphothreonine (By similarity).
FT   MOD_RES     816    816       Phosphothreonine (By similarity).
FT   MOD_RES     819    819       Phosphothreonine.
FT   MOD_RES     834    834       Phosphothreonine (By similarity).
FT   MOD_RES     848    848       Phosphoserine (By similarity).
FT   MOD_RES     853    853       N6-methyllysine; by SMYD2; alternate (By
FT                                similarity).
FT   MOD_RES     889    889       N6-acetyllysine (By similarity).
FT   MUTAGEN     746    746       I->A: Abolishes the interaction with many
FT                                chromatin regulators but not that with
FT                                SUV420H1 and SUV420H2; when associated
FT                                with A-750 and A-754.
FT   MUTAGEN     750    750       N->A: Abolishes the interaction with many
FT                                chromatin regulators but not that with
FT                                SUV420H1 and SUV420H2; when associated
FT                                with A-746 and A-754.
FT   MUTAGEN     754    754       M->A: Abolishes the interaction with many
FT                                chromatin regulators but not that with
FT                                SUV420H1 and SUV420H2; when associated
FT                                with A-746 and A-750.
SQ   SEQUENCE   921 AA;  105338 MW;  149ED65A07BC6495 CRC64;
     MPPKAPRRAA AAEPPPPPPP PPREDDPAQD SGPEELPLAR LEFEEIEEPE FIALCQKLKV
     PDHVRERAWL TWEKVSSVDG ILEGYIQKKK ELWGICIFIA AVDLDEMPFT FTELQKSIET
     SVYKFFDLLK EIDTSTKVDN AMSRLLKKYN VLCALYSKLE RTCELIYLTQ PSSALSTEIN
     SMLVLKISWI TFLLAKGEVL QMEDDLVISF QLMLCVVDYF IKFSPPALLR EPYKTAAIPI
     NGSPRTPRRG QNRSARIAKQ LENDTRIIEV LCKEHECNID EVKNVYFKNF IPFINSLGIV
     SSNGLPEVES LSKRYEEVYL KNKDLDARLF LDHDKTLQTD PIDSFETERT PRKNNPDEEA
     NVVTPHTPVR TVMNTIQQLM VILNSASDQP SENLISYFNN CTVNPKENIL KRVKDVGHIF
     KEKFANAVGQ GCVDIGVQRY KLGVRLYYRV MESMLKSEEE RLSIQNFSKL LNDNIFHMSL
     LACALEVVMA TYSRSTLQHL DSGTDLSFPW ILNVLNLKAF DFYKVIESFI KVEANLTREM
     IKHLERCEHR IMESLAWLSD SPLFDLIKQS KDGEGPDNLE PACPLSLPLQ GNHTAADMYL
     SPLRSPKKRT STTRVNSAAN TETQAASAFH TQKPLKSTSL ALFYKKVYRL AYLRLNTLCA
     RLLSDHPELE HIIWTLFQHT LQNEYELMRD RHLDQIMMCS MYGICKVKNI DLKFKIIVTA
     YKDLPHAAQE TFKRVLIREE EFDSIIVFYN SVFMQRLKTN ILQYASTRPP TLSPIPHIPR
     SPYKFSSSPL RIPGGNIYIS PLKSPYKISE GLPTPTKMTP RSRILVSIGE SFGTSEKFQK
     INQMVCNSDR VLKRSAEGGN PPKPLKNVRF DIEGADEADG SKHLPAESKF QQKLAEMTST
     RTRMQKQRMN ESKDVSNKEE K
//
ID   NCAM1_MOUSE             Reviewed;        1115 AA.
AC   P13595; P13594; Q61949; Q61950; Q6LBU8; Q8BQ96; Q8C4B2; Q921P2;
AC   Q9R2A7;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 3.
DT   08-MAR-2011, entry version 119.
DE   RecName: Full=Neural cell adhesion molecule 1;
DE            Short=N-CAM-1;
DE            Short=NCAM-1;
DE   AltName: CD_antigen=CD56;
DE   Flags: Precursor;
GN   Name=Ncam1; Synonyms=Ncam;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=87246524; PubMed=3595563;
RA   Barthels D., Santoni M.-J., Wille W., Ruppert C., Chaix J.-C.,
RA   Hirsch M.-R., Fontecilla-Camps J.-C., Goridis C.;
RT   "Isolation and nucleotide sequence of mouse NCAM cDNA that codes for a
RT   Mr 79,000 polypeptide without a membrane-spanning region.";
RL   EMBO J. 6:907-914(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1106 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 20-700 AND 702-1115 (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=89251563; PubMed=2721486;
RA   Santoni M.J., Barthels D., Vopper G., Boned A., Goridis C., Wille W.;
RT   "Differential exon usage involving an unusual splicing mechanism
RT   generates at least eight types of NCAM cDNA in mouse brain.";
RL   EMBO J. 8:385-392(1989).
RN   [5]
RP   PROTEIN SEQUENCE OF 20-36.
RX   MEDLINE=86140120; PubMed=3512556;
RA   Rougon G., Marshak D.R.;
RT   "Structural and immunological characterization of the amino-terminal
RT   domain of mammalian neural cell adhesion molecules.";
RL   J. Biol. Chem. 261:3396-3401(1986).
RN   [6]
RP   PROTEIN SEQUENCE OF 38-48; 122-152; 166-177; 555-572; 584-595;
RP   607-619; 652-662 AND 685-691, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 529-1115 (ISOFORM 2).
RC   STRAIN=C57BL/6;
RX   MEDLINE=88067687; PubMed=3684567; DOI=10.1093/nar/15.21.8621;
RA   Santoni M.-J., Barthels D., Barbas J.A., Hirsch M.-R., Steinmetz M.,
RA   Goridis C., Wille W.;
RT   "Analysis of cDNA clones that code for the transmembrane forms of the
RT   mouse neural cell adhesion molecule (NCAM) and are generated by
RT   alternative RNA splicing.";
RL   Nucleic Acids Res. 15:8621-8641(1987).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 642-1115.
RX   MEDLINE=88283628; PubMed=3396534;
RA   Barbas J.A., Chaix J.-C., Steinmetz M., Goridis C.;
RT   "Differential splicing and alternative polyadenylation generates
RT   distinct NCAM transcripts and proteins in the mouse.";
RL   EMBO J. 7:625-632(1988).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 804-1081 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   MEDLINE=88247737; PubMed=2454455; DOI=10.1093/nar/16.10.4217;
RA   Barthels D., Vopper G., Wille W.;
RT   "NCAM-180, the large isoform of the neural cell adhesion molecule of
RT   the mouse, is encoded by an alternatively spliced transcript.";
RL   Nucleic Acids Res. 16:4217-4225(1988).
RN   [10]
RP   GLYCOSYLATION AT ASN-222; ASN-316; ASN-348; ASN-424; ASN-450 AND
RP   ASN-479, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=14658030; DOI=10.1007/s00216-003-2383-2;
RA   Albach C., Damoc E., Denzinger T., Schachner M., Przybylski M.,
RA   Schmitz B.;
RT   "Identification of N-glycosylation sites of the murine neural cell
RT   adhesion molecule NCAM by MALDI-TOF and MALDI-FTICR mass
RT   spectrometry.";
RL   Anal. Bioanal. Chem. 378:1129-1135(2004).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-887; SER-946; THR-950;
RP   SER-958 AND SER-1005, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774; SER-887; SER-946;
RP   THR-950; THR-952; SER-958 AND SER-1005, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [15]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-450 AND ASN-453, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [16]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-450, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [17]
RP   STRUCTURE BY NMR OF 20-116, AND DISULFIDE BONDS.
RX   PubMed=8673600; DOI=10.1038/nsb0796-581;
RA   Thomsen N.K., Soroka V., Jensen P.H., Berezin V., Kiselyov V.V.,
RA   Bock E., Poulsen F.M.;
RT   "The three-dimensional structure of the first domain of neural cell
RT   adhesion molecule.";
RL   Nat. Struct. Biol. 3:581-585(1996).
RN   [18]
RP   STRUCTURE BY NMR OF 119-208, AND DISULFIDE BONDS.
RX   PubMed=10331878; DOI=10.1038/8292;
RA   Jensen P.H., Soroka V., Thomsen N.K., Ralets I., Berezin V., Bock E.,
RA   Poulsen F.M.;
RT   "Structure and interactions of NCAM modules 1 and 2, basic elements in
RT   neural cell adhesion.";
RL   Nat. Struct. Biol. 6:486-493(1999).
CC   -!- FUNCTION: This protein is a cell adhesion molecule involved in
CC       neuron-neuron adhesion, neurite fasciculation, outgrowth of
CC       neurites, etc.
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
CC       membrane protein.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Single-pass type I
CC       membrane protein.
CC   -!- SUBCELLULAR LOCATION: Isoform 3: Cell membrane; Lipid-anchor, GPI-
CC       anchor.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=N-CAM 180;
CC         IsoId=P13595-1; Sequence=Displayed;
CC       Name=2; Synonyms=N-CAM 140;
CC         IsoId=P13595-2; Sequence=VSP_002588;
CC       Name=3; Synonyms=N-CAM 120;
CC         IsoId=P13595-3, P13594-1;
CC         Sequence=VSP_034828, VSP_034829;
CC         Note=GPI-anchored form. GPI-anchor amidated asparagine at
CC         position Ser-706;
CC       Name=4;
CC         IsoId=P13595-4; Sequence=VSP_034826, VSP_034827;
CC   -!- SIMILARITY: Contains 2 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 5 Ig-like C2-type (immunoglobulin-like)
CC       domains.
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DR   EMBL; Y00051; CAA68263.1; -; mRNA.
DR   EMBL; BC011310; AAH11310.1; -; mRNA.
DR   EMBL; AK051197; BAC34554.2; -; mRNA.
DR   EMBL; AK082621; BAC38551.2; -; mRNA.
DR   EMBL; X15049; CAA33148.1; -; mRNA.
DR   EMBL; X15051; CAA33150.1; -; mRNA.
DR   EMBL; X15052; CAA33151.1; -; mRNA.
DR   EMBL; X06328; CAA29641.1; -; mRNA.
DR   EMBL; X07195; CAA30173.1; -; Genomic_DNA.
DR   EMBL; X07197; CAA30175.1; -; Genomic_DNA.
DR   EMBL; X07198; CAB40820.1; -; Genomic_DNA.
DR   EMBL; X07200; CAA30177.1; -; Genomic_DNA.
DR   EMBL; X07244; CAA30230.1; -; mRNA.
DR   IPI; IPI00122971; -.
DR   IPI; IPI00230665; -.
DR   IPI; IPI00830721; -.
DR   IPI; IPI00900395; -.
DR   PIR; A29673; IJMSNL.
DR   RefSeq; NP_001074914.1; NM_001081445.1.
DR   RefSeq; NP_001106675.1; NM_001113204.1.
DR   RefSeq; NP_035005.2; NM_010875.3.
DR   UniGene; Mm.439182; -.
DR   UniGene; Mm.4974; -.
DR   PDB; 2NCM; NMR; -; A=20-116.
DR   PDB; 3NCM; NMR; -; A=119-208.
DR   PDBsum; 2NCM; -.
DR   PDBsum; 3NCM; -.
DR   ProteinModelPortal; P13595; -.
DR   SMR; P13595; 20-696.
DR   MINT; MINT-1176881; -.
DR   PhosphoSite; P13595; -.
DR   PRIDE; P13595; -.
DR   Ensembl; ENSMUST00000053131; ENSMUSP00000058580; ENSMUSG00000039542.
DR   Ensembl; ENSMUST00000114481; ENSMUSP00000110125; ENSMUSG00000039542.
DR   Ensembl; ENSMUST00000114483; ENSMUSP00000110127; ENSMUSG00000039542.
DR   GeneID; 17967; -.
DR   KEGG; mmu:17967; -.
DR   CTD; 17967; -.
DR   MGI; MGI:97281; Ncam1.
DR   HOVERGEN; HBG052579; -.
DR   InParanoid; P13595; -.
DR   OrthoDB; EOG40VVP1; -.
DR   NextBio; 292903; -.
DR   ArrayExpress; P13595; -.
DR   Bgee; P13595; -.
DR   Genevestigator; P13595; -.
DR   GermOnline; ENSMUSG00000039542; Mus musculus.
DR   GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0007166; P:cell surface receptor linked signaling pathway; IDA:MGI.
DR   GO; GO:0034109; P:homotypic cell-cell adhesion; IMP:MGI.
DR   GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IDA:MGI.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR009138; Neural_cell_adh.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 7.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07679; I-set; 5.
DR   PRINTS; PR01838; NCAMFAMILY.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00408; IGc2; 5.
DR   SUPFAM; SSF49265; FN_III-like; 2.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS50835; IG_LIKE; 5.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Heparin-binding; Immunoglobulin domain; Lipoprotein; Membrane;
KW   Phosphoprotein; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     19
FT   CHAIN        20   1115       Neural cell adhesion molecule 1.
FT                                /FTId=PRO_0000015012.
FT   TOPO_DOM     20    711       Extracellular (Potential).
FT   TRANSMEM    712    729       Helical; (Potential).
FT   TOPO_DOM    730   1115       Cytoplasmic (Potential).
FT   DOMAIN       20    111       Ig-like C2-type 1.
FT   DOMAIN      116    205       Ig-like C2-type 2.
FT   DOMAIN      212    302       Ig-like C2-type 3.
FT   DOMAIN      309    402       Ig-like C2-type 4.
FT   DOMAIN      407    492       Ig-like C2-type 5.
FT   DOMAIN      497    596       Fibronectin type-III 1.
FT   DOMAIN      598    692       Fibronectin type-III 2.
FT   REGION      152    156       Heparin-binding (Potential).
FT   REGION      161    165       Heparin-binding (Potential).
FT   MOD_RES     774    774       Phosphoserine.
FT   MOD_RES     887    887       Phosphoserine.
FT   MOD_RES     946    946       Phosphoserine.
FT   MOD_RES     950    950       Phosphothreonine.
FT   MOD_RES     952    952       Phosphothreonine.
FT   MOD_RES     958    958       Phosphoserine.
FT   MOD_RES    1005   1005       Phosphoserine.
FT   CARBOHYD    222    222       N-linked (GlcNAc...); partial.
FT   CARBOHYD    316    316       N-linked (GlcNAc...).
FT   CARBOHYD    348    348       N-linked (GlcNAc...).
FT   CARBOHYD    424    424       N-linked (GlcNAc...).
FT   CARBOHYD    450    450       N-linked (GlcNAc...).
FT   CARBOHYD    453    453       N-linked (GlcNAc...).
FT   CARBOHYD    479    479       N-linked (GlcNAc...).
FT   DISULFID     41     96
FT   DISULFID    139    189
FT   DISULFID    235    288       Probable.
FT   DISULFID    330    386       Probable.
FT   DISULFID    427    480       Probable.
FT   VAR_SEQ     601    605       EPSAP -> KSSLF (in isoform 4).
FT                                /FTId=VSP_034826.
FT   VAR_SEQ     606   1115       Missing (in isoform 4).
FT                                /FTId=VSP_034827.
FT   VAR_SEQ     702    725       NGSPTAGLSTGAIVGILIVIFVLL -> TLGGSSTSYTLVS
FT                                LLFSAVTLLLL (in isoform 3).
FT                                /FTId=VSP_034828.
FT   VAR_SEQ     726   1115       Missing (in isoform 3).
FT                                /FTId=VSP_034829.
FT   VAR_SEQ     810   1076       Missing (in isoform 2).
FT                                /FTId=VSP_002588.
FT   CONFLICT     20     20       L -> M (in Ref. 4; CAA33148).
FT   CONFLICT    158    158       V -> F (in Ref. 2; AAH11310).
FT   CONFLICT    261    268       DEKHIFSD -> ERSRSSVS (in Ref. 1;
FT                                CAA68263).
FT   CONFLICT    273    273       L -> V (in Ref. 1; CAA68263).
FT   CONFLICT    354    355       KT -> QD (in Ref. 1; CAA68263).
FT   CONFLICT    379    379       T -> R (in Ref. 1; CAA68263 and 4;
FT                                CAA33148).
FT   CONFLICT    385    385       I -> M (in Ref. 1; CAA68263 and 4;
FT                                CAA33148).
FT   CONFLICT    399    400       MY -> ID (in Ref. 1; CAA68263 and 4;
FT                                CAA33148).
FT   CONFLICT    403    403       F -> V (in Ref. 2; AAH11310 and 3;
FT                                BAC34554/BAC38551).
FT   CONFLICT    549    549       K -> T (in Ref. 1; CAA68263).
FT   CONFLICT    572    572       R -> T (in Ref. 1; CAA68263).
FT   CONFLICT    575    575       V -> D (in Ref. 1; CAA68263).
FT   CONFLICT    589    594       SAATEF -> MQPSES (in Ref. 1; CAA68263).
FT   CONFLICT    600    602       REP -> PEL (in Ref. 1; CAA68263).
FT   CONFLICT    657    657       D -> H (in Ref. 1; CAA68263).
FT   CONFLICT    733    733       C -> W (in Ref. 3; BAC34554).
FT   CONFLICT   1082   1082       T -> A (in Ref. 3; BAC34554).
FT   STRAND       21     32
FT   STRAND       37     44
FT   STRAND       47     49
FT   STRAND       51     56
FT   TURN         57     59
FT   STRAND       64     73
FT   STRAND       75     77
FT   STRAND       79     85
FT   TURN         88     90
FT   STRAND       92     99
FT   STRAND      101    103
FT   STRAND      105    115
FT   STRAND      119    122
FT   STRAND      125    128
FT   STRAND      133    137
FT   STRAND      140    143
FT   STRAND      145    157
FT   HELIX       158    161
FT   STRAND      166    168
FT   STRAND      174    178
FT   STRAND      185    193
FT   TURN        194    197
FT   STRAND      198    207
SQ   SEQUENCE   1115 AA;  119427 MW;  78AF831BABD23918 CRC64;
     MLRTKDLIWT LFFLGTAVSL QVDIVPSQGE ISVGESKFFL CQVAGDAKDK DISWFSPNGE
     KLSPNQQRIS VVWNDDDSST LTIYNANIDD AGIYKCVVTA EDGTQSEATV NVKIFQKLMF
     KNAPTPQEFK EGEDAVIVCD VVSSLPPTII WKHKGRDVIL KKDVRFIVLS NNYLQIRGIK
     KTDEGTYRCE GRILARGEIN FKDIQVIVNV PPTVQARQSI VNATANLGQS VTLVCDADGF
     PEPTMSWTKD GEPIENEEED DEKHIFSDDS SELTIRNVDK NDEAEYVCIA ENKAGEQDAS
     IHLKVFAKPK ITYVENQTAM ELEEQVTLTC EASGDPIPSI TWRTSTRNIS SEEKTLDGHM
     VVRSHARVSS LTLKSIQYTD AGEYICTASN TIGQDSQSMY LEFQYAPKLQ GPVAVYTWEG
     NQVNITCEVF AYPSATISWF RDGQLLPSSN YSNIKIYNTP SASYLEVTPD SENDFGNYNC
     TAVNRIGQES LEFILVQADT PSSPSIDRVE PYSSTAQVQF DEPEATGGVP ILKYKAEWKS
     LGEESWHFKW YDAKEANMEG IVTIMGLKPE TRYSVRLAAL NGKGLGEISA ATEFKTQPVR
     EPSAPKLEGQ MGEDGNSIKV NLIKQDDGGS PIRHYLVKYR ALASEWKPEI RLPSGSDHVM
     LKSLDWNAEY EVYVVAENQQ GKSKAAHFVF RTSAQPTAIP ANGSPTAGLS TGAIVGILIV
     IFVLLLVVMD ITCYFLNKCG LLMCIAVNLC GKAGPGAKGK DMEEGKAAFS KDESKEPIVE
     VRTEEERTPN HDGGKHTEPN ETTPLTEPEL PADTTATVED MLPSVTTVTT NSDTITETFA
     TAQNSPTSET TTLTSSIAPP ATTVPDSNSV PAGQATPSKG VTASSSSPAS APKVAPLVDL
     SDTPTSAPSA SNLSSTVLAN QGAVLSPSTP ASAGETSKAP PASKASPAPT PTPAGAASPL
     AAVAAPATDA PQAKQEAPST KGPDPEPTQP GTVKNPPEAA TAPASPKSKA ATTNPSQGED
     LKMDEGNFKT PDIDLAKDVF AALGSPRPAT GASGQASELA PSPADSAVPP APAKTEKGPV
     ETKSEPPESE AKPAPTEVKT VPNDATQTKE NESKA
//
ID   B3A2_MOUSE              Reviewed;        1237 AA.
AC   P13808; Q9ES09; Q9ES10; Q9ES11; Q9ES12; Q9ES13;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   08-MAR-2011, entry version 102.
DE   RecName: Full=Anion exchange protein 2;
DE            Short=AE 2;
DE            Short=Anion exchanger 2;
DE   AltName: Full=Band 3-related protein;
DE            Short=B3RP;
DE   AltName: Full=Non-erythroid band 3-like protein;
DE   AltName: Full=Solute carrier family 4 member 2;
GN   Name=Slc4a2; Synonyms=Ae2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX   MEDLINE=89034212; PubMed=3182834;
RA   Alper S.L., Kopito R.R., Libresco S.M., Lodish H.F.;
RT   "Cloning and characterization of a murine band 3-related cDNA from
RT   kidney and from a lymphoid cell line.";
RL   J. Biol. Chem. 263:17092-17099(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND TISSUE
RP   SPECIFICITY.
RX   MEDLINE=20462926; PubMed=11006093; DOI=10.1006/bbrc.2000.3439;
RA   Lecanda J., Urtasun R., Medina J.F.;
RT   "Molecular cloning and genomic organization of the mouse AE2 anion
RT   exchanger gene.";
RL   Biochem. Biophys. Res. Commun. 276:117-124(2000).
CC   -!- FUNCTION: Plasma membrane anion exchange protein of wide
CC       distribution.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=A;
CC         IsoId=P13808-1; Sequence=Displayed;
CC       Name=B1;
CC         IsoId=P13808-2; Sequence=VSP_000458;
CC       Name=B2;
CC         IsoId=P13808-3; Sequence=VSP_000457;
CC       Name=C1;
CC         IsoId=P13808-4; Sequence=VSP_000460;
CC       Name=C2;
CC         IsoId=P13808-5; Sequence=VSP_000459, VSP_000461;
CC   -!- TISSUE SPECIFICITY: Isoform a is widely expressed at similar
CC       levels in all tissues examined. Isoforms B1 and B2 are
CC       predominantly expressed in stomach although they are also detected
CC       at lower levels in other tissues. Isoform C1 is stomach-specific.
CC       Isoform C2 is expressed at slightly higher levels in lung and
CC       stomach than in other tissues.
CC   -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
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DR   EMBL; J04036; AAA65505.1; -; mRNA.
DR   EMBL; AF255774; AAG23154.1; -; Genomic_DNA.
DR   EMBL; AF255774; AAG23155.1; -; Genomic_DNA.
DR   EMBL; AF255774; AAG23156.1; -; Genomic_DNA.
DR   EMBL; AF255774; AAG23158.1; -; Genomic_DNA.
DR   EMBL; AF255774; AAG23157.1; -; Genomic_DNA.
DR   IPI; IPI00126500; -.
DR   IPI; IPI00230579; -.
DR   IPI; IPI00230580; -.
DR   IPI; IPI00230581; -.
DR   IPI; IPI00230582; -.
DR   PIR; A31789; A31789.
DR   RefSeq; NP_033233.2; NM_009207.3.
DR   UniGene; Mm.4580; -.
DR   ProteinModelPortal; P13808; -.
DR   SMR; P13808; 317-637, 688-729, 1129-1161.
DR   STRING; P13808; -.
DR   PhosphoSite; P13808; -.
DR   PRIDE; P13808; -.
DR   Ensembl; ENSMUST00000080067; ENSMUSP00000078972; ENSMUSG00000028962.
DR   Ensembl; ENSMUST00000115047; ENSMUSP00000110699; ENSMUSG00000028962.
DR   Ensembl; ENSMUST00000115049; ENSMUSP00000110701; ENSMUSG00000028962.
DR   GeneID; 20535; -.
DR   KEGG; mmu:20535; -.
DR   UCSC; uc008wrm.1; mouse.
DR   CTD; 20535; -.
DR   MGI; MGI:109351; Slc4a2.
DR   HOGENOM; HBG355640; -.
DR   HOVERGEN; HBG004326; -.
DR   InParanoid; P13808; -.
DR   OrthoDB; EOG4WDDB2; -.
DR   PhylomeDB; P13808; -.
DR   ArrayExpress; P13808; -.
DR   Bgee; P13808; -.
DR   Genevestigator; P13808; -.
DR   GermOnline; ENSMUSG00000028962; Mus musculus.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015108; F:chloride transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
DR   InterPro; IPR001717; Anion_exchange.
DR   InterPro; IPR002978; Anion_exchange_2.
DR   InterPro; IPR018241; Anion_exchange_CS.
DR   InterPro; IPR011531; HCO3_transpt_C.
DR   InterPro; IPR013769; HCO3_transpt_cyt.
DR   InterPro; IPR003020; HCO3_transpt_euk.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   Gene3D; G3DSA:3.40.1100.10; HCO3_transpt_cyt; 1.
DR   PANTHER; PTHR11453:SF14; Anion_exhngr2; 1.
DR   PANTHER; PTHR11453; HCO3_transpt_euk; 1.
DR   Pfam; PF07565; Band_3_cyto; 1.
DR   Pfam; PF00955; HCO3_cotransp; 1.
DR   PRINTS; PR00165; ANIONEXCHNGR.
DR   PRINTS; PR01188; ANIONEXHNGR2.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   SUPFAM; SSF55804; PTrfase/Anion_transptr; 1.
DR   TIGRFAMs; TIGR00834; ae; 1.
DR   PROSITE; PS00219; ANION_EXCHANGER_1; 1.
DR   PROSITE; PS00220; ANION_EXCHANGER_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Anion exchange; Antiport; Glycoprotein;
KW   Ion transport; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1   1237       Anion exchange protein 2.
FT                                /FTId=PRO_0000079216.
FT   TOPO_DOM      1    703       Cytoplasmic (Potential).
FT   TRANSMEM    704    727       Helical; (Potential).
FT   TRANSMEM    733    770       Helical; (Potential).
FT   TRANSMEM    790    812       Helical; (Potential).
FT   TRANSMEM    822    843       Helical; (Potential).
FT   TOPO_DOM    844    896       Extracellular (Potential).
FT   TRANSMEM    897    914       Helical; (Potential).
FT   TOPO_DOM    915    929       Cytoplasmic (Potential).
FT   TRANSMEM    930    950       Helical; (Potential).
FT   TRANSMEM    984   1006       Helical; (Potential).
FT   TRANSMEM   1032   1053       Helical; (Potential).
FT   TRANSMEM   1087   1132       Helical; (Potential).
FT   TRANSMEM   1159   1195       Helical; (Potential).
FT   REGION      704   1237       Membrane (anion exchange).
FT   COMPBIAS      5    316       Pro-rich.
FT   COMPBIAS     73     87       His-rich.
FT   COMPBIAS    861    865       Poly-Ser.
FT   MOD_RES      72     72       Phosphotyrosine (By similarity).
FT   MOD_RES     112    112       Phosphoserine (By similarity).
FT   MOD_RES     131    131       Phosphoserine (By similarity).
FT   MOD_RES     144    144       Phosphoserine (By similarity).
FT   MOD_RES     170    170       Phosphoserine (By similarity).
FT   MOD_RES     172    172       Phosphoserine (By similarity).
FT   LIPID      1169   1169       S-palmitoyl cysteine (By similarity).
FT   CARBOHYD    855    855       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    866    866       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    878    878       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1    198       Missing (in isoform C1).
FT                                /FTId=VSP_000460.
FT   VAR_SEQ       1    166       Missing (in isoform C2).
FT                                /FTId=VSP_000459.
FT   VAR_SEQ       1     17       MSSAPRRPASGADSLHT -> MTQ (in isoform B1).
FT                                /FTId=VSP_000458.
FT   VAR_SEQ       1     17       MSSAPRRPASGADSLHT -> MDFLLRPQ (in isoform
FT                                B2).
FT                                /FTId=VSP_000457.
FT   VAR_SEQ     167    193       ERTSPSPPTQTPHQEAAPRASKGAQTG -> MPAFQEWKSG
FT                                GLREEAVFGAHGCSVCR (in isoform C2).
FT                                /FTId=VSP_000461.
FT   CONFLICT    205    205       A -> G (in Ref. 2; AAG23154/AAG23155/
FT                                AAG23156/AAG23158/AAG23157).
SQ   SEQUENCE   1237 AA;  136814 MW;  1A0782C0071782EE CRC64;
     MSSAPRRPAS GADSLHTPEP ESLSPGTPGF PEQEEDELRT LGVERFEEIL QEAGSRGGEE
     PGRSYGEEDF EYHRQSSHHI HHPLSTHLPP DARRRKTPQG PGRKPRRRPG ASPTGETPTI
     EEGEEDEEEA SEAEGFRAPP QQPSPATTPS AVQFFLQEDE GAERKPERTS PSPPTQTPHQ
     EAAPRASKGA QTGTLVEEMV AVASATAGGD DGGAAGRPLT KAQPGHRSYN LQERRRIGSM
     TGVEQALLPR VPTDESEAQT LATADLDLMK SHRFEDVPGV RRHLVRKNAK GSTQAAREGR
     EPGPTPRARP RAPHKPHEVF VELNELLLDK NQEPQWRETA RWIKFEEDVE EETERWGKPH
     VASLSFRSLL ELRRTLAHGA VLLDLDQQTL PGVAHQVVEQ MVISDQIKAE DRANVLRALL
     LKHSHPSDEK EFSFPRNISA GSLGSLLGHH HAQGTESDPH VTEPLIGGVP ETRLEVDRER
     ELPPPAPPAG ITRSKSKHEL KLLEKIPENA EATVVLVGCV EFLSRPTMAF VRLREAVELD
     AVLEVPVPVR FLFLLLGPSS ANMDYHEIGR SISTLMSDKQ FHEAAYLADE RDDLLTAINA
     FLDCSVVLPP SEVQGEELLR SVAHFQRQML KKREEQGRLL PPGAGLEPKS AQDKALLQMV
     EVAGAAEDDP LRRTGRPFGG LIRDVRRRYP HYLSDFRDAL DPQCLAAVIF IYFAALSPAI
     TFGGLLGEKT KDLIGVSELI MSTALQGVVF CLLGAQPLLV IGFSGPLLVF EEAFFSFCSS
     NELEYLVGRV WIGFWLVFLA LLMVALEGSF LVRFVSRFTQ EIFAFLISLI FIYETFYKLI
     KIFQEHPLHG CSGSNDSEAG SSSSSNMTWA TTILVPDNSS ASGQSGQEKP RGQPNTALLS
     LVLMAGTFFI AFFLRKFKNS RFFPGRIRRV IGDFGVPIAI LIMVLVDYSI EDTYTQKLSV
     PSGFSVTAPD KRGWVINPLG EKTPFPVWMM VASLLPAVLV FILIFMETQI TTLIISKKER
     MLQKGSGFHL DLLLIVAMGG ICALFGLPWL AAATVRSVTH ANALTVMSKA VAPGDKPKIQ
     EVKEQRVTGL LVALLVGLSM VIGDLLRQIP LAVLFGIFLY MGVTSLNGIQ FYERLHLLLM
     PPKHHPDVTY VKKVRTMRMH LFTALQLLCL ALLWAVMSTA ASLAFPFILI LTVPLRMVVL
     TRIFTEREMK CLDANEAEPV FDECEGVDEY NEMPMPV
//
ID   DNMT1_MOUSE             Reviewed;        1620 AA.
AC   P13864; P97413; Q80ZU3; Q9CSC6; Q9QXX6;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2002, sequence version 5.
DT   08-MAR-2011, entry version 134.
DE   RecName: Full=DNA (cytosine-5)-methyltransferase 1;
DE            Short=Dnmt1;
DE            Short=Met-1;
DE            EC=2.1.1.37;
DE   AltName: Full=DNA methyltransferase MmuI;
DE            Short=DNA MTase MmuI;
DE            Short=M.MmuI;
DE   AltName: Full=MCMT;
GN   Name=Dnmt1; Synonyms=Dnmt, Met1, Uim;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=89094873; PubMed=3210246; DOI=10.1016/0022-2836(88)90122-2;
RA   Bestor T.H., Laudano A., Mattaliano R., Ingram V.;
RT   "Cloning and sequencing of a cDNA encoding DNA methyltransferase of
RT   mouse cells. The carboxyl-terminal domain of the mammalian enzymes is
RT   related to bacterial restriction methyltransferases.";
RL   J. Mol. Biol. 203:971-983(1988).
RN   [2]
RP   SEQUENCE REVISION TO N-TERMINUS.
RC   TISSUE=Embryo;
RX   MEDLINE=97094871; PubMed=8940105; DOI=10.1074/jbc.271.49.31092;
RA   Yoder J.A., Yen R.-W.C., Vertino P.M., Bestor T.H., Baylin S.B.;
RT   "New 5' regions of the murine and human genes for DNA (cytosine-5)-
RT   methyltransferase.";
RL   J. Biol. Chem. 271:31092-31097(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Skeletal muscle;
RX   MEDLINE=20515133; PubMed=11063128;
RA   Aguirre-Arteta A.M., Grunewald I., Cardoso M.C., Leonhardt H.;
RT   "Expression of an alternative Dnmt1 isoform during muscle
RT   differentiation.";
RL   Cell Growth Differ. 11:551-559(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6;
RX   MEDLINE=20181859; PubMed=10715201; DOI=10.1006/jmbi.2000.3588;
RA   Margot J.B., Aguirre-Arteta A.M., Di Giacco B.V., Pradhan S.,
RA   Roberts R.J., Cardoso M.C., Leonhardt H.;
RT   "Structure and function of the mouse DNA methyltransferase gene: Dnmt1
RT   shows a tripartite structure.";
RL   J. Mol. Biol. 297:293-300(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-27 AND 119-1619
RP   (ISOFORMS 1 AND 2).
RX   MEDLINE=98119799; PubMed=9449671;
RA   Mertineit C., Yoder J.A., Taketo T., Laird D.W., Trasler J.M.,
RA   Bestor T.H.;
RT   "Sex-specific exons control DNA methyltransferase in mammalian germ
RT   cells.";
RL   Development 125:889-897(1998).
RN   [7]
RP   NUCLEOTIDE SEQUENCE OF 1-144 (ISOFORMS 1 AND 2), AND PROTEIN SEQUENCE
RP   OF 3-6.
RC   STRAIN=129/Sv, and BALB/c; TISSUE=Embryonic stem cell;
RX   MEDLINE=99047652; PubMed=9830015; DOI=10.1074/jbc.273.49.32725;
RA   Gaudet F., Talbot D., Leonhardt H., Jaenisch R.;
RT   "A short DNA methyltransferase isoform restores methylation in vivo.";
RL   J. Biol. Chem. 273:32725-32729(1998).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-119 (ISOFORM 1).
RC   STRAIN=129/Sv; TISSUE=Embryonic stem cell, and Kidney;
RX   MEDLINE=97075093; PubMed=8917520; DOI=10.1073/pnas.93.23.12920;
RA   Tucker K.L., Talbot D., Lee M.A., Leonhardt H., Jaenisch R.;
RT   "Complementation of methylation deficiency in embryonic stem cells by
RT   a DNA methyltransferase minigene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:12920-12925(1996).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-272 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [10]
RP   PROTEIN SEQUENCE OF 1108-1154, AND ENZYME REGULATION.
RX   MEDLINE=92331613; PubMed=1628623;
RA   Bestor T.H.;
RT   "Activation of mammalian DNA methyltransferase by cleavage of a Zn
RT   binding regulatory domain.";
RL   EMBO J. 11:2611-2617(1992).
RN   [11]
RP   PHOSPHORYLATION AT SER-515, AND MASS SPECTROMETRY.
RC   TISSUE=Erythroleukemia;
RX   MEDLINE=97362284; PubMed=9211941; DOI=10.1074/jbc.272.28.17851;
RA   Glickman J.F., Pavlovich J.G., Reich N.O.;
RT   "Peptide mapping of the murine DNA methyltransferase reveals a major
RT   phosphorylation site and the start of translation.";
RL   J. Biol. Chem. 272:17851-17857(1997).
RN   [12]
RP   INTERACTION WITH HDAC1.
RX   MEDLINE=20082816; PubMed=10615135; DOI=10.1038/71750;
RA   Fuks F., Burgers W.A., Brehm A., Hughes-Davies L., Kouzarides T.;
RT   "DNA methyltransferase Dnmt1 associates with histone deacetylase
RT   activity.";
RL   Nat. Genet. 24:88-91(2000).
RN   [13]
RP   INTERACTION WITH HDAC2 AND DMAP1.
RX   MEDLINE=20347709; PubMed=10888872; DOI=10.1038/77023;
RA   Rountree M.R., Bachman K.E., Baylin S.B.;
RT   "DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at
RT   replication foci.";
RL   Nat. Genet. 25:269-277(2000).
RN   [14]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   MEDLINE=21185930; PubMed=11290321; DOI=10.1016/S0092-8674(01)00280-X;
RA   Howell C.Y., Bestor T.H., Ding F., Latham K.E., Mertineit C.,
RA   Trasler J.M., Chaillet J.R.;
RT   "Genomic imprinting disrupted by a maternal effect mutation in the
RT   Dnmt1 gene.";
RL   Cell 104:829-838(2001).
RN   [15]
RP   ALLOSTERIC REGULATION.
RX   MEDLINE=21293215; PubMed=11399088; DOI=10.1006/jmbi.2001.4709;
RA   Fatemi M., Hermann A., Pradhan S., Jeltsch A.;
RT   "The activity of the murine DNA methyltransferase Dnmt1 is controlled
RT   by interaction of the catalytic domain with the N-terminal part of the
RT   enzyme leading to an allosteric activation of the enzyme after binding
RT   to methylated DNA.";
RL   J. Mol. Biol. 309:1189-1199(2001).
RN   [16]
RP   FUNCTION.
RX   PubMed=15550930; DOI=10.1038/sj.embor.7400295;
RA   Easwaran H.P., Schermelleh L., Leonhardt H., Cardoso M.C.;
RT   "Replication-independent chromatin loading of Dnmt1 during G2 and M
RT   phases.";
RL   EMBO Rep. 5:1181-1186(2004).
RN   [17]
RP   INTERACTION WITH BAZ2A.
RX   PubMed=16085498; DOI=10.1016/j.cub.2005.06.057;
RA   Zhou Y., Grummt I.;
RT   "The PHD finger/bromodomain of NoRC interacts with acetylated histone
RT   H4K16 and is sufficient for rDNA silencing.";
RL   Curr. Biol. 15:1434-1438(2005).
RN   [18]
RP   INTERACTION WITH THE PRC2 COMPLEX.
RX   PubMed=16357870; DOI=10.1038/nature04431;
RA   Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C.,
RA   Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M.,
RA   Esteller M., Di Croce L., de Launoit Y., Fuks F.;
RT   "The Polycomb group protein EZH2 directly controls DNA methylation.";
RL   Nature 439:871-874(2006).
RN   [19]
RP   ERRATUM.
RA   Vire E., Brenner C., Deplus R., Blanchon L., Fraga M., Didelot C.,
RA   Morey L., Van Eynde A., Bernard D., Vanderwinden J.-M., Bollen M.,
RA   Esteller M., Di Croce L., de Launoit Y., Fuks F.;
RL   Nature 446:824-824(2006).
RN   [20]
RP   PHOSPHORYLATION AT SER-515, AND MUTAGENESIS OF SER-515.
RX   PubMed=17965600;
RA   Goyal R., Rathert P., Laser H., Gowher H., Jeltsch A.;
RT   "Phosphorylation of serine-515 activates the mammalian maintenance
RT   methyltransferase Dnmt1.";
RL   Epigenetics 2:155-160(2007).
RN   [21]
RP   FUNCTION, AND MUTAGENESIS OF GLN-162; PHE-169 AND CYS-1229.
RX   PubMed=17576694; DOI=10.1093/nar/gkm432;
RA   Schermelleh L., Haemmer A., Spada F., Roesing N., Meilinger D.,
RA   Rothbauer U., Cardoso M.C., Leonhardt H.;
RT   "Dynamics of Dnmt1 interaction with the replication machinery and its
RT   role in postreplicative maintenance of DNA methylation.";
RL   Nucleic Acids Res. 35:4301-4312(2007).
RN   [22]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Methylates CpG residues. Preferentially methylates
CC       hemimethylated DNA. Associates with DNA replication sites in S
CC       phase maintaining the methylation pattern in the newly synthesized
CC       strand, that is essential for epigenetic inheritance. Associates
CC       with chromatin during G2 and M phases to maintain DNA methylation
CC       independently of replication. It is responsible for maintaining
CC       methylation patterns established in development. DNA methylation
CC       is coordinated with methylation of histones. Mediates
CC       transcriptional repression by direct binding to HDAC2. In
CC       association with DNMT3B and via the recruitment of CTCFL/BORIS,
CC       involved in activation of BAG1 gene expression by modulating
CC       dimethylation of promoter histone H3 at H3K4 and H3K9.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L-
CC       homocysteine + DNA containing 5-methylcytosine.
CC   -!- ENZYME REGULATION: Allosterically regulated. The binding of 5-
CC       methylcytosine-containing DNA to the N-terminal parts of DNMT1
CC       causes an allosteric activation of the catalytic domain by a
CC       direct interaction of its Zn-binding domain with the catalytic
CC       domain.
CC   -!- SUBUNIT: Homodimer. Interacts with HDAC1 and with PCNA. Binds MBD2
CC       and MBD3. Component of complexes containing SUV39H1. Interacts
CC       with DNMT3A and DNMT3B (By similarity). Forms a complex with DMAP1
CC       and HDAC2, with direct interaction. Interacts with the PRC2/EED-
CC       EZH2 complex. Interacts with UBC9 (By similarity). Interacts with
CC       BAZ2A/TIP5.
CC   -!- INTERACTION:
CC       O09106:Hdac1; NbExp=2; IntAct=EBI-301927, EBI-301912;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=It is nucleoplasmic
CC       through most of the cell cycle and associates with replication
CC       foci during S-phase. In germ cells, spermatogonia, preleptotene
CC       and leptotene spermatocytes all express high levels of nuclear
CC       protein, while the protein is not detected in pachytene
CC       spermatocytes, despite the fact they expressed high levels of
CC       mRNA. In females, the protein is not detected in non-growing
CC       oocytes, in contrast to the growing oocytes. During the growing,
CC       the protein is no longer detectable in nuclei but accumulates to
CC       very high levels first throughout the cytoplasm. At the time of
CC       ovulation, all the protein is cytoplasmic and is actively
CC       associated with the oocyte cortex. After fecondation, in the
CC       preimplantation embryo, the protein remains cytoplasmic and after
CC       implantation, it is exclusively nuclear in all tissue types.
CC       Isoform 2 is sequestered in the cytoplasm of maturing oocytes and
CC       of preimplantation embryos, except for the 8-cell stage, while
CC       isoform 1 is exclusively nuclear.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Long;
CC         IsoId=P13864-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short;
CC         IsoId=P13864-2; Sequence=VSP_005619;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is expressed in embryonic stem cells
CC       and in somatic tissues. Isoform 2 is expressed in oocytes,
CC       preimplantation embryos, testis and in skeletal muscle during
CC       myogenesis.
CC   -!- DEVELOPMENTAL STAGE: In germ cells, it is present at high levels
CC       in spermatogonia and spermatocytes until the pachytene stage,
CC       where it falls to undetectable levels. The transient drop at the
CC       pachytene stage coincides with the disappearance of the 5.2 kb
CC       mRNA and the accumulation of a larger 6.0 kb mRNA. Oocytes
CC       accumulate very large amounts of Dnmt1 protein during the growth
CC       phase.
CC   -!- DOMAIN: The N-terminal part is required for homodimerization and
CC       acts as a regulatory domain.
CC   -!- PTM: Sumoylated (By similarity).
CC   -!- MISCELLANEOUS: There are three 5' exons, one specific to the
CC       oocyte (1c), one specific to the pachytene spermatocyte and also
CC       found in skeletal muscle (1b) and one found in somatic cells (1a).
CC       Three differents mRNAs can be produced which give rise to two
CC       different translation products: isoform 1 (mRNAs-1a) and isoform 2
CC       (mRNA-1b or -1c). Association of DNMT1 with the replication
CC       machinery is not strictly required for maintaining global
CC       methylation but still enhances methylation efficiency by 2-fold.
CC       Pre-existing cytosine methylation at CpG and non-CpG sites
CC       enhances methylation activity.
CC   -!- SIMILARITY: Belongs to the C5-methyltransferase family.
CC   -!- SIMILARITY: Contains 2 BAH domains.
CC   -!- SIMILARITY: Contains 1 CXXC-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC52900.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; X14805; CAA32910.1; -; mRNA.
DR   EMBL; AF175432; AAF97695.1; -; mRNA.
DR   EMBL; AF162282; AAF19352.1; -; mRNA.
DR   EMBL; AF175431; AAF60965.1; -; Genomic_DNA.
DR   EMBL; AF175412; AAF60965.1; JOINED; Genomic_DNA.
DR   EMBL; AF175413; AAF60965.1; JOINED; Genomic_DNA.
DR   EMBL; AF175414; AAF60965.1; JOINED; Genomic_DNA.
DR   EMBL; AF244089; AAF60965.1; JOINED; Genomic_DNA.
DR   EMBL; AF244090; AAF60965.1; JOINED; Genomic_DNA.
DR   EMBL; AF175416; AAF60965.1; JOINED; Genomic_DNA.
DR   EMBL; AF175417; AAF60965.1; JOINED; Genomic_DNA.
DR   EMBL; AF175418; AAF60965.1; JOINED; Genomic_DNA.
DR   EMBL; AF175419; AAF60965.1; JOINED; Genomic_DNA.
DR   EMBL; AF175420; AAF60965.1; JOINED; Genomic_DNA.
DR   EMBL; AF175421; AAF60965.1; JOINED; Genomic_DNA.
DR   EMBL; AF175422; AAF60965.1; JOINED; Genomic_DNA.
DR   EMBL; AF175423; AAF60965.1; JOINED; Genomic_DNA.
DR   EMBL; AF234317; AAF60965.1; JOINED; Genomic_DNA.
DR   EMBL; AF175424; AAF60965.1; JOINED; Genomic_DNA.
DR   EMBL; AF175425; AAF60965.1; JOINED; Genomic_DNA.
DR   EMBL; AF175426; AAF60965.1; JOINED; Genomic_DNA.
DR   EMBL; AF234318; AAF60965.1; JOINED; Genomic_DNA.
DR   EMBL; AF175427; AAF60965.1; JOINED; Genomic_DNA.
DR   EMBL; AF175428; AAF60965.1; JOINED; Genomic_DNA.
DR   EMBL; AF175429; AAF60965.1; JOINED; Genomic_DNA.
DR   EMBL; AF175430; AAF60965.1; JOINED; Genomic_DNA.
DR   EMBL; BC048148; AAH48148.2; -; mRNA.
DR   EMBL; AF036007; AAC40061.1; -; mRNA.
DR   EMBL; AF036008; AAC53551.1; -; Genomic_DNA.
DR   EMBL; U70051; AAC52900.1; ALT_INIT; mRNA.
DR   EMBL; AK013247; BAB28743.1; -; mRNA.
DR   IPI; IPI00469323; -.
DR   IPI; IPI00474974; -.
DR   PIR; S01845; S01845.
DR   RefSeq; NP_001186362.1; NM_001199433.1.
DR   UniGene; Mm.128580; -.
DR   PDB; 3PT6; X-ray; 3.00 A; A/B=650-1602.
DR   PDB; 3PT9; X-ray; 2.50 A; A=731-1602.
DR   PDBsum; 3PT6; -.
DR   PDBsum; 3PT9; -.
DR   ProteinModelPortal; P13864; -.
DR   SMR; P13864; 357-603, 648-699, 759-883, 1139-1599.
DR   IntAct; P13864; 3.
DR   STRING; P13864; -.
DR   REBASE; 2844; M.MmuDnmt1.
DR   PhosphoSite; P13864; -.
DR   PRIDE; P13864; -.
DR   Ensembl; ENSMUST00000004202; ENSMUSP00000004202; ENSMUSG00000004099.
DR   GeneID; 13433; -.
DR   KEGG; mmu:13433; -.
DR   UCSC; uc009ojo.1; mouse.
DR   UCSC; uc009ojq.1; mouse.
DR   CTD; 13433; -.
DR   MGI; MGI:94912; Dnmt1.
DR   eggNOG; roNOG11123; -.
DR   HOVERGEN; HBG051384; -.
DR   InParanoid; P13864; -.
DR   OrthoDB; EOG4T1HKN; -.
DR   PhylomeDB; P13864; -.
DR   BRENDA; 2.1.1.37; 244.
DR   ArrayExpress; P13864; -.
DR   Bgee; P13864; -.
DR   CleanEx; MM_DNMT1; -.
DR   Genevestigator; P13864; -.
DR   GermOnline; ENSMUSG00000004099; Mus musculus.
DR   GO; GO:0005721; C:centromeric heterochromatin; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005657; C:replication fork; IDA:MGI.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0008134; F:transcription factor binding; IEA:InterPro.
DR   GO; GO:0016564; F:transcription repressor activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IDA:MGI.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0016458; P:gene silencing; IDA:UniProtKB.
DR   GO; GO:0010216; P:maintenance of DNA methylation; IMP:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:MGI.
DR   GO; GO:0042127; P:regulation of cell proliferation; IGI:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR001025; BAH_dom.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR022702; Cytosine_MeTrfase1_RFD.
DR   InterPro; IPR010506; DMAP1-bd.
DR   InterPro; IPR017198; DNA_C5-MeTrfase_1_euk.
DR   InterPro; IPR002857; Znf_CXXC.
DR   PANTHER; PTHR10629; C5_DNA_meth; 1.
DR   Pfam; PF01426; BAH; 2.
DR   Pfam; PF06464; DMAP_binding; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   Pfam; PF12047; DNMT1-RFD; 1.
DR   Pfam; PF02008; zf-CXXC; 1.
DR   PIRSF; PIRSF037404; DNMT1; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SMART; SM00439; BAH; 2.
DR   TIGRFAMs; TIGR00675; dcm; 1.
DR   PROSITE; PS51038; BAH; 2.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS00095; C5_MTASE_2; 1.
DR   PROSITE; PS51058; ZF_CXXC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Allosteric enzyme;
KW   Alternative splicing; Chromatin regulator; Cytoplasm;
KW   Direct protein sequencing; DNA-binding; Metal-binding; Methylation;
KW   Methyltransferase; Nucleus; Phosphoprotein; Repeat; Repressor;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1   1620       DNA (cytosine-5)-methyltransferase 1.
FT                                /FTId=PRO_0000088035.
FT   DOMAIN      758    884       BAH 1.
FT   DOMAIN      976   1103       BAH 2.
FT   REPEAT     1112   1113       1.
FT   REPEAT     1114   1115       2.
FT   REPEAT     1116   1117       3.
FT   REPEAT     1118   1119       4.
FT   REPEAT     1120   1121       5.
FT   REPEAT     1122   1123       6.
FT   REPEAT     1124   1125       7; approximate.
FT   ZN_FING     649    695       CXXC-type.
FT   REGION        1    343       Interaction with the PRC2/EED-EZH2
FT                                complex.
FT   REGION        1    145       Interaction with DNMT3A (By similarity).
FT   REGION        1    120       Interaction with DMAP1.
FT   REGION      147    217       Interaction with DNMT3B (By similarity).
FT   REGION      161    172       Interaction with PCNA.
FT   REGION      305    609       Interaction with the PRC2/EED-EZH2
FT                                complex.
FT   REGION      328    556       DNA replication foci-targeting sequence
FT                                (By similarity).
FT   REGION      696    813       Interaction with HDAC1.
FT   REGION     1112   1125       7 X 2 AA tandem repeats of K-G.
FT   REGION     1124   1620       Interaction with the PRC2/EED-EZH2
FT                                complex.
FT   REGION     1142   1620       Catalytic.
FT   MOTIF       175    202       Nuclear localization signal (Potential).
FT   ACT_SITE   1229   1229
FT   METAL       359    359       Zinc (By similarity).
FT   METAL       362    362       Zinc (By similarity).
FT   METAL       420    420       Zinc (By similarity).
FT   METAL       424    424       Zinc (By similarity).
FT   MOD_RES      70     70       N6,N6-dimethyllysine; by EHMT2 (By
FT                                similarity).
FT   MOD_RES     150    150       Phosphoserine (By similarity).
FT   MOD_RES     152    152       Phosphoserine (By similarity).
FT   MOD_RES     171    171       N6-acetyllysine (By similarity).
FT   MOD_RES     285    285       Phosphoserine.
FT   MOD_RES     515    515       Phosphoserine.
FT   MOD_RES     717    717       Phosphoserine (By similarity).
FT   MOD_RES     735    735       Phosphoserine (By similarity).
FT   MOD_RES     958    958       Phosphoserine (By similarity).
FT   MOD_RES     973    973       Phosphotyrosine (By similarity).
FT   MOD_RES    1108   1108       Phosphoserine (By similarity).
FT   MOD_RES    1116   1116       N6-acetyllysine (By similarity).
FT   MOD_RES    1118   1118       N6-acetyllysine (By similarity).
FT   MOD_RES    1120   1120       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1    118       Missing (in isoform 2).
FT                                /FTId=VSP_005619.
FT   MUTAGEN     162    162       Q->E: Abolishes interaction with PCNA. No
FT                                effect on activity.
FT   MUTAGEN     169    169       F->S: Abolishes interaction with PCNA. No
FT                                effect on activity.
FT   MUTAGEN     515    515       S->A: Loss of activity. No effect on DNA-
FT                                binding capacity.
FT   MUTAGEN     515    515       S->E: Slightly reduces activity.
FT   MUTAGEN    1229   1229       C->W: Loss of activity.
FT   CONFLICT    146    147       SV -> F (in Ref. 1; CAA32910 and 6;
FT                                AAC40061).
FT   CONFLICT    299    309       AEPEQVAPETP -> VRARAGSSRDS (in Ref. 1;
FT                                CAA32910 and 6; AAC40061).
FT   CONFLICT    936    936       V -> C (in Ref. 1; CAA32910 and 6;
FT                                AAC40061).
FT   CONFLICT    947    947       P -> R (in Ref. 1; CAA32910 and 6;
FT                                AAC40061).
FT   CONFLICT    969    976       NETLYPEH -> KENPVPRDT (in Ref. 1;
FT                                CAA32910 and 6; AAC40061).
FT   CONFLICT    987    987       S -> R (in Ref. 1; CAA32910 and 6;
FT                                AAC40061).
FT   CONFLICT   1046   1046       Y -> C (in Ref. 1; CAA32910 and 6;
FT                                AAC40061).
FT   CONFLICT   1068   1068       G -> R (in Ref. 1; CAA32910 and 6;
FT                                AAC40061).
FT   CONFLICT   1429   1429       R -> P (in Ref. 1; CAA32910 and 6;
FT                                AAC40061).
FT   CONFLICT   1456   1456       H -> D (in Ref. 1; CAA32910 and 6;
FT                                AAC40061).
SQ   SEQUENCE   1620 AA;  183189 MW;  4F9A98CEAF09F037 CRC64;
     MPARTAPARV PALASPAGSL PDHVRRRLKD LERDGLTEKE CVREKLNLLH EFLQTEIKSQ
     LCDLETKLHK EELSEEGYLA KVKSLLNKDL SLENGTHTLT QKANGCPANG SRPTWRAEMA
     DSNRSPRSRP KPRGPRRSKS DSDTLSVETS PSSVATRRTT RQTTITAHFT KGPTKRKPKE
     ESEEGNSAES AAEERDQDKK RRVVDTESGA AAAVEKLEEV TAGTQLGPEE PCEQEDDNRS
     LRRHTRELSL RRKSKEDPDR EARPETHLDE DEDGKKDKRS SRPRSQPRDP AAKRRPKEAE
     PEQVAPETPE DRDEDEREEK RRKTTRKKLE SHTVPVQSRS ERKAAQSKSV IPKINSPKCP
     ECGQHLDDPN LKYQQHPEDA VDEPQMLTSE KLSIYDSTST WFDTYEDSPM HRFTSFSVYC
     SRGHLCPVDT GLIEKNVELY FSGCAKAIHD ENPSMEGGIN GKNLGPINQW WLSGFDGGEK
     VLIGFSTAFA EYILMEPSKE YEPIFGLMQE KIYISKIVVE FLQNNPDAVY EDLINKIETT
     VPPSTINVNR FTEDSLLRHA QFVVSQVESY DEAKDDDETP IFLSPCMRAL IHLAGVSLGQ
     RRATRRVMGA TKEKDKAPTK ATTTKLVYQI FDTFFSEQIE KYDKEDKENA MKRRRCGVCE
     VCQQPECGKC KACKDMVKFG GTGRSKQACL KRRCPNLAVK EADDDEEADD DVSEMPSPKK
     LHQGKKKKQN KDRISWLGQP MKIEENRTYY QKVSIDEEML EVGDCVSVIP DDSSKPLYLA
     RVTALWEDKN GQMMFHAHWF CAGTDTVLGA TSDPLELFLV GECENMQLSY IHSKVKVIYK
     APSENWAMEG GTDPETTLPG AEDGKTYFFQ LWYNQEYARF ESPPKTQPTE DNKHKFCLSC
     IRLAELRQKE MPKVLEQIEE VDGRVYCSSI TKNGVVYRLG DSVYLPPEAF TFNIKVASPV
     KRPKKDPVNE TLYPEHYRKY SDYIKGSNLD APEPYRIGRI KEIHCGKKKG KVNEADIKLR
     LYKFYRPENT HRSYNGSYHT DINMLYWSDE EAVVNFSDVQ GRCTVEYGED LLESIQDYSQ
     GGPDRFYFLE AYNSKTKNFE DPPNHARSPG NKGKGKGKGK GKGKHQVSEP KEPEAAIKLP
     KLRTLDVFSG CGGLSEGFHQ AGISETLWAI EMWDPAAQAF RLNNPGTTVF TEDCNVLLKL
     VMAGEVTNSL GQRLPQKGDV EMLCGGPPCQ GFSGMNRFNS RTYSKFKNSL VVSFLSYCDY
     YRPRFFLLEN VRNFVSYRRS MVLKLTLRCL VRMGYQCTFG VLQAGQYGVA QTRRRAIILA
     AAPGEKLPLF PEPLHVFAPR ACQLSVVVDD KKFVSNITRL SSGPFRTITV RDTMSDLPEI
     QNGASNSEIP YNGEPLSWFQ RQLRGSHYQP ILRDHICKDM SPLVAARMRH IPLFPGSDWR
     DLPNIQVRLG DGVIAHKLQY TFHDVKNGYS STGALRGVCS CAEGKACDPE SRQFSTLIPW
     CLPHTGNRHN HWAGLYGRLE WDGFFSTTVT NPEPMGKQGR VLHPEQHRVV SVRECARSQG
     FPDSYRFFGN ILDRHRQVGN AVPPPLAKAI GLEIKLCLLS SARESASAAV KAKEEAATKD
//
ID   GTR4_MOUSE              Reviewed;         509 AA.
AC   P14142; Q9JJN9;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2001, sequence version 2.
DT   08-MAR-2011, entry version 116.
DE   RecName: Full=Solute carrier family 2, facilitated glucose transporter member 4;
DE   AltName: Full=GT2;
DE   AltName: Full=Glucose transporter type 4, insulin-responsive;
DE            Short=GLUT-4;
GN   Name=Slc2a4; Synonyms=Glut-4, Glut4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=89240694; PubMed=2654938; DOI=10.1073/pnas.86.9.3150;
RA   Kaestner K.H., Christy R.J., McLenithan J.C., Braiterman L.T.,
RA   Cornelius P., Pekala P.H., Lane M.D.;
RT   "Sequence, tissue distribution, and differential expression of mRNA
RT   for a putative insulin-responsive glucose transporter in mouse 3T3-L1
RT   adipocytes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:3150-3154(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C3H, and NSY; TISSUE=Muscle;
RX   MEDLINE=20407000; PubMed=10952468; DOI=10.1007/s001250051472;
RA   Ueda H., Ikegami H., Kawaguchi Y., Fujisawa T., Nojima K., Babaya N.,
RA   Yamada K., Shibata M., Yamato E., Ogihara T.;
RT   "Age-dependent changes in phenotypes and candidate gene analysis in a
RT   polygenic animal model of type II diabetes; NSY mouse.";
RL   Diabetologia 43:932-938(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   EFFECT OF TBC1D4 ON GLUT4 TRANSLOCATION.
RX   MEDLINE=22590501; PubMed=12637568; DOI=10.1074/jbc.C300063200;
RA   Sano H., Kane S., Sano E., Miinea C.P., Asara J.M., Lane W.S.,
RA   Garner C.W., Lienhard G.E.;
RT   "Insulin-stimulated phosphorylation of a Rab GTPase-activating protein
RT   regulates GLUT4 translocation.";
RL   J. Biol. Chem. 278:14599-14602(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-57, AND MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Insulin-regulated facilitative glucose transporter.
CC   -!- SUBUNIT: Binds to DAXX. Interacts via its N-terminus with SRFBP1
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endomembrane system; Multi-pass membrane
CC       protein (By similarity). Cytoplasm, perinuclear region (By
CC       similarity). Note=Localizes primarily to the perinuclear region,
CC       undergoing continued recycling to the plasma membrane where it is
CC       rapidly reinternalized. The dileucine internalization motif is
CC       critical for intracellular sequestration (By similarity).
CC   -!- TISSUE SPECIFICITY: Skeletal and cardiac muscles; brown and white
CC       fat.
CC   -!- DISEASE: Note=Defects in Slc2a4 may be the cause of certain post-
CC       receptor defects in non-insulin-dependent diabetes mellitus
CC       (NIDDM).
CC   -!- MISCELLANEOUS: Insulin-stimulated phosphorylation of TBC1D4 is
CC       required for GLUT4 translocation.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC       transporter (TC 2.A.1.1) family. Glucose transporter subfamily.
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DR   EMBL; M23383; AAA37753.1; -; mRNA.
DR   EMBL; AB008453; BAB03251.1; -; mRNA.
DR   EMBL; BC014282; AAH14282.1; -; mRNA.
DR   IPI; IPI00762242; -.
DR   PIR; B30310; B30310.
DR   RefSeq; NP_033230.2; NM_009204.2.
DR   UniGene; Mm.10661; -.
DR   ProteinModelPortal; P14142; -.
DR   DIP; DIP-42440N; -.
DR   MINT; MINT-1342290; -.
DR   STRING; P14142; -.
DR   PhosphoSite; P14142; -.
DR   PRIDE; P14142; -.
DR   Ensembl; ENSMUST00000018710; ENSMUSP00000018710; ENSMUSG00000018566.
DR   GeneID; 20528; -.
DR   KEGG; mmu:20528; -.
DR   CTD; 20528; -.
DR   MGI; MGI:95758; Slc2a4.
DR   eggNOG; roNOG11437; -.
DR   HOGENOM; HBG744444; -.
DR   HOVERGEN; HBG014816; -.
DR   InParanoid; P14142; -.
DR   OrthoDB; EOG4BG8W5; -.
DR   PhylomeDB; P14142; -.
DR   ArrayExpress; P14142; -.
DR   Bgee; P14142; -.
DR   Genevestigator; P14142; -.
DR   GermOnline; ENSMUSG00000018566; Mus musculus.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:MGI.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:MGI.
DR   GO; GO:0000299; C:integral to membrane of membrane fraction; IDA:MGI.
DR   GO; GO:0005887; C:integral to plasma membrane; IDA:MGI.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR   GO; GO:0030140; C:trans-Golgi network transport vesicle; IDA:MGI.
DR   GO; GO:0005360; F:insulin-responsive hydrogen:glucose symporter activity; TAS:MGI.
DR   GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
DR   InterPro; IPR002441; Glc_transpt_4.
DR   InterPro; IPR020846; Major_facilitator_SF.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   InterPro; IPR005828; Sub_transporter.
DR   InterPro; IPR003663; Sugar/inositol_transpt.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   PRINTS; PR01193; GLUCTRSPORT4.
DR   PRINTS; PR00171; SUGRTRNSPORT.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
DR   TIGRFAMs; TIGR00879; SP; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR   PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Diabetes mellitus; Glycoprotein; Membrane; Phosphoprotein;
KW   Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    509       Solute carrier family 2, facilitated
FT                                glucose transporter member 4.
FT                                /FTId=PRO_0000050364.
FT   TOPO_DOM      1     23       Cytoplasmic (Potential).
FT   TRANSMEM     24     44       Helical; Name=1; (Potential).
FT   TOPO_DOM     45     80       Extracellular (Potential).
FT   TRANSMEM     81    101       Helical; Name=2; (Potential).
FT   TOPO_DOM    102    110       Cytoplasmic (Potential).
FT   TRANSMEM    111    131       Helical; Name=3; (Potential).
FT   TOPO_DOM    132    141       Extracellular (Potential).
FT   TRANSMEM    142    162       Helical; Name=4; (Potential).
FT   TOPO_DOM    163    170       Cytoplasmic (Potential).
FT   TRANSMEM    171    191       Helical; Name=5; (Potential).
FT   TOPO_DOM    192    200       Extracellular (Potential).
FT   TRANSMEM    201    221       Helical; Name=6; (Potential).
FT   TOPO_DOM    222    286       Cytoplasmic (Potential).
FT   TRANSMEM    287    307       Helical; Name=7; (Potential).
FT   TOPO_DOM    308    322       Extracellular (Potential).
FT   TRANSMEM    323    343       Helical; Name=8; (Potential).
FT   TOPO_DOM    344    352       Cytoplasmic (Potential).
FT   TRANSMEM    353    373       Helical; Name=9; (Potential).
FT   TOPO_DOM    374    384       Extracellular (Potential).
FT   TRANSMEM    385    405       Helical; Name=10; (Potential).
FT   TOPO_DOM    406    416       Cytoplasmic (Potential).
FT   TRANSMEM    417    437       Helical; Name=11; (Potential).
FT   TOPO_DOM    438    444       Extracellular (Potential).
FT   TRANSMEM    445    465       Helical; Name=12; (Potential).
FT   TOPO_DOM    466    508       Cytoplasmic (Potential).
FT   REGION        7     13       SRFBP1-binding (By similarity).
FT   REGION      294    296       Defines substrate specificity (By
FT                                similarity).
FT   MOTIF       489    490       Dileucine internalization motif
FT                                (Potential).
FT   MOD_RES     488    488       Phosphoserine.
FT   CARBOHYD     57     57       N-linked (GlcNAc...).
FT   CONFLICT     11     11       D -> DVK (in Ref. 1; AAA37753).
FT   CONFLICT    132    132       V -> A (in Ref. 2; BAB03251).
FT   CONFLICT    177    177       Q -> R (in Ref. 1; AAA37753).
FT   CONFLICT    246    246       R -> P (in Ref. 1; AAA37753).
FT   CONFLICT    406    406       Missing (in Ref. 1; AAA37753).
FT   CONFLICT    444    444       A -> R (in Ref. 1; AAA37753).
SQ   SEQUENCE   509 AA;  54783 MW;  6D260D7C45EB889D CRC64;
     MPSGFQQIGS DDGEPPRQRV TGTLVLAVFS AVLGSLQFGY NIGVINAPQK VIEQSYNATW
     LGRQGPGGPD SIPQGTLTTL WALSVAIFSV GGMISSFLIG IISQWLGRKR AMLANNVLAV
     LGGALMGLAN AVASYEILIL GRFLIGAYSG LTSGLVPMYV GEIAPTHLRG ALGTLNQLAI
     VIGILVAQVL GLESMLGTAT LWPLLLALTV LPALLQLILL PFCPESPRYL YIIRNLEGPA
     RKSLKRLTGW ADVSDALAEL KDEKRKLERE RPMSLLQLLG SRTHRQPLII AVVLQLSQQL
     SGINAVFYYS TSIFESAGVG QPAYATIGAG VVNTVFTLVS VLLVERAGRR TLHLLGLAGM
     CGCAILMTVA LLLLERVPAM SYVSIVAIFG FVAFFEIGPG PIPWFIVAEL FSQGPRPAAM
     AVAGFSNWTC NFIVGMGFQY VADAMGPYVF LLFAVLLLGF FIFTFLKVPE TRGRTFDQIS
     AAFRRTPSLL EQEVKPSTEL EYLGPDEND
//
ID   MDHC_MOUSE              Reviewed;         334 AA.
AC   P14152; Q3TP22; Q80Y13; Q9DB45;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 114.
DE   RecName: Full=Malate dehydrogenase, cytoplasmic;
DE            EC=1.1.1.37;
DE   AltName: Full=Cytosolic malate dehydrogenase;
GN   Name=Mdh1; Synonyms=Mor2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=88033094; PubMed=3312200;
RA   Joh T., Takeshima H., Tsuzuki T., Setoyama C., Shimada K., Tanase S.,
RA   Kuramitsu S., Kagamiyama H., Morino Y.;
RT   "Cloning and sequence analysis of cDNAs encoding mammalian cytosolic
RT   malate dehydrogenase. Comparison of the amino acid sequences of
RT   mammalian and bacterial malate dehydrogenase.";
RL   J. Biol. Chem. 262:15127-15131(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C3H/He; TISSUE=Liver;
RX   MEDLINE=89011964; PubMed=3172222; DOI=10.1016/0022-2836(88)90270-7;
RA   Setoyama C., Joh T., Tsuzuki T., Shimada K.;
RT   "Structural organization of the mouse cytosolic malate dehydrogenase
RT   gene: comparison with that of the mouse mitochondrial malate
RT   dehydrogenase gene.";
RL   J. Mol. Biol. 202:355-364(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Mammary gland, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 80-92; 126-142; 171-199; 206-230; 299-310 AND
RP   325-334, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [7]
RP   ISGYLATION.
RX   PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA   Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA   Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT   "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT   human cells.";
RL   Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-210, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: ISGylated.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
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CC   -----------------------------------------------------------------------
DR   EMBL; M29462; AAA39510.1; -; mRNA.
DR   EMBL; M36084; AAA37423.1; -; Genomic_DNA.
DR   EMBL; AK005237; BAB23897.1; -; mRNA.
DR   EMBL; AK164785; BAE37915.1; -; mRNA.
DR   EMBL; AK168545; BAE40421.1; -; mRNA.
DR   EMBL; AL663049; CAI24411.1; -; Genomic_DNA.
DR   EMBL; BC050940; AAH50940.2; -; mRNA.
DR   IPI; IPI00336324; -.
DR   PIR; S02654; DEMSMC.
DR   RefSeq; NP_032644.3; NM_008618.3.
DR   UniGene; Mm.212703; -.
DR   ProteinModelPortal; P14152; -.
DR   SMR; P14152; 2-334.
DR   STRING; P14152; -.
DR   PhosphoSite; P14152; -.
DR   SWISS-2DPAGE; P14152; -.
DR   COMPLUYEAST-2DPAGE; P14152; -.
DR   REPRODUCTION-2DPAGE; P14152; -.
DR   UCD-2DPAGE; P14152; -.
DR   PRIDE; P14152; -.
DR   Ensembl; ENSMUST00000102874; ENSMUSP00000099938; ENSMUSG00000020321.
DR   GeneID; 17449; -.
DR   KEGG; mmu:17449; -.
DR   NMPDR; fig|10090.3.peg.23330; -.
DR   UCSC; uc007idv.1; mouse.
DR   CTD; 17449; -.
DR   MGI; MGI:97051; Mdh1.
DR   eggNOG; roNOG11216; -.
DR   GeneTree; ENSGT00530000063410; -.
DR   HOGENOM; HBG289884; -.
DR   HOVERGEN; HBG006340; -.
DR   InParanoid; P14152; -.
DR   OMA; NFSAMTR; -.
DR   OrthoDB; EOG4CVG78; -.
DR   PhylomeDB; P14152; -.
DR   BRENDA; 1.1.1.37; 244.
DR   NextBio; 292088; -.
DR   ArrayExpress; P14152; -.
DR   Bgee; P14152; -.
DR   CleanEx; MM_MDH1; -.
DR   Genevestigator; P14152; -.
DR   GermOnline; ENSMUSG00000020321; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR001252; Malate_DH_AS.
DR   InterPro; IPR011274; Malate_DH_NAD-dep_euk.
DR   InterPro; IPR010945; Malate_DH_type2.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.90.110.10; lact_mal_DH; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR23382; MDH_SF1; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF56327; Lactate_DH/Glyco_hydro_4_C; 1.
DR   TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
DR   TIGRFAMs; TIGR01758; MDH_euk_cyt; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; NAD;
KW   Oxidoreductase; Phosphoprotein; Tricarboxylic acid cycle;
KW   Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    334       Malate dehydrogenase, cytoplasmic.
FT                                /FTId=PRO_0000113410.
FT   NP_BIND      11     17       NAD (By similarity).
FT   NP_BIND     129    131       NAD (By similarity).
FT   ACT_SITE    187    187       Proton acceptor (By similarity).
FT   BINDING      92     92       Substrate (By similarity).
FT   BINDING      98     98       Substrate (By similarity).
FT   BINDING     105    105       NAD (By similarity).
FT   BINDING     112    112       NAD (By similarity).
FT   BINDING     131    131       Substrate (By similarity).
FT   BINDING     162    162       Substrate (By similarity).
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES     103    103       N6-acetyllysine (By similarity).
FT   MOD_RES     118    118       N6-acetyllysine (By similarity).
FT   MOD_RES     210    210       Phosphotyrosine.
FT   MOD_RES     241    241       Phosphoserine.
FT   MOD_RES     298    298       N6-acetyllysine (By similarity).
FT   CONFLICT     92     92       R -> I (in Ref. 3; BAB23897).
FT   CONFLICT    177    177       D -> N (in Ref. 3; BAE37915).
FT   CONFLICT    288    288       F -> L (in Ref. 1 and 2).
SQ   SEQUENCE   334 AA;  36511 MW;  3B9F00372AA939DF CRC64;
     MSEPIRVLVT GAAGQIAYSL LYSIGNGSVF GKDQPIILVL LDITPMMGVL DGVLMELQDC
     ALPLLQDVIA TDKEEIAFKD LDVAVLVGSM PRREGMERKD LLKANVKIFK SQGTALEKYA
     KKSVKVIVVG NPANTNCLTA SKSAPSIPKE NFSCLTRLDH NRAKSQIALK LGVTADDVKN
     VIIWGNHSST QYPDVNHAKV KLQGKEVGVY EALKDDSWLK GEFITTVQQR GAAVIKARKL
     SSAMSAAKAI ADHIRDIWFG TPEGEFVSMG VISDGNSYGV PDDLLYSFPV VIKNKTWKFV
     EGLPINDFSR EKMDLTAKEL TEEKETAFEF LSSA
//
ID   CALR_MOUSE              Reviewed;         416 AA.
AC   P14211;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   08-MAR-2011, entry version 124.
DE   RecName: Full=Calreticulin;
DE   AltName: Full=CRP55;
DE   AltName: Full=Calregulin;
DE   AltName: Full=Endoplasmic reticulum resident protein 60;
DE            Short=ERp60;
DE   AltName: Full=HACBP;
DE   Flags: Precursor;
GN   Name=Calr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 18-48 AND 129-161.
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=90059955; PubMed=2583110;
RA   Smith M.J., Koch G.L.E.;
RT   "Multiple zones in the sequence of calreticulin (CRP55, calregulin,
RT   HACBP), a major calcium binding ER/SR protein.";
RL   EMBO J. 8:3581-3586(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=93013037; PubMed=1398135; DOI=10.1016/0378-1119(92)90096-8;
RA   Mazzarella R.A., Gold P., Cunningham M., Green M.;
RT   "Determination of the sequence of an expressible cDNA clone encoding
RT   ERp60/calregulin by the use of a novel nested set method.";
RL   Gene 120:217-225(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 18-38.
RC   TISSUE=Fibroblast;
RX   MEDLINE=95009907; PubMed=7523108; DOI=10.1002/elps.11501501101;
RA   Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.;
RT   "Separation and sequencing of familiar and novel murine proteins using
RT   preparative two-dimensional gel electrophoresis.";
RL   Electrophoresis 15:735-745(1994).
RN   [6]
RP   PROTEIN SEQUENCE OF 25-36; 56-64; 74-151; 154-159; 163-222; 225-272;
RP   323-351; 341-357 AND 392-413, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=93115648; PubMed=8418194; DOI=10.1084/jem.177.1.1;
RA   Dupuis M., Schaerer E., Krause K.-H., Tschopp J.;
RT   "The calcium-binding protein calreticulin is a major constituent of
RT   lytic granules in cytolytic T lymphocytes.";
RL   J. Exp. Med. 177:1-7(1993).
RN   [8]
RP   IDENTIFICATION IN AN EIF2 COMPLEX WITH EIF2S1; EIF2S2; CELF1; CALR3;
RP   HSPA5 AND HSP90B1.
RX   PubMed=16931514; DOI=10.1074/jbc.M605701200;
RA   Timchenko L.T., Salisbury E., Wang G.-L., Nguyen H., Albrecht J.H.,
RA   Hershey J.W., Timchenko N.A.;
RT   "Age-specific CUGBP1-eIF2 complex increases translation of
RT   CCAAT/enhancer-binding protein beta in old liver.";
RL   J. Biol. Chem. 281:32806-32819(2006).
CC   -!- FUNCTION: Molecular calcium-binding chaperone promoting folding,
CC       oligomeric assembly and quality control in the ER via the
CC       calreticulin/calnexin cycle. This lectin interacts transiently
CC       with almost all of the monoglucosylated glycoproteins that are
CC       synthesized in the ER. Interacts with the DNA-binding domain of
CC       NR3C1 and mediates its nuclear export (By similarity).
CC   -!- SUBUNIT: Monomer. Interacts with NR3C1, PDIA3/ERp57 and TRIM21 (By
CC       similarity). Component of an EIF2 complex at least composed of
CC       CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Cytoplasmic
CC       granule. Note=Associated with the lytic granules in the cytolytic
CC       T-lymphocytes.
CC   -!- DOMAIN: Can be divided into a N-terminal globular domain, a
CC       proline-rich P-domain forming an elongated arm-like structure and
CC       a C-terminal acidic domain. The P-domain binds one molecule of
CC       calcium with high affinity, whereas the acidic C-domain binds
CC       multiple calcium ions with low affinity (By similarity).
CC   -!- DOMAIN: The interaction with glycans occurs through a binding site
CC       in the globular lectin domain (By similarity).
CC   -!- DOMAIN: The zinc binding sites are localized to the N-domain (By
CC       similarity).
CC   -!- DOMAIN: Associates with PDIA3 through the tip of the extended arm
CC       formed by the P-domain (By similarity).
CC   -!- SIMILARITY: Belongs to the calreticulin family.
CC   -----------------------------------------------------------------------
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DR   EMBL; X14926; CAA33053.1; -; mRNA.
DR   EMBL; M92988; AAA37569.1; -; mRNA.
DR   EMBL; AK075605; BAC35852.1; -; mRNA.
DR   EMBL; BC003453; AAH03453.1; -; mRNA.
DR   IPI; IPI00123639; -.
DR   PIR; S06763; S06763.
DR   RefSeq; NP_031617.1; NM_007591.3.
DR   UniGene; Mm.1971; -.
DR   ProteinModelPortal; P14211; -.
DR   SMR; P14211; 16-363.
DR   IntAct; P14211; 7.
DR   STRING; P14211; -.
DR   PhosphoSite; P14211; -.
DR   SWISS-2DPAGE; P14211; -.
DR   COMPLUYEAST-2DPAGE; P14211; -.
DR   REPRODUCTION-2DPAGE; IPI00123639; -.
DR   REPRODUCTION-2DPAGE; P14211; -.
DR   PRIDE; P14211; -.
DR   Ensembl; ENSMUST00000003912; ENSMUSP00000003912; ENSMUSG00000003814.
DR   GeneID; 12317; -.
DR   KEGG; mmu:12317; -.
DR   UCSC; uc009mnp.1; mouse.
DR   CTD; 12317; -.
DR   MGI; MGI:88252; Calr.
DR   eggNOG; roNOG10495; -.
DR   HOGENOM; HBG444251; -.
DR   HOVERGEN; HBG005407; -.
DR   InParanoid; P14211; -.
DR   OMA; DSNIYAY; -.
DR   OrthoDB; EOG41JZCD; -.
DR   PhylomeDB; P14211; -.
DR   NextBio; 280884; -.
DR   ArrayExpress; P14211; -.
DR   Bgee; P14211; -.
DR   CleanEx; MM_CALR; -.
DR   Genevestigator; P14211; -.
DR   GermOnline; ENSMUSG00000003814; Mus musculus.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0042824; C:MHC class I peptide loading complex; IMP:BHF-UCL.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0005844; C:polysome; IDA:BHF-UCL.
DR   GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR   GO; GO:0003729; F:mRNA binding; IDA:BHF-UCL.
DR   GO; GO:0005529; F:sugar binding; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0090398; P:cellular senescence; IMP:BHF-UCL.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IDA:MGI.
DR   GO; GO:0002502; P:peptide antigen assembly with MHC class I protein complex; IMP:BHF-UCL.
DR   GO; GO:0045787; P:positive regulation of cell cycle; IMP:BHF-UCL.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; IMP:BHF-UCL.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0040020; P:regulation of meiosis; IDA:MGI.
DR   InterPro; IPR001580; Calret/calnex.
DR   InterPro; IPR018124; Calret/calnex_CS.
DR   InterPro; IPR009169; Calreticulin.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 2.
DR   PANTHER; PTHR11073; Calret/calnex; 1.
DR   Pfam; PF00262; Calreticulin; 1.
DR   PIRSF; PIRSF002356; Calreticulin; 1.
DR   PRINTS; PR00626; CALRETICULIN.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 2.
DR   PROSITE; PS00803; CALRETICULIN_1; 1.
DR   PROSITE; PS00804; CALRETICULIN_2; 1.
DR   PROSITE; PS00805; CALRETICULIN_REPEAT; 3.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Calcium; Chaperone; Direct protein sequencing;
KW   Disulfide bond; Endoplasmic reticulum; Lectin; Metal-binding; Repeat;
KW   Signal; Zinc.
FT   SIGNAL        1     17
FT   CHAIN        18    416       Calreticulin.
FT                                /FTId=PRO_0000004174.
FT   REPEAT      191    202       1-1.
FT   REPEAT      210    221       1-2.
FT   REPEAT      227    238       1-3.
FT   REPEAT      244    255       1-4.
FT   REPEAT      259    269       2-1.
FT   REPEAT      273    283       2-2.
FT   REPEAT      287    297       2-3.
FT   REGION       18    197       N-domain.
FT   REGION      191    255       4 X approximate repeats.
FT   REGION      198    308       P-domain.
FT   REGION      259    297       3 X approximate repeats.
FT   REGION      309    416       C-domain.
FT   MOTIF       413    416       Prevents secretion from ER.
FT   COMPBIAS    351    407       Asp/Glu/Lys-rich.
FT   MOD_RES      48     48       N6-acetyllysine (By similarity).
FT   MOD_RES     159    159       N6-acetyllysine (By similarity).
FT   MOD_RES     209    209       N6-acetyllysine (By similarity).
FT   DISULFID    105    137       By similarity.
SQ   SEQUENCE   416 AA;  47995 MW;  24C03B00913408D8 CRC64;
     MLLSVPLLLG LLGLAAADPA IYFKEQFLDG DAWTNRWVES KHKSDFGKFV LSSGKFYGDL
     EKDKGLQTSQ DARFYALSAK FEPFSNKGQT LVVQFTVKHE QNIDCGGGYV KLFPSGLDQK
     DMHGDSEYNI MFGPDICGPG TKKVHVIFNY KGKNVLINKD IRCKDDEFTH LYTLIVRPDN
     TYEVKIDNSQ VESGSLEDDW DFLPPKKIKD PDAAKPEDWD ERAKIDDPTD SKPEDWDKPE
     HIPDPDAKKP EDWDEEMDGE WEPPVIQNPE YKGEWKPRQI DNPDYKGTWI HPEIDNPEYS
     PDANIYAYDS FAVLGLDLWQ VKSGTIFDNF LITNDEAYAE EFGNETWGVT KAAEKQMKDK
     QDEEQRLKEE EEDKKRKEEE EAEDKEDDDD RDEDEDEEDE KEEDEEESPG QAKDEL
//
ID   HSPB1_MOUSE             Reviewed;         209 AA.
AC   P14602;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 3.
DT   08-MAR-2011, entry version 118.
DE   RecName: Full=Heat shock protein beta-1;
DE            Short=HspB1;
DE   AltName: Full=Growth-related 25 kDa protein;
DE   AltName: Full=Heat shock 25 kDa protein;
DE            Short=HSP 25;
DE   AltName: Full=Heat shock 27 kDa protein;
DE            Short=HSP 27;
DE   AltName: Full=p25;
GN   Name=Hspb1; Synonyms=Hsp25, Hsp27;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
RX   MEDLINE=93292999; PubMed=8514194; DOI=10.1016/0378-1119(93)90575-N;
RA   Gaestel M., Gotthardt R., Mueller T.;
RT   "Structure and organisation of a murine gene encoding small heat-shock
RT   protein Hsp25.";
RL   Gene 128:279-283(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A).
RX   MEDLINE=93292998; PubMed=8514193; DOI=10.1016/0378-1119(93)90574-M;
RA   Froehli E., Aoyama X., Klemenz R.;
RT   "Cloning of the mouse hsp25 gene and an extremely conserved hsp25
RT   pseudogene.";
RL   Gene 128:273-277(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A), AND PARTIAL PROTEIN
RP   SEQUENCE.
RX   MEDLINE=89137083; PubMed=2645135;
RX   DOI=10.1111/j.1432-1033.1989.tb14542.x;
RA   Gaestel M., Gross B., Benndorf R., Strauss M., Schunk W.-H., Kraft R.,
RA   Otto A., Boehm H., Stahl J., Drabsch H., Bielka H.;
RT   "Molecular cloning, sequencing and expression in Escherichia coli of
RT   the 25-kDa growth-related protein of Ehrlich ascites tumor and its
RT   homology to mammalian stress proteins.";
RL   Eur. J. Biochem. 179:209-213(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
RC   TISSUE=Bone;
RX   MEDLINE=94179147; PubMed=8132504;
RA   Cooper L.F., Uoshima K.;
RT   "Differential estrogenic regulation of small M(r) heat shock protein
RT   expression in osteoblasts.";
RL   J. Biol. Chem. 269:7869-7873(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PHOSPHORYLATION AT SER-15 AND SER-86.
RX   MEDLINE=91317843; PubMed=1860870;
RA   Gaestel M., Schroeder W., Benndorf R., Lippmann C., Buchner K.,
RA   Hucho F., Erdmann V.A., Bielka H.;
RT   "Identification of the phosphorylation sites of the murine small heat
RT   shock protein hsp25.";
RL   J. Biol. Chem. 266:14721-14724(1991).
RN   [7]
RP   INTERACTION WITH HSPBAP1.
RX   MEDLINE=20317062; PubMed=10751411; DOI=10.1074/jbc.M001981200;
RA   Liu C., Gilmont R.R., Benndorf R., Welsh M.J.;
RT   "Identification and characterization of a novel protein from Sertoli
RT   cells, PASS1, that associates with mammalian small stress protein
RT   hsp27.";
RL   J. Biol. Chem. 275:18724-18731(2000).
RN   [8]
RP   INTERACTION WITH TGFB1I1.
RX   MEDLINE=21523971; PubMed=11546764; DOI=10.1074/jbc.M103510200;
RA   Jia Y., Ransom R.F., Shibanuma M., Liu C., Welsh M.J., Smoyer W.E.;
RT   "Identification and characterization of hic-5/ARA55 as an hsp27
RT   binding protein.";
RL   J. Biol. Chem. 276:39911-39918(2001).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Involved in stress resistance and actin organization.
CC   -!- SUBUNIT: Associates with alpha- and beta-tubulin, microtubules and
CC       CRYAB. Interacts with HSPB8 (By similarity). Interacts with
CC       HSPBAP1 and TGFB1I1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Cytoplasm, cytoskeleton, spindle (By similarity).
CC       Note=Cytoplasmic in interphase cells. Colocalizes with mitotic
CC       spindles in mitotic cells. Translocates to the nucleus during heat
CC       shock and resides in sub-nuclear structures known as SC35 speckles
CC       or nuclear splicing speckles (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Additional isoforms seem to exist;
CC       Name=A;
CC         IsoId=P14602-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=P14602-2; Sequence=VSP_002422;
CC       Name=C;
CC         IsoId=P14602-3; Sequence=VSP_002423;
CC   -!- SIMILARITY: Belongs to the small heat shock protein (HSP20)
CC       family.
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DR   EMBL; X14687; CAA32818.1; -; mRNA.
DR   EMBL; X14686; CAB37341.1; -; mRNA.
DR   EMBL; L11609; AAA37862.1; -; Genomic_DNA.
DR   EMBL; L11608; AAA37862.1; JOINED; Genomic_DNA.
DR   EMBL; L07577; AAA37861.1; -; Genomic_DNA.
DR   EMBL; U03560; AAA18335.1; -; mRNA.
DR   EMBL; U03561; AAA18336.1; -; mRNA.
DR   EMBL; U03562; AAA18337.1; -; mRNA.
DR   EMBL; BC018257; AAH18257.1; -; mRNA.
DR   IPI; IPI00128522; -.
DR   IPI; IPI00468068; -.
DR   IPI; IPI00623819; -.
DR   PIR; A53423; A53423.
DR   PIR; I49763; JN0679.
DR   PIR; S02143; S02143.
DR   RefSeq; NP_038588.2; NM_013560.2.
DR   UniGene; Mm.13849; -.
DR   ProteinModelPortal; P14602; -.
DR   SMR; P14602; 101-169.
DR   DisProt; DP00142; -.
DR   IntAct; P14602; 4.
DR   STRING; P14602; -.
DR   PhosphoSite; P14602; -.
DR   SWISS-2DPAGE; P14602; -.
DR   REPRODUCTION-2DPAGE; IPI00128522; -.
DR   REPRODUCTION-2DPAGE; IPI00468068; -.
DR   REPRODUCTION-2DPAGE; P14602; -.
DR   UCD-2DPAGE; P14602; -.
DR   PRIDE; P14602; -.
DR   Ensembl; ENSMUST00000005077; ENSMUSP00000005077; ENSMUSG00000004951.
DR   Ensembl; ENSMUST00000111156; ENSMUSP00000106786; ENSMUSG00000004951.
DR   GeneID; 15507; -.
DR   KEGG; mmu:15507; -.
DR   CTD; 15507; -.
DR   MGI; MGI:96240; Hspb1.
DR   eggNOG; roNOG11002; -.
DR   GeneTree; ENSGT00550000074302; -.
DR   HOGENOM; HBG748242; -.
DR   HOVERGEN; HBG054766; -.
DR   InParanoid; P14602; -.
DR   OMA; AEITIPV; -.
DR   OrthoDB; EOG4DR9DF; -.
DR   PhylomeDB; P14602; -.
DR   NextBio; 288412; -.
DR   ArrayExpress; P14602; -.
DR   Bgee; P14602; -.
DR   CleanEx; MM_HSPB1; -.
DR   Genevestigator; P14602; -.
DR   GermOnline; ENSMUSG00000004951; Mus musculus.
DR   GO; GO:0005626; C:insoluble fraction; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005625; C:soluble fraction; IDA:MGI.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0030018; C:Z disc; IDA:MGI.
DR   GO; GO:0009408; P:response to heat; IEA:InterPro.
DR   InterPro; IPR001436; Alpha-crystallin/HSP.
DR   InterPro; IPR002068; Hsp20.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   Pfam; PF00011; HSP20; 1.
DR   PRINTS; PR00299; ACRYSTALLIN.
DR   SUPFAM; SSF49764; HSP20_chap; 1.
DR   PROSITE; PS01031; HSP20; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Nucleus; Phosphoprotein; Stress response.
FT   CHAIN         1    209       Heat shock protein beta-1.
FT                                /FTId=PRO_0000125928.
FT   REGION       74    209       Interaction with TGFB1I1 (By similarity).
FT   MOD_RES      13     13       Phosphoserine (By similarity).
FT   MOD_RES      15     15       Phosphoserine; by PKA and PKC.
FT   MOD_RES      27     27       Phosphoserine (By similarity).
FT   MOD_RES      86     86       Phosphoserine; by PKA and PKC.
FT   MOD_RES      87     87       Phosphoserine (By similarity).
FT   MOD_RES     127    127       N6-acetyllysine (By similarity).
FT   MOD_RES     203    203       Phosphoserine (By similarity).
FT   VAR_SEQ      37     70       Missing (in isoform C).
FT                                /FTId=VSP_002423.
FT   VAR_SEQ      61     72       Missing (in isoform B).
FT                                /FTId=VSP_002422.
FT   CONFLICT     13     13       S -> T (in Ref. 4; AAA18335/AAA18336/
FT                                AAA18337).
FT   CONFLICT     17     17       E -> G (in Ref. 4; AAA18335).
FT   CONFLICT     67     68       PA -> L (in Ref. 4; AAA18335).
FT   CONFLICT     99     99       Missing (in Ref. 3; CAA32818/CAB37341).
FT   CONFLICT    108    109       FA -> VI (in Ref. 3; CAA32818/CAB37341).
FT   CONFLICT    141    141       C -> Q (in Ref. 3; AA sequence).
FT   CONFLICT    181    181       A -> T (in Ref. 3; CAA32818/CAB37341).
SQ   SEQUENCE   209 AA;  23014 MW;  31BD9FAF4E107C50 CRC64;
     MTERRVPFSL LRSPSWEPFR DWYPAHSRLF DQAFGVPRLP DEWSQWFSAA GWPGYVRPLP
     AATAEGPAAV TLAAPAFSRA LNRQLSSGVS EIRQTADRWR VSLDVNHFAP EELTVKTKEG
     VVEITGKHEE RQDEHGYISR CFTRKYTLPP GVDPTLVSSS LSPEGTLTVE APLPKAVTQS
     AEITIPVTFE ARAQIGGPEA GKSEQSGAK
//
ID   PSMD3_MOUSE             Reviewed;         530 AA.
AC   P14685; Q99LL7;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 3;
DE   AltName: Full=26S proteasome regulatory subunit RPN3;
DE   AltName: Full=26S proteasome regulatory subunit S3;
DE   AltName: Full=Proteasome subunit p58;
DE   AltName: Full=Transplantation antigen P91A;
DE   AltName: Full=Tum-P91A antigen;
GN   Name=Psmd3; Synonyms=P91a, Tstap91a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=89324076; PubMed=2568889; DOI=10.1016/0092-8674(89)90844-1;
RA   Lurquin C., van Pel A., Mariame B., de Plaen E., Szikora J.-P.,
RA   Janssens C., Reddehase M.J., Lejeune J., Boon T.;
RT   "Structure of the gene of tum- transplantation antigen P91A: the
RT   mutated exon encodes a peptide recognized with Ld by cytolytic T
RT   cells.";
RL   Cell 58:293-303(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Acts as a regulatory subunit of the 26 proteasome which
CC       is involved in the ATP-dependent degradation of ubiquitinated
CC       proteins.
CC   -!- SUBUNIT: The 26S proteasome is composed of a core protease, known
CC       as the 20S proteasome, capped at one or both ends by the 19S
CC       regulatory complex (RC). The RC is composed of at least 18
CC       different subunits in two subcomplexes, the base and the lid,
CC       which form the portions proximal and distal to the 20S proteolytic
CC       core, respectively.
CC   -!- SIMILARITY: Belongs to the proteasome subunit S3 family.
CC   -!- SIMILARITY: Contains 1 PCI domain.
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DR   EMBL; M25149; AAA37241.1; -; Genomic_DNA.
DR   EMBL; BC003197; AAH03197.1; -; mRNA.
DR   IPI; IPI00314439; -.
DR   PIR; I49504; I49504.
DR   RefSeq; NP_033465.1; NM_009439.1.
DR   UniGene; Mm.12194; -.
DR   ProteinModelPortal; P14685; -.
DR   STRING; P14685; -.
DR   PhosphoSite; P14685; -.
DR   PRIDE; P14685; -.
DR   Ensembl; ENSMUST00000017365; ENSMUSP00000017365; ENSMUSG00000017221.
DR   GeneID; 22123; -.
DR   KEGG; mmu:22123; -.
DR   CTD; 22123; -.
DR   MGI; MGI:98858; Psmd3.
DR   eggNOG; roNOG09977; -.
DR   HOGENOM; HBG523170; -.
DR   HOVERGEN; HBG000703; -.
DR   InParanoid; P14685; -.
DR   OrthoDB; EOG4VHK6D; -.
DR   PhylomeDB; P14685; -.
DR   NextBio; 301989; -.
DR   ArrayExpress; P14685; -.
DR   Bgee; P14685; -.
DR   Genevestigator; P14685; -.
DR   GermOnline; ENSMUSG00000017221; Mus musculus.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR   InterPro; IPR013586; 26S_Psome_reg_C.
DR   InterPro; IPR013143; PAM.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF01399; PCI; 1.
DR   Pfam; PF08375; Rpn3_C; 1.
DR   SMART; SM00753; PAM; 1.
DR   SMART; SM00088; PINT; 1.
PE   2: Evidence at transcript level;
KW   Proteasome; Tumor antigen.
FT   CHAIN         1    530       26S proteasome non-ATPase regulatory
FT                                subunit 3.
FT                                /FTId=PRO_0000173817.
FT   DOMAIN      354    458       PCI.
FT   COMPBIAS     25     30       Poly-Pro.
FT   CONFLICT     12     13       AD -> H (in Ref. 1; AAA37241).
FT   CONFLICT    196    196       H -> R (in Ref. 2; AAH03197).
SQ   SEQUENCE   530 AA;  60699 MW;  E5964394503F9B78 CRC64;
     MKQEGSARRR GADKAKPPPG GEQEPPPPAP QDVEMKEEAA AGSGSTGEGD GKAAATEHSQ
     RELDTVTLED IKEHVRQLEK AVSGKEPRFV LRALRMLPST SRRLNHYVLY KAVHGFFTSN
     NATRDFLLPF LEEPMDTEAD LQFRPRTGKA ASAPLLPEVE AYLQLLMVIF LMNSKRYKEA
     QKISDDLMQK ISTQNHRALD LVAAKCYYYH ARVYEFLDKL DVVRSFLHAR LRTATLRHDA
     DGQATLLNLL LRNYLHYSLY DQAEKLVSKS VFPEQANNNE WARYLYYTGR IKAIQLEYSE
     ARRTMTNALR KAPQHTAVGF KQTVHKLLIV VELLLGEIPD RLQFRQPSLK RSLMPYFLLT
     QAVRTGNLAK FNQVLDQFGE KFQTDGTYTL IIRLRHNVIK TGVRMISLSY SRISLADIAQ
     KLQLDSPEDA EFIVAKAIRD GVIEASINHE KGYVQSKEMI DIYSTREPQL AFHQRISFCL
     DIHNMSVKAM RFPPKSYNKD LESAEERRER EQQDLEFAKE MAEDDDDSFP
//
ID   LMNB1_MOUSE             Reviewed;         588 AA.
AC   P14733; Q61791;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 116.
DE   RecName: Full=Lamin-B1;
DE   Flags: Precursor;
GN   Name=Lmnb1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RX   MEDLINE=89210899; PubMed=3243285;
RA   Hoeger T.H., Krohne G., Franke W.W.;
RT   "Amino acid sequence and molecular characterization of murine lamin B
RT   as deduced from cDNA clones.";
RL   Eur. J. Cell Biol. 47:283-290(1988).
RN   [2]
RP   SEQUENCE REVISION.
RA   Hoeger T.H.;
RL   Submitted (OCT-1989) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C3H/He;
RX   MEDLINE=96163889; PubMed=8586436; DOI=10.1006/geno.1995.9868;
RA   Maeno H., Sugimoto K., Nakajima N.;
RT   "Genomic structure of the mouse gene (Lmnb1) encoding nuclear lamin
RT   B1.";
RL   Genomics 30:342-346(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND THR-21, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; THR-21 AND SER-24,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392 AND SER-394, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Lamins are components of the nuclear lamina, a fibrous
CC       layer on the nucleoplasmic side of the inner nuclear membrane,
CC       which is thought to provide a framework for the nuclear envelope
CC       and may also interact with chromatin.
CC   -!- SUBCELLULAR LOCATION: Nucleus inner membrane; Lipid-anchor;
CC       Nucleoplasmic side.
CC   -!- PTM: B-type lamins undergo a series of modifications, such as
CC       farnesylation and phosphorylation. Increased phosphorylation of
CC       the lamins occurs before envelope disintegration and probably
CC       plays a role in regulating lamin associations.
CC   -!- MISCELLANEOUS: The structural integrity of the lamina is strictly
CC       controlled by the cell cycle, as seen by the disintegration and
CC       formation of the nuclear envelope in prophase and telophase,
CC       respectively.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
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DR   EMBL; X16705; CAA34677.1; -; mRNA.
DR   EMBL; M35153; AAC96023.1; ALT_SEQ; mRNA.
DR   EMBL; D50080; BAA08784.1; -; Genomic_DNA.
DR   EMBL; BC052729; AAH52729.1; -; mRNA.
DR   EMBL; BC058392; AAH58392.1; -; mRNA.
DR   IPI; IPI00230394; -.
DR   PIR; S07720; S07720.
DR   RefSeq; NP_034851.2; NM_010721.2.
DR   UniGene; Mm.4105; -.
DR   ProteinModelPortal; P14733; -.
DR   SMR; P14733; 32-68, 243-310, 312-386, 432-549.
DR   IntAct; P14733; 3.
DR   STRING; P14733; -.
DR   PhosphoSite; P14733; -.
DR   SWISS-2DPAGE; P14733; -.
DR   REPRODUCTION-2DPAGE; IPI00230394; -.
DR   PRIDE; P14733; -.
DR   Ensembl; ENSMUST00000025486; ENSMUSP00000025486; ENSMUSG00000024590.
DR   GeneID; 16906; -.
DR   KEGG; mmu:16906; -.
DR   UCSC; uc008eyt.1; mouse.
DR   CTD; 16906; -.
DR   MGI; MGI:96795; Lmnb1.
DR   eggNOG; roNOG07322; -.
DR   HOGENOM; HBG716303; -.
DR   HOVERGEN; HBG013015; -.
DR   InParanoid; P14733; -.
DR   OMA; HQQGTPR; -.
DR   OrthoDB; EOG45MN55; -.
DR   NextBio; 290940; -.
DR   ArrayExpress; P14733; -.
DR   Bgee; P14733; -.
DR   CleanEx; MM_LMNB1; -.
DR   Genevestigator; P14733; -.
DR   GermOnline; ENSMUSG00000024590; Mus musculus.
DR   GO; GO:0005638; C:lamin filament; IDA:MGI.
DR   GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR016044; F.
DR   InterPro; IPR001664; IF.
DR   InterPro; IPR001322; IF_tail_C.
DR   InterPro; IPR018039; Intermediate_filament_CS.
DR   PANTHER; PTHR23239; IF; 1.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF00932; IF_tail; 1.
DR   PROSITE; PS00226; IF; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Direct protein sequencing;
KW   Intermediate filament; Lipoprotein; Membrane; Methylation; Nucleus;
KW   Phosphoprotein; Prenylation.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    585       Lamin-B1.
FT                                /FTId=PRO_0000063817.
FT   PROPEP      586    588       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000403467.
FT   REGION        2     35       Head.
FT   REGION       36    387       Rod.
FT   REGION       36     70       Coil 1A.
FT   REGION       71     82       Linker 1.
FT   REGION       83    216       Coil 1B.
FT   REGION      217    244       Linker 2.
FT   REGION      245    387       Coil 2.
FT   REGION      388    588       Tail.
FT   MOTIF       416    421       Nuclear localization signal (Potential).
FT   COMPBIAS    553    561       Glu-rich (highly acidic; could be
FT                                involved in chromatin binding).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       5      5       Phosphothreonine (By similarity).
FT   MOD_RES      14     14       Phosphoserine (By similarity).
FT   MOD_RES      17     17       Phosphoserine.
FT   MOD_RES      21     21       Phosphothreonine.
FT   MOD_RES      24     24       Phosphoserine.
FT   MOD_RES      29     29       Phosphoserine (By similarity).
FT   MOD_RES     158    158       N6-acetyllysine (By similarity).
FT   MOD_RES     201    201       Phosphoserine (By similarity).
FT   MOD_RES     272    272       N6-acetyllysine (By similarity).
FT   MOD_RES     279    279       Phosphoserine (By similarity).
FT   MOD_RES     280    280       Phosphoserine (By similarity).
FT   MOD_RES     285    285       Phosphoserine (By similarity).
FT   MOD_RES     376    376       Phosphoserine (By similarity).
FT   MOD_RES     392    392       Phosphoserine.
FT   MOD_RES     394    394       Phosphoserine.
FT   MOD_RES     405    405       Phosphoserine (By similarity).
FT   MOD_RES     484    484       N6-acetyllysine (By similarity).
FT   MOD_RES     581    581       Phosphoserine (By similarity).
FT   MOD_RES     585    585       Cysteine methyl ester (By similarity).
FT   LIPID       585    585       S-farnesyl cysteine (By similarity).
FT   CONFLICT    581    581       S -> W (in Ref. 1; CAA34677/AAC96023).
SQ   SEQUENCE   588 AA;  66786 MW;  3602BCE63588A32D CRC64;
     MATATPVQQQ RAGSRASAPA TPLSPTRLSR LQEKEELREL NDRLAVYIDK VRSLETENSA
     LQLQVTEREE VRGRELTGLK ALYETELADA RRALDDTARE RAKLQIELGK FKAEHDQLLL
     NYAKKESDLS GAQIKLREYE AALNSKDAAL ATALGDKKSL EGDLEDLKDQ IAQLEASLSA
     AKKQLADETL LKVDLENRCQ SLTEDLEFRK NMYEEEINET RRKHETRLVE VDSGRQIEYE
     YKLAQALHEM REQHDAQVRL YKEELEQTYH AKLENARLSS EMNTSTVNSA REELMESRMR
     IESLSSQLSN LQKESRACLE RIQELEDMLA KERDNSRRML SDREREMAEI RDQMQQQLSD
     YEQLLDVKLA LDMEISAYRK LLEGEEERLK LSPSPSSRVT VSRASSSRSV RTTRGKRKRV
     DVEESEASSS VSISHSASAT GNVCIEEIDV DGKFIRLKNT SEQDQPMGGW EMIRKIGDTS
     VSYKYTSRYV LKAGQTVTVW AANAGVTASP PTDLIWKNQN SWGTGEDVKV ILKNSQGEEV
     AQRSTVFKTT IPEEEEEEEE EPIGVAVEEE RFHQQGAPRA SNKSCAIM
//
ID   ANXA6_MOUSE             Reviewed;         673 AA.
AC   P14824;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Annexin A6;
DE   AltName: Full=67 kDa calelectrin;
DE   AltName: Full=Annexin VI;
DE   AltName: Full=Annexin-6;
DE   AltName: Full=Calphobindin-II;
DE            Short=CPB-II;
DE   AltName: Full=Chromobindin-20;
DE   AltName: Full=Lipocortin VI;
DE   AltName: Full=Protein III;
DE   AltName: Full=p68;
DE   AltName: Full=p70;
GN   Name=Anxa6; Synonyms=Anx6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=89030687; PubMed=2972541;
RX   DOI=10.1111/j.1432-1033.1988.tb14340.x;
RA   Moss S.E., Crompton M.R., Crumpton M.J.;
RT   "Molecular cloning of murine p68, a Ca2+-binding protein of the
RT   lipocortin family.";
RL   Eur. J. Biochem. 177:21-27(1988).
RN   [2]
RP   PROTEIN SEQUENCE OF 35-50; 69-81; 123-135; 282-290; 378-393; 457-465;
RP   484-498; 500-509 AND 630-638, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-201, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-30, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: May associate with CD21. May regulate the release of
CC       Ca(2+) from intracellular stores.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Melanosome (By
CC       similarity).
CC   -!- DOMAIN: A pair of annexin repeats may form one binding site for
CC       calcium and phospholipid.
CC   -!- MISCELLANEOUS: Seems to bind one calcium ion with high affinity.
CC   -!- SIMILARITY: Belongs to the annexin family.
CC   -!- SIMILARITY: Contains 8 annexin repeats.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X13460; CAA31808.1; -; mRNA.
DR   IPI; IPI00554894; -.
DR   PIR; S01786; S01786.
DR   UniGene; Mm.265347; -.
DR   ProteinModelPortal; P14824; -.
DR   SMR; P14824; 10-673.
DR   STRING; P14824; -.
DR   PhosphoSite; P14824; -.
DR   PRIDE; P14824; -.
DR   Ensembl; ENSMUST00000108883; ENSMUSP00000104511; ENSMUSG00000018340.
DR   MGI; MGI:88255; Anxa6.
DR   eggNOG; roNOG07341; -.
DR   HOGENOM; HBG444222; -.
DR   HOVERGEN; HBG061815; -.
DR   InParanoid; P14824; -.
DR   OrthoDB; EOG4PVNZ6; -.
DR   ArrayExpress; P14824; -.
DR   Bgee; P14824; -.
DR   CleanEx; MM_ANXA6; -.
DR   Genevestigator; P14824; -.
DR   GermOnline; ENSMUSG00000018340; Mus musculus.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR   GO; GO:0006937; P:regulation of muscle contraction; IMP:MGI.
DR   InterPro; IPR001464; Annexin.
DR   InterPro; IPR018502; Annexin_repeat.
DR   InterPro; IPR018252; Annexin_repeat_CS.
DR   InterPro; IPR002393; AnnexinVI.
DR   Gene3D; G3DSA:1.10.220.10; Annexin; 8.
DR   PANTHER; PTHR10502; Annexin; 1.
DR   Pfam; PF00191; Annexin; 8.
DR   PRINTS; PR00196; ANNEXIN.
DR   PRINTS; PR00202; ANNEXINVI.
DR   SMART; SM00335; ANX; 8.
DR   SUPFAM; SSF47874; Annexin; 2.
DR   PROSITE; PS00223; ANNEXIN; 8.
PE   1: Evidence at protein level;
KW   Acetylation; Annexin; Calcium; Calcium/phospholipid-binding;
KW   Cytoplasm; Direct protein sequencing; Phosphoprotein; Repeat.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    673       Annexin A6.
FT                                /FTId=PRO_0000067495.
FT   REPEAT       29     89       Annexin 1.
FT   REPEAT      101    161       Annexin 2.
FT   REPEAT      185    245       Annexin 3.
FT   REPEAT      260    320       Annexin 4.
FT   REPEAT      372    432       Annexin 5.
FT   REPEAT      444    504       Annexin 6.
FT   REPEAT      533    593       Annexin 7.
FT   REPEAT      608    668       Annexin 8.
FT   MOD_RES      30     30       Phosphotyrosine.
FT   MOD_RES      63     63       N6-acetyllysine (By similarity).
FT   MOD_RES      68     68       N6-acetyllysine (By similarity).
FT   MOD_RES      75     75       N6-acetyllysine (By similarity).
FT   MOD_RES      81     81       N6-acetyllysine (By similarity).
FT   MOD_RES     201    201       Phosphotyrosine.
FT   MOD_RES     299    299       N6-acetyllysine (By similarity).
FT   MOD_RES     306    306       N6-acetyllysine (By similarity).
FT   MOD_RES     370    370       N6-acetyllysine (By similarity).
FT   MOD_RES     418    418       N6-acetyllysine (By similarity).
FT   MOD_RES     483    483       N6-acetyllysine (By similarity).
FT   MOD_RES     607    607       N6-acetyllysine (By similarity).
FT   MOD_RES     620    620       N6-acetyllysine (By similarity).
SQ   SEQUENCE   673 AA;  75886 MW;  955896190C7E360B CRC64;
     MAKIAQGAMY RGSVHDFPEF DANQDAEALY TAMKGFGSDK ESILELITSR SNKQRQEICQ
     SYKSLYGKDL IEDLKYELTG KFERLIVNLM RPLAYCDAKE IKDAISGIGT DEKCLIEILA
     SRTNEQMHQL VAAYKDAYER DLESDIIGDT SGHFQKMLVV LLQGTRENDD VVSEDLVQQD
     VQDLYEAGEL KWGTDEAQFI YILGNRSKQH LRLVFDEYLK TTGKPIEASI RGELSGDFEK
     LMLAVVKCIR STPEYFAERL FKAMKGLGTR DNTLIRIMVS RSELDMLDIR EIFRTKYEKS
     LYSMIKNDTS GEYKKALLKL CGGDDDAAAQ FFPEAAQVAY QMWELSAVSR VELKGTVCAA
     NDFNPDADAK ALRKAMKGIG TDEATIIDIV THRSNAQRQQ IRQTFKSHFG RDLMADLKSE
     ISGDLARLIL GLMMPPAHYD AKQLKKAMEG AGTDEKTLIE ILATRTNAEI RAINEAYKED
     YHKSLEDALS SDTSGHFRRI LISLATGNRE EGGENRDQAQ EDAQVAAEIL EIADTPSGDK
     TSLETRFMTV LCTRSYPHLR RVFQEFIKKT NYDIEHVIKK EMSGDVKDAF VAIVQSVKNK
     PLFFADKLYK SMKGAGTDEK TLTRVMVSRS EIDLLNIRRE FIEKYDKSLH QAIEGDTSGD
     FMKALLALCG GED
//
ID   RLA0_MOUSE              Reviewed;         317 AA.
AC   P14869; Q99L54;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 3.
DT   08-MAR-2011, entry version 100.
DE   RecName: Full=60S acidic ribosomal protein P0;
DE   AltName: Full=60S ribosomal protein L10E;
GN   Name=Rplp0; Synonyms=Arbp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=89366686; PubMed=2771657; DOI=10.1093/nar/17.15.6408;
RA   Krowczynska A.M., Coutts M., Makrides S., Brawerman G.;
RT   "The mouse homologue of the human acidic ribosomal phosphoprotein PO:
RT   a highly conserved polypeptide that is under translational control.";
RL   Nucleic Acids Res. 17:6408-6408(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 135-146 AND 150-162.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Ribosomal protein P0 is the functional equivalent of
CC       E.coli protein L10.
CC   -!- SUBUNIT: P0 forms a pentameric complex by interaction with dimers
CC       of P1 and P2. Identified in a mRNP granule complex, at least
CC       composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB,
CC       HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3,
CC       NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X,
CC       RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs.
CC       Interacts with APEX1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity). Note=Localized in cytoplasmic mRNP granules
CC       containing untranslated mRNAs (By similarity).
CC   -!- SIMILARITY: Belongs to the ribosomal protein L10P family.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; X15267; CAA33338.1; -; mRNA.
DR   EMBL; AK010267; BAB26807.1; -; mRNA.
DR   EMBL; AK012606; BAB28352.1; -; mRNA.
DR   EMBL; AK029816; BAC26631.1; -; mRNA.
DR   EMBL; AK081678; BAC38288.1; -; mRNA.
DR   EMBL; BC003833; AAH03833.1; -; mRNA.
DR   EMBL; BC011106; AAH11106.1; -; mRNA.
DR   EMBL; BC011291; AAH11291.1; -; mRNA.
DR   IPI; IPI00314950; -.
DR   PIR; S05305; R5MS10.
DR   RefSeq; NP_031501.1; NM_007475.5.
DR   UniGene; Mm.371545; -.
DR   UniGene; Mm.5286; -.
DR   ProteinModelPortal; P14869; -.
DR   SMR; P14869; 1-259, 262-308.
DR   STRING; P14869; -.
DR   PhosphoSite; P14869; -.
DR   PRIDE; P14869; -.
DR   Ensembl; ENSMUST00000086519; ENSMUSP00000083705; ENSMUSG00000067274.
DR   GeneID; 11837; -.
DR   KEGG; mmu:11837; -.
DR   UCSC; uc008zed.1; mouse.
DR   CTD; 11837; -.
DR   MGI; MGI:1927636; Rplp0.
DR   eggNOG; roNOG12568; -.
DR   HOGENOM; HBG601294; -.
DR   HOVERGEN; HBG000711; -.
DR   InParanoid; P14869; -.
DR   OMA; GKNTMIR; -.
DR   OrthoDB; EOG4VDQ10; -.
DR   PhylomeDB; P14869; -.
DR   NextBio; 279771; -.
DR   ArrayExpress; P14869; -.
DR   Bgee; P14869; -.
DR   CleanEx; MM_RPLP0; -.
DR   Genevestigator; P14869; -.
DR   GermOnline; ENSMUSG00000067274; Mus musculus.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:InterPro.
DR   GO; GO:0006414; P:translational elongation; IEA:InterPro.
DR   InterPro; IPR001813; Ribosomal_60S.
DR   InterPro; IPR001790; Ribosomal_L10/acidic_P0.
DR   Pfam; PF00428; Ribosomal_60s; 1.
DR   Pfam; PF00466; Ribosomal_L10; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Nucleus;
KW   Phosphoprotein; Ribonucleoprotein; Ribosomal protein.
FT   CHAIN         1    317       60S acidic ribosomal protein P0.
FT                                /FTId=PRO_0000154759.
FT   MOD_RES      24     24       Phosphotyrosine.
FT   MOD_RES      77     77       N6-acetyllysine (By similarity).
FT   MOD_RES     304    304       Phosphoserine.
FT   MOD_RES     307    307       Phosphoserine.
FT   CONFLICT    262    262       T -> A (in Ref. 3; AAH03833/AAH11106/
FT                                AAH11291).
SQ   SEQUENCE   317 AA;  34216 MW;  7985E1D7B235EAD0 CRC64;
     MPREDRATWK SNYFLKIIQL LDDYPKCFIV GADNVGSKQM QQIRMSLRGK AVVLMGKNTM
     MRKAIRGHLE NNPALEKLLP HIRGNVGFVF TKEDLTEIRD MLLANKVPAA ARAGAIAPCE
     VTVPAQNTGL GPEKTSFFQA LGITTKISRG TIEILSDVQL IKTGDKVGAS EATLLNMLNI
     SPFSFGLIIQ QVFDNGSIYN PEVLDITEQA LHSRFLEGVR NVASVCLQIG YPTVASVPHS
     IINGYKRVLA LSVETEYTFP LTEKVKAFLA DPSAFAAAAP AAAATTAAPA AAAAPAKAEA
     KEESEESDED MGFGLFD
//
ID   JUND_MOUSE              Reviewed;         341 AA.
AC   P15066;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   08-MAR-2011, entry version 102.
DE   RecName: Full=Transcription factor jun-D;
GN   Name=Jund; Synonyms=Jun-d, Jund1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=89160806; PubMed=2493644; DOI=10.1073/pnas.86.5.1500;
RA   Ryder K., Lanahan A., Perez-Albuerne E., Nathans D.;
RT   "jun-D: a third member of the jun gene family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:1500-1503(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=89356612; PubMed=2504580;
RA   Hirai S., Ryseck R.P., Mechta F., Bravo R., Yaniv M.;
RT   "Characterization of junD: a new member of the jun proto-oncogene
RT   family.";
RL   EMBO J. 8:1433-1439(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90110219; PubMed=2104845;
RA   Li L., Hu J.-S., Olson E.N.;
RT   "Different members of the jun proto-oncogene family exhibit distinct
RT   patterns of expression in response to type beta transforming growth
RT   factor.";
RL   J. Biol. Chem. 265:1556-1562(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBUNIT: Binds DNA as a dimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Brain and kidney.
CC   -!- SIMILARITY: Belongs to the bZIP family. Jun subfamily.
CC   -!- SIMILARITY: Contains 1 bZIP domain.
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DR   EMBL; J04509; AAA39344.1; -; Genomic_DNA.
DR   EMBL; X15358; CAA33418.1; -; mRNA.
DR   EMBL; J05205; AAA39345.1; -; mRNA.
DR   EMBL; BC010572; AAH10572.1; -; mRNA.
DR   IPI; IPI00126223; -.
DR   PIR; A32158; TVMSJD.
DR   RefSeq; NP_034722.1; NM_010592.4.
DR   UniGene; Mm.419851; -.
DR   ProteinModelPortal; P15066; -.
DR   SMR; P15066; 267-318.
DR   STRING; P15066; -.
DR   PhosphoSite; P15066; -.
DR   PRIDE; P15066; -.
DR   Ensembl; ENSMUST00000095267; ENSMUSP00000092901; ENSMUSG00000071076.
DR   GeneID; 16478; -.
DR   KEGG; mmu:16478; -.
DR   UCSC; uc009mbe.1; mouse.
DR   CTD; 16478; -.
DR   MGI; MGI:96648; Jund.
DR   GeneTree; ENSGT00390000009929; -.
DR   HOGENOM; HBG446073; -.
DR   HOVERGEN; HBG001722; -.
DR   InParanoid; P15066; -.
DR   OMA; QFLYPKV; -.
DR   OrthoDB; EOG4RV2RS; -.
DR   PhylomeDB; P15066; -.
DR   NextBio; 289771; -.
DR   ArrayExpress; P15066; -.
DR   Bgee; P15066; -.
DR   CleanEx; MM_JUND; -.
DR   Genevestigator; P15066; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0071277; P:cellular response to calcium ion; IDA:MGI.
DR   GO; GO:0002076; P:osteoblast development; IGI:MGI.
DR   GO; GO:0010552; P:positive regulation of gene-specific transcription from RNA polymerase II promoter; IGI:MGI.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; IGI:MGI.
DR   InterPro; IPR011616; bZIP_1.
DR   InterPro; IPR008917; Euk_TF_DNA-bd.
DR   InterPro; IPR005643; JNK.
DR   InterPro; IPR002112; Leuzip_Jun.
DR   InterPro; IPR004827; TF_bZIP.
DR   Pfam; PF00170; bZIP_1; 1.
DR   Pfam; PF03957; Jun; 1.
DR   PRINTS; PR00043; LEUZIPPRJUN.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF47454; Euk_transcr_DNA; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    341       Transcription factor jun-D.
FT                                /FTId=PRO_0000076443.
FT   DOMAIN      290    318       Leucine-zipper.
FT   DNA_BIND    268    286       Basic motif.
FT   MOD_RES     100    100       Phosphoserine (By similarity).
FT   MOD_RES     245    245       Phosphoserine (By similarity).
FT   MOD_RES     249    249       Phosphoserine (By similarity).
FT   MOD_RES     253    253       Phosphoserine (By similarity).
FT   CONFLICT      5      5       F -> L (in Ref. 3; AAA39345).
FT   CONFLICT     61     62       EQ -> DE (in Ref. 3; AAA39345).
FT   CONFLICT    317    318       QL -> HV (in Ref. 3; AAA39345).
SQ   SEQUENCE   341 AA;  34905 MW;  2727392F6B65188D CRC64;
     METPFYGEEA LSGLAAGASS VAGATGAPGG GGFAPPGRAF PGAPPTSSML KKDALTLSLA
     EQGAAGLKPG SATAPSALRP DGAPDGLLAS PDLGLLKLAS PELERLIIQS NGLVTTTPTS
     TQFLYPKVAA SEEQEFAEGF VKALEDLHKQ SQLGAATAAT SGAPAPPAPA DLAATPGATE
     TPVYANLSSF AGGAGPPGGA ATVAFAAEPV PFPPPPGALG PPPPPHPPRL AALKDEPQTV
     PDVPSFGDSP PLSPIDMDTQ ERIKAERKRL RNRIAASKCR KRKLERISRL EEKVKTLKSQ
     NTELASTASL LREQVAQLKQ KVLSHVNSGC QLLPQHQVPA Y
//
ID   GLNA_MOUSE              Reviewed;         373 AA.
AC   P15105; Q3TRK7; Q64432; Q91VC6;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 6.
DT   08-MAR-2011, entry version 104.
DE   RecName: Full=Glutamine synthetase;
DE            Short=GS;
DE            EC=6.3.1.2;
DE   AltName: Full=Glutamate decarboxylase;
DE            EC=4.1.1.15;
DE   AltName: Full=Glutamate--ammonia ligase;
GN   Name=Glul; Synonyms=Glns;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=89362463; PubMed=2475638; DOI=10.1016/0022-2836(89)90086-7;
RA   Kuo C.F., Darnell J.E. Jr.;
RT   "Mouse glutamine synthetase is encoded by a single gene that can be
RT   expressed in a localized fashion.";
RL   J. Mol. Biol. 208:45-56(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Thymus;
RA   Lindemann A.E., Tempest P.R.;
RT   "Sequence of a mouse glutamine synthetase cDNA.";
RL   Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=FVB; TISSUE=Liver;
RA   Labruyere W.T., van Hemert F.J., Lamers W.H.;
RT   "Glutamine synthetase mRNA in rodents.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Amnion, Hippocampus, and Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-11; 15-25; 96-103; 174-181; 292-298 AND 341-357,
RP   CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Liver;
RA   Bienvenut W.V.;
RL   Submitted (JUL-2005) to UniProtKB.
RN   [7]
RP   PROTEIN SEQUENCE OF 26-41; 46-52; 174-222 AND 341-357, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-104 AND TYR-180, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Essential for proliferation of fetal skin fibroblasts.
CC       This enzyme has 2 functions: it catalyzes the production of
CC       glutamine and 4-aminobutanoate (gamma-aminobutyric acid, GABA),
CC       the latter in a pyridoxal phosphate-independent manner (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
CC       L-glutamine.
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC   -!- COFACTOR: Biotin (By similarity).
CC   -!- COFACTOR: Magnesium or manganese (By similarity).
CC   -!- SUBUNIT: Homooctamer and homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; X16314; CAA34381.1; -; mRNA.
DR   EMBL; U09114; AAA17989.1; -; mRNA.
DR   EMBL; AY044241; AAK95328.1; -; mRNA.
DR   EMBL; AK159106; BAE34822.1; -; mRNA.
DR   EMBL; AK160670; BAE35950.1; -; mRNA.
DR   EMBL; AK162685; BAE37022.1; -; mRNA.
DR   EMBL; AK168493; BAE40380.1; -; mRNA.
DR   EMBL; BC015086; AAH15086.1; -; mRNA.
DR   IPI; IPI00626790; -.
DR   PIR; S04991; AJMSQ.
DR   RefSeq; NP_032157.2; NM_008131.3.
DR   UniGene; Mm.210745; -.
DR   ProteinModelPortal; P15105; -.
DR   SMR; P15105; 10-365.
DR   IntAct; P15105; 6.
DR   STRING; P15105; -.
DR   PhosphoSite; P15105; -.
DR   SWISS-2DPAGE; P15105; -.
DR   REPRODUCTION-2DPAGE; IPI00626790; -.
DR   REPRODUCTION-2DPAGE; P15105; -.
DR   UCD-2DPAGE; P15105; -.
DR   PRIDE; P15105; -.
DR   Ensembl; ENSMUST00000086199; ENSMUSP00000083375; ENSMUSG00000026473.
DR   GeneID; 14645; -.
DR   KEGG; mmu:14645; -.
DR   CTD; 14645; -.
DR   MGI; MGI:95739; Glul.
DR   eggNOG; roNOG14268; -.
DR   GeneTree; ENSGT00390000010047; -.
DR   HOGENOM; HBG299709; -.
DR   HOVERGEN; HBG005847; -.
DR   InParanoid; P15105; -.
DR   OMA; RLSKRHQ; -.
DR   OrthoDB; EOG444KKD; -.
DR   PhylomeDB; P15105; -.
DR   BRENDA; 6.3.1.2; 244.
DR   NextBio; 286500; -.
DR   ArrayExpress; P15105; -.
DR   Bgee; P15105; -.
DR   CleanEx; MM_GLUL; -.
DR   Genevestigator; P15105; -.
DR   GermOnline; ENSMUSG00000026473; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:EC.
DR   GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:EC.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR   GO; GO:0009749; P:response to glucose stimulus; IMP:MGI.
DR   InterPro; IPR008147; Gln_synt_beta.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR008146; Gln_synth_cat_dom.
DR   Gene3D; G3DSA:3.30.590.10; ATP-gua_Ptrans; 1.
DR   Gene3D; G3DSA:3.10.20.70; G3DSA:3.10.20.70; 1.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   Pfam; PF03951; Gln-synt_N; 1.
DR   SUPFAM; SSF54368; Gln_synt_beta; 1.
DR   PROSITE; PS00180; GLNA_1; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing;
KW   Ligase; Lyase; Mitochondrion; Nucleotide-binding; Phosphoprotein.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    373       Glutamine synthetase.
FT                                /FTId=PRO_0000153141.
FT   MOD_RES       2      2       N-acetylalanine.
FT   MOD_RES     104    104       Phosphotyrosine.
FT   MOD_RES     180    180       Phosphotyrosine.
FT   CONFLICT     91     91       K -> R (in Ref. 1; CAA34381).
FT   CONFLICT    111    111       T -> S (in Ref. 2; AAA17989).
FT   CONFLICT    133    133       M -> L (in Ref. 4; BAE37022).
FT   CONFLICT    249    249       G -> V (in Ref. 1; CAA34381).
FT   CONFLICT    269    269       C -> W (in Ref. 2; AAA17989).
FT   CONFLICT    299    299       R -> A (in Ref. 1; CAA34381).
FT   CONFLICT    342    343       PS -> LR (in Ref. 1; CAA34381).
SQ   SEQUENCE   373 AA;  42120 MW;  1EC9CDC5D81DE63F CRC64;
     MATSASSHLN KGIKQMYMSL PQGEKVQAMY IWVDGTGEGL RCKTRTLDCE PKCVEELPEW
     NFDGSSTFQS EGSNSDMYLH PVAMFRDPFR KDPNKLVLCE VFKYNRKPAE TNLRHICKRI
     MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADKA YGRDIVEAHY
     RACLYAGVKI TGTNAEVMPA QWEFQIGPCE GIRMGDHLWI ARFILHRVCE DFGVIATFDP
     KPIPGNWNGA GCHTNFSTKA MREENGLKCI EEAIDKLSKR HQYHIRAYDP KGGLDNARRL
     TGFHETSNIN DFSAGVANRG ASIRIPRTVG QEKKGYFEDR RPSANCDPYA VTEAIVRTCL
     LNETGDEPFQ YKN
//
ID   NTRK2_MOUSE             Reviewed;         821 AA.
AC   P15209; Q3TUF9; Q80WU0; Q91XJ9;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   08-MAR-2011, entry version 133.
DE   RecName: Full=BDNF/NT-3 growth factors receptor;
DE            EC=2.7.10.1;
DE   AltName: Full=GP145-TrkB/GP95-TrkB;
DE            Short=Trk-B;
DE   AltName: Full=Neurotrophic tyrosine kinase receptor type 2;
DE   AltName: Full=TrkB tyrosine kinase;
DE   Flags: Precursor;
GN   Name=Ntrk2; Synonyms=Trkb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GP145-TRKB).
RC   TISSUE=Brain;
RX   MEDLINE=90059970; PubMed=2555172;
RA   Klein R., Parada L.F., Coulier F., Barbacid M.;
RT   "trkB, a novel tyrosine protein kinase receptor expressed during mouse
RT   neural development.";
RL   EMBO J. 8:3701-3709(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS GP145-TRKB AND GP95-TRKB).
RC   TISSUE=Brain;
RX   MEDLINE=90263089; PubMed=2160854; DOI=10.1016/0092-8674(90)90476-U;
RA   Klein R., Conway D., Parada L.F., Barbacid M.;
RT   "The trkB tyrosine protein kinase gene codes for a second neurogenic
RT   receptor that lacks the catalytic kinase domain.";
RL   Cell 61:647-656(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS GP145-TRKB AND
RP   GP95-TRKB).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GP95-TRKB).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PARTIAL NUCLEOTIDE SEQUENCE (ISOFORMS L1 AND L10).
RC   TISSUE=Trigeminal ganglion;
RX   MEDLINE=97294706; PubMed=9148911; DOI=10.1074/jbc.272.20.13019;
RA   Ninkina N., Grashchuck M., Buchman V.L., Davies A.M.;
RT   "TrkB variants with deletions in the leucine-rich motifs of the
RT   extracellular domain.";
RL   J. Biol. Chem. 272:13019-13025(1997).
RN   [6]
RP   FUNCTION.
RX   MEDLINE=91249395; PubMed=1645620; DOI=10.1016/0092-8674(91)90396-G;
RA   Soppet D., Escandon E., Maragos J., Middlemas D.S., Reid S.W.,
RA   Blair J., Burton L.E., Stanton B.R., Kaplan D.R., Hunter T.,
RA   Nicolics K., Parada L.F.;
RT   "The neurotrophic factors brain-derived neurotrophic factor and
RT   neurotrophin-3 are ligands for the trkB tyrosine kinase receptor.";
RL   Cell 65:895-903(1991).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-515, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Receptor for brain-derived neurotrophic factor (BDNF),
CC       neurotrophin-3 and neurotrophin-4/5 but not nerve growth factor
CC       (NGF). Involved in the development and/or maintenance of the
CC       nervous system. This is a tyrosine-protein kinase receptor. Known
CC       substrates for the TRK receptors are SHC1, PI-3 kinase, and PLC-
CC       gamma-1.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBUNIT: Exists in a dynamic equilibrium between monomeric (low
CC       affinity) and dimeric (high affinity) structures. Binds SH2B2.
CC       Interacts with SQSTM1 and KIDINS220 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Additional isoforms seem to exist;
CC       Name=GP145-TRKB; Synonyms=L3;
CC         IsoId=P15209-1; Sequence=Displayed;
CC       Name=GP95-TRKB; Synonyms=T1;
CC         IsoId=P15209-2; Sequence=VSP_002908, VSP_002909;
CC       Name=L1;
CC         IsoId=P15209-3; Sequence=VSP_002907;
CC       Name=L10;
CC         IsoId=P15209-4; Sequence=VSP_002905, VSP_002906;
CC   -!- TISSUE SPECIFICITY: The different forms are differentially
CC       expressed in various cell types.
CC   -!- PTM: Ligand-mediated auto-phosphorylation.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Insulin receptor subfamily.
CC   -!- SIMILARITY: Contains 2 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SIMILARITY: Contains 2 LRR (leucine-rich) repeats.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M33385; AAA40482.1; -; mRNA.
DR   EMBL; X17647; CAA35636.1; -; mRNA.
DR   EMBL; AK018789; BAB31412.1; -; mRNA.
DR   EMBL; AK147391; BAE27880.1; -; mRNA.
DR   EMBL; AK160789; BAE36012.1; -; mRNA.
DR   EMBL; BC052014; AAH52014.2; -; mRNA.
DR   IPI; IPI00128360; -.
DR   IPI; IPI00229333; -.
DR   IPI; IPI00229334; -.
DR   IPI; IPI00270098; -.
DR   PIR; A35104; A35104.
DR   PIR; S06943; S06943.
DR   RefSeq; NP_001020245.1; NM_001025074.1.
DR   RefSeq; NP_032771.1; NM_008745.2.
DR   UniGene; Mm.130054; -.
DR   ProteinModelPortal; P15209; -.
DR   SMR; P15209; 32-385, 529-811.
DR   DIP; DIP-5722N; -.
DR   IntAct; P15209; 1.
DR   STRING; P15209; -.
DR   PhosphoSite; P15209; -.
DR   PRIDE; P15209; -.
DR   Ensembl; ENSMUST00000078541; ENSMUSP00000077623; ENSMUSG00000055254.
DR   Ensembl; ENSMUST00000079828; ENSMUSP00000078757; ENSMUSG00000055254.
DR   Ensembl; ENSMUST00000109838; ENSMUSP00000105464; ENSMUSG00000055254.
DR   Ensembl; ENSMUST00000109839; ENSMUSP00000105465; ENSMUSG00000055254.
DR   Ensembl; ENSMUST00000109840; ENSMUSP00000105466; ENSMUSG00000055254.
DR   GeneID; 18212; -.
DR   KEGG; mmu:18212; -.
DR   UCSC; uc007qui.1; mouse.
DR   CTD; 18212; -.
DR   MGI; MGI:97384; Ntrk2.
DR   eggNOG; roNOG12558; -.
DR   GeneTree; ENSGT00590000082855; -.
DR   HOGENOM; HBG402948; -.
DR   HOVERGEN; HBG056735; -.
DR   InParanoid; P15209; -.
DR   OMA; KFVAYKA; -.
DR   OrthoDB; EOG4255S6; -.
DR   PhylomeDB; P15209; -.
DR   BRENDA; 2.7.10.1; 244.
DR   NextBio; 293608; -.
DR   ArrayExpress; P15209; -.
DR   Bgee; P15209; -.
DR   CleanEx; MM_NTRK2; -.
DR   Genevestigator; P15209; -.
DR   GermOnline; ENSMUSG00000055254; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005887; C:integral to plasma membrane; IEA:InterPro.
DR   GO; GO:0043195; C:terminal button; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:EC.
DR   GO; GO:0007631; P:feeding behavior; IMP:MGI.
DR   GO; GO:0014047; P:glutamate secretion; IPI:MGI.
DR   GO; GO:0042490; P:mechanoreceptor differentiation; IMP:MGI.
DR   GO; GO:0019222; P:regulation of metabolic process; IMP:MGI.
DR   GO; GO:0046548; P:retinal rod cell development; IMP:MGI.
DR   GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000372; LRR-contain_N.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR020455; Tyr_kin_neurotrophic_rcpt_2.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   InterPro; IPR020777; Tyr_prot_kinase_NGF_rcpt.
DR   InterPro; IPR002011; Tyr_prot_kinase_rcpt_2_CS.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF01462; LRRNT; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PRINTS; PR01939; NTKRECEPTOR.
DR   PRINTS; PR01941; NTKRECEPTOR2.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00013; LRRNT; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Developmental protein;
KW   Differentiation; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Kinase; Leucine-rich repeat; Membrane; Neurogenesis;
KW   Nucleotide-binding; Phosphoprotein; Receptor; Repeat; Signal;
KW   Transferase; Transmembrane; Transmembrane helix;
KW   Tyrosine-protein kinase.
FT   SIGNAL        1     31
FT   CHAIN        32    821       BDNF/NT-3 growth factors receptor.
FT                                /FTId=PRO_0000016728.
FT   TOPO_DOM     32    429       Extracellular (Potential).
FT   TRANSMEM    430    453       Helical; (Potential).
FT   TOPO_DOM    454    821       Cytoplasmic (Potential).
FT   REPEAT       72     93       LRR 1.
FT   REPEAT       96    117       LRR 2.
FT   DOMAIN      197    282       Ig-like C2-type 1.
FT   DOMAIN      301    365       Ig-like C2-type 2.
FT   DOMAIN      537    806       Protein kinase.
FT   NP_BIND     543    551       ATP (By similarity).
FT   ACT_SITE    675    675       Proton acceptor (By similarity).
FT   BINDING     571    571       ATP (By similarity).
FT   SITE        515    515       Interaction with SHC1 (By similarity).
FT   SITE        816    816       Interaction with PLC-gamma-1 (By
FT                                similarity).
FT   MOD_RES     515    515       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     701    701       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     705    705       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     706    706       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     816    816       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   CARBOHYD     67     67       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     95     95       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    121    121       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    178    178       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    205    205       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    241    241       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    254    254       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    280    280       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    325    325       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    338    338       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    411    411       N-linked (GlcNAc...) (Potential).
FT   DISULFID     32     38       By similarity.
FT   DISULFID     36     45       By similarity.
FT   DISULFID    152    176       By similarity.
FT   DISULFID    154    194       By similarity.
FT   DISULFID    218    266       By similarity.
FT   DISULFID    302    345       By similarity.
FT   VAR_SEQ      71     71       I -> M (in isoform L10).
FT                                /FTId=VSP_002905.
FT   VAR_SEQ      72    143       Missing (in isoform L10).
FT                                /FTId=VSP_002906.
FT   VAR_SEQ      72    120       Missing (in isoform L1).
FT                                /FTId=VSP_002907.
FT   VAR_SEQ     466    476       PASVISNDDDS -> FVLFHKIPLDG (in isoform
FT                                GP95-TRKB).
FT                                /FTId=VSP_002908.
FT   VAR_SEQ     477    821       Missing (in isoform GP95-TRKB).
FT                                /FTId=VSP_002909.
SQ   SEQUENCE   821 AA;  92133 MW;  50E08D5FF86D8F30 CRC64;
     MSPWLKWHGP AMARLWGLCL LVLGFWRASL ACPTSCKCSS ARIWCTEPSP GIVAFPRLEP
     NSVDPENITE ILIANQKRLE IINEDDVEAY VGLRNLTIVD SGLKFVAYKA FLKNSNLRHI
     NFTRNKLTSL SRRHFRHLDL SDLILTGNPF TCSCDIMWLK TLQETKSSPD TQDLYCLNES
     SKNMPLANLQ IPNCGLPSAR LAAPNLTVEE GKSVTLSCSV GGDPLPTLYW DVGNLVSKHM
     NETSHTQGSL RITNISSDDS GKQISCVAEN LVGEDQDSVN LTVHFAPTIT FLESPTSDHH
     WCIPFTVRGN PKPALQWFYN GAILNESKYI CTKIHVTNHT EYHGCLQLDN PTHMNNGDYT
     LMAKNEYGKD ERQISAHFMG RPGVDYETNP NYPEVLYEDW TTPTDIGDTT NKSNEIPSTD
     VADQSNREHL SVYAVVVIAS VVGFCLLVML LLLKLARHSK FGMKGPASVI SNDDDSASPL
     HHISNGSNTP SSSEGGPDAV IIGMTKIPVI ENPQYFGITN SQLKPDTFVQ HIKRHNIVLK
     RELGEGAFGK VFLAECYNLC PEQDKILVAV KTLKDASDNA RKDFHREAEL LTNLQHEHIV
     KFYGVCVEGD PLIMVFEYMK HGDLNKFLRA HGPDAVLMAE GNPPTELTQS QMLHIAQQIA
     AGMVYLASQH FVHRDLATRN CLVGENLLVK IGDFGMSRDV YSTDYYRVGG HTMLPIRWMP
     PESIMYRKFT TESDVWSLGV VLWEIFTYGK QPWYQLSNNE VIECITQGRV LQRPRTCPQE
     VYELMLGCWQ REPHTRKNIK SIHTLLQNLA KASPVYLDIL G
//
ID   INGR1_MOUSE             Reviewed;         477 AA.
AC   P15261;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 2.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Interferon gamma receptor 1;
DE            Short=IFN-gamma receptor 1;
DE            Short=IFN-gamma-R1;
DE   AltName: CD_antigen=CD119;
DE   Flags: Precursor;
GN   Name=Ifngr1; Synonyms=Ifngr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90083245; PubMed=2531896; DOI=10.1073/pnas.86.23.9248;
RA   Munro S., Maniatis T.;
RT   "Expression cloning of the murine interferon gamma receptor cDNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:9248-9252(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90046824; PubMed=2530582; DOI=10.1073/pnas.86.21.8497;
RA   Gray P.W., Leong S., Fennie E.H., Farrar M.A., Pingel J.T.,
RA   Fernandez-Luna J., Schreiber R.D.;
RT   "Cloning and expression of the cDNA for the murine interferon gamma
RT   receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:8497-8501(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90099370; PubMed=2532365; DOI=10.1073/pnas.86.24.9901;
RA   Hemmi S., Peghini P., Metzler M., Merlin G., Dembic Z., Aguet M.;
RT   "Cloning of murine interferon gamma receptor cDNA: expression in human
RT   cells mediates high-affinity binding but is not sufficient to confer
RT   sensitivity to murine interferon gamma.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:9901-9905(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90036866; PubMed=2530216;
RA   Kumar C.S., Muthukumaran G., Frost L.J., Noe M., Ahn Y.H.,
RA   Mariano T.M., Pestka S.;
RT   "Molecular characterization of the murine interferon gamma receptor
RT   cDNA.";
RL   J. Biol. Chem. 264:17939-17946(1989).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90154099; PubMed=2137461;
RA   Cofano F., Moore S.K., Tanaka S., Yuhki N., Landolfo S., Appella E.;
RT   "Affinity purification, peptide analysis, and cDNA sequence of the
RT   mouse interferon gamma receptor.";
RL   J. Biol. Chem. 265:4064-4071(1990).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RX   MEDLINE=95197006; PubMed=7890167; DOI=10.1016/0378-1119(94)00869-T;
RA   Raval P., Obici S., Russell S.W., Murphy W.J.;
RT   "Characterization of the 5' flanking region and gene encoding the
RT   mouse interferon-gamma receptor.";
RL   Gene 154:219-223(1995).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370 AND THR-373, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Receptor for interferon gamma. Two receptors bind one
CC       interferon gamma dimer.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- PTM: Phosphorylated at Ser/Thr residues.
CC   -!- SIMILARITY: Belongs to the type II cytokine receptor family.
CC   -!- SIMILARITY: Contains 2 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 2 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA37895.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; M28995; AAA37895.1; ALT_INIT; mRNA.
DR   EMBL; M26711; AAA37896.1; -; mRNA.
DR   EMBL; M28233; AAA37898.1; -; mRNA.
DR   EMBL; M25764; AAA39177.1; -; mRNA.
DR   EMBL; J05265; AAA39178.1; -; mRNA.
DR   EMBL; U05960; AAA80980.1; -; Genomic_DNA.
DR   IPI; IPI00323231; -.
DR   PIR; A34368; A34368.
DR   RefSeq; NP_034641.1; NM_010511.2.
DR   UniGene; Mm.549; -.
DR   ProteinModelPortal; P15261; -.
DR   SMR; P15261; 38-248.
DR   STRING; P15261; -.
DR   PRIDE; P15261; -.
DR   Ensembl; ENSMUST00000020188; ENSMUSP00000020188; ENSMUSG00000020009.
DR   GeneID; 15979; -.
DR   KEGG; mmu:15979; -.
DR   CTD; 15979; -.
DR   MGI; MGI:107655; Ifngr1.
DR   eggNOG; roNOG17254; -.
DR   HOGENOM; HBG124982; -.
DR   HOVERGEN; HBG052128; -.
DR   InParanoid; P15261; -.
DR   OrthoDB; EOG4P5K9K; -.
DR   ArrayExpress; P15261; -.
DR   Bgee; P15261; -.
DR   CleanEx; MM_IFNGR1; -.
DR   Genevestigator; P15261; -.
DR   GermOnline; ENSMUSG00000020009; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019955; F:cytokine binding; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007596; P:blood coagulation; IEA:InterPro.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR021126; Interferon_gamma_pox/mammal.
DR   InterPro; IPR008355; Interferon_gamma_rcpt_asu.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   PANTHER; PTHR20859:SF5; IFNR_rcpt_alpha; 1.
DR   Pfam; PF07140; IFNGR1; 1.
DR   PRINTS; PR01777; INTERFERONGR.
DR   SUPFAM; SSF49265; FN_III-like; 2.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW   Phosphoprotein; Receptor; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     22
FT   CHAIN        23    477       Interferon gamma receptor 1.
FT                                /FTId=PRO_0000011010.
FT   TOPO_DOM     23    253       Extracellular (Potential).
FT   TRANSMEM    254    277       Helical; (Potential).
FT   TOPO_DOM    278    477       Cytoplasmic (Potential).
FT   MOD_RES     370    370       Phosphoserine.
FT   MOD_RES     373    373       Phosphothreonine.
FT   CARBOHYD     61     61       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     85     85       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    186    186       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    204    204       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    211    211       N-linked (GlcNAc...) (Potential).
FT   DISULFID     83     91       By similarity.
FT   DISULFID    128    174       By similarity.
FT   DISULFID    203    208       By similarity.
FT   DISULFID    222    243       By similarity.
FT   CONFLICT     95     95       G -> E (in Ref. 2 and 3).
SQ   SEQUENCE   477 AA;  52271 MW;  A1FC66E9BAA0B20A CRC64;
     MGPQAAAGRM ILLVVLMLSA KVGSGALTST EDPEPPSVPV PTNVLIKSYN LNPVVCWEYQ
     NMSQTPIFTV QVKVYSGSWT DSCTNISDHC CNIYGQIMYP DVSAWARVKA KVGQKESDYA
     RSKEFLMCLK GKVGPPGLEI RRKKEEQLSV LVFHPEVVVN GESQGTMFGD GSTCYTFDYT
     VYVEHNRSGE ILHTKHTVEK EECNETLCEL NISVSTLDSR YCISVDGISS FWQVRTEKSK
     DVCIPPFHDD RKDSIWILVV APLTVFTVVI LVFAYWYTKK NSFKRKSIML PKSLLSVVKS
     ATLETKPESK YSLVTPHQPA VLESETVICE EPLSTVTAPD SPEAAEQEEL SKETKALEAG
     GSTSAMTPDS PPTPTQRRSF SLLSSNQSGP CSLTAYHSRN GSDSGLVGSG SSISDLESLP
     NNNSETKMAE HDPPPVRKAP MASGYDKPHM LVDVLVDVGG KESLMGYRLT GEAQELS
//
ID   PERI_MOUSE              Reviewed;         475 AA.
AC   P15331; O35688; O35689;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Peripherin;
GN   Name=Prph; Synonyms=Prph1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=93192779; PubMed=1294287;
RA   Karpov V., Landon F., Djabali K., Gros F., Portier M.M.;
RT   "Structure of the mouse gene encoding peripherin: a neuronal
RT   intermediate filament protein.";
RL   Biol. Cell 76:43-48(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5G).
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 70-475, AND ALTERNATIVE SPLICING.
RX   MEDLINE=89356645; PubMed=2767051;
RA   Landon F., Lemonnier M., Benarous R., Huc C., Fiszman M., Gros F.,
RA   Portier M.M.;
RT   "Multiple mRNAs encode peripherin, a neuronal intermediate filament
RT   protein.";
RL   EMBO J. 8:1719-1726(1989).
RN   [4]
RP   PROTEIN SEQUENCE OF 411-424.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
CC   -!- FUNCTION: Class-III neuronal intermediate filament protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=5g;
CC         IsoId=P15331-1; Sequence=Displayed;
CC       Name=3u;
CC         IsoId=P15331-2; Sequence=VSP_002466;
CC       Name=5b;
CC         IsoId=P15331-3; Sequence=VSP_002467;
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
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DR   EMBL; X15475; CAA33502.1; -; mRNA.
DR   EMBL; BC046291; AAH46291.1; -; mRNA.
DR   EMBL; X59840; CAA42499.1; -; Genomic_DNA.
DR   EMBL; X59840; CAA42500.1; -; Genomic_DNA.
DR   EMBL; X59840; CAA42501.1; -; Genomic_DNA.
DR   IPI; IPI00129527; -.
DR   IPI; IPI00230444; -.
DR   IPI; IPI00230445; -.
DR   PIR; S14887; S14887.
DR   UniGene; Mm.2477; -.
DR   ProteinModelPortal; P15331; -.
DR   SMR; P15331; 99-135, 139-246, 263-406.
DR   STRING; P15331; -.
DR   PhosphoSite; P15331; -.
DR   UCD-2DPAGE; P15331; -.
DR   PRIDE; P15331; -.
DR   Ensembl; ENSMUST00000024249; ENSMUSP00000024249; ENSMUSG00000023484.
DR   Ensembl; ENSMUST00000047104; ENSMUSP00000049303; ENSMUSG00000023484.
DR   UCSC; uc007xon.1; mouse.
DR   UCSC; uc007xoo.1; mouse.
DR   MGI; MGI:97774; Prph.
DR   eggNOG; roNOG11948; -.
DR   GeneTree; ENSGT00560000076592; -.
DR   HOVERGEN; HBG013015; -.
DR   OrthoDB; EOG4JWVDP; -.
DR   ArrayExpress; P15331; -.
DR   Bgee; P15331; -.
DR   CleanEx; MM_PRPH; -.
DR   Genevestigator; P15331; -.
DR   GermOnline; ENSMUSG00000023484; Mus musculus.
DR   GO; GO:0044299; C:C-fiber; IDA:MGI.
DR   GO; GO:0005883; C:neurofilament; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0045104; P:intermediate filament cytoskeleton organization; IDA:MGI.
DR   InterPro; IPR016044; F.
DR   InterPro; IPR001664; IF.
DR   InterPro; IPR006821; Intermed_filament_DNA-bd.
DR   InterPro; IPR018039; Intermediate_filament_CS.
DR   InterPro; IPR002957; Keratin_I.
DR   PANTHER; PTHR23239; IF; 1.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF04732; Filament_head; 1.
DR   PRINTS; PR01248; TYPE1KERATIN.
DR   PROSITE; PS00226; IF; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Direct protein sequencing;
KW   Intermediate filament; Nitration; Phosphoprotein.
FT   CHAIN         1    475       Peripherin.
FT                                /FTId=PRO_0000063780.
FT   REGION        1    103       Head.
FT   REGION      104    409       Rod.
FT   REGION      104    136       Coil 1A.
FT   REGION      137    147       Linker 1.
FT   REGION      148    243       Coil 1B.
FT   REGION      244    266       Linker 2.
FT   REGION      267    409       Coil 2.
FT   REGION      410    475       Tail.
FT   MOD_RES      24     24       Nitrated tyrosine (By similarity).
FT   MOD_RES     383    383       Nitrated tyrosine (By similarity).
FT   MOD_RES     475    475       Phosphotyrosine (By similarity).
FT   VAR_SEQ     294    294       K -> KVREHWGNPGGPRVGRHWEWRCASQPGLSATAQ
FT                                (in isoform 3u).
FT                                /FTId=VSP_002466.
FT   VAR_SEQ     454    475       KVVTESQKEQHSDLDKSSIHSY -> LLRPQPEL (in
FT                                isoform 5b).
FT                                /FTId=VSP_002467.
SQ   SEQUENCE   475 AA;  54268 MW;  777300B08A312953 CRC64;
     MPSSASMSHH HSSGLRSSIS STSYRRTFGP PPSLSPGAFS YSSSSRFSSS RLLGSGSPSS
     SARLGSFRAP RAGALRLPSE RLDFSMAEAL NQEFLATRSN EKQELQELND RFANFIEKVR
     FLEQQNAALR GELSQARGQE PARADQLCQQ ELRELRRELE LLGRERDRVQ VERDGLAEDL
     AALKQRLEEE TRKREDAEHN LVLFRKDVDD ATLSRLELER KIESLMDEIE FLKKLHEEEL
     RDLQVSVESQ QVQQVEVEAT VKPELTAALR DIRAQYENIA AKNLQEAEEW YKSKYADLSD
     AANRNHEALR QAKQEMNESR RQIQSLTCEV DGLRGTNEAL LRQLRELEEQ FALEAGGYQA
     GAARLEEELR QLKEEMARHL REYQELLNVK MALDIEIATY RKLLEGEESR ISVPVHSFAS
     LSLKTTVPEM EPLQDSHSKK MVLIRTIETR DGEKVVTESQ KEQHSDLDKS SIHSY
//
ID   CD44_MOUSE              Reviewed;         778 AA.
AC   P15379; Q05732; Q61395; Q62060; Q62061; Q62062; Q62063; Q62408;
AC   Q62409; Q64296; Q99J14; Q9QYX8;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   30-APR-2003, sequence version 3.
DT   08-MAR-2011, entry version 124.
DE   RecName: Full=CD44 antigen;
DE   AltName: Full=Extracellular matrix receptor III;
DE            Short=ECMR-III;
DE   AltName: Full=GP90 lymphocyte homing/adhesion receptor;
DE   AltName: Full=HUTCH-I;
DE   AltName: Full=Hermes antigen;
DE   AltName: Full=Hyaluronate receptor;
DE   AltName: Full=Lymphocyte antigen 24;
DE            Short=Ly-24;
DE   AltName: Full=Phagocytic glycoprotein 1;
DE            Short=PGP-1;
DE   AltName: Full=Phagocytic glycoprotein I;
DE            Short=PGP-I;
DE   AltName: CD_antigen=CD44;
DE   Flags: Precursor;
GN   Name=Cd44; Synonyms=Ly-24;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 6; 7 AND 12).
RC   STRAIN=DBA/2; TISSUE=Lung;
RX   MEDLINE=93107170; PubMed=1469058; DOI=10.1083/jcb.119.6.1711;
RA   He Q., Lesley J., Hyman R., Ishihara K., Kincade P.W.;
RT   "Molecular isoforms of murine CD44 and evidence that the membrane
RT   proximal domain is not critical for hyaluronate recognition.";
RL   J. Cell Biol. 119:1711-1719(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 13).
RX   MEDLINE=90038499; PubMed=2681416;
RA   Zhou D.F.H., Ding J.F., Picker L.J., Bargatze R.F., Butcher E.C.,
RA   Goeddel D.V.;
RT   "Molecular cloning and expression of Pgp-1. The mouse homolog of the
RT   human H-CAM (Hermes) lymphocyte homing receptor.";
RL   J. Immunol. 143:3390-3395(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 13).
RX   MEDLINE=90046829; PubMed=2682651; DOI=10.1073/pnas.86.21.8521;
RA   Nottenburg C., Rees G., St John T.;
RT   "Isolation of mouse CD44 cDNA: structural features are distinct from
RT   the primate cDNA.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:8521-8525(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 1).
RX   MEDLINE=20318634; PubMed=10859330; DOI=10.1084/jem.191.12.2053;
RA   Wittig B.M., Johansson B., Zoeller M., Schwaerzler C., Guenthert U.;
RT   "Abrogation of experimental colitis correlates with increased
RT   apoptosis in mice deficient for CD44 variant exon 7 (CD44v7).";
RL   J. Exp. Med. 191:2053-2064(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 13).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 13).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-778 (ISOFORM 13).
RX   MEDLINE=90094420; PubMed=2403559;
RA   Wolffe E.J., Gause W.C., Pelfrey C.M., Holland S.M., Steinberg A.D.,
RA   August J.T.;
RT   "The cDNA sequence of mouse Pgp-1 and homology to human CD44 cell
RT   surface antigen and proteoglycan core/link proteins.";
RL   J. Biol. Chem. 265:341-347(1990).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 224-637 (ISOFORMS 1; 2; 3; 4; 5; 6; 7
RP   AND 8).
RC   STRAIN=GR;
RX   MEDLINE=93219085; PubMed=8464707; DOI=10.1093/nar/21.5.1225;
RA   Toelg C., Hofmann M., Herrlich P., Ponta H.;
RT   "Splicing choice from ten variant exons establishes CD44
RT   variability.";
RL   Nucleic Acids Res. 21:1225-1229(1993).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 224-637 (ISOFORM 9).
RC   STRAIN=BALB/c;
RX   MEDLINE=93286043; PubMed=8509359;
RA   Screaton G.R., Bell M.V., Bell J.I., Jackson D.G.;
RT   "The identification of a new alternative exon with highly restricted
RT   tissue expression in transcripts encoding the mouse Pgp-1 (CD44)
RT   homing receptor. Comparison of all 10 variable exons between mouse,
RT   human, and rat.";
RL   J. Biol. Chem. 268:12235-12238(1993).
RN   [10]
RP   PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 10 AND 11).
RC   STRAIN=Swiss Webster;
RX   MEDLINE=96355396; PubMed=8702806; DOI=10.1074/jbc.271.34.20603;
RA   Yu Q., Toole B.P.;
RT   "A new alternatively spliced exon between v9 and v10 provides a
RT   molecular basis for synthesis of soluble CD44.";
RL   J. Biol. Chem. 271:20603-20607(1996).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-726; SER-733 AND
RP   SER-742, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-726; SER-733 AND
RP   SER-771, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Main cell surface receptor for hyaluronate. Adhesion to
CC       mucosal high endothelial venule and to types I and VI collagen.
CC       Probably involved in matrix adhesion, lymphocyte activation and
CC       lymph node homing.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=13;
CC       Name=1;
CC         IsoId=P15379-14; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P15379-7; Sequence=VSP_007329;
CC       Name=3;
CC         IsoId=P15379-8; Sequence=VSP_007330;
CC       Name=4; Synonyms=M2;
CC         IsoId=P15379-4; Sequence=VSP_007331;
CC       Name=5;
CC         IsoId=P15379-9; Sequence=VSP_007332;
CC       Name=6; Synonyms=M3;
CC         IsoId=P15379-5; Sequence=VSP_005326;
CC       Name=7; Synonyms=M4;
CC         IsoId=P15379-6; Sequence=VSP_005327;
CC       Name=8;
CC         IsoId=P15379-10; Sequence=VSP_007330, VSP_007334;
CC       Name=9;
CC         IsoId=P15379-11; Sequence=VSP_007332, VSP_007335;
CC       Name=10;
CC         IsoId=P15379-12; Sequence=VSP_007336, VSP_007337;
CC       Name=11;
CC         IsoId=P15379-13; Sequence=VSP_007338, VSP_007339;
CC       Name=12; Synonyms=M1;
CC         IsoId=P15379-3; Sequence=VSP_005328;
CC       Name=13; Synonyms=M0;
CC         IsoId=P15379-2; Sequence=VSP_005329, VSP_007333;
CC   -!- PTM: N-glycosylated (By similarity).
CC   -!- PTM: O-glycosylated; contains chondroitin sulfate glycans which
CC       can be more or less sulfated (By similarity).
CC   -!- PTM: Phosphorylated; activation of PKC results in the
CC       dephosphorylation of Ser-742 (constitutive phosphorylation site),
CC       and the phosphorylation of Ser-708 (By similarity).
CC   -!- POLYMORPHISM: Two allelic forms of this glycoprotein, PGP-1.1 and
CC       PGP-1.2, have been reported. The expressed product is PGP-1.1 (Ly-
CC       24.1).
CC   -!- SIMILARITY: Contains 1 Link domain.
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DR   EMBL; X66084; CAA46883.1; -; mRNA.
DR   EMBL; X66083; CAA46882.1; -; mRNA.
DR   EMBL; X66082; CAA46881.1; -; mRNA.
DR   EMBL; X66081; CAA46880.1; -; mRNA.
DR   EMBL; M30655; AAA39922.1; -; mRNA.
DR   EMBL; M27129; AAA37406.1; -; mRNA.
DR   EMBL; M27130; AAA37407.1; -; mRNA.
DR   EMBL; AJ251594; CAB61888.1; -; mRNA.
DR   EMBL; BC005676; AAH05676.1; -; mRNA.
DR   EMBL; AK045226; BAC32269.1; -; mRNA.
DR   EMBL; J05163; AAA39923.1; -; mRNA.
DR   EMBL; X69724; CAA49380.1; -; mRNA.
DR   EMBL; L13611; AAA37145.1; -; mRNA.
DR   EMBL; U57610; AAC52804.1; -; mRNA.
DR   EMBL; U57611; AAB08756.1; -; mRNA.
DR   EMBL; U57612; AAC52805.1; -; Genomic_DNA.
DR   EMBL; U57612; AAC52806.1; -; Genomic_DNA.
DR   IPI; IPI00223770; -.
DR   IPI; IPI00223772; -.
DR   IPI; IPI00223773; -.
DR   IPI; IPI00265503; -.
DR   IPI; IPI00265504; -.
DR   IPI; IPI00265505; -.
DR   IPI; IPI00266152; -.
DR   IPI; IPI00266154; -.
DR   IPI; IPI00266155; -.
DR   IPI; IPI00410802; -.
DR   IPI; IPI00720073; -.
DR   IPI; IPI00828592; -.
DR   IPI; IPI00828623; -.
DR   PIR; A34424; A34424.
DR   PIR; A37009; A37009.
DR   PIR; B44355; B44355.
DR   PIR; D44355; D44355.
DR   PIR; S30397; S30397.
DR   RefSeq; NP_001034240.1; NM_001039151.1.
DR   RefSeq; NP_001171256.1; NM_001177785.1.
DR   RefSeq; NP_001171257.1; NM_001177786.1.
DR   RefSeq; NP_001171258.1; NM_001177787.1.
DR   RefSeq; NP_033981.2; NM_009851.2.
DR   UniGene; Mm.423621; -.
DR   PDB; 2JCP; X-ray; 1.30 A; A=23-174.
DR   PDB; 2JCQ; X-ray; 1.25 A; A=23-174.
DR   PDB; 2JCR; X-ray; 2.00 A; A=23-174.
DR   PDB; 2ZPY; X-ray; 2.10 A; B=708-727.
DR   PDBsum; 2JCP; -.
DR   PDBsum; 2JCQ; -.
DR   PDBsum; 2JCR; -.
DR   PDBsum; 2ZPY; -.
DR   ProteinModelPortal; P15379; -.
DR   SMR; P15379; 23-171.
DR   DIP; DIP-29095N; -.
DR   STRING; P15379; -.
DR   PhosphoSite; P15379; -.
DR   PRIDE; P15379; -.
DR   Ensembl; ENSMUST00000005218; ENSMUSP00000005218; ENSMUSG00000005087.
DR   Ensembl; ENSMUST00000099673; ENSMUSP00000097265; ENSMUSG00000005087.
DR   Ensembl; ENSMUST00000111189; ENSMUSP00000106820; ENSMUSG00000005087.
DR   Ensembl; ENSMUST00000111194; ENSMUSP00000106825; ENSMUSG00000005087.
DR   Ensembl; ENSMUST00000111195; ENSMUSP00000106826; ENSMUSG00000005087.
DR   Ensembl; ENSMUST00000111196; ENSMUSP00000106827; ENSMUSG00000005087.
DR   Ensembl; ENSMUST00000111197; ENSMUSP00000106828; ENSMUSG00000005087.
DR   Ensembl; ENSMUST00000111198; ENSMUSP00000106829; ENSMUSG00000005087.
DR   Ensembl; ENSMUST00000111199; ENSMUSP00000106830; ENSMUSG00000005087.
DR   Ensembl; ENSMUST00000111200; ENSMUSP00000106831; ENSMUSG00000005087.
DR   GeneID; 12505; -.
DR   KEGG; mmu:12505; -.
DR   UCSC; uc008lie.1; mouse.
DR   UCSC; uc008lih.1; mouse.
DR   UCSC; uc008lii.1; mouse.
DR   UCSC; uc008lij.1; mouse.
DR   CTD; 12505; -.
DR   MGI; MGI:88338; Cd44.
DR   GeneTree; ENSGT00530000063822; -.
DR   HOVERGEN; HBG003850; -.
DR   InParanoid; P15379; -.
DR   OrthoDB; EOG4PZJ66; -.
DR   NextBio; 281466; -.
DR   ArrayExpress; P15379; -.
DR   Bgee; P15379; -.
DR   CleanEx; MM_CD44; -.
DR   Genevestigator; P15379; -.
DR   GermOnline; ENSMUSG00000005087; Mus musculus.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005540; F:hyaluronic acid binding; IDA:MGI.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0060442; P:branching involved in prostate gland morphogenesis; IMP:MGI.
DR   GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI.
DR   GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR   GO; GO:0071445; P:cellular response to protein stimulus; IDA:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptosis; IMP:BHF-UCL.
DR   GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:BHF-UCL.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:BHF-UCL.
DR   GO; GO:0010628; P:positive regulation of gene expression; IGI:MGI.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:BHF-UCL.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IDA:MGI.
DR   GO; GO:0002246; P:wound healing involved in inflammatory response; IMP:MGI.
DR   InterPro; IPR016186; C-type_lectin-like.
DR   InterPro; IPR016187; C-type_lectin_fold.
DR   InterPro; IPR001231; CD44_antigen.
DR   InterPro; IPR000538; Link.
DR   Gene3D; G3DSA:3.10.100.10; C-type_lectin-like; 1.
DR   Pfam; PF00193; Xlink; 1.
DR   PRINTS; PR00658; CD44.
DR   PRINTS; PR01265; LINKMODULE.
DR   SMART; SM00445; LINK; 1.
DR   SUPFAM; SSF56436; C-type_lectin_fold; 1.
DR   PROSITE; PS01241; LINK_1; 1.
DR   PROSITE; PS50963; LINK_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell adhesion; Disulfide bond;
KW   Glycoprotein; Membrane; Phosphoprotein; Proteoglycan;
KW   Pyrrolidone carboxylic acid; Receptor; Signal; Sulfation;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     22       By similarity.
FT   CHAIN        23    778       CD44 antigen.
FT                                /FTId=PRO_0000026689.
FT   TOPO_DOM     23    685       Extracellular (Potential).
FT   TRANSMEM    686    706       Helical; (Potential).
FT   TOPO_DOM    707    778       Cytoplasmic (Potential).
FT   DOMAIN       34    123       Link.
FT   REGION      227    685       Stem.
FT   COMPBIAS    153    161       Arg/Lys-rich (basic).
FT   MOD_RES      23     23       Pyrrolidone carboxylic acid (By
FT                                similarity).
FT   MOD_RES     410    410       Sulfotyrosine (By similarity).
FT   MOD_RES     708    708       Phosphoserine; by PKC (By similarity).
FT   MOD_RES     726    726       Phosphothreonine.
FT   MOD_RES     733    733       Phosphoserine.
FT   MOD_RES     742    742       Phosphoserine.
FT   MOD_RES     756    756       Phosphothreonine (By similarity).
FT   MOD_RES     771    771       Phosphoserine.
FT   CARBOHYD     27     27       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     59     59       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    102    102       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    113    113       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    123    123       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    368    368       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    425    425       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    529    529       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    545    545       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    603    603       N-linked (GlcNAc...) (Potential).
FT   DISULFID     55    121       By similarity.
FT   DISULFID     79     99       By similarity.
FT   VAR_SEQ     223    637       Missing (in isoform 13).
FT                                /FTId=VSP_005329.
FT   VAR_SEQ     223    539       Missing (in isoform 12).
FT                                /FTId=VSP_005328.
FT   VAR_SEQ     223    504       Missing (in isoform 7).
FT                                /FTId=VSP_005327.
FT   VAR_SEQ     223    424       Missing (in isoform 6).
FT                                /FTId=VSP_005326.
FT   VAR_SEQ     223    383       Missing (in isoform 5 and isoform 9).
FT                                /FTId=VSP_007332.
FT   VAR_SEQ     223    346       Missing (in isoform 4).
FT                                /FTId=VSP_007331.
FT   VAR_SEQ     223    303       Missing (in isoform 3 and isoform 8).
FT                                /FTId=VSP_007330.
FT   VAR_SEQ     223    264       Missing (in isoform 2).
FT                                /FTId=VSP_007329.
FT   VAR_SEQ     424    504       Missing (in isoform 8).
FT                                /FTId=VSP_007334.
FT   VAR_SEQ     463    504       Missing (in isoform 9).
FT                                /FTId=VSP_007335.
FT   VAR_SEQ     569    592       TKSSAKDARRGGSLPTDTTTSVEG -> VRIIKSNWLLSRN
FT                                QDVMGVSGGGC (in isoform 11).
FT                                /FTId=VSP_007338.
FT   VAR_SEQ     569    580       TKSSAKDARRGG -> VCLVVVADFSAL (in isoform
FT                                10).
FT                                /FTId=VSP_007336.
FT   VAR_SEQ     581    778       Missing (in isoform 10).
FT                                /FTId=VSP_007337.
FT   VAR_SEQ     593    778       Missing (in isoform 11).
FT                                /FTId=VSP_007339.
FT   VAR_SEQ     638    638       G -> R (in isoform 13).
FT                                /FTId=VSP_007333.
FT   VARIANT      21     21       H -> HPH (in Ly-24.2).
FT   VARIANT     194    194       G -> S (in Ly-24.2).
FT   CONFLICT    326    326       T -> K (in Ref. 4 and 9).
FT   CONFLICT    348    348       T -> S (in Ref. 9).
FT   CONFLICT    559    559       Y -> H (in Ref. 4, 8 and 9).
FT   CONFLICT    572    572       S -> G (in Ref. 4, 8 and 9).
FT   CONFLICT    639    639       D -> RD (in Ref. 7).
FT   STRAND       23     28
FT   STRAND       35     40
FT   HELIX        48     57
FT   HELIX        65     73
FT   STRAND       85     94
FT   HELIX       100    102
FT   STRAND      105    108
FT   STRAND      117    122
FT   STRAND      128    131
FT   STRAND      142    152
FT   STRAND      157    163
FT   HELIX       168    170
SQ   SEQUENCE   778 AA;  85617 MW;  BD2C073250F6C956 CRC64;
     MDKFWWHTAW GLCLLQLSLA HQQIDLNVTC RYAGVFHVEK NGRYSISRTE AADLCQAFNS
     TLPTMDQMKL ALSKGFETCR YGFIEGNVVI PRIHPNAICA ANHTGVYILV TSNTSHYDTY
     CFNASAPPEE DCTSVTDLPN SFDGPVTITI VNRDGTRYSK KGEYRTHQED IDASNIIDDD
     VSSGSTIEKS TPEGYILHTY LPTEQPTGDQ DDSFFIRSTL ATIASTVHSK SHAAAQKQNN
     WIWSWFGNSQ STTQTQEPTT SATTALMTTP ETPPKRQEAQ NWFSWLFQPS ESKSHLHTTT
     KMPGTESNTN PTGWEPNEEN EDETDTYPSF SGSGIDDDED FISSTIATTP RVSARTEDNQ
     DWTQWKPNHS NPEVLLQTTT RMADIDRIST SAHGENWTPE PQPPFNNHEY QDEEETPHAT
     STTPNSTAEA AATQQETWFQ NGWQGKNPPT PSEDSHVTEG TTASAHNNHP SQRITTQSQE
     DVSWTDFFDP ISHPMGQGHQ TESKDTDSSH STTLQPTAAP NTHLVEDLNR TGPLSVTTPQ
     SHSQNFSTLH GEPEEDENYP TTSILPSSTK SSAKDARRGG SLPTDTTTSV EGYTFQYPDT
     MENGTLFPVT PAKTEVFGET EVTLATDSNV NVDGSLPGDR DSSKDSRGSS RTVTHGSELA
     GHSSANQDSG VTTTSGPMRR PQIPEWLIIL ASLLALALIL AVCIAVNSRR RCGQKKKLVI
     NGGNGTVEDR KPSELNGEAS KSQEMVHLVN KEPSETPDQC MTADETRNLQ SVDMKIGV
//
ID   KCNC1_MOUSE             Reviewed;         511 AA.
AC   P15388;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   08-MAR-2011, entry version 104.
DE   RecName: Full=Potassium voltage-gated channel subfamily C member 1;
DE   AltName: Full=NGK2;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv3.1;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv4;
GN   Name=Kcnc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90092535; PubMed=2599109; DOI=10.1016/0014-5793(89)81488-7;
RA   Yokoyama S., Imoto K., Kawamura T., Higashida H., Iwabe N., Miyata T.,
RA   Numa S.;
RT   "Potassium channels from NG108-15 neuroblastoma-glioma hybrid cells.
RT   Primary structure and functional expression from cDNAs.";
RL   FEBS Lett. 259:37-42(1989).
CC   -!- FUNCTION: Mediates the voltage-dependent potassium ion
CC       permeability of excitable membranes. Assuming opened or closed
CC       conformations in response to the voltage difference across the
CC       membrane, the protein forms a potassium-selective channel through
CC       which potassium ions may pass in accordance with their
CC       electrochemical gradient.
CC   -!- SUBUNIT: Heteromultimer with KCNG3, KCNG4 and KCNV2 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=KV3.1;
CC         IsoId=P15388-1; Sequence=Displayed;
CC       Name=KV4;
CC         IsoId=P15388-2; Sequence=Not described;
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position.
CC   -!- DOMAIN: The tail may be important in modulation of channel
CC       activity and/or targeting of the channel to specific subcellular
CC       compartments.
CC   -!- SIMILARITY: Belongs to the potassium channel family. C (Shaw)
CC       (TC 1.A.1.2) subfamily. Kv3.1/KCNC1 sub-subfamily.
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DR   EMBL; Y07521; CAA68814.1; -; mRNA.
DR   IPI; IPI00129776; -.
DR   PIR; S07095; S07095.
DR   RefSeq; NP_032447.1; NM_008421.3.
DR   UniGene; Mm.249386; -.
DR   ProteinModelPortal; P15388; -.
DR   SMR; P15388; 4-446.
DR   STRING; P15388; -.
DR   PhosphoSite; P15388; -.
DR   PRIDE; P15388; -.
DR   Ensembl; ENSMUST00000025202; ENSMUSP00000025202; ENSMUSG00000058975.
DR   GeneID; 16502; -.
DR   KEGG; mmu:16502; -.
DR   UCSC; uc009gyo.1; mouse.
DR   CTD; 16502; -.
DR   MGI; MGI:96667; Kcnc1.
DR   eggNOG; roNOG09423; -.
DR   HOGENOM; HBG445693; -.
DR   HOVERGEN; HBG105862; -.
DR   InParanoid; P15388; -.
DR   OMA; SGGFWRR; -.
DR   OrthoDB; EOG4CRKZX; -.
DR   PhylomeDB; P15388; -.
DR   NextBio; 289827; -.
DR   ArrayExpress; P15388; -.
DR   Bgee; P15388; -.
DR   Genevestigator; P15388; -.
DR   GermOnline; ENSMUSG00000058975; Mus musculus.
DR   GO; GO:0030673; C:axolemma; IDA:MGI.
DR   GO; GO:0032590; C:dendrite membrane; IDA:MGI.
DR   GO; GO:0032809; C:neuronal cell body membrane; IDA:MGI.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003974; K_chnl_volt-dep_Kv3.
DR   InterPro; IPR005403; K_chnl_volt-dep_Kv3.1.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01581; KV31CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01498; SHAWCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Ion transport; Ionic channel;
KW   Membrane; Phosphoprotein; Potassium; Potassium channel;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN         1    511       Potassium voltage-gated channel subfamily
FT                                C member 1.
FT                                /FTId=PRO_0000054052.
FT   TOPO_DOM      1    190       Cytoplasmic (Potential).
FT   TRANSMEM    191    209       Helical; Name=Segment S1; (Potential).
FT   TRANSMEM    248    267       Helical; Name=Segment S2; (Potential).
FT   TOPO_DOM    268    276       Cytoplasmic (Potential).
FT   TRANSMEM    277    295       Helical; Name=Segment S3; (Potential).
FT   TRANSMEM    309    331       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TOPO_DOM    332    344       Cytoplasmic (Potential).
FT   TRANSMEM    345    366       Helical; Name=Segment S5; (Potential).
FT   TRANSMEM    415    436       Helical; Name=Segment S6; (Potential).
FT   TOPO_DOM    437    511       Cytoplasmic (Potential).
FT   MOTIF       400    405       Selectivity filter (By similarity).
FT   MOD_RES     188    188       Phosphotyrosine (By similarity).
FT   CARBOHYD    220    220       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    229    229       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   511 AA;  57928 MW;  50A939E8F7120F37 CRC64;
     MGQGDESERI VINVGGTRHQ TYRSTLRTLP GTRLAWLAEP DAHSHFDYDP RADEFFFDRH
     PGVFAHILNY YRTGKLHCPA DVCGPLYEEE LAFWGIDETD VEPCCWMTYR QHRDAEEALD
     SFGGAPLDNS ADDADADGPG DSGDGEDELE MTKRLALSDS PDGRPGGFWR RWQPRIWALF
     EDPYSSRYAR YVAFASLFFI LVSITTFCLE THERFNPIVN KTEIENVRNG TQVRYYREAE
     TEAFLTYIEG VCVVWFTFEF LMRVVFCPNK VEFIKNSLNI IDFVAILPFY LEVGLSGLSS
     KAAKDVLGFL RVVRFVRILR IFKLTRHFVG LRVLGHTLRA STNEFLLLII FLALGVLIFA
     TMIYYAERIG AQPNDPSASE HTHFKNIPIG FWWAVVTMTT LGYGDMYPQT WSGMLVGALC
     ALAGVLTIAM PVPVIVNNFG MYYSLAMAKQ KLPKKKKKHI PRPPQLGSPN YCKSVVNSPH
     HSTQSDTCPL AQEEILEINR AGRKPLRGMS I
//
ID   SPTB1_MOUSE             Reviewed;        2128 AA.
AC   P15508;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Spectrin beta chain, erythrocyte;
DE   AltName: Full=Beta-I spectrin;
GN   Name=Sptb; Synonyms=Spnb-1, Spnb1, Sptb1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94033578; PubMed=8219239;
RA   Bloom M.L., Birkenmeier C.S., Barker J.E.;
RT   "Complete nucleotide sequence of the murine erythroid beta-spectrin
RT   cDNA and tissue-specific expression in normal and jaundiced mice.";
RL   Blood 82:2906-2914(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1055-1290.
RX   MEDLINE=88001019; PubMed=3307952;
RA   Cioe L., Laurila P., Meo P., Krebs K., Goodman S., Curtis P.J.;
RT   "Cloning and nucleotide sequence of a mouse erythrocyte beta-spectrin
RT   cDNA.";
RL   Blood 70:915-920(1987).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-2105, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Spectrin is the major constituent of the cytoskeletal
CC       network underlying the erythrocyte plasma membrane. It associates
CC       with band 4.1 and actin to form the cytoskeletal superstructure of
CC       the erythrocyte plasma membrane.
CC   -!- SUBUNIT: Composed of nonhomologous chains, alpha and beta, which
CC       aggregate to form dimers, tetramers, and higher polymers.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell
CC       cortex.
CC   -!- MISCELLANEOUS: This complex is anchored to the cytoplasmic face of
CC       the plasma membrane via another protein, ankyrin, which binds to
CC       beta-spectrin and mediates the binding of the whole complex to a
CC       transmembrane protein band 3. The interaction of erythrocyte
CC       spectrin with other proteins through specific binding domains lead
CC       to the formation of an extensive subplasmalemmal meshwork which is
CC       thought to be responsible for the maintenance of the biconcave
CC       shape of human erythrocytes, for the regulation of plasma membrane
CC       components and for the maintenance of the lipid asymmetry of the
CC       plasma membrane.
CC   -!- SIMILARITY: Belongs to the spectrin family.
CC   -!- SIMILARITY: Contains 2 CH (calponin-homology) domains.
CC   -!- SIMILARITY: Contains 17 spectrin repeats.
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DR   EMBL; S66283; AAB28600.1; -; mRNA.
DR   EMBL; M18641; AAA40126.1; -; mRNA.
DR   IPI; IPI00131376; -.
DR   PIR; A45929; A45929.
DR   UniGene; Mm.32881; -.
DR   ProteinModelPortal; P15508; -.
DR   SMR; P15508; 45-281, 297-1265, 1373-2074.
DR   STRING; P15508; -.
DR   PhosphoSite; P15508; -.
DR   PRIDE; P15508; -.
DR   Ensembl; ENSMUST00000021458; ENSMUSP00000021458; ENSMUSG00000021061.
DR   UCSC; uc007nyp.1; mouse.
DR   MGI; MGI:98387; Spnb1.
DR   eggNOG; maNOG08733; -.
DR   HOVERGEN; HBG057912; -.
DR   InParanoid; P15508; -.
DR   OrthoDB; EOG4H9XJK; -.
DR   ArrayExpress; P15508; -.
DR   Bgee; P15508; -.
DR   CleanEx; MM_SPNB1; -.
DR   Genevestigator; P15508; -.
DR   GermOnline; ENSMUSG00000021061; Mus musculus.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0008091; C:spectrin; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR   GO; GO:0006779; P:porphyrin biosynthetic process; IMP:MGI.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR016343; Spectrin_bsu.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 2.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF00435; Spectrin; 16.
DR   PIRSF; PIRSF002297; Spectrin_beta_subunit; 1.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00150; SPEC; 17.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
PE   1: Evidence at protein level;
KW   Actin capping; Actin-binding; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW   Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   2128       Spectrin beta chain, erythrocyte.
FT                                /FTId=PRO_0000073460.
FT   DOMAIN        2    275       Actin-binding.
FT   DOMAIN       54    158       CH 1.
FT   DOMAIN      173    275       CH 2.
FT   REPEAT      276    384       Spectrin 1.
FT   REPEAT      385    490       Spectrin 2.
FT   REPEAT      491    599       Spectrin 3.
FT   REPEAT      600    705       Spectrin 4.
FT   REPEAT      706    810       Spectrin 5.
FT   REPEAT      811    916       Spectrin 6.
FT   REPEAT      917   1023       Spectrin 7.
FT   REPEAT     1024   1130       Spectrin 8.
FT   REPEAT     1131   1236       Spectrin 9.
FT   REPEAT     1237   1341       Spectrin 10.
FT   REPEAT     1342   1447       Spectrin 11.
FT   REPEAT     1448   1546       Spectrin 12.
FT   REPEAT     1547   1652       Spectrin 13.
FT   REPEAT     1653   1759       Spectrin 14.
FT   REPEAT     1760   1864       Spectrin 15.
FT   REPEAT     1865   1970       Spectrin 16.
FT   REPEAT     1971   2073       Spectrin 17.
FT   MOD_RES      36     36       Phosphoserine.
FT   MOD_RES    2064   2064       Phosphothreonine (By similarity).
FT   MOD_RES    2105   2105       Phosphoserine.
SQ   SEQUENCE   2128 AA;  245250 MW;  10E576111106DFE1 CRC64;
     MTSATEFENV GNQPPFSRIN ARWDAPDDEL DNDNSSARLF ERSRIKALAD EREVVQKKTF
     TKWVNSHLAR VSCRISDLYK DLRDGRMLIK LLEVLSGEML PRPTKGKMRI HCLENVDKAL
     QFLKEQRVHL ENMGSHDIVD GNHRLVLGLI WTIILRFQIQ DIVVQTQEGR EQRSAKDALL
     LWCQMKTAGY PHVNVTNFTS SWKDGLAFNA LIHKHRPDLI DFDKLKDSNA RHNLEHAFDV
     AERQLGIIPL LDPEDVFTEN PDEKSIITYV VAFYHYFSKM KVLAVEGKRV GKVIDHAIET
     EKMIEKYSGL ASDLLTWIEQ TISVLNSRKF ANSLSGVQQQ LQAFSTYRTV EKPPKFQEKG
     NLEVLLFTIQ SRMRANNQKV YTPHDGKLVS DINRAWESLE EAEYQRELAL RSELIRQEFD
     RKAAMRETWL NENQRLVTQD NFGYDLAAVE AAKKKHEAIE TDTAAYEERV KALEDLAQEL
     EKENYHDQKR IIARKDNILR LWSYLQELLR SRRQRLEATL ALQKLFQDML HSIDWMDEIK
     AHILSAEFGK HLLEVEDLLQ KHKLMEADIA IQGDKVKAIT AATLQFAEGK GYQPCDPQVI
     QDRVSHLEQC FSELSNMAAG RKAQLEQSKR LWKFFWEMDE AESWIKEKEQ IYSSLDYGKD
     LTSVLILQRK HKAFEDELRG LDAHLKQIFQ EADDMVAQKQ FGHPQIETRV KEVSAQWDHL
     KELAAFRKKD LQDAENFFQF QGDADDLKAW LQDAHRLLSG EDVGQDEGAT RALGKKHKEF
     LEELEESRGV MEHLEHQAQG FPEEFRDSPD VTNRLQALRK LYQQVLTQAE LRGHKLQEAL
     DLYTVFGESD ACELWMTEKG KWLDQMDIPN TLEDLEVVQH RFDILDQEMK TLMAQIDGVN
     LAANNLVESG HPRSGEVKQY QDRLNKRWQA FQAVVSEQRE AVDSALRVNN YCVDCEETSK
     WIMDKTKVVE STKDLGQDLA GVIAIQRKLS GLERDVLAIR DRVSALERES QYLMESHPEQ
     KEDIGQRQAD VEKLWKGLQD ALQGQELSLG EASKLQAFLQ DLDDFKAWLS MAQKAVASED
     MPESLPEAEQ LLQQHAAIKE EIDAHRDDYH RVKASGEKVI EGQTDPDYQL LGQRLEGLDT
     DWDALRRMWE SRGNTLTQCL GFQEFQKDAK QAEAILSNQE YTLAHLEPPD SLAAAEAGIR
     KFEDFLVSME NNRDKILSPV DSGNKLVAEG NLYSNKIMEK VQLIEDRHKK NNEKAQEATV
     LLKDNLELQN FLQNCKELTL WINDKLLTSP DVSYDEARNL HNKWMKHQAF MAELASHQGW
     LENIDAEGRQ LMAEKPQFKD VVSERLEALH KLWEELQSTA KAKAEQLSAA RSSDLRLQTH
     ADLNKWIGAM EDQLRSDDLG KDLTTVNRML AKLKRVEEQV NLRKEELEEL FADAPSLGAE
     AGDTDMSIEK RFLDLLEPLG RRKKQLELSK AKLQISRDLE DETLWVEERL PLAQSADYGT
     NLQTVQLFMK KNQTLQNEIL GHAPRVEDVL RRGQELVKAA EIDCQDIEER LGHLQSSWDT
     LREAAAGRLQ RLRDAHEAQQ YYLDAGEAEA WISEQELYVF SDEPPKDEEG AIVMLKRHLR
     QQRTVEEYGR NIKQLAGRAQ SLLSAGHPEG EQIIRLQGQV DKQYAGLKDM AEERRRRLEN
     MYHLFQLKRE ADDLEQWITE KEMVASSQEM GQDFDHVTML RDKFRDFARE TGAIGQERVD
     NVTIIERLID AGHSEAATIA EWKDGLNDMW ADLLELIDTR MQLLAASYDL HRYFYTGTEI
     LGLIDEKHRE LPEDVGLDAS TAESFHRVHT AFERELHLLG VQVQQFQDVA TRLQTAYAGE
     KADAIQSKEQ EVSAAWQALL DACAGRRAQL VDTADKFRFF SMVRDLLSWM ESIIRQIETQ
     ERPRDVSSVE LLLKYHQGIK AEINTRAKNF STCLELGESL LQRQHQASDE IREKLQQVIS
     RRQEMNDKWE ARSDRLHMLL EVCQFSRDAS VAEAWLIAQE PYLASRDFGH TVDSVEKLIK
     RHEAFEKSTA SWAERFAALE KPTTLELKER QTPERPTEEP GPQEEEGETA GEAPQVHHAA
     TERTSPVSFM SRLSSSWESL LPEPAHPF
//
ID   NDKA_MOUSE              Reviewed;         152 AA.
AC   P15532;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   08-MAR-2011, entry version 107.
DE   RecName: Full=Nucleoside diphosphate kinase A;
DE            Short=NDK A;
DE            Short=NDP kinase A;
DE            EC=2.7.4.6;
DE   AltName: Full=Metastasis inhibition factor NM23;
DE   AltName: Full=NDPK-A;
DE   AltName: Full=Tumor metastatic process-associated protein;
DE   AltName: Full=nm23-M1;
GN   Name=Nme1; Synonyms=Nm23;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90044071; PubMed=2509941; DOI=10.1038/342177a0;
RA   Rosengard A.M., Krutzsch H.C., Shearn A., Biggs J.R., Barker E.,
RA   Margulies I.M.K., King C.R., Liotta L.A., Steeg P.S.;
RT   "Reduced Nm23/Awd protein in tumour metastasis and aberrant Drosophila
RT   development.";
RL   Nature 342:177-180(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=88155671; PubMed=3346912; DOI=10.1093/jnci/80.3.200;
RA   Steeg P.S., Bevilacqua G., Kopper L., Thorgeirsson U.P.,
RA   Talmadge J.E., Liotta L.A., Sobel M.E.;
RT   "Evidence for a novel gene associated with low tumor metastatic
RT   potential.";
RL   J. Natl. Cancer Inst. 80:200-204(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=91191558; PubMed=2013093; DOI=10.1016/0092-8674(91)90404-M;
RA   Leone A., Flatow U., King C.R., Sandeen M.A., Margulies I.M.,
RA   Liotta L.A., Steeg P.S.;
RT   "Reduced tumor incidence, metastatic potential, and cytokine
RT   responsiveness of nm23-transfected melanoma cells.";
RL   Cell 65:25-35(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/Sv;
RA   Dabernat S., Masse K., Daniel J.Y.;
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster / NIH;
RA   Gervasi F., Fanciulli M., Lombardi D.;
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 7-26; 67-85; 89-124 AND 129-143, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Major role in the synthesis of nucleoside triphosphates
CC       other than ATP. The ATP gamma phosphate is transferred to the NDP
CC       beta phosphate via a ping-pong mechanism, using a phosphorylated
CC       active-site intermediate. Possesses nucleoside-diphosphate kinase,
CC       serine/threonine-specific protein kinase, geranyl and farnesyl
CC       pyrophosphate kinase, histidine protein kinase and 3'-5'
CC       exonuclease activities. Involved in cell proliferation,
CC       differentiation and development, signal transduction, G protein-
CC       coupled receptor endocytosis, and gene expression. Required for
CC       neural development including neural patterning and cell fate
CC       determination (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + nucleoside diphosphate = ADP +
CC       nucleoside triphosphate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Autophosphorylation at His-118 increases
CC       serine/threonine protein kinase activity of the enzyme.
CC       Interaction with the SET complex inhibits exonuclease activity (By
CC       similarity).
CC   -!- SUBUNIT: Hexamer of two different chains: A and B (A6, A5B, A4B2,
CC       A3B3, A2B4, AB5, B6). Interacts with SET and PRUNE (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- DISEASE: Note=This protein is found in reduced amount in tumor
CC       cells of high metastatic potential.
CC   -!- SIMILARITY: Belongs to the NDK family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA39826.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M35970; AAA39826.1; ALT_INIT; mRNA.
DR   EMBL; M65037; AAA63391.1; -; mRNA.
DR   EMBL; U85511; AAB42080.1; -; mRNA.
DR   EMBL; AF033377; AAB87689.1; -; mRNA.
DR   EMBL; BC005629; AAH05629.1; -; mRNA.
DR   IPI; IPI00131459; -.
DR   PIR; A46557; A46557.
DR   RefSeq; NP_032730.1; NM_008704.2.
DR   UniGene; Mm.439702; -.
DR   ProteinModelPortal; P15532; -.
DR   SMR; P15532; 5-152.
DR   STRING; P15532; -.
DR   PhosphoSite; P15532; -.
DR   SWISS-2DPAGE; P15532; -.
DR   REPRODUCTION-2DPAGE; P15532; -.
DR   PRIDE; P15532; -.
DR   Ensembl; ENSMUST00000021220; ENSMUSP00000021220; ENSMUSG00000037601.
DR   GeneID; 18102; -.
DR   KEGG; mmu:18102; -.
DR   UCSC; uc007kxu.1; mouse.
DR   CTD; 18102; -.
DR   MGI; MGI:97355; Nme1.
DR   eggNOG; maNOG10260; -.
DR   HOGENOM; HBG445152; -.
DR   HOVERGEN; HBG000423; -.
DR   InParanoid; P15532; -.
DR   OMA; IRAEFAE; -.
DR   PhylomeDB; P15532; -.
DR   BRENDA; 2.7.4.6; 244.
DR   NextBio; 459792; -.
DR   ArrayExpress; P15532; -.
DR   Bgee; P15532; -.
DR   Genevestigator; P15532; -.
DR   GermOnline; ENSMUSG00000037601; Mus musculus.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005625; C:soluble fraction; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:EC.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR   GO; GO:0007595; P:lactation; IMP:MGI.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
DR   InterPro; IPR001564; Nucleoside_diP_kinase.
DR   InterPro; IPR023005; Nucleoside_diP_kinase_AS.
DR   Gene3D; G3DSA:3.30.70.141; NDK; 1.
DR   PANTHER; PTHR11349; Nuc_diP_kinase_core; 1.
DR   Pfam; PF00334; NDK; 1.
DR   PRINTS; PR01243; NUCDPKINASE.
DR   SMART; SM00562; NDK; 1.
DR   SUPFAM; SSF54919; NDK; 1.
DR   PROSITE; PS00469; NDP_KINASES; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Differentiation;
KW   Direct protein sequencing; Endocytosis; Isopeptide bond; Kinase;
KW   Magnesium; Metal-binding; Neurogenesis; Nucleotide metabolism;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Transferase;
KW   Ubl conjugation.
FT   CHAIN         1    152       Nucleoside diphosphate kinase A.
FT                                /FTId=PRO_0000137115.
FT   ACT_SITE    118    118       Pros-phosphohistidine intermediate.
FT   BINDING      12     12       ATP (By similarity).
FT   BINDING      60     60       ATP (By similarity).
FT   BINDING      88     88       ATP (By similarity).
FT   BINDING      94     94       ATP (By similarity).
FT   BINDING     105    105       ATP (By similarity).
FT   BINDING     115    115       ATP (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      52     52       Phosphotyrosine (By similarity).
FT   MOD_RES      56     56       N6-acetyllysine (By similarity).
FT   MOD_RES      94     94       Phosphothreonine (By similarity).
FT   CROSSLNK    100    100       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
SQ   SEQUENCE   152 AA;  17208 MW;  EE2E4DB218024686 CRC64;
     MANSERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVGLKF LQASEDLLKE HYTDLKDRPF
     FTGLVKYMHS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRNIIHGS
     DSVKSAEKEI SLWFQPEELV EYKSCAQNWI YE
//
ID   FGF5_MOUSE              Reviewed;         264 AA.
AC   P15656; O88825;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   08-MAR-2011, entry version 101.
DE   RecName: Full=Fibroblast growth factor 5;
DE            Short=FGF-5;
DE   AltName: Full=Heparin-binding growth factor 5;
DE            Short=HBGF-5;
DE   Flags: Precursor;
GN   Name=Fgf5; Synonyms=Fgf-5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RX   MEDLINE=90201563; PubMed=2318343; DOI=10.1016/0012-1606(90)90211-Z;
RA   Hebert J.M., Basilico C., Goldfarb M., Haub O., Martin G.R.;
RT   "Isolation of cDNAs encoding four mouse FGF family members and
RT   characterization of their expression patterns during embryogenesis.";
RL   Dev. Biol. 138:454-463(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG).
RC   STRAIN=C57BL/6;
RX   MEDLINE=91045929; PubMed=1700424; DOI=10.1073/pnas.87.20.8022;
RA   Haub O., Drucker B., Goldfarb M.;
RT   "Expression of the murine fibroblast growth factor 5 gene in the adult
RT   central nervous system.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:8022-8026(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RX   MEDLINE=99003286; PubMed=9786939; DOI=10.1074/jbc.273.44.29262;
RA   Ozawa K., Suzuki S., Asada M., Tomooka Y., Li A.J., Yoneda A.,
RA   Komi A., Imamura T.;
RT   "An alternatively spliced fibroblast growth factor (FGF)-5 mRNA is
RT   abundant in brain and translates into a partial agonist/antagonist for
RT   FGF-5 neurotrophic activity.";
RL   J. Biol. Chem. 273:29262-29271(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Functions as an inhibitor of hair elongation by
CC       promoting progression from anagen, the growth phase of the hair
CC       follicle, into catagen the apoptosis-induced regression phase.
CC   -!- SUBCELLULAR LOCATION: Secreted (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=P15656-1; Sequence=Displayed;
CC       Name=Short; Synonyms=FGF-5S;
CC         IsoId=P15656-2; Sequence=VSP_001520, VSP_001521;
CC         Note=Seems to have an antagonistic effect compared to that of
CC         the isoform Long;
CC   -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M30643; AAA96698.1; -; mRNA.
DR   EMBL; M37823; AAB02660.1; -; Genomic_DNA.
DR   EMBL; M37821; AAB02660.1; JOINED; Genomic_DNA.
DR   EMBL; M37822; AAB02660.1; JOINED; Genomic_DNA.
DR   EMBL; M37821; AAB02659.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AB016516; BAA33737.1; -; mRNA.
DR   EMBL; AK028694; BAC26069.1; -; mRNA.
DR   EMBL; AK028894; BAC26179.1; -; mRNA.
DR   EMBL; BC071227; AAH71227.1; -; mRNA.
DR   IPI; IPI00132611; -.
DR   IPI; IPI00230752; -.
DR   PIR; A36207; A36207.
DR   PIR; B36207; B36207.
DR   RefSeq; NP_034333.1; NM_010203.4.
DR   UniGene; Mm.5055; -.
DR   ProteinModelPortal; P15656; -.
DR   SMR; P15656; 53-218.
DR   STRING; P15656; -.
DR   PRIDE; P15656; -.
DR   Ensembl; ENSMUST00000031280; ENSMUSP00000031280; ENSMUSG00000029337.
DR   GeneID; 14176; -.
DR   KEGG; mmu:14176; -.
DR   UCSC; uc008ygc.1; mouse.
DR   UCSC; uc008ygd.1; mouse.
DR   CTD; 14176; -.
DR   MGI; MGI:95519; Fgf5.
DR   eggNOG; roNOG13900; -.
DR   GeneTree; ENSGT00590000082822; -.
DR   HOGENOM; HBG715603; -.
DR   HOVERGEN; HBG007580; -.
DR   InParanoid; P15656; -.
DR   OMA; SHEANML; -.
DR   OrthoDB; EOG4HT8T7; -.
DR   PhylomeDB; P15656; -.
DR   NextBio; 285354; -.
DR   ArrayExpress; P15656; -.
DR   Bgee; P15656; -.
DR   CleanEx; MM_FGF5; -.
DR   Genevestigator; P15656; -.
DR   GermOnline; ENSMUSG00000029337; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0010001; P:glial cell differentiation; IMP:MGI.
DR   GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR   InterPro; IPR008996; Cytokine_IL1-like.
DR   InterPro; IPR002209; GF_heparin-bd.
DR   InterPro; IPR002348; IL1_HBGF.
DR   PANTHER; PTHR11486; IL1_HBGF; 1.
DR   Pfam; PF00167; FGF; 1.
DR   PRINTS; PR00263; HBGFFGF.
DR   PRINTS; PR00262; IL1HBGF.
DR   SMART; SM00442; FGF; 1.
DR   SUPFAM; SSF50353; Cytok_IL1_like; 1.
DR   PROSITE; PS00247; HBGF_FGF; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Growth factor; Mitogen; Secreted;
KW   Signal.
FT   SIGNAL        1     17       Potential.
FT   CHAIN        18    264       Fibroblast growth factor 5.
FT                                /FTId=PRO_0000008959.
FT   COMPBIAS     53     59       Poly-Ser.
FT   CARBOHYD    108    108       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     118    121       ILEI -> QIYG (in isoform Short).
FT                                /FTId=VSP_001520.
FT   VAR_SEQ     122    264       Missing (in isoform Short).
FT                                /FTId=VSP_001521.
SQ   SEQUENCE   264 AA;  29103 MW;  F6A9C8153EE923D1 CRC64;
     MSLSLLFLIF CSHLIHSAWA HGEKRLTPEG QPAPPRNPGD SSGSRGRSSA TFSSSSASSP
     VAASPGSQGS GSEHSSFQWS PSGRRTGSLY CRVGIGFHLQ IYPDGKVNGS HEASVLSILE
     IFAVSQGIVG IRGVFSNKFL AMSKKGKLHA SAKFTDDCKF RERFQENSYN TYASAIHRTE
     KTGREWYVAL NKRGKAKRGC SPRVKPQHVS THFLPRFKQS EQPELSFTVT VPEKKKPPVK
     PKVPLSQPRR SPSPVKYRLK FRFG
//
ID   H12_MOUSE               Reviewed;         212 AA.
AC   P15864;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   30-NOV-2010, entry version 95.
DE   RecName: Full=Histone H1.2;
DE   AltName: Full=H1 VAR.1;
DE   AltName: Full=H1c;
GN   Name=Hist1h1c; Synonyms=H1f2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=89386668; PubMed=2780558; DOI=10.1073/pnas.86.18.7002;
RA   Cheng G., Nandi A., Clerk S., Skoultchi A.I.;
RT   "Different 3'-end processing produces two independently regulated
RT   mRNAs from a single H1 histone gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:7002-7006(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=88059119; PubMed=2824517;
RA   Yang Y.-S., Brown D.T., Wellman S.E., Sittman D.B.;
RT   "Isolation and characterization of a mouse fully replication-dependent
RT   H1 gene within a genomic cluster of core histone genes.";
RL   J. Biol. Chem. 262:17118-17125(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=98322109; PubMed=9655912; DOI=10.1016/S0167-4781(98)00062-1;
RA   Franke K., Drabent B., Doenecke D.;
RT   "Expression of murine H1 histone genes during postnatal development.";
RL   Biochim. Biophys. Acta 1398:232-242(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=22296985; PubMed=12408966; DOI=10.1016/S0888-7543(02)96850-3;
RA   Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
RT   "The human and mouse replication-dependent histone genes.";
RL   Genomics 80:487-498(2002).
CC   -!- FUNCTION: Histones H1 are necessary for the condensation of
CC       nucleosome chains into higher order structures.
CC   -!- INTERACTION:
CC       Q99MD9:Nasp; NbExp=2; IntAct=EBI-913436, EBI-913410;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- SIMILARITY: Belongs to the histone H1/H5 family.
CC   -!- SIMILARITY: Contains 1 H15 (linker histone H1/H5 globular) domain.
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DR   EMBL; M25365; AAA37808.1; -; Genomic_DNA.
DR   EMBL; J03482; AAA37807.1; -; Genomic_DNA.
DR   EMBL; Y12291; CAA72970.1; -; Genomic_DNA.
DR   EMBL; AY158905; AAO06216.1; -; Genomic_DNA.
DR   IPI; IPI00223713; -.
DR   PIR; A28470; A28470.
DR   PIR; B35245; B35245.
DR   RefSeq; NP_056601.1; NM_015786.2.
DR   UniGene; Mm.193539; -.
DR   ProteinModelPortal; P15864; -.
DR   SMR; P15864; 36-109.
DR   IntAct; P15864; 3.
DR   STRING; P15864; -.
DR   PhosphoSite; P15864; -.
DR   PRIDE; P15864; -.
DR   Ensembl; ENSMUST00000040914; ENSMUSP00000045816; ENSMUSG00000036181.
DR   GeneID; 50708; -.
DR   KEGG; mmu:50708; -.
DR   UCSC; uc007puq.1; mouse.
DR   CTD; 50708; -.
DR   MGI; MGI:1931526; Hist1h1c.
DR   eggNOG; roNOG17301; -.
DR   HOGENOM; HBG446956; -.
DR   HOVERGEN; HBG009035; -.
DR   InParanoid; P15864; -.
DR   NextBio; 307561; -.
DR   ArrayExpress; P15864; -.
DR   Bgee; P15864; -.
DR   CleanEx; MM_HIST1H1C; -.
DR   Genevestigator; P15864; -.
DR   GermOnline; ENSMUSG00000036181; Mus musculus.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   GO; GO:0016584; P:nucleosome positioning; IMP:MGI.
DR   InterPro; IPR005818; Histone_H1/H5.
DR   InterPro; IPR005819; Histone_H5.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF00538; Linker_histone; 1.
DR   PRINTS; PR00624; HISTONEH5.
DR   SMART; SM00526; H15; 1.
DR   PROSITE; PS51504; H15; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromosome; DNA-binding; Isopeptide bond; Methylation;
KW   Nucleus; Phosphoprotein; Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    212       Histone H1.2.
FT                                /FTId=PRO_0000195915.
FT   DOMAIN       36    109       H15.
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES       2      2       Phosphoserine (By similarity).
FT   MOD_RES      34     34       N6-methyllysine (By similarity).
FT   MOD_RES      36     36       Phosphoserine (By similarity).
FT   MOD_RES     146    146       Phosphothreonine (By similarity).
FT   MOD_RES     173    173       Phosphoserine (By similarity).
FT   CROSSLNK     17     17       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK    205    205       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
SQ   SEQUENCE   212 AA;  21267 MW;  2872A9BCD50C840D CRC64;
     MSEAAPAAPA AAPPAEKAPA KKKAAKKPAG VRRKASGPPV SELITKAVAA SKERSGVSLA
     ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GILVQTKGTG ASGSFKLNKK AASGEAKPQA
     KKAGAAKAKK PAGAAKKPKK ATGAATPKKA AKKTPKKAKK PAAAAVTKKV AKSPKKAKVT
     KPKKVKSASK AVKPKAAKPK VAKAKKVAAK KK
//
ID   VPP2_MOUSE              Reviewed;         856 AA.
AC   P15920; A4FU82; Q3U2X3; Q8VHU0; Q9JHJ2;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   08-MAR-2011, entry version 109.
DE   RecName: Full=V-type proton ATPase 116 kDa subunit a isoform 2;
DE            Short=V-ATPase 116 kDa isoform a2;
DE   AltName: Full=Immune suppressor factor J6B7;
DE            Short=ISF;
DE   AltName: Full=Lysosomal H(+)-transporting ATPase V0 subunit a2;
DE   AltName: Full=ShIF;
DE   AltName: Full=Vacuolar proton translocating ATPase 116 kDa subunit a isoform 2;
GN   Name=Atp6v0a2; Synonyms=Atp6n1b, Tj6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=91061805; PubMed=2247090; DOI=10.1016/0161-5890(90)90102-6;
RA   Lee C.-K., Ghoshal K., Beaman K.D.;
RT   "Cloning of a cDNA for a T cell produced molecule with a putative
RT   immune regulatory role.";
RL   Mol. Immunol. 27:1137-1144(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=20187595; PubMed=10722719; DOI=10.1074/jbc.275.12.8760;
RA   Toyomura T., Oka T., Yamaguchi C., Wada Y., Futai M.;
RT   "Three subunit a isoforms of mouse vacuolar H+-ATPase. Preferential
RT   expression of the a3 isoform during osteoclast differentiation.";
RL   J. Biol. Chem. 275:8760-8765(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain, and Heart;
RX   MEDLINE=20167151; PubMed=10702241; DOI=10.1074/jbc.275.10.6824;
RA   Nishi T., Forgac M.;
RT   "Molecular cloning and expression of three isoforms of the 100-kDa a
RT   subunit of the mouse vacuolar proton-translocating ATPase.";
RL   J. Biol. Chem. 275:6824-6830(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=NOD; TISSUE=Dendritic cell, and Wolffian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 569-856, AND TISSUE SPECIFICITY.
RX   PubMed=11375395; DOI=10.1074/jbc.M101781200;
RA   Tulin E.E., Onoda N., Maeda M., Hasegawa M., Nosaka T., Nomura H.,
RA   Asano S., Kitamura T.;
RT   "A novel secreted form of immune suppressor factor with high homology
RT   to vacuolar ATPases identified by a forward genetic approach of
RT   functional screening based on cell proliferation.";
RL   J. Biol. Chem. 276:27519-27526(2001).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PSCD2.
RX   PubMed=16415858; DOI=10.1038/ncb1348;
RA   Hurtado-Lorenzo A., Skinner M., El Annan J., Futai M., Sun-Wada G.-H.,
RA   Bourgoin S., Casanova J., Wildeman A., Bechoua S., Ausiello D.A.,
RA   Brown D., Marshansky V.;
RT   "V-ATPase interacts with ARNO and Arf6 in early endosomes and
RT   regulates the protein degradative pathway.";
RL   Nat. Cell Biol. 8:124-136(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695 AND SER-700, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695 AND SER-700, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Part of the proton channel of V-ATPases (By similarity).
CC       Essential component of the endosomal pH-sensing machinery. May
CC       play a role in maintaining the Golgi functions, such as
CC       glycosylation maturation, by controlling the Golgi pH.
CC   -!- SUBUNIT: The V-ATPase is an heteromultimeric enzyme composed of at
CC       least thirteen different subunits. It has a membrane peripheral V1
CC       sector for ATP hydrolysis and an integral V0 for proton
CC       translocation. The V1 sector comprises subunits A-H, whereas V0
CC       includes subunits a, d, c, c', and c''. Directly interacts with
CC       PSCD2 through its N-terminal cytosolic tail in an intra-endosomal
CC       acidification-dependent manner. Disruption of this interaction
CC       results in the inhibition of endocytosis.
CC   -!- INTERACTION:
CC       P63034:Cyth2; NbExp=2; IntAct=EBI-988456, EBI-988425;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Endosome membrane. Note=In kidney proximal tubules, detected in
CC       subapical early endosomes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P15920-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P15920-2; Sequence=VSP_032088;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Relatively high expression in kidney and
CC       liver. Lower levels in the spleen, testis, and skeletal muscle.
CC       Also expressed in the thymus.
CC   -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL57303.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M31226; AAA39336.1; -; mRNA.
DR   EMBL; X55184; CAA38968.1; -; mRNA.
DR   EMBL; AB022323; BAA93007.1; -; mRNA.
DR   EMBL; AF218252; AAF59921.1; -; mRNA.
DR   EMBL; AK032909; BAC28081.1; -; mRNA.
DR   EMBL; AK155055; BAE33017.1; -; mRNA.
DR   EMBL; BC108991; AAI08992.1; -; mRNA.
DR   EMBL; BC108992; AAI08993.1; -; mRNA.
DR   EMBL; BC112905; AAI12906.1; -; mRNA.
DR   EMBL; AF388674; AAL57303.1; ALT_INIT; mRNA.
DR   IPI; IPI00135975; -.
DR   IPI; IPI00889297; -.
DR   PIR; JH0287; JH0287.
DR   RefSeq; NP_035726.2; NM_011596.4.
DR   UniGene; Mm.1158; -.
DR   UniGene; Mm.391970; -.
DR   UniGene; Mm.392098; -.
DR   ProteinModelPortal; P15920; -.
DR   IntAct; P15920; 5.
DR   STRING; P15920; -.
DR   PhosphoSite; P15920; -.
DR   PRIDE; P15920; -.
DR   Ensembl; ENSMUST00000037865; ENSMUSP00000039737; ENSMUSG00000038023.
DR   GeneID; 21871; -.
DR   KEGG; mmu:21871; -.
DR   UCSC; uc008zqk.1; mouse.
DR   CTD; 21871; -.
DR   MGI; MGI:104855; Atp6v0a2.
DR   eggNOG; roNOG14122; -.
DR   GeneTree; ENSGT00390000004941; -.
DR   HOGENOM; HBG629705; -.
DR   HOVERGEN; HBG014606; -.
DR   InParanoid; P15920; -.
DR   OMA; TIPSFMN; -.
DR   OrthoDB; EOG4J6RQ7; -.
DR   PhylomeDB; P15920; -.
DR   NextBio; 301372; -.
DR   ArrayExpress; P15920; -.
DR   Bgee; P15920; -.
DR   CleanEx; MM_ATP6V0A2; -.
DR   Genevestigator; P15920; -.
DR   GermOnline; ENSMUSG00000038023; Mus musculus.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033177; C:proton-transporting two-sector ATPase complex, proton-transporting domain; IEA:InterPro.
DR   GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR002490; ATPase_V0/A0-cplx_116kDa_su.
DR   PANTHER; PTHR11629; ATPase_V0/A0_116; 1.
DR   Pfam; PF01496; V_ATPase_I; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell membrane; Endosome;
KW   Hydrogen ion transport; Ion transport; Membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    856       V-type proton ATPase 116 kDa subunit a
FT                                isoform 2.
FT                                /FTId=PRO_0000119217.
FT   TOPO_DOM      1    409       Cytoplasmic (Potential).
FT   TRANSMEM    410    430       Helical; (Potential).
FT   TOPO_DOM    431    451       Lumenal (Potential).
FT   TRANSMEM    452    472       Helical; (Potential).
FT   TOPO_DOM    473    554       Cytoplasmic (Potential).
FT   TRANSMEM    555    575       Helical; (Potential).
FT   TOPO_DOM    576    585       Lumenal (Potential).
FT   TRANSMEM    586    606       Helical; (Potential).
FT   TOPO_DOM    607    622       Cytoplasmic (Potential).
FT   TRANSMEM    623    643       Helical; (Potential).
FT   TOPO_DOM    644    650       Lumenal (Potential).
FT   TRANSMEM    651    671       Helical; (Potential).
FT   TOPO_DOM    672    755       Cytoplasmic (Potential).
FT   TRANSMEM    756    779       Helical; (Potential).
FT   TOPO_DOM    780    786       Lumenal (Potential).
FT   TRANSMEM    787    807       Helical; (Potential).
FT   TOPO_DOM    808    856       Cytoplasmic (Potential).
FT   MOD_RES     177    177       Phosphoserine (By similarity).
FT   MOD_RES     279    279       N6-acetyllysine (By similarity).
FT   MOD_RES     695    695       Phosphoserine.
FT   MOD_RES     700    700       Phosphoserine.
FT   VAR_SEQ       1    593       Missing (in isoform 2).
FT                                /FTId=VSP_032088.
FT   CONFLICT    486    486       S -> C (in Ref. 1; AAA39336/CAA38968).
FT   CONFLICT    791    791       Missing (in Ref. 1; AAA39336/CAA38968).
SQ   SEQUENCE   856 AA;  98145 MW;  6A0D593F6F401E22 CRC64;
     MGSLFRSESM CLAQLFLQSG TAYECLSALG EKGLVQFRDL NQNVSSFQRK FVGEVKRCEE
     LERILVYLVQ EITRADIPLP EGEASPPAPP LKHVLEMQEQ LQKLEVELRE VTKNKEKLRK
     NLLELVEYTH MLRVTKTFLK RNVEFEPTYE EFPALENDSL LDYSCMQRLG AKLGFVSGLI
     QQGRVEAFER MLWRACKGYT IVTYAELDEC LEDPETGEVI KWYVFLISFW GEQIGHKVKK
     ICDCYHCHIY PYPNTAEERR EIQEGLNTRI QDLYTVLHKT EDYLRQVLCK AAESVCSRVV
     QVRKMKAIYH MLNMCSFDVT NKCLIAEVWC PEVDLPGLRR ALEEGSRESG ATIPSFMNTI
     PTKETPPTLI RTNKFTEGFQ NIVDAYGVGS YREVNPALFT IITFPFLFAV MFGDFGHGFV
     MFLFALLLVL NENHPRLSQS QEILRMFFDG RYILLLMGLF SVYTGLIYND CFSKSVNLFG
     SGWNVSAMYS SSHSPEEQRK MVLWNDSTIR HSRTLQLDPN IPGVFRGPYP FGIDPIWNLA
     TNRLTFLNSF KMKMSVILGI FHMTFGVVLG IFNHLHFRKK FNVYLVSVPE ILFMLCIFGY
     LIFMIIYKWL AYSAETSREA PSILIEFINM FLFPTSKTHG LYPGQAHVQR VLVALTVLAV
     PVLFLGKPLF LLWLHNGRNC FGMSRSGYTL VRKDSEEEVS LLGNQDIEEG NSRMEEGCRE
     VTCEEFNFGE ILMTQAIHSI EYCLGCISNT ASYLRLWALS LAHAQLSDVL WAMLMRVGLR
     VDTTYGVLLL LPVMAFFAVL TIFILLVMEG LSAFLHAIRL HWVEFQNKFY VGAGTKFVPF
     SFSLLSSKFS NDDSIA
//
ID   SCG1_MOUSE              Reviewed;         677 AA.
AC   P16014;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 2.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Secretogranin-1;
DE   AltName: Full=Chromogranin-B;
DE            Short=CgB;
DE   AltName: Full=Secretogranin I;
DE            Short=SgI;
DE   Flags: Precursor;
GN   Name=Chgb; Synonyms=Scg-1, Scg1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   MEDLINE=90206804; PubMed=2320426; DOI=10.1093/nar/18.5.1298;
RA   Linard C.G., Mbikay M., Seidah N.G., Chretien M.;
RT   "Primary structure of mouse chromogranin B deduced from cDNA
RT   sequence.";
RL   Nucleic Acids Res. 18:1298-1298(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90242932; PubMed=2335203; DOI=10.1016/0014-5793(90)80194-N;
RA   Pohl T.M., Phillips E., Song K., Gerdes H.-H., Huttner W.B.,
RA   Ruether U.;
RT   "The organisation of the mouse chromogranin B (secretogranin I)
RT   gene.";
RL   FEBS Lett. 262:219-224(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-151, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- FUNCTION: Secretogranin-1 is a neuroendocrine secretory granule
CC       protein, which may be the precursor for other biologically active
CC       peptides.
CC   -!- INTERACTION:
CC       P00441:SOD1 (xeno); NbExp=2; IntAct=EBI-990820, EBI-990792;
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Neuroendocrine and endocrine
CC       secretory granules.
CC   -!- SIMILARITY: Belongs to the chromogranin/secretogranin protein
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X53028; CAA37199.1; -; mRNA.
DR   EMBL; X51429; CAA35792.1; -; mRNA.
DR   EMBL; BC014736; AAH14736.1; -; mRNA.
DR   IPI; IPI00130307; -.
DR   PIR; S09078; S09078.
DR   RefSeq; NP_031720.1; NM_007694.4.
DR   UniGene; Mm.255241; -.
DR   ProteinModelPortal; P16014; -.
DR   IntAct; P16014; 9.
DR   STRING; P16014; -.
DR   PhosphoSite; P16014; -.
DR   PRIDE; P16014; -.
DR   Ensembl; ENSMUST00000028826; ENSMUSP00000028826; ENSMUSG00000027350.
DR   GeneID; 12653; -.
DR   KEGG; mmu:12653; -.
DR   UCSC; uc008mnf.1; mouse.
DR   CTD; 12653; -.
DR   MGI; MGI:88395; Chgb.
DR   eggNOG; roNOG14731; -.
DR   HOGENOM; HBG126015; -.
DR   HOVERGEN; HBG057317; -.
DR   InParanoid; P16014; -.
DR   OMA; NWGYEKR; -.
DR   OrthoDB; EOG4Z0B5C; -.
DR   PhylomeDB; P16014; -.
DR   NextBio; 281868; -.
DR   PMAP-CutDB; P16014; -.
DR   ArrayExpress; P16014; -.
DR   Bgee; P16014; -.
DR   CleanEx; MM_CHGB; -.
DR   Genevestigator; P16014; -.
DR   GermOnline; ENSMUSG00000027350; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   InterPro; IPR001819; Chromogranin_AB.
DR   InterPro; IPR018054; Chromogranin_CS.
DR   InterPro; IPR001990; Granin.
DR   PANTHER; PTHR10583; Chromogranin_AB; 1.
DR   Pfam; PF01271; Granin; 1.
DR   PRINTS; PR00659; CHROMOGRANIN.
DR   PROSITE; PS00422; GRANINS_1; 1.
DR   PROSITE; PS00423; GRANINS_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cleavage on pair of basic residues; Disulfide bond;
KW   Glycoprotein; Phosphoprotein; Secreted; Signal; Sulfation.
FT   SIGNAL        1     20
FT   CHAIN        21    677       Secretogranin-1.
FT                                /FTId=PRO_0000005441.
FT   MOD_RES      99     99       Phosphoserine (Potential).
FT   MOD_RES     100    100       Phosphoserine (Potential).
FT   MOD_RES     151    151       N6-acetyllysine.
FT   MOD_RES     171    171       Sulfotyrosine (Potential).
FT   MOD_RES     256    256       Phosphoserine (By similarity).
FT   MOD_RES     260    260       Phosphoserine (By similarity).
FT   MOD_RES     300    300       Phosphoserine (Potential).
FT   MOD_RES     301    301       Phosphoserine (Potential).
FT   MOD_RES     318    318       Phosphoserine (By similarity).
FT   MOD_RES     342    342       Phosphoserine (By similarity).
FT   MOD_RES     348    348       Sulfotyrosine (By similarity).
FT   MOD_RES     375    375       Phosphoserine (By similarity).
FT   MOD_RES     378    378       Phosphoserine (By similarity).
FT   MOD_RES     469    469       Sulfotyrosine (Potential).
FT   MOD_RES     472    472       Sulfotyrosine (Probable).
FT   MOD_RES     532    532       Phosphoserine (Potential).
FT   MOD_RES     543    543       Phosphoserine (Potential).
FT   MOD_RES     566    566       Sulfotyrosine (Probable).
FT   MOD_RES     568    568       Sulfotyrosine (Potential).
FT   MOD_RES     626    626       Phosphoserine (By similarity).
FT   CARBOHYD    115    115       O-linked (GalNAc...) (Probable).
FT   DISULFID     36     57       By similarity.
FT   CONFLICT    422    424       REP -> LGA (in Ref. 1; CAA35792).
SQ   SEQUENCE   677 AA;  77969 MW;  C73291E781E4F9B9 CRC64;
     MQPAMLLGLL GAAALAAVSS APVDNRDHNE EMVTRCIIEV LSNALSKSSV PTITPECRQV
     LKKSGKEVKG EEKGENQNSK FEVRLLRDPA DASGTRWASS REDAGAPVED SQGQTKVGNE
     KWTEGGGHSR EGVDDQESLR PSNQQASKEA KIYHSEERVG KEREKEEGKI YPMGEHREDA
     GEEKKHIEDS GEKPNTFSNK RSEASAKKKD ESVARADAHS MELEEKTHSR EQSSQESGEE
     TRRQEKPQEL TDQDQSQEES QEGEEGEEGE EGEEGEEDSA SEVTKRRPRH HHGRSGSNKS
     SYEGHPLSEE RRPSPKESKE ADVATVRLGE KRSHHLAHYR ASEEEPEYGE ESRSYRGLQY
     RGRGSEEDRA PRPRSEESQE REYKRNHPDS ELESTANRHG EETEEERSYE GANGRQHRGR
     GREPGAHSAL DTREEKRLLD EGHYPVRESP IDTAKRYPQS KWQEQEKNYL NYGEEGDQGR
     WWQQEEQLGP EESREEVRFP DRQYEPYPIT EKRKRLGALF NPYFDPLQWK NSDFEKRGNP
     DDSFLEDEGE DRNGVTLTEK NSFPEYNYDW WERRPFSEDV NWGYEKRSFA RAPQLDLKRQ
     YDGVAELDQL LHYRKKADEF PDFYDSEEQM GPHQEANDEK ARADQRVLTA EEKKELENLA
     AMDLELQKIA EKFSQRG
//
ID   KPCE_MOUSE              Reviewed;         737 AA.
AC   P16054;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   08-MAR-2011, entry version 117.
DE   RecName: Full=Protein kinase C epsilon type;
DE            EC=2.7.11.13;
DE   AltName: Full=nPKC-epsilon;
GN   Name=Prkce; Synonyms=Pkce, Pkcea;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=89137541; PubMed=2917656; DOI=10.1016/0014-5793(89)80160-7;
RA   Schaap D., Parker P.J., Bristol A., Kriz R., Knopf J.;
RT   "Unique substrate specificity and regulatory properties of PKC-
RT   epsilon: a rationale for diversity.";
RL   FEBS Lett. 243:351-357(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=98127436; PubMed=9467942; DOI=10.1038/sj.onc.1201507;
RA   Wang Q.J., Acs P., Goodnight J., Blumberg P.M., Mischak H.,
RA   Mushinski J.F.;
RT   "The catalytic domain of PKC-epsilon, in reciprocal PKC-delta and -
RT   epsilon chimeras, is responsible for conferring tumorgenicity to
RT   NIH3T3 cells, whereas both regulatory and catalytic domains of PKC-
RT   epsilon contribute to in vitro transformation.";
RL   Oncogene 16:53-60(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Wheeler D.L.;
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND THR-349, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: This is calcium-independent, phospholipid-dependent,
CC       serine- and threonine-specific enzyme.
CC   -!- FUNCTION: PKC is activated by diacylglycerol which in turn
CC       phosphorylates a range of cellular proteins. PKC also serves as
CC       the receptor for phorbol esters, a class of tumor promoters.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Three specific sites; Thr-566 (activation loop
CC       of the kinase domain), Thr-710 (turn motif) and Ser-729
CC       (hydrophobic region), need to be phosphorylated for its full
CC       activation.
CC   -!- SUBUNIT: Forms a ternary complex with TRIM63 and GN2BL1. Interacts
CC       with DGKQ (By similarity).
CC   -!- DOMAIN: The C1 domain, containing the phorbol ester/DAG-type
CC       region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor and the
CC       C2 domain is a non-calcium binding domain.
CC   -!- PTM: Phosphorylation on Thr-566 triggers autophosphorylation on
CC       Ser-729 (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. PKC subfamily.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 2 phorbol-ester/DAG-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF028009; AAB84189.1; -; mRNA.
DR   EMBL; AF325507; AAG53692.1; -; mRNA.
DR   IPI; IPI00130419; -.
DR   PIR; S02270; KIMSCE.
DR   RefSeq; NP_035234.1; NM_011104.3.
DR   UniGene; Mm.24614; -.
DR   ProteinModelPortal; P16054; -.
DR   SMR; P16054; 1-136, 165-295, 405-736.
DR   DIP; DIP-31066N; -.
DR   MINT; MINT-98243; -.
DR   STRING; P16054; -.
DR   PhosphoSite; P16054; -.
DR   PRIDE; P16054; -.
DR   Ensembl; ENSMUST00000097274; ENSMUSP00000094873; ENSMUSG00000045038.
DR   Ensembl; ENSMUST00000097275; ENSMUSP00000094874; ENSMUSG00000045038.
DR   GeneID; 18754; -.
DR   KEGG; mmu:18754; -.
DR   UCSC; uc008dug.1; mouse.
DR   CTD; 18754; -.
DR   MGI; MGI:97599; Prkce.
DR   eggNOG; roNOG12670; -.
DR   GeneTree; ENSGT00590000082973; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108317; -.
DR   InParanoid; P16054; -.
DR   OMA; SPCDQEL; -.
DR   OrthoDB; EOG40P467; -.
DR   PhylomeDB; P16054; -.
DR   BRENDA; 2.7.11.13; 244.
DR   NextBio; 294933; -.
DR   ArrayExpress; P16054; -.
DR   Bgee; P16054; -.
DR   CleanEx; MM_PRKCE; -.
DR   Genevestigator; P16054; -.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004699; F:calcium-independent protein kinase C activity; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007635; P:chemosensory behavior; TAS:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR   GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR014376; Prot_kin_PKC_delta.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   PIRSF; PIRSF000551; PKC_delta; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Repeat; Serine/threonine-protein kinase; Transferase;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    737       Protein kinase C epsilon type.
FT                                /FTId=PRO_0000055698.
FT   DOMAIN        1     99       C2.
FT   DOMAIN      408    668       Protein kinase.
FT   DOMAIN      669    737       AGC-kinase C-terminal.
FT   ZN_FING     169    220       Phorbol-ester/DAG-type 1.
FT   ZN_FING     242    292       Phorbol-ester/DAG-type 2.
FT   NP_BIND     414    422       ATP (By similarity).
FT   ACT_SITE    532    532       Proton acceptor (By similarity).
FT   BINDING     437    437       ATP (By similarity).
FT   MOD_RES     228    228       Phosphothreonine (By similarity).
FT   MOD_RES     309    309       Phosphothreonine (By similarity).
FT   MOD_RES     316    316       Phosphoserine (By similarity).
FT   MOD_RES     329    329       Phosphoserine (By similarity).
FT   MOD_RES     337    337       Phosphoserine.
FT   MOD_RES     339    339       Phosphoserine (By similarity).
FT   MOD_RES     346    346       Phosphoserine (By similarity).
FT   MOD_RES     349    349       Phosphothreonine.
FT   MOD_RES     350    350       Phosphoserine (By similarity).
FT   MOD_RES     368    368       Phosphoserine (By similarity).
FT   MOD_RES     566    566       Phosphothreonine; by PDPK1 (By
FT                                similarity).
FT   MOD_RES     703    703       Phosphothreonine; by autocatalysis
FT                                (Potential).
FT   MOD_RES     710    710       Phosphothreonine; by autocatalysis
FT                                (Potential).
FT   MOD_RES     729    729       Phosphoserine; by autocatalysis (By
FT                                similarity).
SQ   SEQUENCE   737 AA;  83561 MW;  7AEBB8CC10C99F57 CRC64;
     MVVFNGLLKI KICEAVSLKP TAWSLRHAVG PRPQTFLLDP YIALNVDDSR IGQTATKQKT
     NSPAWHDEFV TDVCNGRKIE LAVFHDAPIG YDDFVANCTI QFEELLQNGS RHFEDWIDLE
     PEGKVYVIID LSGSSGEAPK DNEERVFRER MRPRKRQGAV RRRVHQVNGH KFMATYLRQP
     TYCSHCRDFI WGVIGKQGYQ CQVCTCVVHK RCHELIITKC AGLKKQETPD EVGSQRFSVN
     MPHKFGIHNY KVPTFCDHCG SLLWGLLRQG LQCKVCKMNV HRRCETNVAP NCGVDARGIA
     KVLADLGVTP DKITNSGQRR KKLAAGAESP QPASGNSPSE DDRSKSAPTS PCDQELKELE
     NNIRKALSFD NRGEEHRASS ATDGQLASPG ENGEVRPGQA KRLGLDEFNF IKVLGKGSFG
     KVMLAELKGK DEVYAVKVLK KDVILQDDDV DCTMTEKRIL ALARKHPYLT QLYCCFQTKD
     RLFFVMEYVN GGDLMFQIQR SRKFDEPRSR FYAAEVTSAL MFLHQHGVIY RDLKLDNILL
     DAEGHCKLAD FGMCKEGIMN GVTTTTFCGT PDYIAPEILQ ELEYGPSVDW WALGVLMYEM
     MAGQPPFEAD NEDDLFESIL HDDVLYPVWL SKEAVSILKA FMTKNPHKRL GCVAAQNGED
     AIKQHPFFKE IDWVLLEQKK IKPPFKPRIK TKRDVNNFDQ DFTREEPILT LVDEAIIKQI
     NQEEFKGFSY FGEDLMP
//
ID   MET_MOUSE               Reviewed;        1379 AA.
AC   P16056; Q62125;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   08-MAR-2011, entry version 121.
DE   RecName: Full=Hepatocyte growth factor receptor;
DE            Short=HGF receptor;
DE            EC=2.7.10.1;
DE   AltName: Full=HGF/SF receptor;
DE   AltName: Full=Proto-oncogene c-Met;
DE   AltName: Full=Scatter factor receptor;
DE            Short=SF receptor;
DE   AltName: Full=Tyrosine-protein kinase Met;
DE   Flags: Precursor;
GN   Name=Met;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=88262253; PubMed=2838789;
RA   Chan A.M.-L., King H.W.S., Deakin E.A., Tempest P.R., Hilkens J.,
RA   Kroezen V., Edwards D.R., Wills A.J., Brookes P., Cooper C.S.;
RT   "Characterization of the mouse met proto-oncogene.";
RL   Oncogene 2:593-599(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1199-1270.
RX   MEDLINE=90152381; PubMed=2482828; DOI=10.1016/0378-1119(89)90465-4;
RA   Wilks A.F., Kurban R.R., Hovens C.M., Ralph S.J.;
RT   "The application of the polymerase chain reaction to cloning members
RT   of the protein tyrosine kinase family.";
RL   Gene 85:67-74(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 924-935.
RX   MEDLINE=93209981; PubMed=8384622; DOI=10.1083/jcb.121.1.145;
RA   Weidner K.M., Sachs M., Birchmeier W.;
RT   "The Met receptor tyrosine kinase transduces motility, proliferation,
RT   and morphogenic signals of scatter factor/hepatocyte growth factor in
RT   epithelial cells.";
RL   J. Cell Biol. 121:145-154(1993).
RN   [4]
RP   INTERACTION WITH INPP5D.
RX   PubMed=11896575; DOI=10.1038/sj.onc.1205224;
RA   Mancini A., Koch A., Wilms R., Tamura T.;
RT   "The SH2-containing inositol 5-phosphatase (SHIP)-1 is implicated in
RT   the control of cell-cell junction and induces dissociation and
RT   dispersion of MDCK cells.";
RL   Oncogene 21:1477-1484(2002).
RN   [5]
RP   INTERACTION WITH MUC20.
RX   PubMed=15314156; DOI=10.1128/MCB.24.17.7456-7468.2004;
RA   Higuchi T., Orita T., Katsuya K., Yamasaki Y., Akiyama K., Li H.,
RA   Yamamoto T., Saito Y., Nakamura M.;
RT   "MUC20 suppresses the hepatocyte growth factor-induced Grb2-Ras
RT   pathway by binding to a multifunctional docking site of met.";
RL   Mol. Cell. Biol. 24:7456-7468(2004).
RN   [6]
RP   INTERACTION WITH SPSB1; SPSB2 AND SPSB4.
RX   PubMed=16369487; DOI=10.1038/nsmb1034;
RA   Masters S.L., Yao S., Willson T.A., Zhang J.-G., Palmer K.R.,
RA   Smith B.J., Babon J.J., Nicola N.A., Norton R.S., Nicholson S.E.;
RT   "The SPRY domain of SSB-2 adopts a novel fold that presents conserved
RT   Par-4-binding residues.";
RL   Nat. Struct. Mol. Biol. 13:77-84(2006).
CC   -!- FUNCTION: Receptor for hepatocyte growth factor and scatter
CC       factor. Has a tyrosine-protein kinase activity. Functions in cell
CC       proliferation, scattering, morphogenesis and survival (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBUNIT: Heterodimer formed of an alpha chain (50 kDa) and a beta
CC       chain (145 kDa) which are disulfide linked (By similarity). Binds
CC       PLXNB1 and GRB2 (By similarity). When phosphorylated at Tyr-1354,
CC       interacts with INPPL1/SHIP2 (By similarity). Interacts with RANBP9
CC       and RANBP10 (By similarity). Interacts with INPP5D/SHIP1.
CC       Interacts with SPSB1, SPSB2, SPSB4 and probably SPSB3. SPSB1
CC       binding occurs in the presence and in the absence of HGF, however
CC       HGF treatment has a positive effect on this interaction. Interacts
CC       with MUC20; prevents interaction with GRB2 and suppresses
CC       hepatocyte growth factor-induced cell proliferation. Interacts
CC       with GRB10 (By similarity).
CC   -!- INTERACTION:
CC       P14210:HGF (xeno); NbExp=2; IntAct=EBI-1798780, EBI-1039104;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- DOMAIN: The kinase domain is involved in SPSB1 binding (By
CC       similarity).
CC   -!- PTM: Dephosphorylated by PTPRJ at Tyr-1347 and Tyr-1363 (By
CC       similarity).
CC   -!- DISEASE: Note=Activation of Met after rearrangement with the TPR
CC       (translocated promoter) locus of chromosome 1 produces an
CC       oncogenic protein.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family.
CC   -!- SIMILARITY: Contains 3 IPT/TIG domains.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 Sema domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Y00671; CAA68680.1; -; mRNA.
DR   EMBL; M33424; AAA40015.1; -; mRNA.
DR   IPI; IPI00130420; -.
DR   PIR; S01254; S01254.
DR   UniGene; Mm.86844; -.
DR   ProteinModelPortal; P16056; -.
DR   SMR; P16056; 40-740, 1044-1344.
DR   IntAct; P16056; 2.
DR   MINT; MINT-137318; -.
DR   STRING; P16056; -.
DR   PhosphoSite; P16056; -.
DR   PRIDE; P16056; -.
DR   Ensembl; ENSMUST00000080469; ENSMUSP00000079324; ENSMUSG00000009376.
DR   Ensembl; ENSMUST00000115442; ENSMUSP00000111102; ENSMUSG00000009376.
DR   Ensembl; ENSMUST00000115443; ENSMUSP00000111103; ENSMUSG00000009376.
DR   UCSC; uc009azr.1; mouse.
DR   MGI; MGI:96969; Met.
DR   HOGENOM; HBG445765; -.
DR   HOVERGEN; HBG006348; -.
DR   InParanoid; P16056; -.
DR   OrthoDB; EOG466VK2; -.
DR   BRENDA; 2.7.10.1; 244.
DR   PMAP-CutDB; P16056; -.
DR   ArrayExpress; P16056; -.
DR   Bgee; P16056; -.
DR   CleanEx; MM_MET; -.
DR   Genevestigator; P16056; -.
DR   GermOnline; ENSMUSG00000009376; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005008; F:hepatocyte growth factor receptor activity; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0000187; P:activation of MAPK activity; IPI:MGI.
DR   GO; GO:0030534; P:adult behavior; IMP:MGI.
DR   GO; GO:0007420; P:brain development; IMP:MGI.
DR   GO; GO:0001889; P:liver development; IMP:MGI.
DR   GO; GO:0014812; P:muscle cell migration; IMP:MGI.
DR   GO; GO:0051450; P:myoblast proliferation; IMP:MGI.
DR   GO; GO:0014902; P:myotube differentiation; IMP:MGI.
DR   GO; GO:0001890; P:placenta development; IMP:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR   GO; GO:0060665; P:regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling; IMP:MGI.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002909; IPT_TIG_rcpt.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR003659; Plexin-like.
DR   InterPro; IPR016201; Plexin-like_fold.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001627; Semaphorin/CD100_Ag.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   InterPro; IPR016244; Tyr_prot_kinase_HGF/MSP_rcpt.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF01437; PSI; 1.
DR   Pfam; PF01403; Sema; 1.
DR   Pfam; PF01833; TIG; 3.
DR   PIRSF; PIRSF000617; TyrPK_HGF-R; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00429; IPT; 4.
DR   SMART; SM00423; PSI; 1.
DR   SMART; SM00630; Sema; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF81296; Ig_E-set; 3.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF103575; Plexin-like_fold; 1.
DR   SUPFAM; SSF101912; Sema; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS51004; SEMA; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Disulfide bond; Glycoprotein; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Proto-oncogene; Receptor; Repeat;
KW   Signal; Transferase; Transmembrane; Transmembrane helix;
KW   Tyrosine-protein kinase.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25   1379       Hepatocyte growth factor receptor.
FT                                /FTId=PRO_0000024441.
FT   TOPO_DOM     25    931       Extracellular (Potential).
FT   TRANSMEM    932    954       Helical; (Potential).
FT   TOPO_DOM    955   1379       Cytoplasmic (Potential).
FT   DOMAIN       27    514       Sema.
FT   DOMAIN      562    654       IPT/TIG 1.
FT   DOMAIN      656    738       IPT/TIG 2.
FT   DOMAIN      741    835       IPT/TIG 3.
FT   DOMAIN     1076   1343       Protein kinase.
FT   NP_BIND    1082   1090       ATP (By similarity).
FT   REGION     1210   1379       Interaction with RANBP9 (By similarity).
FT   REGION     1318   1357       Interaction with MUC20 (By similarity).
FT   ACT_SITE   1202   1202       Proton acceptor (By similarity).
FT   BINDING    1108   1108       ATP (By similarity).
FT   SITE        306    307       Cleavage (Potential).
FT   MOD_RES     964    964       Phosphoserine (By similarity).
FT   MOD_RES     975    975       Phosphothreonine (By similarity).
FT   MOD_RES     986    986       Phosphoserine (By similarity).
FT   MOD_RES     988    988       Phosphoserine (By similarity).
FT   MOD_RES     995    995       Phosphoserine (By similarity).
FT   MOD_RES     998    998       Phosphoserine (By similarity).
FT   MOD_RES    1001   1001       Phosphotyrosine (By similarity).
FT   MOD_RES    1228   1228       Phosphotyrosine (By similarity).
FT   MOD_RES    1232   1232       Phosphotyrosine (By similarity).
FT   MOD_RES    1233   1233       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES    1287   1287       Phosphothreonine (By similarity).
FT   MOD_RES    1347   1347       Phosphotyrosine (By similarity).
FT   MOD_RES    1354   1354       Phosphotyrosine (By similarity).
FT   MOD_RES    1363   1363       Phosphotyrosine (By similarity).
FT   CARBOHYD     45     45       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    106    106       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    201    201       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    357    357       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    398    398       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    404    404       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    606    606       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    634    634       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    784    784       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    878    878       N-linked (GlcNAc...) (Potential).
FT   CONFLICT   1199   1199       V -> I (in Ref. 2; AAA40015).
FT   CONFLICT   1255   1255       T -> R (in Ref. 2; AAA40015).
FT   CONFLICT   1261   1261       K -> T (in Ref. 2; AAA40015).
FT   CONFLICT   1269   1270       VL -> IP (in Ref. 2).
SQ   SEQUENCE   1379 AA;  153549 MW;  FC5CC87FDD8ADED8 CRC64;
     MKAPTVLAPG ILVLLLSLVQ RSHGECKEAL VKSEMNVNMK YQLPNFTAET PIQNVVLHGH
     HIYLGATNYI YVLNDKDLQK VSEFKTGPVL EHPDCLPCRD CSSKANSSGG VWKDNINMAL
     LVDTYYDDQL ISCGSVNRGT CQRHVLPPDN SADIQSEVHC MFSPEEESGQ CPDCVVSALG
     AKVLLSEKDR FINFFVGNTI NSSYPPGYSL HSISVRRLKE TQDGFKFLTD QSYIDVLPEF
     LDSYPIKYIH AFESNHFIYF LTVQKETLDA QTFHTRIIRF CSVDSGLHSY MEMPLECILT
     EKRRKRSTRE EVFNILQAAY VSKPGANLAK QIGASPSDDI LFGVFAQSKP DSAEPVNRSA
     VCAFPIKYVN DFFNKIVNKN NVRCLQHFYG PNHEHCFNRT LLRNSSGCEA RSDEYRTEFT
     TALQRVDLFM GRLNQVLLTS ISTFIKGDLT IANLGTSEGR FMQVVLSRTA HLTPHVNFLL
     DSHPVSPEVI VEHPSNQNGY TLVVTGKKIT KIPLNGLGCG HFQSCSQCLS APYFIQCGWC
     HNQCVRFDEC PSGTWTQEIC LPAVYKVFPT SAPLEGGTVL TICGWDFGFR KNNKFDLRKT
     KVLLGNESCT LTLSESTTNT LKCTVGPAMS EHFNVSVIIS NSRETTQYSA FSYVDPVITS
     ISPRYGPQAG GTLLTLTGKY LNSGNSRHIS IGGKTCTLKS VSDSILECYT PAQTTSDEFP
     VKLKIDLANR ETSSFSYRED PVVYEIHPTK SFISGGSTIT GIGKTLNSVS LPKLVIDVHE
     VGVNYTVACQ HRSNSEIICC TTPSLKQLGL QLPLKTKAFF LLDGILSKHF DLTYVHNPVF
     EPFEKPVMIS MGNENVVEIK GNNIDPEAVK GEVLKVGNQS CESLHWHSGA VLCTVPSDLL
     KLNSELNIEW KQAVSSTVLG KVIVQPDQNF AGLIIGAVSI SVVVLLLSGL FLWMRKRKHK
     DLGSELVRYD ARVHTPHLDR LVSARSVSPT TEMVSNESVD YRATFPEDQF PNSSQNGACR
     QVQYPLTDLS PILTSGDSDI SSPLLQNTVH IDLSALNPEL VQAVQHVVIG PSSLIVHFNE
     VIGRGHFGCV YHGTLLDNDG KKIHCAVKSL NRITDIEEVS QFLTEGIIMK DFSHPNVLSL
     LGICLRSEGS PLVVLPYMKH GDLRNFIRNE THNPTVKDLI GFGLQVAKGM KYLASKKFVH
     RDLAARNCML DEKFTVKVAD FGLARDMYDK EYYSVHNKTG AKLPVKWMAL ESLQTQKFTT
     KSDVWSFGVL LWELMTRGAP PYPDVNTFDI TIYLLQGRRL LQPEYCPDAL YEVMLKCWHP
     KAEMRPSFSE LVSRISSIFS TFIGEHYVHV NATYVNVKCV APYPSLLPSQ DNIDGEGNT
//
ID   FGFR1_MOUSE             Reviewed;         822 AA.
AC   P16092; Q01736; Q61562; Q80T10;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 2.
DT   08-MAR-2011, entry version 130.
DE   RecName: Full=Basic fibroblast growth factor receptor 1;
DE            Short=FGFR-1;
DE            Short=bFGF-R-1;
DE            EC=2.7.10.1;
DE   AltName: Full=MFR;
DE   AltName: Full=Proto-oncogene c-Fgr;
DE   AltName: CD_antigen=CD331;
DE   Flags: Precursor;
GN   Name=Fgfr1; Synonyms=Flg;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=90160373; PubMed=1689490; DOI=10.1073/pnas.87.4.1596;
RA   Reid H.H., Wilks A.F., Bernard O.;
RT   "Two forms of the basic fibroblast growth factor receptor-like mRNA
RT   are expressed in the developing mouse brain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:1596-1600(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=90265603; PubMed=2161096;
RA   Safran A., Avivi A., Orr-Urtereger A., Neufeld G., Lonai P., Givol D.,
RA   Yarden Y.;
RT   "The murine flg gene encodes a receptor for fibroblast growth
RT   factor.";
RL   Oncogene 5:635-643(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX   MEDLINE=91207411; PubMed=1708247; DOI=10.1016/0006-291X(91)90885-B;
RA   Kouhara H., Kasayama S., Saito H., Matsumoto K., Sato B.;
RT   "Expression cDNA cloning of fibroblast growth factor (FGF) receptor in
RT   mouse breast cancer cells: a variant form in FGF-responsive
RT   transformed cells.";
RL   Biochem. Biophys. Res. Commun. 176:31-37(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   MEDLINE=90272715; PubMed=2161540; DOI=10.1073/pnas.87.11.4378;
RA   Mansukhani A., Moscatelli D., Talarico D., Levytska V., Basilico C.;
RT   "A murine fibroblast growth factor (FGF) receptor expressed in CHO
RT   cells is activated by basic FGF and Kaposi FGF.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:4378-4382(1990).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-15, AND ALTERNATIVE SPLICING.
RX   MEDLINE=95100926; PubMed=7802632; DOI=10.1006/bbrc.1994.2773;
RA   Harada T., Saito H., Kouhara H., Kurebayashi S., Kasayama S.,
RA   Terakawa N., Kishimoto T., Sato B.;
RT   "Murine fibroblast growth factor receptor 1 gene generates multiple
RT   messenger RNAs containing two open reading frames via alternative
RT   splicing.";
RL   Biochem. Biophys. Res. Commun. 205:1057-1063(1994).
RN   [7]
RP   INTERACTION WITH SHB.
RX   PubMed=12181353; DOI=10.1091/mbc.E02-02-0103;
RA   Cross M.J., Lu L., Magnusson P., Nyqvist D., Holmqvist K., Welsh M.,
RA   Claesson-Welsh L.;
RT   "The Shb adaptor protein binds to tyrosine 766 in the FGFR-1 and
RT   regulates the Ras/MEK/MAPK pathway via FRS2 phosphorylation in
RT   endothelial cells.";
RL   Mol. Biol. Cell 13:2881-2893(2002).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH KL AND FGF23.
RX   PubMed=17086194; DOI=10.1038/nature05315;
RA   Urakawa I., Yamazaki Y., Shimada T., Iijima K., Hasegawa H., Okawa K.,
RA   Fujita T., Fukumoto S., Yamashita T.;
RT   "Klotho converts canonical FGF receptor into a specific receptor for
RT   FGF23.";
RL   Nature 444:770-774(2006).
RN   [9]
RP   INTERACTION WITH KLB.
RX   PubMed=17452648; DOI=10.1073/pnas.0701600104;
RA   Ogawa Y., Kurosu H., Yamamoto M., Nandi A., Rosenblatt K.P., Goetz R.,
RA   Eliseenkova A.V., Mohammadi M., Kuro-o M.;
RT   "BetaKlotho is required for metabolic activity of fibroblast growth
RT   factor 21.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7432-7437(2007).
RN   [10]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-317, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Receptor for basic fibroblast growth factor. A shorter
CC       form of the receptor could be a receptor for FGF1 (aFGF). Receptor
CC       for FGF23 in the presence of KL.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBUNIT: Interacts with SHB and KLB. Interacts with KL and FGF23.
CC       Interacts with GRB10 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P16092-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P16092-2; Sequence=VSP_002962;
CC       Name=3; Synonyms=Variant;
CC         IsoId=P16092-3; Sequence=VSP_002961, VSP_002963;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Fibroblast growth factor receptor subfamily.
CC   -!- SIMILARITY: Contains 3 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; M28998; AAA37290.1; -; mRNA.
DR   EMBL; X51893; CAA36175.1; -; mRNA.
DR   EMBL; M65053; AAA37620.1; -; mRNA.
DR   EMBL; M33760; AAA37622.1; -; mRNA.
DR   EMBL; AK028354; BAC25899.1; -; mRNA.
DR   EMBL; S74765; AAB32845.1; ALT_SEQ; mRNA.
DR   IPI; IPI00130549; -.
DR   IPI; IPI00399479; -.
DR   IPI; IPI00466590; -.
DR   PIR; A34849; TVMSFG.
DR   PIR; JH0393; JH0393.
DR   RefSeq; NP_001073377.1; NM_001079908.1.
DR   RefSeq; NP_001073378.1; NM_001079909.1.
DR   RefSeq; NP_034336.2; NM_010206.2.
DR   UniGene; Mm.265716; -.
DR   PDB; 2CKN; NMR; -; A=25-119.
DR   PDBsum; 2CKN; -.
DR   ProteinModelPortal; P16092; -.
DR   SMR; P16092; 25-359, 457-764.
DR   DIP; DIP-6033N; -.
DR   MINT; MINT-2635590; -.
DR   STRING; P16092; -.
DR   PhosphoSite; P16092; -.
DR   PRIDE; P16092; -.
DR   Ensembl; ENSMUST00000084027; ENSMUSP00000081041; ENSMUSG00000031565.
DR   Ensembl; ENSMUST00000110623; ENSMUSP00000106253; ENSMUSG00000031565.
DR   Ensembl; ENSMUST00000118241; ENSMUSP00000112496; ENSMUSG00000031565.
DR   GeneID; 14182; -.
DR   KEGG; mmu:14182; -.
DR   UCSC; uc009lfy.1; mouse.
DR   UCSC; uc009lga.1; mouse.
DR   CTD; 14182; -.
DR   MGI; MGI:95522; Fgfr1.
DR   eggNOG; roNOG13193; -.
DR   HOVERGEN; HBG000345; -.
DR   OMA; VIVYKMK; -.
DR   OrthoDB; EOG4BCDMC; -.
DR   BRENDA; 2.7.10.1; 244.
DR   NextBio; 285378; -.
DR   ArrayExpress; P16092; -.
DR   Bgee; P16092; -.
DR   CleanEx; MM_FGFR1; -.
DR   CleanEx; MM_FLG; -.
DR   Genevestigator; P16092; -.
DR   GermOnline; ENSMUSG00000031565; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017134; F:fibroblast growth factor binding; IPI:UniProtKB.
DR   GO; GO:0005007; F:fibroblast growth factor receptor activity; IDA:MGI.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0001525; P:angiogenesis; IGI:MGI.
DR   GO; GO:0060117; P:auditory receptor cell development; IMP:MGI.
DR   GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IMP:MGI.
DR   GO; GO:0048469; P:cell maturation; IMP:MGI.
DR   GO; GO:0002062; P:chondrocyte differentiation; IGI:MGI.
DR   GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
DR   GO; GO:0035607; P:fibroblast growth factor receptor signaling pathway involved in orbitofrontal cortex development; IMP:UniProtKB.
DR   GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR   GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR   GO; GO:0060484; P:lung-associated mesenchyme development; IGI:MGI.
DR   GO; GO:0048762; P:mesenchymal cell differentiation; IGI:MGI.
DR   GO; GO:0030901; P:midbrain development; IGI:MGI.
DR   GO; GO:0042474; P:middle ear morphogenesis; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptosis; IMP:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
DR   GO; GO:0001759; P:organ induction; IMP:MGI.
DR   GO; GO:0042473; P:outer ear morphogenesis; IMP:MGI.
DR   GO; GO:0048339; P:paraxial mesoderm development; IGI:MGI.
DR   GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IGI:MGI.
DR   GO; GO:0045787; P:positive regulation of cell cycle; IMP:UniProtKB.
DR   GO; GO:0090080; P:positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway; IGI:MGI.
DR   GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0060665; P:regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling; IDA:MGI.
DR   GO; GO:0048378; P:regulation of lateral mesodermal cell fate specification; IGI:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR   GO; GO:0001657; P:ureteric bud development; IGI:MGI.
DR   GO; GO:0021847; P:ventricular zone neuroblast division; IMP:UniProtKB.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR016248; Tyr_kinase_fibroblast_GF_rcpt.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3.
DR   Pfam; PF07679; I-set; 3.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PIRSF; PIRSF000628; FGFR; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00408; IGc2; 3.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Disulfide bond;
KW   Glycoprotein; Heparin-binding; Immunoglobulin domain; Kinase;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Receptor; Repeat;
KW   Signal; Transferase; Transmembrane; Transmembrane helix;
KW   Tyrosine-protein kinase.
FT   SIGNAL        1     21       Potential.
FT   CHAIN        22    822       Basic fibroblast growth factor receptor
FT                                1.
FT                                /FTId=PRO_0000016781.
FT   TOPO_DOM     22    376       Extracellular (Potential).
FT   TRANSMEM    377    397       Helical; (Potential).
FT   TOPO_DOM    398    822       Cytoplasmic (Potential).
FT   DOMAIN       25    119       Ig-like C2-type 1.
FT   DOMAIN      158    246       Ig-like C2-type 2.
FT   DOMAIN      255    357       Ig-like C2-type 3.
FT   DOMAIN      478    767       Protein kinase.
FT   NP_BIND     484    492       ATP (By similarity).
FT   REGION      160    177       Heparin-binding.
FT   ACT_SITE    623    623       Proton acceptor (By similarity).
FT   BINDING     514    514       ATP (By similarity).
FT   SITE        766    766       Mediates interaction with PLC-gamma and
FT                                SHB (By similarity).
FT   MOD_RES     653    653       Phosphotyrosine (By similarity).
FT   MOD_RES     654    654       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   CARBOHYD     77     77       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    117    117       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    227    227       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    240    240       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    264    264       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    296    296       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    317    317       N-linked (GlcNAc...).
FT   CARBOHYD    330    330       N-linked (GlcNAc...) (Potential).
FT   DISULFID     55    101       Potential.
FT   DISULFID    178    230       Potential.
FT   DISULFID    277    341       Potential.
FT   VAR_SEQ      30     30       Q -> QGSSSWPLWVAAA (in isoform 3).
FT                                /FTId=VSP_002961.
FT   VAR_SEQ      31    119       Missing (in isoform 2).
FT                                /FTId=VSP_002962.
FT   VAR_SEQ     148    149       Missing (in isoform 3).
FT                                /FTId=VSP_002963.
FT   CONFLICT    229    229       T -> S (in Ref. 4; AAA37622).
FT   CONFLICT    256    258       ILQ -> HPS (in Ref. 1 and 3).
FT   CONFLICT    270    270       G -> A (in Ref. 4; AAA37622).
FT   CONFLICT    387    387       I -> M (in Ref. 3; AAA37620).
FT   CONFLICT    440    440       G -> A (in Ref. 2; CAA36175).
FT   CONFLICT    508    508       V -> L (in Ref. 3; AAA37620).
FT   CONFLICT    544    544       I -> M (in Ref. 4; AAA37622).
FT   CONFLICT    756    756       R -> H (in Ref. 1; AAA37290).
FT   CONFLICT    765    765       E -> D (in Ref. 4; AAA37622).
FT   STRAND       43     45
FT   STRAND       51     54
FT   STRAND       57     60
FT   STRAND       63     68
FT   STRAND       77     81
FT   STRAND       83     90
FT   HELIX        93     95
FT   STRAND       96    105
FT   STRAND      108    118
SQ   SEQUENCE   822 AA;  91981 MW;  D5A4695FA680926B CRC64;
     MWGWKCLLFW AVLVTATLCT ARPAPTLPEQ AQPWGVPVEV ESLLVHPGDL LQLRCRLRDD
     VQSINWLRDG VQLVESNRTR ITGEEVEVRD SIPADSGLYA CVTSSPSGSD TTYFSVNVSD
     ALPSSEDDDD DDDSSSEEKE TDNTKPNRRP VAPYWTSPEK MEKKLHAVPA AKTVKFKCPS
     SGTPNPTLRW LKNGKEFKPD HRIGGYKVRY ATWSIIMDSV VPSDKGNYTC IVENEYGSIN
     HTYQLDVVER SPHRPILQAG LPANKTVALG SNVEFMCKVY SDPQPHIQWL KHIEVNGSKI
     GPDNLPYVQI LKTAGVNTTD KEMEVLHLRN VSFEDAGEYT CLAGNSIGLS HHSAWLTVLE
     ALEERPAVMT SPLYLEIIIY CTGAFLISCM LGSVIIYKMK SGTKKSDFHS QMAVHKLAKS
     IPLRRQVTVS ADSSASMNSG VLLVRPSRLS SSGTPMLAGV SEYELPEDPR WELPRDRLVL
     GKPLGEGCFG QVVLAEAIGL DKDKPNRVTK VAVKMLKSDA TEKDLSDLIS EMEMMKMIGK
     HKNIINLLGA CTQDGPLYVI VEYASKGNLR EYLQARRPPG LEYCYNPSHN PEEQLSSKDL
     VSCAYQVARG MEYLASKKCI HRDLAARNVL VTEDNVMKIA DFGLARDIHH IDYYKKTTNG
     RLPVKWMAPE ALFDRIYTHQ SDVWSFGVLL WEIFTLGGSP YPGVPVEELF KLLKEGHRMD
     KPSNCTNELY MMMRDCWHAV PSQRPTFKQL VEDLDRIVAL TSNQEYLDLS IPLDQYSPSF
     PDTRSSTCSS GEDSVFSHEP LPEEPCLPRH PTQLANSGLK RR
//
ID   LDHB_MOUSE              Reviewed;         334 AA.
AC   P16125; Q545Y4;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 109.
DE   RecName: Full=L-lactate dehydrogenase B chain;
DE            Short=LDH-B;
DE            EC=1.1.1.27;
DE   AltName: Full=LDH heart subunit;
DE            Short=LDH-H;
GN   Name=Ldhb; Synonyms=Ldh-2, Ldh2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90249362; PubMed=2338075;
RX   DOI=10.1111/j.1432-1033.1990.tb15479.x;
RA   Hiraoka B.Y., Sharief F.S., Yang Y.W., Li W.H., Li S.S.-L.;
RT   "The cDNA and protein sequences of mouse lactate dehydrogenase B.
RT   Molecular evolution of vertebrate lactate dehydrogenase genes A
RT   (muscle), B (heart) and C (testis).";
RL   Eur. J. Biochem. 189:215-220(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 24-77; 120-127; 159-170 AND 271-299, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- CATALYTIC ACTIVITY: (S)-lactate + NAD(+) = pyruvate + NADH.
CC   -!- PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-
CC       lactate from pyruvate: step 1/1.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. LDH family.
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DR   EMBL; X51905; CAA36185.1; -; mRNA.
DR   EMBL; AK002257; BAB21970.1; -; mRNA.
DR   EMBL; AK019391; BAB31697.1; -; mRNA.
DR   EMBL; AK131637; BAE20732.1; -; mRNA.
DR   EMBL; BC046755; AAH46755.1; -; mRNA.
DR   IPI; IPI00229510; -.
DR   PIR; S09954; S09954.
DR   RefSeq; NP_032518.1; NM_008492.2.
DR   UniGene; Mm.9745; -.
DR   ProteinModelPortal; P16125; -.
DR   SMR; P16125; 2-333.
DR   STRING; P16125; -.
DR   PhosphoSite; P16125; -.
DR   REPRODUCTION-2DPAGE; P16125; -.
DR   REPRODUCTION-2DPAGE; Q545Y4; -.
DR   UCD-2DPAGE; P16125; -.
DR   PRIDE; P16125; -.
DR   Ensembl; ENSMUST00000032373; ENSMUSP00000032373; ENSMUSG00000030246.
DR   GeneID; 16832; -.
DR   KEGG; mmu:16832; -.
DR   UCSC; uc009epj.1; mouse.
DR   CTD; 16832; -.
DR   MGI; MGI:96763; Ldhb.
DR   eggNOG; maNOG09588; -.
DR   HOGENOM; HBG566126; -.
DR   HOVERGEN; HBG000462; -.
DR   InParanoid; P16125; -.
DR   OMA; KVVDSAY; -.
DR   OrthoDB; EOG4RR6HR; -.
DR   PhylomeDB; P16125; -.
DR   BRENDA; 1.1.1.27; 244.
DR   NextBio; 290742; -.
DR   ArrayExpress; P16125; -.
DR   Bgee; P16125; -.
DR   CleanEx; MM_LDHB; -.
DR   Genevestigator; P16125; -.
DR   GermOnline; ENSMUSG00000030246; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0004459; F:L-lactate dehydrogenase activity; IDA:MGI.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR011304; L-lactate_DH.
DR   InterPro; IPR018177; L-lactate_DH_AS.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.90.110.10; lact_mal_DH; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   PRINTS; PR00086; LLDHDRGNASE.
DR   SUPFAM; SSF56327; Lactate_DH/Glyco_hydro_4_C; 1.
DR   TIGRFAMs; TIGR01771; L-LDH-NAD; 1.
DR   PROSITE; PS00064; L_LDH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Glycolysis; NAD;
KW   Oxidoreductase; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    334       L-lactate dehydrogenase B chain.
FT                                /FTId=PRO_0000168461.
FT   NP_BIND      30     58       NAD (By similarity).
FT   ACT_SITE    194    194       Proton acceptor (By similarity).
FT   BINDING     100    100       NAD (By similarity).
FT   BINDING     107    107       Substrate (By similarity).
FT   BINDING     139    139       NAD or substrate (By similarity).
FT   BINDING     170    170       Substrate (By similarity).
FT   BINDING     249    249       Substrate (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       7      7       N6-acetyllysine (By similarity).
FT   MOD_RES      58     58       N6-acetyllysine (By similarity).
FT   MOD_RES     119    119       N6-acetyllysine (By similarity).
FT   MOD_RES     240    240       Phosphotyrosine.
FT   MOD_RES     248    248       Phosphotyrosine (By similarity).
FT   MOD_RES     249    249       Phosphothreonine (By similarity).
FT   MOD_RES     319    319       N6-acetyllysine (By similarity).
FT   MOD_RES     329    329       N6-acetyllysine (By similarity).
SQ   SEQUENCE   334 AA;  36572 MW;  86E6CDCDD251285D CRC64;
     MATLKEKLIA SVADDEAAVP NNKITVVGVG QVGMACAISI LGKSLADELA LVDVLEDKLK
     GEMMDLQHGS LFLQTPKIVA DKDYSVTANS KIVVVTAGVR QQEGESRLNL VQRNVNVFKF
     IIPQIVKYSP DCTIIVVSNP VDILTYVTWK LSGLPKHRVI GSGCNLDSAR FRYLMAEKLG
     IHPSSCHGWI LGEHGDSSVA VWSGVNVAGV SLQELNPEMG TDNDSENWKE VHKMVVDSAY
     EVIKLKGYTN WAIGLSVADL IESMLKNLSR IHPVSTMVKG MYGIENEVFL SLPCILNARG
     LTSVINQKLK DDEVAQLRKS ADTLWDIQKD LKDL
//
ID   SRP14_MOUSE             Reviewed;         110 AA.
AC   P16254; Q3TIK2;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Signal recognition particle 14 kDa protein;
DE            Short=SRP14;
GN   Name=Srp14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-19 AND 77-95.
RX   MEDLINE=90099341; PubMed=2557625; DOI=10.1073/pnas.86.24.9747;
RA   Strub K., Walter P.;
RT   "Isolation of a cDNA clone of the 14-kDa subunit of the signal
RT   recognition particle by cross-hybridization of differently primed
RT   polymerase chain reactions.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:9747-9751(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Hippocampus, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) IN COMPLEX WITH SRP9.
RX   MEDLINE=97377014; PubMed=9233785; DOI=10.1093/emboj/16.13.3757;
RA   Birse D.E., Kapp U., Strub K., Cusack S., Aaberg A.;
RT   "The crystal structure of the signal recognition particle Alu RNA
RT   binding heterodimer, SRP9/14.";
RL   EMBO J. 16:3757-3766(1997).
CC   -!- FUNCTION: Signal-recognition-particle assembly has a crucial role
CC       in targeting secretory proteins to the rough endoplasmic reticulum
CC       membrane. SRP9 together with SRP14 and the Alu portion of the SRP
CC       RNA, constitutes the elongation arrest domain of SRP. The complex
CC       of SRP9 and SRP14 is required for SRP RNA binding.
CC   -!- SUBUNIT: Signal recognition particle consists of a 7S RNA molecule
CC       of 300 nucleotides and six protein subunits: SRP72, SRP68, SRP54,
CC       SRP19, SRP14 and SRP9.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the SRP14 family.
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DR   EMBL; M29264; AAA40136.1; -; mRNA.
DR   EMBL; AK019310; BAB31658.1; -; mRNA.
DR   EMBL; AK156845; BAE33873.1; -; mRNA.
DR   EMBL; AK167821; BAE39844.1; -; mRNA.
DR   EMBL; AK168144; BAE40110.1; -; mRNA.
DR   EMBL; BC021537; AAH21537.1; -; mRNA.
DR   IPI; IPI00132418; -.
DR   PIR; B34501; B34501.
DR   RefSeq; NP_033299.1; NM_009273.4.
DR   RefSeq; XP_003086285.1; XM_003086237.1.
DR   UniGene; Mm.363404; -.
DR   PDB; 1914; X-ray; 2.53 A; A=1-110.
DR   PDBsum; 1914; -.
DR   ProteinModelPortal; P16254; -.
DR   SMR; P16254; 1-104.
DR   STRING; P16254; -.
DR   PhosphoSite; P16254; -.
DR   PRIDE; P16254; -.
DR   Ensembl; ENSMUST00000009693; ENSMUSP00000009693; ENSMUSG00000009549.
DR   GeneID; 100504988; -.
DR   GeneID; 20813; -.
DR   KEGG; mmu:100504988; -.
DR   KEGG; mmu:20813; -.
DR   UCSC; uc008lsa.1; mouse.
DR   CTD; 20813; -.
DR   MGI; MGI:107169; Srp14.
DR   GeneTree; ENSGT00390000008496; -.
DR   HOGENOM; HBG629003; -.
DR   HOVERGEN; HBG057435; -.
DR   InParanoid; P16254; -.
DR   OMA; PVPRKGH; -.
DR   OrthoDB; EOG415GG0; -.
DR   PhylomeDB; P16254; -.
DR   NextBio; 299537; -.
DR   ArrayExpress; P16254; -.
DR   Bgee; P16254; -.
DR   CleanEx; MM_SRP14; -.
DR   Genevestigator; P16254; -.
DR   GermOnline; ENSMUSG00000009549; Mus musculus.
DR   GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IEA:UniProtKB-KW.
DR   GO; GO:0008312; F:7S RNA binding; IEA:InterPro.
DR   GO; GO:0030942; F:endoplasmic reticulum signal peptide binding; IEA:InterPro.
DR   GO; GO:0045900; P:negative regulation of translational elongation; IEA:InterPro.
DR   GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR   InterPro; IPR003210; Signal_recog_particle_SRP14.
DR   InterPro; IPR009018; Signal_recog_particle_SRP9/14.
DR   Gene3D; G3DSA:3.30.720.10; Signal_recog_particle_SRP9/14; 1.
DR   PANTHER; PTHR12013; SRP14; 1.
DR   Pfam; PF02290; SRP14; 1.
DR   ProDom; PD009170; Signal_recog_particle_SRP14; 1.
DR   SUPFAM; SSF54762; SRP9/14; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW   Ribonucleoprotein; RNA-binding; Signal recognition particle.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    110       Signal recognition particle 14 kDa
FT                                protein.
FT                                /FTId=PRO_0000135191.
FT   MOD_RES      45     45       Phosphoserine.
FT   HELIX         6     19
FT   TURN         20     20
FT   STRAND       26     33
FT   STRAND       55     61
FT   STRAND       66     72
FT   TURN         73     74
FT   HELIX        76     90
SQ   SEQUENCE   110 AA;  12510 MW;  95EB062DBC0CCA25 CRC64;
     MVLLESEQFL TELTRLFQKC RSSGSVFITL KKYDGRTKPI PRKSSVEGLE PAENKCLLRA
     TDGKRKISTV VSSKEVNKFQ MAYSNLLRAN MDGLKKRDKK NKSKKSKPAQ
//
ID   B3A3_MOUSE              Reviewed;        1227 AA.
AC   P16283;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   11-JAN-2011, entry version 98.
DE   RecName: Full=Anion exchange protein 3;
DE            Short=AE 3;
DE            Short=Anion exchanger 3;
DE   AltName: Full=Neuronal band 3-like protein;
DE   AltName: Full=Solute carrier family 4 member 3;
GN   Name=Slc4a3; Synonyms=Ae3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90075236; PubMed=2686841; DOI=10.1016/0092-8674(89)90615-6;
RA   Kopito R.R., Lee B.S., Simmons D.M., Lindsey A.E., Morgans C.W.,
RA   Schneider K.;
RT   "Regulation of intracellular pH by a neuronal homolog of the
RT   erythrocyte anion exchanger.";
RL   Cell 59:927-937(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX   MEDLINE=94171936; PubMed=8126106;
RA   Morgans C.W., Kopito R.R.;
RT   "Generation of truncated brain AE3 isoforms by alternate mRNA
RT   processing.";
RL   J. Cell Sci. 106:1275-1282(1993).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170; SER-198 AND
RP   SER-296, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Plasma membrane anion exchange protein.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=FL-AE3;
CC         IsoId=P16283-1; Sequence=Displayed;
CC       Name=311-AE3;
CC         IsoId=P16283-2; Sequence=VSP_000464, VSP_000465;
CC       Name=14-AE3;
CC         IsoId=P16283-3; Sequence=VSP_000466, VSP_000467;
CC   -!- TISSUE SPECIFICITY: Neuronal.
CC   -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
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DR   EMBL; M28383; AAA37184.1; -; mRNA.
DR   EMBL; S69314; AAB30140.1; -; mRNA.
DR   IPI; IPI00470963; -.
DR   IPI; IPI00875624; -.
DR   IPI; IPI00919051; -.
DR   PIR; A33638; A33638.
DR   UniGene; Mm.5053; -.
DR   ProteinModelPortal; P16283; -.
DR   SMR; P16283; 318-643, 691-732.
DR   STRING; P16283; -.
DR   PRIDE; P16283; -.
DR   Ensembl; ENSMUST00000027415; ENSMUSP00000027415; ENSMUSG00000006576.
DR   Ensembl; ENSMUST00000113545; ENSMUSP00000109173; ENSMUSG00000006576.
DR   UCSC; uc007bpv.1; mouse.
DR   MGI; MGI:109350; Slc4a3.
DR   eggNOG; roNOG11460; -.
DR   HOVERGEN; HBG004326; -.
DR   PhylomeDB; P16283; -.
DR   ArrayExpress; P16283; -.
DR   Bgee; P16283; -.
DR   Genevestigator; P16283; -.
DR   GermOnline; ENSMUSG00000006576; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
DR   InterPro; IPR001717; Anion_exchange.
DR   InterPro; IPR002979; Anion_exchange_3.
DR   InterPro; IPR018241; Anion_exchange_CS.
DR   InterPro; IPR011531; HCO3_transpt_C.
DR   InterPro; IPR013769; HCO3_transpt_cyt.
DR   InterPro; IPR003020; HCO3_transpt_euk.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   Gene3D; G3DSA:3.40.1100.10; HCO3_transpt_cyt; 1.
DR   PANTHER; PTHR11453:SF15; Anion_exhngr3; 1.
DR   PANTHER; PTHR11453; HCO3_transpt_euk; 1.
DR   Pfam; PF07565; Band_3_cyto; 1.
DR   Pfam; PF00955; HCO3_cotransp; 2.
DR   PRINTS; PR00165; ANIONEXCHNGR.
DR   PRINTS; PR01189; ANIONEXHNGR3.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   SUPFAM; SSF55804; PTrfase/Anion_transptr; 1.
DR   TIGRFAMs; TIGR00834; ae; 1.
DR   PROSITE; PS00219; ANION_EXCHANGER_1; 1.
DR   PROSITE; PS00220; ANION_EXCHANGER_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Anion exchange; Antiport; Glycoprotein;
KW   Ion transport; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1   1227       Anion exchange protein 3.
FT                                /FTId=PRO_0000079220.
FT   TOPO_DOM      1    707       Cytoplasmic.
FT   TRANSMEM    708    730       Helical; (Potential).
FT   TRANSMEM    736    773       Helical; (Potential).
FT   TRANSMEM    793    815       Helical; (Potential).
FT   TRANSMEM    825    846       Helical; (Potential).
FT   TRANSMEM    888    905       Helical; (Potential).
FT   TOPO_DOM    906    920       Cytoplasmic (Potential).
FT   TRANSMEM    921    941       Helical; (Potential).
FT   TRANSMEM    975    997       Helical; (Potential).
FT   TRANSMEM   1023   1044       Helical; (Potential).
FT   TRANSMEM   1078   1123       Helical; (Potential).
FT   TRANSMEM   1150   1186       Helical; (Potential).
FT   REGION      708   1227       Membrane (anion exchange).
FT   COMPBIAS    135    145       Poly-Glu.
FT   MOD_RES     170    170       Phosphoserine.
FT   MOD_RES     198    198       Phosphoserine.
FT   MOD_RES     296    296       Phosphoserine.
FT   MOD_RES     950    950       Phosphothreonine (By similarity).
FT   MOD_RES     953    953       Phosphothreonine (By similarity).
FT   MOD_RES     956    956       Phosphoserine (By similarity).
FT   LIPID      1160   1160       S-palmitoyl cysteine (By similarity).
FT   CARBOHYD    868    868       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     381    391       AALLDLEQTTL -> RAFWAGNESLL (in isoform
FT                                311-AE3).
FT                                /FTId=VSP_000464.
FT   VAR_SEQ     392   1227       Missing (in isoform 311-AE3).
FT                                /FTId=VSP_000465.
FT   VAR_SEQ     487    503       KPLHMPGGDGHRGKSLK -> FCVLRSPSPCLGETVTEGKA
FT                                (in isoform 14-AE3).
FT                                /FTId=VSP_000466.
FT   VAR_SEQ     504   1227       Missing (in isoform 14-AE3).
FT                                /FTId=VSP_000467.
SQ   SEQUENCE   1227 AA;  135164 MW;  D5BEC46E03F4251C CRC64;
     MANGVIPPPG GASPLPQVRV PLEEPPLGPD VEEEDDDLGK TLAVSRFGDL ISKTPAWDPE
     KPSRSYSERD FEFHRHTSHH THHPLSARLP PPHKLRRPPP TSARHTRRKR KKEKTSAPPS
     EGTPPIQEEG GAGAEEEEEE EEEEEGESEA EPVEPLPPGP PQKAKFSIGS DEDDSPGLPV
     KAPCAKALPS VGLQSDQSPQ RSGSSPSPRA RASRISTEKS RPWSPSASYD LRERLCPGSA
     LGNPGPEQRV PTDEAEAQML GSADLDDMKS HRLEDNPGVR RHLVKKPSRI QGGRGSPSGL
     APILRRKKKK KKLDRRPHEV FVELNELMLD RSQEPHWRET ARWIKFEEDV EEETERWGKP
     HVASLSFRSL LELRRTIAQG AALLDLEQTT LPGIAHLVVE TMIVSDQIRP EDRASVLRTL
     LLKHSHPNDD KDSGFFPRNP SSSSVNSVLG NHHPTPSHGP DGAVPTMADD QGEPAPLWPH
     DPDAKEKPLH MPGGDGHRGK SLKLLEKIPE DAEATVVLVG CVPFLEQPAG AFVRLSEAVL
     LESVLEVPVP VRFLFVMLGP SHTSTDYHEL GRSIATLMSD KLFHEAAYQA DDRQDLLGAI
     SEFLDGSIVI PPSEVEGRDL LRSVAAFQRE LLRKRREREQ TKVEMTTRGG YAAPGKELSL
     EMGGSEATSE DDPLQRTGSV FGGLVRDVKR RYPHYPSDLR DALHSQCVAA VLFIYFAALS
     PAITFGGLLG EKTEGLMGVS ELIVSTAVLG VLFSLLGAQP LLVVGFSGPL LVFEEAFFKF
     CRAQDLEYLT GRVWVGLWLV VFVLALVAAE GTFLVRYISP FTQEIFAFLI SLIFIYETFH
     KLYKVFTEHP LLPFYPPDEA LETGLELNSS ALPPTEGPPG PRNQPNTALL SLILMLGTFL
     IAFFLRKFRN SRFLGGKARR IIGDFGIPIS ILVMVLVDYS ITDTYTQKLT VPTGLSVTSP
     HKRTWFIPPL GSARPFPPWM MVAAAVPALL VLILIFMETQ ITALIVSQKA RRLLKGSGFH
     LDLLLIGSLG GLCGLFGLPW LTAATVRSVT HVNALTVMRT AIAPGDKPQI QEVREQRVTG
     VLIASLVGLS IVMGAVLRRI PLAVLFGIFL YMGVTSLSGI QLSQRLLLIF MPAKHHPEQP
     YVTKVKTWRI DLFTCIQLGC IALLWVVKST AASLAFPFLL LLTVPLSGCL LPRLFQDREL
     QALDSEDAEP NFDEDGQDEY NELHMPV
//
ID   GBRA6_MOUSE             Reviewed;         453 AA.
AC   P16305; Q9R0V3; Q9R0V4; Q9R0V5;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   04-MAY-2001, sequence version 2.
DT   08-MAR-2011, entry version 109.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit alpha-6;
DE   AltName: Full=GABA(A) receptor subunit alpha-6;
DE   Flags: Precursor;
GN   Name=Gabra6; Synonyms=Gabra-6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=90355175; PubMed=2167378; DOI=10.1016/0022-2836(90)90276-R;
RA   Kato K.;
RT   "Novel GABAA receptor alpha subunit is expressed only in cerebellar
RT   granule cells.";
RL   J. Mol. Biol. 214:619-624(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2; 3 AND 4).
RC   STRAIN=129/Sv;
RA   Glencorse T.A., Montgomery K.I., Livingston D., Davies R.W.;
RT   "Characterization of the murine GABAA receptor alpha 6 subunit gene.";
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and DBA/2J; TISSUE=Cerebellum;
RA   Buck K.J., Lischka T.R.;
RT   "Detection and ethanol regulation of two forms of the GABA-A receptor
RT   alpha-6 subunit in DBA/2J and C57BL/6J mice.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   INTERACTION WITH UBQLN1.
RX   MEDLINE=21419682; PubMed=11528422; DOI=10.1038/nn0901-908;
RA   Bedford F.K., Kittler J.T., Muller E., Thomas P., Uren J.M., Merlo D.,
RA   Wisden W., Triller A., Smart T.G., Moss S.J.;
RT   "GABA(A) receptor cell surface number and subunit stability are
RT   regulated by the ubiquitin-like protein Plic-1.";
RL   Nat. Neurosci. 4:908-916(2001).
CC   -!- FUNCTION: GABA, the major inhibitory neurotransmitter in the
CC       vertebrate brain, mediates neuronal inhibition by binding to the
CC       GABA/benzodiazepine receptor and opening an integral chloride
CC       channel.
CC   -!- SUBUNIT: Generally pentameric. There are five types of GABA(A)
CC       receptor chains: alpha, beta, gamma, delta, and rho. Binds UBQLN1.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane; Multi-pass membrane protein. Cell membrane; Multi-pass
CC       membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=P16305-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P16305-2; Sequence=VSP_000086;
CC       Name=3;
CC         IsoId=P16305-3; Sequence=VSP_000085;
CC       Name=4;
CC         IsoId=P16305-4; Sequence=VSP_000085, VSP_000086;
CC   -!- TISSUE SPECIFICITY: Only found in cerebellar granule cells.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
CC       family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily.
CC       GABRA6 sub-subfamily.
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DR   EMBL; X51986; CAA36244.1; -; mRNA.
DR   EMBL; U77411; AAD52001.1; -; Genomic_DNA.
DR   EMBL; U77409; AAD52001.1; JOINED; Genomic_DNA.
DR   EMBL; U77410; AAD52001.1; JOINED; Genomic_DNA.
DR   EMBL; U77411; AAD52002.1; -; Genomic_DNA.
DR   EMBL; U77409; AAD52002.1; JOINED; Genomic_DNA.
DR   EMBL; U77410; AAD52002.1; JOINED; Genomic_DNA.
DR   EMBL; U77411; AAD52003.1; -; Genomic_DNA.
DR   EMBL; U77409; AAD52003.1; JOINED; Genomic_DNA.
DR   EMBL; U77410; AAD52003.1; JOINED; Genomic_DNA.
DR   EMBL; U77411; AAD52004.1; -; Genomic_DNA.
DR   EMBL; U77409; AAD52004.1; JOINED; Genomic_DNA.
DR   EMBL; U77410; AAD52004.1; JOINED; Genomic_DNA.
DR   EMBL; AF256197; AAG28024.1; -; mRNA.
DR   EMBL; AF256198; AAG28025.1; -; mRNA.
DR   IPI; IPI00133501; -.
DR   IPI; IPI00230732; -.
DR   IPI; IPI00648214; -.
DR   IPI; IPI00857474; -.
DR   PIR; S11396; S11396.
DR   UniGene; Mm.4915; -.
DR   ProteinModelPortal; P16305; -.
DR   SMR; P16305; 269-328.
DR   STRING; P16305; -.
DR   PhosphoSite; P16305; -.
DR   PRIDE; P16305; -.
DR   Ensembl; ENSMUST00000020703; ENSMUSP00000020703; ENSMUSG00000020428.
DR   Ensembl; ENSMUST00000109286; ENSMUSP00000104909; ENSMUSG00000020428.
DR   MGI; MGI:95618; Gabra6.
DR   HOGENOM; HBG506497; -.
DR   HOVERGEN; HBG051707; -.
DR   InParanoid; P16305; -.
DR   OrthoDB; EOG4MPHQ4; -.
DR   ArrayExpress; P16305; -.
DR   Bgee; P16305; -.
DR   Genevestigator; P16305; -.
DR   GermOnline; ENSMUSG00000020428; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IEA:InterPro.
DR   InterPro; IPR006028; GABAA_rcpt.
DR   InterPro; IPR001390; GABAAa_rcpt.
DR   InterPro; IPR005436; GABBAa6_rcpt.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   Gene3D; G3DSA:2.70.170.10; Neur_chan_lig_bd; 1.
DR   PANTHER; PTHR18945; Neur_channel; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR01079; GABAARALPHA.
DR   PRINTS; PR01619; GABAARALPHA6.
DR   PRINTS; PR00253; GABAARECEPTR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF90112; Neu_channel_TM; 1.
DR   SUPFAM; SSF63712; Neur_chan_LBD; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Chloride;
KW   Chloride channel; Disulfide bond; Glycoprotein; Ion transport;
KW   Ionic channel; Ligand-gated ion channel; Membrane;
KW   Postsynaptic cell membrane; Receptor; Signal; Synapse; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     19       Potential.
FT   CHAIN        20    453       Gamma-aminobutyric acid receptor subunit
FT                                alpha-6.
FT                                /FTId=PRO_0000000448.
FT   TOPO_DOM     20    242       Extracellular (Probable).
FT   TRANSMEM    243    264       Helical; (Probable).
FT   TRANSMEM    269    290       Helical; (Probable).
FT   TRANSMEM    301    324       Helical; (Probable).
FT   TOPO_DOM    325    419       Cytoplasmic (Probable).
FT   TRANSMEM    420    441       Helical; (Probable).
FT   CARBOHYD     31     31       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    128    128       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    141    141       N-linked (GlcNAc...) (Potential).
FT   DISULFID    156    170       By similarity.
FT   VAR_SEQ       1     13       MVLLLPWLFIILW -> MRNMKDLEDFSR (in isoform
FT                                3 and isoform 4).
FT                                /FTId=VSP_000085.
FT   VAR_SEQ      76     85       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_000086.
SQ   SEQUENCE   453 AA;  51107 MW;  B0CC2F972908689D CRC64;
     MVLLLPWLFI ILWLENAQAQ LEDEGNFYSE NVSRILDNLL EGYDNRLRPG FGGAVTEVKT
     DIYVTSFGPV SDVEMEYTMD VFFRQTWTDE RLKFKGPAEI LSLNNLMVSK IWTPDTFFRN
     GKKSIAHNMT TPNKLFRLMQ NGTILYTMRL TINADCPMRL VNFPMDGHAC PLKFGSYAYP
     KTEIIYTWKK GPLYSVEVPE ESSSLLQYDL IGQTVSSETI KSNTGEYVIM TVYFHLQRKM
     GYFMIQIYTP CIMTVILSQV SFWINKESVP ARTVFGITTV LTMTTLSISA RHSLPKVSYA
     TAMDWFIAVC FAFVFSALIE FAAVNYFTNL QSQKAERQAQ TAATPPVAKS KASESLEAEI
     VVHSDSKYHL KKRISSLTLP IVPSSEASKA LSRTPILKST PVSPPLLLPA TGGTSKIDQY
     SRILFPVAFA GFNLVYWIVY LSKDTMEVSS TVE
//
ID   CN37_MOUSE              Reviewed;         420 AA.
AC   P16330; Q61424; Q8C7C9; Q91V42; Q923F3;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 3.
DT   08-MAR-2011, entry version 104.
DE   RecName: Full=2',3'-cyclic-nucleotide 3'-phosphodiesterase;
DE            Short=CNP;
DE            Short=CNPase;
DE            EC=3.1.4.37;
GN   Name=Cnp; Synonyms=Cnp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM CNPI).
RC   STRAIN=DBA;
RX   MEDLINE=90121227; PubMed=2558653; DOI=10.1016/0006-291X(89)92731-9;
RA   Monoh K., Kurihara T., Sakimura K., Takahashi Y.;
RT   "Structure of mouse 2',3'-cyclic-nucleotide 3'-phosphodiesterase
RT   gene.";
RL   Biochem. Biophys. Res. Commun. 165:1213-1220(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS CNPI AND CNPII).
RC   STRAIN=DBA; TISSUE=Brain;
RX   MEDLINE=90358801; PubMed=2167669; DOI=10.1016/0006-291X(90)90502-E;
RA   Kurihara T., Monoh K., Sakimura K., Takahashi Y.;
RT   "Alternative splicing of mouse brain 2',3'-cyclic-nucleotide 3'-
RT   phosphodiesterase mRNA.";
RL   Biochem. Biophys. Res. Commun. 170:1074-1081(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CNPI).
RC   STRAIN=ILS, and ISS;
RX   MEDLINE=21363810; PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CNPII).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-418 (ISOFORM CNPII).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   PROTEIN SEQUENCE OF 94-101; 103-112; 117-127; 130-150; 164-174;
RP   183-195; 203-216; 235-243; 261-274; 276-293; 356-368; 379-385 AND
RP   391-399.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-110 AND TYR-372, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- CATALYTIC ACTIVITY: Nucleoside 2',3'-cyclic phosphate + H(2)O =
CC       nucleoside 2'-phosphate.
CC   -!- SUBCELLULAR LOCATION: Membrane. Melanosome (By similarity).
CC       Note=Firmly bound to membrane structures of brain white matter.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=CNPII; Synonyms=DNAII;
CC         IsoId=P16330-1; Sequence=Displayed;
CC       Name=CNPI; Synonyms=DNAI;
CC         IsoId=P16330-2; Sequence=VSP_004172;
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
CC       family.
CC   -----------------------------------------------------------------------
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DR   EMBL; D38642; BAA07621.1; -; Genomic_DNA.
DR   EMBL; D38642; BAA07622.1; -; Genomic_DNA.
DR   EMBL; M31810; AAA37429.1; -; mRNA.
DR   EMBL; M58045; AAA37430.1; -; mRNA.
DR   EMBL; M58047; AAA37431.1; -; Genomic_DNA.
DR   EMBL; M58046; AAA37431.1; JOINED; Genomic_DNA.
DR   EMBL; AF332055; AAK56084.1; -; mRNA.
DR   EMBL; AF332056; AAK56085.1; -; mRNA.
DR   EMBL; BC005544; AAH05544.1; -; mRNA.
DR   EMBL; BC021904; AAH21904.1; -; mRNA.
DR   EMBL; AK050628; BAC34351.1; -; mRNA.
DR   IPI; IPI00229598; -.
DR   IPI; IPI00319602; -.
DR   PIR; A35708; ESMS32.
DR   RefSeq; NP_001139790.1; NM_001146318.1.
DR   RefSeq; NP_034053.2; NM_009923.2.
DR   UniGene; Mm.15711; -.
DR   ProteinModelPortal; P16330; -.
DR   SMR; P16330; 48-73, 184-398.
DR   MINT; MINT-1955077; -.
DR   STRING; P16330; -.
DR   PhosphoSite; P16330; -.
DR   PRIDE; P16330; -.
DR   Ensembl; ENSMUST00000103120; ENSMUSP00000099409; ENSMUSG00000006782.
DR   GeneID; 12799; -.
DR   KEGG; mmu:12799; -.
DR   CTD; 12799; -.
DR   MGI; MGI:88437; Cnp.
DR   eggNOG; roNOG11933; -.
DR   HOGENOM; HBG717781; -.
DR   HOVERGEN; HBG001451; -.
DR   InParanoid; P16330; -.
DR   OMA; QYQVVLV; -.
DR   OrthoDB; EOG4D52ZC; -.
DR   PhylomeDB; P16330; -.
DR   BRENDA; 3.1.4.37; 244.
DR   ArrayExpress; P16330; -.
DR   Bgee; P16330; -.
DR   CleanEx; MM_CNP; -.
DR   Genevestigator; P16330; -.
DR   GermOnline; ENSMUSG00000006782; Mus musculus.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0004113; F:2',3'-cyclic-nucleotide 3'-phosphodiesterase activity; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR   GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR   GO; GO:0001906; P:cell killing; IEA:InterPro.
DR   GO; GO:0009214; P:cyclic nucleotide catabolic process; IEA:InterPro.
DR   GO; GO:0016070; P:RNA metabolic process; IEA:InterPro.
DR   InterPro; IPR008431; CNPase.
DR   InterPro; IPR009097; RNA_ligase/cNuc_Pdiesterase.
DR   InterPro; IPR010488; Zeta_toxin_P-loop_hydrolase.
DR   PANTHER; PTHR10156; CNPase; 1.
DR   Pfam; PF05881; CNPase; 1.
DR   Pfam; PF06414; Zeta_toxin; 1.
DR   PIRSF; PIRSF000970; CNPase; 1.
DR   SUPFAM; SSF55144; Cyc_nuc_Pdiester; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing; Hydrolase; Membrane;
KW   Phosphoprotein.
FT   CHAIN         1    420       2',3'-cyclic-nucleotide 3'-
FT                                phosphodiesterase.
FT                                /FTId=PRO_0000089962.
FT   ACT_SITE    250    250       Proton acceptor (By similarity).
FT   ACT_SITE    329    329       Proton donor (By similarity).
FT   BINDING     252    252       Substrate (By similarity).
FT   BINDING     331    331       Substrate (By similarity).
FT   MOD_RES     110    110       Phosphotyrosine.
FT   MOD_RES     169    169       Phosphoserine (By similarity).
FT   MOD_RES     372    372       Phosphotyrosine.
FT   VAR_SEQ       1     20       Missing (in isoform CNPI).
FT                                /FTId=VSP_004172.
FT   CONFLICT    115    115       I -> M (in Ref. 1; BAA07621/BAA07622).
FT   CONFLICT    136    136       M -> L (in Ref. 1; BAA07621/BAA07622).
SQ   SEQUENCE   420 AA;  47123 MW;  2FAFFDE5F0E99EAB CRC64;
     MNTSFTRKSH TFLPKLFFRK MSSSGAKEKP ELQFPFLQDE DTVATLHECK TLFILRGLPG
     SGKSTLARLI LEKYHDGTKM VSADAYKIIP GSRADFSEAY KRLDEDLAGY CRRDIRVLVL
     DDTNHERERL DQLFEMADQY QYQVVLVEPK TAWRLDCAQL KEKNQWQLSA DDLKKLKPGL
     EKDFLPLYFG WFLTKKSSET LRKAGQVFLE ELGNHKAFKK ELRHFISGDE PKEKLELVSY
     FGKRPPGVLH CTTKFCDYGK AAGAEEYAQQ EVVKRSYGKA FKLSISALFV TPKTAGAQVV
     LTDQELQLWP SDLDKPSASE GLPPGSRAHV TLGCAADVQP VQTGLDLLDI LQQVKGGSQG
     EAVGELPRGK LYSLGKGRWM LSLTKKMEVK AIFTGYYGKG KPVPIHGSRK GGAMQICTII
//
ID   KCNA1_MOUSE             Reviewed;         495 AA.
AC   P16388;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   08-MAR-2011, entry version 106.
DE   RecName: Full=Potassium voltage-gated channel subfamily A member 1;
DE   AltName: Full=MBK1;
DE   AltName: Full=MKI;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv1.1;
GN   Name=Kcna1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=90161996; PubMed=2305265; DOI=10.1126/science.2305265;
RA   Chandy K.G., Williams C.B., Spencer R.H., Aguilar B.A., Ghanshani S.,
RA   Tempel B.L., Gutman G.A.;
RT   "A family of three mouse potassium channel genes with intronless
RT   coding regions.";
RL   Science 247:973-975(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=88189348; PubMed=2451788; DOI=10.1038/332837a0;
RA   Tempel B.L., Jan Y.N., Jan L.Y.;
RT   "Cloning of a probable potassium channel gene from mouse brain.";
RL   Nature 332:837-839(1988).
RN   [3]
RP   RNA EDITING OF POSITION 400.
RX   MEDLINE=22789647; PubMed=12907802; DOI=10.1126/science.1086763;
RA   Hoopengardner B., Bhalla T., Staber C., Reenan R.;
RT   "Nervous system targets of RNA editing identified by comparative
RT   genomics.";
RL   Science 301:832-836(2003).
CC   -!- FUNCTION: Mediates the voltage-dependent potassium ion
CC       permeability of excitable membranes. Assuming opened or closed
CC       conformations in response to the voltage difference across the
CC       membrane, the protein forms a potassium-selective channel through
CC       which potassium ions may pass in accordance with their
CC       electrochemical gradient.
CC   -!- SUBUNIT: Heterotetramer of potassium channel proteins. Binds
CC       KCNAB2 and PDZ domains of DLG1, DLG2 and DLG4 (By similarity).
CC       Interacts with LGI1 within a complex containing LGI1, KCNA4 and
CC       KCNAB1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- DOMAIN: The N-terminus may be important in determining the rate of
CC       inactivation of the channel while the tail may play a role in
CC       modulation of channel activity and/or targeting of the channel to
CC       specific subcellular compartments.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position.
CC   -!- PTM: Palmitoylated on Cys-243; which may be required for membrane
CC       targeting (By similarity).
CC   -!- RNA EDITING: Modified_positions=400; Note=Partially edited. RNA
CC       editing varies from 35% in the frontal cortex to 75% in the spinal
CC       chord.
CC   -!- SIMILARITY: Belongs to the potassium channel family. A (Shaker)
CC       (TC 1.A.1.2) subfamily. Kv1.1/KCNA1 sub-subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; M30439; AAA39711.1; -; Genomic_DNA.
DR   EMBL; Y00305; CAA68408.1; -; mRNA.
DR   IPI; IPI00133719; -.
DR   PIR; A40090; A40090.
DR   PIR; S09042; S09042.
DR   RefSeq; NP_034725.3; NM_010595.3.
DR   UniGene; Mm.40424; -.
DR   ProteinModelPortal; P16388; -.
DR   SMR; P16388; 3-419.
DR   STRING; P16388; -.
DR   PhosphoSite; P16388; -.
DR   PRIDE; P16388; -.
DR   Ensembl; ENSMUST00000055168; ENSMUSP00000055225; ENSMUSG00000047976.
DR   GeneID; 16485; -.
DR   KEGG; mmu:16485; -.
DR   NMPDR; fig|10090.3.peg.15284; -.
DR   UCSC; uc009dvb.1; mouse.
DR   CTD; 16485; -.
DR   MGI; MGI:96654; Kcna1.
DR   eggNOG; roNOG14095; -.
DR   HOGENOM; HBG445693; -.
DR   HOVERGEN; HBG052230; -.
DR   InParanoid; P16388; -.
DR   OMA; DDHECCE; -.
DR   OrthoDB; EOG4DR9CB; -.
DR   PhylomeDB; P16388; -.
DR   NextBio; 289783; -.
DR   ArrayExpress; P16388; -.
DR   Bgee; P16388; -.
DR   Genevestigator; P16388; -.
DR   GermOnline; ENSMUSG00000047976; Mus musculus.
DR   GO; GO:0044224; C:juxtaparanode region of axon; IDA:BHF-UCL.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003972; K_chnl_volt-dep_Kv1.
DR   InterPro; IPR004048; K_chnl_volt-dep_Kv1.1.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01508; KV11CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01496; SHAKERCHANEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Ion transport; Ionic channel; Lipoprotein; Membrane;
KW   Palmitate; Phosphoprotein; Potassium; Potassium channel;
KW   Potassium transport; RNA editing; Transmembrane; Transmembrane helix;
KW   Transport; Voltage-gated channel.
FT   CHAIN         1    495       Potassium voltage-gated channel subfamily
FT                                A member 1.
FT                                /FTId=PRO_0000053969.
FT   TRANSMEM    168    186       Helical; Name=Segment S1; (Potential).
FT   TRANSMEM    221    242       Helical; Name=Segment S2; (Potential).
FT   TRANSMEM    254    274       Helical; Name=Segment S3; (Potential).
FT   TRANSMEM    290    309       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TRANSMEM    326    345       Helical; Name=Segment S5; (Potential).
FT   TRANSMEM    387    408       Helical; Name=Segment S6; (Potential).
FT   MOTIF       372    377       Selectivity filter (By similarity).
FT   MOTIF       493    495       PDZ-binding (By similarity).
FT   MOD_RES     322    322       Phosphoserine; by PKA (Potential).
FT   MOD_RES     446    446       Phosphoserine; by PKA (Potential).
FT   LIPID       243    243       S-palmitoyl cysteine (By similarity).
FT   CARBOHYD    207    207       N-linked (GlcNAc...) (Potential).
FT   VARIANT     400    400       I -> V (in RNA edited version).
SQ   SEQUENCE   495 AA;  56409 MW;  C9249F130E943D3D CRC64;
     MTVMSGENAD EASTAPGHPQ DGSYPRQADH DDHECCERVV INISGLRFET QLKTLAQFPN
     TLLGNPKKRM RYFDPLRNEY FFDRNRPSFD AILYYYQSGG RLRRPVNVPL DMFSEEIKFY
     ELGEEAMEKF REDEGFIKEE ERPLPEKEYQ RQVWLLFEYP ESSGPARVIA IVSVMVILIS
     IVIFCLETLP ELKDDKDFTG TIHRIDNTTV IYTSNIFTDP FFIVETLCII WFSFELVVRF
     FACPSKTDFF KNIMNFIDIV AIIPYFITLG TEIAEQEGNQ KGEQATSLAI LRVIRLVRVF
     RIFKLSRHSK GLQILGQTLK ASMRELGLLI FFLFIGVILF SSAVYFAEAE EAESHFSSIP
     DAFWWAVVSM TTVGYGDMYP VTIGGKIVGS LCAIAGVLTI ALPVPVIVSN FNYFYHRETE
     GEEQAQLLHV SSPNLASDSD LSRRSSSTIS KSEYMEIEED MNNSIAHYRQ ANIRTGNCTT
     ADQNCVNKSK LLTDV
//
ID   KCNA3_MOUSE             Reviewed;         528 AA.
AC   P16390; A3KMM2;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 3.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Potassium voltage-gated channel subfamily A member 3;
DE   AltName: Full=MK3;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv1.3;
GN   Name=Kcna3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=90161996; PubMed=2305265; DOI=10.1126/science.2305265;
RA   Chandy K.G., Williams C.B., Spencer R.H., Aguilar B.A., Ghanshani S.,
RA   Tempel B.L., Gutman G.A.;
RT   "A family of three mouse potassium channel genes with intronless
RT   coding regions.";
RL   Science 247:973-975(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Mediates the voltage-dependent potassium ion
CC       permeability of excitable membranes. Assuming opened or closed
CC       conformations in response to the voltage difference across the
CC       membrane, the protein forms a potassium-selective channel through
CC       which potassium ions may pass in accordance with their
CC       electrochemical gradient.
CC   -!- SUBUNIT: Heterotetramer of potassium channel proteins. Binds PDZ
CC       domains of DLG4 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- DOMAIN: The N-terminus may be important in determining the rate of
CC       inactivation of the channel while the tail may play a role in
CC       modulation of channel activity and/or targeting of the channel to
CC       specific subcellular compartments.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position.
CC   -!- SIMILARITY: Belongs to the potassium channel family. A (Shaker)
CC       (TC 1.A.1.2) subfamily. Kv1.3/KCNA3 sub-subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; M30441; AAA39716.1; -; Genomic_DNA.
DR   EMBL; CH466607; EDL01888.1; -; Genomic_DNA.
DR   EMBL; BC132349; AAI32350.1; -; mRNA.
DR   EMBL; BC137667; AAI37668.1; -; mRNA.
DR   IPI; IPI00133732; -.
DR   PIR; C40090; I84205.
DR   PIR; S09044; S09044.
DR   RefSeq; NP_032444.2; NM_008418.2.
DR   UniGene; Mm.30640; -.
DR   ProteinModelPortal; P16390; -.
DR   SMR; P16390; 16-444.
DR   STRING; P16390; -.
DR   PhosphoSite; P16390; -.
DR   Ensembl; ENSMUST00000052718; ENSMUSP00000050680; ENSMUSG00000047959.
DR   GeneID; 16491; -.
DR   KEGG; mmu:16491; -.
DR   UCSC; uc008qwp.1; mouse.
DR   CTD; 16491; -.
DR   MGI; MGI:96660; Kcna3.
DR   eggNOG; maNOG06053; -.
DR   GeneTree; ENSGT00560000076957; -.
DR   HOGENOM; HBG445693; -.
DR   HOVERGEN; HBG052230; -.
DR   InParanoid; P16390; -.
DR   OMA; DRYEPLP; -.
DR   OrthoDB; EOG4QC155; -.
DR   PhylomeDB; P16390; -.
DR   ArrayExpress; P16390; -.
DR   Bgee; P16390; -.
DR   Genevestigator; P16390; -.
DR   GermOnline; ENSMUSG00000047959; Mus musculus.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003972; K_chnl_volt-dep_Kv1.
DR   InterPro; IPR004050; K_chnl_volt-dep_Kv1.3.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01510; KV13CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01496; SHAKERCHANEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Ion transport; Ionic channel; Lipoprotein; Membrane;
KW   Palmitate; Phosphoprotein; Potassium; Potassium channel;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN         1    528       Potassium voltage-gated channel subfamily
FT                                A member 3.
FT                                /FTId=PRO_0000053978.
FT   TRANSMEM    188    206       Helical; Name=Segment S1; (Potential).
FT   TRANSMEM    248    269       Helical; Name=Segment S2; (Potential).
FT   TRANSMEM    281    301       Helical; Name=Segment S3; (Potential).
FT   TRANSMEM    316    334       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TRANSMEM    351    370       Helical; Name=Segment S5; (Potential).
FT   TRANSMEM    412    434       Helical; Name=Segment S6; (Potential).
FT   MOTIF       397    402       Selectivity filter (By similarity).
FT   MOTIF       526    528       PDZ-binding (By similarity).
FT   MOD_RES     473    473       Phosphoserine; by PKA (Potential).
FT   LIPID       270    270       S-palmitoyl cysteine (Potential).
FT   CARBOHYD     62     62       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    231    231       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    232    232       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    369    369       V -> A (in Ref. 1; AAA39716).
FT   CONFLICT    492    492       H -> Q (in Ref. 1; AAA39716).
SQ   SEQUENCE   528 AA;  58564 MW;  12AC94FB13A523E7 CRC64;
     MTVVPGDHLL EPEAAGGGGG DPPQGGCGSG GGGGGCDRYE PLPPALPAAG EQDCCGERVV
     INISGLRFET QLKTLCQFPE TLLGDPKRRM RYFDPLRNEY FFDRNRPSFD AILYYYQSGG
     RIRRPVNVPI DIFSEEIRFY QLGEEAMEKF REDEGFLREE ERPLPRRDFQ RQVWLLFEYP
     ESSGPARGIA IVSVLVILIS IVIFCLETLP EFRDEKDYPA SPSQDVFEAA NNSTSGAPSG
     ASSFSDPFFV VETLCIIWFS FELLVRFFAC PSKATFSRNI MNLIDIVAII PYFITLGTEL
     AERQGNGQQA MSLAILRVIR LVRVFRIFKL SRHSKGLQIL GQTLKASMRE LGLLIFFLFI
     GVILFSSAVY FAEADDPSSG FNSIPDAFWW AVVTMTTVGY GDMHPVTIGG KIVGSLCAIA
     GVLTIALPVP VIVSNFNYFY HRETEGEEQA QYMHVGSCQH LSSSAEELRK ARSNSTLSKS
     EYMVIEEGGM NHSAFPQTPF KTGNSTATCT TNNNPNSCVN IKKIFTDV
//
ID   G3P_MOUSE               Reviewed;         333 AA.
AC   P16858; A6H6A8; Q0QEU0; Q3THM2; Q3TUI2; Q3UMT2; Q4V783; Q569X2;
AC   Q569X5; Q5U410;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 116.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase;
DE            Short=GAPDH;
DE            EC=1.2.1.12;
DE   AltName: Full=Peptidyl-cysteine S-nitrosylase GAPDH;
DE            EC=2.6.99.-;
GN   Name=Gapdh; Synonyms=Gapd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=91007274; PubMed=2145197; DOI=10.1016/0378-1119(90)90087-8;
RA   Sabath D.E., Broome H.E., Prystowsky M.B.;
RT   "Glyceraldehyde-3-phosphate dehydrogenase mRNA is a major interleukin
RT   2-induced transcript in a cloned T-helper lymphocyte.";
RL   Gene 91:185-191(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, C57BL/6J, and DBA/2;
RC   TISSUE=Cerebellum, Eye, Head, Kidney, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129, C57BL/6, C57BL/6J, Czech II, FVB/N, and FVB/N-3;
RC   TISSUE=Brain, Colon, Embryo, Eye, Mammary gland, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 4-11; 27-50; 65-78; 85-105; 116-137; 144-189;
RP   199-213; 218-246 AND 262-333, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B.,
RA   Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 24-249.
RX   PubMed=16751257; DOI=10.1093/molbev/msl027;
RA   Kullberg M., Nilsson M.A., Arnason U., Harley E.H., Janke A.;
RT   "Housekeeping genes for phylogenetic analysis of eutherian
RT   relationships.";
RL   Mol. Biol. Evol. 23:1493-1503(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-316 AND TYR-318, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-312; TYR-316; TYR-318
RP   AND TYR-328, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-209, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and
CC       nitrosylase activities, thereby playing a role in glycolysis and
CC       nuclear functions, respectively. Glyceraldehyde-3-phosphate
CC       dehydrogenase is a key enzyme in glycolysis that catalyzes the
CC       first step of the pathway by converting D-glyceraldehyde 3-
CC       phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Also
CC       participates in nuclear events including transcription, RNA
CC       transport, DNA replication and apoptosis. Nuclear functions are
CC       probably due to the nitrosylase activity that mediates cysteine S-
CC       nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and
CC       PRKDC (By similarity).
CC   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
CC       NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5.
CC   -!- SUBUNIT: Homotetramer. Interacts with EIF1AD, USP25, PRKCI and
CC       WARS. Interacts with TPPP; the interaction is direct. Interacts
CC       (when S-nitrosylated) with SIAH1; leading to nuclear
CC       translocation. Interacts with RILPL1/GOSPEL, leading to prevent
CC       the interaction between GAPDH and SIAH1 and prevent nuclear
CC       translocation (By similarity).
CC   -!- INTERACTION:
CC       Q08460:Kcnma1; NbExp=1; IntAct=EBI-444871, EBI-1633915;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity). Nucleus
CC       (By similarity). Note=Translocates to the nucleus following S-
CC       nitrosylation and interaction with SIAH1, which contains a nuclear
CC       localization signal (By similarity).
CC   -!- PTM: ISGylated (By similarity).
CC   -!- PTM: S-nitrosylation of Cys-150 leads to interaction with SIAH1,
CC       followed by translocation to the nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
CC       dehydrogenase family.
CC   -----------------------------------------------------------------------
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DR   EMBL; M32599; AAA37659.1; -; mRNA.
DR   EMBL; AK002273; BAB21979.1; -; mRNA.
DR   EMBL; AK081405; BAC38211.1; -; mRNA.
DR   EMBL; AK140794; BAE24481.1; -; mRNA.
DR   EMBL; AK144690; BAE26016.1; -; mRNA.
DR   EMBL; AK146435; BAE27169.1; -; mRNA.
DR   EMBL; AK147738; BAE28105.1; -; mRNA.
DR   EMBL; AK147891; BAE28208.1; -; mRNA.
DR   EMBL; AK160399; BAE35768.1; -; mRNA.
DR   EMBL; AK160753; BAE35989.1; -; mRNA.
DR   EMBL; AK164415; BAE37778.1; -; mRNA.
DR   EMBL; AK168217; BAE40174.1; -; mRNA.
DR   EMBL; AL662926; CAI25599.1; -; Genomic_DNA.
DR   EMBL; BC082592; AAH82592.1; -; mRNA.
DR   EMBL; BC083065; AAH83065.1; -; mRNA.
DR   EMBL; BC083079; AAH83079.1; -; mRNA.
DR   EMBL; BC083080; AAH83080.1; -; mRNA.
DR   EMBL; BC083149; AAH83149.1; -; mRNA.
DR   EMBL; BC085274; AAH85274.1; -; mRNA.
DR   EMBL; BC085275; AAH85275.1; -; mRNA.
DR   EMBL; BC085315; AAH85315.1; -; mRNA.
DR   EMBL; BC091768; AAH91768.1; -; mRNA.
DR   EMBL; BC092252; AAH92252.1; -; mRNA.
DR   EMBL; BC092264; AAH92264.1; -; mRNA.
DR   EMBL; BC092267; AAH92267.1; -; mRNA.
DR   EMBL; BC092294; AAH92294.1; -; mRNA.
DR   EMBL; BC093508; AAH93508.1; -; mRNA.
DR   EMBL; BC094037; AAH94037.1; -; mRNA.
DR   EMBL; BC095932; AAH95932.1; -; mRNA.
DR   EMBL; BC096440; AAH96440.1; -; mRNA.
DR   EMBL; BC096590; AAH96590.1; -; mRNA.
DR   EMBL; BC110311; AAI10312.1; -; mRNA.
DR   EMBL; BC145810; AAI45811.1; -; mRNA.
DR   EMBL; BC145812; AAI45813.1; -; mRNA.
DR   EMBL; DQ403054; ABD77187.1; -; mRNA.
DR   IPI; IPI00273646; -.
DR   PIR; JT0553; DEMSG.
DR   RefSeq; NP_032110.1; NM_008084.2.
DR   RefSeq; XP_001476757.1; XM_001476707.2.
DR   UniGene; Mm.304088; -.
DR   UniGene; Mm.309092; -.
DR   UniGene; Mm.317779; -.
DR   UniGene; Mm.343110; -.
DR   UniGene; Mm.392463; -.
DR   UniGene; Mm.392480; -.
DR   UniGene; Mm.414470; -.
DR   UniGene; Mm.426339; -.
DR   UniGene; Mm.458138; -.
DR   UniGene; Mm.458416; -.
DR   UniGene; Mm.458822; -.
DR   UniGene; Mm.465013; -.
DR   UniGene; Mm.475698; -.
DR   ProteinModelPortal; P16858; -.
DR   SMR; P16858; 2-333.
DR   IntAct; P16858; 11.
DR   MINT; MINT-1869564; -.
DR   STRING; P16858; -.
DR   PhosphoSite; P16858; -.
DR   SWISS-2DPAGE; P16858; -.
DR   REPRODUCTION-2DPAGE; P16858; -.
DR   REPRODUCTION-2DPAGE; Q5U410; -.
DR   PRIDE; P16858; -.
DR   Ensembl; ENSMUST00000073605; ENSMUSP00000073289; ENSMUSG00000057666.
DR   Ensembl; ENSMUST00000097205; ENSMUSP00000100482; ENSMUSG00000078088.
DR   Ensembl; ENSMUST00000098560; ENSMUSP00000100572; ENSMUSG00000078162.
DR   Ensembl; ENSMUST00000104945; ENSMUSP00000100550; ENSMUSG00000078142.
DR   Ensembl; ENSMUST00000109588; ENSMUSP00000105217; ENSMUSG00000078965.
DR   Ensembl; ENSMUST00000109590; ENSMUSP00000105219; ENSMUSG00000078965.
DR   Ensembl; ENSMUST00000109595; ENSMUSP00000105224; ENSMUSG00000078967.
DR   Ensembl; ENSMUST00000113842; ENSMUSP00000109473; ENSMUSG00000079501.
DR   Ensembl; ENSMUST00000117757; ENSMUSP00000113942; ENSMUSG00000057666.
DR   Ensembl; ENSMUST00000118875; ENSMUSP00000113213; ENSMUSG00000057666.
DR   GeneID; 100042025; -.
DR   GeneID; 14433; -.
DR   KEGG; mmu:100042025; -.
DR   KEGG; mmu:14433; -.
DR   UCSC; uc009dts.1; mouse.
DR   CTD; 14433; -.
DR   MGI; MGI:95640; Gapdh.
DR   eggNOG; roNOG06117; -.
DR   HOVERGEN; HBG000227; -.
DR   InParanoid; P16858; -.
DR   OrthoDB; EOG4Q84XS; -.
DR   PhylomeDB; P16858; -.
DR   BRENDA; 1.2.1.12; 244.
DR   NextBio; 447908; -.
DR   Bgee; P16858; -.
DR   CleanEx; MM_GAPDH; -.
DR   Genevestigator; P16858; -.
DR   GermOnline; ENSMUSG00000057666; Mus musculus.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) activity; ISS:UniProtKB.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0035605; F:peptidyl-cysteine S-nitrosylase activity; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0051402; P:neuron apoptosis; ISS:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0035606; P:peptidyl-cysteine S-trans-nitrosylation; ISS:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR   InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR   InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR10836; GAP_DH; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PIRSF; PIRSF000149; GAP_DH; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
DR   SMART; SM00846; Gp_dh_N; 1.
DR   TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ADP-ribosylation; Apoptosis; Cytoplasm;
KW   Direct protein sequencing; Glycolysis; Methylation; NAD; Nucleus;
KW   Oxidoreductase; Phosphoprotein; S-nitrosylation; Transferase;
KW   Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    333       Glyceraldehyde-3-phosphate dehydrogenase.
FT                                /FTId=PRO_0000145490.
FT   NP_BIND      11     12       NAD (By similarity).
FT   REGION        2    146       Interaction with WARS (By similarity).
FT   REGION      149    151       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   REGION      209    210       Glyceraldehyde 3-phosphate binding (By
FT                                similarity).
FT   ACT_SITE    150    150       Nucleophile (By similarity).
FT   BINDING      33     33       NAD (By similarity).
FT   BINDING      78     78       NAD; via carbonyl oxygen (By similarity).
FT   BINDING     120    120       NAD (By similarity).
FT   BINDING     180    180       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     232    232       Glyceraldehyde 3-phosphate (By
FT                                similarity).
FT   BINDING     314    314       NAD (By similarity).
FT   SITE        177    177       Activates thiol group during catalysis
FT                                (By similarity).
FT   MOD_RES       3      3       N6,N6-dimethyllysine (By similarity).
FT   MOD_RES       7      7       Deamidated asparagine (By similarity).
FT   MOD_RES      59     59       N6-acetyllysine (By similarity).
FT   MOD_RES      62     62       Deamidated asparagine (By similarity).
FT   MOD_RES      64     64       N6,N6-dimethyllysine (By similarity).
FT   MOD_RES      68     68       Deamidated asparagine (By similarity).
FT   MOD_RES      73     73       Phosphothreonine (By similarity).
FT   MOD_RES     120    120       Phosphoserine (By similarity).
FT   MOD_RES     146    146       Phosphoserine (By similarity).
FT   MOD_RES     147    147       Deamidated asparagine (By similarity).
FT   MOD_RES     149    149       Phosphoserine (By similarity).
FT   MOD_RES     150    150       ADP-ribosylcysteine; by autocatalysis; in
FT                                irreversibly inhibited form (By
FT                                similarity).
FT   MOD_RES     150    150       S-nitrosocysteine; in reversibly
FT                                inhibited form (By similarity).
FT   MOD_RES     152    152       Phosphothreonine (By similarity).
FT   MOD_RES     153    153       Deamidated asparagine (By similarity).
FT   MOD_RES     182    182       Phosphothreonine (By similarity).
FT   MOD_RES     184    184       N6-acetyllysine (By similarity).
FT   MOD_RES     192    192       N6,N6-dimethyllysine (By similarity).
FT   MOD_RES     192    192       N6-acetyllysine (By similarity).
FT   MOD_RES     208    208       Phosphoserine (By similarity).
FT   MOD_RES     209    209       Phosphothreonine.
FT   MOD_RES     213    213       N6,N6-dimethyllysine (By similarity).
FT   MOD_RES     217    217       N6-acetyllysine (By similarity).
FT   MOD_RES     223    223       Deamidated asparagine (By similarity).
FT   MOD_RES     225    225       N6,N6-dimethyllysine (By similarity).
FT   MOD_RES     225    225       N6-acetyllysine (By similarity).
FT   MOD_RES     227    227       Phosphothreonine (By similarity).
FT   MOD_RES     235    235       Phosphothreonine (By similarity).
FT   MOD_RES     252    252       N6-acetyllysine (By similarity).
FT   MOD_RES     258    258       N6,N6-dimethyllysine (By similarity).
FT   MOD_RES     261    261       N6,N6-dimethyllysine (By similarity).
FT   MOD_RES     310    310       Phosphoserine (By similarity).
FT   MOD_RES     312    312       Phosphotyrosine.
FT   MOD_RES     314    314       Deamidated asparagine (By similarity).
FT   MOD_RES     316    316       Phosphotyrosine.
FT   MOD_RES     318    318       Phosphotyrosine.
FT   MOD_RES     328    328       Phosphotyrosine.
FT   MOD_RES     332    332       N6,N6-dimethyllysine (By similarity).
FT   CONFLICT      3      3       K -> E (in Ref. 2; BAE40174).
FT   CONFLICT     30     30       A -> V (in Ref. 4; AAH92267).
FT   CONFLICT     82     82       N -> S (in Ref. 2; BAE35989).
FT   CONFLICT     84     84       K -> E (in Ref. 2; BAE40174).
FT   CONFLICT     89     89       G -> S (in Ref. 2; BAE26016).
FT   CONFLICT     91     91       E -> K (in Ref. 2; BAE35989).
FT   CONFLICT    134    134       N -> D (in Ref. 4; AAH85315).
FT   CONFLICT    195    195       R -> C (in Ref. 4; AAH85315).
FT   CONFLICT    300    300       A -> S (in Ref. 4; AAH85315).
SQ   SEQUENCE   333 AA;  35810 MW;  F25131EFFA9F2BD6 CRC64;
     MVKVGVNGFG RIGRLVTRAA ICSGKVEIVA INDPFIDLNY MVYMFQYDST HGKFNGTVKA
     ENGKLVINGK PITIFQERDP TNIKWGEAGA EYVVESTGVF TTMEKAGAHL KGGAKRVIIS
     APSADAPMFV MGVNHEKYDN SLKIVSNASC TTNCLAPLAK VIHDNFGIVE GLMTTVHAIT
     ATQKTVDGPS GKLWRDGRGA AQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV
     VDLTCRLEKP AKYDDIKKVV KQASEGPLKG ILGYTEDQVV SCDFNSNSHS STFDAGAGIA
     LNDNFVKLIS WYDNEYGYSN RVVDLMAYMA SKE
//
ID   ZFX_MOUSE               Reviewed;         799 AA.
AC   P17012; P17011;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   08-MAR-2011, entry version 101.
DE   RecName: Full=Zinc finger X-chromosomal protein;
GN   Name=Zfx;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90136582; PubMed=2105457;
RA   Mardon G., Luoh S.-W., Simpson E.M., Gill G., Brown L.G., Page D.C.;
RT   "Mouse Zfx protein is similar to Zfy-2: each contains an acidic
RT   activating domain and 13 zinc fingers.";
RL   Mol. Cell. Biol. 10:681-688(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-216.
RC   STRAIN=FVB/N; TISSUE=Testis;
RX   MEDLINE=94245202; PubMed=8188262; DOI=10.1006/geno.1994.1063;
RA   Luoh S.-W., Page D.C.;
RT   "The structure of the Zfx gene on the mouse X chromosome.";
RL   Genomics 19:310-319(1994).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Probable transcriptional activator.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. ZFX/ZFY subfamily.
CC   -!- SIMILARITY: Contains 13 C2H2-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA40585.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown due to a duplication of 120 bp after position 480;
CC   -----------------------------------------------------------------------
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DR   EMBL; M32308; AAA40584.1; -; mRNA.
DR   EMBL; M32309; AAA40585.1; ALT_SEQ; mRNA.
DR   EMBL; L19714; AAA75393.1; -; mRNA.
DR   IPI; IPI00134493; -.
DR   PIR; A34729; A34729.
DR   RefSeq; NP_001037851.1; NM_001044386.1.
DR   RefSeq; NP_035898.2; NM_011768.2.
DR   UniGene; Mm.919; -.
DR   ProteinModelPortal; P17012; -.
DR   SMR; P17012; 417-797.
DR   STRING; P17012; -.
DR   PhosphoSite; P17012; -.
DR   PRIDE; P17012; -.
DR   Ensembl; ENSMUST00000088102; ENSMUSP00000085423; ENSMUSG00000079509.
DR   Ensembl; ENSMUST00000113926; ENSMUSP00000109559; ENSMUSG00000079509.
DR   Ensembl; ENSMUST00000113927; ENSMUSP00000109560; ENSMUSG00000079509.
DR   GeneID; 22764; -.
DR   KEGG; mmu:22764; -.
DR   UCSC; uc009tsz.1; mouse.
DR   CTD; 22764; -.
DR   MGI; MGI:99211; Zfx.
DR   eggNOG; roNOG13720; -.
DR   HOGENOM; HBG444122; -.
DR   HOVERGEN; HBG000337; -.
DR   InParanoid; P17012; -.
DR   OMA; GNCEDYL; -.
DR   OrthoDB; EOG4ZW59C; -.
DR   NextBio; 303289; -.
DR   ArrayExpress; P17012; -.
DR   Bgee; P17012; -.
DR   CleanEx; MM_ZFX; -.
DR   Genevestigator; P17012; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030528; F:transcription regulator activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR006794; Transcrp_activ_Zfx/Zfy-dom.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 9.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   Pfam; PF04704; Zfx_Zfy_act; 1.
DR   SMART; SM00355; ZnF_C2H2; 13.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 13.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    799       Zinc finger X-chromosomal protein.
FT                                /FTId=PRO_0000047259.
FT   ZN_FING     419    444       C2H2-type 1.
FT   ZN_FING     450    472       C2H2-type 2.
FT   ZN_FING     482    504       C2H2-type 3.
FT   ZN_FING     513    536       C2H2-type 4.
FT   ZN_FING     542    564       C2H2-type 5.
FT   ZN_FING     570    593       C2H2-type 6.
FT   ZN_FING     599    621       C2H2-type 7.
FT   ZN_FING     627    650       C2H2-type 8.
FT   ZN_FING     656    678       C2H2-type 9.
FT   ZN_FING     684    707       C2H2-type 10.
FT   ZN_FING     713    735       C2H2-type 11.
FT   ZN_FING     741    764       C2H2-type 12.
FT   ZN_FING     770    792       C2H2-type 13.
FT   MOD_RES     269    269       Phosphoserine.
SQ   SEQUENCE   799 AA;  90026 MW;  3FB6B4D2159EADFD CRC64;
     MDEDGLELQQ QAPNSFFDAT GAGATHMDGN QIVVEVQETV YVSDVVDSDI TVHNYVPDDP
     DSVVIQDVIE DVVIEDVQCT DIMDEADVSE TVIIPEQVLD SDVTEEVSLT HCTVPDDVLA
     SDITSASISM PEHVLTSESI HVSDVGHVEH VVHDSVVEAE IVTDPLAADV VSEEVLVADC
     ASEAVIDANG IPVNQQDEEK NNCEDYLMIS LDDAGKIEHD GSSGLTMDNE TEIDPCKVDG
     TCPEVIKVYI FKADPGEDDL GGTVDIVESE PENEHGVELL DPNNSIRVPR EKMVYMAVND
     SQQEEEELNV AEIADEVYME VIVGEEDAAA AAAAAVHEQQ VEDNEMKTFM PIAWAAAYGN
     NSDGIENRNG TASALLHIDE SAGLGRLAKQ KPKKRRRPDS RQYQTAIIIG PDGHPLTVYP
     CMICGKKFKS RGFLKRHMKN HPEHLAKKKY RCTDCDYTTN KKISLHNHLE SHKLTSKAEK
     AIECDECGKH FSHAGALFTH KMVHKEKGAN KMHKCKFCEY ETAEQGLLNR HLLAVHSKNF
     PHICVECGKG FRHPSELKKH MRIHTGEKPY ECQYCEYRSA DSSNLKTHVK TKHSKEMPFK
     CDICLLTFSD TKEVQQHALV HQESKTHQCL HCDHKSSNSS DLKRHIISVH TKDYPHKCDM
     CDKGFHRPSE LKKHVAAHKG KKMHQCRHCD FKIADPFVLS RHILSVHTKD LPFRCKRCRK
     GFRQQSELKK HMKTHSGRKV YQCEYCEYST TDASGFKRHV ISIHTKDYPH RCEYCKKGFR
     RPSEKNQHIM RHHKEVGLP
//
ID   HSP72_MOUSE             Reviewed;         633 AA.
AC   P17156;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Heat shock-related 70 kDa protein 2;
DE            Short=Heat shock protein 70.2;
GN   Name=Hspa2; Synonyms=Hcp70.2, Hsp70-2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=88302212; PubMed=3405224;
RA   Zakeri Z.F., Wolgemuth D.J., Hunt C.R.;
RT   "Identification and sequence analysis of a new member of the mouse
RT   HSP70 gene family and characterization of its unique cellular and
RT   developmental pattern of expression in the male germ line.";
RL   Mol. Cell. Biol. 8:2925-2932(1988).
RN   [2]
RP   INTERACTION WITH ZNF541.
RX   PubMed=18849567; DOI=10.1074/jbc.M805590200;
RA   Choi E., Han C., Park I., Lee B., Jin S., Choi H., Kim do H.,
RA   Park Z.Y., Eddy E.M., Cho C.;
RT   "A novel germ cell-specific protein, SHIP1, forms a complex with
RT   chromatin remodeling activity during spermatogenesis.";
RL   J. Biol. Chem. 283:35283-35294(2008).
CC   -!- FUNCTION: In cooperation with other chaperones, Hsp70s stabilize
CC       preexistent proteins against aggregation and mediate the folding
CC       of newly translated polypeptides in the cytosol as well as within
CC       organelles. These chaperones participate in all these processes
CC       through their ability to recognize nonnative conformations of
CC       other proteins. They bind extended peptide segments with a net
CC       hydrophobic character exposed by polypeptides during translation
CC       and membrane translocation, or following stress-induced damage.
CC   -!- SUBUNIT: Interacts with ZNF541.
CC   -!- DEVELOPMENTAL STAGE: Specifically expressed in prophage stage of
CC       meiosis.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
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DR   EMBL; M20567; AAA37859.1; -; Genomic_DNA.
DR   IPI; IPI00331546; -.
DR   PIR; S10859; S10859.
DR   UniGene; Mm.296181; -.
DR   ProteinModelPortal; P17156; -.
DR   SMR; P17156; 3-616.
DR   DIP; DIP-42071N; -.
DR   MINT; MINT-1207820; -.
DR   STRING; P17156; -.
DR   PhosphoSite; P17156; -.
DR   REPRODUCTION-2DPAGE; IPI00331546; -.
DR   REPRODUCTION-2DPAGE; P17156; -.
DR   UCD-2DPAGE; P17156; -.
DR   PRIDE; P17156; -.
DR   Ensembl; ENSMUST00000080449; ENSMUSP00000079306; ENSMUSG00000059970.
DR   Ensembl; ENSMUST00000110404; ENSMUSP00000106034; ENSMUSG00000059970.
DR   MGI; MGI:96243; Hspa2.
DR   eggNOG; roNOG06558; -.
DR   HOGENOM; HBG334976; -.
DR   HOVERGEN; HBG051845; -.
DR   InParanoid; P17156; -.
DR   OrthoDB; EOG4W6NVK; -.
DR   PhylomeDB; P17156; -.
DR   ArrayExpress; P17156; -.
DR   Bgee; P17156; -.
DR   CleanEx; MM_HSPA2; -.
DR   Genevestigator; P17156; -.
DR   GermOnline; ENSMUSG00000059970; Mus musculus.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0000795; C:synaptonemal complex; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0051861; F:glycolipid binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0007141; P:male meiosis I; IMP:MGI.
DR   GO; GO:0031662; P:positive regulation of cyclin-dependent protein kinase activity involved in G2/M; IMP:MGI.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:MGI.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   GO; GO:0007286; P:spermatid development; IMP:MGI.
DR   GO; GO:0070194; P:synaptonemal complex disassembly; IMP:MGI.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR001023; Hsp70.
DR   InterPro; IPR013126; Hsp_70.
DR   PANTHER; PTHR19375; Hsp70; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Nucleotide-binding; Phosphoprotein;
KW   Stress response.
FT   CHAIN         1    633       Heat shock-related 70 kDa protein 2.
FT                                /FTId=PRO_0000078259.
FT   MOD_RES      42     42       Phosphotyrosine (By similarity).
FT   MOD_RES     108    108       Phosphotyrosine (By similarity).
SQ   SEQUENCE   633 AA;  69741 MW;  E7F9040F2AB138DD CRC64;
     MSARGPAIGI DLGTTYSCVG VFQHGKVEII ANDQGNRTTP SYVAFTDTER LIGDAAKNQV
     AMNPTNTIFD RKRLIGRKFE DATVQSDMKH WPFRVVSEGG KPKVQVEYKG EMKTFFPEEI
     SSMVLTKMKE IAEAYLGGKV QSAVITVPAY FNDSQRQATK DAGTITGLNV LRIINEPTAA
     AIAYGLDKKG CAGGEKNVLI FDLGGGTFDV SILTIEDGIF ELKSTAGDTH LGGEDFDNRM
     VSHLAEEFKR KHKKDIGPNK RAVRRLRTAC ERAKRTLSSS TQASIEIDSL YEGVDFYTSI
     TRARFEELNA DLFRGTLEPV EKALRDAKLD KGQIQEIVLV GGSTRIPKIQ KLLQDFFNGK
     ELNKSINPDE AVAYGAAVQA AILIGDKSEN VQDLLLLDVT PLSLGIETAG GVMTPLIKRN
     TTIPTKQTQT FTTYSDNQSS VLVQVYEGER AMTKDNNLLG KFDLTGIPPA PRGVPQIEVT
     FDIDANGILN VTAADKSTGK ENKITITNDK GRLSKDDIDR MVQEAERYKS EDEANRDRVA
     AKNAVESYTY NIKQTVEDEK LRGKISEQDK NKILDKCQEV INWLDRNQMA EKDEYEHKQK
     ELERVCNPII SKLYQGGPGG GGSSGGPTIE EVD
//
ID   ENOA_MOUSE              Reviewed;         434 AA.
AC   P17182; Q99KT7; Q9DCY7;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 127.
DE   RecName: Full=Alpha-enolase;
DE            EC=4.2.1.11;
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE   AltName: Full=Enolase 1;
DE   AltName: Full=Non-neural enolase;
DE            Short=NNE;
GN   Name=Eno1; Synonyms=Eno-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=90301487; PubMed=2362815; DOI=10.1093/nar/18.12.3638;
RA   Kaghad M., Dumont X., Chalon P., Lelias J.M., Lamande N., Lucas M.,
RA   Lazar M., Caput D.;
RT   "Nucleotide sequences of cDNAs alpha and gamma enolase mRNAs from
RT   mouse brain.";
RL   Nucleic Acids Res. 18:3638-3638(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 10-28; 33-50; 61-120; 133-179; 184-193; 203-228;
RP   234-253; 257-262; 270-281; 307-326; 344-358; 373-394 AND 413-420, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B.,
RA   Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   PROTEIN SEQUENCE OF 60-71; 100-114; 184-198 AND 246-259.
RC   TISSUE=Macrophage;
RX   PubMed=8427861;
RA   Bottalico L.A., Kendrick N.C., Keller A., Li Y., Tabas I.;
RT   "Cholesteryl ester loading of mouse peritoneal macrophages is
RT   associated with changes in the expression or modification of specific
RT   cellular proteins, including increase in an alpha-enolase isoform.";
RL   Arterioscler. Thromb. 13:264-275(1993).
RN   [6]
RP   INTERACTION WITH PKM2; PGM; CKM; ALDO AND TROPONIN, AND DEVELOPMENTAL
RP   STAGE.
RX   MEDLINE=97270626; PubMed=9169614;
RA   Merkulova T., Lucas M., Jabet C., Lamande N., Rouzeau J.-D., Gros F.,
RA   Lazar M., Keller A.;
RT   "Biochemical characterization of the mouse muscle-specific enolase:
RT   developmental changes in electrophoretic variants and selective
RT   binding to other proteins.";
RL   Biochem. J. 323:791-800(1997).
RN   [7]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   MEDLINE=21121273; PubMed=11229603; DOI=10.1016/S0248-4900(00)01103-5;
RA   Keller A., Demeurie J., Merkulova T., Geraud G., Cywiner-Golenzer C.,
RA   Lucas M., Chatelet F.-P.;
RT   "Fibre-type distribution and subcellular localisation of alpha and
RT   beta enolase in mouse striated muscle.";
RL   Biol. Cell 92:527-535(2000).
RN   [8]
RP   ISGYLATION.
RX   PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA   Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA   Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT   "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT   human cells.";
RL   Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Multifunctional enzyme that, as well as its role in
CC       glycolysis, plays a part in various processes such as growth
CC       control, hypoxia tolerance and allergic responses (By similarity).
CC       May also function in the intravascular and pericellular
CC       fibrinolytic system due to its ability to serve as a receptor and
CC       activator of plasminogen on the cell surface of several cell-types
CC       such as leukocytes and neurons. Stimulates immunoglobulin
CC       production (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate +
CC       H(2)O.
CC   -!- COFACTOR: Magnesium. Required for catalysis and for stabilizing
CC       the dimer.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5.
CC   -!- SUBUNIT: Mammalian enolase is composed of 3 isozyme subunits,
CC       alpha, beta and gamma, which can form homodimers or heterodimers
CC       which are cell-type and development-specific. ENO1 interacts with
CC       PLG in the neuronal plasma membrane and promotes its activation.
CC       The C-terminal lysine is required for this binding (By
CC       similarity). In vitro, interacts with several glycolytic enzymes
CC       including PKM2, PGM, CKM and aldolase. Also binds troponin, in
CC       vitro.
CC   -!- INTERACTION:
CC       P22303:ACHE (xeno); NbExp=1; IntAct=EBI-299507, EBI-1637793;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By
CC       similarity). Note=Can translocate to the plasma membrane in either
CC       the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form
CC       (By similarity). ENO1 is localized to the M-band.
CC   -!- TISSUE SPECIFICITY: The alpha/alpha homodimer is expressed in
CC       embryo and in most adult tissues. The alpha/beta heterodimer and
CC       the beta/beta homodimer are found in striated muscle, and the
CC       alpha/gamma heterodimer and the gamma/gamma homodimer in neurons.
CC       In striated muscle, expression of ENO1 appears to be independent
CC       of fiber type.
CC   -!- DEVELOPMENTAL STAGE: During ontogenesis, there is a transition
CC       from the alpha/alpha homodimer to the alpha/beta heterodimer in
CC       striated muscle cells, and to the alpha/gamma heterodimer in nerve
CC       cells. In embryonic muscle, ENO1 is highly expressed until E17.
CC       Decreased levels from P5.
CC   -!- PTM: ISGylated.
CC   -!- SIMILARITY: Belongs to the enolase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X52379; CAA36605.1; -; mRNA.
DR   EMBL; AK002336; BAB22021.1; -; mRNA.
DR   EMBL; BC003891; AAH03891.1; -; mRNA.
DR   EMBL; BC004017; AAH04017.1; -; mRNA.
DR   EMBL; BC010685; AAH10685.1; -; mRNA.
DR   EMBL; BC024644; AAH24644.1; -; mRNA.
DR   EMBL; BC085098; AAH85098.1; -; mRNA.
DR   IPI; IPI00462072; -.
DR   PIR; S10246; S10246.
DR   RefSeq; NP_001020559.1; NM_001025388.1.
DR   RefSeq; NP_075608.2; NM_023119.2.
DR   RefSeq; XP_003086454.1; XM_003086406.1.
DR   RefSeq; XP_003086455.1; XM_003086407.1.
DR   RefSeq; XP_003086457.1; XM_003086409.1.
DR   RefSeq; XP_003086458.1; XM_003086410.1.
DR   RefSeq; XP_003086459.1; XM_003086411.1.
DR   RefSeq; XP_003086596.1; XM_003086548.1.
DR   UniGene; Mm.372357; -.
DR   UniGene; Mm.372389; -.
DR   UniGene; Mm.70666; -.
DR   ProteinModelPortal; P17182; -.
DR   SMR; P17182; 2-434.
DR   IntAct; P17182; 7.
DR   STRING; P17182; -.
DR   PhosphoSite; P17182; -.
DR   SWISS-2DPAGE; P17182; -.
DR   REPRODUCTION-2DPAGE; IPI00462072; -.
DR   REPRODUCTION-2DPAGE; P17182; -.
DR   UCD-2DPAGE; P17182; -.
DR   PRIDE; P17182; -.
DR   Ensembl; ENSMUST00000076155; ENSMUSP00000075513; ENSMUSG00000059040.
DR   Ensembl; ENSMUST00000080926; ENSMUSP00000079727; ENSMUSG00000063524.
DR   GeneID; 100045967; -.
DR   GeneID; 100503183; -.
DR   GeneID; 13806; -.
DR   GeneID; 433182; -.
DR   KEGG; mmu:100045967; -.
DR   KEGG; mmu:100503183; -.
DR   KEGG; mmu:13806; -.
DR   KEGG; mmu:433182; -.
DR   UCSC; uc008ewh.1; mouse.
DR   CTD; 13806; -.
DR   MGI; MGI:95393; Eno1.
DR   eggNOG; roNOG10078; -.
DR   HOGENOM; HBG726599; -.
DR   HOVERGEN; HBG000067; -.
DR   InParanoid; P17182; -.
DR   OMA; IHARQIY; -.
DR   OrthoDB; EOG4T783B; -.
DR   PhylomeDB; P17182; -.
DR   BRENDA; 4.2.1.11; 244.
DR   NextBio; 457726; -.
DR   Bgee; P17182; -.
DR   Genevestigator; P17182; -.
DR   GermOnline; ENSMUSG00000059040; Mus musculus.
DR   GermOnline; ENSMUSG00000063524; Mus musculus.
DR   GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR000941; Enolase.
DR   InterPro; IPR020810; Enolase_C.
DR   InterPro; IPR020809; Enolase_CS.
DR   InterPro; IPR020811; Enolase_N.
DR   Pfam; PF00113; Enolase_C; 1.
DR   Pfam; PF03952; Enolase_N; 1.
DR   PIRSF; PIRSF001400; Enolase; 1.
DR   PRINTS; PR00148; ENOLASE.
DR   TIGRFAMs; TIGR01060; eno; 1.
DR   PROSITE; PS00164; ENOLASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Cytoplasm; Direct protein sequencing;
KW   Glycolysis; Lyase; Magnesium; Membrane; Metal-binding; Phosphoprotein;
KW   Ubl conjugation.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    434       Alpha-enolase.
FT                                /FTId=PRO_0000134098.
FT   REGION      370    373       Substrate binding (By similarity).
FT   REGION      405    434       Required for interaction with PLG (By
FT                                similarity).
FT   ACT_SITE    210    210       Proton donor (By similarity).
FT   ACT_SITE    343    343       Proton acceptor (By similarity).
FT   METAL       245    245       Magnesium (By similarity).
FT   METAL       293    293       Magnesium (By similarity).
FT   METAL       318    318       Magnesium (By similarity).
FT   BINDING     158    158       Substrate (By similarity).
FT   BINDING     167    167       Substrate (By similarity).
FT   BINDING     293    293       Substrate (By similarity).
FT   BINDING     318    318       Substrate (By similarity).
FT   BINDING     394    394       Substrate (By similarity).
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES      44     44       Phosphotyrosine.
FT   MOD_RES      60     60       N6-acetyllysine (By similarity).
FT   MOD_RES      63     63       Phosphoserine (By similarity).
FT   MOD_RES      71     71       N6-acetyllysine (By similarity).
FT   MOD_RES      72     72       Phosphothreonine (By similarity).
FT   MOD_RES      89     89       N6-acetyllysine (By similarity).
FT   MOD_RES     126    126       N6-acetyllysine (By similarity).
FT   MOD_RES     193    193       N6-acetyllysine (By similarity).
FT   MOD_RES     199    199       N6-acetyllysine (By similarity).
FT   MOD_RES     228    228       N6-acetyllysine (By similarity).
FT   MOD_RES     233    233       N6-acetyllysine (By similarity).
FT   MOD_RES     254    254       Phosphoserine (By similarity).
FT   MOD_RES     256    256       N6-acetyllysine (By similarity).
FT   MOD_RES     263    263       Phosphoserine.
FT   MOD_RES     281    281       N6-acetyllysine (By similarity).
FT   MOD_RES     287    287       Phosphotyrosine (By similarity).
FT   MOD_RES     406    406       N6-acetyllysine (By similarity).
FT   MOD_RES     420    420       N6-acetyllysine (By similarity).
FT   CONFLICT    359    359       L -> P (in Ref. 1; CAA36605).
SQ   SEQUENCE   434 AA;  47141 MW;  DBEF6270A70DE3A6 CRC64;
     MSILRIHARE IFDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR DNDKTRFMGK
     GVSQAVEHIN KTIAPALVSK KVNVVEQEKI DKLMIEMDGT ENKSKFGANA ILGVSLAVCK
     AGAVEKGVPL YRHIADLAGN PEVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFRE
     AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEALELLKTA IAKAGYTDQV
     VIGMDVAASE FYRSGKYDLD FKSPDDPSRY ITPDQLADLY KSFVQNYPVV SIEDPFDQDD
     WGAWQKFTAS AGIQVVGDDL TVTNPKRIAK AASEKSCNCL LLKVNQIGSV TESLQACKLA
     QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQI LRIEEELGSK
     AKFAGRSFRN PLAK
//
ID   ENOG_MOUSE              Reviewed;         434 AA.
AC   P17183;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 112.
DE   RecName: Full=Gamma-enolase;
DE            EC=4.2.1.11;
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE   AltName: Full=Enolase 2;
DE   AltName: Full=Neural enolase;
DE   AltName: Full=Neuron-specific enolase;
DE            Short=NSE;
GN   Name=Eno2; Synonyms=Eno-2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=90301487; PubMed=2362815; DOI=10.1093/nar/18.12.3638;
RA   Kaghad M., Dumont X., Chalon P., Lelias J.M., Lamande N., Lucas M.,
RA   Lazar M., Caput D.;
RT   "Nucleotide sequences of cDNAs alpha and gamma enolase mRNAs from
RT   mouse brain.";
RL   Nucleic Acids Res. 18:3638-3638(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=98112780; PubMed=9445485;
RA   Ansari-Lari M.A., Oeltjen J.C., Schwartz S., Zhang Z., Muzny D.M.,
RA   Lu J., Gorrell J.H., Chinault A.C., Belmont J.W., Miller W.,
RA   Gibbs R.A.;
RT   "Comparative sequence analysis of a gene-rich cluster at human
RT   chromosome 12p13 and its syntenic region in mouse chromosome 6.";
RL   Genome Res. 8:29-40(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 16-28; 33-50; 73-89; 104-120; 163-179; 184-193;
RP   203-228; 240-262; 270-285; 307-326; 336-358; 373-394 AND 413-429, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15648052; DOI=10.1002/pmic.200401066;
RA   Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA   Hart G.W., Burlingame A.L.;
RT   "Quantitative analysis of both protein expression and serine /
RT   threonine post-translational modifications through stable isotope
RT   labeling with dithiothreitol.";
RL   Proteomics 5:388-398(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-25 AND TYR-44, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-25 AND TYR-44, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Has neurotrophic and neuroprotective properties on a
CC       broad spectrum of central nervous system (CNS) neurons. Binds, in
CC       a calcium-dependent manner, to cultured neocortical neurons and
CC       promotes cell survival (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate +
CC       H(2)O.
CC   -!- COFACTOR: Magnesium. Required for catalysis and for stabilizing
CC       the dimer.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5.
CC   -!- SUBUNIT: Mammalian enolase is composed of 3 isozyme subunits,
CC       alpha, beta and gamma, which can form homodimers or heterodimers
CC       which are cell-type and development-specific.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By
CC       similarity). Note=Can translocate to the plasma membrane in either
CC       the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form
CC       (By similarity).
CC   -!- TISSUE SPECIFICITY: The alpha/alpha homodimer is expressed in
CC       embryo and in most adult tissues. The alpha/beta heterodimer and
CC       the beta/beta homodimer are found in striated muscle, and the
CC       alpha/gamma heterodimer and the gamma/gamma homodimer in neurons.
CC   -!- DEVELOPMENTAL STAGE: During ontogenesis, there is a transition
CC       from the alpha/alpha homodimer to the alpha/beta heterodimer in
CC       striated muscle cells, and to the alpha/gamma heterodimer in nerve
CC       cells.
CC   -!- SIMILARITY: Belongs to the enolase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X52380; CAA36606.1; -; mRNA.
DR   EMBL; AC002397; AAC36002.1; -; Genomic_DNA.
DR   EMBL; BC031739; AAH31739.1; -; mRNA.
DR   IPI; IPI00331704; -.
DR   PIR; S10247; S10247.
DR   RefSeq; NP_038537.1; NM_013509.2.
DR   UniGene; Mm.3913; -.
DR   ProteinModelPortal; P17183; -.
DR   SMR; P17183; 2-434.
DR   STRING; P17183; -.
DR   PhosphoSite; P17183; -.
DR   UCD-2DPAGE; P17183; -.
DR   PRIDE; P17183; -.
DR   Ensembl; ENSMUST00000004378; ENSMUSP00000004378; ENSMUSG00000004267.
DR   GeneID; 13807; -.
DR   KEGG; mmu:13807; -.
DR   UCSC; uc009drs.1; mouse.
DR   CTD; 13807; -.
DR   MGI; MGI:95394; Eno2.
DR   eggNOG; roNOG10078; -.
DR   HOGENOM; HBG726599; -.
DR   HOVERGEN; HBG000067; -.
DR   InParanoid; P17183; -.
DR   OMA; GSHADSN; -.
DR   OrthoDB; EOG4T783B; -.
DR   PhylomeDB; P17183; -.
DR   BRENDA; 4.2.1.11; 244.
DR   NextBio; 284588; -.
DR   ArrayExpress; P17183; -.
DR   Bgee; P17183; -.
DR   CleanEx; MM_ENO2; -.
DR   Genevestigator; P17183; -.
DR   GermOnline; ENSMUSG00000004267; Mus musculus.
DR   GO; GO:0043204; C:perikaryon; IDA:MGI.
DR   GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR   GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR000941; Enolase.
DR   InterPro; IPR020810; Enolase_C.
DR   InterPro; IPR020809; Enolase_CS.
DR   InterPro; IPR020811; Enolase_N.
DR   Pfam; PF00113; Enolase_C; 1.
DR   Pfam; PF03952; Enolase_N; 1.
DR   PIRSF; PIRSF001400; Enolase; 1.
DR   PRINTS; PR00148; ENOLASE.
DR   TIGRFAMs; TIGR01060; eno; 1.
DR   PROSITE; PS00164; ENOLASE; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; Direct protein sequencing; Glycolysis;
KW   Lyase; Magnesium; Membrane; Metal-binding; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    434       Gamma-enolase.
FT                                /FTId=PRO_0000134113.
FT   REGION      370    373       Substrate binding (By similarity).
FT   ACT_SITE    210    210       Proton donor (By similarity).
FT   ACT_SITE    343    343       Proton acceptor (By similarity).
FT   METAL       245    245       Magnesium (By similarity).
FT   METAL       293    293       Magnesium (By similarity).
FT   METAL       318    318       Magnesium (By similarity).
FT   BINDING     158    158       Substrate (By similarity).
FT   BINDING     167    167       Substrate (By similarity).
FT   BINDING     293    293       Substrate (By similarity).
FT   BINDING     318    318       Substrate (By similarity).
FT   BINDING     394    394       Substrate (By similarity).
FT   MOD_RES      25     25       Phosphotyrosine.
FT   MOD_RES      44     44       Phosphotyrosine.
FT   MOD_RES      80     80       Phosphoserine.
SQ   SEQUENCE   434 AA;  47297 MW;  A5C7F189E913392E CRC64;
     MSIEKIWARE ILDSRGNPTV EVDLYTAKGL FRAAVPSGAS TGIYEALELR DGDKQRYLGK
     GVLKAVDHIN SRIAPALISS GISVVEQEKL DNLMLELDGT ENKSKFGANA ILGVSLAVCK
     AGAAERDLPL YRHIAQLAGN SDLILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAESFRD
     AMRLGAEVYH TLKGVIKDKY GKDATNVGDE GGFAPNILEN SEALELVKEA IDKAGYTEKM
     VIGMDVAASE FYRDGKYDLD FKSPADPSRY ITGDQLGALY QDFVRNYPVV SIEDPFDQDD
     WAAWSKFTAN VGIQIVGDDL TVTNPKRIER AVEEKACNCL LLKVNQIGSV TEAIQACKLA
     QENGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEELGDE
     ARFAGHNFRN PSVL
//
ID   AP2A1_MOUSE             Reviewed;         977 AA.
AC   P17426;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   08-MAR-2011, entry version 108.
DE   RecName: Full=AP-2 complex subunit alpha-1;
DE   AltName: Full=100 kDa coated vesicle protein A;
DE   AltName: Full=Adapter-related protein complex 2 alpha-1 subunit;
DE   AltName: Full=Adaptor protein complex AP-2 subunit alpha-1;
DE   AltName: Full=Alpha-adaptin A;
DE   AltName: Full=Alpha1-adaptin;
DE   AltName: Full=Clathrin assembly protein complex 2 alpha-A large chain;
DE   AltName: Full=Plasma membrane adaptor HA2/AP2 adaptin alpha A subunit;
GN   Name=Ap2a1; Synonyms=Adtaa, Clapa1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=89155572; PubMed=2564002; DOI=10.1083/jcb.108.3.833;
RA   Robinson M.S.;
RT   "Cloning of cDNAs encoding two related 100-kD coated vesicle proteins
RT   (alpha-adaptins).";
RL   J. Cell Biol. 108:833-842(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH CLATHRIN.
RX   PubMed=7559550; DOI=10.1074/jbc.270.40.23768;
RA   Goodman O.B. Jr., Keen J.H.;
RT   "The alpha chain of the AP-2 adaptor is a clathrin binding subunit.";
RL   J. Biol. Chem. 270:23768-23773(1995).
RN   [4]
RP   CHARACTERIZATION OF ISOFORMS A AND B.
RX   MEDLINE=96034323; PubMed=7593326;
RA   Ball C.L., Hunt S.P., Robinson M.S.;
RT   "Expression and localization of alpha-adaptin isoforms.";
RL   J. Cell Sci. 108:2865-2875(1995).
RN   [5]
RP   FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX   PubMed=14745134; DOI=10.1247/csf.28.419;
RA   Nakatsu F., Ohno H.;
RT   "Adaptor protein complexes as the key regulators of protein sorting in
RT   the post-Golgi network.";
RL   Cell Struct. Funct. 28:419-429(2003).
RN   [6]
RP   FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX   PubMed=15473838; DOI=10.1146/annurev.cellbio.20.010403.104543;
RA   Owen D.J., Collins B.M., Evans P.R.;
RT   "Adaptors for clathrin coats: structure and function.";
RL   Annu. Rev. Cell Dev. Biol. 20:153-191(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-650; SER-652; THR-653
RP   AND SER-655, AND MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-655, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [9]
RP   INTERACTION WITH SLC12A5.
RX   PubMed=18625303; DOI=10.1016/j.cellsig.2008.06.011;
RA   Zhao B., Wong A.Y.C., Murshid A., Bowie D., Presley J.F.,
RA   Bedford F.K.;
RT   "Identification of a novel di-leucine motif mediating K(+)/Cl(-)
RT   cotransporter KCC2 constitutive endocytosis.";
RL   Cell. Signal. 20:1769-1779(2008).
CC   -!- FUNCTION: Component of the adaptor protein complex 2 (AP-2).
CC       Adaptor protein complexes function in protein transport via
CC       transport vesicles in different membrane traffic pathways. Adaptor
CC       protein complexes are vesicle coat components and appear to be
CC       involved in cargo selection and vesicle formation. AP-2 is
CC       involved in clathrin-dependent endocytosis in which cargo proteins
CC       are incorporated into vesicles surrrounded by clathrin (clathrin-
CC       coated vesicles, CCVs) which are destined for fusion with the
CC       early endosome. The clathrin lattice serves as a mechanical
CC       scaffold but is itself unable to bind directly to membrane
CC       components. Clathrin-associated adaptor protein (AP) complexes
CC       which can bind directly to both the clathrin lattice and to the
CC       lipid and protein components of membranes are considered to be the
CC       major clathrin adaptors contributing the CCV formation. AP-2 also
CC       serves as a cargo receptor to selectively sort the membrane
CC       proteins involved in receptor-mediated endocytosis. AP-2 seems to
CC       play a role in the recycling of synaptic vesicle membranes from
CC       the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi)
CC       and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the
CC       cytosolic tails of transmembrane cargo molecules. AP-2 may also
CC       play a role in maintaining normal post-endocytic trafficking
CC       through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha
CC       subunit binds polyphosphoinositide-containing lipids, positioning
CC       AP-2 on the membrane. The AP-2 alpha subunit acts via its C-
CC       terminal appendage domain as a scaffolding platform for endocytic
CC       accessory proteins. The AP-2 alpha and AP-2 sigma subunits are
CC       thought to contribute to the recognition of the [ED]-X-X-X-L-[LI]
CC       motif (By similarity).
CC   -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is an heterotetramer
CC       composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2
CC       and beta-type subunit AP2B1), a medium adaptin (mu-type subunit
CC       AP2M1) and a small adaptin (sigma-type subunit AP2S1). Interacts
CC       with HIP1 and RAB11FIP2 (By similarity). Interacts with SLC12A5.
CC       Interacts with clathrin. Interacts with SLC12A5. Interacts with
CC       clathrin.
CC   -!- SUBCELLULAR LOCATION: Cell membrane (By similarity). Membrane,
CC       coated pit; Peripheral membrane protein; Cytoplasmic side (By
CC       similarity). Note=AP-2 appears to be excluded from internalizing
CC       CCVs and to disengage from sites of endocytosis seconds before
CC       internalization of the nascent CCV (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=P17426-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=P17426-2; Sequence=VSP_000162;
CC   -!- TISSUE SPECIFICITY: Isoform A is expressed only in neuronal tissue
CC       and skeletal muscle. Isoform B is widely expressed.
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC   -----------------------------------------------------------------------
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DR   EMBL; X14971; CAA33096.1; -; mRNA.
DR   EMBL; BC031433; AAH31433.1; -; mRNA.
DR   IPI; IPI00108780; -.
DR   IPI; IPI00622911; -.
DR   PIR; A30111; A30111.
DR   RefSeq; NP_001070732.1; NM_001077264.1.
DR   RefSeq; NP_031484.1; NM_007458.2.
DR   UniGene; Mm.6877; -.
DR   ProteinModelPortal; P17426; -.
DR   SMR; P17426; 3-621, 746-977.
DR   MINT; MINT-1865011; -.
DR   STRING; P17426; -.
DR   PhosphoSite; P17426; -.
DR   PRIDE; P17426; -.
DR   Ensembl; ENSMUST00000085399; ENSMUSP00000082519; ENSMUSG00000060279.
DR   Ensembl; ENSMUST00000107857; ENSMUSP00000103489; ENSMUSG00000060279.
DR   GeneID; 11771; -.
DR   KEGG; mmu:11771; -.
DR   UCSC; uc009grv.1; mouse.
DR   UCSC; uc009grw.1; mouse.
DR   CTD; 11771; -.
DR   MGI; MGI:101921; Ap2a1.
DR   eggNOG; roNOG04940; -.
DR   GeneTree; ENSGT00550000074757; -.
DR   HOGENOM; HBG315674; -.
DR   HOVERGEN; HBG050518; -.
DR   InParanoid; P17426; -.
DR   OMA; PSSHDIN; -.
DR   OrthoDB; EOG4HMJ8J; -.
DR   PhylomeDB; P17426; -.
DR   NextBio; 279549; -.
DR   PMAP-CutDB; P17426; -.
DR   ArrayExpress; P17426; -.
DR   Bgee; P17426; -.
DR   CleanEx; MM_AP2A1; -.
DR   Genevestigator; P17426; -.
DR   GermOnline; ENSMUSG00000060279; Mus musculus.
DR   GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR   GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030141; C:stored secretory granule; TAS:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR   InterPro; IPR017104; AP2_complex_asu.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR009028; Calthrin/coatomer_app_sub_C.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   InterPro; IPR013041; Clathrin/coatomer_app_Ig-like.
DR   InterPro; IPR013038; Clathrin_a-adaptin_app_Ig-like.
DR   InterPro; IPR003164; Clathrin_a-adaptin_app_sub_C.
DR   InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR   InterPro; IPR015873; Clathrin_a/coatomer_app_sub_C.
DR   Gene3D; G3DSA:3.30.310.30; AP2_A_adaptin_C; 1.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Gene3D; G3DSA:2.60.40.1030; Clathrin_a-adaptin_app_Ig-like; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   Pfam; PF02296; Alpha_adaptin_C; 1.
DR   Pfam; PF02883; Alpha_adaptinC2; 1.
DR   PIRSF; PIRSF037091; AP2_complex_alpha; 1.
DR   SMART; SM00809; Alpha_adaptinC2; 1.
DR   SUPFAM; SSF55711; AP2_adap_app; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF49348; Clath_adapt; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Coated pit; Endocytosis;
KW   Membrane; Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1    977       AP-2 complex subunit alpha-1.
FT                                /FTId=PRO_0000193731.
FT   MOD_RES     626    626       Phosphoserine (By similarity).
FT   MOD_RES     650    650       Phosphothreonine.
FT   MOD_RES     652    652       Phosphoserine.
FT   MOD_RES     653    653       Phosphothreonine.
FT   MOD_RES     655    655       Phosphoserine.
FT   MOD_RES     657    657       Phosphoserine (By similarity).
FT   VAR_SEQ     706    727       Missing (in isoform B).
FT                                /FTId=VSP_000162.
SQ   SEQUENCE   977 AA;  107664 MW;  F4ED87D3F9EF230A CRC64;
     MPAVSKGDGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL DGYSKKKYVC
     KLLFIFLLGH DIDFGHMEAV NLLSSNKYTE KQIGYLFISV LVNSNSELIR LINNAIKNDL
     ASRNPTFMCL ALHCIANVGS REMGEAFAAD IPRILVAGDS MDSVKQSAAL CLLRLYKASP
     DLVPMGEWTA RVVHLLNDQH MGVVTAAVSL ITCLCKKNPD DFKTCISLAV SRLSRIVSSA
     STDLQDYTYY FVPAPWLSVK LLRLLQCYPP PEDAAVKGRL VECLETVLNK AQEPPKSKKV
     QHSNAKNAIL FETISLIIHY DSEPNLLVRA CNQLGQFLQH RETNLRYLAL ESMCTLASSE
     FSHEAVKTHI DTVINALKTE RDVSVRQRAA DLLYAMCDRS NAKQIVSEML RYLETADYAI
     REEIVLKVAI LAEKYAVDYS WYVDTILNLI RIAGDYVSEE VWYRVLQIVT NRDDVQGYAA
     KTVFEALQAP ACHENMVKVG GYILGEFGNL IAGDPRSSPP VQFSLLHSKF HLCSVATRAL
     LLSTYIKFIN LFPETKATIQ GVLRAGSQLR NADVELQQRA VEYLTLSSVA STDVLATVLE
     EMPPFPERES SILAKLKRKK GPGAASALDD SRRDTSSNDI NGGVEPTPST VSTPSPSADL
     LGLRAAPPPA APPAPVGGNL LVDVFSDGPT AQPSLGPTPE EAFLSELEPP APESPMALLA
     DPAPAADPGP EDIGPPIPEA DELLNKFVCK NSGVLFENQL LQIGVKSEFR QNLGRMYLFY
     GNKTSVQFQN FLPTVVHPGD LQTQLAVQTK RVAAQVDGGA QVQQVLNIEC LRDFLTPPLL
     SVRFRYGGTA QSLTLKLPVT INKFFQPTEM AAQDFFQRWK QLSLPLQEAQ KIFKANHPMD
     AEVTKAKLLG FGSALLDNVD PNPENFVGAG IIQTKALQVG CLLRLEPNAQ AQMYRLTLRT
     SKEPVSRHLC ELLAQQF
//
ID   AP2A2_MOUSE             Reviewed;         938 AA.
AC   P17427; Q921V0;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   08-MAR-2011, entry version 119.
DE   RecName: Full=AP-2 complex subunit alpha-2;
DE   AltName: Full=100 kDa coated vesicle protein C;
DE   AltName: Full=Adapter-related protein complex 2 alpha-2 subunit;
DE   AltName: Full=Adaptor protein complex AP-2 subunit alpha-2;
DE   AltName: Full=Alpha-adaptin C;
DE   AltName: Full=Alpha2-adaptin;
DE   AltName: Full=Clathrin assembly protein complex 2 alpha-C large chain;
DE   AltName: Full=Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit;
GN   Name=Ap2a2; Synonyms=Adtab;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=89155572; PubMed=2564002; DOI=10.1083/jcb.108.3.833;
RA   Robinson M.S.;
RT   "Cloning of cDNAs encoding two related 100-kD coated vesicle proteins
RT   (alpha-adaptins).";
RL   J. Cell Biol. 108:833-842(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 104-859.
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 379-938.
RC   TISSUE=Fetal liver;
RX   MEDLINE=98284108; PubMed=9618202; DOI=10.1006/abio.1998.2653;
RA   Jurecic R., Nachtman R.G., Colicos S.M., Belmont J.W.;
RT   "Identification and cloning of differentially expressed genes by long-
RT   distance differential display.";
RL   Anal. Biochem. 259:235-244(1998).
RN   [4]
RP   FUNCTION, SUBUNIT, INTERACTION WITH CLATHRIN, AND MUTAGENESIS OF
RP   LYS-31; ARG-32; LYS-35; LYS-45; LYS-55; LYS-56; LYS-57 AND LYS-61.
RX   MEDLINE=99389738; PubMed=10459011; DOI=10.1083/jcb.146.4.755;
RA   Gaidarov I., Keen J.H.;
RT   "Phosphoinositide-AP-2 interactions required for targeting to plasma
RT   membrane clathrin-coated pits.";
RL   J. Cell Biol. 146:755-764(1999).
RN   [5]
RP   FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX   PubMed=14745134; DOI=10.1247/csf.28.419;
RA   Nakatsu F., Ohno H.;
RT   "Adaptor protein complexes as the key regulators of protein sorting in
RT   the post-Golgi network.";
RL   Cell Struct. Funct. 28:419-429(2003).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=14530274; DOI=10.1074/jbc.C300390200;
RA   Rappoport J.Z., Taha B.W., Lemeer S., Benmerah A., Simon S.M.;
RT   "The AP-2 complex is excluded from the dynamic population of plasma
RT   membrane-associated clathrin.";
RL   J. Biol. Chem. 278:47357-47360(2003).
RN   [7]
RP   FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX   PubMed=15473838; DOI=10.1146/annurev.cellbio.20.010403.104543;
RA   Owen D.J., Collins B.M., Evans P.R.;
RT   "Adaptors for clathrin coats: structure and function.";
RL   Annu. Rev. Cell Dev. Biol. 20:153-191(2004).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17035303; DOI=10.1152/ajpcell.00160.2006;
RA   Rappoport J.Z., Kemal S., Benmerah A., Simon S.M.;
RT   "Dynamics of clathrin and adaptor proteins during endocytosis.";
RL   Am. J. Physiol. 291:C1072-C1081(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-807, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [10]
RP   INTERACTION WITH DKGD, AND MUTAGENESIS OF TRP-840.
RX   PubMed=17880279; DOI=10.1042/BJ20070755;
RA   Kawasaki T., Kobayashi T., Ueyama T., Shirai Y., Saito N.;
RT   "Regulation of clathrin-dependent endocytosis by diacylglycerol kinase
RT   delta: importance of kinase activity and binding to AP2alpha.";
RL   Biochem. J. 409:471-479(2008).
RN   [11]
RP   INTERACTION WITH DENND1A; DENND1B AND DENND1C, AND MUTAGENESIS OF
RP   GLN-782 AND ARG-916.
RX   PubMed=20154091; DOI=10.1074/jbc.M109.050930;
RA   Marat A.L., McPherson P.S.;
RT   "The connecdenn family, Rab35 guanine nucleotide exchange factors
RT   interfacing with the clathrin machinery.";
RL   J. Biol. Chem. 285:10627-10637(2010).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 701-938, MUTAGENESIS OF
RP   PHE-837; TRP-840; GLU-849; ARG-905; GLU-907 AND ARG-920, AND
RP   INTERACTION WITH AMPH; EPS15; EPN1; SNAP91; BIN1 AND AUXILIN.
RX   PubMed=10380931; DOI=10.1016/S0092-8674(00)80791-6;
RA   Owen D.J., Vallis Y., Noble M.E.M., Hunter J.B., Dafforn T.R.,
RA   Evans P.R., McMahon H.T.;
RT   "A structural explanation for the binding of multiple ligands by the
RT   alpha-adaptin appendage domain.";
RL   Cell 97:805-815(1999).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 9-592 IN COMPLEX WITH AP2B1;
RP   AP2M1; AP2S1 AND AN INOSITOL POLYPHOSPHATE HEADGROUP.
RX   PubMed=12086608; DOI=10.1016/S0092-8674(02)00735-3;
RA   Collins B.M., McCoy A.J., Kent H.M., Evans P.R., Owen D.J.;
RT   "Molecular architecture and functional model of the endocytic AP2
RT   complex.";
RL   Cell 109:523-535(2002).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 701-938 IN COMPLEX WITH
RP   EPS15; EPN1 OR AMPH.
RX   PubMed=12057195; DOI=10.1016/S0969-2126(02)00784-0;
RA   Brett T.J., Traub L.M., Fremont D.H.;
RT   "Accessory protein recruitment motifs in clathrin-mediated
RT   endocytosis.";
RL   Structure 10:797-809(2002).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 692-938, MUTAGENESIS OF
RP   PHE-837; ARG-905 AND ARG-916, AND INTERACTION WITH EPN1; EPS15; AMPH;
RP   SNAP91 AND BIN1.
RX   PubMed=10430869; DOI=10.1073/pnas.96.16.8907;
RA   Traub L.M., Downs M.A., Westrich J.L., Fremont D.H.;
RT   "Crystal structure of the alpha appendage of AP-2 reveals a
RT   recruitment platform for clathrin-coat assembly.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:8907-8912(1999).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-620 IN COMPLEX WITH AP2B1;
RP   AP2M1; AP2S1 AND CD4 INTERNALIZATION SIGNAL, AND MUTAGENESIS OF
RP   ARG-21.
RX   PubMed=18978775; DOI=10.1038/nature07422;
RA   Kelly B.T., McCoy A.J., Spaete K., Miller S.E., Evans P.R.,
RA   Hoening S., Owen D.J.;
RT   "A structural explanation for the binding of endocytic dileucine
RT   motifs by the AP2 complex.";
RL   Nature 456:976-979(2008).
CC   -!- FUNCTION: Component of the adaptor protein complex 2 (AP-2).
CC       Adaptor protein complexes function in protein transport via
CC       transport vesicles in different membrane traffic pathways. Adaptor
CC       protein complexes are vesicle coat components and appear to be
CC       involved in cargo selection and vesicle formation. AP-2 is
CC       involved in clathrin-dependent endocytosis in which cargo proteins
CC       are incorporated into vesicles surrrounded by clathrin (clathrin-
CC       coated vesicles, CCVs) which are destined for fusion with the
CC       early endosome. The clathrin lattice serves as a mechanical
CC       scaffold but is itself unable to bind directly to membrane
CC       components. Clathrin-associated adaptor protein (AP) complexes
CC       which can bind directly to both the clathrin lattice and to the
CC       lipid and protein components of membranes are considered to be the
CC       major clathrin adaptors contributing the CCV formation. AP-2 also
CC       serves as a cargo receptor to selectively sort the membrane
CC       proteins involved in receptor-mediated endocytosis. AP-2 seems to
CC       play a role in the recycling of synaptic vesicle membranes from
CC       the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi)
CC       and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the
CC       cytosolic tails of transmembrane cargo molecules. AP-2 may also
CC       play a role in maintaining normal post-endocytic trafficking
CC       through the ARF6-regulated, non-clathrin pathway. The AP-2 alpha
CC       subunit binds polyphosphoinositide-containing lipids, positioning
CC       AP-2 on the membrane. The AP-2 alpha subunit acts via its C-
CC       terminal appendage domain as a scaffolding platform for endocytic
CC       accessory proteins. The AP-2 alpha and AP-2 sigma subunits are
CC       thought to contribute to the recognition of the [ED]-X-X-X-L-[LI]
CC       motif.
CC   -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is an heterotetramer
CC       composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2
CC       and beta-type subunit AP2B1), a medium adaptin (mu-type subunit
CC       AP2M1) and a small adaptin (sigma-type subunit AP2S1). Binds EPN1,
CC       EPS15, AMPH, SNAP91 and BIN1. Interacts with HIP1 (By similarity).
CC       Interacts with DGKD isoform 2. Interacts with DENND1A, DENND1B and
CC       DENND1C.
CC   -!- SUBCELLULAR LOCATION: Cell membrane. Membrane, coated pit;
CC       Peripheral membrane protein; Cytoplasmic side. Note=AP-2 appears
CC       to be excluded from internalizing CCVs and to disengage from sites
CC       of endocytosis seconds before internalization of the nascent CCV.
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC   -----------------------------------------------------------------------
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DR   EMBL; X14972; CAA33097.1; -; mRNA.
DR   EMBL; BC010597; AAH10597.1; -; mRNA.
DR   EMBL; AF006990; AAB62703.1; -; mRNA.
DR   IPI; IPI00310131; -.
DR   PIR; B30111; B30111.
DR   PIR; S12471; S12471.
DR   UniGene; Mm.253090; -.
DR   PDB; 1B9K; X-ray; 1.90 A; A=701-938.
DR   PDB; 1KY6; X-ray; 2.00 A; A=701-938.
DR   PDB; 1KY7; X-ray; 2.15 A; A=701-938.
DR   PDB; 1KYD; X-ray; 2.00 A; A=701-938.
DR   PDB; 1KYF; X-ray; 1.22 A; A=701-938.
DR   PDB; 1KYU; X-ray; 1.80 A; A=701-938.
DR   PDB; 1QTP; X-ray; 1.60 A; A=701-938.
DR   PDB; 1QTS; X-ray; 1.40 A; A=701-938.
DR   PDB; 1W80; X-ray; 1.90 A; A=695-938.
DR   PDB; 2JKR; X-ray; 2.98 A; A/L=1-620.
DR   PDB; 2JKT; X-ray; 3.40 A; A/L=1-620.
DR   PDB; 2VJ0; X-ray; 1.60 A; A=695-938.
DR   PDB; 3HS8; X-ray; 1.90 A; A=702-938.
DR   PDBsum; 1B9K; -.
DR   PDBsum; 1KY6; -.
DR   PDBsum; 1KY7; -.
DR   PDBsum; 1KYD; -.
DR   PDBsum; 1KYF; -.
DR   PDBsum; 1KYU; -.
DR   PDBsum; 1QTP; -.
DR   PDBsum; 1QTS; -.
DR   PDBsum; 1W80; -.
DR   PDBsum; 2JKR; -.
DR   PDBsum; 2JKT; -.
DR   PDBsum; 2VJ0; -.
DR   PDBsum; 3HS8; -.
DR   ProteinModelPortal; P17427; -.
DR   SMR; P17427; 9-607, 701-938.
DR   MINT; MINT-101068; -.
DR   STRING; P17427; -.
DR   PhosphoSite; P17427; -.
DR   PRIDE; P17427; -.
DR   Ensembl; ENSMUST00000003038; ENSMUSP00000003038; ENSMUSG00000002957.
DR   MGI; MGI:101920; Ap2a2.
DR   eggNOG; roNOG04940; -.
DR   HOVERGEN; HBG050518; -.
DR   InParanoid; P17427; -.
DR   OrthoDB; EOG4HMJ8J; -.
DR   PhylomeDB; P17427; -.
DR   PMAP-CutDB; P17427; -.
DR   ArrayExpress; P17427; -.
DR   Bgee; P17427; -.
DR   CleanEx; MM_AP2A2; -.
DR   Genevestigator; P17427; -.
DR   GermOnline; ENSMUSG00000002957; Mus musculus.
DR   GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR   GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030141; C:stored secretory granule; TAS:MGI.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR   InterPro; IPR017104; AP2_complex_asu.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR009028; Calthrin/coatomer_app_sub_C.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   InterPro; IPR013041; Clathrin/coatomer_app_Ig-like.
DR   InterPro; IPR013038; Clathrin_a-adaptin_app_Ig-like.
DR   InterPro; IPR003164; Clathrin_a-adaptin_app_sub_C.
DR   InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR   InterPro; IPR015873; Clathrin_a/coatomer_app_sub_C.
DR   Gene3D; G3DSA:3.30.310.30; AP2_A_adaptin_C; 1.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Gene3D; G3DSA:2.60.40.1030; Clathrin_a-adaptin_app_Ig-like; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   Pfam; PF02296; Alpha_adaptin_C; 1.
DR   Pfam; PF02883; Alpha_adaptinC2; 1.
DR   PIRSF; PIRSF037091; AP2_complex_alpha; 1.
DR   SMART; SM00809; Alpha_adaptinC2; 1.
DR   SUPFAM; SSF55711; AP2_adap_app; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF49348; Clath_adapt; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell membrane; Coated pit; Endocytosis;
KW   Lipid-binding; Membrane; Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1    938       AP-2 complex subunit alpha-2.
FT                                /FTId=PRO_0000193733.
FT   REGION        5     80       Lipid-binding.
FT   BINDING      43     43       Phosphatidylinositol lipid headgroup.
FT   BINDING      53     53       Phosphatidylinositol lipid headgroup.
FT   BINDING      57     57       Phosphatidylinositol lipid headgroup.
FT   BINDING      58     58       Phosphatidylinositol lipid headgroup.
FT   BINDING      61     61       Phosphatidylinositol lipid headgroup.
FT   MOD_RES      35     35       N6-acetyllysine (By similarity).
FT   MOD_RES     807    807       Phosphotyrosine.
FT   MUTAGEN      21     21       R->E: Reduces interaction with CD4
FT                                endocytosis signal motif; when associated
FT                                with AP2S1 S-15.
FT   MUTAGEN      31     31       K->Q: Reduces phosphatidylinositol
FT                                binding.
FT   MUTAGEN      32     32       R->Q: Reduces phosphatidylinositol
FT                                binding.
FT   MUTAGEN      35     35       K->Q: Reduces phosphatidylinositol
FT                                binding.
FT   MUTAGEN      45     45       K->Q: Reduces phosphatidylinositol
FT                                binding.
FT   MUTAGEN      55     55       K->Q: Strongly reduces
FT                                phosphatidylinositol binding. Abolishes
FT                                phosphatidylinositol binding; when
FT                                associated with Q-56 and Q-57.
FT   MUTAGEN      56     56       K->E: Strongly reduces
FT                                phosphatidylinositol binding.
FT   MUTAGEN      56     56       K->Q: Strongly reduces
FT                                phosphatidylinositol binding. Abolishes
FT                                phosphatidylinositol binding; when
FT                                associated with Q-55 and Q-57.
FT   MUTAGEN      57     57       K->Q: Strongly reduces
FT                                phosphatidylinositol binding. Abolishes
FT                                phosphatidylinositol binding; when
FT                                associated with Q-55 and Q-56.
FT   MUTAGEN      61     61       K->Q: Reduces phosphatidylinositol
FT                                binding.
FT   MUTAGEN     727    727       K->A: No effect on DENND1A-,DENND1B- nor
FT                                DENND1C-binding.
FT   MUTAGEN     782    782       Q->A: Reduces DENND1A- and DENND1C-
FT                                binding.
FT   MUTAGEN     837    837       F->A: Reduces SNAP91, AMPH and BIN1
FT                                binding. Abolishes AMPH and SNAP91
FT                                binding; when associated with A-916.
FT                                Abolishes EPN1 and EPS15 binding; when
FT                                associated with A-905.
FT   MUTAGEN     840    840       W->A: Abolishes AMPH, BIN1, EPS15, EPN1,
FT                                auxilin and SNAP91 binding. Abolishes
FT                                interaction with DGKD.
FT   MUTAGEN     849    849       E->A: No effect.
FT   MUTAGEN     905    905       R->A: Strongly reduces AMPH, SNAP91,
FT                                auxilin and BIN1 binding. Abolishes EPN1
FT                                and EPS15 binding; when associated with
FT                                A-837.
FT   MUTAGEN     907    907       E->A: Strongly reduces AMPH, SNAP91 and
FT                                BIN1 binding. Slightly reduces EPS15 and
FT                                auxilin binding.
FT   MUTAGEN     916    916       R->A: Strongly reduces AMPH and SNAP91
FT                                binding. Abolishes DENND1B-binding; no
FT                                effect on DENND1A-, nor DENND1C-binding.
FT                                Abolishes AMPH and SNAP91 binding; when
FT                                associated with A-837.
FT   MUTAGEN     920    920       R->A: Abolishes AMPH and BIN1 binding.
FT                                Reduces EPS15, SNAP91 and auxilin
FT                                binding.
FT   CONFLICT    858    859       HP -> LE (in Ref. 2; AAH10597).
FT   HELIX        11     21
FT   HELIX        26     45
FT   STRAND       46     48
FT   HELIX        52     68
FT   HELIX        76     81
FT   HELIX        82     84
FT   HELIX        88    100
FT   HELIX       106    121
FT   HELIX       125    138
FT   HELIX       141    147
FT   HELIX       150    156
FT   STRAND      158    160
FT   HELIX       162    178
FT   HELIX       180    182
FT   HELIX       189    195
FT   HELIX       201    215
FT   HELIX       219    222
FT   HELIX       225    238
FT   STRAND      252    254
FT   HELIX       255    264
FT   HELIX       265    267
FT   STRAND      268    270
FT   HELIX       273    289
FT   HELIX       299    319
FT   HELIX       323    336
FT   HELIX       342    356
FT   TURN        359    361
FT   HELIX       362    366
FT   HELIX       369    378
FT   HELIX       382    394
FT   TURN        398    400
FT   HELIX       401    414
FT   HELIX       417    434
FT   HELIX       438    452
FT   HELIX       453    455
FT   HELIX       458    470
FT   HELIX       475    486
FT   HELIX       493    506
FT   HELIX       516    522
FT   HELIX       528    534
FT   HELIX       546    554
FT   HELIX       561    573
FT   HELIX       578    581
FT   TURN        582    584
FT   HELIX       705    708
FT   STRAND      714    718
FT   STRAND      720    731
FT   STRAND      734    743
FT   STRAND      745    747
FT   STRAND      749    757
FT   HELIX       760    765
FT   STRAND      766    770
FT   STRAND      782    791
FT   STRAND      800    807
FT   STRAND      810    817
FT   HELIX       822    825
FT   STRAND      826    828
FT   HELIX       833    840
FT   HELIX       846    848
FT   STRAND      849    855
FT   HELIX       862    872
FT   STRAND      874    877
FT   STRAND      879    883
FT   STRAND      886    894
FT   STRAND      899    909
FT   TURN        910    913
FT   STRAND      914    923
FT   HELIX       924    935
SQ   SEQUENCE   938 AA;  104101 MW;  10C92E0C7AE9DBCA CRC64;
     MPAVSKGDGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL DGYSKKKYVC
     KLLFIFLLGH DIDFGHMEAV NLLSSNRYTE KQIGYLFISV LVNSNSELIR LINNAIKNDL
     ASRNPTFMGL ALHCIANVGS REMAEAFAGE IPKILVAGDT MDSVKQSAAL CLLRLYRTSP
     DLVPMGDWTS RVVHLLNDQH LGVVTAATSL ITTLAQKNPE EFKTSVSLAV SRLSRIVTSA
     STDLQDYTYY FVPAPWLSVK LLRLLQCYPP PDPAVRGRLT ECLETILNKA QEPPKSKKVQ
     HSNAKNAVLF EAISLIIHHD SEPNLLVRAC NQLGQFLQHR ETNLRYLALE SMCTLASSEF
     SHEAVKTHIE TVINALKTER DVSVRQRAVD LLYAMCDRSN AQQIVAEMLS YLETADYSIR
     EEIVLKVAIL AEKYAVDYTW YVDTILNLIR IAGDYVSEEV WYRVIQIVIN RDDVQGYAAK
     TVFEALQAPA CHENLVKVGG YILGEFGNLI AGDPRSSPLI QFNLLHSKFH LCSVPTRALL
     LSTYIKFVNL FPEVKATIQD VLRSDSQLKN ADVELQQRAV EYLRLSTVAS TDILATVLEE
     MPPFPERESS ILAKLKKKKG PSTVTDLEET KRERSIDVNG GPEPVPASTS AASTPSPSAD
     LLGLGAVPPA PTGPPPSSGG GLLVDVFSDS ASAVAPLAPG SEDNFARFVC KNNGVLFENQ
     LLQIGLKSEF RQNLGRMFIF YGNKTSTQFL NFTPTLICAD DLQTNLNLQT KPVDPTVDGG
     AQVQQVVNIE CISDFTEAPV LNIQFRYGGT FQNVSVKLPI TLNKFFQPTE MASQDFFQRW
     KQLSNPQQEV QNIFKAKHPM DTEITKAKII GFGSALLEEV DPNPANFVVL GIIHTKTTQI
     GCLLRLEPNL QAQMYRLTLR TSKDTVSQRL CELLSEQF
//
ID   PPIA_MOUSE              Reviewed;         164 AA.
AC   P17742; Q9CWJ5; Q9R137;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 122.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase A;
DE            Short=PPIase A;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin A;
DE   AltName: Full=Cyclosporin A-binding protein;
DE   AltName: Full=Rotamase A;
DE   AltName: Full=SP18;
GN   Name=Ppia;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X CBA; TISSUE=Thymus;
RX   MEDLINE=90326555; PubMed=2197604; DOI=10.1093/nar/18.13.4019;
RA   Hasel K.W., Sutcliffe J.G.;
RT   "Nucleotide sequence of a cDNA coding for mouse cyclophilin.";
RL   Nucleic Acids Res. 18:4019-4019(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryo, Embryonic stem cell, Kidney, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-20; 22-28 AND 77-85.
RC   TISSUE=Macrophage;
RX   MEDLINE=92228816; PubMed=1565646; DOI=10.1073/pnas.89.8.3511;
RA   Sherry B., Yarlett N., Strupp A., Cerami A.;
RT   "Identification of cyclophilin as a proinflammatory secretory product
RT   of lipopolysaccharide-activated macrophages.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:3511-3515(1992).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-21.
RC   TISSUE=Macrophage;
RX   MEDLINE=95394146; PubMed=7664883; DOI=10.1016/0014-5793(95)00815-Q;
RA   Krummrei U., Bang R., Schmidtchen R., Brune K., Bang H.;
RT   "Cyclophilin-A is a zinc-dependent DNA binding protein in
RT   macrophages.";
RL   FEBS Lett. 371:47-51(1995).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-31; 56-59; 77-118; 132-144 AND 155-164, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-63.
RC   STRAIN=129/Ola;
RX   MEDLINE=20422670; PubMed=10964515; DOI=10.1006/geno.2000.6295;
RA   Colgan J., Asmal M., Luban J.;
RT   "Isolation, characterization and targeted disruption of mouse Ppia:
RT   cyclophilin A is not essential for mammalian cell viability.";
RL   Genomics 68:167-178(2000).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15648052; DOI=10.1002/pmic.200401066;
RA   Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA   Hart G.W., Burlingame A.L.;
RT   "Quantitative analysis of both protein expression and serine /
RT   threonine post-translational modifications through stable isotope
RT   labeling with dithiothreitol.";
RL   Proteomics 5:388-398(2005).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC       the cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides.
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- ENZYME REGULATION: Binds cyclosporin A (CsA). CsA mediates some of
CC       its effects via an inhibitory action on PPIase.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase
CC       A subfamily.
CC   -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; X52803; CAA36989.1; -; mRNA.
DR   EMBL; AK002236; BAB21954.1; -; mRNA.
DR   EMBL; AK007981; BAB25387.1; -; mRNA.
DR   EMBL; AK010649; BAB27089.1; -; mRNA.
DR   EMBL; AK012531; BAB28300.1; -; mRNA.
DR   EMBL; AK012663; BAB28392.1; -; mRNA.
DR   EMBL; AK028210; BAC25817.1; -; mRNA.
DR   EMBL; BC083076; AAH83076.1; -; mRNA.
DR   EMBL; AF171073; AAD50996.1; -; Genomic_DNA.
DR   IPI; IPI00554989; -.
DR   PIR; S10327; CSMSA.
DR   RefSeq; NP_032933.1; NM_008907.1.
DR   UniGene; Mm.440058; -.
DR   UniGene; Mm.5246; -.
DR   ProteinModelPortal; P17742; -.
DR   SMR; P17742; 2-164.
DR   STRING; P17742; -.
DR   PhosphoSite; P17742; -.
DR   SWISS-2DPAGE; P17742; -.
DR   REPRODUCTION-2DPAGE; P17742; -.
DR   UCD-2DPAGE; P17742; -.
DR   PRIDE; P17742; -.
DR   Ensembl; ENSMUST00000071781; ENSMUSP00000071686; ENSMUSG00000062933.
DR   GeneID; 268373; -.
DR   KEGG; mmu:268373; -.
DR   UCSC; uc007hyn.1; mouse.
DR   CTD; 268373; -.
DR   MGI; MGI:97749; Ppia.
DR   eggNOG; roNOG10445; -.
DR   HOVERGEN; HBG001065; -.
DR   InParanoid; P17742; -.
DR   OMA; HSGPGCL; -.
DR   OrthoDB; EOG4DJJXN; -.
DR   PhylomeDB; P17742; -.
DR   BRENDA; 5.2.1.8; 244.
DR   NextBio; 392255; -.
DR   ArrayExpress; P17742; -.
DR   CleanEx; MM_PPIA; -.
DR   Genevestigator; P17742; -.
DR   GermOnline; ENSMUSG00000059583; Mus musculus.
DR   GermOnline; ENSMUSG00000062933; Mus musculus.
DR   GermOnline; ENSMUSG00000071866; Mus musculus.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0042277; F:peptide binding; IEA:UniProtKB-KW.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR   GO; GO:0045069; P:regulation of viral genome replication; ISS:UniProtKB.
DR   InterPro; IPR015891; Cyclophilin-like.
DR   InterPro; IPR020892; Pep-Pro_Isoase_cyclophilin_CS.
DR   InterPro; IPR002130; PPIase_cyclophilin.
DR   Gene3D; G3DSA:2.40.100.10; PPIase_cyclophilin; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SUPFAM; SSF50891; CSA_PPIase; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cyclosporin; Cytoplasm; Direct protein sequencing;
KW   Isomerase; Isopeptide bond; Phosphoprotein; Rotamase; Ubl conjugation.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    164       Peptidyl-prolyl cis-trans isomerase A.
FT                                /FTId=PRO_0000064117.
FT   DOMAIN        7    163       PPIase cyclophilin-type.
FT   MOD_RES       2      2       N-acetylvaline (By similarity).
FT   MOD_RES      21     21       Phosphoserine.
FT   MOD_RES      28     28       N6-acetyllysine (By similarity).
FT   MOD_RES      44     44       N6-acetyllysine (By similarity).
FT   MOD_RES      49     49       N6-acetyllysine (By similarity).
FT   MOD_RES      82     82       N6-acetyllysine (By similarity).
FT   MOD_RES     125    125       N6-acetyllysine (By similarity).
FT   MOD_RES     131    131       N6-acetyllysine (By similarity).
FT   MOD_RES     157    157       Phosphothreonine (By similarity).
FT   CROSSLNK     28     28       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CONFLICT     13     14       DD -> NE (in Ref. 2; BAB27089).
FT   CONFLICT     18     20       GRV -> TXP (in Ref. 4; AA sequence).
SQ   SEQUENCE   164 AA;  17971 MW;  3528824224EA8849 CRC64;
     MVNPTVFFDI TADDEPLGRV SFELFADKVP KTAENFRALS TGEKGFGYKG SSFHRIIPGF
     MCQGGDFTRH NGTGGRSIYG EKFEDENFIL KHTGPGILSM ANAGPNTNGS QFFICTAKTE
     WLDGKHVVFG KVKEGMNIVE AMERFGSRNG KTSKKITISD CGQL
//
ID   TPIS_MOUSE              Reviewed;         249 AA.
AC   P17751; Q3TJH2; Q3UC04; Q3UKG9; Q64513; Q9CVF9; Q9CWE7;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 105.
DE   RecName: Full=Triosephosphate isomerase;
DE            Short=TIM;
DE            EC=5.3.1.1;
DE   AltName: Full=Triose-phosphate isomerase;
GN   Name=Tpi1; Synonyms=Tpi;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90332435; PubMed=2377473; DOI=10.1093/nar/18.14.4261;
RA   Cheng J., Mielnicki L.M., Pruitt S.C., Maquat L.E.;
RT   "Nucleotide sequence of murine triosephosphate isomerase cDNA.";
RL   Nucleic Acids Res. 18:4261-4261(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=98112780; PubMed=9445485;
RA   Ansari-Lari M.A., Oeltjen J.C., Schwartz S., Zhang Z., Muzny D.M.,
RA   Lu J., Gorrell J.H., Chinault A.C., Belmont J.W., Miller W.,
RA   Gibbs R.A.;
RT   "Comparative sequence analysis of a gene-rich cluster at human
RT   chromosome 12p13 and its syntenic region in mouse chromosome 6.";
RL   Genome Res. 8:29-40(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Placenta, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 6-14; 21-53; 60-131; 143-156; 161-188; 195-206 AND
RP   220-248, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Yang J.W., Zigmond M., Kang S.U., Sunyer B.,
RA   Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 40-249, AND MUTAGENESIS OF
RP   LEU-163 AND LEU-193.
RX   MEDLINE=95258008; PubMed=7739600; DOI=10.1016/0027-5107(95)00004-3;
RA   Zingg B.C., Pretsch W., Mohrenweiser H.W.;
RT   "Molecular analysis of four ENU induced triosephosphate isomerase null
RT   mutants in Mus musculus.";
RL   Mutat. Res. 328:163-173(1995).
RN   [7]
RP   NITRATION [LARGE SCALE ANALYSIS] AT TYR-68 AND TYR-209, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16800626; DOI=10.1021/bi060474w;
RA   Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
RA   Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
RA   Squier T.C., Bigelow D.J.;
RT   "Endogenously nitrated proteins in mouse brain: links to
RT   neurodegenerative disease.";
RL   Biochemistry 45:8009-8022(2006).
CC   -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate = glycerone
CC       phosphate.
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate from glycerone phosphate: step 1/1.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the triosephosphate isomerase family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC002397; AAC36016.1; -; Genomic_DNA.
DR   EMBL; X53333; CAA37420.1; -; mRNA.
DR   EMBL; AK008373; BAB25634.1; -; mRNA.
DR   EMBL; AK010808; BAB27194.1; -; mRNA.
DR   EMBL; AK146013; BAE26832.1; -; mRNA.
DR   EMBL; AK149768; BAE29073.1; -; mRNA.
DR   EMBL; AK150735; BAE29810.1; -; mRNA.
DR   EMBL; AK159741; BAE35334.1; -; mRNA.
DR   EMBL; AK167437; BAE39523.1; -; mRNA.
DR   EMBL; AK168446; BAE40350.1; -; mRNA.
DR   EMBL; AK168756; BAE40594.1; -; mRNA.
DR   EMBL; BC046761; AAH46761.1; -; mRNA.
DR   EMBL; L31777; AAB48543.1; -; Genomic_DNA.
DR   IPI; IPI00467833; -.
DR   PIR; S10490; ISMST.
DR   RefSeq; NP_033441.2; NM_009415.2.
DR   UniGene; Mm.391520; -.
DR   UniGene; Mm.4222; -.
DR   UniGene; Mm.439915; -.
DR   ProteinModelPortal; P17751; -.
DR   SMR; P17751; 5-249.
DR   STRING; P17751; -.
DR   PhosphoSite; P17751; -.
DR   SWISS-2DPAGE; P17751; -.
DR   COMPLUYEAST-2DPAGE; P17751; -.
DR   REPRODUCTION-2DPAGE; IPI00467833; -.
DR   REPRODUCTION-2DPAGE; P17751; -.
DR   UCD-2DPAGE; P17751; -.
DR   PRIDE; P17751; -.
DR   Ensembl; ENSMUST00000024223; ENSMUSP00000024223; ENSMUSG00000023456.
DR   GeneID; 21991; -.
DR   KEGG; mmu:21991; -.
DR   NMPDR; fig|10090.3.peg.15242; -.
DR   UCSC; uc009drz.1; mouse.
DR   CTD; 21991; -.
DR   MGI; MGI:98797; Tpi1.
DR   eggNOG; roNOG08237; -.
DR   GeneTree; ENSGT00390000013354; -.
DR   HOVERGEN; HBG002599; -.
DR   InParanoid; P17751; -.
DR   OMA; VKIINAR; -.
DR   OrthoDB; EOG40S0GF; -.
DR   PhylomeDB; P17751; -.
DR   BRENDA; 5.3.1.1; 244.
DR   NextBio; 301728; -.
DR   ArrayExpress; P17751; -.
DR   Bgee; P17751; -.
DR   CleanEx; MM_TPI1; -.
DR   Genevestigator; P17751; -.
DR   GermOnline; ENSMUSG00000023456; Mus musculus.
DR   GO; GO:0004807; F:triose-phosphate isomerase activity; IDA:MGI.
DR   GO; GO:0009790; P:embryo development; IMP:MGI.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0019682; P:glyceraldehyde-3-phosphate metabolic process; IDA:UniProtKB.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-KW.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR022896; TrioseP_Isoase_bac/euk.
DR   InterPro; IPR000652; Triosephosphate_isomerase.
DR   InterPro; IPR020861; Triosephosphate_isomerase_AS.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   PANTHER; PTHR21139; Triophos_ismrse; 1.
DR   Pfam; PF00121; TIM; 1.
DR   SUPFAM; SSF51351; Triophos_ismrse; 1.
DR   TIGRFAMs; TIGR00419; tim; 1.
DR   PROSITE; PS00171; TIM_1; 1.
DR   PROSITE; PS51440; TIM_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Fatty acid biosynthesis;
KW   Gluconeogenesis; Glycolysis; Isomerase; Lipid synthesis; Nitration;
KW   Pentose shunt; Phosphoprotein.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    249       Triosephosphate isomerase.
FT                                /FTId=PRO_0000090116.
FT   ACT_SITE     96     96       Electrophile (By similarity).
FT   ACT_SITE    166    166       Proton acceptor (By similarity).
FT   BINDING      12     12       Substrate (By similarity).
FT   BINDING      14     14       Substrate (By similarity).
FT   MOD_RES      14     14       N6-acetyllysine (By similarity).
FT   MOD_RES      68     68       Nitrated tyrosine.
FT   MOD_RES      80     80       Phosphoserine (By similarity).
FT   MOD_RES     188    188       N6-acetyllysine (By similarity).
FT   MOD_RES     194    194       N6-acetyllysine (By similarity).
FT   MOD_RES     209    209       Nitrated tyrosine.
FT   MOD_RES     238    238       N6-acetyllysine (By similarity).
FT   MUTAGEN     163    163       L->Q: 50% reduced activity.
FT   MUTAGEN     193    193       L->Q: 50% reduced activity.
FT   CONFLICT     74     74       A -> P (in Ref. 1; CAA37420).
FT   CONFLICT    107    107       D -> G (in Ref. 3; BAE39523).
FT   CONFLICT    194    194       K -> R (in Ref. 3; BAB27194).
FT   CONFLICT    195    195       S -> P (in Ref. 3; BAE26832).
FT   CONFLICT    216    216       A -> G (in Ref. 3; BAB27194).
FT   CONFLICT    222    222       A -> Q (in Ref. 3; BAB27194).
FT   CONFLICT    223    225       SQP -> TPA (in Ref. 1; CAA37420).
FT   CONFLICT    227    227       V -> M (in Ref. 3; BAB25634).
SQ   SEQUENCE   249 AA;  26713 MW;  4C69846D0C8AF33A CRC64;
     MAPTRKFFVG GNWKMNGRKK CLGELICTLN AANVPAGTEV VCAPPTAYID FARQKLDPKI
     AVAAQNCYKV TNGAFTGEIS PGMIKDLGAT WVVLGHSERR HVFGESDELI GQKVSHALAE
     GLGVIACIGE KLDEREAGIT EKVVFEQTKV IADNVKDWSK VVLAYEPVWA IGTGKTATPQ
     QAQEVHEKLR GWLKSNVNDG VAQSTRIIYG GSVTGATCKE LASQPDVDGF LVGGASLKPE
     FVDIINAKQ
//
ID   GTR1_MOUSE              Reviewed;         492 AA.
AC   P17809; Q61608;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 3.
DT   08-MAR-2011, entry version 114.
DE   RecName: Full=Solute carrier family 2, facilitated glucose transporter member 1;
DE   AltName: Full=Glucose transporter type 1, erythrocyte/brain;
DE            Short=GLUT-1;
DE            Short=GT1;
GN   Name=Slc2a1; Synonyms=Glut-1, Glut1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=89240694; PubMed=2654938; DOI=10.1073/pnas.86.9.3150;
RA   Kaestner K.H., Christy R.J., McLenithan J.C., Braiterman L.T.,
RA   Cornelius P., Pekala P.H., Lane M.D.;
RT   "Sequence, tissue distribution, and differential expression of mRNA
RT   for a putative insulin-responsive glucose transporter in mouse 3T3-L1
RT   adipocytes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:3150-3154(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90274408; PubMed=2190533; DOI=10.1016/0003-9861(90)90490-P;
RA   Reed B.C., Shade D., Alperovich F., Vang M.;
RT   "3T3-L1 adipocyte glucose transporter (HepG2 class): sequence and
RT   regulation of protein and mRNA expression by insulin, differentiation,
RT   and glucose starvation.";
RL   Arch. Biochem. Biophys. 279:261-274(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-6.
RX   MEDLINE=92250534; PubMed=1339457;
RA   Murakami T., Nishiyama T., Shirotani T., Shinohara Y., Kan M.,
RA   Ishii K., Kanai F., Nakazuru S., Ebina Y.;
RT   "Identification of two enhancer elements in the gene encoding the type
RT   1 glucose transporter from the mouse which are responsive to serum,
RT   growth factor, and oncogenes.";
RL   J. Biol. Chem. 267:9300-9306(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 151-237, AND DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6; TISSUE=Embryo;
RX   MEDLINE=93170163; PubMed=1289053;
RA   Smith D.E., Gridley T.;
RT   "Differential screening of a PCR-generated mouse embryo cDNA library:
RT   glucose transporters are differentially expressed in early
RT   postimplantation mouse embryos.";
RL   Development 116:555-561(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 357-463, AND DEVELOPMENTAL STAGE.
RC   STRAIN=CD-1; TISSUE=Embryo;
RX   MEDLINE=92111400; PubMed=1765007;
RA   Hogan A., Heyner S., Charron M.J., Copeland N.G., Gilbert D.J.,
RA   Jenkins N.A., Thorens B., Schultz G.A.;
RT   "Glucose transporter gene expression in early mouse embryos.";
RL   Development 113:363-372(1991).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-234, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-45 AND ASN-49, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-45 AND ASN-49, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Facilitative glucose transporter. This isoform may be
CC       responsible for constitutive or basal glucose uptake. Has a very
CC       broad substrate specificity; can transport a wide range of aldoses
CC       including both pentoses and hexoses.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity). Melanosome (By similarity). Note=Localizes
CC       primarily at the cell surface (By similarity).
CC   -!- DEVELOPMENTAL STAGE: Levels decline 3-fold between days 7.5 and
CC       12.5 of gestation. At 7.5 dpc, expressed more strongly in
CC       extraembryonic tissues than in the embryo proper. Expressed in
CC       amnion, chorion, and ectoplacental cone. In the yolk sac,
CC       expressed more strongly in the mesoderm layer than the ectoderm.
CC       Expression fairly widespread in the embryo at 8.5 dpc, but by 10.5
CC       dpc, expression is down-regulated and observed in the eye and the
CC       spinal cord.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC       transporter (TC 2.A.1.1) family. Glucose transporter subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M23384; AAA37752.1; -; mRNA.
DR   EMBL; M22998; AAA37707.1; -; mRNA.
DR   EMBL; X69697; CAA49367.1; -; mRNA.
DR   EMBL; S77924; AAB20846.2; -; mRNA.
DR   IPI; IPI00308691; -.
DR   PIR; A44887; A44887.
DR   PIR; S09705; S09705.
DR   RefSeq; NP_035530.2; NM_011400.3.
DR   UniGene; Mm.21002; -.
DR   ProteinModelPortal; P17809; -.
DR   IntAct; P17809; 3.
DR   MINT; MINT-348833; -.
DR   STRING; P17809; -.
DR   PhosphoSite; P17809; -.
DR   PRIDE; P17809; -.
DR   Ensembl; ENSMUST00000030398; ENSMUSP00000030398; ENSMUSG00000028645.
DR   GeneID; 20525; -.
DR   KEGG; mmu:20525; -.
DR   CTD; 20525; -.
DR   MGI; MGI:95755; Slc2a1.
DR   HOGENOM; HBG744444; -.
DR   HOVERGEN; HBG014816; -.
DR   InParanoid; P17809; -.
DR   OrthoDB; EOG4QNMW2; -.
DR   PhylomeDB; P17809; -.
DR   ArrayExpress; P17809; -.
DR   Bgee; P17809; -.
DR   Genevestigator; P17809; -.
DR   GermOnline; ENSMUSG00000028645; Mus musculus.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0055056; F:D-glucose transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0033300; F:dehydroascorbic acid transporter activity; IDA:UniProtKB.
DR   InterPro; IPR002439; Glu_transpt_1.
DR   InterPro; IPR020846; Major_facilitator_SF.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   InterPro; IPR005828; Sub_transporter.
DR   InterPro; IPR003663; Sugar/inositol_transpt.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   PRINTS; PR01190; GLUCTRSPORT1.
DR   PRINTS; PR00171; SUGRTRNSPORT.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
DR   TIGRFAMs; TIGR00879; SP; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR   PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Membrane; Phosphoprotein;
KW   Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    492       Solute carrier family 2, facilitated
FT                                glucose transporter member 1.
FT                                /FTId=PRO_0000050339.
FT   TOPO_DOM      1     12       Cytoplasmic (Potential).
FT   TRANSMEM     13     33       Helical; Name=1; (Potential).
FT   TOPO_DOM     34     66       Extracellular (Potential).
FT   TRANSMEM     67     87       Helical; Name=2; (Potential).
FT   TOPO_DOM     88     95       Cytoplasmic (Potential).
FT   TRANSMEM     96    116       Helical; Name=3; (Potential).
FT   TOPO_DOM    117    126       Extracellular (Potential).
FT   TRANSMEM    127    147       Helical; Name=4; (Potential).
FT   TOPO_DOM    148    155       Cytoplasmic (Potential).
FT   TRANSMEM    156    176       Helical; Name=5; (Potential).
FT   TOPO_DOM    177    185       Extracellular (Potential).
FT   TRANSMEM    186    206       Helical; Name=6; (Potential).
FT   TOPO_DOM    207    271       Cytoplasmic (Potential).
FT   TRANSMEM    272    292       Helical; Name=7; (Potential).
FT   TOPO_DOM    293    307       Extracellular (Potential).
FT   TRANSMEM    308    328       Helical; Name=8; (Potential).
FT   TOPO_DOM    329    337       Cytoplasmic (Potential).
FT   TRANSMEM    338    358       Helical; Name=9; (Potential).
FT   TOPO_DOM    359    371       Extracellular (Potential).
FT   TRANSMEM    372    392       Helical; Name=10; (Potential).
FT   TOPO_DOM    393    401       Cytoplasmic (Potential).
FT   TRANSMEM    402    422       Helical; Name=11; (Potential).
FT   TOPO_DOM    423    429       Extracellular (Potential).
FT   TRANSMEM    430    450       Helical; Name=12; (Potential).
FT   TOPO_DOM    451    492       Cytoplasmic (Potential).
FT   REGION      279    281       Defines substrate specificity (By
FT                                similarity).
FT   MOD_RES     234    234       Phosphothreonine.
FT   MOD_RES     490    490       Phosphoserine (By similarity).
FT   CARBOHYD     45     45       N-linked (GlcNAc...).
FT   CARBOHYD     49     49       N-linked (GlcNAc...).
FT   CONFLICT     52     52       I -> Y (in Ref. 2; AAA37707).
FT   CONFLICT    193    195       IFI -> VFV (in Ref. 1; AAA37752).
FT   CONFLICT    357    360       LLER -> MQEQ (in Ref. 5; AAB20846).
FT   CONFLICT    403    403       A -> R (in Ref. 1; AAA37752).
SQ   SEQUENCE   492 AA;  53935 MW;  42106466B26F3735 CRC64;
     MDPSSKKVTG RLMLAVGGAV LGSLQFGYNT GVINAPQKVI EEFYNQTWNH RIGEPIPSTT
     LTTLWSLSVA IFSVGGMIGS FSVGLFVNRF GRRNSMLMMN LLAFVAAVLM GFSKLGKSFE
     MLILGRFIIG VYCGLTTGFV PMYVGEVSPT ALRGALGTLH QLGIVVGILI AQVFGLDSIM
     GNADLWPLLL SVIFIPALLQ CILLPFCPES PRFLLINRNE ENRAKSVLKK LRGTADVTRD
     LQEMKEEGRQ MMREKKVTIL ELFRSPAYRQ PILIAVVLQL SQQLSGINAV FYYSTSIFEK
     AGVQQPVYAT IGSGIVNTAF TVVSLFVVER AGRRTLHLIG LAGMAGCAVL MTIALALLER
     LPWMSYLSIV AIFGFVAFFE VGPGPIPWFI VAELFSQGPR PAAIAVAGFS NWTSNFIVGM
     CFQYVEQLCG PYVFIIFTVL LVLFFIFTYF KVPETKGRTF DEIASGFRQG GASQSDKTPE
     ELFHPLGADS QV
//
ID   PTPRA_MOUSE             Reviewed;         829 AA.
AC   P18052; Q61808;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   08-MAR-2011, entry version 115.
DE   RecName: Full=Receptor-type tyrosine-protein phosphatase alpha;
DE            Short=Protein-tyrosine phosphatase alpha;
DE            Short=R-PTP-alpha;
DE            EC=3.1.3.48;
DE   AltName: Full=LCA-related phosphatase;
DE   AltName: Full=PTPTY-28;
DE   Flags: Precursor;
GN   Name=Ptpra; Synonyms=Lrp, Ptpa;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6 X DBA/2;
RX   MEDLINE=90280391; PubMed=2162042; DOI=10.1073/pnas.87.12.4444;
RA   Matthews R.J., Cahir E.D., Thomas M.L.;
RT   "Identification of an additional member of the protein-tyrosine-
RT   phosphatase family: evidence for alternative splicing in the tyrosine
RT   phosphatase domain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:4444-4448(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=90349565; PubMed=2166945; DOI=10.1073/pnas.87.16.6112;
RA   Sap J., D'Eustachio P., Givol D., Schlessinger J.;
RT   "Cloning and expression of a widely expressed receptor tyrosine
RT   phosphatase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:6112-6116(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=94010906; PubMed=8406469; DOI=10.1006/geno.1993.1279;
RA   Wong E.C., Mullersman J.E., Thomas M.L.;
RT   "Leukocyte common antigen-related phosphatase (LRP) gene structure:
RT   conservation of the genomic organization of transmembrane protein
RT   tyrosine phosphatases.";
RL   Genomics 17:33-38(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE OF 322-356.
RX   MEDLINE=92272714; PubMed=1590786; DOI=10.1016/S0006-291X(05)80015-4;
RA   den Hertog J., Pals C.E., Jonk L.J., Kruijer W.;
RT   "Differential expression of a novel murine non-receptor protein
RT   tyrosine phosphatase during differentiation of P19 embryonal carcinoma
RT   cells.";
RL   Biochem. Biophys. Res. Commun. 184:1241-1249(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE OF 358-467, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Myeloid leukemia cell;
RX   MEDLINE=92032882; PubMed=1932742;
RA   Yi T., Cleveland J.L., Ihle J.N.;
RT   "Identification of novel protein tyrosine phosphatases of
RT   hematopoietic cells by polymerase chain reaction amplification.";
RL   Blood 78:2222-2228(1991).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 358-467.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=95134232; PubMed=7832766;
RA   Hendriks W., Schepens J., Brugman C., Zeeuwen P., Wieringa B.;
RT   "A novel receptor-type protein tyrosine phosphatase with a single
RT   catalytic domain is specifically expressed in mouse brain.";
RL   Biochem. J. 305:499-504(1995).
RN   [7]
RP   PROTEIN SEQUENCE OF 566-576, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [8]
RP   NUCLEOTIDE SEQUENCE OF 651-756.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=93086603; PubMed=1454056; DOI=10.1007/BF00419663;
RA   Schepens J., Zeeuwen P., Wieringa B., Hendriks W.;
RT   "Identification and typing of members of the protein-tyrosine
RT   phosphatase gene family expressed in mouse brain.";
RL   Mol. Biol. Rep. 16:241-248(1992).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-825, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-825, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180; SER-204 AND
RP   TYR-825, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 202-503.
RX   MEDLINE=96320562; PubMed=8700232; DOI=10.1038/382555a0;
RA   Bilwes A.M., den Hertog J., Hunter T., Noel J.P.;
RT   "Structural basis for inhibition of receptor protein-tyrosine
RT   phosphatase-alpha by dimerization.";
RL   Nature 382:555-559(1996).
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Long;
CC         IsoId=P18052-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short;
CC         IsoId=P18052-2; Sequence=VSP_011880, VSP_005146;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Highest expression in brain
CC       and kidney.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 4 subfamily.
CC   -!- SIMILARITY: Contains 2 tyrosine-protein phosphatase domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; M36033; AAA39448.1; -; mRNA.
DR   EMBL; M36034; AAA39449.2; -; Genomic_DNA.
DR   EMBL; L13607; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z23054; CAA80589.1; -; mRNA.
DR   EMBL; Z23055; CAA80590.1; -; mRNA.
DR   IPI; IPI00108685; -.
DR   IPI; IPI00336550; -.
DR   PIR; A47373; A47373.
DR   UniGene; Mm.224246; -.
DR   PDB; 1P15; X-ray; 2.00 A; A/B=577-829.
DR   PDB; 1YFO; X-ray; 2.25 A; A/B=202-539.
DR   PDBsum; 1P15; -.
DR   PDBsum; 1YFO; -.
DR   ProteinModelPortal; P18052; -.
DR   SMR; P18052; 208-821.
DR   MINT; MINT-129698; -.
DR   STRING; P18052; -.
DR   PhosphoSite; P18052; -.
DR   PRIDE; P18052; -.
DR   Ensembl; ENSMUST00000077303; ENSMUSP00000076533; ENSMUSG00000027303.
DR   Ensembl; ENSMUST00000110266; ENSMUSP00000105895; ENSMUSG00000027303.
DR   UCSC; uc008mjc.1; mouse.
DR   MGI; MGI:97808; Ptpra.
DR   HOGENOM; HBG716815; -.
DR   HOVERGEN; HBG053758; -.
DR   InParanoid; P18052; -.
DR   BRENDA; 3.1.3.48; 244.
DR   NextBio; 296124; -.
DR   ArrayExpress; P18052; -.
DR   Bgee; P18052; -.
DR   CleanEx; MM_PTPRA; -.
DR   Genevestigator; P18052; -.
DR   GermOnline; ENSMUSG00000027303; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IMP:MGI.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   InterPro; IPR016336; Tyr_Pase_rcpt_a/e-type.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PIRSF; PIRSF002006; PTPR_alpha_epsilon; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 2.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing;
KW   Glycoprotein; Hydrolase; Membrane; Phosphoprotein;
KW   Protein phosphatase; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     19       Probable.
FT   CHAIN        20    829       Receptor-type tyrosine-protein
FT                                phosphatase alpha.
FT                                /FTId=PRO_0000025434.
FT   TOPO_DOM     20    142       Extracellular (Potential).
FT   TRANSMEM    143    166       Helical; (Potential).
FT   TOPO_DOM    167    829       Cytoplasmic (Potential).
FT   DOMAIN      232    528       Tyrosine-protein phosphatase 1.
FT   DOMAIN      560    818       Tyrosine-protein phosphatase 2.
FT   REGION      469    475       Substrate binding (By similarity).
FT   ACT_SITE    469    469       Phosphocysteine intermediate (By
FT                                similarity).
FT   ACT_SITE    759    759       Phosphocysteine intermediate (By
FT                                similarity).
FT   BINDING     437    437       Substrate (By similarity).
FT   BINDING     513    513       Substrate (By similarity).
FT   MOD_RES     180    180       Phosphoserine.
FT   MOD_RES     204    204       Phosphoserine.
FT   MOD_RES     825    825       Phosphotyrosine.
FT   CARBOHYD     21     21       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     47     47       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     51     51       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     68     68       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     80     80       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     86     86       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    104    104       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    124    124       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     268    268       F -> Y (in isoform 2).
FT                                /FTId=VSP_011880.
FT   VAR_SEQ     269    303       Missing (in isoform 2).
FT                                /FTId=VSP_005146.
FT   CONFLICT    231    231       I -> L (in Ref. 2).
FT   CONFLICT    326    326       S -> G (in Ref. 4).
FT   CONFLICT    411    411       C -> S (in Ref. 2).
FT   HELIX       214    238
FT   HELIX       249    252
FT   HELIX       254    259
FT   TURN        305    307
FT   TURN        318    321
FT   STRAND      324    330
FT   STRAND      333    340
FT   HELIX       345    347
FT   HELIX       348    357
FT   STRAND      362    365
FT   STRAND      369    371
FT   STRAND      383    389
FT   STRAND      392    401
FT   STRAND      403    413
FT   STRAND      425    432
FT   STRAND      437    439
FT   HELIX       445    457
FT   STRAND      465    468
FT   STRAND      470    473
FT   HELIX       474    491
FT   STRAND      492    495
FT   HELIX       497    504
FT   TURN        505    507
FT   HELIX       515    530
FT   HELIX       579    581
FT   TURN        583    585
FT   STRAND      608    612
FT   STRAND      617    621
FT   STRAND      630    633
FT   STRAND      638    640
FT   HELIX       641    650
FT   STRAND      655    658
FT   STRAND      664    667
FT   STRAND      676    678
FT   STRAND      696    706
FT   STRAND      712    721
FT   STRAND      726    728
FT   STRAND      731    733
FT   HELIX       736    746
FT   TURN        747    751
FT   STRAND      755    763
FT   HELIX       764    782
FT   HELIX       789    795
FT   TURN        805    808
FT   HELIX       809    817
FT   TURN        818    820
SQ   SEQUENCE   829 AA;  93698 MW;  7B1E335D4CCEB09B CRC64;
     MDSWFILVLF GSGLIHVSAN NATTVSPSLG TTRLIKTSTT ELAKEENKTS NSTSSVISLS
     VAPTFSPNLT LEPTYVTTVN SSHSDNGTRR AASTESGGTT ISPNGSWLIE NQFTDAITEP
     WEGNSSTAAT TPETFPPADE TPIIAVMVAL SSLLVIVFII IVLYMLRFKK YKQAGSHSNS
     FRLSNGRTED VEPQSVPLLA RSPSTNRKYP PLPVDKLEEE INRRMADDNK IFREEFNALP
     ACPIQATCEA ASKEENKEKN RYVNILPFLS LAVSKDAVKA LNKTTPLLER RFIGKSNSRG
     CLSDDHSRVH LTPVEGVPDS DYINASFING YQEKNKFIAA QGPKEETVND FWRMIWEQNT
     ATIVMVTNLK ERKECKCAQY WPDQGCWTYG NVRVSVEDVT VLVDYTVRKF CIQQVGDVTN
     RKPQRLITQF HFTSWPDFGV PFTPIGMLKF LKKVKACNPQ YAGAIVVHCS AGVGRTGTFV
     VIDAMLDMMH SERKVDVYGF VSRIRAQRCQ MVQTDMQYVF IYQALLEHYL YGDTELEVTS
     LETHLQKIYN KIPGTSNNGL EEEFKKLTSI KIQNDKMRTG NLPANMKKNR VLQIIPYEFN
     RVIIPVKRGE ENTDYVNASF IDGYRQKDSY IASQGPLLHT IEDFWRMIWE WKSCSIVMLT
     ELEERGQEKC AQYWPSDGLV SYGDITVELK KEEECESYTV RDLLVTNTRE NKSRQIRQFH
     FHGWPEVGIP SDGKGMINII AAVQKQQQQS GNHPITVHCS AGAGRTGTFC ALSTVLERVK
     AEGILDVFQT VKSLRLQRPH MVQTLEQYEF CYKVVQEYID AFSDYANFK
//
ID   CATD_MOUSE              Reviewed;         410 AA.
AC   P18242;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   08-MAR-2011, entry version 109.
DE   RecName: Full=Cathepsin D;
DE            EC=3.4.23.5;
DE   Flags: Precursor;
GN   Name=Ctsd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   MEDLINE=91088345; PubMed=2263503; DOI=10.1093/nar/18.23.7184;
RA   Diedrich J.F., Staskus K.A., Retzel E.F., Haase A.T.;
RT   "Nucleotide sequence of a cDNA encoding mouse cathepsin D.";
RL   Nucleic Acids Res. 18:7184-7184(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90326544; PubMed=2374732; DOI=10.1093/nar/18.13.4008;
RA   Grusby M.J., Mitchell S.C., Glimcher L.H.;
RT   "Molecular cloning of mouse cathepsin D.";
RL   Nucleic Acids Res. 18:4008-4008(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   MEDLINE=94280622; PubMed=8011168; DOI=10.1089/dna.1994.13.419;
RA   Hetman M., Perschl A., Saftig P., von Figura K., Peters C.;
RT   "Mouse cathepsin D gene: molecular organization, characterization of
RT   the promoter, and chromosomal localization.";
RL   DNA Cell Biol. 13:419-427(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-261, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Epidermis;
RX   PubMed=16170054; DOI=10.1074/mcp.M500203-MCP200;
RA   Uematsu R., Furukawa J., Nakagawa H., Shinohara Y., Deguchi K.,
RA   Monde K., Nishimura S.;
RT   "High throughput quantitative glycomics and glycoform-focused
RT   proteomics of murine dermis and epidermis.";
RL   Mol. Cell. Proteomics 4:1977-1989(2005).
CC   -!- FUNCTION: Acid protease active in intracellular protein breakdown.
CC   -!- CATALYTIC ACTIVITY: Specificity similar to, but narrower than,
CC       that of pepsin A. Does not cleave the 4-Gln-|-His-5 bond in B
CC       chain of insulin.
CC   -!- SUBUNIT: Consists of a light chain and a heavy chain (By
CC       similarity).
CC   -!- INTERACTION:
CC       Q07113:Igf2r; NbExp=1; IntAct=EBI-738562, EBI-2891155;
CC   -!- SUBCELLULAR LOCATION: Lysosome. Melanosome (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
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CC   -----------------------------------------------------------------------
DR   EMBL; X53337; CAA37423.1; -; mRNA.
DR   EMBL; X52886; CAA37067.1; -; mRNA.
DR   EMBL; X68378; CAA48453.1; -; Genomic_DNA.
DR   EMBL; X68379; CAA48453.1; JOINED; Genomic_DNA.
DR   EMBL; X68380; CAA48453.1; JOINED; Genomic_DNA.
DR   EMBL; X68381; CAA48453.1; JOINED; Genomic_DNA.
DR   EMBL; X68382; CAA48453.1; JOINED; Genomic_DNA.
DR   EMBL; X68383; CAA48453.1; JOINED; Genomic_DNA.
DR   EMBL; BC054758; AAH54758.1; -; mRNA.
DR   EMBL; BC057931; AAH57931.1; -; mRNA.
DR   IPI; IPI00111013; -.
DR   PIR; I48278; KHMSD.
DR   RefSeq; NP_034113.1; NM_009983.2.
DR   UniGene; Mm.231395; -.
DR   ProteinModelPortal; P18242; -.
DR   SMR; P18242; 21-408.
DR   IntAct; P18242; 3.
DR   STRING; P18242; -.
DR   MEROPS; A01.009; -.
DR   PRIDE; P18242; -.
DR   Ensembl; ENSMUST00000066401; ENSMUSP00000063904; ENSMUSG00000007891.
DR   GeneID; 13033; -.
DR   KEGG; mmu:13033; -.
DR   UCSC; uc009kmv.1; mouse.
DR   CTD; 13033; -.
DR   MGI; MGI:88562; Ctsd.
DR   eggNOG; roNOG09342; -.
DR   GeneTree; ENSGT00600000084042; -.
DR   HOVERGEN; HBG000482; -.
DR   PhylomeDB; P18242; -.
DR   BRENDA; 3.4.23.5; 244.
DR   NextBio; 282908; -.
DR   ArrayExpress; P18242; -.
DR   Bgee; P18242; -.
DR   CleanEx; MM_CTSD; -.
DR   Genevestigator; P18242; -.
DR   GermOnline; ENSMUSG00000007891; Mus musculus.
DR   GO; GO:0005764; C:lysosome; IDA:MGI.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0000045; P:autophagic vacuole assembly; IMP:MGI.
DR   GO; GO:0006508; P:proteolysis; IC:MGI.
DR   InterPro; IPR001461; Peptidase_A1.
DR   InterPro; IPR021109; Peptidase_aspartic.
DR   InterPro; IPR001969; Peptidase_aspartic_AS.
DR   InterPro; IPR009007; Peptidase_aspartic_catalytic.
DR   InterPro; IPR012848; Propep_A1.
DR   Gene3D; G3DSA:2.40.70.10; Pept_Aspartc_cat; 2.
DR   PANTHER; PTHR13683; Peptidase_A1; 1.
DR   Pfam; PF07966; A1_Propeptide; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Pept_Aspartic; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 2.
PE   1: Evidence at protein level;
KW   Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Lysosome;
KW   Protease; Signal; Zymogen.
FT   SIGNAL        1     20       Potential.
FT   PROPEP       21     64       Activation peptide (Potential).
FT                                /FTId=PRO_0000025953.
FT   CHAIN        65    410       Cathepsin D.
FT                                /FTId=PRO_0000025954.
FT   ACT_SITE     97     97       By similarity.
FT   ACT_SITE    293    293       By similarity.
FT   CARBOHYD    134    134       N-linked (GlcNAc...) (By similarity).
FT   CARBOHYD    261    261       N-linked (GlcNAc...) (high mannose).
FT   DISULFID     91    160       By similarity.
FT   DISULFID    110    117       By similarity.
FT   DISULFID    284    288       By similarity.
FT   DISULFID    327    364       By similarity.
SQ   SEQUENCE   410 AA;  44954 MW;  DC4928EC46928BF0 CRC64;
     MKTPGVLLLI LGLLASSSFA IIRIPLRKFT SIRRTMTEVG GSVEDLILKG PITKYSMQSS
     PKTTEPVSEL LKNYLDAQYY GDIGIGTPPQ CFTVVFDTGS SNLWVPSIHC KILDIACWVH
     HKYNSDKSST YVKNGTSFDI HYGSGSLSGY LSQDTVSVPC KSDQSKARGI KVEKQIFGEA
     TKQPGIVFVA AKFDGILGMG YPHISVNNVL PVFDNLMQQK LVDKNIFSFY LNRDPEGQPG
     GELMLGGTDS KYYHGELSYL NVTRKAYWQV HMDQLEVGNE LTLCKGGCEA IVDTGTSLLV
     GPVEEVKELQ KAIGAVPLIQ GEYMIPCEKV SSLPTVYLKL GGKNYELHPD KYILKVSQGG
     KTICLSGFMG MDIPPPSGPL WILGDVFIGS YYTVFDRDNN RVGFANAVVL
//
ID   CTR2_MOUSE              Reviewed;         657 AA.
AC   P18581; Q38RA6; Q3TB99; Q3U3R5;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   08-MAR-2011, entry version 104.
DE   RecName: Full=Low affinity cationic amino acid transporter 2;
DE            Short=CAT-2;
DE            Short=CAT2;
DE   AltName: Full=20.5;
DE   AltName: Full=Solute carrier family 7 member 2;
DE   AltName: Full=T-cell early activation protein;
DE            Short=TEA;
GN   Name=Slc7a2; Synonyms=Atrc2, Tea;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=AKR/J; TISSUE=T-cell;
RX   MEDLINE=90287157; PubMed=1694015;
RA   Macleod C.L., Finley K., Kakuda D., Kozak C.A., Wilkinson M.F.;
RT   "Activated T cells express a novel gene on chromosome 8 that is
RT   closely related to the murine ecotropic retroviral receptor.";
RL   Mol. Cell. Biol. 10:3663-3674(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC   TISSUE=Liver;
RX   MEDLINE=93216705; PubMed=8385111;
RA   Closs E.I., Albritton L.M., Kim J.W., Cunningham J.M.;
RT   "Identification of a low affinity, high capacity transporter of
RT   cationic amino acids in mouse liver.";
RL   J. Biol. Chem. 268:7538-7544(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RX   MEDLINE=94253120; PubMed=8195186;
RA   Kavanaugh M.P., Wang H., Zhang Z., Zhang W., Wu Y.N., Dechant E.,
RA   North R.A., Kabat D.;
RT   "Control of cationic amino acid transport and retroviral receptor
RT   functions in a membrane protein family.";
RL   J. Biol. Chem. 269:15445-15450(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC   STRAIN=Swiss Webster / NIH;
RX   PubMed=16239143; DOI=10.1016/j.cell.2005.08.033;
RA   Prasanth K.V., Prasanth S.G., Xuan Z., Hearn S., Freier S.M.,
RA   Bennett C.F., Zhang M.Q., Spector D.L.;
RT   "Regulating gene expression through RNA nuclear retention.";
RL   Cell 123:249-263(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J, and NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=16670299;
RA   Yeramian A., Martin L., Serrat N., Arpa L., Soler C., Bertran J.,
RA   McLeod C., Palacin M., Modolell M., Lloberas J., Celada A.;
RT   "Arginine transport via cationic amino acid transporter 2 plays a
RT   critical regulatory role in classical or alternative activation of
RT   macrophages.";
RL   J. Immunol. 176:5918-5924(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Low-affinity, high capacity permease involved in the
CC       transport of the cationic amino acids (arginine, lysine and
CC       ornithine). Plays a regulatory role in classical or alternative
CC       activation of macrophages.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Alpha;
CC         IsoId=P18581-1; Sequence=Displayed;
CC       Name=2; Synonyms=Beta;
CC         IsoId=P18581-2; Sequence=VSP_000025;
CC         Note=Affinity of isoform 2 for arginine uptake is 70-fold higher
CC         than for isoform 1;
CC   -!- TISSUE SPECIFICITY: Highest expression in liver and T-cells. Also
CC       expressed in brain and lung.
CC   -!- INDUCTION: By macrophage activation.
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily. Cationic amino acid transporter (CAT) (TC 2.A.3.3)
CC       family.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; M62838; AAA75250.1; -; mRNA.
DR   EMBL; L03290; AAA37372.1; -; mRNA.
DR   EMBL; L11600; AAA37350.1; -; mRNA.
DR   EMBL; L29006; AAA20397.1; -; mRNA.
DR   EMBL; DQ086834; AAY87029.1; -; mRNA.
DR   EMBL; AK154621; BAE32720.1; -; mRNA.
DR   EMBL; AK171369; BAE42415.1; -; mRNA.
DR   EMBL; BC127082; AAI27083.1; -; mRNA.
DR   IPI; IPI00227855; -.
DR   IPI; IPI00652731; -.
DR   PIR; A54011; A54011.
DR   RefSeq; NP_031540.2; NM_007514.3.
DR   UniGene; Mm.4676; -.
DR   ProteinModelPortal; P18581; -.
DR   STRING; P18581; -.
DR   TCDB; 2.A.3.3.2; amino acid-polyamine-organocation (APC) family.
DR   PhosphoSite; P18581; -.
DR   PRIDE; P18581; -.
DR   Ensembl; ENSMUST00000057784; ENSMUSP00000058866; ENSMUSG00000031596.
DR   Ensembl; ENSMUST00000098816; ENSMUSP00000096414; ENSMUSG00000031596.
DR   Ensembl; ENSMUST00000118432; ENSMUSP00000112848; ENSMUSG00000031596.
DR   GeneID; 11988; -.
DR   KEGG; mmu:11988; -.
DR   CTD; 11988; -.
DR   MGI; MGI:99828; Slc7a2.
DR   eggNOG; roNOG10464; -.
DR   HOGENOM; HBG727793; -.
DR   HOVERGEN; HBG000280; -.
DR   InParanoid; P18581; -.
DR   OrthoDB; EOG46143S; -.
DR   NextBio; 280145; -.
DR   ArrayExpress; P18581; -.
DR   Bgee; P18581; -.
DR   Genevestigator; P18581; -.
DR   GermOnline; ENSMUSG00000031596; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IDA:MGI.
DR   GO; GO:0005289; F:high affinity arginine transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0015189; F:L-lysine transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0000064; F:L-ornithine transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0042116; P:macrophage activation; IMP:MGI.
DR   GO; GO:0006809; P:nitric oxide biosynthetic process; IMP:MGI.
DR   GO; GO:0002537; P:nitric oxide production involved in inflammatory response; IMP:MGI.
DR   GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
DR   GO; GO:0043030; P:regulation of macrophage activation; IMP:UniProtKB.
DR   InterPro; IPR004841; AA-permease_dom.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   InterPro; IPR015606; Cat-AATrans.
DR   InterPro; IPR004755; Cat_AA_permease.
DR   PANTHER; PTHR11785; AA/rel_permease1; 1.
DR   PANTHER; PTHR11785:SF53; Cat-AATrans; 1.
DR   Pfam; PF00324; AA_permease; 1.
DR   PIRSF; PIRSF006060; AA_transporter; 1.
DR   TIGRFAMs; TIGR00906; 2A0303; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Amino-acid transport; Glycoprotein; Membrane;
KW   Phosphoprotein; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    657       Low affinity cationic amino acid
FT                                transporter 2.
FT                                /FTId=PRO_0000054265.
FT   TOPO_DOM      1     37       Cytoplasmic (Potential).
FT   TRANSMEM     38     59       Helical; (Potential).
FT   TOPO_DOM     60     63       Extracellular (Potential).
FT   TRANSMEM     64     84       Helical; (Potential).
FT   TOPO_DOM     85    104       Cytoplasmic (Potential).
FT   TRANSMEM    105    125       Helical; (Potential).
FT   TOPO_DOM    126    163       Extracellular (Potential).
FT   TRANSMEM    164    184       Helical; (Potential).
FT   TOPO_DOM    185    192       Cytoplasmic (Potential).
FT   TRANSMEM    193    213       Helical; (Potential).
FT   TOPO_DOM    214    248       Extracellular (Potential).
FT   TRANSMEM    249    269       Helical; (Potential).
FT   TOPO_DOM    270    289       Cytoplasmic (Potential).
FT   TRANSMEM    290    309       Helical; (Potential).
FT   TOPO_DOM    310    339       Extracellular (Potential).
FT   TRANSMEM    340    360       Helical; (Potential).
FT   TOPO_DOM    361    385       Cytoplasmic (Potential).
FT   TRANSMEM    386    406       Helical; (Potential).
FT   TOPO_DOM    407    409       Extracellular (Potential).
FT   TRANSMEM    410    430       Helical; (Potential).
FT   TOPO_DOM    431    489       Cytoplasmic (Potential).
FT   TRANSMEM    490    510       Helical; (Potential).
FT   TOPO_DOM    511    523       Extracellular (Potential).
FT   TRANSMEM    524    548       Helical; (Potential).
FT   TOPO_DOM    549    556       Cytoplasmic (Potential).
FT   TRANSMEM    557    577       Helical; (Potential).
FT   TOPO_DOM    578    581       Extracellular (Potential).
FT   TRANSMEM    582    602       Helical; (Potential).
FT   TOPO_DOM    603    657       Cytoplasmic (Potential).
FT   MOD_RES     645    645       Phosphoserine.
FT   CARBOHYD    157    157       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    227    227       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    239    239       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     357    397       MFPLPRILFAMARDGLLFRFLARVSKRQSPVAATMTAGVIS
FT                                -> IFPMPRVIYAMAEDGLLFKCLAQINSKTKTPVIATLSS
FT                                GAVA (in isoform 2).
FT                                /FTId=VSP_000025.
FT   CONFLICT    142    142       L -> P (in Ref. 5; BAE32720).
FT   CONFLICT    242    242       S -> R (in Ref. 5; BAE32720).
FT   CONFLICT    280    280       E -> K (in Ref. 5; BAE42415).
FT   CONFLICT    335    335       G -> S (in Ref. 5; BAE32720).
FT   CONFLICT    342    342       A -> S (in Ref. 5; BAE32720).
FT   CONFLICT    430    430       I -> M (in Ref. 2; AAA37372).
FT   CONFLICT    440    440       E -> D (in Ref. 5; BAE32720).
FT   CONFLICT    537    537       A -> V (in Ref. 5; BAE32720).
FT   CONFLICT    622    622       E -> D (in Ref. 5; BAE32720).
FT   CONFLICT    626    626       V -> A (in Ref. 5; BAE32720).
FT   CONFLICT    633    633       V -> A (in Ref. 5; BAE32720).
SQ   SEQUENCE   657 AA;  71866 MW;  3B0995C4F41EC2B9 CRC64;
     MIPCRAVLTF ARCLIRRKIV TLDSLEDSKL CRCLTTVDLI ALGVGSTLGA GVYVLAGEVA
     KADSGPSIVV SFLIAALASV MAGLCYAEFG ARVPKTGSAY LYTYVTVGEL WAFITGWNLI
     LSYVIGTSSV ARAWSGTFDE LLNKQIGQFF KTYFKMNYTG LAEYPDFFAV CLVLLLAGLL
     SFGVKESAWV NKFFTAINIL VLLFVMVAGF VKGNVANWKI SEEFLKNISA SAREPPSENG
     TSIYGAGGFM PYGFTGTLAG AATCFYAFVG FDCIATTGEE VRNPQKAIPI GIVTSLLVCF
     MAYFGVSAAL TLMMPYYLLD EKSPLPVAFE YVRWGPAKYV VAAGSLCALS TSLLGSMFPL
     PRILFAMARD GLLFRFLARV SKRQSPVAAT MTAGVISAVM AFLFDLKALV DMMSIGTLMA
     YSLVAACVLI LRYQPGLCYE QPKYTPEKET LESCTNATLK SESQVTMLQG QGFSLRTLFS
     PSALPTRQSA SLVSFLVGFL AFLILGLSIL TTYGVQAIAR LEAWSLALLA LFLVLCAAVI
     LTIWRQPQNQ QKVAFMVPFL PFLPAFSILV NIYLMVQLSA DTWIRFSIWM ALGFLIYFAY
     GIRHSLEGNP RDEEDDEDAF SENINVATEE KSVMQANDHH QRNLSLPFIL HEKTSEC
//
ID   HMGN1_MOUSE             Reviewed;          96 AA.
AC   P18608; Q5HZY9;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Non-histone chromosomal protein HMG-14;
DE   AltName: Full=High mobility group nucleosome-binding domain-containing protein 1;
GN   Name=Hmgn1; Synonyms=Hmg-14, Hmg14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=90384862; PubMed=2402471; DOI=10.1093/nar/18.17.5311;
RA   Landsman D., Bustin M.;
RT   "Mouse non-histone chromosomal protein HMG-14 cDNA sequence.";
RL   Nucleic Acids Res. 18:5311-5311(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, and Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-19.
RX   MEDLINE=88137601; PubMed=3342876; DOI=10.1016/0014-5793(88)80581-7;
RA   Vartiainen E., Palvimo J., Mahonen A., Linnala-Kankkunen A.,
RA   Maeenpaeae P.H.;
RT   "Selective decrease in low-Mr HMG proteins HMG I and HMG Y during
RT   differentiation of mouse teratocarcinoma cells.";
RL   FEBS Lett. 228:45-48(1988).
RN   [4]
RP   PHOSPHORYLATION AT SER-7.
RX   PubMed=7925294;
RA   Barratt M.J., Hazzalin C.A., Zhelev N., Mahadevan L.C.;
RT   "A mitogen- and anisomycin-stimulated kinase phosphorylates HMG-14 in
RT   its basic amino-terminal domain in vivo and on isolated
RT   mononucleosomes.";
RL   EMBO J. 13:4524-4535(1994).
RN   [5]
RP   FUNCTION, AND PHOSPHORYLATION AT SER-7; SER-20 AND SER-24.
RX   PubMed=15327773; DOI=10.1016/j.molcel.2004.08.006;
RA   Lim J.-H., Catez F., Birger Y., West K.L., Prymakowska-Bosak M.,
RA   Postnikov Y.V., Bustin M.;
RT   "Chromosomal protein HMGN1 modulates histone H3 phosphorylation.";
RL   Mol. Cell 15:573-584(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-80; SER-84; SER-87 AND
RP   SER-95, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-87, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Binds to the inner side of the nucleosomal DNA thus
CC       altering the interaction between the DNA and the histone octamer.
CC       May be involved in the process which maintains transcribable genes
CC       in an unique chromatin conformation. Inhibits the phosphorylation
CC       of nucleosomal histones H3 and H2A by RPS6KA5/MSK1 and
CC       RPS6KA3/RSK2.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm (By similarity).
CC       Note=Cytoplasmic enrichment upon phosphorylation (By similarity).
CC   -!- PTM: Phosphorylation favors cytoplasmic localization (By
CC       similarity). Phosphorylation on Ser-20 and Ser-24 weakens binding
CC       to nucleosomes and increases the rate of H3 phosphorylation.
CC   -!- SIMILARITY: Belongs to the HMGN family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X53476; CAA37569.1; -; mRNA.
DR   EMBL; BC083138; AAH83138.1; -; mRNA.
DR   EMBL; BC088834; AAH88834.1; -; mRNA.
DR   IPI; IPI00338745; -.
DR   PIR; S11219; S11219.
DR   RefSeq; NP_032277.3; NM_008251.3.
DR   RefSeq; XP_001472107.1; XM_001472057.2.
DR   UniGene; Mm.2756; -.
DR   ProteinModelPortal; P18608; -.
DR   STRING; P18608; -.
DR   PhosphoSite; P18608; -.
DR   PRIDE; P18608; -.
DR   Ensembl; ENSMUST00000050884; ENSMUSP00000061012; ENSMUSG00000040681.
DR   GeneID; 100044391; -.
DR   GeneID; 15312; -.
DR   KEGG; mmu:100044391; -.
DR   KEGG; mmu:15312; -.
DR   UCSC; uc008aco.1; mouse.
DR   CTD; 15312; -.
DR   MGI; MGI:96120; Hmgn1.
DR   eggNOG; maNOG21326; -.
DR   GeneTree; ENSGT00530000063649; -.
DR   HOVERGEN; HBG073479; -.
DR   InParanoid; P18608; -.
DR   OMA; AKDKSEN; -.
DR   NextBio; 457890; -.
DR   ArrayExpress; P18608; -.
DR   Bgee; P18608; -.
DR   CleanEx; MM_HMGN1; -.
DR   Genevestigator; P18608; -.
DR   GermOnline; ENSMUSG00000040681; Mus musculus.
DR   GO; GO:0000785; C:chromatin; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006325; P:chromatin organization; IMP:MGI.
DR   GO; GO:0048597; P:post-embryonic camera-type eye morphogenesis; IMP:MGI.
DR   GO; GO:0000720; P:pyrimidine dimer repair by nucleotide-excision repair; IMP:MGI.
DR   GO; GO:0050678; P:regulation of epithelial cell proliferation; IMP:MGI.
DR   GO; GO:0010224; P:response to UV-B; IMP:MGI.
DR   GO; GO:0010225; P:response to UV-C; IDA:MGI.
DR   GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IMP:MGI.
DR   InterPro; IPR000079; HMG14/HMG17.
DR   PANTHER; PTHR23087; HMG_14_17; 1.
DR   Pfam; PF01101; HMG14_17; 1.
DR   PRINTS; PR00925; NONHISHMG17.
DR   SMART; SM00527; HMG17; 1.
DR   PROSITE; PS00355; HMG14_17; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; DNA-binding;
KW   Nucleus; Phosphoprotein.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2     96       Non-histone chromosomal protein HMG-14.
FT                                /FTId=PRO_0000206692.
FT   MOD_RES       7      7       Phosphoserine; by RPS6KA5.
FT   MOD_RES      13     13       N6-acetyllysine (By similarity).
FT   MOD_RES      20     20       Phosphoserine; by RPS6KA5.
FT   MOD_RES      24     24       Phosphoserine; by RPS6KA5.
FT   MOD_RES      70     70       Phosphothreonine (By similarity).
FT   MOD_RES      80     80       Phosphothreonine.
FT   MOD_RES      84     84       Phosphoserine.
FT   MOD_RES      87     87       Phosphoserine.
FT   MOD_RES      95     95       Phosphoserine.
SQ   SEQUENCE   96 AA;  10152 MW;  65C4C09DE0973786 CRC64;
     MPKRKVSADG AAKAEPKRRS ARLSAKPAPA KVDAKPKKAA GKDKASDKKV QIKGKRGAKG
     KQADVADQQT TELPAENGET ENQSPASEEE KEAKSD
//
ID   KS6A1_MOUSE             Reviewed;         724 AA.
AC   P18653;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   08-FEB-2011, entry version 100.
DE   RecName: Full=Ribosomal protein S6 kinase alpha-1;
DE            Short=S6K-alpha-1;
DE            EC=2.7.11.1;
DE   AltName: Full=90 kDa ribosomal protein S6 kinase 1;
DE            Short=p90-RSK 1;
DE            Short=p90RSK1;
DE            Short=p90S6K;
DE   AltName: Full=MAP kinase-activated protein kinase 1a;
DE            Short=MAPK-activated protein kinase 1a;
DE            Short=MAPKAP kinase 1a;
DE            Short=MAPKAPK-1a;
DE   AltName: Full=Ribosomal S6 kinase 1;
DE            Short=RSK-1;
GN   Name=Rps6ka1; Synonyms=Mapkapk1a, Rsk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=89384612; PubMed=2779569;
RA   Alcorta D.A., Crews C.M., Sweet L.J., Bankston L., Jones S.W.,
RA   Erikson R.L.;
RT   "Sequence and expression of chicken and mouse rsk: homologs of Xenopus
RT   laevis ribosomal S6 kinase.";
RL   Mol. Cell. Biol. 9:3850-3859(1989).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-721, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-369, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-369, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Serine/threonine kinase that may play a role in
CC       mediating the growth-factor and stress induced activation of the
CC       transcription factor CREB (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activated by multiple phosphorylations on
CC       threonine and serine residues (By similarity).
CC   -!- SUBUNIT: Forms a complex with either ERK1 or ERK2 in quiescent
CC       cells. Transiently dissociates following mitogenic stimulation (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Intestine, thymus, and lung.
CC   -!- PTM: Autophosphorylated on Ser-369, as part of the activation
CC       process (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. S6 kinase subfamily.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 2 protein kinase domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M28489; AAA50300.1; -; mRNA.
DR   IPI; IPI00114332; -.
DR   PIR; B32571; B32571.
DR   UniGene; Mm.301827; -.
DR   ProteinModelPortal; P18653; -.
DR   SMR; P18653; 53-374, 404-698.
DR   IntAct; P18653; 1.
DR   MINT; MINT-1486951; -.
DR   STRING; P18653; -.
DR   PhosphoSite; P18653; -.
DR   PRIDE; P18653; -.
DR   Ensembl; ENSMUST00000003741; ENSMUSP00000003741; ENSMUSG00000003644.
DR   UCSC; uc008vdk.1; mouse.
DR   MGI; MGI:104558; Rps6ka1.
DR   GeneTree; ENSGT00590000082790; -.
DR   HOVERGEN; HBG108317; -.
DR   PhylomeDB; P18653; -.
DR   BRENDA; 2.7.11.1; 244.
DR   ArrayExpress; P18653; -.
DR   Bgee; P18653; -.
DR   CleanEx; MM_RPS6KA1; -.
DR   Genevestigator; P18653; -.
DR   GermOnline; ENSMUSG00000003644; Mus musculus.
DR   GO; GO:0005819; C:spindle; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007243; P:intracellular protein kinase cascade; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR016239; Ribosomal_S6_kinase_II.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 2.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   PIRSF; PIRSF000606; Ribsml_S6_kin_2; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF56112; Kinase_like; 2.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; Repeat;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    724       Ribosomal protein S6 kinase alpha-1.
FT                                /FTId=PRO_0000086199.
FT   DOMAIN       62    310       Protein kinase 1.
FT   DOMAIN      311    380       AGC-kinase C-terminal.
FT   DOMAIN      407    664       Protein kinase 2.
FT   NP_BIND      68     76       ATP (By similarity).
FT   NP_BIND     413    421       ATP (By similarity).
FT   ACT_SITE    187    187       Proton acceptor (By similarity).
FT   ACT_SITE    524    524       Proton acceptor (By similarity).
FT   BINDING      94     94       ATP (By similarity).
FT   BINDING     436    436       ATP (By similarity).
FT   MOD_RES      25     25       Phosphothreonine (By similarity).
FT   MOD_RES      26     26       Phosphoserine (By similarity).
FT   MOD_RES      54     54       Phosphoserine (By similarity).
FT   MOD_RES      72     72       Phosphoserine (By similarity).
FT   MOD_RES     204    204       Phosphothreonine (By similarity).
FT   MOD_RES     209    209       Phosphoserine (By similarity).
FT   MOD_RES     220    220       Phosphotyrosine (By similarity).
FT   MOD_RES     221    221       Phosphoserine (By similarity).
FT   MOD_RES     225    225       Phosphothreonine (By similarity).
FT   MOD_RES     296    296       Phosphoserine (By similarity).
FT   MOD_RES     348    348       Phosphothreonine (By similarity).
FT   MOD_RES     352    352       Phosphoserine (By similarity).
FT   MOD_RES     358    358       Phosphoserine (By similarity).
FT   MOD_RES     369    369       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     562    562       Phosphothreonine (By similarity).
FT   MOD_RES     565    565       Phosphotyrosine (By similarity).
FT   MOD_RES     624    624       Phosphothreonine (By similarity).
FT   MOD_RES     626    626       Phosphoserine (By similarity).
FT   MOD_RES     673    673       Phosphoserine (By similarity).
FT   MOD_RES     721    721       Phosphoserine.
SQ   SEQUENCE   724 AA;  81595 MW;  A5D8E5E5FDBCE4BF CRC64;
     MPLAQLKEPW PLMELVPLDP ENGQTSGEEA GLQPSKDEAI LKEISITHHV KAGSEKADPS
     QFELLKVLGQ GSFGKVFLVR KVTRPDSGHL YAMKVLKKAT LKVRDRVRTK MERDILADVN
     HPFVVKLHYA FQTEGKLYLI LDFLRGGDLF TRLSKEVMFT EEDVKFYLAE LALGLDHLHS
     LGIIYRDLKP ENILLDEEGH IKLTDFGLSK EAIDHEKKAY SFCGTVEYMA PEVVNRQGHT
     HSADWWSYGV LMGKDRKETM TLILKAKLGM PQFLSTEAQS LLRALFKRNP ANRLGSGPDG
     AEEIKRHIFY STIDWNKLYR REIKPPFKPA VAQPDDTFYF DTEFTSRTPR DSPGIPPSAG
     AHQLFRGFSF VATGLMEDDG KPRTTQAPLH SVVQQLHGKN LVFSDGYVVK ETIGVGSYSV
     CKRCVHKATN MEYAVKVIDK SKRDPSEEIE ILLRYGQHPN IITLKDVYDD GKHVYLVTEL
     MRGGELLDKI LRQKFFSERE ASFVLHTISK TVEYLHSQGV VHRDLKPSNI LYVDESGNPE
     CLRICDFGFA KQLRAENGLL MTPCYTANFV APEVLKRQGY DEGCDIWSLG ILLYTMLAGY
     TPFANGPSDT PEEILTRIGS GKFTLSGGNW NTVSETAKDL VSKMLHVDPH QRLTAKQVLQ
     HPWITQKDKL PQSQLSHQDL QLVKGAMAAT YSALNSSKPT PQLKPIESSI LAQRRVRKLP
     STTL
//
ID   KS6A3_MOUSE             Reviewed;         740 AA.
AC   P18654; B1AXN4; Q03140; Q8K3J8;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   25-MAR-2003, sequence version 2.
DT   08-MAR-2011, entry version 116.
DE   RecName: Full=Ribosomal protein S6 kinase alpha-3;
DE            Short=S6K-alpha-3;
DE            EC=2.7.11.1;
DE   AltName: Full=90 kDa ribosomal protein S6 kinase 3;
DE            Short=p90-RSK 3;
DE            Short=p90RSK3;
DE   AltName: Full=MAP kinase-activated protein kinase 1b;
DE            Short=MAPK-activated protein kinase 1b;
DE            Short=MAPKAP kinase 1b;
DE            Short=MAPKAPK-1b;
DE   AltName: Full=Ribosomal S6 kinase 2;
DE            Short=RSK-2;
DE   AltName: Full=pp90RSK2;
GN   Name=Rps6ka3; Synonyms=Mapkapk1b, Rps6ka-rs1, Rsk2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=22140319; PubMed=12016217; DOI=10.1074/jbc.M202663200;
RA   Chrestensen C.A., Sturgill T.W.;
RT   "Characterization of the p90 ribosomal S6 kinase 2 carboxyl-terminal
RT   domain as a protein kinase.";
RL   J. Biol. Chem. 277:27733-27741(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 108-740.
RX   MEDLINE=89384612; PubMed=2779569;
RA   Alcorta D.A., Crews C.M., Sweet L.J., Bankston L., Jones S.W.,
RA   Erikson R.L.;
RT   "Sequence and expression of chicken and mouse rsk: homologs of Xenopus
RT   laevis ribosomal S6 kinase.";
RL   Mol. Cell. Biol. 9:3850-3859(1989).
RN   [4]
RP   PHOSPHORYLATION AT SER-227; SER-369 AND SER-386.
RX   PubMed=10480933; DOI=10.1074/jbc.274.38.27168;
RA   Jensen C.J., Buch M.-B., Krag T.O., Hemmings B.A., Gammeltoft S.,
RA   Froedin M.;
RT   "90-kDa ribosomal S6 kinase is phosphorylated and activated by 3-
RT   phosphoinositide-dependent protein kinase-1.";
RL   J. Biol. Chem. 274:27168-27176(1999).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-365 AND SER-369, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Serine/threonine kinase that may play a role in
CC       mediating the growth-factor and stress induced activation of the
CC       transcription factor CREB (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activated by multiple phosphorylations on
CC       threonine and serine residues (By similarity).
CC   -!- SUBUNIT: Forms a complex with either ERK1 or ERK2 in quiescent
CC       cells. Transiently dissociates following mitogenic stimulation.
CC       Interacts with NFATC4 (By similarity).
CC   -!- TISSUE SPECIFICITY: Intestine, thymus, lung, heart and brain.
CC   -!- PTM: Ser-227 phosphorylation by PDPK1 promotes Ser-386
CC       phosphorylation and leads to basal activation. Full activation by
CC       growth factors requires additional phosphorylation on Ser-369 by
CC       ERK.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. S6 kinase subfamily.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 2 protein kinase domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY083469; AAM00022.1; -; mRNA.
DR   EMBL; AL808146; CAM25836.1; -; Genomic_DNA.
DR   IPI; IPI00114333; -.
DR   PIR; C32571; C32571.
DR   PIR; S30504; S30504.
DR   RefSeq; NP_683747.1; NM_148945.1.
DR   UniGene; Mm.328476; -.
DR   PDB; 2QR7; X-ray; 2.00 A; A=399-740.
DR   PDB; 2QR8; X-ray; 2.00 A; A=399-740.
DR   PDB; 3G51; X-ray; 1.80 A; A=44-367.
DR   PDBsum; 2QR7; -.
DR   PDBsum; 2QR8; -.
DR   PDBsum; 3G51; -.
DR   ProteinModelPortal; P18654; -.
DR   SMR; P18654; 47-390, 417-714.
DR   MINT; MINT-1486771; -.
DR   STRING; P18654; -.
DR   PhosphoSite; P18654; -.
DR   PRIDE; P18654; -.
DR   Ensembl; ENSMUST00000033671; ENSMUSP00000033671; ENSMUSG00000031309.
DR   GeneID; 110651; -.
DR   KEGG; mmu:110651; -.
DR   UCSC; uc009usj.1; mouse.
DR   CTD; 110651; -.
DR   MGI; MGI:104557; Rps6ka3.
DR   eggNOG; roNOG08048; -.
DR   GeneTree; ENSGT00590000082790; -.
DR   HOVERGEN; HBG108317; -.
DR   InParanoid; P18654; -.
DR   OMA; RQFELRK; -.
DR   OrthoDB; EOG402WRK; -.
DR   PhylomeDB; P18654; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 364399; -.
DR   ArrayExpress; P18654; -.
DR   Bgee; P18654; -.
DR   CleanEx; MM_RPS6KA3; -.
DR   Genevestigator; P18654; -.
DR   GermOnline; ENSMUSG00000031309; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
DR   GO; GO:0007243; P:intracellular protein kinase cascade; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR016239; Ribosomal_S6_kinase_II.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 2.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   PIRSF; PIRSF000606; Ribsml_S6_kin_2; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF56112; Kinase_like; 2.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Repeat; Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    740       Ribosomal protein S6 kinase alpha-3.
FT                                /FTId=PRO_0000086204.
FT   DOMAIN       68    327       Protein kinase 1.
FT   DOMAIN      328    397       AGC-kinase C-terminal.
FT   DOMAIN      422    679       Protein kinase 2.
FT   NP_BIND      74     82       ATP (By similarity).
FT   NP_BIND     428    436       ATP (By similarity).
FT   ACT_SITE    193    193       Proton acceptor (By similarity).
FT   ACT_SITE    539    539       Proton acceptor (By similarity).
FT   BINDING     100    100       ATP (By similarity).
FT   BINDING     451    451       ATP (By similarity).
FT   MOD_RES      17     17       Phosphoserine (By similarity).
FT   MOD_RES      19     19       Phosphoserine (By similarity).
FT   MOD_RES     226    226       Phosphotyrosine (By similarity).
FT   MOD_RES     227    227       Phosphoserine; by PDPK1.
FT   MOD_RES     231    231       Phosphothreonine (By similarity).
FT   MOD_RES     365    365       Phosphothreonine.
FT   MOD_RES     369    369       Phosphoserine.
FT   MOD_RES     375    375       Phosphoserine (By similarity).
FT   MOD_RES     386    386       Phosphoserine.
FT   MOD_RES     391    391       Phosphothreonine (By similarity).
FT   MOD_RES     415    415       Phosphoserine (By similarity).
FT   MOD_RES     556    556       Phosphoserine (By similarity).
FT   MOD_RES     577    577       Phosphothreonine (By similarity).
FT   MOD_RES     715    715       Phosphoserine (By similarity).
FT   MOD_RES     737    737       Phosphoserine (By similarity).
FT   HELIX       418    421
FT   STRAND      422    430
FT   STRAND      432    441
FT   TURN        442    444
FT   STRAND      447    454
FT   TURN        455    457
FT   HELIX       461    470
FT   STRAND      479    484
FT   STRAND      486    493
FT   HELIX       501    506
FT   HELIX       513    532
FT   HELIX       542    544
FT   STRAND      545    551
FT   HELIX       554    556
FT   STRAND      557    559
FT   HELIX       587    613
FT   HELIX       626    635
FT   TURN        643    647
FT   HELIX       650    659
FT   TURN        664    666
FT   HELIX       670    673
FT   HELIX       677    680
FT   HELIX       682    684
FT   HELIX       696    710
FT   TURN        711    713
SQ   SEQUENCE   740 AA;  83694 MW;  0CD54E5918567007 CRC64;
     MPLAQLADPW QKMAVESPSD SAENGQQIMD EPMGEEEINP QTEEGSIKEI AITHHVKEGH
     EKADPSQFEL LKVLGQGSFG KVFLVKKISG SDARQLYAMK VLKKATLKVR DRVRTKMERD
     ILVEVNHPFI VKLHYAFQTE GKLYLILDFL RGGDLFTRLS KEVMFTEEDV KFYLAELALA
     LDHLHSLGII YRDLKPENIL LDEEGHIKLT DFGLSKESID HEKKAYSFCG TVEYMAPEVV
     NRRGHTQSAD WWSFGVLMFE MLTGTLPFQG KDRKETMTMI LKAKLGMPQF LSPEAQSLLR
     MLFKRNPANR LGAGPDGVEE IKRHSFFSTI DWNKLYRREI HPPFKPATGR PEDTFYFDPE
     FTAKTPKDSP GIPPSANAHQ LFRGFSFVAI TSDDESQAMQ TVGVHSIVQQ LHRNSIQFTD
     GYEVKEDIGV GSYSVCKRCI HKATNMEFAV KIIDKSKRDP TEEIEILLRY GQHPNIITLK
     DVYDDGKYVY VVTELMKGGE LLDKILRQKF FSEREASAVL FTITKTVEYL HAQGVVHRDL
     KPSNILYVDE SGNPESIRIC DFGFAKQLRA ENGLLMTPCY TANFVAPEVL KRQGYDAACD
     IWSLGVLLYT MLTGYTPFAN GPDDTPEEIL ARIGSGKFSL SGGYWNSVSD TAKDLVSKML
     HVDPHQRLTA ALVLRHPWIV HWDQLPQYQL NRQDAPHLVK GAMAATYSAL NRNQSPVLEP
     VGRSTLAQRR GIKKITSTAL
//
ID   COF1_MOUSE              Reviewed;         166 AA.
AC   P18760;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 114.
DE   RecName: Full=Cofilin-1;
DE   AltName: Full=Cofilin, non-muscle isoform;
GN   Name=Cfl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster;
RX   MEDLINE=90272419; PubMed=2349104; DOI=10.1093/nar/18.10.3053;
RA   Moriyama K., Matsumoto S., Nishida E., Sakai H., Yahara I.;
RT   "Nucleotide sequence of mouse cofilin cDNA.";
RL   Nucleic Acids Res. 18:3053-3053(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-13 AND 153-166, CLEAVAGE OF INITIATOR
RP   METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Liver;
RA   Bienvenut W.V.;
RL   Submitted (JUL-2005) to UniProtKB.
RN   [4]
RP   PROTEIN SEQUENCE OF 54-73 AND 96-112, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION AT SER-3,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-68 AND TYR-140, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-8, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Controls reversibly actin polymerization and
CC       depolymerization in a pH-sensitive manner. It has the ability to
CC       bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the
CC       major component of intranuclear and cytoplasmic actin rods.
CC   -!- SUBCELLULAR LOCATION: Nucleus matrix. Cytoplasm, cytoskeleton.
CC       Note=Almost completely in nucleus in cells exposed to heat shock
CC       or 10% dimethyl sulfoxide.
CC   -!- TISSUE SPECIFICITY: Widely distributed in various tissues.
CC   -!- PTM: Phosphorylated on Ser-3 in resting cells (By similarity).
CC   -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC   -!- SIMILARITY: Contains 1 ADF-H domain.
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DR   EMBL; D00472; BAA00364.1; -; mRNA.
DR   EMBL; BC046225; AAH46225.1; -; mRNA.
DR   EMBL; BC058726; AAH58726.1; -; mRNA.
DR   IPI; IPI00890117; -.
DR   PIR; S12584; S12584.
DR   RefSeq; NP_031713.1; NM_007687.5.
DR   UniGene; Mm.329655; -.
DR   ProteinModelPortal; P18760; -.
DR   SMR; P18760; 1-166.
DR   STRING; P18760; -.
DR   PhosphoSite; P18760; -.
DR   SWISS-2DPAGE; P18760; -.
DR   REPRODUCTION-2DPAGE; P18760; -.
DR   PRIDE; P18760; -.
DR   Ensembl; ENSMUST00000116560; ENSMUSP00000112259; ENSMUSG00000056201.
DR   GeneID; 12631; -.
DR   KEGG; mmu:12631; -.
DR   UCSC; uc008gdq.1; mouse.
DR   CTD; 12631; -.
DR   MGI; MGI:101757; Cfl1.
DR   eggNOG; roNOG07842; -.
DR   HOVERGEN; HBG000381; -.
DR   OrthoDB; EOG4WSWBP; -.
DR   NextBio; 281816; -.
DR   ArrayExpress; P18760; -.
DR   Bgee; P18760; -.
DR   CleanEx; MM_CFL1; -.
DR   Genevestigator; P18760; -.
DR   GermOnline; ENSMUSG00000056201; Mus musculus.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005576; C:extracellular region; EXP:Reactome.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0007015; P:actin filament organization; IMP:MGI.
DR   GO; GO:0000910; P:cytokinesis; IMP:MGI.
DR   GO; GO:0030010; P:establishment of cell polarity; IMP:MGI.
DR   GO; GO:0001755; P:neural crest cell migration; IMP:MGI.
DR   GO; GO:0001842; P:neural fold formation; IMP:MGI.
DR   GO; GO:0030836; P:positive regulation of actin filament depolymerization; IMP:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR   GO; GO:0043200; P:response to amino acid stimulus; IDA:MGI.
DR   InterPro; IPR002108; Actin-bd_cofilin/tropomyosin.
DR   InterPro; IPR017904; ADF/Cofilin/Destrin.
DR   Pfam; PF00241; Cofilin_ADF; 1.
DR   PRINTS; PR00006; COFILIN.
DR   SMART; SM00102; ADF; 1.
DR   PROSITE; PS51263; ADF_H; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Nucleus; Phosphoprotein.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    166       Cofilin-1.
FT                                /FTId=PRO_0000214900.
FT   DOMAIN        4    153       ADF-H.
FT   MOTIF        30     34       Nuclear localization signal (Potential).
FT   MOD_RES       2      2       N-acetylalanine.
FT   MOD_RES       3      3       Phosphoserine.
FT   MOD_RES       8      8       Phosphoserine.
FT   MOD_RES      13     13       N6-acetyllysine (By similarity).
FT   MOD_RES      19     19       N6-acetyllysine (By similarity).
FT   MOD_RES      25     25       Phosphothreonine (By similarity).
FT   MOD_RES      41     41       Phosphoserine (By similarity).
FT   MOD_RES      68     68       Phosphotyrosine.
FT   MOD_RES      73     73       N6-acetyllysine (By similarity).
FT   MOD_RES      89     89       Phosphotyrosine (By similarity).
FT   MOD_RES     132    132       N6-acetyllysine (By similarity).
FT   MOD_RES     140    140       Phosphotyrosine.
FT   MOD_RES     144    144       N6-acetyllysine (By similarity).
FT   MOD_RES     156    156       Phosphoserine (By similarity).
SQ   SEQUENCE   166 AA;  18560 MW;  19834E8CA80747B2 CRC64;
     MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE EGKEILVGDV
     GQTVDDPYTT FVKMLPDKDC RYALYDATYE TKESKKEDLV FIFWAPENAP LKSKMIYASS
     KDAIKKKLTG IKHELQANCY EEVKDRCTLA EKLGGSAVIS LEGKPL
//
ID   KPB1_MOUSE              Reviewed;        1241 AA.
AC   P18826;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   08-MAR-2011, entry version 106.
DE   RecName: Full=Phosphorylase b kinase regulatory subunit alpha, skeletal muscle isoform;
DE            Short=Phosphorylase kinase alpha M subunit;
GN   Name=Phka1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=BALB/c; TISSUE=Skeletal muscle;
RX   MEDLINE=94129617; PubMed=8298647; DOI=10.1038/ng1293-381;
RA   Schneider A., Davidson J.J., Wuellrich A., Kilimann M.W.;
RT   "Phosphorylase kinase deficiency in I-strain mice is associated with a
RT   frameshift mutation in the alpha subunit muscle isoform.";
RL   Nat. Genet. 5:381-385(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 243-579.
RX   MEDLINE=90099389; PubMed=2602386; DOI=10.1073/pnas.86.24.9996;
RA   Bender P.K., Lalley P.A.;
RT   "I/Lyn mouse phosphorylase kinase deficiency: mutation disrupts
RT   expression of the alpha/alpha'-subunit mRNAs.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:9996-10000(1989).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200 AND SER-201, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of
CC       serine in certain substrates, including troponin I. The alpha
CC       chain may bind calmodulin.
CC   -!- ENZYME REGULATION: By phosphorylation of various serine residues
CC       and by calcium.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen metabolism.
CC   -!- SUBUNIT: Polymer of 16 chains, four each of alpha, beta, gamma,
CC       and delta. Alpha and beta are regulatory chains, gamma is the
CC       catalytic chain, and delta is calmodulin.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=ABC;
CC         IsoId=P18826-1; Sequence=Displayed;
CC       Name=2; Synonyms=AC;
CC         IsoId=P18826-2; Sequence=VSP_004698;
CC   -!- TISSUE SPECIFICITY: Both isoforms are expressed in muscle.
CC   -!- PTM: Although the final Cys may be farnesylated, the terminal
CC       tripeptide is probably not removed, and the C-terminus is not
CC       methylated (By similarity).
CC   -!- DISEASE: Note=Defects in Phka1 are the cause of phosphorylase
CC       kinase deficiency in I-strain mice.
CC   -!- SIMILARITY: Belongs to the phosphorylase b kinase regulatory chain
CC       family.
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DR   EMBL; X74616; CAA52687.1; -; mRNA.
DR   EMBL; M28867; AAA39927.1; -; mRNA.
DR   EMBL; X73877; CAA52085.1; -; Transcribed_RNA.
DR   IPI; IPI00115449; -.
DR   IPI; IPI00222459; -.
DR   PIR; S40528; S40528.
DR   UniGene; Mm.212889; -.
DR   UniGene; Mm.295539; -.
DR   UniGene; Mm.454789; -.
DR   ProteinModelPortal; P18826; -.
DR   STRING; P18826; -.
DR   PhosphoSite; P18826; -.
DR   PRIDE; P18826; -.
DR   Ensembl; ENSMUST00000052012; ENSMUSP00000061991; ENSMUSG00000034055.
DR   Ensembl; ENSMUST00000113611; ENSMUSP00000109241; ENSMUSG00000034055.
DR   UCSC; uc009tyr.1; mouse.
DR   MGI; MGI:97576; Phka1.
DR   HOVERGEN; HBG000273; -.
DR   OrthoDB; EOG4ZPDTH; -.
DR   ArrayExpress; P18826; -.
DR   Bgee; P18826; -.
DR   CleanEx; MM_PHKA1; -.
DR   Genevestigator; P18826; -.
DR   GermOnline; ENSMUSG00000034055; Mus musculus.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA:InterPro.
DR   GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR008928; 6-hairpin_glycosidase-like.
DR   InterPro; IPR012341; 6hp_glycosidase.
DR   InterPro; IPR011613; Glyco_hydro_15-rel.
DR   InterPro; IPR008734; PHK_AB.
DR   Gene3D; G3DSA:1.50.10.10; CelA/Cel48F_cat; 1.
DR   PANTHER; PTHR10749; PHK_AB; 1.
DR   Pfam; PF00723; Glyco_hydro_15; 1.
DR   SUPFAM; SSF48208; Glyco_trans_6hp; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calmodulin-binding; Carbohydrate metabolism;
KW   Cell membrane; Glycogen metabolism; Lipoprotein; Membrane;
KW   Muscle protein; Phosphoprotein; Prenylation.
FT   CHAIN         1   1241       Phosphorylase b kinase regulatory subunit
FT                                alpha, skeletal muscle isoform.
FT                                /FTId=PRO_0000057727.
FT   REGION      811    841       Calmodulin-binding (Potential).
FT   REGION     1064   1104       Calmodulin-binding (Potential).
FT   MOD_RES     200    200       Phosphoserine.
FT   MOD_RES     201    201       Phosphoserine.
FT   MOD_RES     736    736       Phosphoserine (By similarity).
FT   MOD_RES     973    973       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     986    986       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES    1008   1008       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES    1019   1019       Phosphoserine; by PKA (By similarity).
FT   MOD_RES    1021   1021       Phosphoserine (By similarity).
FT   MOD_RES    1024   1024       Phosphoserine (By similarity).
FT   LIPID      1238   1238       S-farnesyl cysteine (By similarity).
FT   VAR_SEQ    1026   1042       Missing (in isoform 2).
FT                                /FTId=VSP_004698.
SQ   SEQUENCE   1241 AA;  138793 MW;  B8740B7D90237050 CRC64;
     MRSRSNSGVR LDGYARLVHQ TILCHQNPVT GLLPASYDQK DAWVRDNVYS ILAVWGLGLA
     YRKNADRDED KAKAYELEQS VVKLMRGLLH CMIRQVDKVE SFKYSQSTPD SLHAKYNTKT
     CATVVGDDQW GHLQLDATSV YLLFLAQMTA SGLHIIHSLD EVNFIQNLVF YIEAAYKTAD
     FGIWERGDKT NQGISELNAS SVGMAKAALE ALDELDLFGV KGGPQSVIHV LADEVQHCQS
     ILNSLLPRAS TSKEVDASLL SVVSFPAFAV EDSHLVELTK QEIITKLQGR YGCCRFLRDG
     YKTPKEDPQR LYYNPAELKL FENIECEWPL FWTYFILDGI FSGNVEQVQE YREALDAVLI
     KGKNGVPLLP ELYSVPPDRV DEEYQNPHTV DRVPMGKLPH MWGQSLYILG SLMAEGFLAP
     GEIDPLNRRF STVPKPDVVV QVSILAETEE IKAILKDKGI DVETIAEVYP IRVQPARILS
     HIYSSLGCNS RMKLSGRPYR LMGVLGTSKL YDIRKTIFTF TPQFIDQQQF YLALDNQMIV
     EMLRTDLSYL CSRWRMTGQP TITFPISHTM LDEDGTSLNS SILAALRKMQ DGYFGGARIQ
     TGKLSEFLTT SCCTHLSFMD PGPEGKLYSE DYDEDYEDDL DSGNWMDSYD STSNARCGDE
     VARYLDRLLA HTVPHPKLAP TSRKGGLDRF RAAVQTTCDL MSLVAKAKEL HIQNVHMYIP
     TKLFQPSRPS LNLLDSPESP QDSQVPSVHV EVHLPRDQSG EVDFQSLVSQ LKETSSLQEQ
     ADILYMLYSM KGPDWNTELY EEGGATVREL LSELYVKVGE IRHWGLIRYI SGILRKKVEA
     LDEACTDLLS YQKHLTVGLP PEPREKTISA PLPYEALTKL IDEASEGDMS ISTLTQEIMV
     YLAMYMRTQP GLFAEMFRLR IGLIIQVMAT ELAHSLRCSA EEATEGLMNL SPSAMKNLLH
     HILSGKEFGV ERSVRPTDSN VSPAISIHEI GAVGATKTER TGIMQLKSEI KQVEFRRLSV
     SMESQTSGGH PSGVDLMSPS FLSPAACIAA SSGSFPTVCD HQTSKDSRQG QWQRRRRLDG
     ALNRVPIGFY QKVWKILQKC HGLSVEGFVL PSSTTREMTP GEIKFSVHVE SVLNRVPQPE
     YRQLLVEAIL VLTMLADIEI HSIGSIIAVE KIVHIANDLF LQEQKTLGAD DTMLAKDPAS
     GICTLLYDSA PSGRFGTMTY LSKAAATYVQ EFLPHSLCAM Q
//
ID   GNAO_MOUSE              Reviewed;         354 AA.
AC   P18872; P18873;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 121.
DE   RecName: Full=Guanine nucleotide-binding protein G(o) subunit alpha;
GN   Name=Gnao1; Synonyms=Gna0, Gnao;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1 AND ALPHA-2).
RC   TISSUE=Brain, and Spermatid;
RX   MEDLINE=90370808; PubMed=1697681; DOI=10.1073/pnas.87.17.6477;
RA   Strathmann M., Wilkie T.M., Simon M.I.;
RT   "Alternative splicing produces transcripts encoding two forms of the
RT   alpha subunit of GTP-binding protein Go.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:6477-6481(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA-1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 22-32; 36-46; 55-100; 106-143; 146-177; 182-193;
RP   199-206 AND 244-272, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC       involved as modulators or transducers in various transmembrane
CC       signaling systems. The G(o) protein function is not clear.
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and
CC       gamma. The alpha chain contains the guanine nucleotide binding
CC       site.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Alpha-1;
CC         IsoId=P18872-1; Sequence=Displayed;
CC       Name=Alpha-2;
CC         IsoId=P18872-2, P18873-1;
CC         Sequence=VSP_031251;
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
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DR   EMBL; M36777; AAA37645.1; -; mRNA.
DR   EMBL; M36778; AAA74566.1; -; mRNA.
DR   EMBL; BC051989; AAH51989.1; -; mRNA.
DR   IPI; IPI00115546; -.
DR   IPI; IPI00230192; -.
DR   PIR; A36038; RGMSO1.
DR   PIR; B36038; RGMSO2.
DR   RefSeq; NP_001106855.1; NM_001113384.1.
DR   RefSeq; NP_034438.1; NM_010308.3.
DR   UniGene; Mm.251445; -.
DR   PDB; 3C7K; X-ray; 2.90 A; A/C=22-354.
DR   PDBsum; 3C7K; -.
DR   ProteinModelPortal; P18872; -.
DR   SMR; P18872; 35-345.
DR   DIP; DIP-29921N; -.
DR   STRING; P18872; -.
DR   PhosphoSite; P18872; -.
DR   PRIDE; P18872; -.
DR   Ensembl; ENSMUST00000034198; ENSMUSP00000034198; ENSMUSG00000031748.
DR   GeneID; 14681; -.
DR   KEGG; mmu:14681; -.
DR   UCSC; uc009mvl.1; mouse.
DR   CTD; 14681; -.
DR   MGI; MGI:95775; Gnao1.
DR   HOVERGEN; HBG063184; -.
DR   OMA; GRSNEYQ; -.
DR   OrthoDB; EOG44F69B; -.
DR   PhylomeDB; P18872; -.
DR   NextBio; 286592; -.
DR   ArrayExpress; P18872; -.
DR   Bgee; P18872; -.
DR   CleanEx; MM_GNAO1; -.
DR   Genevestigator; P18872; -.
DR   GermOnline; ENSMUSG00000031748; Mus musculus.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; TAS:MGI.
DR   GO; GO:0005622; C:intracellular; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IMP:MGI.
DR   GO; GO:0003924; F:GTPase activity; TAS:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0007212; P:dopamine receptor signaling pathway; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0008016; P:regulation of heart contraction; IMP:MGI.
DR   InterPro; IPR001408; Gprotein_alpha_I.
DR   InterPro; IPR001019; Gprotein_alpha_su.
DR   InterPro; IPR011025; GproteinA_insert.
DR   Gene3D; G3DSA:1.10.400.10; GproteinA_insert; 1.
DR   PANTHER; PTHR10218; Gprotein_alph_bd; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00441; GPROTEINAI.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF47895; Transducn_insert; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing;
KW   GTP-binding; Lipoprotein; Myristate; Nucleotide-binding; Palmitate;
KW   Transducer.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    354       Guanine nucleotide-binding protein G(o)
FT                                subunit alpha.
FT                                /FTId=PRO_0000203704.
FT   NP_BIND      40     47       GTP (By similarity).
FT   NP_BIND     201    205       GTP (By similarity).
FT   NP_BIND     270    273       GTP (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
FT   LIPID         3      3       S-palmitoyl cysteine (By similarity).
FT   VAR_SEQ     249    354       MLFDSICNNKFFIDTSIILFLNKKDLFGEKIKKSPLTICFP
FT                                EYPGSNTYEDAAAYIQTQFESKNRSPNKEIYCHMTCATDTN
FT                                NIQVVFDAVTDIIIANNLRGCGLY -> KLFDSICNNKWFT
FT                                DTSIILFLNKKDIFEEKIKKSPLTICFPEYTGPSAFTEAVA
FT                                HIQGQYESKNKSAHKEVYSHVTCATDTNNIQFVFDAVTDVI
FT                                IAKNLRGCGLY (in isoform Alpha-2).
FT                                /FTId=VSP_031251.
FT   STRAND       36     41
FT   TURN         46     49
FT   HELIX        50     52
FT   HELIX        63     91
FT   HELIX       100    113
FT   TURN        114    116
FT   HELIX       122    131
FT   HELIX       135    141
FT   TURN        142    145
FT   HELIX       153    157
FT   HELIX       160    163
FT   TURN        172    176
FT   STRAND      186    188
FT   STRAND      199    201
FT   TURN        206    208
FT   HELIX       209    212
FT   HELIX       214    216
FT   STRAND      220    225
FT   HELIX       228    232
FT   STRAND      239    242
FT   HELIX       243    255
FT   HELIX       258    260
FT   STRAND      263    268
FT   HELIX       272    279
FT   HELIX       284    286
FT   HELIX       297    310
FT   HELIX       329    344
SQ   SEQUENCE   354 AA;  40085 MW;  B73A84F3BDB09F2C CRC64;
     MGCTLSAEER AALERSKAIE KNLKEDGISA AKDVKLLLLG AGESGKSTIV KQMKIIHEDG
     FSGEDVKQYK PVVYSNTIQS LAAIVRAMDT LGVEYGDKER KTDSKMVCDV VSRMEDTEPF
     SAELLSAMMR LWGDSGIQEC FNRSREYQLN DSAKYYLDSL DRIGAGDYQP TEQDILRTRV
     KTTGIVETHF TFKNLHFRLF DVGGQRSERK KWIHCFEDVT AIIFCVALSG YDQVLHEDET
     TNRMHESLML FDSICNNKFF IDTSIILFLN KKDLFGEKIK KSPLTICFPE YPGSNTYEDA
     AAYIQTQFES KNRSPNKEIY CHMTCATDTN NIQVVFDAVT DIIIANNLRG CGLY
//
ID   FAS_MOUSE               Reviewed;        2504 AA.
AC   P19096; B1ATU8; Q6PB72; Q8C4Z0; Q9EQR0;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 2.
DT   08-MAR-2011, entry version 113.
DE   RecName: Full=Fatty acid synthase;
DE            EC=2.3.1.85;
DE   Includes:
DE     RecName: Full=[Acyl-carrier-protein] S-acetyltransferase;
DE              EC=2.3.1.38;
DE   Includes:
DE     RecName: Full=[Acyl-carrier-protein] S-malonyltransferase;
DE              EC=2.3.1.39;
DE   Includes:
DE     RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase;
DE              EC=2.3.1.41;
DE   Includes:
DE     RecName: Full=3-oxoacyl-[acyl-carrier-protein] reductase;
DE              EC=1.1.1.100;
DE   Includes:
DE     RecName: Full=3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase;
DE              EC=4.2.1.61;
DE   Includes:
DE     RecName: Full=Enoyl-[acyl-carrier-protein] reductase;
DE              EC=1.3.1.10;
DE   Includes:
DE     RecName: Full=Oleoyl-[acyl-carrier-protein] hydrolase;
DE              EC=3.1.2.14;
GN   Name=Fasn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20485744; PubMed=11029661;
RX   DOI=10.1046/j.1365-2443.2000.00369.x;
RA   Ueno K.;
RT   "Involvement of fatty acid synthase in axonal development in mouse
RT   embryos.";
RL   Genes Cells 5:859-869(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Brain, and Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-12; 225-235; 299-310; 385-409; 469-478;
RP   1252-1270; 1333-1344; 1388-1398; 1501-1508; 1705-1717; 1733-1745;
RP   2124-2132; 2376-2384 AND 2476-2498, ACETYLATION AT MET-1, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Liver;
RA   Bienvenut W.V.;
RL   Submitted (JUL-2005) to UniProtKB.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1527-2504.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1666-2504.
RC   STRAIN=CD-1; TISSUE=Liver;
RX   MEDLINE=89149781; PubMed=2920037; DOI=10.1016/0006-291X(89)92776-9;
RA   Paulauskis J.D., Sul H.S.;
RT   "Structure of mouse fatty acid synthase mRNA. Identification of the
RT   two NADPH binding sites.";
RL   Biochem. Biophys. Res. Commun. 158:690-695(1989).
CC   -!- FUNCTION: Fatty acid synthetase catalyzes the formation of long-
CC       chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This
CC       multifunctional protein has 7 catalytic activities and an acyl
CC       carrier protein.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + n malonyl-CoA + 2n NADPH = a
CC       long-chain fatty acid + (n+1) CoA + n CO(2) + 2n NADP(+).
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + [acyl-carrier-protein] = CoA +
CC       acetyl-[acyl-carrier-protein].
CC   -!- CATALYTIC ACTIVITY: Malonyl-CoA + [acyl-carrier-protein] = CoA +
CC       malonyl-[acyl-carrier-protein].
CC   -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + malonyl-[acyl-
CC       carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) +
CC       [acyl-carrier-protein].
CC   -!- CATALYTIC ACTIVITY: (3R)-3-hydroxyacyl-[acyl-carrier-protein] +
CC       NADP(+) = 3-oxoacyl-[acyl-carrier-protein] + NADPH.
CC   -!- CATALYTIC ACTIVITY: (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein]
CC       = hexadec-2-enoyl-[acyl-carrier-protein] + H(2)O.
CC   -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + NADP(+) = trans-
CC       2,3-dehydroacyl-[acyl-carrier-protein] + NADPH.
CC   -!- CATALYTIC ACTIVITY: Oleoyl-[acyl-carrier-protein] + H(2)O = [acyl-
CC       carrier-protein] + oleate.
CC   -!- SUBUNIT: Homodimer which is arranged in a head to tail fashion.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Melanosome (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 acyl carrier domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA31525.1; Type=Frameshift; Positions=1842, 1855, 1863, 1964, 1967;
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DR   EMBL; AF127033; AAG02285.1; -; mRNA.
DR   EMBL; AL663090; CAM27545.1; -; Genomic_DNA.
DR   EMBL; BC046513; AAH46513.1; -; mRNA.
DR   EMBL; BC059850; AAH59850.1; -; mRNA.
DR   EMBL; AK080374; BAC37895.1; -; mRNA.
DR   EMBL; X13135; CAA31525.1; ALT_FRAME; mRNA.
DR   IPI; IPI00113223; -.
DR   PIR; A32262; A32262.
DR   RefSeq; NP_032014.3; NM_007988.3.
DR   UniGene; Mm.236443; -.
DR   ProteinModelPortal; P19096; -.
DR   SMR; P19096; 2-853, 1215-2107, 2113-2201, 2214-2500.
DR   STRING; P19096; -.
DR   PhosphoSite; P19096; -.
DR   PRIDE; P19096; -.
DR   Ensembl; ENSMUST00000055655; ENSMUSP00000052872; ENSMUSG00000025153.
DR   GeneID; 14104; -.
DR   KEGG; mmu:14104; -.
DR   NMPDR; fig|10090.3.peg.25828; -.
DR   UCSC; uc007mut.1; mouse.
DR   CTD; 14104; -.
DR   MGI; MGI:95485; Fasn.
DR   HOGENOM; HBG316016; -.
DR   HOVERGEN; HBG005640; -.
DR   InParanoid; P19096; -.
DR   OMA; DIFRNSI; -.
DR   OrthoDB; EOG4KH2T3; -.
DR   PhylomeDB; P19096; -.
DR   BRENDA; 1.1.1.100; 244.
DR   BRENDA; 1.3.1.10; 244.
DR   BRENDA; 2.3.1.38; 244.
DR   BRENDA; 2.3.1.39; 244.
DR   BRENDA; 2.3.1.41; 244.
DR   BRENDA; 2.3.1.85; 244.
DR   BRENDA; 3.1.2.14; 244.
DR   BRENDA; 4.2.1.61; 244.
DR   NextBio; 285138; -.
DR   ArrayExpress; P19096; -.
DR   Bgee; P19096; -.
DR   CleanEx; MM_FASN; -.
DR   Genevestigator; P19096; -.
DR   GermOnline; ENSMUSG00000025153; Mus musculus.
DR   GO; GO:0042587; C:glycogen granule; IDA:MGI.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0004317; F:3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity; IEA:EC.
DR   GO; GO:0004316; F:3-oxoacyl-[acyl-carrier-protein] reductase activity; IEA:EC.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:EC.
DR   GO; GO:0004313; F:[acyl-carrier-protein] S-acetyltransferase activity; IEA:EC.
DR   GO; GO:0004314; F:[acyl-carrier-protein] S-malonyltransferase activity; IEA:EC.
DR   GO; GO:0000036; F:acyl carrier activity; IEA:InterPro.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0004319; F:enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific) activity; IEA:EC.
DR   GO; GO:0004320; F:oleoyl-[acyl-carrier-protein] hydrolase activity; IEA:EC.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR001227; Ac_transferase_dom.
DR   InterPro; IPR009081; Acyl_carrier_prot-like.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPlipase.
DR   InterPro; IPR013149; ADH_C.
DR   InterPro; IPR000794; Beta-ketoacyl_synthase.
DR   InterPro; IPR023102; Fatty_acid_synthase_dom_2.
DR   InterPro; IPR011032; GroES-like.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR013217; Methyltransf_12.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR006163; Phsphopanteth-bd.
DR   InterPro; IPR020842; PKS/FAS_KR.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR006162; PPantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR016038; Thiolase-like_subgr.
DR   Gene3D; G3DSA:3.40.366.10; Ac_transferase_reg; 2.
DR   Gene3D; G3DSA:1.10.1200.10; ACP_like; 1.
DR   Gene3D; G3DSA:1.10.1470.20; Fatty_acid_synthase_dom_2; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 2.
DR   Gene3D; G3DSA:3.40.47.10; Thiolase-like_subgr; 2.
DR   PANTHER; PTHR11712; Ketoacyl_synth; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF08242; Methyltransf_12; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF47336; ACP_like; 1.
DR   SUPFAM; SSF52151; Acyl_Trfase/lysoPlipase; 1.
DR   SUPFAM; SSF50129; GroES_like; 1.
DR   SUPFAM; SSF55048; Malonyl_transacylase_ACP-bd; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; ACP_DOMAIN; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing;
KW   Fatty acid biosynthesis; Hydrolase; Lipid synthesis; Lyase;
KW   Multifunctional enzyme; NAD; NADP; Oxidoreductase; Phosphopantetheine;
KW   Phosphoprotein; Pyridoxal phosphate; Transferase.
FT   CHAIN         1   2504       Fatty acid synthase.
FT                                /FTId=PRO_0000180277.
FT   DOMAIN     2117   2173       Acyl carrier.
FT   NP_BIND    1664   1681       NADP (ER) (By similarity).
FT   NP_BIND    1879   1894       NADP (KR) (By similarity).
FT   REGION        1    414       Beta-ketoacyl synthase.
FT   REGION      429    817       Acyl and malonyl transferases.
FT   REGION     1628   1856       Enoyl reductase.
FT   REGION     1857   2111       Beta-ketoacyl reductase.
FT   REGION     2201   2504       Thioesterase.
FT   ACT_SITE    161    161       For beta-ketoacyl synthase activity (By
FT                                similarity).
FT   ACT_SITE    581    581       For malonyltransferase activity (By
FT                                similarity).
FT   ACT_SITE    878    878       For beta-hydroxyacyl dehydratase activity
FT                                (By similarity).
FT   ACT_SITE   2301   2301       For thioesterase activity (By
FT                                similarity).
FT   ACT_SITE   2474   2474       For thioesterase activity (By
FT                                similarity).
FT   MOD_RES       1      1       N-acetylmethionine.
FT   MOD_RES      70     70       N6-acetyllysine (By similarity).
FT   MOD_RES     207    207       Phosphoserine (By similarity).
FT   MOD_RES     298    298       N6-acetyllysine (By similarity).
FT   MOD_RES     528    528       N6-acetyllysine (By similarity).
FT   MOD_RES     673    673       N6-acetyllysine (By similarity).
FT   MOD_RES    1697   1697       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
FT   MOD_RES    1697   1697       N6-acetyllysine (By similarity).
FT   MOD_RES    1745   1745       N6-acetyllysine (By similarity).
FT   MOD_RES    1764   1764       N6-acetyllysine (By similarity).
FT   MOD_RES    1840   1840       N6-acetyllysine (By similarity).
FT   MOD_RES    1988   1988       N6-acetyllysine (By similarity).
FT   MOD_RES    2150   2150       O-(pantetheine 4'-phosphoryl)serine (By
FT                                similarity).
FT   MOD_RES    2229   2229       Phosphoserine (By similarity).
FT   CONFLICT   1992   1992       T -> N (in Ref. 6; CAA31525).
FT   CONFLICT   2028   2028       G -> C (in Ref. 6; CAA31525).
FT   CONFLICT   2045   2045       G -> V (in Ref. 6; CAA31525).
FT   CONFLICT   2117   2117       T -> N (in Ref. 6; CAA31525).
FT   CONFLICT   2175   2175       Q -> R (in Ref. 6; CAA31525).
FT   CONFLICT   2295   2295       Y -> H (in Ref. 6; CAA31525).
SQ   SEQUENCE   2504 AA;  272428 MW;  2B48068B9D370C6F CRC64;
     MEEVVIAGMS GKLPESENLQ EFWANLIGGV DMVTDDDRRW KAGLYGLPKR SGKLKDLSKF
     DASFFGVHPK QAHTMDPQLR LLLEVSYEAI VDGGINPASL RGTNTGVWVG VSGSEASEAL
     SRDPETLLGY SMVGCQRAMM ANRLSFFFDF KGPSIALDTA CSSSLLALQN AYQAIRSGEC
     PAALVGGINL LLKPNTSVQF MKLGMLSPDG TCRSFDDSGS GYCRSEAVVA VLLTKKSLAR
     RVYATILNAG TNTDGSKEQG VTFPSGEVQE QLICSLYQPA GLAPESLEYI EAHGTGTKVG
     DPQELNGITR SLCAFRQAPL LIGSTKSNMG HPEPASGLAA LTKVLLSLEH GVWAPNLHFH
     NPNPEIPALL DGRLQVVDRP LPVRGGNVGI NSFGFGGSNV HVILQPNTRQ APAPTAHAAL
     PHLLHASGRT LEAVQDLLEQ GRQHSQDLAF VSMLNDIAAT PTAAMPFRGY TVLGVEGRVQ
     EVQQVSTNKR PLWFICSGMG TQWRGMGLSL MRLDSFRESI LRSDEAVKPL GVKVSDLLLS
     TDERTFDDIV HAFVSLTAIQ IALIDLLTSV GLKPDGIIGH SLGEVACGYA DGCLSQREAV
     LAAYWRGQCI KDAHLPPGSM AAVGLSWEEC KQRCPAGVVP ACHNSEDTVT ISGPQAAVNE
     FVEQLKQEGV FAKEVRTGGL AFHSYFMEGI APTLLQALKK VIREPRPRSA RWLSTSIPEA
     QWQSSLARTS SAEYNVNNLV SPVLFQEALW HIPEHAVVLE IAPHALLQAV LKRGVKSSCT
     IIPLMKRDHK DNLEFFLTNL GKVHLTGINV NPNALFPPVE FPAPRGTPLI SPHIKWDHSQ
     TWDVPVAEDF PNGSSSSSAT VYSIDASPES PDHYLVDHCI DGRVIFPGTG YLCLVWKTLA
     RSLGLSLEET PVVFENVSFH QATILPKTGT VALEVRLLEA SHAFEVSDTG NLIVSGKVYL
     WEDPNSKLFD HPEVPTPPES ASVSRLTQGE VYKELRLRGY DYGPQFQGIC EATLEGEQGK
     LLWKDNWVTF MDTMLQVSIL GSSQQSLQLP TRVTAIYIDP ATHRQKVYRL KEDTQVADVT
     TSRCLGITVS GGIHISRLQT TATSRRQQEQ LVPTLEKFVF TPHMEAECLS ESTALQKELQ
     LCKGLARALQ TKATQQGLKA AMLGQEDPPQ HGLPRLLAAA CQLQLNGNLQ LELGEALAQE
     RLLLPEDPLI SGLLNSQALK ACVDTALENL STLKMKVAEV LAGEGHLYSR IPALLNTQPM
     LQLEYTATDR HPQALKDVQT KLQQHDVAQG QWNPSDPAPS SLGALDLLVC NCALATLGDP
     ALALDNMVAA LKEGGFLLVH TVLKGHALGE TLACLPSEVQ PAPSLLSQEE WESLFSRKAL
     HLVGLKRSFY GTALFLCRRA IPQEKPIFLS VEDTSFQWVD SLKSTLATSS SQPVWLTAMD
     CPTSGVVGLV NCLRKEPGGH RIRCILLSNL SNTSHAPKLD PGSPELQQVL KHDLVMNVYR
     DGAWGAFRHF QLEQDKPKEQ TAHAFVNVLT RGDLASIRWV SSPLKHTQPS SSGAQLCTVY
     YASLNFRDIM LATGKLSPDA IPGKWASRDC MLGMEFSGRD RCGRRVMGLV PAEGLATSVL
     LSSDFLWDVP SSWTLEEAAS VPVVYTTAYY SLVVRGRIQR GETVLIHSGS GGVGQAAISI
     ALSLGCRVFT TVGSAEKRAY LQARFPQLDD TSFANSRDTS FEQHVLLHTG GKGVDLVLNS
     LAEEKLQASV RCLAQHGRFL EIGKFDLSNN HPLGMAIFLK NVTFHGILLD ALFEEANDSW
     REVAALLKAG IRDGVVKPLK CTVFPKAQVE DAFRYMAQGK HIGKVLVQVR EEEPEAVLPG
     AQPTLISAIS KTFCPAHKSY IITGGLGGFG LELARWLVLR GAQRLVLTSR SGIRTGYQAK
     HIREWRRQGI QVLVSTSNVS SLEGARALIA EATKLGPVGG VFNLAMVLRD AMLENQTPEL
     FQDVNKPKYN GTLNLDRATR EACPELDYFV AFSSVSCGRG NAGQTNYGFA NSTMERICEQ
     RRHDGLPGLA VQWGAIGDVG IVLEAMGTND TVIGGTLPQR ISSCMEVLDL FLNQPHAVLS
     SFVLAEKKAV AHGDGDTQRD LVKAVAHILG IRDLAGINLD STLADLGLDS LMGVEVRQIL
     EREHDLVLPM REVRQLTLRK LQEMSSKTDS ATDTTAPKSR SDTSLKQNQL NLSTLLVNPE
     GPTLTQLNSV QSSERPLFLV HPIEGSTTVF HSLAAKLSVP TYGLQCTQAA PLDSIPNLAA
     YYIDCIKQVQ PEGPYRIAGY SFGACVAFEM CSQLQAQQGP APTHNNLFLF DGSHTYVLAY
     TQSYRAKMTP GCEAEAEAEA LCFFIKQFLD VEHSKVLEAL LPLKSLEDRV AASVDLITKS
     HHSLDRRELS FAAVSFYHKL RAADQYKPKA KYHGNVTLLR AKTGGTYGED LGADYNLSQV
     CDGKVSVHII EGDHRTLLEG SGLESIINII HSSLAEPRVS VREG
//
ID   NFH_MOUSE               Reviewed;        1090 AA.
AC   P19246; A1E2H9; Q5SVF6; Q61959;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 3.
DT   08-MAR-2011, entry version 109.
DE   RecName: Full=Neurofilament heavy polypeptide;
DE            Short=NF-H;
DE   AltName: Full=200 kDa neurofilament protein;
DE   AltName: Full=Neurofilament triplet H protein;
GN   Name=Nefh; Synonyms=Kiaa0845, Nfh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster; TISSUE=Brain;
RX   MEDLINE=89089138; PubMed=3145094;
RA   Shneidman P.S., Carden M.J., Lees J.F., Lazzarini R.A.;
RT   "The structure of the largest murine neurofilament protein (NF-H) as
RT   revealed by cDNA and genomic sequences.";
RL   Brain Res. 464:217-231(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=89121513; PubMed=3220257; DOI=10.1016/0378-1119(88)90033-9;
RA   Julien J.-P., Cote F., Beaudet L., Sidky M., Flavell D., Grosveld F.,
RA   Mushynski W.;
RT   "Sequence and structure of the mouse gene coding for the largest
RT   neurofilament subunit.";
RL   Gene 68:307-314(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Swiss Webster; TISSUE=Brain;
RA   Carden M.J.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   PROTEIN SEQUENCE OF 167-180; 351-370; 382-401 AND 903-917, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Klug S., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 814-961.
RC   STRAIN=VM;
RA   Huysentruyt L.C., Banerjee D., Seyfried T.N.;
RT   "Novel metastatic mouse tumor cells express multiple properties of
RT   macrophages.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-416; SER-500;
RP   SER-523; SER-529; SER-535; SER-541; SER-547; SER-553; SER-559;
RP   SER-565; SER-571; SER-577; SER-583; SER-613; SER-619; SER-625;
RP   SER-631; SER-637; SER-649; SER-655; SER-661; SER-667; SER-673;
RP   SER-679; SER-685; SER-691; SER-697; SER-703; SER-709; SER-715;
RP   SER-721; SER-727; SER-733; SER-739; SER-745; SER-751; SER-757;
RP   SER-763; SER-769; THR-775; SER-783; SER-789; SER-815; SER-834;
RP   THR-839; SER-867 AND SER-888, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 AND THR-499, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-685 AND SER-691, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Neurofilaments usually contain three intermediate
CC       filament proteins: L, M, and H which are involved in the
CC       maintenance of neuronal caliber. NF-H has an important function in
CC       mature axons that is not subserved by the two smaller NF proteins.
CC   -!- PTM: There are a number of repeats of the tripeptide K-S-P, NFH is
CC       phosphorylated on a number of the serines in this motif. It is
CC       thought that phosphorylation of NFH results in the formation of
CC       interfilament cross bridges that are important in the maintenance
CC       of axonal caliber.
CC   -!- PTM: Phosphorylation seems to play a major role in the functioning
CC       of the larger neurofilament polypeptides (NF-M and NF-H), the
CC       levels of phosphorylation being altered developmentally and
CC       coincident with a change in the neurofilament function.
CC   -!- PTM: Phosphorylated in the Head and Rod regions by the PKC kinase
CC       PKN1, leading to inhibit polymerization (By similarity).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA39813.1; Type=Erroneous initiation;
CC       Sequence=CAA83229.1; Type=Erroneous initiation;
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DR   EMBL; M35131; AAA39809.1; -; mRNA.
DR   EMBL; M24496; AAA39813.1; ALT_INIT; Genomic_DNA.
DR   EMBL; M23349; AAA39813.1; JOINED; Genomic_DNA.
DR   EMBL; M24494; AAA39813.1; JOINED; Genomic_DNA.
DR   EMBL; M24495; AAA39813.1; JOINED; Genomic_DNA.
DR   EMBL; Z31012; CAA83229.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL645522; CAI25933.1; -; Genomic_DNA.
DR   EMBL; EF101556; ABK96805.1; -; mRNA.
DR   IPI; IPI00114241; -.
DR   PIR; JT0368; QFMSH.
DR   RefSeq; NP_035034.2; NM_010904.3.
DR   UniGene; Mm.298283; -.
DR   ProteinModelPortal; P19246; -.
DR   SMR; P19246; 94-130, 135-242, 264-334, 338-406.
DR   DisProt; DP00050; -.
DR   STRING; P19246; -.
DR   PhosphoSite; P19246; -.
DR   UCD-2DPAGE; P19246; -.
DR   PRIDE; P19246; -.
DR   Ensembl; ENSMUST00000093369; ENSMUSP00000091061; ENSMUSG00000020396.
DR   GeneID; 380684; -.
DR   KEGG; mmu:380684; -.
DR   UCSC; uc007hvm.1; mouse.
DR   CTD; 380684; -.
DR   MGI; MGI:97309; Nefh.
DR   eggNOG; roNOG14784; -.
DR   GeneTree; ENSGT00560000076592; -.
DR   HOGENOM; HBG715391; -.
DR   HOVERGEN; HBG013015; -.
DR   InParanoid; P19246; -.
DR   OMA; EAKSPGE; -.
DR   OrthoDB; EOG4NS3BW; -.
DR   NextBio; 401100; -.
DR   ArrayExpress; P19246; -.
DR   Bgee; P19246; -.
DR   CleanEx; MM_NEFH; -.
DR   Genevestigator; P19246; -.
DR   GermOnline; ENSMUSG00000020396; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005883; C:neurofilament; IDA:MGI.
DR   GO; GO:0045110; P:intermediate filament bundle assembly; IGI:MGI.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IGI:MGI.
DR   GO; GO:0060052; P:neurofilament cytoskeleton organization; IGI:MGI.
DR   InterPro; IPR010790; DUF1388.
DR   InterPro; IPR016044; F.
DR   InterPro; IPR001419; Glutenin.
DR   InterPro; IPR018039; Intermediate_filament_CS.
DR   Pfam; PF07142; DUF1388; 17.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF03157; Glutenin_hmw; 1.
DR   PROSITE; PS00226; IF; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Direct protein sequencing; Intermediate filament;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1   1090       Neurofilament heavy polypeptide.
FT                                /FTId=PRO_0000063801.
FT   REPEAT      522    527       1.
FT   REPEAT      528    533       2.
FT   REPEAT      534    539       3.
FT   REPEAT      540    545       4.
FT   REPEAT      546    551       5.
FT   REPEAT      552    557       6.
FT   REPEAT      558    563       7.
FT   REPEAT      564    569       8.
FT   REPEAT      570    575       9.
FT   REPEAT      576    581       10.
FT   REPEAT      582    587       11.
FT   REPEAT      588    593       12.
FT   REPEAT      594    599       13.
FT   REPEAT      600    605       14.
FT   REPEAT      606    611       15.
FT   REPEAT      612    617       16.
FT   REPEAT      618    623       17.
FT   REPEAT      624    629       18.
FT   REPEAT      630    635       19.
FT   REPEAT      636    641       20.
FT   REPEAT      642    647       21.
FT   REPEAT      648    653       22.
FT   REPEAT      654    659       23.
FT   REPEAT      660    665       24.
FT   REPEAT      666    671       25.
FT   REPEAT      672    677       26.
FT   REPEAT      678    683       27.
FT   REPEAT      684    689       28.
FT   REPEAT      690    695       29.
FT   REPEAT      696    701       30.
FT   REPEAT      702    707       31.
FT   REPEAT      708    713       32.
FT   REPEAT      714    719       33.
FT   REPEAT      720    725       34.
FT   REPEAT      726    731       35.
FT   REPEAT      732    737       36.
FT   REPEAT      738    743       37.
FT   REPEAT      744    749       38.
FT   REPEAT      750    755       39.
FT   REPEAT      756    761       40.
FT   REPEAT      762    767       41.
FT   REPEAT      768    773       42.
FT   REPEAT      774    779       43; approximate.
FT   REPEAT      782    787       44.
FT   REPEAT      788    793       45.
FT   REPEAT      794    799       46.
FT   REPEAT      808    813       47.
FT   REPEAT      814    819       48.
FT   REPEAT      833    838       49.
FT   REPEAT      858    863       50.
FT   REPEAT      866    871       51.
FT   REPEAT      887    892       52.
FT   REGION        2     98       Head.
FT   REGION       99    411       Rod.
FT   REGION       99    130       Coil 1A.
FT   REGION      131    143       Linker 1.
FT   REGION      144    242       Coil 1B.
FT   REGION      243    264       Linker 12.
FT   REGION      265    286       Coil 2A.
FT   REGION      287    290       Linker 2.
FT   REGION      291    411       Coil 2B.
FT   REGION      412   1090       Tail.
FT   REGION      522    892       52 X 6 AA approximate tandem repeats of
FT                                K-S-P-[AGISV]-[EATK]-[APVQ].
FT   COMPBIAS    439    520       Glu-rich (acidic).
FT   COMPBIAS    890   1090       Glu/Lys-rich.
FT   MOD_RES      61     61       Phosphoserine.
FT   MOD_RES     416    416       Phosphoserine.
FT   MOD_RES     499    499       Phosphothreonine.
FT   MOD_RES     500    500       Phosphoserine.
FT   MOD_RES     523    523       Phosphoserine.
FT   MOD_RES     529    529       Phosphoserine.
FT   MOD_RES     535    535       Phosphoserine.
FT   MOD_RES     541    541       Phosphoserine.
FT   MOD_RES     547    547       Phosphoserine.
FT   MOD_RES     553    553       Phosphoserine.
FT   MOD_RES     559    559       Phosphoserine.
FT   MOD_RES     565    565       Phosphoserine.
FT   MOD_RES     571    571       Phosphoserine.
FT   MOD_RES     577    577       Phosphoserine.
FT   MOD_RES     583    583       Phosphoserine.
FT   MOD_RES     613    613       Phosphoserine.
FT   MOD_RES     619    619       Phosphoserine.
FT   MOD_RES     625    625       Phosphoserine.
FT   MOD_RES     631    631       Phosphoserine.
FT   MOD_RES     637    637       Phosphoserine.
FT   MOD_RES     649    649       Phosphoserine.
FT   MOD_RES     655    655       Phosphoserine.
FT   MOD_RES     661    661       Phosphoserine.
FT   MOD_RES     667    667       Phosphoserine.
FT   MOD_RES     673    673       Phosphoserine.
FT   MOD_RES     679    679       Phosphoserine.
FT   MOD_RES     685    685       Phosphoserine.
FT   MOD_RES     691    691       Phosphoserine.
FT   MOD_RES     697    697       Phosphoserine.
FT   MOD_RES     703    703       Phosphoserine.
FT   MOD_RES     709    709       Phosphoserine.
FT   MOD_RES     715    715       Phosphoserine.
FT   MOD_RES     721    721       Phosphoserine.
FT   MOD_RES     727    727       Phosphoserine.
FT   MOD_RES     733    733       Phosphoserine.
FT   MOD_RES     739    739       Phosphoserine.
FT   MOD_RES     745    745       Phosphoserine.
FT   MOD_RES     751    751       Phosphoserine.
FT   MOD_RES     757    757       Phosphoserine.
FT   MOD_RES     763    763       Phosphoserine.
FT   MOD_RES     769    769       Phosphoserine.
FT   MOD_RES     775    775       Phosphothreonine.
FT   MOD_RES     783    783       Phosphoserine.
FT   MOD_RES     789    789       Phosphoserine.
FT   MOD_RES     815    815       Phosphoserine.
FT   MOD_RES     834    834       Phosphoserine.
FT   MOD_RES     839    839       Phosphothreonine.
FT   MOD_RES     867    867       Phosphoserine.
FT   MOD_RES     888    888       Phosphoserine.
FT   CONFLICT    134    135       QA -> K (in Ref. 2; AAA39813).
FT   CONFLICT    202    202       Missing (in Ref. 2; AAA39813).
FT   CONFLICT    284    284       T -> S (in Ref. 2; AAA39813).
FT   CONFLICT    495    495       G -> L (in Ref. 2; AAA39813).
FT   CONFLICT    519    519       E -> EEAKSPG (in Ref. 1; AAA39809 and 3;
FT                                CAA83229).
FT   CONFLICT    549    549       G -> R (in Ref. 1; AAA39809 and 3;
FT                                CAA83229).
FT   CONFLICT    694    717       Missing (in Ref. 1; AAA39809 and 3;
FT                                CAA83229).
FT   CONFLICT    817    817       V -> M (in Ref. 1; AAA39809, 3; CAA83229
FT                                and 6; ABK96805).
FT   CONFLICT    846    847       KH -> ND (in Ref. 1; AAA39809, 3;
FT                                CAA83229 and 6; ABK96805).
FT   CONFLICT    846    847       KH -> TV (in Ref. 2; AAA39813).
SQ   SEQUENCE   1090 AA;  116994 MW;  B2A7D7D36FF2F448 CRC64;
     MMSFGSADAL LGAPFAPLHG GGSLHYSLSR KAGPGGTRSA AGSSSGFHSW ARTSVSSVSA
     SPSRFRGAAS STDSLDTLSN GPEGCVVAAV AARSEKEQLQ ALNDRFAGYI DKVRQLEAHN
     RSLEGEAAAL RQQQAGRAAM GELYEREVRE MRGAVLRLGA ARGQLRLEQE HLLEDIAHVR
     QRLDEEARQR EEAEAAARAL ARFAQEAEAA RVELQKKAQA LQEECGYLRR HHQEEVGELL
     GQIQGCGAAQ AQAQAEARDA LKCDVTSALR EIRAQLEGHA VQSTLQSEEW FRVRLDRLSE
     AAKVNTDAMR SAQEEITEYR RQLQARTTEL EALKSTKESL ERQRSELEDR HQADIASYQD
     AIQQLDSELR NTKWEMAAQL REYQDLLNVK MALDIEIAAY RKLLEGEECR IGFGPSPFSL
     TEGLPKIPSI STHIKVKSEE MIKVVEKSEK ETVIVEGQTE EIRVTEGVTE EEDKEAQGQE
     GEEAEEGEEK EEEEGAAATS PPAEEAASPE KETKSRVKEE AKSPGEAKSP GEAKSPAEAK
     SPGEAKSPGE AKSPGEAKSP AEPKSPAEPK SPAEAKSPAE PKSPATVKSP GEAKSPSEAK
     SPAEAKSPAE AKSPAEAKSP AEAKSPAEAK SPAEAKSPAT VKSPGEAKSP SEAKSPAEAK
     SPAEAKSPAE AKSPAEVKSP GEAKSPAEPK SPAEAKSPAE VKSPAEAKSP AEVKSPGEAK
     SPAAVKSPAE AKSPAAVKSP GEAKSPGEAK SPAEAKSPAE AKSPIEVKSP EKAKTPVKEG
     AKSPAEAKSP EKAKSPVKED IKPPAEAKSP EKAKSPVKEG AKPPEKAKPL DVKSPEAQTP
     VQEEAKHPTD IRPPEQVKSP AKEKAKSPEK EEAKTSEKVA PKKEEVKSPV KEEVKAKEPP
     KKVEEEKTLP TPKTEAKESK KDEAPKEAPK PKVEEKKETP TEKPKDSTAE AKKEEAGEKK
     KAVASEEETP AKLGVKEEAK PKEKTETTKT EAEDTKAKEP SKPTETEKPK KEEMPAAPEK
     KDTKEEKTTE SRKPEEKPKM EAKVKEDDKS LSKEPSKPKT EKAEKSSSTD QKESQPPEKT
     TEDKATKGEK
//
ID   COX41_MOUSE             Reviewed;         169 AA.
AC   P19783; Q545A9;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 2.
DT   08-MAR-2011, entry version 105.
DE   RecName: Full=Cytochrome c oxidase subunit 4 isoform 1, mitochondrial;
DE   AltName: Full=Cytochrome c oxidase polypeptide IV;
DE   AltName: Full=Cytochrome c oxidase subunit IV isoform 1;
DE            Short=COX IV-1;
DE   Flags: Precursor;
GN   Name=Cox4i1; Synonyms=Cox4, Cox4a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Heart;
RX   MEDLINE=91057158; PubMed=2173832; DOI=10.1093/nar/18.21.6454;
RA   Grossman L.I., Akamatsu M.;
RT   "Nucleotide sequence of a mouse cDNA for subunit IV of cytochrome c
RT   oxidase.";
RL   Nucleic Acids Res. 18:6454-6454(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   MEDLINE=91378465; PubMed=1654830; DOI=10.1016/0003-9861(91)90169-J;
RA   Carter R.S., Avadhani N.G.;
RT   "Cloning and characterization of the mouse cytochrome c oxidase
RT   subunit IV gene.";
RL   Arch. Biochem. Biophys. 288:97-106(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PROTEIN SEQUENCE OF 30-41; 43-60; 68-75; 84-95; 136-143 AND 160-169,
RP   AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: This protein is one of the nuclear-coded polypeptide
CC       chains of cytochrome c oxidase, the terminal oxidase in
CC       mitochondrial electron transport.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase IV family.
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DR   EMBL; X54691; CAA38507.1; -; mRNA.
DR   EMBL; M37831; AAB02139.1; -; Genomic_DNA.
DR   EMBL; M58034; AAB02139.1; JOINED; Genomic_DNA.
DR   EMBL; M37829; AAB02140.1; -; mRNA.
DR   EMBL; AK012583; BAB28333.1; -; mRNA.
DR   EMBL; AK019276; BAB31643.1; -; mRNA.
DR   EMBL; AK150447; BAE29569.1; -; mRNA.
DR   IPI; IPI00117978; -.
DR   PIR; S12142; S12142.
DR   RefSeq; NP_034071.1; NM_009941.2.
DR   UniGene; Mm.386758; -.
DR   ProteinModelPortal; P19783; -.
DR   SMR; P19783; 26-169.
DR   MINT; MINT-1860013; -.
DR   STRING; P19783; -.
DR   PhosphoSite; P19783; -.
DR   PRIDE; P19783; -.
DR   Ensembl; ENSMUST00000034276; ENSMUSP00000034276; ENSMUSG00000031818.
DR   GeneID; 12857; -.
DR   KEGG; mmu:12857; -.
DR   UCSC; uc009nrh.1; mouse.
DR   CTD; 12857; -.
DR   MGI; MGI:88473; Cox4i1.
DR   GeneTree; ENSGT00390000002407; -.
DR   HOGENOM; HBG717867; -.
DR   HOVERGEN; HBG051087; -.
DR   InParanoid; P19783; -.
DR   OMA; WSSLSID; -.
DR   OrthoDB; EOG48SGV7; -.
DR   PhylomeDB; P19783; -.
DR   NextBio; 282412; -.
DR   ArrayExpress; P19783; -.
DR   Bgee; P19783; -.
DR   CleanEx; MM_COX4I1; -.
DR   Genevestigator; P19783; -.
DR   GermOnline; ENSMUSG00000031818; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR   InterPro; IPR004203; Cyt_c_oxidase_su4.
DR   InterPro; IPR013288; Cyt_c_oxidase_su4_sub.
DR   Gene3D; G3DSA:1.10.442.10; COX4; 1.
DR   Pfam; PF02936; COX4; 1.
DR   PRINTS; PR01873; CYTCOXIDASE4.
DR   SUPFAM; SSF81406; COX4; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Transit peptide.
FT   TRANSIT       1     22       Mitochondrion.
FT   CHAIN        23    169       Cytochrome c oxidase subunit 4 isoform 1,
FT                                mitochondrial.
FT                                /FTId=PRO_0000006085.
FT   MOD_RES      60     60       N6-acetyllysine (By similarity).
FT   CONFLICT    140    141       MQ -> IE (in Ref. 2; AAB02139/AAB02140).
SQ   SEQUENCE   169 AA;  19530 MW;  D30B1DBBE14FDBEA CRC64;
     MLASRALSLI GKRAISTSVC LRAHGSVVKS EDYAFPTYAD RRDYPLPDVA HVTMLSASQK
     ALKEKEKADW SSLSRDEKVQ LYRIQFNESF AEMNRGTNEW KTVVGMAMFF IGFTALVLIW
     EKSYVYGPIP HTFDRDWVAM QTKRMLDMKA NPIQGFSAKW DYDKNEWKK
//
ID   LSP1_MOUSE              Reviewed;         330 AA.
AC   P19973; A2A6J5; A2A6J6; P97339; Q04950; Q62022; Q62023; Q62024;
AC   Q8CD28; Q99L65;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   08-MAR-2011, entry version 108.
DE   RecName: Full=Lymphocyte-specific protein 1;
DE   AltName: Full=52 kDa phosphoprotein;
DE            Short=pp52;
DE   AltName: Full=Lymphocyte-specific antigen WP34;
DE   AltName: Full=S37 protein;
GN   Name=Lsp1; Synonyms=Pp52, S37, Wp34;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC   STRAIN=BALB/c;
RX   MEDLINE=89035543; PubMed=3263441;
RA   Jongstra J., Tidmarsh G.F., Jongstra-Bilen J., Davis M.M.;
RT   "A new lymphocyte-specific gene which encodes a putative Ca2+-binding
RT   protein is not expressed in transformed T lymphocyte lines.";
RL   J. Immunol. 141:3999-4004(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   MEDLINE=93107706; PubMed=8417117;
RA   Gimble J.M., Dorheim M.-A., Youkhana K., Hudson J., Nead M., Gilly M.,
RA   Wood W.J. Jr., Hermanson G.G., Kuehl M., Wall R., Kincade P.W.;
RT   "Alternatively spliced pp52 mRNA in nonlymphoid stromal cells.";
RL   J. Immunol. 150:115-121(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c;
RX   MEDLINE=95021322; PubMed=7935501; DOI=10.1016/0161-5890(94)90026-4;
RA   Jongstra J., Ittel M.E., Iscove N.N., Brady G.;
RT   "The LSP1 gene is expressed in cultured normal and transformed mouse
RT   macrophages.";
RL   Mol. Immunol. 31:1125-1131(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PHOSPHORYLATION.
RC   STRAIN=ICR; TISSUE=Thymus;
RX   MEDLINE=95293928; PubMed=7775393;
RA   Matsumoto N., Kojima S., Osawa T., Toyoshima S.;
RT   "Protein kinase C phosphorylates p50 LSP1 and induces translocation of
RT   p50 LSP1 in T lymphocytes.";
RL   J. Biochem. 117:222-229(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING.
RC   STRAIN=ICR; TISSUE=Thymus;
RX   MEDLINE=96015175; PubMed=8537319;
RA   Matsumoto N., Kita K., Kojima S., Yamamoto K., Irimura T., Miyagi M.,
RA   Tsunasawa S., Toyoshima S.;
RT   "Lymphocyte isoforms of mouse p50 LSP1, which are phosphorylated in
RT   mitogen-activated T cells, are formed through alternative splicing and
RT   phosphorylation.";
RL   J. Biochem. 118:237-243(1995).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-124 (ISOFORMS 1 AND 2),
RP   AND ALTERNATIVE SPLICING.
RC   STRAIN=BALB/c; TISSUE=Leukocyte, and Stromal cell;
RX   MEDLINE=96435912; PubMed=8838798; DOI=10.1006/geno.1996.0129;
RA   Thompson A.A., Omori S.A., Gilly M.J., May W., Gordon M.S.,
RA   Wood W.J. Jr., Miyoshi E., Malone C.S., Gimble J., Denny C.T.,
RA   Wall R.;
RT   "Alternatively spliced exons encode the tissue-specific 5' termini of
RT   leukocyte pp52 and stromal cell S37 mRNA isoforms.";
RL   Genomics 32:352-357(1996).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-127 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [10]
RP   PROTEIN SEQUENCE OF 55-81; 131-144; 211-229; 238-255 AND 311-330, AND
RP   PHOSPHORYLATION.
RC   TISSUE=T-cell;
RX   PubMed=8340356;
RA   Matsumoto N., Toyoshima S., Osawa T.;
RT   "Characterization of the 50 kDa protein phosphorylated in concanavalin
RT   A-stimulated mouse T cells.";
RL   J. Biochem. 113:630-636(1993).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-166 AND SER-168, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [13]
RP   PHOSPHORYLATION AT SER-243 BY MAPKAPK2, MUTAGENESIS OF SER-195 AND
RP   SER-243, AND FUNCTION.
RX   PubMed=17481585; DOI=10.1016/j.bbrc.2007.04.104;
RA   Wu Y., Zhan L., Ai Y., Hannigan M., Gaestel M., Huang C.-K.,
RA   Madri J.A.;
RT   "MAPKAPK2-mediated LSP1 phosphorylation and FMLP-induced neutrophil
RT   polarization.";
RL   Biochem. Biophys. Res. Commun. 358:170-175(2007).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-166 AND SER-168, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-166; SER-168 AND
RP   SER-243, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May play a role in mediating neutrophil activation and
CC       chemotaxis.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P19973-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P19973-2; Sequence=VSP_004313;
CC         Note=Ref.8 (AAB37543) sequence is in conflict in position:
CC         16:L->Q;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is expressed in normal mouse B and
CC       T-lymphocytes and in transformed B-cells but not (or in smaller
CC       amounts) in nine T-lymphoma lines tested. Isoform 2 is expressed
CC       in non-lymphoid cell lines (myocytes, stromal cells, fibroblasts).
CC   -!- PTM: Phosphorylated by casein kinase II, protein kinase C and
CC       MAPKAPK2. Phosphorylation by PKC induces translocation from
CC       membrane to cytoplasm. Phosphorylation by MAPKAPK2 may regulate
CC       neutrophil chemotaxis.
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DR   EMBL; M90316; AAA65108.1; -; mRNA.
DR   EMBL; S74179; AAB32257.1; -; mRNA.
DR   EMBL; M89956; AAB48537.1; -; mRNA.
DR   EMBL; D49691; BAA08541.1; -; mRNA.
DR   EMBL; AL603651; CAM23282.1; -; Genomic_DNA.
DR   EMBL; AL603651; CAM23283.1; -; Genomic_DNA.
DR   EMBL; BC003796; AAH03796.1; -; mRNA.
DR   EMBL; U30942; AAB37542.1; -; Genomic_DNA.
DR   EMBL; U30939; AAB37542.1; JOINED; Genomic_DNA.
DR   EMBL; U30941; AAB37542.1; JOINED; Genomic_DNA.
DR   EMBL; U30942; AAB37543.1; -; Genomic_DNA.
DR   EMBL; U30940; AAB37543.1; JOINED; Genomic_DNA.
DR   EMBL; U30941; AAB37543.1; JOINED; Genomic_DNA.
DR   EMBL; AK031587; BAC27463.1; -; mRNA.
DR   IPI; IPI00313672; -.
DR   IPI; IPI00331430; -.
DR   PIR; A30533; A30533.
DR   PIR; A46521; A46521.
DR   RefSeq; NP_001129543.1; NM_001136071.1.
DR   RefSeq; NP_062264.1; NM_019391.2.
DR   UniGene; Mm.234003; -.
DR   STRING; P19973; -.
DR   PhosphoSite; P19973; -.
DR   PRIDE; P19973; -.
DR   Ensembl; ENSMUST00000018963; ENSMUSP00000018963; ENSMUSG00000018819.
DR   Ensembl; ENSMUST00000105968; ENSMUSP00000101588; ENSMUSG00000018819.
DR   GeneID; 16985; -.
DR   KEGG; mmu:16985; -.
DR   UCSC; uc009knb.1; mouse.
DR   UCSC; uc009knf.1; mouse.
DR   CTD; 16985; -.
DR   MGI; MGI:96832; Lsp1.
DR   GeneTree; ENSGT00440000038768; -.
DR   HOVERGEN; HBG001610; -.
DR   InParanoid; P19973; -.
DR   OMA; ACKDIVA; -.
DR   OrthoDB; EOG4NKBW0; -.
DR   ArrayExpress; P19973; -.
DR   Bgee; P19973; -.
DR   CleanEx; MM_LSP1; -.
DR   Genevestigator; P19973; -.
DR   GermOnline; ENSMUSG00000018819; Mus musculus.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; TAS:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; TAS:MGI.
DR   GO; GO:0006935; P:chemotaxis; IMP:MGI.
DR   GO; GO:0007010; P:cytoskeleton organization; TAS:MGI.
DR   GO; GO:0006952; P:defense response; IMP:MGI.
DR   InterPro; IPR006018; Caldesmon_LSP.
DR   InterPro; IPR002211; Lymphspecific.
DR   PANTHER; PTHR12060; Lymphspecific; 1.
DR   Pfam; PF02029; Caldesmon; 1.
DR   PRINTS; PR01083; LYMPHSPCIFIC.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell membrane;
KW   Direct protein sequencing; Membrane; Phosphoprotein.
FT   CHAIN         1    330       Lymphocyte-specific protein 1.
FT                                /FTId=PRO_0000084504.
FT   MOD_RES      77     77       Phosphoserine; by CK2 (Potential).
FT   MOD_RES      78     78       Phosphoserine; by CK2 (Potential).
FT   MOD_RES      90     90       Phosphoserine.
FT   MOD_RES     166    166       Phosphothreonine.
FT   MOD_RES     168    168       Phosphoserine.
FT   MOD_RES     180    180       Phosphoserine (By similarity).
FT   MOD_RES     243    243       Phosphoserine; by MAPKAPK2.
FT   MOD_RES     318    318       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1     23       MAEAAIDPRCEEQEELHAEDSEG -> MNGPALLRRNASKR
FT                                GLEKLLR (in isoform 2).
FT                                /FTId=VSP_004313.
FT   MUTAGEN     195    195       S->A: No effect on phosphorylation by
FT                                PKC, PKA, MAPKAPK2 and CaMK2.
FT   MUTAGEN     243    243       S->A: Complete loss of phosphorylation by
FT                                MAPKAPK2, partial loss of phosphorylation
FT                                by PKA, no effect on phosphorylation by
FT                                PKC and CaMK2.
FT   MUTAGEN     243    243       S->E: Complete loss of phosphorylation by
FT                                MAPKAPK2, partial loss of phosphorylation
FT                                by PKA, no effect on phosphorylation by
FT                                PKC and CaMK2.
FT   CONFLICT    125    127       SSH -> RQV (in Ref. 9; BAC27463).
FT   CONFLICT    155    156       AE -> PK (in Ref. 1).
FT   CONFLICT    158    163       Missing (in Ref. 7; AAH03796).
FT   CONFLICT    160    160       I -> T (in Ref. 1).
FT   CONFLICT    168    168       S -> N (in Ref. 1).
FT   CONFLICT    253    253       S -> G (in Ref. 1).
FT   CONFLICT    283    283       S -> T (in Ref. 4 and 5).
SQ   SEQUENCE   330 AA;  36714 MW;  CCC27150F02859FB CRC64;
     MAEAAIDPRC EEQEELHAED SEGLTTQWRE EDEEEAAREQ RQRERERQLQ DQDKDKEDDG
     GHSLEQPGQQ TLISLKSSEL DEDEGFGDWS QKPEPRQQFW GNEGTAEGTE PSQSERPEEK
     QTEESSHQAK VHLEESNLSY REPDPEDAVG GSGEAEEHLI RHQVRTPSPL ALEDTVELSS
     PPLSPTTKLA DRTESLNRSI KKSNSVKKSQ PTLPISTIDE RLQQYTQATE SSGRTPKLSR
     QPSIELPSMA VASTKTLWET GEVQSQSASK TPSCQDIVAG DMSKKSLWEQ KGGSKISSTI
     KSTPSGKRYK FVATGHGKYE KVLVDEGSAP
//
ID   GRP78_MOUSE             Reviewed;         655 AA.
AC   P20029; O35642; Q3UFF2; Q61630;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 3.
DT   08-MAR-2011, entry version 118.
DE   RecName: Full=78 kDa glucose-regulated protein;
DE            Short=GRP-78;
DE   AltName: Full=Heat shock 70 kDa protein 5;
DE   AltName: Full=Immunoglobulin heavy chain-binding protein;
DE            Short=BiP;
DE   Flags: Precursor;
GN   Name=Hspa5; Synonyms=Grp78;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=88176922; PubMed=2895472; DOI=10.1073/pnas.85.7.2250;
RA   Haas I.G., Meo T.;
RT   "cDNA cloning of the immunoglobulin heavy chain binding protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:2250-2254(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 20-46.
RX   MEDLINE=90130686; PubMed=2559088;
RA   Kozutsumi Y., Normington K., Press E., Slaughter C., Sambrook J.,
RA   Gething M.J.;
RT   "Identification of immunoglobulin heavy chain binding protein as
RT   glucose-regulated protein 78 on the basis of amino acid sequence,
RT   immunological cross-reactivity, and functional activity.";
RL   J. Cell Sci. Suppl. 11:115-137(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=96216731; PubMed=8645260; DOI=10.1006/bbrc.1996.0313;
RA   Kajiwara K., Nagawawa H., Shimizu-Nishikawa K., Ookura T., Kimura M.,
RA   Sugaya E.;
RT   "Molecular characterization of seizure-related genes isolated by
RT   differential screening.";
RL   Biochem. Biophys. Res. Commun. 219:795-799(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RC   STRAIN=C3B10RF1; TISSUE=Liver;
RX   MEDLINE=95331621; PubMed=7607546; DOI=10.1016/0378-1119(95)00083-I;
RA   Tillman J.B., Mote P.L., Walford R.L., Spindler S.R.;
RT   "Structure and regulation of the mouse GRP78 (BiP) promoter by glucose
RT   and calcium ionophore.";
RL   Gene 158:225-229(1995).
RN   [7]
RP   PROTEIN SEQUENCE OF 20-36.
RC   TISSUE=Fibroblast;
RX   MEDLINE=95009907; PubMed=7523108; DOI=10.1002/elps.11501501101;
RA   Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.;
RT   "Separation and sequencing of familiar and novel murine proteins using
RT   preparative two-dimensional gel electrophoresis.";
RL   Electrophoresis 15:735-745(1994).
RN   [8]
RP   PROTEIN SEQUENCE OF 51-75; 140-153; 156-164; 166-182; 187-215;
RP   308-337; 354-368; 449-493; 525-541 AND 623-634, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Friebe K., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 488-655.
RX   MEDLINE=90060818; PubMed=2583523; DOI=10.1016/0378-1119(89)90054-1;
RA   Parfett C.L.J., Hofbauer R., Brudzynski K., Edwards D.R.,
RA   Denhardt D.T.;
RT   "Differential screening of a cDNA library with cDNA probes amplified
RT   in a heterologous host: isolation of murine GRP78 (BiP) and other
RT   serum-regulated low-abundance mRNAs.";
RL   Gene 82:291-303(1989).
RN   [10]
RP   COMPONENT OF A CHAPERONE COMPLEX.
RX   PubMed=12475965; DOI=10.1091/mbc.E02-05-0311;
RA   Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
RT   "A subset of chaperones and folding enzymes form multiprotein
RT   complexes in endoplasmic reticulum to bind nascent proteins.";
RL   Mol. Biol. Cell 13:4456-4469(2002).
RN   [11]
RP   INTERACTION WITH DNAJC1.
RX   PubMed=12065409; DOI=10.1093/emboj/cdf315;
RA   Dudek J., Volkmer J., Bies C., Guth S., Mueller A., Lerner M.,
RA   Feick P., Schaefer K.-H., Morgenstern E., Hennessy F., Blatch G.L.,
RA   Janoscheck K., Heim N., Scholtes P., Frien M., Nastainczyk W.,
RA   Zimmermann R.;
RT   "A novel type of co-chaperone mediates transmembrane recruitment of
RT   DnaK-like chaperones to ribosomes.";
RL   EMBO J. 21:2958-2967(2002).
RN   [12]
RP   NITRATION [LARGE SCALE ANALYSIS] AT TYR-161, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16800626; DOI=10.1021/bi060474w;
RA   Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
RA   Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
RA   Squier T.C., Bigelow D.J.;
RT   "Endogenously nitrated proteins in mouse brain: links to
RT   neurodegenerative disease.";
RL   Biochemistry 45:8009-8022(2006).
RN   [13]
RP   IDENTIFICATION IN AN EIF2 COMPLEX WITH EIF2S1; EIF2S2; CELF1; CALR;
RP   CALR3 AND HSP90B1.
RX   PubMed=16931514; DOI=10.1074/jbc.M605701200;
RA   Timchenko L.T., Salisbury E., Wang G.-L., Nguyen H., Albrecht J.H.,
RA   Hershey J.W., Timchenko N.A.;
RT   "Age-specific CUGBP1-eIF2 complex increases translation of
RT   CCAAT/enhancer-binding protein beta in old liver.";
RL   J. Biol. Chem. 281:32806-32819(2006).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-650, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-167 AND SER-572, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RA   Lubec G., Kang S.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Probably plays a role in facilitating the assembly of
CC       multimeric protein complexes inside the ER, AND MASS SPECTROMETRY.
CC   -!- SUBUNIT: Interacts with TMEM132A and TRIM21. May form a complex
CC       with ERLEC1, OS9, SEL1L and SYVN1 (By similarity). Component of an
CC       EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3,
CC       EIF2S1, EIF2S2, HSP90B1 and HSPA5. Part a large chaperone
CC       multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU,
CC       PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts
CC       of ERP29, but not, or at very low levels, CALR nor CANX. Interacts
CC       with DNAJC1 (via J domain).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Melanosome (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
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DR   EMBL; AJ002387; CAA05361.1; -; mRNA.
DR   EMBL; M19351; AAA37315.1; -; mRNA.
DR   EMBL; D78645; BAA11462.1; -; mRNA.
DR   EMBL; AK076079; BAC36166.1; -; mRNA.
DR   EMBL; AK146647; BAE27328.1; -; mRNA.
DR   EMBL; AK148539; BAE28609.1; -; mRNA.
DR   EMBL; AK151647; BAE30576.1; -; mRNA.
DR   EMBL; AK152020; BAE30882.1; -; mRNA.
DR   EMBL; AK166739; BAE38982.1; -; mRNA.
DR   EMBL; AK169034; BAE40825.1; -; mRNA.
DR   EMBL; BC050927; AAH50927.1; -; mRNA.
DR   EMBL; U16277; AAA76734.1; -; Genomic_DNA.
DR   EMBL; M30779; AAA37742.1; -; mRNA.
DR   IPI; IPI00319992; -.
DR   PIR; A37048; A37048.
DR   RefSeq; NP_001156906.1; NM_001163434.1.
DR   RefSeq; NP_071705.3; NM_022310.3.
DR   UniGene; Mm.330160; -.
DR   ProteinModelPortal; P20029; -.
DR   SMR; P20029; 28-641.
DR   DIP; DIP-32341N; -.
DR   MINT; MINT-1177274; -.
DR   STRING; P20029; -.
DR   PhosphoSite; P20029; -.
DR   SWISS-2DPAGE; P20029; -.
DR   COMPLUYEAST-2DPAGE; P20029; -.
DR   REPRODUCTION-2DPAGE; IPI00319992; -.
DR   REPRODUCTION-2DPAGE; P20029; -.
DR   UCD-2DPAGE; P20029; -.
DR   PRIDE; P20029; -.
DR   Ensembl; ENSMUST00000028222; ENSMUSP00000028222; ENSMUSG00000026864.
DR   Ensembl; ENSMUST00000100171; ENSMUSP00000097747; ENSMUSG00000026864.
DR   GeneID; 14828; -.
DR   KEGG; mmu:14828; -.
DR   UCSC; uc008jis.1; mouse.
DR   CTD; 14828; -.
DR   MGI; MGI:95835; Hspa5.
DR   HOGENOM; HBG334976; -.
DR   HOVERGEN; HBG051845; -.
DR   InParanoid; P20029; -.
DR   OMA; KNSKPHI; -.
DR   OrthoDB; EOG444KJV; -.
DR   PhylomeDB; P20029; -.
DR   ArrayExpress; P20029; -.
DR   Bgee; P20029; -.
DR   CleanEx; MM_HSPA5; -.
DR   Genevestigator; P20029; -.
DR   GermOnline; ENSMUSG00000026864; Mus musculus.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:BHF-UCL.
DR   GO; GO:0005576; C:extracellular region; EXP:Reactome.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0051787; F:misfolded protein binding; IDA:BHF-UCL.
DR   GO; GO:0043022; F:ribosome binding; IDA:MGI.
DR   GO; GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; IMP:BHF-UCL.
DR   GO; GO:0021680; P:cerebellar Purkinje cell layer development; IMP:BHF-UCL.
DR   GO; GO:0021589; P:cerebellum structural organization; IMP:BHF-UCL.
DR   GO; GO:0006983; P:ER overload response; IDA:MGI.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IGI:MGI.
DR   GO; GO:0040019; P:positive regulation of embryonic development; TAS:BHF-UCL.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; IMP:BHF-UCL.
DR   GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IDA:BHF-UCL.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR001023; Hsp70.
DR   InterPro; IPR013126; Hsp_70.
DR   PANTHER; PTHR19375; Hsp70; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Direct protein sequencing;
KW   Endoplasmic reticulum; Nitration; Nucleotide-binding; Phosphoprotein;
KW   Signal.
FT   SIGNAL        1     19
FT   CHAIN        20    655       78 kDa glucose-regulated protein.
FT                                /FTId=PRO_0000013568.
FT   MOTIF       652    655       Prevents secretion from ER.
FT   MOD_RES     161    161       Nitrated tyrosine.
FT   MOD_RES     167    167       Phosphothreonine.
FT   MOD_RES     269    269       N6-acetyllysine (By similarity).
FT   MOD_RES     467    467       Phosphotyrosine (By similarity).
FT   MOD_RES     572    572       Phosphoserine.
FT   MOD_RES     650    650       Phosphoserine.
FT   CONFLICT     43     43       V -> F (in Ref. 3; BAA11462).
FT   CONFLICT    245    245       V -> W (in Ref. 3; BAA11462).
FT   CONFLICT    329    329       E -> G (in Ref. 3; BAA11462).
FT   CONFLICT    361    361       V -> A (in Ref. 3; BAA11462).
FT   CONFLICT    474    474       T -> R (in Ref. 1; CAA05361).
FT   CONFLICT    591    591       D -> G (in Ref. 9; AAA37742).
FT   CONFLICT    596    596       E -> K (in Ref. 2; AA sequence).
SQ   SEQUENCE   655 AA;  72422 MW;  AFB795D15E20FAC2 CRC64;
     MMKFTVVAAA LLLLGAVRAE EEDKKEDVGT VVGIDLGTTY SCVGVFKNGR VEIIANDQGN
     RITPSYVAFT PEGERLIGDA AKNQLTSNPE NTVFDAKRLI GRTWNDPSVQ QDIKFLPFKV
     VEKKTKPYIQ VDIGGGQTKT FAPEEISAMV LTKMKETAEA YLGKKVTHAV VTVPAYFNDA
     QRQATKDAGT IAGLNVMRII NEPTAAAIAY GLDKREGEKN ILVFDLGGGT FDVSLLTIDN
     GVFEVVATNG DTHLGGEDFD QRVMEHFIKL YKKKTGKDVR KDNRAVQKLR REVEKAKRAL
     SSQHQARIEI ESFFEGEDFS ETLTRAKFEE LNMDLFRSTM KPVQKVLEDS DLKKSDIDEI
     VLVGGSTRIP KIQQLVKEFF NGKEPSRGIN PDEAVAYGAA VQAGVLSGDQ DTGDLVLLDV
     CPLTLGIETV GGVMTKLIPR NTVVPTKKSQ IFSTASDNQP TVTIKVYEGE RPLTKDNHLL
     GTFDLTGIPP APRGVPQIEV TFEIDVNGIL RVTAEDKGTG NKNKITITND QNRLTPEEIE
     RMVNDAEKFA EEDKKLKERI DTRNELESYA YSLKNQIGDK EKLGGKLSSE DKETMEKAVE
     EKIEWLESHQ DADIEDFKAK KKELEEIVQP IISKLYGSGG PPPTGEEDTS EKDEL
//
ID   HEXB_MOUSE              Reviewed;         536 AA.
AC   P20060;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Beta-hexosaminidase subunit beta;
DE            EC=3.2.1.52;
DE   AltName: Full=Beta-N-acetylhexosaminidase subunit beta;
DE            Short=Hexosaminidase subunit B;
DE   AltName: Full=N-acetyl-beta-glucosaminidase subunit beta;
DE   Flags: Precursor;
GN   Name=Hexb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=89005625; PubMed=2971567; DOI=10.1016/0014-5793(88)80199-6;
RA   Bapat B., Ethier M., Neote K., Mahuran D., Gravel R.A.;
RT   "Cloning and sequence analysis of a cDNA encoding the beta-subunit of
RT   mouse beta-hexosaminidase.";
RL   FEBS Lett. 237:191-195(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX   MEDLINE=95048337; PubMed=7959736; DOI=10.1006/geno.1994.1318;
RA   Yamanaka S., Johnson O.N., Norflus F., Boles D.J., Proia R.L.;
RT   "Structure and expression of the mouse beta-hexosaminidase genes, Hexa
RT   and Hexb.";
RL   Genomics 21:588-596(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=95002207; PubMed=7918686; DOI=10.1016/0925-4439(94)90110-4;
RA   Triggs-Raine B.L., Benoit G., Salo T.J., Trasler J.M., Gravel R.A.;
RT   "Characterization of the murine beta-hexosaminidase (HEXB) gene.";
RL   Biochim. Biophys. Acta 1227:79-86(1994).
CC   -!- FUNCTION: Responsible for the degradation of GM2 gangliosides, and
CC       a variety of other molecules containing terminal N-acetyl
CC       hexosamines, in the brain and other tissues.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing N-acetyl-
CC       D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
CC   -!- SUBCELLULAR LOCATION: Lysosome.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 20 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Y00964; CAA68781.1; -; mRNA.
DR   EMBL; U07633; AAA18776.1; -; mRNA.
DR   EMBL; U07049; AAA74738.1; -; Genomic_DNA.
DR   EMBL; U07036; AAA74738.1; JOINED; Genomic_DNA.
DR   EMBL; U07037; AAA74738.1; JOINED; Genomic_DNA.
DR   EMBL; U07038; AAA74738.1; JOINED; Genomic_DNA.
DR   EMBL; U07039; AAA74738.1; JOINED; Genomic_DNA.
DR   EMBL; U07040; AAA74738.1; JOINED; Genomic_DNA.
DR   EMBL; U07041; AAA74738.1; JOINED; Genomic_DNA.
DR   EMBL; U07042; AAA74738.1; JOINED; Genomic_DNA.
DR   EMBL; U07043; AAA74738.1; JOINED; Genomic_DNA.
DR   EMBL; U07044; AAA74738.1; JOINED; Genomic_DNA.
DR   EMBL; U07045; AAA74738.1; JOINED; Genomic_DNA.
DR   EMBL; U07046; AAA74738.1; JOINED; Genomic_DNA.
DR   EMBL; U07047; AAA74738.1; JOINED; Genomic_DNA.
DR   EMBL; U07048; AAA74738.1; JOINED; Genomic_DNA.
DR   EMBL; U07742; AAB60667.1; -; Genomic_DNA.
DR   EMBL; U07722; AAB60667.1; JOINED; Genomic_DNA.
DR   EMBL; U07723; AAB60667.1; JOINED; Genomic_DNA.
DR   EMBL; U07724; AAB60667.1; JOINED; Genomic_DNA.
DR   EMBL; U07725; AAB60667.1; JOINED; Genomic_DNA.
DR   EMBL; U07726; AAB60667.1; JOINED; Genomic_DNA.
DR   EMBL; U07727; AAB60667.1; JOINED; Genomic_DNA.
DR   EMBL; U07728; AAB60667.1; JOINED; Genomic_DNA.
DR   EMBL; U07737; AAB60667.1; JOINED; Genomic_DNA.
DR   EMBL; U07738; AAB60667.1; JOINED; Genomic_DNA.
DR   EMBL; U07739; AAB60667.1; JOINED; Genomic_DNA.
DR   EMBL; U07740; AAB60667.1; JOINED; Genomic_DNA.
DR   EMBL; U07741; AAB60667.1; JOINED; Genomic_DNA.
DR   IPI; IPI00115530; -.
DR   PIR; B54745; B54745.
DR   RefSeq; NP_034552.1; NM_010422.2.
DR   UniGene; Mm.27816; -.
DR   ProteinModelPortal; P20060; -.
DR   SMR; P20060; 33-532.
DR   STRING; P20060; -.
DR   CAZy; GH20; Glycoside Hydrolase Family 20.
DR   PRIDE; P20060; -.
DR   Ensembl; ENSMUST00000022169; ENSMUSP00000022169; ENSMUSG00000021665.
DR   GeneID; 15212; -.
DR   KEGG; mmu:15212; -.
DR   UCSC; uc007roc.1; mouse.
DR   CTD; 15212; -.
DR   MGI; MGI:96074; Hexb.
DR   eggNOG; roNOG12854; -.
DR   HOGENOM; HBG591688; -.
DR   HOVERGEN; HBG005961; -.
DR   InParanoid; P20060; -.
DR   OMA; PWYLDWI; -.
DR   OrthoDB; EOG42Z4Q7; -.
DR   PhylomeDB; P20060; -.
DR   BRENDA; 3.2.1.52; 244.
DR   NextBio; 287781; -.
DR   ArrayExpress; P20060; -.
DR   Bgee; P20060; -.
DR   CleanEx; MM_HEXB; -.
DR   Genevestigator; P20060; -.
DR   GermOnline; ENSMUSG00000021665; Mus musculus.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR   GO; GO:0005764; C:lysosome; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IGI:MGI.
DR   GO; GO:0044267; P:cellular protein metabolic process; IMP:MGI.
DR   GO; GO:0006689; P:ganglioside catabolic process; IMP:MGI.
DR   GO; GO:0030203; P:glycosaminoglycan metabolic process; IGI:MGI.
DR   GO; GO:0019915; P:lipid storage; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0007040; P:lysosome organization; IMP:MGI.
DR   GO; GO:0008049; P:male courtship behavior; IMP:MGI.
DR   GO; GO:0042552; P:myelination; IGI:MGI.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR   GO; GO:0009313; P:oligosaccharide catabolic process; IMP:MGI.
DR   GO; GO:0048477; P:oogenesis; IMP:MGI.
DR   GO; GO:0007341; P:penetration of zona pellucida; IMP:MGI.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IMP:MGI.
DR   GO; GO:0031323; P:regulation of cellular metabolic process; IMP:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; IGI:MGI.
DR   GO; GO:0001501; P:skeletal system development; IGI:MGI.
DR   InterPro; IPR015882; Acetylhexosaminidase_sua/b.
DR   InterPro; IPR001540; Glyco_hydro_20.
DR   InterPro; IPR015883; Glyco_hydro_20_cat-core.
DR   InterPro; IPR013781; Glyco_hydro_sg_catalytic.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Gene3D; G3DSA:3.20.20.80; Glyco_hydro_cat; 1.
DR   PANTHER; PTHR22600; Glyco_hydro_20; 1.
DR   Pfam; PF00728; Glyco_hydro_20; 1.
DR   Pfam; PF02838; Glyco_hydro_20b; 1.
DR   PRINTS; PR00738; GLHYDRLASE20.
DR   SUPFAM; SSF51445; Glyco_hydro_cat; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Lysosome;
KW   Signal.
FT   SIGNAL        1     31       Potential.
FT   CHAIN        32    536       Beta-hexosaminidase subunit beta.
FT                                /FTId=PRO_0000012006.
FT   ACT_SITE    334    334       Proton donor (By similarity).
FT   CARBOHYD     63     63       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    169    169       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    306    306       N-linked (GlcNAc...) (Potential).
FT   DISULFID     70    116       By similarity.
FT   DISULFID    288    339       By similarity.
FT   DISULFID    513    530       By similarity.
SQ   SEQUENCE   536 AA;  61116 MW;  579BBEEE9CB508BC CRC64;
     MPQSPRSAPG LLLLQALVSL VSLALVAPAR LQPALWPFPR SVQMFPRLLY ISAEDFSIDH
     SPNSTAGPSC SLLQEAFRRY YNYVFGFYKR HHGPARFRAE PQLQKLLVSI TLESECESFP
     SLSSDETYSL LVQEPVAVLK ANSVWGALRG LETFSQLVYQ DSFGTFTINE SSIADSPRFP
     HRGILIDTSR HFLPVKTILK TLDAMAFNKF NVLHWHIVDD QSFPYQSTTF PELSNKGSYS
     LSHVYTPNDV RMVLEYARLR GIRVIPEFDT PGHTQSWGKG QKNLLTPCYN QKTKTQVFGP
     VDPTVNTTYA FFNTFFKEIS SVFPDQFIHL GGDEVEFQCW ASNPNIQGFM KRKGFGSDFR
     RLESFYIKKI LEIISSLKKN SIVWQEVFDD KVELQPGTVV EVWKSEHYSY ELKQVTGSGF
     PAILSAPWYL DLISYGQDWK NYYKVEPLNF EGSEKQKQLV IGGEACLWGE FVDATNLTPR
     LWPRASAVGE RLWSPKTVTD LENAYKRLAV HRCRMVSRGI AAQPLYTGYC NYENKI
//
ID   VIME_MOUSE              Reviewed;         466 AA.
AC   P20152; O08704; Q8CCH1;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 121.
DE   RecName: Full=Vimentin;
GN   Name=Vim;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=89306653; PubMed=2744479; DOI=10.1016/0378-1119(89)90020-6;
RA   Wood L., Theriault N., Vogeli G.;
RT   "Vimentin cDNA clones covering the complete intermediate-filament
RT   protein are found in an EHS tumor cDNA library.";
RL   Gene 76:171-175(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Spleen;
RA   Podolin P.L., Prystowsky M.B.;
RL   Submitted (OCT-1990) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90220517; PubMed=2325630; DOI=10.1007/BF00280364;
RA   Hennekes H., Kuehn S., Traub P.;
RT   "Coding sequence and flanking regions of the mouse vimentin gene.";
RL   Mol. Gen. Genet. 221:33-36(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Smooth muscle;
RX   MEDLINE=90265604; PubMed=2140597;
RA   Capetanaki Y., Kuisk I., Rothblum K., Starnes S.;
RT   "Mouse vimentin: structural relationship to fos, jun, CREB and tpr.";
RL   Oncogene 5:645-655(1990).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Rauscher A.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-115.
RC   STRAIN=BALB/c;
RX   MEDLINE=96125204; PubMed=8543176; DOI=10.1016/0378-1119(95)00600-1;
RA   Nakamura N., Shida M., Hirayoshi K., Nagata K.;
RT   "Transcriptional regulation of the vimentin-encoding gene in mouse
RT   myeloid leukemia M1 cells.";
RL   Gene 166:281-286(1995).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 32-188.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [8]
RP   PROTEIN SEQUENCE OF 5-69, AND PHOSPHORYLATION AT SER-7; SER-9; SER-10;
RP   SER-21; SER-25; SER-26; SER-34; SER-39; SER-42; SER-47; SER-51 AND
RP   SER-66.
RC   TISSUE=Smooth muscle;
RX   MEDLINE=89302884; PubMed=2500966; DOI=10.1021/bi00433a035;
RA   Ando S., Tanabe K., Gonda Y., Sato C., Inagaki M.;
RT   "Domain- and sequence-specific phosphorylation of vimentin induces
RT   disassembly of the filament structure.";
RL   Biochemistry 28:2974-2979(1989).
RN   [9]
RP   PROTEIN SEQUENCE OF 72-91.
RC   TISSUE=Fibroblast;
RX   MEDLINE=95009907; PubMed=7523108; DOI=10.1002/elps.11501501101;
RA   Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.;
RT   "Separation and sequencing of familiar and novel murine proteins using
RT   preparative two-dimensional gel electrophoresis.";
RL   Electrophoresis 15:735-745(1994).
RN   [10]
RP   PHOSPHORYLATION AT SER-39 AND SER-83.
RX   MEDLINE=91222208; PubMed=1850997; DOI=10.1016/0006-291X(91)91658-Y;
RA   Ando S., Tokui T., Yamauchi T., Sugiura H., Tanabe K., Inagaki M.;
RT   "Evidence that Ser-82 is a unique phosphorylation site on vimentin for
RT   Ca2(+)-calmodulin-dependent protein kinase II.";
RL   Biochem. Biophys. Res. Commun. 175:955-962(1991).
RN   [11]
RP   INTERACTION WITH PLEC.
RX   PubMed=15128297; DOI=10.1111/j.1432-1033.2004.04095.x;
RA   Sevcik J., Urbanikova L., Kost'an J., Janda L., Wiche G.;
RT   "Actin-binding domain of mouse plectin. Crystal structure and binding
RT   to vimentin.";
RL   Eur. J. Biochem. 271:1873-1884(2004).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-73, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [13]
RP   INTERACTION WITH SYNM.
RX   PubMed=17356066; DOI=10.1242/jcs.03423;
RA   Jing R., Wilhelmsson U., Goodwill W., Li L., Pan Y., Pekny M.,
RA   Skalli O.;
RT   "Synemin is expressed in reactive astrocytes in neurotrauma and
RT   interacts differentially with vimentin and GFAP intermediate filament
RT   networks.";
RL   J. Cell Sci. 120:1267-1277(2007).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-53 AND TYR-61, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [15]
RP   INTERACTION WITH LGSN.
RX   PubMed=18178558; DOI=10.1074/jbc.M709144200;
RA   Wyatt K., Gao C., Tsai J.-Y., Fariss R.N., Ray S., Wistow G.;
RT   "A role for lengsin, a recruited enzyme, in terminal differentiation
RT   in the vertebrate lens.";
RL   J. Biol. Chem. 283:6607-6615(2008).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-72; SER-73;
RP   SER-144; SER-226; SER-430 AND SER-459, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-214, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-49; SER-56;
RP   SER-66; SER-419; SER-420; SER-430 AND SER-459, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Vimentins are class-III intermediate filaments found in
CC       various non-epithelial cells, especially mesenchymal cells.
CC   -!- SUBUNIT: Homopolymer. Interacts with SLC6A4 (By similarity).
CC       Interacts with LGSN and SYNM. Interacts (via rod region) with PLEC
CC       (via CH 1 domain).
CC   -!- INTERACTION:
CC       P35465:Pak1 (xeno); NbExp=2; IntAct=EBI-299269, EBI-444379;
CC       Q9R269:Ppl; NbExp=1; IntAct=EBI-299269, EBI-368293;
CC   -!- PTM: Phosphorylation by PKN1 inhibits the formation of filaments.
CC       Filament disassembly during mitosis is promoted by phosphorylation
CC       at Ser-55 as well as by nestin (By similarity). One of the most
CC       prominent phosphoproteins in various cells of mesenchymal origin.
CC       Phosphorylation is enhanced during cell division, at which time
CC       vimentin filaments are significantly reorganized.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M24849; AAA40555.1; -; mRNA.
DR   EMBL; X56397; CAA39807.1; -; mRNA.
DR   EMBL; M26251; AAA40556.1; -; mRNA.
DR   EMBL; Z22526; CAA80251.1; -; Genomic_DNA.
DR   EMBL; X51438; CAA35803.1; -; mRNA.
DR   EMBL; Y07738; CAA69019.1; -; Genomic_DNA.
DR   EMBL; AK033175; BAC28181.1; -; mRNA.
DR   EMBL; D50805; BAA19834.1; -; Genomic_DNA.
DR   IPI; IPI00227299; -.
DR   PIR; A43803; A43803.
DR   RefSeq; NP_035831.2; NM_011701.4.
DR   UniGene; Mm.268000; -.
DR   ProteinModelPortal; P20152; -.
DR   SMR; P20152; 101-138, 144-248, 263-406.
DR   DIP; DIP-188N; -.
DR   IntAct; P20152; 9.
DR   MINT; MINT-1202726; -.
DR   STRING; P20152; -.
DR   PhosphoSite; P20152; -.
DR   SWISS-2DPAGE; P20152; -.
DR   REPRODUCTION-2DPAGE; IPI00227299; -.
DR   UCD-2DPAGE; P20152; -.
DR   PRIDE; P20152; -.
DR   Ensembl; ENSMUST00000028062; ENSMUSP00000028062; ENSMUSG00000026728.
DR   GeneID; 22352; -.
DR   KEGG; mmu:22352; -.
DR   UCSC; uc008ikb.1; mouse.
DR   CTD; 22352; -.
DR   MGI; MGI:98932; Vim.
DR   HOGENOM; HBG715391; -.
DR   HOVERGEN; HBG013015; -.
DR   InParanoid; P20152; -.
DR   OMA; SPGGAYV; -.
DR   OrthoDB; EOG4GHZPD; -.
DR   PhylomeDB; P20152; -.
DR   NextBio; 302643; -.
DR   ArrayExpress; P20152; -.
DR   Bgee; P20152; -.
DR   CleanEx; MM_VIM; -.
DR   Genevestigator; P20152; -.
DR   GermOnline; ENSMUSG00000026728; Mus musculus.
DR   GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR   GO; GO:0045098; C:type III intermediate filament; TAS:MGI.
DR   GO; GO:0005212; F:structural constituent of eye lens; IDA:MGI.
DR   GO; GO:0045103; P:intermediate filament-based process; IMP:MGI.
DR   GO; GO:0070307; P:lens fiber cell development; IDA:MGI.
DR   InterPro; IPR016044; F.
DR   InterPro; IPR001664; IF.
DR   InterPro; IPR006821; Intermed_filament_DNA-bd.
DR   InterPro; IPR018039; Intermediate_filament_CS.
DR   PANTHER; PTHR23239; IF; 1.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF04732; Filament_head; 1.
DR   PROSITE; PS00226; IF; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Direct protein sequencing;
KW   Intermediate filament; Phosphoprotein.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    466       Vimentin.
FT                                /FTId=PRO_0000063756.
FT   REGION        2     95       Head.
FT   REGION       96    407       Rod.
FT   REGION       96    131       Coil 1A.
FT   REGION      132    153       Linker 1.
FT   REGION      154    245       Coil 1B.
FT   REGION      246    268       Linker 12.
FT   REGION      269    407       Coil 2.
FT   REGION      408    466       Tail.
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES       5      5       Phosphoserine (By similarity).
FT   MOD_RES       7      7       Phosphoserine; by PKA and PKC.
FT   MOD_RES       8      8       Phosphoserine (By similarity).
FT   MOD_RES       9      9       Phosphoserine; by PKC.
FT   MOD_RES      10     10       Phosphoserine; by PKC.
FT   MOD_RES      20     20       Phosphothreonine (By similarity).
FT   MOD_RES      21     21       Phosphoserine; by PKC.
FT   MOD_RES      25     25       Phosphoserine; by PKA and PKC.
FT   MOD_RES      26     26       Phosphoserine; by PKC.
FT   MOD_RES      29     29       Phosphoserine (By similarity).
FT   MOD_RES      33     33       Phosphothreonine (By similarity).
FT   MOD_RES      34     34       Phosphoserine; by PKC.
FT   MOD_RES      38     38       Phosphotyrosine (By similarity).
FT   MOD_RES      39     39       Phosphoserine; by CaMK2, PKA and PKC.
FT   MOD_RES      42     42       Phosphoserine; by PKC.
FT   MOD_RES      47     47       Phosphoserine; by PKA.
FT   MOD_RES      49     49       Phosphoserine.
FT   MOD_RES      51     51       Phosphoserine; by PKA and PKC.
FT   MOD_RES      53     53       Phosphotyrosine.
FT   MOD_RES      55     55       Phosphoserine (By similarity).
FT   MOD_RES      55     55       Phosphoserine; by CDK1.
FT   MOD_RES      56     56       Phosphoserine.
FT   MOD_RES      61     61       Phosphotyrosine.
FT   MOD_RES      66     66       Phosphoserine; by PKA and PKC.
FT   MOD_RES      72     72       Phosphoserine.
FT   MOD_RES      73     73       Phosphoserine.
FT   MOD_RES      83     83       Phosphoserine; by CaMK2.
FT   MOD_RES     104    104       N6-acetyllysine (By similarity).
FT   MOD_RES     117    117       Phosphotyrosine (By similarity).
FT   MOD_RES     120    120       N6-acetyllysine (By similarity).
FT   MOD_RES     139    139       N6-acetyllysine (By similarity).
FT   MOD_RES     144    144       Phosphoserine.
FT   MOD_RES     214    214       Phosphoserine.
FT   MOD_RES     226    226       Phosphoserine.
FT   MOD_RES     261    261       Phosphoserine (By similarity).
FT   MOD_RES     266    266       Phosphothreonine (By similarity).
FT   MOD_RES     292    292       N6-acetyllysine (By similarity).
FT   MOD_RES     299    299       Phosphoserine (By similarity).
FT   MOD_RES     373    373       N6-acetyllysine (By similarity).
FT   MOD_RES     402    402       N6-acetyllysine (By similarity).
FT   MOD_RES     409    409       Phosphoserine (By similarity).
FT   MOD_RES     412    412       Phosphoserine (By similarity).
FT   MOD_RES     419    419       Phosphoserine.
FT   MOD_RES     420    420       Phosphoserine.
FT   MOD_RES     430    430       Phosphoserine.
FT   MOD_RES     445    445       N6-acetyllysine (By similarity).
FT   MOD_RES     446    446       Phosphothreonine (By similarity).
FT   MOD_RES     458    458       Phosphothreonine (By similarity).
FT   MOD_RES     459    459       Phosphoserine.
FT   CONFLICT     70     70       L -> S (in Ref. 6; BAA19834).
FT   CONFLICT    110    115       LNDRFA -> ILLAEL (in Ref. 6; BAA19834).
FT   CONFLICT    156    157       EL -> DV (in Ref. 4; CAA35803).
FT   CONFLICT    164    164       L -> F (in Ref. 2; CAA39807).
FT   CONFLICT    338    338       E -> V (in Ref. 4; CAA35803).
FT   CONFLICT    374    374       E -> D (in Ref. 1; AAA40555).
SQ   SEQUENCE   466 AA;  53688 MW;  A94EECEA6D70C899 CRC64;
     MSTRSVSSSS YRRMFGGSGT SSRPSSNRSY VTTSTRTYSL GSALRPSTSR SLYSSSPGGA
     YVTRSSAVRL RSSVPGVRLL QDSVDFSLAD AINTEFKNTR TNEKVELQEL NDRFANYIDK
     VRFLEQQNKI LLAELEQLKG QGKSRLGDLY EEEMRELRRQ VDQLTNDKAR VEVERDNLAE
     DIMRLREKLQ EEMLQREEAE STLQSFRQDV DNASLARLDL ERKVESLQEE IAFLKKLHDE
     EIQELQAQIQ EQHVQIDVDV SKPDLTAALR DVRQQYESVA AKNLQEAEEW YKSKFADLSE
     AANRNNDALR QAKQESNEYR RQVQSLTCEV DALKGTNESL ERQMREMEEN FALEAANYQD
     TIGRLQDEIQ NMKEEMARHL REYQDLLNVK MALDIEIATY RKLLEGEESR ISLPLPTFSS
     LNLRETNLES LPLVDTHSKR TLLIKTVETR DGQVINETSQ HHDDLE
//
ID   TF_MOUSE                Reviewed;         294 AA.
AC   P20352;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 2.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Tissue factor;
DE            Short=TF;
DE   AltName: Full=Coagulation factor III;
DE   AltName: CD_antigen=CD142;
DE   Flags: Precursor;
GN   Name=F3; Synonyms=Cf-3, Cf3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=91093171; PubMed=1985911;
RA   Ranganathan G., Blatti S.P., Subramaniam M., Fass D.N., Maihle N.J.,
RA   Getz M.J.;
RT   "Cloning of murine tissue factor and regulation of gene expression by
RT   transforming growth factor type beta 1.";
RL   J. Biol. Chem. 266:496-501(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=89343974; PubMed=2761539;
RA   Hartzell S., Ryder K., Lanahan A., Lau L.F., Nathans D.;
RT   "A growth factor-responsive gene of murine BALB/c 3T3 cells encodes a
RT   protein homologous to human tissue factor.";
RL   Mol. Cell. Biol. 9:2567-2573(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-37 AND ASN-57, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
CC   -!- FUNCTION: Initiates blood coagulation by forming a complex with
CC       circulating factor VII or VIIa. The [TF:VIIa] complex activates
CC       factors IX or X by specific limited protolysis. TF plays a role in
CC       normal hemostasis by initiating the cell-surface assembly and
CC       propagation of the coagulation protease cascade.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the tissue factor family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M57896; AAA63400.1; -; mRNA.
DR   EMBL; M26071; AAA40414.1; -; mRNA.
DR   EMBL; BC016397; AAH16397.1; -; mRNA.
DR   IPI; IPI00118069; -.
DR   PIR; A32318; KFMS3.
DR   RefSeq; NP_034301.3; NM_010171.3.
DR   UniGene; Mm.273188; -.
DR   ProteinModelPortal; P20352; -.
DR   SMR; P20352; 35-244.
DR   STRING; P20352; -.
DR   PhosphoSite; P20352; -.
DR   PRIDE; P20352; -.
DR   Ensembl; ENSMUST00000029771; ENSMUSP00000029771; ENSMUSG00000028128.
DR   GeneID; 14066; -.
DR   KEGG; mmu:14066; -.
DR   CTD; 14066; -.
DR   MGI; MGI:88381; F3.
DR   eggNOG; roNOG06715; -.
DR   HOGENOM; HBG445882; -.
DR   HOVERGEN; HBG005051; -.
DR   InParanoid; P20352; -.
DR   ArrayExpress; P20352; -.
DR   Bgee; P20352; -.
DR   CleanEx; MM_F3; -.
DR   Genevestigator; P20352; -.
DR   GermOnline; ENSMUSG00000028128; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007596; P:blood coagulation; TAS:MGI.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR015373; Interferon_alpha/beta_rcpt_bsu.
DR   InterPro; IPR016354; Tissue_fac/coagulation_fac-3.
DR   InterPro; IPR001187; Tissue_factor.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Pfam; PF09294; Interfer-bind; 1.
DR   PIRSF; PIRSF002498; Tissue_factor_3; 1.
DR   PRINTS; PR00346; TISSUEFACTOR.
DR   SUPFAM; SSF49265; FN_III-like; 2.
DR   PROSITE; PS00621; TISSUE_FACTOR; 1.
PE   1: Evidence at protein level;
KW   Blood coagulation; Disulfide bond; Glycoprotein; Lipoprotein;
KW   Membrane; Palmitate; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     28
FT   CHAIN        29    294       Tissue factor.
FT                                /FTId=PRO_0000033639.
FT   TOPO_DOM     29    251       Extracellular (Potential).
FT   TRANSMEM    252    274       Helical; (Potential).
FT   TOPO_DOM    275    294       Cytoplasmic (Potential).
FT   MOTIF       245    247       WKS motif.
FT   LIPID       275    275       S-palmitoyl cysteine (By similarity).
FT   CARBOHYD     37     37       N-linked (GlcNAc...).
FT   CARBOHYD     57     57       N-linked (GlcNAc...).
FT   CARBOHYD    169    169       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    200    200       N-linked (GlcNAc...) (Potential).
FT   DISULFID     75     83       By similarity.
FT   DISULFID    218    241       By similarity.
FT   CONFLICT     26     26       I -> T (in Ref. 2; AAA40414).
SQ   SEQUENCE   294 AA;  32935 MW;  A306101293C31FA0 CRC64;
     MAILVRPRLL AALAPTFLGC LLLQVIAGAG IPEKAFNLTW ISTDFKTILE WQPKPTNYTY
     TVQISDRSRN WKNKCFSTTD TECDLTDEIV KDVTWAYEAK VLSVPRRNSV HGDGDQLVIH
     GEEPPFTNAP KFLPYRDTNL GQPVIQQFEQ DGRKLNVVVK DSLTLVRKNG TFLTLRQVFG
     KDLGYIITYR KGSSTGKKTN ITNTNEFSID VEEGVSYCFF VQAMIFSRKT NQNSPGSSTV
     CTEQWKSFLG ETLIIVGAVV LLATIFIILL SISLCKRRKN RAGQKGKNTP SRLA
//
ID   MAP2_MOUSE              Reviewed;        1828 AA.
AC   P20357;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Microtubule-associated protein 2;
DE            Short=MAP-2;
GN   Name=Map2; Synonyms=Mtap2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=89083571; PubMed=3205744; DOI=10.1093/nar/16.23.11369;
RA   Wang D., Lewis S.A., Cowan N.J.;
RT   "Complete sequence of a cDNA encoding mouse MAP2.";
RL   Nucleic Acids Res. 16:11369-11370(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=89043973; PubMed=3142041; DOI=10.1126/science.3142041;
RA   Lewis S.A., Wang D., Cowan N.J.;
RT   "Microtubule-associated protein MAP2 shares a microtubule binding
RT   motif with tau protein.";
RL   Science 242:936-939(1988).
RN   [3]
RP   PROTEIN SEQUENCE OF 94-107; 583-597; 909-920; 989-1004; 1159-1174;
RP   1403-1414 AND 1511-1538, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-626; SER-655;
RP   SER-730; SER-737; SER-823; SER-1352; THR-1358; SER-1595; THR-1598;
RP   THR-1606; THR-1609 AND SER-1615, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-746; SER-1161; SER-1352;
RP   THR-1358; SER-1539 AND SER-1783, AND MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1352; THR-1358;
RP   SER-1426; THR-1445; SER-1485; SER-1539; THR-1609 AND THR-1650, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-823; SER-1352;
RP   THR-1358; THR-1599; THR-1609; SER-1612; THR-1620 AND SER-1783, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1791, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1650; THR-1657 AND
RP   SER-1783, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: The exact function of MAP2 is unknown but MAPs may
CC       stabilize the microtubules against depolymerization. They also
CC       seem to have a stiffening effect on microtubules.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (Probable).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 3 Tau/MAP repeats.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M21041; AAA39490.1; -; mRNA.
DR   IPI; IPI00118075; -.
DR   PIR; A40115; A40115.
DR   UniGene; Mm.256966; -.
DR   MINT; MINT-4101182; -.
DR   STRING; P20357; -.
DR   PhosphoSite; P20357; -.
DR   PRIDE; P20357; -.
DR   Ensembl; ENSMUST00000024639; ENSMUSP00000024639; ENSMUSG00000015222.
DR   Ensembl; ENSMUST00000114013; ENSMUSP00000109646; ENSMUSG00000015222.
DR   UCSC; uc007bhz.1; mouse.
DR   MGI; MGI:97175; Mtap2.
DR   eggNOG; roNOG04591; -.
DR   HOGENOM; HBG281882; -.
DR   HOVERGEN; HBG006322; -.
DR   InParanoid; P20357; -.
DR   OrthoDB; EOG4QVCB3; -.
DR   ArrayExpress; P20357; -.
DR   Bgee; P20357; -.
DR   CleanEx; MM_MTAP2; -.
DR   Genevestigator; P20357; -.
DR   GermOnline; ENSMUSG00000015222; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0043198; C:dendritic shaft; IDA:MGI.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005875; C:microtubule associated complex; TAS:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005519; F:cytoskeletal regulatory protein binding; TAS:MGI.
DR   GO; GO:0016358; P:dendrite development; IMP:MGI.
DR   GO; GO:0001578; P:microtubule bundle formation; IMP:MGI.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:InterPro.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:MGI.
DR   InterPro; IPR013588; MAP2_projctn.
DR   InterPro; IPR001084; Tau_tubulin-bd.
DR   Pfam; PF08377; MAP2_projctn; 1.
DR   Pfam; PF00418; Tubulin-binding; 3.
DR   PROSITE; PS00229; TAU_MAP_1; 2.
DR   PROSITE; PS51491; TAU_MAP_2; 3.
PE   1: Evidence at protein level;
KW   Calmodulin-binding; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Microtubule; Phosphoprotein; Repeat.
FT   CHAIN         1   1828       Microtubule-associated protein 2.
FT                                /FTId=PRO_0000072748.
FT   REPEAT     1662   1692       Tau/MAP 1.
FT   REPEAT     1693   1723       Tau/MAP 2.
FT   REPEAT     1724   1755       Tau/MAP 3.
FT   REGION     1452   1472       Calmodulin-binding (Potential).
FT   MOD_RES      63     63       Phosphoserine (By similarity).
FT   MOD_RES     608    608       Phosphoserine.
FT   MOD_RES     626    626       Phosphoserine.
FT   MOD_RES     655    655       Phosphoserine.
FT   MOD_RES     730    730       Phosphoserine.
FT   MOD_RES     737    737       Phosphoserine.
FT   MOD_RES     746    746       Phosphotyrosine.
FT   MOD_RES     823    823       Phosphoserine.
FT   MOD_RES     835    835       Phosphoserine (By similarity).
FT   MOD_RES    1161   1161       Phosphoserine.
FT   MOD_RES    1352   1352       Phosphoserine.
FT   MOD_RES    1358   1358       Phosphothreonine.
FT   MOD_RES    1426   1426       Phosphoserine.
FT   MOD_RES    1445   1445       Phosphothreonine.
FT   MOD_RES    1485   1485       Phosphoserine.
FT   MOD_RES    1539   1539       Phosphoserine.
FT   MOD_RES    1595   1595       Phosphoserine.
FT   MOD_RES    1598   1598       Phosphothreonine.
FT   MOD_RES    1599   1599       Phosphothreonine.
FT   MOD_RES    1606   1606       Phosphothreonine.
FT   MOD_RES    1609   1609       Phosphothreonine.
FT   MOD_RES    1612   1612       Phosphoserine.
FT   MOD_RES    1615   1615       Phosphoserine.
FT   MOD_RES    1617   1617       Phosphothreonine (By similarity).
FT   MOD_RES    1620   1620       Phosphothreonine.
FT   MOD_RES    1650   1650       Phosphothreonine.
FT   MOD_RES    1657   1657       Phosphothreonine.
FT   MOD_RES    1783   1783       Phosphoserine.
FT   MOD_RES    1791   1791       Phosphoserine.
FT   MOD_RES    1799   1799       Phosphoserine (By similarity).
FT   MOD_RES    1800   1800       Phosphoserine (By similarity).
FT   MOD_RES    1801   1801       Phosphoserine (By similarity).
FT   MOD_RES    1803   1803       Phosphoserine (By similarity).
SQ   SEQUENCE   1828 AA;  198982 MW;  200BC59E360538CA CRC64;
     MADERKDEGK APHWTSASLT EAAAHPHSPE MKDQGGAGEG LSRNANGFPY REEEEGAFGE
     HRSQGTYSDT KENGINGELT SADRETAEEV SARIVQVVTA EAVAVLKGEQ EKEAQYKDQP
     AALPLAAEET ANLPPSPPPS PASEQTATVE EDLLTASKME FPEQEKFPSS FAEPLDKGEM
     EFKMPSKPGE DFEHAALVPD TSKTPQDKKD LQGMEGEKLP PVPFAQTFGT NLEDRKQSTE
     PSIVMPSIGL SAEPPAPKEP KDWFIEMPTE SKKDEWGLAA PISPGPLTPM REKDVLEDIP
     RWEGKQFDSP MPSPFHGGSF TLPLDTMKNE RVSEGPRPFA PVFFQSDDKV SLQDPSALAT
     SKESSKDEEP LKDKADKVAD VSISEVTTLL GNVHSPVVEG YVGENISGEV KVTTDQEKKE
     TSAPSVQEPT LTETEPQTKL DEKSTVSIEE AVAKEEESLK LRDDKTGVIQ TSTEQSFSKE
     DQKGQEHTID ELKQDSFPIS LEQAVTDAAM TSKTLGKVTS EPEAVSERRE IQGLFEEKTA
     DKNKLEGAGS ATIAEVEMPF YEDKSGMSKY FETSALKEDM TRSTELGSDY YELSDSRGSA
     QESLDTISPK NQHDEKELQA KASQPSPPAQ EAGYSTLAQS YTPGHPSELP EEPSSPQERM
     FTIDPKVYGE KRDLHSKNKD DLTLSRSLGL GGRSAIEQRS MSINLPMSCL DSIALGFNFG
     RGHDLSPLAS DILTNTSGSM DEGDDYLPPT TPAVEKMPCF PIESKEEEDK AEQAKVTGGQ
     TIQVETSSES PFPAKEYYKN GTVMAPDLPE MLDLAGTRSR LASVSADAEV ARRKSVPSEA
     MLAESSTSLP PVADESPVTV KPDSQLEDMG YCVFNKYTVP LPSPVQDSEN LSGESGSFYE
     GTDDKVRRDL ATDLSLIEVK LAAAGRVKDE FTAEKEATPP TSADKSGLSR EFDHDRKAND
     KLDTVLEKSE EHIDSKEHAK ESEEMGGKVE LFGLGITYDQ ASTKELITTK DTSPEKTEKG
     LSSVPEVAEV EPTTKADQGL DFAATKAEPS QLDIKVSDFG QMASGMNVDA GKAIELKFEV
     AQELTLSSEA PQEADSFMGV ESGHIKEGGK VNETEVKEKV TKPDLVHQEA VDKEESYESS
     GEHESLTMES LKPDEGKKET SPETSLIQDE VALKLSVEIP CPPPVSEADL STDEKGEVQM
     EFIQLPKEES TETPDIPAIP SDVTQPQPEA IVSEPAEVPS EEEEIEAGGE YDKLLFRSDT
     LQISDLLVSE SREEFVETCP GELKGVVESV VTIEDDFITV VQTTTDEGES GSHSVRFAAP
     AQPEEERRPR PHDEELEIEM AAEAQAEPKD GSPDAPATPE KEEVAFSEYK TETYDDYKDE
     TTIDDSIMDA DSLWVDTQDD DRSILTEQLE TIPKEERAEK DARRPSLEKH RKEKPFKTGR
     GRISTPERKV AKKEPSTVSR DEVRRKKAVY KKAELAKKSE VQAHSPSRKL ILKPAIKYTR
     PTHLSCVKRK TTAASGDLAQ APGAFKQAKD KVTDGISKSP EKRSSLPRPS SILPPRRGVS
     GDREENSFSL NSSISSARRT TRSEPIRRAG KSGTSTPTTP GSTAITPGTP PSYSSRTPGT
     PGTPSYPRTP GTPKSGILVP SEKKVAIIRT PPKSPATPKQ LRLINQPLPD LKNVKSKIGS
     TDNIKYQPKG GQVQIVTKKI DLSHVTSKCG SLKNIRHRPG GGRVKIESVK LDFKEKAQAK
     VGSLDNAHHV PGGGNVKIDS QKLNFREHAK ARVDHGAEII TQSPSRSSVA SPRRLSNVSS
     SGSINLLESP QLATLAEDVT AALAKQGL
//
ID   GNAT1_MOUSE             Reviewed;         350 AA.
AC   P20612; Q80X34;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 110.
DE   RecName: Full=Guanine nucleotide-binding protein G(t) subunit alpha-1;
DE   AltName: Full=Transducin alpha-1 chain;
GN   Name=Gnat1; Synonyms=Gnat-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=89214143; PubMed=2708360;
RA   Raport C.J., Dere B., Hurley J.B.;
RT   "Characterization of the mouse rod transducin alpha subunit gene.";
RL   J. Biol. Chem. 264:7122-7128(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 32-42; 194-201; 267-273 AND 330-341, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 124-317.
RC   STRAIN=CF-1 / Harlan; TISSUE=Retina;
RX   MEDLINE=97011591; PubMed=8858601;
RX   DOI=10.1002/(SICI)1098-2795(199607)44:3<315::AID-MRD5>3.3.CO;2-V;
RA   Williams C.J., Schultz R.M., Kopf G.S.;
RT   "G protein gene expression during mouse oocyte growth and maturation,
RT   and preimplantation embryo development.";
RL   Mol. Reprod. Dev. 44:315-323(1996).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC       involved as modulators or transducers in various transmembrane
CC       signaling systems. Transducin is an amplifier and one of the
CC       transducers of a visual impulse that performs the coupling between
CC       rhodopsin and cGMP-phosphodiesterase.
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and
CC       gamma. The alpha chain contains the guanine nucleotide binding
CC       site.
CC   -!- TISSUE SPECIFICITY: Rod.
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; M25513; AAA40473.1; -; Genomic_DNA.
DR   EMBL; M25506; AAA40473.1; JOINED; Genomic_DNA.
DR   EMBL; M25507; AAA40473.1; JOINED; Genomic_DNA.
DR   EMBL; M25508; AAA40473.1; JOINED; Genomic_DNA.
DR   EMBL; M25509; AAA40473.1; JOINED; Genomic_DNA.
DR   EMBL; M25510; AAA40473.1; JOINED; Genomic_DNA.
DR   EMBL; M25511; AAA40473.1; JOINED; Genomic_DNA.
DR   EMBL; M25512; AAA40473.1; JOINED; Genomic_DNA.
DR   EMBL; BC022793; AAH22793.1; -; mRNA.
DR   EMBL; BC051412; AAH51412.2; -; mRNA.
DR   EMBL; BC058810; AAH58810.1; -; mRNA.
DR   EMBL; U38504; AAB01735.1; -; mRNA.
DR   IPI; IPI00330646; -.
DR   PIR; A33352; RGMST1.
DR   RefSeq; NP_032166.1; NM_008140.2.
DR   UniGene; Mm.284853; -.
DR   ProteinModelPortal; P20612; -.
DR   SMR; P20612; 27-344.
DR   STRING; P20612; -.
DR   PhosphoSite; P20612; -.
DR   PRIDE; P20612; -.
DR   Ensembl; ENSMUST00000010205; ENSMUSP00000010205; ENSMUSG00000034837.
DR   GeneID; 14685; -.
DR   KEGG; mmu:14685; -.
DR   UCSC; uc009rmr.1; mouse.
DR   CTD; 14685; -.
DR   MGI; MGI:95778; Gnat1.
DR   eggNOG; roNOG10660; -.
DR   GeneTree; ENSGT00560000076725; -.
DR   HOGENOM; HBG444960; -.
DR   HOVERGEN; HBG063184; -.
DR   InParanoid; P20612; -.
DR   OMA; MHLADTI; -.
DR   OrthoDB; EOG47D9GD; -.
DR   PhylomeDB; P20612; -.
DR   NextBio; 286619; -.
DR   ArrayExpress; P20612; -.
DR   Bgee; P20612; -.
DR   Genevestigator; P20612; -.
DR   GermOnline; ENSMUSG00000034837; Mus musculus.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; TAS:MGI.
DR   GO; GO:0005624; C:membrane fraction; TAS:MGI.
DR   GO; GO:0032391; C:photoreceptor connecting cilium; IDA:MGI.
DR   GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IDA:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0008283; P:cell proliferation; IDA:MGI.
DR   GO; GO:0050908; P:detection of light stimulus involved in visual perception; IMP:MGI.
DR   GO; GO:0042462; P:eye photoreceptor cell development; IMP:MGI.
DR   GO; GO:0007199; P:G-protein signaling, coupled to cGMP nucleotide second messenger; TAS:MGI.
DR   GO; GO:0050917; P:sensory perception of umami taste; IMP:MGI.
DR   InterPro; IPR001408; Gprotein_alpha_I.
DR   InterPro; IPR001019; Gprotein_alpha_su.
DR   InterPro; IPR011025; GproteinA_insert.
DR   Gene3D; G3DSA:1.10.400.10; GproteinA_insert; 1.
DR   PANTHER; PTHR10218; Gprotein_alph_bd; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00441; GPROTEINAI.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF47895; Transducn_insert; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; GTP-binding; Lipoprotein; Myristate;
KW   Nucleotide-binding; Sensory transduction; Transducer; Vision.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    350       Guanine nucleotide-binding protein G(t)
FT                                subunit alpha-1.
FT                                /FTId=PRO_0000203738.
FT   NP_BIND      36     43       GTP (By similarity).
FT   NP_BIND     196    200       GTP (By similarity).
FT   NP_BIND     265    268       GTP (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
SQ   SEQUENCE   350 AA;  39967 MW;  3810BA8DEEFBD7D5 CRC64;
     MGAGASAEEK HSRELEKKLK EDAEKDARTV KLLLLGAGES GKSTIVKQMK IIHQDGYSLE
     ECLEFIAIIY GNTLQSILAI VRAMTTLNIQ YGDSARQDDA RKLMHMADTI EEGTMPKEMS
     DIIQRLWKDS GIQACFDRAS EYQLNDSAGY YLSDLERLVT PGYVPTEQDV LRSRVKTTGI
     IETQFSFKDL NFRMFDVGGQ RSERKKWIHC FEGVTCIIFI AALSAYDMVL VEDDEVNRMH
     ESLHLFNSIC NHRYFATTSI VLFLNKKDVF SEKIKKAHLS ICFPDYDGPN TYEDAGNYIK
     VQFLELNMRR DVKEIYSHMT CATDTQNVKF VFDAVTDIII KENLKDCGLF
//
ID   MAG_MOUSE               Reviewed;         626 AA.
AC   P20917; P16880;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   08-MAR-2011, entry version 109.
DE   RecName: Full=Myelin-associated glycoprotein;
DE   AltName: Full=Siglec-4a;
DE   Flags: Precursor;
GN   Name=Mag;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ISOFORMS L-MAG AND S-MAG).
RX   MEDLINE=90121220; PubMed=2482022; DOI=10.1016/0006-291X(89)92724-1;
RA   Fujita N., Sato S., Kurihara T., Kuwano R., Sakimura K., Inuzuka T.,
RA   Takahashi Y., Miyatake T.;
RT   "cDNA cloning of mouse myelin-associated glycoprotein: a novel
RT   alternative splicing pattern.";
RL   Biochem. Biophys. Res. Commun. 165:1162-1169(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM S-MAG).
RC   TISSUE=Brain;
RX   MEDLINE=91298961; PubMed=1712586; DOI=10.1016/0006-291X(91)91811-P;
RA   Nakano R., Fujita N., Sato S., Inuzuka T., Sakimura K., Ishiguro H.,
RA   Mishina M., Miyatake T.;
RT   "Structure of mouse myelin-associated glycoprotein gene.";
RL   Biochem. Biophys. Res. Commun. 178:282-290(1991).
RN   [3]
RP   PROTEIN SEQUENCE OF 78-88 AND 466-477, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=91366725; PubMed=1716323; DOI=10.1002/jnr.490290202;
RA   Pedraza L., Frey A.B., Hempstead B.L., Colman D.R., Salzer J.L.;
RT   "Differential expression of MAG isoforms during development.";
RL   J. Neurosci. Res. 29:141-148(1991).
RN   [5]
RP   SIALIC ACID-BINDING.
RX   MEDLINE=95179521; PubMed=7533044; DOI=10.1016/S0960-9822(00)00220-7;
RA   Kelm S., Pelz A., Schauer R., Filbin M.T., Tang S., de Bellard M.E.,
RA   Schnaar R.L., Mahoney J.A., Hartnell A., Bradfield P., Crocker P.R.;
RT   "Sialoadhesin, myelin-associated glycoprotein and CD22 define a new
RT   family of sialic acid-dependent adhesion molecules of the
RT   immunoglobulin superfamily.";
RL   Curr. Biol. 4:965-972(1994).
RN   [6]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   MEDLINE=20090811; PubMed=10625334;
RX   DOI=10.1002/(SICI)1098-1136(20000115)29:2<154::AID-GLIA9>3.0.CO;2-3;
RA   Schachner M., Bartsch U.;
RT   "Multiple functions of the myelin-associated glycoprotein MAG (siglec-
RT   4a) in formation and maintenance of myelin.";
RL   Glia 29:154-165(2000).
RN   [7]
RP   INTERACTION WITH RTN4R.
RX   MEDLINE=22171378; PubMed=12089450; DOI=10.1126/science.1073031;
RA   Liu B.P., Fournier A., GrandPre T., Strittmatter S.M.;
RT   "Myelin-associated glycoprotein as a functional ligand for the Nogo-66
RT   receptor.";
RL   Science 297:1190-1193(2002).
CC   -!- FUNCTION: Adhesion molecule in postnatal neural development that
CC       mediates sialic-acid dependent cell-cell interactions between
CC       neuronal and myelinating cells. Preferentially binds to alpha-2,3-
CC       linked sialic acid. Isoform L-MAG is critical for the formation of
CC       myelin in the CNS, whereas isoform S-MAG is sufficient to maintain
CC       the integrity of myelin in PNS.
CC   -!- SUBUNIT: Binds to RTN4R.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=L-MAG;
CC         IsoId=P20917-1; Sequence=Displayed;
CC       Name=S-MAG;
CC         IsoId=P20917-2; Sequence=VSP_002527, VSP_002528;
CC   -!- TISSUE SPECIFICITY: Expressed by myelinating glial cells in the
CC       central and peripheral nervous system. Detected in oligodendrocyte
CC       processes before formation of compact myelin. Restricted to the
CC       periaxonal space after myelination. Isoform S-MAG is the
CC       predominant isoform in CNS and PNS of the adult.
CC   -!- DEVELOPMENTAL STAGE: In CNS isoform L-MAG is the major form
CC       synthesized early in development, and it persists as a significant
CC       proportion of the MAG present in the adult. In the PNS isoform L-
CC       MAG is expressed at modest levels during development; it is absent
CC       in the adult.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC
CC       (sialic acid binding Ig-like lectin) family.
CC   -!- SIMILARITY: Contains 4 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC       domain.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=Siglec-4;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Itlect_196";
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=Siglec-4a [3 Fc Domains];
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Itlect_00003";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M31811; AAA39487.1; -; mRNA.
DR   EMBL; M74793; AAA91743.1; -; Genomic_DNA.
DR   EMBL; M74783; AAA91743.1; JOINED; Genomic_DNA.
DR   EMBL; M74784; AAA91743.1; JOINED; Genomic_DNA.
DR   EMBL; M74785; AAA91743.1; JOINED; Genomic_DNA.
DR   EMBL; M74786; AAA91743.1; JOINED; Genomic_DNA.
DR   EMBL; M74787; AAA91743.1; JOINED; Genomic_DNA.
DR   EMBL; M74788; AAA91743.1; JOINED; Genomic_DNA.
DR   EMBL; M74790; AAA91743.1; JOINED; Genomic_DNA.
DR   EMBL; M74791; AAA91743.1; JOINED; Genomic_DNA.
DR   IPI; IPI00230151; -.
DR   IPI; IPI00276515; -.
DR   PIR; B33785; B33785.
DR   RefSeq; NP_034888.1; NM_010758.2.
DR   UniGene; Mm.241355; -.
DR   ProteinModelPortal; P20917; -.
DR   SMR; P20917; 14-504.
DR   MINT; MINT-202735; -.
DR   STRING; P20917; -.
DR   PhosphoSite; P20917; -.
DR   PRIDE; P20917; -.
DR   Ensembl; ENSMUST00000040548; ENSMUSP00000041464; ENSMUSG00000036634.
DR   Ensembl; ENSMUST00000073818; ENSMUSP00000073489; ENSMUSG00000036634.
DR   GeneID; 17136; -.
DR   KEGG; mmu:17136; -.
DR   UCSC; uc009gha.1; mouse.
DR   CTD; 17136; -.
DR   MGI; MGI:96912; Mag.
DR   eggNOG; roNOG07403; -.
DR   HOGENOM; HBG755240; -.
DR   HOVERGEN; HBG006317; -.
DR   InParanoid; P20917; -.
DR   OrthoDB; EOG4M3985; -.
DR   PhylomeDB; P20917; -.
DR   ArrayExpress; P20917; -.
DR   Bgee; P20917; -.
DR   CleanEx; MM_MAG; -.
DR   Genevestigator; P20917; -.
DR   GermOnline; ENSMUSG00000036634; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0033270; C:paranode region of axon; IDA:BHF-UCL.
DR   GO; GO:0043220; C:Schmidt-Lanterman incisure; IDA:BHF-UCL.
DR   GO; GO:0005529; F:sugar binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   InterPro; IPR013162; CD80_C2-set.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 4.
DR   Pfam; PF08205; C2-set_2; 1.
DR   Pfam; PF07679; I-set; 2.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Lectin;
KW   Lipoprotein; Membrane; Palmitate; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     19
FT   CHAIN        20    626       Myelin-associated glycoprotein.
FT                                /FTId=PRO_0000014857.
FT   TOPO_DOM     20    516       Extracellular (Potential).
FT   TRANSMEM    517    536       Helical; (Potential).
FT   TOPO_DOM    537    626       Cytoplasmic (Potential).
FT   DOMAIN       22    120       Ig-like V-type.
FT   DOMAIN      139    237       Ig-like C2-type 1.
FT   DOMAIN      241    325       Ig-like C2-type 2.
FT   DOMAIN      327    412       Ig-like C2-type 3.
FT   DOMAIN      413    508       Ig-like C2-type 4.
FT   BINDING     118    118       Sialic acid (By similarity).
FT   LIPID       531    531       S-palmitoyl cysteine (By similarity).
FT   CARBOHYD     99     99       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    223    223       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    246    246       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    315    315       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    332    332       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    406    406       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    450    450       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    454    454       N-linked (GlcNAc...) (Potential).
FT   DISULFID     37    165       By similarity.
FT   DISULFID     42    100       By similarity.
FT   DISULFID    159    217       By similarity.
FT   DISULFID    261    305       By similarity.
FT   DISULFID    347    392       By similarity.
FT   DISULFID    421    430       By similarity.
FT   DISULFID    432    488       By similarity.
FT   VAR_SEQ     574    582       EKRLGSERR -> REVSTRDCH (in isoform S-
FT                                MAG).
FT                                /FTId=VSP_002527.
FT   VAR_SEQ     583    626       Missing (in isoform S-MAG).
FT                                /FTId=VSP_002528.
SQ   SEQUENCE   626 AA;  69260 MW;  9C797BD6B52B6057 CRC64;
     MIFLATLPLF WIMISASRGG HWGAWMPSTI SAFEGTCVSI PCRFDFPDEL RPAVVHGVWY
     FNSPYPKNYP PVVFKSRTQV VHESFQGRSR LLGDLGLRNC TLLLSTLSPE LGGKYYFRGD
     LGGYNQYTFS EHSVLDIVNT PNIVVPPEVV AGTEVEVSCM VPDNCPELRP ELSWLGHEGL
     GEPTVLGRLR EDEGTWVQVS LLHFVPTREA NGHRLGCQAA FPNTTLQFEG YASLDVKYPP
     VIVEMNSSVE AIEGSHVSLL CGADSNPPPL LTWMRDGMVL REAVAKSLYL DLEEVTPGED
     GVYACLAENA YGQDNRTVEL SVMYAPWKPT VNGTVVAVEG ETVSILCSTQ SNPDPILTIF
     KEKQILATVI YESQLQLELP AVTPEDDGEY WCVAENQYGQ RATAFNLSVE FAPIILLESH
     CAAARDTVQC LCVVKSNPEP SVAFELPSRN VTVNETEREF VYSERSGLLL TSILTIRGQA
     QAPPRVICTS RNLYGTQSLE LPFQGAHRLM WAKIGPVGAV VAFAILIAIV CYITQTRRKK
     NVTESSSFSG GDNPHVLYSP EFRISGAPDK YESEKRLGSE RRLLGLRGES PELDLSYSHS
     DLGKRPTKDS YTLTEELAEY AEIRVK
//
ID   TPM3_MOUSE              Reviewed;         284 AA.
AC   P21107; Q09021; Q60606; Q80SW6; Q9EPW3;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2002, sequence version 2.
DT   08-MAR-2011, entry version 104.
DE   RecName: Full=Tropomyosin alpha-3 chain;
DE   AltName: Full=Gamma-tropomyosin;
DE   AltName: Full=Tropomyosin-3;
GN   Name=Tpm3; Synonyms=Tpm-5, Tpm5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=BALB/c;
RX   MEDLINE=90381307; PubMed=2400784; DOI=10.1016/0167-4781(90)90129-P;
RA   Takenaga K., Nakamura Y., Kageyama H., Sakiyama S.;
RT   "Nucleotide sequence of cDNA for nonmuscle tropomyosin 5 of mouse
RT   fibroblast.";
RL   Biochim. Biophys. Acta 1087:101-103(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Diaphragm;
RA   Hailstones D.L.;
RT   "Regulation of non-muscle isoforms of contractile proteins dring
RT   myogenesis.";
RL   Thesis (1993), University of Sydney, Australia.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Skeletal muscle;
RX   MEDLINE=20349356; PubMed=10889038; DOI=10.1021/bi000047x;
RA   Pieples K., Wieczorek D.F.;
RT   "Tropomyosin 3 increases striated muscle isoform diversity.";
RL   Biochemistry 39:8291-8297(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 243-284 (ISOFORM 1).
RC   STRAIN=ICR;
RX   MEDLINE=93260014; PubMed=8491774; DOI=10.1083/jcb.121.4.811;
RA   Schevzov G., Lloyd C., Hailstones D.L., Gunning P.;
RT   "Differential regulation of tropomyosin isoform organization and gene
RT   expression in response to altered actin gene expression.";
RL   J. Cell Biol. 121:811-821(1993).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: Binds to actin filaments in muscle and non-muscle cells.
CC       Plays a central role, in association with the troponin complex, in
CC       the calcium dependent regulation of vertebrate striated muscle
CC       contraction. Smooth muscle contraction is regulated by interaction
CC       with caldesmon. In non-muscle cells is implicated in stabilizing
CC       cytoskeleton actin filaments.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain. Binds to TMOD1
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytoskeleton.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1; Synonyms=Skeletal muscle;
CC         IsoId=P21107-1; Sequence=Displayed;
CC       Name=2; Synonyms=Cytoskeletal;
CC         IsoId=P21107-2; Sequence=VSP_006608, VSP_006609, VSP_006610;
CC         Note=Initiator Met-1 is removed (By similarity). Acetylated on
CC         Ala-2 and Lys-228 (By similarity);
CC   -!- DOMAIN: The molecule is in a coiled coil structure that is formed
CC       by 2 polypeptide chains. The sequence exhibits a prominent seven-
CC       residues periodicity.
CC   -!- SIMILARITY: Belongs to the tropomyosin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA03725.1; Type=Erroneous initiation;
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DR   EMBL; X53753; CAA37782.1; -; mRNA.
DR   EMBL; U04541; AAA03725.1; ALT_INIT; mRNA.
DR   EMBL; AF317223; AAG38596.1; -; mRNA.
DR   EMBL; AK088111; BAC40150.1; -; mRNA.
DR   EMBL; AK088902; BAC40643.1; -; mRNA.
DR   EMBL; X72633; CAA51209.1; -; mRNA.
DR   IPI; IPI00230044; -.
DR   IPI; IPI00278611; -.
DR   PIR; I48852; I48852.
DR   PIR; S11390; S11390.
DR   UniGene; Mm.240839; -.
DR   UniGene; Mm.474711; -.
DR   ProteinModelPortal; P21107; -.
DR   SMR; P21107; 8-284.
DR   DIP; DIP-32061N; -.
DR   STRING; P21107; -.
DR   PhosphoSite; P21107; -.
DR   SWISS-2DPAGE; P21107; -.
DR   COMPLUYEAST-2DPAGE; P21107; -.
DR   REPRODUCTION-2DPAGE; P21107; -.
DR   PRIDE; P21107; -.
DR   Ensembl; ENSMUST00000029549; ENSMUSP00000029549; ENSMUSG00000027940.
DR   Ensembl; ENSMUST00000029550; ENSMUSP00000029550; ENSMUSG00000027940.
DR   Ensembl; ENSMUST00000121503; ENSMUSP00000113578; ENSMUSG00000027940.
DR   NMPDR; fig|10090.3.peg.8420; -.
DR   UCSC; uc008qbf.1; mouse.
DR   UCSC; uc008qbj.1; mouse.
DR   MGI; MGI:1890149; Tpm3.
DR   eggNOG; roNOG11550; -.
DR   GeneTree; ENSGT00550000074494; -.
DR   HOVERGEN; HBG107404; -.
DR   OMA; SKQHEDE; -.
DR   ArrayExpress; P21107; -.
DR   Bgee; P21107; -.
DR   CleanEx; MM_TPM3; -.
DR   Genevestigator; P21107; -.
DR   GermOnline; ENSMUSG00000027940; Mus musculus.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR   GO; GO:0030426; C:growth cone; IDA:MGI.
DR   GO; GO:0002102; C:podosome; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR000533; Tropomyosin.
DR   Pfam; PF00261; Tropomyosin; 1.
DR   PRINTS; PR00194; TROPOMYOSIN.
DR   PROSITE; PS00326; TROPOMYOSIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Alternative splicing; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Muscle protein; Phosphoprotein.
FT   CHAIN         1    284       Tropomyosin alpha-3 chain.
FT                                /FTId=PRO_0000205633.
FT   COILED        1    284       By similarity.
FT   MOD_RES      12     12       N6-acetyllysine (By similarity).
FT   MOD_RES     162    162       Phosphotyrosine (By similarity).
FT   MOD_RES     252    252       Phosphothreonine (By similarity).
FT   MOD_RES     283    283       Phosphoserine.
FT   VAR_SEQ       1     80       MEAIKKKMQMLKLDKENVLDRAEQAEAEQKQAEERSKQLED
FT                                ELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAAD
FT                                -> MAGTTTIEAVKRKIQVLQQQADDAEERAERLQREVEGE
FT                                RRAREQ (in isoform 2).
FT                                /FTId=VSP_006608.
FT   VAR_SEQ     189    211       KCSELEEELKNVTNNLKSLEAQA -> RCREMDEQIRLMDQ
FT                                NLKCLSAAE (in isoform 2).
FT                                /FTId=VSP_006609.
FT   VAR_SEQ     259    284       ELYAQKLKYKAISDELDHALNDMTSI -> KLKCTKEEHLC
FT                                TQRMLDQTLLDLNEM (in isoform 2).
FT                                /FTId=VSP_006610.
FT   CONFLICT     18     18       V -> F (in Ref. 2; AAA03725).
FT   CONFLICT    111    111       Q -> R (in Ref. 2; AAA03725).
FT   CONFLICT    180    180       E -> G (in Ref. 2; AAA03725).
SQ   SEQUENCE   284 AA;  32863 MW;  CE16494A3018A185 CRC64;
     MEAIKKKMQM LKLDKENVLD RAEQAEAEQK QAEERSKQLE DELATMQKKL KGTEDELDKY
     SEALKDAQEK LELAEKKAAD AEAEVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA
     DESERGMKVI ENRALKDEEK MELQEIQLKE AKHIAEEADR KYEEVARKLV IIEGDLERTE
     ERAELAESKC SELEEELKNV TNNLKSLEAQ AEKYSQKEDK YEEEIKILTD KLKEAETRAE
     FAERSVAKLE KTIDDLEDEL YAQKLKYKAI SDELDHALND MTSI
//
ID   MYO5B_MOUSE             Reviewed;        1818 AA.
AC   P21271; Q148A3; Q69ZR6; Q811F6; Q91X59;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Myosin-Vb;
GN   Name=Myo5b; Synonyms=Kiaa1119;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1054-1818 (ISOFORM 3).
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1086-1818 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=91046023; PubMed=2236059; DOI=10.1073/pnas.87.21.8491;
RA   Huang W.-M., Reed-Fourquet L., Wu E., Wu J.-Y.;
RT   "Molecular cloning and amino acid sequence of brain L-glutamate
RT   decarboxylase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:8491-8495(1990).
RN   [4]
RP   DOUBTS ON THE FUNCTION.
RX   MEDLINE=93107155; PubMed=1469047; DOI=10.1083/jcb.119.6.1541;
RA   Espreafico E.M., Cheney R.E., Matteoli M., Nascimento A.A.,
RA   de Camilli P.V., Larson R.E., Mooseker M.S.;
RT   "Primary structure and cellular localization of chicken brain myosin-V
RT   (p190), an unconventional myosin with calmodulin light chains.";
RL   J. Cell Biol. 119:1541-1557(1992).
CC   -!- FUNCTION: May be involved in vesicular trafficking via its
CC       association with the CART complex. The CART complex is necessary
CC       for efficient transferrin receptor recycling but not for EGFR
CC       degradation (By similarity).
CC   -!- SUBUNIT: Component of the CART complex, at least composed of
CC       ACTN4, HGS/HRS, MYO5B and TRIM3. Interacts with RAB11FIP2 (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P21271-1; Sequence=Displayed;
CC       Name=3;
CC         IsoId=P21271-3; Sequence=VSP_022099;
CC   -!- SIMILARITY: Contains 1 dilute domain.
CC   -!- SIMILARITY: Contains 6 IQ domains.
CC   -!- SIMILARITY: Contains 1 myosin head-like domain.
CC   -!- CAUTION: Was originally (PubMed:2236059) thought to be a glutamate
CC       decarboxylase (GAD).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA37655.1; Type=Erroneous initiation;
CC       Sequence=AAA37655.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part;
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DR   EMBL; BC011494; AAH11494.1; -; mRNA.
DR   EMBL; BC046444; AAH46444.1; -; mRNA.
DR   EMBL; BC118525; AAI18526.1; -; mRNA.
DR   EMBL; AK173102; BAD32380.1; -; Transcribed_RNA.
DR   EMBL; M55253; AAA37655.1; ALT_INIT; mRNA.
DR   IPI; IPI00410957; -.
DR   IPI; IPI00816932; -.
DR   PIR; A36481; A36481.
DR   UniGene; Mm.260098; -.
DR   ProteinModelPortal; P21271; -.
DR   SMR; P21271; 1-790, 812-866, 1451-1818.
DR   STRING; P21271; -.
DR   PhosphoSite; P21271; -.
DR   PRIDE; P21271; -.
DR   Ensembl; ENSMUST00000074157; ENSMUSP00000073790; ENSMUSG00000025885.
DR   Ensembl; ENSMUST00000114883; ENSMUSP00000110533; ENSMUSG00000025885.
DR   UCSC; uc008fpp.1; mouse.
DR   MGI; MGI:106598; Myo5b.
DR   eggNOG; roNOG04978; -.
DR   HOVERGEN; HBG052556; -.
DR   OrthoDB; EOG4KPT8Z; -.
DR   PhylomeDB; P21271; -.
DR   ArrayExpress; P21271; -.
DR   Bgee; P21271; -.
DR   CleanEx; MM_MYO5B; -.
DR   Genevestigator; P21271; -.
DR   GermOnline; ENSMUSG00000025885; Mus musculus.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:motor activity; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR018444; Dil_domain.
DR   InterPro; IPR002710; Dilute.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   Pfam; PF01843; DIL; 1.
DR   Pfam; PF00612; IQ; 6.
DR   Pfam; PF00063; Myosin_head; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 6.
DR   SMART; SM00242; MYSc; 1.
DR   PROSITE; PS51126; DILUTE; 1.
DR   PROSITE; PS50096; IQ; 6.
PE   2: Evidence at transcript level;
KW   Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding;
KW   Coiled coil; Motor protein; Myosin; Nucleotide-binding;
KW   Phosphoprotein; Protein transport; Repeat; Transport.
FT   CHAIN         1   1818       Myosin-Vb.
FT                                /FTId=PRO_0000123461.
FT   DOMAIN        1    765       Myosin head-like.
FT   DOMAIN      765    794       IQ 1.
FT   DOMAIN      788    817       IQ 2.
FT   DOMAIN      813    842       IQ 3.
FT   DOMAIN      836    865       IQ 4.
FT   DOMAIN      861    890       IQ 5.
FT   DOMAIN      884    913       IQ 6.
FT   DOMAIN     1496   1773       Dilute.
FT   NP_BIND     163    170       ATP (Potential).
FT   REGION      641    663       Actin-binding (Potential).
FT   COILED     1140   1261       Potential.
FT   COILED     1313   1415       Potential.
FT   MOD_RES     695    695       Phosphotyrosine (By similarity).
FT   MOD_RES    1416   1416       Phosphoserine (By similarity).
FT   VAR_SEQ    1310   1310       N -> NSQTEDWGYLNEDGELGLAYQGLKQVA (in
FT                                isoform 3).
FT                                /FTId=VSP_022099.
FT   CONFLICT    829    829       A -> V (in Ref. 1; AAH46444).
FT   CONFLICT    840    840       T -> A (in Ref. 1; AAH46444).
FT   CONFLICT    879    880       KR -> RC (in Ref. 1; AAH46444).
FT   CONFLICT    884    884       E -> Q (in Ref. 1; AAH46444).
FT   CONFLICT   1217   1218       KA -> NG (in Ref. 3; AAA37655).
FT   CONFLICT   1257   1257       V -> A (in Ref. 3; AAA37655).
FT   CONFLICT   1446   1446       D -> V (in Ref. 3; AAA37655).
FT   CONFLICT   1464   1464       S -> L (in Ref. 3; AAA37655).
FT   CONFLICT   1544   1544       T -> I (in Ref. 3; AAA37655).
FT   CONFLICT   1578   1579       IA -> MP (in Ref. 3; AAA37655).
FT   CONFLICT   1620   1631       Missing (in Ref. 3; AAA37655).
SQ   SEQUENCE   1818 AA;  210570 MW;  78CFFA626CADC4A0 CRC64;
     MSYSELYTRY TRVWIPDPDE VWRSAELTKD YKEGDKSLQL RLEDDTILEY PVDVQNNQVP
     FLRNPDILVG ENDLTALSHL HEPAVLHNLK VRFLESNHIY TYCGIVLVAI NPYEQLPIYG
     QDVIYAYSGQ NMGDMDPHIF AVAEEAYKQM ARDEKNQSII VSGESGAGKT VSAKYAMRYF
     ATVGGSASDT NIEEKVLASS PIMEAIGNAK TTRNDNSSRF GKFIEIGFDK KYHIIGANMR
     TYLLEKSRVV FQADDERNYH IFYQLCAAAS LPEFKELALT CAEDFFYTAH GGNTTIEGVN
     DADDFEKTRQ ALTLLGVRDS HQISIFKIIA SILHLGSVEI QSERDGDSCS ISPQDEHLSN
     FCSLLGIEHS QMEHWLCHRK LVTTSETYVK TMSLQQVVNA RDALAKHIYA QLFSWIVEHI
     NKALHTSHKQ HSFIGVLDIY GFETFEINSF EQFCINYANE KLQQQFNSHV FKLEQEEYMK
     EQIPWTLIDF YDNQPCIDLI EAKLGILDLL DEECKVPKGT DQNWAQKLYE RHSNSQHFQK
     PRMSNTAFIV NHFADKVEYL SDGFLEKNRD TVYEEQINIL KASKFPLVAD LFHDDKDSAP
     ATNTAKNRSS SKINVRSSRP LIKVPNKEHK KSVGYQFRTS LNLLMETLNA TTPHYVRCIK
     PNDEKLPFHF DPKRAVQQLR ACGVLETIRI SAAGYPSRWT YHDFFNRYRV LMKKRELTNT
     DKKNICKSVL ESLIKDPDKF QFGRTKIFFR AGQVAYLEKL RADKFREATI MIQKSVRGWL
     QRVKYRRLRA ATLSLQRFCR GYLARRLAEH LRRTRAAIVF QKQYRMLKAR RAYRRVCRAT
     VIIQSFTRAM FVRRNYRQVL MEHKATIIQK YARGWMARKR FLRERDAAIV IQCAFRRLKA
     RQELKALKIE ARSAEHLKRL NVGMENKVVQ LQRKIDDQNK EFKTLSEQLS AVTSSHAVEV
     EKLKKELAHY QQNQEADTSL QLQEEVQSLR TELQKAHSER RVLEDAHNKE NGELRKRVAD
     LEHENALLKD EKEYLNNQIL CQSKAESSQS SVEENLLMKK ELEEERSRYQ NLVKEYSQLE
     QRYENLRDEQ TPGHRKNPSN QSSLESDSNY PSISTSEIGD TEDALQQVEE IGIEKAAMDM
     TVFLKLQKRV RELEQERKKL QAQLEKGQQD SKKGQVEQQN NGLDVDQDAD IAYNSLKRQE
     LESENKKLKN DLNELRKAVA DQAMQDNSTH SSPDSYSLLL NQLKLANEEL EVRKEEVLIL
     RTQIMNADQR RLSGKNMEPN INARTSWPNS EKHVDQEDAI EAYHGVCQTN RLLEAQLQAQ
     SLEHEEEVEH LKAQVEALKE EMDKQQQTFC QTLLLSPEAQ VEFGVQQEIS RLTNENLDFK
     ELVEKLEKNE RKLKKQLKIY MKKVQDLEAA QALAQSDRRH HELTRQVTVQ RKEKDFQGML
     EYHKEDEALL IRNLVTDLKP QMLSGTVPCL PAYILYMCIR HADYTNDDLK VHSLLSSTIN
     GIKKVLKKHN DDFEMTSFWL SNTCRFLHCL KQYSGDEGFM TQNTAKQNEH CLKNFDLTEY
     RQVLSDLSIQ IYQQLIKIAE GLLQPMIVSA MLENESIQGL SGVRPTGYRK RSSSMVDGEN
     SYCLEAIVRQ MNSFHTVLCD QGLDPEIILQ VFKQLFYMIN AVTLNNLLLR KDACSWSTGM
     QLRYNISQLE EWLRGKNLHQ SGAVQTMEPL IQAAQLLQLK KKTHEDAEAI CSLCTSLSTQ
     QIVKILNLYT PLNEFEERVT VSFIRTIQAQ LQERNDPQQL LLDSKHVFPV LFPYNPSALT
     MDSIHIPACL NLEFLNEV
//
ID   GNAQ_MOUSE              Reviewed;         359 AA.
AC   P21279; Q6PFF5;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 4.
DT   08-MAR-2011, entry version 123.
DE   RecName: Full=Guanine nucleotide-binding protein G(q) subunit alpha;
DE   AltName: Full=Guanine nucleotide-binding protein alpha-q;
GN   Name=Gnaq;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=91067657; PubMed=2123549; DOI=10.1073/pnas.87.23.9113;
RA   Strathmann M., Simon M.I.;
RT   "G protein diversity: a distinct class of alpha subunits is present in
RT   vertebrates and invertebrates.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:9113-9117(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 20-27; 61-73; 78-92; 121-133; 159-181; 184-210;
RP   283-300; 312-338 AND 346-354, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   PALMITOYLATION AT CYS-9 AND CYS-10, AND MUTAGENESIS OF CYS-9 AND
RP   CYS-10.
RC   TISSUE=Brain;
RX   MEDLINE=94043367; PubMed=8227063;
RA   Wedegaertner P.B., Chu D.H., Wilson P.T., Levis M.J., Bourne H.R.;
RT   "Palmitoylation is required for signaling functions and membrane
RT   attachment of Gq alpha and Gs alpha.";
RL   J. Biol. Chem. 268:25001-25008(1993).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC       involved as modulators or transducers in various transmembrane
CC       signaling systems.
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and
CC       gamma. The alpha chain contains the guanine nucleotide binding
CC       site. Binds SLC9A3R1. Forms a complex with PECAM1 and BDKRB2.
CC       Interacts with PECAM1 (By similarity).
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(q) subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; M55412; AAA63306.1; -; mRNA.
DR   EMBL; BC057583; AAH57583.1; -; mRNA.
DR   IPI; IPI00228618; -.
DR   PIR; A38414; RGMSQ.
DR   RefSeq; NP_032165.3; NM_008139.5.
DR   UniGene; Mm.439701; -.
DR   UniGene; Mm.441601; -.
DR   PDB; 2BCJ; X-ray; 3.06 A; Q=37-353.
DR   PDB; 2RGN; X-ray; 3.50 A; A/D=37-359.
DR   PDB; 3AH8; X-ray; 2.90 A; A=37-359.
DR   PDB; 3OHM; X-ray; 2.70 A; A=35-359.
DR   PDBsum; 2BCJ; -.
DR   PDBsum; 2RGN; -.
DR   PDBsum; 3AH8; -.
DR   PDBsum; 3OHM; -.
DR   ProteinModelPortal; P21279; -.
DR   SMR; P21279; 37-354.
DR   DIP; DIP-606N; -.
DR   STRING; P21279; -.
DR   PhosphoSite; P21279; -.
DR   PRIDE; P21279; -.
DR   Ensembl; ENSMUST00000025541; ENSMUSP00000025541; ENSMUSG00000024639.
DR   GeneID; 14682; -.
DR   KEGG; mmu:14682; -.
DR   UCSC; uc008gwt.1; mouse.
DR   CTD; 14682; -.
DR   MGI; MGI:95776; Gnaq.
DR   eggNOG; roNOG09485; -.
DR   HOGENOM; HBG444960; -.
DR   HOVERGEN; HBG063184; -.
DR   InParanoid; P21279; -.
DR   OMA; HNKANAN; -.
DR   OrthoDB; EOG4S4PGD; -.
DR   PhylomeDB; P21279; -.
DR   ArrayExpress; P21279; -.
DR   Bgee; P21279; -.
DR   Genevestigator; P21279; -.
DR   GermOnline; ENSMUSG00000024639; Mus musculus.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; TAS:MGI.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; TAS:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0007189; P:activation of adenylate cyclase activity by G-protein signaling pathway; IDA:MGI.
DR   GO; GO:0060158; P:activation of phospholipase C activity by dopamine receptor signaling pathway; IGI:MGI.
DR   GO; GO:0007610; P:behavior; IMP:MGI.
DR   GO; GO:0048066; P:developmental pigmentation; IMP:MGI.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; IGI:MGI.
DR   GO; GO:0021884; P:forebrain neuron development; IMP:MGI.
DR   GO; GO:0007215; P:glutamate signaling pathway; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0016322; P:neuron remodeling; IMP:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0006471; P:protein ADP-ribosylation; IEA:InterPro.
DR   GO; GO:0001508; P:regulation of action potential; IMP:MGI.
DR   GO; GO:0045634; P:regulation of melanocyte differentiation; IMP:MGI.
DR   GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR   InterPro; IPR000654; Gprotein_alpha_Q.
DR   InterPro; IPR001019; Gprotein_alpha_su.
DR   InterPro; IPR011025; GproteinA_insert.
DR   Gene3D; G3DSA:1.10.400.10; GproteinA_insert; 1.
DR   PANTHER; PTHR10218; Gprotein_alph_bd; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00442; GPROTEINAQ.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF47895; Transducn_insert; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing; GTP-binding;
KW   Lipoprotein; Nucleotide-binding; Palmitate; Transducer.
FT   CHAIN         1    359       Guanine nucleotide-binding protein G(q)
FT                                subunit alpha.
FT                                /FTId=PRO_0000203761.
FT   NP_BIND      46     53       GTP (By similarity).
FT   NP_BIND     205    209       GTP (By similarity).
FT   NP_BIND     274    277       GTP (By similarity).
FT   MOD_RES     102    102       N6-acetyllysine (By similarity).
FT   LIPID         9      9       S-palmitoyl cysteine.
FT   LIPID        10     10       S-palmitoyl cysteine.
FT   MUTAGEN       9      9       C->S: Abolishes palmitoylation.
FT   MUTAGEN      10     10       C->S: Abolishes palmitoylation.
FT   CONFLICT     28     29       QL -> HV (in Ref. 1; AAA63306).
FT   CONFLICT     62     62       Missing (in Ref. 2; AAH57583).
FT   STRAND       39     45
FT   STRAND       47     51
FT   HELIX        52     63
FT   HELIX        69     73
FT   HELIX        76     96
FT   HELIX       106    114
FT   TURN        118    120
FT   HELIX       126    137
FT   HELIX       139    146
FT   HELIX       148    150
FT   HELIX       157    162
FT   HELIX       164    168
FT   HELIX       176    181
FT   STRAND      190    196
FT   STRAND      199    205
FT   HELIX       210    212
FT   HELIX       215    219
FT   STRAND      221    231
FT   HELIX       232    236
FT   HELIX       247    260
FT   STRAND      267    274
FT   HELIX       276    282
FT   TURN        283    285
FT   TURN        289    291
FT   HELIX       302    315
FT   STRAND      325    328
FT   HELIX       334    354
SQ   SEQUENCE   359 AA;  42158 MW;  3BCBA4EE7DADADBF CRC64;
     MTLESIMACC LSEEAKEARR INDEIERQLR RDKRDARREL KLLLLGTGES GKSTFIKQMR
     IIHGSGYSDE DKRGFTKLVY QNIFTAMQAM IRAMDTLKIP YKYEHNKAHA QLVREVDVEK
     VSAFENPYVD AIKSLWNDPG IQECYDRRRE YQLSDSTKYY LNDLDRVADP SYLPTQQDVL
     RVRVPTTGII EYPFDLQSVI FRMVDVGGQR SERRKWIHCF ENVTSIMFLV ALSEYDQVLV
     ESDNENRMEE SKALFRTIIT YPWFQNSSVI LFLNKKDLLE EKIMYSHLVD YFPEYDGPQR
     DAQAAREFIL KMFVDLNPDS DKIIYSHFTC ATDTENIRFV FAAVKDTILQ LNLKEYNLV
//
ID   ENOB_MOUSE              Reviewed;         434 AA.
AC   P21550;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 115.
DE   RecName: Full=Beta-enolase;
DE            EC=4.2.1.11;
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE   AltName: Full=Enolase 3;
DE   AltName: Full=Muscle-specific enolase;
DE            Short=MSE;
DE   AltName: Full=Skeletal muscle enolase;
GN   Name=Eno3; Synonyms=Eno-3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=BALB/c, and Swiss Webster; TISSUE=Liver, and Skeletal muscle;
RA   Lamande N., Brosset S., Keller A., Lucas M., Lazar M.;
RL   Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C3H;
RX   MEDLINE=92290133; PubMed=1339335; DOI=10.1016/0012-1606(92)90201-Q;
RA   Peterson C.A., Cho M., Rastinejad F., Blau H.M.;
RT   "Beta-enolase is a marker of human myoblast heterogeneity prior to
RT   differentiation.";
RL   Dev. Biol. 151:626-629(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 33-50; 104-120; 257-262; 336-358 AND 373-394, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 59-434.
RX   MEDLINE=89282789; PubMed=2734297; DOI=10.1073/pnas.86.12.4445;
RA   Lamande N., Mazo A.M., Lucas M., Montarras D., Pinset C., Gros F.,
RA   Legault-Demare L., Lazar M.;
RT   "Murine muscle-specific enolase: cDNA cloning, sequence, and
RT   developmental expression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:4445-4449(1989).
RN   [7]
RP   ACTIVATION DURING MYOGENESIS.
RX   PubMed=1525038; DOI=10.1016/0925-4773(92)90037-K;
RA   Keller A., Ott M.O., Lamande N., Lucas M., Gros F., Buckingham M.,
RA   Lazar M.;
RT   "Activation of the gene encoding the glycolytic enzyme beta-enolase
RT   during early myogenesis precedes an increased expression during fetal
RT   muscle development.";
RL   Mech. Dev. 38:41-54(1992).
RN   [8]
RP   DEVELOPMENTAL STAGE.
RX   MEDLINE=96134716; PubMed=8594891;
RA   Keller A., Rouzeau J.-D., Farhadian F., Wisnewsky C., Marotte F.,
RA   Lamande N., Samuel J.L., Schwartz K., Lazar M., Lucas M.;
RT   "Differential expression of alpha- and beta-enolase genes during rat
RT   heart development and hypertrophy.";
RL   Am. J. Physiol. 269:H1843-H1851(1995).
RN   [9]
RP   INTERACTION WITH PKM2; PGM; CKM; ALDO AND TROPONIN, AND DEVELOPMENTAL
RP   STAGE.
RX   MEDLINE=97270626; PubMed=9169614;
RA   Merkulova T., Lucas M., Jabet C., Lamande N., Rouzeau J.-D., Gros F.,
RA   Lazar M., Keller A.;
RT   "Biochemical characterization of the mouse muscle-specific enolase:
RT   developmental changes in electrophoretic variants and selective
RT   binding to other proteins.";
RL   Biochem. J. 323:791-800(1997).
RN   [10]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   MEDLINE=21121273; PubMed=11229603; DOI=10.1016/S0248-4900(00)01103-5;
RA   Keller A., Demeurie J., Merkulova T., Geraud G., Cywiner-Golenzer C.,
RA   Lucas M., Chatelet F.-P.;
RT   "Fibre-type distribution and subcellular localisation of alpha and
RT   beta enolase in mouse striated muscle.";
RL   Biol. Cell 92:527-535(2000).
RN   [11]
RP   EXPRESSION REGULATION.
RX   PubMed=10848992; DOI=10.1046/j.1432-1327.2000.01408.x;
RA   Merkulova T., Dehaupas M., Nevers M.C., Creminon C., Alameddine H.,
RA   Keller A.;
RT   "Differential modulation of alpha, beta and gamma enolase isoforms in
RT   regenerating mouse skeletal muscle.";
RL   Eur. J. Biochem. 267:3735-3743(2000).
CC   -!- FUNCTION: Appears to have a function in striated muscle
CC       development and regeneration.
CC   -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate +
CC       H(2)O.
CC   -!- COFACTOR: Magnesium. Required for catalysis and for stabilizing
CC       the dimer.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5.
CC   -!- SUBUNIT: Mammalian enolase is composed of 3 isozyme subunits,
CC       alpha, beta and gamma, which can form homodimers or heterodimers
CC       which are cell-type and development-specific. In vitro, interacts
CC       with several glycolytic enzymes including PKM2, PGM, CKM and ALDO.
CC       Also binds PLG and troponin, in vitro. Interacts with PNKD (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Localized to the Z line.
CC       Some colocalization with CKM at M-band (By similarity).
CC   -!- TISSUE SPECIFICITY: The alpha/alpha homodimer is expressed in
CC       embryo and in most adult tissues. The alpha/beta heterodimer and
CC       the beta/beta homodimer are found in striated muscle, and the
CC       alpha/gamma heterodimer and the gamma/gamma homodimer in neurons.
CC       In striated muscle, the fiber-type order of ENO3 expression is IIB
CC       > IIX > IIA > I.
CC   -!- DEVELOPMENTAL STAGE: During ontogenesis, there is a transition
CC       from the alpha/alpha homodimer to the alpha/beta heterodimer in
CC       striated muscle cells, and to the alpha/gamma heterodimer in nerve
CC       cells. In hindleg muscle, first expressed at E15 after which,
CC       levels increase sharply between E15 and E17. A steep prenatal rise
CC       in expression accompanies the formation of secondary myofibers and
CC       the development of innervation. High levels continue throughout
CC       newborn and adult stages. Beginning at postnatal day 5, a second
CC       sharp increase in expression correlates with the definitive
CC       specialization of the myofibers. Later in development, mainly
CC       expressed in fast-twitch fibers. In cardiac muscle, first
CC       expressed in the embryo in the cardiac tube.
CC   -!- INDUCTION: Levels decrease in degenerating myofibers, and increase
CC       with their regeneration.
CC   -!- SIMILARITY: Belongs to the enolase family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X61600; CAA43797.1; -; Genomic_DNA.
DR   EMBL; X57747; CAA40913.1; -; mRNA.
DR   EMBL; X62667; CAA44540.1; -; mRNA.
DR   EMBL; AK002485; BAB22137.1; -; mRNA.
DR   EMBL; BC013460; AAH13460.1; -; mRNA.
DR   EMBL; M20745; AAA37554.1; -; mRNA.
DR   IPI; IPI00228548; -.
DR   PIR; S17109; NOMSB.
DR   RefSeq; NP_001129534.1; NM_001136062.1.
DR   RefSeq; NP_031959.1; NM_007933.2.
DR   UniGene; Mm.251322; -.
DR   ProteinModelPortal; P21550; -.
DR   SMR; P21550; 1-434.
DR   STRING; P21550; -.
DR   PhosphoSite; P21550; -.
DR   SWISS-2DPAGE; P21550; -.
DR   UCD-2DPAGE; P21550; -.
DR   PRIDE; P21550; -.
DR   Ensembl; ENSMUST00000072841; ENSMUSP00000072620; ENSMUSG00000060600.
DR   Ensembl; ENSMUST00000108548; ENSMUSP00000104188; ENSMUSG00000060600.
DR   GeneID; 13808; -.
DR   KEGG; mmu:13808; -.
DR   UCSC; uc007jvx.1; mouse.
DR   CTD; 13808; -.
DR   MGI; MGI:95395; Eno3.
DR   eggNOG; roNOG10078; -.
DR   HOGENOM; HBG726599; -.
DR   HOVERGEN; HBG000067; -.
DR   InParanoid; P21550; -.
DR   OMA; GELYKNF; -.
DR   OrthoDB; EOG4T783B; -.
DR   PhylomeDB; P21550; -.
DR   BRENDA; 4.2.1.11; 244.
DR   NextBio; 284592; -.
DR   ArrayExpress; P21550; -.
DR   Bgee; P21550; -.
DR   CleanEx; MM_ENO3; -.
DR   Genevestigator; P21550; -.
DR   GermOnline; ENSMUSG00000060600; Mus musculus.
DR   GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR000941; Enolase.
DR   InterPro; IPR020810; Enolase_C.
DR   InterPro; IPR020809; Enolase_CS.
DR   InterPro; IPR020811; Enolase_N.
DR   Pfam; PF00113; Enolase_C; 1.
DR   Pfam; PF03952; Enolase_N; 1.
DR   PIRSF; PIRSF001400; Enolase; 1.
DR   PRINTS; PR00148; ENOLASE.
DR   TIGRFAMs; TIGR01060; eno; 1.
DR   PROSITE; PS00164; ENOLASE; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Glycolysis; Lyase; Magnesium;
KW   Metal-binding.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    434       Beta-enolase.
FT                                /FTId=PRO_0000134108.
FT   REGION      370    373       Substrate binding (By similarity).
FT   ACT_SITE    210    210       Proton donor (By similarity).
FT   ACT_SITE    343    343       Proton acceptor (By similarity).
FT   METAL       245    245       Magnesium (By similarity).
FT   METAL       293    293       Magnesium (By similarity).
FT   METAL       318    318       Magnesium (By similarity).
FT   BINDING     158    158       Substrate (By similarity).
FT   BINDING     167    167       Substrate (By similarity).
FT   BINDING     293    293       Substrate (By similarity).
FT   BINDING     318    318       Substrate (By similarity).
FT   BINDING     394    394       Substrate (By similarity).
FT   CONFLICT    234    235       AG -> NA (in Ref. 6; AAA37554).
SQ   SEQUENCE   434 AA;  47025 MW;  A1F757D83709D2B8 CRC64;
     MAMQKIFARE ILDSRGNPTV EVDLHTAKGR FRAAVPSGAS TGIYEALELR DGDKARYLGK
     GVLKAVEHIN KTLGPALLEK KLSVVDQEKV DKFMIELDGT ENKSKFGANA ILGVSLAVCK
     AGAAEKGVPL YRHIADLAGN PDLVLPVPAF NVINGGSHAG NKLAMQEFMI LPVGASSFKE
     AMRIGAEVYH HLKGVIKAKY GKDATNVGDE GGFAPNILEN NEALELLKTA IQAAGYPDKV
     VIGMDVAASE FYRNGKYDLD FKSPDDPARH ISGEKLGELY KNFIQNYPVV SIEDPFDQDD
     WATWTSFLSG VDIQIVGDDL TVTNPKRIAQ AVEKKACNCL LLKVNQIGSV TESIQACKLA
     QSNGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL MRIEEALGDK
     AVFAGRKFRN PKAK
//
ID   LMNB2_MOUSE             Reviewed;         596 AA.
AC   P21619; P48680; Q8CGB1;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 2.
DT   08-MAR-2011, entry version 104.
DE   RecName: Full=Lamin-B2;
DE   Flags: Precursor;
GN   Name=Lmnb2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B2).
RX   MEDLINE=91106216; PubMed=2102682; DOI=10.1007/BF01726689;
RA   Hoeger T.H., Zatloukal K., Waizenegger I., Krohne G.;
RT   "Characterization of a second highly conserved B-type lamin present in
RT   cells previously thought to contain only a single B-type lamin.";
RL   Chromosoma 99:379-390(1990).
RN   [2]
RP   ERRATUM.
RX   MEDLINE=91339548; PubMed=2102440; DOI=10.1007/BF00337604;
RA   Hoeger T.H., Zatloukal K., Waizenegger I., Krohne G.;
RL   Chromosoma 100:67-69(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B3).
RX   MEDLINE=93154351; PubMed=8094052;
RA   Furukawa K., Hotta Y.;
RT   "cDNA cloning of a germ cell specific lamin B3 from mouse
RT   spermatocytes and analysis of its function by ectopic expression in
RT   somatic cells.";
RL   EMBO J. 12:97-106(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 165-172; 254-262 AND 482-491.
RX   PubMed=1939065;
RA   Kasahara K., Chida K., Tsunenaga M., Kohno Y., Ikuta T., Kuroki T.;
RT   "Identification of lamin B2 as a substrate of protein kinase C in
RT   BALB/MK-2 mouse keratinocytes.";
RL   J. Biol. Chem. 266:20018-20023(1991).
RN   [6]
RP   PROTEIN SEQUENCE OF 182-206; 234-286; 290-319; 364-401 AND 470-496.
RX   PubMed=2311764; DOI=10.1016/0014-5793(90)80592-7;
RA   Weber K., Plessmann U., Traub P.;
RT   "Protein chemical analysis of purified murine lamin B identifies two
RT   distinct polypeptides B1 and B2.";
RL   FEBS Lett. 261:361-364(1990).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [8]
RP   INTERACTION WITH TMEM43.
RX   PubMed=18230648; DOI=10.1242/jcs.019281;
RA   Bengtsson L., Otto H.;
RT   "LUMA interacts with emerin and influences its distribution at the
RT   inner nuclear membrane.";
RL   J. Cell Sci. 121:536-548(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-494, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Lamins are components of the nuclear lamina, a fibrous
CC       layer on the nucleoplasmic side of the inner nuclear membrane,
CC       which is thought to provide a framework for the nuclear envelope
CC       and may also interact with chromatin.
CC   -!- SUBUNIT: Interacts with TMEM43.
CC   -!- SUBCELLULAR LOCATION: Nucleus inner membrane; Lipid-anchor;
CC       Nucleoplasmic side.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=B2;
CC         IsoId=P21619-1; Sequence=Displayed;
CC       Name=B3;
CC         IsoId=P21619-2, P48680-1;
CC         Sequence=VSP_017070;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Isoform B3 is germ cell specific.
CC   -!- PTM: B-type lamins undergo a series of modifications, such as
CC       farnesylation and phosphorylation. Increased phosphorylation of
CC       the lamins occurs before envelope disintegration and probably
CC       plays a role in regulating lamin associations.
CC   -!- MISCELLANEOUS: The structural integrity of the lamina is strictly
CC       controlled by the cell cycle, as seen by the disintegration and
CC       formation of the nuclear envelope in prophase and telophase,
CC       respectively.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH42430.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC       Sequence=AAH51985.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; X54098; CAA38032.1; -; mRNA.
DR   EMBL; D13455; BAA02708.1; -; mRNA.
DR   EMBL; BC042430; AAH42430.1; ALT_INIT; mRNA.
DR   EMBL; BC051985; AAH51985.1; ALT_INIT; mRNA.
DR   IPI; IPI00113886; -.
DR   IPI; IPI00126191; -.
DR   PIR; B48315; B48315.
DR   PIR; S28419; S28419.
DR   RefSeq; NP_034852.2; NM_010722.5.
DR   UniGene; Mm.7362; -.
DR   ProteinModelPortal; P21619; -.
DR   SMR; P21619; 23-59, 66-213, 234-301, 307-379, 447-551.
DR   STRING; P21619; -.
DR   PhosphoSite; P21619; -.
DR   PRIDE; P21619; -.
DR   Ensembl; ENSMUST00000057623; ENSMUSP00000057291; ENSMUSG00000062075.
DR   Ensembl; ENSMUST00000105332; ENSMUSP00000100969; ENSMUSG00000062075.
DR   GeneID; 16907; -.
DR   KEGG; mmu:16907; -.
DR   UCSC; uc007gfk.1; mouse.
DR   CTD; 16907; -.
DR   MGI; MGI:96796; Lmnb2.
DR   eggNOG; roNOG13933; -.
DR   GeneTree; ENSGT00560000076873; -.
DR   HOGENOM; HBG716303; -.
DR   HOVERGEN; HBG013015; -.
DR   InParanoid; P21619; -.
DR   OMA; ARLQIEI; -.
DR   OrthoDB; EOG4ZCT4D; -.
DR   NextBio; 290944; -.
DR   ArrayExpress; P21619; -.
DR   Bgee; P21619; -.
DR   CleanEx; MM_LMNB2; -.
DR   Genevestigator; P21619; -.
DR   GermOnline; ENSMUSG00000062075; Mus musculus.
DR   GO; GO:0005638; C:lamin filament; IDA:MGI.
DR   GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR016044; F.
DR   InterPro; IPR001664; IF.
DR   InterPro; IPR001322; IF_tail_C.
DR   InterPro; IPR018039; Intermediate_filament_CS.
DR   PANTHER; PTHR23239; IF; 1.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF00932; IF_tail; 1.
DR   PROSITE; PS00226; IF; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil;
KW   Direct protein sequencing; Intermediate filament; Lipoprotein;
KW   Membrane; Methylation; Nucleus; Phosphoprotein; Prenylation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    593       Lamin-B2.
FT                                /FTId=PRO_0000063821.
FT   PROPEP      594    596       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000403471.
FT   REGION        2     26       Head.
FT   REGION       27    378       Rod.
FT   REGION       27     61       Coil 1A.
FT   REGION       62     73       Linker 1.
FT   REGION       74    207       Coil 1B.
FT   REGION      208    234       Linker 2.
FT   REGION      235    378       Coil 2.
FT   REGION      379    596       Tail.
FT   MOTIF       415    420       Nuclear localization signal (Potential).
FT   COMPBIAS    565    578       Asp/Glu-rich (highly acidic; could be
FT                                involved in chromatin binding).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      12     12       Phosphothreonine (By similarity).
FT   MOD_RES      15     15       Phosphoserine (By similarity).
FT   MOD_RES      17     17       Phosphothreonine (By similarity).
FT   MOD_RES      25     25       N6-acetyllysine (By similarity).
FT   MOD_RES      59     59       N6-acetyllysine (By similarity).
FT   MOD_RES     371    371       N6-acetyllysine (By similarity).
FT   MOD_RES     383    383       Phosphoserine (By similarity).
FT   MOD_RES     385    385       Phosphoserine (By similarity).
FT   MOD_RES     387    387       Phosphoserine (By similarity).
FT   MOD_RES     397    397       Phosphoserine (By similarity).
FT   MOD_RES     399    399       Phosphoserine (By similarity).
FT   MOD_RES     400    400       Phosphoserine (By similarity).
FT   MOD_RES     402    402       Phosphoserine (By similarity).
FT   MOD_RES     427    427       Phosphoserine.
FT   MOD_RES     494    494       Phosphothreonine.
FT   MOD_RES     496    496       N6-acetyllysine (By similarity).
FT   MOD_RES     593    593       Cysteine methyl ester (By similarity).
FT   LIPID       593    593       S-farnesyl cysteine (By similarity).
FT   VAR_SEQ       1    206       MASLPPHAGPATPLSPTRLSRLQEKEELRELNDRLAHYIDR
FT                                VRALELENDRLLLRISEKEEVTTREVSGIKTLYESELADAR
FT                                RVLDETARERARLQIEIGKVQAELEEARKSAKKREGELTVA
FT                                QGRVKDLESLFHRSEAELATALSDKQGLETEVAELRAQLAK
FT                                AEDGHAVAKKQLEKETLMRVDLENRCQSLQEELAFSKSVFE
FT                                E -> MGESESMRGTGEGCGRDCPEAARPLMETVEGALPEL
FT                                RGRPLREYVKRRPRGLGKTPVEDPVKSEGAVGYPRTWNNHL
FT                                RVPTREQ (in isoform B3).
FT                                /FTId=VSP_017070.
FT   CONFLICT    148    149       KQ -> NE (in Ref. 1; CAA38032).
FT   CONFLICT    314    314       H -> R (in Ref. 6; AA sequence).
FT   CONFLICT    321    321       A -> R (in Ref. 1; CAA38032).
FT   CONFLICT    344    344       A -> R (in Ref. 1; CAA38032).
FT   CONFLICT    403    403       Missing (in Ref. 1; CAA38032).
FT   CONFLICT    412    413       GR -> RG (in Ref. 1; CAA38032).
FT   CONFLICT    421    422       Missing (in Ref. 1).
FT   CONFLICT    443    443       Missing (in Ref. 1; CAA38032).
SQ   SEQUENCE   596 AA;  67318 MW;  4FEF5A76FFDF2D96 CRC64;
     MASLPPHAGP ATPLSPTRLS RLQEKEELRE LNDRLAHYID RVRALELEND RLLLRISEKE
     EVTTREVSGI KTLYESELAD ARRVLDETAR ERARLQIEIG KVQAELEEAR KSAKKREGEL
     TVAQGRVKDL ESLFHRSEAE LATALSDKQG LETEVAELRA QLAKAEDGHA VAKKQLEKET
     LMRVDLENRC QSLQEELAFS KSVFEEEVRE TRRRHERRLV EVDSSRQQEY DFKMAQALED
     LRSQHDEQVR LYRVELEQTY QAKLDNAKLL SDQNDKAAHA AREELKEARM RVESLSYQLL
     GLQKQASAAE NHIHELEEAL AGERDKFRKM LDAKEQEMTE VRDAMQQQLA EYQELLDIKL
     ALDMEISAYR KLLEGEEERL KLSPSPSSRI TISRATSSSS SSSGVGMSVG QGRGKRRRLE
     TEDTSGSPSR ASRVSSGSRL AQQTVATGVV NIDEVDPEGR FVRLKNSSDK DQSLGNWRIK
     RQVLEGEDIA YKFTPKYVLR AGQTVTVWAA GAGATHSPPS TLVWKSQTNW GPGESFRTAL
     VSADGEEVAV KAAKHSSVQG RENGEEEEEE EAEFGEEDLF HQQGDPRTTS RGCRLM
//
ID   NEC2_MOUSE              Reviewed;         637 AA.
AC   P21661; Q80WU1;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   08-MAR-2011, entry version 106.
DE   RecName: Full=Neuroendocrine convertase 2;
DE            Short=NEC 2;
DE            EC=3.4.21.94;
DE   AltName: Full=KEX2-like endoprotease 2;
DE   AltName: Full=Prohormone convertase 2;
DE   AltName: Full=Proprotein convertase 2;
DE            Short=PC2;
DE   Flags: Precursor;
GN   Name=Pcsk2; Synonyms=Nec-2, Nec2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   MEDLINE=91000356; PubMed=2169760; DOI=10.1089/dna.1990.9.415;
RA   Seidah N.G., Gaspar L., Mion P., Marcinkiewicz M., Mbikay M.,
RA   Chretien M.;
RT   "cDNA sequence of two distinct pituitary proteins homologous to Kex2
RT   and furin gene products: tissue-specific mRNAs encoding candidates for
RT   pro-hormone processing proteinases.";
RL   DNA Cell Biol. 9:415-424(1990).
RN   [2]
RP   ERRATUM.
RX   MEDLINE=91090850; PubMed=2264933; DOI=10.1089/dna.1990.9.789;
RA   Seidah N.G., Gaspar L., Mion P., Marcinkiewicz M., Mbikay M.,
RA   Chretien M.;
RL   DNA Cell Biol. 9:789-789(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Involved in the processing of hormone and other protein
CC       precursors at sites comprised of pairs of basic amino acid
CC       residues.
CC   -!- CATALYTIC ACTIVITY: Release of protein hormones and neuropeptides
CC       from their precursors, generally by hydrolysis of -Lys-Arg-|-
CC       bonds.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle.
CC       Note=Localized in the secretion granules.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
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DR   EMBL; M55669; AAA39376.1; -; mRNA.
DR   EMBL; BC052013; AAH52013.2; -; mRNA.
DR   EMBL; BC057348; AAH57348.1; -; mRNA.
DR   IPI; IPI00126390; -.
DR   PIR; B35571; KXMSC2.
DR   RefSeq; NP_032818.1; NM_008792.4.
DR   UniGene; Mm.294493; -.
DR   UniGene; Mm.447466; -.
DR   ProteinModelPortal; P21661; -.
DR   SMR; P21661; 29-101, 118-596.
DR   STRING; P21661; -.
DR   MEROPS; S08.073; -.
DR   PRIDE; P21661; -.
DR   Ensembl; ENSMUST00000028905; ENSMUSP00000028905; ENSMUSG00000027419.
DR   GeneID; 18549; -.
DR   KEGG; mmu:18549; -.
DR   UCSC; uc008mqf.1; mouse.
DR   CTD; 18549; -.
DR   MGI; MGI:97512; Pcsk2.
DR   eggNOG; roNOG07042; -.
DR   HOVERGEN; HBG008705; -.
DR   InParanoid; P21661; -.
DR   OMA; NYNADAS; -.
DR   OrthoDB; EOG46MBJ1; -.
DR   PhylomeDB; P21661; -.
DR   BRENDA; 3.4.21.94; 244.
DR   NextBio; 294342; -.
DR   PMAP-CutDB; P21661; -.
DR   ArrayExpress; P21661; -.
DR   Bgee; P21661; -.
DR   CleanEx; MM_PCSK2; -.
DR   Genevestigator; P21661; -.
DR   GermOnline; ENSMUSG00000027419; Mus musculus.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL.
DR   GO; GO:0034230; P:enkephalin processing; IDA:BHF-UCL.
DR   GO; GO:0007399; P:nervous system development; IEP:HGNC.
DR   GO; GO:0016540; P:protein autoprocessing; IDA:HGNC.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR000209; Peptidase_S8/S53.
DR   InterPro; IPR022398; Peptidase_S8/S53_AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR009020; Prot_inh_propept.
DR   InterPro; IPR002884; PrprotnconvertsP.
DR   Gene3D; G3DSA:3.40.50.200; Pept_S8_S53; 1.
DR   PANTHER; PTHR10795; SubtilSerProt; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49785; Gal_bind_like; 1.
DR   SUPFAM; SSF52743; Pept_S8_S53; 1.
DR   SUPFAM; SSF54897; Prot_inh_propept; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Serine protease;
KW   Signal; Zymogen.
FT   SIGNAL        1     24       Potential.
FT   PROPEP       25    108       Potential.
FT                                /FTId=PRO_0000027067.
FT   CHAIN       109    637       Neuroendocrine convertase 2.
FT                                /FTId=PRO_0000027068.
FT   REGION      121    414       Catalytic.
FT   ACT_SITE    166    166       Charge relay system (By similarity).
FT   ACT_SITE    207    207       Charge relay system (By similarity).
FT   ACT_SITE    383    383       Charge relay system (By similarity).
FT   CARBOHYD    374    374       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    513    513       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    523    523       N-linked (GlcNAc...) (Potential).
FT   DISULFID    224    375       By similarity.
FT   DISULFID    316    346       By similarity.
FT   DISULFID    467    493       By similarity.
SQ   SEQUENCE   637 AA;  70785 MW;  B69F2DCCD00FB0E6 CRC64;
     MEGGCGSQWK AAGFLFCVMV FASAERPVFT NHFLVELHKD GEEEARQVAA EHGFGVRKLP
     FAEGLYHFYH NGLAKAKRRR SLHHKRQLER DPRIKMALQQ EGFDRKKRGY RDINEIDINM
     NDPLFTKQWY LFNTGQADGT PGLDLNVAEA WELGYTGKGV TIGIMDDGID YLHPDLAYNY
     NADASYDFSS NDPYPYPRYT DDWFNSHGTR CAGEVSAAAS NNICGVGVAY NSKVAGIRML
     DQPFMTDIIE ASSISHMPQL IDIYSASWGP TDNGKTVDGP RELTLQAMAD GVNKGRGGKG
     SIYVWASGDG GSYDDCNCDG YASSMWTISI NSAINDGRTA LYDESCSSTL ASTFSNGRKR
     NPEAGVATTD LYGNCTLRHS GTSAAAPEAA GVFALALEAN LDLTWRDMQH LTVLTSKRNQ
     LHDEVHQWRR NGVGLEFNHL FGYGVLDAGA MVKMAKDWKT VPERFHCVGG SVQNPEKIPP
     TGKLVLTLKT NACEGKENFV RYLEHVQAVI TVNATRRGDL NINMTSPMGT KSILLSRRPR
     DDDSKVGFDK WPFMTTHTWG EDARGTWTLE LGFVGSAPQK GLLKEWTLML HGTQSAPYID
     QVVRDYQSKL AMSKKQELEE ELDEAVERSL QSILRKN
//
ID   EMB_MOUSE               Reviewed;         330 AA.
AC   P21995; Q3UFF1; Q8C2J8; Q8C543; Q96C38;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Embigin;
DE   AltName: Full=Teratocarcinoma glycoprotein Gp-70;
DE   Flags: Precursor;
GN   Name=Emb; Synonyms=Gp70;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=88139366; PubMed=2963822;
RA   Ozawa M., Huang R.-P., Furukawa T., Muramatsu T.;
RT   "A teratocarcinoma glycoprotein carrying a developmentally regulated
RT   carbohydrate marker is a member of the immunoglobulin gene
RT   superfamily.";
RL   J. Biol. Chem. 263:3059-3062(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Hypothalamus, Pancreas, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-55; ASN-70; ASN-76;
RP   ASN-101; ASN-118; ASN-198; ASN-210; ASN-216 AND ASN-221, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-55; ASN-62; ASN-76;
RP   ASN-98; ASN-101; ASN-118; ASN-198; ASN-216 AND ASN-221, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: May function as a regulator of cell/ECM interactions
CC       during development and in the homeostasis of normal adult tissues
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Only member of the immunoglobulin superfamily
CC       to be expressed in embryonal carcinoma cells, which resemble
CC       multipotential cells of early embryos.
CC   -!- SIMILARITY: Contains 2 Ig-like V-type (immunoglobulin-like)
CC       domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; J03535; AAA37730.1; -; mRNA.
DR   EMBL; AK079570; BAC37687.1; -; mRNA.
DR   EMBL; AK088480; BAC40381.1; -; mRNA.
DR   EMBL; AK138271; BAE23603.1; -; mRNA.
DR   EMBL; AK148540; BAE28610.1; -; mRNA.
DR   EMBL; AK150625; BAE29715.1; -; mRNA.
DR   EMBL; AK166602; BAE38887.1; -; mRNA.
DR   EMBL; BC014858; AAH14858.1; -; mRNA.
DR   IPI; IPI00129968; -.
DR   PIR; A29915; A29915.
DR   RefSeq; NP_034460.3; NM_010330.4.
DR   UniGene; Mm.274926; -.
DR   ProteinModelPortal; P21995; -.
DR   SMR; P21995; 75-260.
DR   STRING; P21995; -.
DR   PRIDE; P21995; -.
DR   Ensembl; ENSMUST00000022242; ENSMUSP00000022242; ENSMUSG00000021728.
DR   GeneID; 13723; -.
DR   KEGG; mmu:13723; -.
DR   UCSC; uc007rym.1; mouse.
DR   CTD; 13723; -.
DR   MGI; MGI:95321; Emb.
DR   eggNOG; maNOG10882; -.
DR   HOGENOM; HBG127380; -.
DR   HOVERGEN; HBG051471; -.
DR   InParanoid; P21995; -.
DR   OMA; PLNWTWY; -.
DR   OrthoDB; EOG46Q6TB; -.
DR   PhylomeDB; P21995; -.
DR   NextBio; 284508; -.
DR   ArrayExpress; P21995; -.
DR   Bgee; P21995; -.
DR   CleanEx; MM_EMB; -.
DR   Genevestigator; P21995; -.
DR   GermOnline; ENSMUSG00000021728; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Pfam; PF07679; I-set; 1.
DR   SMART; SM00409; IG; 1.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     33       Potential.
FT   CHAIN        34    330       Embigin.
FT                                /FTId=PRO_0000014750.
FT   TOPO_DOM     34    254       Extracellular (Potential).
FT   TRANSMEM    255    283       Helical; (Potential).
FT   TOPO_DOM    284    330       Cytoplasmic (Potential).
FT   DOMAIN       38    161       Ig-like V-type 1.
FT   DOMAIN      162    256       Ig-like V-type 2.
FT   CARBOHYD     55     55       N-linked (GlcNAc...).
FT   CARBOHYD     62     62       N-linked (GlcNAc...).
FT   CARBOHYD     70     70       N-linked (GlcNAc...).
FT   CARBOHYD     76     76       N-linked (GlcNAc...).
FT   CARBOHYD     98     98       N-linked (GlcNAc...).
FT   CARBOHYD    101    101       N-linked (GlcNAc...).
FT   CARBOHYD    118    118       N-linked (GlcNAc...).
FT   CARBOHYD    191    191       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    198    198       N-linked (GlcNAc...).
FT   CARBOHYD    210    210       N-linked (GlcNAc...).
FT   CARBOHYD    216    216       N-linked (GlcNAc...).
FT   CARBOHYD    221    221       N-linked (GlcNAc...).
FT   DISULFID     89    145       By similarity.
FT   DISULFID    182    240       By similarity.
FT   CONFLICT     78     78       I -> S (in Ref. 2; BAC40381).
FT   CONFLICT     98     98       N -> S (in Ref. 2; BAC37687).
FT   CONFLICT     99     99       L -> S (in Ref. 2; BAC40381).
FT   CONFLICT    162    166       KAHGK -> QSSWE (in Ref. 1; AAA37730).
FT   CONFLICT    294    294       D -> G (in Ref. 1; AAA37730).
SQ   SEQUENCE   330 AA;  37064 MW;  FC4D729A993A1EDD CRC64;
     MRSHTGLRAL VAPGYPLLLL CLLAATRPDP AEGDPTDPTF TSLPVREEMM AKYSNLSLKS
     CNISVTEKSN VSVEENVILE KPSHVELKCV YTATKDLNLM NVTWKKDDEP LETTGDFNTT
     KMGNTLTSQY RFIVFNSKQL GKYSCVFGEK ELRGTFNIHV PKAHGKKKSL IAYVGDSTVL
     KCVCQDCLPL NWTWYMGNET AQVPIDAHSN EKYIINGSHA NETRLKIKHL LEEDGGSYWC
     RATFQLGESE EQNELVVLSF LVPLKPFLAI LAEVILLVAI ILLCEVYTHK KKNDPDAGKE
     FEQIEQLKSD DSNGIENNVP RYRKTDSADQ
//
ID   PENK_MOUSE              Reviewed;         268 AA.
AC   P22005; Q68G73;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Proenkephalin-A;
DE   Contains:
DE     RecName: Full=Synenkephalin;
DE   Contains:
DE     RecName: Full=Met-enkephalin;
DE     AltName: Full=Opioid growth factor;
DE              Short=OGF;
DE   Contains:
DE     RecName: Full=PENK(114-133);
DE   Contains:
DE     RecName: Full=PENK(143-184);
DE   Contains:
DE     RecName: Full=Met-enkephalin-Arg-Ser-Leu;
DE   Contains:
DE     RecName: Full=Leu-enkephalin;
DE   Contains:
DE     RecName: Full=PENK(238-259);
DE   Contains:
DE     RecName: Full=Met-enkephalin-Arg-Phe;
DE   Flags: Precursor;
GN   Name=Penk; Synonyms=Penk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   MEDLINE=90287163; PubMed=2355920;
RA   Kilpatrick D.L., Zinn S.A., Fitzgerald M., Higuchi H., Sabol S.L.,
RA   Meyerhardt J.;
RT   "Transcription of the rat and mouse proenkephalin genes is initiated
RT   at distinct sites in spermatogenic and somatic cells.";
RL   Mol. Cell. Biol. 10:3717-3726(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 29-268.
RC   TISSUE=T-cell;
RX   MEDLINE=86179902; PubMed=2938259; DOI=10.1126/science.2938259;
RA   Zurawski G., Benedik M., Kamb B.J., Abrams J.S., Zurawski S.M.,
RA   Lee F.D.;
RT   "Activation of mouse T-helper cells induces abundant preproenkephalin
RT   mRNA synthesis.";
RL   Science 232:772-775(1986).
CC   -!- FUNCTION: Met- and Leu-enkephalins compete with and mimic the
CC       effects of opiate drugs. They play a role in a number of
CC       physiologic functions, including pain perception and responses to
CC       stress. PENK(114-133) and PENK(238-259) increase glutamate release
CC       in the striatum. PENK(114-133) decreases GABA concentration in the
CC       striatum.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Spermatogenic and somatic cells.
CC   -!- DEVELOPMENTAL STAGE: Highest expression in late pachytene
CC       spermatocytes and postmeiotic round spermatids.
CC   -!- PTM: The N-terminal domain contains 6 conserved cysteines thought
CC       to be involved in disulfide bonding and/or processing.
CC   -!- SIMILARITY: Belongs to the opioid neuropeptide precursor family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M55181; AAA40128.1; -; mRNA.
DR   EMBL; AK161272; BAE36283.1; -; mRNA.
DR   EMBL; BX004841; CAM26883.1; -; Genomic_DNA.
DR   EMBL; CH466538; EDL05699.1; -; Genomic_DNA.
DR   EMBL; CH466538; EDL05700.1; -; Genomic_DNA.
DR   EMBL; BC049766; AAH49766.1; -; mRNA.
DR   EMBL; M13227; AAA37553.1; -; mRNA.
DR   IPI; IPI00123302; -.
DR   PIR; B35678; B35678.
DR   RefSeq; NP_001002927.1; NM_001002927.2.
DR   UniGene; Mm.475097; -.
DR   ProteinModelPortal; P22005; -.
DR   STRING; P22005; -.
DR   PhosphoSite; P22005; -.
DR   PRIDE; P22005; -.
DR   Ensembl; ENSMUST00000070375; ENSMUSP00000066822; ENSMUSG00000045573.
DR   Ensembl; ENSMUST00000108381; ENSMUSP00000104018; ENSMUSG00000045573.
DR   GeneID; 18619; -.
DR   KEGG; mmu:18619; -.
DR   CTD; 18619; -.
DR   MGI; MGI:104629; Penk.
DR   eggNOG; roNOG09455; -.
DR   HOGENOM; HBG716475; -.
DR   HOVERGEN; HBG000063; -.
DR   InParanoid; P22005; -.
DR   OMA; GGFMKKD; -.
DR   OrthoDB; EOG4HMJBF; -.
DR   PhylomeDB; P22005; -.
DR   ArrayExpress; P22005; -.
DR   Bgee; P22005; -.
DR   CleanEx; MM_PENK1; -.
DR   Genevestigator; P22005; -.
DR   GermOnline; ENSMUSG00000045573; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0001515; F:opioid peptide activity; IEA:UniProtKB-KW.
DR   GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR   InterPro; IPR006024; Opioid_neupept.
DR   InterPro; IPR000703; Proenkphlin_A.
DR   PANTHER; PTHR11438; Opioid_neupept; 1.
DR   PANTHER; PTHR11438:SF3; Proenkphlin_A; 1.
DR   Pfam; PF01160; Opiods_neuropep; 1.
DR   PRINTS; PR01028; OPIOIDPRCRSR.
DR   PRINTS; PR01029; PENKAPRCRSR.
DR   PROSITE; PS01252; OPIOIDS_PRECURSOR; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Disulfide bond; Endorphin;
KW   Neuropeptide; Opioid peptide; Secreted; Signal.
FT   SIGNAL        1     24
FT   PEPTIDE      25     97       Synenkephalin.
FT                                /FTId=PRO_0000008268.
FT   PEPTIDE     100    104       Met-enkephalin.
FT                                /FTId=PRO_0000008269.
FT   PEPTIDE     107    111       Met-enkephalin.
FT                                /FTId=PRO_0000008270.
FT   PEPTIDE     114    133       PENK(114-133) (By similarity).
FT                                /FTId=PRO_0000377694.
FT   PEPTIDE     136    140       Met-enkephalin.
FT                                /FTId=PRO_0000008272.
FT   PEPTIDE     143    184       PENK(143-184) (By similarity).
FT                                /FTId=PRO_0000377695.
FT   PEPTIDE     187    194       Met-enkephalin-Arg-Ser-Leu.
FT                                /FTId=PRO_0000008274.
FT   PROPEP      197    208
FT                                /FTId=PRO_0000008275.
FT   PEPTIDE     211    215       Met-enkephalin.
FT                                /FTId=PRO_0000008276.
FT   PROPEP      218    228
FT                                /FTId=PRO_0000008277.
FT   PEPTIDE     231    235       Leu-enkephalin.
FT                                /FTId=PRO_0000008278.
FT   PEPTIDE     238    259       PENK(238-259) (By similarity).
FT                                /FTId=PRO_0000377696.
FT   PEPTIDE     262    268       Met-enkephalin-Arg-Phe.
FT                                /FTId=PRO_0000008280.
FT   DISULFID     26     48       By similarity.
FT   DISULFID     30     52       By similarity.
FT   DISULFID     33     65       By similarity.
FT   CONFLICT     34     34       S -> T (in Ref. 1; AAA40128).
FT   CONFLICT    184    184       S -> SS (in Ref. 1; AAA40128).
SQ   SEQUENCE   268 AA;  31004 MW;  637F848B49F44013 CRC64;
     MARFLRLCTW LLALGSCLLA TVQAECSQDC AKCSYRLVRP GDINFLACTL ECEGQLPSFK
     IWETCKDLLQ VSRPEFPWDN IDMYKDSSKQ DESHLLAKKY GGFMKRYGGF MKKMDELYPM
     EPEEEANGGE ILAKRYGGFM KKDADEGDTL ANSSDLLKEL LGTGDNRAKD SHQQESTNND
     EDMSKRYGGF MRSLKRSPQL EDEAKELQKR YGGFMRRVGR PEWWMDYQKR YGGFLKRFAE
     SLPSDEEGEN YSKEVPEIEK RYGGFMRF
//
ID   GBRG2_MOUSE             Reviewed;         474 AA.
AC   P22723; Q91V50; Q91VA8;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 3.
DT   08-MAR-2011, entry version 114.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit gamma-2;
DE   AltName: Full=GABA(A) receptor subunit gamma-2;
DE   Flags: Precursor;
GN   Name=Gabrg2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2L AND 2S).
RX   MEDLINE=91108470; PubMed=1846404;
RX   DOI=10.1111/j.1471-4159.1991.tb08209.x;
RA   Kofuji P., Wang J.B., Moss S.J., Huganir R.L., Burt D.R.;
RT   "Generation of two forms of the gamma-aminobutyric acidA receptor
RT   gamma 2-subunit in mice by alternative splicing.";
RL   J. Neurochem. 56:713-715(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2L).
RA   Sikela J.M., Shaw W.D., Khan A.S., Lin L.-H., Leidenheimer G.,
RA   Siegel R.E.;
RL   Submitted (APR-1991) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2L).
RC   STRAIN=C57BL/6J, DBA/2J, and Various BXD strains; TISSUE=Brain;
RX   MEDLINE=20456530; PubMed=11003197;
RX   DOI=10.1097/00000374-200009000-00002;
RA   Hood H.M., Buck K.J.;
RT   "Allelic variation in the GABA A receptor gamma2 subunit is associated
RT   with genetic susceptibility to ethanol-induced motor incoordination
RT   and hypothermia, conditioned taste aversion, and withdrawal in BXD/Ty
RT   recombinant inbred mice.";
RL   Alcohol. Clin. Exp. Res. 24:1327-1334(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2L).
RC   TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PALMITOYLATION.
RX   PubMed=15229235; DOI=10.1523/JNEUROSCI.1037-04.2004;
RA   Keller C.A., Yuan X., Panzanelli P., Martin M.L., Alldred M.,
RA   Sassoe-Pognetto M., Luescher B.;
RT   "The gamma2 subunit of GABA(A) receptors is a substrate for
RT   palmitoylation by GODZ.";
RL   J. Neurosci. 24:5881-5891(2004).
RN   [6]
RP   PALMITOYLATION.
RX   PubMed=15207850; DOI=10.1016/j.mcn.2004.01.012;
RA   Rathenberg J., Kittler J.T., Moss S.J.;
RT   "Palmitoylation regulates the clustering and cell surface stability of
RT   GABAA receptors.";
RL   Mol. Cell. Neurosci. 26:251-257(2004).
CC   -!- FUNCTION: GABA, the major inhibitory neurotransmitter in the
CC       vertebrate brain, mediates neuronal inhibition by binding to the
CC       GABA/benzodiazepine receptor and opening an integral chloride
CC       channel.
CC   -!- SUBUNIT: Generally pentameric. There are five types of GABA(A)
CC       receptor chains: alpha, beta, gamma, delta, and rho.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane; Multi-pass membrane protein. Cell membrane; Multi-pass
CC       membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2L;
CC         IsoId=P22723-1; Sequence=Displayed;
CC       Name=2S;
CC         IsoId=P22723-2; Sequence=VSP_000091;
CC   -!- PTM: Palmitoylated by ZDHHC3/GODZ; which may affect presynaptic
CC       clustering and/or cell surface stability.
CC   -!- MISCELLANEOUS: This subunit carries the benzodiazepine binding
CC       site.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
CC       family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily.
CC       GABRG2 sub-subfamily.
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DR   EMBL; M86572; AAB59635.1; -; mRNA.
DR   EMBL; M62374; AAA37653.1; -; mRNA.
DR   EMBL; AF233775; AAK71573.1; -; mRNA.
DR   EMBL; AF233776; AAK71574.1; -; mRNA.
DR   EMBL; AF233777; AAK71575.1; -; mRNA.
DR   EMBL; AF233778; AAK71576.1; -; mRNA.
DR   EMBL; AF233779; AAK71577.1; -; mRNA.
DR   EMBL; AF233780; AAK71578.1; -; mRNA.
DR   EMBL; AF233781; AAK71579.1; -; mRNA.
DR   EMBL; AF233782; AAK71580.1; -; mRNA.
DR   EMBL; AF233783; AAK71581.1; -; mRNA.
DR   EMBL; AF233784; AAK71582.1; -; mRNA.
DR   EMBL; AF233785; AAK71583.1; -; mRNA.
DR   EMBL; AF233786; AAK71584.1; -; mRNA.
DR   EMBL; AF233787; AAK71585.1; -; mRNA.
DR   EMBL; AF233788; AAK71586.1; -; mRNA.
DR   EMBL; AF233789; AAK71587.1; -; mRNA.
DR   EMBL; AF233790; AAK71588.1; -; mRNA.
DR   EMBL; AF233791; AAK71589.1; -; mRNA.
DR   EMBL; AF233792; AAK71590.1; -; mRNA.
DR   EMBL; AF233793; AAK71591.1; -; mRNA.
DR   EMBL; AF233794; AAK71592.1; -; mRNA.
DR   EMBL; AF233795; AAK71593.1; -; mRNA.
DR   EMBL; AF233796; AAK71594.1; -; mRNA.
DR   EMBL; AF233797; AAK71595.1; -; mRNA.
DR   EMBL; AF233798; AAK71596.1; -; mRNA.
DR   EMBL; AF233799; AAK71597.1; -; mRNA.
DR   EMBL; AF233800; AAK71598.1; -; mRNA.
DR   EMBL; AF233801; AAK71599.1; -; mRNA.
DR   EMBL; AF233802; AAK71600.1; -; mRNA.
DR   EMBL; BC031762; AAH31762.1; -; mRNA.
DR   IPI; IPI00131369; -.
DR   IPI; IPI00228358; -.
DR   PIR; JH0316; JH0316.
DR   PIR; JH0317; JH0317.
DR   RefSeq; NP_032099.1; NM_008073.2.
DR   UniGene; Mm.5309; -.
DR   ProteinModelPortal; P22723; -.
DR   SMR; P22723; 300-357.
DR   DIP; DIP-48995N; -.
DR   STRING; P22723; -.
DR   PhosphoSite; P22723; -.
DR   PRIDE; P22723; -.
DR   Ensembl; ENSMUST00000070725; ENSMUSP00000064739; ENSMUSG00000020436.
DR   Ensembl; ENSMUST00000070735; ENSMUSP00000063812; ENSMUSG00000020436.
DR   GeneID; 14406; -.
DR   KEGG; mmu:14406; -.
DR   UCSC; uc007imb.1; mouse.
DR   CTD; 14406; -.
DR   MGI; MGI:95623; Gabrg2.
DR   eggNOG; roNOG07684; -.
DR   HOGENOM; HBG506497; -.
DR   HOVERGEN; HBG051707; -.
DR   InParanoid; P22723; -.
DR   OMA; WSTGSSV; -.
DR   OrthoDB; EOG44BB25; -.
DR   PhylomeDB; P22723; -.
DR   NextBio; 285971; -.
DR   ArrayExpress; P22723; -.
DR   Bgee; P22723; -.
DR   Genevestigator; P22723; -.
DR   GermOnline; ENSMUSG00000020436; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0004890; F:GABA-A receptor activity; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0030534; P:adult behavior; IMP:MGI.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IDA:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0007268; P:synaptic transmission; IDA:MGI.
DR   InterPro; IPR006028; GABAA_rcpt.
DR   InterPro; IPR005439; GABBAg2_rcpt.
DR   InterPro; IPR005437; GABBAg_rcpt.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   Gene3D; G3DSA:2.70.170.10; Neur_chan_lig_bd; 1.
DR   PANTHER; PTHR18945; Neur_channel; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR00253; GABAARECEPTR.
DR   PRINTS; PR01620; GABAARGAMMA.
DR   PRINTS; PR01622; GABAARGAMMA2.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF90112; Neu_channel_TM; 1.
DR   SUPFAM; SSF63712; Neur_chan_LBD; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Chloride;
KW   Chloride channel; Disulfide bond; Glycoprotein; Ion transport;
KW   Ionic channel; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Postsynaptic cell membrane; Signal; Synapse; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     38       Potential.
FT   CHAIN        39    474       Gamma-aminobutyric acid receptor subunit
FT                                gamma-2.
FT                                /FTId=PRO_0000000478.
FT   TOPO_DOM     39    272       Extracellular (Probable).
FT   TRANSMEM    273    295       Helical; (Probable).
FT   TRANSMEM    299    321       Helical; (Probable).
FT   TRANSMEM    333    355       Helical; (Probable).
FT   TOPO_DOM    356    450       Cytoplasmic (Probable).
FT   TRANSMEM    451    474       Helical; (Probable).
FT   MOD_RES     381    381       Phosphoserine; by PKC (Probable).
FT   CARBOHYD     51     51       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    128    128       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    246    246       N-linked (GlcNAc...) (Potential).
FT   DISULFID    189    203       By similarity.
FT   VAR_SEQ     376    383       Missing (in isoform 2S).
FT                                /FTId=VSP_000091.
FT   VARIANT      49     49       A -> T (in strain: DBA/2J).
SQ   SEQUENCE   474 AA;  55099 MW;  45BD61649C296EA9 CRC64;
     MSSPNTWSIG SSVYSPVFSQ KMTLWILLLL SLYPGFTSQK SDDDYEDYAS NKTWVLTPKV
     PEGDVTVILN NLLEGYDNKL RPDIGVKPTL IHTDMYVNSI GPVNAINMEY TIDIFFAQTW
     YDRRLKFNST IKVLRLNSNM VGKIWIPDTF FRNSKKADAH WITTPNRMLR IWNDGRVLYT
     LRLTIDAECQ LQLHNFPMDE HSCPLEFSSY GYPREEIVYQ WKRSSVEVGD TRSWRLYQFS
     FVGLRNTTEV VKTTSGDYVV MSVYFDLSRR MGYFTIQTYI PCTLIVVLSW VSFWINKDAV
     PARTSLGITT VLTMTTLSTI ARKSLPKVSY VTAMDLFVSV CFIFVFSALV EYGTLHYFVS
     NRKPSKDKDK KKKNPLLRMF SFKAPTIDIR PRSATIQMNN ATHLQERDEE YGYECLDGKD
     CASFFCCFED CRTGAWRHGR IHIRIAKMDS YARIFFPTAF CLFNLVYWVS YLYL
//
ID   AP1G1_MOUSE             Reviewed;         822 AA.
AC   P22892;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 103.
DE   RecName: Full=AP-1 complex subunit gamma-1;
DE   AltName: Full=Adapter-related protein complex 1 subunit gamma-1;
DE   AltName: Full=Adaptor protein complex AP-1 subunit gamma-1;
DE   AltName: Full=Clathrin assembly protein complex 1 gamma-1 large chain;
DE   AltName: Full=Gamma-adaptin;
DE   AltName: Full=Gamma1-adaptin;
DE   AltName: Full=Golgi adaptor HA1/AP1 adaptin subunit gamma-1;
GN   Name=Ap1g1; Synonyms=Adtg, Clapg1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-25.
RC   TISSUE=Brain;
RX   MEDLINE=91115927; PubMed=2126014; DOI=10.1083/jcb.111.6.2319;
RA   Robinson M.S.;
RT   "Cloning and expression of gamma-adaptin, a component of clathrin-
RT   coated vesicles associated with the Golgi apparatus.";
RL   J. Cell Biol. 111:2319-2326(1990).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 704-822, MUTAGENESIS OF
RP   ALA-753; LEU-762 AND PRO-765, AND INTERACTION WITH EPS15 AND SYNRG.
RX   PubMed=12176391; DOI=10.1016/S0969-2126(02)00801-8;
RA   Kent H.M., McMahon H.T., Evans P.R., Benmerah A., Owen D.J.;
RT   "Gamma-adaptin appendage domain: structure and binding site for Eps15
RT   and gamma-synergin.";
RL   Structure 10:1139-1148(2002).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 1-613, AND SUBUNIT.
RX   PubMed=15377783; DOI=10.1073/pnas.0406102101;
RA   Heldwein E.E., Macia E., Wang J., Yin H.L., Kirchhausen T.,
RA   Harrison S.C.;
RT   "Crystal structure of the clathrin adaptor protein 1 core.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14108-14113(2004).
CC   -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1
CC       that plays a role in protein sorting in the late-Golgi/trans-Golgi
CC       network (TGN) and/or endosomes. The AP complexes mediate both the
CC       recruitment of clathrin to membranes and the recognition of
CC       sorting signals within the cytosolic tails of transmembrane cargo
CC       molecules.
CC   -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is an heterotetramer
CC       composed of two large adaptins (gamma-type subunit AP1G1 and beta-
CC       type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or
CC       AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or
CC       AP1S3) (By similarity). Binds RABEP1 (By similarity). Binds EPS15
CC       and SYNRG. Interacts (via GAE domain) with AP1AR (via coiled-coil
CC       domain) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle,
CC       clathrin-coated vesicle membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Note=Component of the coat surrounding the
CC       cytoplasmic face of coated vesicles located at the Golgi complex.
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC   -!- SIMILARITY: Contains 1 GAE domain.
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DR   EMBL; X54424; CAA38296.1; -; mRNA.
DR   IPI; IPI00621460; -.
DR   PIR; A36680; A36680.
DR   UniGene; Mm.37210; -.
DR   UniGene; Mm.430782; -.
DR   UniGene; Mm.471663; -.
DR   PDB; 1GYU; X-ray; 1.81 A; A=704-822.
DR   PDB; 1GYV; X-ray; 1.71 A; A=704-822.
DR   PDB; 1GYW; X-ray; 2.40 A; A/B=695-822.
DR   PDB; 1W63; X-ray; 4.00 A; A/C/E/G/I/K=1-613.
DR   PDB; 2A7B; X-ray; 1.65 A; A=704-821.
DR   PDBsum; 1GYU; -.
DR   PDBsum; 1GYV; -.
DR   PDBsum; 1GYW; -.
DR   PDBsum; 1W63; -.
DR   PDBsum; 2A7B; -.
DR   ProteinModelPortal; P22892; -.
DR   SMR; P22892; 1-589, 704-822.
DR   MINT; MINT-200421; -.
DR   STRING; P22892; -.
DR   PhosphoSite; P22892; -.
DR   PRIDE; P22892; -.
DR   Ensembl; ENSMUST00000034171; ENSMUSP00000034171; ENSMUSG00000031731.
DR   MGI; MGI:101919; Ap1g1.
DR   eggNOG; roNOG11683; -.
DR   HOVERGEN; HBG067473; -.
DR   OrthoDB; EOG4ZGPBP; -.
DR   PhylomeDB; P22892; -.
DR   ArrayExpress; P22892; -.
DR   Bgee; P22892; -.
DR   CleanEx; MM_AP1G1; -.
DR   Genevestigator; P22892; -.
DR   GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR   GO; GO:0030665; C:clathrin coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR   InterPro; IPR017107; AP1_complex_gsu.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   InterPro; IPR013041; Clathrin/coatomer_app_Ig-like.
DR   InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR   InterPro; IPR008153; Clathrin_g-adaptin_app.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Gene3D; G3DSA:2.60.40.1230; Clathrin_g-adaptin_app; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   Pfam; PF02883; Alpha_adaptinC2; 1.
DR   PIRSF; PIRSF037094; AP1_complex_gamma; 1.
DR   SMART; SM00809; Alpha_adaptinC2; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF49348; Clath_adapt; 1.
DR   PROSITE; PS50180; GAE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasmic vesicle;
KW   Direct protein sequencing; Endocytosis; Golgi apparatus; Membrane;
KW   Protein transport; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    822       AP-1 complex subunit gamma-1.
FT                                /FTId=PRO_0000193759.
FT   DOMAIN      702    817       GAE.
FT   MOD_RES     144    144       N6-acetyllysine (By similarity).
FT   MUTAGEN     753    753       A->D: Strongly reduces interaction with
FT                                EPS15 and SYNRG.
FT   MUTAGEN     762    762       L->E: Strongly reduces interaction with
FT                                EPS15 and SYNRG.
FT   MUTAGEN     765    765       P->N: Reduces interaction with EPS15 and
FT                                SYNRG.
FT   HELIX         7     14
FT   HELIX        20     38
FT   TURN         39     41
FT   TURN         43     45
FT   HELIX        46     58
FT   HELIX        64     66
FT   HELIX        67     75
FT   STRAND       76     78
FT   HELIX        79     92
FT   HELIX        97    111
FT   STRAND      114    116
FT   HELIX       117    129
FT   HELIX       132    147
FT   HELIX       151    167
FT   HELIX       169    178
FT   TURN        179    181
FT   HELIX       188    201
FT   HELIX       205    213
FT   HELIX       216    228
FT   TURN        233    235
FT   STRAND      237    241
FT   HELIX       243    256
FT   TURN        257    259
FT   HELIX       261    265
FT   HELIX       268    276
FT   HELIX       284    298
FT   HELIX       303    317
FT   TURN        322    324
FT   HELIX       325    343
FT   HELIX       344    346
FT   HELIX       347    352
FT   HELIX       353    355
FT   HELIX       359    372
FT   STRAND      375    377
FT   HELIX       379    391
FT   HELIX       394    409
FT   HELIX       415    428
FT   HELIX       430    432
FT   HELIX       437    447
FT   HELIX       452    465
FT   HELIX       471    487
FT   STRAND      493    495
FT   HELIX       502    514
FT   HELIX       520    534
FT   HELIX       541    551
FT   HELIX       557    571
FT   TURN        572    575
FT   HELIX       576    581
FT   STRAND      707    712
FT   STRAND      715    723
FT   STRAND      730    739
FT   STRAND      741    743
FT   STRAND      745    753
FT   STRAND      759    762
FT   HELIX       772    774
FT   STRAND      778    785
FT   STRAND      794    802
FT   STRAND      805    813
FT   HELIX       818    820
SQ   SEQUENCE   822 AA;  91350 MW;  15317E4BCD9503EB CRC64;
     MPAPIRLREL IRTIRTARTQ AEEREMIQKE CAAIRSSFRE EDNTYRCRNV AKLLYMHMLG
     YPAHFGQLEC LKLIASQKFT DKRIGYLGAM LLLDERQDVH LLMTNCIKND LNHSTQFVQG
     LALCTLGCMG SSEMCRDLAG EVEKLLKTSN SYLRKKAALC AVHVIRKVPE LMEMFLPATK
     NLLNEKNHGV LHTSVVLLTE MCERSPDMLA HFRKLVPQLV RILKNLIMSG YSPEHDVSGI
     SDPFLQVRIL RLLRILGRND DDSSEAMNDI LAQVATNTET SKNVGNAILY ETVLTIMDIK
     SESGLRVLAI NILGRFLLNN DKNIRYVALT SLLKTVQTDH NAVQRHRSTI VDCLKDLDVS
     IKRRAMELSF ALVNGNNIRG MMKELLYFLD SCEPEFKADC ASGIFLAAEK YAPSKRWHID
     TIMRVLTTAG SYVRDDAVPN LIQLITNSVE MHAYTVQRLY KAILGDYSQQ PLVQVAAWCI
     GEYGDLLVSG QCEEEEPIQV TEDEVLDILE SVLISNMSTS VTRGYALTAI MKLSTRFTCT
     VNRIKKVVSI YGSSIDVELQ QRAVEYNALF KKYDHMRSAL LERMPVMEKV TTNGPSEIVQ
     TNGETEPAPL ETKPPPSGPQ PTSQANDLLD LLGGNDITPV IPTAPTSKPA SAGGELLDLL
     GDITLTGAPA AAPTPASVPQ ISQPPFLLDG LSSQPLFNDI APGIPSITAY SKNGLKIEFT
     FERSNTNPSV TVITIQASNS TELDMTDFVF QAAVPKTFQL QLLSPSSSVV PAFNTGTITQ
     VIKVLNPQKQ QLRMRIKLTY NHKGSAMQDL AEVNNFPPQS WQ
//
ID   GBRD_MOUSE              Reviewed;         449 AA.
AC   P22933;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   08-MAR-2011, entry version 102.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit delta;
DE   AltName: Full=GABA(A) receptor subunit delta;
DE   Flags: Precursor;
GN   Name=Gabrd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=91103876; PubMed=2176788; DOI=10.1089/dna.1990.9.561;
RA   Sommer B., Poustka A., Spurr N.K., Seeburg P.H.;
RT   "The murine GABAA receptor delta-subunit gene: structure and
RT   assignment to human chromosome 1.";
RL   DNA Cell Biol. 9:561-568(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=DBA/2J; TISSUE=Brain;
RX   MEDLINE=92370453; PubMed=1324097; DOI=10.1016/0361-9230(92)90015-P;
RA   Wang J.B., Kofuji P., Burt D.R.;
RT   "Strain comparisons and developmental profile of the delta subunit of
RT   the murine GABAA receptor.";
RL   Brain Res. Bull. 29:119-123(1992).
CC   -!- FUNCTION: GABA, the major inhibitory neurotransmitter in the
CC       vertebrate brain, mediates neuronal inhibition by binding to the
CC       GABA/benzodiazepine receptor and opening an integral chloride
CC       channel.
CC   -!- SUBUNIT: Generally pentameric. There are five types of GABA(A)
CC       receptor chains: alpha, beta, gamma, delta, and rho.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane; Multi-pass membrane protein. Cell membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
CC       family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily.
CC       GABRD sub-subfamily.
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DR   EMBL; M60596; AAA37652.1; -; Genomic_DNA.
DR   EMBL; M60587; AAA37652.1; JOINED; Genomic_DNA.
DR   EMBL; M60588; AAA37652.1; JOINED; Genomic_DNA.
DR   EMBL; M60589; AAA37652.1; JOINED; Genomic_DNA.
DR   EMBL; M60591; AAA37652.1; JOINED; Genomic_DNA.
DR   EMBL; M60592; AAA37652.1; JOINED; Genomic_DNA.
DR   EMBL; M60593; AAA37652.1; JOINED; Genomic_DNA.
DR   EMBL; M60594; AAA37652.1; JOINED; Genomic_DNA.
DR   EMBL; M60595; AAA37652.1; JOINED; Genomic_DNA.
DR   EMBL; S42882; AAB22967.1; -; mRNA.
DR   IPI; IPI00323796; -.
DR   PIR; A36303; A36303.
DR   PIR; I52630; I52630.
DR   RefSeq; NP_032098.2; NM_008072.2.
DR   UniGene; Mm.388925; -.
DR   ProteinModelPortal; P22933; -.
DR   SMR; P22933; 63-336.
DR   STRING; P22933; -.
DR   PRIDE; P22933; -.
DR   Ensembl; ENSMUST00000030925; ENSMUSP00000030925; ENSMUSG00000029054.
DR   GeneID; 14403; -.
DR   KEGG; mmu:14403; -.
DR   CTD; 14403; -.
DR   MGI; MGI:95622; Gabrd.
DR   eggNOG; roNOG12460; -.
DR   HOGENOM; HBG506497; -.
DR   HOVERGEN; HBG051707; -.
DR   InParanoid; P22933; -.
DR   OMA; EQECMLD; -.
DR   OrthoDB; EOG4H9XKN; -.
DR   PhylomeDB; P22933; -.
DR   NextBio; 285959; -.
DR   ArrayExpress; P22933; -.
DR   Bgee; P22933; -.
DR   Genevestigator; P22933; -.
DR   GermOnline; ENSMUSG00000029054; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IEA:InterPro.
DR   InterPro; IPR006028; GABAA_rcpt.
DR   InterPro; IPR008098; GABAAd_rcpt.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   Gene3D; G3DSA:2.70.170.10; Neur_chan_lig_bd; 1.
DR   PANTHER; PTHR18945; Neur_channel; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR01722; GABAARDELTA.
DR   PRINTS; PR00253; GABAARECEPTR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF90112; Neu_channel_TM; 1.
DR   SUPFAM; SSF63712; Neur_chan_LBD; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Chloride; Chloride channel;
KW   Disulfide bond; Glycoprotein; Ion transport; Ionic channel; Membrane;
KW   Postsynaptic cell membrane; Signal; Synapse; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     16
FT   CHAIN        17    449       Gamma-aminobutyric acid receptor subunit
FT                                delta.
FT                                /FTId=PRO_0000000469.
FT   TOPO_DOM     17    248       Extracellular (Probable).
FT   TRANSMEM    249    271       Helical; (Probable).
FT   TRANSMEM    275    297       Helical; (Probable).
FT   TRANSMEM    309    331       Helical; (Probable).
FT   TOPO_DOM    332    426       Cytoplasmic (Probable).
FT   TRANSMEM    427    449       Helical; (Probable).
FT   CARBOHYD    103    103       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    106    106       N-linked (GlcNAc...) (Potential).
FT   DISULFID    164    178       By similarity.
FT   CONFLICT    255    255       Y -> H (in Ref. 2; AAB22967).
SQ   SEQUENCE   449 AA;  50522 MW;  C00BCA1C3322BF19 CRC64;
     MDVLGWLLLP LLLLCTQPHH GARAMNDIGD YVGSNLEISW LPNLDGLMEG YARNFRPGIG
     GAPVNVALAL EVASIDHISE ANMEYTMTVF LHQSWRDSRL SYNHTNETLG LDSRFVDKLW
     LPDTFIVNAK SAWFHDVTVE NKLIRLQPDG VILYSIRITS TVACDMDLAK YPLDEQECML
     DLESYGYSSE DIVYYWSENQ EQIHGLDRLQ LAQFTITSYR FTTELMNFKS AGQFPRLSLH
     FQLRRNRGVY IIQSYMPSVL LVAMSWVSFW ISQAAVPARV SLGITTVLTM TTLMVSARSS
     LPRASAIKAL DVYFWICYVF VFAALVEYAF AHFNADYRKK RKAKVKVTKP RAEMDVRNAI
     VLFSLSAAGV SQELAISRRQ GRVPGNLMGS YRSVEVEAKK EGGSRPGGPG GIRSRLKPID
     ADTIDIYARA VFPAAFAAVN IIYWAAYTM
//
ID   CXA1_MOUSE              Reviewed;         382 AA.
AC   P23242;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 121.
DE   RecName: Full=Gap junction alpha-1 protein;
DE   AltName: Full=Connexin-43;
DE            Short=Cx43;
DE   AltName: Full=Gap junction 43 kDa heart protein;
GN   Name=Gja1; Synonyms=Cxn-43;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=91217014; PubMed=1708769;
RA   Beyer E.C., Steinberg T.H.;
RT   "Evidence that the gap junction protein connexin-43 is the ATP-induced
RT   pore of mouse macrophages.";
RL   J. Biol. Chem. 266:7971-7974(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CD-1; TISSUE=Ovary;
RX   MEDLINE=91285228; PubMed=2060697; DOI=10.1016/0012-1606(91)90452-9;
RA   Nishi M., Kumar N.M., Gilula N.B.;
RT   "Developmental regulation of gap junction gene expression during mouse
RT   embryonic development.";
RL   Dev. Biol. 146:117-130(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=92299686; PubMed=1318884; DOI=10.1083/jcb.117.6.1299;
RA   Hennemann J., Suchyna T., Lichtenberg-Frate H., Jungbluth S., Dahl E.,
RA   Schwarz J., Nicholson B.J., Willecke K.;
RT   "Molecular cloning and functional expression of mouse connexin40, a
RT   second gap junction gene preferentially expressed in lung.";
RL   J. Cell Biol. 117:1299-1310(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   MEDLINE=93366174; PubMed=8395450; DOI=10.1016/0378-1119(93)90419-4;
RA   Sullivan R., Ruangvoravat C., Joo D., Morgan J., Wang B.L., Wang X.K.,
RA   Lo C.W.;
RT   "Structure, sequence and expression of the mouse Cx43 gene encoding
RT   connexin 43.";
RL   Gene 130:191-199(1993).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=91132668; PubMed=2178193; DOI=10.1016/0022-2828(90)90061-6;
RA   Fromaget C., el Aoumari A., Dupont E., Briand J.-P., Gros D.;
RT   "Changes in the expression of connexin 43, a cardiac gap junctional
RT   protein, during mouse heart development.";
RL   J. Mol. Cell. Cardiol. 22:1245-1258(1990).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=21617229; PubMed=11741837; DOI=10.1093/hmg/10.25.2945;
RA   Liu X.Z., Xia X.J., Adams J., Chen Z.Y., Welch K.O., Tekin M.,
RA   Ouyang X.M., Kristiansen A., Pandya A., Balkany T., Arnos K.S.,
RA   Nance W.E.;
RT   "Mutations in GJA1 (connexin 43) are associated with non-syndromic
RT   autosomal recessive deafness.";
RL   Hum. Mol. Genet. 10:2945-2951(2001).
RN   [8]
RP   INTERACTION WITH SGSM3.
RX   PubMed=15709751; DOI=10.1021/bi048306w;
RA   Lan Z., Kurata W.E., Martyn K.D., Jin C., Lau A.F.;
RT   "Novel rab GAP-like protein, CIP85, interacts with connexin43 and
RT   induces its degradation.";
RL   Biochemistry 44:2385-2396(2005).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-247 AND TYR-313, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-314; THR-326;
RP   SER-328 AND SER-330, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [11]
RP   INTERACTION WITH CNST.
RX   PubMed=19864490; DOI=10.1093/hmg/ddp490;
RA   del Castillo F.J., Cohen-Salmon M., Charollais A., Caille D.,
RA   Lampe P.D., Chavrier P., Meda P., Petit C.;
RT   "Consortin, a trans-Golgi network cargo receptor for the plasma
RT   membrane targeting and recycling of connexins.";
RL   Hum. Mol. Genet. 19:262-275(2010).
CC   -!- FUNCTION: One gap junction consists of a cluster of closely packed
CC       pairs of transmembrane channels, the connexons, through which
CC       materials of low MW diffuse from one cell to a neighboring cell.
CC   -!- FUNCTION: Connexin 43 is possibly the ATP-induced pore of mouse
CC       macrophages.
CC   -!- SUBUNIT: A connexon is composed of a hexamer of connexins.
CC       Interacts with SGSM3. Interacts with KIAA1432/CIP150 (By
CC       similarity). Interacts with CNST.
CC   -!- INTERACTION:
CC       Q6PJW8:CNST (xeno); NbExp=1; IntAct=EBI-298630, EBI-750390;
CC       Q8CBC4-3:Cnst; NbExp=1; IntAct=EBI-298630, EBI-2615407;
CC       P28231:Gjb3; NbExp=1; IntAct=EBI-298630, EBI-1767245;
CC       P28229:Gjc1; NbExp=1; IntAct=EBI-298630, EBI-1767271;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Cell junction, gap junction.
CC   -!- TISSUE SPECIFICITY: Expressed in heart, non-sensory epithelial
CC       cells, and in fibrocytes of the spiral ligament and the spiral
CC       limbus.
CC   -!- DEVELOPMENTAL STAGE: At E7.5, expressed in the embryo, but not in
CC       the extraembryonic region containing the ectoplacental cone.
CC   -!- SIMILARITY: Belongs to the connexin family. Alpha-type (group II)
CC       subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; M61896; AAA37444.1; -; Genomic_DNA.
DR   EMBL; M63801; AAA53027.1; -; mRNA.
DR   EMBL; X62836; CAA44640.1; -; Genomic_DNA.
DR   EMBL; X61576; CAA43778.1; -; mRNA.
DR   EMBL; BC006894; AAH06894.1; -; mRNA.
DR   IPI; IPI00380273; -.
DR   PIR; A39802; A39802.
DR   RefSeq; NP_034418.1; NM_010288.3.
DR   UniGene; Mm.378921; -.
DR   UniGene; Mm.419098; -.
DR   ProteinModelPortal; P23242; -.
DR   SMR; P23242; 3-234, 252-382.
DR   DIP; DIP-29207N; -.
DR   IntAct; P23242; 9.
DR   MINT; MINT-1326689; -.
DR   STRING; P23242; -.
DR   PhosphoSite; P23242; -.
DR   PRIDE; P23242; -.
DR   Ensembl; ENSMUST00000068581; ENSMUSP00000064536; ENSMUSG00000050953.
DR   GeneID; 14609; -.
DR   KEGG; mmu:14609; -.
DR   UCSC; uc007fcc.1; mouse.
DR   CTD; 14609; -.
DR   MGI; MGI:95713; Gja1.
DR   eggNOG; maNOG05724; -.
DR   HOVERGEN; HBG009576; -.
DR   InParanoid; P23242; -.
DR   OMA; TDGANVD; -.
DR   OrthoDB; EOG402WSC; -.
DR   NextBio; 286404; -.
DR   ArrayExpress; P23242; -.
DR   Bgee; P23242; -.
DR   CleanEx; MM_GJA1; -.
DR   Genevestigator; P23242; -.
DR   GermOnline; ENSMUSG00000050953; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005243; F:gap junction channel activity; IDA:MGI.
DR   GO; GO:0005102; F:receptor binding; IPI:MGI.
DR   GO; GO:0007512; P:adult heart development; IMP:MGI.
DR   GO; GO:0006915; P:apoptosis; IMP:MGI.
DR   GO; GO:0048514; P:blood vessel morphogenesis; IMP:MGI.
DR   GO; GO:0007267; P:cell-cell signaling; IDA:MGI.
DR   GO; GO:0002070; P:epithelial cell maturation; IMP:MGI.
DR   GO; GO:0001947; P:heart looping; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0060174; P:limb bud formation; IMP:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR   GO; GO:0045844; P:positive regulation of striated muscle tissue development; IMP:MGI.
DR   GO; GO:0008016; P:regulation of heart contraction; IMP:MGI.
DR   GO; GO:0043403; P:skeletal muscle tissue regeneration; IDA:MGI.
DR   InterPro; IPR000500; Connexin.
DR   InterPro; IPR002261; Connexin43.
DR   InterPro; IPR013124; Connexin43_C.
DR   InterPro; IPR019570; Connexin_CCC.
DR   InterPro; IPR017990; Connexin_CS.
DR   InterPro; IPR013092; Connexin_N.
DR   PANTHER; PTHR11984; Connexin; 1.
DR   Pfam; PF00029; Connexin; 1.
DR   Pfam; PF03508; Connexin43; 1.
DR   Pfam; PF10582; Connexin_CCC; 1.
DR   PRINTS; PR00206; CONNEXIN.
DR   PRINTS; PR01132; CONNEXINA1.
DR   SMART; SM00037; CNX; 1.
DR   PROSITE; PS00407; CONNEXINS_1; 1.
DR   PROSITE; PS00408; CONNEXINS_2; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Disulfide bond; Gap junction; Membrane;
KW   Phosphoprotein; Transmembrane; Transmembrane helix.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    382       Gap junction alpha-1 protein.
FT                                /FTId=PRO_0000057802.
FT   TOPO_DOM      2     13       Cytoplasmic (Potential).
FT   TRANSMEM     14     36       Helical; (Potential).
FT   TOPO_DOM     37     76       Extracellular (Potential).
FT   TRANSMEM     77     99       Helical; (Potential).
FT   TOPO_DOM    100    154       Cytoplasmic (Potential).
FT   TRANSMEM    155    177       Helical; (Potential).
FT   TOPO_DOM    178    208       Extracellular (Potential).
FT   TRANSMEM    209    231       Helical; (Potential).
FT   TOPO_DOM    232    382       Cytoplasmic (Potential).
FT   MOD_RES     247    247       Phosphotyrosine.
FT   MOD_RES     306    306       Phosphoserine.
FT   MOD_RES     313    313       Phosphotyrosine.
FT   MOD_RES     314    314       Phosphoserine.
FT   MOD_RES     326    326       Phosphothreonine.
FT   MOD_RES     328    328       Phosphoserine.
FT   MOD_RES     330    330       Phosphoserine.
FT   MOD_RES     365    365       Phosphoserine (By similarity).
FT   MOD_RES     368    368       Phosphoserine (By similarity).
FT   MOD_RES     369    369       Phosphoserine (By similarity).
FT   MOD_RES     373    373       Phosphoserine (By similarity).
FT   DISULFID     54    192       By similarity.
FT   DISULFID    187    198       By similarity.
FT   CONFLICT    320    320       M -> T (in Ref. 3; AAA53027).
SQ   SEQUENCE   382 AA;  43004 MW;  018DCB461FA69490 CRC64;
     MGDWSALGKL LDKVQAYSTA GGKVWLSVLF IFRILLLGTA VESAWGDEQS AFRCNTQQPG
     CENVCYDKSF PISHVRFWVL QIIFVSVPTL LYLAHVFYVM RKEEKLNKKE EELKVAQTDG
     VNVEMHLKQI EIKKFKYGIE EHGKVKMRGG LLRTYIISIL FKSVFEVAFL LIQWYIYGFS
     LSAVYTCKRD PCPHQVDCFL SRPTEKTIFI IFMLVVSLVS LALNIIELFY VFFKGVKDRV
     KGRSDPYHAT TGPLSPSKDC GSPKYAYFNG CSSPTAPLSP MSPPGYKLVT GDRNNSSCRN
     YNKQASEQNW ANYSAEQNRM GQAGSTISNS HAQPFDFPDD SQNAKKVAAG HELQPLAIVD
     QRPSSRASSR ASSRPRPDDL EI
//
ID   KPCL_MOUSE              Reviewed;         683 AA.
AC   P23298;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   08-MAR-2011, entry version 108.
DE   RecName: Full=Protein kinase C eta type;
DE            EC=2.7.11.13;
DE   AltName: Full=PKC-L;
DE   AltName: Full=nPKC-eta;
GN   Name=Prkch; Synonyms=Pkch;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Epidermis;
RX   MEDLINE=91093089; PubMed=2266135;
RA   Osada S., Mizuno K., Saido T.C., Akita Y., Suzuki K., Kuroki T.,
RA   Ohno S.;
RT   "A phorbol ester receptor/protein kinase, nPKC eta, a new member of
RT   the protein kinase C family predominantly expressed in lung and
RT   skin.";
RL   J. Biol. Chem. 265:22434-22440(1990).
CC   -!- FUNCTION: This is calcium-independent, phospholipid-dependent,
CC       serine- and threonine-specific enzyme.
CC   -!- FUNCTION: PKC is activated by diacylglycerol which in turn
CC       phosphorylates a range of cellular proteins. PKC also serves as
CC       the receptor for phorbol esters, a class of tumor promoters.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Three specific sites; Thr-513 (activation loop
CC       of the kinase domain), Thr-656 (turn motif) and Ser-675
CC       (hydrophobic region), need to be phosphorylated for its full
CC       activation.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in lunk and skin.
CC   -!- DOMAIN: The C1 domain, containing the phorbol ester/DAG-type
CC       region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor and the
CC       C2 domain is a non-calcium binding domain.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. PKC subfamily.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 2 phorbol-ester/DAG-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; D90242; BAA14288.1; -; mRNA.
DR   IPI; IPI00130491; -.
DR   PIR; A23690; A23690.
DR   UniGene; Mm.341677; -.
DR   ProteinModelPortal; P23298; -.
DR   SMR; P23298; 3-137, 167-298, 352-681.
DR   STRING; P23298; -.
DR   PhosphoSite; P23298; -.
DR   PRIDE; P23298; -.
DR   Ensembl; ENSMUST00000021527; ENSMUSP00000021527; ENSMUSG00000021108.
DR   MGI; MGI:97600; Prkch.
DR   eggNOG; roNOG06998; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108317; -.
DR   InParanoid; P23298; -.
DR   OrthoDB; EOG4P2Q1P; -.
DR   PhylomeDB; P23298; -.
DR   BRENDA; 2.7.11.13; 244.
DR   ArrayExpress; P23298; -.
DR   Bgee; P23298; -.
DR   CleanEx; MM_PRKCH; -.
DR   Genevestigator; P23298; -.
DR   GermOnline; ENSMUSG00000021108; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004697; F:protein kinase C activity; IEA:EC.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR014376; Prot_kin_PKC_delta.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   PIRSF; PIRSF000551; PKC_delta; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Repeat; Serine/threonine-protein kinase; Transferase;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    683       Protein kinase C eta type.
FT                                /FTId=PRO_0000055706.
FT   DOMAIN       12    102       C2.
FT   DOMAIN      355    614       Protein kinase.
FT   DOMAIN      615    683       AGC-kinase C-terminal.
FT   ZN_FING     171    222       Phorbol-ester/DAG-type 1.
FT   ZN_FING     245    295       Phorbol-ester/DAG-type 2.
FT   NP_BIND     361    369       ATP (By similarity).
FT   ACT_SITE    479    479       Proton acceptor (By similarity).
FT   BINDING     384    384       ATP (By similarity).
FT   MOD_RES      57     57       Phosphothreonine (By similarity).
FT   MOD_RES     317    317       Phosphoserine (By similarity).
FT   MOD_RES     320    320       Phosphoserine (By similarity).
FT   MOD_RES     513    513       Phosphothreonine (Potential).
FT   MOD_RES     656    656       Phosphothreonine (Probable).
FT   MOD_RES     675    675       Phosphoserine (Probable).
SQ   SEQUENCE   683 AA;  77974 MW;  C7DB338A9F95F576 CRC64;
     MSSGTMKFNG YLRVRIGEAV GLQPTRWSLR HSLFKKGHQL LDPYLTVSVD QVRVGQTSTK
     QKTNKPTYNE EFCANVTDGG HLELAVFHET PLGYDHFVAN CTLQFQELLR TAGTSDTFEG
     WVDLEPEGKV FVVITLTGSF TEATLQRDRI FKHFTRKRQR AMRRRVHQVN GHKFMATYLR
     QPTYCSHCRE FIWGVFGKQG YQCQVCTCVV HKRCHHLIVT ACTCQNNINK VDAKIAEQRF
     GINIPHKFNV HNYKVPTFCD HCGSLLWGIM RQGLQCKICK MNVHIRCQAN VAPNCGVNAV
     ELAKTLAGMG LQPGNISPTS KLISRSTLRR QGKEGSKEGN GIGVNSSSRF GIDNFEFIRV
     LGKGSFGKVM LARIKETGEL YAVKVLKKDV ILQDDDVECT MTEKRILSLA RNHPFLTQLF
     CCFQTPDRLF FVMEFVNGGD LMFHIQKSRR FDEARARFYA AEIISALMFL HEKGIIYRDL
     KLDNVLLDHE GHCKLADFGM CKEGICNGVT TATFCGTPDY IAPEILQEML YGPAVDWWAM
     GVLLYEMLCG HAPFEAENED DLFEAILNDE VVYPTWLHED ARGILKSFMT KNPTMRLGSL
     TQGGEHEILR HPFFKEIDWA QLNHRQLEPP FRPRIKSRED VSNFDPDFIK EEPVLTPIDE
     GHLPMINQDE FRNFSYVSPE LQL
//
ID   GRIA1_MOUSE             Reviewed;         907 AA.
AC   P23818;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   08-MAR-2011, entry version 107.
DE   RecName: Full=Glutamate receptor 1;
DE            Short=GluR-1;
DE   AltName: Full=AMPA-selective glutamate receptor 1;
DE   AltName: Full=GluR-A;
DE   AltName: Full=GluR-K1;
DE   AltName: Full=Glutamate receptor ionotropic, AMPA 1;
DE            Short=GluA1;
DE   Flags: Precursor;
GN   Name=Gria1; Synonyms=Glur1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=91032147; PubMed=1699805; DOI=10.1016/0014-5793(90)80452-O;
RA   Sakimura K., Bujo H., Kushiya E., Araki K., Yamazaki M., Yamazaki M.,
RA   Meguro H., Warashina A., Numa S., Mishina M.;
RT   "Functional expression from cloned cDNAs of glutamate receptor species
RT   responsive to kainate and quisqualate.";
RL   FEBS Lett. 272:73-80(1990).
RN   [2]
RP   INTERACTION WITH HIP1.
RX   PubMed=12839988; DOI=10.1093/emboj/cdg334;
RA   Metzler M., Li B., Gan L., Georgiou J., Gutekunst C.A., Wang Y.,
RA   Torre E., Devon R.S., Oh R., Legendre-Guillemin V., Rich M.,
RA   Alvarez C., Gertsenstein M., McPherson P.S., Nagy A., Wang Y.T.,
RA   Roder J.C., Raymond L.A., Hayden M.R.;
RT   "Disruption of the endocytic protein HIP1 results in neurological
RT   deficits and decreased AMPA receptor trafficking.";
RL   EMBO J. 22:3254-3266(2003).
RN   [3]
RP   PALMITOYLATION AT CYS-603 AND CYS-829.
RX   PubMed=16129400; DOI=10.1016/j.neuron.2005.06.035;
RA   Hayashi T., Rumbaugh G., Huganir R.L.;
RT   "Differential regulation of AMPA receptor subunit trafficking by
RT   palmitoylation of two distinct sites.";
RL   Neuron 47:709-723(2005).
RN   [4]
RP   INTERACTION WITH RASGRF2.
RX   PubMed=16407208; DOI=10.1074/jbc.M512060200;
RA   Tian X., Feig L.A.;
RT   "Age-dependent participation of Ras-GRF proteins in coupling calcium-
RT   permeable AMPA glutamate receptors to Ras/Erk signaling in cortical
RT   neurons.";
RL   J. Biol. Chem. 281:7578-7582(2006).
RN   [5]
RP   INTERACTION WITH TMEM90B AND GRIA2.
RX   PubMed=20152115; DOI=10.1016/j.neuron.2009.12.021;
RA   Kalashnikova E., Lorca R.A., Kaur I., Barisone G.A., Li B.,
RA   Ishimaru T., Trimmer J.S., Mohapatra D.P., Diaz E.;
RT   "SynDIG1: an activity-regulated, AMPA- receptor-interacting
RT   transmembrane protein that regulates excitatory synapse development.";
RL   Neuron 65:80-93(2010).
CC   -!- FUNCTION: Ionotropic glutamate receptor. L-glutamate acts as an
CC       excitatory neurotransmitter at many synapses in the central
CC       nervous system. Binding of the excitatory neurotransmitter L-
CC       glutamate induces a conformation change, leading to the opening of
CC       the cation channel, and thereby converts the chemical signal to an
CC       electrical impulse. The receptor then desensitizes rapidly and
CC       enters a transient inactive state, characterized by the presence
CC       of bound agonist.
CC   -!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate
CC       receptor subunits. Tetramers may be formed by the dimerization of
CC       dimers. Interacts with DLG1 via its C-terminus. Interacts with
CC       CACNG2 (By similarity). Interacts with HIP1 and RASGRF2. Interacts
CC       with TMEM90B and GRIA2. Interacts with LRFN1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Endoplasmic reticulum membrane; Multi-pass membrane protein (By
CC       similarity). Cell junction, synapse, postsynaptic cell membrane;
CC       Multi-pass membrane protein. Note=Interaction with CACNG2 promotes
CC       cell surface expression (By similarity).
CC   -!- PTM: Palmitoylated. Depalmitoylated upon glutamate stimulation.
CC       ZDHHC3/GODZ specifically palmitoylates Cys-603, which leads to
CC       Golgi retention and decreased cell surface expression. In
CC       contrast, Cys-829 palmitoylation does not affect cell surface
CC       expression but regulates stimulation-dependent endocytosis.
CC   -!- MISCELLANEOUS: The postsynaptic actions of Glu are mediated by a
CC       variety of receptors that are named according to their selective
CC       agonists. This receptor binds AMPA (quisqualate) > glutamate >
CC       kainate.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel
CC       (TC 1.A.10.1) family. GRIA1 subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; X57497; CAA40734.1; -; mRNA.
DR   IPI; IPI00136965; -.
DR   PIR; S12874; S12874.
DR   RefSeq; NP_001106796.1; NM_001113325.1.
DR   UniGene; Mm.4920; -.
DR   ProteinModelPortal; P23818; -.
DR   SMR; P23818; 23-831.
DR   MINT; MINT-1897734; -.
DR   STRING; P23818; -.
DR   PhosphoSite; P23818; -.
DR   PRIDE; P23818; -.
DR   Ensembl; ENSMUST00000036315; ENSMUSP00000044494; ENSMUSG00000020524.
DR   GeneID; 14799; -.
DR   KEGG; mmu:14799; -.
DR   UCSC; uc007izs.1; mouse.
DR   CTD; 14799; -.
DR   MGI; MGI:95808; Gria1.
DR   eggNOG; maNOG06626; -.
DR   HOGENOM; HBG381523; -.
DR   HOVERGEN; HBG051839; -.
DR   InParanoid; P23818; -.
DR   NextBio; 286953; -.
DR   ArrayExpress; P23818; -.
DR   Bgee; P23818; -.
DR   CleanEx; MM_GRIA1; -.
DR   Genevestigator; P23818; -.
DR   GermOnline; ENSMUSG00000020524; Mus musculus.
DR   GO; GO:0032281; C:alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex; IDA:MGI.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0004970; F:ionotropic glutamate receptor activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0007616; P:long-term memory; IMP:UniProtKB.
DR   GO; GO:0031623; P:receptor internalization; IMP:UniProtKB.
DR   GO; GO:0007268; P:synaptic transmission; IGI:MGI.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR019594; Glu_rcpt_Glu/Gly-bd.
DR   InterPro; IPR001320; Iontro_glu_rcpt.
DR   InterPro; IPR001508; NMDA_rcpt.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR   PRINTS; PR00177; NMDARECEPTOR.
DR   SMART; SM00918; Lig_chan-Glu_bd; 1.
DR   SMART; SM00079; PBPe; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Endoplasmic reticulum; Glycoprotein;
KW   Ion transport; Ionic channel; Ligand-gated ion channel; Lipoprotein;
KW   Membrane; Palmitate; Phosphoprotein; Postsynaptic cell membrane;
KW   Receptor; Signal; Synapse; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL        1     18       Potential.
FT   CHAIN        19    907       Glutamate receptor 1.
FT                                /FTId=PRO_0000011530.
FT   TOPO_DOM     19    536       Extracellular (Potential).
FT   TRANSMEM    537    557       Helical; (Potential).
FT   TOPO_DOM    558    617       Cytoplasmic (Potential).
FT   TRANSMEM    618    638       Helical; (Potential).
FT   TOPO_DOM    639    805       Extracellular (Potential).
FT   TRANSMEM    806    826       Helical; (Potential).
FT   TOPO_DOM    827    907       Cytoplasmic (Potential).
FT   REGION      492    494       Glutamate binding (By similarity).
FT   REGION      668    669       Glutamate binding (By similarity).
FT   BINDING     499    499       Glutamate (By similarity).
FT   BINDING     719    719       Glutamate (By similarity).
FT   MOD_RES     645    645       Phosphoserine (By similarity).
FT   MOD_RES     710    710       Phosphoserine (By similarity).
FT   MOD_RES     849    849       Phosphoserine (By similarity).
FT   MOD_RES     863    863       Phosphoserine (By similarity).
FT   LIPID       603    603       S-palmitoyl cysteine.
FT   LIPID       829    829       S-palmitoyl cysteine.
FT   CARBOHYD     63     63       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    249    249       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    257    257       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    363    363       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    401    401       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    406    406       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   907 AA;  101569 MW;  F0FF7031DADD7CEB CRC64;
     MPYIFAFFCT GFLGAVVGAN FPNNIQIGGL FPNQQSQEHA AFRFALSQLT EPPKLLPQID
     IVNISDSFEM TYRFCSQFSK GVYAIFGFYE RRTVNMLTSF CGALHVCFIT PSFPVDTSNQ
     FVLQLRPELQ EALISIIDHY KWQTFVYIYD ADRGLSVLQR VLDTAAEKNW QVTAVNILTT
     TEEGYRMLFQ DLEKKKERLV VVDCESERLN AILGQIVKLE KNGIGYHYIL ANLGFMDIDL
     NKFKESGANV TGFQLVNYTD TIPARIMQQW RTSDARDHTR VDWKRPKYTS ALTYDGVKVM
     AEAFQSLRRQ RIDISRRGNA GDCLANPAVP WGQGIDIQRA LQQVRFEGLT GNVQFNEKGR
     RTNYTLHVIE MKHDGIRKIG YWNEDDKFVP AATDAQAGGD NSSVQNRTYI VTTILEDPYV
     MLKKNANQFE GNDRYEGYCV ELAAEIAKHV GYSYRLEIVS DGKYGARDPD TKAWNGMVGE
     LVYGRADVAV APLTITLVRE EVIDFSKPFM SLGISIMIKK PQKSKPGVFS FLDPLAYEIW
     MCIVFAYIGV SVVLFLVSRF SPYEWHSEEF EEGRDQTTSD QSNEFGIFNS LWFSLGAFMQ
     QGCDISPRSL SGRIVGGVWW FFTLIIISSY TANLAAFLTV ERMVSPIESA EDLAKQTEIA
     YGTLEAGSTK EFFRRSKIAV FEKMWTYMKS AEPSVFVRTT EEGMIRVRKS KGKYAYLLES
     TMNEYIEQRK PCDTMKVGGN LDSKGYGIAT PKGSALRGPV NLAVLKLSEQ GVLDKLKSKW
     WYDKGECGSK DSGSKDKTSA LSLSNVAGVF YILIGGLGLA MLVALIEFCY KSRSESKRMK
     GFCLIPQQSI NEAIRTSTLP RNSGAGASGG SGSGENGRVV SQDFPKSMQS IPCMSHSSGM
     PLGATGL
//
ID   TISD_MOUSE              Reviewed;         367 AA.
AC   P23949;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Zinc finger protein 36, C3H1 type-like 2;
DE   AltName: Full=Butyrate response factor 2;
DE   AltName: Full=Protein TIS11D;
GN   Name=Zfp36l2; Synonyms=Brf2, Tis11d;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=91141531; PubMed=1996120;
RA   Varnum B.C., Ma Q., Chi T., Fletcher B.S., Herschman H.R.;
RT   "The TIS11 primary response gene is a member of a gene family that
RT   encodes proteins with a highly conserved sequence containing an
RT   unusual Cys-His repeat.";
RL   Mol. Cell. Biol. 11:1754-1758(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50.
RA   Fletcher B.S.;
RT   "Structure and expression of two mitogen inducible genes.";
RL   Thesis (1992), University of California Los Angeles, United States.
CC   -!- FUNCTION: Probable regulatory protein involved in regulating the
CC       response to growth factors. RNA-binding protein that binds to
CC       5'UUAUUUAUUU-3' core sequence. Binds to the class II AU-rich
CC       element (ARE) in the 3'-UTR of target mRNAs and promotes their
CC       deadenylation and degradation (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- SIMILARITY: Contains 2 C3H1-type zinc fingers.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M58564; AAA72946.1; -; mRNA.
DR   EMBL; M97165; AAA39709.1; -; Genomic_DNA.
DR   IPI; IPI00138319; -.
DR   PIR; C39590; C39590.
DR   UniGene; Mm.259321; -.
DR   ProteinModelPortal; P23949; -.
DR   SMR; P23949; 124-193.
DR   STRING; P23949; -.
DR   PhosphoSite; P23949; -.
DR   PRIDE; P23949; -.
DR   Ensembl; ENSMUST00000060366; ENSMUSP00000050820; ENSMUSG00000045817.
DR   MGI; MGI:107945; Zfp36l2.
DR   eggNOG; maNOG19008; -.
DR   HOVERGEN; HBG008483; -.
DR   InParanoid; P23949; -.
DR   OrthoDB; EOG480HXD; -.
DR   ArrayExpress; P23949; -.
DR   Bgee; P23949; -.
DR   CleanEx; MM_ZFP36L2; -.
DR   Genevestigator; P23949; -.
DR   GermOnline; ENSMUSG00000045817; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:MGI.
DR   GO; GO:0043488; P:regulation of mRNA stability; IDA:MGI.
DR   GO; GO:0033077; P:T cell differentiation in thymus; IGI:BHF-UCL.
DR   InterPro; IPR007635; Tis11B_N.
DR   InterPro; IPR000571; Znf_CCCH.
DR   Pfam; PF04553; Tis11B_N; 1.
DR   Pfam; PF00642; zf-CCCH; 2.
DR   SMART; SM00356; ZnF_C3H1; 2.
DR   PROSITE; PS50103; ZF_C3H1; 2.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Repeat; RNA-binding; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    367       Zinc finger protein 36, C3H1 type-like 2.
FT                                /FTId=PRO_0000089171.
FT   ZN_FING     126    154       C3H1-type 1.
FT   ZN_FING     164    192       C3H1-type 2.
FT   REGION      143    184       RNA-binding (By similarity).
FT   MOTIF       126    131       RNA-binding (By similarity).
FT   COMPBIAS     64     67       Poly-Gly.
FT   COMPBIAS    111    114       Poly-Gln.
FT   COMPBIAS    200    203       Poly-Gly.
FT   COMPBIAS    263    266       Poly-Pro.
FT   COMPBIAS    297    303       Poly-Ala.
SQ   SEQUENCE   367 AA;  37593 MW;  361244AF6244E46E CRC64;
     MLDKKAVGTP VAAAPSSSFT PGFLRRHSAS NLHALAHPVP SPGSCSPKFP GAPNGGGSSC
     GPAGGGGLAS YGQLKEPSGG SGTALVTKES KFRDRSFSEN GERSQHLLHL QQQQKGGSGS
     QINSTRYKTE LCRPFEESGT CKYGEKCQFA HGFHELRSLT RHPKYKTELC RTFHTIGFCP
     YGPRCHFIHN ADERRPAPSG GGGASGDLRA FGARDALHLG FAREPRPKLH HSLSFSGFPS
     GHHQPPGGLE SPLLLDSPTS RTPPPPSSSA SSCSSSASSC SSASAASTPS GAPTCCATAA
     AAALLYGPGG AEDLLSPGAP CASCSSSGAN NAFAFGPELS SLITPLAIQT HNFAAAPPPT
     TATSSRA
//
ID   BCAT1_MOUSE             Reviewed;         386 AA.
AC   P24288; Q7TMT2;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   11-JAN-2011, entry version 103.
DE   RecName: Full=Branched-chain-amino-acid aminotransferase, cytosolic;
DE            Short=BCAT(c);
DE            EC=2.6.1.42;
DE   AltName: Full=Protein ECA39;
GN   Name=Bcat1; Synonyms=Eca39;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96293490; PubMed=8692959; DOI=10.1073/pnas.93.14.7143;
RA   Schuldiner O., Eden A., Ben-Yosef T., Yanuka O., Simchen G.,
RA   Benvenisty N.;
RT   "ECA39, a conserved gene regulated by c-Myc in mice, is involved in
RT   G1/S cell cycle regulation in yeast.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:7143-7148(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129;
RX   MEDLINE=91067482; PubMed=2251142; DOI=10.1093/nar/18.22.6709;
RA   Niwa O., Kumazaki T., Tsukiyama T., Soma G., Miyajima N., Yokoro K.;
RT   "A cDNA clone overexpressed and amplified in a mouse teratocarcinoma
RT   line.";
RL   Nucleic Acids Res. 18:6709-6709(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C3H/He; TISSUE=Mesenchymal stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Catalyzes the first reaction in the catabolism of the
CC       essential branched chain amino acids leucine, isoleucine, and
CC       valine.
CC   -!- CATALYTIC ACTIVITY: L-leucine + 2-oxoglutarate = 4-methyl-2-
CC       oxopentanoate + L-glutamate.
CC   -!- CATALYTIC ACTIVITY: 2-oxoglutaric acid + L-isoleucine = (S)-3-
CC       methyl-2-oxopentanoic acid + L-glutamic acid.
CC   -!- CATALYTIC ACTIVITY: 2-oxoglutaric acid + L-valine = 3-methyl-2-
CC       oxobutanoic acid + L-glutamic acid.
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Expressed in brain and kidney. Overexpressed
CC       in C-myc induced brain tumors, lymphomas, as well as in a
CC       teratocarcinoma cell line.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed at day 9 of embryogenesis.
CC       Expression decreases to moderate levels through day 13. In the
CC       developing embryo, expressed in the brain, somites and mesenophric
CC       tubules.
CC   -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent
CC       aminotransferase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA35543.1; Type=Frameshift; Positions=277, 360;
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DR   EMBL; U42443; AAB05673.1; -; mRNA.
DR   EMBL; X17502; CAA35543.1; ALT_FRAME; mRNA.
DR   EMBL; BC053706; AAH53706.1; -; mRNA.
DR   IPI; IPI00875896; -.
DR   PIR; S13108; S13108.
DR   RefSeq; NP_031558.3; NM_007532.5.
DR   UniGene; Mm.4606; -.
DR   ProteinModelPortal; P24288; -.
DR   SMR; P24288; 24-385.
DR   STRING; P24288; -.
DR   PRIDE; P24288; -.
DR   Ensembl; ENSMUST00000111742; ENSMUSP00000107371; ENSMUSG00000030268.
DR   GeneID; 12035; -.
DR   KEGG; mmu:12035; -.
DR   CTD; 12035; -.
DR   MGI; MGI:104861; Bcat1.
DR   eggNOG; roNOG07606; -.
DR   HOVERGEN; HBG050678; -.
DR   NextBio; 280283; -.
DR   ArrayExpress; P24288; -.
DR   Bgee; P24288; -.
DR   CleanEx; MM_BCAT1; -.
DR   Genevestigator; P24288; -.
DR   GermOnline; ENSMUSG00000030268; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IDA:MGI.
DR   GO; GO:0009082; P:branched chain family amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009083; P:branched chain family amino acid catabolic process; IDA:MGI.
DR   InterPro; IPR001544; Aminotrans_IV.
DR   InterPro; IPR018300; Aminotrans_IV_CS.
DR   InterPro; IPR005786; B_amino_transII.
DR   PANTHER; PTHR11825; Aminotrans_IV; 1.
DR   PANTHER; PTHR11825:SF2; B_amino_transII; 1.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   PIRSF; PIRSF006468; BCAT1; 1.
DR   SUPFAM; SSF56752; Aminotrans_IV; 1.
DR   TIGRFAMs; TIGR01123; ilvE_II; 1.
DR   PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Amino-acid biosynthesis; Aminotransferase;
KW   Branched-chain amino acid biosynthesis; Cytoplasm;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN         1    386       Branched-chain-amino-acid
FT                                aminotransferase, cytosolic.
FT                                /FTId=PRO_0000103293.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     222    222       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
FT   CONFLICT    238    238       V -> A (in Ref. 3; AAH53706).
FT   CONFLICT    265    265       L -> P (in Ref. 3; AAH53706).
SQ   SEQUENCE   386 AA;  42791 MW;  8185C4C227843B5E CRC64;
     MKDCSNGCSA PFAGERGSEE VAETFRAKDL IITPATVLKE KPDPDSLVFG ATFTDHMLTV
     EWSSASGWEK PHIKPFGNLP IHPAASVLHY AVELFEGLKA FRGVDNKIRL FRPDLNMDRM
     CRSAVRTTLP MFDKEELLKC ILQLLQIDQE WVPYSTSASL YIRPTFIGTE PSLGVKKPSK
     ALLFVILSPV GPYFSSGSFT PVSLWANPKY IRAWKGGTGD CKMGGNYGAS LLAQCEAVEN
     GCQQVLWLYG KDNQITEVGT MNLFLYWINE DGEEELATPP LDGIILPGVT RQSILELAQQ
     WGEFKVCERH LTMDDLATAL EGNRVKEMFG SGTACVVCPV SDILYKGQML HIPTMENGPK
     LASRILGKLT DIQYGRVESD WTIELP
//
ID   TY3H_MOUSE              Reviewed;         498 AA.
AC   P24529;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-FEB-2011, entry version 95.
DE   RecName: Full=Tyrosine 3-monooxygenase;
DE            EC=1.14.16.2;
DE   AltName: Full=Tyrosine 3-hydroxylase;
DE            Short=TH;
GN   Name=Th;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=91248263; PubMed=1674869; DOI=10.1016/0006-291X(91)90472-J;
RA   Ichikawa S., Sasaoka T., Nagatsu T.;
RT   "Primary structure of mouse tyrosine hydroxylase deduced from its
RT   cDNA.";
RL   Biochem. Biophys. Res. Commun. 176:1610-1616(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-30.
RC   STRAIN=BALB/c;
RA   Morgan W.W., Bermudez J., Sharp Z.D.;
RL   Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 78-90.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
CC   -!- FUNCTION: Plays an important role in the physiology of adrenergic
CC       neurons.
CC   -!- CATALYTIC ACTIVITY: L-tyrosine + tetrahydrobiopterin + O(2) = 3,4-
CC       dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin.
CC   -!- COFACTOR: Fe(2+) ion.
CC   -!- ENZYME REGULATION: Phosphorylation leads to an increase in the
CC       catalytic activity.
CC   -!- PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis;
CC       dopamine from L-tyrosine: step 1/2.
CC   -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
CC       hydroxylase family.
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DR   EMBL; M69200; AAA40434.1; -; mRNA.
DR   EMBL; X53503; CAA37580.1; -; Genomic_DNA.
DR   IPI; IPI00138131; -.
DR   PIR; JN0068; JN0068.
DR   RefSeq; NP_033403.1; NM_009377.1.
DR   UniGene; Mm.1292; -.
DR   ProteinModelPortal; P24529; -.
DR   SMR; P24529; 75-498.
DR   STRING; P24529; -.
DR   PhosphoSite; P24529; -.
DR   PRIDE; P24529; -.
DR   Ensembl; ENSMUST00000000219; ENSMUSP00000000219; ENSMUSG00000000214.
DR   GeneID; 21823; -.
DR   KEGG; mmu:21823; -.
DR   UCSC; uc009koi.1; mouse.
DR   CTD; 21823; -.
DR   MGI; MGI:98735; Th.
DR   eggNOG; roNOG12445; -.
DR   HOGENOM; HBG484724; -.
DR   HOVERGEN; HBG006841; -.
DR   InParanoid; P24529; -.
DR   OMA; SELDKCH; -.
DR   PhylomeDB; P24529; -.
DR   BRENDA; 1.14.16.2; 244.
DR   NextBio; 301244; -.
DR   ArrayExpress; P24529; -.
DR   Bgee; P24529; -.
DR   CleanEx; MM_TH; -.
DR   Genevestigator; P24529; -.
DR   GermOnline; ENSMUSG00000000214; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0043204; C:perikaryon; IDA:MGI.
DR   GO; GO:0004511; F:tyrosine 3-monooxygenase activity; TAS:MGI.
DR   GO; GO:0006585; P:dopamine biosynthetic process from tyrosine; IDA:MGI.
DR   GO; GO:0042755; P:eating behavior; IMP:MGI.
DR   GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0042462; P:eye photoreceptor cell development; IMP:BHF-UCL.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0007612; P:learning; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0007617; P:mating behavior; IMP:MGI.
DR   GO; GO:0007613; P:memory; IMP:MGI.
DR   GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0008016; P:regulation of heart contraction; IMP:MGI.
DR   GO; GO:0001963; P:synaptic transmission, dopaminergic; IMP:MGI.
DR   GO; GO:0007601; P:visual perception; IMP:BHF-UCL.
DR   InterPro; IPR001273; ArAA_hydroxylase.
DR   InterPro; IPR018301; ArAA_hydroxylase_Fe/CU_BS.
DR   InterPro; IPR019774; Aromatic-AA_hydroxylase_C.
DR   InterPro; IPR005962; Tyr_3_mOase.
DR   InterPro; IPR019773; Tyrosine_3-monooxygenase-like.
DR   InterPro; IPR021164; Tyrosine_hydroxylase_CS.
DR   Gene3D; G3DSA:1.10.800.10; Aaa_hydroxylase; 1.
DR   PANTHER; PTHR11473; Aaa_hydroxylase; 1.
DR   Pfam; PF00351; Biopterin_H; 1.
DR   Pfam; PF12549; TOH_N; 2.
DR   PIRSF; PIRSF000336; TH; 1.
DR   PRINTS; PR00372; FYWHYDRXLASE.
DR   SUPFAM; SSF56534; Aaa_hydroxylase; 1.
DR   TIGRFAMs; TIGR01269; Tyr_3_monoox; 1.
DR   PROSITE; PS00367; BH4_AAA_HYDROXYL_1; 1.
DR   PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1.
PE   1: Evidence at protein level;
KW   Catecholamine biosynthesis; Direct protein sequencing; Iron;
KW   Metal-binding; Monooxygenase; Neurotransmitter biosynthesis;
KW   Oxidoreductase; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    498       Tyrosine 3-monooxygenase.
FT                                /FTId=PRO_0000205562.
FT   COMPBIAS     51     59       Poly-Ala.
FT   METAL       331    331       Iron (By similarity).
FT   METAL       336    336       Iron (By similarity).
FT   METAL       376    376       Iron (By similarity).
FT   MOD_RES      19     19       Phosphoserine; by CaMK2 (By similarity).
FT   MOD_RES      31     31       Phosphoserine (By similarity).
FT   MOD_RES      40     40       Phosphoserine; by PKA (By similarity).
SQ   SEQUENCE   498 AA;  55993 MW;  62790179664F6DC6 CRC64;
     MPTPSASSPQ PKGFRRAVSE QDTKQAEAVT SPRFIGRRQS LIEDARKERE AAAAAAAAAV
     ASAEPGNPLE AVVFEERDGN AVLNLLFSLR GTKPSSLSRA LKVFETFEAK IHHLETRPAQ
     RPLAGSPHLE YFVRFEVPSG DLAALLSSVR RVSDDVRSAR EDKVPWFPRK VSELDKCHHL
     VTKFDPDLDL DHPGFSDQAY RQRRKLIAEI AFQYKQGEPI PHVEYTKEEI ATWKEVYATL
     KGLYATHACR EHLEAFQLLE RYCGYREDSI PQLEDVSHFL KERTGFQLRP VAGLLSARDF
     LASLAFRVFQ CTQYIRHASS PMHSPEPDCC HELLGHVPML ADRTFAQFSQ DIGLASLGAS
     DEEIEKLSTV YWFTVEFGLC KQNGELKAYG AGLLSSYGEL LHSLSEEPEV RAFDPDTAAV
     QPYQDQTYQP VYFVSESFSD AKDKLRNYAS RIQRPFSVKF DPYTLAIDVL DSPHTIRRSL
     EGVQDELHTL TQALSAIS
//
ID   IMDH2_MOUSE             Reviewed;         514 AA.
AC   P24547; Q61734; Q91Z11;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2003, sequence version 2.
DT   08-MAR-2011, entry version 118.
DE   RecName: Full=Inosine-5'-monophosphate dehydrogenase 2;
DE            Short=IMP dehydrogenase 2;
DE            Short=IMPD 2;
DE            Short=IMPDH 2;
DE            EC=1.1.1.205;
DE   AltName: Full=IMPDH-II;
GN   Name=Impdh2; Synonyms=Impdh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=91153661; PubMed=1671845; DOI=10.1016/0378-1119(91)90065-J;
RA   Tiedeman A.A., Smith J.M.;
RT   "Isolation and sequence of a cDNA encoding mouse IMP dehydrogenase.";
RL   Gene 97:289-293(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS MYCOPHENOLIC ACID RESISTANT.
RC   TISSUE=Brain;
RX   MEDLINE=94153991; PubMed=7906545; DOI=10.1016/0167-4781(94)90029-9;
RA   Lightfoot T., Snyder F.F.;
RT   "Gene amplification and dual point mutations of mouse IMP
RT   dehydrogenase associated with cellular resistance to mycophenolic
RT   acid.";
RL   Biochim. Biophys. Acta 1217:156-162(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C3H/He, and Czech II; TISSUE=Mammary gland, and Osteoblast;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 125-133; 182-194; 289-290; 439-449; 456-466 AND
RP   475-478.
RX   PubMed=2572589;
RA   Hodges S.D., Fung E., McKay D.J., Renaux B.S., Snyder F.F.;
RT   "Increased activity, amount, and altered kinetic properties of IMP
RT   dehydrogenase from mycophenolic acid-resistant neuroblastoma cells.";
RL   J. Biol. Chem. 264:18137-18141(1989).
RN   [5]
RP   PROTEIN SEQUENCE OF 137-149.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
CC   -!- FUNCTION: Rate limiting enzyme in the de novo synthesis of guanine
CC       nucleotides and therefore is involved in the regulation of cell
CC       growth. It may also have a role in the development of malignancy
CC       and the growth progression of some tumors.
CC   -!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NAD(+) + H(2)O =
CC       xanthosine 5'-phosphate + NADH.
CC   -!- COFACTOR: Potassium (By similarity).
CC   -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway;
CC       XMP from IMP: step 1/1.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the IMPDH/GMPR family.
CC   -!- SIMILARITY: Contains 2 CBS domains.
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DR   EMBL; M33934; AAA39311.1; -; mRNA.
DR   EMBL; M98333; AAA20181.1; -; mRNA.
DR   EMBL; BC010314; AAH10314.1; -; mRNA.
DR   EMBL; BC052671; AAH52671.1; -; mRNA.
DR   IPI; IPI00323971; -.
DR   PIR; JT0565; JT0565.
DR   RefSeq; NP_035960.2; NM_011830.3.
DR   UniGene; Mm.6065; -.
DR   ProteinModelPortal; P24547; -.
DR   SMR; P24547; 10-514.
DR   STRING; P24547; -.
DR   PhosphoSite; P24547; -.
DR   PMMA-2DPAGE; P24547; -.
DR   REPRODUCTION-2DPAGE; P24547; -.
DR   PRIDE; P24547; -.
DR   Ensembl; ENSMUST00000081111; ENSMUSP00000079888; ENSMUSG00000062867.
DR   GeneID; 23918; -.
DR   KEGG; mmu:23918; -.
DR   UCSC; uc009rqg.1; mouse.
DR   CTD; 23918; -.
DR   MGI; MGI:109367; Impdh2.
DR   eggNOG; roNOG06960; -.
DR   HOGENOM; HBG298985; -.
DR   HOVERGEN; HBG052122; -.
DR   InParanoid; P24547; -.
DR   OMA; AIGTHND; -.
DR   OrthoDB; EOG40VVP8; -.
DR   PhylomeDB; P24547; -.
DR   BRENDA; 1.1.1.205; 244.
DR   NextBio; 303689; -.
DR   Bgee; P24547; -.
DR   CleanEx; MM_IMPDH2; -.
DR   Genevestigator; P24547; -.
DR   GermOnline; ENSMUSG00000071041; Mus musculus.
DR   GO; GO:0003938; F:IMP dehydrogenase activity; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0046651; P:lymphocyte proliferation; IMP:MGI.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000644; Cysta_beta_synth_core.
DR   InterPro; IPR005990; IMP_DH.
DR   InterPro; IPR018529; IMP_DH-rel.
DR   InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS.
DR   InterPro; IPR001093; IMP_DH_GMPRt.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF00478; IMPDH; 1.
DR   PIRSF; PIRSF000130; IMPDH; 1.
DR   SMART; SM00116; CBS; 2.
DR   TIGRFAMs; TIGR01302; IMP_dehydrog; 1.
DR   PROSITE; PS51371; CBS; 2.
DR   PROSITE; PS00487; IMP_DH_GMP_RED; 1.
PE   1: Evidence at protein level;
KW   Acetylation; CBS domain; Direct protein sequencing; GMP biosynthesis;
KW   Metal-binding; NAD; Oxidoreductase; Phosphoprotein; Potassium;
KW   Purine biosynthesis; Repeat.
FT   CHAIN         1    514       Inosine-5'-monophosphate dehydrogenase 2.
FT                                /FTId=PRO_0000093674.
FT   DOMAIN      114    173       CBS 1.
FT   DOMAIN      179    237       CBS 2.
FT   NP_BIND     253    276       NAD (By similarity).
FT   REGION      329    331       IMP binding (By similarity).
FT   REGION      364    366       IMP binding (By similarity).
FT   REGION      387    388       IMP binding (By similarity).
FT   REGION      411    415       IMP binding (By similarity).
FT   REGION      441    442       IMP binding (By similarity).
FT   ACT_SITE    331    331       Thioimidate intermediate (By similarity).
FT   METAL       326    326       Potassium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       328    328       Potassium; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING      68     68       IMP (By similarity).
FT   BINDING     276    276       Inhibitor (By similarity).
FT   BINDING     322    322       IMP (By similarity).
FT   BINDING     333    333       Inhibitor (By similarity).
FT   MOD_RES     122    122       Phosphoserine (By similarity).
FT   MOD_RES     400    400       Phosphotyrosine (By similarity).
FT   MOD_RES     416    416       Phosphoserine (By similarity).
FT   MOD_RES     511    511       N6-acetyllysine (By similarity).
FT   VARIANT     333    333       T -> I (in mycophenolic acid resistant
FT                                cells).
FT   VARIANT     351    351       S -> Y (in mycophenolic acid resistant
FT                                cells).
FT   CONFLICT    458    458       P -> L (in Ref. 4; AA sequence).
FT   CONFLICT    465    465       Q -> S (in Ref. 4; AA sequence).
FT   CONFLICT    483    483       M -> T (in Ref. 1; AAA39311).
SQ   SEQUENCE   514 AA;  55815 MW;  17D25A5C5EBCC439 CRC64;
     MADYLISGGT SYVPDDGLTA QQLFNCGDGL TYNDFLILPG YIDFTADQVD LTSALTKKIT
     LKTPLVSSPM DTVTEAGMAI AMALTGGIGF IHHNCTPEFQ ANEVRKVKKY EQGFITDPVV
     LSPKDRVRDV FEAKARHGFC GIPITDTGRM GSRLVGIISS RDIDFLKEEE HDRFLEEIMT
     KREDLVVAPA GVTLKEANEI LQRSKKGKLP IVNENDELVA IIARTDLKKN RDYPLASKDA
     KKQLLCGAAI GTHEDDKYRL DLLALAGVDV VVLDSSQGNS IFQINMIKYI KEKYPSLQVI
     GGNVVTAAQA KNLIDAGVDA LRVGMGSGSI CITQEVLACG RPQATAVYKV SEYARRFGVP
     VIADGGIQNV GHIAKALALG ASTVMMGSLL AATTEAPGEY FFSDGIRLKK YRGMGSLDAM
     DKHLSSQNRY FSEADKIKVA QGVSGAVQDK GSIHKFVPYL IAGIQHSCQD IGAKSLTQVR
     AMMYSGELKF EKRTSSAQVE GGVHSLHSYE KRLF
//
ID   MPRD_MOUSE              Reviewed;         278 AA.
AC   P24668;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Cation-dependent mannose-6-phosphate receptor;
DE            Short=CD Man-6-P receptor;
DE            Short=CD-MPR;
DE   AltName: Full=46 kDa mannose 6-phosphate receptor;
DE            Short=MPR 46;
DE   Flags: Precursor;
GN   Name=M6pr; Synonyms=46mpr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=92291105; PubMed=1376319;
RA   Ludwig T., Ruether U., Metzger R., Copeland N.G., Jenkins N.A.,
RA   Lobel P., Hoflack B.;
RT   "Gene and pseudogene of the mouse cation-dependent mannose 6-phosphate
RT   receptor. Genomic organization, expression, and chromosomal
RT   localization.";
RL   J. Biol. Chem. 267:12211-12219(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=91282985; PubMed=1647783;
RA   Koester A., Nagel G., von Figura K., Pohlmann R.;
RT   "Molecular cloning of the mouse 46-kDa mannose 6-phosphate receptor
RT   (MPR 46).";
RL   Biol. Chem. Hoppe-Seyler 372:297-300(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=91244839; PubMed=1645352;
RA   Ma Z., Grubb J.H., Sly W.S.;
RT   "Cloning, sequencing, and functional characterization of the murine
RT   46-kDa mannose 6-phosphate receptor.";
RL   J. Biol. Chem. 266:10589-10595(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 156-233.
RX   MEDLINE=91170218; PubMed=1848553;
RA   Szebenyi G., Rotwein P.;
RT   "Differential regulation of mannose 6-phosphate receptors and their
RT   ligands during the myogenic development of C2 cells.";
RL   J. Biol. Chem. 266:5534-5539(1991).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-84, AND MASS SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-84, AND MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Transport of phosphorylated lysosomal enzymes from the
CC       Golgi complex and the cell surface to lysosomes. Lysosomal enzymes
CC       bearing phosphomannosyl residues bind specifically to mannose-6-
CC       phosphate receptors in the Golgi apparatus and the resulting
CC       receptor-ligand complex is transported to an acidic prelyosomal
CC       compartment where the low pH mediates the dissociation of the
CC       complex.
CC   -!- SUBUNIT: Homodimer. Binds GGA1, GGA2 and GGA3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane; Single-pass type I
CC       membrane protein.
CC   -!- DOMAIN: The extracellular domain is homologous to the repeating
CC       units (of approximately 147 AA) of the cation-independent mannose
CC       6-phosphate receptor.
CC   -!- MISCELLANEOUS: This receptor has optimal binding in the presence
CC       of divalent cations.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X64068; CAA45423.1; -; mRNA.
DR   EMBL; X64070; CAA45426.1; -; mRNA.
DR   EMBL; X56831; CAA40162.1; -; mRNA.
DR   EMBL; M63286; AAA39735.1; -; mRNA.
DR   EMBL; BC027210; AAH27210.1; -; mRNA.
DR   EMBL; BC046956; AAH46956.1; -; mRNA.
DR   EMBL; BC080811; AAH80811.1; -; mRNA.
DR   EMBL; M58585; AAA39482.1; -; mRNA.
DR   IPI; IPI00108844; -.
DR   PIR; A40399; A40399.
DR   RefSeq; NP_034879.2; NM_010749.6.
DR   UniGene; Mm.249225; -.
DR   ProteinModelPortal; P24668; -.
DR   SMR; P24668; 29-181.
DR   STRING; P24668; -.
DR   PhosphoSite; P24668; -.
DR   PRIDE; P24668; -.
DR   Ensembl; ENSMUST00000007602; ENSMUSP00000007602; ENSMUSG00000007458.
DR   Ensembl; ENSMUST00000112610; ENSMUSP00000108229; ENSMUSG00000007458.
DR   GeneID; 17113; -.
DR   KEGG; mmu:17113; -.
DR   UCSC; uc009dow.1; mouse.
DR   CTD; 17113; -.
DR   MGI; MGI:96904; M6pr.
DR   HOGENOM; HBG268550; -.
DR   HOVERGEN; HBG006395; -.
DR   InParanoid; P24668; -.
DR   OMA; NETHVFN; -.
DR   OrthoDB; EOG43FGXF; -.
DR   PhylomeDB; P24668; -.
DR   NextBio; 291264; -.
DR   ArrayExpress; P24668; -.
DR   Bgee; P24668; -.
DR   CleanEx; MM_M6PR; -.
DR   Genevestigator; P24668; -.
DR   GermOnline; ENSMUSG00000007458; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005770; C:late endosome; IDA:MGI.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005537; F:mannose binding; IEA:InterPro.
DR   GO; GO:0015578; F:mannose transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR   InterPro; IPR009011; Man6P_isomerase_rcpt-bd.
DR   InterPro; IPR000296; Man_6_P_rcpt.
DR   PRINTS; PR00715; MAN6PRECEPTR.
DR   SUPFAM; SSF50911; Man6php_recept; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Lysosome; Membrane; Phosphoprotein; Receptor; Signal;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL        1     21
FT   CHAIN        22    278       Cation-dependent mannose-6-phosphate
FT                                receptor.
FT                                /FTId=PRO_0000019227.
FT   TOPO_DOM     22    186       Lumenal (Potential).
FT   TRANSMEM    187    211       Helical; (Potential).
FT   TOPO_DOM    212    278       Cytoplasmic (Potential).
FT   MOD_RES     268    268       Phosphoserine.
FT   CARBOHYD     58     58       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     84     84       N-linked (GlcNAc...).
FT   CARBOHYD     95     95       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    108    108       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    114    114       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    196    196       I -> T (in Ref. 5; AAA39482).
FT   CONFLICT    221    221       M -> T (in Ref. 5; AAA39482).
FT   CONFLICT    226    226       H -> P (in Ref. 5; AAA39482).
SQ   SEQUENCE   278 AA;  31172 MW;  8E0E8727CE793E7D CRC64;
     MFPFSGCWRT ELLLLLLLAV AVRESWQIEE KSCDLVGEKD KESKNEVALL ERLRPLFNKS
     FESTVGQGSD TYSYIFRVCR EASNHSSGAG LVQINKSNDK ETVVGRINET HIFNGSNWIM
     LIYKGGDEYD NHCGKEQRRA VVMISCNRHT LAANFNPVSE ERGKVQDCFY LFEMDSSLAC
     SPEVSHLSVG SILLVIFASL VAVYIIGGFL YQRLVVGAKG MEQFPHLAFW QDLGNLVADG
     CDFVCRSKPR NVPAAYRGVG DDQLGEESEE RDDHLLPM
//
ID   CDK11_MOUSE             Reviewed;         784 AA.
AC   P24788; Q3UI03; Q61399; Q7TST4; Q8BP53;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   08-MAR-2011, entry version 104.
DE   RecName: Full=Cyclin-dependent kinase 11;
DE            EC=2.7.11.22;
DE   AltName: Full=Cell division cycle 2-like protein kinase 1;
DE   AltName: Full=Cell division protein kinase 11;
DE   AltName: Full=Galactosyltransferase-associated protein kinase p58/GTA;
DE   AltName: Full=PITSLRE serine/threonine-protein kinase CDC2L1;
GN   Name=Cdk11; Synonyms=Cdc2l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   MEDLINE=91299577; PubMed=2069872;
RA   Kidd V.J., Luo W., Xiang J.L., Tu F., Easton J., McCune S.,
RA   Snead M.L.;
RT   "Regulated expression of a cell division control-related protein
RT   kinase during development.";
RL   Cell Growth Differ. 2:85-93(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=95105189; PubMed=7528743;
RA   Malek S.N., Desiderio S.;
RT   "A cyclin-dependent kinase homologue, p130PITSLRE is a
RT   phosphotyrosine-independent SH2 ligand.";
RL   J. Biol. Chem. 269:33009-33020(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-784 (ISOFORM 1).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-740 AND SER-741, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-264; SER-270;
RP   THR-740 AND SER-741, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Acts as a negative regulator of the normal cell cycle
CC       progression. In vitro, this protein kinase has been shown to
CC       phosphorylate a number of substrates, including histone h1,
CC       casein, and galactosyltransferase. May function in regulating
CC       proliferation by the phosphorylation and subsequent plasma
CC       membrane targeting of galactosyltransferase.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: Phosphorylation at Thr-437 or Tyr-438
CC       inactivates the enzyme, while phosphorylation at Thr-584 activates
CC       it (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=1; Synonyms=p130PITSLRE;
CC         IsoId=P24788-1; Sequence=Displayed;
CC       Name=2; Synonyms=p58clk-1;
CC         IsoId=P24788-2; Sequence=VSP_018835;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. CDC2/CDKX subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA03518.1; Type=Frameshift; Positions=Several;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M58633; AAA03518.1; ALT_FRAME; mRNA.
DR   EMBL; L37092; AAA66169.1; -; mRNA.
DR   EMBL; AK077668; BAC36942.1; -; mRNA.
DR   EMBL; AK147133; BAE27703.1; -; mRNA.
DR   EMBL; BC052920; AAH52920.1; -; mRNA.
DR   IPI; IPI00110050; -.
DR   IPI; IPI00649424; -.
DR   PIR; A55817; A55817.
DR   RefSeq; NP_031687.2; NM_007661.3.
DR   UniGene; Mm.267410; -.
DR   ProteinModelPortal; P24788; -.
DR   SMR; P24788; 424-714.
DR   STRING; P24788; -.
DR   PhosphoSite; P24788; -.
DR   PRIDE; P24788; -.
DR   Ensembl; ENSMUST00000067081; ENSMUSP00000070527; ENSMUSG00000029062.
DR   Ensembl; ENSMUST00000105599; ENSMUSP00000101224; ENSMUSG00000029062.
DR   Ensembl; ENSMUST00000105600; ENSMUSP00000101225; ENSMUSG00000029062.
DR   GeneID; 12537; -.
DR   KEGG; mmu:12537; -.
DR   UCSC; uc008wea.1; mouse.
DR   CTD; 12537; -.
DR   MGI; MGI:88353; Cdc2l1.
DR   HOGENOM; HBG402926; -.
DR   HOVERGEN; HBG014652; -.
DR   InParanoid; P24788; -.
DR   OMA; EGDFVPD; -.
DR   OrthoDB; EOG4HQDJ1; -.
DR   PhylomeDB; P24788; -.
DR   BRENDA; 2.7.11.22; 244.
DR   NextBio; 281574; -.
DR   ArrayExpress; P24788; -.
DR   Bgee; P24788; -.
DR   CleanEx; MM_CDC2L1; -.
DR   Genevestigator; P24788; -.
DR   GermOnline; ENSMUSG00000029062; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004693; F:cyclin-dependent protein kinase activity; IEA:EC.
DR   GO; GO:0006915; P:apoptosis; IMP:MGI.
DR   GO; GO:0001824; P:blastocyst development; IMP:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0007088; P:regulation of mitosis; IMP:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative initiation; ATP-binding; Cell cycle; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN         1    784       Cyclin-dependent kinase 11.
FT                                /FTId=PRO_0000024313.
FT   DOMAIN      427    712       Protein kinase.
FT   NP_BIND     433    441       ATP (By similarity).
FT   COMPBIAS    291    304       Poly-Glu.
FT   COMPBIAS    309    325       Poly-Glu.
FT   ACT_SITE    551    551       Proton acceptor (By similarity).
FT   BINDING     456    456       ATP (By similarity).
FT   MOD_RES      47     47       Phosphoserine.
FT   MOD_RES      65     65       Phosphoserine (By similarity).
FT   MOD_RES     234    234       Phosphoserine (By similarity).
FT   MOD_RES     264    264       Phosphoserine.
FT   MOD_RES     270    270       Phosphoserine.
FT   MOD_RES     370    370       Phosphoserine (By similarity).
FT   MOD_RES     373    373       Phosphoserine (By similarity).
FT   MOD_RES     384    384       Phosphothreonine (By similarity).
FT   MOD_RES     399    399       Phosphoserine (By similarity).
FT   MOD_RES     403    403       Phosphoserine (By similarity).
FT   MOD_RES     437    437       Phosphothreonine (By similarity).
FT   MOD_RES     438    438       Phosphotyrosine (By similarity).
FT   MOD_RES     578    578       Phosphoserine (By similarity).
FT   MOD_RES     583    583       Phosphotyrosine (By similarity).
FT   MOD_RES     584    584       Phosphothreonine (By similarity).
FT   MOD_RES     740    740       Phosphothreonine.
FT   MOD_RES     741    741       Phosphoserine.
FT   VAR_SEQ       1    345       Missing (in isoform 2).
FT                                /FTId=VSP_018835.
FT   CONFLICT     35     37       LKN -> MSQ (in Ref. 4; AAH52920).
FT   CONFLICT    284    284       Missing (in Ref. 2; AAA66169).
FT   CONFLICT    560    560       S -> T (in Ref. 1; AAA03518).
FT   CONFLICT    608    608       V -> C (in Ref. 1; AAA03518).
FT   CONFLICT    645    645       T -> S (in Ref. 1; AAA03518).
FT   CONFLICT    668    668       Y -> I (in Ref. 1; AAA03518).
SQ   SEQUENCE   784 AA;  91513 MW;  CDF03AC3957FA351 CRC64;
     MGDEKDSWKV KTLDEILQEK KRRKEQEEKA EIKRLKNSDD RDSKRDSLEE GELRDHRMEI
     TIRNSPYRRE DSMEDRGEED DSLAIKPPQQ MSRKEKAHHR KDEKRKEKRR HRSHSAEGGK
     HARVKEKERE HERRKRHREE QDKARREWER QKRREMAREH SRRERDRLEQ LERKRERERK
     LREQQKEQRE QKERERRAEE RRKEREARRE VSAHHRTMRE EYSDKGKVGH WSRSPLRPPR
     ERFEMGDNRK PVKEEKVEER DLLSDLQDIS DSERKTSSAE SSSAESGSGS EEEEEEEEEE
     EEEEGSTSEE SEEEEEEEEE EEEEETGSNS EEASEQSAEE VSDEEMSEDE DRENENHILV
     VPESRFDRDS GDSEEGEEEV GEGTPQSSAP TEGDYVPDSP ALSPIELKQE LPKYLPALQG
     CRSVEEFQCL NRIEEGTYGV VYRAKDKKTD EIVALKRLKM EKEKEGFPIT SLREINTILK
     AQHPNIVTVR EIVVGSNMDK IYIVMNYVEH DLKSLMETMK QPFLPGEVKT LMIQLLSGVK
     HLHDNWILHR DLKTSNLLLS HAGILKVGDF GLAREYGSPL KAYTPVVVTL WYRAPELLLG
     AKEYSTAVDM WSVGCIFGEL LTQKPLFPGK SDIDQINKIF KDLGTPSEKI WPGYNDLPAV
     KKMTFSEYPY NNLRKRFGAL LSDQGFDLMN KFLTYYPGRR INAEDGLKHE YFRETPLPID
     PSMFPTWPAK SEQQRVKRGT SPRPPEGGLG YSQLGDDDLK ETGFHLTTTN QGASAAGPGF
     SLKF
//
ID   TNR1B_MOUSE             Reviewed;         474 AA.
AC   P25119; O88734; P97893;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Tumor necrosis factor receptor superfamily member 1B;
DE   AltName: Full=Tumor necrosis factor receptor 2;
DE            Short=TNF-R2;
DE   AltName: Full=Tumor necrosis factor receptor type II;
DE            Short=TNF-RII;
DE            Short=TNFR-II;
DE   AltName: Full=p75;
DE   AltName: Full=p80 TNF-alpha receptor;
DE   AltName: CD_antigen=CD120b;
DE   Flags: Precursor;
GN   Name=Tnfrsf1b; Synonyms=Tnfr-2, Tnfr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=91187885; PubMed=1849278; DOI=10.1073/pnas.88.7.2830;
RA   Lewis M., Tartaglia L.A., Lee A., Bennett G.L., Rice G.C., Wong G.H.,
RA   Chen E.Y., Goeddel D.V.;
RT   "Cloning and expression of cDNAs for two distinct murine tumor
RT   necrosis factor receptors demonstrate one receptor is species
RT   specific.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:2830-2834(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=91246168; PubMed=1645445;
RA   Goodwin R.G., Anderson D., Jerzy R., Davis T., Brannan C.I.,
RA   Copeland N.G., Jenkins N.A., Smith C.A.;
RT   "Molecular cloning and expression of the type 1 and type 2 murine
RT   receptors for tumor necrosis factor.";
RL   Mol. Cell. Biol. 11:3020-3026(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=98414512; PubMed=9740674; DOI=10.1006/geno.1998.5407;
RA   Hurle B., Segade F., Rodriguez R., Ramos S.S., Lazo P.S.;
RT   "The mouse tumor necrosis factor receptor 2 gene: genomic structure
RT   and characterization of the two transcripts.";
RL   Genomics 52:79-89(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE OF 1-26.
RC   STRAIN=NOD;
RA   Jacob C.O., Liu J.;
RL   Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE OF 1-22.
RC   TISSUE=Liver;
RA   Kissonerghis M., Fellowes R., Feldmann M., Chernajovsky Y.;
RL   Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor with high affinity for TNFSF2/TNF-alpha and
CC       approximately 5-fold lower affinity for homotrimeric
CC       TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the
CC       apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2 (By
CC       similarity).
CC   -!- SUBUNIT: Binds to TRAF2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- SIMILARITY: Contains 4 TNFR-Cys repeats.
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DR   EMBL; M60469; AAA39752.1; -; mRNA.
DR   EMBL; M59378; AAA40463.1; -; mRNA.
DR   EMBL; Y14619; CAA74969.1; -; Genomic_DNA.
DR   EMBL; Y14620; CAA74969.1; JOINED; Genomic_DNA.
DR   EMBL; Y14621; CAA74969.1; JOINED; Genomic_DNA.
DR   EMBL; Y14622; CAA74969.1; JOINED; Genomic_DNA.
DR   EMBL; Y14679; CAA74969.1; JOINED; Genomic_DNA.
DR   EMBL; Y14623; CAA74969.1; JOINED; Genomic_DNA.
DR   EMBL; U39488; AAA85021.1; -; Genomic_DNA.
DR   EMBL; X87128; CAA60618.1; -; Genomic_DNA.
DR   IPI; IPI00137744; -.
DR   PIR; B38634; B38634.
DR   RefSeq; NP_035740.2; NM_011610.3.
DR   UniGene; Mm.235328; -.
DR   ProteinModelPortal; P25119; -.
DR   SMR; P25119; 44-206.
DR   IntAct; P25119; 2.
DR   STRING; P25119; -.
DR   PhosphoSite; P25119; -.
DR   PRIDE; P25119; -.
DR   Ensembl; ENSMUST00000030336; ENSMUSP00000030336; ENSMUSG00000028599.
DR   GeneID; 21938; -.
DR   KEGG; mmu:21938; -.
DR   UCSC; uc008vrt.1; mouse.
DR   CTD; 21938; -.
DR   MGI; MGI:1314883; Tnfrsf1b.
DR   eggNOG; roNOG14895; -.
DR   HOGENOM; HBG126373; -.
DR   HOVERGEN; HBG054237; -.
DR   InParanoid; P25119; -.
DR   OMA; KDEQVPF; -.
DR   OrthoDB; EOG48D0W0; -.
DR   PhylomeDB; P25119; -.
DR   NextBio; 301550; -.
DR   ArrayExpress; P25119; -.
DR   Bgee; P25119; -.
DR   Genevestigator; P25119; -.
DR   GermOnline; ENSMUSG00000028599; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
DR   GO; GO:0005031; F:tumor necrosis factor receptor activity; IPI:MGI.
DR   GO; GO:0008219; P:cell death; IMP:MGI.
DR   GO; GO:0008283; P:cell proliferation; TAS:MGI.
DR   GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
DR   GO; GO:0050779; P:RNA destabilization; IMP:MGI.
DR   InterPro; IPR020411; TNFR_1B.
DR   InterPro; IPR001368; TNFR_Cys_rich_reg.
DR   Pfam; PF00020; TNFR_c6; 2.
DR   PRINTS; PR01919; TNFACTORR1B.
DR   SMART; SM00208; TNFR; 4.
DR   PROSITE; PS00652; TNFR_NGFR_1; 2.
DR   PROSITE; PS50050; TNFR_NGFR_2; 3.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Membrane; Receptor; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     22
FT   CHAIN        23    474       Tumor necrosis factor receptor
FT                                superfamily member 1B.
FT                                /FTId=PRO_0000034550.
FT   TOPO_DOM     23    258       Extracellular (Potential).
FT   TRANSMEM    259    288       Helical; (Potential).
FT   TOPO_DOM    289    474       Cytoplasmic (Potential).
FT   REPEAT       39     77       TNFR-Cys 1.
FT   REPEAT       78    119       TNFR-Cys 2.
FT   REPEAT      120    164       TNFR-Cys 3.
FT   REPEAT      165    203       TNFR-Cys 4.
FT   CARBOHYD     69     69       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    195    195       N-linked (GlcNAc...) (Potential).
FT   DISULFID     40     54       By similarity.
FT   DISULFID     55     68       By similarity.
FT   DISULFID     58     76       By similarity.
FT   DISULFID     79     94       By similarity.
FT   DISULFID     97    111       By similarity.
FT   DISULFID    101    119       By similarity.
FT   DISULFID    121    127       By similarity.
FT   DISULFID    136    145       By similarity.
FT   DISULFID    139    163       By similarity.
FT   DISULFID    166    181       By similarity.
FT   CONFLICT     78     78       D -> DSDTVCAD (in Ref. 3).
FT   CONFLICT    102    102       T -> S (in Ref. 3; CAA74969).
FT   CONFLICT    108    108       I -> T (in Ref. 3; CAA74969).
FT   CONFLICT    283    283       I -> F (in Ref. 3; CAA74969).
FT   CONFLICT    331    331       S -> SS (in Ref. 3; CAA74969).
FT   CONFLICT    360    360       F -> S (in Ref. 3; CAA74969).
FT   CONFLICT    436    436       C -> Y (in Ref. 3; CAA74969).
SQ   SEQUENCE   474 AA;  50320 MW;  462EAE398C4D6563 CRC64;
     MAPAALWVAL VFELQLWATG HTVPAQVVLT PYKPEPGYEC QISQEYYDRK AQMCCAKCPP
     GQYVKHFCNK TSDTVCADCE ASMYTQVWNQ FRTCLSCSSS CTTDQVEIRA CTKQQNRVCA
     CEAGRYCALK THSGSCRQCM RLSKCGPGFG VASSRAPNGN VLCKACAPGT FSDTTSSTDV
     CRPHRICSIL AIPGNASTDA VCAPESPTLS AIPRTLYVSQ PEPTRSQPLD QEPGPSQTPS
     ILTSLGSTPI IEQSTKGGIS LPIGLIVGVT SLGLLMLGLV NCIILVQRKK KPSCLQRDAK
     VPHVPDEKSQ DAVGLEQQHL LTTAPSSSSS SLESSASAGD RRAPPGGHPQ ARVMAEAQGF
     QEARASSRIS DSSHGSHGTH VNVTCIVNVC SSSDHSSQCS SQASATVGDP DAKPSASPKD
     EQVPFSQEEC PSQSPCETTE TLQSHEKPLP LGVPDMGMKP SQAGWFDQIA VKVA
//
ID   NECD_MOUSE              Reviewed;         325 AA.
AC   P25233; B9EJJ5; Q542W7; Q61951;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Necdin;
GN   Name=Ndn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryonic carcinoma;
RX   MEDLINE=91298962; PubMed=2069569; DOI=10.1016/0006-291X(91)91812-Q;
RA   Maruyama K., Usami M., Aizawa T., Yoshikawa K.;
RT   "A novel brain-specific mRNA encoding nuclear protein (necdin)
RT   expressed in neurally differentiated embryonal carcinoma cells.";
RL   Biochem. Biophys. Res. Commun. 178:291-296(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ALA-17.
RC   STRAIN=129/Sv;
RX   MEDLINE=96132826; PubMed=8557705; DOI=10.1074/jbc.271.2.918;
RA   Uetsuki T., Takagi K., Sugiura H., Yoshikawa K.;
RT   "Structure and expression of the mouse necdin gene. Identification of
RT   a postmitotic neuron-restrictive core promoter.";
RL   J. Biol. Chem. 271:918-924(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Muellerian duct, and Sympathetic ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH VIRAL TRANSFORMING PROTEINS AND EF21.
RX   MEDLINE=98086237; PubMed=9422723; DOI=10.1074/jbc.273.2.720;
RA   Taniura H., Taniguchi N., Hara M., Yoshikawa K.;
RT   "Necdin, a postmitotic neuron-specific growth suppressor, interacts
RT   with viral transforming proteins and cellular transcription factor
RT   E2F1.";
RL   J. Biol. Chem. 273:720-728(1998).
RN   [6]
RP   INTERACTION WITH TP53.
RX   MEDLINE=99278391; PubMed=10347180; DOI=10.1074/jbc.274.23.16242;
RA   Taniura H., Matsumoto K., Yoshikawa K.;
RT   "Physical and functional interactions of neuronal growth suppressor
RT   necdin with p53.";
RL   J. Biol. Chem. 274:16242-16248(1999).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=20422532; PubMed=10965153; DOI=10.1159/000017455;
RA   Niinobe M., Koyama K., Yoshikawa K.;
RT   "Cellular and subcellular localization of necdin in fetal and adult
RT   mouse brain.";
RL   Dev. Neurosci. 22:310-319(2000).
CC   -!- FUNCTION: Growth suppressor that facilitates the entry of the cell
CC       into cell cycle arrest. Functionally similar to the retinoblastoma
CC       protein it binds to and represses the activity of cell-cycle-
CC       promoting proteins such as SV40 large T antigen, adenovirus E1A,
CC       and the transcription factor E2F. Necdin also interacts with p53
CC       and works in an additive manner to inhibit cell growth. Functions
CC       also as transcription factor and binds directly to specific
CC       guanosine-rich DNA sequences.
CC   -!- SUBUNIT: Binds to the transactivation domains of E2F1 and p53.
CC       Binds also SV40 large T antigen and adenovirus E1A. Interacts with
CC       nucleobindin 1 and 2.
CC   -!- INTERACTION:
CC       Q9Y6B2:EID1 (xeno); NbExp=3; IntAct=EBI-1801080, EBI-1049975;
CC       Q9QYH6:Maged1; NbExp=3; IntAct=EBI-1801080, EBI-1801274;
CC       P13297:Msx1; NbExp=1; IntAct=EBI-1801080, EBI-903969;
CC       Q03358:Msx2; NbExp=1; IntAct=EBI-1801080, EBI-1801354;
CC       O55176-2:Pja1; NbExp=1; IntAct=EBI-1801080, EBI-1801670;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleoplasm. Nucleus
CC       matrix. Note=Mainly cytoplasmic. Translocates to the nucleus where
CC       it is found associated with the nuclear matrix.
CC   -!- TISSUE SPECIFICITY: Brain specific. Not detected in other tissues.
CC       Expressed in postmitotic neurons. In adult brain the highest
CC       expression is in hypothalamus. Highly expressed in thalamus and
CC       midbrain. Relatively low levels are in cerebral cortex,
CC       hippocampus, striatum, olfactory bulb, cerebellum, pons and spinal
CC       cord. Also detected in neurally differentiated embryonal carcinoma
CC       cells.
CC   -!- DEVELOPMENTAL STAGE: Expression levels were high during embryonic
CC       and neonatal periods (E14 to P7) and decreased thereafter.
CC   -!- SIMILARITY: Contains 1 MAGE domain.
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DR   EMBL; M80840; AAA39805.1; -; mRNA.
DR   EMBL; D76440; BAA11183.1; -; Genomic_DNA.
DR   EMBL; AK005078; BAB23802.1; -; mRNA.
DR   EMBL; AK075729; BAC35914.1; -; mRNA.
DR   EMBL; AK075735; BAC35917.1; -; mRNA.
DR   EMBL; AK076025; BAC36130.1; -; mRNA.
DR   EMBL; AK135444; BAE22535.1; -; mRNA.
DR   EMBL; AK149086; BAE28734.1; -; mRNA.
DR   EMBL; BC147249; AAI47250.1; -; mRNA.
DR   EMBL; BC147250; AAI47251.1; -; mRNA.
DR   IPI; IPI00108492; -.
DR   PIR; JN0148; JN0148.
DR   RefSeq; NP_035012.2; NM_010882.3.
DR   UniGene; Mm.400253; -.
DR   ProteinModelPortal; P25233; -.
DR   SMR; P25233; 98-310.
DR   IntAct; P25233; 18.
DR   MINT; MINT-1350583; -.
DR   STRING; P25233; -.
DR   PRIDE; P25233; -.
DR   Ensembl; ENSMUST00000038775; ENSMUSP00000045369; ENSMUSG00000033585.
DR   GeneID; 17984; -.
DR   KEGG; mmu:17984; -.
DR   UCSC; uc009hff.1; mouse.
DR   CTD; 17984; -.
DR   MGI; MGI:97290; Ndn.
DR   eggNOG; maNOG17867; -.
DR   HOGENOM; HBG126941; -.
DR   HOVERGEN; HBG098101; -.
DR   InParanoid; P25233; -.
DR   OMA; KRMIIWF; -.
DR   OrthoDB; EOG4GQQ5P; -.
DR   PhylomeDB; P25233; -.
DR   NextBio; 292955; -.
DR   ArrayExpress; P25233; -.
DR   Bgee; P25233; -.
DR   CleanEx; MM_NDN; -.
DR   Genevestigator; P25233; -.
DR   GermOnline; ENSMUSG00000033585; Mus musculus.
DR   GO; GO:0042995; C:cell projection; IDA:MGI.
DR   GO; GO:0005813; C:centrosome; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0043015; F:gamma-tubulin binding; IDA:MGI.
DR   GO; GO:0048676; P:axon extension involved in development; IMP:MGI.
DR   GO; GO:0007413; P:axonal fasciculation; IMP:MGI.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; TAS:MGI.
DR   GO; GO:0007417; P:central nervous system development; IMP:MGI.
DR   GO; GO:0071514; P:genetic imprinting; IMP:MGI.
DR   GO; GO:0008347; P:glial cell migration; IMP:MGI.
DR   GO; GO:0048871; P:multicellular organismal homeostasis; IMP:MGI.
DR   GO; GO:0048011; P:nerve growth factor receptor signaling pathway; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0001558; P:regulation of cell growth; TAS:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IGI:MGI.
DR   GO; GO:0003016; P:respiratory system process; IMP:MGI.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR002190; MAGE.
DR   PANTHER; PTHR11736; MAGE; 1.
DR   Pfam; PF01454; MAGE; 1.
DR   PROSITE; PS50838; MAGE; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; DNA-binding; Growth regulation; Nucleus; Polymorphism;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    325       Necdin.
FT                                /FTId=PRO_0000156741.
FT   DOMAIN      102    301       MAGE.
FT   VARIANT      17     17       V -> A.
SQ   SEQUENCE   325 AA;  36832 MW;  777385B0B75E443F CRC64;
     MSEQSKDLSD PNFAAEVPDC EMQDSDAVPV GIPPPASLAA NLAGPPCAPE GPMAAQQASP
     PPEERIEDVD PKILQQAAEE GRAHQPQSPA RPIPAPPAPA QLVQKAHELM WYVLVKDQKR
     MVLWFPDMVK EVMGSYKKWC RSILRRTSVI LARVFGLHLR LTNLHTMEFA LVKALSPEEL
     DRVALNNRMP MTGLLLMILS LIYVKGRGAR EGAVWNVLRI LGLRPWKKHS TFGDVRKIIT
     EEFVQQNYLK YQRVPHIEPP EYEFFWGSRA NREITKMQIM EFLARVFKKD PQAWPSRYRE
     ALEQARALRE ANLAAQAPRS SVSED
//
ID   RS2_MOUSE               Reviewed;         293 AA.
AC   P25444;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 3.
DT   08-MAR-2011, entry version 106.
DE   RecName: Full=40S ribosomal protein S2;
DE   AltName: Full=40S ribosomal protein S4;
DE   AltName: Full=Protein LLRep3;
GN   Name=Rps2; Synonyms=Llrep3, Rps4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=88302198; PubMed=3405219;
RA   Heller D.L., Gianola K.M., Leinwand L.A.;
RT   "A highly conserved mouse gene with a propensity to form pseudogenes
RT   in mammals.";
RL   Mol. Cell. Biol. 8:2797-2803(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster;
RA   Smith J.B., Nguyen T.T.;
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; TYR-82 AND SER-85,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-133, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SIMILARITY: Belongs to the ribosomal protein S5P family.
CC   -!- SIMILARITY: Contains 1 S5 DRBM domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA40074.1; Type=Frameshift; Positions=24;
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DR   EMBL; M20632; AAA40074.1; ALT_FRAME; mRNA.
DR   EMBL; AF283559; AAG13953.1; -; mRNA.
DR   EMBL; BC002186; AAH02186.1; -; mRNA.
DR   IPI; IPI00318492; -.
DR   PIR; A31139; A31139.
DR   RefSeq; NP_032529.2; NM_008503.5.
DR   UniGene; Mm.157452; -.
DR   UniGene; Mm.328846; -.
DR   UniGene; Mm.389704; -.
DR   ProteinModelPortal; P25444; -.
DR   SMR; P25444; 1-279.
DR   STRING; P25444; -.
DR   PhosphoSite; P25444; -.
DR   PRIDE; P25444; -.
DR   Ensembl; ENSMUST00000054289; ENSMUSP00000092502; ENSMUSG00000044533.
DR   GeneID; 16898; -.
DR   KEGG; mmu:16898; -.
DR   UCSC; uc008axy.1; mouse.
DR   CTD; 16898; -.
DR   CTD; 546298; -.
DR   CTD; 667279; -.
DR   MGI; MGI:105110; Rps2.
DR   eggNOG; roNOG06562; -.
DR   HOVERGEN; HBG000437; -.
DR   InParanoid; P25444; -.
DR   OMA; NPGVEAP; -.
DR   OrthoDB; EOG4SXND8; -.
DR   PhylomeDB; P25444; -.
DR   NextBio; 290926; -.
DR   Bgee; P25444; -.
DR   CleanEx; MM_RPS2; -.
DR   Genevestigator; P25444; -.
DR   GermOnline; ENSMUSG00000044533; Mus musculus.
DR   GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR014720; dsRNA-bd-like.
DR   InterPro; IPR000851; Ribosomal_S5.
DR   InterPro; IPR005324; Ribosomal_S5_C.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR005711; Ribosomal_S5_euk/arc.
DR   InterPro; IPR013810; Ribosomal_S5_N.
DR   InterPro; IPR018192; Ribosomal_S5_N_CS.
DR   Gene3D; G3DSA:3.30.160.20; dsRNA-bd-like; 1.
DR   Gene3D; G3DSA:3.30.230.10; Ribosomal_S5_D2-type_fold; 1.
DR   PANTHER; PTHR13718; Ribosomal_S5; 1.
DR   Pfam; PF00333; Ribosomal_S5; 1.
DR   Pfam; PF03719; Ribosomal_S5_C; 1.
DR   SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR   TIGRFAMs; TIGR01020; rpsE_arch; 1.
DR   PROSITE; PS00585; RIBOSOMAL_S5; 1.
DR   PROSITE; PS50881; S5_DSRBD; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein; Repeat; Ribonucleoprotein;
KW   Ribosomal protein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    293       40S ribosomal protein S2.
FT                                /FTId=PRO_0000131674.
FT   DOMAIN      102    165       S5 DRBM.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      77     77       Phosphoserine.
FT   MOD_RES      82     82       Phosphotyrosine.
FT   MOD_RES      85     85       Phosphoserine.
FT   MOD_RES     133    133       Phosphotyrosine.
FT   MOD_RES     263    263       N6-acetyllysine (By similarity).
FT   MOD_RES     264    264       Phosphoserine.
FT   MOD_RES     275    275       N6-acetyllysine (By similarity).
FT   MOD_RES     278    278       Phosphothreonine (By similarity).
FT   MOD_RES     281    281       Phosphoserine (By similarity).
FT   MOD_RES     293    293       Phosphothreonine (By similarity).
FT   CONFLICT    270    270       T -> S (in Ref. 1; AAA40074).
SQ   SEQUENCE   293 AA;  31231 MW;  9092DB564AA624C9 CRC64;
     MADDAGAAGG PGGPGGPGLG GRGGFRGGFG SGLRGRGRGR GRGRGRGRGA RGGKAEDKEW
     IPVTKLGRLV KDMKIKSLEE IYLFSLPIKE SEIIDFFLGA SLKDEVLKIM PVQKQTRAGQ
     RTRFKAFVAI GDYNGHVGLG VKCSKEVATA IRGAIILAKL SIVPVRRGYW GNKIGKPHTV
     PCKVTGRCGS VLVRLIPAPR GTGIVSAPVP KKLLMMAGID DCYTSARGCT ATLGNFAKAT
     FDAISKTYSY LTPDLWKETV FTKSPYQEFT DHLVKTHTRV SVQRTQAPAV ATT
//
ID   TLN1_MOUSE              Reviewed;        2541 AA.
AC   P26039; Q8VEF0;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   08-MAR-2011, entry version 115.
DE   RecName: Full=Talin-1;
GN   Name=Tln1; Synonyms=Tln;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Fibroblast;
RX   MEDLINE=91015390; PubMed=2120593; DOI=10.1038/347685a0;
RA   Rees D.J.G., Ades S.A., Singer S.J., Hynes R.O.;
RT   "Sequence and domain structure of talin.";
RL   Nature 347:685-689(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1603-2541.
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2040, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1116, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2040, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2273, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 482-789 IN COMPLEX WITH VCL.
RX   PubMed=15272303; DOI=10.1038/sj.emboj.7600285;
RA   Papagrigoriou E., Gingras A.R., Barsukov I.L., Bate N.,
RA   Fillingham I.J., Patel B., Frank R., Ziegler W.H., Roberts G.C.K.,
RA   Critchley D.R., Emsley J.;
RT   "Activation of a vinculin-binding site in the talin rod involves
RT   rearrangement of a five-helix bundle.";
RL   EMBO J. 23:2942-2951(2004).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 209-410 IN COMPLEX WITH
RP   PIP5K1C.
RX   PubMed=15623515; DOI=10.1074/jbc.M413180200;
RA   de Pereda J.M., Wegener K.L., Santelli E., Bate N., Ginsberg M.H.,
RA   Critchley D.R., Campbell I.D., Liddington R.C.;
RT   "Structural basis for phosphatidylinositol phosphate kinase type
RT   Igamma binding to talin at focal adhesions.";
RL   J. Biol. Chem. 280:8381-8386(2005).
RN   [9]
RP   STRUCTURE BY NMR OF 755-889.
RX   PubMed=15642262; DOI=10.1016/j.str.2004.11.006;
RA   Fillingham I., Gingras A.R., Papagrigoriou E., Patel B., Emsley J.,
RA   Critchley D.R., Roberts G.C.K., Barsukov I.L.;
RT   "A vinculin binding domain from the talin rod unfolds to form a
RT   complex with the vinculin head.";
RL   Structure 13:65-74(2005).
CC   -!- FUNCTION: Probably involved in connections of major cytoskeletal
CC       structures to the plasma membrane. High molecular weight
CC       cytoskeletal protein concentrated at regions of cell-substratum
CC       contact and, in lymphocytes, at cell-cell contacts.
CC   -!- SUBUNIT: Binds with high affinity to vinculin and with low
CC       affinity to integrins. Interacts with NRAP and LAYN. Interacts
CC       with SYNM (By similarity).
CC   -!- INTERACTION:
CC       P05106:ITGB3 (xeno); NbExp=1; IntAct=EBI-1039593, EBI-702847;
CC       P12003:VCL (xeno); NbExp=1; IntAct=EBI-1039593, EBI-1039563;
CC   -!- SUBCELLULAR LOCATION: Cell projection, ruffle membrane; Peripheral
CC       membrane protein; Cytoplasmic side (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity). Note=Colocalizes with LAYN at the
CC       membrane ruffles (By similarity).
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -!- SIMILARITY: Contains 1 I/LWEQ domain.
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DR   EMBL; X56123; CAA39588.1; -; mRNA.
DR   EMBL; BC018557; AAH18557.1; -; mRNA.
DR   IPI; IPI00465786; -.
DR   PIR; S11661; S11661.
DR   UniGene; Mm.208601; -.
DR   PDB; 1SJ7; X-ray; 2.50 A; A/B/C=482-655.
DR   PDB; 1SJ8; X-ray; 2.60 A; A=482-789.
DR   PDB; 1T01; X-ray; 2.06 A; B=605-628.
DR   PDB; 1U89; NMR; -; A=755-889.
DR   PDB; 1XWX; Model; -; A=486-889.
DR   PDB; 1Y19; X-ray; 2.60 A; B/D/F/H/J/L=209-410.
DR   PDB; 1ZW3; X-ray; 3.30 A; B=1628-1652.
DR   PDB; 2B0H; NMR; -; A=1843-1973.
DR   PDB; 2G35; NMR; -; A=305-404.
DR   PDB; 2JSW; NMR; -; A=2300-2482.
DR   PDB; 2KBB; NMR; -; A=1655-1822.
DR   PDB; 2KC1; NMR; -; A=1-85.
DR   PDB; 2KC2; NMR; -; A=86-202.
DR   PDB; 2KGX; NMR; -; A=1655-1822, B=311-401.
DR   PDB; 2KMA; NMR; -; A=1-202.
DR   PDB; 2KVP; NMR; -; A=1815-1973.
DR   PDB; 2QDQ; X-ray; 2.20 A; A/B=2494-2541.
DR   PDB; 2X0C; X-ray; 2.00 A; A=1359-1659.
DR   PDB; 3DYJ; X-ray; 1.85 A; A/B=1974-2293.
DR   PDB; 3IVF; X-ray; 1.94 A; A=1-400.
DR   PDBsum; 1SJ7; -.
DR   PDBsum; 1SJ8; -.
DR   PDBsum; 1T01; -.
DR   PDBsum; 1U89; -.
DR   PDBsum; 1XWX; -.
DR   PDBsum; 1Y19; -.
DR   PDBsum; 1ZW3; -.
DR   PDBsum; 2B0H; -.
DR   PDBsum; 2G35; -.
DR   PDBsum; 2JSW; -.
DR   PDBsum; 2KBB; -.
DR   PDBsum; 2KC1; -.
DR   PDBsum; 2KC2; -.
DR   PDBsum; 2KGX; -.
DR   PDBsum; 2KMA; -.
DR   PDBsum; 2KVP; -.
DR   PDBsum; 2QDQ; -.
DR   PDBsum; 2X0C; -.
DR   PDBsum; 3DYJ; -.
DR   PDBsum; 3IVF; -.
DR   ProteinModelPortal; P26039; -.
DR   SMR; P26039; 2-400, 486-889, 952-1038, 1145-1203, 1359-1659, 1838-1973, 1975-2482, 2496-2529.
DR   DIP; DIP-647N; -.
DR   IntAct; P26039; 9.
DR   MINT; MINT-258500; -.
DR   STRING; P26039; -.
DR   PhosphoSite; P26039; -.
DR   PRIDE; P26039; -.
DR   Ensembl; ENSMUST00000030187; ENSMUSP00000030187; ENSMUSG00000028465.
DR   UCSC; uc008sqe.1; mouse.
DR   MGI; MGI:1099832; Tln1.
DR   HOVERGEN; HBG023870; -.
DR   InParanoid; P26039; -.
DR   OrthoDB; EOG48PMJ8; -.
DR   NextBio; 301428; -.
DR   ArrayExpress; P26039; -.
DR   Bgee; P26039; -.
DR   CleanEx; MM_TLN1; -.
DR   Genevestigator; P26039; -.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR   GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR   GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0005158; F:insulin receptor binding; IEA:InterPro.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0007044; P:cell-substrate junction assembly; IMP:MGI.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:MGI.
DR   GO; GO:0007016; P:cytoskeletal anchoring at plasma membrane; IEA:InterPro.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR002558; ILWEQ.
DR   InterPro; IPR002404; Insln_rcpt_S1.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR015711; Talin.
DR   InterPro; IPR015710; Talin-rel.
DR   InterPro; IPR015224; Talin_cent.
DR   InterPro; IPR015009; Vinculin-bd_dom.
DR   InterPro; IPR006077; Vinculin/catenin.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.1420.10; Talin_cent; 1.
DR   PANTHER; PTHR19981; Talin; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF01608; I_LWEQ; 1.
DR   Pfam; PF02174; IRS; 1.
DR   Pfam; PF09141; Talin_middle; 1.
DR   Pfam; PF08913; VBS; 2.
DR   ProDom; PD011820; ILWEQ; 1.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00307; ILWEQ; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   SUPFAM; SSF109880; Talin_cent; 1.
DR   SUPFAM; SSF47220; Vinculin/catenin; 5.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS50945; I_LWEQ; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell membrane; Cell projection; Cytoplasm;
KW   Cytoskeleton; Membrane; Phosphoprotein.
FT   CHAIN         1   2541       Talin-1.
FT                                /FTId=PRO_0000219429.
FT   DOMAIN       86    403       FERM.
FT   DOMAIN     2293   2533       I/LWEQ.
FT   REGION      280    435       Interaction with LAYN (By similarity).
FT   REGION     1327   1948       Interaction with SYNM (By similarity).
FT   MOD_RES      26     26       Phosphotyrosine (By similarity).
FT   MOD_RES      70     70       Phosphotyrosine (By similarity).
FT   MOD_RES     167    167       Phosphothreonine (By similarity).
FT   MOD_RES     425    425       Phosphoserine (By similarity).
FT   MOD_RES     436    436       Phosphotyrosine (By similarity).
FT   MOD_RES    1116   1116       Phosphotyrosine.
FT   MOD_RES    1945   1945       Phosphotyrosine (By similarity).
FT   MOD_RES    2031   2031       N6-acetyllysine (By similarity).
FT   MOD_RES    2040   2040       Phosphoserine.
FT   MOD_RES    2115   2115       N6-acetyllysine (By similarity).
FT   MOD_RES    2273   2273       Phosphoserine.
FT   MOD_RES    2338   2338       Phosphoserine (By similarity).
FT   MOD_RES    2530   2530       Phosphotyrosine (By similarity).
FT   VARIANT    1105   1105       L -> P.
FT   VARIANT    2180   2180       K -> M.
FT   HELIX       210    224
FT   STRAND      226    228
FT   HELIX       232    247
FT   TURN        252    254
FT   HELIX       262    264
FT   HELIX       268    273
FT   HELIX       276    284
FT   TURN        285    288
FT   HELIX       291    303
FT   TURN        306    309
FT   STRAND      311    317
FT   STRAND      326    332
FT   STRAND      334    340
FT   TURN        342    344
FT   STRAND      347    352
FT   HELIX       353    355
FT   STRAND      358    362
FT   STRAND      365    369
FT   STRAND      371    376
FT   STRAND      378    381
FT   HELIX       385    399
FT   HELIX       493    512
FT   HELIX       526    560
FT   STRAND      565    567
FT   HELIX       570    600
FT   HELIX       606    626
FT   HELIX       634    652
FT   HELIX       664    690
FT   STRAND      696    699
FT   HELIX       700    723
FT   TURN        724    726
FT   HELIX       730    756
FT   HELIX       762    780
FT   HELIX      1631   1649
FT   HELIX      1847   1874
FT   TURN       1875   1877
FT   HELIX      1882   1904
FT   HELIX      1910   1939
FT   HELIX      1944   1968
FT   HELIX      1969   1971
FT   HELIX      2301   2324
FT   STRAND     2332   2334
FT   HELIX      2341   2373
FT   HELIX      2380   2382
FT   HELIX      2383   2416
FT   HELIX      2421   2442
FT   TURN       2443   2445
FT   HELIX      2451   2476
FT   HELIX      2497   2528
SQ   SEQUENCE   2541 AA;  269833 MW;  14EF75ABE9FC2CBB CRC64;
     MVALSLKISI GNVVKTMQFE PSTMVYDACR MIRERIPEAL AGPPNDFGLF LSDDDPKKGI
     WLEAGKALDY YMLRNGDTME YRKKQRPLKI RMLDGTVKTI MVDDSKTVTD MLMTICARIG
     ITNHDEYSLV RELMEEKKDE GTGTLRKDKT LLRDEKKMEK LKQKLHTDDE LNWLDHGRTL
     REQGVEEHET LLLRRKFFYS DQNVDSRDPV QLNLLYVQAR DDILNGSHPV SFDKACEFAG
     FQCQIQFGPH NEQKHKAGFL DLKDFLPKEY VKQKGERKIF QAHKNCGQMS EIEAKVRYVK
     LARSLKTYGV SFFLVKEKMK GKNKLVPRLL GITKECVMRV DEKTKEVIQE WSLTNIKRWA
     ASPKSFTLDF GDYQDGYYSV QTTEGEQIAQ LIAGYIDIIL KKKKSKDHFG LEGDEESTML
     EDSVSPKKST VLQQQYNRVG KVEHGSVALP AIMRSGASGP ENFQVGSMPP AQQQITSGQM
     HRGHMPPLTS AQQALTGTIN SSMQAVQAAQ ATLDDFETLP PLGQDAASKA WRKNKMDESK
     HEIHSQVDAI TAGTASVVNL TAGDPAETDY TAVGCAVTTI SSNLTEMSRG VKLLAALLED
     EGGNGRPLLQ AAKGLAGAVS ELLRSAQPAS AEPRQNLLQA AGNVGQASGE LLQQIGESDT
     DPHFQDVLMQ LANAVASAAA ALVLKAKSVA QRTEDSGLQT QVIAAATQCA LSTSQLVACT
     KVVAPTISSP VCQEQLVEAG RLVAKAVEGC VSASQAATED GQLLRGVGAA ATAVTQALNE
     LLQHVKAHAT GAGPAGRYDQ ATDTILTVTE NIFSSMGDAG EMVRQARILA QATSDLVNAI
     KADAEGESDL ENSRKLLSAA KILADATAKM VEAAKGAAAH PDSEEQQQRL REAAEGLRMA
     TNAAAQNAIK KKLVQRLEHA AKQAAASATQ TIAAAQHAAS APKASAGPQP LLVQSCKAVA
     EQIPLLVQGV RGSQAQPDSP SAQLALIAAS QSFLQPGGKM VAAAKASVPT IQDQASAMQL
     SQCAKNLGTA LAELRTAAQK AQEACGPLEM DSALSVVQNL EKDLQEIKAA ARDGKLKPLP
     GETMEKCTQD LGNSTKAVSS AIAKLLGEIA QGNENYAGIA ARDVAGGLRS LAQAARGVAA
     LTSDPAVQAI VLDTASDVLD KASSLIEEAK KASGHPGDPE SQQRLAQVAK AVTQALNRCV
     SCLPGQRDVD NALRAVGDAS KRLLSDLLPP STGTFQEAQS RLNEAAAGLN QAATELVQAS
     RGTPQDLARA SGRFGQDFST FLEAGVEMAG QAPSQEDRAQ VVSNLKGISM SSSKLLLAAK
     ALSTDPASPN LKSQLAAAAR AVTDSINQLI TMCTQQAPGQ KECDNALRQL ETVRELLENP
     VQPINDMSYF GCLDSVMENS KVLGEAMTGI SQNAKNGNLP EFGDAIATAS KALCGFTEAA
     AQAAYLVGVS DPNSQAGQQG LVEPTQFARA NQAIQMACQS LGEPGCTQAQ VLSAATIVAK
     HTSALCNSCR LASARTANPT AKRQFVQSAK EVANSTANLV KTIKALDGDF TEENRAQCRA
     ATAPLLEAVD NLSAFASNPE FSSVPAQISP EGRAAMEPIV ISAKTMLESA GGLIQTARAL
     AVNPRDPPRW SVLAGHSRTV SDSIKKLITS MRDKAPGQLE CETAIAALNS CLRDLDQASL
     AAVSQQLAPR EGISQEALHT QMLTAVQEIS HLIEPLASAA RAEASQLGHK VSQMAQYFEP
     LTLAAVGAAS KTLSHPQQMA LLDQTKTLAE SALQLLYTAK EAGGNPKQAA HTQEALEEAV
     QMMTEAVEDL TTTLNEAASA AGVVGGMVDS ITQAINQLDE GPMGDPEGSF VDYQTTMVRT
     AKAIAVTVQE MVTKSNTSPE ELGPLANQLT SDYGRLASQA KPAAVAAENE EIGAHIKHRV
     QELGHGCSAL VTKAGALQCS PSDVYTKKEL IECARRVSEK VSHVLAALQA GNRGTQACIT
     AASAVSGIIA DLDTTIMFAT AGTLNREGAE TFADHREGIL KTAKVLVEDT KVLVQNAAGS
     QEKLAQAAQS SVATITRLAD VVKLGAASLG AEDPETQVVL INAVKDVAKA LGDLISATKA
     AAGKVGDDPA VWQLKNSAKV MVTNVTSLLK TVKAVEDEAT KGTRALEATT EHIRQELAVF
     CSPEPPAKTS TPEDFIRMTK GITMATAKAV AAGNSCRQED VIATANLSRR AIADMLRACK
     EAAFHPEVAP DVRLRALHYG RECANGYLEL LDHVLLTLQK PNPDLKQQLT GHSKRVAGSV
     TELIQAAEAM KGTEWVDPED PTVIAENELL GAAAAIEAAA KKLEQLKPRA KPKEADESLN
     FEEQILEAAK SIAAATSALV KAASAAQREL VAQGKVGAIP ANALDDGQWS QGLISAARMV
     AAATNNLCEA ANAAVQGHAS QEKLISSAKQ VAASTAQLLV ACKVKADQDS EAMKRLQAAG
     NAVKRASDNL VKAAQKAAAF EDQENETVVV KEKMVGGIAQ IIAAQEEMLR KERELEEARK
     KLAQIRQQQY KFLPSELRDE H
//
ID   GBRA2_MOUSE             Reviewed;         451 AA.
AC   P26048;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit alpha-2;
DE   AltName: Full=GABA(A) receptor subunit alpha-2;
DE   Flags: Precursor;
GN   Name=Gabra2; Synonyms=Gabra-2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J, and DBA/2J; TISSUE=Brain;
RX   MEDLINE=93002190; PubMed=1356407;
RA   Wang J.B., Kofuji P., Fernando J.C., Moss S.J., Huganir R.L.,
RA   Burt D.R.;
RT   "The alpha 1, alpha 2, and alpha 3 subunits of GABAA receptors:
RT   comparison in seizure-prone and -resistant mice and during
RT   development.";
RL   J. Mol. Neurosci. 3:177-184(1992).
RN   [2]
RP   INTERACTION WITH UBQLN1.
RX   MEDLINE=21419682; PubMed=11528422; DOI=10.1038/nn0901-908;
RA   Bedford F.K., Kittler J.T., Muller E., Thomas P., Uren J.M., Merlo D.,
RA   Wisden W., Triller A., Smart T.G., Moss S.J.;
RT   "GABA(A) receptor cell surface number and subunit stability are
RT   regulated by the ubiquitin-like protein Plic-1.";
RL   Nat. Neurosci. 4:908-916(2001).
CC   -!- FUNCTION: GABA, the major inhibitory neurotransmitter in the
CC       vertebrate brain, mediates neuronal inhibition by binding to the
CC       GABA/benzodiazepine receptor and opening an integral chloride
CC       channel.
CC   -!- SUBUNIT: Generally pentameric. There are five types of GABA(A)
CC       receptor chains: alpha, beta, gamma, delta, and rho. Binds UBQLN1.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane; Multi-pass membrane protein. Cell membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
CC       family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily.
CC       GABRA2 sub-subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M86567; AAA37650.1; -; mRNA.
DR   IPI; IPI00110598; -.
DR   RefSeq; NP_032092.1; NM_008066.3.
DR   UniGene; Mm.5304; -.
DR   ProteinModelPortal; P26048; -.
DR   SMR; P26048; 279-339.
DR   STRING; P26048; -.
DR   PRIDE; P26048; -.
DR   Ensembl; ENSMUST00000000572; ENSMUSP00000000572; ENSMUSG00000000560.
DR   GeneID; 14395; -.
DR   KEGG; mmu:14395; -.
DR   UCSC; uc008xqw.1; mouse.
DR   CTD; 14395; -.
DR   MGI; MGI:95614; Gabra2.
DR   eggNOG; roNOG13930; -.
DR   HOGENOM; HBG506497; -.
DR   HOVERGEN; HBG051707; -.
DR   InParanoid; P26048; -.
DR   OMA; MKMKLNI; -.
DR   OrthoDB; EOG4ZS935; -.
DR   PhylomeDB; P26048; -.
DR   NextBio; 460878; -.
DR   ArrayExpress; P26048; -.
DR   Bgee; P26048; -.
DR   Genevestigator; P26048; -.
DR   GermOnline; ENSMUSG00000000560; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0004890; F:GABA-A receptor activity; IEA:InterPro.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IEA:InterPro.
DR   InterPro; IPR006028; GABAA_rcpt.
DR   InterPro; IPR001390; GABAAa_rcpt.
DR   InterPro; IPR005432; GABBAa2_rcpt.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   Gene3D; G3DSA:2.70.170.10; Neur_chan_lig_bd; 1.
DR   PANTHER; PTHR18945; Neur_channel; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 2.
DR   PRINTS; PR01079; GABAARALPHA.
DR   PRINTS; PR01615; GABAARALPHA2.
DR   PRINTS; PR00253; GABAARECEPTR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF90112; Neu_channel_TM; 1.
DR   SUPFAM; SSF63712; Neur_chan_LBD; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Chloride; Chloride channel;
KW   Disulfide bond; Glycoprotein; Ion transport; Ionic channel;
KW   Ligand-gated ion channel; Membrane; Postsynaptic cell membrane;
KW   Receptor; Signal; Synapse; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL        1     28       Potential.
FT   CHAIN        29    451       Gamma-aminobutyric acid receptor subunit
FT                                alpha-2.
FT                                /FTId=PRO_0000000434.
FT   TOPO_DOM     29    251       Extracellular (Probable).
FT   TRANSMEM    252    273       Helical; (Probable).
FT   TRANSMEM    279    300       Helical; (Probable).
FT   TRANSMEM    313    334       Helical; (Probable).
FT   TOPO_DOM    335    419       Cytoplasmic (Probable).
FT   TRANSMEM    420    441       Helical; (Probable).
FT   CARBOHYD     38     38       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    138    138       N-linked (GlcNAc...) (Potential).
FT   DISULFID    166    180       By similarity.
SQ   SEQUENCE   451 AA;  51139 MW;  C5E47898963A36CF CRC64;
     MKTKLSTCNV WSLLLVLLVW DPVRLVLANI QEDEAKNNIT IFTRILDRLL DGYDNRLRPG
     LGDSITEVFT NIYVTSFGPV SDTDMEYTID VFFRQKWKDE RLKFKGPMNI LRLNNLMASK
     IWTPDTFFHN GKKSVAHNMT MPNKLLRIQD DGTLLYTMRL TVQAECPMHL EDFPMDAHSC
     PLKFGSYAYT TSEVTYIWTY NASDSVQVAP DGSRLNQYDL LGQSIGKETI KSSTGEYTVM
     TAHFHLKRKI GYFVIQTYLP CIMTVILSQV SFWLNRESVP ARTVFGVTTV LTMTTLSISA
     RNSLPKVAYA TAMDWFIAVC YAFVFSALIE FATVNYFTKR GWAWDGKSVV NDKKKEKGSV
     MIQNNAYAVA VANYAPNLSK DPVLSTISKS ATTPEPNKKP ENKPAEAKKT FNSVSKIDRM
     SRIVFPVLFG TFNLVYWATY LNREPVLGVS P
//
ID   GBRA3_MOUSE             Reviewed;         492 AA.
AC   P26049;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit alpha-3;
DE   AltName: Full=GABA(A) receptor subunit alpha-3;
DE   Flags: Precursor;
GN   Name=Gabra3; Synonyms=Gabra-3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J, and DBA/2J; TISSUE=Brain;
RX   MEDLINE=93002190; PubMed=1356407;
RA   Wang J.B., Kofuji P., Fernando J.C., Moss S.J., Huganir R.L.,
RA   Burt D.R.;
RT   "The alpha 1, alpha 2, and alpha 3 subunits of GABAA receptors:
RT   comparison in seizure-prone and -resistant mice and during
RT   development.";
RL   J. Mol. Neurosci. 3:177-184(1992).
RN   [2]
RP   INTERACTION WITH UBQLN1.
RX   MEDLINE=21419682; PubMed=11528422; DOI=10.1038/nn0901-908;
RA   Bedford F.K., Kittler J.T., Muller E., Thomas P., Uren J.M., Merlo D.,
RA   Wisden W., Triller A., Smart T.G., Moss S.J.;
RT   "GABA(A) receptor cell surface number and subunit stability are
RT   regulated by the ubiquitin-like protein Plic-1.";
RL   Nat. Neurosci. 4:908-916(2001).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: GABA, the major inhibitory neurotransmitter in the
CC       vertebrate brain, mediates neuronal inhibition by binding to the
CC       GABA/benzodiazepine receptor and opening an integral chloride
CC       channel.
CC   -!- SUBUNIT: Generally pentameric. There are five types of GABA(A)
CC       receptor chains: alpha, beta, gamma, delta, and rho. Binds UBQLN1.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane; Multi-pass membrane protein. Cell membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
CC       family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily.
CC       GABRA3 sub-subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M86568; AAA37651.1; -; mRNA.
DR   IPI; IPI00110601; -.
DR   RefSeq; NP_032093.3; NM_008067.4.
DR   UniGene; Mm.102286; -.
DR   UniGene; Mm.447666; -.
DR   ProteinModelPortal; P26049; -.
DR   SMR; P26049; 304-364.
DR   STRING; P26049; -.
DR   PhosphoSite; P26049; -.
DR   PRIDE; P26049; -.
DR   Ensembl; ENSMUST00000055966; ENSMUSP00000062638; ENSMUSG00000031343.
DR   Ensembl; ENSMUST00000114554; ENSMUSP00000110201; ENSMUSG00000031343.
DR   GeneID; 14396; -.
DR   KEGG; mmu:14396; -.
DR   UCSC; uc009tkp.1; mouse.
DR   CTD; 14396; -.
DR   MGI; MGI:95615; Gabra3.
DR   eggNOG; roNOG05645; -.
DR   HOVERGEN; HBG051707; -.
DR   InParanoid; P26049; -.
DR   OrthoDB; EOG4X0MSC; -.
DR   PhylomeDB; P26049; -.
DR   ArrayExpress; P26049; -.
DR   Bgee; P26049; -.
DR   Genevestigator; P26049; -.
DR   GermOnline; ENSMUSG00000031343; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0004890; F:GABA-A receptor activity; IEA:InterPro.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IEA:InterPro.
DR   InterPro; IPR006028; GABAA_rcpt.
DR   InterPro; IPR001390; GABAAa_rcpt.
DR   InterPro; IPR005433; GABBAa3_rcpt.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   Gene3D; G3DSA:2.70.170.10; Neur_chan_lig_bd; 1.
DR   PANTHER; PTHR18945; Neur_channel; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 2.
DR   PRINTS; PR01079; GABAARALPHA.
DR   PRINTS; PR01616; GABAARALPHA3.
DR   PRINTS; PR00253; GABAARECEPTR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF90112; Neu_channel_TM; 1.
DR   SUPFAM; SSF63712; Neur_chan_LBD; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Chloride; Chloride channel;
KW   Disulfide bond; Glycoprotein; Ion transport; Ionic channel;
KW   Ligand-gated ion channel; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Receptor; Signal; Synapse; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     28       Potential.
FT   CHAIN        29    492       Gamma-aminobutyric acid receptor subunit
FT                                alpha-3.
FT                                /FTId=PRO_0000000438.
FT   TOPO_DOM     29    276       Extracellular (Probable).
FT   TRANSMEM    277    298       Helical; (Probable).
FT   TRANSMEM    304    325       Helical; (Probable).
FT   TRANSMEM    338    359       Helical; (Probable).
FT   TOPO_DOM    360    457       Cytoplasmic (Probable).
FT   TRANSMEM    458    479       Helical; (Probable).
FT   MOD_RES     433    433       Phosphoserine.
FT   CARBOHYD     63     63       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    163    163       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    176    176       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    228    228       N-linked (GlcNAc...) (Potential).
FT   DISULFID    191    205       By similarity.
SQ   SEQUENCE   492 AA;  55398 MW;  3CA193B97833CAE2 CRC64;
     MIITQMWHFY VTRVVLLLLI SILPGTTSQG ESRRQEPGDF VKQDIGGLSP KHAPDIPDDS
     TDNITIFTRI LDRLLDGYDN RLRPGLGDAV TEVKTDIYVT SFGPVSDTDM EYTIDVFFRQ
     TWHDERLKFD GPMKILPLNN LLASKIWTPD TFFHNGKKSV AHNMTTPNKL LRLVDNGTLL
     YTMRLTIHAE CPMHLEDFPM DVHACPLKFG SYAYTKAEVI YSWTLGKNKS VEVAQDGSRL
     NQYDLLGHVV GTEIIRSSTG EYVVMTTHFH LKRKIGYFVI QTYLPCIMTV ILSQVSFWLN
     RESVPARTVF GVTTVLTMTT LSISARNSLP KVAYATAMDW FIAVCYAFVF SALIEFATVN
     YFTKRSWAWE GKKVPEALEM KKKTPAAPTK KNTTFNIVGT TYPINLAKDT EFSTISKSAA
     APSASSTPTA IASPKATYVQ DSPAETKTYN SVSKVDKISR IIFPVLFAIF NLVYWATYVN
     RESAIKGMIR KQ
//
ID   CTNA1_MOUSE             Reviewed;         906 AA.
AC   P26231;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   08-MAR-2011, entry version 112.
DE   RecName: Full=Catenin alpha-1;
DE   AltName: Full=102 kDa cadherin-associated protein;
DE   AltName: Full=Alpha E-catenin;
DE   AltName: Full=CAP102;
GN   Name=Ctnna1; Synonyms=Catna1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=129/Sv;
RX   MEDLINE=92021009; PubMed=1924379; DOI=10.1073/pnas.88.20.9156;
RA   Herrenknecht K., Ozawa M., Eckerskorn C., Lottspeich F., Lenter M.,
RA   Kemler R.;
RT   "The uvomorulin-anchorage protein alpha catenin is a vinculin
RT   homologue.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:9156-9160(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=91249391; PubMed=1904011; DOI=10.1016/0092-8674(91)90392-C;
RA   Nagafuchi A., Takeichi M., Tsukita S.;
RT   "The 102 kd cadherin-associated protein: similarity to vinculin and
RT   posttranscriptional regulation of expression.";
RL   Cell 65:849-857(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
RX   PubMed=7982500; DOI=10.1016/0014-5793(94)01205-9;
RA   Butz S., Kemler R.;
RT   "Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell
RT   adhesion.";
RL   FEBS Lett. 355:195-200(1994).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641; THR-654 AND
RP   THR-658, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   RECONSTITUTION OF THE E-CADHERIN/CATENIN ADHESION COMPLEX, AND LACK OF
RP   ACTIN BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
RX   PubMed=16325582; DOI=10.1016/j.cell.2005.09.020;
RA   Yamada S., Pokutta S., Drees F., Weis W.I., Nelson W.J.;
RT   "Deconstructing the cadherin-catenin-actin complex.";
RL   Cell 123:889-901(2005).
RN   [7]
RP   SUBUNIT, AND FUNCTION.
RX   PubMed=16325583; DOI=10.1016/j.cell.2005.09.021;
RA   Drees F., Pokutta S., Yamada S., Nelson W.J., Weis W.I.;
RT   "Alpha-catenin is a molecular switch that binds E-cadherin-beta-
RT   catenin and regulates actin-filament assembly.";
RL   Cell 123:903-915(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-652 AND SER-655, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-654; SER-655 AND
RP   THR-658, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641 AND SER-652, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [14]
RP   INTERACTION WITH LIMA1, AND LACK OF ACTIN BINDING BY THE
RP   E-CADHERIN/CATENIN ADHESION COMPLEX.
RX   PubMed=18093941; DOI=10.1073/pnas.0710504105;
RA   Abe K., Takeichi M.;
RT   "EPLIN mediates linkage of the cadherin catenin complex to F-actin and
RT   stabilizes the circumferential actin belt.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:13-19(2008).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 57-261 IN COMPLEX WITH
RP   CTNNB1.
RX   MEDLINE=20337986; PubMed=10882138; DOI=10.1016/S1097-2765(00)80447-5;
RA   Pokutta S., Weis W.I.;
RT   "Structure of the dimerization and beta-catenin-binding region of
RT   alpha-catenin.";
RL   Mol. Cell 5:533-543(2000).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 385-651, AND INTERACTION WITH
RP   MLLT4 AND F-ACTIN.
RX   PubMed=11907041; DOI=10.1074/jbc.M201463200;
RA   Pokutta S., Drees F., Takai Y., Nelson W.J., Weis W.I.;
RT   "Biochemical and structural definition of the l-afadin- and actin-
RT   binding sites of alpha-catenin.";
RL   J. Biol. Chem. 277:18868-18874(2002).
CC   -!- FUNCTION: Associates with the cytoplasmic domain of a variety of
CC       cadherins. The association of catenins to cadherins produces a
CC       complex which is linked to the actin filament network, and which
CC       seems to be of primary importance for cadherins cell-adhesion
CC       properties. Can associate with both E- and N-cadherins. Originally
CC       believed to be a stable component of E-cadherin/catenin adhesion
CC       complexes and to mediate the linkage of cadherins to the actin
CC       cytoskeleton at adherens junctions. In contrast, cortical actin
CC       was found to be much more dynamic than E-cadherin/catenin
CC       complexes and CTNNA1 was shown not to bind to F-actin when
CC       assembled in the complex suggesting a different linkage between
CC       actin and adherence junctions components. The homodimeric form may
CC       regulate actin filament assembly and inhibit actin branching by
CC       competing with the Arp2/3 complex for binding to actin filaments.
CC       May play a crucial role in cell differentiation.
CC   -!- SUBUNIT: Monomer and homodimer; the monomer preferentially binds
CC       to CTNNB1 and the homodimer to actin. Binds MLLT4 and F-actin.
CC       Possible component of an E-cadherin/ catenin adhesion complex
CC       together with E-cadherin/CDH1 and beta-catenin/CTNNB1 or gamma-
CC       catenin/JUP; the complex is located to adherens junctions. The
CC       stable association of CTNNA1 is controversial as CTNNA1 was shown
CC       not to bind to F-actin when assembled in the complex.
CC       Alternatively, the CTNNA1-containing complex may be linked to F-
CC       actin by other proteins such as LIMA1. Interacts with ARHGAP21 and
CC       with JUB (By similarity). Interacts with LIMA1.
CC   -!- INTERACTION:
CC       Q02248:Ctnnb1; NbExp=1; IntAct=EBI-647895, EBI-397872;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction,
CC       adherens junction. Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Cell junction. Note=Found at cell-cell
CC       boundaries and probably at cell-matrix boundaries.
CC   -!- TISSUE SPECIFICITY: Expressed ubiquitously in normal tissues.
CC   -!- PTM: Sumoylated (By similarity).
CC   -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
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DR   EMBL; X59990; CAA42607.1; -; mRNA.
DR   EMBL; D90362; BAA14376.1; -; mRNA.
DR   EMBL; BC048163; AAH48163.1; -; mRNA.
DR   IPI; IPI00112963; -.
DR   PIR; A39529; A39529.
DR   RefSeq; NP_033948.1; NM_009818.1.
DR   UniGene; Mm.18962; -.
DR   PDB; 1DOV; X-ray; 3.00 A; A=82-262.
DR   PDB; 1DOW; X-ray; 1.80 A; A=57-261.
DR   PDB; 1L7C; X-ray; 2.50 A; A/B/C=385-651.
DR   PDBsum; 1DOV; -.
DR   PDBsum; 1DOW; -.
DR   PDBsum; 1L7C; -.
DR   ProteinModelPortal; P26231; -.
DR   SMR; P26231; 57-261, 377-631.
DR   IntAct; P26231; 5.
DR   MINT; MINT-138480; -.
DR   STRING; P26231; -.
DR   PhosphoSite; P26231; -.
DR   PRIDE; P26231; -.
DR   Ensembl; ENSMUST00000042345; ENSMUSP00000049007; ENSMUSG00000037815.
DR   GeneID; 12385; -.
DR   KEGG; mmu:12385; -.
DR   UCSC; uc008ely.1; mouse.
DR   CTD; 12385; -.
DR   MGI; MGI:88274; Ctnna1.
DR   eggNOG; roNOG05635; -.
DR   HOGENOM; HBG356872; -.
DR   HOVERGEN; HBG000069; -.
DR   InParanoid; P26231; -.
DR   OMA; HAGNINF; -.
DR   OrthoDB; EOG49W2G4; -.
DR   PhylomeDB; P26231; -.
DR   NextBio; 281096; -.
DR   ArrayExpress; P26231; -.
DR   Bgee; P26231; -.
DR   CleanEx; MM_CTNNA1; -.
DR   Genevestigator; P26231; -.
DR   GermOnline; ENSMUSG00000037815; Mus musculus.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0005915; C:zonula adherens; IDA:MGI.
DR   GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR   GO; GO:0045296; F:cadherin binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0043297; P:apical junction assembly; IMP:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptosis; IMP:MGI.
DR   GO; GO:0007406; P:negative regulation of neuroblast proliferation; IGI:MGI.
DR   GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IGI:MGI.
DR   InterPro; IPR001033; Alpha_catenin.
DR   InterPro; IPR006077; Vinculin/catenin.
DR   InterPro; IPR000633; Vinculin_CS.
DR   Pfam; PF01044; Vinculin; 2.
DR   PRINTS; PR00805; ALPHACATENIN.
DR   SUPFAM; SSF47220; Vinculin/catenin; 4.
DR   PROSITE; PS00663; VINCULIN_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell adhesion; Cell junction;
KW   Cell membrane; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Membrane; Phosphoprotein; Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    906       Catenin alpha-1.
FT                                /FTId=PRO_0000064262.
FT   REGION        2    228       Involved in homodimerization (By
FT                                similarity).
FT   REGION       97    148       Interaction with JUP and CTNNB1 (By
FT                                similarity).
FT   REGION      325    394       Interaction with alpha-actinin (By
FT                                similarity).
FT   MOD_RES       2      2       N-acetylthreonine (By similarity).
FT   MOD_RES     177    177       Phosphotyrosine (By similarity).
FT   MOD_RES     186    186       N6-acetyllysine (By similarity).
FT   MOD_RES     619    619       Phosphotyrosine (By similarity).
FT   MOD_RES     641    641       Phosphoserine.
FT   MOD_RES     645    645       Phosphothreonine (By similarity).
FT   MOD_RES     652    652       Phosphoserine.
FT   MOD_RES     654    654       Phosphothreonine.
FT   MOD_RES     655    655       Phosphoserine.
FT   MOD_RES     658    658       Phosphothreonine.
FT   HELIX        59     82
FT   STRAND       84     86
FT   HELIX        87    113
FT   HELIX       118    165
FT   HELIX       170    195
FT   HELIX       201    230
FT   HELIX       235    259
FT   HELIX       392    396
FT   HELIX       399    409
FT   HELIX       413    440
FT   HELIX       444    473
FT   HELIX       478    506
FT   HELIX       508    531
FT   HELIX       535    560
FT   HELIX       567    581
FT   HELIX       583    598
FT   HELIX       608    629
SQ   SEQUENCE   906 AA;  100106 MW;  3ED1EC50925DBBB5 CRC64;
     MTAVHAGNIN FKWDPKSLEI RTLAVERLLE PLVTQVTTLV NTNSKGPSNK KRGRSKKAHV
     LAASVEQATE NFLEKGDKIA KESQFLKEEL VVAVEDVRKQ GDLMKSAAGE FADDPCSSVK
     RGNMVRAARA LLSAVTRLLI LADMADVYKL LVQLKVVEDG ILKLRNAGNE QDLGIQYKAL
     KPEVDKLNIM AAKRQQELKD VGNRDQMAAA RGILQKNVPI LYTASQACLQ HPDVAAYKAN
     RDLIYKQLQQ AVTGISNAAQ ATASDDAAQH QGGSGGELAY ALNNFDKQII VDPLSFSEER
     FRPSLEERLE SIISGAALMA DSSCTRDDRR ERIVAECNAV RQALQDLLSE YMGNAGRKER
     SDALNSAIDK MTKKTRDLRR QLRKAVMDHV SDSFLETNVP LLVLIEAAKN GNEKEVKEYA
     QVFREHANKL IEVANLACSI SNNEEGVKLV RMSASQLEAL CPQVINAALA LAAKPQSKLA
     QENMDLFKEQ WEKQVRVLTD AVDDITSIDD FLAVSENHIL EDVNKCVIAL QEKDVDGLDR
     TAGAIRGRAA RVIHVVTSEM DNYEPGVYTE KVLEATKLLS NTVMPRFTEQ VEAAVEALSS
     DPAQPMDENE FIDASRLVYD GIRDIRKAVL MIRTPEELDD SDFETEDFDV RSRTSVQTED
     DQLIAGQSAR AIMAQLPQEQ KAKIAEQVAS FQEEKSKLDA EVSKWDDSGN DIIVLAKQMC
     MIMMEMTDFT RGKGPLKNTS DVISAAKKIA EAGSRMDKLG RTIADHCPDS ACKQDLLAYL
     QRIALYCHQL NICSKVKAEV QNLGGELVVS GVDSAMSLIQ AAKNLMNAVV QTVKASYVAS
     TKYQKSQGMA SLNLPAVSWK MKAPEKKPLV KREKQDETQT KIKRASQKKH VNPVQALSEF
     KAMDSI
//
ID   CMGA_MOUSE              Reviewed;         463 AA.
AC   P26339;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Chromogranin-A;
DE            Short=CgA;
DE   Contains:
DE     RecName: Full=Pancreastatin;
DE   Contains:
DE     RecName: Full=Beta-granin;
DE   Contains:
DE     RecName: Full=WE-14;
DE   Flags: Precursor;
GN   Name=Chga;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=91302337; PubMed=2071596;
RA   Wu H.J., Rozansky D.J., Parmer R.J., Gill B.M., O'Connor D.T.;
RT   "Structure and function of the chromogranin A gene. Clues to evolution
RT   and tissue-specific expression.";
RL   J. Biol. Chem. 266:13130-13134(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Pancreastatin strongly inhibits glucose induced insulin
CC       release from the pancreas.
CC   -!- INTERACTION:
CC       P00441:SOD1 (xeno); NbExp=2; IntAct=EBI-990900, EBI-990792;
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Neuroendocrine and endocrine
CC       secretory granules.
CC   -!- PTM: CgA is O-glycosylated.
CC   -!- MISCELLANEOUS: Binds calcium with a low-affinity.
CC   -!- SIMILARITY: Belongs to the chromogranin/secretogranin protein
CC       family.
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DR   EMBL; M64278; AAA37457.1; -; mRNA.
DR   EMBL; BC026554; AAH26554.1; -; mRNA.
DR   IPI; IPI00113703; -.
DR   PIR; A39868; A39868.
DR   RefSeq; NP_031719.1; NM_007693.1.
DR   UniGene; Mm.4137; -.
DR   ProteinModelPortal; P26339; -.
DR   IntAct; P26339; 9.
DR   STRING; P26339; -.
DR   PhosphoSite; P26339; -.
DR   PRIDE; P26339; -.
DR   Ensembl; ENSMUST00000021610; ENSMUSP00000021610; ENSMUSG00000021194.
DR   GeneID; 12652; -.
DR   KEGG; mmu:12652; -.
DR   UCSC; uc007oui.1; mouse.
DR   CTD; 12652; -.
DR   MGI; MGI:88394; Chga.
DR   eggNOG; roNOG16074; -.
DR   HOGENOM; HBG280118; -.
DR   HOVERGEN; HBG001272; -.
DR   InParanoid; P26339; -.
DR   OMA; EWEDAKR; -.
DR   OrthoDB; EOG4CZBGF; -.
DR   PhylomeDB; P26339; -.
DR   NextBio; 281864; -.
DR   ArrayExpress; P26339; -.
DR   Bgee; P26339; -.
DR   CleanEx; MM_CHGA; -.
DR   Genevestigator; P26339; -.
DR   GermOnline; ENSMUSG00000021194; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   InterPro; IPR001819; Chromogranin_AB.
DR   InterPro; IPR018054; Chromogranin_CS.
DR   InterPro; IPR001990; Granin.
DR   PANTHER; PTHR10583; Chromogranin_AB; 1.
DR   Pfam; PF01271; Granin; 2.
DR   PRINTS; PR00659; CHROMOGRANIN.
DR   PROSITE; PS00422; GRANINS_1; 1.
DR   PROSITE; PS00423; GRANINS_2; 1.
PE   1: Evidence at protein level;
KW   Amidation; Calcium; Cleavage on pair of basic residues;
KW   Disulfide bond; Glycoprotein; Phosphoprotein; Secreted; Signal.
FT   SIGNAL        1     18
FT   CHAIN        19    463       Chromogranin-A.
FT                                /FTId=PRO_0000005422.
FT   PEPTIDE      19    151       Beta-granin (By similarity).
FT                                /FTId=PRO_0000005423.
FT   PEPTIDE     276    329       Pancreastatin (By similarity).
FT                                /FTId=PRO_0000005424.
FT   PEPTIDE     358    371       WE-14 (By similarity).
FT                                /FTId=PRO_0000005425.
FT   COMPBIAS    103    116       Poly-Gln.
FT   COMPBIAS    236    245       Poly-Glu.
FT   COMPBIAS    340    347       Poly-Glu.
FT   MOD_RES     132    132       Phosphoserine (By similarity).
FT   MOD_RES     156    156       Phosphoserine (By similarity).
FT   MOD_RES     220    220       Phosphoserine (By similarity).
FT   MOD_RES     308    308       Phosphoserine (By similarity).
FT   MOD_RES     329    329       Glycine amide (Probable).
FT   MOD_RES     414    414       Phosphoserine (By similarity).
FT   DISULFID     35     56       By similarity.
SQ   SEQUENCE   463 AA;  51789 MW;  1AB3C5FF433C39E4 CRC64;
     MRSTAVLALL LCAGQVFALP VNSPMTKGDT KVMKCVLEVI SDSLSKPSPM PVSPECLETL
     QGDERILSIL RHQNLLKELQ DLALQGAKER AQQPLKQQQP PKQQQQQQQQ QQQEQQHSSF
     EDELSEVFEN QSPDAKHRDA AAEVPSRDTM EKRKDSDKGQ QDGFEATTEG PRPQAFPEPN
     QESPMMGDSE SPGEDTATNT QSPTSLPSQE HVDPQATGDS ERGLSAQQQA RKAKQEEKEE
     EEEEEAVARE KAGPEEVPTA ASSSHFHAGY KAIQKDDGQS DSQAVDGDGK TEASEALPSE
     GKGELEHSQQ EEDGEEAMVG TPQGLFPQGG KGRELEHKQE EEEEEEERLS REWEDKRWSR
     MDQLAKELTA EKRLEGEDDP DRSMKLSFRT RAYGFRDPGP QLRRGWRPSS REDSVEARSD
     FEEKKEEEGS ANRRAEDQEL ESLSAIEAEL EKVAHQLQAL RRG
//
ID   U2AF2_MOUSE             Reviewed;         475 AA.
AC   P26369;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Splicing factor U2AF 65 kDa subunit;
DE   AltName: Full=U2 auxiliary factor 65 kDa subunit;
DE   AltName: Full=U2 snRNP auxiliary factor large subunit;
GN   Name=U2af2; Synonyms=U2af65;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=SL/AM;
RX   MEDLINE=92279036; PubMed=1594454; DOI=10.1093/nar/20.9.2374;
RA   Sailer A., Macdonald N.J., Weissmann C.;
RT   "Cloning and sequencing of the murine homologue of the human splicing
RT   factor U2AF65.";
RL   Nucleic Acids Res. 20:2374-2374(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   INTERACTION WITH U2AF1L4.
RX   PubMed=16819553; DOI=10.1038/ni1361;
RA   Heyd F., ten Dam G., Moeroey T.;
RT   "Auxiliary splice factor U2AF26 and transcription factor Gfi1
RT   cooperate directly in regulating CD45 alternative splicing.";
RL   Nat. Immunol. 7:859-867(2006).
CC   -!- FUNCTION: Necessary for the splicing of pre-mRNA. Induces cardiac
CC       troponin-T (TNNT2) pre-mRNA exon inclusion in muscle. Regulates
CC       the TNNT2 exon 5 inclusion through competition with MBNL1. Binds
CC       preferentially to a single-stranded structure within the
CC       polypyrimidine tract of TNNT2 intron 4 during spliceosome
CC       assembly. Required for the export of mRNA out of the nucleus, even
CC       if the mRNA is encoded by an intron-less gene (By similarity).
CC   -!- SUBUNIT: Heterodimer with U2AF1. Binds unphosphorylated SF1.
CC       Interacts with SCAF11. Interacts with ZRSR2/U2AF1-RS2 (By
CC       similarity). Interacts with U2AF1L4.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- PTM: Lysyl-hydroxylation at Lys-15 and Lys-276 affects the mRNA
CC       splicing activity of the protein, leading to regulate some, but
CC       not all, alternative splicing events (By similarity).
CC   -!- SIMILARITY: Belongs to the splicing factor SR family.
CC   -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA45875.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; X64587; CAA45874.1; -; mRNA.
DR   EMBL; X64587; CAA45875.1; ALT_INIT; mRNA.
DR   EMBL; AK078496; BAC37309.1; -; mRNA.
DR   IPI; IPI00113746; -.
DR   PIR; S22646; S22646.
DR   UniGene; Mm.360389; -.
DR   ProteinModelPortal; P26369; -.
DR   SMR; P26369; 148-475.
DR   STRING; P26369; -.
DR   PhosphoSite; P26369; -.
DR   PRIDE; P26369; -.
DR   Ensembl; ENSMUST00000005041; ENSMUSP00000005041; ENSMUSG00000030435.
DR   UCSC; uc009ezu.1; mouse.
DR   MGI; MGI:98886; U2af2.
DR   eggNOG; roNOG08959; -.
DR   HOGENOM; HBG558924; -.
DR   HOVERGEN; HBG062169; -.
DR   InParanoid; P26369; -.
DR   OMA; MAFDGIN; -.
DR   OrthoDB; EOG4PRSQX; -.
DR   PMAP-CutDB; P26369; -.
DR   ArrayExpress; P26369; -.
DR   Bgee; P26369; -.
DR   Genevestigator; P26369; -.
DR   GermOnline; ENSMUSG00000030435; Mus musculus.
DR   GO; GO:0016607; C:nuclear speck; TAS:UniProtKB.
DR   GO; GO:0070742; F:C2H2 zinc finger domain binding; IPI:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IDA:UniProtKB.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR006529; U2AF_lg.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 3.
DR   Pfam; PF00076; RRM_1; 3.
DR   SMART; SM00360; RRM; 3.
DR   TIGRFAMs; TIGR01642; U2AF_lg; 1.
DR   PROSITE; PS50102; RRM; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Hydroxylation; mRNA processing; mRNA splicing; Nucleus;
KW   Phosphoprotein; Repeat; RNA-binding.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    475       Splicing factor U2AF 65 kDa subunit.
FT                                /FTId=PRO_0000081989.
FT   DOMAIN      149    231       RRM 1.
FT   DOMAIN      259    337       RRM 2.
FT   DOMAIN      385    466       RRM 3.
FT   COMPBIAS     27     62       Arg/Ser-rich (RS domain).
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES       2      2       Phosphoserine (By similarity).
FT   MOD_RES      15     15       5-hydroxylysine; by JMJD6 (By
FT                                similarity).
FT   MOD_RES      53     53       Phosphoserine (By similarity).
FT   MOD_RES      55     55       Phosphoserine (By similarity).
FT   MOD_RES      70     70       N6-acetyllysine (By similarity).
FT   MOD_RES      79     79       Phosphoserine (By similarity).
FT   MOD_RES     276    276       5-hydroxylysine; by JMJD6 (By
FT                                similarity).
FT   MOD_RES     462    462       N6-acetyllysine (By similarity).
SQ   SEQUENCE   475 AA;  53517 MW;  2D81375CD8FC7251 CRC64;
     MSDFDEFERQ LNENKQERDK ENRHRKRSHS RSRSRDRKRR SRSRDRRNRD QRSASRDRRR
     RSKPLTRGAK EEHGGLIRSP RHEKKKKVRK YWDVPPPGFE HITPMQYKAM QAAGQIPATA
     LLPTMTPDGL AVTPTPVPVV GSQMTRQARR LYVGNIPFGI TEEAMMDFFN AQMRLGGLTQ
     APGNPVLAVQ INQDKNFAFL EFRSVDETTQ AMAFDGIIFQ GQSLKIRRPH DYQPLPGMSE
     NPSVYVPGVV STVVPDSAHK LFIGGLPNYL NDDQVKELLT SFGPLKAFNL VKDSATGLSK
     GYAFCEYVDI NVTDQAIAGL NGMQLGDKKL LVQRASVGAK NATLVSLPST INQTPVTLQV
     PGLMSSQVQM GGHPTEVLCL MNMVLPEELL DDEEYEEIVE DVRDECSKYG LVKSIEIPRP
     VDGVEVPGCG KIFVEFTSVF DCQKAMQGLT GRKFANRVVV TKYCDPDSYH RRDFW
//
ID   DHE3_MOUSE              Reviewed;         558 AA.
AC   P26443; Q8C273;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   08-MAR-2011, entry version 106.
DE   RecName: Full=Glutamate dehydrogenase 1, mitochondrial;
DE            Short=GDH 1;
DE            EC=1.4.1.3;
DE   Flags: Precursor;
GN   Name=Glud1; Synonyms=Glud;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=91274358; PubMed=1711373; DOI=10.1016/0167-4781(91)90017-G;
RA   Tzimagiorgis G., Moschonas N.K.;
RT   "Molecular cloning, structure and expression analysis of a full-length
RT   mouse brain glutamate dehydrogenase cDNA.";
RL   Biochim. Biophys. Acta 1089:250-253(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 61-76; 108-123; 125-136; 152-183; 192-200;
RP   212-231; 275-318; 327-346; 353-363; 366-386; 400-420; 461-476;
RP   481-496; 504-516; 528-545 AND 549-558.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-503 AND LYS-527, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-135 AND TYR-512, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May be involved in learning and memory reactions by
CC       increasing the turnover of the excitatory neurotransmitter
CC       glutamate (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-glutamate + H(2)O + NAD(P)(+) = 2-
CC       oxoglutarate + NH(3) + NAD(P)H.
CC   -!- ENZYME REGULATION: Subject to allosteric regulation. Activated by
CC       ADP. Inhibited by GTP and ATP. ADP can occupy the NADH binding
CC       site and activate the enzyme (By similarity).
CC   -!- SUBUNIT: Homohexamer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- PTM: Acetylation of Lys-84 is observed in liver mitochondria from
CC       fasted mice but not from fed mice.
CC   -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X57024; CAA40341.1; -; mRNA.
DR   EMBL; AK089152; BAC40767.1; -; mRNA.
DR   EMBL; BC052724; AAH52724.1; -; mRNA.
DR   EMBL; BC057347; AAH57347.1; -; mRNA.
DR   IPI; IPI00114209; -.
DR   PIR; S16239; S16239.
DR   RefSeq; NP_032159.1; NM_008133.4.
DR   UniGene; Mm.10600; -.
DR   ProteinModelPortal; P26443; -.
DR   SMR; P26443; 63-558.
DR   STRING; P26443; -.
DR   PhosphoSite; P26443; -.
DR   SWISS-2DPAGE; P26443; -.
DR   REPRODUCTION-2DPAGE; P26443; -.
DR   UCD-2DPAGE; P26443; -.
DR   PRIDE; P26443; -.
DR   Ensembl; ENSMUST00000022322; ENSMUSP00000022322; ENSMUSG00000021794.
DR   GeneID; 14661; -.
DR   KEGG; mmu:14661; -.
DR   NMPDR; fig|10090.3.peg.28839; -.
DR   UCSC; uc007tas.1; mouse.
DR   CTD; 14661; -.
DR   MGI; MGI:95753; Glud1.
DR   eggNOG; roNOG05123; -.
DR   HOGENOM; HBG590661; -.
DR   HOVERGEN; HBG005479; -.
DR   InParanoid; P26443; -.
DR   OMA; SGLEYTM; -.
DR   OrthoDB; EOG4H72B7; -.
DR   PhylomeDB; P26443; -.
DR   BRENDA; 1.4.1.3; 244.
DR   NextBio; 286534; -.
DR   ArrayExpress; P26443; -.
DR   Bgee; P26443; -.
DR   Genevestigator; P26443; -.
DR   GermOnline; ENSMUSG00000021794; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; IGI:MGI.
DR   InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR   InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR   InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00208; ELFV_dehydrog; 1.
DR   Pfam; PF02812; ELFV_dehydrog_N; 1.
DR   PRINTS; PR00082; GLFDHDRGNASE.
DR   SMART; SM00839; ELFV_dehydrog; 1.
DR   PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Direct protein sequencing; GTP-binding;
KW   Mitochondrion; NADP; Nucleotide-binding; Oxidoreductase;
KW   Phosphoprotein; Transit peptide.
FT   TRANSIT       1     53       Mitochondrion.
FT   CHAIN        54    558       Glutamate dehydrogenase 1, mitochondrial.
FT                                /FTId=PRO_0000007212.
FT   NP_BIND     141    143       NAD (By similarity).
FT   ACT_SITE    183    183       By similarity.
FT   BINDING     147    147       Substrate (By similarity).
FT   BINDING     171    171       Substrate (By similarity).
FT   BINDING     176    176       NAD (By similarity).
FT   BINDING     252    252       NAD (By similarity).
FT   BINDING     266    266       GTP (By similarity).
FT   BINDING     270    270       GTP (By similarity).
FT   BINDING     319    319       GTP (By similarity).
FT   BINDING     322    322       GTP (By similarity).
FT   BINDING     438    438       Substrate (By similarity).
FT   BINDING     444    444       NAD (By similarity).
FT   BINDING     450    450       ADP (By similarity).
FT   BINDING     516    516       ADP (By similarity).
FT   MOD_RES      84     84       N6-acetyllysine.
FT   MOD_RES     128    128       Phosphoserine (By similarity).
FT   MOD_RES     135    135       Phosphotyrosine.
FT   MOD_RES     227    227       Phosphoserine.
FT   MOD_RES     410    410       Phosphothreonine (By similarity).
FT   MOD_RES     450    450       Phosphoserine.
FT   MOD_RES     480    480       N6-acetyllysine (By similarity).
FT   MOD_RES     503    503       N6-acetyllysine.
FT   MOD_RES     512    512       Phosphotyrosine.
FT   MOD_RES     527    527       N6-acetyllysine.
FT   CONFLICT    495    495       D -> G (in Ref. 2; BAC40767).
SQ   SEQUENCE   558 AA;  61337 MW;  92738AA5A133838A CRC64;
     MYRRLGEALL LSRAGPAALG SAAADSAALL GWARGQPSAA PQPGLTPVAR RHYSEAAADR
     EDDPNFFKMV EGFFDRGASI VEDKLVEDLK TRESEEQKRN RVRGILRIIK PCNHVLSLSF
     PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI RYSTDVSVDE VKALASLMTY KCAVVDVPFG
     GAKAGVKINP KNYTDNELEK ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY
     ASTIGHYDIN AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG
     DKTFVVQGFG NVGLHSMRYL HRFGAKCVGV GESDGSIWNP DGIDPKELED FKLQHGSILG
     FPKAKVYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI IAEGANGPTT PEADKIFLER
     NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS YGRLTFKYER DSNYHLLMSV QESLERKFGK
     HGGTIPVVPT AEFQDRISGA SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV
     NAIEKVFKVY NEAGVTFT
//
ID   MARCS_MOUSE             Reviewed;         309 AA.
AC   P26645;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 101.
DE   RecName: Full=Myristoylated alanine-rich C-kinase substrate;
DE            Short=MARCKS;
GN   Name=Marcks; Synonyms=Macs;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Macrophage;
RX   MEDLINE=91172836; PubMed=2006186; DOI=10.1073/pnas.88.6.2505;
RA   Seykora J.T., Ravetch J.V., Aderem A.;
RT   "Cloning and molecular characterization of the murine macrophage '68-
RT   kDa' protein kinase C substrate and its regulation by bacterial
RT   lipopolysaccharide.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:2505-2509(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Fibroblast;
RX   MEDLINE=91330872; PubMed=1868832;
RA   Brooks S.F., Herget T., Erusalimsky J.D., Rozengurt E.;
RT   "Protein kinase C activation potently down-regulates the expression of
RT   its major substrate, 80K, in Swiss 3T3 cells.";
RL   EMBO J. 10:2497-2505(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 131-145 AND 170-186, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=Swiss; TISSUE=Fibroblast;
RX   MEDLINE=90346162; PubMed=2384168; DOI=10.1016/0014-5793(90)81030-R;
RA   Brooks S.F., Erusalimsky J.D., Totty N.F., Rozengurt E.;
RT   "Purification and internal amino acid sequence of the 80 kDa protein
RT   kinase C substrate from Swiss 3T3 fibroblasts. Homology with
RT   substrates from brain.";
RL   FEBS Lett. 268:291-295(1990).
RN   [6]
RP   PROTEIN SEQUENCE OF 102-130, PHOSPHORYLATION AT SER-113, AND
RP   MUTAGENESIS OF SER-113.
RX   PubMed=8849678; DOI=10.1016/0014-5793(96)00991-X;
RA   Schoenwasser D.C., Palmer R.H., Herget T., Parker P.J.;
RT   "p42 MAPK phosphorylates 80 kDa MARCKS at Ser-113.";
RL   FEBS Lett. 395:1-5(1996).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 182-301.
RX   MEDLINE=93011168; PubMed=1396720;
RX   DOI=10.1111/j.1432-1033.1992.tb17255.x;
RA   Herget T., Brooks S.F., Broad S., Rozengurt E.;
RT   "Relationship between the major protein kinase C substrates acidic 80-
RT   kDa protein-kinase-C substrate (80K) and myristoylated alanine-rich C-
RT   kinase substrate (MARCKS). Members of a gene family or equivalent
RT   genes in different species.";
RL   Eur. J. Biochem. 209:7-14(1992).
RN   [8]
RP   PHOSPHORYLATION AT SER-152; SER-156 AND SER-163.
RX   PubMed=7588787; DOI=10.1111/j.1432-1033.1995.448_2.x;
RA   Herget T., Oehrlein S.A., Pappin D.J.C., Rozengurt E., Parker P.J.;
RT   "The myristoylated alanine-rich C-kinase substrate (MARCKS) is
RT   sequentially phosphorylated by conventional, novel and atypical
RT   isotypes of protein kinase C.";
RL   Eur. J. Biochem. 233:448-457(1995).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138 AND THR-143, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-113; SER-128;
RP   THR-143 AND SER-246, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-113 AND SER-163,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND THR-143, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND SER-171, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-143 AND SER-163, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: MARCKS is the most prominent cellular substrate for
CC       protein kinase C. This protein binds calmodulin, actin, and
CC       synapsin. MARCKS is a filamentous (F) actin cross-linking protein.
CC   -!- INTERACTION:
CC       P62158:CALM1 (xeno); NbExp=1; IntAct=EBI-911805, EBI-397435;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (Probable).
CC       Membrane; Lipid-anchor (By similarity).
CC   -!- TISSUE SPECIFICITY: Brain, spleen, less in kidney and heart, and
CC       very low levels in liver.
CC   -!- INDUCTION: By lipopolysaccharides (LPS).
CC   -!- PTM: Phosphorylation by PKC displaces MARCKS from the membrane. It
CC       also inhibits the F-actin cross-linking activity.
CC   -!- SIMILARITY: Belongs to the MARCKS family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M60474; AAA39491.1; -; mRNA.
DR   EMBL; BC046601; AAH46601.1; -; mRNA.
DR   IPI; IPI00229534; -.
DR   PIR; A39169; A39169.
DR   RefSeq; NP_032564.1; NM_008538.2.
DR   UniGene; Mm.480567; -.
DR   PDB; 1IWQ; X-ray; 2.00 A; B=148-166.
DR   PDBsum; 1IWQ; -.
DR   ProteinModelPortal; P26645; -.
DR   DisProt; DP00253; -.
DR   IntAct; P26645; 2.
DR   STRING; P26645; -.
DR   PhosphoSite; P26645; -.
DR   PRIDE; P26645; -.
DR   Ensembl; ENSMUST00000092584; ENSMUSP00000090245; ENSMUSG00000069662.
DR   GeneID; 17118; -.
DR   KEGG; mmu:17118; -.
DR   UCSC; uc007evg.1; mouse.
DR   CTD; 17118; -.
DR   MGI; MGI:96907; Marcks.
DR   eggNOG; roNOG17852; -.
DR   InParanoid; P26645; -.
DR   OMA; QPAGKEQ; -.
DR   NextBio; 291280; -.
DR   ArrayExpress; P26645; -.
DR   Bgee; P26645; -.
DR   Genevestigator; P26645; -.
DR   GermOnline; ENSMUSG00000069662; Mus musculus.
DR   GO; GO:0005938; C:cell cortex; IDA:MGI.
DR   GO; GO:0005813; C:centrosome; IDA:MGI.
DR   GO; GO:0042585; C:germinal vesicle; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005080; F:protein kinase C binding; IPI:BHF-UCL.
DR   InterPro; IPR002101; MARCKS.
DR   PANTHER; PTHR14353; MARCKS; 1.
DR   Pfam; PF02063; MARCKS; 1.
DR   PRINTS; PR00963; MARCKS.
DR   PROSITE; PS00826; MARCKS_1; 1.
DR   PROSITE; PS00827; MARCKS_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Calmodulin-binding; Cytoplasm;
KW   Cytoskeleton; Direct protein sequencing; Lipoprotein; Membrane;
KW   Myristate; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    309       Myristoylated alanine-rich C-kinase
FT                                substrate.
FT                                /FTId=PRO_0000157149.
FT   REGION      145    169       Calmodulin-binding (PSD).
FT   MOD_RES      26     26       Phosphoserine (By similarity).
FT   MOD_RES      27     27       Phosphoserine (By similarity).
FT   MOD_RES      29     29       Phosphoserine (By similarity).
FT   MOD_RES      46     46       Phosphoserine.
FT   MOD_RES      63     63       Phosphoserine (By similarity).
FT   MOD_RES     113    113       Phosphoserine; by MAPK.
FT   MOD_RES     124    124       Phosphoserine (By similarity).
FT   MOD_RES     125    125       Phosphoserine (By similarity).
FT   MOD_RES     127    127       Phosphoserine (By similarity).
FT   MOD_RES     128    128       Phosphoserine.
FT   MOD_RES     138    138       Phosphoserine.
FT   MOD_RES     140    140       Phosphoserine.
FT   MOD_RES     143    143       Phosphothreonine.
FT   MOD_RES     152    152       Phosphoserine; by PKC.
FT   MOD_RES     156    156       Phosphoserine; by PKC.
FT   MOD_RES     163    163       Phosphoserine; by PKC.
FT   MOD_RES     171    171       Phosphoserine.
FT   MOD_RES     246    246       Phosphoserine.
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
FT   MUTAGEN     113    113       S->A: Poorly phosphorylated.
FT   CONFLICT     96     98       AGA -> TGT (in Ref. 2; AA sequence).
FT   HELIX       157    162
SQ   SEQUENCE   309 AA;  29661 MW;  3BB1E392D74B5A98 CRC64;
     MGAQFSKTAA KGEATAERPG EAAVASSPSK ANGQENGHVK VNGDASPAAA EPGAKEELQA
     NGSAPAADKE EPASGSAATP AAAEKDEAAA ATEPGAGAAD KEAAEAEPAE PSSPAAEAEG
     ASASSTSSPK AEDGAAPSPS SETPKKKKKR FSFKKSFKLS GFSFKKSKKE SGEGAEAEGA
     TAEGAKDEAA AAAGGEGAAA PGEQAGGAGA EGAAGGEPRE AEAAEPEQPE QPEQPAAEEP
     QAEEQSEAAG EKAEEPAPGA TAGDASSAAG PEQEAPAATD EAAASAAPAA SPEPQPECSP
     EAPPAPTAE
//
ID   TWST1_MOUSE             Reviewed;         206 AA.
AC   P26687;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Twist-related protein 1;
DE   AltName: Full=M-twist;
GN   Name=Twist1; Synonyms=Twist;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=91122450; PubMed=1840517; DOI=10.1016/0012-1606(91)90086-I;
RA   Wolf C., Thisse C., Stoetzel C., Thisse B., Gerlinger P.,
RA   Perrin-Schmitt F.;
RT   "The M-twist gene of Mus is expressed in subsets of mesodermal cells
RT   and is closely related to the Xenopus X-twi and the Drosophila twist
RT   genes.";
RL   Dev. Biol. 143:363-373(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION.
RX   MEDLINE=98001585; PubMed=9343420;
RA   Hamamori Y., Wu H.Y., Sartorelli V., Kedes L.;
RT   "The basic domain of myogenic basic helix-loop-helix (bHLH) proteins
RT   is the novel target for direct inhibition by another bHLH protein,
RT   Twist.";
RL   Mol. Cell. Biol. 17:6563-6573(1997).
RN   [4]
RP   FUNCTION, AND INDUCTION.
RX   MEDLINE=22441800; PubMed=12553906; DOI=10.1016/S0092-8674(03)00002-3;
RA   Sosic D., Richardson J.A., Yu K., Ornitz D.M., Olson E.N.;
RT   "Twist regulates cytokine gene expression through a negative feedback
RT   loop that represses NF-kappaB activity.";
RL   Cell 112:169-180(2003).
RN   [5]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=16502419; DOI=10.1002/dvdy.20717;
RA   Connerney J., Andreeva V., Leshem Y., Muentener C., Mercado M.A.,
RA   Spicer D.B.;
RT   "Twist1 dimer selection regulates cranial suture patterning and
RT   fusion.";
RL   Dev. Dyn. 235:1345-1357(2006).
RN   [6]
RP   FUNCTION, SUBUNIT, AND MUTAGENESIS OF CYS-179; GLU-185; ARG-186;
RP   LEU-187; SER-188; PHE-191; SER-192 AND ARG-195.
RX   PubMed=17893140; DOI=10.1074/jbc.M707085200;
RA   Laursen K.B., Mielke E., Iannaccone P., Fuchtbauer E.M.;
RT   "Mechanism of transcriptional activation by the proto-oncogene
RT   Twist1.";
RL   J. Biol. Chem. 282:34623-34633(2007).
CC   -!- FUNCTION: Acts as a transcriptional regulator. Inhibits myogenesis
CC       by sequestrating E proteins, inhibiting trans-activation by MEF2,
CC       and inhibiting DNA-binding by MYOD1 through physical interaction.
CC       This interaction probably involves the basic domains of both
CC       proteins. Also represses expression of proinflammatory cytokines
CC       such as TNFA and IL1B. Regulates cranial suture patterning and
CC       fusion. Activates transcription as a heterodimer with E proteins.
CC       Regulates gene expression differentially, depending on dimer
CC       composition. Homodimers induce expression of FGFR2 and POSTN while
CC       heterodimers repress FGFR2 and POSTN expression and induce THBS1
CC       expression. Heterodimerization is also required for osteoblast
CC       differentiation.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another
CC       bHLH protein. Homodimer or heterodimer with E proteins such as
CC       TCF3. ID1 binds preferentially to TCF3 but does not interact
CC       efficiently with TWIST1 so ID1 levels control the amount of TCF3
CC       available to dimerize with TWIST1 and thus determine the type of
CC       dimer formed.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Subset of mesodermal cells.
CC   -!- INDUCTION: By TNF-alpha.
CC   -!- SIMILARITY: Contains 1 basic helix-loop-helix (bHLH) domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M63649; AAA40514.1; -; Genomic_DNA.
DR   EMBL; M63650; AAA40515.1; -; mRNA.
DR   EMBL; BC033434; AAH33434.1; -; mRNA.
DR   EMBL; BC083139; AAH83139.1; -; mRNA.
DR   IPI; IPI00115425; -.
DR   PIR; I53066; I53066.
DR   RefSeq; NP_035788.1; NM_011658.2.
DR   UniGene; Mm.3280; -.
DR   ProteinModelPortal; P26687; -.
DR   SMR; P26687; 113-169.
DR   STRING; P26687; -.
DR   PhosphoSite; P26687; -.
DR   PRIDE; P26687; -.
DR   Ensembl; ENSMUST00000049089; ENSMUSP00000040089; ENSMUSG00000035799.
DR   GeneID; 22160; -.
DR   KEGG; mmu:22160; -.
DR   UCSC; uc007niw.1; mouse.
DR   CTD; 22160; -.
DR   MGI; MGI:98872; Twist1.
DR   eggNOG; maNOG10879; -.
DR   GeneTree; ENSGT00590000082747; -.
DR   InParanoid; P26687; -.
DR   OMA; EEEPDRQ; -.
DR   OrthoDB; EOG434W7J; -.
DR   PhylomeDB; P26687; -.
DR   NextBio; 302090; -.
DR   PMAP-CutDB; P26687; -.
DR   ArrayExpress; P26687; -.
DR   Bgee; P26687; -.
DR   CleanEx; MM_TWIST1; -.
DR   Genevestigator; P26687; -.
DR   GermOnline; ENSMUSG00000035799; Mus musculus.
DR   GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR   GO; GO:0070888; F:E-box binding; IDA:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0030528; F:transcription regulator activity; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IMP:MGI.
DR   GO; GO:0060363; P:cranial suture morphogenesis; IMP:UniProtKB.
DR   GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IGI:MGI.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR   GO; GO:0035115; P:embryonic forelimb morphogenesis; IMP:MGI.
DR   GO; GO:0035137; P:hindlimb morphogenesis; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR   GO; GO:0044092; P:negative regulation of molecular function; IDA:MGI.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; IDA:MGI.
DR   GO; GO:0045843; P:negative regulation of striated muscle tissue development; IDA:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IGI:MGI.
DR   GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0001649; P:osteoblast differentiation; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   InterPro; IPR011598; HLH_DNA-bd.
DR   InterPro; IPR001092; HLH_DNA-bd_dom.
DR   InterPro; IPR015789; Twist.
DR   Gene3D; G3DSA:4.10.280.10; HLH_DNA_bd; 1.
DR   PANTHER; PTHR23349:SF6; Twist; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; HLH_basic; 1.
DR   PROSITE; PS50888; HLH; 1.
PE   1: Evidence at protein level;
KW   Activator; Developmental protein; Differentiation; DNA-binding;
KW   Myogenesis; Nucleus; Transcription; Transcription regulation.
FT   CHAIN         1    206       Twist-related protein 1.
FT                                /FTId=PRO_0000127488.
FT   DOMAIN      125    164       Helix-loop-helix motif.
FT   DNA_BIND    112    124       Basic motif.
FT   REGION      165    195       Sufficient for transactivation activity.
FT   COMPBIAS     80    102       Gly-rich.
FT   MUTAGEN     179    179       C->G: High transactivation activity.
FT   MUTAGEN     185    185       E->D,K,R: High transactivation activity.
FT   MUTAGEN     186    186       R->A,K: High transactivation activity.
FT   MUTAGEN     187    187       L->G: Low transactivation activity.
FT   MUTAGEN     188    188       S->A: High transactivation activity.
FT   MUTAGEN     191    191       F->A,G,P: Low transactivation activity.
FT   MUTAGEN     192    192       S->A: High transactivation activity.
FT   MUTAGEN     192    192       S->P: Intermediate transactivation
FT                                activity.
FT   MUTAGEN     195    195       R->E: Intermediate transactivation
FT                                activity.
FT   MUTAGEN     195    195       R->G: Low transactivation activity.
FT   CONFLICT     36     36       A -> R (in Ref. 1; AAA40515).
FT   CONFLICT     91     91       G -> P (in Ref. 1; AAA40515).
SQ   SEQUENCE   206 AA;  21198 MW;  618AD8E9BE87C555 CRC64;
     MMQDVSSSPV SPADDSLSNS EEEPDRQQPA SGKRGARKRR SSRRSAGGSA GPGGATGGGI
     GGGDEPGSPA QGKRGKKSAG GGGGGGAGGG GGGGGGSSSG GGSPQSYEEL QTQRVMANVR
     ERQRTQSLNE AFAALRKIIP TLPSDKLSKI QTLKLAARYI DFLYQVLQSD ELDSKMASCS
     YVAHERLSYA FSVWRMEGAW SMSASH
//
ID   FKB1A_MOUSE             Reviewed;         108 AA.
AC   P26883; Q545E9;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase FKBP1A;
DE            Short=PPIase FKBP1A;
DE            EC=5.2.1.8;
DE   AltName: Full=12 kDa FK506-binding protein;
DE            Short=12 kDa FKBP;
DE            Short=FKBP-12;
DE   AltName: Full=FK506-binding protein 1A;
DE            Short=FKBP-1A;
DE   AltName: Full=Immunophilin FKBP12;
DE   AltName: Full=Rotamase;
GN   Name=Fkbp1a; Synonyms=Fkbp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X CBA;
RX   MEDLINE=92112051; PubMed=1722474; DOI=10.1016/0378-1119(91)90617-K;
RA   Nelson P.A., Lippke J.A., Murcko M.A., Rosborough S.L., Peattie D.A.;
RT   "cDNA encoding murine FK506-binding protein (FKBP): nucleotide and
RT   deduced amino acid sequence.";
RL   Gene 109:255-258(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129/Sv;
RA   Shou W., Bao S., Mathews L.S., Matzuk M.M.;
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ILS, and ISS;
RX   MEDLINE=21363810; PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in modulation of ryanodine receptor
CC       isoform-1 (RYR-1), a component of the calcium release channel of
CC       skeletal muscle sarcoplasmic reticulum. There are four molecules
CC       of FKBP12 per skeletal muscle RYR. PPIases accelerate the folding
CC       of proteins. It catalyzes the cis-trans isomerization of proline
CC       imidic peptide bonds in oligopeptides (By similarity).
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- ENZYME REGULATION: Inhibited by both FK506 and rapamycin.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family. FKBP1
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 PPIase FKBP-type domain.
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DR   EMBL; X60203; CAA42762.1; -; mRNA.
DR   EMBL; U65100; AAB17554.1; -; Genomic_DNA.
DR   EMBL; U65098; AAB17554.1; JOINED; Genomic_DNA.
DR   EMBL; U65099; AAB17554.1; JOINED; Genomic_DNA.
DR   EMBL; AF483488; AAL90762.1; -; mRNA.
DR   EMBL; AF483489; AAL90763.1; -; mRNA.
DR   EMBL; AK002777; BAB22351.1; -; mRNA.
DR   EMBL; AK010693; BAB27125.1; -; mRNA.
DR   EMBL; AK019362; BAB31680.1; -; mRNA.
DR   EMBL; AK154751; BAE32804.1; -; mRNA.
DR   EMBL; AK168333; BAE40271.1; -; mRNA.
DR   EMBL; AK169186; BAE40963.1; -; mRNA.
DR   EMBL; AK169242; BAE41008.1; -; mRNA.
DR   EMBL; BC004671; AAH04671.1; -; mRNA.
DR   IPI; IPI00266899; -.
DR   PIR; JH0528; JH0528.
DR   RefSeq; NP_032045.1; NM_008019.2.
DR   UniGene; Mm.278458; -.
DR   UniGene; Mm.381214; -.
DR   ProteinModelPortal; P26883; -.
DR   SMR; P26883; 2-108.
DR   DIP; DIP-29707N; -.
DR   STRING; P26883; -.
DR   PhosphoSite; P26883; -.
DR   PRIDE; P26883; -.
DR   Ensembl; ENSMUST00000044011; ENSMUSP00000037206; ENSMUSG00000032966.
DR   GeneID; 14225; -.
DR   KEGG; mmu:14225; -.
DR   UCSC; uc008ndy.1; mouse.
DR   CTD; 14225; -.
DR   MGI; MGI:95541; Fkbp1a.
DR   HOVERGEN; HBG051623; -.
DR   OMA; MTADYAY; -.
DR   OrthoDB; EOG42NJ1X; -.
DR   PhylomeDB; P26883; -.
DR   BRENDA; 5.2.1.8; 244.
DR   NextBio; 285479; -.
DR   ArrayExpress; P26883; -.
DR   Bgee; P26883; -.
DR   CleanEx; MM_FKBP1A; -.
DR   Genevestigator; P26883; -.
DR   GermOnline; ENSMUSG00000032966; Mus musculus.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:MGI.
DR   GO; GO:0005528; F:FK506 binding; IDA:MGI.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IMP:MGI.
DR   GO; GO:0060347; P:heart trabecula formation; IMP:BHF-UCL.
DR   GO; GO:0006936; P:muscle contraction; IMP:MGI.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:MGI.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR   GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IMP:BHF-UCL.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:MGI.
DR   GO; GO:0031000; P:response to caffeine; IMP:MGI.
DR   GO; GO:0042098; P:T cell proliferation; IMP:MGI.
DR   GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   Pfam; PF00254; FKBP_C; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Isomerase; Phosphoprotein; Rotamase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    108       Peptidyl-prolyl cis-trans isomerase
FT                                FKBP1A.
FT                                /FTId=PRO_0000075290.
FT   DOMAIN       20    108       PPIase FKBP-type.
FT   MOD_RES       9      9       Phosphoserine (By similarity).
FT   MOD_RES      53     53       N6-acetyllysine (By similarity).
SQ   SEQUENCE   108 AA;  11923 MW;  8C265ED5803F6987 CRC64;
     MGVQVETISP GDGRTFPKRG QTCVVHYTGM LEDGKKFDSS RDRNKPFKFT LGKQEVIRGW
     EEGVAQMSVG QRAKLIISSD YAYGATGHPG IIPPHATLVF DVELLKLE
//
ID   MAP4_MOUSE              Reviewed;        1125 AA.
AC   P27546; Q05BJ2; Q3UIS2; Q3UUH5; Q3UY36; Q7TPC6; Q7TPD4; Q80YQ5;
AC   Q8CFP5;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 3.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Microtubule-associated protein 4;
DE            Short=MAP-4;
GN   Name=Map4; Synonyms=Mtap4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=92042100; PubMed=1718985;
RA   West R.R., Tenbarge K.M., Olmsted J.B.;
RT   "A model for microtubule-associated protein 4 structure. Domains
RT   defined by comparisons of human, mouse, and bovine sequences.";
RL   J. Biol. Chem. 266:21886-21896(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=C57BL/6J; TISSUE=Heart, Hypothalamus, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC   STRAIN=C3H/He, and C57BL/6; TISSUE=Brain, Eye, and Osteoblast;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254; THR-260; THR-511;
RP   SER-517; SER-519 AND SER-617, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517; SER-598; THR-784
RP   AND THR-847, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254; THR-503; SER-506;
RP   SER-517 AND SER-785, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-630, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1046, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475 AND SER-1046, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475 AND SER-667, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Non-neuronal microtubule-associated protein. Promotes
CC       microtubule assembly.
CC   -!- SUBUNIT: Interacts with SEPT2; this interaction impedes tubulin-
CC       binding (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=P27546-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P27546-2; Sequence=VSP_026097;
CC       Name=3;
CC         IsoId=P27546-3; Sequence=VSP_026095, VSP_026097;
CC       Name=4;
CC         IsoId=P27546-4; Sequence=VSP_026089, VSP_026090, VSP_026091,
CC                                  VSP_026092, VSP_026093, VSP_026094,
CC                                  VSP_026095, VSP_026096, VSP_026097;
CC         Note=Phosphorylated on Ser-333 and Ser-334 (By similarity).
CC         Ref.2 (BAE23650/BAE22377) sequences are in conflict in position:
CC         435:K->E;
CC   -!- TISSUE SPECIFICITY: Testis, striated and cardiac muscle.
CC   -!- PTM: Phosphorylation on Ser-760 negatively regulates MAP4 activity
CC       to promote microtubule assembly. Isoform 4 is phosphorylated on
CC       Ser-333 and Ser-334 (By similarity). Phosphorylated upon DNA
CC       damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Contains 4 Tau/MAP repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH42645.1; Type=Erroneous initiation;
CC       Sequence=BAE27434.1; Type=Erroneous initiation;
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DR   EMBL; M72414; AAA16372.1; -; mRNA.
DR   EMBL; AK134996; BAE22377.1; -; mRNA.
DR   EMBL; AK138416; BAE23650.1; -; mRNA.
DR   EMBL; AK146790; BAE27434.1; ALT_INIT; mRNA.
DR   EMBL; BC042645; AAH42645.1; ALT_INIT; mRNA.
DR   EMBL; BC044654; AAH44654.1; -; mRNA.
DR   EMBL; BC050893; AAH50893.1; -; mRNA.
DR   EMBL; BC055332; AAH55332.1; -; mRNA.
DR   EMBL; BC055364; AAH55364.1; -; mRNA.
DR   IPI; IPI00406741; -.
DR   IPI; IPI00408119; -.
DR   IPI; IPI00473748; -.
DR   IPI; IPI00848818; -.
DR   PIR; B41206; B41206.
DR   RefSeq; NP_032659.2; NM_008633.3.
DR   UniGene; Mm.217318; -.
DR   UniGene; Mm.443428; -.
DR   MINT; MINT-1861472; -.
DR   STRING; P27546; -.
DR   PhosphoSite; P27546; -.
DR   PRIDE; P27546; -.
DR   Ensembl; ENSMUST00000035055; ENSMUSP00000035055; ENSMUSG00000032479.
DR   Ensembl; ENSMUST00000065171; ENSMUSP00000069933; ENSMUSG00000032479.
DR   Ensembl; ENSMUST00000072772; ENSMUSP00000072551; ENSMUSG00000032479.
DR   GeneID; 17758; -.
DR   KEGG; mmu:17758; -.
DR   CTD; 17758; -.
DR   MGI; MGI:97178; Mtap4.
DR   eggNOG; roNOG08235; -.
DR   GeneTree; ENSGT00530000063491; -.
DR   HOVERGEN; HBG006323; -.
DR   InParanoid; P27546; -.
DR   OMA; EVAPAKD; -.
DR   OrthoDB; EOG4X6C9T; -.
DR   PhylomeDB; P27546; -.
DR   NextBio; 292437; -.
DR   ArrayExpress; P27546; -.
DR   Bgee; P27546; -.
DR   CleanEx; MM_MTAP4; -.
DR   Genevestigator; P27546; -.
DR   GermOnline; ENSMUSG00000032479; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:InterPro.
DR   InterPro; IPR001084; Tau_tubulin-bd.
DR   Pfam; PF00418; Tubulin-binding; 4.
DR   PROSITE; PS00229; TAU_MAP_1; 4.
DR   PROSITE; PS51491; TAU_MAP_2; 4.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton;
KW   Microtubule; Phosphoprotein; Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1125       Microtubule-associated protein 4.
FT                                /FTId=PRO_0000072752.
FT   REPEAT      896    926       Tau/MAP 1.
FT   REPEAT      965    995       Tau/MAP 2.
FT   REPEAT      996   1026       Tau/MAP 3.
FT   REPEAT     1027   1058       Tau/MAP 4.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      60     60       Phosphoserine (By similarity).
FT   MOD_RES      96     96       Phosphothreonine (By similarity).
FT   MOD_RES      99     99       Phosphoserine (By similarity).
FT   MOD_RES     201    201       Phosphoserine (By similarity).
FT   MOD_RES     206    206       Phosphoserine (By similarity).
FT   MOD_RES     254    254       Phosphoserine.
FT   MOD_RES     260    260       Phosphothreonine.
FT   MOD_RES     277    277       Phosphothreonine (By similarity).
FT   MOD_RES     349    349       Phosphothreonine (By similarity).
FT   MOD_RES     452    452       Phosphothreonine (By similarity).
FT   MOD_RES     475    475       Phosphoserine.
FT   MOD_RES     494    494       Phosphothreonine (By similarity).
FT   MOD_RES     503    503       Phosphothreonine.
FT   MOD_RES     506    506       Phosphoserine.
FT   MOD_RES     511    511       Phosphothreonine.
FT   MOD_RES     517    517       Phosphoserine.
FT   MOD_RES     519    519       Phosphoserine.
FT   MOD_RES     583    583       Phosphoserine (By similarity).
FT   MOD_RES     598    598       Phosphoserine.
FT   MOD_RES     617    617       Phosphoserine.
FT   MOD_RES     630    630       Phosphoserine.
FT   MOD_RES     667    667       Phosphoserine.
FT   MOD_RES     713    713       Phosphoserine (By similarity).
FT   MOD_RES     716    716       Phosphoserine (By similarity).
FT   MOD_RES     737    737       Phosphoserine (By similarity).
FT   MOD_RES     760    760       Phosphoserine (By similarity).
FT   MOD_RES     766    766       Phosphoserine (By similarity).
FT   MOD_RES     784    784       Phosphothreonine.
FT   MOD_RES     785    785       Phosphoserine.
FT   MOD_RES     798    798       Phosphoserine (By similarity).
FT   MOD_RES     801    801       Phosphothreonine (By similarity).
FT   MOD_RES     847    847       Phosphothreonine.
FT   MOD_RES     872    872       Phosphoserine (By similarity).
FT   MOD_RES     888    888       Phosphoserine (By similarity).
FT   MOD_RES     898    898       Phosphothreonine (By similarity).
FT   MOD_RES     901    901       Phosphoserine (By similarity).
FT   MOD_RES     914    914       Phosphoserine (By similarity).
FT   MOD_RES     973    973       Phosphoserine (By similarity).
FT   MOD_RES     974    974       Phosphotyrosine (By similarity).
FT   MOD_RES    1009   1009       Phosphoserine (By similarity).
FT   MOD_RES    1010   1010       Phosphoserine (By similarity).
FT   MOD_RES    1014   1014       Phosphoserine (By similarity).
FT   MOD_RES    1046   1046       Phosphoserine.
FT   MOD_RES    1124   1124       Phosphoserine (By similarity).
FT   VAR_SEQ       1     26       MADLSLVDALTEPPPEIEGEIKRDFM -> MSLPEKQPAAL
FT                                T (in isoform 4).
FT                                /FTId=VSP_026089.
FT   VAR_SEQ      30    259       EAEPYDDIVGETVEKTEFIPLLDGDEKTGNSESKKKPCLDT
FT                                SQVEGIPSSKPTLLANGDHGMEGNNTAGSPTDFLEERVDYP
FT                                DYQSSQNWPEDASFCFQPQQVLDTDQAEPFNEHRDDGLADL
FT                                LFVSSGPTNASAFTERDNPSEDSYGMLPCDSFASTAVVSQE
FT                                WSVGAPNSPCSESCVSPEVTIETLQPATELSKAAEVESVKE
FT                                QLPAKALETMAEQTTDVVHSPSTDT -> AAEDEQLSKGNP
FT                                PECGMDSRKEIGQDGFEWQRTEGKLNEIGLNVSMDGQLKDR
FT                                LVKNSSFLEQNKLGFFEGKLDKELSIEKPNKAYQETSGHLE
FT                                SGYVISGTCQPSEGNLVHQKAAEFHPGLTEGKDKAATVQGK
FT                                VAGKSGLEIKSQPDLNFPGAADTLTQHGEEQETSAWNANFY
FT                                SVTQSPQAA (in isoform 4).
FT                                /FTId=VSP_026090.
FT   VAR_SEQ     263    419       PDTEAALAKDIEEITKPDVILANVTQPSTESDMFLAQDMEL
FT                                LTGTEAAHANNIILPTEPDESSTKDVAPPMEEEIVPGNDTT
FT                                SPKETETTLPIKMDLAPPEDVLLTKETELAPAKGMVSLSEI
FT                                EEALAKNDESSAEIPVAQETVVSETEVVLATEVV -> KEK
FT                                NGLVSSCSVTGVMSDNSGQLNNKSPLLVAITHPDPTSEHLP
FT                                TTSPPITMVEFTQENLNAGQDKELEKLRSSEEGPMLDQVPQ
FT                                QKKAIRRALSECYHLSVPPAVNLVDKYPELPAREE (in
FT                                isoform 4).
FT                                /FTId=VSP_026091.
FT   VAR_SEQ     424    531       PITTLTKDVTLPLEAERPLVTDMTPSLETEMTLGKETAPPT
FT                                ETNLGMAKDMSPLPESEVTLGKDVVILPETKVAEFNNVTPL
FT                                SEEEVTSVKDMSPSAETEAPLAKNAD -> LLPPTSSPMPS
FT                                PMPRKLGVPAMRRSMTVAEDQSASCRLSAGELASLSASQVP
FT                                TALTFEEPVAKEREEQIHFSNDSNSSGKKELGIAGLY (in
FT                                isoform 4).
FT                                /FTId=VSP_026092.
FT   VAR_SEQ     535    625       GTELIVDNSMAPASDLALPLETKVATVPIKDKGTVQTEEKP
FT                                REDSQLASMQHKGQSTVPPCTASPEPVKAAEQMSTLPIDAP
FT                                SPLENLEQK -> KLEQIPEGSHKGKGQKNTGETRVDSCPF
FT                                ICLGGEKQLMALAGKKEIEVTATQSIPSLLLE (in
FT                                isoform 4).
FT                                /FTId=VSP_026093.
FT   VAR_SEQ     629    637       GSQPSEPCS -> RD (in isoform 4).
FT                                /FTId=VSP_026094.
FT   VAR_SEQ     927    964       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_026095.
FT   VAR_SEQ     965    995       Missing (in isoform 4).
FT                                /FTId=VSP_026096.
FT   VAR_SEQ    1124   1125       SI -> N (in isoform 2, isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_026097.
FT   CONFLICT    225    225       K -> E (in Ref. 3; AAH55364).
FT   CONFLICT    252    252       V -> A (in Ref. 3; AAH55364).
FT   CONFLICT    394    395       ES -> VR (in Ref. 1; AAA16372).
FT   CONFLICT    416    416       T -> I (in Ref. 3; AAH55332).
FT   CONFLICT    955    955       A -> V (in Ref. 3; AAH55364).
FT   CONFLICT    982    982       G -> V (in Ref. 1; AAA16372).
FT   CONFLICT    993    993       G -> C (in Ref. 1; AAA16372).
FT   CONFLICT   1053   1053       L -> F (in Ref. 1; AAA16372).
FT   CONFLICT   1060   1060       K -> KV (in Ref. 3; AAH44654/AAH55364).
FT   CONFLICT   1089   1089       A -> R (in Ref. 1; AAA16372).
SQ   SEQUENCE   1125 AA;  117429 MW;  E948B7F1F5B903E9 CRC64;
     MADLSLVDAL TEPPPEIEGE IKRDFMAALE AEPYDDIVGE TVEKTEFIPL LDGDEKTGNS
     ESKKKPCLDT SQVEGIPSSK PTLLANGDHG MEGNNTAGSP TDFLEERVDY PDYQSSQNWP
     EDASFCFQPQ QVLDTDQAEP FNEHRDDGLA DLLFVSSGPT NASAFTERDN PSEDSYGMLP
     CDSFASTAVV SQEWSVGAPN SPCSESCVSP EVTIETLQPA TELSKAAEVE SVKEQLPAKA
     LETMAEQTTD VVHSPSTDTT PGPDTEAALA KDIEEITKPD VILANVTQPS TESDMFLAQD
     MELLTGTEAA HANNIILPTE PDESSTKDVA PPMEEEIVPG NDTTSPKETE TTLPIKMDLA
     PPEDVLLTKE TELAPAKGMV SLSEIEEALA KNDESSAEIP VAQETVVSET EVVLATEVVL
     PSDPITTLTK DVTLPLEAER PLVTDMTPSL ETEMTLGKET APPTETNLGM AKDMSPLPES
     EVTLGKDVVI LPETKVAEFN NVTPLSEEEV TSVKDMSPSA ETEAPLAKNA DLHSGTELIV
     DNSMAPASDL ALPLETKVAT VPIKDKGTVQ TEEKPREDSQ LASMQHKGQS TVPPCTASPE
     PVKAAEQMST LPIDAPSPLE NLEQKETPGS QPSEPCSGVS RQEEAKAAVG VTGNDITTPP
     NKEPPPSPEK KAKPLATTQP AKTSTSKAKT QPTSLPKQPA PTTSGGLNKK PMSLASGSVP
     AAPHKRPAAA TATARPSTLP ARDVKPKPIT EAKVAEKRTS PSKPSSAPAL KPGPKTTPTV
     SKATSPSTLV STGPSSRSPA TTLPKRPTSI KTEGKPADVK RMTAKSASAD LSRSKTTSAS
     SVKRNTTPTG AAPPAGMTST RVKPMSAPSR SSGALSVDKK PTSTKPSSSA PRVSRLATTV
     SAPDLKSVRS KVGSTENIKH QPGGGRAKVE KKTEAATTAG KPEPNAVTKA AGSIASAQKP
     PAGKVQIVSK KVSYSHIQSK CGSKDNIKHV PGGGNVQIQN KKVDISKVSS KCGSKANIKH
     KPGGGDVKIE SQKLNFKEKA QAKVGSLDNV GHLPAGGAVK TEGGGSEALP CPGPPAGEEP
     VIPEAAPDAG APTSASGLSG HTTLSGGGDQ REPQTLDSQI QETSI
//
ID   RGRF1_MOUSE             Reviewed;        1262 AA.
AC   P27671;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   08-MAR-2011, entry version 108.
DE   RecName: Full=Ras-specific guanine nucleotide-releasing factor 1;
DE            Short=Ras-GRF1;
DE   AltName: Full=CDC25Mm;
DE   AltName: Full=Guanine nucleotide-releasing protein;
DE            Short=GNRP;
DE   AltName: Full=Ras-specific nucleotide exchange factor CDC25;
GN   Name=Rasgrf1; Synonyms=Cdc25, Grf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=93010996; PubMed=1396590;
RA   Cen H., Lowy D.D.;
RT   "Isolation of multiple mouse cDNAs with coding homology to
RT   Saccharomyces cerevisiae CDC25: identification of a region related to
RT   Bcr, Vav, Dbl and CDC24.";
RL   EMBO J. 11:4007-4015(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 791-1262.
RC   STRAIN=Swiss; TISSUE=Brain;
RX   MEDLINE=92289680; PubMed=1376246;
RA   Martegani E., Vanoni M., Zippel R., Coccetti P., Brambilla R.,
RA   Ferrari C., Sturani E.P., Alberghina L.;
RT   "Cloning by functional complementation of a mouse cDNA encoding a
RT   homologue of CDC25, a Saccharomyces cerevisiae RAS activator.";
RL   EMBO J. 11:2151-2157(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1031-1226.
RX   MEDLINE=92357779; PubMed=1379731; DOI=10.1073/pnas.89.15.7100;
RA   Wei W., Mosteller R.D., Sanyal P., Gonzales E., McKinney D.,
RA   Dasgupta C., Li P., Liu B.-X., Broek D.;
RT   "Identification of a mammalian gene structurally and functionally
RT   related to the CDC25 gene of Saccharomyces cerevisiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:7100-7104(1992).
RN   [4]
RP   FUNCTION, OLIGOMERIZATION, INTERACTION WITH RASGRF2, AND MUTAGENESIS
RP   OF LEU-263 AND 394-LEU--LEU-400.
RX   MEDLINE=99303753; PubMed=10373510;
RA   Anborgh P.H., Qian X., Papageorge A.G., Vass W.C., DeClue J.E.,
RA   Lowy D.R.;
RT   "Ras-specific exchange factor GRF: oligomerization through its Dbl
RT   homology domain and calcium-dependent activation of Raf.";
RL   Mol. Cell. Biol. 19:4611-4622(1999).
RN   [5]
RP   UBIQUITINATION, AND INTERACTION WITH USP8.
RX   PubMed=11500497; DOI=10.1074/jbc.M103454200;
RA   Gnesutta N., Ceriani M., Innocenti M., Mauri I., Zippel R.,
RA   Sturani E., Borgonovo B., Berruti G., Martegani E.;
RT   "Cloning and characterization of mouse UBPy, a deubiquitinating enzyme
RT   that interacts with the ras guanine nucleotide exchange factor
RT   CDC25(Mm)/Ras-GRF1.";
RL   J. Biol. Chem. 276:39448-39454(2001).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Promotes the exchange of Ras-bound GDP by GTP.
CC   -!- SUBUNIT: Homooligomer and heterooligomer with RASGRF2. Interacts
CC       with USP8, thereby regulating its stability.
CC   -!- TISSUE SPECIFICITY: Brain.
CC   -!- DOMAIN: The DH (DBL-homology) domain mediates interaction with
CC       RASGRF2.
CC   -!- PTM: Ubiquitinated.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 IQ domain.
CC   -!- SIMILARITY: Contains 1 N-terminal Ras-GEF domain.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -!- SIMILARITY: Contains 1 Ras-GEF domain.
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DR   EMBL; L20899; AAA02741.1; -; mRNA.
DR   EMBL; X59868; CAA42525.1; -; mRNA.
DR   IPI; IPI00118835; -.
DR   PIR; S28407; S28407.
DR   RefSeq; NP_035375.1; NM_011245.2.
DR   UniGene; Mm.44561; -.
DR   PDB; 2IJE; X-ray; 2.20 A; S=1028-1262.
DR   PDBsum; 2IJE; -.
DR   ProteinModelPortal; P27671; -.
DR   SMR; P27671; 23-129, 243-441, 565-591, 1028-1259.
DR   DIP; DIP-41194N; -.
DR   IntAct; P27671; 1.
DR   MINT; MINT-207405; -.
DR   STRING; P27671; -.
DR   PhosphoSite; P27671; -.
DR   PRIDE; P27671; -.
DR   Ensembl; ENSMUST00000034912; ENSMUSP00000034912; ENSMUSG00000032356.
DR   GeneID; 19417; -.
DR   KEGG; mmu:19417; -.
DR   UCSC; uc009qzt.1; mouse.
DR   CTD; 19417; -.
DR   MGI; MGI:99694; Rasgrf1.
DR   HOGENOM; HBG443647; -.
DR   HOVERGEN; HBG005208; -.
DR   InParanoid; P27671; -.
DR   OMA; SMYSAMS; -.
DR   OrthoDB; EOG49KFPQ; -.
DR   PhylomeDB; P27671; -.
DR   NextBio; 296553; -.
DR   ArrayExpress; P27671; -.
DR   Bgee; P27671; -.
DR   Genevestigator; P27671; -.
DR   GermOnline; ENSMUSG00000032356; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:HGNC.
DR   GO; GO:0030426; C:growth cone; IDA:HGNC.
DR   GO; GO:0035254; F:glutamate receptor binding; IPI:MGI.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0032863; P:activation of Rac GTPase activity; IDA:HGNC.
DR   GO; GO:0008283; P:cell proliferation; IMP:MGI.
DR   GO; GO:0031175; P:neuron projection development; IDA:HGNC.
DR   GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:MGI.
DR   GO; GO:0035020; P:regulation of Rac protein signal transduction; IDA:HGNC.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR   InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR   InterPro; IPR008937; Ras_GEF.
DR   InterPro; IPR001895; RasGRF_CDC25.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Gene3D; G3DSA:1.10.840.10; RasGRF_CDC25; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   PANTHER; PTHR23113; Ras_GEF; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00015; IQ; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00229; RasGEFN; 2.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS00720; RASGEF; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50212; RASGEF_NTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Guanine-nucleotide releasing factor; Phosphoprotein;
KW   Repeat; Ubl conjugation.
FT   CHAIN         1   1262       Ras-specific guanine nucleotide-releasing
FT                                factor 1.
FT                                /FTId=PRO_0000068881.
FT   DOMAIN       22    130       PH 1.
FT   DOMAIN      208    233       IQ.
FT   DOMAIN      244    430       DH.
FT   DOMAIN      460    588       PH 2.
FT   DOMAIN      635    749       N-terminal Ras-GEF.
FT   DOMAIN     1027   1259       Ras-GEF.
FT   MOD_RES     727    727       Phosphoserine.
FT   MUTAGEN     263    263       L->Q: Loss of function and
FT                                oligomerization.
FT   MUTAGEN     394    400       LTLHELL->IIIRDII: Partial loss of
FT                                function. No effect on oligomerization.
FT   CONFLICT   1033   1033       E -> D (in Ref. 3).
FT   HELIX      1028   1044
FT   HELIX      1048   1057
FT   HELIX      1061   1064
FT   HELIX      1066   1087
FT   HELIX      1092   1111
FT   HELIX      1115   1125
FT   HELIX      1128   1131
FT   HELIX      1134   1138
FT   HELIX      1142   1154
FT   HELIX      1158   1169
FT   HELIX      1179   1192
FT   HELIX      1204   1222
FT   HELIX      1231   1238
FT   HELIX      1246   1256
SQ   SEQUENCE   1262 AA;  144102 MW;  38BFE68F7C228DC8 CRC64;
     MQKAIRLNDG HVVTLGLLAQ KDGTRKGYLS KRSADNPKWQ TKWFALLQNL LFYFESDSSP
     RPSGLYLLEG SICKRAPSPK RGTSSKESGE KQQHYFTVNF SNDSQKTLEL RTEDAKDCDE
     WVAAIARASY KILATEHEAL MQKYLHLLQV VETEKTVAKQ LRQQLEDGEV EIERLKTEVT
     ITNLIKDNDR IQSSNKAGSA DDEDSDIKKI KKVQSFLRGW LCRRKWKNII QDYIRSPHAD
     SMRKRNQVVF SMLEAEAEYV QQLHILVNNF LRPLRMAASS KKPPITHDDV SSIFLNSETI
     MFLHQIFYQG LKARISSWPT LVLADLFDIL LPMLNIYQEF VRNHQYSLQI LAHCKQNRDF
     DKLLKQYEAK PDCEERTLET FLTYPMFQIP RYILTLHELL AHTPHEHVER NSLDYAKSKL
     EELSRIMHDE VSETENIRKN LAIERMITEG CEILLDTSQT FVRQGSLMQM SLSEKSKSSR
     GRLGSLSTKK EGERQCFLFS KHLIICTRGS GGKLHLTKNG VISLIDCTLL DEPENLDDEA
     KGAGPEIEHL EFKIGVEPKD SLPFTVILVA STRQEKAAWT SDIIQCVDNI RCNGLMMNAF
     EENSKVTVPQ MIKSDASLYC DDVDIRFSKT MNSCKVLQIR YASVERLLER LTDLRFLSID
     FLNTFLHSYR VFTNAMVVLD KLINIYRKPM SAIPARSLEL LFSSSHNAKL LYGDAPKSPR
     ASRKFSSPPP LAIGTSSPSR RRKLSLNIPI ITGGKALELA SLGCSSDSYA NIHSPISPFG
     KTTLDTGKLC MASSLPKTPE EIDVPATIPE KPGELSASRK HSSDVLKEES EDDQNHSDED
     NTEVSPVKSP PTPKSFLNRT ITEFPFFNYN NGILMTTCRD LVDNNRSTLS ATSAFAIATA
     GANEGPSNKE VFRRMSLANT GFSSDQRNID KEFVIRRAAT NRVLNVLRHW VTKHTQDFDT
     DDTLKYRVIC FLEEVMHDPD LLTQERKAAA NIIRTLTLEE TTEQHSMLEE VILMTEGVKT
     EPFENHPALE IAEQLTLLDH LVFKSIPYEE FFGQGWMKAE KYERTPYIMK TTKHFNHVSN
     FIASEIIRNE DISARASAIE KWVAVADICR CLHNYNAVLE ITSSINRSAI FRLKKTWLKV
     SKQTKSLLDK LQKLVSSDGR FKNLRESLRN CDPPCVPYLG MYLTDLVFIE EGTPNYTEDG
     LVNFSKMRMI SHIIREIRQF QQTTYKIDPQ PKVIQYLLDE SFMLDEESLY ESSLLIEPKL
     PT
//
ID   BRAF_MOUSE              Reviewed;         804 AA.
AC   P28028; Q3USE9;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 107.
DE   RecName: Full=Serine/threonine-protein kinase B-raf;
DE            EC=2.7.11.1;
DE   AltName: Full=Proto-oncogene B-Raf;
GN   Name=Braf; Synonyms=B-raf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 476-804 (ISOFORM 2).
RX   MEDLINE=91271351; PubMed=2052597; DOI=10.1073/pnas.88.12.5167;
RA   Miki T., Fleming T.P., Crescenzi M., Molloy C.J., Blam S.B.,
RA   Reynolds S.H., Aaronson S.A.;
RT   "Development of a highly efficient expression cDNA cloning system:
RT   application to oncogene isolation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:5167-5171(1991).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Involved in the transduction of mitogenic signals from
CC       the cell membrane to the nucleus. May play a role in the
CC       postsynaptic responses of hippocampal neuron (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit (Potential).
CC   -!- SUBUNIT: Interacts with RIT1 (By similarity).
CC   -!- INTERACTION:
CC       Q99N57:Raf1; NbExp=1; IntAct=EBI-2584830, EBI-397757;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P28028-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P28028-2; Sequence=VSP_022169, VSP_022170;
CC         Note=No experimental confirmation available;
CC   -!- DISEASE: Note=Participates in a chromosomal translocation that
CC       produces a Tif1a-BRAF (T18) oncogene originally isolated from a
CC       furfural-induced hepatoma.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. RAF subfamily.
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 RBD (Ras-binding) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA37320.1; Type=Erroneous initiation;
CC       Sequence=AAA37320.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA;
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DR   EMBL; AK140431; BAE24384.1; -; mRNA.
DR   EMBL; M64429; AAA37320.1; ALT_INIT; mRNA.
DR   IPI; IPI00230719; -.
DR   IPI; IPI00816967; -.
DR   PIR; A40951; TVMSBF.
DR   RefSeq; NP_647455.3; NM_139294.5.
DR   UniGene; Mm.245513; -.
DR   UniGene; Mm.480758; -.
DR   ProteinModelPortal; P28028; -.
DR   SMR; P28028; 137-267, 485-757.
DR   IntAct; P28028; 1.
DR   STRING; P28028; -.
DR   PhosphoSite; P28028; -.
DR   PRIDE; P28028; -.
DR   Ensembl; ENSMUST00000002487; ENSMUSP00000002487; ENSMUSG00000002413.
DR   GeneID; 109880; -.
DR   KEGG; mmu:109880; -.
DR   UCSC; uc009bme.1; mouse.
DR   UCSC; uc009bmf.1; mouse.
DR   CTD; 109880; -.
DR   MGI; MGI:88190; Braf.
DR   eggNOG; roNOG15305; -.
DR   HOGENOM; HBG506535; -.
DR   HOVERGEN; HBG001886; -.
DR   InParanoid; P28028; -.
DR   OrthoDB; EOG41G33M; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 362941; -.
DR   ArrayExpress; P28028; -.
DR   Bgee; P28028; -.
DR   CleanEx; MM_BRAF; -.
DR   Genevestigator; P28028; -.
DR   GermOnline; ENSMUSG00000002413; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR003116; Raf-like_ras-bd.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF02196; RBD; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00455; RBD; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50898; RBD; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding;
KW   Chromosomal rearrangement; Kinase; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Proto-oncogene; Serine/threonine-protein kinase;
KW   Transferase; Zinc.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    804       Serine/threonine-protein kinase B-raf.
FT                                /FTId=PRO_0000085666.
FT   DOMAIN      139    211       RBD.
FT   DOMAIN      494    754       Protein kinase.
FT   NP_BIND     500    508       ATP (By similarity).
FT   COMPBIAS      6     30       Poly-Gly.
FT   COMPBIAS    465    469       Poly-Ser.
FT   ACT_SITE    613    613       Proton acceptor (By similarity).
FT   METAL       219    219       Zinc 1 (By similarity).
FT   METAL       232    232       Zinc 2 (By similarity).
FT   METAL       235    235       Zinc 2 (By similarity).
FT   METAL       245    245       Zinc 1 (By similarity).
FT   METAL       248    248       Zinc 1 (By similarity).
FT   METAL       253    253       Zinc 2 (By similarity).
FT   METAL       256    256       Zinc 2 (By similarity).
FT   METAL       264    264       Zinc 1 (By similarity).
FT   BINDING     520    520       ATP (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     135    135       Phosphoserine (By similarity).
FT   MOD_RES     348    348       Phosphoserine (By similarity).
FT   MOD_RES     356    356       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     431    431       Phosphothreonine (By similarity).
FT   MOD_RES     434    434       Phosphoserine (By similarity).
FT   MOD_RES     436    436       Phosphothreonine (By similarity).
FT   MOD_RES     453    453       N6-acetyllysine (By similarity).
FT   MOD_RES     454    454       Phosphoserine (By similarity).
FT   MOD_RES     483    483       Phosphoserine.
FT   MOD_RES     484    484       Phosphoserine (By similarity).
FT   MOD_RES     502    502       Phosphoserine (By similarity).
FT   MOD_RES     651    651       Phosphoserine (By similarity).
FT   MOD_RES     766    766       Phosphoserine (By similarity).
FT   MOD_RES     787    787       Phosphoserine (By similarity).
FT   VAR_SEQ       1    474       Missing (in isoform 2).
FT                                /FTId=VSP_022169.
FT   VAR_SEQ     799    804       EFAAFK -> GFPVH (in isoform 2).
FT                                /FTId=VSP_022170.
SQ   SEQUENCE   804 AA;  88918 MW;  2485AF8A33363DEB CRC64;
     MAALSGGGGR RSGGGGGGGG GGGGGDGGGG AEQGQALFNG DMEPEAGAGA AASSAADPAI
     PEEVWNIKQM IKLTQEHIEA LLDKFGGEHN PPSIYLEAYE EYTSKLDALQ QREQQLLESL
     VFQTPTDASR NNPKSPQKPI VRVFLPNKQR TVVPARCGVT VRDSLKKALM MRGLIPECCA
     VYRIQDGEKK PIGWDTDISW LTGEELHVEV LENVPLTTHN FVRKTFFTLA FCDFCRKLLF
     QGFRCQTCGY KFHQRCSTEV PLMCVNYDQL DLLFVSKFFE HHPVPQEEAS FPETALPSGS
     SSAPPSDSTG PQILTSPSPS KSIPIPQPFR PADEDHRNQF GQRDRSSSAP NVHINTIEPV
     NIDEKFPEVE LQDQRDLIRD QGFRGDGAPL NQLMRCLRKY QSRTPSPLLH SVPSEIVFDF
     EPGPVFRGST TGLSATPPAS LPGSLTNVKA LQKSPGPQRE RKSSSSSSSE DRSRMKTLGR
     RDSSDDWEIP DGQITVGQRI GSGSFGTVYK GKWHGDVAVK MLNVTAPTPQ QLQAFKNEVG
     VLRKTRHVNI LLFMGYSTKP QLAIVTQWCE GSSLYHHLHI IETKFEMIKL IDIARQTAQG
     MDYLHAKSII HRDLKSNNIF LHEDLTVKIG DFGLATVKSR WSGSHQFEQL SGSILWMAPE
     VIRMQDKNPY SFQSDVYAFG IVLYELMTGQ LPYSNINNRD QIIFMVGRGY LSPDLSKVRS
     NCPKAMKRLM AECLKKKRDE RPLFPQILAS IELLARSLPK IHRSASEPSL NRAGFQTEDF
     SLYACASPKT PIQAGGYGEF AAFK
//
ID   CXB1_MOUSE              Reviewed;         283 AA.
AC   P28230;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 3.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Gap junction beta-1 protein;
DE   AltName: Full=Connexin-32;
DE            Short=Cx32;
GN   Name=Gjb1; Synonyms=Cxn-32;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=91285228; PubMed=2060697; DOI=10.1016/0012-1606(91)90452-9;
RA   Nishi M., Kumar N.M., Gilula N.B.;
RT   "Developmental regulation of gap junction gene expression during mouse
RT   embryonic development.";
RL   Dev. Biol. 146:117-130(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92354576; PubMed=1322820;
RA   Willecke K., Nicholson B.J., Dahl E., Kozjek G., Hennemann H.;
RT   "Molecular cloning of mouse connexins26 and -32: similar genomic
RT   organization but distinct promoter sequences of two gap junction
RT   genes.";
RL   Eur. J. Cell Biol. 58:81-89(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RA   Soehl G., Theis M., Hallas G., Brambach S., Dahl E., Kidder G.,
RA   Willecke K.;
RT   "A new alternatively spliced transcript of the mouse connexin32 gene
RT   is expressed in embryonic stem cells, oocytes and liver.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=12843301;
RA   Menichella D.M., Goodenough D.A., Sirkowski E., Scherer S.S.,
RA   Paul D.L.;
RT   "Connexins are critical for normal myelination in the CNS.";
RL   J. Neurosci. 23:5963-5973(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258 AND SER-266, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [7]
RP   INTERACTION WITH CNST.
RX   PubMed=19864490; DOI=10.1093/hmg/ddp490;
RA   del Castillo F.J., Cohen-Salmon M., Charollais A., Caille D.,
RA   Lampe P.D., Chavrier P., Meda P., Petit C.;
RT   "Consortin, a trans-Golgi network cargo receptor for the plasma
RT   membrane targeting and recycling of connexins.";
RL   Hum. Mol. Genet. 19:262-275(2010).
CC   -!- FUNCTION: One gap junction consists of a cluster of closely packed
CC       pairs of transmembrane channels, the connexons, through which
CC       materials of low MW diffuse from one cell to a neighboring cell.
CC   -!- SUBUNIT: A connexon is composed of a hexamer of connexins.
CC       Interacts with CNST.
CC   -!- INTERACTION:
CC       Q8CBC4-3:Cnst; NbExp=1; IntAct=EBI-2616081, EBI-2615407;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Cell junction, gap junction.
CC   -!- DISRUPTION PHENOTYPE: Mice lacking both Gja12 and Gjb1 display a
CC       severe demyelination phenotype associated with oligodendrocyte
CC       death. These mice develop action tremors, tonic seizures, sporadic
CC       convulsions and loss of consciousness preceding death in the sixth
CC       week after birth.
CC   -!- SIMILARITY: Belongs to the connexin family. Beta-type (group I)
CC       subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; M63802; AAA37296.2; -; mRNA.
DR   EMBL; M81447; AAA37496.1; -; Genomic_DNA.
DR   EMBL; AJ271753; CAB72446.1; -; Genomic_DNA.
DR   EMBL; BC026833; AAH26833.1; -; mRNA.
DR   IPI; IPI00118459; -.
DR   PIR; B49769; B49769.
DR   RefSeq; NP_032150.2; NM_008124.2.
DR   UniGene; Mm.21198; -.
DR   ProteinModelPortal; P28230; -.
DR   SMR; P28230; 2-215.
DR   IntAct; P28230; 1.
DR   STRING; P28230; -.
DR   PhosphoSite; P28230; -.
DR   PRIDE; P28230; -.
DR   Ensembl; ENSMUST00000052130; ENSMUSP00000062723; ENSMUSG00000047797.
DR   Ensembl; ENSMUST00000119080; ENSMUSP00000113904; ENSMUSG00000047797.
DR   Ensembl; ENSMUST00000119190; ENSMUSP00000113516; ENSMUSG00000047797.
DR   GeneID; 14618; -.
DR   KEGG; mmu:14618; -.
DR   UCSC; uc009txk.1; mouse.
DR   CTD; 14618; -.
DR   MGI; MGI:95719; Gjb1.
DR   GeneTree; ENSGT00560000076934; -.
DR   HOGENOM; HBG717760; -.
DR   HOVERGEN; HBG009576; -.
DR   InParanoid; P28230; -.
DR   OMA; SSEYKQN; -.
DR   OrthoDB; EOG4PVP0F; -.
DR   PhylomeDB; P28230; -.
DR   NextBio; 286436; -.
DR   PMAP-CutDB; P28230; -.
DR   ArrayExpress; P28230; -.
DR   Bgee; P28230; -.
DR   CleanEx; MM_GJB1; -.
DR   Genevestigator; P28230; -.
DR   GermOnline; ENSMUSG00000047797; Mus musculus.
DR   GO; GO:0005922; C:connexon complex; IEA:InterPro.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   InterPro; IPR000500; Connexin.
DR   InterPro; IPR002267; Connexin32.
DR   InterPro; IPR019570; Connexin_CCC.
DR   InterPro; IPR017990; Connexin_CS.
DR   InterPro; IPR013092; Connexin_N.
DR   PANTHER; PTHR11984; Connexin; 1.
DR   Pfam; PF00029; Connexin; 1.
DR   Pfam; PF10582; Connexin_CCC; 1.
DR   PRINTS; PR00206; CONNEXIN.
DR   PRINTS; PR01138; CONNEXINB1.
DR   SMART; SM00037; CNX; 1.
DR   PROSITE; PS00407; CONNEXINS_1; 1.
DR   PROSITE; PS00408; CONNEXINS_2; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Gap junction; Membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    283       Gap junction beta-1 protein.
FT                                /FTId=PRO_0000057851.
FT   TOPO_DOM      1     22       Cytoplasmic (Potential).
FT   TRANSMEM     23     45       Helical; (Potential).
FT   TOPO_DOM     46     75       Extracellular (Potential).
FT   TRANSMEM     76     95       Helical; (Potential).
FT   TOPO_DOM     96    130       Cytoplasmic (Potential).
FT   TRANSMEM    131    153       Helical; (Potential).
FT   TOPO_DOM    154    191       Extracellular (Potential).
FT   TRANSMEM    192    214       Helical; (Potential).
FT   TOPO_DOM    215    283       Cytoplasmic (Potential).
FT   MOD_RES     258    258       Phosphoserine.
FT   MOD_RES     266    266       Phosphoserine.
FT   CONFLICT    235    235       F -> S (in Ref. 1; AAA37296).
FT   CONFLICT    263    266       LRRS -> PXPH (in Ref. 1; AAA37296).
SQ   SEQUENCE   283 AA;  32004 MW;  C79FC46AA13BC5D7 CRC64;
     MNWTGLYTLL SGVNRHSTAI GRVWLSVIFI FRIMVLVVAA ESVWGDEKSS FICNTLQPGC
     NSVCYDHFFP ISHVRLWSLQ LILVSTPALL VAMHVAHQQH IEKKMLRLEG HGDPLHLEEV
     KRHKVHISGT LWWTYVISVV FRLLFEAVFM YVFYLLYPGY AMVRLVKCEA FPCPNTVDCF
     VSRPTEKTVF TVFMLAASGI CIILNVAEVV YLIIRACARR AQRRSNPPSR KGSGFGHRLS
     PEYKQNEINK LLSEQDGSLK DILRRSPGTG AGLAEKSDRC SAC
//
ID   5HT1B_MOUSE             Reviewed;         386 AA.
AC   P28334;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=5-hydroxytryptamine receptor 1B;
DE            Short=5-HT-1B;
DE            Short=5-HT1B;
DE   AltName: Full=Serotonin receptor 1B;
GN   Name=Htr1b; Synonyms=5ht1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92212959; PubMed=1557407; DOI=10.1073/pnas.89.7.3020;
RA   Maroteaux L., Saudou F., Amlaiky N., Boschert U., Plassat J.-L.,
RA   Hen R.;
RT   "Mouse 5HT1B serotonin receptor: cloning, functional expression, and
RT   localization in motor control centers.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:3020-3024(1992).
CC   -!- FUNCTION: This is one of the several different receptors for 5-
CC       hydroxytryptamine (serotonin), a biogenic hormone that functions
CC       as a neurotransmitter, a hormone, and a mitogen. The activity of
CC       this receptor is mediated by G proteins that inhibit adenylate
CC       cyclase activity.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in striatum and
CC       Purkinje cells.
CC   -!- PTM: Phosphorylated (By similarity).
CC   -!- PTM: Palmitoylated (By similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
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DR   EMBL; Z11597; CAA77678.1; -; Genomic_DNA.
DR   EMBL; M85151; AAA83221.1; -; Genomic_DNA.
DR   IPI; IPI00119583; -.
DR   PIR; A42688; A42688.
DR   RefSeq; NP_034612.1; NM_010482.1.
DR   UniGene; Mm.445308; -.
DR   ProteinModelPortal; P28334; -.
DR   SMR; P28334; 43-382.
DR   STRING; P28334; -.
DR   PhosphoSite; P28334; -.
DR   PRIDE; P28334; -.
DR   Ensembl; ENSMUST00000051005; ENSMUSP00000050898; ENSMUSG00000049511.
DR   GeneID; 15551; -.
DR   KEGG; mmu:15551; -.
DR   UCSC; uc009qvl.1; mouse.
DR   CTD; 15551; -.
DR   MGI; MGI:96274; Htr1b.
DR   eggNOG; roNOG07877; -.
DR   HOGENOM; HBG445348; -.
DR   HOVERGEN; HBG106962; -.
DR   InParanoid; P28334; -.
DR   OMA; ALPWKVL; -.
DR   OrthoDB; EOG4R7VB6; -.
DR   PhylomeDB; P28334; -.
DR   NextBio; 288484; -.
DR   ArrayExpress; P28334; -.
DR   Bgee; P28334; -.
DR   CleanEx; MM_HTR1B; -.
DR   Genevestigator; P28334; -.
DR   GermOnline; ENSMUSG00000049511; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0008144; F:drug binding; IDA:UniProtKB.
DR   GO; GO:0051378; F:serotonin binding; IDA:UniProtKB.
DR   GO; GO:0004993; F:serotonin receptor activity; IDA:UniProtKB.
DR   GO; GO:0007205; P:activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway; IMP:UniProtKB.
DR   GO; GO:0046849; P:bone remodeling; IGI:MGI.
DR   GO; GO:0071502; P:cellular response to temperature stimulus; IDA:UniProtKB.
DR   GO; GO:0002031; P:G-protein coupled receptor internalization; IDA:UniProtKB.
DR   GO; GO:0042493; P:response to drug; IDA:UniProtKB.
DR   InterPro; IPR002147; 5HT1B_rcpt.
DR   InterPro; IPR002231; 5HT_rcpt.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00513; 5HT1BRECEPTR.
DR   PRINTS; PR01101; 5HTRECEPTOR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Receptor; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN         1    386       5-hydroxytryptamine receptor 1B.
FT                                /FTId=PRO_0000068917.
FT   TOPO_DOM      1     47       Extracellular (By similarity).
FT   TRANSMEM     48     71       Helical; Name=1; (By similarity).
FT   TOPO_DOM     72     82       Cytoplasmic (By similarity).
FT   TRANSMEM     83    109       Helical; Name=2; (By similarity).
FT   TOPO_DOM    110    119       Extracellular (By similarity).
FT   TRANSMEM    120    141       Helical; Name=3; (By similarity).
FT   TOPO_DOM    142    163       Cytoplasmic (By similarity).
FT   TRANSMEM    164    183       Helical; Name=4; (By similarity).
FT   TOPO_DOM    184    204       Extracellular (By similarity).
FT   TRANSMEM    205    224       Helical; Name=5; (By similarity).
FT   TOPO_DOM    225    311       Cytoplasmic (By similarity).
FT   TRANSMEM    312    332       Helical; Name=6; (By similarity).
FT   TOPO_DOM    333    346       Extracellular (By similarity).
FT   TRANSMEM    347    369       Helical; Name=7; (By similarity).
FT   TOPO_DOM    370    386       Cytoplasmic (By similarity).
FT   LIPID       384    384       S-palmitoyl cysteine (Potential).
FT   CARBOHYD     24     24       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     28     28       N-linked (GlcNAc...) (Potential).
FT   DISULFID    118    195       By similarity.
SQ   SEQUENCE   386 AA;  43079 MW;  58F70FBEA770C0B3 CRC64;
     MEEQGIQCAP PPPAASQTGV PLTNLSHNCS ADGYIYQDSI ALPWKVLLVA LLALITLATT
     LSNAFVIATV YRTRKLHTPA NYLIASLAVT DLLVSILVMP ISTMYTVTGR WTLGQVVCDF
     WLSSDITCCT ASIMHLCVIA LDRYWAITDA VEYSAKRTPK RAAIMIVLVW VFSISISLPP
     FFWRQAKAEE EMLDCFVNTD HVLYTVYSTV GAFYLPTLLL IALYGRIYVE ARSRILKQTP
     NKTGKRLTRA QLITDSPGST SSVTSINSRA PDVPSESGSP VYVNQVKVRV SDALLEKKKL
     MAARERKATK TLGIILGAFI VCWLPFFIIS LVMPICKDAC WFHMAIFDFF NWLGYLNSLI
     NPIIYTMSNE DFKQAFHKLI RFKCAG
//
ID   ADHX_MOUSE              Reviewed;         374 AA.
AC   P28474; Q3TW83; Q8C662;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 110.
DE   RecName: Full=Alcohol dehydrogenase class-3;
DE            EC=1.1.1.1;
DE   AltName: Full=Alcohol dehydrogenase 2;
DE   AltName: Full=Alcohol dehydrogenase 5;
DE   AltName: Full=Alcohol dehydrogenase B2;
DE            Short=ADH-B2;
DE   AltName: Full=Alcohol dehydrogenase class-III;
DE   AltName: Full=Glutathione-dependent formaldehyde dehydrogenase;
DE            Short=FALDH;
DE            Short=FDH;
DE            Short=GSH-FDH;
DE            EC=1.1.1.-;
DE   AltName: Full=S-(hydroxymethyl)glutathione dehydrogenase;
DE            EC=1.1.1.284;
GN   Name=Adh5; Synonyms=Adh-2, Adh2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=91272926; PubMed=2053480;
RA   Edenberg H.J., Brown C.J., Carr L.G., Ho W.H., Hur M.W.;
RT   "Alcohol dehydrogenase gene expression and cloning of the mouse chi-
RT   like ADH.";
RL   Adv. Exp. Med. Biol. 284:253-262(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=93112997; PubMed=1472709;
RA   Hur M.W., Ho W.H., Brown C.J., Goldman D., Edenberg H.J.;
RT   "Molecular cloning of mouse alcohol dehydrogenase-B2 cDNA: nucleotide
RT   sequences of the class III ADH genes evolve slowly even for silent
RT   substitutions.";
RL   DNA Seq. 3:167-175(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   MEDLINE=96215448; PubMed=8647091;
RX   DOI=10.1111/j.1432-1033.1996.0496k.x;
RA   Foglio M.H., Duester G.;
RT   "Characterization of the functional gene encoding mouse class III
RT   alcohol dehydrogenase (glutathione-dependent formaldehyde
RT   dehydrogenase) and an unexpressed processed pseudogene with an intact
RT   open reading frame.";
RL   Eur. J. Biochem. 237:496-504(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 234-248, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   TISSUE SPECIFICITY.
RC   STRAIN=FVB/N;
RX   MEDLINE=95256259; PubMed=7738026; DOI=10.1074/jbc.270.18.10868;
RA   Zgombic-Knight M., Ang H.L., Foglio M.H., Duester G.;
RT   "Cloning of the mouse class IV alcohol dehydrogenase (retinol
RT   dehydrogenase) cDNA and tissue-specific expression patterns of the
RT   murine ADH gene family.";
RL   J. Biol. Chem. 270:10868-10877(1995).
CC   -!- FUNCTION: Class-III ADH is remarkably ineffective in oxidizing
CC       ethanol, but it readily catalyzes the oxidation of long-chain
CC       primary alcohols and the oxidation of S-(hydroxymethyl)
CC       glutathione.
CC   -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone +
CC       NADH.
CC   -!- CATALYTIC ACTIVITY: S-(hydroxymethyl)glutathione + NAD(P)(+) = S-
CC       formylglutathione + NAD(P)H.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Class-III subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; M84147; AAA68896.1; -; mRNA.
DR   EMBL; U48970; AAC52763.1; -; Genomic_DNA.
DR   EMBL; U48964; AAC52763.1; JOINED; Genomic_DNA.
DR   EMBL; U48965; AAC52763.1; JOINED; Genomic_DNA.
DR   EMBL; U48966; AAC52763.1; JOINED; Genomic_DNA.
DR   EMBL; U48968; AAC52763.1; JOINED; Genomic_DNA.
DR   EMBL; U48969; AAC52763.1; JOINED; Genomic_DNA.
DR   EMBL; AK076507; BAC36370.1; -; mRNA.
DR   EMBL; AK146949; BAE27558.1; -; mRNA.
DR   EMBL; AK159803; BAE35383.1; -; mRNA.
DR   EMBL; BC090978; AAH90978.1; -; mRNA.
DR   IPI; IPI00555004; -.
DR   PIR; A56643; A56643.
DR   RefSeq; NP_031436.2; NM_007410.2.
DR   UniGene; Mm.3874; -.
DR   PDB; 1OTQ; Model; -; A=1-374.
DR   PDBsum; 1OTQ; -.
DR   ProteinModelPortal; P28474; -.
DR   SMR; P28474; 2-374.
DR   STRING; P28474; -.
DR   PhosphoSite; P28474; -.
DR   REPRODUCTION-2DPAGE; P28474; -.
DR   PRIDE; P28474; -.
DR   Ensembl; ENSMUST00000005964; ENSMUSP00000005964; ENSMUSG00000028138.
DR   GeneID; 11532; -.
DR   KEGG; mmu:11532; -.
DR   UCSC; uc008rnk.1; mouse.
DR   CTD; 11532; -.
DR   MGI; MGI:87929; Adh5.
DR   eggNOG; roNOG14979; -.
DR   HOGENOM; HBG753318; -.
DR   HOVERGEN; HBG000195; -.
DR   InParanoid; P28474; -.
DR   OMA; LYVPQCG; -.
DR   OrthoDB; EOG4J6RR3; -.
DR   PhylomeDB; P28474; -.
DR   BRENDA; 1.1.1.1; 244.
DR   BRENDA; 1.1.1.284; 244.
DR   NextBio; 278968; -.
DR   ArrayExpress; P28474; -.
DR   Bgee; P28474; -.
DR   Genevestigator; P28474; -.
DR   GermOnline; ENSMUSG00000028138; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0004022; F:alcohol dehydrogenase (NAD) activity; IDA:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
DR   GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase activity; IMP:MGI.
DR   GO; GO:0046294; P:formaldehyde catabolic process; IMP:MGI.
DR   GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; IMP:MGI.
DR   GO; GO:0045777; P:positive regulation of blood pressure; IMP:MGI.
DR   GO; GO:0003016; P:respiratory system process; IMP:MGI.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR   GO; GO:0051409; P:response to nitrosative stress; IMP:MGI.
DR   GO; GO:0001523; P:retinoid metabolic process; IMP:MGI.
DR   InterPro; IPR014183; ADH_3.
DR   InterPro; IPR013149; ADH_C.
DR   InterPro; IPR013154; ADH_GroES-like.
DR   InterPro; IPR002085; ADH_SF_Zn.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR11695; ADH_Sf_Zn; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; GroES_like; 2.
DR   TIGRFAMs; TIGR02818; adh_III_F_hyde; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Metal-binding; NAD; Oxidoreductase; Zinc.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    374       Alcohol dehydrogenase class-3.
FT                                /FTId=PRO_0000160760.
FT   METAL        45     45       Zinc 1; catalytic (By similarity).
FT   METAL        67     67       Zinc 1; catalytic (By similarity).
FT   METAL        97     97       Zinc 2 (By similarity).
FT   METAL       100    100       Zinc 2 (By similarity).
FT   METAL       103    103       Zinc 2 (By similarity).
FT   METAL       111    111       Zinc 2 (By similarity).
FT   METAL       174    174       Zinc 1; catalytic (By similarity).
FT   SITE        115    115       Important for FDH activity and activation
FT                                by fatty acids (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   CONFLICT     55     55       A -> R (in Ref. 1; no nucleotide entry,
FT                                2; AAA68896 and 3; AAC52763).
FT   CONFLICT    133    133       K -> R (in Ref. 4; BAE35383).
FT   CONFLICT    183    183       A -> T (in Ref. 4; BAE35383).
FT   CONFLICT    253    253       V -> I (in Ref. 4; BAE35383).
FT   STRAND        5     12
FT   STRAND       20     26
FT   STRAND       33     43
FT   HELIX        45     52
FT   STRAND       60     62
FT   STRAND       68     75
FT   STRAND       87     90
FT   STRAND       97     99
FT   HELIX       100    103
FT   HELIX       114    118
FT   STRAND      128    131
FT   TURN        140    142
FT   STRAND      146    152
FT   HELIX       153    155
FT   STRAND      156    158
FT   HELIX       165    168
FT   HELIX       169    172
FT   HELIX       174    183
FT   STRAND      193    197
FT   HELIX       201    213
FT   STRAND      216    221
FT   HELIX       225    227
FT   HELIX       228    234
FT   STRAND      237    240
FT   HELIX       242    244
FT   HELIX       249    257
FT   STRAND      261    266
FT   HELIX       271    280
FT   TURN        283    285
FT   STRAND      287    290
FT   HELIX       305    308
FT   STRAND      312    315
FT   HELIX       318    320
FT   HELIX       323    335
FT   HELIX       342    344
FT   STRAND      347    351
FT   HELIX       354    363
FT   STRAND      369    372
SQ   SEQUENCE   374 AA;  39548 MW;  32A3727B5DAB0919 CRC64;
     MANQVIRCKA AVAWEAGKPL SIEEIEVAPP KAHEVRIKIL ATAVCHTDAY TLSGADPEGC
     FPVILGHEGA GIVESVGEGV TKLKAGDTVI PLYIPQCGEC KFCLNPKTNL CQKIRVTQGK
     GLMPDGTSRF TCKGKSVFHF MGTSTFSEYT VVADISVAKI DPSAPLDKVC LLGCGISTGY
     GAAVNTAKVE PGSTCAVFGL GGVGLAVIMG CKVAGASRII GIDINKDKFA KAKEFGASEC
     ISPQDFSKSI QEVLVEMTDG GVDYSFECIG NVKVMRSALE AAHKGWGVSV VVGVAASGEE
     ISTRPFQLVT GRTWKGTAFG GWKSVESVPK LVSEYMSKKI KVDEFVTGNL SFDQINQAFD
     LMHSGDSIRT VLKM
//
ID   SC6A9_MOUSE             Reviewed;         692 AA.
AC   P28571; B1ASI9; Q8VC47;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 3.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Sodium- and chloride-dependent glycine transporter 1;
DE            Short=GlyT-1;
DE            Short=GlyT1;
DE   AltName: Full=Solute carrier family 6 member 9;
GN   Name=Slc6a9; Synonyms=Glyt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GLYT-1A).
RC   TISSUE=Brain;
RX   MEDLINE=92316254; PubMed=1618338; DOI=10.1016/0014-5793(92)80875-H;
RA   Liu Q.-R., Nelson H., Mandiyan S., Lopez-Corcuera B., Nelson N.;
RT   "Cloning and expression of a glycine transporter from mouse brain.";
RL   FEBS Lett. 305:110-114(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS GLYT-1A; GLYT-1B AND
RP   GLYT-1C), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, ALTERNATIVE
RP   PROMOTER USAGE, AND ALTERNATIVE SPLICING.
RC   STRAIN=NMRI;
RX   PubMed=7891186;
RA   Adams R.H., Sato K., Shimada S., Tohyama M., Puschel A.W., Betz H.;
RT   "Gene structure and glial expression of the glycine transporter GlyT1
RT   in embryonic and adult rodents.";
RL   J. Neurosci. 15:2524-2532(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GLYT-1A).
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-117 (ISOFORMS GLYT-1A AND GLYT-1B),
RP   AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=94043045; PubMed=8226790;
RA   Liu Q.-R., Lopez-Corcuera B., Mandiyan S., Nelson H., Nelson N.;
RT   "Cloning and expression of a spinal cord- and brain-specific glycine
RT   transporter with novel structural features.";
RL   J. Biol. Chem. 268:22802-22808(1993).
CC   -!- FUNCTION: Terminates the action of glycine by its high affinity
CC       sodium-dependent reuptake into presynaptic terminals. May play a
CC       role in regulation of glycine levels in NMDA receptor-mediated
CC       neurotransmission.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
CC       Name=GlyT-1C; Synonyms=GLYT1c;
CC         IsoId=P28571-3; Sequence=Displayed;
CC         Note=Produced by alternative promoter usage;
CC       Name=GlyT-1A; Synonyms=GLYT1a;
CC         IsoId=P28571-1; Sequence=VSP_006272;
CC         Note=Produced by alternative promoter usage;
CC       Name=GlyT-1B; Synonyms=GLYT1b;
CC         IsoId=P28571-2; Sequence=VSP_039241;
CC         Note=Produced by alternative splicing of isoform GlyT-1C;
CC   -!- TISSUE SPECIFICITY: At E11, expressed in the ventral part of the
CC       ventricular zone. At E15, also expressed in adjacent mantle tissue
CC       and the meninges. Strongly expressed in E12 and E15 liver.
CC   -!- DEVELOPMENTAL STAGE: Expression is present at low levels as early
CC       as E9 and E10, but strongly increases at E13 and remains at high
CC       levels up to E15. Also expressed in adult.
CC   -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF)
CC       (TC 2.A.22) family. SLC6A9 subfamily.
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DR   EMBL; X67056; CAA47440.1; -; mRNA.
DR   EMBL; X82567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X82568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X82569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X82570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X82571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X82572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL627128; CAM14713.1; -; Genomic_DNA.
DR   EMBL; BC021828; AAH21828.1; -; mRNA.
DR   IPI; IPI00122101; -.
DR   IPI; IPI00468633; -.
DR   IPI; IPI00968359; -.
DR   PIR; E46027; E46027.
DR   PIR; S23151; S23151.
DR   RefSeq; NP_032161.2; NM_008135.4.
DR   UniGene; Mm.244549; -.
DR   STRING; P28571; -.
DR   PRIDE; P28571; -.
DR   Ensembl; ENSMUST00000030269; ENSMUSP00000030269; ENSMUSG00000028542.
DR   Ensembl; ENSMUST00000063857; ENSMUSP00000066102; ENSMUSG00000028542.
DR   Ensembl; ENSMUST00000102685; ENSMUSP00000099746; ENSMUSG00000028542.
DR   GeneID; 14664; -.
DR   KEGG; mmu:14664; -.
DR   UCSC; uc008uiy.1; mouse.
DR   CTD; 14664; -.
DR   MGI; MGI:95760; Slc6a9.
DR   eggNOG; roNOG12125; -.
DR   GeneTree; ENSGT00600000084044; -.
DR   HOVERGEN; HBG071421; -.
DR   OrthoDB; EOG4HT8RR; -.
DR   ArrayExpress; P28571; -.
DR   Bgee; P28571; -.
DR   Genevestigator; P28571; -.
DR   GermOnline; ENSMUSG00000028542; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; IEA:InterPro.
DR   GO; GO:0015187; F:glycine transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0005328; F:neurotransmitter:sodium symporter activity; IEA:InterPro.
DR   GO; GO:0005283; F:sodium:amino acid symporter activity; IEA:InterPro.
DR   InterPro; IPR000175; Na/ntran_symport.
DR   InterPro; IPR003028; Na/ntran_symport_glycine_GLY1.
DR   PANTHER; PTHR11616; Na/ntran_symport; 1.
DR   Pfam; PF00209; SNF; 1.
DR   PRINTS; PR01204; GLY1TRNSPORT.
DR   PRINTS; PR00176; NANEUSMPORT.
DR   PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR   PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
DR   PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE   2: Evidence at transcript level;
KW   Alternative promoter usage; Alternative splicing;
KW   Amino-acid transport; Membrane; Neurotransmitter transport; Symport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    692       Sodium- and chloride-dependent glycine
FT                                transporter 1.
FT                                /FTId=PRO_0000214781.
FT   TOPO_DOM      1     94       Cytoplasmic (Potential).
FT   TRANSMEM     95    115       Helical; Name=1; (Potential).
FT   TRANSMEM    122    142       Helical; Name=2; (Potential).
FT   TRANSMEM    174    194       Helical; Name=3; (Potential).
FT   TOPO_DOM    195    271       Extracellular (Potential).
FT   TRANSMEM    272    292       Helical; Name=4; (Potential).
FT   TRANSMEM    301    321       Helical; Name=5; (Potential).
FT   TRANSMEM    346    366       Helical; Name=6; (Potential).
FT   TRANSMEM    393    413       Helical; Name=7; (Potential).
FT   TRANSMEM    436    456       Helical; Name=8; (Potential).
FT   TRANSMEM    492    512       Helical; Name=9; (Potential).
FT   TRANSMEM    516    536       Helical; Name=10; (Potential).
FT   TRANSMEM    556    576       Helical; Name=11; (Potential).
FT   TRANSMEM    596    616       Helical; Name=12; (Potential).
FT   TOPO_DOM    617    692       Cytoplasmic (Potential).
FT   VAR_SEQ       1     69       MIGGDTRAASAHPGMASAQGPVATPSPEQPFPGTTSVSLAR
FT                                PVLRVWHGAHSSGLLPNLIAQHSPAMAQ -> MVGKGAKGM
FT                                L (in isoform GlyT-1A).
FT                                /FTId=VSP_006272.
FT   VAR_SEQ      29     69       Missing (in isoform GlyT-1B).
FT                                /FTId=VSP_039241.
FT   CONFLICT    341    341       I -> Y (in Ref. 1; CAA47440 and 2;
FT                                X82570).
FT   CONFLICT    393    394       SV -> RL (in Ref. 1; CAA47440).
FT   CONFLICT    597    597       A -> R (in Ref. 1; CAA47440 and 2;
FT                                X82571).
SQ   SEQUENCE   692 AA;  76544 MW;  C4A78A6562DAB01E CRC64;
     MIGGDTRAAS AHPGMASAQG PVATPSPEQP FPGTTSVSLA RPVLRVWHGA HSSGLLPNLI
     AQHSPAMAQN GAVPSEATKK DQNLTRGNWG NQIEFVLTSV GYAVGLGNVW RFPYLCYRNG
     GGAFMFPYFI MLIFCGIPLF FMELSFGQFA SQGCLGVWRI SPMFKGVGYG MMVVSTYIGI
     YYNVVICIAF YYFFSSMTHV LPWAYCNNPW NTPDCAGVLD ASNLTNGSRP AALSGNLSHL
     FNYTLQRTSP SEEYWRLYVL KLSDDIGNFG EVRLPLLGCL GVSWVVVFLC LIRGVKSSGK
     VVYFTATFPY VVLTILFVRG VTLEGAFTGI MYYLTPQWDK ILEAKVWGDA ASQIFYSLGC
     AWGGLITMAS YNKFHNNCYR DSVIISITNC ATSVYAGFVI FSILGFMANH LGVDVSRVAD
     HGPGLAFVAY PEALTLLPIS PLWSLLFFFM LILLGLGTQF CLLETLVTAI VDEVGNEWIL
     QKKTYVTLGV AVAGFLLGIP LTSQAGIYWL LLMDNYAASF SLVVISCIMC VSIMYIYGHR
     NYFQDIQMML GFPPPLFFQI CWRFVSPAII FFILIFTVIQ YRPITYNHYQ YPGWAVAIGF
     LMALSSVICI PLYALFQLCR TDGDTLLQRL KNATKPSRDW GPALLEHRTG RYAPTTTPSP
     EDGFEVQPLH PDKAQIPIVG SNGSSRFQDS RI
//
ID   NP1L1_MOUSE             Reviewed;         391 AA.
AC   P28656; Q3UL14;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Nucleosome assembly protein 1-like 1;
DE   AltName: Full=Brain protein DN38;
DE   AltName: Full=NAP-1-related protein;
DE   Flags: Precursor;
GN   Name=Nap1l1; Synonyms=Nrp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Okuda A.;
RL   Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Egg, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 50-391.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   PubMed=12106288; DOI=10.1111/j.1460-9568.1990.tb00460.x;
RA   Kato K.;
RT   "A collection of cDNA clones with specific expression patterns in
RT   mouse brain.";
RL   Eur. J. Neurosci. 2:704-711(1990).
RN   [5]
RP   PROTEIN SEQUENCE OF 267-275, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-62, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   POLYGLUTAMYLATION.
RC   STRAIN=C57BL/6; TISSUE=Testis;
RX   PubMed=17499049; DOI=10.1016/j.molcel.2007.04.012;
RA   van Dijk J., Rogowski K., Miro J., Lacroix B., Edde B., Janke C.;
RT   "A targeted multienzyme mechanism for selective microtubule
RT   polyglutamylation.";
RL   Mol. Cell 26:437-448(2007).
RN   [8]
RP   POLYGLYCYLATION AT GLU-359 AND GLU-360, AND MUTAGENESIS OF GLU-359 AND
RP   GLU-360.
RX   PubMed=18331838; DOI=10.1016/j.febslet.2008.02.079;
RA   Ikegami K., Horigome D., Mukai M., Livnat I., MacGregor G.R.,
RA   Setou M.;
RT   "TTLL10 is a protein polyglycylase that can modify nucleosome assembly
RT   protein 1.";
RL   FEBS Lett. 582:1129-1134(2008).
CC   -!- FUNCTION: May be involved in modulating chromatin formation and
CC       contribute to regulation of cell proliferation.
CC   -!- INTERACTION:
CC       Q9WVS7:Map2k5; NbExp=2; IntAct=EBI-645055, EBI-446144;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Melanosome (By similarity).
CC   -!- TISSUE SPECIFICITY: High expression in cerebral cortex, not in
CC       cerebellar cortex.
CC   -!- DOMAIN: The acidic domains are probably involved in the
CC       interaction with histones.
CC   -!- PTM: Polyglutamylated and polyglycylated. These 2 modifications
CC       occur exclusively on glutamate residues and result in either
CC       polyglutamate or polyglycine chains on the gamma-carboxyl group.
CC       Both modifications can coexist on the same protein on adjacent
CC       residues, and lowering polyglycylation levels increases
CC       polyglutamylation, and reciprocally. Polyglutamylated by TTLL4
CC       Polyglycylated by TTLL10.
CC   -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP)
CC       family.
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DR   EMBL; D12618; BAA02142.1; -; mRNA.
DR   EMBL; AK050375; BAC34219.1; -; mRNA.
DR   EMBL; AK136161; BAE22850.1; -; mRNA.
DR   EMBL; AK145766; BAE26637.1; -; mRNA.
DR   EMBL; BC076591; AAH76591.1; -; mRNA.
DR   EMBL; X61449; CAA43689.1; -; mRNA.
DR   IPI; IPI00123199; -.
DR   PIR; JS0707; JS0707.
DR   RefSeq; NP_001140179.1; NM_001146707.1.
DR   RefSeq; NP_056596.1; NM_015781.4.
DR   UniGene; Mm.290407; -.
DR   ProteinModelPortal; P28656; -.
DR   SMR; P28656; 52-352.
DR   IntAct; P28656; 21.
DR   STRING; P28656; -.
DR   PhosphoSite; P28656; -.
DR   PRIDE; P28656; -.
DR   Ensembl; ENSMUST00000065917; ENSMUSP00000070068; ENSMUSG00000058799.
DR   GeneID; 53605; -.
DR   KEGG; mmu:53605; -.
DR   UCSC; uc007hac.1; mouse.
DR   CTD; 53605; -.
DR   MGI; MGI:1855693; Nap1l1.
DR   eggNOG; roNOG17400; -.
DR   HOGENOM; HBG619916; -.
DR   HOVERGEN; HBG052653; -.
DR   InParanoid; P28656; -.
DR   OMA; PDYDSKK; -.
DR   OrthoDB; EOG46WZ99; -.
DR   PhylomeDB; P28656; -.
DR   NextBio; 310297; -.
DR   ArrayExpress; P28656; -.
DR   Bgee; P28656; -.
DR   CleanEx; MM_NAP1L1; -.
DR   Genevestigator; P28656; -.
DR   GermOnline; ENSMUSG00000058799; Mus musculus.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   InterPro; IPR002164; NAP_family.
DR   PANTHER; PTHR11875; NAP_family; 1.
DR   Pfam; PF00956; NAP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Lipoprotein; Methylation;
KW   Nucleus; Phosphoprotein; Prenylation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    388       Nucleosome assembly protein 1-like 1.
FT                                /FTId=PRO_0000185653.
FT   PROPEP      389    391       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000396686.
FT   MOTIF       273    279       Nuclear localization signal (Potential).
FT   COMPBIAS     11     30       Asp/Glu-rich (acidic).
FT   COMPBIAS    129    145       Asp/Glu-rich (acidic).
FT   COMPBIAS    348    378       Asp/Glu-rich (acidic).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      10     10       Phosphoserine (By similarity).
FT   MOD_RES      62     62       Phosphothreonine.
FT   MOD_RES      69     69       Phosphoserine (By similarity).
FT   MOD_RES     116    116       N6-acetyllysine (By similarity).
FT   MOD_RES     143    143       Phosphoserine (By similarity).
FT   MOD_RES     359    359       5-glutamyl polyglycine (Probable).
FT   MOD_RES     360    360       5-glutamyl polyglycine (Probable).
FT   MOD_RES     388    388       Cysteine methyl ester (By similarity).
FT   LIPID       388    388       S-farnesyl cysteine (By similarity).
FT   MUTAGEN     359    359       E->D: Reduced polyglycylation.
FT   MUTAGEN     360    360       E->D: Reduced polyglycylation.
FT   CONFLICT    377    390       YDPKKDQNPAECKQ -> MTQRRIRTQPSASSSE (in
FT                                Ref. 4; CAA43689).
SQ   SEQUENCE   391 AA;  45345 MW;  48F17F3A44D9A597 CRC64;
     MADIDNKEQS ELDQDLEDVE EVEEEETGEE TKIKARQLTV QMMQNPQILA ALQERLDGLV
     DTPTGYIESL PKVVKRRVNA LKNLQVKCAQ IEAKFYEEVH DLERKYAVLY QPLFDKRFEI
     INAIYEPTEE ECEWKPDEED EVSEELKEKA KIEDEKKDEE KEDPKGIPEF WLTVFKNVDL
     LSDMVQEHDE PILKHLKDIK VKFSDAGQPM SFVLEFHFEP NDYFTNEVLT KTYRMRSEPD
     DSDPFSFDGP EIMGCTGCQI DWKKGKNVTL KTIKKKQKHK GRGTVRTVTK TVSNDSFFNF
     FAPPEVPENG DLDDDAEAIL AADFEIGHFL RERIIPRSVL YFTGEAIEDD DDDYDEEGEE
     ADEEGEEEGD EENDPDYDPK KDQNPAECKQ Q
//
ID   SEPT4_MOUSE             Reviewed;         478 AA.
AC   P28661; B2KGM6; Q3UVH1; Q3UZC3; Q5ND10; Q5ND15; Q5ND16; Q7TPM7;
AC   Q80VX1;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Septin-4;
DE   AltName: Full=Brain protein H5;
DE   AltName: Full=Peanut-like protein 2;
GN   Name=Sept4; Synonyms=Pnutl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   PubMed=12106288; DOI=10.1111/j.1460-9568.1990.tb00460.x;
RA   Kato K.;
RT   "A collection of cDNA clones with specific expression patterns in
RT   mouse brain.";
RL   Eur. J. Neurosci. 2:704-711(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), INTERACTION WITH DPYSL5,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Brain;
RX   MEDLINE=22469591; PubMed=12581152;
RX   DOI=10.1046/j.1365-2443.2003.00617.x;
RA   Takahashi S., Inatome R., Yamamura H., Yanagi S.;
RT   "Isolation and expression of a novel mitochondrial septin that
RT   interacts with CRMP/CRAM in the developing neurones.";
RL   Genes Cells 8:81-93(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 5 AND 6).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
RP   SPLICING.
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 282-290, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [10]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17546647; DOI=10.1002/humu.20554;
RA   Sudo K., Ito H., Iwamoto I., Morishita R., Asano T., Nagata K.;
RT   "SEPT9 sequence alternations causing hereditary neuralgic amyotrophy
RT   are associated with altered interactions with SEPT4/SEPT11 and
RT   resistance to Rho/Rhotekin-signaling.";
RL   Hum. Mutat. 28:1005-1013(2007).
CC   -!- FUNCTION: Filament-forming cytoskeletal GTPase (By similarity).
CC       May play a role in cytokinesis (Potential). May play a role in
CC       platelet secretion (By similarity).
CC   -!- SUBUNIT: Septins polymerize into heterooligomeric protein
CC       complexes that form filaments, and can associate with cellular
CC       membranes, actin filaments and microtubules. GTPase activity is
CC       required for filament formation (By similarity). Interacts with
CC       SEPT8 (By similarity). Isoform 4 interacts with DPYSL5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 4: Mitochondrion. Note=In retinoic
CC       acid-treated P19 cells, isoform 4 is found first in the
CC       mitochondria and at later times, as neuronal differentiation
CC       proceeds, in the cytosol.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=P28661-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P28661-2; Sequence=VSP_038308;
CC       Name=3;
CC         IsoId=P28661-3; Sequence=VSP_038313, VSP_038314;
CC         Note=No experimental confirmation available;
CC       Name=4; Synonyms=Mitochindrial septin, M-septin;
CC         IsoId=P28661-4; Sequence=VSP_038309;
CC       Name=5;
CC         IsoId=P28661-5; Sequence=VSP_038307, VSP_038310, VSP_038313,
CC                                  VSP_038314;
CC         Note=No experimental confirmation available;
CC       Name=6;
CC         IsoId=P28661-6; Sequence=VSP_038308, VSP_038311, VSP_038312;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in the brain. Abundant in areas of
CC       high cell density, particularly in the stria terminalis. Isoform 4
CC       is predominantly expressed in embryonic mouse brain and dorsal
CC       root ganglion neurons.
CC   -!- DEVELOPMENTAL STAGE: Widely expressed in embryos at 7 dpc. Isoform
CC       4 predominantly expressed in the brain at 14 dpc and on postnatal
CC       day 1.
CC   -!- SIMILARITY: Belongs to the septin family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X61452; CAA43692.1; -; mRNA.
DR   EMBL; AB078010; BAC55241.1; -; mRNA.
DR   EMBL; AK133933; BAE21934.1; -; mRNA.
DR   EMBL; AK135143; BAE22437.1; -; mRNA.
DR   EMBL; AK137299; BAE23298.1; -; mRNA.
DR   EMBL; AL596086; CAI35128.2; -; Genomic_DNA.
DR   EMBL; AL596086; CAI35129.1; -; Genomic_DNA.
DR   EMBL; AL596086; CAI35132.1; -; Genomic_DNA.
DR   EMBL; AL596086; CAI35133.1; -; Genomic_DNA.
DR   EMBL; AL596086; CAI35134.1; -; Genomic_DNA.
DR   EMBL; CU406988; CAQ52271.1; -; Genomic_DNA.
DR   EMBL; CU406988; CAQ52272.1; -; Genomic_DNA.
DR   EMBL; CU406988; CAQ52274.1; -; Genomic_DNA.
DR   EMBL; CU406988; CAQ52275.1; -; Genomic_DNA.
DR   EMBL; CU406988; CAQ52276.1; -; Genomic_DNA.
DR   EMBL; CH466556; EDL15822.1; -; Genomic_DNA.
DR   EMBL; BC055101; AAH55101.1; -; mRNA.
DR   IPI; IPI00123219; -.
DR   IPI; IPI00341299; -.
DR   IPI; IPI00551370; -.
DR   IPI; IPI00648822; -.
DR   IPI; IPI00649441; -.
DR   IPI; IPI00649730; -.
DR   PIR; S16867; S16867.
DR   RefSeq; NP_035259.1; NM_011129.1.
DR   UniGene; Mm.2214; -.
DR   ProteinModelPortal; P28661; -.
DR   SMR; P28661; 141-410.
DR   STRING; P28661; -.
DR   PhosphoSite; P28661; -.
DR   PRIDE; P28661; -.
DR   Ensembl; ENSMUST00000018544; ENSMUSP00000018544; ENSMUSG00000020486.
DR   GeneID; 18952; -.
DR   KEGG; mmu:18952; -.
DR   UCSC; uc007ktw.1; mouse.
DR   CTD; 18952; -.
DR   MGI; MGI:1270156; Sept4.
DR   eggNOG; roNOG14189; -.
DR   GeneTree; ENSGT00590000082878; -.
DR   HOVERGEN; HBG065093; -.
DR   OMA; GNESCHP; -.
DR   PhylomeDB; P28661; -.
DR   NextBio; 295304; -.
DR   ArrayExpress; P28661; -.
DR   Bgee; P28661; -.
DR   CleanEx; MM_SEPT4; -.
DR   Genevestigator; P28661; -.
DR   GermOnline; ENSMUSG00000020486; Mus musculus.
DR   GO; GO:0009434; C:microtubule-based flagellum; IMP:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0031105; C:septin complex; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007420; P:brain development; IMP:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0048240; P:sperm capacitation; IMP:MGI.
DR   GO; GO:0030382; P:sperm mitochondrion organization; IMP:MGI.
DR   InterPro; IPR000038; Cell_Div_GTP-bd.
DR   InterPro; IPR016491; Septin.
DR   PANTHER; PTHR18884; Cell_Div_GTP_bd; 1.
DR   Pfam; PF00735; Septin; 1.
DR   PIRSF; PIRSF006698; Septin; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Cell division; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding;
KW   Mitochondrion; Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1    478       Septin-4.
FT                                /FTId=PRO_0000173520.
FT   NP_BIND     151    158       GTP (By similarity).
FT   NP_BIND     290    298       GTP (By similarity).
FT   COILED      447    478       Potential.
FT   BINDING     185    185       GTP (By similarity).
FT   BINDING     211    211       GTP; via amide nitrogen (By similarity).
FT   BINDING     348    348       GTP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     363    363       GTP (By similarity).
FT   MOD_RES      68     68       Phosphoserine.
FT   MOD_RES     325    325       Phosphoserine.
FT   VAR_SEQ       1    118       Missing (in isoform 5).
FT                                /FTId=VSP_038307.
FT   VAR_SEQ       1     20       MDHSLGWQGNSVPEDGTEAG -> M (in isoform 2
FT                                and isoform 6).
FT                                /FTId=VSP_038308.
FT   VAR_SEQ      21    119       Missing (in isoform 4).
FT                                /FTId=VSP_038309.
FT   VAR_SEQ     119    119       E -> M (in isoform 5).
FT                                /FTId=VSP_038310.
FT   VAR_SEQ     221    223       CWK -> WYV (in isoform 6).
FT                                /FTId=VSP_038311.
FT   VAR_SEQ     224    478       Missing (in isoform 6).
FT                                /FTId=VSP_038312.
FT   VAR_SEQ     426    431       NKLTRE -> KDRSRN (in isoform 3 and
FT                                isoform 5).
FT                                /FTId=VSP_038313.
FT   VAR_SEQ     432    478       Missing (in isoform 3 and isoform 5).
FT                                /FTId=VSP_038314.
FT   CONFLICT    394    394       D -> N (in Ref. 3; BAE21934).
SQ   SEQUENCE   478 AA;  54936 MW;  36655DE54A6C4908 CRC64;
     MDHSLGWQGN SVPEDGTEAG IKHFLEDSSD DAELSKFVKD FPGSEPYHSA ESKTRVARPQ
     ILEPRPQSPD LCDDDVEFRG SLWPQPSDSQ QYFSAPAPLS PSSRPRSPWG KLDPYDSSED
     DKEYVGFATL PNQVHRKSVK KGFDFTLMVA GESGLGKSTL VNSLFLTDLY RDRKLLGAEE
     RIMQTVEITK HAVDIEEKGV RLRLTIVDTP GFGDAVNNTE CWKPVAEYID QQFEQYFRDE
     SGLNRKNIQD NRVHCCLYFI SPFGHGLRPL DVEFMKALHQ RVNIVPILAK ADTLTPPEVD
     RKKCKIREEI EHFGIKIYQF PDCDSDEDED FKLQDQALKE SIPFAVIGSN TVVEARGRRV
     RGRLYPWGIV EVENPGHCDF VKLRTMLVRT HMQDLKDVTR ETHYENYRAQ CIQSMTRLVV
     KERNRNKLTR ESGTDFPIPA VPPGTDPETE KLIREKDEEL RRMQEMLHKI QRQMKETH
//
ID   SNAB_MOUSE              Reviewed;         298 AA.
AC   P28663;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Beta-soluble NSF attachment protein;
DE            Short=SNAP-beta;
DE   AltName: Full=Brain protein I47;
DE   AltName: Full=N-ethylmaleimide-sensitive factor attachment protein beta;
GN   Name=Napb; Synonyms=Snapb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 52-298.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   PubMed=12106288; DOI=10.1111/j.1460-9568.1990.tb00460.x;
RA   Kato K.;
RT   "A collection of cDNA clones with specific expression patterns in
RT   mouse brain.";
RL   Eur. J. Neurosci. 2:704-711(1990).
RN   [4]
RP   PROTEIN SEQUENCE OF 123-140; 209-222 AND 228-239, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [5]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=93205122; PubMed=8455721; DOI=10.1038/362353a0;
RA   Whiteheart S.W., Griff I.C., Brunner M., Clary D.O., Mayer T.,
RA   Buhrow S.A., Rothman J.E.;
RT   "SNAP family of NSF attachment proteins includes a brain-specific
RT   isoform.";
RL   Nature 362:353-355(1993).
CC   -!- FUNCTION: Required for vesicular transport between the endoplasmic
CC       reticulum and the Golgi apparatus.
CC   -!- SUBUNIT: Interacts with PRKCABP, and disrupts the interaction
CC       between GRIA2 and PRKCABP, leading to the internalization of GRIA2
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC   -!- TISSUE SPECIFICITY: Cerebral cortex, cerebellar cortex,
CC       hippocampus, and dentate gyrus, weakly expressed in the putamen,
CC       the thalamus and the brain stem.
CC   -!- SIMILARITY: Belongs to the SNAP family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK083184; BAC38798.1; -; mRNA.
DR   EMBL; BC038362; AAH38362.1; -; mRNA.
DR   EMBL; BC049874; AAH49874.1; -; mRNA.
DR   EMBL; X61455; CAA43695.1; -; mRNA.
DR   IPI; IPI00311515; -.
DR   PIR; S16869; S16869.
DR   RefSeq; NP_062606.1; NM_019632.3.
DR   UniGene; Mm.274308; -.
DR   UniGene; Mm.391579; -.
DR   ProteinModelPortal; P28663; -.
DR   SMR; P28663; 9-293.
DR   STRING; P28663; -.
DR   PhosphoSite; P28663; -.
DR   PRIDE; P28663; -.
DR   Ensembl; ENSMUST00000028926; ENSMUSP00000028926; ENSMUSG00000027438.
DR   GeneID; 17957; -.
DR   KEGG; mmu:17957; -.
DR   UCSC; uc008mti.1; mouse.
DR   CTD; 17957; -.
DR   MGI; MGI:104562; Napb.
DR   GeneTree; ENSGT00390000005826; -.
DR   HOGENOM; HBG397841; -.
DR   HOVERGEN; HBG001325; -.
DR   InParanoid; P28663; -.
DR   OMA; GNTRVEE; -.
DR   OrthoDB; EOG428227; -.
DR   PhylomeDB; P28663; -.
DR   NextBio; 292879; -.
DR   ArrayExpress; P28663; -.
DR   Bgee; P28663; -.
DR   Genevestigator; P28663; -.
DR   GermOnline; ENSMUSG00000027438; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:InterPro.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019905; F:syntaxin binding; IDA:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000744; NSF_attach.
DR   InterPro; IPR011990; TPR-like_helical.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
DR   PANTHER; PTHR13768; NSF_attach; 1.
DR   PRINTS; PR00448; NSFATTACHMNT.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; ER-Golgi transport; Membrane;
KW   Protein transport; Transport.
FT   CHAIN         1    298       Beta-soluble NSF attachment protein.
FT                                /FTId=PRO_0000219061.
FT   MOD_RES     203    203       N6-acetyllysine (By similarity).
SQ   SEQUENCE   298 AA;  33557 MW;  5B7BE0FB84BABD83 CRC64;
     MDNAGKEREA VQLMAEAEKR VKASHSFLRG LFGGNTRIEE ACEMYTRAAN MFKMAKNWSA
     AGNAFCQAAK LHMQLQSKHD SATSFVDAGN AYKKADPQEA INCLNAAIDI YTDMGRFTIA
     AKHHITIAEI YETELVDIEK AIAHYEQSAD YYKGEESNSS ANKCLLKVAA YAAQLEQYQK
     AIEIYEQVGA NTMDNPLLKY SAKDYFFKAA LCHFIVDELN AKLALEKYEE MFPAFTDSRE
     CKLLKKLLEA HEEQNSEAYT EAVKEFDSIS RLDQWLTTML LRIKKSIQGD GEGDGDLK
//
ID   MRP_MOUSE               Reviewed;         200 AA.
AC   P28667; Q3TEZ4; Q91W07;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=MARCKS-related protein;
DE   AltName: Full=Brain protein F52;
DE   AltName: Full=MARCKS-like protein 1;
DE   AltName: Full=Macrophage myristoylated alanine-rich C kinase substrate;
DE            Short=Mac-MARCKS;
DE            Short=MacMARCKS;
GN   Name=Marcksl1; Synonyms=Mlp, Mrp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=91323504; PubMed=1864362; DOI=10.1016/0014-5793(91)80961-2;
RA   Umekage T., Kato K.;
RT   "A mouse brain cDNA encodes a novel protein with the protein kinase C
RT   phosphorylation site domain common to MARCKS.";
RL   FEBS Lett. 286:147-151(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=92386598; PubMed=1516135; DOI=10.1016/0092-8674(92)90312-Z;
RA   Li J., Aderem A.;
RT   "MacMARCKS, a novel member of the MARCKS family of protein kinase C
RT   substrates.";
RL   Cell 70:791-801(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=94010885; PubMed=8406449; DOI=10.1006/geno.1993.1301;
RA   Lobach D.F., Rochelle J.M., Watson M.L., Seldin M.F., Blackshear P.J.;
RT   "Nucleotide sequence, expression, and chromosomal mapping of Mrp and
RT   mapping of five related sequences.";
RL   Genomics 17:194-204(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow, Cerebellum, Kidney, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NMRI; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   CHARACTERIZATION.
RX   MEDLINE=92317080; PubMed=1618855;
RA   Blackshear P.J., Verghese G.M., Johnson J.D., Haupt D.M., Stumpo D.J.;
RT   "Characteristics of the F52 protein, a MARCKS homologue.";
RL   J. Biol. Chem. 267:13540-13546(1992).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-48; SER-71;
RP   SER-120; SER-135; THR-148; SER-162; SER-165; THR-170; THR-183; SER-185
RP   AND THR-192, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-85, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-36; THR-85 AND
RP   SER-104, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May be involved in coupling the protein kinase C and
CC       calmodulin signal transduction systems.
CC   -!- TISSUE SPECIFICITY: Brain (mostly in dentate gyrus, anterior
CC       olfactory nucleus, primary olfactory cortex, entorhinal cortex,
CC       medial preoptic area, and dorsomedial hypothalamic nucleus).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the MARCKS family.
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DR   EMBL; X61399; CAA43671.1; -; mRNA.
DR   EMBL; S65597; AAP13962.1; -; Genomic_DNA.
DR   EMBL; AK079390; BAC37630.1; -; mRNA.
DR   EMBL; AK083913; BAC39058.1; -; mRNA.
DR   EMBL; AK152990; BAE31636.1; -; mRNA.
DR   EMBL; AK169355; BAE41104.1; -; mRNA.
DR   EMBL; BC006757; AAH06757.1; -; mRNA.
DR   IPI; IPI00281011; -.
DR   PIR; S17185; S17185.
DR   RefSeq; NP_034937.1; NM_010807.4.
DR   UniGene; Mm.424974; -.
DR   ProteinModelPortal; P28667; -.
DR   STRING; P28667; -.
DR   PhosphoSite; P28667; -.
DR   PRIDE; P28667; -.
DR   Ensembl; ENSMUST00000062356; ENSMUSP00000055637; ENSMUSG00000047945.
DR   GeneID; 17357; -.
DR   KEGG; mmu:17357; -.
DR   UCSC; uc008uxf.1; mouse.
DR   CTD; 17357; -.
DR   MGI; MGI:97143; Marcksl1.
DR   eggNOG; roNOG16568; -.
DR   GeneTree; ENSGT00530000063911; -.
DR   HOGENOM; HBG126341; -.
DR   HOVERGEN; HBG003515; -.
DR   InParanoid; P28667; -.
DR   OMA; ACSEEGT; -.
DR   OrthoDB; EOG4TB4CR; -.
DR   PhylomeDB; P28667; -.
DR   NextBio; 291970; -.
DR   PMAP-CutDB; P28667; -.
DR   ArrayExpress; P28667; -.
DR   Bgee; P28667; -.
DR   CleanEx; MM_MARCKSL1; -.
DR   Genevestigator; P28667; -.
DR   GermOnline; ENSMUSG00000047945; Mus musculus.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
DR   InterPro; IPR002101; MARCKS.
DR   PANTHER; PTHR14353; MARCKS; 1.
DR   Pfam; PF02063; MARCKS; 2.
DR   PRINTS; PR00963; MARCKS.
DR   PROSITE; PS00826; MARCKS_1; 1.
DR   PROSITE; PS00827; MARCKS_2; 1.
PE   1: Evidence at protein level;
KW   Calmodulin-binding; Lipoprotein; Myristate; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    200       MARCKS-related protein.
FT                                /FTId=PRO_0000157153.
FT   REGION       87    100       Calmodulin-binding (PSD).
FT   MOD_RES      14     14       Phosphothreonine (By similarity).
FT   MOD_RES      22     22       Phosphoserine.
FT   MOD_RES      36     36       Phosphoserine.
FT   MOD_RES      48     48       Phosphoserine.
FT   MOD_RES      71     71       Phosphoserine.
FT   MOD_RES      85     85       Phosphothreonine.
FT   MOD_RES      93     93       Phosphoserine; by PKC (By similarity).
FT   MOD_RES     101    101       Phosphoserine; by PKC (By similarity).
FT   MOD_RES     104    104       Phosphoserine; by PKC.
FT   MOD_RES     116    116       Phosphoserine (By similarity).
FT   MOD_RES     117    117       Phosphoserine (By similarity).
FT   MOD_RES     119    119       Phosphoserine (By similarity).
FT   MOD_RES     120    120       Phosphoserine.
FT   MOD_RES     122    122       Phosphothreonine (By similarity).
FT   MOD_RES     135    135       Phosphoserine.
FT   MOD_RES     148    148       Phosphothreonine.
FT   MOD_RES     151    151       Phosphoserine (By similarity).
FT   MOD_RES     162    162       Phosphoserine.
FT   MOD_RES     165    165       Phosphoserine.
FT   MOD_RES     170    170       Phosphothreonine.
FT   MOD_RES     182    182       Phosphoserine (By similarity).
FT   MOD_RES     183    183       Phosphothreonine.
FT   MOD_RES     185    185       Phosphoserine.
FT   MOD_RES     189    189       Phosphoserine (By similarity).
FT   MOD_RES     192    192       Phosphothreonine.
FT   LIPID         2      2       N-myristoyl glycine.
FT   CONFLICT    134    134       C -> S (in Ref. 5; AAH06757).
SQ   SEQUENCE   200 AA;  20165 MW;  AA50A0E2029921AF CRC64;
     MGSQSSKAPR GDVTAEEAAG ASPAKANGQE NGHVRSNGDL TPKGEGESPP VNGTDEAAGA
     TGDAIEPAPP SQEAEAKGEV APKETPKKKK KFSFKKPFKL SGLSFKRNRK EGGGDSSASS
     PTEEEQEQGE MSACSDEGTA QEGKAAATPE SQEPQAKGAE ASAASKEGDT EEEAGPQAAE
     PSTPSGPESG PTPASAEQNE
//
ID   KPCD_MOUSE              Reviewed;         674 AA.
AC   P28867; Q91V85; Q9Z333;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 3.
DT   08-MAR-2011, entry version 119.
DE   RecName: Full=Protein kinase C delta type;
DE            EC=2.7.11.13;
DE   AltName: Full=nPKC-delta;
GN   Name=Prkcd; Synonyms=Pkcd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=91329364; PubMed=1868068; DOI=10.1021/bi00246a008;
RA   Mischak H., Bodenteich A., Kolch W., Goodnight J., Hofer F.,
RA   Mushinski J.F.;
RT   "Mouse protein kinase C-delta, the major isoform expressed in mouse
RT   hemopoietic cells: sequence of the cDNA, expression patterns, and
RT   characterization of the protein.";
RL   Biochemistry 30:7925-7931(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=92111544; PubMed=1765103;
RX   DOI=10.1111/j.1432-1033.1991.tb16453.x;
RA   Mizuno K., Kubo K., Saido T.C., Akita Y., Osada S., Kuroki T.,
RA   Ohno S., Suzuki K.;
RT   "Structure and properties of a ubiquitously expressed protein kinase
RT   C, nPKC delta.";
RL   Eur. J. Biochem. 202:931-940(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC   STRAIN=129/SvJ;
RA   Wheeler D.L., Gillis M.E., Verma A.K.;
RT   "Intron/exon structure of the murine protein kinase C delta gene.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   MEDLINE=21442254; PubMed=11558579; DOI=10.1248/bpb.24.973;
RA   Sakurai Y., Onishi Y., Tanimoto Y., Kizaki H.;
RT   "Novel protein kinase C delta isoform insensitive to caspase-3.";
RL   Biol. Pharm. Bull. 24:973-977(2001).
RN   [5]
RP   FUNCTION.
RX   MEDLINE=21973242; PubMed=11976686; DOI=10.1038/416860a;
RA   Mecklenbraeuker I., Saijo K., Zheng N.Y., Leitges M., Tarakhovsky A.;
RT   "Protein kinase Cdelta controls self-antigen-induced B-cell
RT   tolerance.";
RL   Nature 416:860-865(2002).
RN   [6]
RP   PHOSPHORYLATION AT THR-505.
RX   MEDLINE=98421571; PubMed=9748166; DOI=10.1126/science.281.5385.2042;
RA   Le Good J.A., Ziegler W.H., Parekh D.B., Alessi D.R., Cohen P.,
RA   Parker P.J.;
RT   "Protein kinase C isotypes controlled by phosphoinositide 3-kinase
RT   through the protein kinase PDK1.";
RL   Science 281:2042-2045(1998).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-311, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-311, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43; TYR-311 AND SER-662,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-311, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 231-280 IN COMPLEX WITH
RP   PHORBOL ESTER AND ZINC IONS.
RX   MEDLINE=95300223; PubMed=7781068; DOI=10.1016/0092-8674(95)90011-X;
RA   Zhang G., Kazanietz M.G., Blumberg P.M., Hurley J.H.;
RT   "Crystal structure of the cys2 activator-binding domain of protein
RT   kinase C delta in complex with phorbol ester.";
RL   Cell 81:917-924(1995).
CC   -!- FUNCTION: This is calcium-independent, phospholipid-dependent,
CC       serine- and threonine-specific enzyme. PKC is activated by
CC       diacylglycerol which in turn phosphorylates a range of cellular
CC       proteins. PKC also serves as the receptor for phorbol esters, a
CC       class of tumor promoters. May play a role in antigen-dependent
CC       control of B-cell function. Phosphorylates MUC1 in the C-terminal
CC       and regulates the interaction between MUC1 and beta-catenin (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Three specific sites; Thr-505 (activation loop
CC       of the kinase domain), Ser-643 (turn motif) and Ser-662
CC       (hydrophobic region), need to be phosphorylated for its full
CC       activation.
CC   -!- SUBUNIT: Interacts with RAD9A, CDCP1, PDK1 and MUC1 (By
CC       similarity).
CC   -!- INTERACTION:
CC       Q8WV44-2:TRIM41 (xeno); NbExp=1; IntAct=EBI-1551324, EBI-726015;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane;
CC       Peripheral membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=PKC-delta-I;
CC         IsoId=P28867-1; Sequence=Displayed;
CC       Name=2; Synonyms=PKC-delta-II;
CC         IsoId=P28867-2; Sequence=VSP_004741;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is highly expressed in developing
CC       pro- and pre-B-cells and moderately in mature T-cells. Isoform 2
CC       is highly expressed in testis and ovary and at a lower level in
CC       thymocytes, brain and kidney.
CC   -!- DOMAIN: The C1 domain, containing the phorbol ester/DAG-type
CC       region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor.
CC   -!- DOMAIN: The C2 domain is a non-calcium binding domain. It binds
CC       proteins containing phosphotyrosine in a sequence-specific manner
CC       (By similarity).
CC   -!- PTM: Phosphorylated on residue Thr-505, within the activation
CC       loop. Autophosphorylated and/or phosphorylated. Although the Thr-
CC       505 phosphorylation occurs it is not a prerequisite for enzymatic
CC       activity (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. PKC subfamily.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 2 phorbol-ester/DAG-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; M69042; AAA73056.1; -; mRNA.
DR   EMBL; X60304; CAA42845.1; -; mRNA.
DR   EMBL; AF274044; AAF79208.1; -; Genomic_DNA.
DR   EMBL; AF251036; AAF64316.1; -; mRNA.
DR   EMBL; AB011812; BAA36408.1; -; mRNA.
DR   IPI; IPI00125855; -.
DR   IPI; IPI00227880; -.
DR   PIR; A40281; KIMSCD.
DR   RefSeq; NP_035233.1; NM_011103.2.
DR   UniGene; Mm.2314; -.
DR   PDB; 1PTQ; X-ray; 1.95 A; A=231-280.
DR   PDB; 1PTR; X-ray; 2.20 A; A=231-280.
DR   PDBsum; 1PTQ; -.
DR   PDBsum; 1PTR; -.
DR   ProteinModelPortal; P28867; -.
DR   SMR; P28867; 1-123, 149-218, 231-280, 344-666.
DR   DIP; DIP-1169N; -.
DR   IntAct; P28867; 3.
DR   MINT; MINT-97906; -.
DR   STRING; P28867; -.
DR   PhosphoSite; P28867; -.
DR   PRIDE; P28867; -.
DR   Ensembl; ENSMUST00000112208; ENSMUSP00000107827; ENSMUSG00000021948.
DR   Ensembl; ENSMUST00000112210; ENSMUSP00000107829; ENSMUSG00000021948.
DR   Ensembl; ENSMUST00000112211; ENSMUSP00000107830; ENSMUSG00000021948.
DR   GeneID; 18753; -.
DR   KEGG; mmu:18753; -.
DR   UCSC; uc007svf.1; mouse.
DR   UCSC; uc007svg.1; mouse.
DR   CTD; 18753; -.
DR   MGI; MGI:97598; Prkcd.
DR   eggNOG; roNOG14957; -.
DR   HOVERGEN; HBG108317; -.
DR   OMA; RCTGTAT; -.
DR   OrthoDB; EOG4M91QX; -.
DR   PhylomeDB; P28867; -.
DR   BRENDA; 2.7.11.13; 244.
DR   NextBio; 294929; -.
DR   ArrayExpress; P28867; -.
DR   Bgee; P28867; -.
DR   CleanEx; MM_PRKCD; -.
DR   Genevestigator; P28867; -.
DR   GermOnline; ENSMUSG00000021948; Mus musculus.
DR   GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0016363; C:nuclear matrix; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043560; F:insulin receptor substrate binding; IPI:BHF-UCL.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004697; F:protein kinase C activity; IEA:EC.
DR   GO; GO:0042100; P:B cell proliferation; IMP:MGI.
DR   GO; GO:0016064; P:immunoglobulin mediated immune response; IMP:MGI.
DR   GO; GO:0032613; P:interleukin-10 production; IMP:MGI.
DR   GO; GO:0032615; P:interleukin-12 production; IMP:MGI.
DR   GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR014376; Prot_kin_PKC_delta.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   PIRSF; PIRSF000551; PKC_delta; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50004; C2; FALSE_NEG.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Kinase;
KW   Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Repeat;
KW   Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    674       Protein kinase C delta type.
FT                                /FTId=PRO_0000055695.
FT   DOMAIN        1     90       C2.
FT   DOMAIN      347    601       Protein kinase.
FT   DOMAIN      602    673       AGC-kinase C-terminal.
FT   ZN_FING     158    208       Phorbol-ester/DAG-type 1.
FT   ZN_FING     230    280       Phorbol-ester/DAG-type 2.
FT   NP_BIND     353    361       ATP (By similarity).
FT   ACT_SITE    471    471       Proton acceptor (By similarity).
FT   BINDING     376    376       ATP (By similarity).
FT   SITE         48     48       Interaction with phosphotyrosine-
FT                                containing peptide (By similarity).
FT   SITE         62     62       Interaction with phosphotyrosine-
FT                                containing peptide (By similarity).
FT   SITE         67     67       Interaction with phosphotyrosine-
FT                                containing peptide (By similarity).
FT   SITE        123    123       Interaction with phosphotyrosine-
FT                                containing peptide (By similarity).
FT   MOD_RES      43     43       Phosphothreonine.
FT   MOD_RES      50     50       Phosphothreonine (By similarity).
FT   MOD_RES     130    130       Phosphoserine (By similarity).
FT   MOD_RES     218    218       Phosphothreonine (By similarity).
FT   MOD_RES     295    295       Phosphothreonine (By similarity).
FT   MOD_RES     299    299       Phosphoserine (By similarity).
FT   MOD_RES     311    311       Phosphotyrosine.
FT   MOD_RES     332    332       Phosphotyrosine (By similarity).
FT   MOD_RES     372    372       Phosphotyrosine (By similarity).
FT   MOD_RES     504    504       Phosphoserine (By similarity).
FT   MOD_RES     505    505       Phosphothreonine; by PDPK1 (By
FT                                similarity).
FT   MOD_RES     643    643       Phosphoserine (Probable).
FT   MOD_RES     645    645       Phosphoserine (By similarity).
FT   MOD_RES     652    652       Phosphoserine (By similarity).
FT   MOD_RES     662    662       Phosphoserine.
FT   VAR_SEQ     326    326       L -> LGEAGSHISLKLSFPSRAKEKDSSETC (in
FT                                isoform 2).
FT                                /FTId=VSP_004741.
FT   CONFLICT    214    214       N -> I (in Ref. 4; BAA36408).
FT   CONFLICT    226    226       N -> S (in Ref. 4; BAA36408).
FT   CONFLICT    319    319       E -> D (in Ref. 1; AAA73056).
FT   CONFLICT    330    330       G -> W (in Ref. 1; AAA73056).
FT   CONFLICT    337    337       E -> V (in Ref. 1; AAA73056).
FT   CONFLICT    501    501       G -> D (in Ref. 1; AAA73056).
FT   CONFLICT    503    503       A -> P (in Ref. 1; AAA73056).
FT   CONFLICT    513    513       I -> S (in Ref. 1; AAA73056).
FT   CONFLICT    518    520       LQG -> PARA (in Ref. 4; BAA36408).
FT   CONFLICT    538    538       E -> R (in Ref. 4; BAA36408).
FT   STRAND      233    236
FT   TURN        245    247
FT   STRAND      253    256
FT   STRAND      258    261
FT   TURN        262    264
FT   HELIX       270    275
SQ   SEQUENCE   674 AA;  77547 MW;  6E9F753348F03D59 CRC64;
     MAPFLRISFN SYELGSLQVE DEASQPFCAV KMKEALSTER GKTLVQKKPT MYPEWKTTFD
     AHIYEGRVIQ IVLMRAAEDP VSEVTVGVSV LAERCKKNNG KAEFWLDLQP QAKVLMCVQY
     FLEDGDCKQS MRSEEEAKFP TMNRRGAIKQ AKIHYIKNHE FIATFFGQPT FCSVCKEFVW
     GLNKQGYKCR QCNAAIHKKC IDKIIGRCTG TATNSRDTIF QKERFNIDMP HRFKVYNYMS
     PTFCDHCGSL LWGLVKQGLK CEDCGMNVHH KCREKVANLC GINQKLLAEA LNQVTQRSSR
     KLDTTESVGI YQGFEKKPEV SGSDILDNNG TYGKIWEGST RCTLENFTFQ KVLGKGSFGK
     VLLAELKGKD KYFAIKCLKK DVVLIDDDVE CTMVEKRVLA LAWESPFLTH LICTFQTKDH
     LFFVMEFLNG GDLMFHIQDK GRFELYRATF YAAEIICGLQ FLHSKGIIYR DLKLDNVMLD
     RDGHIKIADF GMCKENIFGE GRASTFCGTP DYIAPEILQG LKYSFSVDWW SFGVLLYEML
     IGQSPFHGDD EDELFESIRV DTPHYPRWIT KESKDIMEKL FERDPDKRLG VTGNIRIHPF
     FKTINWSLLE KRKVEPPFKP KVKSPSDYSN FDPEFLNEKP QLSFSDKNLI DSMDQEAFHG
     FSFVNPKFEQ FLDI
//
ID   PCSK4_MOUSE             Reviewed;         655 AA.
AC   P29121; Q62094;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Proprotein convertase subtilisin/kexin type 4;
DE            EC=3.4.21.-;
DE   AltName: Full=KEX2-like endoprotease 3;
DE   AltName: Full=Neuroendocrine convertase 3;
DE            Short=NEC 3;
DE   AltName: Full=Prohormone convertase 3;
DE   Flags: Precursor;
GN   Name=Pcsk4; Synonyms=Nec-3, Nec3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Testis;
RX   MEDLINE=92210552; PubMed=1372895;
RA   Nakayama K., Kim W.-S., Torii S., Hosaka M., Nakagawa T., Ikemizu J.,
RA   Baba T., Murakami K.;
RT   "Identification of the fourth member of the mammalian endoprotease
RT   family homologous to the yeast Kex2 protease. Its testis-specific
RT   expression.";
RL   J. Biol. Chem. 267:5897-5900(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4).
RC   TISSUE=Testis;
RX   MEDLINE=93078790; PubMed=1448111; DOI=10.1210/me.6.10.1559;
RA   Seidah N.G., Day R., Hamelin J., Gaspar A., Collard M.W., Chretien M.;
RT   "Testicular expression of PC4 in the rat: molecular diversity of a
RT   novel germ cell-specific Kex2/subtilisin-like proprotein convertase.";
RL   Mol. Endocrinol. 6:1559-1570(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 5; 6; 7 AND
RP   8).
RC   STRAIN=C57BL/6; TISSUE=Liver;
RX   MEDLINE=94292203; PubMed=8020970; DOI=10.1006/geno.1994.1158;
RA   Mbikay M., Raffin-Sanson M.-L., Tadros H., Sirois F., Seidah N.G.,
RA   Chretien M.;
RT   "Structure of the gene for the testis-specific proprotein convertase 4
RT   and of its alternate messenger RNA isoforms.";
RL   Genomics 20:231-237(1994).
CC   -!- FUNCTION: Involved in the processing of hormone and other protein
CC       precursors at sites comprised of pairs of basic amino acid
CC       residues.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC       Name=1; Synonyms=mPC4-A;
CC         IsoId=P29121-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P29121-2; Sequence=VSP_011268;
CC       Name=3; Synonyms=mPC4-B;
CC         IsoId=P29121-3; Sequence=VSP_011271;
CC       Name=4; Synonyms=mPC4-C;
CC         IsoId=P29121-4; Sequence=VSP_011272;
CC       Name=5; Synonyms=E;
CC         IsoId=P29121-5; Sequence=VSP_011266;
CC       Name=6; Synonyms=D;
CC         IsoId=P29121-6; Sequence=VSP_011267;
CC       Name=7; Synonyms=B;
CC         IsoId=P29121-7; Sequence=VSP_011269;
CC       Name=8; Synonyms=C;
CC         IsoId=P29121-8; Sequence=VSP_011270;
CC   -!- TISSUE SPECIFICITY: Expressed abundantly in the testis.
CC   -!- DEVELOPMENTAL STAGE: Detected only after the 20th day of postnatal
CC       development. Mainly expressed in the round spermatids. Expressed
CC       mainly in the early stages of spermiogenesis.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
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DR   EMBL; D01093; BAA00877.1; -; mRNA.
DR   EMBL; L21221; AAA39973.1; -; Genomic_DNA.
DR   EMBL; L21210; AAA39973.1; JOINED; Genomic_DNA.
DR   EMBL; L21211; AAA39973.1; JOINED; Genomic_DNA.
DR   EMBL; L21212; AAA39973.1; JOINED; Genomic_DNA.
DR   EMBL; L21213; AAA39973.1; JOINED; Genomic_DNA.
DR   EMBL; L21214; AAA39973.1; JOINED; Genomic_DNA.
DR   EMBL; L21215; AAA39973.1; JOINED; Genomic_DNA.
DR   EMBL; L21216; AAA39973.1; JOINED; Genomic_DNA.
DR   EMBL; L21217; AAA39973.1; JOINED; Genomic_DNA.
DR   EMBL; L21218; AAA39973.1; JOINED; Genomic_DNA.
DR   EMBL; L21219; AAA39973.1; JOINED; Genomic_DNA.
DR   EMBL; L21220; AAA39973.1; JOINED; Genomic_DNA.
DR   EMBL; L21222; AAA39973.1; JOINED; Genomic_DNA.
DR   EMBL; L21223; AAA39973.1; JOINED; Genomic_DNA.
DR   IPI; IPI00121742; -.
DR   IPI; IPI00407815; -.
DR   IPI; IPI00458863; -.
DR   IPI; IPI00458864; -.
DR   IPI; IPI00458865; -.
DR   IPI; IPI00458866; -.
DR   IPI; IPI00458867; -.
DR   IPI; IPI00458868; -.
DR   PIR; A54306; A54306.
DR   RefSeq; NP_032819.1; NM_008793.2.
DR   UniGene; Mm.299916; -.
DR   ProteinModelPortal; P29121; -.
DR   SMR; P29121; 31-103, 115-580.
DR   STRING; P29121; -.
DR   MEROPS; S08.074; -.
DR   PRIDE; P29121; -.
DR   Ensembl; ENSMUST00000020340; ENSMUSP00000020340; ENSMUSG00000020131.
DR   GeneID; 18551; -.
DR   KEGG; mmu:18551; -.
DR   UCSC; uc007gcs.1; mouse.
DR   CTD; 18551; -.
DR   MGI; MGI:97514; Pcsk4.
DR   eggNOG; roNOG12537; -.
DR   GeneTree; ENSGT00600000084064; -.
DR   HOGENOM; HBG715943; -.
DR   HOVERGEN; HBG008705; -.
DR   InParanoid; P29121; -.
DR   OMA; DMTARPQ; -.
DR   OrthoDB; EOG4K6G3R; -.
DR   PhylomeDB; P29121; -.
DR   NextBio; 294352; -.
DR   ArrayExpress; P29121; -.
DR   Bgee; P29121; -.
DR   CleanEx; MM_PCSK4; -.
DR   Genevestigator; P29121; -.
DR   GermOnline; ENSMUSG00000020131; Mus musculus.
DR   GO; GO:0002080; C:acrosomal membrane; IDA:MGI.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007340; P:acrosome reaction; IMP:MGI.
DR   GO; GO:0007339; P:binding of sperm to zona pellucida; IMP:MGI.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0048240; P:sperm capacitation; IMP:MGI.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR000209; Peptidase_S8/S53.
DR   InterPro; IPR022398; Peptidase_S8/S53_AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR009020; Prot_inh_propept.
DR   InterPro; IPR002884; PrprotnconvertsP.
DR   Gene3D; G3DSA:3.40.50.200; Pept_S8_S53; 1.
DR   PANTHER; PTHR10795; SubtilSerProt; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF49785; Gal_bind_like; 1.
DR   SUPFAM; SSF52743; Pept_S8_S53; 1.
DR   SUPFAM; SSF54897; Prot_inh_propept; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cleavage on pair of basic residues;
KW   Glycoprotein; Hydrolase; Protease; Serine protease; Signal; Zymogen.
FT   SIGNAL        1     26       By similarity.
FT   PROPEP       27    110       Potential.
FT                                /FTId=PRO_0000027098.
FT   CHAIN       111    655       Proprotein convertase subtilisin/kexin
FT                                type 4.
FT                                /FTId=PRO_0000027099.
FT   REGION      121    414       Catalytic.
FT   ACT_SITE    155    155       Charge relay system (By similarity).
FT   ACT_SITE    196    196       Charge relay system (By similarity).
FT   ACT_SITE    370    370       Charge relay system (By similarity).
FT   CARBOHYD    472    472       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ      22     60       Missing (in isoform 5).
FT                                /FTId=VSP_011266.
FT   VAR_SEQ      51     60       Missing (in isoform 6).
FT                                /FTId=VSP_011267.
FT   VAR_SEQ     273    282       Missing (in isoform 2).
FT                                /FTId=VSP_011268.
FT   VAR_SEQ     590    655       VTSRARACVQRDTEGLCQESHSPLSILAGLCLISSQQWWWL
FT                                YSHPQQPVTEGQASCHPPVTPAAAA -> KVTVPSPSWQDS
FT                                ASSPASSGGGSTATHSSQ (in isoform 3).
FT                                /FTId=VSP_011271.
FT   VAR_SEQ     590    655       VTSRARACVQRDTEGLCQESHSPLSILAGLCLISSQQWWWL
FT                                YSHPQQPVTEGQASCHPPVTPAAAA -> DSASSPASSGGG
FT                                STATHSSQ (in isoform 4).
FT                                /FTId=VSP_011272.
FT   VAR_SEQ     590    617       Missing (in isoform 8).
FT                                /FTId=VSP_011270.
FT   VAR_SEQ     590    608       Missing (in isoform 7).
FT                                /FTId=VSP_011269.
FT   CONFLICT     65     65       D -> N (in Ref. 3; AAA39973).
FT   CONFLICT     87     87       R -> P (in Ref. 3; AAA39973).
SQ   SEQUENCE   655 AA;  73214 MW;  4E4E32CEDECBCB59 CRC64;
     MRPSQTELWL GLTLTLALLA VRWASAQAPI YVSSWAVRVT KGYQEAERLA RKFGFVNLGQ
     IFPDDQYFHL RHRGVAQQSL TPHWGHRLRL KKDPKVRWFE QQTLRRRVKR SLVVPTDPWF
     SKQWYMNKEI QQDLNILKAW NQGLTGRGVV ISILDDGIEK DHPDLWANYD PLASYDFNDY
     DPDPQPRYTP NDENRHGTRC AGEVSATANN GFCGAGVAFN ARIGGVRMLD GAITDIVEAQ
     SLSLQPQHIH IYSASWGPED DGRTVDGPGL LTQEAFRRGV TKGRQGLGTL FIWASGNGGL
     HYDNCNCDGY TNSIHTLSVG STTRQGRVPW YSEACASTFT TTFSSGVVTD PQIVTTDLHH
     QCTDKHTGTS ASAPLAAGMI ALALEANPLL TWRDLQHLVV RASRPAQLQA EDWRINGVGR
     QVSHHYGYGL LDAGLLVDLA RVWLPTKPQK KCAIRVVHTP TPILPRMLVP KNVTACSDGS
     RRRLIRSLEH VQVQLSLSYS RRGDLEIFLT SPMGTRSTLV AIRPLDISGQ GYNNWIFMST
     HYWDEDPQGL WTLGLENKGY YFNTGTLYYY TLLLYGTAED MTARPQAPQV TSRARACVQR
     DTEGLCQESH SPLSILAGLC LISSQQWWWL YSHPQQPVTE GQASCHPPVT PAAAA
//
ID   PABP1_MOUSE             Reviewed;         636 AA.
AC   P29341;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   08-MAR-2011, entry version 109.
DE   RecName: Full=Polyadenylate-binding protein 1;
DE            Short=PABP-1;
DE            Short=Poly(A)-binding protein 1;
GN   Name=Pabpc1; Synonyms=Pabp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   MEDLINE=92335015; PubMed=1630930; DOI=10.1093/nar/20.13.3519;
RA   Wang M.-Y., Cutler M., Karimpour I., Kleene K.C.;
RT   "Nucleotide sequence of a mouse testis poly(A) binding protein cDNA.";
RL   Nucleic Acids Res. 20:3519-3519(1992).
RN   [2]
RP   IDENTIFICATION IN A MRNP COMPLEX WITH YBX2.
RX   PubMed=10076007; DOI=10.1093/nar/27.7.1747;
RA   Herbert T.P., Hecht N.B.;
RT   "The mouse Y-box protein, MSY2, is associated with a kinase on non-
RT   polysomal mouse testicular mRNAs.";
RL   Nucleic Acids Res. 27:1747-1753(1999).
RN   [3]
RP   INTERACTION WITH CSDE1.
RX   PubMed=15314026; DOI=10.1101/gad.1219104;
RA   Chang T.-C., Yamashita A., Chen C.-Y.A., Yamashita Y., Zhu W.,
RA   Durdan S., Kahvejian A., Sonenberg N., Shyu A.-B.;
RT   "UNR, a new partner of poly(A)-binding protein, plays a key role in
RT   translationally coupled mRNA turnover mediated by the c-fos major
RT   coding-region determinant.";
RL   Genes Dev. 18:2010-2023(2004).
RN   [4]
RP   INTERACTION WITH PAPD4.
RX   PubMed=17927953; DOI=10.1016/j.bbrc.2007.09.096;
RA   Nakanishi T., Kumagai S., Kimura M., Watanabe H., Sakurai T.,
RA   Kimura M., Kashiwabara S., Baba T.;
RT   "Disruption of mouse poly(A) polymerase mGLD-2 does not alter
RT   polyadenylation status in oocytes and somatic cells.";
RL   Biochem. Biophys. Res. Commun. 364:14-19(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-116, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [6]
RP   INTERACTION WITH PIWIL1.
RX   PubMed=19020299; DOI=10.1095/biolreprod.108.072553;
RA   Kimura M., Ishida K., Kashiwabara S., Baba T.;
RT   "Characterization of two cytoplasmic poly(A)-binding proteins, PABPC1
RT   and PABPC2, in mouse spermatogenic cells.";
RL   Biol. Reprod. 80:545-554(2009).
CC   -!- FUNCTION: Binds the poly(A) tail of mRNA. May be involved in
CC       cytoplasmic regulatory processes of mRNA metabolism such as pre-
CC       mRNA splicing. Its function in translational initiation regulation
CC       can either be enhanced by PAIP1 or repressed by PAIP2. Can
CC       probably bind to cytoplasmic RNA sequences other than poly(A) in
CC       vivo. May be involved in translationally coupled mRNA turnover.
CC       Implicated with other RNA-binding proteins in the cytoplasmic
CC       deadenylation/translational and decay interplay of the FOS mRNA
CC       mediated by the major coding-region determinant of instability
CC       (mCRD) domain (By similarity).
CC   -!- SUBUNIT: Component of a multi subunit autoregulatory
CC       ribonucleoprotein complex (ARC), at least composed of IGF2BP1,
CC       PABPC1 and CSDE1. Identified in a mRNP complex, at least composed
CC       of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2,
CC       PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Identified in a mRNP
CC       granule complex, at least composed of ACTB, ACTN4, DHX9, ERG,
CC       HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU,
CC       HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4,
CC       PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2,
CC       YBX1 and untranslated mRNAs. Interacts with IGF2BP1 (By
CC       similarity). Part of a complex associated with the FOS mCRD domain
CC       and consisting of HNRPD, SYNCRIP, PAIP1 and CSDE1/UNR. Interacts
CC       with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1
CC       and PAIP2. Interacts with PAIP1 with a 1:1 stoichiometry and with
CC       PAIP2 with a 1:2 stoichiometry. Identified in the spliceosome C
CC       complex, at least composed of AQR, ASCC3L1, C19orf29, CDC40,
CC       CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38,
CC       DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC,
CC       HNRPF, HNRPH1, HNRPK, HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604,
CC       LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3,
CC       PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX,
CC       SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2,
CC       SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF,
CC       SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1,
CC       WDR57, XAB2 and ZCCHC8. Interacts with NFX1 (By similarity). The
CC       interaction with CSDE1 is direct and RNA-independent. Found in a
CC       mRNP complex with YBX2. Interacts with PAPD4/GLD2 and PIWIL1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Localized in cytoplasmic mRNP granules
CC       containing untranslated mRNAs. Shuttles between the cytoplasm and
CC       the nucleus (By similarity).
CC   -!- DOMAIN: The RNA-binding domains RRM1 and RRM2 and the C-terminus
CC       (last 138 amino acids) regions interact respectively with the
CC       PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1,
CC       respectively (By similarity).
CC   -!- DOMAIN: The RNA-binding domains RRM2 and RRM3 and the C-terminus
CC       (last 138 amino acids) regions interact with the PABPC1-
CC       interacting motif-1 (PAM1) and -2 (PAM2) of PAIP2, respectively
CC       (By similarity).
CC   -!- PTM: Methylated by CARM1 (By similarity).
CC   -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1
CC       family.
CC   -!- SIMILARITY: Contains 1 PABC domain.
CC   -!- SIMILARITY: Contains 4 RRM (RNA recognition motif) domains.
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DR   EMBL; X65553; CAA46522.1; -; mRNA.
DR   IPI; IPI00124287; -.
DR   PIR; I48718; I48718.
DR   UniGene; Mm.371570; -.
DR   ProteinModelPortal; P29341; -.
DR   SMR; P29341; 11-376, 494-636.
DR   DIP; DIP-32127N; -.
DR   STRING; P29341; -.
DR   PhosphoSite; P29341; -.
DR   REPRODUCTION-2DPAGE; P29341; -.
DR   PRIDE; P29341; -.
DR   Ensembl; ENSMUST00000001809; ENSMUSP00000001809; ENSMUSG00000022283.
DR   MGI; MGI:1349722; Pabpc1.
DR   eggNOG; roNOG05108; -.
DR   HOGENOM; HBG756718; -.
DR   HOVERGEN; HBG002295; -.
DR   InParanoid; P29341; -.
DR   OrthoDB; EOG40ZQX5; -.
DR   PhylomeDB; P29341; -.
DR   ArrayExpress; P29341; -.
DR   Bgee; P29341; -.
DR   CleanEx; MM_PABPC1; -.
DR   Genevestigator; P29341; -.
DR   GermOnline; ENSMUSG00000022283; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0008143; F:poly(A) RNA binding; ISS:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR006515; PABP_1234.
DR   InterPro; IPR002004; PABP_HYD.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 4.
DR   Gene3D; G3DSA:1.10.1900.10; PABP_HYD; 1.
DR   Pfam; PF00658; PABP; 1.
DR   Pfam; PF00076; RRM_1; 4.
DR   SMART; SM00517; PolyA; 1.
DR   SMART; SM00360; RRM; 4.
DR   SUPFAM; SSF63570; PABP_HYD; 1.
DR   TIGRFAMs; TIGR01628; PABP-1234; 1.
DR   PROSITE; PS51309; PABC; 1.
DR   PROSITE; PS50102; RRM; 4.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Methylation; mRNA processing; mRNA splicing;
KW   Nucleus; Phosphoprotein; Repeat; RNA-binding; Spliceosome.
FT   CHAIN         1    636       Polyadenylate-binding protein 1.
FT                                /FTId=PRO_0000081699.
FT   DOMAIN       11     89       RRM 1.
FT   DOMAIN       99    175       RRM 2.
FT   DOMAIN      191    268       RRM 3.
FT   DOMAIN      294    370       RRM 4.
FT   DOMAIN      542    619       PABC.
FT   REGION      166    289       CSDE1-binding (By similarity).
FT   COMPBIAS    495    501       Poly-Ala.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      96     96       Phosphoserine (By similarity).
FT   MOD_RES     116    116       Phosphotyrosine.
FT   MOD_RES     299    299       N6-methyllysine (By similarity).
FT   MOD_RES     315    315       Phosphoserine (By similarity).
FT   MOD_RES     319    319       Phosphothreonine (By similarity).
FT   MOD_RES     342    342       Phosphoserine (By similarity).
FT   MOD_RES     364    364       Phosphotyrosine (By similarity).
FT   MOD_RES     455    455       Omega-N-methylated arginine; by CARM1 (By
FT                                similarity).
FT   MOD_RES     460    460       Omega-N-methylated arginine; by CARM1 (By
FT                                similarity).
FT   MOD_RES     493    493       Dimethylated arginine; alternate (By
FT                                similarity).
FT   MOD_RES     493    493       Omega-N-methylarginine; alternate (By
FT                                similarity).
FT   MOD_RES     512    512       N6-acetyllysine (By similarity).
SQ   SEQUENCE   636 AA;  70643 MW;  8876B3E99675FD49 CRC64;
     MNPSAPSYPM ASLYVGDLHP DVTEAMLYEK FSPAGPILSI RVCRDMITRR SLGYAYVNFQ
     QPADAERALD TMNFDVIKGK PVRIMWSQRD PSLRKSGVGN IFIKNLDKSI DNKALYDTFS
     AFGNILSCKV VCDENGSKGY GFVHFETQEA AERAIEKMNG MLLNDRKVFV GRFKSQKERE
     AELGARAKEF TNVYIKNFGE DMDDERLKEL FGKFGPALSV KVMTDESGKS KGFGFVSFER
     HEDAQKAVDE MNGKELNGKQ IYVGRAQKKV ERQTELKRKF EQMKQDRITR YQGVNLYVKN
     LDDGIDDERL RKEFSPFGTI TSAKVMMEGG RSKGFGFVCF SSPEEATKAV TEMNGRIVAT
     KPLYVALAQR KEERQAHLTN QYMQRMASVR AVPNPVINPY QPAPPSGYFM AAIPQTQNRA
     AYYPPSQIAQ LRPSPRWTAQ GARPHPFQNM PGAIRPAAPR PPFSTMRPAS SQVPRVMSTQ
     RVANTSTQTM GPRPAAAAAA ATPAVRTVPQ YKYAAGVRNP QQHLNAQPQV TMQQPAVHVQ
     GQEPLTASML ASAPPQEQKQ MLGERLFPLI QAMHPSLAGK ITGMLLEIDN SELLHMLESP
     ESLRSKVDEA VAVLQAHQAK EAAQKAVNSA TGVPTV
//
ID   GBB4_MOUSE              Reviewed;         340 AA.
AC   P29387; Q3TJJ1; Q8R475; Q9JHX8;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Guanine nucleotide-binding protein subunit beta-4;
DE   AltName: Full=Transducin beta chain 4;
GN   Name=Gnb4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92181467; PubMed=1543505; DOI=10.1016/0006-291X(92)91650-F;
RA   von Weizsaecker E., Strathmann M.P., Simon M.I.;
RT   "Diversity among the beta subunits of heterotrimeric GTP-binding
RT   proteins: characterization of a novel beta-subunit cDNA.";
RL   Biochem. Biophys. Res. Commun. 183:350-356(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=20429030; PubMed=10970423;
RA   Arnot M.I., Stotz S.C., Jarvis S.E., Zamponi G.W.;
RT   "Differential modulation of N-type 1B and P/Q-type 1A calcium channels
RT   by different G protein subunit isoforms.";
RL   J. Physiol. (Lond.) 527:203-212(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RX   MEDLINE=21831144; PubMed=11842130;
RX   DOI=10.1152/physiolgenomics.00085.2001;
RA   Ruiz-Velasco V., Ikeda S.R., Puhl H.L. III;
RT   "Cloning, tissue distribution, and functional expression of the human
RT   G protein beta 4-subunit.";
RL   Physiol. Genomics 8:41-50(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Placenta, and Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC       involved as a modulator or transducer in various transmembrane
CC       signaling systems. The beta and gamma chains are required for the
CC       GTPase activity, for replacement of GDP by GTP, and for G protein-
CC       effector interaction.
CC   -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and
CC       gamma.
CC   -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC   -!- SIMILARITY: Contains 7 WD repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; S86124; AAB21609.1; -; mRNA.
DR   EMBL; M87286; AAA37756.1; -; mRNA.
DR   EMBL; M63658; AAA37664.1; -; mRNA.
DR   EMBL; AF277893; AAF82124.1; -; mRNA.
DR   EMBL; AF501886; AAM15922.1; -; mRNA.
DR   EMBL; AK036816; BAC29589.1; -; mRNA.
DR   EMBL; AK152227; BAE31054.1; -; mRNA.
DR   EMBL; AK167416; BAE39504.1; -; mRNA.
DR   EMBL; BC028753; AAH28753.1; -; mRNA.
DR   IPI; IPI00310220; -.
DR   PIR; JS0669; RGMSB4.
DR   RefSeq; NP_038559.2; NM_013531.4.
DR   UniGene; Mm.139192; -.
DR   ProteinModelPortal; P29387; -.
DR   SMR; P29387; 1-340.
DR   DIP; DIP-604N; -.
DR   STRING; P29387; -.
DR   PhosphoSite; P29387; -.
DR   REPRODUCTION-2DPAGE; P29387; -.
DR   PRIDE; P29387; -.
DR   Ensembl; ENSMUST00000108234; ENSMUSP00000103869; ENSMUSG00000027669.
DR   GeneID; 14696; -.
DR   KEGG; mmu:14696; -.
DR   UCSC; uc008owl.1; mouse.
DR   CTD; 14696; -.
DR   MGI; MGI:104581; Gnb4.
DR   eggNOG; roNOG13354; -.
DR   HOGENOM; HBG396231; -.
DR   HOVERGEN; HBG000188; -.
DR   InParanoid; P29387; -.
DR   OMA; TRELPGH; -.
DR   PhylomeDB; P29387; -.
DR   NextBio; 286647; -.
DR   ArrayExpress; P29387; -.
DR   Bgee; P29387; -.
DR   Genevestigator; P29387; -.
DR   GermOnline; ENSMUSG00000027669; Mus musculus.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; TAS:MGI.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR001632; Gprotein_B.
DR   InterPro; IPR016346; Guanine_nucleotide-bd_bsu.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 7.
DR   PIRSF; PIRSF002394; GN-bd_beta; 1.
DR   PRINTS; PR00319; GPROTEINB.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 3.
DR   PROSITE; PS50082; WD_REPEATS_2; 6.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Repeat; Transducer; WD repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    340       Guanine nucleotide-binding protein
FT                                subunit beta-4.
FT                                /FTId=PRO_0000127703.
FT   REPEAT       53     92       WD 1.
FT   REPEAT       95    134       WD 2.
FT   REPEAT      141    179       WD 3.
FT   REPEAT      182    221       WD 4.
FT   REPEAT      224    263       WD 5.
FT   REPEAT      268    307       WD 6.
FT   REPEAT      310    339       WD 7.
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   CONFLICT    132    132       N -> D (in Ref. 1; AAB21609/AAA37756/
FT                                AAA37664).
FT   CONFLICT    140    140       P -> A (in Ref. 1; AAB21609/AAA37756/
FT                                AAA37664).
FT   CONFLICT    238    238       G -> V (in Ref. 3; AAM15922).
SQ   SEQUENCE   340 AA;  37379 MW;  F06827EBC2F0E966 CRC64;
     MSELEQLRQE AEQLRNQIQD ARKACNDATL VQITSNMDSV GRIQMRTRRT LRGHLAKIYA
     MHWGYDSRLL VSASQDGKLI IWDSYTTNKM HAIPLRSSWV MTCAYAPSGN YVACGGLDNI
     CSIYNLKTRE GNVRVSRELP GHTGYLSCCR FLDDGQIITS SGDTTCALWD IETGQQTTTF
     TGHSGDVMSL SLSPDLKTFV SGACDASSKL WDIRDGMCRQ SFTGHISDIN AVSFFPSGYA
     FATGSDDATC RLFDLRADQE LLLYSHDNII CGITSVAFSK SGRLLLAGYD DFNCSVWDAL
     KGGRSGVLAG HDNRVSCLGV TDDGMAVATG SWDSFLRIWN
//
ID   VCAM1_MOUSE             Reviewed;         739 AA.
AC   P29533;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   08-MAR-2011, entry version 107.
DE   RecName: Full=Vascular cell adhesion protein 1;
DE            Short=V-CAM 1;
DE            Short=VCAM-1;
DE   AltName: CD_antigen=CD106;
DE   Flags: Precursor;
GN   Name=Vcam1; Synonyms=Vcam-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=FVB; TISSUE=Lung;
RX   MEDLINE=92181437; PubMed=1371918; DOI=10.1016/0006-291X(92)91623-X;
RA   Hession C., Moy P., Tizard R., Chisholm P., Williams C., Wysk M.,
RA   Burkly L., Miyake K., Kincade P., Lobb R.;
RT   "Cloning of murine and rat vascular cell adhesion molecule-1.";
RL   Biochem. Biophys. Res. Commun. 183:163-169(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC   TISSUE=Lymph node;
RX   MEDLINE=93246254; PubMed=7683304; DOI=10.1016/0378-1119(93)90377-F;
RA   Araki M., Araki K., Vassalli P.;
RT   "Cloning and sequencing of mouse VCAM-1 cDNA.";
RL   Gene 126:261-264(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC   STRAIN=129; TISSUE=Embryo;
RX   MEDLINE=94117008; PubMed=7507076; DOI=10.1006/geno.1993.1480;
RA   Cybulsky M.I., Allan-Motamed M., Collins T.;
RT   "Structure of the murine VCAM1 gene.";
RL   Genomics 18:387-391(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE OF 1-693 (ISOFORM 1).
RC   STRAIN=129/Sv, and NIH Swiss;
RA   Kumar A.G., Dai Y.X., Kozak C.A., Mims M.P., Gotto A.M. Jr.,
RA   Ballantyne C.M.;
RL   Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=FVB; TISSUE=Lung;
RX   MEDLINE=93232042; PubMed=7682556;
RA   Moy P., Lobb R., Tizard R., Olson D., Hession C.;
RT   "Cloning of an inflammation-specific phosphatidyl inositol-linked form
RT   of murine vascular cell adhesion molecule-1.";
RL   J. Biol. Chem. 268:8835-8841(1993).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Liver;
RX   MEDLINE=95015899; PubMed=7523515;
RA   Kumar A.G., Dai X.Y., Kozak C.A., Mims M.P., Gotto A.M. Jr.,
RA   Ballantyne C.M.;
RT   "Murine VCAM-1. Molecular cloning, mapping, and analysis of a
RT   truncated form.";
RL   J. Immunol. 153:4088-4098(1994).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 311-345 (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   MEDLINE=93317595; PubMed=7687058; DOI=10.1073/pnas.90.13.5919;
RA   Terry R.W., Kwee L., Levine J.F., Labow M.A.;
RT   "Cytokine induction of an alternatively spliced murine vascular cell
RT   adhesion molecule (VCAM) mRNA encoding a glycosylphosphatidylinositol-
RT   anchored VCAM protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:5919-5923(1993).
RN   [8]
RP   NUCLEOTIDE SEQUENCE OF 1-21.
RC   TISSUE=Endothelial cell;
RA   Korenaga R., Ando J., Tsuboi H., Kamiya A.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   INTERACTION WITH ECMV-D CAPSID PROTEINS.
RX   PubMed=7514674;
RA   Huber S.A.;
RT   "VCAM-1 is a receptor for encephalomyocarditis virus on murine
RT   vascular endothelial cells.";
RL   J. Virol. 68:3453-3458(1994).
RN   [10]
RP   PROTEIN SEQUENCE OF 27-32, AND TISSUE SPECIFICITY.
RX   PubMed=1713592; DOI=10.1083/jcb.114.3.557;
RA   Miyake K., Medina K., Ishihara K., Kimoto M., Auerbach R.,
RA   Kincade P.W.;
RT   "A VCAM-like adhesion molecule on murine bone marrow stromal cells
RT   mediates binding of lymphocyte precursors in culture.";
RL   J. Cell Biol. 114:557-565(1991).
RN   [11]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-225; ASN-264; ASN-273;
RP   ASN-552 AND ASN-561, AND MASS SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
CC   -!- FUNCTION: Important in cell-cell recognition. Appears to function
CC       in leukocyte-endothelial cell adhesion. Interacts with the beta-1
CC       integrin VLA4 on leukocytes, and mediates both adhesion and signal
CC       transduction. The VCAM1/VLA4 interaction may play a
CC       pathophysiologic role both in immune responses and in leukocyte
CC       emigration to sites of inflammation.
CC   -!- SUBUNIT: Binds to ECMV-D capsid proteins and acts as a receptor
CC       for this virus.
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
CC       membrane protein.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Lipid-anchor, GPI-
CC       anchor.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Long;
CC         IsoId=P29533-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short;
CC         IsoId=P29533-2; Sequence=VSP_002581, VSP_002582;
CC         Note=GPI-anchored form;
CC   -!- TISSUE SPECIFICITY: Expressed on inflamed vascular endothelium, as
CC       well as on macrophage-like and dendritic cell types in both normal
CC       and inflamed tissue. Expressed in the bone marrow.
CC   -!- PTM: The GPI-anchor is located on position 319 of isoform 2.
CC   -!- SIMILARITY: Contains 7 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=VCAM-1;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Itlect_192";
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; M84487; AAA40545.1; -; mRNA.
DR   EMBL; X67783; CAA47989.1; -; mRNA.
DR   EMBL; L22355; AAA16921.1; -; Genomic_DNA.
DR   EMBL; L22301; AAA16921.1; JOINED; Genomic_DNA.
DR   EMBL; L22349; AAA16921.1; JOINED; Genomic_DNA.
DR   EMBL; L22350; AAA16921.1; JOINED; Genomic_DNA.
DR   EMBL; L22351; AAA16921.1; JOINED; Genomic_DNA.
DR   EMBL; L22352; AAA16921.1; JOINED; Genomic_DNA.
DR   EMBL; L22353; AAA16921.1; JOINED; Genomic_DNA.
DR   EMBL; L22354; AAA16921.1; JOINED; Genomic_DNA.
DR   EMBL; L22350; AAA16920.1; -; Genomic_DNA.
DR   EMBL; L22301; AAA16920.1; JOINED; Genomic_DNA.
DR   EMBL; L22349; AAA16920.1; JOINED; Genomic_DNA.
DR   EMBL; U12878; AAB60659.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U12879; AAB60660.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U12880; AAB60661.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U12874; AAB60662.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U12871; AAB60663.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U12883; AAB60664.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U12881; AAA80010.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U12882; AAA80011.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U12875; AAA80012.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U12872; AAA80013.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U12876; AAA80014.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U12873; AAA80015.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U12877; AAA80016.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; L08431; AAA40546.1; -; mRNA.
DR   EMBL; U12884; AAA64832.1; -; mRNA.
DR   EMBL; L12541; AAC37607.1; -; mRNA.
DR   EMBL; U42327; AAB88576.1; -; Genomic_DNA.
DR   IPI; IPI00126834; -.
DR   IPI; IPI00264750; -.
DR   PIR; B48919; A46052.
DR   PIR; JN0581; JN0581.
DR   RefSeq; NP_035823.3; NM_011693.3.
DR   UniGene; Mm.440909; -.
DR   UniGene; Mm.76649; -.
DR   ProteinModelPortal; P29533; -.
DR   SMR; P29533; 25-223, 231-511, 523-687.
DR   DIP; DIP-29097N; -.
DR   STRING; P29533; -.
DR   PhosphoSite; P29533; -.
DR   PRIDE; P29533; -.
DR   Ensembl; ENSMUST00000029574; ENSMUSP00000029574; ENSMUSG00000027962.
DR   Ensembl; ENSMUST00000106493; ENSMUSP00000102102; ENSMUSG00000027962.
DR   GeneID; 22329; -.
DR   KEGG; mmu:22329; -.
DR   CTD; 22329; -.
DR   MGI; MGI:98926; Vcam1.
DR   eggNOG; roNOG04595; -.
DR   HOGENOM; HBG126178; -.
DR   HOVERGEN; HBG053965; -.
DR   InParanoid; P29533; -.
DR   OrthoDB; EOG4894M1; -.
DR   ArrayExpress; P29533; -.
DR   Bgee; P29533; -.
DR   CleanEx; MM_VCAM1; -.
DR   Genevestigator; P29533; -.
DR   GermOnline; ENSMUSG00000027962; Mus musculus.
DR   GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0060710; P:chorio-allantoic fusion; IMP:MGI.
DR   GO; GO:0060669; P:embryonic placenta morphogenesis; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion; IMP:MGI.
DR   GO; GO:0044419; P:interspecies interaction between organisms; IEA:UniProtKB-KW.
DR   InterPro; IPR003987; ICAM_VCAM_N.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008424; Ig_C2-set.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR003989; VCAM-1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 7.
DR   Pfam; PF05790; C2-set; 2.
DR   Pfam; PF07679; I-set; 5.
DR   PRINTS; PR01472; ICAMVCAM1.
DR   PRINTS; PR01474; VCAM1.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 3.
DR   PROSITE; PS50835; IG_LIKE; 5.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Cell membrane;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Host-virus interaction; Immunoglobulin domain; Lipoprotein; Membrane;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     24       Probable.
FT   CHAIN        25    739       Vascular cell adhesion protein 1.
FT                                /FTId=PRO_0000014998.
FT   TOPO_DOM     25    698       Extracellular (Potential).
FT   TRANSMEM    699    720       Helical; (Potential).
FT   TOPO_DOM    721    739       Cytoplasmic (Potential).
FT   DOMAIN       25    111       Ig-like C2-type 1.
FT   DOMAIN      119    212       Ig-like C2-type 2.
FT   DOMAIN      223    309       Ig-like C2-type 3.
FT   DOMAIN      312    393       Ig-like C2-type 4.
FT   DOMAIN      408    506       Ig-like C2-type 5.
FT   DOMAIN      511    595       Ig-like C2-type 6.
FT   DOMAIN      600    682       Ig-like C2-type 7.
FT   CARBOHYD    225    225       N-linked (GlcNAc...).
FT   CARBOHYD    264    264       N-linked (GlcNAc...).
FT   CARBOHYD    273    273       N-linked (GlcNAc...).
FT   CARBOHYD    424    424       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    531    531       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    552    552       N-linked (GlcNAc...).
FT   CARBOHYD    561    561       N-linked (GlcNAc...).
FT   DISULFID     47     95       By similarity.
FT   DISULFID     52     99       By similarity.
FT   DISULFID    137    195       By similarity.
FT   DISULFID    246    291       By similarity.
FT   DISULFID    335    383       By similarity.
FT   DISULFID    534    579       By similarity.
FT   VAR_SEQ     310    345       EKPFIVDISPGSQVAAQVGDSVVLTCAAIGCDSPSF -> D
FT                                GRMKSQITNGHQLTVHLMFAKSFYFICYLCLYLAL (in
FT                                isoform 2).
FT                                /FTId=VSP_002581.
FT   VAR_SEQ     346    739       Missing (in isoform 2).
FT                                /FTId=VSP_002582.
FT   CONFLICT    693    693       D -> N (in Ref. 3; AAA16921).
SQ   SEQUENCE   739 AA;  81317 MW;  3D2134C341E5E449 CRC64;
     MPVKMVAVLG ASTVLWILFA VSQAFKIEIS PEYKTIAQIG DSMALTCSTT GCESPLFSWR
     TQIDSPLNAK VRTEGSKSVL TMEPVSFENE HSYLCTATCG SGKLERSIHV DIYSFPKDPE
     IQFSGPLEVG KPVTVKCLAP DIYPVYRLEI DLFKGDQLMN RQEFSSEEMT KSLETKSLEV
     TFTPVIEDIG KALVCRAKLH IDQIDSTLKE RETVKELQVY ISPRNTTISV HPSTRLQEGG
     AVTMTCSSEG LPAPEIFWGR KLDNEVLQLL SGNATLTLIA MRMEDSGVYV CEGVNLIGRD
     KAEVELVVQE KPFIVDISPG SQVAAQVGDS VVLTCAAIGC DSPSFSWRTQ TDSPLNGVVR
     NEGAKSTLVL SSVGFEDEHS YLCAVTCLQR TLEKRTQVEV YSFPEDPVIK MSGPLVHGRP
     VTVNCTVPNV YPFDHLEIEL LKGETTLMKK YFLEEMGIKS LETKILETTF IPTIEDTGKS
     LVCLARLHSG EMESEPKQRQ SVQPLYVNVA PKETTIWVSP SPILEEGSPV NLTCSSDGIP
     APKILWSRQL NNGELQPLSE NTTLTFMSTK RDDSGIYVCE GINEAGISRK SVELIIQVSP
     KDIQLTVFPS KSVKEGDTVI ISCTCGNVPE TWIILKKKAK TGDMVLKSVD GSYTIRQAQL
     QDAGIYECES KTEVGSQLRS LTLDVKGKEH NKDYFSPELL ALYCASSLVI PAIGMIVYFA
     RKANMKGSYS LVEAQKSKV
//
ID   FETUA_MOUSE             Reviewed;         345 AA.
AC   P29699; O35634;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Alpha-2-HS-glycoprotein;
DE   AltName: Full=Countertrypin;
DE   AltName: Full=Fetuin-A;
DE   Flags: Precursor;
GN   Name=Ahsg; Synonyms=Fetua;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Liver;
RX   MEDLINE=92223088; PubMed=1373325; DOI=10.1016/0167-4781(92)90522-2;
RA   Yang F., Chen Z.-L., Bergeron J.M., Cupples R.L., Friedrichs W.E.;
RT   "Human alpha 2-HS-glycoprotein/bovine fetuin homologue in mice:
RT   identification and developmental regulation of the gene.";
RL   Biochim. Biophys. Acta 1130:149-156(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129;
RX   MEDLINE=98058938; PubMed=9395485; DOI=10.1074/jbc.272.50.31496;
RA   Jahnen-Dechent W., Schinke T., Trindl A., Mueller-Esterl W.,
RA   Sablitzky F., Kaiser S., Blessing M.;
RT   "Cloning and targeted deletion of the mouse fetuin gene.";
RL   J. Biol. Chem. 272:31496-31503(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=93352581; PubMed=7688730;
RA   Yamamoto K., Sinohara H.;
RT   "Isolation and characterization of mouse countertrypin, a new trypsin
RT   inhibitor belonging to the mammalian fetuin family.";
RL   J. Biol. Chem. 268:17750-17753(1993).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-176, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Plasma;
RX   PubMed=16944957; DOI=10.1021/pr060186m;
RA   Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
RA   Gevaert K.;
RT   "Proteome-wide characterization of N-glycosylation events by diagonal
RT   chromatography.";
RL   J. Proteome Res. 5:2438-2447(2006).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-99; ASN-156 AND ASN-176,
RP   AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Plasma;
RX   PubMed=17330941; DOI=10.1021/pr0604559;
RA   Bernhard O.K., Kapp E.A., Simpson R.J.;
RT   "Enhanced analysis of the mouse plasma proteome using cysteine-
RT   containing tryptic glycopeptides.";
RL   J. Proteome Res. 6:987-995(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305; SER-309; SER-312
RP   AND SER-314, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138; SER-309 AND
RP   SER-312, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Probably involved in differentiation.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Liver is the major site of synthesis, but
CC       fetuin is also expressed in limb buds and other extrahepatic
CC       tissues during development.
CC   -!- SIMILARITY: Belongs to the fetuin family.
CC   -!- SIMILARITY: Contains 2 cystatin domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; S96534; AAB22070.1; -; mRNA.
DR   EMBL; AF007900; AAB81718.1; -; Genomic_DNA.
DR   EMBL; AJ002146; CAA05210.1; -; Genomic_DNA.
DR   EMBL; BC012678; AAH12678.1; -; mRNA.
DR   EMBL; BC019822; AAH19822.1; -; mRNA.
DR   IPI; IPI00128249; -.
DR   PIR; S21094; S21094.
DR   RefSeq; NP_038493.1; NM_013465.1.
DR   UniGene; Mm.197554; -.
DR   ProteinModelPortal; P29699; -.
DR   IntAct; P29699; 3.
DR   STRING; P29699; -.
DR   MEROPS; I25.020; -.
DR   MEROPS; I25.021; -.
DR   PhosphoSite; P29699; -.
DR   REPRODUCTION-2DPAGE; IPI00128249; -.
DR   PRIDE; P29699; -.
DR   Ensembl; ENSMUST00000023583; ENSMUSP00000023583; ENSMUSG00000022868.
DR   GeneID; 11625; -.
DR   KEGG; mmu:11625; -.
DR   UCSC; uc007ysr.1; mouse.
DR   CTD; 11625; -.
DR   MGI; MGI:107189; Ahsg.
DR   HOGENOM; HBG506561; -.
DR   HOVERGEN; HBG051607; -.
DR   InParanoid; P29699; -.
DR   OMA; KQYGFCK; -.
DR   OrthoDB; EOG4QC164; -.
DR   PhylomeDB; P29699; -.
DR   NextBio; 279179; -.
DR   ArrayExpress; P29699; -.
DR   Bgee; P29699; -.
DR   CleanEx; MM_AHSG; -.
DR   Genevestigator; P29699; -.
DR   GermOnline; ENSMUSG00000022868; Mus musculus.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   GO; GO:0006953; P:acute-phase response; ISS:UniProtKB.
DR   GO; GO:0030502; P:negative regulation of bone mineralization; IDA:UniProtKB.
DR   GO; GO:0001503; P:ossification; IDA:MGI.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; ISS:UniProtKB.
DR   GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR   InterPro; IPR000010; Prot_inh_cystat.
DR   InterPro; IPR001363; Prot_inh_fetuin_CS.
DR   Pfam; PF00031; Cystatin; 1.
DR   SMART; SM00043; CY; 2.
DR   PROSITE; PS01254; FETUIN_1; 1.
DR   PROSITE; PS01255; FETUIN_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Phosphoprotein; Repeat; Secreted; Signal.
FT   SIGNAL        1     18       Potential.
FT   CHAIN        19    345       Alpha-2-HS-glycoprotein.
FT                                /FTId=PRO_0000008891.
FT   DOMAIN       27    144       Cystatin 1.
FT   DOMAIN      145    255       Cystatin 2.
FT   MOD_RES     134    134       Phosphoserine (By similarity).
FT   MOD_RES     138    138       Phosphoserine.
FT   MOD_RES     305    305       Phosphoserine.
FT   MOD_RES     309    309       Phosphoserine.
FT   MOD_RES     312    312       Phosphoserine.
FT   MOD_RES     314    314       Phosphoserine.
FT   CARBOHYD     99     99       N-linked (GlcNAc...).
FT   CARBOHYD    156    156       N-linked (GlcNAc...).
FT   CARBOHYD    176    176       N-linked (GlcNAc...).
FT   DISULFID     32    336       By similarity.
FT   DISULFID     89    100       By similarity.
FT   DISULFID    114    132       By similarity.
FT   DISULFID    146    149       By similarity.
FT   DISULFID    208    219       By similarity.
FT   DISULFID    230    247       By similarity.
FT   CONFLICT     71     71       R -> RQ (in Ref. 2; CAA05210).
SQ   SEQUENCE   345 AA;  37326 MW;  4B7B9C9B1410658E CRC64;
     MKSLVLLLCF AQLWGCQSAP QGTGLGFREL ACDDPEAEQV ALLAVDYLNN HLLQGFKQVL
     NQIDKVKVWS RRPFGVVYEM EVDTLETTCH ALDPTPLANC SVRQLTEHAV EGDCDFHILK
     QDGQFRVMHT QCHSTPDSAE DVRKLCPRCP LLTPFNDTNV VHTVNTALAA FNTQNNGTYF
     KLVEISRAQN VPLPVSTLVE FVIAATDCTA KEVTDPAKCN LLAEKQHGFC KANLMHNLGG
     EEVSVACKLF QTQPQPANAN AVGPVPTANA ALPADPPASV VVGPVVVPRG LSDHRTYHDL
     RHAFSPVASV ESASGETLHS PKVGQPGAAG PVSPMCPGRI RHFKI
//
ID   KCRU_MOUSE              Reviewed;         418 AA.
AC   P30275;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Creatine kinase U-type, mitochondrial;
DE            EC=2.7.3.2;
DE   AltName: Full=Acidic-type mitochondrial creatine kinase;
DE            Short=Mia-CK;
DE   AltName: Full=Ubiquitous mitochondrial creatine kinase;
DE            Short=U-MtCK;
DE   Flags: Precursor;
GN   Name=Ckmt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   MEDLINE=95322032; PubMed=7598809; DOI=10.1089/dna.1995.14.539;
RA   Steeghs K., Peters W., Brueckwilder M., Croes H., van Alewijk D.,
RA   Wieringa B.;
RT   "Mouse ubiquitous mitochondrial creatine kinase: gene organization and
RT   consequences from inactivation in mouse embryonic stem cells.";
RL   DNA Cell Biol. 14:539-553(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 47-75; 105-130; 152-158; 173-182; 191-200;
RP   250-270; 302-326 AND 355-375, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   NITRATION [LARGE SCALE ANALYSIS] AT TYR-313, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16800626; DOI=10.1021/bi060474w;
RA   Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
RA   Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
RA   Squier T.C., Bigelow D.J.;
RT   "Endogenously nitrated proteins in mouse brain: links to
RT   neurodegenerative disease.";
RL   Biochemistry 45:8009-8022(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-154, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between
CC       ATP and various phosphogens (e.g. creatine phosphate). Creatine
CC       kinase isoenzymes play a central role in energy transduction in
CC       tissues with large, fluctuating energy demands, such as skeletal
CC       muscle, heart, brain and spermatozoa.
CC   -!- CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine.
CC   -!- SUBUNIT: Exists as an octamer composed of four MTCK homodimers.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein; Intermembrane side.
CC   -!- MISCELLANEOUS: Mitochondrial creatine kinase binds cardiolipin.
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC   -!- SIMILARITY: Contains 1 phosphagen kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 phosphagen kinase N-terminal domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Z13968; CAA78371.1; -; mRNA.
DR   EMBL; Z13969; CAA78372.1; -; Genomic_DNA.
DR   EMBL; BC025976; AAH25976.1; -; mRNA.
DR   IPI; IPI00128296; -.
DR   PIR; I48308; S24612.
DR   RefSeq; NP_034027.1; NM_009897.2.
DR   UniGene; Mm.252145; -.
DR   ProteinModelPortal; P30275; -.
DR   SMR; P30275; 40-418.
DR   STRING; P30275; -.
DR   PhosphoSite; P30275; -.
DR   PRIDE; P30275; -.
DR   Ensembl; ENSMUST00000000317; ENSMUSP00000000317; ENSMUSG00000000308.
DR   Ensembl; ENSMUST00000078222; ENSMUSP00000077349; ENSMUSG00000000308.
DR   GeneID; 12716; -.
DR   KEGG; mmu:12716; -.
DR   UCSC; uc008lyt.1; mouse.
DR   CTD; 12716; -.
DR   MGI; MGI:99441; Ckmt1.
DR   HOGENOM; HBG445448; -.
DR   HOVERGEN; HBG001339; -.
DR   InParanoid; P30275; -.
DR   OMA; ERHNGYN; -.
DR   OrthoDB; EOG40VVPN; -.
DR   PhylomeDB; P30275; -.
DR   BRENDA; 2.7.3.2; 244.
DR   NextBio; 281988; -.
DR   ArrayExpress; P30275; -.
DR   Bgee; P30275; -.
DR   CleanEx; MM_CKMT1; -.
DR   Genevestigator; P30275; -.
DR   GermOnline; ENSMUSG00000000308; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004111; F:creatine kinase activity; IEA:EC.
DR   InterPro; IPR000749; ATP-guanido_PTrfase.
DR   InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR   InterPro; IPR022415; ATP-guanido_PTrfase_cat_AS.
DR   InterPro; IPR022413; ATP-guanido_PTrfase_N.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   Gene3D; G3DSA:1.10.135.10; ATP-gua_Ptrans; 1.
DR   Gene3D; G3DSA:3.30.590.10; ATP-gua_Ptrans; 1.
DR   PANTHER; PTHR11547; ATP-gua_Ptrans; 1.
DR   Pfam; PF00217; ATP-gua_Ptrans; 1.
DR   Pfam; PF02807; ATP-gua_PtransN; 1.
DR   SUPFAM; SSF48034; ATP-gua_Ptrans; 1.
DR   PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR   PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
DR   PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Kinase; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Nitration;
KW   Nucleotide-binding; Phosphoprotein; Transferase; Transit peptide.
FT   TRANSIT       1     39       Mitochondrion (By similarity).
FT   CHAIN        40    418       Creatine kinase U-type, mitochondrial.
FT                                /FTId=PRO_0000016591.
FT   DOMAIN       46    132       Phosphagen kinase N-terminal.
FT   DOMAIN      159    401       Phosphagen kinase C-terminal.
FT   NP_BIND     162    166       ATP (By similarity).
FT   NP_BIND     354    359       ATP (By similarity).
FT   REGION       40     64       Cardiolipin-binding (By similarity).
FT   BINDING     225    225       ATP (By similarity).
FT   BINDING     270    270       ATP (By similarity).
FT   BINDING     326    326       ATP (By similarity).
FT   BINDING     369    369       ATP (By similarity).
FT   MOD_RES     154    154       Phosphotyrosine.
FT   MOD_RES     313    313       Nitrated tyrosine.
SQ   SEQUENCE   418 AA;  47004 MW;  993CD8C290C8BFB9 CRC64;
     MAGPFSRLLS ARPGLRLLAL AGAGSLTAGI LLRPESVGAA AAERRRLYPP SAEYPDLRKH
     NNCMASHLTP AVYARLCDKT TPTGWTLDQC IQTGVDNPGH PFIKTVGMVA GDEETYEVFA
     ELFDPVIQER HNGYDPRTMK HTTDLDASKI RSGYFDERYV LSSRVRTGRS IRGLSLPPAC
     TRAERREVER VVVDALSGLK GDLAGRYYRL SEMTEAEQQQ LIDDHFLFDK PVSPLLTAAG
     MARDWPDARG IWHNNEKSFL IWVNEEDHTR VISMEKGGNM KRVFERFCRG LKEVEKLIQE
     RGWEFMWNER LGYILTCPSN LGTGLRAGVH IKLPLLSKDN RFPKILENLR LQKRGTGGVD
     TAATGSVFDI SNLDRLGKSE VELVQLVIDG VNYLIDCERR LERGQDIRIP PPLVHSKH
//
ID   NK1R_MOUSE              Reviewed;         407 AA.
AC   P30548;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Substance-P receptor;
DE            Short=SPR;
DE   AltName: Full=NK-1 receptor;
DE            Short=NK-1R;
DE   AltName: Full=Tachykinin receptor 1;
GN   Name=Tacr1; Synonyms=Tac1r;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Intestine;
RX   MEDLINE=92137253; PubMed=1370937;
RX   DOI=10.1111/j.1432-1033.1992.tb16592.x;
RA   Sundelin J.B., Provvedini D.M., Wahlestedt C.R., Laurell H.,
RA   Pohl J.S., Peterson P.A.;
RT   "Molecular cloning of the murine substance K and substance P receptor
RT   genes.";
RL   Eur. J. Biochem. 203:625-631(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 63-290.
RC   STRAIN=CBA; TISSUE=Brain, and T-cell;
RX   MEDLINE=94165478; PubMed=8120392;
RA   Cook G.A., Elliott D., Metwali A., Blum A.M., Sandor M., Lynch R.,
RA   Weinstock J.V.;
RT   "Molecular evidence that granuloma T lymphocytes in murine
RT   schistosomiasis mansoni express an authentic substance P (NK-1)
RT   receptor.";
RL   J. Immunol. 152:1830-1835(1994).
CC   -!- FUNCTION: This is a receptor for the tachykinin neuropeptide
CC       substance P. It is probably associated with G proteins that
CC       activate a phosphatidylinositol-calcium second messenger system.
CC       The rank order of affinity of this receptor to tachykinins is:
CC       substance P > substance K > neuromedin K.
CC   -!- SUBUNIT: Interacts with ARRB1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
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DR   EMBL; X62934; CAA44707.1; -; mRNA.
DR   EMBL; L27828; AAA17892.1; -; mRNA.
DR   EMBL; L27826; AAA17891.1; -; mRNA.
DR   IPI; IPI00131251; -.
DR   PIR; S20304; S20304.
DR   UniGene; Mm.8055; -.
DR   ProteinModelPortal; P30548; -.
DR   SMR; P30548; 33-321.
DR   STRING; P30548; -.
DR   PRIDE; P30548; -.
DR   Ensembl; ENSMUST00000032122; ENSMUSP00000032122; ENSMUSG00000030043.
DR   MGI; MGI:98475; Tacr1.
DR   eggNOG; roNOG08125; -.
DR   HOGENOM; HBG443644; -.
DR   HOVERGEN; HBG103412; -.
DR   InParanoid; P30548; -.
DR   OrthoDB; EOG4WQ12N; -.
DR   ArrayExpress; P30548; -.
DR   Bgee; P30548; -.
DR   CleanEx; MM_TACR1; -.
DR   Genevestigator; P30548; -.
DR   GermOnline; ENSMUSG00000030043; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR001681; Neurokn_rcpt.
DR   InterPro; IPR000046; NK1_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01024; NEUROKININ1R.
DR   PRINTS; PR00244; NEUROKININR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Receptor; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN         1    407       Substance-P receptor.
FT                                /FTId=PRO_0000069887.
FT   TOPO_DOM      1     31       Extracellular (Potential).
FT   TRANSMEM     32     54       Helical; Name=1; (Potential).
FT   TOPO_DOM     55     64       Cytoplasmic (Potential).
FT   TRANSMEM     65     86       Helical; Name=2; (Potential).
FT   TOPO_DOM     87    106       Extracellular (Potential).
FT   TRANSMEM    107    128       Helical; Name=3; (Potential).
FT   TOPO_DOM    129    148       Cytoplasmic (Potential).
FT   TRANSMEM    149    169       Helical; Name=4; (Potential).
FT   TOPO_DOM    170    194       Extracellular (Potential).
FT   TRANSMEM    195    219       Helical; Name=5; (Potential).
FT   TOPO_DOM    220    248       Cytoplasmic (Potential).
FT   TRANSMEM    249    270       Helical; Name=6; (Potential).
FT   TOPO_DOM    271    283       Extracellular (Potential).
FT   TRANSMEM    284    308       Helical; Name=7; (Potential).
FT   TOPO_DOM    309    407       Cytoplasmic (Potential).
FT   LIPID       322    322       S-palmitoyl cysteine (Potential).
FT   CARBOHYD     14     14       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     18     18       N-linked (GlcNAc...) (Potential).
FT   DISULFID    105    180       By similarity.
SQ   SEQUENCE   407 AA;  46304 MW;  451B6D475A6659A0 CRC64;
     MDNVLPVDSD LFPNTSTNTS ESNQFVQPTW QIVLWAAAYT VIVVTSVVGN VVVIWIILAH
     KRMRTVTNYF LVNLAFAEAC MAAFNTVVNF TYAVHNVWYY GLFYCKFHNF FPIAALFASI
     YSMTAVAFDR YMAIIHPLQP RLSATATKVV IFVIWVLALL LAFPQGYYST TETMPSRVVC
     MIEWPEHPNR TYEKAYHICV TVLIYFLPLL VIGYAYTVVG ITLWASEIPG DSSDRYHEQV
     SAKRKVVKMM IVVVCTFAIC WLPFHIFFLL PYINPDLYLK KFIQQVYLAS MWLAMSSTMY
     NPIIYCCLND RFRLGFKHAF RCCPFISAGD YEGLEMKSTR YLQTQSSVYK VSRLETTIST
     VVGAHEDEPE EGPKATPSSL DLTSNGSSRS NSKTMTESSS FYSNILA
//
ID   SSR1_MOUSE              Reviewed;         391 AA.
AC   P30873;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Somatostatin receptor type 1;
DE            Short=SS-1-R;
DE            Short=SS1-R;
DE            Short=SS1R;
DE   AltName: Full=SRIF-2;
GN   Name=Sstr1; Synonyms=Smstr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92108031; PubMed=1346068; DOI=10.1073/pnas.89.1.251;
RA   Yamada Y., Post S.R., Wang K., Tager H.S., Bell G.I., Seino S.;
RT   "Cloning and functional characterization of a family of human and
RT   mouse somatostatin receptors expressed in brain, gastrointestinal
RT   tract, and kidney.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:251-255(1992).
CC   -!- FUNCTION: Receptor for somatostatin with higher affinity for
CC       somatostatin-14 than -28. This receptor is coupled via pertussis
CC       toxin sensitive G proteins to inhibition of adenylyl cyclase. In
CC       addition it stimulates phosphotyrosine phosphatase and Na(+)/H(+)
CC       exchanger via pertussis toxin insensitive G proteins.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Jejunum and stomach.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
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DR   EMBL; M81831; AAA58255.1; -; Genomic_DNA.
DR   IPI; IPI00134657; -.
DR   PIR; C41795; C41795.
DR   RefSeq; NP_033242.1; NM_009216.3.
DR   UniGene; Mm.278336; -.
DR   ProteinModelPortal; P30873; -.
DR   SMR; P30873; 59-339.
DR   MINT; MINT-6504720; -.
DR   STRING; P30873; -.
DR   PRIDE; P30873; -.
DR   Ensembl; ENSMUST00000044299; ENSMUSP00000037045; ENSMUSG00000035431.
DR   Ensembl; ENSMUST00000110671; ENSMUSP00000106299; ENSMUSG00000035431.
DR   GeneID; 20605; -.
DR   KEGG; mmu:20605; -.
DR   UCSC; uc007npu.1; mouse.
DR   CTD; 20605; -.
DR   MGI; MGI:98327; Sstr1.
DR   eggNOG; maNOG12790; -.
DR   HOGENOM; HBG715643; -.
DR   HOVERGEN; HBG106919; -.
DR   InParanoid; P30873; -.
DR   OMA; CTSRITT; -.
DR   OrthoDB; EOG44J2J9; -.
DR   PhylomeDB; P30873; -.
DR   NextBio; 298945; -.
DR   ArrayExpress; P30873; -.
DR   Bgee; P30873; -.
DR   CleanEx; MM_SSTR1; -.
DR   Genevestigator; P30873; -.
DR   GermOnline; ENSMUSG00000035431; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0004994; F:somatostatin receptor activity; IDA:MGI.
DR   GO; GO:0007215; P:glutamate signaling pathway; IDA:MGI.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR000586; Somatstn_rcpt.
DR   InterPro; IPR001116; Somatstn_rcpt_1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00246; SOMATOSTATNR.
DR   PRINTS; PR00587; SOMATOSTTN1R.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Lipoprotein; Membrane; Palmitate; Receptor; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    391       Somatostatin receptor type 1.
FT                                /FTId=PRO_0000070117.
FT   TOPO_DOM      1     56       Extracellular (Potential).
FT   TRANSMEM     57     84       Helical; Name=1; (Potential).
FT   TOPO_DOM     85     94       Cytoplasmic (Potential).
FT   TRANSMEM     95    120       Helical; Name=2; (Potential).
FT   TOPO_DOM    121    131       Extracellular (Potential).
FT   TRANSMEM    132    153       Helical; Name=3; (Potential).
FT   TOPO_DOM    154    175       Cytoplasmic (Potential).
FT   TRANSMEM    176    196       Helical; Name=4; (Potential).
FT   TOPO_DOM    197    219       Extracellular (Potential).
FT   TRANSMEM    220    244       Helical; Name=5; (Potential).
FT   TOPO_DOM    245    270       Cytoplasmic (Potential).
FT   TRANSMEM    271    296       Helical; Name=6; (Potential).
FT   TOPO_DOM    297    303       Extracellular (Potential).
FT   TRANSMEM    304    327       Helical; Name=7; (Potential).
FT   TOPO_DOM    328    391       Cytoplasmic (Potential).
FT   LIPID       339    339       S-palmitoyl cysteine (Potential).
FT   CARBOHYD      4      4       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     44     44       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     48     48       N-linked (GlcNAc...) (Potential).
FT   DISULFID    130    208       By similarity.
SQ   SEQUENCE   391 AA;  42718 MW;  4461673956F2BD22 CRC64;
     MFPNGTASSP SSSPSPSPGS CGEGACSRGP GSGAADGMEE PGRNASQNGT LSEGQGSAIL
     ISFIYSVVCL VGLCGNSMVI YVILRYAKMK TATNIYILNL AIADELLMLS VPFLVTSTLL
     RHWPFGALLC RLVLSVDAVN MFTSIYCLTV LSVDRYVAVV HPIKAARYRR PTVAKVVNLG
     VWVLSLLVIL PIVVFSRTAA NSDGTVACNM LMPEPAQRWL VGFVLYTFLM GFLLPVGAIC
     LCYVLIIAKM RMVALKAGWQ QRKRSERKIT LMVMMVVMVF VICWMPFYVV QLVNVFAEQD
     DATVSQLSVI LGYANSCANP ILYGFLSDNF KRSFQRILCL SWMDNAAEEP VDYYATALKS
     RAYSVEDFQP ENLESGGVFR NGTCASRIST L
//
ID   SSR3_MOUSE              Reviewed;         428 AA.
AC   P30935;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Somatostatin receptor type 3;
DE            Short=SS-3-R;
DE            Short=SS3-R;
DE            Short=SS3R;
DE   AltName: Full=SSR-28;
GN   Name=Sstr3; Synonyms=Smstr3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=93015924; PubMed=1328199;
RA   Yasuda K., Rens-Domiano S., Breder C.D., Law S.F., Saper C.B.,
RA   Reisine T., Bell G.I.;
RT   "Cloning of a novel somatostatin receptor, SSTR3, coupled to
RT   adenylylcyclase.";
RL   J. Biol. Chem. 267:20422-20428(1992).
CC   -!- FUNCTION: Receptor for somatostatins-14 and -28. This receptor is
CC       coupled via pertussis toxin sensitive G proteins to inhibition of
CC       adenylyl cyclase.
CC   -!- INTERACTION:
CC       Q8NFJ9:BBS1 (xeno); NbExp=1; IntAct=EBI-2892516, EBI-1805484;
CC       Q9BXC9:BBS2 (xeno); NbExp=1; IntAct=EBI-2892516, EBI-748297;
CC       Q96RK4:BBS4 (xeno); NbExp=1; IntAct=EBI-2892516, EBI-1805814;
CC       Q8N3I7:BBS5 (xeno); NbExp=1; IntAct=EBI-2892516, EBI-2892592;
CC       Q8IWZ6:BBS7 (xeno); NbExp=1; IntAct=EBI-2892516, EBI-1806001;
CC       Q8TAM2:TTC8 (xeno); NbExp=1; IntAct=EBI-2892516, EBI-2892638;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity). Note=Internalized into endoplasmic vesicles upon
CC       somatostatin-stimulation (By similarity).
CC   -!- PTM: Phosphorylated. Phosphorylation increases upon somatostatin
CC       binding (By similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
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DR   EMBL; M91000; AAA40144.1; -; Genomic_DNA.
DR   IPI; IPI00135713; -.
DR   PIR; A44021; A44021.
DR   UniGene; Mm.211411; -.
DR   ProteinModelPortal; P30935; -.
DR   SMR; P30935; 46-338.
DR   IntAct; P30935; 9.
DR   STRING; P30935; -.
DR   PhosphoSite; P30935; -.
DR   PRIDE; P30935; -.
DR   Ensembl; ENSMUST00000053239; ENSMUSP00000058040; ENSMUSG00000044933.
DR   MGI; MGI:98329; Sstr3.
DR   eggNOG; roNOG10482; -.
DR   HOGENOM; HBG715643; -.
DR   HOVERGEN; HBG106919; -.
DR   InParanoid; P30935; -.
DR   OrthoDB; EOG4XPQGG; -.
DR   ArrayExpress; P30935; -.
DR   Bgee; P30935; -.
DR   CleanEx; MM_SSTR3; -.
DR   Genevestigator; P30935; -.
DR   GermOnline; ENSMUSG00000044933; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031513; C:nonmotile primary cilium; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004994; F:somatostatin receptor activity; IEA:InterPro.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR000586; Somatstn_rcpt.
DR   InterPro; IPR001856; Somatstn_rcpt_3.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00246; SOMATOSTATNR.
DR   PRINTS; PR00589; SOMATOSTTN3R.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Phosphoprotein; Receptor; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    428       Somatostatin receptor type 3.
FT                                /FTId=PRO_0000070125.
FT   TOPO_DOM      1     45       Extracellular (Potential).
FT   TRANSMEM     46     71       Helical; Name=1; (Potential).
FT   TOPO_DOM     72     81       Cytoplasmic (Potential).
FT   TRANSMEM     82    103       Helical; Name=2; (Potential).
FT   TOPO_DOM    104    118       Extracellular (Potential).
FT   TRANSMEM    119    140       Helical; Name=3; (Potential).
FT   TOPO_DOM    141    162       Cytoplasmic (Potential).
FT   TRANSMEM    163    182       Helical; Name=4; (Potential).
FT   TOPO_DOM    183    206       Extracellular (Potential).
FT   TRANSMEM    207    232       Helical; Name=5; (Potential).
FT   TOPO_DOM    233    266       Cytoplasmic (Potential).
FT   TRANSMEM    267    288       Helical; Name=6; (Potential).
FT   TOPO_DOM    289    302       Extracellular (Potential).
FT   TRANSMEM    303    325       Helical; Name=7; (Potential).
FT   TOPO_DOM    326    428       Cytoplasmic (Potential).
FT   COMPBIAS    358    373       Poly-Glu.
FT   MOD_RES     341    341       Phosphoserine (By similarity).
FT   MOD_RES     346    346       Phosphoserine (By similarity).
FT   MOD_RES     351    351       Phosphoserine (By similarity).
FT   MOD_RES     357    357       Phosphothreonine (By similarity).
FT   CARBOHYD     18     18       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     31     31       N-linked (GlcNAc...) (Potential).
FT   DISULFID    117    192       By similarity.
SQ   SEQUENCE   428 AA;  47391 MW;  D006E4B7BE501FAA CRC64;
     MATVTYPSSE PMTLDPGNTS STWPLDTTLG NTSAGASLTG LAVSGILISL VYLVVCVVGL
     LGNSLVIYVV LRHTSSPSVT SVYILNLALA DELFMLGLPF LAAQNALSYW PFGSLMCRLV
     MAVDGINQFT SIFCLTVMSV DRYLAVVHPT RSARWRTAPV ARTVSRAVWV ASAVVVLPVV
     VFSGVPRGMS TCHMQWPEPA AAWRTAFIIY MAALGFFGPL LVICLCYLLI VVKVRSTTRR
     VRAPSCQWVQ APACQRRRRS ERRVTRMVVA VVALFVLCWM PFYLLNIVNV VCPLPEEPAF
     FGLYFLVVAL PYANSCANPI LYGFLSYRFK QGFRRILLRP SRRIRSQEPG SGPPEKTEEE
     EDEEEEERRE EEERRMQRGQ EMNGRLSQIA QAGTSGQQPR PCTGTAKEQQ LLPQEATAGD
     KASTLSHL
//
ID   CTND1_MOUSE             Reviewed;         938 AA.
AC   P30999; Q3TSU9; Q80XQ4; Q8CHF8;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   08-MAR-2011, entry version 100.
DE   RecName: Full=Catenin delta-1;
DE   AltName: Full=Cadherin-associated Src substrate;
DE            Short=CAS;
DE   AltName: Full=p120 catenin;
DE            Short=p120(ctn);
DE   AltName: Full=p120(cas);
GN   Name=Ctnnd1; Synonyms=Catns, Kiaa0384;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=Swiss;
RX   MEDLINE=93096477; PubMed=1334250;
RA   Reynolds A.B., Herbert L., Cleveland J.L., Berg S.T., Gaut J.R.;
RT   "p120, a novel substrate of protein tyrosine kinase receptors and of
RT   p60v-src, is related to cadherin-binding factors beta-catenin,
RT   plakoglobin and armadillo.";
RL   Oncogene 7:2439-2445(1992).
RN   [2]
RP   SEQUENCE REVISION.
RA   Reynolds A.B.;
RL   Submitted (DEC-1992) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   INTERACTION WITH ZBTB33.
RX   MEDLINE=99223590; PubMed=10207085;
RA   Daniel J.M., Reynolds A.B.;
RT   "The catenin p120(ctn) interacts with Kaiso, a novel BTB/POZ domain
RT   zinc finger transcription factor.";
RL   Mol. Cell. Biol. 19:3614-3623(1999).
RN   [7]
RP   INTERACTION WITH ZBTB33.
RX   MEDLINE=22082336; PubMed=12087177; DOI=10.1093/nar/gkf398;
RA   Daniel J.M., Spring C.M., Crawford H.C., Reynolds A.B., Baig A.;
RT   "The p120(ctn)-binding partner Kaiso is a bi-modal DNA-binding protein
RT   that recognizes both a sequence-specific consensus and methylated CpG
RT   dinucleotides.";
RL   Nucleic Acids Res. 30:2911-2919(2002).
RN   [8]
RP   FUNCTION, NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF 622-LYS-LYS-623.
RX   PubMed=15138284; DOI=10.1242/jcs.01101;
RA   Kelly K.F., Spring C.M., Otchere A.A., Daniel J.M.;
RT   "NLS-dependent nuclear localization of p120ctn is necessary to relieve
RT   Kaiso-mediated transcriptional repression.";
RL   J. Cell Sci. 117:2675-2686(2004).
RN   [9]
RP   ERRATUM.
RA   Kelly K.F., Spring C.M., Otchere A.A., Daniel J.M.;
RL   J. Cell Sci. 117:3405-3405(2004).
RN   [10]
RP   FUNCTION.
RX   PubMed=15817151; DOI=10.1016/j.yexcr.2005.01.007;
RA   Spring C.M., Kelly K.F., O'Kelly I., Graham M., Crawford H.C.,
RA   Daniel J.M.;
RT   "The catenin p120ctn inhibits Kaiso-mediated transcriptional
RT   repression of the beta-catenin/TCF target gene matrilysin.";
RL   Exp. Cell Res. 305:253-265(2005).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-904, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [12]
RP   INTERACTION WITH GLIS2, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=17344476; DOI=10.1091/mbc.E06-10-0941;
RA   Hosking C.R., Ulloa F., Hogan C., Ferber E.C., Figueroa A.,
RA   Gevaert K., Birchmeier W., Briscoe J., Fujita Y.;
RT   "The transcriptional repressor Glis2 is a novel binding partner for
RT   p120 catenin.";
RL   Mol. Biol. Cell 18:1918-1927(2007).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; TYR-291; SER-320;
RP   SER-349; SER-352; SER-859 AND TYR-865, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; SER-252; SER-269;
RP   SER-346; SER-349; SER-352; SER-857; SER-864 AND SER-920, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-228; TYR-257; SER-349;
RP   SER-352 AND TYR-904, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: May associate with and regulate the cell adhesion
CC       properties of both C- and E-cadherins. Implicated both in cell
CC       transformation by SRC and in ligand-induced receptor signaling
CC       through the EGF, PDGF, CSF-1 and ERBB2 receptors (By similarity).
CC       Binds to and inhibits the transcriptional repressor ZBTB33, which
CC       may lead to activation of target genes of the Wnt signaling
CC       pathway. Promotes GLIS2 C-terminal cleavage.
CC   -!- SUBUNIT: Belongs to a multiprotein cell-cell adhesion complex that
CC       also contains E-cadherin, alpha-catenin, beta-catenin, and gamma-
CC       catenin. Binds to the C-terminal fragment of PSEN1 and mutually
CC       competes for E-cadherin (By similarity). Interacts with ZBTB33.
CC       Interacts with GLIS2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane.
CC       Note=Interaction with GLIS2 promotes nuclear translocation.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P30999-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P30999-2; Sequence=VSP_030567, VSP_030568;
CC       Name=3;
CC         IsoId=P30999-3; Sequence=VSP_030568;
CC   -!- PTM: Phosphorylated by protein-tyrosine kinases. Dephosphorylated
CC       by PTPRJ (By similarity).
CC   -!- SIMILARITY: Belongs to the beta-catenin family.
CC   -!- SIMILARITY: Contains 10 ARM repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC41421.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; Z17804; CAA79078.1; -; mRNA.
DR   EMBL; AB093237; BAC41421.1; ALT_INIT; mRNA.
DR   EMBL; AK133193; BAE21551.1; -; mRNA.
DR   EMBL; AK161790; BAE36576.1; -; mRNA.
DR   EMBL; BC043108; AAH43108.1; -; mRNA.
DR   EMBL; BC054544; AAH54544.1; -; mRNA.
DR   IPI; IPI00316623; -.
DR   IPI; IPI00403823; -.
DR   IPI; IPI00660602; -.
DR   PIR; I48701; S28498.
DR   RefSeq; NP_001078917.1; NM_001085448.1.
DR   RefSeq; NP_001078918.1; NM_001085449.1.
DR   RefSeq; NP_001078919.1; NM_001085450.1.
DR   RefSeq; NP_001078922.1; NM_001085453.1.
DR   RefSeq; NP_031641.2; NM_007615.4.
DR   UniGene; Mm.35738; -.
DR   ProteinModelPortal; P30999; -.
DR   SMR; P30999; 358-852.
DR   IntAct; P30999; 5.
DR   MINT; MINT-89877; -.
DR   STRING; P30999; -.
DR   PhosphoSite; P30999; -.
DR   PRIDE; P30999; -.
DR   Ensembl; ENSMUST00000067232; ENSMUSP00000064518; ENSMUSG00000034101.
DR   Ensembl; ENSMUST00000111691; ENSMUSP00000107320; ENSMUSG00000034101.
DR   Ensembl; ENSMUST00000111697; ENSMUSP00000107326; ENSMUSG00000034101.
DR   GeneID; 12388; -.
DR   KEGG; mmu:12388; -.
DR   CTD; 12388; -.
DR   MGI; MGI:105100; Ctnnd1.
DR   eggNOG; roNOG07536; -.
DR   HOVERGEN; HBG004284; -.
DR   OrthoDB; EOG4D52WX; -.
DR   NextBio; 281110; -.
DR   ArrayExpress; P30999; -.
DR   Bgee; P30999; -.
DR   CleanEx; MM_CTNND1; -.
DR   Genevestigator; P30999; -.
DR   GermOnline; ENSMUSG00000034101; Mus musculus.
DR   GO; GO:0005913; C:cell-cell adherens junction; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR   GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR   GO; GO:0042153; F:RPTP-like protein binding; IPI:MGI.
DR   GO; GO:0016337; P:cell-cell adhesion; IMP:MGI.
DR   GO; GO:0060690; P:epithelial cell differentiation involved in salivary gland development; IMP:MGI.
DR   GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI.
DR   GO; GO:0001738; P:morphogenesis of a polarized epithelium; IMP:MGI.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0007435; P:salivary gland morphogenesis; IMP:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF00514; Arm; 3.
DR   SMART; SM00185; ARM; 6.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Cell membrane; Coiled coil;
KW   Cytoplasm; Membrane; Nucleus; Phosphoprotein; Repeat; Transcription;
KW   Transcription regulation; Wnt signaling pathway.
FT   CHAIN         1    938       Catenin delta-1.
FT                                /FTId=PRO_0000064297.
FT   REPEAT      358    395       ARM 1.
FT   REPEAT      398    437       ARM 2.
FT   REPEAT      441    475       ARM 3.
FT   REPEAT      476    516       ARM 4.
FT   REPEAT      534    573       ARM 5.
FT   REPEAT      583    624       ARM 6.
FT   REPEAT      653    693       ARM 7.
FT   REPEAT      700    739       ARM 8.
FT   REPEAT      740    780       ARM 9.
FT   REPEAT      781    826       ARM 10.
FT   COILED       10     46       Potential.
FT   MOTIF       622    635       Nuclear localization signal.
FT   MOD_RES      47     47       Phosphoserine (By similarity).
FT   MOD_RES      96     96       Phosphotyrosine (By similarity).
FT   MOD_RES     174    174       Phosphotyrosine (By similarity).
FT   MOD_RES     193    193       Phosphotyrosine (By similarity).
FT   MOD_RES     208    208       Phosphotyrosine (By similarity).
FT   MOD_RES     213    213       Phosphotyrosine (By similarity).
FT   MOD_RES     217    217       Phosphotyrosine (By similarity).
FT   MOD_RES     228    228       Phosphotyrosine.
FT   MOD_RES     230    230       Phosphoserine.
FT   MOD_RES     232    232       Phosphoserine (By similarity).
FT   MOD_RES     244    244       Phosphoserine (By similarity).
FT   MOD_RES     248    248       Phosphotyrosine (By similarity).
FT   MOD_RES     252    252       Phosphoserine.
FT   MOD_RES     257    257       Phosphotyrosine.
FT   MOD_RES     268    268       Phosphoserine (By similarity).
FT   MOD_RES     269    269       Phosphoserine.
FT   MOD_RES     280    280       Phosphotyrosine (By similarity).
FT   MOD_RES     288    288       Phosphoserine.
FT   MOD_RES     291    291       Phosphotyrosine.
FT   MOD_RES     302    302       Phosphotyrosine (By similarity).
FT   MOD_RES     310    310       Phosphothreonine (By similarity).
FT   MOD_RES     320    320       Phosphoserine.
FT   MOD_RES     321    321       Phosphotyrosine (By similarity).
FT   MOD_RES     334    334       Phosphotyrosine (By similarity).
FT   MOD_RES     346    346       Phosphoserine.
FT   MOD_RES     349    349       Phosphoserine.
FT   MOD_RES     352    352       Phosphoserine.
FT   MOD_RES     857    857       Phosphoserine.
FT   MOD_RES     859    859       Phosphoserine.
FT   MOD_RES     864    864       Phosphoserine.
FT   MOD_RES     865    865       Phosphotyrosine.
FT   MOD_RES     869    869       Phosphothreonine (By similarity).
FT   MOD_RES     904    904       Phosphotyrosine.
FT   MOD_RES     916    916       Phosphothreonine (By similarity).
FT   MOD_RES     920    920       Phosphoserine.
FT   VAR_SEQ     626    631       Missing (in isoform 2).
FT                                /FTId=VSP_030567.
FT   VAR_SEQ     880    900       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_030568.
FT   MUTAGEN     622    623       KK->AA: Abolishes nuclear localization.
FT   CONFLICT    405    405       R -> A (in Ref. 1; CAA79078).
FT   CONFLICT    676    676       K -> N (in Ref. 1; CAA79078).
FT   CONFLICT    715    715       I -> R (in Ref. 1; CAA79078).
FT   CONFLICT    752    752       I -> R (in Ref. 1; CAA79078).
SQ   SEQUENCE   938 AA;  104925 MW;  2F13DB7350355832 CRC64;
     MDDSEVESTA SILASVKEQE AQFEKLTRAL EEERRHVSAQ LERVRVSPQD ANSLMANGTL
     TRRHQNGRFV GDADLERQKF SDLKLNGPQD HNHLLYSTIP RMQEPGQIVE TYTEEDPEGA
     MSVVSVETTD DGTTRRTETT VKKVVKTMTT RTVQPVPMGP DGLPVDASAV SNNYIQTLGR
     DFRKNGNGGP GPYVGQAGTA TLPRNFHYPP DGYGRHYEDG YPGGSDNYGS LSRVTRIEER
     YRPSMEGYRA PSRQDVYGPQ PQVRVGGSSV DLHRFHPEPY GLEDDQRSMG YDDLDYGMMS
     DYGTARRTGT PSDPRRRLRS YEDMIGEEVP PDQYYWAPLA QHERGSLASL DSLRKGMPPP
     SNWRQPELPE VIAMLGFRLD AVKSNAAAYL QHLCYRNDKV KTDVRKLKGI PILVGLLDHP
     KKEVHLGACG ALKNISFGRD QDNKIAIKNC DGVPALVRLL RKARDMDLTE VITGTLWNLS
     SHDSIKMEIV DHALHALTDE VIIPHSGWER EPNEDCKPRH IEWESVLTNT AGCLRNVSSE
     RSEARRKLRE CDGLVDALIF IVQAEIGQKD SDSKLVENCV CLLRNLSYQV HREIPQAERY
     QEALPTVANS TGPHAASCFG AKKGKDEWFS RGKKPTEDPA NDTVDFPKRT SPARGYELLF
     QPEVVRIYIS LLKESKTPAI LEASAGAIQN LCAGRWTYGR YIRSALRQEK ALSAIAELLT
     SEHERVVKAA SGALRNLAVD ARNKELIGKH AIPNLVKNLP GGQQNSSWNF SEDTVVSILN
     TINEVIAENL EAAKKLRETQ GIEKLVLINK SGNRSEKEVR AAALVLQTIW GYKELRKPLE
     KEGWKKSDFQ VNLNNASRSQ SSHSYDDSTL PLIDRNQKSD KKPDREEIPM SNMGSNTKSL
     DNNYSTLNER GDHNRTLDRS GDLGDMEPLK GAPLMQKI
//
ID   DESM_MOUSE              Reviewed;         469 AA.
AC   P31001;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Desmin;
GN   Name=Des;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94165148; PubMed=8120103; DOI=10.1083/jcb.124.5.827;
RA   Li H., Choudhary S.K., Milner D.J., Munir M.I., Kuisk I.R.,
RA   Capetanaki Y.;
RT   "Inhibition of desmin expression blocks myoblast fusion and interferes
RT   with the myogenic regulators MyoD and myogenin.";
RL   J. Cell Biol. 124:827-841(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 1-40.
RC   STRAIN=BALB/c; TISSUE=Spleen;
RX   MEDLINE=93181210; PubMed=8382796; DOI=10.1093/nar/21.2.335;
RA   Li H., Capetanaki Y.;
RT   "Regulation of the mouse desmin gene: transactivated by MyoD,
RT   myogenin, MRF4 and Myf5.";
RL   Nucleic Acids Res. 21:335-343(1993).
CC   -!- FUNCTION: Desmin are class-III intermediate filaments found in
CC       muscle cells. In adult striated muscle they form a fibrous network
CC       connecting myofibrils to each other and to the plasma membrane
CC       from the periphery of the Z-line structures.
CC   -!- SUBUNIT: Homopolymer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
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DR   EMBL; L22550; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC031760; AAH31760.1; -; mRNA.
DR   EMBL; Z18892; CAA79330.1; -; Genomic_DNA.
DR   IPI; IPI00130102; -.
DR   PIR; A54104; A54104.
DR   RefSeq; NP_034173.1; NM_010043.1.
DR   UniGene; Mm.6712; -.
DR   ProteinModelPortal; P31001; -.
DR   SMR; P31001; 105-142, 152-253, 267-410.
DR   DIP; DIP-256N; -.
DR   MINT; MINT-220806; -.
DR   STRING; P31001; -.
DR   PhosphoSite; P31001; -.
DR   SWISS-2DPAGE; P31001; -.
DR   PRIDE; P31001; -.
DR   Ensembl; ENSMUST00000027409; ENSMUSP00000027409; ENSMUSG00000026208.
DR   GeneID; 13346; -.
DR   KEGG; mmu:13346; -.
DR   UCSC; uc007box.1; mouse.
DR   CTD; 13346; -.
DR   MGI; MGI:94885; Des.
DR   eggNOG; roNOG11511; -.
DR   HOGENOM; HBG715391; -.
DR   HOVERGEN; HBG013015; -.
DR   InParanoid; P31001; -.
DR   OMA; SSEMHSK; -.
DR   OrthoDB; EOG4H9XKM; -.
DR   PhylomeDB; P31001; -.
DR   NextBio; 283662; -.
DR   PMAP-CutDB; P31001; -.
DR   ArrayExpress; P31001; -.
DR   Bgee; P31001; -.
DR   CleanEx; MM_DES; -.
DR   Genevestigator; P31001; -.
DR   GermOnline; ENSMUSG00000026208; Mus musculus.
DR   GO; GO:0005626; C:insoluble fraction; IDA:MGI.
DR   GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0030018; C:Z disc; IDA:MGI.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:MGI.
DR   GO; GO:0007517; P:muscle organ development; TAS:MGI.
DR   InterPro; IPR016044; F.
DR   InterPro; IPR001664; IF.
DR   InterPro; IPR006821; Intermed_filament_DNA-bd.
DR   InterPro; IPR018039; Intermediate_filament_CS.
DR   PANTHER; PTHR23239; IF; 1.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF04732; Filament_head; 1.
DR   PROSITE; PS00226; IF; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Intermediate filament; Muscle protein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    469       Desmin.
FT                                /FTId=PRO_0000063773.
FT   REGION        2    108       Head.
FT   REGION      109    411       Rod.
FT   REGION      109    140       Coil 1A.
FT   REGION      141    150       Linker 1.
FT   REGION      151    251       Coil 1B.
FT   REGION      252    267       Linker 12.
FT   REGION      268    286       Coil 2A.
FT   REGION      287    294       Linker 2.
FT   REGION      295    411       Coil 2B.
FT   REGION      412    469       Tail.
FT   COMPBIAS     45     48       Poly-Ser.
FT   SITE        353    353       Stutter.
SQ   SEQUENCE   469 AA;  53498 MW;  58A8A13C7CC11EEF CRC64;
     MSQAYSSSQR VSSYRRTFGG APGFSLGSPL SSPVFPRAGF GTKGSSSSMT SRVYQVSRTS
     GGAGGLGSLR SSRLGTTRAP SYGAGELLDF SLADAVNQEF LATRTNEKVE LQELNDRFAN
     YIEKVRFLEQ QNAALAAEVN RLKGREPTRV AELYEEEMRE LRRQVEVLTN QRARVDVERD
     NLIDDLQRLK AKLQEEIQLR EEAENNLAAF RADVDAATLA RIDLERRIES LNEEIAFLKK
     VHEEEIRELQ AQLQEQQVQV EMDMSKPDLT AALRDIRAQY ETIAAKNISE AEEWYKSKVS
     DLTQAANKNN DALRQAKQEM MEYRHQIQSY TCEIDALKGT NDSLMRQMRE LEDRFASEAN
     GYQDNIARLE EEIRHLKDEM ARHLREYQDL LNVKMALDVE IATYRKLLEG EESRINLPIQ
     TFSALNFRET SPEQRGSEVH TKKTVMIKTI ETRDGEVVSE ATQQQHEVL
//
ID   KAP3_MOUSE              Reviewed;         416 AA.
AC   P31324; B1B199; Q3UTZ1; Q80ZM4; Q8BRZ7;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=cAMP-dependent protein kinase type II-beta regulatory subunit;
GN   Name=Prkar2b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
RX   MEDLINE=91298951; PubMed=2069562; DOI=10.1016/0006-291X(91)91802-J;
RA   Singh I.S., Luo Z., Eng A., Erlichman J.;
RT   "Molecular cloning and characterization of the promoter region of the
RT   mouse regulatory subunit RII beta of type II cAMP-dependent protein
RT   kinase.";
RL   Biochem. Biophys. Res. Commun. 178:221-226(1991).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Type II regulatory chains mediate membrane association
CC       by binding to anchoring proteins, including the MAP2 kinase.
CC   -!- SUBUNIT: The inactive form of the enzyme is composed of two
CC       regulatory chains and two catalytic chains. Activation by cAMP
CC       produces two active catalytic monomers and a regulatory dimer that
CC       binds four cAMP molecules.
CC   -!- TISSUE SPECIFICITY: Four types of regulatory chains are found: I-
CC       alpha, I-beta, II-alpha, and II-beta. Their expression varies
CC       among tissues and is in some cases constitutive and in others
CC       inducible.
CC   -!- PTM: Phosphorylated by the activated catalytic chain.
CC   -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC       family.
CC   -!- SIMILARITY: Contains 2 cyclic nucleotide-binding domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK041013; BAC30779.1; -; mRNA.
DR   EMBL; AK138963; BAE23838.1; -; mRNA.
DR   EMBL; CT010463; CAM17140.1; -; Genomic_DNA.
DR   EMBL; BC048710; AAH48710.1; -; mRNA.
DR   EMBL; M68861; AAA40057.1; -; Genomic_DNA.
DR   IPI; IPI00224570; -.
DR   PIR; PQ0161; PQ0161.
DR   RefSeq; NP_035288.2; NM_011158.3.
DR   UniGene; Mm.480655; -.
DR   ProteinModelPortal; P31324; -.
DR   SMR; P31324; 5-41, 103-412.
DR   STRING; P31324; -.
DR   PhosphoSite; P31324; -.
DR   PRIDE; P31324; -.
DR   Ensembl; ENSMUST00000003079; ENSMUSP00000003079; ENSMUSG00000002997.
DR   Ensembl; ENSMUST00000036497; ENSMUSP00000039797; ENSMUSG00000002997.
DR   GeneID; 19088; -.
DR   KEGG; mmu:19088; -.
DR   UCSC; uc007nhx.1; mouse.
DR   CTD; 19088; -.
DR   MGI; MGI:97760; Prkar2b.
DR   eggNOG; roNOG05504; -.
DR   HOGENOM; HBG736470; -.
DR   HOVERGEN; HBG002025; -.
DR   InParanoid; P31324; -.
DR   OMA; TYDIYVK; -.
DR   OrthoDB; EOG4RV2RN; -.
DR   PhylomeDB; P31324; -.
DR   NextBio; 295636; -.
DR   ArrayExpress; P31324; -.
DR   Bgee; P31324; -.
DR   Genevestigator; P31324; -.
DR   GermOnline; ENSMUSG00000002997; Mus musculus.
DR   GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; IDA:MGI.
DR   GO; GO:0008283; P:cell proliferation; TAS:MGI.
DR   GO; GO:0006631; P:fatty acid metabolic process; IMP:MGI.
DR   GO; GO:0007612; P:learning; IMP:MGI.
DR   GO; GO:0009887; P:organ morphogenesis; TAS:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; TAS:MGI.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR002373; cAMP/cGMP_kin.
DR   InterPro; IPR012198; cAMP_dep_PK_reg_su.
DR   InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 2.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF02197; RIIa; 1.
DR   PIRSF; PIRSF000548; PK_regulatory; 1.
DR   PRINTS; PR00103; CAMPKINASE.
DR   SMART; SM00100; cNMP; 2.
DR   SMART; SM00394; RIIa; 1.
DR   SUPFAM; SSF47391; cAMP-dep_prot_kin_reg_I/II_a/b; 1.
DR   SUPFAM; SSF51206; cNMP_binding; 2.
DR   PROSITE; PS00888; CNMP_BINDING_1; 2.
DR   PROSITE; PS00889; CNMP_BINDING_2; 2.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
PE   1: Evidence at protein level;
KW   Acetylation; cAMP; cAMP-binding; Nucleotide-binding; Phosphoprotein;
KW   Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    416       cAMP-dependent protein kinase type II-
FT                                beta regulatory subunit.
FT                                /FTId=PRO_0000205391.
FT   NP_BIND     152    273       cAMP 1.
FT   NP_BIND     274    416       cAMP 2.
FT   REGION        2    151       Dimerization and phosphorylation.
FT   BINDING     221    221       cAMP 1 (By similarity).
FT   BINDING     230    230       cAMP 1 (By similarity).
FT   BINDING     350    350       cAMP 2 (By similarity).
FT   BINDING     359    359       cAMP 2 (By similarity).
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES      83     83       Phosphoserine (By similarity).
FT   MOD_RES      85     85       Phosphoserine (By similarity).
FT   MOD_RES     112    112       Phosphoserine.
FT   CONFLICT     69     69       I -> T (in Ref. 3; AAH48710).
SQ   SEQUENCE   416 AA;  46167 MW;  24196C3037789827 CRC64;
     MSIEIPAGLT ELLQGFTVEV LRHQPADLLE FALQHFTRLQ QENERKGAAR FGHEGRTWGD
     AGAAAGGGIP SKGVNFAEEP MRSDSENGEE EEAAEAGAFN APVINRFTRR ASVCAEAYNP
     DEEEDDAESR IIHPKTDDQR NRLQEACKDI LLFKNLDPEQ MSQVLDAMFE KLVKEGEHVI
     DQGDDGDNFY VIDRGTFDIY VKCDGVGRCV GNYDNRGSFG ELALMYNTPR AATITATSPG
     ALWGLDRVTF RRIIVKNNAK KRKMYESFIE SLPFLKSLEV SERLKVVDVI GTKVYNDGEQ
     IIAQGDLADS FFIVESGEVK ITMKRKGKSE VEENGAVEIA RCFRGQYFGE LALVTNKPRA
     ASAHAIGTVK CLAMDVQAFE RLLGPCMEIM KRNIATYEEQ LVALFGTNMD IVEPTA
//
ID   SC6A1_MOUSE             Reviewed;         599 AA.
AC   P31648;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Sodium- and chloride-dependent GABA transporter 1;
DE            Short=GAT-1;
DE   AltName: Full=Solute carrier family 6 member 1;
GN   Name=Slc6a1; Synonyms=Gabt1, Gat-1, Gat1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   MEDLINE=92335351; PubMed=1631167; DOI=10.1073/pnas.89.14.6639;
RA   Liu Q.-R., Mandiyan S., Nelson H., Nelson N.;
RT   "A family of genes encoding neurotransmitter transporters.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:6639-6643(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Eye, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   INTERACTION WITH MPP5, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=15234345; DOI=10.1016/j.mcn.2004.03.006;
RA   McHugh E.M., Zhu W., Milgram S., Mager S.;
RT   "The GABA transporter GAT1 and the MAGUK protein Pals1: interaction,
RT   uptake modulation, and coexpression in the brain.";
RL   Mol. Cell. Neurosci. 26:406-417(2004).
CC   -!- FUNCTION: Terminates the action of GABA by its high affinity
CC       sodium-dependent reuptake into presynaptic terminals.
CC   -!- SUBUNIT: Interacts with MPP5.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity). Membrane; Multi-pass membrane protein (By
CC       similarity). Note=Localized at the plasma membrane and in a subset
CC       of intracellular vesicles (By similarity). Localized at the
CC       presynaptic terminals of interneurons.
CC   -!- TISSUE SPECIFICITY: Brain. Expressed in the dentate gyrus of
CC       hippocampus, striatum and cerebellum (at protein level).
CC   -!- DOMAIN: The PDZ domain-binding motif is involved in the
CC       interaction with MPP5 (By similarity).
CC   -!- MISCELLANEOUS: This protein is the target of psychomotor
CC       stimulants such as amphetamines or cocaine.
CC   -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF)
CC       (TC 2.A.22) family. SLC6A1 subfamily.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; M92377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M92378; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK042956; BAC31418.1; -; mRNA.
DR   EMBL; AK052971; BAC35226.1; -; mRNA.
DR   EMBL; AK053883; BAC35574.1; -; mRNA.
DR   IPI; IPI00227928; -.
DR   PIR; F46027; F46027.
DR   RefSeq; NP_848818.1; NM_178703.4.
DR   UniGene; Mm.5260; -.
DR   ProteinModelPortal; P31648; -.
DR   SMR; P31648; 43-549.
DR   STRING; P31648; -.
DR   PhosphoSite; P31648; -.
DR   PRIDE; P31648; -.
DR   Ensembl; ENSMUST00000032454; ENSMUSP00000032454; ENSMUSG00000030310.
DR   GeneID; 232333; -.
DR   KEGG; mmu:232333; -.
DR   UCSC; uc009dhv.1; mouse.
DR   CTD; 232333; -.
DR   MGI; MGI:95627; Slc6a1.
DR   eggNOG; roNOG04622; -.
DR   HOGENOM; HBG702834; -.
DR   HOVERGEN; HBG071421; -.
DR   InParanoid; P31648; -.
DR   OMA; TDLPDRD; -.
DR   OrthoDB; EOG4JQ3X4; -.
DR   PhylomeDB; P31648; -.
DR   NextBio; 381034; -.
DR   ArrayExpress; P31648; -.
DR   Bgee; P31648; -.
DR   Genevestigator; P31648; -.
DR   GermOnline; ENSMUSG00000030310; Mus musculus.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0005887; C:integral to plasma membrane; IEA:InterPro.
DR   GO; GO:0005328; F:neurotransmitter:sodium symporter activity; IEA:InterPro.
DR   InterPro; IPR000175; Na/ntran_symport.
DR   InterPro; IPR002980; Na/ntran_symport_GABA_GAT1.
DR   PANTHER; PTHR11616; Na/ntran_symport; 1.
DR   Pfam; PF00209; SNF; 1.
DR   PRINTS; PR01195; GAT1TRNSPORT.
DR   PRINTS; PR00176; NANEUSMPORT.
DR   PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR   PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
DR   PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Membrane; Neurotransmitter transport;
KW   Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    599       Sodium- and chloride-dependent GABA
FT                                transporter 1.
FT                                /FTId=PRO_0000214744.
FT   TOPO_DOM      1     52       Cytoplasmic (Potential).
FT   TRANSMEM     53     73       Helical; Name=1; (Potential).
FT   TRANSMEM     81    100       Helical; Name=2; (Potential).
FT   TRANSMEM    124    144       Helical; Name=3; (Potential).
FT   TOPO_DOM    145    211       Extracellular (Potential).
FT   TRANSMEM    212    230       Helical; Name=4; (Potential).
FT   TRANSMEM    239    256       Helical; Name=5; (Potential).
FT   TRANSMEM    292    309       Helical; Name=6; (Potential).
FT   TRANSMEM    321    342       Helical; Name=7; (Potential).
FT   TRANSMEM    375    394       Helical; Name=8; (Potential).
FT   TRANSMEM    422    440       Helical; Name=9; (Potential).
FT   TRANSMEM    457    477       Helical; Name=10; (Potential).
FT   TRANSMEM    498    517       Helical; Name=11; (Potential).
FT   TRANSMEM    536    554       Helical; Name=12; (Potential).
FT   TOPO_DOM    555    599       Cytoplasmic (Potential).
FT   MOTIF       597    599       PDZ-binding.
FT   CARBOHYD    176    176       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    181    181       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    184    184       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    117    118       KL -> NW (in Ref. 1; M92378).
FT   CONFLICT    126    127       GL -> AV (in Ref. 1; M92378).
FT   CONFLICT    212    213       WP -> C (in Ref. 1; M92378).
FT   CONFLICT    285    286       WL -> IF (in Ref. 1; M92378).
SQ   SEQUENCE   599 AA;  67001 MW;  4FEF85092DC1D045 CRC64;
     MATDNSKVAD GQISTEVSEA PVASDKPKTL VVKVQKKAGD LPDRDTWKGR FDFLMSCVGY
     AIGLGNVWRF PYLCGKNGGG AFLIPYFLTL IFAGVPLFLL ECSLGQYTSI GGLGVWKLAP
     MFKGVGLAAA VLSFWLNIYY IVIISWAIYY LYNSFTTTLP WKQCDNPWNT DRCFSNYSLV
     NTTNMTSAVV EFWERNMHQM TDGLDKPGQI RWPLAITLAI AWVLVYFCIW KGVGWTGKVV
     YFSATYPYIM LIILFFRGVT LPGAKEGILF YITPNFRKLS DSEVWLDAAT QIFFSYGLGL
     GSLIALGSYN SFHNNVYRDS IIVCCINSCT SMFAGFVIFS IVGFMAHVTK RSIADVAASG
     PGLAFLAYPE AVTQLPISPL WAILFFSMLL MLGIDSQFCT VEGFITALVD EYPRLLRNRR
     ELFIAAVCIV SYLIGLSNIT QGGIYVFKLF DYYSASGMSL LFLVFFECVS ISWFYGVNRF
     YDNIQEMVGS RPCIWWKLCW SFFTPIIVAG VFLFSAVQMT PLTMGSYVFP KWGQGVGWLM
     ALSSMVLIPG YMAYMFLTLK GSLKQRLQVM IQPSEDIVRP ENGPEQPQAG SSASKEAYI
//
ID   S6A13_MOUSE             Reviewed;         602 AA.
AC   P31649;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Sodium- and chloride-dependent GABA transporter 2;
DE            Short=GAT-2;
DE   AltName: Full=Sodium- and chloride-dependent GABA transporter 3;
DE            Short=GAT-3;
DE   AltName: Full=Solute carrier family 6 member 13;
GN   Name=Slc6a13; Synonyms=Gabt2, Gabt3, Gat-3, Gat2, Gat3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=93131969; PubMed=8420981;
RA   Liu Q.-R., Lopez-Coecuera B., Mandiyan S., Nelson H., Nelson N.;
RT   "Molecular characterization of four pharmacologically distinct gamma-
RT   aminobutyric acid transporters in mouse brain.";
RL   J. Biol. Chem. 268:2106-2112(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney, and Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-587 AND SER-591, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Terminates the action of GABA by its high affinity
CC       sodium-dependent reuptake into presynaptic terminals. Can also
CC       transport beta-alanine and taurine.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=18 uM for GABA;
CC         KM=28 uM for beta-alanine;
CC         KM=540 uM for taurine;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Brain, liver and kidney.
CC   -!- DEVELOPMENTAL STAGE: Abundant in neonatal brain but not in adult
CC       brain.
CC   -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF)
CC       (TC 2.A.22) family. SLC6A13 subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; L04663; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC023117; AAH23117.1; -; mRNA.
DR   EMBL; BC029637; AAH29637.1; -; mRNA.
DR   IPI; IPI00136863; -.
DR   PIR; A44409; A44409.
DR   RefSeq; NP_653095.1; NM_144512.2.
DR   UniGene; Mm.258596; -.
DR   ProteinModelPortal; P31649; -.
DR   STRING; P31649; -.
DR   TCDB; 2.A.22.3.8; neurotransmitter:sodium symporter (NSS) family.
DR   PhosphoSite; P31649; -.
DR   PRIDE; P31649; -.
DR   Ensembl; ENSMUST00000064580; ENSMUSP00000066779; ENSMUSG00000030108.
DR   GeneID; 14412; -.
DR   KEGG; mmu:14412; -.
DR   UCSC; uc009doj.1; mouse.
DR   CTD; 14412; -.
DR   MGI; MGI:95629; Slc6a13.
DR   eggNOG; roNOG05228; -.
DR   HOGENOM; HBG702834; -.
DR   HOVERGEN; HBG071421; -.
DR   InParanoid; P31649; -.
DR   OMA; YASQMIV; -.
DR   OrthoDB; EOG43N7CD; -.
DR   PhylomeDB; P31649; -.
DR   NextBio; 285993; -.
DR   ArrayExpress; P31649; -.
DR   Bgee; P31649; -.
DR   Genevestigator; P31649; -.
DR   GermOnline; ENSMUSG00000030108; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; IEA:InterPro.
DR   GO; GO:0005328; F:neurotransmitter:sodium symporter activity; IEA:InterPro.
DR   InterPro; IPR000175; Na/ntran_symport.
DR   InterPro; IPR002981; Na/ntran_symport_GABA_GAT2.
DR   PANTHER; PTHR11616; Na/ntran_symport; 1.
DR   Pfam; PF00209; SNF; 1.
DR   PRINTS; PR01196; GAT2TRNSPORT.
DR   PRINTS; PR00176; NANEUSMPORT.
DR   PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR   PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
DR   PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Neurotransmitter transport; Phosphoprotein;
KW   Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    602       Sodium- and chloride-dependent GABA
FT                                transporter 2.
FT                                /FTId=PRO_0000214793.
FT   TOPO_DOM      1     40       Cytoplasmic (Potential).
FT   TRANSMEM     41     61       Helical; Name=1; (Potential).
FT   TRANSMEM     68     88       Helical; Name=2; (Potential).
FT   TRANSMEM    121    141       Helical; Name=3; (Potential).
FT   TOPO_DOM    142    206       Extracellular (Potential).
FT   TRANSMEM    207    227       Helical; Name=4; (Potential).
FT   TRANSMEM    233    253       Helical; Name=5; (Potential).
FT   TRANSMEM    282    302       Helical; Name=6; (Potential).
FT   TRANSMEM    319    339       Helical; Name=7; (Potential).
FT   TRANSMEM    366    386       Helical; Name=8; (Potential).
FT   TRANSMEM    418    438       Helical; Name=9; (Potential).
FT   TRANSMEM    453    473       Helical; Name=10; (Potential).
FT   TRANSMEM    490    510       Helical; Name=11; (Potential).
FT   TRANSMEM    528    548       Helical; Name=12; (Potential).
FT   TOPO_DOM    549    602       Cytoplasmic (Potential).
FT   MOD_RES     587    587       Phosphothreonine.
FT   MOD_RES     591    591       Phosphoserine.
FT   CARBOHYD    169    169       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    173    173       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    178    178       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    269    269       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   602 AA;  68285 MW;  372FE77F3126ABEA CRC64;
     MENRASGTTS NGETKPVCPA MEKVEEDGTL EREHWNNKME FVLSVAGEII GLGNVWRFPY
     LCYKNGGGAF FIPYLIFLFT CGIPVFFLET ALGQYTNQGG ITAWRRICPI FEGIGYASQM
     IVSLLNVYYI VVLAWALFYL FSSFTTDLPW GSCSHEWNTE NCVEFQKAND SMNVTSENAT
     SPVIEFWERR VLKLSDGIQH LGSLRWELVL CLLLAWIICY FCIWKGVKST GKVVYFTATF
     PYLMLVVLLI RGVTLPGAAQ GIQFYLYPNI TRLWDPQVWM DAGTQIFFSF AICLGCLTAL
     GSYNKYHNNC YRDCIALCIL NSSTSFMAGF AIFSILGFMS QEQGVPISEV AESGPGLAFI
     AYPRAVVMLP FSPLWACCFF FMVVLLGLDS QFVCVESLVT ALVDMYPRVF RKKNRREVLI
     LIVSVISFFI GLIMLTEGGM YVFQLFDYYA ASGMCLLFVA IFESLCVAWV YGAGRFYDNI
     EDMIGYKPWP LIKYCWLFFT PAVCLATFLF SLIKYTPLTY NKKYTYPWWG DALGWLLALS
     SMICIPAWSI YKLRTLKGPL RERLRQLVCP AEDLPQKNQP EPTAPATPMT SLLRLTELES
     NC
//
ID   S6A11_MOUSE             Reviewed;         627 AA.
AC   P31650;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Sodium- and chloride-dependent GABA transporter 3;
DE            Short=GAT-3;
DE   AltName: Full=Sodium- and chloride-dependent GABA transporter 4;
DE            Short=GAT-4;
DE   AltName: Full=Solute carrier family 6 member 11;
GN   Name=Slc6a11; Synonyms=Gabt3, Gabt4, Gat-4, Gat3, Gat4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=93131969; PubMed=8420981;
RA   Liu Q.-R., Lopez-Coecuera B., Mandiyan S., Nelson H., Nelson N.;
RT   "Molecular characterization of four pharmacologically distinct gamma-
RT   aminobutyric acid transporters in mouse brain.";
RL   J. Biol. Chem. 268:2106-2112(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 20-35 AND 206-220, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Terminates the action of GABA by its high affinity
CC       sodium-dependent reuptake into presynaptic terminals. Can also
CC       transport beta-alanine and taurine.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.8 uM for GABA;
CC         KM=99 uM for beta-alanine;
CC         KM=1.4 mM for taurine;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Brain.
CC   -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF)
CC       (TC 2.A.22) family. SLC6A11 subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; L04662; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00136867; -.
DR   PIR; B44409; B44409.
DR   UniGene; Mm.44683; -.
DR   UniGene; Mm.448312; -.
DR   ProteinModelPortal; P31650; -.
DR   STRING; P31650; -.
DR   PhosphoSite; P31650; -.
DR   PRIDE; P31650; -.
DR   Ensembl; ENSMUST00000032451; ENSMUSP00000032451; ENSMUSG00000030307.
DR   MGI; MGI:95630; Slc6a11.
DR   eggNOG; maNOG12013; -.
DR   HOGENOM; HBG702834; -.
DR   HOVERGEN; HBG071421; -.
DR   InParanoid; P31650; -.
DR   OrthoDB; EOG4BCDMH; -.
DR   ArrayExpress; P31650; -.
DR   Bgee; P31650; -.
DR   Genevestigator; P31650; -.
DR   GermOnline; ENSMUSG00000030307; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; IEA:InterPro.
DR   GO; GO:0005328; F:neurotransmitter:sodium symporter activity; IEA:InterPro.
DR   InterPro; IPR000175; Na/ntran_symport.
DR   InterPro; IPR002982; Na/ntran_symport_GABA_GAT3.
DR   PANTHER; PTHR11616; Na/ntran_symport; 1.
DR   Pfam; PF00209; SNF; 1.
DR   PRINTS; PR01197; GAT3TRNSPORT.
DR   PRINTS; PR00176; NANEUSMPORT.
DR   PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR   PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
DR   PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Membrane;
KW   Neurotransmitter transport; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    627       Sodium- and chloride-dependent GABA
FT                                transporter 3.
FT                                /FTId=PRO_0000214785.
FT   TOPO_DOM      1     53       Cytoplasmic (Potential).
FT   TRANSMEM     54     74       Helical; Name=1; (Potential).
FT   TRANSMEM     82    101       Helical; Name=2; (Potential).
FT   TRANSMEM    126    146       Helical; Name=3; (Potential).
FT   TOPO_DOM    147    220       Extracellular (Potential).
FT   TRANSMEM    221    239       Helical; Name=4; (Potential).
FT   TRANSMEM    248    265       Helical; Name=5; (Potential).
FT   TRANSMEM    301    318       Helical; Name=6; (Potential).
FT   TRANSMEM    330    351       Helical; Name=7; (Potential).
FT   TRANSMEM    384    403       Helical; Name=8; (Potential).
FT   TRANSMEM    433    451       Helical; Name=9; (Potential).
FT   TRANSMEM    468    488       Helical; Name=10; (Potential).
FT   TRANSMEM    509    528       Helical; Name=11; (Potential).
FT   TRANSMEM    548    566       Helical; Name=12; (Potential).
FT   TOPO_DOM    567    627       Cytoplasmic (Potential).
FT   CARBOHYD    182    182       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    185    185       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    193    193       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   627 AA;  69889 MW;  E6D4E45FC92C4CB7 CRC64;
     MTAEQALPLG NGKAAEEARG SETLGGGGGG AAGTREARDK AVHERGHWNN KVEFVLSVAG
     EIIGLGNVWR FPYLCYKNGG GAFLIPYVVF FICCGIPVFF LETALGQFTS EGGITCWRRV
     CPLFEGIGYA TQVIEAHLNV YYIIILAWAI FYLSNCFTTE LPWATCGHEW NTEKCVEFQK
     LNFSNYSHVS LQNATSPVME FWERRVLAIS DGIEHIGNLR WELALCLLAG WTICYFCIWK
     GTKSTGKVVY VTATFPYIML LILLIRGVTL PGASEGIKFY LYPDLSRLSD PQVWVDAGTQ
     IFFSYAICLG CLTALGSYNN YNNNCYRDCI MLCCLNSGTS FVAGFAIFSV LGFMAYEQGV
     PIAEVAESGP GLAFIAYPKA VTMMPLSPLW ATLFFMMLIF LGLDSQFVCV ESLVTAVVDM
     YPKVFRRGYR RELLILALSI ISYFLGLVML TEGGMYIFQL FGSYAASGMC LLFVAIFECV
     CIGWVYGSNR FYDNIEDMIG YRPLSLIKWC WKVVTPGICA GIFIFFLVKY KPLKYNNVYT
     YPAWGYGIGW LMALSSMLCI PLWIFIKLWK TEGTLPEKLQ KLTVPSADLK MRGKLGASPR
     TVTVNDCEAK VKGDGTISAI TEKETHF
//
ID   AKT1_MOUSE              Reviewed;         480 AA.
AC   P31750; Q62274;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   08-MAR-2011, entry version 121.
DE   RecName: Full=RAC-alpha serine/threonine-protein kinase;
DE            EC=2.7.11.1;
DE   AltName: Full=AKT1 kinase;
DE   AltName: Full=Protein kinase B;
DE            Short=PKB;
DE   AltName: Full=Proto-oncogene c-Akt;
DE   AltName: Full=RAC-PK-alpha;
DE   AltName: Full=Thymoma viral proto-oncogene;
GN   Name=Akt1; Synonyms=Akt, Rac;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Bousquets X., Powell C.T.;
RT   "Complete nucleotide coding sequence for murine rac (related to A and
RT   C kinases) protein kinase.";
RL   Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=AKR/J; TISSUE=Thymus;
RX   MEDLINE=93173519; PubMed=8437858;
RA   Bellacosa A., Franke T.F., Gonzalez-Portal M.E., Datta K., Taguchi T.,
RA   Gardner J., Cheng J.Q., Testa J.R., Tsichlis P.N.;
RT   "Structure, expression and chromosomal mapping of c-akt: relationship
RT   to v-akt and its implications.";
RL   Oncogene 8:745-754(1993).
RN   [3]
RP   FUNCTION, AND MUTAGENESIS OF LYS-179.
RX   PubMed=9415393; DOI=10.1210/me.11.13.1881;
RA   Cong L.N., Chen H., Li Y., Zhou L., McGibbon M.A., Taylor S.I.,
RA   Quon M.J.;
RT   "Physiological role of Akt in insulin-stimulated translocation of
RT   GLUT4 in transfected rat adipose cells.";
RL   Mol. Endocrinol. 11:1881-1890(1997).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=10716693; DOI=10.1073/pnas.040557697;
RA   Pekarsky Y., Koval A., Hallas C., Bichi R., Tresini M., Malstrom S.,
RA   Russo G., Tsichlis P., Croce C.M.;
RT   "Tcl1 enhances Akt kinase activity and mediates its nuclear
RT   translocation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:3028-3033(2000).
RN   [5]
RP   FUNCTION.
RX   PubMed=11282895;
RA   Yamashita K., Kajstura J., Discher D.J., Wasserlauf B.J.,
RA   Bishopric N.H., Anversa P., Webster K.A.;
RT   "Reperfusion-activated Akt kinase prevents apoptosis in transgenic
RT   mouse hearts overexpressing insulin-like growth factor-1.";
RL   Circ. Res. 88:609-614(2001).
RN   [6]
RP   INTERACTION WITH THEM4.
RX   PubMed=11598301; DOI=10.1126/science.1062030;
RA   Maira S.-M., Galetic I., Brazil D.P., Kaech S., Ingley E., Thelen M.,
RA   Hemmings B.A.;
RT   "Carboxyl-terminal modulator protein (CTMP), a negative regulator of
RT   PKB/Akt and v-Akt at the plasma membrane.";
RL   Science 294:374-380(2001).
RN   [7]
RP   FUNCTION IN PHOSPHORYLATION OF TBC1D4.
RX   MEDLINE=22063368; PubMed=11994271; DOI=10.1074/jbc.C200198200;
RA   Kane S., Sano H., Liu S.C.H., Asara J.M., Lane W.S., Garner C.C.,
RA   Lienhard G.E.;
RT   "A method to identify serine kinase substrates. Akt phosphorylates a
RT   novel adipocyte protein with a Rab GTPase-activating protein (GAP)
RT   domain.";
RL   J. Biol. Chem. 277:22115-22118(2002).
RN   [8]
RP   INTERACTION WITH CCDC88A, AND PHOSPHORYLATION AT THR-308 AND SER-473.
RX   PubMed=15753085; DOI=10.1074/jbc.M500586200;
RA   Anai M., Shojima N., Katagiri H., Ogihara T., Sakoda H., Onishi Y.,
RA   Ono H., Fujishiro M., Fukushima Y., Horike N., Viana A., Kikuchi M.,
RA   Noguchi N., Takahashi S., Takata K., Oka Y., Uchijima Y., Kurihara H.,
RA   Asano T.;
RT   "A novel protein kinase B (PKB)/AKT-binding protein enhances PKB
RT   kinase activity and regulates DNA synthesis.";
RL   J. Biol. Chem. 280:18525-18535(2005).
RN   [9]
RP   INTERACTION WITH GRB10.
RX   PubMed=15722337; DOI=10.1074/jbc.M501477200;
RA   Urschel S., Bassermann F., Bai R.Y., Munch S., Peschel C., Duyster J.;
RT   "Phosphorylation of grb10 regulates its interaction with 14-3-3.";
RL   J. Biol. Chem. 280:16987-16993(2005).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124; SER-126 AND
RP   SER-129, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [12]
RP   FUNCTION.
RX   PubMed=19778506; DOI=10.1016/j.neuron.2009.08.008;
RA   Kim J.Y., Duan X., Liu C.Y., Jang M.H., Guo J.U., Pow-anpongkul N.,
RA   Kang E., Song H., Ming G.L.;
RT   "DISC1 regulates new neuron development in the adult brain via
RT   modulation of AKT-mTOR signaling through KIAA1212.";
RL   Neuron 63:761-773(2009).
CC   -!- FUNCTION: General protein kinase capable of phosphorylating
CC       several known proteins. Phosphorylates TBC1D4. Signals downstream
CC       of phosphatidylinositol 3-kinase (PI(3)K) to mediate the effects
CC       of various growth factors such as platelet-derived growth factor
CC       (PDGF), epidermal growth factor (EGF), insulin and insulin-like
CC       growth factor I (IGF-I). Plays a role in glucose transport by
CC       mediating insulin-induced translocation of the GLUT4 glucose
CC       transporter to the cell surface. Mediates the antiapoptotic
CC       effects of IGF-I. Mediates insulin-stimulated protein synthesis by
CC       phosphorylating TSC2 at 'Ser-939' and 'Thr-1465', thereby
CC       activating mTORC1 signaling and leading to both phosphorylation of
CC       4E-BP1 and in activation of RPS6KB1 (By similarity). Plays a role
CC       as a key modulator of the AKT-mTOR signaling pathway controlling
CC       the tempo of the process of newborn neurons integration during
CC       adult neurogenesis, including correct neuron positioning,
CC       dendritic development and synapse formation. Promotes glycogen
CC       synthesis by mediating the insulin-induced activation of glycogen
CC       synthase.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Three specific sites, one in the kinase domain
CC       (Thr-308) and the two other ones in the C-terminal regulatory
CC       region (Ser-473 and Tyr-474), need to be phosphorylated for its
CC       full activation.
CC   -!- SUBUNIT: Interacts with AGAP2 isoform 2 (PIKE-A) in the presence
CC       of guanine nucleotides. The C-terminus interacts with CCDC88A/GRDN
CC       and THEM4. Interacts with AKTIP (By similarity). Interacts (via PH
CC       domain) with MTCP1, TCL1A AND TCL1B. Interacts with CDKN1B; the
CC       interaction phosphorylates CDKN1B promoting 14-3-3 binding and
CC       cell-cycle progression. Interacts with TRAF6 (By similarity).
CC       Interacts with GRB10; the interaction leads to GRB10
CC       phosphorylation thus promoting YWHAE/14-3-3-binding.
CC   -!- INTERACTION:
CC       P49407:ARRB1 (xeno); NbExp=1; IntAct=EBI-298707, EBI-743313;
CC       P32121:ARRB2 (xeno); NbExp=1; IntAct=EBI-298707, EBI-714559;
CC       O35099:Map3k5; NbExp=1; IntAct=EBI-298707, EBI-777493;
CC       Q8K4K2:Trib3; NbExp=5; IntAct=EBI-298707, EBI-448962;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cell membrane (By
CC       similarity). Note=Nucleus after activation by integrin-linked
CC       protein kinase 1 (ILK1) (By similarity). Nuclear translocation is
CC       enhanced by interaction with TCL1A.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Low levels found in liver
CC       with slightly higher levels present in thymus and testis.
CC   -!- DOMAIN: Binding of the PH domain to the phosphatidylinositol 3-
CC       kinase alpha (PI(3)K) results in its targeting to the plasma
CC       membrane.
CC   -!- DOMAIN: The AGC-kinase C-terminal mediates interaction with THEM4
CC       (By similarity).
CC   -!- PTM: Phosphorylation on Thr-308, Ser-473 and Tyr-474 is required
CC       for full activity. Ser-473 phosphorylation by mTORC2 favors Thr-
CC       308 phosphorylation by PDPK1 (By similarity).
CC   -!- PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked
CC       polyubiquitination. TRAF6-induced 'Lys-63'-linked AKT1
CC       ubiquitination is critical for phosphorylation and activation.
CC       When ubiquitinated, it translocates to the plasma membrane, where
CC       it becomes phosphorylated. When fully phosphorylated and
CC       translocated into the nucleus, undergoes 'Lys-48'-
CC       polyubiquitination catalyzed by TTC3, leading to its degradation
CC       by the proteasome (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. RAC subfamily.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; M94335; AAA18254.1; -; mRNA.
DR   EMBL; X65687; CAA46620.1; -; mRNA.
DR   IPI; IPI00323969; -.
DR   PIR; S33364; S33364.
DR   RefSeq; NP_033782.1; NM_009652.3.
DR   UniGene; Mm.6645; -.
DR   ProteinModelPortal; P31750; -.
DR   SMR; P31750; 1-477.
DR   DIP; DIP-736N; -.
DR   IntAct; P31750; 12.
DR   MINT; MINT-4049532; -.
DR   STRING; P31750; -.
DR   PhosphoSite; P31750; -.
DR   PRIDE; P31750; -.
DR   Ensembl; ENSMUST00000001780; ENSMUSP00000001780; ENSMUSG00000001729.
DR   Ensembl; ENSMUST00000109749; ENSMUSP00000105371; ENSMUSG00000001729.
DR   Ensembl; ENSMUST00000121171; ENSMUSP00000113658; ENSMUSG00000001729.
DR   GeneID; 11651; -.
DR   KEGG; mmu:11651; -.
DR   CTD; 11651; -.
DR   MGI; MGI:87986; Akt1.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108317; -.
DR   InParanoid; P31750; -.
DR   OrthoDB; EOG40GCQP; -.
DR   PhylomeDB; P31750; -.
DR   BRENDA; 2.7.11.1; 244.
DR   Reactome; REACT_13641; Regulation of Beta-Cell Development.
DR   ArrayExpress; P31750; -.
DR   Bgee; P31750; -.
DR   CleanEx; MM_AKT1; -.
DR   Genevestigator; P31750; -.
DR   GermOnline; ENSMUSG00000001729; Mus musculus.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005819; C:spindle; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; TAS:Reactome.
DR   GO; GO:0042640; P:anagen; IMP:MGI.
DR   GO; GO:0008637; P:apoptotic mitochondrial changes; IDA:MGI.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:MGI.
DR   GO; GO:0031018; P:endocrine pancreas development; TAS:Reactome.
DR   GO; GO:0007281; P:germ cell development; IDA:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0015758; P:glucose transport; IMP:UniProtKB.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0060709; P:glycogen cell development involved in embryonic placenta development; IMP:MGI.
DR   GO; GO:0006954; P:inflammatory response; IDA:MGI.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0060716; P:labyrinthine layer blood vessel development; IMP:MGI.
DR   GO; GO:0001893; P:maternal placenta development; IMP:MGI.
DR   GO; GO:0001649; P:osteoblast differentiation; IGI:MGI.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:MGI.
DR   GO; GO:0010765; P:positive regulation of sodium ion transport; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
DR   GO; GO:0030163; P:protein catabolic process; IDA:MGI.
DR   GO; GO:0043491; P:protein kinase B signaling cascade; IGI:MGI.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:MGI.
DR   GO; GO:0010975; P:regulation of neuron projection development; IDA:UniProtKB.
DR   GO; GO:0045884; P:regulation of survival gene product expression; IDA:MGI.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0032094; P:response to food; IDA:MGI.
DR   GO; GO:0051146; P:striated muscle cell differentiation; IGI:MGI.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; ATP-binding; Carbohydrate metabolism; Cell membrane;
KW   Cytoplasm; Glucose metabolism; Glycogen biosynthesis;
KW   Glycogen metabolism; Kinase; Membrane; Neurogenesis;
KW   Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Serine/threonine-protein kinase; Sugar transport; Transferase;
KW   Translation regulation; Transport; Ubl conjugation.
FT   CHAIN         1    480       RAC-alpha serine/threonine-protein
FT                                kinase.
FT                                /FTId=PRO_0000085606.
FT   DOMAIN        5    108       PH.
FT   DOMAIN      150    408       Protein kinase.
FT   DOMAIN      409    480       AGC-kinase C-terminal.
FT   NP_BIND     156    164       ATP (By similarity).
FT   ACT_SITE    274    274       Proton acceptor (By similarity).
FT   BINDING     179    179       ATP.
FT   MOD_RES     124    124       Phosphoserine.
FT   MOD_RES     126    126       Phosphoserine.
FT   MOD_RES     129    129       Phosphoserine.
FT   MOD_RES     308    308       Phosphothreonine; by PDPK1.
FT   MOD_RES     473    473       Phosphoserine.
FT   MOD_RES     474    474       Phosphotyrosine (By similarity).
FT   MUTAGEN     179    179       K->A: Lacks kinase activity.
FT                                Overexpression inhibits insulin-
FT                                stimulated translocation of GLUT4 in a
FT                                dominant negative manner.
FT   CONFLICT    367    367       A -> R (in Ref. 2; CAA46620).
SQ   SEQUENCE   480 AA;  55622 MW;  18D21018593B5A98 CRC64;
     MNDVAIVKEG WLHKRGEYIK TWRPRYFLLK NDGTFIGYKE RPQDVDQRES PLNNFSVAQC
     QLMKTERPRP NTFIIRCLQW TTVIERTFHV ETPEEREEWA TAIQTVADGL KRQEEETMDF
     RSGSPSDNSG AEEMEVSLAK PKHRVTMNEF EYLKLLGKGT FGKVILVKEK ATGRYYAMKI
     LKKEVIVAKD EVAHTLTENR VLQNSRHPFL TALKYSFQTH DRLCFVMEYA NGGELFFHLS
     RERVFSEDRA RFYGAEIVSA LDYLHSEKNV VYRDLKLENL MLDKDGHIKI TDFGLCKEGI
     KDGATMKTFC GTPEYLAPEV LEDNDYGRAV DWWGLGVVMY EMMCGRLPFY NQDHEKLFEL
     ILMEEIAFPR TLGPEAKSLL SGLLKKDPTQ RLGGGSEDAK EIMQHRFFAN IVWQDVYEKK
     LSPPFKPQVT SETDTRYFDE EFTAQMITIT PPDQDDSMEC VDSERRPHFP QFSYSASGTA
//
ID   ACBP_MOUSE              Reviewed;          87 AA.
AC   P31786;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Acyl-CoA-binding protein;
DE            Short=ACBP;
DE   AltName: Full=Diazepam-binding inhibitor;
DE            Short=DBI;
DE   AltName: Full=Endozepine;
DE            Short=EP;
GN   Name=Dbi;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90135913; PubMed=2615592; DOI=10.1016/0169-328X(89)90043-0;
RA   Owens G.P., Sinha A.K., Sikela J.M., Hahn W.E.;
RT   "Sequence and expression of the murine diazepam binding inhibitor.";
RL   Brain Res. Mol. Brain Res. 6:101-108(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   PubMed=12106288; DOI=10.1111/j.1460-9568.1990.tb00460.x;
RA   Kato K.;
RT   "A collection of cDNA clones with specific expression patterns in
RT   mouse brain.";
RL   Eur. J. Neurosci. 2:704-711(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 34-51, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Binds medium- and long-chain acyl-CoA esters with very
CC       high affinity and may function as an intracellular carrier of
CC       acyl-CoA esters. It is also able to displace diazepam from the
CC       benzodiazepine (BZD) recognition site located on the GABA type A
CC       receptor. It is therefore possible that this protein also acts as
CC       a neuropeptide to modulate the action of the GABA receptor.
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the ACBP family.
CC   -!- SIMILARITY: Contains 1 ACB (acyl-CoA-binding) domain.
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DR   EMBL; X61431; CAA43673.1; -; mRNA.
DR   EMBL; AK018720; BAB31366.1; -; mRNA.
DR   EMBL; AK027906; BAC25658.1; -; mRNA.
DR   EMBL; BC028874; AAH28874.1; -; mRNA.
DR   IPI; IPI00667117; -.
DR   PIR; A60059; A60059.
DR   RefSeq; NP_031856.1; NM_007830.4.
DR   UniGene; Mm.2785; -.
DR   ProteinModelPortal; P31786; -.
DR   SMR; P31786; 2-87.
DR   STRING; P31786; -.
DR   PhosphoSite; P31786; -.
DR   SWISS-2DPAGE; P31786; -.
DR   PRIDE; P31786; -.
DR   Ensembl; ENSMUST00000027634; ENSMUSP00000027634; ENSMUSG00000026385.
DR   GeneID; 13167; -.
DR   KEGG; mmu:13167; -.
DR   UCSC; uc007cjf.1; mouse.
DR   CTD; 13167; -.
DR   MGI; MGI:94865; Dbi.
DR   eggNOG; roNOG17150; -.
DR   HOVERGEN; HBG000398; -.
DR   OrthoDB; EOG4GF3GS; -.
DR   PhylomeDB; P31786; -.
DR   NextBio; 283250; -.
DR   ArrayExpress; P31786; -.
DR   Bgee; P31786; -.
DR   CleanEx; MM_DBI; -.
DR   Genevestigator; P31786; -.
DR   GermOnline; ENSMUSG00000026385; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR   GO; GO:0001942; P:hair follicle development; IMP:MGI.
DR   GO; GO:0043588; P:skin development; IMP:MGI.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   GO; GO:0006641; P:triglyceride metabolic process; IMP:MGI.
DR   InterPro; IPR022408; Acyl-CoA-binding_prot_CS.
DR   InterPro; IPR000582; Acyl-CoA-binding_protein.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   PANTHER; PTHR23310; ACBP; 1.
DR   Pfam; PF00887; ACBP; 1.
DR   PRINTS; PR00689; ACOABINDINGP.
DR   SUPFAM; SSF47027; ACBP; 1.
DR   PROSITE; PS00880; ACB_1; 1.
DR   PROSITE; PS51228; ACB_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Lipid-binding; Phosphoprotein;
KW   Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2     87       Acyl-CoA-binding protein.
FT                                /FTId=PRO_0000214005.
FT   DOMAIN        2     87       ACB.
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES       8      8       N6-acetyllysine (By similarity).
FT   MOD_RES      29     29       Phosphotyrosine.
FT   MOD_RES      55     55       N6-acetyllysine.
FT   MOD_RES      77     77       N6-acetyllysine (By similarity).
SQ   SEQUENCE   87 AA;  10000 MW;  86F725C998785675 CRC64;
     MSQAEFDKAA EEVKRLKTQP TDEEMLFIYS HFKQATVGDV NTDRPGLLDL KGKAKWDSWN
     KLKGTSKESA MKTYVEKVDE LKKKYGI
//
ID   MP2K1_MOUSE             Reviewed;         393 AA.
AC   P31938;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 113.
DE   RecName: Full=Dual specificity mitogen-activated protein kinase kinase 1;
DE            Short=MAP kinase kinase 1;
DE            Short=MAPKK 1;
DE            EC=2.7.12.2;
DE   AltName: Full=ERK activator kinase 1;
DE   AltName: Full=MAPK/ERK kinase 1;
DE            Short=MEK 1;
GN   Name=Map2k1; Synonyms=Mek1, Prkmk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=93030761; PubMed=1411546; DOI=10.1126/science.1411546;
RA   Crews C.M., Alessandrini A., Erikson R.L.;
RT   "The primary structure of MEK, a protein kinase that phosphorylates
RT   the ERK gene product.";
RL   Science 258:478-480(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 4-20; 71-84; 114-136; 206-234 AND 363-384.
RC   TISSUE=T-cell;
RX   MEDLINE=92390415; PubMed=1381507; DOI=10.1073/pnas.89.17.8205;
RA   Crews C.M., Erikson R.L.;
RT   "Purification of a murine protein-tyrosine/threonine kinase that
RT   phosphorylates and activates the Erk-1 gene product: relationship to
RT   the fission yeast byr1 gene product.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:8205-8209(1992).
RN   [4]
RP   PROTEIN SEQUENCE OF 206-227; 270-291 AND 325-340, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [5]
RP   CLEAVAGE BY ANTHRAX LETHAL FACTOR.
RX   MEDLINE=98230732; PubMed=9563949; DOI=10.1126/science.280.5364.734;
RA   Duesbery N.S., Webb C.P., Leppla S.H., Gordon V.M., Klimpel K.R.,
RA   Copeland T.D., Ahn N.G., Oskarsson M.K., Fukasawa K., Paull K.D.,
RA   Vande Woude G.F.;
RT   "Proteolytic inactivation of MAP-kinase-kinase by anthrax lethal
RT   factor.";
RL   Science 280:734-737(1998).
RN   [6]
RP   INTERACTION WITH MORG1.
RX   PubMed=15118098; DOI=10.1073/pnas.0305894101;
RA   Vomastek T., Schaeffer H.-J., Tarcsafalvi A., Smolkin M.E.,
RA   Bissonette E.A., Weber M.J.;
RT   "Modular construction of a signaling scaffold: MORG1 interacts with
RT   components of the ERK cascade and links ERK signaling to specific
RT   agonists.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:6981-6986(2004).
CC   -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine
CC       and a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP
CC       kinases. Activates ERK1 and ERK2 MAP kinases.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Inhibited by serine/threonine phosphatase 2A.
CC   -!- SUBUNIT: Interacts with MORG1.. Interacts with ARRB2 (By
CC       similarity).
CC   -!- PTM: MAPKK is itself dependent on Ser/Thr phosphorylation for
CC       activity catalyzed by MAP kinase kinase kinases (RAF or MEKK1).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; L02526; AAA39523.1; -; mRNA.
DR   EMBL; BC054754; AAH54754.1; -; mRNA.
DR   IPI; IPI00466610; -.
DR   PIR; I59571; I59571.
DR   RefSeq; NP_032953.1; NM_008927.3.
DR   UniGene; Mm.248907; -.
DR   ProteinModelPortal; P31938; -.
DR   SMR; P31938; 39-381.
DR   DIP; DIP-467N; -.
DR   STRING; P31938; -.
DR   PhosphoSite; P31938; -.
DR   UCD-2DPAGE; P31938; -.
DR   PRIDE; P31938; -.
DR   Ensembl; ENSMUST00000005066; ENSMUSP00000005066; ENSMUSG00000004936.
DR   GeneID; 26395; -.
DR   KEGG; mmu:26395; -.
DR   UCSC; uc009qbp.1; mouse.
DR   CTD; 26395; -.
DR   MGI; MGI:1346866; Map2k1.
DR   eggNOG; roNOG05418; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108518; -.
DR   InParanoid; P31938; -.
DR   OMA; ELMFGCP; -.
DR   OrthoDB; EOG4SF965; -.
DR   PhylomeDB; P31938; -.
DR   BRENDA; 2.7.12.2; 244.
DR   NextBio; 304339; -.
DR   ArrayExpress; P31938; -.
DR   Bgee; P31938; -.
DR   CleanEx; MM_MAP2K1; -.
DR   Genevestigator; P31938; -.
DR   GermOnline; ENSMUSG00000004936; Mus musculus.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004708; F:MAP kinase kinase activity; IMP:MGI.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004728; F:receptor signaling protein tyrosine phosphatase activity; IMP:MGI.
DR   GO; GO:0000187; P:activation of MAPK activity; IMP:MGI.
DR   GO; GO:0048870; P:cell motility; IMP:MGI.
DR   GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI.
DR   GO; GO:0060711; P:labyrinthine layer development; IMP:MGI.
DR   GO; GO:0060674; P:placenta blood vessel development; IMP:MGI.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; IDA:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase;
KW   Tyrosine-protein kinase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    393       Dual specificity mitogen-activated
FT                                protein kinase kinase 1.
FT                                /FTId=PRO_0000086366.
FT   DOMAIN       68    361       Protein kinase.
FT   NP_BIND      74     82       ATP (By similarity).
FT   COMPBIAS    262    307       Pro-rich.
FT   ACT_SITE    190    190       Proton acceptor (By similarity).
FT   BINDING      97     97       ATP (By similarity).
FT   SITE          8      9       Cleavage; by anthrax lethal factor (By
FT                                similarity).
FT   MOD_RES     218    218       Phosphoserine; by RAF (By similarity).
FT   MOD_RES     222    222       Phosphoserine; by RAF (By similarity).
FT   MOD_RES     231    231       Phosphoserine (By similarity).
FT   MOD_RES     286    286       Phosphothreonine (By similarity).
FT   MOD_RES     385    385       Phosphoserine (By similarity).
FT   MOD_RES     386    386       Phosphothreonine (By similarity).
FT   CONFLICT    374    374       W -> Q (in Ref. 3; AA sequence).
SQ   SEQUENCE   393 AA;  43474 MW;  01D1D18572AE40E7 CRC64;
     MPKKKPTPIQ LNPAPDGSAV NGTSSAETNL EALQKKLEEL ELDEQQRKRL EAFLTQKQKV
     GELKDDDFEK ISELGAGNGG VVFKVSHKPS GLVMARKLIH LEIKPAIRNQ IIRELQVLHE
     CNSPYIVGFY GAFYSDGEIS ICMEHMDGGS LDQVLKKAGR IPEQILGKVS IAVIKGLTYL
     REKHKIMHRD VKPSNILVNS RGEIKLCDFG VSGQLIDSMA NSFVGTRSYM SPERLQGTHY
     SVQSDIWSMG LSLVEMAVGR YPIPPPDAKE LELLFGCHVE GDAAETPPRP RTPGRPLSSY
     GMDSRPPMAI FELLDYIVNE PPPKLPSGVF SLEFQDFVNK CLIKNPAERA DLKQLMVHAF
     IKRSDAEEVD FAGWLCSTIG LNQPSTPTHA ASI
//
ID   NLTP_MOUSE              Reviewed;         547 AA.
AC   P32020; A2APS2; A2APS3; Q9DBM7;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 3.
DT   08-MAR-2011, entry version 110.
DE   RecName: Full=Non-specific lipid-transfer protein;
DE            Short=NSL-TP;
DE            EC=2.3.1.176;
DE   AltName: Full=Propanoyl-CoA C-acyltransferase;
DE   AltName: Full=SCP-chi;
DE   AltName: Full=SCPX;
DE   AltName: Full=Sterol carrier protein 2;
DE            Short=SCP-2;
DE   AltName: Full=Sterol carrier protein X;
DE            Short=SCP-X;
GN   Name=Scp2; Synonyms=Scp-2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=93154580; PubMed=8428655; DOI=10.1016/0378-1119(93)90120-R;
RA   Seedorf U., Raabe M., Assmann G.;
RT   "Cloning, expression and sequences of mouse sterol-carrier protein-x-
RT   encoding cDNAs and a related pseudogene.";
RL   Gene 123:165-172(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 525-534, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 405-547, AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Liver;
RX   MEDLINE=91236770; PubMed=1709640;
RA   Moncecchi D.T., Pastuszyn A., Scallen T.J.;
RT   "cDNA sequence and bacterial expression of mouse liver sterol carrier
RT   protein-2.";
RL   J. Biol. Chem. 266:9885-9892(1991).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
RC   STRAIN=129/Sv; TISSUE=Liver;
RX   MEDLINE=96354847; PubMed=8751375;
RA   Raabe M., Seedorf U., Hameister H., Ellinghaus P., Assmann G.;
RT   "Structure and chromosomal assignment of the murine sterol carrier
RT   protein 2 gene (Scp2) and two related pseudogenes by in situ
RT   hybridization.";
RL   Cytogenet. Cell Genet. 73:279-281(1996).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142; LYS-173; LYS-282;
RP   LYS-341 AND LYS-453, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-425, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
CC   -!- FUNCTION: Mediates in vitro the transfer of all common
CC       phospholipids, cholesterol and gangliosides between membranes. May
CC       play a role in regulating steroidogenesis.
CC   -!- CATALYTIC ACTIVITY: 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-
CC       cholanoyl-CoA + propanoyl-CoA = CoA + 3-alpha,7-alpha,12-alpha-
CC       trihydroxy-24-oxo-5-beta-cholestanoyl-CoA.
CC   -!- SUBUNIT: Interacts with PEX5 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Cytoplasmic in the liver and
CC       also associated with mitochondria especially in steroidogenic
CC       tissues.
CC   -!- SUBCELLULAR LOCATION: Isoform SCP2: Mitochondrion.
CC   -!- SUBCELLULAR LOCATION: Isoform SCPx: Peroxisome. Note=Interaction
CC       with PEX5 is essential for peroxisomal import (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=SCPx;
CC         IsoId=P32020-1; Sequence=Displayed;
CC       Name=SCP2;
CC         IsoId=P32020-2; Sequence=VSP_018895;
CC         Note=Mitochondrial precursor. Contains a mitochondrial transit
CC         peptide at positions 405-424 (Potential);
CC   -!- TISSUE SPECIFICITY: Present at low levels in all tissues examined
CC       but expressed predominantly in the liver.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the thiolase
CC       family.
CC   -!- SIMILARITY: Contains 1 SCP2 domain.
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DR   EMBL; M91458; AAA40098.1; -; mRNA.
DR   EMBL; AK002425; BAB22092.2; -; mRNA.
DR   EMBL; AK004860; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AL844206; CAM27075.1; -; Genomic_DNA.
DR   EMBL; AL844206; CAM27076.1; -; Genomic_DNA.
DR   EMBL; BC018384; AAH18384.1; -; mRNA.
DR   EMBL; BC034613; AAH34613.1; -; mRNA.
DR   EMBL; M62361; AAA40099.1; -; mRNA.
DR   EMBL; X91150; CAA62592.1; -; Genomic_DNA.
DR   IPI; IPI00134131; -.
DR   IPI; IPI00648476; -.
DR   PIR; A40015; A40015.
DR   PIR; JU0157; JU0157.
DR   RefSeq; NP_035457.1; NM_011327.3.
DR   UniGene; Mm.379011; -.
DR   ProteinModelPortal; P32020; -.
DR   SMR; P32020; 13-398, 425-547.
DR   IntAct; P32020; 2.
DR   MINT; MINT-219254; -.
DR   STRING; P32020; -.
DR   PhosphoSite; P32020; -.
DR   PRIDE; P32020; -.
DR   Ensembl; ENSMUST00000030340; ENSMUSP00000030340; ENSMUSG00000028603.
DR   GeneID; 20280; -.
DR   KEGG; mmu:20280; -.
DR   UCSC; uc008uas.1; mouse.
DR   CTD; 20280; -.
DR   MGI; MGI:98254; Scp2.
DR   GeneTree; ENSGT00530000062928; -.
DR   HOGENOM; HBG567272; -.
DR   HOVERGEN; HBG006506; -.
DR   InParanoid; P32020; -.
DR   OMA; PQMFGNA; -.
DR   OrthoDB; EOG40K7ZM; -.
DR   PhylomeDB; P32020; -.
DR   BRENDA; 2.3.1.176; 244.
DR   NextBio; 297975; -.
DR   ArrayExpress; P32020; -.
DR   Bgee; P32020; -.
DR   CleanEx; MM_SCP2; -.
DR   Genevestigator; P32020; -.
DR   GermOnline; ENSMUSG00000028603; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005777; C:peroxisome; TAS:MGI.
DR   GO; GO:0033814; F:propanoyl-CoA C-acyltransferase activity; IEA:EC.
DR   GO; GO:0050632; F:propionyl-CoA C2-trimethyltridecanoyltransferase activity; TAS:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0032934; F:sterol binding; IEA:InterPro.
DR   GO; GO:0006637; P:acyl-CoA metabolic process; TAS:MGI.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0007031; P:peroxisome organization; IMP:MGI.
DR   InterPro; IPR003033; SCP2_sterol-bd_dom.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR016038; Thiolase-like_subgr.
DR   InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR   InterPro; IPR020617; Thiolase_C.
DR   InterPro; IPR020613; Thiolase_CS.
DR   InterPro; IPR020616; Thiolase_N.
DR   Gene3D; G3DSA:3.40.47.10; Thiolase-like_subgr; 3.
DR   Pfam; PF02036; SCP2; 1.
DR   Pfam; PF02803; Thiolase_C; 1.
DR   Pfam; PF00108; Thiolase_N; 1.
DR   SUPFAM; SSF55718; SCP2; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   PROSITE; PS00098; THIOLASE_1; 1.
DR   PROSITE; PS00737; THIOLASE_2; 1.
DR   PROSITE; PS00099; THIOLASE_3; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative initiation; Cytoplasm;
KW   Direct protein sequencing; Lipid transport; Lipid-binding;
KW   Mitochondrion; Peroxisome; Phosphoprotein; Transferase;
KW   Transit peptide; Transport.
FT   CHAIN         1    547       Non-specific lipid-transfer protein.
FT                                /FTId=PRO_0000034093.
FT   DOMAIN      433    543       SCP2.
FT   MOTIF       545    547       Microbody targeting signal (Potential).
FT   MOD_RES       8      8       Phosphoserine.
FT   MOD_RES     132    132       N6-acetyllysine (By similarity).
FT   MOD_RES     142    142       N6-acetyllysine.
FT   MOD_RES     173    173       N6-acetyllysine.
FT   MOD_RES     183    183       N6-acetyllysine (By similarity).
FT   MOD_RES     197    197       Phosphotyrosine (By similarity).
FT   MOD_RES     204    204       Phosphotyrosine (By similarity).
FT   MOD_RES     282    282       N6-acetyllysine.
FT   MOD_RES     341    341       N6-acetyllysine.
FT   MOD_RES     425    425       Phosphoserine.
FT   MOD_RES     438    438       N6-acetyllysine (By similarity).
FT   MOD_RES     453    453       N6-acetyllysine.
FT   MOD_RES     470    470       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1    404       Missing (in isoform SCP2).
FT                                /FTId=VSP_018895.
FT   CONFLICT    232    232       A -> C (in Ref. 1; AAA40098).
FT   CONFLICT    478    478       V -> A (in Ref. 6; AAA40099).
SQ   SEQUENCE   547 AA;  59126 MW;  37BA2E730D9CB105 CRC64;
     MPSVALKSPR LRRVFVVGVG MTKFMKPGGE NSRDYPDMAK EAGQKALEDA QIPYSAVEQA
     CVGYVYGDST SGQRAIYHSL GLTGIPIINV NNNCSTGSTA LFMAHQLIQG GLANCVLALG
     FEKMERGSIG TKFSDRTTPT DKHIEVLIDK YGLSAHPITP QMFGYAGKEH MEKYGTKVEH
     FAKIGWKNHK HSVNNTYSQF QDEYSLEEVM KSKPVFDFLT ILQCCPTSDG AAAAILSSEE
     FVQQYGLQSK AVEIVAQEMM TDLPSTFEEK SIIKVVGYDM SKEAARRCYE KSGLTPNDVD
     VIELHDCFSV NELITYEALG LCPEGQGGTL VDRGDNTYGG KWVINPSGGL ISKGHPLGAT
     GLAQCAELCW QLRGEAGKRQ VPGAKVALQH NLGLGGAVVV TLYRMGFPEA ASSFRTHQVS
     AAPTSSAGDG FKANLVFKEI EKKLEEEGEQ FVKKIGGIFA FKVKDGPGGK EATWVVDVKN
     GKGSVLPNSD KKADCTITMA DSDLLALMTG KMNPQSAFFQ GKLKIAGNMG LAMKLQNLQL
     QPGKAKL
//
ID   GTR3_MOUSE              Reviewed;         493 AA.
AC   P32037;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Solute carrier family 2, facilitated glucose transporter member 3;
DE   AltName: Full=Glucose transporter type 3, brain;
DE            Short=GLUT-3;
GN   Name=Slc2a3; Synonyms=Glut-3, Glut3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=92112695; PubMed=1730609;
RA   Nagamatsu S., Kornhauser J.M., Seino S., Mayo K.E., Steiner D.F.,
RA   Bell G.I.;
RT   "Glucose transporter expression in brain. cDNA sequence of mouse
RT   GLUT3, the brain facilitative glucose transporter isoform, and
RT   identification of sites of expression by in situ hybridization.";
RL   J. Biol. Chem. 267:467-472(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Takeda J., Minokoshi Y., Yasuda K., Kayano T., Graeme B.I.;
RT   "Evolution of facilitative sugar transporter gene family:
RT   Characterization of mouse GLUT3 and human GLUT5 genes.";
RL   Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 218-228, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-43, AND MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Facilitative glucose transporter. Probably a neuronal
CC       glucose transporter.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC       transporter (TC 2.A.1.1) family. Glucose transporter subfamily.
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DR   EMBL; M75135; AAA37704.1; -; mRNA.
DR   EMBL; X61093; CAA43406.1; -; mRNA.
DR   EMBL; U11853; AAB60666.1; -; Genomic_DNA.
DR   EMBL; U11844; AAB60666.1; JOINED; Genomic_DNA.
DR   EMBL; U11845; AAB60666.1; JOINED; Genomic_DNA.
DR   EMBL; U11846; AAB60666.1; JOINED; Genomic_DNA.
DR   EMBL; U11848; AAB60666.1; JOINED; Genomic_DNA.
DR   EMBL; U11849; AAB60666.1; JOINED; Genomic_DNA.
DR   EMBL; U11850; AAB60666.1; JOINED; Genomic_DNA.
DR   EMBL; U11851; AAB60666.1; JOINED; Genomic_DNA.
DR   EMBL; U11852; AAB60666.1; JOINED; Genomic_DNA.
DR   EMBL; BC034122; AAH34122.1; -; mRNA.
DR   EMBL; BC058811; AAH58811.1; -; mRNA.
DR   IPI; IPI00134191; -.
DR   PIR; A41751; A41751.
DR   RefSeq; NP_035531.3; NM_011401.4.
DR   UniGene; Mm.395108; -.
DR   ProteinModelPortal; P32037; -.
DR   STRING; P32037; -.
DR   PhosphoSite; P32037; -.
DR   PRIDE; P32037; -.
DR   Ensembl; ENSMUST00000032476; ENSMUSP00000032476; ENSMUSG00000003153.
DR   GeneID; 20527; -.
DR   KEGG; mmu:20527; -.
DR   CTD; 20527; -.
DR   MGI; MGI:95757; Slc2a3.
DR   eggNOG; roNOG09613; -.
DR   HOGENOM; HBG744444; -.
DR   HOVERGEN; HBG014816; -.
DR   InParanoid; P32037; -.
DR   OMA; FERRTED; -.
DR   OrthoDB; EOG4QNMW2; -.
DR   PhylomeDB; P32037; -.
DR   ArrayExpress; P32037; -.
DR   Bgee; P32037; -.
DR   Genevestigator; P32037; -.
DR   GermOnline; ENSMUSG00000003153; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0055056; F:D-glucose transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0033300; F:dehydroascorbic acid transporter activity; IDA:UniProtKB.
DR   InterPro; IPR002945; Glc_transpt_3.
DR   InterPro; IPR020846; Major_facilitator_SF.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   InterPro; IPR005828; Sub_transporter.
DR   InterPro; IPR003663; Sugar/inositol_transpt.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   PRINTS; PR01192; GLUCTRSPORT3.
DR   PRINTS; PR00171; SUGRTRNSPORT.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
DR   TIGRFAMs; TIGR00879; SP; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR   PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Membrane; Phosphoprotein;
KW   Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    493       Solute carrier family 2, facilitated
FT                                glucose transporter member 3.
FT                                /FTId=PRO_0000050354.
FT   TOPO_DOM      1     10       Cytoplasmic (Potential).
FT   TRANSMEM     11     31       Helical; Name=1; (Potential).
FT   TOPO_DOM     32     64       Extracellular (Potential).
FT   TRANSMEM     65     85       Helical; Name=2; (Potential).
FT   TOPO_DOM     86     93       Cytoplasmic (Potential).
FT   TRANSMEM     94    114       Helical; Name=3; (Potential).
FT   TOPO_DOM    115    124       Extracellular (Potential).
FT   TRANSMEM    125    145       Helical; Name=4; (Potential).
FT   TOPO_DOM    146    153       Cytoplasmic (Potential).
FT   TRANSMEM    154    174       Helical; Name=5; (Potential).
FT   TOPO_DOM    175    183       Extracellular (Potential).
FT   TRANSMEM    184    204       Helical; Name=6; (Potential).
FT   TOPO_DOM    205    269       Cytoplasmic (Potential).
FT   TRANSMEM    270    290       Helical; Name=7; (Potential).
FT   TOPO_DOM    291    304       Extracellular (Potential).
FT   TRANSMEM    305    325       Helical; Name=8; (Potential).
FT   TOPO_DOM    326    334       Cytoplasmic (Potential).
FT   TRANSMEM    335    355       Helical; Name=9; (Potential).
FT   TOPO_DOM    356    363       Extracellular (Potential).
FT   TRANSMEM    364    384       Helical; Name=10; (Potential).
FT   TOPO_DOM    385    399       Cytoplasmic (Potential).
FT   TRANSMEM    400    420       Helical; Name=11; (Potential).
FT   TOPO_DOM    421    427       Extracellular (Potential).
FT   TRANSMEM    428    448       Helical; Name=12; (Potential).
FT   TOPO_DOM    449    493       Cytoplasmic (Potential).
FT   REGION      277    279       Defines substrate specificity (By
FT                                similarity).
FT   MOD_RES     482    482       Phosphoserine (By similarity).
FT   CARBOHYD     43     43       N-linked (GlcNAc...).
SQ   SEQUENCE   493 AA;  53479 MW;  9090B8DCB8780082 CRC64;
     MGTTKVTPSL VFAVTVATIG SFQFGYNTGV INAPETILKD FLNYTLEERL EDLPSEGLLT
     ALWSLCVAIF SVGGMIGSFS VGLFVNRFGR RNSMLLVNLL AIIAGCLMGF AKIAESVEML
     ILGRLLIGIF CGLCTGFVPM YIGEVSPTAL RGAFGTLNQL GIVVGILVAQ IFGLDFILGS
     EELWPGLLGL TIIPAILQSA ALPFCPESPR FLLINKKEED QATEILQRLW GTSDVVQEIQ
     EMKDESVRMS QEKQVTVLEL FRSPNYVQPL LISIVLQLSQ QLSGINAVFY YSTGIFKDAG
     VQEPIYATIG AGVVNTIFTV VSLFLVERAG RRTLHMIGLG GMAVCSVFMT ISLLLKDDYE
     AMSFVCIVAI LIYVAFFEIG PGPIPWFIVA ELFSQGPRPA AIAVAGCCNW TSNFLVGMLF
     PSAAAYLGAY VFIIFAAFLI FFLIFTFFKV PETKGRTFED IARAFEGQAH SGKGPAGVEL
     NSMQPVKETP GNA
//
ID   ACM4_MOUSE              Reviewed;         479 AA.
AC   P32211; Q64056;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Muscarinic acetylcholine receptor M4;
DE   AltName: Full=Mm4 mAChR;
GN   Name=Chrm4; Synonyms=Chrm-4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=93305731; PubMed=7916637; DOI=10.1016/0167-4781(93)90135-Z;
RA   van Koppen C.J., Lenz W., Nathanson N.M.;
RT   "Isolation, sequence and functional expression of the mouse m4
RT   muscarinic acetylcholine receptor gene.";
RL   Biochim. Biophys. Acta 1173:342-344(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 235-355.
RC   TISSUE=Brain;
RX   MEDLINE=95179320; PubMed=7874308;
RX   DOI=10.1111/j.1460-9568.1994.tb00561.x;
RA   Andre C., Dos Santos G., Koulakoff A.;
RT   "Cultured neurons from mouse brain reproduce the muscarinic receptor
RT   profile of their tissue of origin.";
RL   Eur. J. Neurosci. 6:1691-1701(1994).
CC   -!- FUNCTION: The muscarinic acetylcholine receptor mediates various
CC       cellular responses, including inhibition of adenylate cyclase,
CC       breakdown of phosphoinositides and modulation of potassium
CC       channels through the action of G proteins. Primary transducing
CC       effect is inhibition of adenylate cyclase.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Cell junction, synapse, postsynaptic cell membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Muscarinic acetylcholine receptor subfamily. CHRM4 sub-subfamily.
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DR   EMBL; X63473; CAA45071.1; -; Genomic_DNA.
DR   EMBL; S74916; AAB33577.1; -; mRNA.
DR   IPI; IPI00136358; -.
DR   PIR; S33776; S33776.
DR   RefSeq; NP_031725.1; NM_007699.2.
DR   UniGene; Mm.330405; -.
DR   ProteinModelPortal; P32211; -.
DR   SMR; P32211; 28-469.
DR   STRING; P32211; -.
DR   PRIDE; P32211; -.
DR   Ensembl; ENSMUST00000045537; ENSMUSP00000040808; ENSMUSG00000040495.
DR   GeneID; 12672; -.
DR   KEGG; mmu:12672; -.
DR   UCSC; uc008kwv.1; mouse.
DR   CTD; 12672; -.
DR   MGI; MGI:88399; Chrm4.
DR   eggNOG; maNOG19089; -.
DR   HOGENOM; HBG713567; -.
DR   HOVERGEN; HBG105720; -.
DR   InParanoid; P32211; -.
DR   OMA; VEMVFIA; -.
DR   OrthoDB; EOG41JZCC; -.
DR   PhylomeDB; P32211; -.
DR   NextBio; 281914; -.
DR   ArrayExpress; P32211; -.
DR   Bgee; P32211; -.
DR   CleanEx; MM_CHRM4; -.
DR   Genevestigator; P32211; -.
DR   GermOnline; ENSMUSG00000040495; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004981; F:muscarinic acetylcholine receptor activity; IDA:MGI.
DR   GO; GO:0007197; P:inhibition of adenylate cyclase activity by muscarinic acetylcholine receptor signaling pathway; IDA:MGI.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR001432; Musac_M4_rcpt.
DR   InterPro; IPR000995; Musac_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00243; MUSCARINICR.
DR   PRINTS; PR00541; MUSCRINICM4R.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Receptor; Synapse; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    479       Muscarinic acetylcholine receptor M4.
FT                                /FTId=PRO_0000069038.
FT   TOPO_DOM      1     30       Extracellular (By similarity).
FT   TRANSMEM     31     53       Helical; Name=1; (By similarity).
FT   TOPO_DOM     54     67       Cytoplasmic (By similarity).
FT   TRANSMEM     68     88       Helical; Name=2; (By similarity).
FT   TOPO_DOM     89    105       Extracellular (By similarity).
FT   TRANSMEM    106    127       Helical; Name=3; (By similarity).
FT   TOPO_DOM    128    147       Cytoplasmic (By similarity).
FT   TRANSMEM    148    170       Helical; Name=4; (By similarity).
FT   TOPO_DOM    171    192       Extracellular (By similarity).
FT   TRANSMEM    193    215       Helical; Name=5; (By similarity).
FT   TOPO_DOM    216    401       Cytoplasmic (By similarity).
FT   TRANSMEM    402    422       Helical; Name=6; (By similarity).
FT   TOPO_DOM    423    436       Extracellular (By similarity).
FT   TRANSMEM    437    456       Helical; Name=7; (By similarity).
FT   TOPO_DOM    457    479       Cytoplasmic (By similarity).
FT   MOD_RES     459    459       Phosphothreonine (Potential).
FT   MOD_RES     463    463       Phosphothreonine (Potential).
FT   MOD_RES     477    477       Phosphothreonine (Potential).
FT   CARBOHYD      8      8       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     13     13       N-linked (GlcNAc...) (Potential).
FT   DISULFID    104    184       By similarity.
FT   CONFLICT    322    323       AL -> V (in Ref. 2; AAB33577).
FT   CONFLICT    351    351       S -> N (in Ref. 2; AAB33577).
SQ   SEQUENCE   479 AA;  52973 MW;  04F301E78814CD70 CRC64;
     MANFTPVNGS SANQSVRLVT TAHNHLETVE MVFIATVTGS LSLVTVVGNI LVMLSIKVNR
     QLQTVNNYFL FSLACADLII GAFSMNLYTL YIIKGYWPLG AVVCDLWLAL DYVVSNASVM
     NLLIISFDRY FCVTKPLTYP ARRTTKMAGL MIAAAWVLSF VLWAPAILFW QFVVGKRTVP
     DNQCFIQFLS NPAVTFGTAI AAFYLPVVIM TVLYIHISLA SRSRVHKHRP EGPKEKKAKT
     LAFLKSPLMK PSIKKPPPGG ASREELRNGK LEEAPPPALP PPPRPVADKD TSNESSSGSA
     TQNTKERPPT ELSTTEAATT PALPAPTLQP RTLNPASKWS KIQIVTKQTG SECVTAIEIV
     PATPAGMRPA ANVARKFASI ARNQVRKKRQ MAARERKVTR TIFAILLAFI LTWTPYNVMV
     LVNTFCQSCI PERVWSIGYW LCYVNSTINP ACYALCNATF KKTFRHLLLC QYRNIGTAR
//
ID   CAD15_MOUSE             Reviewed;         784 AA.
AC   P33146; Q9QYZ7;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Cadherin-15;
DE   AltName: Full=Cadherin-14;
DE   AltName: Full=Muscle cadherin;
DE            Short=M-cadherin;
DE   Flags: Precursor;
GN   Name=Cdh15; Synonyms=Cdh14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C3H; TISSUE=Muscle;
RA   Link D.;
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 55-784.
RC   TISSUE=Muscle;
RX   MEDLINE=91376079; PubMed=1840697; DOI=10.1073/pnas.88.18.8024;
RA   Donalies M., Cramer M., Ringwald M., Starzinski-Powitz A.;
RT   "Expression of M-cadherin, a member of the cadherin multigene family,
RT   correlates with differentiation of skeletal muscle cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:8024-8028(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 539-617.
RX   MEDLINE=20079143; PubMed=10610704; DOI=10.1006/geno.1999.6022;
RA   Kelsey G., Bodle D., Miller H.J., Beechey C.V., Coombes C., Peters J.,
RA   Williamson C.M.;
RT   "Identification of imprinted loci by methylation-sensitive
RT   representational difference analysis: application to mouse distal
RT   chromosome 2.";
RL   Genomics 62:129-138(1999).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-106 AND ASN-537, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
CC   -!- FUNCTION: Cadherins are calcium dependent cell adhesion proteins.
CC       They preferentially interact with themselves in a homophilic
CC       manner in connecting cells; cadherins may thus contribute to the
CC       sorting of heterogeneous cell types. M-cadherin is part of the
CC       myogenic program and may provide a trigger for terminal muscle
CC       differentiation.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Skeletal muscle.
CC   -!- SIMILARITY: Contains 5 cadherin domains.
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DR   EMBL; M74541; AAC23585.1; -; mRNA.
DR   EMBL; AJ245402; CAB57281.2; -; Genomic_DNA.
DR   IPI; IPI00109330; -.
DR   PIR; A40986; IJMSCM.
DR   UniGene; Mm.1976; -.
DR   ProteinModelPortal; P33146; -.
DR   SMR; P33146; 45-584, 689-783.
DR   STRING; P33146; -.
DR   PRIDE; P33146; -.
DR   Ensembl; ENSMUST00000034443; ENSMUSP00000034443; ENSMUSG00000031962.
DR   UCSC; uc009ntv.1; mouse.
DR   MGI; MGI:106672; Cdh15.
DR   eggNOG; roNOG13029; -.
DR   GeneTree; ENSGT00550000074431; -.
DR   HOGENOM; HBG505775; -.
DR   HOVERGEN; HBG106438; -.
DR   InParanoid; P33146; -.
DR   OrthoDB; EOG4BRWK5; -.
DR   ArrayExpress; P33146; -.
DR   Bgee; P33146; -.
DR   CleanEx; MM_CDH15; -.
DR   Genevestigator; P33146; -.
DR   GermOnline; ENSMUSG00000031962; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 4.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF01049; Cadherin_C; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 4.
DR   SUPFAM; SSF49313; Cadherin; 5.
DR   PROSITE; PS00232; CADHERIN_1; 2.
DR   PROSITE; PS50268; CADHERIN_2; 5.
PE   1: Evidence at protein level;
KW   Calcium; Cell adhesion; Cell membrane;
KW   Cleavage on pair of basic residues; Glycoprotein; Membrane; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     21       Potential.
FT   PROPEP       22     59       Potential.
FT                                /FTId=PRO_0000003807.
FT   CHAIN        60    784       Cadherin-15.
FT                                /FTId=PRO_0000003808.
FT   TOPO_DOM     60    605       Extracellular (Potential).
FT   TRANSMEM    606    625       Helical; (Potential).
FT   TOPO_DOM    626    784       Cytoplasmic (Potential).
FT   DOMAIN       60    151       Cadherin 1.
FT   DOMAIN      152    259       Cadherin 2.
FT   DOMAIN      260    374       Cadherin 3.
FT   DOMAIN      375    480       Cadherin 4.
FT   DOMAIN      481    589       Cadherin 5.
FT   COMPBIAS    745    756       Ser-rich.
FT   CARBOHYD    106    106       N-linked (GlcNAc...).
FT   CARBOHYD    226    226       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    530    530       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    537    537       N-linked (GlcNAc...).
FT   CARBOHYD    575    575       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   784 AA;  85660 MW;  D31AA287F2988DFA CRC64;
     MGSALLLALG LLAQSLGLSW AVPEPEPSTL YPWRRASAPG RVRRAWVIPP ISVSENHKRL
     PYPLVQIKSD KQQLGSVIYS IQGPGVDEEP RNVFSIDKFT GRVYLNATLD REKTDRFRLR
     AFALDLGGST LEDPTDLEIV VVDQNDNRPA FLQDVFRGHI LEGAIPGTFV TRAEATDADD
     PETDNAALRF SILEQGSPEF FSIDEHTGEI RTVQVGLDRE VVAVYNLTLQ VADMSGDGLT
     ATASAIISID DINDNAPEFT KDEFFMEAAE AVSGVDVGRL EVEDKDLPGS PNWVARFTIL
     EGDPDGQFKI YTDPKTNEGV LSVVKPLDYE SREQYELRVS VQNEAPLQAA APRARRGQTR
     VSVWVQDTNE APVFPENPLR TSIAEGAPPG TSVATFSARD PDTEQLQRIS YSKDYDPEDW
     LQVDGATGRI QTQRVLSPAS PFLKDGWYRA IILALDNAIP PSTATGTLSI EILEVNDHAP
     ALALPPSGSL CSEPDQGPGL LLGATDEDLP PHGAPFHFQL NPRVPDLGRN WSVSQINVSH
     ARLRLRHQVS EGLHRLSLLL QDSGEPPQQR EQTLNVTVCR CGSDGTCLPG AAALRGGGVG
     VSLGALVIVL ASTVVLLVLI LFAALRTRFR GHSRGKSLLH GLQEDLRDNI LNYDEQGGGE
     EDQDAYDINQ LRHPVEPRAT SRSLGRPPLR RDAPFSYVPQ PHRVLPTSPS DIANFISDGL
     EAADSDPSVP PYDTALIYDY EGDGSVAGTL SSILSSLGDE DQDYDYLRDW GPRFARLADM
     YGHQ
//
ID   KIF5A_MOUSE             Reviewed;        1027 AA.
AC   P33175; Q5DTP1; Q6PDY7; Q9Z2F9;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 3.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Kinesin heavy chain isoform 5A;
DE   AltName: Full=Kinesin heavy chain neuron-specific 1;
DE   AltName: Full=Neuronal kinesin heavy chain;
DE            Short=NKHC;
GN   Name=Kif5a; Synonyms=Kiaa4086, Kif5, Nkhc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=99000842; PubMed=9782088; DOI=10.1006/geno.1998.5427;
RA   Xia C., Rahman A., Yang Z., Goldstein L.S.B.;
RT   "Chromosomal localization reveals three kinesin heavy chain genes in
RT   mouse.";
RL   Genomics 52:209-213(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 89-237.
RC   TISSUE=Brain;
RX   MEDLINE=93077686; PubMed=1447303; DOI=10.1083/jcb.119.5.1287;
RA   Aizawa H., Sekine Y., Takemura R., Zhang Z., Nangaku M., Hirokawa N.;
RT   "Kinesin family in murine central nervous system.";
RL   J. Cell Biol. 119:1287-1296(1992).
RN   [6]
RP   INTERACTION WITH GRIP1.
RX   PubMed=11986669; DOI=10.1038/nature743;
RA   Setou M., Seog D.-H., Tanaka Y., Kanai Y., Takei Y., Kawagishi M.,
RA   Hirokawa N.;
RT   "Glutamate-receptor-interacting protein GRIP1 directly steers kinesin
RT   to dendrites.";
RL   Nature 417:83-87(2002).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12682084; DOI=10.1083/jcb.200301026;
RA   Xia C.H., Roberts E.A., Her L.S., Liu X., Williams D.S.,
RA   Cleveland D.W., Goldstein L.S.;
RT   "Abnormal neurofilament transport caused by targeted disruption of
RT   neuronal kinesin heavy chain KIF5A.";
RL   J. Cell Biol. 161:55-66(2003).
CC   -!- FUNCTION: Microtubule-dependent motor required for slow axonal
CC       transport of neurofilament proteins (NFH, NFM and NFL).
CC   -!- SUBUNIT: Oligomer composed of two heavy chains and two light
CC       chains (By similarity). Interacts with GRIP1.
CC   -!- INTERACTION:
CC       O70585:Dtnb; NbExp=2; IntAct=EBI-349710, EBI-349714;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Cytoplasm,
CC       cytoskeleton. Note=Concentrated in the cell body of the neurons,
CC       particularly in the perinuclear region.
CC   -!- DOMAIN: Composed of three structural domains: a large globular N-
CC       terminal domain which is responsible for the motor activity of
CC       kinesin (it hydrolyzes ATP and binds microtubule), a central
CC       alpha-helical coiled coil domain that mediates the heavy chain
CC       dimerization; and a small globular C-terminal domain which
CC       interacts with other proteins (such as the kinesin light chains),
CC       vesicles and membranous organelles.
CC   -!- DISRUPTION PHENOTYPE: Death shortly after birth. Neuron-specific
CC       deletion within the first 3 weeks after birth is lethal in 75% of
CC       animals. Surviving animals show accumulation of neurofilament
CC       proteins in neuronal soma, age-dependent sensory neuron
CC       degeneration, loss of large caliber axons, and hind limb paralysis
CC       with a stronger effect on sensory neurons compared with motor
CC       neurons.
CC   -!- SIMILARITY: Belongs to the kinesin-like protein family. Kinesin
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 kinesin-motor domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90503.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF067179; AAC79803.1; -; mRNA.
DR   EMBL; AK147352; BAE27862.1; -; mRNA.
DR   EMBL; AK147660; BAE28054.1; -; mRNA.
DR   EMBL; AK147707; BAE28087.1; -; mRNA.
DR   EMBL; AK220479; BAD90503.1; ALT_INIT; mRNA.
DR   EMBL; BC058396; AAH58396.1; -; mRNA.
DR   IPI; IPI00109420; -.
DR   PIR; C44259; C44259.
DR   RefSeq; NP_001034089.1; NM_001039000.4.
DR   RefSeq; NP_032473.2; NM_008447.4.
DR   UniGene; Mm.30355; -.
DR   ProteinModelPortal; P33175; -.
DR   SMR; P33175; 7-372.
DR   IntAct; P33175; 3.
DR   MINT; MINT-236733; -.
DR   STRING; P33175; -.
DR   PhosphoSite; P33175; -.
DR   PRIDE; P33175; -.
DR   Ensembl; ENSMUST00000099172; ENSMUSP00000096775; ENSMUSG00000074657.
DR   GeneID; 16572; -.
DR   KEGG; mmu:16572; -.
DR   UCSC; uc007his.1; mouse.
DR   CTD; 16572; -.
DR   MGI; MGI:109564; Kif5a.
DR   HOGENOM; HBG381775; -.
DR   HOVERGEN; HBG006210; -.
DR   InParanoid; P33175; -.
DR   OMA; RWRSGEN; -.
DR   OrthoDB; EOG4Q2DDS; -.
DR   NextBio; 290089; -.
DR   ArrayExpress; P33175; -.
DR   Bgee; P33175; -.
DR   CleanEx; MM_KIF5A; -.
DR   Genevestigator; P33175; -.
DR   GermOnline; ENSMUSG00000074657; Mus musculus.
DR   GO; GO:0035253; C:ciliary rootlet; IDA:MGI.
DR   GO; GO:0005871; C:kinesin complex; TAS:MGI.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003777; F:microtubule motor activity; TAS:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   Gene3D; G3DSA:3.40.850.10; kinesin_motor; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_DOMAIN1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_DOMAIN2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Microtubule; Motor protein; Nucleotide-binding.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1027       Kinesin heavy chain isoform 5A.
FT                                /FTId=PRO_0000125354.
FT   DOMAIN        2    330       Kinesin-motor.
FT   NP_BIND      86     93       ATP (By similarity).
FT   REGION      174    315       Microtubule-binding.
FT   REGION      907   1027       Globular.
FT   COILED      331    906
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   CONFLICT    146    146       L -> P (in Ref. 5).
FT   CONFLICT    282    282       S -> T (in Ref. 1; AAC79803).
FT   CONFLICT    362    363       KL -> NV (in Ref. 1; AAC79803).
FT   CONFLICT    727    727       T -> I (in Ref. 3; BAD90503).
FT   CONFLICT    976    976       A -> R (in Ref. 1; AAC79803).
SQ   SEQUENCE   1027 AA;  117019 MW;  419AD8C2D747DA0A CRC64;
     MAETNNECSI KVLCRFRPLN QAEILRGDKF IPIFQGDDSV IIGGKPYVFD RVFPPNTTQE
     QVYHACAMQI VKDVLAGYNG TIFAYGQTSS GKTHTMEGKL HDPQLMGIIP RIARDIFNHI
     YSMDENLEFH IKVSYFEIYL DKIRDLLDVT KTNLSVHEDK NRVPFVKGCT ERFVSSPEEI
     LDVIDEGKSN RHVAVTNMNE HSSRSHSIFL INIKQENVET EQKLSGKLYL VDLAGSEKVS
     KTGAEGAVLD EAKNINKSLS ALGNVISALA EGTKSYVPYR DSKMTRILQD SLGGNCRTTM
     FICCSPSSYN DAETKSTLMF GQRAKTIKNT ASVNLELTAE QWKKKYEKEK EKTKAQKETI
     AKLEAELSRW RNGENVPETE RLAGEDSALG AELCEETPVN DNSSIVVRIA PEERQKYEEE
     IRRLYKQLDD KDDEINQQSQ LIEKLKQQML DQEELLVSTR GDNEKVQREL SHLQSENDAA
     KDEVKEVLQA LEELAVNYDQ KSQEVEEKSQ QNQLLVDELS QKVATMLSLE SELQRLQEVS
     GHQRKRIAEV LNGLMRDLSE FSVIVGNGEI KLPVEISGAI EEEFTVARLY ISKIKSEVKS
     VVKRCRQLEN LQVECHRKME VTGRELSSCQ LLISQHEAKI RSLTEYMQTV ELKKRHLEES
     YDSLSDELAR LQAHETVHEV ALKDKEPDTQ DAEEVKKALE LQMENHREAH HRQLARLRDE
     INEKQKTIDE LKDLNQKLQL ELEKLQADYE RLKNEENEKS AKLQELTFLY ERHEQSKQDL
     KGLEETVARE LQTLHNLRKL FVQDVTTRVK KSAEMEPEDS GGIHSQKQKI SFLENNLEQL
     TKVHKQLVRD NADLRCELPK LEKRLRATAE RVKALEGALK EAKEGAMKDK RRYQQEVDRI
     KEAVRYKSSG KRGHSAQIAK PVRPGHYPAS SPTNPYGTRS PECISYTNNL FQNYQNLHLQ
     AAPSSTSDMY FASSGATSVA PLASYQKANM DNGNATDIND NRSDLPCGYE AEDQAKLFPL
     HQETAAS
//
ID   OPRK_MOUSE              Reviewed;         380 AA.
AC   P33534;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Kappa-type opioid receptor;
DE            Short=K-OR-1;
DE            Short=KOR-1;
DE   AltName: Full=MSL-1;
GN   Name=Oprk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=93342064; PubMed=8393575; DOI=10.1073/pnas.90.14.6736;
RA   Yasuda K., Raynor K., Kong H., Breder C.D., Takeda J., Reisine T.,
RA   Bell G.I.;
RT   "Cloning and functional comparison of kappa and delta opioid receptors
RT   from mouse brain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:6736-6740(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95100967; PubMed=7802669; DOI=10.1006/bbrc.1994.2814;
RA   Nishi M., Takeshima H., Mori M., Nakagawara K., Takeuchi T.;
RT   "Structure and chromosomal mapping of genes for the mouse kappa-opioid
RT   receptor and an opioid receptor homologue (MOR-C).";
RL   Biochem. Biophys. Res. Commun. 205:1353-1357(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95251663; PubMed=7733933; DOI=10.1006/bbrc.1995.1547;
RA   Liu H.C., Lu S., Augustin L.B., Felsheim R.F., Chen H.C., Loh H.H.,
RA   Wei L.N.;
RT   "Cloning and promoter mapping of mouse kappa opioid receptor gene.";
RL   Biochem. Biophys. Res. Commun. 209:639-647(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96084989; PubMed=7499487; DOI=10.1016/0165-5728(95)00116-J;
RA   Belkowski S.M., Zhu J., Liu-Chen L.Y., Eisenstein T.K., Adler M.W.,
RA   Rogers T.J.;
RT   "Sequence of kappa-opioid receptor cDNA in the R1.1 thymoma cell
RT   line.";
RL   J. Neuroimmunol. 62:113-117(1995).
CC   -!- FUNCTION: Inhibits neurotransmitter release by reducing calcium
CC       ion currents and increasing potassium ion conductance. Receptor
CC       for dynorphins. May play a role in arousal and regulation of
CC       autonomic and neuroendocrine functions.
CC   -!- SUBUNIT: Interacts with SLC9A3R1. Interacts with GABARAPL1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Brain (neocortex, hippocampus, amygdala,
CC       medial habenula, hypothalamus, locus ceruleus, and parabrachial
CC       nucleus).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; L11065; AAA39363.1; -; mRNA.
DR   EMBL; D31665; BAA06508.1; -; Genomic_DNA.
DR   EMBL; S77872; AAB34130.2; -; Genomic_DNA.
DR   EMBL; S77868; AAB34130.2; JOINED; Genomic_DNA.
DR   EMBL; S77869; AAB34130.2; JOINED; Genomic_DNA.
DR   EMBL; S81111; AAP32232.1; -; mRNA.
DR   IPI; IPI00113663; -.
DR   PIR; A48227; A48227.
DR   PIR; JC2434; JC2434.
DR   RefSeq; NP_035141.1; NM_011011.1.
DR   UniGene; Mm.7977; -.
DR   ProteinModelPortal; P33534; -.
DR   SMR; P33534; 59-346.
DR   STRING; P33534; -.
DR   PhosphoSite; P33534; -.
DR   PRIDE; P33534; -.
DR   Ensembl; ENSMUST00000027038; ENSMUSP00000027038; ENSMUSG00000025905.
DR   GeneID; 18387; -.
DR   KEGG; mmu:18387; -.
DR   UCSC; uc007afo.1; mouse.
DR   CTD; 18387; -.
DR   MGI; MGI:97439; Oprk1.
DR   eggNOG; roNOG11103; -.
DR   HOGENOM; HBG715643; -.
DR   HOVERGEN; HBG106919; -.
DR   InParanoid; P33534; -.
DR   OMA; RNTVQDP; -.
DR   OrthoDB; EOG4GMTXD; -.
DR   PhylomeDB; P33534; -.
DR   NextBio; 293980; -.
DR   ArrayExpress; P33534; -.
DR   Bgee; P33534; -.
DR   CleanEx; MM_OPRK1; -.
DR   Genevestigator; P33534; -.
DR   GermOnline; ENSMUSG00000025905; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004987; F:kappa-opioid receptor activity; IEA:InterPro.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR000452; Kappa_opi_rcpt.
DR   InterPro; IPR001418; Opioid_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00532; KAPPAOPIOIDR.
DR   PRINTS; PR00384; OPIOIDR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Receptor; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN         1    380       Kappa-type opioid receptor.
FT                                /FTId=PRO_0000069968.
FT   TOPO_DOM      1     58       Extracellular (Potential).
FT   TRANSMEM     59     85       Helical; Name=1; (Potential).
FT   TOPO_DOM     86     95       Cytoplasmic (Potential).
FT   TRANSMEM     96    117       Helical; Name=2; (Potential).
FT   TOPO_DOM    118    132       Extracellular (Potential).
FT   TRANSMEM    133    154       Helical; Name=3; (Potential).
FT   TOPO_DOM    155    173       Cytoplasmic (Potential).
FT   TRANSMEM    174    196       Helical; Name=4; (Potential).
FT   TOPO_DOM    197    222       Extracellular (Potential).
FT   TRANSMEM    223    247       Helical; Name=5; (Potential).
FT   TOPO_DOM    248    275       Cytoplasmic (Potential).
FT   TRANSMEM    276    299       Helical; Name=6; (Potential).
FT   TOPO_DOM    300    311       Extracellular (Potential).
FT   TRANSMEM    312    333       Helical; Name=7; (Potential).
FT   TOPO_DOM    334    380       Cytoplasmic (Potential).
FT   LIPID       345    345       S-palmitoyl cysteine (Potential).
FT   CARBOHYD     25     25       N-linked (GlcNAc...) (By similarity).
FT   CARBOHYD     39     39       N-linked (GlcNAc...) (By similarity).
FT   DISULFID    131    210       By similarity.
FT   CONFLICT    211    211       S -> L (in Ref. 2 and 3).
FT   CONFLICT    231    231       F -> V (in Ref. 2 and 3).
SQ   SEQUENCE   380 AA;  42652 MW;  FA4FC947D4545318 CRC64;
     MESPIQIFRG DPGPTCSPSA CLLPNSSSWF PNWAESDSNG SVGSEDQQLE SAHISPAIPV
     IITAVYSVVF VVGLVGNSLV MFVIIRYTKM KTATNIYIFN LALADALVTT TMPFQSAVYL
     MNSWPFGDVL CKIVISIDYY NMFTSIFTLT MMSVDRYIAV CHPVKALDFR TPLKAKIINI
     CIWLLASSVG ISAIVLGGTK VREDVDVIEC SLQFPDDEYS WWDLFMKICV FVFAFVIPVL
     IIIVCYTLMI LRLKSVRLLS GSREKDRNLR RITKLVLVVV AVFIICWTPI HIFILVEALG
     STSHSTAALS SYYFCIALGY TNSSLNPVLY AFLDENFKRC FRDFCFPIKM RMERQSTNRV
     RNTVQDPASM RDVGGMNKPV
//
ID   RANG_MOUSE              Reviewed;         203 AA.
AC   P34022; P34023; Q3TL81; Q9D894; Q9DCA3;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Ran-specific GTPase-activating protein;
DE   AltName: Full=HpaII tiny fragments locus 9a protein;
DE   AltName: Full=Ran-binding protein 1;
DE            Short=RANBP1;
GN   Name=Ranbp1; Synonyms=Htf9-a, Htf9a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94077185; PubMed=8255297; DOI=10.1038/366585a0;
RA   Coutavas E., Ren M., Oppenheim J.D., D'Eustachio P., Rush M.G.;
RT   "Characterization of proteins that interact with the cell-cycle
RT   regulatory protein Ran/TC4.";
RL   Nature 366:585-587(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=91365246; PubMed=1889746; DOI=10.1016/0378-1119(91)90274-F;
RA   Bressan A., Somma M.P., Lewis J., Santolamazza C., Copeland N.G.,
RA   Gilbert D.J., Jenkins N.A., Lavia P.;
RT   "Characterization of the opposite-strand genes from the mouse
RT   bidirectionally transcribed HTF9 locus.";
RL   Gene 103:201-209(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RA   Lavia P.;
RL   Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow, Brain, Small intestine, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
CC   -!- FUNCTION: Inhibits GTP exchange on Ran. Forms a Ran-GTP-RANBP1
CC       trimeric complex. Increase GTP hydrolysis induced by the Ran
CC       GTPase activating protein RANGAP1. May act in an intracellular
CC       signaling pathway which may control the progression through the
CC       cell cycle by regulating the transport of protein and nucleic
CC       acids across the nuclear membrane.
CC   -!- MISCELLANEOUS: Htf9a (RanBP1) and Htf9c are transcribed with
CC       opposite polarity from complementary DNA strands from a shared
CC       bidirectional TATA-less promoter.
CC   -!- SIMILARITY: Belongs to the RANBP1 family.
CC   -!- SIMILARITY: Contains 1 RanBD1 domain.
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DR   EMBL; X56046; CAA39517.1; -; mRNA.
DR   EMBL; L25255; AAA16195.1; -; mRNA.
DR   EMBL; X56045; CAA39516.1; -; mRNA.
DR   EMBL; AK002989; BAB22501.1; -; mRNA.
DR   EMBL; AK008276; BAB25569.1; -; mRNA.
DR   EMBL; AK088781; BAC40569.1; -; mRNA.
DR   EMBL; AK151167; BAE30170.1; -; mRNA.
DR   EMBL; AK166642; BAE38911.1; -; mRNA.
DR   EMBL; AK167053; BAE39217.1; -; mRNA.
DR   EMBL; BC061140; AAH61140.1; -; mRNA.
DR   IPI; IPI00321978; -.
DR   PIR; JQ1973; JQ1973.
DR   RefSeq; NP_035369.2; NM_011239.2.
DR   UniGene; Mm.235287; -.
DR   UniGene; Mm.477077; -.
DR   ProteinModelPortal; P34022; -.
DR   SMR; P34022; 22-167.
DR   STRING; P34022; -.
DR   PhosphoSite; P34022; -.
DR   REPRODUCTION-2DPAGE; P34022; -.
DR   PRIDE; P34022; -.
DR   Ensembl; ENSMUST00000115645; ENSMUSP00000111309; ENSMUSG00000005732.
DR   GeneID; 19385; -.
DR   KEGG; mmu:19385; -.
DR   UCSC; uc007ymy.1; mouse.
DR   CTD; 19385; -.
DR   MGI; MGI:96269; Ranbp1.
DR   HOGENOM; HBG619641; -.
DR   HOVERGEN; HBG006958; -.
DR   InParanoid; P34022; -.
DR   OMA; EHDTSTE; -.
DR   OrthoDB; EOG4XD3S8; -.
DR   PhylomeDB; P34022; -.
DR   NextBio; 296493; -.
DR   ArrayExpress; P34022; -.
DR   Bgee; P34022; -.
DR   CleanEx; MM_RANBP1; -.
DR   Genevestigator; P34022; -.
DR   GermOnline; ENSMUSG00000005732; Mus musculus.
DR   GO; GO:0005813; C:centrosome; IDA:MGI.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0046907; P:intracellular transport; IEA:InterPro.
DR   GO; GO:0046604; P:positive regulation of mitotic centrosome separation; IDA:MGI.
DR   GO; GO:0007051; P:spindle organization; IDA:MGI.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR000156; RanBP.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00638; Ran_BP1; 1.
DR   SMART; SM00160; RanBD; 1.
DR   PROSITE; PS50196; RANBD1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; GTPase activation; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    203       Ran-specific GTPase-activating protein.
FT                                /FTId=PRO_0000213668.
FT   DOMAIN       26    164       RanBD1.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      13     13       Phosphothreonine (By similarity).
FT   MOD_RES      14     14       Phosphoserine (By similarity).
FT   MOD_RES      15     15       Phosphothreonine (By similarity).
FT   MOD_RES      21     21       Phosphoserine (By similarity).
FT   MOD_RES      60     60       Phosphoserine.
FT   MOD_RES     150    150       N6-acetyllysine (By similarity).
FT   MOD_RES     182    182       N6-acetyllysine (By similarity).
FT   CONFLICT      9      9       E -> A (in Ref. 2).
FT   CONFLICT     22     24       NHD -> TTH (in Ref. 2).
FT   CONFLICT     33     33       L -> V (in Ref. 1 and 2).
FT   CONFLICT     67     67       W -> R (in Ref. 4; BAB25569).
FT   CONFLICT     70     72       RGT -> PRH (in Ref. 2).
FT   CONFLICT     85     85       T -> P (in Ref. 4; BAB25569).
FT   CONFLICT    126    126       A -> T (in Ref. 2 and 3).
SQ   SEQUENCE   203 AA;  23596 MW;  4CA6C21DDF5B6F4F CRC64;
     MAAAKDSHED HDTSTENADE SNHDPQFEPI VSLPEQEIKT LEEDEEELFK MRAKLFRFAS
     ENDLPEWKER GTGDVKLLKH KEKGTIRLLM RRDKTLKICA NHYITPMMEL KPNAGSDRAW
     VWNTHADFAD ECPKPELLAI RFLNAENAQK FKTKFEECRK EIEEREKKGP GKNDNAEKVA
     EKLEALSVRE AREEAEEKSE EKQ
//
ID   FAK1_MOUSE              Reviewed;        1090 AA.
AC   P34152; O08578; Q5DTH7; Q8C513; Q8CFH7; Q8CHM2; Q8K2S0; Q9DAW3;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 3.
DT   08-MAR-2011, entry version 137.
DE   RecName: Full=Focal adhesion kinase 1;
DE            Short=FADK 1;
DE            EC=2.7.10.2;
DE   AltName: Full=Protein-tyrosine kinase 2;
DE   AltName: Full=pp125FAK;
GN   Name=Ptk2; Synonyms=Fadk, Fak, Fak1, Kiaa4203;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   STRAIN=BALB/c; TISSUE=Embryo;
RX   MEDLINE=92409541; PubMed=1528852; DOI=10.1073/pnas.89.18.8487;
RA   Hanks S.K., Calalb M.B., Harper M.C., Patel S.K.;
RT   "Focal adhesion protein-tyrosine kinase phosphorylated in response to
RT   cell attachment to fibronectin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:8487-8491(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 7).
RC   STRAIN=BALB/c; TISSUE=Brain, and Embryo;
RA   Yamakawa N.;
RT   "Focal adhesion kinase.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 8).
RC   STRAIN=C57BL/6J; TISSUE=Placenta, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 2-19; 39-57; 77-86; 92-121; 132-177; 179-204;
RP   210-218; 222-259; 313-319; 350-381; 465-492; 504-546; 589-616;
RP   622-635; 666-703; 707-728; 735-762; 836-876; 885-971; 942-971;
RP   980-993; 1001-1019 AND 1027-1082, PROTEIN SEQUENCE OF 386-451 (ISOFORM
RP   3), CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2,
RP   PHOSPHORYLATION AT SER-948, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RA   Bienvenut W.V., Sandilands E., Serrels B., Brunton V.G., Sumpton D.P.,
RA   Frame M.C.;
RL   Submitted (MAR-2008) to UniProtKB.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 391-460 (ISOFORMS 1 AND 2).
RC   STRAIN=ICR X Swiss Webster;
RX   MEDLINE=98019252; PubMed=9353341; DOI=10.1074/jbc.272.45.28720;
RA   Burgaya F., Toutant M., Studler J.-M., Costa A., Le Bert M.,
RA   Gelman M., Girault J.A.;
RT   "Alternatively spliced focal adhesion kinase in rat brain with
RT   increased autophosphorylation activity.";
RL   J. Biol. Chem. 272:28720-28725(1997).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 391-417.
RC   STRAIN=129/SvJ;
RA   Asano H., Komiyama H.K., Grant S.G.;
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   INTERACTION WITH TGFB1I1.
RX   MEDLINE=98086276; PubMed=9422762; DOI=10.1074/jbc.273.2.1003;
RA   Matsuya M., Sasaki H., Aoto H., Mitaka T., Nagura K., Ohba T.,
RA   Ishino M., Takahashi S., Suzuki R., Sasaki T.;
RT   "Cell adhesion kinase beta forms a complex with a new member, Hic-5,
RT   of proteins localized at focal adhesions.";
RL   J. Biol. Chem. 273:1003-1014(1998).
RN   [10]
RP   INTERACTION WITH TGFB1I1.
RX   PubMed=9756887; DOI=10.1074/jbc.273.41.26516;
RA   Fujita H., Kamiguchi K., Cho D., Shibanuma M., Morimoto C.,
RA   Tachibana K.;
RT   "Interaction of Hic-5, A senescence-related protein, with focal
RT   adhesion kinase.";
RL   J. Biol. Chem. 273:26516-26521(1998).
RN   [11]
RP   PHOSPHORYLATION AT TYR-428; TYR-438; TYR-614; TYR-615; TYR-899 AND
RP   TYR-963.
RX   MEDLINE=21313779; PubMed=11420674; DOI=10.1038/sj.onc.1204359;
RA   Nakamura K., Yano H., Schaefer E., Sabe H.;
RT   "Different modes and qualities of tyrosine phosphorylation of Fak and
RT   Pyk2 during epithelial-mesenchymal transdifferentiation and cell
RT   migration: analysis of specific phosphorylation events using site-
RT   directed antibodies.";
RL   Oncogene 20:2626-2635(2001).
RN   [12]
RP   INTERACTION WITH SORBS1.
RX   PubMed=9461600; DOI=10.1074/jbc.273.7.4073;
RA   Ribon V., Herrera R., Kay B.K., Saltiel A.R.;
RT   "A role for CAP, a novel, multifunctional Src homology 3 domain-
RT   containing protein in formation of actin stress fibers and focal
RT   adhesions.";
RL   J. Biol. Chem. 273:4073-4080(1998).
RN   [13]
RP   INTERACTION WITH BCAR3.
RX   PubMed=10896938; DOI=10.1074/jbc.M003074200;
RA   Gotoh T., Cai D., Tian X., Feig L.A., Lerner A.;
RT   "p130Cas regulates the activity of AND-34, a novel Ral, Rap1, and R-
RT   Ras guanine nucleotide exchange factor.";
RL   J. Biol. Chem. 275:30118-30123(2000).
RN   [14]
RP   INTERACTION WITH SHB.
RX   PubMed=12464388; DOI=10.1016/S0898-6568(02)00076-1;
RA   Holmqvist K., Cross M.J., Riley D., Welsh M.;
RT   "The Shb adaptor protein causes Src-dependent cell spreading and
RT   activation of focal adhesion kinase in murine brain endothelial
RT   cells.";
RL   Cell. Signal. 15:171-179(2003).
RN   [15]
RP   FUNCTION, INTERACTION WITH RGNEF, AND MUTAGENESIS OF LEU-1072.
RX   PubMed=12702722; DOI=10.1074/jbc.M302381200;
RA   Zhai J., Lin H., Nie Z., Wu J., Canete-Soler R., Schlaepfer W.W.,
RA   Schlaepfer D.D.;
RT   "Direct interaction of focal adhesion kinase with p190RhoGEF.";
RL   J. Biol. Chem. 278:24865-24873(2003).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-614; TYR-615 AND
RP   TYR-963, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-948, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-614 AND TYR-615, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 959-1084, AND INTERACTION
RP   WITH PXN.
RX   PubMed=11799401; DOI=10.1038/nsb755;
RA   Hayashi I., Vuori K., Liddington R.C.;
RT   "The focal adhesion targeting (FAT) region of focal adhesion kinase is
RT   a four-helix bundle that binds paxillin.";
RL   Nat. Struct. Biol. 9:101-106(2002).
CC   -!- FUNCTION: Non-receptor protein-tyrosine kinase implicated in
CC       signaling pathways involved in cell motility, proliferation and
CC       apoptosis. Activated by tyrosine-phosphorylation in response to
CC       either integrin clustering induced by cell adhesion or antibody
CC       cross-linking, or via G-protein coupled receptor (GPCR) occupancy
CC       by ligands such as bombesin or lysophosphatidic acid, or via LDL
CC       receptor occupancy. Microtubule-induced dephosphorylation at Tyr-
CC       397 is crucial for the induction of focal adhesion disassembly (By
CC       similarity). Plays a potential role in oncogenic transformations
CC       resulting in increased kinase activity.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBUNIT: Interacts with STEAP4 (By similarity). Interacts with CAS
CC       family members and with GIT1, SORBS1 and BCAR3. Interacts with
CC       RGNEF, SHB and TGFB1I1. Interacts with ZFYVE21. Interacts with
CC       ESR1, PIK3R (alpha and/or beta) and SRC (By similarity).
CC   -!- INTERACTION:
CC       Q61140:Bcar1; NbExp=1; IntAct=EBI-77070, EBI-77088;
CC       P54763:Ephb2; NbExp=1; IntAct=EBI-77070, EBI-537711;
CC       Q60631:Grb2; NbExp=1; IntAct=EBI-77070, EBI-1688;
CC       Q8VI36:Pxn; NbExp=1; IntAct=EBI-77070, EBI-983394;
CC   -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell
CC       membrane; Peripheral membrane protein; Cytoplasmic side.
CC       Note=Constituent of focal adhesions.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC       Name=1;
CC         IsoId=P34152-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P34152-2; Sequence=VSP_004976;
CC       Name=3;
CC         IsoId=P34152-3; Sequence=VSP_004975, VSP_004976;
CC         Note=Peptide 386-413 identified and sequenced in Ref.6;
CC       Name=4;
CC         IsoId=P34152-4; Sequence=VSP_004975, VSP_004976, VSP_034003;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=P34152-5; Sequence=VSP_033999, VSP_034004, VSP_034005;
CC       Name=6;
CC         IsoId=P34152-6; Sequence=VSP_004975, VSP_004976, VSP_034004,
CC                                  VSP_034005;
CC         Note=Ref.5 (BC030180) sequence differs from that shown due to a
CC         stop codon in position 912 which was translated as Trp to extend
CC         the sequence. No experimental confirmation available;
CC       Name=7;
CC         IsoId=P34152-7; Sequence=VSP_034000, VSP_034001, VSP_034002;
CC         Note=No experimental confirmation available;
CC       Name=8;
CC         IsoId=P34152-8; Sequence=VSP_033998;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The first Pro-rich domain interacts with the SH3 domain of
CC       CRK-associated substrate (BCAR1) and CASL.
CC   -!- DOMAIN: The C-terminal region is the site of focal adhesion
CC       targeting (FAT) sequence which mediates the localization of FAK1
CC       to focal adhesions.
CC   -!- PTM: Phosphorylated on 6 tyrosine residues upon activation.
CC       Microtubule-induced dephosphorylation at Tyr-428 could be
CC       catalyzed by PTPN11 and regulated by ZFYVE21 (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. FAK subfamily.
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC37757.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC       Sequence=BAD90317.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; M95408; AAA37592.1; -; mRNA.
DR   EMBL; AB030035; BAC53924.1; -; mRNA.
DR   EMBL; AB011499; BAC53890.1; -; mRNA.
DR   EMBL; AK005468; BAB24058.1; -; mRNA.
DR   EMBL; AK079821; BAC37757.1; ALT_INIT; mRNA.
DR   EMBL; AK220543; BAD90317.1; ALT_INIT; mRNA.
DR   EMBL; BC030180; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AF025652; AAB95262.1; -; Genomic_DNA.
DR   EMBL; AF025648; AAB95262.1; JOINED; Genomic_DNA.
DR   EMBL; AF025649; AAB95262.1; JOINED; Genomic_DNA.
DR   EMBL; AF025650; AAB95262.1; JOINED; Genomic_DNA.
DR   EMBL; AF025651; AAB95262.1; JOINED; Genomic_DNA.
DR   EMBL; AF025652; AAB95263.1; -; Genomic_DNA.
DR   EMBL; AF025648; AAB95263.1; JOINED; Genomic_DNA.
DR   EMBL; AF025649; AAB95263.1; JOINED; Genomic_DNA.
DR   EMBL; AF025650; AAB95263.1; JOINED; Genomic_DNA.
DR   EMBL; U77074; AAB51229.1; -; Genomic_DNA.
DR   IPI; IPI00113563; -.
DR   IPI; IPI00230629; -.
DR   IPI; IPI00338858; -.
DR   IPI; IPI00625418; -.
DR   IPI; IPI00875543; -.
DR   IPI; IPI00895208; -.
DR   IPI; IPI00895269; -.
DR   IPI; IPI00895396; -.
DR   PIR; A46166; A46166.
DR   RefSeq; NP_001123881.1; NM_001130409.1.
DR   RefSeq; NP_032008.2; NM_007982.2.
DR   UniGene; Mm.254494; -.
DR   PDB; 1K40; X-ray; 2.25 A; A=959-1084.
DR   PDB; 1KKY; Model; -; B=959-1084.
DR   PDB; 1KL0; Model; -; A=959-1084.
DR   PDBsum; 1K40; -.
DR   PDBsum; 1KKY; -.
DR   PDBsum; 1KL0; -.
DR   ProteinModelPortal; P34152; -.
DR   SMR; P34152; 33-724, 959-1084.
DR   IntAct; P34152; 8.
DR   MINT; MINT-141959; -.
DR   STRING; P34152; -.
DR   PhosphoSite; P34152; -.
DR   PRIDE; P34152; -.
DR   Ensembl; ENSMUST00000057684; ENSMUSP00000059308; ENSMUSG00000022607.
DR   Ensembl; ENSMUST00000068756; ENSMUSP00000067956; ENSMUSG00000022607.
DR   Ensembl; ENSMUST00000080736; ENSMUSP00000079561; ENSMUSG00000022607.
DR   Ensembl; ENSMUST00000110033; ENSMUSP00000105660; ENSMUSG00000022607.
DR   Ensembl; ENSMUST00000110036; ENSMUSP00000105663; ENSMUSG00000022607.
DR   GeneID; 14083; -.
DR   KEGG; mmu:14083; -.
DR   UCSC; uc007wbx.1; mouse.
DR   CTD; 14083; -.
DR   MGI; MGI:95481; Ptk2.
DR   eggNOG; roNOG14526; -.
DR   GeneTree; ENSGT00600000084269; -.
DR   HOVERGEN; HBG004018; -.
DR   InParanoid; P34152; -.
DR   OrthoDB; EOG4WH8K1; -.
DR   BRENDA; 2.7.10.2; 244.
DR   NextBio; 285100; -.
DR   ArrayExpress; P34152; -.
DR   Bgee; P34152; -.
DR   CleanEx; MM_PTK2; -.
DR   Genevestigator; P34152; -.
DR   GermOnline; ENSMUSG00000022607; Mus musculus.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:EC.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR   GO; GO:0021955; P:central nervous system neuron axonogenesis; IMP:MGI.
DR   GO; GO:0043542; P:endothelial cell migration; IMP:MGI.
DR   GO; GO:0040023; P:establishment of nucleus localization; IDA:MGI.
DR   GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; TAS:MGI.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:MGI.
DR   GO; GO:0050771; P:negative regulation of axonogenesis; IMP:MGI.
DR   GO; GO:0046621; P:negative regulation of organ growth; IGI:MGI.
DR   GO; GO:0051964; P:negative regulation of synaptogenesis; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IDA:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; IMP:MGI.
DR   GO; GO:0007172; P:signal complex assembly; IEA:InterPro.
DR   GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR005189; Focal_adhesion_kin_target_dom.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF03623; Focal_AT; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   ProDom; PD006413; Focal_adhesion_target_reg; 1.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   SUPFAM; SSF68993; Focal_AT; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00660; FERM_1; FALSE_NEG.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW   Cell junction; Cell membrane; Direct protein sequencing; Kinase;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Transferase;
KW   Tyrosine-protein kinase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2   1090       Focal adhesion kinase 1.
FT                                /FTId=PRO_0000088078.
FT   DOMAIN       35    355       FERM.
FT   DOMAIN      469    718       Protein kinase.
FT   NP_BIND     466    474       ATP (By similarity).
FT   REGION      745   1090       Interaction with TGFB1I1 (By similarity).
FT   REGION      950   1090       Interaction with RGNEF.
FT   COMPBIAS    750    771       Pro-rich.
FT   COMPBIAS    901    951       Pro-rich.
FT   ACT_SITE    584    584       Proton acceptor (By similarity).
FT   BINDING     492    492       ATP (By similarity).
FT   MOD_RES       2      2       N-acetylalanine.
FT   MOD_RES       5      5       Phosphotyrosine (By similarity).
FT   MOD_RES      13     13       Phosphothreonine (By similarity).
FT   MOD_RES      16     16       Phosphoserine (By similarity).
FT   MOD_RES      29     29       Phosphoserine (By similarity).
FT   MOD_RES     386    386       Phosphothreonine (By similarity).
FT   MOD_RES     390    390       Phosphoserine (By similarity).
FT   MOD_RES     392    392       Phosphoserine (By similarity).
FT   MOD_RES     425    425       Phosphothreonine (By similarity).
FT   MOD_RES     428    428       Phosphotyrosine.
FT   MOD_RES     437    437       Phosphothreonine (By similarity).
FT   MOD_RES     438    438       Phosphotyrosine.
FT   MOD_RES     606    606       Phosphoserine (By similarity).
FT   MOD_RES     608    608       Phosphotyrosine (By similarity).
FT   MOD_RES     613    613       Phosphothreonine (By similarity).
FT   MOD_RES     614    614       Phosphotyrosine; by autocatalysis.
FT   MOD_RES     615    615       Phosphotyrosine; by autocatalysis.
FT   MOD_RES     618    618       Phosphoserine (By similarity).
FT   MOD_RES     715    715       Phosphoserine (By similarity).
FT   MOD_RES     738    738       Phosphothreonine (By similarity).
FT   MOD_RES     740    740       Phosphoserine (By similarity).
FT   MOD_RES     743    743       Phosphoserine (By similarity).
FT   MOD_RES     746    746       Phosphoserine (By similarity).
FT   MOD_RES     754    754       Phosphoserine (By similarity).
FT   MOD_RES     758    758       Phosphotyrosine (By similarity).
FT   MOD_RES     760    760       Phosphoserine (By similarity).
FT   MOD_RES     878    878       Phosphoserine (By similarity).
FT   MOD_RES     881    881       Phosphoserine (By similarity).
FT   MOD_RES     899    899       Phosphotyrosine.
FT   MOD_RES     948    948       Phosphoserine.
FT   MOD_RES     963    963       Phosphotyrosine.
FT   VAR_SEQ     199   1090       Missing (in isoform 8).
FT                                /FTId=VSP_033998.
FT   VAR_SEQ     392    392       S -> SGVS (in isoform 5).
FT                                /FTId=VSP_033999.
FT   VAR_SEQ     393    423       Missing (in isoform 3, isoform 4 and
FT                                isoform 6).
FT                                /FTId=VSP_004975.
FT   VAR_SEQ     393    417       Missing (in isoform 7).
FT                                /FTId=VSP_034000.
FT   VAR_SEQ     443    450       KSYGIDEA -> T (in isoform 2, isoform 3,
FT                                isoform 4 and isoform 6).
FT                                /FTId=VSP_004976.
FT   VAR_SEQ     511    534       LTMRQFDHPHIVKLIGVITENPVW -> SEVIFASKKIQLG
FT                                PGIFDIICLSA (in isoform 7).
FT                                /FTId=VSP_034001.
FT   VAR_SEQ     535   1090       Missing (in isoform 7).
FT                                /FTId=VSP_034002.
FT   VAR_SEQ     941    941       K -> KPWR (in isoform 4).
FT                                /FTId=VSP_034003.
FT   VAR_SEQ     942    954       LQPQEISPPPTAN -> VGICACAMWSVPC (in
FT                                isoform 5 and isoform 6).
FT                                /FTId=VSP_034004.
FT   VAR_SEQ     955   1090       Missing (in isoform 5 and isoform 6).
FT                                /FTId=VSP_034005.
FT   MUTAGEN    1072   1072       L->S: Loss of interaction with RGNEF.
FT   CONFLICT     32     32       A -> T (in Ref. 5; BC030180).
FT   CONFLICT     42     42       Y -> H (in Ref. 1; AAA37592).
FT   CONFLICT     87     87       L -> V (in Ref. 3; BAB24058).
FT   CONFLICT    128    128       Y -> D (in Ref. 3; BAB24058).
FT   CONFLICT    146    146       F -> V (in Ref. 3; BAB24058).
FT   CONFLICT    157    157       Q -> L (in Ref. 5; BC030180).
FT   CONFLICT    225    225       Q -> H (in Ref. 3; BAC37757).
FT   CONFLICT    250    250       V -> M (in Ref. 3; BAC37757).
FT   CONFLICT    800    800       Q -> P (in Ref. 5; BC030180).
FT   HELIX       960    980
FT   HELIX       985    987
FT   HELIX       989   1009
FT   HELIX      1010   1012
FT   HELIX      1018   1044
FT   HELIX      1048   1081
SQ   SEQUENCE   1090 AA;  123537 MW;  7C795105A9B9DCA6 CRC64;
     MAAAYLDPNL NHTPSSSTKT HLGTGMERSP GAMERVLKVF HYFESSSEPT TWASIIRHGD
     ATDVRGIIQK IVDSHKVKHV ACYGFRLSHL RSEEVHWLHV DMGVSSVREK YELAHPPEEW
     KYELRIRYLP KGFLNQFTED KPTLNFFYQQ VKSDYMQEIA DQVDQEIALK LGCLEIRRSY
     WEMRGNALEK KSNYEVLEKD VGLKRFFPKS LLDSVKAKTL RKLIQQTFRQ FANLNREESI
     LKFFEILSPV YRFDKECFKC ALGSSWIISV ELAIGPEEGI SYLTDKGCNP THLADFNQVQ
     TIQYSNSEDK DRKGMLQLKI AGAPEPLTVT APSLTIAENM ADLIDGYCRL VNGATQSFII
     RPQKEGERAL PSIPKLANSE KQGMRTHAVS VSHCQHKVKK ARRFLPLVFC SLEPPPTDEI
     SGDETDDYAE IIDEEDTYTM PSKSYGIDEA RDYEIQRERI ELGRCIGEGQ FGDVHQGVYL
     SPENPALAVA IKTCKNCTSD SVREKFLQEA LTMRQFDHPH IVKLIGVITE NPVWIIMELC
     TLGELRSFLQ VRKYSLDLAS LILYAYQLST ALAYLESKRF VHRDIAARNV LVSSNDCVKL
     GDFGLSRYME DSTYYKASKG KLPIKWMAPE SINFRRFTSA SDVWMFGVCM WEILMHGVKP
     FQGVKNNDVI GRIENGERLP MPPNCPPTLY SLMTKCWAYD PSRRPRFTEL KAQLSTILEE
     EKVQQEERMR MESRRQATVS WDSGGSDEAP PKPSRPGYPS PRSSEGFYPS PQHMVQTNHY
     QVSGYPGSHG IPAMAGSIYQ GQASLLDQTE LWNHRPQEMS MWQPSVEDSA ALDLRGMGQV
     LPPHLMEERL IRQQQEMEED QRWLEKEERF LKPDVRLSRG SIDREDGSFQ GPTGNQHIYQ
     PVGKPDPAAP PKKPPRPGAP GHLSNLSSIS SPADSYNEGV KLQPQEISPP PTANLDRSND
     KVYENVTGLV KAVIEMSSKI QPAPPEEYVP MVKEVGLALR TLLATVDETI PALPASTHRE
     IEMAQKLLNS DLGELISKMK LAQQYVMTSL QQEYKKQMLT AAHALAVDAK NLLDVIDQAR
     LKMLGQTRPH
//
ID   MIF_MOUSE               Reviewed;         115 AA.
AC   P34884;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 105.
DE   RecName: Full=Macrophage migration inhibitory factor;
DE            Short=MIF;
DE            EC=5.3.2.1;
DE   AltName: Full=Delayed early response protein 6;
DE            Short=DER6;
DE   AltName: Full=Glycosylation-inhibiting factor;
DE            Short=GIF;
DE   AltName: Full=L-dopachrome isomerase;
DE   AltName: Full=L-dopachrome tautomerase;
DE            EC=5.3.3.12;
DE   AltName: Full=Phenylpyruvate tautomerase;
GN   Name=Mif;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-28.
RC   TISSUE=Pituitary;
RX   MEDLINE=94019845; PubMed=8413654; DOI=10.1038/365756a0;
RA   Bernhagen J., Calandra T., Mitchell R.A., Martin S.B., Tracey K.J.,
RA   Voelter W., Manogue K.R., Cerami A., Bucala R.;
RT   "MIF is a pituitary-derived cytokine that potentiates lethal
RT   endotoxaemia.";
RL   Nature 365:756-759(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=92375060; PubMed=1508193;
RA   Lanahan A.A., Williams J.B., Sanders L.K., Nathans D.;
RT   "Growth factor-induced delayed early response genes.";
RL   Mol. Cell. Biol. 12:3919-3929(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBSCELLULAR LOCATION.
RX   MEDLINE=94052102; PubMed=8234256; DOI=10.1073/pnas.90.21.10056;
RA   Mikayama T., Nakano T., Gomi H., Nakagawa Y., Liu Y.C., Iwamatsu A.,
RA   Weiser W.Y., Ishizaka K., Sato M., Ishii Y.;
RT   "Molecular cloning and functional expression of a cDNA encoding
RT   glycosylation-inhibiting factor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:10056-10060(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=95221891; PubMed=7706726;
RA   Mitchell R., Bacher M., Bernhagen J., Pushkarskaya T., Seldin M.F.,
RA   Bucala R.;
RT   "Cloning and characterization of the gene for mouse macrophage
RT   migration inhibitory factor (MIF).";
RL   J. Immunol. 154:3863-3870(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=96047325; PubMed=7558021; DOI=10.1006/geno.1995.1071;
RA   Bozza M., Kolakowski L.F. Jr., Jenkins N.A., Gilbert D.J.,
RA   Copeland N.G., David J.R., Gerard C.;
RT   "Structural characterization and chromosomal location of the mouse
RT   macrophage migration inhibitory factor gene and pseudogenes.";
RL   Genomics 27:412-419(1995).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=96047324; PubMed=7558020; DOI=10.1006/geno.1995.1070;
RA   Kozak C.A., Adamson M.C., Buckler C.E., Segovia L., Paralkar V.,
RA   Wistow G.;
RT   "Genomic cloning of mouse MIF (macrophage inhibitory factor) and
RT   genetic mapping of the human and mouse expressed gene and nine mouse
RT   pseudogenes.";
RL   Genomics 27:405-411(1995).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   PROTEIN SEQUENCE OF 2-12, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-115.
RC   TISSUE=Lens;
RX   MEDLINE=93165679; PubMed=7679497; DOI=10.1073/pnas.90.4.1272;
RA   Wistow G.J., Shaughnessy M., Lee D.C., Hodin J., Zelenka P.S.;
RT   "A macrophage migration inhibitory factor is expressed in the
RT   differentiating cells of the eye lens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:1272-1275(1993).
RN   [10]
RP   CHARACTERIZATION.
RX   MEDLINE=95034860; PubMed=7947826; DOI=10.1021/bi00251a025;
RA   Bernhagen J., Mitchell R.A., Calandra T., Voelter W., Cerami A.,
RA   Bucala R.;
RT   "Purification, bioactivity, and secondary structure analysis of mouse
RT   and human macrophage migration inhibitory factor (MIF).";
RL   Biochemistry 33:14144-14155(1994).
RN   [11]
RP   SUBCELLULAR LOCATION, AND ROLE OF TAUTOMERASE INHIBITORS IN IMPROVED
RP   SURVIVAL IN CASE OF SEPSIS.
RX   PubMed=17526494; DOI=10.1074/jbc.M701825200;
RA   Crichlow G.V., Cheng K.F., Dabideen D., Ochani M., Aljabari B.,
RA   Pavlov V.A., Miller E.J., Lolis E., Al-Abed Y.;
RT   "Alternative chemical modifications reverse the binding orientation of
RT   a pharmacophore scaffold in the active site of macrophage migration
RT   inhibitory factor.";
RL   J. Biol. Chem. 282:23089-23095(2007).
RN   [12]
RP   INTERACTION WITH CD74; CXCR2 AND COPS5, CATALYTIC ACTIVITY, AND
RP   MUTAGENESIS OF PRO-2.
RX   PubMed=19188446; DOI=10.1128/MCB.01907-08;
RA   Fingerle-Rowson G., Kaleswarapu D.R., Schlander C., Kabgani N.,
RA   Brocks T., Reinart N., Busch R., Schuetz A., Lue H., Du X., Liu A.,
RA   Xiong H., Chen Y., Nemajerova A., Hallek M., Bernhagen J., Leng L.,
RA   Bucala R.;
RT   "A tautomerase-null macrophage migration-inhibitory factor (MIF) gene
RT   knock-in mouse model reveals that protein interactions and not
RT   enzymatic activity mediate MIF-dependent growth regulation.";
RL   Mol. Cell. Biol. 29:1922-1932(2009).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   MEDLINE=99303983; PubMed=10360941; DOI=10.1021/bi9904048;
RA   Taylor A.B., Johnson W.H. Jr., Czerwinski R.M., Li H.S., Hackert M.L.,
RA   Whitman C.P.;
RT   "Crystal structure of macrophage migration inhibitory factor complexed
RT   with (E)-2-fluoro-p-hydroxycinnamate at 1.8 A resolution: implications
RT   for enzymatic catalysis and inhibition.";
RL   Biochemistry 38:7444-7452(1999).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), TAUTOMERASE ACTIVITY, MASS
RP   SPECTROMETRY, REMOVAL OF MET-1, AND MUTAGENESIS OF PRO-2.
RX   MEDLINE=20393856; PubMed=10933783; DOI=10.1021/bi000373c;
RA   Stamps S.L., Taylor A.B., Wang S.C., Hackert M.L., Whitman C.P.;
RT   "Mechanism of the phenylpyruvate tautomerase activity of macrophage
RT   migration inhibitory factor: properties of the P1G, P1A, Y95F, and
RT   N97A mutants.";
RL   Biochemistry 39:9671-9678(2000).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH INHIBITOR,
RP   TAUTOMERASE ACTIVITY, MASS SPECTROMETRY, AND SUBUNIT.
RX   PubMed=16780921; DOI=10.1016/j.bioorg.2006.05.001;
RA   Golubkov P.A., Johnson W.H. Jr., Czerwinski R.M., Person M.D.,
RA   Wang S.C., Whitman C.P., Hackert M.L.;
RT   "Inactivation of the phenylpyruvate tautomerase activity of macrophage
RT   migration inhibitory factor by 2-oxo-4-phenyl-3-butynoate.";
RL   Bioorg. Chem. 34:183-199(2006).
CC   -!- FUNCTION: Pro-inflammatory cytokine. Involved in the innate immune
CC       response to bacterial pathogens. The expression of MIF at sites of
CC       inflammation suggests a role as mediator in regulating the
CC       function of macrophages in host defense. Counteracts the anti-
CC       inflammatory activity of glucocorticoids. Has phenylpyruvate
CC       tautomerase and dopachrome tautomerase activity (in vitro), but
CC       the physiological substrate is not known. It is not clear whether
CC       the tautomerase activity has any physiological relevance, and
CC       whether it is important for cytokine activity (By similarity).
CC   -!- CATALYTIC ACTIVITY: Keto-phenylpyruvate = enol-phenylpyruvate.
CC   -!- CATALYTIC ACTIVITY: L-dopachrome = 5,6-dihydroxyindole-2-
CC       carboxylate.
CC   -!- SUBUNIT: Homotrimer. Interacts with BNIPL (By similarity).
CC       Interacts with the CD74 extracellular domain. Interacts with COPS5
CC       and with the CXCR2 extracellular domain.
CC   -!- SUBCELLULAR LOCATION: Secreted. Cytoplasm (By similarity).
CC       Note=Does not have a cleavable signal sequence and is secreted via
CC       a specialized, non-classical pathway. Secreted by macrophages upon
CC       stimulation by bacterial lipopolysaccharide (LPS), or by
CC       M.tuberculosis antigens (By similarity).
CC   -!- MISCELLANEOUS: MIF tautomerase inhibitors improve survival in case
CC       of sepsis.
CC   -!- SIMILARITY: Belongs to the MIF family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Z23048; CAA80583.1; -; mRNA.
DR   EMBL; U19825; AAA91637.1; -; Genomic_DNA.
DR   EMBL; L10613; AAA37693.1; -; mRNA.
DR   EMBL; U20156; AAA91638.1; -; Genomic_DNA.
DR   EMBL; L39357; AAA74321.1; -; Genomic_DNA.
DR   EMBL; BC024895; AAH24895.1; -; mRNA.
DR   EMBL; BC086928; AAH86928.1; -; mRNA.
DR   EMBL; L07607; AAA37111.1; -; mRNA.
DR   IPI; IPI00230427; -.
DR   PIR; A44499; A44499.
DR   RefSeq; NP_034928.1; NM_010798.2.
DR   UniGene; Mm.2326; -.
DR   PDB; 1MFF; X-ray; 2.00 A; A/B/C=2-115.
DR   PDB; 1MFI; X-ray; 1.80 A; A/B/C=2-115.
DR   PDB; 2GDG; X-ray; 1.45 A; A/B/C=2-114.
DR   PDBsum; 1MFF; -.
DR   PDBsum; 1MFI; -.
DR   PDBsum; 2GDG; -.
DR   ProteinModelPortal; P34884; -.
DR   SMR; P34884; 2-115.
DR   STRING; P34884; -.
DR   PhosphoSite; P34884; -.
DR   PRIDE; P34884; -.
DR   Ensembl; ENSMUST00000038169; ENSMUSP00000041149; ENSMUSG00000033307.
DR   GeneID; 17319; -.
DR   KEGG; mmu:17319; -.
DR   UCSC; uc007ftc.1; mouse.
DR   CTD; 17319; -.
DR   MGI; MGI:96982; Mif.
DR   eggNOG; roNOG16810; -.
DR   HOGENOM; HBG629499; -.
DR   HOVERGEN; HBG003240; -.
DR   InParanoid; P34884; -.
DR   OMA; FVVNTNV; -.
DR   OrthoDB; EOG49GKJ5; -.
DR   PhylomeDB; P34884; -.
DR   BRENDA; 5.3.2.1; 244.
DR   NextBio; 291888; -.
DR   ArrayExpress; P34884; -.
DR   Bgee; P34884; -.
DR   CleanEx; MM_MIF; -.
DR   Genevestigator; P34884; -.
DR   GermOnline; ENSMUSG00000033307; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR   GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL.
DR   GO; GO:0004167; F:dopachrome isomerase activity; ISS:UniProtKB.
DR   GO; GO:0050178; F:phenylpyruvate tautomerase activity; IEA:EC.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0032269; P:negative regulation of cellular protein metabolic process; IDA:BHF-UCL.
DR   GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IDA:BHF-UCL.
DR   GO; GO:0033033; P:negative regulation of myeloid cell apoptosis; IMP:BHF-UCL.
DR   GO; GO:0090238; P:positive regulation of arachidonic acid secretion; IDA:BHF-UCL.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:BHF-UCL.
DR   GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:BHF-UCL.
DR   GO; GO:0061081; P:positive regulation of myeloid leukocyte cytokine production involved in immune response; IMP:BHF-UCL.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
DR   GO; GO:0061078; P:positive regulation of prostaglandin secretion involved in immune response; IMP:BHF-UCL.
DR   InterPro; IPR001398; Macrophage_inhib_fac.
DR   InterPro; IPR019829; Macrophage_inhib_fac_CS.
DR   InterPro; IPR014347; Tautomerase.
DR   Gene3D; G3DSA:3.30.429.10; Tautomerase; 1.
DR   PANTHER; PTHR11954; MIF; 1.
DR   Pfam; PF01187; MIF; 1.
DR   ProDom; PD004816; Macrophage_inhib_fac; 1.
DR   PROSITE; PS01158; MIF; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytokine; Cytoplasm;
KW   Direct protein sequencing; Immunity; Inflammatory response;
KW   Innate immunity; Isomerase; Phosphoprotein; Secreted.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    115       Macrophage migration inhibitory factor.
FT                                /FTId=PRO_0000158066.
FT   ACT_SITE      2      2       Proton acceptor; via imino nitrogen.
FT   BINDING      33     33       Substrate.
FT   BINDING      65     65       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING      98     98       Substrate.
FT   MOD_RES      37     37       Phosphotyrosine (By similarity).
FT   MOD_RES      78     78       N6-acetyllysine (By similarity).
FT   MUTAGEN       2      2       P->G: Loss of tautomerase activity,
FT                                reduced activation of intracellular
FT                                signaling pathways, and reduced
FT                                interaction with CXCR2 and COPS5.
FT   STRAND        3     10
FT   HELIX        12     14
FT   HELIX        19     31
FT   HELIX        35     37
FT   STRAND       39     43
FT   STRAND       47     50
FT   STRAND       58     66
FT   HELIX        70     88
FT   HELIX        92     94
FT   STRAND       95    101
FT   HELIX       104    106
FT   STRAND      107    109
SQ   SEQUENCE   115 AA;  12504 MW;  92D207B81B149945 CRC64;
     MPMFIVNTNV PRASVPEGFL SELTQQLAQA TGKPAQYIAV HVVPDQLMTF SGTNDPCALC
     SLHSIGKIGG AQNRNYSKLL CGLLSDRLHI SPDRVYINYY DMNAANVGWN GSTFA
//
ID   ADRB1_MOUSE             Reviewed;         466 AA.
AC   P34971;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Beta-1 adrenergic receptor;
DE   AltName: Full=Beta-1 adrenoreceptor;
DE            Short=Beta-1 adrenoceptor;
GN   Name=Adrb1; Synonyms=Adrb1r;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=93372116; PubMed=8395893; DOI=10.1016/0167-4889(93)90209-8;
RA   Jasper J.R., Link R.E., Chruscinski A.J., Kobilka B.K., Bernstein D.;
RT   "Primary structure of the mouse beta 1-adrenergic receptor gene.";
RL   Biochim. Biophys. Acta 1178:307-309(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 303-307, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: Beta-adrenergic receptors mediate the catecholamine-
CC       induced activation of adenylate cyclase through the action of G
CC       proteins. This receptor binds epinephrine and norepinephrine with
CC       approximately equal affinity.
CC   -!- SUBUNIT: Interacts with GOPC, MAGI3 and DLG4 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity). Note=Localized at the plasma membrane. Found in
CC       the Golgi upon GOPC overexpression (By similarity).
CC   -!- DOMAIN: The PDZ domain-binding motif mediates competitive
CC       interactions with GOPC, MAGI3 and DLG4 and plays a role in
CC       subcellular location of the receptor (By similarity).
CC   -!- PTM: Homologous desensitization of the receptor is mediated by its
CC       phosphorylation by beta-adrenergic receptor kinase.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Adrenergic receptor subfamily. ADRB1 sub-subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; L10084; AAA02929.1; -; Genomic_DNA.
DR   IPI; IPI00119827; -.
DR   PIR; S36794; S36794.
DR   UniGene; Mm.46797; -.
DR   ProteinModelPortal; P34971; -.
DR   SMR; P34971; 56-380.
DR   STRING; P34971; -.
DR   PhosphoSite; P34971; -.
DR   PRIDE; P34971; -.
DR   Ensembl; ENSMUST00000038949; ENSMUSP00000040847; ENSMUSG00000035283.
DR   UCSC; uc008hze.1; mouse.
DR   MGI; MGI:87937; Adrb1.
DR   eggNOG; maNOG04780; -.
DR   HOGENOM; HBG445348; -.
DR   HOVERGEN; HBG106962; -.
DR   InParanoid; P34971; -.
DR   OrthoDB; EOG4WQ12W; -.
DR   ArrayExpress; P34971; -.
DR   Bgee; P34971; -.
DR   CleanEx; MM_ADRB1; -.
DR   Genevestigator; P34971; -.
DR   GermOnline; ENSMUSG00000035283; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004940; F:beta1-adrenergic receptor activity; IDA:MGI.
DR   GO; GO:0007189; P:activation of adenylate cyclase activity by G-protein signaling pathway; IMP:MGI.
DR   GO; GO:0050873; P:brown fat cell differentiation; IGI:MGI.
DR   GO; GO:0002024; P:diet induced thermogenesis; IGI:MGI.
DR   GO; GO:0042596; P:fear response; IMP:MGI.
DR   GO; GO:0031649; P:heat generation; IGI:MGI.
DR   GO; GO:0040015; P:negative regulation of multicellular organism growth; IGI:MGI.
DR   GO; GO:0001996; P:positive regulation of heart rate by epinephrine-norepinephrine; IMP:MGI.
DR   GO; GO:0001997; P:positive regulation of the force of heart contraction by epinephrine-norepinephrine; IDA:MGI.
DR   GO; GO:0009409; P:response to cold; IGI:MGI.
DR   GO; GO:0002025; P:vasodilation by norepinephrine-epinephrine involved in regulation of systemic arterial blood pressure; IGI:MGI.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR000507; Adrgc_rcpt_B1.
DR   InterPro; IPR002233; Adrnrgc_rcpt.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01103; ADRENERGICR.
DR   PRINTS; PR00561; ADRENRGCB1AR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
KW   Palmitate; Phosphoprotein; Receptor; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    466       Beta-1 adrenergic receptor.
FT                                /FTId=PRO_0000069122.
FT   TOPO_DOM      1     55       Extracellular (By similarity).
FT   TRANSMEM     56     84       Helical; Name=1; (By similarity).
FT   TOPO_DOM     85     93       Cytoplasmic (By similarity).
FT   TRANSMEM     94    120       Helical; Name=2; (By similarity).
FT   TOPO_DOM    121    132       Extracellular (By similarity).
FT   TRANSMEM    133    154       Helical; Name=3; (By similarity).
FT   TOPO_DOM    155    172       Cytoplasmic (By similarity).
FT   TRANSMEM    173    196       Helical; Name=4; (By similarity).
FT   TOPO_DOM    197    222       Extracellular (By similarity).
FT   TRANSMEM    223    248       Helical; Name=5; (By similarity).
FT   TOPO_DOM    249    308       Cytoplasmic (By similarity).
FT   TRANSMEM    309    338       Helical; Name=6; (By similarity).
FT   TOPO_DOM    339    343       Extracellular (By similarity).
FT   TRANSMEM    344    366       Helical; Name=7; (By similarity).
FT   TOPO_DOM    367    466       Cytoplasmic (By similarity).
FT   REGION      218    232       Agonist and antagonist binding (By
FT                                similarity).
FT   REGION      326    333       Agonist and antagonist binding (By
FT                                similarity).
FT   REGION      352    356       Agonist and antagonist binding (By
FT                                similarity).
FT   MOTIF       463    466       PDZ-Binding (By similarity).
FT   BINDING     138    138       Agonist or antagonist (By similarity).
FT   BINDING     143    143       Agonist or antagonist (By similarity).
FT   MOD_RES     296    296       Phosphoserine; by PKA (Potential).
FT   MOD_RES     301    301       Phosphoserine; by PKA (Potential).
FT   MOD_RES     401    401       Phosphoserine; by PKA (Potential).
FT   LIPID       381    381       S-palmitoyl cysteine (By similarity).
FT   CARBOHYD     15     15       N-linked (GlcNAc...) (Probable).
FT   DISULFID    131    216       By similarity.
FT   DISULFID    209    215       By similarity.
SQ   SEQUENCE   466 AA;  50480 MW;  753CD44C42BC9211 CRC64;
     MGAGALALGA SEPCNLSSAA PLPDGAATAA RLLVLASPPA SLLPPASEGS APLSQQWTAG
     MGLLVALIVL LIVVGNVLVI VAIAKTPRLQ TLTNLFIMSL ASADLVMGLL VVPFGATIVV
     WGRWEYGSFF CELWTSVDVL CVTASIETLC VIALDRYLAI TSPFRYQSLL TRARARALVC
     TVWAISALVS FLPILMHWWR AESDEARRCY NDPKCCDFVT NRAYAIASSV VSFYVPLCIM
     AFVYLRVFRE AQKQVKKIDS CERRFLGGPA RPPSPEPSPS PGPPRPADSL ANGRSSKRRP
     SRLVALREQK ALKTLGIIMG VFTLCWLPFF LANVVKAFHR DLVPDRLFVF FNWLGYANSA
     FNPIIYCRSP DFRKAFQRLL CCARRAACRR RAAHGDRPRA SGCLARAGPP PSPGAPSDDD
     DDDAGTTPPA RLLEPWTGCN GGTTTVDSDS SLDEPGRQGF SSESKV
//
ID   PTN11_MOUSE             Reviewed;         597 AA.
AC   P35235; Q3TQ84; Q64509; Q6PCL5;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   08-MAR-2011, entry version 124.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type 11;
DE            EC=3.1.3.48;
DE   AltName: Full=Protein-tyrosine phosphatase SYP;
DE   AltName: Full=SH-PTP2;
DE            Short=SHP-2;
DE            Short=Shp2;
GN   Name=Ptpn11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=96411777; PubMed=8810330; DOI=10.1074/jbc.271.41.25569;
RA   Ohnishi H., Kubota M., Ohtake A., Sato K., Sano S.;
RT   "Activation of protein-tyrosine phosphatase SH-PTP2 by a tyrosine-
RT   based activation motif of a novel brain molecule.";
RL   J. Biol. Chem. 271:25569-25574(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-552 (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   MEDLINE=93206094; PubMed=8096088; DOI=10.1126/science.8096088;
RA   Feng G.-S., Hui C.-C., Pawson T.;
RT   "SH2-containing phosphotyrosine phosphatase as a target of protein-
RT   tyrosine kinases.";
RL   Science 259:1607-1611(1993).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=93206095; PubMed=7681217; DOI=10.1126/science.7681217;
RA   Vogel W., Lammers R., Huang J., Ullrich A.;
RT   "Activation of a phosphotyrosine phosphatase by tyrosine
RT   phosphorylation.";
RL   Science 259:1611-1614(1993).
RN   [6]
RP   INTERACTION WITH INPP5D.
RX   PubMed=9110989; DOI=10.1074/jbc.272.17.10998;
RA   Liu L., Damen J.E., Ware M.D., Krystal G.;
RT   "Interleukin-3 induces the association of the inositol 5-phosphatase
RT   SHIP with SHP2.";
RL   J. Biol. Chem. 272:10998-11001(1997).
RN   [7]
RP   INTERACTION WITH PTPNS1.
RX   MEDLINE=97215901; PubMed=9062191; DOI=10.1038/386181a0;
RA   Kharitonenkov A., Chen Z., Sures I., Wang H., Schilling J.,
RA   Ullrich A.;
RT   "A family of proteins that inhibit signalling through tyrosine kinase
RT   receptors.";
RL   Nature 386:181-186(1997).
RN   [8]
RP   INTERACTION WITH INPP5D.
RX   PubMed=9393882; DOI=10.1038/sj.onc.1201422;
RA   Sattler M., Salgia R., Shrikhande G., Verma S., Choi J.-L.,
RA   Rohrschneider L.R., Griffin J.D.;
RT   "The phosphatidylinositol polyphosphate 5-phosphatase SHIP and the
RT   protein tyrosine phosphatase SHP-2 form a complex in hematopoietic
RT   cells which can be regulated by BCR/ABL and growth factors.";
RL   Oncogene 15:2379-2384(1997).
RN   [9]
RP   INTERACTION WITH GAB2.
RX   MEDLINE=99168966; PubMed=10068651;
RA   Nishida K., Yoshida Y., Itoh M., Fukada T., Ohtani T., Shirogane T.,
RA   Atsumi T., Takahashi-Tezuka M., Ishihara K., Hibi M., Hirano T.;
RT   "Gab-family adapter proteins act downstream of cytokine and growth
RT   factor receptors and T- and B-cell antigen receptors.";
RL   Blood 93:1809-1816(1999).
RN   [10]
RP   INTERACTION WITH BCAR3.
RX   PubMed=10896938; DOI=10.1074/jbc.M003074200;
RA   Gotoh T., Cai D., Tian X., Feig L.A., Lerner A.;
RT   "p130Cas regulates the activity of AND-34, a novel Ral, Rap1, and R-
RT   Ras guanine nucleotide exchange factor.";
RL   J. Biol. Chem. 275:30118-30123(2000).
RN   [11]
RP   INTERACTION WITH SHB.
RX   PubMed=12181353; DOI=10.1091/mbc.E02-02-0103;
RA   Cross M.J., Lu L., Magnusson P., Nyqvist D., Holmqvist K., Welsh M.,
RA   Claesson-Welsh L.;
RT   "The Shb adaptor protein binds to tyrosine 766 in the FGFR-1 and
RT   regulates the Ras/MEK/MAPK pathway via FRS2 phosphorylation in
RT   endothelial cells.";
RL   Mol. Biol. Cell 13:2881-2893(2002).
RN   [12]
RP   INTERACTION WITH LIME1.
RX   PubMed=14610044; DOI=10.1084/jem.20030232;
RA   Hur E.M., Son M., Lee O.-H., Choi Y.B., Park C., Lee H., Yun Y.;
RT   "LIME, a novel transmembrane adaptor protein, associates with p56lck
RT   and mediates T cell activation.";
RL   J. Exp. Med. 198:1463-1473(2003).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-584, AND MASS
RP   SPECTROMETRY.
RX   MEDLINE=22426906; PubMed=12522270; DOI=10.1073/pnas.2436191100;
RA   Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,
RA   Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.;
RT   "Profiling of tyrosine phosphorylation pathways in human cells using
RT   mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
RN   [14]
RP   FUNCTION.
RX   PubMed=14967142; DOI=10.1016/S1097-2765(04)00050-4;
RA   Zhang S.Q., Yang W., Kontaridis M.I., Bivona T.G., Wen G., Araki T.,
RA   Luo J., Thompson J.A., Schraven B.L., Philips M.R., Neel B.G.;
RT   "Shp2 regulates SRC family kinase activity and Ras/Erk activation by
RT   controlling Csk recruitment.";
RL   Mol. Cell 13:341-355(2004).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-62, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-62 AND TYR-66, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 4-103.
RX   MEDLINE=94363243; PubMed=7521735; DOI=10.1016/S0969-2126(00)00044-7;
RA   Lee C.-H., Kominos D., Jacques S., Margolis B., Schlessinger J.,
RA   Shoelson S.E., Kuriyan J.;
RT   "Crystal structures of peptide complexes of the amino-terminal SH2
RT   domain of the Syp tyrosine phosphatase.";
RL   Structure 2:423-438(1994).
CC   -!- FUNCTION: Acts downstream of various receptor and cytoplasmic
CC       protein tyrosine kinases to participate in the signal transduction
CC       from the cell surface to the nucleus.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- SUBUNIT: Interacts with CD84 and with phosphorylated SIT1 and
CC       MZPL1. Interacts with FCRL3, FCRL4, FCRL6 and ANKHD1 (By
CC       similarity). Interacts with PTPNS1 and BCAR3. Interacts with
CC       phosphorylated LIME1. Interacts with SHB and INPP5D/SHIP1.
CC       Interacts with KIR2DL1; the interaction is enhanced by ARRB2 (By
CC       similarity). Interacts with GAB2. Interacts with TERT; the
CC       interaction retains TERT in the nucleus. Interacts with PECAM1 (By
CC       similarity).
CC   -!- INTERACTION:
CC       P62993:GRB2 (xeno); NbExp=1; IntAct=EBI-397236, EBI-401755;
CC       P10721:KIT (xeno); NbExp=2; IntAct=EBI-397236, EBI-1379503;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P35235-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P35235-2; Sequence=VSP_016675;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain, heart and kidney.
CC   -!- DOMAIN: The SH2 domains repress phosphatase activity. Binding of
CC       these domains to phosphotyrosine-containing proteins relieves this
CC       auto-inhibition, possibly by inducing a conformational change in
CC       the enzyme.
CC   -!- PTM: Phosphorylated on Tyr-546 and Tyr-584 upon receptor protein
CC       tyrosine kinase activation; which creates a binding site for GRB2
CC       and other SH2-containing proteins.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class 2 subfamily.
CC   -!- SIMILARITY: Contains 2 SH2 domains.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; D84372; BAA12328.1; -; mRNA.
DR   EMBL; AK159501; BAE35134.1; -; mRNA.
DR   EMBL; AK159587; BAE35207.1; -; mRNA.
DR   EMBL; AK163809; BAE37500.1; -; mRNA.
DR   EMBL; BC057398; AAH57398.1; -; mRNA.
DR   EMBL; BC059278; AAH59278.1; -; mRNA.
DR   EMBL; L08663; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00116554; -.
DR   IPI; IPI00316479; -.
DR   PIR; A46209; A46209.
DR   RefSeq; NP_001103462.1; NM_001109992.1.
DR   RefSeq; NP_035332.1; NM_011202.3.
DR   UniGene; Mm.474046; -.
DR   UniGene; Mm.8681; -.
DR   PDB; 1AYA; X-ray; 2.05 A; A/B=4-103.
DR   PDB; 1AYB; X-ray; 3.00 A; A=4-103.
DR   PDB; 1AYC; X-ray; 2.30 A; A=4-103.
DR   PDB; 1AYD; X-ray; 2.20 A; A=4-103.
DR   PDBsum; 1AYA; -.
DR   PDBsum; 1AYB; -.
DR   PDBsum; 1AYC; -.
DR   PDBsum; 1AYD; -.
DR   ProteinModelPortal; P35235; -.
DR   SMR; P35235; 3-532.
DR   DIP; DIP-29669N; -.
DR   IntAct; P35235; 16.
DR   MINT; MINT-4110032; -.
DR   STRING; P35235; -.
DR   PhosphoSite; P35235; -.
DR   PRIDE; P35235; -.
DR   Ensembl; ENSMUST00000054547; ENSMUSP00000058757; ENSMUSG00000043733.
DR   GeneID; 19247; -.
DR   KEGG; mmu:19247; -.
DR   UCSC; uc008zio.1; mouse.
DR   UCSC; uc008zip.1; mouse.
DR   CTD; 19247; -.
DR   MGI; MGI:99511; Ptpn11.
DR   eggNOG; roNOG04182; -.
DR   HOGENOM; HBG379880; -.
DR   HOVERGEN; HBG000223; -.
DR   InParanoid; P35235; -.
DR   OMA; HKQESIV; -.
DR   BRENDA; 3.1.3.48; 244.
DR   NextBio; 296074; -.
DR   ArrayExpress; P35235; -.
DR   Bgee; P35235; -.
DR   Genevestigator; P35235; -.
DR   GermOnline; ENSMUSG00000043733; Mus musculus.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0051428; F:peptide hormone receptor binding; IPI:MGI.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
DR   GO; GO:0000187; P:activation of MAPK activity; IMP:MGI.
DR   GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR   GO; GO:0000077; P:DNA damage checkpoint; IMP:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0042445; P:hormone metabolic process; IMP:MGI.
DR   GO; GO:0009755; P:hormone-mediated signaling pathway; IDA:MGI.
DR   GO; GO:0048609; P:multicellular organismal reproductive process; IMP:MGI.
DR   GO; GO:0051463; P:negative regulation of cortisol secretion; IMP:MGI.
DR   GO; GO:0060125; P:negative regulation of growth hormone secretion; IMP:MGI.
DR   GO; GO:0046676; P:negative regulation of insulin secretion; IMP:MGI.
DR   GO; GO:0048011; P:nerve growth factor receptor signaling pathway; IMP:MGI.
DR   GO; GO:0035265; P:organ growth; IMP:MGI.
DR   GO; GO:0046887; P:positive regulation of hormone secretion; IMP:MGI.
DR   GO; GO:0009967; P:positive regulation of signal transduction; IMP:MGI.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
DR   GO; GO:0046825; P:regulation of protein export from nucleus; IMP:MGI.
DR   GO; GO:0006641; P:triglyceride metabolic process; IMP:MGI.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR012152; Tyr_Pase_non-rcpt_typ-6/11.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 2.
DR   Pfam; PF00017; SH2; 2.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PIRSF; PIRSF000929; Tyr-Ptase_nr_6; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00252; SH2; 2.
DR   PROSITE; PS50001; SH2; 2.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm; Hydrolase;
KW   Phosphoprotein; Protein phosphatase; Repeat; SH2 domain.
FT   CHAIN         1    597       Tyrosine-protein phosphatase non-receptor
FT                                type 11.
FT                                /FTId=PRO_0000094768.
FT   DOMAIN        6    102       SH2 1.
FT   DOMAIN      112    216       SH2 2.
FT   DOMAIN      247    525       Tyrosine-protein phosphatase.
FT   REGION      463    469       Substrate binding (By similarity).
FT   ACT_SITE    463    463       Phosphocysteine intermediate (By
FT                                similarity).
FT   BINDING     429    429       Substrate (By similarity).
FT   BINDING     510    510       Substrate (By similarity).
FT   MOD_RES      62     62       Phosphotyrosine.
FT   MOD_RES      63     63       Phosphotyrosine (By similarity).
FT   MOD_RES      66     66       Phosphotyrosine.
FT   MOD_RES     280    280       N6-acetyllysine (By similarity).
FT   MOD_RES     546    546       Phosphotyrosine (By similarity).
FT   MOD_RES     562    562       Phosphoserine (By similarity).
FT   MOD_RES     584    584       Phosphotyrosine.
FT   MOD_RES     595    595       Phosphoserine (By similarity).
FT   VAR_SEQ     408    411       Missing (in isoform 2).
FT                                /FTId=VSP_016675.
FT   CONFLICT    390    390       E -> G (in Ref. 2; BAE37500).
FT   HELIX        13     22
FT   STRAND       28     33
FT   STRAND       35     37
FT   STRAND       41     47
FT   STRAND       50     55
FT   STRAND       63     68
FT   STRAND       71     73
FT   HELIX        74     83
SQ   SEQUENCE   597 AA;  68460 MW;  C742BED37E39EA23 CRC64;
     MTSRRWFHPN ITGVEAENLL LTRGVDGSFL ARPSKSNPGD FTLSVRRNGA VTHIKIQNTG
     DYYDLYGGEK FATLAELVQY YMEHHGQLKE KNGDVIELKY PLNCADPTSE RWFHGHLSGK
     EAEKLLTEKG KHGSFLVRES QSHPGDFVLS VRTGDDKGES NDGKSKVTHV MIRCQELKYD
     VGGGERFDSL TDLVEHYKKN PMVETLGTVL QLKQPLNTTR INAAEIESRV RELSKLAETT
     DKVKQGFWEE FETLQQQECK LLYSRKEGQR QENKNKNRYK NILPFDHTRV VLHDGDPNEP
     VSDYINANII MPEFETKCNN SKPKKSYIAT QGCLQNTVND FWRMVFQENS RVIVMTTKEV
     ERGKSKCVKY WPDEYALKEY GVMRVRNVKE SAAHDYTLRE LKLSKVGQAL LQGNTERTVW
     QYHFRTWPDH GVPSDPGGVL DFLEEVHHKQ ESIVDAGPVV VHCSAGIGRT GTFIVIDILI
     DIIREKGVDC DIDVPKTIQM VRSQRSGMVQ TEAQYRFIYM AVQHYIETLQ RRIEEEQKSK
     RKGHEYTNIK YSLVDQTSGD QSPLPPCTPT PPCAEMREDS ARVYENVGLM QQQRSFR
//
ID   RAB3D_MOUSE             Reviewed;         219 AA.
AC   P35276;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   08-MAR-2011, entry version 103.
DE   RecName: Full=Ras-related protein Rab-3D;
GN   Name=Rab3d;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92279263; PubMed=1594612; DOI=10.1073/pnas.89.11.5049;
RA   Baldini G., Hohl T., Lin H.Y., Lodish H.F.;
RT   "Cloning of a Rab3 isotype predominantly expressed in adipocytes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:5049-5052(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=20351194; PubMed=10891340; DOI=10.1006/bbrc.2000.3032;
RA   Adachi R., Nigam R., Tuvim M.J., DeMayo F., Dickey B.F.;
RT   "Genomic organization, chromosomal localization, and expression of the
RT   murine RAB3D gene.";
RL   Biochem. Biophys. Res. Commun. 273:877-883(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 25-35; 42-60; 73-83; 122-136 AND 179-186, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   INTERACTION WITH RIMS1.
RX   MEDLINE=21413899; PubMed=11431472; DOI=10.1074/jbc.M103337200;
RA   Wang X., Hu B., Zimmermann B., Kilimann M.W.;
RT   "Rim1 and rabphilin-3 bind Rab3-GTP by composite determinants
RT   partially related through N-terminal alpha-helix motifs.";
RL   J. Biol. Chem. 276:32480-32488(2001).
CC   -!- FUNCTION: Protein transport. Probably involved in vesicular
CC       traffic (By similarity). May be involved in the insulin-induced
CC       exocytosis of glut4-containing vesicles in adipocytes.
CC   -!- SUBUNIT: Binds RIMS1. Interacts with RAB3IP.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in the adipocyte
CC       tissue, but is also expressed in several other organs including
CC       skin, spleen, heart and lung.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR   EMBL; M89777; AAA40026.1; -; mRNA.
DR   EMBL; AF263365; AAF82769.1; -; mRNA.
DR   EMBL; AF263366; AAF82770.1; -; Genomic_DNA.
DR   EMBL; BC010779; AAH10779.1; -; mRNA.
DR   EMBL; BC020010; AAH20010.1; -; mRNA.
DR   IPI; IPI00116688; -.
DR   PIR; A45384; A45384.
DR   RefSeq; NP_114080.2; NM_031874.4.
DR   UniGene; Mm.260157; -.
DR   ProteinModelPortal; P35276; -.
DR   SMR; P35276; 20-189.
DR   STRING; P35276; -.
DR   PRIDE; P35276; -.
DR   Ensembl; ENSMUST00000115351; ENSMUSP00000111008; ENSMUSG00000019066.
DR   Ensembl; ENSMUST00000122211; ENSMUSP00000113322; ENSMUSG00000019066.
DR   GeneID; 19340; -.
DR   KEGG; mmu:19340; -.
DR   UCSC; uc009omu.1; mouse.
DR   CTD; 19340; -.
DR   MGI; MGI:97844; Rab3d.
DR   eggNOG; roNOG05031; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; P35276; -.
DR   OMA; YDIANQE; -.
DR   OrthoDB; EOG4TB4C6; -.
DR   PhylomeDB; P35276; -.
DR   NextBio; 296343; -.
DR   ArrayExpress; P35276; -.
DR   Bgee; P35276; -.
DR   CleanEx; MM_RAB3D; -.
DR   Genevestigator; P35276; -.
DR   GermOnline; ENSMUSG00000019066; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042588; C:zymogen granule; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0018125; P:peptidyl-cysteine methylation; IDA:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0017157; P:regulation of exocytosis; IDA:MGI.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Direct protein sequencing; Exocytosis;
KW   GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW   Prenylation; Protein transport; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    219       Ras-related protein Rab-3D.
FT                                /FTId=PRO_0000121089.
FT   NP_BIND      29     37       GTP (By similarity).
FT   NP_BIND      77     81       GTP (By similarity).
FT   NP_BIND     135    138       GTP (By similarity).
FT   NP_BIND     165    167       GTP (By similarity).
FT   MOTIF        51     59       Effector region (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     219    219       Cysteine methyl ester (By similarity).
FT   LIPID       217    217       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   LIPID       219    219       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   219 AA;  24416 MW;  438115B0B5710648 CRC64;
     MASASEPPAS PRDAADQNFD YMFKLLLIGN SSVGKTSFLF RYADDSFTPA FVSTVGIDFK
     VKTVYRHDKR IKLQIWDTAG QERYRTITTA YYRGAMGFLL MYDIANQESF TAVQDWATQI
     KTYSWDNAQV ILVGNKCDLE DERVVPAEDG RRLADDLGFE FFEASAKENI NVKQVFERLV
     DIICDKMNES LEPSSSPGSN GKGPALGDTP PPQPSSCSC
//
ID   RAB6A_MOUSE             Reviewed;         208 AA.
AC   P35279; Q542M6; Q8R2Z7; Q8VEE5; Q9JJD4;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   08-MAR-2011, entry version 113.
DE   RecName: Full=Ras-related protein Rab-6A;
DE            Short=Rab-6;
GN   Name=Rab6a; Synonyms=Rab6; ORFNames=MNCb-1660;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S.,
RA   Hashimoto K.;
RT   "Isolation of full-length cDNA clones from mouse brain cDNA library
RT   made by oligo-capping method.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Hippocampus, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-73 (ISOFORM 2).
RC   TISSUE=Kidney;
RX   MEDLINE=92210010; PubMed=1555775; DOI=10.1016/0378-1119(92)90387-5;
RA   Chavrier P., Simons K., Zerial M.;
RT   "The complexity of the Rab and Rho GTP-binding protein subfamilies
RT   revealed by a PCR cloning approach.";
RL   Gene 112:261-264(1992).
RN   [5]
RP   PROTEIN SEQUENCE OF 64-74 AND 144-158, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   MUTAGENESIS.
RX   MEDLINE=98101856; PubMed=9438855; DOI=10.1126/science.279.5350.580;
RA   Echard A., Jollivet F., Martinez O., Lacapere J.-J., Rousselet A.,
RA   Janoueix-Lerosey I., Goud B.;
RT   "Interaction of a Golgi-associated kinesin-like protein with Rab6.";
RL   Science 279:580-585(1998).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [8]
RP   INTERACTION WITH SCYL1BP1.
RX   PubMed=18997784; DOI=10.1038/ng.252;
RA   Hennies H.C., Kornak U., Zhang H., Egerer J., Zhang X., Seifert W.,
RA   Kuhnisch J., Budde B., Naetebus M., Brancati F., Wilcox W.R.,
RA   Mueller D., Kaplan P.B., Rajab A., Zampino G., Fodale V.,
RA   Dallapiccola B., Newman W., Metcalfe K., Clayton-Smith J.,
RA   Tassabehji M., Steinmann B., Barr F.A., Nuernberg P., Wieacker P.,
RA   Mundlos S.;
RT   "Gerodermia osteodysplastica is caused by mutations in SCYL1BP1, a
RT   Rab-6 interacting golgin.";
RL   Nat. Genet. 40:1410-1412(2008).
RN   [9]
RP   INTERACTION WITH CCDC64.
RX   PubMed=20360680; DOI=10.1038/emboj.2010.51;
RA   Schlager M.A., Kapitein L.C., Grigoriev I., Burzynski G.M., Wulf P.S.,
RA   Keijzer N., de Graaff E., Fukuda M., Shepherd I.T., Akhmanova A.,
RA   Hoogenraad C.C.;
RT   "Pericentrosomal targeting of Rab6 secretory vesicles by Bicaudal-D-
RT   related protein 1 (BICDR-1) regulates neuritogenesis.";
RL   EMBO J. 29:1637-1651(2010).
CC   -!- FUNCTION: Protein transport. Regulator of membrane traffic from
CC       the Golgi apparatus towards the endoplasmic reticulum (ER) (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with VSP52 and RABGAP1 (By similarity).
CC       Interacts with GCC2 (via its GRIP domain) (By similarity).
CC       Interacts with RAB6IP1 (via its RUN 1 domain) (By similarity).
CC       Interacts with RAB6KIFL (By similarity). Interacts with BICD1 (By
CC       similarity). Interacts with BICD2 (By similarity). Interacts with
CC       TMF1 (By similarity). Interacts (GTP-bound) with DYNLRB1; the
CC       interaction is direct (By similarity). Interacts with SCYL1BP1.
CC       Interacts with CCDC64; leads to its accumulation in the
CC       pericentrosomal region.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Lipid-anchor.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Rab-6a;
CC         IsoId=P35279-1; Sequence=Displayed;
CC       Name=2; Synonyms=Rab-6a', Rab6C;
CC         IsoId=P35279-2; Sequence=VSP_005528;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB041575; BAA95059.1; -; mRNA.
DR   EMBL; AK051246; BAC34572.1; -; mRNA.
DR   EMBL; AK083262; BAC38834.1; -; mRNA.
DR   EMBL; AK084131; BAC39121.1; -; mRNA.
DR   EMBL; AK160134; BAE35649.1; -; mRNA.
DR   EMBL; AK160866; BAE36058.1; -; mRNA.
DR   EMBL; AK169842; BAE41406.1; -; mRNA.
DR   EMBL; BC019118; AAH19118.1; -; mRNA.
DR   EMBL; BC026915; AAH26915.1; -; mRNA.
DR   EMBL; M79313; AAK14837.1; -; mRNA.
DR   IPI; IPI00116697; -.
DR   IPI; IPI00230011; -.
DR   PIR; A38883; A38883.
DR   RefSeq; NP_001157135.1; NM_001163663.1.
DR   RefSeq; NP_077249.1; NM_024287.4.
DR   UniGene; Mm.28650; -.
DR   ProteinModelPortal; P35279; -.
DR   SMR; P35279; 13-174.
DR   DIP; DIP-120N; -.
DR   STRING; P35279; -.
DR   PhosphoSite; P35279; -.
DR   PRIDE; P35279; -.
DR   Ensembl; ENSMUST00000032946; ENSMUSP00000032946; ENSMUSG00000030704.
DR   Ensembl; ENSMUST00000098252; ENSMUSP00000095852; ENSMUSG00000030704.
DR   GeneID; 19346; -.
DR   KEGG; mmu:19346; -.
DR   UCSC; uc009ini.1; mouse.
DR   CTD; 19346; -.
DR   MGI; MGI:894313; Rab6.
DR   eggNOG; roNOG11398; -.
DR   HOVERGEN; HBG009351; -.
DR   OMA; FKWIDEV; -.
DR   OrthoDB; EOG4NP74D; -.
DR   PhylomeDB; P35279; -.
DR   NextBio; 296365; -.
DR   ArrayExpress; P35279; -.
DR   Bgee; P35279; -.
DR   CleanEx; MM_RAB6; -.
DR   Genevestigator; P35279; -.
DR   GermOnline; ENSMUSG00000030704; Mus musculus.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0000042; P:protein targeting to Golgi; ISS:UniProtKB.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Direct protein sequencing;
KW   ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein;
KW   Membrane; Methylation; Nucleotide-binding; Phosphoprotein;
KW   Prenylation; Protein transport; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    208       Ras-related protein Rab-6A.
FT                                /FTId=PRO_0000121113.
FT   NP_BIND      20     28       GTP (By similarity).
FT   NP_BIND      68     72       GTP (By similarity).
FT   NP_BIND     126    129       GTP (By similarity).
FT   NP_BIND     156    158       GTP (By similarity).
FT   MOTIF        42     50       Effector region (By similarity).
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES     180    180       Phosphothreonine.
FT   MOD_RES     208    208       Cysteine methyl ester (By similarity).
FT   LIPID       206    206       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   LIPID       208    208       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   VAR_SEQ      62     88       VRLQLWDTAGQERFRSLIPSYIRDSTV -> IRLQLWDTAG
FT                                QERFRSLIPSYIRDSAA (in isoform 2).
FT                                /FTId=VSP_005528.
FT   MUTAGEN      22     22       Q->V: Loss of binding to rabkinesin-6.
FT   MUTAGEN      27     27       T->N: Loss of binding to rabkinesin-6;
FT                                when associated with L-73.
FT   MUTAGEN      46     46       I->E: Loss of binding to rabkinesin-6.
FT   MUTAGEN      72     72       Q->L: Loss of binding to rabkinesin-6;
FT                                when associated with N-28.
SQ   SEQUENCE   208 AA;  23590 MW;  DD08CC2914668FD4 CRC64;
     MSAGGDFGNP LRKFKLVFLG EQSVGKTSLI TRFMYDSFDN TYQATIGIDF LSKTMYLEDR
     TVRLQLWDTA GQERFRSLIP SYIRDSTVAV VVYDITNVNS FQQTTKWIDD VRTERGSDVI
     IMLVGNKTDL ADKRQVSIEE GERKAKELNV MFIETSAKAG YNVKQLFRRV AAALPGMEST
     QDRSREDMID IKLEKPQEQP VNEGGCSC
//
ID   RAB12_MOUSE             Reviewed;         243 AA.
AC   P35283; Q0PD43; Q9CUW7;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Ras-related protein Rab-12;
DE   AltName: Full=Rab-13;
GN   Name=Rab12;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16923123; DOI=10.1111/j.1365-2443.2006.00997.x;
RA   Itoh T., Satoh M., Kanno E., Fukuda M.;
RT   "Screening for target Rabs of TBC (Tre-2/Bub2/Cdc16) domain-containing
RT   proteins based on their Rab-binding activity.";
RL   Genes Cells 11:1023-1037(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 53-101.
RC   TISSUE=Kidney;
RX   MEDLINE=92210010; PubMed=1555775; DOI=10.1016/0378-1119(92)90387-5;
RA   Chavrier P., Simons K., Zerial M.;
RT   "The complexity of the Rab and Rho GTP-binding protein subfamilies
RT   revealed by a PCR cloning approach.";
RL   Gene 112:261-264(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 83-243.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-20 AND SER-105,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Lipid-anchor (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR   EMBL; AB232607; BAF02869.1; -; mRNA.
DR   EMBL; M79303; AAK14827.1; -; mRNA.
DR   EMBL; AK013690; BAB28956.1; -; mRNA.
DR   IPI; IPI00169699; -.
DR   PIR; JH0643; JH0643.
DR   RefSeq; NP_077768.2; NM_024448.2.
DR   UniGene; Mm.248313; -.
DR   ProteinModelPortal; P35283; -.
DR   SMR; P35283; 37-207.
DR   PhosphoSite; P35283; -.
DR   PRIDE; P35283; -.
DR   Ensembl; ENSMUST00000070538; ENSMUSP00000070134; ENSMUSG00000023460.
DR   GeneID; 19328; -.
DR   KEGG; mmu:19328; -.
DR   UCSC; uc008djy.1; mouse.
DR   CTD; 19328; -.
DR   MGI; MGI:894284; Rab12.
DR   GeneTree; ENSGT00550000074219; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; P35283; -.
DR   OrthoDB; EOG45757M; -.
DR   NextBio; 296297; -.
DR   ArrayExpress; P35283; -.
DR   Bgee; P35283; -.
DR   CleanEx; MM_RAB12; -.
DR   Genevestigator; P35283; -.
DR   GermOnline; ENSMUSG00000023460; Mus musculus.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW   Transport.
FT   CHAIN         1    243       Ras-related protein Rab-12.
FT                                /FTId=PRO_0000121180.
FT   NP_BIND      48     56       GTP (By similarity).
FT   NP_BIND      96    100       GTP (By similarity).
FT   NP_BIND     154    158       GTP (By similarity).
FT   NP_BIND     186    187       GTP (By similarity).
FT   MOTIF        70     78       Effector region (By similarity).
FT   MOD_RES      15     15       Phosphoserine.
FT   MOD_RES      20     20       Phosphoserine.
FT   MOD_RES      24     24       Phosphoserine (By similarity).
FT   MOD_RES     105    105       Phosphoserine.
FT   LIPID       242    242       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   LIPID       243    243       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   CONFLICT     83     83       V -> L (in Ref. 3; BAB28956).
FT   CONFLICT     86     86       R -> T (in Ref. 3; BAB28956).
FT   CONFLICT    184    185       AS -> PD (in Ref. 3; BAB28956).
SQ   SEQUENCE   243 AA;  27329 MW;  34E4EDC67F710510 CRC64;
     MDPSAALHRR PAGGSLGAVS PALSGGQARR RKQPPRPADF KLQVIIIGSR GVGKTSLMER
     FTDDTFCEAC KSTVGVDFKI KTVELRGKKI RLQIWDTAGQ ERFNSITSAY YRSAKGIILV
     YDITKKETFD DLPKWMKMID KYASEDAELL LVGNKLDCET DREISRQQGE KFAQQITGMR
     FCEASAKDNF NVDEIFLKLV DDILKKMPLD VLRNELSNSI LSLQPEPEIP PELPPPRPHV
     RCC
//
ID   RAB24_MOUSE             Reviewed;         203 AA.
AC   P35290;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   08-MAR-2011, entry version 105.
DE   RecName: Full=Ras-related protein Rab-24;
DE   AltName: Full=Rab-16;
GN   Name=Rab24;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   MEDLINE=94171934; PubMed=8126105;
RA   Olkkonen V.M., Dupree P., Killisch I., Luetcke A., Simons K.,
RA   Zerial M.;
RT   "Molecular cloning and subcellular localization of three GTP-binding
RT   proteins of the rab subfamily.";
RL   J. Cell Sci. 106:1249-1261(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-68.
RC   TISSUE=Kidney;
RX   MEDLINE=92210010; PubMed=1555775; DOI=10.1016/0378-1119(92)90387-5;
RA   Chavrier P., Simons K., Zerial M.;
RT   "The complexity of the Rab and Rho GTP-binding protein subfamilies
RT   revealed by a PCR cloning approach.";
RL   Gene 112:261-264(1992).
RN   [4]
RP   SUBCELLULAR LOCATION, INEFFICIENT ISOPRENYLATION, LACK OF INTERACTION
RP   WITH ARHGDIA AND ARHGDIB, AND MUTAGENESIS OF SER-67.
RX   PubMed=10660536; DOI=10.1074/jbc.275.6.3848;
RA   Erdman R.A., Shellenberger K.E., Overmeyer J.H., Maltese W.A.;
RT   "Rab24 is an atypical member of the Rab GTPase family. Deficient
RT   GTPase activity, GDP dissociation inhibitor interaction, and
RT   prenylation of Rab24 expressed in cultured cells.";
RL   J. Biol. Chem. 275:3848-3856(2000).
RN   [5]
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-22; THR-120 AND ASP-123.
RX   PubMed=12323076; DOI=10.1186/1471-2121-3-25;
RA   Maltese W.A., Soule G., Gunning W., Calomeni E., Alexander B.;
RT   "Mutant Rab24 GTPase is targeted to nuclear inclusions.";
RL   BMC Cell Biol. 3:25-25(2002).
CC   -!- FUNCTION: May be involved in autophagy-related processes.
CC   -!- SUBUNIT: Unlike other Rab family members, does not interact with
CC       GDP dissociation inhibitors (GDIs), including ARHGDIA and ARHGDIB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Membrane; Lipid-anchor.
CC       Note=Only about 20% is recovered in the particulate fraction.
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in
CC       brain.
CC   -!- PTM: Isoprenylation is inefficient compared to other Rab family
CC       members.
CC   -!- MISCELLANEOUS: The unusual Ser-67, instead of a conserved Gln in
CC       other family members, is the cause of low GTPase activity. As a
CC       result, the predominant nucleotide associated with the protein is
CC       GTP.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR   EMBL; Z22819; CAA80472.1; -; mRNA.
DR   EMBL; BC019950; AAH19950.1; -; mRNA.
DR   EMBL; BC054466; AAH54466.1; -; mRNA.
DR   EMBL; BC055894; AAH55894.1; -; mRNA.
DR   EMBL; M79306; AAK14830.1; -; mRNA.
DR   IPI; IPI00116760; -.
DR   PIR; JH0646; JH0646.
DR   PIR; S40235; S40235.
DR   RefSeq; NP_033026.1; NM_009000.3.
DR   UniGene; Mm.220923; -.
DR   ProteinModelPortal; P35290; -.
DR   SMR; P35290; 2-201.
DR   PhosphoSite; P35290; -.
DR   PRIDE; P35290; -.
DR   Ensembl; ENSMUST00000035242; ENSMUSP00000046188; ENSMUSG00000034789.
DR   GeneID; 19336; -.
DR   KEGG; mmu:19336; -.
DR   UCSC; uc007qqk.1; mouse.
DR   CTD; 19336; -.
DR   MGI; MGI:105065; Rab24.
DR   eggNOG; maNOG18834; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; P35290; -.
DR   OMA; FWVKELQ; -.
DR   OrthoDB; EOG469QVS; -.
DR   NextBio; 296327; -.
DR   ArrayExpress; P35290; -.
DR   Bgee; P35290; -.
DR   CleanEx; MM_RAB24; -.
DR   Genevestigator; P35290; -.
DR   GermOnline; ENSMUSG00000034789; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Autophagy; Cytoplasm; GTP-binding; Lipoprotein; Membrane;
KW   Nucleotide-binding; Prenylation; Protein transport; Transport.
FT   CHAIN         1    203       Ras-related protein Rab-24.
FT                                /FTId=PRO_0000121214.
FT   NP_BIND      14     22       GTP (By similarity).
FT   NP_BIND      63     67       GTP (By similarity).
FT   NP_BIND     120    123       GTP (By similarity).
FT   NP_BIND     154    156       GTP (By similarity).
FT   MOTIF        37     45       Effector region (By similarity).
FT   LIPID       200    200       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   LIPID       201    201       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   MUTAGEN      22     22       S->N: Predominantly in the GTP-bound
FT                                state. No effect on subcellular location.
FT   MUTAGEN      67     67       S->Q: Increase in GTPase activity. No
FT                                effect neither on prenylation, nor on
FT                                subcellular location.
FT   MUTAGEN     120    120       T->A,I: Accumulates in punctate
FT                                structures in both cytoplasmic and
FT                                nuclear compartments.
FT   MUTAGEN     123    123       D->I: Accumulates in punctate structures
FT                                in both cytoplasmic and nuclear
FT                                compartments. Disruptes the integrity of
FT                                the nuclear envelope.
FT   CONFLICT     67     67       S -> Q (in Ref. 3; AAK14830).
SQ   SEQUENCE   203 AA;  23144 MW;  872EA5E2E7B5B0F0 CRC64;
     MSGQRVDVKV VMLGKEYVGK TSLVERYVHD RFLVGPYQNT IGAAFVAKVM CVGDRTVTLG
     IWDTAGSERY EAMSRIYYRG AKAAIVCYDL TDSSSFERAK FWVKELRSLE EGCQIYLCGT
     KSDLLEEDRR RRRVDFHDVQ DYADNIKAQL FETSSKTGQS VDELFQKVAE DYVSVAAFQV
     MTEDKGVDLS QKANPYFYSC CHH
//
ID   CRFR1_MOUSE             Reviewed;         415 AA.
AC   P35347;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Corticotropin-releasing factor receptor 1;
DE            Short=CRF-R-1;
DE            Short=CRF-R1;
DE            Short=CRFR-1;
DE   AltName: Full=Corticotropin-releasing hormone receptor 1;
DE            Short=CRH-R-1;
DE            Short=CRH-R1;
DE   Flags: Precursor;
GN   Name=Crhr1; Synonyms=Crhr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pituitary;
RX   MEDLINE=94063063; PubMed=8243652; DOI=10.1016/0014-5793(93)80427-V;
RA   Vita N., Laurent P., Lefort S., Chalon P., Lelias J.-M., Kaghad M.,
RA   le Fur G., Caput D., Ferrara P.;
RT   "Primary structure and functional expression of mouse pituitary and
RT   human brain corticotrophin releasing factor receptors.";
RL   FEBS Lett. 335:1-5(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ILS, and ISS;
RX   MEDLINE=21363810; PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
CC   -!- FUNCTION: This is a receptor for corticotropin releasing factor.
CC       Shows high-affinity CRF binding. The activity of this receptor is
CC       mediated by G proteins which activate adenylyl cyclase.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Brain, pituitary gland, testis. Not detected
CC       in placenta, peripheral blood, lymphocytes, kidney and liver.
CC   -!- PTM: C-terminal Ser or Thr residues may be phosphorylated.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
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DR   EMBL; X72305; CAA51053.1; -; mRNA.
DR   EMBL; AF483484; AAL90758.1; -; mRNA.
DR   EMBL; AF483485; AAL90759.1; -; mRNA.
DR   IPI; IPI00117450; -.
DR   PIR; S39535; S39535.
DR   RefSeq; NP_031788.1; NM_007762.4.
DR   UniGene; Mm.1892; -.
DR   ProteinModelPortal; P35347; -.
DR   SMR; P35347; 24-108.
DR   STRING; P35347; -.
DR   PhosphoSite; P35347; -.
DR   PRIDE; P35347; -.
DR   Ensembl; ENSMUST00000093925; ENSMUSP00000091455; ENSMUSG00000018634.
DR   GeneID; 12921; -.
DR   KEGG; mmu:12921; -.
DR   UCSC; uc007lvz.1; mouse.
DR   CTD; 12921; -.
DR   MGI; MGI:88498; Crhr1.
DR   eggNOG; roNOG08744; -.
DR   HOGENOM; HBG713881; -.
DR   HOVERGEN; HBG106921; -.
DR   InParanoid; P35347; -.
DR   OMA; SPEVHQS; -.
DR   OrthoDB; EOG4DBTDQ; -.
DR   NextBio; 282572; -.
DR   ArrayExpress; P35347; -.
DR   Bgee; P35347; -.
DR   CleanEx; MM_CRHR1; -.
DR   Genevestigator; P35347; -.
DR   GermOnline; ENSMUSG00000018634; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015056; F:corticotrophin-releasing factor receptor activity; IMP:MGI.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR003052; GPCR_2_CRF1_rcpt.
DR   InterPro; IPR003051; GPCR_2_CRF_rcpt.
DR   InterPro; IPR001879; GPCR_2_extracellular_dom.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR   PANTHER; PTHR12011:SF73; CRF_rcpt; 1.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF02793; HRM; 1.
DR   PRINTS; PR01279; CRFRECEPTOR.
DR   PRINTS; PR01280; CRFRECEPTOR1.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   SMART; SM00008; HormR; 1.
DR   PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1.
DR   PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR   PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Phosphoprotein; Receptor; Signal; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     23       Potential.
FT   CHAIN        24    415       Corticotropin-releasing factor receptor
FT                                1.
FT                                /FTId=PRO_0000012815.
FT   TOPO_DOM     24    121       Extracellular (Potential).
FT   TRANSMEM    122    142       Helical; Name=1; (Potential).
FT   TOPO_DOM    143    151       Cytoplasmic (Potential).
FT   TRANSMEM    152    171       Helical; Name=2; (Potential).
FT   TOPO_DOM    172    189       Extracellular (Potential).
FT   TRANSMEM    190    213       Helical; Name=3; (Potential).
FT   TOPO_DOM    214    227       Cytoplasmic (Potential).
FT   TRANSMEM    228    249       Helical; Name=4; (Potential).
FT   TOPO_DOM    250    268       Extracellular (Potential).
FT   TRANSMEM    269    291       Helical; Name=5; (Potential).
FT   TOPO_DOM    292    314       Cytoplasmic (Potential).
FT   TRANSMEM    315    334       Helical; Name=6; (Potential).
FT   TOPO_DOM    335    349       Extracellular (Potential).
FT   TRANSMEM    350    369       Helical; Name=7; (Potential).
FT   TOPO_DOM    370    415       Cytoplasmic (Potential).
FT   CARBOHYD     38     38       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     45     45       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     78     78       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     90     90       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     98     98       N-linked (GlcNAc...) (Potential).
FT   DISULFID     30     54       By similarity.
FT   DISULFID     44     87       By similarity.
FT   DISULFID     68    102       By similarity.
SQ   SEQUENCE   415 AA;  47769 MW;  81423BDA6D1CA070 CRC64;
     MGQRPQLRLV KALLLLGLNP VSTSLQDQQC ESLSLASNVS GLQCNASVDL IGTCWPRSPA
     GQLVVRPCPA FFYGVRYNTT NNGYRECLAN GSWAARVNYS ECQEILNEEK KSKVHYHIAV
     IINYLGHCIS LVALLVAFVL FLRLRSIRCL RNIIHWNLIS AFILRNATWF VVQLTVSPEV
     HQSNVAWCRL VTAAYNYFHV TNFFWMFGEG CYLHTAIVLT YSTDRLRKWM FVCIGWGVPF
     PIIVAWAIGK LYYDNEKCWF GKRPGVYTDY IYQGPMILVL LINFIFLFNI VRILMTKLRA
     STTSETIQYR KAVKATLVLL PLLGITYMLF FVNPGEDEVS RVVFIYFNSF LESFQGFFVS
     VFYCFLNSEV RSAIRKRWRR WQDKHSIRAR VARAMSIPTS PTRVSFHSIK QSTAV
//
ID   5HT2A_MOUSE             Reviewed;         471 AA.
AC   P35363;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=5-hydroxytryptamine receptor 2A;
DE            Short=5-HT-2;
DE            Short=5-HT-2A;
DE   AltName: Full=Serotonin receptor 2A;
GN   Name=Htr2a; Synonyms=Htr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=93085774; PubMed=1333538; DOI=10.1002/jnr.490330203;
RA   Yang W., Chen K., Lan N.C., Gallaher T.K., Shih J.C.;
RT   "Gene structure and expression of the mouse 5-HT2 receptor.";
RL   J. Neurosci. Res. 33:196-204(1992).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=14988405; DOI=10.1074/jbc.M312106200;
RA   Becamel C., Gavarini S., Chanrion B., Alonso G., Galeotti N.,
RA   Dumuis A., Bockaert J., Marin P.;
RT   "The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets
RT   of PDZ proteins.";
RL   J. Biol. Chem. 279:20257-20266(2004).
CC   -!- FUNCTION: This is one of the several different receptors for 5-
CC       hydroxytryptamine (serotonin), a biogenic hormone that functions
CC       as a neurotransmitter, a hormone, and a mitogen. This receptor
CC       mediates its action by association with G proteins that activate a
CC       phosphatidylinositol-calcium second messenger system. This
CC       receptor is involved in tracheal smooth muscle contraction,
CC       bronchoconstriction, and control of aldosterone production.
CC   -!- SUBUNIT: Interacts with MPDZ and INADL. May interact with MPP3,
CC       PRDX6, DLG4, DLG1, CASK, APBA1 and MAGI2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Note=Localizes to the post-synaptic thickening of axo-dendritic
CC       synapses.
CC   -!- DOMAIN: The PDZ domain-binding motif is involved in the
CC       interaction with INADL, CASK, APBA1, DLG1 and DLG4 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; S49542; AAB24369.1; -; mRNA.
DR   IPI; IPI00117490; -.
DR   PIR; S40689; S40689.
DR   RefSeq; NP_766400.1; NM_172812.2.
DR   UniGene; Mm.214351; -.
DR   ProteinModelPortal; P35363; -.
DR   SMR; P35363; 77-396.
DR   STRING; P35363; -.
DR   PhosphoSite; P35363; -.
DR   PRIDE; P35363; -.
DR   Ensembl; ENSMUST00000036653; ENSMUSP00000047774; ENSMUSG00000034997.
DR   GeneID; 15558; -.
DR   KEGG; mmu:15558; -.
DR   UCSC; uc007uqc.1; mouse.
DR   CTD; 15558; -.
DR   MGI; MGI:109521; Htr2a.
DR   eggNOG; roNOG07344; -.
DR   HOGENOM; HBG445348; -.
DR   HOVERGEN; HBG107487; -.
DR   InParanoid; P35363; -.
DR   OMA; NSGEANT; -.
DR   OrthoDB; EOG4TMR24; -.
DR   PhylomeDB; P35363; -.
DR   NextBio; 288500; -.
DR   ArrayExpress; P35363; -.
DR   Bgee; P35363; -.
DR   CleanEx; MM_HTR2A; -.
DR   Genevestigator; P35363; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000455; 5HT2A_rcpt.
DR   InterPro; IPR002231; 5HT_rcpt.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00516; 5HT2ARECEPTR.
DR   PRINTS; PR01101; 5HTRECEPTOR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Receptor; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    471       5-hydroxytryptamine receptor 2A.
FT                                /FTId=PRO_0000068948.
FT   TOPO_DOM      1     75       Extracellular (By similarity).
FT   TRANSMEM     76     99       Helical; Name=1; (By similarity).
FT   TOPO_DOM    100    110       Cytoplasmic (By similarity).
FT   TRANSMEM    111    132       Helical; Name=2; (By similarity).
FT   TOPO_DOM    133    147       Extracellular (By similarity).
FT   TRANSMEM    148    171       Helical; Name=3; (By similarity).
FT   TOPO_DOM    172    191       Cytoplasmic (By similarity).
FT   TRANSMEM    192    215       Helical; Name=4; (By similarity).
FT   TOPO_DOM    216    233       Extracellular (By similarity).
FT   TRANSMEM    234    254       Helical; Name=5; (By similarity).
FT   TOPO_DOM    255    324       Cytoplasmic (By similarity).
FT   TRANSMEM    325    346       Helical; Name=6; (By similarity).
FT   TOPO_DOM    347    362       Extracellular (By similarity).
FT   TRANSMEM    363    384       Helical; Name=7; (By similarity).
FT   TOPO_DOM    385    471       Cytoplasmic (By similarity).
FT   MOTIF       469    471       PDZ-binding.
FT   CARBOHYD      8      8       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     38     38       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     44     44       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     51     51       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     54     54       N-linked (GlcNAc...) (Potential).
FT   DISULFID    148    227       By similarity.
SQ   SEQUENCE   471 AA;  52842 MW;  DE763E5617EE8435 CRC64;
     MEILCEDNIS LSSIPNSLMQ LGDDSRLYPN DFNSRDANTS EASNWTIDAE NRTNLSCEGY
     LPPTCLSILH LQEKNWSALL TTVVIILTIA GNILVIMAVS LEKKLQNATN YFLMSLAIAD
     MLLGFLVMPV SMLTILYGYR WPLPSKLCAV WIYLDVLFST ASIMHLCAIS LDRYVAIQNP
     IHHSRFNSRT KAFLKIIAVW TISVGISMPI PVFGLQDDSK VFKEGSCLLA DDNFVLIGSF
     VAFFIPLTIM VITYFLTIKS LQKEATLCVS DLSTRAKLSS FSFLPQSSLS SEKLFQRSIH
     REPGSYAGRR TMQSISNEQK ACKVLGIVFF LFVVMWCPFF ITNIMAVICK ESCNENVIGA
     LLNVFVWIGY LSSAVNPLVY TLFNKTYRSA FSRYIQCQYK ENRKPLQLIL VNTIPTLAYK
     SSQLQVGQKK NSQEDAEPTA NDCSMVTLGN QHSEEMCTDN IETVNEKVSC V
//
ID   NMDE1_MOUSE             Reviewed;        1464 AA.
AC   P35436;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   08-MAR-2011, entry version 116.
DE   RecName: Full=Glutamate [NMDA] receptor subunit epsilon-1;
DE   AltName: Full=N-methyl D-aspartate receptor subtype 2A;
DE            Short=NMDAR2A;
DE            Short=NR2A;
DE   Flags: Precursor;
GN   Name=Grin2a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92244361; PubMed=1374164; DOI=10.1038/357070a0;
RA   Meguro H., Mori H., Araki K., Kushiya E., Kutsuwada T., Yamazaki M.,
RA   Kumanishi T., Arakawa M., Sakimura K., Mishina M.;
RT   "Functional characterization of a heteromeric NMDA receptor channel
RT   expressed from cloned cDNAs.";
RL   Nature 357:70-74(1992).
RN   [2]
RP   SEQUENCE REVISION TO 384.
RA   Meguro H., Mori H., Araki K., Kushiya E., Kutsuwada T., Yamazaki M.,
RA   Kumanishi T., Arakawa M., Sakimura K., Mishina M.;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3B.
RX   PubMed=12008020; DOI=10.1016/S0169-328X(02)00173-0;
RA   Matsuda K., Kamiya Y., Matsuda S., Yuzaki M.;
RT   "Cloning and characterization of a novel NMDA receptor subunit NR3B: a
RT   dominant subunit that reduces calcium permeability.";
RL   Brain Res. Mol. Brain Res. 100:43-52(2002).
RN   [4]
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION IN A COMPLEX WITH GRIN1 AND
RP   GRIN3B.
RX   PubMed=14602821;
RA   Matsuda K., Fletcher M., Kamiya Y., Yuzaki M.;
RT   "Specific assembly with the NMDA receptor 3B subunit controls surface
RT   expression and calcium permeability of NMDA receptors.";
RL   J. Neurosci. 23:10064-10073(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-917, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   INTERACTION WITH HIP1.
RX   PubMed=17329427; DOI=10.1523/JNEUROSCI.5175-06.2007;
RA   Metzler M., Gan L., Wong T.P., Liu L., Helm J., Liu L., Georgiou J.,
RA   Wang Y., Bissada N., Cheng K., Roder J.C., Wang Y.T., Hayden M.R.;
RT   "NMDA receptor function and NMDA receptor-dependent phosphorylation of
RT   huntingtin is altered by the endocytic protein HIP1.";
RL   J. Neurosci. 27:2298-2308(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-943, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-888; SER-929; SER-1025
RP   AND SER-1459, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [9]
RP   INTERACTION WITH NETO1.
RX   PubMed=19243221; DOI=10.1371/journal.pbio.1000041;
RA   Ng D., Pitcher G.M., Szilard R.K., Sertie A., Kanisek M.,
RA   Clapcote S.J., Lipina T., Kalia L.V., Joo D., McKerlie C., Cortez M.,
RA   Roder J.C., Salter M.W., McInnes R.R.;
RT   "Neto1 is a novel CUB-domain NMDA receptor-interacting protein
RT   required for synaptic plasticity and learning.";
RL   PLoS Biol. 7:E41-E41(2009).
CC   -!- FUNCTION: NMDA receptor subtype of glutamate-gated ion channels
CC       possesses high calcium permeability and voltage-dependent
CC       sensitivity to magnesium. Activation requires binding of agonist
CC       to both types of subunits.
CC   -!- SUBUNIT: Forms heteromeric channel of a zeta subunit (GRIN1), a
CC       epsilon subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third
CC       subunit (GRIN3A or GRIN3B). Found in a complex with GRIN1 and
CC       GRIN3B. Found in a complex with GRIN1, GRIN3A and PPP2CB.
CC       Interacts with PDZ domains of AIP1, INADL and DLG4 (By
CC       similarity). Interacts with HIP1 and NETO1. Interacts with LRFN2
CC       (By similarity).
CC   -!- INTERACTION:
CC       Q62108:Dlg4; NbExp=2; IntAct=EBI-400115, EBI-300895;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Cell junction, synapse, postsynaptic cell membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel
CC       (TC 1.A.10.1) family. NR2A/GRIN2A subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; D10217; BAA01069.2; -; mRNA.
DR   IPI; IPI00118380; -.
DR   PIR; S29159; S29159.
DR   RefSeq; NP_032196.2; NM_008170.2.
DR   UniGene; Mm.2953; -.
DR   ProteinModelPortal; P35436; -.
DR   SMR; P35436; 31-392, 404-801.
DR   DIP; DIP-31567N; -.
DR   IntAct; P35436; 15.
DR   MINT; MINT-103939; -.
DR   STRING; P35436; -.
DR   PhosphoSite; P35436; -.
DR   PRIDE; P35436; -.
DR   Ensembl; ENSMUST00000032331; ENSMUSP00000032331; ENSMUSG00000059003.
DR   Ensembl; ENSMUST00000115835; ENSMUSP00000111501; ENSMUSG00000059003.
DR   GeneID; 14811; -.
DR   KEGG; mmu:14811; -.
DR   UCSC; uc007ydc.1; mouse.
DR   CTD; 14811; -.
DR   MGI; MGI:95820; Grin2a.
DR   eggNOG; roNOG08083; -.
DR   GeneTree; ENSGT00540000070221; -.
DR   HOGENOM; HBG717736; -.
DR   HOVERGEN; HBG052635; -.
DR   InParanoid; P35436; -.
DR   OMA; KMPSIES; -.
DR   OrthoDB; EOG4X0MRG; -.
DR   PhylomeDB; P35436; -.
DR   NextBio; 286999; -.
DR   ArrayExpress; P35436; -.
DR   Bgee; P35436; -.
DR   Genevestigator; P35436; -.
DR   GermOnline; ENSMUSG00000059003; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0017146; C:N-methyl-D-aspartate selective glutamate receptor complex; IPI:MGI.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
DR   GO; GO:0005262; F:calcium channel activity; IMP:MGI.
DR   GO; GO:0004972; F:N-methyl-D-aspartate selective glutamate receptor activity; IMP:MGI.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0033058; P:directional locomotion; IGI:MGI.
DR   GO; GO:0042417; P:dopamine metabolic process; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; TAS:UniProtKB.
DR   GO; GO:0007613; P:memory; IMP:MGI.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IGI:MGI.
DR   GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptosis; IGI:MGI.
DR   GO; GO:0008104; P:protein localization; IGI:MGI.
DR   GO; GO:0060079; P:regulation of excitatory postsynaptic membrane potential; IMP:MGI.
DR   GO; GO:0051930; P:regulation of sensory perception of pain; IMP:MGI.
DR   GO; GO:0001975; P:response to amphetamine; IMP:MGI.
DR   GO; GO:0042493; P:response to drug; IMP:MGI.
DR   GO; GO:0045471; P:response to ethanol; IMP:MGI.
DR   GO; GO:0009611; P:response to wounding; IMP:MGI.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR   GO; GO:0042428; P:serotonin metabolic process; IMP:MGI.
DR   GO; GO:0030431; P:sleep; IMP:MGI.
DR   GO; GO:0001964; P:startle response; IMP:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR019594; Glu_rcpt_Glu/Gly-bd.
DR   InterPro; IPR001320; Iontro_glu_rcpt.
DR   InterPro; IPR001508; NMDA_rcpt.
DR   InterPro; IPR018884; NMDAR2_C.
DR   InterPro; IPR001638; SBP_bac_3.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF10565; NMDAR2_C; 1.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   PRINTS; PR00177; NMDARECEPTOR.
DR   SMART; SM00918; Lig_chan-Glu_bd; 1.
DR   SMART; SM00079; PBPe; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell junction; Cell membrane; Disulfide bond; Glycoprotein;
KW   Ion transport; Ionic channel; Ligand-gated ion channel; Magnesium;
KW   Membrane; Metal-binding; Phosphoprotein; Postsynaptic cell membrane;
KW   Receptor; Signal; Synapse; Transmembrane; Transmembrane helix;
KW   Transport; Zinc.
FT   SIGNAL        1     22       Potential.
FT   CHAIN        23   1464       Glutamate [NMDA] receptor subunit
FT                                epsilon-1.
FT                                /FTId=PRO_0000011574.
FT   TOPO_DOM     23    555       Extracellular (Potential).
FT   TRANSMEM    556    576       Helical; (Potential).
FT   TOPO_DOM    577    633       Cytoplasmic (Potential).
FT   TRANSMEM    634    654       Helical; (Potential).
FT   TOPO_DOM    655    816       Extracellular (Potential).
FT   TRANSMEM    817    837       Helical; (Potential).
FT   TOPO_DOM    838   1464       Cytoplasmic (Potential).
FT   REGION      511    513       Glutamate binding (By similarity).
FT   REGION      689    690       Glutamate binding (By similarity).
FT   MOTIF      1462   1464       PDZ-binding (By similarity).
FT   METAL       128    128       Zinc (By similarity).
FT   METAL       283    283       Zinc (By similarity).
FT   BINDING     518    518       Glutamate (By similarity).
FT   BINDING     731    731       Glutamate; via amide nitrogen (By
FT                                similarity).
FT   SITE        614    614       Functional determinant of NMDA receptors
FT                                (By similarity).
FT   MOD_RES     888    888       Phosphothreonine.
FT   MOD_RES     912    912       Phosphoserine (By similarity).
FT   MOD_RES     917    917       Phosphoserine.
FT   MOD_RES     929    929       Phosphoserine.
FT   MOD_RES     943    943       Phosphotyrosine.
FT   MOD_RES    1025   1025       Phosphoserine.
FT   MOD_RES    1459   1459       Phosphoserine.
FT   CARBOHYD     75     75       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    340    340       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    380    380       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    443    443       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    444    444       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    541    541       N-linked (GlcNAc...) (Potential).
FT   DISULFID     87    320       By similarity.
SQ   SEQUENCE   1464 AA;  165421 MW;  438986DD5666C152 CRC64;
     MGRLGYWTLL VLPALLVWHG PAQNAAAEKG TPALNIAVLL GHSHDVTERE LRNLWGPEQA
     TGLPLDVNVV ALLMNRTDPK SLITHVCDLM SGARIHGLVF GDDTDQEAVA QMLDFISSQT
     FIPILGIHGG ASMIMADKDP TSTFFQFGAS IQQQATVMLK IMQDYDWHVF SLVTTIFPGY
     RDFISFIKTT VDNSFVGWDM QNVITLDTSF EDAKTQVQLK KIHSSVILLY CSKDEAVLIL
     SEARSLGLTG YDFFWIVPSL VSGNTELIPK EFPSGLISVS YDDWDYSLEA RVRDGLGILT
     TAASSMLEKF SYIPEAKASC YGQTEKPETP LHTLHQFMVN VTWDGKDLSF TEEGYQVHPR
     LVVIVLNKDR EWEKVGKWEN QTLSLRHAVW PRYKSFSDCE PDDNHLSIVT LEEAPFVIVE
     DIDPLTETCV RNTVPCRKFV KINNSTNEGM NVKKCCKGFC IDILKKLSRT VKFTYDLYLV
     TNGKHGKKVN NVWNGMIGEV VYQRAVMAVG SLTINEERSE VVDFSVPFVE TGISVMVSRS
     NGTVSPSAFL EPFSASVWVM MFVMLLIVSA IAVFVFEYFS PVGYNRNLAK GKAPHGPSFT
     IGKAIWLLWG LVFNNSVPVQ NPKGTTSKIM VSVWAFFAVI FLASYTANLA AFMIQEEFVD
     QVTGLSDKKF QRPHDYSPPF RFGTVPNGST ERNIRNNYPY MHQYMTKFNQ RGVEDALVSL
     KTGKLDAFIY DAAVLNYKAG RDEGCKLVTI GSGYIFATTG YGIALQKGSP WKRQIDLALL
     QFVGDGEMEE LETLWLTGIC HNEKNEVMSS QLDIDNMAGV FYMLAAAMAL SLITFIWEHL
     FYWKLRFCFT GVCSDRPGLL FSISRGIYSC IHGVHIEEKK KSPDFNLTGS QSNMLKLLRS
     AKNISNMSNM NSSRMDSPKR AADFIQRGSL IVDMVSDKGN LIYSDNRSFQ GKDSIFGENM
     NELQTFVANR HKDSLSNYVF QGQHPLTLNE SNPNTVEVAV STESKGNSRP RQLWKKSMES
     LRQDSLNQNP VSQRDEKTAE NRTHSLKSPR YLPEEVAHSD ISETSSRATC HREPDNNKNH
     KTKDNFKRSM ASKYPKDCSE VERTYVKTKA SSPRDKIYTI DGEKEPSFHL DPPQFIENIV
     LPENVDFPDT YQDHNENFRK GDSTLPMNRN PLHNEDGLPN NDQYKLYAKH FTLKDKGSPH
     SEGSDRYRQN STHCRSCLSN LPTYSGHFTM RSPFKCDACL RMGNLYDIDE DQMLQETGNP
     ATREEAYQQD WSQNNALQFQ KNKLKINRQH SYDNILDKPR EIDLSRPSRS ISLKDRERLL
     EGNLYGSLFS VPSSKLLGNK SSLFPQGLED SKRSKSLLPD HTSDNPFLHT YGDDQRLVIG
     RCPSDPYKHS LPSQAVNDSY LRSSLRSTAS YCSRDSRGHS DVYISEHVMP YAANKNNMYS
     TPRVLNSCSN RRVYKKMPSI ESDV
//
ID   ODPA_MOUSE              Reviewed;         390 AA.
AC   P35486;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial;
DE            EC=1.2.4.1;
DE   AltName: Full=PDHE1-A type I;
DE   Flags: Precursor;
GN   Name=Pdha1; Synonyms=Pdha-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92256495; PubMed=1581363; DOI=10.1016/0167-4781(92)90102-6;
RA   Fitzgerald G.F., Hutchison W.M., Dahl H.-H.M.;
RT   "Isolation and characterisation of the mouse pyruvate dehydrogenase E1
RT   alpha genes.";
RL   Biochim. Biophys. Acta 1131:83-90(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 46-58; 120-127; 133-141; 159-182; 216-244;
RP   246-263; 268-274; 278-321; 324-343 AND 379-385, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-301, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; SER-293 AND
RP   SER-300, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; TYR-289; SER-293
RP   AND SER-300, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293 AND SER-300, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains
CC       multiple copies of three enzymatic components: pyruvate
CC       dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and
CC       lipoamide dehydrogenase (E3).
CC   -!- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue
CC       acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       acetyltransferase] S-acetyldihydrolipoyllysine + CO(2).
CC   -!- COFACTOR: Thiamine pyrophosphate.
CC   -!- ENZYME REGULATION: E1 activity is regulated by phosphorylation
CC       (inactivation) and dephosphorylation (activation) of the alpha
CC       subunit.
CC   -!- SUBUNIT: Tetramer of 2 alpha and 2 beta subunits.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- TISSUE SPECIFICITY: In all tissues, but in very low amount in
CC       testis.
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DR   EMBL; M76727; AAA53046.1; -; mRNA.
DR   EMBL; BC007142; AAH07142.1; -; mRNA.
DR   IPI; IPI00337893; -.
DR   PIR; S23506; S23506.
DR   RefSeq; NP_032836.1; NM_008810.2.
DR   UniGene; Mm.34775; -.
DR   ProteinModelPortal; P35486; -.
DR   SMR; P35486; 29-390.
DR   STRING; P35486; -.
DR   PhosphoSite; P35486; -.
DR   REPRODUCTION-2DPAGE; P35486; -.
DR   PRIDE; P35486; -.
DR   Ensembl; ENSMUST00000033662; ENSMUSP00000033662; ENSMUSG00000031299.
DR   GeneID; 18597; -.
DR   KEGG; mmu:18597; -.
DR   UCSC; uc009utc.1; mouse.
DR   CTD; 18597; -.
DR   MGI; MGI:97532; Pdha1.
DR   eggNOG; roNOG13286; -.
DR   HOGENOM; HBG753263; -.
DR   HOVERGEN; HBG001863; -.
DR   InParanoid; P35486; -.
DR   OMA; IVENNRY; -.
DR   OrthoDB; EOG4W0XD6; -.
DR   PhylomeDB; P35486; -.
DR   BRENDA; 1.2.4.1; 244.
DR   NextBio; 294490; -.
DR   ArrayExpress; P35486; -.
DR   Bgee; P35486; -.
DR   CleanEx; MM_PDHA1; -.
DR   Genevestigator; P35486; -.
DR   GermOnline; ENSMUSG00000031299; Mus musculus.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR   Pfam; PF00676; E1_dh; 1.
DR   TIGRFAMs; TIGR03182; PDH_E1_alph_y; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Glycolysis; Mitochondrion;
KW   Oxidoreductase; Phosphoprotein; Pyruvate; Thiamine pyrophosphate;
KW   Transit peptide.
FT   TRANSIT       1     29       Mitochondrion (By similarity).
FT   CHAIN        30    390       Pyruvate dehydrogenase E1 component
FT                                subunit alpha, somatic form,
FT                                mitochondrial.
FT                                /FTId=PRO_0000020442.
FT   MOD_RES      77     77       N6-acetyllysine (By similarity).
FT   MOD_RES      83     83       N6-acetyllysine (By similarity).
FT   MOD_RES     231    231       Phosphothreonine (By similarity).
FT   MOD_RES     232    232       Phosphoserine.
FT   MOD_RES     289    289       Phosphotyrosine.
FT   MOD_RES     293    293       Phosphoserine.
FT   MOD_RES     295    295       Phosphoserine (By similarity).
FT   MOD_RES     300    300       Phosphoserine.
FT   MOD_RES     301    301       Phosphotyrosine.
FT   MOD_RES     321    321       N6-acetyllysine (By similarity).
FT   MOD_RES     336    336       N6-acetyllysine (By similarity).
SQ   SEQUENCE   390 AA;  43232 MW;  40898944CE8E0A03 CRC64;
     MRKMLAAVSR VLAGSAQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP PVTTVLTRED
     GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC CVGLEAGINP TDHLITAYRA
     HGFTFTRGLP VRAILAELTG RRGGCAKGKG GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA
     CKYNGKDEVC LTLYGDGAAN QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST
     DYYKRGDFIP GLRVDGMDIL CVREATKFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS
     YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA QFATADPEPP
     LEELGYHIYS SDPPFEVRGA NQWIKFKSVS
//
ID   FAAA_MOUSE              Reviewed;         419 AA.
AC   P35505; Q9QW65;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Fumarylacetoacetase;
DE            Short=FAA;
DE            EC=3.7.1.2;
DE   AltName: Full=Beta-diketonase;
DE   AltName: Full=Fumarylacetoacetate hydrolase;
GN   Name=Fah;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92159050; PubMed=1741389; DOI=10.1073/pnas.89.4.1363;
RA   Klebig M.L., Russell L.B., Rinchik E.M.;
RT   "Murine fumarylacetoacetate hydrolase (Fah) gene is disrupted by a
RT   neonatally lethal albino deletion that defines the hepatocyte-specific
RT   developmental regulation 1 (hsdr-1) locus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:1363-1367(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Liver;
RX   MEDLINE=92399018; PubMed=1524868; DOI=10.1016/0885-4505(92)90044-Y;
RA   Grompe M., Al-Dhalimy M.;
RT   "Nucleotide sequence of a cDNA encoding murine fumarylacetoacetate
RT   hydrolase.";
RL   Biochem. Med. Metab. Biol. 48:26-31(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=92354906; PubMed=1644288;
RA   Ruppert S., Kelsey G., Schedl A., Schmid E., Thies E., Schutz G.;
RT   "Deficiency of an enzyme of tyrosine metabolism underlies altered gene
RT   expression in newborn liver of lethal albino mice.";
RL   Genes Dev. 6:1430-1443(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   MUTAGENESIS OF GLU-201.
RX   MEDLINE=21143362; PubMed=11209059; DOI=10.1073/pnas.98.2.641;
RA   Aponte J.L., Sega G.A., Hauser L.J., Dhar M.S., Withrow C.M.,
RA   Carpenter D.A., Rinchik E.M., Culiat C.T., Johnson D.K.;
RT   "Point mutations in the murine fumarylacetoacetate hydrolase gene:
RT   animal models for the human genetic disorder hereditary tyrosinemia
RT   type 1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:641-645(2001).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH PRODUCTS AND
RP   DIVALENT METAL CATIONS.
RX   PubMed=10508789; DOI=10.1016/S0969-2126(99)80170-1;
RA   Timm D.E., Mueller H.A., Bhanumoorthy P., Harp J.M., Bunick G.J.;
RT   "Crystal structure and mechanism of a carbon-carbon bond hydrolase.";
RL   Structure 7:1023-1033(1999).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH INHIBITOR AND
RP   METAL IONS.
RX   PubMed=11154690; DOI=10.1074/jbc.M007621200;
RA   Bateman R.L., Bhanumoorthy P., Witte J.F., McClard R.W., Grompe M.,
RA   Timm D.E.;
RT   "Mechanistic inferences from the crystal structure of
RT   fumarylacetoacetate hydrolase with a bound phosphorus-based
RT   inhibitor.";
RL   J. Biol. Chem. 276:15284-15291(2001).
CC   -!- CATALYTIC ACTIVITY: 4-fumarylacetoacetate + H(2)O = acetoacetate +
CC       fumarate.
CC   -!- COFACTOR: Calcium.
CC   -!- COFACTOR: Magnesium.
CC   -!- PATHWAY: Amino-acid degradation; L-phenylalanine degradation;
CC       acetoacetate and fumarate from L-phenylalanine: step 6/6.
CC   -!- SUBUNIT: Homodimer.
CC   -!- TISSUE SPECIFICITY: Mainly in liver and kidney.
CC   -!- SIMILARITY: Belongs to the FAH family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M84145; AAA37591.1; -; mRNA.
DR   EMBL; Z11774; CAA77819.1; -; mRNA.
DR   EMBL; BC010767; AAH10767.1; -; mRNA.
DR   IPI; IPI00310035; -.
DR   PIR; A40219; A40219.
DR   PIR; A56825; A56825.
DR   UniGene; Mm.3798; -.
DR   PDB; 1HYO; X-ray; 1.30 A; A/B=1-419.
DR   PDB; 1QCN; X-ray; 1.90 A; A/B=1-419.
DR   PDB; 1QCO; X-ray; 1.90 A; A/B=1-419.
DR   PDB; 1QQJ; X-ray; 1.55 A; A/B=1-419.
DR   PDB; 2HZY; X-ray; 1.35 A; A/B=1-419.
DR   PDBsum; 1HYO; -.
DR   PDBsum; 1QCN; -.
DR   PDBsum; 1QCO; -.
DR   PDBsum; 1QQJ; -.
DR   PDBsum; 2HZY; -.
DR   ProteinModelPortal; P35505; -.
DR   SMR; P35505; 1-417.
DR   STRING; P35505; -.
DR   PhosphoSite; P35505; -.
DR   SWISS-2DPAGE; P35505; -.
DR   PRIDE; P35505; -.
DR   Ensembl; ENSMUST00000032865; ENSMUSP00000032865; ENSMUSG00000030630.
DR   MGI; MGI:95482; Fah.
DR   eggNOG; roNOG15538; -.
DR   HOGENOM; HBG289935; -.
DR   HOVERGEN; HBG001919; -.
DR   InParanoid; P35505; -.
DR   OrthoDB; EOG4Q2DFM; -.
DR   BRENDA; 3.7.1.2; 244.
DR   NextBio; 285108; -.
DR   ArrayExpress; P35505; -.
DR   Bgee; P35505; -.
DR   CleanEx; MM_FAH; -.
DR   Genevestigator; P35505; -.
DR   GermOnline; ENSMUSG00000030630; Mus musculus.
DR   GO; GO:0004334; F:fumarylacetoacetase activity; IMP:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006527; P:arginine catabolic process; IMP:MGI.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006572; P:tyrosine catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005959; Fumarylacetoacetase.
DR   InterPro; IPR002529; Fumarylacetoacetase_C-like.
DR   InterPro; IPR011234; Fumarylacetoacetase_C-rel.
DR   InterPro; IPR015377; Fumarylacetoacetase_N.
DR   Gene3D; G3DSA:3.90.850.10; Fumarylacetoacetase_C-rel; 1.
DR   Gene3D; G3DSA:2.30.30.230; Fumarylacetoacetase_N; 1.
DR   PANTHER; PTHR11820:SF1; Fum_ac_acetase; 1.
DR   Pfam; PF09298; DUF1969; 1.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   SUPFAM; SSF56529; Fumarylacetoacetase_C-rel; 1.
DR   SUPFAM; SSF63433; Fumarylacetoacetase_N; 1.
DR   TIGRFAMs; TIGR01266; fum_ac_acetase; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Calcium; Hydrolase; Magnesium;
KW   Metal-binding; Phenylalanine catabolism; Tyrosine catabolism.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    419       Fumarylacetoacetase.
FT                                /FTId=PRO_0000156826.
FT   ACT_SITE    133    133       Proton acceptor (Probable).
FT   METAL       126    126       Calcium.
FT   METAL       199    199       Calcium.
FT   METAL       201    201       Calcium.
FT   METAL       233    233       Calcium.
FT   METAL       233    233       Magnesium.
FT   METAL       253    253       Magnesium.
FT   METAL       257    257       Magnesium.
FT   BINDING     128    128       Substrate.
FT   BINDING     142    142       Substrate.
FT   BINDING     240    240       Substrate.
FT   BINDING     244    244       Substrate.
FT   BINDING     350    350       Substrate.
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MUTAGEN     201    201       E->G: Decrease in activity.
FT   CONFLICT    129    130       SS -> PF (in Ref. 2; CAA77819).
FT   CONFLICT    307    307       G -> R (in Ref. 3; no nucleotide entry).
FT   CONFLICT    376    376       G -> E (in Ref. 2; CAA77819).
FT   TURN         14     16
FT   STRAND       19     23
FT   STRAND       31     36
FT   STRAND       39     42
FT   TURN         43     46
FT   HELIX        47     49
FT   TURN         53     57
FT   HELIX        59     63
FT   STRAND       64     67
FT   HELIX        68     73
FT   HELIX        75     89
FT   HELIX        95     98
FT   HELIX       100    106
FT   STRAND      107    110
FT   STRAND      114    116
FT   STRAND      124    127
FT   HELIX       131    142
FT   HELIX       144    146
FT   TURN        150    154
FT   STRAND      158    160
FT   STRAND      166    168
FT   STRAND      177    180
FT   STRAND      189    192
FT   STRAND      199    206
FT   HELIX       218    221
FT   HELIX       222    224
FT   STRAND      225    232
FT   HELIX       237    243
FT   TURN        245    247
FT   HELIX       251    254
FT   STRAND      257    259
FT   STRAND      263    265
FT   HELIX       266    269
FT   HELIX       270    272
FT   HELIX       285    287
FT   STRAND      298    304
FT   STRAND      312    318
FT   HELIX       326    334
FT   STRAND      345    347
FT   HELIX       356    358
FT   HELIX       362    365
FT   TURN        366    370
FT   STRAND      380    383
FT   STRAND      389    397
FT   STRAND      402    413
SQ   SEQUENCE   419 AA;  46104 MW;  771C2471D53FBB02 CRC64;
     MSFIPVAEDS DFPIQNLPYG VFSTQSNPKP RIGVAIGDQI LDLSVIKHLF TGPALSKHQH
     VFDETTLNNF MGLGQAAWKE ARASLQNLLS ASQARLRDDK ELRQRAFTSQ ASATMHLPAT
     IGDYTDFYSS RQHATNVGIM FRGKENALLP NWLHLPVGYH GRASSIVVSG TPIRRPMGQM
     RPDNSKPPVY GACRLLDMEL EMAFFVGPGN RFGEPIPISK AHEHIFGMVL MNDWSARDIQ
     QWEYVPLGPF LGKSFGTTIS PWVVPMDALM PFVVPNPKQD PKPLPYLCHS QPYTFDINLS
     VSLKGEGMSQ AATICRSNFK HMYWTMLQQL THHSVNGCNL RPGDLLASGT ISGSDPESFG
     SMLELSWKGT KAIDVGQGQT RTFLLDGDEV IITGHCQGDG YRVGFGQCAG KVLPALSPA
//
ID   RET_MOUSE               Reviewed;        1115 AA.
AC   P35546; Q8BQ34; Q9QXH9;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   08-MAR-2011, entry version 110.
DE   RecName: Full=Proto-oncogene tyrosine-protein kinase receptor Ret;
DE            EC=2.7.10.1;
DE   AltName: Full=Proto-oncogene c-Ret;
DE   Flags: Precursor;
GN   Name=Ret;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=93205390; PubMed=8455936;
RA   Iwamoto T., Taniguchi M., Asai N., Ohkusu K., Nakashima I.,
RA   Takahashi M.;
RT   "cDNA cloning of mouse ret proto-oncogene and its sequence similarity
RT   to the cadherin superfamily.";
RL   Oncogene 8:1087-1091(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=A;
RA   Phua C.Y.D., Too H.P.;
RT   "Molecular characterization of mouse neuro-2a c-ret proto-oncogene.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=BALB/c;
RA   Wang Y.-Z., Yoong L.-F., Too H.-P.;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   INTERACTION WITH DOK2; DOK4 AND DOK5, PHOSPHORYLATION, AND MUTAGENESIS
RP   OF TYR-1063.
RX   MEDLINE=21363571; PubMed=11470823; DOI=10.1083/jcb.200102032;
RA   Grimm J., Sachs M., Britsch S., Di Cesare S., Schwarz-Romond T.,
RA   Alitalo K., Birchmeier W.;
RT   "Novel p62dok family members, dok-4 and dok-5, are substrates of the
RT   c-Ret receptor tyrosine kinase and mediate neuronal differentiation.";
RL   J. Cell Biol. 154:345-354(2001).
CC   -!- FUNCTION: Probable receptor with tyrosine-protein kinase activity;
CC       important for development.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBUNIT: Phosphorylated form interacts with the PBT domain of
CC       DOK2, DOK4 and DOK5.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P35546-1; Sequence=Displayed;
CC       Name=2; Synonyms=Ret9;
CC         IsoId=P35546-2; Sequence=VSP_011304;
CC   -!- TISSUE SPECIFICITY: Expressed in peripheral nerve cells and
CC       hematopoietic cells.
CC   -!- PTM: Autophosphorylated on C-terminal tyrosine residues upon
CC       ligand stimulation. Dephosphorylated by PTPRJ on Tyr-906, Tyr-1016
CC       and Tyr-1063 (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family.
CC   -!- SIMILARITY: Contains 1 cadherin domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X67812; CAA48013.1; -; mRNA.
DR   EMBL; AF209436; AAF21033.1; -; mRNA.
DR   EMBL; AY326397; AAP88379.1; -; mRNA.
DR   EMBL; AK051633; BAC34699.1; -; mRNA.
DR   EMBL; BC059012; AAH59012.1; -; mRNA.
DR   IPI; IPI00463765; -.
DR   IPI; IPI00463766; -.
DR   PIR; I48735; S29926.
DR   RefSeq; NP_001074249.1; NM_001080780.1.
DR   RefSeq; NP_033076.2; NM_009050.2.
DR   UniGene; Mm.57199; -.
DR   PDB; 1UEF; X-ray; 2.50 A; C/D=1055-1067.
DR   PDBsum; 1UEF; -.
DR   ProteinModelPortal; P35546; -.
DR   SMR; P35546; 29-273, 369-407, 714-1012.
DR   STRING; P35546; -.
DR   PhosphoSite; P35546; -.
DR   PRIDE; P35546; -.
DR   Ensembl; ENSMUST00000032201; ENSMUSP00000032201; ENSMUSG00000030110.
DR   Ensembl; ENSMUST00000088790; ENSMUSP00000086169; ENSMUSG00000030110.
DR   GeneID; 19713; -.
DR   KEGG; mmu:19713; -.
DR   UCSC; uc009dlm.1; mouse.
DR   UCSC; uc009dln.1; mouse.
DR   CTD; 19713; -.
DR   MGI; MGI:97902; Ret.
DR   eggNOG; roNOG08011; -.
DR   HOGENOM; HBG444015; -.
DR   HOVERGEN; HBG002609; -.
DR   InParanoid; P35546; -.
DR   OMA; GCARVYF; -.
DR   OrthoDB; EOG4P2Q1H; -.
DR   PhylomeDB; P35546; -.
DR   BRENDA; 2.7.10.1; 244.
DR   NextBio; 297098; -.
DR   ArrayExpress; P35546; -.
DR   Bgee; P35546; -.
DR   CleanEx; MM_RET; -.
DR   Genevestigator; P35546; -.
DR   GermOnline; ENSMUSG00000030110; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:EC.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; TAS:MGI.
DR   GO; GO:0001838; P:embryonic epithelial tube formation; IDA:MGI.
DR   GO; GO:0048484; P:enteric nervous system development; IMP:MGI.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   GO; GO:0000165; P:MAPKKK cascade; IGI:MGI.
DR   GO; GO:0001755; P:neural crest cell migration; IMP:MGI.
DR   GO; GO:0042551; P:neuron maturation; IMP:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IGI:MGI.
DR   GO; GO:0001657; P:ureteric bud development; IMP:MGI.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   InterPro; IPR016249; Tyr_prot_kinase_Ret_rcpt.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 1.
DR   Pfam; PF00028; Cadherin; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PIRSF; PIRSF000631; TyrPK_receptor_Ret; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00112; CA; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49313; Cadherin; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50268; CADHERIN_2; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Glycoprotein; Kinase;
KW   Membrane; Nucleotide-binding; Phosphoprotein; Proto-oncogene; Signal;
KW   Transferase; Transmembrane; Transmembrane helix;
KW   Tyrosine-protein kinase.
FT   SIGNAL        1     28       Potential.
FT   CHAIN        29   1115       Proto-oncogene tyrosine-protein kinase
FT                                receptor Ret.
FT                                /FTId=PRO_0000024451.
FT   TOPO_DOM     29    637       Extracellular (Potential).
FT   TRANSMEM    638    659       Helical; (Potential).
FT   TOPO_DOM    660   1115       Cytoplasmic (Potential).
FT   DOMAIN      168    273       Cadherin.
FT   DOMAIN      725   1017       Protein kinase.
FT   NP_BIND     731    739       ATP (By similarity).
FT   ACT_SITE    875    875       Proton acceptor (By similarity).
FT   BINDING     759    759       ATP (By similarity).
FT   MOD_RES     697    697       Phosphoserine (By similarity).
FT   MOD_RES     807    807       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     810    810       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     901    901       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     906    906       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     982    982       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES    1016   1016       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES    1063   1063       Phosphotyrosine; by autocatalysis.
FT   MOD_RES    1091   1091       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES    1097   1097       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   CARBOHYD     89     89       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     98     98       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    151    151       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    156    156       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    199    199       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    345    345       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    360    360       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    378    378       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    396    396       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    450    450       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    470    470       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    556    556       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ    1065   1115       MSDPNWPGESPVPLTRADGTSTGFPRYANDSVYANWMVSPS
FT                                AAKLMDTFDS -> RISHAFTRF (in isoform 2).
FT                                /FTId=VSP_011304.
FT   MUTAGEN    1063   1063       Y->F: Abolishes interaction with DOK
FT                                proteins.
FT   CONFLICT    174    174       F -> S (in Ref. 1; CAA48013).
FT   STRAND     1057   1059
FT   TURN       1061   1064
SQ   SEQUENCE   1115 AA;  123874 MW;  A5CF1EF45A640413 CRC64;
     MAKATSGAAG LGLKLILLLP LLGEAPLGLY FSRDAYWERL YVDQPAGTPL LYVHALRDAP
     GEVPSFRLGQ HLYGVYRTRL HENDWIRINE TTGLLYLNQS LDHSSWEQLS IRNGGFPLLT
     IFLQVFLGST AQREGECHWP GCTRVYFSFI NDTFPNCSSF KAQDLCIPET AVSFRVRENR
     PPGTFYHFHM LPVQFLCPNI SVKYSLLGGD SLPFRCDPDC LEVSTRWALD RELREKYVLE
     ALCIVAGPGA NKETVTLSFP VTVYDEDDSA PTFSGGVGTA SAVVEFKRKE GTVVATLQVF
     DADVVPASGE LVRRYTNTLL SGDSWAQQTF RVEHSPIETL VQVNNNSVRA TMHNYKLILN
     RSLSISESRV LQLAVLVNDS DFQGPGAGGI LVLHFNVSVL PVTLNLPRAY SFPVNKRARR
     YAQIGKVCVE NCQEFSGVSI QYKLQPSSIN CTALGVVTSP EDTSGTLFVN DTEALRRPEC
     TKLQYTVVAT DRQTRRQTQA SLVVTVEGTS ITEEVGCPKS CAVNKRRPEC EECGGLGSPT
     GRCEWRQGDG KGITRNFSTC SPSTRTCPDG HCDAVESRDA NICPQDCLRA DIVGGHERGE
     RQGIKAGYGI CNCFPDEKKC FCEPEDSQGP LCDALCRTII TAALFSLIIS ILLSIFCVCH
     HHKHGHKPPI ASAEMTFCRP AQGFPISYSS SGTRRPSLDS TENQVPVDSF KIPEDPKWEF
     PRKNLVLGKT LGEGEFGKVV KATAFRLKGR AGYTTVAVKM LKENASQSEL RDLLSEFNLL
     KQVNHPHVIK LYGACSQDGP LLLIVEYAKY GSLRGFLRDS RKIGPAYVSG GGSRNSSSLD
     HPDERVLTMG DLISFAWQIS RGMQYLAEMK LVHRDLAARN ILVAEGRKMK ISDFGLSRDV
     YEEDSYVKKS KGRIPVKWMA IESLFDHIYT TQSDVWSFGV LLWEIVTLGG NPYPGIPPER
     LFNLLKTGHR MERPDNCSEE MYRLMLQCWK QEPDKRPVFA DISKDLEKMM VKSRDYLDLA
     ASTPSDSLLY DDGLSEEETP LVDCNNAPLP RSLPSTWIEN KLYGMSDPNW PGESPVPLTR
     ADGTSTGFPR YANDSVYANW MVSPSAAKLM DTFDS
//
ID   IRK2_MOUSE              Reviewed;         428 AA.
AC   P35561;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   08-MAR-2011, entry version 107.
DE   RecName: Full=Inward rectifier potassium channel 2;
DE   AltName: Full=Inward rectifier K(+) channel Kir2.1;
DE            Short=IRK-1;
DE   AltName: Full=Potassium channel, inwardly rectifying subfamily J member 2;
GN   Name=Kcnj2; Synonyms=Irk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Macrophage;
RX   MEDLINE=93196696; PubMed=7680768; DOI=10.1038/362127a0;
RA   Kubo Y., Baldwin T.J., Jan Y.N., Jan L.Y.;
RT   "Primary structure and functional expression of a mouse inward
RT   rectifier potassium channel.";
RL   Nature 362:127-132(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=94109571; PubMed=8282096; DOI=10.1016/0014-5793(93)80840-Q;
RA   Morishige K., Takahashi N., Findlay I., Koyama H., Zanelli J.S.,
RA   Peterson C., Jenkins N.A., Copeland N.G., Mori N., Kurachi Y.;
RT   "Molecular cloning, functional expression and localization of an
RT   inward rectifier potassium channel in the mouse brain.";
RL   FEBS Lett. 336:375-380(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lens epithelium;
RX   MEDLINE=98288410; PubMed=9533862; DOI=10.1006/exer.1997.0432;
RA   Rae J.L., Shepard A.R.;
RT   "Inwardly rectifying potassium channels in lens epithelium are from
RT   the IRK1 (Kir 2.1) family.";
RL   Exp. Eye Res. 66:347-359(1998).
CC   -!- FUNCTION: Probably participates in establishing action potential
CC       waveform and excitability of neuronal and muscle tissues. Inward
CC       rectifier potassium channels are characterized by a greater
CC       tendency to allow potassium to flow into the cell rather than out
CC       of it. Their voltage dependence is regulated by the concentration
CC       of extracellular potassium; as external potassium is raised, the
CC       voltage range of the channel opening shifts to more positive
CC       voltages. The inward rectification is mainly due to the blockage
CC       of outward current by internal magnesium. Can be blocked by
CC       extracellular barium and cesium.
CC   -!- SUBUNIT: Homomultimeric and heteromultimeric association with
CC       Kir2.3, resulting in an enhanced G-protein-induced current.
CC       Association, via its PDZ-recognition domain, with LIN7A, LIN7B,
CC       LIN7C, DLG1, CASK and APBA1 plays a key role in its localization
CC       and trafficking (By similarity).
CC   -!- INTERACTION:
CC       P24588:AKAP5 (xeno); NbExp=2; IntAct=EBI-703793, EBI-703640;
CC       Q15700-4:DLG2 (xeno); NbExp=2; IntAct=EBI-703793, EBI-663057;
CC       Q2YHQ3:FLNA (xeno); NbExp=3; IntAct=EBI-703793, EBI-779542;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Prominently expressed in the central nervous
CC       system. Also found in other excitable tissues such as heart and
CC       skeletal muscle.
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
CC       (TC 1.A.2.1) family. KCNJ2 subfamily.
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DR   EMBL; X73052; CAA51526.1; -; mRNA.
DR   EMBL; AF021136; AAB88794.1; -; mRNA.
DR   IPI; IPI00119613; -.
DR   PIR; S32351; S32351.
DR   RefSeq; NP_032451.1; NM_008425.4.
DR   UniGene; Mm.4951; -.
DR   PDB; 1U4F; X-ray; 2.41 A; A/B/C/D=41-428.
DR   PDB; 2GIX; X-ray; 2.02 A; A/B/C/D=44-371.
DR   PDBsum; 1U4F; -.
DR   PDBsum; 2GIX; -.
DR   ProteinModelPortal; P35561; -.
DR   SMR; P35561; 45-371.
DR   IntAct; P35561; 14.
DR   MINT; MINT-104054; -.
DR   STRING; P35561; -.
DR   PhosphoSite; P35561; -.
DR   PRIDE; P35561; -.
DR   Ensembl; ENSMUST00000042970; ENSMUSP00000037192; ENSMUSG00000041695.
DR   GeneID; 16518; -.
DR   KEGG; mmu:16518; -.
DR   UCSC; uc007mdw.1; mouse.
DR   CTD; 16518; -.
DR   MGI; MGI:104744; Kcnj2.
DR   eggNOG; roNOG05227; -.
DR   HOGENOM; HBG716702; -.
DR   HOVERGEN; HBG006178; -.
DR   InParanoid; P35561; -.
DR   OMA; SRESKAC; -.
DR   OrthoDB; EOG4N04DV; -.
DR   PhylomeDB; P35561; -.
DR   NextBio; 289885; -.
DR   ArrayExpress; P35561; -.
DR   Bgee; P35561; -.
DR   Genevestigator; P35561; -.
DR   GermOnline; ENSMUSG00000041695; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR016449; K_chnl_inward-rec_Kir.
DR   InterPro; IPR001838; K_chnl_inward-rec_Kir-like.
DR   InterPro; IPR003271; K_chnl_inward-rec_Kir2.1.
DR   InterPro; IPR013521; K_chnl_inward-rec_Kir_Cr2.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   InterPro; IPR013673; K_chnl_inward-rec_Kir_N.
DR   Gene3D; G3DSA:2.60.40.1400; IR_K+channel_cytopl; 1.
DR   PANTHER; PTHR11767; K+channel_IR; 1.
DR   PANTHER; PTHR11767:SF15; KIR21_channel; 1.
DR   Pfam; PF01007; IRK; 1.
DR   Pfam; PF08466; IRK_N; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01324; KIR21CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; Ig_E-set; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Ion transport; Ionic channel; Membrane; Phosphoprotein;
KW   Potassium; Potassium transport; Transmembrane; Transmembrane helix;
KW   Transport; Voltage-gated channel.
FT   CHAIN         1    428       Inward rectifier potassium channel 2.
FT                                /FTId=PRO_0000154925.
FT   TOPO_DOM      1     81       Cytoplasmic (By similarity).
FT   TRANSMEM     82    106       Helical; Name=M1; (By similarity).
FT   TOPO_DOM    107    128       Extracellular (By similarity).
FT   INTRAMEM    129    140       Helical; Pore-forming; Name=H5; (By
FT                                similarity).
FT   INTRAMEM    141    147       Pore-forming; (By similarity).
FT   TOPO_DOM    148    156       Extracellular (By similarity).
FT   TRANSMEM    157    178       Helical; Name=M2; (By similarity).
FT   TOPO_DOM    179    428       Cytoplasmic (By similarity).
FT   MOTIF       142    147       Selectivity filter (By similarity).
FT   MOTIF       426    428       PDZ-binding (Potential).
FT   SITE        172    172       Role in the control of polyamine-mediated
FT                                channel gating and in the blocking by
FT                                intracellular magnesium (By similarity).
FT   MOD_RES     337    337       Phosphotyrosine (By similarity).
FT   STRAND      180    184
FT   TURN        188    190
FT   STRAND      192    195
FT   STRAND      197    204
FT   STRAND      207    216
FT   STRAND      218    220
FT   STRAND      222    236
FT   STRAND      242    249
FT   TURN        254    259
FT   STRAND      267    272
FT   TURN        278    281
FT   HELIX       284    289
FT   STRAND      293    302
FT   STRAND      308    316
FT   HELIX       317    319
FT   STRAND      320    322
FT   STRAND      324    326
FT   STRAND      330    332
FT   STRAND      334    340
FT   HELIX       341    343
FT   STRAND      347    349
FT   HELIX       358    364
SQ   SEQUENCE   428 AA;  48389 MW;  5B4219F979BBA41C CRC64;
     MGSVRTNRYS IVSSEEDGMK LATMAVANGF GNGKSKVHTR QQCRSRFVKK DGHCNVQFIN
     VGEKGQRYLA DIFTTCVDIR WRWMLVIFCL AFVLSWLFFG CVFWLIALLH GDLDTSKVSK
     ACVSEVNSFT AAFLFSIETQ TTIGYGFRCV TDECPIAVFM VVFQSIVGCI IDAFIIGAVM
     AKMAKPKKRN ETLVFSHNAV IAMRDGKLCL MWRVGNLRKS HLVEAHVRAQ LLKSRITSEG
     EYIPLDQIDI NVGFDSGIDR IFLVSPITIV HEIDEDSPLY DLSKQDIDNA DFEIVVILEG
     MVEATAMTTQ CRSSYLANEI LWGHRYEPVL FEEKHYYKVD YSRFHKTYEV PNTPLCSARD
     LAEKKYILSN ANSFCYENEV ALTSKEEEED SENGVPESTS TDSPPGIDLH NQASVPLEPR
     PLRRESEI
//
ID   CALX_MOUSE              Reviewed;         591 AA.
AC   P35564;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   08-MAR-2011, entry version 110.
DE   RecName: Full=Calnexin;
DE   Flags: Precursor;
GN   Name=Canx;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94183823; PubMed=8136357; DOI=10.1021/bi00177a013;
RA   Tjoelker L.W., Seyfried C.E., Eddy R.L. Jr., Shows T.B. Jr.,
RA   Calderon J., Schreiber R.B., Gray P.W.;
RT   "Human, mouse, and rat calnexin cDNA cloning: identification of
RT   potential calcium binding motifs and gene localization to human
RT   chromosome 5.";
RL   Biochemistry 33:3229-3236(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-155.
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 21-591.
RC   STRAIN=BALB/c;
RX   MEDLINE=94198223; PubMed=8148318; DOI=10.1093/intimm/6.1.101;
RA   Schreiber K.L., Bell M.P., Huntoon C.J., Rajagopalan S., Brenner M.B.,
RA   McKean D.J.;
RT   "Class II histocompatibility molecules associate with calnexin during
RT   assembly in the endoplasmic reticulum.";
RL   Int. Immunol. 6:101-111(1994).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=7628443;
RA   Wiest D.L., Burgess W.H., McKean D., Kearse K.P., Singer A.;
RT   "The molecular chaperone calnexin is expressed on the surface of
RT   immature thymocytes in association with clonotype-independent CD3
RT   complexes.";
RL   EMBO J. 14:3425-3433(1995).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553 AND SER-563, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553; THR-561 AND
RP   SER-563, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553; THR-561; SER-563
RP   AND SER-582, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553; SER-563; SER-569
RP   AND SER-582, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553; SER-563 AND
RP   SER-582, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553 AND SER-582, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Calcium-binding protein that interacts with newly
CC       synthesized glycoproteins in the endoplasmic reticulum. It may act
CC       in assisting protein assembly and/or in the retention within the
CC       ER of unassembled protein subunits. It seems to play a major role
CC       in the quality control apparatus of the ER by the retention of
CC       incorrectly folded proteins. Partial T-cell antigen receptor
CC       complexes can escape the ER of immature thymocytes in association
CC       with their molecular chaperone to be expressed at low levels on
CC       the cell surface where they may function as a signaling complex to
CC       regulate thymocyte maturation.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       type I membrane protein. Melanosome (By similarity). Note=When
CC       bound to CD3 epsilon chains, calnexin's ER retention signal can be
CC       masked, permitting it to escape ER retention.
CC   -!- SIMILARITY: Belongs to the calreticulin family.
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DR   EMBL; L18888; AAA21014.1; -; mRNA.
DR   EMBL; BC012408; AAH12408.1; -; mRNA.
DR   EMBL; BC040244; AAH40244.1; -; mRNA.
DR   EMBL; AK084175; BAC39133.1; -; mRNA.
DR   EMBL; L23865; AAA62450.1; -; mRNA.
DR   IPI; IPI00119618; -.
DR   PIR; B54354; B54354.
DR   RefSeq; NP_001103969.1; NM_001110499.1.
DR   RefSeq; NP_001103970.1; NM_001110500.1.
DR   RefSeq; NP_031623.1; NM_007597.3.
DR   UniGene; Mm.248827; -.
DR   ProteinModelPortal; P35564; -.
DR   SMR; P35564; 61-458.
DR   IntAct; P35564; 4.
DR   MINT; MINT-1862151; -.
DR   STRING; P35564; -.
DR   PhosphoSite; P35564; -.
DR   PRIDE; P35564; -.
DR   Ensembl; ENSMUST00000020637; ENSMUSP00000020637; ENSMUSG00000020368.
DR   GeneID; 12330; -.
DR   KEGG; mmu:12330; -.
DR   UCSC; uc007isf.1; mouse.
DR   CTD; 12330; -.
DR   MGI; MGI:88261; Canx.
DR   eggNOG; roNOG12927; -.
DR   HOGENOM; HBG444251; -.
DR   HOVERGEN; HBG005407; -.
DR   InParanoid; P35564; -.
DR   OMA; SAAEYKK; -.
DR   OrthoDB; EOG4DBTDB; -.
DR   PhylomeDB; P35564; -.
DR   NextBio; 280926; -.
DR   PMAP-CutDB; P35564; -.
DR   ArrayExpress; P35564; -.
DR   Bgee; P35564; -.
DR   CleanEx; MM_CANX; -.
DR   Genevestigator; P35564; -.
DR   GermOnline; ENSMUSG00000020368; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IDA:MGI.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005529; F:sugar binding; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   InterPro; IPR001580; Calret/calnex.
DR   InterPro; IPR018124; Calret/calnex_CS.
DR   InterPro; IPR009033; Calreticulin/calnexin_P.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   Gene3D; G3DSA:2.10.250.10; Calreticulin/calnexin_P; 2.
DR   Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 1.
DR   PANTHER; PTHR11073; Calret/calnex; 1.
DR   Pfam; PF00262; Calreticulin; 1.
DR   PRINTS; PR00626; CALRETICULIN.
DR   SUPFAM; SSF63887; Calret_calnex_P; 1.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 2.
DR   PROSITE; PS00803; CALRETICULIN_1; 1.
DR   PROSITE; PS00804; CALRETICULIN_2; 1.
DR   PROSITE; PS00805; CALRETICULIN_REPEAT; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Calcium; Chaperone; Disulfide bond;
KW   Endoplasmic reticulum; Lectin; Membrane; Metal-binding;
KW   Phosphoprotein; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21    591       Calnexin.
FT                                /FTId=PRO_0000004199.
FT   TOPO_DOM     21    482       Lumenal (Potential).
FT   TRANSMEM    483    503       Helical; (Potential).
FT   TOPO_DOM    504    591       Cytoplasmic (Potential).
FT   REPEAT      279    291       1-1.
FT   REPEAT      296    308       1-2.
FT   REPEAT      315    327       1-3.
FT   REPEAT      334    346       1-4.
FT   REPEAT      349    359       2-1.
FT   REPEAT      368    378       2-2.
FT   REPEAT      382    392       2-3.
FT   REPEAT      396    406       2-4.
FT   REGION      277    410       P domain (Extended arm) (By similarity).
FT   REGION      279    346       4 X approximate repeats.
FT   REGION      349    406       4 X approximate repeats.
FT   METAL        75     75       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       118    118       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       437    437       Calcium (By similarity).
FT   BINDING     165    165       Carbohydrate (By similarity).
FT   BINDING     167    167       Carbohydrate (By similarity).
FT   BINDING     186    186       Carbohydrate (By similarity).
FT   BINDING     217    217       Carbohydrate (By similarity).
FT   MOD_RES     138    138       N6-acetyllysine (By similarity).
FT   MOD_RES     553    553       Phosphoserine.
FT   MOD_RES     561    561       Phosphothreonine.
FT   MOD_RES     563    563       Phosphoserine.
FT   MOD_RES     569    569       Phosphoserine.
FT   MOD_RES     582    582       Phosphoserine.
FT   DISULFID    161    195       By similarity.
FT   DISULFID    361    367       By similarity.
FT   CONFLICT    416    416       K -> R (in Ref. 4; AAA62450).
FT   CONFLICT    468    468       P -> L (in Ref. 4; AAA62450).
FT   CONFLICT    472    472       L -> G (in Ref. 4; AAA62450).
FT   CONFLICT    538    538       R -> G (in Ref. 4; AAA62450).
FT   CONFLICT    560    560       V -> G (in Ref. 4; AAA62450).
SQ   SEQUENCE   591 AA;  67278 MW;  0D9F8FE03434BADC CRC64;
     MEGKWLLCLL LVLGTAAVEA HDGHDDDAID IEDDLDDVIE EVEDSKSKSD ASTPPSPKVT
     YKAPVPTGEV YFADSFDRGS LSGWILSKAK KDDTDDEIAK YDGKWEVDEM KETKLPGDKG
     LVLMSRAKHH AISAKLNKPF LFDTKPLIVQ YEVNFQNGIE CGGAYVKLLS KTAELSLDQF
     HDKTPYTIMF GPDKCGEDYK LHFIFRHKNP KTGVYEEKHA KRPDADLKTY FTDKKTHLYT
     LILNPDNSFE ILVDQSVVNS GNLLNDMTPP VNPSREIEDP EDRKPEDWDE RPKIADPDAV
     KPDDWDEDAP SKIPDEEATK PEGWLDDEPE YIPDPDAEKP EDWDEDMDGE WEAPQIANPK
     CESAPGCGVW QRPMIDNPNY KGKWKPPMID NPNYQGIWKP RKIPNPDFFE DLEPFKMTPF
     SAIGLELWSM TSDIFFDNFI ISGDRRVVDD WANDGWGLKK AADGAAEPGV VLQMLEAAEE
     RPWLWVVYIL TVALPVFLVI LFCCSGKKQS NAMEYKKTDA PQPDVKDEEG KEEEKNKRDE
     EEEEEKLEEK QKSDAEEDGV TGSQDEEDSK PKAEEDEILN RSPRNRKPRR E
//
ID   IRS1_MOUSE              Reviewed;        1233 AA.
AC   P35569;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   08-MAR-2011, entry version 103.
DE   RecName: Full=Insulin receptor substrate 1;
DE            Short=IRS-1;
GN   Name=Irs1; Synonyms=Irs-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94220494; PubMed=8167159; DOI=10.1016/0167-4889(94)90261-5;
RA   Araki E., Haag B.L. III, Kahn C.R.;
RT   "Cloning of the mouse insulin receptor substrate-1 (IRS-1) gene and
RT   complete sequence of mouse IRS-1.";
RL   Biochim. Biophys. Acta 1221:353-356(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=93192326; PubMed=8448209; DOI=10.1016/0167-4781(93)90222-Y;
RA   Keller S.R., Aebersold R., Garner C.W., Lienhard G.E.;
RT   "The insulin-elicited 160 kDa phosphotyrosine protein in mouse
RT   adipocytes is an insulin receptor substrate 1: identification by
RT   cloning.";
RL   Biochim. Biophys. Acta 1172:323-326(1993).
RN   [3]
RP   INTERACTION WITH PHIP.
RX   MEDLINE=20568313; PubMed=11018022; DOI=10.1074/jbc.C000611200;
RA   Farhang-Fallah J., Yin X., Trentin G., Cheng A.M., Rozakis-Adcock M.;
RT   "Cloning and characterization of PHIP, a novel insulin receptor
RT   substrate-1 pleckstrin homology domain interacting protein.";
RL   J. Biol. Chem. 275:40492-40497(2000).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=10749573; DOI=10.1172/JCI9017;
RA   Ogata N., Chikazu D., Kubota N., Terauchi Y., Tobe K., Azuma Y.,
RA   Ohta T., Kadowaki T., Nakamura K., Kawaguchi H.;
RT   "Insulin receptor substrate-1 in osteoblast is indispensable for
RT   maintaining bone turnover.";
RL   J. Clin. Invest. 105:935-943(2000).
RN   [5]
RP   INTERACTION WITH UBTF AND PIK3CA, AND EFFECT ON CELL AND BODY SIZE.
RX   PubMed=15197263; DOI=10.1073/pnas.0403328101;
RA   Drakas R., Tu X., Baserga R.;
RT   "Control of cell size through phosphorylation of upstream binding
RT   factor 1 by nuclear phosphatidylinositol 3-kinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9272-9276(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-324; SER-340;
RP   SER-1139 AND SER-1214, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May mediate the control of various cellular processes by
CC       insulin. When phosphorylated by the insulin receptor binds
CC       specifically to various cellular proteins containing SH2 domains
CC       such as phosphatidylinositol 3-kinase p85 subunit or GRB2.
CC       Activates phosphatidylinositol 3-kinase when bound to the
CC       regulatory p85 subunit (By similarity).
CC   -!- SUBUNIT: Interacts (via phosphorylated YXXM motifs) with PIK3R1
CC       (By similarity). Interacts with ROCK1 (By similarity). Interacts
CC       with GRB2 (By similarity). Interacts with SOCS7 (By similarity).
CC       Interacts (via IRS-type PTB domain) with IGF1R and INSR (via the
CC       tyrosine-phosphorylated NPXY motif) (By similarity). Interacts
CC       with UBTF and PIK3CA. Interacts (via PH domain) with PHIP.
CC   -!- INTERACTION:
CC       Q03963:Eif2ak2; NbExp=1; IntAct=EBI-400825, EBI-2603444;
CC       Q8VDD9:Phip; NbExp=1; IntAct=EBI-400825, EBI-1369766;
CC       Q13625-2:TP53BP2 (xeno); NbExp=2; IntAct=EBI-400825, EBI-287091;
CC       Q8CG79:Tp53bp2; NbExp=1; IntAct=EBI-400825, EBI-645416;
CC   -!- TISSUE SPECIFICITY: Expressed in osteoblasts, but not in
CC       osteoclasts.
CC   -!- PTM: Serine phosphorylation of IRS1 is a mechanism for insulin
CC       resistance. Ser-307 phosphorylation inhibits insulin action
CC       through disruption of IRS1 interaction with the insulin receptor
CC       (By similarity).
CC   -!- PTM: Phosphorylation of Tyr-891 is required for GRB2-binding (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 IRS-type PTB domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
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DR   EMBL; L24563; AAA39335.1; -; mRNA.
DR   EMBL; X69722; CAA49378.1; -; mRNA.
DR   IPI; IPI00119627; -.
DR   PIR; S30185; S30185.
DR   RefSeq; NP_034700.2; NM_010570.4.
DR   UniGene; Mm.4952; -.
DR   PDB; 1AYB; X-ray; 3.00 A; P=887-898.
DR   PDBsum; 1AYB; -.
DR   ProteinModelPortal; P35569; -.
DR   SMR; P35569; 11-262.
DR   IntAct; P35569; 44.
DR   MINT; MINT-1540686; -.
DR   STRING; P35569; -.
DR   PhosphoSite; P35569; -.
DR   PRIDE; P35569; -.
DR   Ensembl; ENSMUST00000069799; ENSMUSP00000063795; ENSMUSG00000055980.
DR   GeneID; 16367; -.
DR   KEGG; mmu:16367; -.
DR   CTD; 16367; -.
DR   MGI; MGI:99454; Irs1.
DR   eggNOG; roNOG14058; -.
DR   HOGENOM; HBG443689; -.
DR   HOVERGEN; HBG000542; -.
DR   InParanoid; P35569; -.
DR   OrthoDB; EOG4J6RQG; -.
DR   ArrayExpress; P35569; -.
DR   Bgee; P35569; -.
DR   CleanEx; MM_IRS1; -.
DR   Genevestigator; P35569; -.
DR   GermOnline; ENSMUSG00000055980; Mus musculus.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005158; F:insulin receptor binding; ISS:UniProtKB.
DR   GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB.
DR   GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISS:UniProtKB.
DR   GO; GO:0042169; F:SH2 domain binding; ISS:UniProtKB.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0030879; P:mammary gland development; IGI:MGI.
DR   GO; GO:0030335; P:positive regulation of cell migration; IGI:MGI.
DR   GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IGI:MGI.
DR   GO; GO:0043491; P:protein kinase B signaling cascade; IGI:MGI.
DR   InterPro; IPR002404; Insln_rcpt_S1.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Pfam; PF02174; IRS; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00628; INSULINRSI.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00310; PTBI; 1.
DR   PROSITE; PS51064; IRS_PTB; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Phosphoprotein; Repeat; Transducer.
FT   CHAIN         1   1233       Insulin receptor substrate 1.
FT                                /FTId=PRO_0000084237.
FT   DOMAIN       12    115       PH.
FT   DOMAIN      155    259       IRS-type PTB.
FT   REGION        3    133       Mediates interaction with PHIP (By
FT                                similarity).
FT   REGION      891    893       GRB2-binding (By similarity).
FT   MOTIF       460    463       YXXM motif 1.
FT   MOTIF       546    549       YXXM motif 2.
FT   MOTIF       608    611       YXXM motif 3.
FT   MOTIF       628    631       YXXM motif 4.
FT   MOTIF       658    661       YXXM motif 5.
FT   MOTIF       727    730       YXXM motif 6.
FT   MOTIF       935    938       YXXM motif 7.
FT   MOTIF       983    986       YXXM motif 8.
FT   MOTIF      1006   1009       YXXM motif 9.
FT   COMPBIAS    675    680       Poly-Ser.
FT   COMPBIAS    872    877       Poly-Gln.
FT   COMPBIAS   1119   1128       Poly-Gly.
FT   COMPBIAS   1194   1198       Poly-Pro.
FT   MOD_RES       3      3       Phosphoserine.
FT   MOD_RES      46     46       Phosphotyrosine (By similarity).
FT   MOD_RES      99     99       Phosphoserine; by CK2 (By similarity).
FT   MOD_RES     307    307       Phosphoserine (By similarity).
FT   MOD_RES     324    324       Phosphoserine.
FT   MOD_RES     340    340       Phosphoserine.
FT   MOD_RES     343    343       Phosphoserine (By similarity).
FT   MOD_RES     460    460       Phosphotyrosine; by INSR (By similarity).
FT   MOD_RES     526    526       Phosphoserine (By similarity).
FT   MOD_RES     608    608       Phosphotyrosine; by INSR (By similarity).
FT   MOD_RES     628    628       Phosphotyrosine; by INSR (By similarity).
FT   MOD_RES     632    632       Phosphoserine (By similarity).
FT   MOD_RES     658    658       Phosphotyrosine (By similarity).
FT   MOD_RES     789    789       Phosphoserine; by SNF1LK2 (By
FT                                similarity).
FT   MOD_RES     891    891       Phosphotyrosine; by INSR (By similarity).
FT   MOD_RES     935    935       Phosphotyrosine; by INSR (By similarity).
FT   MOD_RES     983    983       Phosphotyrosine; by INSR (By similarity).
FT   MOD_RES    1074   1074       Phosphoserine (By similarity).
FT   MOD_RES    1097   1097       Phosphoserine (By similarity).
FT   MOD_RES    1139   1139       Phosphoserine.
FT   MOD_RES    1173   1173       Phosphotyrosine; by INSR (By similarity).
FT   MOD_RES    1214   1214       Phosphoserine.
FT   MOD_RES    1220   1220       Phosphotyrosine; by INSR (By similarity).
FT   CONFLICT   1038   1039       Missing (in Ref. 2).
FT   CONFLICT   1182   1182       H -> R (in Ref. 2; CAA49378).
SQ   SEQUENCE   1233 AA;  130723 MW;  C0E9B2D890DADD87 CRC64;
     MASPPDTDGF SDVRKVGYLR KPKSMHKRFF VLRAASEAGG PARLEYYENE KKWRHKSSAP
     KRSIPLESCF NINKRADSKN KHLVALYTRD EHFAIAADSE AEQDSWYQAL LQLHNRAKAH
     HDGAGGGCGG SCSGSSGVGE AGEDLSYDTG PGPAFKEVWQ VILKPKGLGQ TKNLIGIYRL
     CLTSKTISFV KLNSEAAAVV LQLMNIRRCG HSENFFFIEV GRSAVTGPGE FWMQVDDSVV
     AQNMHETILE AMRAMSDEFR PRSKSQSSSS CSNPISVPLR RHHLNNPPPS QVGLTRRSRT
     ESITATSPAS MVGGKPGSFR VRASSDGEGT MSRPASVDGS PVSPSTNRTH AHRHRGSSRL
     HPPLNHSRSI PMPSSRCSPS ATSPVSLSSS STSGHGSTSD CLFPRRSSAS VSGSPSDGGF
     ISSDEYGSSP CDFRSSFRSV TPDSLGHTPP ARGEEELSNY ICMGGKGAST LAAPNGHYIL
     SRGGNGHRYI PGANLGTSPA LPGDEAAGAA DLDNRFRKRT HSAGTSPTIS HQKTPSQSSV
     ASIEEYTEMM PAAYPPGGGS GGRLPGYRHS AFVPTHSYPE EGLEMHHLER RGGHHRPDTS
     NLHTDDGYMP MSPGVAPVPS NRKGNGDYMP MSPKSVSAPQ QIINPIRRHP QRVDPNGYMM
     MSPSGSCSPD IGGGSSSSSS ISAAPSGSSY GKPWTNGVGG HHTHALPHAK PPVESGGGKL
     LPCTGDYMNM SPVGDSNTSS PSECYYGPED PQHKPVLSYY SLPRSFKHTQ RPGEPEEGAR
     HQHLRLSSSS GRLRYTATAE DSSSSTSSDS LGGGYCGARP ESSLTHPHHH VLQPHLPRKV
     DTAAQTNSRL ARPTRLSLGD PKASTLPRVR EQQQQQQSSL HPPEPKSPGE YVNIEFGSGQ
     PGYLAGPATS RSSPSVRCPP QLHPAPREET GSEEYMNMDL GPGRRATWQE SGGVELGRIG
     PAPPGSATVC RPTRSVPNSR GDYMTMQIGC PRQSYVDTSP VAPVSYADMR TGIAAEKASL
     PRPTGAAPPP SSTASSSASV TPQGATAEQA THSSLLGGPQ GPGGMSAFTR VNLSPNHNQS
     AKVIRADTQG CRRRHSSETF SAPTRAGNTV PFGAGAAVGG SGGGGGGGSE DVKRHSSASF
     ENVWLRPGDL GGVSKESAPV CGAAGGLEKS LNYIDLDLAK EHSQDCPSQQ QSLPPPPPHQ
     PLGSNEGNSP RRSSEDLSNY ASISFQKQPE DRQ
//
ID   RFC1_MOUSE              Reviewed;        1131 AA.
AC   P35601;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   08-MAR-2011, entry version 106.
DE   RecName: Full=Replication factor C subunit 1;
DE   AltName: Full=A1-P145;
DE   AltName: Full=Activator 1 140 kDa subunit;
DE            Short=A1 140 kDa subunit;
DE   AltName: Full=Activator 1 large subunit;
DE   AltName: Full=Activator 1 subunit 1;
DE   AltName: Full=Differentiation-specific element-binding protein;
DE   AltName: Full=ISRE-binding protein;
DE   AltName: Full=Replication factor C 140 kDa subunit;
DE            Short=RF-C 140 kDa subunit;
DE            Short=RFC140;
DE   AltName: Full=Replication factor C large subunit;
GN   Name=Rfc1; Synonyms=Ibf-1, Recc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c;
RX   MEDLINE=94089669; PubMed=8265586; DOI=10.1073/pnas.90.24.11543;
RA   Burbelo P.D., Utani A., Pan Z., Yamada Y.;
RT   "Cloning of the large subunit of activator 1 (replication factor C)
RT   reveals homology with bacterial DNA ligases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:11543-11547(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RX   MEDLINE=94158835; PubMed=8114700;
RA   Luckow B., Bunz F., Stillman B., Lichter P., Schuetz G.;
RT   "Cloning, expression, and chromosomal localization of the 140-
RT   kilodalton subunit of replication factor C from mice and humans.";
RL   Mol. Cell. Biol. 14:1626-1634(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=Swiss;
RX   MEDLINE=95388065; PubMed=7659092; DOI=10.1210/me.9.4.487;
RA   McGehee Habener J.F.;
RT   "Differentiation-specific element binding protein (DSEB) binds to a
RT   defined element in the promoter of the angiotensinogen gene required
RT   for the irreversible induction of gene expression during
RT   differentiation of 3T3-L1 adipoblasts to adipocytes.";
RL   Mol. Endocrinol. 9:487-501(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Haque S.J.;
RL   Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-565.
RC   STRAIN=LAF1;
RA   Lossie A.C., Haugen B.H., Wood W.M., Camper S.A., Gordon D.F.;
RL   Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 354-528.
RX   MEDLINE=90229765; PubMed=1691767;
RA   Haque S.J., Kumar A., Fischer T., Rutherford M.N., Williams B.R.;
RT   "Evaluation of inter- and intramolecular primary structure homologies
RT   of interferons by a Monte Carlo method.";
RL   J. Interferon Res. 10:31-31(1990).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; SER-70; SER-107;
RP   THR-109 AND SER-244, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: The elongation of primed DNA templates by DNA polymerase
CC       delta and epsilon requires the action of the accessory proteins
CC       PCNA and activator 1. This subunit binds to the primer-template
CC       junction.
CC   -!- SUBUNIT: Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that
CC       can form a complex either with RFC1 or with RAD17. The former
CC       interacts with PCNA in the presence of ATP, while the latter has
CC       ATPase activity but is not stimulated by PCNA (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P35601-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P35601-2; Sequence=VSP_008444;
CC         Note=Alternative use of an acceptor site;
CC   -!- SIMILARITY: Belongs to the activator 1 large subunit family.
CC   -!- SIMILARITY: Contains 1 BRCT domain.
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DR   EMBL; U01222; AAA21643.1; -; mRNA.
DR   EMBL; X72711; CAA51260.1; -; mRNA.
DR   EMBL; U36441; AAA79698.1; -; mRNA.
DR   EMBL; U07157; AAC52140.1; -; mRNA.
DR   EMBL; U15037; AAB60452.1; -; mRNA.
DR   IPI; IPI00378168; -.
DR   IPI; IPI00896013; -.
DR   PIR; A49393; A49393.
DR   RefSeq; NP_035388.2; NM_011258.2.
DR   UniGene; Mm.148877; -.
DR   ProteinModelPortal; P35601; -.
DR   SMR; P35601; 389-493, 567-809.
DR   STRING; P35601; -.
DR   PhosphoSite; P35601; -.
DR   PRIDE; P35601; -.
DR   Ensembl; ENSMUST00000031092; ENSMUSP00000031092; ENSMUSG00000029191.
DR   GeneID; 19687; -.
DR   KEGG; mmu:19687; -.
DR   UCSC; uc008xni.1; mouse.
DR   UCSC; uc008xnj.1; mouse.
DR   CTD; 19687; -.
DR   MGI; MGI:97891; Rfc1.
DR   eggNOG; roNOG12673; -.
DR   HOVERGEN; HBG004167; -.
DR   InParanoid; P35601; -.
DR   OrthoDB; EOG4D26P3; -.
DR   PhylomeDB; P35601; -.
DR   ArrayExpress; P35601; -.
DR   Bgee; P35601; -.
DR   CleanEx; MM_RFC1; -.
DR   Genevestigator; P35601; -.
DR   GermOnline; ENSMUSG00000029191; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003689; F:DNA clamp loader activity; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR001357; BRCT.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR012178; DNA_replication_fac_C_lsu.
DR   InterPro; IPR013725; DNA_replication_fac_RFC1_C.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF08519; RFC1; 1.
DR   PIRSF; PIRSF036578; RFC1; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SUPFAM; SSF52113; BRCT; 1.
DR   SUPFAM; SSF48019; Pol_clamp_load_C; 1.
DR   PROSITE; PS50172; BRCT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Alternative splicing; ATP-binding;
KW   DNA replication; DNA-binding; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Transcription; Transcription regulation.
FT   CHAIN         1   1131       Replication factor C subunit 1.
FT                                /FTId=PRO_0000121773.
FT   DOMAIN      399    489       BRCT.
FT   NP_BIND     635    642       ATP (By similarity).
FT   REGION      354    528       Interferon-stimulated-response-element
FT                                binding region.
FT   MOTIF      1104   1108       Nuclear localization signal (Potential).
FT   MOD_RES      66     66       Phosphotyrosine (By similarity).
FT   MOD_RES      68     68       Phosphoserine.
FT   MOD_RES      70     70       Phosphoserine.
FT   MOD_RES      72     72       Phosphoserine (By similarity).
FT   MOD_RES     107    107       Phosphoserine.
FT   MOD_RES     109    109       Phosphothreonine.
FT   MOD_RES     155    155       Phosphoserine (By similarity).
FT   MOD_RES     160    160       Phosphothreonine (By similarity).
FT   MOD_RES     162    162       Phosphothreonine (By similarity).
FT   MOD_RES     163    163       Phosphoserine (By similarity).
FT   MOD_RES     170    170       Phosphothreonine (By similarity).
FT   MOD_RES     172    172       Phosphoserine (By similarity).
FT   MOD_RES     189    189       Phosphoserine (By similarity).
FT   MOD_RES     244    244       Phosphoserine.
FT   MOD_RES     281    281       Phosphoserine (By similarity).
FT   MOD_RES     309    309       Phosphoserine (By similarity).
FT   MOD_RES     618    618       N6-acetyllysine (By similarity).
FT   MOD_RES     654    654       Phosphotyrosine (By similarity).
FT   MOD_RES     656    656       Phosphotyrosine (By similarity).
FT   VAR_SEQ     614    614       Missing (in isoform 2).
FT                                /FTId=VSP_008444.
FT   CONFLICT     66     66       Y -> N (in Ref. 3; AAA79698).
FT   CONFLICT    187    187       E -> EPDFCLSCLIFFGIQ (in Ref. 4;
FT                                AAC52140).
FT   CONFLICT    254    254       V -> A (in Ref. 5; AAB60452).
FT   CONFLICT    559    559       N -> S (in Ref. 4; AAC52140).
FT   CONFLICT    945    945       S -> N (in Ref. 1; AAA21643).
FT   CONFLICT   1071   1071       T -> A (in Ref. 3; AAA79698).
FT   CONFLICT   1104   1104       K -> KQ (in Ref. 4; AAC52140).
SQ   SEQUENCE   1131 AA;  125985 MW;  A6F4F970A7F9EE94 CRC64;
     MDIRKFFGVI SSGKKPVNET VKNEKTKASE GTVKGKKGVK EAKVNNSGKE DASKPKQHSK
     KKRIIYDSDS ESEETVQVKN AKKKSEKLSL SYKPGKVSQK DPVTYVSETD EDDDFVCKKA
     ASKSKENGVS TNSYLGTSNV KKNEENVKTK NKPLSPIKLT PTSVLDYFGT ESVQRSGKKM
     VTSKRKESSQ NTEDSRLNDE AIAKQLQLDE DAELERQLHE DEEFARTLAL LDEEPKIKKA
     RKDSEEGEES FSSVQDDLSK AEKQKSPNKA ELFSTARKTY SPAKHGKGRA SEDAKQPCKS
     AHRKEACSSP KASAKLALMK AKEESSYNET ELLAARRKES ATEPKGEKTT PKKTKVSPTK
     RESVSPEDSE KKRTNYQAYR SYLNREGPKA LGSKEIPKGA ENCLEGLTFV ITGVLESIER
     DEAKSLIERY GGKVTGNVSK KTNYLVMGRD SGQSKSDKAA ALGTKILDED GLLDLIRTMP
     GKRSKYEMAA EAEMKKEKSK LERTPQKNDQ GKRKISPAKK ESESKKCKLT LLKNSPMKAV
     KKEASTCPRG LDVKETHGNR SSNKEECLLW VDKYKPASLK NIIGQQGDQS CANKLLRWLR
     NWHKSSPEEK KHAAKFGKLA SKDDGSSFKA ALLSGPPGVG KTTTASLVCQ ELGYSYVELN
     ASDTRSKNSL KAVVAESLNN TSIKGFYTSG AAPSVSARHA LIMDEVDGMA GNEDRGGIQE
     LIGLIKHTKI PIICMCNDRN HPKIRSLVHY CFDLRFQRPR VEQIKSAMLS IAFKEGLKIP
     PPAMNEIILG ANQDVRQVLH NLSMWCAQSK ALTYDQAKAD SQRAKKDIRL GPFDVTRKVF
     AAGEETAHMS LMDKSDLFFH DYSIAPLFVQ ENYLHVKPVA AGGDMKKHLM LLSRAADSIC
     DGDLVDNQIR SKQNWSLLPT QAIYASVLPG ELMRGYMTQF PSFPSWLGKH SSTGKHDRIV
     QDLSLHMSLR TYSSKRTVNM DYLSHIRDAL VRPLTSQGVE GAQHVIKLMD TYYLMKEDFE
     NIMEVSSWGG KPSAFSKLDP KVKAAFTRAY NKEAHLTPYS LQVVKTSRLS TGPALDSEYS
     EEFQEDDTQS EKEQDAVETD AMIKKKTRSS KPSKSEREKE SKKGKGKNWK K
//
ID   ERCC5_MOUSE             Reviewed;        1170 AA.
AC   P35689; Q61528; Q64248;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 3.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=DNA repair protein complementing XP-G cells homolog;
DE            EC=3.1.-.-;
DE   AltName: Full=DNA excision repair protein ERCC-5;
DE   AltName: Full=Xeroderma pigmentosum group G-complementing protein homolog;
GN   Name=Ercc5; Synonyms=Ercc-5, Xpg;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94173288; PubMed=7510366; DOI=10.1016/0921-8777(94)90080-9;
RA   Shiomi T., Harada Y.-N., Saito T., Shiomi N., Okuno Y., Yamaizumi M.;
RT   "An ERCC5 gene with homology to yeast RAD2 is involved in group G
RT   Xeroderma pigmentosum.";
RL   Mutat. Res. 314:167-175(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/10; TISSUE=Liver;
RX   MEDLINE=96070433; PubMed=7590748; DOI=10.1006/geno.1995.1106;
RA   Harada Y.N., Matsuda Y., Shiomi N., Shiomi T.;
RT   "Complementary DNA sequence and chromosomal localization of xpg, the
RT   mouse counterpart of human repair gene XPG/ERCC5.";
RL   Genomics 28:59-65(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=DBA/2;
RX   MEDLINE=96359149; PubMed=8703115; DOI=10.1007/s003359900198;
RA   Ludwig D.L., Mudgett J.S., Park M.S., Perez-Castro A.V.,
RA   Macinnes M.A.;
RT   "Molecular cloning and structural analysis of the functional mouse
RT   genomic XPG gene.";
RL   Mamm. Genome 7:644-649(1996).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-704 AND SER-705, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Single-stranded structure-specific DNA endonuclease
CC       involved in DNA excision repair. Makes the 3'incision in DNA
CC       nucleotide excision repair (NER). Acts as a cofactor for a DNA
CC       glycosylase that removes oxidized pyrimidines from DNA. May also
CC       be involved in transcription-coupled repair of this kind of
CC       damage, in transcription by RNA polymerase II, and perhaps in
CC       other processes too (By similarity).
CC   -!- COFACTOR: Binds 2 magnesium ions per subunit. They probably
CC       participate in the reaction catalyzed by the enzyme. May bind an
CC       additional third magnesium ion after substrate binding (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with PCNA (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. XPG
CC       subfamily.
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DR   EMBL; D16306; BAA03813.1; -; mRNA.
DR   EMBL; U40796; AAA91039.1; -; mRNA.
DR   EMBL; U40795; AAB17885.1; -; Genomic_DNA.
DR   EMBL; U39892; AAB17885.1; JOINED; Genomic_DNA.
DR   EMBL; U39893; AAB17885.1; JOINED; Genomic_DNA.
DR   EMBL; U39894; AAB17885.1; JOINED; Genomic_DNA.
DR   EMBL; U39896; AAB17885.1; JOINED; Genomic_DNA.
DR   EMBL; U40073; AAB17885.1; JOINED; Genomic_DNA.
DR   EMBL; U40431; AAB17885.1; JOINED; Genomic_DNA.
DR   EMBL; U40432; AAB17885.1; JOINED; Genomic_DNA.
DR   EMBL; U40668; AAB17885.1; JOINED; Genomic_DNA.
DR   EMBL; U40669; AAB17885.1; JOINED; Genomic_DNA.
DR   EMBL; U40670; AAB17885.1; JOINED; Genomic_DNA.
DR   EMBL; U40792; AAB17885.1; JOINED; Genomic_DNA.
DR   EMBL; U40793; AAB17885.1; JOINED; Genomic_DNA.
DR   EMBL; U40794; AAB17885.1; JOINED; Genomic_DNA.
DR   IPI; IPI00310463; -.
DR   PIR; A57650; A57650.
DR   UniGene; Mm.2213; -.
DR   ProteinModelPortal; P35689; -.
DR   SMR; P35689; 756-997.
DR   STRING; P35689; -.
DR   PhosphoSite; P35689; -.
DR   PRIDE; P35689; -.
DR   Ensembl; ENSMUST00000027214; ENSMUSP00000027214; ENSMUSG00000026048.
DR   MGI; MGI:103582; Ercc5.
DR   eggNOG; roNOG08442; -.
DR   HOGENOM; HBG402878; -.
DR   HOVERGEN; HBG051501; -.
DR   InParanoid; P35689; -.
DR   OrthoDB; EOG4CNQQZ; -.
DR   PhylomeDB; P35689; -.
DR   ArrayExpress; P35689; -.
DR   Bgee; P35689; -.
DR   Genevestigator; P35689; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008340; P:determination of adult lifespan; IMP:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR   GO; GO:0009650; P:UV protection; IDA:MGI.
DR   InterPro; IPR020045; 5-3_exonuclease_C.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR006086; XPG/RAD2_endonuclease.
DR   InterPro; IPR019974; XPG_CS.
DR   InterPro; IPR006085; XPG_DNA_repair_N.
DR   InterPro; IPR001044; XPGC_DNA_repair.
DR   InterPro; IPR006084; XPGC_Rad_DNA_repair.
DR   PANTHER; PTHR11081:SF1; XPGC_DNA_repair; 1.
DR   PANTHER; PTHR11081; XPGC_Rad; 1.
DR   Pfam; PF00867; XPG_I; 1.
DR   Pfam; PF00752; XPG_N; 1.
DR   PRINTS; PR00853; XPGRADSUPER.
DR   PRINTS; PR00066; XRODRMPGMNTG.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00484; XPGI; 1.
DR   SMART; SM00485; XPGN; 1.
DR   SUPFAM; SSF47807; 5_3_exo_C; 1.
DR   TIGRFAMs; TIGR00600; rad2; 1.
DR   PROSITE; PS00841; XPG_1; 1.
DR   PROSITE; PS00842; XPG_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; DNA damage; DNA repair; DNA-binding; Endonuclease;
KW   Hydrolase; Magnesium; Metal-binding; Nuclease; Nucleus;
KW   Phosphoprotein.
FT   CHAIN         1   1170       DNA repair protein complementing XP-G
FT                                cells homolog.
FT                                /FTId=PRO_0000154032.
FT   REGION        1     95       N-domain.
FT   REGION      752    882       I-domain.
FT   MOTIF      1049   1065       Nuclear localization signal (Potential).
FT   METAL        30     30       Magnesium 1 (By similarity).
FT   METAL        77     77       Magnesium 1 (By similarity).
FT   METAL       788    788       Magnesium 1 (By similarity).
FT   METAL       790    790       Magnesium 1 (By similarity).
FT   METAL       809    809       Magnesium 2 (By similarity).
FT   METAL       811    811       Magnesium 2 (By similarity).
FT   METAL       860    860       Magnesium 2 (By similarity).
FT   MOD_RES       8      8       N6-acetyllysine (By similarity).
FT   MOD_RES     156    156       Phosphoserine (By similarity).
FT   MOD_RES     157    157       Phosphoserine (By similarity).
FT   MOD_RES     341    341       Phosphoserine (By similarity).
FT   MOD_RES     355    355       Phosphoserine (By similarity).
FT   MOD_RES     356    356       Phosphoserine (By similarity).
FT   MOD_RES     357    357       Phosphoserine (By similarity).
FT   MOD_RES     382    382       Phosphoserine (By similarity).
FT   MOD_RES     384    384       Phosphoserine (By similarity).
FT   MOD_RES     418    418       Phosphoserine (By similarity).
FT   MOD_RES     429    429       Phosphothreonine (By similarity).
FT   MOD_RES     568    568       Phosphoserine (By similarity).
FT   MOD_RES     571    571       Phosphoserine (By similarity).
FT   MOD_RES     572    572       Phosphoserine (By similarity).
FT   MOD_RES     704    704       Phosphoserine.
FT   MOD_RES     705    705       Phosphoserine.
FT   VARIANT     388    388       R -> C (in strain: DBA/2).
FT   VARIANT     488    488       S -> R (in strain: DBA/2).
FT   VARIANT     688    688       I -> T (in strain: DBA/2).
FT   VARIANT    1015   1015       S -> N (in strain: DBA/2).
FT   VARIANT    1021   1021       M -> I (in strain: DBA/2).
FT   VARIANT    1121   1121       S -> P (in strain: DBA/2).
FT   CONFLICT    227    227       N -> M (in Ref. 1).
FT   CONFLICT    249    249       N -> M (in Ref. 1).
FT   CONFLICT    300    302       VMD -> MDE (in Ref. 1).
FT   CONFLICT    313    313       N -> M (in Ref. 1).
FT   CONFLICT    320    320       N -> M (in Ref. 1).
FT   CONFLICT    399    399       N -> M (in Ref. 1).
FT   CONFLICT    408    408       D -> DVQTGG (in Ref. 1).
FT   CONFLICT    581    581       N -> NSASEVIGPV (in Ref. 1).
FT   CONFLICT    795    795       M -> V (in Ref. 1).
FT   CONFLICT   1039   1039       A -> AMEKEFEL (in Ref. 1).
FT   CONFLICT   1134   1134       S -> SD (in Ref. 1).
FT   CONFLICT   1157   1158       KL -> RR (in Ref. 1).
SQ   SEQUENCE   1170 AA;  130858 MW;  41E2FACE47167A57 CRC64;
     MGVQGLWKLL ECSGHRVSPE ALEGKVLAVD ISIWLNQALK GVRDSHGNVI ENAHLLTLFH
     RLCKLLFFRI RPIFVFDGDA PLLKKQTLAK RRQRKDSASI DSRKTTEKLL KTFLKRQALK
     TAFRSSRHEA PPSLTQVQRQ DDIYVLPPLP EEEKHSSEEE DEKQWQARMD QKQALQEEFF
     HNPQAIDIES EDFSSLPPEV KHEILTDMKE FTKRRRTLFE AMPEESNDFS QYQLKGLLKK
     NYLNQHIENV QKEMNQQHSG QIQRQYQDEG GFLKEVESRR VVSEDTSHYI LIKGIQGKKV
     MDVDSESLPS SSNVHSVSSN LKSSPHEKVK PEREPEAAPP SPRTLLAIQA AMLGSSSEDE
     PESREGRQSK ERNSGATADA GSISPRTRAA IQKALDDDND EKVSGSSDDL AEKMLLGSRL
     EQEEHADETA ERGGGVPFDT APLTPSVTEV KECVTSGSSA NEQTDSAHSF TTASHRCDTP
     KETVSLASAV KEASQISSEC EVEGRPAALS PAFIGTPSSH VSGVLSEREP TLAPPTTRTH
     SDQGIDIHPE DPELQNGLYP LETKCNSSRL SSDDETEGGQ NPAPKACSTV HVPAEAMSNL
     ENALPSNAEE RGDFQETIQL REVPEAAARE LISAPKPMGP MEMESEESES DGSFIEVQSV
     VSNSELQTES SEASTHLSEK DAEEPREILE EGTSRDTECL LQDSSDIEAM EGHREADIDA
     EDMPNEWQDI NLEELDALES NLLAEQNSLK AQKQQQDRIA ASVTGQMFLE SQELLRLFGV
     PYIQAPMEAE AQCAMLDLSD QTSGTITDDS DIWLFGARHV YKNFFNKNKF VEYYQYVDFY
     SQLGLDRNKL INLAYLLGSD YTEGIPTVGC VTAMEILNEF PGRGLDPLLK FSEWWHEAQN
     NKKVAENPYD TKVKKKLRKL QLTPGFPNPA VADAYLRPVV DDSRGSFLWG KPDVDKIREF
     CQRYFGWNRM KTDESLYPVL KHLNAHQTQL RIDSFFRLAQ QEKQDAKLIK SHRLSRAVTC
     MLRKEREEKA PELTKVTEAL DDAKGKTQKR ELPYKKETSV PKRRRPSGNG GFLGDPYCSE
     SPQESSCEDG EGSSVMSARQ RSAAESSKIG CSDVPDLVRD SPHGRQGCVS TSSSSEDGED
     KAKTVLVTAR PVFGKKKLKL KSMKRRKKKT
//
ID   GPM6A_MOUSE             Reviewed;         278 AA.
AC   P35802;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Neuronal membrane glycoprotein M6-a;
DE            Short=M6a;
GN   Name=Gpm6a; Synonyms=M6a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 67-78.
RC   TISSUE=Brain;
RX   MEDLINE=94000809; PubMed=8398137; DOI=10.1016/0896-6273(93)90147-J;
RA   Yan Y., Lagenaur C., Narayanan V.;
RT   "Molecular cloning of M6: identification of a PLP/DM20 gene family.";
RL   Neuron 11:423-431(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, Eye, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 13-20; 67-82; 112-118; 179-200 AND 256-269, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Widely expressed in the CNS. Found especially
CC       in the granule cell layer of the cerebellum but not in the
CC       molecular layer or white matter.
CC   -!- DEVELOPMENTAL STAGE: First detected in presumptive postmitotic
CC       neurons in the developing neural tube at embryonic day 9.
CC   -!- SIMILARITY: Belongs to the myelin proteolipid protein family.
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DR   EMBL; S65735; AAB28350.1; -; mRNA.
DR   EMBL; BC024759; AAH24759.1; -; mRNA.
DR   EMBL; BC029683; AAH29683.1; -; mRNA.
DR   EMBL; BC029711; AAH29711.1; -; mRNA.
DR   EMBL; BC033357; AAH33357.1; -; mRNA.
DR   EMBL; BC033394; AAH33394.1; -; mRNA.
DR   EMBL; BC043130; AAH43130.1; -; mRNA.
DR   IPI; IPI00122974; -.
DR   RefSeq; NP_705809.1; NM_153581.5.
DR   UniGene; Mm.241700; -.
DR   STRING; P35802; -.
DR   TCDB; 9.B.38.1.1; myelin proteolipid protein (MPLP) family.
DR   PhosphoSite; P35802; -.
DR   PRIDE; P35802; -.
DR   Ensembl; ENSMUST00000033915; ENSMUSP00000033915; ENSMUSG00000031517.
DR   GeneID; 234267; -.
DR   KEGG; mmu:234267; -.
DR   UCSC; uc009lsl.1; mouse.
DR   CTD; 234267; -.
DR   MGI; MGI:107671; Gpm6a.
DR   eggNOG; roNOG09615; -.
DR   HOGENOM; HBG714762; -.
DR   HOVERGEN; HBG000096; -.
DR   InParanoid; P35802; -.
DR   OMA; TICRNAT; -.
DR   OrthoDB; EOG4KSPKC; -.
DR   NextBio; 382077; -.
DR   ArrayExpress; P35802; -.
DR   Bgee; P35802; -.
DR   CleanEx; MM_GPM6A; -.
DR   Genevestigator; P35802; -.
DR   GermOnline; ENSMUSG00000031517; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR001614; Myelin_PLP.
DR   InterPro; IPR018237; Myelin_PLP_CS.
DR   PANTHER; PTHR11683; Myelin_PLP; 1.
DR   Pfam; PF01275; Myelin_PLP; 1.
DR   PRINTS; PR00214; MYELINPLP.
DR   SMART; SM00002; PLP; 1.
DR   PROSITE; PS00575; MYELIN_PLP_1; 1.
DR   PROSITE; PS01004; MYELIN_PLP_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    278       Neuronal membrane glycoprotein M6-a.
FT                                /FTId=PRO_0000159019.
FT   TOPO_DOM      1     22       Cytoplasmic (Potential).
FT   TRANSMEM     23     43       Helical; (Potential).
FT   TOPO_DOM     44     84       Extracellular (Potential).
FT   TRANSMEM     85    105       Helical; (Potential).
FT   TOPO_DOM    106    127       Cytoplasmic (Potential).
FT   TRANSMEM    128    148       Helical; (Potential).
FT   TOPO_DOM    149    213       Extracellular (Potential).
FT   TRANSMEM    214    234       Helical; (Potential).
FT   TOPO_DOM    235    278       Cytoplasmic (Potential).
FT   MOD_RES     267    267       Phosphoserine (By similarity).
FT   CARBOHYD    164    164       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    208    208       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   278 AA;  31149 MW;  CEE0688873E786CE CRC64;
     MEENMEEGQT QKGCFECCIK CLGGIPYASL IATILLYAGV ALFCGCGHEA LSGTVNILQT
     YFELARTAGD TLDVFTMIDI FKYVIYGIAA AFFVYGILLM VEGFFTTGAI KDLYGDFKIT
     TCGRCVSAWF IMLTYLFMLA WLGVTAFTSL PVYMYFNVWT ICRNTTLVEG ANLCLDLRQF
     GIVTIGEEKK ICTASENFLR MCESTELNMT FHLFIVALAG AGAAVIAMVH YLMVLSANWA
     YVKDACRMQK YEDIKSKEEQ ELHDIHSTRS KERLNAYT
//
ID   PTN1_MOUSE              Reviewed;         432 AA.
AC   P35821; Q60840; Q62131; Q64498; Q99JS1;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   08-MAR-2011, entry version 116.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type 1;
DE            EC=3.1.3.48;
DE   AltName: Full=Protein-tyrosine phosphatase 1B;
DE            Short=PTP-1B;
DE   AltName: Full=Protein-tyrosine phosphatase HA2;
DE            Short=PTP-HA2;
GN   Name=Ptpn1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92032882; PubMed=1932742;
RA   Yi T., Cleveland J.L., Ihle J.N.;
RT   "Identification of novel protein tyrosine phosphatases of
RT   hematopoietic cells by polymerase chain reaction amplification.";
RL   Blood 78:2222-2228(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   MEDLINE=92328784; PubMed=1378268; DOI=10.1016/0006-291X(92)91700-Z;
RA   Miyasaka H., Li S.S.L.;
RT   "The cDNA cloning, nucleotide sequence and expression of an
RT   intracellular protein tyrosine phosphatase from mouse testis.";
RL   Biochem. Biophys. Res. Commun. 185:818-825(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Liao K., Lane M.D.;
RL   Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Park K., Byun S.;
RL   Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 102-213.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=95134232; PubMed=7832766;
RA   Hendriks W., Schepens J., Brugman C., Zeeuwen P., Wieringa B.;
RT   "A novel receptor-type protein tyrosine phosphatase with a single
RT   catalytic domain is specifically expressed in mouse brain.";
RL   Biochem. J. 305:499-504(1995).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May play an important role in CKII- and p60c-src-induced
CC       signal transduction cascades (By similarity).
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein; Cytoplasmic side (By similarity).
CC   -!- TISSUE SPECIFICITY: Most abundant in testis. Also found in kidney,
CC       spleen, muscle, liver, heart and brain.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class 1 subfamily.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; M97590; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; L40595; AAA64615.1; -; mRNA.
DR   EMBL; U24700; AAA98605.1; -; mRNA.
DR   EMBL; Z23057; CAA80592.1; -; mRNA.
DR   EMBL; BC005729; AAH05729.1; -; mRNA.
DR   EMBL; BC010191; AAH10191.1; -; mRNA.
DR   IPI; IPI00123039; -.
DR   PIR; JN0317; JN0317.
DR   RefSeq; NP_035331.3; NM_011201.3.
DR   UniGene; Mm.277916; -.
DR   ProteinModelPortal; P35821; -.
DR   SMR; P35821; 2-283.
DR   MINT; MINT-5313580; -.
DR   STRING; P35821; -.
DR   PhosphoSite; P35821; -.
DR   PRIDE; P35821; -.
DR   Ensembl; ENSMUST00000029053; ENSMUSP00000029053; ENSMUSG00000027540.
DR   GeneID; 19246; -.
DR   KEGG; mmu:19246; -.
DR   UCSC; uc008oaj.1; mouse.
DR   CTD; 19246; -.
DR   MGI; MGI:97805; Ptpn1.
DR   eggNOG; roNOG10703; -.
DR   HOGENOM; HBG444576; -.
DR   HOVERGEN; HBG008321; -.
DR   InParanoid; P35821; -.
DR   OMA; AYLCYRV; -.
DR   OrthoDB; EOG418BND; -.
DR   PhylomeDB; P35821; -.
DR   BRENDA; 3.1.3.48; 244.
DR   NextBio; 296070; -.
DR   ArrayExpress; P35821; -.
DR   Bgee; P35821; -.
DR   CleanEx; MM_PTPN1; -.
DR   Genevestigator; P35821; -.
DR   GermOnline; ENSMUSG00000027540; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IMP:MGI.
DR   GO; GO:0006470; P:protein dephosphorylation; IMP:MGI.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR012265; Tyr_Pase_non-rcpt_typ-1/2.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   PANTHER; PTHR19134:SF57; Tyr_Phos_no_rcpt; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PIRSF; PIRSF000926; Tyr-Ptase_nr1; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Hydrolase; Membrane; Phosphoprotein;
KW   Protein phosphatase.
FT   CHAIN         1    432       Tyrosine-protein phosphatase non-receptor
FT                                type 1.
FT                                /FTId=PRO_0000094749.
FT   DOMAIN        3    277       Tyrosine-protein phosphatase.
FT   REGION      215    221       Substrate binding (By similarity).
FT   ACT_SITE    215    215       Phosphocysteine intermediate (By
FT                                similarity).
FT   BINDING     181    181       Substrate (By similarity).
FT   BINDING     262    262       Substrate (By similarity).
FT   MOD_RES      20     20       Phosphotyrosine (By similarity).
FT   MOD_RES      50     50       Phosphoserine (By similarity).
FT   MOD_RES     295    295       Phosphoserine (By similarity).
FT   MOD_RES     392    392       Phosphoserine.
FT   CONFLICT     48     48       D -> Y (in Ref. 2; M97590).
FT   CONFLICT    104    104       S -> P (in Ref. 2).
FT   CONFLICT    173    173       H -> P (in Ref. 3; AAA64615).
FT   CONFLICT    266    267       QL -> HV (in Ref. 3; AAA64615).
FT   CONFLICT    405    405       H -> K (in Ref. 2).
SQ   SEQUENCE   432 AA;  49593 MW;  4843D2DD4C288C48 CRC64;
     MEMEKEFEEI DKAGNWAAIY QDIRHEASDF PCKVAKLPKN KNRNRYRDVS PFDHSRIKLH
     QEDNDYINAS LIKMEEAQRS YILTQGPLPN TCGHFWEMVW EQKSRGVVML NRIMEKGSLK
     CAQYWPQQEE KEMVFDDTGL KLTLISEDVK SYYTVRQLEL ENLTTKETRE ILHFHYTTWP
     DFGVPESPAS FLNFLFKVRE SGSLSLEHGP IVVHCSAGIG RSGTFCLADT CLLLMDKRKD
     PSSVDIKKVL LEMRRFRMGL IQTADQLRFS YLAVIEGAKF IMGDSSVQDQ WKELSREDLD
     LPPEHVPPPP RPPKRTLEPH NGKCKELFSS HQWVSEETCG DEDSLAREEG RAQSSAMHSV
     SSMSPDTEVR RRMVGGGLQS AQASVPTEEE LSSTEEEHKA HWPSHWKPFL VNVCMATLLA
     TGAYLCYRVC FH
//
ID   PTN12_MOUSE             Reviewed;         775 AA.
AC   P35831;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type 12;
DE            EC=3.1.3.48;
DE   AltName: Full=MPTP-PEST;
DE   AltName: Full=Protein-tyrosine phosphatase P19;
DE            Short=P19-PTP;
GN   Name=Ptpn12;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92272714; PubMed=1590786; DOI=10.1016/S0006-291X(05)80015-4;
RA   den Hertog J., Pals C.E., Jonk L.J., Kruijer W.;
RT   "Differential expression of a novel murine non-receptor protein
RT   tyrosine phosphatase during differentiation of P19 embryonal carcinoma
RT   cells.";
RL   Biochem. Biophys. Res. Commun. 184:1241-1249(1992).
RN   [2]
RP   SEQUENCE REVISION TO 297-416.
RX   MEDLINE=93112015; PubMed=1472029; DOI=10.1016/0006-291X(92)92335-U;
RA   Takekawa M., Itoh F., Hinoda Y., Arimura Y., Toyota M., Sekiya M.,
RA   Adachi M., Imai K., Yachi A.;
RT   "Cloning and characterization of a human cDNA encoding a novel
RT   putative cytoplasmic protein-tyrosine-phosphatase.";
RL   Biochem. Biophys. Res. Commun. 189:1223-1230(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=95289971; PubMed=7772023;
RA   Charest A., Wagner J., Shen S.H., Tremblay M.L.;
RT   "Murine protein tyrosine phosphatase-PEST, a stable cytosolic protein
RT   tyrosine phosphatase.";
RL   Biochem. J. 308:425-432(1995).
RN   [4]
RP   INTERACTION WITH TGFB1I1.
RX   PubMed=10092676; DOI=10.1074/jbc.274.14.9847;
RA   Nishiya N., Iwabuchi Y., Shibanuma M., Cote J.-F., Tremblay M.L.,
RA   Nose K.;
RT   "Hic-5, a paxillin homologue, binds to the protein-tyrosine
RT   phosphatase PEST (PTP-PEST) through its LIM 3 domain.";
RL   J. Biol. Chem. 274:9847-9853(1999).
RN   [5]
RP   INTERACTION WITH PSTPIP1.
RX   PubMed=11711533; DOI=10.1074/jbc.M106428200;
RA   Cote J.-F., Chung P.L., Theberge J.-F., Halle M., Spencer S.,
RA   Lasky L.A., Tremblay M.L.;
RT   "PSTPIP is a substrate of PTP-PEST and serves as a scaffold guiding
RT   PTP-PEST toward a specific dephosphorylation of WASP.";
RL   J. Biol. Chem. 277:2973-2986(2002).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-748, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186 AND SER-673, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-596; THR-598; SER-603
RP   AND SER-608, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- SUBUNIT: Interacts with PSTPIP1 and TGFB1I1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class 4 subfamily.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; X63440; CAA45037.1; ALT_SEQ; mRNA.
DR   EMBL; X86781; CAA60477.1; -; Genomic_DNA.
DR   IPI; IPI00337948; -.
DR   PIR; JH0609; JH0609.
DR   PIR; S55345; S55345.
DR   UniGene; Mm.319117; -.
DR   ProteinModelPortal; P35831; -.
DR   SMR; P35831; 3-300.
DR   MINT; MINT-1486617; -.
DR   STRING; P35831; -.
DR   PRIDE; P35831; -.
DR   Ensembl; ENSMUST00000030556; ENSMUSP00000030556; ENSMUSG00000028771.
DR   MGI; MGI:104673; Ptpn12.
DR   eggNOG; roNOG07013; -.
DR   HOGENOM; HBG714475; -.
DR   HOVERGEN; HBG007666; -.
DR   InParanoid; P35831; -.
DR   OrthoDB; EOG42BX89; -.
DR   BRENDA; 3.1.3.48; 244.
DR   ArrayExpress; P35831; -.
DR   Bgee; P35831; -.
DR   Genevestigator; P35831; -.
DR   GermOnline; ENSMUSG00000028771; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR012266; Tyr_Pase_non-rcpt_typ-12.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PIRSF; PIRSF000932; Tyr-Ptase_nr12; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Hydrolase; Phosphoprotein;
KW   Protein phosphatase.
FT   CHAIN         1    775       Tyrosine-protein phosphatase non-receptor
FT                                type 12.
FT                                /FTId=PRO_0000094772.
FT   DOMAIN       28    293       Tyrosine-protein phosphatase.
FT   REGION      231    237       Substrate binding (By similarity).
FT   REGION      344    437       Interaction with TGFB1I1.
FT   ACT_SITE    231    231       Phosphocysteine intermediate (By
FT                                similarity).
FT   BINDING     199    199       Substrate (By similarity).
FT   BINDING     278    278       Substrate (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     186    186       Phosphoserine.
FT   MOD_RES     331    331       Phosphoserine (By similarity).
FT   MOD_RES     434    434       Phosphoserine.
FT   MOD_RES     467    467       Phosphoserine (By similarity).
FT   MOD_RES     519    519       Phosphothreonine (By similarity).
FT   MOD_RES     569    569       Phosphothreonine (By similarity).
FT   MOD_RES     588    588       Phosphoserine (By similarity).
FT   MOD_RES     596    596       Phosphoserine.
FT   MOD_RES     598    598       Phosphothreonine.
FT   MOD_RES     603    603       Phosphoserine.
FT   MOD_RES     608    608       Phosphoserine.
FT   MOD_RES     613    613       Phosphoserine (By similarity).
FT   MOD_RES     673    673       Phosphoserine.
FT   MOD_RES     748    748       Phosphoserine.
FT   CONFLICT    296    296       K -> N (in Ref. 1).
FT   CONFLICT    328    332       KQDSP -> DETS (in Ref. 1).
FT   CONFLICT    380    380       W -> V (in Ref. 1).
SQ   SEQUENCE   775 AA;  86992 MW;  7106D73F5014E411 CRC64;
     MEQVEILRRF IQRVQAMKSP DHNGEDNFAR DFMRLRRLST KYRTEKIYPT ATGEKEENVK
     KNRYKDILPF DHSRVKLTLK TPSQDSDYIN ANFIKGVYGP KAYVATQGPF RNTVIDFWRM
     IWEYNVVMIV MACREFEMGR KKCERYWPLY GEDPITFAPF KISCENEQAR TDYFIRTLLL
     EFQNESRRLY QFHYVNWPDH DVPSSFDSIL DMISLMRKYQ EHEDVPICIH CSAGCGRTGA
     ICAIDYTWNL LKAGKIPEEF NVFNLIQEMR TQRHSAVQTK EQYELVHRAI AQLFEKQLQL
     YEIHGAQKIR DGNEITTGTM VSSIDSEKQD SPPPKPPRTR SCLVEGDAKE EILQPPEPHP
     VPPILTPSPP SAFPTVTTVW QDSDRYHPKP VLHMASPEQH PADLNRSYDK SADQWGKSES
     AIEHIDKKLE RNLSFEIKKV PLQEGPKSFD GNTLLNRGHA IKIKSASSSV VDRTSKPQEL
     SAGALKVDDV SQNSCADCSA AHSHRAAESS EESQSNSHTP PRPDCLPLDK KGHVTWSLHG
     PENATPVPDS PDGKSPDNHS QTLKTVSSTP NSTAEEEAHD LTEHHNSSPL LKAPLSFTNP
     LHSDDWHSDG GSSDGAVTRN KTSISTASAT VSPASSAESA CHRRVLPMSI ARQEVAGTPH
     SGAEKDADVS EESPPPLPER TPESFVLADM PVRPEWHELP NQEWSEQRES EGLTTSGNEK
     HDAGGIHTEA SADSPPAFSD KKDQITKSPA EVTDIGFGNR CGKPKGPREP PSEWT
//
ID   FMR1_MOUSE              Reviewed;         614 AA.
AC   P35922;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Fragile X mental retardation protein 1 homolog;
DE            Short=FMRP;
DE            Short=Protein FMR-1;
DE            Short=mFmr1p;
GN   Name=Fmr1; Synonyms=Fmr-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=93364418; PubMed=8358432; DOI=10.1038/ng0793-244;
RA   Ashley C.T. Jr., Sutcliffe J.S., Kunst C.B., Leiner H.A.,
RA   Eichler E.E., Nelson D.L., Warren S.T.;
RT   "Human and murine FMR-1: alternative splicing and translational
RT   initiation downstream of the CGG-repeat.";
RL   Nat. Genet. 4:244-251(1993).
RN   [2]
RP   INTERACTION WITH NUFIP1.
RX   MEDLINE=20025766; PubMed=10556305; DOI=10.1093/hmg/8.13.2557;
RA   Bardoni B., Schenck A., Mandel J.-L.;
RT   "A novel RNA-binding nuclear protein that interacts with the fragile X
RT   mental retardation (FMR1) protein.";
RL   Hum. Mol. Genet. 8:2557-2566(1999).
RN   [3]
RP   INTERACTION WITH CYFIP1 AND CYFIP2.
RX   MEDLINE=21352978; PubMed=11438699; DOI=10.1073/pnas.151231598;
RA   Schenck A., Bardoni B., Moro A., Bagni C., Mandel J.-L.;
RT   "A highly conserved protein family interacting with the fragile X
RT   mental retardation protein (FMRP) and displaying selective
RT   interactions with FMRP-related proteins FXR1P and FXR2P.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:8844-8849(2001).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-499,
RP   MUTAGENESIS OF SER-499, AND MASS SPECTROMETRY.
RX   PubMed=14570712; DOI=10.1093/hmg/ddg350;
RA   Ceman S., O'Donnell W.T., Reed M., Patton S., Pohl J., Warren S.T.;
RT   "Phosphorylation influences the translation state of FMRP-associated
RT   polyribosomes.";
RL   Hum. Mol. Genet. 12:3295-3305(2003).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=16000371; DOI=10.1091/mbc.E05-04-0304;
RA   Huot M.-E., Bisson N., Davidovic L., Mazroui R., Labelle Y., Moss T.,
RA   Khandjian E.W.;
RT   "The RNA-binding protein Fragile X-related 1 regulates somite
RT   formation in Xenopus laevis.";
RL   Mol. Biol. Cell 16:4350-4361(2005).
RN   [6]
RP   FUNCTION, INTERACTION WITH CYFIP1-EIF4E COMPLEX, AND BC1 RNA-BINDING.
RX   PubMed=18805096; DOI=10.1016/j.cell.2008.07.031;
RA   Napoli I., Mercaldo V., Boyl P.P., Eleuteri B., Zalfa F.,
RA   De Rubeis S., Di Marino D., Mohr E., Massimi M., Falconi M., Witke W.,
RA   Costa-Mattioli M., Sonenberg N., Achsel T., Bagni C.;
RT   "The fragile X syndrome protein represses activity-dependent
RT   translation through CYFIP1, a new 4E-BP.";
RL   Cell 134:1042-1054(2008).
RN   [7]
RP   INTERACTION WITH THE SMN CORE COMPLEX.
RX   PubMed=18093976; DOI=10.1074/jbc.M707304200;
RA   Piazzon N., Rage F., Schlotter F., Moine H., Branlant C., Massenet S.;
RT   "In vitro and in cellulo evidences for association of the survival of
RT   motor neuron complex with the fragile X mental retardation protein.";
RL   J. Biol. Chem. 283:5598-5610(2008).
CC   -!- FUNCTION: RNA-binding protein that plays a role in intracellular
CC       RNA transport and in the regulation of translation of target
CC       mRNAs. Associated with polysomes. May play a role in the transport
CC       of mRNA from the nucleus to the cytoplasm. Binds strongly to
CC       poly(G), binds moderately to poly(U) but shows very little binding
CC       to poly(A) or poly(C) (By similarity). Translation repressor.
CC       Component of the CYFIP1-EIF4E-FMR1 complex which binds to the mRNA
CC       cap and mediates translational repression. In the CYFIP1-EIF4E-
CC       FMR1 complex this subunit mediates translation repression.
CC   -!- SUBUNIT: Homooligomer. Found in a RNP granule complex with
CC       IGF2BP1. Interacts with FXR1, FXR2, IGF2BP1 and RANBP9. Directly
CC       interacts with SMN and TDRD3 (By similarity). Component of the
CC       CYFIP1-EIF4E-FMR1 complex which is composed of CYFIP, EIF4E and
CC       FMR1. Interacts with CYFIP1 and CYFIP2. The interaction with brain
CC       cytoplasmic RNA 1 (BC1) increases binding affinity for the CYFIP1-
CC       EIF4E complex in the brain. Interacts with CYFIP1 and CYFIP2.
CC       Interacts with the SMN core complex that contains SMN1,
CC       SIP1/GEMIN2, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8
CC       and STRAP/UNRIP.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=12;
CC       Name=ISO1;
CC         IsoId=P35922-1; Sequence=Displayed;
CC       Name=ISO2;
CC         IsoId=P35922-2; Sequence=VSP_002828;
CC       Name=ISO3;
CC         IsoId=P35922-3; Sequence=VSP_002829;
CC       Name=ISO4;
CC         IsoId=P35922-4; Sequence=VSP_002831, VSP_002830;
CC       Name=ISO5;
CC         IsoId=P35922-5; Sequence=VSP_002832, VSP_002833;
CC       Name=ISO6;
CC         IsoId=P35922-6; Sequence=VSP_002834, VSP_002835;
CC       Name=ISO7;
CC         IsoId=P35922-7; Sequence=VSP_002827;
CC       Name=ISO8;
CC         IsoId=P35922-8; Sequence=VSP_002827, VSP_002828;
CC       Name=ISO9;
CC         IsoId=P35922-9; Sequence=VSP_002827, VSP_002829;
CC       Name=ISO10;
CC         IsoId=P35922-10; Sequence=VSP_002827, VSP_002831, VSP_002830;
CC       Name=ISO11;
CC         IsoId=P35922-11; Sequence=VSP_002827, VSP_002832, VSP_002833;
CC       Name=ISO12;
CC         IsoId=P35922-12; Sequence=VSP_002827, VSP_002834, VSP_002835;
CC   -!- TISSUE SPECIFICITY: In adults, expressed predominantly in the
CC       brain.
CC   -!- PTM: Phosphorylated on several serine residues. Phosphorylation at
CC       Ser-499 is required for phosphorylation of other nearby serine
CC       residues. Phosphorylation has no effect on the binding of
CC       individual mRNA species, but may affect the interaction with
CC       polyribosomes.
CC   -!- MISCELLANEOUS: RNA-binding activity is inhibited by RANBP9.
CC   -!- SIMILARITY: Belongs to the FMR1 family.
CC   -!- SIMILARITY: Contains 2 KH domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; L23971; AAA37635.1; -; mRNA.
DR   IPI; IPI00227005; -.
DR   IPI; IPI00227006; -.
DR   IPI; IPI00227007; -.
DR   IPI; IPI00227008; -.
DR   IPI; IPI00227013; -.
DR   IPI; IPI00230029; -.
DR   IPI; IPI00230030; -.
DR   IPI; IPI00230031; -.
DR   IPI; IPI00270737; -.
DR   IPI; IPI00469993; -.
DR   IPI; IPI00474739; -.
DR   IPI; IPI00475390; -.
DR   PIR; S36173; S36173.
DR   UniGene; Mm.3451; -.
DR   ProteinModelPortal; P35922; -.
DR   SMR; P35922; 1-134, 216-424.
DR   IntAct; P35922; 10.
DR   MINT; MINT-111096; -.
DR   STRING; P35922; -.
DR   PhosphoSite; P35922; -.
DR   PRIDE; P35922; -.
DR   Ensembl; ENSMUST00000088546; ENSMUSP00000085906; ENSMUSG00000000838.
DR   Ensembl; ENSMUST00000101518; ENSMUSP00000099055; ENSMUSG00000000838.
DR   Ensembl; ENSMUST00000114651; ENSMUSP00000110298; ENSMUSG00000000838.
DR   Ensembl; ENSMUST00000114657; ENSMUSP00000110305; ENSMUSG00000000838.
DR   UCSC; uc009tiv.1; mouse.
DR   MGI; MGI:95564; Fmr1.
DR   eggNOG; roNOG10151; -.
DR   HOVERGEN; HBG005739; -.
DR   OrthoDB; EOG4PK27F; -.
DR   ArrayExpress; P35922; -.
DR   Bgee; P35922; -.
DR   CleanEx; MM_FMR1; -.
DR   Genevestigator; P35922; -.
DR   GermOnline; ENSMUSG00000000838; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005845; C:mRNA cap binding complex; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0007417; P:central nervous system development; IMP:MGI.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0045947; P:negative regulation of translational initiation; IDA:UniProtKB.
DR   InterPro; IPR008395; Agenet.
DR   InterPro; IPR022034; FXR1P_C.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR004088; KH_type_1.
DR   InterPro; IPR018111; KH_type_1_subgr.
DR   Pfam; PF05641; Agenet; 1.
DR   Pfam; PF12235; FXR1P_C; 1.
DR   Pfam; PF00013; KH_1; 2.
DR   SMART; SM00322; KH; 2.
DR   PROSITE; PS50084; KH_TYPE_1; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Methylation; mRNA transport; Nucleus;
KW   Phosphoprotein; Repeat; Repressor; RNA-binding; Transport.
FT   CHAIN         1    614       Fragile X mental retardation protein 1
FT                                homolog.
FT                                /FTId=PRO_0000050103.
FT   DOMAIN      222    251       KH 1.
FT   DOMAIN      285    314       KH 2.
FT   REGION      418    614       Interaction with RANBP9 (By similarity).
FT   REGION      534    547       RNA-binding RGG-box.
FT   MOD_RES     499    499       Phosphoserine.
FT   MOD_RES     543    543       Omega-N-methylated arginine (By
FT                                similarity).
FT   VAR_SEQ     375    395       Missing (in isoform ISO7, isoform ISO8,
FT                                isoform ISO9, isoform ISO10, isoform
FT                                ISO11 and isoform ISO12).
FT                                /FTId=VSP_002827.
FT   VAR_SEQ     425    512       EVDQLRLERLQIDEQLRQIGASSRPPPNRTDKEKGYVTDDG
FT                                QGMGRGSRPYRNRGHGRRGPGYTSGTNSEASNASETESDHR
FT                                DELSDW -> LQQRKRGRASCAEETDGGVEEEEEDKEEEEE
FT                                EEASKETTIIPEQIIVHVIQERLKEEQLMDPCRVPPVKGAG
FT                                CARVKIVTRRRKSQTA (in isoform ISO6 and
FT                                isoform ISO12).
FT                                /FTId=VSP_002834.
FT   VAR_SEQ     425    448       EVDQLRLERLQIDEQLRQIGASSR -> ELILKHQMLLKQN
FT                                LTTETNSVIGH (in isoform ISO4 and isoform
FT                                ISO10).
FT                                /FTId=VSP_002831.
FT   VAR_SEQ     425    436       EVDQLRLERLQI -> NLTTETNSVIGH (in isoform
FT                                ISO5 and isoform ISO11).
FT                                /FTId=VSP_002832.
FT   VAR_SEQ     437    614       Missing (in isoform ISO5 and isoform
FT                                ISO11).
FT                                /FTId=VSP_002833.
FT   VAR_SEQ     449    614       Missing (in isoform ISO4 and isoform
FT                                ISO10).
FT                                /FTId=VSP_002830.
FT   VAR_SEQ     490    514       Missing (in isoform ISO3 and isoform
FT                                ISO9).
FT                                /FTId=VSP_002829.
FT   VAR_SEQ     490    501       Missing (in isoform ISO2 and isoform
FT                                ISO8).
FT                                /FTId=VSP_002828.
FT   VAR_SEQ     513    614       Missing (in isoform ISO6 and isoform
FT                                ISO12).
FT                                /FTId=VSP_002835.
FT   MUTAGEN     499    499       S->A: Loss of phosphorylation.
FT   MUTAGEN     499    499       S->D: Leads to phosphorylation on other
FT                                serine residues.
SQ   SEQUENCE   614 AA;  68989 MW;  093DD90D589ED066 CRC64;
     MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPER QIPFHDVRFP PPVGYNKDIN
     ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD ATYNEIVTIE RLRSVNPNKP
     ATKDTFHKIK LEVPEDLRQM CAKESAHKDF KKAVGAFSVT YDPENYQLVI LSINEVTSKR
     AHMLIDMHFR SLRTKLSLIL RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN
     IQQARKVPGV TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN
     GKLIQEIVDK SGVVRVRIEA ENEKSVPQEE EIMPPSSLPS NNSRVGPNSS EEKKHLDTKE
     NTHFSQPNST KVQRVLVVSS IVAGGPQKPE PKAWQGMVPF VFVGTKDSIA NATVLLDYHL
     NYLKEVDQLR LERLQIDEQL RQIGASSRPP PNRTDKEKGY VTDDGQGMGR GSRPYRNRGH
     GRRGPGYTSG TNSEASNASE TESDHRDELS DWSLAPTEEE RESFLRRGDG RRRRGGGRGQ
     GGRGRGGGFK GNDDHSRTDN RPRNPREAKG RTADGSLQSA SSEGSRLRTG KDRNQKKEKP
     DSVDGLQPLV NGVP
//
ID   RL12_MOUSE              Reviewed;         165 AA.
AC   P35979; Q9CQK4;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 2.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=60S ribosomal protein L12;
GN   Name=Rpl12;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X CBA; TISSUE=Lung;
RX   MEDLINE=93366188; PubMed=8359697; DOI=10.1016/0378-1119(93)90433-4;
RA   Hou E.W., Li S.S.L.;
RT   "Sequence analysis of mouse cDNAs encoding ribosomal proteins L12 and
RT   L18.";
RL   Gene 130:287-290(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, Embryo, and Small intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   STRUCTURE BY NMR OF 2-80.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the N-terminal domain from mouse hypothetical
RT   protein BAB22488.";
RL   Submitted (NOV-2004) to the PDB data bank.
CC   -!- FUNCTION: Binds directly to 26S ribosomal RNA.
CC   -!- SIMILARITY: Belongs to the ribosomal protein L11P family.
CC   -----------------------------------------------------------------------
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DR   EMBL; L04280; AAA40066.1; -; mRNA.
DR   EMBL; AK002973; BAB22488.1; -; mRNA.
DR   EMBL; AK008347; BAB25619.1; -; mRNA.
DR   EMBL; AK012349; BAB28180.1; -; mRNA.
DR   EMBL; AK012428; BAB28232.1; -; mRNA.
DR   EMBL; BC018321; AAH18321.1; -; mRNA.
DR   EMBL; BC081469; AAH81469.1; -; mRNA.
DR   IPI; IPI00849793; -.
DR   PIR; JN0778; JN0778.
DR   RefSeq; NP_033102.2; NM_009076.3.
DR   UniGene; Mm.250030; -.
DR   UniGene; Mm.378999; -.
DR   UniGene; Mm.381297; -.
DR   PDB; 1WIB; NMR; -; A=2-79.
DR   PDBsum; 1WIB; -.
DR   ProteinModelPortal; P35979; -.
DR   SMR; P35979; 2-144.
DR   STRING; P35979; -.
DR   PhosphoSite; P35979; -.
DR   PRIDE; P35979; -.
DR   Ensembl; ENSMUST00000076703; ENSMUSP00000084807; ENSMUSG00000063328.
DR   Ensembl; ENSMUST00000092620; ENSMUSP00000090284; ENSMUSG00000069682.
DR   GeneID; 269261; -.
DR   KEGG; mmu:269261; -.
DR   CTD; 269261; -.
DR   MGI; MGI:98002; Rpl12.
DR   eggNOG; roNOG14523; -.
DR   HOGENOM; HBG594170; -.
DR   HOVERGEN; HBG007231; -.
DR   InParanoid; P35979; -.
DR   OMA; IQNRQAT; -.
DR   OrthoDB; EOG473PSB; -.
DR   PhylomeDB; P35979; -.
DR   NextBio; 392764; -.
DR   Bgee; P35979; -.
DR   CleanEx; MM_RPL12; -.
DR   Genevestigator; P35979; -.
DR   GermOnline; ENSMUSG00000068612; Mus musculus.
DR   GermOnline; ENSMUSG00000069682; Mus musculus.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR000911; Ribosomal_L11.
DR   InterPro; IPR020783; Ribosomal_L11_C.
DR   InterPro; IPR020785; Ribosomal_L11_CS.
DR   InterPro; IPR020784; Ribosomal_L11_N.
DR   Gene3D; G3DSA:1.10.10.250; Ribosomal_L11; 1.
DR   Gene3D; G3DSA:3.30.1550.10; Ribosomal_L11_N; 1.
DR   PANTHER; PTHR11661; Ribosomal_L11; 1.
DR   Pfam; PF00298; Ribosomal_L11; 1.
DR   Pfam; PF03946; Ribosomal_L11_N; 1.
DR   SMART; SM00649; RL11; 1.
DR   SUPFAM; SSF46906; Ribosomal_L11; 1.
DR   SUPFAM; SSF54747; Ribosomal_L11; 1.
DR   PROSITE; PS00359; RIBOSOMAL_L11; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Phosphoprotein; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding.
FT   CHAIN         1    165       60S ribosomal protein L12.
FT                                /FTId=PRO_0000104457.
FT   MOD_RES      14     14       Phosphotyrosine (By similarity).
FT   MOD_RES      38     38       Phosphoserine (By similarity).
FT   MOD_RES      54     54       N6-acetyllysine (By similarity).
FT   MOD_RES     165    165       Phosphoserine (By similarity).
FT   CONFLICT     79     79       A -> G (in Ref. 1; AAA40066).
FT   STRAND        7      9
FT   STRAND       11     18
FT   HELIX        29     32
FT   TURN         33     35
FT   HELIX        39     49
FT   TURN         50     55
FT   STRAND       56     65
FT   STRAND       68     70
SQ   SEQUENCE   165 AA;  17805 MW;  7EEEC00C57193116 CRC64;
     MPPKFDPNEV KVVYLRCTGG EVGATSALAP KIGPLGLSPK KVGDDIAKAT GDWKGLRITV
     KLTIQNRQAQ IEVVPSASAL IIKALKEPPR DRKKQKNIKH SGNITFDEIV NIARQMRHRS
     LARELSGTIK EILGTAQSVG CNVDGRHPHD IIDDINSGAV ECPAS
//
ID   GNL1_MOUSE              Reviewed;         607 AA.
AC   P36916; Q91Z20;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 3.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Guanine nucleotide-binding protein-like 1;
DE   AltName: Full=GTP-binding protein MMR1;
GN   Name=Gnl1; Synonyms=Gna-rs1, Mmr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   MEDLINE=93122794; PubMed=1478666; DOI=10.1016/S0888-7543(05)80105-3;
RA   Denizot F., Mattei M.-G., Vernet C., Pontarotti P., Chimini G.;
RT   "YAC-assisted cloning of a putative G-protein mapping to the MHC class
RT   I region.";
RL   Genomics 14:857-862(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=129; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND THR-48, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Possible regulatory or functional link with the
CC       histocompatibility cluster (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P36916-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P36916-2; Sequence=VSP_026994, VSP_026995;
CC   -!- DOMAIN: In contrast to other GTP-binding proteins, this family is
CC       characterized by a circular permutation of the GTPase motifs
CC       described by a G4-G1-G3 pattern.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the MMR1/HSR1 GTP-binding protein family.
CC   -!- SIMILARITY: Contains 1 G (guanine nucleotide-binding) domain.
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DR   EMBL; X65026; CAA46160.1; -; mRNA.
DR   EMBL; BC010298; AAH10298.1; -; mRNA.
DR   IPI; IPI00762316; -.
DR   IPI; IPI00855216; -.
DR   UniGene; Mm.335754; -.
DR   ProteinModelPortal; P36916; -.
DR   SMR; P36916; 180-235, 362-418.
DR   PhosphoSite; P36916; -.
DR   PRIDE; P36916; -.
DR   Ensembl; ENSMUST00000087200; ENSMUSP00000084450; ENSMUSG00000024429.
DR   MGI; MGI:95764; Gnl1.
DR   HOGENOM; HBG281218; -.
DR   HOVERGEN; HBG005865; -.
DR   InParanoid; P36916; -.
DR   OrthoDB; EOG4229JN; -.
DR   PhylomeDB; P36916; -.
DR   ArrayExpress; P36916; -.
DR   Bgee; P36916; -.
DR   Genevestigator; P36916; -.
DR   GermOnline; ENSMUSG00000024429; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR002917; MMR_HSR1_GTP-bd.
DR   Pfam; PF01926; MMR_HSR1; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; GTP-binding; Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1    607       Guanine nucleotide-binding protein-like
FT                                1.
FT                                /FTId=PRO_0000122442.
FT   DOMAIN      372    419       G.
FT   NP_BIND     225    228       GTP (Potential).
FT   NP_BIND     367    374       GTP (Potential).
FT   NP_BIND     411    415       GTP (Potential).
FT   COMPBIAS    551    607       Asp/Glu-rich (highly acidic).
FT   MOD_RES      32     32       Phosphoserine.
FT   MOD_RES      33     33       Phosphoserine (By similarity).
FT   MOD_RES      34     34       Phosphoserine (By similarity).
FT   MOD_RES      48     48       Phosphothreonine.
FT   MOD_RES      50     50       Phosphothreonine (By similarity).
FT   MOD_RES      51     51       Phosphoserine (By similarity).
FT   MOD_RES      68     68       Phosphoserine (By similarity).
FT   MOD_RES     324    324       Phosphoserine (By similarity).
FT   MOD_RES     561    561       Phosphoserine (By similarity).
FT   MOD_RES     562    562       Phosphoserine (By similarity).
FT   MOD_RES     563    563       Phosphoserine (By similarity).
FT   VAR_SEQ       1    177       Missing (in isoform 2).
FT                                /FTId=VSP_026994.
FT   VAR_SEQ     178    183       WRQLWR -> MEAAVA (in isoform 2).
FT                                /FTId=VSP_026995.
FT   CONFLICT    310    310       K -> Q (in Ref. 1; CAA46160).
FT   CONFLICT    491    491       A -> R (in Ref. 1; CAA46160).
SQ   SEQUENCE   607 AA;  68824 MW;  BB641571CAEC0C34 CRC64;
     MPRKKPFSVK QKKKQLQDKR ERKRGLQDGL RSSSNSRSGS RERREEQTDT SDGESVTHHI
     RRLNQQPSQG LGPRGYDPNR YRLHFERDSR EEVERRKRAA REQVLQPVSA EVLELDIREV
     YQPGSVLDFP RRPPWSYEMS KEQLMSQEER SFQEYLGKIH GAYTSEKLSY FEHNLETWRQ
     LWRVLEMSDI VLLITDIRHP VVNFPPALYE YVTGELGLAL VLVLNKVDLA PPALVVAWKH
     YFHQRYPQLH IVLFTSFPRD TRTPQEPGGV LKKNRRRGKG WTRALGPEQL LRACEAITVG
     KVDLSSWREK IARDVAGASW GNVSGEEEEE EDGPAVLVEQ LTDSAMEPTG PSRERYKDGV
     VTIGCIGFPN VGKSSLINGL VGRKVVSVSR TPGHTRYFQT YFLTPSVKLC DCPGLIFPSL
     LPRQLQVLAG IYPIAQIQEP YTSVGYLASR IPVQALLHLR HPEAEDPSAE HPWCAWDICE
     AWAEKRGYKT AKAARNDVYR AANSLLRLAV DGRLSLCFYP PGYSEQRGTW ESHPETAELV
     LSQGRVGPAG DEEEEEEEEL SSSCEEEGEE DRDADEEGEG DEDTPTSDPG SCLTARNPYA
     LLGEDEC
//
ID   GRP75_MOUSE             Reviewed;         679 AA.
AC   P38647; Q9CQ05;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 2.
DT   08-MAR-2011, entry version 107.
DE   RecName: Full=Stress-70 protein, mitochondrial;
DE   AltName: Full=75 kDa glucose-regulated protein;
DE            Short=GRP-75;
DE   AltName: Full=Heat shock 70 kDa protein 9;
DE   AltName: Full=Mortalin;
DE   AltName: Full=Peptide-binding protein 74;
DE            Short=PBP74;
DE   AltName: Full=p66 MOT;
DE   Flags: Precursor;
GN   Name=Hspa9; Synonyms=Grp75, Hsp74, Hspa9a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CD-1-ICR; TISSUE=Embryonic fibroblast;
RX   MEDLINE=93203261; PubMed=8454632;
RA   Wadhwa R., Kaul S.C., Ikawa Y., Sugimoto Y.;
RT   "Identification of a novel member of mouse hsp70 family. Its
RT   association with cellular mortal phenotype.";
RL   J. Biol. Chem. 268:6615-6621(1993).
RN   [2]
RP   SEQUENCE REVISION TO 123.
RA   Wadhwa R.;
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CD-1-ICR; TISSUE=Embryonic fibroblast;
RX   MEDLINE=94042962; PubMed=7693662;
RA   Wadhwa R., Kaul S.C., Sugimoto Y., Mitsui Y.;
RT   "Induction of cellular senescence by transfection of cytosolic
RT   mortalin cDNA in NIH 3T3 cells.";
RL   J. Biol. Chem. 268:22239-22242(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=B-cell;
RX   MEDLINE=93268309; PubMed=7684501;
RA   Domanico S.Z., Denagel D.C., Dahlseid J.N., Green J.M., Pierce S.K.;
RT   "Cloning of the gene encoding peptide-binding protein 74 shows that it
RT   is a new member of the heat shock protein 70 family.";
RL   Mol. Cell. Biol. 13:3598-3610(1993).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=94085585; PubMed=8262211; DOI=10.1016/0014-5793(93)81602-V;
RA   Michikawa Y., Baba T., Arai Y., Sakakura T., Kusakabe M.;
RT   "Structure and organization of the gene encoding a mouse mitochondrial
RT   stress-70 protein.";
RL   FEBS Lett. 336:27-33(1993).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C3H/HeN; TISSUE=Kidney;
RX   MEDLINE=94029998; PubMed=7692847; DOI=10.1006/bbrc.1993.2238;
RA   Michikawa Y., Baba T., Arai Y., Sakakura T., Tanaka M., Kusakabe M.;
RT   "Antigenic protein specific for C3H strain mouse is a mitochondrial
RT   stress-70 protein.";
RL   Biochem. Biophys. Res. Commun. 196:223-232(1993).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [8]
RP   PROTEIN SEQUENCE OF 47-70.
RC   TISSUE=Fibroblast;
RX   MEDLINE=95009907; PubMed=7523108; DOI=10.1002/elps.11501501101;
RA   Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.;
RT   "Separation and sequencing of familiar and novel murine proteins using
RT   preparative two-dimensional gel electrophoresis.";
RL   Electrophoresis 15:735-745(1994).
RN   [9]
RP   PROTEIN SEQUENCE OF 188-202; 266-284; 349-360; 395-405 AND 499-513,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [10]
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=95170122; PubMed=7865888;
RA   Dahlseid J.N., Lill R., Green J.M., Xu X., Qiu Y., Pierce S.K.;
RT   "PBP74, a new member of the mammalian 70-kDa heat shock protein
RT   family, is a mitochondrial protein.";
RL   Mol. Biol. Cell 5:1265-1275(1994).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288; LYS-300 AND LYS-360,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- FUNCTION: Implicated in the control of cell proliferation and
CC       cellular aging. May also act as a chaperone.
CC   -!- SUBUNIT: Interacts with FXN (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- TISSUE SPECIFICITY: Found in all the cell types examined.
CC   -!- INDUCTION: Not induced by heat shock, instead protein level is
CC       decreased.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- POLYMORPHISM: Two forms of the protein have been found, MOT-1,
CC       found in mortal cells and MOT-2, found in immortal cells. The
CC       sequence of MOT-1 is shown here.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D11089; BAA01862.2; -; mRNA.
DR   EMBL; L06896; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; D17666; BAA04548.1; -; Genomic_DNA.
DR   EMBL; D17556; BAA04493.1; -; mRNA.
DR   EMBL; AK004946; BAB23690.1; -; mRNA.
DR   EMBL; AK002634; BAB22248.1; -; mRNA.
DR   IPI; IPI00133903; -.
DR   PIR; S39839; A48127.
DR   RefSeq; NP_034611.2; NM_010481.2.
DR   UniGene; Mm.209419; -.
DR   UniGene; Mm.479254; -.
DR   ProteinModelPortal; P38647; -.
DR   SMR; P38647; 54-656.
DR   STRING; P38647; -.
DR   PhosphoSite; P38647; -.
DR   SWISS-2DPAGE; P38647; -.
DR   COMPLUYEAST-2DPAGE; P38647; -.
DR   REPRODUCTION-2DPAGE; IPI00133903; -.
DR   REPRODUCTION-2DPAGE; P38647; -.
DR   PRIDE; P38647; -.
DR   Ensembl; ENSMUST00000025217; ENSMUSP00000025217; ENSMUSG00000024359.
DR   GeneID; 15526; -.
DR   KEGG; mmu:15526; -.
DR   UCSC; uc008elv.1; mouse.
DR   CTD; 15526; -.
DR   MGI; MGI:96245; Hspa9.
DR   eggNOG; roNOG13746; -.
DR   HOGENOM; HBG334976; -.
DR   HOVERGEN; HBG051845; -.
DR   InParanoid; P38647; -.
DR   OrthoDB; EOG49KFQ6; -.
DR   PhylomeDB; P38647; -.
DR   ArrayExpress; P38647; -.
DR   Bgee; P38647; -.
DR   CleanEx; MM_HSPA9; -.
DR   Genevestigator; P38647; -.
DR   GermOnline; ENSMUSG00000024359; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006611; P:protein export from nucleus; IDA:MGI.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   InterPro; IPR012725; Chaperone_DnaK.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR001023; Hsp70.
DR   InterPro; IPR013126; Hsp_70.
DR   PANTHER; PTHR19375; Hsp70; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   TIGRFAMs; TIGR02350; prok_dnaK; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Chaperone; Direct protein sequencing;
KW   Mitochondrion; Nucleotide-binding; Phosphoprotein; Transit peptide.
FT   TRANSIT       1     46       Mitochondrion.
FT   CHAIN        47    679       Stress-70 protein, mitochondrial.
FT                                /FTId=PRO_0000013564.
FT   MOD_RES     135    135       N6-acetyllysine (By similarity).
FT   MOD_RES     138    138       N6-acetyllysine (By similarity).
FT   MOD_RES     143    143       N6-acetyllysine (By similarity).
FT   MOD_RES     200    200       Phosphoserine (By similarity).
FT   MOD_RES     234    234       N6-acetyllysine (By similarity).
FT   MOD_RES     288    288       N6-acetyllysine.
FT   MOD_RES     300    300       N6-acetyllysine.
FT   MOD_RES     345    345       N6-acetyllysine (By similarity).
FT   MOD_RES     360    360       N6-acetyllysine.
FT   MOD_RES     567    567       N6-acetyllysine (By similarity).
FT   MOD_RES     568    568       Phosphotyrosine (By similarity).
FT   MOD_RES     646    646       N6-acetyllysine (By similarity).
FT   VARIANT     618    618       V -> M (in MOT-2, perinuclear form).
FT   VARIANT     624    624       R -> G (in MOT-2, perinuclear form).
FT   CONFLICT      5      5       S -> T (in Ref. 4; AA sequence).
FT   CONFLICT    106    106       K -> R (in Ref. 4; AA sequence).
FT   CONFLICT    203    203       Q -> D (in Ref. 3).
FT   CONFLICT    522    522       F -> S (in Ref. 4; AA sequence).
SQ   SEQUENCE   679 AA;  73528 MW;  3E58DC6275796232 CRC64;
     MISASRAAAA RLVGTAASRS PAAARPQDGW NGLSHEAFRF VSRRDYASEA IKGAVVGIDL
     GTTNSCVAVM EGKQAKVLEN AEGARTTPSV VAFTADGERL VGMPAKRQAV TNPNNTFYAT
     KRLIGRRYDD PEVQKDTKNV PFKIVRASNG DAWVEAHGKL YSPSQIGAFV LMKMKETAEN
     YLGHTAKNAV ITVPAYFNDS QRQATKDAGQ ISGLNVLRVI NEPTAAALAY GLDKSEDKVI
     AVYDLGGGTF DISILEIQKG VFEVKSTNGD TFLGGEDFDQ ALLRHIVKEF KRETGVDLTK
     DNMALQRVRE AAEKAKCELS SSVQTDINLP YLTMDASGPK HLNMKLTRAQ FEGIVTDLIK
     RTIAPCQKAM QDAEVSKSDI GEVILVGGMT RMPKVQQTVQ DLFGRAPSKA VNPDEAVAIG
     AAIQGGVLAG DVTDVLLLDV TPLSLGIETL GGVFTKLINR NTTIPTKKSQ VFSTAADGQT
     QVEIKVCQGE REMAGDNKLL GQFTLIGIPP APRGVPQIEV TFDIDANGIV HVSAKDKGTG
     REQQIVIQSS GGLSKDDIEN MVKNAEKYAE EDRRKKERVE AVNMAEGIIH DTETKMEEFK
     DQLPADECNK LKEEISKVRA LLARKDSETG ENIRQAASSL QQASLKLFEM AYKKMASERE
     GSGSSGTGEQ KEDQKEEKQ
//
ID   CADH4_MOUSE             Reviewed;         913 AA.
AC   P39038;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Cadherin-4;
DE   AltName: Full=Retinal cadherin;
DE            Short=R-CAD;
DE            Short=R-cadherin;
DE   Flags: Precursor;
GN   Name=Cdh4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreatic islet;
RX   MEDLINE=94067164; PubMed=8247017; DOI=10.1210/me.7.9.1151;
RA   Hutton J.C., Christofori G., Chi W.Y., Edman U., Guest P.C.,
RA   Hanahan D., Kelly R.B.;
RT   "Molecular cloning of mouse pancreatic islet R-cadherin: differential
RT   expression in endocrine and exocrine tissue.";
RL   Mol. Endocrinol. 7:1151-1160(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94095672; PubMed=8270638;
RA   Matsunami H., Miyatani S., Inoue T., Copeland N.G., Gilbert D.,
RA   Jenkins N.A., Takeichi M.;
RT   "Cell binding specificity of mouse R-cadherin and chromosomal mapping
RT   of the gene.";
RL   J. Cell Sci. 106:401-409(1993).
CC   -!- FUNCTION: Cadherins are calcium dependent cell adhesion proteins.
CC       They preferentially interact with themselves in a homophilic
CC       manner in connecting cells; cadherins may thus contribute to the
CC       sorting of heterogeneous cell types. May play an important role in
CC       retinal development.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Distributed widely in mouse tissues with high
CC       levels present in brain, skeletal muscle and thymus.
CC   -!- SIMILARITY: Contains 5 cadherin domains.
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DR   EMBL; X69966; CAA49589.1; -; mRNA.
DR   EMBL; D14888; BAA03605.1; -; mRNA.
DR   IPI; IPI00131397; -.
DR   PIR; A47543; A47543.
DR   RefSeq; NP_033997.1; NM_009867.2.
DR   UniGene; Mm.184711; -.
DR   ProteinModelPortal; P39038; -.
DR   SMR; P39038; 24-716, 825-910.
DR   STRING; P39038; -.
DR   PhosphoSite; P39038; -.
DR   PRIDE; P39038; -.
DR   Ensembl; ENSMUST00000000314; ENSMUSP00000000314; ENSMUSG00000000305.
DR   GeneID; 12561; -.
DR   KEGG; mmu:12561; -.
DR   UCSC; uc008ohv.1; mouse.
DR   CTD; 12561; -.
DR   MGI; MGI:99218; Cdh4.
DR   eggNOG; roNOG15574; -.
DR   GeneTree; ENSGT00550000074431; -.
DR   HOGENOM; HBG505775; -.
DR   HOVERGEN; HBG106438; -.
DR   InParanoid; P39038; -.
DR   OMA; CEKPNLN; -.
DR   OrthoDB; EOG483D43; -.
DR   PhylomeDB; P39038; -.
DR   NextBio; 281632; -.
DR   ArrayExpress; P39038; -.
DR   Bgee; P39038; -.
DR   CleanEx; MM_CDH4; -.
DR   Genevestigator; P39038; -.
DR   GermOnline; ENSMUSG00000000305; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007411; P:axon guidance; IDA:MGI.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion; IDA:MGI.
DR   GO; GO:0007156; P:homophilic cell adhesion; IDA:MGI.
DR   GO; GO:0045773; P:positive regulation of axon extension; IDA:MGI.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR   InterPro; IPR014868; Cadherin_pro.
DR   InterPro; IPR009124; Desmocollin.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 5.
DR   Pfam; PF00028; Cadherin; 4.
DR   Pfam; PF01049; Cadherin_C; 1.
DR   Pfam; PF08758; Cadherin_pro; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   PRINTS; PR01820; DESMOCOLLIN.
DR   SMART; SM00112; CA; 5.
DR   SUPFAM; SSF49313; Cadherin; 6.
DR   PROSITE; PS00232; CADHERIN_1; 3.
DR   PROSITE; PS50268; CADHERIN_2; 5.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell membrane;
KW   Cleavage on pair of basic residues; Glycoprotein; Membrane; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     20       Potential.
FT   PROPEP       21    166       Potential.
FT                                /FTId=PRO_0000003751.
FT   CHAIN       167    913       Cadherin-4.
FT                                /FTId=PRO_0000003752.
FT   TOPO_DOM    167    731       Extracellular (Potential).
FT   TRANSMEM    732    753       Helical; (Potential).
FT   TOPO_DOM    754    913       Cytoplasmic (Potential).
FT   DOMAIN      167    274       Cadherin 1.
FT   DOMAIN      275    389       Cadherin 2.
FT   DOMAIN      390    504       Cadherin 3.
FT   DOMAIN      505    610       Cadherin 4.
FT   DOMAIN      611    721       Cadherin 5.
FT   COMPBIAS    870    885       Ser-rich.
FT   CARBOHYD    146    146       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    280    280       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    409    409       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    554    554       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    629    629       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    658    658       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    699    699       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   913 AA;  100030 MW;  1245A8CE8C338481 CRC64;
     MTTGSVLPLL LLGLSGALRA HREDLTVREA CKAGFSEEGY TALISPNVLE GEKLLKVEFS
     SCVGTKGMQY ETNSLDFKVG ADGTVFATRE LKIPSEQVAF TVTARERQSA EQWAAMVRLL
     VAQTSSAHSE HKKGQTVALD PSQPPNDTLL PWPQHQSSGG LRRQKRDWVI PPINVPENSR
     GPFPQQLVRI RSDKDNDIPI RYSITGVGAD QPPMEVFNID SMSGRMYVTR PMDREERASY
     HLRAHAVDMN GNKVENPIDL YIYVIDMNDN RPEFINQVYN GSVDEGSKPG TYVMTVTAND
     ADDSTTANGM VRYRIVTQTP QSPSQNMFTI NSETGDIVTV AAGLDREKVQ QYTVIVQATD
     MEGNLNYGLS NTATAIITVT DVNDNPPEFT TSTFAGEVPE NRIETVVANL TVMDRDQPHS
     PNWNAVYRII SGDPSGHFSV RTDPVTNEGM VTVVKAVDYE LNRAFMLTVM VSNQAPLASG
     IQMSFQSTAG VTISVTDVNE APYFPSNHKL IRLEEGVPAG TALTTFSAVD PDRFMQQAVR
     YSKLSDPANW LHINTSNGQI TTAAILDRES LYTKNNVYEA TFLAADNGIP PASGTGTLQI
     YLIDINDNAP QLLPKEAQIC ERPGLNAINI TAADADMDPN IGPYVFELPF IPTTVRKNWT
     ITRLNGDYAQ LSLRILYLEA GVYDVPIIVT DSGNPPLSNT SVIKVKVCPC DENGDCTTVG
     AVAAAGLGTG AIVAILICIV ILLIMVLLFV VWMKRREKER HTKQLLIDPE DDVRDNILKY
     DEEGGGEEDQ DYDLSQLQQP EAMEHVLSKT PGVRRVDERP VGAEPQYPVR PVVPHPGDIG
     DFINEGLRAA DNDPTAPPYD SLLVFDYEGS GSTAGSVSSL NSSSSGDQDY DYLNDWGPRF
     KKLADMYGGG EED
//
ID   DYN1_MOUSE              Reviewed;         867 AA.
AC   P39053; A2AN50; A2AN51; A2AN54; A2AN55; Q3UNM1; Q5DTN7; Q61358;
AC   Q61359; Q61360; Q6PDM5; Q8JZZ4; Q9CSY7; Q9QXX1;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2003, sequence version 2.
DT   08-MAR-2011, entry version 108.
DE   RecName: Full=Dynamin-1;
DE            EC=3.6.5.5;
GN   Name=Dnm1; Synonyms=Dnm, Kiaa4093;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5).
RC   STRAIN=NIH Swiss; TISSUE=Brain;
RX   MEDLINE=97288532; PubMed=9143510; DOI=10.1006/geno.1997.4634;
RA   Klocke R., Augustin A., Ronsiek M., Stief A., van der Putten H.,
RA   Jockusch H.;
RT   "Dynamin genes Dnm1 and Dnm2 are located on proximal mouse chromosomes
RT   2 and 9, respectively.";
RL   Genomics 41:290-292(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC   STRAIN=C57BL/6J; TISSUE=Colon, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
RX   MEDLINE=20498746; PubMed=11042120; DOI=10.1042/0264-6021:3510661;
RA   Yoo J., Lee S.S., Jeong M.J., Lee K.I., Kwon B.M., Kim S.H.,
RA   Park Y.M., Han M.Y.;
RT   "Characterization of the mouse dynamin I gene promoter and
RT   identification of sequences that direct expression in neuronal
RT   cells.";
RL   Biochem. J. 351:661-668(2000).
RN   [7]
RP   PROTEIN SEQUENCE OF 5-54; 67-87; 91-107; 114-188; 207-217; 230-237;
RP   247-266; 280-290; 300-309; 328-361; 370-376; 400-414; 511-535;
RP   563-571; 584-594; 664-675 AND 684-694.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [8]
RP   INTERACTION WITH CAV1, AND PHOSPHORYLATION.
RX   MEDLINE=21952646; PubMed=11956154; DOI=10.1210/en.143.5.1726;
RA   Kim Y.N., Bertics P.J.;
RT   "The endocytosis-linked protein dynamin associates with caveolin-1 and
RT   is tyrosine phosphorylated in response to the activation of a
RT   noninternalizing epidermal growth factor receptor mutant.";
RL   Endocrinology 143:1726-1731(2002).
RN   [9]
RP   INTERACTION WITH SH3GLB1.
RX   PubMed=12456676; DOI=10.1074/jbc.M208568200;
RA   Modregger J., Schmidt A.A., Ritter B., Huttner W.B., Plomann M.;
RT   "Characterization of endophilin B1b, a brain-specific membrane-
RT   associated lysophosphatidic acid acyl transferase with properties
RT   distinct from endophilin A1.";
RL   J. Biol. Chem. 278:4160-4167(2003).
RN   [10]
RP   NITRATION [LARGE SCALE ANALYSIS] AT TYR-125, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16800626; DOI=10.1021/bi060474w;
RA   Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
RA   Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
RA   Squier T.C., Bigelow D.J.;
RT   "Endogenously nitrated proteins in mouse brain: links to
RT   neurodegenerative disease.";
RL   Biochemistry 45:8009-8022(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-80; TYR-125 AND TYR-354,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-778, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-847 (ISOFORM 6), AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Microtubule-associated force-producing protein involved
CC       in producing microtubule bundles and able to bind and hydrolyze
CC       GTP. Most probably involved in vesicular trafficking processes.
CC       Involved in receptor-mediated endocytosis (By similarity).
CC   -!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate.
CC   -!- SUBUNIT: Binds SH3GL1, SH3GL2 and SH3GL3 (By similarity).
CC       Interacts with CAV1 and SH3GLB1.
CC   -!- INTERACTION:
CC       Self; NbExp=1; IntAct=EBI-397785, EBI-397785;
CC       Q9JJV2:Pfn2; NbExp=1; IntAct=EBI-397785, EBI-990247;
CC       Q9JJV2-1:Pfn2; NbExp=1; IntAct=EBI-397785, EBI-990256;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
CC       Note=Microtubule-associated.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=P39053-1; Sequence=Displayed;
CC         Note=Phosphorylated on Ser-847;
CC       Name=2; Synonyms=BreDnm19;
CC         IsoId=P39053-2; Sequence=VSP_007644, VSP_007646;
CC       Name=3; Synonyms=BraDnm8;
CC         IsoId=P39053-3; Sequence=VSP_007643, VSP_007645;
CC       Name=4; Synonyms=BraDnm2;
CC         IsoId=P39053-4; Sequence=VSP_007647;
CC       Name=5; Synonyms=BreDnm15;
CC         IsoId=P39053-5; Sequence=VSP_007645;
CC       Name=6;
CC         IsoId=P39053-6; Sequence=VSP_007644, VSP_024845;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated in response to EGF stimulation in cells
CC       expressing truncated EGFR.
CC   -!- SIMILARITY: Belongs to the dynamin family.
CC   -!- SIMILARITY: Contains 1 GED domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90284.1; Type=Erroneous initiation;
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DR   EMBL; L29457; AAA37319.1; -; mRNA.
DR   EMBL; L31395; AAA37318.1; -; mRNA.
DR   EMBL; L31396; AAA37323.1; -; mRNA.
DR   EMBL; L31397; AAA37324.1; -; mRNA.
DR   EMBL; AK011651; BAB27759.1; -; mRNA.
DR   EMBL; AK144142; BAE25726.1; -; mRNA.
DR   EMBL; AK220483; BAD90284.1; ALT_INIT; mRNA.
DR   EMBL; AL808027; CAM15852.1; -; Genomic_DNA.
DR   EMBL; AL808027; CAM15853.1; -; Genomic_DNA.
DR   EMBL; AL808027; CAM15855.1; -; Genomic_DNA.
DR   EMBL; AL808027; CAM15857.1; -; Genomic_DNA.
DR   EMBL; BC034679; AAH34679.1; -; mRNA.
DR   EMBL; BC058623; AAH58623.1; -; mRNA.
DR   EMBL; AF170568; AAF24220.1; -; Genomic_DNA.
DR   IPI; IPI00272878; -.
DR   IPI; IPI00331291; -.
DR   IPI; IPI00331293; -.
DR   IPI; IPI00465648; -.
DR   IPI; IPI00753037; -.
DR   IPI; IPI00845595; -.
DR   RefSeq; NP_034195.2; NM_010065.2.
DR   UniGene; Mm.44736; -.
DR   ProteinModelPortal; P39053; -.
DR   SMR; P39053; 6-344, 518-630, 715-746.
DR   IntAct; P39053; 18.
DR   MINT; MINT-86537; -.
DR   STRING; P39053; -.
DR   PhosphoSite; P39053; -.
DR   PRIDE; P39053; -.
DR   Ensembl; ENSMUST00000002626; ENSMUSP00000002626; ENSMUSG00000026825.
DR   Ensembl; ENSMUST00000035664; ENSMUSP00000039033; ENSMUSG00000026825.
DR   Ensembl; ENSMUST00000091089; ENSMUSP00000088618; ENSMUSG00000026825.
DR   Ensembl; ENSMUST00000116534; ENSMUSP00000112233; ENSMUSG00000026825.
DR   GeneID; 13429; -.
DR   KEGG; mmu:13429; -.
DR   CTD; 13429; -.
DR   MGI; MGI:107384; Dnm1.
DR   eggNOG; roNOG10695; -.
DR   GeneTree; ENSGT00600000084144; -.
DR   HOVERGEN; HBG107833; -.
DR   OMA; KTSGNQD; -.
DR   OrthoDB; EOG49GKG1; -.
DR   PhylomeDB; P39053; -.
DR   BRENDA; 3.6.5.5; 244.
DR   NextBio; 283851; -.
DR   ArrayExpress; P39053; -.
DR   Bgee; P39053; -.
DR   CleanEx; MM_DNM1; -.
DR   Genevestigator; P39053; -.
DR   GermOnline; ENSMUSG00000026825; Mus musculus.
DR   GO; GO:0030117; C:membrane coat; IDA:MGI.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0003774; F:motor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   InterPro; IPR022812; Dynamin.
DR   InterPro; IPR000375; Dynamin_central.
DR   InterPro; IPR001401; Dynamin_GTPase.
DR   InterPro; IPR019762; Dynamin_GTPase_CS.
DR   InterPro; IPR003130; GED.
DR   InterPro; IPR020850; GTPase_effector_domain_GED.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Pfam; PF01031; Dynamin_M; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   Pfam; PF02212; GED; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00195; DYNAMIN.
DR   SMART; SM00053; DYNc; 1.
DR   SMART; SM00302; GED; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS00410; DYNAMIN; 1.
DR   PROSITE; PS51388; GED; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Endocytosis; GTP-binding; Hydrolase;
KW   Microtubule; Motor protein; Nitration; Nucleotide-binding;
KW   Phosphoprotein.
FT   CHAIN         1    867       Dynamin-1.
FT                                /FTId=PRO_0000206564.
FT   DOMAIN      515    625       PH.
FT   DOMAIN      659    750       GED.
FT   NP_BIND      38     45       GTP (By similarity).
FT   NP_BIND     136    140       GTP (By similarity).
FT   NP_BIND     205    208       GTP (By similarity).
FT   MOD_RES      80     80       Phosphotyrosine.
FT   MOD_RES     125    125       Nitrated tyrosine.
FT   MOD_RES     125    125       Phosphotyrosine.
FT   MOD_RES     354    354       Phosphotyrosine.
FT   MOD_RES     774    774       Phosphoserine (By similarity).
FT   MOD_RES     776    776       Phosphothreonine (By similarity).
FT   MOD_RES     778    778       Phosphoserine.
FT   VAR_SEQ     407    444       MAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTK ->
FT                                LAFEATVKKQVQKLKEPSIKCVDMVVSELTSTIRKCSE
FT                                (in isoform 3).
FT                                /FTId=VSP_007643.
FT   VAR_SEQ     516    519       Missing (in isoform 2 and isoform 6).
FT                                /FTId=VSP_007644.
FT   VAR_SEQ     845    867       SLGAWRLNSPQGKHENRAGKARL -> RITISDP (in
FT                                isoform 3 and isoform 5).
FT                                /FTId=VSP_007645.
FT   VAR_SEQ     846    867       LGAWRLNSPQGKHENRAGKARL -> RKAQPHLRDLQPPDQ
FT                                RRLPS (in isoform 2).
FT                                /FTId=VSP_007646.
FT   VAR_SEQ     846    867       LGAWRLNSPQGKHENRAGKARL -> RSGQASPSRPESPRP
FT                                PFDL (in isoform 4).
FT                                /FTId=VSP_007647.
FT   VAR_SEQ     846    867       LGAWRLNSPQGKHENRAGKARL -> RKGPASPTRPAAPRP
FT                                TEAPLLDL (in isoform 6).
FT                                /FTId=VSP_024845.
FT   CONFLICT    135    135       V -> A (in Ref. 1; AAA37318).
FT   CONFLICT    450    450       P -> R (in Ref. 1; AAA37318).
FT   CONFLICT    531    531       I -> S (in Ref. 1; AAA37318).
FT   CONFLICT    573    573       R -> H (in Ref. 2; BAE25726).
FT   CONFLICT    600    600       Y -> N (in Ref. 1; AAA37318).
FT   CONFLICT    703    703       A -> V (in Ref. 5; AAH58623).
FT   CONFLICT    722    722       A -> R (in Ref. 1; AAA37319/AAA37323/
FT                                AAA37324).
SQ   SEQUENCE   867 AA;  97803 MW;  F48EC3DF5F39A08B CRC64;
     MGNRGMEDLI PLVNRLQDAF SAIGQNADLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
     SGIVTRRPLV LQLVNSTTEY AEFLHCKGKK FTDFEEVRLE IEAETDRVTG TNKGISPVPI
     NLRVYSPHVL NLTLVDLPGM TKVPVGDQPP DIEFQIRDML MQFVTKENCL ILAVSPANSD
     LANSDALKIA KEVDPQGQRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK
     DIDGKKDITA ALAAERKFFL SHPSYRHLAD RMGTPYLQKV LNQQLTNHIR DTLPGLRNKL
     QSQLLSIEKE VDEYKNFRPD DPARKTKALL QMVQQFAVDF EKRIEGSGDQ IDTYELSGGA
     RINRIFHERF PFELVKMEFD EKELRREISY AIKNIHGIRT GLFTPDMAFE TIVKKQVKKI
     REPCLKCVDM VISELISTVR QCTKKLQQYP RLREEMERIV TTHIREREGR TKEQVMLLID
     IELAYMNTNH EDFIGFANAQ QRSNQMNKKK TSGNQDEILV IRKGWLTINN IGIMKGGSKE
     YWFVLTAENL SWYKDDEEKE KKYMLSVDNL KLRDVEKGFM SSKHIFALFN TEQRNVYKDY
     RQLELACETQ EEVDSWKASF LRAGVYPERV GDKEKASETE ENGSDSFMHS MDPQLERQVE
     TIRNLVDSYM AIVNKTVRDL MPKTIMHLMI NNTKEFIFSE LLANLYSCGD QNTLMEESAE
     QAQRRDEMLR MYHALKEALS IIGDINTTTV STPMPPPVDD SWLQVQSVPA GRRSPTSSPT
     PQRRAPAVPP ARPGSRGPAP GPPPAGSALG GAPPVPSRPG ASPDPFGPPP QVPSRPNRAP
     PGVPSLGAWR LNSPQGKHEN RAGKARL
//
ID   DYN2_MOUSE              Reviewed;         870 AA.
AC   P39054; Q9DBE1;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   26-JUL-2002, sequence version 2.
DT   08-FEB-2011, entry version 102.
DE   RecName: Full=Dynamin-2;
DE            EC=3.6.5.5;
DE   AltName: Full=Dynamin UDNM;
GN   Name=Dnm2; Synonyms=Dyn2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=NIH Swiss;
RX   MEDLINE=97288532; PubMed=9143510; DOI=10.1006/geno.1997.4634;
RA   Klocke R., Augustin A., Ronsiek M., Stief A., van der Putten H.,
RA   Jockusch H.;
RT   "Dynamin genes Dnm1 and Dnm2 are located on proximal mouse chromosomes
RT   2 and 9, respectively.";
RL   Genomics 41:290-292(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF 45-54; 91-107; 114-142; 207-217; 230-237; 300-309;
RP   370-376 AND 678-688, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   INTERACTION WITH SH3BP4.
RX   PubMed=16325581; DOI=10.1016/j.cell.2005.10.021;
RA   Tosoni D., Puri C., Confalonieri S., Salcini A.E., De Camilli P.,
RA   Tacchetti C., Di Fiore P.P.;
RT   "TTP specifically regulates the internalization of the transferrin
RT   receptor.";
RL   Cell 123:875-888(2005).
RN   [5]
RP   INTERACTION WITH MYOF.
RX   PubMed=17702744; DOI=10.1074/jbc.M704798200;
RA   Bernatchez P.N., Acevedo L., Fernandez-Hernando C., Murata T.,
RA   Chalouni C., Kim J., Erdjument-Bromage H., Shah V., Gratton J.-P.,
RA   McNally E.M., Tempst P., Sessa W.C.;
RT   "Myoferlin regulates vascular endothelial growth factor receptor-2
RT   stability and function.";
RL   J. Biol. Chem. 282:30745-30753(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; SER-302 AND
RP   TYR-597, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: Microtubule-associated force-producing protein involved
CC       in producing microtubule bundles and able to bind and hydrolyze
CC       GTP. Most probably involved in vesicular trafficking processes, in
CC       particular endocytosis.
CC   -!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate.
CC   -!- SUBUNIT: Interacts with SHANK1, SHANK2 and NOSTRIN (By
CC       similarity). Interacts with MYOF and SH3BP4.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity). Cell junction, synapse, postsynaptic
CC       cell membrane, postsynaptic density (By similarity). Cell
CC       junction, synapse (By similarity). Note=Microtubule-associated.
CC       Also found in the postsynaptic density of neuronal cells (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P39054-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P39054-2; Sequence=VSP_001326;
CC   -!- SIMILARITY: Belongs to the dynamin family.
CC   -!- SIMILARITY: Contains 1 GED domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
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DR   EMBL; L31398; AAA40523.1; -; mRNA.
DR   EMBL; AK005012; BAB23745.1; -; mRNA.
DR   IPI; IPI00131445; -.
DR   IPI; IPI00314883; -.
DR   UniGene; Mm.433257; -.
DR   ProteinModelPortal; P39054; -.
DR   SMR; P39054; 6-320, 520-625.
DR   IntAct; P39054; 10.
DR   STRING; P39054; -.
DR   PhosphoSite; P39054; -.
DR   REPRODUCTION-2DPAGE; IPI00131445; -.
DR   PRIDE; P39054; -.
DR   Ensembl; ENSMUST00000072362; ENSMUSP00000072199; ENSMUSG00000033335.
DR   Ensembl; ENSMUST00000091087; ENSMUSP00000088616; ENSMUSG00000033335.
DR   UCSC; uc009olk.1; mouse.
DR   MGI; MGI:109547; Dnm2.
DR   eggNOG; roNOG04822; -.
DR   GeneTree; ENSGT00600000084144; -.
DR   HOGENOM; HBG434086; -.
DR   HOVERGEN; HBG107833; -.
DR   InParanoid; P39054; -.
DR   OMA; FPAPPQI; -.
DR   PhylomeDB; P39054; -.
DR   BRENDA; 3.6.5.5; 244.
DR   ArrayExpress; P39054; -.
DR   Bgee; P39054; -.
DR   CleanEx; MM_DNM2; -.
DR   Genevestigator; P39054; -.
DR   GermOnline; ENSMUSG00000033335; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003774; F:motor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   InterPro; IPR022812; Dynamin.
DR   InterPro; IPR000375; Dynamin_central.
DR   InterPro; IPR001401; Dynamin_GTPase.
DR   InterPro; IPR019762; Dynamin_GTPase_CS.
DR   InterPro; IPR003130; GED.
DR   InterPro; IPR020850; GTPase_effector_domain_GED.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Pfam; PF01031; Dynamin_M; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   Pfam; PF02212; GED; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00195; DYNAMIN.
DR   SMART; SM00053; DYNc; 1.
DR   SMART; SM00302; GED; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS00410; DYNAMIN; 1.
DR   PROSITE; PS51388; GED; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell junction; Cell membrane;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; Endocytosis;
KW   GTP-binding; Hydrolase; Membrane; Microtubule; Motor protein;
KW   Nucleotide-binding; Phosphoprotein; Postsynaptic cell membrane;
KW   Synapse.
FT   CHAIN         1    870       Dynamin-2.
FT                                /FTId=PRO_0000206571.
FT   DOMAIN      519    625       PH.
FT   DOMAIN      653    744       GED.
FT   NP_BIND      38     45       GTP (By similarity).
FT   NP_BIND     136    140       GTP (By similarity).
FT   NP_BIND     205    208       GTP (By similarity).
FT   COMPBIAS    747    866       Pro-rich.
FT   MOD_RES     298    298       Phosphoserine.
FT   MOD_RES     302    302       Phosphoserine.
FT   MOD_RES     449    449       Phosphotyrosine (By similarity).
FT   MOD_RES     597    597       Phosphotyrosine.
FT   MOD_RES     598    598       N6-acetyllysine (By similarity).
FT   MOD_RES     766    766       Phosphothreonine (By similarity).
FT   VAR_SEQ     516    519       Missing (in isoform 2).
FT                                /FTId=VSP_001326.
FT   CONFLICT    297    298       RS -> HG (in Ref. 1; AAA40523).
FT   CONFLICT    848    870       SRRAPAAPSRPTIIRPAEPSLLD -> RRPPPLAPARPFF
FT                                (in Ref. 2; BAB23745).
SQ   SEQUENCE   870 AA;  98145 MW;  E80864AF94B8F778 CRC64;
     MGNRGMEELI PLVNKLQDAF SSIGQSCHLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
     SGIVTRRPLI LQLIFSKTEY AEFLHCKSKK FTDFDEVRQE IEAETDRVTG TNKGISPVPI
     NLRVYSPHVL NLTLIDLPGI TKVPVGDQPP DIEYQIKDMI LQFISRESSL ILAVTPANMD
     LANSDALKLA KEVDPQGLRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK
     DIEGKKDIRA ALAAERKFFL SHPAYRHMAD RMGTPHLQKT LNQQLTNHIR ESLPTLRSKL
     QSQLLSLEKE VEEYKNFRPD DPTRKTKALL QMVQQFGVDF EKRIEGSGDQ VDTLELSGGA
     RINRIFHERF PFELVKMEFD EKDLRREISY AIKNIHGVRT GLFTPDLAFE AIVKKQVVKL
     KEPCLKCVDL VIQELISTVR QCTSKLSSYP RLREETERIV TTYIREREGR TKDQILLLID
     IEQSYINTNH EDFIGFANAQ QRSTQLNKKR AIPNQGEILV IRRGWLTINN ISLMKGGSKE
     YWFVLTAESL SWYKDEEEKE KKYMLPLDNL KIRDVEKGFM SNKHVFAIFN TEQRNVYKDL
     RQIELACDSQ EDVDSWKASF LRAGVYPEKD QAENEDGAQE NTFSMDPQLE RQVETIRNLV
     DSYVAIINKS IRDLMPKTIM HLMINNTKAF IHHELLAYLY SSADQSSLME ESAEQAQRRD
     DMLRMYHALK EALNIIGDIS TSTVSTPVPP PVDDTWLQNT SGHSPTPQRR PVSSVHPPGR
     PPAVRGPTPG PPLIPMPVGA TSSFSAPPIP SRPGPQSVFA NNDPFSAPPQ IPSRPARIPP
     GIPPGVPSRR APAAPSRPTI IRPAEPSLLD
//
ID   TRAF1_MOUSE             Reviewed;         409 AA.
AC   P39428;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=TNF receptor-associated factor 1;
GN   Name=Traf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 123-135 AND 390-402,
RP   AND INTERACTION WITH TRAF2 AND TNFRSF1B.
RX   MEDLINE=94349371; PubMed=8069916; DOI=10.1016/0092-8674(94)90532-0;
RA   Rothe M., Wong S.C., Henzel W.J., Goeddel D.V.;
RT   "A novel family of putative signal transducers associated with the
RT   cytoplasmic domain of the 75 kDa tumor necrosis factor receptor.";
RL   Cell 78:681-692(1994).
RN   [2]
RP   INTERACTION WITH TRAIP.
RX   MEDLINE=97258620; PubMed=9104814; DOI=10.1084/jem.185.7.1275;
RA   Lee S.Y., Lee S.Y., Choi Y.;
RT   "TRAF-interacting protein (TRIP): a novel component of the tumor
RT   necrosis factor receptor (TNFR)- and CD30-TRAF signaling complexes
RT   that inhibits TRAF2-mediated NF-kappaB activation.";
RL   J. Exp. Med. 185:1275-1285(1997).
RN   [3]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=11672546; DOI=10.1016/S1074-7613(01)00207-2;
RA   Tsitsikov E.N., Laouini D., Dunn I.F., Sannikova T.Y., Davidson L.,
RA   Alt F.W., Geha R.S.;
RT   "TRAF1 is a negative regulator of TNF signaling. enhanced TNF
RT   signaling in TRAF1-deficient mice.";
RL   Immunity 15:647-657(2001).
RN   [4]
RP   INTERACTION WITH HIVEP3.
RX   PubMed=11804591; DOI=10.1016/S1097-2765(01)00434-8;
RA   Oukka M., Kim S.T., Lugo G., Sun J., Wu L.-C., Glimcher L.H.;
RT   "A mammalian homolog of Drosophila schnurri, KRC, regulates TNF
RT   receptor-driven responses and interacts with TRAF2.";
RL   Mol. Cell 9:121-131(2002).
RN   [5]
RP   INTERACTION WITH NFATC2IP.
RX   PubMed=16352630; DOI=10.1093/intimm/dxh354;
RA   Bryce P.J., Oyoshi M.K., Kawamoto S., Oettgen H.C., Tsitsikov E.N.;
RT   "TRAF1 regulates Th2 differentiation, allergic inflammation and
RT   nuclear localization of the Th2 transcription factor, NIP45.";
RL   Int. Immunol. 18:101-111(2006).
RN   [6]
RP   FUNCTION, PHOSPHORYLATION AT SER-139, INTERACTION WITH TNFRSF1B, AND
RP   MUTAGENESIS OF SER-139.
RX   PubMed=18429822; DOI=10.1111/j.1365-2443.2008.01182.x;
RA   Kato T. Jr., Gotoh Y., Hoffmann A., Ono Y.;
RT   "Negative regulation of constitutive NF-kappaB and JNK signaling by
RT   PKN1-mediated phosphorylation of TRAF1.";
RL   Genes Cells 13:509-520(2008).
RN   [7]
RP   INTERACTION WITH TRAFD1.
RX   PubMed=18849341; DOI=10.1074/jbc.M806923200;
RA   Sanada T., Takaesu G., Mashima R., Yoshida R., Kobayashi T.,
RA   Yoshimura A.;
RT   "FLN29 deficiency reveals its negative regulatory role in the Toll-
RT   like receptor (TLR) and retinoic acid-inducible gene I (RIG-I)-like
RT   helicase signaling pathway.";
RL   J. Biol. Chem. 283:33858-33864(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Adapter molecule that regulates the activation of NF-
CC       kappa-B and JNK. Plays a role in the regulation of cell survival
CC       and apoptosis. The heterotrimer formed by TRAF1 and TRAF2 is part
CC       of a E3 ubiquitin-protein ligase complex that promotes
CC       ubiquitination of target proteins, such as MAP3K14. The
CC       TRAF1/TRAF2 complex recruits the antiapoptotic E3 protein-
CC       ubiquitin ligases BIRC2 and BIRC3 to TNFRSF1B/TNFR2 (By
CC       similarity).
CC   -!- SUBUNIT: Homotrimer. Heterotrimer with TRAF2. Interacts with
CC       TNFRSF1A/TNFR1, TNFRSF1B/TNFR2, TNFRSF4, TNFRSF5/CD40,
CC       TNFRSF8/CD30, TNFRSF9/CD137, TNFRSF11A/RANK, TNFRSF13C,
CC       TNFRSF18/AITR, TNFRSF17/BCMA, TNFRSF19/TROY, TNFRSF19L/RELT,
CC       XEDAR, EDAR, Epstein-Barr virus BNFL1/LMP-1, TANK/ITRAF, TRAIP and
CC       RIPK2. Interacts with BIRC2 and BIRC3 N-terminus; a single BIRC2
CC       or BIRC3 molecule interacts with a heterotrimer formed by TRAF1
CC       and TRAF2. Interacts with MAP3K14 (By similarity). Interacts with
CC       NFATC2IP, TRAFD1 and with HIVEP3.
CC   -!- INTERACTION:
CC       Q9UNE0:EDAR (xeno); NbExp=1; IntAct=EBI-520123, EBI-529289;
CC       P20333:TNFRSF1B (xeno); NbExp=1; IntAct=EBI-520123, EBI-358983;
CC       P28908:TNFRSF8 (xeno); NbExp=1; IntAct=EBI-520123, EBI-529023;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: The coiled coil domain mediates homo- and hetero-
CC       oligomerization (By similarity).
CC   -!- DOMAIN: The MATH/TRAF domain binds to receptor cytoplasmic
CC       domains.
CC   -!- DOMAIN: Cleavage by CASP8 liberates a C-terminal fragment that
CC       promotes apoptosis and inhibits the activation of NF-kappa-B in
CC       response to TNF signaling (By similarity).
CC   -!- PTM: Polyubiquitinated by BIRC2 and/or BIRC3, leading to its
CC       subsequent proteasomal degradation (By similarity).
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice have normal B-
CC       cell proliferation and antibody response, but increased T-cell
CC       proliferation in response to CD3 signaling. Their T-cells show
CC       enhanced activation of JNK and NF-kappa-B. Mice are highly
CC       susceptible to TNF-induced skin necrosis.
CC   -!- SIMILARITY: Contains 1 MATH domain.
CC   -!- CAUTION: Lacks a RING domain and has therefore no E3 ubiquitin-
CC       protein ligase activity by itself.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; L35302; AAC37663.1; -; mRNA.
DR   IPI; IPI00135899; -.
DR   PIR; A54750; A54750.
DR   UniGene; Mm.239514; -.
DR   ProteinModelPortal; P39428; -.
DR   SMR; P39428; 174-409.
DR   DIP; DIP-260N; -.
DR   IntAct; P39428; 5.
DR   STRING; P39428; -.
DR   PhosphoSite; P39428; -.
DR   PRIDE; P39428; -.
DR   Ensembl; ENSMUST00000028234; ENSMUSP00000028234; ENSMUSG00000026875.
DR   Ensembl; ENSMUST00000113064; ENSMUSP00000108687; ENSMUSG00000026875.
DR   MGI; MGI:101836; Traf1.
DR   eggNOG; roNOG08042; -.
DR   HOGENOM; HBG506127; -.
DR   HOVERGEN; HBG058222; -.
DR   InParanoid; P39428; -.
DR   OrthoDB; EOG42Z4Q6; -.
DR   ArrayExpress; P39428; -.
DR   Bgee; P39428; -.
DR   CleanEx; MM_TRAF1; -.
DR   Genevestigator; P39428; -.
DR   GermOnline; ENSMUSG00000026875; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR002083; MATH.
DR   InterPro; IPR012227; TNF_recpt_TRAF.
DR   InterPro; IPR008974; TRAF-like.
DR   InterPro; IPR013322; TRAF-type.
DR   Gene3D; G3DSA:2.60.210.10; TRAF-type; 1.
DR   Pfam; PF00917; MATH; 1.
DR   PIRSF; PIRSF015614; TRAF; 1.
DR   SMART; SM00061; MATH; 1.
DR   SUPFAM; SSF49599; Traf_like; 1.
DR   PROSITE; PS50144; MATH; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Coiled coil; Cytoplasm; Direct protein sequencing;
KW   Isopeptide bond; Phosphoprotein; Ubl conjugation.
FT   CHAIN         1    409       TNF receptor-associated factor 1.
FT                                /FTId=PRO_0000056398.
FT   DOMAIN      259    405       MATH.
FT   COILED      167    256       By similarity.
FT   SITE        156    157       Cleavage; by CASP8 (By similarity).
FT   MOD_RES      63     63       Phosphoserine.
FT   MOD_RES     139    139       Phosphoserine.
FT   CROSSLNK    178    178       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK    186    186       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   MUTAGEN     139    139       S->A: Loss of phosphorylation site.
FT                                Reduces global phosphorylation.
SQ   SEQUENCE   409 AA;  45465 MW;  EBA7FEE5639FEDDF CRC64;
     MASSSAPDEN EFQFGCPPAP CQDPSEPRVL CCTACLSENL RDDEDRICPK CRADNLHPVS
     PGSPLTQEKV HSDVAEAEIM CPFAGVGCSF KGSPQSMQEH EATSQSSHLY LLLAVLKEWK
     SSPGSNLGSA PMALERNLSE LQLQAAVEAT GDLEVDCYRA PCCESQEELA LQHLVKEKLL
     AQLEEKLRVF ANIVAVLNKE VEASHLALAA SIHQSQLDRE HLLSLEQRVV ELQQTLAQKD
     QVLGKLEHSL RLMEEASFDG TFLWKITNVT KRCHESVCGR TVSLFSPAFY TAKYGYKLCL
     RLYLNGDGSG KKTHLSLFIV IMRGEYDALL PWPFRNKVTF MLLDQNNREH AIDAFRPDLS
     SASFQRPQSE TNVASGCPLF FPLSKLQSPK HAYVKDDTMF LKCIVDTSA
//
ID   ZO1_MOUSE               Reviewed;        1745 AA.
AC   P39447;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   08-MAR-2011, entry version 109.
DE   RecName: Full=Tight junction protein ZO-1;
DE   AltName: Full=Tight junction protein 1;
DE   AltName: Full=Zona occludens protein 1;
DE   AltName: Full=Zonula occludens protein 1;
GN   Name=Tjp1; Synonyms=Zo1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129;
RX   MEDLINE=93252986; PubMed=8486731; DOI=10.1083/jcb.121.3.491;
RA   Itoh M., Nagafuchi A., Yonemura S., Yasuda-Kitani T., Tsukita S.,
RA   Tsukita S.;
RT   "The 220-kD protein colocalizing with cadherins in non-epithelial
RT   cells is identical to ZO-1, a tight junction-associated protein in
RT   epithelial cells: cDNA cloning and immunoelectron microscopy.";
RL   J. Cell Biol. 121:491-502(1993).
RN   [2]
RP   INTERACTION WITH KIRREL1.
RC   STRAIN=Swiss Webster; TISSUE=Brain;
RX   PubMed=12424224; DOI=10.1096/fj.02-0242fje;
RA   Sellin L., Huber T.B., Gerke P., Quack I., Pavenstaedt H., Walz G.;
RT   "NEPH1 defines a novel family of podocin interacting proteins.";
RL   FASEB J. 17:115-117(2003).
RN   [3]
RP   INTERACTION WITH GJA12, AND DOMAIN.
RX   PubMed=15183511; DOI=10.1016/j.neuroscience.2004.03.063;
RA   Li X., Ionescu A.V., Lynn B.D., Lu S., Kamasawa N., Morita M.,
RA   Davidson K.G.V., Yasumura T., Rash J.E., Nagy J.I.;
RT   "Connexin47, connexin29 and connexin32 co-expression in
RT   oligodendrocytes and Cx47 association with zonula occludens-1 (ZO-1)
RT   in mouse brain.";
RL   Neuroscience 126:611-630(2004).
RN   [4]
RP   INTERACTION WITH BVES.
RX   PubMed=16188940; DOI=10.1242/jcs.02588;
RA   Osler M.E., Chang M.S., Bader D.M.;
RT   "Bves modulates epithelial integrity through an interaction at the
RT   tight junction.";
RL   J. Cell Sci. 118:4667-4678(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1139 AND TYR-1353, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175; SER-284; SER-297;
RP   SER-300 AND SER-617, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-912, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-175; SER-178;
RP   SER-179; SER-300; SER-617 AND SER-912, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1164, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: The N-terminal may be involved in transducing a signal
CC       required for tight junction assembly, while the C-terminal may
CC       have specific properties of tight junctions. The alpha domain
CC       might be involved in stabilizing junctions.
CC   -!- SUBUNIT: Homodimer, and heterodimer with TJP2/ZO-2 and TJP3/ZO-3.
CC       Interacts with CGN/cingulin, CXADR, GJD3, HSPA4 and UBN1 (By
CC       similarity). Interacts with occludin, claudins, GJA12 and KIRREL1.
CC       Interacts with BVES (via the C-terminus cytoplasmic tail).
CC   -!- INTERACTION:
CC       P57780:Actn4; NbExp=3; IntAct=EBI-79508, EBI-445071;
CC       Q9P2M7:CGN (xeno); NbExp=1; IntAct=EBI-79508, EBI-79537;
CC       Q9PTD7:cgn (xeno); NbExp=1; IntAct=EBI-79508, EBI-79525;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity). Cell junction, tight junction
CC       (By similarity). Note=Movement of ZO-1 from the cytoplasm to
CC       membrane is an early event occurring concurrently with cell-cell
CC       contact (By similarity).
CC   -!- DOMAIN: The second PDZ domain mediates interaction with GJA12.
CC   -!- PTM: Phosphorylated. Dephosphorylated by PTPRJ (By similarity).
CC   -!- SIMILARITY: Belongs to the MAGUK family.
CC   -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC   -!- SIMILARITY: Contains 3 PDZ (DHR) domains.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SIMILARITY: Contains 1 ZU5 domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; D14340; BAA03274.1; -; mRNA.
DR   IPI; IPI00135971; -.
DR   PIR; A46431; A46431.
DR   UniGene; Mm.4342; -.
DR   ProteinModelPortal; P39447; -.
DR   SMR; P39447; 18-266, 422-513, 516-803, 1631-1745.
DR   DIP; DIP-30946N; -.
DR   IntAct; P39447; 11.
DR   MINT; MINT-113090; -.
DR   STRING; P39447; -.
DR   PhosphoSite; P39447; -.
DR   PRIDE; P39447; -.
DR   Ensembl; ENSMUST00000102592; ENSMUSP00000099652; ENSMUSG00000030516.
DR   UCSC; uc009hgp.1; mouse.
DR   MGI; MGI:98759; Tjp1.
DR   eggNOG; roNOG11407; -.
DR   HOVERGEN; HBG007849; -.
DR   OrthoDB; EOG4WSW8R; -.
DR   NextBio; 301376; -.
DR   ArrayExpress; P39447; -.
DR   Bgee; P39447; -.
DR   CleanEx; MM_TJP1; -.
DR   Genevestigator; P39447; -.
DR   GermOnline; ENSMUSG00000030516; Mus musculus.
DR   GO; GO:0005913; C:cell-cell adherens junction; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0046581; C:intercellular canaliculus; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005923; C:tight junction; IDA:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR   GO; GO:0001825; P:blastocyst formation; IMP:MGI.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR005417; ZonOcculdens.
DR   InterPro; IPR005418; ZonOcculS1.
DR   InterPro; IPR000906; ZU5.
DR   PANTHER; PTHR13865:SF9; ZonOcculS1; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF00595; PDZ; 3.
DR   Pfam; PF07653; SH3_2; 1.
DR   Pfam; PF00791; ZU5; 1.
DR   PRINTS; PR01597; ZONOCCLUDNS.
DR   PRINTS; PR01598; ZONOCCLUDNS1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 3.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00218; ZU5; 1.
DR   SUPFAM; SSF50156; PDZ; 3.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; FALSE_NEG.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 3.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS51145; ZU5; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Membrane; Phosphoprotein; Repeat;
KW   SH3 domain; Tight junction.
FT   CHAIN         1   1745       Tight junction protein ZO-1.
FT                                /FTId=PRO_0000094541.
FT   DOMAIN       23    110       PDZ 1.
FT   DOMAIN      186    264       PDZ 2.
FT   DOMAIN      421    502       PDZ 3.
FT   DOMAIN      516    584       SH3.
FT   DOMAIN      610    791       Guanylate kinase-like.
FT   DOMAIN     1629   1721       ZU5.
FT   COMPBIAS   1242   1247       Poly-Pro.
FT   COMPBIAS   1424   1430       Poly-Pro.
FT   MOD_RES     125    125       Phosphoserine.
FT   MOD_RES     131    131       Phosphoserine (By similarity).
FT   MOD_RES     132    132       Phosphotyrosine (By similarity).
FT   MOD_RES     166    166       Phosphoserine (By similarity).
FT   MOD_RES     168    168       Phosphoserine (By similarity).
FT   MOD_RES     175    175       Phosphoserine.
FT   MOD_RES     178    178       Phosphoserine.
FT   MOD_RES     179    179       Phosphoserine.
FT   MOD_RES     275    275       Phosphoserine (By similarity).
FT   MOD_RES     277    277       Phosphoserine (By similarity).
FT   MOD_RES     280    280       Phosphoserine (By similarity).
FT   MOD_RES     284    284       Phosphoserine.
FT   MOD_RES     297    297       Phosphoserine.
FT   MOD_RES     300    300       Phosphoserine.
FT   MOD_RES     329    329       Phosphoserine (By similarity).
FT   MOD_RES     337    337       Phosphoserine (By similarity).
FT   MOD_RES     353    353       Phosphoserine (By similarity).
FT   MOD_RES     354    354       Phosphothreonine (By similarity).
FT   MOD_RES     402    402       Phosphoserine (By similarity).
FT   MOD_RES     617    617       Phosphoserine.
FT   MOD_RES     868    868       Phosphothreonine (By similarity).
FT   MOD_RES     912    912       Phosphoserine.
FT   MOD_RES     927    927       Phosphoserine (By similarity).
FT   MOD_RES    1139   1139       Phosphotyrosine.
FT   MOD_RES    1164   1164       Phosphotyrosine.
FT   MOD_RES    1353   1353       Phosphotyrosine.
FT   MOD_RES    1365   1365       Phosphoserine (By similarity).
FT   MOD_RES    1542   1542       Phosphoserine (By similarity).
FT   MOD_RES    1614   1614       Phosphoserine (By similarity).
FT   MOD_RES    1616   1616       Phosphoserine (By similarity).
SQ   SEQUENCE   1745 AA;  194711 MW;  C3DA2C0A9F411F66 CRC64;
     MSARAAAAKS TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG ETSIVISDVL
     KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK NAKITIRRKK KVQIPVSHPD
     PEPVSDNEDD SYDEEVHDPR AGRGALANRR SEKSWARDRS ASRERSLSPR SDRRSVASSQ
     PAKPTKVTLV KSRKNEEYGL RPASHIFVKE ISQDSLAARD GDIQEGDVVL KINGTVTENM
     SLTDAKTLIE RSKGKLKMVV QRDERATLLN VPDLSDSIHS ANASERDDIS EIQSLASDHS
     GRSHDRPPRR SQSRSPDQRS EPSDHSTQSP QQPSNGSLRS REEERMSKPG AISTPVKHVD
     DHPPKAVEEV TVEKNEKQTP TLPEPKPVYA QVGQPDVDLP VSPSDGALPN SAHEDGILRP
     SMKLVKFRKG DSVGLRLAGG NDVGIFVAGV LEDSPAAKEG LEEGDQILRV NNVDFTNIIR
     EEAVLFLLDL PKGEEVTILA QKKKDVYRRI VESDVGDSFY IRTHFEYEKE SPYGLSFNKG
     EVFRVVDTLY NGKLGSWLAI RIGKNHKEVE RGIIPNKNRA EQLASVQYTL PKTAGGDRAD
     FWRFRGLRSS KRNLRKSRED LSAQPVQTKF PAYERVVLRE AGFLRPVTIF GPIADVAREK
     LAREEPDIYQ IAKSELRDAG TDHRSSGIIR LHTIKQIIDQ DKHALLDVTP NAVDRLNYAQ
     WYPIVVFLNP DSKQGVKTMR MRLCPESRKS ARKLYERSHK LRKNNHHLFT TTINLNSMND
     GWYGALKEAI QQQQNQLVWV SEGKADGATS DDLDLHDDRL SYLSAPGSEY SMYSTDSRHT
     SDYEDTDTEG GAYTDQELDE TLNDEVGTPP ESAITRSSEP VREDSSGMHH ENQTYPPYSP
     QAQPQAIHRI DSPGLKPASQ QKAEASSPVP YLSPETTPAS SASAVNHNVS VTNVSLEEPA
     PAPPTSHASQ PGCLGAPSAE AAHVGLRGEG PPLPPHADPA KVYRKEPYSE EMMRQNHILK
     QPALGHPGQR PDKEPNLAYE PQLPYIEKQA SRDLEQPSYR YEVSSYTDQF SRNYDHRLRF
     EDRIPTYEDQ WSYYDDKQPY QPRPFENQHP RDLDSRQHPE EASERGYFQR FEEPAPLSYD
     SRTRYEQLPR TSTLRHEEQP APAYEVHNRY RPEAQPYSST GPKSSEPKQY FDQYPRSYEQ
     VPPPGFTSKT GHYEPLHGAA VVPPLIPSSQ QKPEVLRSAT KPQPPPPTLT EEEEDPAMKP
     QSVLTRVKMF ENKRSASLEN KKDVNDTASF KPPEVASKPP GASLAGPKPV PQSQFSEHDK
     TLYRLPEPQK PQVKPPEDIV RSNHYDPEED EEYYRKQLSY FDRRSFESKP SAHLPAGHHS
     EPAKPVHSQS QPNFPSYSSK GKPETDAVDR SFSEKRYDPA QATPPPPPLP SQYSQPAPPL
     SSSSLHIHSK GAQGEGNSVS LDFQNSYMSK PDPPPSQSKP ATFRPPTRED PPQTFYPQKS
     FPDKAPVNGA EQTQKTITPV YNRFTPKPYT SSARPFERKF ESPKFNHNLL PSETVHKPEL
     SSKTPTSPKT LMKAHSSTQP PEFGSGVETF SVHTDKPKYQ MNNISTMPKA VPVSPSAVEE
     DEDEDGHTVV ATARGIFNSN GGVLSSIETG VSIIIPQGAI PEGIEQEIYF KVCRDNSILP
     PLDKEKGETL LSPLVMCGPH GLKFLKPVEL RLPHCDPKTW QNKCLPGDPN YLVGANCVSV
     LIDHF
//
ID   FYN_MOUSE               Reviewed;         537 AA.
AC   P39688; Q3TAT3; Q3U0T5; Q8K2A3;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 3.
DT   08-MAR-2011, entry version 113.
DE   RecName: Full=Tyrosine-protein kinase Fyn;
DE            EC=2.7.10.2;
DE   AltName: Full=Proto-oncogene c-Fyn;
DE   AltName: Full=p59-Fyn;
GN   Name=Fyn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   MEDLINE=91175680; PubMed=2488273;
RA   Cooke M.P., Perlmutter R.M.;
RT   "Expression of a novel form of the fyn proto-oncogene in hematopoietic
RT   cells.";
RL   New Biol. 1:66-74(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=T-cell;
RX   PubMed=9895129;
RA   Lee C., Kim M.G., Jeon S.H., Park D.E., Park S.D., Seong R.H.;
RT   "Two species of mRNAs for the fyn proto-oncogene are produced by an
RT   alternative polyadenylation.";
RL   Mol. Cells 8:746-749(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=NOD; TISSUE=Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=1361685; DOI=10.1126/science.1361685;
RA   Grant S.G., O'Dell T.J., Karl K.A., Stein P.L., Soriano P.,
RA   Kandel E.R.;
RT   "Impaired long-term potentiation, spatial learning, and hippocampal
RT   development in fyn mutant mice.";
RL   Science 258:1903-1910(1992).
RN   [6]
RP   PHOSPHORYLATION AT TYR-531, AUTOPHOSPHORYLATION AT TYR-420, AND ENZYME
RP   REGULATION.
RX   PubMed=8441403;
RA   Hurley T.R., Hyman R., Sefton B.M.;
RT   "Differential effects of expression of the CD45 tyrosine protein
RT   phosphatase on the tyrosine phosphorylation of the lck, fyn, and c-src
RT   tyrosine protein kinases.";
RL   Mol. Cell. Biol. 13:1651-1656(1993).
RN   [7]
RP   PALMITOYLATION AT CYS-3 AND CYS-6, AND MUTAGENESIS OF CYS-3 AND CYS-6.
RX   MEDLINE=94019312; PubMed=8413237;
RA   Shenoy-Scaria A.M., Timson L.K., Kwong J., Shaw A.S., Lublin D.M.;
RT   "Palmitylation of an amino-terminal cysteine motif of protein tyrosine
RT   kinases p56lck and p59fyn mediates interaction with glycosyl-
RT   phosphatidylinositol-anchored proteins.";
RL   Mol. Cell. Biol. 13:6385-6392(1993).
RN   [8]
RP   PALMITOYLATION AT CYS-3 AND CYS-6, AND MUTAGENESIS OF GLY-2; CYS-3 AND
RP   CYS-6.
RX   MEDLINE=95071286; PubMed=7980442;
RA   Koegl M., Zlatkine P., Ley S.C., Courtneidge S.A., Magee A.I.;
RT   "Palmitoylation of multiple Src-family kinases at a homologous N-
RT   terminal motif.";
RL   Biochem. J. 303:749-753(1994).
RN   [9]
RP   INTERACTION WITH CD79A.
RX   PubMed=8168489;
RA   Clark M.R., Johnson S.A., Cambier J.C.;
RT   "Analysis of Ig-alpha-tyrosine kinase interaction reveals two levels
RT   of binding specificity and tyrosine phosphorylated Ig-alpha
RT   stimulation of Fyn activity.";
RL   EMBO J. 13:1911-1919(1994).
RN   [10]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=8007959;
RA   Davidson D., Viallet J., Veillette A.;
RT   "Unique catalytic properties dictate the enhanced function of p59fynT,
RT   the hemopoietic cell-specific isoform of the Fyn tyrosine protein
RT   kinase, in T cells.";
RL   Mol. Cell. Biol. 14:4554-4564(1994).
RN   [11]
RP   MYRISTOYLATION AT GLY-2.
RX   MEDLINE=96251668; PubMed=8655574; DOI=10.1083/jcb.133.5.1007;
RA   Gauen L.K.T., Linder M.E., Shaw A.S.;
RT   "Multiple features of the p59fyn src homology 4 domain define a motif
RT   for immune-receptor tyrosine-based activation motif (ITAM) binding and
RT   for plasma membrane localization.";
RL   J. Cell Biol. 133:1007-1015(1996).
RN   [12]
RP   PALMITOYLATION AT CYS-3, AND MUTAGENESIS OF CYS-3.
RX   MEDLINE=97345356; PubMed=9201723;
RA   Wolven A., Okamura H., Rosenblatt Y., Resh M.D.;
RT   "Palmitoylation of p59fyn is reversible and sufficient for plasma
RT   membrane association.";
RL   Mol. Biol. Cell 8:1159-1173(1997).
RN   [13]
RP   INTERACTION WITH TOM1L1.
RX   MEDLINE=21659738; PubMed=11711534; DOI=10.1074/jbc.M106813200;
RA   Seykora J.T., Mei L., Dotto G.P., Stein P.L.;
RT   "'Srcasm: a novel Src activating and signaling molecule.";
RL   J. Biol. Chem. 277:2812-2822(2002).
RN   [14]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12218089;
RA   Yasuda K., Nagafuku M., Shima T., Okada M., Yagi T., Yamada T.,
RA   Minaki Y., Kato A., Tani-Ichi S., Hamaoka T., Kosugi A.;
RT   "Fyn is essential for tyrosine phosphorylation of Csk-binding
RT   protein/phosphoprotein associated with glycolipid-enriched
RT   microdomains in lipid rafts in resting T cells.";
RL   J. Immunol. 169:2813-2817(2002).
RN   [15]
RP   SUBCELLULAR LOCATION.
RX   PubMed=14645715; DOI=10.1073/pnas.2432139100;
RA   Shima T., Nada S., Okada M.;
RT   "Transmembrane phosphoprotein Cbp senses cell adhesion signaling
RT   mediated by Src family kinase in lipid rafts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:14897-14902(2003).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-185 AND TYR-531, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-420, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-254 AND SER-257, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Implicated in the control of cell growth. Plays a role
CC       in the regulation of intracellular calcium levels, with isoform 2
CC       showing the greater ability to mobilize cytoplasmic calcium in
CC       comparison to isoform 1. Required in brain development and mature
CC       brain function with important roles in the regulation of axon
CC       growth, axon guidance, and neurite extension. Blocks axon
CC       outgrowth and attraction induced by NTN1 by phosphorylating its
CC       receptor DDC.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- COFACTOR: Manganese.
CC   -!- ENZYME REGULATION: Inhibited by phosphorylation of Tyr-531 by
CC       leukocyte common antigen and activated by dephosphorylation of
CC       this site.
CC   -!- SUBUNIT: Interacts (via its SH3 domain) with PIK3R1 and PRMT8.
CC       Interacts with FYB, PAG1, and SH2D1A (By similarity). Interacts
CC       with SH2D1A and SLAMF1. Interacts with ITCH; the interaction
CC       phosphorylates ITCH and negatively regulates its activity (By
CC       similarity). Interacts with CD79A (tyrosine-phosphorylated form);
CC       the interaction increases FYN activity. Interacts with TOM1L1
CC       (phosphorylated form). Interacts with FASLG (By similarity).
CC   -!- INTERACTION:
CC       P51807:Dynlt1; NbExp=2; IntAct=EBI-524514, EBI-642797;
CC       P49710:Hcls1; NbExp=1; IntAct=EBI-524514, EBI-924601;
CC       Q60749:Khdrbs1; NbExp=4; IntAct=EBI-524514, EBI-519077;
CC       Q9H204:MED28 (xeno); NbExp=1; IntAct=EBI-524514, EBI-514199;
CC       Q920D3:Med28; NbExp=1; IntAct=EBI-524514, EBI-309215;
CC       Q80YF9:Snx26; NbExp=1; IntAct=EBI-524514, EBI-1210140;
CC       Q9JIA7:Sphk2; NbExp=2; IntAct=EBI-524514, EBI-985434;
CC   -!- SUBCELLULAR LOCATION: Cell membrane. Note=Present and active in
CC       lipid rafts. Present in cell body and along the process of mature
CC       and developing oligodendroyctes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=B;
CC         IsoId=P39688-1; Sequence=Displayed;
CC       Name=2; Synonyms=T;
CC         IsoId=P39688-2; Sequence=VSP_024111, VSP_024112;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is highly expressed in the brain,
CC       isoform 2 is expressed in cells of hemopoietic lineages,
CC       especially T lymphocytes.
CC   -!- PTM: It is uncertain whether palmitoylation is on Cys-3 and/or
CC       Cys-6.
CC   -!- PTM: Myristoylation is required prior to palmitoylation.
CC   -!- DISRUPTION PHENOTYPE: Mice have various neural defects, including
CC       defective long term potentiation, impaired spatial memory,
CC       hypomyelination, abnormal dendrite orientation and uncoordinated
CC       hippocampal structure.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. SRC subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; M27266; AAA37644.1; -; mRNA.
DR   EMBL; U70324; AAB09568.1; -; mRNA.
DR   EMBL; AK156584; BAE33766.1; -; mRNA.
DR   EMBL; AK171646; BAE42585.1; -; mRNA.
DR   EMBL; BC032149; AAH32149.1; -; mRNA.
DR   EMBL; BC092217; AAH92217.1; -; mRNA.
DR   IPI; IPI00322097; -.
DR   IPI; IPI00762435; -.
DR   PIR; A44991; A44991.
DR   RefSeq; NP_001116364.1; NM_001122892.1.
DR   RefSeq; NP_001116365.1; NM_001122893.1.
DR   RefSeq; NP_032080.2; NM_008054.2.
DR   UniGene; Mm.4848; -.
DR   ProteinModelPortal; P39688; -.
DR   SMR; P39688; 84-537.
DR   DIP; DIP-198N; -.
DR   IntAct; P39688; 28.
DR   MINT; MINT-85422; -.
DR   STRING; P39688; -.
DR   PhosphoSite; P39688; -.
DR   PRIDE; P39688; -.
DR   Ensembl; ENSMUST00000063091; ENSMUSP00000057707; ENSMUSG00000019843.
DR   Ensembl; ENSMUST00000099967; ENSMUSP00000097547; ENSMUSG00000019843.
DR   GeneID; 14360; -.
DR   KEGG; mmu:14360; -.
DR   UCSC; uc007evz.1; mouse.
DR   CTD; 14360; -.
DR   MGI; MGI:95602; Fyn.
DR   eggNOG; roNOG12442; -.
DR   GeneTree; ENSGT00600000084003; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG008761; -.
DR   InParanoid; P39688; -.
DR   OrthoDB; EOG41ZF9H; -.
DR   BRENDA; 2.7.10.2; 244.
DR   NextBio; 285821; -.
DR   ArrayExpress; P39688; -.
DR   Bgee; P39688; -.
DR   CleanEx; MM_FYN; -.
DR   Genevestigator; P39688; -.
DR   GermOnline; ENSMUSG00000019843; Mus musculus.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:EC.
DR   GO; GO:0015631; F:tubulin binding; IDA:MGI.
DR   GO; GO:0050798; P:activated T cell proliferation; IMP:MGI.
DR   GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IMP:MGI.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0042552; P:myelination; TAS:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:BHF-UCL.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR   GO; GO:0008360; P:regulation of cell shape; IDA:MGI.
DR   GO; GO:0045471; P:response to ethanol; IGI:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell membrane;
KW   Developmental protein; Kinase; Lipoprotein; Manganese; Membrane;
KW   Metal-binding; Myristate; Nucleotide-binding; Palmitate;
KW   Phosphoprotein; Proto-oncogene; SH2 domain; SH3 domain; Transferase;
KW   Tyrosine-protein kinase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    537       Tyrosine-protein kinase Fyn.
FT                                /FTId=PRO_0000088100.
FT   DOMAIN       82    143       SH3.
FT   DOMAIN      149    246       SH2.
FT   DOMAIN      271    524       Protein kinase.
FT   NP_BIND     277    285       ATP (By similarity).
FT   ACT_SITE    390    390       Proton acceptor (By similarity).
FT   BINDING     299    299       ATP (By similarity).
FT   MOD_RES      15     15       Phosphothreonine (By similarity).
FT   MOD_RES      21     21       Phosphoserine.
FT   MOD_RES      25     25       Phosphoserine (By similarity).
FT   MOD_RES     185    185       Phosphotyrosine.
FT   MOD_RES     213    213       Phosphotyrosine (By similarity).
FT   MOD_RES     214    214       Phosphotyrosine (By similarity).
FT   MOD_RES     254    254       Phosphothreonine.
FT   MOD_RES     257    257       Phosphoserine.
FT   MOD_RES     420    420       Phosphotyrosine; by autocatalysis.
FT   MOD_RES     440    440       Phosphotyrosine (By similarity).
FT   MOD_RES     512    512       Phosphothreonine (By similarity).
FT   MOD_RES     531    531       Phosphotyrosine.
FT   LIPID         2      2       N-myristoyl glycine.
FT   LIPID         3      3       S-palmitoyl cysteine.
FT   LIPID         6      6       S-palmitoyl cysteine (Probable).
FT   VAR_SEQ     234    236       RAA -> KAD (in isoform 2).
FT                                /FTId=VSP_024111.
FT   VAR_SEQ     240    283       CRLVVPCHKGMPRLTDLSVKTKDVWEIPRESLQLIKRLGNG
FT                                QFG -> FNLTVVSSSCTPQTSGLAKDAWEVARDSLFLEKK
FT                                LGQGCFA (in isoform 2).
FT                                /FTId=VSP_024112.
FT   MUTAGEN       2      2       G->A: Abolishes myristoylation and
FT                                palmitoylation.
FT   MUTAGEN       3      3       C->A: Abolishes palmitoylation and plasma
FT                                membrane association; when associated
FT                                with A-6.
FT   MUTAGEN       3      3       C->S: Abolishes palmitoylation and plasma
FT                                membrane association; when associated
FT                                with S-6. Abolishes plasma membrane
FT                                association.
FT   MUTAGEN       6      6       C->A: Abolishes palmitoylation and plasma
FT                                membrane association; when associated
FT                                with A-3.
FT   MUTAGEN       6      6       C->S: Abolishes palmitoylation and plasma
FT                                membrane association; when associated
FT                                with S-3.
FT   CONFLICT    179    179       Q -> E (in Ref. 3; BAE42585 and 4;
FT                                AAH92217/AAH32149).
FT   CONFLICT    287    287       L -> M (in Ref. 3; BAE33766).
FT   CONFLICT    432    432       W -> R (in Ref. 3; BAE42585).
SQ   SEQUENCE   537 AA;  60656 MW;  50B21D7FB58E2345 CRC64;
     MGCVQCKDKE AAKLTEERDG SLNQSSGYRY GTDPTPQHYP SFGVTSIPNY NNFHAAGGQG
     LTVFGGVNSS SHTGTLRTRG GTGVTLFVAL YDYEARTEDD LSFHKGEKFQ ILNSSEGDWW
     EARSLTTGET GYIPSNYVAP VDSIQAEEWY FGKLGRKDAE RQLLSFGNPR GTFLIRESQT
     TKGAYSLSIR DWDDMKGDHV KHYKIRKLDN GGYYITTRAQ FETLQQLVQH YSERAAGLCC
     RLVVPCHKGM PRLTDLSVKT KDVWEIPRES LQLIKRLGNG QFGEVWLGTW NGNTKVAIKT
     LKPGTMSPES FLEEAQIMKK LKHDKLVQLY AVVSEEPIYI VTEYMSKGSL LDFLKDGEGR
     ALKLPNLVDM AAQVAAGMAY IERMNYIHRD LRSANILVGN GLICKIADFG LARLIEDNEY
     TARQGAKFPI KWTAPEAALY GRFTIKSDVW SFGILLTELV TKGRVPYPGM NNREVLEQVE
     RGYRMPCPQD CPISLHELMI HCWKKDPEER PTFEYLQGFL EDYFTATEPQ YQPGENL
//
ID   TKT_MOUSE               Reviewed;         623 AA.
AC   P40142; Q3U7Y1; Q3UK62; Q545A1; Q9ESA0;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Transketolase;
DE            Short=TK;
DE            EC=2.2.1.1;
DE   AltName: Full=P68;
GN   Name=Tkt;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=LAF1;
RX   MEDLINE=96214928; PubMed=8617775; DOI=10.1074/jbc.271.9.4993;
RA   Schimmer B.P., Tsao J., Czerwinski W.;
RT   "Amplification of the transketolase gene in desensitization-resistant
RT   mutant Y1 mouse adrenocortical tumor cells.";
RL   J. Biol. Chem. 271:4993-4998(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, and C57BL/6J;
RC   TISSUE=Bone marrow, Head, Kidney, and Pituitary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
RC   STRAIN=129/Sv;
RX   MEDLINE=98190521; PubMed=9521875; DOI=10.1006/geno.1997.5187;
RA   Salamon C., Chervenak M., Piatigorsky J., Sax C.M.;
RT   "The mouse transketolase (TKT) gene: cloning, characterization, and
RT   functional promoter analysis.";
RL   Genomics 48:209-220(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 65-623.
RC   STRAIN=BALB/c; TISSUE=Thymus;
RA   Su H., He W., Li Y.;
RT   "Cloning new genes possibly associated with atrophy of murine
RT   thymus.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PROTEIN SEQUENCE OF 175-204; 344-352; 382-395 AND 472-493, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-275, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde
CC       3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.
CC   -!- COFACTOR: Binds 1 calcium ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 thiamine pyrophosphate per subunit (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U05809; AAC52443.1; -; mRNA.
DR   EMBL; AK002627; BAB22242.1; -; mRNA.
DR   EMBL; AK012794; BAB28474.1; -; mRNA.
DR   EMBL; AK030446; BAC26968.1; -; mRNA.
DR   EMBL; AK140965; BAE24531.1; -; mRNA.
DR   EMBL; AK144146; BAE25728.1; -; mRNA.
DR   EMBL; AK146157; BAE26940.1; -; mRNA.
DR   EMBL; AK150139; BAE29335.1; -; mRNA.
DR   EMBL; AK150769; BAE29835.1; -; mRNA.
DR   EMBL; AK150844; BAE29902.1; -; mRNA.
DR   EMBL; AK150856; BAE29911.1; -; mRNA.
DR   EMBL; AK152460; BAE31238.1; -; mRNA.
DR   EMBL; AK159922; BAE35484.1; -; mRNA.
DR   EMBL; AK167084; BAE39242.1; -; mRNA.
DR   EMBL; BC055336; AAH55336.1; -; mRNA.
DR   EMBL; U90889; AAC53570.1; -; Genomic_DNA.
DR   EMBL; AF195533; AAG28459.1; -; mRNA.
DR   IPI; IPI00137409; -.
DR   RefSeq; NP_033414.1; NM_009388.5.
DR   UniGene; Mm.290692; -.
DR   ProteinModelPortal; P40142; -.
DR   SMR; P40142; 4-618.
DR   MINT; MINT-1855010; -.
DR   STRING; P40142; -.
DR   PhosphoSite; P40142; -.
DR   SWISS-2DPAGE; P40142; -.
DR   PMMA-2DPAGE; P40142; -.
DR   REPRODUCTION-2DPAGE; P40142; -.
DR   PRIDE; P40142; -.
DR   Ensembl; ENSMUST00000022529; ENSMUSP00000022529; ENSMUSG00000021957.
DR   GeneID; 21881; -.
DR   KEGG; mmu:21881; -.
DR   NMPDR; fig|10090.3.peg.28740; -.
DR   UCSC; uc007svc.1; mouse.
DR   CTD; 21881; -.
DR   MGI; MGI:105992; Tkt.
DR   HOGENOM; HBG465450; -.
DR   HOVERGEN; HBG004036; -.
DR   InParanoid; P40142; -.
DR   OMA; HKPDQQK; -.
DR   OrthoDB; EOG4R23TG; -.
DR   PhylomeDB; P40142; -.
DR   BRENDA; 2.2.1.1; 244.
DR   NextBio; 301390; -.
DR   ArrayExpress; P40142; -.
DR   Bgee; P40142; -.
DR   CleanEx; MM_TKT; -.
DR   Genevestigator; P40142; -.
DR   GermOnline; ENSMUSG00000021957; Mus musculus.
DR   GO; GO:0004802; F:transketolase activity; IDA:MGI.
DR   GO; GO:0040008; P:regulation of growth; IMP:MGI.
DR   InterPro; IPR009014; Transketo_C/Pyr-ferredox_oxred.
DR   InterPro; IPR015941; Transketolase-like_C.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR020826; Transketolase_BS.
DR   InterPro; IPR005476; Transketolase_C.
DR   InterPro; IPR005474; Transketolase_N.
DR   Gene3D; G3DSA:3.40.50.920; Transketo_C_like; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52922; Transketo_C_like; 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Calcium; Direct protein sequencing; Metal-binding;
KW   Phosphoprotein; Thiamine pyrophosphate; Transferase.
FT   CHAIN         1    623       Transketolase.
FT                                /FTId=PRO_0000191896.
FT   METAL       155    155       Calcium (By similarity).
FT   METAL       185    185       Calcium (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES       6      6       N6-acetyllysine (By similarity).
FT   MOD_RES      11     11       N6-acetyllysine (By similarity).
FT   MOD_RES     144    144       N6-acetyllysine (By similarity).
FT   MOD_RES     204    204       N6-acetyllysine (By similarity).
FT   MOD_RES     232    232       N6-acetyllysine (By similarity).
FT   MOD_RES     241    241       N6-acetyllysine (By similarity).
FT   MOD_RES     260    260       N6-acetyllysine (By similarity).
FT   MOD_RES     275    275       Phosphotyrosine.
FT   MOD_RES     287    287       Phosphothreonine (By similarity).
FT   MOD_RES     295    295       Phosphoserine (By similarity).
FT   MOD_RES     314    314       N6-acetyllysine (By similarity).
FT   MOD_RES     597    597       N6-acetyllysine (By similarity).
FT   MOD_RES     603    603       N6-acetyllysine (By similarity).
FT   CONFLICT    555    555       R -> G (in Ref. 2; BAE26940).
SQ   SEQUENCE   623 AA;  67630 MW;  870045AD5C58FA09 CRC64;
     MEGYHKPDQQ KLQALKDTAN RLRISSIQAT TAAGSGHPTS CCSAAEIMAV LFFHTMRYKA
     LDPRNPHNDR FVLSKGHAAP ILYAVWAEAG FLPEAELLNL RKISSDLDGH PVPKQAFTDV
     ATGSLGQGLG AACGMAYTGK YFDKASYRVY CMLGDGEVSE GSVWEAMAFA GIYKLDNLVA
     IFDINRLGQS DPAPLQHQVD IYQKRCEAFG WHTIIVDGHS VEELCKAFGQ AKHQPTAIIA
     KTFKGRGITG IEDKEAWHGK PLPKNMAEQI IQEIYSQVQS KKKILATPPQ EDAPSVDIAN
     IRMPTPPSYK VGDKIATRKA YGLALAKLGH ASDRIIALDG DTKNSTFSEL FKKEHPDRFI
     ECYIAEQNMV SIAVGCATRD RTVPFCSTFA AFFTRAFDQI RMAAISESNI NLCGSHCGVS
     IGEDGPSQMA LEDLAMFRSV PMSTVFYPSD GVATEKAVEL AANTKGICFI RTSRPENAII
     YSNNEDFQVG QAKVVLKSKD DQVTVIGAGV TLHEALAAAE SLKKDKISIR VLDPFTIKPL
     DRKLILDSAR ATKGRILTVE DHYYEGGIGE AVSAAVVGEP GVTVTRLAVS QVPRSGKPAE
     LLKMFGIDKD AIVQAVKGLV TKG
//
ID   VP26A_MOUSE             Reviewed;         327 AA.
AC   P40336; Q3TGY3; Q3THM5; Q3TW99; Q3UD54; Q8C1E9;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Vacuolar protein sorting-associated protein 26A;
DE   AltName: Full=H<beta>58 protein;
DE            Short=H beta 58;
DE   AltName: Full=Vesicle protein sorting 26A;
DE            Short=mVPS26;
GN   Name=Vps26a; Synonyms=Vps26;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=92347186; PubMed=1638986;
RA   Lee J.J., Radice G., Perkins C.P., Costantini F.;
RT   "Identification and characterization of a novel, evolutionarily
RT   conserved gene disrupted by the murine H beta 58 embryonic lethal
RT   transgene insertion.";
RL   Development 115:277-288(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J, and DBA/2;
RC   TISSUE=Amnion, Bone marrow, Lung, Placenta, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15078902; DOI=10.1083/jcb.200312034;
RA   Seaman M.N.J.;
RT   "Cargo-selective endosomal sorting for retrieval to the Golgi requires
RT   retromer.";
RL   J. Cell Biol. 165:111-122(2004).
CC   -!- FUNCTION: Essential component of the retromer complex, a complex
CC       required to retrieve lysosomal enzyme receptors (IGF2R and M6PR)
CC       from endosomes to the trans-Golgi network. Also required to
CC       regulate transcytosis of the polymeric immunoglobulin receptor
CC       (pIgR-pIgA).
CC   -!- SUBUNIT: Component of the retromer complex composed of VPS26
CC       (VPS26A or VPS26B), VPS29, VPS35, SNX1 and SNX2. Interacts
CC       directly with VPS35. Found in a complex with XPO7, EIF4A1,
CC       ARHGAP1, VPS26A, VPS29, VPS35 and SFN (By similarity). Interacts
CC       with ECM29 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome membrane; Peripheral
CC       membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P40336-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P40336-2; Sequence=VSP_019926;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the VPS26 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; S41204; AAB22718.1; -; mRNA.
DR   EMBL; AK028096; BAC25745.1; -; mRNA.
DR   EMBL; AK150244; BAE29408.1; -; mRNA.
DR   EMBL; AK147989; BAE28271.1; -; mRNA.
DR   EMBL; AK151360; BAE30335.1; -; mRNA.
DR   EMBL; AK159783; BAE35367.1; -; mRNA.
DR   EMBL; AK167592; BAE39650.1; -; mRNA.
DR   EMBL; AK165853; BAE38415.1; -; mRNA.
DR   EMBL; AK168213; BAE40171.1; -; mRNA.
DR   EMBL; AK168537; BAE40415.1; -; mRNA.
DR   EMBL; BC007148; AAH07148.1; -; mRNA.
DR   IPI; IPI00329942; -.
DR   IPI; IPI00776216; -.
DR   PIR; A44882; A44882.
DR   PIR; B44882; B44882.
DR   RefSeq; NP_001106826.1; NM_001113355.1.
DR   RefSeq; NP_598433.1; NM_133672.3.
DR   UniGene; Mm.260703; -.
DR   UniGene; Mm.473468; -.
DR   ProteinModelPortal; P40336; -.
DR   SMR; P40336; 6-299.
DR   STRING; P40336; -.
DR   PhosphoSite; P40336; -.
DR   PRIDE; P40336; -.
DR   Ensembl; ENSMUST00000092473; ENSMUSP00000090130; ENSMUSG00000020078.
DR   Ensembl; ENSMUST00000105447; ENSMUSP00000101087; ENSMUSG00000020078.
DR   GeneID; 30930; -.
DR   KEGG; mmu:30930; -.
DR   UCSC; uc007fhf.1; mouse.
DR   UCSC; uc007fhg.1; mouse.
DR   CTD; 30930; -.
DR   MGI; MGI:1353654; Vps26a.
DR   eggNOG; roNOG07380; -.
DR   GeneTree; ENSGT00390000002588; -.
DR   HOVERGEN; HBG082914; -.
DR   OMA; PVCEIDV; -.
DR   OrthoDB; EOG470THM; -.
DR   PhylomeDB; P40336; -.
DR   NextBio; 307338; -.
DR   ArrayExpress; P40336; -.
DR   Bgee; P40336; -.
DR   CleanEx; MM_VPS26A; -.
DR   Genevestigator; P40336; -.
DR   GermOnline; ENSMUSG00000020078; Mus musculus.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030904; C:retromer complex; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:MGI.
DR   GO; GO:0007034; P:vacuolar transport; IEA:InterPro.
DR   InterPro; IPR005377; VPS26.
DR   Pfam; PF03643; Vps26; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Endosome; Membrane;
KW   Protein transport; Transport.
FT   CHAIN         1    327       Vacuolar protein sorting-associated
FT                                protein 26A.
FT                                /FTId=PRO_0000073008.
FT   VAR_SEQ       1      1       M -> MSEPLPAFLDRLWGPWLGTRSPPSRSSAASPSK
FT                                (in isoform 2).
FT                                /FTId=VSP_019926.
FT   CONFLICT     37     37       E -> Q (in Ref. 2; BAC25745).
FT   CONFLICT     71     71       E -> G (in Ref. 2; BAE35367).
FT   CONFLICT     79     79       F -> L (in Ref. 2; BAE40171).
FT   CONFLICT    188    188       K -> R (in Ref. 2; BAE40415).
SQ   SEQUENCE   327 AA;  38114 MW;  419DAED54264AC13 CRC64;
     MSFLGGFFGP ICEIDVALND GETRKMAEMK TEDGKVEKHY LFYDGESVSG KVNLAFKQPG
     KRLEHQGIRI EFVGQIELFN DKSNTHEFVN LVKELALPGE LTQSRSYDFE FMQVEKPYES
     YIGANVRLRY FLKVTIVRRL TDLVKEYDLI VHQLATYPDV NNSIKMEVGI EDCLHIEFEY
     NKSKYHLKDV IVGKIYFLLV RIKIQHMELQ LIKKEITGIG PSTTTETETI AKYEIMDGAP
     VKGESIPIRL FLAGYDPTPT MRDVNKKFSV RYFLNLVLVD EEDRRYFKQQ EIILWRKAPE
     KLRKQRTNFH QRFESPDSQA SAEQPEM
//
ID   SMBP2_MOUSE             Reviewed;         993 AA.
AC   P40694;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=DNA-binding protein SMUBP-2;
DE            EC=3.6.4.12;
DE            EC=3.6.4.13;
DE   AltName: Full=ATP-dependent helicase IGHMBP2;
DE   AltName: Full=Cardiac transcription factor 1;
DE            Short=CATF1;
DE   AltName: Full=Immunoglobulin mu-binding protein 2;
GN   Name=Ighmbp2; Synonyms=Smbp-2, Smbp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DNA-BINDING.
RC   STRAIN=BALB/c; TISSUE=Spleen;
RX   MEDLINE=93261806; PubMed=8493094; DOI=10.1093/nar/21.8.1761;
RA   Mizuta T.-R., Fukita Y., Miyoshi T., Shimizu A., Honjo T.;
RT   "Isolation of cDNA encoding a binding protein specific to 5'-
RT   phosphorylated single-stranded DNA with G-rich sequences.";
RL   Nucleic Acids Res. 21:1761-1766(1993).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-800, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RIBOSOMES.
RX   PubMed=19158098; DOI=10.1093/hmg/ddp028;
RA   Guenther U.P., Handoko L., Laggerbauer B., Jablonka S., Chari A.,
RA   Alzheimer M., Ohmer J., Ploettner O., Gehring N., Sickmann A.,
RA   von Au K., Schuelke M., Fischer U.;
RT   "IGHMBP2 is a ribosome-associated helicase inactive in the
RT   neuromuscular disorder distal SMA type 1 (DSMA1).";
RL   Hum. Mol. Genet. 18:1288-1300(2009).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TRNA-BINDING.
RX   PubMed=19299493; DOI=10.1093/hmg/ddp134;
RA   de Planell-Saguer M., Schroeder D.G., Rodicio M.C., Cox G.A.,
RA   Mourelatos Z.;
RT   "Biochemical and genetic evidence for a role of IGHMBP2 in the
RT   translational machinery.";
RL   Hum. Mol. Genet. 18:2115-2126(2009).
CC   -!- FUNCTION: 5' to 3' helicase that unwinds RNA and DNA duplices in
CC       an ATP-dependent reaction. Acts as a transcription regulator.
CC       Required for the transcriptional activation of the flounder liver-
CC       type antifreeze protein gene. Exhibits strong binding specificity
CC       to the enhancer element B of the flounder antifreeze protein gene
CC       intron. Binds to the insulin II gene RIPE3B enhancer region (By
CC       similarity). May be involved in translation. DNA-binding protein
CC       specific to 5'-phosphorylated single-stranded guanine-rich
CC       sequence related to the immunoglobulin mu chain switch region.
CC       Preferentially binds to the 5'-GGGCT-3' motif. Interacts with
CC       tRNA-Tyr.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Homooligomer (By similarity). Interacts with RUVBL1,
CC       RUVBL2, GTF3C1 and ABT1 (By similarity). Is part of large
CC       cytosolic ribonucleoprotein complexes (Probable). Associates with
CC       the ribosomes.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cell projection, axon.
CC       Note=Colocalizes with the traslation initiation factor EIF4G2.
CC   -!- TISSUE SPECIFICITY: In all tissues examined.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC   -!- SIMILARITY: Contains 1 AN1-type zinc finger.
CC   -!- SIMILARITY: Contains 1 R3H domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; L10075; AAA40143.1; -; mRNA.
DR   IPI; IPI00113033; -.
DR   PIR; S35633; S35633.
DR   UniGene; Mm.3179; -.
DR   ProteinModelPortal; P40694; -.
DR   SMR; P40694; 2-637, 725-784, 893-942.
DR   IntAct; P40694; 1.
DR   STRING; P40694; -.
DR   PhosphoSite; P40694; -.
DR   PRIDE; P40694; -.
DR   Ensembl; ENSMUST00000025751; ENSMUSP00000025751; ENSMUSG00000024831.
DR   UCSC; uc008fwa.1; mouse.
DR   MGI; MGI:99954; Ighmbp2.
DR   eggNOG; roNOG07945; -.
DR   GeneTree; ENSGT00600000084518; -.
DR   HOGENOM; HBG713547; -.
DR   HOVERGEN; HBG077019; -.
DR   InParanoid; P40694; -.
DR   OrthoDB; EOG4GHZNJ; -.
DR   PhylomeDB; P40694; -.
DR   ArrayExpress; P40694; -.
DR   Bgee; P40694; -.
DR   CleanEx; MM_IGHMBP2; -.
DR   Genevestigator; P40694; -.
DR   GermOnline; ENSMUSG00000024831; Mus musculus.
DR   GO; GO:0030424; C:axon; IDA:UniProtKB.
DR   GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0043141; F:ATP-dependent 5'-3' DNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0032575; F:ATP-dependent 5'-3' RNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR   GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR   GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0021522; P:spinal cord motor neuron differentiation; IMP:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; NAS:UniProtKB.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR004483; DNA_helicase_put.
DR   InterPro; IPR001374; R3H_ss-bd.
DR   InterPro; IPR006935; Restrct_endonuc_I_R/III_Res.
DR   InterPro; IPR000058; Znf_AN1.
DR   Gene3D; G3DSA:4.10.1110.10; Znf_AN1; 1.
DR   Pfam; PF01424; R3H; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00393; R3H; 1.
DR   SMART; SM00154; ZnF_AN1; 1.
DR   TIGRFAMs; TIGR00376; put_DNA_helic; 1.
DR   PROSITE; PS51061; R3H; 1.
DR   PROSITE; PS51039; ZF_AN1; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; ATP-binding; Cell projection; Cytoplasm;
KW   DNA-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Ribonucleoprotein; RNA-binding;
KW   Transcription; Transcription regulation; tRNA-binding; Zinc;
KW   Zinc-finger.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    993       DNA-binding protein SMUBP-2.
FT                                /FTId=PRO_0000080703.
FT   DOMAIN      721    784       R3H.
FT   NP_BIND     213    220       ATP (By similarity).
FT   DNA_BIND    637    783       SS DNA-binding (By similarity).
FT   ZN_FING     892    938       AN1-type.
FT   MOTIF       862    866       Nuclear localization signal (Potential).
FT   COMPBIAS    249    425       Leu-rich.
FT   COMPBIAS    370    373       Poly-Val.
FT   COMPBIAS    793    861       Gln/Pro-rich.
FT   COMPBIAS    862    866       Poly-Lys.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     655    655       Phosphoserine (By similarity).
FT   MOD_RES     800    800       Phosphoserine.
SQ   SEQUENCE   993 AA;  109466 MW;  2FA0850DBABDE35B CRC64;
     MASSTVESFV AQQLQLLELE RDAEVEERRS WQEHSSLREL QSRGVCLLKL QVSSQRTGLY
     GQRLVTFEPR KFGPAVVLPS NSFTSGDIVG LYDTNENSQL ATGVLTRITQ KSVTVAFDES
     HDLQLNLDRE NTYRLLKLAN DVTYKRLKKA LMTLKKYHSG PASSLIDILL GSSTPSPAME
     IPPLSFYNTT LDLSQKEAVS FALAQKELAI IHGPPGTGKT TTVVEIILQA VKQGLKVLCC
     APSNIAVDNL VERLALCKKR ILRLGHPARL LESVQHHSLD AVLARSDNAQ IVADIRRDID
     QVFGKNKKTQ DKREKGNFRS EIKLLRKELK EREEAAIVQS LTAADVVLAT NTGASSDGPL
     KLLPEDYFDV VVVDECAQAL EASCWIPLLK APKCILAGDH RQLPPTTVSH RAALAGLSRS
     LMERLAEKHG AGVVRMLTVQ YRMHQAIMCW ASEAMYHGQF TSHPSVAGHL LKDLPGVTDT
     EETRVPLLLI DTAGCGLLEL EEEDSQSKGN PGEVRLVTLH IQALVDAGVQ AGDIAVIAPY
     NLQVDLLRQS LSNKHPELEI KSVDGFQGRE KEAVLLTFVR SNRKGEVGFL AEDRRINVAV
     TRARRHVAVI CDSHTVNNHA FLETLVDYFT EHGEVRTAFE YLDDIVPENY THEGSQGHSR
     VPKPKCPSTS IRKPASDQES GQETRAAPRH GRRKPSEKPP GSHVQSQHSS SANGSDRTGG
     PDRTEHFRAT IEEFVASKES QLEFPTSLSS HDRLRVHQLA EEFGLRHDST GEGKARHITV
     SRRSPASSGS VAPQPSSPPS PAQAEPEPRA EEPVTVVQAH CPVQLDLKAL HLERLQRQQS
     SQAQTAKGQP GGDSRPQKAS QKKKKKEPKG PVMALPCEED FDALVSAVVK ADNTCSFSKC
     SVSTTTLGQF CMHCSHRYYL SHHLPEIHGC GEKARAHARQ RISREGVLYA GSGTKDRALD
     PAKRAQLQRR LDKKLGELSS QRTSRKKEKE RGT
//
ID   BCL6_MOUSE              Reviewed;         707 AA.
AC   P41183; Q61065;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=B-cell lymphoma 6 protein homolog;
GN   Name=Bcl6; Synonyms=Bcl-6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Skeletal muscle;
RX   MEDLINE=96038894; PubMed=7478591;
RA   Fukuda T., Miki T., Yoshida T., Hatano M., Ohashi K., Hirosawa S.,
RA   Tokuhisa T.;
RT   "The murine BCL6 gene is induced in activated lymphocytes as an
RT   immediate early gene.";
RL   Oncogene 11:1657-1663(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RX   MEDLINE=96247530; PubMed=8652841;
RA   Allman D., Jain A., Dent A., Maile R.R., Selvaggi T., Kehry M.R.,
RA   Staudt L.M.;
RT   "BCL-6 expression during B-cell activation.";
RL   Blood 87:5257-5268(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH BCL6B.
RX   MEDLINE=98298267; PubMed=9632807;
RA   Okabe S., Fukuda T., Ishibashi K., Kojima S., Okada S., Hatano M.,
RA   Ebara M., Saisho H., Tokuhisa T.;
RT   "BAZF, a novel Bcl6 homolog, functions as a transcriptional
RT   repressor.";
RL   Mol. Cell. Biol. 18:4235-4244(1998).
RN   [5]
RP   INTERACTION WITH ZBTB7, AND SUBCELLULAR LOCATION.
RX   MEDLINE=99124383; PubMed=9927193; DOI=10.1038/sj.onc.1202332;
RA   Davies J.M., Hawe N., Kabarowski J., Huang Q.-H., Zhu J., Brand N.J.,
RA   Leprince D., Dhordain P., Cook M., Moriss-Kay G., Zelent A.;
RT   "Novel BTB/POZ domain zinc-finger protein, LRF, is a potential target
RT   of the LAZ-3/BCL-6 oncogene.";
RL   Oncogene 18:365-375(1999).
CC   -!- FUNCTION: Transcriptional repressor which is required for germinal
CC       center formation and antibody affinity maturation. Probably plays
CC       an important role in lymphomagenesis (By similarity).
CC   -!- SUBUNIT: Homodimer. Interacts (via BTB domain) with BCOR; the
CC       interaction is direct. Interacts (via BTB domain) with NCOR2; the
CC       interaction is direct. Interacts with ZBTB7 and BCL6B. Interacts
CC       with the catalytic domain of HDAC9 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DOMAIN: The BTB domain mediates homodimerization. Its dimer
CC       interface mediates peptide binding such as to corepressors BCOR
CC       and NCOR2 (By similarity).
CC   -!- PTM: Phosphorylated by MAPK1 in response to antigen receptor
CC       activation. Phosphorylation induces its degradation by
CC       ubiquitin/proteasome pathway (By similarity).
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC   -!- SIMILARITY: Contains 6 C2H2-type zinc fingers.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D38377; BAA07456.1; -; mRNA.
DR   EMBL; U41465; AAB17432.1; -; mRNA.
DR   EMBL; BC052315; AAH52315.1; -; mRNA.
DR   IPI; IPI00111606; -.
DR   RefSeq; NP_033874.1; NM_009744.3.
DR   UniGene; Mm.347398; -.
DR   ProteinModelPortal; P41183; -.
DR   SMR; P41183; 5-129, 385-681.
DR   STRING; P41183; -.
DR   PhosphoSite; P41183; -.
DR   PRIDE; P41183; -.
DR   Ensembl; ENSMUST00000023151; ENSMUSP00000023151; ENSMUSG00000022508.
DR   GeneID; 12053; -.
DR   KEGG; mmu:12053; -.
DR   UCSC; uc007ytz.1; mouse.
DR   CTD; 12053; -.
DR   MGI; MGI:107187; Bcl6.
DR   eggNOG; roNOG08576; -.
DR   HOGENOM; HBG445860; -.
DR   HOVERGEN; HBG004831; -.
DR   InParanoid; P41183; -.
DR   OMA; QASFRYK; -.
DR   OrthoDB; EOG4NVZJS; -.
DR   PhylomeDB; P41183; -.
DR   NextBio; 280351; -.
DR   ArrayExpress; P41183; -.
DR   Bgee; P41183; -.
DR   CleanEx; MM_BCL6; -.
DR   Genevestigator; P41183; -.
DR   GermOnline; ENSMUSG00000022508; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0016564; F:transcription repressor activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR   GO; GO:0030183; P:B cell differentiation; IGI:MGI.
DR   GO; GO:0000902; P:cell morphogenesis; IGI:MGI.
DR   GO; GO:0048821; P:erythrocyte development; IMP:MGI.
DR   GO; GO:0002467; P:germinal center formation; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptosis; IDA:MGI.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IMP:MGI.
DR   GO; GO:0048294; P:negative regulation of isotype switching to IgE isotypes; IGI:MGI.
DR   GO; GO:0032764; P:negative regulation of mast cell cytokine production; IMP:MGI.
DR   GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:MGI.
DR   GO; GO:0045629; P:negative regulation of T-helper 2 cell differentiation; IGI:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0002829; P:negative regulation of type 2 immune response; IGI:MGI.
DR   GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:MGI.
DR   GO; GO:0051272; P:positive regulation of cellular component movement; IMP:MGI.
DR   GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
DR   GO; GO:0043380; P:regulation of memory T cell differentiation; IMP:MGI.
DR   GO; GO:0032319; P:regulation of Rho GTPase activity; IMP:MGI.
DR   GO; GO:0007266; P:Rho protein signal transduction; IGI:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   GO; GO:0042092; P:type 2 immune response; IMP:MGI.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR013069; BTB_POZ.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 5.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 6.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Repeat; Repressor; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    707       B-cell lymphoma 6 protein homolog.
FT                                /FTId=PRO_0000047099.
FT   DOMAIN       32     99       BTB.
FT   ZN_FING     519    542       C2H2-type 1.
FT   ZN_FING     547    569       C2H2-type 2.
FT   ZN_FING     575    597       C2H2-type 3.
FT   ZN_FING     603    625       C2H2-type 4.
FT   ZN_FING     631    653       C2H2-type 5.
FT   ZN_FING     659    682       C2H2-type 6.
FT   CONFLICT    456    456       A -> G (in Ref. 2; AAB17432).
SQ   SEQUENCE   707 AA;  78982 MW;  2051DD808D32D5EC CRC64;
     MASPADSCIQ FTRHASDVLL NLNRLRSRDI LTDVVIVVSR EQFRAHKTVL MACSGLFYSI
     FTDQLKCNLS VINLDPEISP EGFCILLDFM YTSRLNLREG NIMAVMTTAM YLQMEHVVDT
     CRKFIKASEA EMAPALKPPR EEFLNSRMLM PHDIMAYRGR EVVENNMPLR NTPGCESRAF
     APPLYSGLST PPASYPMYSH LPLSTFLFSD EELRDAPRMP VANPFPKERA LPCDSARQVP
     NEYSRPAMEV SPSLCHSNIY SPKEAVPEEA RSDIHYSVPE GPKPAVPSAR NAPYFPCDKA
     SKEEERPSSE DEIALHFEPP NAPLNRKGLV SPQSPQKSDC QPNSPTESCS SKNACILQAS
     GSPPAKSPTD PKACNWKKYK FIVLNSLNQN AKPEGSEQAE LGRLSPRAYP APPACQPPME
     PANLDLQSPT KLSASGEDST IPQASRLNNL VNRSLAGSPR SSSESHSPLY MHPPKCTSCG
     SQSPQHTEMC LHTAGPTFPE EMGETQSEYS DSSCENGTFF CNECDCRFSE EASLKRHTLQ
     THSDKPYKCD RCQASFRYKG NLASHKTVHT GEKPYRCNIC GAQFNRPANL KTHTRIHSGE
     KPYKCETCGA RFVQVAHLRA HVLIHTGEKP YPCEICGTRF RHLQTLKSHL RIHTGEKPYH
     CEKCNLHFRH KSQLRLHLRQ KHGAITNTKV QYRVSAADLP PELPKAC
//
ID   ABCA1_MOUSE             Reviewed;        2261 AA.
AC   P41233;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 3.
DT   08-MAR-2011, entry version 106.
DE   RecName: Full=ATP-binding cassette sub-family A member 1;
DE   AltName: Full=ATP-binding cassette transporter 1;
DE            Short=ABC-1;
DE            Short=ATP-binding cassette 1;
GN   Name=Abca1; Synonyms=Abc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=DBA/2; TISSUE=Macrophage;
RX   MEDLINE=94375008; PubMed=8088782; DOI=10.1006/geno.1994.1237;
RA   Luciani M.-F., Denizot F., Savary S., Mattei M.-G., Chimini G.;
RT   "Cloning of two novel ABC transporters mapping on human chromosome
RT   9.";
RL   Genomics 21:150-159(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   MEDLINE=21251004; PubMed=11352567; DOI=10.1006/geno.2000.6467;
RA   Qiu Y., Cavelier L., Chiu S., Yang X., Rubin E., Cheng J.-F.;
RT   "Human and mouse ABCA1 comparative sequencing and transgenesis studies
RT   revealing novel regulatory sequences.";
RL   Genomics 73:66-76(2001).
RN   [3]
RP   INDUCTION BY LIPOPOLYSACCHARIDE.
RX   MEDLINE=22028260; PubMed=12032171;
RA   Kaplan R., Gan X., Menke J.G., Wright S.D., Cai T.-Q.;
RT   "Bacterial lipopolysaccharide induces expression of ABCA1 but not
RT   ABCG1 via an LXR-independent pathway.";
RL   J. Lipid Res. 43:952-959(2002).
RN   [4]
RP   DOWN-REGULATION BY ENDOTOXIN.
RX   PubMed=12777468; DOI=10.1194/jlr.M300100-JLR200;
RA   Khovidhunkit W., Moser A.H., Shigenaga J.K., Grunfeld C.,
RA   Feingold K.R.;
RT   "Endotoxin down-regulates ABCG5 and ABCG8 in mouse liver and ABCA1 and
RT   ABCG1 in J774 murine macrophages: differential role of LXR.";
RL   J. Lipid Res. 44:1728-1736(2003).
RN   [5]
RP   INTERACTION WITH MEGF10.
RX   PubMed=17205124; DOI=10.1371/journal.pone.0000120;
RA   Hamon Y., Trompier D., Ma Z., Venegas V., Pophillat M., Mignotte V.,
RA   Zhou Z., Chimini G.;
RT   "Cooperation between engulfment receptors: the case of ABCA1 and
RT   MEGF10.";
RL   PLoS ONE 1:E120-E120(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1141 AND SER-1147, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-489, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: cAMP-dependent and sulfonylurea-sensitive anion
CC       transporter. Key gatekeeper influencing intracellular cholesterol
CC       transport (By similarity).
CC   -!- SUBUNIT: Interacts with MEGF10.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- TISSUE SPECIFICITY: Widely expressed in adult tissues. Highest
CC       levels are found in pregnant uterus and uterus.
CC   -!- INDUCTION: Down-regulated by endotoxins (LPS) or cytokines (TNF
CC       and IL-1) in J774 macrophages. The down-regulation by endotoxin in
CC       macrophages is not likely to be mediated by the liver X
CC       receptor/retinoic X receptor (LXR/RXR).
CC   -!- DOMAIN: Multifunctional polypeptide with two homologous halves,
CC       each containing an hydrophobic membrane-anchoring domain and an
CC       ATP binding cassette (ABC) domain.
CC   -!- PTM: Phosphorylation on Ser-2054 regulates phospholipid efflux (By
CC       similarity).
CC   -!- PTM: Palmitoylation by DHHC8 is essential for membrane
CC       localization (By similarity).
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA
CC       family.
CC   -!- SIMILARITY: Contains 2 ABC transporter domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG39073.1; Type=Erroneous initiation;
CC       Sequence=CAA53530.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X75926; CAA53530.1; ALT_INIT; mRNA.
DR   EMBL; AF287263; AAG39073.1; ALT_INIT; Genomic_DNA.
DR   IPI; IPI00112614; -.
DR   PIR; A54774; A54774.
DR   UniGene; Mm.277376; -.
DR   ProteinModelPortal; P41233; -.
DR   SMR; P41233; 898-1125, 1911-2137.
DR   STRING; P41233; -.
DR   TCDB; 3.A.1.211.1; ATP-binding cassette (ABC) superfamily.
DR   PhosphoSite; P41233; -.
DR   PRIDE; P41233; -.
DR   Ensembl; ENSMUST00000030010; ENSMUSP00000030010; ENSMUSG00000015243.
DR   UCSC; uc008swu.1; mouse.
DR   MGI; MGI:99607; Abca1.
DR   eggNOG; roNOG04635; -.
DR   HOGENOM; HBG444243; -.
DR   HOVERGEN; HBG050436; -.
DR   InParanoid; P41233; -.
DR   OrthoDB; EOG44F686; -.
DR   ArrayExpress; P41233; -.
DR   Bgee; P41233; -.
DR   Genevestigator; P41233; -.
DR   GermOnline; ENSMUSG00000015243; Mus musculus.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0005887; C:integral to plasma membrane; IDA:MGI.
DR   GO; GO:0008509; F:anion transmembrane transporter activity; IDA:BHF-UCL.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0017127; F:cholesterol transporter activity; IDA:MGI.
DR   GO; GO:0005548; F:phospholipid transporter activity; IDA:MGI.
DR   GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
DR   GO; GO:0071300; P:cellular response to retinoic acid; IDA:UniProtKB.
DR   GO; GO:0033344; P:cholesterol efflux; IDA:MGI.
DR   GO; GO:0008203; P:cholesterol metabolic process; IDA:MGI.
DR   GO; GO:0002790; P:peptide secretion; IMP:MGI.
DR   GO; GO:0006911; P:phagocytosis, engulfment; IMP:MGI.
DR   GO; GO:0033700; P:phospholipid efflux; IDA:MGI.
DR   GO; GO:0045332; P:phospholipid translocation; IMP:MGI.
DR   GO; GO:0010875; P:positive regulation of cholesterol efflux; IMP:BHF-UCL.
DR   GO; GO:0006497; P:protein lipidation; IMP:MGI.
DR   GO; GO:0043691; P:reverse cholesterol transport; IMP:BHF-UCL.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Disulfide bond; Glycoprotein; Lipoprotein; Membrane;
KW   Nucleotide-binding; Palmitate; Phosphoprotein; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1   2261       ATP-binding cassette sub-family A member
FT                                1.
FT                                /FTId=PRO_0000093289.
FT   TRANSMEM     22     42       Helical; (Potential).
FT   TOPO_DOM     43    639       Extracellular (By similarity).
FT   TRANSMEM    640    660       Helical; (Potential).
FT   TRANSMEM    683    703       Helical; (Potential).
FT   TRANSMEM    716    736       Helical; (Potential).
FT   TRANSMEM    745    765       Helical; (Potential).
FT   TRANSMEM    777    797       Helical; (Potential).
FT   TRANSMEM    827    847       Helical; (Potential).
FT   TRANSMEM    941    961       Helical; (Potential).
FT   TRANSMEM   1351   1371       Helical; (Potential).
FT   TOPO_DOM   1372   1656       Extracellular (By similarity).
FT   TRANSMEM   1657   1677       Helical; (Potential).
FT   TRANSMEM   1703   1723       Helical; (Potential).
FT   TRANSMEM   1735   1755       Helical; (Potential).
FT   TRANSMEM   1768   1788       Helical; (Potential).
FT   TRANSMEM   1802   1822       Helical; (Potential).
FT   TRANSMEM   1852   1872       Helical; (Potential).
FT   DOMAIN      899   1131       ABC transporter 1.
FT   DOMAIN     1912   2144       ABC transporter 2.
FT   NP_BIND     933    940       ATP 1 (Potential).
FT   NP_BIND    1946   1953       ATP 2 (Potential).
FT   MOD_RES    1042   1042       Phosphoserine; by PKA (By similarity).
FT   MOD_RES    1141   1141       Phosphoserine.
FT   MOD_RES    1147   1147       Phosphoserine.
FT   MOD_RES    2054   2054       Phosphoserine; by PKA (By similarity).
FT   LIPID         3      3       S-palmitoyl cysteine (By similarity).
FT   LIPID        23     23       S-palmitoyl cysteine (By similarity).
FT   LIPID      1110   1110       S-palmitoyl cysteine (By similarity).
FT   LIPID      1111   1111       S-palmitoyl cysteine (By similarity).
FT   CARBOHYD     14     14       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     98     98       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    151    151       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    161    161       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    196    196       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    244    244       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    292    292       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    337    337       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    349    349       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    400    400       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    478    478       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    489    489       N-linked (GlcNAc...).
FT   CARBOHYD    521    521       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    820    820       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1144   1144       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1294   1294       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1453   1453       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1499   1499       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1504   1504       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1637   1637       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2044   2044       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2238   2238       N-linked (GlcNAc...) (Potential).
FT   DISULFID     75    309       By similarity.
FT   DISULFID   1463   1477       By similarity.
FT   CONFLICT   1567   1568       Missing (in Ref. 2; AAG39073).
FT   CONFLICT   2024   2024       Missing (in Ref. 2; AAG39073).
SQ   SEQUENCE   2261 AA;  253974 MW;  F0C3C5F1FCEF34F1 CRC64;
     MACWPQLRLL LWKNLTFRRR QTCQLLLEVA WPLFIFLILI SVRLSYPPYE QHECHFPNKA
     MPSAGTLPWV QGIICNANNP CFRYPTPGEA PGVVGNFNKS IVSRLFSDAQ RLLLYSQRDT
     SIKDMHKVLR MLRQIKHPNS NLKLQDFLVD NETFSGFLQH NLSLPRSTVD SLLQANVGLQ
     KVFLQGYQLH LASLCNGSKL EEIIQLGDAE VSALCGLPRK KLDAAERVLR YNMDILKPVV
     TKLNSTSHLP TQHLAEATTV LLDSLGGLAQ ELFSTKSWSD MRQEVMFLTN VNSSSSSTQI
     YQAVSRIVCG HPEGGGLKIK SLNWYEDNNY KALFGGNNTE EDVDTFYDNS TTPYCNDLMK
     NLESSPLSRI IWKALKPLLV GKILYTPDTP ATRQVMAEVN KTFQELAVFH DLEGMWEELS
     PQIWTFMENS QEMDLVRTLL DSRGNDQFWE QKLDGLDWTA QDIMAFLAKN PEDVQSPNGS
     VYTWREAFNE TNQAIQTISR FMECVNLNKL EPIPTEVRLI NKSMELLDER KFWAGIVFTG
     ITPDSVELPH HVKYKIRMDI DNVERTNKIK DGYWDPGPRA DPFEDMRYVW GGFAYLQDVV
     EQAIIRVLTG SEKKTGVYVQ QMPYPCYVDD IFLRVMSRSM PLFMTLAWIY SVAVIIKSIV
     YEKEARLKET MRIMGLDNGI LWFSWFVSSL IPLLVSAGLL VVILKLGNLL PYSDPSVVFV
     FLSVFAMVTI LQCFLISTLF SRANLAAACG GIIYFTLYLP YVLCVAWQDY VGFSIKIFAS
     LLSPVAFGFG CEYFALFEEQ GIGVQWDNLF ESPVEEDGFN LTTAVSMMLF DTFLYGVMTW
     YIEAVFPGQY GIPRPWYFPC TKSYWFGEEI DEKSHPGSSQ KGVSEICMEE EPTHLRLGVS
     IQNLVKVYRD GMKVAVDGLA LNFYEGQITS FLGHNGAGKT TTMSILTGLF PPTSGTAYIL
     GKDIRSEMSS IRQNLGVCPQ HNVLFDMLTV EEHIWFYARL KGLSEKHVKA EMEQMALDVG
     LPPSKLKSKT SQLSGGMQRK LSVALAFVGG SKVVILDEPT AGVDPYSRRG IWELLLKYRQ
     GRTIILSTHH MDEADILGDR IAIISHGKLC CVGSSLFLKN QLGTGYYLTL VKKDVESSLS
     SCRNSSSTVS CLKKEDSVSQ SSSDAGLGSD HESDTLTIDV SAISNLIRKH VSEARLVEDI
     GHELTYVLPY EAAKEGAFVE LFHEIDDRLS DLGISSYGIS ETTLEEIFLK VAEESGVDAE
     TSDGTLPARR NRRAFGDKQS CLHPFTEDDA VDPNDSDIDP ESRETDLLSG MDGKGSYQLK
     GWKLTQQQFV ALLWKRLLIA RRSRKGFFAQ IVLPAVFVCI ALVFSLIVPP FGKYPSLELQ
     PWMYNEQYTF VSNDAPEDMG TQELLNALTK DPGFGTRCME GNPIPDTPCL AGEEDWTISP
     VPQSIVDLFQ NGNWTMKNPS PACQCSSDKI KKMLPVCPPG AGGLPPPQRK QKTADILQNL
     TGRNISDYLV KTYVQIIAKS LKNKIWVNEF RYGGFSLGVS NSQALPPSHE VNDAIKQMKK
     LLKLTKDTSA DRFLSSLGRF MAGLDTKNNV KVWFNNKGWH AISSFLNVIN NAILRANLQK
     GENPSQYGIT AFNHPLNLTK QQLSEVALMT TSVDVLVSIC VIFAMSFVPA SFVVFLIQER
     VSKAKHLQFI SGVKPVIYWL SNFVWDMCNY VVPATLVIII FICFQQKSYV SSTNLPVLAL
     LLLLYGWSIT PLMYPASFVF KIPSTAYVVL TSVNLFIGIN GSVATFVLEL FTNNKLNDIN
     DILKSVFLIF PHFCLGRGLI DMVKNQAMAD ALERFGENRF VSPLSWDLVG RNLFAMAVEG
     VVFFLITVLI QYRFFIRPRP VKAKLPPLND EDEDVRRERQ RILDGGGQND ILEIKELTKI
     YRRKRKPAVD RICIGIPPGE CFGLLGVNGA GKSTTFKMLT GDTPVTRGDA FLNKNSILSN
     IHEVHQNMGY CPQFDAITEL LTGREHVEFF ALLRGVPEKE VGKFGEWAIR KLGLVKYGEK
     YASNYSGGNK RKLSTAMALI GGPPVVFLDE PTTGMDPKAR RFLWNCALSI VKEGRSVVLT
     SHSMEECEAL CTRMAIMVNG RFRCLGSVQH LKNRFGDGYT IVVRIAGSNP DLKPVQEFFG
     LAFPGSVLKE KHRNMLQYQL PSSLSSLARI FSILSQSKKR LHIEDYSVSQ TTLDQVFVNF
     AKDQSDDDHL KDLSLHKNQT VVDVAVLTSF LQDEKVKESY V
//
ID   ABCA2_MOUSE             Reviewed;        2434 AA.
AC   P41234;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 4.
DT   11-JAN-2011, entry version 95.
DE   RecName: Full=ATP-binding cassette sub-family A member 2;
DE   AltName: Full=ATP-binding cassette transporter 2;
DE            Short=ATP-binding cassette 2;
GN   Name=Abca2; Synonyms=Abc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=DBA/2;
RA   Chimini G.;
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 964-2434.
RC   STRAIN=DBA/2; TISSUE=Macrophage;
RX   MEDLINE=94375008; PubMed=8088782; DOI=10.1006/geno.1994.1237;
RA   Luciani M.-F., Denizot F., Savary S., Mattei M.-G., Chimini G.;
RT   "Cloning of two novel ABC transporters mapping on human chromosome
RT   9.";
RL   Genomics 21:150-159(1994).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1327 AND SER-1331, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Probable transporter, its natural substrate has not been
CC       found yet. May have a role in macrophage lipid metabolism and
CC       neural development.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- TISSUE SPECIFICITY: Widely expressed in adult tissues. Highest
CC       levels are found in brain and pregnant uterus.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA
CC       family.
CC   -!- SIMILARITY: Contains 2 ABC transporter domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X75927; CAA53531.2; -; mRNA.
DR   IPI; IPI00112616; -.
DR   PIR; B54774; B54774.
DR   UniGene; Mm.2210; -.
DR   ProteinModelPortal; P41234; -.
DR   SMR; P41234; 989-1214, 2050-2280.
DR   STRING; P41234; -.
DR   PhosphoSite; P41234; -.
DR   PRIDE; P41234; -.
DR   Ensembl; ENSMUST00000095124; ENSMUSP00000092742; ENSMUSG00000026944.
DR   MGI; MGI:99606; Abca2.
DR   HOVERGEN; HBG050436; -.
DR   ArrayExpress; P41234; -.
DR   Bgee; P41234; -.
DR   Genevestigator; P41234; -.
DR   GermOnline; ENSMUSG00000026944; Mus musculus.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; ISS:UniProtKB.
DR   GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR   GO; GO:0005815; C:microtubule organizing center; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
DR   GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB.
DR   GO; GO:0032383; P:regulation of intracellular cholesterol transport; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR   GO; GO:0048545; P:response to steroid hormone stimulus; ISS:UniProtKB.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Glycoprotein; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1   2434       ATP-binding cassette sub-family A member
FT                                2.
FT                                /FTId=PRO_0000093291.
FT   TRANSMEM     22     42       Helical; (Potential).
FT   TRANSMEM     54     74       Helical; (Potential).
FT   TRANSMEM    698    718       Helical; (Potential).
FT   TRANSMEM    749    769       Helical; (Potential).
FT   TRANSMEM    781    801       Helical; (Potential).
FT   TRANSMEM    812    832       Helical; (Potential).
FT   TRANSMEM    893    913       Helical; (Potential).
FT   TRANSMEM   1461   1481       Helical; (Potential).
FT   TRANSMEM   1793   1813       Helical; (Potential).
FT   TRANSMEM   1842   1862       Helical; (Potential).
FT   TRANSMEM   1873   1893       Helical; (Potential).
FT   TRANSMEM   1906   1926       Helical; (Potential).
FT   TRANSMEM   1992   2012       Helical; (Potential).
FT   DOMAIN      990   1221       ABC transporter 1.
FT   DOMAIN     2051   2286       ABC transporter 2.
FT   NP_BIND    1024   1031       ATP 1 (Potential).
FT   NP_BIND    2088   2095       ATP 2 (Potential).
FT   MOD_RES    1327   1327       Phosphoserine.
FT   MOD_RES    1331   1331       Phosphoserine.
FT   MOD_RES    2411   2411       Phosphothreonine (By similarity).
FT   CARBOHYD     14     14       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     89     89       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    168    168       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    173    173       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    305    305       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    368    368       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    379    379       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    420    420       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    432    432       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    476    476       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    484    484       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    494    494       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    530    530       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    548    548       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    589    589       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    599    599       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    627    627       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1408   1408       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1496   1496       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1549   1549       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1557   1557       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1613   1613       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1678   1678       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1776   1776       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2055   2055       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   2434 AA;  270509 MW;  38564C2989F0CFCC CRC64;
     MGFLHQLQLL LWKNVTLKRR SPWVLAFEIF IPLVLFFILL GLRQKKPTIS VKEAFYTAAP
     LTSAGILPVM QSLCPDGQRD EFGFLQYANS TVTQLLERLH RVVEEGNLFD PVRPSLGSEL
     EALRQRLEAL SSGPGTWESH SARPAVSSFS LDSVARDQRE LWRFLMQNLS LPNSTAQALL
     AARVDPSEVY RLLFGPLPDL DGKLGFLRKQ EPWSRLGSNP LLQMEELLLA PALLEQLTCA
     PGSGELGRIL TMPEGHQVDL QGYRDAVCSG QATARAQRFS DLAAELRNQL DTAKIAQQLG
     FDVPNGSDPQ PQAPSPQSLP ALLGDLLDAQ KLLQDVDVLS ALALLLPQGA CAGQASAPQA
     SSLNGLANST GIGANSGSNT TVEEGTQSPV SPASPDTLQG QCSAFVQLWA GLQPILCGNN
     RTIEPEALRR GNMSSLGFTS KEQRNLGLLV HLMTSNPKIL YAPVGSEADR VILKANETFA
     FVGNVTHYAQ VWLNISTEIR SFLEQGRLQQ HLQWLQQYVA DLQLHPEAMN LSLEELPPAL
     RQDFSLPNGT ALLQQLDTID NAACGWIQFM SKVSVDIFKG FPDEESIVNY TLNQAYQDNV
     TVFASVIFQT RKDGSLPPHV HYKIRQNSSF TEKTNEIRRA YWRPGPNTGG RFYFLYGLRL
     DQDMMERAII NTFVGHDVVE PGNYVQMFPY PCYTRDDFLF VIEHMMPLCM VISWVYSVAM
     TIQHIVAEKE HRLKEVMKTM GLNNAVHWVA WFITGFVQLS ISVTALTAIL KYCQVLMHSH
     VLIIWLFLAV YAVATIMFCF LVSVLYSKAK LASACGGIIY FLSYVPYMYV AIREEVAHDK
     ITAFEKCIAS RCPQQPLAWV PSTLHCMKWQ EWASIQWHTF SQSPVEGDDF NLLLAVTMLM
     VDTVVYGVLT WYIEAVHPGM YGLPRPWYSR YRSPIGWAVG GQKPGSGAGH GHTHRASALW
     RRIQACAMES RHFEETRGME EEPTHLPLVV CVDKLTKVYK NDKKLALNKL SLNLYENQVV
     SFLGHNGAGK TTTMSILTGL FPPTSGSATI YGHDIRTEMD EIRKNLGMCP QHNVLFDRLT
     VEEHLWFYSR LKSMAQEEIR KETDKMIEDL ELSNKRHSLV QTLSGGMKRK LSVAIAFVGG
     SRAIILDEPT AGVDPYARRA IWDLILKYKP GRTILLSTHH MDEADLLGDR IAIISHGKLK
     CCGSPLFLKG AYGDGYRLTL VKQPAEPGTS QEPGLASSPS GCPRLSSCSE PQVSQFIRKH
     VASSLLVSDT STELSYILPS EAVKKGAFER LFQQLEHSLD ALHLSSFGLM DTTLEEVFLK
     VSEEDQSLEN SEADVKESRK DVLPGAEGLT AVGGQAGNLA RCSELAQSQA SLQSASSVGS
     ARGEEGTGYS DGYGDYRPLF DNLQDPDNVS LQEAEMEALA QVGQGSRKLE GWWLKMRQFH
     GLLVKRFHCA RRNSKALCSQ ILLPAFFVCV AMTVALSVPE IGDLPPLVLS PSQYHNYTQP
     RGNFIPYANE ERQEYRLRLS PDASPQQLVS TFRLPSGVGA TCVLKSPANG SLGPMLNLSS
     GESRLLAARF FDSMCLESFT QGLPLSNFVP PPPSPAPSDS PVSPDEDSLQ AWNMSLPPTA
     GPETWTSAPS LPRLVHEPVR CTCSAQGTGF SCPSSVGGHP PQMRVVTGDI LTDITGHNVS
     EYLLFTSDRF RLHRYGAITF GNVQKSIPAS FGARVPPMVR KIAVRRVAQV LYNNKGYHSM
     PTYLNSLNNA ILRANLPKSK GNPAAYGITV TNHPMNKTSA SLSLDYLLQG TDVVIAIFII
     VAMSFVPASF VVFLVAEKST KAKHLQFVSG CNPVIYWLAN YVWDMLNYLV PATCCVIILF
     VFDLPAYTSP TNFPAVLSLF LLYGWSITPI MYPASFWFEV PSSAYVFLIV INLFIGITAT
     VATFLLQLFE HDKDLKVVNS YLKSCFLIFP NYNLGHGLME MAYNEYINEY YAKIGQFDKM
     KSPFEWDIVT RGLVAMTVEG FVGFFLTIMC QYNFLRQPQR LPVSTKPVED DVDVASERQR
     VLRGDADNDM VKIENLTKVY KSRKIGRILA VDRLCLGVRP GECFGLLGVN GAGKTSTFKM
     LTGDESTTGG EAFVNGHSVL KDLLQVQQSL GYCPQFDALF DELTAREHLQ LYTRLRGIPW
     KDEAQVVKWA LEKLELTKYA DKPAGTYSGG NKRKLSTAIA LIGYPAFIFL DEPTTGMDPK
     ARRFLWNLIL DLIKTGRSVV LTSHSMEECE ALCTRLAIMV NGRLRCLGSI QHLKNRFGDG
     YMITVRTKSS QNVKDVVRFF NRNFPEAMLK ERHHTKVQYQ LKSEHISLAQ VFSKMEQVVG
     VLGIEDYSVS QTTLDNVFVN FAKKQSDNVE QQEAEPSSLP SPLGLLSLLR PRPAPTELRA
     LVADEPEDLD TEDEGLISFE EERAQLSFNT DTLC
//
ID   CD86_MOUSE              Reviewed;         309 AA.
AC   P42082;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=T-lymphocyte activation antigen CD86;
DE   AltName: Full=Activation B7-2 antigen;
DE   AltName: Full=Early T-cell costimulatory molecule 1;
DE            Short=ETC-1;
DE   AltName: CD_antigen=CD86;
DE   Flags: Precursor;
GN   Name=Cd86;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=94065585; PubMed=7504059; DOI=10.1084/jem.178.6.2185;
RA   Freeman G.J., Borriello F., Hodes R.J., Reiser H., Gribben J.G.,
RA   Ng J.W., Kim J., Goldberg J.M., Hathcock K., Laszlo G., Lombard L.A.,
RA   Wang S., Gray G.S., Nadler L.M., Sharpe A.H.;
RT   "Murine B7-2, an alternative CTLA4 counter-receptor that costimulates
RT   T cell proliferation and interleukin 2 production.";
RL   J. Exp. Med. 178:2185-2192(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=94230971; PubMed=7513726;
RA   Chen C., Gault A., Shen L., Nabavi N.;
RT   "Molecular cloning and expression of early T cell costimulatory
RT   molecule-1 and its characterization as B7-2 molecule.";
RL   J. Immunol. 152:4929-4936(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=129;
RX   MEDLINE=96094437; PubMed=7499829;
RA   Borriello F., Oliveros J., Freeman G.J., Nadler L.M., Sharpe A.H.;
RT   "Differential expression of alternate mB7-2 transcripts.";
RL   J. Immunol. 155:5490-5497(1995).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-291, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Receptor involved in the costimulatory signal essential
CC       for T-lymphocyte proliferation and interleukin-2 production, by
CC       binding CD28 or CTLA-4. May play a critical role in the early
CC       events of T-cell activation and costimulation of naive T-cells,
CC       such as deciding between immunity and anergy that is made by T-
CC       cells within 24 hours after activation.
CC   -!- SUBUNIT: Interacts with MARCH8 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P42082-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P42082-2; Sequence=VSP_023125;
CC   -!- TISSUE SPECIFICITY: Expressed on activated B-cells.
CC   -!- PTM: Polyubiquitinated; which is promoted by MARCH8 and results in
CC       endocytosis and lysosomal degradation (By similarity).
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC       domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB30744.2; Type=Erroneous initiation;
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DR   EMBL; L25606; AAA79770.1; -; mRNA.
DR   EMBL; S70108; AAB30744.2; ALT_INIT; mRNA.
DR   EMBL; U39456; AAC52334.1; -; Genomic_DNA.
DR   EMBL; U39459; AAC52334.1; JOINED; Genomic_DNA.
DR   EMBL; U39461; AAC52334.1; JOINED; Genomic_DNA.
DR   EMBL; U39462; AAC52334.1; JOINED; Genomic_DNA.
DR   EMBL; U39463; AAC52334.1; JOINED; Genomic_DNA.
DR   EMBL; U39464; AAC52334.1; JOINED; Genomic_DNA.
DR   EMBL; U39465; AAC52334.1; JOINED; Genomic_DNA.
DR   EMBL; U39466; AAC52334.1; JOINED; Genomic_DNA.
DR   EMBL; U39456; AAC52336.1; -; Genomic_DNA.
DR   EMBL; U39461; AAC52336.1; JOINED; Genomic_DNA.
DR   EMBL; U39462; AAC52336.1; JOINED; Genomic_DNA.
DR   EMBL; U39463; AAC52336.1; JOINED; Genomic_DNA.
DR   EMBL; U39464; AAC52336.1; JOINED; Genomic_DNA.
DR   EMBL; U39465; AAC52336.1; JOINED; Genomic_DNA.
DR   EMBL; U39466; AAC52336.1; JOINED; Genomic_DNA.
DR   IPI; IPI00620020; -.
DR   IPI; IPI00828409; -.
DR   PIR; I49522; I49522.
DR   RefSeq; NP_062261.3; NM_019388.3.
DR   UniGene; Mm.1452; -.
DR   ProteinModelPortal; P42082; -.
DR   SMR; P42082; 26-222.
DR   STRING; P42082; -.
DR   PhosphoSite; P42082; -.
DR   Ensembl; ENSMUST00000023618; ENSMUSP00000023618; ENSMUSG00000022901.
DR   Ensembl; ENSMUST00000089620; ENSMUSP00000087047; ENSMUSG00000022901.
DR   GeneID; 12524; -.
DR   KEGG; mmu:12524; -.
DR   CTD; 12524; -.
DR   MGI; MGI:101773; Cd86.
DR   eggNOG; roNOG16208; -.
DR   HOVERGEN; HBG004093; -.
DR   OrthoDB; EOG49S66Q; -.
DR   NextBio; 281542; -.
DR   ArrayExpress; P42082; -.
DR   Bgee; P42082; -.
DR   CleanEx; MM_CD86; -.
DR   Genevestigator; P42082; -.
DR   GermOnline; ENSMUSG00000022901; Mus musculus.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:MGI.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0042113; P:B cell activation; IDA:MGI.
DR   GO; GO:0002224; P:toll-like receptor signaling pathway; IDA:MGI.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR003596; Ig_V-set_sub.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00406; IGv; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00290; IG_MHC; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Phosphoprotein; Receptor; Signal;
KW   Transmembrane; Transmembrane helix; Ubl conjugation.
FT   SIGNAL        1     23       Potential.
FT   CHAIN        24    309       T-lymphocyte activation antigen CD86.
FT                                /FTId=PRO_0000014551.
FT   TOPO_DOM     24    244       Extracellular (Potential).
FT   TRANSMEM    245    265       Helical; (Potential).
FT   TOPO_DOM    266    309       Cytoplasmic (Potential).
FT   DOMAIN       33    128       Ig-like V-type.
FT   DOMAIN      150    223       Ig-like C2-type.
FT   MOD_RES     291    291       Phosphothreonine.
FT   CARBOHYD     33     33       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     47     47       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     92     92       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    135    135       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    146    146       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    154    154       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    175    175       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    190    190       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    231    231       N-linked (GlcNAc...) (Potential).
FT   DISULFID     40    110       Potential.
FT   DISULFID    157    216       Potential.
FT   VAR_SEQ       1      6       Missing (in isoform 2).
FT                                /FTId=VSP_023125.
SQ   SEQUENCE   309 AA;  34666 MW;  8F58DCD1FB81D5EA CRC64;
     MDPRCTMGLA ILIFVTVLLI SDAVSVETQA YFNGTAYLPC PFTKAQNISL SELVVFWQDQ
     QKLVLYEHYL GTEKLDSVNA KYLGRTSFDR NNWTLRLHNV QIKDMGSYDC FIQKKPPTGS
     IILQQTLTEL SVIANFSEPE IKLAQNVTGN SGINLTCTSK QGHPKPKKMY FLITNSTNEY
     GDNMQISQDN VTELFSISNS LSLSFPDGVW HMTVVCVLET ESMKISSKPL NFTQEFPSPQ
     TYWKEITASV TVALLLVMLL IIVCHKKPNQ PSRPSNTASK LERDSNADRE TINLKELEPQ
     IASAKPNAE
//
ID   SEPT2_MOUSE             Reviewed;         361 AA.
AC   P42208; B2RRZ2; Q3U9Y5;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   08-MAR-2011, entry version 104.
DE   RecName: Full=Septin-2;
DE   AltName: Full=Neural precursor cell expressed developmentally down-regulated protein 5;
DE            Short=NEDD-5;
GN   Name=Sept2; Synonyms=Nedd-5, Nedd5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF GLY-47;
RP   SER-51 AND GLN-125.
RC   TISSUE=Neural tube;
RX   MEDLINE=97347241; PubMed=9203580;
RA   Kinoshita M., Kumar S., Noda M.;
RT   "Nedd5, a mammalian septin, is a novel cytoskeletal component
RT   interacting with actin-based structures.";
RL   Genes Dev. 11:1535-1547(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 51-66; 97-112 AND 117-128, AND MASS SPECTROMETRY.
RC   TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [6]
RP   INTERACTION WITH SEPT5 AND SEPT7, LACK OF INTERACTION WITH SEPT4, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=11739749; DOI=10.1128/MCB.22.1.378-387.2002;
RA   Peng X.-R., Jia Z., Zhang Y., Ware J., Trimble W.S.;
RT   "The septin CDCrel-1 is dispensable for normal development and
RT   neurotransmitter release.";
RL   Mol. Cell. Biol. 22:378-387(2002).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 33-306 IN COMPLEX WITH
RP   GPPNHP, AND MUTAGENESIS OF SER-46 AND THR-78.
RX   PubMed=19805342; DOI=10.1073/pnas.0902858106;
RA   Sirajuddin M., Farkasovsky M., Zent E., Wittinghofer A.;
RT   "GTP-induced conformational changes in septins and implications for
RT   function.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:16592-16597(2009).
CC   -!- FUNCTION: Filament-forming cytoskeletal GTPase. Required for
CC       normal organization of the actin cytoskeleton. Plays a role in the
CC       biogenesis of polarized columnar-shaped epithelium. Required for
CC       the progression through mitosis. Forms a scaffold at the midplane
CC       of the mitotic splindle required to maintain CENPE localization at
CC       kinetochores and consequently chromosome congression. During
CC       anaphase, may be required for chromosome segregation and spindle
CC       elongation (By similarity).
CC   -!- SUBUNIT: Septins polymerize into heterooligomeric protein
CC       complexes that form filaments, and associate with cellular
CC       membranes, actin filaments and microtubules. GTPase activity is
CC       required for filament formation. Septin filaments are assembled
CC       from asymmetrical heterotrimers, composed of SEPT2, SEPT6 and
CC       SEPT7 that associate head-to-head to form a hexameric unit.
CC       Interaction between SEPT2 and SEPT7 seems indirect. Interacts also
CC       with SEPT9 and SEPT5. Interaction with SEPT4 not detected.
CC       Interacts with MAP4 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
CC       Cytoplasm, cytoskeleton, spindle (By similarity). Chromosome,
CC       centromere, kinetochore (By similarity). Cleavage furrow (By
CC       similarity). Midbody (By similarity). Note=In metaphase cells,
CC       localized within the microtubule spindle. At the metaphase plate,
CC       in close apposition to the kinetochores of the congressed
CC       chromosomes. In cells undergoing cytokinesis, localized to the
CC       midbody, the ingressing cleavage furrow, and the central spindle
CC       (By similarity). In interphase and postmitotic cells, localised to
CC       fibrous or granular structures, depending on the growth state of
CC       the cell.
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- DEVELOPMENTAL STAGE: Expressed at 17 dpc in the brain with levels
CC       remaining relatively stable up to adulthood (at protein level).
CC   -!- MISCELLANEOUS: Coordinated expression with SEPT6 and SEPT7 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the septin family.
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DR   EMBL; D49382; BAA08380.1; -; mRNA.
DR   EMBL; AK028072; BAC25737.1; -; mRNA.
DR   EMBL; AK146616; BAE27305.1; -; mRNA.
DR   EMBL; AK151591; BAE30531.1; -; mRNA.
DR   EMBL; AK171331; BAE42396.1; -; mRNA.
DR   EMBL; CH466520; EDL39946.1; -; Genomic_DNA.
DR   EMBL; CH466520; EDL39948.1; -; Genomic_DNA.
DR   EMBL; BC138636; AAI38637.1; -; mRNA.
DR   EMBL; BC138637; AAI38638.1; -; mRNA.
DR   IPI; IPI00114945; -.
DR   RefSeq; NP_001153189.1; NM_001159717.1.
DR   RefSeq; NP_001153190.1; NM_001159718.1.
DR   RefSeq; NP_001153191.1; NM_001159719.1.
DR   RefSeq; NP_035021.1; NM_010891.2.
DR   UniGene; Mm.428652; -.
DR   PDB; 3FTQ; X-ray; 2.90 A; A/B/C/D=33-306.
DR   PDBsum; 3FTQ; -.
DR   ProteinModelPortal; P42208; -.
DR   SMR; P42208; 34-305.
DR   DIP; DIP-32438N; -.
DR   MINT; MINT-3378243; -.
DR   STRING; P42208; -.
DR   PhosphoSite; P42208; -.
DR   REPRODUCTION-2DPAGE; IPI00114945; -.
DR   REPRODUCTION-2DPAGE; P42208; -.
DR   PRIDE; P42208; -.
DR   Ensembl; ENSMUST00000027495; ENSMUSP00000027495; ENSMUSG00000026276.
DR   GeneID; 18000; -.
DR   KEGG; mmu:18000; -.
DR   UCSC; uc007cea.1; mouse.
DR   CTD; 18000; -.
DR   MGI; MGI:97298; Sept2.
DR   eggNOG; roNOG14561; -.
DR   GeneTree; ENSGT00590000082878; -.
DR   HOGENOM; HBG715249; -.
DR   HOVERGEN; HBG065093; -.
DR   InParanoid; P42208; -.
DR   OMA; MQLQMQG; -.
DR   OrthoDB; EOG47SSF3; -.
DR   PhylomeDB; P42208; -.
DR   NextBio; 292999; -.
DR   ArrayExpress; P42208; -.
DR   Bgee; P42208; -.
DR   CleanEx; MM_SEPT2; -.
DR   Genevestigator; P42208; -.
DR   GermOnline; ENSMUSG00000026276; Mus musculus.
DR   GO; GO:0005826; C:actomyosin contractile ring; NAS:UniProtKB.
DR   GO; GO:0042995; C:cell projection; IDA:MGI.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR   GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; TAS:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0031105; C:septin complex; IEA:InterPro.
DR   GO; GO:0005876; C:spindle microtubule; TAS:MGI.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
DR   GO; GO:0030234; F:enzyme regulator activity; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; NAS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; TAS:MGI.
DR   GO; GO:0032947; F:protein complex scaffold; IDA:MGI.
DR   GO; GO:0000910; P:cytokinesis; NAS:UniProtKB.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0051258; P:protein polymerization; TAS:MGI.
DR   GO; GO:0002036; P:regulation of L-glutamate transport; IDA:MGI.
DR   GO; GO:0032880; P:regulation of protein localization; IDA:MGI.
DR   InterPro; IPR000038; Cell_Div_GTP-bd.
DR   InterPro; IPR016491; Septin.
DR   InterPro; IPR008113; Septin2.
DR   PANTHER; PTHR18884; Cell_Div_GTP_bd; 1.
DR   Pfam; PF00735; Septin; 1.
DR   PIRSF; PIRSF006698; Septin; 1.
DR   PRINTS; PR01740; SEPTIN2.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell cycle; Cell division; Centromere;
KW   Chromosome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   GTP-binding; Kinetochore; Mitosis; Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1    361       Septin-2.
FT                                /FTId=PRO_0000173516.
FT   NP_BIND      44     52       GTP.
FT   NP_BIND     183    186       GTP.
FT   REGION      260    270       Important for dimerization (By
FT                                similarity).
FT   BINDING      78     78       GTP.
FT   BINDING     104    104       GTP; via amide nitrogen.
FT   BINDING     241    241       GTP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     256    256       GTP.
FT   BINDING     258    258       GTP (By similarity).
FT   SITE        156    156       Important for dimerization (By
FT                                similarity).
FT   MOD_RES      17     17       Phosphotyrosine (By similarity).
FT   MOD_RES     190    190       N6-acetyllysine (By similarity).
FT   MOD_RES     211    211       Phosphotyrosine (By similarity).
FT   MOD_RES     218    218       Phosphoserine.
FT   MOD_RES     228    228       Phosphothreonine (By similarity).
FT   MUTAGEN      46     46       S->D: Loss of GTP-binding.
FT   MUTAGEN      47     47       G->V: Loss of GTP-binding activity.
FT   MUTAGEN      51     51       S->N: Loss of GTP-binding activity.
FT   MUTAGEN      78     78       T->G: Reduces affinity for GTP 20-fold.
FT   MUTAGEN     125    125       Q->L: Loss of GTP-binding activity.
FT   STRAND       37     43
FT   HELIX        51     55
FT   STRAND       82     89
FT   STRAND       94    101
FT   HELIX       111    133
FT   STRAND      148    153
FT   HELIX       162    171
FT   TURN        172    175
FT   STRAND      177    182
FT   HELIX       184    186
FT   HELIX       189    205
FT   HELIX       222    233
FT   STRAND      236    238
FT   TURN        268    270
FT   HELIX       273    293
FT   HELIX       295    303
SQ   SEQUENCE   361 AA;  41526 MW;  C4BFFB3F1815E081 CRC64;
     MSKQQPTQFI NPETPGYVGF ANLPNQVHRK SVKKGFEFTL MVVGESGLGK STLINSLFLT
     DLYPERIIPG AAEKIERTVQ IEASTVEIEE RGVKLRLTVV DTPGYGDAIN CRDCFKTIIS
     YIDEQFERYL HDESGLNRRH IIDNRVHCCF YFISPFGHGL KPLDVAFMKA IHNKVNIVPV
     IAKADTLTLK ERERLKKRIL DEIEEHSIKI YHLPDAESDE DEDFKEQTRL LKASIPFSVV
     GSNQLIEAKG KKVRGRLYPW GVVEVENPEH NDFLKLRTML ITHMQDLQEV TQDLHYENFR
     SERLKRGGRK VENEDMNKDQ ILLEKEAELR RMQEMIARMQ AQMQMQMQGG DSDSGALGQH
     V
//
ID   STAT3_MOUSE             Reviewed;         770 AA.
AC   P42227; A2A5D1; B7ZC17;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   08-MAR-2011, entry version 129.
DE   RecName: Full=Signal transducer and activator of transcription 3;
DE   AltName: Full=Acute-phase response factor;
GN   Name=Stat3; Synonyms=Aprf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM STAT3A), AND PROTEIN SEQUENCE OF
RP   154-158; 181-185 AND 632-640.
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=94208062; PubMed=7512451; DOI=10.1016/0092-8674(94)90235-6;
RA   Akira S., Nishio Y., Inoue M., Wang X.-J., Wei S., Matsusaka T.,
RA   Yoshida K., Sudo T., Naruto M., Kishimoto T.;
RT   "Molecular cloning of APRF, a novel IFN-stimulated gene factor 3 p91-
RT   related transcription factor involved in the gp130-mediated signaling
RT   pathway.";
RL   Cell 77:63-71(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DEL-701).
RC   TISSUE=Brain;
RX   MEDLINE=95014185; PubMed=7523373;
RA   Raz R., Durbin J.E., Levy D.E.;
RT   "Acute phase response factor and additional members of the interferon-
RT   stimulated gene factor 3 family integrate diverse signals from
RT   cytokines, interferons, and growth factors.";
RL   J. Biol. Chem. 269:24391-24395(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM STAT3A).
RC   TISSUE=Thymus;
RX   MEDLINE=94188718; PubMed=8140422; DOI=10.1126/science.8140422;
RA   Zhong Z., Wen Z., Darnell J.E. Jr.;
RT   "Stat3: a STAT family member activated by tyrosine phosphorylation in
RT   response to epidermal growth factor and interleukin-6.";
RL   Science 264:95-98(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM STAT3B).
RC   STRAIN=BALB/c, and C57BL/6; TISSUE=Liver;
RX   MEDLINE=96016116; PubMed=7568080; DOI=10.1073/pnas.92.20.9097;
RA   Schaefer T.S., Sanders L.K., Nathans D.;
RT   "Cooperative transcriptional activity of Jun and Stat3 beta, a short
RT   form of Stat3.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:9097-9101(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM STAT3A).
RC   STRAIN=129/SvJ;
RX   MEDLINE=21100887; PubMed=11161808; DOI=10.1006/geno.2000.6433;
RA   Miyoshi K., Cui Y., Riedlinger G., Robinson P., Lehoczky J., Zon L.,
RA   Oka T., Dewar K., Hennighausen L.;
RT   "Structure of the mouse Stat 3/5 locus: evolution from Drosophila to
RT   zebrafish to mouse.";
RL   Genomics 71:150-155(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM STAT3A).
RC   STRAIN=C57BL/6J, and NOD/LtJ;
RA   Davoodi-Semiromi A., She J.-X.;
RT   "A mutant Stat5b with weaker DNA binding defines a key defective
RT   pathway in non-obese diabetic (NOD) mice.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM STAT3A).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   PHOSPHORYLATION AT SER-727, AND MUTAGENESIS.
RX   MEDLINE=95354205; PubMed=7543024; DOI=10.1016/0092-8674(95)90311-9;
RA   Wen Z., Zhong Z., Darnell J.E. Jr.;
RT   "Maximal activation of transcription by Stat1 and Stat3 requires both
RT   tyrosine and serine phosphorylation.";
RL   Cell 82:241-250(1995).
RN   [10]
RP   INTERACTION WITH STATIP1.
RX   MEDLINE=20420342; PubMed=10954736; DOI=10.1073/pnas.170192197;
RA   Collum R.G., Brutsaert S., Lee G., Schindler C.;
RT   "A Stat3-interacting protein (StIP1) regulates cytokine signal
RT   transduction.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:10120-10125(2000).
RN   [11]
RP   INTERACTION WITH NLK, PHOSPHORYLATION AT SER-727, AND MUTAGENESIS OF
RP   SER-727.
RX   PubMed=15004007; DOI=10.1101/gad.1166904;
RA   Ohkawara B., Shirakabe K., Hyodo-Miura J., Matsuo R., Ueno N.,
RA   Matsumoto K., Shibuya H.;
RT   "Role of the TAK1-NLK-STAT3 pathway in TGF-beta-mediated mesoderm
RT   induction.";
RL   Genes Dev. 18:381-386(2004).
RN   [12]
RP   SUBCELLULAR LOCATION, MUTAGENESIS OF VAL-77; LEU-78; PHE-174; ARG-609
RP   AND TYR-705, INTERACTION WITH KPNA4 AND KPNA5, AND NUCLEAR IMPORT
RP   MOTIF.
RX   PubMed=15919823; DOI=10.1073/pnas.0501643102;
RA   Liu L., McBride K.M., Reich N.C.;
RT   "STAT3 nuclear import is independent of tyrosine phosphorylation and
RT   mediated by importin-alpha3.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:8150-8155(2005).
RN   [13]
RP   INTERACTION WITH SIPAR.
RC   STRAIN=Swiss Webster / NIH;
RA   Ning H., Rong Y., Zhang Y., Chang Z.;
RT   "SIPAR interacts with STAT3 to regulate its signal pathway.";
RL   Sheng Wu Hua Xue Yu Sheng Wu Wu Li Jin Zhan 32:173-179(2005).
RN   [14]
RP   INTERACTION WITH ARL2BP.
RX   PubMed=18234692; DOI=10.1093/intimm/dxm154;
RA   Muromoto R., Sekine Y., Imoto S., Ikeda O., Okayama T., Sato N.,
RA   Matsuda T.;
RT   "BART is essential for nuclear retention of STAT3.";
RL   Int. Immunol. 20:395-403(2008).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-705, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 136-716.
RX   MEDLINE=98334373; PubMed=9671298; DOI=10.1038/28101;
RA   Becker S., Groner B., Mueller C.W.;
RT   "Three-dimensional structure of the Stat3beta homodimer bound to
RT   DNA.";
RL   Nature 394:145-151(1998).
CC   -!- FUNCTION: Transcription factor that binds to the interleukin-6
CC       (IL-6)-responsive elements identified in the promoters of various
CC       acute-phase protein genes. Activated by IL31 through IL31RA.
CC       STAT3B interacts with the N-terminal part of JUN to activate such
CC       promoters in a cooperative way.
CC   -!- SUBUNIT: Forms a homodimer or a heterodimer with a related family
CC       member (at least STAT1). Interacts with IL31RA, NCOA1, PELP1,
CC       SIPAR, SOCS7, STATIP1 and TMF1. Interacts with IL23R in presence
CC       of IL23. Interacts (via SH2 domain) with NLK. Interacts with KPNA4
CC       and KPNA5; KPNA4 may be the primary mediator of nuclear import.
CC       Interacts with CAV2; the interaction is increased on insulin-
CC       induced tyrosine phosphorylation of CAV2 and leads to STAT3
CC       activation. Interacts with ARL2BP; interaction is enhanced with
CC       ARL2 (By similarity). Interacts with ARL2BP; the interaction is
CC       enhanced by LIF and JAK1 expression.
CC   -!- INTERACTION:
CC       O35387:Hax1; NbExp=2; IntAct=EBI-602878, EBI-642449;
CC       P40189:IL6ST (xeno); NbExp=2; IntAct=EBI-602878, EBI-1030834;
CC       O43318:MAP3K7 (xeno); NbExp=1; IntAct=EBI-602878, EBI-358684;
CC       Q99KX1:Mlf2; NbExp=2; IntAct=EBI-602878, EBI-646781;
CC       P12931:SRC (xeno); NbExp=1; IntAct=EBI-602878, EBI-621482;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly
CC       present in the cytoplasm without stimuli. Upon leukemia inhibitory
CC       factor (LIF) stimulation, accumulates in the nucleus. The complex
CC       composed of BART and ARL2 plays an important role in the nuclear
CC       translocation and retention of STAT3 (By similarity). Shuttles
CC       between the nucleus and the cytoplasm. Constitutive nuclear
CC       presence is independent of tyrosine phosphorylation.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=Stat3A;
CC         IsoId=P42227-1; Sequence=Displayed;
CC       Name=Stat3B;
CC         IsoId=P42227-2; Sequence=VSP_006287;
CC       Name=Del-701;
CC         IsoId=P42227-3; Sequence=VSP_010475;
CC   -!- TISSUE SPECIFICITY: STAT3A is seen in the liver, spleen, and
CC       kidney. STAT3B is also detected in the liver, although in a much
CC       less abundant manner.
CC   -!- PTM: Tyrosine phosphorylated in response to IL-6, IL-11, CNTF,
CC       LIF, CSF-1, EGF, PDGF, IFN-alpha and OSM. Phosphorylated on serine
CC       upon DNA damage, probably by ATM or ATR. Serine phosphorylation is
CC       important for the formation of stable DNA-binding STAT3 homodimers
CC       and maximal transcriptional activity. ARL2BP may participate in
CC       keeping the phosphorylated state of STAT3 within the nucleus.
CC       Tyrosine phosphorylated upon stimulation with EGF (By similarity).
CC   -!- MISCELLANEOUS: Involved in the gp130-mediated signaling pathway.
CC   -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
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DR   EMBL; L29278; AAA37254.1; -; mRNA.
DR   EMBL; U08378; AAA56668.1; -; mRNA.
DR   EMBL; U06922; AAA19452.1; -; mRNA.
DR   EMBL; U30709; AAC52612.1; -; mRNA.
DR   EMBL; AF246978; AAL59017.1; -; Genomic_DNA.
DR   EMBL; AY299489; AAQ75418.1; -; mRNA.
DR   EMBL; AY299490; AAQ75419.1; -; mRNA.
DR   EMBL; AL591466; CAM19461.1; -; Genomic_DNA.
DR   EMBL; AL591466; CAX15620.1; -; Genomic_DNA.
DR   EMBL; BC003806; AAH03806.1; -; mRNA.
DR   IPI; IPI00227814; -.
DR   IPI; IPI00228955; -.
DR   IPI; IPI00753792; -.
DR   PIR; I49508; I49508.
DR   RefSeq; NP_035616.1; NM_011486.4.
DR   RefSeq; NP_998824.1; NM_213659.2.
DR   RefSeq; NP_998825.1; NM_213660.2.
DR   UniGene; Mm.249934; -.
DR   PDB; 1BG1; X-ray; 2.25 A; A=127-715.
DR   PDB; 3CWG; X-ray; 3.05 A; A/B=127-688.
DR   PDBsum; 1BG1; -.
DR   PDBsum; 3CWG; -.
DR   ProteinModelPortal; P42227; -.
DR   SMR; P42227; 2-715.
DR   DIP; DIP-24240N; -.
DR   DIP; DIP-442N; -.
DR   IntAct; P42227; 30.
DR   MINT; MINT-4135802; -.
DR   STRING; P42227; -.
DR   PhosphoSite; P42227; -.
DR   PRIDE; P42227; -.
DR   Ensembl; ENSMUST00000092671; ENSMUSP00000090342; ENSMUSG00000004040.
DR   Ensembl; ENSMUST00000103113; ENSMUSP00000099402; ENSMUSG00000004040.
DR   GeneID; 20848; -.
DR   KEGG; mmu:20848; -.
DR   UCSC; uc007lmp.1; mouse.
DR   UCSC; uc007lmq.1; mouse.
DR   CTD; 20848; -.
DR   MGI; MGI:103038; Stat3.
DR   HOGENOM; HBG446644; -.
DR   HOVERGEN; HBG055669; -.
DR   InParanoid; P42227; -.
DR   OMA; NKESHAT; -.
DR   OrthoDB; EOG4G4GPS; -.
DR   NextBio; 299623; -.
DR   ArrayExpress; P42227; -.
DR   Bgee; P42227; -.
DR   Genevestigator; P42227; -.
DR   GermOnline; ENSMUSG00000004040; Mus musculus.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IPI:MGI.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0016563; F:transcription activator activity; IDA:MGI.
DR   GO; GO:0008134; F:transcription factor binding; ISS:UniProtKB.
DR   GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; NAS:UniProtKB.
DR   GO; GO:0042755; P:eating behavior; IMP:MGI.
DR   GO; GO:0001754; P:eye photoreceptor cell differentiation; IMP:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0060397; P:JAK-STAT cascade involved in growth hormone signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
DR   GO; GO:0006606; P:protein import into nucleus; ISS:UniProtKB.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
DR   GO; GO:0019953; P:sexual reproduction; IMP:MGI.
DR   GO; GO:0001659; P:temperature homeostasis; IMP:MGI.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:MGI.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR013800; STAT_TF_alpha.
DR   InterPro; IPR015988; STAT_TF_coiled-coil.
DR   InterPro; IPR001217; STAT_TF_core.
DR   InterPro; IPR013801; STAT_TF_DNA-bd.
DR   InterPro; IPR012345; STAT_TF_DNA-bd_sub.
DR   InterPro; IPR013799; STAT_TF_prot_interaction.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Gene3D; G3DSA:1.20.1050.20; STAT_alpha; 1.
DR   Gene3D; G3DSA:2.60.40.630; STAT_DNA_bd_sub; 1.
DR   Gene3D; G3DSA:1.10.532.10; STAT_protein_interaction; 1.
DR   PANTHER; PTHR11801; STAT; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF01017; STAT_alpha; 1.
DR   Pfam; PF02864; STAT_bind; 1.
DR   Pfam; PF02865; STAT_int; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00964; STAT_int; 1.
DR   SUPFAM; SSF49417; P53_like_DNA_bnd; 1.
DR   SUPFAM; SSF47655; STAT; 1.
DR   SUPFAM; SSF48092; STAT; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Acute phase; Alternative splicing; Cytoplasm;
KW   Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein;
KW   SH2 domain; Transcription; Transcription regulation.
FT   CHAIN         1    770       Signal transducer and activator of
FT                                transcription 3.
FT                                /FTId=PRO_0000182418.
FT   DOMAIN      580    670       SH2.
FT   MOTIF       150    162       Essential for nuclear import.
FT   MOD_RES     539    539       Phosphotyrosine (By similarity).
FT   MOD_RES     691    691       Phosphoserine (By similarity).
FT   MOD_RES     705    705       Phosphotyrosine.
FT   MOD_RES     714    714       Phosphothreonine (By similarity).
FT   MOD_RES     727    727       Phosphoserine; by NLK.
FT   VAR_SEQ     701    701       Missing (in isoform Del-701).
FT                                /FTId=VSP_010475.
FT   VAR_SEQ     716    770       TTCSNTIDLPMSPRTLDSLMQFGNNGEGAEPSAGGQFESLT
FT                                FDMDLTSECATSPM -> FIDAVWK (in isoform
FT                                Stat3B).
FT                                /FTId=VSP_006287.
FT   MUTAGEN      77     77       V->A: No effect on nuclear import; when
FT                                associated with A-78 and W-174.
FT   MUTAGEN      78     78       L->A: No effect on nuclear import; when
FT                                associated with A-77 and W-174.
FT   MUTAGEN     174    174       F->W: No effect on nuclear import; when
FT                                associated with A-77 and A-78.
FT   MUTAGEN     609    609       R->A: Nuclear localization to the same
FT                                extent as wild-type; when associated with
FT                                F-705.
FT   MUTAGEN     705    705       Y->F: Nuclear localization to the same
FT                                extent as wild-type; when associated with
FT                                A-609.
FT   MUTAGEN     727    727       S->A: Decreased transcriptional
FT                                activation.
FT   CONFLICT     16     16       E -> K (in Ref. 2; AAA19452).
FT   CONFLICT     25     25       S -> T (in Ref. 2; AAA19452 and 4;
FT                                AAC52612).
FT   CONFLICT    394    394       M -> I (in Ref. 1; AAA37254).
FT   HELIX       139    180
FT   HELIX       199    237
FT   HELIX       239    251
FT   HELIX       261    290
FT   TURN        297    301
FT   HELIX       302    320
FT   STRAND      321    328
FT   STRAND      338    340
FT   STRAND      345    353
FT   HELIX       356    358
FT   TURN        359    361
FT   STRAND      363    369
FT   HELIX       371    373
FT   STRAND      375    377
FT   STRAND      384    388
FT   STRAND      391    393
FT   STRAND      404    415
FT   STRAND      418    420
FT   HELIX       426    428
FT   HELIX       432    434
FT   STRAND      439    447
FT   STRAND      450    457
FT   STRAND      461    466
FT   HELIX       467    469
FT   HELIX       470    483
FT   HELIX       492    494
FT   HELIX       501    515
FT   HELIX       522    533
FT   HELIX       546    549
FT   HELIX       561    574
FT   HELIX       578    581
FT   HELIX       593    595
FT   TURN        596    600
FT   STRAND      608    610
FT   STRAND      619    621
FT   STRAND      626    628
FT   HELIX       642    645
FT   HELIX       650    653
FT   STRAND      664    666
FT   STRAND      671    673
FT   TURN        674    676
FT   TURN        679    683
FT   HELIX       684    686
SQ   SEQUENCE   770 AA;  88054 MW;  6C00626711C8012D CRC64;
     MAQWNQLQQL DTRYLEQLHQ LYSDSFPMEL RQFLAPWIES QDWAYAASKE SHATLVFHNL
     LGEIDQQYSR FLQESNVLYQ HNLRRIKQFL QSRYLEKPME IARIVARCLW EESRLLQTAA
     TAAQQGGQAN HPTAAVVTEK QQMLEQHLQD VRKRVQDLEQ KMKVVENLQD DFDFNYKTLK
     SQGDMQDLNG NNQSVTRQKM QQLEQMLTAL DQMRRSIVSE LAGLLSAMEY VQKTLTDEEL
     ADWKRRQQIA CIGGPPNICL DRLENWITSL AESQLQTRQQ IKKLEELQQK VSYKGDPIVQ
     HRPMLEERIV ELFRNLMKSA FVVERQPCMP MHPDRPLVIK TGVQFTTKVR LLVKFPELNY
     QLKIKVCIDK DSGDVAALRG SRKFNILGTN TKVMNMEESN NGSLSAEFKH LTLREQRCGN
     GGRANCDASL IVTEELHLIT FETEVYHQGL KIDLETHSLP VVVISNICQM PNAWASILWY
     NMLTNNPKNV NFFTKPPIGT WDQVAEVLSW QFSSTTKRGL SIEQLTTLAE KLLGPGVNYS
     GCQITWAKFC KENMAGKGFS FWVWLDNIID LVKKYILALW NEGYIMGFIS KERERAILST
     KPPGTFLLRF SESSKEGGVT FTWVEKDISG KTQIQSVEPY TKQQLNNMSF AEIIMGYKIM
     DATNILVSPL VYLYPDIPKE EAFGKYCRPE SQEHPEADPG SAAPYLKTKF ICVTPTTCSN
     TIDLPMSPRT LDSLMQFGNN GEGAEPSAGG QFESLTFDMD LTSECATSPM
//
ID   EPS15_MOUSE             Reviewed;         897 AA.
AC   P42567; Q8C431;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   08-MAR-2011, entry version 112.
DE   RecName: Full=Epidermal growth factor receptor substrate 15;
DE            Short=Protein Eps15;
DE   AltName: Full=Protein AF-1p;
GN   Name=Eps15;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Fibroblast;
RX   MEDLINE=93361014; PubMed=7689153;
RA   Fazioli F., Minichiello L., Matoskova B., Wong W.T., di Fiore P.P.;
RT   "eps15, a novel tyrosine kinase substrate, exhibits transforming
RT   activity.";
RL   Mol. Cell. Biol. 13:5814-5828(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   PROTEIN SEQUENCE OF 838-862, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION AT TYR-850, AND MUTAGENESIS OF TYR-850.
RX   MEDLINE=20411232; PubMed=10953014; DOI=10.1083/jcb.150.4.905;
RA   Confalonieri S., Salcini A.E., Puri C., Tacchetti C., Di Fiore P.P.;
RT   "Tyrosine phosphorylation of Eps15 is required for ligand-regulated,
RT   but not constitutive, endocytosis.";
RL   J. Cell Biol. 150:905-912(2000).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-324; SER-561;
RP   SER-562 AND THR-781, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-779 AND SER-816, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   STRUCTURE BY NMR OF 7-105.
RX   MEDLINE=99400466; PubMed=10471276; DOI=10.1021/bi990922i;
RA   Whitehead B., Tessari M., Carotenuto A.,
RA   van Bergen en Henegouwen P.M., Vuister G.W.;
RT   "The EH1 domain of Eps15 is structurally classified as a member of the
RT   S100 subclass of EF-hand-containing proteins.";
RL   Biochemistry 38:11271-11277(1999).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.22 ANGSTROMS) OF 628-632 IN COMPLEX WITH
RP   AP2A2.
RX   PubMed=12057195; DOI=10.1016/S0969-2126(02)00784-0;
RA   Brett T.J., Traub L.M., Fremont D.H.;
RT   "Accessory protein recruitment motifs in clathrin-mediated
RT   endocytosis.";
RL   Structure 10:797-809(2002).
CC   -!- FUNCTION: Involved in cell growth regulation. May be involved in
CC       the regulation of mitogenic signals and control of cell
CC       proliferation. Involved in the internalization of ligand-inducible
CC       receptors of the receptor tyrosine kinase (RTK) type, in
CC       particular EGFR. Plays a role in the assembly of clathrin-coated
CC       pits.
CC   -!- SUBUNIT: Interacts with HGS; the interaction bridges the
CC       interaction of STAM or STAM2 with EPS15. Isoform 2 interacts with
CC       HGS and AP2A2. Part of a complex at least composed of EPS15, HGS,
CC       and either STAM1 or STAM2. Binds AP2A2. Interacts with AP2B1;
CC       clathrin competes with EPS15. Binds STON2 and EPN1. Interacts (via
CC       its SH3-binding sites) with CRK. Interacts with SH3BP4/TTP (By
CC       similarity).
CC   -!- INTERACTION:
CC       Q60902:Eps15l1; NbExp=1; IntAct=EBI-443923, EBI-443931;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral
CC       membrane protein; Cytoplasmic side. Note=Recruited to the plasma
CC       membrane upon EGFR activation and localizes to coated pits.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Early endosome membrane;
CC       Peripheral membrane protein; Cytoplasmic side (By similarity).
CC       Note=Colocalizes with HGS on bilayered clathrin coats on endosomes
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P42567-1; Sequence=Displayed;
CC       Name=2; Synonyms=Eps15b;
CC         IsoId=P42567-2; Sequence=VSP_036170, VSP_036171;
CC   -!- DOMAIN: The EH domain interacts with Asn-Pro-Phe (NPF) motifs of
CC       target proteins (By similarity).
CC   -!- PTM: Phosphorylated on serine upon DNA damage, probably by ATM or
CC       ATR (By similarity). Phosphorylation on Tyr-850 is involved in the
CC       internalization of EGFR. Not required for membrane translocation
CC       after EGF treatment or for targeting to coated pits, but essential
CC       for a subsequent step in EGFR endocytosis.
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
CC   -!- SIMILARITY: Contains 3 EH domains.
CC   -!- SIMILARITY: Contains 2 UIM (ubiquitin-interacting motif) repeats.
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DR   EMBL; L21768; AAA02912.1; -; mRNA.
DR   EMBL; AK083176; BAC38796.1; -; mRNA.
DR   EMBL; AL669905; CAM13653.1; -; Genomic_DNA.
DR   IPI; IPI00117454; -.
DR   IPI; IPI00473528; -.
DR   PIR; A54696; A54696.
DR   RefSeq; NP_001153436.1; NM_001159964.1.
DR   RefSeq; NP_031969.1; NM_007943.3.
DR   UniGene; Mm.318250; -.
DR   PDB; 1KYF; X-ray; 1.22 A; P=627-632.
DR   PDB; 1KYU; X-ray; 1.80 A; P=627-632.
DR   PDB; 1QJT; NMR; -; A=7-105.
DR   PDBsum; 1KYF; -.
DR   PDBsum; 1KYU; -.
DR   PDBsum; 1QJT; -.
DR   ProteinModelPortal; P42567; -.
DR   SMR; P42567; 7-105, 121-215, 217-311, 344-376, 455-486.
DR   DIP; DIP-29052N; -.
DR   IntAct; P42567; 2.
DR   MINT; MINT-86610; -.
DR   STRING; P42567; -.
DR   PhosphoSite; P42567; -.
DR   PRIDE; P42567; -.
DR   Ensembl; ENSMUST00000102729; ENSMUSP00000099790; ENSMUSG00000028552.
DR   GeneID; 13858; -.
DR   KEGG; mmu:13858; -.
DR   UCSC; uc008ucf.1; mouse.
DR   CTD; 13858; -.
DR   MGI; MGI:104583; Eps15.
DR   HOGENOM; HBG714644; -.
DR   HOVERGEN; HBG005591; -.
DR   InParanoid; P42567; -.
DR   OMA; WALCDTK; -.
DR   OrthoDB; EOG4BRWKB; -.
DR   PhylomeDB; P42567; -.
DR   NextBio; 284734; -.
DR   ArrayExpress; P42567; -.
DR   Bgee; P42567; -.
DR   Genevestigator; P42567; -.
DR   GermOnline; ENSMUSG00000028552; Mus musculus.
DR   GO; GO:0030122; C:AP-2 adaptor complex; IDA:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR000261; EPS15_homology.
DR   InterPro; IPR003903; Ubiquitin-int_motif.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 3.
DR   SMART; SM00054; EFh; 4.
DR   SMART; SM00027; EH; 3.
DR   SMART; SM00726; UIM; 2.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 4.
DR   PROSITE; PS50031; EH; 3.
DR   PROSITE; PS50330; UIM; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Cell membrane; Cytoplasm;
KW   Direct protein sequencing; Endosome; Membrane; Phosphoprotein;
KW   Protein transport; Repeat; SH3-binding; Transport.
FT   CHAIN         1    897       Epidermal growth factor receptor
FT                                substrate 15.
FT                                /FTId=PRO_0000146117.
FT   DOMAIN       15    104       EH 1.
FT   DOMAIN      128    216       EH 2.
FT   DOMAIN      160    195       EF-hand 1.
FT   DOMAIN      223    258       EF-hand 2.
FT   DOMAIN      224    314       EH 3.
FT   REPEAT      599    601       1.
FT   REPEAT      623    625       2.
FT   REPEAT      629    631       3.
FT   REPEAT      634    636       4.
FT   REPEAT      640    642       5.
FT   REPEAT      645    647       6.
FT   REPEAT      651    653       7.
FT   REPEAT      665    667       8.
FT   REPEAT      673    675       9.
FT   REPEAT      693    695       10.
FT   REPEAT      711    713       11.
FT   REPEAT      806    808       12.
FT   REPEAT      827    829       13.
FT   REPEAT      852    871       UIM 1.
FT   REPEAT      878    897       UIM 2.
FT   CA_BIND     173    184       1 (Potential).
FT   CA_BIND     236    247       2 (Potential).
FT   REGION      599    829       13 X 3 AA repeats of D-P-F.
FT   MOD_RES     106    106       Phosphoserine.
FT   MOD_RES     108    108       Phosphoserine (By similarity).
FT   MOD_RES     140    140       Phosphoserine (By similarity).
FT   MOD_RES     323    323       Phosphoserine (By similarity).
FT   MOD_RES     324    324       Phosphoserine.
FT   MOD_RES     485    485       Phosphoserine (By similarity).
FT   MOD_RES     561    561       Phosphoserine.
FT   MOD_RES     562    562       Phosphoserine.
FT   MOD_RES     779    779       Phosphothreonine.
FT   MOD_RES     781    781       Phosphothreonine.
FT   MOD_RES     798    798       Phosphoserine (By similarity).
FT   MOD_RES     816    816       Phosphoserine.
FT   MOD_RES     850    850       Phosphotyrosine; by EGFR.
FT   VAR_SEQ       1    314       Missing (in isoform 2).
FT                                /FTId=VSP_036170.
FT   VAR_SEQ     315    346       SLQKNITGSSPVADFSAIKELDTLNNEIVDLQ -> MYSDS
FT                                GLGGWIAIPAVADVLRYSCIVCWSS (in isoform 2).
FT                                /FTId=VSP_036171.
FT   MUTAGEN     850    850       Y->F: Inefficient EGFR internalization.
FT   HELIX         9     12
FT   TURN         13     15
FT   HELIX        18     26
FT   HELIX        37     44
FT   STRAND       46     48
FT   HELIX        50     60
FT   STRAND       63     67
FT   HELIX        71     83
FT   TURN         84     86
FT   HELIX        91     93
SQ   SEQUENCE   897 AA;  98471 MW;  08A0C0D423F873C2 CRC64;
     MAAAAQLSLT QLSSGNPVYE KYYRQVEAGN TGRVLALDAA AFLKKSGLPD LILGKIWDLA
     DTDGKGVLSK QEFFVALRLV ACAQNGLEVS LSSLSLAVPP PRFHDSSSPL LTSGPSVAEL
     PWAVKSEDKA KYDAIFDSLS PVDGFLSGDK VKPVLLNSKL PVEILGRVWE LSDIDHDGKL
     DRDEFAVAMF LVYCALEKEP VPMSLPPALV PPSKRKTWVV SPAEKAKYDE IFLKTDKDMD
     GYVSGLEVRE TFLKTGLPSA LLAHIWSLCD TKGCGKLSKD QFALAFHLIN QKLIKGIDPP
     HSLTPEMIPP SDRSSLQKNI TGSSPVADFS AIKELDTLNN EIVDLQREKN NVEQDLKEKE
     DTVKQRTSEV QDLQDEVQRE SINLQKLQAQ KQQVQELLGE LDEQKAQLEE QLQEVRKKCA
     EEAQLISSLK AEITSQESQI SSYEEELLKA REELSRLQQE TAQLEESVES GKAQLEPLQQ
     HLQESQQEIS SMQMRLEMKD LETDNNQSNW SSSPQSVLVN GATDYCSLST SSSETANFNE
     HAEGQNNLES EPTHQESSVR SSPEIAPSDV TDESEAVTVA GNEKVTPRFD DDKHSKEEDP
     FNVESSSLTD AVADTNLDFF QSDPFVGSDP FKDDPFGKID PFGGDPFKGS DPFASDCFFK
     QTSTDPFTTS STDPFSASSN SSNTSVETWK HNDPFAPGGT VVAAASDSAT DPFASVFGNE
     SFGDGFADFS TLSKVNNEDA FNPTISSSTS SVTIAKPMLE ETASKSEDVP PALPPKVGTP
     TRPCPPPPGK RPINKLDSSD PLKLNDPFQP FPGNDSPKEK DPDMFCDPFT SSTTTNKEAD
     PSNFANFSAY PSEEDMIEWA KRESEREEEQ RLARLNQQEQ EDLELAIALS KSEISEA
//
ID   PURA_MOUSE              Reviewed;         321 AA.
AC   P42669;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Transcriptional activator protein Pur-alpha;
DE   AltName: Full=Purine-rich single-stranded DNA-binding protein alpha;
GN   Name=Pura;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=95047494; PubMed=7959008; DOI=10.1016/0378-1119(94)90167-8;
RA   Ma Z.-W., Bergemann A.D., Johnson E.M.;
RT   "Conservation in human and mouse Pur alpha of a motif common to
RT   several proteins involved in initiation of DNA replication.";
RL   Gene 149:311-314(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X CBA; TISSUE=Lung;
RX   MEDLINE=97476282; PubMed=9334258; DOI=10.1074/jbc.272.42.26727;
RA   Kelm R.J. Jr., Elder P.K., Strauch A.R., Getz M.J.;
RT   "Sequence of cDNAs encoding components of vascular actin single-
RT   stranded DNA-binding factor 2 establish identity to Puralpha and
RT   Purbeta.";
RL   J. Biol. Chem. 272:26727-26733(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 176-198 AND 204-228, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   SUBUNIT.
RX   PubMed=10318844; DOI=10.1074/jbc.274.20.14238;
RA   Kelm R.J. Jr., Cogan J.G., Elder P.K., Strauch A.R., Getz M.J.;
RT   "Molecular interactions between single-stranded DNA-binding proteins
RT   associated with an essential MCAT element in the mouse smooth muscle
RT   alpha-actin promoter.";
RL   J. Biol. Chem. 274:14238-14245(1999).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-252, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: This is a probable transcription activator that
CC       specifically binds the purine-rich single strand of the PUR
CC       element located upstream of the c-Myc gene. May play a role in the
CC       initiation of DNA replication and in recombination.
CC   -!- SUBUNIT: Homodimer, heterodimer with PURB and heterotrimer with
CC       PURB and YBX1/Y-box protein 1.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the PUR DNA-binding protein family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U02098; AAA64630.1; -; mRNA.
DR   EMBL; AF017631; AAB71860.1; -; mRNA.
DR   IPI; IPI00118447; -.
DR   RefSeq; NP_033015.1; NM_008989.3.
DR   UniGene; Mm.231802; -.
DR   ProteinModelPortal; P42669; -.
DR   SMR; P42669; 57-277.
DR   STRING; P42669; -.
DR   PhosphoSite; P42669; -.
DR   UCD-2DPAGE; P42669; -.
DR   PRIDE; P42669; -.
DR   Ensembl; ENSMUST00000051301; ENSMUSP00000059404; ENSMUSG00000043991.
DR   GeneID; 19290; -.
DR   KEGG; mmu:19290; -.
DR   UCSC; uc008enh.1; mouse.
DR   CTD; 19290; -.
DR   MGI; MGI:103079; Pura.
DR   eggNOG; roNOG10448; -.
DR   HOGENOM; HBG383187; -.
DR   HOVERGEN; HBG006888; -.
DR   InParanoid; P42669; -.
DR   OMA; MSTAAEF; -.
DR   OrthoDB; EOG4PRSRB; -.
DR   PhylomeDB; P42669; -.
DR   NextBio; 459411; -.
DR   ArrayExpress; P42669; -.
DR   Bgee; P42669; -.
DR   CleanEx; MM_PURA; -.
DR   Genevestigator; P42669; -.
DR   GermOnline; ENSMUSG00000043991; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0005662; C:DNA replication factor A complex; IDA:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0003697; F:single-stranded DNA binding; IDA:UniProtKB.
DR   GO; GO:0046332; F:SMAD binding; IDA:MGI.
DR   GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0006915; P:apoptosis; NAS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; NAS:UniProtKB.
DR   GO; GO:0008283; P:cell proliferation; NAS:UniProtKB.
DR   GO; GO:0031575; P:mitotic cell cycle G1/S transition checkpoint; NAS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:MGI.
DR   GO; GO:0007399; P:nervous system development; IMP:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
DR   InterPro; IPR006628; PUR_DNA_RNA-bd.
DR   PANTHER; PTHR12611; PUR_DNA_RNA_bd; 1.
DR   Pfam; PF04845; PurA; 1.
DR   SMART; SM00712; PUR; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Direct protein sequencing; DNA-binding;
KW   Nucleus; Phosphoprotein; Transcription; Transcription regulation.
FT   CHAIN         1    321       Transcriptional activator protein Pur-
FT                                alpha.
FT                                /FTId=PRO_0000097108.
FT   COMPBIAS     11     52       Gly-rich.
FT   COMPBIAS    292    321       Gln/Glu-rich (part of the transcriptional
FT                                activation domain).
FT   MOD_RES       6      6       Phosphoserine (By similarity).
FT   MOD_RES       8      8       Phosphoserine (By similarity).
FT   MOD_RES     181    181       Phosphoserine (By similarity).
FT   MOD_RES     252    252       Phosphotyrosine.
FT   MOD_RES     272    272       N6-acetyllysine (By similarity).
SQ   SEQUENCE   321 AA;  34884 MW;  0379DBD96D47DCEA CRC64;
     MADRDSGSEQ GGAALGSGGS LGHPGSGSGS GGGGGGGGGG GGSGGGGGAP GGLQHETQEL
     ASKRVDIQNK RFYLDVKQNA KGRFLKIAEV GAGGNKSRLT LSMSVAVEFR DYLGDFIEHY
     AQLGPSQPPD LAQAQDEPRR ALKSEFLVRE NRKYYMDLKE NQRGRFLRIR QTVNRGPGLG
     STQGQTIALP AQGLIEFRDA LAKLIDDYGV EEEPAELPEG TSLTVDNKRF FFDVGSNKYG
     VFMRVSEVKP TYRNSITVPY KVWAKFGHTF CKYSEEMKKI QEKQREKRAA CEQLHQQQQQ
     QQEETTAATL LLQGEEEGEE D
//
ID   LIFR_MOUSE              Reviewed;        1092 AA.
AC   P42703; Q5I0Y2;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   08-MAR-2011, entry version 102.
DE   RecName: Full=Leukemia inhibitory factor receptor;
DE            Short=LIF receptor;
DE            Short=LIF-R;
DE   AltName: Full=D-factor/LIF receptor;
DE   AltName: CD_antigen=CD118;
DE   Flags: Precursor;
GN   Name=Lifr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   MEDLINE=92007727; PubMed=1915266;
RA   Gearing D.P., Thut C.J., Vanden Bos T., Gimpel S.D., Delaney P.B.,
RA   King J., Price V., Cosman D., Beckmann M.P.;
RT   "Leukemia inhibitory factor receptor is structurally related to the
RT   IL-6 signal transducer, gp130.";
RL   EMBO J. 10:2839-2848(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=ICR; TISSUE=Liver;
RX   MEDLINE=94039833; PubMed=7901054; DOI=10.1016/0014-5793(93)81710-H;
RA   Tomida M., Yamamoto-Yamaguchi Y., Hozumi M.;
RT   "Pregnancy associated increase in mRNA for soluble D-factor/LIF
RT   receptor in mouse liver.";
RL   FEBS Lett. 334:193-197(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX   MEDLINE=94334302; PubMed=8056772;
RA   Tomida M., Yamamoto-Yamaguchi Y., Hozumi M.;
RT   "Three different cDNAs encoding mouse D-factor/LIF receptor.";
RL   J. Biochem. 115:557-562(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-385; ASN-402 AND ASN-675,
RP   AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Plasma;
RX   PubMed=16944957; DOI=10.1021/pr060186m;
RA   Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
RA   Gevaert K.;
RT   "Proteome-wide characterization of N-glycosylation events by diagonal
RT   chromatography.";
RL   J. Proteome Res. 5:2438-2447(2006).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-385 AND ASN-658, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Plasma;
RX   PubMed=17330941; DOI=10.1021/pr0604559;
RA   Bernhard O.K., Kapp E.A., Simpson R.J.;
RT   "Enhanced analysis of the mouse plasma proteome using cysteine-
RT   containing tryptic glycopeptides.";
RL   J. Proteome Res. 6:987-995(2007).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-385, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 49-529 IN COMPLEX WITH HUMAN
RP   LIF, DISULFIDE BOND, AND GLYCOSYLATION AT ASN-164; ASN-199; ASN-238;
RP   ASN-261; ASN-385; ASN-402; ASN-421; ASN-440 AND ASN-453.
RX   PubMed=17652170; DOI=10.1073/pnas.0705577104;
RA   Huyton T., Zhang J.G., Luo C.S., Lou M.Z., Hilton D.J., Nicola N.A.,
RA   Garrett T.P.;
RT   "An unusual cytokine:Ig-domain interaction revealed in the crystal
RT   structure of leukemia inhibitory factor (LIF) in complex with the LIF
RT   receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12737-12742(2007).
CC   -!- FUNCTION: Signal-transducing molecule. May have a common pathway
CC       with IL6ST. The soluble form inhibits the biological activity of
CC       LIF by blocking its binding to receptors on target cells.
CC   -!- SUBUNIT: Heterodimer composed of LIFR and IL6ST. The heterodimer
CC       formed by LIFR and IL6ST interacts with the complex formed by CNTF
CC       and CNTFR (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
CC       membrane protein.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Membrane;
CC         IsoId=P42703-1; Sequence=Displayed;
CC       Name=2; Synonyms=Secreted;
CC         IsoId=P42703-2; Sequence=VSP_001686, VSP_001687;
CC   -!- TISSUE SPECIFICITY: Placenta, liver, kidney, heart, lung, brain,
CC       and embryos. The liver may be the primary site of synthesis of the
CC       secreted form.
CC   -!- DOMAIN: The WSXWS motif appears to be necessary for proper protein
CC       folding and thereby efficient intracellular transport and cell-
CC       surface receptor binding.
CC   -!- DOMAIN: The box 1 motif is required for JAK interaction and/or
CC       activation.
CC   -!- SIMILARITY: Belongs to the type I cytokine receptor family. Type 2
CC       subfamily.
CC   -!- SIMILARITY: Contains 6 fibronectin type-III domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; S73496; AAC60698.1; -; mRNA.
DR   EMBL; S73495; AAC60697.1; -; mRNA.
DR   EMBL; D26177; BAA05165.1; -; mRNA.
DR   EMBL; D17444; BAA04258.1; -; mRNA.
DR   EMBL; BC031929; AAH31929.1; -; mRNA.
DR   IPI; IPI00119299; -.
DR   IPI; IPI00407541; -.
DR   PIR; JX0312; JX0312.
DR   RefSeq; NP_001106857.1; NM_001113386.1.
DR   RefSeq; NP_038612.1; NM_013584.2.
DR   UniGene; Mm.149720; -.
DR   PDB; 2Q7N; X-ray; 4.00 A; A/C=50-529.
DR   PDBsum; 2Q7N; -.
DR   ProteinModelPortal; P42703; -.
DR   SMR; P42703; 50-620, 708-829.
DR   DIP; DIP-5772N; -.
DR   STRING; P42703; -.
DR   PhosphoSite; P42703; -.
DR   PRIDE; P42703; -.
DR   Ensembl; ENSMUST00000067190; ENSMUSP00000064551; ENSMUSG00000054263.
DR   GeneID; 16880; -.
DR   KEGG; mmu:16880; -.
DR   UCSC; uc007vdx.1; mouse.
DR   CTD; 16880; -.
DR   MGI; MGI:96788; Lifr.
DR   HOGENOM; HBG280994; -.
DR   HOVERGEN; HBG006266; -.
DR   InParanoid; P42703; -.
DR   OMA; WSFTNFF; -.
DR   OrthoDB; EOG4G7BXJ; -.
DR   PhylomeDB; P42703; -.
DR   NextBio; 290878; -.
DR   ArrayExpress; P42703; -.
DR   Bgee; P42703; -.
DR   CleanEx; MM_LIFR; -.
DR   Genevestigator; P42703; -.
DR   GermOnline; ENSMUSG00000054263; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IGI:MGI.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR003529; Hematopoietin_rcpt_gp130_CS.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 4.
DR   Pfam; PF00041; fn3; 1.
DR   SMART; SM00060; FN3; 5.
DR   SUPFAM; SSF49265; FN_III-like; 5.
DR   PROSITE; PS50853; FN3; 5.
DR   PROSITE; PS01353; HEMATOPO_REC_L_F2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW   Glycoprotein; Membrane; Phosphoprotein; Receptor; Repeat; Secreted;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     43       Potential.
FT   CHAIN        44   1092       Leukemia inhibitory factor receptor.
FT                                /FTId=PRO_0000010903.
FT   TOPO_DOM     44    828       Extracellular (Potential).
FT   TRANSMEM    829    853       Helical; (Potential).
FT   TOPO_DOM    854   1092       Cytoplasmic (Potential).
FT   DOMAIN       45    126       Fibronectin type-III 1.
FT   DOMAIN      327    423       Fibronectin type-III 2.
FT   DOMAIN      428    522       Fibronectin type-III 3.
FT   DOMAIN      530    620       Fibronectin type-III 4.
FT   DOMAIN      622    714       Fibronectin type-III 5.
FT   DOMAIN      719    824       Fibronectin type-III 6.
FT   MOTIF       514    518       WSXWS motif.
FT   MOTIF       864    872       Box 1 motif.
FT   MOD_RES     922    922       Phosphoserine (By similarity).
FT   CARBOHYD    164    164       N-linked (GlcNAc...).
FT   CARBOHYD    199    199       N-linked (GlcNAc...).
FT   CARBOHYD    238    238       N-linked (GlcNAc...).
FT   CARBOHYD    261    261       N-linked (GlcNAc...).
FT   CARBOHYD    385    385       N-linked (GlcNAc...).
FT   CARBOHYD    402    402       N-linked (GlcNAc...).
FT   CARBOHYD    421    421       N-linked (GlcNAc...).
FT   CARBOHYD    440    440       N-linked (GlcNAc...).
FT   CARBOHYD    453    453       N-linked (GlcNAc...).
FT   CARBOHYD    476    476       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    567    567       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    647    647       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    658    658       N-linked (GlcNAc...).
FT   CARBOHYD    675    675       N-linked (GlcNAc...).
FT   CARBOHYD    724    724       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    782    782       N-linked (GlcNAc...) (Potential).
FT   DISULFID     53     63
FT   DISULFID     80     88
FT   DISULFID    208    265
FT   DISULFID    336    346
FT   DISULFID    461    506
FT   VAR_SEQ     718    719       AP -> EA (in isoform 2).
FT                                /FTId=VSP_001686.
FT   VAR_SEQ     720   1092       Missing (in isoform 2).
FT                                /FTId=VSP_001687.
FT   STRAND       54     64
FT   STRAND       69     71
FT   STRAND       76     90
FT   STRAND       92     99
FT   STRAND      106    115
FT   STRAND      117    122
FT   STRAND      136    138
FT   TURN        143    146
FT   STRAND      147    152
FT   HELIX       156    158
FT   STRAND      161    170
FT   STRAND      174    177
FT   STRAND      190    192
FT   STRAND      197    201
FT   STRAND      207    209
FT   STRAND      212    219
FT   STRAND      255    259
FT   STRAND      263    266
FT   STRAND      272    277
FT   STRAND      288    290
FT   STRAND      292    295
FT   STRAND      307    315
FT   STRAND      317    325
FT   STRAND      335    348
FT   STRAND      363    368
FT   TURN        369    371
FT   STRAND      374    378
FT   STRAND      388    393
FT   STRAND      402    409
FT   STRAND      412    419
FT   HELIX       422    424
FT   STRAND      432    438
FT   STRAND      444    453
FT   STRAND      455    466
FT   STRAND      473    480
FT   STRAND      483    491
FT   STRAND      504    510
SQ   SEQUENCE   1092 AA;  122574 MW;  6F02BBC8E154DE70 CRC64;
     MAAYSWWRQP SWMVDNKRSR MTPNLPWLLS ALTLLHLTMH ANGLKRGVQD LKCTTNNMRV
     WDCTWPAPLG VSPGTVKDIC IKDRFHSCHP LETTNVKIPA LSPGDHEVTI NYLNGFQSKF
     TLNEKDVSLI PETPEILDLS ADFFTSSLLL KWNDRGSALP HPSNATWEIK VLQNPRTEPV
     ALVLLNTMLS GKDTVQHWNW TSDLPLQCAT HSVSIRWHID SPHFSGYKEW SDWSPLKNIS
     WIRNTETNVF PQDKVVLAGS NMTICCMSPT KVLSGQIGNT LRPLIHLYGQ TVAIHILNIP
     VSENSGTNII FITDDDVYGT VVFAGYPPDV PQKLSCETHD LKEIICSWNP GRITGLVGPR
     NTEYTLFESI SGKSAVFHRI EGLTNETYRL GVQMHPGQEI HNFTLTGRNP LGQAQSAVVI
     NVTERVAPHD PTSLKVKDIN STVVTFSWYL PGNFTKINLL CQIEICKANS KKEVRNATIR
     GAEDSTYHVA VDKLNPYTAY TFRVRCSSKT FWKWSRWSDE KRHLTTEATP SKGPDTWREW
     SSDGKNLIVY WKPLPINEAN GKILSYNVSC SLNEETQSVL EIFDPQHRAE IQLSKNDYII
     SVVARNSAGS SPPSKIASME IPNDDITVEQ AVGLGNRIFL TWRHDPNMTC DYVIKWCNSS
     RSEPCLLDWR KVPSNSTETV IESDQFQPGV RYNFYLYGCT NQGYQLLRSI IGYVEELAPI
     VAPNFTVEDT SADSILVKWD DIPVEELRGF LRGYLFYFQK GERDTPKTRS LEPHHSDIKL
     KNITDISQKT LRIADLQGKT SYHLVLRAYT HGGLGPEKSM FVVTKENSVG LIIAILIPVA
     VAVIVGVVTS ILCYRKREWI KETFYPDIPN PENCKALQFQ KSVCEGSNAL KTLEMNPCTP
     NNVEVLESRS IVPKIEDTEI ISPVAERPGE RSEVDPENHV VVSYCPPIIE EEITNPAADE
     VGGASQVVYI DVQSMYQPQA KAEEEQDVDP VVVAGYKPQM RLPISPAVED TAAEDEEGKT
     AGYRPQANVN TWNLVSPDSP RSTDSNNEVV SFGSPCSINS RQFLIPPKDE DSPKSNGGGW
     SFTNFFQNKP ND
//
ID   HD_MOUSE                Reviewed;        3119 AA.
AC   P42859;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Huntingtin;
DE   AltName: Full=Huntington disease protein homolog;
DE            Short=HD protein homolog;
GN   Name=Htt; Synonyms=Hd, Hdh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Spleen;
RX   MEDLINE=94214482; PubMed=8162057; DOI=10.1093/hmg/3.1.85;
RA   Lin B., Nasir J., Macdonald H., Hutchinson G., Graham R.K.,
RA   Rommens J.M., Hayden M.R.;
RT   "Sequence of the murine Huntington disease gene: evidence for
RT   conservation, alternate splicing and polymorphism in a triplet (CCG)
RT   repeat.";
RL   Hum. Mol. Genet. 3:85-92(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94278649; PubMed=8009370; DOI=10.1007/BF02290678;
RA   Barnes G.T., Duyao M.P., Ambrose C.M., McNeil S., Persichetti F.,
RA   Srinidhi J., Gusella J.F., Macdonald M.E.;
RT   "Mouse Huntington's disease gene homolog (Hdh).";
RL   Somat. Cell Mol. Genet. 20:87-97(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=95375771; PubMed=7647777; DOI=10.1038/ng0595-104;
RA   Trottier Y., Devys D., Imbert G., Saudou F., An I., Lutz Y., Weber C.,
RA   Agid Y., Hirsch E.C., Mandel J.-L.;
RT   "Cellular localization of the Huntington's disease protein and
RT   discrimination of the normal and mutated form.";
RL   Nat. Genet. 10:104-110(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-181.
RX   MEDLINE=95278941; PubMed=7759106; DOI=10.1016/0888-7543(95)80014-D;
RA   Lin B., Nasir J., Kalchman M.A., McDonald H., Zeisler J.,
RA   Goldberg Y.P., Hayden M.R.;
RT   "Structural analysis of the 5' region of mouse and human Huntington
RT   disease genes reveals conservation of putative promoter region and di-
RT   and trinucleotide polymorphisms.";
RL   Genomics 25:707-715(1995).
RN   [5]
RP   INTERACTION WITH SH3GLB1.
RX   PubMed=12456676; DOI=10.1074/jbc.M208568200;
RA   Modregger J., Schmidt A.A., Ritter B., Huttner W.B., Plomann M.;
RT   "Characterization of endophilin B1b, a brain-specific membrane-
RT   associated lysophosphatidic acid acyl transferase with properties
RT   distinct from endophilin A1.";
RL   J. Biol. Chem. 278:4160-4167(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1853, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May play a role in microtubule-mediated transport or
CC       vesicle function.
CC   -!- SUBUNIT: Interacts with PQBP1 and SETD2 (By similarity). Binds
CC       SH3GLB1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=P42859-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=P42859-2; Sequence=VSP_004282;
CC         Note=Cannot be explained by a simple splicing event;
CC   -!- TISSUE SPECIFICITY: The highest level is seen throughout the
CC       brain, but it is also found in the stomach, heart, testis, adipose
CC       tissue, muscle, spleen, liver, and kidney.
CC   -!- DEVELOPMENTAL STAGE: Predominant expression in neuronal tissues at
CC       all developmental stages. In 14.5 day old embryos, it is also
CC       detected in non-neuronal tissues. This expression is down-
CC       regulated in later stages of development.
CC   -!- DOMAIN: The N-terminal Gln-rich and Pro-rich domain has great
CC       conformational flexibility and is likely to exist in a fluctuating
CC       equilibrium of alpha-helical, random coil, and extended
CC       conformations (By similarity).
CC   -!- POLYMORPHISM: The first poly-Pro repeat stretch differs in length
CC       by one unit (three) in Mus spretus strain compared to other
CC       strains (four). The poly-Gln region does not appear to be
CC       polymorphic, explaining the absence of a murine HD-like disorder.
CC   -!- SIMILARITY: Belongs to the huntingtin family.
CC   -!- SIMILARITY: Contains 10 HEAT repeats.
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DR   EMBL; L23312; AAA37799.1; -; mRNA.
DR   EMBL; L23313; AAA37800.1; -; mRNA.
DR   EMBL; L28827; AAA89100.1; ALT_SEQ; mRNA.
DR   EMBL; U24233; AAC52218.1; -; mRNA.
DR   EMBL; L34024; AAA91085.1; -; Genomic_DNA.
DR   EMBL; L34008; AAA91085.1; JOINED; Genomic_DNA.
DR   EMBL; L34021; AAA91085.1; JOINED; Genomic_DNA.
DR   EMBL; L34022; AAA91085.1; JOINED; Genomic_DNA.
DR   EMBL; L34023; AAA91085.1; JOINED; Genomic_DNA.
DR   IPI; IPI00271166; -.
DR   IPI; IPI00623970; -.
DR   PIR; I49729; I49729.
DR   UniGene; Mm.209071; -.
DR   ProteinModelPortal; P42859; -.
DR   MINT; MINT-270833; -.
DR   STRING; P42859; -.
DR   PhosphoSite; P42859; -.
DR   PRIDE; P42859; -.
DR   Ensembl; ENSMUST00000080036; ENSMUSP00000078945; ENSMUSG00000029104.
DR   Ensembl; ENSMUST00000114300; ENSMUSP00000109939; ENSMUSG00000029104.
DR   KEGG; mmu:15194; -.
DR   UCSC; uc008xdc.1; mouse.
DR   CTD; 15194; -.
DR   MGI; MGI:96067; Htt.
DR   eggNOG; roNOG07647; -.
DR   GeneTree; ENSGT00390000015863; -.
DR   HOGENOM; HBG356385; -.
DR   HOVERGEN; HBG005953; -.
DR   InParanoid; P42859; -.
DR   OrthoDB; EOG4RNB7G; -.
DR   NextBio; 287727; -.
DR   ArrayExpress; P42859; -.
DR   Bgee; P42859; -.
DR   CleanEx; MM_HTT; -.
DR   Genevestigator; P42859; -.
DR   GermOnline; ENSMUSG00000029104; Mus musculus.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:MGI.
DR   GO; GO:0016234; C:inclusion body; IDA:MGI.
DR   GO; GO:0005625; C:soluble fraction; IDA:MGI.
DR   GO; GO:0050809; F:diazepam binding; IMP:MGI.
DR   GO; GO:0008134; F:transcription factor binding; IPI:MGI.
DR   GO; GO:0009952; P:anterior/posterior pattern formation; IMP:MGI.
DR   GO; GO:0006916; P:anti-apoptosis; IDA:MGI.
DR   GO; GO:0008088; P:axon cargo transport; IMP:MGI.
DR   GO; GO:0007569; P:cell aging; IMP:MGI.
DR   GO; GO:0000052; P:citrulline metabolic process; IMP:MGI.
DR   GO; GO:0008340; P:determination of adult lifespan; IMP:MGI.
DR   GO; GO:0007212; P:dopamine receptor signaling pathway; IMP:MGI.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; IMP:MGI.
DR   GO; GO:0016197; P:endosome transport; IMP:MGI.
DR   GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IMP:MGI.
DR   GO; GO:0042445; P:hormone metabolic process; IMP:MGI.
DR   GO; GO:0030073; P:insulin secretion; IMP:MGI.
DR   GO; GO:0055072; P:iron ion homeostasis; IMP:MGI.
DR   GO; GO:0051938; P:L-glutamate import; IMP:MGI.
DR   GO; GO:0019244; P:lactate biosynthetic process from pyruvate; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptosis; IMP:MGI.
DR   GO; GO:0021990; P:neural plate formation; IMP:MGI.
DR   GO; GO:0051402; P:neuron apoptosis; IMP:MGI.
DR   GO; GO:0048666; P:neuron development; IMP:MGI.
DR   GO; GO:0021988; P:olfactory lobe development; IMP:MGI.
DR   GO; GO:0048341; P:paraxial mesoderm formation; IMP:MGI.
DR   GO; GO:0006606; P:protein import into nucleus; IMP:MGI.
DR   GO; GO:0019805; P:quinolinate biosynthetic process; IMP:MGI.
DR   GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IMP:MGI.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; IMP:MGI.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR   GO; GO:0051592; P:response to calcium ion; IMP:MGI.
DR   GO; GO:0035176; P:social behavior; IMP:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   GO; GO:0021756; P:striatum development; IMP:MGI.
DR   GO; GO:0000050; P:urea cycle; IMP:MGI.
DR   GO; GO:0047496; P:vesicle transport along microtubule; IDA:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000091; Huntingtin.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 3.
DR   PANTHER; PTHR10170; Huntingtin; 1.
DR   PRINTS; PR00375; HUNTINGTIN.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW   Polymorphism; Repeat.
FT   CHAIN         1   3119       Huntingtin.
FT                                /FTId=PRO_0000083943.
FT   REPEAT      183    220       HEAT 1.
FT   REPEAT      225    262       HEAT 2.
FT   REPEAT      782    819       HEAT 3.
FT   REPEAT      882    920       HEAT 4.
FT   REPEAT     1404   1441       HEAT 5.
FT   MOTIF      2372   2381       Nuclear export signal (By similarity).
FT   COMPBIAS     18     24       Poly-Gln.
FT   COMPBIAS     25     45       Poly-Pro.
FT   COMPBIAS     49     59       Poly-Pro.
FT   COMPBIAS   1417   1420       Poly-Thr.
FT   COMPBIAS   1696   1699       Poly-Gly.
FT   COMPBIAS   2615   2620       Poly-Glu.
FT   MOD_RES     398    398       Phosphoserine.
FT   MOD_RES     411    411       Phosphoserine (By similarity).
FT   MOD_RES    1159   1159       Phosphoserine (By similarity).
FT   MOD_RES    1179   1179       Phosphoserine (By similarity).
FT   MOD_RES    1853   1853       Phosphoserine.
FT   VAR_SEQ    1522   2001       Missing (in isoform Short).
FT                                /FTId=VSP_004282.
FT   CONFLICT      2      2       A -> G (in Ref. 1; AAA37799/AAA37800 and
FT                                4; AAA91085).
FT   CONFLICT     29     29       A -> P (in Ref. 2; AAA89100).
FT   CONFLICT    116    116       N -> D (in Ref. 2; AAA89100 and 4;
FT                                AAA91085).
FT   CONFLICT    138    138       M -> L (in Ref. 1; AAA37799/AAA37800).
FT   CONFLICT    521    521       S -> P (in Ref. 1; AAA37799/AAA37800).
FT   CONFLICT    524    524       A -> P (in Ref. 1; AAA37799/AAA37800).
FT   CONFLICT    533    533       A -> P (in Ref. 1; AAA37799/AAA37800).
FT   CONFLICT    607    607       A -> T (in Ref. 1; AAA37799/AAA37800).
FT   CONFLICT    769    769       D -> E (in Ref. 2; AAA89100).
FT   CONFLICT    972    972       S -> R (in Ref. 1; AAA37799/AAA37800).
FT   CONFLICT   1106   1106       W -> C (in Ref. 1; AAA37799/AAA37800).
FT   CONFLICT   1240   1240       T -> N (in Ref. 1; AAA37799/AAA37800).
FT   CONFLICT   1384   1384       N -> T (in Ref. 1; AAA37799/AAA37800).
FT   CONFLICT   1827   1827       H -> Y (in Ref. 1; AAA37799).
FT   CONFLICT   1979   1980       PF -> SS (in Ref. 1; AAA37799).
FT   CONFLICT   2062   2062       D -> G (in Ref. 1; AAA37799/AAA37800).
FT   CONFLICT   2570   2570       S -> N (in Ref. 1; AAA37799/AAA37800).
FT   CONFLICT   2866   2866       E -> V (in Ref. 1; AAA37799/AAA37800).
FT   CONFLICT   2877   2877       V -> G (in Ref. 1; AAA37799/AAA37800).
FT   CONFLICT   2882   2882       D -> G (in Ref. 1; AAA37799/AAA37800).
FT   CONFLICT   2887   2887       Q -> H (in Ref. 1; AAA37799/AAA37800).
FT   CONFLICT   2915   2915       A -> T (in Ref. 1; AAA37799/AAA37800).
FT   CONFLICT   3025   3025       P -> S (in Ref. 3; AAC52218).
FT   CONFLICT   3062   3063       QV -> LM (in Ref. 1; AAA37799/AAA37800).
FT   CONFLICT   3095   3096       VV -> EE (in Ref. 1; AAA37799/AAA37800).
SQ   SEQUENCE   3119 AA;  344690 MW;  ECA42B5916F50F4F CRC64;
     MATLEKLMKA FESLKSFQQQ QQQQPPPQAP PPPPPPPPQP PQPPPQGQPP PPPPPLPGPA
     EEPLHRPKKE LSATKKDRVN HCLTICENIV AQSLRNSPEF QKLLGIAMEL FLLCSNDAES
     DVRMVADECL NKVIKALMDS NLPRLQLELY KEIKKNGAPR SLRAALWRFA ELAHLVRPQK
     CRPYLVNLLP CLTRTSKRPE ESVQETLAAA VPKIMASFGN FANDNEIKVL LKAFIANLKS
     SSPTVRRTAA GSAVSICQHS RRTQYFYNWL LNVLLGLLVP MEEEHSTLLI LGVLLTLRCL
     VPLLQQQVKD TSLKGSFGVT RKEMEVSPST EQLVQVYELT LHHTQHQDHN VVTGALELLQ
     QLFRTPPPEL LQALTTPGGL GQLTLVQEEA RGRGRSGSIV ELLAGGGSSC SPVLSRKQKG
     KVLLGEEEAL EDDSESRSDV SSSAFAASVK SEIGGELAAS SGVSTPGSVG HDIITEQPRS
     QHTLQADSVD LSGCDLTSAA TDGDEEDILS HSSSQFSAVP SDPAMDLNDG TQASSPISDS
     SQTTTEGPDS AVTPSDSSEI VLDGADSQYL GMQIGQPQED DEEGAAGVLS GEVSDVFRNS
     SLALQQAHLL ERMGHSRQPS DSSIDKYVTR DEVAEASDPE SKPCRIKGDI GQPNDDDSAP
     LVHCVRLLSA SFLLTGEKKA LVPDRDVRVS VKALALSCIG AAVALHPESF FSRLYKVPLN
     TTESTEEQYV SDILNYIDHG DPQVRGATAI LCGTLVYSIL SRSRLRVGDW LGNIRTLTGN
     TFSLVDCIPL LQKTLKDESS VTCKLACTAV RHCVLSLCSS SYSDLGLQLL IDMLPLKNSS
     YWLVRTELLD TLAEIDFRLV SFLEAKAESL HRGAHHYTGF LKLQERVLNN VVIYLLGDED
     PRVRHVAATS LTRLVPKLFY KCDQGQADPV VAVARDQSSV YLKLLMHETQ PPSHFSVSTI
     TRIYRGYSLL PSITDVTMEN NLSRVVAAVS HELITSTTRA LTFGCCEALC LLSAAFPVCT
     WSLGWHCGVP PLSASDESRK SCTVGMASMI LTLLSSAWFP LDLSAHQDAL ILAGNLLAAS
     APKSLRSSWT SEEEANSAAT RQEEIWPALG DRTLVPLVEQ LFSHLLKVIN ICAHVLDDVT
     PGPAIKAALP SLTNPPSLSP IRRKGKEKEP GEQASTPMSP KKVGEASAAS RQSDTSGPVT
     ASKSSSLGSF YHLPSYLKLH DVLKATHANY KVTLDLQNST EKFGGFLRSA LDVLSQILEL
     ATLQDIGKCV EEVLGYLKSC FSREPMMATV CVQQLLKTLF GTNLASQFDG LSSNPSKSQC
     RAQRLGSSSV RPGLYHYCFM APYTHFTQAL ADASLRNMVQ AEQERDASGW FDVLQKVSAQ
     LKTNLTSVTK NRADKNAIHN HIRLFEPLVI KALKQYTTTT SVQLQKQVLD LLAQLVQLRV
     NYCLLDSDQV FIGFVLKQFE YIEVGQFRES EAIIPNIFFF LVLLSYERYH SKQIIGIPKI
     IQLCDGIMAS GRKAVTHAIP ALQPIVHDLF VLRGTNKADA GKELETQKEV VVSMLLRLIQ
     YHQVLEMFIL VLQQCHKENE DKWKRLSRQV ADIILPMLAK QQMHIDSHEA LGVLNTLFEI
     LAPSSLRPVD MLLRSMFITP STMASVSTVQ LWISGILAIL RVLISQSTED IVLCRIQELS
     FSPHLLSCPV INRLRGGGGN VTLGECSEGK QKSLPEDTFS RFLLQLVGIL LEDIVTKQLK
     VDMSEQQHTF YCQELGTLLM CLIHIFKSGM FRRITAAATR LFTSDGCEGS FYTLESLNAR
     VRSMVPTHPA LVLLWCQILL LINHTDHRWW AEVQQTPKRH SLSCTKSLNP QKSGEEEDSG
     SAAQLGMCNR EIVRRGALIL FCDYVCQNLH DSEHLTWLIV NHIQDLISLS HEPPVQDFIS
     AIHRNSAASG LFIQAIQSRC ENLSTPTTLK KTLQCLEGIH LSQSGAVLTL YVDRLLGTPF
     RALARMVDTL ACRRVEMLLA ANLQSSMAQL PEEELNRIQE HLQNSGLAQR HQRLYSLLDR
     FRLSTVQDSL SPLPPVTSHP LDGDGHTSLE TVSPDKDWYL QLVRSQCWTR SDSALLEGAE
     LVNRIPAEDM NDFMMSSEFN LSLLAPCLSL GMSEIANGQK SPLFEAARGV ILNRVTSVVQ
     QLPAVHQVFQ PFLPIEPTAY WNKLNDLLGD TTSYQSLTIL ARALAQYLVV LSKVPAHLHL
     PPEKEGDTVK FVVMTVEALS WHLIHEQIPL SLDLQAGLDC CCLALQVPGL WGVLSSPEYV
     THACSLIHCV RFILEAIAVQ PGDQLLGPES RSHTPRAVRK EEVDSDIQNL SHVTSACEMV
     ADMVESLQSV LALGHKRNST LPSFLTAVLK NIVISLARLP LVNSYTRVPP LVWKLGWSPK
     PGGDFGTVFP EIPVEFLQEK EILKEFIYRI NTLGWTNRTQ FEETWATLLG VLVTQPLVME
     QEESPPEEDT ERTQIHVLAV QAITSLVLSA MTVPVAGNPA VSCLEQQPRN KPLKALDTRF
     GRKLSMIRGI VEQEIQEMVS QRENTATHHS HQAWDPVPSL LPATTGALIS HDKLLLQINP
     EREPGNMSYK LGQVSIHSVW LGNNITPLRE EEWDEEEEEE SDVPAPTSPP VSPVNSRKHR
     AGVDIHSCSQ FLLELYSRWI LPSSAARRTP VILISEVVRS LLVVSDLFTE RTQFEMMYLT
     LTELRRVHPS EDEILIQYLV PATCKAAAVL GMDKTVAEPV SRLLESTLRS SHLPSQIGAL
     HGILYVLECD LLDDTAKQLI PVVSDYLLSN LKGIAHCVNI HSQQHVLVMC ATAFYLMENY
     PLDVGPEFSA SVIQMCGVML SGSEESTPSI IYHCALRGLE RLLLSEQLSR LDTESLVKLS
     VDRVNVQSPH RAMAALGLML TCMYTGKEKA SPGRASDPSP ATPDSESVIV AMERVSVLFD
     RIRKGFPCEA RVVARILPQF LDDFFPPQDV MNKVIGEFLS NQQPYPQFMA TVVYKVFQTL
     HSAGQSSMVR DWVMLSLSNF TQRTPVAMAM WSLSCFLVSA STSPWVSAIL PHVISRMGKL
     EQVDVNLFCL VATDFYRHQI EEEFDRRAFQ SVFEVVAAPG SPYHRLLACL QNVHKVTTC
//
ID   EAA2_MOUSE              Reviewed;         572 AA.
AC   P43006; O35877; O54686; O54687;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Excitatory amino acid transporter 2;
DE   AltName: Full=GLT-1;
DE   AltName: Full=Sodium-dependent glutamate/aspartate transporter 2;
DE   AltName: Full=Solute carrier family 1 member 2;
GN   Name=Slc1a2; Synonyms=Eaat2, Glt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=95213010; PubMed=7698742; DOI=10.1006/geno.1994.1609;
RA   Kirschner M.A., Copeland N.G., Gilbert D.J., Jenkins N.A., Amara S.G.;
RT   "Mouse excitatory amino acid transporter EAAT2: isolation,
RT   characterization, and proximity to neuroexcitability loci on mouse
RT   chromosome 2.";
RL   Genomics 24:218-224(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=JCL:ICR; TISSUE=Cerebellum;
RX   MEDLINE=95284091; PubMed=7766664; DOI=10.1016/0304-4165(95)00062-G;
RA   Mukainaka Y., Tanaka K., Hagiwara T., Wada K.;
RT   "Molecular cloning of two glutamate transporter subtypes from mouse
RT   brain.";
RL   Biochim. Biophys. Acta 1244:233-237(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=96032356; PubMed=7557442; DOI=10.1016/0378-1119(95)00293-F;
RA   Sutherland M.L., Delaney T.A., Noebels J.L.;
RT   "Molecular characterization of a high-affinity mouse glutamate
RT   transporter.";
RL   Gene 162:271-274(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Peng J.-B., Guo L.-H.;
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=JCL:ICR; TISSUE=Brain, and Liver;
RX   MEDLINE=98039013; PubMed=9373176; DOI=10.1016/S0014-5793(97)01232-5;
RA   Utsunomiya-Tate N., Endou H., Kanai Y.;
RT   "Tissue specific variants of glutamate transporter GLT-1.";
RL   FEBS Lett. 416:312-316(1997).
RN   [6]
RP   PROTEIN SEQUENCE OF 66-87; 159-173 AND 478-525, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-493 AND TYR-537, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Transports L-glutamate and also L- and D-aspartate.
CC       Essential for terminating the postsynaptic action of glutamate by
CC       rapidly removing released glutamate from the synaptic cleft. Acts
CC       as a symport by cotransporting sodium.
CC   -!- SUBUNIT: Homotrimer (By similarity). Interacts with JUB (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=Glt-1;
CC         IsoId=P43006-1; Sequence=Displayed;
CC       Name=Glt-1A;
CC         IsoId=P43006-2; Sequence=VSP_006264;
CC       Name=Glt-1B;
CC         IsoId=P43006-3; Sequence=VSP_006264, VSP_006265;
CC   -!- TISSUE SPECIFICITY: Isoform GLT1 is expressed in the brain.
CC       Isoforms GLT-1A and GLT-1B are expressed in the liver.
CC   -!- PTM: Glycosylated.
CC   -!- SIMILARITY: Belongs to the sodium:dicarboxylate (SDF) symporter
CC       (TC 2.A.23) family. SLC1A2 subfamily.
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DR   EMBL; U11763; AAA77673.1; -; mRNA.
DR   EMBL; D43796; BAA07854.1; -; mRNA.
DR   EMBL; U24699; AAA91643.1; -; mRNA.
DR   EMBL; U75372; AAB71737.1; -; mRNA.
DR   EMBL; U75373; AAB71738.1; -; mRNA.
DR   EMBL; AB007810; BAA23770.1; -; mRNA.
DR   EMBL; AB007811; BAA23771.1; -; mRNA.
DR   EMBL; AB007812; BAA23772.1; -; mRNA.
DR   IPI; IPI00230289; -.
DR   IPI; IPI00230290; -.
DR   IPI; IPI00470184; -.
DR   PIR; A55676; A55676.
DR   PIR; JC4262; JC4262.
DR   RefSeq; NP_001070982.1; NM_001077514.3.
DR   RefSeq; NP_001070983.1; NM_001077515.2.
DR   RefSeq; NP_035523.1; NM_011393.2.
DR   UniGene; Mm.267547; -.
DR   UniGene; Mm.371582; -.
DR   ProteinModelPortal; P43006; -.
DR   SMR; P43006; 46-494.
DR   STRING; P43006; -.
DR   PhosphoSite; P43006; -.
DR   PRIDE; P43006; -.
DR   Ensembl; ENSMUST00000080210; ENSMUSP00000079100; ENSMUSG00000005089.
DR   GeneID; 20511; -.
DR   KEGG; mmu:20511; -.
DR   UCSC; uc008lhz.1; mouse.
DR   UCSC; uc008lia.1; mouse.
DR   UCSC; uc008lib.1; mouse.
DR   CTD; 20511; -.
DR   MGI; MGI:101931; Slc1a2.
DR   HOVERGEN; HBG000080; -.
DR   OrthoDB; EOG4P8FHT; -.
DR   PhylomeDB; P43006; -.
DR   NextBio; 298703; -.
DR   ArrayExpress; P43006; -.
DR   Bgee; P43006; -.
DR   Genevestigator; P43006; -.
DR   GermOnline; ENSMUSG00000005089; Mus musculus.
DR   GO; GO:0030673; C:axolemma; IDA:MGI.
DR   GO; GO:0005887; C:integral to plasma membrane; IC:MGI.
DR   GO; GO:0015501; F:glutamate:sodium symporter activity; IDA:MGI.
DR   GO; GO:0017153; F:sodium:dicarboxylate symporter activity; IEA:InterPro.
DR   GO; GO:0030534; P:adult behavior; IMP:MGI.
DR   GO; GO:0031668; P:cellular response to extracellular stimulus; IMP:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR   GO; GO:0010259; P:multicellular organismal aging; IMP:MGI.
DR   GO; GO:0046326; P:positive regulation of glucose import; IMP:MGI.
DR   GO; GO:0043200; P:response to amino acid stimulus; IMP:MGI.
DR   GO; GO:0042493; P:response to drug; IMP:MGI.
DR   GO; GO:0009611; P:response to wounding; IMP:MGI.
DR   GO; GO:0021537; P:telencephalon development; IMP:MGI.
DR   GO; GO:0007632; P:visual behavior; IMP:MGI.
DR   InterPro; IPR001991; Na-dicarboxylate_symporter.
DR   InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR   PANTHER; PTHR11958; Na/diCO_symport; 1.
DR   Pfam; PF00375; SDF; 1.
DR   PRINTS; PR00173; EDTRNSPORT.
DR   PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
DR   PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing; Glycoprotein;
KW   Membrane; Phosphoprotein; Symport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    572       Excitatory amino acid transporter 2.
FT                                /FTId=PRO_0000202062.
FT   TOPO_DOM      1     44       Cytoplasmic (Potential).
FT   TRANSMEM     45     64       Helical; (Potential).
FT   TRANSMEM     88    108       Helical; (Potential).
FT   TRANSMEM    121    142       Helical; (Potential).
FT   TOPO_DOM    143    238       Extracellular (Potential).
FT   TRANSMEM    239    258       Helical; (Potential).
FT   TRANSMEM    279    300       Helical; (Potential).
FT   TRANSMEM    316    338       Helical; (Potential).
FT   TRANSMEM    405    429       Helical; (Potential).
FT   TRANSMEM    436    458       Helical; (Potential).
FT   MOD_RES      21     21       Phosphoserine (By similarity).
FT   MOD_RES     493    493       Phosphotyrosine.
FT   MOD_RES     537    537       Phosphotyrosine.
FT   MOD_RES     562    562       Phosphoserine.
FT   CARBOHYD    205    205       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    215    215       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1      6       MASTEG -> MVS (in isoform Glt-1A and
FT                                isoform Glt-1B).
FT                                /FTId=VSP_006264.
FT   VAR_SEQ     551    572       TLAANGKSADCSVEEEPWKREK -> PFPFLDIETCI (in
FT                                isoform Glt-1B).
FT                                /FTId=VSP_006265.
FT   CONFLICT     26     26       D -> E (in Ref. 3; AAA91643).
FT   CONFLICT     62     62       G -> R (in Ref. 3; AAA91643).
FT   CONFLICT    112    112       A -> V (in Ref. 3; AAA91643).
FT   CONFLICT    454    454       T -> I (in Ref. 4; AAB71737).
FT   CONFLICT    525    525       K -> L (in Ref. 4; AAB71737).
FT   CONFLICT    572    572       K -> EFD (in Ref. 3; AAA91643).
SQ   SEQUENCE   572 AA;  62030 MW;  13C7C30DED40CA81 CRC64;
     MASTEGANNM PKQVEVRMHD SHLSSDEPKH RNLGMRMCDK LGKNLLLSLT VFGVILGAVC
     GGLLRLASPI HPDVVMLIAF PGDILMRMLK MLILPLIISS LITGLSGLDA KASGRLGTRA
     MVYYMSTTII AAVLGVILVL AIHPGNPKLK KQLGPGKKND EVSSLDAFLD LIRNLFPENL
     VQACFQQIQT VTKKVLVAPP SEEANTTKAV ISMLNETMNE APEETKIVIK KGLEFKDGMN
     VLGLIGFFIA FGIAMGKMGE QAKLMVEFFN ILNEIVMKLV IMIMWYSPLG IACLICGKII
     AIKDLEVVAR QLGMYMITVI VGLIIHGGIF LPLIYFVVTR KNPFSFFAGI FQAWITALGT
     ASSAGTLPVT FRCLEDNLGI DKRVTRFVLP VGATINMDGT ALYEAVAAIF IAQMNGVILD
     GGQIVTVSLT ATLASIGAAS IPSAGLVTML LILTAVGLPT EDISLLVAVD WLLDRMRTSV
     NVVGDSFGAG IVYHLSKSEL DTIDSQHRMQ EDIEMTKTQS IYDDKNHRES NSNQCVYAAH
     NSVVIDECKV TLAANGKSAD CSVEEEPWKR EK
//
ID   H14_MOUSE               Reviewed;         219 AA.
AC   P43274; Q5EBH3;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Histone H1.4;
DE   AltName: Full=H1 VAR.2;
DE   AltName: Full=H1e;
GN   Name=Hist1h1e; Synonyms=H1f4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/c; TISSUE=Spleen;
RX   MEDLINE=94248041; PubMed=8190634; DOI=10.1093/nar/22.8.1421;
RA   Dong Y., Sirotkin A.M., Yang Y.-S., Brown D.T., Sittman D.B.,
RA   Skoultchi A.I.;
RT   "Isolation and characterization of two replication-dependent mouse H1
RT   histone genes.";
RL   Nucleic Acids Res. 22:1421-1428(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=93107085; PubMed=8416974;
RA   Brown D.T., Sittman D.B.;
RT   "Identification through overexpression and tagging of the variant type
RT   of the mouse H1e and H1c genes.";
RL   J. Biol. Chem. 268:713-718(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=98322109; PubMed=9655912; DOI=10.1016/S0167-4781(98)00062-1;
RA   Franke K., Drabent B., Doenecke D.;
RT   "Expression of murine H1 histone genes during postnatal development.";
RL   Biochim. Biophys. Acta 1398:232-242(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Histones H1 are necessary for the condensation of
CC       nucleosome chains into higher order structures.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- PTM: Acetylated at Lys-26. Deacetylated at Lys-26 by SIRT1 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the histone H1/H5 family.
CC   -!- SIMILARITY: Contains 1 H15 (linker histone H1/H5 globular) domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; L26163; AAA37760.1; -; Genomic_DNA.
DR   EMBL; L04141; AAA37814.1; -; Genomic_DNA.
DR   EMBL; Y12292; CAA72971.1; -; Genomic_DNA.
DR   EMBL; BC089600; AAH89600.1; -; mRNA.
DR   IPI; IPI00223714; -.
DR   PIR; I49742; I49742.
DR   RefSeq; NP_056602.1; NM_015787.3.
DR   UniGene; Mm.170587; -.
DR   ProteinModelPortal; P43274; -.
DR   SMR; P43274; 36-109.
DR   STRING; P43274; -.
DR   PhosphoSite; P43274; -.
DR   PRIDE; P43274; -.
DR   Ensembl; ENSMUST00000062045; ENSMUSP00000057308; ENSMUSG00000051627.
DR   GeneID; 50709; -.
DR   KEGG; mmu:50709; -.
DR   UCSC; uc007puj.1; mouse.
DR   CTD; 50709; -.
DR   MGI; MGI:1931527; Hist1h1e.
DR   eggNOG; roNOG17301; -.
DR   GeneTree; ENSGT00550000074201; -.
DR   HOGENOM; HBG446956; -.
DR   HOVERGEN; HBG009035; -.
DR   InParanoid; P43274; -.
DR   OMA; PAYRINQ; -.
DR   OrthoDB; EOG4H19XG; -.
DR   PhylomeDB; P43274; -.
DR   NextBio; 307565; -.
DR   ArrayExpress; P43274; -.
DR   Bgee; P43274; -.
DR   CleanEx; MM_HIST1H1E; -.
DR   Genevestigator; P43274; -.
DR   GermOnline; ENSMUSG00000051627; Mus musculus.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   GO; GO:0016584; P:nucleosome positioning; IMP:MGI.
DR   InterPro; IPR005818; Histone_H1/H5.
DR   InterPro; IPR005819; Histone_H5.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF00538; Linker_histone; 1.
DR   PRINTS; PR00624; HISTONEH5.
DR   SMART; SM00526; H15; 1.
DR   PROSITE; PS51504; H15; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromosome; DNA-binding; Nucleus; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    219       Histone H1.4.
FT                                /FTId=PRO_0000195917.
FT   DOMAIN       36    109       H15.
FT   MOD_RES       2      2       N-acetylserine.
FT   MOD_RES       2      2       Phosphoserine (By similarity).
FT   MOD_RES       4      4       Phosphothreonine.
FT   MOD_RES      17     17       N6-acetyllysine (By similarity).
FT   MOD_RES      18     18       Phosphothreonine.
FT   MOD_RES      26     26       N6-acetyllysine (By similarity).
FT   MOD_RES      36     36       Phosphoserine.
FT   MOD_RES      41     41       Phosphoserine (By similarity).
FT   MOD_RES      46     46       N6-acetyllysine (By similarity).
FT   MOD_RES     146    146       Phosphothreonine (By similarity).
FT   MOD_RES     187    187       Phosphoserine (By similarity).
SQ   SEQUENCE   219 AA;  21977 MW;  9463467F699F3625 CRC64;
     MSETAPAAPA APAPAEKTPV KKKARKAAGG AKRKTSGPPV SELITKAVAA SKERSGVSLA
     ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG ASGSFKLNKK AASGEAKPKA
     KRAGAAKAKK PAGAAKKPKK AAGTATAKKS TKKTPKKAKK PAAAAGAKKA KSPKKAKATK
     AKKAPKSPAK AKTVKPKAAK PKTSKPKAAK PKKTAAKKK
//
ID   H11_MOUSE               Reviewed;         213 AA.
AC   P43275;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Histone H1.1;
DE   AltName: Full=H1 VAR.3;
DE            Short=H1a;
GN   Name=Hist1h1a; Synonyms=H1f1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=94248041; PubMed=8190634; DOI=10.1093/nar/22.8.1421;
RA   Dong Y., Sirotkin A.M., Yang Y.-S., Brown D.T., Sittman D.B.,
RA   Skoultchi A.I.;
RT   "Isolation and characterization of two replication-dependent mouse H1
RT   histone genes.";
RL   Nucleic Acids Res. 22:1421-1428(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=98322109; PubMed=9655912; DOI=10.1016/S0167-4781(98)00062-1;
RA   Franke K., Drabent B., Doenecke D.;
RT   "Expression of murine H1 histone genes during postnatal development.";
RL   Biochim. Biophys. Acta 1398:232-242(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=22296985; PubMed=12408966; DOI=10.1016/S0888-7543(02)96850-3;
RA   Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
RT   "The human and mouse replication-dependent histone genes.";
RL   Genomics 80:487-498(2002).
CC   -!- FUNCTION: Histones H1 are necessary for the condensation of
CC       nucleosome chains into higher order structures.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- SIMILARITY: Belongs to the histone H1/H5 family.
CC   -!- SIMILARITY: Contains 1 H15 (linker histone H1/H5 globular) domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; L26164; AAA37761.1; -; Genomic_DNA.
DR   EMBL; Y12290; CAA72969.1; -; Genomic_DNA.
DR   EMBL; AY158903; AAO06214.1; -; Genomic_DNA.
DR   IPI; IPI00228616; -.
DR   PIR; S43949; S43949.
DR   RefSeq; NP_085112.1; NM_030609.2.
DR   UniGene; Mm.377137; -.
DR   UniGene; Mm.480242; -.
DR   ProteinModelPortal; P43275; -.
DR   SMR; P43275; 38-111.
DR   STRING; P43275; -.
DR   PhosphoSite; P43275; -.
DR   PRIDE; P43275; -.
DR   Ensembl; ENSMUST00000055770; ENSMUSP00000062030; ENSMUSG00000049539.
DR   GeneID; 80838; -.
DR   KEGG; mmu:80838; -.
DR   UCSC; uc007puz.1; mouse.
DR   CTD; 80838; -.
DR   MGI; MGI:1931523; Hist1h1a.
DR   eggNOG; maNOG23433; -.
DR   HOGENOM; HBG446956; -.
DR   HOVERGEN; HBG009035; -.
DR   InParanoid; P43275; -.
DR   OMA; NRARTAK; -.
DR   OrthoDB; EOG4H19XG; -.
DR   NextBio; 350151; -.
DR   ArrayExpress; P43275; -.
DR   Bgee; P43275; -.
DR   CleanEx; MM_HIST1H1A; -.
DR   Genevestigator; P43275; -.
DR   GermOnline; ENSMUSG00000049539; Mus musculus.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   GO; GO:0007283; P:spermatogenesis; IGI:MGI.
DR   InterPro; IPR005818; Histone_H1/H5.
DR   InterPro; IPR005819; Histone_H5.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF00538; Linker_histone; 1.
DR   PRINTS; PR00624; HISTONEH5.
DR   SMART; SM00526; H15; 1.
DR   PROSITE; PS51504; H15; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Chromosome; DNA-binding; Nucleus.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    213       Histone H1.1.
FT                                /FTId=PRO_0000195914.
FT   DOMAIN       38    111       H15.
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES      87     87       N6-acetyllysine (By similarity).
SQ   SEQUENCE   213 AA;  21785 MW;  03A46320A100B203 CRC64;
     MSETAPVAQA ASTATEKPAA AKKTKKPAKA AAPRKKPAGP SVSELIVQAV SSSKERSGVS
     LAALKKSLAA AGYDVEKNNS RIKLGLKSLV NKGTLVQTKG TGAAGSFKLN KKAESKAITT
     KVSVKAKASG AAKKPKKTAG AAAKKTVKTP KKPKKPAVSK KTSKSPKKPK VVKAKKVAKS
     PAKAKAVKPK ASKAKVTKPK TPAKPKKAAP KKK
//
ID   H15_MOUSE               Reviewed;         223 AA.
AC   P43276; Q9CRM8;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Histone H1.5;
DE   AltName: Full=H1 VAR.5;
DE   AltName: Full=H1b;
GN   Name=Hist1h1b; Synonyms=H1f5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/c; TISSUE=Blood;
RX   MEDLINE=96014286; PubMed=8589518; DOI=10.1007/BF00356166;
RA   Drabent B., Franke K., Bode C., Kosciessa U., Bouterfa H.,
RA   Hameister H., Doenecke D.;
RT   "Isolation of two murine H1 histone genes and chromosomal mapping of
RT   the H1 gene complement.";
RL   Mamm. Genome 6:505-511(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=97011334; PubMed=8858344;
RA   Wang Z.-F., Krasikov T., Frey M.R., Wang J., Matera A.G.,
RA   Marzluff W.F.;
RT   "Characterization of the mouse histone gene cluster on chromosome 13:
RT   45 histone genes in three patches spread over 1Mb.";
RL   Genome Res. 6:688-701(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=22296985; PubMed=12408966; DOI=10.1016/S0888-7543(02)96850-3;
RA   Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
RT   "The human and mouse replication-dependent histone genes.";
RL   Genomics 80:487-498(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-220.
RC   STRAIN=C57BL/6J; TISSUE=Embryonic kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION AT
RP   SER-18, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Histones H1 are necessary for the condensation of
CC       nucleosome chains into higher order structures.
CC   -!- INTERACTION:
CC       P13297:Msx1; NbExp=2; IntAct=EBI-903960, EBI-903969;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- SIMILARITY: Belongs to the histone H1/H5 family.
CC   -!- SIMILARITY: Contains 1 H15 (linker histone H1/H5 globular) domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Z46227; CAA86299.1; -; Genomic_DNA.
DR   EMBL; U62922; AAB05798.1; -; Genomic_DNA.
DR   EMBL; AY158904; AAO06215.1; -; Genomic_DNA.
DR   EMBL; AK020117; BAB32001.1; -; mRNA.
DR   IPI; IPI00230133; -.
DR   PIR; A35245; A35245.
DR   PIR; S49492; S49492.
DR   RefSeq; NP_064418.1; NM_020034.1.
DR   UniGene; Mm.221314; -.
DR   ProteinModelPortal; P43276; -.
DR   SMR; P43276; 37-109.
DR   IntAct; P43276; 4.
DR   STRING; P43276; -.
DR   PhosphoSite; P43276; -.
DR   PRIDE; P43276; -.
DR   Ensembl; ENSMUST00000080511; ENSMUSP00000079356; ENSMUSG00000058773.
DR   GeneID; 56702; -.
DR   KEGG; mmu:56702; -.
DR   UCSC; uc007pri.1; mouse.
DR   CTD; 56702; -.
DR   MGI; MGI:1861461; Hist1h1b.
DR   eggNOG; roNOG17301; -.
DR   HOGENOM; HBG446956; -.
DR   HOVERGEN; HBG009035; -.
DR   InParanoid; P43276; -.
DR   OMA; SKERNVC; -.
DR   OrthoDB; EOG4H19XG; -.
DR   NextBio; 313147; -.
DR   ArrayExpress; P43276; -.
DR   Bgee; P43276; -.
DR   CleanEx; MM_HIST1H1B; -.
DR   Genevestigator; P43276; -.
DR   GermOnline; ENSMUSG00000058773; Mus musculus.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0007517; P:muscle organ development; IPI:MGI.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   InterPro; IPR005818; Histone_H1/H5.
DR   InterPro; IPR005819; Histone_H5.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF00538; Linker_histone; 1.
DR   PRINTS; PR00624; HISTONEH5.
DR   SMART; SM00526; H15; 1.
DR   PROSITE; PS51504; H15; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromosome; DNA-binding; Nucleus; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    223       Histone H1.5.
FT                                /FTId=PRO_0000195918.
FT   DOMAIN       36    109       H15.
FT   MOD_RES       2      2       N-acetylserine.
FT   MOD_RES       2      2       Phosphoserine (By similarity).
FT   MOD_RES       4      4       Phosphothreonine.
FT   MOD_RES      18     18       Phosphoserine.
FT   MOD_RES      36     36       Phosphothreonine (By similarity).
FT   MOD_RES      41     41       Phosphoserine (By similarity).
FT   MOD_RES      90     90       N6-acetyllysine (By similarity).
FT   MOD_RES     104    104       Phosphoserine (By similarity).
FT   MOD_RES     106    106       N6-acetyllysine (By similarity).
FT   MOD_RES     135    135       Phosphothreonine (By similarity).
FT   MOD_RES     165    165       N6-acetyllysine (By similarity).
FT   MOD_RES     186    186       Phosphoserine (By similarity).
FT   MOD_RES     206    206       N6-acetyllysine (By similarity).
FT   CONFLICT     61     61       A -> T (in Ref. 3; BAB32001).
FT   CONFLICT    120    120       A -> V (in Ref. 3; BAB32001).
FT   CONFLICT    137    137       K -> N (in Ref. 3; BAB32001).
FT   CONFLICT    195    195       S -> F (in Ref. 3; BAB32001).
SQ   SEQUENCE   223 AA;  22576 MW;  B9C26AC31C2716B6 CRC64;
     MSETAPAETA APAPVEKSPA KKKTTKKAGA AKRKATGPPV SELITKAVSA SKERGGVSLP
     ALKKALAAGG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG ASGSFKLNKK AASGEAKPKA
     KKTGAAKAKK PAGATPKKPK KTAGAKKTVK KTPKKAKKPA AAGVKKVAKS PKKAKAAAKP
     KKAAKSPAKP KAVKSKASKP KVTKPKTAKP KAAKAKKAVS KKK
//
ID   H13_MOUSE               Reviewed;         221 AA.
AC   P43277; Q8C6M4;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   30-NOV-2010, entry version 90.
DE   RecName: Full=Histone H1.3;
DE   AltName: Full=H1 VAR.4;
DE   AltName: Full=H1d;
GN   Name=Hist1h1d; Synonyms=H1f3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=96014286; PubMed=8589518; DOI=10.1007/BF00356166;
RA   Drabent B., Franke K., Bode C., Kosciessa U., Bouterfa H.,
RA   Hameister H., Doenecke D.;
RT   "Isolation of two murine H1 histone genes and chromosomal mapping of
RT   the H1 gene complement.";
RL   Mamm. Genome 6:505-511(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=97011334; PubMed=8858344;
RA   Wang Z.-F., Krasikov T., Frey M.R., Wang J., Matera A.G.,
RA   Marzluff W.F.;
RT   "Characterization of the mouse histone gene cluster on chromosome 13:
RT   45 histone genes in three patches spread over 1Mb.";
RL   Genome Res. 6:688-701(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=22296985; PubMed=12408966; DOI=10.1016/S0888-7543(02)96850-3;
RA   Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
RT   "The human and mouse replication-dependent histone genes.";
RL   Genomics 80:487-498(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Ovary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Histones H1 are necessary for the condensation of
CC       nucleosome chains into higher order structures.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- SIMILARITY: Belongs to the histone H1/H5 family.
CC   -!- SIMILARITY: Contains 1 H15 (linker histone H1/H5 globular) domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Z38128; CAA86288.1; -; Genomic_DNA.
DR   EMBL; U62923; AAB05799.1; -; Genomic_DNA.
DR   EMBL; AY158906; AAO06217.1; -; Genomic_DNA.
DR   EMBL; AK054269; BAC35711.1; -; mRNA.
DR   IPI; IPI00331597; -.
DR   PIR; B35245; B35245.
DR   PIR; S49482; S49482.
DR   RefSeq; NP_663759.3; NM_145713.3.
DR   UniGene; Mm.247046; -.
DR   ProteinModelPortal; P43277; -.
DR   SMR; P43277; 37-110.
DR   STRING; P43277; -.
DR   PhosphoSite; P43277; -.
DR   PRIDE; P43277; -.
DR   Ensembl; ENSMUST00000045301; ENSMUSP00000044395; ENSMUSG00000052565.
DR   GeneID; 14957; -.
DR   KEGG; mmu:14957; -.
DR   CTD; 14957; -.
DR   MGI; MGI:107502; Hist1h1d.
DR   eggNOG; maNOG23410; -.
DR   HOGENOM; HBG446956; -.
DR   HOVERGEN; HBG009035; -.
DR   InParanoid; P43277; -.
DR   OMA; RKSAGAT; -.
DR   NextBio; 287298; -.
DR   ArrayExpress; P43277; -.
DR   Bgee; P43277; -.
DR   CleanEx; MM_HIST1H1D; -.
DR   Genevestigator; P43277; -.
DR   GermOnline; ENSMUSG00000052565; Mus musculus.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   GO; GO:0016584; P:nucleosome positioning; IMP:MGI.
DR   InterPro; IPR005818; Histone_H1/H5.
DR   InterPro; IPR005819; Histone_H5.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF00538; Linker_histone; 1.
DR   PRINTS; PR00624; HISTONEH5.
DR   SMART; SM00526; H15; 1.
DR   PROSITE; PS51504; H15; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromosome; DNA-binding; Nucleus; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    221       Histone H1.3.
FT                                /FTId=PRO_0000195916.
FT   DOMAIN       37    110       H15.
FT   MOD_RES       2      2       N-acetylserine.
FT   MOD_RES       4      4       Phosphothreonine (By similarity).
FT   MOD_RES      18     18       Phosphothreonine.
FT   MOD_RES      37     37       Phosphoserine.
FT   CONFLICT     57     57       G -> C (in Ref. 4; BAC35711).
SQ   SEQUENCE   221 AA;  22100 MW;  19D888981281E55C CRC64;
     MSETAPAAPA APAPVEKTPV KKKAKKTGAA AGKRKASGPP VSELITKAVA ASKERSGVSL
     AALKKALAAA GYDVEKNNSR IKLGLKSLVS KGTLVQTKGT GASGSFKLNK KAASGEAKPK
     AKKAGAAKAK KPAGAAKKPK KATGAATPKK TAKKTPKKAK KPAAAAGAKK VSKSPKKVKA
     AKPKKAAKSP AKAKAPKAKA SKPKASKPKA TKAKKAAPRK K
//
ID   ITAV_MOUSE              Reviewed;        1044 AA.
AC   P43406;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Integrin alpha-V;
DE   AltName: Full=Vitronectin receptor subunit alpha;
DE   AltName: CD_antigen=CD51;
DE   Contains:
DE     RecName: Full=Integrin alpha-V heavy chain;
DE   Contains:
DE     RecName: Full=Integrin alpha-V light chain;
DE   Flags: Precursor;
GN   Name=Itgav;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CD-1; TISSUE=Kidney;
RX   MEDLINE=96176309; PubMed=8601592; DOI=10.1083/jcb.132.6.1161;
RA   Wada J., Kumar A., Liu Z., Ruoslahti E., Reichardt L., Marvaldi J.,
RA   Kanwar Y.S.;
RT   "Cloning of mouse integrin alphaV cDNA and role of the alphaV-related
RT   matrix receptors in metanephric development.";
RL   J. Cell Biol. 132:1161-1176(1996).
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74; ASN-615; ASN-869;
RP   ASN-939 AND ASN-941, AND MASS SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-74; ASN-615 AND ASN-869,
RP   AND MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: The alpha-V integrins are receptors for vitronectin,
CC       cytotactin, fibronectin, fibrinogen, laminin, matrix
CC       metalloproteinase-2, osteopontin, osteomodulin, prothrombin,
CC       thrombospondin and vWF. They recognize the sequence R-G-D in a
CC       wide array of ligands. Alpha-V integrins may play a role in embryo
CC       implantation, angiogenesis and wound healing. Mice expressing a
CC       null mutation of the alpha-V subunit gene survive until late in
CC       embryonic development and occasionally even to birth. They
CC       demonstrate cleft palate, and defective development of CNS and
CC       gastrointestinal blood vessels.
CC   -!- SUBUNIT: Interacts with RAB25 (By similarity). Heterodimer of an
CC       alpha and a beta subunit. The alpha subunit is composed of an
CC       heavy and a light chain linked by a disulfide bond. Alpha-V
CC       associates with either beta-1, beta-3, beta-5, beta-6 or beta-8.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the integrin alpha chain family.
CC   -!- SIMILARITY: Contains 7 FG-GAP repeats.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U14135; AAC52497.1; -; mRNA.
DR   IPI; IPI00120245; -.
DR   PIR; T10050; T10050.
DR   UniGene; Mm.227; -.
DR   ProteinModelPortal; P43406; -.
DR   SMR; P43406; 31-1022.
DR   STRING; P43406; -.
DR   PhosphoSite; P43406; -.
DR   PRIDE; P43406; -.
DR   Ensembl; ENSMUST00000028499; ENSMUSP00000028499; ENSMUSG00000027087.
DR   UCSC; uc008kid.1; mouse.
DR   MGI; MGI:96608; Itgav.
DR   HOGENOM; HBG402992; -.
DR   HOVERGEN; HBG006186; -.
DR   InParanoid; P43406; -.
DR   OrthoDB; EOG46DM20; -.
DR   ArrayExpress; P43406; -.
DR   Bgee; P43406; -.
DR   CleanEx; MM_ITGAV; -.
DR   Genevestigator; P43406; -.
DR   GermOnline; ENSMUSG00000027087; Mus musculus.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0043277; P:apoptotic cell clearance; IMP:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR013519; Int_alpha_beta-p.
DR   InterPro; IPR000413; Integrin_alpha.
DR   InterPro; IPR013649; Integrin_alpha-2.
DR   InterPro; IPR018184; Integrin_alpha_C_CS.
DR   Pfam; PF01839; FG-GAP; 3.
DR   Pfam; PF00357; Integrin_alpha; 1.
DR   Pfam; PF08441; Integrin_alpha2; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   SMART; SM00191; Int_alpha; 5.
DR   PROSITE; PS51470; FG_GAP; 7.
DR   PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE   1: Evidence at protein level;
KW   Angiogenesis; Calcium; Cell adhesion;
KW   Cleavage on pair of basic residues; Developmental protein;
KW   Differentiation; Disulfide bond; Glycoprotein; Integrin; Membrane;
KW   Receptor; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     30       By similarity.
FT   CHAIN        31   1044       Integrin alpha-V.
FT                                /FTId=PRO_0000016304.
FT   CHAIN        31    885       Integrin alpha-V heavy chain (By
FT                                similarity).
FT                                /FTId=PRO_0000016305.
FT   CHAIN       887   1044       Integrin alpha-V light chain (By
FT                                similarity).
FT                                /FTId=PRO_0000016306.
FT   TOPO_DOM     31    988       Extracellular (Potential).
FT   TRANSMEM    989   1012       Helical; (Potential).
FT   TOPO_DOM   1013   1044       Cytoplasmic (Potential).
FT   REPEAT       32     98       FG-GAP 1.
FT   REPEAT      109    170       FG-GAP 2.
FT   REPEAT      173    225       FG-GAP 3.
FT   REPEAT      237    295       FG-GAP 4.
FT   REPEAT      296    357       FG-GAP 5.
FT   REPEAT      358    415       FG-GAP 6.
FT   REPEAT      419    482       FG-GAP 7.
FT   CA_BIND     260    268       Potential.
FT   CA_BIND     314    322       Potential.
FT   CA_BIND     379    387       Potential.
FT   CA_BIND     443    451       Potential.
FT   MOTIF      1015   1019       GFFKR motif.
FT   CARBOHYD     74     74       N-linked (GlcNAc...).
FT   CARBOHYD    290    290       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    296    296       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    615    615       N-linked (GlcNAc...).
FT   CARBOHYD    704    704       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    835    835       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    851    851       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    869    869       N-linked (GlcNAc...).
FT   CARBOHYD    939    939       N-linked (GlcNAc...).
FT   CARBOHYD    941    941       N-linked (GlcNAc...).
FT   CARBOHYD    969    969       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    976    976       N-linked (GlcNAc...) (Potential).
FT   DISULFID     89     97       By similarity.
FT   DISULFID    138    158       By similarity.
FT   DISULFID    172    185       By similarity.
FT   DISULFID    491    502       By similarity.
FT   DISULFID    508    565       By similarity.
FT   DISULFID    626    632       By similarity.
FT   DISULFID    698    711       By similarity.
FT   DISULFID    852    900       Interchain (between heavy and light
FT                                chains) (By similarity).
FT   DISULFID    905    910       By similarity.
SQ   SEQUENCE   1044 AA;  115278 MW;  F06A8FF22705183D CRC64;
     MAAPGRLLLR PRPGGLLLLL PGLLLPLADA FNLDVESPAE YAGPEGSYFG FAVDFFEPST
     SSRMFLLVGA PKANTTQPGI VEGGQVLKCE CSSSRRCQPI EFDSTGNRDY AKDDPLEFKS
     HQWFGASVRS KQDKILACAP LYHWRTEMKQ EREPVGTCFL QDGTKTVEYA PCRSKNIDAD
     GQGFCQGGFS IDFTKADRVL LGGPGSFYWQ GQLISDQVAE IISKYDPNVY SIKYNNQLAT
     RTAQAIFDDS YLGYSVAVGD FNGDGIEDFV SGVPRAARTL GMVYIYDGKN MSSLHNFTGE
     QMAAYFGFSV AATDINGDDY ADVFIGAPLF MDRGSDGKLQ EVGQVSVSLQ RAVGDFQTTK
     LNGFEVFARF GSAIAPLGDL DQDGFNDIAI AAPYGGEDKK GLVYIFNGRS TGLNSVPSQI
     LEGQWAAQSM PPSFGYSMKG ATDVDRNGYP DLVVGAFGVD RAVLYRARPV VTVNAGLEVY
     PSILNQDNKI CPLPGTALKV SCFNVRFCLK ADGKGTLPRK LHFQVDVLLD KLKQKGAIRR
     ALFLHNRSPV HSKTMTVFRG GQMQCEELVA YLRDESEFRD KLTPITIFME YRLDQRTAAD
     ATGLQPILNQ FTPANVSRQA HILLDCGEDN VCKPKLEVSV NSDQKKIYIG DDNPLTLTVK
     AQNQGEGAYE AELIVSIPPQ ADFIGVVRNN EALARLSCAF KTENQTRQVV CDLGNPMKAG
     TQLLAGLRFS VHQQSEMDTS VKFDLKIQSS NSFDNVSPVV SYKVDLAEKA AVEIRGVSSP
     DHIFLPIPNW EYKENPETEE DVGPIVQHIY ELRNNGPSSF SKAILNLQWP YKYNNNTLLY
     ILHYDIDGPM NCTADTEINP LRIKTPEKND TGAAGQGERS HLITKRGLTL REGDVHTLGC
     GIAKCLQITC QVGRLDRGKS AILYVKSLLW TETFMNKENQ NHSYSLKSSA SFNIIEFPYK
     NLPIEDLFNS TLVTTNITWG IQPAPMPVPV WVIILAVLAG LLLLAVLVFV MYRMGFFKRV
     RPPQEEQERE QLQPHENGEG NSET
//
ID   COF2_MOUSE              Reviewed;         166 AA.
AC   P45591;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Cofilin-2;
DE   AltName: Full=Cofilin, muscle isoform;
GN   Name=Cfl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C3H; TISSUE=Skeletal muscle;
RX   MEDLINE=94253093; PubMed=8195165;
RA   Ono S., Minami N., Abe H., Obinata T.;
RT   "Characterization of a novel cofilin isoform that is predominantly
RT   expressed in mammalian skeletal muscle.";
RL   J. Biol. Chem. 269:15280-15286(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND THR-6, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Controls reversibly actin polymerization and
CC       depolymerization in a pH-sensitive manner. It has the ability to
CC       bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the
CC       major component of intranuclear and cytoplasmic actin rods.
CC   -!- SUBCELLULAR LOCATION: Nucleus matrix. Cytoplasm, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle.
CC   -!- PTM: The phosphorylation of Ser-24 may prevent recognition of the
CC       nuclear localization signal.
CC   -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC   -!- SIMILARITY: Contains 1 ADF-H domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; L29468; AAA37433.1; -; mRNA.
DR   EMBL; BC007138; AAH07138.1; -; mRNA.
DR   IPI; IPI00266188; -.
DR   PIR; A53812; A53812.
DR   RefSeq; NP_031714.1; NM_007688.2.
DR   UniGene; Mm.276826; -.
DR   ProteinModelPortal; P45591; -.
DR   SMR; P45591; 1-166.
DR   STRING; P45591; -.
DR   PhosphoSite; P45591; -.
DR   REPRODUCTION-2DPAGE; P45591; -.
DR   PRIDE; P45591; -.
DR   Ensembl; ENSMUST00000078124; ENSMUSP00000077262; ENSMUSG00000062929.
DR   GeneID; 12632; -.
DR   KEGG; mmu:12632; -.
DR   UCSC; uc007nnx.1; mouse.
DR   CTD; 12632; -.
DR   MGI; MGI:101763; Cfl2.
DR   eggNOG; roNOG16316; -.
DR   HOGENOM; HBG628477; -.
DR   HOVERGEN; HBG000381; -.
DR   InParanoid; P45591; -.
DR   OMA; GLYDATY; -.
DR   OrthoDB; EOG4WSWBP; -.
DR   PhylomeDB; P45591; -.
DR   NextBio; 281820; -.
DR   ArrayExpress; P45591; -.
DR   Bgee; P45591; -.
DR   CleanEx; MM_CFL2; -.
DR   Genevestigator; P45591; -.
DR   GermOnline; ENSMUSG00000062929; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR002108; Actin-bd_cofilin/tropomyosin.
DR   InterPro; IPR017904; ADF/Cofilin/Destrin.
DR   Pfam; PF00241; Cofilin_ADF; 1.
DR   PRINTS; PR00006; COFILIN.
DR   SMART; SM00102; ADF; 1.
DR   PROSITE; PS51263; ADF_H; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Cytoplasm; Cytoskeleton; Nucleus;
KW   Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    166       Cofilin-2.
FT                                /FTId=PRO_0000214908.
FT   DOMAIN        4    153       ADF-H.
FT   MOTIF        30     34       Nuclear localization signal (Potential).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       3      3       Phosphoserine.
FT   MOD_RES       6      6       Phosphothreonine.
FT   MOD_RES      24     24       Phosphoserine (By similarity).
FT   MOD_RES      89     89       Phosphotyrosine.
FT   MOD_RES      92     92       N6-acetyllysine (By similarity).
SQ   SEQUENCE   166 AA;  18710 MW;  48B6D7E5AE9FE1CC CRC64;
     MASGVTVNDE VIKVFNDMKV RKSSTQEEIK KRKKAVLFCL SDDKRQIIVE EAKQILVGDI
     GDTVEDPYTS FVKLLPLNDC RYALYDATYE TKESKKEDLV FIFWAPESAP LKSKMIYASS
     KDAIKKKFTG IKHEWQVNGL DDIKDRSTLG EKLGGSVVVS LEGKPL
//
ID   SIPA1_MOUSE             Reviewed;        1037 AA.
AC   P46062; P70204;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2002, sequence version 2.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Signal-induced proliferation-associated protein 1;
DE            Short=Sipa-1;
DE   AltName: Full=GTPase-activating protein Spa-1;
GN   Name=Sipa1; Synonyms=Spa-1, Spa1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=95098034; PubMed=7799964;
RA   Hattori M., Tsukamoto N., Nur-E-Kamal M.S.A., Rubinfeld B., Iwai K.,
RA   Kubota H., Maruta H., Minato N.;
RT   "Molecular cloning of a novel mitogen-inducible nuclear protein with a
RT   Ran GTPase-activating domain that affects cell cycle progression.";
RL   Mol. Cell. Biol. 15:552-560(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 324-1037.
RC   STRAIN=DBA/2;
RX   MEDLINE=97179201; PubMed=9027487; DOI=10.1006/geno.1996.4464;
RA   Wada Y., Kubota H., Maeda M., Taniwaki M., Hattori M., Imamura S.,
RA   Iwai K., Minato N.;
RT   "Mitogen-inducible SIPA1 is mapped to the conserved syntenic groups of
RT   chromosome 19 in mouse and chromosome 11q13.3 centromeric to BCL1 in
RT   human.";
RL   Genomics 39:66-73(1997).
RN   [3]
RP   IDENTIFICATION OF PROBABLE FRAMESHIFTS.
RX   MEDLINE=98010656; PubMed=9346962; DOI=10.1074/jbc.272.44.28081;
RA   Kurachi H., Wada Y., Tsukamoto N., Maeda M., Kubota H., Hattori M.,
RA   Iwai K., Minato N.;
RT   "Human SPA-1 product selectively expressed in lymphoid tissues is a
RT   specific GTPase-activating protein for Rap1 and Rap2.";
RL   J. Biol. Chem. 272:28081-28088(1997).
CC   -!- FUNCTION: GTPase activator for the nuclear Ras-related regulatory
CC       protein Rap1, Rsr1 and Ran in vitro, converting it to the
CC       putatively inactive GDP-bound state. Affects cell cycle
CC       progression.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Mostly nuclear.
CC   -!- TISSUE SPECIFICITY: Preferentially expressed in both fetal and
CC       adult lymphohematopoietic tissues.
CC   -!- INDUCTION: By mitogens.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 Rap-GAP domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA01973.1; Type=Frameshift; Positions=Several;
CC       Sequence=BAA13469.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; D11374; BAA01973.1; ALT_FRAME; mRNA.
DR   EMBL; D87849; BAA13469.1; ALT_INIT; Genomic_DNA.
DR   IPI; IPI00129472; -.
DR   PIR; I49709; I49709.
DR   UniGene; Mm.3072; -.
DR   ProteinModelPortal; P46062; -.
DR   SMR; P46062; 202-542, 679-754.
DR   STRING; P46062; -.
DR   PhosphoSite; P46062; -.
DR   PRIDE; P46062; -.
DR   Ensembl; ENSMUST00000071857; ENSMUSP00000073618; ENSMUSG00000056917.
DR   Ensembl; ENSMUST00000080824; ENSMUSP00000079637; ENSMUSG00000056917.
DR   MGI; MGI:107576; Sipa1.
DR   eggNOG; maNOG17954; -.
DR   HOVERGEN; HBG061666; -.
DR   InParanoid; P46062; -.
DR   OrthoDB; EOG4XPQF5; -.
DR   ArrayExpress; P46062; -.
DR   Bgee; P46062; -.
DR   CleanEx; MM_SIPA1; -.
DR   Genevestigator; P46062; -.
DR   GermOnline; ENSMUSG00000056917; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR000331; Rap_GAP.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF02145; Rap_GAP; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50085; RAPGAP; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; GTPase activation; Nucleus; Phosphoprotein.
FT   CHAIN         1   1037       Signal-induced proliferation-associated
FT                                protein 1.
FT                                /FTId=PRO_0000056745.
FT   DOMAIN      316    534       Rap-GAP.
FT   DOMAIN      682    758       PDZ.
FT   COILED      968   1025       Potential.
FT   MOD_RES      51     51       Phosphoserine (By similarity).
FT   MOD_RES      53     53       Phosphoserine (By similarity).
FT   MOD_RES      62     62       Phosphothreonine (By similarity).
FT   MOD_RES      65     65       Phosphoserine (By similarity).
FT   MOD_RES      72     72       Phosphoserine (By similarity).
FT   MOD_RES     834    834       Phosphoserine (By similarity).
FT   CONFLICT    738    738       T -> A (in Ref. 2; BAA13469).
FT   CONFLICT    763    763       R -> Q (in Ref. 2; BAA13469).
FT   CONFLICT    829    829       T -> S (in Ref. 2; BAA13469).
SQ   SEQUENCE   1037 AA;  112066 MW;  2A30592E920A9AA5 CRC64;
     MWAGGVGSPR RGMAPAPTDD LFARKLRQPA RPPLTPNTFE PRPARGPLLR SGSDAGEVRP
     PTPASPRARA HSHEDASRPA ATPTRLFTDP LALLGLPAEE PEPTFPPVLE PRWFAHYDVQ
     SLLFDWAPRP RGTGSHTEAN SGTLAEGQTT TSDLLLGAPG FVSELGGEGE LGLGGPISPP
     VPPALPNAAV SVLEEPQTRT TTYSLEHADL GAGYYRKYFY GKEHQNFFGL DEALGPVAVS
     LRREEKEGSG GGTLHSYRVI VRTTQLRTLR GTISEDALPP GPPSVSPRKL LEHVAPRLSP
     TCLRLGSASP KVPRQLLTLD EQVLSFQRKG GILYCRAGQG SEEEMYNNQE AGAAFMQFLT
     LLGDVVRLKG FESYRAQLDT KTDSTGTHSL YTTYQDHEIM FHVSTMLPYT PNNQQQLLRK
     RHIGNDIVTI VFQEPGSKPF CPTTIRSHFQ HVFLVVRAHA PCTPHTSYRV AVSRTQDTPA
     FGPALPEGGG PFAANADFRA FLLAKALNGE QAAGHARQFH AMATRTRQQY LQDLATNEVT
     TTSLDSASRF GLPSLGGRRR ATPRSPGADV QAAGALMWGV RAAPGARVAA GAETSGPDDA
     EVPCLLGISA ETLVLVAPRD GRVVFNCACR DVLAWTFSEH QLDLYHGRGE AITLRLDGAP
     GQAVGEVVAR LQLVSRGCET RELALPRDGQ GRLGFEVDAE GFITHVERFT FAETTGLRPG
     ARLLRVCGQT LPKLGPETAA QMLRSAPKVC VTVLPPDESG RPRRSFSELY MLSLKEPSRR
     GGPEPVQDET GKLVILPPTK QLLHFCLKDS SSPPGPGDLT EERTEFLRTH NSLSSGSSLS
     DEAPVLPNTT PDLLLVTTAN PSAPGTDRET PPSQDQSGSP SSHEDTSDSG PELRASILPR
     TLSLRNSISK IMSEAGSETL EDEWQSISEI ASTCNTILES LSREGQPISE SGDPKEALKC
     DSEPEPGSLS EKVSHLESML WKLQEDLQRE KADRAALEEE VRSLRHNNQR LLAESESAAT
     RLLLASKHLG APTTDLA
//
ID   SYT1_MOUSE              Reviewed;         421 AA.
AC   P46096;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   08-MAR-2011, entry version 106.
DE   RecName: Full=Synaptotagmin-1;
DE   AltName: Full=Synaptotagmin I;
DE            Short=SytI;
DE   AltName: Full=p65;
GN   Name=Syt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=95050743; PubMed=7961887;
RA   Fukuda M., Aruga J., Niinobe M., Aimoto S., Mikoshiba K.;
RT   "Inositol-1,3,4,5-tetrakisphosphate binding to C2B domain of
RT   IP4BP/synaptotagmin II.";
RL   J. Biol. Chem. 269:29206-29211(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 183-189; 201-233; 245-260; 273-281; 289-297;
RP   302-313; 333-366 AND 376-388, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   INTERACTION WITH SV2B; SYNTAXIN-1 AND SNAP25.
RX   PubMed=15466855; DOI=10.1074/jbc.M407502200;
RA   Lazzell D.R., Belizaire R., Thakur P., Sherry D.M., Janz R.;
RT   "SV2B regulates synaptotagmin 1 by direct interaction.";
RL   J. Biol. Chem. 279:52124-52131(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-229 AND TYR-380, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-128, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-364, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RA   Lubec G., Kang S.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: May have a regulatory role in the membrane interactions
CC       during trafficking of synaptic vesicles at the active zone of the
CC       synapse. It binds acidic phospholipids with a specificity that
CC       requires the presence of both an acidic head group and a diacyl
CC       backbone. A Ca(2+)-dependent interaction between synaptotagmin and
CC       putative receptors for activated protein kinase C has also been
CC       reported. It can bind to at least three additional proteins in a
CC       Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.
CC   -!- COFACTOR: Binds 3 calcium ions per subunit. The ions are bound to
CC       the C2 domains (By similarity).
CC   -!- SUBUNIT: Homotetramer (Probable). Interacts with SCAMP5, STON2,
CC       SV2A, SV2B, SV2C and RIMS1 (By similarity). Forms a complex with
CC       SV2B, syntaxin 1 and SNAP25.
CC   -!- INTERACTION:
CC       Q8TAC9:SCAMP5 (xeno); NbExp=1; IntAct=EBI-445340, EBI-2695784;
CC       Q8JZZ9:Sv2b; NbExp=1; IntAct=EBI-445340, EBI-466179;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane; Single-pass membrane protein.
CC       Cytoplasmic vesicle, secretory vesicle, chromaffin granule
CC       membrane; Single-pass membrane protein. Cytoplasm. Note=Synaptic
CC       vesicles and chromaffin granules.
CC   -!- DOMAIN: The first C2 domain mediates Ca(2+)-dependent phospholipid
CC       binding.
CC   -!- DOMAIN: The second C2 domain mediates interaction with SV2A and
CC       STN2 (By similarity).
CC   -!- SIMILARITY: Belongs to the synaptotagmin family.
CC   -!- SIMILARITY: Contains 2 C2 domains.
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DR   EMBL; D37792; BAA07040.1; -; mRNA.
DR   EMBL; AK078790; BAC37395.1; -; mRNA.
DR   EMBL; BC042519; AAH42519.1; -; mRNA.
DR   IPI; IPI00129618; -.
DR   RefSeq; NP_033332.1; NM_009306.2.
DR   UniGene; Mm.289702; -.
DR   ProteinModelPortal; P46096; -.
DR   SMR; P46096; 140-418.
DR   IntAct; P46096; 10.
DR   MINT; MINT-4136555; -.
DR   STRING; P46096; -.
DR   TCDB; 9.A.48.1.1; unconventional protein secretion (UPS) system.
DR   PhosphoSite; P46096; -.
DR   PRIDE; P46096; -.
DR   Ensembl; ENSMUST00000064054; ENSMUSP00000063293; ENSMUSG00000035864.
DR   Ensembl; ENSMUST00000105276; ENSMUSP00000100912; ENSMUSG00000035864.
DR   GeneID; 20979; -.
DR   KEGG; mmu:20979; -.
DR   UCSC; uc007gzg.1; mouse.
DR   CTD; 20979; -.
DR   MGI; MGI:99667; Syt1.
DR   eggNOG; roNOG10139; -.
DR   HOGENOM; HBG716633; -.
DR   HOVERGEN; HBG005010; -.
DR   InParanoid; P46096; -.
DR   OMA; HDIIGEY; -.
DR   OrthoDB; EOG4MGS7Q; -.
DR   PhylomeDB; P46096; -.
DR   NextBio; 299964; -.
DR   ArrayExpress; P46096; -.
DR   Bgee; P46096; -.
DR   CleanEx; MM_SYT1; -.
DR   Genevestigator; P46096; -.
DR   GermOnline; ENSMUSG00000035864; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:MGI.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; TAS:MGI.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IPI:HGNC.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   GO; GO:0007269; P:neurotransmitter secretion; IDA:MGI.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   InterPro; IPR001565; Synaptotagmin.
DR   InterPro; IPR015428; Synaptotagmin1.
DR   PANTHER; PTHR10024:SF39; Synaptotagmin1_2; 1.
DR   Pfam; PF00168; C2; 2.
DR   PRINTS; PR00360; C2DOMAIN.
DR   PRINTS; PR00399; SYNAPTOTAGMN.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Calcium; Cell junction; Cytoplasmic vesicle;
KW   Direct protein sequencing; Glycoprotein; Lipoprotein; Membrane;
KW   Metal-binding; Palmitate; Phosphoprotein; Repeat; Synapse;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    421       Synaptotagmin-1.
FT                                /FTId=PRO_0000183938.
FT   TOPO_DOM      1     57       Vesicular (Potential).
FT   TRANSMEM     58     79       Helical; (Potential).
FT   TOPO_DOM     80    421       Cytoplasmic (Potential).
FT   DOMAIN      143    244       C2 1.
FT   DOMAIN      274    377       C2 2.
FT   REGION      135    381       Phospholipid binding (Probable).
FT   COMPBIAS     80    119       Lys-rich.
FT   METAL       171    171       Calcium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       172    172       Calcium 1 (By similarity).
FT   METAL       172    172       Calcium 2 (By similarity).
FT   METAL       178    178       Calcium 1 (By similarity).
FT   METAL       230    230       Calcium 1 (By similarity).
FT   METAL       230    230       Calcium 2 (By similarity).
FT   METAL       231    231       Calcium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       232    232       Calcium 1 (By similarity).
FT   METAL       232    232       Calcium 2 (By similarity).
FT   METAL       232    232       Calcium 3 (By similarity).
FT   METAL       235    235       Calcium 3 (By similarity).
FT   METAL       236    236       Calcium 3; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       238    238       Calcium 2 (By similarity).
FT   METAL       238    238       Calcium 3 (By similarity).
FT   MOD_RES     128    128       Phosphothreonine.
FT   MOD_RES     229    229       Phosphotyrosine.
FT   MOD_RES     236    236       N6-acetyllysine (By similarity).
FT   MOD_RES     364    364       Phosphotyrosine.
FT   MOD_RES     380    380       Phosphotyrosine.
FT   LIPID        74     74       S-palmitoyl cysteine (By similarity).
FT   LIPID        75     75       S-palmitoyl cysteine (By similarity).
FT   LIPID        77     77       S-palmitoyl cysteine (By similarity).
FT   LIPID        79     79       S-palmitoyl cysteine (By similarity).
FT   LIPID        82     82       S-palmitoyl cysteine (By similarity).
FT   CARBOHYD     24     24       N-linked (GlcNAc...) (By similarity).
SQ   SEQUENCE   421 AA;  47418 MW;  7FDEFF37170BD169 CRC64;
     MVSASRPEAL AAPVTTVATL VPHNATEPAS PGEGKEDAFS KLKQKFMNEL HKIPLPPWAL
     IAIAIVAVLL VVTCCFCVCK KCLFKKKNKK KGKEKGGKNA INMKDVKDLG KTMKDQALKD
     DDAETGLTDG EEKEEPKEEE KLGKLQYSLD YDFQNNQLLV GIIQAAELPA LDMGGTSDPY
     VKVFLLPDKK KKFETKVHRK TLNPVFNEQF TFKVPYSELG GKTLVMAVYD FDRFSKHDII
     GEFKVPMNTV DFGHVTEEWR DLQSAEKEEQ EKLGDICFSL RYVPTAGKLT VVILEAKNLK
     KMDVGGLSDP YVKIHLMQNG KRLKKKKTTI KKNTLNPYYN ESFSFEVPFE QIQKVQVVVT
     VLDYDKIGKN DAIGKVFVGY NSTGAELRHW SDMLANPRRP IAQWHTLQVE EEVDAMLAVK
     K
//
ID   NSF_MOUSE               Reviewed;         744 AA.
AC   P46460; A2A646; Q8BQ65; Q8C3R2; Q8CCT9; Q8CEF0; Q923C6;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 105.
DE   RecName: Full=Vesicle-fusing ATPase;
DE            EC=3.6.4.6;
DE   AltName: Full=N-ethylmaleimide-sensitive fusion protein;
DE            Short=NEM-sensitive fusion protein;
DE   AltName: Full=Suppressor of K(+) transport growth defect 2;
DE            Short=Protein SKD2;
DE   AltName: Full=Vesicular-fusion protein NSF;
GN   Name=Nsf; Synonyms=Skd2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=94364487; PubMed=8082782; DOI=10.1016/0014-5793(94)00879-5;
RA   Perier F., Coulter K.L., Liang H., Radeke C.M., Gaber R.F.,
RA   Vandenberg C.A.;
RT   "Identification of a novel mammalian member of the
RT   NSF/CDC48p/Pas1p/TBP-1 family through heterologous expression in
RT   yeast.";
RL   FEBS Lett. 351:286-290(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Head, Lung, Medulla oblongata, Spinal ganglion, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 45-50; 69-87; 106-116; 151-161; 170-198; 218-232;
RP   255-266; 294-303; 305-314; 316-335; 338-357; 404-413; 416-427;
RP   435-446; 517-529; 534-559; 573-581; 595-631; 640-648 AND 710-725, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-259, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Required for vesicle-mediated transport. Catalyzes the
CC       fusion of transport vesicles within the Golgi cisternae. Is also
CC       required for transport from the endoplasmic reticulum to the Golgi
CC       stack. Seem to function as a fusion protein required for the
CC       delivery of cargo proteins to all compartments of the Golgi stack
CC       independent of vesicle origin.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- SUBUNIT: Homohexamer. Interacts with GABARAP and GABARAPL2 (By
CC       similarity).
CC   -!- INTERACTION:
CC       Q62108:Dlg4; NbExp=1; IntAct=EBI-398006, EBI-300895;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM20943.1; Type=Erroneous gene model prediction;
CC       Sequence=CAM23742.1; Type=Erroneous gene model prediction;
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DR   EMBL; U10120; AAA50498.1; -; mRNA.
DR   EMBL; AK028415; BAC25937.1; -; mRNA.
DR   EMBL; AK032120; BAC27713.1; -; mRNA.
DR   EMBL; AK049281; BAC33656.1; -; mRNA.
DR   EMBL; AK051430; BAC34637.1; -; mRNA.
DR   EMBL; AK085086; BAC39361.1; -; mRNA.
DR   EMBL; AK153905; BAE32247.1; -; mRNA.
DR   EMBL; AL596108; CAM20943.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL603829; CAM20943.1; JOINED; Genomic_DNA.
DR   EMBL; AL596108; CAM20945.1; -; Genomic_DNA.
DR   EMBL; AL603829; CAM20945.1; JOINED; Genomic_DNA.
DR   EMBL; AL603829; CAM23742.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL596108; CAM23742.1; JOINED; Genomic_DNA.
DR   EMBL; AL603829; CAM23743.1; -; Genomic_DNA.
DR   EMBL; AL596108; CAM23743.1; JOINED; Genomic_DNA.
DR   EMBL; BC006627; AAH06627.1; -; mRNA.
DR   EMBL; BC019167; AAH19167.1; -; mRNA.
DR   IPI; IPI00656325; -.
DR   RefSeq; NP_032766.2; NM_008740.4.
DR   UniGene; Mm.260117; -.
DR   ProteinModelPortal; P46460; -.
DR   SMR; P46460; 1-201, 209-486, 497-742.
DR   IntAct; P46460; 14.
DR   MINT; MINT-89339; -.
DR   STRING; P46460; -.
DR   PhosphoSite; P46460; -.
DR   REPRODUCTION-2DPAGE; P46460; -.
DR   PRIDE; P46460; -.
DR   Ensembl; ENSMUST00000103075; ENSMUSP00000099364; ENSMUSG00000034187.
DR   GeneID; 18195; -.
DR   KEGG; mmu:18195; -.
DR   CTD; 18195; -.
DR   MGI; MGI:104560; Nsf.
DR   eggNOG; roNOG08218; -.
DR   GeneTree; ENSGT00530000064085; -.
DR   HOVERGEN; HBG000324; -.
DR   InParanoid; P46460; -.
DR   OrthoDB; EOG4DZ1TR; -.
DR   PhylomeDB; P46460; -.
DR   BRENDA; 3.6.4.6; 244.
DR   NextBio; 293548; -.
DR   ArrayExpress; P46460; -.
DR   Bgee; P46460; -.
DR   CleanEx; MM_NSF; -.
DR   Genevestigator; P46460; -.
DR   GermOnline; ENSMUSG00000034187; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0019905; F:syntaxin binding; IDA:MGI.
DR   GO; GO:0006813; P:potassium ion transport; IDA:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR009010; Asp_de-COase-like_fold.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR003338; ATPase_AAA_VAT_N.
DR   InterPro; IPR004201; Cell_division_protein_CDC48_2.
DR   InterPro; IPR001984; Peptidase_S16_C.
DR   Gene3D; G3DSA:2.40.40.20; Asp_decarboxylase-like_fold; 1.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF02933; CDC48_2; 1.
DR   Pfam; PF02359; CDC48_N; 1.
DR   PRINTS; PR00830; ENDOLAPTASE.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF50692; Asp_decarb_fold; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Direct protein sequencing; Hydrolase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Protein transport; Repeat; Transport.
FT   CHAIN         1    744       Vesicle-fusing ATPase.
FT                                /FTId=PRO_0000084564.
FT   NP_BIND     260    267       ATP (Potential).
FT   NP_BIND     543    550       ATP (Potential).
FT   METAL       550    550       Magnesium.
FT   MOD_RES     259    259       Phosphotyrosine.
FT   CONFLICT    300    300       A -> G (in Ref. 2; BAC39361).
FT   CONFLICT    316    326       LGANSGLHIII -> VCGHKTNLLKM (in Ref. 2;
FT                                BAC34637).
FT   CONFLICT    492    492       F -> I (in Ref. 1; AAA50498).
FT   CONFLICT    552    552       L -> V (in Ref. 1; AAA50498).
FT   CONFLICT    657    657       M -> I (in Ref. 2; BAC25937).
SQ   SEQUENCE   744 AA;  82613 MW;  BE55AD0056AD5585 CRC64;
     MAGRTMQAAR CPTDELSLSN CAVVNEKDFQ SGQHVMVRTS PNHKYIFTLR THPSVVPGCI
     AFSLPQRKWA GLSIGQDIEV ALYSFDKAKQ CIGTMTIEID FLQKKNIDSN PYDTDKMAAE
     FIQQFNNQAF SVGQQLVFSF NDKLFGLLVK DIEAMDPSIL KGEPASGKRQ KIEVGLVVGN
     SQVAFEKAEN SSLNLIGKAK TKENRQSIIN PDWNFEKMGI GGLDKEFSDI FRRAFASRVF
     PPEIVEQMGC KHVKGILLYG PPGCGKTLLA RQIGKMLNAR EPKVVNGPEI LNKYVGESEA
     NIRKLFADAE EEQRRLGANS GLHIIIFDEI DAICKQRGSM AGSTGVHDTV VNQLLSKIDG
     VEQLNNILVI GMTNRPDLID EALLRPGRLE VKMEIGLPDE KGRLQILHIH TARMRGHQLL
     SADVDIKELA VETKNFSGAE LEGLVRAAQS TAMNRHIKAS TKVEVDMEKA ESLQVTRGDF
     LASLENDIKP AFGTNQEDYA SYIMNGIIKW GDPVTRVLDD GELLVQQTKN SDRTPLVSVL
     LEGPPHSGKT ALAAKIAEES NFPFIKICSP DKMIGFSETA KCQAMKKIFD DAYKSQLSCV
     VVDDIERLLD YVPIGPRFSN LVLQALLVLL KKAPPQGRKL LIIGTTSRKD VLQEMEMLNA
     FSTTIHVPNI ATGEQLLEAL ELLGNFKDKE RTTIAQQVKG KKVWIGIKKL LMLIEMSLQM
     DPEYRVRKFL ALMREEGASP LDFD
//
ID   RB11B_MOUSE             Reviewed;         218 AA.
AC   P46638;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Ras-related protein Rab-11B;
GN   Name=Rab11b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   MEDLINE=95095258; PubMed=8001972; DOI=10.1006/geno.1994.1434;
RA   Lai F., Stubbs L., Artzt K.;
RT   "Molecular analysis of mouse Rab11b: a new type of mammalian YPT/Rab
RT   protein.";
RL   Genomics 22:610-616(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 5-24; 42-51; 62-72; 75-104; 111-125 AND 167-174,
RP   AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: GTPase that modulates endosomal trafficking. Acts as a
CC       major regulator of membrane delivery during cytokinesis (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with RAB11FIP1, RAB11FIP2, RAB11FIP3 and
CC       RAB11FIP4 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in brain, heart and
CC       testis.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR   EMBL; L26528; AAC42093.1; -; mRNA.
DR   EMBL; BC054753; AAH54753.1; -; mRNA.
DR   EMBL; BC085270; AAH85270.1; -; mRNA.
DR   IPI; IPI00135869; -.
DR   PIR; A55005; A55005.
DR   RefSeq; NP_033023.1; NM_008997.3.
DR   UniGene; Mm.387587; -.
DR   ProteinModelPortal; P46638; -.
DR   SMR; P46638; 8-188.
DR   STRING; P46638; -.
DR   PhosphoSite; P46638; -.
DR   PRIDE; P46638; -.
DR   Ensembl; ENSMUST00000057373; ENSMUSP00000110021; ENSMUSG00000077450.
DR   GeneID; 19326; -.
DR   KEGG; mmu:19326; -.
DR   UCSC; uc008bzm.1; mouse.
DR   CTD; 19326; -.
DR   MGI; MGI:99425; Rab11b.
DR   eggNOG; roNOG09728; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; P46638; -.
DR   OMA; ELAFQNI; -.
DR   OrthoDB; EOG4RR6J7; -.
DR   PhylomeDB; P46638; -.
DR   NextBio; 296291; -.
DR   ArrayExpress; P46638; -.
DR   Bgee; P46638; -.
DR   CleanEx; MM_RAB11B; -.
DR   Genevestigator; P46638; -.
DR   GermOnline; ENSMUSG00000002290; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell cycle; Cell membrane; Direct protein sequencing;
KW   GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW   Prenylation; Protein transport; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    215       Ras-related protein Rab-11B.
FT                                /FTId=PRO_0000121159.
FT   PROPEP      216    218       Removed in mature form (Potential).
FT                                /FTId=PRO_0000370816.
FT   NP_BIND      18     26       GTP (By similarity).
FT   NP_BIND      66     70       GTP (By similarity).
FT   NP_BIND     124    127       GTP (By similarity).
FT   NP_BIND     154    156       GTP (By similarity).
FT   MOTIF        40     48       Effector region (By similarity).
FT   MOD_RES       2      2       N-acetylglycine (By similarity).
FT   MOD_RES     215    215       Cysteine methyl ester (Potential).
FT   LIPID       214    214       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   LIPID       215    215       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   218 AA;  24489 MW;  8DE0A98739EBD9FF CRC64;
     MGTRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT RSIQVDGKTI
     KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHLTYE NVERWLKELR DHADSNIVIM
     LVGNKSDLRH LRAVPTDEAR AFAEKNNLSF IETSALDSTN VEEAFKNILT EIYRIVSQKQ
     IADRAAHDES PGNNVVDISV PPTTDGQRPN KLQCCQSL
//
ID   AINX_MOUSE              Reviewed;         504 AA.
AC   P46660; Q61958; Q8VCW5;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Alpha-internexin;
DE            Short=Alpha-Inx;
DE   AltName: Full=66 kDa neurofilament protein;
DE            Short=NF-66;
DE            Short=Neurofilament-66;
GN   Name=Ina;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C57BL/6 X CBA; TISSUE=Spleen;
RX   MEDLINE=95047490; PubMed=7959004; DOI=10.1016/0378-1119(94)90163-5;
RA   Chien C.-L., Liem R.K.H.;
RT   "Characterization of the mouse gene encoding the neuronal intermediate
RT   filament protein alpha-internexin.";
RL   Gene 149:289-292(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=96322433; PubMed=8734438; DOI=10.1007/BF02527709;
RA   Chan S.O., Chiu F.C.;
RT   "The 66-kDa neurofilament protein (NF-66): sequence analysis and
RT   evolution.";
RL   Neurochem. Res. 21:449-455(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 17-24; 29-39; 46-83; 92-130; 139-145; 152-177;
RP   202-210; 216-228; 270-288; 291-300; 310-316; 323-366; 378-430; 431-438
RP   AND 471-487, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Klug S., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72 AND SER-335, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452088; DOI=10.1074/mcp.T500040-MCP200;
RA   Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G.,
RA   Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F.,
RA   Maltby D.A., Schoepfer R., Burlingame A.L.;
RT   "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT   preparations using lectin weak affinity chromatography and mass
RT   spectrometry.";
RL   Mol. Cell. Proteomics 5:923-934(2006).
CC   -!- FUNCTION: Class-IV neuronal intermediate filament that is able to
CC       self-assemble. It is involved in the morphogenesis of neurons. It
CC       may form an independent structural network without the involvement
CC       of other neurofilaments or it may cooperate with NF-L to form the
CC       filamentous backbone to which NF-M and NF-H attach to form the
CC       cross-bridges (By similarity).
CC   -!- PTM: O-glycosylated.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC   -----------------------------------------------------------------------
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DR   EMBL; L27220; AAA62617.1; -; Genomic_DNA.
DR   EMBL; L36390; AAB37740.1; -; mRNA.
DR   EMBL; BC018383; AAH18383.1; -; mRNA.
DR   IPI; IPI00135965; -.
DR   PIR; I53868; I53868.
DR   RefSeq; NP_666212.3; NM_146100.4.
DR   UniGene; Mm.276251; -.
DR   ProteinModelPortal; P46660; -.
DR   SMR; P46660; 92-129, 133-241, 259-329, 333-402.
DR   MINT; MINT-136763; -.
DR   STRING; P46660; -.
DR   PhosphoSite; P46660; -.
DR   UCD-2DPAGE; P46660; -.
DR   PRIDE; P46660; -.
DR   Ensembl; ENSMUST00000037636; ENSMUSP00000041347; ENSMUSG00000034336.
DR   GeneID; 226180; -.
DR   KEGG; mmu:226180; -.
DR   UCSC; uc008huk.1; mouse.
DR   CTD; 226180; -.
DR   MGI; MGI:96568; Ina.
DR   eggNOG; roNOG10691; -.
DR   HOGENOM; HBG715391; -.
DR   HOVERGEN; HBG013015; -.
DR   InParanoid; P46660; -.
DR   OrthoDB; EOG4R5031; -.
DR   NextBio; 378052; -.
DR   ArrayExpress; P46660; -.
DR   Bgee; P46660; -.
DR   Genevestigator; P46660; -.
DR   GermOnline; ENSMUSG00000034336; Mus musculus.
DR   GO; GO:0005883; C:neurofilament; IDA:MGI.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0060052; P:neurofilament cytoskeleton organization; IGI:MGI.
DR   InterPro; IPR016044; F.
DR   InterPro; IPR001664; IF.
DR   InterPro; IPR006821; Intermed_filament_DNA-bd.
DR   InterPro; IPR018039; Intermediate_filament_CS.
DR   PANTHER; PTHR23239; IF; 1.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF04732; Filament_head; 1.
DR   PROSITE; PS00226; IF; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Developmental protein; Differentiation;
KW   Direct protein sequencing; Glycoprotein; Intermediate filament;
KW   Neurogenesis; Phosphoprotein.
FT   CHAIN         1    504       Alpha-internexin.
FT                                /FTId=PRO_0000063784.
FT   REGION        1     87       Head.
FT   REGION       88    408       Rod.
FT   REGION       88    129       Coil 1A.
FT   REGION      130    142       Linker 1.
FT   REGION      143    238       Coil 1B.
FT   REGION      239    262       Linker 2.
FT   REGION      263    408       Coil 2.
FT   REGION      409    504       Tail.
FT   COMPBIAS    449    458       Poly-Glu.
FT   MOD_RES      72     72       Phosphoserine.
FT   MOD_RES     290    290       N6-acetyllysine (By similarity).
FT   MOD_RES     335    335       Phosphoserine.
FT   MOD_RES     501    501       Phosphoserine (By similarity).
FT   CONFLICT     28     28       R -> P (in Ref. 2; AAB37740).
FT   CONFLICT     34     34       G -> A (in Ref. 2; AAB37740).
FT   CONFLICT    141    141       E -> Q (in Ref. 2; AAB37740).
FT   CONFLICT    147    147       L -> R (in Ref. 2; AAB37740).
FT   CONFLICT    163    163       Q -> E (in Ref. 1; AAA62617).
FT   CONFLICT    297    297       Q -> L (in Ref. 2; AAB37740).
FT   CONFLICT    301    301       S -> T (in Ref. 2; AAB37740).
FT   CONFLICT    318    319       QL -> HV (in Ref. 2; AAB37740).
FT   CONFLICT    347    347       H -> D (in Ref. 1; AAA62617).
FT   CONFLICT    383    383       L -> F (in Ref. 1; AAA62617).
FT   CONFLICT    388    388       A -> G (in Ref. 1; AAA62617).
FT   CONFLICT    403    403       E -> N (in Ref. 2; AAB37740).
FT   CONFLICT    442    443       AG -> TR (in Ref. 1; AAA62617).
FT   CONFLICT    442    442       A -> T (in Ref. 2; AAB37740).
FT   CONFLICT    449    451       Missing (in Ref. 3; AAH18383).
FT   CONFLICT    454    456       Missing (in Ref. 2).
FT   CONFLICT    459    459       D -> E (in Ref. 3; AAH18383).
FT   CONFLICT    492    492       S -> L (in Ref. 2; AAB37740).
SQ   SEQUENCE   504 AA;  55742 MW;  910F89E93260E3B6 CRC64;
     MSFGSEHYLC SASSYRKVFG DSSRLSARLS GPGGSGSFRS QSLSRSNVAS TAACSSASSL
     GLGLAYRRLP ASDGLDLSQA AARTNEYKII RTNEKEQLQG LNDRFAVFIE KVHQLETQNR
     ALEAELAALR QRHAEPSRVG ELFQRELREL RAQLEEASSA RAQALLERDG LAEEVQRLRA
     RCEEESRGRE GAERALKAQQ RDVDGATLAR LDLEKKVESL LDELAFVRQV HDEEVAELLA
     TLQASSQAAA EVDVAVAKPD LTSALREIRA QYESLAAKNL QSAEEWYKSK FANLNEQAAR
     STEAIRASRE EIHEYRRQLQ ARTIEIEGLR GANESLERQI LELEERHSAE VAGYQDSIGQ
     LESDLRNTKS EMARHLREYQ DLLNVKMALD IEIAAYRKLL EGEETRFSTG GLSISGLNPL
     PNPSYLLPPR ILSSTASKVS SAGLSLKKED EEEEEEEEDA SKEVSKKTSK VGEGFEETLG
     EAVISTKKTG KSATEESTSS SQKM
//
ID   NEDD4_MOUSE             Reviewed;         887 AA.
AC   P46935; O08758; Q3UZI2; Q8BGB3;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2003, sequence version 3.
DT   08-MAR-2011, entry version 111.
DE   RecName: Full=E3 ubiquitin-protein ligase NEDD4;
DE            EC=6.3.2.-;
DE   AltName: Full=Neural precursor cell expressed developmentally down-regulated protein 4;
DE            Short=NEDD-4;
GN   Name=Nedd4; Synonyms=Kiaa0093, Nedd-4, Nedd4-1, Nedd4a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RX   MEDLINE=92328780; PubMed=1378265; DOI=10.1016/0006-291X(92)91747-E;
RA   Kumar S., Tomooka Y., Noda M.;
RT   "Identification of a set of genes with developmentally down-regulated
RT   expression in the mouse brain.";
RL   Biochem. Biophys. Res. Commun. 185:1155-1161(1992).
RN   [2]
RP   SEQUENCE REVISION.
RA   Kumar S.;
RL   Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH
RP   UBE2D2.
RC   STRAIN=C57BL/6 X CBA;
RX   MEDLINE=97326076; PubMed=9182527; DOI=10.1074/jbc.272.24.15085;
RA   Hatakeyama S., Jensen J.P., Weissman A.M.;
RT   "Subcellular localization and ubiquitin-conjugating enzyme (E2)
RT   interactions of mammalian HECT family ubiquitin protein ligases.";
RL   J. Biol. Chem. 272:15085-15092(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [6]
RP   INTERACTION WITH ENAH.
RX   MEDLINE=98070482; PubMed=9407065; DOI=10.1074/jbc.272.52.32869;
RA   Ermekova K.S., Zambrano N., Linn H., Minopoli G., Gertler F.,
RA   Russo T., Sudol M.;
RT   "The WW domain of neural protein FE65 interacts with proline-rich
RT   motifs in Mena, the mammalian homolog of Drosophila enabled.";
RL   J. Biol. Chem. 272:32869-32877(1997).
RN   [7]
RP   INTERACTION WITH BEAN1; LITAF; RNF11; WBP1; WBP2; TMEPAI; NDFIP1 AND
RP   PRRG2, AND DOMAINS.
RC   TISSUE=Embryo;
RX   MEDLINE=20498735; PubMed=11042109; DOI=10.1042/0264-6021:3510557;
RA   Jolliffe C.N., Harvey K.F., Haines B.P., Parasivam G., Kumar S.;
RT   "Identification of multiple proteins expressed in murine embryos as
RT   binding partners for the WW domains of the ubiquitin-protein ligase
RT   Nedd4.";
RL   Biochem. J. 351:557-565(2000).
RN   [8]
RP   INTERACTION WITH GRB10.
RX   PubMed=12697834; DOI=10.1128/MCB.23.9.3363-3372.2003;
RA   Vecchione A., Marchese A., Henry P., Rotin D., Morrione A.;
RT   "The Grb10/Nedd4 complex regulates ligand-induced ubiquitination and
RT   stability of the insulin-like growth factor I receptor.";
RL   Mol. Cell. Biol. 23:3363-3372(2003).
RN   [9]
RP   FUNCTION, INTERACTION WITH GRB10, AND MUTAGENESIS OF CYS-854.
RX   PubMed=15060076; DOI=10.1074/jbc.M311802200;
RA   Murdaca J., Treins C., Monthouel-Kartmann M.N., Pontier-Bres R.,
RA   Kumar S., Van Obberghen E., Giorgetti-Peraldi S.;
RT   "Grb10 prevents Nedd4-mediated vascular endothelial growth factor
RT   receptor-2 degradation.";
RL   J. Biol. Chem. 279:26754-26761(2004).
RN   [10]
RP   INTERACTION WITH MURINE LEUKEMIA VIRUS GAG POLYPROTEIN.
RX   PubMed=15908698; DOI=10.1074/jbc.M413735200;
RA   Segura-Morales C., Pescia C., Chatellard-Causse C., Sadoul R.,
RA   Bertrand E., Basyuk E.;
RT   "Tsg101 and Alix interact with murine leukemia virus Gag and cooperate
RT   with Nedd4 ubiquitin ligases during budding.";
RL   J. Biol. Chem. 280:27004-27012(2005).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [13]
RP   FUNCTION, INTERACTION WITH GRB10, AND SUBCELLULAR LOCATION.
RX   PubMed=18286479; DOI=10.1002/jcp.21405;
RA   Monami G., Emiliozzi V., Morrione A.;
RT   "Grb10/Nedd4-mediated multiubiquitination of the insulin-like growth
RT   factor receptor regulates receptor internalization.";
RL   J. Cell. Physiol. 216:426-437(2008).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287 AND SER-309, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [15]
RP   FUNCTION IN UBIQUITINATION OF ERBB4, AND INTERACTION WITH ERBB4.
RX   PubMed=19193720; DOI=10.1096/fj.08-121947;
RA   Zeng F., Xu J., Harris R.C.;
RT   "Nedd4 mediates ErbB4 JM-a/CYT-1 ICD ubiquitination and degradation in
RT   MDCK II cells.";
RL   FASEB J. 23:1935-1945(2009).
RN   [16]
RP   FUNCTION IN UBIQUITINATION OF ERBB4, INTERACTION WITH ERBB4, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=19047365; DOI=10.1128/MCB.00595-08;
RA   Feng S.M., Muraoka-Cook R.S., Hunter D., Sandahl M.A., Caskey L.S.,
RA   Miyazawa K., Atfi A., Earp H.S. III;
RT   "The E3 ubiquitin ligase WWP1 selectively targets HER4 and its
RT   proteolytically derived signaling isoforms for degradation.";
RL   Mol. Cell. Biol. 29:892-906(2009).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287 AND SER-309, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [18]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH RAP2A AND TNIK.
RX   PubMed=20159449; DOI=10.1016/j.neuron.2010.01.007;
RA   Kawabe H., Neeb A., Dimova K., Young S.M. Jr., Takeda M.,
RA   Katsurabayashi S., Mitkovski M., Malakhova O.A., Zhang D.E.,
RA   Umikawa M., Kariya K., Goebbels S., Nave K.A., Rosenmund C., Jahn O.,
RA   Rhee J., Brose N.;
RT   "Regulation of Rap2A by the ubiquitin ligase Nedd4-1 controls neurite
RT   development.";
RL   Neuron 65:358-372(2010).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from
CC       an E2 ubiquitin-conjugating enzyme in the form of a thioester and
CC       then directly transfers the ubiquitin to targeted substrates.
CC       Monoubiquitinates IGF1R at multiple sites, thus leading to
CC       receptor internalization and degradation in lysosomes. Involved in
CC       ubiquitination of ERBB4 intracellular domain E4ICD1
CC       (PubMed:19193720). Predominantly involved in ubiquitination of
CC       membrane bound forms of ERBB4 rather than processed precursors and
CC       intermediate membrane-anchored 80 kDa fragments (m80HER4), with a
CC       lesser role in ubiquitination of ERBB4 intracellular domain E4ICD1
CC       (PubMed:19047365). Involved in the pathway leading to the
CC       degradation of VEGFR-2/KDFR, independently of its ubiquitin-ligase
CC       activity. Part of a signaling complex composed of NEDD4, RAP2A and
CC       TNIK which regulates neuronal dendrite extension and arborization
CC       during development.
CC   -!- ENZYME REGULATION: Activated by NDFIP1- and NDFIP2-binding (By
CC       similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Binds SCNN1A, SCNN1B and SCNN1G. Interacts with NDFIP1
CC       and NDFIP2; this interaction activates the E3 ubiquitin-protein
CC       ligase and may induce its recruitment to exosomes. Interacts with
CC       UBE2D2. Binds, in vitro, through the WW2 and WW3 domains, to
CC       neural isoforms of ENAH that contain the PPSY motif. Interacts
CC       with BEAN1, LITAF, RNF11, WBP1, WBP2, TMEPAI and PRRG2. Interacts
CC       with murine leukemia virus Gag polyprotein (via PPXY motif).
CC       Interacts with GRB10. Interacts with ERBB4. Interacts with TNIK;
CC       the interaction is direct, allows the TNIK-dependent recruitment
CC       of RAP2A and its ubiquitination by NEDD4.
CC   -!- INTERACTION:
CC       Q60760:Grb10; NbExp=4; IntAct=EBI-773516, EBI-861810;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral
CC       membrane protein. Note=Recruited to the plasma membrane by GRB10.
CC       Once complexed with GRB10 and IGF1R, follows IGF1R
CC       internalization, remaining associated with early endosomes.
CC       Uncouples from IGF1R-containing endosomes before the sorting of
CC       the receptor to the lysosomal compartment (By similarity). May be
CC       recruited to exosomes by NDFIP1.
CC   -!- TISSUE SPECIFICITY: Brain.
CC   -!- DOMAIN: The WW domains mediate interaction with LITAF, RNF11,
CC       WBP1, WBP2, TMEPAI, NDFIP1 and PRRG2.
CC   -!- PTM: Auto-ubiquitinated (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Lethal during late gestation. Embryos show a
CC       retarded development and defects in vasculogenesis and
CC       angiogenesis.
CC   -!- MISCELLANEOUS: A cysteine residue is required for ubiquitin-
CC       thioester formation.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 HECT (E6AP-type E3 ubiquitin-protein
CC       ligase) domain.
CC   -!- SIMILARITY: Contains 3 WW domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB63360.1; Type=Frameshift; Positions=12;
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DR   EMBL; D85414; BAA12803.1; -; mRNA.
DR   EMBL; U96635; AAB63360.1; ALT_FRAME; mRNA.
DR   EMBL; AK088620; BAC40458.1; -; mRNA.
DR   EMBL; AK088767; BAC40558.1; -; mRNA.
DR   EMBL; AK122203; BAC65485.1; -; mRNA.
DR   EMBL; AK133838; BAE21875.1; -; mRNA.
DR   IPI; IPI00462445; -.
DR   RefSeq; NP_035020.2; NM_010890.3.
DR   UniGene; Mm.279923; -.
DR   PDB; 3M7F; X-ray; 2.00 A; B=71-246.
DR   PDBsum; 3M7F; -.
DR   ProteinModelPortal; P46935; -.
DR   SMR; P46935; 71-246, 250-281, 347-500, 508-882.
DR   DIP; DIP-32323N; -.
DR   IntAct; P46935; 8.
DR   MINT; MINT-90132; -.
DR   STRING; P46935; -.
DR   PhosphoSite; P46935; -.
DR   PRIDE; P46935; -.
DR   Ensembl; ENSMUST00000034740; ENSMUSP00000034740; ENSMUSG00000032216.
DR   GeneID; 17999; -.
DR   KEGG; mmu:17999; -.
DR   UCSC; uc009qqe.1; mouse.
DR   CTD; 17999; -.
DR   MGI; MGI:97297; Nedd4.
DR   HOGENOM; HBG607874; -.
DR   HOVERGEN; HBG004134; -.
DR   InParanoid; P46935; -.
DR   OMA; VDVPLYP; -.
DR   OrthoDB; EOG4P5K8F; -.
DR   PhylomeDB; P46935; -.
DR   NextBio; 292995; -.
DR   ArrayExpress; P46935; -.
DR   Bgee; P46935; -.
DR   Genevestigator; P46935; -.
DR   GermOnline; ENSMUSG00000032216; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IPI:MGI.
DR   GO; GO:0050815; F:phosphoserine binding; IDA:BHF-UCL.
DR   GO; GO:0050816; F:phosphothreonine binding; IDA:BHF-UCL.
DR   GO; GO:0070064; F:proline-rich region binding; IPI:MGI.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IDA:MGI.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:MGI.
DR   GO; GO:0010766; P:negative regulation of sodium ion transport; IDA:MGI.
DR   GO; GO:0030948; P:negative regulation of vascular endothelial growth factor receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:MGI.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:UniProtKB.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR000569; HECT.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00397; WW; 3.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00456; WW; 3.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF56204; HECT; 1.
DR   SUPFAM; SSF51045; WW_Rsp5_WWP; 3.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 3.
DR   PROSITE; PS50020; WW_DOMAIN_2; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Cytoplasm; Ligase; Membrane;
KW   Neurogenesis; Phosphoprotein; Repeat; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   CHAIN         1    887       E3 ubiquitin-protein ligase NEDD4.
FT                                /FTId=PRO_0000120320.
FT   DOMAIN       65    166       C2.
FT   DOMAIN      249    282       WW 1.
FT   DOMAIN      405    438       WW 2.
FT   DOMAIN      460    493       WW 3.
FT   DOMAIN      552    887       HECT.
FT   REGION      217    549       Mediates interaction with TNIK.
FT   ACT_SITE    854    854       Glycyl thioester intermediate.
FT   MOD_RES     287    287       Phosphothreonine.
FT   MOD_RES     309    309       Phosphoserine; by host.
FT   MOD_RES     385    385       Phosphoserine; by host (By similarity).
FT   MUTAGEN     854    854       C->S: Loss of ubiquitin-ligase activity.
FT                                No effect on VEGFR-2/KDFR degradation.
SQ   SEQUENCE   887 AA;  102706 MW;  AE7DD3ED63986C50 CRC64;
     MSSDMAADES EAPVLSEDEV WEFCLDKTED GGGSPGSDVT DTCEPPCGCW ELNPNSLEEE
     HVLFTADPYL ELHNDDTRVV RVKVIAGIGL AKKDILGASD PYVRVTLYDP MSGILTSVQT
     KTIKKSLNPK WNEEILFRVL PQRHRILFEV FDENRLTRDD FLGQVDVPLY PLPTENPRME
     RPYTFKDFVL HPRSHKSRVK GYLRLKMTYL PKNGSEDENA DQAEELEPGW VVLDQPDAAT
     HLPHPPEPSP LPPGWEERQD VLGRTYYVNH ESRRTQWKRP SPDDDLTDED NDDMQLQAQR
     AFTTRRQISE DVDGPDNRES PENWEIVRED ENTEYSGQAV QSPPSGHIDV QTHLAEEFNT
     RLAVCGNPAT SQPVTSSNHS SRGGSLQTCI FEEQPTLPVL LPTSSGLPPG WEEKQDDRGR
     SYYVDHNSKT TTWSKPTMQD DPRSKIPAHL RGKTDSNDLG PLPPGWEERT HTDGRVFFIN
     HNIKKTQWED PRLQNVAITG PAVPYSRDYK RKYEFFRRKL KKQTDIPNKF EMKLRRANIL
     EDSYRRIMGV KRADLLKARL WIEFDGEKGL DYGGVAREWF FLISKEMFNP YYGLFEYSAT
     DNYTLQINPN SGLCNEDHLS YFKFIGRVAG MAVYHGKLLD GFFIRPFYKM MLQKLITLHD
     MESVDSEYYS SLRWILENDP TELDLRFIID EELFGQTHQH ELKTGGSEIV VTNKNKKEYI
     YLVIQWRFVN RIQKQMAAFK EGFFELIPQD LIKIFDENEL ELLMCGLGDV DVNDWREHTK
     YKNGYSMNHQ VIHWFWKAVW MMDSEKRIRL LQFVTGTSRV PMNGFAELYG SNGPQSFTVE
     QWGTPDKLPR AHTCFNRLDL PPYESFDELW DKLQMAIENT QGFDGVD
//
ID   YAP1_MOUSE              Reviewed;         488 AA.
AC   P46938; Q52KJ5; Q91WL1;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   08-FEB-2011, entry version 85.
DE   RecName: Full=Yorkie homolog;
DE   AltName: Full=65 kDa Yes-associated protein;
DE            Short=YAP65;
GN   Name=Yap1; Synonyms=Yap, Yap65;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=NIH Swiss; TISSUE=Embryo;
RX   MEDLINE=95301570; PubMed=7782338; DOI=10.1074/jbc.270.24.14733;
RA   Sudol M., Bork P., Einbond A., Kastury K., Druck T., Negrini M.,
RA   Huebner K., Lehman D.;
RT   "Characterization of the mammalian YAP (Yes-associated protein) gene
RT   and its role in defining a novel protein module, the WW domain.";
RL   J. Biol. Chem. 270:14733-14741(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX   PubMed=12807903; DOI=10.1074/jbc.M305597200;
RA   Komuro A., Nagai M., Navin N.E., Sudol M.;
RT   "WW domain-containing protein YAP associates with ErbB-4 and acts as a
RT   co-transcriptional activator for the carboxyl-terminal fragment of
RT   ErbB-4 that translocates to the nucleus.";
RL   J. Biol. Chem. 278:33334-33341(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=129, C57BL/6, and FVB/N;
RC   TISSUE=Brain, Kidney, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH WBP1 AND WBP2.
RX   MEDLINE=95372370; PubMed=7644498; DOI=10.1073/pnas.92.17.7819;
RA   Chen H.I., Sudol M.;
RT   "The WW domain of Yes-associated protein binds a proline-rich ligand
RT   that differs from the consensus established for Src homology 3-binding
RT   modules.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:7819-7823(1995).
RN   [6]
RP   INTERACTION WITH ENAH.
RX   MEDLINE=98070482; PubMed=9407065; DOI=10.1074/jbc.272.52.32869;
RA   Ermekova K.S., Zambrano N., Linn H., Minopoli G., Gertler F.,
RA   Russo T., Sudol M.;
RT   "The WW domain of neural protein FE65 interacts with proline-rich
RT   motifs in Mena, the mammalian homolog of Drosophila enabled.";
RL   J. Biol. Chem. 272:32869-32877(1997).
RN   [7]
RP   IDENTIFICATION OF ISOFORMS LACKING THE TRANSCRIPTIONAL ACTIVATION
RP   DOMAIN, AND TISSUE SPECIFICITY.
RX   PubMed=16461361; DOI=10.1083/jcb.200509132;
RA   Hoshino M., Qi M.-L., Yoshimura N., Tagawa K., Wada Y.-I., Enokido Y.,
RA   Marubuchi S., Harjes P., Arai N., Oyanagi K., Blandino G., Sudol M.,
RA   Rich T., Kanazawa I., Wanker E.E., Saitoe M., Okazawa H.;
RT   "Transcriptional repression induces a slowly progressive atypical
RT   neuronal death associated with changes of YAP isoforms and p73.";
RL   J. Cell Biol. 172:589-604(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112 AND SER-113, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [11]
RP   INTERACTION WITH TEAD4, AND X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF
RP   47-85 IN COMPLEX WITH TEAD4.
RX   PubMed=20123908; DOI=10.1101/gad.1865310;
RA   Chen L., Chan S.W., Zhang X., Walsh M., Lim C.J., Hong W., Song H.;
RT   "Structural basis of YAP recognition by TEAD4 in the hippo pathway.";
RL   Genes Dev. 24:290-300(2010).
CC   -!- FUNCTION: Transcriptional regulator which can act both as a
CC       coactivator and a corepressor and is the critical downstream
CC       regulatory target in the Hippo signaling pathway that plays a
CC       pivotal role in organ size control and tumor suppression by
CC       restricting proliferation and promoting apoptosis. The core of
CC       this pathway is composed of a kinase cascade wherein MST1/MST2, in
CC       complex with its regulatory protein SAV1, phosphorylates and
CC       activates LATS1/2 in complex with its regulatory protein MOB1,
CC       which in turn phosphorylates and inactivates YAP1 oncoprotein and
CC       WWTR1/TAZ. Plays a key role to control cell proliferation in
CC       response to cell contact. Phosphorylation of YAP1 by LATS1/2
CC       inhibits its translocation into the nucleus to regulate cellular
CC       genes important for cell proliferation, cell death, and cell
CC       migration. The presence of TEAD transcription factors are required
CC       for it to stimulate gene expression, cell growth, anchorage-
CC       independent growth, and epithelial mesenchymal transition (EMT)
CC       induction (By similarity).
CC   -!- SUBUNIT: Binds to the SH3 domain of the YES kinase. Binds to WBP1
CC       and WBP2. Binds, in vitro, through the WW1 domain, to neural
CC       isoforms of ENAH that contain the PPSY motif. The phosphorylated
CC       form interacts with YWHAB. Interacts (via WW domains) with LATS1
CC       (via PPxY motif 2). Interacts with LATS2. Interacts (via WW domain
CC       1) with isoform JM-A of ERBB4 (via PPxY motif 2). Interacts with
CC       TEAD1, TEAD2 and TEAD3 (By similarity). Interacts with TP73 (By
CC       similarity). Interacts with RUNX1 (By similarity). Interacts with
CC       TEAD4.
CC   -!- INTERACTION:
CC       Q9EPK5:Wwtr1; NbExp=1; IntAct=EBI-1211949, EBI-1211920;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Both phosphorylation and cell density can
CC       regulate its subcellular localization. Phosphorylation sequesters
CC       it in the cytoplasm by inhibiting its translocation into the
CC       nucleus. At low density, predominantly nuclear and is translocated
CC       to the cytoplasm at high density (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms lacking the transactivation domain
CC         exist;
CC       Name=1; Synonyms=YAP2L;
CC         IsoId=P46938-1; Sequence=Displayed;
CC       Name=2; Synonyms=YAP2;
CC         IsoId=P46938-2; Sequence=VSP_039056;
CC   -!- TISSUE SPECIFICITY: Isoforms lacking the transactivation domain
CC       seen in striatal neurons (at protein level). Ubiquitous. Isoform 2
CC       is expressed at higher levels in the neural tissues.
CC   -!- PTM: Phosphorylated by LATS1 and LATS2; leading to cytoplasmic
CC       translocation and inactivation. Phosphorylated by ABL1; leading to
CC       YAP1 stabilization, enhanced interaction with TP73 and recruitment
CC       onto proapoptotic genes; in response to DNA damage (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the YORKIE family.
CC   -!- SIMILARITY: Contains 2 WW domains.
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DR   EMBL; X80508; CAA56673.1; -; mRNA.
DR   EMBL; CH466522; EDL24950.1; -; Genomic_DNA.
DR   EMBL; BC014733; AAH14733.1; -; mRNA.
DR   EMBL; BC039125; AAH39125.1; -; mRNA.
DR   EMBL; BC094313; AAH94313.1; -; mRNA.
DR   IPI; IPI00108989; -.
DR   IPI; IPI00621717; -.
DR   PIR; B56954; B56954.
DR   RefSeq; NP_001164618.1; NM_001171147.1.
DR   RefSeq; NP_033560.1; NM_009534.3.
DR   UniGene; Mm.221992; -.
DR   PDB; 3JUA; X-ray; 3.00 A; B/D/F/H=47-85.
DR   PDBsum; 3JUA; -.
DR   ProteinModelPortal; P46938; -.
DR   SMR; P46938; 47-85, 150-247.
DR   IntAct; P46938; 3.
DR   MINT; MINT-85211; -.
DR   STRING; P46938; -.
DR   PhosphoSite; P46938; -.
DR   PRIDE; P46938; -.
DR   Ensembl; ENSMUST00000086580; ENSMUSP00000083772; ENSMUSG00000053110.
DR   GeneID; 22601; -.
DR   KEGG; mmu:22601; -.
DR   UCSC; uc009ode.1; mouse.
DR   CTD; 22601; -.
DR   MGI; MGI:103262; Yap1.
DR   eggNOG; roNOG11028; -.
DR   HOVERGEN; HBG002748; -.
DR   OMA; QSSYEIP; -.
DR   NextBio; 302957; -.
DR   ArrayExpress; P46938; -.
DR   Bgee; P46938; -.
DR   CleanEx; MM_YAP1; -.
DR   Genevestigator; P46938; -.
DR   GermOnline; ENSMUSG00000053110; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005667; C:transcription factor complex; IGI:MGI.
DR   GO; GO:0070064; F:proline-rich region binding; IPI:MGI.
DR   GO; GO:0016563; F:transcription activator activity; IGI:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Pfam; PF00397; WW; 2.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF51045; WW_Rsp5_WWP; 2.
DR   PROSITE; PS01159; WW_DOMAIN_1; 2.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; Cytoplasm; Nucleus;
KW   Phosphoprotein; Proto-oncogene; Repeat; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    488       Yorkie homolog.
FT                                /FTId=PRO_0000076072.
FT   DOMAIN      156    189       WW 1.
FT   DOMAIN      215    248       WW 2.
FT   REGION      276    488       Transactivation domain.
FT   COMPBIAS      3     34       Pro-rich.
FT   MOD_RES      46     46       Phosphoserine; by LATS1 and LATS2 (By
FT                                similarity).
FT   MOD_RES      94     94       Phosphoserine; by LATS1 and LATS2 (By
FT                                similarity).
FT   MOD_RES      95     95       Phosphothreonine (By similarity).
FT   MOD_RES     112    112       Phosphoserine; by LATS1 and LATS2 (By
FT                                similarity).
FT   MOD_RES     113    113       Phosphoserine.
FT   MOD_RES     116    116       Phosphoserine (By similarity).
FT   MOD_RES     123    123       Phosphoserine (By similarity).
FT   MOD_RES     128    128       Phosphothreonine (By similarity).
FT   MOD_RES     134    134       Phosphoserine (By similarity).
FT   MOD_RES     149    149       Phosphoserine; by LATS1 and LATS2 (By
FT                                similarity).
FT   MOD_RES     261    261       Phosphoserine (By similarity).
FT   MOD_RES     274    274       Phosphoserine (By similarity).
FT   MOD_RES     352    352       Phosphoserine (By similarity).
FT   MOD_RES     356    356       Phosphoserine.
FT   MOD_RES     382    382       Phosphoserine; by LATS1 and LATS2 (By
FT                                similarity).
FT   MOD_RES     392    392       Phosphotyrosine; by ABL1 (By similarity).
FT   VAR_SEQ     313    328       Missing (in isoform 2).
FT                                /FTId=VSP_039056.
FT   HELIX        51     58
FT   STRAND       61     63
FT   HELIX        71     73
FT   HELIX        79     81
SQ   SEQUENCE   488 AA;  52383 MW;  5A2221B74B1400F9 CRC64;
     MEPAQQPPPQ PAPQGPAPPS VSPAGTPAAP PAPPAGHQVV HVRGDSETDL EALFNAVMNP
     KTANVPQTVP MRLRKLPDSF FKPPEPKSHS RQASTDAGTA GALTPQHVRA HSSPASLQLG
     AVSPGTLTAS GVVSGPAAAP AAQHLRQSSF EIPDDVPLPA GWEMAKTSSG QRYFLNHNDQ
     TTTWQDPRKA MLSQLNVPAP ASPAVPQTLM NSASGPLPDG WEQAMTQDGE VYYINHKNKT
     TSWLDPRLDP RFAMNQRITQ SAPVKQPPPL APQSPQGGVL GGGSSNQQQQ IQLQQLQMEK
     ERLRLKQQEL FRQAIRNINP STANAPKCQE LALRSQLPTL EQDGGTPNAV SSPGMSQELR
     TMTTNSSDPF LNSGTYHSRD ESTDSGLSMS SYSIPRTPDD FLNSVDEMDT GDTISQSTLP
     SQQSRFPDYL EALPGTNVDL GTLEGDAMNI EGEELMPSLQ EALSSEILDV ESVLAATKLD
     KESFLTWL
//
ID   GALA_MOUSE              Reviewed;         124 AA.
AC   P47212;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Galanin;
DE   Contains:
DE     RecName: Full=Galanin;
DE   Contains:
DE     RecName: Full=Galanin message-associated peptide;
DE              Short=GMAP;
DE   Flags: Precursor;
GN   Name=Gal; Synonyms=Galn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129; TISSUE=Liver;
RX   MEDLINE=97136692; PubMed=8982069; DOI=10.1016/S0378-1119(96)00477-5;
RA   Kofler B., Liu M.L., Jacoby A.S., Shine J., Iismaa T.P.;
RT   "Molecular cloning and characterisation of the mouse preprogalanin
RT   gene.";
RL   Gene 182:71-75(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 26-124.
RC   TISSUE=Hypothalamus;
RX   PubMed=8614559; DOI=10.1016/0304-3940(95)12094-K;
RA   Lundkvist J., Land T., Kahl U., Bedecs K., Bartfai T.;
RT   "cDNA sequence, ligand biding, and regulation of galanin/GMAP in mouse
RT   brain.";
RL   Neurosci. Lett. 200:121-124(1995).
CC   -!- FUNCTION: Contracts smooth muscle of the gastrointestinal and
CC       genitourinary tract, regulates growth hormone release, modulates
CC       insulin release, and may be involved in the control of adrenal
CC       secretion.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the galanin family.
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DR   EMBL; L38580; AAB41545.1; -; Genomic_DNA.
DR   EMBL; L38576; AAB41545.1; JOINED; Genomic_DNA.
DR   EMBL; L38577; AAB41545.1; JOINED; Genomic_DNA.
DR   EMBL; L38578; AAB41545.1; JOINED; Genomic_DNA.
DR   EMBL; L38579; AAB41545.1; JOINED; Genomic_DNA.
DR   EMBL; BC044055; AAH44055.1; -; mRNA.
DR   EMBL; Z23069; CAA80610.1; -; mRNA.
DR   IPI; IPI00135641; -.
DR   PIR; JC5480; JC5480.
DR   PIR; S34301; S34301.
DR   RefSeq; NP_034383.1; NM_010253.3.
DR   UniGene; Mm.4655; -.
DR   STRING; P47212; -.
DR   PhosphoSite; P47212; -.
DR   PRIDE; P47212; -.
DR   Ensembl; ENSMUST00000025842; ENSMUSP00000025842; ENSMUSG00000024907.
DR   GeneID; 14419; -.
DR   KEGG; mmu:14419; -.
DR   UCSC; uc008fwj.1; mouse.
DR   CTD; 14419; -.
DR   MGI; MGI:95637; Gal.
DR   eggNOG; roNOG17170; -.
DR   HOGENOM; HBG269505; -.
DR   HOVERGEN; HBG005799; -.
DR   InParanoid; P47212; -.
DR   OMA; NHRSFSD; -.
DR   OrthoDB; EOG43N7F9; -.
DR   PhylomeDB; P47212; -.
DR   NextBio; 286005; -.
DR   ArrayExpress; P47212; -.
DR   Bgee; P47212; -.
DR   CleanEx; MM_GAL; -.
DR   Genevestigator; P47212; -.
DR   GermOnline; ENSMUSG00000024907; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IMP:MGI.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IMP:MGI.
DR   InterPro; IPR008174; Galanin.
DR   InterPro; IPR008175; Galanin_pre.
DR   InterPro; IPR013068; GMAP.
DR   Pfam; PF01296; Galanin; 1.
DR   Pfam; PF06540; GMAP; 1.
DR   PRINTS; PR00273; GALANIN.
DR   ProDom; PD005962; Galanin; 1.
DR   ProDom; PD012185; GMAP; 1.
DR   SMART; SM00071; Galanin; 1.
DR   PROSITE; PS00861; GALANIN; 1.
PE   2: Evidence at transcript level;
KW   Amidation; Cleavage on pair of basic residues; Hormone; Neuropeptide;
KW   Secreted; Signal.
FT   SIGNAL        1     19       Potential.
FT   PROPEP       20     30       By similarity.
FT                                /FTId=PRO_0000010451.
FT   PEPTIDE      33     61       Galanin (By similarity).
FT                                /FTId=PRO_0000010452.
FT   PEPTIDE      65    124       Galanin message-associated peptide (By
FT                                similarity).
FT                                /FTId=PRO_0000010453.
FT   MOD_RES      61     61       Threonine amide (By similarity).
SQ   SEQUENCE   124 AA;  13471 MW;  B49B03B60FACEFD7 CRC64;
     MARGSVILLG WLLLVVTLSA TLGLGMPAKE KRGWTLNSAG YLLGPHAIDN HRSFSDKHGL
     TGKRELQLEV EERRPGSVDV PLPESNIVRT IMEFLSFLHL KEAGALDSLP GIPLATSSED
     LEKS
//
ID   RP3A_MOUSE              Reviewed;         681 AA.
AC   P47708;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 2.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Rabphilin-3A;
DE   AltName: Full=Exophilin-1;
GN   Name=Rph3a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RA   Inagaki N.;
RL   Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-606.
RC   STRAIN=C57BL/6;
RX   MEDLINE=95122445; PubMed=7822236;
RA   Inagaki N., Mizuta M., Seino S.;
RT   "Cloning of a mouse Rabphilin-3A expressed in hormone-secreting
RT   cells.";
RL   J. Biochem. 116:239-242(1994).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-271, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Protein transport. Probably involved with Ras-related
CC       protein Rab-3A in synaptic vesicle traffic and/or synaptic vesicle
CC       fusion. Could play a role in neurotransmitter release by
CC       regulating membrane flow in the nerve terminal.
CC   -!- SUBUNIT: Monomer.
CC   -!- INTERACTION:
CC       Q9ERI2:Rab27a; NbExp=2; IntAct=EBI-398376, EBI-398172;
CC       P63011:Rab3a; NbExp=2; IntAct=EBI-398376, EBI-398393;
CC       P55258:Rab8a; NbExp=2; IntAct=EBI-398376, EBI-398411;
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse (By similarity).
CC   -!- TISSUE SPECIFICITY: Specifically expressed in brain.
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 1 RabBD (Rab-binding) domain.
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DR   EMBL; BC042585; AAH42585.1; -; mRNA.
DR   EMBL; BC050883; AAH50883.1; -; mRNA.
DR   EMBL; D29965; BAA06231.2; -; mRNA.
DR   IPI; IPI00111151; -.
DR   PIR; JX0338; JX0338.
DR   RefSeq; NP_035416.1; NM_011286.2.
DR   UniGene; Mm.181166; -.
DR   PDB; 2K3H; NMR; -; A=368-507.
DR   PDBsum; 2K3H; -.
DR   ProteinModelPortal; P47708; -.
DR   SMR; P47708; 44-167, 379-680.
DR   IntAct; P47708; 9.
DR   STRING; P47708; -.
DR   PhosphoSite; P47708; -.
DR   PRIDE; P47708; -.
DR   Ensembl; ENSMUST00000079204; ENSMUSP00000078198; ENSMUSG00000029608.
DR   GeneID; 19894; -.
DR   KEGG; mmu:19894; -.
DR   UCSC; uc008zil.1; mouse.
DR   CTD; 19894; -.
DR   MGI; MGI:102788; Rph3a.
DR   eggNOG; maNOG04022; -.
DR   HOGENOM; HBG716633; -.
DR   HOVERGEN; HBG017739; -.
DR   InParanoid; P47708; -.
DR   OMA; GWSVHPS; -.
DR   OrthoDB; EOG4Z0B5S; -.
DR   NextBio; 297420; -.
DR   ArrayExpress; P47708; -.
DR   Bgee; P47708; -.
DR   CleanEx; MM_RPH3A; -.
DR   Genevestigator; P47708; -.
DR   GermOnline; ENSMUSG00000029608; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0017137; F:Rab GTPase binding; IEA:InterPro.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   InterPro; IPR010911; Rab-bd_domain.
DR   InterPro; IPR003315; Rabphilin3A_effector_Zn-bd.
DR   InterPro; IPR001565; Synaptotagmin.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF02318; RPH3A_effector; 1.
DR   PRINTS; PR00360; C2DOMAIN.
DR   PRINTS; PR00399; SYNAPTOTAGMN.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS50916; RABBD; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell junction; Metal-binding; Phosphoprotein;
KW   Protein transport; Repeat; Synapse; Transport; Zinc; Zinc-finger.
FT   CHAIN         1    681       Rabphilin-3A.
FT                                /FTId=PRO_0000190228.
FT   DOMAIN       40    157       RabBD.
FT   DOMAIN      381    485       C2 1.
FT   DOMAIN      539    642       C2 2.
FT   ZN_FING      88    145       FYVE-type.
FT   COMPBIAS    277    361       Pro-rich.
FT   MOD_RES     271    271       Phosphoserine.
FT   STRAND      383    390
FT   TURN        391    394
FT   STRAND      395    403
FT   STRAND      417    424
FT   TURN        428    430
FT   STRAND      432    437
FT   STRAND      445    452
FT   HELIX       457    460
FT   STRAND      464    472
FT   STRAND      478    480
FT   STRAND      484    487
FT   HELIX       488    490
FT   STRAND      495    501
SQ   SEQUENCE   681 AA;  75489 MW;  D09F8D8D2CBB271E CRC64;
     MTDTVVNRWM YPGDGPLQSN DKEQLQAGWS VHPGAQTDRQ RKQEELTDEE KEIINRVIAR
     AEKMEAMEQE RIGRLVDRLE TMRKNVAGDG VNRCILCGEQ LGMLGSACVV CEDCKKNVCT
     KCGVETSNNR PHPVWLCKIC LEQREVWKRS GAWFFKGFPK QVLPQPMPIK KTKPQQPAGE
     PATQEQPTPE SRHPARAPAR GDMEDRRPPG QKPGPDLTSA PGRGSHGPPT RRASEARMST
     AARDSEGWDH AHGGGTGDTS RSPAGLRRAN SVQAARPAPA PVPSPAPPQP VQPGPPGGSR
     ATPGPGRFPE QSTEAPPSDP GYPGAVAPAR EERTGPAGGF QAAPHTAAPY SQAAPARQPP
     PAEEEEEEAN SYDSDEATTL GALEFSLLYD QDNSNLQCTI IRAKGLKPMD SNGLADPYVK
     LHLLPGASKS NKLRTKTLRN TRNPVWNETL QYHGITEEDM QRKTLRISVC DEDKFGHNEF
     IGETRFSLKK LKANQRKNFN ICLERVIPMK RAGTTGSARG MALYEEEQVE RIGDIEERGK
     ILVSLMYSTQ QGGLIVGIIR CVHLAAMDAN GYSDPFVKLW LKPDMGKKAK HKTQIKKKTL
     NPEFNEEFFY DIKHSDLAKK SLDISVWDYD IGKSNDYIGG CQLGISAKGE RLKHWYECLK
     NKDKKIERWH QLQNENHVSS D
//
ID   PA24A_MOUSE             Reviewed;         748 AA.
AC   P47713;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   08-MAR-2011, entry version 103.
DE   RecName: Full=Cytosolic phospholipase A2;
DE            Short=cPLA2;
DE   AltName: Full=Phospholipase A2 group IVA;
DE   Includes:
DE     RecName: Full=Phospholipase A2;
DE              EC=3.1.1.4;
DE     AltName: Full=Phosphatidylcholine 2-acylhydrolase;
DE   Includes:
DE     RecName: Full=Lysophospholipase;
DE              EC=3.1.1.5;
GN   Name=Pla2g4a; Synonyms=Cpla2, Pla2g4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=91256305; PubMed=1904318; DOI=10.1016/0092-8674(91)90556-E;
RA   Clark J.D., Lin L.-L., Kriz R.W., Ramesha C.S., Sultzman L.A.,
RA   Lin A.Y., Milona N., Knopf J.L.;
RT   "A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-
RT   dependent translocation domain with homology to PKC and GAP.";
RL   Cell 65:1043-1051(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION AT SER-505 AND SER-726, AND ACTIVATION.
RX   PubMed=10978317; DOI=10.1074/jbc.M003395200;
RA   Hefner Y., Boersch-Haubold A.G., Murakami M., Wilde J.I., Pasquet S.,
RA   Schieltz D., Ghomashchi F., Yates J.R. III, Armstrong C.G.,
RA   Paterson A., Cohen P., Fukunaga R., Hunter T., Kudo I., Watson S.P.,
RA   Gelb M.H.;
RT   "Serine 727 phosphorylation and activation of cytosolic phospholipase
RT   A2 by MNK1-related protein kinases.";
RL   J. Biol. Chem. 275:37542-37551(2000).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-726, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Selectively hydrolyzes arachidonyl phospholipids in the
CC       sn-2 position releasing arachidonic acid. Together with its
CC       lysophospholipid activity, it is implicated in the initiation of
CC       the inflammatory response.
CC   -!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
CC       acylglycerophosphocholine + a carboxylate.
CC   -!- CATALYTIC ACTIVITY: 2-lysophosphatidylcholine + H(2)O =
CC       glycerophosphocholine + a carboxylate.
CC   -!- ENZYME REGULATION: Stimulated by agonists such as ATP, EGF,
CC       thrombin and bradykinin as well as by cytosolic Ca(2+).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic vesicle.
CC       Note=Translocates to membrane vesicles in a calcium-dependent
CC       fashion.
CC   -!- DOMAIN: The N-terminal C2 domain associates with lipid membranes
CC       upon calcium binding. It modulates enzyme activity by presenting
CC       the active site to its substrate in response to elevations of
CC       cytosolic Ca(2+) (By similarity).
CC   -!- PTM: Activated by phosphorylation at both Ser-505 and Ser-726.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 PLA2c domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M72394; AAB00796.1; -; mRNA.
DR   EMBL; BC003816; AAH03816.1; -; mRNA.
DR   IPI; IPI00111169; -.
DR   PIR; B39898; B39898.
DR   RefSeq; NP_032895.1; NM_008869.3.
DR   UniGene; Mm.4186; -.
DR   ProteinModelPortal; P47713; -.
DR   SMR; P47713; 13-720.
DR   IntAct; P47713; 15.
DR   STRING; P47713; -.
DR   PhosphoSite; P47713; -.
DR   PRIDE; P47713; -.
DR   Ensembl; ENSMUST00000070200; ENSMUSP00000070868; ENSMUSG00000056220.
DR   GeneID; 18783; -.
DR   KEGG; mmu:18783; -.
DR   UCSC; uc007cxt.1; mouse.
DR   CTD; 18783; -.
DR   MGI; MGI:1195256; Pla2g4a.
DR   eggNOG; roNOG07997; -.
DR   HOGENOM; HBG445891; -.
DR   HOVERGEN; HBG053479; -.
DR   InParanoid; P47713; -.
DR   OMA; IHFVLAN; -.
DR   OrthoDB; EOG4Z62MZ; -.
DR   PhylomeDB; P47713; -.
DR   BRENDA; 3.1.1.4; 244.
DR   BRENDA; 3.1.1.5; 244.
DR   NextBio; 295044; -.
DR   PMAP-CutDB; P47713; -.
DR   ArrayExpress; P47713; -.
DR   Bgee; P47713; -.
DR   Genevestigator; P47713; -.
DR   GermOnline; ENSMUSG00000056220; Mus musculus.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; ISS:UniProtKB.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:EC.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPlipase.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR002642; Lysophospholipase_cat_dom.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF01735; PLA2_B; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00022; PLAc; 1.
DR   SUPFAM; SSF52151; Acyl_Trfase/lysoPlipase; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS51210; PLA2C; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cytoplasm; Cytoplasmic vesicle; Hydrolase; Lipid degradation;
KW   Metal-binding; Phosphoprotein.
FT   CHAIN         1    748       Cytosolic phospholipase A2.
FT                                /FTId=PRO_0000187263.
FT   DOMAIN        5    106       C2.
FT   DOMAIN      140    739       PLA2c.
FT   REGION        1    178       Phospholipid binding (Probable).
FT   ACT_SITE    228    228       Nucleophile (By similarity).
FT   ACT_SITE    548    548       Proton acceptor (By similarity).
FT   METAL        40     40       Calcium 1 (By similarity).
FT   METAL        40     40       Calcium 2 (By similarity).
FT   METAL        41     41       Calcium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        43     43       Calcium 1 (By similarity).
FT   METAL        43     43       Calcium 2 (By similarity).
FT   METAL        65     65       Calcium 1 (By similarity).
FT   METAL        93     93       Calcium 2 (By similarity).
FT   METAL        94     94       Calcium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        95     95       Calcium 2 (By similarity).
FT   MOD_RES     268    268       Phosphothreonine (By similarity).
FT   MOD_RES     434    434       Phosphoserine (By similarity).
FT   MOD_RES     435    435       Phosphoserine (By similarity).
FT   MOD_RES     437    437       Phosphoserine.
FT   MOD_RES     505    505       Phosphoserine; by MAPK.
FT   MOD_RES     534    534       Phosphotyrosine (By similarity).
FT   MOD_RES     726    726       Phosphoserine.
FT   MOD_RES     728    728       Phosphoserine (By similarity).
SQ   SEQUENCE   748 AA;  85222 MW;  49D12BBB2911492A CRC64;
     MSFIDPYQHI IVEHQYSHKF TVVVLRATKV TKGTFGDMLD TPDPYVELFI STTPDSRKRT
     RHFNNDINPV WNETFEFILD PNQENVLEIT LMDANYVMDE TLGTATFPVS SMKVGEKKEV
     PFIFNQVTEM ILEMSLEVCS CPDLRFSMAL CDQEKTFRQQ RKENIKENMK KLLGPKKSEG
     LYSTRDVPVV AILGSGGGFR AMVGFSGVMK ALYESGILDC ATYIAGLSGS TWYMSTLYSH
     PDFPEKGPEE INEELMKNVS HNPLLLLTPQ KVKRYVESLW KKKSSGQPVT FTDIFGMLIG
     ETLIQNRMSM TLSSLKEKVN AARCPLPLFT CLHVKPDVSE LMFADWVEFS PYEIGMAKYG
     TFMAPDLFGS KFFMGTVVKK YEENPLHFLM GVWGSAFSIL FNRVLGVSGS QNKGSTMEEE
     LENITAKHIV SNDSSDSDDE AQGPKGTENE EAEKEYQSDN QASWVHRMLM ALVSDSALFN
     TREGRAGKVH NFMLGLNLNT SYPLSPLRDF SSQDSFDDEL DAAVADPDEF ERIYEPLDVK
     SKKIHVVDSG LTFNLPYPLI LRPQRGVDLI ISFDFSARPS DTSPPFKELL LAEKWAKMNK
     LPFPKIDPYV FDREGLKECY VFKPKNPDVE KDCPTIIHFV LANINFRKYK APGVLRETKE
     EKEIADFDIF DDPESPFSTF NFQYPNQAFK RLHDLMYFNT LNNIDVIKDA IVESIEYRRQ
     NPSRCSVSLS NVEARKFFNK EFLSKPTV
//
ID   GRM8_MOUSE              Reviewed;         908 AA.
AC   P47743; Q6B964;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Metabotropic glutamate receptor 8;
DE            Short=mGluR8;
DE   Flags: Precursor;
GN   Name=Grm8; Synonyms=Gprc1h, Mglur8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Retina;
RX   MEDLINE=95239344; PubMed=7722646;
RA   Duvoisin R.M., Zhang C., Ramonell K.;
RT   "A novel metabotropic glutamate receptor expressed in the retina and
RT   olfactory bulb.";
RL   J. Neurosci. 15:3075-3083(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   PubMed=15755905; DOI=10.1124/mol.105.010975;
RA   Guo J., Ikeda S.R.;
RT   "Coupling of metabotropic glutamate receptor 8 to N-type Ca2+ channels
RT   in rat sympathetic neurons.";
RL   Mol. Pharmacol. 67:1840-1851(2005).
RN   [3]
RP   SUMOYLATION AT LYS-882, AND MUTAGENESIS OF LYS-868; LYS-872 AND
RP   LYS-882.
RX   PubMed=16144832; DOI=10.1074/jbc.M508168200;
RA   Tang Z., El Far O., Betz H., Scheschonka A.;
RT   "Pias1 interaction and sumoylation of metabotropic glutamate receptor
RT   8.";
RL   J. Biol. Chem. 280:38153-38159(2005).
CC   -!- FUNCTION: Receptor for glutamate. The activity of this receptor is
CC       mediated by a G-protein that inhibits adenylate cyclase activity.
CC   -!- SUBUNIT: Interacts with PICK1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in olfactory bulb,
CC       accessory olfactory bulb, and mammillary body. Weaker expression
CC       in the retina, and in scattered cells in the cortex and hindbrain.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U17252; AAA68149.1; -; mRNA.
DR   EMBL; AY673682; AAT76980.1; -; mRNA.
DR   IPI; IPI00111240; -.
DR   PIR; I49142; I49142.
DR   UniGene; Mm.320732; -.
DR   ProteinModelPortal; P47743; -.
DR   SMR; P47743; 38-574.
DR   STRING; P47743; -.
DR   PhosphoSite; P47743; -.
DR   PRIDE; P47743; -.
DR   Ensembl; ENSMUST00000090512; ENSMUSP00000087998; ENSMUSG00000024211.
DR   UCSC; uc009bcj.1; mouse.
DR   MGI; MGI:1351345; Grm8.
DR   GeneTree; ENSGT00580000081222; -.
DR   HOVERGEN; HBG107965; -.
DR   OMA; LTQKGND; -.
DR   ArrayExpress; P47743; -.
DR   Bgee; P47743; -.
DR   CleanEx; MM_GRM8; -.
DR   Genevestigator; P47743; -.
DR   GermOnline; ENSMUSG00000024211; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:UniProtKB.
DR   GO; GO:0001642; F:group III metabotropic glutamate receptor activity; IDA:MGI.
DR   GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; TAS:UniProtKB.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR000337; GPCR_3.
DR   InterPro; IPR011500; GPCR_3_9-Cys_dom.
DR   InterPro; IPR017978; GPCR_3_C.
DR   InterPro; IPR017979; GPCR_3_CS.
DR   InterPro; IPR000162; GPCR_3_mtglu_rcpt.
DR   InterPro; IPR000144; GPCR_3_mtglu_rcpt_8.
DR   Pfam; PF00003; 7tm_3; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF07562; NCD3G; 1.
DR   PRINTS; PR00248; GPCRMGR.
DR   PRINTS; PR01058; MTABOTROPC8R.
DR   PRINTS; PR00593; MTABOTROPICR.
DR   PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; 1.
DR   PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; 1.
DR   PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
DR   PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein;
KW   Isopeptide bond; Membrane; Olfaction; Receptor; Sensory transduction;
KW   Signal; Transducer; Transmembrane; Transmembrane helix;
KW   Ubl conjugation.
FT   SIGNAL        1     33       Potential.
FT   CHAIN        34    908       Metabotropic glutamate receptor 8.
FT                                /FTId=PRO_0000012942.
FT   TOPO_DOM     34    583       Extracellular (Potential).
FT   TRANSMEM    584    608       Helical; Name=1; (Potential).
FT   TOPO_DOM    609    620       Cytoplasmic (Potential).
FT   TRANSMEM    621    641       Helical; Name=2; (Potential).
FT   TOPO_DOM    642    647       Extracellular (Potential).
FT   TRANSMEM    648    668       Helical; Name=3; (Potential).
FT   TOPO_DOM    669    695       Cytoplasmic (Potential).
FT   TRANSMEM    696    716       Helical; Name=4; (Potential).
FT   TOPO_DOM    717    746       Extracellular (Potential).
FT   TRANSMEM    747    768       Helical; Name=5; (Potential).
FT   TOPO_DOM    769    781       Cytoplasmic (Potential).
FT   TRANSMEM    782    803       Helical; Name=6; (Potential).
FT   TOPO_DOM    804    818       Extracellular (Potential).
FT   TRANSMEM    819    843       Helical; Name=7; (Potential).
FT   TOPO_DOM    844    908       Cytoplasmic (Potential).
FT   CARBOHYD     95     95       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    298    298       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    452    452       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    480    480       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    565    565       N-linked (GlcNAc...) (Potential).
FT   CROSSLNK    882    882       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO-1).
FT   MUTAGEN     868    868       K->R: No change in sumoylation. Abolishes
FT                                sumoylation; when associated with R-872
FT                                and R-882.
FT   MUTAGEN     872    872       K->R: No change in sumoylation. Abolishes
FT                                sumoylation; when associated with R-868
FT                                and R-882.
FT   MUTAGEN     882    882       K->R: Abolishes sumoylation. Abolishes
FT                                sumoylation; when associated with R-868
FT                                and R-872.
FT   CONFLICT     86     86       I -> T (in Ref. 1; AAA68149).
FT   CONFLICT    289    289       R -> G (in Ref. 1; AAA68149).
FT   CONFLICT    363    365       WEE -> SEG (in Ref. 1; AAA68149).
FT   CONFLICT    371    371       L -> S (in Ref. 1; AAA68149).
FT   CONFLICT    539    539       E -> G (in Ref. 1; AAA68149).
FT   CONFLICT    589    589       F -> L (in Ref. 1; AAA68149).
FT   CONFLICT    905    905       N -> D (in Ref. 1; AAA68149).
SQ   SEQUENCE   908 AA;  101828 MW;  E9952B6D356EB8A8 CRC64;
     MVCEGKRSTS CPCFFLLTAK FYWILTMMQR THSQEYAHSI RLDGDIILGG LFPVHAKGER
     GVPCGDLKKE KGIHRLEAML YAIDQINKDP DLLSNITLGV RILDTCSRDT YALEQSLTFV
     QALIEKDASD VKCANGDPPI FTKPDKISGV IGAAASSVSI MVANILRLFK IPQISYASTA
     PELSDNTRYD FFSRVVPPDS YQAQAMVDIV TALGWNYVST LASEGNYGES GVEAFTQISR
     EIGGVCIAQS QKIPREPRPG EFEKIIKRLL ETPNARAVIM FANEDDIRRI LEAAKKLNQS
     GHFLWIGSDS WGSKIAPVYQ QEEIAEGAVT ILPKRASIDG FDRYFRSRTL ANNRRNVWFA
     EFWEENFGCK LGSHGKRNSH IKKCTGLERI ARDSSYEQEG KVQFVIDAVY SMAYALHNMH
     KELCPGYIGL CPRMVTIDGK ELLGYIRAVN FNGSAGTPVT FNENGDAPGR YDIFQYQINN
     KSTEYKIIGH WTNQLHLKVE DMQWANREHT HPASVCSLPC KPGERKKTVK GVPCCWHCER
     CEGYNYQVDE LSCELCPLDQ RPNINRTGCQ RIPIIKLEWH SPWAVVPVFI AILGIIATTF
     VIVTFVRYND TPIVRASGRE LSYVLLTGIF LCYSITFLMI AAPDTIICSF RRIFLGLGMC
     FSYAALLTKT NRIHRIFEQG KKSVTAPKFI SPASQLVITF SLISVQLLGV FVWFVVDPPH
     TIIDYGEQRT LDPENARGVL KCDISDLSLI CSLGYSILLM VTCTVYAIKT RGVPETFNEA
     KPIGFTMYTT CIIWLAFIPI FFGTAQSAEK MYIQTTTLTV SMSLSASVSL GMLYMPKVYI
     IIFHPEQNVQ KRKRSFKAVV TAATMQSKLI QKGNDRPNGE VKSELCESLE TNTSSTKTTY
     ISYSNHSI
//
ID   CNR1_MOUSE              Reviewed;         473 AA.
AC   P47746; Q5SF33;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Cannabinoid receptor 1;
DE            Short=CB-R;
DE            Short=CB1;
DE   AltName: Full=Brain-type cannabinoid receptor;
GN   Name=Cnr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=96272305; PubMed=8777318;
RA   Chakrabarti A., Onaivi E.S., Chaudhuri G.;
RT   "Cloning and sequencing of a cDNA encoding the mouse brain-type
RT   cannabinoid receptor protein.";
RL   DNA Seq. 5:385-388(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96429553; PubMed=8832654; DOI=10.1016/0304-3940(96)12792-0;
RA   Ho B.Y., Zhao J.;
RT   "Determination of the cannabinoid receptors in mouse x rat hybridoma
RT   NG108-15 cells and rat GH4C1 cells.";
RL   Neurosci. Lett. 212:123-126(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=99105999; PubMed=9888857; DOI=10.1126/science.283.5400.401;
RA   Ledent C., Valverde O., Cossu G., Petitet F., Aubert J.F., Beslot F.,
RA   Boehme G.A., Imperato A., Pedrazzini T., Roques B.P., Vassart G.,
RA   Fratta W., Parmentier M.;
RT   "Unresponsiveness to cannabinoids and reduced addictive effects of
RT   opiates in CB1 receptor knockout mice.";
RL   Science 283:401-404(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=C57BL/6 X CBA;
RX   PubMed=15606779; DOI=10.1111/j.1432-1033.2004.04460.x;
RA   McCaw E.A., Hu H., Gomez G.T., Hebb A.L., Kelly M.E.,
RA   Denovan-Wright E.M.;
RT   "Structure, expression and regulation of the cannabinoid receptor gene
RT   (CB1) in Huntington's disease transgenic mice.";
RL   Eur. J. Biochem. 271:4909-4920(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129;
RA   Bonner T.I.;
RL   Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yuan Z.-Q., Li L., Qiu B.-S., Song D.-K.;
RT   "cDNA cloning and expression analysis of mouse cannabinoid receptor
RT   (CB1) gene.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Involved in cannabinoid-induced CNS effects. Acts by
CC       inhibiting adenylate cyclase. Could be a receptor for anandamide.
CC       Inhibits L-type Ca(2+) channel current.
CC   -!- SUBUNIT: Interacts (via C-terminus) with CNRIP1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U17985; AAA57202.1; -; mRNA.
DR   EMBL; U40709; AAA91176.1; -; mRNA.
DR   EMBL; Y18374; CAB42647.1; -; Genomic_DNA.
DR   EMBL; AY522555; AAS91801.1; -; Genomic_DNA.
DR   EMBL; AY522554; AAS91800.1; -; mRNA.
DR   EMBL; U22948; AAA64413.1; -; Genomic_DNA.
DR   EMBL; AF153345; AAD34624.1; -; mRNA.
DR   EMBL; AK139417; BAE24003.1; -; mRNA.
DR   EMBL; BC070447; AAH70447.1; -; mRNA.
DR   EMBL; BC079564; AAH79564.1; -; mRNA.
DR   IPI; IPI00111245; -.
DR   RefSeq; NP_031752.1; NM_007726.3.
DR   UniGene; Mm.7992; -.
DR   ProteinModelPortal; P47746; -.
DR   SMR; P47746; 118-414.
DR   STRING; P47746; -.
DR   PhosphoSite; P47746; -.
DR   PRIDE; P47746; -.
DR   Ensembl; ENSMUST00000057188; ENSMUSP00000055797; ENSMUSG00000044288.
DR   Ensembl; ENSMUST00000084736; ENSMUSP00000081787; ENSMUSG00000044288.
DR   GeneID; 12801; -.
DR   KEGG; mmu:12801; -.
DR   NMPDR; fig|10090.3.peg.9375; -.
DR   UCSC; uc008sfw.1; mouse.
DR   CTD; 12801; -.
DR   MGI; MGI:104615; Cnr1.
DR   eggNOG; roNOG10571; -.
DR   HOGENOM; HBG716518; -.
DR   HOVERGEN; HBG051045; -.
DR   InParanoid; P47746; -.
DR   OMA; FVYSFVD; -.
DR   OrthoDB; EOG41ZF9S; -.
DR   PhylomeDB; P47746; -.
DR   NextBio; 282226; -.
DR   ArrayExpress; P47746; -.
DR   Bgee; P47746; -.
DR   CleanEx; MM_CNR1; -.
DR   Genevestigator; P47746; -.
DR   GermOnline; ENSMUSG00000044288; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004949; F:cannabinoid receptor activity; ISS:UniProtKB.
DR   GO; GO:0007188; P:G-protein signaling, coupled to cAMP nucleotide second messenger; ISS:UniProtKB.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR002230; Cnbnoid_rcpt.
DR   InterPro; IPR000810; Cnoid_rcpt_1.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   PANTHER; PTHR22750:SF10; Cnoid_rcpt_1; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PIRSF; PIRSF037995; Cnoid_rcpt_1; 1.
DR   PRINTS; PR00522; CANABINOID1R.
DR   PRINTS; PR00362; CANNABINOIDR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Receptor; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN         1    473       Cannabinoid receptor 1.
FT                                /FTId=PRO_0000069316.
FT   TOPO_DOM      1    117       Extracellular (Potential).
FT   TRANSMEM    118    143       Helical; Name=1; (Potential).
FT   TOPO_DOM    144    155       Cytoplasmic (Potential).
FT   TRANSMEM    156    176       Helical; Name=2; (Potential).
FT   TOPO_DOM    177    188       Extracellular (Potential).
FT   TRANSMEM    189    213       Helical; Name=3; (Potential).
FT   TOPO_DOM    214    233       Cytoplasmic (Potential).
FT   TRANSMEM    234    256       Helical; Name=4; (Potential).
FT   TOPO_DOM    257    274       Extracellular (Potential).
FT   TRANSMEM    275    300       Helical; Name=5; (Potential).
FT   TOPO_DOM    301    345       Cytoplasmic (Potential).
FT   TRANSMEM    346    366       Helical; Name=6; (Potential).
FT   TOPO_DOM    367    378       Extracellular (Potential).
FT   TRANSMEM    379    400       Helical; Name=7; (Potential).
FT   TOPO_DOM    401    473       Cytoplasmic (Potential).
FT   CARBOHYD     78     78       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     84     84       N-linked (GlcNAc...) (Potential).
FT   CONFLICT      9      9       A -> G (in Ref. 1; AAA57202).
FT   CONFLICT    115    115       S -> R (in Ref. 1; AAA57202).
FT   CONFLICT    211    211       T -> R (in Ref. 1; AAA57202).
SQ   SEQUENCE   473 AA;  52831 MW;  E504168191CB6429 CRC64;
     MKSILDGLAD TTFRTITTDL LYVGSNDIQY EDIKGDMASK LGYFPQKFPL TSFRGSPFQE
     KMTAGDNSPL VPAGDTTNIT EFYNKSLSSF KENEDNIQCG ENFMDMECFM ILNPSQQLAI
     AVLSLTLGTF TVLENLLVLC VILHSRSLRC RPSYHFIGSL AVADLLGSVI FVYSFVDFHV
     FHRKDSPNVF LFKLGGVTAS FTASVGSLFL TAIDRYISIH RPLAYKRIVT RPKAVVAFCL
     MWTIAIVIAV LPLLGWNCKK LQSVCSDIFP LIDETYLMFW IGVTSVLLLF IVYAYMYILW
     KAHSHAVRMI QRGTQKSIII HTSEDGKVQV TRPDQARMDI RLAKTLVLIL VVLIICWGPL
     LAIMVYDVFG KMNKLIKTVF AFCSMLCLLN STVNPIIYAL RSKDLRHAFR SMFPSCEGTA
     QPLDNSMGDS DCLHKHANNT ASMHRAAESC IKSTVKIAKV TMSVSTDTSA EAL
//
ID   CAZA1_MOUSE             Reviewed;         286 AA.
AC   P47753; Q91YN7;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=F-actin-capping protein subunit alpha-1;
DE   AltName: Full=CapZ alpha-1;
GN   Name=Capza1; Synonyms=Cappa1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-286.
RC   TISSUE=Muscle;
RX   MEDLINE=97470757; PubMed=9331217;
RX   DOI=10.1002/(SICI)1097-0169(1997)38:2<120::AID-CM2>3.0.CO;2-B;
RA   Hart M.C., Korshunova Y.O., Cooper J.A.;
RT   "Vertebrates have conserved capping protein alpha isoforms with
RT   specific expression patterns.";
RL   Cell Motil. Cytoskeleton 38:120-132(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 194-210.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
CC   -!- FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent
CC       manner to the fast growing ends of actin filaments (barbed end)
CC       thereby blocking the exchange of subunits at these ends. Unlike
CC       other capping proteins (such as gelsolin and severin), these
CC       proteins do not sever actin filaments.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Component of
CC       the WASH complex, composed of F-actin-capping protein subunit
CC       alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit
CC       beta (CAPZB), WASH1, FAM21, KIAA1033, KIAA0196 and CCDC53.
CC       Interacts with S100B and S100A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC   -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC016232; AAH16232.1; -; mRNA.
DR   EMBL; U16740; AAC00566.1; -; mRNA.
DR   IPI; IPI00330063; -.
DR   RefSeq; NP_033927.2; NM_009797.2.
DR   UniGene; Mm.19142; -.
DR   UniGene; Mm.476746; -.
DR   ProteinModelPortal; P47753; -.
DR   SMR; P47753; 7-281.
DR   STRING; P47753; -.
DR   PhosphoSite; P47753; -.
DR   REPRODUCTION-2DPAGE; P47753; -.
DR   PRIDE; P47753; -.
DR   Ensembl; ENSMUST00000094028; ENSMUSP00000102381; ENSMUSG00000070372.
DR   GeneID; 12340; -.
DR   KEGG; mmu:12340; -.
DR   UCSC; uc008quq.1; mouse.
DR   CTD; 12340; -.
DR   MGI; MGI:106227; Capza1.
DR   eggNOG; roNOG04932; -.
DR   HOVERGEN; HBG050810; -.
DR   InParanoid; P47753; -.
DR   OrthoDB; EOG45DWQ0; -.
DR   PhylomeDB; P47753; -.
DR   ArrayExpress; P47753; -.
DR   Bgee; P47753; -.
DR   Genevestigator; P47753; -.
DR   GermOnline; ENSMUSG00000074348; Mus musculus.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR   GO; GO:0008290; C:F-actin capping protein complex; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0071203; C:WASH complex; ISS:UniProtKB.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR   InterPro; IPR017865; F-actin_cap_asu_CS.
DR   InterPro; IPR002189; WASH_F-actin_cap_alpha.
DR   PANTHER; PTHR10653; F-actin_cap_A; 1.
DR   Pfam; PF01267; F-actin_cap_A; 1.
DR   PRINTS; PR00191; FACTINCAPA.
DR   PROSITE; PS00748; F_ACTIN_CAPPING_A_1; 1.
DR   PROSITE; PS00749; F_ACTIN_CAPPING_A_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin capping; Actin-binding; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    286       F-actin-capping protein subunit alpha-1.
FT                                /FTId=PRO_0000208625.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      19     19       N6-acetyllysine (By similarity).
FT   MOD_RES      97     97       N6-acetyllysine (By similarity).
FT   CONFLICT    222    222       V -> I (in Ref. 2; AAC00566).
SQ   SEQUENCE   286 AA;  32940 MW;  6FE97BCE5D9B9D3A CRC64;
     MADFEDRVSD EEKVRIAAKF ITHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNMD
     QFTPVKIEGY DDQVLITEHG DLGNSRFLDP RNQISFKFDH LRKEASDPQP EDVDGGLKSW
     RESCDSALRA YVKDHYSNGF CTVYAKTIDG QQTIIACIES HQFQPKNFWN GRWRSEWKFT
     ITPPSAQVVG VLKIQVHYYE DGNVQLVSHK DVQDSVTVSN EVQTTKEFIK IIESAENEYQ
     TAISENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA
//
ID   CAZA2_MOUSE             Reviewed;         286 AA.
AC   P47754;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=F-actin-capping protein subunit alpha-2;
DE   AltName: Full=CapZ alpha-2;
GN   Name=Capza2; Synonyms=Cappa2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RX   MEDLINE=97470757; PubMed=9331217;
RX   DOI=10.1002/(SICI)1097-0169(1997)38:2<120::AID-CM2>3.0.CO;2-B;
RA   Hart M.C., Korshunova Y.O., Cooper J.A.;
RT   "Vertebrates have conserved capping protein alpha isoforms with
RT   specific expression patterns.";
RL   Cell Motil. Cytoskeleton 38:120-132(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-13; 20-86 AND 104-129, CLEAVAGE OF INITIATOR
RP   METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RA   Sumpton D.P., Sandilands E., Frame M.C., Bienvenut W.V.;
RL   Submitted (MAR-2008) to UniProtKB.
RN   [4]
RP   PROTEIN SEQUENCE OF 20-37; 67-86 AND 194-210, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
CC   -!- FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent
CC       manner to the fast growing ends of actin filaments (barbed end)
CC       thereby blocking the exchange of subunits at these ends. Unlike
CC       other capping proteins (such as gelsolin and severin), these
CC       proteins do not sever actin filaments.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Component of
CC       the WASH complex, composed of F-actin-capping protein subunit
CC       alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-capping protein subunit
CC       beta (CAPZB), WASH1, FAM21, KIAA1033, KIAA0196 and CCDC53.
CC       Interacts with RCSD1/CAPZIP (By similarity).
CC   -!- SIMILARITY: Belongs to the F-actin-capping protein alpha subunit
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U16741; AAC00567.1; -; mRNA.
DR   EMBL; BC082589; AAH82589.1; -; mRNA.
DR   IPI; IPI00111265; -.
DR   RefSeq; NP_031630.1; NM_007604.2.
DR   UniGene; Mm.392504; -.
DR   ProteinModelPortal; P47754; -.
DR   SMR; P47754; 8-276.
DR   DIP; DIP-31382N; -.
DR   STRING; P47754; -.
DR   PhosphoSite; P47754; -.
DR   REPRODUCTION-2DPAGE; P47754; -.
DR   PRIDE; P47754; -.
DR   Ensembl; ENSMUST00000015877; ENSMUSP00000015877; ENSMUSG00000015733.
DR   GeneID; 12343; -.
DR   KEGG; mmu:12343; -.
DR   UCSC; uc009azt.1; mouse.
DR   CTD; 12343; -.
DR   MGI; MGI:106222; Capza2.
DR   eggNOG; roNOG04256; -.
DR   HOGENOM; HBG397839; -.
DR   HOVERGEN; HBG050810; -.
DR   InParanoid; P47754; -.
DR   OMA; YDHLRKE; -.
DR   OrthoDB; EOG45DWQ0; -.
DR   PhylomeDB; P47754; -.
DR   NextBio; 280972; -.
DR   ArrayExpress; P47754; -.
DR   Bgee; P47754; -.
DR   Genevestigator; P47754; -.
DR   GermOnline; ENSMUSG00000015733; Mus musculus.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR   GO; GO:0008290; C:F-actin capping protein complex; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR   InterPro; IPR017865; F-actin_cap_asu_CS.
DR   InterPro; IPR002189; WASH_F-actin_cap_alpha.
DR   PANTHER; PTHR10653; F-actin_cap_A; 1.
DR   Pfam; PF01267; F-actin_cap_A; 1.
DR   PRINTS; PR00191; FACTINCAPA.
DR   PROSITE; PS00748; F_ACTIN_CAPPING_A_1; 1.
DR   PROSITE; PS00749; F_ACTIN_CAPPING_A_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin capping; Actin-binding; Direct protein sequencing;
KW   Phosphoprotein.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    286       F-actin-capping protein subunit alpha-2.
FT                                /FTId=PRO_0000208628.
FT   MOD_RES       2      2       N-acetylalanine.
FT   MOD_RES       9      9       Phosphoserine (By similarity).
FT   MOD_RES      86     86       N6-acetyllysine (By similarity).
FT   MOD_RES      97     97       N6-acetyllysine (By similarity).
FT   MOD_RES     273    273       N6-acetyllysine (By similarity).
SQ   SEQUENCE   286 AA;  32967 MW;  E706A9BC1830E70B CRC64;
     MADLEEQLSD EEKVRIAAKF IIHAPPGEFN EVFNDVRLLL NNDNLLREGA AHAFAQYNLD
     QFTPVKIEGY EDQVLITEHG DLGNGKFLDP KNRICFKFDH LRKEATDPRP YEAENAIESW
     RTSVETALRA YVKEHYPNGV CTVYGKKVDG QQTIIACIES HQFQAKNFWN GRWRSEWKFT
     VTPSTTQVVG ILKIQVHYYE DGNVQLVSHK DIQDSLTVSN EVQTAKEFIK IVEAAENEYQ
     TAISENYQTM SDTTFKALRR QLPVTRTKID WNKILSYKIG KEMQNA
//
ID   MTX1_MOUSE              Reviewed;         317 AA.
AC   P47802;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Metaxin-1;
DE   AltName: Full=Mitochondrial outer membrane import complex protein 1;
GN   Name=Mtx1; Synonyms=Mtx, Mtxn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=95273400; PubMed=7753840; DOI=10.1073/pnas.92.10.4547;
RA   Bornstein P., McKinney C.E., Lamarca M.E., Winfield S., Shingu T.,
RA   Devarayalu S., Vos H.L., Ginns E.I.;
RT   "Metaxin, a gene contiguous to both thrombospondin 3 and
RT   glucocerebrosidase, is required for embryonic development in the
RT   mouse: implications for Gaucher disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:4547-4551(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RX   MEDLINE=97025352; PubMed=8871542; DOI=10.1093/nar/24.19.3661;
RA   Collins M., Bornstein P.;
RT   "SP1-binding elements, within the common metaxin-thrombospondin 3
RT   intergenic region, participate in the regulation of the metaxin
RT   gene.";
RL   Nucleic Acids Res. 24:3661-3669(1996).
RN   [3]
RP   PROTEIN SEQUENCE OF 89-103; 118-124 AND 169-175, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 109-317.
RX   MEDLINE=98371020; PubMed=9705320; DOI=10.1074/jbc.273.34.21816;
RA   Collins M., Rojnuckarin P., Zhu Y.H., Bornstein P.;
RT   "A far upstream, cell type-specific enhancer of the mouse
RT   thrombospondin 3 gene is located within intron 6 of the adjacent
RT   metaxin gene.";
RL   J. Biol. Chem. 273:21816-21824(1998).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   MEDLINE=97197826; PubMed=9045676; DOI=10.1074/jbc.272.10.6510;
RA   Armstrong L.C., Komiya T., Bergman B.E., Mihara K., Bornstein P.;
RT   "Metaxin is a component of a preprotein import complex in the outer
RT   membrane of the mammalian mitochondrion.";
RL   J. Biol. Chem. 272:6510-6518(1997).
RN   [6]
RP   INTERACTION WITH MTX2.
RX   MEDLINE=99308987; PubMed=10381257;
RX   DOI=10.1002/(SICI)1097-4644(19990701)74:1<11::AID-JCB2>3.3.CO;2-M;
RA   Armstrong L.C., Saenz A.J., Bornstein P.;
RT   "Metaxin 1 interacts with metaxin 2, a novel related protein
RT   associated with the mammalian mitochondrial outer membrane.";
RL   J. Cell. Biochem. 74:11-22(1999).
CC   -!- FUNCTION: Involved in transport of proteins into the
CC       mitochondrion. Essential for embryonic development.
CC   -!- SUBUNIT: Interacts with MTX2/metaxin-2.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Higher levels are seen in the
CC       kidney as compared to other tissues.
CC   -!- SIMILARITY: Belongs to the metaxin family.
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DR   EMBL; L36962; AAC37672.1; -; mRNA.
DR   EMBL; U66257; AAC52818.1; -; Genomic_DNA.
DR   EMBL; AF059277; AAC63229.1; -; Genomic_DNA.
DR   IPI; IPI00112327; -.
DR   PIR; I59379; I59379.
DR   UniGene; Mm.280943; -.
DR   ProteinModelPortal; P47802; -.
DR   SMR; P47802; 176-240.
DR   IntAct; P47802; 2.
DR   STRING; P47802; -.
DR   PRIDE; P47802; -.
DR   Ensembl; ENSMUST00000073572; ENSMUSP00000073261; ENSMUSG00000064068.
DR   UCSC; uc008pye.1; mouse.
DR   MGI; MGI:103025; Mtx1.
DR   eggNOG; roNOG16695; -.
DR   HOVERGEN; HBG001655; -.
DR   OrthoDB; EOG46DM2V; -.
DR   NextBio; 292521; -.
DR   ArrayExpress; P47802; -.
DR   Bgee; P47802; -.
DR   CleanEx; MM_MTX1; -.
DR   Genevestigator; P47802; -.
DR   GermOnline; ENSMUSG00000064068; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006626; P:protein targeting to mitochondrion; IEA:InterPro.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR017410; Mt-OM_transp_Metaxin.
DR   InterPro; IPR019564; Mt-OM_transp_Tom37/Metaxin.
DR   Gene3D; G3DSA:1.20.1050.10; GST_C_like; 1.
DR   Pfam; PF10568; Tom37; 1.
DR   PIRSF; PIRSF038150; Metaxin; 1.
DR   SUPFAM; SSF47616; GST_C_like; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Protein transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    317       Metaxin-1.
FT                                /FTId=PRO_0000220992.
FT   TRANSMEM    272    292       Helical; (Potential).
SQ   SEQUENCE   317 AA;  35624 MW;  F7528371DC986562 CRC64;
     MAAPMELFCW SGGWGLPSVD LDSLAVLTYT RFTGAPLKIH KTSNPWQSPS GTLPALRTSD
     GKVITVPDKI ITHLRKEKYN ADYDLSARQG ADTLAFMSLL EEKLLPVLIH TFWIDAKNYV
     EVTRKWYAEA MPFPLNFFLP GRMQRQYMER LQLLCGEHKS ENEEELEKEL YQEARECLTL
     LSQRLGSQKF FFGDAPASLD AFVFSHLALL LQAKLPSGKL QAHLRGLHNL CAYCTHILNL
     YFPRDGDEVP LPRQTPAAPE TEEEPYRRRT QILSVLAGLA AMVGYALLSG IVSIQRTSPA
     RAPGTRALGL AEEDEED
//
ID   MP2K4_MOUSE             Reviewed;         397 AA.
AC   P47809;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Dual specificity mitogen-activated protein kinase kinase 4;
DE            Short=MAP kinase kinase 4;
DE            Short=MAPKK 4;
DE            EC=2.7.12.2;
DE   AltName: Full=C-JUN N-terminal kinase kinase 1;
DE            Short=JNK kinase 1;
DE            Short=JNKK 1;
DE   AltName: Full=JNK-activating kinase 1;
DE   AltName: Full=MAPK/ERK kinase 4;
DE            Short=MEK 4;
DE   AltName: Full=SAPK/ERK kinase 1;
DE            Short=SEK1;
GN   Name=Map2k4; Synonyms=Jnkk1, Prkmk4, Sek1, Serk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RX   MEDLINE=95089821; PubMed=7997269;
RA   Sanchez I., Hughes R.T., Mayer B.J., Yee K., Woodgett J.R., Avruch J.,
RA   Kyriakis J.M., Zon L.I.;
RT   "Role of SAPK/ERK kinase-1 in the stress-activated pathway regulating
RT   transcription factor c-Jun.";
RL   Nature 372:794-798(1994).
RN   [2]
RP   SEQUENCE REVISION.
RA   Zon L.I.;
RL   Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INTERACTION WITH SPAG9.
RX   MEDLINE=22295031; PubMed=12391307; DOI=10.1073/pnas.232310199;
RA   Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.;
RT   "JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules
RT   and transcription factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002).
CC   -!- FUNCTION: Dual specificity kinase that activates the JUN kinases
CC       MAPK8 (JNK1) and MAPK9 (JNK2) as well as MAPK14 (p38) but not
CC       MAPK1 (ERK2) or MAPK3 (ERK1).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts with SPAG9. Interacts with ARRB2 (By
CC       similarity).
CC   -!- INTERACTION:
CC       P53349:Map3k1; NbExp=1; IntAct=EBI-447934, EBI-447913;
CC   -!- TISSUE SPECIFICITY: Expressed abundantly in the adult brain and
CC       muscle.
CC   -!- PTM: Activated by phosphorylation on Ser/Thr by MAP kinase kinase
CC       kinases (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; U18310; AAB81554.1; -; mRNA.
DR   IPI; IPI00112335; -.
DR   PIR; S52423; S52423.
DR   RefSeq; NP_033183.1; NM_009157.4.
DR   UniGene; Mm.412922; -.
DR   ProteinModelPortal; P47809; -.
DR   SMR; P47809; 93-386.
DR   DIP; DIP-869N; -.
DR   IntAct; P47809; 1.
DR   STRING; P47809; -.
DR   PhosphoSite; P47809; -.
DR   PRIDE; P47809; -.
DR   Ensembl; ENSMUST00000046963; ENSMUSP00000041282; ENSMUSG00000033352.
DR   GeneID; 26398; -.
DR   KEGG; mmu:26398; -.
DR   UCSC; uc007jlb.1; mouse.
DR   CTD; 26398; -.
DR   MGI; MGI:1346869; Map2k4.
DR   eggNOG; roNOG13764; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108518; -.
DR   InParanoid; P47809; -.
DR   OMA; VMKSNDC; -.
DR   PhylomeDB; P47809; -.
DR   BRENDA; 2.7.12.2; 244.
DR   NextBio; 304351; -.
DR   ArrayExpress; P47809; -.
DR   Bgee; P47809; -.
DR   CleanEx; MM_MAP2K4; -.
DR   Genevestigator; P47809; -.
DR   GermOnline; ENSMUSG00000033352; Mus musculus.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    397       Dual specificity mitogen-activated
FT                                protein kinase kinase 4.
FT                                /FTId=PRO_0000086382.
FT   DOMAIN      100    366       Protein kinase.
FT   NP_BIND     106    114       ATP (By similarity).
FT   COMPBIAS      5     17       Gly/Ser-rich.
FT   ACT_SITE    227    227       Proton acceptor (By similarity).
FT   BINDING     129    129       ATP.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      78     78       Phosphoserine (By similarity).
FT   MOD_RES      88     88       Phosphoserine (By similarity).
FT   MOD_RES     255    255       Phosphoserine (By similarity).
FT   MOD_RES     389    389       Phosphothreonine (By similarity).
FT   MOD_RES     392    392       Phosphoserine (By similarity).
FT   MUTAGEN     129    129       K->R: Loss of ATP-binding.
SQ   SEQUENCE   397 AA;  44114 MW;  B99C6688184E5B3D CRC64;
     MAAPSPSGGG GSGGGGGTPG PIGPPASGHP AVSSMQGKRK ALKLNFANPP VKSTARFTLN
     PNTTGVQNPH IERLRTHSIE SSGKLKISPE QHWDFTAEDL KDLGEIGRGA YGSVNKMVHK
     PSGQIMAVKR IRSTVDEKEQ KQLLMDLDVV MRSSDCPYIV QFYGALFREG DCWICMELMS
     TSFDKFYKYV YSVLDDVIPE EILGKITLAT VKALNHLKEN LKIIHRDIKP SNILLDRSGN
     IKLCDFGISG QLVDSIAKTR DAGCRPYMAP ERIDPSASRQ GYDVRSDVWS LGITLYELAT
     GRFPYPKWNS VFDQLTQVVK GDPPQLSNSE EREFSPSFIN FVNLCLTKDE SKRPKYKELL
     KHPFILMYEE RTVEVACYVC KILDQMPATP SSPMYVD
//
ID   K6PF_MOUSE              Reviewed;         780 AA.
AC   P47857; O35513; Q543L1; Q9JK94;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 109.
DE   RecName: Full=6-phosphofructokinase, muscle type;
DE            EC=2.7.1.11;
DE   AltName: Full=Phosphofructo-1-kinase isozyme A;
DE            Short=PFK-A;
DE            Short=Phosphofructokinase-M;
DE   AltName: Full=Phosphofructokinase 1;
DE   AltName: Full=Phosphohexokinase;
GN   Name=Pfkm; Synonyms=Pfk-m, Pfka;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss; TISSUE=Brain;
RX   PubMed=11137296; DOI=10.1016/S0378-1119(00)00463-7;
RA   Gunasekera D., Kemp R.G.;
RT   "Genomic organization, 5'flanking region and tissue-specific
RT   expression of mouse phosphofructokinase C gene.";
RL   Gene 260:103-112(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-212 AND 259-345.
RC   STRAIN=ICR;
RX   MEDLINE=95071243; PubMed=7980403;
RA   Nakajima H., Noguchi T., Hamaguchi T., Tomita K., Hanafusa T.,
RA   Kono N., Tanaka T., Kuwajima M., Matsuzawa Y.;
RT   "Expression of mouse phosphofructokinase-M gene alternative
RT   transcripts: evidence for the conserved two-promoter system.";
RL   Biochem. J. 303:449-453(1994).
RN   [4]
RP   PROTEIN SEQUENCE OF 367-374, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
CC       fructose 1,6-bisphosphate.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: Allosteric enzyme activated by ADP, AMP, or
CC       fructose bisphosphate and inhibited by ATP or citrate.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase family. Two domains
CC       subfamily.
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DR   EMBL; AF249894; AAF63762.1; -; mRNA.
DR   EMBL; AK002711; BAB22303.1; -; mRNA.
DR   EMBL; AK049773; BAC33913.1; -; mRNA.
DR   EMBL; D21864; BAA21892.1; -; Genomic_DNA.
DR   EMBL; D21865; BAA21012.1; -; mRNA.
DR   IPI; IPI00331541; -.
DR   PIR; S53317; S53317.
DR   RefSeq; NP_001156959.1; NM_001163487.1.
DR   RefSeq; NP_001156960.1; NM_001163488.1.
DR   RefSeq; NP_067489.3; NM_021514.4.
DR   UniGene; Mm.272582; -.
DR   ProteinModelPortal; P47857; -.
DR   SMR; P47857; 16-362, 400-745.
DR   STRING; P47857; -.
DR   PhosphoSite; P47857; -.
DR   PRIDE; P47857; -.
DR   Ensembl; ENSMUST00000051226; ENSMUSP00000059801; ENSMUSG00000033065.
DR   GeneID; 18642; -.
DR   KEGG; mmu:18642; -.
DR   NMPDR; fig|10090.3.peg.30538; -.
DR   UCSC; uc007xlv.1; mouse.
DR   CTD; 18642; -.
DR   MGI; MGI:97548; Pfkm.
DR   eggNOG; roNOG13737; -.
DR   HOGENOM; HBG324640; -.
DR   HOVERGEN; HBG000976; -.
DR   InParanoid; P47857; -.
DR   OMA; CMTCDRI; -.
DR   OrthoDB; EOG4RJG0W; -.
DR   PhylomeDB; P47857; -.
DR   BRENDA; 2.7.1.11; 244.
DR   PMAP-CutDB; P47857; -.
DR   ArrayExpress; P47857; -.
DR   Bgee; P47857; -.
DR   CleanEx; MM_PFKM; -.
DR   Genevestigator; P47857; -.
DR   GermOnline; ENSMUSG00000033065; Mus musculus.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0006096; P:glycolysis; IDA:MGI.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; IMP:MGI.
DR   InterPro; IPR009161; 6-phosphofructokinase_euk.
DR   InterPro; IPR022953; Phosphofructokinase.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   Pfam; PF00365; PFK; 2.
DR   PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Ppfruckinase; 2.
DR   TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; ATP-binding; Direct protein sequencing; Glycolysis;
KW   Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Repeat; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    780       6-phosphofructokinase, muscle type.
FT                                /FTId=PRO_0000112018.
FT   NP_BIND      35     39       ATP (By similarity).
FT   NP_BIND     193    197       ATP (By similarity).
FT   NP_BIND     210    226       ATP (By similarity).
FT   ACT_SITE    166    166       Proton acceptor (By similarity).
FT   METAL       224    224       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     201    201       Substrate (By similarity).
FT   BINDING     292    292       Substrate (By similarity).
FT   BINDING     298    298       Substrate (By similarity).
FT   BINDING     301    301       Substrate (By similarity).
FT   MOD_RES       2      2       Phosphothreonine (By similarity).
FT   MOD_RES     775    775       Phosphoserine (By similarity).
SQ   SEQUENCE   780 AA;  85269 MW;  7917C7AC108B25C7 CRC64;
     MTHEEHHAAK TLGIGKAIAV LTSGGDAQGM NAAVRAVVRV GIFTGARVFF VHEGYQGLVD
     GGEHIREATW ESVSMMLQLG GTVIGSARCK DFREREGRLR AAHNLVKRGI TNLCVIGGDG
     SLTGADTFRS EWSDLLNDLQ KDGKITAEEA TKSSYLNIVG LVGSIDNDFC GTDMTIGTDS
     ALHRIVEIVD AITTTAQSHQ RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDDWE
     EHLCRRLSET RTRGSRLNII IVAEGAIDKN GKPITSEDIK NLVVKRLGYD TRVTVLGHVQ
     RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NQAVRLPLME CVQVTKDVTK
     AMDEKRFDEA IKLRGRSFMN NWEVYKLLAH VRPPVSKGGL HTVAVMNVGA PAAGMNAAVR
     STVRIGLIQG NRVLVVHDGF EGLAKGQIEE AGWSYVGGWT GQGGSKLGTK RTLPKKNLEQ
     ISANITKFNI QGLVIIGGFE AYTGGLELME GRKQFDELCI PFVVIPATVS NNVPGSDFSI
     GADTALNTIC TTCDRIKQSA AGTKRRVFII ETMGGYCGYL ATMAGLAAGA DAAYIFEEPF
     TIRDLQVNVE HLVQKMKTTV KRGLVLRNEK CNENYTTDFI FNLYSEEGKG IFDSRKNVLG
     HMQQGGSPTP FDRNFATKMG AKAMNWMSGK IKESYRNGRI FANTPDSGCV LGMRKRALVF
     QPVTELKDQT DFEHRIPKEQ WWLKLRPILK ILAKYEIDLD TSDHAHLEHI SRKRSGEAAV
//
ID   SCG3_MOUSE              Reviewed;         471 AA.
AC   P47867;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Secretogranin-3;
DE   AltName: Full=Secretogranin III;
DE            Short=SgIII;
DE   Flags: Precursor;
GN   Name=Scg3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=95001263; PubMed=7917832; DOI=10.1007/BF02821554;
RA   Dopazo A., Lovenberg T.W., Danielson P.E., Ottiger H.-P.,
RA   Sutcliffe J.G.;
RT   "Primary structure of mouse secretogranin III and its absence from
RT   deficient mice.";
RL   J. Mol. Neurosci. 4:225-233(1993).
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Neuroendocrine and endocrine
CC       secretory granules.
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DR   EMBL; U02982; AAA56636.1; -; mRNA.
DR   IPI; IPI00112446; -.
DR   RefSeq; NP_033156.1; NM_009130.3.
DR   UniGene; Mm.2386; -.
DR   ProteinModelPortal; P47867; -.
DR   STRING; P47867; -.
DR   PhosphoSite; P47867; -.
DR   PRIDE; P47867; -.
DR   Ensembl; ENSMUST00000034699; ENSMUSP00000034699; ENSMUSG00000032181.
DR   GeneID; 20255; -.
DR   KEGG; mmu:20255; -.
DR   UCSC; uc009qss.1; mouse.
DR   CTD; 20255; -.
DR   MGI; MGI:103032; Scg3.
DR   eggNOG; roNOG11872; -.
DR   HOGENOM; HBG715607; -.
DR   HOVERGEN; HBG057085; -.
DR   InParanoid; P47867; -.
DR   OMA; VQKIATR; -.
DR   OrthoDB; EOG4STS4Q; -.
DR   PhylomeDB; P47867; -.
DR   NextBio; 297909; -.
DR   ArrayExpress; P47867; -.
DR   Bgee; P47867; -.
DR   CleanEx; MM_SCG3; -.
DR   Genevestigator; P47867; -.
DR   GermOnline; ENSMUSG00000032181; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Secreted; Signal.
FT   SIGNAL        1     22       Potential.
FT   CHAIN        23    471       Secretogranin-3.
FT                                /FTId=PRO_0000005462.
SQ   SEQUENCE   471 AA;  53326 MW;  FC1E9C381AFCA564 CRC64;
     MGFLWTGSWI LVLVLNSGPI QAFPKPEGSQ DKSLHNRELS AERPLNEQIA EAEADKIKKA
     FPSESKPSES NYSSVDNLNL LRAITEKETV EKERQSIRSP PFDNQLNVED ADSTKNRKLI
     DEYDSTKSGL DHKFQDDPDG LHQLDGTPLT AEDIVHKIAT RIYEENDRGV FDKIVSKLLN
     LGLITESQAH TLEDEVAEAL QKLISKEANN YEETLDKPTS RTENQDGKIP EKVTPVAAVQ
     DGFTNRENDE TVSNTLTLSN GLERRTNPHR EDDFEELQYF PNFYALLTSI DSEKEAKEKE
     TLITIMKTLI DFVKMMVKYG TISPEEGVSY LENLDETIAL QTKNKLEKNT TDSKSKLFPA
     PPEKSQEETD STKEEAAKME KEYGSLKDST KDDNSNLGGK TDEATGKTEA YLEAIRKNIE
     WLKKHNKKGN KEDYDLSKMR DFINQQADAY VEKGILDKEE ANAIKRIYSS L
//
ID   NK3R_MOUSE              Reviewed;         452 AA.
AC   P47937; Q61968; Q8BL44; Q9JKN0;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2003, sequence version 2.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Neuromedin-K receptor;
DE            Short=NKR;
DE   AltName: Full=NK-3 receptor;
DE            Short=NK-3R;
DE   AltName: Full=Neurokinin B receptor;
DE   AltName: Full=Tachykinin receptor 3;
GN   Name=Tacr3; Synonyms=Tac3r;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Feild J.A., Brun K.A.;
RT   "Molecular cloning and characterization of the murine neurokinin-3
RT   receptor.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-385.
RC   TISSUE=Brain;
RA   Maroteaux L.;
RL   Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 103-328.
RC   STRAIN=CBA; TISSUE=Brain;
RX   MEDLINE=94165478; PubMed=8120392;
RA   Cook G.A., Elliott D., Metwali A., Blum A.M., Sandor M., Lynch R.,
RA   Weinstock J.V.;
RT   "Molecular evidence that granuloma T lymphocytes in murine
RT   schistosomiasis mansoni express an authentic substance P (NK-1)
RT   receptor.";
RL   J. Immunol. 152:1830-1835(1994).
CC   -!- FUNCTION: This is a receptor for the tachykinin neuropeptide
CC       neuromedin-K (neurokinin B). It is associated with G proteins that
CC       activate a phosphatidylinositol-calcium second messenger system.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- PTM: The anchoring of this receptor to the plasma membrane is
CC       probably mediated by the palmitoylation of a cysteine residue.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
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DR   EMBL; AF233341; AAF62517.1; -; mRNA.
DR   EMBL; AK031898; BAC27596.1; -; mRNA.
DR   EMBL; AK046424; BAC32723.1; -; mRNA.
DR   EMBL; X87823; CAA61088.1; -; mRNA.
DR   EMBL; L27827; AAA17893.1; -; mRNA.
DR   IPI; IPI00123197; -.
DR   PIR; S55524; S55524.
DR   RefSeq; NP_067357.1; NM_021382.6.
DR   UniGene; Mm.103810; -.
DR   ProteinModelPortal; P47937; -.
DR   SMR; P47937; 70-358.
DR   STRING; P47937; -.
DR   PRIDE; P47937; -.
DR   Ensembl; ENSMUST00000029822; ENSMUSP00000029822; ENSMUSG00000028172.
DR   GeneID; 21338; -.
DR   KEGG; mmu:21338; -.
DR   UCSC; uc008rky.1; mouse.
DR   CTD; 21338; -.
DR   MGI; MGI:892968; Tacr3.
DR   eggNOG; roNOG11982; -.
DR   HOGENOM; HBG443644; -.
DR   HOVERGEN; HBG103412; -.
DR   InParanoid; P47937; -.
DR   OMA; PTRQSSM; -.
DR   OrthoDB; EOG41NTM9; -.
DR   PhylomeDB; P47937; -.
DR   NextBio; 300508; -.
DR   ArrayExpress; P47937; -.
DR   Bgee; P47937; -.
DR   CleanEx; MM_TACR3; -.
DR   Genevestigator; P47937; -.
DR   GermOnline; ENSMUSG00000028172; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR001681; Neurokn_rcpt.
DR   InterPro; IPR001013; NK3_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01026; NEUROKININ3R.
DR   PRINTS; PR00244; NEUROKININR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Receptor; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN         1    452       Neuromedin-K receptor.
FT                                /FTId=PRO_0000069900.
FT   TOPO_DOM      1     71       Extracellular (Potential).
FT   TRANSMEM     72     94       Helical; Name=1; (Potential).
FT   TOPO_DOM     95    104       Cytoplasmic (Potential).
FT   TRANSMEM    105    126       Helical; Name=2; (Potential).
FT   TOPO_DOM    127    146       Extracellular (Potential).
FT   TRANSMEM    147    168       Helical; Name=3; (Potential).
FT   TOPO_DOM    169    188       Cytoplasmic (Potential).
FT   TRANSMEM    189    209       Helical; Name=4; (Potential).
FT   TOPO_DOM    210    232       Extracellular (Potential).
FT   TRANSMEM    233    257       Helical; Name=5; (Potential).
FT   TOPO_DOM    258    286       Cytoplasmic (Potential).
FT   TRANSMEM    287    308       Helical; Name=6; (Potential).
FT   TOPO_DOM    309    321       Extracellular (Potential).
FT   TRANSMEM    322    346       Helical; Name=7; (Potential).
FT   TOPO_DOM    347    452       Cytoplasmic (Potential).
FT   LIPID       361    361       S-palmitoyl cysteine (Potential).
FT   CARBOHYD      9      9       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     23     23       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     40     40       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     60     60       N-linked (GlcNAc...) (Potential).
FT   DISULFID    145    220       By similarity.
FT   CONFLICT     59     59       A -> D (in Ref. 3; CAA61088).
FT   CONFLICT    198    198       A -> S (in Ref. 4; AAA17893).
FT   CONFLICT    267    267       P -> L (in Ref. 3; CAA61088).
FT   CONFLICT    385    385       S -> P (in Ref. 3; CAA61088).
SQ   SEQUENCE   452 AA;  51026 MW;  7A46D400AD7FC444 CRC64;
     MASVPTGENW TDGTAGVGSH TGNLSAALGI TEWLALQAGN FSSALGLPVT SQAPSQVRAN
     LTNQFVQPSW RIALWSLAYG LVVAVAVFGN LIVIWIILAH KRMRTVTNYF LVNLAFSDAS
     VAAFNTLVNF IYGVHSEWYF GANYCRFQNF FPITAVFASI YSMTAIAVDR YMAIIDPLKP
     RLSATATKIV IGSIWILAFL LAFPQCLYSK IKVMPGRTLC YVQWPEGPKQ HFTYHIIVII
     LVYCFPLLIM GVTYTIVGIT LWGGEIPGDT CDKYHEQLKA KRKVVKMMII VVVTFAICWL
     PYHVYFILTA IYQQLNRWKY IQQVYLASFW LAMSSTMYNP IIYCCLNKRF RAGFKRAFRW
     CPFIQVSSYD ELELKTTRFH PTRQSSLYTV SRMESVTVLY DPSEGDPAKS SRKKRAVPRD
     PSANGCSHRE FKSASTTSSF ISSPYTSVDE YS
//
ID   CRKL_MOUSE              Reviewed;         303 AA.
AC   P47941; Q3TQ18; Q8BGC5;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Crk-like protein;
GN   Name=Crkl; Synonyms=Crkol;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL X CBA; TISSUE=Placenta;
RX   MEDLINE=96038874; PubMed=7478571;
RA   de Jong R.L., Haataja L., Voncken J.W., Heisterkamp N., Groffen J.;
RT   "Tyrosine phosphorylation of murine Crkl.";
RL   Oncogene 11:1469-1474(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic head, and Embryonic heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   INTERACTION WITH INPP5D.
RX   PubMed=11031258; DOI=10.1074/jbc.M006250200;
RA   Sattler M., Verma S., Pride Y.B., Salgia R., Rohrschneider L.R.,
RA   Griffin J.D.;
RT   "SHIP1, an SH2 domain containing polyinositol-5-phosphatase, regulates
RT   migration through two critical tyrosine residues and forms a novel
RT   signaling complex with DOK1 and CRKL.";
RL   J. Biol. Chem. 276:2451-2458(2001).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-251, AND MASS
RP   SPECTROMETRY.
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-132 AND TYR-207, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: May mediate the transduction of intracellular signals.
CC   -!- SUBUNIT: Interacts with DOCK2 and EPOR. Interacts with
CC       phosphorylated CBLB and IRS4 (By similarity). Interacts with
CC       INPP5D/SHIP1.
CC   -!- PTM: Phosphorylated on tyrosine. Phosphorylation is prominent
CC       during early development, but decreases at later embryonic stages
CC       and in newborn mice.
CC   -!- SIMILARITY: Belongs to the CRK family.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
CC   -!- SIMILARITY: Contains 2 SH3 domains.
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DR   EMBL; X90648; CAA62220.1; -; mRNA.
DR   EMBL; AK048641; BAC33406.1; -; mRNA.
DR   EMBL; AK052315; BAC34933.1; -; mRNA.
DR   EMBL; AK163981; BAE37567.1; -; mRNA.
DR   IPI; IPI00113362; -.
DR   PIR; S58352; S58352.
DR   RefSeq; NP_031790.2; NM_007764.4.
DR   UniGene; Mm.21048; -.
DR   UniGene; Mm.451241; -.
DR   ProteinModelPortal; P47941; -.
DR   SMR; P47941; 3-180, 237-298.
DR   STRING; P47941; -.
DR   PhosphoSite; P47941; -.
DR   REPRODUCTION-2DPAGE; IPI00113362; -.
DR   PRIDE; P47941; -.
DR   Ensembl; ENSMUST00000006293; ENSMUSP00000006293; ENSMUSG00000006134.
DR   GeneID; 12929; -.
DR   KEGG; mmu:12929; -.
DR   UCSC; uc007ykv.1; mouse.
DR   CTD; 12929; -.
DR   MGI; MGI:104686; Crkl.
DR   HOGENOM; HBG314739; -.
DR   HOVERGEN; HBG105616; -.
DR   InParanoid; P47941; -.
DR   OMA; QNRLQGQ; -.
DR   OrthoDB; EOG4NS3C3; -.
DR   PhylomeDB; P47941; -.
DR   NextBio; 282596; -.
DR   ArrayExpress; P47941; -.
DR   Bgee; P47941; -.
DR   Genevestigator; P47941; -.
DR   GermOnline; ENSMUSG00000006134; Mus musculus.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0009952; P:anterior/posterior pattern formation; IGI:MGI.
DR   GO; GO:0001568; P:blood vessel development; IGI:MGI.
DR   GO; GO:0007507; P:heart development; IGI:MGI.
DR   GO; GO:0009887; P:organ morphogenesis; IMP:MGI.
DR   GO; GO:0060017; P:parathyroid gland development; IGI:MGI.
DR   GO; GO:0048538; P:thymus development; IGI:MGI.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 2.
DR   SUPFAM; SSF50044; SH3; 2.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Repeat; SH2 domain; SH3 domain.
FT   CHAIN         1    303       Crk-like protein.
FT                                /FTId=PRO_0000079348.
FT   DOMAIN       14    102       SH2.
FT   DOMAIN      123    183       SH3 1.
FT   DOMAIN      235    296       SH3 2.
FT   MOD_RES     107    107       Phosphoserine.
FT   MOD_RES     127    127       Phosphotyrosine (By similarity).
FT   MOD_RES     132    132       Phosphotyrosine.
FT   MOD_RES     198    198       Phosphotyrosine (By similarity).
FT   MOD_RES     207    207       Phosphotyrosine.
FT   MOD_RES     251    251       Phosphotyrosine.
FT   CONFLICT    165    165       N -> T (in Ref. 1; CAA62220).
SQ   SEQUENCE   303 AA;  33830 MW;  A8C801F78EF73573 CRC64;
     MSSARFDSSD RSAWYMGPVT RQEAQTRLQG QRHGMFLVRD SSTCPGDYVL SVSENSRVSH
     YIINSLPNRR FKIGDQEFDH LPALLEFYKI HYLDTTTLIE PAPRYPSPPV GSVSAPNLPT
     AEENLEYVRT LYDFPGNDAE DLPFKKGELL VIIEKPEEQW WSARNKDGRV GMIPVPYVEK
     LVRSSPHGKH GNRNSNSYGI PEPAHAYAQP QTTTPLPTVA STPGAAINPL PSTQNGPVFA
     KAIQKRVPCA YDKTALALEV GDIVKVTRMN INGQWEGEVN GRKGLFPFTH VKIFDPQNPD
     DNE
//
ID   RLA1_MOUSE              Reviewed;         114 AA.
AC   P47955;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=60S acidic ribosomal protein P1;
GN   Name=Rplp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Crowe D.L., Cui X.M., Shuler C.F.;
RL   Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-104, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-104, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-104, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-104, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-104, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-104, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-104, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND SER-104, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Plays an important role in the elongation step of
CC       protein synthesis.
CC   -!- SUBUNIT: P1 and P2 exist as dimers at the large ribosomal subunit.
CC   -!- SIMILARITY: Belongs to the ribosomal protein L12P family.
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DR   EMBL; U29402; AAA70106.1; -; mRNA.
DR   EMBL; AK007832; BAB25292.1; -; mRNA.
DR   EMBL; AK010656; BAB27095.1; -; mRNA.
DR   EMBL; AK088070; BAC40128.1; -; mRNA.
DR   EMBL; BC058685; AAH58685.1; -; mRNA.
DR   IPI; IPI00113377; -.
DR   RefSeq; NP_061341.1; NM_018853.3.
DR   UniGene; Mm.3158; -.
DR   ProteinModelPortal; P47955; -.
DR   SMR; P47955; 7-64.
DR   STRING; P47955; -.
DR   PhosphoSite; P47955; -.
DR   PRIDE; P47955; -.
DR   Ensembl; ENSMUST00000008036; ENSMUSP00000008036; ENSMUSG00000007892.
DR   GeneID; 56040; -.
DR   KEGG; mmu:56040; -.
DR   UCSC; uc009pzt.1; mouse.
DR   CTD; 56040; -.
DR   MGI; MGI:1927099; Rplp1.
DR   eggNOG; roNOG17883; -.
DR   HOGENOM; HBG631105; -.
DR   HOVERGEN; HBG002291; -.
DR   InParanoid; P47955; -.
DR   OMA; MASTSEL; -.
DR   OrthoDB; EOG44J2KS; -.
DR   NextBio; 311800; -.
DR   Bgee; P47955; -.
DR   CleanEx; MM_RPLP1; -.
DR   Genevestigator; P47955; -.
DR   GermOnline; ENSMUSG00000007892; Mus musculus.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006414; P:translational elongation; IEA:InterPro.
DR   InterPro; IPR001813; Ribosomal_60S.
DR   Pfam; PF00428; Ribosomal_60s; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein; Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    114       60S acidic ribosomal protein P1.
FT                                /FTId=PRO_0000157687.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       5      5       Phosphoserine (By similarity).
FT   MOD_RES      11     11       Phosphotyrosine (By similarity).
FT   MOD_RES      12     12       Phosphoserine (By similarity).
FT   MOD_RES     101    101       Phosphoserine.
FT   MOD_RES     104    104       Phosphoserine.
SQ   SEQUENCE   114 AA;  11475 MW;  63C344A2772350D2 CRC64;
     MASVSELACI YSALILHDDE VTVTEDKINA LIKAAGVSVE PFWPGLFAKA LANVNIGSLI
     CNVGAGGPAP AAGAAPAGGA APSTAAAPAE EKKVEAKKEE SEESEDDMGF GLFD
//
ID   GLRB_MOUSE              Reviewed;         496 AA.
AC   P48168;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Glycine receptor subunit beta;
DE   AltName: Full=Glycine receptor 58 kDa subunit;
DE   Flags: Precursor;
GN   Name=Glrb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=95004576; PubMed=7920630; DOI=10.1038/ng0694-136;
RA   Kingsmore S.F., Giros B., Suh D., Bieniarz M., Caron M.G.,
RA   Seldin M.F.;
RT   "Glycine receptor beta-subunit gene mutation in spastic mouse
RT   associated with LINE-1 element insertion.";
RL   Nat. Genet. 7:136-141(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS SPASTIC.
RC   STRAIN=BALB/c, and C57BL/6; TISSUE=Brain, and Liver;
RX   MEDLINE=95033198; PubMed=7946325; DOI=10.1016/0896-6273(94)90265-8;
RA   Muelhardt C., Fischer M., Gass P., Simon-Chazottes D., Guenet J.-L.,
RA   Kuhse J., Betz H., Becker C.M.;
RT   "The spastic mouse: aberrant splicing of glycine receptor beta subunit
RT   mRNA caused by intronic insertion of L1 element.";
RL   Neuron 13:1003-1015(1994).
CC   -!- FUNCTION: The glycine receptor is a neurotransmitter-gated ion
CC       channel. Binding of glycine to its receptor increases the chloride
CC       conductance and thus produces hyperpolarization (inhibition of
CC       neuronal firing).
CC   -!- SUBUNIT: Pentamer composed of alpha and beta subunits. Interacts
CC       with GPHN (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane; Multi-pass membrane protein. Cell membrane; Multi-pass
CC       membrane protein.
CC   -!- TISSUE SPECIFICITY: High levels of expression in cortex,
CC       hippocampus, thalamus and cerebellum.
CC   -!- DISEASE: Note=Defects in Glrb cause the spastic condition which is
CC       characterized by muscle rigidity, tremors, myoclonic jerks,
CC       pronounced startle reaction, abnormal gait and impaired righting
CC       ability.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
CC       family. Glycine receptor (TC 1.A.9.3) subfamily. GLRB sub-
CC       subfamily.
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DR   EMBL; U09399; AAA61874.1; -; mRNA.
DR   EMBL; X81202; CAA57076.1; -; mRNA.
DR   EMBL; X81201; CAA57075.1; -; Genomic_DNA.
DR   EMBL; L32594; AAA65966.1; -; Genomic_DNA.
DR   IPI; IPI00108776; -.
DR   PIR; S46459; S46459.
DR   UniGene; Mm.275639; -.
DR   ProteinModelPortal; P48168; -.
DR   SMR; P48168; 79-355.
DR   MINT; MINT-4787310; -.
DR   STRING; P48168; -.
DR   PhosphoSite; P48168; -.
DR   PRIDE; P48168; -.
DR   Ensembl; ENSMUST00000029654; ENSMUSP00000029654; ENSMUSG00000028020.
DR   MGI; MGI:95751; Glrb.
DR   HOGENOM; HBG506497; -.
DR   HOVERGEN; HBG051707; -.
DR   InParanoid; P48168; -.
DR   OrthoDB; EOG4HMJ97; -.
DR   ArrayExpress; P48168; -.
DR   Bgee; P48168; -.
DR   CleanEx; MM_GLRB; -.
DR   Genevestigator; P48168; -.
DR   GermOnline; ENSMUSG00000028020; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016934; F:extracellular-glycine-gated chloride channel activity; IMP:MGI.
DR   GO; GO:0016594; F:glycine binding; IMP:MGI.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007340; P:acrosome reaction; IMP:MGI.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; ISS:UniProtKB.
DR   GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR   GO; GO:0060013; P:righting reflex; IMP:MGI.
DR   GO; GO:0001964; P:startle response; ISS:UniProtKB.
DR   GO; GO:0060012; P:synaptic transmission, glycinergic; IMP:MGI.
DR   GO; GO:0007601; P:visual perception; IMP:MGI.
DR   InterPro; IPR008060; Glycine_rcpt_B.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   Gene3D; G3DSA:2.70.170.10; Neur_chan_lig_bd; 1.
DR   PANTHER; PTHR18945:SF29; Glycine_rcpt_B; 1.
DR   PANTHER; PTHR18945; Neur_channel; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR01677; GLYRBETA.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF90112; Neu_channel_TM; 1.
DR   SUPFAM; SSF63712; Neur_chan_LBD; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Chloride; Chloride channel;
KW   Disease mutation; Disulfide bond; Glycoprotein; Ion transport;
KW   Ionic channel; Ligand-gated ion channel; Membrane;
KW   Postsynaptic cell membrane; Receptor; Signal; Synapse; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     22       By similarity.
FT   CHAIN        23    496       Glycine receptor subunit beta.
FT                                /FTId=PRO_0000000424.
FT   TOPO_DOM     23    265       Extracellular (Probable).
FT   TRANSMEM    266    290       Helical; (Probable).
FT   TRANSMEM    299    316       Helical; (Probable).
FT   TRANSMEM    331    354       Helical; (Probable).
FT   TOPO_DOM    355    477       Cytoplasmic (Probable).
FT   TRANSMEM    478    495       Helical; (Probable).
FT   CARBOHYD     54     54       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    242    242       N-linked (GlcNAc...) (Potential).
FT   DISULFID    183    197       By similarity.
FT   VARIANT      74     83       NFKGIPVDVV -> TTMLDIQPMI (in spastic 1).
FT   VARIANT      84    496       Missing (in spastic 1).
FT   VARIANT     143    151       LFFANEKSA -> VSMSWIYNR (in spastic 2).
FT   VARIANT     152    496       Missing (in spastic 2).
FT   CONFLICT    365    365       R -> A (in Ref. 2; CAA57076).
SQ   SEQUENCE   496 AA;  56036 MW;  555FDFA8918437BE CRC64;
     MKFSLAISFF ILMSLLFEDA CAKEKSSKKG KGKKKQYLCP SQQSPEDLAR VPPNSTSNIL
     NRLLVSYDPR IRPNFKGIPV DVVVNIFINS FGSIQETTMD YRVNIFLRQK WNDPRLKLPS
     DFRGSDALTV DPTMYKCLWK PDLFFANEKS ANFHDVTQEN ILLFIFRDGD VLVSMRLSIT
     LSCPLDLTLF PMDTQRCKMQ LESFGYTTDD LRFIWQSGDP VQLEKIALPQ FDIKKEDIEY
     GNCTKYYKGT GYYTCVEVIF TLRRQVGFYM MGVYAPTLLI VVLSWLSFWI NPDASAARVP
     LGIFSVLSLA SECTTLAAEL PKVSYVKALD VWLIACLLFG FASLVEYAVV QVMLNNPKRV
     EAEKRRIAKA EQADGKGGNA AKKNTVNGTG TPVHISTLQV GETRCKKVCT SKSDLRSNDF
     SIVGSLPRDF ELSNYDCYGK PIEVNNGLGK PQAKNKKPPP AKPVIPTAAK RIDLYARALF
     PFCFLFFNVI YWSIYL
//
ID   41_MOUSE                Reviewed;         858 AA.
AC   P48193; A2A843; Q5DTQ8; Q68FF1; Q6NVF5;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   30-NOV-2010, entry version 95.
DE   RecName: Full=Protein 4.1;
DE            Short=P4.1;
DE   AltName: Full=4.1R;
DE   AltName: Full=Band 4.1;
GN   Name=Epb41; Synonyms=Epb4.1, Kiaa4056;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND ALTERNATIVE SPLICING.
RC   STRAIN=BALB/c;
RX   MEDLINE=93155238; PubMed=8429050;
RA   Huang J.-P., Tang C.-J.C., Kou G.-H., Marchesi V.T., Benz E.J. Jr.,
RA   Tang T.K.;
RT   "Genomic structure of the locus encoding protein 4.1. Structural basis
RT   for complex combinational patterns of tissue-specific alternative RNA
RT   splicing.";
RL   J. Biol. Chem. 268:3758-3766(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 709-713, MASS SPECTROMETRY, AND CHARACTERIZATION
RP   OF CARBOXY-TERMINAL DOMAIN.
RX   MEDLINE=21325946; PubMed=11432737;
RX   DOI=10.1046/j.1432-1327.2001.02276.x;
RA   Scott C., Phillips G.W., Baines A.J.;
RT   "Properties of the C-terminal domain of 4.1 proteins.";
RL   Eur. J. Biochem. 268:3709-3717(2001).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-223, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541; SER-543 AND
RP   SER-556, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543 AND SER-668, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Protein 4.1 is a major structural element of the
CC       erythrocyte membrane skeleton. It plays a key role in regulating
CC       membrane physical properties of mechanical stability and
CC       deformability by stabilizing spectrin-actin interaction. Recruits
CC       DLG1 to membranes (By similarity).
CC   -!- SUBUNIT: Binds with a high affinity to glycophorin and with lower
CC       affinity to band III protein. Associates with the nuclear mitotic
CC       apparatus. Binds calmodulin and DLG1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Cytoplasm, cell cortex (By similarity). Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=A number of isoforms are produced;
CC       Name=1;
CC         IsoId=P48193-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P48193-2; Sequence=VSP_012874;
CC   -!- PTM: O-glycosylated; contains N-acetylglucosamine side chains in
CC       the C-terminal domain (By similarity).
CC   -!- PTM: Phosphorylated at multiple sites by different protein kinases
CC       and each phosphorylation event selectively modulates the protein's
CC       functions.
CC   -!- PTM: Phosphorylation on Tyr-654 reduces the ability of 4.1 to
CC       promote the assembly of the spectrin/actin/4.1 ternary complex.
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90280.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; L00919; AAA37122.1; -; mRNA.
DR   EMBL; L00919; AAA37123.1; -; mRNA.
DR   EMBL; AK220462; BAD90280.1; ALT_INIT; mRNA.
DR   EMBL; AL607088; CAM14971.1; -; Genomic_DNA.
DR   EMBL; AL669981; CAM14971.1; JOINED; Genomic_DNA.
DR   EMBL; AL669981; CAM21329.1; -; Genomic_DNA.
DR   EMBL; AL607088; CAM21329.1; JOINED; Genomic_DNA.
DR   EMBL; BC068138; AAH68138.1; -; mRNA.
DR   EMBL; BC079875; AAH79875.1; -; mRNA.
DR   IPI; IPI00395157; -.
DR   IPI; IPI00462873; -.
DR   PIR; A46613; A46613.
DR   RefSeq; NP_001122078.1; NM_001128606.1.
DR   RefSeq; NP_001122079.1; NM_001128607.1.
DR   RefSeq; NP_906273.3; NM_183428.3.
DR   UniGene; Mm.30038; -.
DR   ProteinModelPortal; P48193; -.
DR   SMR; P48193; 207-517.
DR   STRING; P48193; -.
DR   PhosphoSite; P48193; -.
DR   PRIDE; P48193; -.
DR   Ensembl; ENSMUST00000030739; ENSMUSP00000030739; ENSMUSG00000028906.
DR   Ensembl; ENSMUST00000084253; ENSMUSP00000081274; ENSMUSG00000028906.
DR   Ensembl; ENSMUST00000105972; ENSMUSP00000101592; ENSMUSG00000028906.
DR   Ensembl; ENSMUST00000105981; ENSMUSP00000101601; ENSMUSG00000028906.
DR   GeneID; 269587; -.
DR   KEGG; mmu:269587; -.
DR   NMPDR; fig|10090.3.peg.10484; -.
DR   UCSC; uc008vaj.1; mouse.
DR   CTD; 269587; -.
DR   MGI; MGI:95401; Epb4.1.
DR   HOVERGEN; HBG007777; -.
DR   PhylomeDB; P48193; -.
DR   NextBio; 392903; -.
DR   ArrayExpress; P48193; -.
DR   Bgee; P48193; -.
DR   CleanEx; MM_EPB4.1; -.
DR   Genevestigator; P48193; -.
DR   GermOnline; ENSMUSG00000028906; Mus musculus.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR   GO; GO:0019898; C:extrinsic to membrane; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
DR   InterPro; IPR008379; Band_4.1_C.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR021187; Band_41_protein.
DR   InterPro; IPR000798; Ez/rad/moesin.
DR   InterPro; IPR014847; FERM-adjacent.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR007477; SAB.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF05902; 4_1_CTD; 1.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF04382; SAB; 1.
DR   PIRSF; PIRSF002304; Membrane_skeletal_4_1; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Glycoprotein; Nucleus; Phosphoprotein.
FT   CHAIN         1    858       Protein 4.1.
FT                                /FTId=PRO_0000219391.
FT   DOMAIN      211    492       FERM.
FT   REGION      495    608       Hydrophilic.
FT   REGION      609    707       Spectrin--actin-binding.
FT   REGION      710    858       Carboxyl-terminal (CTD).
FT   MOD_RES      62     62       Phosphothreonine (By similarity).
FT   MOD_RES      94     94       Phosphoserine (By similarity).
FT   MOD_RES     192    192       Phosphoserine (By similarity).
FT   MOD_RES     223    223       Phosphotyrosine.
FT   MOD_RES     541    541       Phosphoserine.
FT   MOD_RES     543    543       Phosphoserine.
FT   MOD_RES     556    556       Phosphoserine.
FT   MOD_RES     654    654       Phosphotyrosine (By similarity).
FT   MOD_RES     668    668       Phosphoserine.
FT   MOD_RES     706    706       Phosphoserine (By similarity).
FT   VAR_SEQ     610    663       Missing (in isoform 2).
FT                                /FTId=VSP_012874.
FT   CONFLICT      1      3       MTT -> EPLKGREPRRARTRPGPARPGPCQVPVLCSP
FT                                (in Ref. 4; AAH68138).
FT   CONFLICT      8      8       A -> V (in Ref. 1; AAA37123).
FT   CONFLICT    232    233       KG -> NL (in Ref. 1; AAA37122).
FT   CONFLICT    443    443       Y -> S (in Ref. 1; AAA37122).
FT   CONFLICT    576    576       A -> R (in Ref. 1; AAA37122).
SQ   SEQUENCE   858 AA;  95911 MW;  7CF1CD52D790D1FD CRC64;
     MTTEKSLAAE AENSQHQQQK EEGEGATNSG QQETQLEEAS QAAAAEGSDQ GEQKLKASNG
     DTPTHEDLTK NKERTSESRG LSRLLSSFLK RPKSQVSEEE GREVESEKEK GEGGQKEIEL
     GNSLDEDIIL KAPIAAPEPE LKTDPSLDLH SLSSIETQPA QEEHREDPDS ETKEGEGIEE
     CSGTEVKEDP ESRAEREPEA SQKPVRRHRN MHCKVSLLDD TVYECVVEKH AKGQDLLKRV
     CEHLNLLEED YFGLALWDSA TSKTWLDSAK EIKKQVRGVP WNFTFNVKFY PPDPAQLTED
     ITRYYLCLQL RQDIVAGRLP CSFATLALLG SYTIQSELGD YDPELHGMDY VSDFKLAPNQ
     TKELEEKVME LHKSYRSMTP AQADLEFLEN AKKLSMYGVD LHKAKDLEGV DIILGVCSSG
     LLVYKDKLRI NRFPWPKVLK ISYKRSSFFI KIRPGEQEHY ESTIGFKLPS YRAAKKLWKV
     CVEHHTFFRL TSTDTIPKSK FLALGSKFRY SGRTQAQTRQ ASALIDRPAP HFERTASKRA
     SRSLDGAAAA ESTDRSPRPT SAPAIAQSQV TEGPGAPIKK TPKEAVKVEE KRGEEPAEPA
     EPEPTEAWKV EKTHTEVTVP TSNGDQTQKL AGKGEDLIRM RKKKRERLDG ENIYIRHSNL
     MLEDLDKSQE EIKKHHASIS ELKKNFMESV PEPRPSEWDK RLSTHSPFRT LNINGQVPTG
     DGPPLVKTQT VTISDTANAV KSEIPTKDVP IVHTETKTIT YEAAQTEDSN GDLDPGVLLT
     AQTITSETTS STTTTQITKT VKGGISETRI EKRIVITGDA DIDHDQVLVQ AIKEAKEQHP
     DMSVTKVVVH QETEISEE
//
ID   EDNRB_MOUSE             Reviewed;         442 AA.
AC   P48302; Q542M3;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Endothelin B receptor;
DE            Short=ET-B;
DE            Short=ET-BR;
DE   AltName: Full=Endothelin receptor non-selective type;
DE   Flags: Precursor;
GN   Name=Ednrb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=95094301; PubMed=8001159; DOI=10.1016/0092-8674(94)90017-5;
RA   Hosoda K., Hammer R.E., Richardson J.A., Baynash A.G., Cheung J.C.,
RA   Giaid A., Yanagisawa M.;
RT   "Targeted and natural (piebald-lethal) mutations of endothelin-B
RT   receptor gene produce megacolon associated with spotted coat color in
RT   mice.";
RL   Cell 79:1267-1276(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Non-specific receptor for endothelin 1, 2, and 3.
CC       Mediates its action by association with G proteins that activate a
CC       phosphatidylinositol-calcium second messenger system. Essential
CC       component in the normal development of two neuronal crest-derived
CC       cell lineages.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Endothelin receptor subfamily. EDNRB sub-subfamily.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; U32329; AAB60508.1; -; mRNA.
DR   EMBL; AK076426; BAC36337.1; -; mRNA.
DR   EMBL; AK082103; BAC38409.1; -; mRNA.
DR   EMBL; AK083415; BAC38908.1; -; mRNA.
DR   EMBL; AK085532; BAC39465.1; -; mRNA.
DR   EMBL; BC026553; AAH26553.1; -; mRNA.
DR   IPI; IPI00110848; -.
DR   RefSeq; NP_001129533.1; NM_001136061.1.
DR   RefSeq; NP_031930.1; NM_007904.3.
DR   UniGene; Mm.229532; -.
DR   ProteinModelPortal; P48302; -.
DR   SMR; P48302; 100-407.
DR   STRING; P48302; -.
DR   PhosphoSite; P48302; -.
DR   PRIDE; P48302; -.
DR   Ensembl; ENSMUST00000022718; ENSMUSP00000022718; ENSMUSG00000022122.
DR   GeneID; 13618; -.
DR   KEGG; mmu:13618; -.
DR   UCSC; uc007uww.1; mouse.
DR   CTD; 13618; -.
DR   MGI; MGI:102720; Ednrb.
DR   eggNOG; roNOG12252; -.
DR   HOGENOM; HBG445038; -.
DR   HOVERGEN; HBG051443; -.
DR   InParanoid; P48302; -.
DR   OMA; PVQKTAF; -.
DR   OrthoDB; EOG45HRX3; -.
DR   PhylomeDB; P48302; -.
DR   NextBio; 284288; -.
DR   ArrayExpress; P48302; -.
DR   Bgee; P48302; -.
DR   CleanEx; MM_EDNRB; -.
DR   Genevestigator; P48302; -.
DR   GermOnline; ENSMUSG00000022122; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001600; F:endothelin-B receptor activity; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0048484; P:enteric nervous system development; IDA:BHF-UCL.
DR   GO; GO:0030318; P:melanocyte differentiation; IDA:MGI.
DR   GO; GO:0010553; P:negative regulation of gene-specific transcription from RNA polymerase II promoter; IDA:BHF-UCL.
DR   GO; GO:0014043; P:negative regulation of neuron maturation; IDA:BHF-UCL.
DR   GO; GO:0001755; P:neural crest cell migration; IMP:MGI.
DR   GO; GO:0007422; P:peripheral nervous system development; IMP:MGI.
DR   GO; GO:0007497; P:posterior midgut development; IMP:MGI.
DR   GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR   GO; GO:0006885; P:regulation of pH; IMP:MGI.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR000499; Endthln_rcpt.
DR   InterPro; IPR001112; ETB_rcpt.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00571; ENDOTHELINBR.
DR   PRINTS; PR00366; ENDOTHELINR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Lipoprotein; Membrane; Palmitate; Receptor; Signal;
KW   Transducer; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     26       Potential.
FT   CHAIN        27    442       Endothelin B receptor.
FT                                /FTId=PRO_0000012730.
FT   TOPO_DOM     27    101       Extracellular (Potential).
FT   TRANSMEM    102    126       Helical; Name=1; (Potential).
FT   TOPO_DOM    127    137       Cytoplasmic (Potential).
FT   TRANSMEM    138    163       Helical; Name=2; (Potential).
FT   TOPO_DOM    164    175       Extracellular (Potential).
FT   TRANSMEM    176    197       Helical; Name=3; (Potential).
FT   TOPO_DOM    198    218       Cytoplasmic (Potential).
FT   TRANSMEM    219    243       Helical; Name=4; (Potential).
FT   TOPO_DOM    244    271       Extracellular (Potential).
FT   TRANSMEM    272    296       Helical; Name=5; (Potential).
FT   TOPO_DOM    297    324       Cytoplasmic (Potential).
FT   TRANSMEM    325    350       Helical; Name=6; (Potential).
FT   TOPO_DOM    351    362       Extracellular (Potential).
FT   TRANSMEM    363    389       Helical; Name=7; (Potential).
FT   TOPO_DOM    390    442       Cytoplasmic (Potential).
FT   LIPID       402    402       S-palmitoyl cysteine (Potential).
FT   LIPID       403    403       S-palmitoyl cysteine (Potential).
FT   LIPID       405    405       S-palmitoyl cysteine (Potential).
FT   CARBOHYD     60     60       N-linked (GlcNAc...) (Potential).
FT   DISULFID    174    255       By similarity.
SQ   SEQUENCE   442 AA;  49561 MW;  ED28A676F854B3D1 CRC64;
     MQSPASRCGR ALVALLLACG FLGVWGEKRG FPPAQATLSL LGTKEVMTPP TKTSWTRGSN
     SSLMRSSAPA EVTKGGRGAG VPPRSFPPPC QRNIEISKTF KYINTIVSCL VFVLGIIGNS
     TLLRIIYKNK CMRNGPNILI ASLALGDLLH IIIDIPINTY KLLAEDWPFG AEMCKLVPFI
     QKASVGITVL SLCALSIDRY RAVASWSRIK GIGVPKWTAV EIVLIWVVSV VLAVPEAIGF
     DMITSDYKGK PLRVCMLNPF QKTAFMQFYK TAKDWWLFSF YFCLPLAITA VFYTLMTCEM
     LRKKSGMQIA LNDHLKQRRE VAKTVFCLVL VFALCWLPLH LSRILKLTLY DQSNPHRCEL
     LSFLLVLDYI GINMASLNSC INPIALYLVS KRFKNCFKSC LCCWCQTFEE KQSLEEKQSC
     LKFKANDHGY DNFRSSNKYS SS
//
ID   DCE1_MOUSE              Reviewed;         593 AA.
AC   P48318; O08685;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2002, sequence version 2.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Glutamate decarboxylase 1;
DE            EC=4.1.1.15;
DE   AltName: Full=67 kDa glutamic acid decarboxylase;
DE            Short=GAD-67;
DE   AltName: Full=Glutamate decarboxylase 67 kDa isoform;
GN   Name=Gad1; Synonyms=Gad67;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=12106047; DOI=10.1111/j.1460-9568.1990.tb00412.x;
RA   Katarova Z., Szabo G., Mugnaini E., Greenspan R.;
RT   "Molecular identification of the 62 kd form of glutamic acid
RT   decarboxylase from the mouse.";
RL   Eur. J. Neurosci. 2:190-202(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RA   Aust G., Steinbrenner H., Thamm B., Rost A.K., Seissler J.;
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ILS, and ISS;
RX   MEDLINE=21363810; PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 198-403.
RC   TISSUE=Brain;
RX   MEDLINE=94062679; PubMed=8243324; DOI=10.1210/en.133.6.2962;
RA   Faulkner-Jones B.E., Cram D.S., Kun J., Harrison L.C.;
RT   "Localization and quantitation of expression of two glutamate
RT   decarboxylase genes in pancreatic beta-cells and other peripheral
RT   tissues of mouse and rat.";
RL   Endocrinology 133:2962-2972(1993).
CC   -!- FUNCTION: Catalyzes the production of GABA.
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Z49976; CAA90277.1; -; mRNA.
DR   EMBL; Y12257; CAA72934.1; -; mRNA.
DR   EMBL; AF483492; AAL90766.1; -; mRNA.
DR   EMBL; AF483493; AAL90767.1; -; mRNA.
DR   EMBL; BC027059; AAH27059.1; -; mRNA.
DR   EMBL; S67453; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00318496; -.
DR   PIR; S61534; S61534.
DR   RefSeq; NP_032103.2; NM_008077.4.
DR   UniGene; Mm.272120; -.
DR   ProteinModelPortal; P48318; -.
DR   SMR; P48318; 92-592.
DR   STRING; P48318; -.
DR   PhosphoSite; P48318; -.
DR   PRIDE; P48318; -.
DR   Ensembl; ENSMUST00000094934; ENSMUSP00000092539; ENSMUSG00000070880.
DR   GeneID; 14415; -.
DR   KEGG; mmu:14415; -.
DR   UCSC; uc008jzk.1; mouse.
DR   CTD; 14415; -.
DR   MGI; MGI:95632; Gad1.
DR   eggNOG; roNOG06194; -.
DR   HOGENOM; HBG433496; -.
DR   HOVERGEN; HBG004980; -.
DR   InParanoid; P48318; -.
DR   OMA; DFEAKIL; -.
DR   OrthoDB; EOG4QJRMS; -.
DR   BRENDA; 4.1.1.15; 244.
DR   NextBio; 285997; -.
DR   ArrayExpress; P48318; -.
DR   Bgee; P48318; -.
DR   CleanEx; MM_GAD1; -.
DR   Genevestigator; P48318; -.
DR   GermOnline; ENSMUSG00000070880; Mus musculus.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IMP:MGI.
DR   GO; GO:0048854; P:brain morphogenesis; IMP:MGI.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0021696; P:cerebellar cortex morphogenesis; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0035108; P:limb morphogenesis; IMP:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR   GO; GO:0061351; P:neural precursor cell proliferation; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0021772; P:olfactory bulb development; IMP:MGI.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase_major_dom.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   InterPro; IPR021115; Pyridoxal-P_BS.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1.
DR   PANTHER; PTHR11999; Pyridoxal_deC; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   2: Evidence at transcript level;
KW   Decarboxylase; Lyase; Neurotransmitter biosynthesis;
KW   Pyridoxal phosphate.
FT   CHAIN         1    593       Glutamate decarboxylase 1.
FT                                /FTId=PRO_0000146964.
FT   REGION      189    191       Substrate binding (By similarity).
FT   BINDING     566    566       Substrate (By similarity).
FT   MOD_RES     404    404       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
FT   CONFLICT    133    133       R -> H (in Ref. 1; CAA90277).
FT   CONFLICT    234    234       E -> K (in Ref. 5; S67453).
FT   CONFLICT    258    258       S -> T (in Ref. 1; CAA90277).
FT   CONFLICT    360    360       D -> S (in Ref. 1; CAA90277).
FT   CONFLICT    461    461       F -> N (in Ref. 1; CAA90277).
FT   CONFLICT    554    554       G -> A (in Ref. 1; CAA90277).
FT   CONFLICT    575    575       T -> S (in Ref. 1; CAA90277).
FT   CONFLICT    583    583       I -> T (in Ref. 1; CAA90277).
SQ   SEQUENCE   593 AA;  66648 MW;  82D1AAF216F25100 CRC64;
     MASSTPSPAT SSNAGADPNT TNLRPTTYDT WCGVAHGCTR KLGLKICGFL QRTNSLEEKS
     RLVSAFRERQ SSKNLLSCEN SDQGARFRRT ETDFSNLFAQ DLLPAKNGEE QTAQFLLEVV
     DILLNYVRKT FDRSTKVLDF HHPHQLLEGM EGFNLELSDH PESLEQILVD CRDTLKYGVR
     TGHPRFFNQL STGLDIIGLA GEWLTSTANT NMFTYEIAPV FVLMEQITLK KMREIVGWSN
     KDGDGIFSPG GAISNMYSIM AARYKYFPEV KTKGMAAVPK LVLFTSEHSH YSIKKAGAAL
     GFGTDNVILI KCNERGKIIP ADLEAKILDA KQKGYVPLYV NATAGTTVYG AFDPIQEIAD
     ICEKYNLWLH VDAAWGGGLL MSRKHRHKLS GIERANSVTW NPHKMMGVLL QCSAILVKEK
     GILQGCNQMC AGYLFQPDKQ YDVSYDTGDK AIQCGRHVDI FKFWLMWKAK GTVGFENQIN
     KCLELADYLY AKIKNREEFE MVFDGEPEHT NVCFWYIPQS LRGVPDSPER REKLHRVAPK
     IKALMMESGT TMVGYQPQGD KANFFRMVIS NPAATQSDID FLIEEIERLG QDL
//
ID   DCE2_MOUSE              Reviewed;         585 AA.
AC   P48320; O35519;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Glutamate decarboxylase 2;
DE            EC=4.1.1.15;
DE   AltName: Full=65 kDa glutamic acid decarboxylase;
DE            Short=GAD-65;
DE   AltName: Full=Glutamate decarboxylase 65 kDa isoform;
GN   Name=Gad2; Synonyms=Gad65;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=94032481; PubMed=8218409; DOI=10.1016/0167-4781(93)90056-J;
RA   Lee D.S., Tian J., Phan T., Kaufman D.L.;
RT   "Cloning and sequence analysis of a murine cDNA encoding glutamate
RT   decarboxylase (GAD65).";
RL   Biochim. Biophys. Acta 1216:157-160(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=97115675; PubMed=8954991; DOI=10.1006/bbrc.1996.1898;
RA   Asada H., Kawamura Y., Maruyama K., Kume H., Ding R.G., Ji F.Y.,
RA   Kanbara N., Kuzume H., Sanbo M., Yagi T., Obata K.;
RT   "Mice lacking the 65 kDa isoform of glutamic acid decarboxylase
RT   (GAD65) maintain normal levels of GAD67 and GABA in their brains but
RT   are susceptible to seizures.";
RL   Biochem. Biophys. Res. Commun. 229:891-895(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 175-379.
RC   TISSUE=Brain;
RX   MEDLINE=94062679; PubMed=8243324; DOI=10.1210/en.133.6.2962;
RA   Faulkner-Jones B.E., Cram D.S., Kun J., Harrison L.C.;
RT   "Localization and quantitation of expression of two glutamate
RT   decarboxylase genes in pancreatic beta-cells and other peripheral
RT   tissues of mouse and rat.";
RL   Endocrinology 133:2962-2972(1993).
CC   -!- FUNCTION: Catalyzes the production of GABA.
CC   -!- CATALYTIC ACTIVITY: L-glutamate = 4-aminobutanoate + CO(2).
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity).
CC       Cytoplasmic vesicle (By similarity). Cell junction, synapse,
CC       presynaptic cell membrane; Lipid-anchor (By similarity). Golgi
CC       apparatus membrane; Peripheral membrane protein; Cytoplasmic side
CC       (By similarity). Note=Associated to cytoplasmic vesicles. In
CC       neurons, cytosolic leaflet of Golgi membranes and presynaptic
CC       clusters (By similarity).
CC   -!- PTM: Phosphorylated; which does not affect kinetic parameters or
CC       subcellular location (By similarity).
CC   -!- PTM: Palmitoylated; which is required for presynaptic clustering
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; L16980; AAA93049.1; -; mRNA.
DR   EMBL; D42051; BAA22893.1; -; mRNA.
DR   EMBL; BC018380; AAH18380.1; -; mRNA.
DR   EMBL; S67454; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00318522; -.
DR   PIR; S38533; S38533.
DR   RefSeq; NP_032104.2; NM_008078.2.
DR   UniGene; Mm.4784; -.
DR   ProteinModelPortal; P48320; -.
DR   SMR; P48320; 88-584.
DR   STRING; P48320; -.
DR   PhosphoSite; P48320; -.
DR   PRIDE; P48320; -.
DR   Ensembl; ENSMUST00000028123; ENSMUSP00000028123; ENSMUSG00000026787.
DR   GeneID; 14417; -.
DR   KEGG; mmu:14417; -.
DR   UCSC; uc008ink.1; mouse.
DR   CTD; 14417; -.
DR   MGI; MGI:95634; Gad2.
DR   eggNOG; roNOG14341; -.
DR   HOGENOM; HBG433496; -.
DR   HOVERGEN; HBG004980; -.
DR   InParanoid; P48320; -.
DR   OMA; WRAKGTT; -.
DR   OrthoDB; EOG408N7N; -.
DR   PhylomeDB; P48320; -.
DR   BRENDA; 4.1.1.15; 244.
DR   NextBio; 286001; -.
DR   ArrayExpress; P48320; -.
DR   Bgee; P48320; -.
DR   CleanEx; MM_GAD2; -.
DR   Genevestigator; P48320; -.
DR   GermOnline; ENSMUSG00000026787; Mus musculus.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0042136; P:neurotransmitter biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase_major_dom.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   InterPro; IPR021115; Pyridoxal-P_BS.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1.
DR   PANTHER; PTHR11999; Pyridoxal_deC; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Cytoplasm; Cytoplasmic vesicle;
KW   Decarboxylase; Golgi apparatus; Lipoprotein; Lyase; Membrane;
KW   Neurotransmitter biosynthesis; Palmitate; Phosphoprotein;
KW   Pyridoxal phosphate; Synapse.
FT   CHAIN         1    585       Glutamate decarboxylase 2.
FT                                /FTId=PRO_0000146969.
FT   REGION      181    183       Substrate binding (By similarity).
FT   BINDING     558    558       Substrate (By similarity).
FT   MOD_RES       3      3       Phosphoserine (By similarity).
FT   MOD_RES       6      6       Phosphoserine (By similarity).
FT   MOD_RES      10     10       Phosphoserine (By similarity).
FT   MOD_RES      13     13       Phosphoserine (By similarity).
FT   MOD_RES     396    396       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
FT   LIPID        30     30       S-palmitoyl cysteine (By similarity).
FT   LIPID        45     45       S-palmitoyl cysteine (By similarity).
FT   CONFLICT    259    259       F -> S (in Ref. 2; BAA22893).
FT   CONFLICT    319    319       I -> S (in Ref. 4; S67454).
FT   CONFLICT    325    325       K -> E (in Ref. 2; BAA22893).
FT   CONFLICT    499    499       P -> S (in Ref. 2; BAA22893).
SQ   SEQUENCE   585 AA;  65224 MW;  C2F486E85123B057 CRC64;
     MASPGSGFWS FGSEDGSADP ENPGTARAWC QVAQKFTGGI GNKLCALLYG DSGKPAEGGG
     SVTSRAATGK VACTCDQKPC NCPKGDVNYA FLHATDLLPA CDGERPTLAF LQDVMNILLQ
     YVVKSFDRST KVIDFHYPNE LLQEYNWELA DQPQNLEEIL THCQTTLKYA IKTGHPRYFN
     QLSTGLDMVG LAADWLTSTA NTNMFTYEIA PVFVLLEYVT LKKMREIIGW PGGSGDGIFS
     PGGAISNMYA MLIARYKMFP EVKEKGMAAV PRLIAFTSEH SHFSLKKGAA ALGIGTDSVI
     LIKCDERGKM IPSDLERRIL EVKQKGFVPF LVSATAGTTV YGAFDPLLAV ADICKKYKIW
     MHVDAAWGGG LLMSRKHKWK LSGVERANSV TWNPHKMMGV PLQCSALLVR EEGLMQSCNQ
     MHASYLFQQD KHYDLSYDTG DKALQCGRHV DVFKLWLMWR AKGTTGFEAH IDKCLELAEY
     LYTIIKNREG YEMVFDGKPQ HTNVCFWFVP PSLRTLEDNE ERMSRLSKVA PVIKARMMEY
     GTTMVSYQPL GDKVNFFRMV ISNPAATHQD IDFLIEEIER LGQDL
//
ID   SOX2_MOUSE              Reviewed;         319 AA.
AC   P48432;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Transcription factor SOX-2;
GN   Name=Sox2; Synonyms=Sox-2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96067156; PubMed=7590241;
RA   Yuan H., Corbi N., Basilico C., Dailey L.;
RT   "Developmental-specific activity of the FGF-4 enhancer requires the
RT   synergistic action of Sox2 and Oct-3.";
RL   Genes Dev. 9:2635-2645(1995).
RN   [2]
RP   SEQUENCE REVISION.
RA   Yuan H., Corbi N., Basilico C., Dailey L.;
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129;
RX   MEDLINE=96189340; PubMed=8625802;
RA   Collignon J., Sockanathan S., Hacker A., Cohen-Tannoudji M.,
RA   Norris D., Rastan S., Stevanovic M., Goodfellow P.N., Lovell-Badge R.;
RT   "A comparison of the properties of Sox-3 with Sry and two related
RT   genes, Sox-1 and Sox-2.";
RL   Development 122:509-520(1996).
RN   [4]
RP   SUMOYLATION AT LYS-247, MUTAGENESIS OF LYS-247, SUBCELLULAR LOCATION,
RP   AND FUNCTION.
RX   PubMed=17097055; DOI=10.1016/j.bbrc.2006.10.130;
RA   Tsuruzoe S., Ishihara K., Uchimura Y., Watanabe S., Sekita Y.,
RA   Aoto T., Saitoh H., Yuasa Y., Niwa H., Kawasuji M., Baba H., Nakao M.;
RT   "Inhibition of DNA binding of Sox2 by the SUMO conjugation.";
RL   Biochem. Biophys. Res. Commun. 351:920-926(2006).
RN   [5]
RP   BIOTECHNOLOGY.
RX   PubMed=16904174; DOI=10.1016/j.cell.2006.07.024;
RA   Takahashi K., Yamanaka S.;
RT   "Induction of pluripotent stem cells from mouse embryonic and adult
RT   fibroblast cultures by defined factors.";
RL   Cell 126:663-676(2006).
RN   [6]
RP   INTERACTION WITH ZSCAN10.
RX   PubMed=19740739; DOI=10.1074/jbc.M109.016162;
RA   Yu H.B., Kunarso G., Hong F.H., Stanton L.W.;
RT   "Zfp206, Oct4, and Sox2 are integrated components of a transcriptional
RT   regulatory network in embryonic stem cells.";
RL   J. Biol. Chem. 284:31327-31335(2009).
CC   -!- FUNCTION: Transcription factor that forms a trimeric complex with
CC       OCT4 on DNA and controls the expression of a number of genes
CC       involved in embryonic development such as YES1, FGF4, UTF1 and
CC       ZFP206. Critical for early embryogenesis and for embryonic stem
CC       cell pluripotency.
CC   -!- SUBUNIT: Interacts with ZSCAN10.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed in the brain and retina. A very low
CC       level expression is seen in the stomach and lung. Expressed in
CC       developing urogenital ridge.
CC   -!- PTM: Sumoylation inhibits binding on DNA and negatively regulates
CC       the FGF4 transactivation.
CC   -!- BIOTECHNOLOGY: POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 are the four
CC       Yamanaka factors. When combined, these factors are sufficient to
CC       reprogram differentiated cells to an embryonic-like state
CC       designated iPS (induced pluripotent stem) cells. iPS cells exhibit
CC       the morphology and growth properties of ES cells and express ES
CC       cell marker genes.
CC   -!- SIMILARITY: Contains 1 HMG box DNA-binding domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U31967; AAC31791.1; -; mRNA.
DR   EMBL; X94127; CAA63847.1; -; Genomic_DNA.
DR   IPI; IPI00319017; -.
DR   PIR; S10949; S10949.
DR   RefSeq; NP_035573.3; NM_011443.3.
DR   UniGene; Mm.65396; -.
DR   PDB; 1GT0; X-ray; 2.60 A; D=41-120.
DR   PDBsum; 1GT0; -.
DR   ProteinModelPortal; P48432; -.
DR   SMR; P48432; 41-119.
DR   IntAct; P48432; 7.
DR   STRING; P48432; -.
DR   PhosphoSite; P48432; -.
DR   PRIDE; P48432; -.
DR   Ensembl; ENSMUST00000099151; ENSMUSP00000096755; ENSMUSG00000074637.
DR   GeneID; 20674; -.
DR   KEGG; mmu:20674; -.
DR   CTD; 20674; -.
DR   MGI; MGI:98364; Sox2.
DR   eggNOG; roNOG07798; -.
DR   HOGENOM; HBG446398; -.
DR   HOVERGEN; HBG105663; -.
DR   InParanoid; P48432; -.
DR   OrthoDB; EOG4MPHQV; -.
DR   ArrayExpress; P48432; -.
DR   Bgee; P48432; -.
DR   CleanEx; MM_SOX2; -.
DR   Genevestigator; P48432; -.
DR   GermOnline; ENSMUSG00000074637; Mus musculus.
DR   GO; GO:0005667; C:transcription factor complex; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0010843; F:promoter binding; IDA:UniProtKB.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0021984; P:adenohypophysis development; IMP:MGI.
DR   GO; GO:0001708; P:cell fate specification; IMP:MGI.
DR   GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR   GO; GO:0050973; P:detection of mechanical stimulus involved in equilibrioception; IMP:MGI.
DR   GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IMP:MGI.
DR   GO; GO:0048852; P:diencephalon morphogenesis; IMP:MGI.
DR   GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IDA:MGI.
DR   GO; GO:0021879; P:forebrain neuron differentiation; IMP:MGI.
DR   GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR   GO; GO:0060235; P:lens induction in camera-type eye; IGI:MGI.
DR   GO; GO:0048286; P:lung alveolus development; IDA:MGI.
DR   GO; GO:0030539; P:male genitalia development; IMP:MGI.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; IDA:MGI.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; IDA:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IGI:MGI.
DR   GO; GO:0048663; P:neuron fate commitment; IMP:MGI.
DR   GO; GO:0030910; P:olfactory placode formation; IGI:MGI.
DR   GO; GO:0046148; P:pigment biosynthetic process; IMP:MGI.
DR   GO; GO:0030858; P:positive regulation of epithelial cell differentiation; IDA:MGI.
DR   GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:MGI.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:MGI.
DR   GO; GO:0045747; P:positive regulation of Notch signaling pathway; IDA:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0032526; P:response to retinoic acid; IDA:MGI.
DR   GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:MGI.
DR   GO; GO:0043586; P:tongue development; IMP:MGI.
DR   InterPro; IPR000910; HMG_HMG1/HMG2.
DR   InterPro; IPR009071; HMG_superfamily.
DR   InterPro; IPR022097; TF_SOX.
DR   Gene3D; G3DSA:1.10.30.10; HMG-box; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   Pfam; PF12336; SOXp; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Developmental protein; DNA-binding;
KW   Isopeptide bond; Nucleus; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN         1    319       Transcription factor SOX-2.
FT                                /FTId=PRO_0000048716.
FT   DNA_BIND     43    111       HMG box.
FT   COMPBIAS     19     25       Poly-Gly.
FT   CROSSLNK    247    247       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT   MUTAGEN     247    247       K->R: Absence of sumoylation. Increased
FT                                FGF4 activation. No effect on nuclear
FT                                localization.
FT   CONFLICT    153    155       GGL -> AGV (in Ref. 3; CAA63847).
FT   CONFLICT    203    203       V -> D (in Ref. 3; CAA63847).
FT   CONFLICT    310    311       KY -> IN (in Ref. 3; CAA63847).
FT   HELIX        49     62
FT   HELIX        70     81
FT   HELIX        86    106
SQ   SEQUENCE   319 AA;  34454 MW;  C40DE49E524C49F1 CRC64;
     MYNMMETELK PPGPQQASGG GGGGGNATAA ATGGNQKNSP DRVKRPMNAF MVWSRGQRRK
     MAQENPKMHN SEISKRLGAE WKLLSETEKR PFIDEAKRLR ALHMKEHPDY KYRPRRKTKT
     LMKKDKYTLP GGLLAPGGNS MASGVGVGAG LGGGLNQRMD SYAHMNGWSN GSYSMMQEQL
     GYPQHPGLNA HGAAQMQPMH RYVVSALQYN SMTSSQTYMN GSPTYSMSYS QQGTPGMALG
     SMGSVVKSEA SSSPPVVTSS SHSRAPCQAG DLRDMISMYL PGAEVPEPAA PSRLHMAQHY
     QSGPVPGTAK YGTLPLSHM
//
ID   PROX1_MOUSE             Reviewed;         737 AA.
AC   P48437; O88478; Q3UPV1; Q543D8;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Prospero homeobox protein 1;
DE   AltName: Full=Homeobox prospero-like protein PROX1;
DE            Short=PROX-1;
GN   Name=Prox1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=98369610; PubMed=9703987; DOI=10.1006/bbrc.1998.8989;
RA   Tomarev S.I., Zinovieva R.D., Chang B., Hawes N.L.;
RT   "Characterization of the mouse Prox1 gene.";
RL   Biochem. Biophys. Res. Commun. 248:684-689(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye, and Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 573-737, AND TISSUE SPECIFICITY.
RX   MEDLINE=94206839; PubMed=7908825; DOI=10.1016/0925-4773(93)90012-M;
RA   Oliver G., Sosa-Pineda B., Geisendorf S., Spana E.P., Doe C.Q.,
RA   Gruss P.;
RT   "Prox 1, a prospero-related homeobox gene expressed during mouse
RT   development.";
RL   Mech. Dev. 44:3-16(1993).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-650, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-179; SER-291;
RP   SER-511 AND SER-514, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
CC   -!- FUNCTION: May play a fundamental role in early development of CNS.
CC       May regulate gene expression and development of postmitotic
CC       undifferentiated young neurons.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- TISSUE SPECIFICITY: Expressed in the young neurons of the
CC       subventricular region of the CNS, developing eye lens and
CC       pancreas. It is also found in the developing liver, heart and
CC       skeletal muscle. In the eye, expressed in the lens and retina at
CC       postnatal day 10. In the retina, localized to the inner nuclear
CC       layer. In the lens, localized to epithelial and fiber cells.
CC   -!- SIMILARITY: Belongs to the Prospero homeobox family.
CC   -!- SIMILARITY: Contains 1 Prospero-type homeobox DNA-binding domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF061576; AAC32824.1; -; mRNA.
DR   EMBL; AK052889; BAC35190.1; -; mRNA.
DR   EMBL; AK143179; BAE25293.1; -; mRNA.
DR   EMBL; BC051411; AAH51411.1; -; mRNA.
DR   IPI; IPI00112219; -.
DR   PIR; JE0269; JE0269.
DR   RefSeq; NP_032963.1; NM_008937.2.
DR   UniGene; Mm.132579; -.
DR   UniGene; Mm.392678; -.
DR   ProteinModelPortal; P48437; -.
DR   SMR; P48437; 580-728.
DR   STRING; P48437; -.
DR   PhosphoSite; P48437; -.
DR   PRIDE; P48437; -.
DR   Ensembl; ENSMUST00000010319; ENSMUSP00000010319; ENSMUSG00000010175.
DR   GeneID; 19130; -.
DR   KEGG; mmu:19130; -.
DR   UCSC; uc007ebb.1; mouse.
DR   CTD; 19130; -.
DR   MGI; MGI:97772; Prox1.
DR   eggNOG; roNOG08824; -.
DR   GeneTree; ENSGT00530000063507; -.
DR   HOGENOM; HBG444696; -.
DR   HOVERGEN; HBG053693; -.
DR   InParanoid; P48437; -.
DR   OMA; FGNVQMP; -.
DR   OrthoDB; EOG418BMZ; -.
DR   NextBio; 295746; -.
DR   ArrayExpress; P48437; -.
DR   Bgee; P48437; -.
DR   CleanEx; MM_PROX1; -.
DR   Genevestigator; P48437; -.
DR   GermOnline; ENSMUSG00000010175; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0003705; F:sequence-specific enhancer binding RNA polymerase II transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0030528; F:transcription regulator activity; IEA:InterPro.
DR   GO; GO:0060414; P:aorta smooth muscle tissue morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0055009; P:atrial cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0001709; P:cell fate determination; IMP:MGI.
DR   GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IEP:BHF-UCL.
DR   GO; GO:0060214; P:endocardium formation; IMP:BHF-UCL.
DR   GO; GO:0070365; P:hepatocyte differentiation; IEP:BHF-UCL.
DR   GO; GO:0070309; P:lens fiber cell morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0046619; P:optic placode formation involved in camera-type eye formation; IEP:BHF-UCL.
DR   GO; GO:0060421; P:positive regulation of heart growth; IMP:BHF-UCL.
DR   GO; GO:0060298; P:positive regulation of sarcomere organization; IMP:BHF-UCL.
DR   GO; GO:0030240; P:skeletal muscle thin filament assembly; IMP:BHF-UCL.
DR   GO; GO:0048845; P:venous blood vessel morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0055005; P:ventricular cardiac myofibril development; IMP:BHF-UCL.
DR   GO; GO:0060412; P:ventricular septum morphogenesis; IMP:BHF-UCL.
DR   InterPro; IPR023082; Homeo_prospero_dom.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR007738; Prox1.
DR   Gene3D; G3DSA:1.10.10.500; Homeo_prospero_dom; 1.
DR   PANTHER; PTHR12198; Prox1; 1.
DR   Pfam; PF05044; Prox1; 3.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; DNA-binding; Homeobox; Nucleus; Phosphoprotein;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    737       Prospero homeobox protein 1.
FT                                /FTId=PRO_0000208881.
FT   DNA_BIND    573    635       Prospero-type homeobox.
FT   REGION      636    737       Prospero-like.
FT   COMPBIAS    215    219       Poly-Gln.
FT   MOD_RES     177    177       Phosphoserine.
FT   MOD_RES     179    179       Phosphoserine.
FT   MOD_RES     291    291       Phosphoserine.
FT   MOD_RES     511    511       Phosphoserine.
FT   MOD_RES     514    514       Phosphoserine.
FT   MOD_RES     650    650       Phosphothreonine.
FT   CONFLICT    685    685       A -> V (in Ref. 2; BAC35190).
SQ   SEQUENCE   737 AA;  83126 MW;  834DF6963FF5C9B5 CRC64;
     MPDHDSTALL SRQTKRRRVD IGVKRTVGTA SAFFAKARAT FFSAMNPQGS EQDVEYSVVQ
     HADGEKSNVL RKLLKRANSY EDAMMPFPGA TIISQLLKNN MNKNGGTEPS FQASGLSSTG
     SEVHQEDICS NSSRDSPPEC LSPFGRPTMS QFDVDRLCDE HLRAKRARVE NIIRGMSHSP
     SVALRGNENE REMAPQSVSP RESYRENKRK QKLPQQQQQS FQQLVSARKE QKREERRQLK
     QQLEDMQKQL RQLQEKFYQV YDSTDSENDE DGDLSEDSMR SEILDARAQD SVGRSDNEMC
     ELDPGQFIDR ARALIREQEM AENKPKREGS NKERDHGPNS LQPEGKHLAE TLKQELNTAM
     SQVVDTVVKV FSAKPSRQVP QVFPPLQIPQ ARFAVNGENH NFHTANQRLQ CFGDVIIPNP
     LDTFGSVQMP SSTDQTEALP LVVRKNSSEQ SASGPATGGH HQPLHQSPLS ATAGFTTPSF
     RHPFPLPLMA YPFQSPLGAP SGSFSGKDRA SPESLDLTRD TTSLRTKMSS HHLSHHPCSP
     AHPPSTAEGL SLSLIKSECG DLQDMSDISP YSGSAMQEGL SPNHLKKAKL MFFYTRYPSS
     NMLKTYFSDV KFNRCITSQL IKWFSNFREF YYIQMEKYAR QAINDGVTST EELSITRDCE
     LYRALNMHYN KANDFEVPER FLEVAQITLR EFFNAIIAGK DVDPSWKKAI YKVICKLDSE
     VPEIFKSPNC LQELLHE
//
ID   PP2BB_MOUSE             Reviewed;         525 AA.
AC   P48453; Q6NZR4;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   09-NOV-2004, sequence version 2.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform;
DE            EC=3.1.3.16;
DE   AltName: Full=CAM-PRP catalytic subunit;
DE   AltName: Full=Calmodulin-dependent calcineurin A subunit beta isoform;
GN   Name=Ppp3cb; Synonyms=Calnb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 11-525 (ISOFORM 2).
RX   MEDLINE=92068200; PubMed=1659808; DOI=10.1016/S0006-291X(05)81410-X;
RA   Giri P.R., Higuchi S., Kincaid R.L.;
RT   "Chromosomal mapping of the human genes for the calmodulin-dependent
RT   protein phosphatase (calcineurin) catalytic subunit.";
RL   Biochem. Biophys. Res. Commun. 181:252-258(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 320-416 (ISOFORMS 1 AND 2), AND TISSUE
RP   SPECIFICITY.
RX   PubMed=1328240;
RA   Gaestel M., Benndorf R., Hayess K., Priemer E., Engel K.;
RT   "Dephosphorylation of the small heat shock protein hsp25 by
RT   calcium/calmodulin-dependent (type 2B) protein phosphatase.";
RL   J. Biol. Chem. 267:21607-21611(1992).
CC   -!- FUNCTION: Calcium-dependent, calmodulin-stimulated protein
CC       phosphatase. This subunit may have a role in the calmodulin
CC       activation of calcineurin.
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- COFACTOR: Binds 1 Fe(3+) ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Composed of two components (A and B), the A component is
CC       the catalytic subunit and the B component confers calcium
CC       sensitivity.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2; Synonyms=2B2;
CC         IsoId=P48453-1; Sequence=Displayed;
CC       Name=1; Synonyms=2B1;
CC         IsoId=P48453-2; Sequence=VSP_011856;
CC   -!- TISSUE SPECIFICITY: Two isoforms in Ehrlich ascites tumor (EAT) is
CC       demonstrated by polymerase chain reaction specific primers to the
CC       catalytic and calmodulin-binding domain, respectively. Isoform 1
CC       is of medium abundance in EAT cells.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B
CC       subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC066000; AAH66000.1; -; mRNA.
DR   EMBL; M81483; AAA37411.1; -; mRNA.
DR   IPI; IPI00112312; -.
DR   IPI; IPI00475109; -.
DR   PIR; JT0976; JT0976.
DR   RefSeq; NP_032940.1; NM_008914.2.
DR   UniGene; Mm.274432; -.
DR   UniGene; Mm.474197; -.
DR   ProteinModelPortal; P48453; -.
DR   SMR; P48453; 24-379.
DR   IntAct; P48453; 4.
DR   STRING; P48453; -.
DR   PhosphoSite; P48453; -.
DR   PRIDE; P48453; -.
DR   Ensembl; ENSMUST00000022355; ENSMUSP00000022355; ENSMUSG00000021816.
DR   GeneID; 19056; -.
DR   KEGG; mmu:19056; -.
DR   UCSC; uc007sjx.1; mouse.
DR   CTD; 19056; -.
DR   MGI; MGI:107163; Ppp3cb.
DR   eggNOG; roNOG04245; -.
DR   GeneTree; ENSGT00530000063087; -.
DR   HOGENOM; HBG716770; -.
DR   HOVERGEN; HBG002819; -.
DR   InParanoid; P48453; -.
DR   OMA; TPHSFAN; -.
DR   OrthoDB; EOG4PVNZK; -.
DR   PhylomeDB; P48453; -.
DR   BRENDA; 3.1.3.16; 244.
DR   NextBio; 295546; -.
DR   ArrayExpress; P48453; -.
DR   Bgee; P48453; -.
DR   Genevestigator; P48453; -.
DR   GermOnline; ENSMUSG00000021816; Mus musculus.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0001915; P:negative regulation of T cell mediated cytotoxicity; IMP:MGI.
DR   GO; GO:0006470; P:protein dephosphorylation; IMP:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR   GO; GO:0034097; P:response to cytokine stimulus; IMP:MGI.
DR   GO; GO:0030217; P:T cell differentiation; IMP:MGI.
DR   GO; GO:0043029; P:T cell homeostasis; IMP:MGI.
DR   InterPro; IPR004843; Metallo-dependent_phosphatase.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR11668; T_phtase_apaH; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Calmodulin-binding; Hydrolase;
KW   Iron; Metal-binding; Protein phosphatase; Zinc.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    525       Serine/threonine-protein phosphatase 2B
FT                                catalytic subunit beta isoform.
FT                                /FTId=PRO_0000058826.
FT   REGION        2    310       Catalytic.
FT   REGION      256    262       Calcineurin B binding-site 1 (Potential).
FT   REGION      305    310       Calcineurin B binding-site 2 (Potential).
FT   REGION      401    423       Calmodulin-binding (Potential).
FT   REGION      474    496       Inhibitory domain.
FT   COMPBIAS     11     20       Poly-Pro.
FT   ACT_SITE    160    160       Proton donor (By similarity).
FT   METAL        99     99       Iron (By similarity).
FT   METAL       101    101       Iron (By similarity).
FT   METAL       127    127       Iron (By similarity).
FT   METAL       127    127       Zinc (By similarity).
FT   METAL       159    159       Zinc (By similarity).
FT   METAL       208    208       Zinc (By similarity).
FT   METAL       290    290       Zinc (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   VAR_SEQ     387    406       MTEGEDQFDVGSAAARKEII -> GSEEDGFDGATAAARKE
FT                                VI (in isoform 1).
FT                                /FTId=VSP_011856.
FT   CONFLICT    481    481       E -> G (in Ref. 2; AAA37411).
FT   CONFLICT    523    524       SA -> TP (in Ref. 2; AAA37411).
SQ   SEQUENCE   525 AA;  59173 MW;  5E73BA3100BE2337 CRC64;
     MAAPEPARAA PPPPPPPPPP LGADRVVKAV PFPPTHRLTS EEVFDMDGIP RVDVLKNHLV
     KEGRVDEEIA LRIINEGAAI LRREKTMIEV EAPITVCGDI HGQFFDLMKL FEVGGSPANT
     RYLFLGDYVD RGYFSIECVL YLWVLKILYP STLFLLRGNH ECRHLTEYFT FKQECKIKYS
     ERVYEACMEA FDSLPLAALL NQQFLCVHGG LSPEIHTLDD IRRLDRFKEP PAFGPMCDLL
     WSDPSEDFGN EKSQEHFSHN TVRGCSYFYN YPAVCEFLQN NNLLSIIRAH EAQDAGYRMY
     RKSQTTGFPS LITIFSAPNY LDVYNNKAAV LKYENNVMNI RQFNCSPHPY WLPNFMDVFT
     WSLPFVGEKV TEMLVNVLSI CSDDELMTEG EDQFDVGSAA ARKEIIRNKI RAIGKMARVF
     SVLREESESV LTLKGLTPTG MLPSGVLAGG RQTLQSATVE AIEAEKAIRG FSPPHRICSF
     EEAKGLDRIN ERMPPRKDAV QQDGFNSLNT AHTTENHGTG NHSAQ
//
ID   IRK6_MOUSE              Reviewed;         425 AA.
AC   P48542; O70290; P70216; P70306; P70307; P70308; P70309; P70454;
AC   Q9QYH5;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=G protein-activated inward rectifier potassium channel 2;
DE            Short=GIRK-2;
DE   AltName: Full=Inward rectifier K(+) channel Kir3.2;
DE   AltName: Full=Potassium channel, inwardly rectifying subfamily J member 6;
GN   Name=Kcnj6; Synonyms=Girk2, Kcnj7, W;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GIRK2-1).
RC   TISSUE=Brain;
RX   MEDLINE=95010760; PubMed=7926018; DOI=10.1016/0014-5793(94)01007-2;
RA   Lesage F., Duprat F., Fink M., Guillemare E., Coppola T.,
RA   Lazdunski M., Hugnot J.-P.;
RT   "Cloning provides evidence for a family of inward rectifier and G-
RT   protein coupled K+ channels in the brain.";
RL   FEBS Lett. 353:37-42(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GIRK2A).
RC   TISSUE=Brain;
RX   MEDLINE=96081927; PubMed=7499385; DOI=10.1074/jbc.270.48.28660;
RA   Lesage F., Guillemare E., Fink M., Duprat F., Heurteaux C., Fosset M.,
RA   Romey G., Barhanin J., Lazdunski M.;
RT   "Molecular properties of neuronal G-protein-activated inwardly
RT   rectifying K+ channels.";
RL   J. Biol. Chem. 270:28660-28667(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GIRK2B).
RC   TISSUE=Brain;
RX   MEDLINE=96136315; PubMed=8573147; DOI=10.1006/bbrc.1996.0050;
RA   Isomoto S., Kondo C., Takahashi N., Matsumoto S., Yamada M.,
RA   Takumi T., Horio Y., Kurachi Y.;
RT   "A novel ubiquitously distributed isoform of GIRK2 (GIRK2B) enhances
RT   GIRK1 expression of the G-protein-gated K+ current in Xenopus
RT   oocytes.";
RL   Biochem. Biophys. Res. Commun. 218:286-291(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=129/SvJ;
RX   MEDLINE=98389623; PubMed=9721208; DOI=10.1006/geno.1998.5369;
RA   Wei J., Hodes M.E., Piva R., Feng Y., Wang Y., Ghetti B., Dlouhy S.R.;
RT   "Characterization of murine Girk2 transcript isoforms: structure and
RT   differential expression.";
RL   Genomics 51:379-390(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GIRK2D).
RA   Inanobe A., Horio Y., Fujita A., Tanemoto M., Kurachi Y.;
RT   "Molecular cloning and characterization of a novel splicing variant of
RT   Kir3.2/GIRK2 predominantly expressed in mouse testis.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PROTEIN SEQUENCE OF 379-390, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   VARIANT WV SER-156.
RX   MEDLINE=96024646; PubMed=7550338; DOI=10.1038/ng1095-126;
RA   Patil N., Cox D.R., Bhat D., Faham M., Myers R.M., Peterson A.S.;
RT   "A potassium channel mutation in weaver mice implicates membrane
RT   excitability in granule cell differentiation.";
RL   Nat. Genet. 11:126-129(1995).
CC   -!- FUNCTION: This potassium channel is controlled by G proteins. It
CC       plays a role in granule cell differentiation, possibly via
CC       membrane hyperpolarization. Inward rectifier potassium channels
CC       are characterized by a greater tendency to allow potassium to flow
CC       into the cell rather than out of it. Their voltage dependence is
CC       regulated by the concentration of extracellular potassium; as
CC       external potassium is raised, the voltage range of the channel
CC       opening shifts to more positive voltages. The inward rectification
CC       is mainly due to the blockage of outward current by internal
CC       magnesium.
CC   -!- SUBUNIT: May associate with GIRK1 or GIRK4 to form a G-protein-
CC       activated heteromultimer pore-forming unit. The resulting inward
CC       current is much larger (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC         Comment=Additional isoforms seem to exist;
CC       Name=GIRK2A;
CC         IsoId=P48542-1; Sequence=Displayed;
CC       Name=GIRK2-1;
CC         IsoId=P48542-2; Sequence=VSP_002803;
CC       Name=GIRK2B;
CC         IsoId=P48542-3; Sequence=VSP_002804, VSP_002805;
CC       Name=GIRK2C;
CC         IsoId=P48542-4; Sequence=VSP_002806, VSP_002807, VSP_002808;
CC       Name=GIRK2D; Synonyms=KIR3.2D;
CC         IsoId=P48542-5; Sequence=Not described;
CC   -!- TISSUE SPECIFICITY: Cerebellum, testes, cortex and substentia
CC       nigra.
CC   -!- DISEASE: Note=Defects in Kcnj6 are the cause of the weaver (wv)
CC       phenotype. Homozygous animals suffer from severe ataxia that is
CC       obvious by about the second postnatal week. The cerebellum of
CC       these animals is drastically reduced in size due to depletion of
CC       the major cell type of cerebellum, the granule cell neuron.
CC       Heterozygous animals are not ataxic but have an intermediate
CC       number of surviving granule cells. Male homozygotes are sterile,
CC       because of complete failure of sperm production. Both hetero- and
CC       homozygous animals undergo sporadic tonic-clonic seizures.
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
CC       (TC 1.A.2.1) family. KCNJ6 subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U37253; AAA91457.1; -; mRNA.
DR   EMBL; U11859; AAA53245.1; -; mRNA.
DR   EMBL; U51122; AAC34141.1; -; mRNA.
DR   EMBL; U51123; AAC34142.1; -; mRNA.
DR   EMBL; U51124; AAC34143.1; -; mRNA.
DR   EMBL; U51125; AAC34144.1; -; mRNA.
DR   EMBL; U51126; AAC34145.1; -; mRNA.
DR   EMBL; AF040049; AAC34286.1; -; Genomic_DNA.
DR   EMBL; AF040047; AAC34286.1; JOINED; Genomic_DNA.
DR   EMBL; AF040050; AAC34287.1; -; Genomic_DNA.
DR   EMBL; AF040049; AAC34287.1; JOINED; Genomic_DNA.
DR   EMBL; AF040051; AAC34285.1; -; Genomic_DNA.
DR   EMBL; AF040047; AAC34285.1; JOINED; Genomic_DNA.
DR   EMBL; AF040049; AAC34285.1; JOINED; Genomic_DNA.
DR   EMBL; AF040052; AAC34284.1; -; Genomic_DNA.
DR   EMBL; AF040047; AAC34284.1; JOINED; Genomic_DNA.
DR   EMBL; AF040049; AAC34284.1; JOINED; Genomic_DNA.
DR   EMBL; AF040051; AAC34284.1; JOINED; Genomic_DNA.
DR   EMBL; D86040; BAA12972.1; -; mRNA.
DR   EMBL; AB029502; BAA88430.1; -; mRNA.
DR   IPI; IPI00227085; -.
DR   IPI; IPI00227086; -.
DR   IPI; IPI00227087; -.
DR   IPI; IPI00313365; -.
DR   PIR; JC4586; JC4586.
DR   PIR; S48738; S48738.
DR   RefSeq; NP_001020756.1; NM_001025585.2.
DR   RefSeq; NP_001020761.1; NM_001025590.1.
DR   RefSeq; NP_034736.2; NM_010606.2.
DR   UniGene; Mm.328720; -.
DR   PDB; 2E4F; X-ray; 2.30 A; A=53-381.
DR   PDBsum; 2E4F; -.
DR   ProteinModelPortal; P48542; -.
DR   SMR; P48542; 53-380.
DR   STRING; P48542; -.
DR   PhosphoSite; P48542; -.
DR   PRIDE; P48542; -.
DR   Ensembl; ENSMUST00000056268; ENSMUSP00000052888; ENSMUSG00000043301.
DR   Ensembl; ENSMUST00000095873; ENSMUSP00000093558; ENSMUSG00000043301.
DR   Ensembl; ENSMUST00000099508; ENSMUSP00000097108; ENSMUSG00000043301.
DR   GeneID; 16522; -.
DR   KEGG; mmu:16522; -.
DR   CTD; 16522; -.
DR   MGI; MGI:104781; Kcnj6.
DR   eggNOG; roNOG05377; -.
DR   HOVERGEN; HBG006178; -.
DR   OrthoDB; EOG4VT5X9; -.
DR   NextBio; 289901; -.
DR   ArrayExpress; P48542; -.
DR   Bgee; P48542; -.
DR   Genevestigator; P48542; -.
DR   GermOnline; ENSMUSG00000043301; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015467; F:G-protein activated inward rectifier potassium channel activity; IDA:MGI.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR016449; K_chnl_inward-rec_Kir.
DR   InterPro; IPR001838; K_chnl_inward-rec_Kir-like.
DR   InterPro; IPR003275; K_chnl_inward-rec_Kir3.2.
DR   InterPro; IPR013521; K_chnl_inward-rec_Kir_Cr2.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   Gene3D; G3DSA:2.60.40.1400; IR_K+channel_cytopl; 1.
DR   PANTHER; PTHR11767; K+channel_IR; 1.
DR   PANTHER; PTHR11767:SF19; KIR32_channel; 1.
DR   Pfam; PF01007; IRK; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01328; KIR32CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; Ig_E-set; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing;
KW   Disease mutation; Ion transport; Ionic channel; Membrane; Potassium;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN         1    425       G protein-activated inward rectifier
FT                                potassium channel 2.
FT                                /FTId=PRO_0000154944.
FT   TOPO_DOM      1     91       Cytoplasmic (By similarity).
FT   TRANSMEM     92    116       Helical; Name=M1; (By similarity).
FT   TOPO_DOM    117    140       Extracellular (By similarity).
FT   INTRAMEM    141    152       Helical; Pore-forming; Name=H5; (By
FT                                similarity).
FT   INTRAMEM    153    159       Pore-forming; (By similarity).
FT   TOPO_DOM    160    168       Extracellular (By similarity).
FT   TRANSMEM    169    190       Helical; Name=M2; (By similarity).
FT   TOPO_DOM    191    425       Cytoplasmic (By similarity).
FT   MOTIF       154    159       Selectivity filter (By similarity).
FT   SITE        184    184       Role in the control of polyamine-mediated
FT                                channel gating and in the blocking by
FT                                intracellular magnesium (By similarity).
FT   VAR_SEQ       1     18       Missing (in isoform GIRK2C).
FT                                /FTId=VSP_002806.
FT   VAR_SEQ     319    327       MTCQARSSY -> KMGFALGFL (in isoform
FT                                GIRK2B).
FT                                /FTId=VSP_002804.
FT   VAR_SEQ     319    320       MT -> QF (in isoform GIRK2C).
FT                                /FTId=VSP_002807.
FT   VAR_SEQ     321    425       Missing (in isoform GIRK2C).
FT                                /FTId=VSP_002808.
FT   VAR_SEQ     328    425       Missing (in isoform GIRK2B).
FT                                /FTId=VSP_002805.
FT   VAR_SEQ     415    425       Missing (in isoform GIRK2-1).
FT                                /FTId=VSP_002803.
FT   VARIANT     156    156       G -> S (in wv).
FT   VARIANT     313    313       I -> M.
FT   VARIANT     344    344       M -> L.
FT   CONFLICT     67     67       V -> C (in Ref. 3 and 4).
FT   CONFLICT    260    260       S -> T (in Ref. 3; BAA12972, 4; AAC34145
FT                                and 5; BAA88430).
FT   CONFLICT    381    381       V -> L (in Ref. 5; BAA88430).
FT   STRAND      205    207
FT   STRAND      211    215
FT   STRAND      220    226
FT   STRAND      238    248
FT   STRAND      254    262
FT   STRAND      279    284
FT   TURN        290    293
FT   TURN        296    301
FT   STRAND      305    311
FT   STRAND      323    328
FT   HELIX       329    331
FT   STRAND      349    351
FT   HELIX       353    355
FT   HELIX       369    378
SQ   SEQUENCE   425 AA;  48652 MW;  2E5153DCB1B60331 CRC64;
     MTMAKLTESM TNVLEGDSMD QDVESPVAIH QPKLPKQARD DLPRHISRDR TKRKIQRYVR
     KDGKCNVHHG NVRETYRYLT DIFTTLVDLK WRFNLLIFVM VYTVTWLFFG MIWWLIAYIR
     GDMDHIEDPS WTPCVTNLNG FVSAFLFSIE TETTIGYGYR VITDKCPEGI ILLLIQSVLG
     SIVNAFMVGC MFVKISQPKK RAETLVFSTH AVISMRDGKL CLMFRVGDLR NSHIVEASIR
     AKLIKSKQTS EGEFIPLNQS DINVGYYTGD DRLFLVSPLI ISHEINQQSP FWEISKAQLP
     KEELEIVVIL EGIVEATGMT CQARSSYITS EILWGYRFTP VLTMEDGFYE VDYNSFHETY
     ETSTPSLSAK ELAELANRAE VPLSWSVSSK LNQHAELETE EEEKNPEELT ERNGDVANLE
     NESKV
//
ID   LMNA_MOUSE              Reviewed;         665 AA.
AC   P48678; P11516; P97859; Q3TIH0; Q3TTS8; Q3UCA0; Q3UCJ8; Q91WF2;
AC   Q9DC21;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 2.
DT   08-MAR-2011, entry version 107.
DE   RecName: Full=Prelamin-A/C;
DE   Contains:
DE     RecName: Full=Lamin-A/C;
DE   Flags: Precursor;
GN   Name=Lmna; Synonyms=Lmn1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95300954; PubMed=7781761; DOI=10.1016/0014-5793(95)00453-G;
RA   Nakajima N., Abe K.;
RT   "Genomic structure of the mouse A-type lamin gene locus encoding
RT   somatic and germ cell-specific lamins.";
RL   FEBS Lett. 365:108-114(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
RX   MEDLINE=89247440; PubMed=2719959; DOI=10.1016/0167-4781(89)90179-6;
RA   Riedel W., Werner D.;
RT   "Nucleotide sequence of the full-length mouse lamin C cDNA and its
RT   deduced amino-acid sequence.";
RL   Biochim. Biophys. Acta 1008:119-122(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C2).
RC   STRAIN=ddY; TISSUE=Testis;
RX   MEDLINE=94244715; PubMed=8187835; DOI=10.1006/excr.1994.1164;
RA   Furukawa K., Inagaki H., Hotta Y.;
RT   "Identification and cloning of an mRNA coding for a germ cell-specific
RT   A-type lamin in mice.";
RL   Exp. Cell Res. 212:426-430(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C).
RC   STRAIN=BALB/c, and C57BL/6J;
RC   TISSUE=Amnion, Bone marrow, Head, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 235-665 (ISOFORM A).
RX   MEDLINE=93144345; PubMed=7916626; DOI=10.1016/0167-4781(93)90072-L;
RA   Nakajima N., Sado T.;
RT   "Nucleotide sequence of a mouse lamin A cDNA and its deduced amino
RT   acid sequence.";
RL   Biochim. Biophys. Acta 1171:311-314(1993).
RN   [7]
RP   PROTEIN SEQUENCE OF 521-574, AND C-TERMINAL PROCESSING OF ISOFORM A.
RX   MEDLINE=90060368; PubMed=2583287; DOI=10.1016/0014-5793(89)81584-4;
RA   Weber K., Plessmann U., Traub P.;
RT   "Maturation of nuclear lamin A involves a specific carboxy-terminal
RT   trimming, which removes the polyisoprenylation site from the
RT   precursor; implications for the structure of the nuclear lamina.";
RL   FEBS Lett. 257:411-414(1989).
RN   [8]
RP   PARTIAL PROTEIN SEQUENCE, AND PHOSPHORYLATION AT SER-392; SER-407 AND
RP   SER-409.
RX   MEDLINE=92070490; PubMed=1959608; DOI=10.1016/0014-5793(91)80868-4;
RA   Eggert M., Radomski N., Tripier D., Traub P., Jost E.;
RT   "Identification of phosphorylation sites on murine nuclear lamin C by
RT   RP-HPLC and microsequencing.";
RL   FEBS Lett. 292:205-209(1991).
RN   [9]
RP   INTERACTION WITH SREBF1 AND SREBF2.
RX   MEDLINE=21927043; PubMed=11929849; DOI=10.1093/hmg/11.7.769;
RA   Lloyd D.J., Trembath R.C., Shackleton S.;
RT   "A novel interaction between lamin A and SREBP1: implications for
RT   partial lipodystrophy and other laminopathies.";
RL   Hum. Mol. Genet. 11:769-777(2002).
RN   [10]
RP   INTERACTION WITH SUN1.
RX   PubMed=16380439; DOI=10.1083/jcb.200509124;
RA   Crisp M., Liu Q., Roux K., Rattner J.B., Shanahan C., Burke B.,
RA   Stahl P.D., Hodzic D.;
RT   "Coupling of the nucleus and cytoplasm: role of the LINC complex.";
RL   J. Cell Biol. 172:41-53(2006).
RN   [11]
RP   INTERACTION WITH SUN1.
RX   PubMed=16648470; DOI=10.1128/MCB.26.10.3738-3751.2006;
RA   Haque F., Lloyd D.J., Smallwood D.T., Dent C.L., Shanahan C.M.,
RA   Fry A.M., Trembath R.C., Shackleton S.;
RT   "SUN1 interacts with nuclear lamin A and cytoplasmic nesprins to
RT   provide a physical connection between the nuclear lamina and the
RT   cytoskeleton.";
RL   Mol. Cell. Biol. 26:3738-3751(2006).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390 AND SER-392, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; THR-19; SER-22;
RP   SER-633 AND SER-637, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [14]
RP   SUBCELLULAR LOCATION, SUMOYLATION AT LYS-201, AND MUTAGENESIS OF
RP   LYS-201 AND GLU-203.
RX   PubMed=18606848; DOI=10.1083/jcb.200712124;
RA   Zhang Y.Q., Sarge K.D.;
RT   "Sumoylation regulates lamin A function and is lost in lamin A mutants
RT   associated with familial cardiomyopathies.";
RL   J. Cell Biol. 182:35-39(2008).
RN   [15]
RP   INTERACTION WITH TMEM43.
RX   PubMed=18230648; DOI=10.1242/jcs.019281;
RA   Bengtsson L., Otto H.;
RT   "LUMA interacts with emerin and influences its distribution at the
RT   inner nuclear membrane.";
RL   J. Cell Sci. 121:536-548(2008).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301; SER-390; SER-392;
RP   SER-398; SER-406; SER-407; SER-409; SER-414; SER-573; SER-575; SER-629
RP   AND SER-633, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [17]
RP   INTERACTION WITH SUN1 AND SUN2.
RX   PubMed=19843581; DOI=10.1242/jcs.057075;
RA   Ostlund C., Folker E.S., Choi J.C., Gomes E.R., Gundersen G.G.,
RA   Worman H.J.;
RT   "Dynamics and molecular interactions of linker of nucleoskeleton and
RT   cytoskeleton (LINC) complex proteins.";
RL   J. Cell Sci. 122:4099-4108(2009).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-390 AND SER-392,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [19]
RP   INTERACTION WITH SUN2.
RX   PubMed=19933576; DOI=10.1074/jbc.M109.071910;
RA   Haque F., Mazzeo D., Patel J.T., Smallwood D.T., Ellis J.A.,
RA   Shanahan C.M., Shackleton S.;
RT   "Mammalian SUN protein interaction networks at the inner nuclear
RT   membrane and their role in laminopathy disease processes.";
RL   J. Biol. Chem. 285:3487-3498(2010).
RN   [20]
RP   STRUCTURE BY NMR OF 406-546.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of immunoglobulin-like domain of mouse nuclear
RT   lamin.";
RL   Submitted (JUN-2004) to the PDB data bank.
CC   -!- FUNCTION: Lamins are components of the nuclear lamina, a fibrous
CC       layer on the nucleoplasmic side of the inner nuclear membrane,
CC       which is thought to provide a framework for the nuclear envelope
CC       and may also interact with chromatin. Lamin A and C are present in
CC       equal amounts in the lamina of mammals. Play an important role in
CC       nuclear assembly, chromatin organization, nuclear membrane and
CC       telomere dynamics (By similarity).
CC   -!- FUNCTION: Prelamin-A/C can accelerate smooth muscle cell
CC       senescence. It acts to disrupt mitosis and induce DNA damage in
CC       vascular smooth muscle cells (VSMCs), leading to mitotic failure,
CC       genomic instability, and premature senescence (By similarity).
CC   -!- SUBUNIT: Homodimer of lamin A and lamin C. Interacts with lamin-
CC       associated polypeptides IA, IB and TMPO-alpha, RB1 and with
CC       emerin. Proteolytically processed isoform A interacts with NARF
CC       (By similarity). Interacts with SREBF1, SREBF2, SUN1, SUN2 and
CC       TMEM43. Prelamin-A/C interacts with EMD (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Nucleus envelope
CC       (By similarity). Note=Farnesylation of prelamin-A/C facilitates
CC       nuclear envelope targeting and subsequent cleaveage by
CC       ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin-
CC       A/C, which can then be inserted into the nuclear lamina. EMD is
CC       required for proper localization of non-farnesylated prelamin-A/C
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Isoform A and isoform C are present in equal amounts in
CC         the lamina of mammals;
CC       Name=A;
CC         IsoId=P48678-1; Sequence=Displayed;
CC       Name=C;
CC         IsoId=P48678-2, P11516-1;
CC         Sequence=VSP_017064, VSP_017065;
CC       Name=C2;
CC         IsoId=P48678-3, P11516-2;
CC         Sequence=VSP_002471, VSP_002472, VSP_017064, VSP_017065;
CC   -!- TISSUE SPECIFICITY: Isoform C2 is specifically expressed in germ
CC       cells. This specific expression and unique structure suggests a
CC       role for this isoform in determining the organization of nuclear
CC       and chromosomal structures during spermatogenesis.
CC   -!- PTM: Proteolytic cleavage of the C-terminal of 18 residues of
CC       prelamin-A/C results in the production of lamin-A/C. The prelamin-
CC       A/C maturation pathway includes farnesylation of CAAX motif,
CC       ZMPSTE24/FACE1 mediated cleavage of the last three amino acids,
CC       methylation of the C-terminal cysteine and endoproteolytic removal
CC       of the last 15 C-terminal amino acids. Proteolytic cleavage
CC       requires prior farnesylation and methylation, and absence of these
CC       blocks cleavage (By similarity).
CC   -!- PTM: Sumoylation is necessary for the localization to the nuclear
CC       envelope (By similarity).
CC   -!- PTM: Farnesylation of prelamin-A/C facilitates nuclear envelope
CC       targeting (By similarity).
CC   -!- PTM: Increased phosphorylation of the lamins occurs before
CC       envelope disintegration and probably plays a role in regulating
CC       lamin associations.
CC   -!- PTM: Isoform C is phosphorylated on Ser-392, Ser-407 and Ser-409
CC       at interphase.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- MISCELLANEOUS: The structural integrity of the lamina is strictly
CC       controlled by the cell cycle, as seen by the disintegration and
CC       formation of the nuclear envelope in prophase and telophase,
CC       respectively.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
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DR   EMBL; D49733; BAA08569.1; -; Genomic_DNA.
DR   EMBL; D49733; BAA08570.1; -; Genomic_DNA.
DR   EMBL; D49733; BAA08571.1; -; Genomic_DNA.
DR   EMBL; X14170; CAA32372.1; -; mRNA.
DR   EMBL; D14850; BAA03578.1; -; mRNA.
DR   EMBL; AK004619; BAB23415.1; -; mRNA.
DR   EMBL; AK147150; BAE27717.1; -; mRNA.
DR   EMBL; AK149998; BAE29226.1; -; mRNA.
DR   EMBL; AK150501; BAE29614.1; -; mRNA.
DR   EMBL; AK150624; BAE29714.1; -; mRNA.
DR   EMBL; AK152539; BAE31294.1; -; mRNA.
DR   EMBL; AK161221; BAE36246.1; -; mRNA.
DR   EMBL; AK167858; BAE39876.1; -; mRNA.
DR   EMBL; BC015302; AAH15302.1; -; mRNA.
DR   EMBL; BC094020; AAH94020.1; -; mRNA.
DR   EMBL; D13181; BAA02476.1; -; mRNA.
DR   IPI; IPI00230435; -.
DR   IPI; IPI00400300; -.
DR   IPI; IPI00620256; -.
DR   PIR; I53414; I53414.
DR   PIR; S04333; S04333.
DR   PIR; S18324; S18324.
DR   PIR; S28182; S28182.
DR   RefSeq; NP_001002011.2; NM_001002011.2.
DR   RefSeq; NP_001104572.1; NM_001111102.1.
DR   RefSeq; NP_062263.1; NM_019390.2.
DR   UniGene; Mm.243014; -.
DR   UniGene; Mm.471227; -.
DR   PDB; 1UFG; NMR; -; A=408-545.
DR   PDBsum; 1UFG; -.
DR   ProteinModelPortal; P48678; -.
DR   SMR; P48678; 30-65, 313-386, 415-546.
DR   MINT; MINT-1868521; -.
DR   STRING; P48678; -.
DR   PhosphoSite; P48678; -.
DR   REPRODUCTION-2DPAGE; IPI00400300; -.
DR   REPRODUCTION-2DPAGE; IPI00620256; -.
DR   PRIDE; P48678; -.
DR   Ensembl; ENSMUST00000029699; ENSMUSP00000029699; ENSMUSG00000028063.
DR   GeneID; 16905; -.
DR   KEGG; mmu:16905; -.
DR   UCSC; uc008pvj.1; mouse.
DR   UCSC; uc008pvk.1; mouse.
DR   UCSC; uc008pvl.1; mouse.
DR   CTD; 16905; -.
DR   MGI; MGI:96794; Lmna.
DR   eggNOG; roNOG12141; -.
DR   HOVERGEN; HBG013015; -.
DR   InParanoid; P48678; -.
DR   OMA; HCSGSGD; -.
DR   OrthoDB; EOG4S4PG2; -.
DR   NextBio; 290934; -.
DR   ArrayExpress; P48678; -.
DR   Bgee; P48678; -.
DR   CleanEx; MM_LMNA; -.
DR   Genevestigator; P48678; -.
DR   GermOnline; ENSMUSG00000028063; Mus musculus.
DR   GO; GO:0005638; C:lamin filament; IDA:MGI.
DR   GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006998; P:nuclear envelope organization; IGI:MGI.
DR   GO; GO:0090343; P:positive regulation of cell aging; ISS:UniProtKB.
DR   GO; GO:0035105; P:sterol regulatory element binding protein import into nucleus; IMP:MGI.
DR   GO; GO:0055015; P:ventricular cardiac muscle cell development; IMP:MGI.
DR   InterPro; IPR016044; F.
DR   InterPro; IPR001664; IF.
DR   InterPro; IPR001322; IF_tail_C.
DR   InterPro; IPR018039; Intermediate_filament_CS.
DR   PANTHER; PTHR23239; IF; 1.
DR   Pfam; PF00038; Filament; 1.
DR   Pfam; PF00932; IF_tail; 1.
DR   PROSITE; PS00226; IF; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Coiled coil;
KW   Direct protein sequencing; Intermediate filament; Isopeptide bond;
KW   Lipoprotein; Methylation; Nucleus; Phosphoprotein; Prenylation;
KW   Ubl conjugation.
FT   CHAIN         1    662       Prelamin-A/C.
FT                                /FTId=PRO_0000398837.
FT   CHAIN         1    647       Lamin-A/C.
FT                                /FTId=PRO_0000063811.
FT   PROPEP      648    662       Removed in Lamin-A/C form.
FT                                /FTId=PRO_0000398838.
FT   PROPEP      663    665       Removed in Prelamin-A/C form and in
FT                                Lamin-A/C form.
FT                                /FTId=PRO_0000403443.
FT   REGION        1     33       Head.
FT   REGION       34    383       Rod.
FT   REGION       34     70       Coil 1A.
FT   REGION       71     80       Linker 1.
FT   REGION       81    218       Coil 1B.
FT   REGION      219    242       Linker 2.
FT   REGION      243    383       Coil 2.
FT   REGION      384    665       Tail.
FT   MOTIF       417    422       Nuclear localization signal (Potential).
FT   SITE        266    266       Heptad change of phase.
FT   SITE        325    325       Stutter (By similarity).
FT   SITE        330    330       Heptad change of phase.
FT   SITE        647    648       Cleavage; by endoprotease (By
FT                                similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      10     10       Phosphothreonine (By similarity).
FT   MOD_RES      12     12       Phosphoserine.
FT   MOD_RES      18     18       Phosphoserine (By similarity).
FT   MOD_RES      19     19       Phosphothreonine.
FT   MOD_RES      22     22       Phosphoserine.
FT   MOD_RES      24     24       Phosphothreonine (By similarity).
FT   MOD_RES      97     97       N6-acetyllysine (By similarity).
FT   MOD_RES     108    108       N6-acetyllysine (By similarity).
FT   MOD_RES     114    114       N6-acetyllysine (By similarity).
FT   MOD_RES     270    270       N6-acetyllysine (By similarity).
FT   MOD_RES     277    277       Phosphoserine (By similarity).
FT   MOD_RES     301    301       Phosphoserine.
FT   MOD_RES     311    311       N6-acetyllysine (By similarity).
FT   MOD_RES     390    390       Phosphoserine.
FT   MOD_RES     392    392       Phosphoserine; by CDK1.
FT   MOD_RES     394    394       Phosphothreonine (By similarity).
FT   MOD_RES     395    395       Phosphoserine (By similarity).
FT   MOD_RES     398    398       Phosphoserine.
FT   MOD_RES     403    403       Phosphoserine (By similarity).
FT   MOD_RES     404    404       Phosphoserine (By similarity).
FT   MOD_RES     406    406       Phosphoserine.
FT   MOD_RES     407    407       Phosphoserine.
FT   MOD_RES     409    409       Phosphoserine.
FT   MOD_RES     414    414       Phosphoserine.
FT   MOD_RES     416    416       Phosphothreonine (By similarity).
FT   MOD_RES     417    417       N6-acetyllysine (By similarity).
FT   MOD_RES     423    423       Phosphoserine (By similarity).
FT   MOD_RES     450    450       N6-acetyllysine (By similarity).
FT   MOD_RES     458    458       Phosphoserine (By similarity).
FT   MOD_RES     496    496       Phosphothreonine (By similarity).
FT   MOD_RES     505    505       Phosphothreonine (By similarity).
FT   MOD_RES     507    507       Phosphoserine (By similarity).
FT   MOD_RES     510    510       Phosphothreonine (By similarity).
FT   MOD_RES     573    573       Phosphoserine.
FT   MOD_RES     575    575       Phosphoserine.
FT   MOD_RES     629    629       Phosphoserine.
FT   MOD_RES     633    633       Phosphoserine.
FT   MOD_RES     637    637       Phosphoserine.
FT   MOD_RES     653    653       Phosphoserine (By similarity).
FT   MOD_RES     662    662       Cysteine methyl ester (By similarity).
FT   LIPID       662    662       S-farnesyl cysteine (By similarity).
FT   CROSSLNK    201    201       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   VAR_SEQ       1    112       Missing (in isoform C2).
FT                                /FTId=VSP_002471.
FT   VAR_SEQ     113    118       FKELKA -> MGNAEG (in isoform C2).
FT                                /FTId=VSP_002472.
FT   VAR_SEQ     569    574       GSHCSG -> VSGSRR (in isoform C and
FT                                isoform C2).
FT                                /FTId=VSP_017064.
FT   VAR_SEQ     575    665       Missing (in isoform C and isoform C2).
FT                                /FTId=VSP_017065.
FT   MUTAGEN     201    201       K->L: Decreased sumoylation; aberrant
FT                                localization with decreased nuclear rim
FT                                staining and formation of intranuclear
FT                                foci; associated with increased cell
FT                                death.
FT   MUTAGEN     203    203       E->G,K: Decreased sumoylation; aberrant
FT                                localization with decreased nuclear rim
FT                                staining and formation of intranuclear
FT                                foci; associated with increased cell
FT                                death.
FT   CONFLICT    118    119       AR -> VC (in Ref. 2; CAA32372).
FT   CONFLICT    118    118       A -> D (in Ref. 4; BAE39876).
FT   CONFLICT    340    340       E -> G (in Ref. 4; BAE29614).
FT   CONFLICT    401    401       R -> P (in Ref. 2; CAA32372).
FT   CONFLICT    439    440       RV -> WL (in Ref. 2; CAA32372).
FT   CONFLICT    453    453       R -> L (in Ref. 4; BAE36246).
FT   CONFLICT    612    612       I -> V (in Ref. 4; BAB23415).
FT   CONFLICT    617    617       S -> Y (in Ref. 4; BAB23415).
FT   CONFLICT    623    623       V -> A (in Ref. 6; BAA02476).
FT   STRAND      417    420
FT   STRAND      433    436
FT   STRAND      438    445
FT   STRAND      449    456
FT   STRAND      458    460
FT   STRAND      468    473
FT   STRAND      479    482
FT   STRAND      494    503
FT   TURN        508    510
FT   STRAND      511    514
FT   STRAND      516    518
FT   STRAND      523    531
FT   STRAND      533    535
FT   STRAND      537    544
SQ   SEQUENCE   665 AA;  74238 MW;  5434F574803FCB15 CRC64;
     METPSQRRAT RSGAQASSTP LSPTRITRLQ EKEDLQELND RLAVYIDRVR SLETENAGLR
     LRITESEEVV SREVSGIKAA YEAELGDARK TLDSVAKERA RLQLELSKVR EEFKELKARN
     TKKEGDLLAA QARLKDLEAL LNSKEAALST ALSEKRTLEG ELHDLRGQVA KLEAALGEAK
     KQLQDEMLRR VDAENRLQTL KEELDFQKNI YSEELRETKR RHETRLVEID NGKQREFESR
     LADALQELRA QHEDQVEQYK KELEKTYSAK LDNARQSAER NSNLVGAAHE ELQQSRIRID
     SLSAQLSQLQ KQLAAKEAKL RDLEDSLARE RDTSRRLLAE KEREMAEMRA RMQQQLDEYQ
     ELLDIKLALD MEIHAYRKLL EGEEERLRLS PSPTSQRSRG RASSHSSQSQ GGGSVTKKRK
     LESSESRSSF SQHARTSGRV AVEEVDEEGK FVRLRNKSNE DQSMGNWQIR RQNGDDPLMT
     YRFPPKFTLK AGQVVTIWAS GAGATHSPPT DLVWKAQNTW GCGSSLRTAL INSTGEEVAM
     RKLVRSLTMV EDNEDDDEDG EELLHHHRGS HCSGSGDPAE YNLRSRTVLC GTCGQPADKA
     AGGAGAQVGG SISSGSSASS VTVTRSFRSV GGSGGGSFGD NLVTRSYLLG NSSPRSQSSQ
     NCSIM
//
ID   HS74L_MOUSE             Reviewed;         838 AA.
AC   P48722; P97854; Q3TQN2; Q3UNG4; Q8BQD0; Q8CC45; Q91X29;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2003, sequence version 2.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Heat shock 70 kDa protein 4L;
DE   AltName: Full=Heat shock 70-related protein APG-1;
DE   AltName: Full=Osmotic stress protein 94;
GN   Name=Hspa4l; Synonyms=Apg1, Hsp4l, Osp94;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   MEDLINE=96218151; PubMed=8647834; DOI=10.1074/jbc.271.21.12327;
RA   Kojima R., Randall J., Brenner B.M., Gullans S.R.;
RT   "Osmotic stress protein 94 (Osp94). A new member of the Hsp110/SSE
RT   gene subfamily.";
RL   J. Biol. Chem. 271:12327-12332(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
RC   STRAIN=DDY/STD; TISSUE=Testis;
RX   MEDLINE=97160564; PubMed=9006898; DOI=10.1074/jbc.272.5.2640;
RA   Kaneko Y., Nishiyama H., Nonoguchi K., Higashitsuji H., Kishishita M.,
RA   Fujita J.;
RT   "A novel hsp110-related gene, apg-1, that is abundantly expressed in
RT   the testis responds to a low temperature heat shock rather than the
RT   traditional elevated temperatures.";
RL   J. Biol. Chem. 272:2640-2645(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=ddY; TISSUE=Testis;
RA   Kaneko Y., Fujita J.;
RT   "Apg-1b, an alternative form of apg-1 transcript.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Brain, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 135-153; 484-500 AND 622-632, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-761, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
CC   -!- FUNCTION: Possesses chaperone activity in vitro where it inhibits
CC       aggregation of citrate synthase (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=May translocate to the nucleus after heat shock
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P48722-1; Sequence=Displayed;
CC       Name=2; Synonyms=Apg-1b;
CC         IsoId=P48722-2; Sequence=VSP_007500;
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis. Also expressed in
CC       renal medulla of water-restricted animals.
CC   -!- INDUCTION: By hyperosmolar salt stress and heat shock.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
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DR   EMBL; U23921; AAC52610.1; -; mRNA.
DR   EMBL; D49482; BAA08446.1; -; mRNA.
DR   EMBL; AB001926; BAA19468.1; -; mRNA.
DR   EMBL; AK033950; BAC28524.1; -; mRNA.
DR   EMBL; AK050997; BAC34491.1; -; mRNA.
DR   EMBL; AK144225; BAE25783.1; -; mRNA.
DR   EMBL; AK163459; BAE37350.1; -; mRNA.
DR   EMBL; BC012712; AAH12712.1; -; mRNA.
DR   EMBL; BC057002; AAH57002.1; -; mRNA.
DR   EMBL; BC110662; AAI10663.1; -; mRNA.
DR   IPI; IPI00317710; -.
DR   IPI; IPI00317711; -.
DR   RefSeq; NP_035150.3; NM_011020.3.
DR   UniGene; Mm.39330; -.
DR   ProteinModelPortal; P48722; -.
DR   STRING; P48722; -.
DR   PhosphoSite; P48722; -.
DR   REPRODUCTION-2DPAGE; IPI00317710; -.
DR   REPRODUCTION-2DPAGE; P48722; -.
DR   PRIDE; P48722; -.
DR   Ensembl; ENSMUST00000077083; ENSMUSP00000076336; ENSMUSG00000025757.
DR   Ensembl; ENSMUST00000108086; ENSMUSP00000103721; ENSMUSG00000025757.
DR   GeneID; 18415; -.
DR   KEGG; mmu:18415; -.
DR   UCSC; uc008pbk.1; mouse.
DR   UCSC; uc008pbl.1; mouse.
DR   CTD; 18415; -.
DR   MGI; MGI:107422; Hspa4l.
DR   eggNOG; roNOG11670; -.
DR   HOVERGEN; HBG047955; -.
DR   InParanoid; P48722; -.
DR   OMA; ISDAMSW; -.
DR   OrthoDB; EOG40K7Z4; -.
DR   PhylomeDB; P48722; -.
DR   NextBio; 294048; -.
DR   ArrayExpress; P48722; -.
DR   Bgee; P48722; -.
DR   CleanEx; MM_HSPA4L; -.
DR   Genevestigator; P48722; -.
DR   GermOnline; ENSMUSG00000025757; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0006457; P:protein folding; ISS:UniProtKB.
DR   GO; GO:0006986; P:response to unfolded protein; ISS:UniProtKB.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR001023; Hsp70.
DR   InterPro; IPR013126; Hsp_70.
DR   PANTHER; PTHR19375; Hsp70; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   PROSITE; PS00297; HSP70_1; FALSE_NEG.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Chaperone; Cytoplasm;
KW   Direct protein sequencing; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Stress response.
FT   CHAIN         1    838       Heat shock 70 kDa protein 4L.
FT                                /FTId=PRO_0000078281.
FT   MOD_RES      74     74       Phosphoserine.
FT   MOD_RES     272    272       N6-acetyllysine (By similarity).
FT   MOD_RES     571    571       Phosphothreonine (By similarity).
FT   MOD_RES     761    761       Phosphothreonine.
FT   VAR_SEQ       1     36       MSVVGIDLGFLNCYIAVARSGGIETIANEYSDRCTP -> M
FT                                GGPPRHGVLDREER (in isoform 2).
FT                                /FTId=VSP_007500.
FT   CONFLICT    175    176       TA -> HS (in Ref. 2; BAA08446 and 3;
FT                                BAA19468).
FT   CONFLICT    221    221       K -> E (in Ref. 2; BAA08446 and 3;
FT                                BAA19468).
FT   CONFLICT    279    279       A -> P (in Ref. 2; BAA08446 and 3;
FT                                BAA19468).
FT   CONFLICT    308    308       Q -> R (in Ref. 2; BAA08446 and 3;
FT                                BAA19468).
FT   CONFLICT    483    483       R -> S (in Ref. 4; BAE37350).
FT   CONFLICT    571    571       T -> A (in Ref. 4; BAE37350).
FT   CONFLICT    776    776       K -> M (in Ref. 1; AAC52610).
SQ   SEQUENCE   838 AA;  94382 MW;  B2C5847DA7EAF6B7 CRC64;
     MSVVGIDLGF LNCYIAVARS GGIETIANEY SDRCTPACIS LGSRTRAIGN AAKSQIVTNV
     RNTIHGFKKL HGRSFDDPIV QTERIRLPYE LQKMPNGSTG VKVRYLEEER PFAIEQVTGM
     LLAKLKETSE NALKKPVADC VISIPSFFTD AERRSVMAAA QVAGLNCLRL MNETTAVALA
     YGIYKQDLPS LDEKPRNVVF IDMGHSAYQV SVCAFNKGKL KVLATTFDPY LGGRNFDEAL
     VDYFCDEFKT KYKINVKENS RALLRLYQEC EKLKKLMSAN ASDLPLNIEC FMNDLDVSSK
     MNRAQFEQLC ASLLARVEPP LKSVMDQANL QREDINSIEI VGGATRIPAV KEQVTRFFLK
     DISTTLNADE AVARGCALQC AILSPAFKVR EFSITDLVPY SVTLRWKTSF EEGTGECEVF
     SKNHPAPFSK VITFHKKEPF ELEAFYTNLH EVPYPDPRIG NFTIQNVFPQ SDGDSSKVKV
     KVRINIHGIF SVASASVIEK QNLEGDHNDA AMETEAPKSE GKEDVDKMQV DQEEGGHQKC
     HAEHTPEEEI DHTGAKAKAP PSDKQDRINQ TIKKGKIKSI DLPIQSSLYR QLTQDLLNSY
     IENEGKMIMQ DKLEKERNDA KNAVEEYVYD FRDKLGTVYE KFITPEDMNK LSAMLEDTEN
     WLYEEGEDQP KQVYVDRLQE LKKYGQPIQM KYVEHEERPK ALNDLGKKIQ LVLKVIEAHR
     NKDERYDHLD PAEMERVEKY ISDSMNWLNS KMNAQNKLSL TQDPVVKVSE IVTKSKELDN
     FCNPIVYKPK PKVEAPEDKA KTGSEHNGPM DGQSGSETSP DPPKGSSQHT DSGEMEVD
//
ID   PCNT_MOUSE              Reviewed;        2898 AA.
AC   P48725; A0JBT0; A0JBT1;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Pericentrin;
GN   Name=Pcnt; Synonyms=Pcnt2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX   MEDLINE=94170365; PubMed=8124707; DOI=10.1016/0092-8674(94)90504-5;
RA   Doxsey S.J., Stein P., Evans L., Calarco P.D., Kirschner M.;
RT   "Pericentrin, a highly conserved centrosome protein involved in
RT   microtubule organization.";
RL   Cell 76:639-650(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=17084386; DOI=10.1016/j.bbrc.2006.10.101;
RA   Miyoshi K., Asanuma M., Miyazaki I., Matsuzaki S., Tohyama M.,
RA   Ogawa N.;
RT   "Characterization of pericentrin isoforms in vivo.";
RL   Biochem. Biophys. Res. Commun. 351:745-749(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1437, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239 AND SER-1437, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [5]
RP   INTERACTION WITH CDK5RAP2, AND DEVELOPMENTAL STAGE.
RX   PubMed=20471352; DOI=10.1016/j.neuron.2010.03.036;
RA   Buchman J.J., Tseng H.C., Zhou Y., Frank C.L., Xie Z., Tsai L.H.;
RT   "Cdk5rap2 interacts with pericentrin to maintain the neural progenitor
RT   pool in the developing neocortex.";
RL   Neuron 66:386-402(2010).
CC   -!- FUNCTION: Integral component of the filamentous matrix of the
CC       centrosome involved in the initial establishment of organized
CC       microtubule arrays in both mitosis and meiosis. Plays a role,
CC       together with DISC1, in the microtubule network formation. Is an
CC       integral component of the pericentriolar material (PCM).
CC   -!- SUBUNIT: Interacts with DISC1 and PCM1. Binds calmodulin (By
CC       similarity). Interacts with CDK5RAP2; the interaction is leading
CC       to centrosomal localization of PCNT and CDK5RAP2.
CC   -!- INTERACTION:
CC       Q9CZA6:Nde1; NbExp=2; IntAct=EBI-2290976, EBI-309934;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome (By
CC       similarity). Note=Centrosomal at all stages of the cell cycle.
CC       Remains associated with centrosomes following microtubule
CC       depolymerization. Colocalized with DISC1 at the centrosome (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Pericentrin B, Pericentrin-360;
CC         IsoId=P48725-1; Sequence=Displayed;
CC       Name=2; Synonyms=Pericentrin S, Pericentrin-250;
CC         IsoId=P48725-2; Sequence=VSP_038927;
CC       Name=3;
CC         IsoId=P48725-3; Sequence=VSP_038928, VSP_038929;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in heart and lung (at protein
CC       level). Expressed in kidney, thymus, liver, brain, muscle, testis,
CC       spleen, lung and heart.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryo at 17 dpc (at protein
CC       level). Expressed in embryos at 7, 11, 15 and 17 dpc. Strongly
CC       expressed in brain tissues at early stages of development.
CC   -!- DOMAIN: Composed of a coiled-coil central region flanked by non-
CC       helical N- and C-terminals.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA17886.1; Type=Erroneous termination; Positions=1923; Note=Translated as Trp;
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DR   EMBL; U05823; AAA17886.1; ALT_SEQ; mRNA.
DR   EMBL; AB207233; BAF36559.1; -; mRNA.
DR   EMBL; AB207234; BAF36560.1; -; mRNA.
DR   IPI; IPI00457623; -.
DR   IPI; IPI00956798; -.
DR   IPI; IPI00956863; -.
DR   PIR; A53188; A53188.
DR   RefSeq; NP_032813.3; NM_008787.3.
DR   UniGene; Mm.251794; -.
DR   ProteinModelPortal; P48725; -.
DR   IntAct; P48725; 2.
DR   STRING; P48725; -.
DR   PhosphoSite; P48725; -.
DR   PRIDE; P48725; -.
DR   Ensembl; ENSMUST00000001179; ENSMUSP00000001179; ENSMUSG00000001151.
DR   GeneID; 18541; -.
DR   KEGG; mmu:18541; -.
DR   CTD; 18541; -.
DR   MGI; MGI:102722; Pcnt.
DR   eggNOG; roNOG04213; -.
DR   HOVERGEN; HBG079443; -.
DR   InParanoid; P48725; -.
DR   OrthoDB; EOG4PNXG1; -.
DR   NextBio; 294320; -.
DR   ArrayExpress; P48725; -.
DR   Bgee; P48725; -.
DR   CleanEx; MM_PCNT; -.
DR   Genevestigator; P48725; -.
DR   GermOnline; ENSMUSG00000001151; Mus musculus.
DR   GO; GO:0005814; C:centriole; IDA:MGI.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptosis; IMP:MGI.
DR   GO; GO:0048854; P:brain morphogenesis; IMP:MGI.
DR   GO; GO:0021696; P:cerebellar cortex morphogenesis; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0035108; P:limb morphogenesis; IMP:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR   GO; GO:0061351; P:neural precursor cell proliferation; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0021772; P:olfactory bulb development; IMP:MGI.
DR   GO; GO:0007051; P:spindle organization; IDA:MGI.
DR   InterPro; IPR019528; PACT_domain.
DR   Pfam; PF10495; PACT_coil_coil; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calmodulin-binding; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Microtubule; Phosphoprotein.
FT   CHAIN         1   2898       Pericentrin.
FT                                /FTId=PRO_0000058258.
FT   REGION     1801   1822       Interaction with CDK5RAP2.
FT   REGION     2758   2771       Calmodulin-binding (By similarity).
FT   COILED      127    343       Potential.
FT   COILED      382    434       Potential.
FT   COILED      468    527       Potential.
FT   COILED      611    696       Potential.
FT   COILED      727    787       Potential.
FT   COILED      872    939       Potential.
FT   COILED     1069   1383       Potential.
FT   COILED     1429   1482       Potential.
FT   COILED     1529   1593       Potential.
FT   COILED     2211   2403       Potential.
FT   COILED     2429   2590       Potential.
FT   MOD_RES     239    239       Phosphoserine.
FT   MOD_RES    1437   1437       Phosphoserine.
FT   MOD_RES    1959   1959       Phosphoserine (By similarity).
FT   MOD_RES    2838   2838       Phosphoserine (By similarity).
FT   VAR_SEQ       1    916       Missing (in isoform 2).
FT                                /FTId=VSP_038927.
FT   VAR_SEQ    2044   2050       ALSESQD -> GNSRLLF (in isoform 3).
FT                                /FTId=VSP_038928.
FT   VAR_SEQ    2501   2898       Missing (in isoform 3).
FT                                /FTId=VSP_038929.
FT   CONFLICT    652    652       Missing (in Ref. 1; AAA17886).
FT   CONFLICT    662    662       Missing (in Ref. 1; AAA17886).
FT   CONFLICT    896    897       EL -> DV (in Ref. 1; AAA17886).
FT   CONFLICT    960    960       R -> G (in Ref. 1; AAA17886).
FT   CONFLICT    982    982       A -> P (in Ref. 1; AAA17886).
FT   CONFLICT   1022   1022       S -> R (in Ref. 1; AAA17886).
FT   CONFLICT   1150   1150       Q -> E (in Ref. 1; AAA17886).
FT   CONFLICT   1266   1267       EH -> DD (in Ref. 1; AAA17886).
FT   CONFLICT   1533   1533       N -> D (in Ref. 1; AAA17886).
FT   CONFLICT   1548   1548       R -> G (in Ref. 1; AAA17886).
FT   CONFLICT   1726   1726       N -> G (in Ref. 1; AAA17886).
FT   CONFLICT   1736   1736       E -> Q (in Ref. 1; AAA17886).
FT   CONFLICT   1772   1772       C -> S (in Ref. 1; AAA17886).
FT   CONFLICT   2040   2040       H -> L (in Ref. 1; AAA17886).
SQ   SEQUENCE   2898 AA;  329465 MW;  50E66D93F7E4E283 CRC64;
     MEDEQEQRRR KVEAGRAKLA NFRQRKTKGD CPNSKKKTAK RKGSAVHASV QEEGSVATPN
     SELPQGGAVF ESPSCSNTLE GTRGASAAQE QEDCELDVTD LQGQQQTQPP PPQTAHSLEL
     EALRLSLNNM HTAQLELTQA NLQKEKETAL TELREMLNGR RAQELALLQS RQQCELELLR
     EQHAREKEEM ALRSGQEAAE LKEKLRSEME KNAQTIETLK QDWESERELC LENLRQELSL
     KHQSEMEGLQ SQFQKELSEQ KVELEKIFQA KHEAEVSLKN LEAQHQAAIK KLQEDLQSEH
     CQYLQDLEQK FREKEKAKEL ELETLQASYE DLKAQSQEEI RLLWSQLESM KTNREELNGS
     WDPVLAQASH LEELEHLRSG FAQQQQQERA QHESELEHLR VYFEKKLKDA EKTYQEDLTV
     FQQRLQEARE DSLESTEISS SCVLPEETSG REGKEPPDPL DLQLGQPKVQ ESLVEDCQVK
     LSKAEEKIQQ MKEEFQKKEA EWELSREELK REAEERLASM FLELREKAES EKLSIISRFE
     HRESSMRHLQ DQQAAQILDL ERSLMEQQGH LRQLEQELTR DDLLPCSQCG QEPAMAQEEK
     NGALLREKED CALQLLMAQN RFLEERKEIM EKFAKEQDAF LRDAQEKHNH ELQLLQQGHQ
     QQLLALRMEL ETKHRSELTE QLASSESRRQ ALLETHVAEL QVKHNAEISA LEKRHLSNLD
     ELESCYVADV QTIRDEHQQA LELLRAELEE QLQKKESCHR EMLTQELENL KRQHAEELQS
     VRDSLRMEMS AQHIENGKGP AADLQGAHQQ DPAMALHNEG HLLVEDGDAV LRSVDAEGLL
     HQAGPQELGD AHTVEMQKSQ AELAKPQELQ ASQDQVAQVR DKVFLLNREL EECRAELEQL
     QQRRERENQE GTTLICMLRA DLELAQGEGK ALRDALRRLL DLFGDTLKAA VTLKSRISER
     AGLLLDHEDA ADTSDARLAA AALGDMWSDE GLLEIDRTLP EGAETSSVCE ISSHVCESFF
     ISPENTLDCE QPIRRVYQSL STAVEGLLEM ALDSSKQLEE ARQLHRCVER EFRHRNEEMA
     QAMQKQQELL ERLREESAAK DRLALELHTA KGLLEGFKVE KVDLQEALGK KEESEQQLIL
     ELEDLRKQLQ QAARELLTLK EEKSVLWNQK ETLTNEAKER EAALQEEVES LTRVQWESRK
     QSEKDRATLL SQMRVLESEL EDQLVQHRGC AQLAEEVATL KQQLAALDKH LRSQRQFMDD
     QAAEREHERE EFQQEIQRLE GQLRQAARPR PPGPRDSQCV QLDEEVELLQ EKLREKLDGF
     NELVIKKDFA DQQLLIQEEE IKRLEETNAS IQRQMVQLQE ELEKQKKSME ELKEKEILKQ
     ENMGDLLLTT VSRSGLDEAG CPMLPQGSSS RGPEAQPDVT ERALLQHENE VVHRRNSEID
     ELKSLIENLQ ENQRQLQKDK AEEIEQLHEV IEKLQSELSL MGPKVHEVSD PQAGSLHSEL
     ACLRGEGLGG QALRSELQAA QAAKEVFGQL LANQAHGHSQ ALEALQQRLQ DAEEVAARHL
     AELEHCVALR EAEVEAMASQ IQEFAATLKA KEAIIEQRDL EIDAVNKWKV SHSLELEAIL
     LALAHFRHAL EQQTCATPDE PPELRQLRVQ CARLSHQLQV LYRPFLKCRM QLDQHQPHVA
     SIGCANPCAD DELEQEGVSN RLALAPHSLA AQAKEELEDC PLGKANLMAQ VRQLQEELDH
     RVHSVASRDT NSETCKLQQP NLSENGPRNH CCNGEESKPS PPDDVLNIAK TTWDVIDIIK
     NQDLLVQVEM PDFPTQEKLT SQGGPFSSQA SGHSGSLLPE EAAEPQQDPV RALDLSSWSS
     PEVVRKDPSL EPQHSLPLTP GVGTVSLHSV DISPDWTDPL LQADVSGLLC YPGKSASGQA
     PLWAVAPSAG KHHAERTATE KDVEDFIVTS FDSQELLTSP SHELARRSDG SRKSDGPDIA
     MMLTLGSEGS ETPTTDLVAA AAAAVPFSRR FVQSPGAMKE KEIHAKQMKA LLQMVFDESH
     QILALSESQD PSSALNKGEP RDPLDGFPRD SQALSEVTTD KGEKESLETH LTWSEELLRA
     IQEVFAREQE KAELQPRPYG SNLGDYNSLV QRLEKVIQEQ GDPQKVQDHL CLSDRSSLLA
     EIQALRAQLR MTHLQNQEKL QQLCAALTST EARGSQREHQ LRRQVELLAY KVEQEKCIAN
     ELQKTLSKEQ ETASDVRKRL VVEQNAVQDL KSELHACKQE NTSLLESLDK VQQEVLRLRA
     VLDGKEKELK VVLEELESER GKGQALQAQQ EEQQLRYLQR EGQSSRALEE LKLSLEKQLA
     QNNQLCVALK HERAAKDNLQ KELQIEASRC EALLAQEKGQ LSELQKSLEA ERSRSLELSE
     ALQHERLLTE QLSRNSQEAC ARQETQVQHA LLRKLKAEKT RALELEAMLE KVQKQAAHTQ
     QQLEAQAQER CVELRREKER ELEIQRQRDE HKIEQLQRLV RELRWKEEVS GGNGPCRGSP
     GRGSLERDQF QEQQQELEKI RQQLLCAAGL LTSFTNHTVD RTIKDWTSSN EKAVSSLMRT
     LEELKSELSM PTSFQKKMTA ELQVQLMNEL LSDNDALTKA VGMATREKAE LCRTVSRLEK
     TLKHHTQKGC VLNRQSKSSL KQDGTDLQSS LRHSDPEWHS QTTSGDTNTC NIKMEKLYLH
     YLRAESFRKA LIYQKKYLLL LIGGFQDSEQ ETLSMIAHLG VFPSKADKKI TMSRPFTKFR
     TAVRVVIAVL RLRFLVKKWQ EVDRKGALVH PKSTRHGHRT SQRQRSPSGP RASLPTRDTS
     SGPTKASRHS PRSAAAGSPG KERSTSTPSS RLERSLTASQ DPEHSLTEYI HHLEMIQQRL
     GGLPPDSTQK SCHQKIKQ
//
ID   CBR1_MOUSE              Reviewed;         277 AA.
AC   P48758; Q91X28;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 3.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Carbonyl reductase [NADPH] 1;
DE            EC=1.1.1.184;
DE   AltName: Full=15-hydroxyprostaglandin dehydrogenase [NADP+];
DE            EC=1.1.1.197;
DE   AltName: Full=NADPH-dependent carbonyl reductase 1;
DE   AltName: Full=Prostaglandin 9-ketoreductase;
DE   AltName: Full=Prostaglandin-E(2) 9-reductase;
DE            EC=1.1.1.189;
GN   Name=Cbr1; Synonyms=Cbr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CBA/CJ; TISSUE=Cerebellum;
RX   MEDLINE=96299674; PubMed=8661038; DOI=10.1006/geno.1996.0255;
RA   Wei J., Dlouhy S.R., Hara A., Ghetti B., Hodes M.E.;
RT   "Cloning a cDNA for carbonyl reductase (Cbr) from mouse cerebellum:
RT   murine genes that express cbr map to chromosomes 16 and 11.";
RL   Genomics 34:147-148(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 59-71; 80-96 AND 221-232, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Klug S., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: NADPH-dependent reductase with broad substrate
CC       specificity. Catalyzes the reduction of a wide variety of carbonyl
CC       compounds including quinones, prostaglandins, menadione, plus
CC       various xenobiotics. Catalyzes the reduction of the antitumor
CC       anthracyclines doxorubicin and daunorubicin to the cardiotoxic
CC       compounds doxorubicinol and daunorubicinol. Can convert
CC       prostaglandin E2 to prostaglandin F2-alpha. Can bind glutathione,
CC       which explains its higher affinity for glutathione-conjugated
CC       substrates. Catalyzes the reduction of S-nitrosoglutathione (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: R-CHOH-R' + NADP(+) = R-CO-R' + NADPH.
CC   -!- CATALYTIC ACTIVITY: (5Z,13E)-(15S)-9-alpha,11-alpha,15-
CC       trihydroxyprosta-5,13-dienoate + NADP(+) = (5Z,13E)-(15S)-11-
CC       alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate + NADPH.
CC   -!- CATALYTIC ACTIVITY: (13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprost-
CC       13-enoate + NADP(+) = (13E)-11-alpha-hydroxy-9,15-dioxoprost-13-
CC       enoate + NADPH.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U31966; AAB19006.1; -; mRNA.
DR   EMBL; BC012714; AAH12714.1; -; mRNA.
DR   IPI; IPI00314191; -.
DR   RefSeq; NP_031646.2; NM_007620.2.
DR   UniGene; Mm.26940; -.
DR   ProteinModelPortal; P48758; -.
DR   SMR; P48758; 7-277.
DR   STRING; P48758; -.
DR   PhosphoSite; P48758; -.
DR   REPRODUCTION-2DPAGE; P48758; -.
DR   PRIDE; P48758; -.
DR   Ensembl; ENSMUST00000039659; ENSMUSP00000049394; ENSMUSG00000051483.
DR   GeneID; 12408; -.
DR   KEGG; mmu:12408; -.
DR   CTD; 12408; -.
DR   MGI; MGI:88284; Cbr1.
DR   eggNOG; roNOG06780; -.
DR   GeneTree; ENSGT00510000046499; -.
DR   HOGENOM; HBG750976; -.
DR   HOVERGEN; HBG001909; -.
DR   InParanoid; P48758; -.
DR   OMA; NTAYGVT; -.
DR   OrthoDB; EOG4BP1CB; -.
DR   PhylomeDB; P48758; -.
DR   BRENDA; 1.1.1.184; 244.
DR   NextBio; 281186; -.
DR   ArrayExpress; P48758; -.
DR   Bgee; P48758; -.
DR   CleanEx; MM_CBR1; -.
DR   Genevestigator; P48758; -.
DR   GermOnline; ENSMUSG00000051483; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047021; F:15-hydroxyprostaglandin dehydrogenase (NADP+) activity; IEA:EC.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004090; F:carbonyl reductase (NADPH) activity; ISS:UniProtKB.
DR   GO; GO:0050221; F:prostaglandin-E2 9-reductase activity; IEA:EC.
DR   GO; GO:0017144; P:drug metabolic process; ISS:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0042373; P:vitamin K metabolic process; ISS:UniProtKB.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; NADP;
KW   Oxidoreductase; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    277       Carbonyl reductase [NADPH] 1.
FT                                /FTId=PRO_0000054603.
FT   NP_BIND      10     34       NADP (By similarity).
FT   NP_BIND      63     64       NADP (By similarity).
FT   NP_BIND     194    198       NADP (By similarity).
FT   NP_BIND     231    233       NADP (By similarity).
FT   REGION       95     97       Glutathione binding (By similarity).
FT   REGION      193    194       Glutathione binding (By similarity).
FT   ACT_SITE    194    194       Proton acceptor (By similarity).
FT   BINDING      90     90       NADP; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     106    106       Glutathione (By similarity).
FT   BINDING     140    140       Substrate (By similarity).
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES     194    194       Phosphotyrosine (By similarity).
FT   CONFLICT     90     90       N -> K (in Ref. 1; AAB19006).
FT   CONFLICT    112    112       K -> E (in Ref. 1; AAB19006).
FT   CONFLICT    218    218       G -> E (in Ref. 1; AAB19006).
SQ   SEQUENCE   277 AA;  30641 MW;  6053423B6D5F82B7 CRC64;
     MSSSRPVALV TGANKGIGFA ITRDLCRKFS GDVVLAARDE ERGQTAVQKL QAEGLSPRFH
     QLDIDNPQSI RALRDFLLKE YGGLDVLVNN AGIAFKVNDD TPFHIQAEVT MKTNFFGTRD
     VCKELLPLIK PQGRVVNVSS MVSLRALKNC RLELQQKFRS ETITEEELVG LMNKFVEDTK
     KGVHAEEGWP NSAYGVTKIG VTVLSRILAR KLNEQRRGDK ILLNACCPGW VRTDMAGPKA
     TKSPEEGAET PVYLALLPPD AEGPHGQFVQ DKKVEPW
//
ID   ADT1_MOUSE              Reviewed;         298 AA.
AC   P48962; Q62164;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   08-MAR-2011, entry version 102.
DE   RecName: Full=ADP/ATP translocase 1;
DE   AltName: Full=ADP,ATP carrier protein 1;
DE   AltName: Full=ADP,ATP carrier protein, heart/skeletal muscle isoform T1;
DE   AltName: Full=Adenine nucleotide translocator 1;
DE            Short=ANT 1;
DE   AltName: Full=Solute carrier family 25 member 4;
DE   AltName: Full=mANC1;
GN   Name=Slc25a4; Synonyms=Anc1, Ant1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=97059403; PubMed=8903724; DOI=10.1007/s003359900007;
RA   Ellison J.W., Li X., Francke U., Shapiro L.J.;
RT   "Rapid evolution of human pseudoautosomal genes and their mouse
RT   homologs.";
RL   Mamm. Genome 7:25-30(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Muscle;
RA   Laplace C., Costet P.;
RL   Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=20432087; PubMed=10974536; DOI=10.1016/S0378-1119(00)00252-3;
RA   Levy S.E., Chen Y.-S., Graham B.H., Wallace D.C.;
RT   "Expression and sequence analysis of the mouse adenine nucleotide
RT   translocase 1 and 2 genes.";
RL   Gene 254:57-66(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 81-92, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   IDENTIFICATION IN A COMPLEX WITH ARL2 AND ARL2BP, INTERACTION WITH
RP   ARL2BP, AND TISSUE SPECIFICITY.
RX   PubMed=11809823; DOI=10.1091/mbc.01-05-0245;
RA   Sharer J.D., Shern J.F., Van Valkenburgh H., Wallace D.C., Kahn R.A.;
RT   "ARL2 and BART enter mitochondria and bind the adenine nucleotide
RT   transporter.";
RL   Mol. Biol. Cell 13:71-83(2002).
RN   [7]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-10, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Heart;
RX   PubMed=17451654; DOI=10.1016/j.bbrc.2007.04.015;
RA   Jeon H.B., Choi E.S., Yoon J.H., Hwang J.H., Chang J.W., Lee E.K.,
RA   Choi H.W., Park Z.-Y., Yoo Y.J.;
RT   "A proteomics approach to identify the ubiquitinated proteins in mouse
RT   heart.";
RL   Biochem. Biophys. Res. Commun. 357:731-736(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-195, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-191, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-126 AND SER-127, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RA   Lubec G., Kang S.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the exchange of ADP and ATP across the
CC       mitochondrial inner membrane.
CC   -!- SUBUNIT: Homodimer. Found in a complex with ARL2, ARL2BP and
CC       SLC25A4. Interacts with ARL2BP.
CC   -!- INTERACTION:
CC       Q9NYF8:BCLAF1 (xeno); NbExp=1; IntAct=EBI-299469, EBI-437804;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC       membrane protein. Note=The complex formed with ARL2BP, ARL2 and
CC       SLC25A4 is expressed in mitochondria.
CC   -!- MISCELLANEOUS: The transmembrane helices are not perpendicular to
CC       the plane of the membrane, but cross the membrane at an angle.
CC       Odd-numbered transmembrane helices exhibit a sharp kink, due to
CC       the presence of a conserved proline residue (By similarity).
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier family.
CC   -!- SIMILARITY: Contains 3 Solcar repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U27315; AAC52837.1; -; mRNA.
DR   EMBL; X74510; CAA52616.1; -; mRNA.
DR   EMBL; AF240002; AAF64470.1; -; Genomic_DNA.
DR   EMBL; BC003791; AAH03791.1; -; mRNA.
DR   EMBL; BC026925; AAH26925.1; -; mRNA.
DR   IPI; IPI00115564; -.
DR   PIR; S37210; S37210.
DR   RefSeq; NP_031476.3; NM_007450.4.
DR   UniGene; Mm.16228; -.
DR   ProteinModelPortal; P48962; -.
DR   SMR; P48962; 3-294.
DR   IntAct; P48962; 7.
DR   STRING; P48962; -.
DR   PhosphoSite; P48962; -.
DR   PRIDE; P48962; -.
DR   Ensembl; ENSMUST00000034049; ENSMUSP00000034049; ENSMUSG00000031633.
DR   GeneID; 11739; -.
DR   KEGG; mmu:11739; -.
DR   UCSC; uc009lpz.1; mouse.
DR   CTD; 11739; -.
DR   MGI; MGI:1353495; Slc25a4.
DR   eggNOG; roNOG15102; -.
DR   HOGENOM; HBG610399; -.
DR   HOVERGEN; HBG108348; -.
DR   InParanoid; P48962; -.
DR   OMA; AKDEGSK; -.
DR   OrthoDB; EOG49CQ86; -.
DR   PhylomeDB; P48962; -.
DR   NextBio; 279463; -.
DR   ArrayExpress; P48962; -.
DR   Bgee; P48962; -.
DR   Genevestigator; P48962; -.
DR   GermOnline; ENSMUSG00000031633; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0008637; P:apoptotic mitochondrial changes; IGI:MGI.
DR   InterPro; IPR002113; Aden_trnslctor.
DR   InterPro; IPR002067; Mit_carrier.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00927; ADPTRNSLCASE.
DR   PRINTS; PR00926; MITOCARRIER.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Isopeptide bond; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Phosphoprotein; Repeat;
KW   Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    298       ADP/ATP translocase 1.
FT                                /FTId=PRO_0000090575.
FT   TRANSMEM      5     39       Helical; Name=1; (By similarity).
FT   TRANSMEM     75    100       Helical; Name=2; (By similarity).
FT   TRANSMEM    109    143       Helical; Name=3; (By similarity).
FT   TRANSMEM    176    202       Helical; Name=4; (By similarity).
FT   TRANSMEM    207    241       Helical; Name=5; (By similarity).
FT   TRANSMEM    273    298       Helical; Name=6; (By similarity).
FT   REPEAT        6     98       Solcar 1.
FT   REPEAT      111    201       Solcar 2.
FT   REPEAT      212    297       Solcar 3.
FT   MOTIF       235    240       Substrate recognition (By similarity).
FT   BINDING      80     80       Nucleotide (By similarity).
FT   MOD_RES       2      2       N-acetylglycine (By similarity).
FT   MOD_RES      96     96       N6-acetyllysine (By similarity).
FT   MOD_RES     126    126       Phosphothreonine.
FT   MOD_RES     127    127       Phosphoserine.
FT   MOD_RES     191    191       Phosphotyrosine.
FT   MOD_RES     195    195       Phosphotyrosine.
FT   CROSSLNK     10     10       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CONFLICT    136    136       F -> L (in Ref. 1; AAC52837).
SQ   SEQUENCE   298 AA;  32904 MW;  3A849FEAB0981462 CRC64;
     MGDQALSFLK DFLAGGIAAA VSKTAVAPIE RVKLLLQVQH ASKQISAEKQ YKGIIDCVVR
     IPKEQGFLSF WRGNLANVIR YFPTQALNFA FKDKYKQIFL GGVDRHKQFW RYFAGNLASG
     GAAGATSLCF VYPLDFARTR LAADVGKGSS QREFNGLGDC LTKIFKSDGL KGLYQGFSVS
     VQGIIIYRAA YFGVYDTAKG MLPDPKNVHI IVSWMIAQSV TAVAGLVSYP FDTVRRRMMM
     QSGRKGADIM YTGTLDCWRK IAKDEGANAF FKGAWSNVLR GMGGAFVLVL YDEIKKYV
//
ID   CTRO_MOUSE              Reviewed;        2055 AA.
AC   P49025; O88528; O88937; O88938; Q3UM99; Q8CIJ1;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 3.
DT   08-MAR-2011, entry version 105.
DE   RecName: Full=Citron Rho-interacting kinase;
DE            Short=CRIK;
DE            EC=2.7.11.1;
DE   AltName: Full=Rho-interacting, serine/threonine-protein kinase 21;
GN   Name=Cit;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND FUNCTION.
RC   TISSUE=Brain;
RX   MEDLINE=96128238; PubMed=8543060; DOI=10.1016/0014-5793(95)01351-2;
RA   Madaule P., Furuyashiki T., Reid T., Ishizaki T., Watanabe G.,
RA   Morii N., Narumiya S.;
RT   "A novel partner for the GTP-bound forms of rho and rac.";
RL   FEBS Lett. 377:243-248(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, CATALYTIC
RP   ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   LYS-126.
RC   TISSUE=Keratinocyte;
RX   MEDLINE=99009084; PubMed=9792683; DOI=10.1074/jbc.273.45.29706;
RA   Di Cunto F., Calautti E., Hsiao J., Ong L., Topley G., Turco E.,
RA   Dotto G.P.;
RT   "Citron Rho-interacting kinase, a novel tissue-specific Ser/Thr kinase
RT   encompassing the Rho-Rac-binding protein Citron.";
RL   J. Biol. Chem. 273:29706-29711(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PROTEIN SEQUENCE OF 246-254, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 373-2055 (ISOFORM 4), AND FUNCTION.
RC   TISSUE=Brain;
RX   MEDLINE=98361238; PubMed=9697773; DOI=10.1038/28873;
RA   Madaule P., Eda M., Watanabe N., Fujisawa K., Matsuoka T., Bito H.,
RA   Ishizaki T., Narumiya S.;
RT   "Role of citron kinase as a target of the small GTPase Rho in
RT   cytokinesis.";
RL   Nature 394:491-494(1998).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 992-2055 (ISOFORM 5).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   MEDLINE=20537823; PubMed=11086988; DOI=10.1016/S0896-6273(00)00090-8;
RA   Di Cunto F., Imarisio S., Hirsch E., Broccoli V., Bulfone A.,
RA   Migheli A., Atzori C., Turco E., Triolo R., Dotto G.P., Silengo L.,
RA   Altruda F.;
RT   "Defective neurogenesis in citron kinase knockout mice by altered
RT   cytokinesis and massive apoptosis.";
RL   Neuron 28:115-127(2000).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1237 AND TYR-1504, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1608, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Required for KIF14 localization to the central spindle
CC       and midbody. May play a role in cytokinesis (By similarity).
CC       Probable RHO/RAC effector that binds to the GTP-bound forms of RHO
CC       and RAC1. It probably binds p21 with a tighter specificity in
CC       vivo. Dual specificity protein kinase activity catalyzing
CC       autophosphorylation and phosphorylation of exogenous substrates on
CC       both serine/threonine and tyrosine residues. Plays an important
CC       role in the regulation of cytokinesis and the development of the
CC       central nervous system.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts with TTC3 (By similarity). Homodimer
CC       (Probable). Directly interacts with KIF14 depending on the
CC       activation state (stronger interaction with the kinase-dead form).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1; Synonyms=CRIK;
CC         IsoId=P49025-1; Sequence=Displayed;
CC       Name=2; Synonyms=CRIK-SK;
CC         IsoId=P49025-2; Sequence=VSP_012438, VSP_012439;
CC       Name=3; Synonyms=Citron;
CC         IsoId=P49025-3; Sequence=VSP_012436, VSP_012437;
CC       Name=4;
CC         IsoId=P49025-4; Sequence=VSP_016093;
CC       Name=5;
CC         IsoId=P49025-5; Sequence=VSP_016094, VSP_016095;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: A major signal was observed in testis and
CC       brain, but it was also detected in thymus, spleen, kidney, heart
CC       and lung.
CC   -!- DEVELOPMENTAL STAGE: Detected at E10.5 with highest expression in
CC       the developing central nervous system. After E16.5 expression
CC       decreases and at two weeks after birth is restricted to the
CC       proliferating neuronal precursor cells in the external germinal
CC       layer of the cerebellum and subventricular migratory stream.
CC   -!- DISRUPTION PHENOTYPE: Death before reaching adulthood, probably
CC       due to lethal epilepsy. Mice display severe defects in the
CC       olfactory bulbs, the hippocampus, and the cerebellum. These
CC       defects appear to result from impaired cytokinesis followed by the
CC       induction of apoptosis in specific neuroblast populations.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 CNH domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC72822.1; Type=Frameshift; Positions=396, 408;
CC       Sequence=AAC72823.1; Type=Frameshift; Positions=396, 408;
CC       Sequence=AAH23775.1; Type=Frameshift; Positions=1011;
CC       Sequence=AAH51165.1; Type=Frameshift; Positions=1011;
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DR   EMBL; U39904; AAC52341.1; -; mRNA.
DR   EMBL; AF086823; AAC72822.1; ALT_FRAME; mRNA.
DR   EMBL; AF086824; AAC72823.1; ALT_FRAME; mRNA.
DR   EMBL; AK145037; BAE26199.1; -; mRNA.
DR   EMBL; AF070066; AAC27933.1; -; mRNA.
DR   EMBL; BC023775; AAH23775.1; ALT_FRAME; mRNA.
DR   EMBL; BC051165; AAH51165.1; ALT_FRAME; mRNA.
DR   IPI; IPI00406762; -.
DR   IPI; IPI00474730; -.
DR   IPI; IPI00655040; -.
DR   IPI; IPI00655108; -.
DR   IPI; IPI00956788; -.
DR   PIR; S68420; S68420.
DR   UniGene; Mm.426282; -.
DR   UniGene; Mm.8321; -.
DR   ProteinModelPortal; P49025; -.
DR   SMR; P49025; 44-423, 1389-1437, 1471-1587.
DR   STRING; P49025; -.
DR   PhosphoSite; P49025; -.
DR   PRIDE; P49025; -.
DR   Ensembl; ENSMUST00000051704; ENSMUSP00000062049; ENSMUSG00000029516.
DR   Ensembl; ENSMUST00000112011; ENSMUSP00000107642; ENSMUSG00000029516.
DR   Ensembl; ENSMUST00000112014; ENSMUSP00000107645; ENSMUSG00000029516.
DR   UCSC; uc008zep.1; mouse.
DR   UCSC; uc008zer.1; mouse.
DR   UCSC; uc008zes.1; mouse.
DR   MGI; MGI:105313; Cit.
DR   eggNOG; roNOG11544; -.
DR   GeneTree; ENSGT00600000084128; -.
DR   HOVERGEN; HBG071093; -.
DR   OrthoDB; EOG402WR8; -.
DR   PhylomeDB; P49025; -.
DR   BRENDA; 2.7.11.1; 244.
DR   ArrayExpress; P49025; -.
DR   Bgee; P49025; -.
DR   CleanEx; MM_CIT; -.
DR   Genevestigator; P49025; -.
DR   GermOnline; ENSMUSG00000029516; Mus musculus.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR   GO; GO:0001726; C:ruffle; IDA:MGI.
DR   GO; GO:0005773; C:vacuole; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0005083; F:small GTPase regulator activity; IEA:InterPro.
DR   GO; GO:0000910; P:cytokinesis; IMP:MGI.
DR   GO; GO:0016358; P:dendrite development; IMP:MGI.
DR   GO; GO:0007091; P:mitotic metaphase/anaphase transition; IMP:MGI.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:MGI.
DR   GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IDA:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR001180; Citron.
DR   InterPro; IPR017405; Citron_Rho-interacting_kinase.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   PIRSF; PIRSF038145; Citron_Rho-interacting_kinase; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Cell cycle;
KW   Cell division; Coiled coil; Cytoplasm; Developmental protein;
KW   Differentiation; Direct protein sequencing; Kinase; Metal-binding;
KW   Mitosis; Neurogenesis; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; SH3-binding; Transferase; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   2055       Citron Rho-interacting kinase.
FT                                /FTId=PRO_0000085909.
FT   DOMAIN       97    359       Protein kinase.
FT   DOMAIN      360    430       AGC-kinase C-terminal.
FT   DOMAIN     1469   1589       PH.
FT   DOMAIN     1617   1907       CNH.
FT   NP_BIND     103    111       ATP (By similarity).
FT   ZN_FING    1388   1437       Phorbol-ester/DAG-type.
FT   REGION     1132   1328       Interaction with Rho/Rac.
FT   COILED      441   1086       Potential.
FT   COILED     1091   1247       Potential.
FT   COILED     1275   1325       Potential.
FT   MOTIF      1979   1984       SH3-binding (Potential).
FT   COMPBIAS    550    962       Glu-rich.
FT   COMPBIAS   1276   1279       Poly-Lys.
FT   ACT_SITE    221    221       Proton acceptor (By similarity).
FT   BINDING     126    126       ATP (By similarity).
FT   MOD_RES     432    432       Phosphoserine (By similarity).
FT   MOD_RES     439    439       Phosphoserine (By similarity).
FT   MOD_RES     479    479       Phosphoserine.
FT   MOD_RES    1237   1237       Phosphotyrosine.
FT   MOD_RES    1504   1504       Phosphotyrosine.
FT   MOD_RES    1608   1608       Phosphoserine.
FT   MOD_RES    1747   1747       N6-acetyllysine (By similarity).
FT   MOD_RES    1999   1999       Phosphoserine (By similarity).
FT   MOD_RES    2021   2021       Phosphoserine (By similarity).
FT   VAR_SEQ       1    458       Missing (in isoform 3).
FT                                /FTId=VSP_012436.
FT   VAR_SEQ     459    466       DSQDKCHK -> MLLGEEAM (in isoform 3).
FT                                /FTId=VSP_012437.
FT   VAR_SEQ     467    494       MEQEMTRLHRRVSEVEAVLSQKEVELKA -> VSISTAGLR
FT                                PCSRILQSIYAEGSAGGHC (in isoform 2).
FT                                /FTId=VSP_012438.
FT   VAR_SEQ     495   2055       Missing (in isoform 2).
FT                                /FTId=VSP_012439.
FT   VAR_SEQ     693    735       Missing (in isoform 4).
FT                                /FTId=VSP_016093.
FT   VAR_SEQ    1279   1279       K -> KGLFSRRKEDPALPTQ (in isoform 5).
FT                                /FTId=VSP_016094.
FT   VAR_SEQ    1602   1602       A -> AARDHTSSEHQPVWVE (in isoform 5).
FT                                /FTId=VSP_016095.
FT   MUTAGEN     126    126       K->A: Loss of phosphorylation.
FT   CONFLICT     78     78       Q -> R (in Ref. 3; BAE26199).
FT   CONFLICT    182    182       F -> L (in Ref. 3; BAE26199).
FT   CONFLICT    234    234       E -> H (in Ref. 3; BAE26199).
FT   CONFLICT   1945   1945       Missing (in Ref. 6; AAH51165).
SQ   SEQUENCE   2055 AA;  235389 MW;  BDA9A12C14E12DF8 CRC64;
     MLKFKYGVRN PPEASASEPI ASRASRLNLF FQGKPPLMTQ QQMSALSREG MLDALFALFE
     ECSQPALMKM KHVSSFVQKY SDTIAELREL QPSARDFEVR SLVGCGHFAE VQVVREKATG
     DVYAMKIMKK KALLAQEQVS FFEEERNILS RSTSPWIPQL QYAFQDKNNL YLVMEYQPGG
     DFLSLLNRYE DQLDESMIQF YLAELILAVH SVHQMGYVHR DIKPENILID RTGEIKLVDF
     GSAAKMNSNK VDAKLPIGTP DYMAPEVLTV MNEDRRGTYG LDCDWWSVGV VAYEMVYGKT
     PFTEGTSART FNNIMNFQRF LKFPDDPKVS SELLDLLQSL LCVQKERLKF EGLCCHPFFA
     RTDWNNIRNS PPPFVPTLKS DDDTSNFDEP EKNSWVSSSV CQLSPSGFSG EELPFVGFSY
     SKALGYLGRS ESVVSSLDSP AKVSSMEKKL LIKSKELQDS QDKCHKMEQE MTRLHRRVSE
     VEAVLSQKEV ELKASETQRS LLEQDLATYI TECSSLKRSL EQARMEVSQE DDKALQLLHD
     IREQSRKLQE IKEQEYQAQV EEMRLMMNQL EEDLVSARRR SDLYESELRE SRLAAEEFKR
     KANECQHKLM KAKDQGKPEV GEYSKLEKIN AEQQLKIQEL QEKLEKAVKA STEATELLQN
     IRQAKERAER ELEKLHNRED SSEGIKKKLV EAEERRHSLE NKVKRLETME RRENRLKDDI
     QTKSEQIQQM ADKILELEEK HREAQVSAQH LEVHLKQKEQ HYEEKIKVLD NQIKKDLADK
     ESLENMMQRH EEEAHEKGKI LSEQKAMINA MDSKIRSLEQ RIVELSEANK LAANSSLFTQ
     RNMKAQEEMI SELRQQKFYL ETQAGKLEAQ NRKLEEQLEK ISHQDHSDKS RLLELETRLR
     EVSLEHEEQK LELKRQLTEL QLSLQERESQ LTALQAARAA LESQLRQAKT ELEETTAEAE
     EEIQALTAHR DEIQRKFDAL RNSCTVITDL EEQLNQLTED NAELNNQNFY LSKQLDEASG
     ANDEIVQLRS EVDHLRREIT EREMQLTSQK QTMEALKTTC TMLEEQVLDL EALNDELLEK
     ERQWEAWRSV LGDEKSQFEC RVRELQRMLD TEKQSRARAD QRITESRQVV ELAVKEHKAE
     ILALQQALKE QKLKAESLSD KLNDLEKKHA MLEMNARSLQ QKLETERELK QRLLEEQAKL
     QQQMDLQKNH IFRLTQGLQE ALDRADLLKT ERSDLEYQLE NIQVLYSHEK VKMEGTISQQ
     TKLIDFLQAK MDQPAKKKKV PLQYNELKLA LEKEKARCAE LEEALQKTRI ELRSAREEAA
     HRKATDHPHP STPATARQQI AMSAIVRSPE HQPSAMSLLA PPSSRRKESS TPEEFSRRLK
     ERMHHNIPHR FNVGLNMRAT KCAVCLDTVH FGRQASKCLE CQVMCHPKCS TCLPATCGLP
     AEYATHFTEA FCRDKMNSPG LQSKEPGSSL HLEGWMKVPR NNKRGQQGWD RKYIVLEGSK
     VLIYDNEARE AGQRPVEEFE LCLPDGDVSI HGAVGASELA NTAKADVPYI LKMESHPHTT
     CWPGRTLYLL APSFPDKQRW VTALESVVAG GRVSREKAEA DAKLLGNSLL KLEGDDRLDM
     NCTLPFSDQV VLVGTEEGLY ALNVLKNSLT HIPGIGAVFQ IYIIKDLEKL LMIAGEERAL
     CLVDVKKVKQ SLAQSHLPAQ PDVSPNIFEA VKGCHLFAAG KIENSLCICA AMPSKVVILR
     YNDNLSKYCI RKEIETSEPC SCIHFTNYSI LIGTNKFYEI DMKQYTLDEF LDKNDHSLAP
     AVFASSSNSF PVSIVQANSA GQREEYLLCF HEFGVFVDSY GRRSRTDDLK WSRLPLAFAY
     REPYLFVTHF NSLEVIEIQA RSSLGSPARA YLEIPNPRYL GPAISSGAIY LASSYQDKLR
     VICCKGNLVK ESGTEQHRVP STSRSSPNKR GPPTYNEHIT KRVASSPAPP EGPSHPREPS
     TPHRYRDREG RTELRRDKSP GRPLEREKSP GRMLSTRRER SPGRLFEDSS RGRLPAGAVR
     TPLSQVNKVW DQSSV
//
ID   CAMLG_MOUSE             Reviewed;         294 AA.
AC   P49070; Q99JU5;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2003, sequence version 2.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Calcium signal-modulating cyclophilin ligand;
DE            Short=CAML;
GN   Name=Camlg; Synonyms=Caml;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X CBA; TISSUE=Thymus;
RX   MEDLINE=96011657; PubMed=7590290; DOI=10.1016/0378-1119(95)00393-K;
RA   Kim H.S., Morales V.M., Dass C., Encinas J., Teitell M.,
RA   Blumberg R.S.;
RT   "Cloning of the gene encoding the mouse homologue of the human calcium
RT   signal-modulating ligand.";
RL   Gene 163:323-324(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 1-55.
RA   Morales V.M., Snapper S.B., Blumberg R.S.;
RT   "Sequence of the promoter region of the mouse CAMLG gene.";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Likely involved in the mobilization of calcium as a
CC       result of the TCR/CD3 complex interaction. Binds to cyclophilin B.
CC   -!- SUBUNIT: The N-terminal domain binds to TNFRSF13B/TACI (By
CC       similarity).
CC   -!- INTERACTION:
CC       Q80X16:Ryr1; NbExp=2; IntAct=EBI-309114, EBI-642079;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
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DR   EMBL; U21960; AAA87004.1; -; mRNA.
DR   EMBL; BC005688; AAH05688.1; -; mRNA.
DR   EMBL; AF078112; AAC33940.1; -; Genomic_DNA.
DR   IPI; IPI00308545; -.
DR   RefSeq; NP_031622.2; NM_007596.2.
DR   UniGene; Mm.2313; -.
DR   ProteinModelPortal; P49070; -.
DR   IntAct; P49070; 5.
DR   STRING; P49070; -.
DR   PhosphoSite; P49070; -.
DR   PRIDE; P49070; -.
DR   Ensembl; ENSMUST00000021963; ENSMUSP00000021963; ENSMUSG00000021501.
DR   GeneID; 12328; -.
DR   KEGG; mmu:12328; -.
DR   UCSC; uc007qrv.1; mouse.
DR   CTD; 12328; -.
DR   MGI; MGI:104728; Caml.
DR   eggNOG; roNOG07533; -.
DR   HOGENOM; HBG445350; -.
DR   HOVERGEN; HBG050786; -.
DR   InParanoid; P49070; -.
DR   OMA; KPSQEDG; -.
DR   OrthoDB; EOG4CNQS0; -.
DR   PhylomeDB; P49070; -.
DR   NextBio; 280920; -.
DR   ArrayExpress; P49070; -.
DR   Bgee; P49070; -.
DR   CleanEx; MM_CAML; -.
DR   Genevestigator; P49070; -.
DR   GermOnline; ENSMUSG00000021501; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:MGI.
DR   GO; GO:0001881; P:receptor recycling; IMP:MGI.
DR   InterPro; IPR016719; Ca_signal-mod_cyclophilin_lig.
DR   PIRSF; PIRSF018259; CAML; 1.
PE   1: Evidence at protein level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    294       Calcium signal-modulating cyclophilin
FT                                ligand.
FT                                /FTId=PRO_0000089292.
FT   TOPO_DOM      1    187       Cytoplasmic (Potential).
FT   TRANSMEM    188    208       Helical; (Potential).
FT   TOPO_DOM    209    238       Extracellular (Potential).
FT   TRANSMEM    239    255       Helical; (Potential).
FT   TOPO_DOM    256    294       Cytoplasmic (Potential).
FT   CONFLICT    254    254       V -> A (in Ref. 1; AAA87004).
SQ   SEQUENCE   294 AA;  32542 MW;  D21AC54BC9F609E5 CRC64;
     MEPVPAATDG GERPATPSGL SASQRRAELR RRKLLMNSEQ RINRIMGFHR PGSGSEEENQ
     TKSKPQDSDK LNSLSIPSVS KRVVLGDSVD GGGADQLGGV AEVRGTQLGD KLDSFIKAPE
     CSSKDGAELR QRTRGDLTAD PAQRASHHGL EQYLSRFEEA MKLRKQLISE KPSQEDGSTA
     EEFDSFRIFR LVGCALLALG VRAFVCKYLS IFAPFLTLQL AYMGLYKYFP KGEKKVKTTV
     LTAALLLSGI PAEVINRSMD TYSKMGEVFT DLCVYFFTFI FCHELLDYWG PEVP
//
ID   ROA1_MOUSE              Reviewed;         320 AA.
AC   P49312; P97312; Q3V269;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 112.
DE   RecName: Full=Heterogeneous nuclear ribonucleoprotein A1;
DE            Short=hnRNP A1;
DE   AltName: Full=HDP-1;
DE   AltName: Full=Helix-destabilizing protein;
DE   AltName: Full=Single-strand-binding protein;
DE   AltName: Full=Topoisomerase-inhibitor suppressed;
DE   AltName: Full=hnRNP core protein A1;
GN   Name=Hnrnpa1; Synonyms=Fli-2, Hnrpa1, Tis;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=93024387; PubMed=1406633;
RA   Ben-David Y., Bani M.R., Chabot B., de Koven A., Bernstein A.;
RT   "Retroviral insertions downstream of the heterogeneous nuclear
RT   ribonucleoprotein A1 gene in erythroleukemia cells: evidence that A1
RT   is not essential for cell growth.";
RL   Mol. Cell. Biol. 12:4449-4455(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lymphoma;
RX   MEDLINE=97069646; PubMed=8912629; DOI=10.1006/bbrc.1996.1609;
RA   Onishi Y., Kizaki H.;
RT   "Molecular cloning of the genes suppressed in RVC lymphoma cells by
RT   topoisomerase inhibitors.";
RL   Biochem. Biophys. Res. Commun. 228:7-13(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2;
RC   TISSUE=Amnion, Liver, Muellerian duct, Pancreas, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC   TISSUE=Limb, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 107-113 AND 285-300.
RC   STRAIN=OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-313, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Involved in the packaging of pre-mRNA into hnRNP
CC       particles, transport of poly(A) mRNA from the nucleus to the
CC       cytoplasm and may modulate splice site selection.
CC   -!- SUBUNIT: Identified in the spliceosome C complex, at least
CC       composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23,
CC       DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1,
CC       GPATC1, HNRNPA1, HNRNPA2B1, HNRPA3, HNRNPC, HNRPF, HNRPH1, HNRPK,
CC       HNRPM, HNRNPR, HNRNPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH,
CC       MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19,
CC       PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1,
CC       SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB,
CC       SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1,
CC       SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and
CC       ZCCHC8. Identified in a mRNP granule complex, at least composed of
CC       ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD,
CC       HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1,
CC       NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8,
CC       RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with
CC       SEPT6 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localized in
CC       cytoplasmic mRNP granules containing untranslated mRNAs (By
CC       similarity). Shuttles continuously between the nucleus and the
CC       cytoplasm along with mRNA. Component of ribonucleosomes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=P49312-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=P49312-2; Sequence=VSP_005825;
CC   -!- PTM: Sumoylated (By similarity).
CC   -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
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DR   EMBL; M99167; AAA37633.1; -; mRNA.
DR   EMBL; D86729; BAA13162.1; -; mRNA.
DR   EMBL; D86728; BAA13161.1; -; mRNA.
DR   EMBL; AK007802; BAB25267.1; -; mRNA.
DR   EMBL; AK088308; BAC40273.1; -; mRNA.
DR   EMBL; AK131999; BAE20929.1; -; mRNA.
DR   EMBL; AK135391; BAE22518.1; -; mRNA.
DR   EMBL; AK161730; BAE36552.1; -; mRNA.
DR   EMBL; AK166901; BAE39104.1; -; mRNA.
DR   EMBL; AK167161; BAE39302.1; -; mRNA.
DR   EMBL; AK167810; BAE39837.1; -; mRNA.
DR   EMBL; AK167913; BAE39920.1; -; mRNA.
DR   EMBL; AK168420; BAE40333.1; -; mRNA.
DR   EMBL; AK168531; BAE40409.1; -; mRNA.
DR   EMBL; BC080675; AAH80675.1; -; mRNA.
DR   EMBL; BC083136; AAH83136.1; -; mRNA.
DR   IPI; IPI00553777; -.
DR   IPI; IPI00817004; -.
DR   PIR; A44485; A44485.
DR   RefSeq; NP_034577.1; NM_010447.4.
DR   UniGene; Mm.237064; -.
DR   UniGene; Mm.432031; -.
DR   ProteinModelPortal; P49312; -.
DR   SMR; P49312; 8-190.
DR   IntAct; P49312; 5.
DR   STRING; P49312; -.
DR   PhosphoSite; P49312; -.
DR   PRIDE; P49312; -.
DR   Ensembl; ENSMUST00000036004; ENSMUSP00000042658; ENSMUSG00000046434.
DR   Ensembl; ENSMUST00000087351; ENSMUSP00000084609; ENSMUSG00000046434.
DR   GeneID; 15382; -.
DR   KEGG; mmu:15382; -.
DR   UCSC; uc007xxp.1; mouse.
DR   CTD; 15382; -.
DR   MGI; MGI:104820; Hnrnpa1.
DR   eggNOG; roNOG09634; -.
DR   HOVERGEN; HBG002295; -.
DR   OrthoDB; EOG4HQDKF; -.
DR   NextBio; 288050; -.
DR   ArrayExpress; P49312; -.
DR   Bgee; P49312; -.
DR   CleanEx; MM_HNRNPA1; -.
DR   Genevestigator; P49312; -.
DR   GermOnline; ENSMUSG00000058922; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:HGNC.
DR   GO; GO:0005654; C:nucleoplasm; ISS:HGNC.
DR   GO; GO:0005681; C:spliceosomal complex; ISS:HGNC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003697; F:single-stranded DNA binding; ISS:HGNC.
DR   GO; GO:0000380; P:alternative nuclear mRNA splicing, via spliceosome; IDA:MGI.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0051168; P:nuclear export; ISS:HGNC.
DR   GO; GO:0051170; P:nuclear import; ISS:HGNC.
DR   InterPro; IPR021662; HnRNPA1.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF11627; HnRNPA1; 1.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm;
KW   Direct protein sequencing; Isopeptide bond; Methylation;
KW   mRNA processing; mRNA splicing; mRNA transport; Nucleus;
KW   Phosphoprotein; Repeat; Ribonucleoprotein; RNA-binding; Spliceosome;
KW   Transport; Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    320       Heterogeneous nuclear ribonucleoprotein
FT                                A1.
FT                                /FTId=PRO_0000081830.
FT   DOMAIN       14     97       RRM 1.
FT   DOMAIN      105    184       RRM 2.
FT   REGION        4     94       Globular A domain.
FT   REGION       95    185       Globular B domain.
FT   REGION      218    240       RNA-binding RGG-box.
FT   REGION      268    305       Nuclear targeting sequence (By
FT                                similarity).
FT   COMPBIAS    195    320       Gly-rich.
FT   COMPBIAS    308    313       Poly-Ser.
FT   MOD_RES       2      2       N-acetylserine.
FT   MOD_RES       3      3       N6-acetyllysine (By similarity).
FT   MOD_RES       4      4       Phosphoserine.
FT   MOD_RES       6      6       Phosphoserine.
FT   MOD_RES      91     91       Phosphoserine (By similarity).
FT   MOD_RES      95     95       Phosphoserine (By similarity).
FT   MOD_RES     113    113       N6-acetyllysine (By similarity).
FT   MOD_RES     138    138       Phosphothreonine (By similarity).
FT   MOD_RES     142    142       Phosphoserine (By similarity).
FT   MOD_RES     167    167       Phosphotyrosine (By similarity).
FT   MOD_RES     194    194       Omega-N-methylated arginine (By
FT                                similarity).
FT   MOD_RES     206    206       Dimethylated arginine; alternate (By
FT                                similarity).
FT   MOD_RES     206    206       Omega-N-methylarginine; alternate (By
FT                                similarity).
FT   MOD_RES     225    225       Dimethylated arginine; alternate (By
FT                                similarity).
FT   MOD_RES     225    225       Omega-N-methylarginine; alternate (By
FT                                similarity).
FT   MOD_RES     259    259       Phosphoserine (By similarity).
FT   MOD_RES     286    286       Phosphoserine (By similarity).
FT   MOD_RES     289    289       Phosphotyrosine (By similarity).
FT   MOD_RES     295    295       Phosphotyrosine (By similarity).
FT   MOD_RES     298    298       N6-acetyllysine (By similarity).
FT   MOD_RES     305    305       Phosphotyrosine (By similarity).
FT   MOD_RES     313    313       Phosphoserine.
FT   MOD_RES     316    316       Phosphoserine (By similarity).
FT   CROSSLNK    113    113       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   VAR_SEQ     252    303       Missing (in isoform Short).
FT                                /FTId=VSP_005825.
SQ   SEQUENCE   320 AA;  34196 MW;  59485C9FA1FF8AE1 CRC64;
     MSKSESPKEP EQLRKLFIGG LSFETTDESL RSHFEQWGTL TDCVVMRDPN TKRSRGFGFV
     TYATVEEVDA AMNARPHKVD GRVVEPKRAV SREDSQRPGA HLTVKKIFVG GIKEDTEEHH
     LRDYFEQYGK IEVIEIMTDR GSGKKRGFAF VTFDDHDSVD KIVIQKYHTV NGHNCEVRKA
     LSKQEMASAS SSQRGRSGSG NFGGGRGGGF GGNDNFGRGG NFSGRGGFGG SRGGGGYGGS
     GDGYNGFGND GSNFGGGGSY NDFGNYNNQS SNFGPMKGGN FGGRSSGPYG GGGQYFAKPR
     NQGGYGGSSS SSSYGSGRRF
//
ID   PPM1A_MOUSE             Reviewed;         382 AA.
AC   P49443;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Protein phosphatase 1A;
DE            EC=3.1.3.16;
DE   AltName: Full=Protein phosphatase 2C isoform alpha;
DE            Short=PP2C-alpha;
DE   AltName: Full=Protein phosphatase IA;
GN   Name=Ppm1a; Synonyms=Pppm1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=94333828; PubMed=8056349; DOI=10.1016/0378-1119(94)90026-4;
RA   Kato S., Kobayashi T., Terasawa T., Ohnishi M., Sasahara Y.,
RA   Kanamaru R., Tamura S.;
RT   "The cDNA sequence encoding mouse Mg2+ -dependent protein phosphatase
RT   alpha.";
RL   Gene 145:311-312(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Enzyme with a broad specificity. Negatively regulates
CC       TGF-beta signaling through dephosphorylating SMAD2 and SMAD3,
CC       resulting in their dissociation from SMAD4, nuclear export of the
CC       SMADs and termination of the TGF-beta-mediated signaling (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- COFACTOR: Binds 2 magnesium or manganese ions per subunit.
CC   -!- SUBUNIT: Monomer (By similarity). Interacts with SMAD2; the
CC       interaction dephosphorylates SMAD2 in its C-terminal SXS motif
CC       resulting in disruption of the SMAD2/SMAD4 complex, SMAD2 nuclear
CC       export and termination of the TGF-beta-mediated signaling.
CC       Interacts with SMAD2; the interaction dephosphorylates SMAD2 in
CC       its C-terminal SXS motif resulting in disruption of the
CC       SMAD2/SMAD4 complex, SMAD2 nuclear export and termination of the
CC       TGF-beta-mediated signaling (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the PP2C family.
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DR   EMBL; D28117; BAA05662.1; -; mRNA.
DR   EMBL; BC008595; AAH08595.1; -; mRNA.
DR   IPI; IPI00114802; -.
DR   PIR; I53823; I53823.
DR   RefSeq; NP_032936.1; NM_008910.3.
DR   UniGene; Mm.261045; -.
DR   ProteinModelPortal; P49443; -.
DR   SMR; P49443; 2-368.
DR   STRING; P49443; -.
DR   PhosphoSite; P49443; -.
DR   PRIDE; P49443; -.
DR   Ensembl; ENSMUST00000021514; ENSMUSP00000021514; ENSMUSG00000021096.
DR   GeneID; 19042; -.
DR   KEGG; mmu:19042; -.
DR   UCSC; uc007nvu.1; mouse.
DR   CTD; 19042; -.
DR   MGI; MGI:99878; Ppm1a.
DR   eggNOG; roNOG14282; -.
DR   HOGENOM; HBG747569; -.
DR   HOVERGEN; HBG053647; -.
DR   InParanoid; P49443; -.
DR   OMA; SVKNGIR; -.
DR   OrthoDB; EOG4GMTX1; -.
DR   PhylomeDB; P49443; -.
DR   BRENDA; 3.1.3.16; 244.
DR   NextBio; 295493; -.
DR   ArrayExpress; P49443; -.
DR   Bgee; P49443; -.
DR   Genevestigator; P49443; -.
DR   GermOnline; ENSMUSG00000021096; Mus musculus.
DR   GO; GO:0008287; C:protein serine/threonine phosphatase complex; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
DR   InterPro; IPR001932; PP2C-like.
DR   InterPro; IPR012911; PP2C_C.
DR   InterPro; IPR000222; PP2C_Mn2_Asp60_BS.
DR   InterPro; IPR014045; PP2C_N.
DR   InterPro; IPR015655; Protein_Pase_2C.
DR   Gene3D; G3DSA:3.60.40.10; PP2C-related; 1.
DR   Gene3D; G3DSA:1.10.10.430; PP2C_C; 1.
DR   PANTHER; PTHR13832; PP2C; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   Pfam; PF07830; PP2C_C; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-related; 1.
DR   SUPFAM; SSF81601; PP2C_C; 1.
DR   PROSITE; PS01032; PP2C; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Nucleus;
KW   Phosphoprotein; Protein phosphatase.
FT   CHAIN         1    382       Protein phosphatase 1A.
FT                                /FTId=PRO_0000057742.
FT   METAL        60     60       Manganese 1 (By similarity).
FT   METAL        60     60       Manganese 2 (By similarity).
FT   METAL        61     61       Manganese 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       239    239       Manganese 2 (By similarity).
FT   METAL       282    282       Manganese 2 (By similarity).
FT   MOD_RES     375    375       Phosphoserine (By similarity).
FT   MOD_RES     377    377       Phosphoserine.
SQ   SEQUENCE   382 AA;  42433 MW;  DC206610E1583870 CRC64;
     MGAFLDKPKM EKHNAQGQGN GLRYGLSSMQ GWRVEMEDAH TAVIGLPSGL ETWSFFAVYD
     GHAGSQVAKY CCEHLLDHIT NNQDFRGSAG APSVENVKNG IRTGFLEIDE HMRVMSEKKH
     GADRSGSTAV GVLISPQHTY FINCGDSRGL LCRNRKVHFF TQDHKPSNPL EKERIQNAGG
     SVMIQRVNGS LAVSRALGDF DYKCVHGKGP TEQLVSPEPE VHDIERSEED DQFIILACDG
     IWDVMGNEEL CDFVRSRLEV TDDLEKVCNE VVDTCLYKGS RDNMSVILIC FPSAPKVSAE
     AVKKEAELDK YLESRVEEII KKQVEGVPDL VHVMRTLASE NIPSLPPGGE LASKRNVIEA
     VYNRLNPYKN DDTDSASTDD MW
//
ID   PTPRE_MOUSE             Reviewed;         699 AA.
AC   P49446; Q3U369; Q60986; Q61042; Q62134; Q62444; Q64496;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 3.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Receptor-type tyrosine-protein phosphatase epsilon;
DE            Short=Protein-tyrosine phosphatase epsilon;
DE            Short=R-PTP-epsilon;
DE            EC=3.1.3.48;
DE   Flags: Precursor;
GN   Name=Ptpre; Synonyms=Ptpe;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N;
RX   MEDLINE=96064677; PubMed=7592814; DOI=10.1074/jbc.270.44.26116;
RA   Elson A., Leder P.;
RT   "Protein-tyrosine phosphatase epsilon. An isoform specifically
RT   expressed in mouse mammary tumors initiated by v-Ha-ras OR neu.";
RL   J. Biol. Chem. 270:26116-26122(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INDUCTION, AND TISSUE
RP   SPECIFICITY.
RX   MEDLINE=96109240; PubMed=8618876; DOI=10.1073/pnas.92.26.12235;
RA   Elson A., Leder P.;
RT   "Identification of a cytoplasmic, phorbol ester-inducible isoform of
RT   protein tyrosine phosphatase epsilon.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:12235-12239(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, ENZYME REGULATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Osteoclast;
RX   MEDLINE=96181534; PubMed=8610169; DOI=10.1073/pnas.93.7.3068;
RA   Schmidt A., Rutledge S.J., Endo N., Opas E., Tanaka H., Wesolowski G.,
RA   Leu C.T., Huang Z., Ramachandaran C., Rodan S.B., Rodan G.A.;
RT   "Protein-tyrosine phosphatase activity regulates osteoclast formation
RT   and function: inhibition by alendronate.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:3068-3073(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=DBA/2;
RA   Mukouyama Y.;
RL   Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Lung;
RA   Hou E.W., Li S.L.;
RL   Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 224-332.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=93086603; PubMed=1454056; DOI=10.1007/BF00419663;
RA   Schepens J., Zeeuwen P., Wieringa B., Hendriks W.;
RT   "Identification and typing of members of the protein-tyrosine
RT   phosphatase gene family expressed in mouse brain.";
RL   Mol. Biol. Rep. 16:241-248(1992).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 224-332, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Myeloid leukemia cell;
RX   MEDLINE=92032882; PubMed=1932742;
RA   Yi T., Cleveland J.L., Ihle J.N.;
RT   "Identification of novel protein tyrosine phosphatases of
RT   hematopoietic cells by polymerase chain reaction amplification.";
RL   Blood 78:2222-2228(1991).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 224-332.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=95134232; PubMed=7832766;
RA   Hendriks W., Schepens J., Brugman C., Zeeuwen P., Wieringa B.;
RT   "A novel receptor-type protein tyrosine phosphatase with a single
RT   catalytic domain is specifically expressed in mouse brain.";
RL   Biochem. J. 305:499-504(1995).
RN   [11]
RP   ALTERNATIVE PROMOTER USAGE.
RX   PubMed=9914474; DOI=10.1046/j.1432-1327.1999.00004.x;
RA   Tanuma N., Nakamura K., Kikuchi K.;
RT   "Distinct promoters control transmembrane and cytosolic protein
RT   tyrosine phosphatase epsilon expression during macrophage
RT   differentiation.";
RL   Eur. J. Biochem. 259:46-54(1999).
RN   [12]
RP   IDENTIFICATION (ISOFORM 3), ALTERNATIVE INITIATION, SUBCELLULAR
RP   LOCATION, AND PROTEOLYTIC PROCESSING.
RX   PubMed=10980613; DOI=10.1038/sj.onc.1203790;
RA   Gil-Henn H., Volohonsky G., Toledano-Katchalski H., Gandre S.,
RA   Elson A.;
RT   "Generation of novel cytoplasmic forms of protein tyrosine phosphatase
RT   epsilon by proteolytic processing and translational control.";
RL   Oncogene 19:4375-4384(2000).
RN   [13]
RP   SUBUNIT, AND DOMAIN.
RX   PubMed=12861030; DOI=10.1128/MCB.23.15.5460-5471.2003;
RA   Toledano-Katchalski H., Tiran Z., Sines T., Shani G., Granot-Attas S.,
RA   den Hertog J., Elson A.;
RT   "Dimerization in vivo and inhibition of the nonreceptor form of
RT   protein tyrosine phosphatase epsilon.";
RL   Mol. Cell. Biol. 23:5460-5471(2003).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-695, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [15]
RP   FUNCTION (ISOFORM 2), SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=18006633; DOI=10.1210/en.2007-0908;
RA   Aga-Mizrachi S., Brutman-Barazani T., Jacob A.I., Bak A., Elson A.,
RA   Sampson S.R.;
RT   "Cytosolic protein tyrosine phosphatase-epsilon is a negative
RT   regulator of insulin signaling in skeletal muscle.";
RL   Endocrinology 149:605-614(2008).
RN   [16]
RP   FUNCTION (ISOFORM 1), DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=18924107; DOI=10.1002/pmic.200700596;
RA   De Franceschi L., Biondani A., Carta F., Turrini F., Laudanna C.,
RA   Deana R., Brunati A.M., Turretta L., Iolascon A., Perrotta S.,
RA   Elson A., Bulato C., Brugnara C.;
RT   "PTPepsilon has a critical role in signaling transduction pathways and
RT   phosphoprotein network topology in red cells.";
RL   Proteomics 8:4695-4708(2008).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-695, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [18]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19508371; DOI=10.1111/j.1365-3083.2009.02235.x;
RA   Akimoto M., Mishra K., Lim K.-T., Tani N., Hisanaga S.-I.,
RA   Katagiri T., Elson A., Mizuno K., Yakura H.;
RT   "Protein tyrosine phosphatase epsilon is a negative regulator of
RT   FcepsilonRI-mediated mast cell responses.";
RL   Scand. J. Immunol. 69:401-411(2009).
CC   -!- FUNCTION: Isoform 1 acts as a negative regulator of insulin
CC       receptor (IR) signaling and is involved in insulin-induced glucose
CC       metabolism mainly through direct dephosphorylation and
CC       inactivation of IR in hepatocytes and liver (By similarity). Plays
CC       a critical role in signaling transduction pathways and
CC       phosphoprotein network topology in red blood cells. May play a
CC       role in osteoclast formation and function.
CC   -!- FUNCTION: Isoform 2 acts as a negative regulator of insulin
CC       receptor (IR) signaling in skeletal muscle. Regulates insulin-
CC       induced tyrosine phosphorylation of insulin receptor (IR) and
CC       insulin receptor substrate 1 (IRS-1), phosphorylation of protein
CC       kinase B and glycogen synthase kinase-3 and insulin induced
CC       stimulation of glucose uptake.
CC   -!- FUNCTION: Isoform 1 and isoform 2 act as a negative regulator of
CC       FceRI-mediated signal transduction leading to cytokine production
CC       and degranulation, most likely by acting at the level of SYK to
CC       affect downstream events such as phosphorylation of SLP76 and LAT
CC       and mobilization of Ca(2+).
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- ENZYME REGULATION: Isoform 1 is inhibited by alendronate (ALN),
CC       orthovanadate, and phenylarsine oxide (PAO).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=70 uM for fluorescein diphosphate (isoform 1);
CC         Vmax=6 umol/min/mg enzyme for fluorescein diphosphate (isoform
CC         1);
CC   -!- SUBUNIT: Monomer (By similarity). Isoform 2: Homodimer. Can form
CC       oligomers. Dimerization is increased by oxidative stress and
CC       decreased by EGFR. Isoform 2 interacts with GRB2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
CC       membrane protein.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Note=Predominantly
CC       cytoplasmic. A small fraction is also associated with nucleus and
CC       membrane. Insulin can induce translocation to the membrane.
CC   -!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage, Alternative initiation; Named isoforms=3;
CC       Name=1; Synonyms=PTPeM, RPTPe, tm-PTPe;
CC         IsoId=P49446-1; Sequence=Displayed;
CC         Note=Produced by alternative promoter usage;
CC       Name=2; Synonyms=PTPeC, cyt-PTPe;
CC         IsoId=P49446-2; Sequence=VSP_038492;
CC         Note=Produced by alternative promoter usage;
CC       Name=3; Synonyms=p67;
CC         IsoId=P49446-3; Sequence=VSP_038491;
CC         Note=Produced by alternative initiation at Met-85 of isoform 1;
CC   -!- TISSUE SPECIFICITY: Isoform 2 is expressed in the spleen and
CC       thymus (at protein level). Detected in fibroblasts, myeloid cells,
CC       macrophages, and T-cells but not in B-cell lines. Isoform 1 and
CC       isoform 2 are expressed predominantly in the brain, testes, and
CC       lungs, with lower levels present in lymph nodes, thymus, spleen,
CC       heart and mammary glands. Isoform 1 is expressed in osteoclasts
CC       and not in osteoblasts and its expression is related to osteoclast
CC       differentiation. It is also expressed in the erythrocytes. Isoform
CC       2 is strongly expressed in skeletal muscle and L6 skeletal muscle
CC       cell line.
CC   -!- INDUCTION: Isoform 2 is induced by 12-O-tetradecanoylphorbol-13-
CC       acetate (TPA) and its induction is dependent upon PKC activity.
CC   -!- DOMAIN: The tyrosine-protein phosphatase 2 domain (D2) mediates
CC       dimerization. The extreme N- and C- termini of the D2 domain act
CC       to inhibit dimerization and removal of these sequences increases
CC       dimerization and inhibits enzyme activity.
CC   -!- PTM: A catalytically active cytoplasmic form (p65) is produced by
CC       proteolytic cleavage of either isoform 1, isoform 2 or isoform 3.
CC   -!- PTM: Isoform 1 and isoform 2 are phosphorylated on tyrosine
CC       residues by tyrosine kinase Neu (By similarity).
CC   -!- PTM: Isoform 1 is glycosylated (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice show greater insulin-induced tyrosine
CC       phosphorylation of insulin receptor (IR) and insulin receptor
CC       substrate 1 (IRS-1) in the skeletal muscle. Antigen- and IgE-
CC       mediated passive systemic anaphylactic reactions are enhanced.
CC       Erythrocytes exhibit abnormal morphology, increased Ca(2+)-
CC       activated-K(+) channel activity and marked perturbation of the
CC       erythrocyte membrane tyrosine phosphoproteome.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 4 subfamily.
CC   -!- SIMILARITY: Contains 2 tyrosine-protein phosphatase domains.
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DR   EMBL; U35368; AAC52281.1; -; mRNA.
DR   EMBL; U36758; AAC52331.1; -; mRNA.
DR   EMBL; U40280; AAB02190.1; -; mRNA.
DR   EMBL; D83484; BAA11927.1; -; mRNA.
DR   EMBL; U62387; AAB04553.1; -; mRNA.
DR   EMBL; AK154910; BAE32920.1; -; mRNA.
DR   EMBL; CH466531; EDL17805.1; -; Genomic_DNA.
DR   EMBL; CH466531; EDL17807.1; -; Genomic_DNA.
DR   EMBL; Z23052; CAA80587.1; -; mRNA.
DR   EMBL; Z23053; CAA80588.1; -; mRNA.
DR   IPI; IPI00405224; -.
DR   IPI; IPI00654319; -.
DR   IPI; IPI00954626; -.
DR   PIR; B61180; B61180.
DR   PIR; JC6132; JC6132.
DR   PIR; S40284; S40284.
DR   RefSeq; NP_035342.3; NM_011212.3.
DR   UniGene; Mm.945; -.
DR   ProteinModelPortal; P49446; -.
DR   SMR; P49446; 110-690.
DR   STRING; P49446; -.
DR   PhosphoSite; P49446; -.
DR   PRIDE; P49446; -.
DR   Ensembl; ENSMUST00000054880; ENSMUSP00000059963; ENSMUSG00000041836.
DR   Ensembl; ENSMUST00000073961; ENSMUSP00000073616; ENSMUSG00000041836.
DR   Ensembl; ENSMUST00000097980; ENSMUSP00000095594; ENSMUSG00000041836.
DR   GeneID; 19267; -.
DR   KEGG; mmu:19267; -.
DR   CTD; 19267; -.
DR   MGI; MGI:97813; Ptpre.
DR   eggNOG; roNOG10614; -.
DR   GeneTree; ENSGT00590000082937; -.
DR   HOVERGEN; HBG053758; -.
DR   InParanoid; P49446; -.
DR   OMA; IVIDAMI; -.
DR   OrthoDB; EOG44BB1S; -.
DR   BRENDA; 3.1.3.48; 244.
DR   ArrayExpress; P49446; -.
DR   Bgee; P49446; -.
DR   CleanEx; MM_PTPRE; -.
DR   Genevestigator; P49446; -.
DR   GermOnline; ENSMUSG00000041836; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:MGI.
DR   GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0033003; P:regulation of mast cell activation; IMP:UniProtKB.
DR   GO; GO:0007185; P:transmembrane receptor protein tyrosine phosphatase signaling pathway; IDA:MGI.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   InterPro; IPR016336; Tyr_Pase_rcpt_a/e-type.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PIRSF; PIRSF002006; PTPR_alpha_epsilon; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 2.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   1: Evidence at protein level;
KW   Alternative initiation; Alternative promoter usage; Cell membrane;
KW   Cytoplasm; Glycoprotein; Hydrolase; Membrane; Phosphoprotein;
KW   Protein phosphatase; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     19       Potential.
FT   CHAIN        20    699       Receptor-type tyrosine-protein
FT                                phosphatase epsilon.
FT                                /FTId=PRO_0000025440.
FT   TOPO_DOM     20     45       Extracellular (Potential).
FT   TRANSMEM     46     68       Helical; (Potential).
FT   TOPO_DOM     69    699       Cytoplasmic (Potential).
FT   DOMAIN      134    393       Tyrosine-protein phosphatase 1.
FT   DOMAIN      425    688       Tyrosine-protein phosphatase 2.
FT   REGION      334    340       Substrate binding (By similarity).
FT   ACT_SITE    334    334       Phosphocysteine intermediate (By
FT                                similarity).
FT   ACT_SITE    629    629       Phosphocysteine intermediate (By
FT                                similarity).
FT   BINDING     302    302       Substrate (By similarity).
FT   BINDING     378    378       Substrate (By similarity).
FT   MOD_RES     695    695       Phosphotyrosine.
FT   CARBOHYD     23     23       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     31     31       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1     84       Missing (in isoform 3).
FT                                /FTId=VSP_038491.
FT   VAR_SEQ       1     69       MEPFCPLLLASFSLSLARAGQGNDTTPTESNWTSTTAGPPD
FT                                PGASQPLLTWLLLPLLLLLFLLAAYFFR -> MSSRKNFSR
FT                                LTW (in isoform 2).
FT                                /FTId=VSP_038492.
FT   CONFLICT    137    137       E -> K (in Ref. 6; BAE32920).
FT   CONFLICT    500    500       G -> A (in Ref. 4; BAA11927).
FT   CONFLICT    506    506       V -> G (in Ref. 1; AAC52281, 2; AAC52331
FT                                and 5; AAB04553).
FT   CONFLICT    521    522       IV -> ML (in Ref. 4; BAA11927).
FT   CONFLICT    606    606       M -> I (in Ref. 1; AAC52281 and 2;
FT                                AAC52331).
SQ   SEQUENCE   699 AA;  80688 MW;  581EF9CB881BC05B CRC64;
     MEPFCPLLLA SFSLSLARAG QGNDTTPTES NWTSTTAGPP DPGASQPLLT WLLLPLLLLL
     FLLAAYFFRF RKQRKAVVSS NDKKMPNGIL EEQEQQRVML LSRSPSGPKK FFPIPVEHLE
     EEIRVRSADD CKRFREEFNS LPSGHIQGTF ELANKEENRE KNRYPNILPN DHCRVILSQV
     DGIPCSDYIN ASYIDGYKEK NKFIAAQGPK QETVNDFWRM VWEQRSATIV MLTNLKERKE
     EKCYQYWPDQ GCWTYGNIRV CVEDCVVLVD YTIRKFCIHP QLPDSCKAPR LVSQLHFTSW
     PDFGVPFTPI GMLKFLKKVK TLNPSHAGPI VVHCSAGVGR TGTFIVIDAM MDMIHSEQKV
     DVFEFVSRIR NQRPQMVQTD VQYTFIYQAL LEYYLYGDTE LDVSSLERHL QTLHSTATHF
     DKIGLEEEFR KLTNVRIMKE NMRTGNLPAN MKKARVIQII PYDFNRVILS MKRGQEFTDY
     INASFIDGYR QKDYFMATQG PLAHTVEDFW RMVWEWKSHT IVMLTEVQER EQDKCYQYWP
     TEGSVTHGDI TIEIKSDTLS EAISVRDFLV TFKQPLARQE EQVRMVRQFH FHGWPEVGIP
     AEGKGMIDLI AAVQKQQQQT GNHPITVHCS AGAGRTGTFI ALSNILERVK AEGLLDVFQA
     VKSLRLQRPH MVQTLEQYEF CYKVVQDFID IFSDYANFK
//
ID   PCY1A_MOUSE             Reviewed;         367 AA.
AC   P49586; Q542W4;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   08-MAR-2011, entry version 100.
DE   RecName: Full=Choline-phosphate cytidylyltransferase A;
DE            EC=2.7.7.15;
DE   AltName: Full=CCT-alpha;
DE   AltName: Full=CTP:phosphocholine cytidylyltransferase A;
DE            Short=CCT A;
DE            Short=CT A;
DE   AltName: Full=Phosphorylcholine transferase A;
GN   Name=Pcyt1a; Synonyms=Ctpct, Pcyt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Testis;
RX   MEDLINE=94140374; PubMed=8307580; DOI=10.1016/S0888-7543(05)80377-5;
RA   Rutherford M.S., Rock C.O., Jenkins N.A., Gilbert D.J., Tessner T.G.,
RA   Copeland N.G., Jackowski S.;
RT   "The gene for murine CTP:phosphocholine cytidylyltransferase (Ctpct)
RT   is located on mouse chromosome 16.";
RL   Genomics 18:698-701(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=95002145; PubMed=7918629; DOI=10.1016/0167-4781(94)90056-6;
RA   Kalmar G.B., Kay R.J., Lachance A.C., Cornell R.B.;
RT   "Primary structure and expression of a human CTP:phosphocholine
RT   cytidylyltransferase.";
RL   Biochim. Biophys. Acta 1219:328-334(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/J;
RX   MEDLINE=97294724; PubMed=9148929; DOI=10.1074/jbc.272.20.13146;
RA   Tang W., Keesler G.A., Tabas I.;
RT   "The structure of the gene for murine CTP:phosphocholine
RT   cytidylyltransferase, Ctpct. Relationship of exon structure to
RT   functional domains and identification of transcriptional start sites
RT   and potential upstream regulatory elements.";
RL   J. Biol. Chem. 272:13146-13151(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-319 AND
RP   SER-347, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Controls phosphatidylcholine synthesis.
CC   -!- CATALYTIC ACTIVITY: CTP + choline phosphate = diphosphate + CDP-
CC       choline.
CC   -!- ENZYME REGULATION: By phosphorylation (By similarity).
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine
CC       biosynthesis; phosphatidylcholine from phosphocholine: step 1/2.
CC   -!- SUBUNIT: Homodimer; disulfide-linked (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity).
CC       Membrane; Peripheral membrane protein (By similarity). Note=It can
CC       interconvert between an inactive cytosolic form and an active
CC       membrane-bound form (By similarity).
CC   -!- PTM: The serine residues of the C-terminus are phosphorylated. The
CC       inactive soluble form is stabilized by phosphorylation, the active
CC       membrane bound form is promoted by anionic lipids or
CC       diacylglycerol, and is stabilized by dephosphorylation (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the cytidylyltransferase family.
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DR   EMBL; Z12302; CAA78172.1; -; mRNA.
DR   EMBL; L28956; AAA53526.1; -; mRNA.
DR   EMBL; U84207; AAB63446.1; -; Genomic_DNA.
DR   EMBL; U84200; AAB63446.1; JOINED; Genomic_DNA.
DR   EMBL; U84201; AAB63446.1; JOINED; Genomic_DNA.
DR   EMBL; U84202; AAB63446.1; JOINED; Genomic_DNA.
DR   EMBL; U84203; AAB63446.1; JOINED; Genomic_DNA.
DR   EMBL; U84204; AAB63446.1; JOINED; Genomic_DNA.
DR   EMBL; U84205; AAB63446.1; JOINED; Genomic_DNA.
DR   EMBL; U84206; AAB63446.1; JOINED; Genomic_DNA.
DR   EMBL; AK076050; BAC36148.1; -; mRNA.
DR   EMBL; AK076830; BAC36497.1; -; mRNA.
DR   EMBL; BC018313; AAH18313.1; -; mRNA.
DR   IPI; IPI00115490; -.
DR   PIR; A49366; S24935.
DR   RefSeq; NP_001156631.1; NM_001163159.1.
DR   RefSeq; NP_001156632.1; NM_001163160.1.
DR   RefSeq; NP_034111.1; NM_009981.4.
DR   UniGene; Mm.98775; -.
DR   ProteinModelPortal; P49586; -.
DR   SMR; P49586; 40-216.
DR   STRING; P49586; -.
DR   PhosphoSite; P49586; -.
DR   PRIDE; P49586; -.
DR   Ensembl; ENSMUST00000079791; ENSMUSP00000078721; ENSMUSG00000005615.
DR   Ensembl; ENSMUST00000115140; ENSMUSP00000110793; ENSMUSG00000005615.
DR   GeneID; 13026; -.
DR   KEGG; mmu:13026; -.
DR   UCSC; uc007yyv.1; mouse.
DR   CTD; 13026; -.
DR   MGI; MGI:88557; Pcyt1a.
DR   eggNOG; roNOG05834; -.
DR   GeneTree; ENSGT00390000000269; -.
DR   HOGENOM; HBG587468; -.
DR   HOVERGEN; HBG053531; -.
DR   InParanoid; P49586; -.
DR   OMA; TEEDGIP; -.
DR   OrthoDB; EOG4DR9CX; -.
DR   PhylomeDB; P49586; -.
DR   BRENDA; 2.7.7.15; 244.
DR   NextBio; 282896; -.
DR   ArrayExpress; P49586; -.
DR   Bgee; P49586; -.
DR   Genevestigator; P49586; -.
DR   GermOnline; ENSMUSG00000005615; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR   GO; GO:0042587; C:glycogen granule; IDA:MGI.
DR   GO; GO:0004105; F:choline-phosphate cytidylyltransferase activity; IEA:EC.
DR   GO; GO:0009628; P:response to abiotic stimulus; IDA:MGI.
DR   InterPro; IPR004821; Cyt_trans-rel.
DR   InterPro; IPR004820; Cytidylyltransf.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Pfam; PF01467; CTP_transf_2; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Disulfide bond; Membrane;
KW   Nucleotidyltransferase; Phospholipid biosynthesis; Phosphoprotein;
KW   Repeat; Transferase.
FT   CHAIN         1    367       Choline-phosphate cytidylyltransferase A.
FT                                /FTId=PRO_0000208454.
FT   REPEAT      319    324       1.
FT   REPEAT      329    333       2; approximate.
FT   REPEAT      343    348       3.
FT   REGION       74    235       Catalytic (Potential).
FT   REGION      228    287       Amphipathic (Potential).
FT   REGION      256    288       3 X 11 AA approximate tandem repeats.
FT   REGION      319    348       3 X repeats.
FT   MOD_RES       8      8       N6-acetyllysine (By similarity).
FT   MOD_RES     315    315       Phosphoserine.
FT   MOD_RES     319    319       Phosphoserine.
FT   MOD_RES     321    321       Phosphoserine (By similarity).
FT   MOD_RES     325    325       Phosphothreonine (By similarity).
FT   MOD_RES     329    329       Phosphoserine (By similarity).
FT   MOD_RES     331    331       Phosphoserine (By similarity).
FT   MOD_RES     347    347       Phosphoserine.
FT   MOD_RES     362    362       Phosphoserine.
FT   DISULFID     37     37       Interchain (By similarity).
FT   CONFLICT    360    360       D -> V (in Ref. 2; AAA53526).
SQ   SEQUENCE   367 AA;  41667 MW;  306B656D2EAAA2B3 CRC64;
     MDAQSSAKVN SRKRRKEAPG PNGATEEDGI PSKVQRCAVG LRQPAPFSDE IEVDFSKPYV
     RVTMEEACRG TPCERPVRVY ADGIFDLFHS GHARALMQAK NLFPNTYLIV GVCSDELTHN
     FKGFTVMNEN ERYDAVQHCR YVDEVVRNAP WTLTPEFLAE HRIDFVAHDD IPYSSAGSDD
     VYKHIKDAGM FAPTQRTEGI STSDIITRIV RDYDVYARRN LQRGYTAKEL NVSFINEKKY
     HLQERVDKVK KKVKDVEEKS KEFVQKVEEK SIDLIQKWEE KSREFIGSFL EMFGPEGALK
     HMLKEGKGRM LQAISPKQSP SSSPTHERSP SPSFRWPFSG KTSPSSSPAS LSRCRAVTCD
     ISEDEED
//
ID   CDK5_MOUSE              Reviewed;         292 AA.
AC   P49615;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   08-MAR-2011, entry version 109.
DE   RecName: Full=Cyclin-dependent kinase 5;
DE            EC=2.7.11.22;
DE   AltName: Full=CRK6;
DE   AltName: Full=Cell division protein kinase 5;
DE   AltName: Full=Serine/threonine-protein kinase PSSALRE;
DE   AltName: Full=Tau protein kinase II catalytic subunit;
DE            Short=TPKII catalytic subunit;
GN   Name=Cdk5; Synonyms=Crk6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=95135945; PubMed=7834371; DOI=10.1016/0006-8993(94)91197-5;
RA   Ino H., Ishizuka T., Chiba T., Tatibana M.;
RT   "Expression of CDK5 (PSSALRE kinase), a neural cdc2-related protein
RT   kinase, in the mature and developing mouse central and peripheral
RT   nervous systems.";
RL   Brain Res. 661:196-206(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 130-165.
RC   STRAIN=CBA; TISSUE=Bone marrow;
RX   MEDLINE=93185941; PubMed=8444355; DOI=10.1016/0378-1119(93)90411-U;
RA   Ershler M.A., Nagorskaya T.V., Visser J.W.M., Belyavsky A.V.;
RT   "Novel CDC2-related protein kinases produced in murine hematopoietic
RT   stem cells.";
RL   Gene 124:305-306(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE OF 1-12.
RX   MEDLINE=96039276; PubMed=7490100; DOI=10.1006/geno.1995.1194;
RA   Ohshima T., Nagle J.W., Pant H.C., Joshi J.B., Kozak C.A., Brady R.O.,
RA   Kulkarni A.B.;
RT   "Molecular cloning and chromosomal mapping of the mouse cyclin-
RT   dependent kinase 5 gene.";
RL   Genomics 28:585-588(1995).
RN   [5]
RP   IDENTIFICATION IN A TRIMOLECULAR COMPLEX WITH CABLES1 AND ABL1,
RP   INTERACTION WITH CABLES1, PHOSPHORYLATION AT TYR-15, AND MUTAGENESIS
RP   OF TYR-15.
RX   MEDLINE=20353055; PubMed=10896159; DOI=10.1016/S0896-6273(00)81200-3;
RA   Zukerberg L.R., Patrick G.N., Nikolic M., Humbert S., Wu C.-L.,
RA   Lanier L.M., Gertler F.B., Vidal M., Van Etten R.A., Tsai L.-H.;
RT   "Cables links Cdk5 and c-Abl and facilitates Cdk5 tyrosine
RT   phosphorylation, kinase upregulation, and neurite outgrowth.";
RL   Neuron 26:633-646(2000).
CC   -!- FUNCTION: Probably involved in the control of the cell cycle.
CC       Interacts with D1 and D3-type G1 cyclins. Can phosphorylate
CC       histone H1, tau, MAP2 and NF-H and NF-M. Also interacts with p35
CC       which activates the kinase.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts with AATK (By similarity). Heterodimer of a
CC       catalytic subunit and a regulatory subunit (p35). Found in a
CC       trimolecular complex with CABLES1 and ABL1. Interacts with
CC       CABLES1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell projection, growth cone.
CC       Cell projection, lamellipodium. Note=In axonal growth cone with
CC       extension to the peripheral lamellipodia.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in post-mitotic
CC       neurons.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. CDC2/CDKX subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; D29678; BAA06148.1; -; mRNA.
DR   EMBL; BC052007; AAH52007.1; -; mRNA.
DR   EMBL; X64604; CAA45888.1; -; mRNA.
DR   EMBL; S80121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00309262; -.
DR   PIR; I49592; I49592.
DR   RefSeq; NP_031694.1; NM_007668.3.
DR   UniGene; Mm.298798; -.
DR   ProteinModelPortal; P49615; -.
DR   SMR; P49615; 1-292.
DR   DIP; DIP-29353N; -.
DR   MINT; MINT-4090424; -.
DR   STRING; P49615; -.
DR   PhosphoSite; P49615; -.
DR   PRIDE; P49615; -.
DR   Ensembl; ENSMUST00000030814; ENSMUSP00000030814; ENSMUSG00000028969.
DR   GeneID; 12568; -.
DR   KEGG; mmu:12568; -.
DR   UCSC; uc008wrl.1; mouse.
DR   CTD; 12568; -.
DR   MGI; MGI:101765; Cdk5.
DR   eggNOG; roNOG09600; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG014652; -.
DR   InParanoid; P49615; -.
DR   OMA; FEYCDQD; -.
DR   OrthoDB; EOG4X6C8R; -.
DR   PhylomeDB; P49615; -.
DR   BRENDA; 2.7.11.22; 244.
DR   NextBio; 281666; -.
DR   ArrayExpress; P49615; -.
DR   Bgee; P49615; -.
DR   CleanEx; MM_CDK5; -.
DR   Genevestigator; P49615; -.
DR   GermOnline; ENSMUSG00000028969; Mus musculus.
DR   GO; GO:0030424; C:axon; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0030175; C:filopodium; IDA:MGI.
DR   GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0031594; C:neuromuscular junction; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR   GO; GO:0030549; F:acetylcholine receptor activator activity; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004693; F:cyclin-dependent protein kinase activity; IEA:EC.
DR   GO; GO:0005176; F:ErbB-2 class receptor binding; IDA:UniProtKB.
DR   GO; GO:0043125; F:ErbB-3 class receptor binding; IDA:UniProtKB.
DR   GO; GO:0002039; F:p53 binding; IPI:MGI.
DR   GO; GO:0050321; F:tau-protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0048148; P:behavioral response to cocaine; IMP:MGI.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007160; P:cell-matrix adhesion; IDA:MGI.
DR   GO; GO:0021954; P:central nervous system neuron development; IMP:MGI.
DR   GO; GO:0021697; P:cerebellar cortex formation; IMP:MGI.
DR   GO; GO:0022038; P:corpus callosum development; IMP:MGI.
DR   GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
DR   GO; GO:0009790; P:embryo development; ISS:UniProtKB.
DR   GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; IMP:MGI.
DR   GO; GO:0021819; P:layer formation in cerebral cortex; IMP:MGI.
DR   GO; GO:0008045; P:motor axon guidance; IMP:MGI.
DR   GO; GO:0045786; P:negative regulation of cell cycle; IMP:MGI.
DR   GO; GO:0046826; P:negative regulation of protein export from nucleus; IMP:MGI.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:MGI.
DR   GO; GO:0031914; P:negative regulation of synaptic plasticity; IMP:MGI.
DR   GO; GO:0051402; P:neuron apoptosis; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IDA:MGI.
DR   GO; GO:0043525; P:positive regulation of neuron apoptosis; ISS:UniProtKB.
DR   GO; GO:0045860; P:positive regulation of protein kinase activity; IMP:MGI.
DR   GO; GO:0032801; P:receptor catabolic process; IMP:MGI.
DR   GO; GO:0043113; P:receptor clustering; IMP:MGI.
DR   GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
DR   GO; GO:0060079; P:regulation of excitatory postsynaptic membrane potential; IMP:MGI.
DR   GO; GO:0014044; P:Schwann cell development; IMP:MGI.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR   GO; GO:0033136; P:serine phosphorylation of STAT3 protein; IDA:MGI.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IDA:MGI.
DR   GO; GO:0001963; P:synaptic transmission, dopaminergic; IMP:MGI.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cell cycle; Cell division; Cell projection;
KW   Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    292       Cyclin-dependent kinase 5.
FT                                /FTId=PRO_0000085785.
FT   DOMAIN        4    286       Protein kinase.
FT   NP_BIND      10     18       ATP (By similarity).
FT   ACT_SITE    126    126       Proton acceptor (By similarity).
FT   BINDING      33     33       ATP (By similarity).
FT   MOD_RES      14     14       Phosphothreonine (By similarity).
FT   MOD_RES      15     15       Phosphotyrosine; by ABL1.
FT   MOD_RES      17     17       Phosphothreonine (By similarity).
FT   MOD_RES      46     46       Phosphoserine (By similarity).
FT   MOD_RES      56     56       N6-acetyllysine (By similarity).
FT   MOD_RES      72     72       Phosphoserine (By similarity).
FT   MOD_RES     159    159       Phosphoserine (By similarity).
FT   MOD_RES     239    239       Phosphotyrosine (By similarity).
FT   MUTAGEN      15     15       Y->F: Loss of thyrosine phosphorylations
FT                                by CABLES1 and ABL1; decreased activity.
SQ   SEQUENCE   292 AA;  33288 MW;  4CB11CED9017D535 CRC64;
     MQKYEKLEKI GEGTYGTVFK AKNRETHEIV ALKRVRLDDD DEGVPSSALR EICLLKELKH
     KNIVRLHDVL HSDKKLTLVF EFCDQDLKKY FDSCNGDLDP EIVKSFLFQL LKGLGFCHSR
     NVLHRDLKPQ NLLINRNGEL KLADFGLARA FGIPVRCYSA EVVTLWYRPP DVLFGAKLYS
     TSIDMWSAGC IFAELANAGR PLFPGNDVDD QLKRIFRLLG TPTEEQWPAM TKLPDYKPYP
     MYPATTSLVN VVPKLNATGR DLLQNLLKCN PVQRISAEEA LQHPYFSDFC PP
//
ID   PSN1_MOUSE              Reviewed;         467 AA.
AC   P49769; Q91WK6; Q9JLP9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAR-2011, entry version 114.
DE   RecName: Full=Presenilin-1;
DE            Short=PS-1;
DE            EC=3.4.23.-;
DE   AltName: Full=Protein S182;
DE   Contains:
DE     RecName: Full=Presenilin-1 NTF subunit;
DE   Contains:
DE     RecName: Full=Presenilin-1 CTF subunit;
DE   Contains:
DE     RecName: Full=Presenilin-1 CTF12;
DE              Short=PS1-CTF12;
GN   Name=Psen1; Synonyms=Ad3h, Psnl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=95319502; PubMed=7596406; DOI=10.1038/375754a0;
RA   Sherrington R., Rogaev E.I., Liang Y., Rogaeva E.A., Levesque G.,
RA   Ikeda M., Chi H., Lin C., Li G., Holman K., Tsuda T., Mar L.,
RA   Foncin J.-F., Bruni A.C., Montesi M.P., Sorbi S., Rainero I.,
RA   Pinessi L., Nee L., Chumakov I., Pollen D., Brookes A., Sanseau P.,
RA   Polinsky R.J., Wasco W., da Silva H.A.R., Haines J.L.,
RA   Pericak-Vance M.A., Tanzi R.E., Roses A.D., Fraser P.E., Rommens J.M.,
RA   St George-Hyslop P.H.;
RT   "Cloning of a gene bearing missense mutations in early-onset familial
RT   Alzheimer's disease.";
RL   Nature 375:754-760(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC   STRAIN=129/SvJ;
RX   MEDLINE=97442406; PubMed=9295283; DOI=10.1074/jbc.272.38.23489;
RA   Mitsuda N., Roses A.D., Vitek M.P.;
RT   "Transcriptional regulation of the mouse presenilin-1 gene.";
RL   J. Biol. Chem. 272:23489-23497(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=SAM P8; TISSUE=Hippocampus;
RA   Kumar V.B., Vyas K.C., Choudhary V., Franko M., Flood J.F.,
RA   Morley J.E.;
RT   "Molecular cloning and tissue distribution of presenilin-1 in
RT   senenscence accelerated mice (SAM P8) mice.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=FVB/N; TISSUE=Eye, Liver, Mammary gland, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH DOCK3.
RC   TISSUE=Brain;
RX   MEDLINE=20312861; PubMed=10854253;
RX   DOI=10.1046/j.1471-4159.2000.0750109.x;
RA   Kashiwa A., Yoshida H., Lee S., Paladino T., Liu Y., Chen Q.,
RA   Dargusch R., Schubert D., Kimura H.;
RT   "Isolation and characterization of novel presenilin binding protein.";
RL   J. Neurochem. 75:109-116(2000).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-370, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; THR-370 AND
RP   SER-371, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365; SER-367; THR-370
RP   AND SER-371, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Probable catalytic subunit of the gamma-secretase
CC       complex, an endoprotease complex that catalyzes the intramembrane
CC       cleavage of integral membrane proteins such as Notch receptors and
CC       APP (beta-amyloid precursor protein). Requires the other members
CC       of the gamma-secretase complex to have a protease activity. May
CC       play a role in intracellular signaling and gene expression or in
CC       linking chromatin to the nuclear membrane. Stimulates cell-cell
CC       adhesion though its association with the E-cadherin/catenin
CC       complex. Under conditions of apoptosis or calcium influx, cleaves
CC       E-cadherin promoting the disassembly of the E-cadherin/catenin
CC       complex and increasing the pool of cytoplasmic beta-catenin, thus
CC       negatively regulating Wnt signaling. May also play a role in
CC       hematopoiesis (By similarity).
CC   -!- SUBUNIT: Homodimer. Component of the gamma-secretase complex, a
CC       complex composed of a presenilin homodimer (PSEN1 or PSEN2),
CC       nicastrin (NCSTN), APH1 (APH1A or APH1B) and PEN2. Such minimal
CC       complex is sufficient for secretase activity. Other components
CC       which are associated with the complex include SLC25A64, SLC5A7,
CC       PHB and PSEN1 isoform 3. Predominantly heterodimer of a N-terminal
CC       (NTF) and a C-terminal (CTF) endoproteolytical fragment.
CC       Associates with proteolytic processed C-terminal fragments C83 and
CC       C99 of the amyloid precursor protein (APP). Associates with
CC       NOTCH1. Associates with cadherin/catenin adhesion complexes
CC       through direct binding to CDH1 or CDH2. Interaction with CDH1
CC       stabilizes the complex and stimulates cell-cell aggregation.
CC       Interaction with CDH2 is essential for trafficking of CDH2 from
CC       the endoplasmic reticulum to the plasma membrane. Interacts with
CC       CTNND2, CTNNB1, HERPUD1, FLNA, FLNB, MTCH1, PKP4 and PARL.
CC       Interacts through its N-terminus with isoform 3 of GFAP. Interacts
CC       with DOCK3 (By similarity).
CC   -!- INTERACTION:
CC       Q9Z1G4:Atp6v0a1; NbExp=1; IntAct=EBI-990067, EBI-771149;
CC       Q02248:Ctnnb1; NbExp=1; IntAct=EBI-990067, EBI-397872;
CC       P14923:JUP (xeno); NbExp=1; IntAct=EBI-990067, EBI-702484;
CC       Q9R0Q3:Tmed2; NbExp=1; IntAct=EBI-990067, EBI-998894;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein. Golgi apparatus membrane; Multi-pass membrane
CC       protein. Cell surface (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P49769-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P49769-2; Sequence=VSP_008381, VSP_008382;
CC         Note=Due to intron retention. No experimental confirmation
CC         available;
CC   -!- DOMAIN: The PAL motif is required for normal active site
CC       conformation (By similarity).
CC   -!- PTM: Heterogeneous proteolytic processing generates N-terminal
CC       (NTF) and C-terminal (CTF) fragments of approximately 35 and 20
CC       kDa, respectively. During apoptosis, the C-terminal fragment (CTF)
CC       is further cleaved by caspase-3 to produce the fragment, PS1-CTF12
CC       (By similarity).
CC   -!- PTM: After endoproteolysis, the C-terminal fragment (CTF) is
CC       phosphorylated on serine residues by PKA and/or PKC.
CC       Phosphorylation on Ser-346 inhibits endoproteolysis (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the peptidase A22A family.
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DR   EMBL; L42177; AAC42094.1; -; mRNA.
DR   EMBL; AF007560; AAB72049.1; -; Genomic_DNA.
DR   EMBL; AF149111; AAF73153.1; -; mRNA.
DR   EMBL; BC014744; AAH14744.1; -; mRNA.
DR   EMBL; BC030409; AAH30409.1; -; mRNA.
DR   EMBL; BC071233; AAH71233.1; -; mRNA.
DR   IPI; IPI00117124; -.
DR   IPI; IPI00352799; -.
DR   PIR; I78388; I78388.
DR   RefSeq; NP_032969.1; NM_008943.2.
DR   UniGene; Mm.998; -.
DR   ProteinModelPortal; P49769; -.
DR   IntAct; P49769; 10.
DR   MINT; MINT-193580; -.
DR   STRING; P49769; -.
DR   MEROPS; A22.001; -.
DR   PhosphoSite; P49769; -.
DR   PRIDE; P49769; -.
DR   Ensembl; ENSMUST00000041806; ENSMUSP00000048363; ENSMUSG00000019969.
DR   Ensembl; ENSMUST00000101225; ENSMUSP00000098786; ENSMUSG00000019969.
DR   GeneID; 19164; -.
DR   KEGG; mmu:19164; -.
DR   UCSC; uc007odo.1; mouse.
DR   UCSC; uc007odp.1; mouse.
DR   CTD; 19164; -.
DR   MGI; MGI:1202717; Psen1.
DR   eggNOG; roNOG12441; -.
DR   HOGENOM; HBG559840; -.
DR   HOVERGEN; HBG011375; -.
DR   InParanoid; P49769; -.
DR   OMA; KNSNYNA; -.
DR   OrthoDB; EOG4TF0KN; -.
DR   PhylomeDB; P49769; -.
DR   NextBio; 295822; -.
DR   ArrayExpress; P49769; -.
DR   Bgee; P49769; -.
DR   CleanEx; MM_PSEN1; -.
DR   Genevestigator; P49769; -.
DR   GermOnline; ENSMUSG00000019969; Mus musculus.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0035253; C:ciliary rootlet; IDA:MGI.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR   GO; GO:0043198; C:dendritic shaft; IDA:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030426; C:growth cone; IDA:MGI.
DR   GO; GO:0005887; C:integral to plasma membrane; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0045296; F:cadherin binding; IPI:MGI.
DR   GO; GO:0004175; F:endopeptidase activity; IMP:MGI.
DR   GO; GO:0000186; P:activation of MAPKK activity; IMP:MGI.
DR   GO; GO:0042987; P:amyloid precursor protein catabolic process; IMP:MGI.
DR   GO; GO:0042640; P:anagen; IGI:MGI.
DR   GO; GO:0006916; P:anti-apoptosis; IDA:MGI.
DR   GO; GO:0000045; P:autophagic vacuole assembly; IMP:MGI.
DR   GO; GO:0050435; P:beta-amyloid metabolic process; IMP:MGI.
DR   GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR   GO; GO:0048854; P:brain morphogenesis; IGI:MGI.
DR   GO; GO:0021870; P:Cajal-Retzius cell differentiation; IMP:MGI.
DR   GO; GO:0001708; P:cell fate specification; IGI:MGI.
DR   GO; GO:0021795; P:cerebral cortex cell migration; IMP:MGI.
DR   GO; GO:0015871; P:choline transport; IMP:MGI.
DR   GO; GO:0021904; P:dorsal/ventral neural tube patterning; IGI:MGI.
DR   GO; GO:0030326; P:embryonic limb morphogenesis; IGI:MGI.
DR   GO; GO:0050673; P:epithelial cell proliferation; IGI:MGI.
DR   GO; GO:0001947; P:heart looping; IGI:MGI.
DR   GO; GO:0002244; P:hemopoietic progenitor cell differentiation; IGI:MGI.
DR   GO; GO:0015813; P:L-glutamate transport; IMP:MGI.
DR   GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISS:UniProtKB.
DR   GO; GO:0007613; P:memory; IMP:MGI.
DR   GO; GO:0006839; P:mitochondrial transport; IMP:MGI.
DR   GO; GO:0002573; P:myeloid leukocyte differentiation; IGI:MGI.
DR   GO; GO:0050771; P:negative regulation of axonogenesis; IMP:MGI.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:MGI.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IGI:MGI.
DR   GO; GO:0051402; P:neuron apoptosis; IGI:MGI.
DR   GO; GO:0048666; P:neuron development; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0007220; P:Notch receptor processing; IMP:MGI.
DR   GO; GO:0007219; P:Notch signaling pathway; IMP:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptosis; IGI:MGI.
DR   GO; GO:0050820; P:positive regulation of coagulation; IMP:MGI.
DR   GO; GO:0043406; P:positive regulation of MAP kinase activity; IMP:MGI.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0006486; P:protein glycosylation; IMP:MGI.
DR   GO; GO:0051605; P:protein maturation by peptide bond cleavage; IMP:MGI.
DR   GO; GO:0015031; P:protein transport; IGI:MGI.
DR   GO; GO:0007176; P:regulation of epidermal growth factor receptor activity; IGI:MGI.
DR   GO; GO:0043393; P:regulation of protein binding; IGI:MGI.
DR   GO; GO:0060075; P:regulation of resting membrane potential; IMP:MGI.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR   GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:MGI.
DR   GO; GO:0006974; P:response to DNA damage stimulus; IMP:MGI.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
DR   GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR   GO; GO:0051563; P:smooth endoplasmic reticulum calcium ion homeostasis; IGI:MGI.
DR   GO; GO:0001756; P:somitogenesis; IMP:MGI.
DR   GO; GO:0016080; P:synaptic vesicle targeting; IMP:MGI.
DR   GO; GO:0002286; P:T cell activation involved in immune response; IGI:MGI.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IGI:MGI.
DR   GO; GO:0048538; P:thymus development; IGI:MGI.
DR   InterPro; IPR002031; Pept_A22A_PS1.
DR   InterPro; IPR006639; Peptidase_A22.
DR   InterPro; IPR001108; Peptidase_A22A.
DR   PANTHER; PTHR10202:SF7; Pept_A22A_PS1; 1.
DR   PANTHER; PTHR10202; Peptidase_A22A; 1.
DR   Pfam; PF01080; Presenilin; 1.
DR   PRINTS; PR01072; PRESENILIN.
DR   PRINTS; PR01073; PRESENILIN1.
DR   SMART; SM00730; PSN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Cell adhesion; Endoplasmic reticulum;
KW   Golgi apparatus; Hydrolase; Membrane; Notch signaling pathway;
KW   Phosphoprotein; Protease; Transmembrane; Transmembrane helix.
FT   CHAIN         1    298       Presenilin-1 NTF subunit (By similarity).
FT                                /FTId=PRO_0000025597.
FT   CHAIN       299    467       Presenilin-1 CTF subunit (By similarity).
FT                                /FTId=PRO_0000025598.
FT   CHAIN       346    467       Presenilin-1 CTF12 (By similarity).
FT                                /FTId=PRO_0000236058.
FT   TOPO_DOM      1     82       Cytoplasmic (Potential).
FT   TRANSMEM     83    103       Helical; (Potential).
FT   TOPO_DOM    104    132       Lumenal (Potential).
FT   TRANSMEM    133    153       Helical; (Potential).
FT   TOPO_DOM    154    160       Cytoplasmic (Potential).
FT   TRANSMEM    161    181       Helical; (Potential).
FT   TOPO_DOM    182    194       Lumenal (Potential).
FT   TRANSMEM    195    215       Helical; (Potential).
FT   TOPO_DOM    216    220       Cytoplasmic (Potential).
FT   TRANSMEM    221    241       Helical; (Potential).
FT   TOPO_DOM    242    243       Lumenal (Potential).
FT   TRANSMEM    244    264       Helical; (Potential).
FT   TOPO_DOM    265    407       Cytoplasmic (Potential).
FT   TRANSMEM    408    428       Helical; (Potential).
FT   TRANSMEM    433    453       Helical; (Potential).
FT   REGION      322    450       Required for interaction with CTNNB1 (By
FT                                similarity).
FT   REGION      372    399       Required for interaction with CTNND2 (By
FT                                similarity).
FT   REGION      464    467       Interaction with MTCH1 (By similarity).
FT   MOTIF       433    435       PAL.
FT   ACT_SITE    257    257       By similarity.
FT   ACT_SITE    385    385       By similarity.
FT   SITE        291    292       Cleavage; alternate (By similarity).
FT   SITE        292    293       Cleavage; alternate (By similarity).
FT   SITE        298    299       Cleavage (By similarity).
FT   SITE        345    346       Cleavage; by caspase (By similarity).
FT   MOD_RES     346    346       Phosphoserine; by PKC (By similarity).
FT   MOD_RES     365    365       Phosphoserine.
FT   MOD_RES     367    367       Phosphoserine.
FT   MOD_RES     370    370       Phosphothreonine.
FT   MOD_RES     371    371       Phosphoserine.
FT   VAR_SEQ     257    261       DLVAV -> GKAQD (in isoform 2).
FT                                /FTId=VSP_008381.
FT   VAR_SEQ     262    467       Missing (in isoform 2).
FT                                /FTId=VSP_008382.
FT   VARIANT       9      9       S -> T (in strain: SAM P8).
FT   VARIANT      40     40       D -> E (in strain: SAM P8).
FT   VARIANT      67     67       E -> CM (in strain: SAM P8).
FT   VARIANT     196    196       V -> L (in strain: SAM P8).
FT   VARIANT     321    322       ER -> RRD (in strain: SAM P8).
SQ   SEQUENCE   467 AA;  52640 MW;  D07215B4BAD2D549 CRC64;
     MTEIPAPLSY FQNAQMSEDS HSSSAIRSQN DSQERQQQHD RQRLDNPEPI SNGRPQSNSR
     QVVEQDEEED EELTLKYGAK HVIMLFVPVT LCMVVVVATI KSVSFYTRKD GQLIYTPFTE
     DTETVGQRAL HSILNAAIMI SVIVIMTILL VVLYKYRCYK VIHAWLIISS LLLLFFFSFI
     YLGEVFKTYN VAVDYVTVAL LIWNFGVVGM IAIHWKGPLR LQQAYLIMIS ALMALVFIKY
     LPEWTAWLIL AVISVYDLVA VLCPKGPLRM LVETAQERNE TLFPALIYSS TMVWLVNMAE
     GDPEAQRRVP KNPKYNTQRA ERETQDSGSG NDDGGFSEEW EAQRDSHLGP HRSTPESRAA
     VQELSGSILT SEDPEERGVK LGLGDFIFYS VLVGKASATA SGDWNTTIAC FVAILIGLCL
     TLLLLAIFKK ALPALPISIT FGLVFYFATD YLVQPFMDQL AFHQFYI
//
ID   ODBA_MOUSE              Reviewed;         442 AA.
AC   P50136;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial;
DE            EC=1.2.4.4;
DE   AltName: Full=Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain;
DE            Short=BCKDE1A;
DE            Short=BCKDH E1-alpha;
DE   Flags: Precursor;
GN   Name=Bckdha;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   MEDLINE=96358490; PubMed=8761456;
RA   Costeas P.A., Chinsky J.M.;
RT   "Effects of insulin on the regulation of branched-chain alpha-keto
RT   acid dehydrogenase E1 alpha subunit gene expression.";
RL   Biochem. J. 318:85-92(1996).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: The branched-chain alpha-keto dehydrogenase complex
CC       catalyzes the overall conversion of alpha-keto acids to acyl-CoA
CC       and CO(2). It contains multiple copies of three enzymatic
CC       components: branched-chain alpha-keto acid decarboxylase (E1),
CC       lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
CC   -!- CATALYTIC ACTIVITY: 3-methyl-2-oxobutanoate +
CC       [dihydrolipoyllysine-residue (2-methylpropanoyl)transferase]
CC       lipoyllysine = [dihydrolipoyllysine-residue (2-
CC       methylpropanoyl)transferase] S-(2-
CC       methylpropanoyl)dihydrolipoyllysine + CO(2).
CC   -!- COFACTOR: Thiamine pyrophosphate.
CC   -!- SUBUNIT: Heterotetramer of alpha and beta chains (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- MISCELLANEOUS: Bound potassium ions stabilize the protein
CC       structure (By similarity).
CC   -!- SIMILARITY: Belongs to the BCKDHA family.
CC   -----------------------------------------------------------------------
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DR   EMBL; L47335; AAB38422.1; -; mRNA.
DR   IPI; IPI00331555; -.
DR   PIR; S71881; S71881.
DR   UniGene; Mm.25848; -.
DR   ProteinModelPortal; P50136; -.
DR   SMR; P50136; 48-442.
DR   STRING; P50136; -.
DR   SWISS-2DPAGE; P50136; -.
DR   PRIDE; P50136; -.
DR   Ensembl; ENSMUST00000071329; ENSMUSP00000071292; ENSMUSG00000060376.
DR   MGI; MGI:107701; Bckdha.
DR   eggNOG; roNOG08618; -.
DR   HOVERGEN; HBG002459; -.
DR   InParanoid; P50136; -.
DR   OrthoDB; EOG4RR6JR; -.
DR   BRENDA; 1.2.4.4; 244.
DR   ArrayExpress; P50136; -.
DR   Bgee; P50136; -.
DR   Genevestigator; P50136; -.
DR   GermOnline; ENSMUSG00000060376; Mus musculus.
DR   GO; GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; ISS:HGNC.
DR   GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:EC.
DR   GO; GO:0003826; F:alpha-ketoacid dehydrogenase activity; ISS:HGNC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009083; P:branched chain family amino acid catabolic process; ISS:HGNC.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR001017; DH_E1.
DR   Pfam; PF00676; E1_dh; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Mitochondrion; Oxidoreductase; Phosphoprotein;
KW   Potassium; Thiamine pyrophosphate; Transit peptide.
FT   TRANSIT       1     42       Mitochondrion (By similarity).
FT   CHAIN        43    442       2-oxoisovalerate dehydrogenase subunit
FT                                alpha, mitochondrial.
FT                                /FTId=PRO_0000020467.
FT   REGION      154    156       Thiamine pyrophosphate binding (By
FT                                similarity).
FT   METAL       203    203       Potassium (By similarity).
FT   METAL       208    208       Potassium (By similarity).
FT   METAL       209    209       Potassium (By similarity).
FT   MOD_RES     334    334       Phosphoserine.
FT   MOD_RES     342    342       Phosphotyrosine (By similarity).
FT   MOD_RES     344    344       Phosphoserine.
SQ   SEQUENCE   442 AA;  50371 MW;  3388213D88BC7C92 CRC64;
     MSAAKIWRPS RGLRQAALLL LGRSGVRGLA RSHPSRQQQQ QFPSLDDKPQ FPGASAEFVD
     KLEFIQPNVI SGIPIYRVMD RQGQIINPSE DPHLPQEEVL KFYRSMTLLN TMDRILYESQ
     REGRISFYMT NYGEEGTHVG SAAALERTDL VFGQYREAGV LMYRDYPLEL FMSQCYGNVN
     DPGKGRQMPV HYGCKERHFV TISSPLATQI PQAVGAAYAA KRANANRIVI CYFGEGAASE
     GDAHAGFNFA ATLECPIIFF CRNNGYAIST PTSEQYRGDG IAARGPGYGI KSIRVDGNDV
     FAVYNATKEA RRRAVAENQP FLIEAMTYRI GHHSTSDDSS AYRSVDEVNY WDKQDHPISR
     LRQYLLNQGW WDEEQEKAWR KQSRKKVMEA FEQAERKLKP NPSLLFSDVY QEMPAQLRRQ
     QESLARHLQT YGEHYPLDHF EK
//
ID   GNAT2_MOUSE             Reviewed;         354 AA.
AC   P50149;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=Guanine nucleotide-binding protein G(t) subunit alpha-2;
DE   AltName: Full=Transducin alpha-2 chain;
GN   Name=Gnat2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Retina;
RX   MEDLINE=94283273; PubMed=8013366; DOI=10.1210/en.135.1.31;
RA   Zigman J.M., Westermark G.T., LaMendola J., Steiner D.F.;
RT   "Expression of cone transducin, Gz alpha, and other G-protein alpha-
RT   subunit messenger ribonucleic acids in pancreatic islets.";
RL   Endocrinology 135:31-37(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC       involved as modulators or transducers in various transmembrane
CC       signaling systems. Transducin is an amplifier and one of the
CC       transducers of a visual impulse that performs the coupling between
CC       rhodopsin and cGMP-phosphodiesterase.
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and
CC       gamma. The alpha chain contains the guanine nucleotide binding
CC       site.
CC   -!- TISSUE SPECIFICITY: Retinal rod outer segment.
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; L10666; AAC37650.1; -; mRNA.
DR   EMBL; BC016272; AAH16272.1; -; mRNA.
DR   IPI; IPI00228620; -.
DR   RefSeq; NP_032167.1; NM_008141.2.
DR   UniGene; Mm.439652; -.
DR   ProteinModelPortal; P50149; -.
DR   SMR; P50149; 31-348.
DR   STRING; P50149; -.
DR   PRIDE; P50149; -.
DR   Ensembl; ENSMUST00000058669; ENSMUSP00000053818; ENSMUSG00000009108.
DR   GeneID; 14686; -.
DR   KEGG; mmu:14686; -.
DR   UCSC; uc008qyc.1; mouse.
DR   CTD; 14686; -.
DR   MGI; MGI:95779; Gnat2.
DR   HOGENOM; HBG444960; -.
DR   HOVERGEN; HBG063184; -.
DR   InParanoid; P50149; -.
DR   OMA; EVIRKLW; -.
DR   OrthoDB; EOG47D9GD; -.
DR   PhylomeDB; P50149; -.
DR   NextBio; 286623; -.
DR   ArrayExpress; P50149; -.
DR   Bgee; P50149; -.
DR   Genevestigator; P50149; -.
DR   GermOnline; ENSMUSG00000009108; Mus musculus.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; TAS:MGI.
DR   GO; GO:0005624; C:membrane fraction; TAS:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; TAS:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0050908; P:detection of light stimulus involved in visual perception; IMP:MGI.
DR   GO; GO:0007199; P:G-protein signaling, coupled to cGMP nucleotide second messenger; TAS:MGI.
DR   GO; GO:0007602; P:phototransduction; IMP:MGI.
DR   GO; GO:0046549; P:retinal cone cell development; IMP:MGI.
DR   InterPro; IPR001408; Gprotein_alpha_I.
DR   InterPro; IPR001019; Gprotein_alpha_su.
DR   InterPro; IPR011025; GproteinA_insert.
DR   Gene3D; G3DSA:1.10.400.10; GproteinA_insert; 1.
DR   PANTHER; PTHR10218; Gprotein_alph_bd; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00441; GPROTEINAI.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF47895; Transducn_insert; 1.
PE   2: Evidence at transcript level;
KW   GTP-binding; Lipoprotein; Myristate; Nucleotide-binding;
KW   Sensory transduction; Transducer; Vision.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    354       Guanine nucleotide-binding protein G(t)
FT                                subunit alpha-2.
FT                                /FTId=PRO_0000203741.
FT   NP_BIND      40     47       GTP (By similarity).
FT   NP_BIND     200    204       GTP (By similarity).
FT   NP_BIND     269    272       GTP (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
SQ   SEQUENCE   354 AA;  40118 MW;  6A14B9B152F14F4E CRC64;
     MGSGISAEDK ELARRSKELE KKLQEDADKE AKTVKLLLLG AGESGKSTIV KQMKIIHQDG
     YSPEECLEFK SVIYGNVLQS ILAIIRAMST LGIDYAEPSC ADAGRQLNNL ADSTEEGTMP
     PELVDVIRKL WKDGGVQACF DRAAEFQLND SASYYLNQLD RITDPNYLPN EQDVLRSRVK
     TTGIIETKFS VKDLNFRMFD VGGQRSERKK WIHCFEGVTC IIFCAALSAY DMVLVEDDEV
     NRMHESLHLF NSICNHKFFA ATSIVLFLNK KDLFEEKIKK VHLSICFPEY DGNNSYEDAG
     NYIKSQFLDL NMRKDVKEIY SHMTCATDTQ NVKFVFDAVT DIIIKENLKD CGLF
//
ID   GBG4_MOUSE              Reviewed;          75 AA.
AC   P50153;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-4;
DE   Flags: Precursor;
GN   Name=Gng4; Synonyms=Gngt4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=96067541; PubMed=7488078; DOI=10.1006/bbrc.1995.2600;
RA   Kalyanaraman S., Kalyanaraman V., Gautam N.;
RT   "A brain-specific G protein gamma subunit.";
RL   Biochem. Biophys. Res. Commun. 216:126-132(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=98234556; PubMed=9570961; DOI=10.1006/geno.1998.5223;
RA   Kalyanaraman S., Copeland N.G., Gilbert D.G., Jenkins N.A., Gautam N.;
RT   "Structure and chromosomal localization of mouse G protein subunit
RT   gamma4 gene.";
RL   Genomics 49:147-151(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC       involved as a modulator or transducer in various transmembrane
CC       signaling systems. The beta and gamma chains are required for the
CC       GTPase activity, for replacement of GDP by GTP, and for G protein-
CC       effector interaction.
CC   -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and
CC       gamma. Interacts with beta-1 and beta-2, but not with beta-3 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- TISSUE SPECIFICITY: Brain.
CC   -!- SIMILARITY: Belongs to the G protein gamma family.
CC   -----------------------------------------------------------------------
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DR   EMBL; U37527; AAB93460.1; -; mRNA.
DR   EMBL; AF038594; AAC40090.1; -; Genomic_DNA.
DR   EMBL; AF038593; AAC40090.1; JOINED; Genomic_DNA.
DR   EMBL; BC016506; AAH16506.1; -; mRNA.
DR   IPI; IPI00115544; -.
DR   PIR; JC4339; JC4339.
DR   RefSeq; NP_034447.1; NM_010317.2.
DR   UniGene; Mm.215394; -.
DR   ProteinModelPortal; P50153; -.
DR   SMR; P50153; 12-71.
DR   DIP; DIP-494N; -.
DR   STRING; P50153; -.
DR   PRIDE; P50153; -.
DR   Ensembl; ENSMUST00000021734; ENSMUSP00000021734; ENSMUSG00000021303.
DR   GeneID; 14706; -.
DR   KEGG; mmu:14706; -.
DR   UCSC; uc007pml.1; mouse.
DR   CTD; 14706; -.
DR   MGI; MGI:102703; Gng4.
DR   eggNOG; roNOG17053; -.
DR   HOGENOM; HBG444905; -.
DR   HOVERGEN; HBG014983; -.
DR   InParanoid; P50153; -.
DR   OMA; KEGMSSN; -.
DR   OrthoDB; EOG47WNQC; -.
DR   PhylomeDB; P50153; -.
DR   NextBio; 286687; -.
DR   ArrayExpress; P50153; -.
DR   Bgee; P50153; -.
DR   Genevestigator; P50153; -.
DR   GermOnline; ENSMUSG00000021303; Mus musculus.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; IEA:InterPro.
DR   InterPro; IPR015898; G-protein_gamma_dom.
DR   InterPro; IPR001770; Gprotein-gamma.
DR   Gene3D; G3DSA:4.10.260.10; G-protein_gamma_dom; 1.
DR   PANTHER; PTHR13809; Gprotein-gamma; 1.
DR   Pfam; PF00631; G-gamma; 1.
DR   PRINTS; PR00321; GPROTEING.
DR   SMART; SM00224; GGL; 1.
DR   SUPFAM; SSF48670; G-protein_gamma-like; 1.
DR   PROSITE; PS50058; G_PROTEIN_GAMMA; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Lipoprotein; Membrane; Methylation; Prenylation;
KW   Transducer.
FT   CHAIN         1     72       Guanine nucleotide-binding protein
FT                                G(I)/G(S)/G(O) subunit gamma-4.
FT                                /FTId=PRO_0000012623.
FT   PROPEP       73     75       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000012624.
FT   MOD_RES      72     72       Cysteine methyl ester (By similarity).
FT   LIPID        72     72       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   75 AA;  8405 MW;  42FAEF47311FA195 CRC64;
     MKEGMSNNST TSISQARKAV EQLKMEACMD RVKVSQAASD LLAYCEAHVR EDPLIIPVPA
     SENPFREKKF FCTIL
//
ID   DHB8_MOUSE              Reviewed;         259 AA.
AC   P50171; Q5M9K0; Q60958; Q60959; Q9Z1W2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Estradiol 17-beta-dehydrogenase 8;
DE            EC=1.1.1.62;
DE   AltName: Full=17-beta-hydroxysteroid dehydrogenase 8;
DE            Short=17-beta-HSD 8;
DE   AltName: Full=3-oxoacyl-[acyl-carrier-protein] reductase;
DE            EC=1.1.1.-;
DE   AltName: Full=Protein Ke6;
DE            Short=Ke-6;
DE   AltName: Full=Testosterone 17-beta-dehydrogenase 8;
DE            EC=1.1.1.63;
GN   Name=Hsd17b8; Synonyms=H2-Ke6, Hke6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DBA/2J; TISSUE=Kidney;
RX   MEDLINE=93180832; PubMed=8441417;
RA   Aziz N., Maxwell M.M., St Jacques B., Brenner B.M.;
RT   "Downregulation of Ke 6, a novel gene encoded within the major
RT   histocompatibility complex, in murine polycystic kidney disease.";
RL   Mol. Cell. Biol. 13:1847-1853(1993).
RN   [2]
RP   ERRATUM.
RA   Aziz N., Maxwell M.M., St Jacques B., Brenner B.M.;
RL   Mol. Cell. Biol. 13:6614-6614(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=96027630; PubMed=7559658; DOI=10.1074/jbc.270.42.25213;
RA   Maxwell M.M., Nearing J., Aziz N.;
RT   "Ke 6 gene. Sequence and organization and aberrant regulation in
RT   murine polycystic kidney disease.";
RL   J. Biol. Chem. 270:25213-25219(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129/SvJ;
RA   Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L.,
RA   Hall J., Lasky S., Hood L.;
RT   "Sequence of the mouse major histocomaptibility locus class II
RT   region.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=9712896; DOI=10.1074/jbc.273.35.22664;
RA   Fomitcheva J., Baker M.E., Anderson E., Lee G.Y., Aziz N.;
RT   "Characterization of Ke 6, a new 17beta-hydroxysteroid dehydrogenase,
RT   and its expression in gonadal tissues.";
RL   J. Biol. Chem. 273:22664-22671(1998).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15923359; DOI=10.1369/jhc.5A6692.2005;
RA   Pelletier G., Luu-The V., Li S., Labrie F.;
RT   "Localization of type 8 17beta-hydroxysteroid dehydrogenase mRNA in
RT   mouse tissues as studied by in situ hybridization.";
RL   J. Histochem. Cytochem. 53:1257-1271(2005).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- FUNCTION: NAD-dependent 17-beta-hydroxysteroid dehydrogenase with
CC       highest activity towards estradiol. Has very low activity towards
CC       testosterone (By similarity). The heteroteramer with CBR4 has
CC       NADH-dependent 3-ketoacyl-acyl carrier protein reductase activity.
CC       May play a role in biosynthesis of fatty acids in mitochondria (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Estradiol-17-beta + NAD(P)(+) = estrone +
CC       NAD(P)H.
CC   -!- CATALYTIC ACTIVITY: Testosterone + NAD(+) = androst-4-ene-3,17-
CC       dione + NADH.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.110 uM for estradiol;
CC         KM=0.422 uM for testosterone;
CC         KM=0.368 uM for estrone;
CC         KM=0.360 uM for dihydrotestosterone;
CC         Vmax=0.405 nmol/min/mg enzyme for estradiol as substrate;
CC         Vmax=0.123 nmol/min/mg enzyme for testosterone as substrate;
CC         Vmax=0.186 nmol/min/mg enzyme for estrone as substrate;
CC         Vmax=0.081 nmol/min/mg enzyme for dihydrotestosterone as
CC         substrate;
CC   -!- PATHWAY: Steroid biosynthesis; estrogen biosynthesis.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBUNIT: Heterotetramer with CBR4; contains two molecules of
CC       HSD17B8 and CBR4 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Short;
CC         IsoId=P50171-1; Sequence=Displayed;
CC       Name=Long;
CC         IsoId=P50171-2; Sequence=VSP_006030;
CC   -!- TISSUE SPECIFICITY: Kidney, liver, testis, ovary, oviduct, uterus,
CC       mammary gland, vagina, prostate, clitoral gland and moderately in
CC       spleen, heart, dorsal skin, brain and lung.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC69902.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
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DR   EMBL; U34072; AAC53573.1; -; Genomic_DNA.
DR   EMBL; U34072; AAC53574.1; -; Genomic_DNA.
DR   EMBL; AF100956; AAC69902.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC086927; AAH86927.1; -; mRNA.
DR   IPI; IPI00115598; -.
DR   IPI; IPI00230550; -.
DR   PIR; A48154; A48154.
DR   RefSeq; NP_038571.2; NM_013543.2.
DR   UniGene; Mm.275452; -.
DR   ProteinModelPortal; P50171; -.
DR   SMR; P50171; 6-258.
DR   STRING; P50171; -.
DR   PhosphoSite; P50171; -.
DR   REPRODUCTION-2DPAGE; P50171; -.
DR   PRIDE; P50171; -.
DR   Ensembl; ENSMUST00000045467; ENSMUSP00000038069; ENSMUSG00000073422.
DR   Ensembl; ENSMUST00000114303; ENSMUSP00000109942; ENSMUSG00000073422.
DR   GeneID; 14979; -.
DR   KEGG; mmu:14979; -.
DR   CTD; 14979; -.
DR   MGI; MGI:95911; H2-Ke6.
DR   eggNOG; roNOG10889; -.
DR   GeneTree; ENSGT00600000084182; -.
DR   HOVERGEN; HBG002145; -.
DR   OrthoDB; EOG4NZTTZ; -.
DR   BRENDA; 1.1.1.62; 244.
DR   BRENDA; 1.1.1.63; 244.
DR   ArrayExpress; P50171; -.
DR   Bgee; P50171; -.
DR   CleanEx; MM_H2-KE6; -.
DR   Genevestigator; P50171; -.
DR   GermOnline; ENSMUSG00000073422; Mus musculus.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005740; C:mitochondrial envelope; IDA:MGI.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004303; F:estradiol 17-beta-dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0050327; F:testosterone 17-beta-dehydrogenase activity; IDA:MGI.
DR   GO; GO:0008209; P:androgen metabolic process; IDA:MGI.
DR   GO; GO:0006703; P:estrogen biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Fatty acid biosynthesis;
KW   Lipid synthesis; Mitochondrion; NAD; Oxidoreductase;
KW   Steroid biosynthesis.
FT   CHAIN         1    259       Estradiol 17-beta-dehydrogenase 8.
FT                                /FTId=PRO_0000054599.
FT   NP_BIND      13     21       NAD (By similarity).
FT   NP_BIND      40     41       NAD (By similarity).
FT   NP_BIND      72     74       NAD (By similarity).
FT   NP_BIND     167    171       NAD (By similarity).
FT   NP_BIND     200    202       NAD (By similarity).
FT   ACT_SITE    167    167       Proton acceptor (By similarity).
FT   BINDING     154    154       Substrate (By similarity).
FT   MOD_RES      66     66       N6-acetyllysine.
FT   VAR_SEQ     256    259       GLFM -> MRPSWGGGQENRTQVVMRK (in isoform
FT                                Long).
FT                                /FTId=VSP_006030.
FT   CONFLICT    229    229       E -> EG (in Ref. 1; AAC53573/AAC53574).
SQ   SEQUENCE   259 AA;  26588 MW;  C4704F02B63C275F CRC64;
     MASQLRLRSA LALVTGAGSG IGRAISVRLA AEGAAVAACD LDGAAAQDTV RLLGSPGSED
     GAPRGKHAAF QADVSQGPAA RRLLEEVQAC FSRPPSVVVS CAGITRDEFL LHMSEEDWDR
     VIAVNLKGTF LVTQAAAQAL VSSGGRGSII NISSIIGKVG NIGQTNYASS KAGVIGLTQT
     AARELGRHGI RCNSVLPGFI ATPMTQKMPE KVKDKVTAMI PLGHMGDPED VADVVAFLAS
     EDSGYITGAS VEVSGGLFM
//
ID   TNR3_MOUSE              Reviewed;         415 AA.
AC   P50284;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Tumor necrosis factor receptor superfamily member 3;
DE   AltName: Full=Lymphotoxin-beta receptor;
DE   Flags: Precursor;
GN   Name=Ltbr; Synonyms=Tnfcr, Tnfrsf3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CVB; TISSUE=Lung;
RX   MEDLINE=96072804; PubMed=7594541;
RA   Force W.R., Walter B.N., Hession C., Tizard R., Kozak C.A.,
RA   Browning J.L., Ware C.F.;
RT   "Mouse lymphotoxin-beta receptor. Molecular genetics, ligand binding,
RT   and expression.";
RL   J. Immunol. 155:5280-5288(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96163885; PubMed=8586432; DOI=10.1006/geno.1995.9872;
RA   Nakamura T., Tashiro K., Nazarea M., Nakano T., Sasayama S., Honjo T.;
RT   "The murine lymphotoxin-beta receptor cDNA: isolation by the signal
RT   sequence trap and chromosomal mapping.";
RL   Genomics 30:312-319(1995).
RN   [3]
RP   INTERACTION WITH TRAF5.
RC   STRAIN=BALB/c;
RX   MEDLINE=96278943; PubMed=8663299; DOI=10.1074/jbc.271.25.14661;
RA   Nakano H., Oshima H., Chung W., Williams-Abbott L., Ware C.F.,
RA   Yagita H., Okumura K.;
RT   "TRAF5, an activator of NF-kappaB and putative signal transducer for
RT   the lymphotoxin-beta receptor.";
RL   J. Biol. Chem. 271:14661-14664(1996).
CC   -!- FUNCTION: Receptor for the heterotrimeric lymphotoxin containing
CC       LTA and LTB, and for TNFS14/LIGHT. Promotes apoptosis via TRAF3
CC       and TRAF5. May play a role in the development of lymphoid organs
CC       (By similarity).
CC   -!- SUBUNIT: Self-associates (By similarity). Associates with TRAF5.
CC       Associates with TRAF3 and TRAF4 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- SIMILARITY: Contains 4 TNFR-Cys repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U29173; AAA68964.1; -; mRNA.
DR   EMBL; L38423; AAB00846.1; -; mRNA.
DR   EMBL; U30798; AAA81334.1; -; Genomic_DNA.
DR   IPI; IPI00116429; -.
DR   RefSeq; NP_034866.1; NM_010736.3.
DR   UniGene; Mm.3122; -.
DR   ProteinModelPortal; P50284; -.
DR   SMR; P50284; 41-212.
DR   IntAct; P50284; 1.
DR   STRING; P50284; -.
DR   PhosphoSite; P50284; -.
DR   PRIDE; P50284; -.
DR   Ensembl; ENSMUST00000032489; ENSMUSP00000032489; ENSMUSG00000030339.
DR   GeneID; 17000; -.
DR   KEGG; mmu:17000; -.
DR   UCSC; uc009duj.1; mouse.
DR   CTD; 17000; -.
DR   MGI; MGI:104875; Ltbr.
DR   eggNOG; roNOG06602; -.
DR   HOGENOM; HBG126624; -.
DR   HOVERGEN; HBG023187; -.
DR   InParanoid; P50284; -.
DR   OMA; TNGIHVT; -.
DR   OrthoDB; EOG41ZFC0; -.
DR   PhylomeDB; P50284; -.
DR   NextBio; 291108; -.
DR   ArrayExpress; P50284; -.
DR   Bgee; P50284; -.
DR   CleanEx; MM_LTBR; -.
DR   Genevestigator; P50284; -.
DR   GermOnline; ENSMUSG00000030339; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0048535; P:lymph node development; TAS:MGI.
DR   InterPro; IPR017349; TNFR_3_LTBR.
DR   InterPro; IPR001368; TNFR_Cys_rich_reg.
DR   Pfam; PF00020; TNFR_c6; 2.
DR   PIRSF; PIRSF037999; TNFR_3_LTBR; 1.
DR   PRINTS; PR01920; TNFACTORR3.
DR   SMART; SM00208; TNFR; 3.
DR   PROSITE; PS00652; TNFR_NGFR_1; 2.
DR   PROSITE; PS50050; TNFR_NGFR_2; 3.
PE   1: Evidence at protein level;
KW   Apoptosis; Disulfide bond; Glycoprotein; Membrane; Receptor; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     30       Potential.
FT   CHAIN        31    415       Tumor necrosis factor receptor
FT                                superfamily member 3.
FT                                /FTId=PRO_0000034553.
FT   TOPO_DOM     31    223       Extracellular (Potential).
FT   TRANSMEM    224    244       Helical; (Potential).
FT   TOPO_DOM    245    415       Cytoplasmic (Potential).
FT   REPEAT       42     81       TNFR-Cys 1.
FT   REPEAT       82    124       TNFR-Cys 2.
FT   REPEAT      125    170       TNFR-Cys 3.
FT   REPEAT      171    213       TNFR-Cys 4.
FT   CARBOHYD     40     40       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    179    179       N-linked (GlcNAc...) (Potential).
FT   DISULFID     43     58       By similarity.
FT   DISULFID     59     72       By similarity.
FT   DISULFID     62     80       By similarity.
FT   DISULFID     83     98       By similarity.
FT   DISULFID    101    116       By similarity.
FT   DISULFID    104    124       By similarity.
FT   DISULFID    126    132       By similarity.
FT   DISULFID    139    150       By similarity.
FT   DISULFID    142    169       By similarity.
FT   DISULFID    172    187       By similarity.
SQ   SEQUENCE   415 AA;  44956 MW;  29B326A566AEF661 CRC64;
     MRLPRASSPC GLAWGPLLLG LSGLLVASQP QLVPPYRIEN QTCWDQDKEY YEPMHDVCCS
     RCPPGEFVFA VCSRSQDTVC KTCPHNSYNE HWNHLSTCQL CRPCDIVLGF EEVAPCTSDR
     KAECRCQPGM SCVYLDNECV HCEEERLVLC QPGTEAEVTD EIMDTDVNCV PCKPGHFQNT
     SSPRARCQPH TRCEIQGLVE AAPGTSYSDT ICKNPPEPGA MLLLAILLSL VLFLLFTTVL
     ACAWMRHPSL CRKLGTLLKR HPEGEESPPC PAPRADPHFP DLAEPLLPMS GDLSPSPAGP
     PTAPSLEEVV LQQQSPLVQA RELEAEPGEH GQVAHGANGI HVTGGSVTVT GNIYIYNGPV
     LGGTRGPGDP PAPPEPPYPT PEEGAPGPSE LSTPYQEDGK AWHLAETETL GCQDL
//
ID   GDIA_MOUSE              Reviewed;         447 AA.
AC   P50396; A2AMA8; Q3TBI9; Q8VHM3; Q91Y71; Q91Z41; Q96CX5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 3.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Rab GDP dissociation inhibitor alpha;
DE            Short=Rab GDI alpha;
DE   AltName: Full=Guanosine diphosphate dissociation inhibitor 1;
DE            Short=GDI-1;
GN   Name=Gdi1; Synonyms=Rabgdia;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=20481952; PubMed=11027356; DOI=10.1073/pnas.97.21.11587;
RA   Ishizaki H., Miyoshi J., Kamiya H., Togawa A., Tanaka M., Sasaki T.,
RA   Endo K., Mizoguchi A., Ozawa S., Takai Y.;
RT   "Role of rab GDP dissociation inhibitor alpha in regulating plasticity
RT   of hippocampal neurotransmission.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:11587-11592(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvEv;
RA   D'Adamo P., Welzl H., Papadimitriou S., Raffaele di Barletta M.,
RA   Tiveron C., Tatangelo L., Chapman P.F., Knevett S.G., Ramsay M.F.,
RA   Valtorta F., Leoni C., Menegon A., Wolfer D.P., Lipp H.-P.,
RA   Toniolo D.;
RT   "Knockout mice carrying a deletion of the mental retardation gene Gdi1
RT   show impaired associative memory and inappropriate social behavior.";
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Skin, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 36-54; 56-68; 104-112; 119-137; 143-169; 174-208;
RP   211-218; 222-240; 300-328; 349-379 AND 424-447, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 125-447.
RC   STRAIN=BALB/c; TISSUE=Skeletal muscle;
RX   MEDLINE=94217740; PubMed=7513052;
RA   Shisheva A., Suedhof T.C., Czech M.P.;
RT   "Cloning, characterization, and expression of a novel GDP dissociation
RT   inhibitor isoform from skeletal muscle.";
RL   Mol. Cell. Biol. 14:3459-3468(1994).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-339, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Regulates the GDP/GTP exchange reaction of most Rab
CC       proteins by inhibiting the dissociation of GDP from them, and the
CC       subsequent binding of GTP to them.
CC   -!- SUBUNIT: Interacts with RHOH (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: High expression in brain, lower in other
CC       tissues.
CC   -!- SIMILARITY: Belongs to the Rab GDI family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF251042; AAK49815.1; -; mRNA.
DR   EMBL; AF441240; AAL60197.1; -; Genomic_DNA.
DR   EMBL; AK028880; BAC26169.1; -; mRNA.
DR   EMBL; AK156224; BAE33632.1; -; mRNA.
DR   EMBL; AK171216; BAE42320.1; -; mRNA.
DR   EMBL; AL807376; CAM24345.1; -; Genomic_DNA.
DR   EMBL; BC010220; AAH10220.1; -; mRNA.
DR   EMBL; BC013758; AAH13758.1; -; mRNA.
DR   EMBL; BC037598; AAH37598.1; -; mRNA.
DR   EMBL; U07950; AAB16907.1; -; mRNA.
DR   IPI; IPI00323179; -.
DR   PIR; C56024; C56024.
DR   RefSeq; NP_034403.1; NM_010273.4.
DR   UniGene; Mm.205830; -.
DR   ProteinModelPortal; P50396; -.
DR   SMR; P50396; 1-430.
DR   MINT; MINT-1869124; -.
DR   STRING; P50396; -.
DR   PhosphoSite; P50396; -.
DR   PRIDE; P50396; -.
DR   Ensembl; ENSMUST00000015435; ENSMUSP00000015435; ENSMUSG00000015291.
DR   GeneID; 14567; -.
DR   KEGG; mmu:14567; -.
DR   UCSC; uc009tom.1; mouse.
DR   CTD; 14567; -.
DR   MGI; MGI:99846; Gdi1.
DR   eggNOG; roNOG15571; -.
DR   GeneTree; ENSGT00530000063044; -.
DR   HOVERGEN; HBG000839; -.
DR   InParanoid; P50396; -.
DR   OMA; PQNQVGR; -.
DR   OrthoDB; EOG4H19VS; -.
DR   PhylomeDB; P50396; -.
DR   NextBio; 286278; -.
DR   ArrayExpress; P50396; -.
DR   Bgee; P50396; -.
DR   Genevestigator; P50396; -.
DR   GermOnline; ENSMUSG00000015291; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:InterPro.
DR   GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR   InterPro; IPR018203; GDP_dissociation_inhibitor.
DR   InterPro; IPR002005; Rab_GDI_REP.
DR   InterPro; IPR000806; RabGDI.
DR   PANTHER; PTHR11787; Rab_GDI_REP; 1.
DR   Pfam; PF00996; GDI; 1.
DR   PRINTS; PR00892; RABGDI.
DR   PRINTS; PR00891; RABGDIREP.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; GTPase activation;
KW   Phosphoprotein.
FT   CHAIN         1    447       Rab GDP dissociation inhibitor alpha.
FT                                /FTId=PRO_0000056673.
FT   MOD_RES     333    333       Phosphotyrosine (By similarity).
FT   MOD_RES     339    339       Phosphotyrosine.
FT   CONFLICT     58     58       I -> M (in Ref. 1; AAK49815 and 3;
FT                                BAE33632/BAE42320).
FT   CONFLICT    128    128       A -> R (in Ref. 7; AAB16907).
FT   CONFLICT    165    165       N -> T (in Ref. 1; AAK49815).
FT   CONFLICT    196    196       D -> E (in Ref. 7; AAB16907).
FT   CONFLICT    223    223       P -> S (in Ref. 2; AAL60197).
SQ   SEQUENCE   447 AA;  50522 MW;  F7B9BC942B35DF58 CRC64;
     MDEEYDVIVL GTGLTECILS GIMSVNGKKV LHMDRNPYYG GESSSITPLE ELYKRFQILE
     GPPESMGRGR DWNVDLIPKF LMANGQLVKM LLYTEVTRYL DFKVVEGSFV YKGGKIYKVP
     STETEALASN LMGMFEKRRF RKFLVFVANF DENDPKTFEG VDPQNTSMRD VYRKFDLGQD
     VIDFTGHALA LYRTDDYLDQ PCLETINRIK LYSESLARYG KSPYLYPLYG LGELPQGFAR
     LSAIYGGTYM LNKPVDDIIM ENGKVVGVKS EGEVARCKQL ICDPSYIPDR VQKAGQVIRI
     ICILSHPIKN TNDANSCQII IPQNQVNRKS DIYVCMISYA HNVAAQGKYI AIASTTVETA
     EPEKEVEPAL ELLEPIDQKF VAISDLYEPI DDGSESQVFC SCSYDATTHF ETTCNDIKDI
     YKRMAGSAFD FENMKRKQND VFGEADQ
//
ID   VATA_MOUSE              Reviewed;         617 AA.
AC   P50516; Q3TKS0; Q3U5W3; Q3U777; Q3UDZ9; Q3US31; Q8CHX2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   08-MAR-2011, entry version 103.
DE   RecName: Full=V-type proton ATPase catalytic subunit A;
DE            Short=V-ATPase subunit A;
DE            EC=3.6.3.14;
DE   AltName: Full=V-ATPase 69 kDa subunit;
DE   AltName: Full=Vacuolar proton pump subunit alpha;
GN   Name=Atp6v1a; Synonyms=Atp6a1, Atp6a2, Atp6v1a1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=96362668; PubMed=8741845;
RA   Laitala T., Howell M.L., Dean G.E., Vaananen H.K.;
RT   "Resorption-cycle-dependent polarization of mRNAs for different
RT   subunits of V-ATPase in bone-resorbing osteoclasts.";
RL   Mol. Biol. Cell 7:129-142(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 45-56; 143-163; 242-251; 253-262; 266-280;
RP   324-338; 514-530 AND 599-613, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-374, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Catalytic subunit of the peripheral V1 complex of
CC       vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for
CC       acidifying a variety of intracellular compartments in eukaryotic
CC       cells.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate +
CC       H(+)(Out).
CC   -!- SUBUNIT: V-ATPase is an heteromultimeric enzyme composed of a
CC       peripheral catalytic V1 complex (main components: subunits A, B,
CC       C, D, E, and F) attached to an integral membrane V0 proton pore
CC       complex (main component: the proteolipid protein).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P50516-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P50516-2; Sequence=VSP_024628, VSP_024629;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U13837; AAC52410.1; -; Genomic_DNA.
DR   EMBL; AK140873; BAE24506.1; -; mRNA.
DR   EMBL; AK149833; BAE29112.1; -; mRNA.
DR   EMBL; AK152785; BAE31494.1; -; mRNA.
DR   EMBL; AK153403; BAE31963.1; -; mRNA.
DR   EMBL; AK154869; BAE32890.1; -; mRNA.
DR   EMBL; AK160792; BAE36015.1; -; mRNA.
DR   EMBL; AK166857; BAE39074.1; -; mRNA.
DR   EMBL; AK170721; BAE41978.1; -; mRNA.
DR   EMBL; BC038392; AAH38392.1; -; mRNA.
DR   IPI; IPI00407692; -.
DR   IPI; IPI00844689; -.
DR   RefSeq; NP_031534.2; NM_007508.5.
DR   UniGene; Mm.217787; -.
DR   ProteinModelPortal; P50516; -.
DR   SMR; P50516; 17-616.
DR   STRING; P50516; -.
DR   PhosphoSite; P50516; -.
DR   PRIDE; P50516; -.
DR   Ensembl; ENSMUST00000063661; ENSMUSP00000066886; ENSMUSG00000052459.
DR   Ensembl; ENSMUST00000114666; ENSMUSP00000110314; ENSMUSG00000052459.
DR   GeneID; 11964; -.
DR   KEGG; mmu:11964; -.
DR   NMPDR; fig|10090.3.peg.31312; -.
DR   CTD; 11964; -.
DR   MGI; MGI:1201780; Atp6v1a.
DR   eggNOG; roNOG10936; -.
DR   GeneTree; ENSGT00550000074787; -.
DR   HOVERGEN; HBG053351; -.
DR   InParanoid; P50516; -.
DR   OMA; KITWNVI; -.
DR   OrthoDB; EOG4TTGHG; -.
DR   PhylomeDB; P50516; -.
DR   BRENDA; 3.6.3.14; 244.
DR   NextBio; 280087; -.
DR   ArrayExpress; P50516; -.
DR   Bgee; P50516; -.
DR   CleanEx; MM_ATP6V1A; -.
DR   Genevestigator; P50516; -.
DR   GermOnline; ENSMUSG00000052459; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:hydrogen ion transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR000194; ATPase_a/bsu_nucl-bd.
DR   InterPro; IPR018118; ATPase_F1/A1-cplx_a/bsu_N.
DR   InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C.
DR   InterPro; IPR004100; ATPase_F1/V1/A1-cplx_a/bsu_N.
DR   InterPro; IPR005725; ATPase_V1-cplx_asu.
DR   InterPro; IPR022878; V-ATPase_su_A/alpha.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF00306; ATP-synt_ab_C; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   SUPFAM; SSF47917; ATPase_a/b_C; 1.
DR   SUPFAM; SSF50615; ATPase_a/b_N; 1.
DR   TIGRFAMs; TIGR01042; V-ATPase_V1_A; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Direct protein sequencing;
KW   Hydrogen ion transport; Hydrolase; Ion transport; Nucleotide-binding;
KW   Phosphoprotein; Transport.
FT   CHAIN         1    617       V-type proton ATPase catalytic subunit A.
FT                                /FTId=PRO_0000144561.
FT   NP_BIND     250    257       ATP (Potential).
FT   MOD_RES     374    374       Phosphotyrosine.
FT   MOD_RES     384    384       Phosphoserine.
FT   VAR_SEQ     499    509       ASLAETDKITL -> VRGGCTGCHAG (in isoform
FT                                2).
FT                                /FTId=VSP_024628.
FT   VAR_SEQ     510    617       Missing (in isoform 2).
FT                                /FTId=VSP_024629.
FT   CONFLICT     86     86       L -> R (in Ref. 1; AAC52410).
FT   CONFLICT    189    189       D -> N (in Ref. 1; AAC52410).
FT   CONFLICT    302    302       V -> A (in Ref. 1; AAC52410).
FT   CONFLICT    330    330       G -> V (in Ref. 2; BAE39074).
FT   CONFLICT    487    487       E -> G (in Ref. 1; AAC52410).
FT   CONFLICT    616    616       E -> G (in Ref. 2; BAE31963).
SQ   SEQUENCE   617 AA;  68326 MW;  D46AC76D9C7580A7 CRC64;
     MDFSKLPKIR DEDKESTFGY VHGVSGPVVT ACDMAGAAMY ELVRVGHSEL VGEIIRLEGD
     MATIQVYEET SGVSVGDPVL RTGKPLSVEL GPGIMGAIFD GIQRPLSDIS SQTQSIYIPR
     GVNVSALSRD IKWEFIPSKN LRVGSHITGG DIYGIVNENS LIKHKIMLPP RNRGSVTYIA
     PPGNYDASDV VLELEFEGVK EKFSMVQVWP VRQVRPVTEK LPANHPLLTG QRVLDALFPC
     VQGGTTAIPG AFGCGKTVIS QSLSKYSNSD VIIYVGCGER GNEMSEVLRD FPELTMEVDG
     KVESIMKRTA LVANTSNMPV AAREASIYTG ITLSEYFRDM GYHVSMMADS TSRWAEALRE
     ISGRLAEMPA DSGYPAYLGA RLASFYERAG RVKCLGNPER EGSVSIVGAV SPPGGDFSDP
     VTSATLGIVQ VFWGLDKKLA QRKHFPSVNW LISYSKYMRA LDEYYDKHFT EFVPLRTKAK
     EILQEEEDLA EIVQLVGKAS LAETDKITLE VAKLIKDDFL QQNGYTPYDR FCPFYKTVGM
     LSNMISFYDM ARRAVETTAQ SDNKITWSII REHMGEILYK LSSMKFKDPV KDGEAKIKAD
     YAQLLEDMQN AFRSLED
//
ID   VATE1_MOUSE             Reviewed;         226 AA.
AC   P50518; Q3UK59; Q8K5D6; Q99LD0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=V-type proton ATPase subunit E 1;
DE            Short=V-ATPase subunit E 1;
DE   AltName: Full=V-ATPase 31 kDa subunit;
DE            Short=p31;
DE   AltName: Full=Vacuolar proton pump subunit E 1;
GN   Name=Atp6v1e1; Synonyms=Atp6e, Atp6e2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=96362668; PubMed=8741845;
RA   Laitala T., Howell M.L., Dean G.E., Vaananen H.K.;
RT   "Resorption-cycle-dependent polarization of mRNAs for different
RT   subunits of V-ATPase in bone-resorbing osteoclasts.";
RL   Mol. Biol. Cell 7:129-142(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=22001299; PubMed=11872743; DOI=10.1074/jbc.M111567200;
RA   Sun-Wada G.H., Imai-Senga Y., Yamamoto A., Murata Y., Hirata T.,
RA   Wada Y., Futai M.;
RT   "A proton pump ATPase with testis-specific E1-subunit isoform required
RT   for acrosome acidification.";
RL   J. Biol. Chem. 277:18098-18105(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, DBA/2, and NOD; TISSUE=Placenta, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 14-26; 35-43; 54-60; 71-82; 86-101; 112-131;
RP   140-147; 200-214 AND 215-224, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-56, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase
CC       essential for assembly or catalytic function. V-ATPase is
CC       responsible for acidifying a variety of intracellular compartments
CC       in eukaryotic cells.
CC   -!- SUBUNIT: V-ATPase is an heteromultimeric enzyme composed of a
CC       peripheral catalytic V1 complex (components A to H) attached to an
CC       integral membrane V0 proton pore complex (components: a, c, c',
CC       c'' and d). Interacts with ALDOC (By similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the V-ATPase E subunit family.
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DR   EMBL; U13841; AAC52412.1; -; Genomic_DNA.
DR   EMBL; AB074758; BAB92084.1; -; mRNA.
DR   EMBL; AK146162; BAE26943.1; -; mRNA.
DR   EMBL; AK149356; BAE28832.1; -; mRNA.
DR   EMBL; AK167644; BAE39695.1; -; mRNA.
DR   EMBL; AK169854; BAE41412.1; -; mRNA.
DR   EMBL; BC003421; AAH03421.1; -; mRNA.
DR   EMBL; BC055438; AAH55438.1; -; mRNA.
DR   IPI; IPI00119115; -.
DR   RefSeq; NP_031536.2; NM_007510.2.
DR   UniGene; Mm.29045; -.
DR   ProteinModelPortal; P50518; -.
DR   SMR; P50518; 108-216.
DR   STRING; P50518; -.
DR   PhosphoSite; P50518; -.
DR   PRIDE; P50518; -.
DR   Ensembl; ENSMUST00000019354; ENSMUSP00000019354; ENSMUSG00000019210.
DR   GeneID; 11973; -.
DR   KEGG; mmu:11973; -.
DR   CTD; 11973; -.
DR   MGI; MGI:894326; Atp6v1e1.
DR   eggNOG; maNOG17603; -.
DR   GeneTree; ENSGT00390000002730; -.
DR   HOGENOM; HBG525538; -.
DR   HOVERGEN; HBG002309; -.
DR   InParanoid; P50518; -.
DR   OMA; EIRVALF; -.
DR   OrthoDB; EOG479F86; -.
DR   PhylomeDB; P50518; -.
DR   BRENDA; 3.6.3.14; 244.
DR   NextBio; 280099; -.
DR   ArrayExpress; P50518; -.
DR   Bgee; P50518; -.
DR   CleanEx; MM_ATP6V1E1; -.
DR   Genevestigator; P50518; -.
DR   GermOnline; ENSMUSG00000019210; Mus musculus.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro.
DR   GO; GO:0008553; F:hydrogen-exporting ATPase activity, phosphorylative mechanism; IMP:MGI.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IMP:MGI.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR002842; ATPase_V1/A1-cplx_esu.
DR   Pfam; PF01991; vATP-synt_E; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Hydrogen ion transport;
KW   Hydrolase; Ion transport; Phosphoprotein; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    226       V-type proton ATPase subunit E 1.
FT                                /FTId=PRO_0000117296.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      56     56       Phosphotyrosine.
FT   CONFLICT      2      5       ALSD -> GLRH (in Ref. 1; AAC52412).
FT   CONFLICT     29     29       E -> EE (in Ref. 1; AAC52412).
FT   CONFLICT     46     47       VQ -> LE (in Ref. 1; AAC52412).
FT   CONFLICT     65     65       E -> R (in Ref. 1; AAC52412).
FT   CONFLICT     67     67       Q -> QQ (in Ref. 1; AAC52412).
FT   CONFLICT     86     86       A -> T (in Ref. 2; BAB92084).
FT   CONFLICT    103    103       S -> M (in Ref. 1; AAC52412).
FT   CONFLICT    153    153       P -> T (in Ref. 3; BAE26943).
FT   CONFLICT    161    161       K -> R (in Ref. 1; AAC52412).
FT   CONFLICT    171    176       AYLPEE -> PTCLRN (in Ref. 1; AAC52412).
SQ   SEQUENCE   226 AA;  26157 MW;  5DD7B0EAB181EA08 CRC64;
     MALSDADVQK QIKHMMAFIE QEANEKAEEI DAKAEEEFNI EKGRLVQTQR LKIMEYYEKK
     EKQIEQQKKI QMSNLMNQAR LKVLRARDDL ITDLLNEAKQ RLSKVVKDTT RYQVLLDGLV
     LQGLYQLLEP RMIVRCRKQD FPLVKAAVQK AIPMYKIATK KDVDVQIDQE AYLPEEIAGG
     VEIYNGDRKI KVSNTLESRL DLIAQQMMPE VRGALFGANA NRKFLD
//
ID   GBRB1_MOUSE             Reviewed;         474 AA.
AC   P50571;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit beta-1;
DE   AltName: Full=GABA(A) receptor subunit beta-1;
DE   Flags: Precursor;
GN   Name=Gabrb1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J, and DBA/2J; TISSUE=Brain;
RX   MEDLINE=95200962; PubMed=7893750; DOI=10.1016/0167-4781(95)00009-6;
RA   Kamatchi G.L., Kofuji P., Wang J.B., Fernando J.C., Liu Z.,
RA   Mathura J.R., Burt D.R.;
RT   "GABAA receptor beta 1, beta 2, and beta 3 subunits: comparisons in
RT   DBA/2J and C57BL/6J mice.";
RL   Biochim. Biophys. Acta 1261:134-142(1995).
RN   [2]
RP   INTERACTION WITH UBQLN1.
RX   MEDLINE=21419682; PubMed=11528422; DOI=10.1038/nn0901-908;
RA   Bedford F.K., Kittler J.T., Muller E., Thomas P., Uren J.M., Merlo D.,
RA   Wisden W., Triller A., Smart T.G., Moss S.J.;
RT   "GABA(A) receptor cell surface number and subunit stability are
RT   regulated by the ubiquitin-like protein Plic-1.";
RL   Nat. Neurosci. 4:908-916(2001).
RN   [3]
RP   INTERACTION WITH KCTD8; KCTD12; KCTD12B AND KCTD16.
RX   PubMed=20400944; DOI=10.1038/nature08964;
RA   Schwenk J., Metz M., Zolles G., Turecek R., Fritzius T., Bildl W.,
RA   Tarusawa E., Kulik A., Unger A., Ivankova K., Seddik R., Tiao J.Y.,
RA   Rajalu M., Trojanova J., Rohde V., Gassmann M., Schulte U., Fakler B.,
RA   Bettler B.;
RT   "Native GABA(B) receptors are heteromultimers with a family of
RT   auxiliary subunits.";
RL   Nature 465:231-235(2010).
CC   -!- FUNCTION: GABA, the major inhibitory neurotransmitter in the
CC       vertebrate brain, mediates neuronal inhibition by binding to the
CC       GABA/benzodiazepine receptor and opening an integral chloride
CC       channel.
CC   -!- SUBUNIT: Generally pentameric. There are five types of GABA(A)
CC       receptor chains: alpha, beta, gamma, delta, and rho. Binds UBQLN1.
CC       Interacts with KCTD8, KCTD12, KCTD12B and KCTD16; this interaction
CC       determines the pharmacology and kinetics of the receptor response,
CC       the KCTD proteins markedly accelerating the GABA-B response,
CC       although to different extents.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane; Multi-pass membrane protein. Cell membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
CC       family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily.
CC       GABRB1 sub-subfamily.
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DR   EMBL; U14418; AAA79973.1; -; mRNA.
DR   IPI; IPI00119283; -.
DR   PIR; S53530; S53530.
DR   RefSeq; NP_032095.1; NM_008069.4.
DR   UniGene; Mm.38567; -.
DR   ProteinModelPortal; P50571; -.
DR   SMR; P50571; 60-331.
DR   STRING; P50571; -.
DR   PhosphoSite; P50571; -.
DR   PRIDE; P50571; -.
DR   Ensembl; ENSMUST00000031122; ENSMUSP00000031122; ENSMUSG00000029212.
DR   GeneID; 14400; -.
DR   KEGG; mmu:14400; -.
DR   UCSC; uc008xrb.1; mouse.
DR   CTD; 14400; -.
DR   MGI; MGI:95619; Gabrb1.
DR   eggNOG; roNOG12839; -.
DR   HOGENOM; HBG506497; -.
DR   HOVERGEN; HBG051707; -.
DR   InParanoid; P50571; -.
DR   OMA; SIQYRRP; -.
DR   OrthoDB; EOG45756F; -.
DR   PhylomeDB; P50571; -.
DR   NextBio; 285945; -.
DR   ArrayExpress; P50571; -.
DR   Bgee; P50571; -.
DR   Genevestigator; P50571; -.
DR   GermOnline; ENSMUSG00000029212; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IEA:InterPro.
DR   InterPro; IPR006028; GABAA_rcpt.
DR   InterPro; IPR002289; GABAAb_rcpt.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   Gene3D; G3DSA:2.70.170.10; Neur_chan_lig_bd; 1.
DR   PANTHER; PTHR18945; Neur_channel; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR01160; GABAARBETA.
DR   PRINTS; PR00253; GABAARECEPTR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF90112; Neu_channel_TM; 1.
DR   SUPFAM; SSF63712; Neur_chan_LBD; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Chloride; Chloride channel;
KW   Disulfide bond; Glycoprotein; Ion transport; Ionic channel;
KW   Ligand-gated ion channel; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Receptor; Signal; Synapse; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     25       Potential.
FT   CHAIN        26    474       Gamma-aminobutyric acid receptor subunit
FT                                beta-1.
FT                                /FTId=PRO_0000000457.
FT   TOPO_DOM     26    245       Extracellular (Probable).
FT   TRANSMEM    246    267       Helical; (Probable).
FT   TRANSMEM    271    293       Helical; (Probable).
FT   TRANSMEM    305    327       Helical; (Probable).
FT   TOPO_DOM    328    451       Cytoplasmic (Probable).
FT   TRANSMEM    452    473       Helical; (Probable).
FT   MOD_RES     448    448       Phosphoserine (By similarity).
FT   CARBOHYD     33     33       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    105    105       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    174    174       N-linked (GlcNAc...) (Potential).
FT   DISULFID    161    175       By similarity.
SQ   SEQUENCE   474 AA;  54100 MW;  986C47E4BD663763 CRC64;
     MWTVQNRESL GLLSFPVMVA MVCCAHSSNE PSNMSYVKET VDRLLKGYDI RLRPDFGGPP
     VDVGMRIDVA SIDMVSEVNM DYTLTMYFQQ SWKDKRLSYS GIPLNLTLDN RVADQLWVPD
     TYFLNDKKSF VHGVTVKNRM IRLHPDGTVL YGLRITTTAA CMMDLRRYPL DEQNCTLEIE
     SYGYTTDDIE FYWNGGEGAV TGVNKIELPQ FSIVDYKMVS KKVEFTTGAY PRLSLSFRLK
     RNIGYFILQT YMPSTLITIL SWVSFWINYD ASAARVALGI TTVLTMTTIS THLRETLPKI
     PYVKAIDIYL MGCFVFVFLA LLEYAFVNYI FFGKGPQKKG ASKQDQSANE KNRLEMNKVQ
     VDAHGNILLS TLEIRNETSG SEVLTGVSDP KATMYSYDSA SIQYRKPLSS REGFGRGLDR
     HGVPGKGRIR RRASQLKVKI PDLTDVNSID KWSRMFFPIT FSLFNVVYWL YYVH
//
ID   PA2G4_MOUSE             Reviewed;         394 AA.
AC   P50580;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 100.
DE   RecName: Full=Proliferation-associated protein 2G4;
DE   AltName: Full=IRES-specific cellular trans-acting factor 45 kDa;
DE            Short=ITAF45;
DE   AltName: Full=Mpp1;
DE   AltName: Full=Proliferation-associated protein 1;
DE   AltName: Full=Protein p38-2G4;
GN   Name=Pa2g4; Synonyms=Ebp1, Plfap;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=NFS;
RX   MEDLINE=96032817; PubMed=7556453; DOI=10.1006/excr.1995.1335;
RA   Radomski N., Jost E.;
RT   "Molecular cloning of a murine cDNA encoding a novel protein, p38-2G4,
RT   which varies with the cell cycle.";
RL   Exp. Cell Res. 220:434-445(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=NFS;
RX   MEDLINE=97430868; PubMed=9284967;
RA   Nakagawa Y., Watanabe S., Akiyama K., Sarker A.H., Tsutsui K.,
RA   Inoue H., Seki S.;
RT   "cDNA cloning, sequence analysis and expression of a mouse 44-kDa
RT   nuclear protein copurified with DNA repair factors for acid-
RT   depurinated DNA.";
RL   Acta Med. Okayama 51:195-206(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA], RNA-BINDING, AND FUNCTION IN VIRAL
RP   TRANSLATION.
RX   PubMed=10950867;
RA   Pilipenko E.V., Pestova T.V., Kolupaeva V.G., Khitrina E.V.,
RA   Poperechnaya A.N., Agol V.I., Hellen C.U.;
RT   "A cell cycle-dependent protein serves as a template-specific
RT   translation initiation factor.";
RL   Genes Dev. 14:2028-2045(2000).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=15064750; DOI=10.1038/sj.onc.1207579;
RA   Squatrito M., Mancino M., Donzelli M., Areces L.B., Draetta G.F.;
RT   "EBP1 is a nucleolar growth-regulating protein that is part of pre-
RT   ribosomal ribonucleoprotein complexes.";
RL   Oncogene 23:4454-4465(2004).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION AT SER-2,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 8-360, ABSENCE OF METAL
RP   COFACTOR AND OF AMINOPEPTIDASE ACTIVITY, FUNCTION, MUTAGENESIS OF
RP   65-LYS--LYS-72, AND INTERACTION WITH RNA.
RX   PubMed=17690690; DOI=10.1038/sj.emboj.7601817;
RA   Monie T.P., Perrin A.J., Birtley J.R., Sweeney T.R.,
RA   Karakasiliotis I., Chaudhry Y., Roberts L.O., Matthews S.,
RA   Goodfellow I.G., Curry S.;
RT   "Structural insights into the transcriptional and translational roles
RT   of Ebp1.";
RL   EMBO J. 26:3936-3944(2007).
CC   -!- FUNCTION: May play a role in a ERBB3-regulated signal transduction
CC       pathway. Seems be involved in growth regulation. Acts a
CC       corepressor of the androgen receptor (AR) and is regulated by the
CC       ERBB3 ligand neuregulin-1/heregulin (HRG). Inhibits transcription
CC       of some E2F1-regulated promoters, probably by recruiting histone
CC       acetylase (HAT) activity. Binds RNA. Associates with 28S, 18S and
CC       5.8S mature rRNAs, several rRNA precursors and probably U3 small
CC       nucleolar RNA. May be involved in regulation of intermediate and
CC       late steps of rRNA processing. May be involved in ribosome
CC       assembly (By similarity). Mediates cap-independent translation of
CC       specific viral IRESs (internal ribosomal entry site). Together
CC       with PTBP1 is required for the translation initiation on the foot-
CC       and-mouth disease virus (FMDV) IRES.
CC   -!- SUBUNIT: Interacts with the cytoplasmic domain of non-
CC       phosphorylated ERBB3; the interaction requires PKC activity.
CC       Interacts with AR. Treatment with HRG leads to dissociation from
CC       ERBB3 and increases association with AR. Interacts with
CC       nucleolin/NCL. Component of a ribonucleoprotein complex containing
CC       at least PA2G4, NCL, TOP1, PABPC2, RPLP0, acetylated histone H1
CC       (HIST1H1A or H1F1), histone H1 2/4, RPL4, RPL8, RPL15, RPL18,
CC       RPL18A, RPL21, RPL11, RPL12, RPL28, RPL27, RPLP2 and RPL24.
CC       Interacts with HDAC2. Interacts with RB1; the interaction is
CC       enhanced upon PA2G4 dephosphorylation (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus,
CC       nucleolus (By similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- DEVELOPMENTAL STAGE: Expressed in proliferating cells. Observed
CC       between G1 and mid S phase, decrease toward the end of S phase,
CC       and disappear at the S/G2 transition.
CC   -!- INDUCTION: By mitogens.
CC   -!- MISCELLANEOUS: Does not contain metal cofactors and does not have
CC       aminopeptidase activity.
CC   -!- SIMILARITY: Belongs to the peptidase M24 family.
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DR   EMBL; X84789; CAA59260.1; ALT_SEQ; mRNA.
DR   EMBL; U43918; AAB60513.1; -; mRNA.
DR   EMBL; BC046532; AAH46532.1; -; mRNA.
DR   IPI; IPI00119305; -.
DR   PIR; I48702; S54181.
DR   RefSeq; NP_035249.1; NM_011119.3.
DR   UniGene; Mm.4742; -.
DR   PDB; 2V6C; X-ray; 2.50 A; A=9-360.
DR   PDBsum; 2V6C; -.
DR   ProteinModelPortal; P50580; -.
DR   SMR; P50580; 8-360.
DR   MINT; MINT-1857756; -.
DR   STRING; P50580; -.
DR   MEROPS; M24.973; -.
DR   PMMA-2DPAGE; P50580; -.
DR   PRIDE; P50580; -.
DR   Ensembl; ENSMUST00000026425; ENSMUSP00000026425; ENSMUSG00000025364.
DR   GeneID; 18813; -.
DR   KEGG; mmu:18813; -.
DR   UCSC; uc007hnl.1; mouse.
DR   CTD; 18813; -.
DR   MGI; MGI:894684; Pa2g4.
DR   eggNOG; roNOG08428; -.
DR   HOGENOM; HBG629020; -.
DR   HOVERGEN; HBG053117; -.
DR   InParanoid; P50580; -.
DR   OMA; AHTFVVG; -.
DR   OrthoDB; EOG4J6RR6; -.
DR   PhylomeDB; P50580; -.
DR   NextBio; 295158; -.
DR   ArrayExpress; P50580; -.
DR   Bgee; P50580; -.
DR   CleanEx; MM_PA2G4; -.
DR   Genevestigator; P50580; -.
DR   GermOnline; ENSMUSG00000025364; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR004545; Pap_1.
DR   InterPro; IPR000994; Pept_M24_structural-domain.
DR   InterPro; IPR018349; Pept_M24A_MAP2_BS.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:3.90.230.10; Peptidase_M24_cat_core; 2.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   PANTHER; PTHR10804; Peptidase_M24_cat_core; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   SUPFAM; SSF55920; Peptidase_M24_cat_core; 1.
DR   TIGRFAMs; TIGR00495; crvDNA_42K; 1.
DR   PROSITE; PS01202; MAP_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Nucleus; Phosphoprotein;
KW   Repressor; Ribonucleoprotein; RNA-binding; rRNA processing;
KW   Transcription; Transcription regulation; Translation regulation.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    394       Proliferation-associated protein 2G4.
FT                                /FTId=PRO_0000148990.
FT   REGION        2     48       Necessary for nucleolar localization (By
FT                                similarity).
FT   REGION       46     54       RNA-binding (By similarity).
FT   REGION      301    394       Necessary for nucleolar localization (By
FT                                similarity).
FT   REGION      361    375       Interaction with RNA.
FT   MOD_RES       2      2       N-acetylserine.
FT   MOD_RES       2      2       Phosphoserine.
FT   MOD_RES      11     11       Phosphothreonine (By similarity).
FT   MOD_RES     361    361       Phosphoserine (By similarity).
FT   MOD_RES     366    366       Phosphothreonine (By similarity).
FT   MOD_RES     383    383       Phosphoserine (By similarity).
FT   MOD_RES     386    386       Phosphothreonine (By similarity).
FT   MUTAGEN      65     72       KKEKEMKK->SSSSSSSS: No effect on RNA-
FT                                binding.
FT   CONFLICT    279    279       T -> A (in Ref. 4).
FT   CONFLICT    311    311       K -> R (in Ref. 4).
FT   HELIX        15     36
FT   HELIX        45     60
FT   STRAND       72     82
FT   STRAND       85     87
FT   STRAND       93     95
FT   STRAND      105    114
FT   STRAND      117    126
FT   HELIX       138    156
FT   HELIX       163    176
FT   STRAND      186    189
FT   STRAND      194    196
FT   STRAND      198    204
FT   HELIX       207    212
FT   STRAND      223    233
FT   STRAND      246    249
FT   HELIX       260    272
FT   TURN        273    275
FT   HELIX       280    282
FT   HELIX       286    298
FT   STRAND      301    305
FT   STRAND      316    326
FT   STRAND      329    332
FT   HELIX       340    342
FT   HELIX       352    357
SQ   SEQUENCE   394 AA;  43699 MW;  ABCD169F064261EB CRC64;
     MSGEDEQQEQ TIAEDLVVTK YKMGGDIANR VLRSLVEASS SGVSVLSLCE KGDAMIMEET
     GKIFKKEKEM KKGIAFPTSI SVNNCVCHFS PLKSDQDYIL KEGDLVKIDL GVHVDGFIAN
     VAHTFVIGVA QGTQVTGRKA DVIKAAHLCA EAALRLVKPG NQNTQVTEAW NKVAHSFNCT
     PIEGMLSHQL KQHVIDGEKT IIQNPTDQQK KDHEKAEFEV HEVYAVDVLV SSGEGKAKDA
     GQRTTIYKRD PSKQYGLKMK TSRAFFSEVE RRFDAMPFTL RAFEDEKKAR MGVVECAKHE
     LLQPFNVLYE KEGEFVAQFK FTVLLMPNGP MRITSGPFEP DLYKSEMEVQ DAELKALLQS
     SASRKTQKKK KKKASKTVEN ATSGETLEEN GAGD
//
ID   ICAL_MOUSE              Reviewed;         788 AA.
AC   P51125; Q9EQV4; Q9EQV5; Q9QXQ3; Q9QXQ4; Q9R0N1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-2002, sequence version 2.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Calpastatin;
DE   AltName: Full=Calpain inhibitor;
GN   Name=Cast;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=C3H; TISSUE=Muscle;
RX   MEDLINE=99333681; PubMed=10403772; DOI=10.1006/bbrc.1999.0903;
RA   Takano J., Kawamura T., Murase M., Hitomi K., Maki M.;
RT   "Structure of mouse calpastatin isoforms: implications of species-
RT   common and species-specific alternative splicing.";
RL   Biochem. Biophys. Res. Commun. 260:339-345(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ISOFORMS 4; 5; 6 AND 7), AND TISSUE SPECIFICITY.
RX   MEDLINE=20336652; PubMed=10876161;
RA   Takano J., Watanabe M., Hitomi K., Maki M.;
RT   "Four types of calpastatin isoforms with distinct amino-terminal
RT   sequences are specified by alternative first exons and differentially
RT   expressed in mouse tissues.";
RL   J. Biochem. 128:83-92(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE (ISOFORMS 4 AND 5).
RC   STRAIN=CD-1;
RA   Li S., Goldberg E.;
RT   "Characterization of a membrane associated testis-specific
RT   calpastatin.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE OF 84-363 (ISOFORM 2).
RC   STRAIN=BALB/c; TISSUE=Heart;
RX   MEDLINE=92110395; PubMed=1730065; DOI=10.1016/0167-4781(92)90500-Y;
RA   Lee W.J., Hatanaka M., Maki M.;
RT   "Multiple forms of rat calpastatin cDNA in the coding region of
RT   functionally unknown amino-terminal domain.";
RL   Biochim. Biophys. Acta 1129:251-253(1992).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-165 AND SER-219,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND THR-479, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Specific inhibition of calpain (calcium-dependent
CC       cysteine protease). Plays a key role in postmortem tenderization
CC       of meat and have been proposed to be involved in muscle protein
CC       degradation in living tissue.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=1; Synonyms=MCS-A;
CC         IsoId=P51125-1; Sequence=Displayed;
CC       Name=2; Synonyms=MCS-B;
CC         IsoId=P51125-2; Sequence=VSP_000751;
CC       Name=3; Synonyms=MCS-C;
CC         IsoId=P51125-3; Sequence=VSP_000751, VSP_000752;
CC       Name=4; Synonyms=TCAST1;
CC         IsoId=P51125-4; Sequence=VSP_000747, VSP_000748;
CC       Name=5; Synonyms=TCAST2;
CC         IsoId=P51125-5; Sequence=VSP_000749, VSP_000750;
CC       Name=6;
CC         IsoId=P51125-6; Sequence=VSP_000745;
CC       Name=7;
CC         IsoId=P51125-7; Sequence=VSP_000746;
CC   -!- TISSUE SPECIFICITY: Isoform 2 is the major form in all tissues
CC       examined. Isoform 1 accounts for 5-10% in tissues such as skeletal
CC       muscle, liver and brain, and 30% in myoblasts. Isoforms 4 and 5
CC       are testis-specific. Isoform 6 is highly expressed in heart and
CC       skeletal muscle with lower levels in liver, brain and testis.
CC       Isoform 7 is expressed at high levels in liver.
CC   -!- DOMAIN: Has four inhibitory domains.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I27 (calpastatin)
CC       family.
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DR   EMBL; AB026997; BAA84768.1; -; mRNA.
DR   EMBL; AF190152; AAF25194.1; -; mRNA.
DR   EMBL; AF190151; AAF25193.1; -; mRNA.
DR   EMBL; AB044334; BAB18888.1; -; Genomic_DNA.
DR   EMBL; AB044334; BAB18889.1; -; Genomic_DNA.
DR   EMBL; AB044334; BAB18886.1; -; Genomic_DNA.
DR   EMBL; AB044334; BAB18887.1; -; Genomic_DNA.
DR   EMBL; X62519; CAA44385.1; -; mRNA.
DR   IPI; IPI00230641; -.
DR   IPI; IPI00230642; -.
DR   IPI; IPI00230643; -.
DR   IPI; IPI00230644; -.
DR   IPI; IPI00230645; -.
DR   IPI; IPI00409176; -.
DR   IPI; IPI00754820; -.
DR   PIR; S20610; S20610.
DR   UniGene; Mm.29163; -.
DR   UniGene; Mm.441995; -.
DR   ProteinModelPortal; P51125; -.
DR   SMR; P51125; 237-321, 644-734.
DR   STRING; P51125; -.
DR   MEROPS; I27.001; -.
DR   MEROPS; I27.002; -.
DR   MEROPS; I27.003; -.
DR   MEROPS; I27.004; -.
DR   PhosphoSite; P51125; -.
DR   PRIDE; P51125; -.
DR   Ensembl; ENSMUST00000072276; ENSMUSP00000072125; ENSMUSG00000021585.
DR   Ensembl; ENSMUST00000109610; ENSMUSP00000105239; ENSMUSG00000021585.
DR   Ensembl; ENSMUST00000109612; ENSMUSP00000105241; ENSMUSG00000021585.
DR   Ensembl; ENSMUST00000109613; ENSMUSP00000105242; ENSMUSG00000021585.
DR   UCSC; uc007rfl.1; mouse.
DR   UCSC; uc007rfq.1; mouse.
DR   MGI; MGI:1098236; Cast.
DR   eggNOG; roNOG08688; -.
DR   HOGENOM; HBG403188; -.
DR   HOVERGEN; HBG000183; -.
DR   InParanoid; P51125; -.
DR   OMA; NPTETKA; -.
DR   OrthoDB; EOG4H463V; -.
DR   PhylomeDB; P51125; -.
DR   ArrayExpress; P51125; -.
DR   Bgee; P51125; -.
DR   CleanEx; MM_CAST; -.
DR   Genevestigator; P51125; -.
DR   GermOnline; ENSMUSG00000021585; Mus musculus.
DR   GO; GO:0010859; F:calcium-dependent cysteine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   InterPro; IPR001259; Prot_inh_calpain.
DR   Pfam; PF00748; Calpain_inhib; 4.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Phosphoprotein; Protease inhibitor;
KW   Repeat; Thiol protease inhibitor.
FT   CHAIN         1    788       Calpastatin.
FT                                /FTId=PRO_0000147633.
FT   REPEAT      251    303       Inhibitory domain 1.
FT   REPEAT      384    436       Inhibitory domain 2.
FT   REPEAT      524    577       Inhibitory domain 3.
FT   REPEAT      661    714       Inhibitory domain 4.
FT   MOD_RES      11     11       Phosphoserine.
FT   MOD_RES     165    165       Phosphoserine.
FT   MOD_RES     219    219       Phosphoserine.
FT   MOD_RES     223    223       Phosphoserine (By similarity).
FT   MOD_RES     303    303       Phosphoserine (By similarity).
FT   MOD_RES     324    324       Phosphoserine (By similarity).
FT   MOD_RES     444    444       Phosphoserine (By similarity).
FT   MOD_RES     446    446       Phosphoserine (By similarity).
FT   MOD_RES     453    453       Phosphoserine (By similarity).
FT   MOD_RES     479    479       Phosphothreonine.
FT   MOD_RES     707    707       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1    357       Missing (in isoform 5).
FT                                /FTId=VSP_000749.
FT   VAR_SEQ       1    341       Missing (in isoform 4).
FT                                /FTId=VSP_000747.
FT   VAR_SEQ       1     83       Missing (in isoform 7).
FT                                /FTId=VSP_000746.
FT   VAR_SEQ       1     25       MSQPGPKPAASPRPSRGAAARHTQE -> MAFASWWYKT
FT                                (in isoform 6).
FT                                /FTId=VSP_000745.
FT   VAR_SEQ      92    110       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_000751.
FT   VAR_SEQ     305    333       Missing (in isoform 3).
FT                                /FTId=VSP_000752.
FT   VAR_SEQ     342    396       AQSAGVTRSSVPPKEKKRKVEEEVINDQALQALSDSLGTRQ
FT                                PDPPSHVSQAEQVK -> MGQFLSSTFWEGSPAAVWQEKLR
FT                                EGERKGAGETIPILQDHVICSEEREHGSKHH (in
FT                                isoform 4).
FT                                /FTId=VSP_000748.
FT   VAR_SEQ     358    397       KRKVEEEVINDQALQALSDSLGTRQPDPPSHVSQAEQVKE
FT                                -> MGQFLSSTFWEGSPAAVWQEKLREGERKGAGETIPILQ
FT                                DH (in isoform 5).
FT                                /FTId=VSP_000750.
SQ   SEQUENCE   788 AA;  84922 MW;  28E4D3B4A68BFEB9 CRC64;
     MSQPGPKPAA SPRPSRGAAA RHTQEHVNEK NIGSSSKPGE KKGSDEKKAA SLGSSQPSRP
     HVGEAATATK VTASSAATSK SPSMSTTETK AIPVNKQLEG PDQKRPREQA VKTESKKPQS
     SEQPVVHEKK SKGGPKEGSE PKNLPKHTSS TGSKHAHKEK ALSRSNEQMV SEKPSESKTK
     FQDVPSAGGE SVAGGGTVAT ALDKVVGKKK EQKPFTPASP VQSTPSKPSD KSGMDAALDD
     LIDTLGGHED TNRDDPPYTG PVVLDPMYST YLEALGIKEG TIPPEYRKLL EKNEGITQPL
     PDSPKPMGTD QAIDALSSDF TCSSPTGKQS EKEKSTGEIF KAQSAGVTRS SVPPKEKKRK
     VEEEVINDQA LQALSDSLGT RQPDPPSHVS QAEQVKEAKA KEERQEKCGE DEDTVPAEYR
     LKPAKDKDGK PLLPEPEETS KSLSESELIG ELSADFDRST YQDKPSTPAE KKSNDTSQTP
     PGETVPRASM CSIRSAPPKL ASLKGVVPED AVETLAGSLG TREADPEHEK TVEDKVKEKA
     KEEEHEKLGE KEETVPPDYR LEEVKDKDGK PLLPKESQEQ LAPLSDDFLL DALSQDFSSP
     ANISSLEFED AKLSAAISEV VSQTPAPSTH AAAPLPGTEQ KDKELDDALD ELSDSLGQRP
     PDPDENKPLD DKVKEKIKPE HSEKLGERDD TIPPEYRHLL DNDGKDKPEK PPTKKTEKPD
     QDRDPIDALS EDLDSCPSTT ETSKNTAKGK SKKTSSSKAS KDGEKTKDSS KKTEEVSKPK
     AKEDARHS
//
ID   RAB7A_MOUSE             Reviewed;         207 AA.
AC   P51150;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   08-MAR-2011, entry version 101.
DE   RecName: Full=Ras-related protein Rab-7a;
GN   Name=Rab7a; Synonyms=Rab7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96138545; PubMed=8547311; DOI=10.1016/0167-4781(95)00188-3;
RA   Vitelli R., Chiariello M., Bruni C.B., Bucci C.;
RT   "Cloning and expression analysis of the murine Rab7 cDNA.";
RL   Biochim. Biophys. Acta 1264:268-270(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 11-31; 70-79; 114-126 AND 147-157, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=12545426; DOI=10.1086/367847;
RA   Verhoeven K., De Jonghe P., Coen K., Verpoorten N., Auer-Grumbach M.,
RA   Kwon J.M., FitzPatrick D., Schmedding E., De Vriendt E., Jacobs A.,
RA   Van Gerwen V., Wagner K., Hartung H.-P., Timmerman V.;
RT   "Mutations in the small GTP-ase late endosomal protein RAB7 cause
RT   Charcot-Marie-Tooth type 2B neuropathy.";
RL   Am. J. Hum. Genet. 72:722-727(2003).
RN   [6]
RP   INTERACTION WITH RNF115.
RX   PubMed=12972561; DOI=10.1091/mbc.E02-08-0495;
RA   Mizuno K., Kitamura A., Sasaki T.;
RT   "Rabring7, a novel Rab7 target protein with a RING finger motif.";
RL   Mol. Biol. Cell 14:3741-3752(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Involved in late endocytic transport. Contributes to the
CC       maturation of phagosomes (acidification) (By similarity).
CC   -!- SUBUNIT: Interacts with RILP (By similarity). Interacts with PSMA7
CC       (By similarity). Interacts with RNF115.
CC   -!- SUBCELLULAR LOCATION: Late endosome (By similarity). Lysosome (By
CC       similarity). Cytoplasmic vesicle, phagosome (By similarity).
CC       Melanosome (By similarity). Note=Found on late endosomes,
CC       lysosomes and phagosomes (By similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed. High expression in liver,
CC       heart and kidney. Found in sensory and motor neurons.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR   EMBL; X89650; CAA61797.1; -; mRNA.
DR   EMBL; AK005004; BAB23738.1; -; mRNA.
DR   EMBL; BC004597; AAH04597.1; -; mRNA.
DR   EMBL; BC086793; AAH86793.1; -; mRNA.
DR   IPI; IPI00408892; -.
DR   PIR; S62733; S62733.
DR   RefSeq; NP_033031.2; NM_009005.2.
DR   UniGene; Mm.333233; -.
DR   UniGene; Mm.405871; -.
DR   UniGene; Mm.471618; -.
DR   ProteinModelPortal; P51150; -.
DR   SMR; P51150; 7-190.
DR   PhosphoSite; P51150; -.
DR   PRIDE; P51150; -.
DR   Ensembl; ENSMUST00000095048; ENSMUSP00000092658; ENSMUSG00000079477.
DR   Ensembl; ENSMUST00000113596; ENSMUSP00000109226; ENSMUSG00000079477.
DR   Ensembl; ENSMUST00000113597; ENSMUSP00000109227; ENSMUSG00000079477.
DR   Ensembl; ENSMUST00000113598; ENSMUSP00000109228; ENSMUSG00000079477.
DR   Ensembl; ENSMUST00000113600; ENSMUSP00000109230; ENSMUSG00000079477.
DR   GeneID; 19349; -.
DR   KEGG; mmu:19349; -.
DR   UCSC; uc009cuv.1; mouse.
DR   CTD; 19349; -.
DR   MGI; MGI:105068; Rab7.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; P51150; -.
DR   OMA; HRYVNDK; -.
DR   OrthoDB; EOG4QFWF4; -.
DR   PhylomeDB; P51150; -.
DR   NextBio; 296377; -.
DR   ArrayExpress; P51150; -.
DR   Bgee; P51150; -.
DR   CleanEx; MM_RAB7; -.
DR   Genevestigator; P51150; -.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0005770; C:late endosome; IDA:MGI.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0045335; C:phagocytic vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Direct protein sequencing; Endosome; GTP-binding;
KW   Lipoprotein; Lysosome; Methylation; Nucleotide-binding;
KW   Phosphoprotein; Prenylation; Protein transport; Transport.
FT   CHAIN         1    207       Ras-related protein Rab-7a.
FT                                /FTId=PRO_0000121122.
FT   NP_BIND      15     22       GTP (By similarity).
FT   NP_BIND      63     67       GTP (By similarity).
FT   NP_BIND     125    128       GTP (By similarity).
FT   MOTIF        37     45       Effector region (By similarity).
FT   MOD_RES      72     72       Phosphoserine.
FT   MOD_RES     183    183       Phosphotyrosine (By similarity).
FT   MOD_RES     207    207       Cysteine methyl ester (By similarity).
FT   LIPID       205    205       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   LIPID       207    207       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   CONFLICT    145    145       S -> R (in Ref. 1; CAA61797).
SQ   SEQUENCE   207 AA;  23490 MW;  A2AF33B16A672971 CRC64;
     MTSRKKVLLK VIILGDSGVG KTSLMNQYVN KKFSNQYKAT IGADFLTKEV MVDDRLVTMQ
     IWDTAGQERF QSLGVAFYRG ADCCVLVFDV TAPNTFKTLD SWRDEFLIQA SPRDPENFPF
     VVLGNKIDLE NRQVATKRAQ AWCYSKNNIP YFETSAKEAI NVEQAFQTIA RNALKQETEV
     ELYNEFPEPI KLDKNDRAKA SAESCSC
//
ID   HEM4_MOUSE              Reviewed;         265 AA.
AC   P51163;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Uroporphyrinogen-III synthase;
DE            Short=UROIIIS;
DE            Short=UROS;
DE            EC=4.2.1.75;
DE   AltName: Full=Hydroxymethylbilane hydrolyase [cyclizing];
DE   AltName: Full=Uroporphyrinogen-III cosynthase;
GN   Name=Uros; Synonyms=Uros3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX   MEDLINE=95331792; PubMed=7607680; DOI=10.1016/0888-7543(95)80175-L;
RA   Xu W., Kozak C.A., Desnick R.J.;
RT   "Uroporphyrinogen-III synthase: molecular cloning, nucleotide
RT   sequence, expression of a mouse full-length cDNA, and its localization
RT   on mouse chromosome 7.";
RL   Genomics 26:556-562(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=95178849; PubMed=7873885; DOI=10.1007/BF00426082;
RA   Bensidhoum M., Ged C.M., Poirier C., Guenet J.-L., de Verneuil H.;
RT   "The cDNA sequence of mouse uroporphyrinogen III synthase and
RT   assignment to mouse chromosome 7.";
RL   Mamm. Genome 5:728-730(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Catalyzes cyclization of the linear tetrapyrrole,
CC       hydroxymethylbilane, to the macrocyclic uroporphyrinogen III, the
CC       branch point for the various sub-pathways leading to the wide
CC       diversity of porphyrins. Porphyrins act as cofactors for a
CC       multitude of enzymes that perform a variety of processes within
CC       the cell such as methionine synthesis (vitamin B12) or oxygen
CC       transport (heme) (By similarity).
CC   -!- CATALYTIC ACTIVITY: Hydroxymethylbilane = uroporphyrinogen III +
CC       H(2)O.
CC   -!- PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis;
CC       coproporphyrinogen-III from 5-aminolevulinate: step 3/4.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SIMILARITY: Belongs to the uroporphyrinogen-III synthase family.
CC   -----------------------------------------------------------------------
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DR   EMBL; U18867; AAA74742.1; -; mRNA.
DR   EMBL; U16216; AAA79978.1; -; mRNA.
DR   EMBL; U04439; AAA81898.1; -; mRNA.
DR   EMBL; BC068161; AAH68161.1; -; mRNA.
DR   IPI; IPI00119087; -.
DR   PIR; A56838; A56838.
DR   RefSeq; NP_033505.1; NM_009479.2.
DR   UniGene; Mm.3160; -.
DR   ProteinModelPortal; P51163; -.
DR   SMR; P51163; 1-260.
DR   STRING; P51163; -.
DR   PRIDE; P51163; -.
DR   Ensembl; ENSMUST00000033276; ENSMUSP00000033276; ENSMUSG00000030979.
DR   Ensembl; ENSMUST00000106145; ENSMUSP00000101751; ENSMUSG00000030979.
DR   Ensembl; ENSMUST00000106146; ENSMUSP00000101752; ENSMUSG00000030979.
DR   GeneID; 22276; -.
DR   KEGG; mmu:22276; -.
DR   UCSC; uc009kdf.1; mouse.
DR   CTD; 22276; -.
DR   MGI; MGI:98917; Uros.
DR   eggNOG; roNOG10846; -.
DR   HOGENOM; HBG675736; -.
DR   HOVERGEN; HBG000492; -.
DR   InParanoid; P51163; -.
DR   OMA; DQIKFAA; -.
DR   OrthoDB; EOG45B1GF; -.
DR   PhylomeDB; P51163; -.
DR   BRENDA; 4.2.1.75; 244.
DR   NextBio; 302397; -.
DR   ArrayExpress; P51163; -.
DR   Bgee; P51163; -.
DR   CleanEx; MM_UROS; -.
DR   Genevestigator; P51163; -.
DR   GermOnline; ENSMUSG00000030979; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0004852; F:uroporphyrinogen-III synthase activity; IDA:MGI.
DR   GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR003754; 4pyrrol_synth_uPrphyn_synth.
DR   Pfam; PF02602; HEM4; 1.
DR   SUPFAM; SSF69618; HEM4_synth; 1.
PE   2: Evidence at transcript level;
KW   Heme biosynthesis; Lyase; Porphyrin biosynthesis.
FT   CHAIN         1    265       Uroporphyrinogen-III synthase.
FT                                /FTId=PRO_0000135252.
SQ   SEQUENCE   265 AA;  28504 MW;  45BD2A6BD709A126 CRC64;
     MKVLLLKDAK EDDSGLDPYI QELRLCGLEA TLIPVLSFEF MSLPSLSEKL SHPEGFGGLI
     FTSPRAVEAV KLCLEKDNKT EAWEKSLKDR WNAKSVYVVG SATASLVNKI GLDAEGAGSG
     NAEKLAEYIC SKPSSELPLL FPCGTIKGDT LPKMLKDKGI PMESMHVYQT VPHPGIQGSL
     KSYYEDQGIP ASITFFSPSG LKYSLEYIQA LSGSSFDQIK FIAIGPSTTR AMAAKGLPVS
     CTAESPTPQA LAAGIRNVLK PNHCC
//
ID   ACADL_MOUSE             Reviewed;         430 AA.
AC   P51174; B2KGC6; O35302; Q8QZR6; Q9CU29; Q9DB83;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 2.
DT   08-MAR-2011, entry version 101.
DE   RecName: Full=Long-chain specific acyl-CoA dehydrogenase, mitochondrial;
DE            Short=LCAD;
DE            EC=1.3.99.13;
DE   Flags: Precursor;
GN   Name=Acadl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=96015043; PubMed=8530022; DOI=10.1006/geno.1995.1127;
RA   Hinsdale M.E., Farmer S.C., Johnson K.R., Davisson M.T., Hamm D.A.,
RA   Tolwani R.J., Wood P.A.;
RT   "RNA expression and chromosomal location of the mouse long-chain acyl-
RT   CoA dehydrogenase gene.";
RL   Genomics 28:163-170(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-201.
RC   STRAIN=129/Sv;
RX   MEDLINE=98213642; PubMed=9545492; DOI=10.1007/s003359900770;
RA   Kurtz D.M., Tolwani R.J., Wood P.A.;
RT   "Structural characterization of the mouse long-chain acyl-CoA
RT   dehydrogenase gene and 5' regulatory region.";
RL   Mamm. Genome 9:361-365(1998).
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA +
CC       reduced acceptor.
CC   -!- COFACTOR: FAD.
CC   -!- PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-
CC       oxidation.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- MISCELLANEOUS: A number of straight-chain acyl-CoA dehydrogenases
CC       of different substrate specificities are present in mammalian
CC       tissues.
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U21489; AAC52329.1; -; mRNA.
DR   EMBL; AK005140; BAB23838.1; -; mRNA.
DR   EMBL; AK018319; BAB31161.1; -; mRNA.
DR   EMBL; CU302198; CAQ52312.1; -; Genomic_DNA.
DR   EMBL; BC027412; AAH27412.1; -; mRNA.
DR   EMBL; AF018437; AAC23587.1; -; Genomic_DNA.
DR   EMBL; AF018433; AAC23587.1; JOINED; Genomic_DNA.
DR   EMBL; AF018435; AAC23587.1; JOINED; Genomic_DNA.
DR   EMBL; AF018436; AAC23587.1; JOINED; Genomic_DNA.
DR   IPI; IPI00119114; -.
DR   RefSeq; NP_031407.2; NM_007381.3.
DR   UniGene; Mm.2445; -.
DR   ProteinModelPortal; P51174; -.
DR   SMR; P51174; 51-426.
DR   STRING; P51174; -.
DR   PhosphoSite; P51174; -.
DR   PRIDE; P51174; -.
DR   Ensembl; ENSMUST00000027153; ENSMUSP00000027153; ENSMUSG00000026003.
DR   GeneID; 11363; -.
DR   KEGG; mmu:11363; -.
DR   UCSC; uc007bir.1; mouse.
DR   CTD; 11363; -.
DR   MGI; MGI:87866; Acadl.
DR   eggNOG; roNOG08008; -.
DR   GeneTree; ENSGT00590000082906; -.
DR   HOGENOM; HBG699365; -.
DR   HOVERGEN; HBG104903; -.
DR   InParanoid; P51174; -.
DR   OrthoDB; EOG4FR0RR; -.
DR   BRENDA; 1.3.99.13; 244.
DR   NextBio; 278636; -.
DR   ArrayExpress; P51174; -.
DR   Bgee; P51174; -.
DR   CleanEx; MM_ACADL; -.
DR   Genevestigator; P51174; -.
DR   GermOnline; ENSMUSG00000026003; Mus musculus.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004466; F:long-chain-acyl-CoA dehydrogenase activity; IMP:BHF-UCL.
DR   GO; GO:0016401; F:palmitoyl-CoA oxidase activity; IMP:BHF-UCL.
DR   GO; GO:0042413; P:carnitine catabolic process; IMP:BHF-UCL.
DR   GO; GO:0019254; P:carnitine metabolic process, CoA-linked; IMP:BHF-UCL.
DR   GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IMP:BHF-UCL.
DR   GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IMP:BHF-UCL.
DR   GO; GO:0046322; P:negative regulation of fatty acid oxidation; IMP:BHF-UCL.
DR   GO; GO:0090181; P:regulation of cholesterol metabolic process; IMP:BHF-UCL.
DR   GO; GO:0001659; P:temperature homeostasis; IMP:BHF-UCL.
DR   InterPro; IPR006089; Acyl-CoA_DH_CS.
DR   InterPro; IPR006092; Acyl-CoA_DH_N.
DR   InterPro; IPR006090; Acyl-CoA_Oxase/DH_1.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR013786; AcylCoA_DH/ox_N.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase.
DR   Gene3D; G3DSA:2.40.110.10; Acyl_CoA_DH/ox_M; 1.
DR   Gene3D; G3DSA:1.10.540.10; AcylCoA_DH/ox_N; 1.
DR   Gene3D; G3DSA:1.20.140.10; AcylCoA_DH_1/2_C; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR   SUPFAM; SSF56645; AcylCoA_dehyd_NM; 1.
DR   SUPFAM; SSF47203; AcylCoADH_C_like; 1.
DR   PROSITE; PS00072; ACYL_COA_DH_1; 1.
DR   PROSITE; PS00073; ACYL_COA_DH_2; 1.
PE   2: Evidence at transcript level;
KW   FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism;
KW   Mitochondrion; Oxidoreductase; Transit peptide.
FT   TRANSIT       1     30       Mitochondrion (By similarity).
FT   CHAIN        31    430       Long-chain specific acyl-CoA
FT                                dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000000511.
FT   CONFLICT     14     15       KA -> RP (in Ref. 1; AAC52329 and 5;
FT                                AAC23587).
FT   CONFLICT     14     14       K -> S (in Ref. 2; BAB23838).
FT   CONFLICT     19     20       PR -> TL (in Ref. 1; AAC52329).
FT   CONFLICT     22     22       P -> L (in Ref. 1; AAC52329 and 2;
FT                                BAB23838).
FT   CONFLICT     25     25       A -> S (in Ref. 1; AAC52329).
FT   CONFLICT     32     32       A -> P (in Ref. 1; AAC52329).
FT   CONFLICT     35     35       R -> G (in Ref. 1; AAC52329).
FT   CONFLICT     47     47       V -> I (in Ref. 1; AAC52329 and 2;
FT                                BAB23838).
FT   CONFLICT     58     58       D -> E (in Ref. 2; BAB31161).
FT   CONFLICT    131    132       GP -> RA (in Ref. 1; AAC52329).
FT   CONFLICT    135    135       S -> T (in Ref. 1; AAC52329).
FT   CONFLICT    225    225       S -> W (in Ref. 1; AAC52329).
SQ   SEQUENCE   430 AA;  47908 MW;  45CFED51640EAFFB CRC64;
     MAARLLLRSL RVLKARSAPR PPPSARCSHS GAEARLETPS AKKLTDVGIR RIFSSEHDIF
     RESVRKFFQE EVIPHHTEWE KAGEVSREVW EKAGKQGLLG INIAEKHGGI GGDLLSTAVT
     WEEQAYSNCT GPGFSLHSDI VMPYIANYGT KEQIEKFIPQ MTAGKCIGAI AMTEPGAGSD
     LQGVRTNAKR SGSDWILNGS KVFITNGWLS DLVIVVAVTN REARSPAHGI SLFLVENGMK
     GFIKGRKLHK MGMKAQDTAE LFFEDVRLPA NALLGEENKG FYYLMQELPQ ERLLIAELAI
     SACEFMFEET RNYVKQRKAF GKTVAHIQTV QHKLAELKTH ICVTRAFVDS CLQLHETKRL
     DSGSASMAKY WASELQNSVA YECVQLHGGW GYMWEYPIAK AYVDARVQPI YGGTNEIMKE
     LIARQIVSDS
//
ID   RL9_MOUSE               Reviewed;         192 AA.
AC   P51410; Q9JK58;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2002, sequence version 2.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=60S ribosomal protein L9;
GN   Name=Rpl9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Cheong C., Lee H.;
RT   "Retinoblastoma(Rb) regulates 60S ribosomal protein L9.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Eye, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, Colon, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 14-185.
RC   STRAIN=C3H/HeN;
RX   MEDLINE=95323681; PubMed=7600302; DOI=10.1016/1074-7613(95)90078-0;
RA   Monach P.A., Meredith S.C., Siegel C.T., Schreiber H.;
RT   "A unique tumor antigen produced by a single amino acid
RT   substitution.";
RL   Immunity 2:45-59(1995).
CC   -!- SIMILARITY: Belongs to the ribosomal protein L6P family.
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DR   EMBL; AF260271; AAF70508.1; -; mRNA.
DR   EMBL; AK012331; BAB28167.1; -; mRNA.
DR   EMBL; AK012445; BAB28244.1; -; mRNA.
DR   EMBL; AK017388; BAB30725.1; -; mRNA.
DR   EMBL; AK017427; BAB30739.1; -; mRNA.
DR   EMBL; AK084278; BAC39154.1; -; mRNA.
DR   EMBL; BC013165; AAH13165.1; -; mRNA.
DR   EMBL; BC081435; AAH81435.1; -; mRNA.
DR   EMBL; BC083166; AAH83166.1; -; mRNA.
DR   EMBL; BC083329; AAH83329.1; -; mRNA.
DR   EMBL; U17332; AAA85686.1; -; mRNA.
DR   EMBL; U17331; AAA85685.1; -; mRNA.
DR   IPI; IPI00122413; -.
DR   RefSeq; NP_035422.1; NM_011292.2.
DR   UniGene; Mm.300271; -.
DR   UniGene; Mm.383918; -.
DR   UniGene; Mm.422908; -.
DR   ProteinModelPortal; P51410; -.
DR   SMR; P51410; 10-184.
DR   STRING; P51410; -.
DR   PhosphoSite; P51410; -.
DR   PRIDE; P51410; -.
DR   Ensembl; ENSMUST00000057885; ENSMUSP00000109399; ENSMUSG00000047215.
DR   Ensembl; ENSMUST00000120094; ENSMUSP00000113704; ENSMUSG00000047215.
DR   GeneID; 20005; -.
DR   KEGG; mmu:20005; -.
DR   UCSC; uc008xno.1; mouse.
DR   CTD; 100042832; -.
DR   CTD; 20005; -.
DR   MGI; MGI:1298373; Rpl9.
DR   eggNOG; roNOG04043; -.
DR   HOGENOM; HBG606796; -.
DR   HOVERGEN; HBG000942; -.
DR   InParanoid; P51410; -.
DR   OMA; CSHIENM; -.
DR   OrthoDB; EOG4T4CWJ; -.
DR   PhylomeDB; P51410; -.
DR   NextBio; 454791; -.
DR   ArrayExpress; P51410; -.
DR   Bgee; P51410; -.
DR   CleanEx; MM_RPL9; -.
DR   Genevestigator; P51410; -.
DR   GermOnline; ENSMUSG00000071269; Mus musculus.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0019843; F:rRNA binding; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR000702; Ribosomal_L6.
DR   InterPro; IPR020040; Ribosomal_L6_a/b-dom.
DR   InterPro; IPR002359; Ribosomal_L6_CS2.
DR   Gene3D; G3DSA:3.90.930.12; Ribosomal_L6; 2.
DR   PANTHER; PTHR11655; Ribosomal_L6; 1.
DR   Pfam; PF00347; Ribosomal_L6; 2.
DR   PIRSF; PIRSF002162; Ribosomal_L6; 1.
DR   SUPFAM; SSF56053; Ribosomal_L6; 2.
DR   PROSITE; PS00700; RIBOSOMAL_L6_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Polymorphism; Ribonucleoprotein; Ribosomal protein;
KW   Tumor antigen.
FT   CHAIN         1    192       60S ribosomal protein L9.
FT                                /FTId=PRO_0000131099.
FT   MOD_RES     121    121       N6-acetyllysine (By similarity).
FT   VARIANT      47     47       L -> H (in UV-induced tumor 6132A
FT                                antigen).
SQ   SEQUENCE   192 AA;  21881 MW;  94948BA07E86BBEB CRC64;
     MKTILSNQTV DIPENVEITL KGRTVIVKGP RGTLRRDFNH INVELSLLGK KKKRLRVDKW
     WGNRKELATV RTICSHVQNM IKGVTLGFRY KMRSVYAHFP INVVIQENGS LVEIRNFLGE
     KYIRRVRMRT GVACSVSQAQ KDELILEGND IELVSNSAAL IQQATTVKNK DIRKFLDGIY
     VSEKGTVQQA DE
//
ID   PLCB3_MOUSE             Reviewed;        1234 AA.
AC   P51432;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3;
DE            EC=3.1.4.11;
DE   AltName: Full=Phosphoinositide phospholipase C-beta-3;
DE   AltName: Full=Phospholipase C-beta-3;
DE            Short=PLC-beta-3;
GN   Name=Plcb3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=BALB/c; TISSUE=Kidney;
RX   MEDLINE=98382438; PubMed=9714794; DOI=10.1016/S0005-2760(98)00074-5;
RA   Wang S., Zhou Y., Lukinius A., Oberg K., Skogseid B., Gobl A.;
RT   "Molecular cloning and characterization of a cDNA encoding mouse
RT   phospholipase C-beta3.";
RL   Biochim. Biophys. Acta 1393:173-178(1998).
CC   -!- FUNCTION: The production of the second messenger molecules
CC       diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is
CC       mediated by activated phosphatidylinositol-specific phospholipase
CC       C enzymes.
CC   -!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-
CC       bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate +
CC       diacylglycerol.
CC   -!- COFACTOR: Calcium (By similarity).
CC   -!- SUBUNIT: Interacts with SHANK2 and LPAR2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Highly expressed in kidney, skeletal muscle,
CC       liver, lung, heart and brain.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 PI-PLC X-box domain.
CC   -!- SIMILARITY: Contains 1 PI-PLC Y-box domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U43144; AAA85199.1; -; mRNA.
DR   IPI; IPI00311203; -.
DR   UniGene; Mm.273204; -.
DR   ProteinModelPortal; P51432; -.
DR   SMR; P51432; 12-883.
DR   IntAct; P51432; 4.
DR   MINT; MINT-126696; -.
DR   STRING; P51432; -.
DR   PhosphoSite; P51432; -.
DR   PRIDE; P51432; -.
DR   Ensembl; ENSMUST00000025912; ENSMUSP00000025912; ENSMUSG00000024960.
DR   MGI; MGI:104778; Plcb3.
DR   eggNOG; roNOG12610; -.
DR   HOGENOM; HBG315986; -.
DR   HOVERGEN; HBG053609; -.
DR   InParanoid; P51432; -.
DR   OrthoDB; EOG41RPT7; -.
DR   PhylomeDB; P51432; -.
DR   BRENDA; 3.1.4.11; 244.
DR   ArrayExpress; P51432; -.
DR   Bgee; P51432; -.
DR   CleanEx; MM_PLCB3; -.
DR   Genevestigator; P51432; -.
DR   GermOnline; ENSMUSG00000024960; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:EC.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR015359; Phospholipase_C_EF-hand-like.
DR   InterPro; IPR001711; Phospholipase_C_Pinositol-sp_Y.
DR   InterPro; IPR001192; Pinositol_Phospholipase-C.
DR   InterPro; IPR016280; PLC-beta.
DR   InterPro; IPR014815; PLC-beta_C.
DR   InterPro; IPR009535; PLC-beta_CS.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Gene3D; G3DSA:3.20.20.190; PLC-like_Pdiesterase_TIM-brl; 2.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF06631; DUF1154; 1.
DR   Pfam; PF09279; efhand_like; 1.
DR   Pfam; PF00388; PI-PLC-X; 1.
DR   Pfam; PF00387; PI-PLC-Y; 1.
DR   Pfam; PF08703; PLC-beta_C; 1.
DR   PIRSF; PIRSF000956; PLC-beta; 1.
DR   PRINTS; PR00390; PHPHLIPASEC.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00148; PLCXc; 1.
DR   SMART; SM00149; PLCYc; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF51695; PLC-like_Pdiesterase_TIM-brl; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Calcium; Hydrolase; Lipid degradation; Nucleus;
KW   Phosphoprotein; Transducer.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1234       1-phosphatidylinositol-4,5-bisphosphate
FT                                phosphodiesterase beta-3.
FT                                /FTId=PRO_0000088492.
FT   DOMAIN      318    468       PI-PLC X-box.
FT   DOMAIN      591    707       PI-PLC Y-box.
FT   DOMAIN      714    811       C2.
FT   REGION     1231   1234       Interaction with SHANK2 (By similarity).
FT   ACT_SITE    332    332       By similarity.
FT   ACT_SITE    379    379       By similarity.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     537    537       Phosphoserine (By similarity).
FT   MOD_RES     927    927       Phosphoserine (By similarity).
FT   MOD_RES     932    932       Phosphoserine (By similarity).
FT   MOD_RES     935    935       Phosphoserine (By similarity).
FT   MOD_RES    1122   1122       Phosphothreonine (By similarity).
SQ   SEQUENCE   1234 AA;  139492 MW;  86195DDB2CC7C255 CRC64;
     MAGARPGVHA LQLEPSTVVK TLRRGSKFIK WDEEASSRNL VTLRVDPNGF FLYWTGPNME
     VDTLDISSIR DTRTGRYARL PKDPKIREVL GFGGPDTRLE EKLMTVVAGP DPVNTTFLNF
     MAVQDDTVKV WSEELFKLAM NILAQNASRN TFLRKAYTKL KLQVNQDGRI PVKNILKMFS
     ADKKRVETAL ESCGLNFNRS ESIRPDEFPL EIFERFLNKL CLRPDIDKIL LEIGAKGKPY
     LTLEQLMDFI NQKQRDPRLN EVLYPPLRSS QARLLIEKYE TNKQFLERDQ MSMEGFSRYL
     GGEENGILPL EALDLSMDMT QPLSAYFINS SHNTYLTAGQ LAGPSSVEMY RQALLWGCRC
     VELDVWKGRP PEEEPFITHG FTMTTEVPLR DVLEAIAEAA FKTSPYPVIL SFENHVDSAK
     QQAKMAEYCR SIFGDALLID PLDKYPLSAG IPLPSPQDLM GRILVKNKKR HRPSTGVPDS
     SVRKRPLEQS NSALSESSAA TEPSSPQLGS PSSDSCPGLS NGEEVGLEKT SLEPQKSLGE
     ESLSREPNVP MPDRDREDEE EDEEEEETTD PKKPTTDEGT ASSEVNATEE MSTLVNYVEP
     VKFKSFEASR KRNKCFEMSS FVETKAMEQL TKSPMEFVEY NKQQLSRIYP KGTRVDSSNY
     MPQLFWNVGC QLVALNFQTL DLPMQLNAGV FEYNGRSGYL LKPEFMRRPD KSFDPFTEVI
     VDGIVANALR VKVISGQFLS DKKVGIYVEV DMFGLPVDTR RKYRTRTSQG NSFNPVWDEE
     PFDFPKVVLP TLASLRIAAF EEGGKFVGHR ILPVSAIRSG YHYVCLRNEA NQPLCLPALL
     IYTEASDYIP DDHQDYAEAL INPIKHVSLM DQRAKQLAAL IGESEAQAST ETYQETPCQQ
     PGSQLPSNPT PNPLDASPRW PPGPTTSSTS SSLSSPGQRD DLIASILSEV TPTPLEELRS
     HKAMVKLRSR QDRDLRELHK KHQRKAVALT RRLLDGLAQA RAEGKCRPSP SALGKATNSE
     DVKEEEEAKQ YREFQNRQVQ SLLELREAQA DVETKRKLEH LRQAHQRLKE VVLDTHTTQF
     KRLKELNERE KKELQKILDR KRNNSISEAK TREKHKKEVE LTEINRRHIT ESVNSIRRLE
     EAQKQRHERL VAGQQQVLQQ LEEEEPKLLA QLTQECQEQR ERLPQEIRRC LLGETAEGLG
     DGPLVACASN GHAPGSGGHL SSADSESQEE NTQL
//
ID   XPC_MOUSE               Reviewed;         930 AA.
AC   P51612; P54732; Q3TKI2; Q920M1; Q9DBW7;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=DNA repair protein complementing XP-C cells homolog;
DE   AltName: Full=Xeroderma pigmentosum group C-complementing protein homolog;
DE   AltName: Full=p125;
GN   Name=Xpc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-930.
RX   MEDLINE=96184849; PubMed=8604333; DOI=10.1093/nar/24.6.1026;
RA   Li L., Peterson C., Legerski R.;
RT   "Sequence of the mouse XPC cDNA and genomic structure of the human XPC
RT   gene.";
RL   Nucleic Acids Res. 24:1026-1028(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yokoi M., Hanaoka F.;
RT   "Molecular cloning of mouse XPC.";
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Lung, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 59-617.
RC   STRAIN=129/Sv;
RX   MEDLINE=95405469; PubMed=7675084; DOI=10.1038/377162a0;
RA   Sands A.T., Abuin A., Sanchez A., Conti C.J., Bradley A.;
RT   "High susceptibility to ultraviolet-induced carcinogenesis in mice
RT   lacking XPC.";
RL   Nature 377:162-165(1995).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-875 AND SER-876, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-395 AND SER-397,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Involved in global genome nucleotide excision repair
CC       (GG-NER) by acting as damage sensing and DNA-binding factor
CC       component of the XPC complex. Has only a low DNA repair activity
CC       by itself which is stimulated by Rad23b and Rad23a. Has a
CC       preference to bind DNA containing a short single-stranded segment
CC       but not to damaged oligonucleotides. This feature is proposed to
CC       be related to a dynamic sensor function: XPC can rapidly screen
CC       duplex DNA for non-hydrogen-bonded bases by forming a transient
CC       nucleoprotein intermediate complex which matures into a stable
CC       recognition complex through an intrinsic single-stranded DNA-
CC       binding activity.
CC   -!- FUNCTION: The XPC complex is proposed to represent the first
CC       factor bound at the sites of DNA damage and together with other
CC       core recognition factors, Xpa, RPA and the TFIIH complex, is part
CC       of the pre-incision (or initial recognition) complex. The XPC
CC       complex recognizes a wide spectrum of damaged DNA characterized by
CC       distortions of the DNA helix such as single-stranded loops,
CC       mismatched bubbles or single stranded overhangs. The orientation
CC       of XPC complex binding appears to be crucial for inducing a
CC       productive NER. XPC complex is proposed to recognize and to
CC       interact with unpaired bases on the undamaged DNA strand which is
CC       followed by recruitment of the TFIIH complex and subsequent
CC       scanning for lesions in the opposite strand in a 5'-to-3'
CC       direction by the NER machinery. Cyclobutane pyrimidine dimers
CC       (CPDs) which are formed upon UV-induced DNA damage esacpe
CC       detection by the XPC complex due to a low degree of structural
CC       perurbation. Instead they are detected by the UV-DDB complex which
CC       in turn recruits and cooperates with the XPC complex in the
CC       respective DNA repair. In vitro, the Xpc:Rad23b dimer is
CC       sufficient to initiate NER; it preferentially binds to cisplatin
CC       and UV-damaged double-stranded DNA and also binds to a variety of
CC       chemically and structurally diverse DNA adducts. XPC:RAD23B
CC       contacts DNA both 5' and 3' of a cisplatin lesion with a
CC       preference for the 5' side. Xpc:Rad23b induces a bend in DNA upon
CC       binding. Xpc:Rad23b stimulates the activity of DNA glycosylases
CC       Tdg and Smug1 (By similarity).
CC   -!- SUBUNIT: Component of the XPC complex composed of XPC, RAD23B and
CC       CETN2. Interacts with RAD23A; the interaction is suggesting the
CC       existence of a functional equivalent variant XPC complex.
CC       Interacts with TDG; the interaction is demonstrated using the
CC       XPC:RAD23B dimer. Interacts with SMUG1; the interaction is
CC       demonstrated using the XPC:RAD23B dimer. Interacts with DDB2.
CC       Interacts with CCNH, GTF2H1 and ERCC3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity). Note=Omnipresent in the nucleus and consistently
CC       associates with and dissociates from DNA in the absence of DNA
CC       damage. Continuously shuttles between the cytoplasm and the
CC       nucleus, which is impeded by the presence of NER lesions (By
CC       similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- PTM: Ubiquitinated upon UV irradiation; the ubiquitination
CC       requires the UV-DDB complex, appears to be reversible and does not
CC       serve as a signal for degradation (By similarity).
CC   -!- SIMILARITY: Belongs to the XPC family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC52500.1; Type=Frameshift; Positions=50, 52, 61;
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DR   EMBL; U27398; AAC52500.1; ALT_FRAME; mRNA.
DR   EMBL; AB071144; BAB64540.1; -; mRNA.
DR   EMBL; AK004713; BAB23497.1; -; mRNA.
DR   EMBL; AK028595; BAC26023.1; -; mRNA.
DR   EMBL; AK166981; BAE39163.1; -; mRNA.
DR   EMBL; U40005; AAA82720.1; -; mRNA.
DR   IPI; IPI00124885; -.
DR   PIR; S70630; S70630.
DR   RefSeq; NP_033557.2; NM_009531.2.
DR   UniGene; Mm.2806; -.
DR   ProteinModelPortal; P51612; -.
DR   SMR; P51612; 522-638.
DR   STRING; P51612; -.
DR   PhosphoSite; P51612; -.
DR   PRIDE; P51612; -.
DR   Ensembl; ENSMUST00000032182; ENSMUSP00000032182; ENSMUSG00000030094.
DR   GeneID; 22591; -.
DR   KEGG; mmu:22591; -.
DR   UCSC; uc009cyd.1; mouse.
DR   CTD; 22591; -.
DR   MGI; MGI:103557; Xpc.
DR   eggNOG; roNOG06165; -.
DR   HOGENOM; HBG506545; -.
DR   HOVERGEN; HBG000407; -.
DR   InParanoid; P51612; -.
DR   OMA; MKRFNKE; -.
DR   OrthoDB; EOG40CHGQ; -.
DR   PhylomeDB; P51612; -.
DR   NextBio; 302933; -.
DR   ArrayExpress; P51612; -.
DR   Bgee; P51612; -.
DR   CleanEx; MM_XPC; -.
DR   Genevestigator; P51612; -.
DR   GermOnline; ENSMUSG00000030094; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0071942; C:XPC complex; ISS:UniProtKB.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0031573; P:intra-S DNA damage checkpoint; IGI:MGI.
DR   GO; GO:0006289; P:nucleotide-excision repair; IDA:MGI.
DR   GO; GO:0010224; P:response to UV-B; IMP:MGI.
DR   InterPro; IPR004583; DNA_repair_Rad4.
DR   InterPro; IPR018326; DNA_repair_Rad4_DNA-bd_1.
DR   InterPro; IPR018327; DNA_repair_Rad4_DNA-bd_2.
DR   InterPro; IPR018328; DNA_repair_Rad4_DNA-bd_3.
DR   InterPro; IPR018026; DNA_repair_Rad4_subg.
DR   InterPro; IPR018325; DNA_repair_Rad4_transGln-dom.
DR   PANTHER; PTHR12135; Rad4; 1.
DR   Pfam; PF10403; BHD_1; 1.
DR   Pfam; PF10404; BHD_2; 1.
DR   Pfam; PF10405; BHD_3; 1.
DR   Pfam; PF03835; Rad4; 1.
DR   TIGRFAMs; TIGR00605; rad4; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; DNA damage; DNA repair; DNA-binding; Nucleus;
KW   Phosphoprotein; Ubl conjugation.
FT   CHAIN         1    930       DNA repair protein complementing XP-C
FT                                cells homolog.
FT                                /FTId=PRO_0000218294.
FT   REGION      489    727       Interaction with RAD23B (By similarity).
FT   REGION      600    759       Minimal sensor domain involved in damage
FT                                recognition (By similarity).
FT   REGION      600    734       DNA-binding; preference for heteroduplex
FT                                DNA (By similarity).
FT   REGION      760    824       DNA-binding; preference for single
FT                                stranded DNA; required for formation of
FT                                stable nucleoprotein complex (By
FT                                similarity).
FT   REGION      809    930       Interaction with ERCC2 and GTF2H1 (By
FT                                similarity).
FT   REGION      840    859       Interaction with CETN2 (By similarity).
FT   MOTIF       388    393       Nuclear localization signal (Potential).
FT   COMPBIAS     27    173       Glu-rich (acidic).
FT   COMPBIAS    355    393       Lys-rich (basic).
FT   COMPBIAS    401    424       Arg/Lys-rich (basic).
FT   COMPBIAS    425    454       Asp/Glu-rich (acidic).
FT   COMPBIAS    459    486       Arg/Lys-rich (basic).
FT   MOD_RES      93     93       Phosphoserine.
FT   MOD_RES     165    165       Phosphothreonine (By similarity).
FT   MOD_RES     343    343       Phosphoserine (By similarity).
FT   MOD_RES     347    347       Phosphoserine (By similarity).
FT   MOD_RES     395    395       Phosphoserine.
FT   MOD_RES     397    397       Phosphoserine.
FT   MOD_RES     875    875       Phosphoserine.
FT   MOD_RES     876    876       Phosphoserine.
FT   MOD_RES     883    883       Phosphoserine (By similarity).
FT   MOD_RES     884    884       Phosphoserine (By similarity).
FT   CONFLICT     13     13       K -> N (in Ref. 2; BAB64540).
FT   CONFLICT     84     84       L -> S (in Ref. 1; AAC52500).
FT   CONFLICT     98     98       F -> L (in Ref. 1; AAC52500).
FT   CONFLICT    101    101       S -> L (in Ref. 1; AAC52500).
FT   CONFLICT    148    149       AT -> CP (in Ref. 2; BAB64540).
FT   CONFLICT    165    166       TP -> RG (in Ref. 1; AAC52500).
FT   CONFLICT    196    201       EVQENM -> GVHEDT (in Ref. 4; AAA82720).
FT   CONFLICT    212    212       S -> N (in Ref. 4; AAA82720).
FT   CONFLICT    218    218       S -> N (in Ref. 4; AAA82720).
FT   CONFLICT    221    223       RQP -> SQL (in Ref. 4; AAA82720).
FT   CONFLICT    373    375       GKA -> AKP (in Ref. 4; AAA82720).
FT   CONFLICT    373    373       G -> GS (in Ref. 1; AAC52500).
FT   CONFLICT    397    397       S -> R (in Ref. 1; AAC52500).
FT   CONFLICT    454    454       E -> K (in Ref. 2; BAB64540).
FT   CONFLICT    458    458       R -> C (in Ref. 4; AAA82720).
FT   CONFLICT    497    497       S -> C (in Ref. 1; AAC52500).
FT   CONFLICT    614    614       E -> K (in Ref. 1; AAC52500).
FT   CONFLICT    621    622       KH -> ND (in Ref. 1; AAC52500).
FT   CONFLICT    683    683       W -> R (in Ref. 1; AAC52500).
FT   CONFLICT    712    715       LSEP -> HLGA (in Ref. 1; AAC52500).
FT   CONFLICT    751    751       N -> K (in Ref. 1; AAC52500).
FT   CONFLICT    777    777       R -> H (in Ref. 1; AAC52500).
FT   CONFLICT    797    797       C -> S (in Ref. 1; AAC52500).
FT   CONFLICT    921    921       A -> P (in Ref. 1; AAC52500).
SQ   SEQUENCE   930 AA;  104522 MW;  0C469AB21B4E4EE9 CRC64;
     MAPKRTADGR RRKRGQKTED NKVARHEESV ADDFEDEKQK PRRKSSFPKV SQGKRKRGCS
     DPGDPTNGAA KKKVAKATAK SKNLKVLKEE ALSDGDDFRD SPADCKKAKK HPKSKVVDQG
     TDEDDSEDDW EEVEELTEPV LDMGENSATS PSDMPVKAVE IEIETPQQAK ERERSEKIKM
     EFETYLRRMM KRFNKEVQEN MHKVHLLCLL ASGFYRNSIC RQPDLLAIGL SIIPIRFTKV
     PLQDRDAYYL SNLVKWFIGT FTVNADLSAS EQDDLQTTLE RRIAIYSARD NEELVHIFLL
     ILRALQLLTR LVLSLQPIPL KSAVTKGRKS SKETSVEGPG GSSELSSNSP ESHNKPTTSR
     RIKEEETLSE GRGKATARGK RGTGTAGSRQ RRKPSCSEGE EAEQKVQGRP HARKRRVAAK
     VSYKEESESD GAGSGSDFEP SSGEGQHSSD EDCEPGPRKQ KRASAPQRTK AGSKSASKTQ
     RGSQCEPSSF PEASSSSSGC KRGKKVSSGA EEMADRKPAG VDQWLEVYCE PQAKWVCVDC
     VHGVVGQPVA CYKYATKPMT YVVGIDSDGW VRDVTQRYDP AWMTATRKCR VDAEWWAETL
     RPYRSLLTER EKKEDQEFQA KHLDQPLPTS ISTYKNHPLY ALKRHLLKFQ AIYPETAAVL
     GYCRGEAVYS RDCVHTLHSR DTWLKQARVV RLGEVPYKMV KGFSNRARKA RLSEPQLHDH
     NDLGLYGHWQ TEEYQPPIAV DGKVPRNEFG NVYLFLPSMM PVGCVQMTLP NLNRVARKLG
     IDCVQAITGF DFHGGYCHPV TDGYIVCEEF RDVLLAAWEN EQAIIEKKEK EKKEKRALGN
     WKLLVRGLLI RERLKLRYGA KSEAAAPHAA GGGLSSDEEE GTSSQAEAAR VLAASWPQNR
     EDPEQKSEYT KMTRKRRAAE ASHLFPFEKL
//
ID   DHB4_MOUSE              Reviewed;         735 AA.
AC   P51660; Q9DBM3;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Peroxisomal multifunctional enzyme type 2;
DE            Short=MFE-2;
DE   AltName: Full=17-beta-hydroxysteroid dehydrogenase 4;
DE            Short=17-beta-HSD 4;
DE   AltName: Full=D-bifunctional protein;
DE            Short=DBP;
DE   AltName: Full=Multifunctional protein 2;
DE            Short=MPF-2;
DE   Contains:
DE     RecName: Full=(3R)-hydroxyacyl-CoA dehydrogenase;
DE              EC=1.1.1.n12;
DE   Contains:
DE     RecName: Full=Enoyl-CoA hydratase 2;
DE              EC=4.2.1.107;
DE              EC=4.2.1.119;
DE     AltName: Full=3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA hydratase;
GN   Name=Hsd17b4; Synonyms=Edh17b4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96135300; PubMed=8547180; DOI=10.1016/0960-0760(95)00204-9;
RA   Normand T., Husen B., Leenders F., Pelczar H., Baert J.-L., Begue A.,
RA   Flourens A.C., Adamski J., de Launoit Y.;
RT   "Molecular characterization of mouse 17 beta-hydroxysteroid
RT   dehydrogenase IV.";
RL   J. Steroid Biochem. Mol. Biol. 55:541-548(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Amnion, Liver, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-662, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION AT SER-3,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Bifunctional enzyme acting on the peroxisomal beta-
CC       oxidation pathway for fatty acids. Catalyzes the formation of 3-
CC       ketoacyl-CoA intermediates from both straight-chain and 2-methyl-
CC       branched-chain fatty acids (By similarity).
CC   -!- CATALYTIC ACTIVITY: (R)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
CC       + NADH.
CC   -!- CATALYTIC ACTIVITY: (24R,25R)-3-alpha,7-alpha,12-alpha,24-
CC       tetrahydroxy-5-beta-cholestanoyl-CoA = (24E)-3-alpha,7-alpha,12-
CC       alpha-trihydroxy-5-beta-cholest-24-enoyl-CoA + H(2)O.
CC   -!- CATALYTIC ACTIVITY: (3R)-3-hydroxyacyl-CoA = (2E)-2-enoyl-CoA +
CC       H(2)O.
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Peroxisome (By similarity).
CC   -!- TISSUE SPECIFICITY: Present in many tissues with highest
CC       concentrations in liver and kidney.
CC   -!- MISCELLANEOUS: The protein is found both as a full length peptide
CC       and in a cleaved version (By similarity).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
CC   -!- SIMILARITY: Contains 1 MaoC-like domain.
CC   -!- SIMILARITY: Contains 1 SCP2 domain.
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DR   EMBL; X89998; CAA62015.1; -; mRNA.
DR   EMBL; AK004866; BAB23627.1; -; mRNA.
DR   EMBL; AK088381; BAC40317.1; -; mRNA.
DR   EMBL; AK166801; BAE39029.1; -; mRNA.
DR   EMBL; AK167060; BAE39222.1; -; mRNA.
DR   EMBL; AK169077; BAE40862.1; -; mRNA.
DR   EMBL; BC022175; AAH22175.1; -; mRNA.
DR   IPI; IPI00331628; -.
DR   RefSeq; NP_032318.2; NM_008292.3.
DR   UniGene; Mm.277857; -.
DR   ProteinModelPortal; P51660; -.
DR   SMR; P51660; 3-303, 322-604, 621-735.
DR   STRING; P51660; -.
DR   PhosphoSite; P51660; -.
DR   PRIDE; P51660; -.
DR   Ensembl; ENSMUST00000025385; ENSMUSP00000025385; ENSMUSG00000024507.
DR   GeneID; 15488; -.
DR   KEGG; mmu:15488; -.
DR   UCSC; uc008eww.1; mouse.
DR   CTD; 15488; -.
DR   MGI; MGI:105089; Hsd17b4.
DR   eggNOG; roNOG06907; -.
DR   HOGENOM; HBG327812; -.
DR   HOVERGEN; HBG002174; -.
DR   InParanoid; P51660; -.
DR   OMA; AKVLHGE; -.
DR   OrthoDB; EOG4255S8; -.
DR   PhylomeDB; P51660; -.
DR   BRENDA; 1.1.1.35; 244.
DR   BRENDA; 4.2.1.107; 244.
DR   NextBio; 288358; -.
DR   ArrayExpress; P51660; -.
DR   Bgee; P51660; -.
DR   CleanEx; MM_HSD17B4; -.
DR   Genevestigator; P51660; -.
DR   GermOnline; ENSMUSG00000024507; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005777; C:peroxisome; IDA:MGI.
DR   GO; GO:0003857; F:3-hydroxyacyl-CoA dehydrogenase activity; IEA:EC.
DR   GO; GO:0033989; F:3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase activity; IEA:EC.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032934; F:sterol binding; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IMP:MGI.
DR   GO; GO:0060009; P:Sertoli cell development; IMP:MGI.
DR   GO; GO:0000038; P:very long-chain fatty acid metabolic process; IMP:MGI.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   InterPro; IPR002539; MaoC_deHydtase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR003033; SCP2_sterol-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   Pfam; PF01575; MaoC_dehydratas; 1.
DR   Pfam; PF02036; SCP2; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF55718; SCP2; 1.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Fatty acid metabolism; Isomerase; Lipid metabolism;
KW   Lyase; NAD; Oxidoreductase; Peroxisome; Phosphoprotein.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    735       Peroxisomal multifunctional enzyme type
FT                                2.
FT                                /FTId=PRO_0000054584.
FT   CHAIN         2    311       (3R)-hydroxyacyl-CoA dehydrogenase.
FT                                /FTId=PRO_0000400084.
FT   CHAIN       312    735       Enoyl-CoA hydratase 2.
FT                                /FTId=PRO_0000400085.
FT   DOMAIN      483    599       MaoC-like.
FT   DOMAIN      623    735       SCP2.
FT   NP_BIND      13     37       NAD (By similarity).
FT   NP_BIND      75     76       NAD (By similarity).
FT   NP_BIND     164    168       NAD (By similarity).
FT   NP_BIND     196    199       NAD (By similarity).
FT   REGION        2    305       (3R)-hydroxyacyl-CoA dehydrogenase.
FT   REGION      321    621       Enoyl-CoA hydratase 2.
FT   REGION      405    406       (3R)-3-hydroxydecanoyl-CoA binding (By
FT                                similarity).
FT   REGION      509    514       (3R)-3-hydroxydecanoyl-CoA binding (By
FT                                similarity).
FT   MOTIF       733    735       Microbody targeting signal (Potential).
FT   ACT_SITE    164    164       Proton acceptor (By similarity).
FT   BINDING      21     21       NAD; via amide nitrogen (By similarity).
FT   BINDING      40     40       NAD (By similarity).
FT   BINDING      99     99       NAD; via carbonyl oxygen (By similarity).
FT   BINDING     151    151       Substrate (By similarity).
FT   BINDING     434    434       (3R)-3-hydroxydecanoyl-CoA (By
FT                                similarity).
FT   BINDING     532    532       (3R)-3-hydroxydecanoyl-CoA; via amide
FT                                nitrogen (By similarity).
FT   BINDING     562    562       (3R)-3-hydroxydecanoyl-CoA; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING     705    705       Substrate (By similarity).
FT   BINDING     723    723       Substrate (By similarity).
FT   MOD_RES       2      2       N-acetylalanine.
FT   MOD_RES       3      3       Phosphoserine.
FT   MOD_RES     265    265       Phosphothreonine (By similarity).
FT   MOD_RES     292    292       Phosphothreonine (By similarity).
FT   MOD_RES     304    304       Phosphoserine (By similarity).
FT   MOD_RES     308    308       Phosphoserine.
FT   MOD_RES     564    564       N6-acetyllysine (By similarity).
FT   MOD_RES     662    662       N6-acetyllysine.
FT   MOD_RES     668    668       N6-acetyllysine (By similarity).
FT   MOD_RES     706    706       N6-acetyllysine (By similarity).
FT   CONFLICT     17     17       A -> P (in Ref. 1; CAA62015).
FT   CONFLICT    417    417       P -> L (in Ref. 1; CAA62015).
SQ   SEQUENCE   735 AA;  79482 MW;  AD7804FE93EB9BA8 CRC64;
     MASPLRFDGR VVLVTGAGGG LGRAYALAFA ERGALVIVND LGGDFKGIGK GSSAADKVVA
     EIRRKGGKAV ANYDSVEAGE KLVKTALDTF GRIDVVVNNA GILRDRSFSR ISDEDWDIIH
     RVHLRGSFQV TRAAWDHMKK QNYGRILMTS SASGIYGNFG QANYSAAKLG ILGLCNTLAI
     EGRKNNIHCN TIAPNAGSRM TETVLPEDLV EALKPEYVAP LVLWLCHESC EENGGLFEVG
     AGWIGKLRWE RTLGAIVRKR NQPMTPEAVR DNWEKICDFS NASKPQTIQE STGGIVEVLH
     KVDSEGISPN RTSHAAPAAT SGFVGAVGHK LPSFSSSYTE LQSIMYALGV GASVKNPKDL
     KFVYEGSADF SCLPTFGVIV AQKSMMNGGL AEVPGLSFNF AKALHGEQYL ELYKPLPRSG
     ELKCEAVIAD ILDKGSGVVI VMDVYSYSGK ELICYNQFSV FVVGSGGFGG KRTSEKLKAA
     VAVPNRPPDA VLRDATSLNQ AALYRLSGDW NPLHIDPDFA SVAGFEKPIL HGLCTFGFSA
     RHVLQQFADN DVSRFKAIKV RFAKPVYPGQ TLQTEMWKEG NRIHFQTKVH ETGDVVISNA
     YVDLVPASGV STQTPSEGGE LQSALVFGEI GRRLKSVGRE VVKKANAVFE WHITKGGTVA
     AKWTIDLKSG SGEVYQGPAK GSADVTIIIS DEDFMEVVFG KLDPQKAFFS GRLKARGNIM
     LSQKLQMILK DYAKL
//
ID   ADCY9_MOUSE             Reviewed;        1353 AA.
AC   P51830; Q61279;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Adenylate cyclase type 9;
DE            EC=4.6.1.1;
DE   AltName: Full=ATP pyrophosphate-lyase 9;
DE   AltName: Full=Adenylate cyclase type IX;
DE   AltName: Full=Adenylyl cyclase 9;
DE   AltName: Full=Adenylyl cyclase type 10;
DE            Short=ACTP10;
GN   Name=Adcy9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=96278831; PubMed=8662814; DOI=10.1074/jbc.271.23.13900;
RA   Premont R.T., Matsuoka I., Mattei M.-G., Pouille Y., Defer N.,
RA   Hanoune J.;
RT   "Identification and characterization of a widely expressed form of
RT   adenylyl cyclase.";
RL   J. Biol. Chem. 271:13900-13907(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96024597; PubMed=7575502; DOI=10.1006/bbrc.1995.2385;
RA   Paterson J.M., Smith S.M., Harmar A.J., Antoni F.A.;
RT   "Control of a novel adenylyl cyclase by calcineurin.";
RL   Biochem. Biophys. Res. Commun. 214:1000-1008(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1106-1193.
RX   MEDLINE=95097788; PubMed=7528319; DOI=10.1016/0076-6879(94)38011-2;
RA   Premont R.T.;
RT   "Identification of adenylyl cyclases by amplification using degenerate
RT   primers.";
RL   Methods Enzymol. 238:116-127(1994).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610 AND SER-613, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-608; SER-610 AND
RP   SER-613, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: May play a fundamental role in situations where fine
CC       interplay between intracellular calcium and cAMP determines the
CC       cellular function. May be a physiologically relevant docking site
CC       for calcineurin.
CC   -!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
CC   -!- COFACTOR: Binds 2 magnesium ions per subunit.
CC   -!- ENZYME REGULATION: Insensitive to calcium/calmodulin. Stimulated
CC       by magnesium, forskolin and mutationally activated G protein (GS)-
CC       alpha. Regulated by calcineurin.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Found in decreasing order in skeletal muscle,
CC       heart, adrenal gland, ovary and brain; and to a lesser extent, in
CC       kidney, liver, testis, lung, thymus and spleen.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
CC       cyclase family.
CC   -!- SIMILARITY: Contains 2 guanylate cyclase domains.
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DR   EMBL; U30602; AAC52603.1; -; mRNA.
DR   EMBL; Z50190; CAA90570.1; -; mRNA.
DR   IPI; IPI00313750; -.
DR   PIR; JC4279; JC4279.
DR   RefSeq; NP_033754.2; NM_009624.2.
DR   UniGene; Mm.439750; -.
DR   ProteinModelPortal; P51830; -.
DR   SMR; P51830; 380-572, 1050-1243.
DR   STRING; P51830; -.
DR   PhosphoSite; P51830; -.
DR   PRIDE; P51830; -.
DR   Ensembl; ENSMUST00000005719; ENSMUSP00000005719; ENSMUSG00000005580.
DR   Ensembl; ENSMUST00000117801; ENSMUSP00000113498; ENSMUSG00000005580.
DR   GeneID; 11515; -.
DR   KEGG; mmu:11515; -.
DR   UCSC; uc007xzq.1; mouse.
DR   CTD; 11515; -.
DR   MGI; MGI:108450; Adcy9.
DR   eggNOG; roNOG10512; -.
DR   HOGENOM; HBG381659; -.
DR   HOVERGEN; HBG050459; -.
DR   InParanoid; P51830; -.
DR   OMA; NTAKYSE; -.
DR   OrthoDB; EOG4CRKZB; -.
DR   PhylomeDB; P51830; -.
DR   BRENDA; 4.6.1.1; 244.
DR   NextBio; 278930; -.
DR   ArrayExpress; P51830; -.
DR   Bgee; P51830; -.
DR   CleanEx; MM_ADCY9; -.
DR   Genevestigator; P51830; -.
DR   GermOnline; ENSMUSG00000005580; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; TAS:MGI.
DR   GO; GO:0004016; F:adenylate cyclase activity; TAS:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:MGI.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   Gene3D; G3DSA:3.30.70.1230; A/G_cyclase; 2.
DR   Pfam; PF00211; Guanylate_cyc; 2.
DR   SMART; SM00044; CYCc; 2.
DR   SUPFAM; SSF55073; A/G_cyclase; 2.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 2.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; cAMP biosynthesis; Glycoprotein; Lyase; Magnesium;
KW   Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Repeat;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1   1353       Adenylate cyclase type 9.
FT                                /FTId=PRO_0000195709.
FT   TOPO_DOM      1    117       Cytoplasmic (Potential).
FT   TRANSMEM    118    138       Helical; (Potential).
FT   TOPO_DOM    139    141       Extracellular (Potential).
FT   TRANSMEM    142    162       Helical; (Potential).
FT   TOPO_DOM    163    171       Cytoplasmic (Potential).
FT   TRANSMEM    172    192       Helical; (Potential).
FT   TOPO_DOM    193    215       Extracellular (Potential).
FT   TRANSMEM    216    235       Helical; (Potential).
FT   TOPO_DOM    236    241       Cytoplasmic (Potential).
FT   TRANSMEM    242    259       Helical; (Potential).
FT   TOPO_DOM    260    280       Extracellular (Potential).
FT   TRANSMEM    281    301       Helical; (Potential).
FT   TOPO_DOM    302    786       Cytoplasmic (Potential).
FT   TRANSMEM    787    807       Helical; (Potential).
FT   TOPO_DOM    808    818       Extracellular (Potential).
FT   TRANSMEM    819    839       Helical; (Potential).
FT   TOPO_DOM    840    867       Cytoplasmic (Potential).
FT   TRANSMEM    868    888       Helical; (Potential).
FT   TOPO_DOM    889    891       Extracellular (Potential).
FT   TRANSMEM    892    912       Helical; (Potential).
FT   TOPO_DOM    913    920       Cytoplasmic (Potential).
FT   TRANSMEM    921    941       Helical; (Potential).
FT   TOPO_DOM    942    975       Extracellular (Potential).
FT   TRANSMEM    976    996       Helical; (Potential).
FT   TOPO_DOM    997   1353       Cytoplasmic (Potential).
FT   METAL       399    399       Magnesium 1 (By similarity).
FT   METAL       399    399       Magnesium 2 (By similarity).
FT   METAL       400    400       Magnesium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       443    443       Magnesium 1 (By similarity).
FT   METAL       443    443       Magnesium 2 (By similarity).
FT   MOD_RES     354    354       Phosphoserine (By similarity).
FT   MOD_RES     357    357       Phosphoserine (By similarity).
FT   MOD_RES     365    365       Phosphoserine (By similarity).
FT   MOD_RES     608    608       Phosphothreonine.
FT   MOD_RES     610    610       Phosphoserine.
FT   MOD_RES     613    613       Phosphoserine.
FT   MOD_RES    1259   1259       Phosphoserine (By similarity).
FT   CARBOHYD    206    206       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    955    955       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    964    964       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    893    893       H -> Q (in Ref. 2; CAA90570).
FT   CONFLICT   1192   1192       N -> D (in Ref. 3; no nucleotide entry).
FT   CONFLICT   1305   1305       R -> H (in Ref. 2; CAA90570).
SQ   SEQUENCE   1353 AA;  150954 MW;  C65736A8304F689E CRC64;
     MASSPHQQLL HHHSTEVSCD SSGDSNSVRV KINPKQLSSN THPKHCKYSI SSSCSSSGDS
     GGLPRRVGGG GRLRRQKKLP QLFERASSRW WDPKFDSMNL EEACLERCFP QTQRRFRYAL
     FYVGFACLLW SIYFAVHMKS KVIVMVVPAL CFLVVCVGFF LFTFTKLYAR HYAWTSLALT
     LLVFALTLAA QFQVWTPLSG RVDSSNHTLT ATPADTCLSQ VGSFSICIEV LLLLYTVMQL
     PLYLSLFLGV VYSVLFETFG YHFRNEDCYP SPGPGALHWE LLSRALLHVC IHAIGIHLFV
     MSQVRSRSTF LKVGQSIMHG KDLEVEKALK ERMIHSVMPR IIADDLMKQG DEESENSVKR
     HATSSPKNRK KKSSIQKAPI AFRPFKMQQI EEVSILFADI VGFTKMSANK SAHALVGLLN
     DLFGRFDRLC EQTKCEKIST LGDCYYCVAG CPEPRADHAY CCIEMGLGMI KAIEQFCQEK
     KEMVNMRVGV HTGTVLCGIL GMRRFKFDVW SNDVNLANLM EQLGVAGKVH ISEATAKYLD
     DRYEMEDGRV IERLGQSVVA DQLKGLKTYL ISGQRAKESH CSCAEALLSG FEVIDDSRES
     SGPRGQGTAS PGSVSDLAQT VKTFDNLKTC PSCGITFAPK SEAGAEGGTV QNGCQDEPKT
     STKASGGPNS KTQNGLLSPP AEEKLTNSQT SLCEILQEKG RWAGVSLDQS ALLPLRFKNI
     REKTDAHFVD VIKEDSLMKD YFFKPPINQF SLNFLDQELE RSYRTSYQEE VIKNSPVKTF
     ASATFSSLLD VFLSTTVFLI LSITCFLKYG ATATPPPPAA LAVFGADLLL EVLSLIVSIR
     MVFFLEDVMT CTKWLLEWIA GWLPRHCIGA ILVSLPALAV YSHITSEFET NIHVTMFTGS
     AVLVAVVHYC NFCQLSSWMR SSLATIVGAG LLLLLHISLC QDSSIVMSPL DSAQNFSAQR
     NPCNSSVLQD GRRPASLIGK ELILTFFLLL LLVWFLNREF EVSYRLHYHG DVEADLHRTK
     IQSMRDQADW LLRNIIPYHV AEQLKVSQTY SKNHDSGGVI FASIVNFSEF YEENYEGGKE
     CYRVLNELIG DFDELLSKPD YNSIEKIKTI GATYMAASGL NTAQCQEGGH PQEHLRILFE
     FAKEMMRVVD DFNNNMLWFN FKLRVGFNHG PLTAGVIGTT KLLYDIWGDT VNIASRMDTT
     GVECRIQVSE ESYRVLSKMG YDFDYRGTVN VKGKGQMKTY LYPKCTDNGV VPQHQLSISP
     DIRVQVDGSI GRSPTDEIAN LVPSVQYSDK ASLGSDDSTQ AKEARLSSKR SWREPVKAEE
     RFPFGKAIEK DSCEDIGVEE ASELSKLNVS KSV
//
ID   HDGF_MOUSE              Reviewed;         237 AA.
AC   P51859; Q8BPG7; Q9CYA4; Q9JK87;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-2002, sequence version 2.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Hepatoma-derived growth factor;
DE            Short=HDGF;
GN   Name=Hdgf; Synonyms=Tdrm1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Testis;
RX   MEDLINE=97445118; PubMed=9299445; DOI=10.1006/bbrc.1997.7233;
RA   Izumoto Y., Kuroda T., Harada H., Kishimoto T., Nakamura H.;
RT   "Hepatoma-derived growth factor belongs to a gene family in mice
RT   showing significant homology in the amino terminus.";
RL   Biochem. Biophys. Res. Commun. 238:26-32(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Thymus;
RA   Zhao Y., Chen W., Wang Y.;
RT   "Cloning of novel gene related to thymus development.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133 AND
RP   SER-165, AND MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-202 AND
RP   SER-206, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; SER-132 AND
RP   SER-133, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; SER-132; SER-133
RP   AND SER-202, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133 AND
RP   SER-165, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; SER-132; SER-133
RP   AND SER-165, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Heparin-binding protein, with mitogenic activity for
CC       fibroblasts. Acts as a transcriptional repressor (By similarity).
CC   -!- SUBUNIT: Monomer, and domain-swapped homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in testis and skeletal
CC       muscle, to intermediate extents in heart, brain, lung, liver, and
CC       kidney, and to a minimal extent in spleen.
CC   -!- DOMAIN: The PWWP domain harbors the heparin-binding sites and is
CC       responsible for DNA-binding, while the C-terminal region is
CC       essentially unstructured (By similarity).
CC   -!- PTM: Sumoylated by SUMO1. Sumoylation prevents binding to
CC       chromatin (By similarity).
CC   -!- SIMILARITY: Belongs to the HDGF family.
CC   -!- SIMILARITY: Contains 1 PWWP domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D63707; BAA09838.1; -; mRNA.
DR   EMBL; AF251787; AAF65469.1; -; mRNA.
DR   EMBL; AK017863; BAB30979.1; -; mRNA.
DR   EMBL; AK029475; BAC26466.1; -; mRNA.
DR   EMBL; AK076021; BAC36126.1; -; mRNA.
DR   EMBL; BC005713; AAH05713.1; -; mRNA.
DR   EMBL; BC021654; AAH21654.1; -; mRNA.
DR   IPI; IPI00313817; -.
DR   PIR; JC5660; JC5660.
DR   RefSeq; NP_032257.3; NM_008231.4.
DR   UniGene; Mm.292208; -.
DR   ProteinModelPortal; P51859; -.
DR   SMR; P51859; 1-109.
DR   STRING; P51859; -.
DR   PhosphoSite; P51859; -.
DR   PRIDE; P51859; -.
DR   Ensembl; ENSMUST00000005017; ENSMUSP00000005017; ENSMUSG00000004897.
DR   GeneID; 15191; -.
DR   KEGG; mmu:15191; -.
DR   UCSC; uc008ptc.1; mouse.
DR   CTD; 15191; -.
DR   MGI; MGI:1194494; Hdgf.
DR   eggNOG; roNOG16577; -.
DR   GeneTree; ENSGT00530000063013; -.
DR   HOGENOM; HBG714869; -.
DR   HOVERGEN; HBG010574; -.
DR   InParanoid; P51859; -.
DR   OMA; SEPSSGR; -.
DR   OrthoDB; EOG4PK28W; -.
DR   NextBio; 287715; -.
DR   PMAP-CutDB; P51859; -.
DR   ArrayExpress; P51859; -.
DR   Bgee; P51859; -.
DR   CleanEx; MM_HDGF; -.
DR   Genevestigator; P51859; -.
DR   GermOnline; ENSMUSG00000004897; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR000313; PWWP.
DR   Pfam; PF00855; PWWP; 1.
DR   SMART; SM00293; PWWP; 1.
DR   PROSITE; PS50812; PWWP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; DNA-binding; Growth factor; Heparin-binding;
KW   Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN         1    237       Hepatoma-derived growth factor.
FT                                /FTId=PRO_0000191701.
FT   DOMAIN       12     69       PWWP.
FT   MOTIF        75     80       Nuclear localization signal (By
FT                                similarity).
FT   MOTIF       155    170       Bipartite nuclear localization signal (By
FT                                similarity).
FT   COMPBIAS    111    227       Glu-rich.
FT   BINDING      19     19       Heparin (By similarity).
FT   BINDING      21     21       Heparin (By similarity).
FT   BINDING      72     72       Heparin (By similarity).
FT   BINDING      75     75       Heparin (By similarity).
FT   BINDING      79     79       Heparin (By similarity).
FT   BINDING      80     80       Heparin (By similarity).
FT   MOD_RES      44     44       N6-acetyllysine (By similarity).
FT   MOD_RES     107    107       Phosphoserine (By similarity).
FT   MOD_RES     128    128       Phosphoserine.
FT   MOD_RES     132    132       Phosphoserine.
FT   MOD_RES     133    133       Phosphoserine.
FT   MOD_RES     165    165       Phosphoserine.
FT   MOD_RES     199    199       Phosphoserine.
FT   MOD_RES     200    200       Phosphothreonine (By similarity).
FT   MOD_RES     202    202       Phosphoserine.
FT   MOD_RES     206    206       Phosphoserine.
FT   MOD_RES     236    236       Phosphoserine (By similarity).
FT   CROSSLNK     80     80       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CONFLICT    118    118       A -> D (in Ref. 3; BAB30979).
FT   CONFLICT    190    190       P -> H (in Ref. 1; BAA09838).
FT   CONFLICT    229    229       Q -> E (in Ref. 3; BAC36126).
FT   CONFLICT    229    229       Q -> P (in Ref. 1; BAA09838).
SQ   SEQUENCE   237 AA;  26269 MW;  AAE4CF574DA4733F CRC64;
     MSRSNRQKEY KCGDLVFAKM KGYPHWPARI DEMPEAAVKS TANKYQVFFF GTHETAFLGP
     KDLFPYEESK EKFGKPNKRK GFSEGLWEIE NNPTVKASGY QSSQKKSCAA EPEVEPEAHE
     GDGDKKGSAE GSSDEEGKLV IDEPAKEKNE KGTLKRRAGD VLEDSPKRPK ESGDHEEEDK
     EIAALEGERP LPVEVEKNST PSEPDSGQGP PAEEEEGEEE AAKEEAEAQG VRDHESL
//
ID   VA0D1_MOUSE             Reviewed;         351 AA.
AC   P51863; Q54A57; Q9QWJ2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=V-type proton ATPase subunit d 1;
DE            Short=V-ATPase subunit d 1;
DE   AltName: Full=P39;
DE   AltName: Full=Physophilin;
DE   AltName: Full=V-ATPase 40 kDa accessory protein;
DE   AltName: Full=V-ATPase AC39 subunit;
DE   AltName: Full=Vacuolar proton pump subunit d 1;
GN   Name=Atp6v0d1; Synonyms=Atp6d;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Howell M.L., Dean G.E.;
RT   "cDNA sequences for mouse vacuolar ATPase subunits.";
RL   Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=98424106; PubMed=9753184;
RX   DOI=10.1046/j.1460-9568.1998.00130.x;
RA   Carrion-Vazquez M., Fernandez A.M., Chowen J., Nieto-Sampedro M.;
RT   "Brain Ac39/physophilin: cloning, coexpression and colocalization with
RT   synaptophysin.";
RL   Eur. J. Neurosci. 10:1153-1166(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=22415104; PubMed=12527205; DOI=10.1016/S0378-1119(02)01099-5;
RA   Sun-Wada G.-H., Yoshimizu T., Imai-Senga Y., Wada Y., Futai M.;
RT   "Diversity of mouse proton-translocating ATPase: presence of multiple
RT   isoforms of the C, d and G subunits.";
RL   Gene 302:147-153(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PROTEIN SEQUENCE OF 25-73; 87-128; 188-237; 240-288; 294-300; 304-320;
RP   328-339 AND 344-351, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   MEDLINE=22982528; PubMed=12963731; DOI=10.1074/jbc.M303924200;
RA   Nishi T., Kawasaki-Nishi S., Forgac M.;
RT   "Expression and function of the mouse V-ATPase d subunit isoforms.";
RL   J. Biol. Chem. 278:46396-46402(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-270, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Subunit of the integral membrane V0 complex of vacuolar
CC       ATPase. Vacuolar ATPase is responsible for acidifying a variety of
CC       intracellular compartments in eukaryotic cells, thus providing
CC       most of the energy required for transport processes in the
CC       vacuolar system. May play a role in coupling of proton transport
CC       and ATP hydrolysis.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.31 mM for ATP;
CC   -!- SUBUNIT: V-ATPase is an heteromultimeric enzyme composed of a
CC       peripheral catalytic V1 complex (components A to H) attached to an
CC       integral membrane V0 proton pore complex (components: a, c, c',
CC       c'' and d).
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout early development.
CC   -!- SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family.
CC   -----------------------------------------------------------------------
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DR   EMBL; U13840; AAC83085.1; -; mRNA.
DR   EMBL; U21549; AAA92288.1; -; mRNA.
DR   EMBL; AB088408; BAC57954.1; -; mRNA.
DR   EMBL; AK083372; BAC38889.1; -; mRNA.
DR   EMBL; AK171515; BAE42500.1; -; mRNA.
DR   IPI; IPI00313841; -.
DR   RefSeq; NP_038505.2; NM_013477.3.
DR   UniGene; Mm.17708; -.
DR   ProteinModelPortal; P51863; -.
DR   STRING; P51863; -.
DR   PhosphoSite; P51863; -.
DR   PRIDE; P51863; -.
DR   Ensembl; ENSMUST00000013304; ENSMUSP00000013304; ENSMUSG00000013160.
DR   GeneID; 11972; -.
DR   KEGG; mmu:11972; -.
DR   UCSC; uc009ndg.1; mouse.
DR   CTD; 11972; -.
DR   MGI; MGI:1201778; Atp6v0d1.
DR   eggNOG; roNOG08793; -.
DR   HOGENOM; HBG317755; -.
DR   HOVERGEN; HBG018065; -.
DR   InParanoid; P51863; -.
DR   OMA; TWIAECI; -.
DR   OrthoDB; EOG4T4CVN; -.
DR   PhylomeDB; P51863; -.
DR   BRENDA; 3.6.3.14; 244.
DR   NextBio; 280095; -.
DR   ArrayExpress; P51863; -.
DR   Bgee; P51863; -.
DR   CleanEx; MM_ATP6V0D1; -.
DR   Genevestigator; P51863; -.
DR   GermOnline; ENSMUSG00000013160; Mus musculus.
DR   GO; GO:0005769; C:early endosome; IDA:MGI.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0008553; F:hydrogen-exporting ATPase activity, phosphorylative mechanism; IDA:MGI.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR016727; ATPase_V0-cplx_dsu.
DR   InterPro; IPR002843; ATPase_V0/A0-cplx_csu/dsu.
DR   Pfam; PF01992; vATP-synt_AC39; 1.
DR   PIRSF; PIRSF018497; V-ATP_synth_D; 1.
DR   SUPFAM; SSF103486; ATPase_V0/A0_c/d; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrogen ion transport; Ion transport;
KW   Phosphoprotein; Transport.
FT   CHAIN         1    351       V-type proton ATPase subunit d 1.
FT                                /FTId=PRO_0000119351.
FT   MOD_RES     270    270       Phosphotyrosine.
FT   MOD_RES     283    283       Phosphoserine.
FT   CONFLICT     23     23       L -> M (in Ref. 1; AAC83085).
SQ   SEQUENCE   351 AA;  40301 MW;  62CDF67B982124C9 CRC64;
     MSFFPELYFN VDNGYLEGLV RGLKAGVLSQ ADYLNLVQCE TLEDLKLHLQ STDYGNFLAN
     EASPLTVSVI DDKLKEKMVV EFRHMRNHAY EPLASFLDFI TYSYMIDNVI LLITGTLHQR
     SIAELVPKCH PLGSFEQMEA VNIAQTPAEL YNAILVDTPL AAFFQDCISE QDLDEMNIEI
     IRNTLYKAYL ESFYKFCTLL GGTTADAMCP ILEFEADRRA FIITINSFGT ELSKEDRAKL
     FPHCGRLYPE GLAQLARADD YEQVKNVADY YPEYKLLFEG AGSNPGDKTL EDRFFEHEVK
     LNKLAFLNQF HFGVFYAFVK LKEQECRNIV WIAECIAQRH RAKIDNYIPI F
//
ID   ADT2_MOUSE              Reviewed;         298 AA.
AC   P51881; Q61311;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 107.
DE   RecName: Full=ADP/ATP translocase 2;
DE   AltName: Full=ADP,ATP carrier protein 2;
DE   AltName: Full=Adenine nucleotide translocator 2;
DE            Short=ANT 2;
DE   AltName: Full=Solute carrier family 25 member 5;
GN   Name=Slc25a5; Synonyms=Ant2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=97059403; PubMed=8903724; DOI=10.1007/s003359900007;
RA   Ellison J.W., Li X., Francke U., Shapiro L.J.;
RT   "Rapid evolution of human pseudoautosomal genes and their mouse
RT   homologs.";
RL   Mamm. Genome 7:25-30(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Skeletal muscle;
RA   Sheldon J.G.;
RL   Thesis (1995), University of Cambridge, United Kingdom.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129/Sv;
RA   Costet P., Laplace C.;
RL   Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   SEQUENCE REVISION.
RA   Laplace C.;
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=20432087; PubMed=10974536; DOI=10.1016/S0378-1119(00)00252-3;
RA   Levy S.E., Chen Y.-S., Graham B.H., Wallace D.C.;
RT   "Expression and sequence analysis of the mouse adenine nucleotide
RT   translocase 1 and 2 genes.";
RL   Gene 254:57-66(2000).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 2-31; 34-43; 64-72; 81-92; 97-106 AND 189-199,
RP   CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Liver;
RA   Bienvenut W.V.;
RL   Submitted (JUL-2005) to UniProtKB.
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-23; LYS-92; LYS-155;
RP   LYS-163; LYS-166 AND LYS-199, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-191 AND TYR-195, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
CC   -!- FUNCTION: Catalyzes the exchange of ADP and ATP across the
CC       mitochondrial inner membrane. As part of the mitotic spindle-
CC       associated MMXD complex it may play a role in chromosome
CC       segregation (By similarity).
CC   -!- SUBUNIT: Homodimer. Component of the MMXD complex, which includes
CC       CIAO1, ERCC2, FAM96B, MMS19 and SLC25A5 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC       membrane protein.
CC   -!- MISCELLANEOUS: The transmembrane helices are not perpendicular to
CC       the plane of the membrane, but cross the membrane at an angle.
CC       Odd-numbered transmembrane helices exhibit a sharp kink, due to
CC       the presence of a conserved proline residue (By similarity).
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier family.
CC   -!- SIMILARITY: Contains 3 Solcar repeats.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U27316; AAC52838.1; -; mRNA.
DR   EMBL; U10404; AAA19009.1; -; mRNA.
DR   EMBL; X70847; CAA50196.1; -; mRNA.
DR   EMBL; AF240003; AAF64471.1; -; Genomic_DNA.
DR   EMBL; BC004570; AAH04570.1; -; mRNA.
DR   EMBL; BC086756; AAH86756.1; -; mRNA.
DR   IPI; IPI00127841; -.
DR   PIR; S31814; S31814.
DR   RefSeq; NP_031477.1; NM_007451.3.
DR   UniGene; Mm.371544; -.
DR   ProteinModelPortal; P51881; -.
DR   SMR; P51881; 2-294.
DR   STRING; P51881; -.
DR   PhosphoSite; P51881; -.
DR   PRIDE; P51881; -.
DR   Ensembl; ENSMUST00000016463; ENSMUSP00000016463; ENSMUSG00000016319.
DR   GeneID; 11740; -.
DR   KEGG; mmu:11740; -.
DR   UCSC; uc009sxs.1; mouse.
DR   CTD; 11740; -.
DR   MGI; MGI:1353496; Slc25a5.
DR   eggNOG; roNOG06425; -.
DR   HOGENOM; HBG610399; -.
DR   HOVERGEN; HBG108348; -.
DR   InParanoid; P51881; -.
DR   OMA; KNTHILV; -.
DR   OrthoDB; EOG49CQ86; -.
DR   PhylomeDB; P51881; -.
DR   NextBio; 279467; -.
DR   ArrayExpress; P51881; -.
DR   Bgee; P51881; -.
DR   Genevestigator; P51881; -.
DR   GermOnline; ENSMUSG00000016319; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0071817; C:MMXD complex; ISS:UniProtKB.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR002113; Aden_trnslctor.
DR   InterPro; IPR002067; Mit_carrier.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00927; ADPTRNSLCASE.
DR   PRINTS; PR00926; MITOCARRIER.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Chromosome partition; Direct protein sequencing;
KW   Membrane; Methylation; Mitochondrion; Mitochondrion inner membrane;
KW   Phosphoprotein; Repeat; Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    298       ADP/ATP translocase 2.
FT                                /FTId=PRO_0000090580.
FT   TRANSMEM      5     39       Helical; Name=1; (By similarity).
FT   TRANSMEM     75    100       Helical; Name=2; (By similarity).
FT   TRANSMEM    109    143       Helical; Name=3; (By similarity).
FT   TRANSMEM    176    202       Helical; Name=4; (By similarity).
FT   TRANSMEM    207    241       Helical; Name=5; (By similarity).
FT   TRANSMEM    273    298       Helical; Name=6; (By similarity).
FT   REPEAT        6     98       Solcar 1.
FT   REPEAT      111    201       Solcar 2.
FT   REPEAT      212    297       Solcar 3.
FT   MOTIF       235    240       Substrate recognition (By similarity).
FT   BINDING      80     80       Nucleotide (By similarity).
FT   MOD_RES       2      2       N-acetylthreonine.
FT   MOD_RES      23     23       N6-acetyllysine.
FT   MOD_RES      42     42       Phosphoserine.
FT   MOD_RES      52     52       N6,N6-dimethyllysine; alternate (By
FT                                similarity).
FT   MOD_RES      52     52       N6-methyllysine; alternate (By
FT                                similarity).
FT   MOD_RES      92     92       N6-acetyllysine.
FT   MOD_RES     105    105       N6-acetyllysine (By similarity).
FT   MOD_RES     155    155       N6-acetyllysine.
FT   MOD_RES     163    163       N6-acetyllysine.
FT   MOD_RES     166    166       N6-acetyllysine.
FT   MOD_RES     191    191       Phosphotyrosine.
FT   MOD_RES     195    195       Phosphotyrosine.
FT   MOD_RES     199    199       N6-acetyllysine.
SQ   SEQUENCE   298 AA;  32931 MW;  0798E04B987EFE20 CRC64;
     MTDAAVSFAK DFLAGGVAAA ISKTAVAPIE RVKLLLQVQH ASKQITADKQ YKGIIDCVVR
     IPKEQGVLSF WRGNLANVIR YFPTQALNFA FKDKYKQIFL GGVDKRTQFW RYFAGNLASG
     GAAGATSLCF VYPLDFARTR LAADVGKAGA EREFKGLGDC LVKIYKSDGI KGLYQGFNVS
     VQGIIIYRAA YFGIYDTAKG MLPDPKNTHI FISWMIAQSV TAVAGLTSYP FDTVRRRMMM
     QSGRKGTDIM YTGTLDCWRK IARDEGSKAF FKGAWSNVLR GMGGAFVLVL YDEIKKYT
//
ID   NEK1_MOUSE              Reviewed;        1203 AA.
AC   P51954;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Serine/threonine-protein kinase Nek1;
DE            EC=2.7.11.1;
DE   AltName: Full=Never in mitosis A-related kinase 1;
DE            Short=NimA-related protein kinase 1;
GN   Name=Nek1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Blood;
RX   MEDLINE=93010942; PubMed=1382974;
RA   Letwin K., Mizzen L., Motro B., Ben-David Y., Bernstein A., Pawson T.;
RT   "A mammalian dual specificity protein kinase, Nek1, is related to the
RT   NIMA cell cycle regulator and highly expressed in meiotic germ
RT   cells.";
RL   EMBO J. 11:3521-3531(1992).
RN   [2]
RP   SEQUENCE REVISION TO C-TERMINUS.
RA   Feige E., Motro B.;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-618, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1071, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   INTERACTION WITH SPERT/NURIT.
RC   STRAIN=CD-1;
RX   MEDLINE=22194721; PubMed=12204287; DOI=10.1016/S0925-4773(02)00217-4;
RA   Feige E., Chen A., Motro B.;
RT   "Nurit, a novel leucine-zipper protein, expressed uniquely in the
RT   spermatid flower-like structure.";
RL   Mech. Dev. 117:369-377(2002).
CC   -!- FUNCTION: Phosphorylates serines and threonines, but also appears
CC       to possess tyrosine kinase activity. Implicated in the control of
CC       meiosis.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium.
CC   -!- SUBUNIT: Binds to SPERT.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- TISSUE SPECIFICITY: Predominantly in testes (germ cells and
CC       Sertoli cells). Lower levels in ovary (ovocytes and granulosa
CC       cells), thymus and lung.
CC   -!- DEVELOPMENTAL STAGE: In female, expressed as follicles enter the
CC       secondary stage until ovulation occurs. In the male reproductive
CC       system, the expression is limited to spermatocytes and spermatids.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY850065; AAB23529.2; -; mRNA.
DR   IPI; IPI00128718; -.
DR   PIR; S25284; S25284.
DR   RefSeq; NP_780298.2; NM_175089.3.
DR   UniGene; Mm.116649; -.
DR   ProteinModelPortal; P51954; -.
DR   SMR; P51954; 1-261.
DR   STRING; P51954; -.
DR   PhosphoSite; P51954; -.
DR   PRIDE; P51954; -.
DR   Ensembl; ENSMUST00000034065; ENSMUSP00000034065; ENSMUSG00000031644.
DR   GeneID; 18004; -.
DR   KEGG; mmu:18004; -.
DR   UCSC; uc009ltt.1; mouse.
DR   CTD; 18004; -.
DR   MGI; MGI:97303; Nek1.
DR   eggNOG; roNOG05728; -.
DR   HOVERGEN; HBG006460; -.
DR   OrthoDB; EOG47D9FH; -.
DR   PhylomeDB; P51954; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 293011; -.
DR   ArrayExpress; P51954; -.
DR   Bgee; P51954; -.
DR   Genevestigator; P51954; -.
DR   GermOnline; ENSMUSG00000031644; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0006974; P:response to DNA damage stimulus; IMP:MGI.
DR   GO; GO:0010212; P:response to ionizing radiation; IMP:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell division; Kinase; Magnesium;
KW   Metal-binding; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT   CHAIN         1   1203       Serine/threonine-protein kinase Nek1.
FT                                /FTId=PRO_0000086419.
FT   DOMAIN        4    258       Protein kinase.
FT   NP_BIND      10     18       ATP (By similarity).
FT   ACT_SITE    128    128       Proton acceptor (By similarity).
FT   BINDING      33     33       ATP (By similarity).
FT   MOD_RES     155    155       Phosphoserine (By similarity).
FT   MOD_RES     162    162       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     417    417       Phosphoserine (By similarity).
FT   MOD_RES     615    615       Phosphothreonine (By similarity).
FT   MOD_RES     618    618       Phosphoserine.
FT   MOD_RES     750    750       Phosphoserine (By similarity).
FT   MOD_RES     786    786       Phosphoserine (By similarity).
FT   MOD_RES     820    820       Phosphoserine (By similarity).
FT   MOD_RES     832    832       Phosphoserine (By similarity).
FT   MOD_RES     953    953       Phosphoserine (By similarity).
FT   MOD_RES     997    997       Phosphoserine (By similarity).
FT   MOD_RES    1070   1070       Phosphotyrosine (By similarity).
FT   MOD_RES    1071   1071       Phosphoserine.
SQ   SEQUENCE   1203 AA;  136690 MW;  06393960F2E719DA CRC64;
     MEKYVRLQKI GEGSFGKAVL VKSTEDGRHY VIKEINISRM SDKERQESRR EVAVLANMKH
     PNIVQYKESF EENGSLYIVM DYCEGGDLFK RINAQKGALF QEDQILDWFV QICLALKHVH
     DRKILHRDIK SQNIFLTKDG TVQLGDFGIA RVLNSTVELA RTCIGTPYYL SPEICENKPY
     NNKSDIWALG CVLYELCTLK HAFEAGNMKN LVLKIISGSF PPVSPHYSYD LRSLLSQLFK
     RNPRDRPSVN SILEKGFIAK RIEKFLSPQL IAEEFCLKTL SKFGPQPLPG KRPASGQGVS
     SFVPAQKITK PAAKYGVPLT YKKYGDKKLL EKKPPPKHKQ AHQIPVKKMN SGEERKKMSE
     EAAKKRRLEF IEKEKKQKDQ IRFLKAEQMK RQEKQRLERI NRAREQGWRN VLRAGGSGEV
     KASFFGIGGA VSPSPCSPRG QYEHYHAIFD QMQRLRAEDN EARWKGGIYG RWLPERQKGH
     LAVERANQVE EFLQRKREAM QNKARAEGHV VYLARLRQIR LQNFNERQQI KAKLRGENKE
     ADGTKGQEAT EETDMRLKKM ESLKAQTNAR AAVLKEQLER KRKEAYEREK KVWEEHLVAR
     VKSSDVPLPL ELLETGGSPS KQQVKPVISV TSALKEVGLD GSLTDTQEEE MEKSNSAISS
     KREILRRLNE NLKAQEDEKE KQHHSGSCET VGHKDEREYE TENAISSDRK KWEMGGQLVI
     PLDAVTLDTS FSATEKHTVG EVIKLDSNGS PRKVWGKNPT DSVLKILGEA ELQLQTELLE
     NTSFKSEVYA EEENYKPLLT EEENLQCISK EINPSATVDS TETKSPKFTE VSPQMSEGNV
     EEPDDLETEV LQEPSSTHTD GSLPPVLNDV WTREKEAAKE TELEDKVAVQ QSEVCEDRIP
     GNVDQSCKDQ RDPAVDDSPQ SGCDVEKSVQ PESIFQKVVH SKDLNLVQAV HCSPEEPIPI
     RSHSDSPPKT KSKNSLLIGL STGLFDANNP KMLRTCSLPD LSKLFRTLMD VPTVGDVHQD
     SLEIDELEDE PIKEGPSDSE DTVFEETDTD LQELQASMEQ LLREQPGDEY SEEEESVLKS
     SDVEQTARGT DAPDEEDNPS SESALNEEWH SDNSDAETTS ECEYDSVFNH LEELRLHLEQ
     EMGFEKFFEV YEKVKAIHED EDENIEICST IVENILGNEH QHLYAKILHL VMADGAYQED
     NDE
//
ID   CLGN_MOUSE              Reviewed;         611 AA.
AC   P52194; Q9D2K5;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAR-2011, entry version 101.
DE   RecName: Full=Calmegin;
DE   AltName: Full=A2/6;
DE   AltName: Full=Calnexin-T;
DE   AltName: Full=MEG 1 antigen;
DE   Flags: Precursor;
GN   Name=Clgn; Synonyms=Meg1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Testis;
RX   MEDLINE=94171811; PubMed=8126001;
RA   Watanabe D., Yamada K., Nishina Y., Tajima Y., Koshimizu U.,
RA   Nagata A., Nishimune Y.;
RT   "Molecular cloning of a novel Ca(2+)-binding protein (calmegin)
RT   specifically expressed during male meiotic germ cell development.";
RL   J. Biol. Chem. 269:7744-7749(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CD-1; TISSUE=Testis;
RX   MEDLINE=94245735; PubMed=8188695;
RA   Ohsako S., Hayashi Y., Bunick D.;
RT   "Molecular cloning and sequencing of calnexin-t. An abundant male germ
RT   cell-specific calcium-binding protein of the endoplasmic reticulum.";
RL   J. Biol. Chem. 269:14140-14148(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Testis;
RX   MEDLINE=98094268; PubMed=9434179; DOI=10.1016/S0378-1119(97)00537-4;
RA   Tanaka H., Ikawa M., Tsuchida J., Nozaki M., Suzuki M., Fujiwara T.,
RA   Okabe M., Nishimune Y.;
RT   "Cloning and characterization of the human Calmegin gene encoding
RT   putative testis-specific chaperone.";
RL   Gene 204:159-163(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Probably plays an important role in spermatogenesis.
CC       Binds calcium ions.
CC   -!- SUBUNIT: Interacts with PDILT (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       type I membrane protein.
CC   -!- TISSUE SPECIFICITY: Testis.
CC   -!- DEVELOPMENTAL STAGE: Specifically expressed during male meiotic
CC       germ cell development.
CC   -!- SIMILARITY: Belongs to the calreticulin family.
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DR   EMBL; D14117; BAA03180.1; -; mRNA.
DR   EMBL; U08373; AAA20599.1; -; mRNA.
DR   EMBL; D86323; BAA22591.1; -; mRNA.
DR   EMBL; AK019534; BAB31782.1; ALT_SEQ; mRNA.
DR   IPI; IPI00123699; -.
DR   PIR; A53418; A53418.
DR   PIR; A54086; A54086.
DR   UniGene; Mm.358581; -.
DR   ProteinModelPortal; P52194; -.
DR   SMR; P52194; 51-446.
DR   MINT; MINT-4592857; -.
DR   STRING; P52194; -.
DR   PRIDE; P52194; -.
DR   Ensembl; ENSMUST00000002259; ENSMUSP00000002259; ENSMUSG00000002190.
DR   Ensembl; ENSMUST00000109831; ENSMUSP00000105457; ENSMUSG00000002190.
DR   MGI; MGI:107472; Clgn.
DR   eggNOG; roNOG13552; -.
DR   HOGENOM; HBG444251; -.
DR   HOVERGEN; HBG005407; -.
DR   InParanoid; P52194; -.
DR   OrthoDB; EOG48D0V1; -.
DR   PhylomeDB; P52194; -.
DR   ArrayExpress; P52194; -.
DR   Bgee; P52194; -.
DR   CleanEx; MM_CLGN; -.
DR   Genevestigator; P52194; -.
DR   GermOnline; ENSMUSG00000002190; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0007339; P:binding of sperm to zona pellucida; IMP:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007126; P:meiosis; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0006461; P:protein complex assembly; IMP:MGI.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR001580; Calret/calnex.
DR   InterPro; IPR018124; Calret/calnex_CS.
DR   InterPro; IPR009033; Calreticulin/calnexin_P.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   Gene3D; G3DSA:2.10.250.10; Calreticulin/calnexin_P; 2.
DR   Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 1.
DR   PANTHER; PTHR11073; Calret/calnex; 1.
DR   Pfam; PF00262; Calreticulin; 1.
DR   PRINTS; PR00626; CALRETICULIN.
DR   SUPFAM; SSF63887; Calret_calnex_P; 1.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 2.
DR   PROSITE; PS00803; CALRETICULIN_1; 1.
DR   PROSITE; PS00804; CALRETICULIN_2; 1.
DR   PROSITE; PS00805; CALRETICULIN_REPEAT; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Chaperone; Developmental protein; Differentiation;
KW   Disulfide bond; Endoplasmic reticulum; Meiosis; Membrane;
KW   Phosphoprotein; Repeat; Signal; Spermatogenesis; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     19       Potential.
FT   CHAIN        20    611       Calmegin.
FT                                /FTId=PRO_0000004211.
FT   TOPO_DOM     20    471       Lumenal (Potential).
FT   TRANSMEM    472    492       Helical; (Potential).
FT   TOPO_DOM    493    611       Cytoplasmic (Potential).
FT   REPEAT      267    280       1-1.
FT   REPEAT      284    297       1-2.
FT   REPEAT      303    316       1-3.
FT   REPEAT      322    335       1-4.
FT   REPEAT      339    352       2-1.
FT   REPEAT      356    369       2-2.
FT   REPEAT      370    383       2-3.
FT   REPEAT      384    397       2-4.
FT   MOD_RES     561    561       Phosphoserine (By similarity).
FT   DISULFID    151    185       By similarity.
FT   DISULFID    351    355       By similarity.
FT   CONFLICT     76     79       LSKA -> YQS (in Ref. 2; AAA20599).
FT   CONFLICT     87     87       E -> Q (in Ref. 2; AAA20599).
FT   CONFLICT    127    127       E -> D (in Ref. 2; AAA20599).
FT   CONFLICT    133    135       ADK -> GAIN (in Ref. 2; AAA20599).
FT   CONFLICT    201    201       K -> Q (in Ref. 2; AAA20599).
FT   CONFLICT    210    210       A -> P (in Ref. 2; AAA20599).
FT   CONFLICT    291    291       K -> R (in Ref. 4; BAB31782).
FT   CONFLICT    350    350       A -> D (in Ref. 2; AAA20599).
FT   CONFLICT    432    432       E -> D (in Ref. 2; AAA20599).
FT   CONFLICT    436    436       A -> P (in Ref. 2; AAA20599).
FT   CONFLICT    440    440       A -> P (in Ref. 2; AAA20599).
FT   CONFLICT    445    445       E -> D (in Ref. 2; AAA20599).
FT   CONFLICT    451    451       A -> T (in Ref. 2; AAA20599).
FT   CONFLICT    522    522       E -> D (in Ref. 2; AAA20599).
FT   CONFLICT    549    549       V -> L (in Ref. 2; AAA20599).
FT   CONFLICT    577    578       LS -> AE (in Ref. 4; BAB31782).
SQ   SEQUENCE   611 AA;  69403 MW;  D5F2BBB4085B2708 CRC64;
     MRFQGVGLCL GLLFITVNAD FMDDGVEVED FSENSDESNI KDEPSSGTFK YKTPQPIGEV
     YFTETFDSGN LAGWVLSKAK KDDMDSEIAI YDGRWEIEEL KENQVPGDRG LVLKSKAKHH
     AIAAVLEKPF IFADKPLIVQ YEVNFQDGID CGGAYIKLLA DTGDLILENF YDKTSYTIMF
     GPDKCGEDYK LHLIFRHKHP KTGVFEEKHA KPPDVDLKEF FTDRKTHLYT LVMNPDDTFE
     VLIDQKVVNQ GTLLDDVVPP INPPREIDDP SDKKPEEWDD RAKIPDPTAV KPEDWDENEP
     AQIEDSSAVK PDGWLDDEPK FIPNPKAEKP EDWSDDMDGE WEAPHIPNPA CQIGCGEWKP
     PMIDNPKYKG IWRPPMINNP NYQGLWSPQK IPNPDYFEDD HPFLLTSFSA LGLELWSMTP
     DIYFDNFIIC SEKEVADQWA TDGWELKIMV ANANEPGVLR QLVIAAEERP WLWLMYLVMA
     GLPVALVASF CWPRKVKKKY EDTGPKKTEL CKLQSKAALE QEAEEEKAPE KPEDVQEEKK
     PGEAEVVTVE KEVIGEPEEK SKEDRETLEG QEEVSKLSKS GSEDEMKDAD ESPGSGDAPL
     KSLRKRRVRK D
//
ID   UBP10_MOUSE             Reviewed;         792 AA.
AC   P52479; Q3T9L4; Q3TNN5; Q3TZB8; Q3U5E0; Q6ZQG9; Q91VY7;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 3.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 10;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 10;
DE   AltName: Full=Ubiquitin thiolesterase 10;
DE   AltName: Full=Ubiquitin-specific-processing protease 10;
GN   Name=Usp10; Synonyms=Kiaa0190, Ode-1, Uchrp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Ito M., Hitomi K., Tsukagoshi N.;
RT   "Cloning from a mouse osteoblastic cell line of a gene, encoding a
RT   ubiquitin carboxyl-terminal hydrolase related polypeptide, down
RT   regulated during ascorbic acid dependent differentiation.";
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Inner ear, Spleen, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205 AND SER-570, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from
CC       target proteins such as p53/TP53, SNX3 and CFTR. Acts as an
CC       essential regulator of p53/TP53 stability: in unstressed cells,
CC       specifically deubiquitinates p53/TP53 in the cytoplasm, leading to
CC       counteract MDM2 action and stabilize p53/TP53. Following DNA
CC       damage, translocates to the nucleus and deubiquitinates p53/TP53,
CC       leading to regulate the p53/TP53-dependent DNA damage response.
CC       Does not deubiquitinate MDM2. Deubiquitinates CFTR in early
CC       endosomes, enhancing its endocytic recycling (By similarity).
CC   -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- SUBUNIT: Interacts with G3BP, which may regulate its function.
CC       Interacts with p53/TP53, SNX3 and CFTR (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Early endosome (By similarity). Note=Cytoplasmic in
CC       normal conditions. After DNA damage, translocates to the nucleus
CC       following phosphorylation by ATM (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P52479-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P52479-2; Sequence=VSP_038870;
CC   -!- PTM: Phosphorylated by ATM following DNA damage, leading to
CC       stablization and translocation it to the nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. USP10 subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97893.1; Type=Erroneous initiation;
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DR   EMBL; D84096; BAA12220.1; -; mRNA.
DR   EMBL; AK129083; BAC97893.1; ALT_INIT; mRNA.
DR   EMBL; AK153675; BAE32139.1; -; mRNA.
DR   EMBL; AK157970; BAE34291.1; -; mRNA.
DR   EMBL; AK165156; BAE38053.1; -; mRNA.
DR   EMBL; AK172443; BAE43006.1; -; mRNA.
DR   EMBL; CH466525; EDL11620.1; -; Genomic_DNA.
DR   EMBL; BC007134; AAH07134.1; -; mRNA.
DR   IPI; IPI00420601; -.
DR   IPI; IPI00955687; -.
DR   RefSeq; NP_033488.1; NM_009462.1.
DR   UniGene; Mm.256910; -.
DR   UniGene; Mm.421337; -.
DR   ProteinModelPortal; P52479; -.
DR   SMR; P52479; 409-789.
DR   STRING; P52479; -.
DR   MEROPS; C19.018; -.
DR   PhosphoSite; P52479; -.
DR   PRIDE; P52479; -.
DR   Ensembl; ENSMUST00000108988; ENSMUSP00000104616; ENSMUSG00000031826.
DR   GeneID; 22224; -.
DR   KEGG; mmu:22224; -.
DR   CTD; 22224; -.
DR   MGI; MGI:894652; Usp10.
DR   eggNOG; roNOG14540; -.
DR   GeneTree; ENSGT00550000074994; -.
DR   HOVERGEN; HBG059823; -.
DR   InParanoid; P52479; -.
DR   OMA; TPRTCNS; -.
DR   BRENDA; 3.1.2.15; 244.
DR   NextBio; 302247; -.
DR   ArrayExpress; P52479; -.
DR   Bgee; P52479; -.
DR   CleanEx; MM_USP10; -.
DR   Genevestigator; P52479; -.
DR   GermOnline; ENSMUSG00000031826; Mus musculus.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0042980; F:cystic fibrosis transmembrane conductance regulator binding; ISS:UniProtKB.
DR   GO; GO:0002039; F:p53 binding; ISS:UniProtKB.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; ISS:UniProtKB.
DR   GO; GO:0004843; F:ubiquitin-specific protease activity; ISS:UniProtKB.
DR   GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR009818; Ataxin-2_C.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19.
DR   Pfam; PF07145; PAM2; 1.
DR   Pfam; PF00443; UCH; 1.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; 1.
DR   PROSITE; PS50235; UCH_2_3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; DNA damage; DNA repair; Endosome;
KW   Hydrolase; Nucleus; Phosphoprotein; Protease; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN         1    792       Ubiquitin carboxyl-terminal hydrolase 10.
FT                                /FTId=PRO_0000080630.
FT   REGION        1     99       Interaction with p53/TP53 (By
FT                                similarity).
FT   ACT_SITE    418    418       Nucleophile (By similarity).
FT   ACT_SITE    743    743       Proton acceptor (By similarity).
FT   MOD_RES     205    205       Phosphothreonine.
FT   MOD_RES     208    208       Phosphoserine (By similarity).
FT   MOD_RES     217    217       Phosphoserine (By similarity).
FT   MOD_RES     223    223       Phosphoserine (By similarity).
FT   MOD_RES     330    330       Phosphoserine; by ATM (By similarity).
FT   MOD_RES     359    359       Phosphoserine (By similarity).
FT   MOD_RES     364    364       Phosphoserine (By similarity).
FT   MOD_RES     541    541       Phosphoserine (By similarity).
FT   MOD_RES     570    570       Phosphoserine.
FT   VAR_SEQ      49     49       D -> DA (in isoform 2).
FT                                /FTId=VSP_038870.
FT   CONFLICT     72     72       P -> R (in Ref. 5; AAH07134).
FT   CONFLICT    101    101       E -> D (in Ref. 5; AAH07134).
FT   CONFLICT    293    293       N -> S (in Ref. 5; AAH07134).
FT   CONFLICT    347    347       A -> S (in Ref. 5; AAH07134).
FT   CONFLICT    448    448       R -> G (in Ref. 3; BAE34291).
FT   CONFLICT    472    472       P -> T (in Ref. 3; BAE32139).
FT   CONFLICT    528    528       G -> R (in Ref. 3; BAE38053).
SQ   SEQUENCE   792 AA;  87022 MW;  02D07A8194215D09 CRC64;
     MALHNPQYIF GDFSPDEFNQ FFVTPRSSVE LPPYSGTLCS IQAEDELPDG QEHQRIEFGV
     DEVIEPSEGL PPTPSYSISS TLNPQAPEFI LGCTTSKKIP EAVEKDETYS SIDQYPASAL
     ALESNSNAEA ETLENDSGAG GLGQRERKKK KKRPPGYYSY LKDGGEDSAS PATLVNGHAT
     SVGTSGEAVE DAEFMDVLPP VMPRTCDSPQ NPVDFISGPV PDSPFPRTLG GDARTAGLCE
     GCHEADFEQP CLPADSLLRT AGTQPYVGTD TTENFAVANG KILESPGEDT AANGAELHTD
     EGADLDPAKP ESQSPPAESA LSASGAIPIS QPAKSWASLF HDSKPSASSP MAYVETKCSP
     PVPSPLASEK QMEVKEGLVP VSEDPVAIKI AELLETVTLI HKPVSLQPRG LINKGNWCYI
     NATLQALVAC PPMYHLMKFI PLYSKVQRPC TSTPMIDSFV RLMNEFTNMP VPPKPRQALG
     DKIVRDIRPG AAFEPTYIYR LLTVIKSSLS EKGRQEDAEE YLGFILNGLH EEMLSLKKLL
     SPTHEKHSVS NGPRSDLIED EELEDTGKGS EDEWEQVGPK NKTSITRQAD FVQTPITGIF
     GGHIRSVVYQ QSSKESATLQ LFFTLQLDIQ SDKIRTVQDA LESLVARESV QGYTTKTKQE
     VEVSRRVTLE KLPPVLVLHL KRFVYEKTGG CQKLVKNIDY PVDLEISREL LSPGIKNKNF
     KCQRTYRLFA VVYHHGNSAT GGHYTTDVFQ IGLNGWLRID DQTVKVINQY QVVKPPADRT
     AYLLYYRRVD LL
//
ID   KPYM_MOUSE              Reviewed;         531 AA.
AC   P52480; Q3TBV8; Q3TBW5; Q3TC59; Q3U1X3; Q3U5P6; Q4VC20; Q64484;
AC   Q91YI8; Q9CWB1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 4.
DT   08-MAR-2011, entry version 119.
DE   RecName: Full=Pyruvate kinase isozymes M1/M2;
DE            EC=2.7.1.40;
DE   AltName: Full=Pyruvate kinase muscle isozyme;
GN   Name=Pkm2; Synonyms=Pk3, Pykm;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M2).
RX   MEDLINE=95337147; PubMed=7612666; DOI=10.1016/0167-4889(95)00071-Y;
RA   Izumi S., Manabe A., Tomoyasu A., Kihara-Negishi F., Ariga H.;
RT   "Molecular cloning of the complementary DNA for the mouse pyruvate
RT   kinase M-2 gene whose expression is dependent upon cell
RT   differentiation.";
RL   Biochim. Biophys. Acta 1267:135-138(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M2).
RC   STRAIN=Swiss;
RX   MEDLINE=98207721; PubMed=9545585; DOI=10.1016/S0167-4781(97)00195-4;
RA   de Luis O., del Mazo J.;
RT   "Gene expression of mouse M1 and M2 pyruvate kinase isoenzymes
RT   correlates with differential poly(A) tract extension of their mRNAs
RT   during the development of spermatogenesis.";
RL   Biochim. Biophys. Acta 1396:294-305(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM M2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-395 (ISOFORM M1).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Kidney, and Muellerian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM M2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 33-56; 67-89; 93-115; 126-136; 142-162; 167-224;
RP   231-246; 248-255; 279-305; 320-336; 343-399; 401-433; 468-498 AND
RP   506-526, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B.,
RA   Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   ISGYLATION.
RX   PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA   Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA   Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT   "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT   human cells.";
RL   Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=18191611; DOI=10.1016/j.biocel.2007.11.009;
RA   Lee J., Kim H.K., Han Y.-M., Kim J.;
RT   "Pyruvate kinase isozyme type M2 (PKM2) interacts and cooperates with
RT   Oct-4 in regulating transcription.";
RL   Int. J. Biochem. Cell Biol. 40:1043-1054(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-105 AND TYR-148, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Glycolytic enzyme that catalyzes the transfer of a
CC       phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating
CC       ATP. Stimulates POU5F1-mediated transcriptional activation (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate.
CC   -!- COFACTOR: Magnesium.
CC   -!- COFACTOR: Potassium.
CC   -!- ENZYME REGULATION: Isoform M2 is allosterically activated by D-
CC       fructose 1,6-biphosphate (FBP). Inhibited by oxalate and 3,3',5-
CC       triiodo-L-thyronine (T3) (By similarity).
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 5/5.
CC   -!- SUBUNIT: Monomer and homotetramer. Exists as a monomer in the
CC       absence of fructose 1,6 bi-phosphate (FBP), and reversibly
CC       associates to form a homotetramer in the presence of FBP. The
CC       monomeric form binds T3. Tetramer formation induces pyruvate
CC       kinase activity. Interacts with HERC1, POU5F1 and PML (By
CC       similarity).
CC   -!- INTERACTION:
CC       P20263:Pou5f1; NbExp=4; IntAct=EBI-647785, EBI-1606219;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=M2;
CC         IsoId=P52480-1; Sequence=Displayed;
CC       Name=M1;
CC         IsoId=P52480-2; Sequence=VSP_025057;
CC   -!- TISSUE SPECIFICITY: Embryonic stem cells and embryonal carcinoma
CC       cells.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- PTM: ISGylated.
CC   -!- MISCELLANEOUS: There are 4 isozymes of pyruvate kinase in mammals:
CC       L, R, M1 and M2. L type is major isozyme in the liver, R is found
CC       in red cells, M1 is the main form in muscle, heart and brain, and
CC       M2 is found in early fetal tissues.
CC   -!- SIMILARITY: Belongs to the pyruvate kinase family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; D38379; BAA07457.1; -; mRNA.
DR   EMBL; X97047; CAA65761.1; -; mRNA.
DR   EMBL; AK002341; BAB22025.1; -; mRNA.
DR   EMBL; AK135397; BAE22519.1; -; mRNA.
DR   EMBL; AK151724; BAE30642.1; -; mRNA.
DR   EMBL; AK153483; BAE32031.1; -; mRNA.
DR   EMBL; AK155110; BAE33055.1; -; mRNA.
DR   EMBL; AK155655; BAE33370.1; -; mRNA.
DR   EMBL; AK170892; BAE42098.1; -; mRNA.
DR   EMBL; AK168943; BAE40751.1; -; mRNA.
DR   EMBL; AK171023; BAE42192.1; -; mRNA.
DR   EMBL; AK171033; BAE42199.1; -; mRNA.
DR   EMBL; AC160637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC016619; AAH16619.1; -; mRNA.
DR   EMBL; BC094663; AAH94663.1; -; mRNA.
DR   IPI; IPI00407130; -.
DR   IPI; IPI00845840; -.
DR   PIR; S55921; S55921.
DR   RefSeq; NP_035229.2; NM_011099.2.
DR   UniGene; Mm.326167; -.
DR   ProteinModelPortal; P52480; -.
DR   SMR; P52480; 13-531.
DR   IntAct; P52480; 13.
DR   MINT; MINT-1850796; -.
DR   STRING; P52480; -.
DR   PhosphoSite; P52480; -.
DR   SWISS-2DPAGE; P52480; -.
DR   PMMA-2DPAGE; P52480; -.
DR   REPRODUCTION-2DPAGE; IPI00407130; -.
DR   REPRODUCTION-2DPAGE; P52480; -.
DR   PRIDE; P52480; -.
DR   Ensembl; ENSMUST00000034834; ENSMUSP00000034834; ENSMUSG00000032294.
DR   GeneID; 18746; -.
DR   KEGG; mmu:18746; -.
DR   CTD; 18746; -.
DR   MGI; MGI:97591; Pkm2.
DR   eggNOG; roNOG11660; -.
DR   GeneTree; ENSGT00390000008859; -.
DR   HOVERGEN; HBG000941; -.
DR   InParanoid; P52480; -.
DR   OMA; TMENAVE; -.
DR   OrthoDB; EOG40GCQJ; -.
DR   PhylomeDB; P52480; -.
DR   BRENDA; 2.7.1.40; 244.
DR   NextBio; 294905; -.
DR   ArrayExpress; P52480; -.
DR   Bgee; P52480; -.
DR   CleanEx; MM_PKM2; -.
DR   Genevestigator; P52480; -.
DR   GermOnline; ENSMUSG00000032294; Mus musculus.
DR   GO; GO:0019861; C:flagellum; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004743; F:pyruvate kinase activity; IDA:MGI.
DR   GO; GO:0006096; P:glycolysis; IDA:MGI.
DR   InterPro; IPR001697; Pyr_Knase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase.
DR   InterPro; IPR011037; Pyrv_Knase-like_insert_dom.
DR   InterPro; IPR015794; Pyrv_Knase_a/b.
DR   InterPro; IPR018209; Pyrv_Knase_AS.
DR   InterPro; IPR015793; Pyrv_Knase_brl.
DR   InterPro; IPR015795; Pyrv_Knase_C-like.
DR   InterPro; IPR015806; Pyrv_Knase_insert_dom.
DR   Gene3D; G3DSA:2.40.33.10; PK_B_barrel_like; 1.
DR   Gene3D; G3DSA:3.20.20.60; Pyrv/PenolPyrv_Kinase_cat; 2.
DR   Gene3D; G3DSA:3.40.1380.20; Pyrv_Knase_a/b; 1.
DR   PANTHER; PTHR11817; Pyruvate_kinase; 1.
DR   Pfam; PF00224; PK; 1.
DR   Pfam; PF02887; PK_C; 1.
DR   PRINTS; PR01050; PYRUVTKNASE.
DR   SUPFAM; SSF50800; PK_B_barrel_like; 1.
DR   SUPFAM; SSF52935; Pyruvate_kinase; 1.
DR   SUPFAM; SSF51621; Pyrv/PenolPyrv_Kinase_cat; 1.
DR   TIGRFAMs; TIGR01064; pyruv_kin; 1.
DR   PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Allosteric enzyme; Alternative splicing; ATP-binding;
KW   Cytoplasm; Direct protein sequencing; Glycolysis; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Potassium;
KW   Pyruvate; Transferase; Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    531       Pyruvate kinase isozymes M1/M2.
FT                                /FTId=PRO_0000112089.
FT   REGION      307    531       Interaction with POU5F1 (By similarity).
FT   REGION      389    433       Intersubunit contact.
FT   REGION      432    437       D-fructose 1,6-bisphosphate binding; part
FT                                of allosteric site (By similarity).
FT   REGION      514    521       D-fructose 1,6-bisphosphate binding; part
FT                                of allosteric site (By similarity).
FT   METAL        75     75       Potassium (By similarity).
FT   METAL        77     77       Potassium (By similarity).
FT   METAL       113    113       Potassium (By similarity).
FT   METAL       114    114       Potassium (By similarity).
FT   METAL       272    272       Magnesium (By similarity).
FT   METAL       296    296       Magnesium (By similarity).
FT   BINDING      73     73       Substrate (By similarity).
FT   BINDING     295    295       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     296    296       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     328    328       Substrate (By similarity).
FT   BINDING     482    482       D-fructose 1,6-bisphosphate; part of
FT                                allosteric site (By similarity).
FT   BINDING     489    489       D-fructose 1,6-bisphosphate; part of
FT                                allosteric site (By similarity).
FT   SITE        270    270       Transition state stabilizer (By
FT                                similarity).
FT   MOD_RES      37     37       Phosphoserine (By similarity).
FT   MOD_RES      45     45       Phosphothreonine (By similarity).
FT   MOD_RES      62     62       N6-acetyllysine (By similarity).
FT   MOD_RES      83     83       Phosphotyrosine (By similarity).
FT   MOD_RES      89     89       N6-acetyllysine (By similarity).
FT   MOD_RES     105    105       Phosphotyrosine.
FT   MOD_RES     148    148       Phosphotyrosine.
FT   MOD_RES     166    166       N6-acetyllysine (By similarity).
FT   MOD_RES     175    175       Phosphotyrosine (By similarity).
FT   MOD_RES     195    195       Phosphothreonine (By similarity).
FT   MOD_RES     266    266       N6-acetyllysine (By similarity).
FT   MOD_RES     328    328       Phosphothreonine (By similarity).
FT   MOD_RES     390    390       Phosphotyrosine (By similarity).
FT   MOD_RES     433    433       N6-acetyllysine (By similarity).
FT   VAR_SEQ     389    433       IYHLQLFEELRRLAPITSDPTEAAAVGAVEASFKCCSGAII
FT                                VLTK -> MFHRLLFEELVRASSHSTDLMEAMAMGSVEASY
FT                                KCLAAALIVLTE (in isoform M1).
FT                                /FTId=VSP_025057.
FT   CONFLICT      8      8       A -> V (in Ref. 2; CAA65761).
FT   CONFLICT    121    121       T -> A (in Ref. 3; BAE30642/BAE32031).
FT   CONFLICT    158    158       W -> R (in Ref. 1; BAA07457).
FT   CONFLICT    166    166       K -> E (in Ref. 3; BAE42098).
FT   CONFLICT    170    170       V -> L (in Ref. 3; BAE30642/BAE32031).
FT   CONFLICT    177    177       D -> G (in Ref. 3; BAE42199).
FT   CONFLICT    230    230       K -> R (in Ref. 3; BAE30642/BAE32031).
FT   CONFLICT    299    299       I -> T (in Ref. 1; BAA07457).
FT   CONFLICT    309    309       A -> S (in Ref. 1; BAA07457).
FT   CONFLICT    327    327       A -> S (in Ref. 1; BAA07457 and 2;
FT                                CAA65761).
FT   CONFLICT    333    333       S -> I (in Ref. 1; BAA07457 and 2;
FT                                CAA65761).
FT   CONFLICT    485    485       D -> N (in Ref. 3; BAE33055/BAE42192).
SQ   SEQUENCE   531 AA;  57845 MW;  34CBBC01BC0C047D CRC64;
     MPKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSAPI TARNTGIICT IGPASRSVEM
     LKEMIKSGMN VARLNFSHGT HEYHAETIKN VREATESFAS DPILYRPVAV ALDTKGPEIR
     TGLIKGSGTA EVELKKGATL KITLDNAYME KCDENILWLD YKNICKVVEV GSKIYVDDGL
     ISLQVKEKGA DFLVTEVENG GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV
     FASFIRKAAD VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE
     IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN AVLDGADCIM
     LSGETAKGDY PLEAVRMQHL IAREAEAAIY HLQLFEELRR LAPITSDPTE AAAVGAVEAS
     FKCCSGAIIV LTKSGRSAHQ VARYRPRAPI IAVTRNPQTA RQAHLYRGIF PVLCKDAVLN
     AWAEDVDLRV NLAMDVGKAR GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P
//
ID   FGD1_MOUSE              Reviewed;         960 AA.
AC   P52734;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=FYVE, RhoGEF and PH domain-containing protein 1;
DE   AltName: Full=Faciogenital dysplasia 1 protein homolog;
DE   AltName: Full=Rho/Rac guanine nucleotide exchange factor FGD1;
DE            Short=Rho/Rac GEF;
DE   AltName: Full=Zinc finger FYVE domain-containing protein 3;
GN   Name=Fgd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96081343; PubMed=8535076; DOI=10.1007/BF00352375;
RA   Pasteris N.G., de Gouyon B., Cadle A.B., Campbell K., Herman G.E.,
RA   Gorski J.L.;
RT   "Cloning and regional localization of the mouse faciogenital dysplasia
RT   (Fgd1) gene.";
RL   Mamm. Genome 6:658-661(1995).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DBNL AND CTTN, AND
RP   MUTAGENESIS OF PRO-159; PRO-162 AND LYS-164.
RX   PubMed=12913069; DOI=10.1093/hmg/ddg209;
RA   Hou P., Estrada L., Kinley A.W., Parsons J.T., Vojtek A.B.,
RA   Gorski J.L.;
RT   "Fgd1, the Cdc42 GEF responsible for faciogenital dysplasia, directly
RT   interacts with cortactin and mAbp1 to modulate cell shape.";
RL   Hum. Mol. Genet. 12:1981-1993(2003).
RN   [3]
RP   POSSIBLE INTERACTION WITH CCPG1.
RX   PubMed=17000758; DOI=10.1128/MCB.00670-06;
RA   Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P.;
RT   "Ccpg1, a novel scaffold protein that regulates the activity of the
RT   Rho guanine nucleotide exchange factor Dbs.";
RL   Mol. Cell. Biol. 26:8964-8975(2006).
CC   -!- FUNCTION: Activates CDC42, a member of the Ras-like family of Rho-
CC       and Rac proteins, by exchanging bound GDP for free GTP. Plays a
CC       role in regulating the actin cytoskeleton and cell shape.
CC   -!- SUBUNIT: Interacts with DBNL/ABP1 and CTTN. Binds CDC42 (By
CC       similarity). May interact with CCPG1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell projection, lamellipodium.
CC       Cell projection, ruffle. Cytoplasm, cytoskeleton. Note=Associated
CC       with membrane ruffles and lamellipodia.
CC   -!- DOMAIN: The DH domain is involved in interaction with CCPG1.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 2 PH domains.
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DR   EMBL; U22325; AAA96001.1; -; mRNA.
DR   IPI; IPI00130529; -.
DR   UniGene; Mm.8142; -.
DR   ProteinModelPortal; P52734; -.
DR   SMR; P52734; 370-686, 723-791, 815-923.
DR   MINT; MINT-272222; -.
DR   STRING; P52734; -.
DR   PhosphoSite; P52734; -.
DR   PRIDE; P52734; -.
DR   Ensembl; ENSMUST00000026296; ENSMUSP00000026296; ENSMUSG00000025265.
DR   MGI; MGI:104566; Fgd1.
DR   HOGENOM; HBG446336; -.
DR   HOVERGEN; HBG007506; -.
DR   InParanoid; P52734; -.
DR   OrthoDB; EOG4PK274; -.
DR   ArrayExpress; P52734; -.
DR   Bgee; P52734; -.
DR   CleanEx; MM_FGD1; -.
DR   Genevestigator; P52734; -.
DR   GermOnline; ENSMUSG00000025265; Mus musculus.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0001726; C:ruffle; IDA:MGI.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; IDA:UniProtKB.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF00169; PH; 2.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS00741; DH_1; FALSE_NEG.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cytoplasm; Cytoskeleton;
KW   Guanine-nucleotide releasing factor; Metal-binding; Phosphoprotein;
KW   Repeat; Zinc; Zinc-finger.
FT   CHAIN         1    960       FYVE, RhoGEF and PH domain-containing
FT                                protein 1.
FT                                /FTId=PRO_0000080941.
FT   DOMAIN      372    560       DH.
FT   DOMAIN      589    688       PH 1.
FT   DOMAIN      820    920       PH 2.
FT   ZN_FING     729    789       FYVE-type.
FT   MOTIF       171    179       SH3-binding (Potential).
FT   MOTIF       179    187       SH3-binding (Potential).
FT   COMPBIAS      7    330       Pro-rich.
FT   MOD_RES      48     48       Phosphoserine (By similarity).
FT   MOD_RES     205    205       Phosphoserine (By similarity).
FT   MOD_RES     703    703       Phosphothreonine (By similarity).
FT   MOD_RES     710    710       Phosphothreonine (By similarity).
FT   MOD_RES     714    714       Phosphoserine (By similarity).
FT   MUTAGEN     159    159       P->A: Abolishes binding to DBNL.
FT   MUTAGEN     162    162       P->A: Abolishes binding to DBNL.
FT   MUTAGEN     164    164       K->E: No effect on binding to DBNL.
SQ   SEQUENCE   960 AA;  106478 MW;  41C1B84DE490FC51 CRC64;
     MHGHRVPGGP GPSDPERSAA NTPGAAPLAC ADSDPGALEP GLPVSRGSGT ALGGPLDPQF
     VGPSDASLGA PPSSRVLPCG PSPQHHRALR FSYHLEGSQP RPGLHQGNRI LVKSLSLDPG
     QSLEPHPEGP QRLRSDPGPP TEIPGPRPSP LKRAPGPKPQ VPPKPSYLQM PRVLPPPEPI
     PPPPSRPLPA DPRVAKGLVP RAEASTSSAA VSSLIEKFER EPVIVASDRP APGPCPVPPE
     PAMLPQPPPQ PTGSQLPEGE ASRCLFLLAP GPRDGEKVPN RDSGIDSISS PSNSEETCFV
     SDDGPPIHSL CPGPPALASM PVALADPHRP GSQEVDSDLE EEEEEEEEEK EREIPVPPME
     RQESVELTVQ QKVFHIANEL LQTEKAYVSR LHLLDQVFCA RLLEEARNRS SFPADVVHGI
     FSNICSIYCF HQQFLLPELE KRMEEWDRYP RIGDILQKLA PFLKMYGEYV KNFDRAVELV
     NTWTERSTQF KVIIHEVQKE EACRNLTLQH HMLEPVQRIP RYELLLKDYL LKLPHGSPDS
     KDAQKSLELI ATAAEHSNAA IRKMERMHKL LKVYELLGGE EDIVSPTKEL IKEGHILKLS
     AKNGTTQDRY LILFNDRLLY CVPRLRLLGQ KFTVRARIDV DGMELKESSN LNMPRTFLVS
     GKQRSLELQA RTEEEKKDWV QAINSTLLKH EQTLETFKLL NSTNRDDEDT PPNSPNVDLG
     KRAPTPIREK EVTMCMRCQE PFNSITKRRH HCKACGHVVC GKCSEFRARL IYDNNRSNRV
     CTDCYVALHG APGSSPACSQ HTPQRRRSIL EKQASVAAEN SVICSFLHYM EKGGKGWHKA
     WFVVPENEPL VLYIYGAPQD VKAQRSLPLI GFEVGPPEAG ERPDRRHVFK ITQSHLSWYF
     SPETEELQRR WMAVLGRAGR GDTFCPGPTL SEDKEMEETP VAASGATAEP PEASQTRDKT
//
ID   EFNB1_MOUSE             Reviewed;         345 AA.
AC   P52795;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Ephrin-B1;
DE   AltName: Full=CEK5 receptor ligand;
DE            Short=CEK5-L;
DE   AltName: Full=ELK ligand;
DE            Short=ELK-L;
DE   AltName: Full=EPH-related receptor tyrosine kinase ligand 2;
DE            Short=LERK-2;
DE   AltName: Full=Stimulated by retinoic acid gene 1 protein;
DE   Flags: Precursor;
GN   Name=Efnb1; Synonyms=Epl2, Eplg2, Lerk2, Stra1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=95203867; PubMed=7896266; DOI=10.1006/geno.1994.1589;
RA   Fletcher F.A., Renshaw B., Hollingsworth T., Baum P., Lyman S.D.,
RA   Jenkins N.A., Gilbert D.J., Copeland N.G., Davison B.L.;
RT   "Genomic organization and chromosomal localization of mouse Eplg2, a
RT   gene encoding a binding protein for the receptor tyrosine kinase
RT   elk.";
RL   Genomics 24:127-132(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=95377533; PubMed=7649373; DOI=10.1006/dbio.1995.1226;
RA   Bouillet P., Oulad-Abdelghani M., Vicaire S., Garnier J.-M.,
RA   Schuhbaur B., Dolle P., Chambon P.;
RT   "Efficient cloning of cDNAs of retinoic acid-responsive genes in P19
RT   embryonal carcinoma cells and characterization of a novel mouse gene,
RT   Stra1 (mouse LERK-2/Eplg2).";
RL   Dev. Biol. 170:420-433(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=95014510; PubMed=7929389;
RA   Shao H., Lou L., Pandey A., Pasquale E.B., Dixit V.M.;
RT   "cDNA cloning and characterization of a ligand for the Cek5 receptor
RT   protein-tyrosine kinase.";
RL   J. Biol. Chem. 269:26606-26609(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION.
RX   MEDLINE=20171264; PubMed=10704386;
RA   Imondi R., Wideman C., Kaprielian Z.;
RT   "Complementary expression of transmembrane ephrins and their receptors
RT   in the mouse spinal cord: a possible role in constraining the
RT   orientation of longitudinally projecting axons.";
RL   Development 127:1397-1410(2000).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Binds to the receptor tyrosine kinases EPHB1 and EPHA1.
CC       Binds to, and induce the collapse of, commissural axons/growth
CC       cones in vitro. May play a role in constraining the orientation of
CC       longitudinally projecting axons.
CC   -!- SUBUNIT: Interacts with GRIP1 and GRIP2.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Expressed on lateral floor plate cells,
CC       specifically on commissural axon segments that have passed through
CC       the floor plate. Expressed in cells of the retinal ganglion cell
CC       layer during retinal axon guidance to the optic disc.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the floor plate throughout the
CC       period of commissural axon pathfinding.
CC   -!- PTM: Inducible phosphorylation of tyrosine residues in the
CC       cytoplasmic domain.
CC   -!- SIMILARITY: Belongs to the ephrin family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U07602; AAC53247.1; -; Genomic_DNA.
DR   EMBL; U07598; AAC53247.1; JOINED; Genomic_DNA.
DR   EMBL; U07599; AAC53247.1; JOINED; Genomic_DNA.
DR   EMBL; U07600; AAC53247.1; JOINED; Genomic_DNA.
DR   EMBL; Z48781; CAA88695.1; -; mRNA.
DR   EMBL; U12983; AAA53231.1; -; mRNA.
DR   EMBL; BC006797; AAH06797.1; -; mRNA.
DR   EMBL; BC021656; AAH21656.1; -; mRNA.
DR   IPI; IPI00130754; -.
DR   PIR; I48780; I48780.
DR   RefSeq; NP_034240.1; NM_010110.4.
DR   UniGene; Mm.3374; -.
DR   ProteinModelPortal; P52795; -.
DR   SMR; P52795; 32-167.
DR   DIP; DIP-29206N; -.
DR   MINT; MINT-1793539; -.
DR   STRING; P52795; -.
DR   PhosphoSite; P52795; -.
DR   PRIDE; P52795; -.
DR   Ensembl; ENSMUST00000052839; ENSMUSP00000050716; ENSMUSG00000031217.
DR   GeneID; 13641; -.
DR   KEGG; mmu:13641; -.
DR   UCSC; uc009tvi.1; mouse.
DR   CTD; 13641; -.
DR   MGI; MGI:102708; Efnb1.
DR   eggNOG; roNOG10301; -.
DR   HOGENOM; HBG443543; -.
DR   HOVERGEN; HBG051448; -.
DR   InParanoid; P52795; -.
DR   OMA; MATQAPG; -.
DR   OrthoDB; EOG4W3SNT; -.
DR   PhylomeDB; P52795; -.
DR   NextBio; 284342; -.
DR   ArrayExpress; P52795; -.
DR   Bgee; P52795; -.
DR   CleanEx; MM_EFNB1; -.
DR   Genevestigator; P52795; -.
DR   GermOnline; ENSMUSG00000031217; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045121; C:membrane raft; IDA:MGI.
DR   GO; GO:0046875; F:ephrin receptor binding; IPI:MGI.
DR   GO; GO:0007411; P:axon guidance; IMP:MGI.
DR   GO; GO:0009880; P:embryonic pattern specification; IMP:MGI.
DR   GO; GO:0001755; P:neural crest cell migration; IMP:MGI.
DR   GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:MGI.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR001799; Ephrin.
DR   InterPro; IPR019765; Ephrin_CS.
DR   Gene3D; G3DSA:2.60.40.420; Cupredoxin; 1.
DR   PANTHER; PTHR11304; Ephrin; 1.
DR   Pfam; PF00812; Ephrin; 1.
DR   PRINTS; PR01347; EPHRIN.
DR   ProDom; PD002533; Ephrin; 1.
DR   SUPFAM; SSF49503; Cupredoxin; 1.
DR   PROSITE; PS01299; EPHRIN; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW   Membrane; Neurogenesis; Phosphoprotein; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25    345       Ephrin-B1.
FT                                /FTId=PRO_0000008388.
FT   TOPO_DOM     25    236       Extracellular (Potential).
FT   TRANSMEM    237    257       Helical; (Potential).
FT   TOPO_DOM    258    345       Cytoplasmic (Potential).
FT   MOTIF       343    345       PDZ-binding (Potential).
FT   MOD_RES     286    286       Phosphoserine.
FT   MOD_RES     312    312       Phosphotyrosine (By similarity).
FT   MOD_RES     316    316       Phosphotyrosine (By similarity).
FT   CARBOHYD    139    139       N-linked (GlcNAc...) (Potential).
FT   DISULFID     64    101       By similarity.
FT   DISULFID     89    153       By similarity.
FT   CONFLICT     90     90       S -> T (in Ref. 2; AAA53231).
SQ   SEQUENCE   345 AA;  37859 MW;  8C96FD3DC5CBC405 CRC64;
     MARPGQRWLS KWLVAMVVLT LCRLATPLAK NLEPVSWSSL NPKFLSGKGL VIYPKIGDKL
     DIICPRAEAG RPYEYYKLYL VRPEQAAACS TVLDPNVLVT CNKPHQEIRF TIKFQEFSPN
     YMGLEFKKYH DYYITSTSNG SLEGLENREG GVCRTRTMKI VMKVGQDPNA VTPEQLTTSR
     PSKESDNTVK TATQAPGRGS QGDSDGKHET VNQEEKSGPG AGGGGSGDSD SFFNSKVALF
     AAVGAGCVIF LLIIIFLTVL LLKLRKRHRK HTQQRAAALS LSTLASPKGG SGTAGTEPSD
     IIIPLRTTEN NYCPHYEKVS GDYGHPVYIV QEMPPQSPAN IYYKV
//
ID   EFNB2_MOUSE             Reviewed;         336 AA.
AC   P52800;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Ephrin-B2;
DE   AltName: Full=ELF-2;
DE   AltName: Full=EPH-related receptor tyrosine kinase ligand 5;
DE            Short=LERK-5;
DE   AltName: Full=HTK ligand;
DE            Short=HTK-L;
DE   Flags: Precursor;
GN   Name=Efnb2; Synonyms=Elf2, Epl5, Eplg5, Htkl, Lerk5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96145238; PubMed=8559144; DOI=10.1016/0161-5890(95)00108-5;
RA   Cerretti D.P., Vanden Bos T., Nelson N., Kozlosky C.J., Reddy P.,
RA   Maraskovsky E., Park L.S., Lyman S.D., Copeland N.G., Gilbert D.J.,
RA   Jenkins N.A., Fletcher R.A.;
RT   "Isolation of LERK-5: a ligand of the eph-related receptor tyrosine
RT   kinases.";
RL   Mol. Immunol. 32:1197-1205(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CB57BL/6J X SJL/J;
RX   MEDLINE=95199254; PubMed=7534404; DOI=10.1073/pnas.92.6.1866;
RA   Bennett B.D., Zeigler F.C., Gu Q., Fendly B., Goddard A.D.,
RA   Gillett N., Matthews W.;
RT   "Molecular cloning of a ligand for the EPH-related receptor protein-
RT   tyrosine kinase Htk.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:1866-1870(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=95379837; PubMed=7651410;
RA   Bergemann A.D., Cheng H.J., Brambilla R., Klein R., Flanagan J.G.;
RT   "ELF-2, a new member of the Eph ligand family, is segmentally
RT   expressed in mouse embryos in the region of the hindbrain and newly
RT   forming somites.";
RL   Mol. Cell. Biol. 15:4921-4929(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION.
RX   MEDLINE=20171264; PubMed=10704386;
RA   Imondi R., Wideman C., Kaprielian Z.;
RT   "Complementary expression of transmembrane ephrins and their receptors
RT   in the mouse spinal cord: a possible role in constraining the
RT   orientation of longitudinally projecting axons.";
RL   Development 127:1397-1410(2000).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 30-170.
RX   PubMed=11703926; DOI=10.1016/S1534-5807(01)00002-8;
RA   Toth J., Cutforth T., Gelinas A.D., Bethoney K.A., Bard J.,
RA   Harrison C.J.;
RT   "Crystal structure of an ephrin ectodomain.";
RL   Dev. Cell 1:83-92(2001).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 31-168 IN COMPLEX WITH EPHB2.
RX   PubMed=11780069; DOI=10.1038/414933a;
RA   Himanen J.-P., Rajashankar K.R., Lackmann M., Cowan C.A.,
RA   Henkemeyer M., Nikolov D.B.;
RT   "Crystal structure of an Eph receptor-ephrin complex.";
RL   Nature 414:933-938(2001).
CC   -!- FUNCTION: Binds to the receptor tyrosine kinases, such as EPHA4,
CC       EPHB4 and EPHA3. May play a role in constraining the orientation
CC       of longitudinally projecting axons.
CC   -!- SUBUNIT: Interacts with PDZRN3. Binds to the receptor tyrosine
CC       kinases EPHA4, EPHB4 and EPHA3 (By similarity).
CC   -!- INTERACTION:
CC       Q03137:Epha4; NbExp=1; IntAct=EBI-1032676, EBI-1539152;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Expressed on lateral floor plate cells,
CC       specifically on commissural axon segments that have passed through
CC       the floor plate. Expressed in cells of the retinal ganglion cell
CC       layer during retinal axon guidance to the optic disk.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the floor plate throughout the
CC       period of commissural axon pathfinding.
CC   -!- PTM: Inducible phosphorylation of tyrosine residues in the
CC       cytoplasmic domain (By similarity).
CC   -!- SIMILARITY: Belongs to the ephrin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC42052.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U16819; AAA99708.1; -; mRNA.
DR   EMBL; L38847; AAC42052.1; ALT_INIT; mRNA.
DR   EMBL; U30244; AAA82934.1; -; mRNA.
DR   EMBL; BC057009; AAH57009.1; -; mRNA.
DR   IPI; IPI00762720; -.
DR   PIR; I49766; I49766.
DR   RefSeq; NP_034241.2; NM_010111.5.
DR   UniGene; Mm.209813; -.
DR   PDB; 1IKO; X-ray; 1.92 A; P=30-207.
DR   PDB; 1KGY; X-ray; 2.70 A; E/F/G/H=31-168.
DR   PDBsum; 1IKO; -.
DR   PDBsum; 1KGY; -.
DR   ProteinModelPortal; P52800; -.
DR   SMR; P52800; 30-170.
DR   DIP; DIP-29208N; -.
DR   IntAct; P52800; 3.
DR   MINT; MINT-1959060; -.
DR   STRING; P52800; -.
DR   PhosphoSite; P52800; -.
DR   PRIDE; P52800; -.
DR   Ensembl; ENSMUST00000001319; ENSMUSP00000001319; ENSMUSG00000001300.
DR   GeneID; 13642; -.
DR   KEGG; mmu:13642; -.
DR   UCSC; uc009kue.1; mouse.
DR   CTD; 13642; -.
DR   MGI; MGI:105097; Efnb2.
DR   eggNOG; roNOG10301; -.
DR   HOVERGEN; HBG051448; -.
DR   OrthoDB; EOG402WSK; -.
DR   PhylomeDB; P52800; -.
DR   NextBio; 284346; -.
DR   ArrayExpress; P52800; -.
DR   Bgee; P52800; -.
DR   CleanEx; MM_EFNB2; -.
DR   CleanEx; MM_ELF2; -.
DR   Genevestigator; P52800; -.
DR   GermOnline; ENSMUSG00000001300; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005102; F:receptor binding; IPI:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0001945; P:lymph vessel development; IMP:MGI.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0007219; P:Notch signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0009887; P:organ morphogenesis; IMP:MGI.
DR   InterPro; IPR008972; Cupredoxin.
DR   InterPro; IPR001799; Ephrin.
DR   InterPro; IPR019765; Ephrin_CS.
DR   Gene3D; G3DSA:2.60.40.420; Cupredoxin; 1.
DR   PANTHER; PTHR11304; Ephrin; 1.
DR   Pfam; PF00812; Ephrin; 1.
DR   PRINTS; PR01347; EPHRIN.
DR   ProDom; PD002533; Ephrin; 1.
DR   SUPFAM; SSF49503; Cupredoxin; 1.
DR   PROSITE; PS01299; EPHRIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Developmental protein; Differentiation; Disulfide bond;
KW   Glycoprotein; Membrane; Neurogenesis; Phosphoprotein; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     28       Potential.
FT   CHAIN        29    336       Ephrin-B2.
FT                                /FTId=PRO_0000008393.
FT   TOPO_DOM     29    232       Extracellular (Potential).
FT   TRANSMEM    233    253       Helical; (Potential).
FT   TOPO_DOM    254    336       Cytoplasmic (Potential).
FT   MOTIF       334    336       PDZ-binding (Potential).
FT   MOD_RES     307    307       Phosphotyrosine (By similarity).
FT   MOD_RES     314    314       Phosphotyrosine (By similarity).
FT   MOD_RES     319    319       Phosphotyrosine (By similarity).
FT   MOD_RES     328    328       Phosphoserine (By similarity).
FT   MOD_RES     333    333       Phosphotyrosine (By similarity).
FT   CARBOHYD     39     39       N-linked (GlcNAc...).
FT   CARBOHYD    142    142       N-linked (GlcNAc...) (Potential).
FT   DISULFID     65    104
FT   DISULFID     92    156
FT   CONFLICT    177    177       A -> T (in Ref. 1; AAA99708).
FT   TURN         47     49
FT   STRAND       50     53
FT   STRAND       60     64
FT   STRAND       70     72
FT   STRAND       78     84
FT   HELIX        86     91
FT   STRAND      101    104
FT   STRAND      112    116
FT   STRAND      133    138
FT   HELIX       145    147
FT   HELIX       154    158
FT   STRAND      162    167
SQ   SEQUENCE   336 AA;  37202 MW;  D08894996E399554 CRC64;
     MAMARSRRDS VWKYCWGLLM VLCRTAISRS IVLEPIYWNS SNSKFLPGQG LVLYPQIGDK
     LDIICPKVDS KTVGQYEYYK VYMVDKDQAD RCTIKKENTP LLNCARPDQD VKFTIKFQEF
     SPNLWGLEFQ KNKDYYIIST SNGSLEGLDN QEGGVCQTRA MKILMKVGQD ASSAGSARNH
     GPTRRPELEA GTNGRSSTTS PFVKPNPGSS TDGNSAGHSG NNLLGSEVAL FAGIASGCII
     FIVIIITLVV LLLKYRRRHR KHSPQHTTTL SLSTLATPKR GGNNNGSEPS DVIIPLRTAD
     SVFCPHYEKV SGDYGHPVYI VQEMPPQSPA NIYYKV
//
ID   CUX1_MOUSE              Reviewed;        1515 AA.
AC   P53564; O08994; P70301; Q571L6; Q91ZD2;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 3.
DT   11-JAN-2011, entry version 100.
DE   RecName: Full=Homeobox protein cut-like 1;
DE   AltName: Full=CCAAT displacement protein;
DE            Short=CDP;
DE   AltName: Full=Homeobox protein cux-1;
GN   Name=Cux1; Synonyms=Cutl1, Cux, Kiaa4047;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC   STRAIN=A/J, and BALB/c; TISSUE=Brain;
RX   MEDLINE=94244481; PubMed=7910552;
RA   Valarche I., Tissier-Seta J.-P., Hirsch M.R., Martinez S., Goridis C.,
RA   Brunet J.-F.;
RT   "The mouse homeodomain protein Phox2 regulates Ncam promoter activity
RT   in concert with Cux/CDP and is a putative determinant of
RT   neurotransmitter phenotype.";
RL   Development 119:881-896(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Testis;
RX   PubMed=8879483;
RA   Vanden Heuvel G.B., Quaggin S.E., Igarashi P.;
RT   "A unique variant of a homeobox gene related to Drosophila cut is
RT   expressed in mouse testis.";
RL   Biol. Reprod. 55:731-739(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND FUNCTION.
RX   MEDLINE=21429086; PubMed=11544187; DOI=10.1101/gad.200101;
RA   Ellis T., Gambardella L., Horcher M., Tschanz S., Capol J.,
RA   Bertram P., Jochum W., Barrandon Y., Busslinger M.;
RT   "The transcriptional repressor CDP (Cutl1) is essential for epithelial
RT   cell differentiation of the lung and the hair follicle.";
RL   Genes Dev. 15:2307-2319(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Embryonic tail;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 121-1515 (ISOFORM 2), AND FUNCTION.
RC   STRAIN=C57BL/6N;
RX   PubMed=9858552;
RA   Wang Z., Goldstein A., Zong R.-T., Lin D., Neufeld E.J.,
RA   Scheuermann R.H., Tucker P.W.;
RT   "Cux/CDP homeoprotein is a component of NF-muNR and represses the
RT   immunoglobulin heavy chain intronic enhancer by antagonizing the
RT   bright transcription activator.";
RL   Mol. Cell. Biol. 19:284-295(1999).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 762-1515 (ISOFORMS 2/3/4/5).
RX   MEDLINE=96437626; PubMed=8840273; DOI=10.1038/ki.1996.336;
RA   Vanden Heuvel G.B., Bodmer R., McConnell K.R., Nagami G.T.,
RA   Igarashi P.;
RT   "Expression of a cut-related homeobox gene in developing and
RT   polycystic mouse kidney.";
RL   Kidney Int. 50:453-461(1996).
RN   [7]
RP   INTERACTION WITH SATB1.
RX   PubMed=10373541;
RA   Liu J., Barnett A., Neufeld E.J., Dudley J.P.;
RT   "Homeoproteins CDP and SATB1 interact: potential for tissue-specific
RT   regulation.";
RL   Mol. Cell. Biol. 19:4918-4926(1999).
RN   [8]
RP   FUNCTION, INTERACTION WITH BANP, AND SUBCELLULAR LOCATION.
RX   PubMed=15371550; DOI=10.1093/nar/gkh807;
RA   Kaul-Ghanekar R., Jalota-Badhwar A., Pavithra L., Tucker P.,
RA   Chattopadhyay S.;
RT   "SMAR1 and Cux/CDP modulate chromatin and act as negative regulators
RT   of the TCRbeta enhancer (Ebeta).";
RL   Nucleic Acids Res. 32:4862-4875(2004).
CC   -!- FUNCTION: Probably has a broad role in mammalian development as a
CC       repressor of developmentally regulated gene expression. May act by
CC       preventing binding of positively-activing CCAAT factors to
CC       promoters. Component of nf-munr repressor; binds to the matrix
CC       attachment regions (MARs) (5' and 3') of the immunoglobulin heavy
CC       chain enhancer. Represses T-cell receptor (TCR) beta enhancer
CC       function by binding to MARbeta, an ATC-rich DNA sequence located
CC       upstream of the TCR beta enhancer.
CC   -!- SUBUNIT: Interacts with BANP. Interaction with SATB1 via DNA-
CC       binding domains inhibits the attachment to DNA.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=5;
CC         IsoId=P53564-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P53564-2; Sequence=VSP_002311;
CC       Name=3;
CC         IsoId=P53564-3; Sequence=VSP_015749, VSP_015750;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=P53564-4; Sequence=VSP_015748;
CC       Name=6;
CC         IsoId=P53564-5; Sequence=VSP_017360;
CC       Name=1; Synonyms=CASP;
CC         IsoId=P70403-1; Sequence=External;
CC   -!- TISSUE SPECIFICITY: Isoform 6 is testis-specific where it is
CC       expressed in germ cells.
CC   -!- DEVELOPMENTAL STAGE: In postpubertal testis, isoform 6 is
CC       expressed from stages IV-V of spermatogenesis in the outer layer
CC       of round spermatids. Expression continues through stages VI-VII
CC       but no expression is detected in stages IX-XI. In prepubertal
CC       testis, isoform 6 is expressed in post-meiotic germ cells at the
CC       round spermatid stage.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- MISCELLANEOUS: Asn-1285 may participate in regulating DNA-binding
CC       activity by promoting homo- and heterodimerization.
CC   -!- SIMILARITY: Belongs to the CUT homeobox family.
CC   -!- SIMILARITY: Contains 3 CUT DNA-binding domains.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90358.1; Type=Erroneous initiation;
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DR   EMBL; X75013; CAA52922.1; -; mRNA.
DR   EMBL; U46684; AAB41146.1; -; mRNA.
DR   EMBL; AY037807; AAK59986.1; -; mRNA.
DR   EMBL; AK220173; BAD90358.1; ALT_INIT; mRNA.
DR   EMBL; AF004225; AAD12485.1; -; mRNA.
DR   EMBL; U46683; AAC52775.1; -; mRNA.
DR   IPI; IPI00227934; -.
DR   IPI; IPI00652887; -.
DR   IPI; IPI00653608; -.
DR   IPI; IPI00742435; -.
DR   IPI; IPI00776206; -.
DR   PIR; I48314; I48314.
DR   RefSeq; NP_034116.3; NM_009986.3.
DR   UniGene; Mm.320317; -.
DR   ProteinModelPortal; P53564; -.
DR   SMR; P53564; 545-633, 929-1019, 1111-1296.
DR   IntAct; P53564; 1.
DR   STRING; P53564; -.
DR   PhosphoSite; P53564; -.
DR   PRIDE; P53564; -.
DR   Ensembl; ENSMUST00000004097; ENSMUSP00000004097; ENSMUSG00000029705.
DR   Ensembl; ENSMUST00000111111; ENSMUSP00000106740; ENSMUSG00000029705.
DR   GeneID; 13047; -.
DR   KEGG; mmu:13047; -.
DR   UCSC; uc009aao.1; mouse.
DR   UCSC; uc009aap.1; mouse.
DR   UCSC; uc009aaq.1; mouse.
DR   UCSC; uc009aas.1; mouse.
DR   CTD; 13047; -.
DR   MGI; MGI:88568; Cux1.
DR   HOGENOM; HBG443591; -.
DR   HOVERGEN; HBG051268; -.
DR   InParanoid; P53564; -.
DR   PhylomeDB; P53564; -.
DR   ArrayExpress; P53564; -.
DR   Bgee; P53564; -.
DR   CleanEx; MM_CUX1; -.
DR   Genevestigator; P53564; -.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0016564; F:transcription repressor activity; IDA:MGI.
DR   GO; GO:0042491; P:auditory receptor cell differentiation; IMP:MGI.
DR   GO; GO:0030324; P:lung development; IMP:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   InterPro; IPR003350; Hmoeo_CUT.
DR   InterPro; IPR001356; Homeobox.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR010982; Lambda_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Pfam; PF02376; CUT; 3.
DR   Pfam; PF00046; Homeobox; 1.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
DR   SUPFAM; SSF47413; Lambda_like_DNA; 3.
DR   PROSITE; PS51042; CUT; 3.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Developmental protein; DNA-binding;
KW   Homeobox; Nucleus; Phosphoprotein; Repeat; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   1515       Homeobox protein cut-like 1.
FT                                /FTId=PRO_0000202394.
FT   DNA_BIND    540    627       CUT 1.
FT   DNA_BIND    929   1016       CUT 2.
FT   DNA_BIND   1112   1199       CUT 3.
FT   DNA_BIND   1239   1298       Homeobox.
FT   COILED      121    363       Potential.
FT   COILED      667    723       Potential.
FT   MOD_RES     320    320       Phosphoserine (By similarity).
FT   MOD_RES    1049   1049       Phosphoserine (By similarity).
FT   MOD_RES    1054   1054       Phosphoserine (By similarity).
FT   MOD_RES    1213   1213       Phosphoserine (By similarity).
FT   MOD_RES    1227   1227       Phosphotyrosine (By similarity).
FT   MOD_RES    1228   1228       Phosphoserine (By similarity).
FT   MOD_RES    1307   1307       Phosphoserine (By similarity).
FT   MOD_RES    1506   1506       Phosphoserine (By similarity).
FT   VAR_SEQ       1   1055       Missing (in isoform 6).
FT                                /FTId=VSP_017360.
FT   VAR_SEQ       1    183       Missing (in isoform 4).
FT                                /FTId=VSP_015748.
FT   VAR_SEQ       1     10       MLCVAGAKLK -> MAANVGSMFQYWKRFDLQQLQ (in
FT                                isoform 3).
FT                                /FTId=VSP_015749.
FT   VAR_SEQ     406    507       Missing (in isoform 2).
FT                                /FTId=VSP_002311.
FT   VAR_SEQ     630    651       Missing (in isoform 3).
FT                                /FTId=VSP_015750.
FT   CONFLICT    276    276       V -> VEQ (in Ref. 3; AAK59986).
FT   CONFLICT    649    649       R -> G (in Ref. 1; CAA52922 and 5;
FT                                AAD12485).
FT   CONFLICT   1480   1480       G -> A (in Ref. 1; CAA52922).
FT   CONFLICT   1485   1485       P -> L (in Ref. 5; AAD12485).
SQ   SEQUENCE   1515 AA;  165596 MW;  72BC6E8D8ECD78DE CRC64;
     MLCVAGAKLK RELDATATVL ANRQDESEQS RKRLIEQSRE FKKNTPEDLR KQVAPLLKSF
     QGEIDALSKR SKEAEAAFLT VYKRLIDVPD PVPALDVGQQ LEIKVQRLHD IETENQKLRE
     TLEEYNKEFA EVKNQEVTIK ALKEKIREYE QTLKSQAETI ALEKEQKLQN DFAEKERKLQ
     ETQMSTTSKL EEAEHKLQTL QTALEKTRTE LFDLKTKYDE ETTAKADEIE MIMTDLERAN
     QRAEVAQREA ETLREQLSSA NHSLQLASQI QKAPDVAIEV LTRSSLEVEL AAKEREIAQL
     VEDVQRLQAS LTKLRENSAS QISQLEQQLN AKNSTLKQLE EKLKGQADYE EVKKELNTLK
     SMEFAPSEGA GTQDSTKPLE VLLLEKNRSL QSENATLRIS NSDLSGSARR KGRDQPESRR
     PGPLPASPPP QLPRNTGEQV SNTNGTHHFS PAGLSQDFFS SNLASPSLPL ASTGKFALNS
     LLQRQLMQSF YSKAMQEAGS TSTIFSTGPY STNSISSPSP LQQSPDVNGM APSPSQSESA
     GSISEGEEID TAEIARQVKE QLIKHNIGQR IFGHYVLGLS QGSVSEILAR PKPWNKLTVR
     GKEPFHKMKQ FLSDEQNILA LRSIQGRQRE NPGQSLNRLF QEVPKRRNRS EGNITTRIRA
     SETGSDEAIK SILEQAKREL QVQKTAEPVQ TSSTSSSGNS DDAIRSILQQ ARREMEAQQA
     ALDPALKPAP LSQPDLTILT PKHLSASPMS TVSTYPPLAI SLKKTPAAPE TSTAALPSAP
     ALKKEAQDVP TLDPPGSADA AQGVLRPMKS ELVRGSTWKD PWWSPIQPER RNLTSSEETK
     ADETTASGKE RAGSSQPRAE RSQLQGPSAS AEYWKEWPSA ESPYSQSSEL SLTGASRSET
     PQNSPLPSSP IVPMAKPAKP SVPPLTPEQY EVYMYQEVDT IELTRQVKEK LAKNGICQRI
     FGEKVLGLSQ GSVSDMLSRP KPWSKLTQKG REPFIRMQLW LNGELGQGVL PVQGQQQGPV
     LHSVASLQDP LQQGCVSSES TPKTSASCSP APESPMSSSE SVKSLTELVQ QPCPAIETSK
     EGKPPEPSDP PASDSQPTTP LPLSGHSALS IQELVAMSPE LDTYGITKRV KEVLTDNNLG
     QRLFGETILG LTQGSVSDLL ARPKPWHKLS LKGREPFVRM QLWLNDPNNV EKLMDMKRME
     KKAYMKRRHS SVSDSQPCEP PSVGIDYSQG ASPQPQHQLK KPRVVLAPEE KEALKRAYQQ
     KPYPSPKTIE ELATQLNLKT STVINWFHNY RSRIRRELFI EEIQAGSQGQ AGASDSPSAR
     SSRAAPSSEG DSCDGVEATD AEEPGGNIVA TKSQGGLAEV AAAPADREEA TQPAEKAKAQ
     PLCSGTPGQD DGEDASRPRP LPEGLADAPA PVPSLAAPAA GEDAATSATA PATATEAPGA
     ARAGPAERSS ALPSTSAPAN APARRPSSLQ SLFGLPEAAG ARDNPVRKKK AANLNSIIHR
     LEKAASREEP IEWEF
//
ID   LIMK1_MOUSE             Reviewed;         647 AA.
AC   P53668;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAR-2011, entry version 105.
DE   RecName: Full=LIM domain kinase 1;
DE            Short=LIMK-1;
DE            EC=2.7.11.1;
DE   AltName: Full=KIZ-1;
GN   Name=Limk1; Synonyms=Limk;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=96017801; PubMed=7478547;
RA   Proeschel C., Blouin M.J., Gutowski N.J., Ludwig R., Noble M.;
RT   "Limk1 is predominantly expressed in neural tissues and phosphorylates
RT   serine, threonine and tyrosine residues in vitro.";
RL   Oncogene 11:1271-1281(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CD-1;
RX   MEDLINE=96081363; PubMed=8541208; DOI=10.1016/0925-4773(95)00400-U;
RA   Cheng A.K., Robertson E.J.;
RT   "The murine LIM-kinase gene (limk) encodes a novel serine threonine
RT   kinase expressed predominantly in trophoblast giant cells and the
RT   developing nervous system.";
RL   Mech. Dev. 52:187-197(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   MEDLINE=20458868; PubMed=11003705; DOI=10.1007/s003350010166;
RA   Martindale D.W., Wilson M.D., Wang D., Burke R.D., Chen X.,
RA   Duronio V., Koop B.F.;
RT   "Comparative genomic sequence analysis of the Williams syndrome region
RT   (LIMK1-RFC2) of human chromosome 7q11.23.";
RL   Mamm. Genome 11:890-898(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 15-647.
RC   STRAIN=BALB/c;
RX   MEDLINE=95151637; PubMed=7848918;
RA   Bernard O., Ganiatsas S., Kannourakis G., Dringen R.;
RT   "Kiz-1, a protein with LIM zinc finger and kinase domains, is
RT   expressed mainly in neurons.";
RL   Cell Growth Differ. 5:1159-1171(1994).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-460.
RX   PubMed=15056216; DOI=10.1111/j.1462-5822.2004.00375.x;
RA   Dai S., Sarmiere P.D., Wiggan O., Bamburg J.R., Zhou D.;
RT   "Efficient Salmonella entry requires activity cycles of host ADF and
RT   cofilin.";
RL   Cell. Microbiol. 6:459-471(2004).
RN   [7]
RP   INTERACTION WITH SSH1.
RX   PubMed=15660133; DOI=10.1038/sj.emboj.7600543;
RA   Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N.,
RA   Sarcevic B., Sampath R., Bamburg J.R., Bernard O.;
RT   "Interplay between components of a novel LIM kinase-slingshot
RT   phosphatase complex regulates cofilin.";
RL   EMBO J. 24:473-486(2005).
RN   [8]
RP   FUNCTION, INTERACTION WITH RLIM AND RNF6, UBIQUITINATION BY RLIM AND
RP   RNF6, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=16204183; DOI=10.1101/gad.1340605;
RA   Tursun B., Schlueter A., Peters M.A., Viehweger B., Ostendorff H.P.,
RA   Soosairajah J., Drung A., Bossenz M., Johnsen S.A., Schweizer M.,
RA   Bernard O., Bach I.;
RT   "The ubiquitin ligase Rnf6 regulates local LIM kinase 1 levels in
RT   axonal growth cones.";
RL   Genes Dev. 19:2307-2319(2005).
RN   [9]
RP   INTERACTION WITH NISCH.
RX   PubMed=18332102; DOI=10.1128/MCB.01832-07;
RA   Ding Y., Milosavljevic T., Alahari S.K.;
RT   "Nischarin inhibits LIM kinase to regulate cofilin phosphorylation and
RT   cell invasion.";
RL   Mol. Cell. Biol. 28:3742-3756(2008).
CC   -!- FUNCTION: Protein kinase which regulates actin filament dynamics.
CC       Phosphorylates and inactivates the actin binding/depolymerizing
CC       factor cofilin, thereby stabilizing the actin cytoskeleton.
CC       Stimulates axonal outgrowth and may be involved in brain
CC       development.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Self-associates. Binds ROCK1 (By similarity). Interacts
CC       with TPPP (By similarity). The LIM domain interacts with the
CC       cytoplasmic domain of NRG1. Interacts with NISCH and SSH1.
CC       Interacts with RLIM and RNF6.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell projection, growth cone.
CC   -!- TISSUE SPECIFICITY: Highest expression in the nervous system,
CC       particularly in the spinal cord and the cranial nerve and dorsal
CC       root ganglia.
CC   -!- DEVELOPMENTAL STAGE: Expressed in ventral neural tube and axonal
CC       projections at E12.5-E13 (at protein level).
CC   -!- PTM: Autophosphorylated.
CC   -!- PTM: Phosphorylated on serine and/or threonine residues by ROCK1.
CC       May be dephosphorylated and inactivated by SSH1 (By similarity).
CC   -!- PTM: Ubiquitinated. 'Lys-48'-linked polyubiquitination by RNF6
CC       leads to proteasomal degradation through the 26S proteasome,
CC       modulating LIMK1 levels in the growth cone and its effect on
CC       axonal outgrowth. Also polyubiquitinated by RLIM.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family.
CC   -!- SIMILARITY: Contains 2 LIM zinc-binding domains.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; X86569; CAA60377.1; -; mRNA.
DR   EMBL; U15159; AAC52254.1; -; mRNA.
DR   EMBL; AF139987; AAD34858.1; -; Genomic_DNA.
DR   EMBL; AF289665; AAF99334.1; -; Genomic_DNA.
DR   EMBL; U14166; AAC52147.1; -; mRNA.
DR   IPI; IPI00133642; -.
DR   PIR; I48737; I48737.
DR   RefSeq; NP_034847.1; NM_010717.2.
DR   UniGene; Mm.15409; -.
DR   ProteinModelPortal; P53668; -.
DR   SMR; P53668; 18-146, 153-260, 333-612.
DR   MINT; MINT-247675; -.
DR   STRING; P53668; -.
DR   PhosphoSite; P53668; -.
DR   PRIDE; P53668; -.
DR   Ensembl; ENSMUST00000015137; ENSMUSP00000015137; ENSMUSG00000029674.
DR   GeneID; 16885; -.
DR   KEGG; mmu:16885; -.
DR   UCSC; uc008zwt.1; mouse.
DR   CTD; 16885; -.
DR   MGI; MGI:104572; Limk1.
DR   eggNOG; roNOG08394; -.
DR   HOGENOM; HBG444279; -.
DR   HOVERGEN; HBG052328; -.
DR   InParanoid; P53668; -.
DR   OMA; CSASLSH; -.
DR   OrthoDB; EOG41C6VP; -.
DR   PhylomeDB; P53668; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 290892; -.
DR   ArrayExpress; P53668; -.
DR   Bgee; P53668; -.
DR   CleanEx; MM_LIMK1; -.
DR   Genevestigator; P53668; -.
DR   GermOnline; ENSMUSG00000029674; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR   GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045773; P:positive regulation of axon extension; IGI:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR001781; Znf_LIM.
DR   Gene3D; G3DSA:2.10.110.10; Znf_LIM; 2.
DR   Pfam; PF00412; LIM; 2.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00132; LIM; 2.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 2.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell projection; Cytoplasm; Kinase; LIM domain;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Repeat;
KW   Serine/threonine-protein kinase; Transferase; Ubl conjugation; Zinc.
FT   CHAIN         1    647       LIM domain kinase 1.
FT                                /FTId=PRO_0000075804.
FT   DOMAIN       25     75       LIM zinc-binding 1.
FT   DOMAIN       84    137       LIM zinc-binding 2.
FT   DOMAIN      165    258       PDZ.
FT   DOMAIN      339    604       Protein kinase.
FT   NP_BIND     345    353       ATP (By similarity).
FT   ACT_SITE    460    460       Probable.
FT   BINDING     368    368       ATP (By similarity).
FT   MOD_RES     210    210       Phosphoserine (By similarity).
FT   MOD_RES     229    229       Phosphothreonine (By similarity).
FT   MOD_RES     296    296       Phosphoserine (By similarity).
FT   MOD_RES     298    298       Phosphoserine (By similarity).
FT   MOD_RES     302    302       Phosphoserine (By similarity).
FT   MOD_RES     307    307       Phosphoserine (By similarity).
FT   MOD_RES     310    310       Phosphoserine (By similarity).
FT   MOD_RES     313    313       Phosphoserine (By similarity).
FT   MOD_RES     337    337       Phosphoserine (By similarity).
FT   MOD_RES     508    508       Phosphothreonine; by ROCK1 (By
FT                                similarity).
FT   MUTAGEN     460    460       D->G: Abrogates kinase activity.
FT   CONFLICT    200    201       RV -> EC (in Ref. 2; AAC52254).
FT   CONFLICT    269    271       DPS -> GSQ (in Ref. 2; AAC52254).
FT   CONFLICT    326    327       VV -> C (in Ref. 2; AAC52254).
FT   CONFLICT    523    523       G -> P (in Ref. 5; AAC52147).
SQ   SEQUENCE   647 AA;  72793 MW;  46E8992425A77883 CRC64;
     MRLTLLCCTW REERMGEEGS ELPVCASCGQ RIYDGQYLQA LNADWHADCF RCCECSVSLS
     HQYYEKDGQL FCKKDYWARY GESCHGCSEH ITKGLVMVAG ELKYHPECFI CLACGNFIGD
     GDTYTLVEHS KLYCGQCYYQ TVVTPVIEQI LPDSPGSHLP HTVTLVSIPA SAHGKRGLSV
     SIDPPHGPPG CGTEHSHTVR VQGVDPGCMS PDVKNSIHVG DRILEINGTP IRNVPLDEID
     LLIQETSRLL QLTLEHDPHD SLGHGPVSDP SPLSSPVHTP SGQAASSARQ KPVLRSCSID
     TSPGTSSLAS PASQRKDLGR SESLRVVCRP HRIFRPSDLI HGEVLGKGCF GQAIKVTHRE
     TGEVMVMKEL IRFDEETQRT FLKEVKVMRC LEHPNVLKFI GVLYKDKRLN FITEYIKGGT
     LRGIIKNMDS QYPWSQRVSF AKDIASGMAY LHSMNIIHRD LNSHNCLVRE NRNVVVADFG
     LARLMIDEKN QSEDLRSLKK PDRKKRYTVV GNPYWMAPEM INGRSYDEKV DVFSFGIVLC
     EIIGRVNADP DYLPRTMDFG LNVRGFLDRY CPPNCPPSFF PITVRCCDLD PEKRPSFVKL
     EQWLETLRMH LSGHLPLGPQ LEQLERGFWE TYRRGESSLP AHPEVPD
//
ID   SOX1_MOUSE              Reviewed;         391 AA.
AC   P53783;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Transcription factor SOX-1;
GN   Name=Sox1; Synonyms=Sox-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129;
RX   MEDLINE=96189340; PubMed=8625802;
RA   Collignon J., Sockanathan S., Hacker A., Cohen-Tannoudji M.,
RA   Norris D., Rastan S., Stevanovic M., Goodfellow P.N., Lovell-Badge R.;
RT   "A comparison of the properties of Sox-3 with Sry and two related
RT   genes, Sox-1 and Sox-2.";
RL   Development 122:509-520(1996).
CC   -!- FUNCTION: Transcriptional activator (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- TISSUE SPECIFICITY: Mainly in the developing central nervous
CC       system. Expressed in developing urogenital ridge.
CC   -!- SIMILARITY: Contains 1 HMG box DNA-binding domain.
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DR   EMBL; X94126; CAA63846.1; -; Genomic_DNA.
DR   IPI; IPI00134803; -.
DR   PIR; S10950; S10950.
DR   UniGene; Mm.39088; -.
DR   ProteinModelPortal; P53783; -.
DR   SMR; P53783; 49-127.
DR   STRING; P53783; -.
DR   PRIDE; P53783; -.
DR   Ensembl; ENSMUST00000116111; ENSMUSP00000111802; ENSMUSG00000079994.
DR   MGI; MGI:98357; Sox1.
DR   HOGENOM; HBG446398; -.
DR   HOVERGEN; HBG105663; -.
DR   InParanoid; P53783; -.
DR   OrthoDB; EOG4DFPQ1; -.
DR   ArrayExpress; P53783; -.
DR   Bgee; P53783; -.
DR   CleanEx; MM_SOX1; -.
DR   Genevestigator; P53783; -.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0021884; P:forebrain neuron development; IMP:MGI.
DR   GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR000910; HMG_HMG1/HMG2.
DR   InterPro; IPR009071; HMG_superfamily.
DR   InterPro; IPR022097; TF_SOX.
DR   Gene3D; G3DSA:1.10.30.10; HMG-box; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   Pfam; PF12336; SOXp; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Nucleus; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    391       Transcription factor SOX-1.
FT                                /FTId=PRO_0000048713.
FT   DNA_BIND     51    119       HMG box.
FT   COMPBIAS     30     43       Poly-Gly.
FT   COMPBIAS    145    150       Poly-Gly.
FT   COMPBIAS    197    204       Poly-Ala.
FT   COMPBIAS    280    288       Poly-Ala.
FT   COMPBIAS    296    306       Poly-Ala.
FT   COMPBIAS    357    364       Poly-Ala.
SQ   SEQUENCE   391 AA;  39237 MW;  9F81ED667F947C05 CRC64;
     MYSMMMETDL HSPGGAQAPT NLSGPAGARG GGGGGGGGGG GGGTKANQDR VKRPMNAFMV
     WSRGQRRKMA QENPKMHNSE ISKRLGAEWK VMSEAEKRPF IDEAKRLRAL HMKEHPDYKY
     RPRRKTKTLL KKDKYSLAGG LLAAGAGGGG AAVAMGVGVG VGAAAVGQRL ESPGGAAGGG
     YAHVNGWANG AYPGSVAAAA AAAAMMQEAQ LAYGQHPGAG GRHPHAHPAH PHPHHPHAHP
     HNPQPMHRYD MGALQYSPIS NSQGYMSASP SGYGGIPYGA AAAAAAAAGG AHQNSAVAAA
     AAAAAASSGA LGALGSLVKS EPSGSPPAPA HSRAPCPGDL REMISMYLPA GEGGDPAAAA
     AAAAQSRLHS LPQHYQGAGA GVNGTVPLTH I
//
ID   MOT1_MOUSE              Reviewed;         493 AA.
AC   P53986;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=Monocarboxylate transporter 1;
DE            Short=MCT 1;
DE   AltName: Full=Solute carrier family 16 member 1;
GN   Name=Slc16a1; Synonyms=Mct1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96177979; PubMed=8603082; DOI=10.1016/0005-2736(95)00254-5;
RA   Carpenter L., Poole R.C., Halestrap A.P.;
RT   "Cloning and sequencing of the monocarboxylate transporter from mouse
RT   Ehrlich Lettre tumour cell confirms its identity as MCT1 and
RT   demonstrates that glycosylation is not required for MCT1 function.";
RL   Biochim. Biophys. Acta 1279:157-163(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129; TISSUE=Kidney;
RX   MEDLINE=98400885; PubMed=9725820;
RA   Koehler-Stec E.M., Simpson I.A., Vannucci S.J., Landschulz K.T.,
RA   Landschulz W.H.;
RT   "Monocarboxylate transporter expression in mouse brain.";
RL   Am. J. Physiol. 275:E516-E524(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210 AND SER-213, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477 AND SER-491, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213 AND SER-491, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210; SER-213 AND
RP   SER-461, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213; SER-230; SER-461;
RP   THR-462 AND SER-491, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Proton-linked monocarboxylate transporter. Catalyzes the
CC       rapid transport across the plasma membrane of many
CC       monocarboxylates such as lactate, pyruvate, branched-chain oxo
CC       acids derived from leucine, valine and isoleucine, and the ketone
CC       bodies acetoacetate, beta-hydroxybutyrate and acetate.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Major isoform present in tumor cells,
CC       erythrocytes.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       Monocarboxylate porter (TC 2.A.1.13) family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; X82438; CAA57819.1; -; mRNA.
DR   EMBL; AF058055; AAC13720.1; -; mRNA.
DR   EMBL; BC014777; AAH14777.1; -; mRNA.
DR   IPI; IPI00137194; -.
DR   RefSeq; NP_033222.1; NM_009196.3.
DR   UniGene; Mm.9086; -.
DR   ProteinModelPortal; P53986; -.
DR   STRING; P53986; -.
DR   PhosphoSite; P53986; -.
DR   PRIDE; P53986; -.
DR   Ensembl; ENSMUST00000046212; ENSMUSP00000045216; ENSMUSG00000032902.
DR   GeneID; 20501; -.
DR   KEGG; mmu:20501; -.
DR   UCSC; uc008qui.1; mouse.
DR   CTD; 20501; -.
DR   MGI; MGI:106013; Slc16a1.
DR   eggNOG; roNOG13672; -.
DR   HOGENOM; HBG444740; -.
DR   HOVERGEN; HBG006384; -.
DR   InParanoid; P53986; -.
DR   OMA; RWIRPRV; -.
DR   OrthoDB; EOG41G341; -.
DR   PhylomeDB; P53986; -.
DR   NextBio; 298671; -.
DR   ArrayExpress; P53986; -.
DR   Bgee; P53986; -.
DR   Genevestigator; P53986; -.
DR   GermOnline; ENSMUSG00000032902; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015355; F:secondary active monocarboxylate transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0015711; P:organic anion transport; IEA:InterPro.
DR   InterPro; IPR020846; Major_facilitator_SF.
DR   InterPro; IPR011701; MFS_1.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   InterPro; IPR004743; Monocarb_transpt.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
DR   TIGRFAMs; TIGR00892; 2A0113; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Phosphoprotein; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    493       Monocarboxylate transporter 1.
FT                                /FTId=PRO_0000211383.
FT   TOPO_DOM      1     15       Cytoplasmic (Potential).
FT   TRANSMEM     16     36       Helical; (Potential).
FT   TOPO_DOM     37     59       Extracellular (Potential).
FT   TRANSMEM     60     80       Helical; (Potential).
FT   TOPO_DOM     81     86       Cytoplasmic (Potential).
FT   TRANSMEM     87    107       Helical; (Potential).
FT   TOPO_DOM    108    111       Extracellular (Potential).
FT   TRANSMEM    112    132       Helical; (Potential).
FT   TOPO_DOM    133    143       Cytoplasmic (Potential).
FT   TRANSMEM    144    164       Helical; (Potential).
FT   TOPO_DOM    165    166       Extracellular (Potential).
FT   TRANSMEM    167    187       Helical; (Potential).
FT   TOPO_DOM    188    255       Cytoplasmic (Potential).
FT   TRANSMEM    256    276       Helical; (Potential).
FT   TOPO_DOM    277    291       Extracellular (Potential).
FT   TRANSMEM    292    312       Helical; (Potential).
FT   TOPO_DOM    313    321       Cytoplasmic (Potential).
FT   TRANSMEM    322    342       Helical; (Potential).
FT   TOPO_DOM    343    346       Extracellular (Potential).
FT   TRANSMEM    347    367       Helical; (Potential).
FT   TOPO_DOM    368    382       Cytoplasmic (Potential).
FT   TRANSMEM    383    403       Helical; (Potential).
FT   TOPO_DOM    404    415       Extracellular (Potential).
FT   TRANSMEM    416    436       Helical; (Potential).
FT   TOPO_DOM    437    493       Cytoplasmic (Potential).
FT   MOD_RES     210    210       Phosphoserine.
FT   MOD_RES     213    213       Phosphoserine.
FT   MOD_RES     230    230       Phosphoserine.
FT   MOD_RES     461    461       Phosphoserine.
FT   MOD_RES     462    462       Phosphothreonine.
FT   MOD_RES     477    477       Phosphoserine.
FT   MOD_RES     491    491       Phosphoserine.
SQ   SEQUENCE   493 AA;  53267 MW;  8B6DAB7741340DD7 CRC64;
     MPPAIGGPVG YTPPDGGWGW AVLVGAFISI GFSYAFPKSI TVFFKEIEVI FSATTSEVSW
     ISSIMLAVMY AGGPISSILV NKYGSRPVMI AGGCLSGCGL IAASFCNTVQ ELYLCIGVIG
     GLGLAFNLNP ALTMIGKYFY KKRPLANGLA MAGSPVFLST LAPLNQAFFD IFDWRGSFLI
     LGGLLLNCCV AGSLMRPIGP EQVKLEKLKS KESLQEAGKS DANTDLIGGS PKGEKLSVFQ
     TINKFLDLSL FTHRGFLLYL SGNVVMFFGL FTPLVFLSSY GKSKDFSSEK SAFLLSILAF
     VDMVARPSMG LAANTKWIRP RIQYFFAASV VANGVCHLLA PLSTTYVGFC VYAGVFGFAF
     GWLSSVLFET LMDLIGPQRF SSAVGLVTIV ECCPVLLGPP LLGRLNDMYG DYKYTYWACG
     VILIIAGIYL FIGMGINYRL LAKEQKAEEK QKREGKEDEA STDVDEKPKE TMKAAQSPQQ
     HSSGDPTEEE SPV
//
ID   APC1_MOUSE              Reviewed;        1944 AA.
AC   P53995; Q8BP33; Q8C772;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Anaphase-promoting complex subunit 1;
DE            Short=APC1;
DE   AltName: Full=Cyclosome subunit 1;
DE   AltName: Full=Mitotic checkpoint regulator;
DE   AltName: Full=Testis-specific gene 24 protein;
GN   Name=Anapc1; Synonyms=Mcpr, Tsg24;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CBA; TISSUE=Testis;
RX   MEDLINE=95014147; PubMed=7929068;
RA   Starborg M., Brundell E., Gell K., Hoeoeg C.;
RT   "A novel murine gene encoding a 216-kDa protein is related to a
RT   mitotic checkpoint regulator previously identified in Aspergillus
RT   nidulans.";
RL   J. Biol. Chem. 269:24133-24137(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1063.
RC   STRAIN=C57BL/6J; TISSUE=Embryonic lung, and Forelimb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC       (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls
CC       progression through mitosis and the G1 phase of the cell cycle.
CC       The APC/C complex acts by mediating ubiquitination and subsequent
CC       degradation of target proteins: it mainly mediates the formation
CC       of 'Lys-11'-linked polyubiquitin chains and, to a lower extent,
CC       the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin
CC       chains (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: The APC/C is composed of at least 12 subunits (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in proliferating
CC       fibroblasts, juvenile testis, adult brain and epididymis.
CC   -!- DEVELOPMENTAL STAGE: Uniformly expressed throughout interphase of
CC       the cell cycle.
CC   -!- PTM: Phosphorylated. Phosphorylation on Ser-355 occurs
CC       specifically during mitosis (By similarity).
CC   -!- SIMILARITY: Belongs to the APC1 family.
CC   -!- SIMILARITY: Contains 4 PC repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; X80169; CAA56450.1; -; mRNA.
DR   EMBL; AK052404; BAC34976.1; -; mRNA.
DR   EMBL; AK077847; BAC37032.2; -; mRNA.
DR   IPI; IPI00137228; -.
DR   PIR; A55117; A55117.
DR   RefSeq; NP_032595.2; NM_008569.2.
DR   UniGene; Mm.277408; -.
DR   UniGene; Mm.449185; -.
DR   UniGene; Mm.478751; -.
DR   STRING; P53995; -.
DR   PhosphoSite; P53995; -.
DR   PRIDE; P53995; -.
DR   Ensembl; ENSMUST00000014499; ENSMUSP00000014499; ENSMUSG00000014355.
DR   GeneID; 17222; -.
DR   KEGG; mmu:17222; -.
DR   UCSC; uc008mgq.1; mouse.
DR   CTD; 17222; -.
DR   MGI; MGI:103097; Anapc1.
DR   HOGENOM; HBG356022; -.
DR   HOVERGEN; HBG045326; -.
DR   InParanoid; P53995; -.
DR   OrthoDB; EOG4Z62MQ; -.
DR   PhylomeDB; P53995; -.
DR   NextBio; 291630; -.
DR   ArrayExpress; P53995; -.
DR   Bgee; P53995; -.
DR   CleanEx; MM_ANAPC1; -.
DR   Genevestigator; P53995; -.
DR   GermOnline; ENSMUSG00000014355; Mus musculus.
DR   GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Mitosis; Phosphoprotein; Repeat;
KW   Ubl conjugation pathway.
FT   CHAIN         1   1944       Anaphase-promoting complex subunit 1.
FT                                /FTId=PRO_0000215872.
FT   REPEAT     1297   1325       PC 1.
FT   REPEAT     1366   1404       PC 2.
FT   REPEAT     1467   1501       PC 3.
FT   REPEAT     1520   1552       PC 4.
FT   MOD_RES      51     51       Phosphoserine (By similarity).
FT   MOD_RES      60     60       Phosphoserine (By similarity).
FT   MOD_RES      65     65       Phosphothreonine (By similarity).
FT   MOD_RES     291    291       Phosphothreonine (By similarity).
FT   MOD_RES     341    341       Phosphoserine (By similarity).
FT   MOD_RES     355    355       Phosphoserine (By similarity).
FT   MOD_RES     362    362       Phosphoserine (By similarity).
FT   MOD_RES     373    373       Phosphoserine (By similarity).
FT   MOD_RES     377    377       Phosphoserine (By similarity).
FT   MOD_RES     537    537       Phosphothreonine (By similarity).
FT   MOD_RES     547    547       Phosphoserine (By similarity).
FT   MOD_RES     555    555       Phosphoserine (By similarity).
FT   MOD_RES     563    563       Phosphoserine (By similarity).
FT   MOD_RES     569    569       Phosphoserine (By similarity).
FT   MOD_RES     571    571       Phosphotyrosine (By similarity).
FT   MOD_RES     686    686       Phosphoserine (By similarity).
FT   MOD_RES     688    688       Phosphoserine.
FT   MOD_RES     699    699       Phosphoserine (By similarity).
FT   MOD_RES     731    731       Phosphothreonine (By similarity).
FT   CONFLICT    112    112       Q -> A (in Ref. 2; BAC34976/BAC37032).
FT   CONFLICT    348    349       GV -> AA (in Ref. 2; BAC34976/BAC37032).
FT   CONFLICT    643    643       N -> K (in Ref. 2; BAC34976).
FT   CONFLICT   1036   1036       H -> D (in Ref. 2; BAC34976).
SQ   SEQUENCE   1944 AA;  216087 MW;  48F1EEF01053E6C3 CRC64;
     MSNFSEERAT MIAAGDLQEF VPFGRDHCKH HPNALNLQLR QLQPASELWS SDGAAGLVGS
     LQEVTIHEKQ KESWQLRKGV SEIGDAADYD EELYVAGNMV IWSKGSKSQA LQVYKAFTVD
     STVQQALWCD FIISQDKSEK IYKSHELEKC ICILQSSCMN MHSIDGKDYI ASLPFQVANV
     WATKYGLLFE RCSSSHEVPP SLPREPLPTM FSMLHPLDEI TPLVCKSGSL FGSSRVQYVV
     DPAVKIVFLN IDPSIVMTYD AVQNVHSVWT LRRVKPEEEN AVLKFPEQAG TLQNATTSSS
     LTAHLRSLSK GESPVASPFQ NYSSIHSQSR STSSPSLHSR SPSISNMGVL SRAHSPALGV
     HSFSGAQRFN LSSHSQSPKR HSISHSPSGS FNDSFLAPET EPIVPELCID HLWTETLPNI
     REKNSQASKV FITTDLCGQK FLCFLVEAQL QLRCVKFQES NDKTQLIFGS VTNIHAKDAA
     PVEKIHTMLV LEGNGNLVLY TGVVRVGKVF IPGLPAPSLT MSNMMPRPST PLDGVGTPKP
     LSKLLGSMDE VVLLSPVPEL RDSSKLNDSL YNEDCTFQQL GTYIHSVRDP VHNRVTLELS
     NGSMVRITIP EVATSELVQT CLQAIKFILP KEVAIQVLVK WYNVHSAPGG PSCHSEWSLF
     VICLLNMMGY NTDRLAWTRS FDFEGSLSPV IAPKKARPSD TGSDEDWEYL LNSEYHRNVE
     SHLLNKSLCL TALEVSNAKD EDFSQNLSLD SSTLLFAHIP AIFFVLHLVY EELKLNTLMG
     EGICSLIDLL VQLARDLKLD SYLDHYYRDS PTLVKTTGQV CTIDQGQMGF MHHPPFFTSE
     PPSIYQWVSS CLKGEGMPPY PYLPGICERS RLVVLSIALY TLGDESCVSD ETCQYLSKVT
     STPQKPQAEQ EENRFTFRHS ASVSVLAERL VVWMASVGFT LRDLETLPFG IALPIRDAIY
     HCREQPDSDW SEAVCLLIGR QDLSKQACEG NLPRGKSVLS SEVSSGTEAE EEDDGMNDLN
     HEVMSLIWSE DLRVQHVRRL LQSAQPVRVN VVQYPELSDH EFIEEKENRL LQLCQRTMAL
     PVGRGMFTLF SYHPVPTEPL PVPKLNLTGR APPRNTTVDL NSGNIDVPPN MASWASFHNG
     VAAGLKIAPA SQIDSAWIVY NKPKHAELAN EYAGFLMALG LNGHLTKLAT LNIHDYLTKG
     HEMTSIGLLL GVSAAKLGTM DMSITRLLSI HVPALLPPTS TELDVPHNVQ VAAVVGIGLV
     YQGTAHRHTA EVLLAEIGRP PGPEMEYCTD RESYSLAAGL ALGMVCLGHG SNLIGMSDLN
     VPEQLYQYMV GGHRRFQTGM HREKHKSPSY QIKEGDTINV DVTCPGATLA LAMIYLKTNN
     RSIADWLRAP DTMYLLDFVK PEFLLLRTLA RCLILWDDIL PNSKWVDSNV PQIIRENSIS
     LSEIELPCSE DLNLETLSQA HVYIIAGACL SLGFRFAGSE NLSAFSCLHK FAKDFMNYLS
     APNASVTGPY NLETCLSVVL LSLAMVMAGS GNLKVLQLCR FLHMKTGGEM NYGFHLAHHM
     ALGLLFLGGG RYSLSTSNSS IAALLCALYP HFPAHSTDNR YHLQALRHLY VLAAEPRLLV
     PVDVDTNTPC YALIEVTYKG TQWYEQTKEE LMAPTLLPEL HLLKQMKVKG PRYWELLIDL
     SKGEQHLRSI LSKDGVLYVK LRAGQLSYKE DPMGWQSLLA QTVANRNSEA RAFKPETISS
     FTSDPALLSF AEYFCKPTVS MGPKQEILDL FSSILYECVA QETPEMLPAY IAMDQALRSL
     KKRDMSDTSD LWQIKLILEF FSSRSHQDRQ HTYPKRGLFI NSEFLPVVKC TVDATLDQWL
     QAGGDVCVHA YLSGQPVEKS QLNMLACFLV YHSVPAPRHL PPMGLEGSTS FAELLYRFRH
     LKMPVRALLR LAPVLLGNPQ PMVM
//
ID   DNJC2_MOUSE             Reviewed;         621 AA.
AC   P54103; Q61866;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 2.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=DnaJ homolog subfamily C member 2;
DE   AltName: Full=Mouse Id associate 1;
DE            Short=MIDA1;
DE   AltName: Full=Zuotin-related factor 1;
GN   Name=Dnajc2; Synonyms=Mida1, Zrf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH ID1.
RX   MEDLINE=96027574; PubMed=7559602; DOI=10.1074/jbc.270.42.24818;
RA   Shoji W., Inoue T., Yamamoto T., Obinata M.;
RT   "MIDA1, a protein associated with Id, regulates cell growth.";
RL   J. Biol. Chem. 270:24818-24825(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-514, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   MEDLINE=96115610; PubMed=8666407; DOI=10.1006/geno.1995.9969;
RA   Hughes R., Chan F.Y., White R.A., Zon L.I.;
RT   "Cloning and chromosomal localization of a mouse cDNA with homology to
RT   the Saccharomyces cerevisiae gene zuotin.";
RL   Genomics 29:546-550(1995).
RN   [5]
RP   INTERACTION WITH ID1.
RX   PubMed=10581180; DOI=10.1006/bbrc.1999.1779;
RA   Inoue T., Shoji W., Obinata M.;
RT   "MIDA1, an Id-associating protein, has two distinct DNA binding
RT   activities that are converted by the association with Id1: a novel
RT   function of Id protein.";
RL   Biochem. Biophys. Res. Commun. 266:147-151(1999).
RN   [6]
RP   DNA-BINDING.
RX   PubMed=10971652;
RA   Inoue T., Shoji W., Obinata M.;
RT   "MIDA1 is a sequence specific DNA binding protein with novel DNA
RT   binding properties.";
RL   Genes Cells 5:699-709(2000).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; THR-48; SER-49;
RP   SER-60 AND SER-63, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Acts both as a chaperone in the cytosol and as a
CC       chromatin regulator in the nucleus. When cytosolic, acts as a
CC       molecular chaperone: component of the ribosome-associated complex
CC       (RAC), a complex involved in folding or maintaining nascent
CC       polypeptides in a folding-competent state. In the RAC complex,
CC       stimulates the ATPase activity of the ribosome-associated pool of
CC       Hsp70-type chaperones HSPA14 that bind to the nascent polypeptide
CC       chain. When nuclear, mediates the switching from polycomb-
CC       repressed genes to an active state: specifically recruited at
CC       histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes
CC       the displacement of the polycomb PRC1 complex from chromatin,
CC       thereby facilitating transcription activation (By similarity).
CC       Specifically binds DNA sequence 5'-GTCAAGC-3'.
CC   -!- SUBUNIT: Component of ribosome-associated complex (RAC), a
CC       heterodimer composed of Hsp70/DnaK-type chaperone HSPA14 and
CC       Hsp40/DnaJ-type chaperone DNAJC2 (By similarity). Interacts (via
CC       ZRF1-UBD region) with ID1.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues.
CC   -!- DOMAIN: The ZRF1-UBD region specifically recognizes and binds
CC       H2AK119ub. The ZRF1-UBD region is also involved in protein-protein
CC       interactions with other proteins, suggesting that it may be masked
CC       by some regulator, thereby preventing its association with
CC       H2AK119ub (By similarity).
CC   -!- PTM: Phosphorylated in M (mitotic) phase (By similarity).
CC   -!- SIMILARITY: Contains 1 J domain.
CC   -!- SIMILARITY: Contains 2 SANT domains.
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DR   EMBL; D63784; BAA09854.1; -; mRNA.
DR   EMBL; AK131964; BAE20907.1; -; mRNA.
DR   EMBL; BC052027; AAH52027.1; -; mRNA.
DR   EMBL; U53208; AAC52486.1; -; mRNA.
DR   IPI; IPI00126317; -.
DR   PIR; A57591; A57591.
DR   RefSeq; NP_033610.1; NM_009584.4.
DR   UniGene; Mm.266312; -.
DR   ProteinModelPortal; P54103; -.
DR   SMR; P54103; 85-162, 450-512, 543-601.
DR   STRING; P54103; -.
DR   PhosphoSite; P54103; -.
DR   PRIDE; P54103; -.
DR   Ensembl; ENSMUST00000030771; ENSMUSP00000030771; ENSMUSG00000029014.
DR   GeneID; 22791; -.
DR   KEGG; mmu:22791; -.
DR   CTD; 22791; -.
DR   MGI; MGI:99470; Dnajc2.
DR   eggNOG; roNOG07168; -.
DR   HOGENOM; HBG383362; -.
DR   HOVERGEN; HBG008782; -.
DR   InParanoid; P54103; -.
DR   OMA; CKTWNHF; -.
DR   OrthoDB; EOG4D26PN; -.
DR   PhylomeDB; P54103; -.
DR   NextBio; 303379; -.
DR   ArrayExpress; P54103; -.
DR   Bgee; P54103; -.
DR   CleanEx; MM_DNAJC2; -.
DR   Genevestigator; P54103; -.
DR   GermOnline; ENSMUSG00000029014; Mus musculus.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR   GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR   GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR   GO; GO:0006260; P:DNA replication; IMP:MGI.
DR   GO; GO:0000085; P:G2 phase of mitotic cell cycle; IMP:MGI.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; ISS:UniProtKB.
DR   InterPro; IPR001623; DnaJ_N.
DR   InterPro; IPR018253; Heat_shock_DnaJ_CS.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR017930; HTH_Myb-type_DNA-bd.
DR   InterPro; IPR014778; Myb_DNA-bd.
DR   InterPro; IPR001005; SANT_DNA-bd.
DR   InterPro; IPR017884; SANT_eukarya.
DR   Gene3D; G3DSA:1.10.287.110; DnaJ_N; 1.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF00249; Myb_DNA-binding; 2.
DR   SMART; SM00271; DnaJ; 1.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF46565; DnaJ_N; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 2.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51293; SANT; 1.
PE   1: Evidence at protein level;
KW   Activator; Chaperone; Chromatin regulator; Cytoplasm; Nucleus;
KW   Phosphoprotein; Repeat; Transcription; Transcription regulation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    621       DnaJ homolog subfamily C member 2.
FT                                /FTId=PRO_0000071124.
FT   DOMAIN       88    161       J.
FT   DOMAIN      449    511       SANT 1.
FT   DOMAIN      549    604       SANT 2.
FT   REGION      160    250       ZRF1-UBD.
FT   MOD_RES      47     47       Phosphoserine.
FT   MOD_RES      48     48       Phosphothreonine.
FT   MOD_RES      49     49       Phosphoserine.
FT   MOD_RES      60     60       Phosphoserine.
FT   MOD_RES      63     63       Phosphoserine.
FT   CONFLICT    473    473       T -> R (in Ref. 4; AAC52486).
FT   CONFLICT    478    478       E -> D (in Ref. 4; AAC52486).
FT   CONFLICT    502    514       KAKSLQKLDPHQK -> EVRGPKSWGSSKR (in Ref.
FT                                4; AAC52486).
SQ   SEQUENCE   621 AA;  71722 MW;  0FFC511028EA1C41 CRC64;
     MLLLPSAAEG QGTAITHALT SASSVCQVEP VGRWFEAFVK RRNRNASTSF QELEDKKELS
     EESEDEELQL EEFPMLKTLD PKDWKNQDHY AVLGLGHVRY TATQRQIKAA HKAMVLKHHP
     DKRKAAGEPI KEGDNDYFTC ITKAYEMLSD PVKRRAFNSV DPTFDNSVPS KSEAKDNFFQ
     VFSPVFERNS RWSNKKNVPK LGDMNSSFED VDAFYSFWYN FDSWREFSYL DEEEKEKAEC
     RDERKWIEKQ NRATRAQRKK EEMNRIRTLV DNAYSCDPRI KKFKEEEKAK KEAEKKAKAE
     ARRKEQEAKE KQRQAELEAV RLAKEKEEEE VRQQALLAKK EKDIQKKAIK KERQKLRNSC
     KSWNHFSDNE ADRVKMMEEV EKLCDRLELA SLQGLNEILA SSTREVGKAA LEKQIEEVNE
     QMRREKEEAD ARMRQASKNA EKSTGGSGSG SKNWSEDDLQ LLIKAVNLFP AGTNSRWEVI
     ANYMNIHSSS GVKRTAKDVI SKAKSLQKLD PHQKDDINKK AFDKFKKEHG VASQADSAAP
     SERFEGPCID STPWTTEEQK LLEQALKTYP VNTPERWEKI AEAVPGRTKK DCMRRYKELV
     EMVKAKKAAQ EQVLNASRAR K
//
ID   STOM_MOUSE              Reviewed;         284 AA.
AC   P54116; O88988; Q3UP81; Q60744; Q62455;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Erythrocyte band 7 integral membrane protein;
DE   AltName: Full=Protein 7.2b;
DE   AltName: Full=Stomatin;
GN   Name=Stom; Synonyms=Epb7.2, Epb72;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J;
RX   PubMed=7540886;
RA   Gallagher P.G., Romana M., Lieman J.H., Ward D.C.;
RT   "cDNA structure, tissue-specific expression, and chromosomal
RT   localization of the murine band 7.2b gene.";
RL   Blood 86:359-365(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Bone marrow;
RX   MEDLINE=97080556; PubMed=8921901; DOI=10.1016/0378-1119(96)00347-2;
RA   Schlegel W., Unfried I., Prohaska R.;
RT   "Cloning and analysis of a cDNA encoding the BALB/c murine erythrocyte
RT   band 7 integral membrane protein.";
RL   Gene 178:115-118(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=96374834; PubMed=8786142; DOI=10.1006/geno.1996.0304;
RA   Gallagher P.G., Turetsky T., Mentzer W.C.;
RT   "Genomic organization and 5'-flanking DNA sequence of the murine
RT   stomatin gene (Epb72).";
RL   Genomics 34:410-412(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND DEVELOPMENTAL STAGE.
RC   TISSUE=Neuron;
RX   MEDLINE=99316085; PubMed=10383825; DOI=10.1006/mcne.1999.0761;
RA   Mannsfeldt A.G., Carroll P., Stucky C.L., Lewin G.R.;
RT   "Stomatin, a MEC-2 like protein, is expressed by mammalian sensory
RT   neurons.";
RL   Mol. Cell. Neurosci. 13:391-404(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow, Cerebellum, Spleen, and Sympathetic ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH ACCN1; ACCN2 AND ACCN3.
RX   PubMed=15471860; DOI=10.1074/jbc.M407708200;
RA   Price M.P., Thompson R.J., Eshcol J.O., Wemmie J.A., Benson C.J.;
RT   "Stomatin modulates gating of acid-sensing ion channels.";
RL   J. Biol. Chem. 279:53886-53891(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161 AND SER-244, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Thought to regulate cation conductance. May regulate
CC       ACCN1 and ACCN3 gating.
CC   -!- SUBUNIT: Homooligomer containing between 9 and 12 monomers.
CC       Interacts with LANCL1 (By similarity). Interacts with ACCN1, ACCN2
CC       and ACCN3.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Cell membrane; Lipid-anchor; Cytoplasmic side.
CC       Melanosome (By similarity). Note=Exposed on the cytoplasmic
CC       surface of the membrane. Associated with lipid rafts. Concentrates
CC       preferentially in plasma membrane protrusions and in a juxta-
CC       nuclear region which may represent Golgi-derived vesicles.
CC       Colocalizes with actin.
CC   -!- TISSUE SPECIFICITY: Expressed in all sensory neurons of the dorsal
CC       root ganglia. In the CNS, expressed in many neurons of the spinal
CC       cord, medulla and pons. Expressed only in scattered neurons in the
CC       cortex, hippocampus, thalamus and basal ganglia. In the
CC       cerebellum, expressed in all Purkinje cells (at protein level).
CC       Widely expressed with high levels in heart, liver, skeletal muscle
CC       and testis and low levels in lung, brain and spleen.
CC   -!- DEVELOPMENTAL STAGE: First expressed in the developing embryo at
CC       E11.5 when target innervation is complete. Expression continues
CC       into adulthood.
CC   -!- SIMILARITY: Belongs to the band 7/mec-2 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB18857.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
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DR   EMBL; U17297; AAA75024.1; -; mRNA.
DR   EMBL; X91043; CAA62503.1; -; mRNA.
DR   EMBL; U50999; AAB18857.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U50993; AAB18857.1; JOINED; Genomic_DNA.
DR   EMBL; U50994; AAB18857.1; JOINED; Genomic_DNA.
DR   EMBL; U50995; AAB18857.1; JOINED; Genomic_DNA.
DR   EMBL; U50996; AAB18857.1; JOINED; Genomic_DNA.
DR   EMBL; U50997; AAB18857.1; JOINED; Genomic_DNA.
DR   EMBL; U50998; AAB18857.1; JOINED; Genomic_DNA.
DR   EMBL; AF093620; AAC64173.1; -; mRNA.
DR   EMBL; AK139242; BAE23930.1; -; mRNA.
DR   EMBL; AK143724; BAE25516.1; -; mRNA.
DR   EMBL; AK148975; BAE28708.1; -; mRNA.
DR   EMBL; AK149689; BAE29028.1; -; mRNA.
DR   EMBL; AK149821; BAE29103.1; -; mRNA.
DR   EMBL; AK149991; BAE29219.1; -; mRNA.
DR   EMBL; AK151129; BAE30137.1; -; mRNA.
DR   IPI; IPI00323748; -.
DR   PIR; JC5221; JC5221.
DR   RefSeq; NP_038543.1; NM_013515.2.
DR   UniGene; Mm.295284; -.
DR   ProteinModelPortal; P54116; -.
DR   SMR; P54116; 87-255.
DR   STRING; P54116; -.
DR   PhosphoSite; P54116; -.
DR   PRIDE; P54116; -.
DR   Ensembl; ENSMUST00000028241; ENSMUSP00000028241; ENSMUSG00000026880.
DR   GeneID; 13830; -.
DR   KEGG; mmu:13830; -.
DR   NMPDR; fig|10090.3.peg.5864; -.
DR   UCSC; uc008jkh.1; mouse.
DR   CTD; 13830; -.
DR   MGI; MGI:95403; Stom.
DR   GeneTree; ENSGT00550000074454; -.
DR   HOGENOM; HBG714701; -.
DR   HOVERGEN; HBG004815; -.
DR   InParanoid; P54116; -.
DR   OMA; NYIMATS; -.
DR   OrthoDB; EOG44QT1S; -.
DR   PhylomeDB; P54116; -.
DR   NextBio; 284640; -.
DR   ArrayExpress; P54116; -.
DR   Bgee; P54116; -.
DR   CleanEx; MM_STOM; -.
DR   Genevestigator; P54116; -.
DR   GermOnline; ENSMUSG00000026880; Mus musculus.
DR   GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005887; C:integral to plasma membrane; ISS:UniProtKB.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR   InterPro; IPR001107; Band_7.
DR   InterPro; IPR018080; Band_7/stomatin-like_CS.
DR   InterPro; IPR001972; Stomatin.
DR   PANTHER; PTHR10264; Stomatin; 1.
DR   Pfam; PF01145; Band_7; 1.
DR   PRINTS; PR00721; STOMATIN.
DR   SMART; SM00244; PHB; 1.
DR   PROSITE; PS01270; BAND_7; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Lipoprotein; Membrane; Palmitate; Phosphoprotein.
FT   CHAIN         1    284       Erythrocyte band 7 integral membrane
FT                                protein.
FT                                /FTId=PRO_0000094028.
FT   TOPO_DOM      1     31       Cytoplasmic (Potential).
FT   INTRAMEM     32     52       Potential.
FT   TOPO_DOM     53    284       Cytoplasmic (Potential).
FT   REGION      265    273       Required for homooligomerization (By
FT                                similarity).
FT   REGION      267    269       Required for lipid raft association (By
FT                                similarity).
FT   REGION      273    284       Interaction with LANCL1 (By similarity).
FT   MOD_RES     161    161       Phosphoserine.
FT   MOD_RES     244    244       Phosphoserine.
FT   LIPID        30     30       S-palmitoyl cysteine (By similarity).
FT   LIPID        87     87       S-palmitoyl cysteine (By similarity).
FT   CONFLICT      3      3       D -> V (in Ref. 4; AAC64173).
FT   CONFLICT     37     37       A -> V (in Ref. 2; CAA62503).
FT   CONFLICT     40     40       F -> I (in Ref. 2; CAA62503).
FT   CONFLICT     43     43       I -> L (in Ref. 2; CAA62503).
FT   CONFLICT     91     91       L -> F (in Ref. 2; CAA62503).
FT   CONFLICT    273    273       V -> I (in Ref. 2; CAA62503).
FT   CONFLICT    283    283       N -> H (in Ref. 2; CAA62503).
SQ   SEQUENCE   284 AA;  31375 MW;  AB7CC0E5FF2DF4A9 CRC64;
     MSDKRQSSHV QSQRIPESFR ENSKTELGAC GWILVAASFF FVIITFPISI WICIKIVKEY
     ERVIIFRLGR ILQGGAKGPG LFFILPCTDS LIKVDMRTIS FDIPPQEVLT KDSVTISVDG
     VVYYRVQNAT LAVANITNAD SATRLLAQTT LRNALGTKNL SQILSDREEI AHHMQSTLDD
     ATDDWGIKVE RVEIKDVKLP VQLQRAMAAE AEAAREARAK VIAAEGEMNA SRALKEASMV
     ITESPAALQL RYLQTLTTIA AEKNSTIVFP LPVDMLQGIM GSNH
//
ID   STMN1_MOUSE             Reviewed;         149 AA.
AC   P54227;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Stathmin;
DE   AltName: Full=Leukemia-associated gene protein;
DE   AltName: Full=Leukemia-associated phosphoprotein p18;
DE   AltName: Full=Metablastin;
DE   AltName: Full=Oncoprotein 18;
DE            Short=Op18;
DE   AltName: Full=Phosphoprotein p19;
DE            Short=pp19;
DE   AltName: Full=Prosolin;
DE   AltName: Full=Protein Pr22;
DE   AltName: Full=pp17;
GN   Name=Stmn1; Synonyms=Lag, Lap18, Pr22;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=94117005; PubMed=8288240; DOI=10.1006/geno.1993.1477;
RA   Okazaki T., Yoshida B.N., Avraham K.B., Wang H., Wuenschell C.W.,
RA   Jenkins N.A., Copeland N.G., Anderson D.J., Mori N.;
RT   "Molecular diversity of the SCG10/stathmin gene family in the mouse.";
RL   Genomics 18:360-373(1993).
RN   [2]
RP   ERRATUM.
RA   Okazaki T., Yoshida B.N., Avraham K.B., Wang H., Wuenschell C.W.,
RA   Jenkins N.A., Copeland N.G., Anderson D.J., Mori N.;
RL   Genomics 21:298-298(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=97062620; PubMed=8906359;
RA   Hosoya H., Ishikawa K., Dohi N., Marunouchi T.;
RT   "Transcriptional and post-transcriptional regulation of pr22 (Op18)
RT   with proliferation control.";
RL   Cell Struct. Funct. 21:237-243(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129; TISSUE=Mammary gland, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 15-27, AND MASS SPECTROMETRY.
RC   TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [6]
RP   PHOSPHORYLATION AT SER-16; SER-25; SER-38 AND SER-63.
RX   MEDLINE=93388570; PubMed=8376365;
RA   Beretta L., Dobransky T., Sobel A.;
RT   "Multiple phosphorylation of stathmin. Identification of four sites
RT   phosphorylated in intact cells and in vitro by cyclic AMP-dependent
RT   protein kinase and p34cdc2.";
RL   J. Biol. Chem. 268:20076-20084(1993).
RN   [7]
RP   INTERACTION WITH KIST.
RC   TISSUE=Embryo;
RX   MEDLINE=95241452; PubMed=7724523; DOI=10.1073/pnas.92.8.3100;
RA   Maucuer A., Camonis J.H., Sobel A.;
RT   "Stathmin interaction with a putative kinase and coiled-coil-forming
RT   protein domains.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3100-3104(1995).
RN   [8]
RP   FUNCTION IN CONTROL OF FEAR, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=16286011; DOI=10.1016/j.cell.2005.08.038;
RA   Shumyatsky G.P., Malleret G., Shin R.-M., Takizawa S., Tully K.,
RA   Tsvetkov E., Zakharenko S.S., Joseph J., Vronskaya S., Yin D.,
RA   Schubart U.K., Kandel E.R., Bolshakov V.Y.;
RT   "Stathmin, a gene enriched in the amygdala, controls both learned and
RT   innate fear.";
RL   Cell 123:697-709(2005).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-38 AND SER-46,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Involved in the regulation of the microtubule (MT)
CC       filament system by destabilizing microtubules. Prevents assembly
CC       and promotes disassembly of microtubules. Phosphorylation at Ser-
CC       16 may be required for axon formation during neurogenesis (By
CC       similarity). Involved in the control of the learned and innate
CC       fear.
CC   -!- SUBUNIT: Binds to two alpha/beta-tubulin heterodimers. Interacts
CC       with KIST.
CC   -!- INTERACTION:
CC       P46414:Cdkn1b; NbExp=2; IntAct=EBI-1006438, EBI-1005742;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the lateral nucleus of the
CC       amygdala.
CC   -!- PTM: Many different phosphorylated forms are observed depending on
CC       specific combinations among the sites which can be phosphorylated.
CC       MAPK is responsible for the phosphorylation of stathmin in
CC       response to NGF (Probable). Phosphorylation at Ser-16 seems to be
CC       required for neuron polarization (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice show deficits in spike-timing-dependent
CC       long-term potentiation, exhibit decreased memory in amygdala-
CC       dependent fear conditioning and fail to recognize danger in
CC       innately aversive environements.
CC   -!- SIMILARITY: Belongs to the stathmin family.
CC   -----------------------------------------------------------------------
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DR   EMBL; L20256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L20257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L20258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X94915; CAA64401.1; -; mRNA.
DR   EMBL; BC010581; AAH10581.1; -; mRNA.
DR   EMBL; BC031831; AAH31831.1; -; mRNA.
DR   EMBL; BC054396; AAH54396.1; -; mRNA.
DR   IPI; IPI00551236; -.
DR   PIR; B48917; B48917.
DR   RefSeq; NP_062615.1; NM_019641.4.
DR   UniGene; Mm.378957; -.
DR   ProteinModelPortal; P54227; -.
DR   SMR; P54227; 6-141.
DR   IntAct; P54227; 3.
DR   STRING; P54227; -.
DR   PhosphoSite; P54227; -.
DR   REPRODUCTION-2DPAGE; P54227; -.
DR   UCD-2DPAGE; P54227; -.
DR   PRIDE; P54227; -.
DR   Ensembl; ENSMUST00000030636; ENSMUSP00000030636; ENSMUSG00000028832.
DR   Ensembl; ENSMUST00000105868; ENSMUSP00000101494; ENSMUSG00000028832.
DR   GeneID; 16765; -.
DR   KEGG; mmu:16765; -.
DR   UCSC; uc008vfc.1; mouse.
DR   CTD; 16765; -.
DR   MGI; MGI:96739; Stmn1.
DR   eggNOG; roNOG12776; -.
DR   HOGENOM; HBG444413; -.
DR   HOVERGEN; HBG054037; -.
DR   InParanoid; P54227; -.
DR   OMA; KEAVPEF; -.
DR   OrthoDB; EOG46MBKT; -.
DR   PhylomeDB; P54227; -.
DR   NextBio; 290586; -.
DR   ArrayExpress; P54227; -.
DR   Bgee; P54227; -.
DR   CleanEx; MM_STMN1; -.
DR   Genevestigator; P54227; -.
DR   GermOnline; ENSMUSG00000028832; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR   GO; GO:0031115; P:negative regulation of microtubule polymerization; IDA:MGI.
DR   GO; GO:0051272; P:positive regulation of cellular component movement; IGI:MGI.
DR   InterPro; IPR000956; Stathmin.
DR   PANTHER; PTHR10104; Stathmin; 1.
DR   Pfam; PF00836; Stathmin; 1.
DR   PIRSF; PIRSF002285; Stathmin; 1.
DR   PRINTS; PR00345; STATHMIN.
DR   SUPFAM; SSF101494; Stathmin; 1.
DR   PROSITE; PS00563; STATHMIN_1; 1.
DR   PROSITE; PS01041; STATHMIN_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Developmental protein; Differentiation; Direct protein sequencing;
KW   Microtubule; Neurogenesis; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    149       Stathmin.
FT                                /FTId=PRO_0000182390.
FT   COILED       41    140       Potential.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       9      9       N6-acetyllysine (By similarity).
FT   MOD_RES      16     16       Phosphoserine; by PKA.
FT   MOD_RES      25     25       Phosphoserine; by CDK1 and MAPK.
FT   MOD_RES      28     28       Phosphoserine (By similarity).
FT   MOD_RES      38     38       Phosphoserine; by CDK1.
FT   MOD_RES      46     46       Phosphoserine.
FT   MOD_RES      63     63       Phosphoserine; by PKA.
FT   MOD_RES      80     80       N6-acetyllysine (By similarity).
FT   MOD_RES      95     95       N6-acetyllysine (By similarity).
FT   MOD_RES     100    100       N6-acetyllysine (By similarity).
FT   MOD_RES     119    119       N6-acetyllysine (By similarity).
FT   MOD_RES     128    128       N6-acetyllysine (By similarity).
FT   MOD_RES     146    146       Phosphothreonine (By similarity).
SQ   SEQUENCE   149 AA;  17274 MW;  616526E0A6667BDA CRC64;
     MASSDIQVKE LEKRASGQAF ELILSPRSKE SVPDFPLSPP KKKDLSLEEI QKKLEAAEER
     RKSHEAEVLK QLAEKREHEK EVLQKAIEEN NNFSKMAEEK LTHKMEANKE NREAQMAAKL
     ERLREKDKHV EEVRKNKESK DPADETEAD
//
ID   ATX1_MOUSE              Reviewed;         791 AA.
AC   P54254; Q8C866;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Ataxin-1;
DE   AltName: Full=Spinocerebellar ataxia type 1 protein homolog;
GN   Name=Atxn1; Synonyms=Sca1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X CBA; TISSUE=Brain, Retina, and Thymus;
RX   MEDLINE=96381424; PubMed=8789437; DOI=10.1093/hmg/5.1.33;
RA   Banfi S., Servadio A., Chung M.-Y., Capozzoli F., Duvick L.A.,
RA   Elde R., Zoghbi H.Y., Orr H.T.;
RT   "Cloning and developmental expression analysis of the murine homolog
RT   of the spinocerebellar ataxia type 1 gene (Sca1).";
RL   Hum. Mol. Genet. 5:33-40(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NMRI; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-771.
RX   MEDLINE=98449695; PubMed=9778246; DOI=10.1016/S0092-8674(00)81781-X;
RA   Klement I.A., Skinner P.J., Kaytor M.D., Yi H., Hersch S.M.,
RA   Clark H.B., Zoghbi H.Y., Orr H.T.;
RT   "Ataxin-1 nuclear localization and aggregation: role in polyglutamine-
RT   induced disease in SCA1 transgenic mice.";
RL   Cell 95:41-53(1998).
RN   [5]
RP   INTERACTION WITH ANP32A.
RX   MEDLINE=98013170; PubMed=9353121; DOI=10.1038/40159;
RA   Matilla A., Koshy B.T., Cummings C.J., Isobe T., Orr H.T.,
RA   Zoghbi H.Y.;
RT   "The cerebellar leucine-rich acidic nuclear protein interacts with
RT   ataxin-1.";
RL   Nature 389:974-978(1997).
RN   [6]
RP   INTERACTION WITH CIC.
RX   PubMed=17190598; DOI=10.1016/j.cell.2006.11.038;
RA   Lam Y.C., Bowman A.B., Jafar-Nejad P., Lim J., Richman R., Fryer J.D.,
RA   Hyun E.D., Duvick L.A., Orr H.T., Botas J., Zoghbi H.Y.;
RT   "ATAXIN-1 interacts with the repressor Capicua in its native complex
RT   to cause SCA1 neuropathology.";
RL   Cell 127:1335-1347(2006).
RN   [7]
RP   INTERACTION WITH ATXN1L.
RX   PubMed=17322884; DOI=10.1038/ng1977;
RA   Bowman A.B., Lam Y.C., Jafar-Nejad P., Chen H.-K., Richman R.,
RA   Samaco R.C., Fryer J.D., Kahle J.J., Orr H.T., Zoghbi H.Y.;
RT   "Duplication of Atxn1l suppresses SCA1 neuropathology by decreasing
RT   incorporation of polyglutamine-expanded ataxin-1 into native
RT   complexes.";
RL   Nat. Genet. 39:373-379(2007).
CC   -!- FUNCTION: May be involved in RNA metabolism.
CC   -!- SUBUNIT: Homooligomer (By similarity). Interacts with PQBP1, UBIN
CC       and USP7 (By similarity). Interacts with ANP32A. Interacts with
CC       CIC and ATXN1L. Interacts with ZNF804A (By similarity).
CC   -!- INTERACTION:
CC       Q8CHK4:Kat5; NbExp=1; IntAct=EBI-1169713, EBI-1169948;
CC       P51448:Rora; NbExp=1; IntAct=EBI-1169713, EBI-1169722;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus.
CC       Note=Colocalizes with USP7 in the nucleus (By similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed. In brain, the pattern of
CC       distribution is limited to neuron populations.
CC   -!- DEVELOPMENTAL STAGE: Transient expression burst in Purkinje cells
CC       as the cerebellar cortex becomes functional (postnatal day 14),
CC       and in mesenchymal cells of the developing intervertebral disks of
CC       the spinal column.
CC   -!- DOMAIN: The AXH domain is required for interaction with CIC.
CC   -!- PTM: Sumoylation is dependent on nuclear localization and
CC       phosphorylation at Ser-751 (By similarity).
CC   -!- POLYMORPHISM: The murine poly-Gln region is very limited in
CC       comparison to human ATXN1 and is not polymorphic.
CC   -!- SIMILARITY: Belongs to the ATXN1 family.
CC   -!- SIMILARITY: Contains 1 AXH domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; X83542; CAA58533.1; -; mRNA.
DR   EMBL; AK048268; BAC33290.1; -; mRNA.
DR   EMBL; BC058178; AAH58178.1; -; mRNA.
DR   IPI; IPI00323787; -.
DR   RefSeq; NP_033150.2; NM_009124.5.
DR   UniGene; Mm.342683; -.
DR   UniGene; Mm.342686; -.
DR   UniGene; Mm.476983; -.
DR   ProteinModelPortal; P54254; -.
DR   SMR; P54254; 549-669.
DR   DIP; DIP-6004N; -.
DR   IntAct; P54254; 5.
DR   STRING; P54254; -.
DR   PhosphoSite; P54254; -.
DR   PRIDE; P54254; -.
DR   Ensembl; ENSMUST00000091628; ENSMUSP00000089217; ENSMUSG00000046876.
DR   GeneID; 20238; -.
DR   KEGG; mmu:20238; -.
DR   CTD; 20238; -.
DR   MGI; MGI:104783; Atxn1.
DR   eggNOG; roNOG07755; -.
DR   GeneTree; ENSGT00390000005939; -.
DR   HOGENOM; HBG506838; -.
DR   HOVERGEN; HBG004319; -.
DR   InParanoid; P54254; -.
DR   OMA; TQPPVIG; -.
DR   OrthoDB; EOG408N7X; -.
DR   ArrayExpress; P54254; -.
DR   Bgee; P54254; -.
DR   CleanEx; MM_ATXN1; -.
DR   Genevestigator; P54254; -.
DR   GermOnline; ENSMUSG00000046876; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0042405; C:nuclear inclusion body; ISS:UniProtKB.
DR   GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR   GO; GO:0034046; F:poly(G) RNA binding; ISS:UniProtKB.
DR   GO; GO:0008266; F:poly(U) RNA binding; ISS:UniProtKB.
DR   GO; GO:0008022; F:protein C-terminus binding; ISS:UniProtKB.
DR   GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR   GO; GO:0016564; F:transcription repressor activity; ISS:UniProtKB.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR   GO; GO:0043569; P:negative regulation of insulin-like growth factor receptor signaling pathway; IMP:MGI.
DR   GO; GO:0042326; P:negative regulation of phosphorylation; IMP:MGI.
DR   GO; GO:0051168; P:nuclear export; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:MGI.
DR   GO; GO:0060079; P:regulation of excitatory postsynaptic membrane potential; IMP:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   InterPro; IPR013723; Ataxin-1_HBP1.
DR   InterPro; IPR003652; Ataxin_AXH_dom.
DR   InterPro; IPR020997; Capicua_tscrpt_rep_mod.
DR   Pfam; PF12547; ATXN-1_C; 1.
DR   Pfam; PF08517; AXH; 1.
DR   SMART; SM00536; AXH; 1.
DR   SUPFAM; SSF102031; Ataxin-1_HBP1; 1.
DR   PROSITE; PS51148; AXH; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Isopeptide bond; Nucleus; Phosphoprotein; RNA-binding;
KW   Ubl conjugation.
FT   CHAIN         1    791       Ataxin-1.
FT                                /FTId=PRO_0000064752.
FT   DOMAIN      538    669       AXH.
FT   REGION      470    580       Self-association (By similarity).
FT   REGION      514    791       Interaction with USP7 (By similarity).
FT   REGION      516    742       RNA-binding (By similarity).
FT   MOTIF       770    773       Nuclear localization signal.
FT   COMPBIAS    214    217       Poly-Pro.
FT   MOD_RES     213    213       Phosphoserine (By similarity).
FT   MOD_RES     229    229       Phosphoserine (By similarity).
FT   MOD_RES     751    751       Phosphoserine (By similarity).
FT   CROSSLNK     16     16       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    193    193       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    585    585       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    672    672       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    721    721       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   MUTAGEN     771    771       K->T: Abolishes nuclear localization.
FT                                Inhibits development of ataxia.
FT   CONFLICT      8      8       S -> T (in Ref. 1; CAA58533).
FT   CONFLICT     77     77       H -> L (in Ref. 1; CAA58533).
FT   CONFLICT    393    395       HLG -> APR (in Ref. 1; CAA58533).
FT   CONFLICT    477    477       T -> M (in Ref. 1; CAA58533).
FT   CONFLICT    519    519       A -> S (in Ref. 1; CAA58533).
FT   CONFLICT    587    587       D -> H (in Ref. 1; CAA58533).
FT   CONFLICT    687    687       A -> V (in Ref. 1; CAA58533).
FT   CONFLICT    749    749       R -> RR (in Ref. 1; CAA58533).
SQ   SEQUENCE   791 AA;  83793 MW;  1F87A5D65527D550 CRC64;
     MKSNQERSNE CLPPKKREIP ATSRPSEEKA TALPSDNHCV EGVAWLPSTP GIRGHGGGRH
     GSAGTSGEHG LQGMGLHKAL SAGLDYSPPS APRSVPTANT LPTVYPPPQS GTPVSPVQYA
     HLSHTFQFIG SSQYSGPYAG FIPSQLISPS GNPVTSAVAS AAGATTPSQR SQLEAYSTLL
     ANMGSLSQAP GHKVEPPPQQ HLSRAAGLVN PGSPPPPTQQ NQYIHISSSP QSSGRATSPP
     PIPVHLHPHQ TMIPHTLTLG PSSQVVVQYS DAGGHFVPRE STKKAESSRL QQAMQAKEVL
     NGEMEKSRRY GASSSVELSL GKASSKSVPH PYESRHVVVH PSPADYSSRD TSGVRGSVMV
     LPNSSTPSAD LEAQQTTHRE ASPSTLNDKS GLHLGKPGHR SYALSPHTVI QTTHSASEPL
     PVGLPATAFY AGTQPPVIGY LSGQQQAITY AGGLPQHLVI PGNQPLLIPV GSPDMDTPGA
     ASAIVTSSPQ FAAVPHTFVT TALPKSENFN PEALVTQAAY PAMVQAQIHL PVVQSVASPT
     TASPTLPPYF MKGSIIQLAN GELKKVEDLK TEDFIQSAEI SNDLKIDSST VERIEESHSP
     GVAVIQFAVG EHRAQVSVEV LVEYPFFVFG QGWSSCCPER TSQLFDLPCS KLSVGDVCIS
     LTLKNLKNGS VKKGQPVDPA SVLLKQAKTD SLAGSRHRYA EQENGINQGS AQVLSENGEL
     KFPEKIGLPA APFLSKIEPS KPTATRKRRW SAPETRKLEK SEDEPPLTLP KPSLIPQEVK
     ICIEGRSNVG K
//
ID   RD23A_MOUSE             Reviewed;         363 AA.
AC   P54726;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-FEB-2011, entry version 85.
DE   RecName: Full=UV excision repair protein RAD23 homolog A;
DE            Short=HR23A;
DE            Short=mHR23A;
GN   Name=Rad23a; Synonyms=Mhr23a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Testis;
RX   MEDLINE=96403997; PubMed=8808275; DOI=10.1006/geno.1996.0004;
RA   van der Spek P.J., Visser C.E., Hanaoka F., Smit B., Hagemeijer A.,
RA   Bootsma D., Hoeijmakers J.H.J.;
RT   "Cloning, comparative mapping, and RNA expression of the mouse
RT   homologues of the Saccharomyces cerevisiae nucleotide excision repair
RT   gene RAD23.";
RL   Genomics 31:20-27(1996).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12815074; DOI=10.1101/gad.260003;
RA   Ng J.M., Vermeulen W., van der Horst G.T., Bergink S., Sugasawa K.,
RA   Vrieling H., Hoeijmakers J.H.;
RT   "A novel regulation mechanism of DNA repair by damage-induced and
RT   RAD23-dependent stabilization of xeroderma pigmentosum group C
RT   protein.";
RL   Genes Dev. 17:1630-1645(2003).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15336624; DOI=10.1016/j.dnarep.2004.06.010;
RA   Okuda Y., Nishi R., Ng J.M., Vermeulen W., van der Horst G.T.,
RA   Mori T., Hoeijmakers J.H., Hanaoka F., Sugasawa K.;
RT   "Relative levels of the two mammalian Rad23 homologs determine
RT   composition and stability of the xeroderma pigmentosum group C protein
RT   complex.";
RL   DNA Repair 3:1285-1295(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
CC   -!- FUNCTION: Multiubiquitin chain receptor involved in modulation of
CC       proteasomal degradation. Binds to 'Lys-48'-linked polyubiquitin
CC       chains in a length-dependent manner and with a lower affinity to
CC       'Lys-63'-linked polyubiquitin chains. Proposed to be capable to
CC       bind simultaneously to the 26S proteasome and to polyubiquitinated
CC       substrates and to deliver ubiquitinated proteins to the proteasome
CC       (By similarity).
CC   -!- FUNCTION: Involved in nucleotide excision repair and is thought to
CC       be functional equivalent for Rad23b in global genome nucleotide
CC       excision repair (GG-NER) by association with Xpc. In vitro, the
CC       XPC:RAD23A dimer has NER activity. Can stabilize Xpc. Reported
CC       differences to Rad23b in regard to NER activity and Xpc
CC       stabilization are probably due to differences in expression levels
CC       with Rad23a being much less expressed than Rad23b.
CC   -!- SUBUNIT: Interacts with XPC; the interaction is suggesting the
CC       existence of a functional equivalent variant XPC complex.
CC       Interacts with PSMD4 and PSMC5. Interacts with ATXN3. Interacts
CC       with UBQLN2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- DOMAIN: The ubiquitin-like (UBL) and the UBA (ubiquitin-
CC       associated) domains interact intramolecularly in a highly dynamic
CC       manner, as each UBA domain competes for an overlapping UBL domain
CC       surface. Binding of ubiquitin or proteasome subunit Psmd4 disrupt
CC       the UBL-UBA domain interactions and drive Rad23a in to an open
CC       conformation (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- DISRUPTION PHENOTYPE: Embryonic lethal with Rad23a and Rad23b
CC       double deficiency. Double deficient cells show reduced cell
CC       survival upopn UV radiation and reduced steady-state level of Xpc
CC       indicating a reduced NER capacity. A single locus Rad23a
CC       deficiency does not show an apparent phenotype (NER competence,
CC       morphology, fertility).
CC   -!- SIMILARITY: Belongs to the RAD23 family.
CC   -!- SIMILARITY: Contains 2 UBA domains.
CC   -!- SIMILARITY: Contains 1 ubiquitin-like domain.
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DR   EMBL; X92410; CAA63145.1; -; mRNA.
DR   IPI; IPI00307988; -.
DR   UniGene; Mm.255539; -.
DR   ProteinModelPortal; P54726; -.
DR   SMR; P54726; 1-363.
DR   STRING; P54726; -.
DR   PhosphoSite; P54726; -.
DR   PRIDE; P54726; -.
DR   Ensembl; ENSMUST00000003911; ENSMUSP00000003911; ENSMUSG00000003813.
DR   MGI; MGI:105126; Rad23a.
DR   eggNOG; maNOG09231; -.
DR   HOGENOM; HBG738030; -.
DR   HOVERGEN; HBG055042; -.
DR   InParanoid; P54726; -.
DR   PhylomeDB; P54726; -.
DR   ArrayExpress; P54726; -.
DR   Bgee; P54726; -.
DR   CleanEx; MM_RAD23A; -.
DR   Genevestigator; P54726; -.
DR   GermOnline; ENSMUSG00000003813; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   GO; GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR004806; Rad23.
DR   InterPro; IPR006636; STI1_HS-bd.
DR   InterPro; IPR009060; UBA-like.
DR   InterPro; IPR000449; UBA/transl_elong_EF1B_N.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   InterPro; IPR000626; Ubiquitin.
DR   InterPro; IPR019955; Ubiquitin_supergroup.
DR   InterPro; IPR015360; XPC-bd.
DR   Gene3D; G3DSA:1.10.10.540; XPC-bd; 1.
DR   Pfam; PF00627; UBA; 2.
DR   Pfam; PF00240; ubiquitin; 1.
DR   Pfam; PF09280; XPC-binding; 1.
DR   PRINTS; PR01839; RAD23PROTEIN.
DR   SMART; SM00727; STI1; 1.
DR   SMART; SM00165; UBA; 2.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF46934; UBA_like; 2.
DR   SUPFAM; SSF101238; XPC-bd; 1.
DR   TIGRFAMs; TIGR00601; rad23; 1.
DR   PROSITE; PS50030; UBA; 2.
DR   PROSITE; PS00299; UBIQUITIN_1; FALSE_NEG.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
KW   DNA damage; DNA repair; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Proteasome; Repeat; Ubl conjugation.
FT   CHAIN         1    363       UV excision repair protein RAD23 homolog
FT                                A.
FT                                /FTId=PRO_0000114905.
FT   DOMAIN        1     79       Ubiquitin-like.
FT   DOMAIN      161    201       UBA 1.
FT   DOMAIN      318    358       UBA 2.
FT   MOD_RES     123    123       Phosphoserine.
FT   MOD_RES     128    128       Phosphoserine (By similarity).
FT   MOD_RES     133    133       Phosphoserine (By similarity).
FT   MOD_RES     205    205       Phosphoserine (By similarity).
FT   MOD_RES     295    295       Phosphoserine (By similarity).
FT   MOD_RES     357    357       Phosphoserine.
FT   CROSSLNK    122    122       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
SQ   SEQUENCE   363 AA;  39770 MW;  67EAB96EEBA5C203 CRC64;
     MAVTITLKTL QQQTFKIRME PDETVKVLKE KIEAEKGRDA FPVAGQKLIY AGKILSDDVP
     IRDYHIDEKN FVVVMVTKAK AGQGISAPPE ASPTAVPEPS TPFPPVLASG MSHPPPTSRE
     DKSPSEESTT TTSPESISGS VPSSGSSGRE EDAASTLVTG SEYETMLTEI MSMGYERERV
     VAALRASYNN PHRAVEYLLT GIPGSPEPEH GSVQESQRAE QPATEAAGEN PLEFLRDQPQ
     FQNMRQVIQQ NPALLPALLQ QLGQENPQLL QQISRHQEQF IQMLNEPPGE LADISDVEGE
     VGAIGEEAPQ MNYIQVTPQE KEAIERLKAL GFPESLVIQA YFACEKNENL AANFLLSQNF
     DDE
//
ID   FAF1_MOUSE              Reviewed;         649 AA.
AC   P54731;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=FAS-associated factor 1;
GN   Name=Faf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96102221; PubMed=8524870; DOI=10.1073/pnas.92.25.11894;
RA   Chu K., Niu X., Williams L.T.;
RT   "A Fas-associated protein factor, FAF1, potentiates Fas-mediated
RT   apoptosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:11894-11898(1995).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-579, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Potentiates but cannot initiate FAS-induced apoptosis.
CC   -!- SUBUNIT: Specifically interacts with the cytoplasmic domain of
CC       FAS.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- SIMILARITY: Contains 1 UBX domain.
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DR   EMBL; U39643; AAA92091.1; -; mRNA.
DR   IPI; IPI00108791; -.
DR   UniGene; Mm.318259; -.
DR   ProteinModelPortal; P54731; -.
DR   SMR; P54731; 5-44, 98-190, 194-265, 324-494, 568-649.
DR   STRING; P54731; -.
DR   PhosphoSite; P54731; -.
DR   PRIDE; P54731; -.
DR   Ensembl; ENSMUST00000102724; ENSMUSP00000099785; ENSMUSG00000010517.
DR   MGI; MGI:109419; Faf1.
DR   eggNOG; roNOG08513; -.
DR   HOGENOM; HBG446902; -.
DR   HOVERGEN; HBG002876; -.
DR   InParanoid; P54731; -.
DR   OrthoDB; EOG4229JC; -.
DR   PhylomeDB; P54731; -.
DR   ArrayExpress; P54731; -.
DR   Bgee; P54731; -.
DR   CleanEx; MM_FAF1; -.
DR   Genevestigator; P54731; -.
DR   GermOnline; ENSMUSG00000010517; Mus musculus.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0031072; F:heat shock protein binding; ISS:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR   GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; ISS:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptosis; IDA:MGI.
DR   GO; GO:0031334; P:positive regulation of protein complex assembly; ISS:UniProtKB.
DR   GO; GO:0030155; P:regulation of cell adhesion; IMP:MGI.
DR   GO; GO:0042176; P:regulation of protein catabolic process; ISS:UniProtKB.
DR   InterPro; IPR006577; UAS.
DR   InterPro; IPR001012; UBX.
DR   Pfam; PF00789; UBX; 1.
DR   SMART; SM00594; UAS; 1.
DR   SMART; SM00166; UBX; 1.
DR   PROSITE; PS50033; UBX; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Nucleus; Phosphoprotein.
FT   CHAIN         1    649       FAS-associated factor 1.
FT                                /FTId=PRO_0000211039.
FT   DOMAIN      568    645       UBX.
FT   MOD_RES     224    224       Phosphotyrosine (By similarity).
FT   MOD_RES     269    269       Phosphoserine.
FT   MOD_RES     319    319       Phosphoserine (By similarity).
FT   MOD_RES     579    579       Phosphothreonine.
FT   MOD_RES     581    581       Phosphoserine (By similarity).
SQ   SEQUENCE   649 AA;  73834 MW;  4E54881196B1A905 CRC64;
     MASNMDLPMI LADFQACTGI ENIDEAITLL EQNNWDLVAA INGVIPQENG ILQSDFGGET
     MPGPTFDPAS HPAPASTPSS SAFRPVMPSR QIVERQPRML DFRVEYRDRN VDVVLEDSCT
     VGEIKQILEN ELQIPVPKML LKGWKTGDVE DSTVLKSLHL PKNNSLYVLT PDLPPPSSSS
     HAGALQESLN QNFMLIITHR EVQREYNLNF SGSSTVQEVK RNVYDLTSIP VRHQLWEGWP
     ASATDDSMCL AESGLSYPCH RLTVGRRTSP VQTREQSEEQ STDVHMVSDS DGDDFEDASE
     FGVDDGEVFG MASSTLRKSP MMPENAENEG DALLQFTAEF SSRYSDCHPV FYIGSLEAAF
     QEAFYVKARD RKLLAIYLHH DESVLTNVFC SQMLCAESIV SYLSQNFITW AWDLTKDTNR
     ARFLTMCNRH FGSVIAQTIR TQKTDQFPLF LIIMGKRSSN EVLNVIQGNT TVDELMMRLM
     AAMEIFSAQQ QEDIKDEDER EARENVKREQ DEAYRLSLEA DRAKREAHER EMAEQFRLEQ
     IRKEQEEERE AIRLSLEQAL PPEPKEENAE PVSKLRIRTP SGEFLERRFL ASNKLQIVFD
     FVASKGFPWD EFKLLSTFPR RDVTQLDPNK SLLEVNLFPQ ETLFLQAKE
//
ID   EPHB2_MOUSE             Reviewed;         994 AA.
AC   P54763; Q62213; Q9QVY4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2003, sequence version 2.
DT   08-MAR-2011, entry version 122.
DE   RecName: Full=Ephrin type-B receptor 2;
DE            EC=2.7.10.1;
DE   AltName: Full=Neural kinase;
DE   AltName: Full=Nuk receptor tyrosine kinase;
DE   AltName: Full=Tyrosine-protein kinase receptor EPH-3;
DE   AltName: Full=Tyrosine-protein kinase receptor SEK-3;
DE   Flags: Precursor;
GN   Name=Ephb2; Synonyms=Epth3, Nuk, Sek3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=94181250; PubMed=8134103;
RA   Henkemeyer M., Marengere L.E., McGlade J., Olivier J.P., Conlon R.A.,
RA   Holmyard D.P., Letwin K., Pawson T.;
RT   "Immunolocalization of the Nuk receptor tyrosine kinase suggests roles
RT   in segmental patterning of the brain and axonogenesis.";
RL   Oncogene 9:1001-1014(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 516-994 (ISOFORM 2).
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=95034306; PubMed=7947319; DOI=10.1016/0925-4773(94)90091-4;
RA   Becker N., Seitanidou T., Murphy P., Mattei M.-G., Topilko P.,
RA   Nieto A., Wilkinson D.G., Charnay P., Gilardi P.;
RT   "Several receptor tyrosine kinase genes of the Eph family are
RT   segmentally expressed in the developing hindbrain.";
RL   Mech. Dev. 47:3-17(1994).
RN   [3]
RP   FUNCTION.
RX   MEDLINE=20171264; PubMed=10704386;
RA   Imondi R., Wideman C., Kaprielian Z.;
RT   "Complementary expression of transmembrane ephrins and their receptors
RT   in the mouse spinal cord: a possible role in constraining the
RT   orientation of longitudinally projecting axons.";
RL   Development 127:1397-1410(2000).
RN   [4]
RP   INTERACTION WITH PRKCABP AND GRIP1.
RX   MEDLINE=99098206; PubMed=9883737; DOI=10.1016/S0896-6273(00)80663-7;
RA   Torres R., Firestein B.L., Dong H., Staudinger J., Olson E.N.,
RA   Huganir R.L., Bredt D.S., Gale N.W., Yancopoulos G.D.;
RT   "PDZ proteins bind, cluster, and synaptically colocalize with Eph
RT   receptors and their ephrin ligands.";
RL   Neuron 21:1453-1463(1998).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-490, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-273, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH ARHGEF15.
RX   PubMed=21029865; DOI=10.1016/j.cell.2010.09.038;
RA   Margolis S.S., Salogiannis J., Lipton D.M., Mandel-Brehm C.,
RA   Wills Z.P., Mardinly A.R., Hu L., Greer P.L., Bikoff J.B., Ho H.Y.,
RA   Soskis M.J., Sahin M., Greenberg M.E.;
RT   "EphB-mediated degradation of the RhoA GEF Ephexin5 relieves a
RT   developmental brake on excitatory synapse formation.";
RL   Cell 143:442-455(2010).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 29-204.
RX   PubMed=9853759; DOI=10.1038/24904;
RA   Himanen J.-P., Henkemeyer M., Nikolov D.B.;
RT   "Crystal structure of the ligand-binding domain of the receptor
RT   tyrosine kinase EphB2.";
RL   Nature 396:486-491(1998).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 29-208 IN COMPLEX WITH
RP   EPHRIN-B2.
RX   PubMed=11780069; DOI=10.1038/414933a;
RA   Himanen J.-P., Rajashankar K.R., Lackmann M., Cowan C.A.,
RA   Henkemeyer M., Nikolov D.B.;
RT   "Crystal structure of an Eph receptor-ephrin complex.";
RL   Nature 414:933-938(2001).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 27-207 IN COMPLEX WITH EPHA5.
RX   PubMed=15107857; DOI=10.1038/nn1237;
RA   Himanen J.P., Chumley M.J., Lackmann M., Li C., Barton W.A.,
RA   Jeffrey P.D., Vearing C., Geleick D., Feldheim D.A., Boyd A.W.,
RA   Henkemeyer M., Nikolov D.B.;
RT   "Repelling class discrimination: ephrin-A5 binds to and activates
RT   EphB2 receptor signaling.";
RL   Nat. Neurosci. 7:501-509(2004).
CC   -!- FUNCTION: Receptor for members of the ephrin-B family.
CC       Phosphorylates ARHGEF15, leading to its ubiquitination and
CC       degradation by the proteasome which promotes EFNB1-dependent
CC       synapse formation. Can function in aspects of retinal ganglion
CC       cell axon guidance to the optic disk even when lacking its
CC       tyrosine kinase domain.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBUNIT: Interacts with PRKCABP. The ligand-activated form
CC       interacts with multiple proteins, including GTPase-activating
CC       protein (RASGAP) through its SH2 domain. Binds RASGAP through the
CC       juxtamembrane tyrosines residues (By similarity). Interacts with
CC       PRKCABP and GRIP1. Interacts with ARHGEF15.
CC   -!- INTERACTION:
CC       O08543:Efna5; NbExp=1; IntAct=EBI-537711, EBI-1038734;
CC       Q60631:Grb2; NbExp=1; IntAct=EBI-537711, EBI-1688;
CC       Q925T6:Grip1; NbExp=1; IntAct=EBI-537711, EBI-537752;
CC       P34152:Ptk2; NbExp=1; IntAct=EBI-537711, EBI-77070;
CC       P05480:Src; NbExp=1; IntAct=EBI-537711, EBI-298680;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P54763-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P54763-2; Sequence=VSP_015714;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in cells of the developing outer
CC       retina.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Ephrin receptor subfamily.
CC   -!- SIMILARITY: Contains 2 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA72411.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; L25890; AAA72411.1; ALT_INIT; mRNA.
DR   EMBL; X76011; CAA53598.1; -; mRNA.
DR   IPI; IPI00108870; -.
DR   IPI; IPI00649277; -.
DR   UniGene; Mm.250981; -.
DR   PDB; 1JPA; X-ray; 1.91 A; A/B=595-906.
DR   PDB; 1KGY; X-ray; 2.70 A; A/B/C/D=28-207.
DR   PDB; 1NUK; X-ray; 2.90 A; A=28-210.
DR   PDB; 1SHW; X-ray; 2.20 A; B=27-207.
DR   PDB; 2HEN; X-ray; 2.60 A; A/B/C/D=622-906.
DR   PDB; 3ETP; X-ray; 2.00 A; A=28-207.
DR   PDBsum; 1JPA; -.
DR   PDBsum; 1KGY; -.
DR   PDBsum; 1NUK; -.
DR   PDBsum; 1SHW; -.
DR   PDBsum; 2HEN; -.
DR   PDBsum; 3ETP; -.
DR   ProteinModelPortal; P54763; -.
DR   SMR; P54763; 27-539, 621-901, 918-993.
DR   IntAct; P54763; 13.
DR   MINT; MINT-3381667; -.
DR   STRING; P54763; -.
DR   PhosphoSite; P54763; -.
DR   PRIDE; P54763; -.
DR   Ensembl; ENSMUST00000105845; ENSMUSP00000101471; ENSMUSG00000028664.
DR   Ensembl; ENSMUST00000105846; ENSMUSP00000101472; ENSMUSG00000028664.
DR   MGI; MGI:99611; Ephb2.
DR   GeneTree; ENSGT00570000078802; -.
DR   HOVERGEN; HBG062180; -.
DR   OrthoDB; EOG4W9J35; -.
DR   BRENDA; 2.7.10.1; 244.
DR   ArrayExpress; P54763; -.
DR   Bgee; P54763; -.
DR   CleanEx; MM_EPHB2; -.
DR   Genevestigator; P54763; -.
DR   GermOnline; ENSMUSG00000028664; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0045202; C:synapse; NAS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008046; F:axon guidance receptor activity; IDA:MGI.
DR   GO; GO:0005102; F:receptor binding; IPI:MGI.
DR   GO; GO:0005005; F:transmembrane-ephrin receptor activity; TAS:MGI.
DR   GO; GO:0048593; P:camera-type eye morphogenesis; IMP:MGI.
DR   GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IMP:MGI.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:MGI.
DR   GO; GO:0007612; P:learning; IMP:MGI.
DR   GO; GO:0050771; P:negative regulation of axonogenesis; IDA:MGI.
DR   GO; GO:0021631; P:optic nerve morphogenesis; IMP:MGI.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
DR   GO; GO:0048170; P:positive regulation of long-term neuronal synaptic plasticity; IMP:MGI.
DR   GO; GO:0031290; P:retinal ganglion cell axon guidance; IDA:MGI.
DR   InterPro; IPR001090; Ephrin_rcpt_lig-bd.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR009030; Growth_fac_rcpt.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   InterPro; IPR016257; Tyr_prot_kinase_ephrin_rcpt.
DR   InterPro; IPR001426; Tyr_prot_kinase_rcpt_V_CS.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF01404; Ephrin_lbd; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07699; GCC2_GCC3; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00615; EPH_lbd; 1.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; FN_III-like; 2.
DR   SUPFAM; SSF49785; Gal_bind_like; 1.
DR   SUPFAM; SSF57184; Grow_fac_recept; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
DR   PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Disulfide bond;
KW   Glycoprotein; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Receptor; Repeat; Signal; Transferase; Transmembrane;
KW   Transmembrane helix; Tyrosine-protein kinase.
FT   SIGNAL        1     26       Potential.
FT   CHAIN        27    994       Ephrin type-B receptor 2.
FT                                /FTId=PRO_0000016828.
FT   TOPO_DOM     27    551       Extracellular (Potential).
FT   TRANSMEM    552    572       Helical; (Potential).
FT   TOPO_DOM    573    994       Cytoplasmic (Potential).
FT   DOMAIN      333    434       Fibronectin type-III 1.
FT   DOMAIN      440    535       Fibronectin type-III 2.
FT   DOMAIN      629    892       Protein kinase.
FT   DOMAIN      921    985       SAM.
FT   NP_BIND     635    643       ATP (By similarity).
FT   MOTIF       992    994       PDZ-binding (Potential).
FT   COMPBIAS    192    329       Cys-rich.
FT   ACT_SITE    754    754       Proton acceptor (By similarity).
FT   BINDING     661    661       ATP (By similarity).
FT   MOD_RES     156    156       Phosphoserine (By similarity).
FT   MOD_RES     604    604       Phosphotyrosine (By similarity).
FT   MOD_RES     610    610       Phosphotyrosine (By similarity).
FT   MOD_RES     783    783       Phosphothreonine (By similarity).
FT   MOD_RES     784    784       Phosphoserine (By similarity).
FT   MOD_RES     787    787       Phosphothreonine (By similarity).
FT   MOD_RES     788    788       Phosphotyrosine (By similarity).
FT   MOD_RES     905    905       Phosphoserine (By similarity).
FT   MOD_RES     991    991       Phosphoserine (By similarity).
FT   CARBOHYD    273    273       N-linked (GlcNAc...).
FT   CARBOHYD    344    344       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    436    436       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    490    490       N-linked (GlcNAc...).
FT   DISULFID     70    192
FT   DISULFID    105    115
FT   VAR_SEQ     576    576       R -> RR (in isoform 2).
FT                                /FTId=VSP_015714.
FT   STRAND       28     33
FT   HELIX        34     36
FT   STRAND       44     47
FT   STRAND       52     57
FT   STRAND       63     70
FT   STRAND       74     76
FT   STRAND       79     82
FT   STRAND       92    103
FT   HELIX       105    107
FT   STRAND      108    110
FT   STRAND      116    128
FT   STRAND      133    136
FT   TURN        140    142
FT   STRAND      143    150
FT   STRAND      168    174
FT   STRAND      179    203
FT   HELIX       607    609
FT   STRAND      610    612
FT   HELIX       613    620
FT   HELIX       626    628
FT   STRAND      629    637
FT   STRAND      639    648
FT   STRAND      656    662
FT   HELIX       669    682
FT   STRAND      693    697
FT   STRAND      699    702
FT   STRAND      704    708
FT   HELIX       715    720
FT   TURN        721    724
FT   HELIX       728    747
FT   HELIX       757    759
FT   STRAND      760    762
FT   STRAND      768    770
FT   HELIX       798    800
FT   HELIX       803    807
FT   HELIX       813    828
FT   TURN        834    837
FT   HELIX       840    848
FT   HELIX       861    870
FT   TURN        875    877
FT   HELIX       881    893
FT   HELIX       895    898
SQ   SEQUENCE   994 AA;  110760 MW;  BC6B9B12A070394C CRC64;
     MGARVPVLPG LDGSFCWLLL LPLLAAVEET LMDSTTATAE LGWMVHPPSG WEEVSGYDEN
     MNTIRTYQVC NVFESSQNNW LRTKFIRRRG AHRIHVEMKF SVRDCSSIPS VPGSCKETFN
     LYYYEADFDL ATKTFPNWME NPWVKVDTIA ADESFSQVDL GGRVMKINTE VRSFGPVSRN
     GFYLAFQDYG GCMSLIAVRV FYRKCPRIIQ NGAIFQETLS GAESTSLVAA RGSCIANAEE
     VDVPIKLYCN GDGEWLVPIG RCMCKAGFEA VENGTVCRGC PSGTFKANQG DEACTHCPIN
     SRTTSEGATN CVCRNGYYRA DLDPLDMPCT TIPSAPQAVI SSVNETSLML EWTPPRDSGG
     REDLVYNIIC KSCGSGRGAC TRCGDNVQYA PRQLGLTEPR IYISDLLAHT QYTFEIQAVN
     GVTDQSPFSP QFASVNITTN QAAPSAVSIM HQVSRTVDSI TLSWSQPDQP NGVILDYELQ
     YYEKELSEYN ATAIKSPTNT VTVQGLKAGA IYVFQVRART VAGYGRYSGK MYFQTMTEAE
     YQTSIKEKLP LIVGSSAAGL VFLIAVVVIA IVCNRRGFER ADSEYTDKLQ HYTSGHMTPG
     MKIYIDPFTY EDPNEAVREF AKEIDISCVK IEQVIGAGEF GEVCSGHLKL PGKREIFVAI
     KTLKSGYTEK QRRDFLSEAS IMGQFDHPNV IHLEGVVTKS TPVMIITEFM ENGSLDSFLR
     QNDGQFTVIQ LVGMLRGIAA GMKYLADMNY VHRDLAARNI LVNSNLVCKV SDFGLSRFLE
     DDTSDPTYTS ALGGKIPIRW TAPEAIQYRK FTSASDVWSY GIVMWEVMSY GERPYWDMTN
     QDVINAIEQD YRLPPPMDCP SALHQLMLDC WQKDRNHRPK FGQIVNTLDK MIRNPNSLKA
     MAPLSSGINL PLLDRTIPDY TSFNTVDEWL EAIKMGQYKE SFANAGFTSF DVVSQMMMED
     ILRVGVTLAG HQKKILNSIQ VMRAQMNQIQ SVEV
//
ID   DDX6_MOUSE              Reviewed;         483 AA.
AC   P54823; O54979; Q3UFI3; Q8BW68;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Probable ATP-dependent RNA helicase DDX6;
DE            EC=3.6.4.13;
DE   AltName: Full=ATP-dependent RNA helicase p54;
DE   AltName: Full=DEAD box protein 6;
DE   AltName: Full=Oncogene RCK homolog;
GN   Name=Ddx6; Synonyms=Hlr2, Rck;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Spleen;
RX   MEDLINE=96125206; PubMed=8543178; DOI=10.1016/0378-1119(95)00559-5;
RA   Seto M., Yamamoto K., Takahashi T., Ueda R.;
RT   "Cloning and expression of a murine cDNA homologous to the human
RT   RCK/P54, a lymphoma-linked chromosomal translocation junction gene on
RT   11q23.";
RL   Gene 166:293-296(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Oviduct, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 26-478, AND DEVELOPMENTAL STAGE.
RC   STRAIN=CB6F1/J; TISSUE=Oocyte;
RX   MEDLINE=99100034; PubMed=9883581;
RX   DOI=10.1002/(SICI)1520-6408(1998)23:4<285::AID-DVG4>3.0.CO;2-W;
RA   Paynton B.V.;
RT   "RNA-binding proteins in mouse oocytes and embryos: expression of
RT   genes encoding Y box, DEAD box RNA helicase, and polyA binding
RT   proteins.";
RL   Dev. Genet. 23:285-298(1998).
CC   -!- FUNCTION: In the process of mRNA degradation, may play a role in
CC       mRNA decapping.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Forms a complex with DCP1A, DCP2, EDC3 and EDC4/HEDLS (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body (By similarity).
CC       Note=Processing bodies (PB) (By similarity).
CC   -!- DEVELOPMENTAL STAGE: Abundant expression in growing oocytes,
CC       levels decline in primary and secondary oocytes, and degradation
CC       appears to be complete by the mid-late two-cell stage.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX6/DHH1
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
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DR   EMBL; D50494; BAA09088.1; -; mRNA.
DR   EMBL; AK054144; BAC35670.1; -; mRNA.
DR   EMBL; AK148483; BAE28578.1; -; mRNA.
DR   EMBL; BC021452; AAH21452.1; -; mRNA.
DR   EMBL; AF038995; AAB94769.1; -; mRNA.
DR   IPI; IPI00109932; -.
DR   RefSeq; NP_001104296.1; NM_001110826.1.
DR   RefSeq; NP_031867.1; NM_007841.4.
DR   RefSeq; NP_851841.2; NM_181324.3.
DR   UniGene; Mm.267061; -.
DR   ProteinModelPortal; P54823; -.
DR   SMR; P54823; 94-472.
DR   STRING; P54823; -.
DR   PhosphoSite; P54823; -.
DR   PRIDE; P54823; -.
DR   Ensembl; ENSMUST00000098836; ENSMUSP00000096435; ENSMUSG00000032097.
DR   GeneID; 13209; -.
DR   KEGG; mmu:13209; -.
DR   CTD; 13209; -.
DR   MGI; MGI:104976; Ddx6.
DR   eggNOG; roNOG14485; -.
DR   GeneTree; ENSGT00530000063986; -.
DR   HOGENOM; HBG737336; -.
DR   HOVERGEN; HBG106685; -.
DR   InParanoid; P54823; -.
DR   OMA; FHDFRQG; -.
DR   OrthoDB; EOG4J1182; -.
DR   PhylomeDB; P54823; -.
DR   NextBio; 283376; -.
DR   ArrayExpress; P54823; -.
DR   Bgee; P54823; -.
DR   CleanEx; MM_DDX6; -.
DR   Genevestigator; P54823; -.
DR   GermOnline; ENSMUSG00000032097; Mus musculus.
DR   GO; GO:0000932; C:cytoplasmic mRNA processing body; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding;
KW   Phosphoprotein; RNA-binding.
FT   CHAIN         1    483       Probable ATP-dependent RNA helicase DDX6.
FT                                /FTId=PRO_0000054984.
FT   DOMAIN      127    298       Helicase ATP-binding.
FT   DOMAIN      308    468       Helicase C-terminal.
FT   NP_BIND     140    147       ATP (By similarity).
FT   MOTIF        96    124       Q motif.
FT   MOTIF       246    249       DEAD box.
FT   MOD_RES      36     36       Phosphothreonine (By similarity).
FT   MOD_RES     473    473       Phosphotyrosine (By similarity).
FT   CONFLICT     38     42       PQPQL -> TQQQM (in Ref. 4; AAB94769).
FT   CONFLICT    202    202       G -> P (in Ref. 4; AAB94769).
FT   CONFLICT    241    241       Q -> R (in Ref. 3; BAC35670).
FT   CONFLICT    311    311       Q -> E (in Ref. 3; BAC35670).
FT   CONFLICT    381    381       R -> E (in Ref. 4; AAB94769).
FT   CONFLICT    407    407       I -> M (in Ref. 3; BAC35670).
FT   CONFLICT    422    422       I -> V (in Ref. 4; AAB94769).
FT   CONFLICT    478    478       A -> V (in Ref. 4; AAB94769).
SQ   SEQUENCE   483 AA;  54192 MW;  9AD22D171F8BC14D CRC64;
     MSTARTENPV IMGLSSQNGQ LRGPVKASAG PGGGGTQPQP QLNQLKNTST INNGTPQQAQ
     SMAATIKPGD DWKKTLKLPP KDLRIKTSDV TSTKGNEFED YCLKRELLMG IFEMGWEKPS
     PIQEESIPIA LSGRDILARA KNGTGKSGAY LIPLLERLDL KKDNIQAMVI VPTRELALQV
     SQICIQVSKH MGGAKVMATT GGTNLRDDIM RLDDTVHVVI ATPGRILDLI KKGVAKVDHV
     QMIVLDEADK LLSQDFVQIM EDIILTLPKN RQILLYSATF PLSVQKFMNS HLQKPYEINL
     MEELTLKGVT QYYAYVTERQ KVHCLNTLFS RLQINQSIIF CNSSQRVELL AKKISQLGYS
     CFYIHAKMRQ EHRNRVFHDF RNGLCRNLVC TDLFTRGIDI QAVNVVINFD FPKLAETYLH
     RIGRSGRFGH LGLAINLITY DDRFNLKSIE EQLGTEIKPI PSNIDKSLYV AEYHSEPAED
     EKP
//
ID   PTN5_MOUSE              Reviewed;         541 AA.
AC   P54830; Q64694; Q8CAN0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type 5;
DE            EC=3.1.3.48;
DE   AltName: Full=Neural-specific protein-tyrosine phosphatase;
DE   AltName: Full=Striatum-enriched protein-tyrosine phosphatase;
DE            Short=STEP;
GN   Name=Ptpn5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS STEP20; STEP38; STEP46 AND
RP   STEP61).
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=96115113; PubMed=7494467; DOI=10.1016/0169-328X(95)00066-2;
RA   Sharma E., Zhao F., Bult A., Lombroso P.J.;
RT   "Identification of two alternatively spliced transcripts of STEP: a
RT   subfamily of brain-enriched protein tyrosine phosphatases.";
RL   Brain Res. Mol. Brain Res. 32:87-93(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM STEP61).
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM STEP61).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Additional isoforms seem to exist;
CC       Name=STEP61;
CC         IsoId=P54830-1; Sequence=Displayed;
CC       Name=STEP46;
CC         IsoId=P54830-2; Sequence=VSP_005126;
CC       Name=STEP38;
CC         IsoId=P54830-3; Sequence=VSP_005127, VSP_005128;
CC         Note=Lacks the catalytic domain;
CC       Name=STEP20;
CC         IsoId=P54830-4; Sequence=VSP_005126, VSP_005127, VSP_005128;
CC         Note=Lacks the catalytic domain;
CC   -!- TISSUE SPECIFICITY: STEP20 is expressed only in the CNS.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class subfamily.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U28217; AAA73574.1; -; mRNA.
DR   EMBL; U28216; AAA73573.1; -; mRNA.
DR   EMBL; S80329; AAB35656.2; -; mRNA.
DR   EMBL; AK038416; BAC29993.1; -; mRNA.
DR   EMBL; CH466603; EDL22958.1; -; Genomic_DNA.
DR   EMBL; BC079592; AAH79592.1; -; mRNA.
DR   IPI; IPI00275198; -.
DR   IPI; IPI00331399; -.
DR   IPI; IPI00467661; -.
DR   IPI; IPI00474037; -.
DR   RefSeq; NP_001157037.1; NM_001163565.1.
DR   RefSeq; NP_038671.2; NM_013643.2.
DR   UniGene; Mm.4654; -.
DR   ProteinModelPortal; P54830; -.
DR   SMR; P54830; 256-536.
DR   STRING; P54830; -.
DR   PhosphoSite; P54830; -.
DR   PRIDE; P54830; -.
DR   Ensembl; ENSMUST00000033142; ENSMUSP00000033142; ENSMUSG00000030854.
DR   Ensembl; ENSMUST00000102626; ENSMUSP00000099686; ENSMUSG00000030854.
DR   GeneID; 19259; -.
DR   KEGG; mmu:19259; -.
DR   UCSC; uc009haa.1; mouse.
DR   UCSC; uc009hab.1; mouse.
DR   UCSC; uc009hac.1; mouse.
DR   CTD; 19259; -.
DR   MGI; MGI:97807; Ptpn5.
DR   eggNOG; roNOG08830; -.
DR   HOVERGEN; HBG001594; -.
DR   InParanoid; P54830; -.
DR   OMA; QGPIVNT; -.
DR   OrthoDB; EOG4229JX; -.
DR   BRENDA; 3.1.3.48; 244.
DR   NextBio; 296112; -.
DR   ArrayExpress; P54830; -.
DR   Bgee; P54830; -.
DR   CleanEx; MM_PTPN5; -.
DR   Genevestigator; P54830; -.
DR   GermOnline; ENSMUSG00000030854; Mus musculus.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IMP:MGI.
DR   GO; GO:0006470; P:protein dephosphorylation; IMP:MGI.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR008356; Tyr_Pase_KIM-con.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   InterPro; IPR016334; Tyr_Pase_rcpt_R/non-rcpt_5.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PIRSF; PIRSF001997; PTPRR; 1.
DR   PRINTS; PR01778; KIMPTPASE.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Hydrolase; Protein phosphatase.
FT   CHAIN         1    541       Tyrosine-protein phosphatase non-receptor
FT                                type 5.
FT                                /FTId=PRO_0000094756.
FT   DOMAIN      276    531       Tyrosine-protein phosphatase.
FT   REGION      472    478       Substrate binding (By similarity).
FT   ACT_SITE    472    472       Phosphocysteine intermediate (By
FT                                similarity).
FT   BINDING     437    437       Substrate (By similarity).
FT   BINDING     516    516       Substrate (By similarity).
FT   VAR_SEQ       1    172       Missing (in isoform STEP20 and isoform
FT                                STEP46).
FT                                /FTId=VSP_005126.
FT   VAR_SEQ     337    346       GYSGEEKVYI -> VCSSIPRAFH (in isoform
FT                                STEP38 and isoform STEP20).
FT                                /FTId=VSP_005127.
FT   VAR_SEQ     347    541       Missing (in isoform STEP38 and isoform
FT                                STEP20).
FT                                /FTId=VSP_005128.
FT   CONFLICT    426    426       S -> T (in Ref. 1; AAA73574).
SQ   SEQUENCE   541 AA;  60815 MW;  31A0D2C9139F90A4 CRC64;
     MCCSERLLGL PQPVEMEAPD EAEGLPSKQK EMPPPPPPSP PSEPAQKLPP QGAGSHSLTV
     RSSLCLFAAS QFLLACGVLW LSGHGHSWLQ NTTDLISSSL TVLNHLGPVA WLGSGTWGIP
     SLLLVSLTVS LVIVTTLVWH LLKAPPEPPA PLPPEDRRQS VSRQPSFTYS EWMEEKVEDD
     FLDLDAVPET PVFDCVMDIK PETDPASLTV KSMGLQERRG SNVSLTLDMC TPGCNEEGFG
     YLVSPREESA HEYLLSASRV LRAEELHEKA LDPFLLQAEF FEIPMNFVDP KEYDIPGLVR
     KNRYKTILPN PHSRVRLTSP DPEDPLSSYI NANYIRGYSG EEKVYIATQG PIVSTVADFW
     RMVWQERTPI IVMITNIEEM NEKCTEYWPE EQVVHDGVEI TVQKVIHTED YRLRLISLRR
     GTEERSLKHY WFTSWPDQKT PDRAPPLLHL VREVEEAAQQ EGPHCSPIIV HCSAGIGRTG
     CFIATSICCQ QLRREGVVDI LKTTCQLRQD RGGMIQTCEQ YQFVHHAMSL YEKQLSLQSS
     E
//
ID   S12A2_MOUSE             Reviewed;        1205 AA.
AC   P55012;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Solute carrier family 12 member 2;
DE   AltName: Full=Basolateral Na-K-Cl symporter;
DE   AltName: Full=Bumetanide-sensitive sodium-(potassium)-chloride cotransporter 1;
GN   Name=Slc12a2; Synonyms=Nkcc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=95014374; PubMed=7929272;
RA   Delpire E., Rauchman M.I., Beier D.R., Hebert S.C., Gullans S.R.;
RT   "Molecular cloning and chromosome localization of a putative
RT   basolateral Na(+)-K(+)-2Cl-cotransporter from mouse inner medullary
RT   collecting duct (mIMCD-3) cells.";
RL   J. Biol. Chem. 269:25677-25683(1994).
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-544 AND ASN-546, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
CC   -!- FUNCTION: Electrically silent transporter system. Mediates sodium
CC       and chloride reabsorption. Plays a vital role in the regulation of
CC       ionic balance and cell volume.
CC   -!- INTERACTION:
CC       P47811:Mapk14; NbExp=1; IntAct=EBI-621078, EBI-298727;
CC       Q9Z1W9:Stk39; NbExp=2; IntAct=EBI-621078, EBI-444764;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the SLC12A transporter family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U13174; AAC77832.1; -; mRNA.
DR   IPI; IPI00135324; -.
DR   PIR; A55015; A55015.
DR   RefSeq; NP_033220.2; NM_009194.3.
DR   UniGene; Mm.399997; -.
DR   ProteinModelPortal; P55012; -.
DR   IntAct; P55012; 6.
DR   STRING; P55012; -.
DR   PhosphoSite; P55012; -.
DR   PRIDE; P55012; -.
DR   Ensembl; ENSMUST00000115366; ENSMUSP00000111023; ENSMUSG00000024597.
DR   GeneID; 20496; -.
DR   KEGG; mmu:20496; -.
DR   CTD; 20496; -.
DR   MGI; MGI:101924; Slc12a2.
DR   eggNOG; roNOG13940; -.
DR   HOGENOM; HBG446860; -.
DR   HOVERGEN; HBG052851; -.
DR   InParanoid; P55012; -.
DR   OrthoDB; EOG4FR0QZ; -.
DR   PhylomeDB; P55012; -.
DR   NextBio; 298651; -.
DR   ArrayExpress; P55012; -.
DR   Bgee; P55012; -.
DR   CleanEx; MM_SLC12A2; -.
DR   Genevestigator; P55012; -.
DR   GermOnline; ENSMUSG00000024597; Mus musculus.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IMP:MGI.
DR   GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR004841; AA-permease_dom.
DR   InterPro; IPR013612; AA_permease_N.
DR   InterPro; IPR002443; Na/K/Cl_cotranspt.
DR   InterPro; IPR002444; Na/K/Cl_cotranspt1.
DR   InterPro; IPR004842; Na/K/Cl_cotransptS.
DR   Pfam; PF00324; AA_permease; 1.
DR   Pfam; PF08403; AA_permease_N; 1.
DR   PRINTS; PR01207; NAKCLTRNSPRT.
DR   PRINTS; PR01208; NAKCLTRSPRT1.
DR   TIGRFAMs; TIGR00930; 2a30; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Ion transport; Membrane; Phosphoprotein; Potassium;
KW   Potassium transport; Sodium; Sodium transport; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1   1205       Solute carrier family 12 member 2.
FT                                /FTId=PRO_0000178024.
FT   TOPO_DOM      1    278       Cytoplasmic (Potential).
FT   TRANSMEM    279    299       Helical; (Potential).
FT   TOPO_DOM    300    302       Extracellular (Potential).
FT   TRANSMEM    303    323       Helical; (Potential).
FT   TOPO_DOM    324    359       Cytoplasmic (Potential).
FT   TRANSMEM    360    380       Helical; (Potential).
FT   TOPO_DOM    381    403       Extracellular (Potential).
FT   TRANSMEM    404    424       Helical; (Potential).
FT   TOPO_DOM    425    428       Cytoplasmic (Potential).
FT   TRANSMEM    429    449       Helical; (Potential).
FT   TOPO_DOM    450    479       Extracellular (Potential).
FT   TRANSMEM    480    500       Helical; (Potential).
FT   TOPO_DOM    501    513       Cytoplasmic (Potential).
FT   TRANSMEM    514    534       Helical; (Potential).
FT   TOPO_DOM    535    584       Extracellular (Potential).
FT   TRANSMEM    585    605       Helical; (Potential).
FT   TOPO_DOM    606    644       Cytoplasmic (Potential).
FT   TRANSMEM    645    667       Helical; (Potential).
FT   TOPO_DOM    668    673       Extracellular (Potential).
FT   TRANSMEM    674    691       Helical; (Potential).
FT   TOPO_DOM    692    709       Cytoplasmic (Potential).
FT   TRANSMEM    710    730       Helical; (Potential).
FT   TOPO_DOM    731    892       Extracellular (Potential).
FT   TRANSMEM    893    913       Helical; (Potential).
FT   TOPO_DOM    914   1205       Cytoplasmic (Potential).
FT   COMPBIAS     87    117       Ala-rich.
FT   MOD_RES      74     74       Phosphoserine (By similarity).
FT   MOD_RES      76     76       Phosphoserine (By similarity).
FT   MOD_RES     259    259       Phosphothreonine (By similarity).
FT   MOD_RES     933    933       Phosphoserine (By similarity).
FT   MOD_RES     987    987       Phosphoserine (By similarity).
FT   CARBOHYD    544    544       N-linked (GlcNAc...).
FT   CARBOHYD    546    546       N-linked (GlcNAc...).
FT   CARBOHYD    555    555       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   1205 AA;  130950 MW;  A93D2A046837712C CRC64;
     MEPGPAGPRL APAARPGWGR AAGCRRRGGP ARHGRASGQE DATTAGRQAG GGVRGEGTPA
     AGDGLGRPLG PTPSQSRFQV DPVSENAGRA AAAAAAAAAA AAAAGAAGKE TPAAGKAGGE
     SGVAKGSEEA KGRFRVNFVD PAASSSADDS LSDAAGVGGD GPNVSFQNGG DTVLSEGSSL
     HSGGGSGHHQ QYYYDTHTNT YYLRTFGHNT MDAVPRIDHY RHTAAQLGEK LLRPSLAELH
     DELEKEPFED GFANGEESTP TRDAVVAYTA ESKGVVKFGW IKGVLVRCML NIWGVMLFIR
     LSWIVGQAGI GLSVVVIAMA TVVTTITGLS TSAIATNGFV RGGGAYYLIS RSLGPEFGGA
     IGLIFAFANA VAVAMYVVGF AETVVELLKE HSILMIDEIN DIRIIGAITV VILLGISVAG
     MEWEAKAQIV LLVILLLAIA DFVIGTFISL ESKKPKGFFG YKSEIFNENF GPDFREEETF
     FSVFAIFFPA ATGILAGANI SGDLADPQSA IPKGTLLAIL ITTVVYIGIA VSVGSCVVRD
     ATGNVNDTIT TELTNCTSAA CKLNFDFSYC ESNTCSYGLM NNFQVMSMVS GFAPLISAGI
     FSATLSSALA SLVSAPKIFQ ALCKDNIYPA FQMFAKGYGK NNEPLRGYIL TFLIALGFIL
     IAELNVIAPI ISNFFLASYA LINFSVFHAS LAKSPGWRPA FKYYNMWISL IGAILCCIVM
     FVINWWAALL TYVIVLGLYI YVTYKKPDVN WGSSTQALTY LSALQHSIRL SGVEDHVKNF
     RPQCLVMTGS PNSRPALLHL VHDFTKNVGL MICGHVHMGP RRQAMKEMSI DQARYQRWLI
     KNKMKAFYAP VHADDLREGA QYLMQAAGLG RMKPNTLVLG FKKDWLQADM RDVDMYINLF
     HDAFDIQFGV VVIRLKEGLD ISHLQGQEEL LSSQEKSPGT KDVVVNVDYS KKSDQDTCKS
     SGEKSITQKD EEEDGKTPTQ PLLKKESKGP IVPLNVADQK LLEASTQFQK KQGKNTIDVW
     WLFDDGGLTL LIPYLLTTKK KWKDCKIRVF IGGKINRIDH DRRAMATLLS KFRIDFSDIM
     VLGDINTKPK KENIIAYDDM IEPYRLHEDD KEQDIADKMK EDEPWRITDN ELELYKTKTY
     RQIRLNELLK EHSSTANIIV MSLPVARKGA VSSALYMAWL EALSKDLPPV LLVRGNHQSV
     LTFYS
//
ID   AQP4_MOUSE              Reviewed;         323 AA.
AC   P55088; P97818; Q4FJP1; Q61131; Q61132; Q8VHE4; Q8VHE5; Q9EQI3;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Aquaporin-4;
DE            Short=AQP-4;
DE   AltName: Full=Mercurial-insensitive water channel;
DE            Short=MIWC;
DE   AltName: Full=WCH4;
GN   Name=Aqp4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=96299634; PubMed=8660998; DOI=10.1006/geno.1996.0214;
RA   Ma T., Yang B., Verkman A.S.;
RT   "Gene structure, cDNA cloning, and expression of a mouse mercurial-
RT   insensitive water channel.";
RL   Genomics 33:382-388(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=97288526; PubMed=9143504; DOI=10.1006/geno.1997.4641;
RA   Turtzo L.C., Lee M.D., Lu M., Smith B.L., Copeland N.G., Gilbert D.J.,
RA   Jenkins N.A., Agre P.;
RT   "Cloning and chromosomal localization of mouse aquaporin 4: exclusion
RT   of a candidate mutant phenotype, ataxia.";
RL   Genomics 41:267-270(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT ARG-4.
RX   MEDLINE=20419017; PubMed=10960499;
RX   DOI=10.1203/00006450-200009000-00012;
RA   Zelenin S., Gunnarson E., Alikina T., Bondar A., Aperia A.;
RT   "Identification of a new form of AQP4 mRNA that is developmentally
RT   expressed in mouse brain.";
RL   Pediatr. Res. 48:335-339(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA   Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E.,
RA   Mollenhauer J., Wiemann S., Schick M., Korn B.;
RT   "Cloning of mouse full open reading frames in Gateway(R) system entry
RT   vector (pDONR201).";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Forms a water-specific channel. Osmoreceptor which
CC       regulates body water balance and mediates water flow within the
CC       central nervous system.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=2; Synonyms=MIWC2, AQP4-M1;
CC         IsoId=P55088-1; Sequence=Displayed;
CC       Name=1; Synonyms=MIWC1, AQP4-M21;
CC         IsoId=P55088-2; Sequence=VSP_003233;
CC       Name=3; Synonyms=MIWC3;
CC         IsoId=P55088-3; Sequence=VSP_003234;
CC   -!- DOMAIN: Aquaporins contain two tandem repeats each containing
CC       three membrane-spanning domains and a pore-forming loop with the
CC       signature motif Asn-Pro-Ala (NPA).
CC   -!- PTM: Phosphorylation by PKC at Ser-180 reduces conductance by 50%.
CC       Phosphorylation by PKG at Ser-111 in response to glutamats
CC       increases conductance by 40% (By similarity).
CC   -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U48398; AAB41569.1; -; mRNA.
DR   EMBL; U48397; AAB41568.1; -; mRNA.
DR   EMBL; U33012; AAA84923.1; -; mRNA.
DR   EMBL; U48400; AAB41571.1; -; Genomic_DNA.
DR   EMBL; U48399; AAB41570.1; -; mRNA.
DR   EMBL; U88623; AAC53155.1; -; mRNA.
DR   EMBL; AF469168; AAL73545.1; -; mRNA.
DR   EMBL; AF469169; AAL73546.1; -; mRNA.
DR   EMBL; AF219992; AAG44243.2; -; Genomic_DNA.
DR   EMBL; CT010362; CAJ18569.1; -; mRNA.
DR   EMBL; BC024526; AAH24526.1; -; mRNA.
DR   IPI; IPI00135626; -.
DR   IPI; IPI00230737; -.
DR   IPI; IPI00230738; -.
DR   RefSeq; NP_033830.2; NM_009700.2.
DR   UniGene; Mm.250786; -.
DR   ProteinModelPortal; P55088; -.
DR   SMR; P55088; 31-254.
DR   STRING; P55088; -.
DR   PhosphoSite; P55088; -.
DR   PRIDE; P55088; -.
DR   Ensembl; ENSMUST00000079081; ENSMUSP00000078088; ENSMUSG00000024411.
DR   Ensembl; ENSMUST00000115856; ENSMUSP00000111522; ENSMUSG00000024411.
DR   GeneID; 11829; -.
DR   KEGG; mmu:11829; -.
DR   UCSC; uc008eds.1; mouse.
DR   CTD; 11829; -.
DR   MGI; MGI:107387; Aqp4.
DR   eggNOG; roNOG13236; -.
DR   HOVERGEN; HBG000312; -.
DR   OMA; CSRESIM; -.
DR   OrthoDB; EOG46Q6T5; -.
DR   PhylomeDB; P55088; -.
DR   NextBio; 279739; -.
DR   ArrayExpress; P55088; -.
DR   Bgee; P55088; -.
DR   CleanEx; MM_AQP4; -.
DR   Genevestigator; P55088; -.
DR   GermOnline; ENSMUSG00000024411; Mus musculus.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:MGI.
DR   GO; GO:0015250; F:water channel activity; IDA:UniProtKB.
DR   GO; GO:0070295; P:renal water absorption; IMP:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR   InterPro; IPR012269; Aquaporin.
DR   InterPro; IPR023271; Aquaporin_like.
DR   InterPro; IPR000425; MIP.
DR   InterPro; IPR022357; MIP_CS.
DR   Gene3D; G3DSA:1.20.1080.10; MIP; 1.
DR   PANTHER; PTHR19139; MIP; 1.
DR   Pfam; PF00230; MIP; 1.
DR   PRINTS; PR00783; MINTRINSICP.
DR   SUPFAM; SSF81338; MIP; 1.
DR   TIGRFAMs; TIGR00861; MIP; 1.
DR   PROSITE; PS00221; MIP; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Membrane; Phosphoprotein; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    323       Aquaporin-4.
FT                                /FTId=PRO_0000063949.
FT   TOPO_DOM      1     36       Cytoplasmic (Potential).
FT   TRANSMEM     37     58       Helical; (Potential).
FT   TOPO_DOM     59     64       Extracellular (Potential).
FT   TRANSMEM     65     85       Helical; (Potential).
FT   TOPO_DOM     86    115       Cytoplasmic (Potential).
FT   TRANSMEM    116    136       Helical; (Potential).
FT   TOPO_DOM    137    155       Extracellular (Potential).
FT   TRANSMEM    156    176       Helical; (Potential).
FT   TOPO_DOM    177    184       Cytoplasmic (Potential).
FT   TRANSMEM    185    205       Helical; (Potential).
FT   TOPO_DOM    206    231       Extracellular (Potential).
FT   TRANSMEM    232    252       Helical; (Potential).
FT   TOPO_DOM    253    323       Cytoplasmic (Potential).
FT   MOTIF        97     99       NPA 1.
FT   MOTIF       213    215       NPA 2.
FT   MOD_RES     111    111       Phosphoserine; by PKG (By similarity).
FT   MOD_RES     180    180       Phosphoserine; by PKC (By similarity).
FT   MOD_RES     285    285       Phosphoserine (By similarity).
FT   MOD_RES     321    321       Phosphoserine (By similarity).
FT   CARBOHYD    153    153       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    206    206       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1     22       Missing (in isoform 1).
FT                                /FTId=VSP_003233.
FT   VAR_SEQ       1     11       MSDGAAARRWG -> MVHGFGCFVFFFLISLSSLWASEDST
FT                                CNSTLPLCHLATTLDCC (in isoform 3).
FT                                /FTId=VSP_003234.
FT   VARIANT       4      4       G -> R.
FT   CONFLICT     37     37       A -> S (in Ref. 1; AAB41571).
FT   CONFLICT     51     51       Missing (in Ref. 1; AAB41569/AAB41570).
FT   CONFLICT     88     88       F -> L (in Ref. 1; AAB41569/AAB41570).
FT   CONFLICT    174    174       I -> V (in Ref. 1; AAB41569/AAB41570).
FT   CONFLICT    313    313       K -> R (in Ref. 1; AAB41569/AAB41570).
SQ   SEQUENCE   323 AA;  34436 MW;  9AC638A3C3F412E2 CRC64;
     MSDGAAARRW GKCGHSCSRE SIMVAFKGVW TQAFWKAVSA EFLATLIFVL LGVGSTINWG
     GSENPLPVDM VLISLCFGLS IATMVQCFGH ISGGHINPAV TVAMVCTRKI SIAKSVFYII
     AQCLGAIIGA GILYLVTPPS VVGGLGVTTV HGNLTAGHGL LVELIITFQL VFTIFASCDS
     KRTDVTGSIA LAIGFSVAIG HLFAINYTGA SMNPARSFGP AVIMGNWANH WIYWVGPIMG
     AVLAGALYEY VFCPDVELKR RLKEAFSKAA QQTKGSYMEV EDNRSQVETE DLILKPGVVH
     VIDIDRGEEK KGKDSSGEVL SSV
//
ID   TYRO3_MOUSE             Reviewed;         880 AA.
AC   P55144; O09070; O09080; P70285; Q60752; Q62482; Q62483; Q62484;
AC   Q78E85; Q78E87;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAR-2011, entry version 108.
DE   RecName: Full=Tyrosine-protein kinase receptor TYRO3;
DE            EC=2.7.10.1;
DE   AltName: Full=Etk2/tyro3;
DE   AltName: Full=TK19-2;
DE   AltName: Full=Tyrosine-protein kinase DTK;
DE   AltName: Full=Tyrosine-protein kinase RSE;
DE   Flags: Precursor;
GN   Name=Tyro3; Synonyms=Dtk, Rse;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=94193774; PubMed=7511603;
RA   Mark M.R., Scadden D.T., Wang Z., Gu Q., Goddard A., Godowski P.J.;
RT   "RSE, a novel receptor-type tyrosine kinase with homology to Axl/Ufo,
RT   is expressed at high levels in the brain.";
RL   J. Biol. Chem. 269:10720-10728(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=95161079; PubMed=7857657;
RA   Crosier P.S., Lewis P.M., Hall L.R., Vitas M.R., Morris C.M.,
RA   Beier D.R., Wood C.R., Crosier K.E.;
RT   "Isolation of a receptor tyrosine kinase (DTK) from embryonic stem
RT   cells: structure, genetic mapping and analysis of expression.";
RL   Growth Factors 11:125-136(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6;
RX   MEDLINE=94336210; PubMed=8058320;
RA   Lai C., Gore M., Lemke G.;
RT   "Structure, expression, and activity of Tyro 3, a neural adhesion-
RT   related receptor tyrosine kinase.";
RL   Oncogene 9:2567-2578(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Brain, and Liver;
RX   MEDLINE=94150990; PubMed=8108111;
RA   Fujimoto J., Yamamoto T.;
RT   "brt, a mouse gene encoding a novel receptor-type protein-tyrosine
RT   kinase, is preferentially expressed in the brain.";
RL   Oncogene 9:693-698(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=94150991; PubMed=8108112;
RA   Ohashi K., Mizuno K., Kuma K., Miyata T., Nakamura T.;
RT   "Cloning of the cDNA for a novel receptor tyrosine kinase, Sky,
RT   predominantly expressed in brain.";
RL   Oncogene 9:699-705(1994).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=95240399; PubMed=7723626; DOI=10.1016/0169-328X(94)00216-2;
RA   Schulz N., Paulhiac C., Lee L., Zhou R.;
RT   "Isolation and expression analysis of tyro3, a murine growth factor
RT   receptor tyrosine kinase preferentially expressed in adult brain.";
RL   Brain Res. Mol. Brain Res. 28:273-280(1995).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=97044738; PubMed=8889809;
RA   Sasaki M., Enami J.;
RT   "Structure and expression of a murine homologue of sky receptor
RT   tyrosine kinase.";
RL   J. Biochem. 120:264-270(1996).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-92 (ISOFORMS 1; 2 AND 3).
RC   STRAIN=129/Sv; TISSUE=Liver;
RX   PubMed=7784069;
RA   Biesecker L.G., Giannola D.M., Emerson S.G.;
RT   "Identification of alternative exons, including a novel exon, in the
RT   tyrosine kinase receptor gene Etk2/tyro3 that explain differences in
RT   5' cDNA sequences.";
RL   Oncogene 10:2239-2242(1995).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-675, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [10]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-181, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: May be involved in cell adhesion processes, particularly
CC       in the central nervous system.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBUNIT: Monomer and homodimer. Interacts with GAS6 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=3; Synonyms=III;
CC         IsoId=P55144-1; Sequence=Displayed;
CC       Name=2; Synonyms=II;
CC         IsoId=P55144-2; Sequence=VSP_012549;
CC       Name=1; Synonyms=I, B;
CC         IsoId=P55144-3; Sequence=VSP_012548;
CC   -!- TISSUE SPECIFICITY: Abundant in the brain and lower levels in
CC       other tissues.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. AXL/UFO subfamily.
CC   -!- SIMILARITY: Contains 2 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 2 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB26942.1; Type=Erroneous initiation;
CC       Sequence=CAA54995.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; U05683; AAA19237.1; -; mRNA.
DR   EMBL; U18933; AAC52148.1; -; mRNA.
DR   EMBL; X78103; CAA54995.1; ALT_INIT; mRNA.
DR   EMBL; U18342; AAB26942.1; ALT_INIT; mRNA.
DR   EMBL; U18343; AAB26943.1; -; mRNA.
DR   EMBL; AB000826; BAA19191.1; -; Genomic_DNA.
DR   EMBL; AB000827; BAA19192.1; -; mRNA.
DR   EMBL; AB000828; BAA19193.1; -; mRNA.
DR   EMBL; U23721; AAC52215.1; -; Genomic_DNA.
DR   EMBL; U23718; AAC52215.1; JOINED; Genomic_DNA.
DR   EMBL; U23721; AAC52216.1; -; Genomic_DNA.
DR   EMBL; U23719; AAC52216.1; JOINED; Genomic_DNA.
DR   EMBL; U23721; AAC52217.1; -; Genomic_DNA.
DR   EMBL; U23720; AAC52217.1; JOINED; Genomic_DNA.
DR   IPI; IPI00126146; -.
DR   IPI; IPI00136714; -.
DR   IPI; IPI00421186; -.
DR   PIR; B53743; B53743.
DR   PIR; I48862; I48862.
DR   PIR; I49152; I49152.
DR   UniGene; Mm.2901; -.
DR   UniGene; Mm.424496; -.
DR   ProteinModelPortal; P55144; -.
DR   SMR; P55144; 37-400, 497-785.
DR   STRING; P55144; -.
DR   PhosphoSite; P55144; -.
DR   PRIDE; P55144; -.
DR   Ensembl; ENSMUST00000028763; ENSMUSP00000028763; ENSMUSG00000027298.
DR   Ensembl; ENSMUST00000110781; ENSMUSP00000106408; ENSMUSG00000027298.
DR   Ensembl; ENSMUST00000110786; ENSMUSP00000106413; ENSMUSG00000027298.
DR   UCSC; uc008lup.1; mouse.
DR   MGI; MGI:104294; Tyro3.
DR   GeneTree; ENSGT00550000074361; -.
DR   HOVERGEN; HBG006346; -.
DR   BRENDA; 2.7.10.1; 244.
DR   NextBio; 461905; -.
DR   ArrayExpress; P55144; -.
DR   Bgee; P55144; -.
DR   CleanEx; MM_TYRO3; -.
DR   Genevestigator; P55144; -.
DR   GermOnline; ENSMUSG00000027298; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:EC.
DR   GO; GO:0043277; P:apoptotic cell clearance; IGI:MGI.
DR   GO; GO:0021885; P:forebrain cell migration; IGI:MGI.
DR   GO; GO:0001779; P:natural killer cell differentiation; IGI:MGI.
DR   GO; GO:0051250; P:negative regulation of lymphocyte activation; IGI:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptosis; IGI:MGI.
DR   GO; GO:0042698; P:ovulation cycle; IGI:MGI.
DR   GO; GO:0030168; P:platelet activation; IMP:MGI.
DR   GO; GO:0043491; P:protein kinase B signaling cascade; IGI:MGI.
DR   GO; GO:0032940; P:secretion by cell; IMP:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IGI:MGI.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:MGI.
DR   GO; GO:0060068; P:vagina development; IGI:MGI.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 4.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; FN_III-like; 2.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell adhesion; Cell membrane;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Receptor; Repeat; Signal;
KW   Transferase; Transmembrane; Transmembrane helix;
KW   Tyrosine-protein kinase.
FT   SIGNAL        1     30       Potential.
FT   CHAIN        31    880       Tyrosine-protein kinase receptor TYRO3.
FT                                /FTId=PRO_0000024479.
FT   TOPO_DOM     31    419       Extracellular (Potential).
FT   TRANSMEM    420    440       Helical; (Potential).
FT   TOPO_DOM    441    880       Cytoplasmic (Potential).
FT   DOMAIN       31    118       Ig-like C2-type 1.
FT   DOMAIN      129    209       Ig-like C2-type 2.
FT   DOMAIN      214    307       Fibronectin type-III 1.
FT   DOMAIN      312    403       Fibronectin type-III 2.
FT   DOMAIN      508    785       Protein kinase.
FT   NP_BIND     514    522       ATP (By similarity).
FT   ACT_SITE    645    645       Proton acceptor (By similarity).
FT   BINDING     540    540       ATP (By similarity).
FT   MOD_RES     675    675       Phosphotyrosine.
FT   MOD_RES     676    676       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   CARBOHYD     53     53       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     75     75       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    181    181       N-linked (GlcNAc...).
FT   CARBOHYD    220    220       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    230    230       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    283    283       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    356    356       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    370    370       N-linked (GlcNAc...) (Potential).
FT   DISULFID     54    107       By similarity.
FT   DISULFID    150    193       By similarity.
FT   VAR_SEQ       1     31       MALRRSMGWPGLRPLLLAGLASLLLPGSAAA -> MDDKLE
FT                                NTLGRWAGENGLSIGEYLAIK (in isoform 1).
FT                                /FTId=VSP_012548.
FT   VAR_SEQ       1     31       MALRRSMGWPGLRPLLLAGLASLLLPGSAAA -> MGCPAG
FT                                DWKVFGEGGAWPGACPGSEAGPPQRQRSGQGAGPAAPSG
FT                                (in isoform 2).
FT                                /FTId=VSP_012549.
FT   CONFLICT    630    630       A -> R (in Ref. 3).
FT   CONFLICT    811    811       L -> V (in Ref. 3).
SQ   SEQUENCE   880 AA;  96222 MW;  3B7AC36CB016B3F7 CRC64;
     MALRRSMGWP GLRPLLLAGL ASLLLPGSAA AGLKLMGAPV KMTVSQGQPV KLNCSVEGME
     DPDIHWMKDG TVVQNASQVS ISISEHSWIG LLSLKSVERS DAGLYWCQVK DGEETKISQS
     VWLTVEGVPF FTVEPKDLAV PPNAPFQLSC EAVGPPEPVT IYWWRGLTKV GGPAPSPSVL
     NVTGVTQRTE FSCEARNIKG LATSRPAIVR LQAPPAAPFN TTVTTISSYN ASVAWVPGAD
     GLALLHSCTV QVAHAPGEWE ALAVVVPVPP FTCLLRNLAP ATNYSLRVRC ANALGPSPYG
     DWVPFQTKGL APARAPQNFH AIRTDSGLIL EWEEVIPEDP GEGPLGPYKL SWVQENGTQD
     ELMVEGTRAN LTDWDPQKDL ILRVCASNAI GDGPWSQPLV VSSHDHAGRQ GPPHSRTSWV
     PVVLGVLTAL ITAAALALIL LRKRRKETRF GQAFDSVMAR GEPAVHFRAA RSFNRERPER
     IEATLDSLGI SDELKEKLED VLIPEQQFTL GRMLGKGEFG SVREAQLKQE DGSFVKVAVK
     MLKADIIASS DIEEFLREAA CMKEFDHPHV AKLVGVSLRS RAKGRLPIPM VILPFMKHGD
     LHAFLLASRI GENPFNLPLQ TLVRFMVDIA CGMEYLSSRN FIHRDLAARN CMLAEDMTVC
     VADFGLSRKI YSGDYYRQGC ASKLPVKWLA LESLADNLYT VHSDVWAFGV TMWEIMTRGQ
     TPYAGIENAE IYNYLIGGNR LKQPPECMEE VYDLMYQCWS ADPKQRPSFT CLRMELENIL
     GHLSVLSTSQ DPLYINIERA EQPTESGSPE LHCGERSSSE AGDGSGVGAV GGIPSDSRYI
     FSPGGLSESP GQLEQQPESP LNENQRLLLL QQGLLPHSSC
//
ID   3BP1_MOUSE              Reviewed;         601 AA.
AC   P55194; Q99KK8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-FEB-2011, entry version 93.
DE   RecName: Full=SH3 domain-binding protein 1;
DE            Short=3BP-1;
GN   Name=Sh3bp1; Synonyms=3bp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=95347339; PubMed=7621827;
RA   Cicchetti P., Ridley A.J., Zheng Y., Cerione R.A., Baltimore D.;
RT   "3BP-1, an SH3 domain binding protein, has GAP activity for Rac and
RT   inhibits growth factor-induced membrane ruffling in fibroblasts.";
RL   EMBO J. 14:3127-3135(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 263-601.
RX   MEDLINE=92358242; PubMed=1379745; DOI=10.1126/science.1379745;
RA   Cicchetti P., Mayer B.J., Thiel G., Baltimore D.;
RT   "Identification of a protein that binds to the SH3 region of Abl and
RT   is similar to Bcr and GAP-rho.";
RL   Science 257:803-806(1992).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 528-537.
RX   MEDLINE=93174278; PubMed=8438166; DOI=10.1126/science.8438166;
RA   Ren R., Mayer B.J., Cicchetti P., Baltimore D.;
RT   "Identification of a ten-amino acid proline-rich SH3 binding site.";
RL   Science 259:1157-1161(1993).
CC   -!- FUNCTION: Binds differentially to the SH3 domains of certain
CC       proteins of signal transduction pathways. This protein binds
CC       preferentially to the ABL1 proto-oncogene, SRC and GRB2. Shows GAP
CC       activity for Rac-related proteins but not for Rho- or Ras-related
CC       proteins. It inhibits PDGF-induced membrane ruffling mediated by
CC       Rac.
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined. Highest
CC       levels found in spleen and brain, lowest in heart and liver.
CC   -!- SIMILARITY: Contains 1 BAR domain.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
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DR   EMBL; X87671; CAA61011.1; -; mRNA.
DR   EMBL; BC004598; AAH04598.1; -; mRNA.
DR   IPI; IPI00136897; -.
DR   PIR; S56144; S56144.
DR   UniGene; Mm.4462; -.
DR   PDB; 1ABO; X-ray; 2.00 A; C/D=528-537.
DR   PDBsum; 1ABO; -.
DR   ProteinModelPortal; P55194; -.
DR   SMR; P55194; 192-392.
DR   STRING; P55194; -.
DR   PhosphoSite; P55194; -.
DR   PRIDE; P55194; -.
DR   Ensembl; ENSMUST00000109695; ENSMUSP00000105317; ENSMUSG00000022436.
DR   UCSC; uc007wrr.1; mouse.
DR   MGI; MGI:104603; Sh3bp1.
DR   GeneTree; ENSGT00600000084016; -.
DR   HOVERGEN; HBG000015; -.
DR   ArrayExpress; P55194; -.
DR   Bgee; P55194; -.
DR   CleanEx; MM_SH3BP1; -.
DR   Genevestigator; P55194; -.
DR   GermOnline; ENSMUSG00000022436; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0017124; F:SH3 domain binding; IPI:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR004148; BAR.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF03114; BAR; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS51021; BAR; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; GTPase activation; Phosphoprotein; SH3-binding.
FT   CHAIN         1    601       SH3 domain-binding protein 1.
FT                                /FTId=PRO_0000056724.
FT   DOMAIN        1    182       BAR.
FT   DOMAIN      196    390       Rho-GAP.
FT   MOTIF       529    537       SH3-binding.
FT   MOD_RES     456    456       Phosphoserine (By similarity).
FT   MOD_RES     553    553       Phosphoserine.
FT   CONFLICT     46     48       RSG -> PLS (in Ref. 2; AAH04598).
FT   CONFLICT    229    229       Missing (in Ref. 2; AAH04598).
FT   CONFLICT    261    261       G -> D (in Ref. 2; AAH04598).
FT   CONFLICT    592    593       PA -> RP (in Ref. 2; AAH04598).
SQ   SEQUENCE   601 AA;  65260 MW;  0FBBF357EEB02ECE CRC64;
     MAESFKELDP DSSMGKALEM TCAIQNQLAR ILAEFEMTLE RDVLQRSGRL SEEELPAILK
     HKKSLQKLVS DWNTLKSRLS QAAKNSGSNQ GLGGASGSHT HTTTANKVEM LKEEEEELKK
     KVEQCKDEYL ADLYHFSTKE DSYANYFIHL LEIQADYHRK SLTSLDTALA ELRDNHNQAD
     HSPLTTAAPF SRVYGVSLRT HLQDLGRDIA LPIEACVLLL LSEGMQEEEG LFRLAAGASV
     LKRLKQTMAS DPHSLEEFCS GPHAVAGALK SYLRELPEPL MTSDLYDDWM RAASLKEPGA
     RLEALHDVCS RLPQENFNNL RYLMKFLALL AEEQDVNKMT PSNIAIVLGP NLLWPPEKEG
     DQAQLDAASV SSIQVVGVVE ALIQNADTLF PGDINFNVSG IFPGLAPQEK VSSQQVSEEL
     PPVTVPAPAT TPAPTLAPAS MAVRERTEAD LPKPTSPKVS RNPTETAASA EDMTRKTKRP
     APARPTMPPP QPSSTRSSPP APSLPPGSVS PGTPQALPRR LVGTSLRAPT MPPPLPPVPP
     QPARRQSRRL PASPVISNMP AQVDQGVATE DREGPEAVGG HPPPPALPPQ PPARGLISET
     E
//
ID   MLL1_MOUSE              Reviewed;        3966 AA.
AC   P55200; Q3UEU1; Q3USE7;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 102.
DE   RecName: Full=Histone-lysine N-methyltransferase MLL;
DE            EC=2.1.1.43;
DE   AltName: Full=ALL-1;
DE   AltName: Full=Zinc finger protein HRX;
DE   Contains:
DE     RecName: Full=MLL cleavage product N320;
DE     AltName: Full=N-terminal cleavage product of 320 kDa;
DE              Short=p320;
DE   Contains:
DE     RecName: Full=MLL cleavage product C180;
DE     AltName: Full=C-terminal cleavage product of 180 kDa;
DE              Short=p180;
GN   Name=Mll; Synonyms=All1, Hrx, Mll1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 101-3966 (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6 X CBA, and C57BL/6J; TISSUE=Lung, and Spleen;
RX   MEDLINE=93317679; PubMed=8327517; DOI=10.1073/pnas.90.13.6350;
RA   Ma Q., Alder H., Nelson K.K., Chatterjee D., Gu Y., Nakamura T.,
RA   Canaani E., Croce C.M., Siracusa L.D., Buchberg A.M.;
RT   "Analysis of the murine All-1 gene reveals conserved domains with
RT   human ALL-1 and identifies a motif shared with DNA
RT   methyltransferases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:6350-6354(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 372-1517 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Histone methyltransferase that plays an essential role
CC       in early development and hematopoiesis. Catalytic subunit of the
CC       MLL1/MLL complex, a multiprotein complex that mediates both
CC       methylation of 'Lys-4' of histone H3 (H3K4me) complex and
CC       acetylation of 'Lys-16' of histone H4 (H4K16ac). In the MLL1/MLL
CC       complex, it specifically mediates H3K4me, a specific tag for
CC       epigenetic transcriptional activation. Has weak methyltransferase
CC       activity by itself, and requires other component of the MLL1/MLL
CC       complex to obtain full methyltransferase activity. Has no activity
CC       toward histone H3 phosphorylated on 'Thr-3', less activity toward
CC       H3 dimethylated on 'Arg-8' or 'Lys-9', while it has higher
CC       activity toward H3 acetylated on 'Lys-9'. Required for
CC       transcriptional activation of HOXA9. Promotes PPP1R15A-induced
CC       apoptosis (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC   -!- SUBUNIT: MLL cleavage product N320 heterodimerizes with MLL
CC       cleavage product C180 (via SET and FYRC domains). Component of
CC       some MLL1/MLL complex, at least composed of the core components
CC       MLL, ASH2L, HCFC1/HCF1, HCFC2, WDR5, DPY30 and RBBP5, as well as
CC       the facultative components C17orf49, CHD8, E2F6, HSP70, IN80C,
CC       KIAA1267, LAS1L, MAX, MCRS1, MEN1, MGA, MYST1/MOF, PELP1, PHF20,
CC       PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6,
CC       TAF7, TAF9 and TEX10. Interacts with WDR5; the interaction is
CC       direct. Interacts with MYST1/MOF; the interaction is direct.
CC       Interacts with SBF1 and PPP1R15A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SUBCELLULAR LOCATION: MLL cleavage product N320: Nucleus (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: MLL cleavage product C180: Nucleus (By
CC       similarity). Note=Localizes to a diffuse nuclear pattern when not
CC       associated with MLL cleavage product N320.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P55200-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P55200-2; Sequence=VSP_006667;
CC   -!- DOMAIN: The SET domain structure is atypical and is not in an
CC       optimal position to have methyltransferase activity. It requires
CC       other components of the MLL1/MLL complex, such as ASH2L or RBBP5,
CC       to order the active site and obtain optimal histone
CC       methyltransferase activity (By similarity).
CC   -!- DOMAIN: The CXXC-type zinc finger binds bind to nonmethyl-CpG
CC       dinucleotides (By similarity).
CC   -!- PTM: Proteolytic cleavage by TASP1 generates MLL cleavage product
CC       N320 and MLL cleavage product C180, which reassemble through a
CC       non-covalent association. 2 cleavage sites exist, cleavage site 1
CC       (CS1) and cleavage site 2 (CS2), to generate MLL cleavage products
CC       N320 and C180. CS2 is the major site (By similarity).
CC   -!- SIMILARITY: Belongs to the histone-lysine methyltransferase
CC       family. TRX/MLL subfamily.
CC   -!- SIMILARITY: Contains 3 A.T hook DNA-binding domains.
CC   -!- SIMILARITY: Contains 1 bromo domain.
CC   -!- SIMILARITY: Contains 1 CXXC-type zinc finger.
CC   -!- SIMILARITY: Contains 1 FY-rich C-terminal domain.
CC   -!- SIMILARITY: Contains 1 FY-rich N-terminal domain.
CC   -!- SIMILARITY: Contains 3 PHD-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 post-SET domain.
CC   -!- SIMILARITY: Contains 1 SET domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE24386.1; Type=Erroneous initiation;
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DR   EMBL; AC061963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC142113; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L17069; AAA62593.1; -; mRNA.
DR   EMBL; AK140439; BAE24386.1; ALT_INIT; mRNA.
DR   EMBL; AK149341; BAE28820.1; -; mRNA.
DR   IPI; IPI00230024; -.
DR   IPI; IPI00315032; -.
DR   UniGene; Mm.2389; -.
DR   ProteinModelPortal; P55200; -.
DR   SMR; P55200; 1143-1211, 1428-1537, 1565-1781, 2021-2076, 2836-2865, 3664-3746, 3787-3966.
DR   STRING; P55200; -.
DR   PhosphoSite; P55200; -.
DR   PRIDE; P55200; -.
DR   Ensembl; ENSMUST00000002095; ENSMUSP00000002095; ENSMUSG00000002028.
DR   Ensembl; ENSMUST00000114689; ENSMUSP00000110337; ENSMUSG00000002028.
DR   UCSC; uc009pep.1; mouse.
DR   UCSC; uc009peq.1; mouse.
DR   MGI; MGI:96995; Mll1.
DR   eggNOG; roNOG12785; -.
DR   HOGENOM; HBG444296; -.
DR   HOVERGEN; HBG051927; -.
DR   InParanoid; P55200; -.
DR   OrthoDB; EOG47H5P3; -.
DR   ArrayExpress; P55200; -.
DR   Bgee; P55200; -.
DR   CleanEx; MM_MLL1; -.
DR   Genevestigator; P55200; -.
DR   GermOnline; ENSMUSG00000002028; Mus musculus.
DR   GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0070577; F:histone acetyl-lysine binding; ISS:UniProtKB.
DR   GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); ISS:UniProtKB.
DR   GO; GO:0045322; F:unmethylated CpG binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0009952; P:anterior/posterior pattern formation; IMP:MGI.
DR   GO; GO:0006306; P:DNA methylation; IMP:MGI.
DR   GO; GO:0035162; P:embryonic hemopoiesis; IMP:MGI.
DR   GO; GO:0043984; P:histone H4-K16 acetylation; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
DR   GO; GO:0051569; P:regulation of histone H3-K4 methylation; IMP:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR003889; FYrich_C.
DR   InterPro; IPR018516; FYrich_C_sg.
DR   InterPro; IPR003888; FYrich_N.
DR   InterPro; IPR018518; FYrich_N_sg.
DR   InterPro; IPR016569; MeTrfase_trithorax.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR002857; Znf_CXXC.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 2.
DR   Pfam; PF05965; FYRC; 1.
DR   Pfam; PF05964; FYRN; 1.
DR   Pfam; PF00628; PHD; 2.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF02008; zf-CXXC; 1.
DR   PIRSF; PIRSF010354; Methyltransferase_trithorax; 1.
DR   SMART; SM00384; AT_hook; 3.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00542; FYRC; 1.
DR   SMART; SM00541; FYRN; 1.
DR   SMART; SM00249; PHD; 4.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 2.
DR   PROSITE; PS00633; BROMODOMAIN_1; FALSE_NEG.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS51058; ZF_CXXC; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 3.
DR   PROSITE; PS50016; ZF_PHD_2; 3.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Bromodomain; Chromatin regulator;
KW   DNA-binding; Isopeptide bond; Metal-binding; Methyltransferase;
KW   Nucleus; Phosphoprotein; Polymorphism; Repeat;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1   3966       Histone-lysine N-methyltransferase MLL.
FT                                /FTId=PRO_0000124877.
FT   CHAIN         1   2714       MLL cleavage product N320 (By
FT                                similarity).
FT                                /FTId=PRO_0000390951.
FT   CHAIN      2715   3966       MLL cleavage product C180 (By
FT                                similarity).
FT                                /FTId=PRO_0000390952.
FT   DOMAIN     1705   1750       Bromo; divergent.
FT   DOMAIN     2025   2075       FY-rich N-terminal.
FT   DOMAIN     3663   3746       FY-rich C-terminal.
FT   DOMAIN     3825   3946       SET.
FT   DOMAIN     3950   3966       Post-SET.
FT   DNA_BIND    167    178       A.T hook 1.
FT   DNA_BIND    215    225       A.T hook 2.
FT   DNA_BIND    299    307       A.T hook 3.
FT   ZN_FING    1144   1192       CXXC-type.
FT   ZN_FING    1430   1481       PHD-type 1.
FT   ZN_FING    1478   1532       PHD-type 2.
FT   ZN_FING    1565   1629       PHD-type 3.
FT   REGION     3903   3904       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   COMPBIAS     14    150       Gly-rich.
FT   COMPBIAS     17    100       Ala/Gly/Ser-rich.
FT   COMPBIAS     80     99       Ser-rich.
FT   COMPBIAS    135    141       Poly-Gly.
FT   COMPBIAS    199    287       Lys-rich.
FT   COMPBIAS    443    491       Ser-rich.
FT   COMPBIAS    559    601       Pro-rich.
FT   COMPBIAS    559    562       Poly-Pro.
FT   COMPBIAS    566    569       Poly-Pro.
FT   COMPBIAS    703    807       Ser-rich.
FT   COMPBIAS   1234   1366       Pro-rich.
FT   COMPBIAS   1819   1867       Pro-rich.
FT   COMPBIAS   2185   2320       Ser-rich.
FT   METAL      3906   3906       Zinc (By similarity).
FT   METAL      3954   3954       Zinc (By similarity).
FT   METAL      3956   3956       Zinc (By similarity).
FT   METAL      3961   3961       Zinc (By similarity).
FT   BINDING    3836   3836       S-adenosyl-L-methionine (By similarity).
FT   BINDING    3838   3838       S-adenosyl-L-methionine (By similarity).
FT   BINDING    3880   3880       S-adenosyl-L-methionine (By similarity).
FT   BINDING    3955   3955       S-adenosyl-L-methionine (By similarity).
FT   SITE       2662   2663       Cleavage; by TASP1, site 1 (By
FT                                similarity).
FT   SITE       2714   2715       Cleavage; by TASP1, site 2 (By
FT                                similarity).
FT   SITE       3762   3762       Important for WDR5-recognition and
FT                                binding (By similarity).
FT   MOD_RES     134    134       Phosphoserine (By similarity).
FT   MOD_RES     151    151       Phosphoserine (By similarity).
FT   MOD_RES     195    195       Phosphoserine (By similarity).
FT   MOD_RES     200    200       Phosphoserine (By similarity).
FT   MOD_RES     277    277       Phosphoserine (By similarity).
FT   MOD_RES     335    335       Phosphothreonine (By similarity).
FT   MOD_RES     504    504       Phosphothreonine (By similarity).
FT   MOD_RES     516    516       Phosphoserine (By similarity).
FT   MOD_RES     634    634       N6-acetyllysine (By similarity).
FT   MOD_RES     678    678       Phosphoserine (By similarity).
FT   MOD_RES     829    829       Phosphoserine (By similarity).
FT   MOD_RES     837    837       Phosphothreonine (By similarity).
FT   MOD_RES     923    923       Phosphoserine (By similarity).
FT   MOD_RES    1053   1053       Phosphoserine (By similarity).
FT   MOD_RES    1127   1127       N6-acetyllysine (By similarity).
FT   MOD_RES    1232   1232       N6-acetyllysine (By similarity).
FT   MOD_RES    1839   1839       Phosphoserine (By similarity).
FT   MOD_RES    1841   1841       Phosphothreonine (By similarity).
FT   MOD_RES    1847   1847       Phosphothreonine (By similarity).
FT   MOD_RES    1860   1860       Phosphoserine (By similarity).
FT   MOD_RES    2100   2100       Phosphoserine (By similarity).
FT   MOD_RES    2148   2148       Phosphothreonine (By similarity).
FT   MOD_RES    2152   2152       Phosphoserine (By similarity).
FT   MOD_RES    2154   2154       Phosphothreonine (By similarity).
FT   MOD_RES    2200   2200       Phosphoserine (By similarity).
FT   MOD_RES    2202   2202       Phosphoserine (By similarity).
FT   MOD_RES    2386   2386       Phosphoserine (By similarity).
FT   MOD_RES    2521   2521       Phosphothreonine (By similarity).
FT   MOD_RES    2687   2687       Phosphoserine (By similarity).
FT   MOD_RES    2720   2720       Phosphothreonine (By similarity).
FT   MOD_RES    2722   2722       Phosphoserine (By similarity).
FT   MOD_RES    2725   2725       Phosphoserine (By similarity).
FT   MOD_RES    2862   2862       Phosphoserine (By similarity).
FT   MOD_RES    2936   2936       Phosphothreonine (By similarity).
FT   MOD_RES    2951   2951       Phosphoserine (By similarity).
FT   MOD_RES    3032   3032       Phosphoserine (By similarity).
FT   MOD_RES    3369   3369       Phosphothreonine (By similarity).
FT   MOD_RES    3510   3510       Phosphoserine (By similarity).
FT   MOD_RES    3513   3513       Phosphoserine (By similarity).
FT   MOD_RES    3514   3514       Phosphoserine (By similarity).
FT   MOD_RES    3521   3521       Phosphoserine (By similarity).
FT   CROSSLNK    214    214       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK    218    218       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK    219    219       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   VAR_SEQ    1603   1605       Missing (in isoform 2).
FT                                /FTId=VSP_006667.
FT   VARIANT    1597   1597       K -> T.
FT   CONFLICT    372    372       Q -> E (in Ref. 3; BAE28820).
FT   CONFLICT    554    554       Q -> K (in Ref. 2; AAA62593).
FT   CONFLICT    564    564       L -> F (in Ref. 2; AAA62593).
FT   CONFLICT    797    797       P -> S (in Ref. 3; BAE28820).
FT   CONFLICT    806    806       E -> D (in Ref. 2; AAA62593 and 3;
FT                                BAE28820).
FT   CONFLICT    821    821       L -> P (in Ref. 2; AAA62593 and 3;
FT                                BAE28820).
FT   CONFLICT   1069   1069       C -> Y (in Ref. 2; AAA62593).
FT   CONFLICT   1230   1230       A -> S (in Ref. 2; AAA62593).
FT   CONFLICT   1349   1349       R -> L (in Ref. 2; AAA62593).
FT   CONFLICT   1437   1437       A -> S (in Ref. 2; AAA62593).
FT   CONFLICT   1440   1440       G -> E (in Ref. 2; AAA62593).
FT   CONFLICT   1632   1632       A -> P (in Ref. 2; AAA62593).
FT   CONFLICT   2292   2292       S -> L (in Ref. 2; AAA62593).
FT   CONFLICT   3481   3481       N -> I (in Ref. 2; AAA62593).
FT   CONFLICT   3493   3493       R -> S (in Ref. 2; AAA62593).
FT   CONFLICT   3548   3548       G -> V (in Ref. 2; AAA62593).
SQ   SEQUENCE   3966 AA;  429649 MW;  E22AE6367B5032AC CRC64;
     MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPQAGGGG PGAPPSPPAV
     AAAAAGSSGA GVPGGAAAAS AASSSSASSS SSSSSSASSG PALLRVGPGF DAALQVSAAI
     GTNLRRFRAV FGESGGGGGS GEDEQFLGFG SDEEVRVRSP TRSPSVKASP RKPRGRPRSG
     SDRNPAILSD PSVFSPLNKS ETKSADKIKK KDSKSIEKKR GRPPTFPGVK IKITHGKDIA
     ELTQGSKEDS LKKVKRTPSA MFQQATKIKK LRAGKLSPLK SKFKTGKLQI GRKGVQIVRR
     RGRPPSTERI KTPSGLLINS ELEKPQKVRK DKEGTPPLTK EDKTVVRQSP RRIKPVRIIP
     SCKRTDATIA KQLLQRAKKG AQKKIEKEAA QLQGRKVKTQ VKNIRQFIMP VVSAISSRII
     KTPRRFIEDE DYDPPMKIAR LESTPNSRFS ATSCGSSEKS SAASQHSSQM SSDSSRSSSP
     SIDTTSDSQA SEEIQALPEE RSNTPEVHTP LPISQSPENE SNDRRSRRYS MSERSFGSRA
     TKKLPTLQSA PQQQTSSSPP PPLLTPPPPL QPASGISDHT PWLMPPTIPL ASPFLPASAA
     PMQGKRKSIL REPTFRWTSL KHSRSEPQYF SSAKYAKEGL IRKPIFDNFR PPPLTPEDVG
     FASGFSASGT AASARLFSPL HSGTRFDIHK RSPILRAPRF TPSEAHSRIF ESVTLPSNRT
     SSGASSSGVS NRKRKRKVFS PIRSEPRSPS HSMRTRSGRL STSELSPLTP PSSVSSSLSI
     PVSPLAASAL NPTFTFPSHS LTQSGESTEK NQRARKQTSA LAEPFSSNSP ALFPWFTPGS
     QTEKGRKKDT APEELSKDRD ADKSVEKDKS RERDREREKE NKRESRKEKR KKGSDIQSSS
     ALYPVGRVSK EKVAGEDVGT SSSAKKATGR KKSSSLDSGA DVAPVTLGDT TAVKAKILIK
     KGRGNLEKNN LDLGPAAPSL EKERTPCLSA PSSSTVKHST SSIGSMLAQA DKLPMTDKRV
     ASLLKKAKAQ LCKIEKSKSL KQTDQPKAQG QESDSSETSV RGPRIKHVCR RAAVALGRKR
     AVFPDDMPTL SALPWEEREK ILSSMGNDDK SSVAGSEDAE PLAPPIKPIK PVTRNKAPQE
     PPVKKGRRSR RCGQCPGCQV PEDCGICTNC LDKPKFGGRN IKKQCCKMRK CQNLQWMPSK
     ASLQKQTKAV KKKEKKSKTT EKKESKESTA VKSPLEPAQK AAPPPREEPA PKKSSSEPPP
     RKPVEEKSEE GGAPAPAPAP EPKQVSAPAS RKSSKQVSQP AAVVPPQPPS TAPQKKEAPK
     AVPSEPKKKQ PPPPEPGPEQ SKQKKVAPRP SIPVKQKPKD KEKPPPVSKQ ENAGTLNILN
     PLSNGISSKQ KIPADGVHRI RVDFKEDCEA ENVWEMGGLG ILTSVPITPR VVCFLCASSG
     HVEFVYCQVC CEPFHKFCLE ENERPLEDQL ENWCCRRCKF CHVCGRQHQA TKQLLECNKC
     RNSYHPECLG PNYPTKPTKK KKVWICTKCV RCKSCGSTTP GKGWDAQWSH DFSLCHDCAK
     LFAKGNFCPL CDKCYDDDDY ESKMMQCGKC DRWVHSKCES LSGTEDEMYE ILSNLPESVA
     YTCVNCTERH PAEWRLALEK ELQASLKQVL TALLNSRTTS HLLRYRQAAK PPDLNPETEE
     SIPSRSSPEG PDPPVLTEVS KQDEQQPLDL EGVKKRMDQG SYVSVLEFSD DIVKIIQAAI
     NSDGGQPEIK KANSMVKSFF IRQMERVFPW FSVKKSRFWE PNKVSNNSGM LPNAVLPPSL
     DHNYAQWQER EESSHTEQPP LMKKIIPAPK PKGPGEPDSP TPLHPPTPPI LSTDRSREDS
     PELNPPPGID DNRQCALCLM YGDDSANDAG RLLYIGQNEW THVNCALWSA EVFEDDDGSL
     KNVHMAVIRG KQLRCEFCQK PGATVGCCLT SCTSNYHFMC SRAKNCVFLD DKKVYCQRHR
     DLIKGEVVPE NGFEVFRRVF VDFEGISLRR KFLNGLEPEN IHMMIGSMTI DCLGILNDLS
     DCEDKLFPIG YQCSRVYWST TDARKRCVYT CKIMECRPPV VEPDINSTVE HDDNRTIAHS
     PSSFIDASCK DSQSTAAILS PPSPDRPHSQ TSGSCYYHVI SKVPRIRTPS YSPTQRSPGC
     RPLPSAGSPT PTTHEIVTVG DPLLSSGLRS IGSRRHSTSS LSPLRSKLRI MSPVRTGSAY
     SRSSVSSVPS LGTATDPEAS AKASDRGGLL SSSANLGHSA PPSSSSQRTV GGSKTSHLDG
     SSPSEVKRCS ASDLVPKGSL VKGEKNRTSS SKSTDGSAHS TAYPGIPKLT PQVHNATPGE
     LNISKIGSFA EPSTVPFSSK DTVSYPQLHL RGQRSDRDQH MDPSQSVKPS PNEDGEIKTL
     KLPGMGHRPS ILHEHIGSSS RDRRQKGKKS SKETCKEKHS SKSYLEPGQV TTGEEGNLKP
     EFADEVLTPG FLGQRPCNNV SSEKIGDKVL PLSGVPKGQS TQVEGSSKEL QAPRKCSVKV
     TPLKMEGENQ SKNTQKESGP GSPAHIESVC PAEPVSASRS PGAGPGVQPS PNNTLSQDPQ
     SNNYQNLPEQ DRNLMIPDGP KPQEDGSFKR RYPRRSARAR SNMFFGLTPL YGVRSYGEED
     IPFYSNSTGK KRGKRSAEGQ VDGADDLSTS DEDDLYYYNF TRTVISSGGE ERLASHNLFR
     EEEQCDLPKI SQLDGVDDGT ESDTSVTATS RKSSQIPKRN GKENGTENLK IDRPEDAGEK
     EHVIKSAVGH KNEPKLDNCH SVSRVKAQGQ DSLEAQLSSL ESSRRVHTST PSDKNLLDTY
     NAELLKSDSD NNNSDDCGNI LPSDIMDFVL KNTPSMQALG ESPESSSSEL LTLGEGLGLD
     SNREKDIGLF EVFSQQLPAT EPVDSSVSSS ISAEEQFELP LELPSDLSVL TTRSPTVPSQ
     NPSRLAVISD SGEKRVTITE KSVASSEGDP ALLSPGVDPA PEGHMTPDHF IQGHMDADHI
     SSPPCGSVEQ GHGNSQDLTR NSGTPGLQVP VSPTVPVQNQ KYVPSSTDSP GPSQISNAAV
     QTTPPHLKPA TEKLIVVNQN MQPLYVLQTL PNGVTQKIQL TSPVSSTPSV METNTSVLGP
     MGSGLTLTTG LNPSLPPSPS LFPPASKGLL SVPHHQHLHS FPAAAQSSFP PNISSPPSGL
     LIGVQPPPDP QLLGSEANQR TDLTTTVATP SSGLKKRPIS RLHTRKNKKL APSSAPSNIA
     PSDVVSNMTL INFTPSQLSN HPSLLDLGSL NPSSHRTVPN IIKRSKSGIM YFEQAPLLPP
     QSVGGTAATA AGSSTISQDT SHLTSGPVSA LASGSSVLNV VSMQTTAAPT SSTSVPGHVT
     LANQRLLGTP DIGSISHLLI KASHQSLGIQ DQPVALPPSS GMFPQLGTSQ TPSAAAMTAA
     SSICVLPSSQ TAGMTAASPP GEAEEHYKLQ RGNQLLAGKT GTLTSQRDRD PDSAPGTQPS
     NFTQTAEAPN GVRLEQNKTL PSAKPASSAS PGSSPSSGQQ SGSSSVPGPT KPKPKAKRIQ
     LPLDKGSGKK HKVSHLRTSS EAHIPHRDTD PAPQPSVTRT PRANREQQDA AGVEQPSQKE
     CGQPAGPVAA LPEVQATQNP ANEQENAEPK AMEEEESGFS SPLMLWLQQE QKRKESITER
     KPKKGLVFEI SSDDGFQICA ESIEDAWKSL TDKVQEARSN ARLKQLSFAG VNGLRMLGIL
     HDAVVFLIEQ LAGAKHCRNY KFRFHKPEEA NEPPLNPHGS ARAEVHLRKS AFDMFNFLAS
     KHRQPPEYNP NDEEEEEVQL KSARRATSMD LPMPMRFRHL KKTSKEAVGV YRSPIHGRGL
     FCKRNIDAGE MVIEYAGNVI RSIQTDKREK YYDSKGIGCY MFRIDDSEVV DATMHGNAAR
     FINHSCEPNC YSRVINIDGQ KHIVIFAMRK IYRGEELTYD YKFPIEDASN KLPCNCGAKK
     CRKFLN
//
ID   RAB8A_MOUSE             Reviewed;         207 AA.
AC   P55258; Q8VCF6;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   08-MAR-2011, entry version 105.
DE   RecName: Full=Ras-related protein Rab-8A;
DE   AltName: Full=Oncogene c-mel;
GN   Name=Rab8a; Synonyms=Mel, Rab8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=91360267; PubMed=1886711;
RA   Nimmo E.R., Sanders P.G., Padua R.A., Hughes D., Williamson R.,
RA   Johnson K.J.;
RT   "The MEL gene: a new member of the RAB/YPT class of RAS-related
RT   genes.";
RL   Oncogene 6:1347-1351(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 11-21; 59-69 AND 139-153, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   INTERACTION WITH MAP4K2.
RC   STRAIN=BALB/c; TISSUE=Melanoma;
RX   MEDLINE=96209873; PubMed=8643544; DOI=10.1073/pnas.93.10.5151;
RA   Ren M., Zeng J., De Lemos-Chiarandini C., Rosenfeld M., Adesnik M.,
RA   Sabatini D.D.;
RT   "In its active form, the GTP-binding protein rab8 interacts with a
RT   stress-activated protein kinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:5151-5155(1996).
RN   [6]
RP   INTERACTION WITH SYTL4.
RX   MEDLINE=22590467; PubMed=12590134; DOI=10.1074/jbc.M213090200;
RA   Fukuda M.;
RT   "Slp4-a/granuphilin-a inhibits dense-core vesicle exocytosis through
RT   interaction with the GDP-bound form of Rab27A in PC12 cells.";
RL   J. Biol. Chem. 278:15390-15396(2003).
RN   [7]
RP   INTERACTION WITH SGSM1 AND SGSM3.
RX   PubMed=17509819; DOI=10.1016/j.ygeno.2007.03.013;
RA   Yang H., Sasaki T., Minoshima S., Shimizu N.;
RT   "Identification of three novel proteins (SGSM1, 2, 3) which modulate
RT   small G protein (RAP and RAB)-mediated signaling pathway.";
RL   Genomics 90:249-260(2007).
CC   -!- FUNCTION: May be involved in vesicular trafficking and
CC       neurotransmitter release.
CC   -!- SUBUNIT: Interacts with MAP4K2 and SYTL4. Interacts with SGSM1 and
CC       SGSM3. Interacts with OPTN (By similarity).
CC   -!- INTERACTION:
CC       P47708:Rph3a; NbExp=2; IntAct=EBI-398411, EBI-398376;
CC       Q9R0Q1:Sytl4; NbExp=1; IntAct=EBI-398411, EBI-398341;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential). Golgi apparatus (By similarity).
CC       Note=Colocalizes with OPTN at the Golgi complex and in vesicular
CC       structures close to the plasma membrane (By similarity).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR   EMBL; S53270; AAB19682.1; -; mRNA.
DR   EMBL; AK076048; BAC36146.1; -; mRNA.
DR   EMBL; AK079306; BAC37603.1; -; mRNA.
DR   EMBL; AK080740; BAC38003.1; -; mRNA.
DR   EMBL; BC019990; AAH19990.1; -; mRNA.
DR   IPI; IPI00331128; -.
DR   RefSeq; NP_075615.2; NM_023126.2.
DR   UniGene; Mm.162811; -.
DR   PDB; 2FU5; X-ray; 2.00 A; C/D=1-175.
DR   PDBsum; 2FU5; -.
DR   ProteinModelPortal; P55258; -.
DR   SMR; P55258; 3-175.
DR   IntAct; P55258; 7.
DR   STRING; P55258; -.
DR   PhosphoSite; P55258; -.
DR   PRIDE; P55258; -.
DR   Ensembl; ENSMUST00000003121; ENSMUSP00000003121; ENSMUSG00000003037.
DR   GeneID; 17274; -.
DR   KEGG; mmu:17274; -.
DR   UCSC; uc009mfk.1; mouse.
DR   CTD; 17274; -.
DR   MGI; MGI:96960; Rab8a.
DR   eggNOG; maNOG05445; -.
DR   HOVERGEN; HBG009351; -.
DR   OrthoDB; EOG4K3KX6; -.
DR   PhylomeDB; P55258; -.
DR   NextBio; 291770; -.
DR   ArrayExpress; P55258; -.
DR   Bgee; P55258; -.
DR   CleanEx; MM_RAB8A; -.
DR   Genevestigator; P55258; -.
DR   GermOnline; ENSMUSG00000003037; Mus musculus.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0055037; C:recycling endosome; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Direct protein sequencing;
KW   Golgi apparatus; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW   Proto-oncogene; Transport.
FT   CHAIN         1    204       Ras-related protein Rab-8A.
FT                                /FTId=PRO_0000121132.
FT   PROPEP      205    207       Removed in mature form (Potential).
FT                                /FTId=PRO_0000370795.
FT   NP_BIND      15     22       GTP (By similarity).
FT   NP_BIND      63     67       GTP (By similarity).
FT   NP_BIND     121    124       GTP (By similarity).
FT   MOTIF        37     45       Effector region (By similarity).
FT   MOD_RES     181    181       Phosphoserine (By similarity).
FT   MOD_RES     185    185       Phosphoserine (By similarity).
FT   MOD_RES     192    192       Phosphothreonine (By similarity).
FT   MOD_RES     204    204       Cysteine methyl ester (Potential).
FT   LIPID       204    204       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   CONFLICT    176    183       KLEGNSPQ -> NWKATAA (in Ref. 1;
FT                                AAB19682).
FT   STRAND        6     14
FT   HELIX        37     41
FT   STRAND       43     52
FT   STRAND       55     63
FT   TURN         76     80
FT   STRAND       82     89
FT   HELIX        93    109
FT   STRAND      115    121
FT   HELIX       133    142
FT   STRAND      146    149
FT   HELIX       158    175
SQ   SEQUENCE   207 AA;  23668 MW;  AC89DC85588FB8F8 CRC64;
     MAKTYDYLFK LLLIGDSGVG KTCVLFRFSE DAFNSTFIST IGIDFKIRTI ELDGKRIKLQ
     IWDTAGQERF RTITTAYYRG AMGIMLVYDI TNEKSFDNIR NWIRNIEEHA SADVEKMILG
     NKCDVNDKRQ VSKERGEKLA LDYGIKFMET SAKANINVEN AFFTLARDIK AKMDKKLEGN
     SPQGSSHGVK ITVEQQKRTS FFRCSLL
//
ID   CAD11_MOUSE             Reviewed;         796 AA.
AC   P55288;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Cadherin-11;
DE   AltName: Full=OSF-4;
DE   AltName: Full=Osteoblast cadherin;
DE            Short=OB-cadherin;
DE   Flags: Precursor;
GN   Name=Cdh11; Synonyms=Cad-11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=95269886; PubMed=7750649; DOI=10.1006/dbio.1995.1148;
RA   Hoffmann I.H., Balling R.;
RT   "Cloning and expression analysis of a novel mesodermally expressed
RT   cadherin.";
RL   Dev. Biol. 169:337-346(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=95269887; PubMed=7750650; DOI=10.1006/dbio.1995.1149;
RA   Kimura Y., Matsunami H., Inoue T., Shimamura K., Uchida N., Ueno T.,
RA   Miyazaki T., Takeichi M.;
RT   "Cadherin-11 expressed in association with mesenchymal morphogenesis
RT   in the head, somite, and limb bud of early mouse embryos.";
RL   Dev. Biol. 169:347-358(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Calvaria;
RX   MEDLINE=94216322; PubMed=8163513;
RA   Okazaki M., Takeshita S., Kawai S., Kikuno R., Tsujimura A., Kudo A.,
RA   Amann E.;
RT   "Molecular cloning and characterization of OB-cadherin, a new member
RT   of cadherin family expressed in osteoblasts.";
RL   J. Biol. Chem. 269:12092-12098(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6; TISSUE=Testis;
RX   MEDLINE=97033837; PubMed=8879495;
RA   Munro S.B., Blaschuk O.W.;
RT   "A comprehensive survey of the cadherins expressed in the testes of
RT   fetal, immature, and adult mice utilizing the polymerase chain
RT   reaction.";
RL   Biol. Reprod. 55:822-827(1996).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-714, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Cadherins are calcium dependent cell adhesion proteins.
CC       They preferentially interact with themselves in a homophilic
CC       manner in connecting cells; cadherins may thus contribute to the
CC       sorting of heterogeneous cell types.
CC   -!- SUBUNIT: Interacts with PCDH8 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Selectively expressed in osteoblastic cell
CC       lines, precursor cell lines of osteoblasts, and primary
CC       osteoblastic cells from calvaria, as well as in lung, testis, and
CC       brain tissues at low levels.
CC   -!- DEVELOPMENTAL STAGE: In the testis, expression is highest in fetal
CC       gonad and decreases 8-fold in newborn.
CC   -!- SIMILARITY: Contains 5 cadherin domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; X77557; CAA54674.1; -; mRNA.
DR   EMBL; D31963; BAA06730.1; -; mRNA.
DR   EMBL; D21253; BAA04797.1; -; mRNA.
DR   EMBL; BC046314; AAH46314.1; -; mRNA.
DR   IPI; IPI00138190; -.
DR   PIR; A53584; A53584.
DR   PIR; I48277; I48277.
DR   PIR; I49556; I49556.
DR   RefSeq; NP_033996.4; NM_009866.4.
DR   UniGene; Mm.1571; -.
DR   PDB; 2A4C; X-ray; 2.90 A; A/B=54-151.
DR   PDB; 2A4E; X-ray; 3.20 A; A=55-260.
DR   PDBsum; 2A4C; -.
DR   PDBsum; 2A4E; -.
DR   ProteinModelPortal; P55288; -.
DR   SMR; P55288; 54-594, 691-789.
DR   STRING; P55288; -.
DR   PhosphoSite; P55288; -.
DR   PRIDE; P55288; -.
DR   Ensembl; ENSMUST00000075190; ENSMUSP00000074681; ENSMUSG00000031673.
DR   GeneID; 12552; -.
DR   KEGG; mmu:12552; -.
DR   UCSC; uc009mzu.1; mouse.
DR   CTD; 12552; -.
DR   MGI; MGI:99217; Cdh11.
DR   eggNOG; roNOG13528; -.
DR   HOGENOM; HBG505775; -.
DR   HOVERGEN; HBG005217; -.
DR   InParanoid; P55288; -.
DR   OMA; HQEAKVP; -.
DR   OrthoDB; EOG4QJRMJ; -.
DR   PhylomeDB; P55288; -.
DR   NextBio; 281602; -.
DR   ArrayExpress; P55288; -.
DR   Bgee; P55288; -.
DR   CleanEx; MM_CDH11; -.
DR   Genevestigator; P55288; -.
DR   GermOnline; ENSMUSG00000031673; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 5.
DR   Pfam; PF00028; Cadherin; 4.
DR   Pfam; PF01049; Cadherin_C; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 5.
DR   SUPFAM; SSF49313; Cadherin; 5.
DR   PROSITE; PS00232; CADHERIN_1; 3.
DR   PROSITE; PS50268; CADHERIN_2; 5.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Cell adhesion; Cell membrane;
KW   Cleavage on pair of basic residues; Glycoprotein; Membrane;
KW   Phosphoprotein; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     24       Potential.
FT   PROPEP       25     53       Potential.
FT                                /FTId=PRO_0000003787.
FT   CHAIN        54    796       Cadherin-11.
FT                                /FTId=PRO_0000003788.
FT   TOPO_DOM     54    617       Extracellular (Potential).
FT   TRANSMEM    618    640       Helical; (Potential).
FT   TOPO_DOM    641    796       Cytoplasmic (Potential).
FT   DOMAIN       54    159       Cadherin 1.
FT   DOMAIN      160    268       Cadherin 2.
FT   DOMAIN      269    383       Cadherin 3.
FT   DOMAIN      384    486       Cadherin 4.
FT   DOMAIN      487    612       Cadherin 5.
FT   MOD_RES     714    714       Phosphoserine.
FT   CARBOHYD    455    455       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    540    540       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    462    462       E -> D (in Ref. 1; CAA54674).
FT   CONFLICT    589    589       T -> L (in Ref. 2; BAA06730).
FT   CONFLICT    655    655       D -> N (in Ref. 2; BAA06730).
FT   CONFLICT    751    751       V -> M (in Ref. 1; CAA54674).
FT   CONFLICT    777    777       P -> Q (in Ref. 2; BAA06730).
FT   CONFLICT    782    782       L -> P (in Ref. 2; BAA06730).
FT   STRAND       59     63
FT   HELIX        64     66
FT   STRAND       68     70
FT   STRAND       72     76
FT   STRAND       84     86
FT   STRAND       88     94
FT   TURN         98    100
FT   STRAND      101    103
FT   TURN        105    107
FT   STRAND      109    112
FT   TURN        118    120
FT   STRAND      122    132
FT   TURN        133    135
FT   STRAND      138    140
FT   STRAND      143    150
FT   STRAND      158    169
FT   STRAND      177    180
FT   TURN        189    191
FT   STRAND      193    195
FT   STRAND      198    204
FT   TURN        205    207
FT   STRAND      208    210
FT   TURN        212    214
FT   STRAND      216    219
FT   STRAND      226    228
FT   STRAND      230    239
FT   TURN        240    243
FT   STRAND      249    259
SQ   SEQUENCE   796 AA;  88112 MW;  0D584D24641DD529 CRC64;
     MKENYCLQAA LVCLSMLYHS QAFALERRSH LHPSFHGHHE KGKEGQVLQR SKRGWVWNQF
     FVIEEYTGPD PVLVGRLHSD IDSGDGNIKY ILSGEGAGTI FVIDDKSGNI HATKTLDREE
     RAQYTLMAQA VDRDTNRPLE PPSEFIVKVQ DINDNPPEFL HEIYHANVPE RSNVGTSVIQ
     VTASDADDPT YGNSAKLVYS ILEGQPYFSV EAQTGIIRTA LPNMDREAKE EYHVVIQAKD
     MGGHMGGLSG TTKVTITLTD VNDNPPKFPQ SVYQMSVSEA AVPGEEVGRV KAKDPDIGEN
     GLVTYNIVDG DGIELFEITT DYETQDGVVK LKKPVDFETK RAYSLKIEAA NVHIDPKFIS
     NGPFKDTVTV KISVEDADEP PMFLAPSYIH EVQENAAAGT VVGRVHAKDP DAANSPIRYS
     IDRHTDLDRF FTINPEDGFI KTTKPLDREE TAWLNISVFA AEIHNRHQET KVPVAIRVLD
     VNDNAPKFAA PYEGFICESD HPKALSNQPI VTVSADDQDD TANGPRFIFS LPPEIMHNPN
     FTVRDNRDNT AGVYARRGGF SRQKQDFYLL PIVISDGGIP PMSSTNTLTI KVCGCDVNGA
     LLSCNAEAYI LNAGLSTGAL IAILACIVIL LVIVVLFVTL RRQKKEPLIV FEEEDVRENI
     ITYDDEGGGE EDTEAFDIAT LQNPDGINGF IPRKDIKPEY QYMPRPGLRP APNSVDVDDF
     INTRIQEADN DPTAPPYDSI QIYGYEGRGS VAGSLSSLES ATTDSDLDYD YLQNWGPRFK
     KLADLYGSKD TFDDDS
//
ID   AMRP_MOUSE              Reviewed;         360 AA.
AC   P55302;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Alpha-2-macroglobulin receptor-associated protein;
DE            Short=Alpha-2-MRAP;
DE   AltName: Full=Heparin-binding protein 44;
DE            Short=HBP-44;
DE   AltName: Full=Low density lipoprotein receptor-related protein-associated protein 1;
DE            Short=RAP;
DE   Flags: Precursor;
GN   Name=Lrpap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=94110255; PubMed=8282724;
RA   Nakamoto M., Ozawa M., Jacinto S.D., Furukawa T., Natori Y.,
RA   Shirahama H., Yonezawa S., Nakayama T., Muramatsu T.;
RT   "Mouse heparin binding protein-44 (HBP-44) associates with brushin, a
RT   high-molecular-weight glycoprotein antigen common to the kidney and
RT   teratocarcinomas.";
RL   J. Biochem. 114:344-349(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2-360, AND TISSUE SPECIFICITY.
RX   PubMed=2229028;
RA   Furukawa T., Ozawa M., Huang R.P., Muramatsu T.;
RT   "A heparin binding protein whose expression increases during
RT   differentiation of embryonal carcinoma cells to parietal endoderm
RT   cells: cDNA cloning and sequence analysis.";
RL   J. Biochem. 108:297-302(1990).
RN   [3]
RP   PROTEIN SEQUENCE OF 310-322, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Interacts with LRP1/alpha-2-macroglobulin receptor and
CC       glycoprotein 330.
CC   -!- SUBUNIT: Present on cell surface forming a complex with the alpha-
CC       2-macroglobulin receptor heavy and light chains. Binds LRP1B;
CC       binding is followed by internalization and degradation (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum (By similarity).
CC       Cytoplasm (By similarity). Cell surface (By similarity).
CC       Note=Intracellular and associated with cell surface receptors.
CC       Found in the endoplasmic reticulum (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in PYS-2 parietal endoderm
CC       cells and in the kidney. The RNA level increased about 10-fold
CC       during differentiation of F9 embryonal carcinoma cells to parietal
CC       endoderm cells.
CC   -!- SIMILARITY: Belongs to the alpha-2-MRAP family.
CC   -----------------------------------------------------------------------
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DR   EMBL; S67967; AAC60668.1; -; mRNA.
DR   EMBL; D00622; BAA00500.1; -; mRNA.
DR   IPI; IPI00469307; -.
DR   PIR; JX0281; JX0281.
DR   RefSeq; NP_038615.2; NM_013587.2.
DR   UniGene; Mm.277661; -.
DR   ProteinModelPortal; P55302; -.
DR   SMR; P55302; 38-360.
DR   STRING; P55302; -.
DR   PhosphoSite; P55302; -.
DR   REPRODUCTION-2DPAGE; IPI00469307; -.
DR   REPRODUCTION-2DPAGE; P55302; -.
DR   PRIDE; P55302; -.
DR   Ensembl; ENSMUST00000030986; ENSMUSP00000030986; ENSMUSG00000029103.
DR   GeneID; 16976; -.
DR   KEGG; mmu:16976; -.
DR   UCSC; uc008xdo.1; mouse.
DR   CTD; 16976; -.
DR   MGI; MGI:96829; Lrpap1.
DR   eggNOG; roNOG10961; -.
DR   HOVERGEN; HBG000197; -.
DR   InParanoid; P55302; -.
DR   OMA; YSREKNE; -.
DR   OrthoDB; EOG479F7K; -.
DR   PhylomeDB; P55302; -.
DR   NextBio; 291044; -.
DR   ArrayExpress; P55302; -.
DR   Bgee; P55302; -.
DR   Genevestigator; P55302; -.
DR   GermOnline; ENSMUSG00000029103; Mus musculus.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR010483; Alpha_2_MRAP_C.
DR   InterPro; IPR009066; MG_RAP_rcpt_1.
DR   Gene3D; G3DSA:1.20.81.10; MG_RAP_rcpt_1; 1.
DR   Pfam; PF06401; Alpha-2-MRAP_C; 1.
DR   Pfam; PF06400; Alpha-2-MRAP_N; 1.
DR   SUPFAM; SSF47045; MG_RAP_rcpt_1; 3.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Cytoplasm; Direct protein sequencing;
KW   Endoplasmic reticulum; Glycoprotein; Heparin-binding; Signal.
FT   SIGNAL        1     28       Potential.
FT   CHAIN        29    360       Alpha-2-macroglobulin receptor-associated
FT                                protein.
FT                                /FTId=PRO_0000020725.
FT   REGION      240    356       LDL receptor binding (Potential).
FT   COILED      184    302       Potential.
FT   MOTIF       357    360       Prevents secretion from ER (Potential).
FT   MOD_RES     290    290       N6-acetyllysine (By similarity).
FT   CARBOHYD    271    271       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   360 AA;  42215 MW;  72ED46FA0AC05D51 CRC64;
     MAPRRERVST LPRLQLLVLL LLPLMLVPQP IAGHGGKYSR EKNEPEMAAK RESGEEFRME
     KLNQLWEKAK RLHLSPVRLA ELHSDLKIQE RDELNWKKLK VEGLDKDGEK EAKLIHNLNV
     ILARYGLDGR KDAQMVHSNA LNEDTQDELG DPRLEKLWHK AKTSGKFSSE ELDKLWREFL
     HYKEKIQEYN VLLDTLSRAE EGYENLLSPS DMAHIKSDTL ISKHSELKDR LRSINQGLDR
     LRKVSHQGYG STTEFEEPRV IDLWDLAQSA NFTEKELESF REELKHFEAK IEKHNHYQKQ
     LEISHQKLKH VESIGDPEHI SRNKEKYVLL EEKTKELGYK VKKHLQDLSS RVSRARHNEL
//
ID   STMN2_MOUSE             Reviewed;         179 AA.
AC   P55821;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Stathmin-2;
DE   AltName: Full=Superior cervical ganglion-10 protein;
DE            Short=Protein SCG10;
GN   Name=Stmn2; Synonyms=Scg10, Scgn10, Stmb2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=94117005; PubMed=8288240; DOI=10.1006/geno.1993.1477;
RA   Okazaki T., Yoshida B.N., Avraham K.B., Wang H., Wuenschell C.W.,
RA   Jenkins N.A., Copeland N.G., Anderson D.J., Mori N.;
RT   "Molecular diversity of the SCG10/stathmin gene family in the mouse.";
RL   Genomics 18:360-373(1993).
RN   [2]
RP   ERRATUM.
RA   Okazaki T., Yoshida B.N., Avraham K.B., Wang H., Wuenschell C.W.,
RA   Jenkins N.A., Copeland N.G., Anderson D.J., Mori N.;
RL   Genomics 21:298-298(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Is a key regulator of neurite extension through
CC       regulation of microtubule instabilily (By similarity).
CC   -!- SUBUNIT: Interacts with ITM2C (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
CC       Cell projection, growth cone. Cell projection, axon. Membrane;
CC       Peripheral membrane protein; Cytoplasmic side (Potential).
CC       Note=Associated with punctate structures in the perinuclear
CC       cytoplasm, axons, and growth cones of developing neurons. SCG10
CC       exists in both soluble and membrane-bound forms.
CC   -!- TISSUE SPECIFICITY: Neuron specific.
CC   -!- PTM: Sumoylated (By similarity).
CC   -!- SIMILARITY: Belongs to the stathmin family.
CC   -----------------------------------------------------------------------
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DR   EMBL; L20259; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L20260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L20261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L20262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; L20263; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC026538; AAH26538.1; -; mRNA.
DR   IPI; IPI00277874; -.
DR   PIR; A48917; A48917.
DR   RefSeq; NP_079561.1; NM_025285.2.
DR   UniGene; Mm.29580; -.
DR   ProteinModelPortal; P55821; -.
DR   SMR; P55821; 39-174.
DR   MINT; MINT-1212338; -.
DR   STRING; P55821; -.
DR   PhosphoSite; P55821; -.
DR   PRIDE; P55821; -.
DR   Ensembl; ENSMUST00000029002; ENSMUSP00000029002; ENSMUSG00000027500.
DR   Ensembl; ENSMUST00000116348; ENSMUSP00000112051; ENSMUSG00000027500.
DR   GeneID; 20257; -.
DR   KEGG; mmu:20257; -.
DR   UCSC; uc008ooo.1; mouse.
DR   CTD; 20257; -.
DR   MGI; MGI:98241; Stmn2.
DR   eggNOG; roNOG04799; -.
DR   HOGENOM; HBG444413; -.
DR   HOVERGEN; HBG054037; -.
DR   InParanoid; P55821; -.
DR   OMA; NSNFSKM; -.
DR   OrthoDB; EOG4DR9DK; -.
DR   NextBio; 297917; -.
DR   ArrayExpress; P55821; -.
DR   Bgee; P55821; -.
DR   CleanEx; MM_STMN2; -.
DR   Genevestigator; P55821; -.
DR   GermOnline; ENSMUSG00000027500; Mus musculus.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0030426; C:growth cone; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR000956; Stathmin.
DR   PANTHER; PTHR10104; Stathmin; 1.
DR   Pfam; PF00836; Stathmin; 1.
DR   PIRSF; PIRSF002285; Stathmin; 1.
DR   PRINTS; PR00345; STATHMIN.
DR   SUPFAM; SSF101494; Stathmin; 1.
DR   PROSITE; PS00563; STATHMIN_1; 1.
DR   PROSITE; PS01041; STATHMIN_2; 1.
PE   2: Evidence at transcript level;
KW   Cell projection; Coiled coil; Cytoplasm; Membrane; Phosphoprotein;
KW   Ubl conjugation.
FT   CHAIN         1    179       Stathmin-2.
FT                                /FTId=PRO_0000182397.
FT   REGION        1     26       Membrane attachment (Potential).
FT   REGION       39     96       Regulatory/phosphorylation domain
FT                                (Potential).
FT   COILED       75    179       Potential.
FT   MOD_RES      16     16       Phosphoserine (Potential).
FT   MOD_RES      50     50       Phosphoserine (Potential).
FT   MOD_RES      62     62       Phosphoserine (Potential).
FT   MOD_RES      73     73       Phosphoserine (Potential).
FT   MOD_RES      80     80       Phosphoserine (Potential).
FT   MOD_RES      97     97       Phosphoserine (Potential).
SQ   SEQUENCE   179 AA;  20828 MW;  F9A258A1B57E620D CRC64;
     MAKTAMAYKE KMKELSMLSL ICSCFYPEPR NINIYTYDDM EVKQINKRAS GQAFELILKP
     PSPISEAPRT LASPKKKDLS LEEIQKKLEA AEERRKSQEA QVLKQLAEKR EHEREVLQKA
     LEENNNFSKM AEEKLILKME QIKENREANL AAIIERLQEK ERHAAEVRRN KELQVELSG
//
ID   GOGA3_MOUSE             Reviewed;        1487 AA.
AC   P55937; Q80VF5; Q8CCK4; Q9QYT2; Q9QYT3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 3.
DT   30-NOV-2010, entry version 82.
DE   RecName: Full=Golgin subfamily A member 3;
DE   AltName: Full=Golgin-160;
DE   AltName: Full=Male-enhanced antigen 2;
DE            Short=MEA-2;
GN   Name=Golga3; Synonyms=Mea2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=CD-1; TISSUE=Testis;
RX   MEDLINE=97217683; PubMed=9063644;
RA   Kondo M., Sutou S.;
RT   "Cloning and molecular characterization of cDNA encoding a mouse male-
RT   enhanced antigen-2 (Mea-2): a putative family of the Golgi
RT   autoantigen.";
RL   DNA Seq. 7:71-82(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), AND FUNCTION.
RC   STRAIN=C57BL/6;
RX   MEDLINE=21824170; PubMed=11835574; DOI=10.1002/mrd.10035;
RA   Banu Y., Matsuda M., Yoshihara M., Kondo M., Sutou S., Matsukuma S.;
RT   "Golgi matrix protein gene, Golga3/Mea2, rearranged and re-expressed
RT   in pachytene spermatocytes restores spermatogenesis in the mouse.";
RL   Mol. Reprod. Dev. 61:288-301(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, and FVB/N-3; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1081-1486.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Plays an important role in spermatogenesis and/or testis
CC       development. Probably identical with the serologically detectable
CC       male antigen (SDM). Probably involved in maintaining Golgi
CC       structure.
CC   -!- SUBUNIT: Homodimer. Interacts with GOLGA7. Interacts with GOPC (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus,
CC       Golgi stack membrane; Peripheral membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2;
CC         IsoId=P55937-2; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=1;
CC         IsoId=P55937-1; Sequence=VSP_016071;
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis. Transcripts can be
CC       found in spermatids during spermatogenesis. No expression in
CC       Leydig cells, spermatogonia or spermatocytes. Detected at low
CC       levels in all tissues.
CC   -!- DOMAIN: Extended rod-like protein with coiled-coil domains.
CC   -!- PTM: Cleaved by caspases in apoptotic cells (By similarity).
CC   -----------------------------------------------------------------------
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DR   EMBL; D78270; BAA19612.2; -; mRNA.
DR   EMBL; AB029537; BAA86889.2; -; Genomic_DNA.
DR   EMBL; AB029537; BAA86890.2; -; Genomic_DNA.
DR   EMBL; BC043452; AAH43452.1; -; mRNA.
DR   EMBL; BC053002; AAH53002.1; -; mRNA.
DR   EMBL; AK032610; BAC27949.1; -; mRNA.
DR   IPI; IPI00336281; -.
DR   IPI; IPI00469799; -.
DR   PIR; T42722; T42722.
DR   RefSeq; NP_032172.3; NM_008146.3.
DR   UniGene; Mm.393008; -.
DR   UniGene; Mm.9392; -.
DR   ProteinModelPortal; P55937; -.
DR   IntAct; P55937; 1.
DR   STRING; P55937; -.
DR   PhosphoSite; P55937; -.
DR   PRIDE; P55937; -.
DR   Ensembl; ENSMUST00000031477; ENSMUSP00000031477; ENSMUSG00000029502.
DR   GeneID; 269682; -.
DR   KEGG; mmu:269682; -.
DR   UCSC; uc008yqd.1; mouse.
DR   CTD; 269682; -.
DR   MGI; MGI:96958; Golga3.
DR   eggNOG; roNOG09353; -.
DR   HOGENOM; HBG402826; -.
DR   HOVERGEN; HBG051753; -.
DR   InParanoid; P55937; -.
DR   PhylomeDB; P55937; -.
DR   NextBio; 392969; -.
DR   ArrayExpress; P55937; -.
DR   Bgee; P55937; -.
DR   CleanEx; MM_GOLGA3; -.
DR   Genevestigator; P55937; -.
DR   GermOnline; ENSMUSG00000029502; Mus musculus.
DR   GO; GO:0005793; C:ER-Golgi intermediate compartment; IDA:MGI.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW   Developmental protein; Differentiation; Golgi apparatus; Membrane;
KW   Phosphoprotein; Spermatogenesis.
FT   CHAIN         1   1487       Golgin subfamily A member 3.
FT                                /FTId=PRO_0000190058.
FT   REGION      121    141       Interaction with GOPC (By similarity).
FT   REGION      172    257       Golgi-targeting domain (By similarity).
FT   COILED      358   1454       Potential.
FT   COMPBIAS    238    321       Ser-rich.
FT   COMPBIAS    363    366       Poly-Ala.
FT   COMPBIAS    534    734       Gln-rich.
FT   COMPBIAS   1228   1366       Gln-rich.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      60     60       Phosphoserine.
FT   MOD_RES     385    385       Phosphoserine (By similarity).
FT   MOD_RES     388    388       Phosphoserine (By similarity).
FT   MOD_RES     389    389       Phosphoserine (By similarity).
FT   MOD_RES     391    391       Phosphoserine (By similarity).
FT   MOD_RES     395    395       Phosphoserine (By similarity).
FT   MOD_RES     524    524       Phosphoserine (By similarity).
FT   MOD_RES     979    979       Phosphoserine (By similarity).
FT   VAR_SEQ      97    136       Missing (in isoform 1).
FT                                /FTId=VSP_016071.
FT   CONFLICT     30     30       T -> I (in Ref. 3; AAH53002).
FT   CONFLICT    477    477       G -> E (in Ref. 3; AAH53002).
FT   CONFLICT    592    592       M -> T (in Ref. 2; BAA86889/BAA86890).
FT   CONFLICT    843    843       Q -> L (in Ref. 2; BAA86889/BAA86890).
FT   CONFLICT    982    982       T -> S (in Ref. 3; AAH53002).
FT   CONFLICT   1015   1015       A -> S (in Ref. 3; AAH43452).
FT   CONFLICT   1466   1466       A -> P (in Ref. 4; BAC27949).
SQ   SEQUENCE   1487 AA;  167220 MW;  831303DC90754F0B CRC64;
     MDGASAKQDG LWESKSSSDV SSCPEASLET VGSLARLPDQ QDTAQDASVE VNRGFKEEGS
     PDRSSQVAIC QNGQIPDLQL SLDPTTSPVG PDASTGVDGF HDNLRNSQGT SAEGSVRKEA
     LQSLRLSLPM QETQLCSTAS SLPLEKEEQV RLQARKRLEE QLMQYRVKRH RERSSQPATK
     MKLFSTLDPE LMLNPENLPR ASTVAVTKEY SFLRTSVPRG PKVGSLGLLA HSKEKKNSKS
     SKIRSLADYR TEDPSDSGGL GSTADAVGSS LKQSRSSTSV VSEVSPSSET DNRVESASMT
     GDSVSEADGN ESDSSSHSSL SARGACGVLG NVGMPGTAYM VDGQEISAEA LGQFPSIKDV
     LQAAAAQHQD QNQEANGEVR SRRDSICSSV SMESSLAEPQ DELLQILKDK RRLEGQVEAL
     SLEASQALQE KAELQAQLAA LSTRLQAQVE HSHSSQQKQD SLSSEVDTLK QSCWDLGRAM
     TDLQSMLEAK NASLASSNND LQVAEEQYQR LMAKVEDMQR NILSKDNTVH DLRQQMTALQ
     SQLQQVQLER TTLTSKLQAS QAEITSLQHA RQWYQQQLTL AQEARVRLQG EMAHIQVGQM
     TQAGLLEHLK LENVSLSHQL TETQHRSIKE KERIAVQLQS IEADMLDQEA AFVQIREAKT
     MVEEDLQRRL EEFEGEREQL QKVADAAASL EQQLEQVKLT LFQRDQQLAA LQQEHLDVIK
     QLTSTQEALQ AKGQSLDDLH TRYDELQARL EELQREADSR EDAIHFLQNE KIVLEVALQS
     AKSDKEELDR GARRLEEDTE ETSGLLEQLR QDLAVKSNQV EHLQQETATL RKQMQKVKEQ
     FVQQKVMVEA YRRDATSKDQ LINELKATKK RLDSEMKELR QELIKLQGEK KTVEVEHSRL
     QKDMSLVHQQ MAELEGHLQS VQKERDEMEI HLQSLKFDKE QMIALTEANE TLKKQIEELQ
     QEAKKAITEQ KQKMKRLGSD LTSAQKEMKT KHKAYENAVS ILSRRLQEAL ASKEATDAEL
     NQLRAQSTGG SSDPVLHEKI RALEVELQNV GQSKILLEKE LQEVITMTSQ ELEESREKVL
     ELEDELQESR GFRRKIKRLE ESNKKLALEL EHERGKLTGL GQSNAALREH NSILETALAK
     READLVQLNL QVQAVLQRKE EEDRQMKQLV QALQVSLEKE KMEVNSLKEQ MAAARIEAGH
     NRRHFKAATL ELSEVKKELQ AKEHLVQTLQ AEVDELQIQD GKHSQEIAQF QTELAEARTQ
     LQLLQKKLDE QMSQQPTGSQ EMEDLKWELD QKEREIQSLK QQLDLTEQQG KKELEGTQQT
     LQTIKSELEM VQEDLSETQK DKFMLQAKVS ELKNNMKTLL QQNQQLKLDL RRGAAKKKEP
     KGESNSSSPA TPIKIPDCPV PASLLEELLR PPPAVSKEPL KNLNNCLQQL KQEMDSLQRQ
     MEEHTITVHE SLSSWAQVEA APAEHAHPRG DTKLHNQNSV PRDGLGQ
//
ID   ATPK_MOUSE              Reviewed;          88 AA.
AC   P56135; Q3THX9; Q9JMF4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=ATP synthase subunit f, mitochondrial;
GN   Name=Atp5j2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=20145471; PubMed=10679242; DOI=10.1006/bbrc.2000.2170;
RA   Inoue S., Sano H., Ohta M.;
RT   "Growth suppression of Escherichia coli by induction of expression of
RT   mammalian genes with transmembrane or ATPase domains.";
RL   Biochem. Biophys. Res. Commun. 268:553-561(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2; TISSUE=Bone marrow, Embryo, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 17-39, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
CC       synthase or Complex V) produces ATP from ADP in the presence of a
CC       proton gradient across the membrane which is generated by electron
CC       transport complexes of the respiratory chain. F-type ATPases
CC       consist of two structural domains, F(1) - containing the
CC       extramembraneous catalytic core and F(0) - containing the membrane
CC       proton channel, linked together by a central stalk and a
CC       peripheral stalk. During catalysis, ATP synthesis in the catalytic
CC       domain of F(1) is coupled via a rotary mechanism of the central
CC       stalk subunits to proton translocation. Part of the complex F(0)
CC       domain. Minor subunit located with subunit a in the membrane.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel. CF(0) seems to
CC       have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC   -!- SIMILARITY: Belongs to the ATPase F chain family.
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DR   EMBL; AB030192; BAA92756.1; -; mRNA.
DR   EMBL; AK002519; BAB22157.1; -; mRNA.
DR   EMBL; AK003235; BAB22660.1; -; mRNA.
DR   EMBL; AK003817; BAB23014.1; -; mRNA.
DR   EMBL; AK013130; BAB28667.1; -; mRNA.
DR   EMBL; AK151737; BAE30651.1; -; mRNA.
DR   EMBL; AK168095; BAE40067.1; -; mRNA.
DR   EMBL; BC029226; AAH29226.1; -; mRNA.
DR   IPI; IPI00271986; -.
DR   RefSeq; NP_065607.1; NM_020582.2.
DR   UniGene; Mm.133551; -.
DR   STRING; P56135; -.
DR   PRIDE; P56135; -.
DR   Ensembl; ENSMUST00000037056; ENSMUSP00000039726; ENSMUSG00000038690.
DR   GeneID; 57423; -.
DR   KEGG; mmu:57423; -.
DR   UCSC; uc009amk.1; mouse.
DR   CTD; 57423; -.
DR   MGI; MGI:1927558; Atp5j2.
DR   eggNOG; maNOG21047; -.
DR   GeneTree; ENSGT00510000046986; -.
DR   HOGENOM; HBG505481; -.
DR   HOVERGEN; HBG002418; -.
DR   InParanoid; P56135; -.
DR   OMA; PARFYGK; -.
DR   OrthoDB; EOG4NVZMX; -.
DR   PhylomeDB; P56135; -.
DR   NextBio; 313776; -.
DR   ArrayExpress; P56135; -.
DR   Bgee; P56135; -.
DR   Genevestigator; P56135; -.
DR   GermOnline; ENSMUSG00000038690; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0015992; P:proton transport; IEA:UniProtKB-KW.
DR   InterPro; IPR019344; F1F0-ATPsyn_F_prd.
DR   PANTHER; PTHR13080; F1F0-ATPsyn_F_prd; 1.
DR   Pfam; PF10206; WRW; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP synthesis; CF(0); Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2     88       ATP synthase subunit f, mitochondrial.
FT                                /FTId=PRO_0000194825.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
SQ   SEQUENCE   88 AA;  10344 MW;  89526C72EC436E48 CRC64;
     MASLVPLKEK KLMEVKLGEL PSWIMMRDFT PSGIAGAFRR GYDRYYNKYI NVRKGSISGI
     SMVLAAYVVF SYCISYKELK HERRRKYH
//
ID   ARP19_MOUSE             Reviewed;         112 AA.
AC   P56212; Q543L2;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=cAMP-regulated phosphoprotein 19;
DE            Short=ARPP-19;
GN   Name=Arpp19;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ARPP-16 AND ARPP-19), AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Brain;
RA   Girault J.-A., Horiuchi A., Gustafson E., Rosen N., Greengard P.;
RT   "Differential expression of ARPP-16 and ARPP-19, two highly related
RT   phosphoproteins, one of which is specifically associated with
RT   dopamine-innervated brain regions.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ARPP-19).
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ARPP-19).
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION.
RX   PubMed=2845422; DOI=10.1073/pnas.85.20.7790;
RA   Girault J.-A., Shalaby I.A., Rosen N.L., Greengard P.;
RT   "Regulation by cAMP and vasoactive intestinal peptide of
RT   phosphorylation of specific proteins in striatal cells in culture.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:7790-7794(1988).
RN   [5]
RP   PHOSPHORYLATION AT SER-104.
RX   PubMed=11279279;
RA   Dulubova I., Horiuchi A., Snyder G.L., Girault J.-A., Czernik A.J.,
RA   Shao L., Ramabhadran R., Greengard P., Nairn A.C.;
RT   "ARPP-16/ARPP-19: a highly conserved family of cAMP-regulated
RT   phosphoproteins.";
RL   J. Neurochem. 77:229-238(2001).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May enhance GAP-43 expression by binding to the NGF-
CC       regulatory region of its mRNA (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=ARPP-19;
CC         IsoId=P56212-1; Sequence=Displayed;
CC       Name=ARPP-16;
CC         IsoId=P56212-2; Sequence=VSP_018556;
CC   -!- DEVELOPMENTAL STAGE: Isoform ARPP-19 is highly expressed in the
CC       embryo and its levels decrease progressively as development
CC       proceeds. In contrast, isoform ARPP-16 appears in the brain at the
CC       end of the first postnatal week and increases to reach a plateau.
CC   -!- PTM: Phosphorylated by PKA.
CC   -!- SIMILARITY: Belongs to the endosulfine family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; AJ005983; CAA06797.1; -; mRNA.
DR   EMBL; AK049760; BAC33908.1; -; mRNA.
DR   EMBL; BC040206; AAH40206.1; -; mRNA.
DR   IPI; IPI00227850; -.
DR   IPI; IPI00752633; -.
DR   RefSeq; NP_067523.1; NM_021548.4.
DR   UniGene; Mm.247837; -.
DR   STRING; P56212; -.
DR   PhosphoSite; P56212; -.
DR   PRIDE; P56212; -.
DR   Ensembl; ENSMUST00000007800; ENSMUSP00000007800; ENSMUSG00000007656.
DR   GeneID; 59046; -.
DR   KEGG; mmu:59046; -.
DR   UCSC; uc009qro.1; mouse.
DR   UCSC; uc009qrp.1; mouse.
DR   CTD; 59046; -.
DR   MGI; MGI:1891691; Arpp19.
DR   eggNOG; roNOG16440; -.
DR   GeneTree; ENSGT00390000010139; -.
DR   HOGENOM; HBG564616; -.
DR   HOVERGEN; HBG000297; -.
DR   InParanoid; P56212; -.
DR   OMA; NLGNKPG; -.
DR   OrthoDB; EOG4KH2WG; -.
DR   NextBio; 314670; -.
DR   ArrayExpress; P56212; -.
DR   Bgee; P56212; -.
DR   CleanEx; MM_ARPP19; -.
DR   Genevestigator; P56212; -.
DR   GermOnline; ENSMUSG00000007656; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR006760; Endosulphine.
DR   Pfam; PF04667; Endosulfine; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    112       cAMP-regulated phosphoprotein 19.
FT                                /FTId=PRO_0000146762.
FT   MOD_RES       2      2       N-acetylserine; in isoform ARPP-19 (By
FT                                similarity).
FT   MOD_RES      17     17       N-acetylmethionine; in isoform ARPP-16
FT                                (By similarity).
FT   MOD_RES      62     62       Phosphoserine (By similarity).
FT   MOD_RES     104    104       Phosphoserine; by PKA.
FT   MOD_RES     109    109       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1     16       Missing (in isoform ARPP-16).
FT                                /FTId=VSP_018556.
SQ   SEQUENCE   112 AA;  12293 MW;  F18BE46E35C839AB CRC64;
     MSAEVPEAAS AEEQKEMEDK VTSPEKAEEA KLKARYPHLG QKPGGSDFLR KRLQKGQKYF
     DSGDYNMAKA KMKNKQLPAA APDKTEVTGD HIPTPQDLPQ RKPSLVASKL AG
//
ID   CART_MOUSE              Reviewed;         129 AA.
AC   P56388; Q9QXZ8;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2001, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Cocaine- and amphetamine-regulated transcript protein;
DE   Contains:
DE     RecName: Full=CART(1-52);
DE   Contains:
DE     RecName: Full=CART(55-102);
DE   Contains:
DE     RecName: Full=CART(62-102);
DE   Flags: Precursor;
GN   Name=Cartpt; Synonyms=Cart;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=129/SvJ;
RX   MEDLINE=20080750; PubMed=10612705; DOI=10.1016/S0006-8993(99)01907-1;
RA   Adams L.D., Gong W., Vechia S.D., Hunter R.G., Kuhar M.J.;
RT   "CART: from gene to function.";
RL   Brain Res. 848:137-140(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Satiety factor closely associated with the actions of
CC       leptin and neuropeptide y; this anorectic peptide inhibits both
CC       normal and starvation-induced feeding and completely blocks the
CC       feeding response induced by neuropeptide Y and regulated by leptin
CC       in the hypothalamus (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=P56388-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=P56388-2; Sequence=VSP_000793;
CC   -!- SIMILARITY: Belongs to the CART family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF148071; AAF24168.1; -; Genomic_DNA.
DR   EMBL; BC056431; AAH56431.1; -; mRNA.
DR   IPI; IPI00113180; -.
DR   IPI; IPI00230430; -.
DR   RefSeq; NP_038760.3; NM_013732.6.
DR   UniGene; Mm.75498; -.
DR   ProteinModelPortal; P56388; -.
DR   SMR; P56388; 89-129.
DR   PRIDE; P56388; -.
DR   Ensembl; ENSMUST00000022150; ENSMUSP00000022150; ENSMUSG00000021647.
DR   GeneID; 27220; -.
DR   KEGG; mmu:27220; -.
DR   UCSC; uc007rpw.1; mouse.
DR   CTD; 27220; -.
DR   MGI; MGI:1351330; Cartpt.
DR   eggNOG; roNOG17238; -.
DR   HOGENOM; HBG713570; -.
DR   HOVERGEN; HBG018929; -.
DR   InParanoid; P56388; -.
DR   OMA; MESSRLR; -.
DR   OrthoDB; EOG4G1MJ1; -.
DR   PhylomeDB; P56388; -.
DR   NextBio; 305124; -.
DR   ArrayExpress; P56388; -.
DR   Bgee; P56388; -.
DR   CleanEx; MM_CARTPT; -.
DR   Genevestigator; P56388; -.
DR   GermOnline; ENSMUSG00000021647; Mus musculus.
DR   GO; GO:0005615; C:extracellular space; IDA:HGNC.
DR   GO; GO:0005184; F:neuropeptide hormone activity; TAS:MGI.
DR   GO; GO:0000186; P:activation of MAPKK activity; IDA:HGNC.
DR   GO; GO:0008343; P:adult feeding behavior; IDA:HGNC.
DR   GO; GO:0001678; P:cellular glucose homeostasis; ISS:HGNC.
DR   GO; GO:0009267; P:cellular response to starvation; IDA:HGNC.
DR   GO; GO:0032922; P:circadian regulation of gene expression; ISS:HGNC.
DR   GO; GO:0032099; P:negative regulation of appetite; IMP:HGNC.
DR   GO; GO:0045779; P:negative regulation of bone resorption; IGI:HGNC.
DR   GO; GO:0045671; P:negative regulation of osteoclast differentiation; TAS:HGNC.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; TAS:MGI.
DR   GO; GO:0045777; P:positive regulation of blood pressure; ISS:HGNC.
DR   GO; GO:0032812; P:positive regulation of epinephrine secretion; ISS:HGNC.
DR   GO; GO:0051971; P:positive regulation of transmission of nerve impulse; ISS:HGNC.
DR   GO; GO:0007268; P:synaptic transmission; IEA:UniProtKB-KW.
DR   InterPro; IPR009106; CART.
DR   Gene3D; G3DSA:4.10.40.30; CART; 1.
DR   PANTHER; PTHR16655; CART; 1.
DR   Pfam; PF06373; CART; 1.
DR   SUPFAM; SSF64546; CART; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cleavage on pair of basic residues;
KW   Disulfide bond; Neuropeptide; Neurotransmitter; Secreted; Signal.
FT   SIGNAL        1     27       Potential.
FT   CHAIN        28    129       Cocaine- and amphetamine-regulated
FT                                transcript protein.
FT                                /FTId=PRO_0000004436.
FT   PEPTIDE      28     79       CART(1-52) (By similarity).
FT                                /FTId=PRO_0000004437.
FT   PEPTIDE      82    129       CART(55-102) (By similarity).
FT                                /FTId=PRO_0000004438.
FT   PEPTIDE      89    129       CART(62-102) (Potential).
FT                                /FTId=PRO_0000004439.
FT   DISULFID     95    113       By similarity.
FT   DISULFID    101    121       By similarity.
FT   DISULFID    115    128       By similarity.
FT   VAR_SEQ      54     66       Missing (in isoform Short).
FT                                /FTId=VSP_000793.
SQ   SEQUENCE   129 AA;  14285 MW;  E4CA6CE70BEE6DF2 CRC64;
     MESSRLRLLP LLGAALLLLL PLLGARAQED AELQPRALDI YSAVDDASHE KELPRRQLRA
     PGAMLQIEAL QEVLKKLKSK RIPIYEKKYG QVPMCDAGEQ CAVRKGARIG KLCDCPRGTS
     CNSFLLKCL
//
ID   CX6B1_MOUSE             Reviewed;          86 AA.
AC   P56391; Q545A3;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Cytochrome c oxidase subunit 6B1;
DE   AltName: Full=Cytochrome c oxidase subunit VIb isoform 1;
DE            Short=COX VIb-1;
GN   Name=Cox6b1; Synonyms=Cox6b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Small intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 29-39; 48-58 AND 63-86, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Connects the two COX monomers into the physiological
CC       dimeric form (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 6B family.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK007996; BAB25398.1; -; mRNA.
DR   EMBL; AK012686; BAB28411.1; -; mRNA.
DR   EMBL; AK018721; BAB31367.1; -; mRNA.
DR   EMBL; BC024343; AAH24343.1; -; mRNA.
DR   IPI; IPI00225390; -.
DR   RefSeq; NP_079904.1; NM_025628.2.
DR   UniGene; Mm.400; -.
DR   ProteinModelPortal; P56391; -.
DR   SMR; P56391; 8-86.
DR   STRING; P56391; -.
DR   PRIDE; P56391; -.
DR   Ensembl; ENSMUST00000075738; ENSMUSP00000075150; ENSMUSG00000036751.
DR   GeneID; 110323; -.
DR   KEGG; mmu:110323; -.
DR   UCSC; uc009gfl.1; mouse.
DR   CTD; 110323; -.
DR   MGI; MGI:107460; Cox6b1.
DR   eggNOG; roNOG17205; -.
DR   GeneTree; ENSGT00390000001191; -.
DR   HOGENOM; HBG330644; -.
DR   HOVERGEN; HBG051090; -.
DR   InParanoid; P56391; -.
DR   OMA; HRCQKAM; -.
DR   OrthoDB; EOG4QNMXS; -.
DR   PhylomeDB; P56391; -.
DR   NextBio; 363775; -.
DR   ArrayExpress; P56391; -.
DR   Bgee; P56391; -.
DR   CleanEx; MM_COX6B1; -.
DR   Genevestigator; P56391; -.
DR   GermOnline; ENSMUSG00000036751; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR   InterPro; IPR003213; Cyt_c_oxidase_su6B.
DR   Gene3D; G3DSA:1.10.10.140; Cyt_c_oxidase_6B; 1.
DR   Pfam; PF02297; COX6B; 1.
DR   PIRSF; PIRSF000278; Cyt_c_oxidase_6B; 1.
DR   SUPFAM; SSF47694; Cyt_c_oxidase_6B; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Disulfide bond; Mitochondrion.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2     86       Cytochrome c oxidase subunit 6B1.
FT                                /FTId=PRO_0000194915.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   DISULFID     30     65       By similarity.
FT   DISULFID     40     54       By similarity.
SQ   SEQUENCE   86 AA;  10071 MW;  A2E96D96CC37509A CRC64;
     MAEDIKTKIK NYKTAPFDSR FPNQNQTKNC WQNYLDFHRC EKAMTAKGGD VSVCEWYRRV
     YKSLCPVSWV SAWDDRIAEG TFPGKI
//
ID   UBP5_MOUSE              Reviewed;         858 AA.
AC   P56399;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 5;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 5;
DE   AltName: Full=Isopeptidase T;
DE   AltName: Full=Ubiquitin thiolesterase 5;
DE   AltName: Full=Ubiquitin-specific-processing protease 5;
GN   Name=Usp5; Synonyms=Isot;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-623, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   INTERACTION WITH TRIML1.
RX   PubMed=19156909; DOI=10.1002/mrd.20997;
RA   Tian L., Wu X., Lin Y., Liu Z., Xiong F., Han Z., Zhou Y., Zeng Q.,
RA   Wang Y., Deng J., Chen H.;
RT   "Characterization and potential function of a novel pre-implantation
RT   embryo-specific RING finger protein: TRIML1.";
RL   Mol. Reprod. Dev. 76:656-664(2009).
CC   -!- FUNCTION: Cleaves linear and branched multiubiquitin polymers with
CC       a marked preference for branched polymers. Involved in unanchored
CC       'Lys-48'-linked polyubiquitin disassembly. Binds linear and 'Lys-
CC       63'-linked polyubiquitin with a lower affinity (By similarity).
CC   -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- COFACTOR: Zinc.
CC   -!- SUBUNIT: Interacts with TRIML1.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC   -!- SIMILARITY: Contains 2 UBA domains.
CC   -!- SIMILARITY: Contains 1 UBP-type zinc finger.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC002397; AAC36015.1; -; Genomic_DNA.
DR   EMBL; BC066993; AAH66993.1; -; mRNA.
DR   IPI; IPI00113214; -.
DR   RefSeq; NP_038728.1; NM_013700.1.
DR   UniGene; Mm.3571; -.
DR   ProteinModelPortal; P56399; -.
DR   SMR; P56399; 1-858.
DR   MINT; MINT-220667; -.
DR   STRING; P56399; -.
DR   MEROPS; C19.001; -.
DR   PhosphoSite; P56399; -.
DR   PRIDE; P56399; -.
DR   Ensembl; ENSMUST00000047510; ENSMUSP00000041299; ENSMUSG00000038429.
DR   GeneID; 22225; -.
DR   KEGG; mmu:22225; -.
DR   UCSC; uc009dsa.1; mouse.
DR   CTD; 22225; -.
DR   MGI; MGI:1347343; Usp5.
DR   eggNOG; roNOG15340; -.
DR   GeneTree; ENSGT00390000000874; -.
DR   HOGENOM; HBG746888; -.
DR   HOVERGEN; HBG002833; -.
DR   InParanoid; P56399; -.
DR   OMA; VIYNDQK; -.
DR   PhylomeDB; P56399; -.
DR   BRENDA; 3.1.2.15; 244.
DR   NextBio; 302251; -.
DR   ArrayExpress; P56399; -.
DR   Bgee; P56399; -.
DR   CleanEx; MM_USP5; -.
DR   Genevestigator; P56399; -.
DR   GermOnline; ENSMUSG00000038429; Mus musculus.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19.
DR   InterPro; IPR009060; UBA-like.
DR   InterPro; IPR000449; UBA/transl_elong_EF1B_N.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   InterPro; IPR016652; Ubiquitinyl_hydrolase.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00627; UBA; 2.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   PIRSF; PIRSF016308; UBP; 1.
DR   SMART; SM00165; UBA; 2.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF46934; UBA_like; 1.
DR   PROSITE; PS50030; UBA; 2.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; 1.
DR   PROSITE; PS50235; UCH_2_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Disulfide bond; Hydrolase; Metal-binding; Phosphoprotein;
KW   Protease; Repeat; Thiol protease; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    858       Ubiquitin carboxyl-terminal hydrolase 5.
FT                                /FTId=PRO_0000080624.
FT   DOMAIN      654    695       UBA 1.
FT   DOMAIN      722    762       UBA 2.
FT   ZN_FING     197    269       UBP-type.
FT   REGION      221    224       Substrate binding (By similarity).
FT   ACT_SITE    335    335       Nucleophile (By similarity).
FT   ACT_SITE    818    818       Proton acceptor (By similarity).
FT   METAL       199    199       Zinc (By similarity).
FT   METAL       202    202       Zinc (By similarity).
FT   METAL       219    219       Zinc (By similarity).
FT   METAL       232    232       Zinc (By similarity).
FT   BINDING     209    209       Substrate (By similarity).
FT   BINDING     259    259       Substrate (By similarity).
FT   BINDING     261    261       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     264    264       Substrate (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     184    184       N6-acetyllysine (By similarity).
FT   MOD_RES     623    623       Phosphothreonine.
FT   MOD_RES     783    783       Phosphoserine (By similarity).
FT   DISULFID    195    816       By similarity.
SQ   SEQUENCE   858 AA;  95833 MW;  E1F31A0C92687CA8 CRC64;
     MAELSEEALL SVLPTIRVPK AGDRVHKDEC AFSFDTPESE GGLYICMNTF LGFGKQYVER
     HFNKTGQRVY LHLRRTRRPK EEDTSAGTGD PPRKKPTRLA IGVEGGFDLT EDKFEFDEDV
     KIVILPDYLE IARDGLGGLP DIVRDRVTSA VEALLSADSA SRKQEVQAWD GEVRQVSKHA
     FNLKQLDNPA RIPPCGWKCS KCDMRENLWL NLTDGSILCG RRYFDGSGGN NHAVEHYRET
     GYPLAVKLGT ITPDGADVYS YDEDDMVLDP SLAEHLSHFG IDMLKMQKTD KTMTELEIDM
     NQRIGEWELI QESGVPLKPL FGPGYTGIRN LGNSCYLNSV VQVLFSIPDF QRKYVDKLEK
     IFQNAPTDPT QDFSTQVAKL GHGLLSGEYS KPALESGDGE QVPEQKEVQD GIAPRMFKAL
     IGKGHPEFST NRQQDAQEFF LHLINMVERN CRSSENPNEV FRFLVEEKIK CLATEKVKYT
     QRVDYIMQLP VPMDAALNKE ELLEYEEKKR QAEEEKVPLP ELVRAQVPFS SCLEAYGAPE
     QVDDFWSTAL QAKSVAVKTT RFASFPDYLV IQIKKFTFGL DWVPKKLDVS IEMPEELDIS
     QLRGTGLQPG EEELPDIAPP LVTPDEPKGS LGFYGNEDED SFCSPHFSSP TSPMLDESVI
     IQLVEMGFPM DACRKAVYYT GNSGAEAAMN WVMSHMDDPD FANPLILPGS SGPGSTSAAA
     DPPPEDCVTT IVSMGFSRDQ ALKALRATNN SLERAVDWIF SHIDDLDAEA AMDISEGRSA
     AESISESVPV GPKVRDGPGK YQLFAFISHM GTSTMCGHYV CHIKKEGRWV IYNDQKVCAS
     EKPPKDLGYI YFYQRVVS
//
ID   CXCR7_MOUSE             Reviewed;         362 AA.
AC   P56485; Q91WI0;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=C-X-C chemokine receptor type 7;
DE            Short=CXC-R7;
DE            Short=CXCR-7;
DE   AltName: Full=Chemokine orphan receptor 1;
DE   AltName: Full=G-protein coupled receptor RDC1 homolog;
DE            Short=RDC-1;
GN   Name=Cxcr7; Synonyms=Cmkor1, Rdc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/SvJ; TISSUE=Peritoneal exudate;
RX   PubMed=9510554; DOI=10.1007/s002510050371;
RA   Heesen M., Berman M.A., Charest A., Housman D., Gerard C., Dorf M.E.;
RT   "Cloning and chromosomal mapping of an orphan chemokine receptor
RT   expressed in heart, spleen, kidney, astrocytes, and neutrophils.";
RL   Immunogenetics 47:364-370(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Forelimb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Receptor for CXCL12/SDF1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in heart, spleen, kidney,
CC       astrocytes, and neutrophils.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF000236; AAB71343.1; -; mRNA.
DR   EMBL; AK031100; BAC27252.1; -; mRNA.
DR   EMBL; BC015254; AAH15254.1; -; mRNA.
DR   IPI; IPI00331263; -.
DR   RefSeq; NP_031748.2; NM_007722.3.
DR   UniGene; Mm.6522; -.
DR   ProteinModelPortal; P56485; -.
DR   SMR; P56485; 34-359.
DR   STRING; P56485; -.
DR   PhosphoSite; P56485; -.
DR   PRIDE; P56485; -.
DR   Ensembl; ENSMUST00000065587; ENSMUSP00000069114; ENSMUSG00000044337.
DR   GeneID; 12778; -.
DR   KEGG; mmu:12778; -.
DR   UCSC; uc007bzh.1; mouse.
DR   CTD; 12778; -.
DR   MGI; MGI:109562; Cxcr7.
DR   eggNOG; roNOG13056; -.
DR   GeneTree; ENSGT00600000084327; -.
DR   HOGENOM; HBG447091; -.
DR   HOVERGEN; HBG106832; -.
DR   InParanoid; P56485; -.
DR   OMA; WVVSLVQ; -.
DR   OrthoDB; EOG45DWPR; -.
DR   PhylomeDB; P56485; -.
DR   NextBio; 282174; -.
DR   ArrayExpress; P56485; -.
DR   Bgee; P56485; -.
DR   CleanEx; MM_CXCR7; -.
DR   Genevestigator; P56485; -.
DR   GermOnline; ENSMUSG00000044337; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR001416; RDC1_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00646; RDC1ORPHANR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Receptor; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    362       C-X-C chemokine receptor type 7.
FT                                /FTId=PRO_0000070102.
FT   TOPO_DOM      1     47       Extracellular (Potential).
FT   TRANSMEM     48     68       Helical; Name=1; (Potential).
FT   TOPO_DOM     69     81       Cytoplasmic (Potential).
FT   TRANSMEM     82    102       Helical; Name=2; (Potential).
FT   TOPO_DOM    103    118       Extracellular (Potential).
FT   TRANSMEM    119    139       Helical; Name=3; (Potential).
FT   TOPO_DOM    140    162       Cytoplasmic (Potential).
FT   TRANSMEM    163    183       Helical; Name=4; (Potential).
FT   TOPO_DOM    184    213       Extracellular (Potential).
FT   TRANSMEM    214    234       Helical; Name=5; (Potential).
FT   TOPO_DOM    235    252       Cytoplasmic (Potential).
FT   TRANSMEM    253    273       Helical; Name=6; (Potential).
FT   TOPO_DOM    274    296       Extracellular (Potential).
FT   TRANSMEM    297    319       Helical; Name=7; (Potential).
FT   TOPO_DOM    320    362       Cytoplasmic (Potential).
FT   CARBOHYD     13     13       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     22     22       N-linked (GlcNAc...) (Potential).
FT   DISULFID    117    196       By similarity.
FT   CONFLICT     97     97       I -> T (in Ref. 1; AAB71343).
FT   CONFLICT    185    185       T -> A (in Ref. 1; AAB71343).
SQ   SEQUENCE   362 AA;  41636 MW;  7A0399DED5B73E66 CRC64;
     MDVHLFDYAE PGNYSDINWP CNSSDCIVVD TVQCPTMPNK NVLLYTLSFI YIFIFVIGMI
     ANSVVVWVNI QAKTTGYDTH CYILNLAIAD LWVVITIPVW VVSLVQHNQW PMGELTCKIT
     HLIFSINLFG SIFFLACMSV DRYLSITYFT GTSSYKKKMV RRVVCILVWL LAFFVSLPDT
     YYLKTVTSAS NNETYCRSFY PEHSIKEWLI GMELVSVILG FAVPFTIIAI FYFLLARAMS
     ASGDQEKHSS RKIIFSYVVV FLVCWLPYHF VVLLDIFSIL HYIPFTCQLE NVLFTALHVT
     QCLSLVHCCV NPVLYSFINR NYRYELMKAF IFKYSAKTGL TKLIDASRVS ETEYSALEQN
     TK
//
ID   EAA1_MOUSE              Reviewed;         543 AA.
AC   P56564; Q99P53;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 2.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Excitatory amino acid transporter 1;
DE   AltName: Full=Glial high affinity glutamate transporter;
DE   AltName: Full=High-affinity neuronal glutamate transporter;
DE   AltName: Full=Sodium-dependent glutamate/aspartate transporter 1;
DE            Short=GLAST-1;
DE   AltName: Full=Solute carrier family 1 member 3;
GN   Name=Slc1a3; Synonyms=Eaat1, Gmt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=94088939; PubMed=7903437; DOI=10.1016/0304-3940(93)90829-A;
RA   Tanaka K.;
RT   "Cloning and expression of a glutamate transporter from mouse brain.";
RL   Neurosci. Lett. 159:183-186(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Neural stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 80-114; 161-175; 189-196; 269-280 AND 480-499, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206; ASN-215 AND ASN-216,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
CC   -!- FUNCTION: Transports L-glutamate and also L- and D-aspartate.
CC       Essential for terminating the postsynaptic action of glutamate by
CC       rapidly removing released glutamate from the synaptic cleft. Acts
CC       as a symport by cotransporting sodium.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Localized in brain and is highly enriched in
CC       the Purkinje cell layer in cerebellum. Intermediate level in lung,
CC       low level in spleen, skeletal muscle and testis.
CC   -!- SIMILARITY: Belongs to the sodium:dicarboxylate (SDF) symporter
CC       (TC 2.A.23) family. SLC1A3 subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF330257; AAK01708.1; -; mRNA.
DR   EMBL; BC058711; AAH58711.1; -; mRNA.
DR   EMBL; BC066154; AAH66154.1; -; mRNA.
DR   IPI; IPI00114279; -.
DR   RefSeq; NP_683740.1; NM_148938.3.
DR   UniGene; Mm.204834; -.
DR   ProteinModelPortal; P56564; -.
DR   SMR; P56564; 50-497.
DR   STRING; P56564; -.
DR   PhosphoSite; P56564; -.
DR   PRIDE; P56564; -.
DR   Ensembl; ENSMUST00000005493; ENSMUSP00000005493; ENSMUSG00000005360.
DR   GeneID; 20512; -.
DR   KEGG; mmu:20512; -.
DR   UCSC; uc007vey.1; mouse.
DR   CTD; 20512; -.
DR   MGI; MGI:99917; Slc1a3.
DR   eggNOG; roNOG12449; -.
DR   HOGENOM; HBG739804; -.
DR   HOVERGEN; HBG000080; -.
DR   InParanoid; P56564; -.
DR   OMA; MGAVINN; -.
DR   OrthoDB; EOG46HG9R; -.
DR   PhylomeDB; P56564; -.
DR   NextBio; 298711; -.
DR   ArrayExpress; P56564; -.
DR   Bgee; P56564; -.
DR   Genevestigator; P56564; -.
DR   GermOnline; ENSMUSG00000005360; Mus musculus.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0043205; C:fibril; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0016595; F:glutamate binding; IDA:MGI.
DR   GO; GO:0005314; F:high-affinity glutamate transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0017153; F:sodium:dicarboxylate symporter activity; IEA:InterPro.
DR   GO; GO:0031223; P:auditory behavior; IMP:MGI.
DR   GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IMP:MGI.
DR   GO; GO:0021545; P:cranial nerve development; IMP:MGI.
DR   GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; IMP:MGI.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IMP:MGI.
DR   GO; GO:0051938; P:L-glutamate import; IMP:MGI.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR   GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:MGI.
DR   GO; GO:0046677; P:response to antibiotic; IMP:MGI.
DR   GO; GO:0042493; P:response to drug; IMP:MGI.
DR   GO; GO:0009416; P:response to light stimulus; IMP:MGI.
DR   GO; GO:0009611; P:response to wounding; IMP:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR   InterPro; IPR001991; Na-dicarboxylate_symporter.
DR   InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR   PANTHER; PTHR11958; Na/diCO_symport; 1.
DR   Pfam; PF00375; SDF; 1.
DR   PRINTS; PR00173; EDTRNSPORT.
DR   PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
DR   PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Membrane; Phosphoprotein;
KW   Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    543       Excitatory amino acid transporter 1.
FT                                /FTId=PRO_0000202058.
FT   TOPO_DOM      1     47       Cytoplasmic (Potential).
FT   TRANSMEM     48     68       Helical; (Potential).
FT   TRANSMEM     91    111       Helical; (Potential).
FT   TRANSMEM    123    145       Helical; (Potential).
FT   TOPO_DOM    146    237       Extracellular (Potential).
FT   TRANSMEM    238    260       Helical; (Potential).
FT   TRANSMEM    281    302       Helical; (Potential).
FT   TRANSMEM    319    340       Helical; (Potential).
FT   COMPBIAS    363    366       Poly-Ser.
FT   MOD_RES     512    512       Phosphoserine.
FT   CARBOHYD    206    206       N-linked (GlcNAc...).
FT   CARBOHYD    215    215       N-linked (GlcNAc...).
FT   CARBOHYD    216    216       N-linked (GlcNAc...).
SQ   SEQUENCE   543 AA;  59622 MW;  E0B24CBA1D5B086D CRC64;
     MTKSNGEEPR MGGRMERLQQ GVRKRTLLAK KKVQSLTKED VKSYLFRNAF VLLTVTAVIV
     GTILGFALRP YKMSYREVKY FSFPGELLMR MLQMLVLPLI ISSLVTGMAA LDSKASGKMG
     MRAVVYYMTT TIIAVVIGII IVIIIHPGKG TKENMYREGK IVQVTAADAF LDLIRNMFPP
     NLVEACFKQF KTSYEKRSFK VPIQSNETLL GAVINNVSEA METLTRIREE MVPVPGSVNG
     VNALGLVVFS MCFGFVIGNM KEQGQALREF FDSLNEAIMR LVAVIMWYAP LGILFLIAGK
     IVEMEDMGVI GGQLAMYTVT VIVGLLIHAV IVLPLLYFLV TRKNPWVFIG GLLQALITAL
     GTSSSSATLP ITFKCLEENN GVDKRITRFV LPVGATINMD GTALYEALAA IFIAQVNNFD
     LNFGQIITIS ITATAASIGA AGIPQAGLVT MVIVLTSVGL PTDDITLIIA VDWFLDRLRT
     TTNVLGDSLG AGIVEHLSRH ELKNRDVEMG NSVIEENEMK KPYQLIAQDN EPEKPVADSE
     TKM
//
ID   WFS1_MOUSE              Reviewed;         890 AA.
AC   P56695; Q9Z276;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Wolframin;
GN   Name=Wfs1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99036670; PubMed=9817917; DOI=10.1093/hmg/7.13.2021;
RA   Strom T.M., Hoertnagel K., Hofmann S., Gekeler F., Scharfe C.,
RA   Rabl W., Gerbitz K.-D., Meitinger T.;
RT   "Diabetes insipidus, diabetes mellitus, optic atrophy and deafness
RT   (DIDMOAD) caused by mutations in a novel gene (wolframin) coding for a
RT   predicted transmembrane protein.";
RL   Hum. Mol. Genet. 7:2021-2028(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Insulinoma;
RX   MEDLINE=98442649; PubMed=9771706; DOI=10.1038/2441;
RA   Inoue H., Tanizawa Y., Wasson J., Behn P., Kalidas K.,
RA   Bernal-Mizrachi E., Mueckler M., Marshall H., Donis-Keller H.,
RA   Crock P., Rogers D., Mikuni M., Kumashiro H., Higashi K., Sobue G.,
RA   Oka Y., Permutt M.A.;
RT   "A gene encoding a transmembrane protein is mutated in patients with
RT   diabetes mellitus and optic atrophy (Wolfram Syndrome).";
RL   Nat. Genet. 20:143-148(1998).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Participates in the regulation of cellular Ca(2+)
CC       homeostasis, at least partly, by modulating the filling state of
CC       the endoplasmic reticulum Ca(2+) store (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
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DR   EMBL; AJ011971; CAA09892.1; -; mRNA.
DR   EMBL; AF084482; AAC64944.1; -; mRNA.
DR   IPI; IPI00114833; -.
DR   RefSeq; NP_035846.1; NM_011716.2.
DR   UniGene; Mm.20916; -.
DR   ProteinModelPortal; P56695; -.
DR   STRING; P56695; -.
DR   PhosphoSite; P56695; -.
DR   PRIDE; P56695; -.
DR   Ensembl; ENSMUST00000043964; ENSMUSP00000048053; ENSMUSG00000039474.
DR   GeneID; 22393; -.
DR   KEGG; mmu:22393; -.
DR   UCSC; uc008xff.1; mouse.
DR   CTD; 22393; -.
DR   MGI; MGI:1328355; Wfs1.
DR   eggNOG; roNOG08427; -.
DR   HOGENOM; HBG444131; -.
DR   HOVERGEN; HBG014957; -.
DR   InParanoid; P56695; -.
DR   OMA; ESAINML; -.
DR   OrthoDB; EOG44BB1V; -.
DR   PhylomeDB; P56695; -.
DR   NextBio; 302771; -.
DR   ArrayExpress; P56695; -.
DR   Bgee; P56695; -.
DR   CleanEx; MM_WFS1; -.
DR   Genevestigator; P56695; -.
DR   GermOnline; ENSMUSG00000039474; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051117; F:ATPase binding; IDA:BHF-UCL.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    890       Wolframin.
FT                                /FTId=PRO_0000065964.
FT   TRANSMEM    314    334       Helical; (Potential).
FT   TRANSMEM    340    360       Helical; (Potential).
FT   TRANSMEM    402    422       Helical; (Potential).
FT   TRANSMEM    427    447       Helical; (Potential).
FT   TRANSMEM    465    485       Helical; (Potential).
FT   TRANSMEM    496    516       Helical; (Potential).
FT   TRANSMEM    529    549       Helical; (Potential).
FT   TRANSMEM    563    583       Helical; (Potential).
FT   TRANSMEM    589    609       Helical; (Potential).
FT   TRANSMEM    632    652       Helical; (Potential).
FT   TRANSMEM    870    890       Helical; (Potential).
FT   COMPBIAS     13     21       Poly-Pro.
FT   COMPBIAS    191    194       Poly-Lys.
FT   COMPBIAS    877    886       Poly-Phe.
FT   MOD_RES      32     32       Phosphoserine.
FT   CONFLICT    215    215       A -> V (in Ref. 2; AAC64944).
SQ   SEQUENCE   890 AA;  100579 MW;  CB6C6CA16171A942 CRC64;
     MNSGTPPPSP SGPPPPPAPQ PQARARLNAT ASLEQDKIEP PRAPRPQADP SAGRSAGEAA
     APEPRAPQTG SREETDRAGP MKADVEIPFE EVLEKAKAGD PKAQTEVGKH YLRLANDADE
     ELNSCSAVAW LILAAKQGRR EAVKLLRRCL ADRKGITSEN EAEVKQLSSE TDLERAVRKA
     ALVMYWKLNP KKKKQVAVSE LLENVGQVNE QDGGAQPGPV PKSLQKQRRM LERLVSSESK
     NYIALDDFVE LTKKYAKGII PTNLFLQDED EDEDELAGKS PEDLPLRQKV VKYPLHAIME
     IKEYLIDVAS KAGMHWLSTI VPTHHINALI FFFIISNLTI DFFAFFIPLV VFYLSFVSMV
     ICTLKVFQDS KAWENFRTLT DLLLRFEPNL DVEQAEVNFG WNHLEPYIHF LLSVVFVIFS
     FPLASKDCIP CSELAVISTF FTVTSYMSLS SSAEPYTRRA LVTEVAAGLL SLLPTVPVDW
     RFLKVLGQTF FTVPVGHFII LNVSLPCLLY VYLFYLFFRM AQLRNFKGTY CYLVPYLVCF
     MWCELSVVIL LQSTGLGLVR ASIGYFLFLF ALPILVAGLA LMGTVQFARW FLSLDLTKIM
     VTTVICGVPL LFRWWTKANF SVMGMVKSLT KSSMVKLILV WLTAILLFCW FYVYRSEGMK
     VYNSTLTWQQ YGFLCGPRAW KETNMARTQI LCSHLEGHRV TWTGRFKYVR VTEIDNSAES
     AINMLPFFLG DWMRCLYGEA YPSCSSGNTS TAEEELCRLK QLAKHPCHIK KFDRYKFEIT
     VGMPFGTNGN RGHEEDDITK DIVLRASSEF KDVLLNLRQG SLIEFSTILE GRLGSKWPVF
     ELKAISCLNC MTQLSPARRH VKIEQDWRST VHGALKFAFD FFFFPFLSAA
//
ID   SMO_MOUSE               Reviewed;         793 AA.
AC   P56726;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Smoothened homolog;
DE            Short=SMO;
DE   Flags: Precursor;
GN   Name=Smo; Synonyms=Smoh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=97339452; PubMed=9196051; DOI=10.1006/bbrc.1997.6750;
RA   Akiyama H., Shigeno C., Hiraki Y., Shukunami C., Kohno H., Akagi M.,
RA   Konishi J., Nakamura T.;
RT   "Cloning of a mouse Smoothened cDNA and expression patterns of
RT   hedgehog signalling molecules during chondrogenesis and cartilage
RT   differentiation in clonal mouse EC cells, ATDC5.";
RL   Biochem. Biophys. Res. Commun. 235:142-147(1997).
RN   [2]
RP   INTERACTION WITH ARRB2.
RX   PubMed=15618519; DOI=10.1126/science.1104135;
RA   Chen W., Ren X.R., Nelson C.D., Barak L.S., Chen J.K., Beachy P.A.,
RA   de Sauvage F., Lefkowitz R.J.;
RT   "Activity-dependent internalization of smoothened mediated by beta-
RT   arrestin 2 and GRK2.";
RL   Science 306:2257-2260(2004).
CC   -!- FUNCTION: G protein-coupled receptor that probably associates with
CC       the patched protein (PTCH) to transduce the hedgehog's proteins
CC       signal. Binding of sonic hedgehog (SHH) to its receptor patched is
CC       thought to prevent normal inhibition by patched of smoothened
CC       (SMO). Required for the accumulation of KIF7 and GLI3 in the cilia
CC       (By similarity).
CC   -!- SUBUNIT: Interacts with ARRB2. Interacts with KIF7 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo
CC       family.
CC   -!- SIMILARITY: Contains 1 FZ (frizzled) domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   IPI; IPI00341032; -.
DR   PIR; JC5539; JC5539.
DR   UniGene; Mm.29279; -.
DR   ProteinModelPortal; P56726; -.
DR   SMR; P56726; 72-182.
DR   STRING; P56726; -.
DR   PhosphoSite; P56726; -.
DR   PRIDE; P56726; -.
DR   Ensembl; ENSMUST00000001812; ENSMUSP00000001812; ENSMUSG00000001761.
DR   MGI; MGI:108075; Smo.
DR   eggNOG; roNOG05761; -.
DR   HOGENOM; HBG714469; -.
DR   HOVERGEN; HBG000352; -.
DR   InParanoid; P56726; -.
DR   OrthoDB; EOG4Q2DDX; -.
DR   ArrayExpress; P56726; -.
DR   Bgee; P56726; -.
DR   CleanEx; MM_SMO; -.
DR   Genevestigator; P56726; -.
DR   GermOnline; ENSMUSG00000001761; Mus musculus.
DR   GO; GO:0005929; C:cilium; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0001708; P:cell fate specification; IMP:MGI.
DR   GO; GO:0021953; P:central nervous system neuron differentiation; IMP:MGI.
DR   GO; GO:0021696; P:cerebellar cortex morphogenesis; IMP:MGI.
DR   GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR   GO; GO:0048589; P:developmental growth; IMP:MGI.
DR   GO; GO:0021904; P:dorsal/ventral neural tube patterning; IMP:MGI.
DR   GO; GO:0060684; P:epithelial-mesenchymal cell signaling; IMP:MGI.
DR   GO; GO:0003007; P:heart morphogenesis; IGI:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IGI:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptosis; IMP:MGI.
DR   GO; GO:0043392; P:negative regulation of DNA binding; IGI:MGI.
DR   GO; GO:0010553; P:negative regulation of gene-specific transcription from RNA polymerase II promoter; IMP:MGI.
DR   GO; GO:0001755; P:neural crest cell migration; IGI:MGI.
DR   GO; GO:0042475; P:odontogenesis of dentine-containing tooth; IMP:MGI.
DR   GO; GO:0001649; P:osteoblast differentiation; IMP:MGI.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:MGI.
DR   GO; GO:0010552; P:positive regulation of gene-specific transcription from RNA polymerase II promoter; IMP:MGI.
DR   GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:MGI.
DR   GO; GO:0002052; P:positive regulation of neuroblast proliferation; IGI:MGI.
DR   GO; GO:0042307; P:positive regulation of protein import into nucleus; IGI:MGI.
DR   GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:MGI.
DR   GO; GO:0050821; P:protein stabilization; IDA:MGI.
DR   GO; GO:0021938; P:smoothened signaling pathway involved in regulation of cerebellar granule cell precursor cell proliferation; IMP:MGI.
DR   GO; GO:0021910; P:smoothened signaling pathway involved in ventral spinal cord patterning; IMP:MGI.
DR   GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR   InterPro; IPR000539; Frizzled.
DR   InterPro; IPR015526; Frizzled-related.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR017981; GPCR_2-like.
DR   Gene3D; G3DSA:1.10.2000.10; Frizzled_Cys-rich; 1.
DR   PANTHER; PTHR11309; Fz_related; 1.
DR   Pfam; PF01534; Frizzled; 1.
DR   Pfam; PF01392; Fz; 1.
DR   PRINTS; PR00489; FRIZZLED.
DR   SMART; SM00063; FRI; 1.
DR   SUPFAM; SSF63501; Frizzled_Cys-rich; 1.
DR   PROSITE; PS50038; FZ; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Phosphoprotein; Receptor; Signal; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     32       Potential.
FT   CHAIN        33    793       Smoothened homolog.
FT                                /FTId=PRO_0000013016.
FT   TOPO_DOM     33    237       Extracellular (Potential).
FT   TRANSMEM    238    258       Helical; Name=1; (Potential).
FT   TOPO_DOM    259    265       Cytoplasmic (Potential).
FT   TRANSMEM    266    286       Helical; Name=2; (Potential).
FT   TOPO_DOM    287    318       Extracellular (Potential).
FT   TRANSMEM    319    339       Helical; Name=3; (Potential).
FT   TOPO_DOM    340    362       Cytoplasmic (Potential).
FT   TRANSMEM    363    383       Helical; Name=4; (Potential).
FT   TOPO_DOM    384    406       Extracellular (Potential).
FT   TRANSMEM    407    427       Helical; Name=5; (Potential).
FT   TOPO_DOM    428    455       Cytoplasmic (Potential).
FT   TRANSMEM    456    476       Helical; Name=6; (Potential).
FT   TOPO_DOM    477    528       Extracellular (Potential).
FT   TRANSMEM    529    549       Helical; Name=7; (Potential).
FT   TOPO_DOM    550    793       Cytoplasmic (Potential).
FT   DOMAIN       69    185       FZ.
FT   MOD_RES     791    791       Phosphoserine (By similarity).
FT   CARBOHYD     38     38       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    192    192       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    497    497       N-linked (GlcNAc...) (Potential).
FT   DISULFID     74    138       By similarity.
FT   DISULFID     82    131       By similarity.
FT   DISULFID    122    158       By similarity.
FT   DISULFID    151    173       By similarity.
SQ   SEQUENCE   793 AA;  87300 MW;  10B2767876171167 CRC64;
     MAAGRPVRGP ELAPRRLLQL LLLVLLGGPG RGAALSGNVT GPGPHSASGS SRRNVPVTSP
     PPPLLSHCGR AAHCEPLRYN VCLGSALPYG ATTTLLAGDS DSQEEAHGKL VLWSGLRNAP
     RCWAVIQPLL CAVYMPKCEN DRVELPSRTL CQATRGPCAI VERERGWPDF LRCTPDHFPE
     GCPNEVQNIK FNSSGQCEAP LVRTDNPKSW YEDVEGCGIQ CQNPLFTEAE HQDMHSYIAA
     FGAVTGLCTL FTLATFVADW RNSNRLPAVI LFYVNACFFV GSIGWLAQFM DGARREIVCR
     ADGTMRFGEP TSSETLSCVI IFVIVYYALM AGVVWFVVLT YAWHTSFKAL GTTYQPLSGK
     TSYFHLLTWS LPFVLTVAIL AVAQVDGDSV SGICFVGYKN YRYRAGFVLA PIGLVLIVGG
     YFLIRGVMTL FSIKSNHPGL LSEKAASKIN ETMLRLGIFG FLAFGFVLIT FSCHFYDFFN
     QAEWERSFRD YVLCQANVTI GLPTKKPIPD CEIKNRPSLL VEKINLFAMF GTGIAMSTWV
     WTKATLLIWR RTWCRLTGHS DDEPKRIKKS KMIAKAFSKR RELLQNPGQE LSFSMHTVSH
     DGPVAGLAFD LNEPSADVSS AWAQHVTKMV ARRGAILPQD VSVTPVATPV PPEEQANMWL
     VEAEISPELE KRLGRKKKRR KRKKEVCPLG PAPELHHSAP VPATSAVPRL PQLPRQKCLV
     AANAWGTGES CRQGAWTLVS NPFCPEPSPH QDPFLPGASA PRVWAQGRLQ GLGSIHSRTN
     LMEAEILDAD SDF
//
ID   PDCD5_MOUSE             Reviewed;         126 AA.
AC   P56812;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Programmed cell death protein 5;
DE   AltName: Full=TF-1 cell apoptosis-related protein 19;
DE            Short=Protein TFAR19;
GN   Name=Pdcd5; Synonyms=Tfar19;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Heart;
RX   MEDLINE=99121216; PubMed=9920759; DOI=10.1006/bbrc.1998.9893;
RA   Liu H.T., Wang Y.G., Zhang Y.M., Song Q.S., Di C.H., Chen G., Tang J.,
RA   Ma D.L.;
RT   "TFAR19, a novel apoptosis-related gene cloned from human leukemia
RT   cell line TF-1, could enhance apoptosis of some tumor cells induced by
RT   growth factor withdrawal.";
RL   Biochem. Biophys. Res. Commun. 254:203-210(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: May function in the process of apoptosis (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- SIMILARITY: Belongs to the PDCD5 family.
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DR   EMBL; AF161074; AAD45607.1; -; mRNA.
DR   EMBL; BC048476; AAH48476.1; -; mRNA.
DR   EMBL; BC056167; AAH56167.1; -; mRNA.
DR   IPI; IPI00116120; -.
DR   RefSeq; NP_062720.1; NM_019746.4.
DR   RefSeq; XP_001478306.1; XM_001478256.2.
DR   RefSeq; XP_003086241.1; XM_003086193.1.
DR   UniGene; Mm.371609; -.
DR   UniGene; Mm.440265; -.
DR   ProteinModelPortal; P56812; -.
DR   SMR; P56812; 8-113.
DR   STRING; P56812; -.
DR   PhosphoSite; P56812; -.
DR   PRIDE; P56812; -.
DR   Ensembl; ENSMUST00000118501; ENSMUSP00000113761; ENSMUSG00000030417.
DR   GeneID; 100042424; -.
DR   GeneID; 56330; -.
DR   KEGG; mmu:100042424; -.
DR   KEGG; mmu:56330; -.
DR   UCSC; uc009gkf.1; mouse.
DR   CTD; 56330; -.
DR   MGI; MGI:1913538; Pdcd5.
DR   eggNOG; roNOG17792; -.
DR   HOVERGEN; HBG053536; -.
DR   OrthoDB; EOG4BCDPG; -.
DR   NextBio; 453703; -.
DR   ArrayExpress; P56812; -.
DR   Bgee; P56812; -.
DR   CleanEx; MM_PDCD5; -.
DR   Genevestigator; P56812; -.
DR   GermOnline; ENSMUSG00000030417; Mus musculus.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   InterPro; IPR002836; TFAR19_DNA-bd.
DR   Gene3D; G3DSA:1.10.8.140; TFAR19_DNA_bd; 1.
DR   PANTHER; PTHR10840; TFAR19_DNA_bd; 1.
DR   Pfam; PF01984; dsDNA_bind; 1.
DR   PIRSF; PIRSF015730; TFAR19; 1.
DR   SUPFAM; SSF46950; TFAR19-related; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    126       Programmed cell death protein 5.
FT                                /FTId=PRO_0000121546.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      63     63       N6-acetyllysine (By similarity).
FT   MOD_RES     119    119       Phosphoserine.
SQ   SEQUENCE   126 AA;  14275 MW;  05796820CD5C780B CRC64;
     MADEELEALR KQRLAELQAK HGDPGDAAQQ EAKQREAEMR NSILAQVLDQ SARARLSNLA
     LVKPEKTKAV ENYLIQMARY GQLSGKVSEQ GLIEILEKVS QQTEKKTTVK FNRRKVMDSD
     EDDADY
//
ID   BACE1_MOUSE             Reviewed;         501 AA.
AC   P56818; Q544D0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   08-MAR-2011, entry version 101.
DE   RecName: Full=Beta-secretase 1;
DE            EC=3.4.23.46;
DE   AltName: Full=Aspartyl protease 2;
DE            Short=ASP2;
DE            Short=Asp 2;
DE   AltName: Full=Beta-site amyloid precursor protein cleaving enzyme 1;
DE            Short=Beta-site APP cleaving enzyme 1;
DE   AltName: Full=Memapsin-2;
DE   AltName: Full=Membrane-associated aspartic protease 2;
DE   Flags: Precursor;
GN   Name=Bace1; Synonyms=Bace;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20002972; PubMed=10531052; DOI=10.1126/science.286.5440.735;
RA   Vassar R., Bennett B.D., Babu-Khan S., Kahn S., Mendiaz E.A.,
RA   Denis P., Teplow D.B., Ross S., Amarante P., Loeloff R., Luo Y.,
RA   Fisher S., Fuller J., Edenson S., Lile J., Jarosinski M.A.,
RA   Biere A.L., Curran E., Burgess T., Louis J.-C., Collins F.,
RA   Treanor J., Rogers G., Citron M.;
RT   "Beta-secretase cleavage of Alzheimer's amyloid precursor protein by
RT   the transmembrane aspartic protease BACE.";
RL   Science 286:735-741(1999).
RN   [2]
RP   SEQUENCE REVISION TO 6 AND 81-87.
RA   Bennett B.D., Vassar R., Citron M.;
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20057170; PubMed=10591213; DOI=10.1038/990107;
RA   Yan R., Bienkowski M.J., Shuck M.E., Miao H., Tory M.C., Pauley A.M.,
RA   Brashier J.R., Stratman N.C., Mathews W.R., Buhl A.E., Carter D.B.,
RA   Tomasselli A.G., Parodi L.A., Heinrikson R.L., Gurney M.E.;
RT   "Membrane-anchored aspartyl protease with Alzheimer's disease beta-
RT   secretase activity.";
RL   Nature 402:533-537(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Aorta, Head, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 301-307, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=15987683; DOI=10.1074/jbc.M505249200;
RA   Dominguez D., Tournoy J., Hartmann D., Huth T., Cryns K., Deforce S.,
RA   Serneels L., Camacho I.E., Marjaux E., Craessaerts K.,
RA   Roebroek A.J.M., Schwake M., D'Hooge R., Bach P., Kalinke U.,
RA   Moechars D., Alzheimer C., Reiss K., Saftig P., De Strooper B.;
RT   "Phenotypic and biochemical analyses of BACE1- and BACE2-deficient
RT   mice.";
RL   J. Biol. Chem. 280:30797-30806(2005).
CC   -!- FUNCTION: Responsible for the proteolytic processing of the
CC       amyloid precursor protein (APP). Cleaves at the N-terminus of the
CC       A-beta peptide sequence, between residues 671 and 672 of APP,
CC       leads to the generation and extracellular release of beta-cleaved
CC       soluble APP, and a corresponding cell-associated C-terminal
CC       fragment which is later released by gamma-secretase (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Broad endopeptidase specificity. Cleaves Glu-
CC       Val-Asn-Leu-|-Asp-Ala-Glu-Phe in the Swedish variant of
CC       Alzheimer's amyloid precursor protein.
CC   -!- ENZYME REGULATION: Inhibited by RTN3 and RTN4 (By similarity).
CC   -!- SUBUNIT: Monomer. Interacts with GGA1, GGA2 and GGA3. Interacts
CC       with RTN3 and RTN4. Interacts with SNX6 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein. Golgi apparatus, trans-Golgi network (By similarity).
CC       Endoplasmic reticulum (By similarity). Endosome (By similarity).
CC       Cell surface (By similarity). Cytoplasmic vesicle membrane (By
CC       similarity). Note=Predominantly localized to the later
CC       Golgi/trans-Golgi network (TGN) and minimally detectable in the
CC       early Golgi compartments. A small portion is also found in the
CC       endoplasmic reticulum, endosomes and on the cell surface (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Brain.
CC   -!- DOMAIN: The transmembrane domain is necessary for its activity. It
CC       determines its late Golgi localization and access to its
CC       substrate, APP (By similarity).
CC   -!- PTM: Glycosylated (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice show a higher mortality rate early in
CC       life.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
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DR   EMBL; AF190726; AAF04143.2; -; mRNA.
DR   EMBL; AF200346; AAF17082.1; -; mRNA.
DR   EMBL; AK014464; BAB29370.1; -; mRNA.
DR   EMBL; AK033112; BAC28156.1; -; mRNA.
DR   EMBL; AK041285; BAC30889.1; -; mRNA.
DR   EMBL; BC048189; AAH48189.1; -; mRNA.
DR   IPI; IPI00116121; -.
DR   RefSeq; NP_001139419.1; NM_001145947.1.
DR   RefSeq; NP_035922.4; NM_011792.5.
DR   UniGene; Mm.24044; -.
DR   ProteinModelPortal; P56818; -.
DR   SMR; P56818; 53-447.
DR   STRING; P56818; -.
DR   MEROPS; A01.004; -.
DR   PhosphoSite; P56818; -.
DR   PRIDE; P56818; -.
DR   Ensembl; ENSMUST00000034591; ENSMUSP00000034591; ENSMUSG00000032086.
DR   GeneID; 23821; -.
DR   KEGG; mmu:23821; -.
DR   UCSC; uc009pgh.1; mouse.
DR   CTD; 23821; -.
DR   MGI; MGI:1346542; Bace1.
DR   eggNOG; roNOG14885; -.
DR   HOGENOM; HBG714116; -.
DR   HOVERGEN; HBG059578; -.
DR   InParanoid; P56818; -.
DR   OMA; SFVEMVD; -.
DR   PhylomeDB; P56818; -.
DR   BRENDA; 3.4.23.46; 244.
DR   ArrayExpress; P56818; -.
DR   Bgee; P56818; -.
DR   CleanEx; MM_BACE1; -.
DR   Genevestigator; P56818; -.
DR   GermOnline; ENSMUSG00000032086; Mus musculus.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0050435; P:beta-amyloid metabolic process; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR   InterPro; IPR009119; Pept_A1_BACE.
DR   InterPro; IPR009120; Pept_A1_BACE1.
DR   InterPro; IPR001461; Peptidase_A1.
DR   InterPro; IPR021109; Peptidase_aspartic.
DR   InterPro; IPR001969; Peptidase_aspartic_AS.
DR   InterPro; IPR009007; Peptidase_aspartic_catalytic.
DR   Gene3D; G3DSA:2.40.70.10; Pept_Aspartc_cat; 2.
DR   PANTHER; PTHR13683; Peptidase_A1; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR01816; BACE1.
DR   PRINTS; PR01815; BACEFAMILY.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Pept_Aspartic; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Aspartyl protease; Cytoplasmic vesicle; Direct protein sequencing;
KW   Disulfide bond; Endoplasmic reticulum; Endosome; Glycoprotein;
KW   Golgi apparatus; Hydrolase; Membrane; Protease; Signal; Transmembrane;
KW   Transmembrane helix; Zymogen.
FT   SIGNAL        1     21       Potential.
FT   PROPEP       22     45       Potential.
FT                                /FTId=PRO_0000025941.
FT   CHAIN        46    501       Beta-secretase 1.
FT                                /FTId=PRO_0000025942.
FT   TOPO_DOM     22    457       Extracellular (Potential).
FT   TRANSMEM    458    478       Helical; (Potential).
FT   TOPO_DOM    479    501       Cytoplasmic (Potential).
FT   REGION      479    501       Interaction with RTN3 (By similarity).
FT   ACT_SITE     93     93       By similarity.
FT   ACT_SITE    289    289       By similarity.
FT   CARBOHYD    153    153       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    172    172       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    223    223       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    354    354       N-linked (GlcNAc...) (Potential).
FT   DISULFID    216    420       By similarity.
FT   DISULFID    278    443       By similarity.
FT   DISULFID    330    380       By similarity.
SQ   SEQUENCE   501 AA;  55748 MW;  C085A013145E474E CRC64;
     MAPALHWLLL WVGSGMLPAQ GTHLGIRLPL RSGLAGPPLG LRLPRETDEE SEEPGRRGSF
     VEMVDNLRGK SGQGYYVEMT VGSPPQTLNI LVDTGSSNFA VGAAPHPFLH RYYQRQLSST
     YRDLRKGVYV PYTQGKWEGE LGTDLVSIPH GPNVTVRANI AAITESDKFF INGSNWEGIL
     GLAYAEIARP DDSLEPFFDS LVKQTHIPNI FSLQLCGAGF PLNQTEALAS VGGSMIIGGI
     DHSLYTGSLW YTPIRREWYY EVIIVRVEIN GQDLKMDCKE YNYDKSIVDS GTTNLRLPKK
     VFEAAVKSIK AASSTEKFPD GFWLGEQLVC WQAGTTPWNI FPVISLYLMG EVTNQSFRIT
     ILPQQYLRPV EDVATSQDDC YKFAVSQSST GTVMGAVIME GFYVVFDRAR KRIGFAVSAC
     HVHDEFRTAA VEGPFVTADM EDCGYNIPQT DESTLMTIAY VMAAICALFM LPLCLMVCQW
     RCLRCLRHQH DDFADDISLL K
//
ID   NPY_MOUSE               Reviewed;          97 AA.
AC   P57774; Q925V2; Q9ET27;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Neuropeptide Y;
DE   Contains:
DE     RecName: Full=Neuropeptide Y;
DE     AltName: Full=Neuropeptide tyrosine;
DE              Short=NPY;
DE   Contains:
DE     RecName: Full=C-flanking peptide of NPY;
DE              Short=CPON;
DE   Flags: Precursor;
GN   Name=Npy;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Hennessey K., Chua S. Jr.;
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-89.
RC   STRAIN=NZO, and SM/J; TISSUE=Brain;
RX   MEDLINE=21077529; PubMed=11210195; DOI=10.1007/s003350010254;
RA   Taylor B.A., Wnek C., Schroeder D., Phillips S.J.;
RT   "Multiple obesity QTLs identified in an intercross between the NZO
RT   (New Zealand obese) and the SM (small) mouse strains.";
RL   Mamm. Genome 12:95-103(2001).
CC   -!- FUNCTION: NPY is implicated in the control of feeding and in
CC       secretion of gonadotrophin-release hormone (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: One of the most abundant peptides in the
CC       nervous system. Also found in some chromaffin cells of the adrenal
CC       medulla.
CC   -!- SIMILARITY: Belongs to the NPY family.
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DR   EMBL; AF273768; AAG00945.1; -; mRNA.
DR   EMBL; AK002982; BAB22495.1; -; mRNA.
DR   EMBL; BC043012; AAH43012.1; -; mRNA.
DR   EMBL; AF286198; AAG01330.1; -; mRNA.
DR   EMBL; AF286199; AAG01331.1; -; mRNA.
DR   IPI; IPI00118874; -.
DR   RefSeq; NP_075945.1; NM_023456.2.
DR   UniGene; Mm.154796; -.
DR   ProteinModelPortal; P57774; -.
DR   SMR; P57774; 29-64.
DR   STRING; P57774; -.
DR   PRIDE; P57774; -.
DR   Ensembl; ENSMUST00000031843; ENSMUSP00000031843; ENSMUSG00000029819.
DR   GeneID; 109648; -.
DR   KEGG; mmu:109648; -.
DR   UCSC; uc009bwt.1; mouse.
DR   CTD; 109648; -.
DR   MGI; MGI:97374; Npy.
DR   eggNOG; maNOG21072; -.
DR   GeneTree; ENSGT00390000010775; -.
DR   HOGENOM; HBG716011; -.
DR   HOVERGEN; HBG006485; -.
DR   InParanoid; P57774; -.
DR   OMA; PRSRFED; -.
DR   OrthoDB; EOG4PVP19; -.
DR   PhylomeDB; P57774; -.
DR   NextBio; 362501; -.
DR   ArrayExpress; P57774; -.
DR   Bgee; P57774; -.
DR   CleanEx; MM_NPY; -.
DR   Genevestigator; P57774; -.
DR   GermOnline; ENSMUSG00000029819; Mus musculus.
DR   GO; GO:0005615; C:extracellular space; ISS:HGNC.
DR   GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR   GO; GO:0008343; P:adult feeding behavior; ISS:HGNC.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0032100; P:positive regulation of appetite; ISS:HGNC.
DR   InterPro; IPR001955; Pancreatic_hormone-like.
DR   InterPro; IPR020392; Pancreatic_hormone-like_CS.
DR   PANTHER; PTHR10533; Pancreatic_hormone; 1.
DR   Pfam; PF00159; Hormone_3; 1.
DR   PRINTS; PR00278; PANCHORMONE.
DR   ProDom; PD001267; Pancreatic_hormone-like; 1.
DR   SMART; SM00309; PAH; 1.
DR   PROSITE; PS00265; PANCREATIC_HORMONE_1; 1.
DR   PROSITE; PS50276; PANCREATIC_HORMONE_2; 1.
PE   2: Evidence at transcript level;
KW   Amidation; Cleavage on pair of basic residues; Neuropeptide; Secreted;
KW   Signal.
FT   SIGNAL        1     28       By similarity.
FT   PEPTIDE      29     64       Neuropeptide Y.
FT                                /FTId=PRO_0000025325.
FT   PEPTIDE      68     97       C-flanking peptide of NPY.
FT                                /FTId=PRO_0000025326.
FT   MOD_RES      64     64       Tyrosine amide (By similarity).
FT   CONFLICT     42     42       A -> R (in Ref. 4; AAG01330/AAG01331).
SQ   SEQUENCE   97 AA;  10874 MW;  7E0CE28FA330844E CRC64;
     MLGNKRMGLC GLTLALSLLV CLGILAEGYP SKPDNPGEDA PAEDMARYYS ALRHYINLIT
     RQRYGKRSSP ETLISDLLMK ESTENAPRTR LEDPSMW
//
ID   RASA2_MOUSE             Reviewed;         848 AA.
AC   P58069;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   04-MAY-2001, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Ras GTPase-activating protein 2;
DE   AltName: Full=GAP1m;
GN   Name=Rasa2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS.
RC   TISSUE=Brain;
RX   MEDLINE=96324967; PubMed=8702543; DOI=10.1074/jbc.271.31.18838;
RA   Fukuda M., Mikoshiba K.;
RT   "Structure-function relationships of the mouse Gap1m: determination of
RT   the inositol 1,3,4,5-tetrakisphosphate-binding domain.";
RL   J. Biol. Chem. 271:18838-18842(1996).
CC   -!- FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway.
CC       Binds inositol tetrakisphosphate (IP4) and phospholipids.
CC   -!- SUBCELLULAR LOCATION: Cell membrane (Potential).
CC   -!- SIMILARITY: Contains 1 Btk-type zinc finger.
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 Ras-GAP domain.
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DR   EMBL; AB056433; BAB32975.1; -; mRNA.
DR   IPI; IPI00115943; -.
DR   UniGene; Mm.124502; -.
DR   ProteinModelPortal; P58069; -.
DR   SMR; P58069; 38-597, 601-741.
DR   STRING; P58069; -.
DR   PhosphoSite; P58069; -.
DR   PRIDE; P58069; -.
DR   Ensembl; ENSMUST00000034984; ENSMUSP00000034984; ENSMUSG00000032413.
DR   UCSC; uc009rcn.1; mouse.
DR   MGI; MGI:2149960; Rasa2.
DR   eggNOG; roNOG12031; -.
DR   HOGENOM; HBG355134; -.
DR   HOVERGEN; HBG055643; -.
DR   InParanoid; P58069; -.
DR   OrthoDB; EOG4MSCXJ; -.
DR   ArrayExpress; P58069; -.
DR   Bgee; P58069; -.
DR   CleanEx; MM_RASA2; -.
DR   Genevestigator; P58069; -.
DR   GermOnline; ENSMUSG00000032413; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001936; RasGAP.
DR   InterPro; IPR023152; RasGAP_CS.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR001562; Znf_Btk_motif.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.10.506.10; RasGAP; 1.
DR   Pfam; PF00779; BTK; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00616; RasGAP; 1.
DR   PRINTS; PR00402; TECBTKDOMAIN.
DR   SMART; SM00107; BTK; 1.
DR   SMART; SM00239; C2; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00323; RasGAP; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR   PROSITE; PS51113; ZF_BTK; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; GTPase activation; Membrane;
KW   Metal-binding; Repeat; Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    848       Ras GTPase-activating protein 2.
FT                                /FTId=PRO_0000056639.
FT   DOMAIN       25    122       C2 1.
FT   DOMAIN      158    273       C2 2.
FT   DOMAIN      356    550       Ras-GAP.
FT   DOMAIN      604    705       PH.
FT   ZN_FING     707    743       Btk-type.
FT   COMPBIAS      1     22       Ala-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     208    208       N6-acetyllysine (By similarity).
FT   MOD_RES     209    209       N6-acetyllysine (By similarity).
FT   MOD_RES     211    211       N6-acetyllysine (By similarity).
FT   MOD_RES     213    213       N6-acetyllysine (By similarity).
FT   MUTAGEN     627    629       KKR->QQQ: No binding to IP4, reduced
FT                                binding to phospholipids.
FT   MUTAGEN     629    629       R->C: Greatly reduced binding to IP4 and
FT                                to phospholipids.
SQ   SEQUENCE   848 AA;  96472 MW;  8F1DCCD5D59108B5 CRC64;
     MAAAAPAAAA ASPEAPAVSG SADPETGDED SREVRVLQSL RGRIYEAKNL LPYLGPNKMR
     DCFCTINLDQ EEVYRTQVVE KSLSPYFSEE FYFEIPRTFQ YLSFYVYDKN VLQRDLRIGK
     VAIKKEDLCS HSGKETWFSL QPIDSNSEVQ GKVHLELRLN ELITENGTVC QQLVVHIKAC
     HGLPLINGQS CDPYATVSLV GPSRNDQKKT KVKKKTSNPQ FNEVFYFEVT RSSSYSRKSQ
     FQVEEEDIEK LEIRIDLWNN ENLVQDVFLG EIKVPVNVLR SDSFHQAWYL LQPRDNGNKS
     SKTDDLGSLL LTLCYTEDCV LPSEYYGPLK TLLLKSPDVQ PVSASAAYIL GEICQDQKDA
     VLPLVRLLLH HNKLVPFITA VAELDLKDTP DANAIFRGNS LATQCLTEMM KIVGGHYLKV
     TLKPVLDEIC ESSKSCEIDP VKLKEGDNVE NNKENLYYYV DKVFNTIVGS SVSCPTVMCD
     IFYSLRQMAA KKFPNHPHVQ YSAVSSFVFL RFFAVAILSP HAFHLRPHYP DTQTVRTLTL
     ISKTIQIIGN WGCQSRKKSR FKKSVMCEFL KMFQEERYFT DVKKFLDEIS STETKESSGT
     SEPVHLKEGE MYKRAQGRTR IGKKNFKKRW FCLTSRELTY HRQQGKDAIY TIPVKNILAV
     EKLEEGSFNK KNMFQVIHTE KTLYIQANNC VEANEWIDVL CRVSRCNHNR LSSFHPSAYL
     NGNWLCCQET SESTPGCKPC TAGIPADIQI DIDEDRETER IYSIFTLSLL KLQKMEETCG
     SIAVYQGPQK EPGYSKFTIE DSVATFKTIQ QIKSTIEKLD EPHEKYRKKR SSSAKYGSKE
     NPIVGKIS
//
ID   OPA1_MOUSE              Reviewed;         960 AA.
AC   P58281; A6H6Q3; Q3ULA5; Q8BKU7; Q8BLL3; Q8BM08; Q8R3J7;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Dynamin-like 120 kDa protein, mitochondrial;
DE   AltName: Full=Large GTP-binding protein;
DE            Short=LargeG;
DE   AltName: Full=Optic atrophy protein 1 homolog;
DE   Contains:
DE     RecName: Full=Dynamin-like 120 kDa protein, form S1;
DE   Flags: Precursor;
GN   Name=Opa1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=11847212; DOI=10.1074/jbc.M109260200;
RA   Misaka T., Miyashita T., Kubo Y.;
RT   "Primary structure of a dynamin-related mouse mitochondrial GTPase and
RT   its distribution in brain, subcellular localization, and effect on
RT   mitochondrial morphology.";
RL   J. Biol. Chem. 277:15834-15842(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-365 (ISOFORM 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Blastocyst, Hypothalamus, Liver, Retina, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PARL, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=16839884; DOI=10.1016/j.cell.2006.06.021;
RA   Cipolat S., Rudka T., Hartmann D., Costa V., Serneels L.,
RA   Craessaerts K., Metzger K., Frezza C., Annaert W., D'Adamio L.,
RA   Derks C., Dejaegere T., Pellegrini L., D'Hooge R., Scorrano L.,
RA   De Strooper B.;
RT   "Mitochondrial rhomboid PARL regulates cytochrome c release during
RT   apoptosis via OPA1-dependent cristae remodeling.";
RL   Cell 126:163-175(2006).
RN   [5]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=16839885; DOI=10.1016/j.cell.2006.06.025;
RA   Frezza C., Cipolat S., Martins de Brito O., Micaroni M.,
RA   Beznoussenko G.V., Rudka T., Bartoli D., Polishuck R.S., Danial N.N.,
RA   De Strooper B., Scorrano L.;
RT   "OPA1 controls apoptotic cristae remodeling independently from
RT   mitochondrial fusion.";
RL   Cell 126:177-189(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-652, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: Dynamin-related GTPase required for mitochondrial fusion
CC       and regulation of apoptosis. May form a diffusion barrier for
CC       proteins stored in mitochondrial cristae. Proteolytic processing
CC       in response to intrinsic apoptotic signals may lead to disassembly
CC       of OPA1 oligomers and release of the caspase activator cytochrome
CC       C (CYCS) into the mitochondrial intermembrane space.
CC   -!- SUBUNIT: Oligomeric complex consisting of membrane-bound and
CC       soluble forms of OPA1. Binds PARL.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass
CC       membrane protein. Mitochondrion intermembrane space.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P58281-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P58281-2; Sequence=VSP_021037;
CC   -!- PTM: PARL-dependent proteolytic processing releases an
CC       antiapoptotic soluble form not required for mitochondrial fusion.
CC   -!- DISRUPTION PHENOTYPE: Embryonic fibroblasts show a defect in
CC       apoptosis in response to intrinsic signals. This defect can be
CC       complemented by a soluble form of Opa1 targeted to the
CC       mitochondrial intermembrane space.
CC   -!- SIMILARITY: Belongs to the dynamin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH25160.1; Type=Erroneous initiation;
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DR   EMBL; AB044138; BAB59000.1; -; mRNA.
DR   EMBL; AK029157; BAC26331.1; -; mRNA.
DR   EMBL; AK038446; BAC30002.1; -; mRNA.
DR   EMBL; AK044657; BAC32021.1; -; mRNA.
DR   EMBL; AK050383; BAC34224.1; -; mRNA.
DR   EMBL; AK145620; BAE26544.1; -; mRNA.
DR   EMBL; BC025160; AAH25160.1; ALT_INIT; mRNA.
DR   EMBL; BC138665; AAI38666.1; -; mRNA.
DR   EMBL; BC145959; AAI45960.1; -; mRNA.
DR   IPI; IPI00117657; -.
DR   IPI; IPI00403336; -.
DR   RefSeq; NP_598513.1; NM_133752.3.
DR   UniGene; Mm.274285; -.
DR   ProteinModelPortal; P58281; -.
DR   SMR; P58281; 262-579.
DR   STRING; P58281; -.
DR   PhosphoSite; P58281; -.
DR   PRIDE; P58281; -.
DR   Ensembl; ENSMUST00000038867; ENSMUSP00000036993; ENSMUSG00000038084.
DR   Ensembl; ENSMUST00000068650; ENSMUSP00000067215; ENSMUSG00000038084.
DR   GeneID; 74143; -.
DR   KEGG; mmu:74143; -.
DR   UCSC; uc007ywf.1; mouse.
DR   CTD; 74143; -.
DR   MGI; MGI:1921393; Opa1.
DR   eggNOG; roNOG09941; -.
DR   GeneTree; ENSGT00550000074851; -.
DR   HOVERGEN; HBG019108; -.
DR   OMA; LLKLRYI; -.
DR   OrthoDB; EOG4KKZ2B; -.
DR   PhylomeDB; P58281; -.
DR   NextBio; 339890; -.
DR   ArrayExpress; P58281; -.
DR   Bgee; P58281; -.
DR   CleanEx; MM_OPA1; -.
DR   Genevestigator; P58281; -.
DR   GermOnline; ENSMUSG00000038084; Mus musculus.
DR   GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030061; C:mitochondrial crista; ISS:UniProtKB.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; TAS:UniProtKB.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0007007; P:inner mitochondrial membrane organization; ISS:UniProtKB.
DR   GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR   GO; GO:0045768; P:positive regulation of anti-apoptosis; ISS:UniProtKB.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; ISS:UniProtKB.
DR   InterPro; IPR022812; Dynamin.
DR   InterPro; IPR001401; Dynamin_GTPase.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   PRINTS; PR00195; DYNAMIN.
DR   SMART; SM00053; DYNc; 1.
DR   PROSITE; PS00410; DYNAMIN; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Apoptosis; Coiled coil;
KW   GTP-binding; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Nucleotide-binding; Phosphoprotein; Sensory transduction;
KW   Transit peptide; Transmembrane; Transmembrane helix; Vision.
FT   TRANSIT       1     87       Mitochondrion (By similarity).
FT   CHAIN        88    960       Dynamin-like 120 kDa protein,
FT                                mitochondrial.
FT                                /FTId=PRO_0000007398.
FT   CHAIN       195    960       Dynamin-like 120 kDa protein, form S1 (By
FT                                similarity).
FT                                /FTId=PRO_0000253480.
FT   TOPO_DOM     88     96       Mitochondrial matrix (Potential).
FT   TRANSMEM     97    113       Helical; (Potential).
FT   TOPO_DOM    114    960       Mitochondrial intermembrane (Potential).
FT   NP_BIND     295    302       GTP (Potential).
FT   NP_BIND     398    402       GTP (Potential).
FT   NP_BIND     467    470       GTP (Potential).
FT   COILED      210    254       Potential.
FT   COILED      895    960       Potential.
FT   MOD_RES      21     21       Phosphoserine (By similarity).
FT   MOD_RES      22     22       Phosphoserine (By similarity).
FT   MOD_RES     228    228       N6-acetyllysine (By similarity).
FT   MOD_RES     652    652       Phosphothreonine.
FT   VAR_SEQ     208    208       K -> KGLLGELILLQQQIQEHEEEARRAAGQYSTSYAQQK
FT                                RK (in isoform 2).
FT                                /FTId=VSP_021037.
FT   CONFLICT    236    236       L -> P (in Ref. 2; BAC30002).
FT   CONFLICT    330    331       TL -> NN (in Ref. 2; BAC32021).
SQ   SEQUENCE   960 AA;  111339 MW;  0F103FB1FD570F49 CRC64;
     MWRAGRAAVA CEVCQSLVKH SSGIQRNVPL QKLHLVSRSI YRSHHPALKL QRPQLRTPFQ
     QFSSLTHLSL HKLKLSPIKY GYQPRRNFWP ARLAARLLKL RYIILGSAVG GGYTAKKTFD
     EWKDMIPDLS DYKWIVPDFI WEIDEYIDLE KIRKALPSSE DLASLAPDLD KITESLSLLK
     DFFTAGSPGE TAFRATDHGS ESDKHYRKVS DKEKIDQLQE ELLHTQLKYQ RILERLEKEN
     KELRKLVLQK DDKGIHHRKL KKSLIDMYSE VLDVLSDYDA SYNTQDHLPR VVVVGDQSAG
     KTSVLEMIAQ ARIFPRGSGE MMTRSPVKVT LSEGPHHVAL FKDSSREFDL TKEEDLAALR
     HEIELRMRKN VKEGCTVSPE TISLNVKGPG LQRMVLVDLP GVINTVTSGM APDTKETIFS
     ISKAYMQNPN AIILCIQDGS VDAERSIVTD LVSQMDPHGR RTIFVLTKVD LAEKNVASPS
     RIQQIIEGKL FPMKALGYFA VVTGKGNSSE SIEAIREYEE EFFQNSKLLK TSMLKAHQVT
     TRNLSLAVSD CFWKMVRESV EQQADSFKAT RFNLETEWKN NYPRLRELDR NELFEKAKNE
     ILDEVISLSQ VTPKHWEEIL QQSLWERVST HVIENIYLPA AQTMNSGTFN TTVDIKLKQW
     TDKQLPNKAV EVAWETLQEE FSRFMTEPKG KEHDDIFDKL KEAVKEESIK RHKWNDFAED
     SLRVIQHNAL EDRSISDKQQ WDAAIYFMEE ALQGRLKDTE NAIENMIGPD WKKRWMYWKN
     RTQEQCVHNE TKNELEKMLK VNDEHPAYLA SDEITTVRKN LESRGVEVDP SLIKDTWHQV
     YRRHFLKTAL NHCNLCRRGF YYYQRHFIDS ELECNDVVLF WRIQRMLAIT ANTLRQQLTN
     TEVRRLEKNV KEVLEDFAED GEKKVKLLTG KRVQLAEDLK KVREIQEKLD AFIEALHQEK
//
ID   OX1R_MOUSE              Reviewed;         416 AA.
AC   P58307; Q3USS9; Q6VNS3; Q80T45;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Orexin receptor type 1;
DE            Short=Ox-1-R;
DE            Short=Ox1-R;
DE            Short=Ox1R;
DE   AltName: Full=Hypocretin receptor type 1;
GN   Name=Hcrtr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   PubMed=15256537; DOI=10.1210/me.2004-0167;
RA   Chen J., Randeva H.S.;
RT   "Genomic organization of mouse orexin receptors: characterization of
RT   two novel tissue-specific splice variants.";
RL   Mol. Endocrinol. 18:2790-2804(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 134-393.
RC   STRAIN=C57BL/6;
RA   Szendro P.I., Maevers K., Eichele G.;
RT   "Cloning of mouse orexin receptors.";
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 141-339.
RX   MEDLINE=22584407; PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA   Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA   Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA   Bergmann J.E., Gaitanaris G.A.;
RT   "The G protein-coupled receptor repertoires of human and mouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
RN   [5]
RP   REVIEW.
RX   MEDLINE=21237974; PubMed=11340621; DOI=10.1002/bies.1058;
RA   Hungs M., Mignot E.;
RT   "Hypocretin/orexin, sleep and narcolepsy.";
RL   Bioessays 23:397-408(2001).
RN   [6]
RP   REVIEW.
RX   MEDLINE=21178476; PubMed=11283317; DOI=10.1146/annurev.neuro.24.1.429;
RA   Willie J.T., Chemelli R.M., Sinton C.M., Yanagisawa M.;
RT   "To eat or to sleep? Orexin in the regulation of feeding and
RT   wakefulness.";
RL   Annu. Rev. Neurosci. 24:429-458(2001).
CC   -!- FUNCTION: Moderately selective excitatory receptor for orexin-A
CC       and, with a lower affinity, for orexin-B neuropeptide. Seems to be
CC       exclusively coupled to the G(q) subclass of heteromeric G
CC       proteins, which activates the phospholipase C mediated signaling
CC       cascade (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY336083; AAR01326.1; -; mRNA.
DR   EMBL; AK140137; BAE24252.1; -; mRNA.
DR   EMBL; AF394596; AAK71326.1; -; mRNA.
DR   EMBL; AY255599; AAO85111.1; -; mRNA.
DR   IPI; IPI00396717; -.
DR   RefSeq; NP_001156499.1; NM_001163027.1.
DR   RefSeq; NP_945197.2; NM_198959.2.
DR   UniGene; Mm.246595; -.
DR   ProteinModelPortal; P58307; -.
DR   SMR; P58307; 48-375.
DR   STRING; P58307; -.
DR   PhosphoSite; P58307; -.
DR   PRIDE; P58307; -.
DR   Ensembl; ENSMUST00000030562; ENSMUSP00000030562; ENSMUSG00000028778.
DR   Ensembl; ENSMUST00000119423; ENSMUSP00000112630; ENSMUSG00000028778.
DR   Ensembl; ENSMUST00000120154; ENSMUSP00000113198; ENSMUSG00000028778.
DR   GeneID; 230777; -.
DR   KEGG; mmu:230777; -.
DR   UCSC; uc008uyx.1; mouse.
DR   CTD; 230777; -.
DR   MGI; MGI:2385650; Hcrtr1.
DR   eggNOG; roNOG04176; -.
DR   HOGENOM; HBG283700; -.
DR   HOVERGEN; HBG101173; -.
DR   InParanoid; P58307; -.
DR   OrthoDB; EOG4JM7PV; -.
DR   NextBio; 380144; -.
DR   ArrayExpress; P58307; -.
DR   Bgee; P58307; -.
DR   CleanEx; MM_HCRTR1; -.
DR   Genevestigator; P58307; -.
DR   GermOnline; ENSMUSG00000028778; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016499; F:orexin receptor activity; IEA:InterPro.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR000204; Orexin_rcpt.
DR   InterPro; IPR004059; Orexin_rcpt_1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01521; OREXIN1R.
DR   PRINTS; PR01064; OREXINR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Phosphoprotein; Receptor; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    416       Orexin receptor type 1.
FT                                /FTId=PRO_0000069985.
FT   TOPO_DOM      1     46       Extracellular (Potential).
FT   TRANSMEM     47     67       Helical; Name=1; (Potential).
FT   TOPO_DOM     68     83       Cytoplasmic (Potential).
FT   TRANSMEM     84    104       Helical; Name=2; (Potential).
FT   TOPO_DOM    105    120       Extracellular (Potential).
FT   TRANSMEM    121    141       Helical; Name=3; (Potential).
FT   TOPO_DOM    142    162       Cytoplasmic (Potential).
FT   TRANSMEM    163    183       Helical; Name=4; (Potential).
FT   TOPO_DOM    184    218       Extracellular (Potential).
FT   TRANSMEM    219    239       Helical; Name=5; (Potential).
FT   TOPO_DOM    240    299       Cytoplasmic (Potential).
FT   TRANSMEM    300    320       Helical; Name=6; (Potential).
FT   TOPO_DOM    321    336       Extracellular (Potential).
FT   TRANSMEM    337    357       Helical; Name=7; (Potential).
FT   TOPO_DOM    358    416       Cytoplasmic (Potential).
FT   MOD_RES      27     27       Phosphotyrosine (By similarity).
FT   CARBOHYD    194    194       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    139    139       F -> V (in Ref. 3; AAK71326).
FT   CONFLICT    232    232       G -> A (in Ref. 2; BAE24252).
SQ   SEQUENCE   416 AA;  46767 MW;  A8958C594C365E00 CRC64;
     MEPSATPGAQ PGVPTSSGEP FHLPPDYEDE FLRYLWRDYL YPKQYEWVLI AAYVAVFLIA
     LVGNTLVCLA VWRNHHMRTV TNYFIVNLSL ADVLVTAICL PASLLVDITE SWLFGQALCK
     VIPYLQAVSV SVAVLTLSFI ALDRWYAICH PLLFKSTARR ARGSILGIWA VSLAVMVPQA
     AVMECSSVLP ELANRTRLFS VCDEHWADEL YPKIYHSCFF IVTYLAPLGL MGMAYFQIFR
     KLWGRQIPGT TSALVRNWKR PSEQLEAQHQ GLCTEPQPRA RAFLAEVKQM RARRKTAKML
     MVVLLVFALC YLPISVLNVL KRVFGMFRQA SDREAVYACF TFSHWLVYAN SAANPIIYNF
     LSGKFREQFK AAFSCCLPGL GPGSSARHKS LSLQSRCSVS KVSEHVVLTT VTTVLS
//
ID   KLF16_MOUSE             Reviewed;         251 AA.
AC   P58334; Q3U3Y4; Q8C8S2;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Krueppel-like factor 16;
DE   AltName: Full=Basic transcription element-binding protein 4;
DE            Short=BTE-binding protein 4;
DE   AltName: Full=Dopamine receptor-regulating factor;
DE   AltName: Full=Transcription factor BTEB4;
GN   Name=Klf16; Synonyms=Bteb4, Drrf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Neuroblastoma;
RX   MEDLINE=21309923; PubMed=11390978; DOI=10.1073/pnas.121635798;
RA   Hwang C.K., D'Souza U.M., Eisch A.J., Yajima S., Lammers C.-H.,
RA   Yang Y., Lee S.-H., Kim Y.-M., Nestler E.J., Mouradian M.M.;
RT   "Dopamine receptor regulating factor, DRRF: a zinc finger
RT   transcription factor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7558-7563(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Transcription factor that binds GC and GT boxes in the
CC       D1A, D2 and D3 dopamine receptor promoters and displaces Sp1 and
CC       Sp3 from these sequences. It modulates dopaminergic transmission
CC       in the brain by repressing or activating transcription from
CC       several different promoters depending on cellular context.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: High expression in brain; olfactory tubercle,
CC       olfactory bulb, nucleus accumbens, striatum, hippocampal CA1
CC       region, amygdala, dentate gyrus and frontal cortex. Moderate
CC       expression in hippocampal CA2-3 regions, piriform cortex, septum,
CC       and distinct thalamic nuclei. Low expression in the cerebellum.
CC   -!- DOMAIN: The Ala/Pro-rich domain may contain discrete activation
CC       and repression subdomains and also can mediate protein-protein
CC       interactions.
CC   -!- SIMILARITY: Belongs to the Sp1 C2H2-type zinc-finger protein
CC       family.
CC   -!- SIMILARITY: Contains 3 C2H2-type zinc fingers.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF283891; AAK66968.1; -; mRNA.
DR   EMBL; AK044577; BAC31987.1; -; mRNA.
DR   EMBL; AK154524; BAE32651.1; -; mRNA.
DR   IPI; IPI00118534; -.
DR   RefSeq; NP_510962.2; NM_078477.2.
DR   UniGene; Mm.41513; -.
DR   ProteinModelPortal; P58334; -.
DR   SMR; P58334; 124-245.
DR   STRING; P58334; -.
DR   PhosphoSite; P58334; -.
DR   PRIDE; P58334; -.
DR   Ensembl; ENSMUST00000038558; ENSMUSP00000048825; ENSMUSG00000035397.
DR   GeneID; 118445; -.
DR   KEGG; mmu:118445; -.
DR   UCSC; uc007gdt.1; mouse.
DR   CTD; 118445; -.
DR   MGI; MGI:2153049; Klf16.
DR   eggNOG; maNOG20584; -.
DR   HOGENOM; HBG125036; -.
DR   HOVERGEN; HBG050746; -.
DR   InParanoid; P58334; -.
DR   OMA; IASTWEP; -.
DR   OrthoDB; EOG479F8G; -.
DR   PhylomeDB; P58334; -.
DR   NextBio; 369718; -.
DR   ArrayExpress; P58334; -.
DR   Bgee; P58334; -.
DR   CleanEx; MM_KLF16; -.
DR   Genevestigator; P58334; -.
DR   GermOnline; ENSMUSG00000035397; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007212; P:dopamine receptor signaling pathway; IDA:MGI.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 3.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    251       Krueppel-like factor 16.
FT                                /FTId=PRO_0000047159.
FT   ZN_FING     126    150       C2H2-type 1.
FT   ZN_FING     156    180       C2H2-type 2.
FT   ZN_FING     186    208       C2H2-type 3.
FT   COMPBIAS      3    136       Ala/Pro-rich.
FT   COMPBIAS    103    116       Ser-rich.
FT   COMPBIAS    223    248       Pro/Ser-rich.
FT   MOD_RES     103    103       Phosphoserine (By similarity).
FT   MOD_RES     106    106       Phosphoserine (By similarity).
FT   MOD_RES     113    113       Phosphoserine (By similarity).
FT   MOD_RES     151    151       Phosphothreonine (By similarity).
SQ   SEQUENCE   251 AA;  25652 MW;  3F0D7739BF7B1FA4 CRC64;
     MSAAVACVDY FAADVLMAIS SGAVVHRGRP GPEGAGPAAG LDVRATRREA TPPGTPGAPP
     PPATAPGPGG ATAAPHLLAA SILADLRGGP VVATAASTAG GTSPVSSSSA ASSPSSGRAP
     GAAKSHRCPF HGCAKAYYKS SHLKSHLRTH TGERPFACDW PGCDKKFARS DELARHHRTH
     TGEKRFPCPL CTKRFTRSDH LTKHARRHPG FRPELLRRPG ARSVSPSDSL PCSLAGSPTP
     SPVPSPAPAG L
//
ID   KCNN3_MOUSE             Reviewed;         731 AA.
AC   P58391;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2001, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Small conductance calcium-activated potassium channel protein 3;
DE            Short=SK3;
DE            Short=SKCa 3;
DE            Short=SKCa3;
DE   AltName: Full=KCa2.3;
GN   Name=Kcnn3; Synonyms=Sk3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Colon;
RX   MEDLINE=21440983; PubMed=11557517;
RA   Ro S., Hatton W.J., Koh S.D., Horowitz B.;
RT   "Molecular properties of small-conductance Ca2+-activated K+ channels
RT   expressed in murine colonic smooth muscle.";
RL   Am. J. Physiol. 281:G964-G973(2001).
CC   -!- FUNCTION: Forms a voltage-independent potassium channel activated
CC       by intracellular calcium. Activation is followed by membrane
CC       hyperpolarization. Thought to regulate neuronal excitability by
CC       contributing to the slow component of synaptic
CC       afterhyperpolarization. The channel is blocked by apamin (By
CC       similarity).
CC   -!- SUBUNIT: Heterooligomer. The complex is composed of 4 channel
CC       subunits each of which binds to a calmodulin subunit which
CC       regulates the channel activity through calcium-binding (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the potassium channel KCNN family.
CC       KCa2.3/KCNN3 subfamily.
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DR   EMBL; AF357241; AAK48902.1; -; mRNA.
DR   IPI; IPI00874338; -.
DR   UniGene; Mm.120250; -.
DR   ProteinModelPortal; P58391; -.
DR   SMR; P58391; 402-674.
DR   STRING; P58391; -.
DR   PhosphoSite; P58391; -.
DR   PRIDE; P58391; -.
DR   Ensembl; ENSMUST00000000811; ENSMUSP00000000811; ENSMUSG00000000794.
DR   UCSC; uc008pzu.1; mouse.
DR   MGI; MGI:2153183; Kcnn3.
DR   eggNOG; roNOG05804; -.
DR   HOVERGEN; HBG052241; -.
DR   InParanoid; P58391; -.
DR   OrthoDB; EOG49CQ7G; -.
DR   ArrayExpress; P58391; -.
DR   Bgee; P58391; -.
DR   Genevestigator; P58391; -.
DR   GermOnline; ENSMUSG00000000794; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004178; CaM-bd_dom.
DR   InterPro; IPR013099; Ion_trans_2.
DR   InterPro; IPR015449; K_chnl_Ca-activ_SK.
DR   InterPro; IPR011996; K_chnl_Ca-activ_SK_con.
DR   InterPro; IPR003931; K_chnl_Ca-activ_SK_sub.
DR   PANTHER; PTHR10153; CaKChannelSK; 1.
DR   Pfam; PF02888; CaMBD; 1.
DR   Pfam; PF07885; Ion_trans_2; 1.
DR   Pfam; PF03530; SK_channel; 1.
DR   PRINTS; PR01451; SKCHANNEL.
DR   SUPFAM; SSF81327; CaM_bd; 1.
PE   2: Evidence at transcript level;
KW   Calmodulin-binding; Ion transport; Ionic channel; Membrane;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    731       Small conductance calcium-activated
FT                                potassium channel protein 3.
FT                                /FTId=PRO_0000155014.
FT   TRANSMEM    288    308       Helical; Name=Segment S1; (Potential).
FT   TRANSMEM    315    335       Helical; Name=Segment S2; (Potential).
FT   TRANSMEM    366    386       Helical; Name=Segment S3; (Potential).
FT   TRANSMEM    405    425       Helical; Name=Segment S4; (Potential).
FT   TRANSMEM    454    474       Helical; Name=Segment S5; (Potential).
FT   INTRAMEM    494    514       Pore-forming; Name=Segment H5;
FT                                (Potential).
FT   TRANSMEM    523    543       Helical; Name=Segment S6; (Potential).
FT   REGION      561    637       Calmodulin-binding (By similarity).
FT   COMPBIAS     30     35       Poly-Gln.
FT   COMPBIAS     36     43       Poly-Pro.
FT   COMPBIAS     60     79       Poly-Gln.
FT   COMPBIAS    683    687       Poly-Gln.
FT   COMPBIAS    727    730       Poly-Ser.
SQ   SEQUENCE   731 AA;  81255 MW;  E509C97E975C1A42 CRC64;
     MDTSGHFHDS GVGDLDEDPK CPCPSSGDEQ QQQQQPPPPP APPAVPQQPP GPLLQPQPPQ
     PQQQQSQQQQ QQQSQQQQQA PLHPLPQLAQ LQSQLVHPGL LHSSPTAFRA PTSANSTAIL
     HPSSRQGSQL NLNDHLLGHS PSSTATSGPG GGSRHRQASP LVHRRDSNPF TEIAMSSCKY
     SGGVMKPLSR LSASRRNLIE AEPEGQPLQL FSPSNPPEII ISSREDNHAH QTLLHHPNAT
     HNHQHAGTTA GSTTFPKANK RKNQNIGYKL GHRRALFEKR KRLSDYALIF GMFGIVVMVI
     ETELSWGLYS KDSMFSLALK CLISLSTVIL LGLIIAYHTR EVQLFVIDNG ADDWRIAMTY
     ERIFYISLEM LVCAIHPIPG EYKFFWTARL AFSYTPSRAE ADVDIILSIP MFLRLYLIAR
     VMLLHSKLFT DASSRSIGAL NKINFNTRFV MKTLMTICPG TVLLVFSISL WIIAAWTVRV
     CERYHDQQDV TSNFLGAMWL ISITFLSIGY GDMVPHTYCG KGVCLLTGIM GAGCTALVVA
     VVARKLELTK AEKHVHNFMM DTQLTKRIKN AATNVLRETW LVYKHTKLLK KIDHAKVRKH
     QRKFLQAIHQ LRGVKMEQRK LSDQANTLVD LSKMQNVMYD LITELNDRSE DLEKQIGSLE
     SKLEHLTASF NSLPLLIADT LRQQQQQLLT AFVEARGISV AVGTSHAPPS DSPIGISSTS
     FPTPYTSSSS C
//
ID   STRN4_MOUSE             Reviewed;         760 AA.
AC   P58404; Q68EF5;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2001, sequence version 1.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Striatin-4;
DE   AltName: Full=Zinedin;
GN   Name=Strn4; Synonyms=Zin;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=20347911; PubMed=10748158; DOI=10.1074/jbc.M909782199;
RA   Castets F., Rakitina T., Gaillard S., Moqrich A., Mattei M.-G.,
RA   Monneron A.;
RT   "Zinedin, SG2NA, and striatin are calmodulin-binding, WD repeat
RT   proteins principally expressed in the brain.";
RL   J. Biol. Chem. 275:19970-19977(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206 AND SER-223, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Binds calmodulin in a calcium dependent manner. May
CC       function as scaffolding or signaling protein.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P58404-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P58404-2; Sequence=VSP_013815;
CC   -!- TISSUE SPECIFICITY: Mainly expressed in brain but is also
CC       expressed at low levels in the kidney.
CC   -!- MISCELLANEOUS: The name 'Zinedin' probably originates from the
CC       name of the famous soccer player from Marseille (Zinedine Zidane).
CC   -!- SIMILARITY: Belongs to the WD repeat striatin family.
CC   -!- SIMILARITY: Contains 7 WD repeats.
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DR   EMBL; AF414080; AAL07439.1; -; mRNA.
DR   EMBL; BC004025; AAH04025.1; -; mRNA.
DR   EMBL; BC080283; AAH80283.1; -; mRNA.
DR   IPI; IPI00119524; -.
DR   IPI; IPI00607010; -.
DR   RefSeq; NP_598550.2; NM_133789.3.
DR   UniGene; Mm.21612; -.
DR   ProteinModelPortal; P58404; -.
DR   SMR; P58404; 417-759.
DR   STRING; P58404; -.
DR   PhosphoSite; P58404; -.
DR   PRIDE; P58404; -.
DR   Ensembl; ENSMUST00000019220; ENSMUSP00000019220; ENSMUSG00000030374.
DR   GeneID; 97387; -.
DR   KEGG; mmu:97387; -.
DR   UCSC; uc009fif.1; mouse.
DR   CTD; 97387; -.
DR   MGI; MGI:2142346; Strn4.
DR   eggNOG; roNOG14412; -.
DR   GeneTree; ENSGT00520000055597; -.
DR   HOGENOM; HBG385782; -.
DR   HOVERGEN; HBG007117; -.
DR   InParanoid; P58404; -.
DR   OrthoDB; EOG4R23TB; -.
DR   NextBio; 352759; -.
DR   ArrayExpress; P58404; -.
DR   Bgee; P58404; -.
DR   CleanEx; MM_STRN4; -.
DR   Genevestigator; P58404; -.
DR   GermOnline; ENSMUSG00000030374; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR013258; Striatin_N.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF08232; Striatin; 1.
DR   Pfam; PF00400; WD40; 5.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Calmodulin-binding; Coiled coil;
KW   Cytoplasm; Membrane; Phosphoprotein; Repeat; WD repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    760       Striatin-4.
FT                                /FTId=PRO_0000051240.
FT   REPEAT      443    482       WD 1.
FT   REPEAT      496    535       WD 2.
FT   REPEAT      549    588       WD 3.
FT   REPEAT      595    635       WD 4.
FT   REPEAT      642    681       WD 5.
FT   REPEAT      684    723       WD 6.
FT   REPEAT      730    759       WD 7.
FT   REGION       71     79       Caveolin-binding (Potential).
FT   REGION      165    182       Calmodulin-binding (Potential).
FT   COILED       69    136       Potential.
FT   MOD_RES       2      2       N-acetylmethionine (By similarity).
FT   MOD_RES     206    206       Phosphoserine.
FT   MOD_RES     223    223       Phosphoserine.
FT   MOD_RES     276    276       Phosphoserine (By similarity).
FT   VAR_SEQ     385    391       Missing (in isoform 2).
FT                                /FTId=VSP_013815.
FT   CONFLICT      9      9       A -> P (in Ref. 2; AAH80283).
FT   CONFLICT    594    594       A -> D (in Ref. 2; AAH80283).
SQ   SEQUENCE   760 AA;  81601 MW;  108745C459E9B327 CRC64;
     MMEERAAAAV ASAASSCRPL GSGTAPNPTA AAPASSPAPG PGPVGKGGGG GGSPGPTAGP
     EPLSLPGILH FIQHEWARFE AEKARWEAER AELQAQVAFL QGERKGQENL KTDLVRRIKM
     LEYALKQERA KYHKLKFGTD LNQGEKKTDL SEQVSNGPVE SVTLENSPLV WKEGRQLLRQ
     YLEEVGYTDT ILDMRSKRVR SLLGRSLELN GAGEPVEGAP RASPGPGGLS GGESLLVKQI
     EEQIKRNAAG KDGKERLGGS VLEQIPFLQN CEDEDSDEDD ELDSVQHKKQ RVRLPSKALV
     PEMEDEDEED DSEDAINEFD FLGSGEDGEG SPDPRRCTSE GNPHELESRR VKLQGILADL
     RDVDGLPPKV TVPPPGTPQP RPHEGSFGFS SDVFIMDTIG GGEVSLGDLA DLTVTNDNDL
     SCDLSDSKDA FKKTWNPKFT LRSHYDGIRS LAFHHSQSAL LTASEDGTLK LWNLQKAVTA
     KKNAALDVEP IHAFRAHRGP VLAVTMGSNS EYCYSGGADA RIHSWKIPDL NMDPYDGYDP
     SVLSHVLEGH GDAVWGLAFS PTSQRLASCS ADGTVRIWDP SSSGPSCLCT FPMAGEHGIP
     TSVAFTSTEP AHVVASFRSG DTVLYDLEAG SALLTLESRG SSGPAQINQV VSHPSQPLTI
     TAHDDRGIRF LDNRTGKSVH SMVAHLDAVT CLAVDPNGVF LMSGSHDCSL RLWSLDNKTC
     VQEITAHRKK HEEAIHAVAC HPSKALIASA GADALAKVFV
//
ID   HRH3_MOUSE              Reviewed;         445 AA.
AC   P58406;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2001, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Histamine H3 receptor;
DE            Short=H3R;
DE            Short=HH3R;
GN   Name=Hrh3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CD-1;
RA   Coge F., Rique H., Levacher B., Leopold O., Guenin S.-P., Boutin J.A.,
RA   Galizzi J.-P.;
RT   "Cloning of mouse histamine H3 receptor.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The H3 subclass of histamine receptors could mediate the
CC       histamine signals in CNS and peripheral nervous system. Signals
CC       through the inhibition of adenylate cyclase and displays high
CC       constitutive activity (spontaneous activity in the absence of
CC       agonist) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
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DR   EMBL; AY044153; AAK72406.1; -; mRNA.
DR   IPI; IPI00119525; -.
DR   RefSeq; NP_598610.1; NM_133849.2.
DR   UniGene; Mm.285360; -.
DR   ProteinModelPortal; P58406; -.
DR   SMR; P58406; 33-428.
DR   STRING; P58406; -.
DR   PRIDE; P58406; -.
DR   Ensembl; ENSMUST00000056480; ENSMUSP00000049963; ENSMUSG00000039059.
DR   GeneID; 99296; -.
DR   KEGG; mmu:99296; -.
DR   UCSC; uc008oij.1; mouse.
DR   CTD; 99296; -.
DR   MGI; MGI:2139279; Hrh3.
DR   eggNOG; roNOG14713; -.
DR   HOGENOM; HBG713567; -.
DR   HOVERGEN; HBG102132; -.
DR   InParanoid; P58406; -.
DR   OMA; HRYGVGE; -.
DR   OrthoDB; EOG45DWPW; -.
DR   PhylomeDB; P58406; -.
DR   NextBio; 353867; -.
DR   ArrayExpress; P58406; -.
DR   Bgee; P58406; -.
DR   CleanEx; MM_HRH3; -.
DR   Genevestigator; P58406; -.
DR   GermOnline; ENSMUSG00000039059; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR003980; Histamine_H3_recept.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01471; HISTAMINEH3R.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Receptor; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN         1    445       Histamine H3 receptor.
FT                                /FTId=PRO_0000069691.
FT   TOPO_DOM      1     39       Extracellular (Potential).
FT   TRANSMEM     40     60       Helical; Name=1; (Potential).
FT   TOPO_DOM     61     70       Cytoplasmic (Potential).
FT   TRANSMEM     71     91       Helical; Name=2; (Potential).
FT   TOPO_DOM     92    108       Extracellular (Potential).
FT   TRANSMEM    109    129       Helical; Name=3; (Potential).
FT   TOPO_DOM    130    156       Cytoplasmic (Potential).
FT   TRANSMEM    157    177       Helical; Name=4; (Potential).
FT   TOPO_DOM    178    196       Extracellular (Potential).
FT   TRANSMEM    197    217       Helical; Name=5; (Potential).
FT   TOPO_DOM    218    359       Cytoplasmic (Potential).
FT   TRANSMEM    360    380       Helical; Name=6; (Potential).
FT   TOPO_DOM    381    396       Extracellular (Potential).
FT   TRANSMEM    397    417       Helical; Name=7; (Potential).
FT   TOPO_DOM    418    445       Cytoplasmic (Potential).
FT   COMPBIAS     20     23       Poly-Ala.
FT   CARBOHYD     11     11       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   445 AA;  48541 MW;  B8D406E29E1F3C5F CRC64;
     MERAPPDGLM NASGALAGEA AAAGGARGFS AAWTAVLAAL MALLIVATVL GNALVMLAFV
     ADSSLRTQNN FFLLNLAISD FLVGAFCIPL YVPYVLTGRW TFGRGLCKLW LVVDYLLCAS
     SVFNIVLISY DRFLSVTRAV SYRAQQGDTR RAVRKMALVW VLAFLLYGPA ILSWEYLSGG
     SSIPEGHCYA EFFYNWYFLI TASTLEFFTP FLSVTFFNLS IYLNIQRRTR LRLDGGREAG
     PEPPPDAQPS PPPAPPSCWG CWPKGHGEAM PLHRYGVGEA GPGVETGEAG LGGGSGGGAA
     ASPTSSSGSS SRGTERPRSL KRGSKPSASS ASLEKRMKMV SQSITQRFRL SRDKKVAKSL
     AIIVSIFGLC WAPYTLLMII RAACHGHCVP DYWYETSFWL LWANSAVNPV LYPLCHYSFR
     RAFTKLLCPQ KLKVQPHGSL EQCWK
//
ID   FOXP1_MOUSE             Reviewed;         705 AA.
AC   P58462; Q6P221; Q8C5V2; Q8CCD9;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2001, sequence version 1.
DT   08-FEB-2011, entry version 86.
DE   RecName: Full=Forkhead box protein P1;
DE   AltName: Full=Forkhead-related transcription factor 1;
GN   Name=Foxp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6; TISSUE=Lung;
RX   MEDLINE=21347947; PubMed=11358962; DOI=10.1074/jbc.M100636200;
RA   Shu W., Yang H., Zhang L., Lu M.M., Morrisey E.E.;
RT   "Characterization of a new subfamily of winged-helix/forkhead (Fox)
RT   genes that are expressed in the lung and act as transcriptional
RT   repressors.";
RL   J. Biol. Chem. 276:27488-27497(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=C57BL/6J; TISSUE=Lung, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   DEVELOPMENTAL STAGE.
RX   MEDLINE=22879833; PubMed=14516685; DOI=10.1016/S0925-4773(03)00116-3;
RA   Lu M.M., Li S., Yang H., Morrisey E.E.;
RT   "Foxp4: a novel member of the Foxp subfamily of winged-helix genes co-
RT   expressed with Foxp1 and Foxp2 in pulmonary and gut tissues.";
RL   Mech. Dev. 119:S197-S202(2002).
RN   [5]
RP   FUNCTION, DIMERIZATION, INTERACTION WITH CTBP1, DOMAIN, AND
RP   MUTAGENESIS OF GLU-388 AND 410-PRO--VAL-414.
RX   PubMed=14701752; DOI=10.1128/MCB.24.2.809-822.2004;
RA   Li S., Weidenfeld J., Morrisey E.E.;
RT   "Transcriptional and DNA binding activity of the Foxp1/2/4 family is
RT   modulated by heterotypic and homotypic protein interactions.";
RL   Mol. Cell. Biol. 24:809-822(2004).
RN   [6]
RP   FUNCTION.
RX   PubMed=16819554; DOI=10.1038/ni1358;
RA   Hu H., Wang B., Borde M., Nardone J., Maika S., Allred L.,
RA   Tucker P.W., Rao A.;
RT   "Foxp1 is an essential transcriptional regulator of B cell
RT   development.";
RL   Nat. Immunol. 7:819-826(2006).
CC   -!- FUNCTION: Transcriptional repressor that plays an important role
CC       in the specification and differentiation of lung epithelium. Can
CC       act with CTBP1 to synergistically repress transcription but CTPBP1
CC       is not essential. Essential transcriptional regulator of B cell
CC       development.
CC   -!- SUBUNIT: Forms homodimers and heterodimers with FOXP2 and FOXP4.
CC       Dimerization is required for DNA-binding. Interacts with CTBP1.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing, Alternative initiation; Named isoforms=4;
CC       Name=1; Synonyms=A;
CC         IsoId=P58462-1; Sequence=Displayed;
CC       Name=2; Synonyms=B;
CC         IsoId=P58462-2; Sequence=VSP_001557;
CC       Name=3; Synonyms=C;
CC         IsoId=P58462-3; Sequence=VSP_018732;
CC         Note=Produced by alternative initiation at Met-251 of isoform 1;
CC       Name=4;
CC         IsoId=P58462-4; Sequence=VSP_026670;
CC         Note=Produced by alternative splicing. No experimental
CC         confirmation available;
CC   -!- TISSUE SPECIFICITY: Highest expression in the lung, brain, and
CC       spleen. Lower expression in heart, skeletal muscle, kidney, small
CC       intestine (isoform 3 not present) and liver.
CC   -!- DEVELOPMENTAL STAGE: Expressed in developing lung, neural,
CC       intestinal and cardiovascular tissues. Expressed in both the
CC       airway epithelium of the forming lung as well as in the
CC       surrounding mesenchyme. By 16.5 dpc, expressed throughout the
CC       conducting airway epithelium, with highest expression in the
CC       distal alveolar regions. Also expressed in the endotheial cells of
CC       the pulmonary vasculature. During intestinal development,
CC       expressed in the mucosal layer but absent from the epithelium at
CC       12.5 dpc. By 16.5 dpc, expressed in both the inner circular and
CC       outer longitudinal muscular layers of the intestine as well as in
CC       the epithelium of the intestine and developing stomach.
CC   -!- DOMAIN: The leucine-zipper is required for dimerization and
CC       transcriptional repression.
CC   -!- SIMILARITY: Contains 1 C2H2-type zinc finger.
CC   -!- SIMILARITY: Contains 1 fork-head DNA-binding domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AF339103; AAK69648.1; -; mRNA.
DR   EMBL; AF339104; AAK69649.1; -; mRNA.
DR   EMBL; AF339105; AAK69650.1; -; mRNA.
DR   EMBL; AK033368; BAC28249.1; -; mRNA.
DR   EMBL; AK077062; BAC36586.1; -; mRNA.
DR   EMBL; BC064764; AAH64764.1; -; mRNA.
DR   IPI; IPI00230542; -.
DR   IPI; IPI00323239; -.
DR   IPI; IPI00621220; -.
DR   IPI; IPI00853941; -.
DR   RefSeq; NP_001184250.1; NM_001197321.1.
DR   RefSeq; NP_001184251.1; NM_001197322.1.
DR   RefSeq; NP_444432.1; NM_053202.2.
DR   UniGene; Mm.234965; -.
DR   UniGene; Mm.392313; -.
DR   UniGene; Mm.461753; -.
DR   ProteinModelPortal; P58462; -.
DR   SMR; P58462; 492-573.
DR   STRING; P58462; -.
DR   PhosphoSite; P58462; -.
DR   PRIDE; P58462; -.
DR   Ensembl; ENSMUST00000074346; ENSMUSP00000073953; ENSMUSG00000030067.
DR   Ensembl; ENSMUST00000113322; ENSMUSP00000108948; ENSMUSG00000030067.
DR   Ensembl; ENSMUST00000113329; ENSMUSP00000108955; ENSMUSG00000030067.
DR   GeneID; 108655; -.
DR   KEGG; mmu:108655; -.
DR   UCSC; uc009dbi.1; mouse.
DR   UCSC; uc009dbl.1; mouse.
DR   CTD; 108655; -.
DR   MGI; MGI:1914004; Foxp1.
DR   eggNOG; roNOG04306; -.
DR   GeneTree; ENSGT00560000076806; -.
DR   HOVERGEN; HBG051657; -.
DR   NextBio; 361173; -.
DR   ArrayExpress; P58462; -.
DR   Bgee; P58462; -.
DR   CleanEx; MM_FOXP1; -.
DR   Genevestigator; P58462; -.
DR   GermOnline; ENSMUSG00000030067; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003705; F:sequence-specific enhancer binding RNA polymerase II transcription factor activity; IDA:MGI.
DR   GO; GO:0016566; F:specific transcriptional repressor activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:MGI.
DR   GO; GO:0009790; P:embryo development; IMP:MGI.
DR   GO; GO:0033152; P:immunoglobulin V(D)J recombination; IMP:MGI.
DR   GO; GO:0030324; P:lung development; IGI:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IGI:MGI.
DR   GO; GO:0002639; P:positive regulation of immunoglobulin production; IMP:MGI.
DR   GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IGI:MGI.
DR   GO; GO:0002329; P:pre-B cell differentiation; IMP:MGI.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IGI:MGI.
DR   GO; GO:0048745; P:smooth muscle tissue development; IGI:MGI.
DR   InterPro; IPR001766; TF_fork_head.
DR   InterPro; IPR018122; TF_fork_head_CS.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   PANTHER; PTHR11829; Fork_box_protein; 1.
DR   Pfam; PF00250; Fork_head; 1.
DR   PRINTS; PR00053; FORKHEAD.
DR   SMART; SM00339; FH; 1.
DR   SMART; SM00355; ZnF_C2H2; 1.
DR   PROSITE; PS00657; FORK_HEAD_1; FALSE_NEG.
DR   PROSITE; PS00658; FORK_HEAD_2; 1.
DR   PROSITE; PS50039; FORK_HEAD_3; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative initiation; Alternative splicing; DNA-binding;
KW   Metal-binding; Nucleus; Phosphoprotein; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    705       Forkhead box protein P1.
FT                                /FTId=PRO_0000009336.
FT   DOMAIN      376    397       Leucine-zipper.
FT   ZN_FING     334    359       C2H2-type.
FT   DNA_BIND    493    583       Fork-head.
FT   REGION      410    414       CTBP1-binding.
FT   COMPBIAS     55    258       Gln-rich.
FT   MOD_RES     468    468       Phosphoserine (By similarity).
FT   VAR_SEQ       1    250       Missing (in isoform 3).
FT                                /FTId=VSP_018732.
FT   VAR_SEQ       1    130       Missing (in isoform 4).
FT                                /FTId=VSP_026670.
FT   VAR_SEQ     539    602       Missing (in isoform 2).
FT                                /FTId=VSP_001557.
FT   MUTAGEN     388    388       Missing: Loss of dimerization. Almost
FT                                complete loss of DNA-binding. Reduced
FT                                transcriptional repression activity.
FT   MUTAGEN     410    414       PLNLV->AANAA: No significant effect on
FT                                transcriptional repression activity.
FT   CONFLICT     61     92       Missing (in Ref. 3; AAH64764).
FT   CONFLICT    199    199       E -> EQ (in Ref. 2; BAC28249/BAC36586).
FT   CONFLICT    281    281       D -> H (in Ref. 2; BAC28249).
FT   CONFLICT    353    353       K -> T (in Ref. 2; BAC28249).
FT   CONFLICT    597    597       L -> F (in Ref. 2; BAC28249).
SQ   SEQUENCE   705 AA;  78833 MW;  92962B82917CC79D CRC64;
     MMQESGSETK SNGSAIQNGS SGGNHLLECG ALRDTRSNGE APAVDLGAAD LAHVQQQQQQ
     ALQVARQLLL QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQVSG LKSPKRNDKQ
     PALQVPVSVA MMTPQVITPQ QMQQILQQQV LSPQQLQVLL QQQQALMLQQ QLQEFYKKQQ
     EQLQLQLLQQ QHAGKQPKEQ QVATQQLAFQ QQLLQMQQLQ QQHLLSLQRQ GLLTIQPGQP
     ALPLQPLAQG MIPTELQQLW KEVTSAHTAE ETTSSNHSSL DLTSTCVSSS APSKSSLIMN
     PHASTNGQLS VHTPKRESLS HEEHPHSHPL YGHGVCKWPG CEAVCDDFPA FLKHLNSEHA
     LDDRSTAQCR VQMQVVQQLE LQLAKDKERL QAMMTHLHVK STEPKAAPQP LNLVSSVTLS
     KSASEASPQS LPHTPTTPTA PLTPVTQGPS VITTTSMHTV GPIRRRYSDK YNVPISSADI
     AQNQEFYKNA EVRPPFTYAS LIRQAILESP EKQLTLNEIY NWFTRMFAYF RRNAATWKNA
     VRHNLSLHKC FVRVENVKGA VWTVDEVEFQ KRRPQKISGN PSLIKNMQSS HAYCTPLNAA
     LQASMAENSI PLYTTASMGN PTLGSLASAI REELNGAMEH TNSNESDSSP GRSPMQAVHP
     IHVKEEPLDP EEAEGPLSLV TTANHSPDFD HDRDYEDEPV NEDME
//
ID   CU070_MOUSE             Reviewed;         219 AA.
AC   P58468;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Uncharacterized protein C21orf70 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=21564202; PubMed=11707072; DOI=10.1006/geno.2001.6640;
RA   Reymond A., Friedli M., Neergaard Henrichsen C., Chapot F.,
RA   Deutsch S., Ucla C., Rossier C., Lyle R., Guipponi M.,
RA   Antonarakis S.E.;
RT   "From PREDs and open reading frames to cDNA isolation: revisiting the
RT   human chromosome 21 transcription map.";
RL   Genomics 78:46-54(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF391115; AAL34506.1; -; mRNA.
DR   EMBL; BC034216; AAH34216.1; -; mRNA.
DR   IPI; IPI00119727; -.
DR   RefSeq; NP_598759.1; NM_133998.3.
DR   UniGene; Mm.259547; -.
DR   ProteinModelPortal; P58468; -.
DR   PhosphoSite; P58468; -.
DR   PRIDE; P58468; -.
DR   Ensembl; ENSMUST00000045454; ENSMUSP00000036382; ENSMUSG00000032977.
DR   GeneID; 108707; -.
DR   KEGG; mmu:108707; -.
DR   UCSC; uc007fvt.1; mouse.
DR   MGI; MGI:1916334; 1810008A18Rik.
DR   eggNOG; maNOG20386; -.
DR   HOGENOM; HBG715434; -.
DR   HOVERGEN; HBG051241; -.
DR   InParanoid; P58468; -.
DR   OrthoDB; EOG4J3WJ8; -.
DR   PhylomeDB; P58468; -.
DR   NextBio; 361249; -.
DR   ArrayExpress; P58468; -.
DR   Bgee; P58468; -.
DR   CleanEx; MM_1810008A18RIK; -.
DR   Genevestigator; P58468; -.
DR   GermOnline; ENSMUSG00000032977; Mus musculus.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    219       Uncharacterized protein C21orf70 homolog.
FT                                /FTId=PRO_0000079529.
FT   MOD_RES      38     38       Phosphoserine.
FT   MOD_RES     192    192       Phosphoserine (By similarity).
SQ   SEQUENCE   219 AA;  24814 MW;  A51E445BB53986C1 CRC64;
     MGKVRALRAR VHRAAVRPDG DSAPGPVPRA VEPALPQSPA GGAGAKDWTF VHNDIFARTQ
     IDPSALVQRL ELDQRSVVSL KRGAEPKAIL PKKEKLKLRR ERWLQKIEAI KLAEQKLREE
     RKRKAMVVVG DLHPLRDALP ELQELEAGRQ RQQARRRVTS KPRPVELSRM TTVQRQQLLE
     EERTRFQKLL ASPTYRASPL LAIGQQLAHQ MQLEGGKQL
//
ID   GCFC1_MOUSE             Reviewed;         917 AA.
AC   P58501; Q78XY2; Q8R2W3; Q9CRB7;
DT   19-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=GC-rich sequence DNA-binding factor 1;
GN   Name=Gcfc1; Synonyms=Gcfc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E).
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 63-917 (ISOFORMS A AND D).
RX   MEDLINE=21564202; PubMed=11707072; DOI=10.1006/geno.2001.6640;
RA   Reymond A., Friedli M., Neergaard Henrichsen C., Chapot F.,
RA   Deutsch S., Ucla C., Rossier C., Lyle R., Guipponi M.,
RA   Antonarakis S.E.;
RT   "From PREDs and open reading frames to cDNA isolation: revisiting the
RT   human chromosome 21 transcription map.";
RL   Genomics 78:46-54(2001).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Possible transcription factor.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=A;
CC         IsoId=P58501-1; Sequence=Displayed;
CC       Name=D;
CC         IsoId=P58501-2; Sequence=VSP_004268, VSP_004269;
CC       Name=E;
CC         IsoId=P58501-3; Sequence=VSP_026540;
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the GCF family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH27145.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAB27645.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; AK007365; BAB24988.2; -; mRNA.
DR   EMBL; AK011477; BAB27645.2; ALT_INIT; mRNA.
DR   EMBL; AC141885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC014838; AAH14838.2; -; mRNA.
DR   EMBL; BC027145; AAH27145.1; ALT_INIT; mRNA.
DR   EMBL; AY033907; AAK68725.1; -; mRNA.
DR   EMBL; AY033908; AAK68726.1; -; mRNA.
DR   IPI; IPI00222810; -.
DR   IPI; IPI00752687; -.
DR   IPI; IPI00849284; -.
DR   UniGene; Mm.347; -.
DR   MINT; MINT-136240; -.
DR   STRING; P58501; -.
DR   PhosphoSite; P58501; -.
DR   PRIDE; P58501; -.
DR   Ensembl; ENSMUST00000023698; ENSMUSP00000023698; ENSMUSG00000022974.
DR   Ensembl; ENSMUST00000118522; ENSMUSP00000113835; ENSMUSG00000022974.
DR   MGI; MGI:1914617; Gcfc1.
DR   eggNOG; roNOG12549; -.
DR   GeneTree; ENSGT00390000000455; -.
DR   HOGENOM; HBG443575; -.
DR   HOVERGEN; HBG005817; -.
DR   InParanoid; P58501; -.
DR   OrthoDB; EOG4TF0JN; -.
DR   ArrayExpress; P58501; -.
DR   Bgee; P58501; -.
DR   CleanEx; MM_1810007M14RIK; -.
DR   Genevestigator; P58501; -.
DR   GermOnline; ENSMUSG00000022974; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR012890; GCFC.
DR   InterPro; IPR022783; GCFC_dom.
DR   PANTHER; PTHR12214; GCFC; 1.
DR   Pfam; PF07842; GCFC; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    917       GC-rich sequence DNA-binding factor 1.
FT                                /FTId=PRO_0000087440.
FT   MOD_RES      16     16       Phosphoserine.
FT   MOD_RES     158    158       Phosphoserine (By similarity).
FT   MOD_RES     191    191       Phosphoserine (By similarity).
FT   MOD_RES     262    262       Phosphoserine (By similarity).
FT   MOD_RES     295    295       Phosphoserine (By similarity).
FT   MOD_RES     378    378       Phosphothreonine (By similarity).
FT   MOD_RES     380    380       Phosphoserine (By similarity).
FT   MOD_RES     557    557       Phosphoserine (By similarity).
FT   MOD_RES     558    558       Phosphoserine (By similarity).
FT   VAR_SEQ       1    506       Missing (in isoform E).
FT                                /FTId=VSP_026540.
FT   VAR_SEQ     505    510       ALMAPN -> SILKIK (in isoform D).
FT                                /FTId=VSP_004268.
FT   VAR_SEQ     512    917       Missing (in isoform D).
FT                                /FTId=VSP_004269.
FT   CONFLICT    540    541       RQ -> SE (in Ref. 1; BAB24988).
FT   CONFLICT    547    547       G -> S (in Ref. 1; BAB24988).
FT   CONFLICT    794    794       T -> S (in Ref. 1; BAB24988).
SQ   SEQUENCE   917 AA;  104601 MW;  8C83C58BD8FCE11E CRC64;
     MFRKARRVNV RKRNDSEEEE RERDEEQEPP PLLPPPASGE EPGPGGGDRA PAGESLLGPG
     PLPPSAHNPG LGAEAGGGIP GGAEPGNGLK PRKRPRENKE VPRASLLSFQ DEEEENEEVF
     KVKKSSYSKK IVKLLKKEYK EDLEKSKIKT ELNTAADSDQ PLDKTCHAKD TNPEDGVVIS
     EHGEDEMDME SEKEEEKPKA GGAFSNALSS LNVLRPGEIP DAAFIHAARK KRQLARELGD
     FTPHDSEPGK GRLVREDEND ASDDEDDDEK RRIVFSVKEK SQRQKIAEEI GIEGSDDDAL
     VTGEQDEELS RWEQEQIRKG INIPQVQASQ PSEVNVYYQN TYQTMPYGAS YGIPYSYTAY
     GSSDAKSQKT DNTVPFKTPS NEMAPVTIDL VKRQLKDRLD SMKELHKTNQ QQHEKHLQSR
     VDSTRAIERL EGSSGGIGER YKFLQEMRGY VQDLLECFSE KVPLINELES AIHQLYKQRA
     SRLVQRRQDD IKDESSEFSS HSSQALMAPN LDSFGRDRAL YQEHAKRRIA EREARRTRRR
     QAREQTGQMA DHLEGLSSDD EETSTDITNF NLEKDRILKE SSKVFEDVLE SFYSIDCIKA
     QFEAWRSKYY MSYKDAYIGL CLPKLFNPLI RLQLLTWTPL EAKCRDFETM LWFESLLFYG
     CEDREQEKDE ADVALLPTIV EKVILPKLTV IAETMWDPFS TTQTSRMVGI TMKLINGYPS
     VVNADNKNTQ VYLKALLLRM RRTLDDDVFM PLYPKNVLEN KNSGPYLFFQ RQFWSSVKLL
     GNFLQWYGIF SNKTLQELSI DGLLNRYILM AFQNSEYGDD SIRKAQNVIN CFPKQWFVNL
     KGERTISQLE NFCRYLVHLA DTIYRNSIGC SDVEKRNARE NIKQIVKLLA SVRALDHAIS
     VASDHNVKEV KSLIEGK
//
ID   AAAS_MOUSE              Reviewed;         546 AA.
AC   P58742; Q544M6;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Aladin;
DE   AltName: Full=Adracalin;
GN   Name=Aaas;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Lung, Spleen, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Plays a role in the normal development of the peripheral
CC       and central nervous system (By similarity).
CC   -!- SIMILARITY: Contains 4 WD repeats.
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DR   EMBL; AK034591; BAC28764.1; -; mRNA.
DR   EMBL; AK083537; BAC38945.1; -; mRNA.
DR   EMBL; AK134406; BAE22131.1; -; mRNA.
DR   EMBL; AK165243; BAE38099.1; -; mRNA.
DR   EMBL; AK166118; BAE38581.1; -; mRNA.
DR   EMBL; BC018191; AAH18191.1; -; mRNA.
DR   IPI; IPI00311509; -.
DR   RefSeq; NP_700465.2; NM_153416.2.
DR   UniGene; Mm.352946; -.
DR   ProteinModelPortal; P58742; -.
DR   SMR; P58742; 144-349.
DR   STRING; P58742; -.
DR   PhosphoSite; P58742; -.
DR   PRIDE; P58742; -.
DR   Ensembl; ENSMUST00000041208; ENSMUSP00000044604; ENSMUSG00000036678.
DR   GeneID; 223921; -.
DR   KEGG; mmu:223921; -.
DR   UCSC; uc007xvl.1; mouse.
DR   CTD; 223921; -.
DR   MGI; MGI:2443767; Aaas.
DR   eggNOG; roNOG14113; -.
DR   HOGENOM; HBG447101; -.
DR   HOVERGEN; HBG026353; -.
DR   InParanoid; P58742; -.
DR   OMA; MCSLALF; -.
DR   OrthoDB; EOG4C2H96; -.
DR   ArrayExpress; P58742; -.
DR   Bgee; P58742; -.
DR   Genevestigator; P58742; -.
DR   GermOnline; ENSMUSG00000036678; Mus musculus.
DR   GO; GO:0009566; P:fertilization; IMP:MGI.
DR   GO; GO:0007612; P:learning; IMP:MGI.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
DR   Pfam; PF00400; WD40; 2.
DR   SMART; SM00320; WD40; 4.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Repeat; WD repeat.
FT   CHAIN         1    546       Aladin.
FT                                /FTId=PRO_0000050829.
FT   REPEAT      149    188       WD 1.
FT   REPEAT      191    230       WD 2.
FT   REPEAT      243    282       WD 3.
FT   REPEAT      285    324       WD 4.
FT   MOTIF       544    546       Microbody targeting signal (Potential).
FT   MOD_RES      33     33       Phosphoserine (By similarity).
FT   MOD_RES     495    495       Phosphoserine.
SQ   SEQUENCE   546 AA;  59431 MW;  5F483AEB8C2E969B CRC64;
     MCSLGLFPPP PPRGQVTLYE HNNELVTGNS YESPPPDFRG QWINLPVLHL TKDPLKAPGR
     LDHGTRTAFI HHREQVWKRC INVWHDVGLF GVLNEIANSE EEVFEWVKTA CSWALALCGR
     ASSLHGSLFP HLSLRSEDLI AEFAQVTNWS SCCLRVFAWH PHTNKFAVAL LDDSIRVYNA
     NSTIVPSLKH RLQRNVAALA WKPLSASVLA VACQSCILIW TLDPTSLSTR PSSGCAQVLS
     HPGHTPVTSL AWAPNGGWLL SASPVDAVIL VWDVSTETCV PLPWFRGGGV TNLLWSPDGS
     KVLATTPSAV FRVWEAQMWT CEAWPTLSGR CQTGCWSPDG NRLLFTVLGE ALIYSLSFPE
     RCGTGKGHVG GAKSATIVAD LSETTIQTPD GEERLGGEAH SMVWDPSGER LAVLMKGNPQ
     VQDGNPVILL FRTRNSPVFE LLPCGIIQGE PGAQAQLITF HPSFNKGALL SVCWSTGRIT
     HIPLYFVNAQ FPRFSPVLGR AQEPPAGGGG SIHEVPLFTE TSPTSAPWDP LPGQSSAQPH
     SPHSHL
//
ID   TPM1_MOUSE              Reviewed;         284 AA.
AC   P58771; P02558; P19354; P46902; P99034;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Tropomyosin alpha-1 chain;
DE   AltName: Full=Alpha-tropomyosin;
DE   AltName: Full=Tropomyosin-1;
GN   Name=Tpm1; Synonyms=Tpm-1, Tpma;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=A2G; TISSUE=Fast-twitch skeletal muscle;
RX   MEDLINE=95003687; PubMed=7522680; DOI=10.1016/0960-8966(94)90021-3;
RA   Schleef M., Zuehlke C., Schoeffl F., Jockusch H.;
RT   "Subtractive cDNA cloning as a tool to analyse secondary effects of a
RT   muscle disease. Characterization of affected genes in the myotonic ADR
RT   mouse.";
RL   Neuromuscul. Disord. 4:205-217(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   MEDLINE=89219020; PubMed=3244365;
RA   Takenaga K., Nakamura Y., Tokunaga K., Kageyama H., Sakiyama S.;
RT   "Isolation and characterization of a cDNA that encodes mouse
RT   fibroblast tropomyosin isoform 2.";
RL   Mol. Cell. Biol. 8:5561-5565(1988).
RN   [3]
RP   INDUCTION.
RX   MEDLINE=89121031; PubMed=2521606; DOI=10.1016/0014-4827(89)90080-3;
RA   Ryseck R.P., MacDonald-Bravo H., Zerial M., Bravo R.;
RT   "Coordinate induction of fibronectin, fibronectin receptor,
RT   tropomyosin, and actin genes in serum-stimulated fibroblasts.";
RL   Exp. Cell Res. 180:537-545(1989).
RN   [4]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-77, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Heart;
RX   PubMed=17451654; DOI=10.1016/j.bbrc.2007.04.015;
RA   Jeon H.B., Choi E.S., Yoon J.H., Hwang J.H., Chang J.W., Lee E.K.,
RA   Choi H.W., Park Z.-Y., Yoo Y.J.;
RT   "A proteomics approach to identify the ubiquitinated proteins in mouse
RT   heart.";
RL   Biochem. Biophys. Res. Commun. 357:731-736(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Binds to actin filaments in muscle and non-muscle cells.
CC       Plays a central role, in association with the troponin complex, in
CC       the calcium dependent regulation of vertebrate striated muscle
CC       contraction. Smooth muscle contraction is regulated by interaction
CC       with caldesmon. In non-muscle cells is implicated in stabilizing
CC       cytoskeleton actin filaments.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1; Synonyms=Skeletal muscle;
CC         IsoId=P58771-1; Sequence=Displayed;
CC       Name=2; Synonyms=Fibroblast;
CC         IsoId=P58771-2; Sequence=VSP_006580;
CC   -!- INDUCTION: Induced in stimulated quiescent cells.
CC   -!- DOMAIN: The molecule is in a coiled coil structure that is formed
CC       by 2 polypeptide chains. The sequence exhibits a prominent seven-
CC       residues periodicity.
CC   -!- MISCELLANEOUS: The sequences of cardiac and skeletal muscles are
CC       identical.
CC   -!- SIMILARITY: Belongs to the tropomyosin family.
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DR   EMBL; X64831; CAA46043.1; -; mRNA.
DR   EMBL; M22479; AAA40483.1; -; mRNA.
DR   IPI; IPI00123316; -.
DR   IPI; IPI00227835; -.
DR   PIR; A31380; A60597.
DR   RefSeq; NP_001157720.1; NM_001164248.1.
DR   RefSeq; NP_077745.2; NM_024427.4.
DR   UniGene; Mm.121878; -.
DR   ProteinModelPortal; P58771; -.
DR   SMR; P58771; 8-284.
DR   DIP; DIP-300N; -.
DR   IntAct; P58771; 6.
DR   STRING; P58771; -.
DR   PhosphoSite; P58771; -.
DR   SWISS-2DPAGE; P58771; -.
DR   PRIDE; P58771; -.
DR   Ensembl; ENSMUST00000113685; ENSMUSP00000109315; ENSMUSG00000032366.
DR   Ensembl; ENSMUST00000113707; ENSMUSP00000109337; ENSMUSG00000032366.
DR   GeneID; 22003; -.
DR   KEGG; mmu:22003; -.
DR   UCSC; uc009qfq.1; mouse.
DR   CTD; 22003; -.
DR   MGI; MGI:98809; Tpm1.
DR   HOVERGEN; HBG107404; -.
DR   OrthoDB; EOG4TXBSM; -.
DR   ArrayExpress; P58771; -.
DR   Bgee; P58771; -.
DR   CleanEx; MM_TPM1; -.
DR   Genevestigator; P58771; -.
DR   GermOnline; ENSMUSG00000032366; Mus musculus.
DR   GO; GO:0005862; C:muscle thin filament tropomyosin; TAS:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:MGI.
DR   GO; GO:0060048; P:cardiac muscle contraction; IMP:BHF-UCL.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0003065; P:positive regulation of heart rate by epinephrine; IMP:BHF-UCL.
DR   GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
DR   InterPro; IPR000533; Tropomyosin.
DR   Pfam; PF00261; Tropomyosin; 1.
DR   PRINTS; PR00194; TROPOMYOSIN.
DR   PROSITE; PS00326; TROPOMYOSIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Alternative splicing; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Isopeptide bond; Muscle protein;
KW   Phosphoprotein; Ubl conjugation.
FT   CHAIN         1    284       Tropomyosin alpha-1 chain.
FT                                /FTId=PRO_0000205621.
FT   COILED        1    284       By similarity.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     283    283       Phosphoserine.
FT   CROSSLNK     77     77       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   VAR_SEQ     258    284       DELYAQKLKYKAISEELDHALNDMTSI -> EKVAHAKEEN
FT                                LSMHQMLDQTLLELNNM (in isoform 2).
FT                                /FTId=VSP_006580.
SQ   SEQUENCE   284 AA;  32681 MW;  E25609F597A72F4D CRC64;
     MDAIKKKMQM LKLDKENALD RAEQAEADKK AAEDRSKQLE DELVSLQKKL KGTEDELDKY
     SEALKDAQEK LELAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA
     DESERGMKVI ESRAQKDEEK MEIQEIQLKE AKHIAEDADR KYEEVARKLV IIESDLERAE
     ERAELSEGKC AELEEELKTV TNNLKSLEAQ AEKYSQKEDK YEEEIKVLSD KLKEAETRAE
     FAERSVTKLE KSIDDLEDEL YAQKLKYKAI SEELDHALND MTSI
//
ID   TB10A_MOUSE             Reviewed;         500 AA.
AC   P58802;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2002, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=TBC1 domain family member 10A;
DE   AltName: Full=EBP50-PDX interactor of 64 kDa;
DE            Short=EPI64 protein;
GN   Name=Tbc1d10a; Synonyms=Epi64, Tbc1d10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=21181854; PubMed=11285285; DOI=10.1083/jcb.153.1.191;
RA   Reczek D., Bretscher A.;
RT   "Identification of EPI64, a TBC/rabGAP domain-containing microvillar
RT   protein that binds to the first PDZ domain of EBP50 and E3KARP.";
RL   J. Cell Biol. 153:191-206(2001).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SUBUNIT: Binds to the first PDZ domain of SLC9A3R1 and SLC9A3R2
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell projection, microvillus (By
CC       similarity). Note=Localizes to the microvilli-rich region of the
CC       syncytiotrophoblast (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in most tissues, except for skeletal
CC       muscle.
CC   -!- SIMILARITY: Contains 1 Rab-GAP TBC domain.
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DR   EMBL; BC018300; AAH18300.1; -; mRNA.
DR   IPI; IPI00139383; -.
DR   RefSeq; NP_598784.1; NM_134023.1.
DR   UniGene; Mm.28140; -.
DR   ProteinModelPortal; P58802; -.
DR   SMR; P58802; 85-362.
DR   STRING; P58802; -.
DR   PhosphoSite; P58802; -.
DR   PRIDE; P58802; -.
DR   Ensembl; ENSMUST00000041042; ENSMUSP00000036861; ENSMUSG00000034412.
DR   GeneID; 103724; -.
DR   KEGG; mmu:103724; -.
DR   UCSC; uc007huq.1; mouse.
DR   CTD; 103724; -.
DR   MGI; MGI:2144164; Tbc1d10a.
DR   eggNOG; roNOG07245; -.
DR   HOVERGEN; HBG070028; -.
DR   InParanoid; P58802; -.
DR   OrthoDB; EOG4D7Z5V; -.
DR   NextBio; 356077; -.
DR   ArrayExpress; P58802; -.
DR   Bgee; P58802; -.
DR   CleanEx; MM_TBC1D10A; -.
DR   Genevestigator; P58802; -.
DR   GermOnline; ENSMUSG00000034412; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005902; C:microvillus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005097; F:Rab GTPase activator activity; IEA:InterPro.
DR   GO; GO:0032313; P:regulation of Rab GTPase activity; IEA:InterPro.
DR   InterPro; IPR000195; RabGAP/TBC_dom.
DR   Pfam; PF00566; TBC; 1.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; RabGAP_TBC; 2.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Phosphoprotein.
FT   CHAIN         1    500       TBC1 domain family member 10A.
FT                                /FTId=PRO_0000208036.
FT   DOMAIN      111    299       Rab-GAP TBC.
FT   REGION      497    500       Binding to the PDZ domain of EBP50 (By
FT                                similarity).
FT   MOD_RES      40     40       Phosphoserine (By similarity).
FT   MOD_RES      43     43       Phosphoserine (By similarity).
FT   MOD_RES     407    407       Phosphoserine.
FT   MOD_RES     495    495       Phosphoserine (By similarity).
SQ   SEQUENCE   500 AA;  56202 MW;  15954DB7A4E3A9B6 CRC64;
     MAKSSRENGP REPAAGGSLS GTRESLAQGP DAATADELSS LGSDSEANGF AERRIDKFGF
     IVGSQGAEGA LEEVPLEVLR QRESKWLDML NNWDKWMAKK HKKIRLRCQK GIPPSLRGRA
     WQYLSGGKVK LQQNPGKFDE LDMSPGDPKW LDVIERDLHR QFPFHEMFVS RGGHGQQDLF
     RVLKAYTLYR PEEGYCQAQA PIAAVLLMHM PAEQAFWCLV QVCEKYLPGY YSEKLEAIQL
     DGEILFSLLQ KVSPVAHKHL SRQKIDPLLY MTEWFMCAFA RTLPWSSVLR VWDMFFCEGV
     KIIFRVGLVL LKHALGSPEK LKACQGQYET IEQLRSLSPK IMQEAFLVQE VIELPVTERQ
     IEREHLIQLR RWQETRGELE CRSLPRMHGA KAILDAEPGP RPALQPSPSI RLPPDAALLS
     SKAKPHKQAQ KEQKRTKTSA QLDKSPGLSQ ATVVTAAGDA CPPQGVSPKD PVPQDPTPQN
     LACHHSQESL TSQESEDTYL
//
ID   TB182_MOUSE             Reviewed;        1720 AA.
AC   P58871; A2BH84; Q6ZPI8;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=182 kDa tankyrase-1-binding protein;
GN   Name=Tnks1bp1; Synonyms=Kiaa1741, Tab182;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 397-1720.
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 812-1720.
RC   TISSUE=Colon, and Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1611, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1611 AND SER-1612, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1370; SER-1373;
RP   SER-1375; SER-1611 AND SER-1612, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1375, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-533; SER-539; SER-568;
RP   SER-602; SER-887; THR-890; SER-912; SER-974; SER-1375; SER-1442;
RP   SER-1611 AND SER-1612, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-974, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429; SER-866; SER-1131;
RP   SER-1611; SER-1612 AND SER-1657, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-692; SER-1611 AND
RP   SER-1612, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- SUBUNIT: Binds to the ANK repeat domain of TNKS1 and TNKS2 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity). Chromosome (By similarity).
CC       Note=Colocalizes with chromosomes during mitosis, and in the
CC       cytoplasm with cortical actin (By similarity).
CC   -!- PTM: ADP-ribosylated by TNKS1 (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM22340.1; Type=Erroneous gene model prediction;
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DR   EMBL; BX546441; CAM22340.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AK129436; BAC98246.1; -; mRNA.
DR   EMBL; BC024499; AAH24499.1; -; mRNA.
DR   EMBL; BC025943; AAH25943.1; -; mRNA.
DR   IPI; IPI00459443; -.
DR   RefSeq; NP_001074729.1; NM_001081260.2.
DR   UniGene; Mm.23606; -.
DR   STRING; P58871; -.
DR   PhosphoSite; P58871; -.
DR   PRIDE; P58871; -.
DR   Ensembl; ENSMUST00000111605; ENSMUSP00000107232; ENSMUSG00000033955.
DR   GeneID; 228140; -.
DR   KEGG; mmu:228140; -.
DR   CTD; 228140; -.
DR   MGI; MGI:2446193; Tnks1bp1.
DR   eggNOG; roNOG08060; -.
DR   GeneTree; ENSGT00530000064083; -.
DR   HOGENOM; HBG282914; -.
DR   HOVERGEN; HBG080593; -.
DR   InParanoid; P58871; -.
DR   OMA; GVWRLDS; -.
DR   NextBio; 378943; -.
DR   ArrayExpress; P58871; -.
DR   Bgee; P58871; -.
DR   CleanEx; MM_TNKS1BP1; -.
DR   Genevestigator; P58871; -.
DR   GermOnline; ENSMUSG00000033955; Mus musculus.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   ADP-ribosylation; Chromosome; Cytoplasm; Cytoskeleton; Nucleus;
KW   Phosphoprotein.
FT   CHAIN         1   1720       182 kDa tankyrase-1-binding protein.
FT                                /FTId=PRO_0000072438.
FT   REGION      209   1563       Acidic.
FT   REGION     1440   1532       Tankyrase-binding (By similarity).
FT   MOTIF      1620   1626       Nuclear localization signal (Potential).
FT   MOTIF      1714   1719       Nuclear localization signal (Potential).
FT   COMPBIAS   1003   1333       Gly-rich.
FT   COMPBIAS   1566   1720       Arg/Glu/Lys-rich (charged).
FT   MOD_RES     178    178       Phosphoserine (By similarity).
FT   MOD_RES     220    220       Phosphoserine (By similarity).
FT   MOD_RES     238    238       Phosphothreonine (By similarity).
FT   MOD_RES     286    286       Phosphoserine (By similarity).
FT   MOD_RES     300    300       Phosphoserine (By similarity).
FT   MOD_RES     429    429       Phosphoserine.
FT   MOD_RES     437    437       Phosphoserine (By similarity).
FT   MOD_RES     496    496       Phosphoserine (By similarity).
FT   MOD_RES     500    500       Phosphoserine (By similarity).
FT   MOD_RES     506    506       Phosphoserine (By similarity).
FT   MOD_RES     520    520       Phosphoserine (By similarity).
FT   MOD_RES     533    533       Phosphothreonine.
FT   MOD_RES     539    539       Phosphoserine.
FT   MOD_RES     568    568       Phosphoserine.
FT   MOD_RES     602    602       Phosphoserine.
FT   MOD_RES     673    673       Phosphoserine (By similarity).
FT   MOD_RES     692    692       Phosphoserine.
FT   MOD_RES     713    713       Phosphoserine (By similarity).
FT   MOD_RES     715    715       Phosphoserine (By similarity).
FT   MOD_RES     763    763       Phosphoserine (By similarity).
FT   MOD_RES     807    807       Phosphoserine (By similarity).
FT   MOD_RES     866    866       Phosphoserine.
FT   MOD_RES     887    887       Phosphoserine.
FT   MOD_RES     890    890       Phosphothreonine.
FT   MOD_RES     912    912       Phosphoserine.
FT   MOD_RES     974    974       Phosphoserine.
FT   MOD_RES     976    976       Phosphoserine (By similarity).
FT   MOD_RES     980    980       Phosphoserine (By similarity).
FT   MOD_RES    1017   1017       Phosphoserine (By similarity).
FT   MOD_RES    1022   1022       Phosphoserine (By similarity).
FT   MOD_RES    1096   1096       Phosphoserine (By similarity).
FT   MOD_RES    1126   1126       Phosphoserine (By similarity).
FT   MOD_RES    1131   1131       Phosphoserine.
FT   MOD_RES    1171   1171       Phosphoserine (By similarity).
FT   MOD_RES    1241   1241       Phosphoserine (By similarity).
FT   MOD_RES    1275   1275       Phosphothreonine (By similarity).
FT   MOD_RES    1290   1290       Phosphoserine (By similarity).
FT   MOD_RES    1321   1321       Phosphoserine (By similarity).
FT   MOD_RES    1324   1324       Phosphoserine (By similarity).
FT   MOD_RES    1370   1370       Phosphoserine.
FT   MOD_RES    1373   1373       Phosphoserine.
FT   MOD_RES    1375   1375       Phosphoserine.
FT   MOD_RES    1395   1395       Phosphoserine (By similarity).
FT   MOD_RES    1429   1429       Phosphoserine (By similarity).
FT   MOD_RES    1442   1442       Phosphoserine.
FT   MOD_RES    1463   1463       Phosphoserine (By similarity).
FT   MOD_RES    1466   1466       Phosphoserine (By similarity).
FT   MOD_RES    1545   1545       Phosphoserine (By similarity).
FT   MOD_RES    1549   1549       Phosphoserine (By similarity).
FT   MOD_RES    1554   1554       Phosphothreonine (By similarity).
FT   MOD_RES    1607   1607       Phosphoserine (By similarity).
FT   MOD_RES    1611   1611       Phosphoserine.
FT   MOD_RES    1612   1612       Phosphoserine.
FT   MOD_RES    1643   1643       Phosphoserine (By similarity).
FT   MOD_RES    1645   1645       Phosphoserine (By similarity).
FT   MOD_RES    1657   1657       Phosphoserine.
FT   MOD_RES    1706   1706       Phosphoserine (By similarity).
FT   CONFLICT    941    941       N -> D (in Ref. 2; BAC98246 and 3;
FT                                AAH25943).
SQ   SEQUENCE   1720 AA;  181825 MW;  7CFF0046559B923D CRC64;
     MKGSTLREGT AMASPLPQDM EEELAPVGSE PGDPRAKPPV KPKPRGLPSK PALPAKPSLL
     VPVGPRPPRG PLAELPSARK MNMLAGPQPY GVSKRPLPFA PRPSAEATAG GDVTQESGKE
     DAGKEDLPPL TPPARCAALG GVRKAPAPFR PSSERFAACT VEEILAKMEQ PRKEILASPD
     RLWGSRLTFN HDGSSRYGPR TYGAPCPREE DSKSPAKGRS QEGTAEIPAE CQEEHSKTPE
     ERNLTSSPAM NGDLAKLACS EAPTDVSKTW VTSSADPVSE HGGSTSAVRL ANISVPASES
     PRLSSRPSSP CHSQLSETQS PAASEASSIC LPVTPASPSA VLPAEPPGHS PSSELPAEAA
     PETLSPNSSP VETVSGHHSP EQPPVLLPQL LTEGAELPDI TRTFPCGEEA AARGHTESRP
     SSLAQRRFSE GVLQPPSQDQ EKLGGSLATL PQGQGSQSAL DRPFGSGTES NWSLSQSFEW
     TFPTRPSGLG VWRLDSPPPS PITEASEAAE AAEADSWAVS GRGEGVSQVG PGTPPAPESP
     RKPISGVQGN DPGISLPQRD DGESQPRSPA LLPSTVEGPP GAPLLQAKEN YEDQEPLVGH
     ESPITLAARE AALPVLEPAL GQQQPTPSDQ PCILFVDVPD PEQALSTEED VVTLGWAETT
     LPMTEAQEPC SVSPEPTGPE SSSRWLDDLL ASPPPNSGSA RRAAGAELKD RQSPSTCSEG
     LLGWAQKDLQ SEFGVATDSH HSSFGSSSWS QDTSQNYSLG GRSPVGDTGL GKRDWSSKCG
     QGSGEGSTRE WASRHSLGQE VIGIGGSQDE SEVPVRERAV GRPAQLGAQG LEADAQQWEF
     GKRESQDPHS IHDKELQDQE FGKRDSLGSF STRDASLQDW EFGKRASVST NQDTDENDQE
     LGMKNLSRGY SSQDAEEQDR EFEKRDSVLD IHGSRATAQQ NQEFGKSAWF QDYSSGGGGS
     RVLGSQERGF GIRSLSSGFS PEEAQQQDEE FEKKTPVGED RFCEASRDVG HLEEGASGGL
     LSPSTPHSRD GAARPKDEGS WQDGDSSQEI TRLQGRMQAE SQSPTNVDLE DKEREQRGWA
     GEFSLGVAAQ SEAAFSPGRQ DWSRDVCVEA SESSYQFGII GNDRVSGAGL SPSRKSGGGH
     FVPPGETKAG AVDWTDQLGL RNLEVSSCVS SEGPSEAREN VVGQMGWSDS LGLNNGDLAR
     RLGTGESEEP RSLGVGEKDW TSSVEARNRD LPGQAEVGRH SQARESGVGE PDWSGAEAGE
     FLKSRERGVG QADWTPDLGL RNMAPGAGCS PGEPRELGVG QVDWGDDLGL RNLEVSCDLE
     SGGSRGCGVG QMDWAQDLGL RNLRLCGAPS EVRECGVGRV GPDLELDPKS SGSLSPGLET
     EDPLEARELG VGEISGPETQ GEDSSSPSFE TPSEDTGMDT GEAPSLGASP SSCLTRSPPS
     GSQSLLEGIM TASSSKGAPQ RESAASGSRV LLEEEGLAAG AGQGEPQEPS RAPLPSSRPQ
     PDGEASQVEE VDGTWSLTGA ARQNEQASAP PPRRPPRGLL PSCPSEDFSF IEDTEILDSA
     MYRSRANLGR KRGHRAPAIR PGGTLGLSET ADSDTRLFQD STEPRASRVP SSDEEVVEEP
     QSRRTRMSLG TKGLKVNLFP GLSPSALKAK LRSRNRSAEE GEVTESKSSQ KESSVQRSKS
     CKVPGLGKPL TLPPKPEKSS GSEGSSPNWL QALKLKKKKI
//
ID   RHBL3_MOUSE             Reviewed;         404 AA.
AC   P58873;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Rhomboid-related protein 3;
DE            EC=3.4.21.105;
DE   AltName: Full=Ventrhoid transmembrane protein;
GN   Name=Rhbdl3; Synonyms=Rhbdl4, Vrho;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=21898529; PubMed=11900977; DOI=10.1016/S0925-4773(01)00655-4;
RA   Jaszai J., Brand M.;
RT   "Cloning and expression of Ventrhoid, a novel vertebrate homologue of
RT   the Drosophila EGF pathway gene Rhomboid.";
RL   Mech. Dev. 113:73-77(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in regulated intramembrane proteolysis
CC       and the subsequent release of functional polypeptides from their
CC       membrane anchors (By similarity).
CC   -!- CATALYTIC ACTIVITY: Cleaves type-1 transmembrane domains using a
CC       catalytic dyad composed of serine and histidine that are
CC       contributed by different transmembrane domains.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Probable).
CC   -!- DEVELOPMENTAL STAGE: At E8, expression is limited to the
CC       developing central nervous system (CNS). From E9 on detected in
CC       the ventral forebrain, pretectum, dorsal diencephalon,
CC       metencephalon, the ventral spinal neural tube, in the ectoderm of
CC       the developing mandibular arches and the developing hindgut.
CC   -!- SIMILARITY: Belongs to the peptidase S54 family.
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; AJ313479; CAC86144.1; -; mRNA.
DR   EMBL; BC054784; AAH54784.1; -; mRNA.
DR   EMBL; BC056969; AAH56969.1; -; mRNA.
DR   IPI; IPI00312148; -.
DR   RefSeq; NP_631974.1; NM_139228.3.
DR   UniGene; Mm.194148; -.
DR   ProteinModelPortal; P58873; -.
DR   SMR; P58873; 34-101.
DR   MEROPS; S54.006; -.
DR   PhosphoSite; P58873; -.
DR   PRIDE; P58873; -.
DR   Ensembl; ENSMUST00000017836; ENSMUSP00000017836; ENSMUSG00000017692.
DR   GeneID; 246104; -.
DR   KEGG; mmu:246104; -.
DR   UCSC; uc007klt.1; mouse.
DR   CTD; 246104; -.
DR   MGI; MGI:2179276; Rhbdl3.
DR   eggNOG; roNOG05928; -.
DR   HOGENOM; HBG716767; -.
DR   HOVERGEN; HBG059476; -.
DR   InParanoid; P58873; -.
DR   OMA; PSFVAHL; -.
DR   OrthoDB; EOG4M398V; -.
DR   PhylomeDB; P58873; -.
DR   BRENDA; 3.4.21.105; 244.
DR   NextBio; 387083; -.
DR   ArrayExpress; P58873; -.
DR   Bgee; P58873; -.
DR   CleanEx; MM_RHBDL3; -.
DR   Genevestigator; P58873; -.
DR   GermOnline; ENSMUSG00000017692; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002610; Peptidase_S54_rhomboid.
DR   InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR   InterPro; IPR017213; Peptidase_S54_rhomboid_met.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   PANTHER; PTHR22936; Peptidase_S54_rhomboid; 1.
DR   Pfam; PF01694; Rhomboid; 1.
DR   PIRSF; PIRSF037470; Rhomboid; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   2: Evidence at transcript level;
KW   Hydrolase; Membrane; Protease; Repeat; Serine protease; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    404       Rhomboid-related protein 3.
FT                                /FTId=PRO_0000206178.
FT   TRANSMEM    164    184       Helical; (Potential).
FT   TRANSMEM    227    247       Helical; (Potential).
FT   TRANSMEM    250    270       Helical; (Potential).
FT   TRANSMEM    274    294       Helical; (Potential).
FT   TRANSMEM    305    324       Helical; (Potential).
FT   TRANSMEM    338    358       Helical; (Potential).
FT   TRANSMEM    371    391       Helical; (Potential).
FT   DOMAIN       34     69       EF-hand 1.
FT   DOMAIN       70    105       EF-hand 2.
FT   ACT_SITE    278    278       Nucleophile (By similarity).
FT   ACT_SITE    343    343       By similarity.
SQ   SEQUENCE   404 AA;  45266 MW;  D738F903C45AC524 CRC64;
     MGEHPSPGPA VAACAEAERI EELEPEAEER LPAAPEDHWK VLFEKFDPGS TGYISTGKFR
     SLLESHSSKL DPHKKEVLLA LADSHADGQI CYQDFVNLMS NKRSNSFRQA ILQGNRRLSS
     KALLEEKGLS LSQRLIRHVA YETLPREIDR KWYYDSYTCC PPPWFMITIT LLEVALFLYN
     GVLLDQFVLQ VTHPRYLKNS LVYHPQLRAQ AWRYVTYIFM HAGVEQLGLN VALQLLVGVP
     LEMVHGATRI GLVYVAGVVA GSLAVSVADM TAPVVGSSGG VYALVSAHLA NIVMNWSGMK
     CQFKLLRMAV ALICMSMEFG RAVWLRFHPS AYPPCPHPSF VAHLGGVAVG ITLGVVVLRN
     YEQRLQDQSL WWIFVTMYTI FVLFAVFWNI FAYTLLDLKL PPAP
//
ID   B2L13_MOUSE             Reviewed;         434 AA.
AC   P59017;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2002, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Bcl-2-like protein 13;
DE            Short=Bcl2-L-13;
DE   AltName: Full=Bcl-rambo;
DE   AltName: Full=Protein Mil1;
GN   Name=Bcl2l13; Synonyms=Mil1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: May promote the activation of caspase-3 and apoptosis.
CC   -!- SUBUNIT: Monomer (Probable).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Belongs to the Bcl-2 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC027307; AAH27307.1; -; mRNA.
DR   EMBL; BC029016; AAH29016.1; -; mRNA.
DR   IPI; IPI00321499; -.
DR   RefSeq; NP_705736.1; NM_153516.2.
DR   UniGene; Mm.27990; -.
DR   ProteinModelPortal; P59017; -.
DR   STRING; P59017; -.
DR   PhosphoSite; P59017; -.
DR   PRIDE; P59017; -.
DR   Ensembl; ENSMUST00000009256; ENSMUSP00000009256; ENSMUSG00000009112.
DR   GeneID; 94044; -.
DR   KEGG; mmu:94044; -.
DR   CTD; 94044; -.
DR   MGI; MGI:2136959; Bcl2l13.
DR   eggNOG; roNOG12308; -.
DR   HOGENOM; HBG126613; -.
DR   HOVERGEN; HBG050648; -.
DR   InParanoid; P59017; -.
DR   OrthoDB; EOG40VVPX; -.
DR   NextBio; 351999; -.
DR   ArrayExpress; P59017; -.
DR   Bgee; P59017; -.
DR   CleanEx; MM_BCL2L13; -.
DR   Genevestigator; P59017; -.
DR   GermOnline; ENSMUSG00000009112; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; ISS:UniProtKB.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR002475; Bcl2-like_apoptosis.
DR   InterPro; IPR000712; Bcl2_BH.
DR   Pfam; PF00452; Bcl-2; 1.
DR   SMART; SM00337; BCL; 1.
DR   PROSITE; PS50062; BCL2_FAMILY; 1.
DR   PROSITE; PS01080; BH1; FALSE_NEG.
DR   PROSITE; PS01258; BH2; FALSE_NEG.
DR   PROSITE; PS01259; BH3; FALSE_NEG.
DR   PROSITE; PS01260; BH4_1; FALSE_NEG.
DR   PROSITE; PS50063; BH4_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Apoptosis; Membrane; Mitochondrion; Phosphoprotein; Repeat;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    434       Bcl-2-like protein 13.
FT                                /FTId=PRO_0000143074.
FT   TRANSMEM    409    429       Helical; (Potential).
FT   REPEAT      243    253       A.
FT   REPEAT      258    268       A; approximate.
FT   MOTIF        14     30       BH4.
FT   MOTIF        97    113       BH3.
FT   MOTIF       144    154       BH1.
FT   MOTIF       190    203       BH2.
FT   COMPBIAS    204    209       Poly-Glu.
FT   COMPBIAS    308    379       Glu-rich.
FT   MOD_RES     343    343       Phosphoserine.
FT   MOD_RES     387    387       Phosphoserine.
FT   CONFLICT      8      8       P -> S (in Ref. 1; AAH29016).
FT   CONFLICT     66     66       A -> T (in Ref. 1; AAH29016).
FT   CONFLICT    326    326       A -> T (in Ref. 1; AAH29016).
SQ   SEQUENCE   434 AA;  46669 MW;  74FBBDE5CEE7DB16 CRC64;
     MASSTTAPLG FHYETKYVVL SYLGLLSQEK QQGPSPPGVQ LDVAPQSLNP EVLLKLKSEI
     EEELKALDKE VSEAFTSTGF DCHTSPVFSP ANPESSIEDC LAHLGERVSQ DLKEPLQKAL
     QTILSQPVTY EAYRECTVET AVHASGWNKL LVPLVLLQHL LLELTRRGQE PLRMLLQFGV
     MYLEEHAAEF IIQQGGWGSV FSLEPEEEEY PGIIAEDSND IYILPSDNSG QVSPPESPTV
     TTSWQSESLP VSLSASQSWH TESLPVSLGP ESWQQIAMDP EEVKSLDSSG AGEKSENNSS
     NSDIVHVEKE EVPEEAFPGA AAPLLAQVPT VEAPEMMRAE KTSPTPSVFV ELGEEELEAV
     TARPEAVERA EGAAQLSEER AGSRKKSHTG EAAAVRGAKS GLPAEGKAVL LFGGAAAVAI
     LAVAVGVALA LRRK
//
ID   PCIF1_MOUSE             Reviewed;         706 AA.
AC   P59114;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2002, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Phosphorylated CTD-interacting factor 1;
GN   Name=Pcif1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May play a role in transcription elongation or in
CC       coupling transcription to pre-mRNA processing through its
CC       association with the phosphorylated C-terminal domain (CTD) of
CC       RNAPII largest subunit (By similarity).
CC   -!- SUBUNIT: Interacts with the phosphorylated C-terminal domain (CTD)
CC       of RNAPII largest subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- DOMAIN: The WW domain is sufficient for direct and specific
CC       interaction with the phosphorylated CTD of RNAPII largest subunit
CC       (By similarity).
CC   -!- SIMILARITY: Contains 1 WW domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; BC031431; AAH31431.1; -; mRNA.
DR   IPI; IPI00173138; -.
DR   RefSeq; NP_666241.1; NM_146129.3.
DR   UniGene; Mm.241134; -.
DR   ProteinModelPortal; P59114; -.
DR   SMR; P59114; 40-86.
DR   STRING; P59114; -.
DR   PhosphoSite; P59114; -.
DR   PRIDE; P59114; -.
DR   Ensembl; ENSMUST00000041643; ENSMUSP00000039555; ENSMUSG00000039849.
DR   GeneID; 228866; -.
DR   KEGG; mmu:228866; -.
DR   UCSC; uc008nwp.1; mouse.
DR   CTD; 228866; -.
DR   MGI; MGI:2443858; Pcif1.
DR   eggNOG; roNOG04653; -.
DR   HOGENOM; HBG357067; -.
DR   HOVERGEN; HBG053525; -.
DR   InParanoid; P59114; -.
DR   OMA; NCYFKQY; -.
DR   OrthoDB; EOG4NS3B5; -.
DR   PhylomeDB; P59114; -.
DR   NextBio; 379220; -.
DR   ArrayExpress; P59114; -.
DR   Bgee; P59114; -.
DR   Genevestigator; P59114; -.
DR   GermOnline; ENSMUSG00000039849; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR022035; PCIF1_WW.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Pfam; PF12237; PCIF1_WW; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF51045; WW_Rsp5_WWP; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; FALSE_NEG.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein.
FT   CHAIN         1    706       Phosphorylated CTD-interacting factor 1.
FT                                /FTId=PRO_0000076088.
FT   DOMAIN       43     77       WW.
FT   MOTIF       109    113       Nuclear localization signal (Potential).
FT   MOTIF       668    686       Nuclear localization signal (Potential).
FT   COMPBIAS    675    686       Poly-Ser.
FT   MOD_RES      19     19       Phosphoserine (By similarity).
FT   MOD_RES      30     30       Phosphoserine.
FT   MOD_RES     116    116       Phosphoserine (By similarity).
FT   MOD_RES     143    143       Phosphoserine (By similarity).
FT   MOD_RES     144    144       Phosphoserine (By similarity).
FT   MOD_RES     152    152       Phosphothreonine (By similarity).
SQ   SEQUENCE   706 AA;  80504 MW;  48646523758CF4FD CRC64;
     MANENHGSPR EGASLLSHSP GTSSQSQPCS PKPVRLVQDL PEELVHAGWE KCWSRRESRP
     YYFNRFTNQS LWEMPVLGQH DVLSDPLGLN ATPLPQDSSL VETPPVENKS RKRQLSEEQP
     SGNGVKKPKI EIPVTPTSQS VPSSPSIPGT PTLKIWGSST EDKQAALLRP TEVYWDLDIQ
     TNAVIKHRGP SEVLPPHPDV ELLRSQLILK LRQHYRELCQ QREGIEPPRE SFNRWMLERK
     VVDKGCDPLL PSNCEPVVSP SMFREIMNDI PIRLSRIKFR EEAKRLLFKY AEAARRLIES
     RSASPDSRKV VKWNVEDTFS WLRKEHSASK EDYMDRLEHL RRQCGPHVSA AAKDSVEGIC
     SKIYHISLEY VKRIREKHLA VLKENNIPEE VEASELEPRL VYCYPVRLAV SAPPMPSVEM
     HVENSVVCIR YKGEMVKVSR SYFSKLWLLY RYSCVDDSAF ERFLPRVWCL LRRYQMMFGV
     GLYEGTGLQG SLPVHVFETL HRLFGVSFEC FASPLNCYFR QYCSAFPDTD GYFGSRGPCL
     DFTPLSGSFE ANPPFCEELM DAMVSHFEKL LESSAEPLSF IVFIPEWREP PTPALTRMEQ
     SRFKRHQLVL PAFEHEYRSG SQHICKKEEM HYKAVHNTAV LFLQNGPGFA KWGPTPERLQ
     ELTAAYKQSG RSHGSSSSSS SSSSSSEAKD RDSGREQGPS REPHPT
//
ID   NPHP4_MOUSE             Reviewed;        1425 AA.
AC   P59240;
DT   27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JAN-2003, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Nephrocystin-4;
DE   AltName: Full=Nephroretinin;
GN   Name=Nphp4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=22242588; PubMed=12244321; DOI=10.1038/ng996;
RA   Mollet G., Salomon R., Gribouval O., Silbermann F., Bacq D.,
RA   Landthaler G., Milford D., Nayir A., Rizzoni G., Antignac C.,
RA   Saunier S.;
RT   "The gene mutated in juvenile nephronophthisis type 4 encodes a novel
RT   protein that interacts with nephrocystin.";
RL   Nat. Genet. 32:300-305(2002).
RN   [2]
RP   ERRATUM.
RA   Mollet G., Salomon R., Gribouval O., Silbermann F., Bacq D.,
RA   Landthaler G., Milford D., Nayir A., Rizzoni G., Antignac C.,
RA   Saunier S.;
RL   Nat. Genet. 32:459-459(2002).
CC   -!- SUBUNIT: Interacts with NPHP1 and RPGRIP1L (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body.
CC       Cytoplasm, cytoskeleton, centrosome (By similarity).
CC   -!- SIMILARITY: Belongs to the NPHP4 family.
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DR   EMBL; AY118229; AAM78559.1; -; mRNA.
DR   IPI; IPI00177203; -.
DR   RefSeq; NP_700473.2; NM_153424.2.
DR   UniGene; Mm.302496; -.
DR   STRING; P59240; -.
DR   PhosphoSite; P59240; -.
DR   PRIDE; P59240; -.
DR   Ensembl; ENSMUST00000056567; ENSMUSP00000049920; ENSMUSG00000039577.
DR   Ensembl; ENSMUST00000081393; ENSMUSP00000080128; ENSMUSG00000039577.
DR   GeneID; 260305; -.
DR   KEGG; mmu:260305; -.
DR   UCSC; uc008wap.1; mouse.
DR   CTD; 260305; -.
DR   MGI; MGI:2384210; Nphp4.
DR   eggNOG; roNOG12446; -.
DR   HOGENOM; HBG357149; -.
DR   HOVERGEN; HBG024036; -.
DR   InParanoid; P59240; -.
DR   OrthoDB; EOG47M207; -.
DR   NextBio; 392081; -.
DR   ArrayExpress; P59240; -.
DR   Bgee; P59240; -.
DR   CleanEx; MM_NPHP4; -.
DR   Genevestigator; P59240; -.
DR   GermOnline; ENSMUSG00000039577; Mus musculus.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR   GO; GO:0005932; C:microtubule basal body; IEA:UniProtKB-SubCell.
PE   2: Evidence at transcript level;
KW   Cell projection; Cilium; Cytoplasm; Cytoskeleton.
FT   CHAIN         1   1425       Nephrocystin-4.
FT                                /FTId=PRO_0000159770.
SQ   SEQUENCE   1425 AA;  157224 MW;  4B621E2E88174A7A CRC64;
     MGDWHRAFTQ NTLVPPHPQR ARQLGKESTA FQCILKWLDG PLIKQGILDM LSELECHLRV
     TLFDVTYKHF FGRTWKTTVK PTNQPSKQPP RITFNEPLYF HTTLSHPSIV AVVEVVTEGR
     KRDGTLQLLS CGFGILRIFG NKPESPTSAA QDKRLRLYHG TPRALLHPLL QDPIEQNKFM
     RLMENCSLQY TLKPHPPLEP AFHLLPENLL VSGFQQIPGL LPPHGDTGDA LRKPRFQKPT
     TWHLDDLFFT LYPSLEKFEE ELVQLLISDR EGVGLLDSGT LEVLERRLHV CVHNGLGFVQ
     RPQVVVLVPE MDVALTRSAS FSRKISASSK NSSGNQALVL RSHLRLPEMV SHPAFAIVFQ
     LEYVFNSPSG ADGGASSPTS ISSVACMHMV RWAVWNPDLE VGPGKVTLPL QGGVQQNPSR
     CLVYKVPSAS MSSEEVKQVE SGTIQFQFSL SSDGPTEHAN GPRVGRRSSR KMPASPSGTP
     APAARDLAAT QDSPVGPGLS LSQLTASPLS PALQSSSKPP LQPPDSSQSP EGPQLQAESV
     LESRVSHLEA DLSQPASLQG TPAVEHLQEL PFTPLHAPIV VGAQTRSSRS QLSRAAMVLL
     QSSGFPEILD ASQQPVEAVN PIDPVRFNPQ KEESDCLRGN EIVLQFLAFS RAAQDCPGTP
     WPQTVYFTFQ FYRFPPETTP RLQLVKLDGT GKSGSGSLSH ILVPINKDGS FDAGSPGLQL
     RYMVDPGFLK PGEQRWFAHY LAAQTLQVDV WDGDSLLLIG SAGVQMKHLL RQGRPAVQVS
     HELEVVATEY EQEMMAVSGD VAGFGSVKPI GVHTVVKGRL HLTLANVGHA CEPRARGSNL
     LPPSRSRVIS NDGASFFSGG SLLIPGGPKR KRVVQAQRLA DVDSELAAML LTHTRAGQGP
     QAAGQEADAV HKRKLERMRL VRLQEAGGDS DSXRISLLAQ HSVRAQHSRD LQVIDAYRER
     TKAESIAGVL SQAITTHHTL YATLGTAEFF EFALKNPHNT QHTVAIEIDS PELSIILDSQ
     EWRYFKEATG LHTPLEEDMF HLRGSLAPQL YLRPRETAHI PLKFQSFSVG PLAPTQAPAE
     VITEKDAESG PLWKCSAMPT KHAKVLFRVE TGQLIAVLCL TVEPQPHVVD QVFRFYHPEL
     TFLKKAIRLP PWHTLPGAPV GMPGEDPPVH VRCSDPNVIC EAQNVGPGEP RDVFLKVASG
     PSPEIKDFFV VIYADRWLAV PVQTWQVCLH SLQRVDVSCV AGQLTRLSLV LRGTQTVRKV
     RAFTSHPQEL KTDPAGVFVL PPHGVQDLHV GVRPRRAGSR FVHLNLVDID YHQLVASWLV
     CLSCRQPLIS KAFEITMAAG DEKGTNKRIT YTNPYPSRRT YRLHSDRPEL LRFKEDSFQV
     AGGETYTIGL RFLPSGSAGQ EEILIYINDH EDKNEETFCV KVLYQ
//
ID   RHG39_MOUSE             Reviewed;        1107 AA.
AC   P59281; Q69ZD4; Q6P9R6;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 2.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Rho GTPase-activating protein 39;
GN   Name=Arhgap39; Synonyms=D15Wsu169e, Kiaa1688;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 11-1107 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-597, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169 AND SER-597, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-597, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P59281-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P59281-2; Sequence=VSP_013707;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 MyTH4 domain.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -!- SIMILARITY: Contains 2 WW domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32510.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK173232; BAD32510.1; ALT_INIT; mRNA.
DR   EMBL; BC060637; AAH60637.1; -; mRNA.
DR   EMBL; AK035479; BAC29074.1; -; mRNA.
DR   IPI; IPI00347255; -.
DR   IPI; IPI00469950; -.
DR   RefSeq; NP_001161760.1; NM_001168288.1.
DR   RefSeq; NP_940812.2; NM_198420.2.
DR   UniGene; Mm.322931; -.
DR   UniGene; Mm.481024; -.
DR   ProteinModelPortal; P59281; -.
DR   SMR; P59281; 28-96, 911-1103.
DR   STRING; P59281; -.
DR   PhosphoSite; P59281; -.
DR   PRIDE; P59281; -.
DR   Ensembl; ENSMUST00000036176; ENSMUSP00000036697; ENSMUSG00000033697.
DR   Ensembl; ENSMUST00000077821; ENSMUSP00000076993; ENSMUSG00000033697.
DR   GeneID; 223666; -.
DR   KEGG; mmu:223666; -.
DR   NMPDR; fig|10090.3.peg.30170; -.
DR   UCSC; uc007wmh.1; mouse.
DR   UCSC; uc007wmi.1; mouse.
DR   CTD; 223666; -.
DR   MGI; MGI:107858; Arhgap39.
DR   eggNOG; roNOG09036; -.
DR   GeneTree; ENSGT00390000003161; -.
DR   HOGENOM; HBG446309; -.
DR   HOVERGEN; HBG052205; -.
DR   InParanoid; P59281; -.
DR   OMA; KHTQGLF; -.
DR   OrthoDB; EOG4D26P6; -.
DR   NextBio; 376800; -.
DR   ArrayExpress; P59281; -.
DR   Bgee; P59281; -.
DR   Genevestigator; P59281; -.
DR   GermOnline; ENSMUSG00000033697; Mus musculus.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR000857; MyTH4_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF00784; MyTH4; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS51016; MYTH4; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; FALSE_NEG.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Nucleus; Phosphoprotein; Repeat.
FT   CHAIN         1   1107       Rho GTPase-activating protein 39.
FT                                /FTId=PRO_0000076093.
FT   DOMAIN       25     58       WW 1.
FT   DOMAIN       63     97       WW 2.
FT   DOMAIN      715    867       MyTH4.
FT   DOMAIN      914   1102       Rho-GAP.
FT   MOD_RES     169    169       Phosphoserine.
FT   MOD_RES     244    244       Phosphoserine (By similarity).
FT   MOD_RES     362    362       Phosphoserine (By similarity).
FT   MOD_RES     384    384       Phosphoserine (By similarity).
FT   MOD_RES     402    402       Phosphoserine (By similarity).
FT   MOD_RES     403    403       Phosphoserine (By similarity).
FT   MOD_RES     597    597       Phosphoserine.
FT   MOD_RES     683    683       Phosphoserine (By similarity).
FT   VAR_SEQ     834    864       Missing (in isoform 2).
FT                                /FTId=VSP_013707.
FT   CONFLICT   1032   1032       R -> Q (in Ref. 2; AAH60637).
SQ   SEQUENCE   1107 AA;  125206 MW;  BCEF3C200664DF31 CRC64;
     MSQAQDYECR SHHVDEQEPR IPGSSTRLEW VEIIEPRTRE RMYANLVTGE CVWDPPAGVR
     IKRTSEDQWW ELFDPNTSRF YYYSAASQRT VWHRPQNCDI IPLAKLQTLK QNTESPRASA
     DNSPGRGSRD GSTGSSLEPE LEERTQELPV RSGRATTLVT SKEDTSSCSP PGVLLEKDYE
     VYRDYSADGQ LLHYRTSSLR WNSGNKERML IKVADREPSF LTPQGNGYPA DNQPGGHHRR
     PSGSQHSPNL QTFVPDTDGT VFFPERRPSP FLRRAELSGN CSPLLIQPRK PSSDSQPSSP
     RYGYEPPLYE EPPVEYQAPI YDEPPMDVQF EANSPYQTGS PQRSPGRKPH PFLQTTKQTP
     TSPCQQLMRT KQKCPERFLS LEYSPVGKEY VRQLVYVEQA GSSPKLRAGP RHKYAPNPGG
     GTYSLQPSPC LLRDQRLGVR SGDYSTMEGP ESRPSQPPTP LPQAQEDAMS WSSQQDTMSS
     TGYSPGTRKR KNRKPSLCQV PSTSSTDGAG GLLGEQPLTE ERSPCRASLT PVKAEADLVR
     GTPEPFLAQA RLAWEAQQAH FHMKQRGSWD SQQDGSGYES DGAVPLPMPG PVVRAFSEDE
     ALAQQDSKHW KRSTFDKLGF PQILLEKSVS VQTNLASPEP HLHPSQSEDL GACAQFESSR
     QNRSAMPSSS CVFPTFTLRK PSSETDIENW ASKHFNKHTQ GLFRRKVSIA NMLAWSSESI
     KKPMIVTSDR HVKKEACEIF KLIQMYMGDR RAKADPLHVA LEIATKGWSA QGLRDELYIQ
     LCRQTTENFR LESLARGWEL MAICLAFFPP TPKFHSYLEG YIYRHMDPVN DTKVTQHIKE
     LLERNSKKKS KLRKKPKPYV EEPDGVAIST YAKYCYHKLQ KAALTGAKKG LKKPNVEEIR
     HAKNAVFSPS MFGSALQEVM SMQKERYPDR QLPWVQTRLS EEVLALNGDQ TEGIFRVPGD
     IDEVNALKLQ VDQWKVPTGL EDPHVPASLL KLWYRELEEP LIPHEFYEQC IAHYESPEAA
     VAVVHALPRI NRMVLCYLIR FLQVFVQPAN VAITKMDVSN LAMVMAPNCL RCQSDDPRVI
     FENTRKEMSF LRVLIQHLDT SFMEGVL
//
ID   IF5_MOUSE               Reviewed;         429 AA.
AC   P59325;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   12-FEB-2003, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Eukaryotic translation initiation factor 5;
DE            Short=eIF-5;
GN   Name=Eif5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Colon, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387 AND SER-388, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387 AND SER-388, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Catalyzes the hydrolysis of GTP bound to the 40S
CC       ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with
CC       the subsequent joining of a 60S ribosomal subunit resulting in the
CC       release of eIF-2 and the guanine nucleotide. The subsequent
CC       joining of a 60S ribosomal subunit results in the formation of a
CC       functional 80S initiation complex (80S.mRNA.Met-tRNA[F]).
CC   -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family.
CC   -!- SIMILARITY: Contains 1 W2 domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC039275; AAH39275.1; -; mRNA.
DR   EMBL; BC042622; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00187443; -.
DR   RefSeq; NP_775539.1; NM_173363.5.
DR   RefSeq; NP_829887.1; NM_178041.2.
DR   RefSeq; XP_001479641.1; XM_001479591.2.
DR   UniGene; Mm.271222; -.
DR   UniGene; Mm.470192; -.
DR   ProteinModelPortal; P59325; -.
DR   SMR; P59325; 3-150, 230-405.
DR   STRING; P59325; -.
DR   PhosphoSite; P59325; -.
DR   PRIDE; P59325; -.
DR   Ensembl; ENSMUST00000050993; ENSMUSP00000061616; ENSMUSG00000021282.
DR   GeneID; 100047658; -.
DR   GeneID; 217869; -.
DR   KEGG; mmu:100047658; -.
DR   KEGG; mmu:217869; -.
DR   UCSC; uc007pdd.1; mouse.
DR   CTD; 217869; -.
DR   MGI; MGI:95309; Eif5.
DR   eggNOG; roNOG04640; -.
DR   HOGENOM; HBG559646; -.
DR   HOVERGEN; HBG006132; -.
DR   InParanoid; P59325; -.
DR   OMA; DHAKNLT; -.
DR   PhylomeDB; P59325; -.
DR   NextBio; 461086; -.
DR   ArrayExpress; P59325; -.
DR   Bgee; P59325; -.
DR   CleanEx; MM_EIF5; -.
DR   Genevestigator; P59325; -.
DR   GermOnline; ENSMUSG00000021282; Mus musculus.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0016070; P:RNA metabolic process; IEA:InterPro.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003307; eIF5C.
DR   InterPro; IPR016021; MIF4-like_typ_1/2/3.
DR   InterPro; IPR002735; Transl_init_fac_IF2/IF5.
DR   InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR   InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR   Gene3D; G3DSA:3.30.30.50; G3DSA:3.30.30.50; 1.
DR   Gene3D; G3DSA:1.25.40.180; MIF4-like_typ_1/2/3; 1.
DR   Pfam; PF01873; eIF-5_eIF-2B; 1.
DR   Pfam; PF02020; W2; 1.
DR   SMART; SM00653; eIF2B_5; 1.
DR   SMART; SM00515; eIF5C; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF100966; Transl_init_fac_IF2/IF5_N; 1.
DR   SUPFAM; SSF75689; Transl_init_fac_IF2/IF5_Zn-bd; 1.
DR   PROSITE; PS51363; W2; 1.
PE   1: Evidence at protein level;
KW   GTP-binding; Initiation factor; Nucleotide-binding; Phosphoprotein;
KW   Protein biosynthesis.
FT   CHAIN         1    429       Eukaryotic translation initiation factor
FT                                5.
FT                                /FTId=PRO_0000212517.
FT   DOMAIN      231    390       W2.
FT   NP_BIND      27     34       GTP (Potential).
FT   COMPBIAS    194    200       Asp/Glu-rich (highly acidic).
FT   COMPBIAS    382    400       Asp/Glu-rich (highly acidic).
FT   COMPBIAS    421    427       Asp-rich (acidic).
FT   MOD_RES      10     10       Phosphoserine (By similarity).
FT   MOD_RES     149    149       Phosphoserine (By similarity).
FT   MOD_RES     227    227       Phosphoserine (By similarity).
FT   MOD_RES     387    387       Phosphoserine.
FT   MOD_RES     388    388       Phosphoserine.
FT   MOD_RES     403    403       Phosphotyrosine (By similarity).
FT   MOD_RES     408    408       Phosphoserine (By similarity).
FT   MOD_RES     417    417       Phosphoserine (By similarity).
SQ   SEQUENCE   429 AA;  48968 MW;  C77DD5DFBB5C1DEF CRC64;
     MSVNVNRSVS DQFYRYKMPR LIAKVEGKGN GIKTVIVNMV DVAKALNRPP TYPTKYFGCE
     LGAQTQFDVK NDRYIVNGSH EANKLQDMLD GFIKKFVLCP ECENPETDLH VNPKKQTIGN
     SCKACGYRGM LDTHHKLCTF ILKNPPENSD IGTGKKEKEK KNRKGKDKEN GSVSTSETPP
     PPPPNEISPP HAVEEEEDDD WGEDTTEEAQ RRRMDEISDH AKGLTLSDDL ERTVEERVNI
     LFDFVKKKKE EGIIDSSDKE IVAEAERLDV KAMGPLVLTE VLFDEKIREQ IKKYRRHFLR
     FCHNNKKAQR YLLHGLECVV AMHQAQLISK IPHILKEMYD ADLLEEEVII SWSEKASKKY
     VSKELAKEIR VKAEPFIKWL KEAEEESSGG EEEDEDENIE VVYSKTASVP KVETVKSDNK
     DDDIDIDAI
//
ID   ASXL1_MOUSE             Reviewed;        1514 AA.
AC   P59598;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Putative Polycomb group protein ASXL1;
DE   AltName: Full=Additional sex combs-like protein 1;
GN   Name=Asxl1; Synonyms=Kiaa0978;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Probable Polycomb group (PcG) protein. Non-catalytic
CC       component of the PR-DUB complex, a complex that specifically
CC       mediates deubiquitination of histone H2A monoubiquitinated at
CC       'Lys-119' (H2AK119ub1) (By similarity).
CC   -!- SUBUNIT: Component of the PR-DUB complex, at least composed of
CC       BAP1 and ASXL1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- DOMAIN: Contains two Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs, which may
CC       be required for an association with nuclear receptors (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the Asx family.
CC   -!- SIMILARITY: Contains 1 PHD-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65695.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK122413; BAC65695.1; ALT_INIT; mRNA.
DR   IPI; IPI00281565; -.
DR   RefSeq; NP_001035028.1; NM_001039939.1.
DR   UniGene; Mm.330677; -.
DR   STRING; P59598; -.
DR   PhosphoSite; P59598; -.
DR   PRIDE; P59598; -.
DR   Ensembl; ENSMUST00000109790; ENSMUSP00000105413; ENSMUSG00000042548.
DR   GeneID; 228790; -.
DR   KEGG; mmu:228790; -.
DR   UCSC; uc008nhs.1; mouse.
DR   CTD; 228790; -.
DR   MGI; MGI:2684063; Asxl1.
DR   eggNOG; roNOG11458; -.
DR   HOGENOM; HBG283728; -.
DR   HOVERGEN; HBG050598; -.
DR   InParanoid; P59598; -.
DR   OMA; FWKLPRE; -.
DR   OrthoDB; EOG4GQQ44; -.
DR   NextBio; 379148; -.
DR   ArrayExpress; P59598; -.
DR   Bgee; P59598; -.
DR   CleanEx; MM_ASXL1; -.
DR   Genevestigator; P59598; -.
DR   GermOnline; ENSMUSG00000042548; Mus musculus.
DR   GO; GO:0035517; C:PR-DUB complex; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   PROSITE; PS01359; ZF_PHD_1; FALSE_NEG.
DR   PROSITE; PS50016; ZF_PHD_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Metal-binding; Nucleus; Phosphoprotein; Repeat;
KW   Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1   1514       Putative Polycomb group protein ASXL1.
FT                                /FTId=PRO_0000059322.
FT   ZN_FING    1476   1513       PHD-type; atypical.
FT   MOTIF       284    288       LXXLL motif 1.
FT   MOTIF       409    413       Nuclear localization signal (Potential).
FT   MOTIF       808    812       LXXLL motif 2.
FT   COMPBIAS    199    209       Poly-Ser.
FT   COMPBIAS    284    288       Poly-Leu.
FT   COMPBIAS    639    670       Gly-rich.
FT   COMPBIAS   1430   1433       Poly-Ser.
FT   MOD_RES     500    500       Phosphoserine.
SQ   SEQUENCE   1514 AA;  162674 MW;  20D9FBE9D4CF9E74 CRC64;
     MKDKQKRKKE RTWAEAARLV LENYSDAPMT PKQILQVIEA EGLKEMRSGT SPLACLNAML
     HSNSRGGEGL FYKLPGRISL FTLKKDAVQW SRNAATVDGD EPEDSADVES CGSNEASTVS
     GENDVSLDET SSNASCSTES QSRPLSNPRD SHRASSQANK QKKRTGVMLP RVVLTPLKVN
     GAHVEPASGF SGRHADGESG SPSSSSSGSL ALGNSAIRGQ AEVTRDPAPL LRGFRKPATG
     QMKRNRGEEV DFETPGSILV NTNLRALINS RTFHALPLHF QQQLLLLLPE VDRQVGTDGL
     LRLSGSALNN EFFTHAAQSW RERLADGEFT HEMQVRLRQE MEKEKKVEQW KEKFFEDYYG
     QKLGLTKEES LQQKEVQEEA KVKSGLCVSG ESVRPQRGPN TRQRDGHFKK RSRPDLRTRS
     RRNIYKKQEP EQAGVAKDAS AAPDVSLSKD TKTDLAGVNS TPGPDVSSAT SGQEGPKCPS
     EPVASQIQAE RDNLACASAS PDRIPTLPQD TVDQETKDQK RKSFEQEASA SFPEKKPRLE
     DRQSFRNTIE SVHTEKPQPT KEEPKVPPIR IQLSRIKPPW VAKGRPTYQI CPRIVPITES
     SCRGWTGART LADIKARALQ ARGARGYHCN RETATTAIGG GGGPGGGGSG AIDEGGGRDS
     SSGDGSEACG HPEPRGAPST SGESASDLQR TQLLPPCPLN GEHTPAEAAM PRARREDSAS
     LRKEESCLLK RVPGVLTSGL EDASQPPIAP TGDQPCQALP PLSSQTPVAE MLTEQPKLLL
     DDRTECESSR EDQGPTIPSE SSSGRFPLGD LLGGGSDQAF DNMKEPVSMT PTFISELSLA
     NYLQDRPDDD GLGLGATGLL IRESSRQEAL TEAFASGSPT SWVPILSNYE VIKTSDPESR
     ENIPCPEPQD EKEWERAVPL IAATESVPQP ESCISHWTPP PAAVGSTGSD SEQVDLERLE
     MNGISEAPSP HSESTDTASD SEGHLSEDSS EVDASEVTVV KGSLGGDEKQ DWDPSASLSK
     VNNDLSVLTR TGGVAASQSW VSRVCSVPHK IPDSLLLSST ECQPRSVCPL RPGSSVEVTN
     PLVMHLLHGN LPLEKVLPPG HRSSRLESSQ LPLREQSQDR GTLQGTGENN RLAARINPGS
     AQTLKESILA QSYGASAGLV RAMASKAPAM SQKIAKMVTS LDSQHPETEL TPSSGNLEEI
     DSKEHLSSFL CEEQKEGHSL SQGSDPGAAP GQCLGDHTTS KVPCFSSTNV SLSFGSEQTD
     GTLSDQNNAG GHEKKLFGPG NTVTTLQCPR SEEQTPLPAE VPPVFPSRKI EPSKNSVSGG
     VQTTRENRMP KPPPVSADSI KTEQTFLRDP IKADAENRKA AGYSSLELVG HLQGMPFVVD
     LPFWKLPREP GKGFSQPLEP SSIPSQLNIK QALYGKLSKL QLSPTSFNYS SSSATFPKGL
     AGGVVQLSHK ASFGTGHTAS LSLQMFADSS AVESISLQCA CSLKAMIMCQ GCGAFCHDDC
     IGPSKLCVLC LVVR
//
ID   PI5PA_MOUSE             Reviewed;        1003 AA.
AC   P59644;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-APR-2003, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A;
DE            EC=3.1.3.56;
DE   AltName: Full=Inositol polyphosphate 5-phosphatase J;
GN   Name=Inpp5j; Synonyms=Pib5pa;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION OF DOMAIN REQUIRED FOR
RP   MEMBRANE RUFFLE LOCALIZATION.
RX   MEDLINE=22538472; PubMed=12536145; DOI=10.1074/jbc.M209991200;
RA   Gurung R., Tan A., Ooms L.M., McGrath M.J., Huysmans R.D.,
RA   Munday A.D., Prescott M., Whisstock J.C., Mitchell C.A.;
RT   "Identification of a novel domain in two mammalian inositol-
RT   polyphosphate 5-phosphatases that mediates membrane ruffle
RT   localization. The inositol 5-phosphatase SKIP localizes to the
RT   endoplasmic reticulum and translocates to membrane ruffles following
RT   epidermal growth factor stimulation.";
RL   J. Biol. Chem. 278:11376-11385(2003).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348 AND SER-350, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Inositol 5-phosphatase, which converts inositol 1,4,5-
CC       trisphosphate to inositol 1,4-bisphosphate. Also converts
CC       phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-
CC       phosphate and inositol 1,3,4,5-tetrakisphosphate to inositol
CC       1,3,4-trisphosphate in vitro. May be involved in modulation of the
CC       function of inositol and phosphatidylinositol polyphosphate-
CC       binding proteins that are present at membranes ruffles (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: D-myo-inositol 1,4,5-trisphosphate + H(2)O =
CC       myo-inositol 1,4-bisphosphate + phosphate.
CC   -!- CATALYTIC ACTIVITY: 1D-myo-inositol 1,3,4,5-tetrakisphosphate +
CC       H(2)O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Predominantly localized to
CC       membrane ruffles.
CC   -!- DOMAIN: The 5 Arg-Ser-Xaa-Ser-Xaa-Xaa (RSXSXX) motifs may
CC       constitute binding sites for the 14-3-3 protein.
CC   -!- SIMILARITY: Belongs to the inositol-1,4,5-trisphosphate 5-
CC       phosphatase type II family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK034272; BAC28654.1; -; mRNA.
DR   IPI; IPI00173277; -.
DR   UniGene; Mm.24313; -.
DR   ProteinModelPortal; P59644; -.
DR   SMR; P59644; 418-732.
DR   STRING; P59644; -.
DR   PhosphoSite; P59644; -.
DR   PRIDE; P59644; -.
DR   Ensembl; ENSMUST00000044507; ENSMUSP00000046625; ENSMUSG00000034570.
DR   UCSC; uc007hta.1; mouse.
DR   MGI; MGI:2158663; Inpp5j.
DR   HOGENOM; HBG125086; -.
DR   HOVERGEN; HBG082135; -.
DR   InParanoid; P59644; -.
DR   OrthoDB; EOG4HDSTN; -.
DR   PhylomeDB; P59644; -.
DR   BRENDA; 3.1.3.56; 244.
DR   NextBio; 370509; -.
DR   ArrayExpress; P59644; -.
DR   Bgee; P59644; -.
DR   Genevestigator; P59644; -.
DR   GermOnline; ENSMUSG00000034570; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043198; C:dendritic shaft; IDA:MGI.
DR   GO; GO:0030426; C:growth cone; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IEA:EC.
DR   GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IDA:MGI.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; IDA:MGI.
DR   GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IDA:MGI.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   InterPro; IPR000300; IPPc.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   SMART; SM00128; IPPc; 1.
DR   SUPFAM; SSF56219; Exo_endo_phos; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Phosphoprotein; Repeat; SH3-binding.
FT   CHAIN         1   1003       Phosphatidylinositol 4,5-bisphosphate 5-
FT                                phosphatase A.
FT                                /FTId=PRO_0000209739.
FT   REGION      422    725       Catalytic (Potential).
FT   REGION      726    837       Required for ruffle localization.
FT   MOTIF         6     11       RSXSXX motif 1.
FT   MOTIF       346    351       SH3-binding (Potential).
FT   MOTIF       351    356       RSXSXX motif 2.
FT   MOTIF       871    876       RSXSXX motif 3.
FT   MOTIF       882    887       RSXSXX motif 4.
FT   MOTIF       908    913       RSXSXX motif 5.
FT   COMPBIAS     50    374       Pro-rich.
FT   COMPBIAS    837    934       Ser-rich.
FT   MOD_RES     348    348       Phosphoserine.
FT   MOD_RES     350    350       Phosphoserine.
SQ   SEQUENCE   1003 AA;  107603 MW;  AFF4FD929CFCB6BA CRC64;
     MEGQTRSGSA RPGTRTGLGP LPGTHGVLQA EIPSKKVNSS FQLPAKNSGP ASSEPRLTLA
     PVGPRAAVSP PSERPRLVLS SPRPVLAPLS IAGEQKRPPP PHSSNRAAKS VGQLVVSAAA
     ASKPPPVASV SILAPKSLGQ LVISASAMPR PSPAPLGSVL TPTSRDQKQL SPTSVGPKPA
     LATSGLSLAL ASQEQPPQSP SSPSPVPSPV LSPSQEGHLA AASVTSTPAS ERQLPARQKD
     TAVPRPTPPA DKCLYTPERA AGPATSPPRA QAFSDPRLSP SFRARPEAPR HSPEDPVLPP
     PPQTLPLDVS PGLPESGTRS PGLLSPTFRP GIPSSQTVPP PLRKPPRSPS RSPSRSPNRS
     PCLPPAPEVA LPKPVTQAAG SGRCPSPNLQ AQESPAAATT TTSPTSSWSA QPTCKSDPGF
     RITVVTWNVG TAMPPDDVTS LLHLGSGHDN DGADMIAIGL QEVNSMINKR LKDALFTDQW
     SELFMDALGP FNFVLVSTVR MQGVILLLFA KYYHLPFLRD VQTDCTRTGL GGYWGNKGGV
     SVRLAAFGHM LCFLNCHLPA HMDKAEQRKD NFQTILSLQQ FQGPGAHGIL DHDLVFWFGD
     LNFRIESYDL HFVKFAIDSN QLHQLWEKDQ LNMAKNTWPI LKGFQEGPLN FAPTFKFDVG
     TNKYDTSAKK RKPAWTDRIL WKVKAPSGGP SPSGRESHRL QVTQHSYRSH MEYTVSDHKP
     VAAQFILQFA FRDDVPLVRL EVADEWARPE QAVVRYRVET VFARSSWDWI GLYRVGFRHC
     KDYVAYVWAK HEEVDGNIYQ VTFSEESLPK GHGDFILGYY SHHHSILIGV TEPFQISLPT
     SESASSSTDS SGTSSEGEDD STLELLAPKS RSPSPGKSKR HRSRSPGLAR FPSLALHPSS
     RERRGGSRSP SPQSRQLPRV APDRGHSSSS RGSSEEGPSG LPGPWAFPPS VPRSLGLLPA
     LRLETVDPGG GGSWGADQEA PDPNSLSPSP QGRLGLEEGG LGP
//
ID   FXYD7_MOUSE             Reviewed;          80 AA.
AC   P59648; Q8BTD2;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-APR-2003, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=FXYD domain-containing ion transport regulator 7;
GN   Name=Fxyd7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   RECONSTRUCTION FROM ESTS, AND CONCEPTUAL TRANSLATION.
RX   MEDLINE=20408885; PubMed=10950925; DOI=10.1006/geno.2000.6274;
RA   Sweadner K.J., Rael E.;
RT   "The FXYD gene family of small ion transport regulators or channels:
RT   cDNA sequence, protein signature sequence, and expression.";
RL   Genomics 68:41-56(2000).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65 AND SER-73, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the FXYD family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK004113; BAC25067.1; -; mRNA.
DR   IPI; IPI00224988; -.
DR   RefSeq; NP_071290.1; NM_022007.1.
DR   UniGene; Mm.41770; -.
DR   ProteinModelPortal; P59648; -.
DR   SMR; P59648; 10-78.
DR   STRING; P59648; -.
DR   PhosphoSite; P59648; -.
DR   PRIDE; P59648; -.
DR   Ensembl; ENSMUST00000073892; ENSMUSP00000073555; ENSMUSG00000036578.
DR   GeneID; 57780; -.
DR   KEGG; mmu:57780; -.
DR   UCSC; uc009ghr.1; mouse.
DR   CTD; 57780; -.
DR   MGI; MGI:1889006; Fxyd7.
DR   eggNOG; roNOG17634; -.
DR   HOVERGEN; HBG051679; -.
DR   InParanoid; P59648; -.
DR   OMA; LSKKVKC; -.
DR   OrthoDB; EOG45B1H6; -.
DR   NextBio; 313960; -.
DR   ArrayExpress; P59648; -.
DR   Bgee; P59648; -.
DR   CleanEx; MM_FXYD7; -.
DR   Genevestigator; P59648; -.
DR   GermOnline; ENSMUSG00000036578; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000272; Ion-transport_regulator_FXYD.
DR   Pfam; PF02038; ATP1G1_PLM_MAT8; 1.
DR   PROSITE; PS01310; FXYD; 1.
PE   1: Evidence at protein level;
KW   Ion transport; Ionic channel; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1     80       FXYD domain-containing ion transport
FT                                regulator 7.
FT                                /FTId=PRO_0000148191.
FT   TRANSMEM     23     45       Helical; (Potential).
FT   MOD_RES      65     65       Phosphoserine.
FT   MOD_RES      73     73       Phosphoserine.
SQ   SEQUENCE   80 AA;  8487 MW;  135CEB39C7A01CDC CRC64;
     MATPTQSPTN VPEETDPFFY DYATVQTVGM TLATIMFVLG IIIILSKKVK CRKADSRSES
     PTCKSCKSEL PSSAPGGGGV
//
ID   ANS1A_MOUSE             Reviewed;        1150 AA.
AC   P59672; Q6ZQG0;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Ankyrin repeat and SAM domain-containing protein 1A;
GN   Name=Anks1a; Synonyms=Anks1, Kiaa0229;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION.
RX   PubMed=12439753; DOI=10.1038/sj.onc.1205988;
RA   Pandey A., Blagoev B., Kratchmarova I., Fernandez M., Nielsen M.,
RA   Kristiansen T.Z., Ohara O., Podtelejnikov A.V., Roche S., Lodish H.F.,
RA   Mann M.;
RT   "Cloning of a novel phosphotyrosine binding domain containing
RT   molecule, Odin, involved in signaling by receptor tyrosine kinases.";
RL   Oncogene 21:8029-8036(2002).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-679, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640; SER-642; SER-644
RP   AND SER-663, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-682 AND SER-903, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May play a negative role in growth factor receptor
CC       signaling pathways.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=Cytoplasmic
CC       before and after growth factor treatment (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P59672-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P59672-2; Sequence=VSP_012704, VSP_012705, VSP_012706;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated on tyrosine residues in response to EGF and
CC       PDGF (By similarity).
CC   -!- SIMILARITY: Contains 6 ANK repeats.
CC   -!- SIMILARITY: Contains 1 PID domain.
CC   -!- SIMILARITY: Contains 2 SAM (sterile alpha motif) domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97904.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK129094; BAC97904.1; ALT_INIT; mRNA.
DR   EMBL; BC050847; AAH50847.1; -; mRNA.
DR   IPI; IPI00346041; -.
DR   IPI; IPI00754201; -.
DR   RefSeq; NP_852078.1; NM_181413.3.
DR   UniGene; Mm.32556; -.
DR   ProteinModelPortal; P59672; -.
DR   SMR; P59672; 4-322, 708-776, 784-847, 949-1085.
DR   PhosphoSite; P59672; -.
DR   PRIDE; P59672; -.
DR   Ensembl; ENSMUST00000088027; ENSMUSP00000085344; ENSMUSG00000024219.
DR   Ensembl; ENSMUST00000114842; ENSMUSP00000110491; ENSMUSG00000024219.
DR   GeneID; 224650; -.
DR   KEGG; mmu:224650; -.
DR   UCSC; uc008bpw.1; mouse.
DR   UCSC; uc008bpx.1; mouse.
DR   CTD; 224650; -.
DR   MGI; MGI:2446180; Anks1.
DR   GeneTree; ENSGT00530000063104; -.
DR   HOVERGEN; HBG050506; -.
DR   OrthoDB; EOG4PVNXV; -.
DR   NextBio; 377283; -.
DR   ArrayExpress; P59672; -.
DR   Bgee; P59672; -.
DR   CleanEx; MM_ANKS1; -.
DR   Genevestigator; P59672; -.
DR   GermOnline; ENSMUSG00000024219; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR011510; SAM_2.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 2.
DR   Pfam; PF00023; Ank; 6.
DR   Pfam; PF00640; PID; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM00454; SAM; 2.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF47769; SAM_homology; 2.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
DR   PROSITE; PS01179; PID; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ANK repeat; Cytoplasm;
KW   Phosphoprotein; Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1150       Ankyrin repeat and SAM domain-containing
FT                                protein 1A.
FT                                /FTId=PRO_0000066922.
FT   REPEAT       75    104       ANK 1.
FT   REPEAT      108    137       ANK 2.
FT   REPEAT      165    194       ANK 3.
FT   REPEAT      198    227       ANK 4.
FT   REPEAT      231    260       ANK 5.
FT   REPEAT      263    292       ANK 6.
FT   DOMAIN      712    778       SAM 1.
FT   DOMAIN      786    853       SAM 2.
FT   DOMAIN      952   1107       PID.
FT   COMPBIAS     31     51       Gly-rich.
FT   MOD_RES       2      2       N-acetylglycine (By similarity).
FT   MOD_RES     335    335       Phosphothreonine (By similarity).
FT   MOD_RES     472    472       Phosphotyrosine (By similarity).
FT   MOD_RES     638    638       Phosphoserine (By similarity).
FT   MOD_RES     640    640       Phosphoserine.
FT   MOD_RES     642    642       Phosphoserine.
FT   MOD_RES     644    644       Phosphoserine.
FT   MOD_RES     663    663       Phosphoserine.
FT   MOD_RES     677    677       Phosphoserine (By similarity).
FT   MOD_RES     679    679       Phosphoserine.
FT   MOD_RES     682    682       Phosphoserine.
FT   MOD_RES     693    693       Phosphoserine (By similarity).
FT   MOD_RES     903    903       Phosphoserine.
FT   VAR_SEQ     142    162       Missing (in isoform 2).
FT                                /FTId=VSP_012704.
FT   VAR_SEQ    1117   1117       A -> AVPVPPDSRCCHCHTCTTHRPSYLPLPSVSPGVK
FT                                (in isoform 2).
FT                                /FTId=VSP_012705.
FT   VAR_SEQ    1150   1150       N -> KYETTIF (in isoform 2).
FT                                /FTId=VSP_012706.
SQ   SEQUENCE   1150 AA;  125242 MW;  551AF44D1DB02D1B CRC64;
     MGKEQELLEA ARTGHLPAVE KLLSGKRLSS GFGGGGGGSG SGGGSGGGGL GSSSHPLSSL
     LSMWRGPNVN CVDSTGYTPL HHAALNGHRD VVEVLLRNDA LTNVADSKGC YPLHLAAWKG
     DAQIVRLLIQ QGPSHTRVNE QNALEIRELK KYGPFDPYIN AKNNDNETAL HCAAQYGHTE
     VVKALLEELT DPTMRNNKFE TPLDLAALYG RLEVVKLLLG AHPNLLSCST RKHTPLHLAA
     RNGHKAVVQV LLDAGMDSNY QTEMGSALHE AALFGKTDVV QILLAAGIDV NIKDNRGLTA
     LDTVRDLPSQ KSQQIAALIE DHMTGKRSVK EVDRTSTAQL PLLSNTDAIA PMSQGSMEKT
     VTELILHFDT HADEEGPYEA LYNAVSCHSL DSTASGRSSD RDSMNKEAEA TGTRAAGVRP
     RERPPPPAKP PPDEEEEERV DKKYFPLAAS EGLAVRPRIQ SSAPQEEEEH PYELLLTAET
     KKLGTTDGRT EDHRQSGSGR SQDSVEGQDG QVPEQFSGLL HGSSPVCEVG QDPFQLLTAP
     SQSHPESSQQ DACHEASMQL EEPGVQGTEP PQPGVPDQSK RVGLPAGLTA LASRTYLDAL
     THTVPLRPAG AEEEDQSGPR SRAPPTSKPK AELKLSRSLS KSDSDLLTCS PTEDATMGSR
     SESLSNCSIG KKRLEKSPSF ASEWDEIEKI MSSIGEGIDF SQEQQKISGS RTLEQSVGEW
     LESIGLQQYE SKLLLNGFDD VRFLGSNVME EQDLREIGIS DPQHRRKLLQ AARSLPKVKA
     LGYDGVSPTS VPSWLDSLGL QDYVHSFLSS GYSSIDTVKN LWELELVNVL KVHLLGHRKR
     IIASLADRPY EEPPQKPPRF SQLRCQDLIS QTSSPLSQND SCTGRSADLL LPSADTSRRR
     HDSLPDPGTA SRADRFRVQE EPSETKLTLR PPSLAAPYAP VQSWQHQPEK LIFESCGYEA
     NYLGSMLIKD LRGTESTQDA CAKMRKSTEH MKKIPTIILS ITYKGVKFID ASNKNVIAEH
     EIRNISCAAQ DPEDLCTFAY ITKDLQTSHH YCHVFSTVDV NLTYEIILTL GQAFEVAYQL
     ALQAQKSRTM AASAASMIET KSSKPVPKPR VGMRKSALEP PDSDQEAPSH ASVSWIVDPK
     PDSKRSLSTN
//
ID   SASH1_MOUSE             Reviewed;        1230 AA.
AC   P59808;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-AUG-2003, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=SAM and SH3 domain-containing protein 1;
GN   Name=Sash1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=22656757; PubMed=12771949; DOI=10.1038/sj.onc.1206474;
RA   Zeller C., Hinzmann B., Seitz S., Prokoph H., Burkhardt-Goettges E.,
RA   Fischer J., Jandrig B., Estevez-Schwarz L., Rosenthal A.,
RA   Scherneck S.;
RT   "SASH1 - a candidate tumour suppressor gene on chromosome 6q24.3 is
RT   downregulated in breast cancer.";
RL   Oncogene 22:2972-2983(2003).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-724, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-813 AND SER-831, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May have a role in a signaling pathway. Could act as a
CC       tumor suppressor.
CC   -!- SIMILARITY: Contains 2 SAM (sterile alpha motif) domains.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AJ507736; CAD47812.1; -; mRNA.
DR   IPI; IPI00338954; -.
DR   RefSeq; NP_780364.3; NM_175155.4.
DR   UniGene; Mm.338275; -.
DR   ProteinModelPortal; P59808; -.
DR   SMR; P59808; 548-607, 621-693, 1149-1230.
DR   STRING; P59808; -.
DR   PhosphoSite; P59808; -.
DR   PRIDE; P59808; -.
DR   Ensembl; ENSMUST00000015449; ENSMUSP00000015449; ENSMUSG00000015305.
DR   GeneID; 70097; -.
DR   KEGG; mmu:70097; -.
DR   UCSC; uc007eiu.1; mouse.
DR   CTD; 70097; -.
DR   MGI; MGI:1917347; Sash1.
DR   eggNOG; roNOG07541; -.
DR   HOGENOM; HBG445921; -.
DR   HOVERGEN; HBG058816; -.
DR   InParanoid; P59808; -.
DR   OrthoDB; EOG4NP72S; -.
DR   NextBio; 330994; -.
DR   ArrayExpress; P59808; -.
DR   Bgee; P59808; -.
DR   CleanEx; MM_SASH1; -.
DR   Genevestigator; P59808; -.
DR   GermOnline; ENSMUSG00000015305; Mus musculus.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR021090; SAM/SH3_domain-containing.
DR   InterPro; IPR011510; SAM_2.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 2.
DR   Pfam; PF07647; SAM_2; 2.
DR   Pfam; PF07653; SH3_2; 1.
DR   Pfam; PF12485; SLY; 1.
DR   SMART; SM00454; SAM; 2.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF47769; SAM_homology; 2.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 2.
DR   PROSITE; PS50002; SH3; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Repeat; SH3 domain; Tumor suppressor.
FT   CHAIN         1   1230       SAM and SH3 domain-containing protein 1.
FT                                /FTId=PRO_0000097598.
FT   DOMAIN      550    607       SH3.
FT   DOMAIN      626    690       SAM 1.
FT   DOMAIN     1160   1224       SAM 2.
FT   COMPBIAS    972   1042       Pro-rich.
FT   MOD_RES      83     83       Phosphoserine.
FT   MOD_RES     724    724       Phosphoserine.
FT   MOD_RES     813    813       Phosphoserine.
FT   MOD_RES     831    831       Phosphoserine.
SQ   SEQUENCE   1230 AA;  135591 MW;  DDE421DB74FE49AF CRC64;
     MEEDAGAASP APEPEPEVDP ARELEPEAGV SESISRLWTD VMGILDGSLG NIDDLAQQYA
     DYYNTCFSDV CERMEELRKR RVSQDLDVEK PDASPTSLQL RSQIEESLGF CSAVSTPEVE
     RKYPLHKSNS EDGCVGKGDW KKKNKYFWQN FRKNQKGIMR QTSKGEDVGY VASEITMSDE
     ERIQLMMMVK EKMITIEEAL ARLKEYEAQH RQSSTLDPAD WPDGSYPTLD GSSTCNSREQ
     SDDETEDSVK FKRLHKLVNS TRRVRKKLIR VEEMKKPSAE GGEEHVFENS PVQDERSALY
     SGVHKKPFFY DGSPEKPPED DADSLTPSPS SSSLDTWGAG RKLVKTFSKG ESRGLIKPPK
     KMGTFFSYPE EEKAQKVSRS LTEGEMKKGL GSLSHGRTCS FGGFDLTNRS LHVGSNNSDP
     AGKEGDFVYK EVIKSPPAPR ISLGKKVRSV KETMRKRMSK KYSSPVSEQD SGLDGMPSSP
     ASGKPDSEHV DKPKLKAGGS VESLRSSLSG QSSMSGQTVS TTDSSTSNRE SVKSEDGDDE
     EPPYRGPFCG RARVHTDFTP SPYDTDSLKL KKGDIIDIIS KPPMGTWMGL LNNKVGTFKF
     IYVDVLNEEE EKPKRPTRRR KKGRPSQPKS VEDLLDRINL KEHMPTFLFN GYEDLDTFKL
     LEEEDLDELN IRDPEHRAVL LTAVELLQEY DSNSDQSGSQ EKLLVDNQGL SGRSPRDSGC
     YESSENLENA KTHKPSVLST KSSTESNLKS FTRSQPGNYP TLPLMKSGEV RKQGEEGRLG
     RGLAPDTAKS CDVPSVTDLS KNRRSLPVSI CRSCETLEGP EPVESWPRSH SLDDLQGDAD
     VGKNVPTEMP ETCSQNVPEV PQKTSACTSK ALPRGRDPTA DVMLLTQSKR FSDPPKTMAK
     KLDGSVVASN LGIAPPQCIP RDFEAQPPVK PGLTRTSLEG LRKGHDHHPL GTKEGVDGEQ
     SAPETRTQSR HPSQPPPVPA KKSRERLANG LHLVPSPEAP ILPLKKASPA SPVSPSDCPS
     PREPRPSSGT EPGSPACTRP PPWLAELPES TSLQEHGVKL GPVLSRKVSC VRGVDLEMLT
     ENKLQAEGID LTEEPYSDKH GRCGIPEALV QRYAEDLEQP ERDVATNMDQ IRVKLLRKQH
     RMAIPSGGLT EICRKPLSPG CVASMSDWLI SIGLPMYTST LSDAGFSTLS QVPSLSHSCL
     QEAGITEERH IRKLITAARL FKLPPSPEAM
//
ID   PCMD1_MOUSE             Reviewed;         357 AA.
AC   P59913;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Protein-L-isoaspartate O-methyltransferase domain-containing protein 1;
GN   Name=Pcmtd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC       isoaspartyl/D-aspartyl protein methyltransferase family.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; BC052741; AAH52741.1; -; mRNA.
DR   IPI; IPI00338743; -.
DR   RefSeq; NP_898849.1; NM_183028.3.
DR   UniGene; Mm.478266; -.
DR   ProteinModelPortal; P59913; -.
DR   SMR; P59913; 9-222.
DR   PRIDE; P59913; -.
DR   Ensembl; ENSMUST00000061280; ENSMUSP00000059261; ENSMUSG00000051285.
DR   GeneID; 319263; -.
DR   KEGG; mmu:319263; -.
DR   UCSC; uc007agb.1; mouse.
DR   CTD; 319263; -.
DR   MGI; MGI:2441773; Pcmtd1.
DR   eggNOG; roNOG13870; -.
DR   HOGENOM; HBG445681; -.
DR   HOVERGEN; HBG013478; -.
DR   InParanoid; P59913; -.
DR   OrthoDB; EOG40GCRC; -.
DR   NextBio; 394490; -.
DR   ArrayExpress; P59913; -.
DR   Bgee; P59913; -.
DR   Genevestigator; P59913; -.
DR   GermOnline; ENSMUSG00000051285; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:InterPro.
DR   InterPro; IPR000682; PCMT.
DR   PANTHER; PTHR11579; PCMT; 1.
DR   Pfam; PF01135; PCMT; 1.
DR   PROSITE; PS01279; PCMT; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Lipoprotein; Myristate.
FT   INIT_MET      1      1       Removed (Potential).
FT   CHAIN         2    357       Protein-L-isoaspartate O-
FT                                methyltransferase domain-containing
FT                                protein 1.
FT                                /FTId=PRO_0000111926.
FT   ACT_SITE     64     64       By similarity.
FT   LIPID         2      2       N-myristoyl glycine (Potential).
SQ   SEQUENCE   357 AA;  40693 MW;  54CAFF921125408F CRC64;
     MGGAVSAGED NDDLIDNLKE AQYIRTERVE QAFRAIDRGD YYLEGYRDNA YKDLAWKHGN
     IHLSAPCIYS EVMEALKLQP GLSFLNLGSG TGYLSTMVGL ILGPFGINHG IELHSDVVEY
     AKEKLESFIK NSDSFDKFEF CEPAFVVGNC LQIASDSHQY DRIYCGAGVQ KDHENYMKIL
     LKVGGILVMP IEDQLTQIMR TGQNTWESKN ILAVSFAPLV QPSKNDNGTP DSVGLPPCAV
     RNLQDLARIY IRRTLRNFIN DEMQAKGIPQ RAPPKRKRKR VKQRINTYVF VGNQLIPQPL
     DSEEDEKMEE DSKEEEEKEH IEAMKREEPP QNLLREKIMK LPLPESLKAY LTYFRDK
//
ID   SMS_MOUSE               Reviewed;         116 AA.
AC   P60041; P01167;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Somatostatin;
DE   Contains:
DE     RecName: Full=Antrin;
DE   Contains:
DE     RecName: Full=Somatostatin-28;
DE   Contains:
DE     RecName: Full=Somatostatin-14;
DE   Flags: Precursor;
GN   Name=Sst; Synonyms=Smst;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Brain;
RX   MEDLINE=90206793; PubMed=1969620; DOI=10.1093/nar/18.5.1287;
RA   Fuhrmann G., Heilig R., Kempf J., Ebel A.;
RT   "Nucleotide sequence of the mouse preprosomatostatin gene.";
RL   Nucleic Acids Res. 18:1287-1287(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Somatostatin inhibits the release of somatotropin.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the somatostatin family.
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DR   EMBL; X51468; CAA35831.1; -; Genomic_DNA.
DR   EMBL; BC010770; AAH10770.1; -; mRNA.
DR   IPI; IPI00132248; -.
DR   PIR; S08416; RIMSS1.
DR   RefSeq; NP_033241.1; NM_009215.1.
DR   UniGene; Mm.2453; -.
DR   STRING; P60041; -.
DR   PRIDE; P60041; -.
DR   Ensembl; ENSMUST00000004480; ENSMUSP00000004480; ENSMUSG00000004366.
DR   GeneID; 20604; -.
DR   KEGG; mmu:20604; -.
DR   UCSC; uc007ytx.1; mouse.
DR   CTD; 20604; -.
DR   MGI; MGI:98326; Sst.
DR   eggNOG; roNOG16786; -.
DR   HOGENOM; HBG269508; -.
DR   HOVERGEN; HBG017816; -.
DR   InParanoid; P60041; -.
DR   OMA; RMELQRS; -.
DR   OrthoDB; EOG4W6NXF; -.
DR   PhylomeDB; P60041; -.
DR   NextBio; 298941; -.
DR   ArrayExpress; P60041; -.
DR   Bgee; P60041; -.
DR   CleanEx; MM_SST; -.
DR   Genevestigator; P60041; -.
DR   GermOnline; ENSMUSG00000004366; Mus musculus.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0030334; P:regulation of cell migration; IDA:MGI.
DR   InterPro; IPR004250; Somatostatin.
DR   InterPro; IPR018142; Somatostatin/Cortistatin_C.
DR   PANTHER; PTHR10558; Somatostatin; 1.
DR   Pfam; PF03002; Somatostatin; 1.
DR   PIRSF; PIRSF001814; Somatostatin; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Disulfide bond; Hormone; Secreted;
KW   Signal.
FT   SIGNAL        1     24       By similarity.
FT   PEPTIDE      25     34       Antrin.
FT                                /FTId=PRO_0000033092.
FT   PROPEP       35     88       By similarity.
FT                                /FTId=PRO_0000033093.
FT   PEPTIDE      89    116       Somatostatin-28.
FT                                /FTId=PRO_0000033094.
FT   PEPTIDE     103    116       Somatostatin-14.
FT                                /FTId=PRO_0000033095.
FT   DISULFID    105    116       By similarity.
SQ   SEQUENCE   116 AA;  12746 MW;  D48B5454C4490375 CRC64;
     MLSCRLQCAL AALCIVLALG GVTGAPSDPR LRQFLQKSLA AATGKQELAK YFLAELLSEP
     NQTENDALEP EDLPQAAEQD EMRLELQRSA NSNPAMAPRE RKAGCKNFFW KTFTSC
//
ID   RIMS4_MOUSE             Reviewed;         269 AA.
AC   P60191;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Regulating synaptic membrane exocytosis protein 4;
DE   AltName: Full=RIM4 gamma;
DE   AltName: Full=Rab3-interacting molecule 4;
DE            Short=RIM 4;
GN   Name=Rims4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=22508184; PubMed=12620390; DOI=10.1016/S0888-7543(02)00024-1;
RA   Wang Y., Suedhof T.C.;
RT   "Genomic definition of RIM proteins: evolutionary amplification of a
RT   family of synaptic regulatory proteins.";
RL   Genomics 81:126-137(2003).
CC   -!- FUNCTION: Regulates synaptic membrane exocytosis (By similarity).
CC   -!- SUBUNIT: Binds PPFIA3 (By similarity). Does not bind RAB3.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 C2 domain.
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DR   EMBL; AY326955; AAQ01682.1; -; mRNA.
DR   IPI; IPI00127791; -.
DR   RefSeq; NP_898844.1; NM_183023.1.
DR   UniGene; Mm.330760; -.
DR   UniGene; Mm.459039; -.
DR   ProteinModelPortal; P60191; -.
DR   SMR; P60191; 99-248.
DR   STRING; P60191; -.
DR   PhosphoSite; P60191; -.
DR   PRIDE; P60191; -.
DR   Ensembl; ENSMUST00000044734; ENSMUSP00000045637; ENSMUSG00000035226.
DR   GeneID; 241770; -.
DR   KEGG; mmu:241770; -.
DR   UCSC; uc008nto.1; mouse.
DR   CTD; 241770; -.
DR   MGI; MGI:2674366; Rims4.
DR   GeneTree; ENSGT00550000074588; -.
DR   HOGENOM; HBG444874; -.
DR   HOVERGEN; HBG056381; -.
DR   InParanoid; P60191; -.
DR   OMA; FMGVARI; -.
DR   OrthoDB; EOG4J118T; -.
DR   PhylomeDB; P60191; -.
DR   NextBio; 385148; -.
DR   Bgee; P60191; -.
DR   CleanEx; MM_RIMS4; -.
DR   Genevestigator; P60191; -.
DR   GermOnline; ENSMUSG00000035226; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   Pfam; PF00168; C2; 1.
DR   SMART; SM00239; C2; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   PROSITE; PS50004; C2; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Exocytosis; Neurotransmitter transport; Phosphoprotein;
KW   Synapse; Transport.
FT   CHAIN         1    269       Regulating synaptic membrane exocytosis
FT                                protein 4.
FT                                /FTId=PRO_0000190208.
FT   DOMAIN      115    217       C2.
FT   MOD_RES       4      4       Phosphoserine (By similarity).
FT   MOD_RES     254    254       Phosphoserine (By similarity).
FT   MOD_RES     257    257       Phosphoserine (By similarity).
SQ   SEQUENCE   269 AA;  29329 MW;  5CB33B573A9CECAC CRC64;
     MERSQSRLSL SASFEALAIY FPCMNSFDDE DAADSRRLKG AIQRSTETGL AVEMPSRTLR
     QASHESIEDS MNSYGSEGNL NYGGVCLASD AQFSDFLGSM GPAQFVGRQT LATTPMGDVE
     IGLQERNGQL EVDIIQARGL TAKPGSKTLP AAYIKAYLLE NGVCIAKKKT KVARKSLDPL
     YNQVLLFPES PQGKVLQVIV WGNYGRMERK QFMGVARVLL EELDLTTLAV GWYKLFPTSS
     MVDPATGPLL RQASQLSLES TVGPCGERS
//
ID   MYPR_MOUSE              Reviewed;         277 AA.
AC   P60202; P04400; P06905; Q9WUS9;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Myelin proteolipid protein;
DE            Short=PLP;
DE   AltName: Full=Lipophilin;
GN   Name=Plp1; Synonyms=Plp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND DM-20).
RX   MEDLINE=87147292; PubMed=3469678; DOI=10.1073/pnas.84.5.1454;
RA   Hudson L.D., Berndt J.A., Puckett C., Kozak C.A., Lazzarini R.A.;
RT   "Aberrant splicing of proteolipid protein mRNA in the dysmyelinating
RT   jimpy mutant mouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:1454-1458(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   MEDLINE=88172505; PubMed=2451027; DOI=10.1016/0022-2836(88)90303-8;
RA   Ikenaka K., Furuichi T., Iwasaki Y., Moriguchi A., Okano H.,
RA   Mikoshiba K.;
RT   "Myelin proteolipid protein gene structure and its regulation of
RT   expression in normal and jimpy mutant mice.";
RL   J. Mol. Biol. 199:587-596(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 1).
RC   STRAIN=BALB/cByJ;
RX   MEDLINE=88141332; PubMed=2449535; DOI=10.1002/jnr.490180302;
RA   Macklin W.B., Campagnoni C.W., Deininger P.L., Gardinier M.V.;
RT   "Structure and expression of the mouse myelin proteolipid protein
RT   gene.";
RL   J. Neurosci. Res. 18:383-394(1987).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=87067491; PubMed=3466187; DOI=10.1073/pnas.83.23.9264;
RA   Nave K.-A., Lai C., Bloom F.E., Milner R.J.;
RT   "Jimpy mutant mouse: a 74-base deletion in the mRNA for myelin
RT   proteolipid protein and evidence for a primary defect in RNA
RT   splicing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:9264-9268(1986).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DM-20).
RX   MEDLINE=87289665; PubMed=2441390; DOI=10.1073/pnas.84.16.5665;
RA   Nave K.-A., Lai C., Bloom F.E., Milner R.J.;
RT   "Splice site selection in the proteolipid protein (PLP) gene
RT   transcript and primary structure of the DM-20 protein of central
RT   nervous system myelin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:5665-5669(1987).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 2-9; 46-53; 99-122; 145-151 AND 193-229, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [8]
RP   NUCLEOTIDE SEQUENCE OF 50-277.
RX   MEDLINE=87310464; PubMed=2442307;
RX   DOI=10.1111/j.1471-4159.1987.tb10005.x;
RA   Sorg B.A., Smith M.M., Campagnoni A.T.;
RT   "Developmental expression of the myelin proteolipid protein and basic
RT   protein mRNAs in normal and dysmyelinating mutant mice.";
RL   J. Neurochem. 49:1146-1154(1987).
RN   [9]
RP   NUCLEOTIDE SEQUENCE OF 176-270.
RX   MEDLINE=87089716; PubMed=2432393;
RA   Gardinier M.V., Macklin W.B., Diniak A.J., Deininger P.L.;
RT   "Characterization of myelin proteolipid mRNAs in normal and jimpy
RT   mice.";
RL   Mol. Cell. Biol. 6:3755-3762(1986).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 209-232, AND ALTERNATIVE
RP   SPLICING.
RX   MEDLINE=88030089; PubMed=2444462; DOI=10.1016/0014-5793(87)80331-9;
RA   Macklin W.B., Gardinier M.V., King K.D., Kampf K.;
RT   "An AG to a GG transition at a splice site in the myelin proteolipid
RT   protein gene in jimpy mice results in the removal of an exon.";
RL   FEBS Lett. 223:417-421(1987).
RN   [11]
RP   VARIANT JIMPY MSD VAL-243.
RX   MEDLINE=90132887; PubMed=1688931;
RA   Gencic S., Hudson L.D.;
RT   "Conservative amino acid substitution in the myelin proteolipid
RT   protein of jimpymsd mice.";
RL   J. Neurosci. 10:117-124(1990).
RN   [12]
RP   VARIANT RUMPSHAKER THR-187.
RX   MEDLINE=92375193; PubMed=1380672; DOI=10.1038/358758a0;
RA   Schneider A., Montague P., Griffiths I., Fanarraga M., Kennedy P.,
RA   Brophy P., Nave K.-A.;
RT   "Uncoupling of hypomyelination and glial cell death by a mutation in
RT   the proteolipid protein gene.";
RL   Nature 358:758-761(1992).
CC   -!- FUNCTION: This is the major myelin protein from the central
CC       nervous system. It plays an important role in the formation or
CC       maintenance of the multilamellar structure of myelin.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P60202-1; Sequence=Displayed;
CC       Name=DM-20;
CC         IsoId=P60202-2; Sequence=VSP_009194;
CC   -!- DISEASE: Note=Defects in Plp1 are the of the dismyelinating
CC       diseases Jimpy and Rumpshaker (rsh).
CC   -!- SIMILARITY: Belongs to the myelin proteolipid protein family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M15442; AAA39951.1; -; mRNA.
DR   EMBL; M15442; AAA39952.1; ALT_SEQ; mRNA.
DR   EMBL; M15442; AAA39953.1; -; mRNA.
DR   EMBL; X07215; CAA30184.1; -; Genomic_DNA.
DR   EMBL; X07216; CAA30184.1; JOINED; Genomic_DNA.
DR   EMBL; X07217; CAA30184.1; JOINED; Genomic_DNA.
DR   EMBL; X07218; CAA30184.1; JOINED; Genomic_DNA.
DR   EMBL; X07219; CAA30184.1; JOINED; Genomic_DNA.
DR   EMBL; X07220; CAA30184.1; JOINED; Genomic_DNA.
DR   EMBL; X07221; CAA30184.1; JOINED; Genomic_DNA.
DR   EMBL; M37335; AAA39954.1; -; Genomic_DNA.
DR   EMBL; M37329; AAA39954.1; JOINED; Genomic_DNA.
DR   EMBL; M37330; AAA39954.1; JOINED; Genomic_DNA.
DR   EMBL; M37331; AAA39954.1; JOINED; Genomic_DNA.
DR   EMBL; M37332; AAA39954.1; JOINED; Genomic_DNA.
DR   EMBL; M37333; AAA39954.1; JOINED; Genomic_DNA.
DR   EMBL; M37334; AAA39954.1; JOINED; Genomic_DNA.
DR   EMBL; M14674; AAA39955.1; -; mRNA.
DR   EMBL; M16472; AAA39950.1; -; mRNA.
DR   EMBL; BC027010; AAH27010.1; -; mRNA.
DR   EMBL; X06375; CAB40821.1; -; Genomic_DNA.
DR   IPI; IPI00230610; -.
DR   IPI; IPI00263013; -.
DR   PIR; S34792; S34792.
DR   RefSeq; NP_035253.1; NM_011123.2.
DR   UniGene; Mm.1268; -.
DR   ProteinModelPortal; P60202; -.
DR   DIP; DIP-46199N; -.
DR   DIP; DIP-46200N; -.
DR   STRING; P60202; -.
DR   PhosphoSite; P60202; -.
DR   PRIDE; P60202; -.
DR   Ensembl; ENSMUST00000033800; ENSMUSP00000033800; ENSMUSG00000031425.
DR   GeneID; 18823; -.
DR   KEGG; mmu:18823; -.
DR   UCSC; uc009ujc.1; mouse.
DR   UCSC; uc009ujd.1; mouse.
DR   CTD; 18823; -.
DR   MGI; MGI:97623; Plp1.
DR   eggNOG; roNOG12818; -.
DR   HOGENOM; HBG714762; -.
DR   HOVERGEN; HBG000096; -.
DR   InParanoid; P60202; -.
DR   OMA; YCIVLLA; -.
DR   OrthoDB; EOG4B8JDT; -.
DR   PhylomeDB; P60202; -.
DR   NextBio; 295188; -.
DR   ArrayExpress; P60202; -.
DR   Bgee; P60202; -.
DR   CleanEx; MM_PLP1; -.
DR   Genevestigator; P60202; -.
DR   GermOnline; ENSMUSG00000031425; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043209; C:myelin sheath; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0048469; P:cell maturation; IMP:MGI.
DR   GO; GO:0022010; P:central nervous system myelination; IMP:MGI.
DR   GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IMP:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR   InterPro; IPR001614; Myelin_PLP.
DR   InterPro; IPR018237; Myelin_PLP_CS.
DR   PANTHER; PTHR11683; Myelin_PLP; 1.
DR   Pfam; PF01275; Myelin_PLP; 1.
DR   PRINTS; PR00214; MYELINPLP.
DR   SMART; SM00002; PLP; 1.
DR   PROSITE; PS00575; MYELIN_PLP_1; 1.
DR   PROSITE; PS01004; MYELIN_PLP_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing; Disease mutation;
KW   Disulfide bond; Lipoprotein; Membrane; Palmitate; Transmembrane;
KW   Transmembrane helix.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    277       Myelin proteolipid protein.
FT                                /FTId=PRO_0000159007.
FT   TOPO_DOM      2      9       Cytoplasmic (Probable).
FT   TRANSMEM     10     36       Helical; Name=1; (Probable).
FT   TOPO_DOM     37     63       Extracellular (Probable).
FT   TRANSMEM     64     88       Helical; Name=2; (Probable).
FT   TOPO_DOM     89    151       Cytoplasmic (Probable).
FT   TRANSMEM    152    177       Helical; Name=3; (Probable).
FT   TOPO_DOM    178    233       Extracellular (Probable).
FT   TRANSMEM    234    260       Helical; Name=4; (Probable).
FT   TOPO_DOM    261    277       Cytoplasmic (Probable).
FT   LIPID         6      6       S-palmitoyl cysteine (By similarity).
FT   LIPID         7      7       S-palmitoyl cysteine (By similarity).
FT   LIPID        10     10       S-palmitoyl cysteine (By similarity).
FT   LIPID       109    109       S-palmitoyl cysteine (By similarity).
FT   LIPID       139    139       S-palmitoyl cysteine (By similarity).
FT   LIPID       141    141       S-palmitoyl cysteine (By similarity).
FT   LIPID       199    199       O-palmitoyl serine (By similarity).
FT   DISULFID    184    228       By similarity.
FT   DISULFID    201    220       By similarity.
FT   VAR_SEQ     117    151       Missing (in isoform DM-20).
FT                                /FTId=VSP_009194.
FT   VARIANT     187    187       I -> T (in Rumpshaker).
FT   VARIANT     243    243       A -> V (in Jimpy MSD).
FT   CONFLICT     70     70       Y -> C (in Ref. 4 and 5).
FT   CONFLICT    126    126       S -> Y (in Ref. 4; AAA39955).
SQ   SEQUENCE   277 AA;  30077 MW;  3C2BC973C3061C38 CRC64;
     MGLLECCARC LVGAPFASLV ATGLCFFGVA LFCGCGHEAL TGTEKLIETY FSKNYQDYEY
     LINVIHAFQY VIYGTASFFF LYGALLLAEG FYTTGAVRQI FGDYKTTICG KGLSATVTGG
     QKGRGSRGQH QAHSLERVCH CLGKWLGHPD KFVGITYALT VVWLLVFACS AVPVYIYFNT
     WTTCQSIAFP SKTSASIGSL CADARMYGVL PWNAFPGKVC GSNLLSICKT AEFQMTFHLF
     IAAFVGAAAT LVSLLTFMIA ATYNFAVLKL MGRGTKF
//
ID   PCBP1_MOUSE             Reviewed;         356 AA.
AC   P60335;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Poly(rC)-binding protein 1;
DE   AltName: Full=Alpha-CP1;
DE   AltName: Full=Heterogeneous nuclear ribonucleoprotein E1;
DE            Short=hnRNP E1;
GN   Name=Pcbp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   MEDLINE=99386965; PubMed=10455157; DOI=10.1074/jbc.274.35.24849;
RA   Makeyev A.V., Chkheidze A.N., Liebhaber S.A.;
RT   "A set of highly conserved RNA-binding proteins, alphaCP-1 and
RT   alphaCP-2, implicated in mRNA stabilization, are coexpressed from an
RT   intronless gene and its intron-containing paralog.";
RL   J. Biol. Chem. 274:24849-24857(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 326-346, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Single-stranded nucleic acid binding protein that binds
CC       preferentially to oligo dC (By similarity).
CC   -!- INTERACTION:
CC       Q99N13:Hdac9; NbExp=2; IntAct=EBI-309059, EBI-645361;
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains 3 KH domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF139894; AAD51920.1; -; mRNA.
DR   EMBL; AF139895; AAD51921.1; -; Genomic_DNA.
DR   EMBL; BC069915; AAH69915.1; -; mRNA.
DR   EMBL; BC004793; AAH04793.1; -; mRNA.
DR   IPI; IPI00128904; -.
DR   RefSeq; NP_035995.1; NM_011865.3.
DR   UniGene; Mm.274146; -.
DR   ProteinModelPortal; P60335; -.
DR   SMR; P60335; 11-169, 278-348.
DR   IntAct; P60335; 12.
DR   STRING; P60335; -.
DR   PhosphoSite; P60335; -.
DR   REPRODUCTION-2DPAGE; IPI00128904; -.
DR   REPRODUCTION-2DPAGE; P60335; -.
DR   PRIDE; P60335; -.
DR   Ensembl; ENSMUST00000053015; ENSMUSP00000054863; ENSMUSG00000051695.
DR   GeneID; 23983; -.
DR   KEGG; mmu:23983; -.
DR   UCSC; uc009csc.1; mouse.
DR   CTD; 23983; -.
DR   MGI; MGI:1345635; Pcbp1.
DR   eggNOG; roNOG07937; -.
DR   GeneTree; ENSGT00550000074311; -.
DR   HOGENOM; HBG445439; -.
DR   HOVERGEN; HBG053520; -.
DR   InParanoid; P60335; -.
DR   OMA; NISERNC; -.
DR   OrthoDB; EOG46WZ8K; -.
DR   PhylomeDB; P60335; -.
DR   NextBio; 303869; -.
DR   ArrayExpress; P60335; -.
DR   Bgee; P60335; -.
DR   CleanEx; MM_PCBP1; -.
DR   Genevestigator; P60335; -.
DR   GermOnline; ENSMUSG00000051695; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003723; F:RNA binding; TAS:MGI.
DR   GO; GO:0008494; F:translation activator activity; TAS:MGI.
DR   GO; GO:0006397; P:mRNA processing; TAS:MGI.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR004088; KH_type_1.
DR   InterPro; IPR018111; KH_type_1_subgr.
DR   Pfam; PF00013; KH_1; 3.
DR   SMART; SM00322; KH; 3.
DR   PROSITE; PS50084; KH_TYPE_1; 3.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein;
KW   Repeat; Ribonucleoprotein; RNA-binding.
FT   CHAIN         1    356       Poly(rC)-binding protein 1.
FT                                /FTId=PRO_0000050088.
FT   DOMAIN       13     75       KH 1.
FT   DOMAIN       97    162       KH 2.
FT   DOMAIN      279    343       KH 3.
FT   MOD_RES     173    173       Phosphoserine.
FT   MOD_RES     189    189       Phosphoserine (By similarity).
FT   MOD_RES     190    190       Phosphoserine (By similarity).
FT   MOD_RES     246    246       Phosphoserine (By similarity).
FT   MOD_RES     262    262       Phosphoserine (By similarity).
FT   MOD_RES     263    263       Phosphoserine (By similarity).
FT   MOD_RES     264    264       Phosphoserine (By similarity).
SQ   SEQUENCE   356 AA;  37498 MW;  6D1A261276CA206D CRC64;
     MDAGVTESGL NVTLTIRLLM HGKEVGSIIG KKGESVKRIR EESGARINIS EGNCPERIIT
     LTGPTNAIFK AFAMIIDKLE EDINSSMTNS TAASRPPVTL RLVVPATQCG SLIGKGGCKI
     KEIRESTGAQ VQVAGDMLPN STERAITIAG VPQSVTECVK QICLVMLETL SQSPQGRVMT
     IPYQPMPASS PVICAGGQDR CSDAAGYPHA THDLEGPPLD AYSIQGQHTI SPLDLAKLNQ
     VARQQSHFAM MHGGTGFAGI DSSSPEVKGY WASLDASTQT THELTIPNNL IGCIIGRQGA
     NINEIRQMSG AQIKIANPVE GSSGRQVTIT GSAASISLAQ YLINARLSSE KGMGCS
//
ID   ACTB_MOUSE              Reviewed;         375 AA.
AC   P60710; P02570; P70514; P99021; Q11211; Q3TI89; Q3TVP6; Q64316;
AC   Q6ZWM3;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Actin, cytoplasmic 1;
DE   AltName: Full=Beta-actin;
DE   Contains:
DE     RecName: Full=Actin, cytoplasmic 1, N-terminally processed;
GN   Name=Actb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=86176768; PubMed=3754329; DOI=10.1093/nar/14.6.2829;
RA   Tokunaga K., Taniguchi H., Yoda K., Shimizu M., Sakiyama S.;
RT   "Nucleotide sequence of a full-length cDNA for mouse cytoskeletal
RT   beta-actin mRNA.";
RL   Nucleic Acids Res. 14:2829-2829(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Mammary gland, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-375.
RC   TISSUE=Thymus;
RX   MEDLINE=79045349; PubMed=213279;
RX   DOI=10.1111/j.1432-1033.1978.tb12624.x;
RA   Vandekerckhove J., Weber K.;
RT   "Actin amino-acid sequences. Comparison of actins from calf thymus,
RT   bovine brain, and SV40-transformed mouse 3T3 cells with rabbit
RT   skeletal muscle actin.";
RL   Eur. J. Biochem. 90:451-462(1978).
RN   [4]
RP   PROTEIN SEQUENCE OF 19-39; 51-61; 85-113; 148-177; 184-191; 197-206;
RP   216-254; 257-284; 291-326 AND 360-372, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 27-375.
RX   MEDLINE=86200234; PubMed=3084797; DOI=10.1007/BF02100994;
RA   Alonso S., Minty A., Bourlet Y., Buckingham M.;
RT   "Comparison of three actin-coding sequences in the mouse; evolutionary
RT   relationships between the actin genes of warm-blooded vertebrates.";
RL   J. Mol. Evol. 23:11-22(1986).
RN   [6]
RP   ACETYLATION.
RC   TISSUE=Muscle;
RA   Vilbois F.;
RL   Submitted (OCT-1998) to UniProtKB.
RN   [7]
RP   ISGYLATION.
RX   PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA   Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA   Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT   "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT   human cells.";
RL   Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN   [8]
RP   NITRATION [LARGE SCALE ANALYSIS] AT TYR-218, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16800626; DOI=10.1021/bi060474w;
RA   Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
RA   Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
RA   Squier T.C., Bigelow D.J.;
RT   "Endogenously nitrated proteins in mouse brain: links to
RT   neurodegenerative disease.";
RL   Biochemistry 45:8009-8022(2006).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others. Identified in a mRNP granule
CC       complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1,
CC       HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8,
CC       IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0,
CC       RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and
CC       untranslated mRNAs. Component of the BAF complex, which includes
CC       at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2,
CC       SMARCA4/BRG1, MARCB1/BAF47, ACTL6A/BAF53, ACTL6B/BAF53B,
CC       SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1,
CC       and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or
CC       SMARCD3/BAF60C. In muscle cells, the BAF complex also contains
CC       DPF3. Found in a complex with XPO6, Ran, ACTB and PFN1. Component
CC       of a complex composed at least of ACTB, AP2M1, AP2A1, AP2A2,
CC       MEGF10 and VIM. Component of the MLL5-L complex, at least composed
CC       of MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT.
CC       Interacts with XPO6 and EMD (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Localized in
CC       cytoplasmic mRNP granules containing untranslated mRNAs (By
CC       similarity).
CC   -!- PTM: ISGylated.
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC       alpha, beta and gamma have been identified. The alpha actins are
CC       found in muscle tissues and are a major constituent of the
CC       contractile apparatus. The beta and gamma actins coexist in most
CC       cell types as components of the cytoskeleton and as mediators of
CC       internal cell motility.
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X03672; CAA27307.1; -; mRNA.
DR   EMBL; AK088691; BAC40507.1; -; mRNA.
DR   EMBL; AK145191; BAE26283.1; -; mRNA.
DR   EMBL; AK145196; BAE26288.1; -; mRNA.
DR   EMBL; AK145308; BAE26359.1; -; mRNA.
DR   EMBL; AK150711; BAE29789.1; -; mRNA.
DR   EMBL; AK150879; BAE29928.1; -; mRNA.
DR   EMBL; AK151010; BAE30031.1; -; mRNA.
DR   EMBL; AK151136; BAE30144.1; -; mRNA.
DR   EMBL; AK151145; BAE30152.1; -; mRNA.
DR   EMBL; AK151159; BAE30164.1; -; mRNA.
DR   EMBL; AK151166; BAE30169.1; -; mRNA.
DR   EMBL; AK151190; BAE30187.1; -; mRNA.
DR   EMBL; AK151202; BAE30199.1; -; mRNA.
DR   EMBL; AK151226; BAE30218.1; -; mRNA.
DR   EMBL; AK151277; BAE30264.1; -; mRNA.
DR   EMBL; AK151350; BAE30326.1; -; mRNA.
DR   EMBL; AK151398; BAE30366.1; -; mRNA.
DR   EMBL; AK151995; BAE30859.1; -; mRNA.
DR   EMBL; AK151999; BAE30863.1; -; mRNA.
DR   EMBL; AK152615; BAE31359.1; -; mRNA.
DR   EMBL; AK152651; BAE31388.1; -; mRNA.
DR   EMBL; AK152844; BAE31537.1; -; mRNA.
DR   EMBL; AK159759; BAE35350.1; -; mRNA.
DR   EMBL; AK159834; BAE35412.1; -; mRNA.
DR   EMBL; AK160029; BAE35572.1; -; mRNA.
DR   EMBL; AK166349; BAE38723.1; -; mRNA.
DR   EMBL; AK166498; BAE38810.1; -; mRNA.
DR   EMBL; AK167117; BAE39265.1; -; mRNA.
DR   EMBL; AK167960; BAE39957.1; -; mRNA.
DR   EMBL; X03765; CAA27396.1; -; mRNA.
DR   EMBL; M12481; AAA37144.1; -; mRNA.
DR   IPI; IPI00110850; -.
DR   PIR; A39104; ATMSB.
DR   RefSeq; NP_031419.1; NM_007393.3.
DR   UniGene; Mm.328431; -.
DR   UniGene; Mm.391967; -.
DR   ProteinModelPortal; P60710; -.
DR   SMR; P60710; 2-375.
DR   IntAct; P60710; 21.
DR   MINT; MINT-1202772; -.
DR   STRING; P60710; -.
DR   SWISS-2DPAGE; P99041; -.
DR   COMPLUYEAST-2DPAGE; P60710; -.
DR   REPRODUCTION-2DPAGE; P60710; -.
DR   UCD-2DPAGE; P60710; -.
DR   PRIDE; P60710; -.
DR   Ensembl; ENSMUST00000031564; ENSMUSP00000031564; ENSMUSG00000029580.
DR   GeneID; 11461; -.
DR   KEGG; mmu:11461; -.
DR   UCSC; uc009ajk.1; mouse.
DR   CTD; 11461; -.
DR   MGI; MGI:87904; Actb.
DR   eggNOG; roNOG11419; -.
DR   HOVERGEN; HBG003771; -.
DR   InParanoid; P60710; -.
DR   OMA; HGILRID; -.
DR   OrthoDB; EOG41JZC9; -.
DR   PhylomeDB; P60710; -.
DR   NextBio; 278784; -.
DR   ArrayExpress; P60710; -.
DR   Bgee; P60710; -.
DR   CleanEx; MM_ACTB; -.
DR   Genevestigator; P60710; -.
DR   GermOnline; ENSMUSG00000029580; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004000; Actin-like.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Methylation; Nitration; Nucleotide-binding;
KW   Phosphoprotein; Ubl conjugation.
FT   CHAIN         1    375       Actin, cytoplasmic 1.
FT                                /FTId=PRO_0000367076.
FT   INIT_MET      1      1       Removed; alternate.
FT   CHAIN         2    375       Actin, cytoplasmic 1, N-terminally
FT                                processed.
FT                                /FTId=PRO_0000000775.
FT   MOD_RES       1      1       N-acetylmethionine; in Actin, cytoplasmic
FT                                1; alternate.
FT   MOD_RES       2      2       N-acetylaspartate; in Actin, cytoplasmic
FT                                1, N-terminally processed.
FT   MOD_RES      53     53       Phosphotyrosine (By similarity).
FT   MOD_RES      73     73       Tele-methylhistidine.
FT   MOD_RES      91     91       Phosphotyrosine (By similarity).
FT   MOD_RES     166    166       Phosphotyrosine (By similarity).
FT   MOD_RES     169    169       Phosphotyrosine (By similarity).
FT   MOD_RES     198    198       Phosphotyrosine (By similarity).
FT   MOD_RES     218    218       Nitrated tyrosine; alternate.
FT   MOD_RES     218    218       Phosphotyrosine; alternate (By
FT                                similarity).
FT   MOD_RES     294    294       Phosphotyrosine (By similarity).
FT   MOD_RES     318    318       Phosphothreonine (By similarity).
FT   CONFLICT     38     38       P -> S (in Ref. 5; CAA27396/AAA37144).
FT   CONFLICT     52     52       S -> F (in Ref. 2; BAE39957).
FT   CONFLICT     80     80       D -> E (in Ref. 2; BAE35572).
FT   CONFLICT    109    109       P -> T (in Ref. 2; BAE39957).
FT   CONFLICT    156    156       G -> R (in Ref. 2; BAE39957).
FT   CONFLICT    178    178       L -> V (in Ref. 2; BAE39957).
SQ   SEQUENCE   375 AA;  41737 MW;  6AFD05CA94E360E2 CRC64;
     MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
     KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
     QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL
     AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY
     ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS
     GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
     EYDESGPSIV HRKCF
//
ID   NEUG_MOUSE              Reviewed;          78 AA.
AC   P60761; B2RRN7; Q3TYH4;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Neurogranin;
DE            Short=Ng;
DE   AltName: Full=RC3;
DE   Contains:
DE     RecName: Full=NEUG(55-78);
GN   Name=Nrgn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=129/SvJ;
RX   MEDLINE=20481891; PubMed=11016969; DOI=10.1073/pnas.210184697;
RA   Pak J.H., Huang F.L., Li J., Balschun D., Reymann K.G., Chiang C.,
RA   Westphal H., Huang K.P.;
RT   "Involvement of neurogranin in the modulation of calcium/calmodulin-
RT   dependent protein kinase II, synaptic plasticity, and spatial
RT   learning: a study with knockout mice.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:11232-11237(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Regulates the affinity of calmodulin for calcium.
CC       Involved in synaptic plasticity and spatial learning.
CC   -!- SUBUNIT: Interacts with apo-calmodulin; this interaction decreases
CC       the affinity of calmodulin for calcium ions (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell junction, synapse. Cell
CC       projection, dendritic spine. Note=Restricted to dendritic spines
CC       of a subset of neurons (By similarity).
CC   -!- PTM: Disulfide bond formation is redox-sensitive. The cysteine
CC       residues are readily oxidized by several nitric acid (NO) donors
CC       and other oxidants to form intramolecular disulfide. Cys-51 can
CC       form a disulfide with any other of the cysteine residues with an
CC       order of reactivity Cys-9 > Cys-4 > Cys-3 (By similarity).
CC   -!- SIMILARITY: Belongs to the neurogranin family.
CC   -!- SIMILARITY: Contains 1 collagen-like domain.
CC   -!- SIMILARITY: Contains 1 IQ domain.
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DR   EMBL; AF230869; AAG27519.1; -; Genomic_DNA.
DR   EMBL; AK002933; BAB22466.1; -; mRNA.
DR   EMBL; AK158630; BAE34589.1; -; mRNA.
DR   EMBL; BC061102; AAH61102.1; -; mRNA.
DR   EMBL; BC138511; AAI38512.1; -; mRNA.
DR   EMBL; BC138513; AAI38514.1; -; mRNA.
DR   IPI; IPI00380227; -.
DR   RefSeq; NP_071312.1; NM_022029.2.
DR   UniGene; Mm.335065; -.
DR   UniGene; Mm.477050; -.
DR   STRING; P60761; -.
DR   PhosphoSite; P60761; -.
DR   PRIDE; P60761; -.
DR   Ensembl; ENSMUST00000065668; ENSMUSP00000070113; ENSMUSG00000053310.
DR   GeneID; 64011; -.
DR   KEGG; mmu:64011; -.
DR   UCSC; uc009ovc.1; mouse.
DR   CTD; 64011; -.
DR   MGI; MGI:1927184; Nrgn.
DR   eggNOG; maNOG21661; -.
DR   GeneTree; ENSGT00440000039324; -.
DR   HOGENOM; HBG127183; -.
DR   HOVERGEN; HBG000470; -.
DR   InParanoid; P60761; -.
DR   OMA; KIKSGEH; -.
DR   OrthoDB; EOG4D26RQ; -.
DR   NextBio; 319863; -.
DR   ArrayExpress; P60761; -.
DR   Bgee; P60761; -.
DR   CleanEx; MM_NRGN; -.
DR   Genevestigator; P60761; -.
DR   GermOnline; ENSMUSG00000053310; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; TAS:MGI.
DR   GO; GO:0007243; P:intracellular protein kinase cascade; TAS:MGI.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   Pfam; PF00612; IQ; 1.
DR   SMART; SM00015; IQ; 1.
DR   PROSITE; PS50096; IQ; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Calmodulin-binding; Cell junction; Cell projection;
KW   Cytoplasm; Disulfide bond; Phosphoprotein; Synapse.
FT   CHAIN         1     78       Neurogranin.
FT                                /FTId=PRO_0000159592.
FT   PEPTIDE      55     78       NEUG(55-78) (By similarity).
FT                                /FTId=PRO_0000377702.
FT   DOMAIN       26     47       IQ.
FT   DOMAIN       48     78       Collagen-like.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      36     36       Phosphoserine; by PKC (By similarity).
FT   DISULFID      3     51       Or C-51 with C-4 or C-9.
SQ   SEQUENCE   78 AA;  7496 MW;  8E47CDB38E095794 CRC64;
     MDCCTESACS KPDDDILDIP LDDPGANAAA AKIQASFRGH MARKKIKSGE CGRKGPGPGG
     PGGAGGARGG AGGGPSGD
//
ID   RAC3_MOUSE              Reviewed;         192 AA.
AC   P60764; O14658;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Ras-related C3 botulinum toxin substrate 3;
DE   AltName: Full=p21-Rac3;
DE   Flags: Precursor;
GN   Name=Rac3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Koga H., Sumimoto H.;
RT   "Mouse Rac3.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Swiss Webster; TISSUE=Submandibular gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Plasma membrane-associated small GTPase which cycles
CC       between an active GTP-bound and inactive GDP-bound state. In
CC       active state binds to a variety of effector proteins to regulate
CC       cellular responses, such as cell spreading and the formation of
CC       actin-based protusions including lamellipodia and membrane ruffles
CC       (By similarity).
CC   -!- SUBUNIT: Interacts with the GEF protein DOCK7, which promotes the
CC       exchange between GDP and GTP, and therefore activates it.
CC       Interacts with C1D (By similarity).
CC   -!- INTERACTION:
CC       Q99PT1:Arhgdia; NbExp=2; IntAct=EBI-644949, EBI-494354;
CC       Q61599:Arhgdib; NbExp=2; IntAct=EBI-644949, EBI-644961;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; Lipid-
CC       anchor (By similarity). Endomembrane system (By similarity). Cell
CC       projection, lamellipodium (By similarity). Note=Membrane-
CC       associated when activated. Co-localizes with NRBP to endomembranes
CC       and at the cell periphery in lamellipodia (By similarity).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
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DR   EMBL; AB040819; BAB40573.1; -; mRNA.
DR   EMBL; AK089930; BAC41001.1; -; mRNA.
DR   IPI; IPI00157462; -.
DR   RefSeq; NP_573486.1; NM_133223.4.
DR   UniGene; Mm.34008; -.
DR   ProteinModelPortal; P60764; -.
DR   SMR; P60764; 1-177.
DR   IntAct; P60764; 6.
DR   STRING; P60764; -.
DR   PRIDE; P60764; -.
DR   Ensembl; ENSMUST00000018156; ENSMUSP00000018156; ENSMUSG00000018012.
DR   GeneID; 170758; -.
DR   KEGG; mmu:170758; -.
DR   UCSC; uc007mug.1; mouse.
DR   CTD; 170758; -.
DR   MGI; MGI:2180784; Rac3.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; P60764; -.
DR   OMA; DYAIRAV; -.
DR   OrthoDB; EOG466VN1; -.
DR   PhylomeDB; P60764; -.
DR   NextBio; 370354; -.
DR   ArrayExpress; P60764; -.
DR   Bgee; P60764; -.
DR   CleanEx; MM_RAC3; -.
DR   Genevestigator; P60764; -.
DR   GermOnline; ENSMUSG00000018012; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0012505; C:endomembrane system; ISS:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0030031; P:cell projection assembly; ISS:UniProtKB.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR   GO; GO:0031175; P:neuron projection development; IDA:MGI.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003578; GTPase_Rho.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00174; RHO; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cytoplasm; GTP-binding; Lipoprotein; Membrane;
KW   Methylation; Nucleotide-binding; Phosphoprotein; Prenylation.
FT   CHAIN         1    189       Ras-related C3 botulinum toxin substrate
FT                                3.
FT                                /FTId=PRO_0000198890.
FT   PROPEP      190    192       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000281241.
FT   NP_BIND      10     17       GTP (By similarity).
FT   NP_BIND      57     61       GTP (By similarity).
FT   NP_BIND     115    118       GTP (By similarity).
FT   MOTIF        32     40       Effector region (Potential).
FT   MOD_RES     167    167       Phosphothreonine (By similarity).
FT   MOD_RES     189    189       Cysteine methyl ester (By similarity).
FT   LIPID       189    189       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   192 AA;  21379 MW;  560BBC26BB7CDF4A CRC64;
     MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP VNLGLWDTAG
     QEDYDRLRPL SYPQTDVFLI CFSLVSPASF ENVRAKWYPE VRHHCPHTPI LLVGTKLDLR
     DDKDTIERLR DKKLAPITYP QGLAMAREIG SVKYLECSAL TQRGLKTVFD EAIRAVLCPP
     PVKKPGKKCT VF
//
ID   CDC42_MOUSE             Reviewed;         191 AA.
AC   P60766; A2A9U6; P21181; P25763; Q3THZ7; Q3TJK6; Q545V0; Q6P201;
AC   Q8BQ51;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 2.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Cell division control protein 42 homolog;
DE   AltName: Full=G25K GTP-binding protein;
DE   Flags: Precursor;
GN   Name=Cdc42;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   MEDLINE=93218723; PubMed=8464478; DOI=10.1038/362462a0;
RA   Miki T., Smith C.L., Long J.E., Eva A., Fleming T.P.;
RT   "Oncogene ect2 is related to regulators of small GTP-binding
RT   proteins.";
RL   Nature 362:462-465(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Liver;
RX   MEDLINE=97368185; PubMed=9224952; DOI=10.1016/S0167-4781(97)00027-4;
RA   Gong T.W., Shin J.J., Burmeister M., Lomax M.I.;
RT   "Complete cDNAs for CDC42 from chicken cochlea and mouse liver.";
RL   Biochim. Biophys. Acta 1352:282-292(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=8954774; DOI=10.1006/geno.1996.0586;
RA   Marks P.W., Kwiatkowski D.J.;
RT   "Genomic organization and chromosomal location of murine Cdc42.";
RL   Genomics 38:13-18(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=BALB/c, C57BL/6J, DBA/2, and NOD;
RC   TISSUE=Amnion, Bone marrow, Heart, Kidney, Liver, Mammary gland,
RC   Placenta, Spinal ganglion, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic germ cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 108-120, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [8]
RP   INTERACTION WITH CDC42EP4.
RX   MEDLINE=99421943; PubMed=10490598;
RA   Joberty G., Perlungher R.R., Macara I.G.;
RT   "The Borgs, a new family of Cdc42 and TC10 GTPase-interacting
RT   proteins.";
RL   Mol. Cell. Biol. 19:6585-6597(1999).
RN   [9]
RP   SUBUNIT OF A COMPLEX CONTAINING PARD6B; PARD3 AND PRKCZ, AND
RP   MUTAGENESIS OF THR-17.
RX   MEDLINE=20394296; PubMed=10934474; DOI=10.1038/35019573;
RA   Joberty G., Petersen C., Gao L., Macara I.G.;
RT   "The cell-polarity protein Par6 links Par3 and atypical protein kinase
RT   C to Cdc42.";
RL   Nat. Cell Biol. 2:531-539(2000).
RN   [10]
RP   INTERACTION WITH NET1.
RX   MEDLINE=98204843; PubMed=9535835; DOI=10.1074/jbc.273.15.8616;
RA   Alberts A.S., Bouquin N., Johnston L.H., Treisman R.;
RT   "Analysis of RhoA-binding proteins reveals an interaction domain
RT   conserved in heterotrimeric G protein beta subunits and the yeast
RT   response regulator protein Skn7.";
RL   J. Biol. Chem. 273:8616-8622(1998).
RN   [11]
RP   INTERACTION WITH ARHGAP33/TCGAP.
RX   MEDLINE=22658047; PubMed=12773384; DOI=10.1093/emboj/cdg262;
RA   Chiang S.-H., Hwang J., Legendre M., Zhang M., Kimura A.,
RA   Saltiel A.R.;
RT   "TCGAP, a multidomain Rho GTPase-activating protein involved in
RT   insulin-stimulated glucose transport.";
RL   EMBO J. 22:2679-2691(2003).
RN   [12]
RP   INTERACTION WITH DOCK11.
RX   PubMed=15710388; DOI=10.1016/j.febslet.2005.01.006;
RA   Nishikimi A., Meller N., Uekawa N., Isobe K., Schwartz M.A.,
RA   Maruyama M.;
RT   "Zizimin2: a novel, DOCK180-related Cdc42 guanine nucleotide exchange
RT   factor expressed predominantly in lymphocytes.";
RL   FEBS Lett. 579:1039-1046(2005).
RN   [13]
RP   INTERACTION WITH DOCK11 AND IQGAP1, AND MUTAGENESIS OF THR-17 AND
RP   GLN-61.
RX   PubMed=16968698; DOI=10.1074/jbc.M606248200;
RA   Lin Q., Yang W., Baird D., Feng Q., Cerione R.A.;
RT   "Identification of a DOCK180-related guanine nucleotide exchange
RT   factor that is capable of mediating a positive feedback activation of
RT   Cdc42.";
RL   J. Biol. Chem. 281:35253-35262(2006).
RN   [14]
RP   INTERACTION WITH CCPG1.
RX   PubMed=17000758; DOI=10.1128/MCB.00670-06;
RA   Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P.;
RT   "Ccpg1, a novel scaffold protein that regulates the activity of the
RT   Rho guanine nucleotide exchange factor Dbs.";
RL   Mol. Cell. Biol. 26:8964-8975(2006).
CC   -!- FUNCTION: Plasma membrane-associated small GTPase which cycles
CC       between an active GTP-bound and an inactive GDP-bound state. In
CC       active state binds to a variety of effector proteins to regulate
CC       cellular responses. Involved in epithelial cell polarization
CC       processes. Causes the formation of thin, actin-rich surface
CC       projections called filopodia.
CC   -!- ENZYME REGULATION: Regulated by guanine nucleotide exchange
CC       factors (GEFs) which promote the exchange of bound GDP for free
CC       GTP, GTPase activating proteins (GAPs) which increase the GTP
CC       hydrolysis activity, and GDP dissociation inhibitors which inhibit
CC       the dissociation of the nucleotide from the GTPase.
CC   -!- SUBUNIT: Interacts with CDC42EP1, CDC42EP2, CDC42EP3, CDC42EP4,
CC       CDC42EP5, CDC42SE1, CDC42SE2, PARD6A, PARD6B and PARD6G (in a GTP-
CC       dependent manner). Interacts with activated CSPG4 and with BAIAP2.
CC       Interacts with Zizimin1/DOCK9 and Zizimin2/DOCK11, which activate
CC       it by exchanging GDP for GTP. Interacts with NET1 and
CC       ARHGAP33/TCGAP. Part of a complex with PARD3, PARD6A or PARD6B and
CC       PRKCI or PRKCZ. The GTP-bound form interacts with CCPG1. Interacts
CC       with USP6 (By similarity).
CC   -!- INTERACTION:
CC       Q13153:PAK1 (xeno); NbExp=1; IntAct=EBI-81763, EBI-1307;
CC       P63044:Vamp2; NbExp=2; IntAct=EBI-81763, EBI-521920;
CC       P42768:WAS (xeno); NbExp=1; IntAct=EBI-81763, EBI-346375;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2; Synonyms=Placental;
CC         IsoId=P60766-2, P21181-4;
CC         Sequence=Displayed;
CC       Name=1; Synonyms=Brain;
CC         IsoId=P60766-1, P21181-1;
CC         Sequence=VSP_040585, VSP_040586;
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
CC       CDC42 subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; L11318; AAA37410.1; -; mRNA.
DR   EMBL; U37720; AAC00028.1; -; mRNA.
DR   EMBL; L78075; AAB40051.1; -; Genomic_DNA.
DR   EMBL; AK003098; BAB22563.1; -; mRNA.
DR   EMBL; AK051543; BAC34669.1; -; mRNA.
DR   EMBL; AK075567; BAC35825.1; -; mRNA.
DR   EMBL; AK144216; BAE25778.1; -; mRNA.
DR   EMBL; AK151087; BAE30100.1; -; mRNA.
DR   EMBL; AK151726; BAE30644.1; -; mRNA.
DR   EMBL; AK153564; BAE32098.1; -; mRNA.
DR   EMBL; AK154870; BAE32891.1; -; mRNA.
DR   EMBL; AK159470; BAE35111.1; -; mRNA.
DR   EMBL; AK166281; BAE38678.1; -; mRNA.
DR   EMBL; AK167195; BAE39325.1; -; mRNA.
DR   EMBL; AK167400; BAE39489.1; -; mRNA.
DR   EMBL; AK167609; BAE39663.1; -; mRNA.
DR   EMBL; AK168013; BAE40000.1; -; mRNA.
DR   EMBL; AK168076; BAE40049.1; -; mRNA.
DR   EMBL; AK168089; BAE40062.1; -; mRNA.
DR   EMBL; AK168276; BAE40222.1; -; mRNA.
DR   EMBL; AK168758; BAE40595.1; -; mRNA.
DR   EMBL; AK168820; BAE40647.1; -; mRNA.
DR   EMBL; AK169122; BAE40902.1; -; mRNA.
DR   EMBL; AK169232; BAE41001.1; -; mRNA.
DR   EMBL; AK169805; BAE41379.1; -; mRNA.
DR   EMBL; AL645468; CAM18513.1; -; Genomic_DNA.
DR   EMBL; AL645468; CAM18514.1; -; Genomic_DNA.
DR   EMBL; BC064792; AAH64792.1; -; mRNA.
DR   IPI; IPI00113849; -.
DR   IPI; IPI00120193; -.
DR   RefSeq; NP_033991.1; NM_009861.2.
DR   UniGene; Mm.1022; -.
DR   UniGene; Mm.447553; -.
DR   UniGene; Mm.475151; -.
DR   PDB; 3EG5; X-ray; 2.70 A; A/C=1-178.
DR   PDBsum; 3EG5; -.
DR   ProteinModelPortal; P60766; -.
DR   DIP; DIP-32554N; -.
DR   IntAct; P60766; 16.
DR   MINT; MINT-1602743; -.
DR   STRING; P60766; -.
DR   PhosphoSite; P60766; -.
DR   PRIDE; P60766; -.
DR   Ensembl; ENSMUST00000030417; ENSMUSP00000030417; ENSMUSG00000006699.
DR   Ensembl; ENSMUST00000051477; ENSMUSP00000054634; ENSMUSG00000006699.
DR   GeneID; 12540; -.
DR   KEGG; mmu:12540; -.
DR   UCSC; uc008viy.1; mouse.
DR   CTD; 12540; -.
DR   MGI; MGI:106211; Cdc42.
DR   eggNOG; roNOG07751; -.
DR   HOVERGEN; HBG009351; -.
DR   OMA; EITHHCQ; -.
DR   OrthoDB; EOG4R23VV; -.
DR   PhylomeDB; P60766; -.
DR   NextBio; 281582; -.
DR   ArrayExpress; P60766; -.
DR   Bgee; P60766; -.
DR   CleanEx; MM_CDC42; -.
DR   Genevestigator; P60766; -.
DR   GermOnline; ENSMUSG00000006699; Mus musculus.
DR   GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR   GO; GO:0042995; C:cell projection; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IDA:MGI.
DR   GO; GO:0030742; F:GTP-dependent protein binding; IPI:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0051017; P:actin filament bundle assembly; IMP:MGI.
DR   GO; GO:0034332; P:adherens junction organization; IMP:MGI.
DR   GO; GO:0060070; P:canonical Wnt receptor signaling pathway; IMP:MGI.
DR   GO; GO:0034613; P:cellular protein localization; IMP:MGI.
DR   GO; GO:0016197; P:endosome transport; TAS:UniProtKB.
DR   GO; GO:0090136; P:epithelial cell-cell adhesion; IMP:MGI.
DR   GO; GO:0060684; P:epithelial-mesenchymal cell signaling; IMP:MGI.
DR   GO; GO:0035088; P:establishment or maintenance of apical/basal cell polarity; IMP:MGI.
DR   GO; GO:0046847; P:filopodium assembly; IDA:MGI.
DR   GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
DR   GO; GO:0060789; P:hair follicle placode formation; IMP:MGI.
DR   GO; GO:0031424; P:keratinization; IMP:MGI.
DR   GO; GO:0003334; P:keratinocyte development; IMP:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR   GO; GO:0048664; P:neuron fate determination; IMP:MGI.
DR   GO; GO:0007097; P:nuclear migration; IMP:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR   GO; GO:0071338; P:positive regulation of hair follicle cell proliferation; IMP:MGI.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:MGI.
DR   GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:MGI.
DR   GO; GO:0007088; P:regulation of mitosis; IMP:MGI.
DR   GO; GO:0042176; P:regulation of protein catabolic process; IMP:MGI.
DR   GO; GO:0043497; P:regulation of protein heterodimerization activity; IDA:MGI.
DR   GO; GO:0045859; P:regulation of protein kinase activity; IMP:MGI.
DR   GO; GO:0031647; P:regulation of protein stability; IMP:MGI.
DR   GO; GO:0007266; P:Rho protein signal transduction; TAS:MGI.
DR   InterPro; IPR003578; GTPase_Rho.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00174; RHO; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW   Direct protein sequencing; GTP-binding; Lipoprotein; Membrane;
KW   Methylation; Nucleotide-binding; Prenylation.
FT   CHAIN         1    188       Cell division control protein 42 homolog.
FT                                /FTId=PRO_0000030427.
FT   PROPEP      189    191       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000030428.
FT   NP_BIND      10     17       GTP (By similarity).
FT   NP_BIND      57     61       GTP (By similarity).
FT   NP_BIND     115    118       GTP (By similarity).
FT   MOTIF        32     40       Effector region (Potential).
FT   MOD_RES     135    135       N6-acetyllysine (By similarity).
FT   MOD_RES     144    144       N6-acetyllysine (By similarity).
FT   MOD_RES     188    188       Cysteine methyl ester (By similarity).
FT   LIPID       188    188       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   VAR_SEQ     163    163       K -> R (in isoform 1).
FT                                /FTId=VSP_040585.
FT   VAR_SEQ     182    191       PKKSRRCVLL -> TQPKRKCCIF (in isoform 1).
FT                                /FTId=VSP_040586.
FT   MUTAGEN      17     17       T->N: Constitutively inactivated.
FT                                Abolishes interaction with PARD6 and
FT                                DOCK11.
FT   MUTAGEN      61     61       Q->L: Constitutively activated. Enhances
FT                                interaction with DOCK11.
FT   CONFLICT     26     26       N -> D (in Ref. 4; BAC34669).
FT   CONFLICT     66     66       R -> G (in Ref. 6; AAH64792).
FT   CONFLICT     85     85       V -> I (in Ref. 4; BAE39489).
FT   CONFLICT    116    116       Q -> K (in Ref. 4; BAE40049).
FT   CONFLICT    171    171       E -> G (in Ref. 6; AAH64792).
FT   STRAND        6      9
FT   HELIX        17     25
FT   STRAND       36     45
FT   STRAND       50     53
FT   STRAND       55     58
FT   HELIX        62     64
FT   TURN         65     67
FT   HELIX        68     71
FT   STRAND       76     81
FT   HELIX        87     95
FT   HELIX        97    104
FT   STRAND      110    113
FT   HELIX       117    119
FT   HELIX       123    131
FT   HELIX       139    148
FT   TURN        159    161
FT   HELIX       166    177
SQ   SEQUENCE   191 AA;  21259 MW;  51A437E22A4D8FFF CRC64;
     MQTIKCVVVG DGAVGKTCLL ISYTTNKFPS EYVPTVFDNY AVTVMIGGEP YTLGLFDTAG
     QEDYDRLRPL SYPQTDVFLV CFSVVSPSSF ENVKEKWVPE ITHHCPKTPF LLVGTQIDLR
     DDPSTIEKLA KNKQKPITPE TAEKLARDLK AVKYVECSAL TQKGLKNVFD EAILAALEPP
     EPKKSRRCVL L
//
ID   LZTS1_MOUSE             Reviewed;         599 AA.
AC   P60853;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Leucine zipper putative tumor suppressor 1;
DE   AltName: Full=F37/Esophageal cancer-related gene-coding leucine-zipper motif;
DE   AltName: Full=Fez1;
GN   Name=Lzts1; Synonyms=Fez1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/J;
RX   MEDLINE=99199287; PubMed=10097140; DOI=10.1073/pnas.96.7.3928;
RA   Ishii H., Baffa R., Numata S., Murakumo Y., Rattan S., Inoue H.,
RA   Mori M., Fidanza V., Alder H., Croce C.M.;
RT   "The FEZ1 gene at chromosome 8p22 encodes a leucine-zipper protein,
RT   and its expression is altered in multiple human tumors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:3928-3933(1999).
CC   -!- FUNCTION: Involved in the regulation of cell growth. May stabilize
CC       the active CDC2-cyclin B1 complex and thereby contribute to the
CC       regulation of the cell cycle and the prevention of uncontrolled
CC       cell proliferation. May act as tumor suppressor (By similarity).
CC   -!- SUBUNIT: Binds EEF1G and CDK1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By
CC       similarity). Cell projection, dendritic spine (By similarity).
CC       Cell junction, synapse, postsynaptic cell membrane, postsynaptic
CC       density (By similarity). Cell junction, synapse (By similarity).
CC       Note=Associated with the plasma membrane and with microtubules.
CC       Detected in dendritic spines, especially in the postsynaptic
CC       density (By similarity).
CC   -!- PTM: Phorphorylated on serine residues. Hyperphosphorylated by the
CC       cAMP-dependent kinase PKA during cell-cycle progression (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the LZTS family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF288601; AAQ14349.1; -; mRNA.
DR   IPI; IPI00400411; -.
DR   UniGene; Mm.479807; -.
DR   ProteinModelPortal; P60853; -.
DR   STRING; P60853; -.
DR   PhosphoSite; P60853; -.
DR   PRIDE; P60853; -.
DR   Ensembl; ENSMUST00000037049; ENSMUSP00000039397; ENSMUSG00000036306.
DR   UCSC; uc009lxa.1; mouse.
DR   MGI; MGI:2684762; Lzts1.
DR   GeneTree; ENSGT00510000046769; -.
DR   HOGENOM; HBG713386; -.
DR   HOVERGEN; HBG052381; -.
DR   InParanoid; P60853; -.
DR   OrthoDB; EOG4F1X32; -.
DR   NextBio; 373144; -.
DR   Bgee; P60853; -.
DR   CleanEx; MM_LZTS1; -.
DR   Genevestigator; P60853; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR009638; Fez1.
DR   Pfam; PF06818; Fez1; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell junction; Cell membrane; Cell projection;
KW   Coiled coil; Cytoplasm; Lipoprotein; Membrane; Myristate;
KW   Phosphoprotein; Postsynaptic cell membrane; Synapse; Tumor suppressor.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    599       Leucine zipper putative tumor suppressor
FT                                1.
FT                                /FTId=PRO_0000182972.
FT   COILED      256    572       Potential.
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
SQ   SEQUENCE   599 AA;  67308 MW;  7B77A3BCF2480593 CRC64;
     MGSVSSLISG HSFHSKHCRA SQYKLRKSSH LKKLNRYSDG LLRFGFSQDS GRGKSSSKMG
     KSEDFFYIKV SQKARGSHRP DYTALSSGDM GGQTGVDFDP ATPPKLMPFS NQLEMSSDKG
     AVRPTAFKPV LPRSGAILHS SPESTSHQLH PMPPDKPKEQ ELKPGLCSGA LSDSGRNSMS
     SLPTHSTTSS YQLDPLVTPV GPTSRFGGSA HNITQGIILQ DSNMMSLKAL SFSDGGSKLA
     HPGKADKGAS CVRSPLSTDE CTIQELEQKL LQRETALQKL QRSFDEKEFA SGQTFEERPR
     RTRDELECLE PKSKLKPPSQ KSQRTQQVLQ LQVLQLQQEK RQLRQELESL MKEQDLLETK
     LRSYEREKTN FAPALEETQW EVCQKSGEIS LLKQQLKESQ LEVNTKASEI LSLKAQLKDT
     RGKLDGMELK TQDLESALRT KGLELEVCEN ELQRKKNEAE LLREKVNLLE QELMELRAQA
     ALHPAPLGPP GVGLTFSEDI PALQRELDRL RAELKEERQG HDQMSSGFQH ERLVWKEEKE
     KVIQYQRQLQ QSYLAMYQRN QRLEKALQQL ARGDGPGEPF EIDLEGADIP YEDIIATEI
//
ID   SNP25_MOUSE             Reviewed;         206 AA.
AC   P60879; A2AIC2; A2AIC3; P13795; P36974; P70557; P70558; Q8IXK3;
AC   Q96FM2; Q9BR45;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Synaptosomal-associated protein 25;
DE            Short=SNAP-25;
DE   AltName: Full=Super protein;
DE            Short=SUP;
DE   AltName: Full=Synaptosomal-associated 25 kDa protein;
GN   Name=Snap25; Synonyms=Snap;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SNAP-25A), AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=BALB/c;
RX   MEDLINE=90078337; PubMed=2592413; DOI=10.1083/jcb.109.6.3039;
RA   Oyler G.A., Higgins G.A., Hart R.A., Battenberg E., Billingsley M.,
RA   Bloom F.E., Wilson M.C.;
RT   "The identification of a novel synaptosomal-associated protein, SNAP-
RT   25, differentially expressed by neuronal subpopulations.";
RL   J. Cell Biol. 109:3039-3052(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SNAP-25A).
RC   STRAIN=ILS, and ISS;
RX   MEDLINE=21363810; PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SNAP-25B).
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SNAP-25A).
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 18-31; 60-72; 125-135 AND 143-176, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [8]
RP   PALMITOYLATION AT CYS-85; CYS-88; CYS-90 AND CYS-92, AND MUTAGENESIS
RP   OF CYS-85; CYS-88; CYS-90 AND CYS-92.
RX   PubMed=9349529;
RA   Lane S.R., Liu Y.;
RT   "Characterization of the palmitoylation domain of SNAP-25.";
RL   J. Neurochem. 69:1864-1869(1997).
RN   [9]
RP   INTERACTION WITH SNAPIN.
RX   MEDLINE=99211098; PubMed=10195194; DOI=10.1038/5673;
RA   Ilardi J.M., Mochida S., Sheng Z.-H.;
RT   "Snapin: a SNARE-associated protein implicated in synaptic
RT   transmission.";
RL   Nat. Neurosci. 2:119-124(1999).
RN   [10]
RP   PHOSPHORYLATION AT THR-138 AND SER-187.
RX   MEDLINE=22347237; PubMed=12459461; DOI=10.1016/S0014-5793(02)03629-3;
RA   Hepp R., Cabaniols J.-P., Roche P.A.;
RT   "Differential phosphorylation of SNAP-25 in vivo by protein kinase C
RT   and protein kinase A.";
RL   FEBS Lett. 532:52-56(2002).
RN   [11]
RP   INTERACTION WITH SYT1; SV2B AND SYNTAXIN-1.
RX   PubMed=15466855; DOI=10.1074/jbc.M407502200;
RA   Lazzell D.R., Belizaire R., Thakur P., Sherry D.M., Janz R.;
RT   "SV2B regulates synaptotagmin 1 by direct interaction.";
RL   J. Biol. Chem. 279:52124-52131(2004).
RN   [12]
RP   INTERACTION WITH OTOF.
RC   STRAIN=BALB/c; TISSUE=Cochlea;
RX   PubMed=17055430; DOI=10.1016/j.cell.2006.08.040;
RA   Roux I., Safieddine S., Nouvian R., Grati M., Simmler M.-C.,
RA   Bahloul A., Perfettini I., Le Gall M., Rostaing P., Hamard G.,
RA   Triller A., Avan P., Moser T., Petit C.;
RT   "Otoferlin, defective in a human deafness form, is essential for
RT   exocytosis at the auditory ribbon synapse.";
RL   Cell 127:277-289(2006).
RN   [13]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CENPF.
RX   PubMed=16672379; DOI=10.1091/mbc.E05-12-1127;
RA   Pooley R.D., Reddy S., Soukoulis V., Roland J.T., Goldenring J.R.,
RA   Bader D.M.;
RT   "CytLEK1 is a regulator of plasma membrane recycling through its
RT   interaction with SNAP-25.";
RL   Mol. Biol. Cell 17:3176-3186(2006).
RN   [14]
RP   3D-STRUCTURE MODELING OF 18-206 IN COMPLEX WITH VAMP2 AND STX1A.
RX   PubMed=9731768; DOI=10.1038/1799;
RA   Poirier M.A., Xiao W., Macosko J.C., Chan C., Shin Y.K., Bennett M.K.;
RT   "The synaptic SNARE complex is a parallel four-stranded helical
RT   bundle.";
RL   Nat. Struct. Biol. 5:765-769(1998).
CC   -!- FUNCTION: t-SNARE involved in the molecular regulation of
CC       neurotransmitter release. May play an important role in the
CC       synaptic function of specific neuronal systems. Associates with
CC       proteins involved in vesicle docking and membrane fusion.
CC       Regulates plasma membrane recycling through its interaction with
CC       CENPF.
CC   -!- SUBUNIT: Part of the SNARE core complex containing SNAP25, VAMP2
CC       and STX1A. This complex binds CPLX1. Interacts with TRIM9, RIMS1,
CC       SNAPIN and HGS. Binds STXBP6. Found in a ternary complex with
CC       STX1A and VAMP8 (By similarity). Found in a complex containing
CC       SYT1, SV2B and syntaxin-1. Interacts with CENPF and OTOF.
CC   -!- INTERACTION:
CC       Q155P7:Cenpf; NbExp=5; IntAct=EBI-445270, EBI-2211248;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Cell
CC       membrane; Lipid-anchor. Cell junction, synapse, synaptosome.
CC       Note=Membrane association requires palmitoylation. Expressed
CC       throughout cytoplasm, concentrating at the perinuclear region.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Isoforms differ by the usage of two alternative
CC         homologous exons (5a and 5b) which encode for positions 56 to 94
CC         and differ only in 9 positions out of 39;
CC       Name=SNAP-25b;
CC         IsoId=P60879-1, P13795-1;
CC         Sequence=Displayed;
CC       Name=SNAP-25a;
CC         IsoId=P60879-2, P13795-2;
CC         Sequence=VSP_010019;
CC   -!- PTM: Palmitoylated. Cys-85 appears to be the main site, and
CC       palmitoylation is required for membrane association.
CC   -!- SIMILARITY: Belongs to the SNAP-25 family.
CC   -!- SIMILARITY: Contains 2 t-SNARE coiled-coil homology domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; M22012; AAA61741.1; -; mRNA.
DR   EMBL; AF483516; AAL90790.1; -; mRNA.
DR   EMBL; AF483517; AAL90791.1; -; mRNA.
DR   EMBL; AK078038; BAC37105.1; -; mRNA.
DR   EMBL; AL732447; CAM15064.1; -; Genomic_DNA.
DR   EMBL; AL732447; CAM15065.1; -; Genomic_DNA.
DR   EMBL; CH466519; EDL28390.1; -; Genomic_DNA.
DR   EMBL; BC018249; AAH18249.1; -; mRNA.
DR   IPI; IPI00125635; -.
DR   IPI; IPI00225389; -.
DR   PIR; A33623; A33623.
DR   RefSeq; NP_035558.1; NM_011428.3.
DR   UniGene; Mm.45953; -.
DR   PDB; 2BU0; Model; -; C=18-82, D=139-206.
DR   PDBsum; 2BU0; -.
DR   ProteinModelPortal; P60879; -.
DR   SMR; P60879; 10-78, 131-204.
DR   DIP; DIP-29066N; -.
DR   DIP; DIP-65N; -.
DR   IntAct; P60879; 29.
DR   MINT; MINT-2411221; -.
DR   STRING; P60879; -.
DR   PhosphoSite; P60879; -.
DR   PRIDE; P60879; -.
DR   Ensembl; ENSMUST00000028727; ENSMUSP00000028727; ENSMUSG00000027273.
DR   Ensembl; ENSMUST00000110098; ENSMUSP00000105725; ENSMUSG00000027273.
DR   GeneID; 20614; -.
DR   KEGG; mmu:20614; -.
DR   UCSC; uc008mop.1; mouse.
DR   CTD; 20614; -.
DR   MGI; MGI:98331; Snap25.
DR   eggNOG; roNOG14459; -.
DR   GeneTree; ENSGT00390000012186; -.
DR   HOVERGEN; HBG056971; -.
DR   InParanoid; P60879; -.
DR   OMA; CVCPWKK; -.
DR   OrthoDB; EOG4X3H29; -.
DR   PhylomeDB; P60879; -.
DR   NextBio; 298983; -.
DR   ArrayExpress; P60879; -.
DR   Bgee; P60879; -.
DR   CleanEx; MM_SNAP25; -.
DR   Genevestigator; P60879; -.
DR   GermOnline; ENSMUSG00000027273; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0019717; C:synaptosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR   InterPro; IPR000928; SNAP-25.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   Pfam; PF00835; SNAP-25; 1.
DR   Pfam; PF05739; SNARE; 1.
DR   SMART; SM00397; t_SNARE; 2.
DR   PROSITE; PS50192; T_SNARE; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW   Coiled coil; Cytoplasm; Direct protein sequencing; Lipoprotein;
KW   Membrane; Palmitate; Phosphoprotein; Repeat; Synapse; Synaptosome.
FT   CHAIN         1    206       Synaptosomal-associated protein 25.
FT                                /FTId=PRO_0000213589.
FT   DOMAIN       19     81       t-SNARE coiled-coil homology 1.
FT   DOMAIN      140    202       t-SNARE coiled-coil homology 2.
FT   REGION        1     75       Interaction with CENPF.
FT   COMPBIAS     85     92       Cys-rich.
FT   SITE        180    181       Cleavage; by BONT/E (By similarity).
FT   MOD_RES     138    138       Phosphothreonine; by PKC and PKA.
FT   MOD_RES     187    187       Phosphoserine; by PKC.
FT   LIPID        85     85       S-palmitoyl cysteine.
FT   LIPID        88     88       S-palmitoyl cysteine.
FT   LIPID        90     90       S-palmitoyl cysteine.
FT   LIPID        92     92       S-palmitoyl cysteine.
FT   VAR_SEQ      58     89       ERIEEGMDQINKDMKEAEKNLTDLGKFCGLCV -> DRVEE
FT                                GMNHINQDMKEAEKNLKDLGKCCGLFI (in isoform
FT                                SNAP-25a).
FT                                /FTId=VSP_010019.
FT   MUTAGEN      85     85       C->S: 91% reduction in palmitoylation
FT                                level. 14% membrane association. No
FT                                palmitoylation and less than 8% membrane
FT                                association; when associated with S-88 or
FT                                A-88.
FT   MUTAGEN      88     88       C->S: 79% reduction in palmitoylation
FT                                level. 18% membrane association. No
FT                                palmitoylation and less than 8% membrane
FT                                association; when associated with S-85 or
FT                                A-85.
FT   MUTAGEN      90     90       C->S: 58% reduction in palmitoylation
FT                                level. 28% membrane association. Very
FT                                little palmitoylation and less than 8%
FT                                membrane association; when associated
FT                                with S-92 or A-92.
FT   MUTAGEN      92     92       C->S: 65% reduction in palmitoylation
FT                                level. 29% membrane association. No
FT                                palmitoylation and less than 8% membrane
FT                                association; when associated with S-90 or
FT                                A-90.
FT   HELIX        21     73
FT   TURN         74     76
FT   HELIX        77     81
FT   TURN        140    143
FT   HELIX       144    202
FT   TURN        203    205
SQ   SEQUENCE   206 AA;  23315 MW;  FBED2B082A4CB6A6 CRC64;
     MAEDADMRNE LEEMQRRADQ LADESLESTR RMLQLVEESK DAGIRTLVML DEQGEQLERI
     EEGMDQINKD MKEAEKNLTD LGKFCGLCVC PCNKLKSSDA YKKAWGNNQD GVVASQPARV
     VDEREQMAIS GGFIRRVTND ARENEMDENL EQVSGIIGNL RHMALDMGNE IDTQNRQIDR
     IMEKADSNKT RIDEANQRAT KMLGSG
//
ID   DNJC5_MOUSE             Reviewed;         198 AA.
AC   P60904; P54101;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=DnaJ homolog subfamily C member 5;
DE   AltName: Full=Cysteine string protein;
DE            Short=CSP;
GN   Name=Dnajc5; Synonyms=Csp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Qin N., Lin T., Birnbaumer L.;
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF 8-24 AND 42-72, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11; SER-12 AND TYR-17,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND THR-11, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-12 AND SER-15,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [11]
RP   STRUCTURE BY NMR OF 5-100.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of J-domain from mouse DnaJ subfamily C member
RT   5.";
RL   Submitted (NOV-2005) to the PDB data bank.
CC   -!- FUNCTION: May have an important role in presynaptic function. May
CC       be involved in calcium-dependent neurotransmitter release at nerve
CC       endings (By similarity).
CC   -!- SUBUNIT: Homodimer (Probable).
CC   -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor (By similarity).
CC       Melanosome (By similarity).
CC   -!- PTM: Fatty acylated. Heavily palmitoylated in the cysteine string
CC       motif (By similarity).
CC   -!- SIMILARITY: Contains 1 J domain.
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DR   EMBL; AF032115; AAB87080.1; -; mRNA.
DR   EMBL; AK029006; BAC26236.1; -; mRNA.
DR   EMBL; AK032373; BAC27841.1; -; mRNA.
DR   IPI; IPI00132206; -.
DR   RefSeq; NP_058055.1; NM_016775.2.
DR   UniGene; Mm.140761; -.
DR   UniGene; Mm.391807; -.
DR   PDB; 2CTW; NMR; -; A=5-100.
DR   PDBsum; 2CTW; -.
DR   ProteinModelPortal; P60904; -.
DR   SMR; P60904; 5-100.
DR   STRING; P60904; -.
DR   PhosphoSite; P60904; -.
DR   PRIDE; P60904; -.
DR   Ensembl; ENSMUST00000072334; ENSMUSP00000072175; ENSMUSG00000000826.
DR   Ensembl; ENSMUST00000108796; ENSMUSP00000104424; ENSMUSG00000000826.
DR   Ensembl; ENSMUST00000108797; ENSMUSP00000104425; ENSMUSG00000000826.
DR   GeneID; 13002; -.
DR   KEGG; mmu:13002; -.
DR   UCSC; uc008omp.1; mouse.
DR   CTD; 13002; -.
DR   MGI; MGI:892995; Dnajc5.
DR   GeneTree; ENSGT00600000084291; -.
DR   HOVERGEN; HBG005414; -.
DR   OrthoDB; EOG4NZTVC; -.
DR   PhylomeDB; P60904; -.
DR   NextBio; 282820; -.
DR   ArrayExpress; P60904; -.
DR   Bgee; P60904; -.
DR   CleanEx; MM_DNAJC5; -.
DR   Genevestigator; P60904; -.
DR   GermOnline; ENSMUSG00000000826; Mus musculus.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0043524; P:negative regulation of neuron apoptosis; IGI:MGI.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   InterPro; IPR001623; DnaJ_N.
DR   InterPro; IPR018253; Heat_shock_DnaJ_CS.
DR   InterPro; IPR003095; Hsp_DnaJ.
DR   Gene3D; G3DSA:1.10.287.110; DnaJ_N; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; DnaJ_N; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Chaperone; Direct protein sequencing;
KW   Lipoprotein; Membrane; Palmitate; Phosphoprotein.
FT   CHAIN         1    198       DnaJ homolog subfamily C member 5.
FT                                /FTId=PRO_0000071053.
FT   DOMAIN       13     82       J.
FT   COMPBIAS    118    128       Poly-Cys.
FT   MOD_RES       8      8       Phosphoserine.
FT   MOD_RES      10     10       Phosphoserine.
FT   MOD_RES      11     11       Phosphothreonine.
FT   MOD_RES      12     12       Phosphoserine.
FT   MOD_RES      15     15       Phosphoserine.
FT   MOD_RES      17     17       Phosphotyrosine.
FT   MOD_RES      41     41       N6-acetyllysine (By similarity).
FT   MOD_RES      56     56       N6-acetyllysine (By similarity).
FT   HELIX        16     20
FT   HELIX        28     41
FT   TURN         44     46
FT   HELIX        51     67
FT   HELIX        70     78
FT   HELIX        81     89
SQ   SEQUENCE   198 AA;  22101 MW;  52F98261FBAD978F CRC64;
     MADQRQRSLS TSGESLYHVL GLDKNATSDD IKKSYRKLAL KYHPDKNPDN PEAADKFKEI
     NNAHAILTDA TKRNIYDKYG SLGLYVAEQF GEENVNTYFV LSSWWAKALF VVCGLLTCCY
     CCCCLCCCFN CCCGKCKPKA PEGEETEFYV SPEDLEAQLQ SDEREATDTP IVIQPASATE
     TTQLTADSHP SYHTDGFN
//
ID   CHP1_MOUSE              Reviewed;         195 AA.
AC   P61022; Q62877; Q6ZWQ8;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Calcium-binding protein p22;
DE   AltName: Full=Calcineurin homologous protein;
DE   AltName: Full=Calcium-binding protein CHP;
DE   AltName: Full=Sid 470;
GN   Name=Chp; Synonyms=Sid470;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.;
RT   "Mouse calcium binding protein p22.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, C57BL/6J, and NOD;
RC   TISSUE=Corpora quadrigemina, Liver, Mammary gland, Placenta, and
RC   Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Required for constitutive membrane traffic. Inhibits
CC       GTPase-stimulated Na(+)/H(+) exchange. Also inhibits calcineurin
CC       phosphatase activity. Required for activity of SLC9A1/NHE1 (By
CC       similarity).
CC   -!- SUBUNIT: Monomer (By similarity). Specifically binds to
CC       SLC9A1/NHE1 at a domain that is critical for growth factor
CC       stimulation of exchange activity (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- PTM: Both N-myristoylation and calcium-mediated conformational
CC       changes are essential for its function (By similarity).
CC   -!- SIMILARITY: Contains 4 EF-hand domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; AB025217; BAA84688.1; -; mRNA.
DR   EMBL; AK005067; BAB23791.1; -; mRNA.
DR   EMBL; AK045920; BAC32532.1; -; mRNA.
DR   EMBL; AK156588; BAE33769.1; -; mRNA.
DR   EMBL; AK166219; BAE38637.1; -; mRNA.
DR   EMBL; AK167179; BAE39314.1; -; mRNA.
DR   EMBL; AK167720; BAE39762.1; -; mRNA.
DR   EMBL; AK168284; BAE40230.1; -; mRNA.
DR   EMBL; AK169146; BAE40925.1; -; mRNA.
DR   EMBL; BC054733; AAH54733.1; -; mRNA.
DR   EMBL; BC064784; AAH64784.1; -; mRNA.
DR   IPI; IPI00229680; -.
DR   RefSeq; NP_062743.1; NM_019769.3.
DR   UniGene; Mm.214765; -.
DR   ProteinModelPortal; P61022; -.
DR   SMR; P61022; 1-195.
DR   STRING; P61022; -.
DR   PhosphoSite; P61022; -.
DR   PRIDE; P61022; -.
DR   Ensembl; ENSMUST00000014221; ENSMUSP00000014221; ENSMUSG00000014077.
DR   GeneID; 56398; -.
DR   KEGG; mmu:56398; -.
DR   UCSC; uc008ltw.1; mouse.
DR   MGI; MGI:1927185; 1500003O03Rik.
DR   GeneTree; ENSGT00600000084053; -.
DR   HOGENOM; HBG746798; -.
DR   HOVERGEN; HBG105307; -.
DR   InParanoid; P61022; -.
DR   OMA; TPNQIER; -.
DR   OrthoDB; EOG4PG61X; -.
DR   PhylomeDB; P61022; -.
DR   NextBio; 462031; -.
DR   ArrayExpress; P61022; -.
DR   Bgee; P61022; -.
DR   CleanEx; MM_1500003O03RIK; -.
DR   Genevestigator; P61022; -.
DR   GermOnline; ENSMUSG00000014077; Mus musculus.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   SMART; SM00054; EFh; 2.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 3.
PE   2: Evidence at transcript level;
KW   Calcium; Cytoplasm; Lipoprotein; Metal-binding; Myristate; Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    195       Calcium-binding protein p22.
FT                                /FTId=PRO_0000073844.
FT   DOMAIN       26     61       EF-hand 1.
FT   DOMAIN       71    106       EF-hand 2.
FT   DOMAIN      110    145       EF-hand 3.
FT   DOMAIN      151    186       EF-hand 4.
FT   CA_BIND     123    134       1 (By similarity).
FT   CA_BIND     164    175       2 (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (Probable).
SQ   SEQUENCE   195 AA;  22432 MW;  7B803EF0ABED829E CRC64;
     MGSRASTLLR DEELEEIKKE TGFSHSQITR LYSRFTSLDK GENGTLSRED FQRIPELAIN
     PLGDRIINAF FSEGEDQVNF RGFMRTLAHF RPIEDNEKSK DVNGPEPLNS RSNKLHFAFR
     LYDLDKDDKI SRDELLQVLR MMVGVNISDE QLGSIADRTI QEADQDGDSA ISFTEFVKVL
     EKVDVEQKMS IRFLH
//
ID   RAB10_MOUSE             Reviewed;         200 AA.
AC   P61027; O88386; Q9D7X6;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Ras-related protein Rab-10;
GN   Name=Rab10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Zeng Q., Tan Y.H., Hong W.;
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Brain, Stomach, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 12-22; 60-70; 96-102; 106-117 AND 148-172, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: May be involved in vesicular trafficking and
CC       neurotransmitter release.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR   EMBL; AF035646; AAC29313.1; -; mRNA.
DR   EMBL; AK008725; BAB25858.1; -; mRNA.
DR   EMBL; AK028320; BAC25878.1; -; mRNA.
DR   EMBL; AK087964; BAC40062.1; -; mRNA.
DR   EMBL; BC056374; AAH56374.1; -; mRNA.
DR   IPI; IPI00130118; -.
DR   RefSeq; NP_057885.1; NM_016676.5.
DR   UniGene; Mm.378993; -.
DR   ProteinModelPortal; P61027; -.
DR   SMR; P61027; 4-173.
DR   STRING; P61027; -.
DR   PhosphoSite; P61027; -.
DR   PRIDE; P61027; -.
DR   Ensembl; ENSMUST00000021001; ENSMUSP00000021001; ENSMUSG00000020671.
DR   GeneID; 19325; -.
DR   KEGG; mmu:19325; -.
DR   UCSC; uc007mwl.1; mouse.
DR   CTD; 19325; -.
DR   MGI; MGI:105066; Rab10.
DR   eggNOG; roNOG07115; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; P61027; -.
DR   OMA; EHASEDV; -.
DR   OrthoDB; EOG4K3KX6; -.
DR   PhylomeDB; P61027; -.
DR   NextBio; 296287; -.
DR   ArrayExpress; P61027; -.
DR   Bgee; P61027; -.
DR   CleanEx; MM_RAB10; -.
DR   Genevestigator; P61027; -.
DR   GermOnline; ENSMUSG00000020671; Mus musculus.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Direct protein sequencing; GTP-binding;
KW   Lipoprotein; Membrane; Nucleotide-binding; Prenylation;
KW   Protein transport; Transport.
FT   CHAIN         1    200       Ras-related protein Rab-10.
FT                                /FTId=PRO_0000121147.
FT   NP_BIND      16     23       GTP (By similarity).
FT   NP_BIND      64     68       GTP (By similarity).
FT   NP_BIND     122    125       GTP (By similarity).
FT   MOTIF        38     46       Effector region (By similarity).
FT   MOD_RES     102    102       N6-acetyllysine (By similarity).
FT   LIPID       199    199       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   LIPID       200    200       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   CONFLICT    106    106       N -> H (in Ref. 2; BAB25858).
SQ   SEQUENCE   200 AA;  22541 MW;  7F02B8E8E46EE1E8 CRC64;
     MAKKTYDLLF KLLLIGDSGV GKTCVLFRFS DDAFNTTFIS TIGIDFKIKT VELQGKKIKL
     QIWDTAGQER FHTITTSYYR GAMGIMLVYD ITNGKSFENI SKWLRNIDEH ANEDVERMLL
     GNKCDMDDKR VVPKGKGEQI AREHGIRFFE TSAKANINIE KAFLTLAEDI LRKTPVKEPN
     SENVDISSGG GVTGWKSKCC
//
ID   RAB8B_MOUSE             Reviewed;         207 AA.
AC   P61028; Q3U1Z3;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 1.
DT   30-NOV-2010, entry version 72.
DE   RecName: Full=Ras-related protein Rab-8B;
GN   Name=Rab8b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH OTOF.
RX   PubMed=18772196; DOI=10.1093/hmg/ddn279;
RA   Heidrych P., Zimmermann U., Bress A., Pusch C.M., Ruth P., Pfister M.,
RA   Knipper M., Blin N.;
RT   "Rab8b GTPase, a protein transport regulator, is an interacting
RT   partner of otoferlin, defective in a human autosomal recessive
RT   deafness form.";
RL   Hum. Mol. Genet. 17:3814-3821(2008).
CC   -!- FUNCTION: May be involved in vesicular trafficking and
CC       neurotransmitter release (By similarity).
CC   -!- SUBUNIT: Interacts with PEX5R (By similarity). Interacts with
CC       OTOF.
CC   -!- INTERACTION:
CC       Q9NR09:BIRC6 (xeno); NbExp=1; IntAct=EBI-911674, EBI-1765160;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK084650; BAC39239.1; -; mRNA.
DR   EMBL; AK155621; BAE33350.1; -; mRNA.
DR   EMBL; BC059208; AAH59208.1; -; mRNA.
DR   IPI; IPI00411115; -.
DR   RefSeq; NP_775589.1; NM_173413.3.
DR   UniGene; Mm.260376; -.
DR   ProteinModelPortal; P61028; -.
DR   SMR; P61028; 3-175.
DR   IntAct; P61028; 3.
DR   STRING; P61028; -.
DR   PhosphoSite; P61028; -.
DR   PRIDE; P61028; -.
DR   Ensembl; ENSMUST00000041139; ENSMUSP00000041857; ENSMUSG00000036943.
DR   GeneID; 235442; -.
DR   KEGG; mmu:235442; -.
DR   UCSC; uc009qfk.1; mouse.
DR   CTD; 235442; -.
DR   MGI; MGI:2442982; Rab8b.
DR   eggNOG; roNOG09936; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; P61028; -.
DR   OMA; CDMNEKR; -.
DR   PhylomeDB; P61028; -.
DR   NextBio; 382678; -.
DR   ArrayExpress; P61028; -.
DR   Bgee; P61028; -.
DR   CleanEx; MM_RAB8B; -.
DR   Genevestigator; P61028; -.
DR   GermOnline; ENSMUSG00000036943; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; GTP-binding; Lipoprotein; Membrane;
KW   Methylation; Nucleotide-binding; Phosphoprotein; Prenylation;
KW   Protein transport; Transport.
FT   CHAIN         1    204       Ras-related protein Rab-8B.
FT                                /FTId=PRO_0000121135.
FT   PROPEP      205    207       Removed in mature form (Potential).
FT                                /FTId=PRO_0000370801.
FT   NP_BIND      15     22       GTP (By similarity).
FT   NP_BIND      63     67       GTP (By similarity).
FT   NP_BIND     121    124       GTP (By similarity).
FT   MOTIF        37     45       Effector region (By similarity).
FT   MOD_RES       3      3       N6-acetyllysine (By similarity).
FT   MOD_RES       5      5       Phosphotyrosine (By similarity).
FT   MOD_RES     204    204       Cysteine methyl ester (Potential).
FT   LIPID       204    204       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   207 AA;  23603 MW;  4A41AB26BF9DCAF4 CRC64;
     MAKTYDYLFK LLLIGDSGVG KTCLLFRFSE DAFNTTFIST IGIDFKIRTI ELDGKKIKLQ
     IWDTAGQERF RTITTAYYRG AMGIMLVYDI TNEKSFDNIK NWIRNIEEHA SSDVERMILG
     NKCDMNDKRQ VSKERGEKLA IDYGIKFLET SAKSSTNVEE AFFTLARDIM TKLNRKMNDS
     NSSGAGGPVK ITESRSKKTS FFRCSLL
//
ID   UBE2K_MOUSE             Reviewed;         200 AA.
AC   P61087; O54806; P27924; Q16721; Q9CVV9;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 K;
DE            EC=6.3.2.19;
DE   AltName: Full=Huntingtin-interacting protein 2;
DE            Short=HIP-2;
DE   AltName: Full=Ubiquitin carrier protein;
DE   AltName: Full=Ubiquitin-conjugating enzyme E2-25 kDa;
DE            Short=Ubiquitin-conjugating enzyme E2(25K);
DE            Short=Ubiquitin-conjugating enzyme E2-25K;
DE   AltName: Full=Ubiquitin-protein ligase;
GN   Name=Ube2k; Synonyms=Hip2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   TISSUE=Brain;
RX   PubMed=10585161; DOI=10.1016/S0891-0618(99)00030-7;
RA   Tanno Y., Mori T., Yokoya S., Kanazawa K., Honma Y., Nikaido T.,
RA   Takeda J., Tojo M., Yamamoto T., Wanaka A.;
RT   "Localization of huntingtin-interacting protein-2 (Hip-2) mRNA in the
RT   developing mouse brain.";
RL   J. Chem. Neuroanat. 17:99-107(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Bone, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 85-200.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   FUNCTION IN UBIQUITINATION OF CASP12, AND DISRUPTION PHENOTYPE.
RX   PubMed=18710920; DOI=10.1083/jcb.200711066;
RA   Song S., Lee H., Kam T.I., Tai M.L., Lee J.Y., Noh J.Y., Shim S.M.,
RA   Seo S.J., Kong Y.Y., Nakagawa T., Chung C.W., Choi D.Y., Oubrahim H.,
RA   Jung Y.K.;
RT   "E2-25K/Hip-2 regulates caspase-12 in ER stress-mediated Abeta
RT   neurotoxicity.";
RL   J. Cell Biol. 182:675-684(2008).
CC   -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC       covalent attachment to other proteins. In vitro, in the presence
CC       or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase
CC       complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin
CC       chains. Does not transfer ubiquitin directly to but elongates
CC       monoubiquitinated substrate protein. Mediates the selective
CC       degradation of short-lived and abnormal proteins, such as the
CC       endoplasmic reticulum-associated degradation (ERAD) of misfolded
CC       lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell
CC       formation by the suppression of apoptosis of lipid-bearing
CC       macrophages through ubiquitination and subsequence degradation of
CC       p53/TP53. Proposed to be involved in ubiquitination and
CC       proteolytic processing of NF-kappa-B; in vitro supports
CC       ubiquitination of NFKB1. Involved in stabilization of CASP12
CC       during ER stress-mediated beta-amyloid neurotoxicity probably by
CC       inhibiting proteasome activity; in vitro ubiquitinates CASP12.
CC   -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC       diphosphate + protein N-ubiquityllysine.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with RNF138/NARF. Interacts with BRCA1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, with highest levels
CC       found in the mitral cells of the olfactory bulb, the pyramidal
CC       cell layer of the hippocampus and the Purkinje cells of the
CC       cerebellar cortex.
CC   -!- DEVELOPMENTAL STAGE: Expressed at all stages of brain development
CC       and increases significantly between postnatal days 7 and 14.
CC   -!- PTM: Sumoylation at Lys-14 impairs catalytic activity (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Neurons are resistant to beta-amyloid
CC       neurotoxicity. Significantly lower CASP12 expression in brain.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC   -!- SIMILARITY: Contains 1 UBA domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB011081; BAA24927.1; -; mRNA.
DR   EMBL; BC002013; AAH02013.1; -; mRNA.
DR   EMBL; BC085311; AAH85311.1; -; mRNA.
DR   EMBL; AK006316; BAB24523.1; -; mRNA.
DR   IPI; IPI00322440; -.
DR   RefSeq; NP_058066.2; NM_016786.3.
DR   UniGene; Mm.319512; -.
DR   UniGene; Mm.441014; -.
DR   ProteinModelPortal; P61087; -.
DR   SMR; P61087; 3-200.
DR   STRING; P61087; -.
DR   PhosphoSite; P61087; -.
DR   REPRODUCTION-2DPAGE; P61087; -.
DR   PRIDE; P61087; -.
DR   Ensembl; ENSMUST00000031105; ENSMUSP00000031105; ENSMUSG00000029203.
DR   GeneID; 53323; -.
DR   KEGG; mmu:53323; -.
DR   UCSC; uc008xnu.1; mouse.
DR   CTD; 53323; -.
DR   MGI; MGI:1858216; Ube2k.
DR   GeneTree; ENSGT00590000083155; -.
DR   HOGENOM; HBG756483; -.
DR   HOVERGEN; HBG063308; -.
DR   InParanoid; P61087; -.
DR   OMA; ILKDNWA; -.
DR   PhylomeDB; P61087; -.
DR   BRENDA; 6.3.2.19; 244.
DR   NextBio; 310133; -.
DR   ArrayExpress; P61087; -.
DR   Bgee; P61087; -.
DR   Genevestigator; P61087; -.
DR   GermOnline; ENSMUSG00000029203; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0043687; P:post-translational protein modification; IEA:InterPro.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0051246; P:regulation of protein metabolic process; IEA:InterPro.
DR   InterPro; IPR009060; UBA-like.
DR   InterPro; IPR000449; UBA/transl_elong_EF1B_N.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Gene3D; G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.
DR   Pfam; PF00627; UBA; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF46934; UBA_like; 1.
DR   SUPFAM; SSF54495; UBQ-conjugat/RWD-like; 1.
DR   PROSITE; PS50030; UBA; 1.
DR   PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
DR   PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Isopeptide bond; Ligase;
KW   Nucleotide-binding; Ubl conjugation; Ubl conjugation pathway.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    200       Ubiquitin-conjugating enzyme E2 K.
FT                                /FTId=PRO_0000082444.
FT   DOMAIN      160    200       UBA.
FT   ACT_SITE     92     92       Glycyl thioester intermediate (By
FT                                similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      14     14       N6-acetyllysine (By similarity).
FT   CROSSLNK     14     14       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CONFLICT    163    163       T -> P (in Ref. 1; BAA24927).
SQ   SEQUENCE   200 AA;  22407 MW;  E40668099ED25828 CRC64;
     MANIAVQRIK REFKEVLKSE ETSKNQIKVD LVDENFTELR GEIAGPPDTP YEGGRYQLEI
     KIPETYPFNP PKVRFITKIW HPNISSVTGA ICLDILKDQW AAAMTLRTVL LSLQALLAAA
     EPDDPQDAVV ANQYKQNPEM FKQTARLWAH VYAGAPVSSP EYTKKIENLC AMGFDRNAVI
     VALSSKSWDV ETATELLLSN
//
ID   DRD2_MOUSE              Reviewed;         444 AA.
AC   P61168; P13953;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=D(2) dopamine receptor;
DE   AltName: Full=Dopamine D2 receptor;
GN   Name=Drd2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX   MEDLINE=91122293; PubMed=1991517; DOI=10.1016/0014-5793(91)80125-M;
RA   Montmayeur J.P., Bausero P., Amlaiky N., Maroteaux L., Hen R.,
RA   Borrelli E.;
RT   "Differential expression of the mouse D2 dopamine receptor isoforms.";
RL   FEBS Lett. 278:239-243(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=90136899; PubMed=2137198; DOI=10.1038/343266a0;
RA   Chio C.L., Hess G.F., Graham R.S., Huff R.M.;
RT   "A second molecular form of D2 dopamine receptor in rat and bovine
RT   caudate nucleus.";
RL   Nature 343:266-269(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 175-270 (ISOFORM 1).
RX   MEDLINE=90076122; PubMed=2531656;
RA   Dal-Toso R., Sommer B., Ewert M., Herb A., Pritchett D.B., Bach A.,
RA   Shivers B.D., Seeburg P.H.;
RT   "The dopamine D2 receptor: two molecular forms generated by
RT   alternative splicing.";
RL   EMBO J. 8:4025-4034(1989).
CC   -!- FUNCTION: This is one of the five types (D1 to D5) of receptors
CC       for dopamine. The activity of this receptor is mediated by G
CC       proteins which inhibit adenylyl cyclase.
CC   -!- SUBUNIT: Interacts with GPRASP1, PPP1R9B, CADPS, CADPS2 and CLIC6.
CC       Interacts with ARRB2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Long;
CC         IsoId=P61168-1, P13953-1;
CC         Sequence=Displayed;
CC       Name=2; Synonyms=Short;
CC         IsoId=P61168-2, P13953-2;
CC         Sequence=VSP_010241;
CC   -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in the
CC       pituitary and brain. Isoform 1 is expressed seven times more than
CC       isoform 2 in the caudate nucleus.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; X55674; CAA39209.1; -; mRNA.
DR   IPI; IPI00229964; -.
DR   IPI; IPI00469269; -.
DR   PIR; S13921; DYMSD2.
DR   UniGene; Mm.41970; -.
DR   ProteinModelPortal; P61168; -.
DR   SMR; P61168; 35-444.
DR   STRING; P61168; -.
DR   PhosphoSite; P61168; -.
DR   PRIDE; P61168; -.
DR   Ensembl; ENSMUST00000075764; ENSMUSP00000075170; ENSMUSG00000032259.
DR   Ensembl; ENSMUST00000114494; ENSMUSP00000110138; ENSMUSG00000032259.
DR   MGI; MGI:94924; Drd2.
DR   eggNOG; roNOG11562; -.
DR   GeneTree; ENSGT00600000084199; -.
DR   HOGENOM; HBG445348; -.
DR   HOVERGEN; HBG106962; -.
DR   InParanoid; P61168; -.
DR   OrthoDB; EOG4MW865; -.
DR   ArrayExpress; P61168; -.
DR   Bgee; P61168; -.
DR   CleanEx; MM_DRD2; -.
DR   Genevestigator; P61168; -.
DR   GermOnline; ENSMUSG00000032259; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0001670; F:dopamine D2 receptor activity; IDA:MGI.
DR   GO; GO:0060158; P:activation of phospholipase C activity by dopamine receptor signaling pathway; IDA:MGI.
DR   GO; GO:0021984; P:adenohypophysis development; IMP:MGI.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR   GO; GO:0048148; P:behavioral response to cocaine; IMP:MGI.
DR   GO; GO:0048149; P:behavioral response to ethanol; IMP:MGI.
DR   GO; GO:0048755; P:branching morphogenesis of a nerve; IMP:MGI.
DR   GO; GO:0021853; P:cerebral cortex GABAergic interneuron migration; IMP:MGI.
DR   GO; GO:0032922; P:circadian regulation of gene expression; IMP:MGI.
DR   GO; GO:0030146; P:diuresis; IMP:MGI.
DR   GO; GO:0042417; P:dopamine metabolic process; IMP:MGI.
DR   GO; GO:0007631; P:feeding behavior; IGI:MGI.
DR   GO; GO:0007625; P:grooming behavior; IMP:MGI.
DR   GO; GO:0007195; P:inhibition of adenylate cyclase activity by dopamine receptor signaling pathway; IDA:MGI.
DR   GO; GO:0030147; P:natriuresis; IMP:MGI.
DR   GO; GO:0045776; P:negative regulation of blood pressure; IMP:MGI.
DR   GO; GO:0030336; P:negative regulation of cell migration; IMP:MGI.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0060160; P:negative regulation of dopamine receptor signaling pathway; IMP:MGI.
DR   GO; GO:0051898; P:negative regulation of protein kinase B signaling cascade; IMP:MGI.
DR   GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IMP:MGI.
DR   GO; GO:0001976; P:neurological system process involved in regulation of systemic arterial blood pressure; IMP:MGI.
DR   GO; GO:0030432; P:peristalsis; IMP:MGI.
DR   GO; GO:0043473; P:pigmentation; IMP:MGI.
DR   GO; GO:0051586; P:positive regulation of dopamine uptake; IMP:MGI.
DR   GO; GO:0060124; P:positive regulation of growth hormone secretion; IMP:MGI.
DR   GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
DR   GO; GO:0002052; P:positive regulation of neuroblast proliferation; IDA:MGI.
DR   GO; GO:0060134; P:prepulse inhibition; IMP:MGI.
DR   GO; GO:0008104; P:protein localization; IMP:MGI.
DR   GO; GO:0014059; P:regulation of dopamine secretion; IMP:MGI.
DR   GO; GO:0002027; P:regulation of heart rate; IMP:MGI.
DR   GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:MGI.
DR   GO; GO:0043266; P:regulation of potassium ion transport; IMP:MGI.
DR   GO; GO:0002028; P:regulation of sodium ion transport; IMP:MGI.
DR   GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IMP:MGI.
DR   GO; GO:0001975; P:response to amphetamine; IMP:MGI.
DR   GO; GO:0042493; P:response to drug; IDA:MGI.
DR   GO; GO:0043278; P:response to morphine; IMP:MGI.
DR   GO; GO:0007608; P:sensory perception of smell; IMP:MGI.
DR   GO; GO:0001659; P:temperature homeostasis; IMP:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR001922; Dopa_D2_rcpt.
DR   InterPro; IPR000929; Dopamine_rcpt.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00567; DOPAMINED2R.
DR   PRINTS; PR00242; DOPAMINER.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW   Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN         1    444       D(2) dopamine receptor.
FT                                /FTId=PRO_0000069388.
FT   TOPO_DOM      1     37       Extracellular (Potential).
FT   TRANSMEM     38     60       Helical; Name=1; (Potential).
FT   TOPO_DOM     61     71       Cytoplasmic (Potential).
FT   TRANSMEM     72     97       Helical; Name=2; (Potential).
FT   TOPO_DOM     98    108       Extracellular (Potential).
FT   TRANSMEM    109    130       Helical; Name=3; (Potential).
FT   TOPO_DOM    131    151       Cytoplasmic (Potential).
FT   TRANSMEM    152    174       Helical; Name=4; (Potential).
FT   TOPO_DOM    175    186       Extracellular (Potential).
FT   TRANSMEM    187    210       Helical; Name=5; (Potential).
FT   TOPO_DOM    211    374       Cytoplasmic (Potential).
FT   TRANSMEM    375    398       Helical; Name=6; (Potential).
FT   TOPO_DOM    399    406       Extracellular (Potential).
FT   TRANSMEM    407    430       Helical; Name=7; (Potential).
FT   TOPO_DOM    431    444       Cytoplasmic (Potential).
FT   REGION      211    374       Interaction with PPP1R9B (By similarity).
FT   SITE        193    193       Implicated in catechol agonist binding.
FT   SITE        194    194       Implicated in receptor activation.
FT   SITE        197    197       Implicated in receptor activation.
FT   CARBOHYD      5      5       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     17     17       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     23     23       N-linked (GlcNAc...) (Potential).
FT   DISULFID    107    182       By similarity.
FT   VAR_SEQ     242    270       Missing (in isoform 2).
FT                                /FTId=VSP_010241.
SQ   SEQUENCE   444 AA;  50904 MW;  216E56CEE5CA32FB CRC64;
     MDPLNLSWYD DDLERQNWSR PFNGSEGKAD RPHYNYYAML LTLLIFIIVF GNVLVCMAVS
     REKALQTTTN YLIVSLAVAD LLVATLVMPW VVYLEVVGEW KFSRIHCDIF VTLDVMMCTA
     SILNLCAISI DRYTAVAMPM LYNTRYSSKR RVTVMIAIVW VLSFTISCPL LFGLNNTDQN
     ECIIANPAFV VYSSIVSFYV PFIVTLLVYI KIYIVLRKRR KRVNTKRSSR AFRANLKTPL
     KGNCTHPEDM KLCTVIMKSN GSFPVNRRRM DAARRAQELE MEMLSSTSPP ERTRYSPIPP
     SHHQLTLPDP SHHGLHSNPD SPAKPEKNGH AKIVNPRIAK FFEIQTMPNG KTRTSLKTMS
     RRKLSQQKEK KATQMLAIVL GVFIICWLPF FITHILNIHC DCNIPPVLYS AFTWLGYVNS
     AVNPIIYTTF NIEFRKAFMK ILHC
//
ID   RAP2B_MOUSE             Reviewed;         183 AA.
AC   P61226; P17964; Q96EG5; Q9CXG0;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Ras-related protein Rap-2b;
DE   Flags: Precursor;
GN   Name=Rap2b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Cerebellum, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 6-16; 43-68 AND 151-162, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   INTERACTION WITH RUNDC3A, AND DOMAIN.
RX   PubMed=9523700; DOI=10.1046/j.1432-1327.1998.2520290.x;
RA   Janoueix-Lerosey I., Pasheva E., de Tand M.-F., Tavitian A.,
RA   de Gunzburg J.;
RT   "Identification of a specific effector of the small GTP-binding
RT   protein Rap2.";
RL   Eur. J. Biochem. 252:290-298(1998).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, PALMITOYLATION, AND MUTAGENESIS OF
RP   CYS-176; CYS-177 AND CYS-180.
RX   PubMed=19061864; DOI=10.1016/j.bbrc.2008.11.107;
RA   Uechi Y., Bayarjargal M., Umikawa M., Oshiro M., Takei K.,
RA   Yamashiro Y., Asato T., Endo S., Misaki R., Taguchi T., Kariya K.;
RT   "Rap2 function requires palmitoylation and recycling endosome
RT   localization.";
RL   Biochem. Biophys. Res. Commun. 378:732-737(2009).
CC   -!- FUNCTION: Small GTP-binding protein which cycles between a GDP-
CC       bound inactive and a GTP-bound active form. Involved in EGFR and
CC       CHRM3 signaling pathways through stimulation of PLCE1. May play a
CC       role in cytoskeletal rearrangements and regulate cell spreading
CC       through activation of the effector TNIK. May regulate membrane
CC       vesiculation in red blood cells.
CC   -!- SUBUNIT: Interacts with PLCE1. Interacts with SGSM1, SGSM2 and
CC       SGSM3 (By similarity). The GTP-bound form of RAP2B interacts with
CC       RUNDC3A.
CC   -!- SUBCELLULAR LOCATION: Recycling endosome membrane; Lipid-anchor;
CC       Cytoplasmic side. Note=Associated with red blood cells-released
CC       vesicles (By similarity).
CC   -!- DOMAIN: The effector domain mediates the interaction with RUNDC3A.
CC   -!- PTM: Palmitoylated. Palmitoylation is required for association
CC       with recycling endosome membranes and activation of TNIK.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK014462; BAB29368.1; -; mRNA.
DR   EMBL; BC032168; AAH32168.1; -; mRNA.
DR   EMBL; BC046528; AAH46528.1; -; mRNA.
DR   IPI; IPI00138716; -.
DR   RefSeq; NP_082988.1; NM_028712.4.
DR   UniGene; Mm.422674; -.
DR   UniGene; Mm.477648; -.
DR   ProteinModelPortal; P61226; -.
DR   SMR; P61226; 1-167.
DR   PRIDE; P61226; -.
DR   Ensembl; ENSMUST00000049064; ENSMUSP00000038841; ENSMUSG00000036894.
DR   GeneID; 74012; -.
DR   KEGG; mmu:74012; -.
DR   UCSC; uc008pjl.1; mouse.
DR   CTD; 74012; -.
DR   MGI; MGI:1921262; Rap2b.
DR   eggNOG; roNOG15845; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; P61226; -.
DR   OMA; ASQPNGD; -.
DR   OrthoDB; EOG4P2Q3G; -.
DR   PhylomeDB; P61226; -.
DR   NextBio; 339528; -.
DR   ArrayExpress; P61226; -.
DR   Bgee; P61226; -.
DR   CleanEx; MM_RAP2B; -.
DR   Genevestigator; P61226; -.
DR   GermOnline; ENSMUSG00000036894; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR   GO; GO:0030336; P:negative regulation of cell migration; IDA:MGI.
DR   GO; GO:0031954; P:positive regulation of protein autophosphorylation; IDA:MGI.
DR   GO; GO:0032486; P:Rap protein signal transduction; IDA:UniProtKB.
DR   GO; GO:0061097; P:regulation of protein tyrosine kinase activity; IDA:UniProtKB.
DR   InterPro; IPR003577; GTPase_Ras.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR020849; Ras_small_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00173; RAS; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endosome; GTP-binding; Lipoprotein;
KW   Membrane; Methylation; Nucleotide-binding; Palmitate; Prenylation.
FT   CHAIN         1    180       Ras-related protein Rap-2b.
FT                                /FTId=PRO_0000030217.
FT   PROPEP      181    183       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000030218.
FT   NP_BIND      10     17       GTP (By similarity).
FT   NP_BIND      57     61       GTP (By similarity).
FT   NP_BIND     116    119       GTP (By similarity).
FT   MOTIF        32     40       Effector region (Probable).
FT   MOD_RES     180    180       Cysteine methyl ester (By similarity).
FT   LIPID       180    180       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   MUTAGEN     176    176       C->G: Reduced association with the
FT                                recycling endosome membranes and loss of
FT                                TNIK activation; when associated with G-
FT                                177.
FT   MUTAGEN     177    177       C->G: Reduced association with the
FT                                recycling endosome membranes and loss of
FT                                TNIK activation; when associated with G-
FT                                176.
FT   MUTAGEN     180    180       C->A: Loss of association with membranes.
SQ   SEQUENCE   183 AA;  20504 MW;  A1139C2D5E7F5865 CRC64;
     MREYKVVVLG SGGVGKSALT VQFVTGSFIE KYDPTIEDFY RKEIEVDSSP SVLEILDTAG
     TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI IRVKRYERVP MILVGNKVDL
     EGEREVSYGE GKALAEEWSC PFMETSAKNK ASVDELFAEI VRQMNYAAQP NGDEGCCSAC
     VIL
//
ID   STX1B_MOUSE             Reviewed;         288 AA.
AC   P61264; A2RSB4; O35525; P32853;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Syntaxin-1B;
GN   Name=Stx1b; Synonyms=Stx1b1, Stx1b2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Fujiwara T., Genda M., Nagai A., Okazaki M., Watanabe T.,
RA   Nagamatsu S., Akagawa K.;
RT   "Cloning and sequence analysis of the various species HPC-1/syntaxin
RT   cDNA.";
RL   Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR;
RA   Horikawa H.P.;
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 10-40; 46-69; 94-107; 125-139; 151-181; 189-197
RP   AND 232-245, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   INTERACTION WITH OTOF.
RC   STRAIN=BALB/c; TISSUE=Cochlea;
RX   PubMed=17055430; DOI=10.1016/j.cell.2006.08.040;
RA   Roux I., Safieddine S., Nouvian R., Grati M., Simmler M.-C.,
RA   Bahloul A., Perfettini I., Le Gall M., Rostaing P., Hamard G.,
RA   Triller A., Avan P., Moser T., Petit C.;
RT   "Otoferlin, defective in a human deafness form, is essential for
RT   exocytosis at the auditory ribbon synapse.";
RL   Cell 127:277-289(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15648052; DOI=10.1002/pmic.200401066;
RA   Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA   Hart G.W., Burlingame A.L.;
RT   "Quantitative analysis of both protein expression and serine /
RT   threonine post-translational modifications through stable isotope
RT   labeling with dithiothreitol.";
RL   Proteomics 5:388-398(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-58 AND THR-160,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Potentially involved in docking of synaptic vesicles at
CC       presynaptic active zones (By similarity).
CC   -!- SUBUNIT: Interacts with OTOF.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane
CC       protein (Potential).
CC   -!- PTM: Phosphorylated by CK2 (By similarity).
CC   -!- SIMILARITY: Belongs to the syntaxin family.
CC   -!- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; D45207; BAA25986.1; -; mRNA.
DR   EMBL; D29743; BAA06162.1; -; mRNA.
DR   EMBL; AC149222; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC132042; AAI32043.1; -; mRNA.
DR   EMBL; BC132068; AAI32069.1; -; mRNA.
DR   IPI; IPI00113149; -.
DR   RefSeq; NP_077725.1; NM_024414.2.
DR   UniGene; Mm.439759; -.
DR   ProteinModelPortal; P61264; -.
DR   SMR; P61264; 2-284.
DR   STRING; P61264; -.
DR   PhosphoSite; P61264; -.
DR   PRIDE; P61264; -.
DR   Ensembl; ENSMUST00000106267; ENSMUSP00000101874; ENSMUSG00000030806.
DR   GeneID; 56216; -.
DR   KEGG; mmu:56216; -.
DR   UCSC; uc009jwx.1; mouse.
DR   CTD; 56216; -.
DR   MGI; MGI:1930705; Stx1b.
DR   eggNOG; roNOG14013; -.
DR   GeneTree; ENSGT00550000074334; -.
DR   HOGENOM; HBG717663; -.
DR   HOVERGEN; HBG000497; -.
DR   InParanoid; P61264; -.
DR   OMA; EEVVQVD; -.
DR   OrthoDB; EOG4PC9SV; -.
DR   PhylomeDB; P61264; -.
DR   NextBio; 312076; -.
DR   ArrayExpress; P61264; -.
DR   Bgee; P61264; -.
DR   Genevestigator; P61264; -.
DR   GermOnline; ENSMUSG00000030806; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR   GO; GO:0007268; P:synaptic transmission; IEA:InterPro.
DR   InterPro; IPR015709; Syntaxin-1.
DR   InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR   InterPro; IPR006011; Syntaxin_N.
DR   InterPro; IPR010989; t-SNARE.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR19957:SF35; Syntaxin-1; 1.
DR   Pfam; PF05739; SNARE; 1.
DR   Pfam; PF00804; Syntaxin; 1.
DR   SMART; SM00503; SynN; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF47661; t-snare; 1.
DR   PROSITE; PS00914; SYNTAXIN; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Direct protein sequencing; Membrane;
KW   Neurotransmitter transport; Phosphoprotein; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    288       Syntaxin-1B.
FT                                /FTId=PRO_0000210193.
FT   TOPO_DOM      1    264       Cytoplasmic (Potential).
FT   TRANSMEM    265    288       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   DOMAIN      191    253       t-SNARE coiled-coil homology.
FT   COILED       29    104       Potential.
FT   MOD_RES      14     14       Phosphoserine.
FT   MOD_RES      58     58       Phosphoserine.
FT   MOD_RES     160    160       Phosphothreonine.
FT   CONFLICT      3      4       DR -> EW (in Ref. 1; BAA25986).
FT   CONFLICT      8      8       L -> R (in Ref. 1; BAA25986).
FT   CONFLICT     26     26       D -> A (in Ref. 1; BAA25986).
FT   CONFLICT     30     30       D -> A (in Ref. 1; BAA25986).
FT   CONFLICT     51     55       EQVKK -> GRVGG (in Ref. 1; BAA25986).
FT   CONFLICT     65     65       N -> K (in Ref. 1; BAA25986).
FT   CONFLICT     98     98       S -> G (in Ref. 1; BAA25986).
FT   CONFLICT    114    116       IRK -> YRT (in Ref. 1; BAA25986).
FT   CONFLICT    122    122       L -> V (in Ref. 1; BAA25986).
FT   CONFLICT    125    125       K -> N (in Ref. 1; BAA25986).
FT   CONFLICT    137    137       Q -> K (in Ref. 1; BAA25986).
FT   CONFLICT    148    148       I -> L (in Ref. 1; BAA25986).
FT   CONFLICT    191    191       L -> R (in Ref. 1; BAA25986).
SQ   SEQUENCE   288 AA;  33245 MW;  2733497E02978BEB CRC64;
     MKDRTQELRS AKDSDDEEEV VHVDRDHFMD EFFEQVEEIR GCIEKLSEDV EQVKKQHSAI
     LAAPNPDEKT KQELEDLTAD IKKTANKVRS KLKAIEQSIE QEEGLNRSSA DLRIRKTQHS
     TLSRKFVEVM TEYNATQSKY RDRCKDRIQR QLEITGRTTT NEELEDMLES GKLAIFTDDI
     KMDSQMTKQA LNEIETRHNE IIKLETSIRE LHDMFVDMAM LVESQGEMID RIEYNVEHSV
     DYVERAVSDT KKAVKYQSKA RRKKIMIIIC CVVLGVVLAS SIGGTLGL
//
ID   RAB6B_MOUSE             Reviewed;         208 AA.
AC   P61294;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Ras-related protein Rab-6B;
GN   Name=Rab6b; Synonyms=D9Bwg0185e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH CCDC64.
RX   PubMed=20360680; DOI=10.1038/emboj.2010.51;
RA   Schlager M.A., Kapitein L.C., Grigoriev I., Burzynski G.M., Wulf P.S.,
RA   Keijzer N., de Graaff E., Fukuda M., Shepherd I.T., Akhmanova A.,
RA   Hoogenraad C.C.;
RT   "Pericentrosomal targeting of Rab6 secretory vesicles by Bicaudal-D-
RT   related protein 1 (BICDR-1) regulates neuritogenesis.";
RL   EMBO J. 29:1637-1651(2010).
CC   -!- FUNCTION: Seems to have a role in retrograde membrane traffic at
CC       the level of the Golgi complex. May function in retrograde
CC       transport in neuronal cells (By similarity).
CC   -!- SUBUNIT: Interacts with RAB6KIFL. Interacts (GTP-bound) with BICD1
CC       (via C-terminus); the interaction is direct. Interacts (GDP-bound)
CC       with DYNLRB1 (By similarity). Interacts with CCDC64/BICDR1; leads
CC       to its accumulation in the pericentrosomal region.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Lipid-anchor (By
CC       similarity). Cytoplasmic vesicle (By similarity). Note=Colocalizes
CC       with BICD1 at vesicular structures that align along microtubules
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR   EMBL; AK035893; BAC29230.1; -; mRNA.
DR   EMBL; BC060618; AAH60618.1; -; mRNA.
DR   IPI; IPI00378145; -.
DR   RefSeq; NP_776142.1; NM_173781.4.
DR   UniGene; Mm.479869; -.
DR   ProteinModelPortal; P61294; -.
DR   SMR; P61294; 13-174.
DR   STRING; P61294; -.
DR   PRIDE; P61294; -.
DR   Ensembl; ENSMUST00000035155; ENSMUSP00000035155; ENSMUSG00000032549.
DR   GeneID; 270192; -.
DR   KEGG; mmu:270192; -.
DR   UCSC; uc009rgf.1; mouse.
DR   CTD; 270192; -.
DR   MGI; MGI:107283; Rab6b.
DR   eggNOG; roNOG11398; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; P61294; -.
DR   OMA; ETSKEGM; -.
DR   OrthoDB; EOG4NP74D; -.
DR   PhylomeDB; P61294; -.
DR   NextBio; 393297; -.
DR   ArrayExpress; P61294; -.
DR   Bgee; P61294; -.
DR   CleanEx; MM_RAB6B; -.
DR   Genevestigator; P61294; -.
DR   GermOnline; ENSMUSG00000032549; Mus musculus.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus; GTP-binding;
KW   Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation;
KW   Protein transport; Transport.
FT   CHAIN         1    208       Ras-related protein Rab-6B.
FT                                /FTId=PRO_0000121116.
FT   NP_BIND      20     27       GTP (By similarity).
FT   NP_BIND      68     72       GTP (By similarity).
FT   NP_BIND     126    129       GTP (By similarity).
FT   MOTIF        42     50       Effector region (By similarity).
FT   BINDING      45     45       GTP (By similarity).
FT   MOD_RES     208    208       Cysteine methyl ester (By similarity).
FT   LIPID       206    206       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   LIPID       208    208       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   208 AA;  23462 MW;  E81C831996E2446D CRC64;
     MSAGGDFGNP LRKFKLVFLG EQSVGKTSLI TRFMYDSFDN TYQATIGIDF LSKTMYLEDR
     TVRLQLWDTA GQERFRSLIP SYIRDSTVAV VVYDITNLNS FQQTSKWIDD VRTERGSDVI
     IMLVGNKTDL ADKRQITIEE GEQRAKELSV MFIETSAKTG YNVKQLFRRV ASALPGMENV
     QEKSKEGMID IKLDKPQEPP ASEGGCSC
//
ID   FGF12_MOUSE             Reviewed;         243 AA.
AC   P61329; O35339; P70376; Q924B4; Q92912; Q93001;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Fibroblast growth factor 12;
DE            Short=FGF-12;
DE   AltName: Full=Fibroblast growth factor homologous factor 1;
DE            Short=FHF-1;
DE   AltName: Full=Myocyte-activating factor;
GN   Name=Fgf12; Synonyms=Fhf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Retina;
RX   MEDLINE=96382556; PubMed=8790420; DOI=10.1073/pnas.93.18.9850;
RA   Smallwood P.M., Munoz-Sanjuan I., Tong P., Macke J.P., Hendry S.H.,
RA   Gilbert D.J., Copeland N.G., Jenkins N.A., Nathans J.;
RT   "Fibroblast growth factor (FGF) homologous factors: new members of the
RT   FGF family implicated in nervous system development.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:9850-9857(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=97376484; PubMed=9232594; DOI=10.1016/S0925-4773(97)00042-7;
RA   Hartung H., Feldman B., Lovec H., Coulier F., Birnbaum D.,
RA   Goldfarb M.;
RT   "Murine FGF-12 and FGF-13: expression in embryonic nervous system,
RT   connective tissue and heart.";
RL   Mech. Dev. 64:31-39(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Probably involved in nervous system development and
CC       function.
CC   -!- SUBUNIT: Interacts with the C-terminal region of SCN9A (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P61329-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P61329-2; Sequence=VSP_010223;
CC   -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U66201; AAB18917.1; -; mRNA.
DR   EMBL; AF020738; AAB71607.1; -; mRNA.
DR   EMBL; AK034335; BAC28679.1; -; mRNA.
DR   EMBL; BC030485; AAH30485.1; -; mRNA.
DR   IPI; IPI00130399; -.
DR   IPI; IPI00338412; -.
DR   RefSeq; NP_034329.1; NM_010199.2.
DR   RefSeq; NP_898887.1; NM_183064.3.
DR   UniGene; Mm.7996; -.
DR   ProteinModelPortal; P61329; -.
DR   SMR; P61329; 68-205.
DR   STRING; P61329; -.
DR   PhosphoSite; P61329; -.
DR   PRIDE; P61329; -.
DR   Ensembl; ENSMUST00000100024; ENSMUSP00000097601; ENSMUSG00000022523.
DR   GeneID; 14167; -.
DR   KEGG; mmu:14167; -.
DR   UCSC; uc007yvr.1; mouse.
DR   UCSC; uc007yvt.1; mouse.
DR   CTD; 14167; -.
DR   MGI; MGI:109183; Fgf12.
DR   GeneTree; ENSGT00590000082822; -.
DR   HOGENOM; HBG715432; -.
DR   HOVERGEN; HBG007580; -.
DR   InParanoid; P61329; -.
DR   OMA; QEYFLQM; -.
DR   OrthoDB; EOG4G7C03; -.
DR   PhylomeDB; P61329; -.
DR   NextBio; 285314; -.
DR   ArrayExpress; P61329; -.
DR   Bgee; P61329; -.
DR   CleanEx; MM_FGF12; -.
DR   Genevestigator; P61329; -.
DR   GermOnline; ENSMUSG00000022523; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR008996; Cytokine_IL1-like.
DR   InterPro; IPR002209; GF_heparin-bd.
DR   InterPro; IPR002348; IL1_HBGF.
DR   PANTHER; PTHR11486; IL1_HBGF; 1.
DR   Pfam; PF00167; FGF; 1.
DR   PRINTS; PR00263; HBGFFGF.
DR   PRINTS; PR00262; IL1HBGF.
DR   SMART; SM00442; FGF; 1.
DR   SUPFAM; SSF50353; Cytok_IL1_like; 1.
DR   PROSITE; PS00247; HBGF_FGF; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Growth factor; Nucleus.
FT   CHAIN         1    243       Fibroblast growth factor 12.
FT                                /FTId=PRO_0000147605.
FT   MOTIF        11     38       Bipartite nuclear localization signal
FT                                (Potential).
FT   VAR_SEQ       1     66       MAAAIASSLIRQKRQARESNSDRVSASKRRSSPSKDGRSLC
FT                                ERHVLGVFSKVRFCSGRKRPVRRRP -> MESK (in
FT                                isoform 2).
FT                                /FTId=VSP_010223.
FT   CONFLICT     42     42       E -> D (in Ref. 2; AAB71607).
FT   CONFLICT    182    182       Q -> P (in Ref. 2; AAB71607).
SQ   SEQUENCE   243 AA;  27399 MW;  773ED10B5BDD033C CRC64;
     MAAAIASSLI RQKRQARESN SDRVSASKRR SSPSKDGRSL CERHVLGVFS KVRFCSGRKR
     PVRRRPEPQL KGIVTRLFSQ QGYFLQMHPD GTIDGTKDEN SDYTLFNLIP VGLRVVAIQG
     VKASLYVAMN GEGYLYSSDV FTPECKFKES VFENYYVIYS STLYRQQESG RAWFLGLNKE
     GQIMKGNRVK KTKPSSHFVP KPIEVCMYRE PSLHEIGEKQ GRSRKSSGTP TMNGGKVVNQ
     DST
//
ID   EST1A_MOUSE             Reviewed;        1418 AA.
AC   P61406; Q5NC64;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Telomerase-binding protein EST1A;
DE            EC=3.1.-.-;
DE   AltName: Full=EST1-like protein A;
DE   AltName: Full=Ever shorter telomeres 1A;
DE   AltName: Full=Smg-6 homolog;
DE   AltName: Full=Telomerase subunit EST1A;
GN   Name=Smg6; Synonyms=Est1a, Kiaa0732;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 447-1418.
RC   TISSUE=Fetal brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
CC   -!- FUNCTION: Component of the telomerase ribonucleoprotein (RNP)
CC       complex that is essential for the replication of chromosome
CC       termini. May have a general role in telomere regulation. Promotes
CC       in vitro the ability of TERT to elongate telomeres. Overexpression
CC       induces telomere uncapping, chromosomal end-to-end fusions
CC       (telomeric DNA persists at the fusion points) and did not perturb
CC       TRF2 telomeric localization. Dephosphorylates RENT1. Plays a role
CC       in nonsense-mediated mRNA decay. May function as endonuclease.
CC       Degrades single-stranded RNA (ssRNA), but not ssDNA or dsRNA (By
CC       similarity).
CC   -!- COFACTOR: Manganese (By similarity).
CC   -!- SUBUNIT: Component of the telomerase holoenzyme complex at least
CC       composed of TERT, DKC1, WRAP53/TCAB1, NOP10, NHP2, GAR1, TEP1,
CC       EST1A, POT1 and a telomerase RNA template component (TERC).
CC       Interacts with TERT, independently of the telomerase RNA. Binds to
CC       the single-stranded 5'-(GTGTGG)(4)GTGT-3' telomeric DNA, but not
CC       to a telomerase RNA template component (TER). Interacts with PP2A
CC       catalytic subunits, SMG1, UPF1, UPF2 and UPF3B (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity).
CC       Chromosome, telomere (Probable). Note=Particularly enriched in the
CC       nucleolus (By similarity).
CC   -----------------------------------------------------------------------
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DR   EMBL; AL604066; CAI24256.1; -; Genomic_DNA.
DR   EMBL; AL603905; CAI24256.1; JOINED; Genomic_DNA.
DR   EMBL; AL662892; CAI24256.1; JOINED; Genomic_DNA.
DR   EMBL; AL603905; CAI35093.1; -; Genomic_DNA.
DR   EMBL; AL604066; CAI35093.1; JOINED; Genomic_DNA.
DR   EMBL; AL662892; CAI35093.1; JOINED; Genomic_DNA.
DR   EMBL; AL662892; CAI35928.1; -; Genomic_DNA.
DR   EMBL; AL603905; CAI35928.1; JOINED; Genomic_DNA.
DR   EMBL; AL604066; CAI35928.1; JOINED; Genomic_DNA.
DR   EMBL; BC066040; AAH66040.1; -; mRNA.
DR   EMBL; AK129203; BAC98013.1; -; mRNA.
DR   IPI; IPI00417158; -.
DR   RefSeq; NP_001002764.1; NM_001002764.1.
DR   UniGene; Mm.288460; -.
DR   ProteinModelPortal; P61406; -.
DR   SMR; P61406; 1238-1416.
DR   STRING; P61406; -.
DR   PhosphoSite; P61406; -.
DR   PRIDE; P61406; -.
DR   Ensembl; ENSMUST00000045281; ENSMUSP00000043555; ENSMUSG00000038290.
DR   GeneID; 103677; -.
DR   KEGG; mmu:103677; -.
DR   UCSC; uc007kcz.1; mouse.
DR   CTD; 103677; -.
DR   MGI; MGI:2144117; Smg6.
DR   GeneTree; ENSGT00560000077120; -.
DR   HOGENOM; HBG715896; -.
DR   HOVERGEN; HBG051511; -.
DR   InParanoid; P61406; -.
DR   OMA; ESTPLGP; -.
DR   OrthoDB; EOG4KKZ29; -.
DR   PhylomeDB; P61406; -.
DR   NextBio; 356057; -.
DR   ArrayExpress; P61406; -.
DR   Bgee; P61406; -.
DR   Genevestigator; P61406; -.
DR   GermOnline; ENSMUSG00000038290; Mus musculus.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; ISS:HGNC.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042162; F:telomeric DNA binding; ISS:HGNC.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR   GO; GO:0000723; P:telomere maintenance; ISS:HGNC.
DR   InterPro; IPR019458; EST1.
DR   InterPro; IPR006596; PINc_nuc-bd.
DR   InterPro; IPR011990; TPR-like_helical.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
DR   Pfam; PF10374; EST1; 1.
DR   SMART; SM00670; PINc; 1.
PE   2: Evidence at transcript level;
KW   Chromosome; Coiled coil; DNA-binding; Endonuclease; Hydrolase;
KW   Manganese; Metal-binding; Nonsense-mediated mRNA decay; Nuclease;
KW   Nucleus; Phosphoprotein; Telomere.
FT   CHAIN         1   1418       Telomerase-binding protein EST1A.
FT                                /FTId=PRO_0000087070.
FT   COILED      566    600       Potential.
FT   COILED     1196   1243       Potential.
FT   METAL      1250   1250       Manganese; catalytic (Potential).
FT   METAL      1352   1352       Manganese; catalytic (Potential).
FT   METAL      1391   1391       Manganese; catalytic (Potential).
FT   MOD_RES     478    478       Phosphothreonine (By similarity).
SQ   SEQUENCE   1418 AA;  160496 MW;  DC48C12B38C6EB8A CRC64;
     MAEGLERVRI SASELRGILA TLAPQAGSRE NMKELKEPRQ RKDNRRPDLE IYKPGLSRLR
     NRPKTKEASG NEEFKDEIVN DRDSSAVGND TQLIQVCKEL DSQQQNGPID AENSQAQETF
     PKTVGLEDRS LKIIKRSKKP DLQIYQPGRR LQTITKESAG RADEEEILNQ VEQLRIEEDE
     CKGEAIKEEV NNKPDKTEIE KHQSNDRVRT AKGEKGKKIE KGEGSKKVAD DSVPGKPGSV
     KRYSRSDKRR NRYRTCSTSS AGSNNSAEGA GLTDNGCRRR RQDRAKERPR LKKQVSLSST
     DSLDEDRVDE PDVLGSRRSS ERKKHLERNW SGCGEGEQKS NGKENRSALR VTFDAETMSK
     DSPVVRSVKD NVDRMKSDKG PSSGGKGSEK QELRHPRQEL RDRGRGILIL PAHTALSVSS
     SGSPESTPLG PRLLFGSGSK GSRSWGRGGT TRRLWDPNNP DQKPALKSQT PQLHFLDTDD
     EISPTSWGDS RQAQASYYKF QNSDNPYYYP RTPGPASQYP YAGYSPLQYP VGPTNGMYPG
     AYYPGYPAPS GQYVCSPLPA STMSPEEIEQ HVRNMQQQEL HRLLRVADNQ ELQLSNLLSR
     DRISTEGMEK MAQLRTELLQ LYERCILLDI EFSDSQNVDQ ILWKNAFYQV IEKFRQLLKD
     PNSENPEQIR NRLLELLDEG SDFFDSLLQK LQVTYKFKLE DYMDGLAIRS KPLRKTVKYA
     LISAQRSMIC QGDISRYREQ ANDTANYGKA RSWYLKAQHI APKNGRPYNQ LALLAVYTRR
     KLDAVYYYMR SLAASNPILT AKESLMSLFE ETKRKAEQME KKQHEEFDMS PDKWRKGKKS
     TFRHVGDDTT RLEIWIHPSH SRSAQGTESG KDSEQENGLG SLSPSDLNKR FILSFLHAHG
     KLFTRIGMET FPAVAEKVLK EFQVLLQHSP SPIGSTRMLQ LMTINMFAVH NSQLKDCFSE
     ECRSVIQEQA ASLGLAMFSL LVQRCTCLLK DSAKAQLSSP EDQEDQDDIK VSSFVPDLKE
     LLPSVKVWSD WMLGYPDTWN PPPTSLDLPL QVAVDVWSTL ADFCNILTAV NQSEVPLYKD
     PDDDLTLLIL EEDRLLSGFV PLLAAPQDPC YVEKTSDKVI AADCKRVTVL KYFLEALCGQ
     EEPLLAFKGG KYVSVAPVPD TMGKEMGSQE GKQLEDEEED VVIEDFEEDS EAEGSGGEDD
     IRELRAKKLA LARKIAEQQR RQEKIQAVLE DQSQMRQMEL EIRPLFLVPD TNGFIDHLAS
     LARLLESRKY ILVVPLIVIN ELDGLAKGQE TDHRAGGYAR VVQEKARKSI EFLERRFESR
     DSCLRALTSR GNELESIAFR SEDITGQLGN NDDLILSCCL HYCKDKAKDY MPTSKEEPIR
     LLREVVLLTD DRNLRVKALT RNVPVRDIPA FLTWAQVG
//
ID   ARF4_MOUSE              Reviewed;         180 AA.
AC   P61750; P36403; Q3TGC2; Q9CXX3;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=ADP-ribosylation factor 4;
GN   Name=Arf4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=97103475; PubMed=8947846;
RA   Hosaka M., Toda K., Takatsu H., Torii S., Murakami K., Nakayama K.;
RT   "Structure and intracellular localization of mouse ADP-ribosylation
RT   factors type 1 to type 6 (ARF1-ARF6).";
RL   J. Biochem. 120:813-819(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Head, and Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: GTP-binding protein that functions as an allosteric
CC       activator of the cholera toxin catalytic subunit, an ADP-
CC       ribosyltransferase. Involved in protein trafficking; may modulate
CC       vesicle budding and uncoating within the Golgi apparatus.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
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DR   EMBL; D87901; BAA13493.1; -; mRNA.
DR   EMBL; AK013892; BAB29041.1; -; mRNA.
DR   EMBL; AK081686; BAC38292.1; -; mRNA.
DR   EMBL; AK153011; BAE31650.1; -; mRNA.
DR   EMBL; AK168793; BAE40626.1; -; mRNA.
DR   IPI; IPI00331663; -.
DR   PIR; JC4948; JC4948.
DR   RefSeq; NP_031505.1; NM_007479.3.
DR   UniGene; Mm.297768; -.
DR   ProteinModelPortal; P61750; -.
DR   SMR; P61750; 4-178.
DR   STRING; P61750; -.
DR   PhosphoSite; P61750; -.
DR   PRIDE; P61750; -.
DR   Ensembl; ENSMUST00000022429; ENSMUSP00000022429; ENSMUSG00000021877.
DR   GeneID; 11843; -.
DR   KEGG; mmu:11843; -.
DR   UCSC; uc007sta.1; mouse.
DR   CTD; 11843; -.
DR   MGI; MGI:99433; Arf4.
DR   eggNOG; roNOG11428; -.
DR   HOVERGEN; HBG002073; -.
DR   OMA; GADELQK; -.
DR   PhylomeDB; P61750; -.
DR   NextBio; 279795; -.
DR   ArrayExpress; P61750; -.
DR   Bgee; P61750; -.
DR   CleanEx; MM_ARF4; -.
DR   Genevestigator; P61750; -.
DR   GermOnline; ENSMUSG00000021877; Mus musculus.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; TAS:MGI.
DR   GO; GO:0015031; P:protein transport; TAS:MGI.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   InterPro; IPR006688; ARF.
DR   InterPro; IPR006689; ARF/SAR.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   PANTHER; PTHR11711; ARF/SAR; 1.
DR   Pfam; PF00025; Arf; 1.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00177; ARF; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51417; ARF; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ER-Golgi transport; Golgi apparatus; GTP-binding;
KW   Lipoprotein; Myristate; Nucleotide-binding; Protein transport;
KW   Transport.
FT   INIT_MET      1      1       Removed (Potential).
FT   CHAIN         2    180       ADP-ribosylation factor 4.
FT                                /FTId=PRO_0000207392.
FT   NP_BIND      24     31       GTP (By similarity).
FT   NP_BIND      67     71       GTP (By similarity).
FT   NP_BIND     126    129       GTP (By similarity).
FT   MOD_RES      36     36       N6-acetyllysine (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (Potential).
FT   CONFLICT    108    108       Q -> E (in Ref. 2; BAB29041).
FT   CONFLICT    176    176       E -> R (in Ref. 2; BAB29041).
SQ   SEQUENCE   180 AA;  20397 MW;  09112917D8CE15D6 CRC64;
     MGLTISSLFS RLFGKKQMRI LMVGLDAAGK TTILYKLKLG EIVTTIPTIG FNVETVEYKN
     ICFTVWDVGG QDKIRPLWRH YFQNTQGLIF VVDSNDRERI QEGAAVLQKM LLEDELQDAV
     LLLFANKQDL PNAMAISEMT DKLGLQSLRN RTWYVQATCA TQGTGLYEGL DWLSNELSKR
//
ID   PFD3_MOUSE              Reviewed;         196 AA.
AC   P61759; O55228; Q15765; Q3U6M9; Q9CPZ0;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Prefoldin subunit 3;
DE   AltName: Full=Von Hippel-Lindau-binding protein 1;
DE            Short=VBP-1;
DE            Short=VHL-binding protein 1;
GN   Name=Vbp1; Synonyms=Pfdn3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Kidney, Stomach, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-196.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=97480721; PubMed=9339366; DOI=10.1006/geno.1997.4902;
RA   Brinke A., Green P.M., Giannelli F.;
RT   "Characterization of the gene (VBP1) and transcript for the von
RT   Hippel-Lindau binding protein and isolation of the highly conserved
RT   murine homologue.";
RL   Genomics 45:105-112(1997).
CC   -!- FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and
CC       transfers target proteins to it. Binds to nascent polypeptide
CC       chain and promotes folding in an environment in which there are
CC       many competing pathways for nonnative proteins (By similarity).
CC   -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta
CC       type subunits. Binds to the C-terminal part of VHL.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=In complex with VHL
CC       can translocate to the nucleus.
CC   -!- SIMILARITY: Belongs to the prefoldin subunit alpha family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC23908.1; Type=Erroneous initiation;
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DR   EMBL; AK002282; BAB21986.1; -; mRNA.
DR   EMBL; AK008847; BAB25926.1; -; mRNA.
DR   EMBL; AK077923; BAC37066.1; -; mRNA.
DR   EMBL; AK151527; BAE30475.1; -; mRNA.
DR   EMBL; AK153069; BAE31695.1; -; mRNA.
DR   EMBL; AK159284; BAE34961.1; -; mRNA.
DR   EMBL; AK167064; BAE39225.1; -; mRNA.
DR   EMBL; AK169185; BAE40962.1; -; mRNA.
DR   EMBL; U96760; AAC23908.1; ALT_INIT; mRNA.
DR   IPI; IPI00121851; -.
DR   RefSeq; NP_035822.2; NM_011692.2.
DR   UniGene; Mm.8294; -.
DR   ProteinModelPortal; P61759; -.
DR   SMR; P61759; 46-171.
DR   STRING; P61759; -.
DR   PhosphoSite; P61759; -.
DR   REPRODUCTION-2DPAGE; IPI00121851; -.
DR   REPRODUCTION-2DPAGE; P61759; -.
DR   PRIDE; P61759; -.
DR   Ensembl; ENSMUST00000033540; ENSMUSP00000033540; ENSMUSG00000031197.
DR   GeneID; 22327; -.
DR   KEGG; mmu:22327; -.
DR   UCSC; uc009tqd.1; mouse.
DR   CTD; 22327; -.
DR   MGI; MGI:1333804; Vbp1.
DR   GeneTree; ENSGT00390000018904; -.
DR   HOGENOM; HBG631514; -.
DR   HOVERGEN; HBG053576; -.
DR   InParanoid; P61759; -.
DR   OMA; QITTTEV; -.
DR   OrthoDB; EOG4DBTFP; -.
DR   PhylomeDB; P61759; -.
DR   NextBio; 302561; -.
DR   ArrayExpress; P61759; -.
DR   Bgee; P61759; -.
DR   CleanEx; MM_VBP1; -.
DR   Genevestigator; P61759; -.
DR   GermOnline; ENSMUSG00000031197; Mus musculus.
DR   GO; GO:0005634; C:nucleus; TAS:MGI.
DR   GO; GO:0016272; C:prefoldin complex; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   InterPro; IPR009053; Prefoldin.
DR   InterPro; IPR016655; Prefoldin_su-3.
DR   InterPro; IPR004127; Prefoldin_subunit.
DR   Pfam; PF02996; Prefoldin; 1.
DR   PIRSF; PIRSF016396; Prefoldin_subunit_3; 1.
DR   SUPFAM; SSF46579; Prefoldin; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Chaperone; Cytoplasm; Nucleus.
FT   CHAIN         1    196       Prefoldin subunit 3.
FT                                /FTId=PRO_0000153653.
FT   MOD_RES      58     58       N6-acetyllysine (By similarity).
SQ   SEQUENCE   196 AA;  22436 MW;  E5B9179296418DDE CRC64;
     MAAAKDGCGL ETAAGNGRRL HLGIPEAVFV EDVDSFMKQP GNETADTVLK KLDEQYQKYK
     FMELNLAQKK RRLKGQIPEI KQTLEILKYM QKKKESTNSM ETRFLLADNL YCKASVPPTD
     KVCLWLGANV MLEYDIDEAQ ALLEKNLSTA TKNLDSLEED LDFLRDQFTT TEVNMARVYN
     WDVKRRNKDD STKNKA
//
ID   SNN_MOUSE               Reviewed;          88 AA.
AC   P61807; O88369;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Stannin;
GN   Name=Snn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=98325608; PubMed=9657854; DOI=10.1007/s003359900818;
RA   Dejneka N.S., Polavarapu R., Deng X., Martin-Deleon P.A.,
RA   Billingsley M.L.;
RT   "Chromosomal localization and characterization of the stannin (Snn)
RT   gene.";
RL   Mamm. Genome 9:556-564(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND SER-83, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
CC   -!- FUNCTION: Plays a role in the toxic effects of organotins.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC       membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the stannin family.
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DR   EMBL; AF030522; AAC28428.1; -; Genomic_DNA.
DR   EMBL; BC017685; AAH17685.1; -; mRNA.
DR   EMBL; BC063027; AAH63027.1; -; mRNA.
DR   IPI; IPI00130066; -.
DR   RefSeq; NP_033249.1; NM_009223.3.
DR   UniGene; Mm.325800; -.
DR   ProteinModelPortal; P61807; -.
DR   SMR; P61807; 1-88.
DR   STRING; P61807; -.
DR   PhosphoSite; P61807; -.
DR   PRIDE; P61807; -.
DR   Ensembl; ENSMUST00000089011; ENSMUSP00000086405; ENSMUSG00000037972.
DR   GeneID; 20621; -.
DR   KEGG; mmu:20621; -.
DR   UCSC; uc007yeq.1; mouse.
DR   CTD; 20621; -.
DR   MGI; MGI:1276549; Snn.
DR   eggNOG; roNOG17649; -.
DR   HOGENOM; HBG269315; -.
DR   HOVERGEN; HBG017824; -.
DR   InParanoid; P61807; -.
DR   OMA; YSARGPC; -.
DR   OrthoDB; EOG4CRM1S; -.
DR   PhylomeDB; P61807; -.
DR   NextBio; 299013; -.
DR   ArrayExpress; P61807; -.
DR   Bgee; P61807; -.
DR   CleanEx; MM_SNN; -.
DR   Genevestigator; P61807; -.
DR   GermOnline; ENSMUSG00000037972; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR015137; SNN_cytoplasm.
DR   InterPro; IPR015136; SNN_linker.
DR   InterPro; IPR015135; SNN_transmemb.
DR   Pfam; PF09051; SNN_cytoplasm; 1.
DR   Pfam; PF09050; SNN_linker; 1.
DR   Pfam; PF09049; SNN_transmemb; 1.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1     88       Stannin.
FT                                /FTId=PRO_0000072015.
FT   TOPO_DOM      1     10       Mitochondrial intermembrane (By
FT                                similarity).
FT   TRANSMEM     11     31       Helical; (Potential).
FT   TOPO_DOM     32     88       Cytoplasmic (By similarity).
FT   MOD_RES      49     49       Phosphoserine.
FT   MOD_RES      83     83       Phosphoserine.
SQ   SEQUENCE   88 AA;  9501 MW;  EB8DA73323D816C5 CRC64;
     MSIMDHSPTT GVVTVIVILI AIAALGALIL GCWCYLRLQR ISQSEDEESI VGDGETKEPF
     LLVQYSAKGP CVERKAKLMT ANSPEVHG
//
ID   GABT_MOUSE              Reviewed;         500 AA.
AC   P61922; Q8BZA3;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=4-aminobutyrate aminotransferase, mitochondrial;
DE            EC=2.6.1.19;
DE   AltName: Full=(S)-3-amino-2-methylpropionate transaminase;
DE            EC=2.6.1.22;
DE   AltName: Full=GABA aminotransferase;
DE            Short=GABA-AT;
DE   AltName: Full=Gamma-amino-N-butyrate transaminase;
DE            Short=GABA transaminase;
DE            Short=GABA-T;
DE   AltName: Full=L-AIBAT;
DE   Flags: Precursor;
GN   Name=Abat; Synonyms=Gabat;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 35-47; 61-173; 221-231; 236-279; 286-310; 318-337;
RP   368-410; 414-432; 437-450 AND 461-470, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Friebe K., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-318, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- FUNCTION: Catalyzes the conversion of gamma-aminobutyrate and L-
CC       beta-aminoisobutyrate to succinate semialdehyde and methylmalonate
CC       semialdehyde, respectively. Can also convert delta-aminovalerate
CC       and beta-alanine (By similarity).
CC   -!- CATALYTIC ACTIVITY: 4-aminobutanoate + 2-oxoglutarate = succinate
CC       semialdehyde + L-glutamate.
CC   -!- CATALYTIC ACTIVITY: (S)-3-amino-2-methylpropanoate + 2-
CC       oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- SUBUNIT: Homodimer; disulfide-linked (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P61922-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=P61922-2; Sequence=VSP_012005;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family.
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DR   EMBL; BC058079; AAH58079.1; -; mRNA.
DR   EMBL; BC058521; AAH58521.1; -; mRNA.
DR   EMBL; AK036128; BAC29312.1; -; mRNA.
DR   IPI; IPI00227445; -.
DR   IPI; IPI00407499; -.
DR   RefSeq; NP_001164449.1; NM_001170978.1.
DR   RefSeq; NP_766549.2; NM_172961.3.
DR   UniGene; Mm.259315; -.
DR   ProteinModelPortal; P61922; -.
DR   SMR; P61922; 39-499.
DR   STRING; P61922; -.
DR   PhosphoSite; P61922; -.
DR   REPRODUCTION-2DPAGE; IPI00407499; -.
DR   PRIDE; P61922; -.
DR   Ensembl; ENSMUST00000065987; ENSMUSP00000063548; ENSMUSG00000057880.
DR   Ensembl; ENSMUST00000115839; ENSMUSP00000111505; ENSMUSG00000057880.
DR   GeneID; 268860; -.
DR   KEGG; mmu:268860; -.
DR   UCSC; uc007yco.1; mouse.
DR   UCSC; uc007ycp.1; mouse.
DR   CTD; 268860; -.
DR   MGI; MGI:2443582; Abat.
DR   eggNOG; roNOG08236; -.
DR   GeneTree; ENSGT00550000074885; -.
DR   HOGENOM; HBG483813; -.
DR   HOVERGEN; HBG000634; -.
DR   InParanoid; P61922; -.
DR   OMA; RSIRFRP; -.
DR   OrthoDB; EOG441QB6; -.
DR   PhylomeDB; P61922; -.
DR   BRENDA; 2.6.1.19; 244.
DR   BRENDA; 2.6.1.22; 244.
DR   NextBio; 392544; -.
DR   ArrayExpress; P61922; -.
DR   Bgee; P61922; -.
DR   CleanEx; MM_ABAT; -.
DR   Genevestigator; P61922; -.
DR   GermOnline; ENSMUSG00000057880; Mus musculus.
DR   GO; GO:0032144; C:4-aminobutyrate transaminase complex; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0047298; F:(S)-3-amino-2-methylpropionate transaminase activity; IEA:EC.
DR   GO; GO:0003867; F:4-aminobutyrate transaminase activity; IEA:EC.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR   GO; GO:0032145; F:succinate-semialdehyde dehydrogenase binding; ISS:UniProtKB.
DR   GO; GO:0048148; P:behavioral response to cocaine; IMP:UniProtKB.
DR   GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:InterPro.
DR   GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR004631; 4NH2But_aminotransferase_euk.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase_major_dom.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 2.
DR   PANTHER; PTHR11986; Aminotrans_3; 1.
DR   PANTHER; PTHR11986:SF6; GABAtrns_euk; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR   TIGRFAMs; TIGR00699; GABAtrns_euk; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Aminotransferase;
KW   Direct protein sequencing; Disulfide bond; Mitochondrion;
KW   Neurotransmitter degradation; Pyridoxal phosphate; Transferase;
KW   Transit peptide.
FT   TRANSIT       1     28       Mitochondrion (By similarity).
FT   CHAIN        29    500       4-aminobutyrate aminotransferase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000001250.
FT   MOD_RES     318    318       N6-acetyllysine.
FT   MOD_RES     357    357       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
FT   DISULFID    163    166       By similarity.
FT   DISULFID    321    321       Interchain (By similarity).
FT   VAR_SEQ     319    374       Missing (in isoform 2).
FT                                /FTId=VSP_012005.
SQ   SEQUENCE   500 AA;  56452 MW;  85AA331AB48355F3 CRC64;
     MAFLLITRRL ACSSQKNLHL FIPGSRYISQ AAAKVDIEFD YDGPLMKTEV PGPRSKELMK
     QLNTIQNAEA VHFFCNYEES RGNYLVDVDG NRMLDLYSQI SSVPIGYNHP ALAKLVQQPQ
     NASTFINRPA LGILPPENFV DKLQESLMSV APRGMSQLIT MACGSCSNEN AFKTIFMWYR
     SKERGQRGFS KEELETCMVN QSPGCPDYSI LSFMGAFHGR TMGCLATTHS KAIHKIDIPS
     FDWPIAPFPR LKYPLEEFTT DNQQEEARCL EEVEDLIVKY RKKKRTVAGI IVEPIQSEGG
     DNHASDDFFR KLRDIARKHG CAFLVDEVQT GGGCTGKFWA HEHWGLDDPA DVMTFSKKMM
     TGGFFHKEEF RPSAPYRIFN TWLGDPSKNL LLAEVINIIK REDLLNNVAR VGKTLLTGLL
     DLQAQYPQFI SRVRGRGTFC SFDTPDEAIR NKLILIARNK GVVLGGCGDK SIRFRPTLVF
     RDHHAHLFLS IFSGILADFK
//
ID   AP1S1_MOUSE             Reviewed;         158 AA.
AC   P61967; P82267; Q00382; Q9BTN4; Q9UDW9;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=AP-1 complex subunit sigma-1A;
DE   AltName: Full=Adapter-related protein complex 1 sigma-1A subunit;
DE   AltName: Full=Adaptor protein complex AP-1 sigma-1A subunit;
DE   AltName: Full=Clathrin assembly protein complex 1 sigma-1A small chain;
DE   AltName: Full=Clathrin coat assembly protein AP19;
DE   AltName: Full=Golgi adaptor HA1/AP1 adaptin sigma-1A subunit;
DE   AltName: Full=HA1 19 kDa subunit;
DE   AltName: Full=Sigma 1a subunit of AP-1 clathrin;
DE   AltName: Full=Sigma-adaptin 1A;
DE   AltName: Full=Sigma1A-adaptin;
GN   Name=Ap1s1; Synonyms=Ap19;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=91250426; PubMed=2040623;
RA   Kirchhausen T., Davis A.C., Frucht S., O'Brine Greco B., Payne G.S.,
RA   Tubb B.;
RT   "AP17 and AP19, the mammalian small chains of the clathrin-associated
RT   protein complexes show homology to Yap17p, their putative homolog in
RT   yeast.";
RL   J. Biol. Chem. 266:11153-11157(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1
CC       that plays a role in protein sorting in the late-Golgi/trans-Golgi
CC       network (TGN) and/or endosomes. The AP complexes mediate both the
CC       recruitment of clathrin to membranes and the recognition of
CC       sorting signals within the cytosolic tails of transmembrane cargo
CC       molecules.
CC   -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is an heterotetramer
CC       composed of two large adaptins (gamma-type subunit AP1G1 and beta-
CC       type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or
CC       AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or
CC       AP1S3).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle
CC       membrane; Peripheral membrane protein; Cytoplasmic side. Membrane,
CC       clathrin-coated pit. Note=Component of the coat surrounding the
CC       cytoplasmic face of coated vesicles located at the Golgi complex.
CC   -!- TISSUE SPECIFICITY: Detected in brain and embryonic stem cells.
CC   -!- SIMILARITY: Belongs to the adaptor complexes small subunit family.
CC   -----------------------------------------------------------------------
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DR   EMBL; M62418; AAA37243.1; -; mRNA.
DR   EMBL; AK002225; BAB21947.1; -; mRNA.
DR   EMBL; BC052692; AAH52692.1; -; mRNA.
DR   IPI; IPI00118026; -.
DR   PIR; A40535; A40535.
DR   RefSeq; NP_031483.1; NM_007457.2.
DR   UniGene; Mm.833; -.
DR   PDB; 1W63; X-ray; 4.00 A; Q/S/T/U/W/X=1-158.
DR   PDBsum; 1W63; -.
DR   ProteinModelPortal; P61967; -.
DR   SMR; P61967; 1-148.
DR   IntAct; P61967; 3.
DR   STRING; P61967; -.
DR   PhosphoSite; P61967; -.
DR   PRIDE; P61967; -.
DR   Ensembl; ENSMUST00000111080; ENSMUSP00000106709; ENSMUSG00000004849.
DR   GeneID; 11769; -.
DR   KEGG; mmu:11769; -.
DR   UCSC; uc009abm.1; mouse.
DR   CTD; 11769; -.
DR   MGI; MGI:1098244; Ap1s1.
DR   eggNOG; maNOG16056; -.
DR   GeneTree; ENSGT00530000062839; -.
DR   HOGENOM; HBG333059; -.
DR   HOVERGEN; HBG050517; -.
DR   InParanoid; P61967; -.
DR   OMA; MMRFMLL; -.
DR   OrthoDB; EOG469QVZ; -.
DR   PhylomeDB; P61967; -.
DR   NextBio; 279541; -.
DR   ArrayExpress; P61967; -.
DR   Bgee; P61967; -.
DR   CleanEx; MM_AP1S1; -.
DR   Genevestigator; P61967; -.
DR   GermOnline; ENSMUSG00000004849; Mus musculus.
DR   GO; GO:0030121; C:AP-1 adaptor complex; NAS:UniProtKB.
DR   GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0005802; C:trans-Golgi network; NAS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0008565; F:protein transporter activity; NAS:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; NAS:UniProtKB.
DR   InterPro; IPR016635; AP_complex_ssu.
DR   InterPro; IPR022775; AP_mu_sigma_su.
DR   InterPro; IPR000804; Clathrin_sm-chain_CS.
DR   InterPro; IPR011012; Longin-like.
DR   PANTHER; PTHR11753; PTHR11753; 1.
DR   Pfam; PF01217; Clat_adaptor_s; 1.
DR   PIRSF; PIRSF015588; AP_complex_sigma; 1.
DR   SUPFAM; SSF64356; Longin_like; 1.
DR   PROSITE; PS00989; CLAT_ADAPTOR_S; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coated pit; Cytoplasmic vesicle; Endocytosis;
KW   Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW   Transport.
FT   CHAIN         1    158       AP-1 complex subunit sigma-1A.
FT                                /FTId=PRO_0000193798.
FT   MOD_RES     147    147       Phosphoserine.
FT   STRAND        2      8
FT   STRAND       10     12
FT   STRAND       14     21
FT   HELIX        25     40
FT   STRAND       44     46
FT   STRAND       48     52
FT   STRAND       55     62
FT   STRAND       65     71
FT   STRAND       73     75
FT   HELIX        77     95
FT   HELIX       100    115
FT   STRAND      122    124
FT   HELIX       128    146
SQ   SEQUENCE   158 AA;  18733 MW;  E461937790406D8B CRC64;
     MMRFMLLFSR QGKLRLQKWY LATSDKERKK MVRELMQVVL ARKPKMCSFL EWRDLKVVYK
     RYASLYFCCA IEGQDNELIT LELIHRYVEL LDKYFGSVCE LDIIFNFEKA YFILDEFLMG
     GDVQDTSKKS VLKAIEQADL LQEEDESPRS VLEEMGLA
//
ID   HNRPK_MOUSE             Reviewed;         463 AA.
AC   P61979; Q07244; Q15671; Q60577; Q8BGQ8; Q922Y7; Q96J62;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   08-FEB-2011, entry version 84.
DE   RecName: Full=Heterogeneous nuclear ribonucleoprotein K;
DE            Short=hnRNP K;
GN   Name=Hnrnpk; Synonyms=Hnrpk;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Lymphoma;
RX   MEDLINE=94292525; PubMed=8021272;
RA   Ostrowski J., van Seuningen I., Seger R., Rauch C.T., Sleath P.R.,
RA   McMullen B.A., Bomsztyk K.;
RT   "Purification, cloning, and expression of a murine phosphoprotein that
RT   binds the kappa B motif in vitro identifies it as the homolog of the
RT   human heterogeneous nuclear ribonucleoprotein K protein. Description
RT   of a novel DNA-dependent phosphorylation process.";
RL   J. Biol. Chem. 269:17626-17634(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Spinal ganglion, Testis, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 149-163 AND 207-219, AND MASS SPECTROMETRY.
RC   TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [5]
RP   INTERACTION WITH ZIK1.
RX   MEDLINE=97066960; PubMed=8910362; DOI=10.1074/jbc.271.44.27701;
RA   Denisenko O.N., O'Neill B., Ostrowski J., Van Seuningen I.,
RA   Bomsztyk K.;
RT   "Zik1, a transcriptional repressor that interacts with the
RT   heterogeneous nuclear ribonucleoprotein particle K protein.";
RL   J. Biol. Chem. 271:27701-27706(1996).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: One of the major pre-mRNA-binding proteins. Binds
CC       tenaciously to poly(C) sequences. Likely to play a role in the
CC       nuclear metabolism of hnRNAs, particularly for pre-mRNAs that
CC       contain cytidine-rich sequences. Can also bind poly(C) single-
CC       stranded DNA.
CC   -!- SUBUNIT: Identified in the spliceosome C complex, at least
CC       composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23,
CC       DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1,
CC       GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRNPK,
CC       HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1,
CC       PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B,
CC       PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2,
CC       SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2,
CC       SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2,
CC       SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8 (By
CC       similarity). Interacts with ANKRD28 and RBM42. Interacts with DDX1
CC       (By similarity). Interacts with ZIK1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus,
CC       nucleoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P61979-1, Q07244-1;
CC         Sequence=Displayed;
CC       Name=2;
CC         IsoId=P61979-2, Q07244-2;
CC         Sequence=VSP_010622;
CC       Name=3;
CC         IsoId=P61979-3; Sequence=VSP_012581;
CC   -!- SIMILARITY: Contains 3 KH domains.
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DR   EMBL; L31961; AAA21731.1; -; mRNA.
DR   EMBL; AK011428; BAB27614.1; -; mRNA.
DR   EMBL; AK051313; BAC34601.1; -; mRNA.
DR   EMBL; AK078777; BAC37389.1; -; mRNA.
DR   EMBL; AK088462; BAC40368.1; -; mRNA.
DR   EMBL; BC006694; AAH06694.1; -; mRNA.
DR   IPI; IPI00223253; -.
DR   IPI; IPI00224575; -.
DR   IPI; IPI00890005; -.
DR   RefSeq; NP_079555.1; NM_025279.2.
DR   UniGene; Mm.142872; -.
DR   UniGene; Mm.470123; -.
DR   ProteinModelPortal; P61979; -.
DR   SMR; P61979; 40-215, 385-463.
DR   IntAct; P61979; 8.
DR   STRING; P61979; -.
DR   PhosphoSite; P61979; -.
DR   REPRODUCTION-2DPAGE; IPI00223253; -.
DR   REPRODUCTION-2DPAGE; P61979; -.
DR   PRIDE; P61979; -.
DR   Ensembl; ENSMUST00000043269; ENSMUSP00000039269; ENSMUSG00000021546.
DR   Ensembl; ENSMUST00000116403; ENSMUSP00000112104; ENSMUSG00000021546.
DR   Ensembl; ENSMUST00000116404; ENSMUSP00000112105; ENSMUSG00000021546.
DR   GeneID; 15387; -.
DR   KEGG; mmu:15387; -.
DR   UCSC; uc007qtx.1; mouse.
DR   UCSC; uc007qty.1; mouse.
DR   CTD; 15387; -.
DR   MGI; MGI:99894; Hnrnpk.
DR   eggNOG; roNOG14775; -.
DR   GeneTree; ENSGT00550000074311; -.
DR   HOVERGEN; HBG051916; -.
DR   OMA; XGLQLPS; -.
DR   PhylomeDB; P61979; -.
DR   NextBio; 288062; -.
DR   ArrayExpress; P61979; -.
DR   Bgee; P61979; -.
DR   Genevestigator; P61979; -.
DR   GermOnline; ENSMUSG00000063902; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR004088; KH_type_1.
DR   InterPro; IPR018111; KH_type_1_subgr.
DR   InterPro; IPR012987; ROK_N.
DR   Pfam; PF00013; KH_1; 3.
DR   Pfam; PF08067; ROKNT; 1.
DR   SMART; SM00322; KH; 3.
DR   PROSITE; PS50084; KH_TYPE_1; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm;
KW   Direct protein sequencing; DNA-binding; Isopeptide bond; Methylation;
KW   mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Repeat;
KW   Ribonucleoprotein; RNA-binding; Spliceosome; Ubl conjugation.
FT   CHAIN         1    463       Heterogeneous nuclear ribonucleoprotein
FT                                K.
FT                                /FTId=PRO_0000050097.
FT   DOMAIN       42    104       KH 1.
FT   REPEAT       54     76       1-1.
FT   REPEAT       59     62       3-1.
FT   DOMAIN      144    209       KH 2.
FT   REPEAT      245    250       2-1.
FT   REPEAT      257    260       3-2.
FT   REPEAT      267    270       3-3.
FT   REPEAT      295    298       3-4.
FT   REPEAT      324    329       2-2.
FT   DOMAIN      387    451       KH 3.
FT   REPEAT      399    421       1-2.
FT   REPEAT      404    407       3-5.
FT   REGION        1    276       Necessary for interaction with DDX1 (By
FT                                similarity).
FT   REGION       54    421       2 X 22 AA approximate repeats.
FT   REGION       59    407       5 X 4 AA repeats of G-X-G-G.
FT   REGION      209    337       Interaction with ZIK1.
FT   REGION      236    273       RNA-binding RGG-box.
FT   REGION      245    329       2 X 6 AA approximate repeats.
FT   COMPBIAS    289    294       Poly-Pro.
FT   COMPBIAS    310    315       Poly-Pro.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES       3      3       Phosphothreonine (By similarity).
FT   MOD_RES      36     36       Phosphoserine (By similarity).
FT   MOD_RES     116    116       Phosphoserine (By similarity).
FT   MOD_RES     214    214       Phosphoserine (By similarity).
FT   MOD_RES     216    216       Phosphoserine.
FT   MOD_RES     284    284       Phosphoserine.
FT   MOD_RES     296    296       Omega-N-methylated arginine (By
FT                                similarity).
FT   MOD_RES     299    299       Omega-N-methylated arginine (By
FT                                similarity).
FT   MOD_RES     379    379       Phosphoserine (By similarity).
FT   MOD_RES     380    380       Phosphotyrosine (By similarity).
FT   CROSSLNK    422    422       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   VAR_SEQ     111    134       Missing (in isoform 3).
FT                                /FTId=VSP_012581.
FT   VAR_SEQ     459    463       SGKFF -> ADVEGF (in isoform 2).
FT                                /FTId=VSP_010622.
FT   CONFLICT    132    132       C -> V (in Ref. 1; AAA21731).
FT   CONFLICT    136    136       Q -> P (in Ref. 1; AAA21731).
FT   CONFLICT    154    154       S -> T (in Ref. 1; AAA21731).
FT   CONFLICT    334    334       D -> S (in Ref. 1; AAA21731).
FT   CONFLICT    350    350       D -> E (in Ref. 1; AAA21731).
SQ   SEQUENCE   463 AA;  50976 MW;  0F70EE169B2A064A CRC64;
     METEQPEETF PNTETNGEFG KRPAEDMEEE QAFKRSRNTD EMVELRILLQ SKNAGAVIGK
     GGKNIKALRT DYNASVSVPD SSGPERILSI SADIETIGEI LKKIIPTLEE GLQLPSPTAT
     SQLPLESDAV ECLNYQHYKG SDFDCELRLL IHQSLAGGII GVKGAKIKEL RENTQTTIKL
     FQECCPHSTD RVVLIGGKPD RVVECIKIIL DLISESPIKG RAQPYDPNFY DETYDYGGFT
     MMFDDRRGRP VGFPMRGRGG FDRMPPGRGG RPMPPSRRDY DDMSPRRGPP PPPPGRGGRG
     GSRARNLPLP PPPPPRGGDL MAYDRRGRPG DRYDGMVGFS ADETWDSAID TWSPSEWQMA
     YEPQGGSGYD YSYAGGRGSY GDLGGPIITT QVTIPKDLAG SIIGKGGQRI KQIRHESGAS
     IKIDEPLEGS EDRIITITGT QDQIQNAQYL LQNSVKQYSG KFF
//
ID   1433G_MOUSE             Reviewed;         247 AA.
AC   P61982; O70457; P35214; Q3UFD6; Q4FK44; Q9UDP2; Q9UN99;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=14-3-3 protein gamma;
DE   Contains:
DE     RecName: Full=14-3-3 protein gamma, N-terminally processed;
GN   Name=Ywhag;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Karpitskiy V.V., Shaw A.S.;
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E.,
RA   Mollenhauer J., Wiemann S., Schick M., Korn B.;
RT   "Cloning of mouse full open reading frames in Gateway(R) system entry
RT   vector (pDONR201).";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 13-50; 43-56; 62-69; 78-83; 92-120 AND 133-247,
RP   AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Friebe K., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-117, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC       spectrum of both general and specialized signaling pathway. Binds
CC       to a large number of partners, usually by recognition of a
CC       phosphoserine or phosphothreonine motif. Binding generally results
CC       in the modulation of the activity of the binding partner.
CC   -!- SUBUNIT: Homodimer. Interacts with RAF1, SSH1 and CRTC2/TORC2.
CC       Interacts with ABL1 (phosphorylated form); the interaction retains
CC       it in the cytoplasm. Interacts with GAB2 (By similarity).
CC   -!- INTERACTION:
CC       Q9P0K1-3:ADAM22 (xeno); NbExp=1; IntAct=EBI-359843, EBI-1567267;
CC       Q08460:Kcnma1; NbExp=1; IntAct=EBI-359843, EBI-1633915;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- PTM: Phosphorylated by various PKC isozymes (By similarity).
CC   -!- SIMILARITY: Belongs to the 14-3-3 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE28625.1; Type=Erroneous initiation;
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DR   EMBL; AF058799; AAC14345.1; -; mRNA.
DR   EMBL; CT010208; CAJ18416.1; -; mRNA.
DR   EMBL; AK088847; BAC40609.1; -; mRNA.
DR   EMBL; AK148618; BAE28625.1; ALT_INIT; mRNA.
DR   EMBL; AK153307; BAE31888.1; -; mRNA.
DR   EMBL; AK164356; BAE37756.1; -; mRNA.
DR   EMBL; BC008129; AAH08129.1; -; mRNA.
DR   IPI; IPI00230707; -.
DR   RefSeq; NP_061359.2; NM_018871.3.
DR   UniGene; Mm.233813; -.
DR   ProteinModelPortal; P61982; -.
DR   SMR; P61982; 2-234.
DR   IntAct; P61982; 14.
DR   STRING; P61982; -.
DR   PhosphoSite; P61982; -.
DR   REPRODUCTION-2DPAGE; P61982; -.
DR   UCD-2DPAGE; P61982; -.
DR   PRIDE; P61982; -.
DR   Ensembl; ENSMUST00000055808; ENSMUSP00000051223; ENSMUSG00000051391.
DR   GeneID; 22628; -.
DR   KEGG; mmu:22628; -.
DR   UCSC; uc008zzf.1; mouse.
DR   CTD; 22628; -.
DR   MGI; MGI:108109; Ywhag.
DR   eggNOG; roNOG10169; -.
DR   GeneTree; ENSGT00550000074221; -.
DR   HOVERGEN; HBG050423; -.
DR   InParanoid; P61982; -.
DR   OMA; CSETQHE; -.
DR   OrthoDB; EOG48PMM0; -.
DR   PhylomeDB; P61982; -.
DR   NextBio; 302991; -.
DR   ArrayExpress; P61982; -.
DR   Bgee; P61982; -.
DR   Genevestigator; P61982; -.
DR   GermOnline; ENSMUSG00000051391; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR   GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; IDA:MGI.
DR   GO; GO:0005080; F:protein kinase C binding; ISS:UniProtKB.
DR   GO; GO:0006605; P:protein targeting; IDA:MGI.
DR   GO; GO:0045664; P:regulation of neuron differentiation; ISS:UniProtKB.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
DR   InterPro; IPR000308; 14-3-3.
DR   PANTHER; PTHR18860; 14-3-3; 1.
DR   PIRSF; PIRSF000868; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Phosphoprotein.
FT   CHAIN         1    247       14-3-3 protein gamma.
FT                                /FTId=PRO_0000367908.
FT   INIT_MET      1      1       Removed; alternate (By similarity).
FT   CHAIN         2    247       14-3-3 protein gamma, N-terminally
FT                                processed.
FT                                /FTId=PRO_0000058607.
FT   SITE         57     57       Interaction with phosphoserine on
FT                                interacting protein (By similarity).
FT   SITE        132    132       Interaction with phosphoserine on
FT                                interacting protein (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine; in 14-3-3 protein
FT                                gamma; alternate (By similarity).
FT   MOD_RES       2      2       N-acetylvaline; in 14-3-3 protein gamma,
FT                                N-terminally processed (By similarity).
FT   MOD_RES     117    117       Phosphotyrosine.
FT   MOD_RES     145    145       Phosphothreonine (By similarity).
FT   CONFLICT    150    150       S -> F (in Ref. 1; AAC14345).
SQ   SEQUENCE   247 AA;  28303 MW;  B0D16C6DE1F4455D CRC64;
     MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK NVVGARRSSW
     RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV LSLLDNYLIK NCSETQYESK
     VFYLKMKGDY YRYLAEVATG EKRATVVESS EKAYSEAHEI SKEHMQPTHP IRLGLALNYS
     VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD
     DGGEGNN
//
ID   LRCH1_MOUSE             Reviewed;         709 AA.
AC   P62046;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Leucine-rich repeat and calponin homology domain-containing protein 1;
DE   AltName: Full=Calponin homology domain-containing protein 1;
GN   Name=Lrch1; Synonyms=Chdc1, Kiaa1016;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-581, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC   -!- SIMILARITY: Contains 9 LRR (leucine-rich) repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98074.1; Type=Erroneous initiation;
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CC   -----------------------------------------------------------------------
DR   EMBL; AK129264; BAC98074.1; ALT_INIT; mRNA.
DR   IPI; IPI00420521; -.
DR   RefSeq; NP_001028611.2; NM_001033439.2.
DR   UniGene; Mm.288868; -.
DR   ProteinModelPortal; P62046; -.
DR   SMR; P62046; 11-266, 586-701.
DR   PhosphoSite; P62046; -.
DR   PRIDE; P62046; -.
DR   Ensembl; ENSMUST00000088970; ENSMUSP00000086363; ENSMUSG00000068015.
DR   GeneID; 380916; -.
DR   KEGG; mmu:380916; -.
DR   UCSC; uc007uqf.1; mouse.
DR   CTD; 380916; -.
DR   MGI; MGI:2443390; Lrch1.
DR   eggNOG; roNOG08733; -.
DR   HOGENOM; HBG717214; -.
DR   HOVERGEN; HBG052350; -.
DR   InParanoid; P62046; -.
DR   OrthoDB; EOG4J6RQF; -.
DR   NextBio; 401373; -.
DR   ArrayExpress; P62046; -.
DR   Bgee; P62046; -.
DR   Genevestigator; P62046; -.
DR   GermOnline; ENSMUSG00000068015; Mus musculus.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF00560; LRR_1; 3.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00369; LRR_TYP; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS51450; LRR; 6.
PE   1: Evidence at protein level;
KW   Leucine-rich repeat; Phosphoprotein; Repeat.
FT   CHAIN         1    709       Leucine-rich repeat and calponin homology
FT                                domain-containing protein 1.
FT                                /FTId=PRO_0000084479.
FT   REPEAT       60     83       LRR 1.
FT   REPEAT       86    108       LRR 2.
FT   REPEAT      109    131       LRR 3.
FT   REPEAT      132    155       LRR 4.
FT   REPEAT      157    176       LRR 5.
FT   REPEAT      177    199       LRR 6.
FT   REPEAT      200    223       LRR 7.
FT   REPEAT      225    244       LRR 8.
FT   REPEAT      245    268       LRR 9.
FT   DOMAIN      589    702       CH.
FT   COMPBIAS     21     37       His-rich.
FT   MOD_RES     581    581       Phosphothreonine.
SQ   SEQUENCE   709 AA;  79032 MW;  B148018FCA7C9E58 CRC64;
     MATPGSEPQA FAPALSVTAL HPHLHQHHQH HQHHQHHGGT GGTGFNLPLN RGLERALEEA
     ANSGGLNLSA RKLKEFPRTT APGHDLSDTV RADLSKNRLV EVPMELCQFV SLEILNLYHN
     CIRVIPEAIV NLQMLTHLNL SRNQLSALPA CLCGLPLKVL IASNNKLGSL PEEIGQLKQL
     MELDVSCNEI TALPQQIGQL KSLRELNVRR NYLKVLPPEL VDLPLVKFDF SCNKVLVIPV
     CFREMKQLQV LLLENNPLQS PPAQICTKGK VHIFKYLSIQ ACQIKTSDSL YLPTIERPHL
     HQHVEDSKKD SDSGVGSDNG DKRLSATEPS DEDTVSLNAP MSNIVEEDQT IKEDACHRLT
     PAKGEFQPKP SVLGDSGISG QEREQLAGRA DARHSGLMNY IKDQAEDCEE LLRIEEDAHW
     HMEELLNSSK DRELDIAMIE QLREAELLQD PNGLSADIIE RSILNLFPMD SGEASEFPDP
     SLNGQLQLET SPDREVQNDL MLQSNGSQYS PNEIRENSPS VSPTANITAP FGLKPRSGSW
     CPEEVQGSLQ AESSPRRPQL LSRHVFLRPQ RNLESIDPQF TIRRKMEQMR EEKELVEQLR
     ESIEMRLKVT LHEDLGAALM DGVVLCHLAN HVRPRSVASI HVPSPAVPKL SMAKCRRNVE
     NFLEACRKLG VPEEKLCLPH HILEEKGLVK VGTTVQALLD VTVTKALFT
//
ID   RRAS2_MOUSE             Reviewed;         204 AA.
AC   P62071; P17082; Q3TA79; Q8C5D1; Q9D0H6;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Ras-related protein R-Ras2;
DE   Flags: Precursor;
GN   Name=Rras2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Colon, Embryo, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: It is a plasma membrane-associated GTP-binding protein
CC       with GTPase activity. Might transduce growth inhibitory signals
CC       across the cell membrane, exerting its effect through an effector
CC       shared with the Ras proteins but in an antagonistic fashion.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (By similarity). Note=Inner surface of plasma membrane
CC       possibly with attachment requiring acylation of the C-terminal
CC       cysteine (By similarity with RAS).
CC   -!- PTM: May be post-translationally modified by both palmitoylation
CC       and polyisoprenylation (By similarity).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
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DR   EMBL; AK011419; BAB27607.1; -; mRNA.
DR   EMBL; AK078870; BAC37432.1; -; mRNA.
DR   EMBL; AK172037; BAE42790.1; -; mRNA.
DR   EMBL; BC003871; AAH03871.1; -; mRNA.
DR   IPI; IPI00323822; -.
DR   RefSeq; NP_080122.2; NM_025846.2.
DR   UniGene; Mm.276572; -.
DR   ProteinModelPortal; P62071; -.
DR   SMR; P62071; 13-181.
DR   STRING; P62071; -.
DR   PhosphoSite; P62071; -.
DR   PRIDE; P62071; -.
DR   Ensembl; ENSMUST00000069449; ENSMUSP00000069752; ENSMUSG00000055723.
DR   GeneID; 66922; -.
DR   KEGG; mmu:66922; -.
DR   UCSC; uc009jhw.1; mouse.
DR   CTD; 66922; -.
DR   MGI; MGI:1914172; Rras2.
DR   eggNOG; roNOG11250; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; P62071; -.
DR   OMA; AITIQFI; -.
DR   OrthoDB; EOG4P5KB6; -.
DR   PhylomeDB; P62071; -.
DR   NextBio; 323025; -.
DR   ArrayExpress; P62071; -.
DR   Bgee; P62071; -.
DR   CleanEx; MM_RRAS2; -.
DR   Genevestigator; P62071; -.
DR   GermOnline; ENSMUSG00000055723; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0030335; P:positive regulation of cell migration; IGI:MGI.
DR   GO; GO:0007265; P:Ras protein signal transduction; IDA:MGI.
DR   InterPro; IPR003577; GTPase_Ras.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR020849; Ras_small_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00173; RAS; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; GTP-binding; Lipoprotein; Membrane;
KW   Methylation; Nucleotide-binding; Palmitate; Phosphoprotein;
KW   Prenylation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    201       Ras-related protein R-Ras2.
FT                                /FTId=PRO_0000082653.
FT   PROPEP      202    204       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000281303.
FT   NP_BIND      21     29       GTP (By similarity).
FT   NP_BIND      68     72       GTP (By similarity).
FT   NP_BIND     127    130       GTP (By similarity).
FT   NP_BIND     157    159       GTP (By similarity).
FT   MOTIF        43     51       Effector region (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     186    186       Phosphoserine.
FT   MOD_RES     190    190       Phosphothreonine (By similarity).
FT   MOD_RES     201    201       Cysteine methyl ester (By similarity).
FT   LIPID       199    199       S-palmitoyl cysteine (Potential).
FT   LIPID       201    201       S-farnesyl cysteine (By similarity).
FT   CONFLICT      4      4       A -> D (in Ref. 1; BAC37432).
FT   CONFLICT     96     96       T -> R (in Ref. 1; BAB27607).
SQ   SEQUENCE   204 AA;  23400 MW;  BA7D4759DC49446F CRC64;
     MAAAGWRDGS GQEKYRLVVV GGGGVGKSAL TIQFIQSYFV TDYDPTIEDS YTKQCVIDDR
     AARLDILDTA GQEEFGAMRE QYMRTGEGFL LVFSVTDRGS FEEIYKFQRQ ILRVKDRDEF
     PMILIGNKAD LDHQRQVTQE EGQQLARQLK VTYMEASAKI RMNVDQAFHE LVRVIRKFQE
     QECPPSPEPT RKEKDKKGCH CVIF
//
ID   PP1A_MOUSE              Reviewed;         330 AA.
AC   P62137; P08129; P20653; P22802; Q3U7G7; Q9Z1G2;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Serine/threonine-protein phosphatase PP1-alpha catalytic subunit;
DE            Short=PP-1A;
DE            EC=3.1.3.16;
GN   Name=Ppp1ca; Synonyms=Ppp1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ortiz J.M., Lorenzo M.L., Eguiraun A., Andres I., Sangrador A.,
RA   Allshire R., Hastie N.D.;
RL   Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2;
RC   TISSUE=Extraembryonic tissue, Liver, Pancreas, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 44-74; 114-122 AND 247-260, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 69-90.
RX   MEDLINE=94357899; PubMed=8077208;
RA   Becker W., Kentrup H., Klumpp S., Schultz J.E., Joost H.G.;
RT   "Molecular cloning of a protein serine/threonine phosphatase
RT   containing a putative regulatory tetratricopeptide repeat domain.";
RL   J. Biol. Chem. 269:22586-22592(1994).
RN   [6]
RP   INTERACTION WITH PPP1R15B.
RX   PubMed=14638860; DOI=10.1083/jcb.200308075;
RA   Jousse C., Oyadomari S., Novoa I., Lu P., Zhang Y., Harding H.P.,
RA   Ron D.;
RT   "Inhibition of a constitutive translation initiation factor 2alpha
RT   phosphatase, CReP, promotes survival of stressed cells.";
RL   J. Cell Biol. 163:767-775(2003).
RN   [7]
RP   IDENTIFICATION IN COMPLEX WITH PPP1R15B AND NCK1.
RX   PubMed=16835242; DOI=10.1074/jbc.M513556200;
RA   Latreille M., Larose L.;
RT   "Nck in a complex containing the catalytic subunit of protein
RT   phosphatase 1 regulates eukaryotic initiation factor 2alpha signaling
RT   and cell survival to endoplasmic reticulum stress.";
RL   J. Biol. Chem. 281:26633-26644(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-320, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-306, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Protein phosphatase 1 (PP1) is essential for cell
CC       division, and participates in the regulation of glycogen
CC       metabolism, muscle contractility and protein synthesis. Involved
CC       in regulation of ionic conductances and long-term synaptic
CC       plasticity. May play an important role in dephosphorylating
CC       substrates such as the postsynaptic density-associated
CC       Ca(2+)/calmodulin dependent protein kinase II. Component of the
CC       PTW/PP1 phosphatase complex, which plays a role in the control of
CC       chromatin structure and cell cycle progression during the
CC       transition from mitosis into interphase (By similarity).
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity).
CC   -!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or
CC       PPP1CC, which is folded into its native form by inhibitor 2 and
CC       glycogen synthetase kinase 3, and then complexed to one or several
CC       targeting or regulatory subunits. PPP1R12A, PPP1R12B and PPP1R12C
CC       mediate binding to myosin. PPP1R3A, PPP1R3B, PPP1R3C and PPP1R3D
CC       mediate binding to glycogen. Component of the MLL5-L complex, at
CC       least composed of MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB
CC       and OGT. Interacts with PPP1R9A, PPP1R9B and PPP1R7 (By
CC       similarity). PPP1R15A and PPP1R15B mediate binding to EIF2S1. Part
CC       of a complex containing PPP1R15B, PP1 and NCK1/2. Interacts with
CC       YLPM1. Forms a complex with ILF2, ILF3, YLPM1, KHDRBS1, RBMX and
CC       NCOA5. Interacts with NOM1 and PPP1R8. Interacts with PPP1R16B.
CC       Interacts. with RPSA only in the presence of PPP1R16B. Component
CC       of the PTW/PP1 phosphatase complex, composed of PPP1R10/PNUTS,
CC       TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC. Interacts with
CC       PPP1R10/PNUTS and PPP1R8. Interacts with WDR82 in the presence of
CC       PPP1R10/PNUTS. Interacts with SH3RF2 (By similarity).
CC   -!- INTERACTION:
CC       O88879:Apaf1; NbExp=1; IntAct=EBI-357187, EBI-1202386;
CC       Q62388:Atm; NbExp=1; IntAct=EBI-357187, EBI-1202183;
CC       Q9JKK8:Atr; NbExp=1; IntAct=EBI-357187, EBI-1202426;
CC       P10417:Bcl2; NbExp=1; IntAct=EBI-357187, EBI-526314;
CC       P30282:Ccnd3; NbExp=1; IntAct=EBI-357187, EBI-847337;
CC       Q8CFI2:Cdc34; NbExp=1; IntAct=EBI-357187, EBI-1202331;
CC       Q64364:Cdkn2a; NbExp=1; IntAct=EBI-357187, EBI-1202287;
CC       Q6ZWX6:Eif2s1; NbExp=1; IntAct=EBI-357187, EBI-1202234;
CC       O09106:Hdac1; NbExp=1; IntAct=EBI-357187, EBI-301912;
CC       P41136:Id2; NbExp=2; IntAct=EBI-357187, EBI-309167;
CC       P10637:Mapt; NbExp=1; IntAct=EBI-357187, EBI-774043;
CC       P28574:Max; NbExp=1; IntAct=EBI-357187, EBI-1183003;
CC       O35942:Nek2; NbExp=1; IntAct=EBI-357187, EBI-1202268;
CC       P17918:Pcna; NbExp=2; IntAct=EBI-357187, EBI-1173716;
CC       P13405:Rb1; NbExp=1; IntAct=EBI-357187, EBI-971782;
CC       Q9WTX5:Skp1; NbExp=2; IntAct=EBI-357187, EBI-1202363;
CC       Q9EP53:Tsc1; NbExp=1; IntAct=EBI-357187, EBI-1202690;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Nucleus, nucleoplasm (By similarity). Nucleus,
CC       nucleolus (By similarity). Note=Primarily nuclear and largely
CC       excluded from the nucleolus. Highly mobile in cells and can be
CC       relocalized through interaction with targeting subunits. NOM1
CC       plays a role in targeting this protein to the nucleolus. In the
CC       presence of PPP1R8 relocalizes from the nucleus to nuclear
CC       speckles (By similarity).
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=The things we forget -
CC       Issue 32 of March 2003;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt032.shtml";
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DR   EMBL; U25809; AAC99814.1; -; mRNA.
DR   EMBL; AK007932; BAB25358.1; -; mRNA.
DR   EMBL; AK028392; BAC25928.1; -; mRNA.
DR   EMBL; AK090070; BAC41078.1; -; mRNA.
DR   EMBL; AK151582; BAE30522.1; -; mRNA.
DR   EMBL; AK152667; BAE31402.1; -; mRNA.
DR   EMBL; AK153517; BAE32060.1; -; mRNA.
DR   EMBL; AK159575; BAE35196.1; -; mRNA.
DR   EMBL; AK167244; BAE39365.1; -; mRNA.
DR   EMBL; AK167538; BAE39605.1; -; mRNA.
DR   EMBL; AK167880; BAE39893.1; -; mRNA.
DR   EMBL; AK167981; BAE39973.1; -; mRNA.
DR   EMBL; BC014828; AAH14828.1; -; mRNA.
DR   IPI; IPI00130185; -.
DR   RefSeq; NP_114074.1; NM_031868.2.
DR   UniGene; Mm.1970; -.
DR   ProteinModelPortal; P62137; -.
DR   SMR; P62137; 7-299.
DR   IntAct; P62137; 22.
DR   STRING; P62137; -.
DR   PhosphoSite; P62137; -.
DR   PRIDE; P62137; -.
DR   Ensembl; ENSMUST00000046094; ENSMUSP00000039109; ENSMUSG00000040385.
DR   GeneID; 19045; -.
DR   KEGG; mmu:19045; -.
DR   UCSC; uc008fzg.1; mouse.
DR   CTD; 19045; -.
DR   MGI; MGI:103016; Ppp1ca.
DR   eggNOG; roNOG09668; -.
DR   HOGENOM; HBG716770; -.
DR   HOVERGEN; HBG000216; -.
DR   InParanoid; P62137; -.
DR   OMA; LTPHCAP; -.
DR   OrthoDB; EOG49GKGT; -.
DR   PhylomeDB; P62137; -.
DR   BRENDA; 3.1.3.16; 244.
DR   NextBio; 295505; -.
DR   ArrayExpress; P62137; -.
DR   Bgee; P62137; -.
DR   Genevestigator; P62137; -.
DR   GermOnline; ENSMUSG00000040385; Mus musculus.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR   GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:MGI.
DR   GO; GO:0048754; P:branching morphogenesis of a tube; IMP:MGI.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007143; P:female meiosis; TAS:MGI.
DR   GO; GO:0005977; P:glycogen metabolic process; TAS:MGI.
DR   GO; GO:0030324; P:lung development; IMP:MGI.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
DR   GO; GO:0006417; P:regulation of translation; TAS:MGI.
DR   InterPro; IPR004843; Metallo-dependent_phosphatase.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR11668; T_phtase_apaH; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Carbohydrate metabolism; Cell cycle; Cell division;
KW   Cytoplasm; Direct protein sequencing; Glycogen metabolism; Hydrolase;
KW   Iron; Manganese; Metal-binding; Nucleus; Phosphoprotein;
KW   Protein phosphatase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    330       Serine/threonine-protein phosphatase PP1-
FT                                alpha catalytic subunit.
FT                                /FTId=PRO_0000058775.
FT   ACT_SITE    125    125       Proton donor (By similarity).
FT   METAL        64     64       Iron (By similarity).
FT   METAL        66     66       Iron (By similarity).
FT   METAL        92     92       Iron (By similarity).
FT   METAL        92     92       Manganese (By similarity).
FT   METAL       124    124       Manganese (By similarity).
FT   METAL       173    173       Manganese (By similarity).
FT   METAL       248    248       Manganese (By similarity).
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES     306    306       Phosphotyrosine.
FT   MOD_RES     320    320       Phosphothreonine.
SQ   SEQUENCE   330 AA;  37540 MW;  8FBFD158A52282E0 CRC64;
     MSDSEKLNLD SIIGRLLEVQ GSRPGKNVQL TENEIRGLCL KSREIFLSQP ILLELEAPLK
     ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIRYPENFFL
     LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL
     QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVQGWGEND RGVSFTFGAE VVAKFLHKHD
     LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAD
     KNKGKYGQFS GLNPGGRPIT PPRNSAKAKK
//
ID   PP1B_MOUSE              Reviewed;         327 AA.
AC   P62141; P37140; Q3TBE5; Q3TL90; Q542E7; Q8C285; Q9DBY2;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Serine/threonine-protein phosphatase PP1-beta catalytic subunit;
DE            Short=PP-1B;
DE            EC=3.1.3.16;
DE            EC=3.1.3.53;
GN   Name=Ppp1cb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=89288305; PubMed=2544298; DOI=10.1016/0092-8674(89)90338-3;
RA   Ohkura H., Kinoshita N., Miyatani S., Toda T., Yanagida M.;
RT   "The fission yeast dis2+ gene required for chromosome disjoining
RT   encodes one of two putative type 1 protein phosphatases.";
RL   Cell 57:997-1007(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Dendritic cell, Embryonic head, Embryonic heart,
RC   Embryonic kidney, Lung, Mammary gland, Morula, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 26-35; 60-73 AND 150-167, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   INTERACTION WITH PPP1R15B.
RX   PubMed=14638860; DOI=10.1083/jcb.200308075;
RA   Jousse C., Oyadomari S., Novoa I., Lu P., Zhang Y., Harding H.P.,
RA   Ron D.;
RT   "Inhibition of a constitutive translation initiation factor 2alpha
RT   phosphatase, CReP, promotes survival of stressed cells.";
RL   J. Cell Biol. 163:767-775(2003).
RN   [6]
RP   IDENTIFICATION IN COMPLEX WITH PPP1R15B AND NCK1.
RX   PubMed=16835242; DOI=10.1074/jbc.M513556200;
RA   Latreille M., Larose L.;
RT   "Nck in a complex containing the catalytic subunit of protein
RT   phosphatase 1 regulates eukaryotic initiation factor 2alpha signaling
RT   and cell survival to endoplasmic reticulum stress.";
RL   J. Biol. Chem. 281:26633-26644(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-316, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Protein phosphatase (PP1) is essential for cell
CC       division, it participates in the regulation of glycogen
CC       metabolism, muscle contractility and protein synthesis. Involved
CC       in regulation of ionic conductances and long-term synaptic
CC       plasticity. Component of the PTW/PP1 phosphatase complex, which
CC       plays a role in the control of chromatin structure and cell cycle
CC       progression during the transition from mitosis into interphase (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- CATALYTIC ACTIVITY: [Myosin light-chain] phosphate + H(2)O =
CC       [myosin light-chain] + phosphate.
CC   -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity).
CC   -!- ENZYME REGULATION: Inhibited by the toxins okadaic acid,
CC       tautomycin and microcystin Leu-Arg. The phosphatase activity of
CC       the PPP1R15A-PP1 complex toward EIF2S1 is specifically inhibited
CC       by Salubrinal, a drug that protects cells from endoplasmic
CC       reticulum stress (By similarity).
CC   -!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or
CC       PPP1CC, which is folded into its native form by inhibitor 2 and
CC       glycogen synthetase kinase 3, and then complexed to one or several
CC       targeting or regulatory subunits. The targeting or regulatory
CC       subunits determine the substrate specificity of PP1. PPP1R12A,
CC       PPP1R12B and PPP1R12C mediate binding to myosin. PPP1R3A, PPP1R3B,
CC       PPP1R3C and PPP1R3D mediate binding to glycogen. Component of the
CC       MLL5-L complex, at least composed of MLL5, STK38, PPP1CA, PPP1CB,
CC       PPP1CC, HCFC1, ACTB and OGT. Interacts with PPP1R7 and PPP1R12C
CC       (By similarity). PPP1R15A and PPP1R15B mediate binding to EIF2S1.
CC       Part of a complex containing PPP1R15B, PP1 and NCK1/2. Interacts
CC       with PPP1R16B. Component of the PTW/PP1 phosphatase complex,
CC       composed of PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or
CC       PPP1CC. Interacts with PPP1R8 (By similarity).
CC   -!- INTERACTION:
CC       P30282:Ccnd3; NbExp=1; IntAct=EBI-352338, EBI-847337;
CC       P28574:Max; NbExp=1; IntAct=EBI-352338, EBI-1183003;
CC       P13405:Rb1; NbExp=1; IntAct=EBI-352338, EBI-971782;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Nucleus, nucleoplasm (By similarity). Nucleus,
CC       nucleolus (By similarity). Note=Highly mobile in cells and can be
CC       relocalized through interaction with targeting subunits. In the
CC       presence of PPP1R8 relocalizes from the nucleus to nuclear
CC       speckles (By similarity).
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=The things we forget -
CC       Issue 32 of March 2003;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt032.shtml";
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DR   EMBL; M27073; AAA37527.1; -; mRNA.
DR   EMBL; AK004686; BAB23473.1; -; mRNA.
DR   EMBL; AK088893; BAC40636.1; -; mRNA.
DR   EMBL; AK089067; BAC40733.1; -; mRNA.
DR   EMBL; AK147112; BAE27684.1; -; mRNA.
DR   EMBL; AK160743; BAE35984.1; -; mRNA.
DR   EMBL; AK166168; BAE38608.1; -; mRNA.
DR   EMBL; AK166623; BAE38902.1; -; mRNA.
DR   EMBL; AK168141; BAE40108.1; -; mRNA.
DR   EMBL; AK169379; BAE41126.1; -; mRNA.
DR   EMBL; AK171283; BAE42366.1; -; mRNA.
DR   EMBL; BC046832; AAH46832.1; -; mRNA.
DR   IPI; IPI00311873; -.
DR   PIR; D32550; D32550.
DR   RefSeq; NP_766295.2; NM_172707.3.
DR   UniGene; Mm.241931; -.
DR   UniGene; Mm.456635; -.
DR   ProteinModelPortal; P62141; -.
DR   SMR; P62141; 1-308.
DR   IntAct; P62141; 6.
DR   STRING; P62141; -.
DR   PhosphoSite; P62141; -.
DR   PRIDE; P62141; -.
DR   Ensembl; ENSMUST00000015100; ENSMUSP00000015100; ENSMUSG00000014956.
DR   GeneID; 19046; -.
DR   KEGG; mmu:19046; -.
DR   CTD; 19046; -.
DR   MGI; MGI:104871; Ppp1cb.
DR   eggNOG; roNOG09668; -.
DR   HOGENOM; HBG716770; -.
DR   HOVERGEN; HBG000216; -.
DR   InParanoid; P62141; -.
DR   OMA; GLETICL; -.
DR   OrthoDB; EOG4MKNGK; -.
DR   PhylomeDB; P62141; -.
DR   BRENDA; 3.1.3.16; 244.
DR   NextBio; 295509; -.
DR   ArrayExpress; P62141; -.
DR   Bgee; P62141; -.
DR   Genevestigator; P62141; -.
DR   GermOnline; ENSMUSG00000014956; Mus musculus.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0072357; C:PTW/PP1 phosphatase complex; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
DR   InterPro; IPR004843; Metallo-dependent_phosphatase.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR11668; T_phtase_apaH; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Carbohydrate metabolism; Cell cycle; Cell division;
KW   Cytoplasm; Direct protein sequencing; Glycogen metabolism; Hydrolase;
KW   Iron; Manganese; Metal-binding; Nucleus; Phosphoprotein;
KW   Protein phosphatase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    327       Serine/threonine-protein phosphatase PP1-
FT                                beta catalytic subunit.
FT                                /FTId=PRO_0000058780.
FT   ACT_SITE    124    124       Proton donor (By similarity).
FT   METAL        63     63       Iron (By similarity).
FT   METAL        65     65       Iron (By similarity).
FT   METAL        91     91       Iron (By similarity).
FT   METAL        91     91       Manganese (By similarity).
FT   METAL       123    123       Manganese (By similarity).
FT   METAL       172    172       Manganese (By similarity).
FT   METAL       247    247       Manganese (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      41     41       Phosphoserine (By similarity).
FT   MOD_RES      47     47       Phosphoserine (By similarity).
FT   MOD_RES     306    306       Phosphotyrosine (By similarity).
FT   MOD_RES     316    316       Phosphothreonine.
FT   CONFLICT     64     64       I -> N (in Ref. 2; BAC40733).
FT   CONFLICT    148    148       W -> R (in Ref. 2; BAE42366).
FT   CONFLICT    223    223       S -> F (in Ref. 2; BAE38902).
FT   CONFLICT    250    250       V -> E (in Ref. 2; BAB23473).
FT   CONFLICT    269    269       P -> S (in Ref. 2; BAE42366).
SQ   SEQUENCE   327 AA;  37187 MW;  E8356022E9B94ECD CRC64;
     MADGELNVDS LITRLLEVRG CRPGKIVQMT EAEVRGLCIK SREIFLSQPI LLELEAPLKI
     CGDIHGQYTD LLRLFEYGGF PPEANYLFLG DYVDRGKQSL ETICLLLAYK IKYPENFFLL
     RGNHECASIN RIYGFYDECK RRFNIKLWKT FTDCFNCLPI AAIVDEKIFC CHGGLSPDLQ
     SMEQIRRIMR PTDVPDTGLL CDLLWSDPDK DVQGWGENDR GVSFTFGADV VSKFLNRHDL
     DLICRAHQVV EDGYEFFAKR QLVTLFSAPN YCGEFDNAGG MMSVDETLMC SFQILKPSEK
     KAKYQYGGLN SGRPVTPPRT ANPPKKR
//
ID   CALM_MOUSE              Reviewed;         149 AA.
AC   P62204; P02593; P70667; P99014; Q3TEH7; Q3THK5; Q3U6Z5; Q3U7C7;
AC   Q498A3; Q61379; Q61380; Q8BNC9; Q91VQ9; Q9D6G4;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=Calmodulin;
DE            Short=CaM;
GN   Name=Calm1; Synonyms=Calm, Cam, Cam1;
GN   and
GN   Name=Calm2; Synonyms=Cam2, Camb;
GN   and
GN   Name=Calm3; Synonyms=Cam3, Camc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=88257100; PubMed=3384819;
RA   Bender P.K., Dedman J.R., Emerson C.P. Jr.;
RT   "The abundance of calmodulin mRNAs is regulated in phosphorylase
RT   kinase-deficient skeletal muscle.";
RL   J. Biol. Chem. 263:9733-9737(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   MEDLINE=90006775; PubMed=2551780; DOI=10.1016/0378-1119(89)90259-X;
RA   Danchin A., Sezer O., Glaser P., Chalon P., Caput D.;
RT   "Cloning and expression of mouse-brain calmodulin as an activator of
RT   Bordetella pertussis adenylate cyclase in Escherichia coli.";
RL   Gene 80:145-149(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CAST/EiJ; TISSUE=Brain;
RX   PubMed=16670015; DOI=10.1186/1471-2164-7-102;
RA   Farber C.R., Corva P.M., Medrano J.F.;
RT   "Genome-wide isolation of growth and obesity QTL using mouse speed
RT   congenic strains.";
RL   BMC Genomics 7:102-102(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   PubMed=12106288; DOI=10.1111/j.1460-9568.1990.tb00460.x;
RA   Kato K.;
RT   "A collection of cDNA clones with specific expression patterns in
RT   mouse brain.";
RL   Eur. J. Neurosci. 2:704-711(1990).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, DBA/2, and NOD;
RC   TISSUE=Amnion, Bone marrow, Colon, Hippocampus, Kidney, Liver, Lung,
RC   Mammary gland, Ovary, Placenta, Stomach, Testis, Thymus, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129, C57BL/6, and Czech II;
RC   TISSUE=Brain, Mammary tumor, Placenta, and Spinal ganglion;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE,
RP   ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Liver;
RA   Bienvenut W.V.;
RL   Submitted (JUL-2005) to UniProtKB.
RN   [8]
RP   PROTEIN SEQUENCE OF 15-31; 79-87 AND 92-107, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 3-147 IN COMPLEX WITH MYO5A.
RX   PubMed=17151196; DOI=10.1073/pnas.0609436103;
RA   Houdusse A., Gaucher J.F., Krementsova E., Mui S., Trybus K.M.,
RA   Cohen C.;
RT   "Crystal structure of apo-calmodulin bound to the first two IQ motifs
RT   of myosin V reveals essential recognition features.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:19326-19331(2006).
CC   -!- FUNCTION: Calmodulin mediates the control of a large number of
CC       enzymes and other proteins by Ca(2+). Among the enzymes to be
CC       stimulated by the calmodulin-Ca(2+) complex are a number of
CC       protein kinases and phosphatases. Together with CEP110 and
CC       centrin, is involved in a genetic pathway that regulates the
CC       centrosome cycle and progression through cytokinesis (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with CEP97, CEP110, MYO1C, TTN/titin and SRY.
CC       Interacts with RRAD (By similarity). Interacts with USP6; the
CC       interaction is calcium dependent (By similarity). Interacts with
CC       CDK5RAP2 (By similarity).
CC   -!- INTERACTION:
CC       P00533:EGFR (xeno); NbExp=1; IntAct=EBI-397460, EBI-297353;
CC       Q08460:Kcnma1; NbExp=1; IntAct=EBI-397460, EBI-1633915;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. Cytoplasm,
CC       cytoskeleton, spindle pole. Note=Distributed throughout the cell
CC       during interphase, but during mitosis becomes dramatically
CC       localized to the spindle poles and the spindle microtubules (By
CC       similarity).
CC   -!- PTM: Ubiquitination results in a strongly decreased activity (By
CC       similarity).
CC   -!- PTM: Phosphorylation results in a decreased activity (By
CC       similarity).
CC   -!- MISCELLANEOUS: This protein has four functional calcium-binding
CC       sites.
CC   -!- SIMILARITY: Belongs to the calmodulin family.
CC   -!- SIMILARITY: Contains 4 EF-hand domains.
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DR   EMBL; M19380; AAA66181.1; -; mRNA.
DR   EMBL; M19381; AAA66182.1; -; mRNA.
DR   EMBL; L31642; AAA65934.1; -; mRNA.
DR   EMBL; M27844; AAA37365.1; -; Genomic_DNA.
DR   EMBL; AY902353; AAY21063.1; -; Genomic_DNA.
DR   EMBL; X61432; CAA43674.1; -; mRNA.
DR   EMBL; AK004673; BAB23462.1; -; mRNA.
DR   EMBL; AK012247; BAB28116.1; -; mRNA.
DR   EMBL; AK012564; BAB28319.1; -; mRNA.
DR   EMBL; AK013068; BAB28631.1; -; mRNA.
DR   EMBL; AK013695; BAB28959.1; -; mRNA.
DR   EMBL; AK083996; BAC39089.2; -; mRNA.
DR   EMBL; AK088141; BAC40168.1; -; mRNA.
DR   EMBL; AK150288; BAE29443.1; -; mRNA.
DR   EMBL; AK150978; BAE30007.1; -; mRNA.
DR   EMBL; AK151001; BAE30025.1; -; mRNA.
DR   EMBL; AK151552; BAE30497.1; -; mRNA.
DR   EMBL; AK151610; BAE30549.1; -; mRNA.
DR   EMBL; AK151784; BAE30686.1; -; mRNA.
DR   EMBL; AK151923; BAE30801.1; -; mRNA.
DR   EMBL; AK151992; BAE30856.1; -; mRNA.
DR   EMBL; AK152148; BAE30984.1; -; mRNA.
DR   EMBL; AK152303; BAE31109.1; -; mRNA.
DR   EMBL; AK152715; BAE31439.1; -; mRNA.
DR   EMBL; AK152719; BAE31442.1; -; mRNA.
DR   EMBL; AK152754; BAE31469.1; -; mRNA.
DR   EMBL; AK152850; BAE31543.1; -; mRNA.
DR   EMBL; AK152897; BAE31579.1; -; mRNA.
DR   EMBL; AK153004; BAE31644.1; -; mRNA.
DR   EMBL; AK153179; BAE31782.1; -; mRNA.
DR   EMBL; AK153348; BAE31924.1; -; mRNA.
DR   EMBL; AK153426; BAE31985.1; -; mRNA.
DR   EMBL; AK153546; BAE32083.1; -; mRNA.
DR   EMBL; AK159762; BAE35353.1; -; mRNA.
DR   EMBL; AK160057; BAE35595.1; -; mRNA.
DR   EMBL; AK160508; BAE35832.1; -; mRNA.
DR   EMBL; AK160636; BAE35930.1; -; mRNA.
DR   EMBL; AK161268; BAE36280.1; -; mRNA.
DR   EMBL; AK161302; BAE36309.1; -; mRNA.
DR   EMBL; AK161984; BAE36667.1; -; mRNA.
DR   EMBL; AK162314; BAE36849.1; -; mRNA.
DR   EMBL; AK166308; BAE38695.1; -; mRNA.
DR   EMBL; AK167353; BAE39452.1; -; mRNA.
DR   EMBL; AK168002; BAE39990.1; -; mRNA.
DR   EMBL; AK168241; BAE40191.1; -; mRNA.
DR   EMBL; AK168663; BAE40516.1; -; mRNA.
DR   EMBL; AK168741; BAE40582.1; -; mRNA.
DR   EMBL; AK168803; BAE40633.1; -; mRNA.
DR   EMBL; AK169027; BAE40819.1; -; mRNA.
DR   EMBL; AK169055; BAE40843.1; -; mRNA.
DR   EMBL; AK169640; BAE41271.1; -; mRNA.
DR   EMBL; BC010730; AAH10730.1; -; mRNA.
DR   EMBL; BC021347; AAH21347.1; -; mRNA.
DR   EMBL; BC050926; AAH50926.1; -; mRNA.
DR   EMBL; BC051444; AAH51444.1; -; mRNA.
DR   EMBL; BC054805; AAH54805.1; -; mRNA.
DR   EMBL; BC100301; AAI00302.1; -; mRNA.
DR   IPI; IPI00761696; -.
DR   PIR; I49567; I49567.
DR   PIR; S37707; S37707.
DR   RefSeq; NP_031615.1; NM_007589.5.
DR   RefSeq; NP_031616.1; NM_007590.3.
DR   RefSeq; NP_033920.1; NM_009790.4.
DR   UniGene; Mm.285993; -.
DR   UniGene; Mm.288630; -.
DR   UniGene; Mm.329243; -.
DR   PDB; 2DFS; EM; 24.00 A; B/C/D/E/F/G/N/O/P/Q/R/S=2-148.
DR   PDB; 2IX7; X-ray; 2.50 A; A/B=3-147.
DR   PDBsum; 2DFS; -.
DR   PDBsum; 2IX7; -.
DR   ProteinModelPortal; P62204; -.
DR   SMR; P62204; 2-148.
DR   IntAct; P62204; 19.
DR   STRING; P62204; -.
DR   PhosphoSite; P62204; -.
DR   SWISS-2DPAGE; P62204; -.
DR   REPRODUCTION-2DPAGE; P62204; -.
DR   PRIDE; P62204; -.
DR   Ensembl; ENSMUST00000019514; ENSMUSP00000019514; ENSMUSG00000019370.
DR   Ensembl; ENSMUST00000040440; ENSMUSP00000048857; ENSMUSG00000036438.
DR   Ensembl; ENSMUST00000110082; ENSMUSP00000105709; ENSMUSG00000001175.
DR   GeneID; 12313; -.
DR   GeneID; 12314; -.
DR   GeneID; 12315; -.
DR   KEGG; mmu:12313; -.
DR   KEGG; mmu:12314; -.
DR   KEGG; mmu:12315; -.
DR   UCSC; uc007osq.1; mouse.
DR   CTD; 12313; -.
DR   CTD; 12314; -.
DR   CTD; 12315; -.
DR   MGI; MGI:88251; Calm1.
DR   MGI; MGI:103250; Calm2.
DR   MGI; MGI:103249; Calm3.
DR   eggNOG; roNOG04065; -.
DR   GeneTree; ENSGT00560000076590; -.
DR   HOVERGEN; HBG012180; -.
DR   InParanoid; P62204; -.
DR   OMA; ESELTDM; -.
DR   OrthoDB; EOG4001KK; -.
DR   PhylomeDB; P62204; -.
DR   NextBio; 280868; -.
DR   ArrayExpress; P62204; -.
DR   Bgee; P62204; -.
DR   CleanEx; MM_CALM1; -.
DR   CleanEx; MM_CALM2; -.
DR   CleanEx; MM_CALM3; -.
DR   Genevestigator; P62204; -.
DR   GermOnline; ENSMUSG00000001175; Mus musculus.
DR   GermOnline; ENSMUSG00000019370; Mus musculus.
DR   GermOnline; ENSMUSG00000036438; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   InterPro; IPR018248; EF-hand.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR001125; Recoverin.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   Pfam; PF00036; efhand; 4.
DR   PRINTS; PR00450; RECOVERIN.
DR   SMART; SM00054; EFh; 4.
DR   PROSITE; PS00018; EF_HAND_1; 4.
DR   PROSITE; PS50222; EF_HAND_2; 4.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Calcium; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Isopeptide bond; Methylation;
KW   Phosphoprotein; Repeat; Ubl conjugation.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    149       Calmodulin.
FT                                /FTId=PRO_0000198224.
FT   DOMAIN        8     43       EF-hand 1.
FT   DOMAIN       44     79       EF-hand 2.
FT   DOMAIN       81    116       EF-hand 3.
FT   DOMAIN      117    149       EF-hand 4.
FT   CA_BIND      21     32       1.
FT   CA_BIND      57     68       2.
FT   CA_BIND      94    105       3.
FT   CA_BIND     130    141       4.
FT   MOD_RES       2      2       N-acetylalanine.
FT   MOD_RES      14     14       N6-acetyllysine (By similarity).
FT   MOD_RES      22     22       N6-acetyllysine (By similarity).
FT   MOD_RES      45     45       Phosphothreonine; by CaMK4 (By
FT                                similarity).
FT   MOD_RES      95     95       N6-acetyllysine (By similarity).
FT   MOD_RES     100    100       Phosphotyrosine.
FT   MOD_RES     116    116       N6,N6,N6-trimethyllysine (By similarity).
FT   MOD_RES     139    139       Phosphotyrosine (By similarity).
FT   CROSSLNK     22     22       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CONFLICT     26     26       G -> N (in Ref. 1; AAA66182).
FT   CONFLICT     55     55       E -> V (in Ref. 5; BAE41271).
FT   CONFLICT     69     69       F -> L (in Ref. 5; BAE40191).
FT   CONFLICT     82     82       S -> G (in Ref. 5; BAE31439/BAE31644/
FT                                BAE31442).
FT   CONFLICT    126    126       I -> T (in Ref. 5; BAE31579).
FT   CONFLICT    142    142       F -> S (in Ref. 5; BAC39089).
FT   CONFLICT    143    143       V -> L (in Ref. 5; BAB28959).
FT   HELIX         7     20
FT   STRAND       24     29
FT   HELIX        30     32
FT   HELIX        33     39
FT   HELIX        46     54
FT   STRAND       63     65
FT   HELIX        66     78
FT   HELIX        83     91
FT   HELIX       103    112
FT   STRAND      113    115
FT   HELIX       119    128
FT   STRAND      135    137
FT   HELIX       139    145
SQ   SEQUENCE   149 AA;  16838 MW;  6B4BC3FCDE10727B CRC64;
     MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
     NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE
     EVDEMIREAD IDGDGQVNYE EFVQMMTAK
//
ID   RS8_MOUSE               Reviewed;         208 AA.
AC   P62242; P09058; Q8C2G6;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=40S ribosomal protein S8;
GN   Name=Rps8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Spleen;
RX   MEDLINE=94051615; PubMed=7694236; DOI=10.1093/nar/21.20.4845;
RA   Su Y., Raj N.B.K., Au W.-C., Pitha P.M.;
RT   "Primary sequence of the mouse ribosomal protein S8.";
RL   Nucleic Acids Res. 21:4845-4845(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Liver, Thymus, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C3H/He, and C57BL/6; TISSUE=Brain, Colon, and Osteoblast;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBUNIT: Identified in a mRNP granule complex, at least composed
CC       of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD,
CC       HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1,
CC       NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8,
CC       RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=Localized in
CC       cytoplasmic mRNP granules containing untranslated mRNAs (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the ribosomal protein S8e family.
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DR   EMBL; X73829; CAA52050.1; -; mRNA.
DR   EMBL; AK009023; BAB26032.1; -; mRNA.
DR   EMBL; AK010650; BAB27090.1; -; mRNA.
DR   EMBL; AK011048; BAB27359.1; -; mRNA.
DR   EMBL; AK011058; BAB27366.1; -; mRNA.
DR   EMBL; AK011642; BAB27754.1; -; mRNA.
DR   EMBL; AK012435; BAB28236.1; -; mRNA.
DR   EMBL; AK012665; BAB28394.1; -; mRNA.
DR   EMBL; AK088660; BAC40485.1; -; mRNA.
DR   EMBL; BC027217; AAH27217.1; -; mRNA.
DR   EMBL; BC051446; AAH51446.1; -; mRNA.
DR   EMBL; BC081465; AAH81465.1; -; mRNA.
DR   IPI; IPI00466820; -.
DR   PIR; S42110; S42110.
DR   RefSeq; NP_033124.1; NM_009098.2.
DR   RefSeq; XP_001474155.1; XM_001474105.2.
DR   UniGene; Mm.260904; -.
DR   UniGene; Mm.338718; -.
DR   ProteinModelPortal; P62242; -.
DR   STRING; P62242; -.
DR   PhosphoSite; P62242; -.
DR   PRIDE; P62242; -.
DR   Ensembl; ENSMUST00000061609; ENSMUSP00000060468; ENSMUSG00000047675.
DR   Ensembl; ENSMUST00000102696; ENSMUSP00000099757; ENSMUSG00000047675.
DR   GeneID; 100040298; -.
DR   GeneID; 20116; -.
DR   KEGG; mmu:100040298; -.
DR   KEGG; mmu:20116; -.
DR   CTD; 20116; -.
DR   MGI; MGI:98166; Rps8.
DR   eggNOG; roNOG06439; -.
DR   HOGENOM; HBG745393; -.
DR   HOVERGEN; HBG030738; -.
DR   InParanoid; P62242; -.
DR   OrthoDB; EOG402WT3; -.
DR   PhylomeDB; P62242; -.
DR   NextBio; 448513; -.
DR   Bgee; P62242; -.
DR   CleanEx; MM_RPS8; -.
DR   Genevestigator; P62242; -.
DR   GermOnline; ENSMUSG00000047675; Mus musculus.
DR   GermOnline; ENSMUSG00000070446; Mus musculus.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR001047; Ribosomal_S8e.
DR   InterPro; IPR022309; Ribosomal_S8e/biogenesis_NSA2.
DR   InterPro; IPR018283; Ribosomal_S8e_CS.
DR   Pfam; PF01201; Ribosomal_S8e; 1.
DR   TIGRFAMs; TIGR00307; S8e; 1.
DR   PROSITE; PS01193; RIBOSOMAL_S8E; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    208       40S ribosomal protein S8.
FT                                /FTId=PRO_0000122241.
FT   MOD_RES     130    130       Phosphothreonine (By similarity).
FT   MOD_RES     160    160       Phosphoserine.
FT   CONFLICT     70     70       E -> V (in Ref. 2; BAC40485).
SQ   SEQUENCE   208 AA;  24205 MW;  407FDF59171F7422 CRC64;
     MGISRDNWHK RRKTGGKRKP YHKKRKYELG RPAANTKIGP RRIHTVRVRG GNKKYRALRL
     DVGNFSWGSE CCTRKTRIID VVYNASNNEL VRTKTLVKNC IVLIDSTPYR QWYESHYALP
     LGRKKGAKLT PEEEEILNKK RSKKIQKKYD ERKKNAKISS LLEEQFQQGK LLACIASRPG
     QCGRADGYVL EGKELEFYLR KIKARKGK
//
ID   1433E_MOUSE             Reviewed;         255 AA.
AC   P62259; P29360; P42655; Q63631;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=14-3-3 protein epsilon;
DE            Short=14-3-3E;
GN   Name=Ywhae;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=Swiss; TISSUE=Kidney;
RX   MEDLINE=95269876; PubMed=7750640; DOI=10.1006/dbio.1995.1139;
RA   McConnell J.E., Armstrong J.F., Bard J.B.;
RT   "The mouse 14-3-3 epsilon isoform, a kinase regulator whose expression
RT   pattern is modulated in mesenchyme and neuronal differentiation.";
RL   Dev. Biol. 169:218-228(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/Sv;
RA   Takihara Y., Irie K., Nomura M., Motaleb M., Matsumoto K., Shimada K.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ILS, and ISS;
RX   MEDLINE=21363810; PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 131-141; 154-170 AND 197-215, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Friebe K., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [6]
RP   INTERACTION WITH RGNEF.
RX   PubMed=11533041; DOI=10.1074/jbc.M107709200;
RA   Zhai J., Lin H., Shamim M., Schlaepfer W.W., Canete-Soler R.;
RT   "Identification of a novel interaction of 14-3-3 with p190RhoGEF.";
RL   J. Biol. Chem. 276:41318-41324(2001).
RN   [7]
RP   INTERACTION WITH NDEL1.
RX   PubMed=12796778; DOI=10.1038/ng1169;
RA   Toyo-oka K., Shionoya A., Gambello M.J., Cardoso C., Leventer R.,
RA   Ward H.L., Ayala R., Tsai L.-H., Dobyns W., Ledbetter D.,
RA   Hirotsune S., Wynshaw-Boris A.;
RT   "14-3-3epsilon is important for neuronal migration by binding to
RT   NUDEL: a molecular explanation for Miller-Dieker syndrome.";
RL   Nat. Genet. 34:274-285(2003).
RN   [8]
RP   INTERACTION WITH GRB10.
RX   PubMed=15722337; DOI=10.1074/jbc.M501477200;
RA   Urschel S., Bassermann F., Bai R.Y., Munch S., Peschel C., Duyster J.;
RT   "Phosphorylation of grb10 regulates its interaction with 14-3-3.";
RL   J. Biol. Chem. 280:16987-16993(2005).
RN   [9]
RP   INTERACTION WITH TIAM2.
RX   PubMed=17320046; DOI=10.1016/j.bbrc.2007.02.028;
RA   Takefuji M., Mori K., Morita Y., Arimura N., Nishimura T.,
RA   Nakayama M., Hoshino M., Iwamatsu A., Murohara T., Kaibuchi K.,
RA   Amano M.;
RT   "Rho-kinase modulates the function of STEF, a Rac GEF, through its
RT   phosphorylation.";
RL   Biochem. Biophys. Res. Commun. 355:788-794(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC       spectrum of both general and specialized signaling pathway. Binds
CC       to a large number of partners, usually by recognition of a
CC       phosphoserine or phosphothreonine motif. Binding generally results
CC       in the modulation of the activity of the binding partner.
CC   -!- SUBUNIT: Homodimer. Heterodimerizes with YWHAZ (By similarity).
CC       Interacts with NDEL1, RGNEF and TIAM2. Interacts with ABL1
CC       (phosphorylated form); the interaction retains it in the
CC       cytoplasm. Weakly interacts with CDKN1B. Interacts with GAB2 (By
CC       similarity). Interacts with phosphorylated GRB10.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Melanosome (By
CC       similarity).
CC   -!- DEVELOPMENTAL STAGE: In the E8.5 embryo, expressed throughout the
CC       embryo. Within a day, expression was more marked in mesenchyme
CC       than elsewhere (e.g., epithelial tissue, where it was generally
CC       low), although levels in neural tissue rose again by about E12.5.
CC       This difference was maintained until E15.5 when expression levels
CC       started to drop in most tissues, with those of the nervous system,
CC       tooth, and kidney being exceptions. Strongly expressed in early
CC       mesenchyme. The expression decreased as the mesenchyme
CC       differentiated.
CC   -!- SIMILARITY: Belongs to the 14-3-3 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; Z19599; CAA79659.1; -; mRNA.
DR   EMBL; D87663; BAA13424.1; -; mRNA.
DR   EMBL; AF483478; AAL90752.1; -; mRNA.
DR   EMBL; AF483479; AAL90753.1; -; mRNA.
DR   EMBL; BC058686; AAH58686.1; -; mRNA.
DR   IPI; IPI00118384; -.
DR   PIR; I48337; S31975.
DR   RefSeq; NP_033562.3; NM_009536.4.
DR   UniGene; Mm.234700; -.
DR   ProteinModelPortal; P62259; -.
DR   SMR; P62259; 3-232.
DR   IntAct; P62259; 10.
DR   MINT; MINT-209058; -.
DR   STRING; P62259; -.
DR   PhosphoSite; P62259; -.
DR   REPRODUCTION-2DPAGE; P62259; -.
DR   PRIDE; P62259; -.
DR   Ensembl; ENSMUST00000067664; ENSMUSP00000070993; ENSMUSG00000020849.
DR   GeneID; 22627; -.
DR   KEGG; mmu:22627; -.
DR   CTD; 22627; -.
DR   MGI; MGI:894689; Ywhae.
DR   eggNOG; roNOG07685; -.
DR   HOGENOM; HBG611720; -.
DR   HOVERGEN; HBG050423; -.
DR   InParanoid; P62259; -.
DR   OMA; HESNTIV; -.
DR   OrthoDB; EOG4HHP34; -.
DR   PhylomeDB; P62259; -.
DR   ArrayExpress; P62259; -.
DR   Bgee; P62259; -.
DR   Genevestigator; P62259; -.
DR   GermOnline; ENSMUSG00000020849; Mus musculus.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; IDA:MGI.
DR   GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR   GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR   GO; GO:0035308; P:negative regulation of protein dephosphorylation; IDA:MGI.
DR   GO; GO:0001764; P:neuron migration; IGI:MGI.
DR   GO; GO:0006605; P:protein targeting; IDA:MGI.
DR   InterPro; IPR000308; 14-3-3.
DR   PANTHER; PTHR18860; 14-3-3; 1.
DR   PIRSF; PIRSF000868; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Phosphoprotein.
FT   CHAIN         1    255       14-3-3 protein epsilon.
FT                                /FTId=PRO_0000058619.
FT   SITE         57     57       Interaction with phosphoserine on
FT                                interacting protein (By similarity).
FT   SITE        130    130       Interaction with phosphoserine on
FT                                interacting protein (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      38     38       Phosphothreonine (By similarity).
FT   MOD_RES      50     50       N6-acetyllysine (By similarity).
FT   MOD_RES      69     69       N6-acetyllysine (By similarity).
FT   MOD_RES     118    118       N6-acetyllysine (By similarity).
FT   MOD_RES     123    123       N6-acetyllysine (By similarity).
FT   MOD_RES     210    210       Phosphoserine.
SQ   SEQUENCE   255 AA;  29174 MW;  07817CCBD1F75B26 CRC64;
     MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW
     RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF
     YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF
     YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE
     EQNKEALQDV EDENQ
//
ID   ARF6_MOUSE              Reviewed;         175 AA.
AC   P62331; P26438;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=ADP-ribosylation factor 6;
GN   Name=Arf6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=97103475; PubMed=8947846;
RA   Hosaka M., Toda K., Takatsu H., Torii S., Murakami K., Nakayama K.;
RT   "Structure and intracellular localization of mouse ADP-ribosylation
RT   factors type 1 to type 6 (ARF1-ARF6).";
RL   J. Biochem. 120:813-819(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION AS REGULATOR OF DENDRITIC SPINE DEVELOPMENT.
RX   PubMed=16325184; DOI=10.1016/j.febslet.2005.11.022;
RA   Miyazaki H., Yamazaki M., Watanabe H., Maehama T., Yokozeki T.,
RA   Kanaho Y.;
RT   "The small GTPase ADP-ribosylation factor 6 negatively regulates
RT   dendritic spine formation.";
RL   FEBS Lett. 579:6834-6838(2005).
CC   -!- FUNCTION: GTP-binding protein involved in protein trafficking;
CC       regulates endocytic recycling and cytoskeleton remodeling. May
CC       modulate vesicle budding and uncoating within the Golgi apparatus
CC       (By similarity). Involved in the regulation of dendritic spine
CC       development.
CC   -!- SUBUNIT: Interacts with ARHGAP21, ASAP2, HERC1, PIP5K1C and UACA
CC       (By similarity). Interacts with NCS1/FREQ at the plasma membrane.
CC       Interacts with RAB11FIP3 and RAB11FIP4 (By similarity). Interacts
CC       with USP6 (via Rab-GAP TBC domain) (By similarity). Interacts with
CC       ECM29 (By similarity). Interacts with TBC1D24 (By similarity).
CC   -!- INTERACTION:
CC       P21283:ATP6V1C1 (xeno); NbExp=1; IntAct=EBI-988682, EBI-988663;
CC       Q9Z1G3:Atp6v1c1; NbExp=1; IntAct=EBI-988682, EBI-772679;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus (By similarity). Cell
CC       membrane; Lipid-anchor (By similarity). Endosome membrane; Lipid-
CC       anchor (By similarity). Cell membrane (By similarity).
CC       Note=Recruited to the cell membrane in association with CYTH2 and
CC       ARL4C (By similarity).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D87903; BAA13495.1; -; mRNA.
DR   EMBL; BC003478; AAH03478.1; -; mRNA.
DR   EMBL; BC083112; AAH83112.1; -; mRNA.
DR   IPI; IPI00221616; -.
DR   PIR; JC4950; JC4950.
DR   RefSeq; NP_031507.1; NM_007481.3.
DR   UniGene; Mm.27308; -.
DR   ProteinModelPortal; P62331; -.
DR   SMR; P62331; 2-174.
DR   IntAct; P62331; 2.
DR   STRING; P62331; -.
DR   PhosphoSite; P62331; -.
DR   PRIDE; P62331; -.
DR   Ensembl; ENSMUST00000050063; ENSMUSP00000055862; ENSMUSG00000044147.
DR   GeneID; 11845; -.
DR   KEGG; mmu:11845; -.
DR   UCSC; uc007nsj.1; mouse.
DR   CTD; 11845; -.
DR   MGI; MGI:99435; Arf6.
DR   eggNOG; roNOG04284; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG002073; -.
DR   InParanoid; P62331; -.
DR   OMA; WLTSNHK; -.
DR   OrthoDB; EOG4GQQ62; -.
DR   PhylomeDB; P62331; -.
DR   NextBio; 279803; -.
DR   ArrayExpress; P62331; -.
DR   Bgee; P62331; -.
DR   CleanEx; MM_ARF6; -.
DR   Genevestigator; P62331; -.
DR   GermOnline; ENSMUSG00000044147; Mus musculus.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; TAS:MGI.
DR   GO; GO:0006915; P:apoptosis; IMP:MGI.
DR   GO; GO:0001889; P:liver development; IMP:MGI.
DR   GO; GO:0015031; P:protein transport; TAS:MGI.
DR   GO; GO:0060998; P:regulation of dendritic spine development; IMP:UniProtKB.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   InterPro; IPR006688; ARF.
DR   InterPro; IPR006689; ARF/SAR.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   PANTHER; PTHR11711; ARF/SAR; 1.
DR   Pfam; PF00025; Arf; 1.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00177; ARF; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51417; ARF; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Endosome; ER-Golgi transport; Golgi apparatus;
KW   GTP-binding; Lipoprotein; Membrane; Myristate; Nucleotide-binding;
KW   Protein transport; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    175       ADP-ribosylation factor 6.
FT                                /FTId=PRO_0000207401.
FT   NP_BIND      20     27       GTP (By similarity).
FT   NP_BIND      63     67       GTP (By similarity).
FT   NP_BIND     122    125       GTP (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
SQ   SEQUENCE   175 AA;  20082 MW;  49E38E59AEA52B98 CRC64;
     MGKVLSKIFG NKEMRILMLG LDAAGKTTIL YKLKLGQSVT TIPTVGFNVE TVTYKNVKFN
     VWDVGGQDKI RPLWRHYYTG TQGLIFVVDC ADRDRIDEAR QELHRIINDR EMRDAIILIF
     ANKQDLPDAM KPHEIQEKLG LTRIRDRNWY VQPSCATSGD GLYEGLTWLT SNYKS
//
ID   KCAB2_MOUSE             Reviewed;         367 AA.
AC   P62482; P97381; Q60942; Q64284;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Voltage-gated potassium channel subunit beta-2;
DE   AltName: Full=K(+) channel subunit beta-2;
DE   AltName: Full=Kv-beta-2;
DE   AltName: Full=Neuroimmune protein F5;
GN   Name=Kcnab2; Synonyms=Ckbeta2, I2rf5, Kcnb3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Fibroblast;
RX   MEDLINE=96161969; PubMed=8576199; DOI=10.1074/jbc.271.5.2406;
RA   Uebele V.N., England S.K., Chaudhary A., Tamkun M.M., Snyders D.J.;
RT   "Functional differences in Kv1.5 currents expressed in mammalian cell
RT   lines are due to the presence of endogenous Kv beta 2.1 subunits.";
RL   J. Biol. Chem. 271:2406-2412(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain cortex;
RX   MEDLINE=96421640; PubMed=8824288; DOI=10.1074/jbc.271.42.26341;
RA   Fink M., Duprat F., Lesage F., Heurteaux C., Romey G., Barhanin J.,
RA   Lazdunski M.;
RT   "A new K+ channel beta subunit to specifically enhance Kv2.2 (CDRK)
RT   expression.";
RL   J. Biol. Chem. 271:26341-26348(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=C57BL/6N; TISSUE=Brain, and T-cell;
RX   MEDLINE=92243514; PubMed=1573677; DOI=10.1002/jnr.490310208;
RA   Cohen J.A., Arai M., Prak E.L., Brooks S.A., Young L.H.,
RA   Prystowsky M.B.;
RT   "Characterization of a novel mRNA expressed by neurons in mature
RT   brain.";
RL   J. Neurosci. Res. 31:273-284(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; TYR-25 AND TYR-360,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Accessory potassium channel protein which modulates the
CC       activity of the pore-forming alpha subunit.
CC   -!- SUBUNIT: Forms heteromultimeric complex with alpha subunits. Forms
CC       a ternary complex with SQSTM1 and PRKCZ (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- TISSUE SPECIFICITY: Strongest expression in brain and eye. Highest
CC       levels in brain detected in brainstem and diencephalon. Strong
CC       expression also detected in lung and heart. Moderate expression in
CC       kidney, T-lymphocytes and skeletal muscle.
CC   -!- DEVELOPMENTAL STAGE: Not detected prior to birth, low levels of
CC       expression detected from postnatal days 1 to 7. Expression reaches
CC       adult levels by postnatal day 21.
CC   -!- DOMAIN: Alteration of functional properties of alpha subunit is
CC       mediated through N-terminal domain of beta subunit (Probable).
CC   -!- PTM: Phosphorylated by PRKCZ; may be regulated by incorporation in
CC       a complex composed of PRKCZ and SQSTM1 (By similarity).
CC   -!- SIMILARITY: Belongs to the shaker potassium channel beta subunit
CC       family.
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DR   EMBL; L48983; AAB00829.1; -; mRNA.
DR   EMBL; U65592; AAB37263.1; -; mRNA.
DR   EMBL; U31908; AAA75174.1; -; mRNA.
DR   EMBL; BC039178; AAH39178.1; -; mRNA.
DR   IPI; IPI00315359; -.
DR   RefSeq; NP_034728.2; NM_010598.2.
DR   UniGene; Mm.388924; -.
DR   ProteinModelPortal; P62482; -.
DR   SMR; P62482; 36-361.
DR   MINT; MINT-138568; -.
DR   STRING; P62482; -.
DR   PhosphoSite; P62482; -.
DR   PRIDE; P62482; -.
DR   Ensembl; ENSMUST00000030768; ENSMUSP00000030768; ENSMUSG00000028931.
DR   Ensembl; ENSMUST00000105648; ENSMUSP00000101273; ENSMUSG00000028931.
DR   GeneID; 16498; -.
DR   KEGG; mmu:16498; -.
DR   UCSC; uc008wal.1; mouse.
DR   CTD; 16498; -.
DR   MGI; MGI:109239; Kcnab2.
DR   eggNOG; roNOG11033; -.
DR   HOGENOM; HBG605727; -.
DR   HOVERGEN; HBG052216; -.
DR   InParanoid; P62482; -.
DR   OMA; IAEQAEY; -.
DR   OrthoDB; EOG476K0F; -.
DR   PhylomeDB; P62482; -.
DR   NextBio; 289815; -.
DR   ArrayExpress; P62482; -.
DR   Bgee; P62482; -.
DR   Genevestigator; P62482; -.
DR   GermOnline; ENSMUSG00000028931; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0044224; C:juxtaparanode region of axon; IDA:BHF-UCL.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:InterPro.
DR   InterPro; IPR001395; Aldo/ket_red.
DR   InterPro; IPR005983; K_chnl_volt-dep_bsu_KCNAB.
DR   InterPro; IPR005399; K_chnl_volt-dep_bsu_KCNAB-rel.
DR   InterPro; IPR005401; K_chnl_volt-dep_bsu_KCNAB2.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   Gene3D; G3DSA:3.20.20.100; Aldo/ket_red; 1.
DR   PANTHER; PTHR11732; Aldo/ket_red; 1.
DR   PANTHER; PTHR11732:SF14; KCNAB_channel; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PRINTS; PR01579; KCNAB2CHANEL.
DR   PRINTS; PR01577; KCNABCHANNEL.
DR   SUPFAM; SSF51430; Aldo/ket_red; 1.
DR   TIGRFAMs; TIGR01293; Kv_beta; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Ion transport; Ionic channel; NADP;
KW   Phosphoprotein; Potassium; Potassium transport; Transport;
KW   Voltage-gated channel.
FT   CHAIN         1    367       Voltage-gated potassium channel subunit
FT                                beta-2.
FT                                /FTId=PRO_0000148747.
FT   NP_BIND      56     57       NADP (By similarity).
FT   NP_BIND     188    189       NADP (By similarity).
FT   NP_BIND     243    248       NADP (By similarity).
FT   NP_BIND     323    329       NADP (By similarity).
FT   BINDING      63     63       NADP (By similarity).
FT   BINDING      85     85       NADP (By similarity).
FT   BINDING      90     90       NADP (By similarity).
FT   BINDING     214    214       NADP (By similarity).
FT   BINDING     254    254       NADP (By similarity).
FT   MOD_RES       9      9       Phosphoserine.
FT   MOD_RES      20     20       Phosphoserine.
FT   MOD_RES      25     25       Phosphotyrosine.
FT   MOD_RES     124    124       N6-acetyllysine (By similarity).
FT   MOD_RES     360    360       Phosphotyrosine.
FT   CONFLICT     64     64       I -> L (in Ref. 2; AAB37263).
FT   CONFLICT     99    100       LG -> FR (in Ref. 3; AAA75174).
FT   CONFLICT    202    202       A -> G (in Ref. 2; AAB37263).
FT   CONFLICT    266    266       S -> L (in Ref. 3; AAA75174).
SQ   SEQUENCE   367 AA;  41021 MW;  5303FD1411B324FC CRC64;
     MYPESTTGSP ARLSLRQTGS PGMIYSTRYG SPKRQLQFYR NLGKSGLRVS CLGLGTWVTF
     GGQITDEMAE HLMTLAYDNG INLFDTAEVY AAGKAEVVLG NIIKKKGWRR SSLVITTKIF
     WGGKAETERG LSRKHIIEGL KASLERLQLE YVDVVFANRP DPNTPMEETV RAMTHVINQG
     MAMYWGTSRW SSMEIMEAYS VARQFNLIPP ICEQAEYHMF QREKVEVQLP ELFHKIGVGA
     MTWSPLACGI VSGKYDSGIP PYSRASLKGY QWLKDKILSE EGRRQQAKLK ELQAIAERLG
     CTLPQLAIAW CLRNEGVSSV LLGASNAEQL MENIGAIQVL PKLSSSIVHE IDSILGNKPY
     SKKDYRS
//
ID   ABI2_MOUSE              Reviewed;         446 AA.
AC   P62484; Q6PHU3;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Abl interactor 2;
DE   AltName: Full=Abelson interactor 2;
DE            Short=Abi-2;
GN   Name=Abi2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11516653; DOI=10.1016/S0960-9822(01)00239-1;
RA   Stradal T.E.B., Courtney K.D., Rottner K., Hahne P., Small J.V.,
RA   Pendergast A.M.;
RT   "The Abl interactor proteins localize to sites of actin polymerization
RT   at the tips of lamellipodia and filopodia.";
RL   Curr. Biol. 11:891-895(2001).
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15143189; DOI=10.1128/MCB.24.11.4979-4993.2004;
RA   Echarri A., Lai M.J., Robinson M.R., Pendergast A.M.;
RT   "Abl interactor 1 (Abi-1) wave-binding and SNARE domains regulate its
RT   nucleocytoplasmic shuttling, lamellipodium localization, and wave-1
RT   levels.";
RL   Mol. Cell. Biol. 24:4979-4993(2004).
RN   [4]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=10995551; DOI=10.1006/mcne.2000.0865;
RA   Courtney K.D., Grove M., Vandongen H., Vandongen A., LaMantia A.-S.,
RA   Pendergast A.M.;
RT   "Localization and phosphorylation of Abl-interactor proteins, Abi-1
RT   and Abi-2, in the developing nervous system.";
RL   Mol. Cell. Neurosci. 16:244-257(2000).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-395, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: May act in regulation of cell growth and transformation
CC       by interacting with nonreceptor tyrosine kinases ABL1 and/or ABL2.
CC       May be involved in cytoskeletal reorganization. Regulates ABL1/c-
CC       Abl-mediated phosphorylation of MENA.
CC   -!- SUBUNIT: Component of the WAVE1 complex composed of ABI2, CYFIP2,
CC       C3orf10/HSPC300, NCKAP1 and WASF1/WAVE1. CYFIP2 binds to activated
CC       RAC1 which causes the complex to dissociate, releasing activated
CC       WASF1. The complex can also be activated by NCK1 (By similarity).
CC       Interacts with ABL1 and ABL2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell projection, lamellipodium.
CC       Cell projection, filopodium. Cytoplasm, cytoskeleton.
CC       Note=Localized to protruding lamellipodia and filopodia tips.
CC   -!- TISSUE SPECIFICITY: Expresses in embryonic and adult brain. In
CC       adult brain prominently expressed in the neocortex, hippocampus
CC       and dentate gyrus.
CC   -!- DEVELOPMENTAL STAGE: Detected at E10 in developing brain, and
CC       expression is more prominent in the neuroepithelium compared to
CC       the surrounding tissue. At E12 expression is enhanced throughout
CC       the CNS and is detected along the full length of the spinal chord.
CC       At E16 expression remains enhanced in the CNS, and is particularly
CC       prominent in the olfactory bulb. Also highly expressed in dorsal
CC       root ganglia.
CC   -!- PTM: Is a substrate for ABL1 (By similarity).
CC   -!- SIMILARITY: Belongs to the ABI family.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain.
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DR   EMBL; BC056345; AAH56345.1; -; mRNA.
DR   IPI; IPI00380956; -.
DR   RefSeq; NP_001185499.1; NM_001198570.1.
DR   RefSeq; NP_001185500.1; NM_001198571.1.
DR   RefSeq; NP_937760.1; NM_198127.2.
DR   UniGene; Mm.212066; -.
DR   ProteinModelPortal; P62484; -.
DR   SMR; P62484; 1-155, 377-441.
DR   DIP; DIP-48418N; -.
DR   STRING; P62484; -.
DR   PhosphoSite; P62484; -.
DR   PRIDE; P62484; -.
DR   Ensembl; ENSMUST00000052332; ENSMUSP00000058754; ENSMUSG00000026782.
DR   GeneID; 329165; -.
DR   KEGG; mmu:329165; -.
DR   UCSC; uc007beq.1; mouse.
DR   CTD; 329165; -.
DR   MGI; MGI:106913; Abi2.
DR   eggNOG; roNOG13215; -.
DR   HOVERGEN; HBG050446; -.
DR   OrthoDB; EOG4ZKJMQ; -.
DR   NextBio; 398613; -.
DR   ArrayExpress; P62484; -.
DR   Bgee; P62484; -.
DR   CleanEx; MM_ABI2; -.
DR   Genevestigator; P62484; -.
DR   GermOnline; ENSMUSG00000026782; Mus musculus.
DR   GO; GO:0005913; C:cell-cell adherens junction; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR   GO; GO:0016477; P:cell migration; IMP:MGI.
DR   GO; GO:0016358; P:dendrite development; IMP:MGI.
DR   GO; GO:0007611; P:learning or memory; IMP:MGI.
DR   InterPro; IPR012849; Abl-interactor_HHR_dom.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   Pfam; PF07815; Abi_HHR; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW   SH3 domain.
FT   CHAIN         1    446       Abl interactor 2.
FT                                /FTId=PRO_0000191791.
FT   DOMAIN       45    107       t-SNARE coiled-coil homology.
FT   DOMAIN      384    443       SH3.
FT   COMPBIAS    166    356       Pro-rich.
FT   MOD_RES     207    207       Phosphotyrosine (By similarity).
FT   MOD_RES     221    221       Phosphoserine (By similarity).
FT   MOD_RES     395    395       Phosphotyrosine.
SQ   SEQUENCE   446 AA;  49387 MW;  8EC1FB543D93BEAA CRC64;
     MAELQMLLEE EIPGGRRALF DSYTNLERVA DYCENNYIQS PDKQRALEET KAYTTQSLAS
     VAYLINTLAN NVLQMLDIQA SQLRRMESSI NHISQTVDIH KEKVARREIG ILTTNKNTSR
     THKIIAPANL ERPVRYIRKP IDYTILDDIG HGVKVSTQNM KMGGLPRTTP PTQKPPSPPM
     SGKGTLGRHS PYRTLEPVRP PVVPNDYVPS PTRNMAPSQQ SPVRTASVNQ RNRTYSSSGS
     SGGSHPSSRS SSRENSGSGS VGVPIAVPTP SPPSVFPGHP VQFYSMNRPA SRHTPPTIGG
     SLPYRRPPSI TSQTSLQNQM NGGPFYNQNP VSDTPPPPPP VEEPVFDESP PPPPPPEDYE
     EEEAAVVEYS DPYAEEDPPW APRAYLEKVV AIYDYTKDKE DELSFQEGAI IYVIKKNDDG
     WYEGVMNGVT GLFPGNYVES IMHYSE
//
ID   RB11A_MOUSE             Reviewed;         216 AA.
AC   P62492; P24410; Q3V1Z6; Q9JLX1;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Ras-related protein Rab-11A;
DE            Short=Rab-11;
GN   Name=Rab11a; Synonyms=Rab11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=20175251; PubMed=10708602; DOI=10.1006/bbrc.2000.2334;
RA   Bhartur S.G., Calhoun B.C., Woodrum J., Kurkjian J., Iyer S., Lai F.,
RA   Goldenring J.R.;
RT   "Genomic structure of murine rab11 family members.";
RL   Biochem. Biophys. Res. Commun. 269:611-617(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Amnion, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 14-24; 42-51 AND 83-95, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   INTERACTION WITH SGSM1; SGSM2 AND SGSM3.
RX   PubMed=17509819; DOI=10.1016/j.ygeno.2007.03.013;
RA   Yang H., Sasaki T., Minoshima S., Shimizu N.;
RT   "Identification of three novel proteins (SGSM1, 2, 3) which modulate
RT   small G protein (RAP and RAB)-mediated signaling pathway.";
RL   Genomics 90:249-260(2007).
RN   [6]
RP   INTERACTION WITH VIPAR.
RX   PubMed=20190753; DOI=10.1038/ng.538;
RA   Cullinane A.R., Straatman-Iwanowska A., Zaucker A., Wakabayashi Y.,
RA   Bruce C.K., Luo G., Rahman F., Gurakan F., Utine E., Ozkan T.B.,
RA   Denecke J., Vukovic J., Di Rocco M., Mandel H., Cangul H.,
RA   Matthews R.P., Thomas S.G., Rappoport J.Z., Arias I.M., Wolburg H.,
RA   Knisely A.S., Kelly D.A., Muller F., Maher E.R., Gissen P.;
RT   "Mutations in VIPAR cause an arthrogryposis, renal dysfunction and
RT   cholestasis syndrome phenotype with defects in epithelial
RT   polarization.";
RL   Nat. Genet. 42:303-312(2010).
CC   -!- FUNCTION: Modulates endosomal trafficking. Acts as a major
CC       regulator of membrane delivery during cytokinesis (By similarity).
CC   -!- SUBUNIT: Interacts with RAB11FIP1, RAB11FIP2, RAB11FIP3 (via its
CC       C-terminus) and RAB11FIP4. Interacts with EVI5; EVI5 and RAB11FIP3
CC       may be mutually exclusive and compete for binding RAB11A.
CC       Interacts with RIP11 and STXBP6 (By similarity). Interacts with
CC       SGSM1, SGSM2, SGSM3 and VIPAR.
CC   -!- INTERACTION:
CC       P59016:Vps33b; NbExp=1; IntAct=EBI-770256, EBI-2656383;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       (By similarity). Recycling endosome membrane; Peripheral membrane
CC       protein (By similarity). Note=Translocates with RAB11FIP2 from the
CC       vesicles of the endocytic recycling compartment (ERC) to the
CC       plasma membrane (By similarity).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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CC   -----------------------------------------------------------------------
DR   EMBL; AF127669; AAF36458.1; -; Genomic_DNA.
DR   EMBL; AK014268; BAB29233.1; -; mRNA.
DR   EMBL; AK132072; BAE20971.1; -; mRNA.
DR   EMBL; AK132159; BAE21003.1; -; mRNA.
DR   EMBL; AK147122; BAE27693.1; -; mRNA.
DR   EMBL; BC010722; AAH10722.1; -; mRNA.
DR   IPI; IPI00323897; -.
DR   RefSeq; NP_059078.2; NM_017382.5.
DR   UniGene; Mm.1387; -.
DR   ProteinModelPortal; P62492; -.
DR   SMR; P62492; 6-173.
DR   IntAct; P62492; 6.
DR   STRING; P62492; -.
DR   PhosphoSite; P62492; -.
DR   PRIDE; P62492; -.
DR   Ensembl; ENSMUST00000004892; ENSMUSP00000004892; ENSMUSG00000004771.
DR   GeneID; 53869; -.
DR   KEGG; mmu:53869; -.
DR   UCSC; uc009qce.1; mouse.
DR   CTD; 53869; -.
DR   MGI; MGI:1858202; Rab11a.
DR   eggNOG; roNOG09728; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; P62492; -.
DR   OMA; PDEEYDY; -.
DR   OrthoDB; EOG4RR6J7; -.
DR   PhylomeDB; P62492; -.
DR   NextBio; 310717; -.
DR   ArrayExpress; P62492; -.
DR   Bgee; P62492; -.
DR   CleanEx; MM_RAB11A; -.
DR   Genevestigator; P62492; -.
DR   GermOnline; ENSMUSG00000004771; Mus musculus.
DR   GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell cycle; Cell membrane; Direct protein sequencing;
KW   Endosome; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation; Protein transport; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    213       Ras-related protein Rab-11A.
FT                                /FTId=PRO_0000121152.
FT   PROPEP      214    216       Removed in mature form (Potential).
FT                                /FTId=PRO_0000370808.
FT   NP_BIND      18     26       GTP (By similarity).
FT   NP_BIND      66     70       GTP (By similarity).
FT   NP_BIND     124    127       GTP (By similarity).
FT   NP_BIND     154    156       GTP (By similarity).
FT   MOTIF        40     48       Effector region (By similarity).
FT   MOD_RES       2      2       N-acetylglycine (By similarity).
FT   MOD_RES     213    213       Cysteine methyl ester (Potential).
FT   LIPID       212    212       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   LIPID       213    213       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   CONFLICT    180    180       Q -> H (in Ref. 1; AAF36458).
SQ   SEQUENCE   216 AA;  24394 MW;  76FC1E113A29B269 CRC64;
     MGTRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT RSIQVDGKTI
     KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHLTYE NVERWLKELR DHADSNIVIM
     LVGNKSDLRH LRAVPTDEAR AFAEKNGLSF IETSALDSTN VEAAFQTILT EIYRIVSQKQ
     MSDRRENDMS PSNNVVPIHV PPTTENKPKV QCCQNI
//
ID   EF1A2_MOUSE             Reviewed;         463 AA.
AC   P62631; P27706;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   08-FEB-2011, entry version 73.
DE   RecName: Full=Elongation factor 1-alpha 2;
DE            Short=EF-1-alpha-2;
DE   AltName: Full=Eukaryotic elongation factor 1 A-2;
DE            Short=eEF1A-2;
DE   AltName: Full=Statin-S1;
GN   Name=Eef1a2; Synonyms=Eef1al, Stn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=95032003; PubMed=7945283; DOI=10.1006/bbrc.1994.2336;
RA   Lee S., Ann D.K., Wang E.;
RT   "Cloning of human and mouse brain cDNAs coding for S1, the second
RT   member of the mammalian elongation factor-1 alpha gene family:
RT   analysis of a possible evolutionary pathway.";
RL   Biochem. Biophys. Res. Commun. 203:1371-1377(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 6-30; 85-96; 135-146; 155-165; 248-266 AND
RP   431-439, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-141, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29 AND TYR-141, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of
CC       aminoacyl-tRNA to the A-site of ribosomes during protein
CC       biosynthesis.
CC   -!- SUBUNIT: Monomer.
CC   -!- INTERACTION:
CC       Q01534:TSPY1 (xeno); NbExp=1; IntAct=EBI-642385, EBI-1973142;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Found in a wide range of tissues.
CC   -!- DEVELOPMENTAL STAGE: The statin expression is specific for
CC       nonproliferating cells. Its message is most abundant in G0 phase
CC       of 3T3 mouse fibroblasts, but becomes significantly reduced in G1
CC       and S1 phases cells.
CC   -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC       EF-Tu/EF-1A subfamily.
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DR   EMBL; L26479; AAA91870.1; -; mRNA.
DR   EMBL; BC018235; AAH18235.1; -; mRNA.
DR   IPI; IPI00119667; -.
DR   PIR; JC2445; JC2445.
DR   RefSeq; NP_031932.1; NM_007906.2.
DR   UniGene; Mm.2645; -.
DR   ProteinModelPortal; P62631; -.
DR   SMR; P62631; 2-443.
DR   IntAct; P62631; 4.
DR   STRING; P62631; -.
DR   PRIDE; P62631; -.
DR   Ensembl; ENSMUST00000055990; ENSMUSP00000054556; ENSMUSG00000016349.
DR   GeneID; 13628; -.
DR   KEGG; mmu:13628; -.
DR   UCSC; uc008olh.1; mouse.
DR   CTD; 13628; -.
DR   MGI; MGI:1096317; Eef1a2.
DR   eggNOG; roNOG10172; -.
DR   GeneTree; ENSGT00570000078778; -.
DR   HOGENOM; HBG307581; -.
DR   HOVERGEN; HBG000179; -.
DR   InParanoid; P62631; -.
DR   OMA; AFIGHVD; -.
DR   PhylomeDB; P62631; -.
DR   NextBio; 284308; -.
DR   ArrayExpress; P62631; -.
DR   Bgee; P62631; -.
DR   Genevestigator; P62631; -.
DR   GermOnline; ENSMUSG00000016349; Mus musculus.
DR   GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003746; F:translation elongation factor activity; IDA:MGI.
DR   GO; GO:0006916; P:anti-apoptosis; IDA:MGI.
DR   InterPro; IPR000795; ProtSyn_GTP-bd.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR   InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   InterPro; IPR009000; Transl_elong_init/rib_B-barrel.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50465; Elong_init_C; 1.
DR   SUPFAM; SSF50447; Translat_factor; 1.
DR   TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR   PROSITE; PS00301; EFACTOR_GTP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Elongation factor;
KW   GTP-binding; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Protein biosynthesis.
FT   CHAIN         1    463       Elongation factor 1-alpha 2.
FT                                /FTId=PRO_0000090892.
FT   NP_BIND      14     21       GTP (By similarity).
FT   NP_BIND      91     95       GTP (By similarity).
FT   NP_BIND     153    156       GTP (By similarity).
FT   MOD_RES      29     29       Phosphotyrosine.
FT   MOD_RES      55     55       N6,N6,N6-trimethyllysine (By similarity).
FT   MOD_RES     141    141       Phosphotyrosine.
FT   MOD_RES     165    165       N6,N6,N6-trimethyllysine (By similarity).
FT   MOD_RES     179    179       N6-acetyllysine (By similarity).
FT   MOD_RES     301    301       5-glutamyl glycerylphosphorylethanolamine
FT                                (By similarity).
FT   MOD_RES     374    374       5-glutamyl glycerylphosphorylethanolamine
FT                                (By similarity).
FT   MOD_RES     439    439       N6-acetyllysine (By similarity).
SQ   SEQUENCE   463 AA;  50454 MW;  31E4F59BC05D8F8C CRC64;
     MGKEKTHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAAEMG KGSFKYAWVL
     DKLKAERERG ITIDISLWKF ETTKYYITII DAPGHRDFIK NMITGTSQAD CAVLIVAAGV
     GEFEAGISKN GQTREHALLA YTLGVKQLIV GVNKMDSTEP AYSEKRYDEI VKEVSAYIKK
     IGYNPATVPF VPISGWHGDN MLEPSPNMPW FKGWKVERKE GNASGVSLLE ALDTILPPTR
     PTDKPLRLPL QDVYKIGGIG TVPVGRVETG ILRPGMVVTF APVNITTEVK SVEMHHEALS
     EALPGDNVGF NVKNVSVKDI RRGNVCGDSK ADPPQEAAQF TSQVIILNHP GQISAGYSPV
     IDCHTAHIAC KFAELKEKID RRSGKKLEDN PKSLKSGDAA IVEMVPGKPM CVESFSQYPP
     LGRFAVRDMR QTVAVGVIKN VEKKSGGAGK VTKSAQKAQK AGK
//
ID   PP2AB_MOUSE             Reviewed;         309 AA.
AC   P62715; P11082;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform;
DE            Short=PP2A-beta;
DE            EC=3.1.3.16;
GN   Name=Ppp2cb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X DBA/2; TISSUE=Brain;
RA   Goetz J.M., Kues W.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 62-83.
RX   MEDLINE=94357899; PubMed=8077208;
RA   Becker W., Kentrup H., Klumpp S., Schultz J.E., Joost H.G.;
RT   "Molecular cloning of a protein serine/threonine phosphatase
RT   containing a putative regulatory tetratricopeptide repeat domain.";
RL   J. Biol. Chem. 269:22586-22592(1994).
RN   [4]
RP   PROTEIN SEQUENCE OF 284-294, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION AT TYR-307.
RX   MEDLINE=94179160; PubMed=7510677;
RA   Chen J., Parsons S., Brautigan D.L.;
RT   "Tyrosine phosphorylation of protein phosphatase 2A in response to
RT   growth stimulation and v-src transformation of fibroblasts.";
RL   J. Biol. Chem. 269:7957-7962(1994).
RN   [6]
RP   MUTAGENESIS OF TYR-307 AND LEU-309.
RX   MEDLINE=99371680; PubMed=10441131; DOI=10.1021/bi990902g;
RA   Chung H., Nairn A.C., Murata K., Brautigan D.L.;
RT   "Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic
RT   subunit favors association with the alpha 4 subunit which promotes
RT   dephosphorylation of elongation factor-2.";
RL   Biochemistry 38:10371-10376(1999).
CC   -!- FUNCTION: PP2A can modulate the activity of phosphorylase B kinase
CC       casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase.
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity).
CC   -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme
CC       (composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa
CC       constant regulatory subunit (PR65) (subunit A)) that associates
CC       with a variety of regulatory subunits. Proteins that associate
CC       with the core dimer include three families of regulatory subunits
CC       B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56
CC       families), the 48 kDa variable regulatory subunit, viral proteins,
CC       and cell signaling molecules. Binds PPME1 (By similarity). May
CC       indirectly interact with SGOL1, most probably through regulatory
CC       B56 subunits. Found in a complex with at least ARL2, PPP2CB,
CC       PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with TBCD (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus (By similarity).
CC       Chromosome, centromere (By similarity). Cytoplasm, cytoskeleton,
CC       spindle pole (By similarity). Note=In prometaphase cells, but not
CC       in anaphase cells, localizes at centromeres. During mitosis, also
CC       found at spindle poles (By similarity).
CC   -!- PTM: Reversibly methyl esterified on Leu-309. Carboxyl methylation
CC       may play a role in holoenzyme assembly. It varies during the cell
CC       cycle. Demethylated by PME1 (in vitro) (By similarity).
CC   -!- PTM: Phosphorylation of either threonine (by autophosphorylation-
CC       activated protein kinase) or tyrosine results in inactivation of
CC       the phosphatase. Auto-dephosphorylation has been suggested as a
CC       mechanism for reactivation (By similarity).
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; Z67746; CAA91559.1; -; mRNA.
DR   EMBL; BC058582; AAH58582.1; -; mRNA.
DR   IPI; IPI00111556; -.
DR   RefSeq; NP_059070.1; NM_017374.3.
DR   UniGene; Mm.288765; -.
DR   ProteinModelPortal; P62715; -.
DR   SMR; P62715; 6-293.
DR   STRING; P62715; -.
DR   PhosphoSite; P62715; -.
DR   PRIDE; P62715; -.
DR   Ensembl; ENSMUST00000009774; ENSMUSP00000009774; ENSMUSG00000009630.
DR   GeneID; 19053; -.
DR   KEGG; mmu:19053; -.
DR   UCSC; uc009lkd.1; mouse.
DR   CTD; 19053; -.
DR   MGI; MGI:1321161; Ppp2cb.
DR   eggNOG; roNOG15147; -.
DR   HOGENOM; HBG716770; -.
DR   HOVERGEN; HBG000216; -.
DR   InParanoid; P62715; -.
DR   OMA; ERLMQCK; -.
DR   OrthoDB; EOG4Q58PR; -.
DR   PhylomeDB; P62715; -.
DR   BRENDA; 3.1.3.16; 244.
DR   NextBio; 295528; -.
DR   ArrayExpress; P62715; -.
DR   Bgee; P62715; -.
DR   Genevestigator; P62715; -.
DR   GermOnline; ENSMUSG00000009630; Mus musculus.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; TAS:MGI.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:MGI.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043066; P:negative regulation of apoptosis; IMP:MGI.
DR   GO; GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; IMP:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR   GO; GO:0046677; P:response to antibiotic; IMP:MGI.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IMP:MGI.
DR   InterPro; IPR004843; Metallo-dependent_phosphatase.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR11668; T_phtase_apaH; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   1: Evidence at protein level;
KW   Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Hydrolase; Iron; Manganese; Metal-binding;
KW   Methylation; Nucleus; Phosphoprotein; Protein phosphatase.
FT   CHAIN         1    309       Serine/threonine-protein phosphatase 2A
FT                                catalytic subunit beta isoform.
FT                                /FTId=PRO_0000058846.
FT   ACT_SITE    118    118       Proton donor (By similarity).
FT   METAL        57     57       Iron (By similarity).
FT   METAL        59     59       Iron (By similarity).
FT   METAL        85     85       Iron (By similarity).
FT   METAL        85     85       Manganese (By similarity).
FT   METAL       117    117       Manganese (By similarity).
FT   METAL       167    167       Manganese (By similarity).
FT   METAL       241    241       Manganese (By similarity).
FT   MOD_RES     307    307       Phosphotyrosine.
FT   MOD_RES     309    309       Leucine methyl ester (By similarity).
FT   MUTAGEN     307    307       Y->Q: Loss of trimeric subunit ABC
FT                                assembly.
FT   MUTAGEN     309    309       L->A: Loss of binding to PP2A B-alpha
FT                                regulatory subunit.
FT   MUTAGEN     309    309       L->Q: Loss of trimeric subunit ABC
FT                                assembly.
SQ   SEQUENCE   309 AA;  35575 MW;  51DA9EB0633FC191 CRC64;
     MDDKAFTKEL DQWVEQLNEC KQLNENQVRT LCEKAKEILT KESNVQEVRC PVTVCGDVHG
     QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL VALKVRYPER ITILRGNHES
     RQITQVYGFY DECLRKYGNA NVWKYFTDLF DYLPLTALVD GQIFCLHGGL SPSIDTLDHI
     RALDRLQEVP HEGPMCDLLW SDPDDRGGWG ISPRGAGYTF GQDISETFNH ANGLTLVSRA
     HQLVMEGYNW CHDRNVVTIF SAPNYCYRCG NQAAIMELDD TLKYSFLQFD PAPRRGEPHV
     TRRTPDYFL
//
ID   RL18A_MOUSE             Reviewed;         176 AA.
AC   P62717; P11249; Q3TSN0;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=60S ribosomal protein L18a;
GN   Name=Rpl18a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Kidney, Liver, Muellerian duct, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SUBUNIT: Binds IPO9 with high affinity (By similarity).
CC   -!- SIMILARITY: Belongs to the ribosomal protein L18Ae family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK010983; BAB27304.1; -; mRNA.
DR   EMBL; AK146543; BAE27248.1; -; mRNA.
DR   EMBL; AK161942; BAE36645.1; -; mRNA.
DR   EMBL; AK162047; BAE36696.1; -; mRNA.
DR   EMBL; BC037146; AAH37146.1; -; mRNA.
DR   IPI; IPI00162790; -.
DR   RefSeq; NP_084027.1; NM_029751.4.
DR   UniGene; Mm.379251; -.
DR   UniGene; Mm.431334; -.
DR   ProteinModelPortal; P62717; -.
DR   SMR; P62717; 3-166.
DR   STRING; P62717; -.
DR   PRIDE; P62717; -.
DR   Ensembl; ENSMUST00000054220; ENSMUSP00000058368; ENSMUSG00000045128.
DR   GeneID; 76808; -.
DR   KEGG; mmu:76808; -.
DR   UCSC; uc009mca.1; mouse.
DR   CTD; 76808; -.
DR   MGI; MGI:1924058; Rpl18a.
DR   eggNOG; roNOG08557; -.
DR   HOGENOM; HBG319315; -.
DR   HOVERGEN; HBG066281; -.
DR   InParanoid; P62717; -.
DR   OMA; KVKNFGI; -.
DR   OrthoDB; EOG40P47V; -.
DR   PhylomeDB; P62717; -.
DR   NextBio; 345857; -.
DR   ArrayExpress; P62717; -.
DR   Bgee; P62717; -.
DR   CleanEx; MM_RPL18A; -.
DR   Genevestigator; P62717; -.
DR   GermOnline; ENSMUSG00000045128; Mus musculus.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR021138; Ribosomal_L18a.
DR   PANTHER; PTHR10052; PTHR10052; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Ribonucleoprotein; Ribosomal protein.
FT   CHAIN         1    176       60S ribosomal protein L18a.
FT                                /FTId=PRO_0000213926.
FT   MOD_RES      24     24       Phosphothreonine (By similarity).
FT   MOD_RES      63     63       Phosphotyrosine (By similarity).
FT   MOD_RES      71     71       Phosphoserine (By similarity).
FT   MOD_RES     123    123       Phosphoserine.
SQ   SEQUENCE   176 AA;  20732 MW;  5E404D28875BE580 CRC64;
     MKASGTLREY KVVGRCLPTP KCHTPPLYRM RIFAPNHVVA KSRFWYFVSQ LKKMKKSSGE
     IVYCGQVFEK SPLRVKNFGI WLRYDSRSGT HNMYREYRDL TTAGAVTQCY RDMGARHRAR
     AHSIQIMKVE EIAAGKCRRP AVKQFHDSKI KFPLPHRVLR RQHKPRFTTK RPNTFF
//
ID   ACTA_MOUSE              Reviewed;         377 AA.
AC   P62737; P03996; P04108;
DT   23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Actin, aortic smooth muscle;
DE   AltName: Full=Alpha-actin-2;
GN   Name=Acta2; Synonyms=Actsa, Actvs;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C3H;
RX   MEDLINE=89057488; PubMed=3194212; DOI=10.1093/nar/16.21.10374;
RA   Min B.H., Strauch A.R., Foster D.N.;
RT   "Nucleotide sequence of a mouse vascular smooth muscle alpha-actin
RT   cDNA.";
RL   Nucleic Acids Res. 16:10374-10374(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C3H/He; TISSUE=Osteoblast;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 3-20.
RX   MEDLINE=84212581; PubMed=6725286;
RA   Strauch A.R., Rubenstein P.A.;
RT   "A vascular smooth muscle alpha-isoactin biosynthetic intermediate in
RT   BC3H1 cells. Identification of acetylcysteine at the NH2 terminus.";
RL   J. Biol. Chem. 259:7224-7229(1984).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
RX   PubMed=2398068;
RA   Min B.H., Foster D.N., Strauch A.R.;
RT   "The 5'-flanking region of the mouse vascular smooth muscle alpha-
RT   actin gene contains evolutionarily conserved sequence motifs within a
RT   functional promoter.";
RL   J. Biol. Chem. 265:16667-16675(1990).
RN   [6]
RP   PROTEIN SEQUENCE OF 21-41; 53-63; 71-86; 98-115; 186-193; 241-256 AND
RP   318-328, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC       alpha, beta and gamma have been identified. The alpha actins are
CC       found in muscle tissues and are a major constituent of the
CC       contractile apparatus. The beta and gamma actins coexist in most
CC       cell types as components of the cytoskeleton and as mediators of
CC       internal cell motility.
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; X13297; CAA31659.1; -; mRNA.
DR   EMBL; AK017374; BAB30715.1; -; mRNA.
DR   EMBL; BC064800; AAH64800.1; -; mRNA.
DR   EMBL; M57409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00117043; -.
DR   PIR; S02135; A22224.
DR   RefSeq; NP_031418.1; NM_007392.2.
DR   UniGene; Mm.213025; -.
DR   ProteinModelPortal; P62737; -.
DR   SMR; P62737; 6-377.
DR   STRING; P62737; -.
DR   PhosphoSite; P62737; -.
DR   REPRODUCTION-2DPAGE; P62737; -.
DR   UCD-2DPAGE; P62737; -.
DR   PRIDE; P62737; -.
DR   Ensembl; ENSMUST00000039631; ENSMUSP00000048218; ENSMUSG00000035783.
DR   GeneID; 11475; -.
DR   KEGG; mmu:11475; -.
DR   UCSC; uc008hgg.1; mouse.
DR   CTD; 11475; -.
DR   MGI; MGI:87909; Acta2.
DR   eggNOG; roNOG14612; -.
DR   HOGENOM; HBG559892; -.
DR   HOVERGEN; HBG003771; -.
DR   InParanoid; P62737; -.
DR   OMA; NSICVIL; -.
DR   OrthoDB; EOG4W9J40; -.
DR   PhylomeDB; P62737; -.
DR   NextBio; 278816; -.
DR   ArrayExpress; P62737; -.
DR   Bgee; P62737; -.
DR   CleanEx; MM_ACTA2; -.
DR   Genevestigator; P62737; -.
DR   GermOnline; ENSMUSG00000035783; Mus musculus.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR   GO; GO:0030485; C:smooth muscle contractile fiber; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR   GO; GO:0014829; P:vascular smooth muscle contraction; IMP:MGI.
DR   InterPro; IPR004000; Actin-like.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Methylation; Muscle protein;
KW   Nucleotide-binding; Phosphoprotein.
FT   PROPEP        1      2       Removed in mature form.
FT                                /FTId=PRO_0000000740.
FT   CHAIN         3    377       Actin, aortic smooth muscle.
FT                                /FTId=PRO_0000000741.
FT   MOD_RES       3      3       N-acetylglutamate.
FT   MOD_RES      75     75       Tele-methylhistidine (By similarity).
FT   MOD_RES     325    325       Phosphoserine (By similarity).
SQ   SEQUENCE   377 AA;  42009 MW;  2D0543262DB35CA5 CRC64;
     MCEEEDSTAL VCDNGSGLCK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
     QSKRGILTLK YPIEHGIITN WDDMEKIWHH SFYNELRVAP EEHPTLLTEA PLNPKANREK
     MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL
     DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK
     SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
     LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS
     KQEYDEAGPS IVHRKCF
//
ID   HPCL1_MOUSE             Reviewed;         193 AA.
AC   P62748; P35333;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Hippocalcin-like protein 1;
DE   AltName: Full=Neural visinin-like protein 3;
DE            Short=NVL-3;
DE            Short=NVP-3;
DE   AltName: Full=Visinin-like protein 3;
DE            Short=VILIP-3;
GN   Name=Hpcal1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RA   Ritter B., Modregger J., Plomann M.;
RT   "Interactions of the murine neural visinin-like protein 3 (mNVP-3).";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in the calcium-dependent regulation of
CC       rhodopsin phosphorylation.
CC   -!- MISCELLANEOUS: Probably binds two or three calcium ions (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the recoverin family.
CC   -!- SIMILARITY: Contains 4 EF-hand domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF085192; AAC35552.1; -; mRNA.
DR   EMBL; BC001997; AAH01997.1; -; mRNA.
DR   IPI; IPI00230449; -.
DR   RefSeq; NP_057886.1; NM_016677.4.
DR   UniGene; Mm.477743; -.
DR   ProteinModelPortal; P62748; -.
DR   SMR; P62748; 5-185.
DR   STRING; P62748; -.
DR   PhosphoSite; P62748; -.
DR   PRIDE; P62748; -.
DR   Ensembl; ENSMUST00000071858; ENSMUSP00000071756; ENSMUSG00000071379.
DR   GeneID; 53602; -.
DR   KEGG; mmu:53602; -.
DR   UCSC; uc007ncx.1; mouse.
DR   CTD; 53602; -.
DR   MGI; MGI:1855689; Hpcal1.
DR   eggNOG; roNOG12066; -.
DR   GeneTree; ENSGT00560000076803; -.
DR   HOGENOM; HBG746798; -.
DR   HOVERGEN; HBG108179; -.
DR   InParanoid; P62748; -.
DR   OMA; LEIVQXK; -.
DR   OrthoDB; EOG4G1MHC; -.
DR   PhylomeDB; P62748; -.
DR   NextBio; 310285; -.
DR   ArrayExpress; P62748; -.
DR   Bgee; P62748; -.
DR   CleanEx; MM_HPCAL1; -.
DR   Genevestigator; P62748; -.
DR   GermOnline; ENSMUSG00000071379; Mus musculus.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR018248; EF-hand.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR001125; Recoverin.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF00036; efhand; 3.
DR   PRINTS; PR00450; RECOVERIN.
DR   SMART; SM00054; EFh; 3.
DR   PROSITE; PS00018; EF_HAND_1; 3.
DR   PROSITE; PS50222; EF_HAND_2; 4.
PE   2: Evidence at transcript level;
KW   Calcium; Lipoprotein; Myristate; Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    193       Hippocalcin-like protein 1.
FT                                /FTId=PRO_0000073772.
FT   DOMAIN       23     58       EF-hand 1.
FT   DOMAIN       60     95       EF-hand 2.
FT   DOMAIN       96    131       EF-hand 3.
FT   DOMAIN      144    179       EF-hand 4.
FT   CA_BIND      73     84       1 (Potential).
FT   CA_BIND     109    120       2 (Potential).
FT   CA_BIND     157    168       3 (Potential).
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
SQ   SEQUENCE   193 AA;  22338 MW;  B7251445F834F91D CRC64;
     MGKQNSKLRP EVLQDLREHT EFTDHELQEW YKGFLKDCPT GHLTVDEFKK IYANFFPYGD
     ASKFAEHVFR TFDTNSDGTI DFREFIIALS VTSRGKLEQK LKWAFSMYDL DGNGYISRSE
     MLEIVQAIYK MVSSVMKMPE DESTPEKRTD KIFRQMDTNN DGKLSLEEFI KGAKSDPSIV
     RLLQCDPSSA SQF
//
ID   RL23A_MOUSE             Reviewed;         156 AA.
AC   P62751; P29316; P39024; Q92774;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=60S ribosomal protein L23a;
GN   Name=Rpl23a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Fan Y., Friedman C., Trask B.J.;
RT   "cDNA cloning, genomic structure, and chromosomal localization of a
RT   novel murine ribosomal protein L23a gene.";
RL   Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon, and Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   CLEAVAGE OF INITIATOR METHIONINE, AND METHYLATION AT ALA-2.
RX   PubMed=20668449; DOI=10.1038/nature09343;
RA   Tooley C.E., Petkowski J.J., Muratore-Schroeder T.L., Balsbaugh J.L.,
RA   Shabanowitz J., Sabat M., Minor W., Hunt D.F., Macara I.G.;
RT   "NRMT is an alpha-N-methyltransferase that methylates RCC1 and
RT   retinoblastoma protein.";
RL   Nature 466:1125-1128(2010).
CC   -!- FUNCTION: This protein binds to a specific region on the 26S rRNA
CC       (By similarity).
CC   -!- PTM: N-terminus is methylated by METTL11A/NTM1.
CC   -!- SIMILARITY: Belongs to the ribosomal protein L23P family.
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DR   EMBL; AF452721; AAQ04686.1; -; mRNA.
DR   EMBL; BC026656; AAH26656.1; -; mRNA.
DR   EMBL; BC029892; AAH29892.1; -; mRNA.
DR   IPI; IPI00461456; -.
DR   RefSeq; NP_997406.1; NM_207523.2.
DR   RefSeq; XP_001480950.1; XM_001480900.2.
DR   UniGene; Mm.22723; -.
DR   UniGene; Mm.304790; -.
DR   UniGene; Mm.352675; -.
DR   ProteinModelPortal; P62751; -.
DR   SMR; P62751; 36-156.
DR   STRING; P62751; -.
DR   PhosphoSite; P62751; -.
DR   PRIDE; P62751; -.
DR   Ensembl; ENSMUST00000079428; ENSMUSP00000078397; ENSMUSG00000063556.
DR   Ensembl; ENSMUST00000102483; ENSMUSP00000099541; ENSMUSG00000058546.
DR   GeneID; 100043755; -.
DR   GeneID; 268449; -.
DR   KEGG; mmu:100043755; -.
DR   KEGG; mmu:268449; -.
DR   UCSC; uc007kil.1; mouse.
DR   CTD; 268449; -.
DR   MGI; MGI:3040672; Rpl23a.
DR   eggNOG; roNOG17212; -.
DR   HOGENOM; HBG439330; -.
DR   HOVERGEN; HBG056619; -.
DR   InParanoid; P62751; -.
DR   OMA; SAAKINT; -.
DR   OrthoDB; EOG43JC62; -.
DR   PhylomeDB; P62751; -.
DR   NextBio; 457012; -.
DR   Bgee; P62751; -.
DR   CleanEx; MM_RPL23A; -.
DR   Genevestigator; P62751; -.
DR   GermOnline; ENSMUSG00000063556; Mus musculus.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR019985; Ribosomal_L23.
DR   InterPro; IPR012678; Ribosomal_L23/L15e.
DR   InterPro; IPR001014; Ribosomal_L23/L25_CS.
DR   InterPro; IPR005633; Ribosomal_L23/L25_N.
DR   InterPro; IPR013025; Ribosomal_L25/23.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF00276; Ribosomal_L23; 1.
DR   Pfam; PF03939; Ribosomal_L23eN; 1.
DR   SUPFAM; SSF54189; L23_L15e_core; 1.
DR   TIGRFAMs; TIGR03636; L23_arch; 1.
DR   PROSITE; PS00050; RIBOSOMAL_L23; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Methylation; Phosphoprotein; Ribonucleoprotein;
KW   Ribosomal protein; RNA-binding; rRNA-binding.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    156       60S ribosomal protein L23a.
FT                                /FTId=PRO_0000129468.
FT   MOD_RES       2      2       N,N,N-trimethylalanine; by NTM1.
FT   MOD_RES      43     43       Phosphoserine (By similarity).
FT   MOD_RES      70     70       N6-acetyllysine (By similarity).
SQ   SEQUENCE   156 AA;  17695 MW;  3980E77B47FAB70E CRC64;
     MAPKAKKEAP APPKAEAKAK ALKAKKAVLK GVHSHKKKKI RTSPTFRRPK TLRLRRQPKY
     PRKSAPRRNK LDHYAIIKFP LTTESAMKKI EDNNTLVFIV DVKANKHQIK QAVKKLYDID
     VAKVNTLIRP DGEKKAYVRL APDYDALDVA NKIGII
//
ID   VISL1_MOUSE             Reviewed;         191 AA.
AC   P62761; P28677; P29103; P42323; Q9UM20;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Visinin-like protein 1;
DE            Short=VILIP;
DE   AltName: Full=Neural visinin-like protein 1;
DE            Short=NVL-1;
DE            Short=NVP-1;
GN   Name=Vsnl1; Synonyms=Visl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RA   Shirai Y., Asami M., Mukai H., Chang C., Shuntoh H., Kuno T.,
RA   Tanaka C.;
RT   "cDNA cloning and primary structure of mouse neural visinin-like CA2+-
RT   binding protein type 1 (NVP-1).";
RL   Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RA   Anton B., Matus M., Leff P., Calva J.C., Acevedo R., Hernandez A.,
RA   Medecigo M., Valdez A., Sanchez Lopez R., Vergara P., Torner C.,
RA   Segovia J., Alagon A.;
RT   "Searching for the endomorphin-1-2 pro-peptide precursor(s)
RT   protein(s): cloning of a protein encoding an endomorphin-2-like
RT   peptide sequence.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 8-18; 43-63 AND 119-150, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Regulates (in vitro) the inhibition of rhodopsin
CC       phosphorylation in a calcium-dependent manner (By similarity).
CC   -!- MISCELLANEOUS: Probably binds three calcium ions.
CC   -!- SIMILARITY: Belongs to the recoverin family.
CC   -!- SIMILARITY: Contains 4 EF-hand domains.
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DR   EMBL; D21165; BAA04701.1; -; mRNA.
DR   EMBL; AY101375; AAM48292.1; -; mRNA.
DR   EMBL; BC046226; AAH46226.1; -; mRNA.
DR   IPI; IPI00230418; -.
DR   RefSeq; NP_036168.1; NM_012038.4.
DR   UniGene; Mm.27005; -.
DR   ProteinModelPortal; P62761; -.
DR   SMR; P62761; 5-187.
DR   STRING; P62761; -.
DR   PRIDE; P62761; -.
DR   Ensembl; ENSMUST00000072299; ENSMUSP00000072145; ENSMUSG00000054459.
DR   GeneID; 26950; -.
DR   KEGG; mmu:26950; -.
DR   UCSC; uc007nba.1; mouse.
DR   CTD; 26950; -.
DR   MGI; MGI:1349453; Vsnl1.
DR   eggNOG; roNOG14398; -.
DR   HOGENOM; HBG746798; -.
DR   HOVERGEN; HBG108179; -.
DR   InParanoid; P62761; -.
DR   OMA; ILQFFPY; -.
DR   OrthoDB; EOG40VVQK; -.
DR   PhylomeDB; P62761; -.
DR   NextBio; 304891; -.
DR   ArrayExpress; P62761; -.
DR   Bgee; P62761; -.
DR   CleanEx; MM_VSNL1; -.
DR   Genevestigator; P62761; -.
DR   GermOnline; ENSMUSG00000054459; Mus musculus.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   InterPro; IPR018248; EF-hand.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR001125; Recoverin.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF00036; efhand; 3.
DR   PRINTS; PR00450; RECOVERIN.
DR   SMART; SM00054; EFh; 3.
DR   PROSITE; PS00018; EF_HAND_1; 3.
DR   PROSITE; PS50222; EF_HAND_2; 4.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Lipoprotein; Myristate; Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    191       Visinin-like protein 1.
FT                                /FTId=PRO_0000073764.
FT   DOMAIN       23     58       EF-hand 1.
FT   DOMAIN       60     95       EF-hand 2.
FT   DOMAIN       96    131       EF-hand 3.
FT   DOMAIN      146    181       EF-hand 4.
FT   CA_BIND      73     84       1 (Potential).
FT   CA_BIND     109    120       2 (Potential).
FT   CA_BIND     159    170       3 (Potential).
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
SQ   SEQUENCE   191 AA;  22142 MW;  ACDC3B4FE8C79265 CRC64;
     MGKQNSKLAP EVMEDLVKST EFNEHELKQW YKGFLKDCPS GRLNLEEFQQ LYVKFFPYGD
     ASKFAQHAFR TFDKNGDGTI DFREFICALS ITSRGSFEQK LNWAFNMYDL DGDGKITRVE
     MLEIIEAIYK MVGTVIMMKM NEDGLTPEQR VDKIFSKMDK NKDDQITLDE FKEAAKSDPS
     IVLLLQCDIQ K
//
ID   H4_MOUSE                Reviewed;         103 AA.
AC   P62806; A0AUM5; A4FUP8; A4QMY0; P02304; P02305; Q0VDL9; Q2M2Q5;
AC   Q5T006; Q6PDS7; Q811M0; Q9D0C9; Q9D6Q8;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Histone H4;
GN   Name=Hist1h4a;
GN   and
GN   Name=Hist1h4b; Synonyms=H4-53;
GN   and
GN   Name=Hist1h4c; Synonyms=H4-12;
GN   and
GN   Name=Hist1h4d;
GN   and
GN   Name=Hist1h4f;
GN   and
GN   Name=Hist1h4h;
GN   and
GN   Name=Hist1h4i;
GN   and
GN   Name=Hist1h4j;
GN   and
GN   Name=Hist1h4k;
GN   and
GN   Name=Hist1h4m;
GN   and
GN   Name=Hist2h4a; Synonyms=Hist2h4;
GN   and
GN   Name=Hist4h4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=82122584; PubMed=6276563; DOI=10.1016/0022-2836(81)90426-5;
RA   Seiler-Tuyns A., Birnstiel M.L.;
RT   "Structure and expression in L-cells of a cloned H4 histone gene of
RT   the mouse.";
RL   J. Mol. Biol. 151:607-625(1981).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H4B AND HIST1H4C).
RX   MEDLINE=89128447; PubMed=2915930; DOI=10.1093/nar/17.2.795;
RA   Meier V.S., Boehni R., Schuemperli D.;
RT   "Nucleotide sequence of two mouse histone H4 genes.";
RL   Nucleic Acids Res. 17:795-795(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H4A).
RC   STRAIN=C57BL/6;
RX   MEDLINE=97011334; PubMed=8858344;
RA   Wang Z.-F., Krasikov T., Frey M.R., Wang J., Matera A.G.,
RA   Marzluff W.F.;
RT   "Characterization of the mouse histone gene cluster on chromosome 13:
RT   45 histone genes in three patches spread over 1Mb.";
RL   Genome Res. 6:688-701(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RA   Franke K., Drabent B., Doenecke D.;
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H4A; HIST1H4B; HIST1H4C;
RP   HIST1H4D; HIST1H4F; HIST1H44; HIST1H4I; HIST1H4J; HIST1H4K; HIST1H4M;
RP   HIST2H4A AND HIST4H4).
RX   MEDLINE=22296985; PubMed=12408966; DOI=10.1016/S0888-7543(02)96850-3;
RA   Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
RT   "The human and mouse replication-dependent histone genes.";
RL   Genomics 80:487-498(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Egg, Pancreas, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain, Embryo, Eye, Heart, Mammary gland, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   METHYLATION AT LYS-21.
RX   PubMed=15145825; DOI=10.1101/gad.300704;
RA   Schotta G., Lachner M., Sarma K., Ebert A., Sengupta R., Reuter G.,
RA   Reinberg D., Jenuwein T.;
RT   "A silencing pathway to induce H3-K9 and H4-K20 trimethylation at
RT   constitutive heterochromatin.";
RL   Genes Dev. 18:1251-1262(2004).
RN   [10]
RP   PHOSPHORYLATION AT SER-2.
RX   PubMed=16980586; DOI=10.1101/gad.1457006;
RA   Krishnamoorthy T., Chen X., Govin J., Cheung W.L., Dorsey J.,
RA   Schindler K., Winter E., Allis C.D., Guacci V., Khochbin S.,
RA   Fuller M.T., Berger S.L.;
RT   "Phosphorylation of histone H4 Ser1 regulates sporulation in yeast and
RT   is conserved in fly and mouse spermatogenesis.";
RL   Genes Dev. 20:2580-2592(2006).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6; LYS-9; LYS-13 AND LYS-17,
RP   AND MASS SPECTROMETRY.
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
RN   [12]
RP   METHYLATION AT ARG-4.
RX   PubMed=16699504; DOI=10.1038/ncb1413;
RA   Ancelin K., Lange U.C., Hajkova P., Schneider R., Bannister A.J.,
RA   Kouzarides T., Surani M.A.;
RT   "Blimp1 associates with Prmt5 and directs histone arginine methylation
RT   in mouse germ cells.";
RL   Nat. Cell Biol. 8:623-630(2006).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-52 AND TYR-89, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RA   Lubec G., Kang S.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH H2A-Z; H2B AND
RP   H3.
RX   PubMed=11101893; DOI=10.1038/81971;
RA   Suto R.K., Clarkson M.J., Tremethick D.J., Luger K.;
RT   "Crystal structure of a nucleosome core particle containing the
RT   variant histone H2A.Z.";
RL   Nat. Struct. Biol. 7:1121-1124(2000).
CC   -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and
CC       compact DNA into chromatin, limiting DNA accessibility to the
CC       cellular machineries which require DNA as a template. Histones
CC       thereby play a central role in transcription regulation, DNA
CC       repair, DNA replication and chromosomal stability. DNA
CC       accessibility is regulated via a complex set of post-translational
CC       modifications of histones, also called histone code, and
CC       nucleosome remodeling.
CC   -!- SUBUNIT: The nucleosome is a histone octamer containing two
CC       molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
CC       heterotetramer and two H2A-H2B heterodimers. The octamer wraps
CC       approximately 147 bp of DNA.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Chromosome (By
CC       similarity).
CC   -!- PTM: Acetylation at Lys-6 (H4K5ac), Lys-9 (H4K8ac), Lys-13
CC       (H4K12ac) and Lys-17 (H4K16ac) occurs in coding regions of the
CC       genome but not in heterochromatin.
CC   -!- PTM: Citrullination at Arg-4 (H4R3ci) by PADI4 impairs
CC       methylation.
CC   -!- PTM: Monomethylation and asymmetric dimethylation at Arg-4
CC       (H4R3me1 and H4R3me2a, respectively) by PRMT1 favors acetylation
CC       at Lys-9 (H4K8ac) and Lys-13 (H4K12ac). Demethylation is performed
CC       by JMJD6. Symmetric dimethylation on Arg-4 (H4R3me2s) by the
CC       PRDM1/PRMT5 complex may play a crucial role in the germ-cell
CC       lineage (By similarity).
CC   -!- PTM: Monomethylated, dimethylated or trimethylated at Lys-21
CC       (H4K20me1, H4K20me2, H4K20me3). Monomethylation is performed by
CC       SET8. Trimethylation is performed by SUV420H1 and SUV420H2 and
CC       induces gene silencing (By similarity).
CC   -!- PTM: Ubiquitinated by the CUL4-DDB-RBX1 complex in response to
CC       ultraviolet irradiation. This may weaken the interaction between
CC       histones and DNA and facilitate DNA accessibility to repair
CC       proteins. Monoubiquitinated at Lys-92 of histone H4 (H4K91ub1) in
CC       response to DNA damage. The exact role of H4K91ub1 in DNA damage
CC       response is still unclear but it may function as a licensing
CC       signal for additional histone H4 post-translational modifications
CC       such as H4 Lys-21 methylation (H4K20me) (By similarity).
CC   -!- PTM: Sumoylated, which is associated with transcriptional
CC       repression (By similarity).
CC   -!- SIMILARITY: Belongs to the histone H4 family.
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DR   EMBL; V00753; CAA24130.1; -; Genomic_DNA.
DR   EMBL; X13235; CAA31621.1; -; Genomic_DNA.
DR   EMBL; X13236; CAA31622.1; -; Genomic_DNA.
DR   EMBL; U62672; AAB04766.1; -; Genomic_DNA.
DR   EMBL; Y12290; CAA72967.1; -; Genomic_DNA.
DR   EMBL; AY158956; AAO06266.1; -; Genomic_DNA.
DR   EMBL; AY158957; AAO06267.1; -; Genomic_DNA.
DR   EMBL; AY158958; AAO06268.1; -; Genomic_DNA.
DR   EMBL; AY158959; AAO06269.1; -; Genomic_DNA.
DR   EMBL; AY158960; AAO06270.1; -; Genomic_DNA.
DR   EMBL; AY158961; AAO06271.1; -; Genomic_DNA.
DR   EMBL; AY158962; AAO06272.1; -; Genomic_DNA.
DR   EMBL; AY158963; AAO06273.1; -; Genomic_DNA.
DR   EMBL; AY158964; AAO06274.1; -; Genomic_DNA.
DR   EMBL; AY158965; AAO06275.1; -; Genomic_DNA.
DR   EMBL; AY158966; AAO06276.1; -; Genomic_DNA.
DR   EMBL; AY158967; AAO06277.1; -; Genomic_DNA.
DR   EMBL; AK007642; BAB25157.1; -; mRNA.
DR   EMBL; AK010085; BAB26692.1; -; mRNA.
DR   EMBL; AK011560; BAB27698.1; -; mRNA.
DR   EMBL; AK139521; BAE24047.1; -; mRNA.
DR   EMBL; AL589651; CAI24108.1; -; Genomic_DNA.
DR   EMBL; AL589651; CAI24109.1; -; Genomic_DNA.
DR   EMBL; AL590388; CAI25838.1; -; Genomic_DNA.
DR   EMBL; AL590388; CAI25839.1; -; Genomic_DNA.
DR   EMBL; AL590614; CAI26128.1; -; Genomic_DNA.
DR   EMBL; BC028550; AAH28550.3; -; mRNA.
DR   EMBL; BC052219; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC057955; AAH57955.1; -; mRNA.
DR   EMBL; BC058529; AAH58529.2; -; mRNA.
DR   EMBL; BC087952; AAH87952.1; -; mRNA.
DR   EMBL; BC092144; AAH92144.1; -; mRNA.
DR   EMBL; BC115446; AAI15447.1; -; mRNA.
DR   EMBL; BC115447; AAI15448.1; -; mRNA.
DR   EMBL; BC115451; AAI15452.1; -; mRNA.
DR   EMBL; BC115448; AAI15449.1; -; mRNA.
DR   EMBL; BC115449; AAI15450.1; -; mRNA.
DR   EMBL; BC115450; AAI15451.1; -; mRNA.
DR   EMBL; BC117010; AAI17011.1; -; mRNA.
DR   EMBL; BC117012; AAI17013.1; -; mRNA.
DR   EMBL; BC111813; AAI11814.1; -; mRNA.
DR   EMBL; BC119241; AAI19242.1; -; mRNA.
DR   EMBL; BC119243; AAI19244.1; -; mRNA.
DR   EMBL; BC119611; AAI19612.1; -; mRNA.
DR   EMBL; BC119612; AAI19613.1; -; mRNA.
DR   EMBL; BC125598; AAI25599.1; -; mRNA.
DR   EMBL; BC125600; AAI25601.1; -; mRNA.
DR   EMBL; BC132186; AAI32187.1; -; mRNA.
DR   EMBL; BC132212; AAI32213.1; -; mRNA.
DR   EMBL; BC139809; AAI39810.1; -; mRNA.
DR   EMBL; BC152397; AAI52398.1; -; mRNA.
DR   IPI; IPI00407339; -.
DR   PIR; S03426; S03426.
DR   PIR; S03427; S03427.
DR   RefSeq; NP_001182350.1; NM_001195421.1.
DR   RefSeq; NP_291074.1; NM_033596.2.
DR   RefSeq; NP_694813.1; NM_153173.3.
DR   RefSeq; NP_783583.1; NM_175652.1.
DR   RefSeq; NP_783585.1; NM_175654.1.
DR   RefSeq; NP_783586.1; NM_175655.1.
DR   RefSeq; NP_783587.1; NM_175656.2.
DR   RefSeq; NP_783588.1; NM_175657.1.
DR   RefSeq; NP_835499.1; NM_178192.1.
DR   RefSeq; NP_835500.1; NM_178193.1.
DR   RefSeq; NP_835515.1; NM_178208.1.
DR   RefSeq; NP_835582.1; NM_178210.1.
DR   RefSeq; NP_835583.1; NM_178211.1.
DR   RefSeq; XP_981474.2; XM_976380.2.
DR   UniGene; Mm.144300; -.
DR   UniGene; Mm.14775; -.
DR   UniGene; Mm.158272; -.
DR   UniGene; Mm.227295; -.
DR   UniGene; Mm.228709; -.
DR   UniGene; Mm.246720; -.
DR   UniGene; Mm.255646; -.
DR   UniGene; Mm.260530; -.
DR   UniGene; Mm.261642; -.
DR   UniGene; Mm.261662; -.
DR   UniGene; Mm.261664; -.
DR   UniGene; Mm.377875; -.
DR   UniGene; Mm.442307; -.
DR   PDB; 1F66; X-ray; 2.60 A; B/F=1-103.
DR   PDB; 1U35; X-ray; 3.00 A; B/F=1-103.
DR   PDB; 2WP2; X-ray; 2.37 A; P/Q=2-21.
DR   PDBsum; 1F66; -.
DR   PDBsum; 1U35; -.
DR   PDBsum; 2WP2; -.
DR   ProteinModelPortal; P62806; -.
DR   SMR; P62806; 21-102.
DR   STRING; P62806; -.
DR   PhosphoSite; P62806; -.
DR   PRIDE; P62806; -.
DR   Ensembl; ENSMUST00000073009; ENSMUSP00000072770; ENSMUSG00000064288.
DR   Ensembl; ENSMUST00000075596; ENSMUSP00000075026; ENSMUSG00000060093.
DR   Ensembl; ENSMUST00000076545; ENSMUSP00000075860; ENSMUSG00000060678.
DR   Ensembl; ENSMUST00000078578; ENSMUSP00000077653; ENSMUSG00000060981.
DR   Ensembl; ENSMUST00000079030; ENSMUSP00000078039; ENSMUSG00000060639.
DR   Ensembl; ENSMUST00000079084; ENSMUSP00000078091; ENSMUSG00000061482.
DR   Ensembl; ENSMUST00000082036; ENSMUSP00000080695; ENSMUSG00000060832.
DR   Ensembl; ENSMUST00000087714; ENSMUSP00000085006; ENSMUSG00000067455.
DR   Ensembl; ENSMUST00000090778; ENSMUSP00000088283; ENSMUSG00000068851.
DR   Ensembl; ENSMUST00000091702; ENSMUSP00000089294; ENSMUSG00000069266.
DR   Ensembl; ENSMUST00000091713; ENSMUSP00000089305; ENSMUSG00000069274.
DR   Ensembl; ENSMUST00000091746; ENSMUSP00000089340; ENSMUSG00000069305.
DR   Ensembl; ENSMUST00000091747; ENSMUSP00000089341; ENSMUSG00000069306.
DR   Ensembl; ENSMUST00000102964; ENSMUSP00000100029; ENSMUSG00000060093.
DR   Ensembl; ENSMUST00000102965; ENSMUSP00000100030; ENSMUSG00000069266.
DR   Ensembl; ENSMUST00000102967; ENSMUSP00000100032; ENSMUSG00000060678.
DR   Ensembl; ENSMUST00000102968; ENSMUSP00000100033; ENSMUSG00000061482.
DR   Ensembl; ENSMUST00000102971; ENSMUSP00000100036; ENSMUSG00000069274.
DR   Ensembl; ENSMUST00000102972; ENSMUSP00000100037; ENSMUSG00000060981.
DR   Ensembl; ENSMUST00000102977; ENSMUSP00000100042; ENSMUSG00000060639.
DR   Ensembl; ENSMUST00000102979; ENSMUSP00000100044; ENSMUSG00000069305.
DR   Ensembl; ENSMUST00000102983; ENSMUSP00000100048; ENSMUSG00000064288.
DR   Ensembl; ENSMUST00000102984; ENSMUSP00000100049; ENSMUSG00000060832.
DR   Ensembl; ENSMUST00000104941; ENSMUSP00000100546; ENSMUSG00000069306.
DR   GeneID; 100041230; -.
DR   GeneID; 319155; -.
DR   GeneID; 319156; -.
DR   GeneID; 319157; -.
DR   GeneID; 319158; -.
DR   GeneID; 319159; -.
DR   GeneID; 319160; -.
DR   GeneID; 319161; -.
DR   GeneID; 320332; -.
DR   GeneID; 326619; -.
DR   GeneID; 326620; -.
DR   GeneID; 674678; -.
DR   GeneID; 69386; -.
DR   GeneID; 97122; -.
DR   KEGG; mmu:100041230; -.
DR   KEGG; mmu:319155; -.
DR   KEGG; mmu:319156; -.
DR   KEGG; mmu:319157; -.
DR   KEGG; mmu:319158; -.
DR   KEGG; mmu:319159; -.
DR   KEGG; mmu:319160; -.
DR   KEGG; mmu:319161; -.
DR   KEGG; mmu:320332; -.
DR   KEGG; mmu:326619; -.
DR   KEGG; mmu:326620; -.
DR   KEGG; mmu:674678; -.
DR   KEGG; mmu:69386; -.
DR   KEGG; mmu:97122; -.
DR   UCSC; uc007pre.1; mouse.
DR   CTD; 319155; -.
DR   CTD; 319156; -.
DR   CTD; 319157; -.
DR   CTD; 319158; -.
DR   CTD; 319159; -.
DR   CTD; 319160; -.
DR   CTD; 319161; -.
DR   CTD; 320332; -.
DR   CTD; 326619; -.
DR   CTD; 326620; -.
DR   CTD; 69386; -.
DR   CTD; 97122; -.
DR   MGI; MGI:2448419; Hist1h4a.
DR   MGI; MGI:2448420; Hist1h4b.
DR   MGI; MGI:2448421; Hist1h4c.
DR   MGI; MGI:2448423; Hist1h4d.
DR   MGI; MGI:2448425; Hist1h4f.
DR   MGI; MGI:2448427; Hist1h4h.
DR   MGI; MGI:2448432; Hist1h4i.
DR   MGI; MGI:2448436; Hist1h4j.
DR   MGI; MGI:2448439; Hist1h4k.
DR   MGI; MGI:2448441; Hist1h4m.
DR   MGI; MGI:2140113; Hist2h4.
DR   MGI; MGI:2448443; Hist4h4.
DR   eggNOG; roNOG16936; -.
DR   HOVERGEN; HBG051878; -.
DR   InParanoid; P62806; -.
DR   OrthoDB; EOG4KD6NP; -.
DR   PhylomeDB; P62806; -.
DR   NextBio; 450734; -.
DR   ArrayExpress; P62806; -.
DR   Bgee; P62806; -.
DR   CleanEx; MM_HIST1H4A; -.
DR   CleanEx; MM_HIST1H4B; -.
DR   CleanEx; MM_HIST1H4C; -.
DR   CleanEx; MM_HIST1H4D; -.
DR   CleanEx; MM_HIST1H4F; -.
DR   CleanEx; MM_HIST1H4H; -.
DR   CleanEx; MM_HIST1H4I; -.
DR   CleanEx; MM_HIST1H4J; -.
DR   CleanEx; MM_HIST1H4K; -.
DR   CleanEx; MM_HIST1H4M; -.
DR   CleanEx; MM_HIST2H4; -.
DR   CleanEx; MM_HIST4H4; -.
DR   Genevestigator; P62806; -.
DR   GermOnline; ENSMUSG00000060093; Mus musculus.
DR   GermOnline; ENSMUSG00000060639; Mus musculus.
DR   GermOnline; ENSMUSG00000060678; Mus musculus.
DR   GermOnline; ENSMUSG00000060832; Mus musculus.
DR   GermOnline; ENSMUSG00000060981; Mus musculus.
DR   GermOnline; ENSMUSG00000061482; Mus musculus.
DR   GermOnline; ENSMUSG00000064288; Mus musculus.
DR   GermOnline; ENSMUSG00000068851; Mus musculus.
DR   GermOnline; ENSMUSG00000069266; Mus musculus.
DR   GermOnline; ENSMUSG00000069274; Mus musculus.
DR   GermOnline; ENSMUSG00000069305; Mus musculus.
DR   GermOnline; ENSMUSG00000069306; Mus musculus.
DR   GO; GO:0000786; C:nucleosome; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR007125; Histone_core_D.
DR   InterPro; IPR001951; Histone_H4.
DR   InterPro; IPR019809; Histone_H4_CS.
DR   Gene3D; G3DSA:1.10.20.10; Histone-fold; 1.
DR   PANTHER; PTHR10484; Histone_H4; 1.
DR   Pfam; PF00125; Histone; 1.
DR   PRINTS; PR00623; HISTONEH4.
DR   SMART; SM00417; H4; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
DR   PROSITE; PS00047; HISTONE_H4; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Chromosome; Citrullination; DNA-binding;
KW   Isopeptide bond; Methylation; Nucleosome core; Nucleus;
KW   Phosphoprotein; Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    103       Histone H4.
FT                                /FTId=PRO_0000158329.
FT   DNA_BIND     17     21
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES       2      2       Phosphoserine.
FT   MOD_RES       4      4       Asymmetric dimethylarginine; by PRMT1;
FT                                alternate.
FT   MOD_RES       4      4       Citrulline; alternate (By similarity).
FT   MOD_RES       4      4       Omega-N-methylarginine; by PRMT1;
FT                                alternate (By similarity).
FT   MOD_RES       4      4       Symmetric dimethylarginine; by PRMT5 and
FT                                PRMT7; alternate.
FT   MOD_RES       6      6       N6-acetyllysine.
FT   MOD_RES       9      9       N6-acetyllysine.
FT   MOD_RES      13     13       N6-acetyllysine.
FT   MOD_RES      17     17       N6-acetyllysine.
FT   MOD_RES      21     21       N6,N6,N6-trimethyllysine; alternate.
FT   MOD_RES      21     21       N6,N6-dimethyllysine; alternate (By
FT                                similarity).
FT   MOD_RES      21     21       N6-methyllysine; alternate (By
FT                                similarity).
FT   MOD_RES      32     32       N6-acetyllysine (By similarity).
FT   MOD_RES      48     48       Phosphoserine.
FT   MOD_RES      52     52       Phosphotyrosine.
FT   MOD_RES      60     60       N6-acetyllysine (By similarity).
FT   MOD_RES      89     89       Phosphotyrosine.
FT   MOD_RES      92     92       N6-acetyllysine; alternate (By
FT                                similarity).
FT   CROSSLNK     92     92       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin);
FT                                alternate (By similarity).
FT   CONFLICT     34     34       A -> V (in Ref. 6; BAB26692).
FT   CONFLICT     80     80       K -> E (in Ref. 6; BAB27698).
FT   CONFLICT     90     90       A -> R (in Ref. 2; CAA31622).
FT   TURN         26     29
FT   HELIX        32     41
FT   HELIX        51     76
FT   STRAND       80     82
FT   HELIX        84     93
FT   STRAND       97    100
SQ   SEQUENCE   103 AA;  11367 MW;  A9E5DFD3F8B97598 CRC64;
     MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK
     VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG
//
ID   GBRA1_MOUSE             Reviewed;         455 AA.
AC   P62812; P18504;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit alpha-1;
DE   AltName: Full=GABA(A) receptor subunit alpha-1;
DE   Flags: Precursor;
GN   Name=Gabra1; Synonyms=Gabra-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J, and DBA/2J; TISSUE=Brain;
RX   MEDLINE=93002190; PubMed=1356407;
RA   Wang J.B., Kofuji P., Fernando J.C., Moss S.J., Huganir R.L.,
RA   Burt D.R.;
RT   "The alpha 1, alpha 2, and alpha 3 subunits of GABAA receptors:
RT   comparison in seizure-prone and -resistant mice and during
RT   development.";
RL   J. Mol. Neurosci. 3:177-184(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=91169549; PubMed=1848528; DOI=10.1016/0888-7543(91)90272-G;
RA   Keir W.J., Kozak C.A., Chakraborti A., Deitrich R.A., Sikela J.M.;
RT   "The cDNA sequence and chromosomal location of the murine GABAA alpha
RT   1 receptor gene.";
RL   Genomics 9:390-395(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c;
RX   PubMed=12106288; DOI=10.1111/j.1460-9568.1990.tb00460.x;
RA   Kato K.;
RT   "A collection of cDNA clones with specific expression patterns in
RT   mouse brain.";
RL   Eur. J. Neurosci. 2:704-711(1990).
RN   [4]
RP   INTERACTION WITH TRAK1.
RX   PubMed=16380713; DOI=10.1038/ng1715;
RA   Gilbert S.L., Zhang L., Forster M.L., Anderson J.R., Iwase T.,
RA   Soliven B., Donahue L.R., Sweet H.O., Bronson R.T., Davisson M.T.,
RA   Wollmann R.L., Lahn B.T.;
RT   "Trak1 mutation disrupts GABA(A) receptor homeostasis in hypertonic
RT   mice.";
RL   Nat. Genet. 38:245-250(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-367, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-374, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: GABA, the major inhibitory neurotransmitter in the
CC       vertebrate brain, mediates neuronal inhibition by binding to the
CC       GABA/benzodiazepine receptor and opening an integral chloride
CC       channel.
CC   -!- SUBUNIT: Generally pentameric. There are five types of GABA(A)
CC       receptor chains: alpha, beta, gamma, delta, and rho. Binds UBQLN1.
CC       Interacts with TRAK1.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane; Multi-pass membrane protein. Cell membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
CC       family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily.
CC       GABRA1 sub-subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; M86566; AAB59634.1; -; mRNA.
DR   EMBL; M63436; AAA37654.1; -; mRNA.
DR   EMBL; X61430; CAA43672.1; -; mRNA.
DR   IPI; IPI00113772; -.
DR   PIR; A39062; A39062.
DR   RefSeq; NP_034380.1; NM_010250.4.
DR   UniGene; Mm.439668; -.
DR   ProteinModelPortal; P62812; -.
DR   SMR; P62812; 278-338.
DR   STRING; P62812; -.
DR   PhosphoSite; P62812; -.
DR   PRIDE; P62812; -.
DR   Ensembl; ENSMUST00000020707; ENSMUSP00000020707; ENSMUSG00000010803.
DR   GeneID; 14394; -.
DR   KEGG; mmu:14394; -.
DR   UCSC; uc007imf.1; mouse.
DR   CTD; 14394; -.
DR   MGI; MGI:95613; Gabra1.
DR   eggNOG; roNOG07582; -.
DR   HOGENOM; HBG506497; -.
DR   HOVERGEN; HBG051707; -.
DR   InParanoid; P62812; -.
DR   OMA; MXAYTRA; -.
DR   OrthoDB; EOG4ZS935; -.
DR   PhylomeDB; P62812; -.
DR   NextBio; 285923; -.
DR   ArrayExpress; P62812; -.
DR   Bgee; P62812; -.
DR   Genevestigator; P62812; -.
DR   GermOnline; ENSMUSG00000010803; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0004890; F:GABA-A receptor activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IEA:InterPro.
DR   InterPro; IPR006028; GABAA_rcpt.
DR   InterPro; IPR001390; GABAAa_rcpt.
DR   InterPro; IPR005431; GABBAa1_rcpt.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   Gene3D; G3DSA:2.70.170.10; Neur_chan_lig_bd; 1.
DR   PANTHER; PTHR18945; Neur_channel; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 2.
DR   PRINTS; PR01079; GABAARALPHA.
DR   PRINTS; PR01614; GABAARALPHA1.
DR   PRINTS; PR00253; GABAARECEPTR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF90112; Neu_channel_TM; 1.
DR   SUPFAM; SSF63712; Neur_chan_LBD; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Chloride; Chloride channel;
KW   Disulfide bond; Glycoprotein; Ion transport; Ionic channel;
KW   Ligand-gated ion channel; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Receptor; Signal; Synapse; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     27       Potential.
FT   CHAIN        28    455       Gamma-aminobutyric acid receptor subunit
FT                                alpha-1.
FT                                /FTId=PRO_0000000429.
FT   TOPO_DOM     28    250       Extracellular (Probable).
FT   TRANSMEM    251    272       Helical; (Probable).
FT   TRANSMEM    278    299       Helical; (Probable).
FT   TRANSMEM    312    333       Helical; (Probable).
FT   TOPO_DOM    334    420       Cytoplasmic (Probable).
FT   TRANSMEM    421    442       Helical; (Probable).
FT   MOD_RES     367    367       Phosphotyrosine.
FT   MOD_RES     374    374       Phosphotyrosine.
FT   CARBOHYD     37     37       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    137    137       N-linked (GlcNAc...) (Potential).
FT   DISULFID    165    179       By similarity.
SQ   SEQUENCE   455 AA;  51754 MW;  A270B43423B4086E CRC64;
     MKKSRGLSDY LWAWTLILST LSGRSYGQPS QDELKDNTTV FTRILDRLLD GYDNRLRPGL
     GERVTEVKTD IFVTSFGPVS DHDMEYTIDV FFRQSWKDER LKFKGPMTVL RLNNLMASKI
     WTPDTFFHNG KKSVAHNMTM PNKLLRITED GTLLYTMRLT VRAECPMHLE DFPMDAHACP
     LKFGSYAYTR AEVVYEWTRE PARSVVVAED GSRLNQYDLL GQTVDSGIVQ SSTGEYVVMT
     THFHLKRKIG YFVIQTYLPC IMTVILSQVS FWLNRESVPA RTVFGVTTVL TMTTLSISAR
     NSLPKVAYAT AMDWFIAVCY AFVFSALIEF ATVNYFTKRG YAWDGKSVVP EKPKKVKDPL
     IKKNNTYAPT ATSYTPNLAR GDPGLATIAK SATIEPKEVK PETKPPEPKK TFNSVSKIDR
     LSRIAFPLLF GIFNLVYWAT YLNREPQLKA PTPHQ
//
ID   VATB2_MOUSE             Reviewed;         511 AA.
AC   P62814; O09045; P50517; Q3TG74; Q3TL62; Q3TVK6; Q3TWR0; Q3U791;
AC   Q3U7C8; Q3U9Z0; Q3UAW7;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=V-type proton ATPase subunit B, brain isoform;
DE            Short=V-ATPase subunit B 2;
DE   AltName: Full=Endomembrane proton pump 58 kDa subunit;
DE   AltName: Full=Vacuolar proton pump subunit B 2;
GN   Name=Atp6v1b2; Synonyms=Atp6b2, Vat2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=96362668; PubMed=8741845;
RA   Laitala T., Howell M.L., Dean G.E., Vaananen H.K.;
RT   "Resorption-cycle-dependent polarization of mRNAs for different
RT   subunits of V-ATPase in bone-resorbing osteoclasts.";
RL   Mol. Biol. Cell 7:129-142(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RA   Westberg M.S., Lundberg L.G.;
RT   "Antisense technology and bone resorption.";
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Amnion, Bone marrow, Brain, and Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 49-64; 68-130; 164-185; 189-208; 277-308; 322-337;
RP   387-400; 404-430; 437-457; 461-485 AND 495-506, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Yang J.W., Zigmond M., Kang S.U., Sunyer B.,
RA   Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Non-catalytic subunit of the peripheral V1 complex of
CC       vacuolar ATPase. V-ATPase is responsible for acidifying a variety
CC       of intracellular compartments in eukaryotic cells.
CC   -!- SUBUNIT: V-ATPase is an heteromultimeric enzyme composed of a
CC       peripheral catalytic V1 complex (main components: subunits A, B,
CC       C, D, E, and F) attached to an integral membrane V0 proton pore
CC       complex (main component: the proteolipid protein).
CC   -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane
CC       protein. Melanosome (By similarity). Note=Endomembrane.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE30303.1; Type=Erroneous initiation;
CC       Sequence=BAE30526.1; Type=Erroneous initiation;
CC       Sequence=BAE31441.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; U13838; AAC52411.1; -; Genomic_DNA.
DR   EMBL; Y12634; CAA73182.1; -; mRNA.
DR   EMBL; AK146499; BAE27215.1; -; mRNA.
DR   EMBL; AK151200; BAE30197.1; -; mRNA.
DR   EMBL; AK151322; BAE30303.1; ALT_INIT; mRNA.
DR   EMBL; AK151586; BAE30526.1; ALT_INIT; mRNA.
DR   EMBL; AK152718; BAE31441.1; ALT_INIT; mRNA.
DR   EMBL; AK152766; BAE31479.1; -; mRNA.
DR   EMBL; AK159133; BAE34845.1; -; mRNA.
DR   EMBL; AK159153; BAE34860.1; -; mRNA.
DR   EMBL; AK159586; BAE35206.1; -; mRNA.
DR   EMBL; AK159701; BAE35300.1; -; mRNA.
DR   EMBL; AK159986; BAE35536.1; -; mRNA.
DR   EMBL; AK160080; BAE35612.1; -; mRNA.
DR   EMBL; AK160854; BAE36047.1; -; mRNA.
DR   EMBL; AK166669; BAE38930.1; -; mRNA.
DR   EMBL; AK168852; BAE40674.1; -; mRNA.
DR   EMBL; AK169155; BAE40934.1; -; mRNA.
DR   EMBL; AK169270; BAE41031.1; -; mRNA.
DR   EMBL; BC012497; AAH12497.1; -; mRNA.
DR   EMBL; BC046302; AAH46302.1; -; mRNA.
DR   EMBL; BC085300; AAH85300.1; -; mRNA.
DR   IPI; IPI00119113; -.
DR   RefSeq; NP_031535.2; NM_007509.3.
DR   UniGene; Mm.249096; -.
DR   UniGene; Mm.392573; -.
DR   ProteinModelPortal; P62814; -.
DR   SMR; P62814; 53-507.
DR   STRING; P62814; -.
DR   PhosphoSite; P62814; -.
DR   REPRODUCTION-2DPAGE; P62814; -.
DR   UCD-2DPAGE; P62814; -.
DR   PRIDE; P62814; -.
DR   Ensembl; ENSMUST00000006435; ENSMUSP00000006435; ENSMUSG00000006273.
DR   GeneID; 11966; -.
DR   KEGG; mmu:11966; -.
DR   UCSC; uc009lwx.1; mouse.
DR   CTD; 11966; -.
DR   MGI; MGI:109618; Atp6v1b2.
DR   eggNOG; roNOG13128; -.
DR   GeneTree; ENSGT00550000074724; -.
DR   HOVERGEN; HBG002176; -.
DR   InParanoid; P62814; -.
DR   OMA; RQAKVRG; -.
DR   OrthoDB; EOG4HMJ93; -.
DR   PhylomeDB; P62814; -.
DR   BRENDA; 3.6.3.14; 244.
DR   NextBio; 280091; -.
DR   ArrayExpress; P62814; -.
DR   Bgee; P62814; -.
DR   CleanEx; MM_ATP6V1B2; -.
DR   Genevestigator; P62814; -.
DR   GermOnline; ENSMUSG00000006273; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR   GO; GO:0046933; F:hydrogen ion transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR000194; ATPase_a/bsu_nucl-bd.
DR   InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C.
DR   InterPro; IPR004100; ATPase_F1/V1/A1-cplx_a/bsu_N.
DR   InterPro; IPR005723; ATPase_V1-cplx_bsu.
DR   InterPro; IPR022879; V-ATPase_su_B/beta.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF00306; ATP-synt_ab_C; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   TIGRFAMs; TIGR01040; V-ATPase_V1_B; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrogen ion transport; Hydrolase;
KW   Ion transport; Membrane; Phosphoprotein; Transport.
FT   CHAIN         1    511       V-type proton ATPase subunit B, brain
FT                                isoform.
FT                                /FTId=PRO_0000144627.
FT   MOD_RES     404    404       Phosphoserine.
FT   MOD_RES     498    498       Phosphoserine.
FT   CONFLICT     22     23       GG -> RP (in Ref. 1; AAC52411).
FT   CONFLICT     36     36       S -> G (in Ref. 1; AAC52411).
FT   CONFLICT     80     80       T -> A (in Ref. 3; BAE35206).
FT   CONFLICT     85     86       QV -> AS (in Ref. 1; AAC52411).
FT   CONFLICT    262    264       NLA -> ILP (in Ref. 1; AAC52411).
FT   CONFLICT    270    270       E -> K (in Ref. 3; BAE35536/BAE35612).
FT   CONFLICT    276    276       R -> C (in Ref. 1; AAC52411).
FT   CONFLICT    300    300       M -> T (in Ref. 1; AAC52411).
FT   CONFLICT    304    304       A -> P (in Ref. 1; AAC52411).
FT   CONFLICT    318    318       P -> H (in Ref. 3; BAE35536/BAE35612).
FT   CONFLICT    365    365       I -> M (in Ref. 3; BAE40674).
FT   CONFLICT    371    371       Y -> C (in Ref. 3; BAE35206).
FT   CONFLICT    373    373       T -> I (in Ref. 3; BAE30303/BAE30526).
FT   CONFLICT    405    405       A -> P (in Ref. 1; AAC52411).
FT   CONFLICT    437    437       A -> V (in Ref. 3; BAE30197).
SQ   SEQUENCE   511 AA;  56551 MW;  E116BF9A36EEF36B CRC64;
     MALRAMRGIV NGAAPELPVP TGGPMAGARE QALAVSRNYL SQPRLTYKTV SGVNGPLVIL
     DHVKFPRYAE IVHLTLPDGT KRSGQVLEVS GSKAVVQVFE GTSGIDAKKT SCEFTGDILR
     TPVSEDMLGR VFNGSGKPID RGPVVLAEDF LDIMGQPINP QCRIYPEEMI QTGISAIDGM
     NSIARGQKIP IFSAAGLPHN EIAAQICRQA GLVKKSKDVV DYSEENFAIV FAAMGVNMET
     ARFFKSDFEE NGSMDNVCLF LNLANDPTIE RIITPRLALT TAEFLAYQCE KHVLVILTDM
     SSYAEALREV SAAREEVPGR RGFPGYMYTD LATIYERAGR VEGRNGSITQ IPILTMPNDD
     ITHPIPDLTG YITEGQIYVD RQLHNRQIYP PINVLPSLSR LMKSAIGEGM TRKDHADVSN
     QLYACYAIGK DVQAMKAVVG EEALTSDDLL YLEFLQKFEK NFITQGPYEN RTVYETLDIG
     WQLLRIFPKE MLKRIPQSTL SEFYPRDSAK H
//
ID   RAB1A_MOUSE             Reviewed;         205 AA.
AC   P62821; P11476; Q3TX44; Q811M4; Q96N61; Q9Y3T2;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   30-NOV-2010, entry version 76.
DE   RecName: Full=Ras-related protein Rab-1A;
DE   AltName: Full=YPT1-related protein;
GN   Name=Rab1A; Synonyms=Rab1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=88166649; PubMed=3127202;
RA   Haubruck H., Disela C., Wagner P., Gallwitz D.;
RT   "The ras-related ypt protein is an ubiquitous eukaryotic protein:
RT   isolation and sequence analysis of mouse cDNA clones highly homologous
RT   to the yeast YPT1 gene.";
RL   EMBO J. 6:4049-4053(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=89386011; PubMed=2506528; DOI=10.1093/nar/17.16.6737;
RA   Wichmann H., Disela C., Haubruck H., Gallwitz D.;
RT   "Nucleotide sequence of the mouse ypt1 gene encoding a ras-related
RT   GTP-binding protein.";
RL   Nucleic Acids Res. 17:6737-6738(1989).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wu G., Dorn G.W. II;
RT   "Mouse Rab1A, member of RAS oncogene family mRNA.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon, and Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 14-24; 31-49; 62-72; 75-103; 112-125 AND 132-156,
RP   AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Probably required for transit of protein from the ER
CC       through Golgi compartment. Binds GTP and GDP and possesses
CC       intrinsic GTPase activity.
CC   -!- SUBUNIT: May interact with YIPF5 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus. Endoplasmic reticulum.
CC   -!- PTM: Phosphorylated by CDK1 kinase during mitosis (By similarity).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR   EMBL; Y00094; CAA68284.1; -; mRNA.
DR   EMBL; X15744; CAA33760.1; -; Genomic_DNA.
DR   EMBL; X15745; CAA33760.1; JOINED; Genomic_DNA.
DR   EMBL; X15746; CAA33760.1; JOINED; Genomic_DNA.
DR   EMBL; X15747; CAA33760.1; JOINED; Genomic_DNA.
DR   EMBL; AF226873; AAF33844.1; -; mRNA.
DR   EMBL; AK034408; BAC28697.1; -; mRNA.
DR   EMBL; AK159425; BAE35072.1; -; mRNA.
DR   EMBL; AK166249; BAE38660.1; -; mRNA.
DR   EMBL; AK167150; BAE39292.1; -; mRNA.
DR   EMBL; BC002077; AAH02077.3; -; mRNA.
DR   IPI; IPI00114560; -.
DR   PIR; S05551; TVMSYP.
DR   RefSeq; NP_033022.1; NM_008996.3.
DR   UniGene; Mm.271944; -.
DR   ProteinModelPortal; P62821; -.
DR   SMR; P62821; 3-176.
DR   STRING; P62821; -.
DR   PhosphoSite; P62821; -.
DR   PRIDE; P62821; -.
DR   Ensembl; ENSMUST00000074741; ENSMUSP00000074301; ENSMUSG00000020149.
DR   GeneID; 19324; -.
DR   KEGG; mmu:19324; -.
DR   UCSC; uc007icv.1; mouse.
DR   CTD; 19324; -.
DR   MGI; MGI:97842; Rab1.
DR   eggNOG; roNOG07724; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; P62821; -.
DR   OMA; IVVYDCT; -.
DR   PhylomeDB; P62821; -.
DR   NextBio; 296283; -.
DR   ArrayExpress; P62821; -.
DR   Bgee; P62821; -.
DR   CleanEx; MM_RAB1; -.
DR   Genevestigator; P62821; -.
DR   GermOnline; ENSMUSG00000020149; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Endoplasmic reticulum;
KW   ER-Golgi transport; Golgi apparatus; GTP-binding; Lipoprotein;
KW   Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW   Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    205       Ras-related protein Rab-1A.
FT                                /FTId=PRO_0000121057.
FT   NP_BIND      18     26       GTP (By similarity).
FT   NP_BIND      66     70       GTP (By similarity).
FT   NP_BIND     124    127       GTP (By similarity).
FT   NP_BIND     154    156       GTP (By similarity).
FT   MOTIF        40     48       Effector region (By similarity).
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES     194    194       Phosphoserine; by CDK1 (By similarity).
FT   LIPID       204    204       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   LIPID       205    205       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   205 AA;  22678 MW;  B2A8F4E3B0FB17D6 CRC64;
     MSSMNPEYDY LFKLLLIGDS GVGKSCLLLR FADDTYTESY ISTIGVDFKI RTIELDGKTI
     KLQIWDTAGQ ERFRTITSSY YRGAHGIIVV YDVTDQESFN NVKQWLQEID RYASENVNKL
     LVGNKCDLTT KKVVDYTTAK EFADSLGIPF LETSAKNATN VEQSFMTMAA EIKKRMGPGA
     TAGGAEKSNV KIQSTPVKQS GGGCC
//
ID   RAB3C_MOUSE             Reviewed;         227 AA.
AC   P62823; Q62858; Q62974; Q63482; Q9CXQ1;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Ras-related protein Rab-3C;
GN   Name=Rab3c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Wang X., Hu B., Kilimann M.W.;
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Schluter O.M., Benseler F., Suedhof T.C.;
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Embryo;
RA   Pavlos N.J., Xu J., Zheng M.H.;
RT   "Molecular cloning and tissue expression of the mouse homolog of
RT   Rab3C.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PROTEIN SEQUENCE OF 1-16; 21-43; 50-68; 81-91; 161-175 AND 187-209,
RP   AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Protein transport. Probably involved in vesicular
CC       traffic (By similarity).
CC   -!- SUBUNIT: Binds RIMS1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR   EMBL; AJ310532; CAC32042.1; -; mRNA.
DR   EMBL; AF312037; AAG60047.1; -; mRNA.
DR   EMBL; AY026947; AAK08980.1; -; mRNA.
DR   EMBL; AK014132; BAB29172.1; -; mRNA.
DR   IPI; IPI00316495; -.
DR   RefSeq; NP_076341.1; NM_023852.5.
DR   UniGene; Mm.151600; -.
DR   ProteinModelPortal; P62823; -.
DR   SMR; P62823; 26-194.
DR   STRING; P62823; -.
DR   PRIDE; P62823; -.
DR   Ensembl; ENSMUST00000022210; ENSMUSP00000022210; ENSMUSG00000021700.
DR   GeneID; 67295; -.
DR   KEGG; mmu:67295; -.
DR   UCSC; uc007rvo.1; mouse.
DR   CTD; 67295; -.
DR   MGI; MGI:1914545; Rab3c.
DR   eggNOG; roNOG14692; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; P62823; -.
DR   OMA; MQMASSQ; -.
DR   OrthoDB; EOG4TB4C6; -.
DR   PhylomeDB; P62823; -.
DR   NextBio; 324148; -.
DR   ArrayExpress; P62823; -.
DR   Bgee; P62823; -.
DR   CleanEx; MM_RAB3C; -.
DR   Genevestigator; P62823; -.
DR   GermOnline; ENSMUSG00000021700; Mus musculus.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0017157; P:regulation of exocytosis; IDA:MGI.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; GTP-binding; Lipoprotein;
KW   Membrane; Methylation; Nucleotide-binding; Prenylation;
KW   Protein transport; Transport.
FT   CHAIN         1    227       Ras-related protein Rab-3C.
FT                                /FTId=PRO_0000121086.
FT   NP_BIND      37     44       GTP (By similarity).
FT   NP_BIND      85     89       GTP (By similarity).
FT   NP_BIND     143    146       GTP (By similarity).
FT   MOTIF        59     67       Effector region (By similarity).
FT   MOD_RES     227    227       Cysteine methyl ester (By similarity).
FT   LIPID       225    225       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   LIPID       227    227       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   227 AA;  25872 MW;  179DF4D9B451B7B0 CRC64;
     MRHEAPMQMA SAQDARFGQK DSSDQNFDYM FKLLIIGNSS VGKTSFLFRY ADDSFTSAFV
     STVGIDFKVK TVFKNEKRIK LQIWDTAGQE RYRTITTAYY RGAMGFILMY DITNEESFNA
     VQDWSTQIKT YSWDNAQVIL AGNKCDMEDE RVVSTERGQR LGEQLGFEFF ETSAKDNINV
     KQTFERLVDI ICDKMSESLE TDPAITAAKQ STRLKETPPP PQPNCGC
//
ID   ELOB_MOUSE              Reviewed;         118 AA.
AC   P62869; Q63529; Q80W20;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Transcription elongation factor B polypeptide 2;
DE   AltName: Full=Elongin 18 kDa subunit;
DE   AltName: Full=Elongin-B;
DE            Short=EloB;
DE   AltName: Full=RNA polymerase II transcription factor SIII subunit B;
DE   AltName: Full=SIII p18;
GN   Name=Tceb2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryo, Hippocampus, Kidney, and Small intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH SOCS1.
RX   MEDLINE=99162559; PubMed=10051596; DOI=10.1073/pnas.96.5.2071;
RA   Zhang J.-G., Farley A., Nicholson S.E., Willson T.A., Zugaro L.M.,
RA   Simpson R.J., Moritz R.L., Cary D., Richardson R., Hausmann G.,
RA   Kile B.J., Kent S.B.H., Alexander W.S., Metcalf D., Hilton D.J.,
RA   Nicola N.A., Baca M.;
RT   "The conserved SOCS box motif in suppressors of cytokine signaling
RT   binds to elongins B and C and may couple bound proteins to proteasomal
RT   degradation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:2071-2076(1999).
RN   [4]
RP   IDENTIFICATION IN E3 UBIQUITIN LIGASE COMPLEXES.
RX   MEDLINE=21380117; PubMed=11384984; DOI=10.1074/jbc.M103093200;
RA   Kamura T., Burian D., Yan Q., Schmidt S.L., Lane W.S., Querido E.,
RA   Branton P.E., Shilatifard A., Conaway R.C., Conaway J.W.;
RT   "Muf1, a novel elongin BC-interacting leucine-rich repeat protein that
RT   can assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase.";
RL   J. Biol. Chem. 276:29748-29753(2001).
CC   -!- FUNCTION: SIII, also known as elongin, is a general transcription
CC       elongation factor that increases the RNA polymerase II
CC       transcription elongation past template-encoded arresting sites.
CC       Subunit A is transcriptionally active and its transcription
CC       activity is strongly enhanced by binding to the dimeric complex of
CC       the SIII regulatory subunits B and C (elongin BC complex).
CC   -!- FUNCTION: The elongin BC complex seems to be involved as an
CC       adapter protein in the proteasomal degradation of target proteins
CC       via different E3 ubiquitin ligase complexes, including the von
CC       Hippel-Lindau ubiquitination complex CBC(VHL). By binding to BC-
CC       box motifs it seems to link target recruitment subunits, like VHL
CC       and members of the SOCS box family, to Cullin/RBX1 modules that
CC       activate E2 ubiquitination enzymes.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Heterotrimer of an A (A1, A2 or A3), B and C subunit.
CC       Part of E3 ubiquitin ligase complexes with CUL5 or CUL2, RBX1 and
CC       a substrate adapter protein that can be either SOCS1, TCEB3, VHL
CC       or WSB1. Interacts with VHL.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- SIMILARITY: Contains 1 ubiquitin-like domain.
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DR   EMBL; AK019358; BAB31677.1; -; mRNA.
DR   EMBL; AK002223; BAB21946.1; -; mRNA.
DR   EMBL; AK002868; BAB22417.1; -; mRNA.
DR   EMBL; AK003277; BAB22684.1; -; mRNA.
DR   EMBL; AK008477; BAB25690.1; -; mRNA.
DR   EMBL; AK008534; BAB25727.1; -; mRNA.
DR   EMBL; AK012254; BAB28121.1; -; mRNA.
DR   EMBL; AK019181; BAB31590.1; -; mRNA.
DR   EMBL; AK019218; BAB31608.1; -; mRNA.
DR   EMBL; BC051927; AAH51927.2; -; mRNA.
DR   EMBL; BC056983; AAH56983.1; -; mRNA.
DR   IPI; IPI00131224; -.
DR   RefSeq; NP_080581.1; NM_026305.2.
DR   UniGene; Mm.153758; -.
DR   PDB; 2FNJ; X-ray; 1.80 A; B=1-118.
DR   PDBsum; 2FNJ; -.
DR   ProteinModelPortal; P62869; -.
DR   SMR; P62869; 1-98.
DR   MINT; MINT-2789207; -.
DR   STRING; P62869; -.
DR   REPRODUCTION-2DPAGE; P62869; -.
DR   PRIDE; P62869; -.
DR   Ensembl; ENSMUST00000069579; ENSMUSP00000066210; ENSMUSG00000055839.
DR   GeneID; 67673; -.
DR   KEGG; mmu:67673; -.
DR   UCSC; uc008atr.1; mouse.
DR   CTD; 67673; -.
DR   MGI; MGI:1914923; Tceb2.
DR   eggNOG; maNOG20078; -.
DR   GeneTree; ENSGT00390000018316; -.
DR   HOGENOM; HBG564567; -.
DR   HOVERGEN; HBG008581; -.
DR   InParanoid; P62869; -.
DR   OrthoDB; EOG4BG8X6; -.
DR   NextBio; 325215; -.
DR   Bgee; P62869; -.
DR   Genevestigator; P62869; -.
DR   GermOnline; ENSMUSG00000055839; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR000626; Ubiquitin.
DR   InterPro; IPR019955; Ubiquitin_supergroup.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SMART; SM00213; UBQ; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Nucleus; Transcription;
KW   Transcription regulation; Ubl conjugation pathway.
FT   CHAIN         1    118       Transcription elongation factor B
FT                                polypeptide 2.
FT                                /FTId=PRO_0000114915.
FT   DOMAIN        1     79       Ubiquitin-like.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   STRAND        2     10
FT   STRAND       12     19
FT   HELIX        24     35
FT   HELIX        39     41
FT   STRAND       42     46
FT   HELIX        57     60
FT   TURN         64     66
FT   STRAND       73     83
SQ   SEQUENCE   118 AA;  13170 MW;  BA702F24CEC0FC02 CRC64;
     MDVFLMIRRH KTTIFTDAKE SSTVFELKRI VEGILKRPPE EQRLYKDDQL LDDGKTLGEC
     GFTSQTARPQ APATVGLAFR ADDTFEALRI EPFSSPPELP DVMKPQDSGG SANEQAVQ
//
ID   GBB1_MOUSE              Reviewed;         340 AA.
AC   P62874; P04697; P04901;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1;
DE   AltName: Full=Transducin beta chain 1;
GN   Name=Gnb1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Adrenal gland;
RA   Qiu R., Schimmer B.P.;
RL   Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv; TISSUE=Liver;
RX   MEDLINE=21910454; PubMed=11913780;
RA   Kitanaka J., Wang X., Kitanaka N., Hembree C.M., Uhl G.R.;
RT   "Genomic organization of the murine G protein beta subunit genes and
RT   related processed pseudogenes.";
RL   DNA Seq. 12:345-354(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 24-42; 58-96; 138-150; 198-209 AND 284-301, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC       involved as a modulator or transducer in various transmembrane
CC       signaling systems. The beta and gamma chains are required for the
CC       GTPase activity, for replacement of GDP by GTP, and for G protein-
CC       effector interaction (By similarity).
CC   -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and
CC       gamma. Interacts with ARHGEF18 and RASD2 (By similarity).
CC   -!- PTM: Phosphorylation at His-266 by NDKB contributes to G protein
CC       activation by increasing the high energetic phosphate transfer
CC       onto GDP (By similarity).
CC   -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC   -!- SIMILARITY: Contains 7 WD repeats.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U29055; AAC52905.1; -; mRNA.
DR   EMBL; AB042854; BAB63904.1; -; Genomic_DNA.
DR   EMBL; BC013058; AAH13058.1; -; mRNA.
DR   IPI; IPI00120716; -.
DR   PIR; JC5057; JC5057.
DR   RefSeq; NP_001153488.1; NM_001160016.1.
DR   RefSeq; NP_001153489.1; NM_001160017.1.
DR   RefSeq; NP_032168.1; NM_008142.4.
DR   UniGene; Mm.2344; -.
DR   ProteinModelPortal; P62874; -.
DR   SMR; P62874; 1-340.
DR   STRING; P62874; -.
DR   PhosphoSite; P62874; -.
DR   PRIDE; P62874; -.
DR   Ensembl; ENSMUST00000030940; ENSMUSP00000030940; ENSMUSG00000029064.
DR   Ensembl; ENSMUST00000105616; ENSMUSP00000101241; ENSMUSG00000029064.
DR   GeneID; 14688; -.
DR   KEGG; mmu:14688; -.
DR   UCSC; uc008wdp.1; mouse.
DR   CTD; 14688; -.
DR   MGI; MGI:95781; Gnb1.
DR   eggNOG; roNOG13354; -.
DR   HOGENOM; HBG396231; -.
DR   HOVERGEN; HBG000188; -.
DR   InParanoid; P62874; -.
DR   OMA; NQIREAR; -.
DR   OrthoDB; EOG4HX51D; -.
DR   PhylomeDB; P62874; -.
DR   NextBio; 286631; -.
DR   ArrayExpress; P62874; -.
DR   Bgee; P62874; -.
DR   Genevestigator; P62874; -.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IPI:MGI.
DR   GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0007200; P:activation of phospholipase C activity by G-protein coupled receptor protein signaling pathway coupled to IP3 second messenger; IDA:MGI.
DR   GO; GO:0008283; P:cell proliferation; IDA:MGI.
DR   GO; GO:0050909; P:sensory perception of taste; IDA:MGI.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR001632; Gprotein_B.
DR   InterPro; IPR016346; Guanine_nucleotide-bd_bsu.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 7.
DR   PIRSF; PIRSF002394; GN-bd_beta; 1.
DR   PRINTS; PR00319; GPROTEINB.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 3.
DR   PROSITE; PS50082; WD_REPEATS_2; 6.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Phosphoprotein; Repeat;
KW   Transducer; WD repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    340       Guanine nucleotide-binding protein
FT                                G(I)/G(S)/G(T) subunit beta-1.
FT                                /FTId=PRO_0000127688.
FT   REPEAT       53     83       WD 1.
FT   REPEAT       95    125       WD 2.
FT   REPEAT      141    170       WD 3.
FT   REPEAT      182    212       WD 4.
FT   REPEAT      224    254       WD 5.
FT   REPEAT      268    298       WD 6.
FT   REPEAT      310    340       WD 7.
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES     266    266       Phosphohistidine (By similarity).
SQ   SEQUENCE   340 AA;  37377 MW;  896CBD32D2686598 CRC64;
     MSELDQLRQE AEQLKNQIRD ARKACADATL SQITNNIDPV GRIQMRTRRT LRGHLAKIYA
     MHWGTDSRLL VSASQDGKLI IWDSYTTNKV HAIPLRSSWV MTCAYAPSGN YVACGGLDNI
     CSIYNLKTRE GNVRVSRELA GHTGYLSCCR FLDDNQIVTS SGDTTCALWD IETGQQTTTF
     TGHTGDVMSL SLAPDTRLFV SGACDASAKL WDVREGMCRQ TFTGHESDIN AICFFPNGNA
     FATGSDDATC RLFDLRADQE LMTYSHDNII CGITSVSFSK SGRLLLAGYD DFNCNVWDAL
     KADRAGVLAG HDNRVSCLGV TDDGMAVATG SWDSFLKIWN
//
ID   GBB2_MOUSE              Reviewed;         340 AA.
AC   P62880; P11016; P54312;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2;
DE   AltName: Full=G protein subunit beta-2;
DE   AltName: Full=Transducin beta chain 2;
GN   Name=Gnb2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/Kaplan;
RA   Kuroda S., Tokunaga C., Konishi H., Kikkawa U.;
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   MEDLINE=21910454; PubMed=11913780;
RA   Kitanaka J., Wang X., Kitanaka N., Hembree C.M., Uhl G.R.;
RT   "Genomic organization of the murine G protein beta subunit genes and
RT   related processed pseudogenes.";
RL   DNA Seq. 12:345-354(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=21138439; PubMed=11239002; DOI=10.1093/nar/29.6.1352;
RA   Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P.,
RA   Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C.,
RA   Miller W., Koop B.F.;
RT   "Comparative analysis of the gene-dense ACHE/TFR2 region on human
RT   chromosome 7q22 with the orthologous region on mouse chromosome 5.";
RL   Nucleic Acids Res. 29:1352-1365(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon, and Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 23-42; 58-96; 138-150; 198-209; 257-280 AND
RP   284-301, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 182-297, AND DEVELOPMENTAL STAGE.
RC   STRAIN=CF-1;
RX   MEDLINE=97011591; PubMed=8858601;
RX   DOI=10.1002/(SICI)1098-2795(199607)44:3<315::AID-MRD5>3.3.CO;2-V;
RA   Williams C.J., Schultz R.M., Kopf G.S.;
RT   "G protein gene expression during mouse oocyte growth and maturation,
RT   and preimplantation embryo development.";
RL   Mol. Reprod. Dev. 44:315-323(1996).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-239, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC       involved as a modulator or transducer in various transmembrane
CC       signaling systems. The beta and gamma chains are required for the
CC       GTPase activity, for replacement of GDP by GTP, and for G protein-
CC       effector interaction.
CC   -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and
CC       gamma. Interacts with ARHGEF18 and RASD2 (By similarity).
CC       Interacts with ATXN10 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region (By
CC       similarity).
CC   -!- DEVELOPMENTAL STAGE: Expressed in meiotically incompetent oocytes.
CC       Expression increases in fully grown meiotically competent oocytes.
CC       Expression then decreases during metaphase-II arrested eggs, one-
CC       cell embryo, two-cell embryo and eight-cell embryo stages, and
CC       increases again during blastocyst stage.
CC   -!- SIMILARITY: Belongs to the WD repeat G protein beta family.
CC   -!- SIMILARITY: Contains 7 WD repeats.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U34960; AAC72250.1; -; mRNA.
DR   EMBL; AB045007; BAB19816.1; -; Genomic_DNA.
DR   EMBL; AF312033; AAK28828.1; -; Genomic_DNA.
DR   EMBL; BC029077; AAH29077.1; -; mRNA.
DR   EMBL; BC059942; AAH59942.1; -; mRNA.
DR   EMBL; BC062178; AAH62178.1; -; mRNA.
DR   EMBL; U38505; AAB01736.1; -; mRNA.
DR   IPI; IPI00162780; -.
DR   RefSeq; NP_034442.1; NM_010312.4.
DR   UniGene; Mm.30141; -.
DR   ProteinModelPortal; P62880; -.
DR   SMR; P62880; 1-340.
DR   STRING; P62880; -.
DR   PhosphoSite; P62880; -.
DR   REPRODUCTION-2DPAGE; IPI00162780; -.
DR   PRIDE; P62880; -.
DR   Ensembl; ENSMUST00000031726; ENSMUSP00000031726; ENSMUSG00000029713.
DR   Ensembl; ENSMUST00000111027; ENSMUSP00000106656; ENSMUSG00000029713.
DR   GeneID; 14693; -.
DR   KEGG; mmu:14693; -.
DR   UCSC; uc009act.1; mouse.
DR   CTD; 14693; -.
DR   MGI; MGI:95784; Gnb2.
DR   eggNOG; roNOG13354; -.
DR   HOGENOM; HBG396231; -.
DR   HOVERGEN; HBG000188; -.
DR   InParanoid; P62880; -.
DR   OrthoDB; EOG4HX51D; -.
DR   PhylomeDB; P62880; -.
DR   NextBio; 286635; -.
DR   ArrayExpress; P62880; -.
DR   Bgee; P62880; -.
DR   Genevestigator; P62880; -.
DR   GermOnline; ENSMUSG00000029713; Mus musculus.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; TAS:MGI.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR001632; Gprotein_B.
DR   InterPro; IPR016346; Guanine_nucleotide-bd_bsu.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 7.
DR   PIRSF; PIRSF002394; GN-bd_beta; 1.
DR   PRINTS; PR00319; GPROTEINB.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 3.
DR   PROSITE; PS50082; WD_REPEATS_2; 6.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW   Repeat; Transducer; WD repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    340       Guanine nucleotide-binding protein
FT                                G(I)/G(S)/G(T) subunit beta-2.
FT                                /FTId=PRO_0000127696.
FT   REPEAT       53     83       WD 1.
FT   REPEAT       95    125       WD 2.
FT   REPEAT      141    170       WD 3.
FT   REPEAT      182    212       WD 4.
FT   REPEAT      224    254       WD 5.
FT   REPEAT      268    298       WD 6.
FT   REPEAT      310    340       WD 7.
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES     239    239       Phosphotyrosine.
FT   CONFLICT    106    106       A -> G (in Ref. 1; AAC72250).
FT   CONFLICT    248    248       A -> S (in Ref. 1; AAC72250).
SQ   SEQUENCE   340 AA;  37331 MW;  5D08FFA240ADEEE6 CRC64;
     MSELEQLRQE AEQLRNQIRD ARKACGDSTL TQITAGLDPV GRIQMRTRRT LRGHLAKIYA
     MHWGTDSRLL VSASQDGKLI IWDSYTTNKV HAIPLRSSWV MTCAYAPSGN FVACGGLDNI
     CSIYSLKTRE GNVRVSRELP GHTGYLSCCR FLDDNQIITS SGDTTCALWD IETGQQTVGF
     AGHSGDVMSL SLAPDGRTFV SGACDASIKL WDVRDSMCRQ TFIGHESDIN AVAFFPNGYA
     FTTGSDDATC RLFDLRADQE LLMYSHDNII CGITSVAFSR SGRLLLAGYD DFNCNIWDAM
     KGDRAGVLAG HDNRVSCLGV TDDGMAVATG SWDSFLKIWN
//
ID   CYC_MOUSE               Reviewed;         105 AA.
AC   P62897; P00009; Q8C2S2;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Cytochrome c, somatic;
GN   Name=Cycs;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=85215501; PubMed=2987801; DOI=10.1093/nar/13.2.617;
RA   Limbach K.J., Wu R.;
RT   "Characterization of a mouse somatic cytochrome c gene and three
RT   cytochrome c pseudogenes.";
RL   Nucleic Acids Res. 13:617-630(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-105, AND ACETYLATION AT GLY-2.
RC   STRAIN=BALB/c;
RX   MEDLINE=77134768; PubMed=191069; DOI=10.1021/bi00626a031;
RA   Carlson S.S., Mross G.A., Wilson A.C., Mead R.T., Wolin L.D.,
RA   Bowers S.F., Foley N.T., Muijsers A.O., Margoliash E.;
RT   "Primary structure of mouse, rat, and guinea pig cytochrome c.";
RL   Biochemistry 16:1437-1442(1977).
RN   [5]
RP   PROTEIN SEQUENCE OF 29-54; 57-74; 81-88 AND 93-100, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   AMINO-ACID COMPOSITION OF TRYPTIC PEPTIDES.
RC   STRAIN=BALB/c;
RX   MEDLINE=76022386; PubMed=240690;
RX   DOI=10.1111/j.1432-1033.1975.tb02149.x;
RA   Hennig B.;
RT   "Change of cytochrome c structure during development of the mouse.";
RL   Eur. J. Biochem. 55:167-183(1975).
CC   -!- FUNCTION: Electron carrier protein. The oxidized form of the
CC       cytochrome c heme group can accept an electron from the heme group
CC       of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c
CC       then transfers this electron to the cytochrome oxidase complex,
CC       the final protein carrier in the mitochondrial electron-transport
CC       chain.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- TISSUE SPECIFICITY: Found in embryos and in adult liver and heart.
CC   -!- PTM: Binds 1 heme group per subunit.
CC   -!- SIMILARITY: Belongs to the cytochrome c family.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Life shuttle - Issue 76
CC       of November 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt076.shtml";
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DR   EMBL; X01756; CAA25899.1; -; Genomic_DNA.
DR   EMBL; AK088098; BAC40143.1; -; mRNA.
DR   EMBL; BC034363; AAH34363.1; -; mRNA.
DR   IPI; IPI00222419; -.
DR   PIR; A23057; CCMS.
DR   RefSeq; NP_031834.1; NM_007808.4.
DR   RefSeq; XP_001478454.1; XM_001478404.2.
DR   UniGene; Mm.35389; -.
DR   UniGene; Mm.391918; -.
DR   ProteinModelPortal; P62897; -.
DR   SMR; P62897; 2-105.
DR   STRING; P62897; -.
DR   PhosphoSite; P62897; -.
DR   PRIDE; P62897; -.
DR   Ensembl; ENSMUST00000073080; ENSMUSP00000072829; ENSMUSG00000058927.
DR   GeneID; 13063; -.
DR   GeneID; 672195; -.
DR   KEGG; mmu:13063; -.
DR   KEGG; mmu:672195; -.
DR   UCSC; uc009bxc.1; mouse.
DR   CTD; 13063; -.
DR   MGI; MGI:88578; Cycs.
DR   eggNOG; roNOG16909; -.
DR   HOGENOM; HBG692582; -.
DR   HOVERGEN; HBG003023; -.
DR   InParanoid; P62897; -.
DR   OMA; GATVFKK; -.
DR   OrthoDB; EOG45DWQX; -.
DR   PhylomeDB; P62897; -.
DR   NextBio; 282990; -.
DR   ArrayExpress; P62897; -.
DR   Bgee; P62897; -.
DR   CleanEx; MM_CYCS; -.
DR   Genevestigator; P62897; -.
DR   GermOnline; ENSMUSG00000058927; Mus musculus.
DR   GermOnline; ENSMUSG00000063694; Mus musculus.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002327; Cyt_c_1A/1B.
DR   InterPro; IPR009056; Cyt_c_dom.
DR   InterPro; IPR003088; Cyt_c_I.
DR   Gene3D; G3DSA:1.10.760.10; Cytochrome_c_R; 1.
DR   PANTHER; PTHR11961; Cyt_CIAB; 1.
DR   Pfam; PF00034; Cytochrom_C; 1.
DR   PRINTS; PR00604; CYTCHRMECIAB.
DR   SUPFAM; SSF46626; Cytochrome_c; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Heme;
KW   Iron; Metal-binding; Mitochondrion; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    105       Cytochrome c, somatic.
FT                                /FTId=PRO_0000108225.
FT   METAL        19     19       Iron (heme axial ligand).
FT   METAL        81     81       Iron (heme axial ligand).
FT   BINDING      15     15       Heme (covalent).
FT   BINDING      18     18       Heme (covalent).
FT   MOD_RES       2      2       N-acetylglycine.
SQ   SEQUENCE   105 AA;  11605 MW;  B5BCA779BCE40492 CRC64;
     MGDVEKGKKI FVQKCAQCHT VEKGGKHKTG PNLHGLFGRK TGQAAGFSYT DANKNKGITW
     GEDTLMEYLE NPKKYIPGTK MIFAGIKKKG ERADLIAYLK KATNE
//
ID   RS3_MOUSE               Reviewed;         243 AA.
AC   P62908; P17073; P47933;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=40S ribosomal protein S3;
GN   Name=Rps3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RA   Harper M., Terol-Garay E., Hraba-Renevey S., Kress M.M.;
RT   "Primary sequence of the mouse ribosomal protein S3.";
RL   Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-221, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SUBUNIT: Identified in a mRNP granule complex, at least composed
CC       of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD,
CC       HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1,
CC       NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8,
CC       RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=Localized in
CC       cytoplasmic mRNP granules containing untranslated mRNAs (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the ribosomal protein S3P family.
CC   -!- SIMILARITY: Contains 1 KH type-2 domain.
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DR   EMBL; X76772; CAA54167.1; -; mRNA.
DR   EMBL; BC010721; AAH10721.1; -; mRNA.
DR   IPI; IPI00134599; -.
DR   PIR; S41170; S41170.
DR   RefSeq; NP_036182.1; NM_012052.2.
DR   UniGene; Mm.236868; -.
DR   ProteinModelPortal; P62908; -.
DR   SMR; P62908; 2-193.
DR   STRING; P62908; -.
DR   PhosphoSite; P62908; -.
DR   PRIDE; P62908; -.
DR   Ensembl; ENSMUST00000032998; ENSMUSP00000032998; ENSMUSG00000030744.
DR   GeneID; 27050; -.
DR   KEGG; mmu:27050; -.
DR   UCSC; uc009ilr.1; mouse.
DR   CTD; 27050; -.
DR   MGI; MGI:1350917; Rps3.
DR   HOGENOM; HBG748975; -.
DR   HOVERGEN; HBG002195; -.
DR   InParanoid; P62908; -.
DR   OMA; TGERAKS; -.
DR   OrthoDB; EOG4GXFNJ; -.
DR   PhylomeDB; P62908; -.
DR   NextBio; 304983; -.
DR   ArrayExpress; P62908; -.
DR   Bgee; P62908; -.
DR   CleanEx; MM_RPS3; -.
DR   Genevestigator; P62908; -.
DR   GermOnline; ENSMUSG00000030744; Mus musculus.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR009019; KH_prok-type.
DR   InterPro; IPR004044; KH_type_2.
DR   InterPro; IPR001351; Ribosomal_S3_C.
DR   InterPro; IPR018280; Ribosomal_S3_CS.
DR   InterPro; IPR005703; Ribosomal_S3_euk/arc.
DR   Gene3D; G3DSA:3.30.300.20; KH_prok; 1.
DR   Gene3D; G3DSA:3.30.1140.32; Ribosomal_S3_C; 1.
DR   Pfam; PF07650; KH_2; 1.
DR   Pfam; PF00189; Ribosomal_S3_C; 1.
DR   SMART; SM00322; KH; 1.
DR   SUPFAM; SSF54814; KH_prok; 1.
DR   SUPFAM; SSF54821; Ribosomal_S3_C; 1.
DR   TIGRFAMs; TIGR01008; rpsC_E_A; 1.
DR   PROSITE; PS50823; KH_TYPE_2; 1.
DR   PROSITE; PS00548; RIBOSOMAL_S3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Isopeptide bond; Phosphoprotein;
KW   Ribonucleoprotein; Ribosomal protein; RNA-binding; Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    243       40S ribosomal protein S3.
FT                                /FTId=PRO_0000130321.
FT   DOMAIN       21     92       KH type-2.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      62     62       N6-acetyllysine (By similarity).
FT   MOD_RES     166    166       Phosphotyrosine (By similarity).
FT   MOD_RES     220    220       Phosphothreonine (By similarity).
FT   MOD_RES     221    221       Phosphothreonine.
FT   MOD_RES     224    224       Phosphoserine (By similarity).
FT   MOD_RES     242    242       Phosphothreonine (By similarity).
FT   CROSSLNK     90     90       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK    202    202       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
SQ   SEQUENCE   243 AA;  26674 MW;  6B9BB34FDEE04AAF CRC64;
     MAVQISKKRK FVADGIFKAE LNEFLTRELA EDGYSGVEVR VTPTRTEIII LATRTQNVLG
     EKGRRIRELT AVVQKRFGFP EGSVELYAEK VATRGLCAIA QAESLRYKLL GGLAVRRACY
     GVLRFIMESG AKGCEVVVSG KLRGQRAKSM KFVDGLMIHS GDPVNYYVDT AVRHVLLRQG
     VLGIKVKIML PWDPSGKIGP KKPLPDHVSI VEPKDEILPT TPISEQKGGK PEPPAMPQPV
     PTA
//
ID   CCG7_MOUSE              Reviewed;         275 AA.
AC   P62956; Q8VBX3; Q8WXS6; Q9BXT1;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Voltage-dependent calcium channel gamma-7 subunit;
DE   AltName: Full=Neuronal voltage-gated calcium channel gamma-7 subunit;
GN   Name=Cacng7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=21601102; PubMed=11738816; DOI=10.1016/S0378-1119(01)00738-7;
RA   Chu P.-J., Robertson H.M., Best P.M.;
RT   "Calcium channel gamma subunits provide insights into the evolution of
RT   this gene family.";
RL   Gene 280:37-48(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=TKDU;
RX   MEDLINE=21924683; PubMed=11927536; DOI=10.1093/emboj/21.7.1514;
RA   Moss F.J., Viard P., Davies A., Bertaso F., Page K.M., Graham A.,
RA   Canti C., Plumpton M., Plumpton C., Clare J.J., Dolphin A.C.;
RT   "The novel product of a five-exon stargazin-related gene abolishes
RT   CaV2.2 calcium channel expression.";
RL   EMBO J. 21:1514-1523(2002).
CC   -!- FUNCTION: Thought to stabilize the calcium channel in an
CC       inactivated (closed) state (By similarity).
CC   -!- SUBUNIT: The L-type calcium channel is composed of five subunits:
CC       alpha-1, alpha-2/delta, beta and gamma.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG
CC       subfamily.
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DR   EMBL; AF361349; AAL50044.1; -; mRNA.
DR   EMBL; AF458899; AAM00596.1; -; mRNA.
DR   IPI; IPI00140061; -.
DR   RefSeq; NP_573452.3; NM_133189.3.
DR   UniGene; Mm.214994; -.
DR   ProteinModelPortal; P62956; -.
DR   STRING; P62956; -.
DR   PRIDE; P62956; -.
DR   Ensembl; ENSMUST00000092891; ENSMUSP00000090567; ENSMUSG00000069806.
DR   GeneID; 81904; -.
DR   KEGG; mmu:81904; -.
DR   UCSC; uc009euu.1; mouse.
DR   CTD; 81904; -.
DR   MGI; MGI:1932374; Cacng7.
DR   eggNOG; maNOG19721; -.
DR   HOGENOM; HBG446234; -.
DR   HOVERGEN; HBG025923; -.
DR   InParanoid; P62956; -.
DR   OMA; FSTRALT; -.
DR   OrthoDB; EOG40S0G8; -.
DR   NextBio; 350469; -.
DR   ArrayExpress; P62956; -.
DR   Bgee; P62956; -.
DR   Genevestigator; P62956; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005262; F:calcium channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   InterPro; IPR008371; VDCC_g7su.
DR   InterPro; IPR008368; VDCC_gsu.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01792; VDCCGAMMA.
DR   PRINTS; PR01795; VDCCGAMMA7.
PE   2: Evidence at transcript level;
KW   Calcium; Calcium channel; Calcium transport; Ion transport;
KW   Ionic channel; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    275       Voltage-dependent calcium channel gamma-7
FT                                subunit.
FT                                /FTId=PRO_0000164688.
FT   TRANSMEM      8     28       Helical; (Potential).
FT   TRANSMEM    103    123       Helical; (Potential).
FT   TRANSMEM    129    149       Helical; (Potential).
FT   TRANSMEM    179    199       Helical; (Potential).
FT   MOD_RES     258    258       Phosphotyrosine (By similarity).
FT   MOD_RES     264    264       Phosphotyrosine (By similarity).
SQ   SEQUENCE   275 AA;  31003 MW;  43CC82B9FA6A5C73 CRC64;
     MSHCSSRALT LLSSVFGACG LLLVGIAVST DYWLYMEEGT VLPQNQTTEV KMALHAGLWR
     VCFFAGREKG RCVASEYFLE PEINLVTENT ENILKTVRTA TPFPMVSLFL VFTAFVISNI
     GHIRPQRTIL AFVSGIFFIL SGLSLVVGLV LYISSINDEV MNRPSSSEQY FHYRYGWSFA
     FAASSFLLKE GAGVMSVYLF TKRYAEEEMY RPHPAFYRPR LSDCSDYSGQ FLQPEAWRRG
     RSPSDISSDV SIQMTQNYPP AIKYPDHLHI STSPC
//
ID   RS27A_MOUSE             Reviewed;         156 AA.
AC   P62983; P02248; P02249; P02250; P49664; P62991; Q29120; Q62317;
AC   Q64223; Q8VCH1; Q91887; Q91888; Q9CXY4; Q9CZM0; Q9D1R5; Q9D2W3;
AC   Q9D8D9; Q9ET23; Q9ET24; Q9Z0H9;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Ubiquitin-40S ribosomal protein S27a;
DE   AltName: Full=Ubiquitin carboxyl extension protein 80;
DE   Contains:
DE     RecName: Full=Ubiquitin;
DE   Contains:
DE     RecName: Full=40S ribosomal protein S27a;
DE   Flags: Precursor;
GN   Name=Rps27a; Synonyms=Uba80, Ubcep1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Liver, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   REVIEW, AND FUNCTION.
RX   PubMed=19754430; DOI=10.1042/BST0370937;
RA   Komander D.;
RT   "The emerging complexity of protein ubiquitination.";
RL   Biochem. Soc. Trans. 37:937-953(2009).
CC   -!- FUNCTION: Ubiquitin exists either covalently attached to another
CC       protein, or free (unanchored). When covalently bound, it is
CC       conjugated to target proteins via an isopeptide bond either as a
CC       monomer (monoubiquitin), a polymer linked via different Lys
CC       residues of the ubiquitin (polyubiquitin chains) or a linear
CC       polymer linked via the initiator Met of the ubiquitin (linear
CC       polyubiquitin chains). Polyubiquitin chains, when attached to a
CC       target protein, have different functions depending on the Lys
CC       residue of the ubiquitin that is linked: Lys-6-linked may be
CC       involved in DNA repair; Lys-11-linked is involved in ERAD
CC       (endoplasmic reticulum-associated degradation) and in cell-cycle
CC       regulation; Lys-29-linked is involved in lysosomal degradation;
CC       Lys-33-linked is involved in kinase modification; Lys-48-linked is
CC       involved in protein degradation via the proteasome; Lys-63-linked
CC       is involved in endocytosis, DNA-damage responses as well as in
CC       signaling processes leading to activation of the transcription
CC       factor NF-kappa-B. Linear polymer chains formed via attachment by
CC       the initiator Met lead to cell signaling. Ubiquitin is usually
CC       conjugated to Lys residues of target proteins, however, in rare
CC       cases, conjugation to Cys or Ser residues has been observed. When
CC       polyubiquitin is free (unanchored-polyubiquitin), it also has
CC       distinct roles, such as in activation of protein kinases, and in
CC       signaling.
CC   -!- FUNCTION: Ribosomal protein S27a is a component of the 40S subunit
CC       of the ribosome.
CC   -!- SUBUNIT: Ribosomal protein S27a is part of the 40S ribosomal
CC       subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Ubiquitin: Cytoplasm (By similarity).
CC       Nucleus (By similarity).
CC   -!- MISCELLANEOUS: Ubiquitin is encoded by 4 different genes. Uba52
CC       and Rps27a genes code for a single copy of ubiquitin fused to the
CC       ribosomal proteins L40 and S27a, respectively. UBB and UBC genes
CC       code for a polyubiquitin precursor with exact head to tail
CC       repeats, the number of repeats differ between species and strains.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin
CC       family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the ribosomal
CC       protein S27Ae family.
CC   -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK018706; BAB31357.1; -; mRNA.
DR   EMBL; BC002108; AAH02108.1; -; mRNA.
DR   IPI; IPI00470152; -.
DR   RefSeq; NP_001029037.1; NM_001033865.1.
DR   RefSeq; NP_077239.1; NM_024277.2.
DR   UniGene; Mm.180003; -.
DR   UniGene; Mm.350435; -.
DR   UniGene; Mm.458088; -.
DR   ProteinModelPortal; P62983; -.
DR   SMR; P62983; 1-76, 100-156.
DR   STRING; P62983; -.
DR   REPRODUCTION-2DPAGE; P62991; -.
DR   PRIDE; P62991; -.
DR   Ensembl; ENSMUST00000078766; ENSMUSP00000077824; ENSMUSG00000058838.
DR   Ensembl; ENSMUST00000102844; ENSMUSP00000099908; ENSMUSG00000020460.
DR   Ensembl; ENSMUST00000102845; ENSMUSP00000099909; ENSMUSG00000020460.
DR   GeneID; 78294; -.
DR   KEGG; mmu:78294; -.
DR   CTD; 619900; -.
DR   CTD; 78294; -.
DR   MGI; MGI:1925544; Rps27a.
DR   InParanoid; P62991; -.
DR   OrthoDB; EOG4PZJ82; -.
DR   PhylomeDB; P62991; -.
DR   Reactome; REACT_24972; Circadian Clock (mouse).
DR   Bgee; P62983; -.
DR   CleanEx; MM_RPS27A; -.
DR   CleanEx; MM_UBB; -.
DR   CleanEx; MM_UBC; -.
DR   Genevestigator; P62991; -.
DR   GermOnline; ENSMUSG00000008348; Mus musculus.
DR   GermOnline; ENSMUSG00000019505; Mus musculus.
DR   GermOnline; ENSMUSG00000020460; Mus musculus.
DR   GermOnline; ENSMUSG00000044285; Mus musculus.
DR   GermOnline; ENSMUSG00000058838; Mus musculus.
DR   GermOnline; ENSMUSG00000061390; Mus musculus.
DR   GermOnline; ENSMUSG00000063789; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR002906; Ribosomal_S27a.
DR   InterPro; IPR000626; Ubiquitin.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_subgroup.
DR   InterPro; IPR019955; Ubiquitin_supergroup.
DR   Pfam; PF01599; Ribosomal_S27; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM00213; UBQ; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Isopeptide bond; Metal-binding; Nucleus;
KW   Phosphoprotein; Ribonucleoprotein; Ribosomal protein; Ubl conjugation;
KW   Zinc; Zinc-finger.
FT   CHAIN         1     76       Ubiquitin.
FT                                /FTId=PRO_0000396479.
FT   CHAIN        77    156       40S ribosomal protein S27a.
FT                                /FTId=PRO_0000137663.
FT   DOMAIN        1     76       Ubiquitin-like.
FT   ZN_FING     121    144       C4-type.
FT   COMPBIAS     77     99       Lys-rich (highly basic).
FT   COMPBIAS     78    107       Lys-rich.
FT   BINDING      54     54       Activating enzyme.
FT   BINDING      72     72       Activating enzyme.
FT   SITE         68     68       Essential for function.
FT   MOD_RES       6      6       N6-acetyllysine (By similarity).
FT   MOD_RES      48     48       N6-acetyllysine (By similarity).
FT   MOD_RES      57     57       Phosphoserine.
FT   MOD_RES      65     65       Phosphoserine (By similarity).
FT   MOD_RES     104    104       N6-acetyllysine (By similarity).
FT   MOD_RES     107    107       N6-acetyllysine (By similarity).
FT   MOD_RES     113    113       N6-acetyllysine (By similarity).
FT   CROSSLNK      6      6       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK     11     11       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK     27     27       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK     29     29       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK     33     33       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK     48     48       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK     63     63       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK     76     76       Glycyl lysine isopeptide (Gly-Lys)
FT                                (interchain with K-? in acceptor
FT                                proteins) (By similarity).
SQ   SEQUENCE   156 AA;  17951 MW;  C11DC63DF3A904F3 CRC64;
     MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
     IQKESTLHLV LRLRGGAKKR KKKSYTTPKK NKHKRKKVKL AVLKYYKVDE NGKISRLRRE
     CPSDECGAGV FMGSHFDRHY CGKCCLTYCF NKPEDK
//
ID   TRA2B_MOUSE             Reviewed;         288 AA.
AC   P62996; O15449; Q15815; Q64283;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Transformer-2 protein homolog beta;
DE            Short=TRA-2 beta;
DE            Short=TRA2-beta;
DE   AltName: Full=Silica-induced gene 41 protein;
DE            Short=SIG-41;
DE   AltName: Full=Splicing factor, arginine/serine-rich 10;
DE   AltName: Full=Transformer-2 protein homolog B;
GN   Name=Tra2b; Synonyms=Sfrs10, Silg41;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
RC   TISSUE=Macrophage;
RX   MEDLINE=95173444; PubMed=7868905;
RA   Segade F., Claudio E., Wrobel K., Ramos S., Lazo P.S.;
RT   "Isolation of nine gene sequences induced by silica in murine
RT   macrophages.";
RL   J. Immunol. 154:2384-2392(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   PubMed=8674539; DOI=10.1016/0014-5793(96)00496-6;
RA   Segade F., Hurle B., Claudio E., Ramos S., Lazo P.S.;
RT   "Molecular cloning of a mouse homologue for the Drosophila splicing
RT   regulator Tra2.";
RL   FEBS Lett. 387:152-156(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264 AND SER-266, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-201; SER-264 AND
RP   SER-266, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-4; SER-14;
RP   SER-50; SER-52; SER-54; SER-56; SER-83; SER-85; SER-264; SER-266 AND
RP   SER-284, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264 AND SER-266, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Sequence-specific RNA-binding protein which participates
CC       in the control of pre-mRNA splicing (By similarity).
CC   -!- SUBUNIT: Found in a pre-mRNA exonic splicing enhancer (ESE)
CC       complex with TRA2B/SFRS10, SNRNP70, SNRPA1 and SRRM1. Binds to A3
CC       enhancer proteins SFRS4, SFRS5, SFRS6 and SFRS9. Interacts with
CC       CPSF6, RBMY1A1, RNPS1, SAFB/SAFB1 and phosphorylated SFRS13A (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P62996-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P62996-2; Sequence=VSP_011509, VSP_011510;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in uterus
CC       and brain.
CC   -!- INDUCTION: Induced by reoxygenation following hypoxia and by
CC       exposure to silica. Repressed by interferon gamma, LPS and TPA.
CC   -!- SIMILARITY: Belongs to the splicing factor SR family.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; X80232; CAA56518.1; -; mRNA.
DR   EMBL; AK049573; BAC33819.1; -; mRNA.
DR   EMBL; AK077418; BAC36791.1; -; mRNA.
DR   EMBL; AK080378; BAC37898.1; -; mRNA.
DR   EMBL; BC061177; AAH61177.1; -; mRNA.
DR   IPI; IPI00139259; -.
DR   IPI; IPI00457594; -.
DR   PIR; S68798; S68798.
DR   RefSeq; NP_033212.1; NM_009186.4.
DR   UniGene; Mm.210352; -.
DR   UniGene; Mm.389440; -.
DR   UniGene; Mm.442193; -.
DR   ProteinModelPortal; P62996; -.
DR   SMR; P62996; 109-191.
DR   STRING; P62996; -.
DR   PhosphoSite; P62996; -.
DR   PRIDE; P62996; -.
DR   Ensembl; ENSMUST00000023564; ENSMUSP00000023564; ENSMUSG00000022858.
DR   GeneID; 20462; -.
DR   KEGG; mmu:20462; -.
DR   UCSC; uc007ysc.1; mouse.
DR   CTD; 20462; -.
DR   MGI; MGI:106016; Tra2b.
DR   eggNOG; roNOG12342; -.
DR   GeneTree; ENSGT00550000074314; -.
DR   HOGENOM; HBG756718; -.
DR   HOVERGEN; HBG104971; -.
DR   InParanoid; P62996; -.
DR   OMA; YSGERRR; -.
DR   OrthoDB; EOG4BVRW2; -.
DR   PhylomeDB; P62996; -.
DR   NextBio; 298551; -.
DR   ArrayExpress; P62996; -.
DR   Bgee; P62996; -.
DR   Genevestigator; P62996; -.
DR   GermOnline; ENSMUSG00000022858; Mus musculus.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000398; P:nuclear mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Methylation; mRNA processing; mRNA splicing;
KW   Nucleus; Phosphoprotein; RNA-binding.
FT   CHAIN         1    288       Transformer-2 protein homolog beta.
FT                                /FTId=PRO_0000081984.
FT   DOMAIN      118    196       RRM.
FT   REGION      193    230       Linker.
FT   COMPBIAS     31    113       Arg/Ser-rich (RS1 domain).
FT   COMPBIAS    231    287       Arg/Ser-rich (RS2 domain).
FT   MOD_RES       2      2       Phosphoserine.
FT   MOD_RES       4      4       Phosphoserine.
FT   MOD_RES      14     14       Phosphoserine.
FT   MOD_RES      29     29       Phosphoserine (By similarity).
FT   MOD_RES      33     33       Phosphothreonine (By similarity).
FT   MOD_RES      37     37       Phosphoserine (By similarity).
FT   MOD_RES      39     39       Phosphoserine (By similarity).
FT   MOD_RES      50     50       Phosphoserine.
FT   MOD_RES      52     52       Phosphoserine.
FT   MOD_RES      54     54       Phosphoserine.
FT   MOD_RES      56     56       Phosphoserine.
FT   MOD_RES      69     69       Phosphothreonine (By similarity).
FT   MOD_RES      71     71       Phosphoserine (By similarity).
FT   MOD_RES      83     83       Phosphoserine.
FT   MOD_RES      85     85       Phosphoserine.
FT   MOD_RES      87     87       Phosphoserine (By similarity).
FT   MOD_RES      95     95       Phosphoserine (By similarity).
FT   MOD_RES      97     97       Phosphoserine (By similarity).
FT   MOD_RES      99     99       Phosphoserine (By similarity).
FT   MOD_RES     201    201       Phosphothreonine.
FT   MOD_RES     207    207       Phosphotyrosine (By similarity).
FT   MOD_RES     212    212       Phosphothreonine (By similarity).
FT   MOD_RES     215    215       Phosphoserine (By similarity).
FT   MOD_RES     216    216       Phosphoserine (By similarity).
FT   MOD_RES     241    241       Dimethylated arginine (By similarity).
FT   MOD_RES     264    264       Phosphoserine.
FT   MOD_RES     266    266       Phosphoserine.
FT   MOD_RES     268    268       Phosphotyrosine (By similarity).
FT   MOD_RES     269    269       Phosphotyrosine (By similarity).
FT   MOD_RES     276    276       Phosphoserine (By similarity).
FT   MOD_RES     280    280       Phosphoserine (By similarity).
FT   MOD_RES     282    282       Phosphoserine (By similarity).
FT   MOD_RES     284    284       Phosphoserine.
FT   VAR_SEQ      23     38       AHGSGKSARHTPARSR -> RHLTSFINEYLKLRNK (in
FT                                isoform 2).
FT                                /FTId=VSP_011509.
FT   VAR_SEQ      39    288       Missing (in isoform 2).
FT                                /FTId=VSP_011510.
SQ   SEQUENCE   288 AA;  33666 MW;  60B310C8BA443E28 CRC64;
     MSDSGEQNYG ERESRSASRS GSAHGSGKSA RHTPARSRSK EDSRRSRSKS RSRSESRSRS
     RRSSRRHYTR SRSRSRSHRR SRSRSYSRDY RRRHSHSHSP MSTRRRHVGN RANPDPNCCL
     GVFGLSLYTT ERDLREVFSK YGPIADVSIV YDQQSRRSRG FAFVYFENVD DAKEAKERAN
     GMELDGRRIR VDFSITKRPH TPTPGIYMGR PTYGSSRRRD YYDRGYDRGY DDRDYYSRSY
     RGGGGGGGGW RAAQDRDQIY RRRSPSPYYS RGGYRSRSRS RSYSPRRY
//
ID   RAC1_MOUSE              Reviewed;         192 AA.
AC   P63001; O95501; P15154; Q9BTB4;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Ras-related C3 botulinum toxin substrate 1;
DE   AltName: Full=p21-Rac1;
DE   Flags: Precursor;
GN   Name=Rac1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Thymus;
RX   MEDLINE=91270906; PubMed=1905006;
RA   Moll J., Sansig G., Fattori E., van der Putten H.;
RT   "The murine rac1 gene: cDNA cloning, tissue distribution and regulated
RT   expression of rac1 mRNA by disassembly of actin microfilaments.";
RL   Oncogene 6:863-866(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Head, Liver, Thymus, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH PARD6A, AND MUTAGENESIS OF GLY-12.
RX   MEDLINE=20394296; PubMed=10934474; DOI=10.1038/35019573;
RA   Joberty G., Petersen C., Gao L., Macara I.G.;
RT   "The cell-polarity protein Par6 links Par3 and atypical protein kinase
RT   C to Cdc42.";
RL   Nat. Cell Biol. 2:531-539(2000).
RN   [5]
RP   INTERACTION WITH PARD6B.
RX   MEDLINE=20394297; PubMed=10934475; DOI=10.1038/35019592;
RA   Lin D., Edwards A.S., Fawcett J.P., Mbamalu G., Scott J.D., Pawson T.;
RT   "A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC
RT   signalling and cell polarity.";
RL   Nat. Cell Biol. 2:540-547(2000).
RN   [6]
RP   INTERACTION WITH RASGRF2.
RX   PubMed=9707409; DOI=10.1016/S0960-9822(07)00376-4;
RA   Fan W.-T., Koch C.A., de Hoog C.L., Fam N.P., Moran M.F.;
RT   "The exchange factor Ras-GRF2 activates Ras-dependent and Rac-
RT   dependent mitogen-activated protein kinase pathways.";
RL   Curr. Biol. 8:935-938(1998).
RN   [7]
RP   INTERACTION WITH MAP3K3; MAP2K3 AND CCM2.
RX   PubMed=14634666; DOI=10.1038/ncb1071;
RA   Uhlik M.T., Abell A.N., Johnson N.L., Sun W., Cuevas B.D.,
RA   Lobel-Rice K.E., Horne E.A., Dell'Acqua M.L., Johnson G.L.;
RT   "Rac-MEKK3-MKK3 scaffolding for p38 MAPK activation during
RT   hyperosmotic shock.";
RL   Nat. Cell Biol. 5:1104-1110(2003).
RN   [8]
RP   INTERACTION WITH NISCH.
RX   PubMed=16002401; DOI=10.1074/jbc.M502546200;
RA   Reddig P.J., Xu D., Juliano R.L.;
RT   "Regulation of p21-activated kinase-independent Rac1 signal
RT   transduction by Nischarin.";
RL   J. Biol. Chem. 280:30994-31002(2005).
CC   -!- FUNCTION: Plasma membrane-associated small GTPase which cycles
CC       between active GTP-bound and inactive GDP-bound states. In its
CC       active state, binds to a variety of effector proteins to regulate
CC       cellular responses such as secretory processes, phagocytosis of
CC       apoptotic cells, epithelial cell polarization and growth-factor
CC       induced formation of membrane ruffles.
CC   -!- ENZYME REGULATION: Regulated by guanine nucleotide exchange
CC       factors (GEFs) which promote the exchange of bound GDP for free
CC       GTP, GTPase activating proteins (GAPs) which increase the GTP
CC       hydrolysis activity, and GDP dissociation inhibitors which inhibit
CC       the dissociation of the nucleotide from the GTPase.
CC   -!- SUBUNIT: Interacts with the GEF proteins PREX1, RASGRF2, DOCK1,
CC       DOCK2 and DOCK7, which promote the exchange between GDP and GTP,
CC       and therefore activate it. Interacts with PARD6A, PARD6B and
CC       PARD6G in a GTP-dependent manner. Part of a quaternary complex
CC       containing PARD3, some PARD6 protein (PARD6A, PARD6B or PARD6G)
CC       and some atypical PKC protein (PRKCI or PRKCZ), which plays a
CC       central role in epithelial cell polarization. Found in a trimeric
CC       complex composed of DOCK1 and ELMO1, which plays a central role in
CC       phagocytosis of apoptotic cells. Interacts with RALBP1 via its
CC       effector domain. Interacts with BAIAP2, BAIAP2L1, PLXNB1,
CC       CYFIP1/SRA-1 and DEF6. Interacts with NOXA1. Interacts with
CC       ARHGEF2. Probably found in a ternary complex composed of DSCAM,
CC       PAK1 and RAC1. Interacts with DSCAM; the interaction requires PAK1
CC       (By similarity). Interacts with TBC1D2 (By similarity). Part of a
CC       complex with MAP2K3, MAP3K3 and CCM2. Interacts with NISCH.
CC       Interacts with UNKL (By similarity). Interacts with USP6 (By
CC       similarity).
CC   -!- INTERACTION:
CC       Q62108:Dlg4; NbExp=1; IntAct=EBI-413646, EBI-300895;
CC       Q13153:PAK1 (xeno); NbExp=1; IntAct=EBI-413646, EBI-1307;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (By similarity). Melanosome (By similarity). Note=Inner
CC       surface of plasma membrane possibly with attachment requiring
CC       prenylation of the C-terminal cysteine (By similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- DOMAIN: The effector region mediates interaction with DEF6 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
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DR   EMBL; X57277; CAA40545.1; -; mRNA.
DR   EMBL; AK009017; BAB26027.1; -; mRNA.
DR   EMBL; AK011072; BAB69451.1; -; mRNA.
DR   EMBL; AK034601; BAC28767.1; -; mRNA.
DR   EMBL; AK047969; BAC33203.1; -; mRNA.
DR   EMBL; AK088825; BAC40596.1; -; mRNA.
DR   EMBL; BC003828; AAH03828.1; -; mRNA.
DR   EMBL; BC051053; AAH51053.1; -; mRNA.
DR   IPI; IPI00761613; -.
DR   PIR; A60347; A60347.
DR   RefSeq; NP_033033.1; NM_009007.2.
DR   UniGene; Mm.292510; -.
DR   UniGene; Mm.342177; -.
DR   ProteinModelPortal; P63001; -.
DR   SMR; P63001; 1-177.
DR   IntAct; P63001; 24.
DR   MINT; MINT-1602774; -.
DR   STRING; P63001; -.
DR   PhosphoSite; P63001; -.
DR   PRIDE; P63001; -.
DR   Ensembl; ENSMUST00000080537; ENSMUSP00000079380; ENSMUSG00000001847.
DR   GeneID; 19353; -.
DR   KEGG; mmu:19353; -.
DR   UCSC; uc009akk.1; mouse.
DR   CTD; 19353; -.
DR   MGI; MGI:97845; Rac1.
DR   eggNOG; roNOG06989; -.
DR   HOVERGEN; HBG009351; -.
DR   OrthoDB; EOG466VN1; -.
DR   PhylomeDB; P63001; -.
DR   NextBio; 296387; -.
DR   ArrayExpress; P63001; -.
DR   Bgee; P63001; -.
DR   CleanEx; MM_RAC1; -.
DR   Genevestigator; P63001; -.
DR   GermOnline; ENSMUSG00000001847; Mus musculus.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0019897; C:extrinsic to plasma membrane; IDA:MGI.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IDA:MGI.
DR   GO; GO:0003924; F:GTPase activity; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0048532; P:anatomical structure arrangement; IMP:MGI.
DR   GO; GO:0002093; P:auditory receptor cell morphogenesis; IMP:MGI.
DR   GO; GO:0007411; P:axon guidance; IMP:MGI.
DR   GO; GO:0045216; P:cell-cell junction organization; IMP:MGI.
DR   GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IMP:MGI.
DR   GO; GO:0090103; P:cochlea morphogenesis; IMP:MGI.
DR   GO; GO:0007010; P:cytoskeleton organization; IDA:MGI.
DR   GO; GO:0016358; P:dendrite development; IDA:MGI.
DR   GO; GO:0071542; P:dopaminergic neuron differentiation; IGI:MGI.
DR   GO; GO:0021831; P:embryonic olfactory bulb interneuron precursor migration; IMP:MGI.
DR   GO; GO:0006897; P:endocytosis; IDA:MGI.
DR   GO; GO:0003382; P:epithelial cell morphogenesis; IMP:MGI.
DR   GO; GO:0006972; P:hyperosmotic response; IDA:MGI.
DR   GO; GO:0030032; P:lamellipodium assembly; IDA:MGI.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:MGI.
DR   GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:MGI.
DR   GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:MGI.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:MGI.
DR   GO; GO:0060071; P:Wnt receptor signaling pathway, planar cell polarity pathway; IGI:MGI.
DR   InterPro; IPR003578; GTPase_Rho.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00174; RHO; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Phosphoprotein; Prenylation.
FT   CHAIN         1    189       Ras-related C3 botulinum toxin substrate
FT                                1.
FT                                /FTId=PRO_0000042038.
FT   PROPEP      190    192       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000042039.
FT   NP_BIND      10     17       GTP (By similarity).
FT   NP_BIND      57     61       GTP (By similarity).
FT   NP_BIND     115    118       GTP (By similarity).
FT   MOTIF        32     40       Effector region (Potential).
FT   MOD_RES      71     71       Phosphoserine (By similarity).
FT   MOD_RES     189    189       Cysteine methyl ester (By similarity).
FT   LIPID       189    189       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   MUTAGEN      12     12       G->V: Constitutively active. Interacts
FT                                with PARD6 proteins.
SQ   SEQUENCE   192 AA;  21450 MW;  ACEDF83A45E5EA67 CRC64;
     MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDGKP VNLGLWDTAG
     QEDYDRLRPL SYPQTDVFLI CFSLVSPASF ENVRAKWYPE VRHHCPNTPI ILVGTKLDLR
     DDKDTIEKLK EKKLTPITYP QGLAMAKEIG AVKYLECSAL TQRGLKTVFD EAIRAVLCPP
     PVKKRKRKCL LL
//
ID   RAB3A_MOUSE             Reviewed;         220 AA.
AC   P63011; P05713; Q3TSL4;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Ras-related protein Rab-3A;
GN   Name=Rab3a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=93319503; PubMed=7687127;
RA   Baumert M., Fischer von Mollard G., Jahn R., Suedhof T.C.;
RT   "Structure of the murine rab3A gene: correlation of genomic
RT   organization with antibody epitopes.";
RL   Biochem. J. 293:157-163(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 13-35; 42-60; 73-83; 122-136; 152-167 AND 179-202,
RP   AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   INTERACTION WITH RIMS2.
RX   MEDLINE=20512528; PubMed=11056535; DOI=10.1038/35041046;
RA   Ozaki N., Shibasaki T., Kashima Y., Miki T., Takahashi K., Ueno H.,
RA   Sunaga Y., Yano H., Matsuura Y., Iwanaga T., Takai Y., Seino S.;
RT   "cAMP-GEFII is a direct target of cAMP in regulated exocytosis.";
RL   Nat. Cell Biol. 2:805-811(2000).
RN   [6]
RP   INTERACTION WITH RIMS1.
RX   MEDLINE=21413899; PubMed=11431472; DOI=10.1074/jbc.M103337200;
RA   Wang X., Hu B., Zimmermann B., Kilimann M.W.;
RT   "Rim1 and rabphilin-3 bind Rab3-GTP by composite determinants
RT   partially related through N-terminal alpha-helix motifs.";
RL   J. Biol. Chem. 276:32480-32488(2001).
RN   [7]
RP   INTERACTION WITH RIMS2.
RX   MEDLINE=22384373; PubMed=12401793; DOI=10.1074/jbc.M210146200;
RA   Fujimoto K., Shibasaki T., Yokoi N., Kashima Y., Matsumoto M.,
RA   Sasaki T., Tajima N., Iwanaga T., Seino S.;
RT   "Piccolo, a Ca2+ sensor in pancreatic beta-cells. Involvement of cAMP-
RT   GEFII.Rim2.Piccolo complex in cAMP-dependent exocytosis.";
RL   J. Biol. Chem. 277:50497-50502(2002).
RN   [8]
RP   INTERACTION WITH SYTL4.
RX   MEDLINE=22590467; PubMed=12590134; DOI=10.1074/jbc.M213090200;
RA   Fukuda M.;
RT   "Slp4-a/granuphilin-a inhibits dense-core vesicle exocytosis through
RT   interaction with the GDP-bound form of Rab27A in PC12 cells.";
RL   J. Biol. Chem. 278:15390-15396(2003).
RN   [9]
RP   INTERACTION WITH SGSM1 AND SGSM3.
RX   PubMed=17509819; DOI=10.1016/j.ygeno.2007.03.013;
RA   Yang H., Sasaki T., Minoshima S., Shimizu N.;
RT   "Identification of three novel proteins (SGSM1, 2, 3) which modulate
RT   small G protein (RAP and RAB)-mediated signaling pathway.";
RL   Genomics 90:249-260(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15648052; DOI=10.1002/pmic.200401066;
RA   Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA   Hart G.W., Burlingame A.L.;
RT   "Quantitative analysis of both protein expression and serine /
RT   threonine post-translational modifications through stable isotope
RT   labeling with dithiothreitol.";
RL   Proteomics 5:388-398(2005).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Involved in exocytosis by regulating a late step in
CC       synaptic vesicle fusion. Could play a role in neurotransmitter
CC       release by regulating membrane flow in the nerve terminal (By
CC       similarity).
CC   -!- SUBUNIT: Heterodimer with RIMS2. Part of a ternary complex
CC       involving PCLO and EPAC2. Interacts with RPH3A. Interacts with the
CC       exocyst complex through SEC15. Binds SYTL4, RIMS1 and RIMS2.
CC       Interacts with RAB3IP. Interacts with SGSM1 and SGSM3.
CC   -!- INTERACTION:
CC       P47708:Rph3a; NbExp=2; IntAct=EBI-398393, EBI-398376;
CC       Q9R0Q1:Sytl4; NbExp=1; IntAct=EBI-398393, EBI-398341;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR   EMBL; X72966; CAA51470.1; -; Genomic_DNA.
DR   EMBL; AK005362; BAB23976.1; -; mRNA.
DR   EMBL; AK158727; BAE34630.1; -; mRNA.
DR   EMBL; AK161975; BAE36661.1; -; mRNA.
DR   EMBL; BC053519; AAH53519.1; -; mRNA.
DR   IPI; IPI00122965; -.
DR   PIR; S34070; S34070.
DR   RefSeq; NP_001159871.1; NM_001166399.2.
DR   RefSeq; NP_033027.1; NM_009001.6.
DR   UniGene; Mm.5083; -.
DR   ProteinModelPortal; P63011; -.
DR   SMR; P63011; 18-186.
DR   DIP; DIP-31051N; -.
DR   IntAct; P63011; 9.
DR   MINT; MINT-85820; -.
DR   STRING; P63011; -.
DR   PhosphoSite; P63011; -.
DR   PRIDE; P63011; -.
DR   Ensembl; ENSMUST00000034301; ENSMUSP00000034301; ENSMUSG00000031840.
DR   Ensembl; ENSMUST00000110090; ENSMUSP00000105717; ENSMUSG00000031840.
DR   Ensembl; ENSMUST00000110092; ENSMUSP00000105719; ENSMUSG00000031840.
DR   Ensembl; ENSMUST00000110093; ENSMUSP00000105720; ENSMUSG00000031840.
DR   GeneID; 19339; -.
DR   KEGG; mmu:19339; -.
DR   UCSC; uc009mbi.1; mouse.
DR   CTD; 19339; -.
DR   MGI; MGI:97843; Rab3a.
DR   eggNOG; roNOG14692; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; P63011; -.
DR   OMA; KLVEIIC; -.
DR   OrthoDB; EOG4TB4C6; -.
DR   PhylomeDB; P63011; -.
DR   NextBio; 296339; -.
DR   ArrayExpress; P63011; -.
DR   Bgee; P63011; -.
DR   CleanEx; MM_RAB3A; -.
DR   Genevestigator; P63011; -.
DR   GermOnline; ENSMUSG00000031840; Mus musculus.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR   GO; GO:0030324; P:lung development; IMP:MGI.
DR   GO; GO:0048790; P:maintenance of presynaptic active zone structure; IMP:MGI.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0031630; P:regulation of synaptic vesicle fusion to presynaptic membrane; IMP:MGI.
DR   GO; GO:0003016; P:respiratory system process; IMP:MGI.
DR   GO; GO:0051602; P:response to electrical stimulus; IMP:MGI.
DR   GO; GO:0050975; P:sensory perception of touch; IMP:MGI.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0016079; P:synaptic vesicle exocytosis; IMP:MGI.
DR   GO; GO:0016188; P:synaptic vesicle maturation; IMP:MGI.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Exocytosis; GTP-binding;
KW   Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW   Phosphoprotein; Prenylation; Protein transport; Transport.
FT   CHAIN         1    220       Ras-related protein Rab-3A.
FT                                /FTId=PRO_0000121078.
FT   NP_BIND      29     36       GTP (By similarity).
FT   NP_BIND      77     81       GTP (By similarity).
FT   NP_BIND     135    138       GTP (By similarity).
FT   MOTIF        51     59       Effector region (By similarity).
FT   MOD_RES      37     37       Phosphoserine.
FT   MOD_RES     188    188       Phosphoserine.
FT   MOD_RES     220    220       Cysteine methyl ester (By similarity).
FT   LIPID       218    218       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   LIPID       220    220       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   220 AA;  24970 MW;  1A3E9F8C9D09EB40 CRC64;
     MASATDSRYG QKESSDQNFD YMFKILIIGN SSVGKTSFLF RYADDSFTPA FVSTVGIDFK
     VKTIYRNDKR IKLQIWDTAG QERYRTITTA YYRGAMGFIL MYDITNEESF NAVQDWSTQI
     KTYSWDNAQV LLVGNKCDME DERVVSSERG RQLADHLGFE FFEASAKDNI NVKQTFERLV
     DVICEKMSES LDTADPAVTG AKQGPQLTDQ QAPPHQDCAC
//
ID   HSP7C_MOUSE             Reviewed;         646 AA.
AC   P63017; P08109; P12225; Q3U6R0; Q3U764; Q3U7D7; Q3U7E2; Q3U9B4;
AC   Q3U9G0; Q3UGM0; Q5FWJ6; Q62373; Q62374; Q62375; Q6NZD0;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Heat shock cognate 71 kDa protein;
DE   AltName: Full=Heat shock 70 kDa protein 8;
GN   Name=Hspa8; Synonyms=Hsc70, Hsc73;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=88055872; PubMed=3334718; DOI=10.1016/0012-1606(88)90073-5;
RA   Giebel L.B., Dworniczak B.P., Bautz E.K.F.;
RT   "Developmental regulation of a constitutively expressed mouse mRNA
RT   encoding a 72-kDa heat shock-like protein.";
RL   Dev. Biol. 125:200-207(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129; TISSUE=Mammary gland;
RX   PubMed=8682318; DOI=10.1016/0378-1119(96)00169-2;
RA   Soulier S., Vilotte J.-L., L'Huillier P.J., Mercier J.-C.;
RT   "Developmental regulation of murine integrin beta 1 subunit- and
RT   Hsc73-encoding genes in mammary gland: sequence of a new mouse Hsc73
RT   cDNA.";
RL   Gene 172:285-289(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129;
RX   PubMed=10095055; DOI=10.1016/S0167-4781(98)00285-1;
RA   Hunt C.R., Parsian A.J., Goswami P.C., Kozak C.A.;
RT   "Characterization and expression of the mouse Hsc70 gene.";
RL   Biochim. Biophys. Acta 1444:315-325(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2;
RC   TISSUE=Amnion, Bone marrow, Heart, Kidney, Liver, Stomach, Thymus, and
RC   Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N;
RC   TISSUE=Brain, Embryo, Embryonic germ cell, Eye, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 4-49; 57-71; 77-102; 113-155; 160-188; 221-246;
RP   300-319; 326-342; 349-357; 362-384; 424-447; 540-550 AND 584-597, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 333-383; 438-452 AND 580-587.
RX   MEDLINE=91067440; PubMed=2251119; DOI=10.1093/nar/18.22.6565;
RA   Liu J., Maxwell E.S.;
RT   "Mouse U14 snRNA is encoded in an intron of the mouse cognate hsc70
RT   heat shock gene.";
RL   Nucleic Acids Res. 18:6565-6571(1990).
RN   [8]
RP   INTERACTION WITH HSPH1.
RX   PubMed=9675148; DOI=10.1006/bbrc.1998.8979;
RA   Hatayama T., Yasuda K., Yasuda K.;
RT   "Association of HSP105 with HSC70 in high molecular mass complexes in
RT   mouse FM3A cells.";
RL   Biochem. Biophys. Res. Commun. 248:395-401(1998).
RN   [9]
RP   INTERACTION WITH HSPH1.
RX   PubMed=15292236; DOI=10.1074/jbc.M407947200;
RA   Yamagishi N., Ishihara K., Hatayama T.;
RT   "Hsp105alpha suppresses Hsc70 chaperone activity by inhibiting Hsc70
RT   ATPase activity.";
RL   J. Biol. Chem. 279:41727-41733(2004).
RN   [10]
RP   ISGYLATION.
RX   PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA   Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA   Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT   "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT   human cells.";
RL   Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN   [11]
RP   INTERACTION WITH IRAK1BP1, AND MASS SPECTROMETRY.
RX   PubMed=17233114; DOI=10.1089/dna.2006.25.704;
RA   Haag Breese E., Uversky V.N., Georgiadis M.M., Harrington M.A.;
RT   "The disordered amino-terminus of SIMPL interacts with members of the
RT   70-kDa heat-shock protein family.";
RL   DNA Cell Biol. 25:704-714(2006).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND TYR-41, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Chaperone.
CC   -!- SUBUNIT: Identified in a mRNP granule complex, at least composed
CC       of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD,
CC       HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1,
CC       NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8,
CC       RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with
CC       PACRG and BAG1. Interacts with DNAJC7 (By similarity). Interacts
CC       with HSPH1/HSP105 and IRAK1BP1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Melanosome (By
CC       similarity). Note=Localized in cytoplasmic mRNP granules
CC       containing untranslated mRNAs. Translocates rapidly from the
CC       cytoplasm to the nuclei, and especially to the nucleoli, upon heat
CC       shock (By similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- INDUCTION: Constitutively synthesized.
CC   -!- DOMAIN: The N-terminal 1-386 residues constitute the ATPase
CC       domain, while residues 387-646 form the peptide-binding domain (By
CC       similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- PTM: ISGylated.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE31508.1; Type=Frameshift; Positions=256, 269;
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DR   EMBL; M19141; AAA37869.1; -; mRNA.
DR   EMBL; U27129; AAC52836.1; -; mRNA.
DR   EMBL; U73744; AAB18391.1; -; Genomic_DNA.
DR   EMBL; AK035286; BAC29016.1; -; mRNA.
DR   EMBL; AK075935; BAC36065.1; -; mRNA.
DR   EMBL; AK145579; BAE26523.1; -; mRNA.
DR   EMBL; AK146708; BAE27374.1; -; mRNA.
DR   EMBL; AK146985; BAE27588.1; -; mRNA.
DR   EMBL; AK147864; BAE28187.1; -; mRNA.
DR   EMBL; AK150474; BAE29591.1; -; mRNA.
DR   EMBL; AK150498; BAE29612.1; -; mRNA.
DR   EMBL; AK150701; BAE29780.1; -; mRNA.
DR   EMBL; AK150958; BAE29990.1; -; mRNA.
DR   EMBL; AK151065; BAE30081.1; -; mRNA.
DR   EMBL; AK151127; BAE30135.1; -; mRNA.
DR   EMBL; AK151287; BAE30272.1; -; mRNA.
DR   EMBL; AK151435; BAE30398.1; -; mRNA.
DR   EMBL; AK151516; BAE30465.1; -; mRNA.
DR   EMBL; AK151537; BAE30484.1; -; mRNA.
DR   EMBL; AK151775; BAE30681.1; -; mRNA.
DR   EMBL; AK151808; BAE30707.1; -; mRNA.
DR   EMBL; AK151865; BAE30753.1; -; mRNA.
DR   EMBL; AK151892; BAE30776.1; -; mRNA.
DR   EMBL; AK151948; BAE30822.1; -; mRNA.
DR   EMBL; AK151997; BAE30861.1; -; mRNA.
DR   EMBL; AK152598; BAE31346.1; -; mRNA.
DR   EMBL; AK152697; BAE31427.1; -; mRNA.
DR   EMBL; AK152703; BAE31432.1; -; mRNA.
DR   EMBL; AK152803; BAE31508.1; ALT_FRAME; mRNA.
DR   EMBL; AK153032; BAE31664.1; -; mRNA.
DR   EMBL; AK153834; BAE32204.1; -; mRNA.
DR   EMBL; AK159479; BAE35116.1; -; mRNA.
DR   EMBL; AK164000; BAE37581.1; -; mRNA.
DR   EMBL; AK166643; BAE38912.1; -; mRNA.
DR   EMBL; AK166721; BAE38970.1; -; mRNA.
DR   EMBL; AK166767; BAE39005.1; -; mRNA.
DR   EMBL; AK166776; BAE39012.1; -; mRNA.
DR   EMBL; AK166808; BAE39036.1; -; mRNA.
DR   EMBL; AK166830; BAE39053.1; -; mRNA.
DR   EMBL; AK166846; BAE39065.1; -; mRNA.
DR   EMBL; AK166861; BAE39076.1; -; mRNA.
DR   EMBL; AK166873; BAE39084.1; -; mRNA.
DR   EMBL; AK166908; BAE39109.1; -; mRNA.
DR   EMBL; AK166910; BAE39111.1; -; mRNA.
DR   EMBL; AK166913; BAE39113.1; -; mRNA.
DR   EMBL; AK166933; BAE39127.1; -; mRNA.
DR   EMBL; AK167043; BAE39211.1; -; mRNA.
DR   EMBL; AK167121; BAE39269.1; -; mRNA.
DR   EMBL; AK167122; BAE39270.1; -; mRNA.
DR   EMBL; AK167134; BAE39280.1; -; mRNA.
DR   EMBL; AK167163; BAE39304.1; -; mRNA.
DR   EMBL; AK167218; BAE39344.1; -; mRNA.
DR   EMBL; AK167229; BAE39353.1; -; mRNA.
DR   EMBL; AK167845; BAE39865.1; -; mRNA.
DR   EMBL; AK167910; BAE39917.1; -; mRNA.
DR   EMBL; AK168492; BAE40379.1; -; mRNA.
DR   EMBL; AK168519; BAE40398.1; -; mRNA.
DR   EMBL; AK168542; BAE40419.1; -; mRNA.
DR   EMBL; AK168711; BAE40553.1; -; mRNA.
DR   EMBL; AK168750; BAE40590.1; -; mRNA.
DR   EMBL; AK168776; BAE40612.1; -; mRNA.
DR   EMBL; AK168887; BAE40704.1; -; mRNA.
DR   EMBL; AK168934; BAE40745.1; -; mRNA.
DR   EMBL; AK169093; BAE40876.1; -; mRNA.
DR   EMBL; AK169179; BAE40957.1; -; mRNA.
DR   EMBL; AK169236; BAE41004.1; -; mRNA.
DR   EMBL; AK169293; BAE41049.1; -; mRNA.
DR   EMBL; BC006722; AAH06722.1; -; mRNA.
DR   EMBL; BC066191; AAH66191.1; -; mRNA.
DR   EMBL; BC085486; AAH85486.1; -; mRNA.
DR   EMBL; BC089322; AAH89322.1; -; mRNA.
DR   EMBL; BC089457; AAH89457.1; -; mRNA.
DR   EMBL; BC106193; AAI06194.1; -; mRNA.
DR   EMBL; X54401; CAA38267.1; -; Genomic_DNA.
DR   EMBL; X54402; CAA38268.1; -; Genomic_DNA.
DR   EMBL; X54403; CAA38269.1; -; Genomic_DNA.
DR   IPI; IPI00323357; -.
DR   PIR; A45935; A45935.
DR   PIR; JC4853; JC4853.
DR   RefSeq; NP_112442.2; NM_031165.4.
DR   UniGene; Mm.290774; -.
DR   UniGene; Mm.336743; -.
DR   UniGene; Mm.351377; -.
DR   UniGene; Mm.412745; -.
DR   PDB; 3CQX; X-ray; 2.30 A; A/B=1-381.
DR   PDBsum; 3CQX; -.
DR   ProteinModelPortal; P63017; -.
DR   SMR; P63017; 1-621.
DR   DIP; DIP-32353N; -.
DR   IntAct; P63017; 13.
DR   MINT; MINT-189032; -.
DR   STRING; P63017; -.
DR   SWISS-2DPAGE; P63017; -.
DR   COMPLUYEAST-2DPAGE; P63017; -.
DR   REPRODUCTION-2DPAGE; IPI00323357; -.
DR   REPRODUCTION-2DPAGE; P63017; -.
DR   REPRODUCTION-2DPAGE; Q6NZD0; -.
DR   UCD-2DPAGE; P63017; -.
DR   PRIDE; P63017; -.
DR   Ensembl; ENSMUST00000015800; ENSMUSP00000015800; ENSMUSG00000015656.
DR   GeneID; 15481; -.
DR   KEGG; mmu:15481; -.
DR   UCSC; uc009ozx.1; mouse.
DR   CTD; 15481; -.
DR   MGI; MGI:105384; Hspa8.
DR   eggNOG; roNOG06558; -.
DR   HOVERGEN; HBG051845; -.
DR   InParanoid; P63017; -.
DR   OMA; EKYKADD; -.
DR   OrthoDB; EOG4W6NVK; -.
DR   PhylomeDB; P63017; -.
DR   NextBio; 288328; -.
DR   Bgee; P63017; -.
DR   CleanEx; MM_HSPA8; -.
DR   Genevestigator; P63017; -.
DR   GermOnline; ENSMUSG00000015656; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:MGI.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0030529; C:ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042623; F:ATPase activity, coupled; IDA:MGI.
DR   GO; GO:0051082; F:unfolded protein binding; IPI:MGI.
DR   GO; GO:0051085; P:chaperone mediated protein folding requiring cofactor; IGI:MGI.
DR   GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR001023; Hsp70.
DR   InterPro; IPR013126; Hsp_70.
DR   PANTHER; PTHR19375; Hsp70; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Chaperone; Cytoplasm;
KW   Direct protein sequencing; Nucleotide-binding; Phosphoprotein;
KW   Stress response; Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    646       Heat shock cognate 71 kDa protein.
FT                                /FTId=PRO_0000078271.
FT   REGION      186    377       Interaction with BAG1 (By similarity).
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES      15     15       Phosphotyrosine.
FT   MOD_RES      41     41       Phosphotyrosine.
FT   MOD_RES      88     88       N6-acetyllysine (By similarity).
FT   MOD_RES     107    107       Phosphotyrosine (By similarity).
FT   MOD_RES     108    108       N6-acetyllysine (By similarity).
FT   MOD_RES     113    113       Phosphoserine (By similarity).
FT   MOD_RES     115    115       Phosphotyrosine (By similarity).
FT   MOD_RES     120    120       Phosphoserine (By similarity).
FT   MOD_RES     121    121       Phosphoserine (By similarity).
FT   MOD_RES     153    153       Phosphoserine (By similarity).
FT   MOD_RES     246    246       N6-acetyllysine (By similarity).
FT   MOD_RES     319    319       N6-acetyllysine (By similarity).
FT   MOD_RES     348    348       N6-acetyllysine (By similarity).
FT   MOD_RES     477    477       Phosphothreonine (By similarity).
FT   MOD_RES     512    512       N6-acetyllysine (By similarity).
FT   MOD_RES     524    524       N6-acetyllysine (By similarity).
FT   MOD_RES     541    541       Phosphoserine (By similarity).
FT   MOD_RES     589    589       N6-acetyllysine (By similarity).
FT   MOD_RES     597    597       N6-acetyllysine (By similarity).
FT   MOD_RES     601    601       N6-acetyllysine (By similarity).
FT   MOD_RES     637    637       Phosphoserine (By similarity).
FT   MOD_RES     638    638       Phosphoserine (By similarity).
FT   CONFLICT      9      9       I -> V (in Ref. 4; BAE28187).
FT   CONFLICT     35     35       N -> K (in Ref. 4; BAE30081/BAE30861/
FT                                BAE30753).
FT   CONFLICT    268    268       E -> G (in Ref. 4; BAE31432/BAE31346).
FT   CONFLICT    269    269       R -> G (in Ref. 4; BAE31508).
FT   CONFLICT    353    353       F -> C (in Ref. 4; BAE31664).
FT   CONFLICT    428    428       F -> L (in Ref. 1; AAA37869 and 3;
FT                                AAB18391).
FT   CONFLICT    432    432       S -> Y (in Ref. 4; BAE30707).
FT   CONFLICT    589    589       K -> E (in Ref. 5; AAH66191).
FT   CONFLICT    645    645       V -> M (in Ref. 4; BAE30272/BAE31427).
FT   STRAND       15     17
FT   STRAND       37     39
FT   STRAND       42     44
FT   HELIX        54     57
FT   TURN         58     61
FT   HELIX        63     65
FT   HELIX        70     72
FT   HELIX        81     86
FT   TURN         87     89
FT   STRAND       91     96
FT   STRAND      101    106
FT   STRAND      111    114
FT   HELIX       116    134
FT   STRAND      141    146
FT   HELIX       152    160
FT   STRAND      168    174
FT   HELIX       175    182
FT   STRAND      193    199
FT   STRAND      206    212
FT   STRAND      217    223
FT   HELIX       232    249
FT   HELIX       257    273
FT   TURN        274    276
FT   STRAND      278    284
FT   STRAND      293    298
FT   HELIX       299    310
FT   HELIX       314    324
FT   HELIX       328    330
FT   STRAND      333    337
FT   HELIX       344    353
FT   TURN        365    370
FT   HELIX       374    380
SQ   SEQUENCE   646 AA;  70871 MW;  03A27B30E6C076ED CRC64;
     MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
     MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR PKVQVEYKGE TKSFYPEEVS
     SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA
     IAYGLDKKVG AERNVLIFDL GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH
     FIAEFKRKHK KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA
     RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL QDFFNGKELN
     KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVM TVLIKRNTTI
     PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI
     DANGILNVSA VDKSTGKENK ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN
     SLESYAFNMK ATVEDEKLQG KINDEDKQKI LDKCNEIISW LDKNQTAEKE EFEHQQKELE
     KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD
//
ID   VAMP3_MOUSE             Reviewed;         103 AA.
AC   P63024; Q3TH70; Q64271;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Vesicle-associated membrane protein 3;
DE            Short=VAMP-3;
DE   AltName: Full=Cellubrevin;
DE            Short=CEB;
DE   AltName: Full=Synaptobrevin-3;
GN   Name=Vamp3; Synonyms=Syb3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Martin S., Tellam J.T., Livington C., Slot J.W., Gould G.W.,
RA   James D.E.;
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C57BL/6x129SV/J;
RX   PubMed=11238894; DOI=10.1128/MCB.21.5.1573-1580.2001;
RA   Yang C.M., Mora S., Ryder J.W., Coker K.J., Hansen P., Allen L.A.,
RA   Pessin J.E.;
RT   "VAMP3 null mice display normal constitutive, insulin- and exercise-
RT   regulated vesicle trafficking.";
RL   Mol. Cell. Biol. 21:1573-1580(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart, Liver, Lung, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   INTERACTION WITH BVES.
RX   PubMed=20057356; DOI=10.1038/emboj.2009.379;
RA   Hager H.A., Roberts R.J., Cross E.E., Proux-Gillardeaux V.,
RA   Bader D.M.;
RT   "Identification of a novel Bves function: regulation of vesicular
RT   transport.";
RL   EMBO J. 29:532-545(2010).
CC   -!- FUNCTION: SNARE involved in vesicular transport from the late
CC       endosomes to the trans-Golgi network (By similarity).
CC   -!- SUBUNIT: Interacts with BVES (via the C-terminus cytoplasmic
CC       tail).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane
CC       protein (Probable). Cell junction, synapse, synaptosome (By
CC       similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the synaptobrevin family.
CC   -!- SIMILARITY: Contains 1 v-SNARE coiled-coil homology domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U60961; AAB03490.1; -; mRNA.
DR   EMBL; AF308434; AAG42468.1; -; Genomic_DNA.
DR   EMBL; AF308433; AAG42468.1; JOINED; Genomic_DNA.
DR   EMBL; AK051272; BAC34586.1; -; mRNA.
DR   EMBL; AK051691; BAC34723.1; -; mRNA.
DR   EMBL; AK165947; BAE38479.1; -; mRNA.
DR   EMBL; AK168413; BAE40328.1; -; mRNA.
DR   EMBL; AK169056; BAE40844.1; -; mRNA.
DR   EMBL; AK169087; BAE40871.1; -; mRNA.
DR   EMBL; BC060045; AAH60045.1; -; mRNA.
DR   IPI; IPI00132276; -.
DR   RefSeq; NP_033524.1; NM_009498.4.
DR   UniGene; Mm.273930; -.
DR   ProteinModelPortal; P63024; -.
DR   SMR; P63024; 15-79.
DR   STRING; P63024; -.
DR   PhosphoSite; P63024; -.
DR   PRIDE; P63024; -.
DR   Ensembl; ENSMUST00000030797; ENSMUSP00000030797; ENSMUSG00000028955.
DR   GeneID; 22319; -.
DR   KEGG; mmu:22319; -.
DR   UCSC; uc008vyj.1; mouse.
DR   CTD; 22319; -.
DR   MGI; MGI:1321389; Vamp3.
DR   GeneTree; ENSGT00550000074449; -.
DR   HOGENOM; HBG386095; -.
DR   HOVERGEN; HBG006675; -.
DR   InParanoid; P63024; -.
DR   OMA; ANVPGNT; -.
DR   OrthoDB; EOG43JC6B; -.
DR   PhylomeDB; P63024; -.
DR   NextBio; 302533; -.
DR   ArrayExpress; P63024; -.
DR   Bgee; P63024; -.
DR   CleanEx; MM_VAMP3; -.
DR   Genevestigator; P63024; -.
DR   GermOnline; ENSMUSG00000028955; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR   GO; GO:0019717; C:synaptosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0017156; P:calcium ion-dependent exocytosis; IMP:MGI.
DR   GO; GO:0001921; P:positive regulation of receptor recycling; IDA:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:UniProtKB.
DR   InterPro; IPR001388; Synaptobrevin.
DR   InterPro; IPR016444; Synaptobrevin_met/fun.
DR   Pfam; PF00957; Synaptobrevin; 1.
DR   PIRSF; PIRSF005409; Synaptobrevin_euk; 1.
DR   PRINTS; PR00219; SYNAPTOBREVN.
DR   PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR   PROSITE; PS50892; V_SNARE; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Coiled coil; Membrane; Phosphoprotein;
KW   Protein transport; Synapse; Synaptosome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    103       Vesicle-associated membrane protein 3.
FT                                /FTId=PRO_0000206729.
FT   TOPO_DOM      1     81       Cytoplasmic (Potential).
FT   TRANSMEM     82    102       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   TOPO_DOM    103    103       Vesicular (Potential).
FT   DOMAIN       18     78       v-SNARE coiled-coil homology.
FT   MOD_RES      48     48       Phosphoserine.
FT   MOD_RES      62     62       Phosphoserine (By similarity).
SQ   SEQUENCE   103 AA;  11480 MW;  EB502BBE5D0F5981 CRC64;
     MSTGVPSGSS AATGSNRRLQ QTQNQVDEVV DIMRVNVDKV LERDQKLSEL DDRADALQAG
     ASQFETSAAK LKRKYWWKNC KMWAIGISVL VIIVIIIIVW CVS
//
ID   DNJA1_MOUSE             Reviewed;         397 AA.
AC   P63037; P54102;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=DnaJ homolog subfamily A member 1;
DE   AltName: Full=DnaJ protein homolog 2;
DE   AltName: Full=Heat shock 40 kDa protein 4;
DE   AltName: Full=Heat shock protein J2;
DE            Short=HSJ-2;
DE   Flags: Precursor;
GN   Name=Dnaja1; Synonyms=Dnaj2, Hsj2, Hspf4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99017984; PubMed=9799614; DOI=10.1006/geno.1998.5501;
RA   Royaux I., Minner F., Goffinet A.M., de Rouvroit C.L.;
RT   "A DnaJ-like gene, Hsj2, maps to mouse chromosome 5, at approximately
RT   24 cM from the centromere.";
RL   Genomics 53:415-415(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 106-124 AND 375-389, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
CC   -!- FUNCTION: Co-chaperone of Hsc70. Seems to play a role in protein
CC       import into mitochondria (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor (Potential).
CC   -!- SIMILARITY: Contains 1 CR-type zinc finger.
CC   -!- SIMILARITY: Contains 1 J domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF055664; AAC78597.1; -; mRNA.
DR   EMBL; AK083046; BAC38744.1; -; mRNA.
DR   EMBL; BC057876; AAH57876.1; -; mRNA.
DR   IPI; IPI00132208; -.
DR   RefSeq; NP_001158143.1; NM_001164671.1.
DR   RefSeq; NP_001158144.1; NM_001164672.1.
DR   RefSeq; NP_032324.1; NM_008298.5.
DR   UniGene; Mm.27897; -.
DR   UniGene; Mm.471544; -.
DR   ProteinModelPortal; P63037; -.
DR   SMR; P63037; 3-68, 101-369.
DR   DIP; DIP-32350N; -.
DR   MINT; MINT-1858917; -.
DR   STRING; P63037; -.
DR   PRIDE; P63037; -.
DR   Ensembl; ENSMUST00000030118; ENSMUSP00000030118; ENSMUSG00000028410.
DR   GeneID; 15502; -.
DR   KEGG; mmu:15502; -.
DR   UCSC; uc008sht.1; mouse.
DR   CTD; 15502; -.
DR   MGI; MGI:1270129; Dnaja1.
DR   eggNOG; roNOG13985; -.
DR   HOGENOM; HBG635315; -.
DR   HOVERGEN; HBG066727; -.
DR   InParanoid; P63037; -.
DR   OMA; HSVFTRR; -.
DR   OrthoDB; EOG4RJG1R; -.
DR   PhylomeDB; P63037; -.
DR   NextBio; 288400; -.
DR   ArrayExpress; P63037; -.
DR   Bgee; P63037; -.
DR   CleanEx; MM_DNAJA1; -.
DR   Genevestigator; P63037; -.
DR   GermOnline; ENSMUSG00000028410; Mus musculus.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0030521; P:androgen receptor signaling pathway; IMP:MGI.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0009408; P:response to heat; IEA:InterPro.
DR   GO; GO:0030317; P:sperm motility; IMP:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   InterPro; IPR012724; DnaJ.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_N.
DR   InterPro; IPR018253; Heat_shock_DnaJ_CS.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR003095; Hsp_DnaJ.
DR   InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR   Gene3D; G3DSA:1.10.287.110; DnaJ_N; 1.
DR   Gene3D; G3DSA:2.10.230.10; HSP_DnaJ_cys-rich; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; DnaJ_N; 1.
DR   SUPFAM; SSF49493; HSP40_DnaJ_pep; 2.
DR   SUPFAM; SSF57938; HSP_DnaJ_cys-rich; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51188; ZF_CR; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chaperone; Direct protein sequencing; Lipoprotein;
KW   Membrane; Metal-binding; Methylation; Phosphoprotein; Prenylation;
KW   Repeat; Zinc; Zinc-finger.
FT   CHAIN         1    394       DnaJ homolog subfamily A member 1.
FT                                /FTId=PRO_0000071009.
FT   PROPEP      395    397       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000396753.
FT   DOMAIN        6     68       J.
FT   REPEAT      134    141       CXXCXGXG motif.
FT   REPEAT      150    157       CXXCXGXG motif.
FT   REPEAT      177    184       CXXCXGXG motif.
FT   REPEAT      193    200       CXXCXGXG motif.
FT   ZN_FING     121    205       CR-type.
FT   COMPBIAS     75     96       Gly-rich.
FT   METAL       134    134       Zinc 1 (By similarity).
FT   METAL       137    137       Zinc 1 (By similarity).
FT   METAL       150    150       Zinc 2 (By similarity).
FT   METAL       153    153       Zinc 2 (By similarity).
FT   METAL       177    177       Zinc 2 (By similarity).
FT   METAL       180    180       Zinc 2 (By similarity).
FT   METAL       193    193       Zinc 1 (By similarity).
FT   METAL       196    196       Zinc 1 (By similarity).
FT   MOD_RES      44     44       N6-acetyllysine (By similarity).
FT   MOD_RES      66     66       N6-acetyllysine (By similarity).
FT   MOD_RES      83     83       Phosphoserine (By similarity).
FT   MOD_RES     335    335       Phosphoserine (By similarity).
FT   MOD_RES     340    340       Phosphoserine (By similarity).
FT   MOD_RES     381    381       Phosphotyrosine (By similarity).
FT   MOD_RES     394    394       Cysteine methyl ester (By similarity).
FT   LIPID       394    394       S-farnesyl cysteine (By similarity).
SQ   SEQUENCE   397 AA;  44868 MW;  1783CE3D5C4CD558 CRC64;
     MVKETTYYDV LGVKPNATQE ELKKAYRKLA LKYHPDKNPN EGEKFKQISQ AYEVLADSKK
     RELYDKGGEQ AIKEGGAGGG FGSPMDIFDM FFGGGGRMQR ERRGKNVVHQ LSVTLEDLYN
     GATRKLALQK NVICDKCEGR GGKKGAVECC PNCRGTGMQI RIHQIGPGMV QQIQSVCMEC
     QGHGERISPK DRCKSCNGRK IVREKKILEV HIDKGMKDGQ KITFHGEGDQ EPGLEPGDII
     IVLDQKDHAV FTRRGEDLFM CMDIQLVEAL CGFQKPISTL DNRTIVITSH PGQIVKHGDI
     KCVLNEGMPI YRRPYEKGRL IIEFKVNFPE NGFLSPDKLS LLEKLLPERK EVEETDEMDQ
     VELVDFDPNQ ERRRHYNGEA YEDDEHHPRG GVQCQTS
//
ID   CH60_MOUSE              Reviewed;         573 AA.
AC   P63038; P19226; P19227; P97602; Q3KQP2; Q3UIP0; Q8C2C7; Q8VEF4;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=60 kDa heat shock protein, mitochondrial;
DE   AltName: Full=60 kDa chaperonin;
DE   AltName: Full=Chaperonin 60;
DE            Short=CPN60;
DE   AltName: Full=HSP-65;
DE   AltName: Full=Heat shock protein 60;
DE            Short=HSP-60;
DE            Short=Hsp60;
DE   AltName: Full=Mitochondrial matrix protein P1;
DE   Flags: Precursor;
GN   Name=Hspd1; Synonyms=Hsp60;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Thymus;
RX   MEDLINE=91088314; PubMed=2263486; DOI=10.1093/nar/18.23.7153;
RA   Loetscher E., Allison J.P.;
RT   "Nucleotide and deduced amino acid sequence of a murine cDNA clone
RT   encoding one member of the hsp65 multigene family.";
RL   Nucleic Acids Res. 18:7153-7153(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 527-548,
RP   AND INTERACTION WITH HRAS.
RX   MEDLINE=92196047; PubMed=1347942; DOI=10.1073/pnas.89.6.2012;
RA   Ikawa S., Weinberg R.A.;
RT   "An interaction between p21ras and heat shock protein hsp60, a
RT   chaperonin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:2012-2016(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Heart, Kidney, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=129, and FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 19-573 (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Fibroblast;
RX   MEDLINE=91064389; PubMed=1979012; DOI=10.1016/0167-4781(90)90008-P;
RA   Venner T.J., Gupta R.S.;
RT   "Nucleotide sequence of mouse HSP60 (chaperonin, GroEL homolog)
RT   cDNA.";
RL   Biochim. Biophys. Acta 1087:336-338(1990).
RN   [6]
RP   PROTEIN SEQUENCE OF 27-47.
RC   TISSUE=Fibroblast;
RX   MEDLINE=95009907; PubMed=7523108; DOI=10.1002/elps.11501501101;
RA   Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.;
RT   "Separation and sequencing of familiar and novel murine proteins using
RT   preparative two-dimensional gel electrophoresis.";
RL   Electrophoresis 15:735-745(1994).
RN   [7]
RP   PROTEIN SEQUENCE OF 38-58; 61-72; 97-121; 134-141; 143-191; 196-202;
RP   206-233; 237-290; 293-309; 345-359; 371-387; 397-417; 421-469; 474-516
RP   AND 527-554.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B.,
RA   Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-223, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: Implicated in mitochondrial protein import and
CC       macromolecular assembly. May facilitate the correct folding of
CC       imported proteins. May also prevent misfolding and promote the
CC       refolding and proper assembly of unfolded polypeptides generated
CC       under stress conditions in the mitochondrial matrix.
CC   -!- SUBUNIT: Interacts with HRAS.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P63038-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P63038-2; Sequence=VSP_025020;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the chaperonin (HSP60) family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI06113.1; Type=Miscellaneous discrepancy; Note=. Potential poly-A sequence;
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DR   EMBL; X55023; CAA38762.1; -; mRNA.
DR   EMBL; AK088844; BAC40607.1; -; mRNA.
DR   EMBL; AK143882; BAE25581.1; -; mRNA.
DR   EMBL; AK146831; BAE27466.1; -; mRNA.
DR   EMBL; BC016400; AAH16400.1; -; mRNA.
DR   EMBL; BC018545; AAH18545.1; -; mRNA.
DR   EMBL; BC106112; AAI06113.1; ALT_SEQ; mRNA.
DR   EMBL; X53584; CAA37653.1; -; mRNA.
DR   IPI; IPI00308885; -.
DR   IPI; IPI00845678; -.
DR   PIR; S13084; HHMS60.
DR   RefSeq; NP_034607.3; NM_010477.4.
DR   UniGene; Mm.1777; -.
DR   UniGene; Mm.476770; -.
DR   ProteinModelPortal; P63038; -.
DR   SMR; P63038; 26-551.
DR   MINT; MINT-1860238; -.
DR   STRING; P63038; -.
DR   PhosphoSite; P63038; -.
DR   SWISS-2DPAGE; P63038; -.
DR   REPRODUCTION-2DPAGE; IPI00308885; -.
DR   REPRODUCTION-2DPAGE; P63038; -.
DR   UCD-2DPAGE; P19227; -.
DR   UCD-2DPAGE; P63038; -.
DR   PRIDE; P63038; -.
DR   Ensembl; ENSMUST00000027123; ENSMUSP00000027123; ENSMUSG00000025980.
DR   GeneID; 15510; -.
DR   KEGG; mmu:15510; -.
DR   CTD; 15510; -.
DR   MGI; MGI:96242; Hspd1.
DR   eggNOG; roNOG14286; -.
DR   GeneTree; ENSGT00390000005727; -.
DR   HOVERGEN; HBG001982; -.
DR   InParanoid; P63038; -.
DR   OMA; CILNKLR; -.
DR   OrthoDB; EOG4PK27J; -.
DR   PhylomeDB; P63038; -.
DR   NextBio; 288418; -.
DR   PMAP-CutDB; P63038; -.
DR   Bgee; P63038; -.
DR   CleanEx; MM_HSPD1; -.
DR   Genevestigator; P63038; -.
DR   GermOnline; ENSMUSG00000025980; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0044459; C:plasma membrane part; IDA:MGI.
DR   GO; GO:0030141; C:stored secretory granule; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0001530; F:lipopolysaccharide binding; IDA:BHF-UCL.
DR   GO; GO:0032727; P:positive regulation of interferon-alpha production; IDA:MGI.
DR   GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:BHF-UCL.
DR   GO; GO:0050870; P:positive regulation of T cell activation; IDA:BHF-UCL.
DR   GO; GO:0042110; P:T cell activation; IDA:MGI.
DR   InterPro; IPR018370; Chaperonin_Cpn60_CS.
DR   InterPro; IPR001844; Chaprnin_Cpn60.
DR   InterPro; IPR002423; Cpn60/TCP-1.
DR   PANTHER; PTHR11353; Cpn60/TCP-1; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00298; CHAPERONIN60.
DR   SUPFAM; SSF48592; GroEL-ATPase; 1.
DR   TIGRFAMs; TIGR02348; GroEL; 1.
DR   PROSITE; PS00296; CHAPERONINS_CPN60; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Chaperone;
KW   Direct protein sequencing; Mitochondrion; Nucleotide-binding;
KW   Phosphoprotein; Transit peptide.
FT   TRANSIT       1     26       Mitochondrion.
FT   CHAIN        27    573       60 kDa heat shock protein, mitochondrial.
FT                                /FTId=PRO_0000005027.
FT   MOD_RES      31     31       N6-acetyllysine (By similarity).
FT   MOD_RES      70     70       Phosphoserine (By similarity).
FT   MOD_RES      82     82       N6-acetyllysine (By similarity).
FT   MOD_RES     125    125       N6-acetyllysine (By similarity).
FT   MOD_RES     130    130       N6-acetyllysine (By similarity).
FT   MOD_RES     202    202       N6-acetyllysine (By similarity).
FT   MOD_RES     218    218       N6-acetyllysine (By similarity).
FT   MOD_RES     223    223       Phosphotyrosine.
FT   MOD_RES     227    227       Phosphotyrosine (By similarity).
FT   MOD_RES     269    269       N6-acetyllysine (By similarity).
FT   MOD_RES     352    352       N6-acetyllysine (By similarity).
FT   MOD_RES     359    359       N6-acetyllysine (By similarity).
FT   MOD_RES     396    396       N6-acetyllysine (By similarity).
FT   MOD_RES     469    469       N6-acetyllysine (By similarity).
FT   MOD_RES     473    473       N6-acetyllysine (By similarity).
FT   MOD_RES     523    523       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1    315       Missing (in isoform 2).
FT                                /FTId=VSP_025020.
FT   CONFLICT      4      4       L -> H (in Ref. 2; AA sequence).
FT   CONFLICT    139    139       E -> K (in Ref. 2; AA sequence).
FT   CONFLICT    251    251       I -> F (in Ref. 5; CAA37653).
FT   CONFLICT    364    364       K -> E (in Ref. 3; BAC40607).
FT   CONFLICT    518    518       I -> V (in Ref. 1; CAA38762).
FT   CONFLICT    527    527       T -> Q (in Ref. 2; AA sequence).
FT   CONFLICT    547    547       T -> V (in Ref. 2; AA sequence).
SQ   SEQUENCE   573 AA;  60955 MW;  0014B58B77D0127B CRC64;
     MLRLPTVLRQ MRPVSRALAP HLTRAYAKDV KFGADARALM LQGVDLLADA VAVTMGPKGR
     TVIIEQSWGS PKVTKDGVTV AKSIDLKDKY KNIGAKLVQD VANNTNEEAG DGTTTATVLA
     RSIAKEGFEK ISKGANPVEI RRGVMLAVDA VIAELKKQSK PVTTPEEIAQ VATISANGDK
     DIGNIISDAM KKVGRKGVIT VKDGKTLNDE LEIIEGMKFD RGYISPYFIN TSKGQKCEFQ
     DAYVLLSEKK ISSVQSIVPA LEIANAHRKP LVIIAEDVDG EALSTLVLNR LKVGLQVVAV
     KAPGFGDNRK NQLKDMAIAT GGAVFGEEGL NLNLEDVQAH DLGKVGEVIV TKDDAMLLKG
     KGDKAHIEKR IQEITEQLDI TTSEYEKEKL NERLAKLSDG VAVLKVGGTS DVEVNEKKDR
     VTDALNATRA AVEEGIVLGG GCALLRCIPA LDSLKPANED QKIGIEIIKR ALKIPAMTIA
     KNAGVEGSLI VEKILQSSSE VGYDAMLGDF VNMVEKGIID PTKVVRTALL DAAGVASLLT
     TAEAVVTEIP KEEKDPGMGA MGGMGGGMGG GMF
//
ID   CPLX1_MOUSE             Reviewed;         134 AA.
AC   P63040; O09057; O09142; Q3UYB3; Q64276; Q91WJ3;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Complexin-1;
DE   AltName: Full=921-S;
DE   AltName: Full=Complexin I;
DE            Short=CPX I;
DE   AltName: Full=Synaphin-2;
GN   Name=Cplx1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=95361923; PubMed=7635198; DOI=10.1016/0014-5793(95)00713-J;
RA   Takahashi S., Yamamoto H., Matsuda Z., Ogawa M., Yagyu K.,
RA   Taniguchi T., Miyata T., Kaba H., Higuchi T., Okutani F., Fujimoto S.;
RT   "Identification of two highly homologous presynaptic proteins
RT   distinctly localized at the dendritic and somatic synapses.";
RL   FEBS Lett. 368:455-460(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Inner ear, Medulla oblongata, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=15126625; DOI=10.1242/jcs.01041;
RA   Abderrahmani A., Niederhauser G., Plaisance V., Roehrich M.-E.,
RA   Lenain V., Coppola T., Regazzi R., Waeber G.;
RT   "Complexin I regulates glucose-induced secretion in pancreatic beta-
RT   cells.";
RL   J. Cell Sci. 117:2239-2247(2004).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16000319; DOI=10.1093/hmg/ddi239;
RA   Glynn D., Drew C.J., Reim K., Brose N., Morton A.J.;
RT   "Profound ataxia in complexin I knockout mice masks a complex
RT   phenotype that includes exploratory and habituation deficits.";
RL   Hum. Mol. Genet. 14:2369-2385(2005).
RN   [6]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15911881; DOI=10.1083/jcb.200502115;
RA   Reim K., Wegmeyer H., Brandstaetter J.H., Xue M., Rosenmund C.,
RA   Dresbach T., Hofmann K., Brose N.;
RT   "Structurally and functionally unique complexins at retinal ribbon
RT   synapses.";
RL   J. Cell Biol. 169:669-680(2005).
CC   -!- FUNCTION: Positively regulates a late step in synaptic vesicle
CC       exocytosis. Also involved in glucose-induced secretion of insulin
CC       by pancreatic beta-cells. Essential for motor behavior.
CC   -!- SUBUNIT: Binds to the SNARE core complex containing SNAP25, VAMP2
CC       and STX1A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Note=Enriched at
CC       synaptic-releasing sites in mature neurons.
CC   -!- TISSUE SPECIFICITY: Nervous system, and pancreatic islet cells.
CC       Present in many brain regions, including hippocampus and
CC       cerebellum. In the retina, present at conventional amacrine cell
CC       synapses (at protein level).
CC   -!- DEVELOPMENTAL STAGE: In the brain, expression starts at P6 and
CC       increases to reach a plateau at P20.
CC   -!- DISRUPTION PHENOTYPE: Mice have no obvious brain abnormality, but
CC       suffer from severe ataxia with dystonia starting from P7. Adult
CC       mice lacking Cplx1 are not capable of coordinated running or
CC       swimming and exhibit pronounced resting tremor. They also fail to
CC       habituate to confinement and have reduced exploration abilities in
CC       open field.
CC   -!- SIMILARITY: Belongs to the complexin/synaphin family.
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DR   EMBL; D38614; BAA07605.1; -; mRNA.
DR   EMBL; AK134820; BAE22299.1; -; mRNA.
DR   EMBL; AK158166; BAE34390.1; -; mRNA.
DR   EMBL; AK159026; BAE34774.1; -; mRNA.
DR   EMBL; BC014803; AAH14803.1; -; mRNA.
DR   IPI; IPI00132278; -.
DR   PIR; S66294; S66294.
DR   RefSeq; NP_031782.3; NM_007756.3.
DR   UniGene; Mm.5195; -.
DR   ProteinModelPortal; P63040; -.
DR   SMR; P63040; 32-72.
DR   STRING; P63040; -.
DR   PhosphoSite; P63040; -.
DR   PRIDE; P63040; -.
DR   Ensembl; ENSMUST00000046892; ENSMUSP00000038502; ENSMUSG00000033615.
DR   GeneID; 12889; -.
DR   KEGG; mmu:12889; -.
DR   UCSC; uc008yof.1; mouse.
DR   CTD; 12889; -.
DR   MGI; MGI:104727; Cplx1.
DR   eggNOG; maNOG20874; -.
DR   GeneTree; ENSGT00490000043416; -.
DR   HOGENOM; HBG444230; -.
DR   HOVERGEN; HBG062792; -.
DR   InParanoid; P63040; -.
DR   OMA; SIVDTVM; -.
DR   OrthoDB; EOG44MXTP; -.
DR   NextBio; 282486; -.
DR   ArrayExpress; P63040; -.
DR   Bgee; P63040; -.
DR   CleanEx; MM_CPLX1; -.
DR   Genevestigator; P63040; -.
DR   GermOnline; ENSMUSG00000033615; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005326; F:neurotransmitter transporter activity; IMP:UniProtKB.
DR   GO; GO:0030073; P:insulin secretion; IMP:UniProtKB.
DR   GO; GO:0016079; P:synaptic vesicle exocytosis; IMP:UniProtKB.
DR   InterPro; IPR008849; Synaphin.
DR   PANTHER; PTHR16705; Synaphin; 1.
DR   Pfam; PF05835; Synaphin; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Exocytosis; Neurotransmitter transport;
KW   Transport.
FT   CHAIN         1    134       Complexin-1.
FT                                /FTId=PRO_0000144871.
FT   REGION       48     70       Interaction with the SNARE complex (By
FT                                similarity).
FT   COILED       29     64       Potential.
FT   CONFLICT     84     84       A -> V (in Ref. 3; AAH14803).
SQ   SEQUENCE   134 AA;  15122 MW;  BA1B6F074923A3A4 CRC64;
     MEFVMKQALG GATKDMGKML GGDEEKDPDA AKKEEERQEA LRQAEEERKA KYAKMEAERE
     VMRQGIRDKY GIKKKEEREA EAQAAMEANS EGSLTRPKKA IPPGCGDEPE EEDESILDTV
     IKYLPGPLQD MFKK
//
ID   STMN4_MOUSE             Reviewed;         189 AA.
AC   P63042; O35414; O35415; O35416;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Stathmin-4;
DE   AltName: Full=Stathmin-like protein B3;
DE            Short=RB3;
GN   Name=Stmn4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ozon S., Sobel A.;
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the stathmin family.
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CC   -----------------------------------------------------------------------
DR   EMBL; AF105222; AAC96328.1; -; mRNA.
DR   EMBL; BC046752; AAH46752.1; -; mRNA.
DR   IPI; IPI00130663; -.
DR   RefSeq; NP_062649.1; NM_019675.2.
DR   UniGene; Mm.35474; -.
DR   ProteinModelPortal; P63042; -.
DR   SMR; P63042; 50-185.
DR   STRING; P63042; -.
DR   PhosphoSite; P63042; -.
DR   PRIDE; P63042; -.
DR   Ensembl; ENSMUST00000074523; ENSMUSP00000074113; ENSMUSG00000022044.
DR   GeneID; 56471; -.
DR   KEGG; mmu:56471; -.
DR   UCSC; uc007ukf.1; mouse.
DR   CTD; 56471; -.
DR   MGI; MGI:1931224; Stmn4.
DR   eggNOG; roNOG08990; -.
DR   GeneTree; ENSGT00390000003691; -.
DR   HOVERGEN; HBG054037; -.
DR   OMA; AFEENNN; -.
DR   OrthoDB; EOG46MBKT; -.
DR   PhylomeDB; P63042; -.
DR   NextBio; 312738; -.
DR   ArrayExpress; P63042; -.
DR   Bgee; P63042; -.
DR   CleanEx; MM_STMN4; -.
DR   Genevestigator; P63042; -.
DR   GermOnline; ENSMUSG00000022044; Mus musculus.
DR   InterPro; IPR000956; Stathmin.
DR   PANTHER; PTHR10104; Stathmin; 1.
DR   Pfam; PF00836; Stathmin; 1.
DR   PIRSF; PIRSF002285; Stathmin; 1.
DR   PRINTS; PR00345; STATHMIN.
DR   SUPFAM; SSF101494; Stathmin; 1.
DR   PROSITE; PS00563; STATHMIN_1; 1.
DR   PROSITE; PS01041; STATHMIN_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil.
FT   CHAIN         1    189       Stathmin-4.
FT                                /FTId=PRO_0000182407.
FT   COILED       90    189       Potential.
SQ   SEQUENCE   189 AA;  22087 MW;  4D61AAE5E8131551 CRC64;
     MTLAAYKEKM KELPLVSLFC SCFLSDPLNK SSYKYEADTV DLNWCVISDM EVIELNKCTS
     GQSFEVILKP PSFDGVPEFN ASLPRRRDPS LEEIQKKLEA AEERRKYQEA ELLKHLAEKR
     EHEREVIQKA IEENNNFIKM AKEKLAQKME SNKENREAHL AAMLERLQEK DKHAEEVRKN
     KELKEEASR
//
ID   VAMP2_MOUSE             Reviewed;         116 AA.
AC   P63044; Q64357;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Vesicle-associated membrane protein 2;
DE            Short=VAMP-2;
DE   AltName: Full=Synaptobrevin-2;
GN   Name=Vamp2; Synonyms=Syb2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   MEDLINE=98104125; PubMed=9430681; DOI=10.1074/jbc.273.3.1444;
RA   Martin L.B., Shewan A., Millar C.A., Gould G.W., James D.E.;
RT   "Vesicle-associated membrane protein 2 plays a specific role in the
RT   insulin-dependent trafficking of the facilitative glucose transporter
RT   GLUT4 in 3T3-L1 adipocytes.";
RL   J. Biol. Chem. 273:1444-1452(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH STX4.
RX   PubMed=17548353; DOI=10.1074/jbc.M701661200;
RA   Ke B., Oh E., Thurmond D.C.;
RT   "Doc2beta is a novel Munc18c-interacting partner and positive effector
RT   of syntaxin 4-mediated exocytosis.";
RL   J. Biol. Chem. 282:21786-21797(2007).
RN   [5]
RP   PROTEIN SEQUENCE OF 31-47 AND 60-83, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   INTERACTION WITH BVES.
RX   PubMed=20057356; DOI=10.1038/emboj.2009.379;
RA   Hager H.A., Roberts R.J., Cross E.E., Proux-Gillardeaux V.,
RA   Bader D.M.;
RT   "Identification of a novel Bves function: regulation of vesicular
RT   transport.";
RL   EMBO J. 29:532-545(2010).
CC   -!- FUNCTION: Involved in the targeting and/or fusion of transport
CC       vesicles to their target membrane.
CC   -!- SUBUNIT: Part of the SNARE core complex containing SNAP25, VAMP2
CC       and STX1A. This complex binds to CPLX1. Interacts with VAPA and
CC       VAPB (By similarity). Interacts with BVES and STX4.
CC   -!- INTERACTION:
CC       P60766:Cdc42; NbExp=2; IntAct=EBI-521920, EBI-81763;
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane; Single-pass type IV membrane protein.
CC       Cell junction, synapse, synaptosome. Note=Neuronal synaptic
CC       vesicles.
CC   -!- SIMILARITY: Belongs to the synaptobrevin family.
CC   -!- SIMILARITY: Contains 1 v-SNARE coiled-coil homology domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; U60150; AAB03463.1; -; mRNA.
DR   EMBL; AK090178; BAC41125.1; -; mRNA.
DR   EMBL; BC055105; AAH55105.1; -; mRNA.
DR   IPI; IPI00229703; -.
DR   RefSeq; NP_033523.1; NM_009497.3.
DR   UniGene; Mm.28643; -.
DR   ProteinModelPortal; P63044; -.
DR   SMR; P63044; 30-116.
DR   DIP; DIP-29065N; -.
DR   IntAct; P63044; 5.
DR   MINT; MINT-2411573; -.
DR   STRING; P63044; -.
DR   PRIDE; P63044; -.
DR   Ensembl; ENSMUST00000021273; ENSMUSP00000021273; ENSMUSG00000020894.
DR   GeneID; 22318; -.
DR   KEGG; mmu:22318; -.
DR   UCSC; uc007jpe.1; mouse.
DR   CTD; 22318; -.
DR   MGI; MGI:1313277; Vamp2.
DR   HOVERGEN; HBG006675; -.
DR   OMA; GVICVII; -.
DR   OrthoDB; EOG43JC6B; -.
DR   PhylomeDB; P63044; -.
DR   NextBio; 302529; -.
DR   ArrayExpress; P63044; -.
DR   Bgee; P63044; -.
DR   CleanEx; MM_VAMP2; -.
DR   Genevestigator; P63044; -.
DR   GermOnline; ENSMUSG00000020894; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR   GO; GO:0019717; C:synaptosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR   GO; GO:0042589; C:zymogen granule membrane; IDA:MGI.
DR   GO; GO:0005516; F:calmodulin binding; IDA:MGI.
DR   GO; GO:0005543; F:phospholipid binding; IDA:MGI.
DR   GO; GO:0019905; F:syntaxin binding; IPI:UniProtKB.
DR   GO; GO:0017156; P:calcium ion-dependent exocytosis; IDA:MGI.
DR   GO; GO:0006944; P:cellular membrane fusion; IMP:MGI.
DR   GO; GO:0017157; P:regulation of exocytosis; IDA:MGI.
DR   GO; GO:0016079; P:synaptic vesicle exocytosis; IMP:MGI.
DR   InterPro; IPR001388; Synaptobrevin.
DR   InterPro; IPR016444; Synaptobrevin_met/fun.
DR   Pfam; PF00957; Synaptobrevin; 1.
DR   PIRSF; PIRSF005409; Synaptobrevin_euk; 1.
DR   PRINTS; PR00219; SYNAPTOBREVN.
DR   PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR   PROSITE; PS50892; V_SNARE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell junction; Coiled coil; Cytoplasmic vesicle;
KW   Direct protein sequencing; Membrane; Phosphoprotein; Synapse;
KW   Synaptosome; Transmembrane; Transmembrane helix.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    116       Vesicle-associated membrane protein 2.
FT                                /FTId=PRO_0000206725.
FT   TOPO_DOM      2     94       Cytoplasmic (Potential).
FT   TRANSMEM     95    114       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   TOPO_DOM    115    116       Vesicular (Potential).
FT   DOMAIN       31     91       v-SNARE coiled-coil homology.
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES      75     75       Phosphoserine.
SQ   SEQUENCE   116 AA;  12691 MW;  4A0D0D56B5409D0A CRC64;
     MSATAATVPP AAPAGEGGPP APPPNLTSNR RLQQTQAQVD EVVDIMRVNV DKVLERDQKL
     SELDDRADAL QAGASQFETS AAKLKRKYWW KNLKMMIILG VICAIILIII IVYFST
//
ID   ST4A1_MOUSE             Reviewed;         284 AA.
AC   P63046; O88872; Q3TXY5; Q91XS5; Q9CWY7; Q9DC97;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Sulfotransferase 4A1;
DE            Short=ST4A1;
DE            EC=2.8.2.-;
DE   AltName: Full=Brain sulfotransferase-like protein;
DE            Short=mBR-STL;
DE   AltName: Full=Nervous system sulfotransferase;
DE            Short=NST;
GN   Name=Sult4a1; Synonyms=Sultx3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=22035352; PubMed=12039030; DOI=10.1016/S0378-1119(02)00431-6;
RA   Sakakibara Y., Suiko M., Pai T.G., Nakayama T., Takami Y.,
RA   Katafuchi J., Liu M.-C.;
RT   "Highly conserved mouse and human brain sulfotransferases: molecular
RT   cloning, expression, and functional characterization.";
RL   Gene 285:39-47(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May catalyze the sulfate conjugation of many drugs,
CC       xenobiotic compounds, hormones, and neurotransmitters. Displays
CC       activity towards L-triiodothyronine, thyroxine, estrone, p-
CC       nitrophenol, 2-naphtylamine, and 2-naphtol. May have a role in the
CC       sulfation of drugs and neurotransmitters in the CNS.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P63046-1, Q9DC97-1;
CC         Sequence=Displayed;
CC       Name=2;
CC         IsoId=P63046-2, Q9DC97-2;
CC         Sequence=VSP_006305;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, cerebellum and
CC       hypothalamus. Not detected in pancreas, liver, lung, intestine,
CC       kidney, uterus, adrenal gland, thymus, spleen, epididymis,
CC       testicle, and heart.
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF059257; AAC63999.1; -; mRNA.
DR   EMBL; AK003034; BAB22522.1; -; mRNA.
DR   EMBL; AK010293; BAB26829.1; -; mRNA.
DR   EMBL; AK159034; BAE34779.1; -; mRNA.
DR   EMBL; BC051132; AAH51132.1; -; mRNA.
DR   EMBL; BC054757; AAH54757.1; -; mRNA.
DR   IPI; IPI00153862; -.
DR   IPI; IPI00228515; -.
DR   RefSeq; NP_038901.3; NM_013873.3.
DR   UniGene; Mm.248796; -.
DR   ProteinModelPortal; P63046; -.
DR   SMR; P63046; 13-284.
DR   STRING; P63046; -.
DR   PhosphoSite; P63046; -.
DR   PRIDE; P63046; -.
DR   Ensembl; ENSMUST00000082365; ENSMUSP00000080973; ENSMUSG00000018865.
DR   Ensembl; ENSMUST00000109463; ENSMUSP00000105089; ENSMUSG00000018865.
DR   GeneID; 29859; -.
DR   KEGG; mmu:29859; -.
DR   UCSC; uc007xbs.1; mouse.
DR   UCSC; uc007xbt.1; mouse.
DR   CTD; 29859; -.
DR   MGI; MGI:1888971; Sult4a1.
DR   eggNOG; maNOG09142; -.
DR   GeneTree; ENSGT00570000079056; -.
DR   HOGENOM; HBG744340; -.
DR   HOVERGEN; HBG105932; -.
DR   InParanoid; P63046; -.
DR   OMA; EDMYKDL; -.
DR   OrthoDB; EOG4HMJ9Q; -.
DR   PhylomeDB; P63046; -.
DR   NextBio; 307062; -.
DR   ArrayExpress; P63046; -.
DR   Bgee; P63046; -.
DR   CleanEx; MM_SULT4A1; -.
DR   Genevestigator; P63046; -.
DR   GermOnline; ENSMUSG00000018865; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; TAS:MGI.
DR   GO; GO:0008146; F:sulfotransferase activity; IDA:MGI.
DR   GO; GO:0008202; P:steroid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006790; P:sulfur compound metabolic process; IDA:MGI.
DR   InterPro; IPR000863; Sulfotransferase_dom.
DR   Pfam; PF00685; Sulfotransfer_1; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Lipid metabolism; Steroid metabolism;
KW   Transferase.
FT   CHAIN         1    284       Sulfotransferase 4A1.
FT                                /FTId=PRO_0000085168.
FT   NP_BIND     246    254       PAPS (Potential).
FT   VAR_SEQ     248    284       GRVGLWKDIFTVSMNEKFDLVYKQKMGKCDLTFDFYL ->
FT                                AHCLFTQKIALRWRGCRGSGSRLHCLDLVHVTA (in
FT                                isoform 2).
FT                                /FTId=VSP_006305.
FT   CONFLICT      6      6       A -> R (in Ref. 2; BAB22522).
SQ   SEQUENCE   284 AA;  33054 MW;  FCAE940F7219E6FC CRC64;
     MAESEAETPG TPGEFESKYF EFHGVRLPPF CRGKMEDIAD FPVRPSDVWI VTYPKSGTSL
     LQEVVYLVSQ GADPDEIGLM NIDEQLPVLE YPQPGLDIIK ELTSPRLIKS HLPYRFLPSD
     LHNGDSKVIY MARNPKDLVV SYYQFHRSLR TMSYRGTFQE FCRRFMNDKL GYGSWFEHVQ
     EFWEHRMDAN VLFLKYEDMH RDLVTMVEQL ARFLGVSCDK AQLESLIEHC HQLVDQCCNA
     EALPVGRGRV GLWKDIFTVS MNEKFDLVYK QKMGKCDLTF DFYL
//
ID   MK01_MOUSE              Reviewed;         358 AA.
AC   P63085; P27703; Q3V1U6;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Mitogen-activated protein kinase 1;
DE            Short=MAP kinase 1;
DE            Short=MAPK 1;
DE            EC=2.7.11.24;
DE   AltName: Full=ERT1;
DE   AltName: Full=Extracellular signal-regulated kinase 2;
DE            Short=ERK-2;
DE   AltName: Full=MAP kinase isoform p42;
DE            Short=p42-MAPK;
DE   AltName: Full=Mitogen-activated protein kinase 2;
DE            Short=MAP kinase 2;
DE            Short=MAPK 2;
GN   Name=Mapk1; Synonyms=Erk2, Mapk, Prkm1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss; TISSUE=Fibroblast;
RX   MEDLINE=91305126; PubMed=1649458; DOI=10.1093/nar/19.13.3743;
RA   Her J.-H., Wu J.-S., Rall T.B., Sturgill T.W., Weber M.J.;
RT   "Sequence of pp42/MAP kinase, a serine/threonine kinase regulated by
RT   tyrosine phosphorylation.";
RL   Nucleic Acids Res. 19:3743-3743(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Brain, Head, Thymus, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 54-65; 76-89; 137-162; 171-189; 193-201 AND
RP   260-268, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 152-190.
RC   STRAIN=CBA; TISSUE=Bone marrow;
RX   MEDLINE=93185941; PubMed=8444355; DOI=10.1016/0378-1119(93)90411-U;
RA   Ershler M.A., Nagorskaya T.V., Visser J.W.M., Belyavsky A.V.;
RT   "Novel CDC2-related protein kinases produced in murine hematopoietic
RT   stem cells.";
RL   Gene 124:305-306(1993).
RN   [6]
RP   PHOSPHORYLATION AT THR-183 AND TYR-185, AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=91184134; PubMed=1849075;
RA   Payne D.M., Rossomando A.J., Martino P., Erickson A.K., Her J.-H.,
RA   Shabanowitz J., Hunt D.F., Weber M.J., Sturgill T.W.;
RT   "Identification of the regulatory phosphorylation sites in
RT   pp42/mitogen-activated protein kinase (MAP kinase).";
RL   EMBO J. 10:885-892(1991).
RN   [7]
RP   INTERACTION WITH MORG1.
RX   PubMed=15118098; DOI=10.1073/pnas.0305894101;
RA   Vomastek T., Schaeffer H.-J., Tarcsafalvi A., Smolkin M.E.,
RA   Bissonette E.A., Weber M.J.;
RT   "Modular construction of a signaling scaffold: MORG1 interacts with
RT   components of the ERK cascade and links ERK signaling to specific
RT   agonists.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:6981-6986(2004).
RN   [8]
RP   PHOSPHORYLATION OF SPZ1.
RX   PubMed=15899793; DOI=10.1158/0008-5472.CAN-04-3658;
RA   Hsu S.-H., Hsieh-Li H.-M., Huang H.-Y., Huang P.-H., Li H.;
RT   "bHLH-zip transcription factor Spz1 mediates mitogen-activated protein
RT   kinase cell proliferation, transformation, and tumorigenesis.";
RL   Cancer Res. 65:4041-4050(2005).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Involved in both the initiation and regulation of
CC       meiosis, mitosis, and postmitotic functions in differentiated
CC       cells by phosphorylating a number of transcription factors such as
CC       ELK1. Phosphorylates EIF4EBP1; required for initiation of
CC       translation. Phosphorylates microtubule-associated protein 2
CC       (MAP2), heat shock factor protein 4 (HSF4) and ARHGEF2 (By
CC       similarity). Phosphorylates SPZ1.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activated by phosphorylation on tyrosine and
CC       threonine in response to insulin and NGF. Both phosphorylations
CC       are required for activity (By similarity).
CC   -!- SUBUNIT: Interacts with ARHGEF2, HSF4 and NISCH (By similarity).
CC       Interacts with MORG1. Interacts (phosphorylated form) with CAV2
CC       ('Tyr-19'-phosphorylated form); the interaction, promoted by
CC       insulin, leads to nuclear location and MAPK1 activation. Interacts
CC       with ARRB2 (By similarity). Interacts with ADAM15 (By similarity).
CC   -!- INTERACTION:
CC       O43521-1:BCL2L11 (xeno); NbExp=1; IntAct=EBI-397697, EBI-526416;
CC       Q62108:Dlg4; NbExp=1; IntAct=EBI-397697, EBI-300895;
CC       P19419:ELK1 (xeno); NbExp=1; IntAct=EBI-397697, EBI-726632;
CC       P49841:GSK3B (xeno); NbExp=1; IntAct=EBI-397697, EBI-373586;
CC       Q03172:Hivep1; NbExp=3; IntAct=EBI-397697, EBI-646850;
CC       O08605:Mknk1; NbExp=2; IntAct=EBI-397697, EBI-646859;
CC       Q8CDB0:Mknk2; NbExp=3; IntAct=EBI-397697, EBI-646209;
CC       Q9Z2B9:Rps6ka4; NbExp=2; IntAct=EBI-397697, EBI-412887;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC       whose phosphorylation activates the MAP kinases.
CC   -!- PTM: Dually phosphorylated on Thr-183 and Tyr-185, which activates
CC       the enzyme. Dephosphorylated by PTPRJ at Tyr-185 (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. MAP kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; X58712; CAA41548.1; -; mRNA.
DR   EMBL; AK035386; BAC29053.1; -; mRNA.
DR   EMBL; AK048127; BAC33251.1; -; mRNA.
DR   EMBL; AK087925; BAC40044.1; -; mRNA.
DR   EMBL; AK132241; BAE21053.1; -; mRNA.
DR   EMBL; BC058258; AAH58258.1; -; mRNA.
DR   EMBL; D10939; BAA01733.1; -; mRNA.
DR   IPI; IPI00119663; -.
DR   PIR; S16444; S16444.
DR   RefSeq; NP_001033752.1; NM_001038663.1.
DR   RefSeq; NP_036079.1; NM_011949.3.
DR   UniGene; Mm.196581; -.
DR   ProteinModelPortal; P63085; -.
DR   SMR; P63085; 6-355.
DR   DIP; DIP-661N; -.
DR   IntAct; P63085; 58.
DR   MINT; MINT-125264; -.
DR   STRING; P63085; -.
DR   PhosphoSite; P63085; -.
DR   PRIDE; P63085; -.
DR   Ensembl; ENSMUST00000023462; ENSMUSP00000023462; ENSMUSG00000063358.
DR   Ensembl; ENSMUST00000069107; ENSMUSP00000065983; ENSMUSG00000063358.
DR   Ensembl; ENSMUST00000115731; ENSMUSP00000111396; ENSMUSG00000063358.
DR   GeneID; 26413; -.
DR   KEGG; mmu:26413; -.
DR   NMPDR; fig|10090.3.peg.30922; -.
DR   UCSC; uc007yjq.1; mouse.
DR   CTD; 26413; -.
DR   MGI; MGI:1346858; Mapk1.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG014652; -.
DR   InParanoid; P63085; -.
DR   OMA; LAREDTA; -.
DR   OrthoDB; EOG45HRXM; -.
DR   PhylomeDB; P63085; -.
DR   BRENDA; 2.7.11.24; 244.
DR   NextBio; 304409; -.
DR   ArrayExpress; P63085; -.
DR   Bgee; P63085; -.
DR   CleanEx; MM_MAPK1; -.
DR   Genevestigator; P63085; -.
DR   GermOnline; ENSMUSG00000063358; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR   GO; GO:0005654; C:nucleoplasm; EXP:Reactome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004707; F:MAP kinase activity; IDA:MGI.
DR   GO; GO:0001784; F:phosphotyrosine binding; IMP:MGI.
DR   GO; GO:0008353; F:RNA polymerase II carboxy-terminal domain kinase activity; IDA:UniProtKB.
DR   GO; GO:0030528; F:transcription regulator activity; NAS:UniProtKB.
DR   GO; GO:0050853; P:B cell receptor signaling pathway; IDA:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0019858; P:cytosine metabolic process; IDA:MGI.
DR   GO; GO:0060716; P:labyrinthine layer blood vessel development; IMP:MGI.
DR   GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:MGI.
DR   GO; GO:0045596; P:negative regulation of cell differentiation; IGI:MGI.
DR   GO; GO:0009887; P:organ morphogenesis; IDA:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR   GO; GO:0051090; P:regulation of transcription factor activity; NAS:UniProtKB.
DR   GO; GO:0006974; P:response to DNA damage stimulus; IDA:MGI.
DR   GO; GO:0043330; P:response to exogenous dsRNA; IDA:MGI.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IDA:MGI.
DR   InterPro; IPR008349; Erk_1_2_MAPK.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR003527; MAP_kinase_CS.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01770; ERK1ERK2MAPK.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS01351; MAPK; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cell cycle; Direct protein sequencing;
KW   Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    358       Mitogen-activated protein kinase 1.
FT                                /FTId=PRO_0000186248.
FT   DOMAIN       23    311       Protein kinase.
FT   NP_BIND      29     37       ATP (By similarity).
FT   MOTIF       183    185       TXY.
FT   COMPBIAS      2      7       Poly-Ala.
FT   ACT_SITE    147    147       Proton acceptor (By similarity).
FT   BINDING      52     52       ATP (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      61     61       Phosphothreonine (By similarity).
FT   MOD_RES     179    179       Phosphothreonine (By similarity).
FT   MOD_RES     183    183       Phosphothreonine.
FT   MOD_RES     185    185       Phosphotyrosine.
FT   MOD_RES     188    188       Phosphothreonine (By similarity).
FT   MOD_RES     200    200       Phosphoserine (By similarity).
FT   MOD_RES     282    282       Phosphoserine (By similarity).
SQ   SEQUENCE   358 AA;  41276 MW;  3BBCF22471EDBA0B CRC64;
     MAAAAAAGPE MVRGQVFDVG PRYTNLSYIG EGAYGMVCSA YDNLNKVRVA IKKISPFEHQ
     TYCQRTLREI KILLRFRHEN IIGINDIIRA PTIEQMKDVY IVQDLMETDL YKLLKTQHLS
     NDHICYFLYQ ILRGLKYIHS ANVLHRDLKP SNLLLNTTCD LKICDFGLAR VADPDHDHTG
     FLTEYVATRW YRAPEIMLNS KGYTKSIDIW SVGCILAEML SNRPIFPGKH YLDQLNHILG
     ILGSPSQEDL NCIINLKARN YLLSLPHKNK VPWNRLFPNA DSKALDLLDK MLTFNPHKRI
     EVEQALAHPY LEQYYDPSDE PIAEAPFKFD MELDDLPKEK LKELIFEETA RFQPGYRS
//
ID   1433Z_MOUSE             Reviewed;         245 AA.
AC   P63101; P35215; P70197; P97286; Q3TSF1; Q5EBQ1;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=14-3-3 protein zeta/delta;
DE   AltName: Full=Protein kinase C inhibitor protein 1;
DE            Short=KCIP-1;
DE   AltName: Full=SEZ-2;
GN   Name=Ywhaz;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=96216731; PubMed=8645260; DOI=10.1006/bbrc.1996.0313;
RA   Kajiwara K., Nagawawa H., Shimizu-Nishikawa K., Ookura T., Kimura M.,
RA   Sugaya E.;
RT   "Molecular characterization of seizure-related genes isolated by
RT   differential screening.";
RL   Biochem. Biophys. Res. Commun. 219:795-799(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/Sv;
RA   Takihara Y., Irie K., Nomura M., Motaleb M., Matsumoto K., Shimada K.;
RT   "14-3-3 family members play an important role in tumorigenic
RT   transformation of NIH 3T3 cells and retinoic acid-mediated F9 cell
RT   differentiation.";
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CDK16.
RX   MEDLINE=97340943; PubMed=9197417; DOI=10.1007/s004380050453;
RA   Sladeczek F., Camonis J.H., Burnol A.-F., Le Bouffant F.;
RT   "The Cdk-like protein PCTAIRE-1 from mouse brain associates with p11
RT   and 14-3-3 proteins.";
RL   Mol. Gen. Genet. 254:571-577(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH WEE1.
RX   MEDLINE=97168955; PubMed=9016762; DOI=10.1006/bbrc.1996.5933;
RA   Honda R., Ohba Y., Yasuda H.;
RT   "14-3-3 zeta protein binds to the carboxyl half of mouse wee1
RT   kinase.";
RL   Biochem. Biophys. Res. Commun. 230:262-265(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Blastocyst, Bone marrow macrophage, Egg, Embryonic kidney, and
RC   Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 12-55; 61-68; 84-115; 128-167 AND 194-245, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Friebe K., Yang J.W., Zigmond M.,
RA   Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [8]
RP   INTERACTION WITH MLF1.
RX   MEDLINE=22287351; PubMed=12176995; DOI=10.1074/jbc.M206041200;
RA   Lim R., Winteringham L.N., Williams J.H., McCulloch R.K., Ingley E.,
RA   Tiao J.Y.-H., Lalonde J.-P., Tsai S., Tilbrook P.A., Sun Y., Wu X.,
RA   Morris S.W., Klinken S.P.;
RT   "MADM, a novel adaptor protein that mediates phosphorylation of the
RT   14-3-3 binding site of myeloid leukemia factor 1.";
RL   J. Biol. Chem. 277:40997-41008(2002).
CC   -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC       spectrum of both general and specialized signaling pathway. Binds
CC       to a large number of partners, usually by recognition of a
CC       phosphoserine or phosphothreonine motif. Binding generally results
CC       in the modulation of the activity of the binding partner.
CC   -!- SUBUNIT: Homodimer. Heterodimerizes with YWHAE (By similarity).
CC       Homo- and hetero-dimerization is inhibited by phosphorylation on
CC       Ser-58 (By similarity). Interacts with FOXO4, NOXA1, SSH1 and
CC       ARHGEF2. Interacts with CDK16 and with WEE1 (C-terminal).
CC       Interacts with MLF1 (phosphorylated form); the interaction retains
CC       it in the cytoplasm. Interacts with BSPRY. Interacts with Thr-
CC       phosphorylated ITGB2 (By similarity). Interacts with Pseudomonas
CC       aeruginosa exoS (unphosphorylated form). Interacts with BAX; the
CC       interaction occurs in the cytoplasm. Under stress conditions,
CC       MAPK8-mediated phosphorylation releases BAX to mitochondria.
CC       Interacts with phosphorylated RAF1; the interaction is inhibited
CC       when YWHAZ is phosphorylated on Thr-232. Interacts with TP53; the
CC       interaction enhances p53 transcriptional acivity. The Ser-58
CC       phosphorylated form inhibits this interaction and p53
CC       transcriptional activity. Interacts with ABL1 (phosphorylated
CC       form); the interaction retains ABL1 in the cytoplasm. Interacts
CC       with AANAT ('Thr-31' phosphorylated form); the interaction
CC       modulates AANAT enzymatic activity through preventing
CC       dephosphorylation and/or proteolysis and stabilizing substrate
CC       binding. Subsequently, a second molecule of AANAT ('Ser-205'
CC       phosphorylated form), can bind the other YWHAZ monomer with
CC       similar effect. Interacts with AKT1; the interaction
CC       phosphorylates YWHAZ and modulates dimerization (By similarity).
CC       Interacts with GAB2 (By similarity).
CC   -!- INTERACTION:
CC       Q9QWV4:Mlf1; NbExp=1; IntAct=EBI-354751, EBI-354765;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=Located to stage
CC       I to stage IV melanosomes (By similarity).
CC   -!- PTM: The delta, brain-specific form differs from the zeta form in
CC       being phosphorylated (By similarity). Phosphorylation on Ser-184
CC       by MAPK8; promotes dissociation of BAX and translocation of BAX to
CC       mitochondria. Phosphorylation on Ser-58 by PKA; disrupts
CC       homodimerization and heterodimerization with YHAE and TP53. This
CC       phosphorylation appears to be activated by sphingosine.
CC       Phosphorylation on Thr-232; inhibits binding of RAF1 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the 14-3-3 family.
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DR   EMBL; D78647; BAA11464.1; -; mRNA.
DR   EMBL; D87660; BAA13421.1; -; mRNA.
DR   EMBL; U79231; AAC53254.1; -; mRNA.
DR   EMBL; D83037; BAA11751.1; -; mRNA.
DR   EMBL; AK083368; BAC38887.1; -; mRNA.
DR   EMBL; AK145657; BAE26570.1; -; mRNA.
DR   EMBL; AK146800; BAE27442.1; -; mRNA.
DR   EMBL; AK150381; BAE29512.1; -; mRNA.
DR   EMBL; AK151900; BAE30783.1; -; mRNA.
DR   EMBL; AK162099; BAE36724.1; -; mRNA.
DR   EMBL; AK167128; BAE39275.1; -; mRNA.
DR   EMBL; BC050891; AAH50891.1; -; mRNA.
DR   EMBL; BC089334; AAH89334.1; -; mRNA.
DR   IPI; IPI00116498; -.
DR   PIR; JC5384; JC5384.
DR   RefSeq; NP_035870.1; NM_011740.3.
DR   UniGene; Mm.3360; -.
DR   ProteinModelPortal; P63101; -.
DR   SMR; P63101; 1-230.
DR   DIP; DIP-31894N; -.
DR   IntAct; P63101; 147.
DR   MINT; MINT-101845; -.
DR   STRING; P63101; -.
DR   PhosphoSite; P63101; -.
DR   PMMA-2DPAGE; P63101; -.
DR   REPRODUCTION-2DPAGE; P63101; -.
DR   UCD-2DPAGE; P63101; -.
DR   PRIDE; P63101; -.
DR   Ensembl; ENSMUST00000022894; ENSMUSP00000022894; ENSMUSG00000022285.
DR   Ensembl; ENSMUST00000110361; ENSMUSP00000105990; ENSMUSG00000022285.
DR   Ensembl; ENSMUST00000110362; ENSMUSP00000105991; ENSMUSG00000022285.
DR   GeneID; 22631; -.
DR   KEGG; mmu:22631; -.
DR   UCSC; uc007vmz.1; mouse.
DR   CTD; 22631; -.
DR   MGI; MGI:109484; Ywhaz.
DR   eggNOG; maNOG07858; -.
DR   HOGENOM; HBG611720; -.
DR   HOVERGEN; HBG050423; -.
DR   InParanoid; P63101; -.
DR   OMA; VMDKNEL; -.
DR   OrthoDB; EOG4N30PR; -.
DR   PhylomeDB; P63101; -.
DR   NextBio; 303003; -.
DR   ArrayExpress; P63101; -.
DR   Bgee; P63101; -.
DR   Genevestigator; P63101; -.
DR   GermOnline; ENSMUSG00000022285; Mus musculus.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; IDA:UniProtKB.
DR   InterPro; IPR000308; 14-3-3.
DR   PANTHER; PTHR18860; 14-3-3; 1.
DR   PIRSF; PIRSF000868; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Phosphoprotein.
FT   CHAIN         1    245       14-3-3 protein zeta/delta.
FT                                /FTId=PRO_0000058628.
FT   SITE         56     56       Interaction with phosphoserine on
FT                                interacting protein (By similarity).
FT   SITE        127    127       Interaction with phosphoserine on
FT                                interacting protein (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES       3      3       N6-acetyllysine (By similarity).
FT   MOD_RES      49     49       N6-acetyllysine (By similarity).
FT   MOD_RES      58     58       Phosphoserine; by PKA (By similarity).
FT   MOD_RES      68     68       N6-acetyllysine (By similarity).
FT   MOD_RES     115    115       N6-acetyllysine (By similarity).
FT   MOD_RES     120    120       N6-acetyllysine (By similarity).
FT   MOD_RES     184    184       Phosphoserine (By similarity).
FT   MOD_RES     207    207       Phosphoserine (By similarity).
FT   MOD_RES     210    210       Phosphoserine (By similarity).
FT   MOD_RES     232    232       Phosphothreonine; by CK1 (By similarity).
FT   CONFLICT     78     78       M -> V (in Ref. 4; BAA11751).
FT   CONFLICT    139    139       K -> R (in Ref. 5; BAE36724).
FT   CONFLICT    218    219       MQ -> IE (in Ref. 2; BAA13421).
FT   CONFLICT    236    236       E -> D (in Ref. 4; BAA11751).
SQ   SEQUENCE   245 AA;  27771 MW;  2164DF3793B45B7A CRC64;
     MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN VVGARRSSWR
     VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL LEKFLIPNAS QPESKVFYLK
     MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE
     ILNSPEKACS LAKTAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG
     EGGEN
//
ID   AAA1_MOUSE              Reviewed;         530 AA.
AC   P63115; Q9CW25; Q9JMH8;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Asc-type amino acid transporter 1;
DE            Short=Asc-1;
DE   AltName: Full=D-serine transporter;
DE   AltName: Full=Solute carrier family 7 member 10;
GN   Name=Slc7a10; Synonyms=Asc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=20200467; PubMed=10734121; DOI=10.1074/jbc.275.13.9690;
RA   Fukasawa Y., Segawa H., Kim J.Y., Chairoungdua A., Kim D.K.,
RA   Matsuo H., Cha S.H., Endou H., Kanai Y.;
RT   "Identification and characterization of a Na+-independent neutral
RT   amino acid transporter that associates with the 4F2 heavy chain and
RT   exhibits substrate selectivity for small neutral D- and L- amino
RT   acids.";
RL   J. Biol. Chem. 275:9690-9698(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 170-530.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Sodium-independent, high affinity transport of small
CC       neutral D- and L-amino acids and amino acid-related compounds. May
CC       play a role in the modulation of glutamatergic transmission
CC       through mobilization of D-serine at the glutamatergic synapse.
CC   -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid
CC       transport protein SLC3A2/4F2hc.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Probable).
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and lung, and to a
CC       lesser extent in placenta and small intestine.
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily.
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DR   EMBL; AB026688; BAA93617.1; -; mRNA.
DR   EMBL; BC054765; AAH54765.1; -; mRNA.
DR   EMBL; AK005282; BAB23930.1; -; mRNA.
DR   IPI; IPI00125687; -.
DR   RefSeq; NP_059090.3; NM_017394.4.
DR   UniGene; Mm.35567; -.
DR   ProteinModelPortal; P63115; -.
DR   STRING; P63115; -.
DR   TCDB; 2.A.3.8.13; amino acid-polyamine-organocation (APC) family.
DR   PRIDE; P63115; -.
DR   Ensembl; ENSMUST00000001854; ENSMUSP00000001854; ENSMUSG00000030495.
DR   GeneID; 53896; -.
DR   KEGG; mmu:53896; -.
DR   UCSC; uc009gjn.1; mouse.
DR   CTD; 53896; -.
DR   MGI; MGI:1858261; Slc7a10.
DR   eggNOG; roNOG10528; -.
DR   HOGENOM; HBG714539; -.
DR   HOVERGEN; HBG000476; -.
DR   InParanoid; P63115; -.
DR   OMA; EENGPCQ; -.
DR   OrthoDB; EOG4V437M; -.
DR   PhylomeDB; P63115; -.
DR   ArrayExpress; P63115; -.
DR   Bgee; P63115; -.
DR   Genevestigator; P63115; -.
DR   GermOnline; ENSMUSG00000030495; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; NAS:UniProtKB.
DR   GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0042941; P:D-alanine transport; IMP:MGI.
DR   GO; GO:0042942; P:D-serine transport; IMP:MGI.
DR   InterPro; IPR004841; AA-permease_dom.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   PANTHER; PTHR11785; AA/rel_permease1; 1.
DR   Pfam; PF00324; AA_permease; 1.
DR   PIRSF; PIRSF006060; AA_transporter; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Disulfide bond; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    530       Asc-type amino acid transporter 1.
FT                                /FTId=PRO_0000054277.
FT   TRANSMEM     46     66       Helical; (Potential).
FT   TRANSMEM     78     98       Helical; (Potential).
FT   TRANSMEM    119    139       Helical; (Potential).
FT   TRANSMEM    192    212       Helical; (Potential).
FT   TRANSMEM    274    294       Helical; (Potential).
FT   TRANSMEM    316    336       Helical; (Potential).
FT   TRANSMEM    368    388       Helical; (Potential).
FT   TRANSMEM    394    414       Helical; (Potential).
FT   TRANSMEM    430    450       Helical; (Potential).
FT   TRANSMEM    454    474       Helical; (Potential).
SQ   SEQUENCE   530 AA;  57549 MW;  0C5A80BF922DB54D CRC64;
     MRRDSDMASH IQQPGGHGNP GPAPSPSPGP GPGPGASERV ALKKEIGLVS ACTIIIGNII
     GSGIFISPKG VLEHSGSVGL ALFVWVLGGG VTALGSLCYA ELGVAIPKSG GDYAYVTEIF
     GGLAGFLLLW SAVLIMYPTS LAVISMTFSN YVLQPVFPNC IPPATASRVL SMACLMLLTW
     VNSSSVRWAT RIQVIFTGGK LLALSLIITV GFVQIFQGHF EELRPTNAFA FWMTPSVGHL
     ALAFLQGSFA FSGWNFLNYV TEELVDPRKN LPRAIFISIP LVTFVYTFTN VAYFTAMSPQ
     ELLSSNAVAV TFGEKLLGYF SWVMPVSVAL STFGGINGYL FTSSRLCFSG AREGHLPSFL
     AMIHVRRCTP IPALLVCCGA TAVIMLVGDT YTLINYVSFI NYLCYGVTIL GLLVLRWRRP
     ALHRPIKVNL LVPVVYLVFW AFLLVFSFIS EPMVCGVGII IILTGVPIFF LGVFWRSKPK
     CVHRFTESMT RWGQELCFVV YPQGSLEEEE NGPMGQPSPL PITDKPLKTQ
//
ID   GBRB2_MOUSE             Reviewed;         512 AA.
AC   P63137; A6H6R7; D1LYT3; P15432;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit beta-2;
DE   AltName: Full=GABA(A) receptor subunit beta-2;
DE   Flags: Precursor;
GN   Name=Gabrb2; Synonyms=Gabrb-2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J, and DBA/2J; TISSUE=Brain;
RX   MEDLINE=95200962; PubMed=7893750; DOI=10.1016/0167-4781(95)00009-6;
RA   Kamatchi G.L., Kofuji P., Wang J.B., Fernando J.C., Liu Z.,
RA   Mathura J.R., Burt D.R.;
RT   "GABAA receptor beta 1, beta 2, and beta 3 subunits: comparisons in
RT   DBA/2J and C57BL/6J mice.";
RL   Biochim. Biophys. Acta 1261:134-142(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=19763268; DOI=10.1371/journal.pone.0006977;
RA   Zhao C., Xu Z., Wang F., Chen J., Ng S.K., Wong P.W., Yu Z., Pun F.W.,
RA   Ren L., Lo W.S., Tsang S.Y., Xue H.;
RT   "Alternative-splicing in the exon-10 region of GABA(A) receptor
RT   beta(2) subunit gene: relationships between novel isoforms and
RT   psychotic disorders.";
RL   PLoS ONE 4:E6977-E6977(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-434 AND TYR-441, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [8]
RP   INTERACTION WITH KCTD8; KCTD12; KCTD12B AND KCTD16.
RX   PubMed=20400944; DOI=10.1038/nature08964;
RA   Schwenk J., Metz M., Zolles G., Turecek R., Fritzius T., Bildl W.,
RA   Tarusawa E., Kulik A., Unger A., Ivankova K., Seddik R., Tiao J.Y.,
RA   Rajalu M., Trojanova J., Rohde V., Gassmann M., Schulte U., Fakler B.,
RA   Bettler B.;
RT   "Native GABA(B) receptors are heteromultimers with a family of
RT   auxiliary subunits.";
RL   Nature 465:231-235(2010).
CC   -!- FUNCTION: GABA, the major inhibitory neurotransmitter in the
CC       vertebrate brain, mediates neuronal inhibition by binding to the
CC       GABA/benzodiazepine receptor and opening an integral chloride
CC       channel.
CC   -!- SUBUNIT: Generally pentameric. There are five types of GABA(A)
CC       receptor chains: alpha, beta, gamma, delta, and rho. Binds UBQLN1.
CC       Interacts with KCTD8, KCTD12, KCTD12B and KCTD16; this interaction
CC       determines the pharmacology and kinetics of the receptor response,
CC       the KCTD proteins markedly accelerating the GABA-B response,
CC       although to different extents.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane; Multi-pass membrane protein. Cell membrane; Multi-pass
CC       membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Long;
CC         IsoId=P63137-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short;
CC         IsoId=P63137-2; Sequence=VSP_038829;
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
CC       family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily.
CC       GABRB2 sub-subfamily.
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DR   EMBL; U14419; AAA79974.1; -; mRNA.
DR   EMBL; GU086167; ACY69098.1; -; mRNA.
DR   EMBL; AK090279; BAC41155.1; -; mRNA.
DR   EMBL; AL627444; CAI25055.1; -; Genomic_DNA.
DR   EMBL; AL645964; CAI25055.1; JOINED; Genomic_DNA.
DR   EMBL; AL645964; CAI25222.1; -; Genomic_DNA.
DR   EMBL; AL627444; CAI25222.1; JOINED; Genomic_DNA.
DR   EMBL; CH466609; EDL32344.1; -; Genomic_DNA.
DR   EMBL; BC145973; AAI45974.1; -; mRNA.
DR   EMBL; BC145975; AAI45976.1; -; mRNA.
DR   IPI; IPI00323554; -.
DR   IPI; IPI00955696; -.
DR   PIR; S53531; S53531.
DR   RefSeq; NP_032096.1; NM_008070.3.
DR   UniGene; Mm.338723; -.
DR   UniGene; Mm.471870; -.
DR   ProteinModelPortal; P63137; -.
DR   SMR; P63137; 59-330.
DR   STRING; P63137; -.
DR   PRIDE; P63137; -.
DR   Ensembl; ENSMUST00000007797; ENSMUSP00000007797; ENSMUSG00000007653.
DR   GeneID; 14401; -.
DR   KEGG; mmu:14401; -.
DR   UCSC; uc007imi.1; mouse.
DR   CTD; 14401; -.
DR   MGI; MGI:95620; Gabrb2.
DR   eggNOG; roNOG12839; -.
DR   HOGENOM; HBG506497; -.
DR   HOVERGEN; HBG051707; -.
DR   InParanoid; P63137; -.
DR   OMA; TSSIQYR; -.
DR   OrthoDB; EOG45756F; -.
DR   PhylomeDB; P63137; -.
DR   NextBio; 285949; -.
DR   ArrayExpress; P63137; -.
DR   Bgee; P63137; -.
DR   Genevestigator; P63137; -.
DR   GermOnline; ENSMUSG00000007653; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0004890; F:GABA-A receptor activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR006028; GABAA_rcpt.
DR   InterPro; IPR002289; GABAAb_rcpt.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   Gene3D; G3DSA:2.70.170.10; Neur_chan_lig_bd; 1.
DR   PANTHER; PTHR18945; Neur_channel; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR01160; GABAARBETA.
DR   PRINTS; PR00253; GABAARECEPTR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF90112; Neu_channel_TM; 1.
DR   SUPFAM; SSF63712; Neur_chan_LBD; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Chloride;
KW   Chloride channel; Disulfide bond; Glycoprotein; Ion transport;
KW   Ionic channel; Isopeptide bond; Ligand-gated ion channel; Membrane;
KW   Phosphoprotein; Postsynaptic cell membrane; Receptor; Signal; Synapse;
KW   Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT   SIGNAL        1     25       By similarity.
FT   CHAIN        26    512       Gamma-aminobutyric acid receptor subunit
FT                                beta-2.
FT                                /FTId=PRO_0000000460.
FT   TOPO_DOM     26    244       Extracellular (Probable).
FT   TRANSMEM    245    266       Helical; (Probable).
FT   TRANSMEM    270    292       Helical; (Probable).
FT   TRANSMEM    304    326       Helical; (Probable).
FT   TOPO_DOM    327    489       Cytoplasmic (Probable).
FT   TRANSMEM    490    511       Helical; (Probable).
FT   MOD_RES     434    434       Phosphotyrosine.
FT   MOD_RES     441    441       Phosphotyrosine.
FT   CARBOHYD     32     32       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    104    104       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    173    173       N-linked (GlcNAc...) (Potential).
FT   DISULFID    160    174       By similarity.
FT   CROSSLNK     45     45       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   VAR_SEQ     360    397       Missing (in isoform 2).
FT                                /FTId=VSP_038829.
SQ   SEQUENCE   512 AA;  59197 MW;  41AC9154A438E4FF CRC64;
     MWRVRKRGYF GIWSFPLIIA AVCAQSVNDP SNMSLVKETV DRLLKGYDIR LRPDFGGPPV
     AVGMNIDIAS IDMVSEVNMD YTLTMYFQQA WRDKRLSYNV IPLNLTLDNR VADQLWVPDT
     YFLNDKKSFV HGVTVKNRMI RLHPDGTVLY GLRITTTAAC MMDLRRYPLD EQNCTLEIES
     YGYTTDDIEF YWRGDDNAVT GVTKIELPQF SIVDYKLITK KVVFSTGSYP RLSLSFKLKR
     NIGYFILQTY MPSILITILS WVSFWINYDA SAARVALGIT TVLTMTTINT HLRETLPKIP
     YVKAIDMYLM GCFVFVFMAL LEYALVNYIF FGRGPQRQKK AAEKAANANN EKMRLDVNKM
     FYKDIKQNGT QYRSLWDPTG DLSPTRRTTN YDFSLYTMDP HENILLSTLE IKNEMATSEA
     VMGLGDPRST MLAYDASSIQ YRKAGLPRHS FGRNALERHV AQKKSRLRRR ASQLKITIPD
     LTDVNAIDRW SRIFFPVVFS FFNIVYWLYY VN
//
ID   KCNA2_MOUSE             Reviewed;         499 AA.
AC   P63141; P15386; Q02010; Q8C8W4;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Potassium voltage-gated channel subfamily A member 2;
DE   AltName: Full=MK2;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv1.2;
GN   Name=Kcna2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=90161996; PubMed=2305265; DOI=10.1126/science.2305265;
RA   Chandy K.G., Williams C.B., Spencer R.H., Aguilar B.A., Ghanshani S.,
RA   Tempel B.L., Gutman G.A.;
RT   "A family of three mouse potassium channel genes with intronless
RT   coding regions.";
RL   Science 247:973-975(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 338-394.
RX   PubMed=1691985; DOI=10.1016/0014-5793(90)80719-Y;
RA   Betsholtz C., Baumann A., Kenna S., Ashcroft F.M., Ashcroft S.J.H.,
RA   Berggren P.-O., Grupe A., Pongs O., Rorsman P., Sandblom J., Welsh M.;
RT   "Expression of voltage-gated K+ channels in insulin-producing cells.
RT   Analysis by polymerase chain reaction.";
RL   FEBS Lett. 263:121-126(1990).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=17925011; DOI=10.1186/1741-7007-5-42;
RA   Douglas C.L., Vyazovskiy V., Southard T., Chiu S.-Y., Messing A.,
RA   Tononi G., Cirelli C.;
RT   "Sleep in Kcna2 knockout mice.";
RL   BMC Biol. 5:42-42(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-429, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-421 AND THR-433, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Mediates the voltage-dependent potassium ion
CC       permeability of excitable membranes. Assuming opened or closed
CC       conformations in response to the voltage difference across the
CC       membrane, the protein forms a potassium-selective channel through
CC       which potassium ions may pass in accordance with their
CC       electrochemical gradient. Regulates neuronal excitability and is
CC       involved in non-rapid eye movement (NREM) sleep.
CC   -!- SUBUNIT: Heterotetramer of potassium channel proteins. Binds PDZ
CC       domains of DLG1, DLG2 and DLG4 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- DOMAIN: The N-terminus may be important in determining the rate of
CC       inactivation of the channel while the tail may play a role in
CC       modulation of channel activity and/or targeting of the channel to
CC       specific subcellular compartments.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position.
CC   -!- DISRUPTION PHENOTYPE: Death by P28 due to generalized seizures.
CC       Pups display less non-rapid eye movement (NREM) sleep and
CC       significantly more waking periods. Mice appear healthy and develop
CC       normally during the first 2 weeks, but die suddenly between around
CC       P12 and P28 due to an episode of generalized seizure, followed by
CC       full tonic extension, which in mice often results in fatal apne.
CC       At P17 seizures are either absent or very rare and abnormal
CC       electroencephalograph activity is only present during the seizure.
CC       P17 pups have significantly less non-rapid NREM sleep (-23%) and
CC       significantly more waking (+21%) than wild-type siblings with no
CC       change in rapid eye movement (REM) sleep time. The decrease in
CC       NREM sleep is due to an increase in the number of waking episodes,
CC       with no change in number or duration of sleep episodes.
CC   -!- SIMILARITY: Belongs to the potassium channel family. A (Shaker)
CC       (TC 1.A.1.2) subfamily. Kv1.2/KCNA2 sub-subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M30440; AAA39713.1; -; Genomic_DNA.
DR   EMBL; AK044342; BAC31877.1; -; mRNA.
DR   IPI; IPI00129774; -.
DR   PIR; B40090; I84204.
DR   RefSeq; NP_032443.3; NM_008417.4.
DR   UniGene; Mm.56930; -.
DR   ProteinModelPortal; P63141; -.
DR   SMR; P63141; 2-421.
DR   DIP; DIP-32239N; -.
DR   IntAct; P63141; 4.
DR   STRING; P63141; -.
DR   PRIDE; P63141; -.
DR   Ensembl; ENSMUST00000038695; ENSMUSP00000041702; ENSMUSG00000040724.
DR   GeneID; 16490; -.
DR   KEGG; mmu:16490; -.
DR   UCSC; uc008qws.1; mouse.
DR   CTD; 16490; -.
DR   MGI; MGI:96659; Kcna2.
DR   eggNOG; maNOG06054; -.
DR   GeneTree; ENSGT00560000076957; -.
DR   HOGENOM; HBG445693; -.
DR   HOVERGEN; HBG052230; -.
DR   InParanoid; P63141; -.
DR   OMA; MTFHTYS; -.
DR   OrthoDB; EOG4DR9CB; -.
DR   PhylomeDB; P63141; -.
DR   NextBio; 289787; -.
DR   ArrayExpress; P63141; -.
DR   Bgee; P63141; -.
DR   Genevestigator; P63141; -.
DR   GermOnline; ENSMUSG00000040724; Mus musculus.
DR   GO; GO:0044224; C:juxtaparanode region of axon; IDA:BHF-UCL.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:BHF-UCL.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003972; K_chnl_volt-dep_Kv1.
DR   InterPro; IPR004049; K_chnl_volt-dep_Kv1.2.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01509; KV12CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01496; SHAKERCHANEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Ion transport; Ionic channel; Lipoprotein; Membrane;
KW   Palmitate; Phosphoprotein; Potassium; Potassium channel;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN         1    499       Potassium voltage-gated channel subfamily
FT                                A member 2.
FT                                /FTId=PRO_0000053973.
FT   TRANSMEM    164    182       Helical; Name=Segment S1; (Potential).
FT   TRANSMEM    222    243       Helical; Name=Segment S2; (Potential).
FT   TRANSMEM    255    275       Helical; Name=Segment S3; (Potential).
FT   TRANSMEM    293    311       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TRANSMEM    328    347       Helical; Name=Segment S5; (Potential).
FT   TRANSMEM    389    411       Helical; Name=Segment S6; (Potential).
FT   MOTIF       374    379       Selectivity filter (By similarity).
FT   MOTIF       497    499       PDZ-binding (By similarity).
FT   MOD_RES     421    421       Phosphothreonine.
FT   MOD_RES     429    429       Phosphotyrosine.
FT   MOD_RES     433    433       Phosphothreonine.
FT   MOD_RES     449    449       Phosphoserine; by PKA (Potential).
FT   LIPID       244    244       S-palmitoyl cysteine (Potential).
FT   CARBOHYD     38     38       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    207    207       N-linked (GlcNAc...) (Potential).
FT   CONFLICT     33     33       E -> G (in Ref. 2; BAC31877).
SQ   SEQUENCE   499 AA;  56701 MW;  A8FEA6F3F59AF42A CRC64;
     MTVATGDPVD EAAALPGHPQ DTYDPEADHE CCERVVINIS GLRFETQLKT LAQFPETLLG
     DPKKRMRYFD PLRNEYFFDR NRPSFDAILY YYQSGGRLRR PVNVPLDIFS EEIRFYELGE
     EAMEMFREDE GYIKEEERPL PENEFQRQVW LLFEYPESSG PARIIAIVSV MVILISIVSF
     CLETLPIFRD ENEDMHGGGV TFHTYSNSTI GYQQSTSFTD PFFIVETLCI IWFSFEFLVR
     FFACPSKAGF FTNIMNIIDI VAIIPYFITL GTELAEKPED AQQGQQAMSL AILRVIRLVR
     VFRIFKLSRH SKGLQILGQT LKASMRELGL LIFFLFIGVI LFSSAVYFAE ADERDSQFPS
     IPDAFWWAVV SMTTVGYGDM VPTTIGGKIV GSLCAIAGVL TIALPVPVIV SNFNYFYHRE
     TEGEEQAQYL QVTSCPKIPS SPDLKKSRSA STISKSDYME IQEGVNNSNE DFREENLKTA
     NCTLANTNYV NITKMLTDV
//
ID   SUMO1_MOUSE             Reviewed;         101 AA.
AC   P63166; P55856; Q3TX92; Q93068;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Small ubiquitin-related modifier 1;
DE            Short=SUMO-1;
DE   AltName: Full=SMT3 homolog 3;
DE   AltName: Full=Ubiquitin-homology domain protein PIC1;
DE   AltName: Full=Ubiquitin-like protein SMT3C;
DE   Flags: Precursor;
GN   Name=Sumo1; Synonyms=Smt3c, Smt3h3, Ubl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR;
RX   MEDLINE=98126440; PubMed=9465300; DOI=10.1006/geno.1997.5091;
RA   Howe K., Williamson J., Boddy M.N., Sheer D., Freemont P.S.,
RA   Solomon E.;
RT   "The ubiquitin-homology gene PIC1: characterization of mouse (Pic1)
RT   and human (UBL1) genes and pseudogenes.";
RL   Genomics 47:92-100(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, Liver, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Colon, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH HIF1A.
RX   PubMed=15225651; DOI=10.1016/j.febslet.2004.05.079;
RA   Shao R., Zhang F.-P., Tian F., Anders Friberg P., Wang X.,
RA   Sjoeland H., Billig H.;
RT   "Increase of SUMO-1 expression in response to hypoxia: direct
RT   interaction with HIF-1alpha in adult mouse brain and heart in vivo.";
RL   FEBS Lett. 569:293-300(2004).
RN   [5]
RP   INTERACTION WITH IKFZ1.
RX   PubMed=15767674; DOI=10.1128/MCB.25.7.2688-2697.2005;
RA   Gomez-del Arco P., Koipally J., Georgopoulos K.;
RT   "Ikaros SUMOylation: switching out of repression.";
RL   Mol. Cell. Biol. 25:2688-2697(2005).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18681895; DOI=10.1111/j.1365-2443.2008.01216.x;
RA   Kuwata T., Nakamura T.;
RT   "BCL11A is a SUMOylated protein and recruits SUMO-conjugation enzymes
RT   in its nuclear body.";
RL   Genes Cells 13:931-940(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Ubiquitin-like protein that can be covalently attached
CC       to proteins as a monomer or a lysine-linked polymer. Covalent
CC       attachment via an isopeptide bond to its substrates requires prior
CC       activation by the E1 complex SAE1-SAE2 and linkage to the E2
CC       enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4,
CC       RANBP2 or CBX4. This post-translational modification on lysine
CC       residues of proteins plays a crucial role in a number of cellular
CC       processes such as nuclear transport, DNA replication and repair,
CC       mitosis and signal transduction. Involved for instance in
CC       targeting RANGAP1 to the nuclear pore complex protein RANBP2.
CC       Polymeric SUMO1 chains are also susceptible to polyubiquitination
CC       which functions as a signal for proteasomal degradation of
CC       modified proteins.
CC   -!- SUBUNIT: Interacts with USP25 (via ts SIM domain) the interaction
CC       weakly sumoylates USP25 (By similarity). Interacts with SAE2,
CC       UBE2I, RANBP2, PIAS1 and PIAS2. Interacts with PARK2. Covalently
CC       attached to a number of proteins such as IKFZ1, PML, RANGAP1,
CC       HIPK2, SP100, p53, p73-alpha, MDM2, JUN, DNMT3B and TDG. Also
CC       interacts with HIF1A, HIPK2, HIPK3, CHD3, EXOSC9, RAD51 and RAD52.
CC   -!- INTERACTION:
CC       Q61221:Hif1a; NbExp=2; IntAct=EBI-80152, EBI-298954;
CC       Q03267:Ikzf1; NbExp=1; IntAct=EBI-80152, EBI-908572;
CC       P18031:PTPN1 (xeno); NbExp=1; IntAct=EBI-80152, EBI-968788;
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane. Nucleus speckle.
CC       Cytoplasm. Note=Recruited by BCL11A into the nuclear body.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- INDUCTION: By hypoxia.
CC   -!- PTM: Cleavage of precursor form by SENP1 or SENP2 is necessary for
CC       function (By similarity).
CC   -!- PTM: Polymeric SUMO1 chains undergo polyubiquitination by RNF4 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily.
CC   -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF033353; AAC39959.1; -; mRNA.
DR   EMBL; AK002536; BAB22172.1; -; mRNA.
DR   EMBL; AK011074; BAB27379.1; -; mRNA.
DR   EMBL; AK089081; BAC40739.1; -; mRNA.
DR   EMBL; AK159366; BAE35024.1; -; mRNA.
DR   EMBL; BC082566; AAH82566.1; -; mRNA.
DR   EMBL; BC083158; AAH83158.1; -; mRNA.
DR   IPI; IPI00124593; -.
DR   RefSeq; NP_033486.1; NM_009460.2.
DR   UniGene; Mm.362118; -.
DR   ProteinModelPortal; P63166; -.
DR   SMR; P63166; 1-101.
DR   DIP; DIP-29278N; -.
DR   IntAct; P63166; 13.
DR   MINT; MINT-154756; -.
DR   STRING; P63166; -.
DR   PhosphoSite; P63166; -.
DR   PRIDE; P63166; -.
DR   Ensembl; ENSMUST00000091374; ENSMUSP00000088935; ENSMUSG00000026021.
DR   GeneID; 22218; -.
DR   KEGG; mmu:22218; -.
DR   UCSC; uc007bdx.1; mouse.
DR   CTD; 22218; -.
DR   MGI; MGI:1197010; Sumo1.
DR   eggNOG; maNOG20287; -.
DR   GeneTree; ENSGT00390000018808; -.
DR   HOGENOM; HBG436396; -.
DR   HOVERGEN; HBG053025; -.
DR   InParanoid; P63166; -.
DR   OrthoDB; EOG42JNSX; -.
DR   PhylomeDB; P63166; -.
DR   NextBio; 302229; -.
DR   ArrayExpress; P63166; -.
DR   Bgee; P63166; -.
DR   CleanEx; MM_SUMO1; -.
DR   Genevestigator; P63166; -.
DR   GermOnline; ENSMUSG00000026021; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0016605; C:PML body; TAS:MGI.
DR   GO; GO:0019789; F:SUMO ligase activity; IDA:MGI.
DR   GO; GO:0008134; F:transcription factor binding; IPI:MGI.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:UniProtKB.
DR   GO; GO:0016925; P:protein sumoylation; ISS:UniProtKB.
DR   GO; GO:0045449; P:regulation of transcription; IDA:MGI.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   InterPro; IPR000626; Ubiquitin.
DR   InterPro; IPR019955; Ubiquitin_supergroup.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SMART; SM00213; UBQ; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Isopeptide bond; Membrane; Nucleus;
KW   Phosphoprotein; Stress response; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2     97       Small ubiquitin-related modifier 1.
FT                                /FTId=PRO_0000035941.
FT   PROPEP       98    101       By similarity.
FT                                /FTId=PRO_0000035942.
FT   DOMAIN       20     97       Ubiquitin-like.
FT   SITE         36     36       Interaction with PIAS2 (By similarity).
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES       2      2       Phosphoserine.
FT   MOD_RES       9      9       Phosphoserine (By similarity).
FT   CROSSLNK      7      7       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO-1) (By
FT                                similarity).
FT   CROSSLNK     25     25       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO-1) (By
FT                                similarity).
FT   CROSSLNK     97     97       Glycyl lysine isopeptide (Gly-Lys)
FT                                (interchain with K-? in acceptor
FT                                proteins).
SQ   SEQUENCE   101 AA;  11557 MW;  89BE97D2D054FB33 CRC64;
     MSDQEAKPST EDLGDKKEGE YIKLKVIGQD SSEIHFKVKM TTHLKKLKES YCQRQGVPMN
     SLRFLFEGQR IADNHTPKEL GMEEEDVIEV YQEQTGGHST V
//
ID   GBG2_MOUSE              Reviewed;          71 AA.
AC   P63213; P16874; Q3TYE8; Q61013; Q9TS47;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2;
DE   AltName: Full=G gamma-I;
DE   Flags: Precursor;
GN   Name=Gng2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=99208677; PubMed=10191100; DOI=10.1006/geno.1999.5763;
RA   Downes G.B., Gilbert D.J., Copeland N.G., Gautam N., Jenkins N.A.;
RT   "Chromosomal mapping of five mouse G protein gamma subunits.";
RL   Genomics 57:173-176(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 18-52.
RC   STRAIN=CF-1 / Harlan; TISSUE=Embryo;
RX   MEDLINE=97011591; PubMed=8858601;
RX   DOI=10.1002/(SICI)1098-2795(199607)44:3<315::AID-MRD5>3.3.CO;2-V;
RA   Williams C.J., Schultz R.M., Kopf G.S.;
RT   "G protein gene expression during mouse oocyte growth and maturation,
RT   and preimplantation embryo development.";
RL   Mol. Reprod. Dev. 44:315-323(1996).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-52, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC       involved as a modulator or transducer in various transmembrane
CC       signaling systems. The beta and gamma chains are required for the
CC       GTPase activity, for replacement of GDP by GTP, and for G protein-
CC       effector interaction.
CC   -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and
CC       gamma.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- TISSUE SPECIFICITY: Adrenal gland and brain.
CC   -!- SIMILARITY: Belongs to the G protein gamma family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF098489; AAD16272.1; -; Genomic_DNA.
DR   EMBL; AF098488; AAD16272.1; JOINED; Genomic_DNA.
DR   EMBL; AK003588; BAB22878.1; -; mRNA.
DR   EMBL; AK012405; BAB28219.1; -; mRNA.
DR   EMBL; AK036138; BAC29316.1; -; mRNA.
DR   EMBL; AK075698; BAC35896.1; -; mRNA.
DR   EMBL; AK158697; BAE34615.1; -; mRNA.
DR   EMBL; AK160396; BAE35765.1; -; mRNA.
DR   EMBL; BC021599; AAH21599.1; -; mRNA.
DR   EMBL; U38496; AAB01727.1; -; mRNA.
DR   IPI; IPI00230194; -.
DR   PIR; D36204; D36204.
DR   RefSeq; NP_001033726.1; NM_001038637.1.
DR   RefSeq; NP_034445.1; NM_010315.4.
DR   UniGene; Mm.41737; -.
DR   ProteinModelPortal; P63213; -.
DR   SMR; P63213; 8-67.
DR   STRING; P63213; -.
DR   PhosphoSite; P63213; -.
DR   PRIDE; P63213; -.
DR   Ensembl; ENSMUST00000055100; ENSMUSP00000055256; ENSMUSG00000043004.
DR   GeneID; 14702; -.
DR   KEGG; mmu:14702; -.
DR   UCSC; uc007siw.1; mouse.
DR   CTD; 14702; -.
DR   MGI; MGI:102705; Gng2.
DR   eggNOG; roNOG17390; -.
DR   GeneTree; ENSGT00550000074352; -.
DR   HOGENOM; HBG444905; -.
DR   HOVERGEN; HBG014983; -.
DR   InParanoid; P63213; -.
DR   OMA; SYCEAHA; -.
DR   OrthoDB; EOG47WNQC; -.
DR   PhylomeDB; P63213; -.
DR   NextBio; 286671; -.
DR   ArrayExpress; P63213; -.
DR   Bgee; P63213; -.
DR   Genevestigator; P63213; -.
DR   GermOnline; ENSMUSG00000043004; Mus musculus.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0008283; P:cell proliferation; IDA:MGI.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; IDA:MGI.
DR   InterPro; IPR015898; G-protein_gamma_dom.
DR   InterPro; IPR001770; Gprotein-gamma.
DR   Gene3D; G3DSA:4.10.260.10; G-protein_gamma_dom; 1.
DR   PANTHER; PTHR13809; Gprotein-gamma; 1.
DR   Pfam; PF00631; G-gamma; 1.
DR   PRINTS; PR00321; GPROTEING.
DR   SMART; SM00224; GGL; 1.
DR   SUPFAM; SSF48670; G-protein_gamma-like; 1.
DR   PROSITE; PS50058; G_PROTEIN_GAMMA; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Lipoprotein; Membrane; Methylation;
KW   Phosphoprotein; Prenylation; Transducer.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2     68       Guanine nucleotide-binding protein
FT                                G(I)/G(S)/G(O) subunit gamma-2.
FT                                /FTId=PRO_0000012613.
FT   PROPEP       69     71       Removed in mature form.
FT                                /FTId=PRO_0000012614.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      52     52       Phosphothreonine.
FT   MOD_RES      68     68       Cysteine methyl ester (By similarity).
FT   LIPID        68     68       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   71 AA;  7850 MW;  EDB74E4135E7A37A CRC64;
     MASNNTASIA QARKLVEQLK MEANIDRIKV SKAAADLMAY CEAHAKEDPL LTPVPASENP
     FREKKFFCAI L
//
ID   GBG3_MOUSE              Reviewed;          75 AA.
AC   P63216; P29798; Q61014;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3;
DE   Flags: Precursor;
GN   Name=Gng3; Synonyms=Gngt3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=96067541; PubMed=7488078; DOI=10.1006/bbrc.1995.2600;
RA   Kalyanaraman S., Kalyanaraman V., Gautam N.;
RT   "A brain-specific G protein gamma subunit.";
RL   Biochem. Biophys. Res. Commun. 216:126-132(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=99009337; PubMed=9790771; DOI=10.1006/geno.1998.5508;
RA   Downes G.B., Copeland N.G., Jenkins N.A., Gautam N.;
RT   "Structure and mapping of the G protein gamma3 subunit gene and a
RT   divergently transcribed novel gene, Gng3lg.";
RL   Genomics 53:220-230(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 1-17 AND 25-31, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 13-68.
RC   STRAIN=CF-1 / Harlan;
RX   MEDLINE=97011591; PubMed=8858601;
RX   DOI=10.1002/(SICI)1098-2795(199607)44:3<315::AID-MRD5>3.3.CO;2-V;
RA   Williams C.J., Schultz R.M., Kopf G.S.;
RT   "G protein gene expression during mouse oocyte growth and maturation,
RT   and preimplantation embryo development.";
RL   Mol. Reprod. Dev. 44:315-323(1996).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5 AND SER-9, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC       involved as a modulator or transducer in various transmembrane
CC       signaling systems. The beta and gamma chains are required for the
CC       GTPase activity, for replacement of GDP by GTP, and for G protein-
CC       effector interaction.
CC   -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and
CC       gamma.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in brain. Low levels in
CC       testis.
CC   -!- SIMILARITY: Belongs to the G protein gamma family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF069953; AAC83941.1; -; Genomic_DNA.
DR   EMBL; AK004459; BAB23313.1; -; mRNA.
DR   EMBL; AK032646; BAC27969.1; -; mRNA.
DR   EMBL; BC029680; AAH29680.1; -; mRNA.
DR   EMBL; U38497; AAB01728.1; -; mRNA.
DR   IPI; IPI00129268; -.
DR   PIR; JC4340; JC4340.
DR   RefSeq; NP_034446.1; NM_010316.3.
DR   UniGene; Mm.329700; -.
DR   ProteinModelPortal; P63216; -.
DR   SMR; P63216; 12-71.
DR   STRING; P63216; -.
DR   PhosphoSite; P63216; -.
DR   PRIDE; P63216; -.
DR   Ensembl; ENSMUST00000096259; ENSMUSP00000093978; ENSMUSG00000071658.
DR   GeneID; 14704; -.
DR   KEGG; mmu:14704; -.
DR   UCSC; uc008gnh.1; mouse.
DR   CTD; 14704; -.
DR   MGI; MGI:102704; Gng3.
DR   eggNOG; maNOG21025; -.
DR   GeneTree; ENSGT00550000074352; -.
DR   HOGENOM; HBG444905; -.
DR   HOVERGEN; HBG014983; -.
DR   InParanoid; P63216; -.
DR   OMA; EASMCRI; -.
DR   OrthoDB; EOG47WNQC; -.
DR   PhylomeDB; P63216; -.
DR   NextBio; 286679; -.
DR   ArrayExpress; P63216; -.
DR   Bgee; P63216; -.
DR   Genevestigator; P63216; -.
DR   GermOnline; ENSMUSG00000071658; Mus musculus.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   InterPro; IPR015898; G-protein_gamma_dom.
DR   InterPro; IPR001770; Gprotein-gamma.
DR   Gene3D; G3DSA:4.10.260.10; G-protein_gamma_dom; 1.
DR   PANTHER; PTHR13809; Gprotein-gamma; 1.
DR   Pfam; PF00631; G-gamma; 1.
DR   PRINTS; PR00321; GPROTEING.
DR   SMART; SM00224; GGL; 1.
DR   SUPFAM; SSF48670; G-protein_gamma-like; 1.
DR   PROSITE; PS50058; G_PROTEIN_GAMMA; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Lipoprotein; Membrane;
KW   Methylation; Phosphoprotein; Prenylation; Transducer.
FT   CHAIN         1     72       Guanine nucleotide-binding protein
FT                                G(I)/G(S)/G(O) subunit gamma-3.
FT                                /FTId=PRO_0000012619.
FT   PROPEP       73     75       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000012620.
FT   MOD_RES       5      5       Phosphothreonine.
FT   MOD_RES       9      9       Phosphoserine.
FT   MOD_RES      72     72       Cysteine methyl ester (By similarity).
FT   LIPID        72     72       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   75 AA;  8305 MW;  35CC03965FE69A9D CRC64;
     MKGETPVNST MSIGQARKMV EQLKIEASLC RIKVSKAAAD LMTYCDAHAC EDPLITPVPT
     SENPFREKKF FCALL
//
ID   IRK3_MOUSE              Reviewed;         501 AA.
AC   P63250; P35562;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=G protein-activated inward rectifier potassium channel 1;
DE            Short=GIRK-1;
DE   AltName: Full=Inward rectifier K(+) channel Kir3.1;
DE   AltName: Full=Potassium channel, inwardly rectifying subfamily J member 3;
GN   Name=Kcnj3; Synonyms=Girk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=95217202; PubMed=7702616; DOI=10.1006/bbrc.1995.1456;
RA   Kobayashi T., Ikeda K., Ichikawa T., Abe S., Togashi S., Kumanishi T.;
RT   "Molecular cloning of a mouse G-protein-activated K+ channel (mGIRK1)
RT   and distinct distributions of three GIRK (GIRK1, 2 and 3) mRNAs in
RT   mouse brain.";
RL   Biochem. Biophys. Res. Commun. 208:1166-1173(1995).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 43-63 AND 190-370.
RX   PubMed=12507423; DOI=10.1016/S0092-8674(02)01227-8;
RA   Nishida M., MacKinnon R.;
RT   "Structural basis of inward rectification: cytoplasmic pore of the G
RT   protein-gated inward rectifier GIRK1 at 1.8 A resolution.";
RL   Cell 111:957-965(2002).
CC   -!- FUNCTION: This potassium channel is controlled by G proteins.
CC       Inward rectifier potassium channels are characterized by a greater
CC       tendency to allow potassium to flow into the cell rather than out
CC       of it. Their voltage dependence is regulated by the concentration
CC       of extracellular potassium; as external potassium is raised, the
CC       voltage range of the channel opening shifts to more positive
CC       voltages. The inward rectification is mainly due to the blockage
CC       of outward current by internal magnesium. This receptor plays a
CC       crucial role in regulating the heartbeat.
CC   -!- SUBUNIT: Associates with GIRK2, GIRK3 or GIRK4 to form a G-protein
CC       activated heteromultimer pore-forming unit. The resulting inward
CC       current is much larger (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
CC       (TC 1.A.2.1) family. KCNJ3 subfamily.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; D45022; BAA08079.1; -; mRNA.
DR   IPI; IPI00119615; -.
DR   PIR; JC4139; JC4139.
DR   RefSeq; NP_032452.1; NM_008426.1.
DR   UniGene; Mm.5127; -.
DR   PDB; 1N9P; X-ray; 1.80 A; A=41-371.
DR   PDB; 1U4E; X-ray; 2.09 A; A=41-371.
DR   PDB; 2QKS; X-ray; 2.20 A; A/B=41-371.
DR   PDB; 3K6N; X-ray; 2.00 A; A=41-371.
DR   PDBsum; 1N9P; -.
DR   PDBsum; 1U4E; -.
DR   PDBsum; 2QKS; -.
DR   PDBsum; 3K6N; -.
DR   ProteinModelPortal; P63250; -.
DR   SMR; P63250; 41-370.
DR   DIP; DIP-48585N; -.
DR   STRING; P63250; -.
DR   PRIDE; P63250; -.
DR   Ensembl; ENSMUST00000067101; ENSMUSP00000063329; ENSMUSG00000026824.
DR   Ensembl; ENSMUST00000112633; ENSMUSP00000108252; ENSMUSG00000026824.
DR   GeneID; 16519; -.
DR   KEGG; mmu:16519; -.
DR   UCSC; uc008jru.1; mouse.
DR   CTD; 16519; -.
DR   MGI; MGI:104742; Kcnj3.
DR   eggNOG; roNOG12417; -.
DR   HOGENOM; HBG716702; -.
DR   HOVERGEN; HBG006178; -.
DR   InParanoid; P63250; -.
DR   OMA; SMQSEQF; -.
DR   OrthoDB; EOG4GXFMM; -.
DR   PhylomeDB; P63250; -.
DR   NextBio; 289889; -.
DR   ArrayExpress; P63250; -.
DR   Bgee; P63250; -.
DR   Genevestigator; P63250; -.
DR   GermOnline; ENSMUSG00000026824; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015467; F:G-protein activated inward rectifier potassium channel activity; TAS:MGI.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR016449; K_chnl_inward-rec_Kir.
DR   InterPro; IPR001838; K_chnl_inward-rec_Kir-like.
DR   InterPro; IPR003274; K_chnl_inward-rec_Kir3.1.
DR   InterPro; IPR013521; K_chnl_inward-rec_Kir_Cr2.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   Gene3D; G3DSA:2.60.40.1400; IR_K+channel_cytopl; 1.
DR   PANTHER; PTHR11767; K+channel_IR; 1.
DR   Pfam; PF01007; IRK; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01327; KIR31CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; Ig_E-set; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Ion transport; Ionic channel; Membrane; Phosphoprotein;
KW   Potassium; Potassium transport; Transmembrane; Transmembrane helix;
KW   Transport; Voltage-gated channel.
FT   CHAIN         1    501       G protein-activated inward rectifier
FT                                potassium channel 1.
FT                                /FTId=PRO_0000154939.
FT   TOPO_DOM      1     80       Cytoplasmic.
FT   TRANSMEM     81    105       Helical; Name=M1; (By similarity).
FT   TOPO_DOM    106    129       Extracellular (By similarity).
FT   INTRAMEM    130    141       Helical; Pore-forming; Name=H5; (By
FT                                similarity).
FT   INTRAMEM    142    148       Pore-forming; (By similarity).
FT   TOPO_DOM    149    157       Extracellular (By similarity).
FT   TRANSMEM    158    179       Helical; Name=M2; (By similarity).
FT   TOPO_DOM    180    501       Cytoplasmic.
FT   MOTIF       143    148       Selectivity filter (By similarity).
FT   SITE        173    173       Role in the control of polyamine-mediated
FT                                channel gating and in the blocking by
FT                                intracellular magnesium (By similarity).
FT   MOD_RES      69     69       Phosphoserine (By similarity).
FT   MOD_RES      73     73       Phosphothreonine (By similarity).
FT   HELIX        69     77
FT   HELIX        80    108
FT   STRAND      113    115
FT   TURN        123    129
FT   HELIX       130    141
FT   HELIX       159    171
FT   STRAND      180    183
FT   STRAND      194    196
FT   STRAND      200    205
FT   STRAND      208    215
FT   STRAND      219    221
FT   STRAND      223    237
FT   STRAND      243    250
FT   TURN        255    257
FT   STRAND      261    263
FT   STRAND      268    273
FT   TURN        279    282
FT   HELIX       287    289
FT   STRAND      294    303
FT   TURN        304    306
FT   STRAND      312    317
FT   HELIX       318    320
FT   STRAND      321    323
FT   STRAND      325    327
FT   STRAND      331    336
FT   STRAND      338    340
FT   HELIX       342    344
FT   STRAND      348    350
FT   HELIX       358    368
SQ   SEQUENCE   501 AA;  56573 MW;  AB8910E9CC08FFEC CRC64;
     MSALRRKFGD DYQVVTTSSS GSGLQPQGPG QGPQQQLVPK KKRQRFVDKN GRCNVQHGNL
     GSETSRYLSD LFTTLVDLKW RWNLFIFILT YTVAWLFMAS MWWVIAYTRG DLNKAHVGNY
     TPCVANVYNF PSAFLFFIET EATIGYGYRY ITDKCPEGII LFLFQSILGS IVDAFLIGCM
     FIKMSQPKKR AETLMFSEHA VISMRDGKLT LMFRVGNLRN SHMVSAQIRC KLLKSRQTPE
     GEFLPLDQLE LDVGFSTGAD QLFLVSPLTI CHVIDAKSPF YDLSQRSMQT EQFEVVVILE
     GIVETTGMTC QARTSYTEDE VLWGHRFFPV ISLEEGFFKV DYSQFHATFE VPTPPYSVKE
     QEEMLLMSSP LIAPAITNSK ERHNSVECLD GLDDISTKLP SKLQKITGRE DFPKKLLRMS
     STTSEKAYSL GDLPMKLQRI SSVPGNSEEK LVSKTTKMLS DPMSQSVADL PPKLQKMAGG
     PTRMEGNLPA KLRKMNSDRF T
//
ID   ACTG_MOUSE              Reviewed;         375 AA.
AC   P63260; P02571; P14104; P99022;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Actin, cytoplasmic 2;
DE   AltName: Full=Gamma-actin;
DE   Contains:
DE     RecName: Full=Actin, cytoplasmic 2, N-terminally processed;
GN   Name=Actg1; Synonyms=Actg;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-375, AND METHYLATION AT HIS-73.
RX   MEDLINE=79045349; PubMed=213279;
RX   DOI=10.1111/j.1432-1033.1978.tb12624.x;
RA   Vandekerckhove J., Weber K.;
RT   "Actin amino-acid sequences. Comparison of actins from calf thymus,
RT   bovine brain, and SV40-transformed mouse 3T3 cells with rabbit
RT   skeletal muscle actin.";
RL   Eur. J. Biochem. 90:451-462(1978).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=89127235; PubMed=3221869;
RA   Tokunaga K., Takeda K., Kamiyama K., Kageyama H., Takenaga K.,
RA   Sakiyama S.;
RT   "Isolation of cDNA clones for mouse cytoskeletal gamma-actin and
RT   differential expression of cytoskeletal actin mRNAs in mouse cells.";
RL   Mol. Cell. Biol. 8:3929-3933(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N, and NMRI; TISSUE=Colon, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-375.
RX   MEDLINE=89094834; PubMed=3210229; DOI=10.1016/0022-2836(88)90200-8;
RA   Peter B., Man Y.M., Begg C.E., Gall I., Leader D.P.;
RT   "Mouse cytoskeletal gamma-actin: analysis and implications of the
RT   structure of cloned cDNA and processed pseudogenes.";
RL   J. Mol. Biol. 203:665-675(1988).
RN   [6]
RP   PROTEIN SEQUENCE OF 29-39.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-169, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others.
CC   -!- INTERACTION:
CC       Q08460:Kcnma1; NbExp=1; IntAct=EBI-351301, EBI-1633915;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC       alpha, beta and gamma have been identified. The alpha actins are
CC       found in muscle tissues and are a major constituent of the
CC       contractile apparatus. The beta and gamma actins coexist in most
CC       cell types as components of the cytoskeleton and as mediators of
CC       internal cell motility.
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X13055; CAA31455.1; -; mRNA.
DR   EMBL; AK076081; BAC36167.1; -; mRNA.
DR   EMBL; AK087983; BAC40075.1; -; mRNA.
DR   EMBL; BC003337; AAH03337.1; -; mRNA.
DR   EMBL; BC021796; AAH21796.1; -; mRNA.
DR   EMBL; BC023248; AAH23248.1; -; mRNA.
DR   EMBL; M21495; AAA37168.1; -; mRNA.
DR   IPI; IPI00874482; -.
DR   PIR; A30243; ATMSG.
DR   RefSeq; NP_033739.1; NM_009609.2.
DR   UniGene; Mm.196173; -.
DR   UniGene; Mm.426706; -.
DR   ProteinModelPortal; P63260; -.
DR   SMR; P63260; 2-375.
DR   IntAct; P63260; 26.
DR   STRING; P63260; -.
DR   COMPLUYEAST-2DPAGE; P63260; -.
DR   REPRODUCTION-2DPAGE; P63260; -.
DR   UCD-2DPAGE; P63260; -.
DR   PRIDE; P63260; -.
DR   Ensembl; ENSMUST00000071555; ENSMUSP00000071486; ENSMUSG00000062825.
DR   GeneID; 11465; -.
DR   KEGG; mmu:11465; -.
DR   UCSC; uc007msi.1; mouse.
DR   CTD; 11465; -.
DR   MGI; MGI:87906; Actg1.
DR   HOVERGEN; HBG003771; -.
DR   OrthoDB; EOG41JZC9; -.
DR   PhylomeDB; P63260; -.
DR   NextBio; 278792; -.
DR   PMAP-CutDB; P63260; -.
DR   ArrayExpress; P63260; -.
DR   Bgee; P63260; -.
DR   CleanEx; MM_ACTG1; -.
DR   Genevestigator; P63260; -.
DR   GermOnline; ENSMUSG00000062825; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   InterPro; IPR004000; Actin-like.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Methylation; Nucleotide-binding;
KW   Phosphoprotein.
FT   CHAIN         1    375       Actin, cytoplasmic 2.
FT                                /FTId=PRO_0000367101.
FT   INIT_MET      1      1       Removed; alternate.
FT   CHAIN         2    375       Actin, cytoplasmic 2, N-terminally
FT                                processed.
FT                                /FTId=PRO_0000000833.
FT   MOD_RES       1      1       N-acetylmethionine; in Actin, cytoplasmic
FT                                2; alternate.
FT   MOD_RES       2      2       N-acetylglutamate; in Actin, cytoplasmic
FT                                2, N-terminally processed.
FT   MOD_RES      73     73       Tele-methylhistidine.
FT   MOD_RES     169    169       Phosphotyrosine.
FT   MOD_RES     198    198       Phosphotyrosine (By similarity).
FT   MOD_RES     294    294       Phosphotyrosine (By similarity).
FT   MOD_RES     318    318       Phosphothreonine (By similarity).
SQ   SEQUENCE   375 AA;  41793 MW;  54D08F986964EFD5 CRC64;
     MEEEIAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
     KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
     QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL
     AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY
     ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS
     GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
     EYDESGPSIV HRKCF
//
ID   ACTH_MOUSE              Reviewed;         376 AA.
AC   P63268; P12718;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Actin, gamma-enteric smooth muscle;
DE   AltName: Full=Alpha-actin-3;
DE   AltName: Full=Gamma-2-actin;
DE   AltName: Full=Smooth muscle gamma-actin;
GN   Name=Actg2; Synonyms=Acta3, Actsg;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=89313731; PubMed=2747639;
RA   Kim E., Waters S.H., Hake L.E., Hecht N.B.;
RT   "Identification and developmental expression of a smooth-muscle gamma-
RT   actin in postmeiotic male germ cells of mice.";
RL   Mol. Cell. Biol. 9:1875-1881(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC       alpha, beta and gamma have been identified. The alpha actins are
CC       found in muscle tissues and are a major constituent of the
CC       contractile apparatus. The beta and gamma actins coexist in most
CC       cell types as components of the cytoskeleton and as mediators of
CC       internal cell motility.
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M26689; AAA56841.1; -; mRNA.
DR   EMBL; BC002042; AAH02042.1; -; mRNA.
DR   IPI; IPI00404804; -.
DR   PIR; A32788; A32788.
DR   RefSeq; NP_033740.2; NM_009610.2.
DR   UniGene; Mm.292865; -.
DR   ProteinModelPortal; P63268; -.
DR   SMR; P63268; 5-376.
DR   STRING; P63268; -.
DR   PRIDE; P63268; -.
DR   Ensembl; ENSMUST00000075161; ENSMUSP00000074658; ENSMUSG00000059430.
DR   Ensembl; ENSMUST00000121731; ENSMUSP00000113552; ENSMUSG00000059430.
DR   GeneID; 11468; -.
DR   KEGG; mmu:11468; -.
DR   CTD; 11468; -.
DR   MGI; MGI:104589; Actg2.
DR   eggNOG; maNOG22495; -.
DR   HOGENOM; HBG559892; -.
DR   HOVERGEN; HBG003771; -.
DR   InParanoid; P63268; -.
DR   OMA; NQIWHHS; -.
DR   OrthoDB; EOG4W9J40; -.
DR   PhylomeDB; P63268; -.
DR   NextBio; 278796; -.
DR   ArrayExpress; P63268; -.
DR   Bgee; P63268; -.
DR   CleanEx; MM_ACTG2; -.
DR   Genevestigator; P63268; -.
DR   GermOnline; ENSMUSG00000059430; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004000; Actin-like.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Muscle protein;
KW   Nucleotide-binding.
FT   PROPEP        1      2       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000000750.
FT   CHAIN         3    376       Actin, gamma-enteric smooth muscle.
FT                                /FTId=PRO_0000000751.
FT   MOD_RES       3      3       N-acetylglutamate (By similarity).
SQ   SEQUENCE   376 AA;  41877 MW;  6EC08CD5EEAD445E CRC64;
     MCEEETTALV CDNGSGLCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ
     SKRGILTLKY PIEHGIITNW DDMEKIWHHS FYNELRVAPE EHPTLLTEAP LNPKANREKM
     TQIMFETFNV PAMYVAIQAV LSLYASGRTT GIVLDSGDGV THNVPIYEGY ALPHAIMRLD
     LAGRDLTDYL MKILTERGYS FVTTAEREIV RDIKEKLCYV ALDFENEMAT AASSSSLEKS
     YELPDGQVIT IGNERFRCPE TLFQPSFIGM ESAGIHETTY NSIMKCDIDI RKDLYANNVL
     SGGTTMYPGI ADRMQKEITA LAPSTMKIKI IAPPERKYSV WIGGSILASL STFQQMWISK
     PEYDEAGPSI VHRKCF
//
ID   RS17_MOUSE              Reviewed;         135 AA.
AC   P63276; P06584;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=40S ribosomal protein S17;
GN   Name=Rps17;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ddY;
RX   MEDLINE=95267035; PubMed=7748157; DOI=10.1007/BF00566061;
RA   Karasaki Y., Satoh Y., Ohji T., Tsukamoto S., Higashi K., Gotoh S.,
RA   Mizusaki K.;
RT   "The nucleotide sequence of a cDNA clone encoding ribosomal protein
RT   S17 of Ehrlich ascites carcinoma cells.";
RL   Biochem. Genet. 32:409-414(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
CC   -!- SIMILARITY: Belongs to the ribosomal protein S17e family.
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DR   EMBL; D25213; BAA04943.1; -; mRNA.
DR   EMBL; AK007992; BAB25394.1; -; mRNA.
DR   EMBL; AK010647; BAB27087.1; -; mRNA.
DR   EMBL; BC002044; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC081466; AAH81466.1; -; mRNA.
DR   IPI; IPI00465880; -.
DR   RefSeq; NP_033118.1; NM_009092.3.
DR   UniGene; Mm.42767; -.
DR   UniGene; Mm.431314; -.
DR   ProteinModelPortal; P63276; -.
DR   SMR; P63276; 1-131.
DR   STRING; P63276; -.
DR   PhosphoSite; P63276; -.
DR   PRIDE; P63276; -.
DR   Ensembl; ENSMUST00000080813; ENSMUSP00000079628; ENSMUSG00000061787.
DR   GeneID; 20068; -.
DR   KEGG; mmu:20068; -.
DR   UCSC; uc009ibv.1; mouse.
DR   CTD; 20068; -.
DR   MGI; MGI:1309526; Rps17.
DR   eggNOG; roNOG10761; -.
DR   HOVERGEN; HBG001708; -.
DR   InParanoid; P63276; -.
DR   OMA; ETNKRIC; -.
DR   OrthoDB; EOG41JZDM; -.
DR   PhylomeDB; P63276; -.
DR   NextBio; 297571; -.
DR   ArrayExpress; P63276; -.
DR   Bgee; P63276; -.
DR   CleanEx; MM_RPS17; -.
DR   Genevestigator; P63276; -.
DR   GermOnline; ENSMUSG00000061787; Mus musculus.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR001210; Ribosomal_S17e.
DR   InterPro; IPR018273; Ribosomal_S17e_CS.
DR   Gene3D; G3DSA:1.10.60.20; Ribosomal_S17e; 1.
DR   PANTHER; PTHR10732; Ribosomal_S17E; 1.
DR   Pfam; PF00833; Ribosomal_S17e; 1.
DR   PROSITE; PS00712; RIBOSOMAL_S17E; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein; Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    135       40S ribosomal protein S17.
FT                                /FTId=PRO_0000141526.
FT   MOD_RES      19     19       N6-acetyllysine (By similarity).
FT   MOD_RES     113    113       Phosphoserine.
FT   MOD_RES     130    130       Phosphothreonine (By similarity).
SQ   SEQUENCE   135 AA;  15524 MW;  29806605C5401325 CRC64;
     MGRVRTKTVK KAARVIIEKY YTRLGNDFHT NKRVCEEIAI IPSKKLRNKI AGYVTHLMKR
     IQRGPVRGIS IKLQEEERER RDNYVPEVSA LDQEIIEVDP DTKEMLKLLD FGSLSNLQVT
     QPTVGMNFKT PRGAV
//
ID   KPCG_MOUSE              Reviewed;         697 AA.
AC   P63318; P05697;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Protein kinase C gamma type;
DE            Short=PKC-gamma;
DE            EC=2.7.11.13;
GN   Name=Prkcg; Synonyms=Pkcc, Pkcg, Prkcc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=93154595; PubMed=8428669; DOI=10.1016/0378-1119(93)90135-P;
RA   Bowers B.J., Parham C.L., Sikela J.M., Wehner J.M.;
RT   "Isolation and sequence of a mouse brain cDNA coding for protein
RT   kinase C-gamma isozyme.";
RL   Gene 123:263-265(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RA   Tseng C.P., Verma A.;
RL   Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-195 AND TYR-312, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322; SER-330; THR-514;
RP   THR-518; THR-655 AND SER-687, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: This is a calcium-activated, phospholipid-dependent,
CC       serine- and threonine-specific enzyme.
CC   -!- FUNCTION: PKC is activated by diacylglycerol which in turn
CC       phosphorylates a range of cellular proteins. PKC also serves as
CC       the receptor for phorbol esters, a class of tumor promoters.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Binds 3 calcium ions per subunit. The ions are bound to
CC       the C2 domain (By similarity).
CC   -!- SUBUNIT: Interacts with CDCP1 (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. PKC subfamily.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 2 phorbol-ester/DAG-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; X67129; CAA47608.1; -; mRNA.
DR   EMBL; L28035; AAA39939.1; -; mRNA.
DR   IPI; IPI00122069; -.
DR   PIR; JN0548; JN0548.
DR   RefSeq; NP_035232.1; NM_011102.3.
DR   UniGene; Mm.7980; -.
DR   ProteinModelPortal; P63318; -.
DR   SMR; P63318; 36-293, 345-683.
DR   MINT; MINT-98016; -.
DR   PRIDE; P63318; -.
DR   Ensembl; ENSMUST00000100301; ENSMUSP00000097874; ENSMUSG00000078816.
DR   GeneID; 18752; -.
DR   KEGG; mmu:18752; -.
DR   CTD; 18752; -.
DR   MGI; MGI:97597; Prkcc.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108317; -.
DR   InParanoid; P63318; -.
DR   OrthoDB; EOG40CHGD; -.
DR   PhylomeDB; P63318; -.
DR   BRENDA; 2.7.11.13; 244.
DR   NextBio; 294925; -.
DR   ArrayExpress; P63318; -.
DR   Bgee; P63318; -.
DR   CleanEx; MM_PRKCC; -.
DR   Genevestigator; P63318; -.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004697; F:protein kinase C activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007635; P:chemosensory behavior; IMP:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR014375; Protein_kinase_C_a/b/g.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   PIRSF; PIRSF000550; PKC_alpha; 1.
DR   PRINTS; PR00360; C2DOMAIN.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Calcium; Kinase; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Repeat;
KW   Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    697       Protein kinase C gamma type.
FT                                /FTId=PRO_0000055690.
FT   DOMAIN      170    260       C2.
FT   DOMAIN      351    614       Protein kinase.
FT   DOMAIN      615    685       AGC-kinase C-terminal.
FT   ZN_FING      35     85       Phorbol-ester/DAG-type 1.
FT   ZN_FING     100    150       Phorbol-ester/DAG-type 2.
FT   NP_BIND     357    365       ATP (By similarity).
FT   ACT_SITE    480    480       Proton acceptor (By similarity).
FT   METAL       186    186       Calcium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       187    187       Calcium 1 (By similarity).
FT   METAL       187    187       Calcium 2 (By similarity).
FT   METAL       193    193       Calcium 2 (By similarity).
FT   METAL       246    246       Calcium 1 (By similarity).
FT   METAL       246    246       Calcium 2 (By similarity).
FT   METAL       247    247       Calcium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       248    248       Calcium 1 (By similarity).
FT   METAL       248    248       Calcium 2 (By similarity).
FT   METAL       248    248       Calcium 3 (By similarity).
FT   METAL       251    251       Calcium 3 (By similarity).
FT   METAL       252    252       Calcium 3; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       254    254       Calcium 1 (By similarity).
FT   METAL       254    254       Calcium 3 (By similarity).
FT   BINDING     380    380       ATP (By similarity).
FT   MOD_RES     195    195       Phosphotyrosine.
FT   MOD_RES     197    197       N6-acetyllysine (By similarity).
FT   MOD_RES     312    312       Phosphotyrosine.
FT   MOD_RES     322    322       Phosphoserine.
FT   MOD_RES     330    330       Phosphoserine.
FT   MOD_RES     514    514       Phosphothreonine.
FT   MOD_RES     518    518       Phosphothreonine.
FT   MOD_RES     648    648       Phosphothreonine; by autocatalysis
FT                                (Potential).
FT   MOD_RES     655    655       Phosphothreonine; by autocatalysis
FT                                (Potential).
FT   MOD_RES     687    687       Phosphoserine.
SQ   SEQUENCE   697 AA;  78358 MW;  E6E2F7A3B93042FF CRC64;
     MAGLGPGGGD SEGGPRPLFC RKGALRQKVV HEVKSHKFTA RFFKQPTFCS HCTDFIWGIG
     KQGLQCQVCS FVVHRRCHEF VTFECPGAGK GPQTDDPRNK HKFRLHSYSS PTFCDHCGSL
     LYGLVHQGMK CSCCEMNVHR RCVRSVPSLC GVDHTERRGR LQLEIRAPTS DEIHITVGEA
     RNLIPMDPNG LSDPYVKLKL IPDPRNLTKQ KTKTVKATLN PVWNETFVFN LKPGDVERRL
     SVEVWDWDRT SRNDFMGAMS FGVSELLKAP VDGWYKLLNQ EEGEYYNVPV ADADNCSLLQ
     KFEACNYPLE LYERVRMGPS SSPIPSPSPS PTDSKRCFFG ASPGRLHISD FSFLMVLGKG
     SFGKVMLAER RGSDELYAIK ILKKDVIVQD DDVDCTLVEK RVLALGGRGP GGRPHFLTQL
     HSTFQTPDRL YFVMEYVTGG DLMYHIQQLG KFKEPHAAFY AAEIAIGLFF LHNQGIIYRD
     LKLDNVMLDA EGHIKITDFG MCKENVFPGS TTRTFCGTPD YIAPEIIAYQ PYGKSVDWWS
     FGVLLYEMLA GQPPFDGEDE EELFQAIMEQ TVTYPKSLSR EAVAICKGFL TKHPGKRLGS
     GPDGEPTIRA HGFFRWIDWE RLERLEIAPP FRPRPCGRSG ENFDKFFTRA APALTPPDRL
     VLASIDQADF QGFTYVNPDF VHPDARSPTS PVPVPVM
//
ID   RALA_MOUSE              Reviewed;         206 AA.
AC   P63321; P05810;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Ras-related protein Ral-A;
DE   Flags: Precursor;
GN   Name=Rala; Synonyms=Ral, Ral-a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Spleen;
RA   Roger T.T.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20480378; PubMed=11025226; DOI=10.1016/S0925-4773(00)00427-5;
RA   Zhao Z., Rivkees S.A.;
RT   "Tissue-specific expression of GTPas RalA and RalB during
RT   embryogenesis and regulation by epithelial-mesenchymal interaction.";
RL   Mech. Dev. 97:201-204(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 8-16; 28-47; 114-128 AND 167-173, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   INTERACTION WITH RALBP1.
RX   MEDLINE=96112637; PubMed=8570186;
RA   Park S.-H., Weinberg R.A.;
RT   "A putative effector of Ral has homology to Rho/Rac GTPase activating
RT   proteins.";
RL   Oncogene 11:2349-2355(1995).
RN   [6]
RP   FUNCTION.
RX   PubMed=20005108; DOI=10.1016/j.cub.2009.11.016;
RA   Balasubramanian N., Meier J.A., Scott D.W., Norambuena A., White M.A.,
RA   Schwartz M.A.;
RT   "RalA-exocyst complex regulates integrin-dependent membrane raft
RT   exocytosis and growth signaling.";
RL   Curr. Biol. 20:75-79(2009).
CC   -!- FUNCTION: Multifuntional GTPase involved in a variety of cellular
CC       processes including gene expression, cell migration, cell
CC       proliferation, oncogenic transformation and membrane trafficking.
CC       Accomplishes its multiple functions by interacting with distinct
CC       downstream effectors. Acts as a GTP sensor for GTP-dependent
CC       exocytosis of dense core vesicles. Plays a role in the early
CC       stages of cytokinesis and is required to tether the exocyst to the
CC       cytokinetic furrow. Key regulator of LPAR1 signaling and competes
CC       with ADRBK1 for binding to LPAR1 thus affecting the signaling
CC       properties of the receptor. Required for anchorage-independent
CC       proliferation of transformed cells (By similarity). The RALA-
CC       exocyst complex regulates integrin-dependent membrane raft
CC       exocytosis and growth signaling.
CC   -!- ENZYME REGULATION: Alternate between an inactive form bound to GDP
CC       and an active form bound to GTP. Activated by a guanine
CC       nucleotide-exchange factor (GEF) and inactivated by a GTPase-
CC       activating protein (GAP).
CC   -!- SUBUNIT: Interacts with CDC42 (By similarity). Interacts with
CC       EXOC8 and EXOC2. EXOC2 and EXOC8 have overlapping binding sites
CC       and compete for RALA binding (By similarity). Interacts with
CC       RALGPS1 (By similarity). Interacts with RALBP1 via its effector
CC       domain. Interacts with LPAR1 and LPAR2. Interacts with ADRBK1 in
CC       response to LPAR1 activation. RALA and ADRBK1 mutually inhibit
CC       each other's binding to LPAR1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell surface (By similarity). Cell membrane;
CC       Lipid-anchor; Cytoplasmic side (By similarity). Cleavage furrow.
CC       Midbody (By similarity). Note=Prior to LPA treatment found
CC       predominantly at the cell surface and in the presence of LPA co-
CC       localizes with LPAR1 and LPAR2 in the endocytic vesicles. During
CC       early cytokinesis localizes at the cleavage furrow membrane.
CC       Colocalizes with EXOC2 at the early midbody ring and persists
CC       there till maturation of the midbody (By similarity).
CC   -!- PTM: Prenylation is essential for membrane localization (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
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DR   EMBL; Z48587; CAA88488.1; -; mRNA.
DR   EMBL; AF244951; AAG23136.1; -; mRNA.
DR   EMBL; BC031741; AAH31741.1; -; mRNA.
DR   IPI; IPI00124282; -.
DR   RefSeq; NP_062364.3; NM_019491.5.
DR   UniGene; Mm.27348; -.
DR   ProteinModelPortal; P63321; -.
DR   SMR; P63321; 11-178.
DR   STRING; P63321; -.
DR   PhosphoSite; P63321; -.
DR   PRIDE; P63321; -.
DR   Ensembl; ENSMUST00000009003; ENSMUSP00000009003; ENSMUSG00000008859.
DR   GeneID; 56044; -.
DR   KEGG; mmu:56044; -.
DR   UCSC; uc007pof.1; mouse.
DR   CTD; 56044; -.
DR   MGI; MGI:1927243; Rala.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; P63321; -.
DR   OMA; SAKRREN; -.
DR   OrthoDB; EOG4HX524; -.
DR   PhylomeDB; P63321; -.
DR   NextBio; 311812; -.
DR   ArrayExpress; P63321; -.
DR   Bgee; P63321; -.
DR   Genevestigator; P63321; -.
DR   GermOnline; ENSMUSG00000008859; Mus musculus.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0031755; F:Edg-2 lysophosphatidic acid receptor binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0000910; P:cytokinesis; ISS:UniProtKB.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0051665; P:membrane raft localization; IDA:UniProtKB.
DR   GO; GO:0017157; P:regulation of exocytosis; IDA:UniProtKB.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003577; GTPase_Ras.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR020849; Ras_small_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00173; RAS; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cell membrane; Direct protein sequencing;
KW   Exocytosis; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation.
FT   CHAIN         1    203       Ras-related protein Ral-A.
FT                                /FTId=PRO_0000082694.
FT   PROPEP      204    206       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000281345.
FT   NP_BIND      21     28       GTP (By similarity).
FT   NP_BIND      68     72       GTP (By similarity).
FT   NP_BIND     127    130       GTP (By similarity).
FT   MOTIF        43     51       Effector region (By similarity).
FT   MOD_RES     203    203       Cysteine methyl ester (By similarity).
FT   LIPID       203    203       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   206 AA;  23553 MW;  6974341FA08C1874 CRC64;
     MAANKPKGQN SLALHKVIMV GSGGVGKSAL TLQFMYDEFV EDYEPTKADS YRKKVVLDGE
     EVQIDILDTA GQEDYAAIRD NYFRSGEGFL CVFSITEMES FAATADFREQ ILRVKEDENV
     PFLLVGNKSD LEDKRQVSVE EAKNRADQWN VNYVETSAKT RANVDKVFFD LMREIRARKM
     EDSKEKNGKK KRKSLAKRIR ERCCIL
//
ID   PP2BA_MOUSE             Reviewed;         521 AA.
AC   P63328; P12816; P20652; Q3UCU1; Q64135;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform;
DE            EC=3.1.3.16;
DE   AltName: Full=CAM-PRP catalytic subunit;
DE   AltName: Full=Calmodulin-dependent calcineurin A subunit alpha isoform;
GN   Name=Ppp3ca; Synonyms=Calna;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=90293081; PubMed=2162844;
RA   Kincaid R.L., Giri P.R., Higuchi S., Tamura J., Dixon S.C.,
RA   Marietta C.A., Amorese D.A., Martin B.M.;
RT   "Cloning and characterization of molecular isoforms of the catalytic
RT   subunit of calcineurin using nonisotopic methods.";
RL   J. Biol. Chem. 265:11312-11319(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=BALB/c, and C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF 64-73; 101-122 AND 425-459, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 95-116.
RX   MEDLINE=94357899; PubMed=8077208;
RA   Becker W., Kentrup H., Klumpp S., Schultz J.E., Joost H.G.;
RT   "Molecular cloning of a protein serine/threonine phosphatase
RT   containing a putative regulatory tetratricopeptide repeat domain.";
RL   J. Biol. Chem. 269:22586-22592(1994).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 215-521 (ISOFORM 1).
RX   MEDLINE=89057863; PubMed=2848250; DOI=10.1073/pnas.85.23.8983;
RA   Kincaid R.L., Nightingale M.S., Martin B.M.;
RT   "Characterization of a cDNA clone encoding the calmodulin-binding
RT   domain of mouse brain calcineurin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 85:8983-8987(1988).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 467-491, AND MUTAGENESIS OF ASP-477.
RX   MEDLINE=95311985; PubMed=7791792;
RA   Fruman D.A., Pai S.-Y., Burakoff S.J., Bierer B.E.;
RT   "Characterization of a mutant calcineurin A alpha gene expressed by
RT   EL4 lymphoma cells.";
RL   Mol. Cell. Biol. 15:3857-3863(1995).
RN   [7]
RP   FUNCTION.
RX   PubMed=1328240;
RA   Gaestel M., Benndorf R., Hayess K., Priemer E., Engel K.;
RT   "Dephosphorylation of the small heat shock protein hsp25 by
RT   calcium/calmodulin-dependent (type 2B) protein phosphatase.";
RL   J. Biol. Chem. 267:21607-21611(1992).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=20570531; PubMed=11114196; DOI=10.1073/pnas.260501097;
RA   Frey N., Richardson J.A., Olson E.N.;
RT   "Calsarcins, a novel family of sarcomeric calcineurin-binding
RT   proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14632-14637(2000).
RN   [9]
RP   NITRATION [LARGE SCALE ANALYSIS] AT TYR-224, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16800626; DOI=10.1021/bi060474w;
RA   Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
RA   Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
RA   Squier T.C., Bigelow D.J.;
RT   "Endogenously nitrated proteins in mouse brain: links to
RT   neurodegenerative disease.";
RL   Biochemistry 45:8009-8022(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Calcium-dependent, calmodulin-stimulated protein
CC       phosphatase. This subunit may have a role in the calmodulin
CC       activation of calcineurin. Dephosphorylates DNM1L and HSPB1 (By
CC       similarity). Dephosphorylates SSH1.
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- COFACTOR: Binds 1 Fe(3+) ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Composed of two components (A and B), the A component is
CC       the catalytic subunit and the B component confers calcium
CC       sensitivity. Interacts with CRTC2, MYOZ1, MYOZ2 and MYOZ3.
CC       Interacts with DNM1L; the interaction dephosphorylates DNM1L and
CC       regulates its translocation to mitochondria (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with ACTN1 and
CC       MYOZ2 at the Z line in heart and skeletal muscle.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P63328-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P63328-2; Sequence=VSP_018563;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2B
CC       subfamily.
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DR   EMBL; J05479; AAA37359.1; -; mRNA.
DR   EMBL; AK146387; BAE27131.1; -; mRNA.
DR   EMBL; AK150393; BAE29521.1; -; mRNA.
DR   EMBL; J04134; AAA37432.1; -; mRNA.
DR   EMBL; S78668; AAB34675.1; -; mRNA.
DR   IPI; IPI00121545; -.
DR   IPI; IPI00756703; -.
DR   PIR; A42232; A31257.
DR   RefSeq; NP_032939.1; NM_008913.4.
DR   UniGene; Mm.331389; -.
DR   ProteinModelPortal; P63328; -.
DR   SMR; P63328; 1-372.
DR   MINT; MINT-135995; -.
DR   STRING; P63328; -.
DR   PhosphoSite; P63328; -.
DR   PRIDE; P63328; -.
DR   Ensembl; ENSMUST00000056758; ENSMUSP00000053101; ENSMUSG00000028161.
DR   Ensembl; ENSMUST00000070198; ENSMUSP00000071040; ENSMUSG00000028161.
DR   GeneID; 19055; -.
DR   KEGG; mmu:19055; -.
DR   UCSC; uc008rmg.1; mouse.
DR   UCSC; uc008rmh.1; mouse.
DR   CTD; 19055; -.
DR   MGI; MGI:107164; Ppp3ca.
DR   eggNOG; roNOG11256; -.
DR   GeneTree; ENSGT00530000063087; -.
DR   HOGENOM; HBG716770; -.
DR   HOVERGEN; HBG002819; -.
DR   InParanoid; P63328; -.
DR   OMA; SVWPAGP; -.
DR   OrthoDB; EOG4PVNZK; -.
DR   PhylomeDB; P63328; -.
DR   BRENDA; 3.1.3.16; 244.
DR   NextBio; 295542; -.
DR   ArrayExpress; P63328; -.
DR   Bgee; P63328; -.
DR   Genevestigator; P63328; -.
DR   GermOnline; ENSMUSG00000028161; Mus musculus.
DR   GO; GO:0005955; C:calcineurin complex; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0030018; C:Z disc; IDA:MGI.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI.
DR   GO; GO:0006606; P:protein import into nucleus; IDA:MGI.
DR   GO; GO:0060079; P:regulation of excitatory postsynaptic membrane potential; IGI:MGI.
DR   GO; GO:0050804; P:regulation of synaptic transmission; IMP:MGI.
DR   GO; GO:0006950; P:response to stress; IDA:MGI.
DR   GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI.
DR   InterPro; IPR004843; Metallo-dependent_phosphatase.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR11668; T_phtase_apaH; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calmodulin-binding; Direct protein sequencing;
KW   Hydrolase; Iron; Metal-binding; Nitration; Nucleus; Phosphoprotein;
KW   Protein phosphatase; Zinc.
FT   CHAIN         1    521       Serine/threonine-protein phosphatase 2B
FT                                catalytic subunit alpha isoform.
FT                                /FTId=PRO_0000058823.
FT   REGION        1    301       Catalytic.
FT   REGION      247    253       Calcineurin B binding-site 1 (Potential).
FT   REGION      296    301       Calcineurin B binding-site 2 (Potential).
FT   REGION      392    414       Calmodulin-binding (Potential).
FT   REGION      465    487       Inhibitory domain.
FT   ACT_SITE    151    151       Proton donor (By similarity).
FT   METAL        90     90       Iron (By similarity).
FT   METAL        92     92       Iron (By similarity).
FT   METAL       118    118       Iron (By similarity).
FT   METAL       118    118       Zinc (By similarity).
FT   METAL       150    150       Zinc (By similarity).
FT   METAL       199    199       Zinc (By similarity).
FT   METAL       281    281       Zinc (By similarity).
FT   MOD_RES     224    224       Nitrated tyrosine.
FT   MOD_RES     469    469       Phosphoserine.
FT   VAR_SEQ     448    457       Missing (in isoform 2).
FT                                /FTId=VSP_018563.
FT   MUTAGEN     477    477       D->N: Greatly reduces inhibition of
FT                                calcineurin phosphatase activity.
SQ   SEQUENCE   521 AA;  58644 MW;  16530C27DDBF1F05 CRC64;
     MSEPKAIDPK LSTTDRVVKA VPFPPSHRLT AKEVFDNDGK PRVDILKAHL MKEGRLEESV
     ALRIITEGAS ILRQEKNLLD IDAPVTVCGD IHGQFFDLMK LFEVGGSPAN TRYLFLGDYV
     DRGYFSIECV LYLWALKILY PKTLFLLRGN HECRHLTEYF TFKQECKIKY SERVYDACMD
     AFDCLPLAAL MNQQFLCVHG GLSPEINTLD DIRKLDRFKE PPAYGPMCDI LWSDPLEDFG
     NEKTQEHFTH NTVRGCSYFY SYPAVCDFLQ HNNLLSILRA HEAQDAGYRM YRKSQTTGFP
     SLITIFSAPN YLDVYNNKAA VLKYENNVMN IRQFNCSPHP YWLPNFMDVF TWSLPFVGEK
     VTEMLVNVLN ICSDDELGSE EDGFDGATAA ARKEVIRNKI RAIGKMARVF SVLREESESV
     LTLKGLTPTG MLPSGVLSGG KQTLQSATVE AIEADEAIKG FSPQHKITSF EEAKGLDRIN
     ERMPPRRDAM PSDANLNSIN KALASETNGT DSNGSNSSNI Q
//
ID   PP2AA_MOUSE             Reviewed;         309 AA.
AC   P63330; O88591; P13353; Q5SNY5;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform;
DE            Short=PP2A-alpha;
DE            EC=3.1.3.16;
GN   Name=Ppp2ca;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X DBA/2; TISSUE=Brain;
RA   Goetz J.M., Kues W.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99121080; PubMed=9920888; DOI=10.1074/jbc.274.6.3439;
RA   Hsu W., Zeng L., Costantini F.;
RT   "Identification of a domain of Axin that binds to the serine/threonine
RT   protein phosphatase 2A and a self-binding domain.";
RL   J. Biol. Chem. 274:3439-3445(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PHOSPHORYLATION.
RX   MEDLINE=94179160; PubMed=7510677;
RA   Chen J., Parsons S., Brautigan D.L.;
RT   "Tyrosine phosphorylation of protein phosphatase 2A in response to
RT   growth stimulation and v-src transformation of fibroblasts.";
RL   J. Biol. Chem. 269:7957-7962(1994).
RN   [7]
RP   MUTAGENESIS OF TYR-307 AND LEU-309.
RX   MEDLINE=99371680; PubMed=10441131; DOI=10.1021/bi990902g;
RA   Chung H., Nairn A.C., Murata K., Brautigan D.L.;
RT   "Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic
RT   subunit favors association with the alpha 4 subunit which promotes
RT   dephosphorylation of elongation factor-2.";
RL   Biochemistry 38:10371-10376(1999).
RN   [8]
RP   INTERACTION WITH NXN.
RX   PubMed=16764867; DOI=10.1016/j.febslet.2006.04.101;
RA   Lechward K., Sugajska E., de Baere I., Goris J., Hemmings B.A.,
RA   Zolnierowicz S.;
RT   "Interaction of nucleoredoxin with protein phosphatase 2A.";
RL   FEBS Lett. 580:3631-3637(2006).
RN   [9]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18084284; DOI=10.1038/ncb1667;
RA   Lee J., Kitajima T.S., Tanno Y., Yoshida K., Morita T., Miyano T.,
RA   Miyake M., Watanabe Y.;
RT   "Unified mode of centromeric protection by shugoshin in mammalian
RT   oocytes and somatic cells.";
RL   Nat. Cell Biol. 10:42-52(2008).
CC   -!- FUNCTION: PP2A can modulate the activity of phosphorylase B kinase
CC       casein kinase 2, mitogen-stimulated S6 kinase, and MAP-2 kinase.
CC       Cooperates with SGOL2 to protect centromeric cohesin from
CC       separase-mediated cleavage in oocytes specifically during meiosis
CC       I.
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- COFACTOR: Binds 1 iron ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity).
CC   -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme,
CC       composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and
CC       PPP2R1A a 65 kDa constant regulatory subunit (PR65 or subunit A),
CC       that associates with a variety of regulatory subunits. Proteins
CC       that associate with the core dimer include three families of
CC       regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59
CC       and R5/B'/B56 families), the 48 kDa variable regulatory subunit,
CC       viral proteins, and cell signaling molecules. Interacts with NXN;
CC       the interaction is direct. Interacts with TP53, SGOL1 and SGOL2.
CC       Interacts with AXIN1; the interaction dephosphorylates AXIN1(By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus (By similarity).
CC       Chromosome, centromere. Cytoplasm, cytoskeleton, spindle pole (By
CC       similarity). Note=In prometaphase cells, but not in anaphase
CC       cells, localizes at centromeres. During mitosis, also found at
CC       spindle poles (By similarity). Centromeric localization requires
CC       the presence of SGOL2.
CC   -!- PTM: Reversibly methyl esterified on Leu-309. Carboxyl methylation
CC       may play a role in holoenzyme assembly. It varies during the cell
CC       cycle.
CC   -!- PTM: Phosphorylation of either threonine (by autophosphorylation-
CC       activated protein kinase) or tyrosine results in inactivation of
CC       the phosphatase. Auto-dephosphorylation has been suggested as a
CC       mechanism for reactivation.
CC   -!- MISCELLANEOUS: Double mutation Phe-307 and Gln-309 results in
CC       association of the PP2A C subunit with alpha-4 protein.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF076192; AAD12587.1; -; mRNA.
DR   EMBL; Z67745; CAA91558.1; -; mRNA.
DR   EMBL; AK076110; BAC36190.1; -; mRNA.
DR   EMBL; AK172644; BAE43111.1; -; mRNA.
DR   EMBL; AL935177; CAI25806.1; -; Genomic_DNA.
DR   EMBL; BC003856; AAH03856.1; -; mRNA.
DR   EMBL; BC054458; AAH54458.1; -; mRNA.
DR   IPI; IPI00120374; -.
DR   RefSeq; NP_062284.1; NM_019411.4.
DR   UniGene; Mm.260288; -.
DR   ProteinModelPortal; P63330; -.
DR   SMR; P63330; 6-293.
DR   STRING; P63330; -.
DR   PhosphoSite; P63330; -.
DR   PRIDE; P63330; -.
DR   Ensembl; ENSMUST00000020608; ENSMUSP00000020608; ENSMUSG00000020349.
DR   GeneID; 19052; -.
DR   KEGG; mmu:19052; -.
DR   UCSC; uc007ivb.1; mouse.
DR   CTD; 19052; -.
DR   MGI; MGI:1321159; Ppp2ca.
DR   eggNOG; roNOG15147; -.
DR   GeneTree; ENSGT00550000074618; -.
DR   HOGENOM; HBG716770; -.
DR   HOVERGEN; HBG000216; -.
DR   InParanoid; P63330; -.
DR   OMA; AIMEIDE; -.
DR   OrthoDB; EOG4Q58PR; -.
DR   PhylomeDB; P63330; -.
DR   BRENDA; 3.1.3.16; 244.
DR   NextBio; 295524; -.
DR   ArrayExpress; P63330; -.
DR   Bgee; P63330; -.
DR   Genevestigator; P63330; -.
DR   GermOnline; ENSMUSG00000020349; Mus musculus.
DR   GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IDA:MGI.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; TAS:MGI.
DR   GO; GO:0007126; P:meiosis; IEA:UniProtKB-KW.
DR   GO; GO:0007498; P:mesoderm development; IMP:MGI.
DR   GO; GO:0006470; P:protein dephosphorylation; TAS:MGI.
DR   GO; GO:0051726; P:regulation of cell cycle; TAS:MGI.
DR   InterPro; IPR004843; Metallo-dependent_phosphatase.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR11668; T_phtase_apaH; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW   Hydrolase; Iron; Manganese; Meiosis; Metal-binding; Methylation;
KW   Nucleus; Phosphoprotein; Protein phosphatase.
FT   CHAIN         1    309       Serine/threonine-protein phosphatase 2A
FT                                catalytic subunit alpha isoform.
FT                                /FTId=PRO_0000058840.
FT   ACT_SITE    118    118       Proton donor (By similarity).
FT   METAL        57     57       Iron (By similarity).
FT   METAL        59     59       Iron (By similarity).
FT   METAL        85     85       Iron (By similarity).
FT   METAL        85     85       Manganese (By similarity).
FT   METAL       117    117       Manganese (By similarity).
FT   METAL       167    167       Manganese (By similarity).
FT   METAL       241    241       Manganese (By similarity).
FT   MOD_RES       4      4       N6-acetyllysine (By similarity).
FT   MOD_RES     307    307       Phosphotyrosine.
FT   MOD_RES     309    309       Leucine methyl ester.
FT   MUTAGEN     307    307       Y->Q: Loss of trimeric subunit ABC
FT                                assembly.
FT   MUTAGEN     309    309       L->A: Loss of binding to PP2A B-alpha
FT                                regulatory subunit.
FT   CONFLICT     31     31       L -> P (in Ref. 2; AAD12587).
FT   CONFLICT     73     73       G -> V (in Ref. 2; AAD12587).
SQ   SEQUENCE   309 AA;  35608 MW;  8DC11276E6DF9E33 CRC64;
     MDEKLFTKEL DQWIEQLNEC KQLSESQVKS LCEKAKEILT KESNVQEVRC PVTVCGDVHG
     QFHDLMELFR IGGKSPDTNY LFMGDYVDRG YYSVETVTLL VALKVRYRER ITILRGNHES
     RQITQVYGFY DECLRKYGNA NVWKYFTDLF DYLPLTALVD GQIFCLHGGL SPSIDTLDHI
     RALDRLQEVP HEGPMCDLLW SDPDDRGGWG ISPRGAGYTF GQDISETFNH ANGLTLVSRA
     HQLVMEGYNW CHDRNVVTIF SAPNYCYRCG NQAAIMELDD TLKYSFLQFD PAPRRGEPHV
     TRRTPDYFL
//
ID   PHB_MOUSE               Reviewed;         272 AA.
AC   P67778; P24142; Q3UB75; Q5SQG4;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Prohibitin;
DE   AltName: Full=B-cell receptor-associated protein 32;
DE            Short=BAP 32;
GN   Name=Phb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Lymphoid tissue;
RX   MEDLINE=94349926; PubMed=8070406;
RA   Terashima M., Kim K.-M., Adachi T., Nielsen P.J., Reth M., Koehler G.,
RA   Lamers M.C.;
RT   "The IgM antigen receptor of B lymphocytes is associated with
RT   prohibitin and a prohibitin-related protein.";
RL   EMBO J. 13:3782-3792(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2; TISSUE=Bone marrow, Heart, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 12-34; 94-105; 158-177; 220-239 AND 241-253, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [6]
RP   INTERACTION WITH PHB2, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=11302691; DOI=10.1006/excr.2001.5166;
RA   Coates P.J., Nenutil R., McGregor A., Picksley S.M., Crouch D.H.,
RA   Hall P.A., Wright E.G.;
RT   "Mammalian prohibitin proteins respond to mitochondrial stress and
RT   decrease during cellular senescence.";
RL   Exp. Cell Res. 265:262-273(2001).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-249, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Prohibitin inhibits DNA synthesis. It has a role in
CC       regulating proliferation. As yet it is unclear if the protein or
CC       the mRNA exhibits this effect. May play a role in regulating
CC       mitochondrial respiration activity and in aging (By similarity).
CC   -!- SUBUNIT: Interacts with PHB2.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
CC   -!- TISSUE SPECIFICITY: Widely expressed in different tissues.
CC   -!- DEVELOPMENTAL STAGE: Throughout gestation, highly expressed in
CC       brown fat, heart, liver, developing renal tubules and neurons, and
CC       detected at lower levels in tissues such as lung and exocrine
CC       pancreas.
CC   -!- SIMILARITY: Belongs to the prohibitin family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X78682; CAA55349.1; -; mRNA.
DR   EMBL; AK002714; BAB22305.1; -; mRNA.
DR   EMBL; AK010619; BAB27067.1; -; mRNA.
DR   EMBL; AK150956; BAE29988.1; -; mRNA.
DR   EMBL; AK151073; BAE30089.1; -; mRNA.
DR   EMBL; AK168248; BAE40198.1; -; mRNA.
DR   EMBL; AK168656; BAE40512.1; -; mRNA.
DR   EMBL; AL732490; CAI24279.1; -; Genomic_DNA.
DR   EMBL; BC083354; AAH83354.1; -; mRNA.
DR   EMBL; BC089034; AAH89034.1; -; mRNA.
DR   IPI; IPI00133440; -.
DR   RefSeq; NP_032857.1; NM_008831.4.
DR   UniGene; Mm.263862; -.
DR   ProteinModelPortal; P67778; -.
DR   STRING; P67778; -.
DR   PhosphoSite; P67778; -.
DR   SWISS-2DPAGE; P67778; -.
DR   REPRODUCTION-2DPAGE; IPI00133440; -.
DR   REPRODUCTION-2DPAGE; P67778; -.
DR   PRIDE; P67778; -.
DR   Ensembl; ENSMUST00000036374; ENSMUSP00000047536; ENSMUSG00000038845.
DR   GeneID; 18673; -.
DR   KEGG; mmu:18673; -.
DR   UCSC; uc007lan.1; mouse.
DR   CTD; 18673; -.
DR   MGI; MGI:97572; Phb.
DR   eggNOG; roNOG05679; -.
DR   HOGENOM; HBG680510; -.
DR   HOVERGEN; HBG004457; -.
DR   InParanoid; P67778; -.
DR   OMA; GNEVLKS; -.
DR   OrthoDB; EOG4X3H23; -.
DR   PhylomeDB; P67778; -.
DR   NextBio; 294690; -.
DR   ArrayExpress; P67778; -.
DR   Bgee; P67778; -.
DR   CleanEx; MM_PHB; -.
DR   Genevestigator; P67778; -.
DR   GermOnline; ENSMUSG00000038845; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   InterPro; IPR001107; Band_7.
DR   InterPro; IPR000163; Prohibitin.
DR   PANTHER; PTHR23222; Prohibitin; 1.
DR   Pfam; PF01145; Band_7; 1.
DR   PRINTS; PR00679; PROHIBITIN.
DR   SMART; SM00244; PHB; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Direct protein sequencing; DNA synthesis;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein.
FT   CHAIN         1    272       Prohibitin.
FT                                /FTId=PRO_0000213879.
FT   COILED      177    211       Potential.
FT   MOD_RES     202    202       N6-acetyllysine (By similarity).
FT   MOD_RES     249    249       Phosphotyrosine.
FT   MOD_RES     252    252       Phosphoserine (By similarity).
FT   MOD_RES     254    254       Phosphoserine (By similarity).
FT   MOD_RES     265    265       Phosphoserine (By similarity).
FT   CONFLICT    255    255       R -> W (in Ref. 2; BAE29988/BAE30089).
SQ   SEQUENCE   272 AA;  29820 MW;  6B26073E169C2FFC CRC64;
     MAAKVFESIG KFGLALAVAG GVVNSALYNV DAGHRAVIFD RFRGVQDIVV GEGTHFLIPW
     VQKPIIFDCR SRPRNVPVIT GSKDLQNVNI TLRILFRPVA SQLPRIYTSI GEDYDERVLP
     SITTEILKSV VARFDAGELI TQRELVSRQV SDDLTERAAT FGLILDDVSL THLTFGKEFT
     EAVEAKQVAQ QEAERARFVV EKAEQQKKAA IISAEGDSKA AELIANSLAT AGDGLIELRK
     LEAAEDIAYQ LSRSRNITYL PAGQSVLLQL PQ
//
ID   CSK2B_MOUSE             Reviewed;         215 AA.
AC   P67871; P07312; P13862; Q3TTJ7;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Casein kinase II subunit beta;
DE            Short=CK II beta;
DE   AltName: Full=Phosvitin;
GN   Name=Csnk2b; Synonyms=Ck2n;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=90301488; PubMed=2362816; DOI=10.1093/nar/18.12.3639;
RA   Kopatz I., Naiman T., Eli D., Canaani D.;
RT   "The nucleotide sequence of the mouse cDNA encoding the beta subunit
RT   of casein kinase II.";
RL   Nucleic Acids Res. 18:3639-3639(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=91198153; PubMed=2015307; DOI=10.1016/0167-4781(91)90140-H;
RA   Boldyreff B., Piontek K., Schmidt-Spaniol I., Issinger O.-J.;
RT   "The beta subunit of casein kinase II: cloning of cDNAs from murine
RT   and porcine origin and expression of the porcine sequence as a fusion
RT   protein.";
RL   Biochim. Biophys. Acta 1088:439-441(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C57BL/6 X CBA; TISSUE=Spleen;
RX   MEDLINE=96079116; PubMed=8530080; DOI=10.1006/geno.1995.1239;
RA   Boldyreff B., Issinger O.G.;
RT   "Structure of the gene encoding the murine protein kinase CK2 beta
RT   subunit.";
RL   Genomics 29:253-256(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129;
RX   PubMed=14656967; DOI=10.1101/gr.1736803;
RA   Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
RA   Campbell R.D., Hood L.;
RT   "Analysis of the gene-dense major histocompatibility complex class III
RT   region and its comparison to mouse.";
RL   Genome Res. 13:2621-2636(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2; TISSUE=Kidney, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   FUNCTION IN WNT SIGNALING.
RX   MEDLINE=20379015; PubMed=10806215; DOI=10.1074/jbc.M909107199;
RA   Song D.H., Sussman D.J., Seldin D.C.;
RT   "Endogenous protein kinase CK2 participates in Wnt signaling in
RT   mammary epithelial cells.";
RL   J. Biol. Chem. 275:23790-23797(2000).
RN   [8]
RP   INTERACTION WITH TCTEX1D3.
RX   MEDLINE=22733188; PubMed=12849985; DOI=10.1016/S0006-291X(03)01118-5;
RA   Bai X., Xu X., Zhang F., Shu H.-B., Chan E.D.;
RT   "The protein of a new gene, Tctex4, interacts with protein kinase
RT   CK2beta subunit and is highly expressed in mouse testis.";
RL   Biochem. Biophys. Res. Commun. 307:86-91(2003).
CC   -!- FUNCTION: Plays a complex role in regulating the basal catalytic
CC       activity of the alpha subunit (By similarity). Participates in Wnt
CC       signaling.
CC   -!- SUBUNIT: Tetramer composed of an alpha subunit, an alpha' subunit
CC       and two beta subunits. Interacts with CD163. Also component of a
CC       CK2-SPT16-SSRP1 complex composed of SSRP1, SUPT16H, CSNK2A1,
CC       CSNK2A2 and CSNK2B, the complex associating following UV
CC       irradiation (By similarity). Interacts with TCTEX1D3.
CC   -!- INTERACTION:
CC       P11985-2:Tcte3; NbExp=1; IntAct=EBI-348179, EBI-1781298;
CC   -!- PTM: Phosphorylated by alpha subunit (By similarity).
CC   -!- SIMILARITY: Belongs to the casein kinase 2 subunit beta family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X52959; CAA37132.1; -; mRNA.
DR   EMBL; X56502; CAA39857.1; -; mRNA.
DR   EMBL; X80685; CAA56700.1; -; Genomic_DNA.
DR   EMBL; AF109719; AAF03911.1; -; Genomic_DNA.
DR   EMBL; AK002903; BAB22445.1; -; mRNA.
DR   EMBL; AK010730; BAB27147.1; -; mRNA.
DR   EMBL; AK012369; BAB28193.1; -; mRNA.
DR   EMBL; AK146186; BAE26962.1; -; mRNA.
DR   EMBL; AK161330; BAE36328.1; -; mRNA.
DR   EMBL; BC003775; AAH03775.1; -; mRNA.
DR   IPI; IPI00126762; -.
DR   PIR; S14724; S14724.
DR   RefSeq; NP_034105.1; NM_009975.2.
DR   UniGene; Mm.378901; -.
DR   ProteinModelPortal; P67871; -.
DR   SMR; P67871; 2-205.
DR   IntAct; P67871; 5.
DR   STRING; P67871; -.
DR   PhosphoSite; P67871; -.
DR   PRIDE; P67871; -.
DR   Ensembl; ENSMUST00000025246; ENSMUSP00000025246; ENSMUSG00000024387.
DR   GeneID; 13001; -.
DR   KEGG; mmu:13001; -.
DR   UCSC; uc008cfu.1; mouse.
DR   CTD; 13001; -.
DR   MGI; MGI:88548; Csnk2b.
DR   eggNOG; roNOG06919; -.
DR   GeneTree; ENSGT00390000003781; -.
DR   HOGENOM; HBG736305; -.
DR   HOVERGEN; HBG051131; -.
DR   InParanoid; P67871; -.
DR   OMA; FKIHPLA; -.
DR   OrthoDB; EOG4FBHTQ; -.
DR   PhylomeDB; P67871; -.
DR   NextBio; 282816; -.
DR   ArrayExpress; P67871; -.
DR   Bgee; P67871; -.
DR   CleanEx; MM_CSNK2B; -.
DR   Genevestigator; P67871; -.
DR   GermOnline; ENSMUSG00000024387; Mus musculus.
DR   GO; GO:0005956; C:protein kinase CK2 complex; IEA:InterPro.
DR   GO; GO:0019887; F:protein kinase regulator activity; IEA:InterPro.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR016149; Casein_kin_II_reg-sub_a-hlx.
DR   InterPro; IPR016150; Casein_kin_II_reg-sub_b-sht.
DR   InterPro; IPR000704; Casein_kinase_II_reg-sub.
DR   Gene3D; G3DSA:1.10.1820.10; Casein_kin_II_reg-sub_a-hlx; 1.
DR   Gene3D; G3DSA:2.20.25.20; Casein_kin_II_reg-sub_b-sht; 1.
DR   PANTHER; PTHR11740; CAS_kinase_II; 1.
DR   Pfam; PF01214; CK_II_beta; 1.
DR   PRINTS; PR00472; CASNKINASEII.
DR   SUPFAM; SSF57798; Casein_kinase_II_reg-sub; 1.
DR   PROSITE; PS01101; CK2_BETA; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein; Wnt signaling pathway.
FT   CHAIN         1    215       Casein kinase II subunit beta.
FT                                /FTId=PRO_0000068237.
FT   COMPBIAS     55     64       Asp/Glu-rich (acidic).
FT   MOD_RES       2      2       Phosphoserine; by autocatalysis
FT                                (Probable).
FT   MOD_RES       3      3       Phosphoserine (By similarity).
FT   MOD_RES       4      4       Phosphoserine (By similarity).
FT   MOD_RES       8      8       Phosphoserine (By similarity).
FT   MOD_RES      69     69       Phosphoserine (By similarity).
FT   MOD_RES     145    145       Phosphothreonine (By similarity).
FT   MOD_RES     197    197       Phosphotyrosine (By similarity).
FT   MOD_RES     205    205       Phosphoserine (By similarity).
FT   MOD_RES     209    209       Phosphoserine (By similarity).
FT   MOD_RES     212    212       N6-acetyllysine (By similarity).
SQ   SEQUENCE   215 AA;  24942 MW;  E465B1E699B0E0EC CRC64;
     MSSSEEVSWI SWFCGLRGNE FFCEVDEDYI QDKFNLTGLN EQVPHYRQAL DMILDLEPDE
     ELEDNPNQSD LIEQAAEMLY GLIHARYILT NRGIAQMLEK YQQGDFGYCP RVYCENQPML
     PIGLSDIPGE AMVKLYCPKC MDVYTPKSSR HHHTDGAYFG TGFPHMLFMV HPEYRPKRPA
     NQFVPRLYGF KIHPMAYQLQ LQAASNFKSP VKTIR
//
ID   ACTC_MOUSE              Reviewed;         377 AA.
AC   P68033; P04270;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-1987, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Actin, alpha cardiac muscle 1;
DE   AltName: Full=Alpha-cardiac actin;
GN   Name=Actc1; Synonyms=Actc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-377.
RX   MEDLINE=87129278; PubMed=3028523; DOI=10.1007/BF01116542;
RA   Leader D.P., Gall I., Campbell P.C.;
RT   "The structure of a cDNA clone corresponding to mouse cardiac muscle
RT   actin mRNA.";
RL   Biosci. Rep. 6:741-747(1986).
RN   [4]
RP   PROTEIN SEQUENCE OF 71-97 AND 241-256, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC       alpha, beta and gamma have been identified. The alpha actins are
CC       found in muscle tissues and are a major constituent of the
CC       contractile apparatus. The beta and gamma actins coexist in most
CC       cell types as components of the cytoskeleton and as mediators of
CC       internal cell motility.
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK014303; BAB29258.1; -; mRNA.
DR   EMBL; BC062138; AAH62138.1; -; mRNA.
DR   EMBL; M15501; AAA37167.1; -; mRNA.
DR   IPI; IPI00114593; -.
DR   PIR; A54728; A54728.
DR   RefSeq; NP_033738.1; NM_009608.3.
DR   UniGene; Mm.686; -.
DR   ProteinModelPortal; P68033; -.
DR   SMR; P68033; 6-377.
DR   IntAct; P68033; 2.
DR   STRING; P68033; -.
DR   PhosphoSite; P68033; -.
DR   PRIDE; P68033; -.
DR   Ensembl; ENSMUST00000090269; ENSMUSP00000087736; ENSMUSG00000068614.
DR   GeneID; 11464; -.
DR   KEGG; mmu:11464; -.
DR   UCSC; uc008lpz.1; mouse.
DR   CTD; 11464; -.
DR   MGI; MGI:87905; Actc1.
DR   HOGENOM; HBG559892; -.
DR   HOVERGEN; HBG003771; -.
DR   InParanoid; P68033; -.
DR   OMA; MWISKEY; -.
DR   OrthoDB; EOG4W9J40; -.
DR   PhylomeDB; P68033; -.
DR   NextBio; 278788; -.
DR   ArrayExpress; P68033; -.
DR   Bgee; P68033; -.
DR   CleanEx; MM_ACTC1; -.
DR   Genevestigator; P68033; -.
DR   GermOnline; ENSMUSG00000068614; Mus musculus.
DR   GO; GO:0031674; C:I band; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptosis; IMP:MGI.
DR   GO; GO:0055008; P:cardiac muscle tissue morphogenesis; IMP:MGI.
DR   GO; GO:0055003; P:cardiac myofibril assembly; IMP:MGI.
DR   GO; GO:0030240; P:skeletal muscle thin filament assembly; IMP:MGI.
DR   InterPro; IPR004000; Actin-like.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Methylation; Muscle protein;
KW   Nucleotide-binding.
FT   PROPEP        1      2       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000000814.
FT   CHAIN         3    377       Actin, alpha cardiac muscle 1.
FT                                /FTId=PRO_0000000815.
FT   MOD_RES       3      3       N-acetylaspartate (By similarity).
FT   MOD_RES      75     75       Tele-methylhistidine (By similarity).
SQ   SEQUENCE   377 AA;  42019 MW;  E5C10FA19730CAD2 CRC64;
     MCDDEETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
     QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK
     MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL
     DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK
     SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
     LSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIS
     KQEYDEAGPS IVHRKCF
//
ID   ACTS_MOUSE              Reviewed;         377 AA.
AC   P68134; P02568; P99020;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Actin, alpha skeletal muscle;
DE   AltName: Full=Alpha-actin-1;
GN   Name=Acta1; Synonyms=Acta;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=86246890; PubMed=3013550;
RA   Leader D.P., Gall I., Campbell P.C., Frischauf A.-M.;
RT   "Isolation and characterization of cDNA clones from mouse skeletal
RT   muscle actin mRNA.";
RL   DNA 5:235-238(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=87064281; PubMed=3023820;
RA   Hu M.C.-T., Sharp S.B., Davidson N.;
RT   "The complete sequence of the mouse skeletal alpha-actin gene reveals
RT   several conserved and inverted repeat sequences outside of the
RT   protein-coding region.";
RL   Mol. Cell. Biol. 6:15-25(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-93, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-55; TYR-93 AND TYR-242,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells.
CC   -!- SUBUNIT: Polymerization of globular actin (G-actin) leads to a
CC       structural filament (F-actin) in the form of a two-stranded helix.
CC       Each actin can bind to 4 others. Interacts with TTID. Interacts
CC       (via its C-terminus) with USP25; the interaction occurs for all
CC       USP25 isoforms but is strongest for isoform USP25m in muscle
CC       differentiating cells (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms,
CC       alpha, beta and gamma have been identified. The alpha actins are
CC       found in muscle tissues and are a major constituent of the
CC       contractile apparatus. The beta and gamma actins coexist in most
CC       cell types as components of the cytoskeleton and as mediators of
CC       internal cell motility.
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M12866; AAA37164.1; -; mRNA.
DR   EMBL; M12347; AAA37141.1; -; Genomic_DNA.
DR   EMBL; BC014877; AAH14877.1; -; mRNA.
DR   IPI; IPI00110827; -.
DR   PIR; A24904; A24904.
DR   RefSeq; NP_033736.1; NM_009606.2.
DR   UniGene; Mm.214950; -.
DR   ProteinModelPortal; P68134; -.
DR   SMR; P68134; 6-377.
DR   STRING; P68134; -.
DR   PhosphoSite; P68134; -.
DR   PRIDE; P68134; -.
DR   Ensembl; ENSMUST00000034453; ENSMUSP00000034453; ENSMUSG00000031972.
DR   GeneID; 11459; -.
DR   KEGG; mmu:11459; -.
DR   UCSC; uc009nwr.1; mouse.
DR   CTD; 11459; -.
DR   MGI; MGI:87902; Acta1.
DR   eggNOG; roNOG14612; -.
DR   HOGENOM; HBG559892; -.
DR   HOVERGEN; HBG003771; -.
DR   InParanoid; P68134; -.
DR   OMA; FVGMESA; -.
DR   OrthoDB; EOG4W9J40; -.
DR   PhylomeDB; P68134; -.
DR   NextBio; 278780; -.
DR   ArrayExpress; P68134; -.
DR   Bgee; P68134; -.
DR   CleanEx; MM_ACTA1; -.
DR   Genevestigator; P68134; -.
DR   GermOnline; ENSMUSG00000031972; Mus musculus.
DR   GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR   GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
DR   GO; GO:0005865; C:striated muscle thin filament; TAS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0048741; P:skeletal muscle fiber development; IDA:UniProtKB.
DR   GO; GO:0030240; P:skeletal muscle thin filament assembly; ISS:UniProtKB.
DR   InterPro; IPR004000; Actin-like.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Methylation;
KW   Muscle protein; Nucleotide-binding; Phosphoprotein.
FT   PROPEP        1      2       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000000846.
FT   CHAIN         3    377       Actin, alpha skeletal muscle.
FT                                /FTId=PRO_0000000847.
FT   MOD_RES       3      3       N-acetylaspartate (By similarity).
FT   MOD_RES      55     55       Phosphotyrosine.
FT   MOD_RES      63     63       N6-acetyllysine (By similarity).
FT   MOD_RES      70     70       N6-acetyllysine (By similarity).
FT   MOD_RES      75     75       Tele-methylhistidine (By similarity).
FT   MOD_RES      93     93       Phosphotyrosine.
FT   MOD_RES     193    193       N6-acetyllysine (By similarity).
FT   MOD_RES     242    242       Phosphotyrosine.
FT   MOD_RES     328    328       N6-acetyllysine (By similarity).
FT   MOD_RES     330    330       N6-acetyllysine (By similarity).
SQ   SEQUENCE   377 AA;  42051 MW;  DF2A3A046346A179 CRC64;
     MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG QKDSYVGDEA
     QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP EEHPTLLTEA PLNPKANREK
     MTQIMFETFN VPAMYVAIQA VLSLYASGRT TGIVLDSGDG VTHNVPIYEG YALPHAIMRL
     DLAGRDLTDY LMKILTERGY SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK
     SYELPDGQVI TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
     MSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS LSTFQQMWIT
     KQEYDEAGPS IVHRKCF
//
ID   KAPCB_MOUSE             Reviewed;         351 AA.
AC   P68181; P05206; Q3TQH5; Q3UDD0; Q3UTH5;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=cAMP-dependent protein kinase catalytic subunit beta;
DE            Short=PKA C-beta;
DE            EC=2.7.11.11;
GN   Name=Prkacb; Synonyms=Pkacb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=87057152; PubMed=3023318;
RA   Uhler M.D., Chrivia J.C., McKnight G.S.;
RT   "Evidence for a second isoform of the catalytic subunit of cAMP-
RT   dependent protein kinase.";
RL   J. Biol. Chem. 261:15360-15363(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Adrenal gland, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15 (ISOFORM 1).
RX   MEDLINE=88186891; PubMed=2833513;
RA   Chrivia J.C., Uhler M.D., McKnight G.S.;
RT   "Characterization of genomic clones coding for the C alpha and C beta
RT   subunits of mouse cAMP-dependent protein kinase.";
RL   J. Biol. Chem. 263:5739-5744(1988).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7 (ISOFORM 2), NUCLEOTIDE
RP   SEQUENCE [GENOMIC DNA] OF 1-8 (ISOFORM 3), FUNCTION, MYRISTOYLATION AT
RP   GLY-2, AND TISSUE SPECIFICITY.
RX   PubMed=9368018; DOI=10.1074/jbc.272.47.29560;
RA   Guthrie C.R., Skalhegg B.S., McKnight G.S.;
RT   "Two novel brain-specific splice variants of the murine Cbeta gene of
RT   cAMP-dependent protein kinase.";
RL   J. Biol. Chem. 272:29560-29565(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 281-351.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   PubMed=12106288; DOI=10.1111/j.1460-9568.1990.tb00460.x;
RA   Kato K.;
RT   "A collection of cDNA clones with specific expression patterns in
RT   mouse brain.";
RL   Eur. J. Neurosci. 2:704-711(1990).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-69, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-198, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-198, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Mediates cAMP-dependent signaling triggered by receptor
CC       binding to GPCRs. PKA activation regulates diverse cellular
CC       processes such as cell proliferation, the cell cycle,
CC       differentiation and regulation of microtubule dynamics, chromatin
CC       condensation and decondensation, nuclear envelope disassembly and
CC       reassembly, as well as regulation of intracellular transport
CC       mechanisms and ion flux.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: Activated by cAMP.
CC   -!- SUBUNIT: A number of inactive tetrameric holoenzymes are produced
CC       by the combination of homo- or heterodimers of the different
CC       regulatory subunits associated with two catalytic subunits. cAMP
CC       causes the dissociation of the inactive holoenzyme into a dimer of
CC       regulatory subunits bound to four cAMP and two free monomeric
CC       catalytic subunits.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Translocates into the nucleus (monomeric
CC       catalytic subunit) (By similarity). The inactive holoenzyme is
CC       found in the cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=Beta1;
CC         IsoId=P68181-1; Sequence=Displayed;
CC       Name=2; Synonyms=Beta2;
CC         IsoId=P68181-2; Sequence=VSP_017373, VSP_017374;
CC       Name=3; Synonyms=Beta3;
CC         IsoId=P68181-3; Sequence=VSP_017372, VSP_017375;
CC       Name=4;
CC         IsoId=P68181-4; Sequence=VSP_017376;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is found in all tissues examined,
CC       with the highest expression in the brain and very low levels in
CC       the testis. Isoform 2 is strongly expressed in the brain, in the
CC       prelimbic and insular cortex. Isoform 3 is also found only in the
CC       brain, but at very low levels.
CC   -!- PTM: Asn-3 is deaminated to Asp in more than 25% of the proteins,
CC       giving rise to 2 major isoelectric variants, called CB and CA
CC       respectively (0.4 pH unit change). Deamidation proceeds via the
CC       so-called beta-aspartyl shift mechanism and yields either 'D-Asp-
CC       2' (major) or 'D-isoAsp-2' (minor), in addition to L-isomers.
CC       Deamidation occurs after the addition of myristate. The Asn-3 form
CC       reaches a significantly larger nuclear/cytoplasmic ratio than the
CC       'Asp-2' form (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. cAMP subfamily.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; J02626; AAA39941.1; -; mRNA.
DR   EMBL; AK048319; BAC33301.1; -; mRNA.
DR   EMBL; AK139419; BAE24005.1; -; mRNA.
DR   EMBL; AK148728; BAE28648.1; -; mRNA.
DR   EMBL; AK150122; BAE29323.1; -; mRNA.
DR   EMBL; AK150134; BAE29331.1; -; mRNA.
DR   EMBL; AK163585; BAE37407.1; -; mRNA.
DR   EMBL; BC054533; AAH54533.1; -; mRNA.
DR   EMBL; M21096; AAA39938.1; -; Genomic_DNA.
DR   EMBL; AF022239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; X61434; CAA43676.1; -; mRNA.
DR   IPI; IPI00263822; -.
DR   IPI; IPI00742329; -.
DR   IPI; IPI00742400; -.
DR   IPI; IPI00742438; -.
DR   PIR; A24596; OKMSCB.
DR   RefSeq; NP_001157670.1; NM_001164198.1.
DR   RefSeq; NP_001157671.1; NM_001164199.1.
DR   RefSeq; NP_001157672.1; NM_001164200.1.
DR   RefSeq; NP_035230.1; NM_011100.4.
DR   UniGene; Mm.16766; -.
DR   ProteinModelPortal; P68181; -.
DR   SMR; P68181; 14-351.
DR   STRING; P68181; -.
DR   PRIDE; P68181; -.
DR   Ensembl; ENSMUST00000005164; ENSMUSP00000005164; ENSMUSG00000005034.
DR   Ensembl; ENSMUST00000102515; ENSMUSP00000099573; ENSMUSG00000005034.
DR   Ensembl; ENSMUST00000106140; ENSMUSP00000101746; ENSMUSG00000005034.
DR   GeneID; 18749; -.
DR   KEGG; mmu:18749; -.
DR   UCSC; uc008rrs.1; mouse.
DR   UCSC; uc008rrt.1; mouse.
DR   UCSC; uc008rru.1; mouse.
DR   UCSC; uc008rrv.1; mouse.
DR   CTD; 18749; -.
DR   MGI; MGI:97594; Prkacb.
DR   eggNOG; roNOG14656; -.
DR   HOVERGEN; HBG108317; -.
DR   OMA; MAAHKEL; -.
DR   OrthoDB; EOG4RXZ0C; -.
DR   PhylomeDB; P68181; -.
DR   BRENDA; 2.7.11.11; 244.
DR   NextBio; 294913; -.
DR   ArrayExpress; P68181; -.
DR   Bgee; P68181; -.
DR   CleanEx; MM_PRKACB; -.
DR   Genevestigator; P68181; -.
DR   GermOnline; ENSMUSG00000005034; Mus musculus.
DR   GO; GO:0005952; C:cAMP-dependent protein kinase complex; TAS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0004691; F:cAMP-dependent protein kinase activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0007188; P:G-protein signaling, coupled to cAMP nucleotide second messenger; TAS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; cAMP; Cytoplasm;
KW   Kinase; Lipoprotein; Myristate; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    351       cAMP-dependent protein kinase catalytic
FT                                subunit beta.
FT                                /FTId=PRO_0000086061.
FT   DOMAIN       44    298       Protein kinase.
FT   DOMAIN      299    351       AGC-kinase C-terminal.
FT   NP_BIND      50     58       ATP (By similarity).
FT   ACT_SITE    167    167       Proton acceptor (By similarity).
FT   BINDING      73     73       ATP (By similarity).
FT   MOD_RES       3      3       Deamidated asparagine (By similarity).
FT   MOD_RES      69     69       Phosphotyrosine.
FT   MOD_RES     198    198       Phosphothreonine.
FT   MOD_RES     267    267       N6-acetyllysine (By similarity).
FT   MOD_RES     339    339       Phosphoserine (By similarity).
FT   LIPID         2      2       N-myristoyl glycine.
FT   VAR_SEQ       1     16       MGNTAIAKKGSEVESV -> MAAHKELSSGQHSGTPTALQK
FT                                LEGFASRLFHRHSRGTAQEHRAALEDDGLRASEHTASWDKS
FT                                M (in isoform 4).
FT                                /FTId=VSP_017376.
FT   VAR_SEQ       1     13       Missing (in isoform 2).
FT                                /FTId=VSP_017373.
FT   VAR_SEQ       1     12       Missing (in isoform 3).
FT                                /FTId=VSP_017372.
FT   VAR_SEQ      13     16       VESV -> MGLL (in isoform 3).
FT                                /FTId=VSP_017375.
FT   VAR_SEQ      14     15       ES -> MN (in isoform 2).
FT                                /FTId=VSP_017374.
SQ   SEQUENCE   351 AA;  40708 MW;  EBAC9B8041DF9F47 CRC64;
     MGNTAIAKKG SEVESVKEFL AKAKEDFLRK WENPPPSNAG LEDFERKKTL GTGSFGRVML
     VKHKATEQYY AMKILDKQKV VKLKQIEHTL NEKRILQAVE FPFLVRLEYS FKDNSNLYMV
     MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDHQGY
     IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF
     ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVS DIKTHKWFAT
     TDWIAIYQRK VEAPFIPKFR GSGDTSNFDD YEEEEIRVSI TEKCGKEFCE F
//
ID   1433T_MOUSE             Reviewed;         245 AA.
AC   P68254; P35216; Q3TW69; Q3UJN5; Q5SP76; Q5U423; Q66JR6;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=14-3-3 protein theta;
DE   AltName: Full=14-3-3 protein tau;
GN   Name=Ywhaq;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH CDK16.
RC   TISSUE=Brain;
RX   MEDLINE=97340943; PubMed=9197417; DOI=10.1007/s004380050453;
RA   Sladeczek F., Camonis J.H., Burnol A.-F., Le Bouffant F.;
RT   "The Cdk-like protein PCTAIRE-1 from mouse brain associates with p11
RT   and 14-3-3 proteins.";
RL   Mol. Gen. Genet. 254:571-577(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=97355226; PubMed=9211421;
RX   DOI=10.1002/(SICI)1098-2795(199708)47:4<370::AID-MRD3>3.3.CO;2-W;
RA   Perego L., Berruti G.;
RT   "Molecular cloning and tissue-specific expression of the mouse
RT   homologue of the rat brain 14-3-3 theta protein: characterization of
RT   its cellular and developmental pattern of expression in the male germ
RT   line.";
RL   Mol. Reprod. Dev. 47:370-379(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=129/Sv;
RA   Takihara Y., Irie K., Nomura M., Motaleb M., Matsumoto K., Shimada K.;
RT   "14-3-3 family members play an important role in tumorigenic
RT   transformation of NIH 3T3 cells and retinoic acid-mediated F9 cell
RT   differentiation.";
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Amnion, Blastocyst, Bone marrow, and Egg;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and FVB/N;
RC   TISSUE=Brain, Mammary tumor, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 12-49; 61-68; 75-80; 84-115; 128-167 AND 194-245,
RP   AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC       spectrum of both general and specialized signaling pathway. Binds
CC       to a large number of partners, usually by recognition of a
CC       phosphoserine or phosphothreonine motif. Binding generally results
CC       in the modulation of the activity of the binding partner.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with CDKN1B ('Thr-
CC       198' phosphorylated form); the interaction translocates CDKN1B to
CC       the cytoplasm. Interacts with SSH1 (By similarity). Interacts with
CC       GAB2 (By similarity). Interacts with CDK16.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P68254-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P68254-2; Sequence=VSP_016340;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the 14-3-3 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH80802.1; Type=Erroneous initiation;
CC       Sequence=AAH85299.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; U57312; AAC53257.1; -; mRNA.
DR   EMBL; U56243; AAB72023.1; -; mRNA.
DR   EMBL; D87662; BAA13423.1; -; mRNA.
DR   EMBL; AK145568; BAE26517.1; -; mRNA.
DR   EMBL; AK146371; BAE27120.1; -; mRNA.
DR   EMBL; AK150850; BAE29907.1; -; mRNA.
DR   EMBL; AK151437; BAE30400.1; -; mRNA.
DR   EMBL; AK151715; BAE30634.1; -; mRNA.
DR   EMBL; AK151864; BAE30752.1; -; mRNA.
DR   EMBL; AK159403; BAE35055.1; -; mRNA.
DR   EMBL; AK159817; BAE35397.1; -; mRNA.
DR   EMBL; AK163237; BAE37249.1; -; mRNA.
DR   EMBL; AK167397; BAE39486.1; -; mRNA.
DR   EMBL; AL929409; CAI25590.1; -; Genomic_DNA.
DR   EMBL; BC080802; AAH80802.1; ALT_INIT; mRNA.
DR   EMBL; BC085299; AAH85299.1; ALT_INIT; mRNA.
DR   EMBL; BC090838; AAH90838.1; -; mRNA.
DR   EMBL; BC106164; AAI06165.1; -; mRNA.
DR   IPI; IPI00408378; -.
DR   IPI; IPI00656269; -.
DR   RefSeq; NP_035869.1; NM_011739.3.
DR   RefSeq; XP_003085850.1; XM_003085802.1.
DR   RefSeq; XP_003085851.1; XM_003085803.1.
DR   RefSeq; XP_003085852.1; XM_003085804.1.
DR   RefSeq; XP_003085853.1; XM_003085805.1.
DR   RefSeq; XP_003085854.1; XM_003085806.1.
DR   UniGene; Mm.289630; -.
DR   UniGene; Mm.458320; -.
DR   ProteinModelPortal; P68254; -.
DR   SMR; P68254; 1-230.
DR   STRING; P68254; -.
DR   PhosphoSite; P68254; -.
DR   REPRODUCTION-2DPAGE; P68254; -.
DR   PRIDE; P68254; -.
DR   Ensembl; ENSMUST00000049531; ENSMUSP00000106602; ENSMUSG00000076432.
DR   Ensembl; ENSMUST00000103002; ENSMUSP00000100067; ENSMUSG00000076432.
DR   Ensembl; ENSMUST00000110976; ENSMUSP00000106604; ENSMUSG00000076432.
DR   GeneID; 100503129; -.
DR   GeneID; 22630; -.
DR   KEGG; mmu:100503129; -.
DR   KEGG; mmu:22630; -.
DR   UCSC; uc007ndw.1; mouse.
DR   UCSC; uc007ndx.1; mouse.
DR   CTD; 22630; -.
DR   MGI; MGI:891963; Ywhaq.
DR   GeneTree; ENSGT00550000074221; -.
DR   HOVERGEN; HBG050423; -.
DR   InParanoid; P68254; -.
DR   OMA; SGDDRKQ; -.
DR   OrthoDB; EOG480HXJ; -.
DR   PhylomeDB; P68254; -.
DR   NextBio; 302999; -.
DR   ArrayExpress; P68254; -.
DR   Bgee; P68254; -.
DR   Genevestigator; P68254; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019904; F:protein domain specific binding; IDA:MGI.
DR   GO; GO:0006605; P:protein targeting; IDA:MGI.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IPI:MGI.
DR   InterPro; IPR000308; 14-3-3.
DR   PANTHER; PTHR18860; 14-3-3; 1.
DR   PIRSF; PIRSF000868; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm;
KW   Direct protein sequencing; Phosphoprotein.
FT   CHAIN         1    245       14-3-3 protein theta.
FT                                /FTId=PRO_0000058637.
FT   SITE         56     56       Interaction with phosphoserine on
FT                                interacting protein (By similarity).
FT   SITE        127    127       Interaction with phosphoserine on
FT                                interacting protein (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES       3      3       N6-acetyllysine (By similarity).
FT   MOD_RES      49     49       N6-acetyllysine (By similarity).
FT   MOD_RES      68     68       N6-acetyllysine (By similarity).
FT   MOD_RES     115    115       N6-acetyllysine (By similarity).
FT   MOD_RES     232    232       Phosphoserine; by CK1 (Probable).
FT   VAR_SEQ     227    245       LWTSDSAGEECDAAEGAEN -> FTCVELETVSVCFSLLS
FT                                (in isoform 2).
FT                                /FTId=VSP_016340.
FT   CONFLICT     26     26       M -> I (in Ref. 4; BAE35397).
FT   CONFLICT    227    227       L -> S (in Ref. 4; BAE27120).
SQ   SEQUENCE   245 AA;  27778 MW;  E30471260E8B366E CRC64;
     MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR
     VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK
     MKGDYFRYLA EVACGDDRKQ TIENSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE
     ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA
     EGAEN
//
ID   TBA4A_MOUSE             Reviewed;         448 AA.
AC   P68368; P05215; Q3TY31;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Tubulin alpha-4A chain;
DE   AltName: Full=Alpha-tubulin 4;
DE   AltName: Full=Alpha-tubulin isotype M-alpha-4;
DE   AltName: Full=Tubulin alpha-4 chain;
GN   Name=Tuba4a; Synonyms=Tuba4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=87064538; PubMed=3785200;
RA   Villasante A., Wang D., Dobner P., Dolph P., Lewis S.A., Cowan N.J.;
RT   "Six mouse alpha-tubulin mRNAs encode five distinct isotypes: testis-
RT   specific expression of two sister genes.";
RL   Mol. Cell. Biol. 6:2409-2419(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Kidney, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 65-79; 85-121; 157-163; 216-304; 312-320; 327-336;
RP   340-370; 374-390; 395-401 AND 403-430, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   NITRATION [LARGE SCALE ANALYSIS] AT TYR-83, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16800626; DOI=10.1021/bi060474w;
RA   Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
RA   Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
RA   Squier T.C., Bigelow D.J.;
RT   "Endogenously nitrated proteins in mouse brain: links to
RT   neurodegenerative disease.";
RL   Biochemistry 45:8009-8022(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RA   Lubec G., Kang S.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-319, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [8]
RP   POLYGLUTAMYLATION.
RX   PubMed=15890843; DOI=10.1126/science.1113010;
RA   Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M.,
RA   Temurak N., van Dijk J., Boucher D., van Dorsselaer A.,
RA   Suryavanshi S., Gaertig J., Edde B.;
RT   "Tubulin polyglutamylase enzymes are members of the TTL domain protein
RT   family.";
RL   Science 308:1758-1762(2005).
RN   [9]
RP   POLYGLYCYLATION.
RX   PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA   Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M.,
RA   Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J.,
RA   Janke C.;
RT   "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT   polyglycylation.";
RL   Cell 137:1076-1087(2009).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. It
CC       binds two moles of GTP, one at an exchangeable site on the beta
CC       chain and one at a non-exchangeable site on the alpha-chain.
CC   -!- SUBUNIT: Dimer of alpha and beta chains.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- PTM: Some glutamate residues at the C-terminus are either
CC       polyglutamylated or polyglycylated. These 2 modifications occur
CC       exclusively on glutamate residues and result in either
CC       polyglutamate or polyglycine chains on the gamma-carboxyl group.
CC       Glycylation is mainly limited to tubulin incorporated into
CC       axonemes (cilia and flagella) whereas glutamylation is prevalent
CC       in neuronal cells, centrioles, axonemes, and the mitotic spindle.
CC       Both modifications can coexist on the same protein on adjacent
CC       residues, and lowering polyglycylation levels increases
CC       polyglutamylation, and reciprocally. The precise function of such
CC       modifications is still unclear but they are regulate the assembly
CC       and dynamics of axonemal microtubules.
CC   -!- PTM: Acetylation of alpha-tubulins at Lys-40 stabilizes
CC       microtubules and affects affinity and processivity of microtubule
CC       motors. This modification has a role in multiple cellular
CC       functions, ranging from cell motility, cell cycle progression or
CC       cell differentiation to intracellular trafficking and signaling
CC       (By similarity).
CC   -!- MISCELLANEOUS: This tubulin does not have a C-terminal tyrosine.
CC   -!- SIMILARITY: Belongs to the tubulin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE34732.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; M13444; AAA40502.1; -; mRNA.
DR   EMBL; AK002427; BAB22094.1; -; mRNA.
DR   EMBL; AK078355; BAC37234.1; -; mRNA.
DR   EMBL; AK158934; BAE34732.1; ALT_INIT; mRNA.
DR   EMBL; BC019959; AAH19959.1; -; mRNA.
DR   IPI; IPI00117350; -.
DR   PIR; I77427; I77427.
DR   RefSeq; NP_033473.1; NM_009447.3.
DR   UniGene; Mm.1155; -.
DR   ProteinModelPortal; P68368; -.
DR   SMR; P68368; 1-439.
DR   MINT; MINT-136355; -.
DR   STRING; P68368; -.
DR   PhosphoSite; P68368; -.
DR   PRIDE; P68368; -.
DR   Ensembl; ENSMUST00000079464; ENSMUSP00000078429; ENSMUSG00000026202.
DR   GeneID; 22145; -.
DR   KEGG; mmu:22145; -.
DR   UCSC; uc007bok.1; mouse.
DR   CTD; 22145; -.
DR   MGI; MGI:1095410; Tuba4a.
DR   eggNOG; roNOG14794; -.
DR   GeneTree; ENSGT00600000084100; -.
DR   HOGENOM; HBG750007; -.
DR   HOVERGEN; HBG000089; -.
DR   InParanoid; P68368; -.
DR   OMA; RGGVYRQ; -.
DR   OrthoDB; EOG44J2HZ; -.
DR   PhylomeDB; P68368; -.
DR   NextBio; 302050; -.
DR   ArrayExpress; P68368; -.
DR   Bgee; P68368; -.
DR   CleanEx; MM_TUBA4A; -.
DR   Genevestigator; P68368; -.
DR   GermOnline; ENSMUSG00000026202; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR   InterPro; IPR002452; Alpha_tubulin.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR023123; Tubulin_C.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   Gene3D; G3DSA:3.30.1330.20; Tubulin/FtsZ_2-layer-sand-dom; 1.
DR   Gene3D; G3DSA:1.10.287.600; Tubulin_C; 1.
DR   Gene3D; G3DSA:3.40.50.1440; Tubulin_FtsZ; 1.
DR   PANTHER; PTHR11588; Tubulin; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01162; ALPHATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF55307; Tub_FtsZ_C; 1.
DR   SUPFAM; SSF52490; Tubulin_FtsZ; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   GTP-binding; Microtubule; Nitration; Nucleotide-binding;
KW   Phosphoprotein.
FT   CHAIN         1    448       Tubulin alpha-4A chain.
FT                                /FTId=PRO_0000048123.
FT   NP_BIND     142    148       GTP (Potential).
FT   MOD_RES      40     40       N6-acetyllysine (By similarity).
FT   MOD_RES      48     48       Phosphoserine (By similarity).
FT   MOD_RES      83     83       Nitrated tyrosine.
FT   MOD_RES     161    161       Phosphotyrosine (By similarity).
FT   MOD_RES     163    163       N6-acetyllysine (By similarity).
FT   MOD_RES     232    232       Phosphoserine.
FT   MOD_RES     311    311       N6-acetyllysine (By similarity).
FT   MOD_RES     319    319       Phosphotyrosine.
FT   MOD_RES     340    340       Phosphoserine (By similarity).
FT   MOD_RES     439    439       Phosphoserine (By similarity).
FT   MOD_RES     440    440       Phosphotyrosine (By similarity).
FT   CONFLICT      1      1       M -> G (in Ref. 2; BAE34732).
SQ   SEQUENCE   448 AA;  49924 MW;  C00ED90A183FE8F2 CRC64;
     MRECISVHVG QAGVQMGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFT TFFCETGAGK
     HVPRAVFVDL EPTVIDEIRN GPYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDPVLD
     RIRKLSDQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA
     VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL ISQIVSSITA
     SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
     QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIAAIKTKRS IQFVDWCPTG FKVGINYQPP
     TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
     AREDMAALEK DYEEVGIDSY EDEDEGEE
//
ID   TBA1A_MOUSE             Reviewed;         451 AA.
AC   P68369; P02551; P05210; P05212; Q3TGF0; Q3TIW2; Q3TPJ1; Q3ULN1;
AC   Q5XJF8;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Tubulin alpha-1A chain;
DE   AltName: Full=Alpha-tubulin 1;
DE   AltName: Full=Alpha-tubulin isotype M-alpha-1;
DE   AltName: Full=Tubulin alpha-1 chain;
GN   Name=Tuba1a; Synonyms=Tuba1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=87064538; PubMed=3785200;
RA   Villasante A., Wang D., Dobner P., Dolph P., Lewis S.A., Cowan N.J.;
RT   "Six mouse alpha-tubulin mRNAs encode five distinct isotypes: testis-
RT   specific expression of two sister genes.";
RL   Mol. Cell. Biol. 6:2409-2419(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Heart, Kidney, Placenta, Spinal ganglion, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 41-60; 65-79; 85-121; 157-163; 216-280; 312-320;
RP   327-336; 340-370; 374-401 AND 403-440, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 254-451.
RX   MEDLINE=85289512; PubMed=3839797; DOI=10.1083/jcb.101.3.852;
RA   Lewis S.A., Lee M.G.-S., Cowan N.J.;
RT   "Five mouse tubulin isotypes and their regulated expression during
RT   development.";
RL   J. Cell Biol. 101:852-861(1985).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   POLYGLUTAMYLATION.
RX   PubMed=15890843; DOI=10.1126/science.1113010;
RA   Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M.,
RA   Temurak N., van Dijk J., Boucher D., van Dorsselaer A.,
RA   Suryavanshi S., Gaertig J., Edde B.;
RT   "Tubulin polyglutamylase enzymes are members of the TTL domain protein
RT   family.";
RL   Science 308:1758-1762(2005).
RN   [8]
RP   POLYGLYCYLATION.
RX   PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA   Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M.,
RA   Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J.,
RA   Janke C.;
RT   "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT   polyglycylation.";
RL   Cell 137:1076-1087(2009).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. It
CC       binds two moles of GTP, one at an exchangeable site on the beta
CC       chain and one at a non-exchangeable site on the alpha-chain.
CC   -!- SUBUNIT: Dimer of alpha and beta chains.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed, although primarily in
CC       lung and brain.
CC   -!- PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic
CC       removal and re-addition of a C-terminal tyrosine residue by the
CC       enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin
CC       tyrosine ligase (TTL), respectively (By similarity).
CC   -!- PTM: Some glutamate residues at the C-terminus are either
CC       polyglutamylated or polyglycylated. These 2 modifications occur
CC       exclusively on glutamate residues and result in either
CC       polyglutamate or polyglycine chains on the gamma-carboxyl group.
CC       Glycylation is mainly limited to tubulin incorporated into
CC       axonemes (cilia and flagella) whereas glutamylation is prevalent
CC       in neuronal cells, centrioles, axonemes, and the mitotic spindle.
CC       Both modifications can coexist on the same protein on adjacent
CC       residues, and lowering polyglycylation levels increases
CC       polyglutamylation, and reciprocally. The precise function of such
CC       modifications is still unclear but they are regulate the assembly
CC       and dynamics of axonemal microtubules.
CC   -!- PTM: Acetylation of alpha-tubulins at Lys-40 stabilizes
CC       microtubules and affects affinity and processivity of microtubule
CC       motors. This modification has a role in multiple cellular
CC       functions, ranging from cell motility, cell cycle progression or
CC       cell differentiation to intracellular trafficking and signaling
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the tubulin family.
CC   -----------------------------------------------------------------------
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DR   EMBL; M13445; AAA40499.1; -; mRNA.
DR   EMBL; AK077529; BAC36848.1; -; mRNA.
DR   EMBL; AK145404; BAE26417.1; -; mRNA.
DR   EMBL; AK146983; BAE27586.1; -; mRNA.
DR   EMBL; AK164335; BAE37745.1; -; mRNA.
DR   EMBL; AK167687; BAE39734.1; -; mRNA.
DR   EMBL; AK168762; BAE40598.1; -; mRNA.
DR   EMBL; AK169610; BAE41258.1; -; mRNA.
DR   EMBL; BC056169; AAH56169.1; -; mRNA.
DR   EMBL; BC083343; AAH83343.1; -; mRNA.
DR   EMBL; BC083345; AAH83345.1; -; mRNA.
DR   EMBL; BC085256; AAH85256.1; -; mRNA.
DR   EMBL; M28729; AAA40506.1; -; mRNA.
DR   EMBL; BC083344; AAH83344.1; -; mRNA.
DR   IPI; IPI00110753; -.
DR   PIR; I77424; I77424.
DR   RefSeq; NP_035783.1; NM_011653.2.
DR   UniGene; Mm.439690; -.
DR   ProteinModelPortal; P68369; -.
DR   SMR; P68369; 1-440.
DR   IntAct; P68369; 12.
DR   MINT; MINT-3288915; -.
DR   STRING; P68369; -.
DR   PhosphoSite; P68369; -.
DR   SWISS-2DPAGE; P68369; -.
DR   PRIDE; P68369; -.
DR   Ensembl; ENSMUST00000097014; ENSMUSP00000094778; ENSMUSG00000072235.
DR   GeneID; 22142; -.
DR   KEGG; mmu:22142; -.
DR   UCSC; uc007xok.1; mouse.
DR   CTD; 22142; -.
DR   MGI; MGI:98869; Tuba1a.
DR   GeneTree; ENSGT00600000084100; -.
DR   HOVERGEN; HBG000089; -.
DR   InParanoid; P68369; -.
DR   OMA; KRATHES; -.
DR   OrthoDB; EOG44J2HZ; -.
DR   PhylomeDB; P68369; -.
DR   NextBio; 302038; -.
DR   PMAP-CutDB; P68369; -.
DR   ArrayExpress; P68369; -.
DR   Bgee; P68369; -.
DR   CleanEx; MM_TUBA1A; -.
DR   Genevestigator; P68369; -.
DR   GermOnline; ENSMUSG00000072235; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR   InterPro; IPR002452; Alpha_tubulin.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR023123; Tubulin_C.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   Gene3D; G3DSA:3.30.1330.20; Tubulin/FtsZ_2-layer-sand-dom; 1.
DR   Gene3D; G3DSA:1.10.287.600; Tubulin_C; 1.
DR   Gene3D; G3DSA:3.40.50.1440; Tubulin_FtsZ; 1.
DR   PANTHER; PTHR11588; Tubulin; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01162; ALPHATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF55307; Tub_FtsZ_C; 1.
DR   SUPFAM; SSF52490; Tubulin_FtsZ; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   GTP-binding; Microtubule; Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1    451       Tubulin alpha-1A chain.
FT                                /FTId=PRO_0000048120.
FT   NP_BIND     142    148       GTP (Potential).
FT   SITE        451    451       Involved in polymerization.
FT   MOD_RES       6      6       Phosphoserine.
FT   MOD_RES      40     40       N6-acetyllysine (By similarity).
FT   MOD_RES      48     48       Phosphoserine (By similarity).
FT   MOD_RES     272    272       Phosphotyrosine (By similarity).
FT   MOD_RES     439    439       Phosphoserine (By similarity).
FT   CONFLICT    124    124       K -> E (in Ref. 2; BAE40598).
FT   CONFLICT    132    132       L -> P (in Ref. 2; BAE26417).
FT   CONFLICT    257    257       T -> I (in Ref. 2; BAE37745).
FT   CONFLICT    273    273       A -> S (in Ref. 3; AAH83344).
FT   CONFLICT    328    328       V -> G (in Ref. 2; BAE26417).
SQ   SEQUENCE   451 AA;  50136 MW;  00F8429A4A10E5FE CRC64;
     MRECISIHVG QAGVQIGNAC WELYCLEHGI QPDGQMPSDK TIGGGDDSFN TFFSETGAGK
     HVPRAVFVDL EPTVIDEVRT GTYRQLFHPE QLITGKEDAA NNYARGHYTI GKEIIDLVLD
     RIRKLADQCT GLQGFLVFHS FGGGTGSGFT SLLMERLSVD YGKKSKLEFS IYPAPQVSTA
     VVEPYNSILT THTTLEHSDC AFMVDNEAIY DICRRNLDIE RPTYTNLNRL IGQIVSSITA
     SLRFDGALNV DLTEFQTNLV PYPRIHFPLA TYAPVISAEK AYHEQLSVAE ITNACFEPAN
     QMVKCDPRHG KYMACCLLYR GDVVPKDVNA AIATIKTKRT IQFVDWCPTG FKVGINYQPP
     TVVPGGDLAK VQRAVCMLSN TTAIAEAWAR LDHKFDLMYA KRAFVHWYVG EGMEEGEFSE
     AREDMAALEK DYEEVGVDSV EGEGEEEGEE Y
//
ID   TBB2C_MOUSE             Reviewed;         445 AA.
AC   P68372; P05217; Q3TKF0; Q3UJ73; Q99JZ6;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Tubulin beta-2C chain;
GN   Name=Tubb2c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=87057644; PubMed=3782288; DOI=10.1083/jcb.103.5.1903;
RA   Wang D., Villasante A., Lewis S.A., Cowan N.J.;
RT   "The mammalian beta-tubulin repertoire: hematopoietic expression of a
RT   novel, heterologous beta-tubulin isotype.";
RL   J. Cell Biol. 103:1903-1910(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 3-19; 47-58; 63-121; 163-174; 217-276; 283-297;
RP   310-318; 321-359; 363-379 AND 381-390, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   POLYGLUTAMYLATION.
RX   PubMed=15890843; DOI=10.1126/science.1113010;
RA   Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M.,
RA   Temurak N., van Dijk J., Boucher D., van Dorsselaer A.,
RA   Suryavanshi S., Gaertig J., Edde B.;
RT   "Tubulin polyglutamylase enzymes are members of the TTL domain protein
RT   family.";
RL   Science 308:1758-1762(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-51, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [8]
RP   POLYGLYCYLATION.
RX   PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA   Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M.,
RA   Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J.,
RA   Janke C.;
RT   "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT   polyglycylation.";
RL   Cell 137:1076-1087(2009).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. It
CC       binds two moles of GTP, one at an exchangeable site on the beta
CC       chain and one at a non-exchangeable site on the alpha-chain.
CC   -!- SUBUNIT: Dimer of alpha and beta chains.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- DOMAIN: The highly acidic C-terminal region may bind cations such
CC       as calcium.
CC   -!- PTM: Some glutamate residues at the C-terminus are either
CC       polyglutamylated or polyglycylated. These 2 modifications occur
CC       exclusively on glutamate residues and result in either
CC       polyglutamate or polyglycine chains on the gamma-carboxyl group.
CC       Glycylation is mainly limited to tubulin incorporated into
CC       axonemes (cilia and flagella) whereas glutamylation is prevalent
CC       in neuronal cells, centrioles, axonemes, and the mitotic spindle.
CC       Both modifications can coexist on the same protein on adjacent
CC       residues, and lowering polyglycylation levels increases
CC       polyglutamylation, and reciprocally. The precise function of such
CC       modifications is still unclear but they are regulate the assembly
CC       and dynamics of axonemal microtubules.
CC   -!- SIMILARITY: Belongs to the tubulin family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK146587; BAE27282.1; -; mRNA.
DR   EMBL; AK167022; BAE39195.1; -; mRNA.
DR   EMBL; AL732309; CAM14671.1; -; Genomic_DNA.
DR   EMBL; BC005547; AAH05547.1; -; mRNA.
DR   EMBL; BC022919; AAH22919.1; -; mRNA.
DR   EMBL; BC083319; AAH83319.1; -; mRNA.
DR   IPI; IPI00169463; -.
DR   PIR; C25437; C25437.
DR   RefSeq; NP_666228.1; NM_146116.2.
DR   UniGene; Mm.227260; -.
DR   UniGene; Mm.479538; -.
DR   ProteinModelPortal; P68372; -.
DR   SMR; P68372; 2-427.
DR   STRING; P68372; -.
DR   PhosphoSite; P68372; -.
DR   Cornea-2DPAGE; P05217; -.
DR   REPRODUCTION-2DPAGE; IPI00169463; -.
DR   REPRODUCTION-2DPAGE; P68372; -.
DR   UCD-2DPAGE; P05217; -.
DR   UCD-2DPAGE; P68372; -.
DR   PRIDE; P68372; -.
DR   Ensembl; ENSMUST00000043584; ENSMUSP00000042342; ENSMUSG00000036752.
DR   GeneID; 227613; -.
DR   KEGG; mmu:227613; -.
DR   UCSC; uc008iqs.1; mouse.
DR   CTD; 227613; -.
DR   MGI; MGI:1915472; Tubb2c.
DR   eggNOG; roNOG14625; -.
DR   HOGENOM; HBG750007; -.
DR   HOVERGEN; HBG000089; -.
DR   InParanoid; P68372; -.
DR   OMA; EVINDEH; -.
DR   OrthoDB; EOG4DFPNJ; -.
DR   PhylomeDB; P68372; -.
DR   NextBio; 378658; -.
DR   ArrayExpress; P68372; -.
DR   Bgee; P68372; -.
DR   CleanEx; MM_TUBB2C; -.
DR   Genevestigator; P68372; -.
DR   GermOnline; ENSMUSG00000036752; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0045298; C:tubulin complex; NAS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; NAS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR   InterPro; IPR013838; Beta-tubulin_BS.
DR   InterPro; IPR002453; Beta_tubulin.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR023123; Tubulin_C.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   Gene3D; G3DSA:3.30.1330.20; Tubulin/FtsZ_2-layer-sand-dom; 1.
DR   Gene3D; G3DSA:1.10.287.600; Tubulin_C; 1.
DR   Gene3D; G3DSA:3.40.50.1440; Tubulin_FtsZ; 1.
DR   PANTHER; PTHR11588; Tubulin; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01163; BETATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF55307; Tub_FtsZ_C; 1.
DR   SUPFAM; SSF52490; Tubulin_FtsZ; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
DR   PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   GTP-binding; Microtubule; Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1    445       Tubulin beta-2C chain.
FT                                /FTId=PRO_0000048249.
FT   NP_BIND     140    146       GTP (Potential).
FT   MOD_RES      51     51       Phosphotyrosine.
FT   MOD_RES      55     55       Phosphothreonine (By similarity).
FT   MOD_RES      58     58       N6-acetyllysine (By similarity).
FT   MOD_RES     172    172       Phosphoserine (By similarity).
FT   MOD_RES     322    322       Phosphoserine (By similarity).
FT   CONFLICT    207    207       L -> P (in Ref. 4; AAH05547).
FT   CONFLICT    342    342       V -> A (in Ref. 2; BAE27282).
SQ   SEQUENCE   445 AA;  49831 MW;  A552C52822AFA072 CRC64;
     MREIVHLQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLERINVY YNEATGGKYV
     PRAVLVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
     RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVV PSPKVSDTVV
     EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL
     RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
     AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG
     LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDATA EEEGEFEEEA EEEVA
//
ID   KPCB_MOUSE              Reviewed;         673 AA.
AC   P68404; A0JNZ5; P04410; P04411;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Protein kinase C beta type;
DE            Short=PKC-B;
DE            Short=PKC-beta;
DE            EC=2.7.11.13;
GN   Name=Prkcb; Synonyms=Pkcb, Prkcb1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR X Swiss Webster; TISSUE=Brain;
RX   MEDLINE=90384861; PubMed=2402470; DOI=10.1093/nar/18.17.5310;
RA   Tang Y.-M., Ashendel C.L.;
RT   "Isolation of cloned mouse protein kinase C beta-II cDNA and its
RT   sequence.";
RL   Nucleic Acids Res. 18:5310-5310(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=8670417; DOI=10.1126/science.273.5276.788;
RA   Leitges M., Schmedt C., Guinamard R., Davoust J., Schaal S.,
RA   Stabel S., Tarakhovsky A.;
RT   "Immunodeficiency in protein kinase cbeta-deficient mice.";
RL   Science 273:788-791(1996).
RN   [4]
RP   FUNCTION.
RX   MEDLINE=22065540; PubMed=12070292; DOI=10.1084/jem.20020408;
RA   Saijo K., Mecklenbrauker I., Santana A., Leitger M., Schmedt C.,
RA   Tarakhovsky A.;
RT   "Protein kinase C beta controls nuclear factor kappaB activation in B
RT   cells through selective regulation of the IkappaB kinase alpha.";
RL   J. Exp. Med. 195:1647-1652(2002).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12118249; DOI=10.1038/ni823;
RA   Su T.T., Guo B., Kawakami Y., Sommer K., Chae K., Humphries L.A.,
RA   Kato R.M., Kang S., Patrone L., Wall R., Teitell M., Leitges M.,
RA   Kawakami T., Rawlings D.J.;
RT   "PKC-beta controls I kappa B kinase lipid raft recruitment and
RT   activation in response to BCR signaling.";
RL   Nat. Immunol. 3:780-786(2002).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH CARD11.
RX   PubMed=16356855; DOI=10.1016/j.immuni.2005.09.014;
RA   Sommer K., Guo B., Pomerantz J.L., Bandaranayake A.D.,
RA   Moreno-Garcia M.E., Ovechkina Y.L., Rawlings D.J.;
RT   "Phosphorylation of the CARMA1 linker controls NF-kappaB activation.";
RL   Immunity 23:561-574(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-641, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [8]
RP   FUNCTION.
RX   PubMed=17272725; DOI=10.1126/science.1135380;
RA   Pinton P., Rimessi A., Marchi S., Orsini F., Migliaccio E.,
RA   Giorgio M., Contursi C., Minucci S., Mantovani F., Wieckowski M.R.,
RA   Del Sal G., Pelicci P.G., Rizzuto R.;
RT   "Protein kinase C beta and prolyl isomerase 1 regulate mitochondrial
RT   effects of the life-span determinant p66Shc.";
RL   Science 315:659-663(2007).
RN   [9]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=17962198; DOI=10.1074/jbc.M707268200;
RA   Bansode R.R., Huang W., Roy S.K., Mehta M., Mehta K.D.;
RT   "Protein kinase C deficiency increases fatty acid oxidation and
RT   reduces fat storage.";
RL   J. Biol. Chem. 283:231-236(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-195, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-641, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-641, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Calcium-activated and phospholipid-dependent
CC       serine/threonine-protein kinase involved in various processes such
CC       as regulation of the B-cell receptor (BCR) signalosome, apoptosis
CC       and transcription regulation. Plays a key role in B-cell
CC       activation and function by regulating BCR-induced NF-kappa-B
CC       activation and B-cell suvival. Required for recruitment and
CC       activation of the IKK kinase to lipid rafts and mediates
CC       phosphorylation of CARD11/CARMA1 at 'Ser-564', 'Ser-649' and 'Ser-
CC       657', leading to activate the NF-kappa-B signaling. Involved in
CC       apoptosis following oxidative damage: in case of oxidative
CC       conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc
CC       of SHC1, leading to mitochondrial accumulation of p66Shc, where
CC       p66Shc acts as a reactive oxygen species producer. Acts as a
CC       coactivator of androgen receptor (ANDR)-dependent transcription,
CC       by being recruited to ANDR target genes and specifically mediating
CC       phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag
CC       for epigenetic transcriptional activation that prevents
CC       demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A. Also
CC       involved in triglyceride homeostasis. Serves as the receptor for
CC       phorbol esters, a class of tumor promoters.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Binds 3 calcium ions per subunit. The ions are bound to
CC       the C2 domain (By similarity).
CC   -!- ENZYME REGULATION: Activated by diacylglycerol which in turn
CC       phosphorylates a range of cellular proteins. Specifically
CC       inhibited by Enzastaurin (LY317615) (By similarity).
CC   -!- SUBUNIT: Interacts with PDK1. Interacts in vitro with PRKCBP1.
CC       Interacts with PHLPP1 and PHLPP2; both proteins mediate its
CC       dephosphorylation. Interacts with KDM1A/LSD1, PKN1 and ANDR (By
CC       similarity).
CC   -!- INTERACTION:
CC       Q13873:BMPR2 (xeno); NbExp=2; IntAct=EBI-397048, EBI-527196;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Membrane; Peripheral membrane protein (By
CC       similarity).
CC   -!- PTM: Phosphorylation on Thr-500 within the activation loop renders
CC       it competent to autophosphorylate. Subsequent autophosphorylation
CC       of Thr-641 maintains catalytic competence, and autophosphorylation
CC       on Ser-660 appears to release the kinase into the cytosol.
CC       Autophosphorylation on other sites i.e. in the N-terminal and
CC       hinge regions have no effect on enzyme activity (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice develop an immunodeficiency
CC       characterized by impaired humoral immune responses and reduced
CC       cellular responses of B-cells similar to X-linked immunodeficiency
CC       (Xid). Mice are unable to activate NF-kappa-B and promote cell
CC       survival in B-cells upon BCR signaling, or even in mast cells. B-
CC       cells fail to recruit the I-kappa-B kinase (IKK) complex into
CC       lipid rafts, activate IKK, degrade I-kappa-B or up-regulate NF-
CC       kappa-B-dependent survival signals. Moreover, mutant animals are
CC       hyperphagic and exhibit higher food intake and reduced feed
CC       efficiency versus wild type. Mice are considerably leaner and
CC       display markedly decreased size of white fat depots. Triglyceride
CC       content in the liver and skeletal muscle is also significantly
CC       low.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. PKC subfamily.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 2 phorbol-ester/DAG-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; X53532; CAA37611.1; -; mRNA.
DR   EMBL; BC127083; AAI27084.1; -; mRNA.
DR   IPI; IPI00227898; -.
DR   PIR; S11213; S11213.
DR   RefSeq; NP_032881.1; NM_008855.2.
DR   UniGene; Mm.207496; -.
DR   UniGene; Mm.446371; -.
DR   ProteinModelPortal; P68404; -.
DR   SMR; P68404; 37-288, 339-669.
DR   IntAct; P68404; 10.
DR   MINT; MINT-98059; -.
DR   STRING; P68404; -.
DR   PRIDE; P68404; -.
DR   Ensembl; ENSMUST00000064989; ENSMUSP00000070019; ENSMUSG00000052889.
DR   GeneID; 18751; -.
DR   KEGG; mmu:18751; -.
DR   UCSC; uc009jou.1; mouse.
DR   CTD; 18751; -.
DR   MGI; MGI:97596; Prkcb.
DR   GeneTree; ENSGT00590000082854; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108317; -.
DR   InParanoid; P68404; -.
DR   OMA; QAHIDRE; -.
DR   OrthoDB; EOG40ZQX0; -.
DR   PhylomeDB; P68404; -.
DR   BRENDA; 2.7.11.13; 244.
DR   NextBio; 294921; -.
DR   ArrayExpress; P68404; -.
DR   Bgee; P68404; -.
DR   Genevestigator; P68404; -.
DR   GermOnline; ENSMUSG00000052889; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0050681; F:androgen receptor binding; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005246; F:calcium channel regulator activity; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR   GO; GO:0035403; F:histone kinase activity (H3-T6 specific); ISS:UniProtKB.
DR   GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; ISS:UniProtKB.
DR   GO; GO:0004697; F:protein kinase C activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0042113; P:B cell activation; IMP:UniProtKB.
DR   GO; GO:0050853; P:B cell receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:0006816; P:calcium ion transport; IDA:MGI.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:MGI.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:UniProtKB.
DR   GO; GO:0034339; P:regulation of transcription from RNA polymerase II promoter by nuclear hormone receptor; ISS:UniProtKB.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR014375; Protein_kinase_C_a/b/g.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   PIRSF; PIRSF000550; PKC_alpha; 1.
DR   PRINTS; PR00360; C2DOMAIN.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Adaptive immunity; Apoptosis; ATP-binding; Calcium;
KW   Chromatin regulator; Cytoplasm; Immunity; Kinase; Membrane;
KW   Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Repeat;
KW   Serine/threonine-protein kinase; Transcription;
KW   Transcription regulation; Transferase; Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    673       Protein kinase C beta type.
FT                                /FTId=PRO_0000055685.
FT   DOMAIN      173    260       C2.
FT   DOMAIN      342    600       Protein kinase.
FT   DOMAIN      601    671       AGC-kinase C-terminal.
FT   ZN_FING      36     86       Phorbol-ester/DAG-type 1.
FT   ZN_FING     101    151       Phorbol-ester/DAG-type 2.
FT   NP_BIND     348    356       ATP (By similarity).
FT   ACT_SITE    466    466       Proton acceptor (By similarity).
FT   METAL       186    186       Calcium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       187    187       Calcium 1 (By similarity).
FT   METAL       187    187       Calcium 2 (By similarity).
FT   METAL       193    193       Calcium 2 (By similarity).
FT   METAL       246    246       Calcium 1 (By similarity).
FT   METAL       246    246       Calcium 2 (By similarity).
FT   METAL       247    247       Calcium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       248    248       Calcium 1 (By similarity).
FT   METAL       248    248       Calcium 2 (By similarity).
FT   METAL       248    248       Calcium 3 (By similarity).
FT   METAL       251    251       Calcium 3 (By similarity).
FT   METAL       252    252       Calcium 3; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       254    254       Calcium 1 (By similarity).
FT   METAL       254    254       Calcium 3 (By similarity).
FT   BINDING     371    371       ATP (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      16     16       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES      17     17       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     195    195       Phosphotyrosine.
FT   MOD_RES     314    314       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     324    324       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     500    500       Phosphothreonine (By similarity).
FT   MOD_RES     504    504       Phosphothreonine (By similarity).
FT   MOD_RES     634    634       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     641    641       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     660    660       Phosphoserine (By similarity).
SQ   SEQUENCE   673 AA;  76894 MW;  A65573AAF6E224C7 CRC64;
     MADPAAGPPP SEGEESTVRF ARKGALRQKN VHEVKNHKFT ARFFKQPTFC SHCTDFIWGF
     GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPASDDPRS KHKFKIHTYS SPTFCDHCGS
     LLYGLIHQGM KCDTCMMNVH KRCVMNVPSL CGTDHTERRG RIYIQAHIDR EVLIVVVRDA
     KNLVPMDPNG LSDPYVKLKL IPDPKSESKQ KTKTIKCSLN PEWNETFRFQ LKESDKDRRL
     SVEIWDWDLT SRNDFMGSLS FGISELQKAG VDGWFKLLSQ EEGEYFNVPV PPEGSEGNEE
     LRQKFERAKI GQGTKAPEEK TANTISKFDN NGNRDRMKLT DFNFLMVLGK GSFGKVMLSE
     RKGTDELYAV KILKKDVVIQ DDDVECTMVE KRVLALPGKP PFLTQLHSCF QTMDRLYFVM
     EYVNGGDLMY HIQQVGRFKE PHAVFYAAEI AIGLFFLQSK GIIYRDLKLD NVMLDSEGHI
     KIADFGMCKE NIWDGVTTKT FCGTPDYIAP EIIAYQPYGK SVDWWAFGVL LYEMLAGQAP
     FEGEDEDELF QSIMEHNVAY PKSMSKEAVA ICKGLMTKHP GKRLGCGPEG ERDIKEHAFF
     RYIDWEKLER KEIQPPYKPK ACGRNAENFD RFFTRHPPVL TPPDQEVIRN IDQSEFEGFS
     FVNSEFLKPE VKS
//
ID   H31_MOUSE               Reviewed;         136 AA.
AC   P68433; P02295; P02296; P16106; Q05A97; Q3B7Z8; Q3B7Z9; Q5T009;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Histone H3.1;
GN   Name=Hist1h3a; Synonyms=H3a;
GN   and
GN   Name=Hist1h3g; Synonyms=H3.1-221, H3g;
GN   and
GN   Name=Hist1h3h; Synonyms=H3.1-291, H3h;
GN   and
GN   Name=Hist1h3i; Synonyms=H3.1-I, H3i;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=84041477; PubMed=6314253; DOI=10.1093/nar/11.19.6679;
RA   Sittman D.B., Graves R.A., Marzluff W.F.;
RT   "Structure of a cluster of mouse histone genes.";
RL   Nucleic Acids Res. 11:6679-6697(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3G AND HIST1H3H).
RX   MEDLINE=87112762; PubMed=3027355; DOI=10.1007/BF02115580;
RA   Taylor J.D., Wellman S.E., Marzluff W.F.;
RT   "Sequences of four mouse histone H3 genes: implications for evolution
RT   of mouse histone genes.";
RL   J. Mol. Evol. 23:242-249(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CD-1; TISSUE=Testis;
RX   MEDLINE=90067856; PubMed=2587222; DOI=10.1093/nar/17.21.8861;
RA   Kosciessa U., Doenecke D.;
RT   "Nucleotide sequences of mouse histone genes H2A and H3.1.";
RL   Nucleic Acids Res. 17:8861-8861(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3I).
RC   STRAIN=C57BL/CJ6;
RX   MEDLINE=97011334; PubMed=8858344;
RA   Wang Z.-F., Krasikov T., Frey M.R., Wang J., Matera A.G.,
RA   Marzluff W.F.;
RT   "Characterization of the mouse histone gene cluster on chromosome 13:
RT   45 histone genes in three patches spread over 1Mb.";
RL   Genome Res. 6:688-701(1996).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3A; HIST1H3G; HIST1H3H AND
RP   HIST1H3I).
RX   MEDLINE=22296985; PubMed=12408966; DOI=10.1016/S0888-7543(02)96850-3;
RA   Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
RT   "The human and mouse replication-dependent histone genes.";
RL   Genomics 80:487-498(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RA   Franke K., Drabent B., Doenecke D.;
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   PROTEIN SEQUENCE OF 58-64, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [11]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=3018484;
RA   Brown D.T., Wellman S.E., Sittman D.B.;
RT   "Changes in the levels of three different classes of histone mRNA
RT   during murine erythroleukemia cell differentiation.";
RL   Mol. Cell. Biol. 5:2879-2886(1985).
RN   [12]
RP   PHOSPHORYLATION AT SER-11 AND SER-29.
RX   PubMed=10464286; DOI=10.1074/jbc.274.36.25543;
RA   Goto H., Tomono Y., Ajiro K., Kosako H., Fujita M., Sakurai M.,
RA   Okawa K., Iwamatsu A., Okigaki T., Takahashi T., Inagaki M.;
RT   "Identification of a novel phosphorylation site on histone H3 coupled
RT   with mitotic chromosome condensation.";
RL   J. Biol. Chem. 274:25543-25549(1999).
RN   [13]
RP   METHYLATION AT LYS-5 AND ARG-18.
RX   PubMed=11747826; DOI=10.1016/S0960-9822(01)00600-5;
RA   Ma H., Baumann C.T., Li H., Strahl B.D., Rice R., Jelinek M.A.,
RA   Aswad D.W., Allis C.D., Hager G.L., Stallcup M.R.;
RT   "Hormone-dependent, CARM1-directed, arginine-specific methylation of
RT   histone H3 on a steroid-regulated promoter.";
RL   Curr. Biol. 11:1981-1985(2001).
RN   [14]
RP   PHOSPHORYLATION AT SER-29.
RX   PubMed=11441012; DOI=10.1074/jbc.M103973200;
RA   Zhong S., Jansen C., She Q.-B., Goto H., Inagaki M., Bode A.M.,
RA   Ma W.-Y., Dong Z.;
RT   "Ultraviolet B-induced phosphorylation of histone H3 at serine 28 is
RT   mediated by MSK1.";
RL   J. Biol. Chem. 276:33213-33219(2001).
RN   [15]
RP   ACETYLATION AT LYS-15; LYS-19 AND LYS-24, AND METHYLATION AT ARG-18.
RX   PubMed=12498683; DOI=10.1016/S0960-9822(02)01387-8;
RA   Daujat S., Bauer U.-M., Shah V., Turner B., Berger S., Kouzarides T.;
RT   "Crosstalk between CARM1 methylation and CBP acetylation on histone
RT   H3.";
RL   Curr. Biol. 12:2090-2097(2002).
RN   [16]
RP   METHYLATION AT ARG-18.
RX   PubMed=11751582; DOI=10.1093/embo-reports/kvf013;
RA   Bauer U.-M., Daujat S., Nielsen S.J., Nightingale K., Kouzarides T.;
RT   "Methylation at arginine 17 of histone H3 is linked to gene
RT   activation.";
RL   EMBO Rep. 3:39-44(2002).
RN   [17]
RP   PHOSPHORYLATION AT SER-11 AND SER-29.
RX   PubMed=11856369; DOI=10.1046/j.1356-9597.2001.00498.x;
RA   Goto H., Yasui Y., Nigg E.A., Inagaki M.;
RT   "Aurora-B phosphorylates Histone H3 at serine28 with regard to the
RT   mitotic chromosome condensation.";
RL   Genes Cells 7:11-17(2002).
RN   [18]
RP   ACETYLATION AT LYS-15; LYS-19 AND LYS-24, METHYLATION AT LYS-10;
RP   LYS-28; LYS-37; LYS-80 AND LYS-123, AND MASS SPECTROMETRY.
RX   PubMed=13678296; DOI=10.1023/A:1025334006014;
RA   Cocklin R.R., Wang M.;
RT   "Identification of methylation and acetylation sites on mouse histone
RT   H3 using matrix-assisted laser desorption/ionization time-of-flight
RT   and nanoelectrospray ionization tandem mass spectrometry.";
RL   J. Protein Chem. 22:327-334(2003).
RN   [19]
RP   CITRULLINATION.
RX   PubMed=15339660; DOI=10.1016/j.cell.2004.08.020;
RA   Cuthbert G.L., Daujat S., Snowden A.W., Erdjument-Bromage H.,
RA   Hagiwara T., Yamada M., Schneider R., Gregory P.D., Tempst P.,
RA   Bannister A.J., Kouzarides T.;
RT   "Histone deimination antagonizes arginine methylation.";
RL   Cell 118:545-553(2004).
RN   [20]
RP   METHYLATION AT ARG-9, AND ACETYLATION AT LYS-10.
RX   PubMed=15485929; DOI=10.1128/MCB.24.21.9630-9645.2004;
RA   Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S.;
RT   "Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and
RT   negatively regulates expression of ST7 and NM23 tumor suppressor
RT   genes.";
RL   Mol. Cell. Biol. 24:9630-9645(2004).
RN   [21]
RP   METHYLATION AT ARG-18.
RX   PubMed=15616592; DOI=10.1038/sj.emboj.7600500;
RA   Covic M., Hassa P.O., Saccani S., Buerki C., Meier N.I., Lombardi C.,
RA   Imhof R., Bedford M.T., Natoli G., Hottiger M.O.;
RT   "Arginine methyltransferase CARM1 is a promoter-specific regulator of
RT   NF-kappaB-dependent gene expression.";
RL   EMBO J. 24:85-96(2005).
RN   [22]
RP   PHOSPHORYLATION AT THR-4 AND SER-11.
RX   PubMed=15681610; DOI=10.1101/gad.1267105;
RA   Dai J., Sultan S., Taylor S.S., Higgins J.M.G.;
RT   "The kinase haspin is required for mitotic histone H3 Thr 3
RT   phosphorylation and normal metaphase chromosome alignment.";
RL   Genes Dev. 19:472-488(2005).
RN   [23]
RP   PHOSPHORYLATION AT SER-29.
RX   PubMed=15684425; DOI=10.1074/jbc.M410521200;
RA   Choi H.S., Choi B.Y., Cho Y.-Y., Zhu F., Bode A.M., Dong Z.;
RT   "Phosphorylation of Ser28 in histone H3 mediated by mixed lineage
RT   kinase-like mitogen-activated protein triple kinase alpha.";
RL   J. Biol. Chem. 280:13545-13553(2005).
RN   [24]
RP   PHOSPHORYLATION AT SER-11 AND SER-29.
RX   PubMed=15870105; DOI=10.1242/jcs.02373;
RA   Dyson M.H., Thomson S., Inagaki M., Goto H., Arthur S.J.,
RA   Nightingale K., Iborra F.J., Mahadevan L.C.;
RT   "MAP kinase-mediated phosphorylation of distinct pools of histone H3
RT   at S10 or S28 via mitogen- and stress-activated kinase 1/2.";
RL   J. Cell Sci. 118:2247-2259(2005).
RN   [25]
RP   PHOSPHORYLATION AT SER-11 AND SER-29.
RX   PubMed=15735677; DOI=10.1038/sj.onc.1208521;
RA   Dunn K.L., Davie J.R.;
RT   "Stimulation of the Ras-MAPK pathway leads to independent
RT   phosphorylation of histone H3 on serine 10 and 28.";
RL   Oncogene 24:3492-3502(2005).
RN   [26]
RP   ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28,
RP   METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28; LYS-37 AND
RP   LYS-80, AND MASS SPECTROMETRY.
RX   PubMed=17194708; DOI=10.1074/jbc.M607900200;
RA   Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J.,
RA   Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.;
RT   "Organismal differences in post-translational modifications in
RT   histones H3 and H4.";
RL   J. Biol. Chem. 282:7641-7655(2007).
RN   [27]
RP   ACETYLATION AT LYS-37.
RX   PubMed=17189264; DOI=10.1074/jbc.M607909200;
RA   Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L.,
RA   Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.;
RT   "Identification of histone H3 lysine 36 acetylation as a highly
RT   conserved histone modification.";
RL   J. Biol. Chem. 282:7632-7640(2007).
RN   [28]
RP   UBIQUITINATION.
RX   PubMed=20122409; DOI=10.1016/j.molcel.2009.12.035;
RA   Grazini U., Zanardi F., Citterio E., Casola S., Goding C.R.,
RA   McBlane F.;
RT   "The RING domain of RAG1 ubiquitylates histone H3: a novel activity in
RT   chromatin-mediated regulation of V(D)J joining.";
RL   Mol. Cell 37:282-293(2010).
CC   -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and
CC       compact DNA into chromatin, limiting DNA accessibility to the
CC       cellular machineries which require DNA as a template. Histones
CC       thereby play a central role in transcription regulation, DNA
CC       repair, DNA replication and chromosomal stability. DNA
CC       accessibility is regulated via a complex set of post-translational
CC       modifications of histones, also called histone code, and
CC       nucleosome remodeling.
CC   -!- SUBUNIT: The nucleosome is a histone octamer containing two
CC       molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
CC       heterotetramer and two H2A-H2B heterodimers. The octamer wraps
CC       approximately 147 bp of DNA.
CC   -!- INTERACTION:
CC       P83917:Cbx1; NbExp=4; IntAct=EBI-79743, EBI-78119;
CC       Q8WTS6:SETD7 (xeno); NbExp=2; IntAct=EBI-79743, EBI-1268586;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- DEVELOPMENTAL STAGE: Expressed during S phase, then expression
CC       strongly decreases as cell division slows down during the process
CC       of differentiation.
CC   -!- PTM: Acetylation is generally linked to gene activation.
CC       Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9
CC       (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac)
CC       favors methylation at Arg-18 (H3R17me).
CC   -!- PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by
CC       PADI4 impairs methylation and represses transcription.
CC   -!- PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is
CC       linked to gene activation. Symmetric dimethylation at Arg-9
CC       (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric
CC       dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene
CC       repression and is mutually exclusive with H3 Lys-5 methylation
CC       (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes
CC       regardless of their transcription state and is enriched on
CC       inactive promoters, while it is absent on active promoters (By
CC       similarity).
CC   -!- PTM: Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80
CC       (H3K79me) are linked to gene activation. Methylation at Lys-5
CC       (H3K4me) facilitates subsequent acetylation of H3 and H4.
CC       Methylation at Lys-80 (H3K79me) is associated with DNA double-
CC       strand break (DSB) responses and is a specific target for TP53BP1.
CC       Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to
CC       gene repression. Methylation at Lys-10 (H3K9me) is a specific
CC       target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents
CC       subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of
CC       H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me)
CC       require preliminary monoubiquitination of H2B at 'Lys-120'.
CC       Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched
CC       in inactive X chromosome chromatin.
CC   -!- PTM: Phosphorylated at Thr-4 (H3T3ph) by GSG2/haspin during
CC       prophase and dephosphorylated during anaphase. Phosphorylation at
CC       Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation
CC       and cell-cycle progression during mitosis and meiosis. In addition
CC       phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is
CC       important during interphase because it enables the transcription
CC       of genes following external stimulation, like mitogens, stress,
CC       growth factors or UV irradiation and result in the activation of
CC       genes, such as c-fos and c-jun. Phosphorylation at Ser-11
CC       (H3S10ph), which is linked to gene activation, prevents
CC       methylation at Lys-10 (H3K9me) but facilitates acetylation of H3
CC       and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the
CC       dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from
CC       heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an
CC       essential regulatory mechanism for neoplastic cell transformation.
CC       Phosphorylated at Ser-29 (H3S28ph) by MLTK isoform 1, RPS6KA5 or
CC       AURKB during mitosis or upon ultraviolet B irradiation.
CC       Phosphorylation at Thr-7 (H3T6ph) by PRKCBB is a specific tag for
CC       epigenetic transcriptional activation that prevents demethylation
CC       of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically
CC       phosphorylated at Thr-12 (H3T11ph) from prophase to early
CC       anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph)
CC       by PKN1 is a specific tag for epigenetic transcriptional
CC       activation that promotes demethylation of Lys-10 (H3K9me) by
CC       KDM4C/JMJD2C. Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes
CC       exclusion of CBX5 (HP1 alpha) from chromatin.
CC   -!- PTM: Ubiquitinated by the CUL4-DDB-RBX1 complex in response to
CC       ultraviolet irradiation. This may weaken the interaction between
CC       histones and DNA and facilitate DNA accessibility to repair
CC       proteins (By similarity). Monoubiquitinated by RAG1 in lymphoid
CC       cells, monoubiquitination is required for V(D)J recombination.
CC   -!- MISCELLANEOUS: This histone is only present in mammals.
CC   -!- SIMILARITY: Belongs to the histone H3 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; X01684; CAA25839.1; -; Genomic_DNA.
DR   EMBL; M32460; AAA37811.1; -; Genomic_DNA.
DR   EMBL; M32462; AAA37813.1; -; Genomic_DNA.
DR   EMBL; X16496; CAA34512.1; -; Genomic_DNA.
DR   EMBL; U62670; AAB04763.1; -; Genomic_DNA.
DR   EMBL; U62672; AAB04765.1; -; Genomic_DNA.
DR   EMBL; AY158944; AAO06254.1; -; Genomic_DNA.
DR   EMBL; AY158945; AAO06255.1; -; Genomic_DNA.
DR   EMBL; AY158946; AAO06256.1; -; Genomic_DNA.
DR   EMBL; AY158952; AAO06262.1; -; Genomic_DNA.
DR   EMBL; Y12290; CAA72968.1; -; Genomic_DNA.
DR   EMBL; AK006742; BAB24722.1; -; mRNA.
DR   EMBL; AK018952; BAB31493.1; -; mRNA.
DR   EMBL; AK155722; BAE33402.1; -; mRNA.
DR   EMBL; AL590388; CAI25837.1; -; Genomic_DNA.
DR   EMBL; AL589651; CAI24113.1; -; Genomic_DNA.
DR   EMBL; AL589651; CAI24105.1; -; Genomic_DNA.
DR   EMBL; BC107285; AAI07286.1; -; mRNA.
DR   EMBL; BC107287; AAI07288.1; -; mRNA.
DR   EMBL; BC115816; AAI15817.1; -; mRNA.
DR   EMBL; BC116383; AAI16384.1; -; mRNA.
DR   EMBL; BC125355; AAI25356.1; -; mRNA.
DR   EMBL; BC125357; AAI25358.1; -; mRNA.
DR   IPI; IPI00553538; -.
DR   PIR; A39525; A39525.
DR   PIR; S06755; S06755.
DR   RefSeq; NP_038578.2; NM_013550.4.
DR   RefSeq; NP_659539.1; NM_145073.2.
DR   RefSeq; NP_835513.1; NM_178206.2.
DR   RefSeq; NP_835514.1; NM_178207.2.
DR   UniGene; Mm.221301; -.
DR   UniGene; Mm.261657; -.
DR   UniGene; Mm.377874; -.
DR   UniGene; Mm.390558; -.
DR   UniGene; Mm.397328; -.
DR   PDB; 1GUW; NMR; -; B=1-17.
DR   PDB; 1U35; X-ray; 3.00 A; A/E=1-136.
DR   PDB; 2WP1; X-ray; 2.10 A; P/Q=15-24.
DR   PDB; 2XL3; X-ray; 2.70 A; D/F=2-9.
DR   PDBsum; 1GUW; -.
DR   PDBsum; 1U35; -.
DR   PDBsum; 2WP1; -.
DR   PDBsum; 2XL3; -.
DR   ProteinModelPortal; P68433; -.
DR   SMR; P68433; 2-136.
DR   IntAct; P68433; 35.
DR   MINT; MINT-191105; -.
DR   STRING; P68433; -.
DR   PhosphoSite; P68433; -.
DR   PRIDE; P68433; -.
DR   Ensembl; ENSMUST00000080859; ENSMUSP00000079670; ENSMUSG00000062417.
DR   Ensembl; ENSMUST00000091701; ENSMUSP00000089293; ENSMUSG00000069265.
DR   Ensembl; ENSMUST00000091752; ENSMUSP00000089346; ENSMUSG00000069310.
DR   Ensembl; ENSMUST00000091754; ENSMUSP00000089348; ENSMUSG00000069312.
DR   GeneID; 319152; -.
DR   GeneID; 319153; -.
DR   GeneID; 360198; -.
DR   GeneID; 97908; -.
DR   KEGG; mmu:319152; -.
DR   KEGG; mmu:319153; -.
DR   KEGG; mmu:360198; -.
DR   KEGG; mmu:97908; -.
DR   UCSC; uc007prc.1; mouse.
DR   CTD; 319152; -.
DR   CTD; 319153; -.
DR   CTD; 360198; -.
DR   CTD; 97908; -.
DR   MGI; MGI:2668828; Hist1h3a.
DR   MGI; MGI:2145541; Hist1h3g.
DR   MGI; MGI:2448349; Hist1h3h.
DR   MGI; MGI:2448350; Hist1h3i.
DR   GeneTree; ENSGT00560000076869; -.
DR   HOVERGEN; HBG001172; -.
DR   InParanoid; P68433; -.
DR   OMA; DLRFQSQ; -.
DR   OrthoDB; EOG412M6S; -.
DR   PhylomeDB; P68433; -.
DR   NextBio; 394196; -.
DR   ArrayExpress; P68433; -.
DR   Bgee; P68433; -.
DR   CleanEx; MM_HIST1H3A; -.
DR   CleanEx; MM_HIST1H3G; -.
DR   CleanEx; MM_HIST1H3H; -.
DR   CleanEx; MM_HIST1H3I; -.
DR   Genevestigator; P68433; -.
DR   GermOnline; ENSMUSG00000062417; Mus musculus.
DR   GermOnline; ENSMUSG00000069265; Mus musculus.
DR   GermOnline; ENSMUSG00000069310; Mus musculus.
DR   GermOnline; ENSMUSG00000069312; Mus musculus.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR007125; Histone_core_D.
DR   InterPro; IPR000164; Histone_H3.
DR   Gene3D; G3DSA:1.10.20.10; Histone-fold; 1.
DR   PANTHER; PTHR11426; Histone_H3; 1.
DR   Pfam; PF00125; Histone; 1.
DR   PRINTS; PR00622; HISTONEH3.
DR   SMART; SM00428; H3; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
DR   PROSITE; PS00322; HISTONE_H3_1; 1.
DR   PROSITE; PS00959; HISTONE_H3_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Chromosome; Citrullination;
KW   Direct protein sequencing; DNA-binding; Methylation; Nucleosome core;
KW   Nucleus; Phosphoprotein; Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    136       Histone H3.1.
FT                                /FTId=PRO_0000221249.
FT   MOD_RES       3      3       Asymmetric dimethylarginine; by PRMT6 (By
FT                                similarity).
FT   MOD_RES       3      3       Phosphoarginine (Probable).
FT   MOD_RES       4      4       Phosphothreonine.
FT   MOD_RES       5      5       N6-acetyllysine; alternate.
FT   MOD_RES       5      5       N6-methyllysine; alternate.
FT   MOD_RES       7      7       Phosphothreonine; by PKC (By similarity).
FT   MOD_RES       9      9       Citrulline; alternate (Probable).
FT   MOD_RES       9      9       Symmetric dimethylarginine; by PRMT5;
FT                                alternate.
FT   MOD_RES      10     10       N6,N6,N6-trimethyllysine; alternate.
FT   MOD_RES      10     10       N6,N6-dimethyllysine; alternate.
FT   MOD_RES      10     10       N6-acetyllysine; alternate.
FT   MOD_RES      10     10       N6-methyllysine; alternate.
FT   MOD_RES      11     11       Phosphoserine.
FT   MOD_RES      12     12       Phosphothreonine; by PKC (By similarity).
FT   MOD_RES      15     15       N6-acetyllysine.
FT   MOD_RES      18     18       Asymmetric dimethylarginine; by CARM1;
FT                                alternate.
FT   MOD_RES      18     18       Citrulline; alternate (Probable).
FT   MOD_RES      19     19       N6-acetyllysine; alternate.
FT   MOD_RES      19     19       N6-methyllysine; alternate.
FT   MOD_RES      24     24       N6-acetyllysine; alternate.
FT   MOD_RES      24     24       N6-methyllysine; alternate.
FT   MOD_RES      28     28       N6,N6,N6-trimethyllysine; alternate.
FT   MOD_RES      28     28       N6,N6-dimethyllysine; alternate.
FT   MOD_RES      28     28       N6-acetyllysine; alternate.
FT   MOD_RES      28     28       N6-methyllysine; alternate.
FT   MOD_RES      29     29       Phosphoserine.
FT   MOD_RES      37     37       N6,N6,N6-trimethyllysine; alternate
FT                                (Probable).
FT   MOD_RES      37     37       N6,N6-dimethyllysine; alternate.
FT   MOD_RES      37     37       N6-acetyllysine; alternate.
FT   MOD_RES      37     37       N6-methyllysine; alternate.
FT   MOD_RES      38     38       N6-methyllysine (By similarity).
FT   MOD_RES      42     42       Phosphotyrosine (By similarity).
FT   MOD_RES      58     58       Phosphoserine (By similarity).
FT   MOD_RES      65     65       N6-methyllysine (By similarity).
FT   MOD_RES      80     80       N6,N6,N6-trimethyllysine; alternate.
FT   MOD_RES      80     80       N6,N6-dimethyllysine; alternate.
FT   MOD_RES      80     80       N6-methyllysine; alternate.
FT   MOD_RES      81     81       Phosphothreonine (By similarity).
FT   MOD_RES     123    123       N6-methyllysine.
FT   MOD_RES     129    129       Phosphoarginine (Probable).
FT   MOD_RES     130    130       Phosphoarginine (Probable).
FT   MOD_RES     132    132       Phosphoarginine (Potential).
FT   HELIX        46     55
FT   HELIX        65     77
FT   STRAND       80     82
FT   HELIX        87    114
FT   STRAND      118    120
FT   HELIX       122    132
SQ   SEQUENCE   136 AA;  15404 MW;  9B89008EA50A0EF6 CRC64;
     MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE
     LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEACEAY LVGLFEDTNL CAIHAKRVTI
     MPKDIQLARR IRGERA
//
ID   1433F_MOUSE             Reviewed;         246 AA.
AC   P68510; P11576; P70198; Q3TGZ9;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=14-3-3 protein eta;
GN   Name=Ywhah;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CDK16.
RC   TISSUE=Brain;
RX   MEDLINE=97340943; PubMed=9197417; DOI=10.1007/s004380050453;
RA   Sladeczek F., Camonis J.H., Burnol A.-F., Le Bouffant F.;
RT   "The Cdk-like protein PCTAIRE-1 from mouse brain associates with p11
RT   and 14-3-3 proteins.";
RL   Mol. Gen. Genet. 254:571-577(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/Sv;
RA   Takihara Y., Irie K., Nomura M., Motaleb M., Matsumoto K., Shimada K.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98411340; PubMed=9738002; DOI=10.1074/jbc.273.39.25356;
RA   Tang S.J., Seun T.-C., McInnes R.R., Buchwald M.;
RT   "Association of the TLX-2 homeodomain and 14-3-3eta signaling
RT   proteins.";
RL   J. Biol. Chem. 273:25356-25363(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12008017; DOI=10.1016/S0169-328X(02)00129-8;
RA   Toyooka K., Muratake T., Watanabe H., Hayashi S., Ichikawa T.,
RA   Usui H., Washiyama K., Kumanishi T., Takahashi Y.;
RT   "Isolation and structure of the mouse 14-3-3 eta chain gene and the
RT   distribution of 14-3-3 eta mRNA in the mouse brain.";
RL   Brain Res. Mol. Brain Res. 100:13-20(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart, Kidney, and Sympathetic ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 13-56; 62-69; 92-106; 111-120; 133-172 AND
RP   199-227, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [8]
RP   INTERACTION WITH RGNEF.
RX   PubMed=11533041; DOI=10.1074/jbc.M107709200;
RA   Zhai J., Lin H., Shamim M., Schlaepfer W.W., Canete-Soler R.;
RT   "Identification of a novel interaction of 14-3-3 with p190RhoGEF.";
RL   J. Biol. Chem. 276:41318-41324(2001).
RN   [9]
RP   INTERACTION WITH KCNK18.
RX   PubMed=18397886; DOI=10.1074/jbc.M800712200;
RA   Czirjak G., Vuity D., Enyedi P.;
RT   "Phosphorylation-dependent binding of 14-3-3 proteins controls TRESK
RT   regulation.";
RL   J. Biol. Chem. 283:15672-15680(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-117, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC       spectrum of both general and specialized signaling pathway. Binds
CC       to a large number of partners, usually by recognition of a
CC       phosphoserine or phosphothreonine motif. Binding generally results
CC       in the modulation of the activity of the binding partner.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with many nuclear
CC       hormone receptors and cofactors including AR, ESR1, ESR2, MC2R,
CC       NR3C1, NRIP1, PPARBP and THRA. Interacts with ABL1 (phosphorylated
CC       form); the interaction retains it in the cytoplasm. Weakly
CC       interacts with CDKN1B (By similarity). Interacts with RGNEF and
CC       CDK16. Interacts with KCNK18 in a phosphorylation-dependent
CC       manner.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the 14-3-3 family.
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DR   EMBL; U57311; AAC53256.1; -; mRNA.
DR   EMBL; D87661; BAA13422.1; -; mRNA.
DR   EMBL; AF077002; AAC36290.1; -; mRNA.
DR   EMBL; AB063572; BAB79599.1; -; Genomic_DNA.
DR   EMBL; AK077596; BAC36887.1; -; mRNA.
DR   EMBL; AK149224; BAE28768.1; -; mRNA.
DR   EMBL; AK168520; BAE40399.1; -; mRNA.
DR   EMBL; AK169035; BAE40826.1; -; mRNA.
DR   EMBL; AK169189; BAE40965.1; -; mRNA.
DR   EMBL; BC008187; AAH08187.1; -; mRNA.
DR   EMBL; BC061497; AAH61497.1; -; mRNA.
DR   IPI; IPI00227392; -.
DR   RefSeq; NP_035868.1; NM_011738.2.
DR   UniGene; Mm.332314; -.
DR   ProteinModelPortal; P68510; -.
DR   SMR; P68510; 2-236.
DR   MINT; MINT-198030; -.
DR   STRING; P68510; -.
DR   UCD-2DPAGE; P68510; -.
DR   PRIDE; P68510; -.
DR   Ensembl; ENSMUST00000019109; ENSMUSP00000019109; ENSMUSG00000018965.
DR   GeneID; 22629; -.
DR   KEGG; mmu:22629; -.
DR   UCSC; uc008xag.1; mouse.
DR   CTD; 22629; -.
DR   MGI; MGI:109194; Ywhah.
DR   eggNOG; roNOG10210; -.
DR   GeneTree; ENSGT00550000074221; -.
DR   HOGENOM; HBG611720; -.
DR   HOVERGEN; HBG050423; -.
DR   InParanoid; P68510; -.
DR   OMA; KYLIKNC; -.
DR   OrthoDB; EOG48PMM0; -.
DR   PhylomeDB; P68510; -.
DR   NextBio; 302995; -.
DR   Bgee; P68510; -.
DR   Genevestigator; P68510; -.
DR   GermOnline; ENSMUSG00000018965; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IDA:ProtInc.
DR   GO; GO:0035259; F:glucocorticoid receptor binding; ISS:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; IDA:MGI.
DR   GO; GO:0016563; F:transcription activator activity; ISS:UniProtKB.
DR   GO; GO:0007010; P:cytoskeleton organization; NAS:ProtInc.
DR   GO; GO:0006713; P:glucocorticoid catabolic process; ISS:UniProtKB.
DR   GO; GO:0042921; P:glucocorticoid receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; IDA:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptosis; NAS:ProtInc.
DR   GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IDA:MGI.
DR   GO; GO:0007088; P:regulation of mitosis; NAS:ProtInc.
DR   InterPro; IPR000308; 14-3-3.
DR   PANTHER; PTHR18860; 14-3-3; 1.
DR   PIRSF; PIRSF000868; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    246       14-3-3 protein eta.
FT                                /FTId=PRO_0000058624.
FT   SITE         57     57       Interaction with phosphoserine on
FT                                interacting protein (By similarity).
FT   SITE        132    132       Interaction with phosphoserine on
FT                                interacting protein (By similarity).
FT   MOD_RES       2      2       N-acetylglycine (By similarity).
FT   MOD_RES      25     25       Phosphoserine (By similarity).
FT   MOD_RES     117    117       Phosphotyrosine.
FT   CONFLICT     15     16       EQ -> DE (in Ref. 2; BAA13422).
SQ   SEQUENCE   246 AA;  28212 MW;  C12F62B4ABA76DA3 CRC64;
     MGDREQLLQR ARLAEQAERY DDMASAMKAV TELNEPLSNE DRNLLSVAYK NVVGARRSSW
     RVISSIEQKT MADGNEKKLE KVKAYREKIE KELETVCNDV LALLDKFLIK NCNDFQYESK
     VFYLKMKGDY YRYLAEVASG EKKNSVVEAS EAAYKEAFEI SKEHMQPTHP IRLGLALNFS
     VFYYEIQNAP EQACLLAKQA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDE
     EAGEGN
//
ID   RANB9_MOUSE             Reviewed;         653 AA.
AC   P69566; P84500; Q3V136;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=Ran-binding protein 9;
DE            Short=RanBP9;
DE   AltName: Full=B-cell antigen receptor Ig beta-associated protein 1;
DE            Short=IBAP-1;
DE   AltName: Full=Ran-binding protein M;
DE            Short=RanBPM;
GN   Name=Ranbp9; Synonyms=Ranbpm;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DDX4, TISSUE
RP   SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Testis;
RX   PubMed=14648869; DOI=10.1002/mrd.20009;
RA   Shibata N., Tsunekawa N., Okamoto-Ito S., Akasu R., Tokumasu A.,
RA   Noce T.;
RT   "Mouse RanBPM is a partner gene to a germline specific RNA helicase,
RT   mouse vasa homolog protein.";
RL   Mol. Reprod. Dev. 67:1-7(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Doi T., Watanabe T.;
RT   "B cell antigen receptor Ig beta associated protein.";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 42-653 (ISOFORM 1), AND INTERACTION WITH
RP   NGFR.
RC   TISSUE=Brain;
RX   MEDLINE=22843461; PubMed=12963025; DOI=10.1016/j.bbrc.2003.08.033;
RA   Bai D., Chen H., Huang B.-R.;
RT   "RanBPM is a novel binding protein for p75NTR.";
RL   Biochem. Biophys. Res. Commun. 309:552-557(2003).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=14722085; DOI=10.1074/jbc.M313515200;
RA   Denti S., Sirri A., Cheli A., Rogge L., Innamorati G., Putignano S.,
RA   Fabbri M., Pardi R., Bianchi E.;
RT   "RanBPM is a phosphoprotein that associates with the plasma membrane
RT   and interacts with the integrin LFA-1.";
RL   J. Biol. Chem. 279:13027-13034(2004).
CC   -!- FUNCTION: May act as an adapter protein to couple membrane
CC       receptors to intracellular signaling pathways. May be involved in
CC       signaling of ITGB2/LFA-1 and other integrins. Enhances HGF-MET
CC       signaling by recruiting Sos and activating the Ras pathway.
CC       Involved in activation of androgen and glucocorticoid receptor in
CC       the presence of their cognate hormones. Stabilizes TP73 isoform
CC       Alpha, probably by inhibiting its ubiquitination, and increases
CC       its proapoptotic activity. Inhibits the kinase activity of DYRK1A
CC       and DYRK1B. Inhibits FMR1 binding to RNA (By similarity).
CC   -!- SUBUNIT: Interacts with GTP-bound Ran, AR, CDC2L1, CALB1, S100A7,
CC       USP11, MKLN1, SOS1 or SOS2, C20ORF11, and FMR1. Interacts with the
CC       Dyrk kinases HIPK2, DYRK1A, and DYRK1B. Interacts with TP73
CC       isoform Alpha but not with TP53. Interacts with the HGF receptor
CC       MET and the integrins ITGB1 and ITGB2, but not with ITGAL. Part of
CC       a complex consisting of RANBP9, MKLN1 and C20ORF11. Part of a
CC       complex consisting of RANBP9, RAN, DYRK1B and COPS5 (By
CC       similarity). Interacts with NGFR and DDX4.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity). Note=Perinuclear in spermatids.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P69566-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P69566-2; Sequence=VSP_028266, VSP_028267;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC       maturating spermatocytes.
CC   -!- DOMAIN: The SPRY domain mediates the interaction with MET, AR, and
CC       CDC2L1 (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC       Phosphorylated in response to stress (By similarity).
CC   -!- PTM: Ubiquitinated. Polyubiquitination targets the protein for
CC       rapid degradation via the ubiquitin system (By similarity).
CC   -!- SIMILARITY: Belongs to the RANBP9/10 family.
CC   -!- SIMILARITY: Contains 1 B30.2/SPRY domain.
CC   -!- SIMILARITY: Contains 1 CTLH domain.
CC   -!- SIMILARITY: Contains 1 LisH domain.
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DR   EMBL; AF006465; AAD01272.1; -; mRNA.
DR   EMBL; AK132714; BAE21317.1; -; mRNA.
DR   IPI; IPI00116285; -.
DR   IPI; IPI00867784; -.
DR   PIR; JC8013; JC8013.
DR   RefSeq; NP_064314.2; NM_019930.2.
DR   UniGene; Mm.148781; -.
DR   ProteinModelPortal; P69566; -.
DR   SMR; P69566; 100-257.
DR   STRING; P69566; -.
DR   PhosphoSite; P69566; -.
DR   PRIDE; P69566; -.
DR   Ensembl; ENSMUST00000045043; ENSMUSP00000045791; ENSMUSG00000038546.
DR   GeneID; 56705; -.
DR   KEGG; mmu:56705; -.
DR   UCSC; uc007qgd.1; mouse.
DR   CTD; 56705; -.
DR   MGI; MGI:1928741; Ranbp9.
DR   eggNOG; roNOG10326; -.
DR   GeneTree; ENSGT00530000063160; -.
DR   HOGENOM; HBG444765; -.
DR   HOVERGEN; HBG053444; -.
DR   InParanoid; P69566; -.
DR   OMA; FTLKVRQ; -.
DR   OrthoDB; EOG4868C1; -.
DR   NextBio; 313155; -.
DR   ArrayExpress; P69566; -.
DR   Bgee; P69566; -.
DR   CleanEx; MM_RANBP9; -.
DR   Genevestigator; P69566; -.
DR   GermOnline; ENSMUSG00000038546; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR001870; B302/SPRY.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR006595; CTLH_C.
DR   InterPro; IPR006594; LisH_dimerisation.
DR   InterPro; IPR013720; LisH_dimerisation_sub.
DR   InterPro; IPR013144; Ran-bd_prot-like_CRA_domain.
DR   InterPro; IPR019589; Ran-bd_prot_CRA_domain.
DR   InterPro; IPR018355; SPla/RYanodine_receptor_sg.
DR   InterPro; IPR003877; SPRY_rcpt.
DR   Pfam; PF08513; LisH; 1.
DR   Pfam; PF10607; RanBPM_CRA; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   SMART; SM00757; CRA; 1.
DR   SMART; SM00668; CTLH; 1.
DR   SMART; SM00667; LisH; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50897; CTLH; 1.
DR   PROSITE; PS50896; LISH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW   Ubl conjugation.
FT   CHAIN         1    653       Ran-binding protein 9.
FT                                /FTId=PRO_0000097170.
FT   DOMAIN       72    259       B30.2/SPRY.
FT   DOMAIN      290    322       LisH.
FT   DOMAIN      328    385       CTLH.
FT   REGION      326    332       Interaction with CALB1 (By similarity).
FT   REGION      539    653       Interaction with FMR1 (By similarity).
FT   COMPBIAS      5     10       Poly-Pro.
FT   COMPBIAS     14     20       Poly-Pro.
FT   MOD_RES     330    330       N6-acetyllysine (By similarity).
FT   MOD_RES     527    527       Phosphoserine (By similarity).
FT   VAR_SEQ       1    107       Missing (in isoform 2).
FT                                /FTId=VSP_028266.
FT   VAR_SEQ     108    115       NNLRVHYK -> MWESSWVL (in isoform 2).
FT                                /FTId=VSP_028267.
FT   CONFLICT     92     92       R -> P (in Ref. 4).
SQ   SEQUENCE   653 AA;  71012 MW;  BE810E69B238BBD5 CRC64;
     MSGQPPPPPP QQQPPPPPPP ASAAAPATAP PGLAVGPGPA AGVPVPGLAA GSSAAAPFPH
     GDSALNEQEK ELQRRLKRLY PAVDEQETPL PRSWSPKDKF SYIGLSQNNL RVHYKGHGKT
     PKDAASVRAT HPIPAACGIY YFEVKIVSKG RDGYMGIGLS AQGVNMNRLP GWDKHSYGYH
     GDDGHSFCSS GTGQPYGPTF TTGDVIGCCV NLINNTCFYT KNGHSLGIAF TDLPPNLYPT
     VGLQTPGEVV DANFGQHPFV FDIEDYMREW RTKIQAQIDR FPIGDREGEW QTMIQKMVSS
     YLVHHGYCAT AEAFARSTDQ TVLEELASIK NRQRIQKLVL AGRMGEAIET TQQLYPSLLE
     RNPNLLFTLK VRQFIEMVNG TDSEVRCLGG RSPKSQDSYP VSPRPFSSPS MSPSHGMSIH
     SLAPGKSSTA HFSGFESCSN GVISNKAHQS YCHSKHQLSS LTVPELNSLN VSRSQQVNNF
     TSNDVDMETD HYSNGVGETS SNGFLNGSSK HDHEMEDCDT EMEVDCSQLR RQLCGGSQAA
     IERMIHFGRE LQAMSEQLRR ECGKNTANKK MLKDAFSLLA YSDPWNSPVG NQLDPIQREP
     VCSALNSAIL ETHNLPKQPP LALAMGQATQ CLGLMARSGV GSCAFATVED YLH
//
ID   ZHX1_MOUSE              Reviewed;         873 AA.
AC   P70121; Q8BQ68; Q8C6T4; Q8CJG3;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 2.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=Zinc fingers and homeoboxes protein 1;
GN   Name=Zhx1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Bone marrow stroma;
RX   MEDLINE=96311380; PubMed=8713137; DOI=10.1006/bbrc.1996.1114;
RA   Barthelemy I., Carramolino L., Gutierrez J., Barbero J.L., Marquez G.,
RA   Zaballos A.;
RT   "zhx-1: a novel mouse homeodomain protein containing two zinc-fingers
RT   and five homeodomains.";
RL   Biochem. Biophys. Res. Commun. 224:870-876(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   PubMed=12527199; DOI=10.1016/S0378-1119(02)01093-4;
RA   Shou Z., Yamada K., Inazu T., Kawata H., Hirano S., Mizutani T.,
RA   Yazawa T., Sekiguchi T., Yoshino M., Kajitani T., Okada K.,
RA   Miyamoto K.;
RT   "Genomic structure and analysis of transcriptional regulation of the
RT   mouse zinc-fingers and homeoboxes 1 (ZHX1) gene.";
RL   Gene 302:83-94(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Lung, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INDUCTION.
RX   PubMed=14741719; DOI=10.1016/j.bbrc.2003.12.162;
RA   Shou Z., Yamada K., Kawata H., Yokoyama O., Miyamoto K.;
RT   "A mechanism of induction of the mouse zinc-fingers and homeoboxes 1
RT   (ZHX1) gene expression by interleukin-2.";
RL   Biochem. Biophys. Res. Commun. 314:885-890(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-47; SER-48;
RP   SER-647 AND SER-648, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Acts as a transcriptional repressor (By similarity).
CC   -!- SUBUNIT: Forms homodimers. Also forms heterodimers with ZHX3 which
CC       is a prerequisite for repressor activity and with ZHX2. Interacts
CC       with NFYA. Interacts with ATF7IP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed with highest levels in brain.
CC   -!- INDUCTION: By interleukin-2.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the ZHX family.
CC   -!- SIMILARITY: Contains 2 C2H2-type zinc fingers.
CC   -!- SIMILARITY: Contains 5 homeobox DNA-binding domains.
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DR   EMBL; Z54200; CAA90905.1; -; mRNA.
DR   EMBL; AB078421; BAC22110.1; -; Genomic_DNA.
DR   EMBL; AK051410; BAC34629.1; -; mRNA.
DR   EMBL; AK053191; BAC35306.1; -; mRNA.
DR   EMBL; BC054543; AAH54543.1; -; mRNA.
DR   IPI; IPI00226439; -.
DR   PIR; JC4863; JC4863.
DR   RefSeq; NP_001035903.1; NM_001042438.1.
DR   RefSeq; NP_033598.2; NM_009572.3.
DR   UniGene; Mm.244931; -.
DR   ProteinModelPortal; P70121; -.
DR   SMR; P70121; 60-153, 298-338, 471-517, 565-636, 662-731, 783-827.
DR   STRING; P70121; -.
DR   PhosphoSite; P70121; -.
DR   PRIDE; P70121; -.
DR   Ensembl; ENSMUST00000070143; ENSMUSP00000066201; ENSMUSG00000022361.
DR   Ensembl; ENSMUST00000110168; ENSMUSP00000105797; ENSMUSG00000022361.
DR   GeneID; 22770; -.
DR   KEGG; mmu:22770; -.
DR   UCSC; uc007vtd.1; mouse.
DR   CTD; 22770; -.
DR   MGI; MGI:109271; Zhx1.
DR   eggNOG; roNOG12272; -.
DR   HOVERGEN; HBG007920; -.
DR   InParanoid; P70121; -.
DR   OMA; KHKFLNE; -.
DR   OrthoDB; EOG4KWJS7; -.
DR   PhylomeDB; P70121; -.
DR   NextBio; 303303; -.
DR   ArrayExpress; P70121; -.
DR   Bgee; P70121; -.
DR   CleanEx; MM_ZHX1; -.
DR   Genevestigator; P70121; -.
DR   GermOnline; ENSMUSG00000022361; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; ISS:UniProtKB.
DR   InterPro; IPR001356; Homeobox.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 5.
DR   Pfam; PF00046; Homeobox; 4.
DR   SMART; SM00389; HOX; 5.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF46689; Homeodomain_like; 5.
DR   PROSITE; PS00027; HOMEOBOX_1; FALSE_NEG.
DR   PROSITE; PS50071; HOMEOBOX_2; 4.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; FALSE_NEG.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Homeobox; Metal-binding; Nucleus; Phosphoprotein; Repeat;
KW   Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    873       Zinc fingers and homeoboxes protein 1.
FT                                /FTId=PRO_0000049389.
FT   ZN_FING      70     93       C2H2-type 1.
FT   ZN_FING     102    125       C2H2-type 2.
FT   DNA_BIND    284    346       Homeobox 1.
FT   DNA_BIND    464    526       Homeobox 2.
FT   DNA_BIND    569    630       Homeobox 3.
FT   DNA_BIND    660    722       Homeobox 4.
FT   DNA_BIND    777    832       Homeobox 5.
FT   REGION      272    564       Required for interaction with NFYA (By
FT                                similarity).
FT   REGION      272    432       Required for dimerization (By
FT                                similarity).
FT   REGION      734    768       Required for nuclear localization (By
FT                                similarity).
FT   REGION      831    873       Required for repressor activity (By
FT                                similarity).
FT   MOD_RES      36     36       Phosphothreonine (By similarity).
FT   MOD_RES      45     45       Phosphoserine.
FT   MOD_RES      47     47       Phosphoserine.
FT   MOD_RES      48     48       Phosphoserine.
FT   MOD_RES     289    289       Phosphotyrosine (By similarity).
FT   MOD_RES     303    303       Phosphotyrosine (By similarity).
FT   MOD_RES     635    635       Phosphoserine (By similarity).
FT   MOD_RES     639    639       Phosphoserine (By similarity).
FT   MOD_RES     647    647       Phosphoserine.
FT   MOD_RES     648    648       Phosphoserine.
FT   MOD_RES     682    682       Phosphothreonine (By similarity).
FT   CONFLICT    375    375       S -> T (in Ref. 1 and 2).
FT   CONFLICT    388    388       C -> Y (in Ref. 3; BAC34629).
FT   CONFLICT    553    553       A -> R (in Ref. 1; CAA90905).
FT   CONFLICT    867    868       KL -> NV (in Ref. 1; CAA90905).
SQ   SEQUENCE   873 AA;  97551 MW;  98C5D5714D479364 CRC64;
     MASRRKSTTP CMVLASEQDP DLELISDLDE GPPILTPVEN AKAESVSSDE EVHGSVDSDN
     QQNKKVEGGY ECKYCTFQTP DLNMFTFHVD SEHPNVVLNS SYVCVECNFL TKRYDALSEH
     NLKYHPGEEN FKLTMVKRNN QTIFEQTIND LTFDGSFVKE ENTEQGESID VSSSGISISK
     TPIMKMMKNK VENKRITVHH NSAEGTSEEK ENGVKASQEE NAESVSSSAL ESNTSTSTIN
     RVHPSPASTV VTPTAVLPGL AQVITAVSAQ QNSNLLPKVL IPVNSIPTYN AALDNNPLLL
     NTYNKFPYPT MSEITVLSAQ AKYTEEQIKI WFSAQRLKHG VSWTPEEVEE ARRKQFNGTV
     HTVPQTITVI PTHISTGSNG LPSILQTCQI VGQPGLVLTQ VAGTNTLPVT APIALTVAGV
     PNQTNVQKSQ VPAAQPATDT KPATAAVPSS PSVRPEAALV NPDSFGIRAK KTKEQLAELK
     VSYLKNQFPH DSEIIRLMKI TGLTKGEIKK WFSDTRYNQR NSKSNQCLHL NNDSSATIII
     DSSDETPEPP AAAASQQKQS WNPFPDFAPQ KFKEKTAEQL RALQASFLNS SVLTDEEVNR
     LRAQTKLTRR EIDAWFTEKN KTKALKDEKI EVDESNVGSS KEEPGESSPG DETVAPKSGG
     TGKICKKTPE QLHMLKSAFV RTQWPSAEEY DKLAEESGLA RTDIVSWFGD TRYAWKNGNL
     KWYYYYQSSN SSSLNGLSSL RRRGRGRPKG RGRGRPRGRP RGGKRMNTWD RVPSLIKFKT
     GTAILKDYYL KHKFLNEQDL DELVNRSHMG YEQVREWFAE RQRRSELGIE LFEENEEEDE
     VVDDQEEDEE ETDDSDTWEP PRHVKRKLSK SDD
//
ID   SBDS_MOUSE              Reviewed;         250 AA.
AC   P70122; Q3TG78; Q9CR18;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Ribosome maturation protein SBDS;
DE   AltName: Full=Protein 22A3;
DE   AltName: Full=Shwachman-Bodian-Diamond syndrome protein homolog;
GN   Name=Sbds;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, Liver, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PRELIMINARY PARTIAL NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c; TISSUE=Cochlea;
RA   Crozet F.;
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in the biogenesis of the 60S ribosomal
CC       subunit and translational activation of ribosomes. May trigger the
CC       GTP-dependent release of Eif6 from 60S pre-ribosomes in the
CC       cytoplasm, thereby activating ribosomes for translation competence
CC       by allowing 80S ribosome assembly and facilitating Eif6 recycling
CC       to the nucleus, where it is required for 60S rRNA processing and
CC       nuclear export (By similarity).
CC   -!- SUBUNIT: Associates with the 60S ribosomal subunit (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the SDO1/SBDS family.
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DR   EMBL; AK005079; BAB23803.1; -; mRNA.
DR   EMBL; AK014648; BAB29487.1; -; mRNA.
DR   EMBL; AK019228; BAB31612.1; -; mRNA.
DR   EMBL; AK168847; BAE40670.1; -; mRNA.
DR   EMBL; BC003849; AAH03849.1; -; mRNA.
DR   EMBL; X99668; CAA67982.1; ALT_SEQ; mRNA.
DR   IPI; IPI00136151; -.
DR   RefSeq; NP_075737.1; NM_023248.1.
DR   UniGene; Mm.280484; -.
DR   ProteinModelPortal; P70122; -.
DR   SMR; P70122; 13-239.
DR   STRING; P70122; -.
DR   PRIDE; P70122; -.
DR   Ensembl; ENSMUST00000026387; ENSMUSP00000026387; ENSMUSG00000025337.
DR   GeneID; 66711; -.
DR   KEGG; mmu:66711; -.
DR   NMPDR; fig|10090.3.peg.12524; -.
DR   UCSC; uc008zuj.1; mouse.
DR   CTD; 66711; -.
DR   MGI; MGI:1913961; Sbds.
DR   eggNOG; roNOG12360; -.
DR   GeneTree; ENSGT00390000008135; -.
DR   HOGENOM; HBG333702; -.
DR   HOVERGEN; HBG039762; -.
DR   InParanoid; P70122; -.
DR   OMA; SNVSKGV; -.
DR   OrthoDB; EOG40ZQZH; -.
DR   PhylomeDB; P70122; -.
DR   NextBio; 322437; -.
DR   ArrayExpress; P70122; -.
DR   Bgee; P70122; -.
DR   CleanEx; MM_SBDS; -.
DR   Genevestigator; P70122; -.
DR   GermOnline; ENSMUSG00000025337; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0001833; P:inner cell mass cell proliferation; IMP:MGI.
DR   InterPro; IPR018978; Ribosome_mat_SBDS_C.
DR   InterPro; IPR018023; Ribosome_mat_SBDS_CS.
DR   InterPro; IPR019783; Ribosome_mat_SBDS_N.
DR   InterPro; IPR002140; Ribosome_maturation_pr_SBDS.
DR   PANTHER; PTHR10927; SBDS; 1.
DR   Pfam; PF01172; SBDS; 1.
DR   Pfam; PF09377; SBDS_C; 1.
DR   SUPFAM; SSF89895; Ribosome_mat_SBDS_N; 1.
DR   TIGRFAMs; TIGR00291; SBDS; 1.
DR   PROSITE; PS01267; UPF0023; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Phosphoprotein; Ribosome biogenesis.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    250       Ribosome maturation protein SBDS.
FT                                /FTId=PRO_0000123763.
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES     124    124       Phosphothreonine (By similarity).
FT   MOD_RES     128    128       Phosphotyrosine (By similarity).
SQ   SEQUENCE   250 AA;  28781 MW;  3137CA2807DD250A CRC64;
     MSIFTPTNQI RLTNVAVVRM KRGGKRFEIA CYKNKVVGWR SGVEKDLDEV LQTHSVFVNV
     SKGQVAKKED LISAFGTDDQ TEICKQILTK GEVQVSDKER HTQLEQMFRD IATIVADKCV
     NPETKRPYTV ILIERAMKDI HYSVKPNKST KQQALEVIKQ LKEKMKIERA HMRLRFILPV
     NEGKKLKEKL KPLMKVVESE DYSQQLEIVC LIDPGCFREI DELIKKETKG RGSLEVLSLK
     DVEEGDEKFE
//
ID   IMB1_MOUSE              Reviewed;         876 AA.
AC   P70168; Q62117;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Importin subunit beta-1;
DE   AltName: Full=Karyopherin subunit beta-1;
DE   AltName: Full=Nuclear factor p97;
DE   AltName: Full=Pore targeting complex 97 kDa subunit;
DE            Short=PTAC97;
DE   AltName: Full=SCG;
GN   Name=Kpnb1; Synonyms=Impnb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RX   MEDLINE=96411672; PubMed=8812441; DOI=10.1006/geno.1996.0450;
RA   Matsuda Y., Hamatani K., Itoh M., Takahashi E., Araki R., Abe M.;
RT   "Localization of the importin-beta gene to mouse chromosome 11D and
RT   rat chromosome 10q32.1.";
RL   Genomics 36:213-215(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 74-92; 212-221;
RP   377-389 AND 860-867.
RC   STRAIN=C57BL/6; TISSUE=Thymus;
RX   MEDLINE=95361913; PubMed=7635189; DOI=10.1016/0014-5793(95)00699-A;
RA   Imamoto N., Shimamoto T., Kose S., Takao T., Tachibana T.,
RA   Matsubae M., Sekimoto T., Shimonishi Y., Yoneda Y.;
RT   "The nuclear pore-targeting complex binds to nuclear pores after
RT   association with a karyophile.";
RL   FEBS Lett. 368:415-419(1995).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH HISTONES H2B; H2A; H3 AND H4.
RX   MEDLINE=21385002; PubMed=11493596; DOI=10.1093/embo-reports/kve168;
RA   Muehlhaeusser P., Mueller E.-C., Otto A., Kutay U.;
RT   "Multiple pathways contribute to nuclear import of core histones.";
RL   EMBO Rep. 2:690-696(2001).
RN   [4]
RP   INTERACTION WITH SRY.
RX   PubMed=11535586; DOI=10.1074/jbc.M101668200;
RA   Forwood J.K., Harley V., Jans D.A.;
RT   "The C-terminal nuclear localization signal of the sex-determining
RT   region Y (SRY) high mobility group domain mediates nuclear import
RT   through importin beta 1.";
RL   J. Biol. Chem. 276:46575-46582(2001).
CC   -!- FUNCTION: Functions in nuclear protein import, either in
CC       association with an adapter protein, like an importin-alpha
CC       subunit, which binds to nuclear localization signals (NLS) in
CC       cargo substrates, or by acting as autonomous nuclear transport
CC       receptor. Acting autonomously, serves itself as NLS receptor.
CC       Docking of the importin/substrate complex to the nuclear pore
CC       complex (NPC) is mediated by KPNB1 through binding to nucleoporin
CC       FxFG repeats and the complex is subsequently translocated through
CC       the pore by an energy requiring, Ran-dependent mechanism. At the
CC       nucleoplasmic side of the NPC, Ran binds to importin-beta and the
CC       three components separate and importin-alpha and -beta are re-
CC       exported from the nucleus to the cytoplasm where GTP hydrolysis
CC       releases Ran from importin. The directionality of nuclear import
CC       is thought to be conferred by an asymmetric distribution of the
CC       GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
CC       Mediates autonomously the nuclear import of ribosomal proteins
CC       RPL23A, RPS7 and RPL5. Binds to a beta-like import receptor
CC       binding (BIB) domain of RPL23A. In association with IPO7 mediates
CC       the nuclear import of H1 histone. In vitro, mediates nuclear
CC       import of H2A, H2B, H3 and H4 histones. In case of HIV-1
CC       infection, binds and mediates the nuclear import of HIV-1 Rev.
CC       Imports PRKCI into the nucleus (By similarity).
CC   -!- SUBUNIT: Forms a complex with an importin alpha subunit. Forms a
CC       heterodimer with IPO7. Interacts with IPO7, SNUPN, RPL23A and
CC       XPO1. The KPNB1/IPO7 heterodimer interacts with H1 histone.
CC       Interacts with H2A, H2B, H3 and H4 histones (By similarity).
CC       Component of an import snRNP complex composed of KPNB1, SNUPN,
CC       SMN1 and ZNF259. Component of a nuclear export receptor complex
CC       composed of KPNB1, Ran, SNUPN and XPO1. Binds to HIV-1 Rev and
CC       Tat. Interacts with HTLV-1 Rex. Interacts with SRY. Interacts with
CC       PRKCI/atypical protein kinase C iota (By similarity).
CC   -!- INTERACTION:
CC       Q14974:KPNB1 (xeno); NbExp=1; IntAct=EBI-540580, EBI-286758;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus envelope
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the importin beta family.
CC   -!- SIMILARITY: Contains 8 HEAT repeats.
CC   -!- SIMILARITY: Contains 1 importin N-terminal domain.
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DR   EMBL; D67015; BAA11034.1; -; mRNA.
DR   EMBL; D45836; BAA08273.1; -; mRNA.
DR   IPI; IPI00323881; -.
DR   PIR; S66288; S66288.
DR   RefSeq; NP_032405.3; NM_008379.3.
DR   UniGene; Mm.251013; -.
DR   PDB; 1GCJ; X-ray; 2.60 A; A/B=1-449.
DR   PDB; 1UKL; X-ray; 3.00 A; A/B=1-876.
DR   PDBsum; 1GCJ; -.
DR   PDBsum; 1UKL; -.
DR   ProteinModelPortal; P70168; -.
DR   SMR; P70168; 1-876.
DR   DIP; DIP-33404N; -.
DR   IntAct; P70168; 9.
DR   STRING; P70168; -.
DR   PhosphoSite; P70168; -.
DR   PRIDE; P70168; -.
DR   Ensembl; ENSMUST00000001479; ENSMUSP00000001479; ENSMUSG00000001440.
DR   GeneID; 16211; -.
DR   KEGG; mmu:16211; -.
DR   CTD; 16211; -.
DR   MGI; MGI:107532; Kpnb1.
DR   eggNOG; roNOG05009; -.
DR   HOGENOM; HBG357195; -.
DR   HOVERGEN; HBG002369; -.
DR   InParanoid; P70168; -.
DR   OrthoDB; EOG4RBQHX; -.
DR   PhylomeDB; P70168; -.
DR   ArrayExpress; P70168; -.
DR   Bgee; P70168; -.
DR   CleanEx; MM_KPNB1; -.
DR   Genevestigator; P70168; -.
DR   GermOnline; ENSMUSG00000001440; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR   GO; GO:0008565; F:protein transporter activity; IDA:MGI.
DR   GO; GO:0006610; P:ribosomal protein import into nucleus; IDA:MGI.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000357; HEAT.
DR   InterPro; IPR021133; HEAT_type_2.
DR   InterPro; IPR001494; Importin-beta_N.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF02985; HEAT; 2.
DR   Pfam; PF03810; IBN_N; 1.
DR   SMART; SM00913; IBN_N; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
DR   PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Isopeptide bond; Nucleus; Phosphoprotein; Protein transport; Repeat;
KW   Transport; Ubl conjugation.
FT   CHAIN         1    876       Importin subunit beta-1.
FT                                /FTId=PRO_0000120746.
FT   DOMAIN       21    101       Importin N-terminal.
FT   REPEAT      124    163       HEAT 1.
FT   REPEAT      168    207       HEAT 2.
FT   REPEAT      213    250       HEAT 3.
FT   REPEAT      317    357       HEAT 4.
FT   REPEAT      362    399       HEAT 5.
FT   REPEAT      404    441       HEAT 6.
FT   REPEAT      602    641       HEAT 7.
FT   REPEAT      687    726       HEAT 8.
FT   REGION      329    342       IAB-binding.
FT   REGION      334    419       Ran-GTP binding (By similarity).
FT   COMPBIAS    337    341       Poly-Asp.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      12     12       Phosphoserine (By similarity).
FT   MOD_RES     211    211       N6-acetyllysine (By similarity).
FT   MOD_RES     835    835       N6-acetyllysine (By similarity).
FT   MOD_RES     867    867       N6-acetyllysine (By similarity).
FT   CROSSLNK    206    206       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK    211    211       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CONFLICT    388    388       V -> M (in Ref. 2; BAA08273).
FT   HELIX         1      7
FT   TURN          8     11
FT   HELIX        15     45
FT   HELIX        51     62
FT   TURN         63     65
FT   HELIX        70     82
FT   HELIX        85     98
FT   STRAND      104    106
FT   HELIX       108    120
FT   HELIX       121    123
FT   HELIX       129    138
FT   HELIX       144    160
FT   HELIX       163    166
FT   HELIX       167    169
FT   HELIX       170    181
FT   HELIX       188    201
FT   TURN        202    204
FT   HELIX       206    209
FT   HELIX       212    225
FT   HELIX       231    247
FT   HELIX       249    254
FT   TURN        255    259
FT   HELIX       260    268
FT   HELIX       273    302
FT   HELIX       314    329
FT   HELIX       330    332
FT   STRAND      338    340
FT   HELIX       344    359
FT   HELIX       360    362
FT   HELIX       363    374
FT   HELIX       380    392
FT   STRAND      394    397
FT   HELIX       399    416
FT   HELIX       422    438
FT   HELIX       440    444
FT   STRAND      447    450
FT   HELIX       452    459
FT   HELIX       464    485
FT   HELIX       486    488
FT   STRAND      491    495
FT   HELIX       500    514
FT   TURN        517    520
FT   HELIX       521    523
FT   HELIX       524    537
FT   HELIX       544    563
FT   HELIX       564    567
FT   HELIX       571    592
FT   HELIX       597    616
FT   HELIX       625    639
FT   TURN        640    643
FT   HELIX       644    648
FT   HELIX       651    659
FT   HELIX       661    663
FT   HELIX       664    680
FT   HELIX       682    685
FT   HELIX       686    701
FT   STRAND      703    705
FT   HELIX       709    724
FT   HELIX       725    728
FT   HELIX       729    743
FT   HELIX       753    777
FT   STRAND      779    782
FT   HELIX       785    790
FT   HELIX       793    806
FT   HELIX       812    828
FT   HELIX       834    838
FT   HELIX       841    849
FT   HELIX       856    871
FT   HELIX       872    875
SQ   SEQUENCE   876 AA;  97152 MW;  B540764C526419E9 CRC64;
     MELITILEKT VSPDRLELEA AQKFLERAAV ENLPTFLVEL SRVLANPGNS QVARVAAGLQ
     IKNSLTSKDP DIKAQYQQRW LAIDANARRE VKNYVLQTLG TETYRPSSAS QCVAGIACAE
     IPVSQWPELI PQLVANVTNP NSTEHMKEST LEAIGYICQD IDPEQLQDKS NEILTAIIQG
     MRKEEPSNNV KLAATNALLN SLEFTKANFD KESERHFIMQ VVCEATQCPD TRVRVAALQN
     LVKIMSLYYQ YMETYMGPAL FAITIEAMKS DIDEVALQGI EFWSNVCDEE MDLAIEASEA
     AEQGRPPEHT SKFYAKGALQ YLVPILTQTL TKQDENDDDD DWNPCKAAGV CLMLLSTCCE
     DDIVPHVLPF IKEHIKNPDW RYRDAAVVAF GSILEGPEPN QLKPLVIQAM PTLIELMKDP
     SVVVRDTTAW TVGRICELLP EAAINDVYLA PLLQCLIEGL SAEPRVASNV CWAFSSLAEA
     AYEAADVADD QEEPATYCLS SSFELIVQKL LETTDRPDGH QNNLRSSAYE SLMEIVKNSA
     KDCYPAVQKT TLVIMERLQQ VLQMESHIQS TSDRIQFNDL QSLLCATLQN VLRKVQHQDA
     LQISDVVMAS LLRMFQSTAG SGGVQEDALM AVSTLVEVLG GEFLKYMEAF KPFLGIGLKN
     YAEYQVCLAA VGLVGDLCRA LQSNILPFCD EVMQLLLENL GNENVHRSVK PQILSVFGDI
     ALAIGGEFKK YLEVVLNTLQ QASQAQVDKS DFDMVDYLNE LRESCLEAYT GIVQGLKGDQ
     ENVHPDVMLV QPRVEFILSF IDHIAGDEDH TDGVVACAAG LIGDLCTAFG KDVLKLVEAR
     PMIHELLTEG RRSKTNKAKT LATWATKELR KLKNQA
//
ID   DOC2B_MOUSE             Reviewed;         412 AA.
AC   P70169; Q6NXK3;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Double C2-like domain-containing protein beta;
DE            Short=Doc2-beta;
GN   Name=Doc2b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Cerebellum;
RX   MEDLINE=97058315; PubMed=8902635;
RA   Kojima T., Fukuda M., Aruga J., Mikoshiba K.;
RT   "Calcium-dependent phospholipid binding to the C2A domain of a
RT   ubiquitous form of double C2 protein (Doc2 beta).";
RL   J. Biochem. 120:671-676(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   SUBCELLULAR LOCATION, INTERACTION WITH STXBP3, AND TISSUE SPECIFICITY.
RX   PubMed=17548353; DOI=10.1074/jbc.M701661200;
RA   Ke B., Oh E., Thurmond D.C.;
RT   "Doc2beta is a novel Munc18c-interacting partner and positive effector
RT   of syntaxin 4-mediated exocytosis.";
RL   J. Biol. Chem. 282:21786-21797(2007).
RN   [4]
RP   INTERACTION WITH STX1A AND SNAP25.
RX   PubMed=18596155; DOI=10.1523/JNEUROSCI.0538-08.2008;
RA   Friedrich R., Groffen A.J., Connell E., van Weering J.R., Gutman O.,
RA   Henis Y.I., Davletov B., Ashery U.;
RT   "DOC2B acts as a calcium switch and enhances vesicle fusion.";
RL   J. Neurosci. 28:6794-6806(2008).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH STX4.
RX   PubMed=19410553; DOI=10.1016/j.bbrc.2009.04.133;
RA   Miyazaki M., Emoto M., Fukuda N., Hatanaka M., Taguchi A.,
RA   Miyamoto S., Tanizawa Y.;
RT   "DOC2b is a SNARE regulator of glucose-stimulated delayed insulin
RT   secretion.";
RL   Biochem. Biophys. Res. Commun. 384:461-465(2009).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STX4, AND MUTAGENESIS
RP   OF ASP-157; ASP-163; ASP-297 AND ASP-303.
RX   PubMed=19033398; DOI=10.2337/db08-0303;
RA   Fukuda N., Emoto M., Nakamori Y., Taguchi A., Miyamoto S., Uraki S.,
RA   Oka Y., Tanizawa Y.;
RT   "DOC2B: a novel syntaxin-4 binding protein mediating insulin-regulated
RT   GLUT4 vesicle fusion in adipocytes.";
RL   Diabetes 58:377-384(2009).
RN   [7]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=20150444; DOI=10.1126/science.1183765;
RA   Groffen A.J., Martens S., Diez Arazola R., Cornelisse L.N.,
RA   Lozovaya N., de Jong A.P., Goriounova N.A., Habets R.L., Takai Y.,
RA   Borst J.G., Brose N., McMahon H.T., Verhage M.;
RT   "Doc2b is a high-affinity Ca2+ sensor for spontaneous neurotransmitter
RT   release.";
RL   Science 327:1614-1618(2010).
CC   -!- FUNCTION: Calcium sensor which positively regulates SNARE-
CC       dependent fusion of vesicles with membranes. Binds phospholipids
CC       in a calcium-dependent manner and may act at the priming stage of
CC       fusion by modifying membrane curvature to stimulate fusion.
CC       Involved in calcium-triggered exocytosis in chromaffin cells and
CC       calcium-dependent spontaneous release of neurotransmitter in
CC       absence of action potentials in neuronal cells. Involved both in
CC       glucose-stimulated insulin secretion in pancreatic cells and
CC       insulin-dependent GLUT4 transport to the plasma membrane in
CC       adipocytes.
CC   -!- SUBUNIT: Interacts with cytoplasmic dynein light chain DYNLT1. May
CC       interact with UNC13A; the interaction mediates targeting to the
CC       plasma membrane (By similarity). Probably interacts with the SNARE
CC       (soluble N-ethylmaleimide-sensitive factor attached protein
CC       receptor) complex composed of SNAP25, STX1A and VAMP2; the
CC       interaction is calcium-dependent and competitive with SYT1.
CC       Interacts with STX4; the interaction is calcium-dependent,
CC       increased by insulin and glucose, and mediates vesicle fusion with
CC       plasma membrane in pancretic cells and adipocytes. Interacts with
CC       STXBP3; the interaction is direct, occurs at the cell membrane and
CC       regulates glucose-stimulated insulin secretion.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasmic granule. Cell
CC       membrane; Peripheral membrane protein. Note=Translocates to the
CC       plasma membrane in a calcium-dependent manner.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed in pancreatic
CC       islet cells (at protein level).
CC   -!- DOMAIN: C2 domain 1 is involved in binding calcium and
CC       phospholipids. According to PubMed:19033398, the C2 domain 2 may
CC       also play a role in the calcium-dependent targeting to membranes.
CC   -!- DISRUPTION PHENOTYPE: Mice are viable and fertile without gross
CC       abnormalities.
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; D85037; BAA12714.1; -; mRNA.
DR   EMBL; BC067030; AAH67030.1; -; mRNA.
DR   IPI; IPI00136301; -.
DR   PIR; JC4921; JC4921.
DR   RefSeq; NP_031899.2; NM_007873.2.
DR   UniGene; Mm.5137; -.
DR   ProteinModelPortal; P70169; -.
DR   SMR; P70169; 126-404.
DR   STRING; P70169; -.
DR   PhosphoSite; P70169; -.
DR   PRIDE; P70169; -.
DR   Ensembl; ENSMUST00000021209; ENSMUSP00000021209; ENSMUSG00000020848.
DR   GeneID; 13447; -.
DR   KEGG; mmu:13447; -.
DR   CTD; 13447; -.
DR   MGI; MGI:1100497; Doc2b.
DR   eggNOG; maNOG17872; -.
DR   HOGENOM; HBG716633; -.
DR   HOVERGEN; HBG051388; -.
DR   InParanoid; P70169; -.
DR   OrthoDB; EOG4Z0B5S; -.
DR   NextBio; 283895; -.
DR   ArrayExpress; P70169; -.
DR   Bgee; P70169; -.
DR   CleanEx; MM_DOC2B; -.
DR   Genevestigator; P70169; -.
DR   GermOnline; ENSMUSG00000020848; Mus musculus.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0008021; C:synaptic vesicle; IEA:InterPro.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; ISS:UniProtKB.
DR   GO; GO:0019905; F:syntaxin binding; IPI:UniProtKB.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   GO; GO:0048791; P:calcium ion-dependent exocytosis of neurotransmitter; IMP:UniProtKB.
DR   GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; ISS:UniProtKB.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; IMP:UniProtKB.
DR   GO; GO:0031340; P:positive regulation of vesicle fusion; ISS:UniProtKB.
DR   GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   InterPro; IPR014638; Doc2.
DR   InterPro; IPR001565; Synaptotagmin.
DR   Pfam; PF00168; C2; 2.
DR   PIRSF; PIRSF036931; Doc2; 1.
DR   PRINTS; PR00360; C2DOMAIN.
DR   PRINTS; PR00399; SYNAPTOTAGMN.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 2.
PE   1: Evidence at protein level;
KW   Calcium; Calcium/phospholipid-binding; Cell membrane; Cytoplasm;
KW   Membrane; Repeat.
FT   CHAIN         1    412       Double C2-like domain-containing protein
FT                                beta.
FT                                /FTId=PRO_0000079969.
FT   DOMAIN      128    232       C2 1.
FT   DOMAIN      268    371       C2 2.
FT   REGION        1     90       Mediates interaction with DYNLT1 (By
FT                                similarity).
FT   REGION        1     36       Negatively regulates targeting to plasma
FT                                membrane.
FT   REGION      257    375       Mediates interaction with STXBP3.
FT   MUTAGEN     157    157       D->N: Loss of interaction with STX4 and
FT                                insulin-dependent translocation to the
FT                                cell membrane; when assoicated with N-
FT                                163, N-297 and N-303.
FT   MUTAGEN     163    163       D->N: Loss of interaction with STX4 and
FT                                insulin-dependent translocation to the
FT                                cell membrane; when assoicated with N-
FT                                157, N-297 and N-303.
FT   MUTAGEN     297    297       D->N: Loss of interaction with STX4 and
FT                                insulin-dependent translocation to the
FT                                cell membrane; when assoicated with N-
FT                                157, N-163 and N-303.
FT   MUTAGEN     303    303       D->N: Loss of interaction with STX4 and
FT                                insulin-dependent translocation to the
FT                                cell membrane; when assoicated with N-
FT                                157, N-163 and N-297.
FT   CONFLICT    389    389       N -> K (in Ref. 2; AAH67030).
SQ   SEQUENCE   412 AA;  45839 MW;  BEC1480BEDE91724 CRC64;
     MTLRRRGEKA TISIQEHMAI DVCPGPIRPI KQISDYFPRF PRGLPPTAAP RAPAPPDAPA
     RSPAASASPR SPSDGARDDD EDVDQLFGAY GASPGPSPGP SPARPPAKPP EDEPDVDGYE
     SDDCTALGTL DFSLLYDQEN NALHCTISKA KGLKPMDHNG LADPYVKLHL LPGASKANKL
     RTKTLRNTLN PSWNETLTYY GITDEDMVRK TLRISVCDED KFRHNEFIGE TRVPLKKLKP
     NHTKTFSICL EKQLPVDKAE DKSLEERGRI LISLKYSSQK QGLLVGIVRC AHLAAMDANG
     YSDPYVKTYL KPDVDKKSKH KTAVKKKTLN PEFNEEFCYE IKHGDLAKKT LEVTVWDYDI
     GKSNDFIGGV VLGINAKGER LKHWFDCLNN KDKRIERWHT LTNELPGAVL SD
//
ID   HRH1_MOUSE              Reviewed;         488 AA.
AC   P70174; Q91V75; Q91XN0; Q91XN1; Q91XN2; Q91XN3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   09-MAY-2003, sequence version 2.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=Histamine H1 receptor;
DE            Short=H1R;
DE            Short=HH1R;
GN   Name=Hrh1; Synonyms=Bphs;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Ola;
RX   MEDLINE=96411663; PubMed=8812432; DOI=10.1006/geno.1996.0441;
RA   Inoue I., Taniuchi I., Kitamura D., Jenkins N.A., Gilbert D.J.,
RA   Copeland N.G., Watanabe T.;
RT   "Characteristics of the mouse genomic histamine H1 receptor gene.";
RL   Genomics 36:178-181(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE, AND VARIANTS LEU-263; MET-312 AND SER-330.
RC   STRAIN=129/SvJ, A/J, B10.S/DvTe, BALB/cByJ, BALB/cJ, C3H/HeJ,
RC   C57BL/6J, CBA/J, DBA/1, DBA/2, FVB/NCr, NOD, SJL, and SWR;
RC   TISSUE=Spleen;
RX   MEDLINE=22138444; PubMed=12142541; DOI=10.1126/science.1072810;
RA   Ma R.Z., Gao J., Meeker N.D., Fillmore P.D., Tung K.S.K., Watanabe T.,
RA   Zachary J.F., Offner H., Blankenhorn E.P., Teuscher C.;
RT   "Identification of Bphs, an autoimmune disease locus, as histamine
RT   receptor H1.";
RL   Science 297:620-623(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Adipose tissue, Cerebellum, Hypothalamus, and Mesonephros;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   FUNCTION.
RX   MEDLINE=97075162; PubMed=8917588; DOI=10.1073/pnas.93.23.13316;
RA   Inoue I., Yanai K., Kitamura D., Taniuchi I., Kobayashi T.,
RA   Niimura K., Watanabe T., Watanabe T.;
RT   "Impaired locomotor activity and exploratory behavior in mice lacking
RT   histamine H1 receptors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:13316-13320(1996).
RN   [5]
RP   FUNCTION.
RX   MEDLINE=22483683; PubMed=12595443;
RX   DOI=10.1128/IAI.71.3.1281-1287.2003;
RA   Gao J.F., Call S.B., Fillmore P.D., Watanabe T., Meeker N.D.,
RA   Teuscher C.;
RT   "Analysis of the role of Bphs/Hrh1 in the genetic control of
RT   responsiveness to pertussis toxin.";
RL   Infect. Immun. 71:1281-1287(2003).
CC   -!- FUNCTION: In peripheral tissues, the H1 subclass of histamine
CC       receptors mediates the contraction of smooth muscles, increase in
CC       capillary permeability due to contraction of terminal venules, and
CC       catecholamine release from adrenal medulla, as well as mediating
CC       neurotransmission in the central nervous system. Involved in
CC       circadian rhythm of locomotor activity and exploratory behavior.
CC       Also involved in responsiveness to pertussis toxin through its
CC       control of susceptibility to histamine hypersensitivity and
CC       enhancement of antigen-specific delayed-type hypersensitivity
CC       responses.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- PTM: Potential sites of phosphorylation in the third cytoplasmic
CC       loop may play an important role in regulating signal transduction
CC       through the receptor molecule.
CC   -!- POLYMORPHISM: Strains C3H/HeJ and CBA/J are resistant to
CC       vasoactive amine sensitization elicited by histamine (VAASH) which
CC       is induced by pertussis toxin.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; D50095; BAA08791.1; -; Genomic_DNA.
DR   EMBL; AF387890; AAK71654.1; -; mRNA.
DR   EMBL; AF387891; AAK71655.1; -; mRNA.
DR   EMBL; AF387892; AAK71656.1; -; mRNA.
DR   EMBL; AF387893; AAK71657.1; -; mRNA.
DR   EMBL; AF387894; AAK71658.1; -; mRNA.
DR   EMBL; AF387895; AAK71659.1; -; mRNA.
DR   EMBL; AF387896; AAK71660.1; -; mRNA.
DR   EMBL; AF388052; AAK66774.2; -; mRNA.
DR   EMBL; AF388053; AAK66775.1; -; mRNA.
DR   EMBL; AF388054; AAK66776.1; -; mRNA.
DR   EMBL; AF388055; AAK66777.1; -; mRNA.
DR   EMBL; AF388056; AAK66778.1; -; mRNA.
DR   EMBL; AF388057; AAK66779.1; -; mRNA.
DR   EMBL; AF388058; AAK66780.1; -; mRNA.
DR   EMBL; AK032763; BAC28011.1; -; mRNA.
DR   EMBL; AK038480; BAC30013.1; -; mRNA.
DR   EMBL; AK046607; BAC32805.1; -; mRNA.
DR   EMBL; AK047070; BAC32950.1; -; mRNA.
DR   IPI; IPI00136348; -.
DR   RefSeq; NP_032311.2; NM_008285.3.
DR   UniGene; Mm.333327; -.
DR   ProteinModelPortal; P70174; -.
DR   SMR; P70174; 27-486.
DR   STRING; P70174; -.
DR   PhosphoSite; P70174; -.
DR   PRIDE; P70174; -.
DR   Ensembl; ENSMUST00000088987; ENSMUSP00000086383; ENSMUSG00000053004.
DR   Ensembl; ENSMUST00000112991; ENSMUSP00000108615; ENSMUSG00000053004.
DR   GeneID; 15465; -.
DR   KEGG; mmu:15465; -.
DR   UCSC; uc009dhw.1; mouse.
DR   CTD; 15465; -.
DR   MGI; MGI:107619; Hrh1.
DR   eggNOG; roNOG14740; -.
DR   GeneTree; ENSGT00560000076730; -.
DR   HOGENOM; HBG447339; -.
DR   HOVERGEN; HBG101103; -.
DR   InParanoid; P70174; -.
DR   OMA; LHMFTIW; -.
DR   OrthoDB; EOG4P2Q2Z; -.
DR   PhylomeDB; P70174; -.
DR   NextBio; 288290; -.
DR   ArrayExpress; P70174; -.
DR   Bgee; P70174; -.
DR   CleanEx; MM_HRH1; -.
DR   Genevestigator; P70174; -.
DR   GermOnline; ENSMUSG00000053004; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004969; F:histamine receptor activity; IEA:InterPro.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR000921; Histamine_H1_recept.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00530; HISTAMINEH1R.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Biological rhythms; Cell membrane; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
KW   Palmitate; Phosphoprotein; Polymorphism; Receptor; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    488       Histamine H1 receptor.
FT                                /FTId=PRO_0000069677.
FT   TOPO_DOM      1     29       Extracellular (Potential).
FT   TRANSMEM     30     49       Helical; Name=1; (Potential).
FT   TOPO_DOM     50     63       Cytoplasmic (Potential).
FT   TRANSMEM     64     83       Helical; Name=2; (Potential).
FT   TOPO_DOM     84    101       Extracellular (Potential).
FT   TRANSMEM    102    123       Helical; Name=3; (Potential).
FT   TOPO_DOM    124    145       Cytoplasmic (Potential).
FT   TRANSMEM    146    165       Helical; Name=4; (Potential).
FT   TOPO_DOM    166    189       Extracellular (Potential).
FT   TRANSMEM    190    210       Helical; Name=5; (Potential).
FT   TOPO_DOM    211    419       Cytoplasmic (Potential).
FT   TRANSMEM    420    439       Helical; Name=6; (Potential).
FT   TOPO_DOM    440    451       Extracellular (Potential).
FT   TRANSMEM    452    471       Helical; Name=7; (Potential).
FT   TOPO_DOM    472    488       Cytoplasmic (Potential).
FT   MOD_RES     255    255       Phosphoserine (By similarity).
FT   MOD_RES     275    275       Phosphoserine (By similarity).
FT   LIPID       446    446       S-palmitoyl cysteine (Potential).
FT   CARBOHYD      5      5       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     18     18       N-linked (GlcNAc...) (Potential).
FT   DISULFID    100    180       By similarity.
FT   VARIANT     263    263       P -> L (in strain: C3H/HeJ and CBA/J).
FT   VARIANT     312    312       V -> M (in strain: C3H/HeJ and CBA/J).
FT   VARIANT     330    330       P -> S (in strain: C3H/HeJ and CBA/J).
FT   CONFLICT      2      2       S -> R (in Ref. 1; BAA08791).
FT   CONFLICT     47     47       L -> G (in Ref. 1; BAA08791).
FT   CONFLICT     79     79       V -> I (in Ref. 1; BAA08791).
FT   CONFLICT    215    216       KA -> NG (in Ref. 1; BAA08791).
FT   CONFLICT    224    224       R -> P (in Ref. 1; BAA08791).
FT   CONFLICT    242    242       E -> D (in Ref. 2; AAK66778).
FT   CONFLICT    244    244       A -> S (in Ref. 1; BAA08791).
FT   CONFLICT    261    261       K -> T (in Ref. 1; BAA08791).
FT   CONFLICT    278    278       E -> A (in Ref. 1; BAA08791).
FT   CONFLICT    379    379       S -> R (in Ref. 1; BAA08791).
SQ   SEQUENCE   488 AA;  55682 MW;  82612DF712998B41 CRC64;
     MSLPNTSSAS EDKMCEGNRT AMASPQLLPL VVVLSSISLV TVGLNLLVLY AVRSERKLHT
     VGNLYIVSLS VADLIVGAVV MPMNILYLIM TKWSLGRPLC LFWLSMDYVA STASIFSVFI
     LCIDRYRSVQ QPLRYLRYRT KTRASATILG AWFLSFLWVI PILGWHHFTP LAPELREDKC
     ETDFYNVTWF KIMTAIINFY LPTLLMLWFY VKIYKAVRRH CQHRQLTNGS LPTFLEIKLR
     SEDAKEGAKK PGKESPWGVQ KRPSRDPTGG LDQKSTSEDP KVTSPTVFSQ EGERETVTRP
     CFRLDVMQTQ PVPEGDARGS KANDQTLSQP KMDEQSLSTC RRISETSEDQ TLVDRQSFSR
     TTDSDTSIEP GLGKVKARSR SNSGLDYIKV TWKRLRSHSR QYVSGLHLNR ERKAAKQLGC
     IMAAFILCWI PYFIFFMVIA FCNSCCSEPV HMFTIWLGYI NSTLNPLIYP LCNENFKKTF
     KKILHIRS
//
ID   DLG3_MOUSE              Reviewed;         849 AA.
AC   P70175;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-FEB-2011, entry version 98.
DE   RecName: Full=Disks large homolog 3;
DE   AltName: Full=Synapse-associated protein 102;
DE            Short=SAP-102;
DE            Short=SAP102;
GN   Name=Dlg3; Synonyms=Dlgh3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Kohmura N., Makino S., Yagi T.;
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-705, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [3]
RP   INTERACTION WITH NETO1.
RX   PubMed=19243221; DOI=10.1371/journal.pbio.1000041;
RA   Ng D., Pitcher G.M., Szilard R.K., Sertie A., Kanisek M.,
RA   Clapcote S.J., Lipina T., Kalia L.V., Joo D., McKerlie C., Cortez M.,
RA   Roder J.C., Salter M.W., McInnes R.R.;
RT   "Neto1 is a novel CUB-domain NMDA receptor-interacting protein
RT   required for synaptic plasticity and learning.";
RL   PLoS Biol. 7:E41-E41(2009).
CC   -!- FUNCTION: Required for learning most likely through its role in
CC       synaptic plasticity following NMDA receptor signaling (By
CC       similarity).
CC   -!- SUBUNIT: Interacts through its PDZ domains with NETO1, GRIN2B,
CC       SYNGAP1 and APC. Interacts through its first two PDZ domains with
CC       ERBB4. Interacts through its third PDZ domain with NLGN1, and
CC       probably with NLGN2 and NLGN3. Interacts through its guanylate
CC       kinase-like domain with DLGAP1, DLGAP2, DLGAP3 and DLGAP4 (By
CC       similarity). Interacts with FRMPD4 (via C-terminus) (By
CC       similarity). Interacts with LRFN1, LRFN2 and LRFN4 (By
CC       similarity).
CC   -!- INTERACTION:
CC       Q62108:Dlg4; NbExp=1; IntAct=EBI-396969, EBI-300895;
CC       Q80TG9:Lrfn2; NbExp=1; IntAct=EBI-396969, EBI-877092;
CC   -!- SIMILARITY: Belongs to the MAGUK family.
CC   -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC   -!- SIMILARITY: Contains 3 PDZ (DHR) domains.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; D87117; BAA13249.1; -; mRNA.
DR   IPI; IPI00136350; -.
DR   RefSeq; NP_058027.1; NM_016747.3.
DR   UniGene; Mm.4615; -.
DR   ProteinModelPortal; P70175; -.
DR   SMR; P70175; 144-493, 522-849.
DR   DIP; DIP-31585N; -.
DR   IntAct; P70175; 13.
DR   MINT; MINT-136046; -.
DR   STRING; P70175; -.
DR   PhosphoSite; P70175; -.
DR   PRIDE; P70175; -.
DR   Ensembl; ENSMUST00000087984; ENSMUSP00000085299; ENSMUSG00000000881.
DR   GeneID; 53310; -.
DR   KEGG; mmu:53310; -.
DR   UCSC; uc009twm.1; mouse.
DR   CTD; 53310; -.
DR   MGI; MGI:1888986; Dlg3.
DR   GeneTree; ENSGT00560000076879; -.
DR   HOGENOM; HBG671982; -.
DR   HOVERGEN; HBG107814; -.
DR   InParanoid; P70175; -.
DR   NextBio; 310085; -.
DR   ArrayExpress; P70175; -.
DR   Bgee; P70175; -.
DR   CleanEx; MM_DLG3; -.
DR   Genevestigator; P70175; -.
DR   GermOnline; ENSMUSG00000000881; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR016313; M-assoc_guanylate_kinase.
DR   InterPro; IPR019590; MAGUK_PEST_N.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR019583; PDZ_assoc.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF10608; MAGUK_N_PEST; 1.
DR   Pfam; PF00595; PDZ; 3.
DR   Pfam; PF10600; PDZ_assoc; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PIRSF; PIRSF001741; MAGUK_DLGH; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 3.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50156; PDZ; 3.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 3.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein; Repeat; SH3 domain.
FT   CHAIN         1    849       Disks large homolog 3.
FT                                /FTId=PRO_0000094558.
FT   DOMAIN      149    235       PDZ 1.
FT   DOMAIN      244    330       PDZ 2.
FT   DOMAIN      404    484       PDZ 3.
FT   DOMAIN      519    589       SH3.
FT   DOMAIN      659    834       Guanylate kinase-like.
FT   MOD_RES     705    705       Phosphotyrosine.
FT   MOD_RES     797    797       N6-acetyllysine (By similarity).
FT   MOD_RES     840    840       Phosphotyrosine (By similarity).
SQ   SEQUENCE   849 AA;  93482 MW;  EF3EF2D7513538EE CRC64;
     MHKHQHCCKC PECYEVTRLA ALRRLEPPGY GDWQVPDPYG PSGGNGASSG YGGYSSQTLP
     SQAGATPTPR TKAKLIPTGR DVGPVPPKPV PGKSTPKLNG SGPGWWPECT CTNRDWYEQA
     SPAPLLVNPE ALEPSLSVNG SDGMFKYEEI VLERGNSGLG FSIAGGIDNP HVPDDPGIFI
     TKIIPGGAAA MDGRLGVNDC VLRVNEVDVS EVVHSRAVEA LKEAGPVVRL VVRRRQPPPE
     TIMEVNLLKG PKGLGFSIAG GIGNQHIPGD NSIYITKIIE GGAAQKDGRL QIGDRLLAVN
     NTNLQDVRHE EAVASLKNTS DMVYLKVAKP GSIHLNDMYA PPDYASTFTA LADNHISHNS
     SLGYLGAVES KVTYPAPPQV PPTRYSPIPR HMLAEEDFTR EPRKIILHKG STGLGFNIVG
     GEDGEGIFVS FILAGGPADL SGELRRGDRI LSVNGVNLRN ATHEQAAAAL KRAGQSVTIV
     AQYRPEEYSR FESKIHDLRE QMMNSSMSSG SGSLRTSEKR SLYVRALFDY DRTRDSCLPS
     QGLSFSYGDI LHVINASDDE WWQARLVTPH GESEQIGVIP SKKRVEKKER ARLKTVKFHA
     RTGMIESNRD FPGLSDDYYG AKNLKGVTSN TSDSESSSKG QEDAILSYEP VTRQEIHYAR
     PVIILGPMKD RVNDDLISEF PHKFGSCVPH TTRPRRDNEV DGQDYHFVVS REQMEKDIQD
     NKFIEAGQFN DNLYGTSIQS VRAVAERGKH CILDVSGNAI KRLQQAQLYP IAIFIKPKSI
     EALMEMNRRQ TYEQANKIFD KAMKLEQEFG EYFTAIVQGD SLEEIYNKIK QIIEDQSGHY
     IWVPSPEKL
//
ID   PI51B_MOUSE             Reviewed;         539 AA.
AC   P70181; O70335; Q8JZY6;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Phosphatidylinositol-4-phosphate 5-kinase type-1 beta;
DE            Short=PIP5K1-beta;
DE            Short=PtdIns(4)P-5-kinase 1 beta;
DE            EC=2.7.1.68;
DE   AltName: Full=Phosphatidylinositol-4-phosphate 5-kinase type I alpha;
DE            Short=PIP5KIalpha;
DE   AltName: Full=Phosphatidylinositol-4-phosphate 5-kinase type I beta;
DE            Short=PIP5KIbeta;
GN   Name=Pip5k1b; Synonyms=Pip5k1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION,
RP   AND TISSUE SPECIFICITY.
RC   TISSUE=Insulinoma;
RX   MEDLINE=96394468; PubMed=8798574; DOI=10.1074/jbc.271.39.23611;
RA   Ishihara H., Shibasaki Y., Kizuki N., Katagiri H., Yazaki Y.,
RA   Asano T., Oka Y.;
RT   "Cloning of cDNAs encoding two isoforms of 68-kDa type I
RT   phosphatidylinositol 4-phosphate 5-kinase.";
RL   J. Biol. Chem. 271:23611-23614(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Machesky L.M.;
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Amnion, Heart, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   MUTAGENESIS OF LYS-138, ENZYME REGULATION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   MEDLINE=98204859; PubMed=9535851; DOI=10.1074/jbc.273.15.8741;
RA   Ishihara H., Shibasaki Y., Kizuki N., Wada T., Yazaki Y., Asano T.,
RA   Oka Y.;
RT   "Type I phosphatidylinositol-4-phosphate 5-kinases. Cloning of the
RT   third isoform and deletion/substitution analysis of members of this
RT   novel lipid kinase family.";
RL   J. Biol. Chem. 273:8741-8748(1998).
RN   [6]
RP   FUNCTION, INTERACTION WITH RAC1, AND MUTAGENESIS OF ASP-227.
RX   MEDLINE=20146116; PubMed=10679324; DOI=10.1016/S0960-9822(00)00315-8;
RA   Tolias K.F., Hartwig J.H., Ishihara H., Shibasaki Y., Cantley L.C.,
RA   Carpenter C.L.;
RT   "Type Ialpha phosphatidylinositol-4-phosphate 5-kinase mediates Rac-
RT   dependent actin assembly.";
RL   Curr. Biol. 10:153-156(2000).
CC   -!- FUNCTION: Participates in the biosynthesis of
CC       phosphatidylinositol-4,5-bisphosphate. Mediates RAC1-dependent
CC       reorganization of actin filaments.
CC   -!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 4-
CC       phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
CC   -!- ENZYME REGULATION: Activated by phosphatidic acid.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=34 uM for PtdIns(4)P;
CC         KM=27 uM for ATP;
CC   -!- SUBUNIT: Interacts with RAC1.
CC   -!- INTERACTION:
CC       Q9Z1Q5:Clic1; NbExp=2; IntAct=EBI-645167, EBI-645184;
CC       Q9QYB1:Clic4; NbExp=3; IntAct=EBI-645167, EBI-645175;
CC   -!- SUBCELLULAR LOCATION: Endomembrane system (By similarity).
CC       Note=Associated with membranes (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P70181-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P70181-2; Sequence=VSP_016012;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and testis. Barely
CC       detectable in liver and skeletal muscle.
CC   -!- SIMILARITY: Contains 1 PIPK domain.
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DR   EMBL; D86176; BAA13030.1; -; mRNA.
DR   EMBL; AF048695; AAC05374.1; -; mRNA.
DR   EMBL; AK149354; BAE28830.1; -; mRNA.
DR   EMBL; AK164552; BAE37836.1; -; mRNA.
DR   EMBL; AK146100; BAE26901.1; -; mRNA.
DR   EMBL; BC034864; AAH34864.1; -; mRNA.
DR   IPI; IPI00117305; -.
DR   IPI; IPI00170400; -.
DR   RefSeq; NP_032872.1; NM_008846.2.
DR   UniGene; Mm.217214; -.
DR   ProteinModelPortal; P70181; -.
DR   SMR; P70181; 25-394.
DR   IntAct; P70181; 7.
DR   STRING; P70181; -.
DR   PhosphoSite; P70181; -.
DR   PRIDE; P70181; -.
DR   Ensembl; ENSMUST00000025800; ENSMUSP00000025800; ENSMUSG00000024867.
DR   Ensembl; ENSMUST00000112673; ENSMUSP00000108292; ENSMUSG00000024867.
DR   GeneID; 18719; -.
DR   KEGG; mmu:18719; -.
DR   UCSC; uc008hap.1; mouse.
DR   CTD; 18719; -.
DR   MGI; MGI:107930; Pip5k1b.
DR   eggNOG; roNOG13429; -.
DR   GeneTree; ENSGT00550000074279; -.
DR   HOGENOM; HBG588608; -.
DR   HOVERGEN; HBG052818; -.
DR   InParanoid; P70181; -.
DR   OMA; LYVNEHY; -.
DR   OrthoDB; EOG41G33V; -.
DR   PhylomeDB; P70181; -.
DR   BRENDA; 2.7.1.68; 244.
DR   NextBio; 294817; -.
DR   ArrayExpress; P70181; -.
DR   Bgee; P70181; -.
DR   Genevestigator; P70181; -.
DR   GermOnline; ENSMUSG00000024867; Mus musculus.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; IDA:MGI.
DR   InterPro; IPR002498; PInositol-4-P-5-kinase_core.
DR   InterPro; IPR016034; PInositol-4P-5-kinase_core_sub.
DR   PANTHER; PTHR23086; PIP5K; 1.
DR   Pfam; PF01504; PIP5K; 1.
DR   SMART; SM00330; PIPKc; 1.
DR   PROSITE; PS51455; PIPK; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Transferase.
FT   CHAIN         1    539       Phosphatidylinositol-4-phosphate 5-kinase
FT                                type-1 beta.
FT                                /FTId=PRO_0000185459.
FT   DOMAIN       25    395       PIPK.
FT   MOD_RES     405    405       Phosphoserine (By similarity).
FT   MOD_RES     445    445       Phosphoserine (By similarity).
FT   MOD_RES     447    447       Phosphoserine (By similarity).
FT   MOD_RES     448    448       Phosphoserine (By similarity).
FT   VAR_SEQ     401    452       Missing (in isoform 2).
FT                                /FTId=VSP_016012.
FT   MUTAGEN     138    138       K->A: Almost complete loss of kinase
FT                                activity.
FT   MUTAGEN     227    227       D->A: Reduces kinase activity by 98%.
FT                                Loss of actin-remodeling activity.
FT   CONFLICT    291    291       V -> A (in Ref. 2; AAC05374).
FT   CONFLICT    425    425       V -> L (in Ref. 2; AAC05374).
FT   CONFLICT    437    437       R -> Q (in Ref. 2; AAC05374).
FT   CONFLICT    525    528       TLDL -> ALET (in Ref. 2; AAC05374).
SQ   SEQUENCE   539 AA;  60803 MW;  A8478C9E21546AC3 CRC64;
     MSSTAENGDA VPGKQNEEKT YKKTASSAIK GAIQLGIGYT VGNLTSKPER DVLMQDFYVV
     ESVFLPSEGS NLTPAHHYPD FRFKTYAPLA FRYFRELFGI KPDDYLYSIC SEPLIELSNP
     GASGSLFFLT SDDEFIIKTV QHKEAEFLQK LLPGYYMNLN QNPRTLLPKF YGLYCMQSGG
     INIRIVVMNN VLPRAMRMHL TYDLKGSTYK RRASRKEREK PNPTFKDLDF LQDMHEGLYF
     DTETYNALMK TLQRDCRVLE SFKIMDYSLL LGIHILDHSL KDKEEEPLQN VPDAKRPGMQ
     KVLYSTAMES IQGPGKSADG IIAENPDTMG GIPAKSHKGE KLLLFMGIID ILQSYRLMKK
     LEHSWKALVY DGDTVSVHRP SFYADRFLKF MNSRVFKKIQ ALKASPSKKR CNSIAALKAT
     SQEIVSSISQ EWKDEKRDLL TEGQSFSSLD EEALGSRHRP DLVPSTPSLF EAASLATTIS
     SSSLYVGEHY PHDRTTLYSN SKGLPSSSTF TLEEGTIYLT AEPNTLDLQD DASVLDVYL
//
ID   PI51A_MOUSE             Reviewed;         546 AA.
AC   P70182; Q8K0D3; Q99L80;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 2.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Phosphatidylinositol-4-phosphate 5-kinase type-1 alpha;
DE            Short=PIP5K1-alpha;
DE            Short=PtdIns(4)P-5-kinase 1 alpha;
DE            EC=2.7.1.68;
DE   AltName: Full=68 kDa type I phosphatidylinositol-4-phosphate 5-kinase;
DE   AltName: Full=Phosphatidylinositol-4-phosphate 5-kinase type I alpha;
DE            Short=PIP5KIalpha;
DE   AltName: Full=Phosphatidylinositol-4-phosphate 5-kinase type I beta;
DE            Short=PI4P5KIbeta;
GN   Name=Pip5k1a; Synonyms=Pip5k1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION,
RP   AND TISSUE SPECIFICITY.
RC   TISSUE=Insulinoma;
RX   MEDLINE=96394468; PubMed=8798574; DOI=10.1074/jbc.271.39.23611;
RA   Ishihara H., Shibasaki Y., Kizuki N., Katagiri H., Yazaki Y.,
RA   Asano T., Oka Y.;
RT   "Cloning of cDNAs encoding two isoforms of 68-kDa type I
RT   phosphatidylinositol 4-phosphate 5-kinase.";
RL   J. Biol. Chem. 271:23611-23614(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Eye, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   MEDLINE=98204859; PubMed=9535851; DOI=10.1074/jbc.273.15.8741;
RA   Ishihara H., Shibasaki Y., Kizuki N., Wada T., Yazaki Y., Asano T.,
RA   Oka Y.;
RT   "Type I phosphatidylinositol-4-phosphate 5-kinases. Cloning of the
RT   third isoform and deletion/substitution analysis of members of this
RT   novel lipid kinase family.";
RL   J. Biol. Chem. 273:8741-8748(1998).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH RAC1.
RX   MEDLINE=20146116; PubMed=10679324; DOI=10.1016/S0960-9822(00)00315-8;
RA   Tolias K.F., Hartwig J.H., Ishihara H., Shibasaki Y., Cantley L.C.,
RA   Carpenter C.L.;
RT   "Type Ialpha phosphatidylinositol-4-phosphate 5-kinase mediates Rac-
RT   dependent actin assembly.";
RL   Curr. Biol. 10:153-156(2000).
RN   [6]
RP   INTERACTION WITH PLD1 AND PLD2, AND SUBCELLULAR LOCATION.
RX   PubMed=11032811; DOI=10.1093/emboj/19.20.5440;
RA   Divecha N., Roefs M., Halstead J.R., D'Andrea S., Fernandez-Borga M.,
RA   Oomen L., Saqib K.M., Wakelam M.J.O., D'Santos C.;
RT   "Interaction of the type Ialpha PIPkinase with phospholipase D: a role
RT   for the local generation of phosphatidylinositol 4, 5-bisphosphate in
RT   the regulation of PLD2 activity.";
RL   EMBO J. 19:5440-5449(2000).
RN   [7]
RP   INTERACTION WITH ARF1, AND SUBCELLULAR LOCATION.
RX   MEDLINE=20250965; PubMed=10747863; DOI=10.1074/jbc.C901019199;
RA   Jones D.H., Morris J.B., Morgan C.P., Kondo H., Irvine R.F.,
RA   Cockcroft S.;
RT   "Type I phosphatidylinositol 4-phosphate 5-kinase directly interacts
RT   with ADP-ribosylation factor 1 and is responsible for
RT   phosphatidylinositol 4,5-bisphosphate synthesis in the Golgi
RT   compartment.";
RL   J. Biol. Chem. 275:13962-13966(2000).
RN   [8]
RP   INTERACTION WITH JUB.
RX   PubMed=15870270; DOI=10.1128/MCB.25.10.3956-3966.2005;
RA   Kisseleva M., Feng Y., Ward M., Song C., Anderson R.A., Longmore G.D.;
RT   "The LIM protein Ajuba regulates phosphatidylinositol 4,5-bisphosphate
RT   levels in migrating cells through an interaction with and activation
RT   of PIPKI alpha.";
RL   Mol. Cell. Biol. 25:3956-3966(2005).
CC   -!- FUNCTION: Participates in the biosynthesis of
CC       phosphatidylinositol-4,5-bisphosphate. Mediates RAC1-dependent
CC       reorganization of actin filaments. Acts as an activator of TUT1
CC       adenylyltransferase activity in nuclear speckles, thereby
CC       regulating mRNA polyadenylation of a select set of mRNAs.
CC       Contributes to the activation of PLD2.
CC   -!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 4-
CC       phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
CC   -!- ENZYME REGULATION: Activated by phosphatidic acid.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=26 uM for PtdIns(4)P;
CC         KM=33 uM for ATP;
CC   -!- SUBUNIT: Interacts with ARF1, RAC1, PLD1, PLD2 and JUB.
CC   -!- SUBCELLULAR LOCATION: Cell membrane. Golgi apparatus, Golgi stack.
CC       Nucleus speckle (By similarity). Note=Detected on RAC1-induced
CC       plasma membrane ruffles, and on membrane ruffles induced by
CC       platelet-derived growth factor (By similarity). Localizes to
CC       nuclear speckles and associates with TUT1 to regulate
CC       polyadenylation of selected mRNAs (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P70182-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P70182-2; Sequence=VSP_016009;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle, testis,
CC       brain and lung.
CC   -!- SIMILARITY: Contains 1 PIPK domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D86177; BAA13031.1; -; mRNA.
DR   EMBL; AK158062; BAE34344.1; -; mRNA.
DR   EMBL; BC003763; AAH03763.1; -; mRNA.
DR   EMBL; BC031774; AAH31774.1; -; mRNA.
DR   IPI; IPI00331736; -.
DR   IPI; IPI00475262; -.
DR   RefSeq; NP_032873.2; NM_008847.2.
DR   UniGene; Mm.296409; -.
DR   ProteinModelPortal; P70182; -.
DR   SMR; P70182; 65-435.
DR   STRING; P70182; -.
DR   PhosphoSite; P70182; -.
DR   PRIDE; P70182; -.
DR   Ensembl; ENSMUST00000107233; ENSMUSP00000102852; ENSMUSG00000028126.
DR   Ensembl; ENSMUST00000107235; ENSMUSP00000102854; ENSMUSG00000028126.
DR   GeneID; 18720; -.
DR   KEGG; mmu:18720; -.
DR   UCSC; uc008qhx.1; mouse.
DR   CTD; 18720; -.
DR   MGI; MGI:107929; Pip5k1a.
DR   eggNOG; roNOG10604; -.
DR   GeneTree; ENSGT00550000074279; -.
DR   HOVERGEN; HBG052818; -.
DR   OrthoDB; EOG4JQ3Z0; -.
DR   PhylomeDB; P70182; -.
DR   BRENDA; 2.7.1.68; 244.
DR   NextBio; 294821; -.
DR   ArrayExpress; P70182; -.
DR   Bgee; P70182; -.
DR   Genevestigator; P70182; -.
DR   GermOnline; ENSMUSG00000028126; Mus musculus.
DR   GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR   GO; GO:0032587; C:ruffle membrane; IDA:MGI.
DR   GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0010761; P:fibroblast migration; IMP:MGI.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; IDA:MGI.
DR   InterPro; IPR002498; PInositol-4-P-5-kinase_core.
DR   InterPro; IPR016034; PInositol-4P-5-kinase_core_sub.
DR   PANTHER; PTHR23086; PIP5K; 1.
DR   Pfam; PF01504; PIP5K; 1.
DR   SMART; SM00330; PIPKc; 1.
DR   PROSITE; PS51455; PIPK; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell membrane; Golgi apparatus;
KW   Isopeptide bond; Kinase; Membrane; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Transferase; Ubl conjugation.
FT   CHAIN         1    546       Phosphatidylinositol-4-phosphate 5-kinase
FT                                type-1 alpha.
FT                                /FTId=PRO_0000185457.
FT   DOMAIN       66    434       PIPK.
FT   MOD_RES      53     53       Phosphoserine (By similarity).
FT   MOD_RES      56     56       Phosphoserine (By similarity).
FT   MOD_RES      57     57       Phosphoserine (By similarity).
FT   MOD_RES     443    443       Phosphoserine (By similarity).
FT   CROSSLNK     88     88       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   VAR_SEQ     238    431       Missing (in isoform 2).
FT                                /FTId=VSP_016009.
FT   CONFLICT     28     28       S -> AS (in Ref. 3; AAH03763).
FT   CONFLICT    120    120       N -> S (in Ref. 3; AAH03763).
FT   CONFLICT    258    258       E -> D (in Ref. 1; BAA13031).
SQ   SEQUENCE   546 AA;  60485 MW;  6E895F22A75B7140 CRC64;
     MASASSGPAA AGFSSLDAGA PAGTAAASGI KRATVSEGPS ASVMPVKKIG HRSVDSSGET
     TYKKTTSSAL KGAIQLGITH TVGSLSTKPE RDVLMQDFYV VESIFFPSEG SNLTPAHHYN
     DFRFKTYAPV AFRYFRELFG IRPDDYLYSL CSEPLIELSN SGASGSLFYV SSDDEFIIKT
     VQHKEAEFLQ KLLPGYYMNL NQNPRTLLPK FYGLYCVQAG GKNIRIVVMN NLLPRSVKMH
     MKYDLKGSTY KRRASQKERE KTLPTFKDLD FLQDIPDGLF LDADMYSALC KTLQRDCLVL
     QSFKIMDYSL LMSIHNMDHA QREPTSNDTQ YSADTRRPAP QKALYSTAME SIQGEARRGG
     TVETEDHMGG IPARNNKGER LLLYIGIIDI LQSYRFVKKL EHSWKALVHD GDTVSVHRPG
     FYAERFQRFM CNTVFKKIPL KPSPTKKFRS GPSFSRRSGP SGNSCTSQLM ASGEHRAQVT
     TKAEVEPDVH LGRPDVLPQT PPLEEISEGS PVPGPSFSPV VGQPLQILNL SSTLEKLDVA
     ESEFTH
//
ID   KIFA3_MOUSE             Reviewed;         793 AA.
AC   P70188; P70189; Q6GTS3;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Kinesin-associated protein 3;
DE            Short=KAP-3;
DE            Short=KAP3;
GN   Name=Kifap3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 86-106; 150-185 AND
RP   486-498, AND ALTERNATIVE SPLICING.
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=96323241; PubMed=8710890; DOI=10.1073/pnas.93.16.8443;
RA   Yamazaki H., Nakata T., Okada Y., Hirokawa N.;
RT   "Cloning and characterization of KAP3: a novel kinesin superfamily-
RT   associated protein of KIF3A/3B.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:8443-8448(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS KAP3A AND KAP3B).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Involved in tethering the chromosomes to the spindle
CC       pole and in chromosome movement. Binds to the tail domain of the
CC       KIF3A/KIF3B heterodimer to form a heterotrimeric KIF3 complex and
CC       may regulate the membrane binding of this complex.
CC   -!- SUBUNIT: Interacts with SMC3 subunit of the cohesin complex (By
CC       similarity). Heterotrimer of KIFAP3, KIF3A and KIF3B. Interacts
CC       with RAP1GDS1/SMG GDS.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=KAP3A;
CC         IsoId=P70188-1; Sequence=Displayed;
CC       Name=KAP3B;
CC         IsoId=P70188-2; Sequence=VSP_003899;
CC   -!- PTM: Phosphorylated on tyrosine residues by SRC in vitro; this
CC       reduces the binding affinity of the protein for RAP1GDS1 (By
CC       similarity).
CC   -!- SIMILARITY: Contains 5 ARM repeats.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D50366; BAA08901.1; -; mRNA.
DR   EMBL; D50367; BAA08902.1; -; mRNA.
DR   EMBL; BC040362; AAH40362.1; -; mRNA.
DR   EMBL; BC049100; AAH49100.1; -; mRNA.
DR   IPI; IPI00230068; -.
DR   IPI; IPI00320484; -.
DR   PIR; JC6161; JC6161.
DR   RefSeq; NP_034759.1; NM_010629.2.
DR   UniGene; Mm.4651; -.
DR   ProteinModelPortal; P70188; -.
DR   STRING; P70188; -.
DR   PhosphoSite; P70188; -.
DR   PRIDE; P70188; -.
DR   Ensembl; ENSMUST00000027877; ENSMUSP00000027877; ENSMUSG00000026585.
DR   Ensembl; ENSMUST00000077642; ENSMUSP00000076830; ENSMUSG00000026585.
DR   GeneID; 16579; -.
DR   KEGG; mmu:16579; -.
DR   CTD; 16579; -.
DR   MGI; MGI:107566; Kifap3.
DR   eggNOG; roNOG04542; -.
DR   HOGENOM; HBG381067; -.
DR   HOVERGEN; HBG052257; -.
DR   InParanoid; P70188; -.
DR   OMA; GDLVGQH; -.
DR   OrthoDB; EOG41JZBX; -.
DR   ArrayExpress; P70188; -.
DR   Bgee; P70188; -.
DR   CleanEx; MM_KIFAP3; -.
DR   Genevestigator; P70188; -.
DR   GermOnline; ENSMUSG00000026585; Mus musculus.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0016939; C:kinesin II complex; IPI:UniProtKB.
DR   GO; GO:0019894; F:kinesin binding; IEA:InterPro.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; TAS:MGI.
DR   GO; GO:0007017; P:microtubule-based process; IPI:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0046587; P:positive regulation of calcium-dependent cell-cell adhesion; IMP:MGI.
DR   GO; GO:0008104; P:protein localization; IMP:MGI.
DR   GO; GO:0007266; P:Rho protein signal transduction; TAS:MGI.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR008658; KAP.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 2.
DR   PANTHER; PTHR15605; KAP; 1.
DR   SMART; SM00185; ARM; 3.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing; Phosphoprotein;
KW   Repeat.
FT   CHAIN         1    793       Kinesin-associated protein 3.
FT                                /FTId=PRO_0000084303.
FT   REPEAT      333    373       ARM 1.
FT   REPEAT      374    412       ARM 2.
FT   REPEAT      494    533       ARM 3.
FT   REPEAT      578    620       ARM 4.
FT   REPEAT      621    662       ARM 5.
FT   VAR_SEQ     759    793       LGMDGFGQPLGILGRPATAYGFRPDEPYYYSFGSR -> TV
FT                                HPRISKCFASVH (in isoform KAP3B).
FT                                /FTId=VSP_003899.
SQ   SEQUENCE   793 AA;  91291 MW;  38EBC7FD5312DAAB CRC64;
     MQGEDARYLK RKVKGGNIDV HPSEKALIVQ YEVEATILGE MGDPMLGERK ECQKIIRLKS
     LNANTDITSL ARKVVEECKL IHPSKLSEVE QLLYYLQNRR DSLPGKEKKE KSSKPKDPPP
     FEGMEIDEVA NINDMDEYIE LLYEDIPDKV RGSALILQLA RNPDNLEELL LNETALGALA
     RVLREDWKQS VELATNIIYI FFCFSSFSHF HGLITHYKIG ALCMNIIDHE LKRHELWQEE
     LSKKKKAVDE DLENQTLRKD YDKTFKKYQG LVVKQEQLLR VALYLLLNLA EDTRTELKMR
     NKNIVHMLVK ALDRDNFELL ILVVSFLKKL SIFMENKNDM VEMDIVEKLV KMIPCEHEDL
     LNITLRLLLN LSFDTGLRNK MVQVGLLPKL TALLGNENYK QIAMCVLYHI SMDDRFKSMF
     AYTDCIPQLM KMLFECSDER IDLELISFCI NLAANKRNVQ LICEGNGLKM LMKRALKLKD
     PLLMKMIRNI SQHDGPTKNL FIDYVGDLAA QISSDEEEEF VIECLGTLAN LTIPDLDWEL
     VLKEYKLVPF LKDKLKPGAA EDDLVLEVVI MIGTVSMDDS CAALLAKSGI IPALIELLNA
     QQEDDEFVCQ IIYVFYQMVF HQATRDVIIK ETQAPAYLID LMHDKNNEIR KVCDNTLDII
     AEYDEEWAKK IQSEKFRWHN SQWLEMVESR QLDESEQYLY GDDRIEPYIH EGDILERPDL
     FYNSDGLITS EGAISPDFFN DFHLQNGDVV GQHAFPGSLG MDGFGQPLGI LGRPATAYGF
     RPDEPYYYSF GSR
//
ID   LRIG1_MOUSE             Reviewed;        1091 AA.
AC   P70193;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Leucine-rich repeats and immunoglobulin-like domains protein 1;
DE            Short=LIG-1;
DE   Flags: Precursor;
GN   Name=Lrig1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=96394313; PubMed=8798419; DOI=10.1074/jbc.271.37.22522;
RA   Suzuki Y., Sato N., Tohyama M., Wanaka A., Takagi T.;
RT   "cDNA cloning of a novel membrane glycoprotein that is expressed
RT   specifically in glial cells in the mouse brain. LIG-1, a protein with
RT   leucine-rich repeats and immunoglobulin-like domains.";
RL   J. Biol. Chem. 271:22522-22527(1996).
RN   [2]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=12067728; DOI=10.1016/S0014-5793(02)02824-7;
RA   Suzuki Y., Miura H., Tanemura A., Kobayashi K., Kondoh G., Sano S.,
RA   Ozawa K., Inui S., Nakata A., Takagi T., Tohyama M., Yoshikawa K.,
RA   Itami S.;
RT   "Targeted disruption of LIG-1 gene results in psoriasiform epidermal
RT   hyperplasia.";
RL   FEBS Lett. 521:67-71(2002).
CC   -!- FUNCTION: Act as a feedback negative regulator of signaling by
CC       receptor tyrosine kinases, through a mechanism that involves
CC       enhancement of receptor ubiquitination and accelerated
CC       intracellular degradation (By similarity).
CC   -!- SUBUNIT: Interacts with EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in the brain,
CC       restricted to a small subset of glial cells, such as Bergmann
CC       glial cells of the cerebellum and glial cells in the nerve fiber
CC       layer of the olfactory bulb. Expressed also in the skin. Low
CC       expression is detected in the thymus and heart. No expression in
CC       the kidney, liver, lung or small intestine.
CC   -!- INDUCTION: Down-regulated in the psoriasis epidermis.
CC   -!- DOMAIN: The LRRs and the Ig-domains are each sufficient for EGFR
CC       binding. This interaction is abolished only when these two domains
CC       are deleted (By similarity).
CC   -!- MISCELLANEOUS: Knockout of the gene results in psiorasiform
CC       epidermal hyperplasia.
CC   -!- SIMILARITY: Contains 3 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SIMILARITY: Contains 14 LRR (leucine-rich) repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D78572; BAA11416.1; -; mRNA.
DR   IPI; IPI00136475; -.
DR   PIR; A58532; A58532.
DR   RefSeq; NP_032403.2; NM_008377.2.
DR   UniGene; Mm.245210; -.
DR   ProteinModelPortal; P70193; -.
DR   SMR; P70193; 41-784.
DR   STRING; P70193; -.
DR   PhosphoSite; P70193; -.
DR   PRIDE; P70193; -.
DR   Ensembl; ENSMUST00000032105; ENSMUSP00000032105; ENSMUSG00000030029.
DR   Ensembl; ENSMUST00000101126; ENSMUSP00000098686; ENSMUSG00000030029.
DR   GeneID; 16206; -.
DR   KEGG; mmu:16206; -.
DR   UCSC; uc009czu.1; mouse.
DR   CTD; 16206; -.
DR   MGI; MGI:107935; Lrig1.
DR   eggNOG; maNOG10582; -.
DR   GeneTree; ENSGT00600000084148; -.
DR   HOGENOM; HBG315254; -.
DR   HOVERGEN; HBG052353; -.
DR   InParanoid; P70193; -.
DR   OrthoDB; EOG48PMJN; -.
DR   PhylomeDB; P70193; -.
DR   NextBio; 289161; -.
DR   ArrayExpress; P70193; -.
DR   Bgee; P70193; -.
DR   Genevestigator; P70193; -.
DR   GermOnline; ENSMUSG00000030029; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR000372; LRR-contain_N.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3.
DR   Pfam; PF07679; I-set; 3.
DR   Pfam; PF00560; LRR_1; 3.
DR   Pfam; PF01463; LRRCT; 1.
DR   Pfam; PF01462; LRRNT; 1.
DR   SMART; SM00408; IGc2; 3.
DR   SMART; SM00369; LRR_TYP; 3.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00013; LRRNT; 1.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS51450; LRR; 14.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Leucine-rich repeat; Membrane; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     34       Potential.
FT   CHAIN        35   1091       Leucine-rich repeats and immunoglobulin-
FT                                like domains protein 1.
FT                                /FTId=PRO_0000014828.
FT   TOPO_DOM     35    796       Extracellular (Potential).
FT   TRANSMEM    797    817       Helical; (Potential).
FT   TOPO_DOM    818   1091       Cytoplasmic (Potential).
FT   REPEAT       68     92       LRR 1.
FT   REPEAT       93    116       LRR 2.
FT   REPEAT      140    163       LRR 3.
FT   REPEAT      164    187       LRR 4.
FT   REPEAT      189    212       LRR 5.
FT   REPEAT      214    235       LRR 6.
FT   REPEAT      236    259       LRR 7.
FT   REPEAT      261    283       LRR 8.
FT   REPEAT      284    307       LRR 9.
FT   REPEAT      309    331       LRR 10.
FT   REPEAT      332    355       LRR 11.
FT   REPEAT      357    382       LRR 12.
FT   REPEAT      383    406       LRR 13.
FT   REPEAT      408    430       LRR 14.
FT   DOMAIN      497    596       Ig-like C2-type 1.
FT   DOMAIN      601    690       Ig-like C2-type 2.
FT   DOMAIN      695    781       Ig-like C2-type 3.
FT   COMPBIAS    522    526       Poly-Ser.
FT   CARBOHYD     76     76       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    152    152       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    248    248       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    294    294       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    320    320       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    385    385       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    686    686       N-linked (GlcNAc...) (Potential).
FT   DISULFID    518    579       By similarity.
FT   DISULFID    622    674       By similarity.
FT   DISULFID    716    765       By similarity.
SQ   SEQUENCE   1091 AA;  119284 MW;  A13D0866CE4C203D CRC64;
     MARPGPGVLG APRLAPRLLL WLLLLLLQWP ESAGAQARPR APCAAACTCA GNSLDCSGRG
     LATLPRDLPS WTRSLNLSYN RLSEIDSAAF EDLTNLQEVY LNSNELTAIP SLGTASIGVV
     SLFLQHNKIL SVDGSQLKSY LSLEVLDLSS NNITEIRSSC FPNGLRIREL NLASNRISIL
     ESGAFDGLSR SLLTLRLSKN RITQLPVKAF KLPRLTQLDL NRNRIRLIEG LTFQGLDSLE
     VLRLQRNNIS RLTDGAFWGL SKMHVLHLEY NSLVEVNSGS LYGLTALHQL HLSNNSISRI
     QRDGWSFCQK LHELILSFNN LTRLDEESLA ELSSLSILRL SHNAISHIAE GAFKGLKSLR
     VLDLDHNEIS GTIEDTSGAF TGLDNLSKLT LFGNKIKSVA KRAFSGLESL EHLNLGENAI
     RSVQFDAFAK MKNLKELYIS SESFLCDCQL KWLPPWLMGR MLQAFVTATC AHPESLKGQS
     IFSVLPDSFV CDDFPKPQII TQPETTMAVV GKDIRFTCSA ASSSSSPMTF AWKKDNEVLA
     NADMENFAHV RAQDGEVMEY TTILHLRHVT FGHEGRYQCI ITNHFGSTYS HKARLTVNVL
     PSFTKIPHDI AIRTGTTARL ECAATGHPNP QIAWQKDGGT DFPAARERRM HVMPDDDVFF
     ITDVKIDDMG VYSCTAQNSA GSVSANATLT VLETPSLAVP LEDRVVTVGE TVAFQCKATG
     SPTPRITWLK GGRPLSLTER HHFTPGNQLL VVQNVMIDDA GRYTCEMSNP LGTERAHSQL
     SILPTPGCRK DGTTVGIFTI AVVCSIVLTS LVWVCIIYQT RKKSEEYSVT NTDETIVPPD
     VPSYLSSQGT LSDRQETVVR TEGGHQANGH IESNGVCLRD PSLFPEVDIH STTCRQPKLC
     VGYTREPWKV TEKADRTAAP HTTAHSGSAV CSDCSTDTAY HPQPVPRDSG QPGTASSQEL
     RQHDREYSPH HPYSGTADGS HTLSGGSLYP SNHDRILPSL KNKAASADGN GDSSWTLAKL
     HEADCIDLKP SPTLASGSPE LMEDAISTEA QHLLVSNGHL PKACDSSPES VPLKGQITGK
     RRGPLLLAPR S
//
ID   PACR_MOUSE              Reviewed;         496 AA.
AC   P70205;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   11-JAN-2011, entry version 78.
DE   RecName: Full=Pituitary adenylate cyclase-activating polypeptide type I receptor;
DE            Short=PACAP type I receptor;
DE            Short=PACAP-R-1;
DE            Short=PACAP-R1;
DE   Flags: Precursor;
GN   Name=Adcyap1r1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96256640; PubMed=8664310; DOI=10.1016/0005-2736(96)00056-9;
RA   Hashimoto H., Yamamoto K., Hagigara N., Ogawa N., Nishino A., Aino H.,
RA   Nogi H., Imanishi K., Matsuda T., Baba A.;
RT   "cDNA cloning of a mouse pituitary adenylate cyclase-activating
RT   polypeptide receptor.";
RL   Biochim. Biophys. Acta 1281:129-133(1996).
CC   -!- FUNCTION: This is a receptor for PACAP-27 and PACAP-38. The
CC       activity of this receptor is mediated by G proteins which activate
CC       adenylyl cyclase. May regulate the release of adrenocorticotropin,
CC       luteinizing hormone, growth hormone, prolactin, epinephrine, and
CC       catecholamine. May play a role in spermatogenesis and sperm
CC       motility. Causes smooth muscle relaxation and secretion in the
CC       gastrointestinal tract.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; D82935; BAA11639.1; -; mRNA.
DR   IPI; IPI00137309; -.
DR   RefSeq; NP_031433.3; NM_007407.3.
DR   UniGene; Mm.44245; -.
DR   ProteinModelPortal; P70205; -.
DR   SMR; P70205; 17-143.
DR   MINT; MINT-4544489; -.
DR   STRING; P70205; -.
DR   PRIDE; P70205; -.
DR   Ensembl; ENSMUST00000070736; ENSMUSP00000063784; ENSMUSG00000029778.
DR   GeneID; 11517; -.
DR   KEGG; mmu:11517; -.
DR   UCSC; uc009cat.1; mouse.
DR   CTD; 11517; -.
DR   MGI; MGI:108449; Adcyap1r1.
DR   eggNOG; roNOG07771; -.
DR   HOGENOM; HBG447108; -.
DR   HOVERGEN; HBG008318; -.
DR   InParanoid; P70205; -.
DR   OMA; ACGFDEY; -.
DR   PhylomeDB; P70205; -.
DR   NextBio; 278938; -.
DR   ArrayExpress; P70205; -.
DR   Bgee; P70205; -.
DR   Genevestigator; P70205; -.
DR   GermOnline; ENSMUSG00000029778; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004999; F:vasoactive intestinal polypeptide receptor activity; TAS:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR001879; GPCR_2_extracellular_dom.
DR   InterPro; IPR002285; GPCR_2_PACAP_1_rcpt.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR   PANTHER; PTHR12011:SF30; PAC_1_rcpt; 1.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF02793; HRM; 1.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   PRINTS; PR01156; PACAPRECEPTR.
DR   SMART; SM00008; HormR; 1.
DR   PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1.
DR   PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR   PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Developmental protein; Differentiation;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Receptor; Signal;
KW   Spermatogenesis; Transducer; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21    496       Pituitary adenylate cyclase-activating
FT                                polypeptide type I receptor.
FT                                /FTId=PRO_0000012842.
FT   TOPO_DOM     21    155       Extracellular (Potential).
FT   TRANSMEM    156    178       Helical; Name=1; (Potential).
FT   TOPO_DOM    179    186       Cytoplasmic (Potential).
FT   TRANSMEM    187    205       Helical; Name=2; (Potential).
FT   TOPO_DOM    206    227       Extracellular (Potential).
FT   TRANSMEM    228    253       Helical; Name=3; (Potential).
FT   TOPO_DOM    254    268       Cytoplasmic (Potential).
FT   TRANSMEM    269    291       Helical; Name=4; (Potential).
FT   TOPO_DOM    292    309       Extracellular (Potential).
FT   TRANSMEM    310    332       Helical; Name=5; (Potential).
FT   TOPO_DOM    333    378       Cytoplasmic (Potential).
FT   TRANSMEM    379    399       Helical; Name=6; (Potential).
FT   TOPO_DOM    400    413       Extracellular (Potential).
FT   TRANSMEM    414    433       Helical; Name=7; (Potential).
FT   TOPO_DOM    434    496       Cytoplasmic (Potential).
FT   CARBOHYD     48     48       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     60     60       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    117    117       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   496 AA;  56640 MW;  47B5D51D4209060A CRC64;
     MARTLQLSLT ALLLLPMAIA MHSDCIFKKE QAMCLERIQR ANDLMGLNES SPGCPGMWDN
     ITCWKPAQIG EMVLVSCPEV FRIFNPDQVW MTETIGDSGF ADSNSLEITD MGVVGRNCTE
     DGWSEPFPHY FDACGFDDYE PESGDQDYYY LSVKALYTVG YSTSLVTLTT AMVILCRFRK
     LHCTRNFIHM NLFVSFMLRA ISVFIKDWIL YAEQDSSHCF VSTVECKAVM VFFHYCVVSN
     YFWLFIEGLY LFTLLVETFF PERRYFYWYT IIGWGTPTVC VTVWAVLRLY FDDAGCWDMN
     DSTALWWVIK GPVVGSIMVN FVLFIGIIII LVQKLQSPDM GGNESSIYFS CVQKCYCKPQ
     RAQQHSCKMS ELSTITLRLA RSTLLLIPLF GIHYTVFAFS PENVSKRERL VFELGLGSFQ
     GFVVAVLYCF LNGEVQAEIK RKWRSWKVNR YFTMDFKHRH PSLASSGVNG GTQLSILSKS
     SSQLRMSSLP ADNLAT
//
ID   PLXA1_MOUSE             Reviewed;        1894 AA.
AC   P70206; B2RQP7; Q5DTR0;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Plexin-A1;
DE            Short=Plex 1;
DE            Short=Plexin-1;
DE   Flags: Precursor;
GN   Name=Plxna1; Synonyms=Kiaa4053;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c, and ICR; TISSUE=Brain;
RX   MEDLINE=96400291; PubMed=8806667; DOI=10.1006/bbrc.1996.1388;
RA   Kameyama T., Murakami Y., Suto F., Kawakami A., Takagi S., Hirata T.,
RA   Fujisawa H.;
RT   "Identification of a neuronal cell surface molecule, plexin, in
RT   mice.";
RL   Biochem. Biophys. Res. Commun. 226:524-529(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 495-1894.
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, AND INTERACTION WITH NRP1; NRP2; SEMA3A AND SEMA3F.
RX   PubMed=10520994; DOI=10.1016/S0092-8674(00)80062-8;
RA   Takahashi T., Fournier A., Nakamura F., Wang L.-H., Murakami Y.,
RA   Kalb R.G., Fujisawa H., Strittmatter S.M.;
RT   "Plexin-neuropilin-1 complexes form functional semaphorin-3A
RT   receptors.";
RL   Cell 99:59-69(1999).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH NRP1; NRP2; SEMA3A AND SEMA3C.
RX   PubMed=10781943; DOI=10.1016/S0925-4773(00)00269-0;
RA   Rohm B., Ottemeyer A., Lohrum M., Pueschel A.W.;
RT   "Plexin/neuropilin complexes mediate repulsion by the axonal guidance
RT   signal semaphorin 3A.";
RL   Mech. Dev. 93:95-104(2000).
RN   [6]
RP   INTERACTION WITH PLXNB1, AND TISSUE SPECIFICITY.
RX   PubMed=12559962; DOI=10.1016/S0006-291X(02)02966-2;
RA   Usui H., Taniguchi M., Yokomizo T., Shimizu T.;
RT   "Plexin-A1 and plexin-B1 specifically interact at their cytoplasmic
RT   domains.";
RL   Biochem. Biophys. Res. Commun. 300:927-931(2003).
RN   [7]
RP   INTERACTION WITH CRMP1; DPYSL2/CRMP2; DPYSL3/CRMP3 AND DPYSL4/CRMP4.
RX   PubMed=14685275; DOI=10.1038/sj.emboj.7600021;
RA   Deo R.C., Schmidt E.F., Elhabazi A., Togashi H., Burley S.K.,
RA   Strittmatter S.M.;
RT   "Structural bases for CRMP function in plexin-dependent semaphorin3A
RT   signaling.";
RL   EMBO J. 23:9-22(2004).
RN   [8]
RP   INTERACTION WITH SEMA6D AND KDR.
RX   PubMed=14977921; DOI=10.1101/gad.1167304;
RA   Toyofuku T., Zhang H., Kumanogoh A., Takegahara N., Suto F., Kamei J.,
RA   Aoki K., Yabuki M., Hori M., Fujisawa H., Kikutani H.;
RT   "Dual roles of Sema6D in cardiac morphogenesis through region-specific
RT   association of its receptor, Plexin-A1, with off-track and vascular
RT   endothelial growth factor receptor type 2.";
RL   Genes Dev. 18:435-447(2004).
RN   [9]
RP   INTERACTION WITH FARP2 AND RND1, AND MUTAGENESIS OF
RP   1266-LYS--LYS-1268.
RX   PubMed=16286926; DOI=10.1038/nn1596;
RA   Toyofuku T., Yoshida J., Sugimoto T., Zhang H., Kumanogoh A., Hori M.,
RA   Kikutani H.;
RT   "FARP2 triggers signals for Sema3A-mediated axonal repulsion.";
RL   Nat. Neurosci. 8:1712-1719(2005).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-120, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [11]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1041, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Coreceptor for SEMA3A, SEMA3C, SEMA3F and SEMA6D.
CC       Necessary for signaling by class 3 semaphorins and subsequent
CC       remodeling of the cytoskeleton. Plays a role in axon guidance,
CC       invasive growth and cell migration. Class 3 semaphorins bind to a
CC       complex composed of a neuropilin and a plexin. The plexin
CC       modulates the affinity of the complex for specific semaphorins,
CC       and its cytoplasmic domain is required for the activation of down-
CC       stream signaling events in the cytoplasm.
CC   -!- SUBUNIT: Interacts directly with NRP1 and NRP2. Interacts with
CC       FARP2, RND1 and KDR/VEGFR2. Binding of SEMA3A leads to
CC       dissociation of FARP2. Interacts with WITH CRMP1, DPYSL2/CRMP2,
CC       DPYSL3/CRMP3 and DPYSL4/CRMP4.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the plexin family.
CC   -!- SIMILARITY: Contains 4 IPT/TIG domains.
CC   -!- SIMILARITY: Contains 1 Sema domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D86948; BAA13188.1; -; mRNA.
DR   EMBL; BC138023; AAI38024.1; -; mRNA.
DR   EMBL; AK220460; BAD90489.1; -; mRNA.
DR   IPI; IPI00137311; -.
DR   PIR; JC4980; JC4980.
DR   RefSeq; NP_032907.1; NM_008881.2.
DR   UniGene; Mm.3789; -.
DR   ProteinModelPortal; P70206; -.
DR   SMR; P70206; 39-563, 654-706, 799-1147, 1269-1893.
DR   DIP; DIP-29745N; -.
DR   STRING; P70206; -.
DR   PhosphoSite; P70206; -.
DR   PRIDE; P70206; -.
DR   Ensembl; ENSMUST00000049845; ENSMUSP00000063066; ENSMUSG00000030084.
DR   GeneID; 18844; -.
DR   KEGG; mmu:18844; -.
DR   UCSC; uc009cwg.1; mouse.
DR   CTD; 18844; -.
DR   MGI; MGI:107685; Plxna1.
DR   eggNOG; roNOG10635; -.
DR   HOGENOM; HBG716170; -.
DR   HOVERGEN; HBG105711; -.
DR   InParanoid; P70206; -.
DR   OMA; EDGRIHC; -.
DR   OrthoDB; EOG49W2DH; -.
DR   PhylomeDB; P70206; -.
DR   NextBio; 295216; -.
DR   ArrayExpress; P70206; -.
DR   Bgee; P70206; -.
DR   CleanEx; MM_PLXNA1; -.
DR   Genevestigator; P70206; -.
DR   GermOnline; ENSMUSG00000030084; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; EXP:Reactome.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0017154; F:semaphorin receptor activity; IPI:MGI.
DR   GO; GO:0060666; P:dichotomous subdivision of terminal units involved in salivary gland branching; IDA:MGI.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002909; IPT_TIG_rcpt.
DR   InterPro; IPR003659; Plexin-like.
DR   InterPro; IPR016201; Plexin-like_fold.
DR   InterPro; IPR013548; Plexin_cytoplasmic_RasGAP_dom.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR001627; Semaphorin/CD100_Ag.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 4.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF08337; Plexin_cytopl; 1.
DR   Pfam; PF01437; PSI; 3.
DR   Pfam; PF01403; Sema; 1.
DR   Pfam; PF01833; TIG; 4.
DR   SMART; SM00429; IPT; 4.
DR   SMART; SM00423; PSI; 3.
DR   SMART; SM00630; Sema; 1.
DR   SUPFAM; SSF81296; Ig_E-set; 4.
DR   SUPFAM; SSF103575; Plexin-like_fold; 2.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   SUPFAM; SSF101912; Sema; 1.
DR   PROSITE; PS51004; SEMA; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Glycoprotein; Membrane; Phosphoprotein; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     27       Potential.
FT   CHAIN        28   1894       Plexin-A1.
FT                                /FTId=PRO_0000232746.
FT   TOPO_DOM     28   1242       Extracellular (Potential).
FT   TRANSMEM   1243   1263       Helical; (Potential).
FT   TOPO_DOM   1264   1894       Cytoplasmic (Potential).
FT   DOMAIN       28    510       Sema.
FT   DOMAIN      862    957       IPT/TIG 1.
FT   DOMAIN      959   1043       IPT/TIG 2.
FT   DOMAIN     1046   1145       IPT/TIG 3.
FT   DOMAIN     1148   1234       IPT/TIG 4.
FT   COILED     1262   1315       Potential.
FT   MOD_RES     120    120       Phosphotyrosine.
FT   CARBOHYD     75     75       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    658    658       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    670    670       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    699    699       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1041   1041       N-linked (GlcNAc...).
FT   CARBOHYD   1185   1185       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1210   1210       N-linked (GlcNAc...) (Potential).
FT   MUTAGEN    1266   1268       KRK->AAA: Loss of interaction with FARP2.
SQ   SEQUENCE   1894 AA;  211099 MW;  A8E6BB29C6824C94 CRC64;
     MPLPPLSSRT LLLLLLLLLR GVWIAISSPP AGLGPQPAFR TFVASDWGLT HLVVHEQTGE
     VYVGAVNRIY KLSGNLTLLR AHVTGPVEDN EKCYPPPSVQ SCPHGLGSTD NVNKLLLLDY
     AANRLLACGS ASQGICQFLR LDDLFKLGEP HHRKEHYLSS VREAGSMAGV LIAGPPGQGQ
     AKLFVGTPID GKSEYFPTLS SRRLMANEED ADMFGFVYQD EFVSSQLKIP SDTLSKFPAF
     DIYYVYSFRS EQFVYYLTLQ LDTQLTSPDA AGEHFFTSKI VRLCVNDPKF YSYVEFPIGC
     EQAGVEYRLV QDAYLSRPGQ ALAKQLGLAE DEEVLFTVFA QGQKNRVKPP KESALCLFTL
     RAIKEKIKER IQSCYRGEGK LSLPWLLNKE LGCINSPLQI DDDFCGQDFN QPLGGTVTIE
     GTPLFVDKED GLTAVAAYDY QGRTVVFAGT RSGRIRKILV DLANPSGRPA LAYESVVAQE
     GNPILRDLVL SPNRQYLYAM TEKQVTQVPV ESCVQYTSCE LCLGSRDPHC GWCVLHSICS
     RQDACERAEE PQRFASDLLQ CVQLTVQPRN VSVTMSQVPL VLQAWNVPDL SAGVNCSFED
     FTETESILED GRIHCHSPSA REVAPITQGQ GDQRVVKLYL KSKETGKKFA SVDFVFYNCS
     VHQSCLACVN GSFPCHWCKY RHVCTNNAAD CAFLEGRVNM SEDCPQILPS THIYVPVGVV
     KPITLAARNL PQPQSGQRGY ECLFHIPGSP ARVTALRFNS SSLQCQNSSY SYEGNDVSDL
     PVNLSVVWNG NFVIDNPQNI QAHLYKCPAL RQSCGLCLKA DPRFECGWCV AERRCSLRHH
     CPADSPASWM HAHHGSSRCT DPKILKLSPE TGPRQGGTRL TITGENLGLR FEDVRLGVHV
     GKVLCSPVES EYISAEQIVC EIGDASTLRA HDALVEVCVR DCSLHYRALS PKRFTFVTPT
     FYRVSPSRGP LSGGTWIGIE GSHLNAGSDV AVSIGGRPCS FSWRNSREIR CLTPPGHTPG
     SAPIVININR AQLSNPEVKY NYTEDPTILR IDPEWSINSG GTLLTVTGTN LATVREPRIR
     AKYGGIEREN SCMVYNDTTM VCRAPSIDNP KRSPPELGER PDEIGFIMDN VRTLLVLNSS
     SFLYYPDPVL EPLSPTGLLE LKPSSPLILK GRNLLPPAPG NSRLNYTVLI GSTPCILTVS
     ETQLLCEAPN LTGQHKVTVR AGGFEFSPGM LQVYSDSLLT LPAIVGIGGG GGLLLLVIVA
     VLIAYKRKSR DADRTLKRLQ LQMDNLESRV ALECKEAFAE LQTDIHELTS DLDGAGIPFL
     DYRTYAMRVL FPGIEDHPVL KEMEVQANVE KSLTLFGQLL TKKHFLLTFI RTLEAQRSFS
     MRDRGNVASL IMTALQGEME YATGVLKQLL SDLIEKNLES KNHPKLLLRR TESVAEKMLT
     NWFTFLLYKF LKECAGEPLF MLYCAIKQQM EKGPIDAITG EARYSLSEDK LIRQQIDYKT
     LTLNCVNPEH ENAPEVPVKG LNCDTVTQVK EKLLDAVYKG VPYSQRPKAG DMDLEWRQGR
     MARIILQDED VTTKIDNDWK RLNTLAHYQV TDGSSVALVP KQTSAYNISN SSTFTKSLSR
     YESMLRTASS PDSLRSRTPM ITPDLESGTK LWHLVKNHDH LDQREGDRGS KMVSEIYLTR
     LLATKGTLQK FVDDLFETIF STAHRGSALP LAIKYMFDFL DEQADKHQIH DSDVRHTWKS
     NCLPLRFWVN VIKNPQFVFD IHKNSITDAC LSVVAQTFMD SCSTSEHKLG KDSPSNKLLY
     AKDIPNYKSW VERYYADIAK MPAISDQDMS AYLAEQSRLH LSQFNSMSAL HEIYSYIAKY
     KDEILVALEK DEQARRQRLR SKLEQVVDTM ALSS
//
ID   PLXA2_MOUSE             Reviewed;        1894 AA.
AC   P70207; Q6NVE6; Q6PHN4; Q80TZ7; Q8R1I4;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Plexin-A2;
DE            Short=Plex 2;
DE            Short=Plexin-2;
DE   Flags: Precursor;
GN   Name=Plxna2; Synonyms=Kiaa0463;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=96400270; PubMed=8806646; DOI=10.1006/bbrc.1996.1367;
RA   Kameyama T., Murakami Y., Suto F., Kawakami A., Takagi S., Hirata T.,
RA   Fujisawa H.;
RT   "Identification of plexin family molecules in mice.";
RL   Biochem. Biophys. Res. Commun. 226:396-402(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 366-1894.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH NRP1 AND SEMA3A.
RX   PubMed=10520994; DOI=10.1016/S0092-8674(00)80062-8;
RA   Takahashi T., Fournier A., Nakamura F., Wang L.-H., Murakami Y.,
RA   Kalb R.G., Fujisawa H., Strittmatter S.M.;
RT   "Plexin-neuropilin-1 complexes form functional semaphorin-3A
RT   receptors.";
RL   Cell 99:59-69(1999).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH NRP1; NRP2 AND SEMA3A.
RX   PubMed=10781943; DOI=10.1016/S0925-4773(00)00269-0;
RA   Rohm B., Ottemeyer A., Lohrum M., Pueschel A.W.;
RT   "Plexin/neuropilin complexes mediate repulsion by the axonal guidance
RT   signal semaphorin 3A.";
RL   Mech. Dev. 93:95-104(2000).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1630 AND SER-1633, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1432, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Coreceptor for SEMA3A. Necessary for signaling by class
CC       3 semaphorins and subsequent remodeling of the cytoskeleton. Plays
CC       a role in axon guidance, invasive growth and cell migration. Class
CC       3 semaphorins bind to a complex composed of a neuropilin and a
CC       plexin. The plexin modulates the affinity of the complex for
CC       specific semaphorins, and its cytoplasmic domain is required for
CC       the activation of down-stream signaling events in the cytoplasm.
CC   -!- SUBUNIT: Interacts directly with NRP1 and NRP2.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- SIMILARITY: Belongs to the plexin family.
CC   -!- SIMILARITY: Contains 4 IPT/TIG domains.
CC   -!- SIMILARITY: Contains 1 Sema domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH68155.1; Type=Erroneous initiation;
CC       Sequence=BAA13189.1; Type=Erroneous initiation;
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DR   EMBL; D86949; BAA13189.1; ALT_INIT; mRNA.
DR   EMBL; BC024509; AAH24509.1; -; mRNA.
DR   EMBL; BC056475; AAH56475.1; -; mRNA.
DR   EMBL; BC068155; AAH68155.1; ALT_INIT; mRNA.
DR   EMBL; AK122289; BAC65571.1; -; mRNA.
DR   IPI; IPI00137313; -.
DR   PIR; JC4975; JC4975.
DR   RefSeq; NP_032908.2; NM_008882.2.
DR   UniGene; Mm.2251; -.
DR   PDB; 3AL8; X-ray; 3.60 A; B=31-561.
DR   PDB; 3AL9; X-ray; 2.10 A; A/B=31-561.
DR   PDB; 3OKT; X-ray; 2.30 A; A=35-703.
DR   PDB; 3OKY; X-ray; 2.20 A; A=35-701.
DR   PDBsum; 3AL8; -.
DR   PDBsum; 3AL9; -.
DR   PDBsum; 3OKT; -.
DR   PDBsum; 3OKY; -.
DR   ProteinModelPortal; P70207; -.
DR   SMR; P70207; 36-702, 798-857, 952-1142, 1264-1891.
DR   STRING; P70207; -.
DR   PhosphoSite; P70207; -.
DR   PRIDE; P70207; -.
DR   Ensembl; ENSMUST00000027952; ENSMUSP00000027952; ENSMUSG00000026640.
DR   GeneID; 18845; -.
DR   KEGG; mmu:18845; -.
DR   UCSC; uc007een.1; mouse.
DR   CTD; 18845; -.
DR   MGI; MGI:107684; Plxna2.
DR   eggNOG; roNOG10635; -.
DR   HOGENOM; HBG716170; -.
DR   HOVERGEN; HBG105711; -.
DR   InParanoid; P70207; -.
DR   OMA; LEVQGNG; -.
DR   OrthoDB; EOG4WDD9V; -.
DR   PhylomeDB; P70207; -.
DR   NextBio; 295220; -.
DR   ArrayExpress; P70207; -.
DR   Bgee; P70207; -.
DR   CleanEx; MM_PLXNA2; -.
DR   Genevestigator; P70207; -.
DR   GermOnline; ENSMUSG00000026640; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0017154; F:semaphorin receptor activity; IGI:MGI.
DR   GO; GO:0007166; P:cell surface receptor linked signaling pathway; IDA:MGI.
DR   GO; GO:0051642; P:centrosome localization; IMP:MGI.
DR   GO; GO:0021935; P:cerebellar granule cell precursor tangential migration; IMP:MGI.
DR   GO; GO:0060174; P:limb bud formation; IEP:BHF-UCL.
DR   GO; GO:0021915; P:neural tube development; IEP:BHF-UCL.
DR   GO; GO:0060037; P:pharyngeal system development; IEP:BHF-UCL.
DR   GO; GO:0001756; P:somitogenesis; IEP:BHF-UCL.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002909; IPT_TIG_rcpt.
DR   InterPro; IPR003659; Plexin-like.
DR   InterPro; IPR016201; Plexin-like_fold.
DR   InterPro; IPR013548; Plexin_cytoplasmic_RasGAP_dom.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR001627; Semaphorin/CD100_Ag.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 4.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF08337; Plexin_cytopl; 1.
DR   Pfam; PF01437; PSI; 3.
DR   Pfam; PF01403; Sema; 1.
DR   Pfam; PF01833; TIG; 4.
DR   SMART; SM00429; IPT; 4.
DR   SMART; SM00423; PSI; 3.
DR   SMART; SM00630; Sema; 1.
DR   SUPFAM; SSF81296; Ig_E-set; 4.
DR   SUPFAM; SSF103575; Plexin-like_fold; 2.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   SUPFAM; SSF101912; Sema; 1.
DR   PROSITE; PS51004; SEMA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Glycoprotein; Membrane; Phosphoprotein;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     34       Potential.
FT   CHAIN        35   1894       Plexin-A2.
FT                                /FTId=PRO_0000232748.
FT   TOPO_DOM     35   1237       Extracellular (Potential).
FT   TRANSMEM   1238   1258       Helical; (Potential).
FT   TOPO_DOM   1259   1894       Cytoplasmic (Potential).
FT   DOMAIN       35    508       Sema.
FT   DOMAIN      858    951       IPT/TIG 1.
FT   DOMAIN      954   1037       IPT/TIG 2.
FT   DOMAIN     1041   1139       IPT/TIG 3.
FT   DOMAIN     1143   1228       IPT/TIG 4.
FT   COILED     1261   1310       Potential.
FT   MOD_RES    1432   1432       Phosphoserine.
FT   MOD_RES    1630   1630       Phosphoserine.
FT   MOD_RES    1633   1633       Phosphoserine.
FT   CARBOHYD     15     15       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     76     76       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    327    327       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    598    598       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    696    696       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    756    756       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1180   1180       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1205   1205       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    211    211       A -> P (in Ref. 2; AAH68155).
SQ   SEQUENCE   1894 AA;  211535 MW;  9F6C34F48BC29CEE CRC64;
     MEQRRFYLRA MQADNLSVVL LSVAWLLLAR GTTGMPQYST FHSENRDWTF NHLTVHRRTG
     AVYVGAINRV YKLTGNLTIQ VAHKTGPEED NKACYPPLIV QPCSEVLTLT NNVNKLLIID
     YSENRLLACG SLYQGVCKLL RLDDLFILVE PSHKKEHYLS SVNKTGTMYG VIVRSEGEDG
     KLFIGTAVDG KQDYFPTLSS RKLPRDPESS AMLDYELHSD FVSSLIKIPS DTLALVSHFD
     IFYIYGFASG GFVYFLTVQP ETPDGMAINS AGDLFYTSRI VRLCKDDPKF HSYVSLPFGC
     TRAGVEYRLL QAAYLAKPGE ALAQAFNISS DEDVLFAIFS KGQKQYHHPP DDSALCAFPI
     RAINLQIKER LQSCYHGEGN LELNWLLGKD VQCTKAPVPI DDNFCGLDIN QPLGGSTPVE
     GLTLYTTSRD RLTSVASYVY NGYSVVFVGT KSGKLKKIRA DGPPHGGVQY EMVSVFKDGS
     PILRDMAFSI NQLYLYVMSE RQVTRVPVES CEQYTTCGEC LSSGDPHCGW CALHNMCSRR
     DKCQRAWEAN RFAASISQCM SLEVHPNSIS VSDHSRLLSL VVNDAPNLSE GIACAFGNLT
     EVEGQVSGSQ VICISPGPKD VPVIPLDQDW FGLELQLRSK ETGKIFVSTE FKFYNCSAHQ
     LCLSCVNSAF RCHWCKYRNL CTHDPTTCSF QEGRINVSED CPQLVPTEEI LIPVGEVKPI
     TLKARNLPQP QSGQRGYECV LSIQGAVHRV PALRFNSSSV QCQNSSYQYD GMDISNLAVD
     FAVVWNGNFI IDNPQDLKVH LYKCAAQRES CGLCLKADHK FECGWCSGER RCTLHQHCPS
     TSSPWLDWSS HNVKCSNPQI TEILTVSGPP EGGTRVTIHG VNLGLDFSEI AHHVQVAGVP
     CTPIPGEYII AEQIVCEMGH AVIGTTSGPV RLCIGECKPE FMTKSHQQYT FVNPSVLSLS
     PIRGPESGGT MVTITGHYLG AGSSVAVYLG NQTCEFYGRS MNEIVCVSPP SSNGLGPVPV
     SVSVDRARVD SSLQFEYIDD PRVQRIEPEW SITSGHTPLT ITGFNLDVIQ EPRVRVKFNG
     KESVNVCTVV NTTTLTCLAP SLTSDYRPGL DTVERPDEFG FLFNNVQSLL IYNDTKFIYY
     PNPTFELLSP TGILDQKPGS PIILKGKNLC PPASGGAKLN YTVMIGETPC TVTVSETQLL
     CEPPNLTGQH KVMVHVGGMV FSPGSVSVIS DSLLTLPAII SIAAGGSLLL IIVIIVLIAY
     KRKSRENDLT LKRLQMQMDN LESRVALECK EAFAELQTDI NELTSDLDRS GIPYLDYRTY
     AMRVLFPGIE DHPVLRELEV QGNGQQHVEK ALKLFAQLIN NKVFLLTFIR TLELQRSFSM
     RDRGNVASLI MTGLQGRLEY ATDVLKQLLS DLIDKNLENK NHPKLLLRRT ESVAEKMLTN
     WFAFLLHKFL KECAGEPLFM LYCAIKQQME KGPIDAITGE ARYSLSEDKL IRQQIEYKTL
     ILNCVNPDNE NSPEIPVKVL NCDTITQVKE KILDAVYKNV PYSQRPRAVD MDLEWRQGRI
     ARVVLQDEDI TTKIEGDWKR LNTLMHYQVS DRSVVALVPK QTSSYNIPAS ASISRTSISR
     YDSSFRYTGS PDSLRSRVPM ITPDLESGVK VWHLVKNHDH GDQKEGDRGS KMVSEIYLTR
     LLATKGTLQK FVDDLFETLF STVHRGSALP LAIKYMFDFL DEQADRHSIH DTDVRHTWKS
     NCLPLRFWVN VIKNPQFVFD IHKGSITDAC LSVVAQTFMD SCSTSEHRLG KDSPSNKLLY
     AKDIPSYKNW VERYYADIAK LPAISDQDMN AYLAEQSRLH ATEFNMLSAL NEIYSYVSKY
     SEELIGALEQ DEQARRQRLA YKVEHLINAM SIES
//
ID   DCC_MOUSE               Reviewed;        1447 AA.
AC   P70211;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAR-2011, entry version 104.
DE   RecName: Full=Netrin receptor DCC;
DE   AltName: Full=Tumor suppressor protein DCC;
DE   Flags: Precursor;
GN   Name=Dcc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=96112625; PubMed=8570174;
RA   Cooper H.M., Armes P., Britto J., Gad J., Wilks A.F.;
RT   "Cloning of the mouse homologue of the deleted in colorectal cancer
RT   gene (mDCC) and its expression in the developing mouse embryo.";
RL   Oncogene 11:2243-2254(1995).
RN   [2]
RP   SEQUENCE REVISION.
RA   Cooper H.M.;
RL   Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INTERACTION WITH DSCAM.
RX   PubMed=18585357; DOI=10.1016/j.cell.2008.05.030;
RA   Ly A., Nikolaev A., Suresh G., Zheng Y., Tessier-Lavigne M., Stein E.;
RT   "DSCAM is a netrin receptor that collaborates with DCC in mediating
RT   turning responses to netrin-1.";
RL   Cell 133:1241-1254(2008).
CC   -!- FUNCTION: Receptor for netrin required for axon guidance. Mediates
CC       axon attraction of neuronal growth cones in the developing nervous
CC       system upon ligand binding. Its association with UNC5 proteins may
CC       trigger signaling for axon repulsion. It also acts as a dependence
CC       receptor required for apoptosis induction when not associated with
CC       netrin ligand. Implicated as a tumor suppressor gene.
CC   -!- SUBUNIT: Interacts with the cytoplasmic part of UNC5A, UNC5B,
CC       UNC5C and probably UNC5D (By similarity). Interacts with DSCAM.
CC   -!- INTERACTION:
CC       Q9ERC8:Dscam; NbExp=1; IntAct=EBI-1798863, EBI-1798601;
CC       P56270:MAZ (xeno); NbExp=1; IntAct=EBI-1798863, EBI-1809742;
CC       P56671:Maz; NbExp=1; IntAct=EBI-1798863, EBI-1809712;
CC       O09118:Ntn1; NbExp=1; IntAct=EBI-1798863, EBI-1798844;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC       Name=A;
CC         IsoId=P70211-1; Sequence=Displayed;
CC       Name=C;
CC         IsoId=P70211-2; Sequence=VSP_002501;
CC       Name=B;
CC         IsoId=P70211-3; Sequence=VSP_018807;
CC         Note=Produced by alternative initiation at Met-85 of isoform A;
CC   -!- TISSUE SPECIFICITY: In the embryo, expressed at high levels in the
CC       developing brain and neural tube. In adult, highly expressed in
CC       brain with very low levels found in testis, heart and thymus.
CC       Isoform C is expressed only in the embryo.
CC   -!- DEVELOPMENTAL STAGE: Low levels in early gestation. Highest levels
CC       expressed during mid gestation. Levels decrease in late gestation
CC       and remain at this level in the adult.
CC   -!- PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its
CC       subsequent proteasomal degradation (By similarity).
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. DCC family.
CC   -!- SIMILARITY: Contains 6 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 4 Ig-like C2-type (immunoglobulin-like)
CC       domains.
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DR   EMBL; X85788; CAA59786.1; -; mRNA.
DR   IPI; IPI00137347; -.
DR   IPI; IPI00225034; -.
DR   IPI; IPI00759859; -.
DR   UniGene; Mm.167882; -.
DR   ProteinModelPortal; P70211; -.
DR   SMR; P70211; 38-1047.
DR   IntAct; P70211; 15.
DR   STRING; P70211; -.
DR   PhosphoSite; P70211; -.
DR   PRIDE; P70211; -.
DR   Ensembl; ENSMUST00000114943; ENSMUSP00000110593; ENSMUSG00000060534.
DR   UCSC; uc008fop.1; mouse.
DR   MGI; MGI:94869; Dcc.
DR   eggNOG; roNOG04119; -.
DR   GeneTree; ENSGT00590000082947; -.
DR   HOGENOM; HBG358293; -.
DR   HOVERGEN; HBG005455; -.
DR   InParanoid; P70211; -.
DR   OrthoDB; EOG4WM4SV; -.
DR   ArrayExpress; P70211; -.
DR   Bgee; P70211; -.
DR   CleanEx; MM_DCC; -.
DR   Genevestigator; P70211; -.
DR   GermOnline; ENSMUSG00000060534; Mus musculus.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0033563; P:dorsal/ventral axon guidance; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0021965; P:spinal cord ventral commissure morphogenesis; IMP:MGI.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR010560; Neogenin_C.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 10.
DR   Pfam; PF00041; fn3; 6.
DR   Pfam; PF07679; I-set; 3.
DR   Pfam; PF06583; Neogenin_C; 1.
DR   SMART; SM00060; FN3; 6.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 3.
DR   SUPFAM; SSF49265; FN_III-like; 6.
DR   PROSITE; PS50853; FN3; 6.
DR   PROSITE; PS50835; IG_LIKE; 4.
PE   1: Evidence at protein level;
KW   Alternative initiation; Alternative splicing; Apoptosis;
KW   Developmental protein; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Phosphoprotein; Receptor; Repeat;
KW   Signal; Transmembrane; Transmembrane helix; Tumor suppressor;
KW   Ubl conjugation.
FT   SIGNAL        1     25       Potential.
FT   CHAIN        26   1447       Netrin receptor DCC.
FT                                /FTId=PRO_0000014745.
FT   TOPO_DOM     26   1097       Extracellular (Potential).
FT   TRANSMEM   1098   1122       Helical; (Potential).
FT   TOPO_DOM   1123   1447       Cytoplasmic (Potential).
FT   DOMAIN       36    135       Ig-like C2-type 1.
FT   DOMAIN      139    229       Ig-like C2-type 2.
FT   DOMAIN      234    326       Ig-like C2-type 3.
FT   DOMAIN      331    416       Ig-like C2-type 4.
FT   DOMAIN      429    520       Fibronectin type-III 1.
FT   DOMAIN      528    616       Fibronectin type-III 2.
FT   DOMAIN      622    714       Fibronectin type-III 3.
FT   DOMAIN      726    814       Fibronectin type-III 4.
FT   DOMAIN      843    939       Fibronectin type-III 5.
FT   DOMAIN      944   1041       Fibronectin type-III 6.
FT   MOD_RES     868    868       Phosphoserine (By similarity).
FT   MOD_RES    1073   1073       Phosphoserine (By similarity).
FT   MOD_RES    1074   1074       Phosphothreonine (By similarity).
FT   CARBOHYD     60     60       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     94     94       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    299    299       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    318    318       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    478    478       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    628    628       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    702    702       N-linked (GlcNAc...) (Potential).
FT   DISULFID     61    117       By similarity.
FT   DISULFID    161    212       By similarity.
FT   DISULFID    261    310       By similarity.
FT   DISULFID    352    400       By similarity.
FT   VAR_SEQ       1     84       Missing (in isoform B).
FT                                /FTId=VSP_018807.
FT   VAR_SEQ     819    838       Missing (in isoform C).
FT                                /FTId=VSP_002501.
SQ   SEQUENCE   1447 AA;  158299 MW;  0D1F1097C22D5B9F CRC64;
     MENSLGCVWV PKLAFVLFGA SLLSAHLQVT GFQIKPFTSL HFVSEPSDAV TMRGGNVLLN
     CSAESDRGVP VIKWKKDGLI LALGMDDRKQ QLPNGSLLIQ NILHSRHHKP DEGLYQCEAS
     LADSGSIISR TAKVTVAGPL RFLSQTESIT AFMGDTVLLK CEVIGEPMPT IHWQKNQQDL
     NPLPGDSRVV VLPSGALQIS RLQPGDSGVY RCSARNPASI RTGNEAEVRI LSDPGLHRQL
     YFLQRPSNVI AIEGKDAVLE CCVSGYPPPS FTWLRGEEVI QLRSKKYSLL GGSNLLISNV
     TDDDSGTYTC VVTYKNENIS ASAELTVLVP PWFLNHPSNL YAYESMDIEF ECAVSGKPVP
     TVNWMKNGDV VIPSDYFQIV GGSNLRILGV VKSDEGFYQC VAENEAGNAQ SSAQLIVPKP
     AIPSSSILPS APRDVLPVLV SSRFVRLSWR PPAEAKGNIQ TFTVFFSREG DNRERALNTT
     QPGSLQLTVG NLKPEAMYTF RVVAYNEWGP GESSQPIKVA TQPELQVPGP VENLHAVSTS
     PTSILITWEP PAYANGPVQG YRLFCTEVST GKEQNIEVDG LSYKLEGLKK FTEYTLRFLA
     YNRYGPGVST DDITVVTLSD VPSAPPQNIS LEVVNSRSIK VSWLPPPSGT QNGFITGYKI
     RHRKTTRRGE METLEPNNLW YLFTGLEKGS QYSFQVSAMT VNGTGPPSNW YTAETPENDL
     DESQVPDQPS SLHVRPQTNC IIMSWTPPLN PNIVVRGYII GYGVGSPYAE TVRVDSKQRY
     YSIERLESSS HYVISLKAFN NAGEGVPLYE SATTRSITDP TDPVDYYPLL DDFPTSGPDV
     STPMLPPVGV QAVALTHEAV RVSWADNSVP KNQKTSDVRL YTVRWRTSFS ASAKYKSEDT
     TSLSYTATGL KPNTMYEFSV MVTKNRRSST WSMTAHATTY EAAPTSAPKD LTVITREGKP
     RAVIVSWQPP LEANGKITAY ILFYTLDKNI PIDDWIMETI SGDRLTHQIM DLSLDTMYYF
     RIQARNVKGV GPLSDPILFR TLKVEHPDKM ANDQGRHGDG GYWPVDTNLI DRSTLNEPPI
     GQMHPPHGSV TPQKNSNLLV ITVVTVGVLT VLVVVIVAVI CTRRSSAQQR KKRATHSGSK
     RKGSQKDLRP PDLWIHHEEM EMKNIEKPTG TDPAGRDSPI QSCQDLTPVS HSQSETQMGS
     KSASHSGQDT EDAGSSMSTL ERSLAARRAT RAKLMIPMEA QSSNPAVVSA IPVPTLESAQ
     YPGILPSPTC GYPHPQFTLR PVPFPTLSVD RGFGAGRTQS VSEGPTTQQQ PMLPPAQPEH
     PSSEEAPSRT IPTACVRPTH PLRSFANPLL PPPMSAIEPK VPYTPLLSQP GPTLPKTHVK
     TASLGLAGKA RSPLLPVSVP TAPEVSEESH KPTEDPASVY EQDDLSEQMA SLEGLMKQLN
     AITGSAF
//
ID   ITPR3_MOUSE             Reviewed;        2670 AA.
AC   P70227; Q5DWM4; Q8CED5; Q91Z08;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 3.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Inositol 1,4,5-trisphosphate receptor type 3;
DE   AltName: Full=IP3 receptor isoform 3;
DE            Short=IP3R 3;
DE            Short=InsP3R3;
DE   AltName: Full=Type 3 inositol 1,4,5-trisphosphate receptor;
DE            Short=Type 3 InsP3 receptor;
GN   Name=Itpr3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP   LYS-507 AND ARG-510.
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=15632133; DOI=10.1074/jbc.M413824200;
RA   Iwai M., Tateishi Y., Hattori M., Mizutani A., Nakamura T.,
RA   Futatsugi A., Inoue T., Furuichi T., Michikawa T., Mikoshiba K.;
RT   "Molecular cloning of mouse type 2 and type 3 inositol 1,4,5-
RT   trisphosphate receptors and identification of a novel type 2 receptor
RT   splice variant.";
RL   J. Biol. Chem. 280:10305-10317(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1857-2670.
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2181-2670.
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2406-2609.
RC   TISSUE=Placenta;
RX   MEDLINE=92262420; PubMed=1374893; DOI=10.1073/pnas.89.10.4265;
RA   Ross C.A., Danoff S.K., Schell M.J., Snyder S.H., Ullrich A.;
RT   "Three additional inositol 1,4,5-trisphosphate receptors: molecular
RT   cloning and differential localization in brain and peripheral
RT   tissues.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:4265-4269(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2433-2629.
RC   STRAIN=C3H; TISSUE=Embryo;
RX   MEDLINE=97218118; PubMed=9065779;
RA   De Smedt H., Missiaen L., Parys J.B., Henning R.H., Sienaert I.,
RA   Vanlingen S., Gijsens A., Himpens B., Casteels R.;
RT   "Isoform diversity of the inositol trisphosphate receptor in cell
RT   types of mouse origin.";
RL   Biochem. J. 322:575-583(1997).
RN   [6]
RP   INTERACTION WITH SIGMAR1.
RX   PubMed=11149946; DOI=10.1073/pnas.021413698;
RA   Hayashi T., Su T.-P.;
RT   "Regulating ankyrin dynamics: roles of sigma-1 receptors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:491-496(2001).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-934 AND SER-1152, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Receptor for inositol 1,4,5-trisphosphate, a second
CC       messenger that mediates the release of intracellular calcium.
CC   -!- SUBUNIT: Homotetramer. Interacts with TRPC1, TRPC3, TRPC4 and
CC       CABP1 (By similarity). Interacts with SIGMAR1.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
CC   -!- DOMAIN: The receptor contains a calcium channel in its C-terminal
CC       extremity. Its large N-terminal cytoplasmic region has the ligand-
CC       binding site in the N-terminus and modulatory sites in the middle
CC       portion immediately upstream of the channel region.
CC   -!- PTM: Phosphorylated on tyrosine residues (By similarity).
CC   -!- SIMILARITY: Belongs to the InsP3 receptor family.
CC   -!- SIMILARITY: Contains 5 MIR domains.
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DR   EMBL; AB182289; BAD90683.1; -; mRNA.
DR   EMBL; AK028491; BAC25977.1; -; mRNA.
DR   EMBL; BC010323; AAH10323.1; -; mRNA.
DR   EMBL; M90088; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; Z71174; CAA94862.1; -; mRNA.
DR   IPI; IPI00137400; -.
DR   RefSeq; NP_542120.2; NM_080553.3.
DR   UniGene; Mm.458106; -.
DR   PDB; 3JRR; X-ray; 1.90 A; A/B=1-224.
DR   PDBsum; 3JRR; -.
DR   ProteinModelPortal; P70227; -.
DR   SMR; P70227; 4-224, 237-602.
DR   STRING; P70227; -.
DR   PhosphoSite; P70227; -.
DR   PRIDE; P70227; -.
DR   Ensembl; ENSMUST00000049308; ENSMUSP00000038150; ENSMUSG00000042644.
DR   GeneID; 16440; -.
DR   KEGG; mmu:16440; -.
DR   UCSC; uc008bfi.1; mouse.
DR   CTD; 16440; -.
DR   MGI; MGI:96624; Itpr3.
DR   eggNOG; roNOG05144; -.
DR   HOGENOM; HBG315164; -.
DR   HOVERGEN; HBG052158; -.
DR   InParanoid; P70227; -.
DR   OMA; MMSTMVL; -.
DR   OrthoDB; EOG4GQQ42; -.
DR   NextBio; 289691; -.
DR   ArrayExpress; P70227; -.
DR   Bgee; P70227; -.
DR   CleanEx; MM_ITPR3; -.
DR   Genevestigator; P70227; -.
DR   GermOnline; ENSMUSG00000042644; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0005730; C:nucleolus; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR   GO; GO:0005220; F:inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IDA:MGI.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0050913; P:sensory perception of bitter taste; IMP:MGI.
DR   GO; GO:0050916; P:sensory perception of sweet taste; IMP:MGI.
DR   GO; GO:0050917; P:sensory perception of umami taste; IMP:MGI.
DR   InterPro; IPR000699; Ca-rel_channel.
DR   InterPro; IPR014821; Ins145_P3_rcpt.
DR   InterPro; IPR000493; InsP3_rcpt-bd.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003608; MIR.
DR   InterPro; IPR016093; MIR_motif.
DR   InterPro; IPR013662; RIH_assoc-dom.
DR   InterPro; IPR015925; Ryanodine_recept-rel.
DR   PANTHER; PTHR13715; Ryanodine_recept-rel; 1.
DR   Pfam; PF08709; Ins145_P3_rec; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02815; MIR; 1.
DR   Pfam; PF08454; RIH_assoc; 1.
DR   Pfam; PF01365; RYDR_ITPR; 2.
DR   PRINTS; PR00779; INSP3RECEPTR.
DR   SMART; SM00472; MIR; 4.
DR   SUPFAM; SSF82109; MIR; 2.
DR   PROSITE; PS50919; MIR; 5.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Calcium channel; Calcium transport;
KW   Endoplasmic reticulum; Ion transport; Ionic channel;
KW   Ligand-gated ion channel; Membrane; Phosphoprotein; Receptor; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1   2670       Inositol 1,4,5-trisphosphate receptor
FT                                type 3.
FT                                /FTId=PRO_0000153929.
FT   TOPO_DOM      1   2233       Cytoplasmic (Potential).
FT   TRANSMEM   2234   2254       Helical; (Potential).
FT   TOPO_DOM   2255   2262       Extracellular (Potential).
FT   TRANSMEM   2263   2283       Helical; (Potential).
FT   TOPO_DOM   2284   2292       Cytoplasmic (Potential).
FT   TRANSMEM   2293   2310       Helical; (Potential).
FT   TOPO_DOM   2311   2324       Extracellular (Potential).
FT   TRANSMEM   2325   2345       Helical; (Potential).
FT   TOPO_DOM   2346   2367       Cytoplasmic (Potential).
FT   TRANSMEM   2368   2388       Helical; (Potential).
FT   TOPO_DOM   2389   2495       Extracellular (Potential).
FT   TRANSMEM   2496   2516       Helical; (Potential).
FT   TOPO_DOM   2517   2670       Cytoplasmic (Potential).
FT   DOMAIN      113    173       MIR 1.
FT   DOMAIN      174    224       MIR 2.
FT   DOMAIN      232    288       MIR 3.
FT   DOMAIN      295    372       MIR 4.
FT   DOMAIN      378    434       MIR 5.
FT   MOD_RES     916    916       Phosphoserine (By similarity).
FT   MOD_RES     934    934       Phosphoserine.
FT   MOD_RES    1152   1152       Phosphoserine.
FT   MOD_RES    1813   1813       Phosphoserine (By similarity).
FT   MOD_RES    1832   1832       Phosphoserine (By similarity).
FT   MOD_RES    2582   2582       Phosphotyrosine (Potential).
FT   MOD_RES    2669   2669       Phosphoserine (By similarity).
FT   MUTAGEN     507    507       K->A: Loss of binding activity.
FT   MUTAGEN     510    510       R->A: Loss of binding activity.
FT   CONFLICT   2406   2413       SRASPLGM -> FPPSRARR (in Ref. 4).
FT   CONFLICT   2430   2430       D -> E (in Ref. 4; M90088).
FT   CONFLICT   2447   2447       P -> L (in Ref. 4; M90088).
FT   CONFLICT   2605   2609       RAMSL -> LGSTS (in Ref. 4).
SQ   SEQUENCE   2670 AA;  304275 MW;  9B5BA808B195C58F CRC64;
     MNEMSSFLHI GDIVSLYAEG SVNGFISTLG LVDDRCVVEP AAGDLDNPPK KFRDCLFKVC
     PMNRYSAQKQ YWKAKQTKQD KEKIADVVLL QKLQHAAQME QKQNDTENKK VHGDVVKYGS
     VIQLLHMKSN KYLTVNKRLP ALLEKNAMRV TLDATGNEGS WLFIQPFWKL RSNGDNVVVG
     DKVILNPVNA GQPLHASNYE LSDNAGCKEV NSVNCNTSWK INLFMQFRDH LEEVLKGGDV
     VRLFHAEQEK FLTCDEYRGK LQVFLRTTLR QSATSATSSN ALWEVEVVHH DPCRGGAGHW
     NGLYRFKHLA TGNYLAAEEN PSYKGDVSDP KAAGLGAQGR TGRRNAGEKI KYRLVAVPHG
     NDIASLFELD PTTLQKTDSF VPRNSYVRLR HLCTNTWIQS TNAPIDVEEE RPIRLMLGTC
     PTKEDKEAFA IVSVPVSEIR DLDFANDASS MLASAVEKLN EGFISQNDRR FVIQLLEDLV
     FFVSDVPNNG QNVLDIMVTK PNRERQKLMR EQNILKQIFG ILKAPFRDKG GEGPLVRLEE
     LSDQKNAPYQ YMFRLCYRVL RHSQEDYRKN QEHIAKQFGM MQSQIGYDIL AEDTITALLH
     NNRKLLEKHI TKTEVETFVS LVRKNREPRF LDYLSDLCVS NRIAIPVTQE LICKCVLDPK
     NSDILIQTEL RPVKEMAQSH EYLSIEYSEE EVWLTWTDRN NEHHEKSVRQ LAQEARAGNA
     HDENVLSYYR YQLKLFARMC LDRQYLAIDE ISKQLGVELL FLCMADEMLP FDLRASFCHL
     MLHVHVDRDP QELVTPVKFA RLWTEIPTAI TIKDYDSNLN ASRDDKKNKF ASTMEFVEDY
     LNNVVSEAVP FANDEKNILT FEVVSLAHNL IYFGFYSFSE LLRLTRTLLG IIDCIQAPAA
     MLQAYEEPGG KNVRRSIQGV GHMMSTMVLS RKQSVFGASS LPAGVGVPEQ LDRSKFEDNE
     HTVVMETKLK ILEILQFILN VRLDYRISYL LSVFKKEFVE VFPMQDSGAD GTAPAFDSST
     ATMNLDRIGE QAEAMFGVGK TSSMLEVDDE GGRMFLRVLL HLTMHDYPSL VSGALQLLFK
     HFSQRQEAMH TFKQVQLLIS AQDVENYKVI KSELDRLRTM VEKSELWVDK KGSVKGEEVE
     AGATKDKKER PSDEEGFLQP HGEKSSENYQ IVKGILERLN KMCGVGEQMR KKQQRLLKNM
     DAHKVMLDLL QIPYDKSDNK MLEILRYTHQ FLQKFCAGNP GNQALLHKHL QLFLTPGLLE
     AETMQHIFLN NYQLCSEISE PVLQHFVHLL ATHGRHVQYL DFLHTVIKAE GKYVKKCQDM
     IMTELTNAGD DVVVFYNDKA SLAHLLDMMK AARDGVEDHS PLMYHISLVD LLAACAEGKN
     VYTEIKCTSL LPLEDVVTVV THEDCITEVK MAYVNFVNHC YVDTEVEMKE IYTSNHIWTL
     FENFTLDMAL VCNKREKRLS DPTLEKYVLT VVLDTISAFF SSPFSENSTS LQTHQTIVVQ
     LLQSTTRLLE CPWLQQQHKG SVEACVRTLA MVAKSRAILL PMDLDAHMSA LLSSGGSCSA
     AAQRSAANYK TATRTFPRVI PTANQWDYKN IIEKLQDIIM ALEERLKPLV QAELSVLVDM
     LHWPELLFPE GSEAYQRCES GGFLSKLIRH TKGLMESEEK LCVKVLRTLQ QMLLKKSKFG
     DRGNQLRKML LQNYLQNRKS GARGELTDPT GSGLDQDWSA IAATQCRLDK EGATKLVCDL
     ITSTKNEKIF QESIGLAIRL LDGGNTEIQK SFYNLMTSDK KSERFFKVLH DRMKRAQQET
     KSTVAVNMSD LGSQPREDRE PADPATKGRV SSFSMPSSSR YLLGLGLHRG HDMSERAQNN
     EMGTSVLIMR PILRFLQLLC ENHNRDLQNF LRCQNNKTNY NLVCETLQFL DIMCGSTTGG
     LGLLGLYINE DNVGLVIQTL ETLTEYCQGP CHENQTCIVT HESNGIDIIT ALILNDISPL
     CKYRMDLVLQ LKDNASKLLL ALMESRHDSE NAERILISLR PQELVDVIKK AYLQEEEREN
     SEVSPREVGH NIYILALQLS RHNKQLQHLL KPVRRIQEEE AEGISSMLSL NNKQLSQMLK
     SSAPAQEEEE DPLAYYENHT SQIEIVRQDR SMEQIVFPVP AICQFLTEET KHRLFTTTEQ
     DEQGSKVSDF FDQSSFLHNE MEWQRRLRSM PLIYWFSRRM TLWGSISFNL AVFINIIIAF
     FYPYVEGAST GVLGSPLISL LFWILICFSI AALFTKRYSV RPLIVALILR SIYYLGIGPT
     LNILGALNLT NKIVFVVSFV GNRGTFIRGY KAMVMDMEFL YHVGYILTSV LGLFAHELFY
     SILLFDLIYR EETLFNVIKS VTRNGRSILL TALLALILVY LFSIVGFLFL KDDFILEVDR
     LPGNHSRASP LGMPHGAATF MGTCSGDKMD CVSEVSVPEI LEEDEEPDST ERACDTLLMC
     IVTVMNHGLR NGGGVGDILR KPSKDESLFP ARVVYDLLFF FIVIIIVLNL IFGVIIDTFA
     DLRSEKQKKE EILKTTCFIC GLERDKFDNK TVSFEEHIKL EHNMWNYLYF IVLVRVKNKT
     DYTGPESYVA QMIKNKNLDW FPRMRAMSLV SGEGEGEQNE IRILQEKLGS TMKLVSHLTS
     QLNELKEQMT EQRKRRQRLG FVDVQNCMSR
//
ID   CHL1_MOUSE              Reviewed;        1209 AA.
AC   P70232; Q8BS24; Q8C6W0; Q8C823; Q8VBY7;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Neural cell adhesion molecule L1-like protein;
DE   AltName: Full=Cell adhesion molecule with homology to L1CAM;
DE   AltName: Full=Chl1-like protein;
DE   AltName: Full=Close homolog of L1;
DE   Contains:
DE     RecName: Full=Processed neural cell adhesion molecule L1-like protein;
DE   Flags: Precursor;
GN   Name=Chl1; Synonyms=Call;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
RP   GLYCOSYLATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=8921253; DOI=10.1111/j.1460-9568.1996.tb01306.x;
RA   Holm J., Hillenbrand R., Steuber V., Bartsch U., Moos M., Luebbert H.,
RA   Montag D., Schachner M.;
RT   "Structural features of a close homologue of L1 (CHL1) in the mouse: a
RT   new member of the L1 family of neural recognition molecules.";
RL   Eur. J. Neurosci. 8:1613-1629(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-425 AND 666-1209 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Aorta, Head, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-129, FUNCTION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=129/Sv;
RX   MEDLINE=22278859; PubMed=12391163;
RX   DOI=10.1128/MCB.22.22.7967-7981.2002;
RA   Montag-Sallaz M., Schachner M., Montag D.;
RT   "Misguided axonal projections, neural cell adhesion molecule 180 mRNA
RT   upregulation, and altered behavior in mice deficient for the close
RT   homolog of L1.";
RL   Mol. Cell. Biol. 22:7967-7981(2002).
RN   [4]
RP   FUNCTION, DEVELOPMENTAL STAGE, INTERACTION WITH L1CAM, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=10103075; DOI=10.1046/j.1460-9568.1999.00496.x;
RA   Hillenbrand R., Molthagen M., Montag D., Schachner M.;
RT   "The close homologue of the neural adhesion molecule L1 (CHL1):
RT   patterns of expression and promotion of neurite outgrowth by
RT   heterophilic interactions.";
RL   Eur. J. Neurosci. 11:813-826(1999).
RN   [5]
RP   FUNCTION.
RX   PubMed=10022583;
RX   DOI=10.1002/(SICI)1097-4695(19990215)38:3<428::AID-NEU10>3.0.CO;2-6;
RA   Chen S., Mantei N., Dong L., Schachner M.;
RT   "Prevention of neuronal cell death by neural adhesion molecules L1 and
RT   CHL1.";
RL   J. Neurobiol. 38:428-439(1999).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=14659567; DOI=10.1016/S0166-4328(03)00114-1;
RA   Pratte M., Rougon G., Schachner M., Jamon M.;
RT   "Mice deficient for the close homologue of the neural adhesion cell L1
RT   (CHL1) display alterations in emotional reactivity and motor
RT   coordination.";
RL   Behav. Brain Res. 147:31-39(2003).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12812975; DOI=10.1093/hmg/ddg165;
RA   Frints S.G.M., Marynen P., Hartmann D., Fryns J.-P., Steyaert J.,
RA   Schachner M., Rolf B., Craessaerts K., Snellinx A., Hollanders K.,
RA   D'Hooge R., De Deyn P.P., Froyen G.;
RT   "CALL interrupted in a patient with non-specific mental retardation:
RT   gene dosage-dependent alteration of murine brain development and
RT   behavior.";
RL   Hum. Mol. Genet. 12:1463-1474(2003).
RN   [8]
RP   FUNCTION, INTERACTION WITH ANK3; ITGB1/ITGA1 HETERODIMER AND
RP   ITGB1/ITGA2 HETERODIMER, MOTIFS, AND MUTAGENESIS OF 555-ASP--ALA-558
RP   AND TYR-1186.
RX   PubMed=12721290; DOI=10.1074/jbc.M303084200;
RA   Buhusi M., Midkiff B.R., Gates A.M., Richter M., Schachner M.,
RA   Maness P.F.;
RT   "Close homolog of L1 is an enhancer of integrin-mediated cell
RT   migration.";
RL   J. Biol. Chem. 278:25024-25031(2003).
RN   [9]
RP   FUNCTION, AND CLEAVAGE BY ADAM8.
RX   PubMed=14761956; DOI=10.1074/jbc.M400560200;
RA   Naus S., Richter M., Wildeboer D., Moss M., Schachner M.,
RA   Bartsch J.W.;
RT   "Ectodomain shedding of the neural recognition molecule CHL1 by the
RT   metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and
RT   suppresses neuronal cell death.";
RL   J. Biol. Chem. 279:16083-16090(2004).
RN   [10]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15504324; DOI=10.1016/j.neuron.2004.10.016;
RA   Demyanenko G.P., Schachner M., Anton E., Schmid R., Feng G., Sanes J.,
RA   Maness P.F.;
RT   "Close homolog of L1 modulates area-specific neuronal positioning and
RT   dendrite orientation in the cerebral cortex.";
RL   Neuron 44:423-437(2004).
RN   [11]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16623841; DOI=10.1111/j.1460-9568.2006.04710.x;
RA   Nikonenko A.G., Sun M., Lepsveridze E., Apostolova I., Petrova I.,
RA   Irintchev A., Dityatev A., Schachner M.;
RT   "Enhanced perisomatic inhibition and impaired long-term potentiation
RT   in the CA1 region of juvenile CHL1-deficient mice.";
RL   Eur. J. Neurosci. 23:1839-1852(2006).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1128 AND SER-1148, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Extracellular matrix and cell adhesion protein that
CC       plays a role in nervous system development and in synaptic
CC       plasticity. Both soluble and membranous forms promote neurite
CC       outgrowth of cerebellar and hippocampal neurons and suppress
CC       neuronal cell death. Plays a role in neuronal positioning of
CC       pyramidal neurons as well as in regulation of both the number of
CC       interneurons and the efficacy of GABAergic synapses. May play a
CC       role in regulating cell migration in nerve regeneration and
CC       cortical development. Potentiates integrin-dependent cell
CC       migration towards extracellular matrix proteins. Recruits ANK3 to
CC       the plasma membrane.
CC   -!- SUBUNIT: May interacts with L1CAM. May interact with ITGB1/ITGA1
CC       heterodimer and ITGB1/ITGA2 heterodimer as well as with ANK3.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Note=Soluble forms produced by cleavage/shedding also
CC       exist.
CC   -!- SUBCELLULAR LOCATION: Processed neural cell adhesion molecule L1-
CC       like protein: Secreted, extracellular space, extracellular matrix.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P70232-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P70232-2; Sequence=VSP_020083, VSP_020084, VSP_020085;
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, in the cerebellum and
CC       in the spinal cord. Detected in the retina and the optic nerve.
CC       Expressed in neurons and glial cells in the central nervous system
CC       and by Schwann cells in the peripheral nervous system.
CC   -!- DEVELOPMENTAL STAGE: Not detectable in the forebrain at E11,
CC       weakly detectable at E13 with highest detection at E18 to
CC       postnatal day 7. Down-regulated at postnatal day 15 and further
CC       reduced in four-week-old animals.
CC   -!- DOMAIN: The FIG[AQ]Y motif seems to be an ankyrin recruitment
CC       region.
CC   -!- DOMAIN: The DGEA motif seems to be a recognition site for
CC       integrin.
CC   -!- PTM: Cleavage by metalloprotease ADAM8 in the extracellular part
CC       generates 2 soluble forms (125 kDa and 165 kDa) in vitro and is
CC       inhibited by metalloprotease inhibitors. In brain extracts, these
CC       two soluble forms are also present and are dramatically reduced in
CC       mice lacking ADAM8.
CC   -!- PTM: N-glycosylated. Contains N-linked oligosaccharides with a
CC       sulfated carbohydrate structure type HNK-1 (SO4-3-
CC       GlcUABeta1,3GalBeta1,4GlcNAc).
CC   -!- PTM: O-glycosylated.
CC   -!- DISRUPTION PHENOTYPE: Mice exhibit misguided axonal projections
CC       and aberrant axonal connectivity. They show alterations of
CC       hippocampal fiber organization and olfactory axon projections.
CC       Their exploratory behavior in novel environments is altered
CC       suggesting deficits in information processing and in attention.
CC       They also display signs of decreased stress and are more sociable
CC       and less aggressive. Heterozygous mice exhibit half levels of CHL1
CC       expression in the hippocampus compared to their wild-type
CC       littermates, reflecting a gene dosage effect.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC       L1/neurofascin/NgCAM family.
CC   -!- SIMILARITY: Contains 4 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 6 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC30699.1; Type=Frameshift; Positions=616, 624, 631, 632, 642, 645;
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DR   EMBL; X94310; CAA63972.1; -; mRNA.
DR   EMBL; AK040765; BAC30699.1; ALT_FRAME; mRNA.
DR   EMBL; AK048639; BAC33405.1; -; mRNA.
DR   EMBL; AK053039; BAC35247.2; -; mRNA.
DR   EMBL; AJ319655; CAC88131.1; -; Genomic_DNA.
DR   EMBL; AJ319656; CAC88131.1; JOINED; Genomic_DNA.
DR   EMBL; AJ319657; CAC88131.1; JOINED; Genomic_DNA.
DR   IPI; IPI00222149; -.
DR   IPI; IPI00404529; -.
DR   PIR; T42718; T42718.
DR   RefSeq; NP_031723.2; NM_007697.2.
DR   UniGene; Mm.251288; -.
DR   ProteinModelPortal; P70232; -.
DR   SMR; P70232; 7-1015.
DR   MINT; MINT-4106227; -.
DR   STRING; P70232; -.
DR   PhosphoSite; P70232; -.
DR   PRIDE; P70232; -.
DR   Ensembl; ENSMUST00000032163; ENSMUSP00000032163; ENSMUSG00000030077.
DR   Ensembl; ENSMUST00000089225; ENSMUSP00000086634; ENSMUSG00000030077.
DR   GeneID; 12661; -.
DR   KEGG; mmu:12661; -.
DR   CTD; 12661; -.
DR   MGI; MGI:1098266; Chl1.
DR   GeneTree; ENSGT00590000082983; -.
DR   HOVERGEN; HBG000144; -.
DR   OrthoDB; EOG4RFKRR; -.
DR   NextBio; 281890; -.
DR   ArrayExpress; P70232; -.
DR   Bgee; P70232; -.
DR   CleanEx; MM_CHL1; -.
DR   Genevestigator; P70232; -.
DR   GermOnline; ENSMUSG00000030077; Mus musculus.
DR   GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; EXP:Reactome.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR   GO; GO:0007411; P:axon guidance; IMP:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0050890; P:cognition; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 10.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF07679; I-set; 5.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 3.
DR   SUPFAM; SSF49265; FN_III-like; 4.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS50835; IG_LIKE; 6.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Cell membrane;
KW   Developmental protein; Differentiation; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Immunoglobulin domain; Membrane;
KW   Neurogenesis; Phosphoprotein; Repeat; Secreted; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     25       Potential.
FT   CHAIN        26   1209       Neural cell adhesion molecule L1-like
FT                                protein.
FT                                /FTId=PRO_0000247897.
FT   CHAIN        26      ?       Processed neural cell adhesion molecule
FT                                L1-like protein (Potential).
FT                                /FTId=PRO_0000314778.
FT   TOPO_DOM     26   1083       Extracellular (Potential).
FT   TRANSMEM   1084   1104       Helical; (Potential).
FT   TOPO_DOM   1105   1209       Cytoplasmic (Potential).
FT   DOMAIN       35    124       Ig-like C2-type 1.
FT   DOMAIN      128    223       Ig-like C2-type 2.
FT   DOMAIN      235    328       Ig-like C2-type 3.
FT   DOMAIN      331    417       Ig-like C2-type 4.
FT   DOMAIN      423    510       Ig-like C2-type 5.
FT   DOMAIN      515    607       Ig-like C2-type 6.
FT   DOMAIN      611    707       Fibronectin type-III 1.
FT   DOMAIN      711    804       Fibronectin type-III 2.
FT   DOMAIN      809    911       Fibronectin type-III 3.
FT   DOMAIN      916   1011       Fibronectin type-III 4.
FT   MOTIF       555    558       DGEA.
FT   MOTIF      1182   1186       FIG[AQ]Y.
FT   SITE        753    754       Cleavage; by ADAM8.
FT   SITE       1040   1041       Cleavage; by ADAM8.
FT   MOD_RES    1128   1128       Phosphoserine.
FT   MOD_RES    1148   1148       Phosphoserine.
FT   CARBOHYD     87     87       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    225    225       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    299    299       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    476    476       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    562    562       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    580    580       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    767    767       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    822    822       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    945    945       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1027   1027       N-linked (GlcNAc...) (Potential).
FT   DISULFID     57    109       By similarity.
FT   DISULFID    153    204       By similarity.
FT   DISULFID    262    310       By similarity.
FT   DISULFID    352    401       By similarity.
FT   DISULFID    445    494       By similarity.
FT   DISULFID    536    591       By similarity.
FT   VAR_SEQ     227    227       S -> LKHASDSSSSTEICSQA (in isoform 2).
FT                                /FTId=VSP_020083.
FT   VAR_SEQ    1016   1070       SKGIRKITEGVNVTQKIHPVEVLVPGAEHIVHLMTKNWGDN
FT                                DSIFQDVIETRGRE -> K (in isoform 2).
FT                                /FTId=VSP_020084.
FT   VAR_SEQ    1138   1209       SDSDEKPLKGSLRSLNRNMQPTESADSLVEYGEGDQSIFNE
FT                                DGSFIGAYTGAKEKGSVESNGSSTATFPLRA -> RKMVLK
FT                                QKLLSWSSSRGRTFYSCTKNTLFDGSSVDMKTLQPLRYFSS
FT                                NKHT (in isoform 2).
FT                                /FTId=VSP_020085.
FT   MUTAGEN     555    558       DGEA->AGEV: Inhibition of migration
FT                                potentiation.
FT   MUTAGEN    1186   1186       Y->A: Inhibition of migration
FT                                potentiation.
FT   CONFLICT     50     50       D -> G (in Ref. 2; BAC35247).
FT   CONFLICT     77     77       D -> E (in Ref. 3; CAC88131).
FT   CONFLICT    425    425       I -> V (in Ref. 2; BAC35247).
FT   CONFLICT    602    602       K -> E (in Ref. 2; BAC30699).
FT   CONFLICT    612    612       G -> P (in Ref. 2; BAC30699).
SQ   SEQUENCE   1209 AA;  134929 MW;  331F5849AE776226 CRC64;
     MMELPLCGRG LILSLIFLLL KLSAAEIPLS VQQVPTIVKQ SYVQVAFPFD EYFQIECEAK
     GNPEPIFSWT KDDKPFDLSD PRIIAANNSG TFKIPNEGHI SHFQGKYRCF ASNRLGTAVS
     EEIEFIVPGV PKFPKEKIEP IDVEEGDSIV LPCNPPKGLP PLHIYWMNIE LEHIEQDERV
     YMSQRGDLYF ANVEENDSRN DYCCFAAFPK LRTIVQKMPM KLTVNSSNSI KQRKPKLLLP
     PAQMGSLSAK TVLKGDTLLL ECFAEGLPTP HIQWSKPGSE LPEGRATIEV HEKTLKIENI
     SYQDRGNYRC TANNLLGKAS HDFHVTVEEP PRWKKKPQSA VYSTGSSGIL LCEAEGEPQP
     TIKWRLNGLP IEKHPFPGDF MFPREISFTN LLPNHTGVYQ CEASNIHGTI LANANIDVID
     VIPLIKTKNE ENYATVVGYS AFLHCEYFAS PKATVVWEVA DETHPLEGDR YHTHENGTLE
     IYRTTEEDAG SYSCWVDNAM GKAVITANLD IRNATKLRVS PKNPRIPKSH VLELYCESQC
     DSHLKHSLKL SWSKDGEAFE MNGTEDGRIV IDGAYLTISN ITAEDQGVYS CSAQTSLDST
     SKKTQVTVLG VGDPPETFTC QKDKNRSVRL LREAGDDHNS KSASTIVEFE GNREEPGKWE
     ELTRVQGEET DVVLSLAPYV RYQFRVTAVN EVGRSHASLP SDHHETPPAA PDKNPQNIRV
     QASQPKEMII KWEPLKSMEQ NGPGLEYKVS WKPQGAPEEW EEEIVTNHTL RVMTPTVYAP
     YDVKVQAINQ LGSSPDPQPV TLYSGEDYPS TAPVIQRVDV MNSTLVKVTW SSIPKETVHG
     LLRGYQINWW KTKSLLDGRT HPKEVNILRF SGQRNSGMVP SLDPFSEFHL TVLAYNSKGA
     GPESEPYIFQ TPEGVPEQPS FLKVIKVDKD TATLSWGLPK KLNGNLTGYL LQYQIINDTY
     ELGELNEINV TTPSKSSWHL SNLNSTTKYK FYLRACTSRG CGKPISEEGA TLGEGSKGIR
     KITEGVNVTQ KIHPVEVLVP GAEHIVHLMT KNWGDNDSIF QDVIETRGRE YAGLYDDIST
     QGWFIGLMCA IALLTLILLT ICFVKRNRGG KYSVKEKEDL HPDPEVQSAK DETFGEYSDS
     DEKPLKGSLR SLNRNMQPTE SADSLVEYGE GDQSIFNEDG SFIGAYTGAK EKGSVESNGS
     STATFPLRA
//
ID   NFIC_MOUSE              Reviewed;         439 AA.
AC   P70255; O09072; P70256; Q3U2I9; Q99MA3; Q99MA4; Q99MA5; Q99MA6;
AC   Q99MA7; Q99MA8; Q9R1G3;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAR-2011, entry version 105.
DE   RecName: Full=Nuclear factor 1 C-type;
DE            Short=NF1-C;
DE            Short=Nuclear factor 1/C;
DE   AltName: Full=CCAAT-box-binding transcription factor;
DE            Short=CTF;
DE   AltName: Full=Nuclear factor I/C;
DE            Short=NF-I/C;
DE            Short=NFI-C;
DE   AltName: Full=TGGCA-binding protein;
GN   Name=Nfic;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=NIH Swiss;
RX   MEDLINE=22456605; PubMed=12568726; DOI=10.1016/S0378-1119(02)01204-0;
RA   Gruender A., Qian F., Ebel T.T., Mincheva A., Lichter P., Kruse U.,
RA   Sippel A.E.;
RT   "Genomic organization, splice products and mouse chromosomal
RT   localization of genes for transcription factor Nuclear Factor One.";
RL   Gene 304:171-181(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Liver, and Skeletal muscle;
RX   MEDLINE=97209336; PubMed=9056636;
RX   DOI=10.1002/(SICI)1097-0177(199703)208:3<313::AID-AJA3>3.3.CO;2-2;
RA   Chaudhry A.Z., Lyons G.E., Gronostajski R.M.;
RT   "Expression patterns of the four nuclear factor I genes during mouse
RT   embryogenesis indicate a potential role in development.";
RL   Dev. Dyn. 208:313-325(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE OF 179-439 (ISOFORMS 1; 3; 4; 5; 6 AND 7).
RC   STRAIN=CD-1; TISSUE=Mammary gland;
RA   Kane R., Martin F.;
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE OF 11-187.
RC   STRAIN=129;
RX   MEDLINE=99189145; PubMed=10087299; DOI=10.1007/s003359901008;
RA   Fletcher C.F., Jenkins N.A., Copeland N.G., Chaudhry A.Z.,
RA   Gronostajski R.M.;
RT   "Exon structure of the nuclear factor I DNA-binding domain from C.
RT   elegans to mammals.";
RL   Mamm. Genome 10:390-396(1999).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-337; SER-339;
RP   SER-343 AND THR-378, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Recognizes and binds the palindromic sequence 5'-
CC       TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in
CC       the origin of replication of adenovirus type 2. These proteins are
CC       individually capable of activating transcription and replication.
CC   -!- SUBUNIT: Binds DNA as a homodimer.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=1; Synonyms=C1A, C2;
CC         IsoId=P70255-1; Sequence=Displayed;
CC       Name=2; Synonyms=C1B;
CC         IsoId=P70255-2; Sequence=VSP_003557;
CC       Name=3; Synonyms=C5;
CC         IsoId=P70255-3; Sequence=VSP_007559;
CC       Name=4; Synonyms=C8;
CC         IsoId=P70255-4; Sequence=VSP_007557;
CC       Name=5; Synonyms=C9;
CC         IsoId=P70255-5; Sequence=VSP_007558;
CC       Name=6; Synonyms=C10;
CC         IsoId=P70255-6; Sequence=VSP_007556;
CC       Name=7; Synonyms=C11;
CC         IsoId=P70255-7; Sequence=VSP_007556, VSP_007559;
CC   -!- TISSUE SPECIFICITY: Highest levels in skeletal muscle. Lower
CC       levels in heart, liver, kidney, lung and brain. Very low levels in
CC       testis and spleen.
CC   -!- SIMILARITY: Belongs to the CTF/NF-I family.
CC   -!- SIMILARITY: Contains 1 CTF/NF-I DNA-binding domain.
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DR   EMBL; Y07692; CAA68956.1; -; mRNA.
DR   EMBL; Y07693; CAA68957.1; -; mRNA.
DR   EMBL; U57635; AAB49930.1; -; mRNA.
DR   EMBL; AK087539; BAC39918.1; -; mRNA.
DR   EMBL; AK155258; BAE33151.1; -; mRNA.
DR   EMBL; AF358455; AAK21331.1; -; mRNA.
DR   EMBL; AF358456; AAK21332.1; -; mRNA.
DR   EMBL; AF358457; AAK21333.1; -; mRNA.
DR   EMBL; AF358458; AAK21334.1; -; mRNA.
DR   EMBL; AF358459; AAK21335.1; -; mRNA.
DR   EMBL; AF358460; AAK21336.1; -; mRNA.
DR   EMBL; AF111265; AAD39100.1; -; Genomic_DNA.
DR   IPI; IPI00137501; -.
DR   IPI; IPI00229362; -.
DR   IPI; IPI00331482; -.
DR   IPI; IPI00331483; -.
DR   IPI; IPI00331484; -.
DR   IPI; IPI00331485; -.
DR   IPI; IPI00331486; -.
DR   RefSeq; NP_032714.1; NM_008688.3.
DR   UniGene; Mm.426936; -.
DR   UniGene; Mm.453078; -.
DR   STRING; P70255; -.
DR   PhosphoSite; P70255; -.
DR   PRIDE; P70255; -.
DR   Ensembl; ENSMUST00000020461; ENSMUSP00000020461; ENSMUSG00000055053.
DR   Ensembl; ENSMUST00000078185; ENSMUSP00000077317; ENSMUSG00000055053.
DR   Ensembl; ENSMUST00000105319; ENSMUSP00000100956; ENSMUSG00000055053.
DR   Ensembl; ENSMUST00000105320; ENSMUSP00000100957; ENSMUSG00000055053.
DR   Ensembl; ENSMUST00000105321; ENSMUSP00000100958; ENSMUSG00000055053.
DR   GeneID; 18029; -.
DR   KEGG; mmu:18029; -.
DR   UCSC; uc007ghx.1; mouse.
DR   UCSC; uc007ghy.1; mouse.
DR   UCSC; uc007gia.1; mouse.
DR   CTD; 18029; -.
DR   MGI; MGI:109591; Nfic.
DR   eggNOG; maNOG17793; -.
DR   GeneTree; ENSGT00390000009905; -.
DR   HOVERGEN; HBG006561; -.
DR   InParanoid; P70255; -.
DR   OMA; LKMPSHC; -.
DR   OrthoDB; EOG47SSDN; -.
DR   NextBio; 293103; -.
DR   ArrayExpress; P70255; -.
DR   Bgee; P70255; -.
DR   CleanEx; MM_NFIC; -.
DR   Genevestigator; P70255; -.
DR   GermOnline; ENSMUSG00000055053; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016563; F:transcription activator activity; IDA:MGI.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0010553; P:negative regulation of gene-specific transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0042475; P:odontogenesis of dentine-containing tooth; IMP:MGI.
DR   GO; GO:0010552; P:positive regulation of gene-specific transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   InterPro; IPR000647; CTF/NFI.
DR   InterPro; IPR020604; CTF/NFI_DNA-bd-dom.
DR   InterPro; IPR019739; CTF/NFI_DNA-bd_CS.
DR   InterPro; IPR019548; CTF/NFI_DNA-bd_N.
DR   InterPro; IPR003619; MAD_homology1_Dwarfin-type.
DR   PANTHER; PTHR11492; CTF_NFI; 1.
DR   Pfam; PF00859; CTF_NFI; 1.
DR   Pfam; PF03165; MH1; 1.
DR   Pfam; PF10524; NfI_DNAbd_pre-N; 1.
DR   SMART; SM00523; DWA; 1.
DR   PROSITE; PS00349; CTF_NFI_1; 1.
DR   PROSITE; PS51080; CTF_NFI_2; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; DNA replication; DNA-binding;
KW   Nucleus; Phosphoprotein; Transcription; Transcription regulation.
FT   CHAIN         1    439       Nuclear factor 1 C-type.
FT                                /FTId=PRO_0000100200.
FT   DNA_BIND      1    195       CTF/NF-I.
FT   MOD_RES       4      4       Phosphoserine (By similarity).
FT   MOD_RES     194    194       Phosphoserine (By similarity).
FT   MOD_RES     294    294       Phosphoserine (By similarity).
FT   MOD_RES     305    305       Phosphoserine (By similarity).
FT   MOD_RES     323    323       Phosphoserine (By similarity).
FT   MOD_RES     333    333       Phosphoserine.
FT   MOD_RES     337    337       Phosphoserine.
FT   MOD_RES     339    339       Phosphoserine.
FT   MOD_RES     343    343       Phosphoserine.
FT   MOD_RES     378    378       Phosphothreonine.
FT   VAR_SEQ       1     10       MYSSPLCLTQ -> M (in isoform 2).
FT                                /FTId=VSP_003557.
FT   VAR_SEQ     247    374       Missing (in isoform 6 and isoform 7).
FT                                /FTId=VSP_007556.
FT   VAR_SEQ     320    361       Missing (in isoform 4).
FT                                /FTId=VSP_007557.
FT   VAR_SEQ     362    423       Missing (in isoform 5).
FT                                /FTId=VSP_007558.
FT   VAR_SEQ     424    439       PALRPTRPLQTVPLWD -> SWYLG (in isoform 3
FT                                and isoform 7).
FT                                /FTId=VSP_007559.
SQ   SEQUENCE   439 AA;  48768 MW;  F794131A7A1B686A CRC64;
     MYSSPLCLTQ DEFHPFIEAL LPHVRAFAYT WFNLQARKRK YFKKHEKRMS KDEERAVKDE
     LLGEKAEVKQ KWASRLLAKL RKDIRPECRE DFVLAVTGKK APGCVLSNPD QKGKMRRIDC
     LRQADKVWRL DLVMVILFKG IPLESTDGER LVKAAACAHP VLCVQPHHIG VAVKELDLYL
     AYFVRERDAE QSSSPRTGVG SDQEDSKPIT LDTTDFQESF VTSGVFSVTE LIQVSRTPVV
     TGTGPNFSLG ELQGHLAYDL NPASAGMRRT LPSTSSSGSK RHKSGSMEED VDTSPGGDYY
     TSPNSPTSSS RNWTEDIEGG ISSPVKKTEM DKSPFNSPSP QDSPRLSSFT QHHRPVIAVH
     SGIARSPHPT SALHFPATPI LPQTASTYFP HTAIRYPPHL NPQDPLKDLV SLACDPATQQ
     PGPPALRPTR PLQTVPLWD
//
ID   NFIX_MOUSE              Reviewed;         488 AA.
AC   P70257; O08519; P70258; Q64192; Q99L78; Q9R1G2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2003, sequence version 2.
DT   08-FEB-2011, entry version 97.
DE   RecName: Full=Nuclear factor 1 X-type;
DE            Short=NF1-X;
DE            Short=Nuclear factor 1/X;
DE   AltName: Full=CCAAT-box-binding transcription factor;
DE            Short=CTF;
DE   AltName: Full=Nuclear factor I/X;
DE            Short=NF-I/X;
DE            Short=NFI-X;
DE   AltName: Full=TGGCA-binding protein;
GN   Name=Nfix;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS NFIX1; NFIX2 AND NFIX3), AND
RP   FUNCTION.
RX   MEDLINE=96089378; PubMed=8581067;
RA   Nebl G., Cato A.C.B.;
RT   "NFI/X proteins: a class of NFI family of transcription factors with
RT   positive and negative regulatory domains.";
RL   Cell. Mol. Biol. Res. 41:85-95(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS NFIX1 AND NFIX2).
RC   STRAIN=NIH Swiss;
RX   MEDLINE=22456605; PubMed=12568726; DOI=10.1016/S0378-1119(02)01204-0;
RA   Gruender A., Qian F., Ebel T.T., Mincheva A., Lichter P., Kruse U.,
RA   Sippel A.E.;
RT   "Genomic organization, splice products and mouse chromosomal
RT   localization of genes for transcription factor Nuclear Factor One.";
RL   Gene 304:171-181(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM NFIX1).
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4-488 (ISOFORM NFIX2).
RC   STRAIN=BALB/c;
RX   MEDLINE=97209336; PubMed=9056636;
RX   DOI=10.1002/(SICI)1097-0177(199703)208:3<313::AID-AJA3>3.3.CO;2-2;
RA   Chaudhry A.Z., Lyons G.E., Gronostajski R.M.;
RT   "Expression patterns of the four nuclear factor I genes during mouse
RT   embryogenesis indicate a potential role in development.";
RL   Dev. Dyn. 208:313-325(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-186.
RC   STRAIN=129;
RX   MEDLINE=99189145; PubMed=10087299; DOI=10.1007/s003359901008;
RA   Fletcher C.F., Jenkins N.A., Copeland N.G., Chaudhry A.Z.,
RA   Gronostajski R.M.;
RT   "Exon structure of the nuclear factor I DNA-binding domain from C.
RT   elegans to mammals.";
RL   Mamm. Genome 10:390-396(1999).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284 AND SER-288, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Recognizes and binds the palindromic sequence 5'-
CC       TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in
CC       the origin of replication of adenovirus type 2. These proteins are
CC       individually capable of activating transcription and replication.
CC       Isoform NFIX1 acts as a transcriptional activator while isoform
CC       NFIX3 acts as a repressor.
CC   -!- SUBUNIT: Binds DNA as a homodimer.
CC   -!- INTERACTION:
CC       Q02078:MEF2A (xeno); NbExp=1; IntAct=EBI-2639047, EBI-2656305;
CC       Q60929:Mef2a; NbExp=1; IntAct=EBI-2639047, EBI-2639094;
CC       Q02111:Prkcq; NbExp=1; IntAct=EBI-2639047, EBI-2639157;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=NFIX3;
CC         IsoId=P70257-3; Sequence=Displayed;
CC       Name=NFIX1;
CC         IsoId=P70257-1; Sequence=VSP_007546, VSP_007547;
CC       Name=NFIX2;
CC         IsoId=P70257-2; Sequence=VSP_003563, VSP_007546, VSP_007547;
CC   -!- SIMILARITY: Belongs to the CTF/NF-I family.
CC   -!- SIMILARITY: Contains 1 CTF/NF-I DNA-binding domain.
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DR   EMBL; S81451; AAB36083.2; -; mRNA.
DR   EMBL; Y07688; CAA68952.1; -; mRNA.
DR   EMBL; Y07689; CAA68953.1; -; mRNA.
DR   EMBL; BC003766; AAH03766.1; -; mRNA.
DR   EMBL; U57636; AAB49931.1; -; mRNA.
DR   EMBL; AF111266; AAD39101.1; -; Genomic_DNA.
DR   IPI; IPI00137503; -.
DR   IPI; IPI00319666; -.
DR   IPI; IPI00762534; -.
DR   RefSeq; NP_001075451.1; NM_001081982.1.
DR   RefSeq; NP_035036.1; NM_010906.2.
DR   UniGene; Mm.9394; -.
DR   IntAct; P70257; 20.
DR   STRING; P70257; -.
DR   PhosphoSite; P70257; -.
DR   PRIDE; P70257; -.
DR   Ensembl; ENSMUST00000076715; ENSMUSP00000076005; ENSMUSG00000001911.
DR   Ensembl; ENSMUST00000098572; ENSMUSP00000096171; ENSMUSG00000001911.
DR   Ensembl; ENSMUST00000099070; ENSMUSP00000096669; ENSMUSG00000001911.
DR   GeneID; 18032; -.
DR   KEGG; mmu:18032; -.
DR   UCSC; uc009mne.1; mouse.
DR   UCSC; uc009mnf.1; mouse.
DR   CTD; 18032; -.
DR   MGI; MGI:97311; Nfix.
DR   eggNOG; roNOG14089; -.
DR   GeneTree; ENSGT00390000009905; -.
DR   HOVERGEN; HBG006561; -.
DR   ArrayExpress; P70257; -.
DR   Bgee; P70257; -.
DR   CleanEx; MM_NFIX; -.
DR   Genevestigator; P70257; -.
DR   GermOnline; ENSMUSG00000001911; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0016563; F:transcription activator activity; IDA:MGI.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0010553; P:negative regulation of gene-specific transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   InterPro; IPR000647; CTF/NFI.
DR   InterPro; IPR020604; CTF/NFI_DNA-bd-dom.
DR   InterPro; IPR019739; CTF/NFI_DNA-bd_CS.
DR   InterPro; IPR019548; CTF/NFI_DNA-bd_N.
DR   InterPro; IPR003619; MAD_homology1_Dwarfin-type.
DR   PANTHER; PTHR11492; CTF_NFI; 1.
DR   Pfam; PF00859; CTF_NFI; 1.
DR   Pfam; PF03165; MH1; 1.
DR   Pfam; PF10524; NfI_DNAbd_pre-N; 1.
DR   SMART; SM00523; DWA; 1.
DR   PROSITE; PS00349; CTF_NFI_1; 1.
DR   PROSITE; PS51080; CTF_NFI_2; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; DNA replication; DNA-binding;
KW   Nucleus; Phosphoprotein; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    488       Nuclear factor 1 X-type.
FT                                /FTId=PRO_0000100205.
FT   DNA_BIND      1    194       CTF/NF-I.
FT   MOD_RES     280    280       Phosphoserine (By similarity).
FT   MOD_RES     284    284       Phosphoserine.
FT   MOD_RES     288    288       Phosphoserine.
FT   VAR_SEQ     320    360       Missing (in isoform NFIX2).
FT                                /FTId=VSP_003563.
FT   VAR_SEQ     419    441       PNGSGQGKVPGSFLLPPPPPVAR -> HSQRQAPPLPTGLS
FT                                ASDPGTATF (in isoform NFIX1 and isoform
FT                                NFIX2).
FT                                /FTId=VSP_007546.
FT   VAR_SEQ     442    488       Missing (in isoform NFIX1 and isoform
FT                                NFIX2).
FT                                /FTId=VSP_007547.
FT   CONFLICT    353    353       V -> L (in Ref. 2; CAA68952).
SQ   SEQUENCE   488 AA;  53394 MW;  157F67EC17C96AD0 CRC64;
     MYSPYCLTQD EFHPFIEALL PHVRAFSYTW FNLQARKRKY FKKHEKRMSK DEERAVKDEL
     LGEKPEIKQK WASRLLAKLR KDIRPEFRED FVLTITGKKP PCCVLSNPDQ KGKIRRIDCL
     RQADKVWRLD LVMVILFKGI PLESTDGERL YKSPQCSNPG LCVQPHHIGV TIKELDLYLA
     YFVHTPESGQ SDSSNQQGDA DIKPLPNGHL SFQDCFVTSG VWNVTELVRV SQTPVATASG
     PNFSLADLES PSYYNINQVT LGRRSITSPP STSSTKRPKS IDDSEMESPV DDVFYPGTGR
     SPAAGSSQSS GWPNDVDAGP ASLKKSGKLD FCSALSSQGS SPRMAFTHHP LPVLAGVRPG
     SPRATASALH FPSTSIIQQS SPYFTHPTIR YHHHHGQDSL KEFVQFVCSD GSGQATGQPN
     GSGQGKVPGS FLLPPPPPVA RPVPLPMPDS KTTSTAPDGA ALTPPSPSFT TTGASSANRF
     VGIGPRDG
//
ID   PKN1_MOUSE              Reviewed;         946 AA.
AC   P70268; Q3UEA6; Q7TST2; Q8BTL8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 3.
DT   08-MAR-2011, entry version 108.
DE   RecName: Full=Serine/threonine-protein kinase N1;
DE            EC=2.7.11.13;
DE   AltName: Full=Protein kinase C-like 1;
DE   AltName: Full=Protein kinase C-like PKN;
DE   AltName: Full=Protein-kinase C-related kinase 1;
DE   AltName: Full=Serine-threonine protein kinase N;
GN   Name=Pkn1; Synonyms=Pkn, Prk1, Prkcl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 664-946.
RC   STRAIN=129;
RX   MEDLINE=97011095; PubMed=8858105; DOI=10.1006/bbrc.1996.1469;
RA   Batshake B., Sundelin S.;
RT   "The mouse genes for the EP1 prostanoid receptor and the PKN protein
RT   kinase overlap.";
RL   Biochem. Biophys. Res. Commun. 227:70-76(1996).
RN   [4]
RP   ENZYME REGULATION, AND INTERACTION WITH RHOA.
RX   PubMed=8571127; DOI=10.1126/science.271.5249.648;
RA   Amano M., Mukai H., Ono Y., Chihara K., Matsui T., Hamajima Y.,
RA   Okawa K., Iwamatsu A., Kaibuchi K.;
RT   "Identification of a putative target for Rho as the serine-threonine
RT   kinase protein kinase N.";
RL   Science 271:648-650(1996).
RN   [5]
RP   INTERACTION WITH ZA20D3.
RC   TISSUE=Liver, Mammary gland, and Uterus;
RX   MEDLINE=20509997; PubMed=11054541; DOI=10.1016/S0378-1119(00)00365-6;
RA   Duan W., Sun B., Li T.W., Tan B.J., Lee M.K., Teo T.S.;
RT   "Cloning and characterization of AWP1, a novel protein that associates
RT   with serine/threonine kinase PRK1 in vivo.";
RL   Gene 256:113-121(2000).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-920, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-920, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: PKC-related serine/threonine-protein kinase involved in
CC       various processes such as regulation of the intermediate filaments
CC       of the actin cytoskeleton and transcription regulation. Regulates
CC       the cytoskeletal network by phosphorylating proteins such as VIM
CC       and neurofilament proteins NEFH, NEFL and NEFM, leading to inhibit
CC       their polymerization. Phosphorylates 'Ser-575', 'Ser-637' and
CC       'Ser-669' of MAPT/Tau, lowering its ability to bind to
CC       microtubules, resulting in disruption of tubulin assembly. Acts as
CC       a key coactivator of androgen receptor (ANDR)-dependent
CC       transcription, by being recruited to ANDR target genes and
CC       specifically mediating phosphorylation of 'Thr-11' of histone H3
CC       (H3T11ph), a specific tag for epigenetic transcriptional
CC       activation that promotes demethylation of histone H3 'Lys-9'
CC       (H3K9me) by KDM4C/JMJD2C. Phosphorylates HDAC5, HDAC7 and HDAC9,
CC       leading to impair their import in the nucleus. Phosphorylates
CC       'Thr-38' of PPP1R14A, 'Ser-159', 'Ser-163' and 'Ser-170', and
CC       GFAP. Able to phosphorylate RPS6 in vitro (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Kinase activity is activated upon binding to
CC       Rho proteins (RHOA, RHOB and RAC1). Activated by lipids,
CC       particularly cardiolipin and to a lesser extent by other acidic
CC       phospholipids. Activated by caspase-3 (CASP3) cleavage during
CC       apoptosis. Two specific sites, Thr-778 (activation loop of the
CC       kinase domain) and Ser-920 (turn motif), need to be phosphorylated
CC       for its full activation.
CC   -!- SUBUNIT: Interacts with ANDR. Interacts with PRKCB. Interacts (via
CC       REM 1 and REM 2 repeats) with RAC1. Interacts with RHOB (By
CC       similarity). Interacts (via REM 1 repeat) with RHOA. Interacts
CC       with ZA20D3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Endosome (By similarity). Cell membrane; Peripheral
CC       membrane protein (By similarity). Note=Associates with chromatin
CC       in a ligand-dependent manner (By similarity). Localization to
CC       endosomes is mediated via its interaction with RHOB (By
CC       similarity). Association to the cell membrane is dependent on Ser-
CC       377 phosphorylation (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P70268-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P70268-2; Sequence=VSP_039223;
CC   -!- DOMAIN: The C1 domain does not bind the diacylglycerol (DAG) (By
CC       similarity).
CC   -!- PTM: Autophosphorylated; preferably on serine (By similarity).
CC   -!- PTM: Activated by limited proteolysis with trypsin (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. PKC subfamily.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 3 REM (Hr1) repeats.
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DR   EMBL; AK089431; BAC40880.2; -; mRNA.
DR   EMBL; AK149649; BAE29005.1; -; mRNA.
DR   EMBL; BC052923; AAH52923.1; -; mRNA.
DR   EMBL; Y07611; CAA68883.1; -; Genomic_DNA.
DR   IPI; IPI00474711; -.
DR   IPI; IPI00762427; -.
DR   PIR; PC4220; PC4220.
DR   RefSeq; NP_001186522.1; NM_001199593.1.
DR   RefSeq; NP_796236.2; NM_177262.4.
DR   UniGene; Mm.213000; -.
DR   ProteinModelPortal; P70268; -.
DR   SMR; P70268; 13-98, 122-202, 211-279, 614-945.
DR   STRING; P70268; -.
DR   PhosphoSite; P70268; -.
DR   PRIDE; P70268; -.
DR   Ensembl; ENSMUST00000005616; ENSMUSP00000005616; ENSMUSG00000057672.
DR   Ensembl; ENSMUST00000109818; ENSMUSP00000105443; ENSMUSG00000057672.
DR   GeneID; 320795; -.
DR   KEGG; mmu:320795; -.
DR   UCSC; uc009mkx.1; mouse.
DR   CTD; 320795; -.
DR   MGI; MGI:108022; Pkn1.
DR   eggNOG; maNOG17213; -.
DR   GeneTree; ENSGT00560000076750; -.
DR   HOVERGEN; HBG108317; -.
DR   OrthoDB; EOG4VDPXV; -.
DR   PhylomeDB; P70268; -.
DR   BRENDA; 2.7.11.13; 244.
DR   NextBio; 397445; -.
DR   PMAP-CutDB; P70268; -.
DR   ArrayExpress; P70268; -.
DR   Bgee; P70268; -.
DR   CleanEx; MM_PKN1; -.
DR   Genevestigator; P70268; -.
DR   GermOnline; ENSMUSG00000057672; Mus musculus.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:MGI.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050681; F:androgen receptor binding; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0017049; F:GTP-Rho binding; ISS:UniProtKB.
DR   GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR   GO; GO:0042826; F:histone deacetylase binding; ISS:UniProtKB.
DR   GO; GO:0035402; F:histone kinase activity (H3-T11 specific); ISS:UniProtKB.
DR   GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; ISS:UniProtKB.
DR   GO; GO:0004697; F:protein kinase C activity; IEA:EC.
DR   GO; GO:0048365; F:Rac GTPase binding; ISS:UniProtKB.
DR   GO; GO:0006972; P:hyperosmotic response; IDA:MGI.
DR   GO; GO:0034339; P:regulation of transcription from RNA polymerase II promoter by nuclear hormone receptor; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR011072; HR1_rho-bd.
DR   InterPro; IPR000861; HR1_rpt_rho-bd.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Gene3D; G3DSA:1.10.287.160; HR1_rho-bd; 3.
DR   Pfam; PF02185; HR1; 3.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00742; Hr1; 3.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF46585; PKN_effector; 3.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50004; C2; FALSE_NEG.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Cell membrane;
KW   Chromatin regulator; Cytoplasm; Endosome; Kinase; Membrane;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Repeat;
KW   Serine/threonine-protein kinase; Transcription;
KW   Transcription regulation; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    946       Serine/threonine-protein kinase N1.
FT                                /FTId=PRO_0000055720.
FT   REPEAT       34    110       REM 1.
FT   REPEAT      123    212       REM 2.
FT   REPEAT      213    294       REM 3.
FT   DOMAIN      328    464       C2.
FT   DOMAIN      619    878       Protein kinase.
FT   DOMAIN      879    946       AGC-kinase C-terminal.
FT   NP_BIND     625    633       ATP (By similarity).
FT   ACT_SITE    744    744       Proton acceptor (By similarity).
FT   BINDING     648    648       ATP (By similarity).
FT   SITE        108    109       Cleavage; by caspase-3 (By similarity).
FT   SITE        457    458       Cleavage; by caspase-3 (By similarity).
FT   SITE        561    562       Cleavage; by caspase-3 (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     356    356       Phosphothreonine (By similarity).
FT   MOD_RES     377    377       Phosphoserine (By similarity).
FT   MOD_RES     379    379       Phosphoserine (By similarity).
FT   MOD_RES     451    451       N6-acetyllysine (By similarity).
FT   MOD_RES     536    536       Phosphoserine (By similarity).
FT   MOD_RES     540    540       Phosphoserine (By similarity).
FT   MOD_RES     562    562       Phosphoserine (By similarity).
FT   MOD_RES     564    564       Phosphoserine (By similarity).
FT   MOD_RES     565    565       Phosphoserine (By similarity).
FT   MOD_RES     778    778       Phosphothreonine (Probable).
FT   MOD_RES     782    782       Phosphothreonine (By similarity).
FT   MOD_RES     918    918       Phosphothreonine (By similarity).
FT   MOD_RES     920    920       Phosphoserine.
FT   VAR_SEQ       1      7       MAGDAVQ -> MAADPPLDSELE (in isoform 2).
FT                                /FTId=VSP_039223.
SQ   SEQUENCE   946 AA;  104411 MW;  FCB4E61AD27C1271 CRC64;
     MAGDAVQSEP RSWSLLEQLG LAGADLAAPG VQQQLELERE RLKREIRKEL KLKEGAENLR
     RATTDLGRSL APVELLLRGS ARRLDLLHQQ LQELHAHVVL PDPAAGSDAT QSLAEGSPIC
     SSTNLSRVAG LEKQLAIELK VKQGAENMIQ TYSNGSSKDR KLLLTAQQML QDSKTKIDII
     RMQLRRALQA LQAGELESQA APDEAQGDPE LGAVELRIEE LRHHFRVEHA VAEGAKNVLR
     LLSGAKAPDR KAVSEAQEKL TESNQKLGLL RESLERRLGE LPADHPKGRL LREELTAASS
     SAFSAILPGP FPATHYSTLS KPAPLTGTLE VRVVGCKNLP ETIPWSPPPS VGASGTPESR
     TPFLSRPARG LYSRSGSLSG RSSLRGEAEN ATEVSTVLKL DNTVVGQTAW KPCGPNAWDQ
     SFTLELERAR ELELAVFWRD QRGLCALKFL KLEDFLDNER HEVQLDMEPQ GCLVAEVTFR
     NPIIERIPRL QRQKKIFSKQ QGKAFQRARQ MNIDVATWVR LLRRLIPSAV ATGTFSPNAS
     PGAEIRHTGD ISMEKLNLGA DSDSSSQKSP PGLPSTSCSL SSPTHESTTS PELPSETQET
     PGPGLCSPLR KSPLTLEDFK FLAVLGRGHF GKVLLSEFRS SGELFAIKAL KKGDIVARDE
     VESLMCEKRI LAAVTRAGHP FLVNLFGCFQ TPEHVCFVME YSAGGDLMLH IHSDVFSEPR
     AVFYSACVVL GLQFLHEHKI VYRDLKLDNL LLDTEGYVKI ADFGLCKEGM GYGDRTSTFC
     GTPEFLAPEV LTDTSYTRAV DWWGLGVLLY EMLVGESPFP GDDEEEVFDS IVNDEVRYPR
     FLSAEAIGIM RRLLRRNPER RLGSTERDAE DVKKQPFFRS LGWDVLLARR LPPPFVPTLS
     GRTDVSNFDE EFTGEAPTLS PPRDARPLTA AEQAAFRDFD FVAGGY
//
ID   PDLI4_MOUSE             Reviewed;         330 AA.
AC   P70271; Q8K0W4;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 2.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=PDZ and LIM domain protein 4;
DE   AltName: Full=LIM protein RIL;
DE   AltName: Full=Reversion-induced LIM protein;
GN   Name=Pdlim4; Synonyms=Ril;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION, AND INTERACTION WITH
RP   PTPN13.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=98155214; PubMed=9487134;
RA   Cuppen E., Gerrits H., Pepers B., Wieringa B., Hendriks W.;
RT   "PDZ motifs in PTP-BL and RIL bind to internal protein segments in the
RT   LIM domain protein RIL.";
RL   Mol. Biol. Cell 9:671-683(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111; SER-118; SER-119
RP   AND SER-124, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111 AND SER-119, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SUBUNIT: Interacts with the LIM domain with the second and fourth
CC       PDZ domains of PTPN13.
CC   -!- PTM: Phosphorylated on tyrosine residue(s). Can be
CC       dephosphorylated by PTPN13.
CC   -!- SIMILARITY: Contains 1 LIM zinc-binding domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; Y08361; CAA69648.1; -; mRNA.
DR   EMBL; BC030068; AAH30068.1; -; mRNA.
DR   IPI; IPI00321557; -.
DR   RefSeq; NP_062290.2; NM_019417.3.
DR   UniGene; Mm.21830; -.
DR   ProteinModelPortal; P70271; -.
DR   SMR; P70271; 1-81, 231-314.
DR   STRING; P70271; -.
DR   PhosphoSite; P70271; -.
DR   PRIDE; P70271; -.
DR   Ensembl; ENSMUST00000018755; ENSMUSP00000018755; ENSMUSG00000020388.
DR   GeneID; 30794; -.
DR   KEGG; mmu:30794; -.
DR   CTD; 30794; -.
DR   MGI; MGI:1353470; Pdlim4.
DR   eggNOG; maNOG16900; -.
DR   HOGENOM; HBG444171; -.
DR   HOVERGEN; HBG061371; -.
DR   InParanoid; P70271; -.
DR   OrthoDB; EOG48KRBW; -.
DR   NextBio; 307210; -.
DR   ArrayExpress; P70271; -.
DR   Bgee; P70271; -.
DR   CleanEx; MM_PDLIM4; -.
DR   Genevestigator; P70271; -.
DR   GermOnline; ENSMUSG00000020388; Mus musculus.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR001781; Znf_LIM.
DR   Gene3D; G3DSA:2.10.110.10; Znf_LIM; 1.
DR   Pfam; PF00412; LIM; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00132; LIM; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   1: Evidence at protein level;
KW   LIM domain; Metal-binding; Phosphoprotein; Zinc.
FT   CHAIN         1    330       PDZ and LIM domain protein 4.
FT                                /FTId=PRO_0000075874.
FT   DOMAIN        1     84       PDZ.
FT   DOMAIN      255    305       LIM zinc-binding.
FT   MOD_RES     111    111       Phosphoserine.
FT   MOD_RES     118    118       Phosphoserine.
FT   MOD_RES     119    119       Phosphoserine.
FT   MOD_RES     124    124       Phosphoserine.
FT   MOD_RES     316    316       Phosphotyrosine (By similarity).
FT   CONFLICT     25     25       A -> L (in Ref. 1; CAA69648).
FT   CONFLICT     91     91       S -> A (in Ref. 2; AAH30068).
FT   CONFLICT    107    107       S -> F (in Ref. 1; CAA69648).
SQ   SEQUENCE   330 AA;  35572 MW;  54CBDEA61BFC086B CRC64;
     MTHSVTLRGP SPWGFRLVGG RDFSAPLTIS RVHAGSKAAL AALCPGDLIQ AINGESTELM
     THLEAQNRIK GCHDHLTLSV SRPENKNWPS SPDDKAQAHR IHIDPESQDC SPATSRRSSV
     SGISLEDNRS GLGSPYGQPP RLPVPHNGSS NEATLPAQMS ALHVSPPTSA DTARVLPRNR
     DCRVDLGSEV YRMLREPAEP TASEPKQSGS FRYLQGMLEA GEGGDRPGSG GPRNLKPAAS
     KLGAPLSGLQ GLPECTRCGH GIVGTIVKAR DKLYHPECFM CSDCGLNLKQ RGYFFLDERL
     YCENHAKARV KPPEGYDVVA VYPNAKVELV
//
ID   HDAC2_MOUSE             Reviewed;         488 AA.
AC   P70288; B2RRP3;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAR-2011, entry version 107.
DE   RecName: Full=Histone deacetylase 2;
DE            Short=HD2;
DE            EC=3.5.1.98;
DE   AltName: Full=YY1 transcription factor-binding protein;
GN   Name=Hdac2; Synonyms=Yy1bp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lymphoma;
RX   MEDLINE=97075080; PubMed=8917507; DOI=10.1073/pnas.93.23.12845;
RA   Yang W.-M., Inouye C.J., Zeng Y., Bearss D., Seto E.;
RT   "Transcriptional repression by YY1 is mediated by interaction with a
RT   mammalian homolog of the yeast global regulator RPD3.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:12845-12850(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH SAP30.
RX   MEDLINE=98367545; PubMed=9702189; DOI=10.1016/S1097-2765(00)80111-2;
RA   Laherty C.D., Billin A.N., Lavinsky R.M., Yochum G.S., Bush A.C.,
RA   Sun J.-M., Mullen T.-M., Davie J.R., Rose D.W., Glass C.K.,
RA   Rosenfeld M.G., Ayer D.E., Eisenman R.N.;
RT   "SAP30, a component of the mSin3 corepressor complex involved in N-
RT   CoR-mediated repression by specific transcription factors.";
RL   Mol. Cell 2:33-42(1998).
RN   [5]
RP   INTERACTION WITH HDAC7.
RX   MEDLINE=20442375; PubMed=10984530; DOI=10.1073/pnas.97.19.10330;
RA   Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M.;
RT   "Identification of a nuclear domain with deacetylase activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000).
RN   [6]
RP   INTERACTION WITH CBFA2T3.
RX   PubMed=11533236; DOI=10.1128/MCB.21.19.6470-6483.2001;
RA   Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N.,
RA   Downing J.R., Meyers S., Hiebert S.W.;
RT   "ETO, a target of t(8;21) in acute leukemia, makes distinct contacts
RT   with multiple histone deacetylases and binds mSin3A through its
RT   oligomerization domain.";
RL   Mol. Cell. Biol. 21:6470-6483(2001).
RN   [7]
RP   INTERACTION WITH SUV39H1.
RX   MEDLINE=21648906; PubMed=11788710; DOI=10.1093/nar/30.2.475;
RA   Vaute O., Nicolas E., Vandel L., Trouche D.;
RT   "Functional and physical interaction between the histone methyl
RT   transferase Suv39H1 and histone deacetylases.";
RL   Nucleic Acids Res. 30:475-481(2002).
RN   [8]
RP   INTERACTION WITH SETDB1.
RX   PubMed=12398767; DOI=10.1042/BJ20020854;
RA   Yang L., Mei Q., Zielinska-Kwiatkowska A., Matsui Y., Blackburn M.L.,
RA   Benedetti D., Krumm A.A., Taborsky G.J. Jr., Chansky H.A.;
RT   "An ERG (ets-related gene)-associated histone methyltransferase
RT   interacts with histone deacetylases 1/2 and transcription co-
RT   repressors mSin3A/B.";
RL   Biochem. J. 369:651-657(2003).
RN   [9]
RP   INTERACTION WITH H2AFY.
RX   PubMed=16107708; DOI=10.1128/MCB.25.17.7616-7624.2005;
RA   Chakravarthy S., Gundimella S.K., Caron C., Perche P.-Y.,
RA   Pehrson J.R., Khochbin S., Luger K.;
RT   "Structural characterization of the histone variant macroH2A.";
RL   Mol. Cell. Biol. 25:7616-7624(2005).
RN   [10]
RP   INTERACTION WITH PRDM6.
RX   PubMed=16537907; DOI=10.1128/MCB.26.7.2626-2636.2006;
RA   Davis C.A., Haberland M., Arnold M.A., Sutherland L.B., McDonald O.G.,
RA   Richardson J.A., Childs G., Harris S., Owens G.K., Olson E.N.;
RT   "PRISM/PRDM6, a transcriptional repressor that promotes the
RT   proliferative gene program in smooth muscle cells.";
RL   Mol. Cell. Biol. 26:2626-2636(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND
RP   SER-424, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [12]
RP   S-NITROSYLATION AT CYS-262 AND CYS-274, AND MUTAGENESIS OF CYS-152;
RP   CYS-262 AND CYS-274.
RX   PubMed=18754010; DOI=10.1038/nature07238;
RA   Nott A., Watson P.M., Robinson J.D., Crepaldi L., Riccio A.;
RT   "S-Nitrosylation of histone deacetylase 2 induces chromatin
RT   remodelling in neurons.";
RL   Nature 455:411-415(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 AND
RP   SER-424, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [15]
RP   S-NITROSYLATION BY GAPDH.
RX   PubMed=20972425; DOI=10.1038/ncb2114;
RA   Kornberg M.D., Sen N., Hara M.R., Juluri K.R., Nguyen J.V.,
RA   Snowman A.M., Law L., Hester L.D., Snyder S.H.;
RT   "GAPDH mediates nitrosylation of nuclear proteins.";
RL   Nat. Cell Biol. 12:1094-1100(2010).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on
CC       the N-terminal part of the core histones (H2A, H2B, H3 and H4).
CC       Histone deacetylation gives a tag for epigenetic repression and
CC       plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events. Histone deacetylases act via
CC       the formation of large multiprotein complexes (By similarity).
CC   -!- FUNCTION: Forms transcriptional repressor complexes by associating
CC       with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of
CC       DNA-replication with DNMT1 in the other transcriptional repressor
CC       complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3
CC       and regulates its transcriptional repressor activity.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC   -!- SUBUNIT: Part of the core histone deacetylase (HDAC) complex
CC       composed of HDAC1, HDAC2, RBBP4 and RBBP7. The core complex
CC       associates with MTA2, MBD3, MTA1L1, CHD3 and CHD4 to form the
CC       nucleosome remodeling and histone deacetylation (NuRD) complex, or
CC       with SIN3, SAP18 and SAP30 to form the SIN3 HDAC complex.
CC       Component of a BHC histone deacetylase complex that contains
CC       HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST and PHF21A/BHC80.
CC       The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and
CC       GTF2I. Part of a complex containing the core histones H2A, H2B, H3
CC       and H4, DEK and unphosphorylated DAXX. Part of a complex
CC       containing ATR and CHD4. Forms a heterologous complex at least
CC       with YY1. Interacts with ATR, DNMT1, MINT, HDAC7, HDAC10, HCFC1,
CC       NRIP1, MJD2A/JHDM3A, PRDM6, SAP30, SETDB1 and SUV39H1. Interacts
CC       with the non-histone region of H2AFY. Interacts with PELP1.
CC       Component of a mSin3A corepressor complex that contains SIN3A,
CC       SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2 (By
CC       similarity). Interacts with CBFA2T3. Interacts with CHFR and
CC       SAP30L. Interacts (CK2 phosphorylated form) with SP3. Interacts
CC       with TSHZ3 (via N-terminus); the interaction is direct. Interacts
CC       with APEX1; the interaction is not dependent on the acetylated
CC       status of APEX1 (By similarity).
CC   -!- INTERACTION:
CC       O88574:Sap30; NbExp=1; IntAct=EBI-302251, EBI-593511;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- PTM: S-nitrosylated by GAPDH. In neurons, S-Nitrosylation at Cys-
CC       262 and Cys-274 does not affect the enzyme activity but abolishes
CC       chromatin-binding, leading to increases acetylation of histones
CC       and activate genes that are associated with neuronal development.
CC       In embryonic cortical neurons, S-Nitrosylation regulates dendritic
CC       growth and branching.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; U31758; AAC52889.1; -; mRNA.
DR   EMBL; CH466540; EDL04897.1; -; Genomic_DNA.
DR   EMBL; BC138517; AAI38518.1; -; mRNA.
DR   IPI; IPI00137668; -.
DR   RefSeq; NP_032255.2; NM_008229.2.
DR   UniGene; Mm.19806; -.
DR   ProteinModelPortal; P70288; -.
DR   SMR; P70288; 9-374.
DR   DIP; DIP-32854N; -.
DR   IntAct; P70288; 14.
DR   MINT; MINT-146936; -.
DR   STRING; P70288; -.
DR   PhosphoSite; P70288; -.
DR   PRIDE; P70288; -.
DR   Ensembl; ENSMUST00000019911; ENSMUSP00000019911; ENSMUSG00000019777.
DR   GeneID; 15182; -.
DR   KEGG; mmu:15182; -.
DR   UCSC; uc007evf.1; mouse.
DR   CTD; 15182; -.
DR   MGI; MGI:1097691; Hdac2.
DR   eggNOG; roNOG06682; -.
DR   HOGENOM; HBG396919; -.
DR   HOVERGEN; HBG057112; -.
DR   InParanoid; P70288; -.
DR   OrthoDB; EOG4868CH; -.
DR   PhylomeDB; P70288; -.
DR   ArrayExpress; P70288; -.
DR   Bgee; P70288; -.
DR   CleanEx; MM_HDAC2; -.
DR   Genevestigator; P70288; -.
DR   GermOnline; ENSMUSG00000019777; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR   GO; GO:0035098; C:ESC/E(Z) complex; ISS:UniProtKB.
DR   GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR   GO; GO:0005657; C:replication fork; IDA:MGI.
DR   GO; GO:0005667; C:transcription factor complex; IPI:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0004407; F:histone deacetylase activity; IDA:UniProtKB.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0008134; F:transcription factor binding; TAS:UniProtKB.
DR   GO; GO:0016358; P:dendrite development; IMP:UniProtKB.
DR   GO; GO:0021766; P:hippocampus development; IGI:MGI.
DR   GO; GO:0016575; P:histone deacetylation; IGI:MGI.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; IDA:BHF-UCL.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR003084; His_deacetylse_1.
DR   Gene3D; G3DSA:3.40.800.20; His_deacetylse; 1.
DR   PANTHER; PTHR10625; His_deacetylse; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   PRINTS; PR01271; HISDACETLASE.
PE   1: Evidence at protein level;
KW   Acetylation; Chromatin regulator; Hydrolase; Nucleus; Phosphoprotein;
KW   Repressor; S-nitrosylation; Transcription; Transcription regulation.
FT   CHAIN         1    488       Histone deacetylase 2.
FT                                /FTId=PRO_0000114694.
FT   REGION        9    322       Histone deacetylase.
FT   COMPBIAS    300    303       Poly-Gly.
FT   ACT_SITE    142    142       By similarity.
FT   MOD_RES      75     75       N6-acetyllysine (By similarity).
FT   MOD_RES      90     90       N6-acetyllysine (By similarity).
FT   MOD_RES     262    262       S-nitrosocysteine.
FT   MOD_RES     274    274       S-nitrosocysteine.
FT   MOD_RES     394    394       Phosphoserine.
FT   MOD_RES     407    407       Phosphoserine (By similarity).
FT   MOD_RES     422    422       Phosphoserine.
FT   MOD_RES     424    424       Phosphoserine.
FT   MUTAGEN     152    152       C->A: Does not affect S-nitrosylation.
FT   MUTAGEN     262    262       C->A: Impairs S-nitrosylation. Abolishes
FT                                S-nitrosylation; when associated with A-
FT                                274.
FT   MUTAGEN     274    274       C->A: Impairs S-nitrosylation. Abolishes
FT                                S-nitrosylation; when associated with A-
FT                                262.
FT   CONFLICT    289    289       A -> V (in Ref. 2; EDL04897).
SQ   SEQUENCE   488 AA;  55302 MW;  B9843D24A775157C CRC64;
     MAYSQGGGKK KVCYYYDGDI GNYYYGQGHP MKPHRIRMTH NLLLNYGLYR KMEIYRPHKA
     TAEEMTKYHS DEYIKFLRSI RPDNMSEYSK QMQRFNVGED CPVFDGLFEF CQLSTGGSVA
     GAVKLNRQQT DMAVNWAGGL HHAKKSEASG FCYVNDIVLA ILELLKYHQR VLYIDIDIHH
     GDGVEEAFYT TDRVMTVSFH KYGEYFPGTG DLRDIGAGKG KYYAVNFPMR DGIDDESYGQ
     IFKPIISKVM EMYQPSAVVL QCGADSLSGD RLGCFNLTVK GHAKCVEVAK TFNLPLLMLG
     GGGYTIRNVA RCWTYETAVA LDCEIPNELP YNDYFEYFGP DFKLHISPSN MTNQNTPEYM
     EKIKQRLFEN LRMLPHAPGV QMQAIPEDAV HEDSGDEDGE DPDKRISIRA SDKRIACDEE
     FSDSEDEGEG GRRNVADHKK GAKKARIEED KKETEDKKTD VKEEDKSKDN SGEKTDPKGA
     KSEQLSNP
//
ID   EM55_MOUSE              Reviewed;         466 AA.
AC   P70290;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=55 kDa erythrocyte membrane protein;
DE            Short=p55;
DE   AltName: Full=Membrane protein, palmitoylated 1;
GN   Name=Mpp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129, and C57BL/6 X CBA;
RX   MEDLINE=97127600; PubMed=8954807; DOI=10.1006/geno.1996.0621;
RA   Elder B., Kuo K., Gitschier J., Kim A., Chishti A., Metzenberg A.;
RT   "cDNA sequence and genomic structure of the murine p55 (Mpp1) gene.";
RL   Genomics 38:231-234(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH WHRN, AND SUBCELLULAR LOCATION.
RX   PubMed=16829577; DOI=10.1073/pnas.0600923103;
RA   Mburu P., Kikkawa Y., Townsend S., Romero R., Yonekawa H., Brown S.D.;
RT   "Whirlin complexes with p55 at the stereocilia tip during hair cell
RT   development.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:10973-10978(2006).
RN   [4]
RP   SUBCELLULAR LOCATION, INTERACTION WITH MPP5 AND WHRN, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=17584769; DOI=10.1093/hmg/ddm147;
RA   Gosens I., van Wijk E., Kersten F.F., Krieger E., van der Zwaag B.,
RA   Maerker T., Letteboer S.J., Dusseljee S., Peters T., Spierenburg H.A.,
RA   Punte I.M., Wolfrum U., Cremers F.P.M., Kremer H., Roepman R.;
RT   "MPP1 links the Usher protein network and the Crumbs protein complex
RT   in the retina.";
RL   Hum. Mol. Genet. 16:1993-2003(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=19897731;
RA   Quinn B.J., Welch E.J., Kim A.C., Lokuta M.A., Huttenlocher A.,
RA   Khan A.A., Kuchay S.M., Chishti A.H.;
RT   "Erythrocyte scaffolding protein p55/MPP1 functions as an essential
RT   regulator of neutrophil polarity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:19842-19847(2009).
CC   -!- FUNCTION: Essential regulator of neutrophil polarity. Regulates
CC       neutrophil polarization by regulating AKT1 phosphorylation through
CC       a mechanism that is independent of PIK3CG activity.
CC   -!- SUBUNIT: Heterodimer with MPP5. Interacts with DLG5 and NF2.
CC       Interacts (via guanylate kinase-like domain) with WHRN (via third
CC       PDZ domain).
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC       similarity). Cell projection, stereocilium. Note=Colocalizes with
CC       WHRN at stereocilium tip during hair cell development. Colocalizes
CC       with MPP5 in the retina, at the outer limiting membrane (OLM).
CC       Colocalizes with WHRN in the retina, at the outer limiting
CC       membrane (OLM), outer plexifirm layer (OPL), basal bodies, and at
CC       connecting cilium (CC). Colocalizes with NF2 in non-myelin-forming
CC       Schwann cells (By similarity).
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in the erythrocytes (at
CC       protein level).
CC   -!- DEVELOPMENTAL STAGE: During development of the retina, expression
CC       is highest in the inner, neuroblastic layer, while at later stages
CC       it is also present in the photoreceptor cell layer. Detected in
CC       the eye from E14.5 onwards. Highly expressed in the liver and
CC       primitive gut, and at lower levels in the umbilical vein, the
CC       ventricular layer of the CNS and upper/lower jaw region. At E14.5
CC       and E16.5, expression in the liver and stomach is maintained. In
CC       addition, expression is present in bone structures (e.g. zygomatic
CC       bone, lower jawbone), cranial nerve ganglia [e.g. trigeminal (V)
CC       ganglion] and cochlea. The expression in the eye is seen in the
CC       neuroblastic layer. At E16.5 and E18.5, a slightly higher
CC       expression is seen in the neuroblastic layer. At E16.5, strong
CC       expression in the upper part of the gut is maintained and with the
CC       onset of ossification, expression is seen in all bone structures
CC       of the body. At P7 and P90, expression in the eye is seen in the
CC       ganglion cell layer, the inner nuclear layer (INL) and
CC       photoreceptor cell layer.
CC   -!- PTM: Extensively palmitoylated (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Neutrophils form multiple transient
CC       pseudopods upon chemotactic stimulation, and do not migrate
CC       efficiently in vitro.
CC   -!- SIMILARITY: Belongs to the MAGUK family.
CC   -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; U38196; AAC52970.1; -; mRNA.
DR   EMBL; BC013444; AAH13444.1; -; mRNA.
DR   IPI; IPI00137706; -.
DR   RefSeq; NP_032647.1; NM_008621.2.
DR   UniGene; Mm.391267; -.
DR   ProteinModelPortal; P70290; -.
DR   SMR; P70290; 69-153, 161-463.
DR   PhosphoSite; P70290; -.
DR   PRIDE; P70290; -.
DR   Ensembl; ENSMUST00000033775; ENSMUSP00000033775; ENSMUSG00000031402.
DR   GeneID; 17524; -.
DR   KEGG; mmu:17524; -.
DR   UCSC; uc009tpp.1; mouse.
DR   CTD; 17524; -.
DR   MGI; MGI:105941; Mpp1.
DR   HOGENOM; HBG446173; -.
DR   HOVERGEN; HBG001858; -.
DR   InParanoid; P70290; -.
DR   OMA; RKVRLIQ; -.
DR   OrthoDB; EOG46HG9K; -.
DR   PhylomeDB; P70290; -.
DR   NextBio; 292136; -.
DR   ArrayExpress; P70290; -.
DR   Bgee; P70290; -.
DR   CleanEx; MM_MPP1; -.
DR   Genevestigator; P70290; -.
DR   GermOnline; ENSMUSG00000031402; Mus musculus.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0032420; C:stereocilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0090022; P:regulation of neutrophil chemotaxis; IMP:UniProtKB.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   SH3 domain.
FT   CHAIN         1    466       55 kDa erythrocyte membrane protein.
FT                                /FTId=PRO_0000094566.
FT   DOMAIN       71    152       PDZ.
FT   DOMAIN      158    228       SH3.
FT   DOMAIN      282    451       Guanylate kinase-like.
FT   REGION      268    466       Interaction with MPP5 (By similarity).
FT   MOD_RES      19     19       Phosphoserine.
FT   MOD_RES      49     49       Phosphothreonine (By similarity).
FT   MOD_RES      57     57       Phosphoserine (By similarity).
FT   MOD_RES     243    243       Phosphoserine (By similarity).
SQ   SEQUENCE   466 AA;  52227 MW;  8724DE75A717A464 CRC64;
     MTLKSSEGEG GNSMRTALSD LYLEHLLQKR NRPETSLNQS NVTTEDMYTN GSPAPGSPAH
     AKGQEARRVR LIQFEKITEE PMGITLKLNE KQSCTVARIL HGGMIHRQGS LHVGDEILEI
     NGTNVTNHSV DQLQKAMKET KGMISLKVIA NQQSRLPALQ MFMRAQFDYD PQKDNLIPCK
     EAGLKFVTGD IIQIINKDDS NWWQGRVEGS SKESAGLIPS PELQEWRVAS VAHSAPSEAP
     SCSPFGKKKK CKDKYLAKHS SIFDQLDVVS YEEVVRLPAF KRKTLVLIGA SGVGRSHIKN
     GLLSHNPEKF AYPAPYTTRP PKKSEEDGKE YHFISTEEMT KNISANEFLE FGSYQGNMFG
     TKFETVHQIH KQDKIAILDI EPQTLKTVRT AELSPFIVFI APTDQGTQTE ALQQLQKDSE
     AIRSQYAHYF DLSLVNNSVD ETLKKLQEAF DQACSSPQWV PVSWVY
//
ID   AUP1_MOUSE              Reviewed;         410 AA.
AC   P70295;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Ancient ubiquitous protein 1;
GN   Name=Aup1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RX   MEDLINE=96411699; PubMed=8812468; DOI=10.1006/geno.1996.0477;
RA   Jang W., Weber J.S., Bashir R., Bushby K., Meisler M.H.;
RT   "Aup1, a novel gene on mouse chromosome 6 and human chromosome 2p13.";
RL   Genomics 36:366-368(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in the translocation of terminally
CC       misfolded proteins from the endoplasmic reticulum lumen to the
CC       cytoplasm and their degradation by the proteasome (By similarity).
CC   -!- SUBUNIT: Identified in a complex that contains SEL1L, OS9,
CC       FAF2/UBXD8, UBE2J1/UBC6E and AUP1. Interacts with the cytoplasmic
CC       tail of ITGA2B, ITGA1, ITGA2, ITGA5, ITGAV and ITGAM (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       type III membrane protein; Cytoplasmic side (By similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the AUP1 family.
CC   -!- SIMILARITY: Contains 1 CUE domain.
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DR   EMBL; U41736; AAC52839.1; -; mRNA.
DR   EMBL; BC016485; AAH16485.1; -; mRNA.
DR   IPI; IPI00137725; -.
DR   UniGene; Mm.386752; -.
DR   ProteinModelPortal; P70295; -.
DR   SMR; P70295; 294-345, 378-404.
DR   STRING; P70295; -.
DR   PhosphoSite; P70295; -.
DR   PRIDE; P70295; -.
DR   Ensembl; ENSMUST00000092618; ENSMUSP00000090281; ENSMUSG00000068328.
DR   MGI; MGI:107789; Aup1.
DR   eggNOG; roNOG12028; -.
DR   HOVERGEN; HBG004321; -.
DR   InParanoid; P70295; -.
DR   OrthoDB; EOG47H5Q7; -.
DR   PhylomeDB; P70295; -.
DR   ArrayExpress; P70295; -.
DR   Bgee; P70295; -.
DR   CleanEx; MM_AUP1; -.
DR   Genevestigator; P70295; -.
DR   GermOnline; ENSMUSG00000068328; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008415; F:acyltransferase activity; IEA:InterPro.
DR   InterPro; IPR002123; Acyltransferase.
DR   InterPro; IPR003892; CUE.
DR   Pfam; PF02845; CUE; 1.
DR   SMART; SM00546; CUE; 1.
DR   SMART; SM00563; PlsC; 1.
DR   PROSITE; PS51140; CUE; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix; Ubl conjugation pathway.
FT   CHAIN         1    410       Ancient ubiquitous protein 1.
FT                                /FTId=PRO_0000020766.
FT   TOPO_DOM      1     20       Lumenal (Potential).
FT   TRANSMEM     21     41       Helical; Signal-anchor for type III
FT                                membrane protein; (Potential).
FT   TOPO_DOM     42    410       Cytoplasmic (Potential).
FT   DOMAIN      296    338       CUE.
FT   MOD_RES     292    292       Phosphoserine (By similarity).
FT   MOD_RES     356    356       Phosphoserine (By similarity).
FT   MOD_RES     363    363       Phosphoserine (By similarity).
FT   MOD_RES     367    367       Phosphothreonine (By similarity).
SQ   SEQUENCE   410 AA;  46121 MW;  E7D070CEB296BD5B CRC64;
     MEPPPAPGPE RLFDSHRLPS DGFLLLALLL YAPVGLCLLV LRLFLGLHVF LVSCALPDSV
     LRRFVVRTMC AVLGLVARQE DSGLRDHRVR VLISNHVTPF DHNIVNLLTT CSTPLLNSPP
     SFVCWSRGFM EMDRRVELVE SLKKFCASTR LPPTPLLLFP EEEATNGREG LLRFSSWPFS
     IQDVVQPLTL QVQRPLVSVT VSDASWVSEL LWSLFVPFTV YQVRWLHPIR RQLGEESEEF
     ALRVQQLVAK ELGQIGTRLT PADKAEHMKR QRHPRLRPQS VQSSFPSPPS PSSDVQLTTL
     AHRVKEVLPH VPLNVIQRDL ARTGCVDLTI TNLLEGAVAF MPEDVTEGSQ SPPAPSAPKF
     PSSGLATPQP TALTFAKSSW ARQESLQERK QALYEYARRR FRERQAQEAE
//
ID   PEBP1_MOUSE             Reviewed;         187 AA.
AC   P70296; Q9D8G9; Q9JJ58;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Phosphatidylethanolamine-binding protein 1;
DE            Short=PEBP-1;
DE   AltName: Full=HCNPpp;
DE   Contains:
DE     RecName: Full=Hippocampal cholinergic neurostimulating peptide;
DE              Short=HCNP;
GN   Name=Pebp1; Synonyms=Pbp, Pebp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Lin B., Frischauf A.-M.;
RT   "Cloning of mouse phosphatidylethanolamine binding protein gene.";
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-12.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=99158500; PubMed=10051191; DOI=10.1016/S0306-4522(98)00215-2;
RA   Matsukawa N., Tooyama I., Kimura H., Yamamoto T., Tsugu Y., Oomura Y.,
RA   Ojika K.;
RT   "Increased expression of hippocampal cholinergic neurostimulating
RT   peptide-related components and their messenger RNAs in the hippocampus
RT   of aged senescence-accelerated mice.";
RL   Neuroscience 88:79-92(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Matsukawa N.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 27-39; 63-76;
RP   94-141 AND 158-180.
RC   STRAIN=C57BL/6;
RX   PubMed=11034991; DOI=10.1074/jbc.M002524200;
RA   Hengst U., Albrecht H., Hess D., Monard D.;
RT   "The phosphatidylethanolamine-binding protein is the prototype of a
RT   novel family of serine protease inhibitors.";
RL   J. Biol. Chem. 276:535-540(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and NMRI; TISSUE=Mammary gland, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 63-76 AND 94-119, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-52 AND SER-54,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Binds ATP, opioids and phosphatidylethanolamine. Has
CC       lower affinity for phosphatidylinositol and phosphatidylcholine.
CC       Serine protease inhibitor which inhibits thrombin, neuropsin and
CC       chymotrypsin but not trypsin, tissue type plasminogen activator
CC       and elastase.
CC   -!- FUNCTION: HCNP may be involved in the function of the presynaptic
CC       cholinergic neurons of the central nervous system. HCNP increases
CC       the production of choline acetyltransferase but not
CC       acetylcholinesterase. Seems to be mediated by a specific receptor
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: HCNP is expressed in brain. Increased
CC       expression in aged senescence-accelerated mice.
CC   -!- SIMILARITY: Belongs to the phosphatidylethanolamine-binding
CC       protein family.
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DR   EMBL; U43206; AAB06983.1; -; mRNA.
DR   EMBL; AF300422; AAG25635.1; -; mRNA.
DR   EMBL; AB046417; BAB03276.1; -; mRNA.
DR   EMBL; AK088212; BAC40214.1; -; mRNA.
DR   EMBL; BC008169; AAH08169.1; -; mRNA.
DR   EMBL; BC083063; AAH83063.1; -; mRNA.
DR   IPI; IPI00137730; -.
DR   PIR; PN0043; PN0043.
DR   RefSeq; NP_061346.2; NM_018858.2.
DR   UniGene; Mm.195898; -.
DR   UniGene; Mm.338476; -.
DR   UniGene; Mm.473809; -.
DR   ProteinModelPortal; P70296; -.
DR   SMR; P70296; 1-187.
DR   STRING; P70296; -.
DR   MEROPS; I51.002; -.
DR   PhosphoSite; P70296; -.
DR   REPRODUCTION-2DPAGE; P70296; -.
DR   UCD-2DPAGE; P70296; -.
DR   PRIDE; P70296; -.
DR   Ensembl; ENSMUST00000036951; ENSMUSP00000048425; ENSMUSG00000032959.
DR   GeneID; 23980; -.
DR   KEGG; mmu:23980; -.
DR   UCSC; uc008zfl.1; mouse.
DR   CTD; 23980; -.
DR   MGI; MGI:1344408; Pebp1.
DR   eggNOG; roNOG05879; -.
DR   HOVERGEN; HBG008165; -.
DR   OrthoDB; EOG4FFD2T; -.
DR   PhylomeDB; P70296; -.
DR   NextBio; 303865; -.
DR   Bgee; P70296; -.
DR   CleanEx; MM_PEBP1; -.
DR   Genevestigator; P70296; -.
DR   GermOnline; ENSMUSG00000032959; Mus musculus.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0048240; P:sperm capacitation; IDA:MGI.
DR   InterPro; IPR001858; Phosphotidylethanolamine-bd_CS.
DR   InterPro; IPR008914; PtdEtn-bd_prot_PEBP.
DR   Gene3D; G3DSA:3.90.280.10; PEBP; 1.
DR   Pfam; PF01161; PBP; 1.
DR   SUPFAM; SSF49777; PEBP; 1.
DR   PROSITE; PS01220; PBP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing;
KW   Lipid-binding; Nucleotide-binding; Phosphoprotein; Protease inhibitor;
KW   Serine protease inhibitor.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    187       Phosphatidylethanolamine-binding protein
FT                                1.
FT                                /FTId=PRO_0000023275.
FT   PEPTIDE       2     12       Hippocampal cholinergic neurostimulating
FT                                peptide.
FT                                /FTId=PRO_0000023276.
FT   MOD_RES       2      2       N-acetylalanine; in peptide hippocampal
FT                                cholinergic neurostimulating (By
FT                                similarity).
FT   MOD_RES      42     42       Phosphothreonine (By similarity).
FT   MOD_RES      51     51       Phosphoserine.
FT   MOD_RES      52     52       Phosphoserine.
FT   MOD_RES      54     54       Phosphoserine.
FT   CONFLICT    116    116       G -> S (in Ref. 1; AAB06983).
SQ   SEQUENCE   187 AA;  20830 MW;  4059C7C6E4A8BAA0 CRC64;
     MAADISQWAG PLCLQEVDEP PQHALRVDYA GVTVDELGKV LTPTQVMNRP SSISWDGLDP
     GKLYTLVLTD PDAPSRKDPK FREWHHFLVV NMKGNDISSG TVLSDYVGSG PPSGTGLHRY
     VWLVYEQEQP LSCDEPILSN KSGDNRGKFK VETFRKKYNL GAPVAGTCYQ AEWDDYVPKL
     YEQLSGK
//
ID   STIM1_MOUSE             Reviewed;         685 AA.
AC   P70302;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Stromal interaction molecule 1;
DE   Flags: Precursor;
GN   Name=Stim1; Synonyms=Sim;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=C57BL/6 X DBA/2; TISSUE=Bone marrow stroma;
RX   MEDLINE=96326680; PubMed=8707854; DOI=10.1083/jcb.134.3.771;
RA   Oritani K., Kincade P.W.;
RT   "Identification of stromal cell products that interact with pre-B
RT   cells.";
RL   J. Cell Biol. 134:771-782(1996).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-665 AND SER-668, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-519 AND SER-524, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257 AND SER-519, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Plays a role in mediating Ca(2+) influx following
CC       depletion of intracellular Ca(2+) stores. Acts as Ca(2+) sensor in
CC       the endoplasmic reticulum via its EF-hand domain. Upon Ca(2+)
CC       depletion, translocates from the endoplasmic reticulum to the
CC       plasma membrane where it activates the Ca(2+) release-activated
CC       Ca(2+) (CRAC) channel subunit, TMEM142A/ORAI1 (By similarity).
CC   -!- SUBUNIT: Forms homooligomers and heterooligomers with STIM2.
CC       Interacts with ORAI1. Interacts with MAPRE1; probably required for
CC       targeting to the growing microtubule plus ends. Interacts with
CC       EFCAB4B/CRACR2A; the interaction is direct and takes place in
CC       absence of Ca(2+). Forms a complex with EFCAB4B/CRACR2A and ORAI1
CC       at low concentration of Ca(2+), the complex dissociates at
CC       elevated Ca(2+) concentrations (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein (By similarity). Endoplasmic reticulum membrane; Single-
CC       pass type I membrane protein (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity). Note=Translocates from the
CC       endoplasmic reticulum to the cell membrane in response to a
CC       depletion of intracellular Ca(2+). Associated with the microtubule
CC       network at the growing distal tip of microtubules (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined and in many
CC       cell types, including bone marrow stroma, fibroblast, B-cell
CC       precursors, lymphoma and erythroleukemia.
CC   -!- DOMAIN: The microtubule tip localization signal (MtLS) motif;
CC       mediates interaction with MAPRE1 and targeting to the growing
CC       microtubule plus ends (By similarity).
CC   -!- PTM: Glycosylation is required for cell surface expression (By
CC       similarity).
CC   -!- PTM: Phosphorylated predominantly on Ser residues (By similarity).
CC   -!- SIMILARITY: Contains 1 EF-hand domain.
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
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DR   EMBL; U47323; AAC52715.1; -; mRNA.
DR   IPI; IPI00108041; -.
DR   UniGene; Mm.645; -.
DR   ProteinModelPortal; P70302; -.
DR   SMR; P70302; 55-201.
DR   DIP; DIP-48770N; -.
DR   STRING; P70302; -.
DR   PhosphoSite; P70302; -.
DR   PRIDE; P70302; -.
DR   Ensembl; ENSMUST00000033289; ENSMUSP00000033289; ENSMUSG00000030987.
DR   MGI; MGI:107476; Stim1.
DR   eggNOG; roNOG13590; -.
DR   HOGENOM; HBG714829; -.
DR   HOVERGEN; HBG054652; -.
DR   InParanoid; P70302; -.
DR   OrthoDB; EOG4F4S9M; -.
DR   ArrayExpress; P70302; -.
DR   Bgee; P70302; -.
DR   CleanEx; MM_STIM1; -.
DR   Genevestigator; P70302; -.
DR   GermOnline; ENSMUSG00000030987; Mus musculus.
DR   GO; GO:0030176; C:integral to endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0005887; C:integral to plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
DR   GO; GO:0032237; P:activation of store-operated calcium channel activity; ISS:UniProtKB.
DR   GO; GO:0006816; P:calcium ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0005513; P:detection of calcium ion; ISS:UniProtKB.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR011510; SAM_2.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS00018; EF_HAND_1; FALSE_NEG.
DR   PROSITE; PS50222; EF_HAND_2; FALSE_NEG.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Calcium; Calcium transport; Cell membrane; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Endoplasmic reticulum; Glycoprotein; Ion transport;
KW   Membrane; Microtubule; Phosphoprotein; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     22       Potential.
FT   CHAIN        23    685       Stromal interaction molecule 1.
FT                                /FTId=PRO_0000033327.
FT   TOPO_DOM     23    213       Extracellular (Potential).
FT   TRANSMEM    214    234       Helical; (Potential).
FT   TOPO_DOM    235    685       Cytoplasmic (Potential).
FT   DOMAIN       63     98       EF-hand.
FT   DOMAIN      132    200       SAM.
FT   CA_BIND      76     87       Potential.
FT   COILED      248    388       Potential.
FT   MOTIF       642    645       Microtubule tip localization signal.
FT   COMPBIAS    270    336       Glu-rich.
FT   COMPBIAS    601    629       Pro/Ser-rich.
FT   COMPBIAS    672    685       Lys-rich.
FT   MOD_RES     257    257       Phosphoserine.
FT   MOD_RES     420    420       Phosphothreonine (By similarity).
FT   MOD_RES     519    519       Phosphoserine.
FT   MOD_RES     524    524       Phosphoserine.
FT   MOD_RES     575    575       Phosphoserine (By similarity).
FT   MOD_RES     608    608       Phosphoserine (By similarity).
FT   MOD_RES     660    660       Phosphoserine (By similarity).
FT   MOD_RES     665    665       Phosphothreonine.
FT   MOD_RES     668    668       Phosphoserine.
FT   CARBOHYD    131    131       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    171    171       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   685 AA;  77583 MW;  6A16100B6405E0DB CRC64;
     MDVCARLALW LLWGLLLHQG QSLSHSHSEK NTGASSGATS EESTEAEFCR IDKPLCHSED
     EKLSFEAVRN IHKLMDDDAN GDVDVEESDE FLREDLNYHD PTVKHSTFHG EDKLISVEDL
     WKAWKSSEVY NWTVDEVIQW LITYVELPQY EETFRKLQLT GHAMPRLAVT NTTMTGTVLK
     MTDRSHRQKL QLKALDTVLF GPPLLTRHNH LKDFMLVVSI VIGVGGCWFA YIQNRYSKEH
     MKKMMKDLEG LHRAEQSLHD LQERLHKAQE EHRTVEVEKV HLEKKLRDEI NLAKQEAQRL
     KELREGTENE RSRQKYAEEE LEQVREALRK SEKELESHSS WYAPEALQKW LQLTHEVEVQ
     YYNIKKQNAE RQLLVAKEGA EKIKKKRNTL FGTFHVAHSS SLDDVDHKIL TAKQALSEVT
     AALRERLHRW QQIEILCGFQ IVNNPGIHSL VAALNIDPSW MGSTRPNPAH FIMTDDVDDM
     DEEIVSPLSM QSPSLQSSVR QRLTEPQLGL GSQRDLTHSD SESSLHMSDR QRVAPKPPQM
     GRAADEALNA MPSNGSHRLI EGVHPGSLVE KLPDSPALAK KTFMALNHGL DKAHSLMELN
     PSVPPGGSPL LDSSHSLSPS SPDPDTPSPV GDNRALQGSR NTRIPHLAGK KAMAEEDNGS
     IGEETDSSPG RKKFPLKIFK KPLKK
//
ID   NTR2_MOUSE              Reviewed;         417 AA.
AC   P70310;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Neurotensin receptor type 2;
DE            Short=NT-R-2;
DE            Short=NTR2;
DE   AltName: Full=Low-affinity levocabastine-sensitive neurotensin receptor;
DE   AltName: Full=NTRL;
GN   Name=Ntsr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=96388216; PubMed=8795617;
RA   Mazella J., Botto J.-M., Guillemare E., Coppola T., Sarret P.,
RA   Vincent J.-P.;
RT   "Structure, functional expression, and cerebral localization of the
RT   levocabastine-sensitive neurotensin/neuromedin N receptor from mouse
RT   brain.";
RL   J. Neurosci. 16:5613-5620(1996).
CC   -!- FUNCTION: Receptor for the tridecapeptide neurotensin. It is
CC       associated with G proteins that activate a phosphatidylinositol-
CC       calcium second messenger system.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed maximally in the cerebellum,
CC       hyppocampus, piriform cortex and neocortex of adult brain.
CC   -!- DEVELOPMENTAL STAGE: Expressed poorly in 7-day-old brain.
CC       Expression increases at day 15 to reach a maximal level in 35-day-
CC       old brain.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Neurotensin receptor subfamily. NTSR2 sub-subfamily.
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DR   EMBL; U51908; AAB17285.1; -; mRNA.
DR   IPI; IPI00346625; -.
DR   UniGene; Mm.281715; -.
DR   ProteinModelPortal; P70310; -.
DR   SMR; P70310; 121-151.
DR   STRING; P70310; -.
DR   PhosphoSite; P70310; -.
DR   PRIDE; P70310; -.
DR   Ensembl; ENSMUST00000020910; ENSMUSP00000020910; ENSMUSG00000020591.
DR   MGI; MGI:108018; Ntsr2.
DR   eggNOG; roNOG11937; -.
DR   HOVERGEN; HBG098285; -.
DR   OrthoDB; EOG4V438D; -.
DR   ArrayExpress; P70310; -.
DR   Bgee; P70310; -.
DR   CleanEx; MM_NTSR2; -.
DR   Genevestigator; P70310; -.
DR   GermOnline; ENSMUSG00000020591; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016492; F:neurotensin receptor activity, G-protein coupled; IDA:MGI.
DR   GO; GO:0007200; P:activation of phospholipase C activity by G-protein coupled receptor protein signaling pathway coupled to IP3 second messenger; IDA:MGI.
DR   GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR003986; NT2_rcpt.
DR   InterPro; IPR003984; NT_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01479; NEUROTENSINR.
DR   PRINTS; PR01481; NEUROTENSN2R.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Lipoprotein; Membrane; Palmitate; Receptor; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    417       Neurotensin receptor type 2.
FT                                /FTId=PRO_0000069950.
FT   TOPO_DOM      1     32       Extracellular (Potential).
FT   TRANSMEM     33     55       Helical; Name=1; (Potential).
FT   TOPO_DOM     56     64       Cytoplasmic (Potential).
FT   TRANSMEM     65     87       Helical; Name=2; (Potential).
FT   TOPO_DOM     88    109       Extracellular (Potential).
FT   TRANSMEM    110    131       Helical; Name=3; (Potential).
FT   TOPO_DOM    132    154       Cytoplasmic (Potential).
FT   TRANSMEM    155    176       Helical; Name=4; (Potential).
FT   TOPO_DOM    177    217       Extracellular (Potential).
FT   TRANSMEM    218    238       Helical; Name=5; (Potential).
FT   TOPO_DOM    239    298       Cytoplasmic (Potential).
FT   TRANSMEM    299    319       Helical; Name=6; (Potential).
FT   TOPO_DOM    320    338       Extracellular (Potential).
FT   TRANSMEM    339    359       Helical; Name=7; (Potential).
FT   TOPO_DOM    360    417       Cytoplasmic (Potential).
FT   LIPID       378    378       S-palmitoyl cysteine (Potential).
FT   DISULFID    108    194       By similarity.
SQ   SEQUENCE   417 AA;  46537 MW;  EBFDDBD6507223DD CRC64;
     METSSLWPPR PSPSAGLSLE ARLGVDTRLW AKVLFTALYS LIFALGTAGN ALSVHVVLKA
     RTGRPGRLRY HVLSLALSAL LLLLISVPME LYNFVWSHYP WVFGDLGCRG YYFVRELCAY
     ATVLSVASLS AERCLAVCQP LRARRLLTPR RTCRLLSLVW VASLGLALPM AVIMGQKHEM
     ERADGEPEPA SRVCTVLVSR ASSRSTFQVK RAGLLRSPLW ELTAILNGIT VNHLVALYSQ
     VPSASAQVNS IPSRLELLSE EGLLGFITWR KTLSLGVQAS LVRHKDASQI RSLQHSAQVL
     RAIVAVYVIC WLPYHARRLM YCYIPDDGWT DELYDFYHYF YMVTNTLFYV SSAVTPVLYN
     AVSSSFRKLF LESLSSLCGE QRSVVPLPQE APESTTSTYS FRLWGSPRNP SLGEIQV
//
ID   HNRH2_MOUSE             Reviewed;         449 AA.
AC   P70333; Q3THV9;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Heterogeneous nuclear ribonucleoprotein H2;
DE            Short=hnRNP H2;
DE   AltName: Full=Heterogeneous nuclear ribonucleoprotein H';
DE            Short=hnRNP H';
GN   Name=Hnrnph2; Synonyms=Hnrph2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C129;
RX   MEDLINE=95352959; PubMed=7626884; DOI=10.1007/BF00364796;
RA   Oeltjen J.C., Liu X., Lu J., Allen R.C., Muzny D.M., Belmont J.W.,
RA   Gibbs R.A.;
RT   "Sixty-nine kilobases of contiguous human genomic sequence containing
RT   the alpha-galactosidase A and Bruton's tyrosine kinase loci.";
RL   Mamm. Genome 6:334-338(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, and C57BL/6J; TISSUE=Kidney, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND THR-107, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: This protein is a component of the heterogeneous nuclear
CC       ribonucleoprotein (hnRNP) complexes which provide the substrate
CC       for the processing events that pre-mRNAs undergo before becoming
CC       functional, translatable mRNAs in the cytoplasm. Binds poly(RG)
CC       (By similarity).
CC   -!- SUBUNIT: Interacts with TXNL4/DIM1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm (By similarity).
CC   -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.
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DR   EMBL; U58105; AAB47243.1; -; Genomic_DNA.
DR   EMBL; AK077716; BAC36976.1; -; mRNA.
DR   EMBL; AK164115; BAE37634.1; -; mRNA.
DR   EMBL; AK168116; BAE40087.1; -; mRNA.
DR   EMBL; AK169104; BAE40886.1; -; mRNA.
DR   EMBL; BC005461; AAH05461.1; -; mRNA.
DR   IPI; IPI00108143; -.
DR   RefSeq; NP_063921.1; NM_019868.3.
DR   UniGene; Mm.315909; -.
DR   ProteinModelPortal; P70333; -.
DR   SMR; P70333; 1-102, 105-193, 283-365.
DR   STRING; P70333; -.
DR   PhosphoSite; P70333; -.
DR   PRIDE; P70333; -.
DR   Ensembl; ENSMUST00000050331; ENSMUSP00000108827; ENSMUSG00000045427.
DR   Ensembl; ENSMUST00000059297; ENSMUSP00000050838; ENSMUSG00000045427.
DR   Ensembl; ENSMUST00000074950; ENSMUSP00000074483; ENSMUSG00000045427.
DR   Ensembl; ENSMUST00000113202; ENSMUSP00000108828; ENSMUSG00000045427.
DR   Ensembl; ENSMUST00000113203; ENSMUSP00000108829; ENSMUSG00000045427.
DR   GeneID; 56258; -.
DR   KEGG; mmu:56258; -.
DR   UCSC; uc009ugh.1; mouse.
DR   CTD; 56258; -.
DR   MGI; MGI:1201779; Hnrnph2.
DR   HOGENOM; HBG447282; -.
DR   HOVERGEN; HBG055557; -.
DR   InParanoid; P70333; -.
DR   OMA; PPRKLMT; -.
DR   OrthoDB; EOG4CRM03; -.
DR   PhylomeDB; P70333; -.
DR   NextBio; 312148; -.
DR   ArrayExpress; P70333; -.
DR   Bgee; P70333; -.
DR   Genevestigator; P70333; -.
DR   GermOnline; ENSMUSG00000045427; Mus musculus.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR012996; Znf_CHHC.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 3.
DR   Pfam; PF00076; RRM_1; 3.
DR   Pfam; PF08080; zf-RNPHF; 1.
DR   SMART; SM00360; RRM; 3.
DR   PROSITE; PS50102; RRM; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Methylation; Nucleus; Phosphoprotein; Repeat;
KW   Ribonucleoprotein; RNA-binding.
FT   CHAIN         1    449       Heterogeneous nuclear ribonucleoprotein
FT                                H2.
FT                                /FTId=PRO_0000081860.
FT   DOMAIN       11     90       RRM 1.
FT   DOMAIN      111    188       RRM 2.
FT   REPEAT      234    249       1-1.
FT   DOMAIN      289    364       RRM 3.
FT   REPEAT      354    372       2-1.
FT   REPEAT      374    392       2-2.
FT   REPEAT      418    433       1-2.
FT   REGION      234    433       2 X 16 AA Gly-rich approximate repeats.
FT   REGION      354    392       2 X 19 AA perfect repeats.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     104    104       Phosphoserine.
FT   MOD_RES     107    107       Phosphothreonine.
FT   MOD_RES     217    217       Asymmetric dimethylarginine (By
FT                                similarity).
FT   MOD_RES     310    310       Phosphoserine (By similarity).
SQ   SEQUENCE   449 AA;  49280 MW;  2ED0A7A87A7EDF5E CRC64;
     MMLSTEGREG FVVKVRGLPW SCSAEEVMRF FSDCKIQNGT SGVRFIYTRE GRPSGEAFVE
     LESEDEVKLA LKKDRETMGH RYVEVFKSNS VEMDWVLKHT GPNSPDTAND GFVRLRGLPF
     GCSKEEIVQF FSGLEIVPNG MTLPVDFQGR STGEAFVQFA SQEIAEKALK KHKERIGHRY
     IEIFKSSRAE VRTHYDPPRK LMTMQRPGPY DRPGAGRGYN SIGRGAGFER MRRGAYGGGY
     GGYDDYGGYN DGYGFGSDRF GRDLNYCFSG MSDHRYGDGG SSFQSTTGHC VHMRGLPYRA
     TENDIYNFFS PLNPMRVHIE IGPDGRVTGE ADVEFATHED AVAAMAKDKA NMQHRYVELF
     LNSTAGTSGG AYDHSYVELF LNSTAGASGG AYGSQMMGGM GLSNQSSYGG PASQQLSGGY
     GGGYGGQSSM SGYDQVLQEN SSDYQSNLA
//
ID   ROCK2_MOUSE             Reviewed;        1388 AA.
AC   P70336; Q8BR64; Q8CBR0;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAR-2011, entry version 107.
DE   RecName: Full=Rho-associated protein kinase 2;
DE            EC=2.7.11.1;
DE   AltName: Full=Rho-associated, coiled-coil-containing protein kinase 2;
DE   AltName: Full=p164 ROCK-2;
GN   Name=Rock2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=96368048; PubMed=8772201; DOI=10.1016/0014-5793(96)00811-3;
RA   Nakagawa O., Fujisawa K., Ishizaki T., Saito Y., Nakao K.,
RA   Narumiya S.;
RT   "ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil
RT   forming protein serine/threonine kinase in mice.";
RL   FEBS Lett. 392:189-193(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 633-1388 AND 677-1388.
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   FUNCTION.
RX   PubMed=12832488; DOI=10.1128/MCB.23.14.5043-5055.2003;
RA   Thumkeo D., Keel J., Ishizaki T., Hirose M., Nonomura K., Oshima H.,
RA   Oshima M., Taketo M.M., Narumiya S.;
RT   "Targeted disruption of the mouse rho-associated kinase 2 gene results
RT   in intrauterine growth retardation and fetal death.";
RL   Mol. Cell. Biol. 23:5043-5055(2003).
CC   -!- FUNCTION: Regulates the assembly of the actin cytoskeleton.
CC       Promotes formation of stress fibers and of focal adhesion
CC       complexes. Plays a role in smooth muscle contraction.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activated by RHOA binding. Inhibited by Y-27632
CC       (By similarity).
CC   -!- SUBUNIT: Homodimer. Binds RHOA that has been activated by GTP
CC       binding. Binds IRS1, RHOB and RHOC. Interacts with CHORDC1 (By
CC       similarity).
CC   -!- INTERACTION:
CC       Q99N57:Raf1; NbExp=1; IntAct=EBI-771800, EBI-397757;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane;
CC       Peripheral membrane protein (By similarity). Note=Cytoplasmic, and
CC       associated with actin microfilaments and the plasma membrane (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain, heart, lung, liver,
CC       stomach, spleen, kidney, testis, muscle, embryo and placenta.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 REM (Hr1) repeat.
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DR   EMBL; U58513; AAC53133.1; -; mRNA.
DR   EMBL; AK045517; BAC32403.1; -; mRNA.
DR   EMBL; AK035509; BAC29084.1; -; mRNA.
DR   IPI; IPI00108150; -.
DR   PIR; S74245; S74245.
DR   RefSeq; NP_033098.2; NM_009072.2.
DR   UniGene; Mm.276024; -.
DR   ProteinModelPortal; P70336; -.
DR   SMR; P70336; 27-417, 979-1045, 1151-1351.
DR   IntAct; P70336; 3.
DR   STRING; P70336; -.
DR   PhosphoSite; P70336; -.
DR   PRIDE; P70336; -.
DR   Ensembl; ENSMUST00000020904; ENSMUSP00000020904; ENSMUSG00000020580.
DR   GeneID; 19878; -.
DR   KEGG; mmu:19878; -.
DR   UCSC; uc007ncg.1; mouse.
DR   CTD; 19878; -.
DR   MGI; MGI:107926; Rock2.
DR   eggNOG; roNOG04526; -.
DR   HOGENOM; HBG445047; -.
DR   HOVERGEN; HBG053111; -.
DR   InParanoid; P70336; -.
DR   OrthoDB; EOG4PZJ5T; -.
DR   PhylomeDB; P70336; -.
DR   BRENDA; 2.7.11.1; 244.
DR   ArrayExpress; P70336; -.
DR   Bgee; P70336; -.
DR   Genevestigator; P70336; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031616; C:spindle pole centrosome; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IGI:MGI.
DR   GO; GO:0000910; P:cytokinesis; IEA:InterPro.
DR   GO; GO:0001843; P:neural tube closure; IGI:MGI.
DR   GO; GO:0010825; P:positive regulation of centrosome duplication; IMP:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR020684; Rho-assoc_coiled-coil_kin-like.
DR   InterPro; IPR015751; Rho-assoc_coiled-coil_kinase.
DR   InterPro; IPR015008; Rho-bd.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Gene3D; G3DSA:1.20.5.730; Rho_bd; 1.
DR   PANTHER; PTHR22988:SF3; Rho_kinase; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   Pfam; PF08912; Rho_Binding; 1.
DR   PIRSF; PIRSF037568; Rho_kinase; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; FALSE_NEG.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Coiled coil; Cytoplasm; Kinase; Magnesium;
KW   Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1   1388       Rho-associated protein kinase 2.
FT                                /FTId=PRO_0000086626.
FT   DOMAIN       92    354       Protein kinase.
FT   DOMAIN      357    425       AGC-kinase C-terminal.
FT   REPEAT      475    559       REM.
FT   DOMAIN     1150   1349       PH.
FT   NP_BIND      98    106       ATP (By similarity).
FT   ZN_FING    1260   1315       Phorbol-ester/DAG-type.
FT   REGION      979   1047       RHOA binding (By similarity).
FT   COILED      439   1131       Potential.
FT   ACT_SITE    214    214       Proton acceptor (By similarity).
FT   BINDING     121    121       ATP (By similarity).
FT   MOD_RES     425    425       Phosphoserine (By similarity).
FT   MOD_RES    1078   1078       Phosphothreonine (By similarity).
FT   MOD_RES    1133   1133       Phosphoserine (By similarity).
FT   MOD_RES    1134   1134       Phosphoserine (By similarity).
FT   MOD_RES    1137   1137       Phosphoserine (By similarity).
FT   MOD_RES    1362   1362       Phosphoserine (By similarity).
FT   MOD_RES    1374   1374       Phosphoserine (By similarity).
SQ   SEQUENCE   1388 AA;  160586 MW;  7A4F331165038161 CRC64;
     MSRPPPTGKM PGAPEAAPGD GAGAGRQRKL EALIRDPRSP INVESLLDGL NSLVLDLDFP
     ALRKNKNIDN FLNRYEKIVK KIRGLQMKAE DYDVVKVIGR GAFGEVQLVR HKASQKVYAM
     KLLSKFEMIK RSDSAFFWEE RDIMAFANSP WVVQLFCAFQ DDRYLYMVME YMPGGDLVNL
     MSNYDVPEKW AKFYTAEVVL ALDAIHSMGL IHRDVKPDNM LLDKHGHLKL ADFGTCMKMD
     ETGMVHCDTA VGTPDYISPE VLKSQGGDGY YGRECDWWSV GVFLFEMLVG DTPFYADSLV
     GTYSKIMDHK NSLCFPEDTE ISKHAKNLIC AFLTDREVRL GRNGVEEIKQ HPFFKNDQWN
     WDNIRETAAP VVPELSSDID SSNFDDIEDD KGDVETFPIP KAFVGNQLPF IGFTYFRENL
     LLSDSPPCRE NDAIQTRKSE ESQEIQKKLY ALEEHLSSEV QAKEELEQKC KSINTRLEKT
     AKELEEEITL RKSVESTLRQ LEREKALLQH KNAEYQRKAD HEADKKRNLE NDVNSLKDQL
     EDLKKRNQSS QISTEKVNQL QKQLDEANAL LRTESDTAAR LRKTQAESSK QIQQLESNNR
     DLQDKNCLLE TAKLKLEKEF INLQSALESE RRDRTHGSEI INDLQGRISG LEEDLKTGKA
     LLAKVELEKR QLQEKLTDLE KEKSNMEIDM TYQLKVIQQS LEQEEAEHKT TKARLADKNK
     IYESIEEAKS EAMKEMEKKL LEERSLKQKV ENLLLEAEKR CSILDCDLKQ SQQKLNELLK
     QKDVLNEDVR NLTLKIEQET QKRCLMQNDL KMQTQQVNTL KMSEKQIKQE NNHLMEMKMN
     LEKQNTELRK ERQDADGQMK ELQDQLEAEQ YFSTLYKTQV RELKEENEEK TKLCKELQQK
     KQDLQDERDS LAAQLEITLT KADSEQLARS IAEEQYSDLE KEKIMKELEI KEMMARHKQE
     LTEKDTTIAS LEETNRTLTS DVANLANEKE ELNNKLKDSQ EQLSKLKDEE MSAAAIKAQF
     EKQLLNERTL KTQAVNKLAE IMNRKEPVKR GSDTDVRRKE KENRKLHMEL KSEREKLTQQ
     MIKYQKELNE MQAQIAEESQ IRIELQMTLD SKDSDIEQLR SQLQALHIGM DSSSIGSGPG
     DAEPDDGFPE SRLEGWLSLP VRNNTKKFGW VKKYVIVSSK KILFYDSEQD KEQSNPYMVL
     DIDKLFHVRP VTQTDVYRAD AKEIPRIFQI LYANEGESKK EPEFPVEPVG EKSNYICHKG
     HEFIPTLYHF PTNCEACMKP LWHMFKPPPA LECRRCHIKC HKDHMDKKEE IIAPCKVYYD
     ISSAKNLLLL ANSTEEQQKW VSRLVKKIPK KPPAPDPFAR SSPRTSMKIQ QNQSIRRPSR
     QLAPNKPS
//
ID   HINT1_MOUSE             Reviewed;         126 AA.
AC   P70349;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=Histidine triad nucleotide-binding protein 1;
DE            EC=3.-.-.-;
DE   AltName: Full=Adenosine 5'-monophosphoramidase;
DE   AltName: Full=Protein kinase C inhibitor 1;
DE   AltName: Full=Protein kinase C-interacting protein 1;
DE            Short=PKCI-1;
GN   Name=Hint1; Synonyms=Hint, Pkci, Pkci1, Prkcnh1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=NIH Swiss;
RX   MEDLINE=98445266; PubMed=9770345; DOI=10.1006/excr.1998.4153;
RA   Klein M.G., Yao Y., Slosberg E.D., Lima C.D., Doki Y., Weinstein I.B.;
RT   "Characterization of PKCI and comparative studies with FHIT, related
RT   members of the HIT protein family.";
RL   Exp. Cell Res. 244:26-32(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 8-21; 38-57 AND 96-119, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
CC   -!- FUNCTION: Hydrolyzes adenosine 5'-monophosphoramidate substrates
CC       such as AMP-morpholidate, AMP-N-alanine methyl ester, AMP-alpha-
CC       acetyl lysine methyl ester and AMP-NH2 (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- DOMAIN: The histidine triad, also called HIT motif, forms part of
CC       the binding loop for the alpha-phosphate of purine mononucleotide.
CC   -!- SIMILARITY: Belongs to the HINT family.
CC   -!- SIMILARITY: Contains 1 HIT domain.
CC   -!- CAUTION: Was originally thought to be a protein kinase C inhibitor
CC       and to bind zinc in solution. Both seem to be incorrect.
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DR   EMBL; U60001; AAC71076.1; -; mRNA.
DR   EMBL; AK002965; BAB22484.1; -; mRNA.
DR   EMBL; AK012433; BAB28235.1; -; mRNA.
DR   EMBL; BC070415; AAH70415.1; -; mRNA.
DR   EMBL; BC080296; AAH80296.1; -; mRNA.
DR   IPI; IPI00108189; -.
DR   PIR; PN0044; PN0044.
DR   RefSeq; NP_032274.1; NM_008248.2.
DR   UniGene; Mm.425; -.
DR   ProteinModelPortal; P70349; -.
DR   SMR; P70349; 14-126.
DR   STRING; P70349; -.
DR   PhosphoSite; P70349; -.
DR   PMMA-2DPAGE; P70349; -.
DR   REPRODUCTION-2DPAGE; P70349; -.
DR   PRIDE; P70349; -.
DR   Ensembl; ENSMUST00000020504; ENSMUSP00000020504; ENSMUSG00000020267.
DR   GeneID; 15254; -.
DR   KEGG; mmu:15254; -.
DR   UCSC; uc007iyj.1; mouse.
DR   CTD; 15254; -.
DR   MGI; MGI:1321133; Hint1.
DR   eggNOG; roNOG16223; -.
DR   GeneTree; ENSGT00510000046448; -.
DR   HOGENOM; HBG743217; -.
DR   HOVERGEN; HBG051906; -.
DR   InParanoid; P70349; -.
DR   OMA; HVMGGPR; -.
DR   OrthoDB; EOG4JM7R3; -.
DR   PhylomeDB; P70349; -.
DR   NextBio; 287869; -.
DR   ArrayExpress; P70349; -.
DR   Bgee; P70349; -.
DR   CleanEx; MM_HINT1; -.
DR   Genevestigator; P70349; -.
DR   GermOnline; ENSMUSG00000020267; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011146; His_triad-like_motif.
DR   InterPro; IPR011151; His_triad_motif.
DR   InterPro; IPR019808; Histidine_triad_CS.
DR   InterPro; IPR001310; Histidine_triad_HIT.
DR   Gene3D; G3DSA:3.30.428.10; His_triad_motif; 1.
DR   PANTHER; PTHR23089; HIT; 1.
DR   Pfam; PF01230; HIT; 1.
DR   PRINTS; PR00332; HISTRIAD.
DR   SUPFAM; SSF54197; His_triad-like_motif; 1.
DR   PROSITE; PS00892; HIT_1; 1.
DR   PROSITE; PS51084; HIT_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase; Nucleus.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    126       Histidine triad nucleotide-binding
FT                                protein 1.
FT                                /FTId=PRO_0000109782.
FT   DOMAIN       18    126       HIT.
FT   MOTIF       110    114       Histidine triad motif (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      21     21       N6-acetyllysine (By similarity).
FT   MOD_RES      30     30       N6-acetyllysine (By similarity).
SQ   SEQUENCE   126 AA;  13777 MW;  30DA241476389805 CRC64;
     MADEIAKAQV AQPGGDTIFG KIIRKEIPAK IIFEDDRCLA FHDISPQAPT HFLVIPKKHI
     SQISVADDDD ESLLGHLMIV GKKCAADLGL KRGYRMVVNE GADGGQSVYH IHLHVLGGRQ
     MNWPPG
//
ID   NCOA1_MOUSE             Reviewed;        1447 AA.
AC   P70365; P70366; Q61202; Q66JL7; Q8CBI9;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 2.
DT   08-MAR-2011, entry version 108.
DE   RecName: Full=Nuclear receptor coactivator 1;
DE            Short=NCoA-1;
DE            EC=2.3.1.48;
DE   AltName: Full=Nuclear receptor coactivator protein 1;
DE            Short=mNRC-1;
DE   AltName: Full=Steroid receptor coactivator 1;
DE            Short=SRC-1;
GN   Name=Ncoa1; Synonyms=Src1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND INTERACTION WITH
RP   EP300 AND CREBBP.
RX   PubMed=8616895; DOI=10.1016/S0092-8674(00)81118-6;
RA   Kamei Y., Xu L., Heinzel T., Torchia J., Kurokawa R., Gloss B.,
RA   Lin S.-C., Heyman R.A., Rose D.W., Glass C.K., Rosenfeld M.G.;
RT   "A CBP integrator complex mediates transcriptional activation and AP-1
RT   inhibition by nuclear receptors.";
RL   Cell 85:403-414(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=9041124;
RA   Zhu Y., Qi C., Calandra C., Rao M.S., Reddy J.K.;
RT   "Cloning and identification of mouse steroid receptor coactivator-1
RT   (mSRC-1), as a coactivator of peroxisome proliferator-activated
RT   receptor gamma.";
RL   Gene Expr. 6:185-195(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND INTERACTION WITH EP300 AND RAR.
RX   MEDLINE=97008053; PubMed=8855229; DOI=10.1073/pnas.93.20.10626;
RA   Yao T.-P., Ku G., Zhou N., Scully R., Livingston D.M.;
RT   "The nuclear hormone receptor coactivator SRC-1 is a specific target
RT   of p300.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:10626-10631(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 21-33, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   ROLE OF LXXLL MOTIFS, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP   695-HIS--LEU-698 AND 756-ARG--LEU-759.
RX   MEDLINE=97336097; PubMed=9192892; DOI=10.1038/42652;
RA   Torchia J., Rose D.W., Inostroza J., Kamei Y., Westin S., Glass C.K.,
RA   Rosenfeld M.G.;
RT   "The transcriptional co-activator p/CIP binds CBP and mediates
RT   nuclear-receptor function.";
RL   Nature 387:677-684(1997).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=9506940; DOI=10.1126/science.279.5358.1922;
RA   Xu J., Qiu Y., DeMayo F.J., Tsai S.Y., Tsai M.-J., O'Malley B.W.;
RT   "Partial hormone resistance in mice with disruption of the steroid
RT   receptor coactivator-1 (SRC-1) gene.";
RL   Science 279:1922-1925(1998).
RN   [9]
RP   INTERACTION WITH CARM1.
RX   MEDLINE=99316081; PubMed=10381882; DOI=10.1126/science.284.5423.2174;
RA   Chen D., Ma H., Hong H., Koh S.S., Huang S.-M., Schurter B.T.,
RA   Aswad D.W., Stallcup M.R.;
RT   "Regulation of transcription by a protein methyltransferase.";
RL   Science 284:2174-2177(1999).
RN   [10]
RP   FUNCTION.
RX   PubMed=12507421; DOI=10.1016/S0092-8674(02)01169-8;
RA   Picard F., Gehin M., Annicotte J.-S., Rocchi S., Champy M.-F.,
RA   O'Malley B.W., Chambon P., Auwerx J.;
RT   "SRC-1 and TIF2 control energy balance between white and brown adipose
RT   tissues.";
RL   Cell 111:931-941(2002).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 257-385 IN COMPLEX WITH
RP   STAT6.
RX   PubMed=14757047; DOI=10.1016/j.jmb.2003.12.057;
RA   Razeto A., Ramakrishnan V., Litterst C.M., Giller K., Griesinger C.,
RA   Carlomagno T., Lakomek N., Heimburg T., Lodrini M., Pfitzner E.,
RA   Becker S.;
RT   "Structure of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif
RT   of the STAT6 transactivation domain.";
RL   J. Mol. Biol. 336:319-329(2004).
CC   -!- FUNCTION: Nuclear receptor coactivator that directly binds nuclear
CC       receptors and stimulates the transcriptional activities in a
CC       hormone-dependent fashion. Involved in the coactivation of
CC       different nuclear receptors, such as for steroids (PGR, GR and
CC       ER), retinoids (RXRs), thyroid hormone (TRs) and prostanoids
CC       (PPARs). Also involved in coactivation mediated by STAT3, STAT5A,
CC       STAT5B and STAT6 transcription factors. Displays histone
CC       acetyltransferase activity toward H3 and H4; the relevance of such
CC       activity remains however unclear. Plays a central role in creating
CC       multisubunit coactivator complexes that act via remodeling of
CC       chromatin, and possibly acts by participating in both chromatin
CC       remodeling and recruitment of general transcription factors.
CC       Required with NCOA2 to control energy balance between white and
CC       brown adipose tissues. Required for mediating steroid hormone
CC       response. Isoform 2 has a higher thyroid hormone-dependent
CC       transactivation activity than isoform 1 and isoform 3.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + [histone] = CoA + acetyl-
CC       [histone].
CC   -!- SUBUNIT: Interacts with NCOA6 and NCOA2. Interacts with the FDL
CC       motif of STAT5A and STAT5B. Interacts with the LXXLL motif of
CC       STAT6. Interacts with STAT3 following IL-6 stimulation. Interacts
CC       with the basal transcription factor GTF2B. Interacts with COPS5,
CC       NR3C1, PCAF and TTLL5/STAMP. Interacts with the histone
CC       acetyltransferases EP300 and CREBBP, and the methyltransferase
CC       CARM1. Interacts with PSMB9. Interacts with UBE2L3; they
CC       functionally interact to regulate progesterone receptor
CC       transcriptional activity. Interacts with PRMT2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=SRC-1A, SRC1a;
CC         IsoId=P70365-1; Sequence=Displayed;
CC       Name=2; Synonyms=SRC-1E, SRC1e;
CC         IsoId=P70365-2; Sequence=VSP_011740;
CC       Name=3;
CC         IsoId=P70365-3; Sequence=VSP_011741;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=P70365-4; Sequence=VSP_027855, VSP_027856;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- DOMAIN: The C-terminal (1113-1447) part mediates the histone
CC       acetyltransferase (HAT) activity (By similarity).
CC   -!- DOMAIN: Contains 7 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. LXXLL
CC       motifs 3, 4 and 5 are essential for the association with nuclear
CC       receptors. LXXLL motif 7, which is not present in isoform 2,
CC       increases the affinity for steroid receptors in vitro.
CC   -!- PTM: Sumoylated; sumoylation increases its interaction with PGR
CC       and prolongs its retention in the nucleus. It does not prevent its
CC       ubiquitination and does not exert a clear effect on the stability
CC       of the protein (By similarity).
CC   -!- PTM: Ubiquitinated; leading to proteasome-mediated degradation.
CC       Ubiquitination and sumoylation take place at different sites (By
CC       similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice show partial hormone resistance: target
CC       organs such as uterus, prostate, testis and mammary gland
CC       exhibiting decreased growth and development in response to steroid
CC       hormones. Moreover, such mice are prone to obesity due to reduced
CC       energy expenditure.
CC   -!- SIMILARITY: Belongs to the SRC/p160 nuclear receptor coactivator
CC       family.
CC   -!- SIMILARITY: Contains 1 basic helix-loop-helix (bHLH) domain.
CC   -!- SIMILARITY: Contains 1 PAS (PER-ARNT-SIM) domain.
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CC   -----------------------------------------------------------------------
DR   EMBL; U56920; AAB01228.1; -; mRNA.
DR   EMBL; U64606; AAB06177.1; -; mRNA.
DR   EMBL; U64828; AAB38841.1; -; mRNA.
DR   EMBL; AK035922; BAC29244.1; -; mRNA.
DR   EMBL; BC068177; AAH68177.1; -; mRNA.
DR   EMBL; BC080866; AAH80866.1; -; mRNA.
DR   IPI; IPI00117839; -.
DR   IPI; IPI00471393; -.
DR   IPI; IPI00471395; -.
DR   IPI; IPI00857158; -.
DR   RefSeq; NP_035011.1; NM_010881.2.
DR   UniGene; Mm.301039; -.
DR   PDB; 1OJ5; X-ray; 2.20 A; A=257-385.
DR   PDB; 2O9I; X-ray; 2.80 A; C/D=686-700.
DR   PDBsum; 1OJ5; -.
DR   PDBsum; 2O9I; -.
DR   ProteinModelPortal; P70365; -.
DR   SMR; P70365; 24-83, 116-172, 259-367, 926-980.
DR   STRING; P70365; -.
DR   PhosphoSite; P70365; -.
DR   PRIDE; P70365; -.
DR   Ensembl; ENSMUST00000072464; ENSMUSP00000072285; ENSMUSG00000020647.
DR   Ensembl; ENSMUST00000085814; ENSMUSP00000082971; ENSMUSG00000020647.
DR   GeneID; 17977; -.
DR   KEGG; mmu:17977; -.
DR   UCSC; uc007mxr.1; mouse.
DR   UCSC; uc007mxs.1; mouse.
DR   CTD; 17977; -.
DR   MGI; MGI:1276523; Ncoa1.
DR   eggNOG; roNOG11578; -.
DR   GeneTree; ENSGT00530000063109; -.
DR   HOGENOM; HBG755348; -.
DR   HOVERGEN; HBG052583; -.
DR   InParanoid; P70365; -.
DR   OMA; FQGMVRQ; -.
DR   OrthoDB; EOG40K7Z6; -.
DR   PhylomeDB; P70365; -.
DR   BRENDA; 2.3.1.48; 244.
DR   NextBio; 458063; -.
DR   ArrayExpress; P70365; -.
DR   Bgee; P70365; -.
DR   CleanEx; MM_NCOA1; -.
DR   Genevestigator; P70365; -.
DR   GermOnline; ENSMUSG00000020647; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:EC.
DR   GO; GO:0035257; F:nuclear hormone receptor binding; IEA:InterPro.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0016563; F:transcription activator activity; ISS:UniProtKB.
DR   GO; GO:0003713; F:transcription coactivator activity; IEA:InterPro.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
DR   InterPro; IPR010011; DUF1518.
DR   InterPro; IPR011598; HLH_DNA-bd.
DR   InterPro; IPR001092; HLH_DNA-bd_dom.
DR   InterPro; IPR009110; Nuc_rcpt_coact.
DR   InterPro; IPR014920; Nuc_rcpt_coact_Ncoa-typ.
DR   InterPro; IPR017426; Nuclear_rcpt_coactivator.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR014935; SRC-1.
DR   InterPro; IPR008955; Src1_rcpt_coact.
DR   Gene3D; G3DSA:4.10.280.10; HLH_DNA_bd; 1.
DR   Gene3D; G3DSA:4.10.630.10; Src1_rcpt_coact; 2.
DR   Pfam; PF07469; DUF1518; 2.
DR   Pfam; PF00010; HLH; 1.
DR   Pfam; PF08815; Nuc_rec_co-act; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF08832; SRC-1; 1.
DR   PIRSF; PIRSF038181; Nuclear_receptor_coactivator; 1.
DR   SMART; SM00353; HLH; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF47459; HLH_basic; 1.
DR   SUPFAM; SSF69125; Nuc_recept_coact; 1.
DR   PROSITE; PS50888; HLH; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Acyltransferase; Alternative splicing;
KW   Direct protein sequencing; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Repeat; Transcription; Transcription regulation; Transferase;
KW   Ubl conjugation.
FT   CHAIN         1   1447       Nuclear receptor coactivator 1.
FT                                /FTId=PRO_0000094401.
FT   DOMAIN       21     81       Helix-loop-helix motif.
FT   DOMAIN      109    180       PAS.
FT   DNA_BIND     17     20       Basic motif.
FT   REGION      361    568       Interaction with STAT3.
FT   REGION      787    994       Interaction with CREBBP.
FT   MOTIF        46     50       LXXLL motif 1.
FT   MOTIF       112    116       LXXLL motif 2.
FT   MOTIF       637    641       LXXLL motif 3.
FT   MOTIF       694    698       LXXLL motif 4.
FT   MOTIF       755    759       LXXLL motif 5.
FT   MOTIF       919    923       LXXLL motif 6.
FT   MOTIF      1441   1445       LXXLL motif 7.
FT   COMPBIAS    389    686       Ser-rich.
FT   COMPBIAS   1059   1144       Gln-rich.
FT   MOD_RES      22     22       Phosphoserine.
FT   MOD_RES     103    103       Phosphoserine (By similarity).
FT   MOD_RES     372    372       Phosphoserine (By similarity).
FT   MOD_RES     395    395       Phosphoserine (By similarity).
FT   MOD_RES     518    518       Phosphoserine (By similarity).
FT   MOD_RES     570    570       Phosphoserine (By similarity).
FT   MOD_RES    1039   1039       Phosphoserine (By similarity).
FT   MOD_RES    1185   1185       Phosphothreonine (By similarity).
FT   MOD_RES    1191   1191       Phosphoserine (By similarity).
FT   CROSSLNK    738    738       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    780    780       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   VAR_SEQ    1300   1376       NVFSQAVQSQPAPAQPGVYNNMSITVSMAGGNANIQNMNPM
FT                                MGQMQMSSLQMPGMNTVCSEQMNDPALRHTGLYCNQ -> K
FT                                WKRKHSEHESNDGPDANELSADARDEYCVL (in
FT                                isoform 4).
FT                                /FTId=VSP_027855.
FT   VAR_SEQ    1377   1447       Missing (in isoform 4).
FT                                /FTId=VSP_027856.
FT   VAR_SEQ    1392   1447       QVQQVQVFADVQCTVNLVGGDPYLNQPGPLGTQKPTSGPQT
FT                                PQAQQKSLLQQLLTE -> DKKTEEFFSVVTTD (in
FT                                isoform 2).
FT                                /FTId=VSP_011740.
FT   VAR_SEQ    1392   1447       QVQQVQVFADVQCTVNLVGGDPYLNQPGPLGTQKPTSGPQT
FT                                PQAQQKSLLQQLLTE -> VSKKDNPSAELADSITLDTWRT
FT                                SHGIC (in isoform 3).
FT                                /FTId=VSP_011741.
FT   MUTAGEN     695    698       HRLL->AAAA: Abolishes the interactions
FT                                with estrogen and retinoid-acids
FT                                receptors.
FT   MUTAGEN     756    759       RYLL->AAAA: Abolishes the interactions
FT                                with estrogen and retinoid-acids
FT                                receptors.
FT   CONFLICT     45     45       E -> G (in Ref. 1; AAB01228).
FT   CONFLICT    223    223       C -> R (in Ref. 2; AAB06177).
FT   CONFLICT    234    234       E -> G (in Ref. 2; AAB06177).
FT   CONFLICT    237    237       E -> K (in Ref. 5; AAH80866).
FT   CONFLICT    465    466       SS -> TT (in Ref. 1; AAB01228).
FT   CONFLICT    699    699       Q -> P (in Ref. 2; AAB06177).
FT   CONFLICT   1115   1115       L -> M (in Ref. 4; BAC29244).
FT   CONFLICT   1130   1130       R -> K (in Ref. 1; AAB01228).
FT   CONFLICT   1137   1138       RA -> KP (in Ref. 1; AAB01228).
FT   CONFLICT   1142   1142       R -> K (in Ref. 1; AAB01228).
FT   CONFLICT   1162   1162       T -> D (in Ref. 1; AAB01228).
FT   CONFLICT   1164   1164       R -> S (in Ref. 2; AAB06177).
FT   CONFLICT   1166   1166       P -> L (in Ref. 1; AAB01228).
FT   STRAND      261    266
FT   STRAND      272    276
FT   HELIX       278    281
FT   HELIX       288    299
FT   HELIX       309    320
FT   STRAND      321    324
FT   STRAND      328    331
FT   STRAND      337    347
FT   STRAND      357    365
SQ   SEQUENCE   1447 AA;  157016 MW;  65C08AFFCF14241D CRC64;
     MSGLGDSSSD PANPDSHKRK GSPCDTLASS TEKRRREQEN KYLEELAELL SANISDIDSL
     SVKPDKCKIL KKTVDQIQLM KRMEQEKSTT DDDVQKSDIS SSSQGVIEKE SLGPLLLEAL
     DGFFFVVNCE GRIVFVSENV TSYLGYNQEE LMNTSVYSIL HVGDHAEFVK NLLPKSLVNG
     VPWPQEATRR NSHTFNCRML IHPPEDPGTE NQEACQRYEV MQCFTVSQPK SIQEDGEDFQ
     SCLICIARRL PRPPAITGVE SFMTKQDTTG KIISIDTSSL RAAGRTGWED LVRKCIYAFF
     QPQGREPSYA RQLFQEVMTR GTASSPSYRF ILNDGTMLSA HTKCKLCYPQ SPDMQPFIMG
     IHIIDREHSG LSPQDDSNSG MSIPRINPSV NPGISPAHGV TRSSTLPPSN NNMVSARVNR
     QQSSDLNSSS SHTNSSNNQG NFGCSPGNQI VANVALNQGQ AGSQSSNPSL NLNNSPMEGT
     GIALSQFMSP RRQANSGLAT RARMSNNSFP PNIPTLSSPV GITSGACNNN NRSYSNIPVT
     SLQGMNEGPN NSVGFSAGSP VLRQMSSQNS PSRLSMQPAK AESKDSKEIA SILNEMIQSD
     NSDNSANEGK PLDSGLLHNN DRLSEGDSKY SQTSHKLVQL LTTTAEQQLR HADIDTSCKD
     VLSCTGTSSS ASSNPSGGTC PSSHSSLTER HKILHRLLQE GSPSDITTLS VEPEKKDSVP
     ASTAVSVSGQ SQGSASIKLE LDAAKKKESK DHQLLRYLLD KDEKDLRSTP NLCLDDVKVK
     VEKKEQMDPC NTNPTPMTKP APEEVKLESQ SQFTADLDQF DQLLPTLEKA AQLPSLCETD
     RMDGAVTGVS IKAEVLPASL QPTTARAAPR LSRLPELELE AIDNQFGQPG AGDQIPWANN
     TLTTINQNKP EDQCISSQLD ELLCPPTTVE GRNDEKALLE QLVSFLSGKD ETELAELDRA
     LGIDKLVQGG GLDVLSERFP PQQATPPLMM EDRPTLYSQP YSSPSPTAGL SGPFQGMVRQ
     KPSLGAMPVQ VTPPRGTFSP NMGMQPRQTL NRPPAAPNQL RLQLQQRLQG QQQLMHQNRQ
     AILNQFAANA PVGMNMRSGM QQQITPQPPL NAQMLAQRQR ELYSQQHRQR QIIQQQRAML
     MRHQSFGNNI PPSSGLPVQM GTPRLPQGAP QQFPYPPNYG TNPGTPPAST SPFSQLAANP
     EASLATRSSM VNRGMAGNMG GQFGAGISPQ MQQNVFQYPG PGLVPQGEAT FAPSLSPGSS
     MVPMPVPPPQ SSLLQQTPPT SGYQSPDMKA WQQGTMGNNN VFSQAVQSQP APAQPGVYNN
     MSITVSMAGG NANIQNMNPM MGQMQMSSLQ MPGMNTVCSE QMNDPALRHT GLYCNQLSST
     DLLKTDADGN QQVQQVQVFA DVQCTVNLVG GDPYLNQPGP LGTQKPTSGP QTPQAQQKSL
     LQQLLTE
//
ID   ELAV1_MOUSE             Reviewed;         326 AA.
AC   P70372; Q60745;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=ELAV-like protein 1;
DE   AltName: Full=Elav-like generic protein;
DE   AltName: Full=Hu-antigen R;
DE            Short=HuR;
DE   AltName: Full=MelG;
GN   Name=Elavl1; Synonyms=Elra, Hua;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain, and Spleen;
RX   MEDLINE=98438560; PubMed=9763509;
RA   Atasoy U., Watson J., Patel D., Keene J.D.;
RT   "ELAV protein HuA (HuR) can redistribute between nucleus and cytoplasm
RT   and is upregulated during serum stimulation and T cell activation.";
RL   J. Cell Sci. 111:3145-3156(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 119-292.
RC   TISSUE=Brain;
RX   MEDLINE=95273402; PubMed=7753842; DOI=10.1073/pnas.92.10.4557;
RA   Good P.J.;
RT   "A conserved family of elav-like genes in vertebrates.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:4557-4561(1995).
RN   [3]
RP   METHYLATION AT ARG-217.
RX   PubMed=12237300; DOI=10.1074/jbc.M206187200;
RA   Li H., Park S., Kilburn B., Jelinek M.A., Henschen-Edman A.,
RA   Aswad D.W., Stallcup M.R., Laird-Offringa I.A.;
RT   "Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing
RT   protein, by CARM1. Coactivator-associated arginine
RT   methyltransferase.";
RL   J. Biol. Chem. 277:44623-44630(2002).
CC   -!- FUNCTION: Binds avidly to the AU-rich element in FOS and
CC       IL3/interleukin-3 mRNAs. In the case of the FOS AU-rich element,
CC       HUR binds to a core element of 27 nucleotides that contain AUUUA,
CC       AUUUUA, and AUUUUUA motifs (By similarity).
CC   -!- SUBUNIT: Identified in a mRNP complex, at least composed of DHX9,
CC       DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1,
CC       STAU2, SYNCRIP and YBX1. Interacts with ANP32A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- PTM: Methylated at Arg-217 by CARM1 in T-cells in response to LPS
CC       challenge.
CC   -!- SIMILARITY: Belongs to the RRM elav family.
CC   -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.
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DR   EMBL; U65735; AAB17967.1; -; mRNA.
DR   EMBL; U17595; AAA96941.1; -; mRNA.
DR   IPI; IPI00108271; -.
DR   PIR; I49144; I49144.
DR   UniGene; Mm.119162; -.
DR   ProteinModelPortal; P70372; -.
DR   SMR; P70372; 18-184, 241-325.
DR   DIP; DIP-46480N; -.
DR   MINT; MINT-4094207; -.
DR   STRING; P70372; -.
DR   PhosphoSite; P70372; -.
DR   PRIDE; P70372; -.
DR   Ensembl; ENSMUST00000098950; ENSMUSP00000096549; ENSMUSG00000040028.
DR   Ensembl; ENSMUST00000116496; ENSMUSP00000112196; ENSMUSG00000040028.
DR   MGI; MGI:1100851; Elavl1.
DR   eggNOG; roNOG13337; -.
DR   HOGENOM; HBG756718; -.
DR   HOVERGEN; HBG002295; -.
DR   InParanoid; P70372; -.
DR   OrthoDB; EOG4Z8XWZ; -.
DR   PhylomeDB; P70372; -.
DR   ArrayExpress; P70372; -.
DR   Bgee; P70372; -.
DR   Genevestigator; P70372; -.
DR   GermOnline; ENSMUSG00000040028; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0070935; P:3'-UTR-mediated mRNA stabilization; ISS:UniProtKB.
DR   InterPro; IPR006548; ELAD_HUD_SF.
DR   InterPro; IPR002343; Hud_Sxl_RNA.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 3.
DR   Pfam; PF00076; RRM_1; 3.
DR   PRINTS; PR00961; HUDSXLRNA.
DR   SMART; SM00360; RRM; 3.
DR   TIGRFAMs; TIGR01661; ELAV_HUD_SF; 1.
DR   PROSITE; PS50102; RRM; 3.
PE   1: Evidence at protein level;
KW   Cytoplasm; Methylation; Phosphoprotein; Repeat; RNA-binding.
FT   CHAIN         1    326       ELAV-like protein 1.
FT                                /FTId=PRO_0000081578.
FT   DOMAIN       20     98       RRM 1.
FT   DOMAIN      106    186       RRM 2.
FT   DOMAIN      244    322       RRM 3.
FT   MOD_RES     202    202       Phosphoserine (By similarity).
FT   MOD_RES     217    217       Omega-N-methylated arginine; by CARM1.
SQ   SEQUENCE   326 AA;  36069 MW;  F3483C5AFC029C22 CRC64;
     MSGGYEDHMA EDCRGDIGRT NLIVNYLPQN MTQEELRSLF SSIGEVESAK LIRDKVAGHS
     LGYGFVNYVT AKDAERAIST LNGLRLQSKT IKVSYARPSS EVIKDANLYI SGLPRTMTQK
     DVEDMFSRFG RIINSRVLVD QTTGLSRGVA FIRFDKRSEA EEAITSFIGH KPPGSSEPIT
     VKFAANPNQN KNMALLSQLY HSPARRFGGP VHHQAQRFRF SPMGVDHMSG ISGVNVPGNA
     SSGWCIFIYN LGQDADEGIL WQMFGPFGAV TNVKVIRDFN TNKCKGFGFV TMTNYEESAM
     AIASLNGYRL GDKILQVSFK TNKSHK
//
ID   RGRF2_MOUSE             Reviewed;        1189 AA.
AC   P70392; Q3TYN3; Q9QX51;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 2.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Ras-specific guanine nucleotide-releasing factor 2;
DE            Short=Ras-GRF2;
DE   AltName: Full=Ras guanine nucleotide exchange factor 2;
GN   Name=Rasgrf2; Synonyms=Grf2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RAS AND
RP   CALMODULIN, AND SUBCELLULAR LOCATION.
RC   TISSUE=Brain;
RX   MEDLINE=97184464; PubMed=9032266;
RA   Fam N.P., Fan W.-T., Wang Z., Zhang L.-J., Chen H., Moran M.F.;
RT   "Cloning and characterization of Ras-GRF2, a novel guanine nucleotide
RT   exchange factor for Ras.";
RL   Mol. Cell. Biol. 17:1396-1406(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF 464-474 AND 723-734, PHOSPHORYLATION,
RP   UBIQUITINATION, AND MUTAGENESIS OF ARG-1022 AND ARG-1092.
RX   PubMed=11238945; DOI=10.1128/MCB.21.6.2107-2117.2001;
RA   de Hoog C.L., Koehler J.A., Goldstein M.D., Taylor P., Figeys D.,
RA   Moran M.F.;
RT   "Ras binding triggers ubiquitination of the Ras exchange factor Ras-
RT   GRF2.";
RL   Mol. Cell. Biol. 21:2107-2117(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 922-1189, DISRUPTION PHENOTYPE,
RP   AND TISSUE SPECIFICITY.
RX   MEDLINE=21907213; PubMed=11909944;
RX   DOI=10.1128/MCB.22.8.2498-2504.2002;
RA   Fernandez-Medarde A., Esteban L.M., Nunez A., Porteros A.,
RA   Tessarollo L., Santos E.;
RT   "Targeted disruption of Ras-Grf2 shows its dispensability for mouse
RT   growth and development.";
RL   Mol. Cell. Biol. 22:2498-2504(2002).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH RAS AND RAC1.
RX   PubMed=9707409; DOI=10.1016/S0960-9822(07)00376-4;
RA   Fan W.-T., Koch C.A., de Hoog C.L., Fam N.P., Moran M.F.;
RT   "The exchange factor Ras-GRF2 activates Ras-dependent and Rac-
RT   dependent mitogen-activated protein kinase pathways.";
RL   Curr. Biol. 8:935-938(1998).
RN   [6]
RP   INTERACTION WITH RASGRF1.
RX   MEDLINE=99303753; PubMed=10373510;
RA   Anborgh P.H., Qian X., Papageorge A.G., Vass W.C., DeClue J.E.,
RA   Lowy D.R.;
RT   "Ras-specific exchange factor GRF: oligomerization through its Dbl
RT   homology domain and calcium-dependent activation of Raf.";
RL   Mol. Cell. Biol. 19:4611-4622(1999).
RN   [7]
RP   FUNCTION.
RX   PubMed=10733575; DOI=10.1128/MCB.20.8.2727-2733.2000;
RA   de Hoog C.L., Fan W.-T., Goldstein M.D., Moran M.F., Koch C.A.;
RT   "Calmodulin-independent coordination of Ras and extracellular signal-
RT   regulated kinase activation by Ras-GRF2.";
RL   Mol. Cell. Biol. 20:2727-2733(2000).
RN   [8]
RP   FUNCTION.
RX   PubMed=11500499; DOI=10.1074/jbc.M104658200;
RA   Gotoh T., Tian X., Feig L.A.;
RT   "Prenylation of target GTPases contributes to signaling specificity of
RT   Ras-guanine nucleotide exchange factors.";
RL   J. Biol. Chem. 276:38029-38035(2001).
RN   [9]
RP   INTERACTION WITH EPB49.
RX   PubMed=11856323; DOI=10.1046/j.0014-2956.2001.02694.x;
RA   Lutchman M., Kim A.C., Cheng L., Whitehead I.P., Oh S.S., Hanspal M.,
RA   Boukharov A.A., Hanada T., Chishti A.H.;
RT   "Dematin interacts with the Ras-guanine nucleotide exchange factor
RT   Ras-GRF2 and modulates mitogen-activated protein kinase pathways.";
RL   Eur. J. Biochem. 269:638-649(2002).
RN   [10]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX   PubMed=15029245; DOI=10.1038/sj.emboj.7600151;
RA   Tian X., Gotoh T., Tsuji K., Lo E.H., Huang S., Feig L.A.;
RT   "Developmentally regulated role for Ras-GRFs in coupling NMDA
RT   glutamate receptors to Ras, Erk and CREB.";
RL   EMBO J. 23:1567-1575(2004).
RN   [11]
RP   PHOSPHORYLATION BY CDK5.
RX   PubMed=15128856; DOI=10.1523/JNEUROSCI.0690-04.2004;
RA   Kesavapany S., Amin N., Zheng Y.-L., Nijhara R., Jaffe H., Sihag R.,
RA   Gutkind J.S., Takahashi S., Kulkarni A., Grant P., Pant H.C.;
RT   "p35/cyclin-dependent kinase 5 phosphorylation of ras guanine
RT   nucleotide releasing factor 2 (RasGRF2) mediates Rac-dependent
RT   extracellular signal-regulated kinase 1/2 activity, altering RasGRF2
RT   and microtubule-associated protein 1b distribution in neurons.";
RL   J. Neurosci. 24:4421-4431(2004).
RN   [12]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=14749369; DOI=10.1128/MCB.24.4.1516-1530.2004;
RA   Arozarena I., Matallanas D., Berciano M.T., Sanz-Moreno V., Calvo F.,
RA   Munoz M.T., Egea G., Lafarga M., Crespo P.;
RT   "Activation of H-Ras in the endoplasmic reticulum by the RasGRF family
RT   guanine nucleotide exchange factors.";
RL   Mol. Cell. Biol. 24:1516-1530(2004).
RN   [13]
RP   INTERACTION WITH MICROTUBULES.
RX   PubMed=16649990; DOI=10.1111/j.1742-4658.2006.05226.x;
RA   Forlani G., Baldassa S., Lavagni P., Sturani E., Zippel R.;
RT   "The guanine nucleotide exchange factor RasGRF1 directly binds
RT   microtubules via DHPH2-mediated interaction.";
RL   FEBS J. 273:2127-2138(2006).
RN   [14]
RP   FUNCTION, AND INTERACTION WITH GRIA1.
RX   PubMed=16407208; DOI=10.1074/jbc.M512060200;
RA   Tian X., Feig L.A.;
RT   "Age-dependent participation of Ras-GRF proteins in coupling calcium-
RT   permeable AMPA glutamate receptors to Ras/Erk signaling in cortical
RT   neurons.";
RL   J. Biol. Chem. 281:7578-7582(2006).
RN   [15]
RP   FUNCTION.
RX   PubMed=16467520; DOI=10.1523/JNEUROSCI.3990-05.2006;
RA   Li S., Tian X., Hartley D.M., Feig L.A.;
RT   "Distinct roles for Ras-guanine nucleotide-releasing factor 1 (Ras-
RT   GRF1) and Ras-GRF2 in the induction of long-term potentiation and
RT   long-term depression.";
RL   J. Neurosci. 26:1721-1729(2006).
CC   -!- FUNCTION: Functions as a calcium-regulated nucleotide exchange
CC       factor activating both Ras and RAC1 through the exchange of bound
CC       GDP for GTP. Preferentially activates HRAS in vivo compared to
CC       RRAS based on their different types of prenylation. Functions in
CC       synaptic plasticity by contributing to the induction of long term
CC       potentiation.
CC   -!- SUBUNIT: Homooligomer and heterooligomer with RASGRF1. Interacts
CC       with Ras and RAC1. Interacts in a calcium-dependent manner with
CC       calmodulin. Interacts with EPB49 and probably CDK5R1. Interacts
CC       with the AMPA receptor through GRIA1. Interacts with microtubules.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral
CC       membrane protein. Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Note=Translocates to membranes when activated.
CC       Found both at cell periphery and along the axon of neurons (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in brain in the nucleus of the
CC       solitary tract. Not observed in the hippocampus (at protein
CC       level).
CC   -!- DEVELOPMENTAL STAGE: Expression increases in the cortex from birth
CC       to adulthood.
CC   -!- DOMAIN: The Ras-GEF domain and the N-terminal Ras-GEF domain form
CC       a Ras-binding site and mediate Ras activation (By similarity).
CC   -!- DOMAIN: The IQ domain mediates the calcium-dependent interaction
CC       with calmodulin but is dispensable for the Ras-GEF activity.
CC   -!- DOMAIN: The DH (DBL-homology) domain mediates interaction with
CC       RASGRF1 and probably EPB49 and is required for RAC1 activation.
CC   -!- PTM: Phosphorylated by CDK5; down-regulates RASGRF2-mediated RAC1
CC       activation.
CC   -!- PTM: Ubiquitinated upon interaction with Ras. Ubiquitination leads
CC       to degradation through the 26S proteasome.
CC   -!- DISRUPTION PHENOTYPE: Mice do not display overt phenotype.
CC   -!- MISCELLANEOUS: Preferentially activates HRAS in vivo compared to
CC       R-RAS based on their different types of prenylation.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 IQ domain.
CC   -!- SIMILARITY: Contains 1 N-terminal Ras-GEF domain.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -!- SIMILARITY: Contains 1 Ras-GEF domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U67326; AAC53058.2; -; mRNA.
DR   EMBL; AK158472; BAE34529.1; -; mRNA.
DR   EMBL; AF109312; AAF18297.1; -; Genomic_DNA.
DR   EMBL; AF109309; AAF18297.1; JOINED; Genomic_DNA.
DR   EMBL; AF109310; AAF18297.1; JOINED; Genomic_DNA.
DR   EMBL; AF109311; AAF18297.1; JOINED; Genomic_DNA.
DR   IPI; IPI00108372; -.
DR   PIR; T42726; T42726.
DR   RefSeq; NP_033053.2; NM_009027.3.
DR   UniGene; Mm.248630; -.
DR   HSSP; Q07889; 1XD2.
DR   ProteinModelPortal; P70392; -.
DR   SMR; P70392; 24-131, 240-427, 551-588, 954-1186.
DR   IntAct; P70392; 3.
DR   STRING; P70392; -.
DR   PhosphoSite; P70392; -.
DR   PRIDE; P70392; -.
DR   Ensembl; ENSMUST00000151408; ENSMUSP00000116892; ENSMUSG00000021708.
DR   GeneID; 19418; -.
DR   KEGG; mmu:19418; -.
DR   UCSC; uc007rke.1; mouse.
DR   CTD; 19418; -.
DR   MGI; MGI:109137; Rasgrf2.
DR   eggNOG; roNOG14601; -.
DR   GeneTree; ENSGT00600000084163; -.
DR   HOVERGEN; HBG005208; -.
DR   InParanoid; P70392; -.
DR   NextBio; 296559; -.
DR   ArrayExpress; P70392; -.
DR   Bgee; P70392; -.
DR   Genevestigator; P70392; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR   InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR   InterPro; IPR008937; Ras_GEF.
DR   InterPro; IPR001895; RasGRF_CDC25.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Gene3D; G3DSA:1.10.840.10; RasGRF_CDC25; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   PANTHER; PTHR23113; Ras_GEF; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00015; IQ; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00229; RasGEFN; 2.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   PROSITE; PS00741; DH_1; FALSE_NEG.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS00720; RASGEF; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50212; RASGEF_NTER; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell membrane; Coiled coil; Cytoplasm;
KW   Direct protein sequencing; Endoplasmic reticulum;
KW   Guanine-nucleotide releasing factor; Membrane; Phosphoprotein; Repeat;
KW   Ubl conjugation.
FT   CHAIN         1   1189       Ras-specific guanine nucleotide-releasing
FT                                factor 2.
FT                                /FTId=PRO_0000312864.
FT   DOMAIN       22    133       PH 1.
FT   DOMAIN      205    234       IQ.
FT   DOMAIN      243    429       DH.
FT   DOMAIN      470    588       PH 2.
FT   DOMAIN      635    755       N-terminal Ras-GEF.
FT   DOMAIN      954   1186       Ras-GEF.
FT   REGION      743    751       Regulates proteasomal degradation.
FT   REGION     1051   1080       Responsible of the affinity for
FT                                farnesylated versus geranylgeranylated
FT                                Ras.
FT   COILED      158    193       Potential.
FT   MOD_RES     736    736       Phosphoserine; by CDK5 (By similarity).
FT   MUTAGEN    1022   1022       R->E: Loss of interaction with Ras. Loss
FT                                of Ras activation. Loss of
FT                                ubiquitination.
FT   MUTAGEN    1092   1092       R->E: Partial loss of interaction with
FT                                Ras. Partial loss of Ras activation.
FT                                Partial loss of ubiquitination.
FT   CONFLICT   1023   1023       A -> P (in Ref. 4; AAF18297).
FT   CONFLICT   1056   1056       A -> P (in Ref. 4; AAF18297).
FT   CONFLICT   1061   1061       K -> R (in Ref. 2; BAE34529).
FT   CONFLICT   1076   1076       D -> N (in Ref. 2; BAE34529).
SQ   SEQUENCE   1189 AA;  135668 MW;  42E346B623F18E59 CRC64;
     MQKSVRYNEG HALYLAMLAR KEGTKRGFLS KKAAEASRWH EKWFALYQNV LFYFEGEQSG
     RPAGMYLLEG CSCERTPAPP RTNAGPAGAR DALDKQYYFT VLFGHDGQKP LELRCEEEQA
     GKEWMEAIHQ ASYADILIER EVLMQKYIHL VQIVETEKIA TNQLRHQLED QDTEIERLKS
     EIVALNKTKE RMRPYHVHQE EEDPDIKKIK KVQSFMRGWL CRRKWKTIVQ DYICSPHAES
     MRKRNQIVFT MVEAETEYVH QLYILVNGFL RPLRMAASSK KPPINHDDVS SIFLNSETIM
     FLHEIFHQGL KARLANWPTL VLADLFDILL PMLNIYQEFV RNHQYSLQVL ANCKQNRDFD
     KLLKQYEANP ACEGRMLETF LTYPMFQIPR YIITLHELLA HTPHEHVERK SLEFAKSKLE
     ELSRVMHDEV SDTENIRKNL AIERMIVEGC DILLDTSQTF IRQGSLIQVP SVERGKLSKV
     RLGSLSLKKE GERQCFLFTK HFLICTRSSG GKLHLLKTGG VLSLIQCTLI EEPDGSDDDP
     KGSGHMFGHL DFKIVVEPPD AASFTVVLLA PSRQEKAAWM SDISQCVDNI RCNGLMTIVF
     EENSKVTVPH MIKSDARLHK DDTDICFSKT LNSCKVPQIR YASVERLLER LTDLRFLSID
     FLNTFLHTYR IFTTATVVLA KLSDIYKRPF TSIPVRSLEL FFATSQNNRE HLVDGKSPRL
     CRKFSSPPPL AVSRTSSPVR ARKLSLTSSL NSRIGALDLT NSSSSSSPTT TTHSPAASPP
     PHTAVLESAP ADKAGDSADM SPCRSPTTPR HLRYRQPGGQ VADSAHCSVS PASAFAIATA
     AAGHGSPPGF NNERTCDKEF IIRRTATNRV LNVLRHWVSK HAQDFELNNE LKMNVLNLLE
     EVLRDPDLLP QERKATANIL RALSQDDQDD IHLKLEDIIQ MTDCPKAECF ETLSAMELAE
     QITLLDHIVF RSIPYEEFLG QGWMKLDKNE RTPYIMKTSQ HFNEMSNLVA SQIMNYADIS
     SRANAIEKWV AVADICRCLH NYNGVLEITS ALNRSAIYRL KKTWAKVSKQ TKALMDKLQK
     TVSSEGRFKN LRETLKNCNP PAVPYLGMYL TDLAFIEEGT PNFTEEGLVN FSKMRMISHI
     IREIRQFQQT AYRIDQQPKV IQYLLDKALV IDEDSLYELS LKIEPRLPA
//
ID   DLX6_MOUSE              Reviewed;         175 AA.
AC   P70397; A0AUM1; A5HKN2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 3.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Homeobox protein DLX-6;
GN   Name=Dlx6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Femur;
RX   PubMed=18280462; DOI=10.1016/j.ydbio.2008.01.001;
RA   Li H., Marijanovic I., Kronenberg M.S., Erceg I., Stover M.L.,
RA   Velonis D., Mina M., Heinrich J.G., Harris S.E., Upholt W.B.,
RA   Kalajzic I., Lichtler A.C.;
RT   "Expression and function of Dlx genes in the osteoblast lineage.";
RL   Dev. Biol. 316:458-470(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Branchial arch region;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-175 (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 18-175 (ISOFORM 1).
RC   TISSUE=Branchial arch region;
RX   MEDLINE=98075915; PubMed=9415433;
RX   DOI=10.1002/(SICI)1097-0177(199712)210:4<498::AID-AJA12>3.0.CO;2-3;
RA   Liu J.K., Ghattas I., Liu S., Chen S., Rubenstein J.L.R.;
RT   "Dlx genes encode DNA-binding proteins that are expressed in an
RT   overlapping and sequential pattern during basal ganglia
RT   differentiation.";
RL   Dev. Dyn. 210:498-512(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 53-175 (ISOFORM 1).
RC   STRAIN=Swiss Webster; TISSUE=Embryo;
RX   MEDLINE=97008096; PubMed=8855272; DOI=10.1073/pnas.93.20.10858;
RA   Stock D.W., Ellies D.L., Zhao Z., Ekker M., Ruddle F.H., Weiss K.M.;
RT   "The evolution of the vertebrate Dlx gene family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:10858-10863(1996).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P70397-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P70397-2; Sequence=VSP_040733;
CC   -!- SIMILARITY: Belongs to the distal-less homeobox family.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; EF535989; ABQ10645.1; -; mRNA.
DR   EMBL; AC122240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC114342; AAI14343.1; -; mRNA.
DR   EMBL; AF022078; AAB94583.1; -; mRNA.
DR   EMBL; U67841; AAC52844.1; -; mRNA.
DR   IPI; IPI00970646; -.
DR   RefSeq; NP_034187.1; NM_010057.2.
DR   UniGene; Mm.439763; -.
DR   ProteinModelPortal; P70397; -.
DR   SMR; P70397; 46-106.
DR   STRING; P70397; -.
DR   PRIDE; P70397; -.
DR   Ensembl; ENSMUST00000031768; ENSMUSP00000031768; ENSMUSG00000029754.
DR   Ensembl; ENSMUST00000160937; ENSMUSP00000124204; ENSMUSG00000029754.
DR   GeneID; 13396; -.
DR   MGI; MGI:101927; Dlx6.
DR   eggNOG; roNOG09568; -.
DR   GeneTree; ENSGT00590000082824; -.
DR   HOVERGEN; HBG005493; -.
DR   InParanoid; P70397; -.
DR   OrthoDB; EOG4QJRP4; -.
DR   ArrayExpress; P70397; -.
DR   Bgee; P70397; -.
DR   CleanEx; MM_DLX6; -.
DR   Genevestigator; P70397; -.
DR   GermOnline; ENSMUSG00000029754; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0030528; F:transcription regulator activity; IEA:InterPro.
DR   GO; GO:0048646; P:anatomical structure formation involved in morphogenesis; IGI:MGI.
DR   GO; GO:0030326; P:embryonic limb morphogenesis; IGI:MGI.
DR   GO; GO:0030855; P:epithelial cell differentiation; IGI:MGI.
DR   GO; GO:0042472; P:inner ear morphogenesis; IGI:MGI.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IGI:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR001356; Homeobox.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR020479; Homeobox_eu.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR000047; HTH_lambrepressr.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Pfam; PF00046; Homeobox; 1.
DR   PRINTS; PR00024; HOMEOBOX.
DR   PRINTS; PR00031; HTHREPRESSR.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Developmental protein; DNA-binding; Homeobox;
KW   Nucleus.
FT   CHAIN        18    175       Homeobox protein DLX-6.
FT                                /FTId=PRO_0000049035.
FT   DNA_BIND     49    108       Homeobox.
FT   VAR_SEQ       1      1       M -> MMTMTTMADGLEGQDSSKSAFMEFGQQQQQQQQQQQ
FT                                QQQQQQQQQQQPPPPPPPPPPQPHSQQTSPAMAGAHYPLHC
FT                                LHSAAAAAAAAGSHHHHHQHHHHGSPYASSGGNSYNHRSLA
FT                                AYPYM (in isoform 2).
FT                                /FTId=VSP_040733.
SQ   SEQUENCE   175 AA;  19677 MW;  55542638D7E0CA42 CRC64;
     MSHSQHSPYL QSYHNSSAAA QTRGDDTDQQ KTTVIENGEI RFNGKGKKIR KPRTIYSSLQ
     LQALNHRFQQ TQYLALPERA ELAASLGLTQ TQVKIWFQNK RSKFKKLLKQ GSNPHESDPL
     PGSAALSPRS PALPPVWDVS ASAKGVSMPP NSYMPGYSHW YSSPHQDTMQ RPQMM
//
ID   USP9X_MOUSE             Reviewed;        2559 AA.
AC   P70398; Q62497;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase FAF-X;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme FAF-X;
DE   AltName: Full=Fat facets homolog;
DE   AltName: Full=Fat facets protein-related, X-linked;
DE   AltName: Full=Ubiquitin carboxyl-terminal hydrolase FAM;
DE   AltName: Full=Ubiquitin thiolesterase FAF-X;
DE   AltName: Full=Ubiquitin-specific protease 9, X chromosome;
DE   AltName: Full=Ubiquitin-specific-processing protease FAF-X;
GN   Name=Usp9x; Synonyms=Fafl, Fam;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=97321544; PubMed=9178254; DOI=10.1016/S0925-4773(97)00672-2;
RA   Wood S.A., Pascoe W.S., Ru K., Yamada T., Hirchenhain J., Kemler R.,
RA   Mattick J.S.;
RT   "Cloning and expression analysis of a novel mouse gene with sequence
RT   similarity to the Drosophila fat facets gene.";
RL   Mech. Dev. 63:29-38(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 152-240.
RC   TISSUE=Cochlea;
RX   MEDLINE=97237053; PubMed=9119401; DOI=10.1006/geno.1996.4526;
RA   Crozet F., El-Amraoui A., Blanchard S., Lenoir M., Ripoll C., Vago P.,
RA   Hamel C., Fizames C., Levi-Acobas F., Depetris D., Mattei M.-G.,
RA   Weil D., Pujol R., Petit C.;
RT   "Cloning of the genes encoding two murine and human cochlear
RT   unconventional type I myosins.";
RL   Genomics 40:332-341(1997).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1815 AND TYR-2540, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Deubiquitinase involved both in the processing of
CC       ubiquitin precursors and of ubiquitinated proteins. May therefore
CC       play an important role regulatory role at the level of protein
CC       turnover by preventing degradation of proteins through the removal
CC       of conjugated ubiquitin. Essential component of TGF-beta/BMP
CC       signaling cascade. Regulates chromosome alignment and segregation
CC       in mitosis by regulating the localization of BIRC5/survivin to
CC       mitotic centromeres. Specifically hydrolyzes both 'Lys-29'- and
CC       'Lys-33'-linked polyubiquitins chains. Specifically
CC       deubiquitinates monoubiquitinated SMAD4, opposing the activity of
CC       E3 ubiquitin-protein ligase TRIM33 (By similarity).
CC   -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- SUBUNIT: Interacts with SMAD4, MARK4, NUAK1 and BIRC5/survivin (By
CC       similarity).
CC   -!- INTERACTION:
CC       Q13485:SMAD4 (xeno); NbExp=4; IntAct=EBI-2214043, EBI-347263;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed in adult tissues.
CC   -!- DEVELOPMENTAL STAGE: At least expressed from 17 dpc to 21
CC       postnatal days.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
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DR   EMBL; U67874; AAB07731.1; -; mRNA.
DR   EMBL; Z78153; CAB01555.1; -; mRNA.
DR   IPI; IPI00108388; -.
DR   PIR; T30850; T30850.
DR   RefSeq; NP_033507.2; NM_009481.2.
DR   UniGene; Mm.242646; -.
DR   ProteinModelPortal; P70398; -.
DR   SMR; P70398; 1546-1956.
DR   IntAct; P70398; 7.
DR   STRING; P70398; -.
DR   MEROPS; C19.017; -.
DR   PhosphoSite; P70398; -.
DR   PRIDE; P70398; -.
DR   Ensembl; ENSMUST00000115466; ENSMUSP00000111126; ENSMUSG00000031010.
DR   GeneID; 22284; -.
DR   KEGG; mmu:22284; -.
DR   CTD; 22284; -.
DR   MGI; MGI:894681; Usp9x.
DR   HOGENOM; HBG358333; -.
DR   HOVERGEN; HBG073749; -.
DR   InParanoid; P70398; -.
DR   OrthoDB; EOG46HG8S; -.
DR   BRENDA; 3.1.2.15; 244.
DR   ArrayExpress; P70398; -.
DR   Bgee; P70398; -.
DR   CleanEx; MM_USP9X; -.
DR   Genevestigator; P70398; -.
DR   GermOnline; ENSMUSG00000031010; Mus musculus.
DR   GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0070410; F:co-SMAD binding; ISS:BHF-UCL.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:EC.
DR   GO; GO:0030509; P:BMP signaling pathway; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 6.
DR   Pfam; PF00443; UCH; 1.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; 1.
DR   PROSITE; PS50235; UCH_2_3; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Chromosome partition; Cytoplasm; Hydrolase;
KW   Mitosis; Phosphoprotein; Protease; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN         1   2559       Probable ubiquitin carboxyl-terminal
FT                                hydrolase FAF-X.
FT                                /FTId=PRO_0000080691.
FT   ACT_SITE   1566   1566       Nucleophile (By similarity).
FT   ACT_SITE   1879   1879       Proton acceptor (By similarity).
FT   MOD_RES    1600   1600       Phosphoserine.
FT   MOD_RES    1815   1815       Phosphotyrosine.
FT   MOD_RES    2443   2443       Phosphoserine (By similarity).
FT   MOD_RES    2540   2540       Phosphotyrosine.
FT   MOD_RES    2547   2547       Phosphoserine (By similarity).
FT   CONFLICT    182    182       C -> F (in Ref. 2; CAB01555).
SQ   SEQUENCE   2559 AA;  290545 MW;  9BDF964A142AFB5D CRC64;
     MTATTRGSPV GGNDNQGQAP DGQSQPPLQQ NQTSSPDSSN ENSPATPPDE QGQGDAPPQI
     EDEEPAFPHT DLPKLDDMIN RPRWVVPVLP KGELEVLLEA AIDLSKKGLD VKSEACQRFF
     RDGLTISFTK ILTDEAVSGW KFEIHRCIIN NTHRLVELCV AKLAQDWFPL LELLAMALNP
     HCKFHIYNGT RPCESVSSSV QLPEDELFAR SPDPRSPKGW LVDLLNKFGT LNGFQILHDR
     FINGSALNVQ IIAALIKPFG QCYEFLTLHT VKKYFLPIIE MVPQFLENLT DEELKKEAKN
     EAKNDALSMI IKSLKNLASR VPGQEETVKN LEIFRLKMIL RLLQISSFNG KMNALNEVNK
     VISSVSYYTH RHGSSEDEEW LTAERMAEWI QQNNILSIVL RDSLHQPQYV EKLEKILRFV
     IKEKALTLQD LDNIWAAQAG KHEAIVKNVH DLLAKLAWDF SPEQLDHLFD CFKASWTNAS
     KKQREKLLEL IRRLAEDDKD GVMAHKVLNL LWNLAHSDDV PVDIMDLALS AHIKILDYSC
     SQDRDTQKIQ WIDRFIEELR TNDKWVIPAL KQIREICSLF GEAPQNLSQS QRSPHVFYRH
     DLINQLQHNH ALVTLVAENL ATYMESMRMY GRDNEDYDPQ TVRLGSRYSH VQEVQERLNF
     LRFLLKDGQL WLCAPQAKQI WKCLAENAVY LCDREACFKW YSKLMGDEPD LDPDINKDFF
     ESNVLQLDPS LLTENGMKCF ERFFKAVNCR EGKLVAKRRA YMMDDLELIG LDYLWRVVIQ
     SNDDIACRAI DLLKEIYTNL GPRLQVNQVV IHEDFIQSCF DRLKASYDTL CVLDGDKDSI
     NCARQEAVRM VRVLTVLREY INECDSDYHE ERTILPMSRA FRGKHLSFIV RFPNQGRQVD
     DLEVWSHTND TIGSVRRCIL NRIKANVAHT KIELFVGGEL IDPGDDRKLI GQLNLKDKSL
     ITAKLTQISS NMPSSPDSSS DSSTGSPGNH GNHYSDGPNP EVESCLPGVI MSLHPRYISF
     LWQVADLGSS LNMPPLRDGA RVLMKLMPPD STTIEKLRAI CLDHAKLGES SLSPSLDSLF
     FGPSASQVLY LTEVVYALLM PAGAPLTDDS SDFQFHFLKS GGLPLVLSML TRNNFLPNAD
     METRRGAYLN ALKIAKLLLT AIGYGHVRAV AEACQPGVEG VNPMTSVNQV THDQAVVLQS
     ALQSIPNPSS ECMLRNVSVR LAQQISDEAS RYMPDICVIR AIHQIIWTSG CGGLQLVFSP
     NEEVTKIYEK TNAGNEPDLE DEQVCCEALE VMTLCFALIP TALDALSKEK AWQTFIIDLL
     LHCHSKTVRQ VAQEQFFLMC TRCCMGHRPL LFFITLLFTV LGSTARERAK HSGDYFTLLR
     HLLNYAYNSN INVPNAEVLL NNEIDWLKRI RDDVKRTGET GVEETILEGH LGVTKELLAF
     QTPEKKFHIG CEKGGANLIK ELIDDFIFPA SNVYLQYMRN GELPAEQAIP VCGSPATINA
     GFELLVALAV GCVRNLKQIV DSLTEMYYIG TAITTCEALT EWEYLPPVGP RPPKGFVGLK
     NAGATCYMNS VIQQLYMIPS IRNGILAIEG TGSDVDDDMS GDEKQDNESN VDPRDDVFGY
     PQQFENKPPL IKTENRKKYN IGVLKHLQVI FGHLAASRLQ YYVPKGFWKQ SRLWGEPVNL
     REQHDALKSF NSLVDSLDEA LKALGHPAML SKVLGGSFAD QKICQGCPHR YECEESFTTL
     NVDIRNHQNL LDSLEQYVKG DLLEGANAYH CEKCNKKVDT VKRLLIKKLP PVLAIQLKRF
     DYDWERECAI KFNDYFEFPR ELDMEPYTVA GVAKLEGDNV NPESQLIQQN EQSESEKAGS
     TKYRLVGVLV HSGQASGGHY YSYIIQRNGG DGEKNRWYKF DDGDVTECKM DDDEEMKTQC
     FGGEYMGEVL DHMMKRMSYR RQKRWWNAYI LFYERMDTIG HDDEVIRYIS EIAITTRPHQ
     IVMPSAIERS VRKQNVQFMH NRMQYSLEYF QFMKKLLTCN GVYLNPPPGQ DHLSPEAEEI
     TMISIQLAAR FLFTTGFHTK KIVRGSASDW YDALCILLRH SKNVRFWFAH NVLFNVSNRF
     SEYLLECPSA EVRGAFAKLI VFIAHFSLQD GPCPSPFASP GPSSQAYDNL SLSDHLLRAV
     LNLLRREVSE HGRHLQQYFN LFVMYANLGV AEKTQLLKLS VPATFMLVSL DEGPGPPIKY
     QYAELGKLYS VVSQLIRCCN VSSRMQSSIN GNPSLPNPFG DPNLSQPIMP IQQNVVDILF
     VRTSYVKKII EDCSNSDETV KLLRFCCWEN PQFSSTVLSE LLWQVAYSYT YELRPYLDLL
     LQILLIEDSW QTHRIHNALK GIPDDRDGLF DTIQRSKNHY QKRAYQCIKC MVALFSSCPV
     AYQILQGNGD LKRKWTWAVE WLGDELERRP YTGNPQYTYN NWSPPVQSNE TSNGYFLERS
     HSARMTLAKA CELCPEEEPD DQDAPDEHES PPPEDAPLYP HSPGSQYQQN NHVHGQPYTG
     PAAHHMNNPQ RTGQRAQENY EGGEEVSPPQ TKGSVKCTY
//
ID   TP53B_MOUSE             Reviewed;        1957 AA.
AC   P70399; Q68FD0; Q8CI97; Q91YC9;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   08-FEB-2011, entry version 92.
DE   RecName: Full=Tumor suppressor p53-binding protein 1;
DE            Short=53BP1;
DE            Short=p53-binding protein 1;
DE            Short=p53BP1;
GN   Name=Tp53bp1; Synonyms=Trp53bp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, PHOSPHORYLATION, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=BALB/c;
RX   PubMed=11801725;
RA   Jullien D., Vagnarelli P., Earnshaw W.C., Adachi Y.;
RT   "Kinetochore localisation of the DNA damage response component 53BP1
RT   during mitosis.";
RL   J. Cell Sci. 115:71-79(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Head, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1164-1261 (ISOFORMS 1/2/3), AND
RP   INTERACTION WITH IFI202A.
RX   MEDLINE=97066938; PubMed=8910340; DOI=10.1074/jbc.271.44.27544;
RA   Datta B., Li B., Choubey D., Nallur G., Lengyel P.;
RT   "p202, an interferon-inducible modulator of transcription, inhibits
RT   transcriptional activation by the p53 tumor suppressor protein, and a
RT   segment from the p53-binding protein 1 that binds to p202 overcomes
RT   this inhibition.";
RL   J. Biol. Chem. 271:27544-27555(1996).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546 AND SER-1347, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1103, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [6]
RP   STRUCTURE BY NMR OF 1463-1617.
RX   PubMed=15341721; DOI=10.1016/j.str.2004.06.014;
RA   Charier G., Couprie J., Alpha-Bazin B., Meyer V., Quemeneur E.,
RA   Guerois R., Callebaut I., Gilquin B., Zinn-Justin S.;
RT   "The Tudor tandem of 53BP1: a new structural motif involved in DNA and
RT   RG-rich peptide binding.";
RL   Structure 12:1551-1562(2004).
CC   -!- FUNCTION: May have a role in checkpoint signaling during mitosis.
CC       Enhances TP53-mediated transcriptional activation. Binds to sites
CC       of DNA damage. Plays a role in the response to DNA damage (By
CC       similarity).
CC   -!- SUBUNIT: May form homooligomers. Interacts with DCLRE1C. Interacts
CC       with histone H2AFX and this requires phosphorylation of H2AFX on
CC       'Ser-139'. Interacts with histone H4 that has been dimethylated at
CC       'Lys-20'. Has low affinity for histone H4 containing
CC       monomethylated 'Lys-20'. Does not bind histone H4 containing
CC       unmethylated or trimethylated 'Lys-20'. Has low affinity for
CC       histone H3 that has been dimethylated on 'Lys-79'. Has very low
CC       affinity for histone H3 that has been monomethylated on 'Lys-79'
CC       (in vitro). Does not bind unmethylated histone H3. Interacts with
CC       MUM1/EXPAND1 (By similarity). Binds to the central domain of TP53.
CC       Interacts with IFI202A.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere,
CC       kinetochore. Note=Associated with kinetochores. Both nuclear and
CC       cytoplasmic in some cells. Recruited to sites of DNA damage, such
CC       as double stand breaks. Methylation of histone H4 at 'Lys-20' is
CC       required for efficient localization to double strand breaks (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P70399-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P70399-2; Sequence=VSP_016899;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=P70399-3; Sequence=VSP_016900, VSP_016901;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Asymmetrically dimethylated on Arg residues by PRMT1.
CC       Methylation is required for DNA binding (By similarity).
CC   -!- PTM: Hyperphosphorylated in mitotic cells. Phosphorylated at basal
CC       level in the absence of DNA damage. Hyper-phosphorylated in an
CC       ATM-dependent manner in response to DNA damage induced by ionizing
CC       radiation. Hyper-phosphorylated in an ATR-dependent manner in
CC       response to DNA damage induced by UV irradiation (By similarity).
CC   -!- SIMILARITY: Contains 2 BRCT domains.
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DR   EMBL; AJ414734; CAC94013.1; -; mRNA.
DR   EMBL; BC035206; AAH35206.1; -; mRNA.
DR   EMBL; BC079906; AAH79906.1; -; mRNA.
DR   EMBL; U67885; AAC52876.1; -; mRNA.
DR   IPI; IPI00674562; -.
DR   IPI; IPI00828418; -.
DR   IPI; IPI00877238; -.
DR   RefSeq; NP_038763.3; NM_013735.3.
DR   UniGene; Mm.215389; -.
DR   PDB; 1SSF; NMR; -; A=1463-1617.
DR   PDBsum; 1SSF; -.
DR   ProteinModelPortal; P70399; -.
DR   SMR; P70399; 1470-1588, 1709-1956.
DR   DIP; DIP-31595N; -.
DR   IntAct; P70399; 3.
DR   MINT; MINT-136714; -.
DR   STRING; P70399; -.
DR   PhosphoSite; P70399; -.
DR   PRIDE; P70399; -.
DR   Ensembl; ENSMUST00000064996; ENSMUSP00000069316; ENSMUSG00000043909.
DR   Ensembl; ENSMUST00000110645; ENSMUSP00000106275; ENSMUSG00000043909.
DR   Ensembl; ENSMUST00000110648; ENSMUSP00000106278; ENSMUSG00000043909.
DR   GeneID; 27223; -.
DR   KEGG; mmu:27223; -.
DR   UCSC; uc008lyd.1; mouse.
DR   UCSC; uc008lye.1; mouse.
DR   CTD; 27223; -.
DR   MGI; MGI:1351320; Trp53bp1.
DR   GeneTree; ENSGT00390000011891; -.
DR   HOVERGEN; HBG060882; -.
DR   InParanoid; P70399; -.
DR   NextBio; 305136; -.
DR   ArrayExpress; P70399; -.
DR   Bgee; P70399; -.
DR   Genevestigator; P70399; -.
DR   GermOnline; ENSMUSG00000043909; Mus musculus.
DR   GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005657; C:replication fork; IDA:MGI.
DR   GO; GO:0003684; F:damaged DNA binding; IDA:MGI.
DR   GO; GO:0042162; F:telomeric DNA binding; IDA:MGI.
DR   GO; GO:0008134; F:transcription factor binding; TAS:MGI.
DR   GO; GO:0006281; P:DNA repair; IDA:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; TAS:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR015125; 53-BP1_Tudor.
DR   InterPro; IPR001357; BRCT.
DR   InterPro; IPR014722; Transl_SH3-like_sub.
DR   Gene3D; G3DSA:2.30.30.30; Ribosomal_L2; 1.
DR   Pfam; PF09038; 53-BP1_Tudor; 1.
DR   SMART; SM00292; BRCT; 2.
DR   SUPFAM; SSF52113; BRCT; 2.
DR   PROSITE; PS50172; BRCT; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; Centromere; Chromosome;
KW   DNA damage; DNA repair; DNA-binding; Kinetochore; Methylation;
KW   Nucleus; Phosphoprotein; Repeat; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   1957       Tumor suppressor p53-binding protein 1.
FT                                /FTId=PRO_0000072644.
FT   DOMAIN     1737   1833       BRCT 1.
FT   DOMAIN     1849   1949       BRCT 2.
FT   REGION     1480   1508       Interaction with dimethylated histone H4
FT                                (By similarity).
FT   MOTIF      1381   1388       GAR.
FT   COMPBIAS    131    143       Poly-Glu.
FT   COMPBIAS    631    808       Glu-rich.
FT   COMPBIAS   1273   1315       Ser-rich.
FT   COMPBIAS   1464   1467       Poly-Ser.
FT   COMPBIAS   1628   1631       Poly-Ser.
FT   COMPBIAS   1745   1749       Poly-Glu.
FT   MOD_RES     104    104       Phosphoserine (By similarity).
FT   MOD_RES     163    163       Phosphoserine (By similarity).
FT   MOD_RES     173    173       Phosphoserine (By similarity).
FT   MOD_RES     175    175       Phosphoserine (By similarity).
FT   MOD_RES     262    262       Phosphoserine (By similarity).
FT   MOD_RES     291    291       Phosphoserine (By similarity).
FT   MOD_RES     299    299       Phosphothreonine (By similarity).
FT   MOD_RES     312    312       Phosphoserine (By similarity).
FT   MOD_RES     362    362       Phosphoserine (By similarity).
FT   MOD_RES     376    376       Phosphoserine (By similarity).
FT   MOD_RES     378    378       Phosphothreonine (By similarity).
FT   MOD_RES     391    391       Phosphoserine (By similarity).
FT   MOD_RES     446    446       Phosphoserine (By similarity).
FT   MOD_RES     516    516       Phosphotyrosine (By similarity).
FT   MOD_RES     517    517       Phosphoserine (By similarity).
FT   MOD_RES     519    519       Phosphoserine (By similarity).
FT   MOD_RES     537    537       Phosphothreonine (By similarity).
FT   MOD_RES     542    542       Phosphothreonine (By similarity).
FT   MOD_RES     546    546       Phosphoserine.
FT   MOD_RES     573    573       Phosphoserine (By similarity).
FT   MOD_RES     611    611       Phosphoserine (By similarity).
FT   MOD_RES     621    621       Phosphoserine (By similarity).
FT   MOD_RES     625    625       Phosphoserine (By similarity).
FT   MOD_RES     626    626       Phosphoserine (By similarity).
FT   MOD_RES     646    646       Phosphoserine (By similarity).
FT   MOD_RES     648    648       Phosphoserine (By similarity).
FT   MOD_RES     736    736       Phosphothreonine (By similarity).
FT   MOD_RES     737    737       Phosphoserine (By similarity).
FT   MOD_RES     740    740       Phosphoserine (By similarity).
FT   MOD_RES     741    741       Phosphoserine (By similarity).
FT   MOD_RES     757    757       Phosphoserine (By similarity).
FT   MOD_RES     768    768       Phosphoserine (By similarity).
FT   MOD_RES     770    770       Phosphoserine (By similarity).
FT   MOD_RES     876    876       Phosphoserine (By similarity).
FT   MOD_RES     977    977       Phosphoserine (By similarity).
FT   MOD_RES     980    980       Phosphothreonine (By similarity).
FT   MOD_RES     983    983       Phosphoserine (By similarity).
FT   MOD_RES     986    986       Phosphoserine (By similarity).
FT   MOD_RES    1004   1004       Phosphothreonine (By similarity).
FT   MOD_RES    1012   1012       Phosphoserine (By similarity).
FT   MOD_RES    1090   1090       Phosphoserine (By similarity).
FT   MOD_RES    1093   1093       Phosphoserine (By similarity).
FT   MOD_RES    1103   1103       Phosphoserine.
FT   MOD_RES    1156   1156       Phosphothreonine (By similarity).
FT   MOD_RES    1199   1199       Phosphothreonine (By similarity).
FT   MOD_RES    1201   1201       Phosphoserine (By similarity).
FT   MOD_RES    1204   1204       Phosphoserine (By similarity).
FT   MOD_RES    1275   1275       Phosphoserine (By similarity).
FT   MOD_RES    1301   1301       Phosphoserine (By similarity).
FT   MOD_RES    1302   1302       Phosphoserine (By similarity).
FT   MOD_RES    1305   1305       Phosphoserine (By similarity).
FT   MOD_RES    1347   1347       Phosphoserine.
FT   MOD_RES    1353   1353       Phosphoserine (By similarity).
FT   MOD_RES    1411   1411       Phosphoserine (By similarity).
FT   MOD_RES    1415   1415       Phosphoserine (By similarity).
FT   MOD_RES    1420   1420       Phosphoserine (By similarity).
FT   MOD_RES    1445   1445       Phosphoserine (By similarity).
FT   MOD_RES    1447   1447       Phosphoserine (By similarity).
FT   MOD_RES    1459   1459       Phosphoserine (By similarity).
FT   MOD_RES    1594   1594       Phosphothreonine (By similarity).
FT   MOD_RES    1603   1603       Phosphoserine (By similarity).
FT   MOD_RES    1616   1616       Phosphoserine (By similarity).
FT   MOD_RES    1619   1619       Phosphoserine (By similarity).
FT   MOD_RES    1620   1620       Phosphoserine (By similarity).
FT   MOD_RES    1623   1623       Phosphothreonine (By similarity).
FT   MOD_RES    1625   1625       Phosphothreonine (By similarity).
FT   MOD_RES    1628   1628       Phosphoserine (By similarity).
FT   MOD_RES    1630   1630       Phosphoserine (By similarity).
FT   MOD_RES    1631   1631       Phosphoserine (By similarity).
FT   MOD_RES    1632   1632       Phosphothreonine (By similarity).
FT   MOD_RES    1633   1633       Phosphothreonine (By similarity).
FT   MOD_RES    1657   1657       Phosphothreonine (By similarity).
FT   MOD_RES    1658   1658       Phosphoserine (By similarity).
FT   MOD_RES    1663   1663       Phosphoserine (By similarity).
FT   MOD_RES    1686   1686       Phosphoserine (By similarity).
FT   VAR_SEQ       1    943       Missing (in isoform 2).
FT                                /FTId=VSP_016899.
FT   VAR_SEQ    1100   1100       E -> EQRASQE (in isoform 3).
FT                                /FTId=VSP_016900.
FT   VAR_SEQ    1347   1396       Missing (in isoform 3).
FT                                /FTId=VSP_016901.
FT   CONFLICT    141    141       E -> EE (in Ref. 2; AAH79906).
FT   CONFLICT    395    395       A -> V (in Ref. 2; AAH79906).
FT   CONFLICT    421    421       T -> A (in Ref. 2; AAH79906).
FT   CONFLICT    669    669       A -> P (in Ref. 2; AAH79906).
FT   CONFLICT   1064   1064       P -> L (in Ref. 2; AAH79906).
FT   CONFLICT   1065   1065       K -> N (in Ref. 2; AAH35206).
FT   CONFLICT   1171   1172       EQ -> DE (in Ref. 3; AAC52876).
FT   CONFLICT   1175   1175       G -> R (in Ref. 1; CAC94013).
FT   CONFLICT   1194   1194       A -> T (in Ref. 3; AAC52876).
FT   CONFLICT   1259   1259       E -> G (in Ref. 3; AAC52876).
FT   CONFLICT   1759   1759       Q -> H (in Ref. 2; AAH79906).
FT   STRAND     1475   1478
FT   STRAND     1483   1493
FT   TURN       1496   1498
FT   STRAND     1499   1503
FT   STRAND     1509   1513
FT   TURN       1514   1516
FT   STRAND     1517   1520
FT   STRAND     1525   1533
FT   TURN       1535   1537
FT   STRAND     1539   1549
FT   STRAND     1552   1559
FT   STRAND     1562   1566
FT   HELIX      1568   1570
FT   STRAND     1571   1574
FT   HELIX      1575   1579
FT   TURN       1580   1584
FT   STRAND     1585   1587
SQ   SEQUENCE   1957 AA;  211340 MW;  0FFA0C26DD526E7B CRC64;
     MDPTGSQLDS DFSQQDTPCL IIEDSQPESQ VLEEDAGSHF SVLSRHLPNL QMHKENPVLD
     IVSNPEQSAV EQGDSNSSFN EHLKEKKASD PVESSHLGTS GSISQVIERL PQPNRTSSAL
     AVTVEAASLP EEEKEEEELE EKEGVGANAP GADSLAAEDS ASSQLGFGVL ELSQSQDVEE
     HTVPYDVNQE HLQLVTTNSG SSPLSDVDAS TAIKCEEQPT EDIAMIEQPS KDIPVTVQPG
     KGIHVVEEQN LPLVRSEDRP SSPQVSVAAV ETKEQVPARE LLEEGPQVQP SSEPEVSSTQ
     EDLFDQSSKT ASDGCSTPSR EEGGCSPVST PATTLQLLQL SGQKPLVQES LSTNSSDLVA
     PSPDAFRSTP FIVPSSPTEQ GGRKDEPMDM SVIPAGGEPF QKLHDDEAME TEKPLLPSQP
     TVSPQASTPV SRSTPVFTPG SLPIPSQPEF SHDIFIPSPS LEEPSDDVKK GGGLHSSSLT
     VECSKTSESE PKNFTDDLGL SMTGDSCKLM LSTSEYSQSS KMESLGSPRT EEDRENTQID
     DTEPLSPVSN SKLPADSENV LVTPSQDDQV EMSQNVDKAK EDETEDRGDC KGREDAVAED
     VCIDLTCDSG SQAVPSPATR SEALSSVLDQ EEAMDTKEHH PEEGFSGSEV EEVPETPCGS
     HREEPKEEAM ESIPLHLSLT ETQSEALCLQ KEAPKEECPE AMEVETSVIS IDSPQKLQVL
     DQELEHKDPD TWEEATSEDS SVVIVDVKEP SPRADVSCEP LEEVEKCSDS QSWEGVAPEE
     EPCAENRLDT PEEKRIECDG DSKAETTEKD AVTEDSPQPP LPSVRDEPVR PDQETQQPQV
     QEKESPVTVD AEVADDKQLG PEGACQQLEK APACASQSFC ESSSETPFHF TLPKEGDIIP
     PLTGATPPLI GHLKLEPKRH STPIGISNYP ESTIATSDVT SESMVEINDP LLGNEKGDSE
     SAPEMDGKLS LKMKLVSPET EASEESLQFS LEKPTTAERK NGSTAIAEPV ASLQKPVPVF
     GCIYEAQQEK EAQSEAPPSA PDRANLLHFP SAQEEDKERP DVTPKLRQSE QPVKPVGPVM
     DDAAPEDSAS PVSQQRASQE PFSPAEDVME TDLLEGLAAN QDRPSKMLMD RPTQSNIGIQ
     TVDHSLCAPE TVSAATQTVK SVCEQGTSTA EQNSGKQDAT VQTERGSGEK PASAPVDDTE
     SLHSQGEEEF EMPQPPHGHV LHRHMRTIRE VRTLVTRVIT DVYYVDGTEV ERKVTEETEE
     PIVECQECET EVSPSQTGGS SGDLGDISSF SSKASSSHHT SSGTSLSAIH SSGSSGRGAG
     PLKGKASGTE AADFALPSSR GGPGKLSPRK GISQTGAPVC EEDGDAGLGI RQGGKAPVTP
     RGRGRRGRPP SRTTGTRETV VSGPLGVEDI SPSMSPDDKS FTRIMPRVPD STKRTDASSS
     TLRRSDSPEI PFQAATGSSD GLDSSSSGNS FVGLRVVAKW SSNGYFYSGK ITRDVGAGKY
     KLLFDDGYEC DVLGKDILLC DPIPLDTEVT ALSEDEYFSA GVVKGHRKES GELYYSIEKE
     GQRKWYKRMA VILSLEQGNR LREQYGLGPY EAVTPLTKAA DISLDNLVEG KRKRRSNISS
     PVTPTAASSS STTPTRKATE SPRASTGVPS GKRKLPTSEE ERSPAKRGRK SATVKPGTVG
     AAEFVSPCET GDNIGEPSVL EEPRGPLPLN KTLFLGYAFL LTMATTSDKL ASRSKLLDGP
     TGSSEEEEEF LEIPPFNKQY TECQLRAGAG YILEDFNEAQ CNTAYQCLLI ADQHCRTRKY
     FLCLASGIPC VSHVWVHDSC HANQLQNYRN YLLPAGYSLE EQRILDWQPR ENPFQNLKVL
     LVSDQQQNFL ELWSEILMTG GAASVKQHHS SAHNKDIALG VFDVVVTDPS CPASVLKCAE
     ALQLPVVSQE WVIQCLIVGE RIGFKQHPKY KHDYVSH
//
ID   IDHG1_MOUSE             Reviewed;         393 AA.
AC   P70404;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Isocitrate dehydrogenase [NAD] subunit gamma 1, mitochondrial;
DE            EC=1.1.1.41;
DE   AltName: Full=Isocitric dehydrogenase subunit gamma;
DE   AltName: Full=NAD(+)-specific ICDH subunit gamma;
DE   Flags: Precursor;
GN   Name=Idh3g;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=97432815; PubMed=9286695; DOI=10.1006/geno.1997.4822;
RA   Brenner V., Nyakatura G., Rosenthal A., Platzer M.;
RT   "Genomic organization of two novel genes on human Xq28: compact head
RT   to head arrangement of IDH gamma and TRAP delta is conserved in rat
RT   and mouse.";
RL   Genomics 44:8-14(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Platzer M., Brenner V., Reichwald K., Wiehe T., Oksche A.,
RA   Rosenthal A.;
RT   "Comparative sequence analysis of the mouse L1cam locus and the
RT   corresponding region of human Xq28.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 70-108; 116-129; 137-190 AND 227-237, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-363, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
CC   -!- CATALYTIC ACTIVITY: Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) +
CC       NADH.
CC   -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By
CC       similarity).
CC   -!- ENZYME REGULATION: Activated by increasing ADP/ATP ratios and by
CC       Ca(2+) (By similarity).
CC   -!- SUBUNIT: Heterooligomer of subunits alpha, beta, and gamma in the
CC       apparent ratio of 2:1:1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
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DR   EMBL; U68564; AAC53340.1; -; mRNA.
DR   EMBL; AF133093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00109169; -.
DR   RefSeq; NP_032349.1; NM_008323.1.
DR   UniGene; Mm.14825; -.
DR   ProteinModelPortal; P70404; -.
DR   SMR; P70404; 40-386.
DR   STRING; P70404; -.
DR   PhosphoSite; P70404; -.
DR   PRIDE; P70404; -.
DR   Ensembl; ENSMUST00000052761; ENSMUSP00000056502; ENSMUSG00000002010.
DR   GeneID; 15929; -.
DR   KEGG; mmu:15929; -.
DR   UCSC; uc009tmp.1; mouse.
DR   CTD; 15929; -.
DR   MGI; MGI:1099463; Idh3g.
DR   eggNOG; roNOG10611; -.
DR   HOGENOM; HBG518924; -.
DR   HOVERGEN; HBG052080; -.
DR   InParanoid; P70404; -.
DR   OMA; YAMLEHE; -.
DR   OrthoDB; EOG4M0F21; -.
DR   PhylomeDB; P70404; -.
DR   BRENDA; 1.1.1.41; 244.
DR   NextBio; 288644; -.
DR   ArrayExpress; P70404; -.
DR   Bgee; P70404; -.
DR   CleanEx; MM_IDH3G; -.
DR   Genevestigator; P70404; -.
DR   GermOnline; ENSMUSG00000002010; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006102; P:isocitrate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR001804; Isocitrate/isopropylmalate_DH.
DR   InterPro; IPR004434; Isocitrate_DH_NAD.
DR   Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1.
DR   PANTHER; PTHR11835; IDH_IMDH_dimeric; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   TIGRFAMs; TIGR00175; mito_nad_idh; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Magnesium; Manganese;
KW   Metal-binding; Mitochondrion; NAD; Nucleotide-binding; Oxidoreductase;
KW   Phosphoprotein; Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT       1     39       Mitochondrion (By similarity).
FT   CHAIN        40    393       Isocitrate dehydrogenase [NAD] subunit
FT                                gamma 1, mitochondrial.
FT                                /FTId=PRO_0000014451.
FT   NP_BIND      56     84       NAD (Potential).
FT   NP_BIND     309    316       ATP (Potential).
FT   METAL       254    254       Magnesium or manganese (By similarity).
FT   BINDING     136    136       Substrate (By similarity).
FT   BINDING     167    167       Substrate (By similarity).
FT   BINDING     254    254       Substrate (By similarity).
FT   SITE        174    174       Critical for catalysis (By similarity).
FT   SITE        221    221       Critical for catalysis (By similarity).
FT   MOD_RES     363    363       Phosphothreonine.
SQ   SEQUENCE   393 AA;  42785 MW;  4023560C44C1F4D3 CRC64;
     MALKVAIAAG GAAKAMLKPT LLCRPWEVLA AHVAPRRSIS SQQTIPPSAK YGGRHTVTMI
     PGDGIGPELM LHVKSVFRHA CVPVDFEEVH VSSNADEEDI RNAIMAIRRN RVALKGNIET
     NHNLPPSHKS RNNILRTSLD LYANVIHCKS LPGVVTRHKD IDILIVRENT EGEYSSLEHE
     SVAGVVESLK IITKAKSLRI AEYAFKLAQE SGRKKVTAVH KANIMKLGDG LFLQCCREVA
     AHYPQITFDS MIVDNTTMQL VSRPQQFDVM VMPNLYGNIV NNVCAGLVGG PGLVAGANYG
     HVYAVFETAT RNTGKSIANK NIANPTATLL ASCMMLDHLK LHSYATSIRK AVLASMDNEN
     MHTPDIGGQG TTSQAIQDII RHIRIINGRA VEA
//
ID   CAD10_MOUSE             Reviewed;         788 AA.
AC   P70408; Q80WS7;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Cadherin-10;
DE   AltName: Full=T2-cadherin;
DE   Flags: Precursor;
GN   Name=Cdh10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 516-788, AND DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6; TISSUE=Testis;
RX   MEDLINE=97033837; PubMed=8879495;
RA   Munro S.B., Blaschuk O.W.;
RT   "A comprehensive survey of the cadherins expressed in the testes of
RT   fetal, immature, and adult mice utilizing the polymerase chain
RT   reaction.";
RL   Biol. Reprod. 55:822-827(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 732-771.
RC   STRAIN=CBA/J; TISSUE=Thymocyte;
RX   MEDLINE=96211873; PubMed=8620560; DOI=10.1006/cimm.1996.0123;
RA   Munro S.B., Duclos A.J., Jackson A.R., Baines M.G., Blaschuk O.W.;
RT   "Characterization of cadherins expressed by murine thymocytes.";
RL   Cell. Immunol. 169:309-312(1996).
CC   -!- FUNCTION: Cadherins are calcium dependent cell adhesion proteins.
CC       They preferentially interact with themselves in a homophilic
CC       manner in connecting cells; cadherins may thus contribute to the
CC       sorting of heterogeneous cell types.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- DEVELOPMENTAL STAGE: Expressed at all stages of testicular
CC       development with highest levels found in fetal gonad.
CC   -!- SIMILARITY: Contains 5 cadherin domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC052056; AAH52056.1; -; mRNA.
DR   EMBL; BC062962; AAH62962.1; -; mRNA.
DR   EMBL; U69137; AAB87708.1; -; mRNA.
DR   IPI; IPI00670856; -.
DR   UniGene; Mm.117794; -.
DR   UniGene; Mm.446240; -.
DR   ProteinModelPortal; P70408; -.
DR   SMR; P70408; 56-594, 685-782.
DR   STRING; P70408; -.
DR   PhosphoSite; P70408; -.
DR   PRIDE; P70408; -.
DR   Ensembl; ENSMUST00000040562; ENSMUSP00000042199; ENSMUSG00000022321.
DR   MGI; MGI:107436; Cdh10.
DR   eggNOG; roNOG13021; -.
DR   HOGENOM; HBG505775; -.
DR   HOVERGEN; HBG005217; -.
DR   InParanoid; P70408; -.
DR   OrthoDB; EOG4CZBF8; -.
DR   ArrayExpress; P70408; -.
DR   Bgee; P70408; -.
DR   CleanEx; MM_CDH10; -.
DR   Genevestigator; P70408; -.
DR   GermOnline; ENSMUSG00000022321; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 5.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF01049; Cadherin_C; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 5.
DR   SUPFAM; SSF49313; Cadherin; 5.
DR   PROSITE; PS00232; CADHERIN_1; 3.
DR   PROSITE; PS50268; CADHERIN_2; 5.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell membrane;
KW   Cleavage on pair of basic residues; Glycoprotein; Membrane;
KW   Phosphoprotein; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     22       Potential.
FT   PROPEP       23     54       Potential.
FT                                /FTId=PRO_0000269662.
FT   CHAIN        55    788       Cadherin-10.
FT                                /FTId=PRO_0000126646.
FT   TOPO_DOM     23    613       Extracellular (Potential).
FT   TRANSMEM    614    634       Helical; (Potential).
FT   TOPO_DOM    635    788       Cytoplasmic (Potential).
FT   DOMAIN       56    160       Cadherin 1.
FT   DOMAIN      161    269       Cadherin 2.
FT   DOMAIN      270    384       Cadherin 3.
FT   DOMAIN      385    489       Cadherin 4.
FT   DOMAIN      489    603       Cadherin 5.
FT   MOD_RES     784    784       Phosphoserine (By similarity).
FT   CARBOHYD    256    256       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    456    456       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    534    534       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    518    525       PLGGQKFF -> VDRRSFS (in Ref. 2;
FT                                AAB87708).
FT   CONFLICT    549    549       T -> A (in Ref. 2; AAB87708).
FT   CONFLICT    607    610       AGLS -> WPH (in Ref. 2; AAB87708).
FT   CONFLICT    635    639       Missing (in Ref. 2; AAB87708).
FT   CONFLICT    699    699       Missing (in Ref. 2; AAB87708).
FT   CONFLICT    706    706       D -> G (in Ref. 2; AAB87708).
FT   CONFLICT    773    773       N -> K (in Ref. 2; AAB87708).
FT   CONFLICT    788    788       A -> S (in Ref. 2; AAB87708).
SQ   SEQUENCE   788 AA;  88302 MW;  11AE32F2BBAFFA70 CRC64;
     MTIYQFLRLF VLWACLPHFC CPELTFRRTP GIQQMTAESR APRSDGKILH RQKRGWMWNQ
     FFLLEEYTGS DYQYVGKLHS DQDKGDGSLK YILSGDGAGT LFIIDEKTGD IHATRRIDRE
     EKAFYTLRAQ AINRRTLRPV ESESEFVIKI HDINDNEPTF PEEIYTASVP EMSVVGTSVV
     QVTATDADDP SYGNSARVIY SILQGQPYFS VEPETGIIRT ALPNMNRENK EQYQVVIQAK
     DMGGQMGGLS GTTTVNITLT DVNDNPPRFP QNTIHLRVLE SSPVGTAVGS VKATDADTGK
     NAEVDYRIID GDGTDMFDII TEKDTQEGII TVKKPLDYEN RRLYTLKVEA ENTHVDPRFY
     YLGPFKDTTI VKISIEDVDE PPVFSRSSYL FEVHEDIEVG TIIGTVMARD PDSTSSPIRF
     TLDRHTDLDR IFNIHSGNGS LYTSKPLDRE LSQWHNLTVI AAEINNPKET TRVSVFVRIL
     DVNDNAPQFA VFYDTFVCEN ARPGQLIQTI SAVDKDDPLG GQKFFFSLAA VNPNFTVQDN
     EDNTARILTR KNGFNRHEIS TYLLPVVISD NDYPIQSSTG TLTIRVCACD SQGNMQSCSA
     EALLLPAGLS TGALIAILLC IIILLVIVVL FAALKRQRKK EPLILSKEDI RDNIVSYNDE
     GGGEEDTQAF DIGTLRNPAA IEEKKLRRDI IPETLFIPRR TPTAPDNTDV RDFINERLKE
     HDLDPTAPPY DSLATYAYEG NDSVAESLSS LESGTTEGDQ NYDYLREWGP RFNKLAEMYG
     GGESDKDA
//
ID   EVL_MOUSE               Reviewed;         414 AA.
AC   P70429; Q9ERU8;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-NOV-2002, sequence version 2.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=Ena/VASP-like protein;
DE   AltName: Full=Ena/vasodilator-stimulated phosphoprotein-like;
GN   Name=Evl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=97015079; PubMed=8861907; DOI=10.1016/S0092-8674(00)81341-0;
RA   Gertler F.B., Niebuhr K., Reinhard M., Wehland J., Soriano P.;
RT   "Mena, a relative of VASP and Drosophila Enabled, is implicated in the
RT   control of microfilament dynamics.";
RL   Cell 87:227-239(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH
RP   PFN2; LYN; APBB1; ABL1 AND SRC, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND PHOSPHORYLATION BY PKA.
RC   STRAIN=C57BL/6J;
RX   PubMed=10945997; DOI=10.1074/jbc.M006274200;
RA   Lambrechts A., Kwiatkowski A.V., Lanier L.M., Bear J.E.,
RA   Vandekerckhove J., Ampe C., Gertler F.B.;
RT   "cAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP
RT   relative, regulates its interaction with actin and SH3 domains.";
RL   J. Biol. Chem. 275:36143-36151(2000).
RN   [3]
RP   FUNCTION IN L.MONOCYTOGENES MOBILITY, AND INTERACTION WITH
RP   L.MONOCYTOGENES ACTA.
RX   PubMed=10087267; DOI=10.1083/jcb.144.6.1245;
RA   Laurent V., Loisel T.P., Harbeck B., Wehman A., Groebe L.,
RA   Jockusch B.M., Wehland J., Gertler F.B., Carlier M.-F.;
RT   "Role of proteins of the Ena/VASP family in actin-based motility of
RT   Listeria monocytogenes.";
RL   J. Cell Biol. 144:1245-1258(1999).
RN   [4]
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   MEDLINE=99166867; PubMed=10069337; DOI=10.1016/S0896-6273(00)81092-2;
RA   Lanier L.M., Gates M.A., Witke W., Menzies A.S., Wehman A.M.,
RA   Macklis J.D., Kwiatkowski D., Soriano P., Gertler F.B.;
RT   "Mena is required for neurulation and commissure formation.";
RL   Neuron 22:313-325(1999).
RN   [5]
RP   INTERACTION WITH SEMA6A.
RX   PubMed=10993894; DOI=10.1074/jbc.M006316200;
RA   Klostermann A., Lutz B., Gertler F., Behl C.;
RT   "The orthologous human and murine semaphorin 6A-1 proteins (SEMA6A-
RT   1/Sema6A-1) bind to the enabled/vasodilator-stimulated phosphoprotein-
RT   like protein (EVL) via a novel carboxyl-terminal zyxin-like domain.";
RL   J. Biol. Chem. 275:39647-39653(2000).
RN   [6]
RP   INTERACTION WITH DNMBP.
RX   PubMed=14506234; DOI=10.1074/jbc.M308104200;
RA   Salazar M.A., Kwiatkowski A.V., Pellegrini L., Cestra G., Butler M.H.,
RA   Rossman K.L., Serna D.M., Sondek J., Gertler F.B., De Camilli P.;
RT   "Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology
RT   domains, links dynamin to regulation of the actin cytoskeleton.";
RL   J. Biol. Chem. 278:49031-49043(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329 AND SER-347, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343 AND SER-367, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-130 IN COMPLEX WITH A
RP   SYNTHETIC PRO-RICH PEPTIDE.
RX   PubMed=10404224; DOI=10.1038/10717;
RA   Fedorov A.A., Fedorov E., Gertler F., Almo S.C.;
RT   "Structure of EVH1, a novel proline-rich ligand-binding module
RT   involved in cytoskeletal dynamics and neural function.";
RL   Nat. Struct. Biol. 6:661-665(1999).
CC   -!- FUNCTION: Ena/VASP proteins are actin-associated proteins involved
CC       in a range of processes dependent on cytoskeleton remodeling and
CC       cell polarity such as axon guidance and lamellipodial and
CC       filopodial dynamics in migrating cells. EVL enhances actin
CC       nucleation and polymerization. Required to transform actin
CC       polymerization into active movement for the propulsive force of
CC       Listeria monocytogenes.
CC   -!- SUBUNIT: Homotetramer (By similarity). Binds to the SH3 domains of
CC       ABL1, LYN and SRC. Also binds to profilin, with preference for
CC       isoform IIa of PFN2, and the WW domain of APBB1/FE65. Binds to
CC       SEMA6A. Interacts, via the Pro-rich region, with the C-terminal
CC       SH3 domain of DNMBP. Interacts with RAPH1. Binds, via the EVH1
CC       domain, the Pro-rich domain of ZYX (By similarity). Binds, via the
CC       EVH1 domain, the Pro-rich domain of Listeria monocytogenes actA.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection,
CC       lamellipodium. Note=Targeted to the leading edge of lamellipodia
CC       and the dital tip of stress fibers through interaction with a
CC       number of proteins. In activated T-cells, localizes to the F-actin
CC       collar and the distal tip of microspikes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2; Synonyms=EVL-I;
CC         IsoId=P70429-1; Sequence=Displayed;
CC       Name=1;
CC         IsoId=P70429-2; Sequence=VSP_004045;
CC   -!- TISSUE SPECIFICITY: Highest expression in thymus and spleen. Lower
CC       levels in placenta, ovary, testis, fat and lung. Isoform 1 and
CC       isoform 2 are expressed in cortical neurons and glial cells.
CC   -!- DEVELOPMENTAL STAGE: First detected at E15 in the branchial and
CC       pharyngeal arches. Not expressed in the developing brain.
CC   -!- DOMAIN: The EVH2 domain is comprised of 3 regions. Block A is a
CC       thymosin-like domain required for G-actin binding. The KLKR motif
CC       within this block is essential for the G-actin binding and for
CC       actin polymerization. Block B is required for F-actin binding and
CC       subcellular location, and Block C for tetramerization.
CC   -!- PTM: Phosphorylated by PKA; phosphorylation abolishes binding to
CC       SH3 domains of ABL and SRC.
CC   -!- SIMILARITY: Belongs to the Ena/VASP family.
CC   -!- SIMILARITY: Contains 1 WH1 domain.
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DR   EMBL; U72519; AAC52862.1; -; mRNA.
DR   EMBL; AF279662; AAG23653.1; -; mRNA.
DR   IPI; IPI00109256; -.
DR   IPI; IPI00311253; -.
DR   RefSeq; NP_001156866.1; NM_001163394.1.
DR   RefSeq; NP_031991.3; NM_007965.3.
DR   UniGene; Mm.238841; -.
DR   PDB; 1QC6; X-ray; 2.60 A; A/B=1-130.
DR   PDBsum; 1QC6; -.
DR   ProteinModelPortal; P70429; -.
DR   SMR; P70429; 1-113, 374-408.
DR   STRING; P70429; -.
DR   PhosphoSite; P70429; -.
DR   PRIDE; P70429; -.
DR   Ensembl; ENSMUST00000021689; ENSMUSP00000021689; ENSMUSG00000021262.
DR   Ensembl; ENSMUST00000077735; ENSMUSP00000076916; ENSMUSG00000021262.
DR   Ensembl; ENSMUST00000109854; ENSMUSP00000105480; ENSMUSG00000021262.
DR   GeneID; 14026; -.
DR   KEGG; mmu:14026; -.
DR   UCSC; uc007ozv.1; mouse.
DR   UCSC; uc007ozw.1; mouse.
DR   CTD; 14026; -.
DR   MGI; MGI:1194884; Evl.
DR   eggNOG; roNOG16263; -.
DR   GeneTree; ENSGT00440000039080; -.
DR   HOGENOM; HBG715851; -.
DR   HOVERGEN; HBG006655; -.
DR   InParanoid; P70429; -.
DR   OMA; LQSQPHS; -.
DR   OrthoDB; EOG4BVRV3; -.
DR   PhylomeDB; P70429; -.
DR   ArrayExpress; P70429; -.
DR   Bgee; P70429; -.
DR   CleanEx; MM_EVL; -.
DR   Genevestigator; P70429; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005522; F:profilin binding; IDA:UniProtKB.
DR   GO; GO:0017124; F:SH3 domain binding; IDA:UniProtKB.
DR   GO; GO:0030048; P:actin filament-based movement; NAS:UniProtKB.
DR   GO; GO:0045010; P:actin nucleation; NAS:UniProtKB.
DR   GO; GO:0008154; P:actin polymerization or depolymerization; IDA:UniProtKB.
DR   GO; GO:0007411; P:axon guidance; NAS:UniProtKB.
DR   GO; GO:0051016; P:barbed-end actin filament capping; NAS:UniProtKB.
DR   GO; GO:0030168; P:platelet activation; NAS:UniProtKB.
DR   InterPro; IPR000697; EVH1.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR017354; Vasodilator_phosphoprotein.
DR   InterPro; IPR014885; VASP_tetra.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF08776; VASP_tetra; 1.
DR   Pfam; PF00568; WH1; 1.
DR   PIRSF; PIRSF038010; Vasodilator_Phospo; 1.
DR   SMART; SM00461; WH1; 1.
DR   PROSITE; PS50229; WH1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Alternative splicing; Cell projection;
KW   Cytoplasm; Cytoskeleton; Phosphoprotein; SH3-binding.
FT   CHAIN         1    414       Ena/VASP-like protein.
FT                                /FTId=PRO_0000087105.
FT   DOMAIN        1    112       WH1.
FT   REGION      220    411       EVH2.
FT   REGION      220    240       EVH2 block A.
FT   REGION      263    280       EVH2 block B.
FT   REGION      377    411       EVH2 block C.
FT   MOTIF       229    232       KLKR.
FT   COMPBIAS    160    204       Pro-rich.
FT   MOD_RES     244    244       Phosphoserine (By similarity).
FT   MOD_RES     248    248       Phosphothreonine (By similarity).
FT   MOD_RES     302    302       Phosphoserine (By similarity).
FT   MOD_RES     304    304       Phosphoserine (By similarity).
FT   MOD_RES     327    327       Phosphoserine (By similarity).
FT   MOD_RES     329    329       Phosphoserine.
FT   MOD_RES     339    339       Phosphoserine (By similarity).
FT   MOD_RES     343    343       Phosphoserine.
FT   MOD_RES     347    347       Phosphoserine.
FT   MOD_RES     352    352       Phosphoserine (By similarity).
FT   MOD_RES     367    367       Phosphoserine.
FT   VAR_SEQ     339    359       Missing (in isoform 1).
FT                                /FTId=VSP_004045.
FT   STRAND        4     17
FT   TURN         18     21
FT   STRAND       22     25
FT   STRAND       34     41
FT   TURN         42     45
FT   STRAND       46     52
FT   TURN         54     56
FT   STRAND       59     64
FT   STRAND       70     75
FT   STRAND       78     82
FT   STRAND       87     93
FT   HELIX        95    111
SQ   SEQUENCE   414 AA;  44337 MW;  146A018BCD6CA370 CRC64;
     MSEQSICQAR ASVMVYDDTS KKWVPIKPGQ QGFSRINIYH NTASSTFRVV GVKLQDQQVV
     INYSIVKGLK YNQATPTFHQ WRDARQVYGL NFASKEEATT FSNAMLFALN IMNSQEGGPS
     TQRQVQNGPS PEEMDIQRRQ VMEQQHRQES LERRISATGP ILPPGHPSSA ASTTLSCSGP
     PPPPPPPVPP PPTGSTPPPP PPLPAGGAQG TNHDESSASG LAAALAGAKL RRVQRPEDAS
     GGSSPSGTSK SDANRASSGG GGGGLMEEMN KLLAKRRKAA SQTDKPADRK EDESQTEDPS
     TSPSPGTRAT SQPPNSSEAG RKPWERSNSV EKPVSSLLSR TPSVAKSPEA KSPLQSQPHS
     RVKPAGSVND VGLDALDLDR MKQEILEEVV RELHKVKEEI IDAIRQELSG ISTT
//
ID   NHRF1_MOUSE             Reviewed;         355 AA.
AC   P70441; Q8BYD8;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 101.
DE   RecName: Full=Na(+)/H(+) exchange regulatory cofactor NHE-RF1;
DE            Short=NHERF-1;
DE   AltName: Full=Ezrin-radixin-moesin-binding phosphoprotein 50;
DE            Short=EBP50;
DE   AltName: Full=Regulatory cofactor of Na(+)/H(+) exchanger;
DE   AltName: Full=Sodium-hydrogen exchanger regulatory factor 1;
DE   AltName: Full=Solute carrier family 9 isoform A3 regulatory factor 1;
GN   Name=Slc9a3r1; Synonyms=Nherf, Nherf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Kidney;
RX   PubMed=10500246; DOI=10.1016/S0167-4781(99)00100-1;
RA   Weinman E.J., Steplock D., Zhang X., Akhter S., Shenolikar S.;
RT   "Molecular cloning of the cDNA and promoter sequences for the mouse
RT   sodium-hydrogen exchanger regulatory factor.";
RL   Biochim. Biophys. Acta 1447:71-76(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH ADRB2.
RX   PubMed=9560162; DOI=10.1038/33458;
RA   Hall R.A., Premont R.T., Chow C.-W., Blitzer J.T., Pitcher J.A.,
RA   Claing A., Stoffel R.H., Barak L.S., Shenolikar S., Weinman E.J.,
RA   Grinstein S., Lefkowitz R.J.;
RT   "The beta2-adrenergic receptor interacts with the Na+/H+-exchanger
RT   regulatory factor to control Na+/H+ exchange.";
RL   Nature 392:626-630(1998).
RN   [5]
RP   INTERACTION WITH PAG1, AND IDENTIFICATION IN A COMPLEX WITH PAG1 AND
RP   MSN.
RX   PubMed=11777944;
RA   Itoh K., Sakakibara M., Yamasaki S., Takeuchi A., Arase H.,
RA   Miyazaki M., Nakajima N., Okada M., Saito T.;
RT   "Negative regulation of immune synapse formation by anchoring lipid
RT   raft to cytoskeleton through Cbp-EBP50-ERM assembly.";
RL   J. Immunol. 168:541-544(2002).
RN   [6]
RP   INTERACTION WITH PDZK1.
RX   MEDLINE=22894942; PubMed=14531806;
RX   DOI=10.1046/j.1523-1755.2003.00266.x;
RA   Gisler S.M., Pribanic S., Bacic D., Forrer P., Gantenbein A.,
RA   Sabourin L.A., Tsuji A., Zhao Z.-S., Manser E., Biber J., Murer H.;
RT   "PDZK1: I. a major scaffolder in brush borders of proximal tubular
RT   cells.";
RL   Kidney Int. 64:1733-1745(2003).
RN   [7]
RP   INTERACTION WITH HTR4.
RX   PubMed=15466885; DOI=10.1242/jcs.01379;
RA   Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W.,
RA   Marin P., Dumuis A., Bockaert J.;
RT   "New sorting nexin (SNX27) and NHERF specifically interact with the 5-
RT   HT4a receptor splice variant: roles in receptor targeting.";
RL   J. Cell Sci. 117:5367-5379(2004).
RN   [8]
RP   PHOSPHORYLATION AT SER-286.
RX   PubMed=15378723; DOI=10.1002/rcm.1604;
RA   Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.;
RT   "Phosphoproteome analysis of mouse liver using immobilized metal
RT   affinity purification and linear ion trap mass spectrometry.";
RL   Rapid Commun. Mass Spectrom. 18:2169-2176(2004).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289 AND SER-297, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275 AND SER-285, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [11]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17311105; DOI=10.1371/journal.pone.0000237;
RA   Nielsen J.S., Graves M.L., Chelliah S., Vogl A.W., Roskelley C.D.,
RA   McNagny K.M.;
RT   "The CD34-related molecule podocalyxin is a potent inducer of
RT   microvillus formation.";
RL   PLoS ONE 2:E237-E237(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-285; SER-286;
RP   SER-289 AND SER-297, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
CC   -!- FUNCTION: Scaffold protein that connects plasma membrane proteins
CC       with members of the ezrin/moesin/radixin family and thereby helps
CC       to link them to the actin cytoskeleton and to regulate their
CC       surface expression. Necessary for recycling of internalized ADRB2.
CC       Was first known to play a role in the regulation of the activity
CC       and subcellular location of SLC9A3. Necessary for cAMP-mediated
CC       phosphorylation and inhibition of SLC9A3. May enhance Wnt
CC       signaling (By similarity). May participate in HTR4 targeting to
CC       microvilli.
CC   -!- SUBUNIT: Homodimer, and heterodimer with SLC9A3R2. Binds the N-
CC       termini of EZR, RDX and MSN. Binds the C-termini of PDGFRA,
CC       PDGFRB, ADRB2, NOS2 and CFTR. Binds ARHGAP17, EPI64, GNB2L1,
CC       OPRK1, GNAQ, CTNNB1, PLCB3 and CLCN3. Forms a complex with CFTR
CC       and SLC4A7. Forms a complex with SLC4A7 and ATP6V1B1 (By
CC       similarity). Binds PDZK1. Binds the C-terminus of PAG1. In resting
CC       T-cells, part of a PAG1-SLC9A3R1-MSN complex which is disrupted
CC       upon TCR activation. Directly interacts with HTR4. Interacts with
CC       MCC (By similarity). Interacts with TRPC4 (via the PDZ-binding
CC       domain) (By similarity). Interacts (via the PDZ 1 domain) with
CC       PODXL (via the C-terminal PDZ-binding motif DTHL); interaction is
CC       not detected in glomerular epithelium cells (By similarity).
CC       Interacts (via the PDZ 1 domain) with PODXL (via the C-terminal
CC       PDZ-binding motif DTHL); the interaction take place early in the
CC       secretory pathway and is necessary for its apical membrane sorting
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Apical cell membrane. Cell
CC       projection, filopodium (By similarity). Cell projection, ruffle
CC       (By similarity). Cell projection, microvillus (By similarity).
CC       Endomembrane system; Peripheral membrane protein (By similarity).
CC       Note=Colocalizes with actin in microvilli-rich apical regions of
CC       the syncytiotrophoblast. Present in lipid rafts of T-cells (By
CC       similarity). Translocates from the cytoplasm to the apical cell
CC       membrane in a PODXL-dependent manner.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P70441-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P70441-2; Sequence=VSP_027877, VSP_027878;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 2 PDZ (DHR) domains.
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DR   EMBL; U74079; AAB17569.1; -; mRNA.
DR   EMBL; AK040371; BAC30573.2; -; mRNA.
DR   EMBL; BC085141; AAH85141.1; -; mRNA.
DR   IPI; IPI00109311; -.
DR   IPI; IPI00857737; -.
DR   RefSeq; NP_036160.1; NM_012030.2.
DR   UniGene; Mm.27842; -.
DR   ProteinModelPortal; P70441; -.
DR   SMR; P70441; 11-231.
DR   MINT; MINT-144615; -.
DR   STRING; P70441; -.
DR   PhosphoSite; P70441; -.
DR   PRIDE; P70441; -.
DR   Ensembl; ENSMUST00000021077; ENSMUSP00000021077; ENSMUSG00000020733.
DR   GeneID; 26941; -.
DR   KEGG; mmu:26941; -.
DR   UCSC; uc007mgp.1; mouse.
DR   CTD; 26941; -.
DR   MGI; MGI:1349482; Slc9a3r1.
DR   eggNOG; roNOG05702; -.
DR   HOGENOM; HBG714863; -.
DR   HOVERGEN; HBG052616; -.
DR   InParanoid; P70441; -.
DR   OMA; LCAMKKG; -.
DR   OrthoDB; EOG4ZS93M; -.
DR   PhylomeDB; P70441; -.
DR   NextBio; 304861; -.
DR   PMAP-CutDB; P70441; -.
DR   ArrayExpress; P70441; -.
DR   Bgee; P70441; -.
DR   Genevestigator; P70441; -.
DR   GermOnline; ENSMUSG00000020733; Mus musculus.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005902; C:microvillus; IEA:UniProtKB-SubCell.
DR   GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR   GO; GO:0030643; P:cellular phosphate ion homeostasis; IMP:MGI.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR015098; EBP50_C-term.
DR   InterPro; IPR017300; NaH_exchngr_reg_CF_NHE-RF.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF09007; EBP50_C-term; 1.
DR   Pfam; PF00595; PDZ; 2.
DR   PIRSF; PIRSF037866; EBP50; 1.
DR   ProDom; PD283022; EBP50_C-term; 1.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; PDZ; 2.
DR   PROSITE; PS50106; PDZ; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell membrane; Cell projection;
KW   Cytoplasm; Membrane; Phosphoprotein; Repeat; Wnt signaling pathway.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    355       Na(+)/H(+) exchange regulatory cofactor
FT                                NHE-RF1.
FT                                /FTId=PRO_0000096800.
FT   DOMAIN       14     94       PDZ 1.
FT   DOMAIN      149    229       PDZ 2.
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES      46     46       Phosphoserine (By similarity).
FT   MOD_RES     275    275       Phosphoserine.
FT   MOD_RES     283    283       Phosphoserine.
FT   MOD_RES     285    285       Phosphoserine.
FT   MOD_RES     286    286       Phosphoserine.
FT   MOD_RES     288    288       Phosphothreonine (By similarity).
FT   MOD_RES     289    289       Phosphoserine.
FT   MOD_RES     297    297       Phosphoserine.
FT   VAR_SEQ       1    317       Missing (in isoform 2).
FT                                /FTId=VSP_027877.
FT   VAR_SEQ     318    318       L -> M (in isoform 2).
FT                                /FTId=VSP_027878.
SQ   SEQUENCE   355 AA;  38600 MW;  331F6BEE31DA0A11 CRC64;
     MSADAAAGEP LPRLCCLEKG PNGYGFHLHG EKGKVGQFIR LVEPGSPAEK SGLLAGDRLV
     EVNGENVEKE THQQVVSRIR AALNAVRLLV VDPETDERLK KLGVSIREEL LRPQEKSEQA
     EPPAAADTHE AGDQNEAEKS HLRELRPRLC TMKKGPNGYG FNLHSDKSKP GQFIRAVDPD
     SPAEASGLRA QDRIVEVNGV CMEGKQHGDV VSAIKGGGDE AKLLVVDKET DEFFKKCKVI
     PSQEHLDGPL PEPFSNGEIQ KESSREALVE PASESPRPAL ARSASSDTSE ELNSQDSPKR
     QVSTEPSSTS SSSSDPILDL NISLAVAKER AHQKRSSKRA PQMDWSKKNE LFSNL
//
ID   4EBP2_MOUSE             Reviewed;         120 AA.
AC   P70445;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Eukaryotic translation initiation factor 4E-binding protein 2;
DE            Short=4E-BP2;
DE            Short=eIF4E-binding protein 2;
DE   AltName: Full=Phosphorylated heat- and acid-stable protein regulated by insulin 2;
DE            Short=PHAS-II;
GN   Name=Eif4ebp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=97094737; PubMed=8939971; DOI=10.1074/jbc.271.47.30199;
RA   Lin T.A., Lawrence J.C. Jr.;
RT   "Control of the translational regulators PHAS-I and PHAS-II by insulin
RT   and cAMP in 3T3-L1 adipocytes.";
RL   J. Biol. Chem. 271:30199-30204(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Regulates eIF4E activity by preventing its assembly into
CC       the eIF4F complex. Mediates the regulation of protein translation
CC       by hormones, growth factors and other stimuli that signal through
CC       the MAP kinase pathway (By similarity).
CC   -!- SUBUNIT: Nonphosphorylated EIF4EBP2 interacts with EIF4E (By
CC       similarity).
CC   -!- PTM: Phosphorylated on serine and threonine residues in response
CC       to insulin, EGF and PDGF (By similarity).
CC   -!- SIMILARITY: Belongs to the eIF4E-binding protein family.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; U75530; AAC52899.1; -; mRNA.
DR   EMBL; BC015082; AAH15082.1; -; mRNA.
DR   IPI; IPI00109318; -.
DR   RefSeq; NP_034254.1; NM_010124.2.
DR   UniGene; Mm.259516; -.
DR   STRING; P70445; -.
DR   PhosphoSite; P70445; -.
DR   PRIDE; P70445; -.
DR   Ensembl; ENSMUST00000020288; ENSMUSP00000020288; ENSMUSG00000020091.
DR   GeneID; 13688; -.
DR   KEGG; mmu:13688; -.
DR   UCSC; uc007fga.1; mouse.
DR   CTD; 13688; -.
DR   MGI; MGI:109198; Eif4ebp2.
DR   eggNOG; roNOG16787; -.
DR   HOGENOM; HBG714775; -.
DR   HOVERGEN; HBG050425; -.
DR   InParanoid; P70445; -.
DR   OMA; RRNSPIA; -.
DR   OrthoDB; EOG47SSG8; -.
DR   PhylomeDB; P70445; -.
DR   NextBio; 284454; -.
DR   ArrayExpress; P70445; -.
DR   Bgee; P70445; -.
DR   Genevestigator; P70445; -.
DR   GermOnline; ENSMUSG00000020091; Mus musculus.
DR   GO; GO:0008190; F:eukaryotic initiation factor 4E binding; IEA:InterPro.
DR   GO; GO:0019933; P:cAMP-mediated signaling; IDA:MGI.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IDA:MGI.
DR   GO; GO:0045947; P:negative regulation of translational initiation; IEA:InterPro.
DR   InterPro; IPR008606; EIF4EBP.
DR   PANTHER; PTHR12669; EIF4EBP; 1.
DR   Pfam; PF05456; eIF_4EBP; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Protein synthesis inhibitor; Translation regulation.
FT   CHAIN         1    120       Eukaryotic translation initiation factor
FT                                4E-binding protein 2.
FT                                /FTId=PRO_0000190517.
FT   MOD_RES      37     37       Phosphothreonine (By similarity).
FT   MOD_RES      41     41       Phosphothreonine (By similarity).
FT   MOD_RES      44     44       Phosphoserine (By similarity).
FT   MOD_RES      45     45       Phosphothreonine (By similarity).
FT   MOD_RES      46     46       Phosphothreonine (By similarity).
FT   MOD_RES      65     65       Phosphoserine; by MAPK1 and MAPK3 (By
FT                                similarity).
SQ   SEQUENCE   120 AA;  12898 MW;  0A1ACC082583F769 CRC64;
     MSASAGGSHQ PSQSRAIPTR TVAISDAAQL PQDYCTTPGG TLFSTTPGGT RIIYDRKFLL
     DRRNSPMAQT PPCHLPNIPG VTSPGALIED SKVEVNNLNN LNNHDRKHAV GDEAQFEMDI
//
ID   FER_MOUSE               Reviewed;         823 AA.
AC   P70451; Q6PEE5; Q80UI3; Q8C481;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Tyrosine-protein kinase Fer;
DE            EC=2.7.10.2;
DE   AltName: Full=Proto-oncogene c-Fer;
DE   AltName: Full=p94-Fer;
GN   Name=Fer; Synonyms=Fert2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Letwin K., Pawson T.;
RT   "Murine Fer.";
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6, and FVB/N-3; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 125-823 (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Tyrosine kinase of the non-receptor type. Probably
CC       performs an important function, perhaps in regulatory processes
CC       such as cell cycle control (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Associated with the chromatin.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P70451-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P70451-2; Sequence=VSP_021634;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Fes/fps subfamily.
CC   -!- SIMILARITY: Contains 1 FCH domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U76762; AAB18988.1; -; mRNA.
DR   EMBL; BC051249; AAH51249.1; -; mRNA.
DR   EMBL; BC058100; AAH58100.1; -; mRNA.
DR   EMBL; AK082799; BAC38626.1; -; mRNA.
DR   IPI; IPI00109334; -.
DR   IPI; IPI00808015; -.
DR   RefSeq; NP_001033086.2; NM_001037997.2.
DR   RefSeq; NP_032026.2; NM_008000.2.
DR   UniGene; Mm.23039; -.
DR   HSSP; P07332; 1WQU.
DR   ProteinModelPortal; P70451; -.
DR   SMR; P70451; 453-820.
DR   STRING; P70451; -.
DR   PhosphoSite; P70451; -.
DR   PRIDE; P70451; -.
DR   Ensembl; ENSMUST00000000129; ENSMUSP00000000129; ENSMUSG00000000127.
DR   Ensembl; ENSMUST00000112833; ENSMUSP00000108452; ENSMUSG00000000127.
DR   GeneID; 14158; -.
DR   KEGG; mmu:14158; -.
DR   UCSC; uc008dfo.1; mouse.
DR   UCSC; uc008dfq.1; mouse.
DR   CTD; 14158; -.
DR   MGI; MGI:105917; Fer.
DR   eggNOG; roNOG11122; -.
DR   GeneTree; ENSGT00600000084126; -.
DR   HOGENOM; HBG446727; -.
DR   HOVERGEN; HBG005655; -.
DR   InParanoid; P70451; -.
DR   OMA; RHFIIQY; -.
DR   OrthoDB; EOG4JM7P1; -.
DR   BRENDA; 2.7.10.2; 244.
DR   NextBio; 285280; -.
DR   ArrayExpress; P70451; -.
DR   Bgee; P70451; -.
DR   Genevestigator; P70451; -.
DR   GermOnline; ENSMUSG00000000127; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:EC.
DR   GO; GO:0007155; P:cell adhesion; IMP:MGI.
DR   GO; GO:0006935; P:chemotaxis; IMP:MGI.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IEA:InterPro.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR   GO; GO:0007165; P:signal transduction; IDA:MGI.
DR   InterPro; IPR001060; FCH.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR016250; Tyr_kinase_non-rcpt_Fes_subgr.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PIRSF; PIRSF000632; TyrPK_fps; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50133; FCH; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Kinase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Proto-oncogene;
KW   SH2 domain; Transferase; Tyrosine-protein kinase.
FT   CHAIN         1    823       Tyrosine-protein kinase Fer.
FT                                /FTId=PRO_0000260825.
FT   DOMAIN        1     58       FCH.
FT   DOMAIN      461    551       SH2.
FT   DOMAIN      564    817       Protein kinase.
FT   NP_BIND     570    578       ATP (By similarity).
FT   ACT_SITE    685    685       Proton acceptor (By similarity).
FT   BINDING     592    592       ATP (By similarity).
FT   MOD_RES     402    402       Phosphotyrosine.
FT   MOD_RES     410    410       Phosphothreonine (By similarity).
FT   MOD_RES     411    411       Phosphoserine (By similarity).
FT   MOD_RES     434    434       Phosphoserine (By similarity).
FT   MOD_RES     715    715       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   VAR_SEQ      70    127       Missing (in isoform 2).
FT                                /FTId=VSP_021634.
FT   CONFLICT    328    328       A -> G (in Ref. 3; BAC38626).
FT   CONFLICT    373    373       T -> S (in Ref. 1; AAB18988).
FT   CONFLICT    444    444       Missing (in Ref. 3; BAC38626).
SQ   SEQUENCE   823 AA;  94579 MW;  F4C22E1E63721663 CRC64;
     MGFGSDLKNS QEAVLKLQDW ELRLLETVKK FMALRIKSDK EYAYTLQNLC NQVDKESTVQ
     VNYVSNVSKS WLLMIQQTEQ LSRIMKTHAE DLNSGPLHRL TMMIKDKQQV KKSYVGIHQQ
     IEAEMIKVTK TELEKLKSSY RQLIKEMNSA KEKYKEALAK GKETEKAKER YDKATMKLHM
     LHNQYVLALK GAQLHQSQYY DTTLPLLLDS VQKMQEEMIK ALKGIFDDYS QITSLVTEEI
     VNVHKEIQMS VEQIDPSTEY NNFIDVHRTT AAKEQEIEFD TSLLEENENL QANEIMWNNL
     TADSLQVMLK TLAEELTQTQ QMLLHKEAAV LELEKRIEES FETCEKKSDI VLLLGQKQAL
     EELKQSVQQL RCTEAKCAAQ KALLEQKVQE NDGKEPPPVV NYEEDARSVT SMERKERLSK
     FESIRHSIAG IIKSPKSVLG SSTQVCDVIS VGERPLAEHD WYHGAIPRIE AQELLKQQGD
     FLVRESHGKP GEYVLSVYSD GQRRHFIIQF VDNLYRFEGT GFSNIPQLID HHFNTKQVIT
     KKSGVVLLNP IPKDKKWVLN HEDVSLGELL GKGNFGEVYK GTLKDKTPVA IKTCKEDLPQ
     ELKIKFLQEA KILKQYDHPN IVKLIGVCTQ RQPVYIIMEL VPGGDFLTFL RKRKDELKLK
     QLVRFSLDVA AGMLYLESKN CIHRDLAARN CLVGENNTLK ISDFGMSRQE DGGVYSSSGL
     KQIPIKWTAP EALNYGRYSS ESDVWSFGIL LWETFSLGVC PYPGMTNQQA REQVERGYRM
     SAPQNCPEEV FTIMMKCWDY KPENRPKFND LHKELTVIKK MIT
//
ID   STX4_MOUSE              Reviewed;         298 AA.
AC   P70452; Q3TSL5; Q3UKQ8; Q80WT8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Syntaxin-4;
GN   Name=Stx4; Synonyms=Stx4a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH STXB3, AND
RP   SUBCELLULAR LOCATION.
RC   TISSUE=Adipocyte;
RX   MEDLINE=97197781; PubMed=9045631; DOI=10.1074/jbc.272.10.6179;
RA   Tellam J.T., Macaulay S.L., McIntosh S., Hewish D.R., Ward C.W.,
RA   James D.E.;
RT   "Characterization of Munc-18c and syntaxin-4 in 3T3-L1 adipocytes.
RT   Putative role in insulin-dependent movement of GLUT-4.";
RL   J. Biol. Chem. 272:6179-6186(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, Czech II, and FVB/N; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH STXBP4; SNAP23 AND VAMP2.
RX   MEDLINE=99322667; PubMed=10394363; DOI=10.1016/S1097-2765(01)80007-1;
RA   Min J., Okada S., Kanzaki M., Elmendorf J.S., Coker K.J., Ceresa B.P.,
RA   Syu L.-J., Noda Y., Saltiel A.R., Pessin J.E.;
RT   "Synip: a novel insulin-regulated syntaxin 4-binding protein mediating
RT   GLUT4 translocation in adipocytes.";
RL   Mol. Cell 3:751-760(1999).
RN   [5]
RP   INTERACTION WITH SNAP23 AND SNAPIN.
RX   PubMed=12877659; DOI=10.1042/BJ20030427;
RA   Buxton P., Zhang X.-M., Walsh B., Sriratana A., Schenberg I.,
RA   Manickam E., Rowe T.;
RT   "Identification and characterization of Snapin as a ubiquitously
RT   expressed SNARE-binding protein that interacts with SNAP23 in non-
RT   neuronal cells.";
RL   Biochem. J. 375:433-440(2003).
RN   [6]
RP   IDENTIFICATION IN A COMPLEX WITH VAMP8 AND SNAP23.
RX   PubMed=15363411; DOI=10.1016/j.devcel.2004.08.002;
RA   Wang C.-C., Ng C.P., Lu L., Atlashkin V., Zhang W., Seet L.-F.,
RA   Hong W.;
RT   "A role of VAMP8/endobrevin in regulated exocytosis of pancreatic
RT   acinar cells.";
RL   Dev. Cell 7:359-371(2004).
RN   [7]
RP   INTERACTION WITH LLGL1.
RX   PubMed=11809830; DOI=10.1091/mbc.01-10-0496;
RA   Musch A., Cohen D., Yeaman C., Nelson W.J., Rodriguez-Boulan E.,
RA   Brennwald P.J.;
RT   "Mammalian homolog of Drosophila tumor suppressor lethal (2) giant
RT   larvae interacts with basolateral exocytic machinery in Madin-Darby
RT   canine kidney cells.";
RL   Mol. Biol. Cell 13:158-168(2002).
RN   [8]
RP   INTERACTION WITH STXBP3 AND VAMP2.
RX   PubMed=17548353; DOI=10.1074/jbc.M701661200;
RA   Ke B., Oh E., Thurmond D.C.;
RT   "Doc2beta is a novel Munc18c-interacting partner and positive effector
RT   of syntaxin 4-mediated exocytosis.";
RL   J. Biol. Chem. 282:21786-21797(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [10]
RP   FUNCTION, INTERACTION WITH CENPF, AND SUBCELLULAR LOCATION.
RX   PubMed=18827011; DOI=10.1242/jcs.032847;
RA   Pooley R.D., Moynihan K.L., Soukoulis V., Reddy S., Francis R., Lo C.,
RA   Ma L.-J., Bader D.M.;
RT   "Murine CENPF interacts with syntaxin 4 in the regulation of vesicular
RT   transport.";
RL   J. Cell Sci. 121:3413-3421(2008).
RN   [11]
RP   INTERACTION WITH DOC2B.
RX   PubMed=19033398; DOI=10.2337/db08-0303;
RA   Fukuda N., Emoto M., Nakamori Y., Taguchi A., Miyamoto S., Uraki S.,
RA   Oka Y., Tanizawa Y.;
RT   "DOC2B: a novel syntaxin-4 binding protein mediating insulin-regulated
RT   GLUT4 vesicle fusion in adipocytes.";
RL   Diabetes 58:377-384(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-29, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Plasma membrane t-SNARE that mediates docking of
CC       transport vesicles. Necessary for the translocation of SLC2A4 from
CC       intracellular vesicles to the plasma membrane. Together with STXB3
CC       and VAMP2, may also play a role in docking/fusion of intracellular
CC       GLUT4-containing vesicles with the cell surface in adipocytes and
CC       in docking of synaptic vesicles at presynaptic active zones.
CC   -!- SUBUNIT: Interacts with STXBP6. Component of the SNARE complex
CC       composed of STX4, SNAP23 and VAMP7 that interacts with SYT7 during
CC       lysosomal exocytosis (By similarity). Found in a complex with
CC       VAMP8 and SNAP23. Detected in a complex with SNAP23 and STXBP4.
CC       Interacts with VAMP2. Interacts with SNAP23 and SNAPIN. Interacts
CC       with LLGL1. Interacts (via C-terminus) with CENPF. Interacts with
CC       DOC2B. Interacts with STXBP3; excludes interaction with DOC2B and
CC       SNAP25. Interacts with STXBP4; excludes interaction with VAMP2.
CC   -!- INTERACTION:
CC       Q155P7:Cenpf; NbExp=4; IntAct=EBI-645716, EBI-2211248;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type IV membrane
CC       protein (Potential).
CC   -!- SIMILARITY: Belongs to the syntaxin family.
CC   -!- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain.
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DR   EMBL; U76832; AAB18991.1; -; mRNA.
DR   EMBL; AK145909; BAE26743.1; -; mRNA.
DR   EMBL; AK161971; BAE36660.1; -; mRNA.
DR   EMBL; BC005791; AAH05791.1; -; mRNA.
DR   EMBL; BC011491; AAH11491.1; -; mRNA.
DR   EMBL; BC052023; AAH52023.1; -; mRNA.
DR   IPI; IPI00109335; -.
DR   RefSeq; NP_033320.1; NM_009294.3.
DR   UniGene; Mm.24867; -.
DR   PDB; 2PJX; X-ray; 3.15 A; C/D=1-29.
DR   PDBsum; 2PJX; -.
DR   ProteinModelPortal; P70452; -.
DR   SMR; P70452; 35-293.
DR   IntAct; P70452; 13.
DR   MINT; MINT-269272; -.
DR   STRING; P70452; -.
DR   PhosphoSite; P70452; -.
DR   PRIDE; P70452; -.
DR   Ensembl; ENSMUST00000033075; ENSMUSP00000033075; ENSMUSG00000030805.
DR   Ensembl; ENSMUST00000121705; ENSMUSP00000112927; ENSMUSG00000030805.
DR   GeneID; 20909; -.
DR   KEGG; mmu:20909; -.
DR   UCSC; uc009jwy.1; mouse.
DR   CTD; 20909; -.
DR   MGI; MGI:893577; Stx4a.
DR   eggNOG; roNOG13912; -.
DR   GeneTree; ENSGT00550000074334; -.
DR   HOGENOM; HBG717663; -.
DR   HOVERGEN; HBG000497; -.
DR   InParanoid; P70452; -.
DR   OMA; QHGVLSQ; -.
DR   OrthoDB; EOG4Z62PD; -.
DR   PhylomeDB; P70452; -.
DR   NextBio; 299793; -.
DR   ArrayExpress; P70452; -.
DR   Bgee; P70452; -.
DR   CleanEx; MM_STX4A; -.
DR   Genevestigator; P70452; -.
DR   GermOnline; ENSMUSG00000030805; Mus musculus.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR   GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR   GO; GO:0000149; F:SNARE binding; IPI:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR   InterPro; IPR006011; Syntaxin_N.
DR   InterPro; IPR010989; t-SNARE.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   Pfam; PF05739; SNARE; 1.
DR   Pfam; PF00804; Syntaxin; 1.
DR   SMART; SM00503; SynN; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF47661; t-snare; 1.
DR   PROSITE; PS00914; SYNTAXIN; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Coiled coil; Membrane;
KW   Neurotransmitter transport; Phosphoprotein; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    298       Syntaxin-4.
FT                                /FTId=PRO_0000210203.
FT   TOPO_DOM      1    274       Cytoplasmic (Potential).
FT   TRANSMEM    275    295       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   TOPO_DOM    296    298       Extracellular (Potential).
FT   DOMAIN      200    262       t-SNARE coiled-coil homology.
FT   REGION      154    298       Interaction with CENPF.
FT   COILED       38    163       Potential.
FT   MOD_RES      15     15       Phosphoserine.
FT   MOD_RES      29     29       Phosphoserine.
FT   MOD_RES     115    115       Phosphotyrosine (By similarity).
FT   MOD_RES     117    117       Phosphoserine.
FT   MOD_RES     251    251       Phosphotyrosine (By similarity).
FT   CONFLICT     47     47       T -> I (in Ref. 3; AAH52023).
FT   CONFLICT    141    141       C -> Y (in Ref. 2; BAE36660).
FT   CONFLICT    281    281       S -> Y (in Ref. 2; BAE26743).
FT   HELIX         5      9
FT   TURN         13     18
SQ   SEQUENCE   298 AA;  34165 MW;  FCD1477E1126CEC1 CRC64;
     MRDRTHELRQ GDNISDDEDE VRVALVVHSG AARLGSPDDE FFQKVQTIRQ TMAKLESKVR
     ELEKQQVTIL ATPLPEESMK QGLQNLREEI KQLGREVRAQ LKAIEPQKEE ADENYNSVNT
     RMKKTQHGVL SQQFVELINK CNSMQSEYRE KNVERIRRQL KITNAGMVSD EELEQMLDSG
     QSEVFVSNIL KDTQVTRQAL NEISARHSEI QQLERSIREL HEIFTFLATE VEMQGEMINR
     IEKNILSSAD YVERGQEHVK IALENQKKAR KKKVMIAICV SVTVLILAVI IGITITVG
//
ID   VASP_MOUSE              Reviewed;         375 AA.
AC   P70460; Q3TAP0; Q3TCD2; Q3U0C2; Q3UDF1; Q91VD2; Q9R214;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Vasodilator-stimulated phosphoprotein;
DE            Short=VASP;
GN   Name=Vasp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-209.
RC   STRAIN=129;
RX   MEDLINE=96411679; PubMed=8812448; DOI=10.1006/geno.1996.0457;
RA   Zimmer M., Fink T., Fischer L., Hauser W., Scherer K., Lichter P.,
RA   Walter U.;
RT   "Cloning of the VASP (vasodilator-stimulated phosphoprotein) genes in
RT   human and mouse: structure, sequence, and chromosomal localization.";
RL   Genomics 36:227-233(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99185054; PubMed=10085070; DOI=10.1074/jbc.274.13.8391;
RA   Collins S.P., Uhler M.D.;
RT   "Cyclic AMP- and cyclic GMP-dependent protein kinases differ in their
RT   regulation of cyclic AMP response element-dependent gene
RT   transcription.";
RL   J. Biol. Chem. 274:8391-8404(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-209.
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Adipose tissue, Bone marrow, Dendritic cell, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   MEDLINE=99166867; PubMed=10069337; DOI=10.1016/S0896-6273(00)81092-2;
RA   Lanier L.M., Gates M.A., Witke W., Menzies A.S., Wehman A.M.,
RA   Macklis J.D., Kwiatkowski D., Soriano P., Gertler F.B.;
RT   "Mena is required for neurulation and commissure formation.";
RL   Neuron 22:313-325(1999).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=10660044; DOI=10.1016/S0092-8674(00)81559-7;
RA   Vasioukhin V., Bauer C., Yin M., Fuchs E.;
RT   "Directed actin polymerization is the driving force for epithelial
RT   cell-cell adhesion.";
RL   Cell 100:209-219(2000).
RN   [7]
RP   INTERACTION WITH ACTN1; PFN1; PFN2; VCL AND ZYX, PHOSPHORYLATION, AND
RP   MUTAGENESIS OF SER-153; SER-235 AND THR-274.
RX   PubMed=10882740; DOI=10.1074/jbc.M005066200;
RA   Harbeck B., Huttelmaier S., Schlueter K., Jockusch B.M.,
RA   Illenberger S.;
RT   "Phosphorylation of the vasodilator-stimulated phosphoprotein
RT   regulates its interaction with actin.";
RL   J. Biol. Chem. 275:30817-30825(2000).
RN   [8]
RP   INTERACTION WITH ACTG1, PHOSPHORYLATION, AND MUTAGENESIS OF
RP   232-ARG-LYS-233.
RX   PubMed=12372613; DOI=10.1016/S0014-5793(02)03356-2;
RA   Walders-Harbeck B., Khaitlina S.Y., Hinssen H., Jockusch B.M.,
RA   Illenberger S.;
RT   "The vasodilator-stimulated phosphoprotein promotes actin
RT   polymerisation through direct binding to monomeric actin.";
RL   FEBS Lett. 529:275-280(2002).
RN   [9]
RP   INTERACTION WITH DNMBP.
RX   PubMed=14506234; DOI=10.1074/jbc.M308104200;
RA   Salazar M.A., Kwiatkowski A.V., Pellegrini L., Cestra G., Butler M.H.,
RA   Rossman K.L., Serna D.M., Sondek J., Gertler F.B., De Camilli P.;
RT   "Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology
RT   domains, links dynamin to regulation of the actin cytoskeleton.";
RL   J. Biol. Chem. 278:49031-49043(2003).
RN   [10]
RP   INTERACTION WITH APBB1IP.
RX   PubMed=15642358; DOI=10.1016/j.febslet.2004.10.110;
RA   Jenzora A., Behrendt B., Small J.V., Wehland J., Stradal T.E.;
RT   "PREL1 provides a link from Ras signalling to the actin cytoskeleton
RT   via Ena/VASP proteins.";
RL   FEBS Lett. 579:455-463(2005).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317 AND SER-318, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Ena/VASP proteins are actin-associated proteins involved
CC       in a range of processes dependent on cytoskeleton remodeling and
CC       cell polarity such as axon guidance, lamellipodial and filopodial
CC       dynamics, platelet activation and cell migration. VASP promotes
CC       actin filament elongation. It protects the barbed end of growing
CC       actin filaments against capping and increases the rate of actin
CC       polymerization in the presence of capping protein. VASP stimulates
CC       actin filament elongation by promoting the transfer of profilin-
CC       bound actin monomers onto the barbed end of growing actin
CC       filaments. Plays a role in actin-based mobility of Listeria
CC       monocytogenes in host cells. Regulates actin dynamics in platelets
CC       and plays an important role in regulating platelet aggregation (By
CC       similarity).
CC   -!- SUBUNIT: Homotetramer (By similarity). Interacts with PFN1, PFN2,
CC       LPP, ACTN1 and ACTG1. Interacts, via the EVH1 domain, with the
CC       Pro-rich regions of ZYX. This interaction is important for
CC       targeting to focal adhesions and the formation of actin-rich
CC       structures at the apical surface of cells. Interacts, via the EVH1
CC       domain, with the Pro-rich domain of Listeria monocytogenes actA.
CC       Interacts with APBB1IP. Interacts, via the Pro-rich domain, with
CC       the C-terminal SH3 domain of DNMBP.
CC   -!- INTERACTION:
CC       Q9JJV2-1:Pfn2; NbExp=1; IntAct=EBI-990384, EBI-990256;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell
CC       junction, focal adhesion. Cell projection, lamellipodium membrane.
CC       Cell projection, filopodium membrane. Note=Targeted to stress
CC       fibers and focal adhesions through interaction with a number of
CC       proteins including MRL family members. Localizes to the plasma
CC       membrane in protruding lamellipodia and filopodial tips.
CC       Stimulation by thrombin or PMA, also translocates VASP to focal
CC       adhesions.
CC   -!- TISSUE SPECIFICITY: Highly expressed in thymus and spleen. Lower
CC       levels in lung, ovary, placenta and fat.
CC   -!- DEVELOPMENTAL STAGE: Expressed constantly throughout brain
CC       development, with lower levels in adulthood.
CC   -!- DOMAIN: The EVH2 domain is comprised of 3 regions. Block A is a
CC       thymosin-like domain required for G-actin binding. The KLKR motif
CC       within this block is essential for the G-actin binding and for
CC       actin polymerization. Block B is required for F-actin binding and
CC       subcellular location, and Block C for tetramerization.
CC   -!- DOMAIN: The WH1 domain mediates interaction with XIRP1 (By
CC       similarity).
CC   -!- PTM: Major substrate for cAMP-dependent (PKA) and cGMP-dependent
CC       protein kinase (PKG) in platelets. The preferred site for PKA is
CC       Ser-153, the preferred site for PKG, Ser-235. In ADP-activated
CC       platelets, phosphorylation by PKA or PKG on Ser-153 leads to
CC       fibrinogen receptor inhibition. Phosphorylation on Thr-274
CC       requires prior phosphorylation on Ser-153 and Ser-235. In response
CC       to phorbol ester (PMA) stimulation, phosphorylated by PKC/PRKCA.
CC       In response to thrombin, phosphorylated by both PKC and ROCK1.
CC       Phosphorylation at Thr-274 by AMPK does not require prior
CC       phosphorylation at Ser-153 or Ser-235. Phosphorylation modulates
CC       F-actin binding, actin filament elongation and platelet
CC       activation. Carbon monoxide (CO) promotes phosphorylation at Ser-
CC       153, while nitric oxide (NO) promotes phosphorylation at Ser-153,
CC       but also at Ser-235 (By similarity).
CC   -!- SIMILARITY: Belongs to the Ena/VASP family.
CC   -!- SIMILARITY: Contains 1 WH1 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA67108.1; Type=Erroneous gene model prediction;
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DR   EMBL; X98475; CAA67108.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF084548; AAD16045.1; -; mRNA.
DR   EMBL; AK140329; BAE24338.1; -; mRNA.
DR   EMBL; AK150103; BAE29310.1; -; mRNA.
DR   EMBL; AK157021; BAE33933.1; -; mRNA.
DR   EMBL; AK170780; BAE42025.1; -; mRNA.
DR   EMBL; AK171715; BAE42628.1; -; mRNA.
DR   EMBL; BC010223; AAH10223.1; -; mRNA.
DR   EMBL; BC015289; AAH15289.1; -; mRNA.
DR   IPI; IPI00624876; -.
DR   RefSeq; NP_033525.2; NM_009499.2.
DR   UniGene; Mm.9684; -.
DR   ProteinModelPortal; P70460; -.
DR   SMR; P70460; 1-115, 333-372.
DR   IntAct; P70460; 1.
DR   MINT; MINT-1215713; -.
DR   STRING; P70460; -.
DR   PhosphoSite; P70460; -.
DR   PRIDE; P70460; -.
DR   Ensembl; ENSMUST00000032561; ENSMUSP00000032561; ENSMUSG00000030403.
DR   GeneID; 22323; -.
DR   KEGG; mmu:22323; -.
DR   UCSC; uc009fld.1; mouse.
DR   CTD; 22323; -.
DR   MGI; MGI:109268; Vasp.
DR   eggNOG; roNOG16319; -.
DR   GeneTree; ENSGT00440000039080; -.
DR   HOVERGEN; HBG006655; -.
DR   InParanoid; P70460; -.
DR   OMA; GTGPQAF; -.
DR   OrthoDB; EOG49GKHQ; -.
DR   PhylomeDB; P70460; -.
DR   NextBio; 302545; -.
DR   ArrayExpress; P70460; -.
DR   Bgee; P70460; -.
DR   CleanEx; MM_VASP; -.
DR   Genevestigator; P70460; -.
DR   GermOnline; ENSMUSG00000030403; Mus musculus.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0031527; C:filopodium membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR   GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IGI:MGI.
DR   GO; GO:0007411; P:axon guidance; IGI:MGI.
DR   GO; GO:0001843; P:neural tube closure; IGI:MGI.
DR   InterPro; IPR000697; EVH1.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR017354; Vasodilator_phosphoprotein.
DR   InterPro; IPR014885; VASP_tetra.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF08776; VASP_tetra; 1.
DR   Pfam; PF00568; WH1; 1.
DR   PIRSF; PIRSF038010; Vasodilator_Phospo; 1.
DR   SMART; SM00461; WH1; 1.
DR   PROSITE; PS50229; WH1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Cell junction; Cell membrane;
KW   Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Membrane;
KW   Phosphoprotein; Polymorphism; Repeat; SH3-binding.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    375       Vasodilator-stimulated phosphoprotein.
FT                                /FTId=PRO_0000065768.
FT   DOMAIN        2    113       WH1.
FT   REPEAT      340    354       1.
FT   REPEAT      355    369       2.
FT   REGION      221    373       EVH2.
FT   REGION      221    241       EVH2 block A.
FT   REGION      257    274       EVH2 block B.
FT   REGION      338    372       EVH2 block C.
FT   REGION      339    368       2 X 15 AA tandem repeats of L-[EQ]-[KR]
FT                                [MV]-K-[EQ]-E-[IL]-[IL]-E-[AEV]-[FV]-
FT                                [KRV]-[KQ]-E.
FT   COILED      337    367       Potential.
FT   MOTIF       230    233       KLKR.
FT   COMPBIAS    166    182       Poly-Pro.
FT   COMPBIAS    317    320       Poly-Ser.
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES     153    153       Phosphoserine; by PKA, PKC, PKG and
FT                                ROCK1.
FT   MOD_RES     235    235       Phosphoserine; by PKA and PKG.
FT   MOD_RES     274    274       Phosphothreonine; by PKA, PKG and AMPK
FT                                (By similarity).
FT   MOD_RES     279    279       N6-acetyllysine (By similarity).
FT   MOD_RES     311    311       Phosphothreonine (By similarity).
FT   MOD_RES     317    317       Phosphoserine.
FT   MOD_RES     318    318       Phosphoserine.
FT   VARIANT     209    209       A -> T.
FT   MUTAGEN     153    153       S->D: Reduces actin polymerization to a
FT                                lesser extent than wild-type. Greater
FT                                effect on actin polymerization; when
FT                                associated with D-235 and E-274.
FT   MUTAGEN     232    233       RK->GE,EE: Reduced binding to monomeric
FT                                actin. No VASP-induced actin
FT                                polymerization.
FT   MUTAGEN     235    235       S->D: Reduces actin polymerization to a
FT                                lesser extent than wild-type.
FT   MUTAGEN     274    274       T->E: Reduces actin polymerization to a
FT                                lesser extent than wild-type.
FT   CONFLICT    106    115       Missing (in Ref. 3; BAE42025).
FT   CONFLICT    237    237       Missing (in Ref. 3; BAE33933).
FT   CONFLICT    337    337       S -> Y (in Ref. 3; BAE29310).
SQ   SEQUENCE   375 AA;  39667 MW;  19369286CF4276C7 CRC64;
     MSETVICSSR ATVMLYDDSN KRWLPAGTGP QAFSRVQIYH NPTANSFRVV GRKMQPDQQV
     VINCAIIRGV KYNQATPIFH QWRDARQVWG LNFGSKEDAI QFATGMANAL EALEGGGPPP
     APAPPAWSAQ NGPSPEELEQ QKRQPEHMER RVSNAGGPPA PPAGGPPPPP GPPPPPGPPP
     PPGLPSSGVS GAGHGAGAAP PPAPPLPTAQ GPNSGGSGAP GLAAAIAGAK LRKVSKQEEA
     SGGPLAPKAE NSRSTGGGLM EEMNAMLARR RKATQVGEKP PKDESASEES EARLPAQSEP
     VRRPWEKNST TLPRMKSSSS VTTSEAHPST PCSSDDSDLE RVKQELLEEV RKELQKMKEE
     IIEVFVQELR KRGSP
//
ID   CXCR4_MOUSE             Reviewed;         359 AA.
AC   P70658; O09059; O09062; P70233; P70346; Q4KMW1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   08-MAR-2011, entry version 104.
DE   RecName: Full=C-X-C chemokine receptor type 4;
DE            Short=CXC-R4;
DE            Short=CXCR-4;
DE   AltName: Full=Fusin;
DE   AltName: Full=Leukocyte-derived seven transmembrane domain receptor;
DE            Short=LESTR;
DE   AltName: Full=Pre-B-cell-derived chemokine receptor;
DE            Short=PB-CKR;
DE   AltName: Full=Stromal cell-derived factor 1 receptor;
DE            Short=SDF-1 receptor;
DE   AltName: CD_antigen=CD184;
GN   Name=Cxcr4; Synonyms=Cmkar4, Lestr, Sdf1r;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM CXCR4-B).
RC   STRAIN=129/Sv, and C57BL/6J; TISSUE=Peritoneal exudate;
RX   MEDLINE=97113334; PubMed=8955194;
RA   Heesen M., Berman M.A., Benson J.D., Gerard C., Dorf M.E.;
RT   "Cloning of the mouse fusin gene, homologue to a human HIV-1 co-
RT   factor.";
RL   J. Immunol. 157:5455-5460(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CXCR4-B).
RC   TISSUE=Pre-B cell;
RX   MEDLINE=97121456; PubMed=8962122; DOI=10.1073/pnas.93.25.14726;
RA   Nagasawa T., Nakajima T., Tachibana K., Iizasa H., Bleul C.C.,
RA   Yoshie O., Matsushima K., Yoshida N., Springer T.A., Kishimoto T.;
RT   "Molecular cloning and characterization of a murine pre-B-cell growth-
RT   stimulating factor/stromal cell-derived factor 1 receptor, a murine
RT   homolog of the human immunodeficiency virus 1 entry coreceptor
RT   fusin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:14726-14729(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CXCR4-B).
RC   STRAIN=129/Sv; TISSUE=Thymus;
RA   Schubel A., Burgstahler R., Lipp M.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS CXCR4-A AND
RP   CXCR4-B).
RC   STRAIN=C57BL/6J X CBA/J; TISSUE=Thymus;
RX   MEDLINE=97439495; PubMed=9295051; DOI=10.1002/eji.1830270839;
RA   Moepps B., Frodl R., Rodewald H.-R., Baggiolini M., Gierschik P.;
RT   "Two murine homologues of the human chemokine receptor CXCR4 mediating
RT   stromal cell-derived factor 1alpha activation of Gi2 are
RT   differentially expressed in vivo.";
RL   Eur. J. Immunol. 27:2102-2112(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS CXCR4-A AND CXCR4-B).
RX   MEDLINE=97256574; PubMed=9103415;
RA   Heesen M., Berman M.A., Hoepken U.E., Gerard N.P., Dorf M.E.;
RT   "Alternate splicing of mouse fusin/CXC chemokine receptor-4: stromal
RT   cell-derived factor-1alpha is a ligand for both CXC chemokine
RT   receptor-4 isoforms.";
RL   J. Immunol. 158:3561-3564(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CXCR4-B).
RC   STRAIN=C57BL/6; TISSUE=Thymus;
RA   Suzuki G., Nakata Y., Uzawa A., Shirasawa T., Saito T., Mita K.;
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CXCR4-B).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   ALTERNATIVE SPLICING.
RX   MEDLINE=99095114; PubMed=9879064;
RA   Frodl R., Gierschik P., Moepps B.;
RT   "Genomic organization and expression of the CXCR4 gene in mouse and
RT   man: absence of a splice variant corresponding to mouse CXCR4-B in
RT   human tissues.";
RL   J. Recept. Signal Transduct. 18:321-344(1998).
RN   [9]
RP   FUNCTION.
RX   MEDLINE=98295994; PubMed=9634237; DOI=10.1038/31261;
RA   Tachibana K., Hirota S., Iizasa H., Yoshida H., Kawabata K.,
RA   Kataoka Y., Kitamura Y., Matsushima K., Yoshida N., Nishikawa S.,
RA   Kishimoto T., Nagasawa T.;
RT   "The chemokine receptor CXCR4 is essential for vascularization of the
RT   gastrointestinal tract.";
RL   Nature 393:591-594(1998).
RN   [10]
RP   FUNCTION.
RX   MEDLINE=98295995; PubMed=9634238; DOI=10.1038/31269;
RA   Zou Y.-R., Kottmann A.H., Kuroda M., Taniuchi I., Littman D.R.;
RT   "Function of the chemokine receptor CXCR4 in haematopoiesis and in
RT   cerebellar development.";
RL   Nature 393:595-599(1998).
RN   [11]
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=ICR;
RX   MEDLINE=99410349; PubMed=10479460; DOI=10.1006/dbio.1999.9405;
RA   McGrath K.E., Koniski A.D., Maltby K.M., McGann J.K., Palis J.;
RT   "Embryonic expression and function of the chemokine SDF-1 and its
RT   receptor, CXCR4.";
RL   Dev. Biol. 213:442-456(1999).
RN   [12]
RP   INTERACTION WITH CD164.
RX   PubMed=18227060; DOI=10.1074/jbc.M706730200;
RA   Bae G.-U., Gaio U., Yang Y.-J., Lee H.-J., Kang J.-S., Krauss R.S.;
RT   "Regulation of myoblast motility and fusion by the CXCR4-associated
RT   sialomucin, CD164.";
RL   J. Biol. Chem. 283:8301-8309(2008).
CC   -!- FUNCTION: Receptor for the C-X-C chemokine CXCL12/SDF-1 that
CC       transduces a signal by increasing intracellular calcium ions
CC       levels and enhancing MAPK1/MAPK3 activation. Acts as a receptor
CC       for extracellular ubiquitin; leading to enhance intracellular
CC       calcium ions and reduce cellular cAMP levels. Involved in
CC       haematopoiesis and in cardiac ventricular septum formation. Plays
CC       also an essential role in vascularization of the gastrointestinal
CC       tract, probably by regulating vascular branching and/or remodeling
CC       processes in endothelial cells. Could be involved in cerebellar
CC       development. In the CNS, could mediate hippocampal-neuron
CC       survival.
CC   -!- SUBUNIT: Monomer (By similarity). Can form dimers (By similarity).
CC       Interacts with ARRB2; the interaction is dependent on the C-
CC       terminal phosphorylation of CXCR4 and allows activation of MAPK1
CC       and MAPK3. Interacts with ARRC; the interaction is dependent on
CC       the C-terminal phosphorylation of CXCR4 and modulates calcium
CC       mobilization. Interacts (via the cytoplasmic C-terminal) with ITCH
CC       (via the WW domains I and II); the interaction, enhanced by
CC       CXCL12, ubiquitinates CXCR4 and leads to its degradation.
CC       Interacts with extracellular ubiquitin; the interaction enhances
CC       intracellular calcium ions and reduces cellular cAMP levels (By
CC       similarity). Interacts with CD164.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity). Note=In unstimulated cells, diffuse pattern on
CC       plasma membrane. On agonist stimulation, colocalizes with ITCH at
CC       the plasma membrane where it becomes ubiquitinated (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=CXCR4-B; Synonyms=LESTR-B;
CC         IsoId=P70658-1; Sequence=Displayed;
CC       Name=CXCR4-A; Synonyms=LESTR-A;
CC         IsoId=P70658-2; Sequence=VSP_001891;
CC   -!- TISSUE SPECIFICITY: Lymphocytes, macrophages, neutrophils,
CC       microglial cells and astrocytes. Found in spleen, thymus, bone
CC       marrow, lymph nodes and, at lower levels in brain, small
CC       intestine, stomach and kidney. CXCR4-A is predominant in all
CC       tissues tested.
CC   -!- DEVELOPMENTAL STAGE: High expression during embryonic development
CC       does not seem to be associated with the differentiation of any
CC       particular cell type, but is widely utilized when there is a
CC       requirement for cell movement. Frequently associated with less
CC       differentiated cell types and down-regulated with subsequent
CC       differentiation. Detected in sites with haemopoietic potential:
CC       the yolk sac (7.5, 8.5 and 12.5 dpc) and fetal liver (12.5 dpc).
CC       During gastrulation, at 7.2 to 7.8 dpc, expressed in the mesoderm
CC       and the definitive endoderm. As gastrulation pattern fades (8.5
CC       dpc), expression in the mesoderm is down-regulated, while it
CC       becomes predominant in neural ectoderm. Endodermal expression is
CC       retained in the foregut and later in a subset of foregut
CC       derivatives, including the stomach (10.5 dpc), the cystic ducts of
CC       the gall bladder and the lung epithelium (12.5 dpc). In neuronal
CC       tissue: at 10.5 and 12.5 dpc, expressed in the dorsal root
CC       ganglia, in the ventral mantle layer of the spinal cord (or basal
CC       plates), in the hindbrain. At 14.5 dpc, expression more tightly
CC       confined to the neural epithelium lining the ventricular space and
CC       to the external granular layer of the ventral rhombic lip (the
CC       developing cerebellum). Expressed in the outpocketing of the
CC       diencephalic floor at 10.5 dpc and in the developing thalamus and,
CC       to a lesser extent, the developing hypothalamus. At 14.5 dpc,
CC       restricted to the region where thalamus and hypothalamus meet.
CC       Detected in a discrete band of cells at the edge of the olfactory
CC       bulb. In the vascular system: expressed in the endothelium of
CC       numerous blood vessels, but not all, at 10.5, 11.5 and 12.5 dpc,
CC       such as vitelline/umbilical vessels, cardiac ventricular wall
CC       capillaries, facial vessels and, at 14.5 pdc, in the vasculature
CC       of the herniated gut. Expression seems to be associated with
CC       expanding vascular networks. In the heart development, expressed
CC       at 10.5 dpc in the precursor to the aortopulmonary (AP) septum. At
CC       12.5 dpc, detected in the AP septum at the base of the outflow
CC       tract and in the atrioventricular valves. Detected in cranofacial
CC       ectoderm from 10.5 to 14.5 dpc. At 10.5 and 11.5 dpc, expressed in
CC       the Rathke pouch.
CC   -!- PTM: Phosphorylated on agonist stimulation. Rapidly phosphorylated
CC       on serine and threonine residues in the C-terminal.
CC       Phosphorylation at Ser-331 and Ser-332 leads to recruitment of
CC       ITCH, ubiquitination and protein degradation (By similarity).
CC   -!- PTM: Ubiquitinated by ITCH at the cell membrane on agonist
CC       stimulation. The ubiquitin-dependent mechanism, endosomal sorting
CC       complex required for transport (ESCRT), then targets CXCR4 for
CC       lysosomal degradation. This process is dependent also on prior
CC       Ser-/Thr-phosphorylation in the C-terminal of CXCR4. Also binding
CC       of ARRB1 to STAM negatively regulates CXCR4 sorting to lysosomes
CC       though modulating ubiquitination of SFR5S (By similarity).
CC   -!- PTM: Sulfation is required for efficient binding of CXCL12/SDF-
CC       1alpha and promotes its dimerization (By similarity).
CC   -!- PTM: O- and N-glycosylated. N-glycosylation can mask coreceptor
CC       function. The O-glycosylation chondroitin sulfate attachment does
CC       not affect interaction with CXCL12/SDF-1alpha nor its coreceptor
CC       activity (By similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
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DR   EMBL; U59760; AAB07725.1; -; mRNA.
DR   EMBL; U65580; AAC52953.1; -; Genomic_DNA.
DR   EMBL; D87747; BAA13451.1; -; mRNA.
DR   EMBL; Z80111; CAB02201.1; -; mRNA.
DR   EMBL; Z80112; CAB02202.1; -; mRNA.
DR   EMBL; X99581; CAA67893.1; -; Genomic_DNA.
DR   EMBL; X99582; CAA67894.1; -; mRNA.
DR   EMBL; AB000803; BAA19187.1; -; mRNA.
DR   EMBL; BC031665; AAH31665.1; -; mRNA.
DR   EMBL; BC098322; AAH98322.1; -; mRNA.
DR   IPI; IPI00111763; -.
DR   IPI; IPI00849797; -.
DR   RefSeq; NP_034041.2; NM_009911.3.
DR   UniGene; Mm.1401; -.
DR   ProteinModelPortal; P70658; -.
DR   SMR; P70658; 29-324.
DR   STRING; P70658; -.
DR   PhosphoSite; P70658; -.
DR   PRIDE; P70658; -.
DR   Ensembl; ENSMUST00000052172; ENSMUSP00000053489; ENSMUSG00000045382.
DR   GeneID; 12767; -.
DR   KEGG; mmu:12767; -.
DR   UCSC; uc007cls.1; mouse.
DR   UCSC; uc007clt.1; mouse.
DR   CTD; 12767; -.
DR   MGI; MGI:109563; Cxcr4.
DR   GeneTree; ENSGT00590000082948; -.
DR   HOGENOM; HBG715940; -.
DR   HOVERGEN; HBG106917; -.
DR   InParanoid; P70658; -.
DR   OrthoDB; EOG46MBKB; -.
DR   NextBio; 460845; -.
DR   ArrayExpress; P70658; -.
DR   Bgee; P70658; -.
DR   CleanEx; MM_CXCR4; -.
DR   Genevestigator; P70658; -.
DR   GermOnline; ENSMUSG00000045382; Mus musculus.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0030426; C:growth cone; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016493; F:C-C chemokine receptor activity; IEA:InterPro.
DR   GO; GO:0016494; F:C-X-C chemokine receptor activity; IEA:InterPro.
DR   GO; GO:0001667; P:ameboidal cell migration; IMP:MGI.
DR   GO; GO:0007420; P:brain development; IMP:MGI.
DR   GO; GO:0007281; P:germ cell development; IMP:MGI.
DR   GO; GO:0008354; P:germ cell migration; IMP:MGI.
DR   GO; GO:0008045; P:motor axon guidance; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IDA:MGI.
DR   GO; GO:0009887; P:organ morphogenesis; TAS:ProtInc.
DR   GO; GO:0001569; P:patterning of blood vessels; IMP:MGI.
DR   GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
DR   GO; GO:0042098; P:T cell proliferation; IMP:MGI.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR001277; Chemokine_CXCR4.
DR   InterPro; IPR022726; Chemokine_CXCR4_N.
DR   InterPro; IPR000355; Chemokine_rcpt.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   Pfam; PF00001; 7tm_1; 1.
DR   Pfam; PF12109; CXCR4_N; 1.
DR   PRINTS; PR00657; CCCHEMOKINER.
DR   PRINTS; PR00645; CXCCHMKINER4.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW   Proteoglycan; Receptor; Sulfation; Transducer; Transmembrane;
KW   Transmembrane helix; Ubl conjugation.
FT   CHAIN         1    359       C-X-C chemokine receptor type 4.
FT                                /FTId=PRO_0000069355.
FT   TOPO_DOM      1     41       Extracellular (Potential).
FT   TRANSMEM     42     65       Helical; Name=1; (Potential).
FT   TOPO_DOM     66     81       Cytoplasmic (Potential).
FT   TRANSMEM     82    101       Helical; Name=2; (Potential).
FT   TOPO_DOM    102    112       Extracellular (Potential).
FT   TRANSMEM    113    134       Helical; Name=3; (Potential).
FT   TOPO_DOM    135    156       Cytoplasmic (Potential).
FT   TRANSMEM    157    177       Helical; Name=4; (Potential).
FT   TOPO_DOM    178    207       Extracellular (Potential).
FT   TRANSMEM    208    227       Helical; Name=5; (Potential).
FT   TOPO_DOM    228    247       Cytoplasmic (Potential).
FT   TRANSMEM    248    268       Helical; Name=6; (Potential).
FT   TOPO_DOM    269    292       Extracellular (Potential).
FT   TRANSMEM    293    312       Helical; Name=7; (Potential).
FT   TOPO_DOM    313    359       Cytoplasmic (Potential).
FT   MOD_RES      23     23       Sulfotyrosine (By similarity).
FT   MOD_RES     326    326       Phosphoserine (By similarity).
FT   MOD_RES     328    328       Phosphoserine (By similarity).
FT   MOD_RES     331    331       Phosphoserine; by PKC and GRK6 (By
FT                                similarity).
FT   MOD_RES     332    332       Phosphoserine; by PKC and GRK6 (By
FT                                similarity).
FT   MOD_RES     337    337       Phosphoserine; by GRK6 (By similarity).
FT   MOD_RES     346    346       Phosphoserine; by GRK6 (By similarity).
FT   MOD_RES     355    355       Phosphoserine (By similarity).
FT   MOD_RES     358    358       Phosphoserine (By similarity).
FT   CARBOHYD     13     13       N-linked (GlcNAc...) (By similarity).
FT   CARBOHYD     20     20       O-linked (Xyl...) (chondroitin sulfate)
FT                                (By similarity).
FT   DISULFID    111    193       By similarity.
FT   VAR_SEQ       6      7       Missing (in isoform CXCR4-A).
FT                                /FTId=VSP_001891.
FT   CONFLICT    216    216       I -> V (in Ref. 4; CAA67893 and 6;
FT                                BAA19187).
SQ   SEQUENCE   359 AA;  40426 MW;  33D1B5552A31595B CRC64;
     MEPISVSIYT SDNYSEEVGS GDYDSNKEPC FRDENVHFNR IFLPTIYFII FLTGIVGNGL
     VILVMGYQKK LRSMTDKYRL HLSVADLLFV ITLPFWAVDA MADWYFGKFL CKAVHIIYTV
     NLYSSVLILA FISLDRYLAI VHATNSQRPR KLLAEKAVYV GVWIPALLLT IPDFIFADVS
     QGDISQGDDR YICDRLYPDS LWMVVFQFQH IMVGLILPGI VILSCYCIII SKLSHSKGHQ
     KRKALKTTVI LILAFFACWL PYYVGISIDS FILLGVIKQG CDFESIVHKW ISITEALAFF
     HCCLNPILYA FLGAKFKSSA QHALNSMSRG SSLKILSKGK RGGHSSVSTE SESSSFHSS
//
ID   LDB1_MOUSE              Reviewed;         411 AA.
AC   P70662; O55204; Q1EQX2; Q71V68;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=LIM domain-binding protein 1;
DE            Short=LDB-1;
DE   AltName: Full=Carboxyl-terminal LIM domain-binding protein 2;
DE            Short=CLIM-2;
DE   AltName: Full=LIM domain-binding factor CLIM2;
DE            Short=mLdb1;
DE   AltName: Full=Nuclear LIM interactor;
GN   Name=Ldb1; Synonyms=Nli;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH
RP   LHX1, AND TISSUE SPECIFICITY.
RC   STRAIN=Swiss Webster; TISSUE=Embryo;
RX   MEDLINE=97078753; PubMed=8918878; DOI=10.1038/384270a0;
RA   Agulnick A.D., Taira M., Breen J.J., Tanaka T., Dawid I.B.,
RA   Westphal H.;
RT   "Interactions of the LIM-domain-binding factor Ldb1 with LIM
RT   homeodomain proteins.";
RL   Nature 384:270-272(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Embryo;
RX   MEDLINE=97030257; PubMed=8876198; DOI=10.1073/pnas.93.21.11693;
RA   Jurata L.W., Kenny D.A., Gill G.N.;
RT   "Nuclear LIM interactor, a rhombotin and LIM homeodomain interacting
RT   protein, is expressed early in neuronal development.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:11693-11698(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Embryonic head;
RX   MEDLINE=97336071; PubMed=9192866;
RA   Bach I., Carriere C., Ostendorff H.P., Andersen B., Rosenfeld M.G.;
RT   "A family of LIM domain-associated cofactors confer transcriptional
RT   synergism between LIM and Otx homeodomain proteins.";
RL   Genes Dev. 11:1370-1380(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, INTERACTION WITH LMO2, AND
RP   IDENTIFICATION IN A COMPLEX WITH LMO2 AND TAL1.
RC   TISSUE=Yolk sac;
RX   MEDLINE=98054298; PubMed=9391090; DOI=10.1073/pnas.94.25.13707;
RA   Visvader J.E., Mao X., Fujiwara Y., Hahm K., Orkin S.H.;
RT   "The LIM-domain binding protein Ldb1 and its partner LMO2 act as
RT   negative regulators of erythroid differentiation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:13707-13712(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=98163750; PubMed=9503020; DOI=10.1006/geno.1997.5163;
RA   Yamashita T., Agulnick A.D., Copeland N.G., Gilbert D.J.,
RA   Jenkins N.A., Westphal H.;
RT   "Genomic structure and chromosomal localization of the mouse LIM
RT   domain-binding protein 1 gene, Ldb1.";
RL   Genomics 48:87-92(1998).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, ALTERNATIVE
RP   SPLICING, AND TISSUE SPECIFICITY.
RC   TISSUE=Heart;
RX   PubMed=16815859; DOI=10.1093/jb/mvj134;
RA   Tran Y.H., Xu Z., Kato A., Mistry A.C., Goya Y., Taira M.,
RA   Brandt S.J., Hirose S.;
RT   "Spliced isoforms of LIM-domain-binding protein (CLIM/NLI/Ldb) lacking
RT   the LIM-interaction domain.";
RL   J. Biochem. 140:105-119(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   FUNCTION, INTERACTION WITH ISL1; LMO2 AND LMX1A, HOMODIMERIZATION,
RP   SUBCELLULAR LOCATION, AND IDENTIFICATION OF LIM-BINDING DOMAIN.
RX   PubMed=9315627;
RA   Jurata L.W., Gill G.N.;
RT   "Functional analysis of the nuclear LIM domain interactor NLI.";
RL   Mol. Cell. Biol. 17:5688-5698(1997).
RN   [9]
RP   INTERACTION WITH LHX1, DOMAIN, AND HOMODIMERIZATION.
RX   PubMed=9468533; DOI=10.1074/jbc.273.8.4712;
RA   Breen J.J., Agulnick A.D., Westphal H., Dawid I.B.;
RT   "Interactions between LIM domains and the LIM domain-binding protein
RT   Ldb1.";
RL   J. Biol. Chem. 273:4712-4717(1998).
RN   [10]
RP   INTERACTION WITH LHX6.
RC   TISSUE=Fetal brain;
RX   MEDLINE=99321857; PubMed=10393337;
RA   Kimura N., Ueno M., Nakashima K., Taga T.;
RT   "A brain region-specific gene product Lhx6.1 interacts with Ldb1
RT   through tandem LIM-domains.";
RL   J. Biochem. 126:180-187(1999).
RN   [11]
RP   INTERACTION WITH LHX9.
RX   MEDLINE=99264291; PubMed=10330499; DOI=10.1016/S0925-4773(98)00233-0;
RA   Bertuzzi S., Porter F.D., Pitts A., Kumar M., Agulnick A., Wassif C.,
RA   Westphal H.;
RT   "Characterization of Lhx9, a novel LIM/homeobox gene expressed by the
RT   pioneer neurons in the mouse cerebral cortex.";
RL   Mech. Dev. 81:193-198(1999).
RN   [12]
RP   INTERACTION WITH RLIM, AND UBIQUITINATION.
RX   PubMed=11882901; DOI=10.1038/416099a;
RA   Ostendorff H.P., Peirano R.I., Peters M.A., Schluter A., Bossenz M.,
RA   Scheffner M., Bach I.;
RT   "Ubiquitination-dependent cofactor exchange on LIM homeodomain
RT   transcription factors.";
RL   Nature 416:99-103(2002).
RN   [13]
RP   IDENTIFICATION IN A NUCLEAR TAL-1 COMPLEX.
RX   PubMed=16407974; DOI=10.1038/sj.emboj.7600934;
RA   Goardon N., Lambert J.A., Rodriguez P., Nissaire P., Herblot S.,
RA   Thibault P., Dumenil D., Strouboulis J., Romeo P.-H., Hoang T.;
RT   "ETO2 coordinates cellular proliferation and differentiation during
RT   erythropoiesis.";
RL   EMBO J. 25:357-366(2006).
RN   [14]
RP   STRUCTURE BY NMR OF 336-375 IN COMPLEXES WITH LMO2 AND LMO4.
RX   PubMed=12727888; DOI=10.1093/emboj/cdg196;
RA   Deane J.E., Mackay J.P., Kwan A.H.Y., Sum E.Y.M., Visvader J.E.,
RA   Matthews J.M.;
RT   "Structural basis for the recognition of ldb1 by the N-terminal LIM
RT   domains of LMO2 and LMO4.";
RL   EMBO J. 22:2224-2233(2003).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 336-375 IN COMPLEX WITH LMO4.
RX   PubMed=15343268; DOI=10.1038/sj.emboj.7600376;
RA   Deane J.E., Ryan D.P., Sunde M., Maher M.J., Guss J.M., Visvader J.E.,
RA   Matthews J.M.;
RT   "Tandem LIM domains provide synergistic binding in the LMO4:Ldb1
RT   complex.";
RL   EMBO J. 23:3589-3598(2004).
CC   -!- FUNCTION: Binds to the LIM domain of a wide variety of LIM domain-
CC       containing transcription factors. May regulate the transcriptional
CC       activity of LIM-containing proteins by determining specific
CC       partner interactions. May play a role in the development of motor
CC       neurons. Acts synergistically with LHX1/LIM1 in axis formation and
CC       activation of gene expression. Acts with LMO2 in the regulation of
CC       red blood cell development, maintaining erythroid precursors in an
CC       immature state.
CC   -!- SUBUNIT: Interacts with ESR1 (By similarity). Forms homodimers and
CC       heterodimers. Interacts with and activates LHX1/LIM1. Interacts
CC       with the LIM domains of ISL1 and LMO2. Can assemble in a complex
CC       with LMO2 and TAL1/SCL but does not interact with TAL1/SCL
CC       directly. Strongly interacts with the LIM2 domain of LMX1A and
CC       more weakly with the LIM1 domain. Homodimerization is not required
CC       for, and does not effect, LMX1A-binding. Component of a nuclear
CC       TAL-1 complex composed at least of CBFA2T3, LDB1, TAL1 and TCF3.
CC       Interacts with LHX6 and LHX9.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Visvader-a;
CC         IsoId=P70662-1; Sequence=Displayed;
CC       Name=2; Synonyms=Tran-b;
CC         IsoId=P70662-2; Sequence=VSP_027833, VSP_027834, VSP_027835;
CC         Note=Due to intron retention. Lacks LIM-binding domain. Lacks
CC         ability to activate LIM domain-dependent transcription;
CC       Name=3; Synonyms=Tran-a;
CC         IsoId=P70662-3; Sequence=VSP_027833;
CC   -!- TISSUE SPECIFICITY: Expression overlaps that of LIM domain-
CC       containing proteins. Expressed widely in the embryo with highest
CC       expression in several regions of the brain the central nervous
CC       system ganglia. Also expressed in fetal liver, lung, kidney,
CC       thymus and olfactory epithelium. Expressed in multiple adult
CC       tissues including heart, brain, liver, kidney, testis, lung and
CC       muscle and a diverse range of neuronal cell types, with expression
CC       highest in the pituitary gland and skin. Expressed in both
CC       embryonic and adult hemopoietic cells, including the erythroid
CC       lineage.
CC   -!- DOMAIN: The dimerization domain is located in the N-terminus.
CC   -!- PTM: Ubiquitinated by RLIM/RNF12, leading to its degradation by
CC       the proteasome.
CC   -!- SIMILARITY: Belongs to the LDB family.
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DR   EMBL; U70375; AAC52933.1; -; mRNA.
DR   EMBL; U69270; AAC52887.1; -; mRNA.
DR   EMBL; U89488; AAB96885.1; -; mRNA.
DR   EMBL; AF030333; AAB94131.1; -; mRNA.
DR   EMBL; AF024524; AAC40064.1; -; Genomic_DNA.
DR   EMBL; AB250383; BAE95401.1; -; mRNA.
DR   EMBL; BC013624; AAH13624.1; -; mRNA.
DR   IPI; IPI00111789; -.
DR   IPI; IPI00624850; -.
DR   IPI; IPI00762229; -.
DR   RefSeq; NP_001106879.1; NM_001113408.1.
DR   RefSeq; NP_034827.1; NM_010697.1.
DR   UniGene; Mm.327442; -.
DR   PDB; 1J2O; NMR; -; A=336-375.
DR   PDB; 1M3V; NMR; -; A=336-375.
DR   PDB; 1RUT; X-ray; 1.30 A; X=336-375.
DR   PDB; 2JTN; NMR; -; A=331-375.
DR   PDB; 2L3K; NMR; -; A=336-375.
DR   PDBsum; 1J2O; -.
DR   PDBsum; 1M3V; -.
DR   PDBsum; 1RUT; -.
DR   PDBsum; 2JTN; -.
DR   PDBsum; 2L3K; -.
DR   ProteinModelPortal; P70662; -.
DR   SMR; P70662; 331-375.
DR   MINT; MINT-2779250; -.
DR   STRING; P70662; -.
DR   PhosphoSite; P70662; -.
DR   PRIDE; P70662; -.
DR   Ensembl; ENSMUST00000026252; ENSMUSP00000026252; ENSMUSG00000025223.
DR   Ensembl; ENSMUST00000056931; ENSMUSP00000053680; ENSMUSG00000025223.
DR   GeneID; 16825; -.
DR   KEGG; mmu:16825; -.
DR   UCSC; uc008hry.1; mouse.
DR   CTD; 16825; -.
DR   MGI; MGI:894762; Ldb1.
DR   eggNOG; roNOG04930; -.
DR   GeneTree; ENSGT00390000005639; -.
DR   HOGENOM; HBG505202; -.
DR   HOVERGEN; HBG000135; -.
DR   InParanoid; P70662; -.
DR   OMA; GSNSPWN; -.
DR   OrthoDB; EOG4XWFXV; -.
DR   PhylomeDB; P70662; -.
DR   NextBio; 290724; -.
DR   ArrayExpress; P70662; -.
DR   Bgee; P70662; -.
DR   CleanEx; MM_LDB1; -.
DR   Genevestigator; P70662; -.
DR   GermOnline; ENSMUSG00000025223; Mus musculus.
DR   GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR   GO; GO:0044451; C:nucleoplasm part; IDA:MGI.
DR   GO; GO:0043234; C:protein complex; IPI:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0030274; F:LIM domain binding; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0003712; F:transcription cofactor activity; IEA:InterPro.
DR   GO; GO:0003711; F:transcription elongation regulator activity; IMP:BHF-UCL.
DR   GO; GO:0009948; P:anterior/posterior axis specification; IMP:MGI.
DR   GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IMP:MGI.
DR   GO; GO:0010669; P:epithelial structure maintenance; IGI:MGI.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
DR   GO; GO:0043973; P:histone H3-K4 acetylation; IMP:BHF-UCL.
DR   GO; GO:0045647; P:negative regulation of erythrocyte differentiation; IMP:UniProtKB.
DR   GO; GO:0010552; P:positive regulation of gene-specific transcription from RNA polymerase II promoter; IMP:BHF-UCL.
DR   GO; GO:0046985; P:positive regulation of hemoglobin biosynthetic process; IMP:BHF-UCL.
DR   GO; GO:0060319; P:primitive erythrocyte differentiation; TAS:BHF-UCL.
DR   GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:BHF-UCL.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IMP:MGI.
DR   InterPro; IPR002691; LIM-bd.
DR   PANTHER; PTHR10378; LIM_bd; 1.
DR   Pfam; PF01803; LIM_bind; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Developmental protein; Nucleus;
KW   Phosphoprotein; Ubl conjugation.
FT   CHAIN         1    411       LIM domain-binding protein 1.
FT                                /FTId=PRO_0000084385.
FT   REGION      336    374       LIM-binding domain (LID).
FT   MOD_RES     302    302       Phosphoserine (By similarity).
FT   MOD_RES     306    306       Phosphothreonine (By similarity).
FT   VAR_SEQ       1     36       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_027833.
FT   VAR_SEQ     336    355       DVMVVGEPTLMGGEFGDEDE -> VSISAFFSSGLPHCSPL
FT                                TPV (in isoform 2).
FT                                /FTId=VSP_027834.
FT   VAR_SEQ     356    411       Missing (in isoform 2).
FT                                /FTId=VSP_027835.
FT   CONFLICT    262    262       Y -> C (in Ref. 3; AAB96885).
FT   CONFLICT    334    334       V -> A (in Ref. 3; AAB96885).
FT   CONFLICT    389    390       PW -> QR (in Ref. 3; AAB96885).
FT   STRAND      238    240
FT   STRAND      243    245
FT   HELIX       247    250
FT   STRAND      253    255
FT   TURN        259    261
FT   STRAND      262    264
FT   STRAND      267    269
FT   STRAND      272    274
FT   HELIX       276    283
FT   STRAND      288    290
FT   STRAND      299    308
FT   TURN        326    331
SQ   SEQUENCE   411 AA;  46503 MW;  47C53DFA23044580 CRC64;
     MSVGCACPGC SSKSFKLYSP KEPPNGNAFP PFHPGTMLDR DVGPTPMYPP TYLEPGIGRH
     TPYGNQTDYR IFELNKRLQN WTEECDNLWW DAFTTEFFED DAMLTITFCL EDGPKRYTIG
     RTLIPRYFRS IFEGGATELY YVLKHPKEAF HSNFVSLDCD QGSMVTQHGK PMFTQVCVEG
     RLYLEFMFDD MMRIKTWHFS IRQHRELIPR SILAMHAQDP QMLDQLSKNI TRCGLSNSTL
     NYLRLCVILE PMQELMSRHK TYSLSPRDCL KTCLFQKWQR MVAPPAEPAR QQPSKRRKRK
     MSGGSTMSSG GGNTNNSNSK KKSPASTFAL SSQVPDVMVV GEPTLMGGEF GDEDERLITR
     LENTQFDAAN GIDDEDSFNN SPALGANSPW NSKPPSSQES KSENPTSQAS Q
//
ID   SPRL1_MOUSE             Reviewed;         650 AA.
AC   P70663; P97810; Q99L82;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2002, sequence version 2.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=SPARC-like protein 1;
DE   AltName: Full=Extracellular matrix protein 2;
DE   AltName: Full=Matrix glycoprotein Sc1;
DE   Flags: Precursor;
GN   Name=Sparcl1; Synonyms=Ecm2, Sc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=129/SvJ;
RX   MEDLINE=97092869; PubMed=8938431;
RA   McKinnon P.J., Kapsetaki M., Margolskee R.F.;
RT   "The exon structure of the mouse Sc1 gene is very similar to the mouse
RT   Sparc gene.";
RL   Genome Res. 6:1077-1083(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=97343039; PubMed=9199668;
RA   Soderling J.A., Reed M.J., Corsa A., Sage E.H.;
RT   "Cloning and expression of murine SC1, a gene product homologous to
RT   SPARC.";
RL   J. Histochem. Cytochem. 45:823-835(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-411, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- TISSUE SPECIFICITY: Highest expression in brain. Moderate levels
CC       in heart, adrenal gland, epididymis and lung. Low levels in
CC       kidney, eye, liver, spleen, submandibular gland and testis.
CC   -!- SIMILARITY: Belongs to the SPARC family.
CC   -!- SIMILARITY: Contains 1 EF-hand domain.
CC   -!- SIMILARITY: Contains 1 follistatin-like domain.
CC   -!- SIMILARITY: Contains 1 Kazal-like domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; U66166; AAB06444.1; -; Genomic_DNA.
DR   EMBL; U66158; AAB06444.1; JOINED; Genomic_DNA.
DR   EMBL; U66159; AAB06444.1; JOINED; Genomic_DNA.
DR   EMBL; U66160; AAB06444.1; JOINED; Genomic_DNA.
DR   EMBL; U66161; AAB06444.1; JOINED; Genomic_DNA.
DR   EMBL; U66162; AAB06444.1; JOINED; Genomic_DNA.
DR   EMBL; U66163; AAB06444.1; JOINED; Genomic_DNA.
DR   EMBL; U66164; AAB06444.1; JOINED; Genomic_DNA.
DR   EMBL; U66165; AAB06444.1; JOINED; Genomic_DNA.
DR   EMBL; U77330; AAC53172.1; -; mRNA.
DR   EMBL; U64827; AAB08451.1; -; mRNA.
DR   EMBL; BC003759; AAH03759.1; -; mRNA.
DR   IPI; IPI00308484; -.
DR   UniGene; Mm.29027; -.
DR   ProteinModelPortal; P70663; -.
DR   SMR; P70663; 419-649.
DR   MINT; MINT-1177391; -.
DR   STRING; P70663; -.
DR   PhosphoSite; P70663; -.
DR   PRIDE; P70663; -.
DR   Ensembl; ENSMUST00000031249; ENSMUSP00000031249; ENSMUSG00000029309.
DR   MGI; MGI:108110; Sparcl1.
DR   eggNOG; roNOG05455; -.
DR   HOGENOM; HBG126458; -.
DR   HOVERGEN; HBG079212; -.
DR   InParanoid; P70663; -.
DR   OrthoDB; EOG4H19VR; -.
DR   NextBio; 284232; -.
DR   ArrayExpress; P70663; -.
DR   Bgee; P70663; -.
DR   CleanEx; MM_SPARCL1; -.
DR   Genevestigator; P70663; -.
DR   GermOnline; ENSMUSG00000029309; Mus musculus.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR003645; Fol_N.
DR   InterPro; IPR015369; Follistatin/Osteonectin_EGF.
DR   InterPro; IPR001999; Osteonectin_CS.
DR   InterPro; IPR002350; Prot_inh_Kazal.
DR   InterPro; IPR011497; Prot_Inh_Kazal_2.
DR   InterPro; IPR016359; SPARC-like_p1.
DR   InterPro; IPR019577; SPARC/Testican_Ca-bd-dom.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF09289; FOLN; 1.
DR   Pfam; PF07648; Kazal_2; 1.
DR   Pfam; PF10591; SPARC_Ca_bdg; 1.
DR   PIRSF; PIRSF002574; SPARC-like_p1; 1.
DR   SMART; SM00274; FOLN; 1.
DR   SMART; SM00280; KAZAL; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
DR   PROSITE; PS00612; OSTEONECTIN_1; 1.
DR   PROSITE; PS00613; OSTEONECTIN_2; 1.
PE   1: Evidence at protein level;
KW   Calcium; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Phosphoprotein; Secreted; Signal.
FT   SIGNAL        1     16       Potential.
FT   CHAIN        17    650       SPARC-like protein 1.
FT                                /FTId=PRO_0000020313.
FT   DOMAIN      418    440       Follistatin-like.
FT   DOMAIN      436    497       Kazal-like.
FT   DOMAIN      608    643       EF-hand.
FT   CA_BIND     621    632       Potential.
FT   COMPBIAS    192    277       Glu-rich.
FT   COMPBIAS    192    209       Poly-Glu.
FT   MOD_RES      70     70       Phosphoserine.
FT   MOD_RES     411    411       Phosphoserine.
FT   CARBOHYD    148    148       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    168    168       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    462    462       N-linked (GlcNAc...) (Potential).
FT   DISULFID    419    430       By similarity.
FT   DISULFID    424    440       By similarity.
FT   DISULFID    442    476       By similarity.
FT   DISULFID    448    469       By similarity.
FT   DISULFID    458    495       By similarity.
FT   DISULFID    501    612       By similarity.
FT   DISULFID    620    636       By similarity.
FT   CONFLICT     25     25       S -> F (in Ref. 2; AAC53172).
FT   CONFLICT    199    199       D -> E (in Ref. 1; AAB06444/AAB08451).
FT   CONFLICT    281    281       A -> S (in Ref. 1; AAB06444/AAB08451).
FT   CONFLICT    385    385       R -> Q (in Ref. 1; AAB06444/AAB08451).
SQ   SEQUENCE   650 AA;  72314 MW;  4F2568E5642D165A CRC64;
     MKAVLLLLCA LGTAVAIPTS TRFLSDHSNP TTATLVTPED ATVPIAGVEA TADIENHPND
     KAEKPSALNS EEETHEQSTE QDKTYSFEVD LKDEEDGDGD LSVDPTEGTL TLDLQEGTSE
     PQQKSLPENG DFPATVSTSY VDPNQRANIT KGKESQEQPV SDSHQQPNES SKQTQDLKAE
     ESQTQDPDIP NEEEEEEEDE EEEEEEEPED IGAPSDNQEE GKEPLEEQPT SKWEGNREQS
     DDTLEESSQP TQISKTEKHQ SEQGNQGQES DSEAEGEDKA AGSKEHIPHT EQQDQEGKAG
     LEAIGNQKDT DEKAVSTEPT DAAVVPRSHG GAGDNGGGDD SKHGAGDDYF IPSQEFLEAE
     RMHSLSYYLK YGGGEETTTG ESENRREAAD NQEAKKAESS PNAEPSDEGN SREHSAGSCT
     NFQCKRGHIC KTDPQGKPHC VCQDPETCPP AKILDQACGT DNQTYASSCH LFATKCRLEG
     TKKGHQLQLD YFGACKSIPA CTDFEVAQFP LRMRDWLKNI LMQLYEPNPK HGGYLNEKQR
     SKVKKIYLDE KRLLAGDHPI ELLLRDFKKN YHMYVYPVHW QFNELDQHPA DRILTHSELA
     PLRASLVPME HCITRFFEEC DPNKDKHITL KEWGHCFGIK EEDIDENLLF
//
ID   NACAM_MOUSE             Reviewed;        2187 AA.
AC   P70670;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Nascent polypeptide-associated complex subunit alpha, muscle-specific form;
DE   AltName: Full=Alpha-NAC, muscle-specific form;
GN   Name=Naca; Synonyms=Gm1878;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), FUNCTION,
RP   ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX   MEDLINE=96312450; PubMed=8698236;
RA   Yotov W.V., St Arnaud R.;
RT   "Differential splicing-in of a proline-rich exon converts alphaNAC
RT   into a muscle-specific transcription factor.";
RL   Genes Dev. 10:1763-1772(1996).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2133 AND SER-2138, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1024, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Prevents inappropriate targeting of non-secretory
CC       polypeptides to the endoplasmic reticulum (ER). Binds to nascent
CC       polypeptide chains as they emerge from the ribosome and blocks
CC       their interaction with the signal recognition particle (SRP),
CC       which normally targets nascent secretory peptides to the ER. Also
CC       reduces the inherent affinity of ribosomes for protein
CC       translocation sites in the ER membrane (M sites) (By similarity).
CC       Isoform 1 and isoform 2 appear to bind DNA and play roles in
CC       transcription. May act to regulate the expression of genes
CC       involved in the development of myotubes.
CC   -!- SUBUNIT: Part of the nascent polypeptide-associated complex (NAC),
CC       consisting of NACA and BTF3. NAC associates with ribosomes through
CC       the BTF3 subunit. Both subunits can contact nascent polypeptide
CC       chains (By similarity). Interacts with TBP and JUN.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2; Synonyms=Gp220, skNAC;
CC         IsoId=P70670-1; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q60817-1; Sequence=External;
CC   -!- TISSUE SPECIFICITY: Specifically expressed in heart and skeletal
CC       muscle: it is present in differentiated myotubes but not in
CC       myoblasts.
CC   -!- DEVELOPMENTAL STAGE: Expressed concomitant with the onset of
CC       mineralization in ossification centers of developing bone.
CC   -!- INDUCTION: Induced in muscle by wounding.
CC   -!- PTM: Phosphorylation of Ser-2015 by ILK during cell adhesion may
CC       promote nuclear localization. Phosphorylation of Thr-2131 by GSK3B
CC       may promote proteasome mediated degradation.
CC   -!- SIMILARITY: Belongs to the NAC-alpha family.
CC   -!- SIMILARITY: Contains 1 NAC-A/B (NAC-alpha/beta) domain.
CC   -!- SIMILARITY: Contains 1 UBA domain.
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DR   EMBL; U48364; AAB18734.1; -; mRNA.
DR   EMBL; U48363; AAB18732.1; -; Genomic_DNA.
DR   IPI; IPI00111831; -.
DR   PIR; T30826; T30826.
DR   RefSeq; NP_001106670.1; NM_001113199.1.
DR   RefSeq; NP_038636.2; NM_013608.3.
DR   UniGene; Mm.3746; -.
DR   ProteinModelPortal; P70670; -.
DR   SMR; P70670; 2051-2185.
DR   IntAct; P70670; 2.
DR   STRING; P70670; -.
DR   PhosphoSite; P70670; -.
DR   PRIDE; P70670; -.
DR   Ensembl; ENSMUST00000092048; ENSMUSP00000089680; ENSMUSG00000061315.
DR   GeneID; 17938; -.
DR   KEGG; mmu:17938; -.
DR   UCSC; uc007hlc.1; mouse.
DR   CTD; 17938; -.
DR   MGI; MGI:106095; Naca.
DR   eggNOG; roNOG09734; -.
DR   GeneTree; ENSGT00440000033468; -.
DR   InParanoid; P70670; -.
DR   OrthoDB; EOG41RPW6; -.
DR   PhylomeDB; P70670; -.
DR   NextBio; 292841; -.
DR   Bgee; P70670; -.
DR   Genevestigator; P70670; -.
DR   GermOnline; ENSMUSG00000061315; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0017025; F:TBP-class protein binding; IDA:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002715; Nas_poly-pep-assoc_cplx.
DR   Pfam; PF01849; NAC; 1.
DR   PROSITE; PS51151; NAC_AB; 1.
DR   PROSITE; PS50030; UBA; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Cytoplasm; DNA-binding; Nucleus;
KW   Phosphoprotein; Protein transport; Transcription;
KW   Transcription regulation; Transport.
FT   CHAIN         1   2187       Nascent polypeptide-associated complex
FT                                subunit alpha, muscle-specific form.
FT                                /FTId=PRO_0000135578.
FT   DOMAIN     2042   2107       NAC-A/B.
FT   DOMAIN     2148   2185       UBA.
FT   REGION     2041   2052       Required for DNA-binding.
FT   MOD_RES    1024   1024       Phosphoserine.
FT   MOD_RES    2015   2015       Phosphoserine; by ILK1 (Probable).
FT   MOD_RES    2131   2131       Phosphothreonine; by GSK3-beta
FT                                (Probable).
FT   MOD_RES    2133   2133       Phosphothreonine.
FT   MOD_RES    2138   2138       Phosphoserine.
SQ   SEQUENCE   2187 AA;  220601 MW;  003646AA864DEBFD CRC64;
     MPGEATETVP ATEQELPQPQ AETAVLPMSS ALKVAAVGQP GPTPPSSLGP QQSPIVTAHQ
     PSPLPSSVSS TPFEVPFAQP ITAETALPSG TAPPTPTFLP HLIGPPISPA ALALASPMIG
     LAQKGARSSS APLSLVALAP HSVQKSSVCP PHPLTSPPSA AGAELGALTA SIPPLEPKTS
     TSQVPSQGTL NLKGTAPCPP DVVRAFPSHL ENPLASVQPG LMSCPQTLSN TSPVKGVPIS
     SALTQSRLSL NLKGPVSPPA RNTAAPSIPL APSTSLGCHL PLLHHSSVDS PIQPPGQSGL
     AVSNPTSVGH SGIAASCPPE RCVVPALPSR LLAVDSGAAP SDDKGSSAVT NELCSPPGSS
     NVAGTSLSPK ASLVPKGSNV ALQPLVTQVP ASQKTGLKEI PVSCIGATHH ALDNPSAISV
     APATHVPPPT SSGLVSSKDP ASPVTSLVVP AAHKQFPAPP ASATLGVPVS PLPATEGLKN
     LPISALVNVG APVSPAQAGL PTRKDTTLQP LAPIALKESP SSQSASSLEV LSEDTVTKKT
     TGGPAPVVRP AIAGVATTTS LRADSPPAVI RADSCVSPNT VSQPLKRSVT DPAMAPRTAK
     NTAPSTTSPL VPLASEGCPV ASSMALSPQN ASVSETALAL SPEIPKSVPF PDPPLAEISF
     SNARKVDAVS HMESSGSSRQ GHPDASVTAK GTVVCLADSS LDTSVSASKG SALSGASSPL
     YPLEVSFLPE AGLAVQGPKG SLNKLSPTPP SSKGAPVPST GAPPSPKGAP IVPTESSISS
     KQVPAEILPS PQKTPEVTAS RLISAVQSPK VDPIMSDVTP TSPKKTSATA VPKDTSATLS
     LKSVPAVTSL SPPKAPVAPS NEATIVPTEI PTSLKNALAA ATPKETLATS IPKVTSPSPQ
     KTPKSVSLKG APAMTSKKAT EIAASKDVSP SQFPKEVPLL QHVPPTSPPK SPVSDTLSGA
     LTSPPPKGPP ATLAETPTYP KKSPKPAASK KTPATPSPEG VTAVPLEIPP CSKKAPKTAA
     PKESSATSSS KRAPKTAVSK EIPSKGVTAV PLEISLPLKE TSKSATPGEK SASSPKRSPK
     TAGPKETPPG GVTAVPPEIS LPPKETPQNA TPNESLAASS QKRSPKTSVP KETPPGGVTA
     MPLEIPSAPQ KAPKTAVPKQ IPTPEDAVTI LAGSPLSPKK ASKTAAPKEA PATPSVGVIA
     VSGEISPSPK KTSKTAAPKE NSATLPPKRS PKTAAPKETP ATSSEGVTAV PSEISPSPPT
     PASKGVPVTL TPKGAPNALA ESPASPKKVP KTAAPEETST TPSPQKIPKV AGPKEASATP
     PSKKTPKTAV PKETSAPSEG VTAVPLEIPP SPRKAPKTAA PKETPAPSPE GATTAPVQIP
     PSPRKGSKKA GSKETPTTPS PEGVTAAPLE IPISSKKTSK MASPKETLVT PSSKKLSQTV
     GPKETSLEGA TAVPLEIPPS HKKAPKTVDP KQVPLTPSPK DAPTTLAESP SSPKKAPKTA
     APPSERVTTV PPEKPATPQK ASGTTASKVP VPAETQEVAV SSRETPVTPA VPPVKNPSSH
     KKTSKTIELK EAPATLPPSP TKSPKIPSSK KAPRTSAPKE FPASPSIKPV TTSLAQTAPP
     SLQKAPSTTI PKENLAAPAV LPVSSKSPAA PARASASLSP ATAAPQTAPK EATTIPSCKK
     AAATETPIET STAPSLEGAP KETSETSVSK VLMSSPPKKA SSSKRASTLP ATTLPSLKEA
     SVLSPTATSS GKDSHISPVS DACSTGTTTP QASEKLPSKK GPTAFTEMLA APAPESALAI
     TAPIQKSPGA NSNSASSPKC PDPSSKKDTK GLPSAVALAP QTVPVEKDTS KAIETLLVSP
     AKGSDCLHSP KGPVGSQVAT PLAAFTSDKV PPEAVSASVA PKPAPAASLT LAPSPVAPLP
     PKQPLLESAP GSVLESPSKL PVPAEEDELP PLIPPEAVSG GEPFQPILVN MPAPKPAGTP
     APAPSAKQPV LKNNKGSGTE SDSDESVPEL EEQDSTQTAT QQAQLAAAAE IDEEPVSKAK
     QSRSEKKARK AMSKLGLRQV TGVTRVTIRK SKNILFVITK PDVYKSPASD TYIVFGEAKI
     EDLSQQAQLA AAEKFKVQGE AVSNIQENTQ TPTVQEESEE EEVDETGVEV KDIELVMSQA
     NVSRAKAVRA LKNNSNDIVN AIMELTM
//
ID   CASP3_MOUSE             Reviewed;         277 AA.
AC   P70677; O08668; Q8CHV5; Q9QWI4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   08-MAR-2011, entry version 104.
DE   RecName: Full=Caspase-3;
DE            Short=CASP-3;
DE            EC=3.4.22.56;
DE   AltName: Full=Apopain;
DE   AltName: Full=Cysteine protease CPP32;
DE            Short=CPP-32;
DE   AltName: Full=LICE;
DE   AltName: Full=Protein Yama;
DE   AltName: Full=SREBP cleavage activity 1;
DE            Short=SCA-1;
DE   Contains:
DE     RecName: Full=Caspase-3 subunit p17;
DE   Contains:
DE     RecName: Full=Caspase-3 subunit p12;
DE   Flags: Precursor;
GN   Name=Casp3; Synonyms=Cpp32;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   MEDLINE=96358624; PubMed=8761296;
RA   Juan T.S.-C., McNiece I.K., Jenkins N.A., Gilbert D.J., Copeland N.G.,
RA   Fletcher F.A.;
RT   "Molecular characterization of mouse and rat CPP32 beta gene encoding
RT   a cysteine protease resembling interleukin-1 beta converting enzyme
RT   and CED-3.";
RL   Oncogene 13:749-755(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=97224429; PubMed=9070890; DOI=10.1006/bbrc.1996.6002;
RA   Mukasa T., Urase K., Momoi M.Y., Kimura I., Momoi T.;
RT   "Specific expression of CPP32 in sensory neurons of mouse embryos and
RT   activation of CPP32 in the apoptosis induced by a withdrawal of NGF.";
RL   Biochem. Biophys. Res. Commun. 231:770-774(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C3H/An;
RX   MEDLINE=97190206; PubMed=9038361; DOI=10.1016/S0014-5793(97)00026-4;
RA   van de Craen M., Vandenabeele P., Declercq W., van den Brande I.,
RA   van Loo G., Molemans F., Schotte P., van Criekinge W., Beyaert R.,
RA   Fiers W.;
RT   "Characterization of seven murine caspase family members.";
RL   FEBS Lett. 403:61-69(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Fernandes-Alnemri T., Litwack G., Alnemri E.S.;
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 58-277.
RA   Denis F., Alam A., Cohen L., Hartgers F., Braun M., Martinez O.,
RA   Fortin J.-P., Sekaly R.-P.;
RT   "Multiple pathways of apoptosis converging on the CPP32 protease.";
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
CC   -!- FUNCTION: Involved in the activation cascade of caspases
CC       responsible for apoptosis execution. At the onset of apoptosis it
CC       proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a
CC       '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory
CC       element binding proteins (SREBPs) between the basic helix-loop-
CC       helix leucine zipper domain and the membrane attachment domain.
CC       Cleaves and activates caspase-6, -7 and -9 (By similarity).
CC       Cleaves IL-1 beta between an Asp and an Ala, releasing the mature
CC       cytokine which is involved in a variety of inflammatory processes.
CC   -!- CATALYTIC ACTIVITY: Strict requirement for an Asp residue at
CC       positions P1 and P4. It has a preferred cleavage sequence of Asp-
CC       Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a
CC       hydrophilic amino-acid residue at P3, although Val or Ala are also
CC       accepted at this position.
CC   -!- SUBUNIT: Heterotetramer that consists of two anti-parallel
CC       arranged heterodimers, each one formed by a 17 kDa (p17) and a 12
CC       kDa (p12) subunit (By similarity).
CC   -!- INTERACTION:
CC       Q96EK4:THAP11 (xeno); NbExp=1; IntAct=EBI-1790419, EBI-1790529;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Highest expression in spleen, lung, liver,
CC       kidney and heart. Lower expression in brain, skeletal muscle and
CC       testis.
CC   -!- PTM: Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10
CC       generates the two active subunits. Additional processing of the
CC       propeptides is likely due to the autocatalytic activity of the
CC       activated protease. Active heterodimers between the small subunit
CC       of caspase-7 protease and the large subunit of caspase-3 also
CC       occur and vice versa (By similarity).
CC   -!- PTM: S-nitrosylated on its catalytic site cysteine in unstimulated
CC       human cell lines and denitrosylated upon activation of the Fas
CC       apoptotic pathway, associated with an increase in intracellular
CC       caspase activity. Fas therefore activates caspase-3 not only by
CC       inducing the cleavage of the caspase zymogen to its active
CC       subunits, but also by stimulating the denitrosylation of its
CC       active site thiol (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase C14A family.
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DR   EMBL; U54803; AAC52768.1; -; Genomic_DNA.
DR   EMBL; U54802; AAC52768.1; JOINED; Genomic_DNA.
DR   EMBL; U49929; AAC52764.1; -; mRNA.
DR   EMBL; D86352; BAA21727.1; -; mRNA.
DR   EMBL; Y13086; CAA73528.1; -; mRNA.
DR   EMBL; U19522; AAC53196.1; -; mRNA.
DR   EMBL; BC038825; AAH38825.2; -; mRNA.
DR   EMBL; U63720; AAD09504.1; -; mRNA.
DR   IPI; IPI00308498; -.
DR   PIR; JC5410; JC5410.
DR   RefSeq; NP_033940.1; NM_009810.2.
DR   UniGene; Mm.34405; -.
DR   ProteinModelPortal; P70677; -.
DR   SMR; P70677; 29-277.
DR   DIP; DIP-44076N; -.
DR   IntAct; P70677; 2.
DR   MINT; MINT-4050331; -.
DR   STRING; P70677; -.
DR   MEROPS; C14.003; -.
DR   PhosphoSite; P70677; -.
DR   PRIDE; P70677; -.
DR   Ensembl; ENSMUST00000093517; ENSMUSP00000091238; ENSMUSG00000031628.
DR   GeneID; 12367; -.
DR   KEGG; mmu:12367; -.
DR   UCSC; uc009lql.1; mouse.
DR   CTD; 12367; -.
DR   MGI; MGI:107739; Casp3.
DR   eggNOG; roNOG08174; -.
DR   HOGENOM; HBG755233; -.
DR   HOVERGEN; HBG050802; -.
DR   InParanoid; P70677; -.
DR   OMA; CAMLKQY; -.
DR   OrthoDB; EOG4CZBGR; -.
DR   PhylomeDB; P70677; -.
DR   BRENDA; 3.4.22.56; 244.
DR   NextBio; 281052; -.
DR   ArrayExpress; P70677; -.
DR   Bgee; P70677; -.
DR   CleanEx; MM_CASP3; -.
DR   Genevestigator; P70677; -.
DR   GermOnline; ENSMUSG00000031628; Mus musculus.
DR   GO; GO:0004861; F:cyclin-dependent protein kinase inhibitor activity; IMP:MGI.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0001782; P:B cell homeostasis; IMP:MGI.
DR   GO; GO:0045165; P:cell fate commitment; IMP:MGI.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptotic nuclear change; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IGI:MGI.
DR   GO; GO:0008631; P:induction of apoptosis by oxidative stress; IDA:MGI.
DR   GO; GO:0008625; P:induction of apoptosis via death domain receptors; IMP:MGI.
DR   GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI.
DR   GO; GO:0046007; P:negative regulation of activated T cell proliferation; IMP:MGI.
DR   GO; GO:0030889; P:negative regulation of B cell proliferation; IMP:MGI.
DR   GO; GO:0045736; P:negative regulation of cyclin-dependent protein kinase activity; IMP:MGI.
DR   GO; GO:0051402; P:neuron apoptosis; IDA:MGI.
DR   GO; GO:0001836; P:release of cytochrome c from mitochondria; IGI:MGI.
DR   GO; GO:0006974; P:response to DNA damage stimulus; IDA:MGI.
DR   GO; GO:0009411; P:response to UV; IDA:MGI.
DR   GO; GO:0009611; P:response to wounding; IDA:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR   GO; GO:0043029; P:T cell homeostasis; IMP:MGI.
DR   InterPro; IPR015470; Caspase_3.
DR   InterPro; IPR011600; Pept_C14_cat.
DR   InterPro; IPR001309; Pept_C14_ICE_p20.
DR   InterPro; IPR016129; Pept_C14_ICE_p20_AS.
DR   InterPro; IPR002138; Pept_C14_p10.
DR   InterPro; IPR002398; Pept_C14_p45.
DR   InterPro; IPR015917; Pept_C14_p45_core.
DR   PANTHER; PTHR10454:SF30; Casp3_like; 1.
DR   PANTHER; PTHR10454; Pept_C14_p45; 1.
DR   Pfam; PF00656; Peptidase_C14; 1.
DR   PRINTS; PR00376; IL1BCENZYME.
DR   SMART; SM00115; CASc; 1.
DR   PROSITE; PS01122; CASPASE_CYS; 1.
DR   PROSITE; PS01121; CASPASE_HIS; 1.
DR   PROSITE; PS50207; CASPASE_P10; 1.
DR   PROSITE; PS50208; CASPASE_P20; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Cytoplasm; Hydrolase; Phosphoprotein;
KW   Protease; S-nitrosylation; Thiol protease; Zymogen.
FT   PROPEP        1      9       By similarity.
FT                                /FTId=PRO_0000004573.
FT   PROPEP       10     28       By similarity.
FT                                /FTId=PRO_0000004574.
FT   CHAIN        29    175       Caspase-3 subunit p17.
FT                                /FTId=PRO_0000004575.
FT   CHAIN       176    277       Caspase-3 subunit p12.
FT                                /FTId=PRO_0000004576.
FT   ACT_SITE    121    121       By similarity.
FT   ACT_SITE    163    163       By similarity.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      26     26       Phosphoserine.
FT   MOD_RES      82     82       N6-acetyllysine (By similarity).
FT   MOD_RES     163    163       S-nitrosocysteine; in inhibited form (By
FT                                similarity).
FT   CONFLICT     63     65       SRS -> ARN (in Ref. 6; AAD09504).
FT   CONFLICT    231    231       E -> Q (in Ref. 6; AAD09504).
FT   CONFLICT    262    262       I -> F (in Ref. 6; AAD09504).
SQ   SEQUENCE   277 AA;  31475 MW;  CE91598F74826605 CRC64;
     MENNKTSVDS KSINNFEVKT IHGSKSVDSG IYLDSSYKMD YPEMGICIII NNKNFHKSTG
     MSSRSGTDVD AANLRETFMG LKYQVRNKND LTREDILELM DSVSKEDHSK RSSFVCVILS
     HGDEGVIYGT NGPVELKKLT SFFRGDYCRS LTGKPKLFII QACRGTELDC GIETDSGTDE
     EMACQKIPVE ADFLYAYSTA PGYYSWRNSK DGSWFIQSLC SMLKLYAHKL EFMHILTRVN
     RKVATEFESF SLDSTFHAKK QIPCIVSMLT KELYFYH
//
ID   PYRG1_MOUSE             Reviewed;         591 AA.
AC   P70698; Q922Y4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=CTP synthase 1;
DE            EC=6.3.4.2;
DE   AltName: Full=CTP synthetase 1;
DE   AltName: Full=UTP--ammonia ligase 1;
GN   Name=Ctps;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Liver;
RA   Ding J.H., Yang B.Z., Zhang H., Roe C.R.;
RT   "Molecular cloning of the mouse liver CTP synthetase cDNA.";
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-566; TYR-567; SER-568;
RP   SER-571; SER-573 AND SER-574, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC       either L-glutamine or ammonia as the source of nitrogen.
CC   -!- CATALYTIC ACTIVITY: ATP + UTP + NH(3) = ADP + phosphate + CTP.
CC   -!- ENZYME REGULATION: Activated by GTP and inhibited by CTP.
CC   -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo
CC       pathway; CTP from UDP: step 2/2.
CC   -!- SIMILARITY: Belongs to the CTP synthase family.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
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DR   EMBL; U49350; AAB06942.1; -; mRNA.
DR   EMBL; AK148259; BAE28443.1; -; mRNA.
DR   EMBL; BC006698; AAH06698.1; -; mRNA.
DR   IPI; IPI00111959; -.
DR   RefSeq; NP_058028.2; NM_016748.2.
DR   UniGene; Mm.1815; -.
DR   ProteinModelPortal; P70698; -.
DR   SMR; P70698; 1-273, 296-562.
DR   STRING; P70698; -.
DR   PhosphoSite; P70698; -.
DR   PRIDE; P70698; -.
DR   Ensembl; ENSMUST00000030381; ENSMUSP00000030381; ENSMUSG00000028633.
DR   GeneID; 51797; -.
DR   KEGG; mmu:51797; -.
DR   NMPDR; fig|10090.3.peg.10283; -.
DR   UCSC; uc008uni.1; mouse.
DR   CTD; 51797; -.
DR   MGI; MGI:1858304; Ctps.
DR   eggNOG; roNOG11081; -.
DR   HOGENOM; HBG597806; -.
DR   HOVERGEN; HBG002243; -.
DR   InParanoid; P70698; -.
DR   OMA; RVTMQKL; -.
DR   OrthoDB; EOG4868C4; -.
DR   PhylomeDB; P70698; -.
DR   BRENDA; 6.3.4.2; 244.
DR   NextBio; 308040; -.
DR   ArrayExpress; P70698; -.
DR   Bgee; P70698; -.
DR   CleanEx; MM_CTPS; -.
DR   Genevestigator; P70698; -.
DR   GermOnline; ENSMUSG00000028633; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003883; F:CTP synthase activity; IEA:EC.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR004468; CTP_synthase.
DR   InterPro; IPR017456; CTP_synthase_N.
DR   InterPro; IPR017926; GATASE_1.
DR   InterPro; IPR000991; GATase_class1_C.
DR   Pfam; PF06418; CTP_synth_N; 1.
DR   Pfam; PF00117; GATase; 1.
DR   TIGRFAMs; TIGR00337; PyrG; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Glutamine amidotransferase; Ligase;
KW   Nucleotide-binding; Phosphoprotein; Pyrimidine biosynthesis.
FT   CHAIN         1    591       CTP synthase 1.
FT                                /FTId=PRO_0000138276.
FT   DOMAIN      300    554       Glutamine amidotransferase type-1.
FT   ACT_SITE    399    399       For GATase activity (By similarity).
FT   ACT_SITE    526    526       For GATase activity (By similarity).
FT   ACT_SITE    528    528       For GATase activity (By similarity).
FT   MOD_RES     100    100       N6-acetyllysine (By similarity).
FT   MOD_RES     562    562       Phosphoserine (By similarity).
FT   MOD_RES     566    566       Phosphothreonine.
FT   MOD_RES     567    567       Phosphotyrosine.
FT   MOD_RES     568    568       Phosphoserine.
FT   MOD_RES     571    571       Phosphoserine.
FT   MOD_RES     573    573       Phosphoserine.
FT   MOD_RES     574    574       Phosphoserine.
FT   MOD_RES     575    575       Phosphoserine.
FT   MOD_RES     581    581       Phosphothreonine (By similarity).
FT   MOD_RES     587    587       Phosphoserine (By similarity).
FT   CONFLICT     37     37       I -> F (in Ref. 1; AAB06942).
FT   CONFLICT    308    308       T -> P (in Ref. 1; AAB06942).
FT   CONFLICT    388    388       A -> S (in Ref. 1; AAB06942).
FT   CONFLICT    402    402       M -> I (in Ref. 1; AAB06942).
SQ   SEQUENCE   591 AA;  66682 MW;  81083429870BF0DE CRC64;
     MKYILVTGGV ISGIGKGVIA SSVGTILKSC GLHVTSIKID PYINIDAGTF SPYEHGEVFV
     LDDGGEVDLD LGNYERFLDI RLTKDNNLTT GKIYQYVINK ERKGDYLGKT VQVVPHITDA
     IQEWVMRQAL IPVDEDGLEP QVCVIELGGT VGDIESMPFI EAFRQFQFKV KRENFCNIHV
     SLVPQPSSTG EQKTKPTQNS VRELRGLGLS PDLVVCRCSN PLDTSVKEKI SMFCHVEPEQ
     VICVHDVSSI YRVPLLLEEQ GVVDYFLRRL DLPIERQSRK MLMKWKEMAD RYDRLLETCS
     IALVGKYTKF SDSYASVIKA LEHSALAINH KLEIKYIDST DLEPSTLQEE PVRYHEAWQK
     LCSAHGVLVP GGFGVRGTEG KIQAIAWARK QKKPFLGVCL GMQLAVVEFS RNVLGWQDAN
     STEFDPKTSH PVVIDMPEHN PGQMGGTMRL GKRRTLFQTK NSVMRKLYGD TDYLEERHRH
     RFEVNPVLKK CLEEQGLKFV GQDVEGERME IVELEDHPFF VGVQYHPEFL SRPIKPSPPY
     FGLLLASVGR LPHYLQKGCR LSPRDTYSDR SGSSSPDSEI TELKFPSISQ D
//
ID   TCPG_MOUSE              Reviewed;         545 AA.
AC   P80318;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   08-MAR-2011, entry version 100.
DE   RecName: Full=T-complex protein 1 subunit gamma;
DE            Short=TCP-1-gamma;
DE   AltName: Full=CCT-gamma;
DE   AltName: Full=Matricin;
DE   AltName: Full=mTRiC-P5;
GN   Name=Cct3; Synonyms=Cctg;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=129/Sv;
RX   MEDLINE=95041331; PubMed=7953530; DOI=10.1016/S0960-9822(94)00024-2;
RA   Kubota H., Hynes G., Carne A., Ashworth A., Willison K.R.;
RT   "Identification of six Tcp-1-related genes encoding divergent subunits
RT   of the TCP-1-containing chaperonin.";
RL   Curr. Biol. 4:89-99(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94154003; PubMed=8110840; DOI=10.1016/0167-4781(94)90041-8;
RA   Joly E.C., Sevigny G., Todorov I.T., Bibor-Hardy V.;
RT   "cDNA encoding a novel TCP1-related protein.";
RL   Biochim. Biophys. Acta 1217:224-226(1994).
RN   [3]
RP   PROTEIN SEQUENCE OF 32-38; 128-138; 150-163; 204-216; 238-248;
RP   428-461; 492-502 AND 508-518, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 210-386.
RX   PubMed=12083524; DOI=10.1016/S0022-2836(02)00190-0;
RA   Pappenberger G., Wilsher J.A., Roe S.M., Counsell D.J., Willison K.R.,
RA   Pearl L.H.;
RT   "Crystal structure of the CCTgamma apical domain: implications for
RT   substrate binding to the eukaryotic cytosolic chaperonin.";
RL   J. Mol. Biol. 318:1367-1379(2002).
CC   -!- FUNCTION: Molecular chaperone; assists the folding of proteins
CC       upon ATP hydrolysis. As part of the BBS/CCT complex may play a
CC       role in the assembly of BBSome, a complex involved in ciliogenesis
CC       regulating transports vesicles to the cilia. Known to play a role,
CC       in vitro, in the folding of actin and tubulin. Plays a role in the
CC       assembly of the von Hippel-Lindau ubiquitination complex (By
CC       similarity).
CC   -!- SUBUNIT: Heterooligomeric complex of about 850 to 900 kDa that
CC       forms two stacked rings, 12 to 16 nm in diameter. Interacts with
CC       PACRG. Component of the BBS/CCT complex composed at least of MKKS,
CC       BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- SIMILARITY: Belongs to the TCP-1 chaperonin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA19749.1; Type=Erroneous initiation;
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DR   EMBL; Z31556; CAA83431.1; -; mRNA.
DR   EMBL; L20509; AAA19749.1; ALT_INIT; mRNA.
DR   IPI; IPI00116283; -.
DR   PIR; S42723; S42723.
DR   PIR; S43062; S43062.
DR   RefSeq; NP_033966.1; NM_009836.1.
DR   UniGene; Mm.256034; -.
DR   PDB; 1GML; X-ray; 2.20 A; A/B/C/D=210-380.
DR   PDB; 1GN1; X-ray; 2.80 A; A/B/C/D/E/F/G/H=210-380.
DR   PDBsum; 1GML; -.
DR   PDBsum; 1GN1; -.
DR   ProteinModelPortal; P80318; -.
DR   SMR; P80318; 7-526.
DR   STRING; P80318; -.
DR   PhosphoSite; P80318; -.
DR   REPRODUCTION-2DPAGE; IPI00116283; -.
DR   REPRODUCTION-2DPAGE; P80318; -.
DR   PRIDE; P80318; -.
DR   Ensembl; ENSMUST00000001452; ENSMUSP00000001452; ENSMUSG00000001416.
DR   GeneID; 12462; -.
DR   KEGG; mmu:12462; -.
DR   UCSC; uc008puo.1; mouse.
DR   CTD; 12462; -.
DR   MGI; MGI:104708; Cct3.
DR   eggNOG; roNOG10671; -.
DR   HOGENOM; HBG497503; -.
DR   HOVERGEN; HBG104982; -.
DR   InParanoid; P80318; -.
DR   OMA; LRGPSKD; -.
DR   OrthoDB; EOG4MPHPZ; -.
DR   PhylomeDB; P80318; -.
DR   NextBio; 281324; -.
DR   ArrayExpress; P80318; -.
DR   Bgee; P80318; -.
DR   CleanEx; MM_CCT3; -.
DR   Genevestigator; P80318; -.
DR   GermOnline; ENSMUSG00000001416; Mus musculus.
DR   GO; GO:0005832; C:chaperonin-containing T-complex; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   InterPro; IPR012719; Chap_CCT_gamma.
DR   InterPro; IPR017998; Chaperone_TCP-1.
DR   InterPro; IPR002194; Chaperonin_TCP-1_CS.
DR   InterPro; IPR002423; Cpn60/TCP-1.
DR   PANTHER; PTHR11353:SF24; Chap_CCT_gamma; 1.
DR   PANTHER; PTHR11353; Cpn60/TCP-1; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   PRINTS; PR00304; TCOMPLEXTCP1.
DR   SUPFAM; SSF48592; GroEL-ATPase; 1.
DR   TIGRFAMs; TIGR02344; chap_CCT_gamma; 1.
DR   PROSITE; PS00750; TCP1_1; 1.
DR   PROSITE; PS00751; TCP1_2; 1.
DR   PROSITE; PS00995; TCP1_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Chaperone; Cytoplasm;
KW   Direct protein sequencing; Disulfide bond; Nucleotide-binding;
KW   Phosphoprotein.
FT   CHAIN         1    545       T-complex protein 1 subunit gamma.
FT                                /FTId=PRO_0000128322.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     222    222       N6-acetyllysine (By similarity).
FT   MOD_RES     244    244       Phosphoserine (By similarity).
FT   MOD_RES     254    254       Phosphothreonine (By similarity).
FT   DISULFID    366    372
FT   CONFLICT    124    124       S -> G (in Ref. 2; AAA19749).
FT   CONFLICT    150    150       E -> D (in Ref. 2; AAA19749).
FT   CONFLICT    154    154       S -> N (in Ref. 2; AAA19749).
FT   CONFLICT    276    276       H -> Q (in Ref. 2; AAA19749).
FT   CONFLICT    365    365       D -> E (in Ref. 2; AAA19749).
FT   CONFLICT    474    474       S -> N (in Ref. 2; AAA19749).
FT   CONFLICT    534    534       N -> S (in Ref. 2; AAA19749).
FT   CONFLICT    537    538       TG -> SS (in Ref. 2; AAA19749).
FT   CONFLICT    542    542       A -> G (in Ref. 2; AAA19749).
FT   STRAND      213    221
FT   STRAND      232    235
FT   STRAND      238    243
FT   HELIX       264    283
FT   STRAND      288    294
FT   HELIX       298    306
FT   STRAND      310    312
FT   HELIX       317    327
FT   STRAND      331    333
FT   HELIX       335    337
FT   HELIX       340    342
FT   STRAND      347    355
FT   STRAND      358    368
FT   STRAND      373    377
SQ   SEQUENCE   545 AA;  60630 MW;  492F9743C607FA1D CRC64;
     MMGHRPVLVL SQNTKRESGR KVQSGNINAA KTIADIIRTC LGPKSMMKML LDPMGGIVMT
     NDGNAILREI QVQHPAAKSM IEISRTQDEE VGDGTTSVII LAGEMLSVAE HFLEQQMHPT
     VVISAYRMAL DDMISTLKKI STPVDVNNRE MMLSIINSSI TTKVISRWSS LACNIALDAV
     KTVQFEENGR KEIDIKKYAR VEKIPGGIIE DSCVLRGVMI NKDVTHPRMR RYIKNPRIVL
     LDSSLEYKKG ESQTDIEITR EEDFTRILQM EEEYIHQLCE DIIQLKPDVV ITEKGISDLA
     QHYLMRANVT AIRRVRKTDN NRIARACGAR IVSRPEELRE DDVGTGAGLL EIKKIGDEYF
     TFITDCKDPK ACTILLRGAS KEILSEVERN LQDAMQVCRN VLLDPQLVPG GGASEMAVAH
     ALTEKSKAMT GVEQWPYRAV AQALEVIPRT LIQNCGASTI RLLTSLRAKH TQESCETWGV
     NGETGTLVDM KELGIWEPLA VKLQTYKTAV ETAVLLLRID DIVSGHKKKG DDQNRQTGAP
     DAGQE
//
ID   PTPR2_MOUSE             Reviewed;        1001 AA.
AC   P80560; O09134; P70328;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Receptor-type tyrosine-protein phosphatase N2;
DE            Short=R-PTP-N2;
DE            EC=3.1.3.48;
DE   AltName: Full=PTP IA-2beta;
DE   AltName: Full=Protein tyrosine phosphatase-NP;
DE            Short=PTP-NP;
DE   Flags: Precursor;
GN   Name=Ptprn2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=96281667; PubMed=8681804;
RA   Chiang M.-K., Flanagan J.G.;
RT   "PTP-NP, a new member of the receptor protein tyrosine phosphatase
RT   family, implicated in development of nervous system and pancreatic
RT   endocrine cells.";
RL   Development 122:2239-2250(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 282-1001.
RC   TISSUE=Neonatal brain;
RX   MEDLINE=96197307; PubMed=8637868; DOI=10.1073/pnas.93.6.2307;
RA   Lu J., Li Q., Xie H., Chen Z.-J., Borovitskaya A.E., Maclaren N.K.,
RA   Notkins A.L., Lan M.S.;
RT   "Identification of a second transmembrane protein tyrosine
RT   phosphatase, IA-2beta, as an autoantigen in insulin-dependent diabetes
RT   mellitus: precursor of the 37-kDa tryptic fragment.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:2307-2311(1996).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-678, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Implicated in development of nervous system and
CC       pancreatic endocrine cells.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1; Synonyms=Type 1-PTP-NP;
CC         IsoId=P80560-1; Sequence=Displayed;
CC       Name=2; Synonyms=Type 2-PTP-NP;
CC         IsoId=P80560-2; Sequence=Not described;
CC   -!- TISSUE SPECIFICITY: Pancreas and brain.
CC   -!- DEVELOPMENTAL STAGE: Expressed in early stages of pancreatic
CC       development. First expressed in day 8.5 embryos (E8.5) in the
CC       dorsal part of the midgut endoderm and by E9.5, in the pancreatic
CC       rudiment specifically in early endocrine progenitor cells. At
CC       later stages expressed in insulin- or glucagon-producing cells.
CC       During neural development, the type 2 PTP-NP is expressed in early
CC       stages of neurogenesis, and the type 1 weakly in the later stages.
CC   -!- PTM: Appears to undergo multiple proteolytic cleavage at
CC       consecutive basic residues (By similarity).
CC   -!- DISEASE: Note=Autoantigen in insulin-dependent diabetes mellitus
CC       (IDDM).
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U57345; AAB06945.1; -; mRNA.
DR   EMBL; U82439; AAB39996.1; -; mRNA.
DR   IPI; IPI00118191; -.
DR   UniGene; Mm.206054; -.
DR   ProteinModelPortal; P80560; -.
DR   SMR; P80560; 494-584, 710-996.
DR   STRING; P80560; -.
DR   PhosphoSite; P80560; -.
DR   PRIDE; P80560; -.
DR   Ensembl; ENSMUST00000070733; ENSMUSP00000064046; ENSMUSG00000056553.
DR   UCSC; uc007phx.1; mouse.
DR   MGI; MGI:107418; Ptprn2.
DR   HOGENOM; HBG446810; -.
DR   HOVERGEN; HBG105788; -.
DR   InParanoid; P80560; -.
DR   OrthoDB; EOG4J6RQ4; -.
DR   BRENDA; 3.1.3.48; 244.
DR   NextBio; 296180; -.
DR   ArrayExpress; P80560; -.
DR   Bgee; P80560; -.
DR   Genevestigator; P80560; -.
DR   GermOnline; ENSMUSG00000056553; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030141; C:stored secretory granule; IDA:MGI.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   InterPro; IPR021613; Receptor_IA-2.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Pfam; PF11548; Receptor_IA-2; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Diabetes mellitus; Glycoprotein;
KW   Hydrolase; Membrane; Phosphoprotein; Protein phosphatase; Receptor;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     27       Potential.
FT   CHAIN        28   1001       Receptor-type tyrosine-protein
FT                                phosphatase N2.
FT                                /FTId=PRO_0000025456.
FT   TOPO_DOM     28    600       Extracellular (Potential).
FT   TRANSMEM    601    621       Helical; (Potential).
FT   TOPO_DOM    622   1001       Cytoplasmic (Potential).
FT   DOMAIN      731    991       Tyrosine-protein phosphatase.
FT   REGION      931    937       Substrate binding (By similarity).
FT   ACT_SITE    931    931       Phosphocysteine intermediate (Potential).
FT   BINDING     899    899       Substrate (By similarity).
FT   BINDING     976    976       Substrate (By similarity).
FT   SITE        413    414       Cleavage (By similarity).
FT   MOD_RES     678    678       Phosphoserine.
FT   MOD_RES     956    956       N6-acetyllysine (By similarity).
FT   MOD_RES     963    963       Phosphothreonine (By similarity).
FT   CARBOHYD    550    550       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    370    371       Missing (in Ref. 2).
FT   CONFLICT    395    395       H -> P (in Ref. 2; AAB39996).
FT   CONFLICT    411    411       I -> M (in Ref. 2; AAB39996).
FT   CONFLICT    414    414       S -> L (in Ref. 2; AAB39996).
FT   CONFLICT    586    586       L -> H (in Ref. 2; AAB39996).
SQ   SEQUENCE   1001 AA;  111555 MW;  6B73EACA535D2BE5 CRC64;
     MGPPLPLLLL LLLPPPLPRA LPAPASARGR QLPGRLGCLF EDGLCGSLET CVNDGVFGRC
     QKVPVMDTYR YEVPPGALLH LKVTLQKLSR TGFTWQDDYT QRVIAQELAN LPKAYLWHGE
     TSGPARSLQQ NADNEKWFSL EREVALAKTL RRYLPYLELL SQTPTANAHS RIDHETRPAK
     GEDSSPENIL TYVAHTSALT YPPATRAKYP DNLLRPFSRL QPDELSPKVD GDIDKQKLIA
     ALGAYTAQRL PGENDPEPRY LVHGSSRAPR PFSATALSQR WPPPPGDAKD SPSMDDDTLL
     QSLLKDLQQN SEVDRLGPLK EEKADSVAGA IQSDPAEGSQ ESHGRGAEGQ PREQTDAPET
     MLQDHRLSDV DDPVYKEVNR LSFQLGDLLK DYGSHLLPEG PLLEKSSREE IKKSEQPEEV
     LSSEEETAGV EHVRSRTYSK DLFERKPNSE PQPRRLEDQF QNRAPELWED EESLKLAAQG
     PPSGGLQLEV QPSEEQQGYI LTGNNPLSPE KGKQLMDQVA HILRVPSSFF ADIKVLGPAV
     TFKVSANIQN MTTADVIKAA ADNKDQLEKA TGLTILQSGI RPKGKLKLLP HQEEQEDSTK
     FILLTFLSIA CILGVLLASS LAYCLRHNSH YKLKDKLSGL GADPSADATE AYQELCRQRM
     AVRPQDRSEG PHTSRINSVS SQFSDGPMPS PSARSSTSSW SEEPVQSNMD ISTGHMILAY
     MEDHLKNKNR LEKEWEALCA YQAEPNSSLV AQREENAPKN RSLAVLTYDH SRILLKSQNS
     HGSSDYINAS PIMDHDPRNP AYIATQGPLP ATVADFWQMV WESGCAVIVM LTPLSENGVR
     QCHHYWPDEG SNLYHVYEVN LVSEHIWCQD FLVRSFYLKN LQTNETRTVT QFHFLSWYDQ
     GVPSSTRSLL DFRRKVNKCY RGRSCPIIVH CSDGAGRSGT YVLIDMVLNK MAKGAKEIDI
     AATLEHLRDQ RPGMVQTKEQ FEFALTAVAE EVNAILKALP Q
//
ID   IRS2_MOUSE              Reviewed;        1321 AA.
AC   P81122;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Insulin receptor substrate 2;
DE            Short=IRS-2;
DE   AltName: Full=4PS;
GN   Name=Irs2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE, AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=95405472; PubMed=7675087; DOI=10.1038/377173a0;
RA   Sun X.J., Wang L.-M., Zhang Y., Yenush L., Myers M.G. Jr.,
RA   Glasheen E., Lane W.S., Pierce J.H., White M.F.;
RT   "Role of IRS-2 in insulin and cytokine signalling.";
RL   Nature 377:173-177(1995).
RN   [2]
RP   INTERACTION WITH PHIP.
RX   MEDLINE=20568313; PubMed=11018022; DOI=10.1074/jbc.C000611200;
RA   Farhang-Fallah J., Yin X., Trentin G., Cheng A.M., Rozakis-Adcock M.;
RT   "Cloning and characterization of PHIP, a novel insulin receptor
RT   substrate-1 pleckstrin homology domain interacting protein.";
RL   J. Biol. Chem. 275:40492-40497(2000).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17636024; DOI=10.1128/MCB.02409-06;
RA   Podcheko A., Northcott P., Bikopoulos G., Lee A., Bommareddi S.R.,
RA   Kushner J.A., Farhang-Fallah J., Rozakis-Adcock M.;
RT   "Identification of a WD40 repeat-containing isoform of PHIP as a novel
RT   regulator of beta-cell growth and survival.";
RL   Mol. Cell. Biol. 27:6484-6496(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-649, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303; SER-556 AND
RP   SER-1165, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May mediate the control of various cellular processes by
CC       insulin.
CC   -!- SUBUNIT: Interacts with PHIP.
CC   -!- INTERACTION:
CC       Q8VDD9:Phip; NbExp=1; IntAct=EBI-1369862, EBI-1369766;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol.
CC   -!- TISSUE SPECIFICITY: Skeletal muscle, lung, brain, liver, kidney,
CC       heart and spleen.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 IRS-type PTB domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   IPI; IPI00379844; -.
DR   UniGene; Mm.407207; -.
DR   PDB; 3BU3; X-ray; 1.65 A; B=620-634.
DR   PDB; 3BU5; X-ray; 2.10 A; B=620-634.
DR   PDB; 3BU6; X-ray; 1.95 A; B=620-634.
DR   PDBsum; 3BU3; -.
DR   PDBsum; 3BU5; -.
DR   PDBsum; 3BU6; -.
DR   ProteinModelPortal; P81122; -.
DR   SMR; P81122; 30-300.
DR   DIP; DIP-39500N; -.
DR   IntAct; P81122; 3.
DR   MINT; MINT-100745; -.
DR   STRING; P81122; -.
DR   PhosphoSite; P81122; -.
DR   PRIDE; P81122; -.
DR   Ensembl; ENSMUST00000040514; ENSMUSP00000038514; ENSMUSG00000038894.
DR   UCSC; uc009kuz.1; mouse.
DR   MGI; MGI:109334; Irs2.
DR   HOGENOM; HBG443689; -.
DR   HOVERGEN; HBG000542; -.
DR   InParanoid; P81122; -.
DR   OrthoDB; EOG44MXTG; -.
DR   ArrayExpress; P81122; -.
DR   Bgee; P81122; -.
DR   CleanEx; MM_IRS2; -.
DR   Genevestigator; P81122; -.
DR   GermOnline; ENSMUSG00000038894; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0019901; F:protein kinase binding; IDA:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0007420; P:brain development; IMP:MGI.
DR   GO; GO:0008283; P:cell proliferation; IMP:MGI.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IMP:MGI.
DR   GO; GO:0030879; P:mammary gland development; IGI:MGI.
DR   GO; GO:0002903; P:negative regulation of B cell apoptosis; IMP:BHF-UCL.
DR   GO; GO:0033673; P:negative regulation of kinase activity; IMP:BHF-UCL.
DR   GO; GO:0030890; P:positive regulation of B cell proliferation; IDA:BHF-UCL.
DR   GO; GO:0030335; P:positive regulation of cell migration; IGI:MGI.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; IMP:BHF-UCL.
DR   GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IGI:MGI.
DR   GO; GO:0009749; P:response to glucose stimulus; IDA:BHF-UCL.
DR   InterPro; IPR002404; Insln_rcpt_S1.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Pfam; PF02174; IRS; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00628; INSULINRSI.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00310; PTBI; 1.
DR   PROSITE; PS51064; IRS_PTB; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Phosphoprotein;
KW   Transducer.
FT   CHAIN         1   1321       Insulin receptor substrate 2.
FT                                /FTId=PRO_0000084240.
FT   DOMAIN       16    144       PH.
FT   DOMAIN      191    295       IRS-type PTB.
FT   MOTIF       536    539       YXXM motif 1.
FT   MOTIF       594    597       YXXM motif 2.
FT   MOTIF       649    652       YXXM motif 3.
FT   MOTIF       671    674       YXXM motif 4.
FT   MOTIF       734    737       YXXM motif 5.
FT   MOTIF       814    817       YXXM motif 6.
FT   MOTIF      1061   1064       YXXM motif 7.
FT   COMPBIAS     19     28       Poly-Asn.
FT   COMPBIAS    444    449       Poly-Ser.
FT   COMPBIAS    638    641       Poly-Ser.
FT   COMPBIAS    936    939       Poly-Ser.
FT   MOD_RES      75     75       Phosphotyrosine (By similarity).
FT   MOD_RES     303    303       Phosphoserine.
FT   MOD_RES     306    306       Phosphoserine (By similarity).
FT   MOD_RES     331    331       Phosphoserine (By similarity).
FT   MOD_RES     343    343       Phosphoserine (By similarity).
FT   MOD_RES     347    347       Phosphothreonine (By similarity).
FT   MOD_RES     360    360       Phosphothreonine (By similarity).
FT   MOD_RES     362    362       Phosphoserine (By similarity).
FT   MOD_RES     381    381       Phosphoserine (By similarity).
FT   MOD_RES     385    385       Phosphoserine (By similarity).
FT   MOD_RES     388    388       Phosphoserine (By similarity).
FT   MOD_RES     517    517       Phosphothreonine (By similarity).
FT   MOD_RES     520    520       Phosphoserine (By similarity).
FT   MOD_RES     524    524       Phosphothreonine (By similarity).
FT   MOD_RES     536    536       Phosphotyrosine; by INSR (By similarity).
FT   MOD_RES     556    556       Phosphoserine.
FT   MOD_RES     573    573       Phosphoserine (By similarity).
FT   MOD_RES     575    575       Phosphothreonine (By similarity).
FT   MOD_RES     576    576       Phosphothreonine (By similarity).
FT   MOD_RES     590    590       Phosphoserine (By similarity).
FT   MOD_RES     594    594       Phosphotyrosine (By similarity).
FT   MOD_RES     604    604       Phosphoserine (By similarity).
FT   MOD_RES     616    616       Phosphoserine (By similarity).
FT   MOD_RES     649    649       Phosphotyrosine.
FT   MOD_RES     671    671       Phosphotyrosine; by INSR (By similarity).
FT   MOD_RES     675    675       Phosphoserine (By similarity).
FT   MOD_RES     722    722       Phosphoserine (By similarity).
FT   MOD_RES     723    723       Phosphoserine (By similarity).
FT   MOD_RES     727    727       Phosphoserine (By similarity).
FT   MOD_RES     728    728       Phosphoserine (By similarity).
FT   MOD_RES     734    734       Phosphotyrosine (By similarity).
FT   MOD_RES     762    762       Phosphoserine (By similarity).
FT   MOD_RES     764    764       Phosphoserine (By similarity).
FT   MOD_RES     771    771       Phosphothreonine (By similarity).
FT   MOD_RES     814    814       Phosphotyrosine (By similarity).
FT   MOD_RES     819    819       Phosphoserine (By similarity).
FT   MOD_RES     886    886       Phosphoserine (By similarity).
FT   MOD_RES     907    907       Phosphoserine (By similarity).
FT   MOD_RES     911    911       Phosphotyrosine; by INSR (By similarity).
FT   MOD_RES     965    965       Phosphoserine (By similarity).
FT   MOD_RES     970    970       Phosphotyrosine; by INSR (By similarity).
FT   MOD_RES    1089   1089       Phosphoserine (By similarity).
FT   MOD_RES    1092   1092       Phosphoserine (By similarity).
FT   MOD_RES    1137   1137       Phosphoserine (By similarity).
FT   MOD_RES    1138   1138       Phosphoserine (By similarity).
FT   MOD_RES    1148   1148       Phosphothreonine (By similarity).
FT   MOD_RES    1151   1151       Phosphoserine (By similarity).
FT   MOD_RES    1163   1163       Phosphoserine (By similarity).
FT   MOD_RES    1165   1165       Phosphoserine.
FT   MOD_RES    1190   1190       Phosphoserine (By similarity).
FT   MOD_RES    1242   1242       Phosphotyrosine; by INSR (By similarity).
FT   MOD_RES    1303   1303       Phosphotyrosine; by INSR (By similarity).
FT   HELIX       625    627
FT   STRAND      629    633
SQ   SEQUENCE   1321 AA;  136527 MW;  5069CE9D614960C7 CRC64;
     MASAPLPGPP ASGGGDGPNL NNNNNNNNHS VRKCGYLRKQ KHGHKRFFVL RGPGTGGDEA
     SAAGGSPPQP PRLEYYESEK KWRSKAGAPK RVIALDCCLN INKRADAKHK YLIALYTKDE
     YFAVAAENEQ EQEGWYRALT DLVSEGRSGE GGSGTTGGSC SASLPGVLGG SAGAAGCDDN
     YGLVTPATAV YREVWQVNLK PKGLGQSKNL TGVYRLCLSA RTIGFVKLNC EGPSVTLQLN
     NIRRCGHSDS FFFIEVGRSA VTGPGELWMQ ADDSVVAQNI HETILEAMKA LKELFEFRPR
     SKSQSSGSSA THPISVPGAR RHHHLVNLPP SQTGLVRRSR TDSLAATPPA AKCTSCRVRT
     ASEGDGGAAG GAGTAGGRPM SVAGSPLSPG PVRAPLSRSH TLSAGCGGRP SKVTLAPAGG
     ALQHSRSNSM PVAHSPPAAT SPGSLSSSSG HGSGSYPLPP GSHPHLPHPL HHPQGQRPSS
     GSASASGSPS DPGFMSLDEY GSSPGDLRAF SSHRSNTPES IAETPPARDG SGGELYGYMS
     MDRPLSHCGR PYRRVSGDGA QDLDRGLRKR TYSLTTPARQ RQVPQPSSAS LDEYTLMRAT
     FSGSSGRLCP SFPASSPKVA YNPYPEDYGD IEIGSHKSSS SNLGADDGYM PMTPGAALRS
     GGPNSCKSDD YMPMSPTSVS APKQILQPRL AAALPPSGAA VPAPPSGVGR TFPVNGGGYK
     ASSPAESSPE DSGYMRMWCG SKLSMENPDP KLLPNGDYLN KSPSEAGTAG TPPDFSAALR
     GGSEGLKGIP GHCYSSLPRS YKAPCSCSGD NDQYVLMSSP VGRILEEERL EPQATPGAGT
     FGAAGGSHTQ PHHSAVPSSM RPSAIGGRPE GFLGQRCRAV RPTRLSLEGL QTLPSMQEYP
     LPTEPKSPGE YINIDPGEAG TRLSPPAPPL LASAASSSSL LSASSPASSL GSGTPGTSSD
     SRQRSPLSDY MNLDPSSPKS PKPSTRSGDT VGSMDGLLSP EASSPYPPLP PRPSTSPSSL
     QQPLPPAPGD LYRLPPASAA TSQGPTAGSS MSSEPGDNGD YSEMAFGVAA TPPQPIVAPP
     KPEGARVASP TSGLKRLSLM DQVSGVEAFL QVSQPPDPHR GAKVIRADPQ GGRRRHSSET
     FSSTTTVTPV SPSFAHNSKR HNSASVENVS LRKSSEGSST LGGGDEPPTS PGQAQPLVAV
     PPVPQARPWN PGQPGALIGC PGGSSSPMRR ETSVGFQNGL NYIAIDVRGE QGSLAQSQPQ
     PGDKNSWSRT RSLGGLLGTV GGSGASGVCG GPGTGALPSA STYASIDFLS HHLKEATVVK
     E
//
ID   ERG_MOUSE               Reviewed;         486 AA.
AC   P81270; A6H6E7; Q8C5L4; Q920K7; Q920K8; Q920K9;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2003, sequence version 2.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Transcriptional regulator ERG;
GN   Name=Erg; Synonyms=Erg-3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RA   Ozawa R., Noguchi H., Taylor T.D., Takeda T., Hattori M., Sakaki Y.;
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 5).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 181-452.
RX   MEDLINE=94019387; PubMed=8413305;
RA   Rivera R.R., Stuiver M.H., Steenbergen R., Murre C.;
RT   "Ets proteins: new factors that regulate immunoglobulin heavy-chain
RT   gene expression.";
RL   Mol. Cell. Biol. 13:7163-7169(1993).
RN   [5]
RP   INTERACTION WITH SETDB1.
RX   MEDLINE=21650957; PubMed=11791185; DOI=10.1038/sj.onc.1204998;
RA   Yang L., Xia L., Wu D.Y., Wang H., Chansky H.A., Schubach W.H.,
RA   Hickstein D.D., Zhang Y.;
RT   "Molecular cloning of ESET, a novel histone H3-specific
RT   methyltransferase that interacts with ERG transcription factor.";
RL   Oncogene 21:148-152(2002).
CC   -!- FUNCTION: Transcriptional regulator. May participate in
CC       transcriptional regulation through the recruitment of SETDB1
CC       histone methyltransferase and subsequent modification of local
CC       chromatin structure.
CC   -!- SUBUNIT: Identified in a mRNP granule complex, at least composed
CC       of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD,
CC       HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1,
CC       NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8,
CC       RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs (By
CC       similarity). Interacts with SETDB1.
CC   -!- INTERACTION:
CC       O88974:Setdb1; NbExp=2; IntAct=EBI-79647, EBI-79658;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm (By similarity).
CC       Note=Localized in cytoplasmic mRNP granules containing
CC       untranslated mRNAs (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=3;
CC         IsoId=P81270-1; Sequence=Displayed;
CC       Name=1;
CC         IsoId=P81270-3; Sequence=VSP_007641;
CC       Name=2;
CC         IsoId=P81270-2; Sequence=VSP_007642;
CC       Name=5;
CC         IsoId=P81270-4; Sequence=VSP_026585;
CC   -!- SIMILARITY: Belongs to the ETS family.
CC   -!- SIMILARITY: Contains 1 ETS DNA-binding domain.
CC   -!- SIMILARITY: Contains 1 PNT (pointed) domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB073078; BAB69948.1; -; mRNA.
DR   EMBL; AB073079; BAB69949.1; -; mRNA.
DR   EMBL; AB073080; BAB69950.1; -; mRNA.
DR   EMBL; AK050922; BAC34461.1; -; mRNA.
DR   EMBL; AK078113; BAC37131.1; -; mRNA.
DR   EMBL; BC145850; AAI45851.1; -; mRNA.
DR   EMBL; S66169; AAB28525.1; -; mRNA.
DR   IPI; IPI00120677; -.
DR   IPI; IPI00267007; -.
DR   IPI; IPI00331406; -.
DR   IPI; IPI00720009; -.
DR   PIR; A54617; A54617.
DR   RefSeq; NP_598420.1; NM_133659.2.
DR   UniGene; Mm.164531; -.
DR   ProteinModelPortal; P81270; -.
DR   SMR; P81270; 112-208, 313-410.
DR   IntAct; P81270; 3.
DR   STRING; P81270; -.
DR   PhosphoSite; P81270; -.
DR   PRIDE; P81270; -.
DR   Ensembl; ENSMUST00000077773; ENSMUSP00000076949; ENSMUSG00000040732.
DR   Ensembl; ENSMUST00000113845; ENSMUSP00000109476; ENSMUSG00000040732.
DR   Ensembl; ENSMUST00000113846; ENSMUSP00000109477; ENSMUSG00000040732.
DR   Ensembl; ENSMUST00000113848; ENSMUSP00000109479; ENSMUSG00000040732.
DR   Ensembl; ENSMUST00000121809; ENSMUSP00000113723; ENSMUSG00000040732.
DR   GeneID; 13876; -.
DR   KEGG; mmu:13876; -.
DR   UCSC; uc008aca.1; mouse.
DR   UCSC; uc008acb.1; mouse.
DR   UCSC; uc008acd.1; mouse.
DR   CTD; 13876; -.
DR   MGI; MGI:95415; Erg.
DR   eggNOG; roNOG13732; -.
DR   GeneTree; ENSGT00600000084192; -.
DR   HOGENOM; HBG443555; -.
DR   HOVERGEN; HBG001553; -.
DR   InParanoid; P81270; -.
DR   OMA; NSNCITW; -.
DR   NextBio; 284804; -.
DR   ArrayExpress; P81270; -.
DR   Bgee; P81270; -.
DR   Genevestigator; P81270; -.
DR   GermOnline; ENSMUSG00000040732; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030529; C:ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR000418; Ets.
DR   InterPro; IPR003118; SAM_PNT.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF00178; Ets; 1.
DR   Pfam; PF02198; SAM_PNT; 1.
DR   PRINTS; PR00454; ETSDOMAIN.
DR   SMART; SM00413; ETS; 1.
DR   SMART; SM00251; SAM_PNT; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR   PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR   PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR   PROSITE; PS51433; PNT; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    486       Transcriptional regulator ERG.
FT                                /FTId=PRO_0000204104.
FT   DOMAIN      120    206       PNT.
FT   DNA_BIND    318    398       ETS.
FT   MOD_RES      93     93       Phosphoserine (By similarity).
FT   VAR_SEQ       1     11       MIQTVPDPAAH -> MAST (in isoform 5).
FT                                /FTId=VSP_026585.
FT   VAR_SEQ     232    255       Missing (in isoform 1).
FT                                /FTId=VSP_007641.
FT   VAR_SEQ     256    278       Missing (in isoform 2).
FT                                /FTId=VSP_007642.
FT   CONFLICT    175    175       L -> Q (in Ref. 2; BAC37131).
SQ   SEQUENCE   486 AA;  54614 MW;  BF1ADF00A4772F75 CRC64;
     MIQTVPDPAA HIKEALSVVS EDQSLFECAY GTPHLAKTEM TASSSSDYGQ TSKMSPRVPQ
     QDWLSQAPAR VTIKMECNPS QVNGSRNSPD ECSVNKGGKM VGSPDTVGMS YGSYMEEKHV
     PPPNMTTNER RVIVPADPTL WSTDHVRQWL EWAVKEYGLL DVDVLLFQNI DGKELCKMTK
     DDFQRLTPSY NADILLSHLH YLRETPLPHL TSDDVDKALQ NSPRLMHARN TGGAAFIFPN
     TSVYPEATQR ITTRPDLPYE PPRRSAWTGH SHLTPQSKAA QPSPSAVPKT EDQRPQLDPY
     QILGPTSSRL ANPGSGQIQL WQFLLELLSD SSNSNCITWE GTNGEFKMTD PDEVARRWGE
     RKSKPNMNYD KLSRALRYYY DKNIMTKVHG KRYAYKFDFH GIAQALQPHP PESSLYKYPS
     DLPYMGSYHA HPQKMNFVSP HPPALPVTSS SFFASPNPYW NSPTGGIYPN TRLPASHMPS
     HLGTYY
//
ID   STIM2_MOUSE             Reviewed;         746 AA.
AC   P83093; Q69ZI3; Q80VF4;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Stromal interaction molecule 2;
DE   Flags: Precursor;
GN   Name=Stim2; Synonyms=Kiaa1482;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreatic islet;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 82-227.
RC   STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
RX   MEDLINE=21356314; PubMed=11463338; DOI=10.1042/0264-6021:3570673;
RA   Williams R.T., Manji S.S.M., Parker N.J., Hancock M.S.,
RA   van Stekelenburg L., Eid J.-P., Senior P.V., Kazenwadel J.S.,
RA   Shandala T., Saint R., Smith P.J., Dziadek M.A.;
RT   "Identification and characterization of the STIM (stromal interaction
RT   molecule) gene family: coding for a novel class of transmembrane
RT   proteins.";
RL   Biochem. J. 357:673-685(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 374-746.
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Functions as a highly sensitive Ca(2+) sensor in the
CC       endoplasmic reticulum which activates both store-operated and
CC       store-independent Ca(2+)-influx. Regulates basal cytosolic and
CC       endoplasmic reticulum Ca(2+) concentrations. Upon mild variations
CC       of the endoplasmic reticulum Ca(2+) concentration, translocates
CC       from the endoplasmic reticulum to the plasma membrane where it
CC       probably activates the Ca(2+) release-activated Ca(2+) (CRAC)
CC       channels ORAI1, ORAI2 and ORAI3. May inhibit STIM1-mediated Ca(2+)
CC       influx (By similarity).
CC   -!- SUBUNIT: Oligomer with STIM1. Interacts with ORAI1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       type I membrane protein (By similarity). Note=Dynamically
CC       translocates from a uniform endoplasmic reticulum distribution to
CC       punctual endoplasmic reticulum-plasma membrane junctions in
CC       response to decrease in endoplasmic reticulum Ca(2+) concentration
CC       (By similarity).
CC   -!- PTM: Glycosylated (By similarity).
CC   -!- PTM: Phosphorylated predominantly on Ser residues (By similarity).
CC   -!- SIMILARITY: Contains 1 EF-hand domain.
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32461.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK173183; BAD32461.1; ALT_INIT; mRNA.
DR   EMBL; AF328907; AAK82339.1; -; mRNA.
DR   EMBL; BC043455; AAH43455.1; -; mRNA.
DR   IPI; IPI00830628; -.
DR   RefSeq; NP_001074572.2; NM_001081103.2.
DR   UniGene; Mm.265985; -.
DR   ProteinModelPortal; P83093; -.
DR   SMR; P83093; 57-205.
DR   STRING; P83093; -.
DR   PRIDE; P83093; -.
DR   Ensembl; ENSMUST00000071083; ENSMUSP00000069272; ENSMUSG00000039156.
DR   Ensembl; ENSMUST00000117661; ENSMUSP00000113174; ENSMUSG00000039156.
DR   GeneID; 116873; -.
DR   KEGG; mmu:116873; -.
DR   UCSC; uc008xlp.1; mouse.
DR   CTD; 116873; -.
DR   MGI; MGI:2151156; Stim2.
DR   HOVERGEN; HBG079219; -.
DR   OrthoDB; EOG457569; -.
DR   ArrayExpress; P83093; -.
DR   Bgee; P83093; -.
DR   CleanEx; MM_STIM2; -.
DR   Genevestigator; P83093; -.
DR   GermOnline; ENSMUSG00000039156; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005246; F:calcium channel regulator activity; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0032237; P:activation of store-operated calcium channel activity; ISS:UniProtKB.
DR   GO; GO:0006816; P:calcium ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0032235; P:negative regulation of calcium ion transport via store-operated calcium channel activity; ISS:UniProtKB.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR011510; SAM_2.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS00018; EF_HAND_1; FALSE_NEG.
DR   PROSITE; PS50222; EF_HAND_2; FALSE_NEG.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Calcium; Calcium transport; Coiled coil; Endoplasmic reticulum;
KW   Glycoprotein; Ion transport; Membrane; Phosphoprotein; Signal;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL        1     14       Potential.
FT   CHAIN        15    746       Stromal interaction molecule 2.
FT                                /FTId=PRO_0000218282.
FT   TOPO_DOM     15    218       Extracellular (Potential).
FT   TRANSMEM    219    235       Helical; (Potential).
FT   TOPO_DOM    236    746       Cytoplasmic (Potential).
FT   DOMAIN       67    102       EF-hand.
FT   DOMAIN      136    204       SAM.
FT   COILED      247    394       Potential.
FT   COMPBIAS    534    552       His-rich.
FT   MOD_RES     609    609       Phosphoserine (By similarity).
FT   MOD_RES     621    621       Phosphoserine (By similarity).
FT   MOD_RES     661    661       Phosphoserine (By similarity).
FT   MOD_RES     680    680       Phosphoserine.
FT   CARBOHYD    135    135       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   746 AA;  83925 MW;  EE48455117B4E0BD CRC64;
     MLLFGLLVAG VADGCDLVPR HLRGRRASGS AGAAASPSAA AAGERQALLT DPCMSLSPPC
     FTEEDRFSLE ALQTIHKQMD DDKDGGIEVD ESDEFIREDM KYKDATNKHS HLHREDKHIT
     VEDLWKQWKT SEVHNWTLED TLQWLIEFVE LPQYEKNFRD NNVKGTTLPR IAVHETSFMI
     SQLKISDRSH RQKLQLKALD VVLFGPLTRP PHNWMKDFIL TISIVIGVGG CWFAYTQNKT
     SKEHVAKMMK DLESLQTAEQ SLMDLQERLE KAQEENRTVA VEKQNLERKM MDEINYAKEE
     ACRLRELREG AECELSRRQY AEQELEQVRM ALKKAEKEFE LRSSWSVPDA LQKWLQLTHE
     VEVQYYNIKR QNAEMQLAIA KDEAEKIKKK RSTVFGTLHV AHSSSLDEVD HKILEAKKAL
     SELTTCLRER LFRWQQIEKI CGFQIAHNSG LPSLTSSLYS DHSWVVMPRV SIPPYPIAGG
     VDDLDEDTPP IVPQFPGTVA KPAGSLARSS SLCRSRRSIV PSSPQSQRAQ LPAHAPLAAH
     PRHPHHPQHP QHSLPSPDPD ILSVSSCPAL YRNEEEEEAI YFTAEKQWEV PDTASECDSL
     NSSSGRKPSP PSSLEMYQTL SSRKISRDEL SLEDSSRGES PVTADVSRGS PECVGLTETK
     SMIFSPASRV YNGILEKSCS MHQLSSGIPV PHPRHTSCSS AGNDSKPVQE ASNVSRVSSI
     PHDLCHNGEK SKKPSKIKSL FKKKSK
//
ID   TNIK_MOUSE              Reviewed;        1323 AA.
AC   P83510;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Traf2 and NCK-interacting protein kinase;
DE            EC=2.7.11.1;
GN   Name=Tnik; Synonyms=Kiaa0551;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-327 AND 735-1323 (ISOFORM
RP   1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Hypothalamus, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 311-1323 (ISOFORM 1).
RC   TISSUE=Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 359-842 (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-950, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-740, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   INTERACTION WITH TCF7L2 AND CTNNB1, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=19816403; DOI=10.1038/emboj.2009.285;
RA   Mahmoudi T., Li V.S.W., Ng S.S., Taouatas N., Vries R.G.J.,
RA   Mohammed S., Heck A.J., Clevers H.;
RT   "The kinase TNIK is an essential activator of Wnt target genes.";
RL   EMBO J. 28:3329-3340(2009).
RN   [8]
RP   INTERACTION WITH NEDD4 AND RAP2A.
RX   PubMed=20159449; DOI=10.1016/j.neuron.2010.01.007;
RA   Kawabe H., Neeb A., Dimova K., Young S.M. Jr., Takeda M.,
RA   Katsurabayashi S., Mitkovski M., Malakhova O.A., Zhang D.E.,
RA   Umikawa M., Kariya K., Goebbels S., Nave K.A., Rosenmund C., Jahn O.,
RA   Rhee J., Brose N.;
RT   "Regulation of Rap2A by the ubiquitin ligase Nedd4-1 controls neurite
RT   development.";
RL   Neuron 65:358-372(2010).
CC   -!- FUNCTION: Serine/threonine kinase that acts as an essential
CC       activator of the Wnt signaling pathway. Recruited to promoters of
CC       Wnt target genes and required to activate their expression. May
CC       act by phosphorylating TCF4/TCF7L2. Appears to act upstream of the
CC       JUN N-terminal pathway. May play a role in the response to
CC       environmental stress. Part of a signaling complex composed of
CC       NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension
CC       and arborization during development. More generally, it may play a
CC       role in cytoskeletal rearrangements and regulate cell spreading
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts (via the CNH domain) with RAP2A (GTP-bound form
CC       preferentially); the interaction is direct and required for the
CC       activation of TNIK by RAP2A. Interacts with NEDD4; recruits RAP2A
CC       to NEDD4. Interacts with TRAF2 and NCK. Interacts with TCF7L2/TCF4
CC       and CTNNB1; the interaction is direct. Interacts with TANC1.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Recycling endosome (By
CC       similarity). Cytoplasm, cytoskeleton (By similarity).
CC       Note=Associated with recycling endosomes and the cytoskeletal
CC       fraction upon RAP2A overexpression (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P83510-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=P83510-2; Sequence=VSP_007351;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Autophosphorylated. Autophosphorylation is activated by RAP2A
CC       and induces association to the cytoskeletal fraction (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC   -!- SIMILARITY: Contains 1 CNH domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65588.2; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
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DR   EMBL; AK039113; BAC30241.1; -; mRNA.
DR   EMBL; AK041777; BAC31061.2; -; mRNA.
DR   EMBL; AK088459; BAC40365.1; -; mRNA.
DR   EMBL; BC050866; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK122306; BAC65588.2; ALT_SEQ; Transcribed_RNA.
DR   IPI; IPI00187510; -.
DR   IPI; IPI00625974; -.
DR   RefSeq; NP_001156480.1; NM_001163008.1.
DR   UniGene; Mm.126193; -.
DR   ProteinModelPortal; P83510; -.
DR   SMR; P83510; 13-313.
DR   STRING; P83510; -.
DR   PhosphoSite; P83510; -.
DR   PRIDE; P83510; -.
DR   Ensembl; ENSMUST00000159236; ENSMUSP00000124681; ENSMUSG00000027692.
DR   Ensembl; ENSMUST00000162037; ENSMUSP00000124622; ENSMUSG00000027692.
DR   GeneID; 665113; -.
DR   KEGG; mmu:665113; -.
DR   CTD; 665113; -.
DR   MGI; MGI:1916264; Tnik.
DR   eggNOG; roNOG04173; -.
DR   GeneTree; ENSGT00600000084021; -.
DR   HOVERGEN; HBG036506; -.
DR   BRENDA; 2.7.11.1; 244.
DR   Bgee; P83510; -.
DR   CleanEx; MM_TNIK; -.
DR   Genevestigator; P83510; -.
DR   GermOnline; ENSMUSG00000027692; Mus musculus.
DR   GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0005083; F:small GTPase regulator activity; IEA:InterPro.
DR   GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR   GO; GO:0007256; P:activation of JNKK activity; ISS:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR   GO; GO:0048814; P:regulation of dendrite morphogenesis; ISS:UniProtKB.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR001180; Citron.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Cytoskeleton; Endosome;
KW   Kinase; Neurogenesis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.
FT   CHAIN         1   1323       Traf2 and NCK-interacting protein kinase.
FT                                /FTId=PRO_0000086762.
FT   DOMAIN       25    289       Protein kinase.
FT   DOMAIN     1010   1297       CNH.
FT   NP_BIND      31     39       ATP (By similarity).
FT   REGION      290   1010       Mediates interaction with NEDD4 (By
FT                                similarity).
FT   ACT_SITE    153    153       Proton acceptor (By similarity).
FT   BINDING      54     54       ATP (By similarity).
FT   MOD_RES     319    319       Phosphothreonine (By similarity).
FT   MOD_RES     321    321       Phosphotyrosine (By similarity).
FT   MOD_RES     323    323       Phosphotyrosine (By similarity).
FT   MOD_RES     324    324       Phosphoserine (By similarity).
FT   MOD_RES     326    326       Phosphoserine (By similarity).
FT   MOD_RES     335    335       Phosphoserine (By similarity).
FT   MOD_RES     531    531       Phosphoserine (By similarity).
FT   MOD_RES     552    552       Phosphothreonine (By similarity).
FT   MOD_RES     611    611       Phosphoserine (By similarity).
FT   MOD_RES     648    648       Phosphothreonine (By similarity).
FT   MOD_RES     649    649       Phosphoserine (By similarity).
FT   MOD_RES     659    659       Phosphoserine (By similarity).
FT   MOD_RES     678    678       Phosphoserine (By similarity).
FT   MOD_RES     691    691       Phosphoserine (By similarity).
FT   MOD_RES     697    697       Phosphoserine (By similarity).
FT   MOD_RES     726    726       Phosphoserine (By similarity).
FT   MOD_RES     737    737       Phosphoserine (By similarity).
FT   MOD_RES     740    740       Phosphoserine.
FT   MOD_RES     793    793       Phosphoserine (By similarity).
FT   MOD_RES     794    794       Phosphoserine (By similarity).
FT   MOD_RES     795    795       Phosphoserine (By similarity).
FT   MOD_RES     796    796       Phosphoserine (By similarity).
FT   MOD_RES     801    801       Phosphoserine (By similarity).
FT   MOD_RES     802    802       Phosphoserine (By similarity).
FT   MOD_RES     914    914       Phosphoserine (By similarity).
FT   MOD_RES     945    945       Phosphotyrosine (By similarity).
FT   MOD_RES     950    950       Phosphothreonine.
FT   MOD_RES     999    999       Phosphothreonine (By similarity).
FT   VAR_SEQ     926    962       YGIGSSTKASFTPFVDPRVYQTSPTDEDEEDDESSAA ->
FT                                SLK (in isoform 2).
FT                                /FTId=VSP_007351.
FT   CONFLICT    735    735       S -> C (in Ref. 1; BAC40365).
SQ   SEQUENCE   1323 AA;  150367 MW;  B8289189530251D2 CRC64;
     MASDSPARSL DEIDLSALRD PAGIFELVEL VGNGTYGQVY KGRHVKTGQL AAIKVMDVTG
     DEEEEIKQEI NMLKKYSHHR NIATYYGAFI KKNPPGMDDQ LWLVMEFCGA GSVTDLIKNT
     KGNTLKEEWI AYICREILRG LSHLHQHKVI HRDIKGQNVL LTENAEVKLV DFGVSAQLDR
     TVGRRNTFIG TPYWMAPEVI ACDENPDATY DFKSDLWSLG ITAIEMAEGA PPLCDMHPMR
     ALFLIPRNPA PRLKSKKWSK KFQSFIESCL VKNHSQRPAT EQLMKHPFIR DQPNERQVRI
     QLKDHIDRTK KKRGEKDETE YEYSGSEEEE EENDSGEPSS ILNLPGESTL RRDFLRLQLA
     NKERSEALRR QQLEQQQREN EEHKRQLLAE RQKRIEEQKE QRRRLEEQQR REKELRKQQE
     REQRRHYEEQ MRREEERRRA EHEQEYKRKQ LEEQRQAERL QRQLKQERDY LVSLQHQRQE
     QRPLEKKPLY HYKEGMSPSE KPAWAKEVEE RSRLNRQSSP AMPHKVANRI SDPNLPPRSE
     SFSISGVQPA RTPPMLRPVD PQIPQLVAVK SQGPALTASQ SVHEQPTKGL SGFQEALNVT
     SHRVEMPRQN SDPTSENPPL PTRIEKFDRS SWLRQEEDIP PKVPQRTTSI SPALARKNSP
     GNGSALGPRL GSQPIRASNP DLRRTEPVLE SSLQRTSSGS SSSSSTPSSQ PSSQGGSQPG
     SQAGSSERSR VRANSKSEGS PVLPHEPSKV KPEESRDITR PSRPADLTAL AKELRELRIE
     ETNRPLKKVT DYSSSSEESE SSEEEEEDGE SETHDGTVAV SDIPRLIPTG APGNNEQYNM
     GMVGTHGLET SHADTFGGSI SREGTLMIRE TAEEKKRSGH SDSNGFAGHI NLPDLVQQSH
     SPAGTPTEGL GRVSTHSQEM DSGAEYGIGS STKASFTPFV DPRVYQTSPT DEDEEDDESS
     AAALFTSELL RQEQAKLNEA RKISVVNVNP TNIRPHSDTP EIRKYKKRFN SEILCAALWG
     VNLLVGTENG LMLLDRSGQG KVYNLINRRR FQQMDVLEGL NVLVTISGKK NKLRVYYLSW
     LRNRILHNDP EVEKKQGWIT VGDLEGCIHY KVVKYERIKF LVIALKNAVE IYAWAPKPYH
     KFMAFKSFAD LQHKPLLVDL TVEEGQRLKV IFGSHTGFHV IDVDSGNSYD IYIPSHIQGN
     ITPHAIVILP KTDGMEMLVC YEDEGVYVNT YGRITKDVVL QWGEMPTSVA YIHSNQIMGW
     GEKAIEIRSV ETGHLDGVFM HKRAQRLKFL CERNDKVFFA SVRSGGSSQV FFMTLNRNSM
     MNW
//
ID   WNK1_MOUSE              Reviewed;        2377 AA.
AC   P83741; A6H6V1; B2RRJ7; B7ZNJ4; Q3UZP3; Q6A083; Q6IFS6;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Serine/threonine-protein kinase WNK1;
DE            EC=2.7.11.1;
DE   AltName: Full=Protein kinase lysine-deficient 1;
DE   AltName: Full=Protein kinase with no lysine 1;
GN   Name=Wnk1; Synonyms=Hsn2, Prkwnk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   ALTERNATIVE SPLICING.
RC   STRAIN=C57BL/6;
RX   PubMed=14514722; DOI=10.1097/01.ASN.0000089830.97681.3B;
RA   O'Reilly M., Marshall E., Speirs H.J., Brown R.W.;
RT   "WNK1, a gene within a novel blood pressure control pathway, tissue-
RT   specifically generates radically different isoforms with and without a
RT   kinase domain.";
RL   J. Am. Soc. Nephrol. 14:2447-2456(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC   TISSUE=Embryonic tail;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), AND PARTIAL
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2/3).
RC   STRAIN=C57BL/6; TISSUE=Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-578.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   MEDLINE=21390047; PubMed=11498583; DOI=10.1126/science.1062844;
RA   Wilson F.H., Disse-Nicodeme S., Choate K.A., Ishikawa K.,
RA   Nelson-Williams C., Desitter I., Gunel M., Milford D.V., Lipkin G.W.,
RA   Achard J.-M., Feely M.P., Dussol B., Berland Y., Unwin R.J., Mayan H.,
RA   Simon D.B., Farfel Z., Jeunemaitre X., Lifton R.P.;
RT   "Human hypertension caused by mutations in WNK kinases.";
RL   Science 293:1107-1112(2001).
RN   [7]
RP   FUNCTION.
RX   MEDLINE=22557942; PubMed=12671053;
RA   Yang C.-L., Angell J., Mitchell R., Ellison D.H.;
RT   "WNK kinases regulate thiazide-sensitive Na-Cl cotransport.";
RL   J. Clin. Invest. 111:1039-1045(2003).
RN   [8]
RP   IDENTIFICATION OF THE HSN2 EXON.
RX   PubMed=15060842; DOI=10.1086/420795;
RA   Lafreniere R.G., MacDonald M.L.E., Dube M.-P., MacFarlane J.,
RA   O'Driscoll M., Brais B., Meilleur S., Brinkman R.R., Dadivas O.,
RA   Pape T., Platon C., Radomski C., Risler J., Thompson J.,
RA   Guerra-Escobio A.-M., Davar G., Breakefield X.O., Pimstone S.N.,
RA   Green R., Pryse-Phillips W., Goldberg Y.P., Younghusband H.B.,
RA   Hayden M.R., Sherrington R., Rouleau G.A., Samuels M.E.;
RT   "Identification of a novel gene (HSN2) causing hereditary sensory and
RT   autonomic neuropathy type II through the study of Canadian genetic
RT   isolates.";
RL   Am. J. Hum. Genet. 74:1064-1073(2004).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2027, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   ALTERNATIVE SPLICING (ISOFORMS 2 AND 3), AND TISSUE SPECIFICITY.
RX   PubMed=18521183; DOI=10.1172/JCI34088;
RA   Shekarabi M., Girard N., Riviere J.B., Dion P., Houle M., Toulouse A.,
RA   Lafreniere R.G., Vercauteren F., Hince P., Laganiere J., Rochefort D.,
RA   Faivre L., Samuels M., Rouleau G.A.;
RT   "Mutations in the nervous system--specific HSN2 exon of WNK1 cause
RT   hereditary sensory neuropathy type II.";
RL   J. Clin. Invest. 118:2496-2505(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Controls sodium and chloride ion transport by inhibiting
CC       the activity of WNK4, potentially by either phosphorylating the
CC       kinase or via an interaction between WNK4 and the autoinhibitory
CC       domain of WNK1. WNK4 regulates the activity of the thiazide-
CC       sensitive Na-Cl cotransporter, SLC12A3, by phosphorylation. WNK1
CC       may also play a role in actin cytoskeletal reorganization.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: By hypertonicity. Activation requires
CC       autophosphorylation of Ser-382. Phosphorylation of Ser-378 also
CC       promotes increased activity (By similarity).
CC   -!- SUBUNIT: Interacts with SYT2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=P83741-1; Sequence=Displayed;
CC       Name=2; Synonyms=Brain and spinal cord variant;
CC         IsoId=P83741-2; Sequence=VSP_040271;
CC         Note=This isoform which includes the HSN2 exon has been
CC         identified in human and mouse. The sequence shown here is the
CC         result of gene prediction;
CC       Name=3; Synonyms=Dorsal root ganglia and sciatic nerve variant,
CC       DRG and sciatic nerve variant;
CC         IsoId=P83741-3; Sequence=VSP_040272;
CC         Note=This isoform which includes the HSN2 exon has been
CC         identified in human and mouse. The sequence shown here is the
CC         result of gene prediction;
CC       Name=4;
CC         IsoId=P83741-4; Sequence=VSP_040273;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=P83741-5; Sequence=VSP_040274, VSP_040277;
CC         Note=No experimental confirmation available;
CC       Name=6;
CC         IsoId=P83741-6; Sequence=VSP_040275, VSP_040276;
CC         Note=May be due to intron retention. No experimental
CC         confirmation available;
CC   -!- TISSUE SPECIFICITY: Widely expressed in both adult and embryonic
CC       tissue, with highest levels observed in the testis and lower
CC       levels in heart, lung, kidney, placenta, brain and skeletal
CC       muscle. Two isoforms are expressed in heart, a single shorter
CC       isoform in the kidney. Locates to the distal convoluted tubule,
CC       the medullary collecting duct and the cortical collecting duct of
CC       the kidney. HSN2-containing isoform 2 and isoform 3 are restricted
CC       to the nervous system, expresse preferentially in sensory neurons
CC       than in motor neurons and in general more abundant in axons than
CC       in cell bodies (at protein level). In the DRG, predominantly
CC       expressed in the satellite cells that envelop sensory neurons, but
CC       low expression also observed in the cell bodies of neurons (at
CC       protein level). In the sciatic nerve, expressed in the Schwann
CC       cells that surround axons and in a mosaic distribution of axons
CC       (at protein level). In the spinal cord, expressed in superficial
CC       layers (LI and LII), as well as in the fibers of the Lissauer
CC       tract (at protein level). Also detected in the axon fibers of
CC       dorsolateral funiculus and lateral funiculus (at protein level).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. WNK subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- CAUTION: Cys-250 is present instead of the conserved Lys which is
CC       expected to be an active site residue. Lys-233 appears to fulfill
CC       the required catalytic function.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-214 is the
CC       initiator.
CC   -!- CAUTION: HSN2 was originally thought to be an intronless gene
CC       lying within a WNK1 gene intron. It has been shown to be a nervous
CC       system-specific exon of WNK1 included in isoform 2 and isoform 3
CC       (PubMed:18521183).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI46010.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
CC       Sequence=AAI46012.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
CC       Sequence=BAD32213.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC       Sequence=DAA04493.1; Type=Erroneous gene model prediction; Note=Includes 3' and 3' intronic sequences;
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DR   EMBL; AY309076; AAQ77243.1; -; mRNA.
DR   EMBL; AK172935; BAD32213.1; ALT_INIT; mRNA.
DR   EMBL; AC113092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC117667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC056761; AAH56761.1; -; mRNA.
DR   EMBL; BC138445; AAI38446.1; -; mRNA.
DR   EMBL; BC145282; AAI45283.1; -; mRNA.
DR   EMBL; BC146009; AAI46010.1; ALT_SEQ; mRNA.
DR   EMBL; BC146011; AAI46012.1; ALT_SEQ; mRNA.
DR   EMBL; BC171955; AAI71955.1; -; mRNA.
DR   EMBL; AK133738; BAE21813.1; -; mRNA.
DR   EMBL; BK004107; DAA04493.1; ALT_SEQ; Genomic_DNA.
DR   IPI; IPI00399953; -.
DR   IPI; IPI00621852; -.
DR   IPI; IPI00749624; -.
DR   IPI; IPI00972877; -.
DR   IPI; IPI00972891; -.
DR   IPI; IPI00972895; -.
DR   RefSeq; NP_001171949.1; NM_001185020.1.
DR   RefSeq; NP_001171950.1; NM_001185021.1.
DR   RefSeq; NP_001186012.1; NM_001199083.1.
DR   RefSeq; NP_001186013.1; NM_001199084.1.
DR   RefSeq; NP_941992.2; NM_198703.3.
DR   RefSeq; XP_003084694.1; XM_003084646.1.
DR   RefSeq; XP_003086576.1; XM_003086528.1.
DR   UniGene; Mm.333349; -.
DR   ProteinModelPortal; P83741; -.
DR   STRING; P83741; -.
DR   PhosphoSite; P83741; -.
DR   PRIDE; P83741; -.
DR   Ensembl; ENSMUST00000060043; ENSMUSP00000063001; ENSMUSG00000045962.
DR   GeneID; 100503989; -.
DR   GeneID; 232341; -.
DR   KEGG; mmu:100503989; -.
DR   KEGG; mmu:232341; -.
DR   UCSC; uc009dmt.1; mouse.
DR   CTD; 232341; -.
DR   MGI; MGI:2442092; Wnk1.
DR   eggNOG; roNOG13383; -.
DR   HOGENOM; HBG278749; -.
DR   HOVERGEN; HBG048577; -.
DR   InParanoid; P83741; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 381051; -.
DR   ArrayExpress; P83741; -.
DR   Bgee; P83741; -.
DR   CleanEx; MM_WNK1; -.
DR   Genevestigator; P83741; -.
DR   GermOnline; ENSMUSG00000045962; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005625; C:soluble fraction; IDA:MGI.
DR   GO; GO:0042598; C:vesicular fraction; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004860; F:protein kinase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IDA:UniProtKB.
DR   GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IMP:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Protein kinase inhibitor;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1   2377       Serine/threonine-protein kinase WNK1.
FT                                /FTId=PRO_0000086820.
FT   DOMAIN      221    479       Protein kinase.
FT   NP_BIND     227    235       ATP (By similarity).
FT   ACT_SITE    349    349       Proton acceptor (By similarity).
FT   BINDING     233    233       ATP (By similarity).
FT   MOD_RES     165    165       Phosphoserine.
FT   MOD_RES     172    172       Phosphoserine (By similarity).
FT   MOD_RES     378    378       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     382    382       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES    1256   1256       Phosphoserine (By similarity).
FT   MOD_RES    1292   1292       Phosphoserine (By similarity).
FT   MOD_RES    1295   1295       Phosphoserine (By similarity).
FT   MOD_RES    1973   1973       Phosphoserine (By similarity).
FT   MOD_RES    2006   2006       Phosphoserine (By similarity).
FT   MOD_RES    2007   2007       Phosphoserine (By similarity).
FT   MOD_RES    2022   2022       Phosphoserine (By similarity).
FT   MOD_RES    2024   2024       Phosphoserine (By similarity).
FT   MOD_RES    2027   2027       Phosphoserine.
FT   MOD_RES    2033   2033       Phosphoserine (By similarity).
FT   MOD_RES    2116   2116       Phosphoserine (By similarity).
FT   MOD_RES    2367   2367       Phosphoserine (By similarity).
FT   VAR_SEQ     715   1032       AQGQNQGQPSSSLAGVLSSQPIQHPQQQGIQPTVPSQQAVQ
FT                                YSLPQAASSSEGTTAQPVSQPQVSAGTQLPVSQTVATVQGE
FT                                PHIPVSTQPSVVPVHSGAHFLPMGQPIPTSLLPQYPVSQIP
FT                                ISTPHVSTAQTGFSSVPITMAAGINQPLLTLASSATASSIP
FT                                GGSPVVPNQLPTLLQPVNQLQSQVHPQLLQPTTVQSIGIPA
FT                                NLGQAAEGPLPSGDVLYQGFPSRLPPQYPGDSNIAPSSNVA
FT                                SVCIHSTVLAPPSMPTEALATQGYFPTVVQPYVESTPLVPM
FT                                GSVGGQVQVSQPAVSLTQQPPTTSSQQAVLE -> PRRGRS
FT                                MSVCVPHLSAVPSLSRISPSAPSTPPPVLSAPLCPSLLRTA
FT                                PEETFAEKLSKALESVLPMHSASQRKHRRSSLPSLFVTTPQ
FT                                SMAHPCGGTPTYPESQIFFPTIHERPVSFSPPPTCPPKVAI
FT                                SQRRKSTSFLEAQTRHFQPLLRTVGQNHLPPGSSPTNWTPE
FT                                AIVMLGATANRVNRELCEMQVQPVFEPTQIYSDYRPGLVLA
FT                                EEAHYFIPQETVYLAGVHYQAQVAGQYEGISYNSPVLSSPM
FT                                KQISEQKPVPGGPASSSVFEFPSGQAFLVGHLQNLRLDSGP
FT                                SPASPLSSISAPNSTDATHLKFHPVFVPHSAPAVLTNSNEN
FT                                RSNCVFEFHAQTPSSSGEGGGILPQRVYRNRQVAVDSNQEE
FT                                LSPQSVGLHCHLQPVTEEQRNNHAPELTISVVEPMGQIWPI
FT                                GSPEYSSDSSQITSSDLSDFQSPPPTGGTAAPFGSDVSLPF
FT                                IRLPQTVLQESPLFFCFPQGTTSQQVLSASYSSGGSTLHPQ
FT                                AQGQNQGQPSSSLAGVLSSQPIQHPQQQGIQPTVPSQQAVQ
FT                                YSLPQAASSSEGTTAQPVSQPQVSAGTQ (in isoform
FT                                2).
FT                                /FTId=VSP_040271.
FT   VAR_SEQ     715    936       AQGQNQGQPSSSLAGVLSSQPIQHPQQQGIQPTVPSQQAVQ
FT                                YSLPQAASSSEGTTAQPVSQPQVSAGTQLPVSQTVATVQGE
FT                                PHIPVSTQPSVVPVHSGAHFLPMGQPIPTSLLPQYPVSQIP
FT                                ISTPHVSTAQTGFSSVPITMAAGINQPLLTLASSATASSIP
FT                                GGSPVVPNQLPTLLQPVNQLQSQVHPQLLQPTTVQSIGIPA
FT                                NLGQAAEGPLPSGDVLY -> PQSMAHPCGGTPTYPESQIF
FT                                FPTIHERPVSFSPPPTCPPKVAISQRRKSTSFLEAQTRHFQ
FT                                PLLRTVGQNHLPPGSSPTNWTPEAIVMLGATANRVNRELCE
FT                                MQVQPVFEPTQIYSDYRPGLVLAEEAHYFIPQETVYLAGVH
FT                                YQAQVAGQYEGISYNSPVLSSPMKQISEQKPVPGGPASSSV
FT                                FEFPSGQAFLVGHLQNLRLDSGPSPASPLSSISAPNSTDAT
FT                                HLKFHPVFVPHSAPAVLTNSNENRSNCVFEFHAQTPSSSGE
FT                                GGGILPQRVYRNRQVAVDSNQEELSPQSVGLHCHLQPVTEE
FT                                QRNNHAPELTISVVEPMGQIWPIGSPEYSSDSSQITSSDLS
FT                                DFQSPPPTGGTAAPFGSDVSLPFIRLPQTVLQESPLFFCFP
FT                                QGTTSQQVLSASYSSGGSTLHPQAQGQNQGQPSSSLAGVLS
FT                                SQPIQHPQQQGIQPTVPSQQAVQYSLPQAASSSEGTTAQPV
FT                                SQPQVSAGT (in isoform 3).
FT                                /FTId=VSP_040272.
FT   VAR_SEQ     784   1032       Missing (in isoform 4).
FT                                /FTId=VSP_040273.
FT   VAR_SEQ     784    937       Missing (in isoform 5).
FT                                /FTId=VSP_040274.
FT   VAR_SEQ     784    788       LPVSQ -> VNSNF (in isoform 6).
FT                                /FTId=VSP_040275.
FT   VAR_SEQ     789   2377       Missing (in isoform 6).
FT                                /FTId=VSP_040276.
FT   VAR_SEQ    1787   1814       Missing (in isoform 5).
FT                                /FTId=VSP_040277.
FT   CONFLICT   1220   1220       G -> R (in Ref. 1; AAQ77243).
FT   CONFLICT   1230   1230       S -> C (in Ref. 1; AAQ77243).
SQ   SEQUENCE   2377 AA;  250934 MW;  0C4D288CCE50B8C6 CRC64;
     MSDGAAEKQS GTPGFLTPPA PVPKNGSSSD SSVGEKLGAT VADSGVGRTE EYRRRRHTMD
     KDSRGAAATT TPTEHRFFRR SVICDSNATA LELPGLPLSI PQPSVPAVVP QSAPPEPHRE
     ETLTATVASQ VSQQPSAAAS PGEQAVVGSA TTTVPSSTSK DRPVSQPSLV GSKEEPPPSR
     SGSGSGGASA KEAQEDRSQQ QDDIEELETK AVGMSNDGRF LKFDIEIGRG SFKTVYKGLD
     TETTVEVAWC ELQDRKLTKS ERQRFKEEAE MLKGLQHPNI VRFYDSWEST VKGKKCIVLV
     TELMTSGTLK TYLKRFKVMK IKVLRSWCRQ ILKGLQFLHT RTPPIIHRDL KCDNIFITGP
     TGSVKIGDLG LATLKRASFA KSVIGTPEFM APEMYEEKYD ESVDVYAFGM CMLEMATSEY
     PYSECQNAAQ IYRRVTSGVK PASFDKVAIP EVKEIIEGCI RQNKDERYSI KDLLNHAFFQ
     EETGVRVELA EEDDGEKIAI KLWLRIEDIK KLKGKYKDNE AIEFSFDLER DVPEDVAQEM
     VESGYVCEGD HKTMAKAIKD RVSLIKRKRE QRQLVREEQE KRKQEESSFK QQNEQQASVS
     QAGIQQLSAA STGIPTAPAT SASVSTQVEP EEPEADQHQQ LQYQQPSISV LSDGTIDSGQ
     GSSVFTESRV SSQQTVSYGS QHEQAHSTGT APGHTVSSIQ AQSQPHGVYP PSSMAQGQNQ
     GQPSSSLAGV LSSQPIQHPQ QQGIQPTVPS QQAVQYSLPQ AASSSEGTTA QPVSQPQVSA
     GTQLPVSQTV ATVQGEPHIP VSTQPSVVPV HSGAHFLPMG QPIPTSLLPQ YPVSQIPIST
     PHVSTAQTGF SSVPITMAAG INQPLLTLAS SATASSIPGG SPVVPNQLPT LLQPVNQLQS
     QVHPQLLQPT TVQSIGIPAN LGQAAEGPLP SGDVLYQGFP SRLPPQYPGD SNIAPSSNVA
     SVCIHSTVLA PPSMPTEALA TQGYFPTVVQ PYVESTPLVP MGSVGGQVQV SQPAVSLTQQ
     PPTTSSQQAV LESTQGVSQA APPEQTPITQ SQPTQPVPLV TSADSAHSDV ASGMSDGNEN
     APSSSGRHEG RTTKRHYRKS VRSRSRHEKT SRPKLRILNV SNKGDRVVEC QLETHNRKMV
     TFKFDLDGDN PEEIATIMVN NDFILAIERE SFVAQVREII EKADEMLSED VSVEPEGDQG
     LESLQGKDDY GFPGSQKLEG EFKQPIAVSS MPQQIGVPTS SLTQVVHSAG RRFIVSPVPE
     SRLRESKVFT SDISDPVVAS TSQAPGMNLS HSASSLSLQQ AFSELKHGQM TEGPNTAPPN
     FNHMAGPTFS PFLASIAGVQ TVAASTPSVS VPITSSPLND ISTSVMQSET ALPTEKGIVG
     VTTTSTGVVA SGGLTTMSVS ESPTSSSAVS SSTVPAVVTV STPSQPVQAS TSGSIASSTG
     SFPPGTFSTT TATTMGSVVA PDAKPPTVLL QQVASNTAGV AIVTSVSTTT PFPGMASQPS
     LPLSSSTSAP TLAETMVVSA HSLDKASHSS TAGLGLSFCA PSSSSSSGTA VSTSVSQPGM
     VHPLVISSAV VSTPGLPQPV VPTSTPLLPQ VPNIPPLVQP VVNVPAVQQT LIHSQPQPAL
     LPNQPHTHCP EMDADTQSKA PGIDDIKTLE EKLRSLFSEH SSSGTQHASV SLETPLVVET
     TVTPGITTTA VAPSKLMTST TSTCLPPTSL PLGAAGMPVM PVGTPGQVST PGTHASAPVG
     TATGVKPGTT PPKPTKTVVP PVGTELSAGT VPCEQLPPFP GPSLIQSQQP LEDLDAQLRR
     TLSPETITVA PAVGPLSTMS STTVTEAGTR LQKDGTEGHV TATSSGAGVV KMGRFQVSVT
     MDDAQKERKN RSEDTKSVHF ESSTSESSVL SSSSPESTLV KPEPNGISIS GISLDVPDST
     HKAPTPEAKS DAGQPTKVGR FQVTTTANKV GRFSVSRTED KVTELKKEGP VTSPPFRDSE
     QTVIPAVIPK KEKPELAEPS HLNGPSSDLE AAFLSRGTED GSGSPHSPPH LCSKSLPVQN
     LSQSLSNSFN SSYMSSDNES DIEDEDLRLE LRRLREKHLK EIQDLQSRQK HEIESLYTKL
     GKVPPAVIIP PAAPLSGRRR RPTKSKGSKS SRSSSLGNKS PQLSGNLSGQ SGTSVLHPQQ
     TLHPAGNTPE TGHNQLLQPL KPSPSSDNLY SAFTSDGAIS VPSLSAPGQG TSSTNTVGGT
     VSSQAAQAQP PAMTSSRKGT FTDDLHKLVD NWARDAMNLS GRRGSKGHMN YEGPGMARKF
     SAPGQLCVPM TSNLGGSTPI SAASATSLGH FTKSMCPPQQ YGFPPAPFGT QWSGTGGPAP
     QPLGQFQPVG TASLQNFNIS NLQKSISNPP GSNLRTT
//
ID   TBG1_MOUSE              Reviewed;         451 AA.
AC   P83887; Q9Z310;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Tubulin gamma-1 chain;
DE   AltName: Full=Gamma-1-tubulin;
DE   AltName: Full=Gamma-tubulin complex component 1;
DE            Short=GCP-1;
GN   Name=Tubg1; Synonyms=Tubg;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 49-84; 195-217 AND 416-425, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [3]
RP   INTERACTION WITH B9D2.
RX   PubMed=18287022; DOI=10.1073/pnas.0712385105;
RA   Town T., Breunig J.J., Sarkisian M.R., Spilianakis C., Ayoub A.E.,
RA   Liu X., Ferrandino A.F., Gallagher A.R., Li M.O., Rakic P.,
RA   Flavell R.A.;
RT   "The stumpy gene is required for mammalian ciliogenesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2853-2858(2008).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. Gamma
CC       tubulin is found at microtubule organizing centers (MTOC) such as
CC       the spindle poles or the centrosome, suggesting that it is
CC       involved in the minus-end nucleation of microtubule assembly (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with GCP2 and GCP3 (By similarity). Interacts
CC       with B9D2. Interacts with CDK5RAP2; the interaction is leading to
CC       centrosomal localization of TUBG1 and CDK5RAP2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the tubulin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC006581; AAH06581.1; -; mRNA.
DR   IPI; IPI00131309; -.
DR   RefSeq; NP_598785.1; NM_134024.2.
DR   UniGene; Mm.479145; -.
DR   ProteinModelPortal; P83887; -.
DR   SMR; P83887; 2-446.
DR   STRING; P83887; -.
DR   PhosphoSite; P83887; -.
DR   PRIDE; P83887; -.
DR   Ensembl; ENSMUST00000043680; ENSMUSP00000048036; ENSMUSG00000035198.
DR   GeneID; 103733; -.
DR   KEGG; mmu:103733; -.
DR   UCSC; uc007lnk.1; mouse.
DR   CTD; 103733; -.
DR   MGI; MGI:101834; Tubg1.
DR   eggNOG; roNOG09862; -.
DR   HOGENOM; HBG750007; -.
DR   HOVERGEN; HBG098558; -.
DR   InParanoid; P83887; -.
DR   OMA; KIQEDIF; -.
DR   OrthoDB; EOG444KK7; -.
DR   PhylomeDB; P83887; -.
DR   NextBio; 356087; -.
DR   ArrayExpress; P83887; -.
DR   Bgee; P83887; -.
DR   CleanEx; MM_TUBG1; -.
DR   Genevestigator; P83887; -.
DR   GermOnline; ENSMUSG00000035198; Mus musculus.
DR   GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR   GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR   GO; GO:0005814; C:centriole; IDA:MGI.
DR   GO; GO:0000794; C:condensed nuclear chromosome; IDA:UniProtKB.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IDA:MGI.
DR   GO; GO:0000242; C:pericentriolar material; IDA:MGI.
DR   GO; GO:0005827; C:polar microtubule; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:UniProtKB.
DR   GO; GO:0000212; P:meiotic spindle organization; IEP:UniProtKB.
DR   GO; GO:0007020; P:microtubule nucleation; TAS:UniProtKB.
DR   GO; GO:0007052; P:mitotic spindle organization; TAS:UniProtKB.
DR   GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR   GO; GO:0007088; P:regulation of mitosis; TAS:UniProtKB.
DR   InterPro; IPR002454; Gamma_tubulin.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR023123; Tubulin_C.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   Gene3D; G3DSA:3.30.1330.20; Tubulin/FtsZ_2-layer-sand-dom; 1.
DR   Gene3D; G3DSA:1.10.287.600; Tubulin_C; 1.
DR   Gene3D; G3DSA:3.40.50.1440; Tubulin_FtsZ; 1.
DR   PANTHER; PTHR11588; Tubulin; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01164; GAMMATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF55307; Tub_FtsZ_C; 1.
DR   SUPFAM; SSF52490; Tubulin_FtsZ; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding;
KW   Microtubule; Nucleotide-binding.
FT   CHAIN         1    451       Tubulin gamma-1 chain.
FT                                /FTId=PRO_0000048466.
FT   NP_BIND     142    148       GTP (Potential).
SQ   SEQUENCE   451 AA;  51101 MW;  A8F1068D12D0C88A CRC64;
     MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY
     IPRAVLLDLE PRVIHSILNS SYAKLYNPEN IYLSEHGGGA GNNWASGFSQ GEKIHEDIFD
     IIDREADGSD SLEGFVLCHS IAGGTGSGLG SYLLERLNDR YPKKLVQTYS VFPNQDEMSD
     VVVQPYNSLL TLKRLTQNAD CVVVLDNTAL NLIATDRLHI QNPSFSQINQ LVSTIMSAST
     TTLRYPGYMN NDLIGLIASL IPTPRLHFLM TGYTPLTTDQ SVASVRKTTV LDVMRRLLQP
     KNVMVSTGRD RQTNHCYIAI LNIIQGEVDP TQVHKSLQRI RERKLANFIP WGPASIQVAL
     SRKSPYLPSA HRVSGLMMAN HTSISSLFER TCRQFDKLRK REAFMEQFRK EDIFKDNFDE
     MDTSREIVQQ LIDEYHAATR PDYISWGTQE Q
//
ID   HPCA_MOUSE              Reviewed;         193 AA.
AC   P84075; A2A7R4; P32076; P41211; P70510;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Neuron-specific calcium-binding protein hippocalcin;
GN   Name=Hpca;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   MEDLINE=99132657; PubMed=9931466; DOI=10.1016/S0378-1119(98)00526-5;
RA   Masaki T., Sakai E., Furuta Y., Kobayashi M., Takamatsu K.;
RT   "Genomic structure and chromosomal mapping of the human and mouse
RT   hippocalcin genes.";
RL   Gene 225:117-124(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J, and DBA/2J; TISSUE=Brain;
RX   MEDLINE=21975488; PubMed=11978849;
RA   Fehr C., Shirley R.L., Belknap J.K., Crabbe J.C., Buck K.J.;
RT   "Congenic mapping of alcohol and pentobarbital withdrawal liability
RT   loci to a <1 centimorgan interval of murine chromosome 4:
RT   identification of Mpdz as a candidate gene.";
RL   J. Neurosci. 22:3730-3738(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in the calcium-dependent regulation of
CC       rhodopsin phosphorylation. Binds two calcium ions.
CC   -!- INTERACTION:
CC       Q08460:Kcnma1; NbExp=1; IntAct=EBI-2128343, EBI-1633915;
CC   -!- PTM: Myristoylation facilitates interaction with membranes (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the recoverin family.
CC   -!- SIMILARITY: Contains 4 EF-hand domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB015200; BAA74455.1; -; Genomic_DNA.
DR   EMBL; AF326551; AAL37397.1; -; mRNA.
DR   EMBL; AF326552; AAL37398.1; -; mRNA.
DR   EMBL; AK002992; BAB22502.1; -; mRNA.
DR   EMBL; AL606977; CAM19712.1; -; Genomic_DNA.
DR   EMBL; BC049607; AAH49607.1; -; mRNA.
DR   EMBL; BC058588; AAH58588.1; -; mRNA.
DR   IPI; IPI00230310; -.
DR   RefSeq; NP_001123891.1; NM_001130419.1.
DR   RefSeq; NP_034601.1; NM_010471.3.
DR   UniGene; Mm.443017; -.
DR   ProteinModelPortal; P84075; -.
DR   SMR; P84075; 5-185.
DR   IntAct; P84075; 3.
DR   STRING; P84075; -.
DR   PhosphoSite; P84075; -.
DR   PRIDE; P84075; -.
DR   Ensembl; ENSMUST00000030572; ENSMUSP00000030572; ENSMUSG00000028785.
DR   Ensembl; ENSMUST00000095807; ENSMUSP00000093486; ENSMUSG00000028785.
DR   Ensembl; ENSMUST00000116442; ENSMUSP00000112143; ENSMUSG00000028785.
DR   Ensembl; ENSMUST00000116444; ENSMUSP00000112145; ENSMUSG00000028785.
DR   GeneID; 15444; -.
DR   KEGG; mmu:15444; -.
DR   UCSC; uc008uwb.1; mouse.
DR   CTD; 15444; -.
DR   MGI; MGI:1336200; Hpca.
DR   GeneTree; ENSGT00560000076803; -.
DR   HOGENOM; HBG746798; -.
DR   HOVERGEN; HBG108179; -.
DR   InParanoid; P84075; -.
DR   OMA; KEDESTP; -.
DR   OrthoDB; EOG4G1MHC; -.
DR   PhylomeDB; P84075; -.
DR   NextBio; 288236; -.
DR   ArrayExpress; P84075; -.
DR   Bgee; P84075; -.
DR   CleanEx; MM_HPCA; -.
DR   Genevestigator; P84075; -.
DR   GermOnline; ENSMUSG00000028785; Mus musculus.
DR   GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   InterPro; IPR018248; EF-hand.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR001125; Recoverin.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF00036; efhand; 3.
DR   PRINTS; PR00450; RECOVERIN.
DR   SMART; SM00054; EFh; 3.
DR   PROSITE; PS00018; EF_HAND_1; 3.
DR   PROSITE; PS50222; EF_HAND_2; 3.
PE   1: Evidence at protein level;
KW   Calcium; Lipoprotein; Myristate; Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    193       Neuron-specific calcium-binding protein
FT                                hippocalcin.
FT                                /FTId=PRO_0000073769.
FT   DOMAIN       24     59       EF-hand 1.
FT   DOMAIN       60     95       EF-hand 2.
FT   DOMAIN       96    131       EF-hand 3.
FT   DOMAIN      144    179       EF-hand 4.
FT   CA_BIND      73     84       1 (Potential).
FT   CA_BIND     109    120       2 (Potential).
FT   CA_BIND     157    168       3 (Potential).
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
SQ   SEQUENCE   193 AA;  22427 MW;  3DBEA176AC945DB1 CRC64;
     MGKQNSKLRP EMLQDLRENT EFSELELQEW YKGFLKDCPT GILNVDEFKK IYANFFPYGD
     ASKFAEHVFR TFDTNSDGTI DFREFIIALS VTSRGRLEQK LMWAFSMYDL DGNGYISREE
     MLEIVQAIYK MVSSVMKMPE DESTPEKRTE KIFRQMDTNN DGKLSLEEFI RGAKSDPSIV
     RLLQCDPSSA SQF
//
ID   CPLX2_MOUSE             Reviewed;         134 AA.
AC   P84086; O09056; Q13329; Q28184; Q32KK4; Q64386;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=Complexin-2;
DE   AltName: Full=921-L;
DE   AltName: Full=Complexin II;
DE            Short=CPX II;
DE   AltName: Full=Synaphin-1;
GN   Name=Cplx2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/Sv; TISSUE=Brain;
RX   MEDLINE=96006530; PubMed=7553862; DOI=10.1016/0092-8674(95)90239-2;
RA   McMahon H.T., Missler M., Li C., Suedhof T.C.;
RT   "Complexins: cytosolic proteins that regulate SNAP receptor
RT   function.";
RL   Cell 83:111-119(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=95361923; PubMed=7635198; DOI=10.1016/0014-5793(95)00713-J;
RA   Takahashi S., Yamamoto H., Matsuda Z., Ogawa M., Yagyu K.,
RA   Taniguchi T., Miyata T., Kaba H., Higuchi T., Okutani F., Fujimoto S.;
RT   "Identification of two highly homologous presynaptic proteins
RT   distinctly localized at the dendritic and somatic synapses.";
RL   FEBS Lett. 368:455-460(1995).
RN   [3]
RP   IDENTIFICATION.
RC   TISSUE=Brain;
RX   PubMed=16162394; DOI=10.1016/j.gene.2005.07.005;
RA   Raevskaya N.M., Dergunova L.V., Vladychenskaya I.P., Stavchansky V.V.,
RA   Oborina M.V., Poltaraus A.B., Limborska S.A.;
RT   "Structural organization of the human complexin 2 gene (CPLX2) and
RT   aspects of its functional activity.";
RL   Gene 359:127-137(2005).
RN   [4]
RP   FUNCTION.
RX   PubMed=11163241; DOI=10.1016/S0092-8674(01)00192-1;
RA   Reim K., Mansour M., Varoqueaux F., McMahon H.T., Suedhof T.C.,
RA   Brose N., Rosenmund C.;
RT   "Complexins regulate a late step in Ca2+-dependent neurotransmitter
RT   release.";
RL   Cell 104:71-81(2001).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12915444; DOI=10.1093/hmg/ddg249;
RA   Glynn D., Bortnick R.A., Morton A.J.;
RT   "Complexin II is essential for normal neurological function in mice.";
RL   Hum. Mol. Genet. 12:2431-2448(2003).
RN   [6]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15911881; DOI=10.1083/jcb.200502115;
RA   Reim K., Wegmeyer H., Brandstaetter J.H., Xue M., Rosenmund C.,
RA   Dresbach T., Hofmann K., Brose N.;
RT   "Structurally and functionally unique complexins at retinal ribbon
RT   synapses.";
RL   J. Cell Biol. 169:669-680(2005).
CC   -!- FUNCTION: Positively regulates a late step in synaptic vesicle
CC       exocytosis. Also involved in mast cell exocytosis. Although not
CC       essential for development, seems critical for the acquisition of
CC       higher cognitive functions in the adult brain.
CC   -!- SUBUNIT: Binds to the SNARE core complex containing SNAP25, VAMP2
CC       and STX1A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Note=Enriched at
CC       synaptic-releasing sites in mature neurons.
CC   -!- TISSUE SPECIFICITY: Nervous system. Expressed predominantly in
CC       brain, where it is present in many regions, including hippocampus
CC       and cerebellum. In the retina, present at conventional amacrine
CC       cell synapses (at protein level).
CC   -!- DEVELOPMENTAL STAGE: In the brain, expression starts at P6 and
CC       increases to reach a plateau at P20.
CC   -!- DISRUPTION PHENOTYPE: Mice show no obvious phenotypic changes and
CC       no significant motor deficiencies. However, they show
CC       abnormalities in a number of complex behaviors including
CC       exploration, socialization, motor coordination, learning and
CC       reversal learning.
CC   -!- SIMILARITY: Belongs to the complexin/synaphin family.
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DR   EMBL; U35101; AAC52272.1; -; Genomic_DNA.
DR   EMBL; D38613; BAA07604.1; -; mRNA.
DR   EMBL; BN000501; CAG26661.1; -; mRNA.
DR   EMBL; BN000502; CAG26662.1; -; mRNA.
DR   IPI; IPI00111501; -.
DR   PIR; S66293; D57233.
DR   RefSeq; NP_034076.1; NM_009946.2.
DR   UniGene; Mm.268902; -.
DR   ProteinModelPortal; P84086; -.
DR   SMR; P84086; 32-72.
DR   PhosphoSite; P84086; -.
DR   PRIDE; P84086; -.
DR   Ensembl; ENSMUST00000026985; ENSMUSP00000026985; ENSMUSG00000025867.
DR   GeneID; 12890; -.
DR   KEGG; mmu:12890; -.
DR   UCSC; uc007qoc.1; mouse.
DR   CTD; 12890; -.
DR   MGI; MGI:104726; Cplx2.
DR   eggNOG; maNOG20874; -.
DR   GeneTree; ENSGT00490000043416; -.
DR   HOGENOM; HBG444230; -.
DR   HOVERGEN; HBG062792; -.
DR   InParanoid; P84086; -.
DR   OMA; KERYKEN; -.
DR   OrthoDB; EOG44MXTP; -.
DR   NextBio; 282490; -.
DR   ArrayExpress; P84086; -.
DR   Bgee; P84086; -.
DR   CleanEx; MM_CPLX2; -.
DR   Genevestigator; P84086; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
DR   InterPro; IPR008849; Synaphin.
DR   PANTHER; PTHR16705; Synaphin; 1.
DR   Pfam; PF05835; Synaphin; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Cytoplasm; Exocytosis;
KW   Mast cell degranulation; Neurotransmitter transport; Phosphoprotein;
KW   Transport.
FT   CHAIN         1    134       Complexin-2.
FT                                /FTId=PRO_0000144876.
FT   REGION       41     97       Interaction with the SNARE complex (By
FT                                similarity).
FT   COILED       28     84       Potential.
FT   MOD_RES      14     14       N6-acetyllysine (By similarity).
FT   MOD_RES      93     93       Phosphoserine (By similarity).
SQ   SEQUENCE   134 AA;  15394 MW;  7791812FD4194AC5 CRC64;
     MDFVMKQALG GATKDMGKML GGEEEKDPDA QKKEEERQEA LRQQEEERKA KHARMEAERE
     KVRQQIRDKY GLKKKEEKEA EEKAALEQPC EGSLTRPKKA IPAGCGDEEE EEEESILDTV
     LKYLPGPLQD MFKK
//
ID   AP2M1_MOUSE             Reviewed;         435 AA.
AC   P84091; P20172; P53679;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=AP-2 complex subunit mu;
DE   AltName: Full=AP-2 mu chain;
DE   AltName: Full=Adapter-related protein complex 2 mu subunit;
DE   AltName: Full=Adaptor protein complex AP-2 subunit mu;
DE   AltName: Full=Clathrin assembly protein complex 2 medium chain;
DE   AltName: Full=Clathrin coat assembly protein AP50;
DE   AltName: Full=Clathrin coat-associated protein AP50;
DE   AltName: Full=Mu2-adaptin;
DE   AltName: Full=Plasma membrane adaptor AP-2 50 kDa protein;
GN   Name=Ap2m1; Synonyms=Clapm1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Spleen;
RX   MEDLINE=96032789; PubMed=7569928; DOI=10.1126/science.7569928;
RA   Ohno H., Stewart J., Fournier M.C., Bosshart H., Rhee I.R.,
RA   Miyatake S., Saito T., Gallusser A., Kirchhausen T., Bonifacino J.S.;
RT   "Interaction of tyrosine-based sorting signals with clathrin-
RT   associated proteins.";
RL   Science 269:1872-1875(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129;
RX   MEDLINE=98248900; PubMed=9573360; DOI=10.1016/S0378-1119(97)00649-5;
RA   Ohno H., Poy G., Bonifacino J.S.;
RT   "Cloning of the gene encoding the murine clathrin-associated adaptor
RT   medium chain mu 2: gene organization, alternative splicing and
RT   chromosomal assignment.";
RL   Gene 210:187-193(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 61-70; 131-139 AND 282-288, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX   PubMed=14745134; DOI=10.1247/csf.28.419;
RA   Nakatsu F., Ohno H.;
RT   "Adaptor protein complexes as the key regulators of protein sorting in
RT   the post-Golgi network.";
RL   Cell Struct. Funct. 28:419-429(2003).
RN   [6]
RP   FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX   PubMed=15473838; DOI=10.1146/annurev.cellbio.20.010403.104543;
RA   Owen D.J., Collins B.M., Evans P.R.;
RT   "Adaptors for clathrin coats: structure and function.";
RL   Annu. Rev. Cell Dev. Biol. 20:153-191(2004).
RN   [7]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=16227583; DOI=10.1128/MCB.25.21.9318-9323.2005;
RA   Mitsunari T., Nakatsu F., Shioda N., Love P.E., Grinberg A.,
RA   Bonifacino J.S., Ohno H.;
RT   "Clathrin adaptor AP-2 is essential for early embryonal development.";
RL   Mol. Cell. Biol. 25:9318-9323(2005).
RN   [8]
RP   INTERACTION WITH PIP5K1C.
RX   PubMed=16707488; DOI=10.1074/jbc.M601465200;
RA   Bairstow S.F., Ling K., Su X., Firestone A.J., Carbonara C.,
RA   Anderson R.A.;
RT   "Type Igamma661 phosphatidylinositol phosphate kinase directly
RT   interacts with AP2 and regulates endocytosis.";
RL   J. Biol. Chem. 281:20632-20642(2006).
CC   -!- FUNCTION: Component of the adaptor protein complex 2 (AP-2).
CC       Adaptor protein complexes function in protein transport via
CC       transport vesicles in different membrane traffic pathways. Adaptor
CC       protein complexes are vesicle coat components and appear to be
CC       involved in cargo selection and vesicle formation. AP-2 is
CC       involved in clathrin-dependent endocytosis in which cargo proteins
CC       are incorporated into vesicles surrrounded by clathrin (clathrin-
CC       coated vesicles, CCVs) which are destined for fusion with the
CC       early endosome. The clathrin lattice serves as a mechanical
CC       scaffold but is itself unable to bind directly to membrane
CC       components. Clathrin-associated adaptor protein (AP) complexes
CC       which can bind directly to both the clathrin lattice and to the
CC       lipid and protein components of membranes are considered to be the
CC       major clathrin adaptors contributing the CCV formation. AP-2 also
CC       serves as a cargo receptor to selectively sort the membrane
CC       proteins involved in receptor-mediated endocytosis. AP-2 seems to
CC       play a role in the recycling of synaptic vesicle membranes from
CC       the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi)
CC       and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the
CC       cytosolic tails of transmembrane cargo molecules. AP-2 may also
CC       play a role in maintaining normal post-endocytic trafficking
CC       through the ARF6-regulated, non-clathrin pathway. The AP-2 mu
CC       subunit binds to transmembrane cargo proteins; it recognizes the
CC       Y-X-X-Phi motifs. The surface region interacting with to the Y-X-
CC       X-Phi motif is inaccessible in cytosolic AP-2, but becomes
CC       accessible through a conformational change following
CC       phosphorylation of AP-2 mu subunit at 'Tyr-156' in membrane-
CC       associated AP-2. The membrane-specific phosphorylation event
CC       appears to involve assembled clathrin which activates the AP-2 mu
CC       kinase AAK1 (By similarity).
CC   -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is an heterotetramer
CC       composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2
CC       and beta-type subunit AP2B1), a medium adaptin (mu-type subunit
CC       AP2M1) and a small adaptin (sigma-type subunit AP2S1). Interacts
CC       with ATP6V1H and MEGF10. Interacts with EGFR. Interacts with F2R.
CC       Interacts with KIAA0319; required for clathrin-mediated
CC       endocytosis of KIAA0319 (By similarity). Interacts with PIP5K1C
CC       isoform 1; tyrosine phosphorylation of PIP5K1C weakens the
CC       interaction. Does not interact with PIP5K1C isoform 3.
CC   -!- SUBCELLULAR LOCATION: Cell membrane. Membrane, coated pit;
CC       Peripheral membrane protein; Cytoplasmic side. Note=AP-2 appears
CC       to be excluded from internalizing CCVs and to disengage from sites
CC       of endocytosis seconds before internalization of the nascent CCV
CC       (By similarity).
CC   -!- TISSUE SPECIFICITY: Detected in spleen.
CC   -!- PTM: Phosphorylated (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Embryonic lethal before day 3.5 postcoitus
CC       (E3.5).
CC   -!- SIMILARITY: Belongs to the adaptor complexes medium subunit
CC       family.
CC   -!- SIMILARITY: Contains 1 MHD (mu homology) domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; U27106; AAC53158.1; -; mRNA.
DR   EMBL; AF001923; AAC53583.1; -; Genomic_DNA.
DR   EMBL; AF001913; AAC53583.1; JOINED; Genomic_DNA.
DR   EMBL; AF001914; AAC53583.1; JOINED; Genomic_DNA.
DR   EMBL; AF001915; AAC53583.1; JOINED; Genomic_DNA.
DR   EMBL; AF001916; AAC53583.1; JOINED; Genomic_DNA.
DR   EMBL; AF001917; AAC53583.1; JOINED; Genomic_DNA.
DR   EMBL; AF001918; AAC53583.1; JOINED; Genomic_DNA.
DR   EMBL; AF001919; AAC53583.1; JOINED; Genomic_DNA.
DR   EMBL; AF001920; AAC53583.1; JOINED; Genomic_DNA.
DR   EMBL; AF001921; AAC53583.1; JOINED; Genomic_DNA.
DR   EMBL; AF001922; AAC53583.1; JOINED; Genomic_DNA.
DR   EMBL; BC056352; AAH56352.1; -; mRNA.
DR   IPI; IPI00116356; -.
DR   PIR; I49327; I49327.
DR   PIR; JC6563; JC6563.
DR   RefSeq; NP_033809.1; NM_009679.2.
DR   UniGene; Mm.18946; -.
DR   ProteinModelPortal; P84091; -.
DR   SMR; P84091; 1-435.
DR   IntAct; P84091; 3.
DR   MINT; MINT-216926; -.
DR   STRING; P84091; -.
DR   PhosphoSite; P84091; -.
DR   PRIDE; P84091; -.
DR   Ensembl; ENSMUST00000007216; ENSMUSP00000007216; ENSMUSG00000022841.
DR   GeneID; 11773; -.
DR   KEGG; mmu:11773; -.
DR   UCSC; uc007ypy.1; mouse.
DR   CTD; 11773; -.
DR   MGI; MGI:1298405; Ap2m1.
DR   eggNOG; roNOG07529; -.
DR   HOGENOM; HBG525531; -.
DR   HOVERGEN; HBG050516; -.
DR   InParanoid; P84091; -.
DR   OMA; KNEAFVD; -.
DR   PhylomeDB; P84091; -.
DR   NextBio; 279559; -.
DR   ArrayExpress; P84091; -.
DR   Bgee; P84091; -.
DR   CleanEx; MM_AP2M1; -.
DR   Genevestigator; P84091; -.
DR   GermOnline; ENSMUSG00000022841; Mus musculus.
DR   GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR   GO; GO:0030132; C:clathrin coat of coated pit; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0030141; C:stored secretory granule; TAS:MGI.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR   GO; GO:0016192; P:vesicle-mediated transport; TAS:MGI.
DR   InterPro; IPR022775; AP_mu_sigma_su.
DR   InterPro; IPR015629; Clathrin_AP50.
DR   InterPro; IPR001392; Clathrin_mu.
DR   InterPro; IPR008968; Clathrin_mu_C.
DR   InterPro; IPR018240; Clathrin_mu_CS.
DR   InterPro; IPR011012; Longin-like.
DR   PANTHER; PTHR11998:SF12; Clathrin_coat_assem_AP50; 1.
DR   Pfam; PF00928; Adap_comp_sub; 1.
DR   Pfam; PF01217; Clat_adaptor_s; 1.
DR   PIRSF; PIRSF005992; Clathrin_mu; 1.
DR   PRINTS; PR00314; CLATHRINADPT.
DR   SUPFAM; SSF49447; AP50; 1.
DR   SUPFAM; SSF64356; Longin_like; 1.
DR   PROSITE; PS00990; CLAT_ADAPTOR_M_1; 1.
DR   PROSITE; PS00991; CLAT_ADAPTOR_M_2; 1.
DR   PROSITE; PS51072; MHD; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Coated pit; Direct protein sequencing; Lipid-binding;
KW   Membrane; Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1    435       AP-2 complex subunit mu.
FT                                /FTId=PRO_0000193775.
FT   DOMAIN      167    435       MHD.
FT   BINDING     341    341       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   BINDING     343    343       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   BINDING     345    345       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   BINDING     354    354       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   BINDING     356    356       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   MOD_RES      45     45       Phosphoserine (By similarity).
FT   MOD_RES     156    156       Phosphothreonine (By similarity).
SQ   SEQUENCE   435 AA;  49655 MW;  82803219BA279954 CRC64;
     MIGGLFIYNH KGEVLISRVY RDDIGRNAVD AFRVNVIHAR QQVRSPVTNI ARTSFFHVKR
     SNIWLAAVTK QNVNAAMVFE FLYKMCDVMA AYFGKISEEN IKNNFVLIYE LLDEILDFGY
     PQNSETGALK TFITQQGIKS QHQTKEEQSQ ITSQVTGQIG WRREGIKYRR NELFLDVLES
     VNLLMSPQGQ VLSAHVSGRV VMKSYLSGMP ECKFGMNDKI VIEKQGKGTA DETSKSGKQS
     IAIDDCTFHQ CVRLSKFDSE RSISFIPPDG EFELMRYRTT KDIILPFRVI PLVREVGRTK
     LEVKVVIKSN FKPSLLAQKI EVRIPTPLNT SGVQVICMKG KAKYKASENA IVWKIKRMAG
     MKESQISAEI ELLPTNDKKK WARPPISMNF EVPFAPSGLK VRYLKVFEPK LNYSDHDVIK
     WVRYIGRSGI YETRC
//
ID   RHOG_MOUSE              Reviewed;         191 AA.
AC   P84096; P35238; Q8NI04;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Rho-related GTP-binding protein RhoG;
DE   AltName: Full=Sid 10750;
DE   Flags: Precursor;
GN   Name=Rhog; Synonyms=Arhg, Sid10750;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.;
RT   "Mouse homolog of GTP-binding protein rhoG.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Required for the formation of membrane ruffles during
CC       macropinocytosis. Required for the formation of cup-like
CC       structures during trans-endothelial migration of leukocytes (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with ARHGEF26/SGEF (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
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DR   EMBL; AB025943; BAA84696.1; -; mRNA.
DR   EMBL; BC059775; AAH59775.1; -; mRNA.
DR   IPI; IPI00116558; -.
DR   RefSeq; NP_062512.1; NM_019566.3.
DR   UniGene; Mm.259795; -.
DR   ProteinModelPortal; P84096; -.
DR   SMR; P84096; 1-177.
DR   STRING; P84096; -.
DR   PRIDE; P84096; -.
DR   Ensembl; ENSMUST00000098230; ENSMUSP00000095832; ENSMUSG00000073982.
DR   Ensembl; ENSMUST00000106923; ENSMUSP00000102536; ENSMUSG00000073982.
DR   GeneID; 56212; -.
DR   KEGG; mmu:56212; -.
DR   UCSC; uc009irk.1; mouse.
DR   CTD; 56212; -.
DR   MGI; MGI:1928370; Rhog.
DR   eggNOG; roNOG12823; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; P84096; -.
DR   OMA; NYSAQNT; -.
DR   OrthoDB; EOG49KFRK; -.
DR   PhylomeDB; P84096; -.
DR   NextBio; 312054; -.
DR   ArrayExpress; P84096; -.
DR   Bgee; P84096; -.
DR   CleanEx; MM_RHOG; -.
DR   Genevestigator; P84096; -.
DR   GermOnline; ENSMUSG00000073982; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR003578; GTPase_Rho.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00174; RHO; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation.
FT   CHAIN         1    188       Rho-related GTP-binding protein RhoG.
FT                                /FTId=PRO_0000042030.
FT   PROPEP      189    191       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000042031.
FT   NP_BIND      10     17       GTP (By similarity).
FT   NP_BIND      57     61       GTP (By similarity).
FT   NP_BIND     115    118       GTP (By similarity).
FT   MOTIF        32     40       Effector region (Potential).
FT   MOD_RES     188    188       Cysteine methyl ester (By similarity).
FT   LIPID       188    188       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   191 AA;  21309 MW;  0C4FE9C54140F499 CRC64;
     MQSIKCVVVG DGAVGKTCLL ICYTTNAFPK EYIPTVFDNY SAQSAVDGRT VNLNLWDTAG
     QEEYDRLRTL SYPQTNVFVI CFSIASPPSY ENVRHKWHPE VCHHCPDVPI LLVGTKKDLR
     AQPDTLRRLK EQGQAPITPQ QGQALAKQIH AVRYLECSAL QQDGVKEVFA EAVRAVLNPT
     PIKRGRSCIL L
//
ID   H32_MOUSE               Reviewed;         136 AA.
AC   P84228; A3KMN6; P02295; P02297; P16105; P17269; P17320; Q60582;
AC   Q78E59; Q8CGN9;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Histone H3.2;
GN   Name=Hist1h3b; Synonyms=H3-53, H3.2, H3b;
GN   and
GN   Name=Hist1h3c; Synonyms=H3-143;
GN   and
GN   Name=Hist1h3d; Synonyms=H3-B;
GN   and
GN   Name=Hist1h3e; Synonyms=H3-F;
GN   and
GN   Name=Hist1h3f; Synonyms=H3.2-221, H3f;
GN   and
GN   Name=Hist2h3b; Synonyms=H3.2-616;
GN   and
GN   Name=Hist2h3c1; Synonyms=H3.2-615, Hist2h3ca1;
GN   and
GN   Name=Hist2h3c2; Synonyms=H3.2-614, Hist2h3ca2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3B).
RX   MEDLINE=84041477; PubMed=6314253; DOI=10.1093/nar/11.19.6679;
RA   Sittman D.B., Graves R.A., Marzluff W.F.;
RT   "Structure of a cluster of mouse histone genes.";
RL   Nucleic Acids Res. 11:6679-6697(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST2H3C2 AND HIST1H3F).
RX   MEDLINE=87112762; PubMed=3027355; DOI=10.1007/BF02115580;
RA   Taylor J.D., Wellman S.E., Marzluff W.F.;
RT   "Sequences of four mouse histone H3 genes: implications for evolution
RT   of mouse histone genes.";
RL   J. Mol. Evol. 23:242-249(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=90067871; PubMed=2587235; DOI=10.1093/nar/17.21.8876;
RA   Hurt M.M., Chodchoy N., Marzluff W.F.;
RT   "The mouse histone H2a.2 gene from chromosome 3.";
RL   Nucleic Acids Res. 17:8876-8876(1989).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3B).
RC   STRAIN=BALB/c;
RX   MEDLINE=91065547; PubMed=2249786; DOI=10.1016/0378-1119(90)90377-4;
RA   Gruber A., Streit A., Reist M., Benninger P., Boehni R.,
RA   Schuemperli D.;
RT   "Structure of a mouse histone-encoding gene cluster.";
RL   Gene 95:303-304(1990).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3C).
RX   MEDLINE=95095046; PubMed=8001786;
RA   DeBry R.W., Marzluff W.F.;
RT   "Selection on silent sites in the rodent histone H3 gene family.";
RL   Genetics 138:191-202(1994).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3C).
RC   STRAIN=C57BL/6J;
RX   MEDLINE=97011334; PubMed=8858344;
RA   Wang Z.-F., Krasikov T., Frey M.R., Wang J., Matera A.G.,
RA   Marzluff W.F.;
RT   "Characterization of the mouse histone gene cluster on chromosome 13:
RT   45 histone genes in three patches spread over 1Mb.";
RL   Genome Res. 6:688-701(1996).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3D; HIST1H3E; HIST2H3B AND
RP   HIST2H3CA1).
RX   MEDLINE=97011335; PubMed=8858345;
RA   Wang Z.-F., Tisovec R., Debry R.W., Frey M.R., Matera A.G.,
RA   Marzluff W.F.;
RT   "Characterization of the 55-kb mouse histone gene cluster on
RT   chromosome 3.";
RL   Genome Res. 6:702-714(1996).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIST1H3B; HIST1H3C; HIST1H3D;
RP   HIST1H3E; HIST1H3F; HIST2H3B; HIST2H3C1 AND HIST2H3C2).
RX   MEDLINE=22296985; PubMed=12408966; DOI=10.1016/S0888-7543(02)96850-3;
RA   Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
RT   "The human and mouse replication-dependent histone genes.";
RL   Genomics 80:487-498(2002).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (HIST2H3C2).
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 79-136.
RC   STRAIN=CD-1; TISSUE=Testis;
RX   MEDLINE=94344781; PubMed=8065931; DOI=10.1093/nar/22.15.3160;
RA   Moss S.B., Ferry R.A., Groudine M.;
RT   "An alternative pathway of histone mRNA 3' end formation in mouse
RT   round spermatids.";
RL   Nucleic Acids Res. 22:3160-3166(1994).
RN   [13]
RP   PHOSPHORYLATION AT SER-11 AND SER-29.
RX   PubMed=10464286; DOI=10.1074/jbc.274.36.25543;
RA   Goto H., Tomono Y., Ajiro K., Kosako H., Fujita M., Sakurai M.,
RA   Okawa K., Iwamatsu A., Okigaki T., Takahashi T., Inagaki M.;
RT   "Identification of a novel phosphorylation site on histone H3 coupled
RT   with mitotic chromosome condensation.";
RL   J. Biol. Chem. 274:25543-25549(1999).
RN   [14]
RP   PHOSPHORYLATION AT SER-29.
RX   PubMed=11441012; DOI=10.1074/jbc.M103973200;
RA   Zhong S., Jansen C., She Q.-B., Goto H., Inagaki M., Bode A.M.,
RA   Ma W.-Y., Dong Z.;
RT   "Ultraviolet B-induced phosphorylation of histone H3 at serine 28 is
RT   mediated by MSK1.";
RL   J. Biol. Chem. 276:33213-33219(2001).
RN   [15]
RP   ACETYLATION AT LYS-15; LYS-19 AND LYS-24, AND METHYLATION AT ARG-18.
RX   PubMed=12498683; DOI=10.1016/S0960-9822(02)01387-8;
RA   Daujat S., Bauer U.-M., Shah V., Turner B., Berger S., Kouzarides T.;
RT   "Crosstalk between CARM1 methylation and CBP acetylation on histone
RT   H3.";
RL   Curr. Biol. 12:2090-2097(2002).
RN   [16]
RP   METHYLATION AT ARG-18.
RX   PubMed=11751582; DOI=10.1093/embo-reports/kvf013;
RA   Bauer U.-M., Daujat S., Nielsen S.J., Nightingale K., Kouzarides T.;
RT   "Methylation at arginine 17 of histone H3 is linked to gene
RT   activation.";
RL   EMBO Rep. 3:39-44(2002).
RN   [17]
RP   PHOSPHORYLATION AT SER-11 AND SER-29.
RX   PubMed=11856369; DOI=10.1046/j.1356-9597.2001.00498.x;
RA   Goto H., Yasui Y., Nigg E.A., Inagaki M.;
RT   "Aurora-B phosphorylates Histone H3 at serine28 with regard to the
RT   mitotic chromosome condensation.";
RL   Genes Cells 7:11-17(2002).
RN   [18]
RP   ACETYLATION AT LYS-15; LYS-19 AND LYS-24, METHYLATION AT LYS-10;
RP   LYS-28; LYS-37; LYS-80 AND LYS-123, AND MASS SPECTROMETRY.
RX   PubMed=13678296; DOI=10.1023/A:1025334006014;
RA   Cocklin R.R., Wang M.;
RT   "Identification of methylation and acetylation sites on mouse histone
RT   H3 using matrix-assisted laser desorption/ionization time-of-flight
RT   and nanoelectrospray ionization tandem mass spectrometry.";
RL   J. Protein Chem. 22:327-334(2003).
RN   [19]
RP   CITRULLINATION.
RX   PubMed=15339660; DOI=10.1016/j.cell.2004.08.020;
RA   Cuthbert G.L., Daujat S., Snowden A.W., Erdjument-Bromage H.,
RA   Hagiwara T., Yamada M., Schneider R., Gregory P.D., Tempst P.,
RA   Bannister A.J., Kouzarides T.;
RT   "Histone deimination antagonizes arginine methylation.";
RL   Cell 118:545-553(2004).
RN   [20]
RP   METHYLATION AT ARG-9, AND ACETYLATION AT LYS-10.
RX   PubMed=15485929; DOI=10.1128/MCB.24.21.9630-9645.2004;
RA   Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S.;
RT   "Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and
RT   negatively regulates expression of ST7 and NM23 tumor suppressor
RT   genes.";
RL   Mol. Cell. Biol. 24:9630-9645(2004).
RN   [21]
RP   METHYLATION AT ARG-18.
RX   PubMed=15616592; DOI=10.1038/sj.emboj.7600500;
RA   Covic M., Hassa P.O., Saccani S., Buerki C., Meier N.I., Lombardi C.,
RA   Imhof R., Bedford M.T., Natoli G., Hottiger M.O.;
RT   "Arginine methyltransferase CARM1 is a promoter-specific regulator of
RT   NF-kappaB-dependent gene expression.";
RL   EMBO J. 24:85-96(2005).
RN   [22]
RP   PHOSPHORYLATION AT THR-4 AND SER-11.
RX   PubMed=15681610; DOI=10.1101/gad.1267105;
RA   Dai J., Sultan S., Taylor S.S., Higgins J.M.G.;
RT   "The kinase haspin is required for mitotic histone H3 Thr 3
RT   phosphorylation and normal metaphase chromosome alignment.";
RL   Genes Dev. 19:472-488(2005).
RN   [23]
RP   PHOSPHORYLATION AT SER-29.
RX   PubMed=15684425; DOI=10.1074/jbc.M410521200;
RA   Choi H.S., Choi B.Y., Cho Y.-Y., Zhu F., Bode A.M., Dong Z.;
RT   "Phosphorylation of Ser28 in histone H3 mediated by mixed lineage
RT   kinase-like mitogen-activated protein triple kinase alpha.";
RL   J. Biol. Chem. 280:13545-13553(2005).
RN   [24]
RP   PHOSPHORYLATION AT SER-11 AND SER-29.
RX   PubMed=15870105; DOI=10.1242/jcs.02373;
RA   Dyson M.H., Thomson S., Inagaki M., Goto H., Arthur S.J.,
RA   Nightingale K., Iborra F.J., Mahadevan L.C.;
RT   "MAP kinase-mediated phosphorylation of distinct pools of histone H3
RT   at S10 or S28 via mitogen- and stress-activated kinase 1/2.";
RL   J. Cell Sci. 118:2247-2259(2005).
RN   [25]
RP   PHOSPHORYLATION AT SER-11 AND SER-29.
RX   PubMed=15735677; DOI=10.1038/sj.onc.1208521;
RA   Dunn K.L., Davie J.R.;
RT   "Stimulation of the Ras-MAPK pathway leads to independent
RT   phosphorylation of histone H3 on serine 10 and 28.";
RL   Oncogene 24:3492-3502(2005).
RN   [26]
RP   ACETYLATION AT LYS-37.
RX   PubMed=17189264; DOI=10.1074/jbc.M607909200;
RA   Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L.,
RA   Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.;
RT   "Identification of histone H3 lysine 36 acetylation as a highly
RT   conserved histone modification.";
RL   J. Biol. Chem. 282:7632-7640(2007).
RN   [27]
RP   ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28,
RP   METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28; LYS-37 AND
RP   LYS-80, AND MASS SPECTROMETRY.
RX   PubMed=17194708; DOI=10.1074/jbc.M607900200;
RA   Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J.,
RA   Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.;
RT   "Organismal differences in post-translational modifications in
RT   histones H3 and H4.";
RL   J. Biol. Chem. 282:7641-7655(2007).
RN   [28]
RP   UBIQUITINATION.
RX   PubMed=20122409; DOI=10.1016/j.molcel.2009.12.035;
RA   Grazini U., Zanardi F., Citterio E., Casola S., Goding C.R.,
RA   McBlane F.;
RT   "The RING domain of RAG1 ubiquitylates histone H3: a novel activity in
RT   chromatin-mediated regulation of V(D)J joining.";
RL   Mol. Cell 37:282-293(2010).
CC   -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and
CC       compact DNA into chromatin, limiting DNA accessibility to the
CC       cellular machineries which require DNA as a template. Histones
CC       thereby play a central role in transcription regulation, DNA
CC       repair, DNA replication and chromosomal stability. DNA
CC       accessibility is regulated via a complex set of post-translational
CC       modifications of histones, also called histone code, and
CC       nucleosome remodeling.
CC   -!- SUBUNIT: The nucleosome is a histone octamer containing two
CC       molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
CC       heterotetramer and two H2A-H2B heterodimers. The octamer wraps
CC       approximately 147 bp of DNA. During nucleosome assembly the
CC       chaperone ASF1A interacts with the histone H3-H4 heterodimer (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- DEVELOPMENTAL STAGE: Expressed during S phase, then expression
CC       strongly decreases as cell division slows down during the process
CC       of differentiation.
CC   -!- PTM: Acetylation is generally linked to gene activation.
CC       Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9
CC       (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac)
CC       favors methylation at Arg-18 (H3R17me).
CC   -!- PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by
CC       PADI4 impairs methylation and represses transcription.
CC   -!- PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is
CC       linked to gene activation. Symmetric dimethylation at Arg-9
CC       (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric
CC       dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene
CC       repression and is mutually exclusive with H3 Lys-5 methylation
CC       (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes
CC       regardless of their transcription state and is enriched on
CC       inactive promoters, while it is absent on active promoters (By
CC       similarity).
CC   -!- PTM: Methylation at Lys-5 (H3K4me), Lys-37 (H3K36me) and Lys-80
CC       (H3K79me) are linked to gene activation. Methylation at Lys-5
CC       (H3K4me) facilitates subsequent acetylation of H3 and H4.
CC       Methylation at Lys-80 (H3K79me) is associated with DNA double-
CC       strand break (DSB) responses and is a specific target for TP53BP1.
CC       Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to
CC       gene repression. Methylation at Lys-10 (H3K9me) is a specific
CC       target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents
CC       subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of
CC       H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me)
CC       require preliminary monoubiquitination of H2B at 'Lys-120'.
CC       Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched
CC       in inactive X chromosome chromatin.
CC   -!- PTM: Phosphorylated at Thr-4 (H3T3ph) by GSG2/haspin during
CC       prophase and dephosphorylated during anaphase. Phosphorylation at
CC       Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation
CC       and cell-cycle progression during mitosis and meiosis. In addition
CC       phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is
CC       important during interphase because it enables the transcription
CC       of genes following external stimulation, like mitogens, stress,
CC       growth factors or UV irradiation and result in the activation of
CC       genes, such as c-fos and c-jun. Phosphorylation at Ser-11
CC       (H3S10ph), which is linked to gene activation, prevents
CC       methylation at Lys-10 (H3K9me) but facilitates acetylation of H3
CC       and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the
CC       dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from
CC       heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an
CC       essential regulatory mechanism for neoplastic cell transformation.
CC       Phosphorylated at Ser-29 (H3S28ph) by MLTK isoform 1, RPS6KA5 or
CC       AURKB during mitosis or upon ultraviolet B irradiation.
CC       Phosphorylation at Thr-7 (H3T6ph) by PRKCBB is a specific tag for
CC       epigenetic transcriptional activation that prevents demethylation
CC       of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically
CC       phosphorylated at Thr-12 (H3T11ph) from prophase to early
CC       anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph)
CC       by PKN1 is a specific tag for epigenetic transcriptional
CC       activation that promotes demethylation of Lys-10 (H3K9me) by
CC       KDM4C/JMJD2C. Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes
CC       exclusion of CBX5 (HP1 alpha) from chromatin.
CC   -!- PTM: Ubiquitinated by the CUL4-DDB-RBX1 complex in response to
CC       ultraviolet irradiation. This may weaken the interaction between
CC       histones and DNA and facilitate DNA accessibility to repair
CC       proteins (By similarity). Monoubiquitinated by RAG1 in lymphoid
CC       cells, monoubiquitination is required for V(D)J recombination.
CC   -!- SIMILARITY: Belongs to the histone H3 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH94041.1; Type=Erroneous initiation;
CC       Sequence=AAO06264.1; Type=Erroneous initiation;
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DR   EMBL; X01685; CAA25840.1; -; Genomic_DNA.
DR   EMBL; M32459; AAA37810.1; -; Genomic_DNA.
DR   EMBL; M32461; AAA37812.1; -; Genomic_DNA.
DR   EMBL; X16148; CAA34274.1; -; Genomic_DNA.
DR   EMBL; M33989; AAA37764.1; -; Genomic_DNA.
DR   EMBL; X80328; CAA56577.1; -; Genomic_DNA.
DR   EMBL; U62669; AAB04760.1; -; Genomic_DNA.
DR   EMBL; U62671; AAB04764.1; -; Genomic_DNA.
DR   EMBL; U62674; AAB04771.1; -; Genomic_DNA.
DR   EMBL; U62675; AAB04772.1; -; Genomic_DNA.
DR   EMBL; AY158941; AAO06251.1; -; Genomic_DNA.
DR   EMBL; AY158947; AAO06257.1; -; Genomic_DNA.
DR   EMBL; AY158948; AAO06258.1; -; Genomic_DNA.
DR   EMBL; AY158949; AAO06259.1; -; Genomic_DNA.
DR   EMBL; AY158950; AAO06260.1; -; Genomic_DNA.
DR   EMBL; AY158951; AAO06261.1; -; Genomic_DNA.
DR   EMBL; AY158954; AAO06264.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AY158955; AAO06265.1; -; Genomic_DNA.
DR   EMBL; AK010121; BAB26714.1; -; mRNA.
DR   EMBL; AK020421; BAB32097.1; -; mRNA.
DR   EMBL; AL590388; CAI25840.1; -; Genomic_DNA.
DR   EMBL; AL590388; CAI25844.1; -; Genomic_DNA.
DR   EMBL; BC015270; AAH15270.1; -; mRNA.
DR   EMBL; BC094041; AAH94041.1; ALT_INIT; mRNA.
DR   EMBL; BC101954; AAI01955.1; -; mRNA.
DR   EMBL; BC101955; AAI01956.1; -; mRNA.
DR   EMBL; BC101956; AAI01957.1; -; mRNA.
DR   EMBL; BC103549; AAI03550.1; -; mRNA.
DR   EMBL; BC120800; AAI20801.1; -; mRNA.
DR   EMBL; BC120802; AAI20803.1; -; mRNA.
DR   EMBL; BC132488; AAI32489.1; -; mRNA.
DR   EMBL; BC132490; AAI32491.1; -; mRNA.
DR   EMBL; Z30939; CAA83209.1; -; mRNA.
DR   IPI; IPI00230730; -.
DR   PIR; A39525; A39525.
DR   PIR; JH0304; JH0304.
DR   PIR; S06743; S06743.
DR   PIR; S48060; S45111.
DR   RefSeq; NP_038576.1; NM_013548.3.
DR   RefSeq; NP_473386.1; NM_054045.2.
DR   RefSeq; NP_783584.1; NM_175653.1.
DR   RefSeq; NP_835510.1; NM_178203.1.
DR   RefSeq; NP_835511.1; NM_178204.1.
DR   RefSeq; NP_835512.1; NM_178205.1.
DR   RefSeq; NP_835587.1; NM_178215.1.
DR   RefSeq; NP_835734.1; NM_178216.1.
DR   UniGene; Mm.221389; -.
DR   UniGene; Mm.261658; -.
DR   UniGene; Mm.262517; -.
DR   UniGene; Mm.342457; -.
DR   UniGene; Mm.347699; -.
DR   UniGene; Mm.358797; -.
DR   UniGene; Mm.383293; -.
DR   UniGene; Mm.422680; -.
DR   UniGene; Mm.474786; -.
DR   ProteinModelPortal; P84228; -.
DR   SMR; P84228; 17-136.
DR   DIP; DIP-49015N; -.
DR   STRING; P84228; -.
DR   PhosphoSite; P84228; -.
DR   PRIDE; P84228; -.
DR   Ensembl; ENSMUST00000075558; ENSMUSP00000074994; ENSMUSG00000059309.
DR   Ensembl; ENSMUST00000090779; ENSMUSP00000088284; ENSMUSG00000070392.
DR   Ensembl; ENSMUST00000091703; ENSMUSP00000089295; ENSMUSG00000069267.
DR   Ensembl; ENSMUST00000091711; ENSMUSP00000089303; ENSMUSG00000070392.
DR   Ensembl; ENSMUST00000098843; ENSMUSP00000096442; ENSMUSG00000074403.
DR   Ensembl; ENSMUST00000099704; ENSMUSP00000097295; ENSMUSG00000075032.
DR   Ensembl; ENSMUST00000105105; ENSMUSP00000100737; ENSMUSG00000062808.
DR   Ensembl; ENSMUST00000105107; ENSMUSP00000100739; ENSMUSG00000069273.
DR   GeneID; 15077; -.
DR   GeneID; 260423; -.
DR   GeneID; 319148; -.
DR   GeneID; 319149; -.
DR   GeneID; 319150; -.
DR   GeneID; 319151; -.
DR   GeneID; 319154; -.
DR   GeneID; 97114; -.
DR   KEGG; mmu:15077; -.
DR   KEGG; mmu:260423; -.
DR   KEGG; mmu:319148; -.
DR   KEGG; mmu:319149; -.
DR   KEGG; mmu:319150; -.
DR   KEGG; mmu:319151; -.
DR   KEGG; mmu:319154; -.
DR   KEGG; mmu:97114; -.
DR   UCSC; uc007ptz.1; mouse.
DR   CTD; 15077; -.
DR   CTD; 260423; -.
DR   CTD; 319148; -.
DR   CTD; 319149; -.
DR   CTD; 319150; -.
DR   CTD; 319151; -.
DR   CTD; 319154; -.
DR   CTD; 97114; -.
DR   MGI; MGI:2448319; Hist1h3b.
DR   MGI; MGI:2448320; Hist1h3c.
DR   MGI; MGI:2448322; Hist1h3d.
DR   MGI; MGI:2448326; Hist1h3e.
DR   MGI; MGI:2448329; Hist1h3f.
DR   MGI; MGI:2448351; Hist2h3b.
DR   MGI; MGI:2448355; Hist2h3c1.
DR   MGI; MGI:2448357; Hist2h3c2.
DR   GeneTree; ENSGT00560000076856; -.
DR   GeneTree; ENSGT00560000076889; -.
DR   HOVERGEN; HBG001172; -.
DR   InParanoid; P84228; -.
DR   OrthoDB; EOG412M6S; -.
DR   OrthoDB; EOG4V9TS1; -.
DR   PhylomeDB; P84228; -.
DR   NextBio; 392124; -.
DR   ArrayExpress; P84228; -.
DR   Bgee; P84228; -.
DR   CleanEx; MM_HIST1H3B; -.
DR   CleanEx; MM_HIST1H3C; -.
DR   CleanEx; MM_HIST1H3D; -.
DR   CleanEx; MM_HIST1H3E; -.
DR   CleanEx; MM_HIST1H3F; -.
DR   CleanEx; MM_HIST2H3C1; -.
DR   CleanEx; MM_HIST2H3C2; -.
DR   Genevestigator; P84228; -.
DR   GermOnline; ENSMUSG00000059309; Mus musculus.
DR   GermOnline; ENSMUSG00000068853; Mus musculus.
DR   GermOnline; ENSMUSG00000069267; Mus musculus.
DR   GermOnline; ENSMUSG00000069273; Mus musculus.
DR   GermOnline; ENSMUSG00000070392; Mus musculus.
DR   GermOnline; ENSMUSG00000071478; Mus musculus.
DR   GermOnline; ENSMUSG00000074403; Mus musculus.
DR   GermOnline; ENSMUSG00000075032; Mus musculus.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR007125; Histone_core_D.
DR   InterPro; IPR000164; Histone_H3.
DR   Gene3D; G3DSA:1.10.20.10; Histone-fold; 1.
DR   PANTHER; PTHR11426; Histone_H3; 1.
DR   Pfam; PF00125; Histone; 1.
DR   PRINTS; PR00622; HISTONEH3.
DR   SMART; SM00428; H3; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
DR   PROSITE; PS00322; HISTONE_H3_1; 1.
DR   PROSITE; PS00959; HISTONE_H3_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromosome; Citrullination; DNA-binding; Methylation;
KW   Nucleosome core; Nucleus; Phosphoprotein; Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    136       Histone H3.2.
FT                                /FTId=PRO_0000221250.
FT   MOD_RES       3      3       Asymmetric dimethylarginine; by PRMT6 (By
FT                                similarity).
FT   MOD_RES       4      4       Phosphothreonine.
FT   MOD_RES       5      5       N6-acetyllysine; alternate.
FT   MOD_RES       5      5       N6-methyllysine; alternate.
FT   MOD_RES       7      7       Phosphothreonine; by PKC (By similarity).
FT   MOD_RES       9      9       Citrulline; alternate (Probable).
FT   MOD_RES       9      9       Symmetric dimethylarginine; by PRMT5;
FT                                alternate.
FT   MOD_RES      10     10       N6,N6,N6-trimethyllysine; alternate.
FT   MOD_RES      10     10       N6,N6-dimethyllysine; alternate.
FT   MOD_RES      10     10       N6-acetyllysine; alternate.
FT   MOD_RES      10     10       N6-methyllysine; alternate.
FT   MOD_RES      11     11       Phosphoserine.
FT   MOD_RES      12     12       Phosphothreonine; by PKC (By similarity).
FT   MOD_RES      15     15       N6-acetyllysine.
FT   MOD_RES      18     18       Asymmetric dimethylarginine; by CARM1;
FT                                alternate.
FT   MOD_RES      18     18       Citrulline; alternate (By similarity).
FT   MOD_RES      19     19       N6-acetyllysine; alternate.
FT   MOD_RES      19     19       N6-methyllysine; alternate.
FT   MOD_RES      24     24       N6-acetyllysine; alternate.
FT   MOD_RES      24     24       N6-methyllysine; alternate.
FT   MOD_RES      28     28       N6,N6,N6-trimethyllysine; alternate.
FT   MOD_RES      28     28       N6,N6-dimethyllysine; alternate.
FT   MOD_RES      28     28       N6-acetyllysine; alternate.
FT   MOD_RES      28     28       N6-methyllysine; alternate.
FT   MOD_RES      29     29       Phosphoserine.
FT   MOD_RES      37     37       N6,N6,N6-trimethyllysine; alternate (By
FT                                similarity).
FT   MOD_RES      37     37       N6,N6-dimethyllysine; alternate.
FT   MOD_RES      37     37       N6-acetyllysine; alternate.
FT   MOD_RES      37     37       N6-methyllysine; alternate.
FT   MOD_RES      42     42       Phosphotyrosine (By similarity).
FT   MOD_RES      58     58       Phosphoserine (By similarity).
FT   MOD_RES      65     65       N6-methyllysine (By similarity).
FT   MOD_RES      80     80       N6,N6,N6-trimethyllysine; alternate.
FT   MOD_RES      80     80       N6,N6-dimethyllysine; alternate.
FT   MOD_RES      80     80       N6-methyllysine; alternate.
FT   MOD_RES      81     81       Phosphothreonine (By similarity).
FT   MOD_RES     123    123       N6-methyllysine (Probable).
SQ   SEQUENCE   136 AA;  15388 MW;  6FD8508EA50A0EEC CRC64;
     MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE
     LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY LVGLFEDTNL CAIHAKRVTI
     MPKDIQLARR IRGERA
//
ID   H33_MOUSE               Reviewed;         136 AA.
AC   P84244; P06351; P33155; Q3TW79; Q3U6D6; Q569U8; Q5HZY8; Q6TXQ5;
AC   Q8VDJ2; Q9D0H3; Q9V3W4;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Histone H3.3;
GN   Name=H3f3a; Synonyms=H3.3a;
GN   and
GN   Name=H3f3b; Synonyms=H3.3b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (H3F3B).
RX   MEDLINE=89240011; PubMed=2470025; DOI=10.1093/nar/17.7.2449;
RA   Hraba-Renevey S., Kress M.;
RT   "Expression of a mouse replacement histone H3.3 gene with a highly
RT   conserved 3' noncoding region during SV40- and polyoma-induced Go to
RT   S-phase transition.";
RL   Nucleic Acids Res. 17:2449-2461(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (H3F3A AND H3F3B), AND DEVELOPMENTAL STAGE.
RC   TISSUE=Spermatid;
RX   PubMed=9373943; DOI=10.1046/j.1432-0436.1997.6210013.x;
RA   Bramlage B., Kosciessa U., Doenecke D.;
RT   "Differential expression of the murine histone genes H3.3A and
RT   H3.3B.";
RL   Differentiation 62:13-20(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (H3F3A).
RC   STRAIN=Swiss; TISSUE=Ovary;
RX   PubMed=9174168; DOI=10.1089/dna.1997.16.639;
RA   Lopez-Alanon D.M., Lopez-Fernandez L.A., Castaneda V., Krimer D.B.,
RA   Del Mazo J.;
RT   "H3.3A variant histone mRNA containing an alpha-globin insertion:
RT   modulated expression during mouse gametogenesis correlates with
RT   meiotic onset.";
RL   DNA Cell Biol. 16:639-644(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (H3F3A AND H3F3B).
RC   STRAIN=BALB/c, C57BL/6J, DBA/2, and NOD;
RC   TISSUE=Bone marrow, Egg, Head, Kidney, Muellerian duct, Stomach, and
RC   Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (H3F3A AND H3F3B).
RC   STRAIN=C57BL/6, and FVB/N;
RC   TISSUE=Brain, Colon, Mammary tumor, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-122.
RX   PubMed=15638457; DOI=10.1007/s00239-004-2637-4;
RA   Mancini P., Pulcrano G., Piscopo M., Aniello F., Branno M., Fucci L.;
RT   "A new family of 'H3L-like' histone genes.";
RL   J. Mol. Evol. 59:458-463(2004).
RN   [7]
RP   PHOSPHORYLATION AT SER-11 AND SER-29.
RX   PubMed=10464286; DOI=10.1074/jbc.274.36.25543;
RA   Goto H., Tomono Y., Ajiro K., Kosako H., Fujita M., Sakurai M.,
RA   Okawa K., Iwamatsu A., Okigaki T., Takahashi T., Inagaki M.;
RT   "Identification of a novel phosphorylation site on histone H3 coupled
RT   with mitotic chromosome condensation.";
RL   J. Biol. Chem. 274:25543-25549(1999).
RN   [8]
RP   PHOSPHORYLATION AT SER-29.
RX   PubMed=11441012; DOI=10.1074/jbc.M103973200;
RA   Zhong S., Jansen C., She Q.-B., Goto H., Inagaki M., Bode A.M.,
RA   Ma W.-Y., Dong Z.;
RT   "Ultraviolet B-induced phosphorylation of histone H3 at serine 28 is
RT   mediated by MSK1.";
RL   J. Biol. Chem. 276:33213-33219(2001).
RN   [9]
RP   ACETYLATION AT LYS-15; LYS-19 AND LYS-24, AND METHYLATION AT ARG-18.
RX   PubMed=12498683; DOI=10.1016/S0960-9822(02)01387-8;
RA   Daujat S., Bauer U.-M., Shah V., Turner B., Berger S., Kouzarides T.;
RT   "Crosstalk between CARM1 methylation and CBP acetylation on histone
RT   H3.";
RL   Curr. Biol. 12:2090-2097(2002).
RN   [10]
RP   METHYLATION AT ARG-18.
RX   PubMed=11751582; DOI=10.1093/embo-reports/kvf013;
RA   Bauer U.-M., Daujat S., Nielsen S.J., Nightingale K., Kouzarides T.;
RT   "Methylation at arginine 17 of histone H3 is linked to gene
RT   activation.";
RL   EMBO Rep. 3:39-44(2002).
RN   [11]
RP   PHOSPHORYLATION AT SER-11 AND SER-29.
RX   PubMed=11856369; DOI=10.1046/j.1356-9597.2001.00498.x;
RA   Goto H., Yasui Y., Nigg E.A., Inagaki M.;
RT   "Aurora-B phosphorylates Histone H3 at serine28 with regard to the
RT   mitotic chromosome condensation.";
RL   Genes Cells 7:11-17(2002).
RN   [12]
RP   ACETYLATION AT LYS-15; LYS-19 AND LYS-24, METHYLATION AT LYS-10;
RP   LYS-28; LYS-37; LYS-80 AND LYS-123, AND MASS SPECTROMETRY.
RX   PubMed=13678296; DOI=10.1023/A:1025334006014;
RA   Cocklin R.R., Wang M.;
RT   "Identification of methylation and acetylation sites on mouse histone
RT   H3 using matrix-assisted laser desorption/ionization time-of-flight
RT   and nanoelectrospray ionization tandem mass spectrometry.";
RL   J. Protein Chem. 22:327-334(2003).
RN   [13]
RP   CITRULLINATION.
RX   PubMed=15339660; DOI=10.1016/j.cell.2004.08.020;
RA   Cuthbert G.L., Daujat S., Snowden A.W., Erdjument-Bromage H.,
RA   Hagiwara T., Yamada M., Schneider R., Gregory P.D., Tempst P.,
RA   Bannister A.J., Kouzarides T.;
RT   "Histone deimination antagonizes arginine methylation.";
RL   Cell 118:545-553(2004).
RN   [14]
RP   METHYLATION AT ARG-9, AND ACETYLATION AT LYS-10.
RX   PubMed=15485929; DOI=10.1128/MCB.24.21.9630-9645.2004;
RA   Pal S., Vishwanath S.N., Erdjument-Bromage H., Tempst P., Sif S.;
RT   "Human SWI/SNF-associated PRMT5 methylates histone H3 arginine 8 and
RT   negatively regulates expression of ST7 and NM23 tumor suppressor
RT   genes.";
RL   Mol. Cell. Biol. 24:9630-9645(2004).
RN   [15]
RP   METHYLATION AT ARG-18.
RX   PubMed=15616592; DOI=10.1038/sj.emboj.7600500;
RA   Covic M., Hassa P.O., Saccani S., Buerki C., Meier N.I., Lombardi C.,
RA   Imhof R., Bedford M.T., Natoli G., Hottiger M.O.;
RT   "Arginine methyltransferase CARM1 is a promoter-specific regulator of
RT   NF-kappaB-dependent gene expression.";
RL   EMBO J. 24:85-96(2005).
RN   [16]
RP   PHOSPHORYLATION AT THR-4 AND SER-11.
RX   PubMed=15681610; DOI=10.1101/gad.1267105;
RA   Dai J., Sultan S., Taylor S.S., Higgins J.M.G.;
RT   "The kinase haspin is required for mitotic histone H3 Thr 3
RT   phosphorylation and normal metaphase chromosome alignment.";
RL   Genes Dev. 19:472-488(2005).
RN   [17]
RP   PHOSPHORYLATION AT SER-29.
RX   PubMed=15684425; DOI=10.1074/jbc.M410521200;
RA   Choi H.S., Choi B.Y., Cho Y.-Y., Zhu F., Bode A.M., Dong Z.;
RT   "Phosphorylation of Ser28 in histone H3 mediated by mixed lineage
RT   kinase-like mitogen-activated protein triple kinase alpha.";
RL   J. Biol. Chem. 280:13545-13553(2005).
RN   [18]
RP   PHOSPHORYLATION AT SER-11 AND SER-29.
RX   PubMed=15870105; DOI=10.1242/jcs.02373;
RA   Dyson M.H., Thomson S., Inagaki M., Goto H., Arthur S.J.,
RA   Nightingale K., Iborra F.J., Mahadevan L.C.;
RT   "MAP kinase-mediated phosphorylation of distinct pools of histone H3
RT   at S10 or S28 via mitogen- and stress-activated kinase 1/2.";
RL   J. Cell Sci. 118:2247-2259(2005).
RN   [19]
RP   PHOSPHORYLATION AT SER-11 AND SER-29.
RX   PubMed=15735677; DOI=10.1038/sj.onc.1208521;
RA   Dunn K.L., Davie J.R.;
RT   "Stimulation of the Ras-MAPK pathway leads to independent
RT   phosphorylation of histone H3 on serine 10 and 28.";
RL   Oncogene 24:3492-3502(2005).
RN   [20]
RP   ACETYLATION AT LYS-5; LYS-10; LYS-15; LYS-19; LYS-24 AND LYS-28,
RP   METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28; LYS-37 AND
RP   LYS-80, AND MASS SPECTROMETRY.
RX   PubMed=17194708; DOI=10.1074/jbc.M607900200;
RA   Garcia B.A., Hake S.B., Diaz R.L., Kauer M., Morris S.A., Recht J.,
RA   Shabanowitz J., Mishra N., Strahl B.D., Allis C.D., Hunt D.F.;
RT   "Organismal differences in post-translational modifications in
RT   histones H3 and H4.";
RL   J. Biol. Chem. 282:7641-7655(2007).
RN   [21]
RP   ACETYLATION AT LYS-37.
RX   PubMed=17189264; DOI=10.1074/jbc.M607909200;
RA   Morris S.A., Rao B., Garcia B.A., Hake S.B., Diaz R.L.,
RA   Shabanowitz J., Hunt D.F., Allis C.D., Lieb J.D., Strahl B.D.;
RT   "Identification of histone H3 lysine 36 acetylation as a highly
RT   conserved histone modification.";
RL   J. Biol. Chem. 282:7632-7640(2007).
RN   [22]
RP   UBIQUITINATION.
RX   PubMed=20122409; DOI=10.1016/j.molcel.2009.12.035;
RA   Grazini U., Zanardi F., Citterio E., Casola S., Goding C.R.,
RA   McBlane F.;
RT   "The RING domain of RAG1 ubiquitylates histone H3: a novel activity in
RT   chromatin-mediated regulation of V(D)J joining.";
RL   Mol. Cell 37:282-293(2010).
CC   -!- FUNCTION: Variant histone H3 which replaces conventional H3 in a
CC       wide range of nucleosomes in active genes. Constitutes the
CC       predominant form of histone H3 in non-dividing cells and is
CC       incorporated into chromatin independently of DNA synthesis.
CC       Deposited at sites of nucleosomal displacement throughout
CC       transcribed genes, suggesting that it represents an epigenetic
CC       imprint of transcriptionally active chromatin. Nucleosomes wrap
CC       and compact DNA into chromatin, limiting DNA accessibility to the
CC       cellular machineries which require DNA as a template. Histones
CC       thereby play a central role in transcription regulation, DNA
CC       repair, DNA replication and chromosomal stability. DNA
CC       accessibility is regulated via a complex set of post-translational
CC       modifications of histones, also called histone code, and
CC       nucleosome remodeling.
CC   -!- SUBUNIT: The nucleosome is a histone octamer containing two
CC       molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
CC       heterotetramer and two H2A-H2B heterodimers. The octamer wraps
CC       approximately 147 bp of DNA. Interacts with HIRA, a chaperone
CC       required for its incorporation into nucleosomes.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout the cell cycle
CC       independently of DNA synthesis.
CC   -!- PTM: Acetylation is generally linked to gene activation.
CC       Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9
CC       (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac)
CC       favors methylation at Arg-18 (H3R17me).
CC   -!- PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by
CC       PADI4 impairs methylation and represses transcription.
CC   -!- PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is
CC       linked to gene activation. Symmetric dimethylation at Arg-9
CC       (H3R8me2s) by PRMT5 is linked to gene repression. Asymmetric
CC       dimethylation at Arg-3 (H3R2me2a) by PRMT6 is linked to gene
CC       repression and is mutually exclusive with H3 Lys-5 methylation
CC       (H3K4me2 and H3K4me3). H3R2me2a is present at the 3' of genes
CC       regardless of their transcription state and is enriched on
CC       inactive promoters, while it is absent on active promoters (By
CC       similarity).
CC   -!- PTM: Specifically enriched in modifications associated with active
CC       chromatin such as methylation at Lys-5 (H3K4me), Lys-37 and Lys-
CC       80. Methylation at Lys-5 (H3K4me) facilitates subsequent
CC       acetylation of H3 and H4. Methylation at Lys-80 (H3K79me) is
CC       associated with DNA double-strand break (DSB) responses and is a
CC       specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and
CC       Lys-28 (H3K27me), which are linked to gene repression, are
CC       underrepresented. Methylation at Lys-10 (H3K9me) is a specific
CC       target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents
CC       subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of
CC       H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 (H3K79me)
CC       require preliminary monoubiquitination of H2B at 'Lys-120'.
CC       Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched
CC       in inactive X chromosome chromatin.
CC   -!- PTM: Phosphorylated at Thr-4 (H3T3ph) by GSG2/haspin during
CC       prophase and dephosphorylated during anaphase. Phosphorylation at
CC       Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation
CC       and cell-cycle progression during mitosis and meiosis. In addition
CC       phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is
CC       important during interphase because it enables the transcription
CC       of genes following external stimulation, like mitogens, stress,
CC       growth factors or UV irradiation and result in the activation of
CC       genes, such as c-fos and c-jun. Phosphorylation at Ser-11
CC       (H3S10ph), which is linked to gene activation, prevents
CC       methylation at Lys-10 (H3K9me) but facilitates acetylation of H3
CC       and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the
CC       dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from
CC       heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an
CC       essential regulatory mechanism for neoplastic cell transformation.
CC       Phosphorylated at Ser-29 (H3S28ph) by MLTK isoform 1, RPS6KA5 or
CC       AURKB during mitosis or upon ultraviolet B irradiation.
CC       Phosphorylation at Thr-7 (H3T6ph) by PRKCBB is a specific tag for
CC       epigenetic transcriptional activation that prevents demethylation
CC       of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically
CC       phosphorylated at Thr-12 (H3T11ph) from prophase to early
CC       anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph)
CC       by PKN1 is a specific tag for epigenetic transcriptional
CC       activation that promotes demethylation of Lys-10 (H3K9me) by
CC       KDM4C/JMJD2C. Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes
CC       exclusion of CBX5 (HP1 alpha) from chromatin. Phosphorylation on
CC       Ser-32 (H3S31ph) is specific to regions bordering centromeres in
CC       metaphase chromosomes. metaphase chromosomes.
CC   -!- PTM: Ubiquitinated. Monoubiquitinated by RAG1 in lymphoid cells,
CC       monoubiquitination is required for V(D)J recombination (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the histone H3 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH92300.1; Type=Frameshift; Positions=127;
CC       Sequence=BAB27616.1; Type=Frameshift; Positions=99;
CC       Sequence=BAE35387.1; Type=Frameshift; Positions=Several;
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DR   EMBL; X13605; CAA31940.1; -; mRNA.
DR   EMBL; Z85979; CAB06625.1; -; mRNA.
DR   EMBL; X91866; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK002928; BAB22464.1; -; mRNA.
DR   EMBL; AK011431; BAB27616.1; ALT_FRAME; mRNA.
DR   EMBL; AK037900; BAC29895.1; -; mRNA.
DR   EMBL; AK088075; BAC40130.1; -; mRNA.
DR   EMBL; AK135839; BAE22687.1; -; mRNA.
DR   EMBL; AK150467; BAE29584.1; -; mRNA.
DR   EMBL; AK150468; BAE29585.1; -; mRNA.
DR   EMBL; AK150591; BAE29685.1; -; mRNA.
DR   EMBL; AK150928; BAE29966.1; -; mRNA.
DR   EMBL; AK151274; BAE30261.1; -; mRNA.
DR   EMBL; AK151336; BAE30314.1; -; mRNA.
DR   EMBL; AK151451; BAE30411.1; -; mRNA.
DR   EMBL; AK151634; BAE30566.1; -; mRNA.
DR   EMBL; AK151658; BAE30586.1; -; mRNA.
DR   EMBL; AK151661; BAE30589.1; -; mRNA.
DR   EMBL; AK151869; BAE30757.1; -; mRNA.
DR   EMBL; AK152293; BAE31102.1; -; mRNA.
DR   EMBL; AK152453; BAE31231.1; -; mRNA.
DR   EMBL; AK152455; BAE31233.1; -; mRNA.
DR   EMBL; AK152623; BAE31366.1; -; mRNA.
DR   EMBL; AK152911; BAE31590.1; -; mRNA.
DR   EMBL; AK153034; BAE31666.1; -; mRNA.
DR   EMBL; AK153189; BAE31789.1; -; mRNA.
DR   EMBL; AK153239; BAE31831.1; -; mRNA.
DR   EMBL; AK153294; BAE31877.1; -; mRNA.
DR   EMBL; AK153371; BAE31939.1; -; mRNA.
DR   EMBL; AK153530; BAE32069.1; -; mRNA.
DR   EMBL; AK159615; BAE35232.1; -; mRNA.
DR   EMBL; AK159807; BAE35387.1; ALT_FRAME; mRNA.
DR   EMBL; AK159850; BAE35427.1; -; mRNA.
DR   EMBL; AK160677; BAE35953.1; -; mRNA.
DR   EMBL; AK161675; BAE36524.1; -; mRNA.
DR   EMBL; AK162040; BAE36694.1; -; mRNA.
DR   EMBL; AK163244; BAE37253.1; -; mRNA.
DR   EMBL; AK167828; BAE39850.1; -; mRNA.
DR   EMBL; AK167879; BAE39892.1; -; mRNA.
DR   EMBL; AK168197; BAE40157.1; -; mRNA.
DR   EMBL; AK168698; BAE40542.1; -; mRNA.
DR   EMBL; AK169042; BAE40831.1; -; mRNA.
DR   EMBL; AK169226; BAE40995.1; -; mRNA.
DR   EMBL; BC002268; AAH02268.1; -; mRNA.
DR   EMBL; BC012687; AAH12687.1; -; mRNA.
DR   EMBL; BC021768; AAH21768.1; -; mRNA.
DR   EMBL; BC037730; AAH37730.1; -; mRNA.
DR   EMBL; BC083353; AAH83353.1; -; mRNA.
DR   EMBL; BC088835; AAH88835.1; -; mRNA.
DR   EMBL; BC092043; AAH92043.1; -; mRNA.
DR   EMBL; BC092300; AAH92300.1; ALT_FRAME; mRNA.
DR   EMBL; BC106177; AAI06178.1; -; mRNA.
DR   EMBL; AY383567; AAQ96274.1; -; Genomic_DNA.
DR   IPI; IPI00785343; -.
DR   PIR; S04186; S04186.
DR   RefSeq; NP_032236.1; NM_008210.4.
DR   RefSeq; NP_032237.1; NM_008211.3.
DR   UniGene; Mm.138832; -.
DR   UniGene; Mm.18516; -.
DR   UniGene; Mm.315189; -.
DR   UniGene; Mm.316825; -.
DR   UniGene; Mm.322735; -.
DR   UniGene; Mm.371563; -.
DR   UniGene; Mm.442502; -.
DR   UniGene; Mm.471842; -.
DR   ProteinModelPortal; P84244; -.
DR   SMR; P84244; 2-136.
DR   IntAct; P84244; 58.
DR   STRING; P84244; -.
DR   PRIDE; P84244; -.
DR   Ensembl; ENSMUST00000016703; ENSMUSP00000016703; ENSMUSG00000016559.
DR   Ensembl; ENSMUST00000081026; ENSMUSP00000079816; ENSMUSG00000060743.
DR   Ensembl; ENSMUST00000106454; ENSMUSP00000102062; ENSMUSG00000016559.
DR   GeneID; 15078; -.
DR   GeneID; 15081; -.
DR   KEGG; mmu:15078; -.
DR   KEGG; mmu:15081; -.
DR   UCSC; uc007dwr.1; mouse.
DR   CTD; 15078; -.
DR   CTD; 15081; -.
DR   MGI; MGI:1097686; H3f3a.
DR   MGI; MGI:1101768; H3f3b.
DR   GeneTree; ENSGT00560000076889; -.
DR   HOVERGEN; HBG001172; -.
DR   InParanoid; P84244; -.
DR   OMA; RIRGERX; -.
DR   OrthoDB; EOG4V9TS1; -.
DR   PhylomeDB; P84244; -.
DR   NextBio; 458959; -.
DR   ArrayExpress; P84244; -.
DR   Bgee; P84244; -.
DR   CleanEx; MM_H3F3A; -.
DR   CleanEx; MM_H3F3B; -.
DR   Genevestigator; P84244; -.
DR   GermOnline; ENSMUSG00000060743; Mus musculus.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR007125; Histone_core_D.
DR   InterPro; IPR000164; Histone_H3.
DR   Gene3D; G3DSA:1.10.20.10; Histone-fold; 1.
DR   PANTHER; PTHR11426; Histone_H3; 1.
DR   Pfam; PF00125; Histone; 1.
DR   PRINTS; PR00622; HISTONEH3.
DR   SMART; SM00428; H3; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
DR   PROSITE; PS00322; HISTONE_H3_1; 1.
DR   PROSITE; PS00959; HISTONE_H3_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromosome; Citrullination; DNA-binding; Methylation;
KW   Nucleosome core; Nucleus; Phosphoprotein; Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    136       Histone H3.3.
FT                                /FTId=PRO_0000221251.
FT   MOD_RES       3      3       Asymmetric dimethylarginine; by PRMT6 (By
FT                                similarity).
FT   MOD_RES       4      4       Phosphothreonine.
FT   MOD_RES       5      5       N6-acetyllysine; alternate.
FT   MOD_RES       5      5       N6-methyllysine; alternate.
FT   MOD_RES       7      7       Phosphothreonine; by PKC (By similarity).
FT   MOD_RES       9      9       Citrulline; alternate (Probable).
FT   MOD_RES       9      9       Symmetric dimethylarginine; by PRMT5;
FT                                alternate.
FT   MOD_RES      10     10       N6,N6,N6-trimethyllysine; alternate.
FT   MOD_RES      10     10       N6,N6-dimethyllysine; alternate.
FT   MOD_RES      10     10       N6-acetyllysine; alternate.
FT   MOD_RES      10     10       N6-methyllysine; alternate.
FT   MOD_RES      11     11       Phosphoserine.
FT   MOD_RES      12     12       Phosphothreonine; by PKC (By similarity).
FT   MOD_RES      15     15       N6-acetyllysine.
FT   MOD_RES      18     18       Asymmetric dimethylarginine; by CARM1;
FT                                alternate.
FT   MOD_RES      18     18       Citrulline; alternate.
FT   MOD_RES      19     19       N6-acetyllysine; alternate.
FT   MOD_RES      19     19       N6-methyllysine; alternate.
FT   MOD_RES      24     24       N6-acetyllysine; alternate.
FT   MOD_RES      24     24       N6-methyllysine; alternate.
FT   MOD_RES      28     28       N6,N6,N6-trimethyllysine; alternate.
FT   MOD_RES      28     28       N6,N6-dimethyllysine; alternate.
FT   MOD_RES      28     28       N6-acetyllysine; alternate.
FT   MOD_RES      28     28       N6-methyllysine; alternate.
FT   MOD_RES      29     29       Phosphoserine.
FT   MOD_RES      32     32       Phosphoserine (By similarity).
FT   MOD_RES      37     37       N6,N6,N6-trimethyllysine; alternate (By
FT                                similarity).
FT   MOD_RES      37     37       N6,N6-dimethyllysine; alternate.
FT   MOD_RES      37     37       N6-acetyllysine; alternate.
FT   MOD_RES      37     37       N6-methyllysine; alternate.
FT   MOD_RES      42     42       Phosphotyrosine (By similarity).
FT   MOD_RES      58     58       Phosphoserine (By similarity).
FT   MOD_RES      65     65       N6-methyllysine (By similarity).
FT   MOD_RES      80     80       N6,N6,N6-trimethyllysine; alternate.
FT   MOD_RES      80     80       N6,N6-dimethyllysine; alternate.
FT   MOD_RES      80     80       N6-methyllysine; alternate.
FT   MOD_RES      81     81       Phosphothreonine (By similarity).
FT   MOD_RES     108    108       Phosphothreonine (By similarity).
FT   MOD_RES     123    123       N6-methyllysine (Probable).
FT   CONFLICT     75     75       I -> T (in Ref. 5; AAH21768).
FT   CONFLICT     99     99       A -> E (in Ref. 4; BAE31789/BAE30411).
FT   CONFLICT    129    129       R -> C (in Ref. 3; X91866).
SQ   SEQUENCE   136 AA;  15328 MW;  5158ED279E6F9E1C CRC64;
     MARTKQTARK STGGKAPRKQ LATKAARKSA PSTGGVKKPH RYRPGTVALR EIRRYQKSTE
     LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY LVGLFEDTNL CAIHAKRVTI
     MPKDIQLARR IRGERA
//
ID   ADCY5_MOUSE             Reviewed;        1262 AA.
AC   P84309; Q3TU67; Q3UH09; Q5BL06;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Adenylate cyclase type 5;
DE            EC=4.6.1.1;
DE   AltName: Full=ATP pyrophosphate-lyase 5;
DE   AltName: Full=Adenylate cyclase type V;
DE   AltName: Full=Adenylyl cyclase 5;
GN   Name=Adcy5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: This is a membrane-bound, calcium-inhibitable adenylyl
CC       cyclase.
CC   -!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
CC   -!- COFACTOR: Binds 2 magnesium ions per subunit (By similarity).
CC   -!- ENZYME REGULATION: Inhibition by calcium in the submicromolar
CC       concentration range (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P84309-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P84309-2; Sequence=VSP_022224;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
CC       cyclase family.
CC   -!- SIMILARITY: Contains 2 guanylate cyclase domains.
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DR   EMBL; AK147649; BAE28048.1; -; mRNA.
DR   EMBL; AK160942; BAE36104.1; -; mRNA.
DR   EMBL; BC035550; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC090846; AAH90846.1; -; mRNA.
DR   IPI; IPI00756908; -.
DR   IPI; IPI00816877; -.
DR   RefSeq; NP_001012783.3; NM_001012765.4.
DR   UniGene; Mm.41137; -.
DR   ProteinModelPortal; P84309; -.
DR   SMR; P84309; 455-644, 1064-1256.
DR   STRING; P84309; -.
DR   PhosphoSite; P84309; -.
DR   PRIDE; P84309; -.
DR   Ensembl; ENSMUST00000023549; ENSMUSP00000023549; ENSMUSG00000022840.
DR   Ensembl; ENSMUST00000114913; ENSMUSP00000110563; ENSMUSG00000022840.
DR   GeneID; 224129; -.
DR   KEGG; mmu:224129; -.
DR   UCSC; uc007zbj.1; mouse.
DR   CTD; 224129; -.
DR   MGI; MGI:99673; Adcy5.
DR   eggNOG; roNOG11298; -.
DR   GeneTree; ENSGT00590000082802; -.
DR   HOVERGEN; HBG050458; -.
DR   OMA; GDEQGFC; -.
DR   OrthoDB; EOG4255S0; -.
DR   BRENDA; 4.6.1.1; 244.
DR   NextBio; 377103; -.
DR   ArrayExpress; P84309; -.
DR   Bgee; P84309; -.
DR   CleanEx; MM_ADCY5; -.
DR   Genevestigator; P84309; -.
DR   GermOnline; ENSMUSG00000022840; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0004016; F:adenylate cyclase activity; IMP:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007191; P:activation of adenylate cyclase activity by dopamine receptor signaling pathway; IGI:MGI.
DR   GO; GO:0001973; P:adenosine receptor signaling pathway; IGI:MGI.
DR   GO; GO:0007195; P:inhibition of adenylate cyclase activity by dopamine receptor signaling pathway; IGI:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   InterPro; IPR009398; Aden_cycl-like.
DR   Gene3D; G3DSA:3.30.70.1230; A/G_cyclase; 2.
DR   Pfam; PF06327; DUF1053; 1.
DR   Pfam; PF00211; Guanylate_cyc; 2.
DR   SMART; SM00044; CYCc; 2.
DR   SUPFAM; SSF55073; A/G_cyclase; 2.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 2.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; cAMP biosynthesis; Coiled coil;
KW   Glycoprotein; Lyase; Magnesium; Membrane; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Repeat; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   1262       Adenylate cyclase type 5.
FT                                /FTId=PRO_0000195695.
FT   TOPO_DOM      1    196       Cytoplasmic (Potential).
FT   TRANSMEM    197    217       Helical; (Potential).
FT   TRANSMEM    243    263       Helical; (Potential).
FT   TRANSMEM    269    289       Helical; (Potential).
FT   TRANSMEM    300    320       Helical; (Potential).
FT   TRANSMEM    326    346       Helical; (Potential).
FT   TRANSMEM    375    395       Helical; (Potential).
FT   TOPO_DOM    396    763       Cytoplasmic (Potential).
FT   TRANSMEM    764    784       Helical; (Potential).
FT   TRANSMEM    790    810       Helical; (Potential).
FT   TRANSMEM    837    857       Helical; (Potential).
FT   TOPO_DOM    858    910       Extracellular (Potential).
FT   TRANSMEM    911    931       Helical; (Potential).
FT   TRANSMEM    936    956       Helical; (Potential).
FT   TRANSMEM    985   1005       Helical; (Potential).
FT   TOPO_DOM   1006   1262       Cytoplasmic (Potential).
FT   DOMAIN      470    597       Guanylate cyclase 1.
FT   DOMAIN     1072   1211       Guanylate cyclase 2.
FT   COILED     1019   1045       Potential.
FT   COMPBIAS     64     67       Poly-Gln.
FT   COMPBIAS    141    147       Poly-Ala.
FT   METAL       475    475       Magnesium 1 (By similarity).
FT   METAL       475    475       Magnesium 2 (By similarity).
FT   METAL       476    476       Magnesium 2; via carbonyl oxygen (By
FT                                similarity).
FT   MOD_RES       8      8       Phosphoserine.
FT   CARBOHYD    239    239       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    834    834       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    871    871       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    888    888       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    973    973       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ    1259   1262       PPLS -> LGHDGVVGKLKAGLGVSMELKGLLFHCGEVTPP
FT                                HNVWGTGTGRRVACAILSPHLHAQRQCPVRETGLLTREARG
FT                                HQARSSGSEQKKIFIK (in isoform 2).
FT                                /FTId=VSP_022224.
FT   CONFLICT     25     25       G -> S (in Ref. 2; AAH90846).
FT   CONFLICT    686    686       G -> D (in Ref. 1; BAE28048).
FT   CONFLICT    924    924       V -> M (in Ref. 2; AAH90846).
SQ   SEQUENCE   1262 AA;  139122 MW;  342966E7CA67E28D CRC64;
     MSGSKSVSPP GYAAQTAASP APRGGPEHRA AWGEADSRAN GYPHAPGGST RGSTKRSGGA
     VTPQQQQRLA SRWRGGDDDE DPPLSGDDPL AGGFGFSFRS KSAWQERGGD DGGRGSRRQR
     RGAAGGGSTR APPAGGSGSS AAAAAAAGGT EVRPRSVELG LEERRGKGRA AEELEPGTGI
     VEDGDGSEDG GSSVASGSGT GAVLSLGACC LALLQIFRSK KFPSDKLERL YQRYFFRLNQ
     SSLTMLMAVL VLVCLVMLAF HAARPPLQIA YLAVLAAAVG VILIMAVLCN RAAFHQDHMG
     LACYALIAVV LAVQVVGLLL PQPRSASEGI WWTVFFIYTI YTLLPVRMRA AVLSGVLLSA
     LHLAISLHTN SQDQFLLKQL VSNVLIFSCT NIVGVCTHYP AEVSQRQAFQ ETRECIQARL
     HSQRENQQQE RLLLSVLPRH VAMEMKADIN AKQEDMMFHK IYIQKHDNVS ILFADIEGFT
     SLASQCTAQE LVMTLNELFA RFDKLAAENH CLRIKILGDC YYCVSGLPEA RADHAHCCVE
     MGMDMIEAIS LVREVTGVNV NMRVGIHSGR VHCGVLGLRK WQFDVWSNDV TLANHMEAGG
     KAGRIHITKA TLNYLNGDYE VEPGCGGDRN AYLKEHSIET FLILSCTQKR KEEKAMIAKM
     NRQRTNSIGH NPPHWGAERP FYNHLGGNQV SKEMKRMGFE DPKDKNAQES ANPEDEVDEF
     LGRAIDARSI DRLRSEHVRK FLLTFREPDL EKKYSKQVDD RFGAYVACAS LVFLFICFVQ
     ITIVPHSLFM LSFYLSCFLL LALVVFVSVI YACVKLFPTP LQTLSRKIVR SKKNSTLVGV
     FTITLVFLSA FVNMFMCNSK NLVGCLAEEH NITVNQVNAC HVMESAFNYS LGDEQGFCGS
     PQPNCNFPEY FTYSVLLSLL ACSVFLQISC IGKLVLMLAI EFIYVLIVEV PGVTLFDNAD
     LLVTANAIDF SNNGTSQCPE HATKVALKVV TPIIISVFVL ALYLHAQQVE STARLDFLWK
     LQATEEKEEM EELQAYNRRL LHNILPKDVA AHFLARERRN DELYYQSCEC VAVMFASIAN
     FSEFYVELEA NNEGVECLRL LNEIIADFDE IISEDRFRQL EKIKTIGSTY MAASGLNDST
     YDKAGKTHIK AIADFAMKLM DQMKYINEHS FNNFQMKIGL NIGPVVAGVI GARKPQYDIW
     GNTVNVASRM DSTGVPDRIQ VTTDMYQVLA ANTYQLECRG VVKVKGKGEM MTYFLNGGPP
     LS
//
ID   CADH8_MOUSE             Reviewed;         799 AA.
AC   P97291;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   08-FEB-2011, entry version 84.
DE   RecName: Full=Cadherin-8;
DE   Flags: Precursor;
GN   Name=Cdh8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster / NIH;
RX   MEDLINE=97174321; PubMed=9022055;
RX   DOI=10.1002/(SICI)1097-0177(199702)208:2<178::AID-AJA5>3.0.CO;2-F;
RA   Korematsu K., Redies C.;
RT   "Restricted expression of cadherin-8 in segmental and functional
RT   subdivisions of the embryonic mouse brain.";
RL   Dev. Dyn. 208:178-189(1997).
CC   -!- FUNCTION: Cadherins are calcium dependent cell adhesion proteins.
CC       They preferentially interact with themselves in a homophilic
CC       manner in connecting cells; cadherins may thus contribute to the
CC       sorting of heterogeneous cell types.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- SIMILARITY: Contains 5 cadherin domains.
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DR   EMBL; X95600; CAA64857.1; -; mRNA.
DR   IPI; IPI00122979; -.
DR   UniGene; Mm.441131; -.
DR   PDB; 1ZXK; X-ray; 2.00 A; A/B=63-159.
DR   PDB; 2A62; X-ray; 4.50 A; A=63-383.
DR   PDBsum; 1ZXK; -.
DR   PDBsum; 2A62; -.
DR   ProteinModelPortal; P97291; -.
DR   SMR; P97291; 62-608, 695-793.
DR   DIP; DIP-46028N; -.
DR   STRING; P97291; -.
DR   PhosphoSite; P97291; -.
DR   PRIDE; P97291; -.
DR   Ensembl; ENSMUST00000067860; ENSMUSP00000068248; ENSMUSG00000036510.
DR   UCSC; uc009mzo.1; mouse.
DR   MGI; MGI:107434; Cdh8.
DR   eggNOG; roNOG12427; -.
DR   GeneTree; ENSGT00590000082742; -.
DR   HOGENOM; HBG505775; -.
DR   HOVERGEN; HBG005217; -.
DR   InParanoid; P97291; -.
DR   Bgee; P97291; -.
DR   CleanEx; MM_CDH8; -.
DR   Genevestigator; P97291; -.
DR   GermOnline; ENSMUSG00000036510; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 5.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF01049; Cadherin_C; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 5.
DR   SUPFAM; SSF49313; Cadherin; 5.
DR   PROSITE; PS00232; CADHERIN_1; 3.
DR   PROSITE; PS50268; CADHERIN_2; 5.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Cell adhesion; Cell membrane;
KW   Cleavage on pair of basic residues; Glycoprotein; Membrane; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     29       Potential.
FT   PROPEP       30     61       Potential.
FT                                /FTId=PRO_0000003775.
FT   CHAIN        62    799       Cadherin-8.
FT                                /FTId=PRO_0000003776.
FT   TOPO_DOM     62    621       Extracellular (Potential).
FT   TRANSMEM    622    642       Helical; (Potential).
FT   TOPO_DOM    643    799       Cytoplasmic (Potential).
FT   DOMAIN       62    167       Cadherin 1.
FT   DOMAIN      168    276       Cadherin 2.
FT   DOMAIN      277    391       Cadherin 3.
FT   DOMAIN      392    494       Cadherin 4.
FT   DOMAIN      495    616       Cadherin 5.
FT   CARBOHYD    188    188       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    463    463       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    473    473       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    544    544       N-linked (GlcNAc...) (Potential).
FT   STRAND       67     70
FT   HELIX        72     74
FT   STRAND       76     78
FT   STRAND       80     84
FT   STRAND       96    102
FT   TURN        106    108
FT   STRAND      109    111
FT   TURN        113    115
FT   STRAND      117    120
FT   TURN        126    128
FT   STRAND      130    140
FT   TURN        141    143
FT   STRAND      146    148
FT   STRAND      151    157
FT   STRAND      168    176
FT   STRAND      197    199
FT   STRAND      205    211
FT   TURN        213    215
FT   STRAND      216    218
FT   TURN        220    222
FT   STRAND      225    227
FT   HELIX       234    236
FT   STRAND      238    249
FT   STRAND      251    254
FT   STRAND      260    266
FT   STRAND      279    285
FT   STRAND      294    299
FT   HELIX       306    308
FT   STRAND      312    315
FT   STRAND      322    324
FT   TURN        330    332
FT   STRAND      333    339
FT   STRAND      350    358
FT   STRAND      377    382
SQ   SEQUENCE   799 AA;  88200 MW;  0E35FEAD563C7F76 CRC64;
     MPERLAETLM DLWTPLIILW ITLPSCVYTA PMNQAHVLTT GSPLELSRQS EDMRILSRSK
     RGWVWNQMFV LEEFSGPEPI LVGRLHTDLD PGSKKIKYIL SGDGAGTIFQ INDITGDIHA
     IKRLDREEKA EYTLTAQAVD FETNKPLEPP SEFIIKVQDI NDNAPEFLNG PYHATVPEMS
     ILGTSVTNVT ATDADDPVYG NSAKLVYSIL EGQPYFSIEP ETAIIKTALP NMDREAKEEY
     LVVIQAIDMG GHSGGLSGTT TLTVTLTDVN DNPPKFAQSL YHFSVPEDVV LGTAIGRVKA
     NDQDIGENAQ SSYDIIDGDG TALFEITSDA QAQDGVIRLR KPLDFETKKS YTLKVEAANI
     HIDPRFSSRG PFKDTATVKI VVEDADEPPV FSSPTYLLEV HENAALNSVI GQVTARDPDI
     TSSPIRFSID RHTDLERQFN INADDGKITL ATPLDRELSV WHNITIIATE IRNHSQISRV
     PVAIKVLDVN DNAPEFASEY EAFLCENGKP GQVIQTVSAM DKDDPKNGHF FLYSLLPEMV
     NNPNFTIKKN EDNSLSILAK HNGFNRQKQE VYLLPIVISD SGNPPLSSTS TLTIRVCGCS
     NDGVVQSCNV EAYVLPIGLS MGALIAILAC IILLLVIVVL FVTLRRHKNE PLIIKDDEDV
     RENIIRYDDE GGGEEDTEAF DIATLQNPDG INGFLPRKDI KPDLQFMPRQ GLAPVPNGVD
     VDEFINVRLH EADNDPTAPP YDSIQIYGYE GRGSVAGSLS SLESTTSDSD QNFDYLSDWG
     PRFKRLGELY SVGESDKET
//
ID   HRH2_MOUSE              Reviewed;         358 AA.
AC   P97292;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Histamine H2 receptor;
DE            Short=H2R;
DE            Short=HH2R;
DE   AltName: Full=Gastric receptor I;
GN   Name=Hrh2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Ola;
RX   MEDLINE=97092891; PubMed=8938453; DOI=10.1006/geno.1996.0575;
RA   Kobayashi T., Inoue I., Jenkins N.A., Gilbert D.J., Copeland N.G.,
RA   Watanabe T.;
RT   "Cloning, RNA expression, and chromosomal location of a mouse
RT   histamine H2 receptor gene.";
RL   Genomics 37:390-394(1996).
CC   -!- FUNCTION: The H2 subclass of histamine receptors mediates gastric
CC       acid secretion. The activity of this receptor is mediated by G
CC       proteins which activate adenylyl cyclase.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; D50096; BAA08792.1; -; Genomic_DNA.
DR   IPI; IPI00467449; -.
DR   UniGene; Mm.57243; -.
DR   ProteinModelPortal; P97292; -.
DR   SMR; P97292; 19-303.
DR   STRING; P97292; -.
DR   PRIDE; P97292; -.
DR   Ensembl; ENSMUST00000038101; ENSMUSP00000038170; ENSMUSG00000034987.
DR   MGI; MGI:108482; Hrh2.
DR   eggNOG; roNOG12936; -.
DR   HOVERGEN; HBG106962; -.
DR   InParanoid; P97292; -.
DR   OrthoDB; EOG418BP4; -.
DR   ArrayExpress; P97292; -.
DR   Bgee; P97292; -.
DR   CleanEx; MM_HRH2; -.
DR   Genevestigator; P97292; -.
DR   GermOnline; ENSMUSG00000034987; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004969; F:histamine receptor activity; IEA:InterPro.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR000503; Histamine_H2_recept.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00531; HISTAMINEH2R.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Lipoprotein; Membrane; Palmitate; Receptor; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    358       Histamine H2 receptor.
FT                                /FTId=PRO_0000069685.
FT   TOPO_DOM      1     22       Extracellular (Potential).
FT   TRANSMEM     23     44       Helical; Name=1; (Potential).
FT   TOPO_DOM     45     57       Cytoplasmic (Potential).
FT   TRANSMEM     58     81       Helical; Name=2; (Potential).
FT   TOPO_DOM     82     92       Extracellular (Potential).
FT   TRANSMEM     93    114       Helical; Name=3; (Potential).
FT   TOPO_DOM    115    134       Cytoplasmic (Potential).
FT   TRANSMEM    135    159       Helical; Name=4; (Potential).
FT   TOPO_DOM    160    179       Extracellular (Potential).
FT   TRANSMEM    180    203       Helical; Name=5; (Potential).
FT   TOPO_DOM    204    233       Cytoplasmic (Potential).
FT   TRANSMEM    234    257       Helical; Name=6; (Potential).
FT   TOPO_DOM    258    266       Extracellular (Potential).
FT   TRANSMEM    267    288       Helical; Name=7; (Potential).
FT   TOPO_DOM    289    358       Cytoplasmic (Potential).
FT   SITE         98     98       Essential for histamine binding (By
FT                                similarity).
FT   SITE        185    185       Essential for tiotidine binding and
FT                                implicated in histamine binding (By
FT                                similarity).
FT   SITE        189    189       Implicated in histamine binding (By
FT                                similarity).
FT   LIPID       304    304       S-palmitoyl cysteine (By similarity).
FT   CARBOHYD      4      4       N-linked (GlcNAc...) (Potential).
FT   DISULFID     91    173       By similarity.
SQ   SEQUENCE   358 AA;  40379 MW;  D3DBA81D71B6D927 CRC64;
     MEPNGTVHSC CLDSIALKVT ISVVLTTLIF ITVAGNVVVC LAVSLNRRLR SLTNCFIVSL
     AATDLLLGLL VMPFSAIYQL SFKWRFGQVF CNIYTSLDVM LCTASILNLF MISLDRYCAV
     TDPLRYPVLV TPVRVAISLV FIWVISITLS FLSIHLGWNS RNGTRGGNDT FKCKVQVNEV
     YGLVDGMVTF YLPLLIMCVT YYRIFKIARE QAKRINHISS WKAATIREHK ATVTLAAVMG
     AFIVCWFPYF TAFVYRGLRG DDPVNEVVEG IVLWLGYANS ALNPILYATL NRDFRMAYQQ
     LFHCKLASHN SHKTSLRLNN SLLSRSQSRE GRWQEEKPLK LQVWSGTELT HPQGSPVR
//
ID   STAC_MOUSE              Reviewed;         403 AA.
AC   P97306;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   30-NOV-2010, entry version 87.
DE   RecName: Full=SH3 and cysteine-rich domain-containing protein;
DE   AltName: Full=Src homology 3 and cysteine-rich domain-containing protein;
GN   Name=Stac;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C3H; TISSUE=Brain;
RX   MEDLINE=97115677; PubMed=8954993; DOI=10.1006/bbrc.1996.1900;
RA   Suzuki H., Kawai J., Taga C., Yaoi T., Hara A., Hirose K.,
RA   Hayashizaki Y., Watanabe S.;
RT   "Stac, a novel neuron-specific protein with cysteine-rich and SH3
RT   domains.";
RL   Biochem. Biophys. Res. Commun. 229:902-909(1996).
CC   -!- FUNCTION: Probably involved in a neuron-specific signal
CC       transduction.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in brain and neurons,
CC       more specifically in hippocampus, cerebellum and inferior olive.
CC       Weak expression is found in heart, liver, lung and kidney. Found
CC       as well in some cell lines.
CC   -!- DEVELOPMENTAL STAGE: Expression in brain started at late E13.5 and
CC       continued to adult (8W) with a peak around P10.
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; D86639; BAA13151.1; -; mRNA.
DR   IPI; IPI00123848; -.
DR   PIR; JC5269; JC5269.
DR   RefSeq; NP_058549.1; NM_016853.2.
DR   UniGene; Mm.1414; -.
DR   ProteinModelPortal; P97306; -.
DR   SMR; P97306; 103-164, 289-343, 348-403.
DR   STRING; P97306; -.
DR   PRIDE; P97306; -.
DR   Ensembl; ENSMUST00000035083; ENSMUSP00000035083; ENSMUSG00000032502.
DR   GeneID; 20840; -.
DR   KEGG; mmu:20840; -.
DR   UCSC; uc009rvw.1; mouse.
DR   CTD; 20840; -.
DR   MGI; MGI:1201400; Stac.
DR   eggNOG; roNOG14988; -.
DR   HOGENOM; HBG716103; -.
DR   HOVERGEN; HBG017859; -.
DR   InParanoid; P97306; -.
DR   OMA; KSADNFF; -.
DR   PhylomeDB; P97306; -.
DR   NextBio; 299589; -.
DR   ArrayExpress; P97306; -.
DR   Bgee; P97306; -.
DR   CleanEx; MM_STAC; -.
DR   Genevestigator; P97306; -.
DR   GermOnline; ENSMUSG00000032502; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0034605; P:cellular response to heat; IDA:MGI.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR013315; Spectrin_alpha_SH3.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR01887; SPECTRNALPHA.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Metal-binding; SH3 domain; Zinc; Zinc-finger.
FT   CHAIN         1    403       SH3 and cysteine-rich domain-containing
FT                                protein.
FT                                /FTId=PRO_0000072236.
FT   DOMAIN      286    345       SH3.
FT   ZN_FING     108    160       Phorbol-ester/DAG-type.
SQ   SEQUENCE   403 AA;  44319 MW;  2B6CAEBFBCFF9982 CRC64;
     MIPPSGARED SGDGLTGEAT GTEQPPSPAS TSSLESKLQK LKRSLSFKTK SLRSKSADNF
     FPRTNSDVKP QADLLAKASP GPSPIAIPGS PASMPTKAGL HPGSNSKLHA FQEHVFKKPT
     FCDVCNHMIV GTHAKHGLRC GACKMSIHHK CADGLAPQRC MGKLPKGFRR YYSSPLLIHE
     QFGCIKEVMP IACGNKVDPV YEALRFGTSL AQRTKKGGSG SGSDSPPRTS TSELVDVPEE
     ADGPGDGSDM RTRSNSVFTY PENGMDDFRD QMKTTNHQGP LSKDPLQMNT YVALYRFIPQ
     ENEDLEMRPG DMITLLEDSN EDWWKGKIQD RVGFFPANFV QRVEEHEKIY RCVRTFIGCK
     DQGQITLKEN QICVTSEEEQ DGFIRVLSGK KRGLVPLDVL VDV
//
ID   CSRP1_MOUSE             Reviewed;         193 AA.
AC   P97315;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Cysteine and glycine-rich protein 1;
DE   AltName: Full=Cysteine-rich protein 1;
DE            Short=CRP;
DE            Short=CRP1;
GN   Name=Csrp1; Synonyms=Crp1, Csrp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C3H;
RA   Hashimoto N., Ogashiwa M.;
RT   "Differential expression of three double LIM proteins during the
RT   skeletal muscle terminal differentiation.";
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10090149;
RX   DOI=10.1002/(SICI)1097-0177(199903)214:3<229::AID-AJA6>3.3.CO;2-J;
RA   Henderson J.R., Macalma T., Brown D., Richardson J.A., Olson E.N.,
RA   Beckerle M.C.;
RT   "The LIM protein, CRP1, is a smooth muscle marker.";
RL   Dev. Dyn. 214:229-238(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 122-131, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-127, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Could play a role in neuronal development (By
CC       similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains 2 LIM zinc-binding domains.
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DR   EMBL; D88793; BAA13723.1; -; mRNA.
DR   EMBL; AF092921; AAD19352.1; -; mRNA.
DR   EMBL; AK077787; BAC37009.1; -; mRNA.
DR   EMBL; AK087436; BAC39873.1; -; mRNA.
DR   EMBL; BC006912; AAH06912.1; -; mRNA.
DR   IPI; IPI00123891; -.
DR   RefSeq; NP_031817.1; NM_007791.5.
DR   UniGene; Mm.196484; -.
DR   ProteinModelPortal; P97315; -.
DR   SMR; P97315; 1-193.
DR   STRING; P97315; -.
DR   PhosphoSite; P97315; -.
DR   PRIDE; P97315; -.
DR   Ensembl; ENSMUST00000027677; ENSMUSP00000027677; ENSMUSG00000026421.
DR   Ensembl; ENSMUST00000097561; ENSMUSP00000095169; ENSMUSG00000026421.
DR   GeneID; 13007; -.
DR   KEGG; mmu:13007; -.
DR   UCSC; uc007cto.1; mouse.
DR   CTD; 13007; -.
DR   MGI; MGI:88549; Csrp1.
DR   eggNOG; roNOG08930; -.
DR   HOGENOM; HBG403138; -.
DR   HOVERGEN; HBG051143; -.
DR   InParanoid; P97315; -.
DR   OMA; ERCPRCT; -.
DR   OrthoDB; EOG4BRWMS; -.
DR   NextBio; 282836; -.
DR   ArrayExpress; P97315; -.
DR   Bgee; P97315; -.
DR   CleanEx; MM_CSRP1; -.
DR   Genevestigator; P97315; -.
DR   GermOnline; ENSMUSG00000026421; Mus musculus.
DR   GO; GO:0015629; C:actin cytoskeleton; TAS:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; TAS:MGI.
DR   InterPro; IPR001781; Znf_LIM.
DR   Gene3D; G3DSA:2.10.110.10; Znf_LIM; 2.
DR   Pfam; PF00412; LIM; 2.
DR   SMART; SM00132; LIM; 2.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; LIM domain; Metal-binding;
KW   Nucleus; Phosphoprotein; Repeat; Zinc.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    193       Cysteine and glycine-rich protein 1.
FT                                /FTId=PRO_0000075716.
FT   DOMAIN       10     61       LIM zinc-binding 1.
FT   DOMAIN      119    170       LIM zinc-binding 2.
FT   MOTIF        64     69       Nuclear localization signal (Potential).
FT   COMPBIAS     63     78       Gly-rich.
FT   COMPBIAS    176    187       Gly-rich.
FT   MOD_RES     112    112       N6-acetyllysine (By similarity).
FT   MOD_RES     127    127       Phosphotyrosine.
FT   MOD_RES     131    131       N6-acetyllysine (By similarity).
FT   MOD_RES     192    192       Phosphoserine.
SQ   SEQUENCE   193 AA;  20583 MW;  AC69703ABD68C97A CRC64;
     MPNWGGGKKC GVCQKTVYFA EEVQCEGNSF HKSCFLCMVC KKNLDSTTVA VHGEEIYCKS
     CYGKKYGPKG YGYGQGAGTL STDKGESLGI KHEEAPGHRP TTNPNASKFA QKIGGSERCP
     RCSQAVYAAE KVIGAGKSWH KSCFRCAKCG KGLESTTLAD KDGEIYCKGC YAKNFGPKGF
     GFGQGAGALV HSE
//
ID   DAB1_MOUSE              Reviewed;         588 AA.
AC   P97318; A2A963; A2A964; A2A965; A2A966; A2A967; A2A970; P97316;
AC   P97317; Q9DAP9;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 2.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Disabled homolog 1;
GN   Name=Dab1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS DAB217; DAB271 AND
RP   DAB555), FUNCTION, SUBUNIT, AND TISSUE SPECIFICITY.
RC   TISSUE=Embryonic brain;
RX   MEDLINE=97162286; PubMed=9009273; DOI=10.1093/emboj/16.1.121;
RA   Howell B.W., Gertler F.B., Cooper J.A.;
RT   "Mouse disabled (mDab1): a Src binding protein implicated in neuronal
RT   development.";
RL   EMBO J. 16:121-132(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM DAB197).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   PHOSPHORYLATION AT TYR-198 AND TYR-220.
RX   MEDLINE=21238270; PubMed=11279201; DOI=10.1074/jbc.M101422200;
RA   Keshvara L., Benhayon D., Magdaleno S., Curran T.;
RT   "Identification of reelin-induced sites of tyrosyl phosphorylation on
RT   disabled 1.";
RL   J. Biol. Chem. 276:16008-16014(2001).
RN   [5]
RP   PHOSPHORYLATION AT SER-524.
RX   MEDLINE=22072265; PubMed=12077184;
RA   Keshvara L., Magdaleno S., Benhayon D., Curran T.;
RT   "Cyclin-dependent kinase 5 phosphorylates disabled 1 independently of
RT   reelin signaling.";
RL   J. Neurosci. 22:4869-4877(2002).
RN   [6]
RP   INTERACTION WITH SIAH1.
RX   PubMed=12646221; DOI=10.1016/S0006-291X(03)00247-X;
RA   Park T.-J., Hamanaka H., Ohshima T., Watanabe N., Mikoshiba K.,
RA   Nukina N.;
RT   "Inhibition of ubiquitin ligase Siah-1A by disabled-1.";
RL   Biochem. Biophys. Res. Commun. 302:671-678(2003).
CC   -!- FUNCTION: Adapter molecule functioning in neural development. May
CC       regulate SIAH1 activity.
CC   -!- SUBUNIT: Interacts with LRP1 (By similarity). Associates with the
CC       SH2 domains of SRC, FYN and ABL. Interacts with DAB2IP and SIAH1.
CC   -!- INTERACTION:
CC       Q03157:Aplp1; NbExp=2; IntAct=EBI-81680, EBI-399929;
CC       Q06335:Aplp2; NbExp=1; IntAct=EBI-81680, EBI-446708;
CC       P12023:App; NbExp=1; IntAct=EBI-81680, EBI-78814;
CC       Q91ZX7:Lrp1; NbExp=1; IntAct=EBI-81680, EBI-300955;
CC       Q8VHR0:Pcdh18; NbExp=2; IntAct=EBI-81680, EBI-399910;
CC       P61092:Siah1a; NbExp=2; IntAct=EBI-81680, EBI-446761;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=DAB588;
CC         IsoId=P97318-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=DAB197;
CC         IsoId=P97318-4; Sequence=VSP_026205, VSP_003841, VSP_003842;
CC         Note=No experimental confirmation available;
CC       Name=DAB204;
CC         IsoId=P97318-5; Sequence=VSP_026208, VSP_026209;
CC         Note=No experimental confirmation available;
CC       Name=DAB217;
CC         IsoId=P97318-6; Sequence=VSP_003841, VSP_003842;
CC       Name=DAB271;
CC         IsoId=P97318-3; Sequence=VSP_003843, VSP_003844, VSP_003845;
CC       Name=DAB553;
CC         IsoId=P97318-8; Sequence=VSP_026206;
CC         Note=No experimental confirmation available;
CC       Name=DAB555;
CC         IsoId=P97318-2; Sequence=VSP_003843;
CC   -!- TISSUE SPECIFICITY: Expressed mainly in brain.
CC   -!- DOMAIN: The PID domain specifically binds to the Asn-Pro-Xaa-
CC       Tyr(P) motif found in many tyrosine-phosphorylated proteins.
CC   -!- PTM: Phosphorylated on Tyr-198 and Tyr-220 upon reelin induction
CC       in embryonic neurons. Also phosphorylated on Ser-524 independently
CC       of reelin signaling.
CC   -!- SIMILARITY: Contains 1 PID domain.
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DR   EMBL; Y08380; CAA69663.1; -; mRNA.
DR   EMBL; Y08379; CAA69662.1; -; mRNA.
DR   EMBL; Y08381; CAA69664.1; -; mRNA.
DR   EMBL; Y08383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK005640; BAB24163.1; -; mRNA.
DR   EMBL; AL627134; CAM26758.1; -; Genomic_DNA.
DR   EMBL; AL645483; CAM26758.1; JOINED; Genomic_DNA.
DR   EMBL; AL627134; CAM26759.1; -; Genomic_DNA.
DR   EMBL; AL645483; CAM26759.1; JOINED; Genomic_DNA.
DR   EMBL; AL669938; CAM26759.1; JOINED; Genomic_DNA.
DR   EMBL; AL627134; CAM26760.1; -; Genomic_DNA.
DR   EMBL; AL645483; CAM26760.1; JOINED; Genomic_DNA.
DR   EMBL; AL669938; CAM26760.1; JOINED; Genomic_DNA.
DR   EMBL; AL627134; CAM26762.1; -; Genomic_DNA.
DR   EMBL; AL645483; CAM26762.1; JOINED; Genomic_DNA.
DR   EMBL; AL669938; CAM26762.1; JOINED; Genomic_DNA.
DR   EMBL; AL627134; CAM26765.1; -; Genomic_DNA.
DR   EMBL; AL645483; CAM26765.1; JOINED; Genomic_DNA.
DR   EMBL; AL669938; CAM26765.1; JOINED; Genomic_DNA.
DR   EMBL; AL645483; CAM17685.1; -; Genomic_DNA.
DR   EMBL; AL627134; CAM17685.1; JOINED; Genomic_DNA.
DR   EMBL; AL645483; CAM17686.1; -; Genomic_DNA.
DR   EMBL; AL627134; CAM17686.1; JOINED; Genomic_DNA.
DR   EMBL; AL669938; CAM17686.1; JOINED; Genomic_DNA.
DR   EMBL; AL645483; CAM17687.1; -; Genomic_DNA.
DR   EMBL; AL627134; CAM17687.1; JOINED; Genomic_DNA.
DR   EMBL; AL669938; CAM17687.1; JOINED; Genomic_DNA.
DR   EMBL; AL645483; CAM17689.1; -; Genomic_DNA.
DR   EMBL; AL627134; CAM17689.1; JOINED; Genomic_DNA.
DR   EMBL; AL669938; CAM17689.1; JOINED; Genomic_DNA.
DR   EMBL; AL645483; CAM17690.1; -; Genomic_DNA.
DR   EMBL; AL627134; CAM17690.1; JOINED; Genomic_DNA.
DR   EMBL; AL669938; CAM17690.1; JOINED; Genomic_DNA.
DR   EMBL; AL669938; CAM19059.1; -; Genomic_DNA.
DR   EMBL; AL627134; CAM19059.1; JOINED; Genomic_DNA.
DR   EMBL; AL645483; CAM19059.1; JOINED; Genomic_DNA.
DR   EMBL; AL669938; CAM19060.1; -; Genomic_DNA.
DR   EMBL; AL627134; CAM19060.1; JOINED; Genomic_DNA.
DR   EMBL; AL645483; CAM19060.1; JOINED; Genomic_DNA.
DR   EMBL; AL669938; CAM19062.1; -; Genomic_DNA.
DR   EMBL; AL627134; CAM19062.1; JOINED; Genomic_DNA.
DR   EMBL; AL645483; CAM19062.1; JOINED; Genomic_DNA.
DR   EMBL; AL669938; CAM19063.1; -; Genomic_DNA.
DR   EMBL; AL627134; CAM19063.1; JOINED; Genomic_DNA.
DR   EMBL; AL645483; CAM19063.1; JOINED; Genomic_DNA.
DR   IPI; IPI00123898; -.
DR   IPI; IPI00230573; -.
DR   IPI; IPI00230574; -.
DR   IPI; IPI00230575; -.
DR   IPI; IPI00750727; -.
DR   IPI; IPI00849536; -.
DR   IPI; IPI00850021; -.
DR   RefSeq; NP_034144.1; NM_010014.2.
DR   RefSeq; NP_796233.2; NM_177259.3.
DR   UniGene; Mm.289682; -.
DR   PDB; 1NTV; X-ray; 1.50 A; A=23-174.
DR   PDB; 1NU2; X-ray; 1.90 A; A=23-174.
DR   PDB; 1OQN; X-ray; 2.30 A; A/B=25-183.
DR   PDBsum; 1NTV; -.
DR   PDBsum; 1NU2; -.
DR   PDBsum; 1OQN; -.
DR   ProteinModelPortal; P97318; -.
DR   SMR; P97318; 23-174.
DR   IntAct; P97318; 18.
DR   MINT; MINT-258594; -.
DR   STRING; P97318; -.
DR   PhosphoSite; P97318; -.
DR   PRIDE; P97318; -.
DR   Ensembl; ENSMUST00000030244; ENSMUSP00000030244; ENSMUSG00000028519.
DR   Ensembl; ENSMUST00000080139; ENSMUSP00000079036; ENSMUSG00000028519.
DR   Ensembl; ENSMUST00000106825; ENSMUSP00000102438; ENSMUSG00000028519.
DR   Ensembl; ENSMUST00000106830; ENSMUSP00000102443; ENSMUSG00000028519.
DR   GeneID; 13131; -.
DR   KEGG; mmu:13131; -.
DR   UCSC; uc008txu.1; mouse.
DR   UCSC; uc008txw.1; mouse.
DR   CTD; 13131; -.
DR   MGI; MGI:108554; Dab1.
DR   eggNOG; roNOG10825; -.
DR   GeneTree; ENSGT00520000055585; -.
DR   HOVERGEN; HBG018945; -.
DR   InParanoid; P97318; -.
DR   OrthoDB; EOG4TB4BG; -.
DR   NextBio; 283176; -.
DR   ArrayExpress; P97318; -.
DR   Bgee; P97318; -.
DR   CleanEx; MM_DAB1; -.
DR   Genevestigator; P97318; -.
DR   GermOnline; ENSMUSG00000028519; Mus musculus.
DR   GO; GO:0005622; C:intracellular; TAS:UniProtKB.
DR   GO; GO:0005543; F:phospholipid binding; TAS:UniProtKB.
DR   GO; GO:0042169; F:SH2 domain binding; TAS:UniProtKB.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0021813; P:cell-cell adhesion involved in neuronal-glial interactions involved in cerebral cortex radial glia guided migration; IMP:MGI.
DR   GO; GO:0021589; P:cerebellum structural organization; IMP:MGI.
DR   GO; GO:0007243; P:intracellular protein kinase cascade; TAS:UniProtKB.
DR   GO; GO:0007162; P:negative regulation of cell adhesion; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0045860; P:positive regulation of protein kinase activity; IGI:MGI.
DR   GO; GO:0021942; P:radial glia guided migration of Purkinje cell; IMP:MGI.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IMP:MGI.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00640; PID; 1.
DR   SMART; SM00462; PTB; 1.
DR   PROSITE; PS01179; PID; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Developmental protein;
KW   Differentiation; Neurogenesis; Phosphoprotein.
FT   CHAIN         1    588       Disabled homolog 1.
FT                                /FTId=PRO_0000079769.
FT   DOMAIN       36    189       PID.
FT   MOD_RES     198    198       Phosphotyrosine.
FT   MOD_RES     220    220       Phosphotyrosine.
FT   MOD_RES     524    524       Phosphoserine; by CDK5.
FT   VAR_SEQ       2     23       STETELQVAVKTSAKKDSRKKG -> LC (in isoform
FT                                DAB197).
FT                                /FTId=VSP_026205.
FT   VAR_SEQ     187    221       Missing (in isoform DAB553).
FT                                /FTId=VSP_026206.
FT   VAR_SEQ     200    217       YIVFEAGHEPIRDPETEE -> VISEPRQGFACSCEGSFD
FT                                (in isoform DAB197 and isoform DAB217).
FT                                /FTId=VSP_003841.
FT   VAR_SEQ     200    204       YIVFE -> NLQKN (in isoform DAB204).
FT                                /FTId=VSP_026208.
FT   VAR_SEQ     205    588       Missing (in isoform DAB204).
FT                                /FTId=VSP_026209.
FT   VAR_SEQ     218    588       Missing (in isoform DAB197 and isoform
FT                                DAB217).
FT                                /FTId=VSP_003842.
FT   VAR_SEQ     240    272       Missing (in isoform DAB555 and isoform
FT                                DAB271).
FT                                /FTId=VSP_003843.
FT   VAR_SEQ     275    304       AVTQLELFGDMSTPPDITSPPTPATPGDAF -> SLVQSPA
FT                                AERAEAESRTGPAEPGSILRPLG (in isoform
FT                                DAB271).
FT                                /FTId=VSP_003844.
FT   VAR_SEQ     305    588       Missing (in isoform DAB271).
FT                                /FTId=VSP_003845.
FT   CONFLICT     29     29       A -> R (in Ref. 2; BAB24163).
FT   CONFLICT    239    239       P -> PVS (in Ref. 3; CAM17685/CAM26758).
FT   CONFLICT    248    248       E -> D (in Ref. 3; CAM17685/CAM26758).
FT   HELIX        28     35
FT   STRAND       40     51
FT   STRAND       53     55
FT   HELIX        58     76
FT   TURN         77     79
FT   STRAND       83     90
FT   STRAND       93     98
FT   TURN         99    101
FT   STRAND      104    108
FT   HELIX       110    112
FT   STRAND      113    118
FT   STRAND      125    132
FT   STRAND      137    145
FT   HELIX       148    166
FT   HELIX       170    173
SQ   SEQUENCE   588 AA;  63578 MW;  08404220792B1DB4 CRC64;
     MSTETELQVA VKTSAKKDSR KKGQDRSEAT LIKRFKGEGV RYKAKLIGID EVSAARGDKL
     CQDSMMKLKG VVAGARSKGE HKQKIFLTIS FGGIKIFDEK TGALQHHHAV HEISYIAKDI
     TDHRAFGYVC GKEGNHRFVA IKTAQAAEPV ILDLRDLFQL IYELKQREEL EKKAQKDKQC
     EQAVYQTILE EDVEDPVYQY IVFEAGHEPI RDPETEENIY QVPTSQKKEG VYDVPKSQPN
     SQPLEDFESR FAAATPNRNL SMDFDELLEA TKVSAVTQLE LFGDMSTPPD ITSPPTPATP
     GDAFLPSSSQ TLPGSADVFG SMSFGTAAVP SGYVAMGAVL PSFWGQQPLV QQQIAMGAQP
     PVAQVIPGAQ PIAWGQPGLF PATQQAWPTV AGQFPPAAFM PTQTVMPLAA AMFQGPLTPL
     ATVPGTNDSA RSSPQSDKPR QKMGKESFKD FQMVQPPPVP SRKPDQPSLT CTSEAFSSYF
     NKVGVAQDTD DCDDFDISQL NLTPVTSTTP STNSPPTPAP RQSSPSKSSA SHVSDPTADD
     IFEEGFESPS KSEEQEAPDG SQASSTSDPF GEPSGEPSGD NISPQDGS
//
ID   S10AD_MOUSE             Reviewed;          98 AA.
AC   P97352;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Protein S100-A13;
DE   AltName: Full=S100 calcium-binding protein A13;
GN   Name=S100a13;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=97032809; PubMed=8878558; DOI=10.1006/bbrc.1996.1551;
RA   Wicki R., Schaefer B.W., Erne P., Heizmann C.W.;
RT   "Characterization of the human and mouse cDNAs coding for S100A13, a
RT   new member of the S100 protein family.";
RL   Biochem. Biophys. Res. Commun. 227:594-599(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12135982; DOI=10.1083/jcb.200203084;
RA   Prudovsky I., Bagala C., Tarantini F., Mandinova A., Soldi R.,
RA   Bellum S., Maciag T.;
RT   "The intracellular translocation of the components of the fibroblast
RT   growth factor 1 release complex precedes their assembly prior to
RT   export.";
RL   J. Cell Biol. 158:201-208(2002).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12746488; DOI=10.1242/jcs.00471;
RA   Mandinova A., Soldi R., Graziani I., Bagala C., Bellum S.,
RA   Landriscina M., Tarantini F., Prudovsky I., Maciag T.;
RT   "S100A13 mediates the copper-dependent stress-induced release of IL-
RT   1alpha from both human U937 and murine NIH 3T3 cells.";
RL   J. Cell Sci. 116:2687-2696(2003).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH LIPID VESICLES.
RX   PubMed=17991455; DOI=10.1016/j.bbamem.2007.09.007;
RA   Kathir K.M., Ibrahim K., Rajalingam D., Prudovsky I., Yu C.,
RA   Kumar T.K.;
RT   "S100A13-lipid interactions-role in the non-classical release of the
RT   acidic fibroblast growth factor.";
RL   Biochim. Biophys. Acta 1768:3080-3089(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   FUNCTION, INTERACTION WITH SYT1 AND FGF1, COPPER BINDING, AND
RP   IDENTIFICATION IN A COPPER-DEPENDENT MULTIPROTEIN COMPLEX CONTAINING
RP   SYT1; FGF1 AND S100A13.
RX   PubMed=11432880; DOI=10.1074/jbc.M102925200;
RA   Landriscina M., Bagala C., Mandinova A., Soldi R., Micucci I.,
RA   Bellum S., Prudovsky I., Maciag T.;
RT   "Copper induces the assembly of a multiprotein aggregate implicated in
RT   the release of fibroblast growth factor 1 in response to stress.";
RL   J. Biol. Chem. 276:25549-25557(2001).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19233122; DOI=10.1016/j.bbrc.2009.02.061;
RA   Graziani I., Doyle A., Sterling S., Kirov A., Tarantini F.,
RA   Landriscina M., Kumar T.K., Neivandt D., Prudovsky I.;
RT   "Protein folding does not prevent the nonclassical export of FGF1 and
RT   S100A13.";
RL   Biochem. Biophys. Res. Commun. 381:350-354(2009).
RN   [9]
RP   STRUCTURE BY NMR, AND SUBUNIT.
RA   Vaithiyalingam S., Kumar T.K.S., Yu C.;
RT   "Three-dimensional solution structure of S100A13.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- FUNCTION: Plays a role in the export of proteins that lack a
CC       signal peptide and are secreted by an alternative pathway. Binds
CC       two calcium ions per subunit. Binds one copper ion. Binding of one
CC       copper ion does not interfere with calcium binding. Required for
CC       the copper-dependent stress-induced export of IL1A and FGF1. The
CC       calcium-free protein binds to lipid vesicles containing
CC       phosphatidylserine, but not to vesicles containing
CC       phosphatidylcholine.
CC   -!- SUBUNIT: Homodimer. Part of a copper-dependent multiprotein
CC       complex containing S100A13, FGF1 and SYT1. Interacts with FGF1 and
CC       SYT1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Secreted. Note=Secretion is
CC       mediated by exposure to stress and requires copper ions.
CC   -!- SIMILARITY: Belongs to the S-100 family.
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X99921; CAA68189.1; -; mRNA.
DR   EMBL; BC005687; AAH05687.1; -; mRNA.
DR   IPI; IPI00124115; -.
DR   PIR; JC5065; JC5065.
DR   RefSeq; NP_033139.1; NM_009113.3.
DR   UniGene; Mm.6523; -.
DR   PDB; 2CXJ; NMR; -; A/B=1-98.
DR   PDBsum; 2CXJ; -.
DR   ProteinModelPortal; P97352; -.
DR   SMR; P97352; 1-98.
DR   STRING; P97352; -.
DR   TCDB; 9.A.48.1.1; unconventional protein secretion (UPS) system.
DR   PhosphoSite; P97352; -.
DR   PRIDE; P97352; -.
DR   Ensembl; ENSMUST00000048138; ENSMUSP00000047737; ENSMUSG00000042312.
DR   Ensembl; ENSMUST00000107338; ENSMUSP00000102961; ENSMUSG00000042312.
DR   GeneID; 20196; -.
DR   KEGG; mmu:20196; -.
DR   UCSC; uc008qcu.1; mouse.
DR   CTD; 20196; -.
DR   MGI; MGI:109581; S100a13.
DR   eggNOG; roNOG17906; -.
DR   HOGENOM; HBG716817; -.
DR   HOVERGEN; HBG001479; -.
DR   InParanoid; P97352; -.
DR   OMA; FTFAGRE; -.
DR   OrthoDB; EOG4G1MJ0; -.
DR   PhylomeDB; P97352; -.
DR   NextBio; 297759; -.
DR   ArrayExpress; P97352; -.
DR   Bgee; P97352; -.
DR   CleanEx; MM_S100A13; -.
DR   Genevestigator; P97352; -.
DR   GermOnline; ENSMUSG00000042312; Mus musculus.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0050703; P:interleukin-1 alpha secretion; ISS:UniProtKB.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR013787; S100_Ca-bd_sub.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF01023; S_100; 1.
DR   PROSITE; PS00018; EF_HAND_1; FALSE_NEG.
DR   PROSITE; PS50222; EF_HAND_2; FALSE_NEG.
DR   PROSITE; PS00303; S100_CABP; FALSE_NEG.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Copper; Cytoplasm; Lipid-binding;
KW   Metal-binding; Phosphoprotein; Protein transport; Repeat; Secreted;
KW   Transport.
FT   CHAIN         1     98       Protein S100-A13.
FT                                /FTId=PRO_0000144020.
FT   DOMAIN       18     53       EF-hand 1.
FT   CA_BIND      24     37       1 (By similarity).
FT   CA_BIND      64     75       2 (By similarity).
FT   MOD_RES      32     32       Phosphoserine.
FT   HELIX        10     19
FT   HELIX        21     26
FT   STRAND       27     32
FT   HELIX        37     40
FT   HELIX        41     45
FT   HELIX        56     65
FT   TURN         66     68
FT   STRAND       69     74
FT   HELIX        77     80
FT   HELIX        82     93
SQ   SEQUENCE   98 AA;  11158 MW;  0A8CE8DA822BD530 CRC64;
     MAAETLTELE AAIETVVSTF FTFAGREGRK GSLNINEFKE LATQQLPHLL KDVGSLDEKM
     KTLDVNQDSE LRFSEYWRLI GELAKEVRKE KALGIRKK
//
ID   G3BP2_MOUSE             Reviewed;         482 AA.
AC   P97379; Q3UL55; Q9R1B8;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 2.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Ras GTPase-activating protein-binding protein 2;
DE            Short=G3BP-2;
DE   AltName: Full=GAP SH3 domain-binding protein 2;
GN   Name=G3bp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RX   MEDLINE=98236259; PubMed=9575347;
RA   Kennedy D., Wood S.A., Ramsdale T., Tam P.P., Steiner K.A.,
RA   Mattick J.S.;
RT   "Identification of a mouse orthologue of the human ras-GAP-SH3-domain
RT   binding protein and structural confirmation that these proteins
RT   contain an RNA recognition motif.";
RL   Biomed. Pept. Proteins Nucleic Acids 2:93-99(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RA   Kennedy D., Mattick J.S.;
RT   "Characterisation and chromosomal location of G3BP-1 and G3BP-2a/b,
RT   members of a novel SH3 domain-binding and RNA-binding protein family
RT   implicated in signal transduction.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-227, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-227, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225 AND THR-227, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Probable scaffold protein that may be involved in mRNA
CC       transport (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=P97379-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=P97379-2; Sequence=VSP_003606;
CC   -!- SIMILARITY: Contains 1 NTF2 domain.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE26595.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U65313; AAC53553.1; -; mRNA.
DR   EMBL; AF145285; AAD51933.1; -; mRNA.
DR   EMBL; AK145697; BAE26595.1; ALT_INIT; mRNA.
DR   IPI; IPI00124245; -.
DR   IPI; IPI00331295; -.
DR   RefSeq; NP_001074263.1; NM_001080794.1.
DR   RefSeq; NP_001074266.1; NM_001080797.1.
DR   RefSeq; NP_035946.2; NM_011816.3.
DR   UniGene; Mm.290530; -.
DR   UniGene; Mm.473827; -.
DR   ProteinModelPortal; P97379; -.
DR   SMR; P97379; 4-133, 331-411.
DR   STRING; P97379; -.
DR   PhosphoSite; P97379; -.
DR   PRIDE; P97379; -.
DR   Ensembl; ENSMUST00000031352; ENSMUSP00000031352; ENSMUSG00000029405.
DR   Ensembl; ENSMUST00000113127; ENSMUSP00000108752; ENSMUSG00000029405.
DR   GeneID; 23881; -.
DR   KEGG; mmu:23881; -.
DR   UCSC; uc008ycg.1; mouse.
DR   CTD; 23881; -.
DR   MGI; MGI:2442040; G3bp2.
DR   eggNOG; roNOG04257; -.
DR   HOVERGEN; HBG007211; -.
DR   InParanoid; P97379; -.
DR   OMA; ESDNRRI; -.
DR   OrthoDB; EOG4XWFZ0; -.
DR   PhylomeDB; P97379; -.
DR   NextBio; 303611; -.
DR   ArrayExpress; P97379; -.
DR   Bgee; P97379; -.
DR   Genevestigator; P97379; -.
DR   GermOnline; ENSMUSG00000029405; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002075; NTF2.
DR   InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF02136; NTF2; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50177; NTF2_DOMAIN; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Methylation; mRNA transport; Phosphoprotein;
KW   RNA-binding; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    482       Ras GTPase-activating protein-binding
FT                                protein 2.
FT                                /FTId=PRO_0000194801.
FT   DOMAIN       11    133       NTF2.
FT   DOMAIN      331    409       RRM.
FT   COMPBIAS    134    223       Glu-rich.
FT   COMPBIAS    419    479       Gly-rich.
FT   MOD_RES     141    141       Phosphoserine (By similarity).
FT   MOD_RES     149    149       Phosphoserine (By similarity).
FT   MOD_RES     225    225       Phosphoserine.
FT   MOD_RES     227    227       Phosphothreonine.
FT   MOD_RES     235    235       Phosphoserine (By similarity).
FT   MOD_RES     457    457       Omega-N-methylated arginine (By
FT                                similarity).
FT   MOD_RES     468    468       Omega-N-methylated arginine (By
FT                                similarity).
FT   VAR_SEQ     243    275       Missing (in isoform B).
FT                                /FTId=VSP_003606.
FT   CONFLICT    476    482       RFTGQRR -> TLHRTASLKSHCWQFWQWYLTHRVCILVKF
FT                                FWLWNVTQPF (in Ref. 1; AAC53553).
SQ   SEQUENCE   482 AA;  54088 MW;  FB8BC2086123A5CE CRC64;
     MVMEKPSPLL VGREFVRQYY TLLNKAPEYL HRFYGRNSSY VHGGVDASGK PQEAVYGQND
     IHHKVLSLNF SECHTKIRHV DAHATLSDGV VVQVMGLLSN SGQPERKFMQ TFVLAPEGSV
     PNKFYVHNDM FRYEDEVFGD SEPELDEESE DEVEEEQEDR QPSPEPVQEN ANSAYYDAHP
     VTNGIEEPLE ESSHEPEPEP ESETKTEELK PQVEEKHLEE LEEKSATPPP AEPASLPQEP
     PKAFSWASVT SKNLPPSGTV SSSGIPPHVK APVSQPRVDA KPEVQSQPPR VREQRPRERP
     GFPPRGPRPG RGDMEQNDSD NRRIIRYPDS HQLFVGNLPH DIDENELKEF FMSFGNVVEL
     RINTKGVGGK LPNFGFVVFD DSEPVQRILI AKPIMFRGEV RLNVEEKKTR AARERETRGG
     GDDRRDIRRN DRGPGGPRGI VGGGMMRDRD GRGPPPRGGM TQKLGSGRGT GQMEGRFTGQ
     RR
//
ID   DNLI3_MOUSE             Reviewed;        1015 AA.
AC   P97386; P97385;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=DNA ligase 3;
DE            EC=6.5.1.1;
DE   AltName: Full=DNA ligase III;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP] 3;
GN   Name=Lig3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
RC   TISSUE=Testis;
RX   MEDLINE=97154534; PubMed=9001252;
RA   Mackey Z.B., Ramos W., Levin D.S., Walter C.A., McCarrey J.R.,
RA   Tomkinson A.E.;
RT   "An alternative splicing event which occurs in mouse pachytene
RT   spermatocytes generates a form of DNA ligase III with distinct
RT   biochemical properties that may function in meiotic recombination.";
RL   Mol. Cell. Biol. 17:989-998(1997).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-210, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: The alpha isoform interacts with DNA-repair protein
CC       XRCC1 and can correct defective DNA strand-break repair and sister
CC       chromatid exchange following treatment with ionizing radiation and
CC       alkylating agents. The beta isoform does not interact with XRCC1
CC       and may be specifically involved in the completion of homologous
CC       recombination events that occur during meiotic prophase.
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) +
CC       (deoxyribonucleotide)(m) = AMP + diphosphate +
CC       (deoxyribonucleotide)(n+m).
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Alpha;
CC         IsoId=P97386-1; Sequence=Displayed;
CC       Name=Beta;
CC         IsoId=P97386-2; Sequence=VSP_001303;
CC   -!- TISSUE SPECIFICITY: The alpha isoform is expressed in all tissues,
CC       while the beta isoform is expressed only in the testis.
CC   -!- DEVELOPMENTAL STAGE: During male germ cell differentiation,
CC       expression of the beta isoform begins in the later stages of
CC       meiotic prophase and ends in the round spermatid stage.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC   -!- SIMILARITY: Contains 1 BRCT domain.
CC   -!- SIMILARITY: Contains 1 PARP-type zinc finger.
CC   -----------------------------------------------------------------------
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DR   EMBL; U66058; AAC53004.1; -; mRNA.
DR   EMBL; U66057; AAC53003.1; -; mRNA.
DR   IPI; IPI00124272; -.
DR   IPI; IPI00230471; -.
DR   UniGene; Mm.277136; -.
DR   UniGene; Mm.413071; -.
DR   ProteinModelPortal; P97386; -.
DR   SMR; P97386; 89-205, 259-838, 929-1015.
DR   STRING; P97386; -.
DR   PhosphoSite; P97386; -.
DR   PRIDE; P97386; -.
DR   Ensembl; ENSMUST00000021039; ENSMUSP00000021039; ENSMUSG00000020697.
DR   Ensembl; ENSMUST00000108174; ENSMUSP00000103809; ENSMUSG00000020697.
DR   MGI; MGI:109152; Lig3.
DR   GeneTree; ENSGT00600000084443; -.
DR   HOGENOM; HBG357148; -.
DR   HOVERGEN; HBG005515; -.
DR   InParanoid; P97386; -.
DR   OrthoDB; EOG44BB1K; -.
DR   PhylomeDB; P97386; -.
DR   BRENDA; 6.5.1.1; 244.
DR   ArrayExpress; P97386; -.
DR   Bgee; P97386; -.
DR   CleanEx; MM_LIG3; -.
DR   Genevestigator; P97386; -.
DR   GermOnline; ENSMUSG00000020697; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   InterPro; IPR001357; BRCT.
DR   InterPro; IPR000977; DNA_ligase_ATP-dep.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR016059; DNA_ligase_ATP-dep_CS.
DR   InterPro; IPR012308; DNA_ligase_ATP-dep_N.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR016027; NA-bd_OB-fold-like.
DR   InterPro; IPR001510; Znf_PARP.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   Gene3D; G3DSA:3.30.1740.10; Znf_PARP; 1.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   Pfam; PF00645; zf-PARP; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SUPFAM; SSF52113; BRCT; 1.
DR   SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1.
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
DR   PROSITE; PS00347; PARP_ZN_FINGER_1; 1.
DR   PROSITE; PS50064; PARP_ZN_FINGER_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Cell cycle;
KW   Cell division; DNA damage; DNA recombination; DNA repair;
KW   DNA replication; Ligase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Zinc; Zinc-finger.
FT   CHAIN         1   1015       DNA ligase 3.
FT                                /FTId=PRO_0000059575.
FT   DOMAIN      939   1015       BRCT.
FT   ZN_FING      94    186       PARP-type.
FT   ACT_SITE    512    512       N6-AMP-lysine intermediate (By
FT                                similarity).
FT   METAL       564    564       Magnesium 1 (By similarity).
FT   METAL       659    659       Magnesium 2 (By similarity).
FT   BINDING     510    510       ATP (By similarity).
FT   BINDING     517    517       ATP (By similarity).
FT   BINDING     532    532       ATP (By similarity).
FT   BINDING     664    664       ATP (By similarity).
FT   BINDING     675    675       ATP (By similarity).
FT   BINDING     679    679       ATP (By similarity).
FT   MOD_RES     210    210       Phosphothreonine.
FT   MOD_RES     211    211       Phosphoserine (By similarity).
FT   MOD_RES     228    228       Phosphoserine (By similarity).
FT   MOD_RES     244    244       Phosphoserine (By similarity).
FT   MOD_RES     321    321       N6-acetyllysine (By similarity).
FT   VAR_SEQ     939   1015       VLLDVFTGVRLYLPPSTPDFKRLKRYFVAFDGDLVQEFDMG
FT                                SATHVLGNREKNTDAQLVSSEWIWACIRKRRLIAPC -> R
FT                                RRASRQRGRKAMQTGRR (in isoform Beta).
FT                                /FTId=VSP_001303.
SQ   SEQUENCE   1015 AA;  113018 MW;  DE96B81CD9C5FC36 CRC64;
     MTLAFKILFP RNLCALGRKE LCLFPEQNRW AAISQFSQWS ETNLLGGCCL LQRRKPVLAL
     QRGHLRPRAT HLTFWPGSHV GLCTGPCAMA EQRFCVDYAK RGTAGCKKCK EKIVKGVCRI
     GKVVPNPFSE SGGDMKEWYH IKCMFEKLER ARATTKKIED LTELEGWEEL EDNEKEQISQ
     HIADLSSKAA ATPKKKAAVQ AKLTTTGQVT SPVKGASFIT STNPRKFSGF SAAKPNNSEQ
     APSSPAPGTS LSASKCDPKH KDCLLREFRK LCAMVAENPS YNTKTQIIHD FLQKGSTGST
     GDGFHGDVYL TVKLLLPGVI KSVYNLNDKQ IVKLFSRIFN CNPDDMARDL EQGDVSETIR
     IFFEQSKSFP PAAKSLLTIQ EVDAFLLHLS KLTKEDEQQQ ALQDIASRCT ANDLKCIRLI
     KHDLKMNSGA KHVLDALDPN AYEAFKASRN LQDVVERVLH NEQEVEKDPG RRRALRVQAS
     LMTPVQPMLA EACKSIEYAM KKCPNGMFSE IKYDGERVQV HKKGDHFSYF SRSLKPVLPH
     KVAHFKDYIP KAFPGGQSMI LDSEVLLIDN NTGKPLPFGT LGVHKKAAFQ DANLCLFVFD
     CIYFNDVSLM DRPLCERRKF LHDNMVEIRN RIMFSEMKQV TKASDLADMI NRVIREGLEG
     LVLKDVKGTY EPGKRHWLKV KKDYLNEGAM ADTADLVVLG VFLIGQGSKG GMMSIFLMGC
     YDPDSQKWCT VTKCAGGHDD ATLARLQKEL VMVKISKDPS KIPSWLKINK IYYPDFIVPD
     PKKAAVWEIT GAEFSRSEAH TADGISIRFP RCTRIRDDKD WKSATNLPQL KELYQLSKDK
     ADFAVVAGDE ASPTTGGSSG ENEGTAGSAG PCKGPPSKSS ASAKTTEQKL NSPSSRGGIK
     PIPKHSPMKP GEKLAVKSSP VKVGMKRKAT DETPCLKKVL LDVFTGVRLY LPPSTPDFKR
     LKRYFVAFDG DLVQEFDMGS ATHVLGNREK NTDAQLVSSE WIWACIRKRR LIAPC
//
ID   VPS45_MOUSE             Reviewed;         570 AA.
AC   P97390; Q91VK9;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Vacuolar protein sorting-associated protein 45;
DE            Short=mVps45;
GN   Name=Vps45; Synonyms=Vps45a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH STX6.
RC   STRAIN=Swiss albino; TISSUE=Adipocyte;
RX   MEDLINE=97197782; PubMed=9045632; DOI=10.1074/jbc.272.10.6187;
RA   Tellam J.T., James D.E., Stevens T.H., Piper R.C.;
RT   "Identification of a mammalian Golgi Sec1p-like protein, mVps45.";
RL   J. Biol. Chem. 272:6187-6193(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in vesicle-mediated protein trafficking
CC       from the Golgi stack through the trans-Golgi network.
CC   -!- SUBUNIT: Interacts with ZFYVE20 (By similarity). Interacts with
CC       STX6.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral
CC       membrane protein. Endosome membrane; Peripheral membrane protein.
CC       Note=Associated with Golgi/endosomal vesicles and the trans-Golgi
CC       network.
CC   -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family.
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CC   -----------------------------------------------------------------------
DR   EMBL; U66865; AAB37577.1; -; mRNA.
DR   EMBL; BC012691; AAH12691.1; -; mRNA.
DR   EMBL; BC058528; AAH58528.1; -; mRNA.
DR   IPI; IPI00124291; -.
DR   RefSeq; NP_038869.1; NM_013841.3.
DR   UniGene; Mm.263185; -.
DR   ProteinModelPortal; P97390; -.
DR   SMR; P97390; 2-129.
DR   STRING; P97390; -.
DR   PhosphoSite; P97390; -.
DR   PRIDE; P97390; -.
DR   Ensembl; ENSMUST00000015891; ENSMUSP00000015891; ENSMUSG00000015747.
DR   GeneID; 22365; -.
DR   KEGG; mmu:22365; -.
DR   UCSC; uc008qly.1; mouse.
DR   CTD; 22365; -.
DR   MGI; MGI:891965; Vps45.
DR   eggNOG; roNOG05944; -.
DR   HOGENOM; HBG559243; -.
DR   HOVERGEN; HBG059810; -.
DR   InParanoid; P97390; -.
DR   OMA; GTTIHNT; -.
DR   OrthoDB; EOG4H463H; -.
DR   PhylomeDB; P97390; -.
DR   NextBio; 302685; -.
DR   ArrayExpress; P97390; -.
DR   Bgee; P97390; -.
DR   CleanEx; MM_VPS45; -.
DR   Genevestigator; P97390; -.
DR   GermOnline; ENSMUSG00000015747; Mus musculus.
DR   GO; GO:0010008; C:endosome membrane; IDA:MGI.
DR   GO; GO:0000139; C:Golgi membrane; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; IEA:InterPro.
DR   InterPro; IPR001619; Sec1-like.
DR   PANTHER; PTHR11679; Sec1-like; 1.
DR   Pfam; PF00995; Sec1; 1.
DR   SUPFAM; SSF56815; Sec1-like; 1.
PE   1: Evidence at protein level;
KW   Endosome; Golgi apparatus; Membrane; Protein transport; Transport.
FT   CHAIN         1    570       Vacuolar protein sorting-associated
FT                                protein 45.
FT                                /FTId=PRO_0000206313.
FT   CONFLICT     55     55       I -> M (in Ref. 2; AAH12691).
SQ   SEQUENCE   570 AA;  65053 MW;  DA704FDE8469F488 CRC64;
     MNVVFAVKQY ISKMIEDSGP GMKVLLMDKE TTGIVSMVYT QSEILQKEVY LFERIDSQNR
     EIMKHLKAIC FLRPTKENVE YLIQELRRPK YSIYFIYFSN VISKSDVKSL AEADEQEVVA
     EVQEFYGDYI AVNPHLFSLN ILGCCQGRNW DPAQLSRTTQ GLTALLLSLK KCPMIRYQLS
     SEAAKRLGEC VKQVISKEYE LFEFRRTEVP PLLLILDRCD DAITPLLNQW TYQAMVHELL
     GINNNRIDLS RVPGISKDLR EVVLSAENDE FYANNMYLNF AEIGSNIKNL MEDFQKKRPK
     EQQKLESIAD MKAFVENYPQ FKKMSGTVSK HVTVVGELSR LVSERNLLEV SEVEQELACQ
     NDHSSALQNV KRLLQNPKVT EFDAVRLVML YALHYERHSS NSLPGLIVDL RSKGVAEKYR
     KLVSAVVEYG GKRVRGSDLF SPKDAVAITK QFLKGLKGVE NVYTQHQPFL HETLDHLIKG
     RLKENLYPYL GPSTLRDRPQ DIIVFIIGGA TYEEALTVYN LNRTTPGVRI VLGGTTIHNT
     KSFLEEVLAS GLHSRSRESS QATSRSANRR
//
ID   LYST_MOUSE              Reviewed;        3788 AA.
AC   P97412; Q62403; Q8VBS6;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Lysosomal-trafficking regulator;
DE   AltName: Full=Beige protein;
DE   AltName: Full=CHS1 homolog;
GN   Name=Lyst; Synonyms=Bg, Chs1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=97358584; PubMed=9215680; DOI=10.1093/hmg/6.7.1091;
RA   Barbosa M.D.F.S., Barrat F.J., Tchernev V.T., Nguyen Q.A.,
RA   Mishra V.S., Colman S.D., Pastural E., Dufourcq-Lagelouse R.,
RA   Fischer A., Holcombe R.F., Wallace M.R., Brandt S.J.,
RA   De Saint Basile G., Kingsmore S.F.;
RT   "Identification of mutations in two major mRNA isoforms of the
RT   Chediak-Higashi syndrome gene in human and mouse.";
RL   Hum. Mol. Genet. 6:1091-1098(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J;
RX   MEDLINE=96353977; PubMed=8717042; DOI=10.1038/382262a0;
RA   Barbosa M.D.F.S., Nguyen Q.A., Tchernev V.T., Ashley J.A.,
RA   Detter J.C., Blaydes S.M., Brandt S.J., Chotai D., Hodgman C.,
RA   Solari R.C.E.S., Lovett M., Kingsmore S.F.;
RT   "Identification of the homologous beige and Chediak-Higashi syndrome
RT   genes.";
RL   Nature 382:262-265(1996).
RN   [3]
RP   ERRATUM.
RA   Barbosa M.D.F.S., Nguyen Q.A., Tchernev V.T., Ashley J.A.,
RA   Detter J.C., Blaydes S.M., Brandt S.J., Chotai D., Hodgman C.,
RA   Solari R.C.E.S., Lovett M., Kingsmore S.F.;
RL   Nature 385:97-97(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1428-3788 (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   MEDLINE=96259558; PubMed=8673129; DOI=10.1038/ng0796-303;
RA   Perou C.M., Moore K.J., Nagle D.L., Misumi D.J., Woolf E.A.,
RA   McGrail S.H., Holmgren L., Brody T.B., Dussault B.J., Monroe C.A.,
RA   Duyk G.M., Pryor R.J., Li L., Justice M.J., Kaplan J.;
RT   "Identification of the murine beige gene by YAC complementation and
RT   positional cloning.";
RL   Nat. Genet. 13:303-308(1996).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2203 AND SER-2207, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1503; SER-1504 AND
RP   SER-2099, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May be required for sorting endosomal resident proteins
CC       into late multivesicular endosomes by a mechanism involving
CC       microtubules.
CC   -!- SUBUNIT: Interacts with CENPJ, LIP8 and ZNF521 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1;
CC         IsoId=P97412-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P97412-2; Sequence=VSP_006783, VSP_006784;
CC   -!- DISEASE: Note=Defects in Lyst are the cause of beige, an autosomal
CC       recessive disorder characterized by hypopigmentation, bleeding,
CC       immune cell dysfunction, abnormal intracellular transport to and
CC       from the lysosome, and giant inclusion bodies in a variety of cell
CC       types.
CC   -!- SIMILARITY: Contains 1 BEACH domain.
CC   -!- SIMILARITY: Contains 7 WD repeats.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U70015; AAC53011.1; -; mRNA.
DR   EMBL; L77884; AAL40134.1; -; mRNA.
DR   EMBL; U52461; AAB60778.1; -; mRNA.
DR   IPI; IPI00227912; -.
DR   IPI; IPI00399954; -.
DR   PIR; T30851; T30851.
DR   RefSeq; NP_034878.2; NM_010748.2.
DR   UniGene; Mm.342337; -.
DR   ProteinModelPortal; P97412; -.
DR   SMR; P97412; 3000-3409, 3523-3771.
DR   STRING; P97412; -.
DR   PhosphoSite; P97412; -.
DR   PRIDE; P97412; -.
DR   Ensembl; ENSMUST00000050664; ENSMUSP00000059413; ENSMUSG00000019726.
DR   GeneID; 17101; -.
DR   KEGG; mmu:17101; -.
DR   UCSC; uc007pmj.1; mouse.
DR   CTD; 17101; -.
DR   MGI; MGI:107448; Lyst.
DR   eggNOG; roNOG06191; -.
DR   HOVERGEN; HBG006300; -.
DR   OrthoDB; EOG418BMF; -.
DR   NextBio; 291244; -.
DR   ArrayExpress; P97412; -.
DR   Bgee; P97412; -.
DR   CleanEx; MM_LYST; -.
DR   Genevestigator; P97412; -.
DR   GermOnline; ENSMUSG00000019726; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0007596; P:blood coagulation; IMP:MGI.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
DR   GO; GO:0042832; P:defense response to protozoan; IMP:MGI.
DR   GO; GO:0051607; P:defense response to virus; IMP:MGI.
DR   GO; GO:0030595; P:leukocyte chemotaxis; IMP:MGI.
DR   GO; GO:0007040; P:lysosome organization; IMP:MGI.
DR   GO; GO:0033364; P:mast cell secretory granule organization; IMP:MGI.
DR   GO; GO:0032438; P:melanosome organization; IMP:MGI.
DR   GO; GO:0007017; P:microtubule-based process; IMP:MGI.
DR   GO; GO:0002446; P:neutrophil mediated immunity; IMP:MGI.
DR   GO; GO:0055091; P:phospholipid homeostasis; IMP:MGI.
DR   GO; GO:0006644; P:phospholipid metabolic process; IMP:MGI.
DR   GO; GO:0032816; P:positive regulation of natural killer cell activation; IMP:MGI.
DR   GO; GO:0042493; P:response to drug; IMP:MGI.
DR   GO; GO:0033299; P:secretion of lysosomal enzymes; IMP:MGI.
DR   GO; GO:0002456; P:T cell mediated immunity; IMP:MGI.
DR   InterPro; IPR000409; Beige_BEACH.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:1.10.1540.10; Beige_BEACH; 1.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF02138; Beach; 1.
DR   Pfam; PF00400; WD40; 2.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF81837; Beige_BEACH; 1.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS50197; BEACH; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Phosphoprotein; Protein transport;
KW   Repeat; Transport; WD repeat.
FT   CHAIN         1   3788       Lysosomal-trafficking regulator.
FT                                /FTId=PRO_0000051072.
FT   REPEAT      662    700       WD 1.
FT   REPEAT     1576   1620       WD 2.
FT   DOMAIN     3126   3409       BEACH.
FT   REPEAT     3550   3589       WD 3.
FT   REPEAT     3601   3640       WD 4.
FT   REPEAT     3643   3686       WD 5.
FT   REPEAT     3687   3731       WD 6.
FT   REPEAT     3736   3775       WD 7.
FT   MOD_RES    1503   1503       Phosphoserine.
FT   MOD_RES    1504   1504       Phosphoserine.
FT   MOD_RES    2097   2097       Phosphoserine (By similarity).
FT   MOD_RES    2099   2099       Phosphoserine.
FT   MOD_RES    2118   2118       Phosphoserine (By similarity).
FT   MOD_RES    2203   2203       Phosphoserine.
FT   MOD_RES    2207   2207       Phosphoserine.
FT   VAR_SEQ    1509   1545       EGDRPEVTESINPGDRLIEDGCIHLISLGSKALMIQV ->
FT                                GMMAGSDLYTKILQIAACLSFKHIWQYFNVFFKCYSP (in
FT                                isoform 2).
FT                                /FTId=VSP_006783.
FT   VAR_SEQ    1546   3788       Missing (in isoform 2).
FT                                /FTId=VSP_006784.
SQ   SEQUENCE   3788 AA;  425287 MW;  F01BE837C676A750 CRC64;
     MSTDSNSLAR EFLIDVNQLC NAVVQRAEAR EEEEEETHMA TLGQYLVHGR GFLLLTKLNS
     IIDQALTCRE ELLTLLLSLL PLVWKIPVQE QQATDFNLPL SSDIILTKEK NSSLQKSTQG
     KLYLEGSAPS GQVSAKVNLF RKIRRQRKST HRYSVRDARK TQLSTSDSEG NSDEKSTVVS
     KHRRLHALPR FLTQSPKEGH LVAKPDPSAT KEQVLSDTMS VENSREVILR QDSNGDILSE
     PAALSILSNM NNSPFDLCHV LLSLLEKVCK FDIALNHNSS LALSVVPTLT EFLAGFGDCC
     NQSDTLEGQL VSAGWTEEPV ALVQRMLFRT VLHLMSVDVS TAEAMPESLR KNLTELLRAA
     LKIRACLEKQ PEPFSPRQKK TLQEVQEGFV FSKYRHRALL LPELLEGVLQ LLISCLQSAA
     SNPFYFSQAM DLVQEFIQHQ GFNLFGTAVL QMEWLLTRDG VPSEAAEHLK ALINSVIKIM
     STVKKVKSEQ LHHSMCTRKR HRRCEYSHFM QHHRDLSGLL VSAFKNQLSK SPFEETAEGD
     VQYPERCCCI AVCAHQCLRL LQQVSLSTTC VQILSGVHSV GICCCMDPKS VIAPLLHAFK
     LPALKAFQQH ILNVLSKLLV DQLGGAELSP RIKKAACNIC TVDSDQLAKL GETLQGTLCG
     AGPTSGLPSP SYRFQGILPS SGSEDLLWKW DALEAYQSFV FQEDRLHNIQ IANHICNLLQ
     KGNVVVQWKL YNYIFNPVLQ RGVELVHHCQ QLSIPSAQTH MCSQLKQYLP QEVLQIYLKT
     LPVLLKSRVI RDLFLSCNGV NHIIELNYLD GIRSHSLKAF ETLIVSLGEQ QKDAAVLDVD
     GLDIQQELPS LSVGPSLHKQ QASSDSPCSL RKFYASLREP DPKKRKTIHQ DVHINTINLF
     LCVAFLCVSK EADSDRESAN ESEDTSGYDS PPSEPLSHML PCLSLEDVVL PSPECLHHAA
     DIWSMCRWIY MLNSVFQKQF HRLGGFQVCH ELIFMIIQKL FRSHTEDQGR RQGEMSRNEN
     QELIRISYPE LTLKGDVSSA TAPDLGFLRK SADSVRGFQS QPVLPTSAEQ IVATESVPGE
     RKAFMSQQSE TSLQSIRLLE SLLDICLHSA RACQQKMELE LPSQGLSVEN ILCELREHLS
     QSKVAETELA KPLFDALLRV ALGNHSADLG PGDAVTEKSH PSEEELLSQP GDFSEEAEDS
     QCCSLKLLGE EEGYEADSES NPEDVDTQDD GVELNPEAEG FSGSIVSNNL LENLTHGEII
     YPEICMLGLN LLSASKAKLD VLAHVFESFL KIVRQKEKNI SLLIQQGTVK ILLGGFLNIL
     TQTNSDFQAC QRVLVDLLVS LMSSRTCSED LTLLWRIFLE KSPCTEILLL GIHKIVESDF
     TMSPSQCLTF PFLHTPSLSN GVLSQKPPGI LNSKALGLLR RARISRGKKE ADRESFPYRL
     LSSWHIAPIH LPLLGQNCWP HLSEGFSVSL VGLMWNTSNE SESAAERGKR VKKRNKPSVL
     EDSSFEGAEG DRPEVTESIN PGDRLIEDGC IHLISLGSKA LMIQVWADPH SGTFIFRVCM
     DSNDDTKAVS LAQVESQENI FFPSKWQHLV LTYIQHPQGK KNVHGEISIW VSGQRKTDVI
     LDFVLPRKTS LSSDSNKTFC MIGHCLTSQE ESLQLAGKWD LGNLLLFNGA KIGSQEAFFL
     YACGPNYTSI MPCKYGQPVI DYSKYINKDI LRCDEIRDLF MTKKEVDVGL LIESLSVVYT
     TCCPAQYTIY EPVIRLKGQV KTQPSQRPFS SKEAQSILLE PSQLKGLQPT ECKAIQGILH
     EIGGAGTFVF LFARVVELSS CEETQALALR VILSLIKYSQ QRTQELENCN GLSMIHQVLV
     KQKCIVGFHI LKTLLEGCCG EEVIHVSEHG EFKLDVESHA IIQDVKLLQE LLLDWKIWNK
     AEQGVWETLL AALEVLIRVE HHQQQFNIKQ LLNAHVVHHF LLTCQVLQEH REGQLTSMPR
     EVCRSFVKII AEVLGSPPDL ELLTVIFNFL LAVHPPTNTY VCHNPTNFYF SLHIDGKIFQ
     EKVQSLAYLR HSSSGGQAFP SPGFLVISPS AFTAAPPEGT SSSNIVPQRM AAQMVRSRSL
     PAFPTYLPLI RAQKLAASLG FSVDKLQNIA DANPEKQNLL GRPYALKTSK EEAFISSCES
     AKTVCEMEAL LGAHASANGV SRGSPRFPRA RVDHKDVGTE PRSDDDSPGD ESYPRRPDNL
     KGLASFQRSQ STVASLGLAF PSQNGSAVAS RWPSLVDRNA DDWENFTFSP AYEASYNRAT
     STHSVIEDCL IPICCGLYEL LSGVLLVLPD AMLEDVMDRI IQADILLVLV NHPSPAIQQG
     VIKLLHAYIN RASKEQKDKF LKNRGFSLLA NQLYLHRGTQ ELLECFVEMF FGRPIGLDEE
     FDLEEVKHME LFQKWSVIPV LGLIETSLYD NVLLHNALLL LLQVLNSCSK VADMLLDNGL
     LYVLCNTVAA LNGLEKNIPV NEYKLLACDI QQLFIAVTIH ACSSSGTQYF RVIEDLIVLL
     GYLHNSKNKR TQNMALALQL RVLQAALEFI RSTANHDSES PVHSPSAHRH SVPPKRRSIA
     GSRKFPLAQT ESLLMKMRSV ASDELHSMMQ RRMSQEHPSQ ASEAELAQRL QRLTILAVNR
     IIYQELNSDI IDILRTPENT SQSKTSVSQT EISEEDMHHE QPSVYNPFQK EMLTYLLDGF
     KVCIGSSKTS VSKQQWTKIL GSCKETLRDQ LGRLLAHILS PTHTVQERKQ ILEIVHEPAH
     QDILRDCLSP SPQHGAKLVL YLSELIHNHQ DELSEEEMDT AELLMNALKL CGHKCIPPSA
     PSKPELIKII REEQKKYESE ESVSKGSWQK TVNNNQQSLF QRLDFKSKDI SKIAADITQA
     VSLSQGIERK KVIQHIRGMY KVDLSASRHW QECIQQLTHD RAVWYDPIYY PTSWQLDPTE
     GPNRERRRLQ RCYLTIPNKY LLRDRQKSEG VLRPPLSYLF EDKTHSSFSS TVKDKAASES
     IRVNRRCISV APSRETAGEL LLGKCGMYFV EDNASDAVES SSLQGELEPA SFSWTYEEIK
     EVHRRWWQLR DNAVEIFLTN GRTLLLAFDN NKVRDDVYQS ILTNNLPNLL EYGNITALTN
     LWYSGQITNF EYLTHLNKHA GRSFNDLMQY PVFPFILSDY VSETLDLNDP SIYRNLSKPI
     AVQYKEKEDR YVDTYKYLEE EYRKGAREDD PMPPVQPYHY GSHYSNSGTV LHFLVRMPPF
     TKMFLAYQDQ SFDIPDRTFH STNTTWRLSS FESMTDVKEL IPEFFYLPEF LVNREGFDFG
     VRQNGERVNH VNLPPWARND PRLFILIHRQ ALESDHVSQN ICHWIDLVFG YKQKGKASVQ
     AINVFHPATY FGMDVSAVED PVQRRALETM IKTYGQTPRQ LFHTAHASRP GAKLNIEGEL
     PAAVGLLVQF AFRETREPVK EVTHPSPLSW IKGLKWGEYV GSPSAPVPVV CFSQPHGERF
     GSLQALPTRA ICGLSRNFCL LMTYNKEQGV RSMNNTNIQW SAILSWGYAD NILRLKSKQS
     EPPINFIQSS QQHQVTSCAW VPDSCQLFTG SKCGVITAYT NRLTSSTPSE IEMESQMHLY
     GHTEEITGLC VCKPYSVMIS VSRDGTCIVW DLNRLCYVQS LAGHKSPVTA VSASETSGDI
     ATVCDSAGGG SDLRLWTVNG DLVGHVHCRE IICSVAFSNQ PEGVSINVIA GGLENGIVRL
     WSTWDLKPVR EITFPKSNKP IISLTFSCDG HHLYTANSEG TVIAWCRKDQ QRVKLPMFYS
     FLSSYAAG
//
ID   DPYL1_MOUSE             Reviewed;         572 AA.
AC   P97427; O08554; O35097;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   08-FEB-2011, entry version 97.
DE   RecName: Full=Dihydropyrimidinase-related protein 1;
DE            Short=DRP-1;
DE   AltName: Full=Collapsin response mediator protein 1;
DE            Short=CRMP-1;
DE   AltName: Full=Unc-33-like phosphoprotein 3;
DE            Short=ULIP-3;
GN   Name=Crmp1; Synonyms=Dpysl1, Ulip3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=97262103; PubMed=9107681; DOI=10.1007/s003359900438;
RA   Cohen-Salmon M., Crozet F., Rebillard G., Petit C.;
RT   "Cloning and characterization of the mouse collapsin response mediator
RT   protein-1, Crmp1.";
RL   Mamm. Genome 8:349-351(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=98314496; PubMed=9652388;
RX   DOI=10.1046/j.1432-1327.1998.2540014.x;
RA   Byk T., Ozon S., Sobel A.;
RT   "The Ulip family phosphoproteins -- common and specific properties.";
RL   Eur. J. Biochem. 254:14-24(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RA   Hamajima N., Kato Y., Kouwaki M., Wada Y., Sasaski M., Nonaka M.;
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 44-56; 150-159; 190-210; 246-254; 259-268;
RP   346-361; 391-397; 401-416; 452-463 AND 472-481, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Klug S., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   NITRATION [LARGE SCALE ANALYSIS] AT TYR-316, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16800626; DOI=10.1021/bi060474w;
RA   Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
RA   Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
RA   Squier T.C., Bigelow D.J.;
RT   "Endogenously nitrated proteins in mouse brain: links to
RT   neurodegenerative disease.";
RL   Biochemistry 45:8009-8022(2006).
RN   [8]
RP   SUBUNIT.
RX   MEDLINE=20545548; PubMed=10956643; DOI=10.1074/jbc.M003277200;
RA   Fukada M., Watakabe I., Yuasa-Kawada J., Kawachi H., Kuroiwa A.,
RA   Matsuda Y., Noda M.;
RT   "Molecular characterization of CRMP5, a novel member of the collapsin
RT   response mediator protein family.";
RL   J. Biol. Chem. 275:37957-37965(2000).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-431; TYR-504 AND
RP   THR-509, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) OF 8-525, FUNCTION, INTERACTION
RP   WITH PLEXA1, AND SUBUNIT.
RX   PubMed=14685275; DOI=10.1038/sj.emboj.7600021;
RA   Deo R.C., Schmidt E.F., Elhabazi A., Togashi H., Burley S.K.,
RA   Strittmatter S.M.;
RT   "Structural bases for CRMP function in plexin-dependent semaphorin3A
RT   signaling.";
RL   EMBO J. 23:9-22(2004).
CC   -!- FUNCTION: Necessary for signaling by class 3 semaphorins and
CC       subsequent remodeling of the cytoskeleton. Plays a role in axon
CC       guidance, invasive growth and cell migration.
CC   -!- SUBUNIT: Homotetramer, and heterotetramer with DPYSL2, DPYSL3,
CC       DPYSL4 or DPYSL5. Interacts with PLXNA1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytoskeleton, centrosome (By similarity). Cytoplasm, cytoskeleton,
CC       spindle (By similarity). Note=Associated with centrosomes and the
CC       mitotic spindle during metaphase (By similarity).
CC   -!- SIMILARITY: Belongs to the DHOase family.
CC       Hydantoinase/dihydropyrimidinase subfamily.
CC   -!- CAUTION: Lacks most of the conserved residues that are essential
CC       for binding the metal cofactor and hence for dihydropyrimidinase
CC       activity. Its enzyme activity is therefore unsure.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U72875; AAB39703.1; -; mRNA.
DR   EMBL; Y09080; CAA70300.1; -; mRNA.
DR   EMBL; AB006714; BAA21887.1; -; mRNA.
DR   EMBL; BC031738; AAH31738.1; -; mRNA.
DR   IPI; IPI00875117; -.
DR   RefSeq; NP_031791.3; NM_007765.3.
DR   UniGene; Mm.290995; -.
DR   PDB; 1KCX; X-ray; 2.12 A; A/B=8-525.
DR   PDBsum; 1KCX; -.
DR   ProteinModelPortal; P97427; -.
DR   SMR; P97427; 15-490.
DR   STRING; P97427; -.
DR   MEROPS; M38.974; -.
DR   PhosphoSite; P97427; -.
DR   PRIDE; P97427; -.
DR   Ensembl; ENSMUST00000031004; ENSMUSP00000031004; ENSMUSG00000029121.
DR   GeneID; 12933; -.
DR   KEGG; mmu:12933; -.
DR   UCSC; uc008xfm.1; mouse.
DR   CTD; 12933; -.
DR   MGI; MGI:107793; Crmp1.
DR   eggNOG; roNOG05528; -.
DR   GeneTree; ENSGT00550000074371; -.
DR   HOVERGEN; HBG000806; -.
DR   NextBio; 282604; -.
DR   ArrayExpress; P97427; -.
DR   Bgee; P97427; -.
DR   CleanEx; MM_CRMP1; -.
DR   Genevestigator; P97427; -.
DR   GermOnline; ENSMUSG00000029121; Mus musculus.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   InterPro; IPR006680; Amidohydro_1.
DR   InterPro; IPR011778; D-hydantoinase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Metalo_hydrolase; 2.
DR   TIGRFAMs; TIGR02033; D-hydantoinase; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Nitration; Phosphoprotein.
FT   CHAIN         1    572       Dihydropyrimidinase-related protein 1.
FT                                /FTId=PRO_0000165910.
FT   MOD_RES     316    316       Nitrated tyrosine.
FT   MOD_RES     431    431       Phosphotyrosine.
FT   MOD_RES     504    504       Phosphotyrosine.
FT   MOD_RES     509    509       Phosphothreonine.
FT   CONFLICT    338    338       T -> I (in Ref. 2; CAA70300).
FT   CONFLICT    476    476       E -> K (in Ref. 3; BAA21887).
FT   CONFLICT    489    489       F -> S (in Ref. 3; BAA21887).
FT   CONFLICT    520    520       K -> E (in Ref. 2; CAA70300).
FT   STRAND       17     21
FT   STRAND       23     25
FT   STRAND       30     32
FT   STRAND       34     38
FT   STRAND       41     48
FT   STRAND       56     59
FT   STRAND       64     67
FT   STRAND       69     74
FT   HELIX        89     98
FT   STRAND      101    108
FT   HELIX       116    130
FT   STRAND      132    141
FT   HELIX       148    157
FT   STRAND      163    168
FT   TURN        171    174
FT   HELIX       178    190
FT   STRAND      194    198
FT   HELIX       202    214
FT   HELIX       221    226
FT   HELIX       230    246
FT   STRAND      250    255
FT   HELIX       258    270
FT   STRAND      274    279
FT   HELIX       280    284
FT   HELIX       287    291
FT   HELIX       295    300
FT   HELIX       313    322
FT   HELIX       338    341
FT   HELIX       342    344
FT   HELIX       348    350
FT   TURN        358    360
FT   HELIX       361    369
FT   TURN        370    373
FT   HELIX       377    384
FT   HELIX       386    391
FT   TURN        395    397
FT   STRAND      409    419
FT   TURN        422    424
FT   STRAND      426    430
FT   TURN        433    436
FT   STRAND      438    448
FT   STRAND      451    455
FT   HELIX       476    488
SQ   SEQUENCE   572 AA;  62168 MW;  FE17DDCD735CAF8F CRC64;
     MSHQGKKSIP HITSDRLLIR GGRIINDDQS FYADVYLEDG LIKQIGENLI VPGGVKTIEA
     NGRMVIPGGI DVNTYLQKPS QGMTSADDFF QGTKAALAGG TTMIIDHVVP EPGSSLLTSF
     EKWHEAADTK SCCDYSLHVD ITSWYDGVRE ELEVLVQDKG VNSFQVYMAY KDLYQMSDSQ
     LYEAFTFLKG LGAVILVHAE NGDLIAQEQK RILEMGITGP EGHALSRPEE LEAEAVFRAI
     AIAGRINCPV YITKVMSKSA ADIIALARKK GPLVFGEPIA ASLGTDGTHY WSKNWAKAAA
     FVTSPPLSPD PTTPDYLTSL LACGDLQVTG SGHCPYSTAQ KAVGKDNFTL IPEGVNGIEE
     RMTVVWDKAV ATGKMDENQF VAVTSTNAAK IFNLYPRKGR IAVGSDADVV IWDPDKMKTI
     TAKSHKSTVE YNIFEGMECH GSPLVVISQG KIVFEDGNIS VSKGMGRFIP RKPFPEHLYQ
     RVRIRSKVFG LHSVSRGMYD GPVYEVPATP KHAAPAPSAK SSPSKHQPPP IRNLHQSNFS
     LSGAQIDDNN PRRTGHRIVA PPGGRSNITS LG
//
ID   KCNK2_MOUSE             Reviewed;         411 AA.
AC   P97438;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 2.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Potassium channel subfamily K member 2;
DE   AltName: Full=Outward rectifying potassium channel protein TREK-1;
DE   AltName: Full=TREK-1 K(+) channel subunit;
DE   AltName: Full=Two pore potassium channel TPKC1;
GN   Name=Kcnk2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=97157476; PubMed=9003761;
RA   Fink M., Duprat F., Lesage F., Reyes R., Romey G., Heurteaux C.,
RA   Lazdunski M.;
RT   "Cloning, functional expression and brain localization of a novel
RT   unconventional outward rectifier K+ channel.";
RL   EMBO J. 15:6854-6862(1996).
RN   [2]
RP   SEQUENCE REVISION.
RA   Fink M., Duprat F., Lesage F., Reyes R., Romey G., Heurteaux C.,
RA   Lazdunski M.;
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   ACTIVATION.
RX   MEDLINE=99254548; PubMed=10321245; DOI=10.1038/8084;
RA   Patel A.J., Honore E., Lesage F., Fink M., Romey G., Lazdunski M.;
RT   "Inhalational anesthetics activate two-pore-domain background K+
RT   channels.";
RL   Nat. Neurosci. 2:422-426(1999).
CC   -!- FUNCTION: Outward rectifying potassium channel.
CC   -!- SUBUNIT: Homodimer (Potential).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- TISSUE SPECIFICITY: High expression in brain and lung. Also
CC       detected in kidney, heart and skeletal muscle. Not detected in
CC       liver. In the brain, highest expression in olfactory bulb,
CC       hippocampus and cerebellum.
CC   -!- MISCELLANEOUS: Inhibited by barium. Activated by volatile general
CC       anaesthetics such as chloroform, diethyl ether, halothane and
CC       isoflurane.
CC   -!- SIMILARITY: Belongs to the two pore domain potassium channel
CC       (TC 1.A.1.8) family.
CC   -----------------------------------------------------------------------
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DR   EMBL; U73488; AAC53005.2; -; mRNA.
DR   IPI; IPI00875469; -.
DR   RefSeq; NP_034737.2; NM_010607.2.
DR   UniGene; Mm.33304; -.
DR   ProteinModelPortal; P97438; -.
DR   SMR; P97438; 126-179, 236-297.
DR   STRING; P97438; -.
DR   TCDB; 1.A.1.9.1; voltage-gated ion channel (VIC) superfamily.
DR   PhosphoSite; P97438; -.
DR   PRIDE; P97438; -.
DR   Ensembl; ENSMUST00000110920; ENSMUSP00000106545; ENSMUSG00000037624.
DR   GeneID; 16526; -.
DR   KEGG; mmu:16526; -.
DR   UCSC; uc007eal.1; mouse.
DR   CTD; 16526; -.
DR   MGI; MGI:109366; Kcnk2.
DR   eggNOG; roNOG04864; -.
DR   GeneTree; ENSGT00600000084129; -.
DR   HOGENOM; HBG717586; -.
DR   HOVERGEN; HBG052234; -.
DR   InParanoid; P97438; -.
DR   OrthoDB; EOG4PVNZM; -.
DR   NextBio; 289923; -.
DR   ArrayExpress; P97438; -.
DR   Bgee; P97438; -.
DR   CleanEx; MM_KCNK2; -.
DR   Genevestigator; P97438; -.
DR   GermOnline; ENSMUSG00000037624; Mus musculus.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:MGI.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:MGI.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; IDA:MGI.
DR   GO; GO:0030322; P:stabilization of membrane potential; TAS:MGI.
DR   InterPro; IPR013099; Ion_trans_2.
DR   InterPro; IPR003280; K_chnl_2pore.
DR   InterPro; IPR003976; K_chnl_2pore_TREK.
DR   Pfam; PF07885; Ion_trans_2; 2.
DR   PRINTS; PR01333; 2POREKCHANEL.
DR   PRINTS; PR01499; TREKCHANNEL.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Ion transport; Ionic channel; Membrane; Potassium;
KW   Potassium channel; Potassium transport; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    411       Potassium channel subfamily K member 2.
FT                                /FTId=PRO_0000101743.
FT   TOPO_DOM      1     46       Cytoplasmic (Potential).
FT   TRANSMEM     47     67       Helical; (Potential).
FT   INTRAMEM    129    155       Pore-forming; Name=Pore-forming 1;
FT                                (Potential).
FT   TRANSMEM    157    177       Helical; (Potential).
FT   TOPO_DOM    178    207       Cytoplasmic (Potential).
FT   TRANSMEM    208    228       Helical; (Potential).
FT   INTRAMEM    238    268       Pore-forming; Name=Pore-forming 2;
FT                                (Potential).
FT   TRANSMEM    273    293       Helical; (Potential).
FT   TOPO_DOM    294    411       Cytoplasmic (Potential).
FT   REGION      354    411       Required for basal channel activity.
FT   REGION      378    411       Essential for chloroform and halothane
FT                                sensitivity.
FT   CARBOHYD     95     95       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    119    119       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   411 AA;  45298 MW;  8F976DDD103EFA05 CRC64;
     MAAPDLLDPK SAAQNSKPRL SFSSKPTVLA SRVESDSAIN VMKWKTVSTI FLVVVLYLII
     GAAVFKALEQ PQEISQRTTI VIQKQTFIAQ HACVNSTELD ELIQQIVAAI NAGIIPLGNS
     SNQVSHWDLG SSFFFAGTVI TTIGFGNISP RTEGGKIFCI IYALLGIPLF GFLLAGVGDQ
     LGTIFGKGIA KVEDTFIKWN VSQTKIRIIS TIIFILFGCV LFVALPAVIF KHIEGWSALD
     AIYFVVITLT TIGFGDYVAG GSDIEYLDFY KPVVWFWILV GLAYFAAVLS MIGDWLRVIS
     KKTKEEVGEF RAHAAEWTAN VTAEFKETRR RLSVEIYDKF QRATSVKRKL SAELAGNHNQ
     ELTPCRRTLS VNHLTSEREV LPPLLKAESI YLNGLTPHCA GEDIAVIENM K
//
ID   ZNT3_MOUSE              Reviewed;         388 AA.
AC   P97441; P97511;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Zinc transporter 3;
DE            Short=ZnT-3;
DE   AltName: Full=Solute carrier family 30 member 3;
GN   Name=Slc30a3; Synonyms=Znt3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND CHARACTERIZATION.
RC   STRAIN=129; TISSUE=Brain;
RX   MEDLINE=97121493; PubMed=8962159; DOI=10.1073/pnas.93.25.14934;
RA   Palmiter R.D., Cole T.B., Quaife C.J., Findley S.D.;
RT   "ZnT-3, a putative transporter of zinc into synaptic vesicles.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:14934-14939(1996).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Involved in accumulation of zinc in synaptic vesicles.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane; Multi-pass membrane protein (Probable).
CC   -!- TISSUE SPECIFICITY: Brain and testis. In the brain, most abundant
CC       in hippocampus and cerebral cortex. In the testis, expression is
CC       restricted to germ cells and is highest in pachytene spermatocytes
CC       and round spermatids.
CC   -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC       transporter (TC 2.A.4) family. SLC30A subfamily.
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CC   -----------------------------------------------------------------------
DR   EMBL; U76007; AAB39731.1; -; mRNA.
DR   EMBL; U76009; AAB39733.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; U76008; AAB39733.1; JOINED; Genomic_DNA.
DR   IPI; IPI00125397; -.
DR   RefSeq; NP_035903.2; NM_011773.3.
DR   UniGene; Mm.1396; -.
DR   ProteinModelPortal; P97441; -.
DR   STRING; P97441; -.
DR   PhosphoSite; P97441; -.
DR   PRIDE; P97441; -.
DR   Ensembl; ENSMUST00000031037; ENSMUSP00000031037; ENSMUSG00000029151.
DR   GeneID; 22784; -.
DR   KEGG; mmu:22784; -.
DR   UCSC; uc008wxa.1; mouse.
DR   CTD; 22784; -.
DR   MGI; MGI:1345280; Slc30a3.
DR   eggNOG; roNOG11921; -.
DR   HOGENOM; HBG317426; -.
DR   HOVERGEN; HBG003345; -.
DR   InParanoid; P97441; -.
DR   OMA; SVWIVVE; -.
DR   OrthoDB; EOG4VQ9PF; -.
DR   PhylomeDB; P97441; -.
DR   ArrayExpress; P97441; -.
DR   Bgee; P97441; -.
DR   Genevestigator; P97441; -.
DR   GermOnline; ENSMUSG00000029151; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030672; C:synaptic vesicle membrane; TAS:Reactome.
DR   GO; GO:0005385; F:zinc ion transmembrane transporter activity; TAS:Reactome.
DR   GO; GO:0010312; P:detoxification of zinc ion; TAS:BHF-UCL.
DR   GO; GO:0061088; P:regulation of sequestering of zinc ion; TAS:BHF-UCL.
DR   GO; GO:0032119; P:sequestering of zinc ion; TAS:BHF-UCL.
DR   InterPro; IPR002524; Cation_efflux.
DR   PANTHER; PTHR11562; Cation_efflux; 1.
DR   Pfam; PF01545; Cation_efflux; 1.
DR   TIGRFAMs; TIGR01297; CDF; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cytoplasmic vesicle; Ion transport; Membrane;
KW   Phosphoprotein; Synapse; Transmembrane; Transmembrane helix;
KW   Transport; Zinc; Zinc transport.
FT   CHAIN         1    388       Zinc transporter 3.
FT                                /FTId=PRO_0000206097.
FT   TOPO_DOM      1     75       Cytoplasmic (Potential).
FT   TRANSMEM     76     96       Helical; (Potential).
FT   TOPO_DOM     97    105       Vacuolar (Potential).
FT   TRANSMEM    106    126       Helical; (Potential).
FT   TOPO_DOM    127    145       Cytoplasmic (Potential).
FT   TRANSMEM    146    166       Helical; (Potential).
FT   TOPO_DOM    167    177       Vacuolar (Potential).
FT   TRANSMEM    178    198       Helical; (Potential).
FT   TOPO_DOM    199    235       Cytoplasmic (Potential).
FT   TRANSMEM    236    256       Helical; (Potential).
FT   TOPO_DOM    257    263       Vacuolar (Potential).
FT   TRANSMEM    264    284       Helical; (Potential).
FT   TOPO_DOM    285    388       Cytoplasmic (Potential).
FT   MOD_RES      38     38       Phosphoserine.
SQ   SEQUENCE   388 AA;  41824 MW;  3CCDD0A37074EF41 CRC64;
     MEPSLATGGS ETTRLVSARD RSSAGGGLRL KSLFTEPSEP LPEEPKLEGM AFHHCHKDPV
     PQSGLSPERV QARRQLYAAC AVCFIFMAGE VVGGYLAHSL AIMTDAAHLL ADIGSMLASL
     FSLWLSTRPA TRTMTFGWHR SETLGALASV VSLWIVTGIL LYLAFLRLLH SDYHIEAGAM
     LLTASIAVCA NLLMAFVLHQ TGAPHSHGST GAEYAPLEEG HGYPMSLGNT SVRAAFVHVL
     GDLLQSFGVL AASILIYFKP QYKVADPIST FLFSICALGS TAPTLRDVLL VLMEGAPRSV
     EFEPVRDTLL SVPGVRATHD LHLWALTLTY HVASAHLAID STADPEAVLA EASSRLYSRF
     GFSSCTLQVE QYQPEMAQCL RCQEPSQA
//
ID   CAC1A_MOUSE             Reviewed;        2368 AA.
AC   P97445; Q2TPN3;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   08-MAR-2011, entry version 105.
DE   RecName: Full=Voltage-dependent P/Q-type calcium channel subunit alpha-1A;
DE   AltName: Full=Brain calcium channel I;
DE            Short=BI;
DE   AltName: Full=Calcium channel, L type, alpha-1 polypeptide isoform 4;
DE   AltName: Full=Voltage-gated calcium channel subunit alpha Cav2.1;
GN   Name=Cacna1a; Synonyms=Caca1a, Cach4, Cacn3, Cacnl1a4, Ccha1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster; TISSUE=Brain;
RA   Richards K.S., Swensen A.M., Lipscombe D.;
RT   "Molecular identity of P-type calcium current in Purkinje neurons.";
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 49-2212, AND VARIANT TG LEU-649.
RC   STRAIN=DBA/2J;
RX   MEDLINE=97083572; PubMed=8929530; DOI=10.1016/S0092-8674(00)81381-1;
RA   Fletcher C.F., Lutz C.M., O'Sullivan T.N., Shaughnessy J.D. Jr.,
RA   Hawkes R., Frankel W.N., Copeland N.G., Jenkins N.A.;
RT   "Absence epilepsy in tottering mutant mice is associated with calcium
RT   channel defects.";
RL   Cell 87:607-617(1996).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-752; SER-1981; TYR-2027;
RP   SER-2220 AND SER-2273, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the
CC       entry of calcium ions into excitable cells and are also involved
CC       in a variety of calcium-dependent processes, including muscle
CC       contraction, hormone or neurotransmitter release, gene expression,
CC       cell motility, cell division and cell death. The isoform alpha-1A
CC       gives rise to P and/or Q-type calcium currents. P/Q-type calcium
CC       channels belong to the 'high-voltage activated' (HVA) group and
CC       are blocked by the funnel toxin (Ftx) and by the omega-agatoxin-
CC       IVA (omega-Aga-IVA). They are however insensitive to
CC       dihydropyridines (DHP), and omega-conotoxin-GVIA (omega-CTx-GVIA).
CC   -!- SUBUNIT: Voltage-dependent calcium channels are multisubunit
CC       complexes, consisting of alpha-1, alpha-2, beta and delta subunits
CC       in a 1:1:1:1 ratio. The channel activity is directed by the pore-
CC       forming and voltage-sensitive alpha-1 subunit. In many cases, this
CC       subunit is sufficient to generate voltage-sensitive calcium
CC       channel activity. The auxiliary subunits beta and alpha-2/delta
CC       linked by a disulfide bridge regulate the channel activity.
CC       Interacts with CABP1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Brain specific; mainly found in the
CC       cerebellum, olfactory bulb, cerebral cortex, hippocampus, and
CC       inferior colliculus. In the hippocampus, expression occurs in
CC       pyramidal and granule neurons, as well as in interneurons.
CC       Purkinje cells contain predominantly P-type VSCC, the Q-type being
CC       a prominent calcium current in cerebellar granule cells.
CC   -!- DOMAIN: Each of the four internal repeats contains five
CC       hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one
CC       positively charged transmembrane segment (S4). S4 segments
CC       probably represent the voltage-sensor and are characterized by a
CC       series of positively charged amino acids at every third position.
CC   -!- DISEASE: Note=Defects in Cacna1a are the cause of a delayed-onset,
CC       recessive neurological disorder seen in tottering (tg) mutants,
CC       resulting in ataxia, motor seizures and behavioral absence
CC       seizures resembling petit mal epilepsy (or absence epilepsy) in
CC       humans. There are two more alleles: leaner (tg(lA)), that is
CC       characterized by severe ataxia and frequent death past weaning,
CC       but no motor seizures; and rolling Nagoya (tg(rol)), that presents
CC       an intermediary phenotype, the ataxia being somewhat more severe
CC       that with tg, but without motors seizures. Selective degeneration
CC       of cerebellar Purkinje cells has been shown for all these types of
CC       mutants.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family. CACNA1A subfamily.
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DR   EMBL; AY714490; AAW56205.1; -; mRNA.
DR   EMBL; U76716; AAC52940.1; -; mRNA.
DR   IPI; IPI00408646; -.
DR   RefSeq; NP_031604.3; NM_007578.3.
DR   UniGene; Mm.334658; -.
DR   ProteinModelPortal; P97445; -.
DR   SMR; P97445; 1846-1923.
DR   STRING; P97445; -.
DR   PhosphoSite; P97445; -.
DR   PRIDE; P97445; -.
DR   Ensembl; ENSMUST00000038122; ENSMUSP00000039351; ENSMUSG00000034656.
DR   Ensembl; ENSMUST00000121390; ENSMUSP00000112436; ENSMUSG00000034656.
DR   GeneID; 12286; -.
DR   KEGG; mmu:12286; -.
DR   UCSC; uc009mmn.1; mouse.
DR   CTD; 12286; -.
DR   MGI; MGI:109482; Cacna1a.
DR   eggNOG; roNOG13514; -.
DR   HOGENOM; HBG713873; -.
DR   HOVERGEN; HBG050763; -.
DR   InParanoid; P97445; -.
DR   OMA; EKDCRGK; -.
DR   OrthoDB; EOG48KR9C; -.
DR   NextBio; 280756; -.
DR   ArrayExpress; P97445; -.
DR   Bgee; P97445; -.
DR   Genevestigator; P97445; -.
DR   GermOnline; ENSMUSG00000034656; Mus musculus.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IMP:MGI.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0048266; P:behavioral response to pain; IMP:MGI.
DR   GO; GO:0017156; P:calcium ion-dependent exocytosis; IMP:MGI.
DR   GO; GO:0048791; P:calcium ion-dependent exocytosis of neurotransmitter; IMP:MGI.
DR   GO; GO:0016049; P:cell growth; IMP:MGI.
DR   GO; GO:0030644; P:cellular chloride ion homeostasis; IMP:MGI.
DR   GO; GO:0021679; P:cerebellar molecular layer development; IMP:MGI.
DR   GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IMP:MGI.
DR   GO; GO:0021590; P:cerebellum maturation; IMP:MGI.
DR   GO; GO:0048813; P:dendrite morphogenesis; IMP:MGI.
DR   GO; GO:0007204; P:elevation of cytosolic calcium ion concentration; ISS:UniProtKB.
DR   GO; GO:0014051; P:gamma-aminobutyric acid secretion; IMP:MGI.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IMP:MGI.
DR   GO; GO:0006006; P:glucose metabolic process; IMP:MGI.
DR   GO; GO:0042445; P:hormone metabolic process; IMP:MGI.
DR   GO; GO:0051899; P:membrane depolarization; IMP:MGI.
DR   GO; GO:0050883; P:musculoskeletal movement, spinal reflex action; IMP:MGI.
DR   GO; GO:0032353; P:negative regulation of hormone biosynthetic process; IMP:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptosis; IMP:MGI.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:MGI.
DR   GO; GO:0042133; P:neurotransmitter metabolic process; IMP:MGI.
DR   GO; GO:0043113; P:receptor clustering; IMP:MGI.
DR   GO; GO:0014056; P:regulation of acetylcholine secretion; IMP:MGI.
DR   GO; GO:0050770; P:regulation of axonogenesis; IMP:MGI.
DR   GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IDA:MGI.
DR   GO; GO:0060024; P:rhythmic synaptic transmission; IMP:MGI.
DR   GO; GO:0021522; P:spinal cord motor neuron differentiation; IMP:MGI.
DR   GO; GO:0000096; P:sulfur amino acid metabolic process; IMP:MGI.
DR   GO; GO:0007416; P:synapse assembly; IMP:MGI.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR   GO; GO:0021750; P:vestibular nucleus development; IMP:MGI.
DR   InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005448; VDCC_P/Q_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF59; PQVDCCAlpha1; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01632; PQVDCCALPHA1.
DR   SMART; SM00384; AT_hook; 1.
PE   1: Evidence at protein level;
KW   Calcium; Calcium channel; Calcium transport; Disease mutation;
KW   Disulfide bond; Glycoprotein; Ion transport; Ionic channel; Membrane;
KW   Phosphoprotein; Repeat; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN         1   2368       Voltage-dependent P/Q-type calcium
FT                                channel subunit alpha-1A.
FT                                /FTId=PRO_0000053917.
FT   TOPO_DOM      1    100       Cytoplasmic (Potential).
FT   TRANSMEM    101    119       Helical; Name=S1 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    120    138       Extracellular (Potential).
FT   TRANSMEM    139    156       Helical; Name=S2 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    157    168       Cytoplasmic (Potential).
FT   TRANSMEM    169    184       Helical; Name=S3 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    185    192       Extracellular (Potential).
FT   TRANSMEM    193    211       Helical; Name=S4 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    212    230       Cytoplasmic (Potential).
FT   TRANSMEM    231    250       Helical; Name=S5 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    251    337       Extracellular (Potential).
FT   TRANSMEM    338    362       Helical; Name=S6 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    363    489       Cytoplasmic (Potential).
FT   TRANSMEM    490    509       Helical; Name=S1 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    510    523       Extracellular (Potential).
FT   TRANSMEM    524    543       Helical; Name=S2 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    544    551       Cytoplasmic (Potential).
FT   TRANSMEM    552    570       Helical; Name=S3 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    571    580       Extracellular (Potential).
FT   TRANSMEM    581    599       Helical; Name=S4 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    600    618       Cytoplasmic (Potential).
FT   TRANSMEM    619    638       Helical; Name=S5 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    639    691       Extracellular (Potential).
FT   TRANSMEM    692    716       Helical; Name=S6 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    717   1190       Cytoplasmic (Potential).
FT   TRANSMEM   1191   1214       Helical; Name=S1 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1215   1231       Extracellular (Potential).
FT   TRANSMEM   1232   1251       Helical; Name=S2 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1252   1258       Cytoplasmic (Potential).
FT   TRANSMEM   1259   1282       Helical; Name=S3 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1283   1293       Extracellular (Potential).
FT   TRANSMEM   1294   1311       Helical; Name=S4 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1312   1330       Cytoplasmic (Potential).
FT   TRANSMEM   1331   1350       Helical; Name=S5 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1351   1437       Extracellular (Potential).
FT   TRANSMEM   1438   1462       Helical; Name=S6 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1463   1518       Cytoplasmic (Potential).
FT   TRANSMEM   1519   1537       Helical; Name=S1 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1538   1551       Extracellular (Potential).
FT   TRANSMEM   1552   1573       Helical; Name=S2 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1574   1580       Cytoplasmic (Potential).
FT   TRANSMEM   1581   1600       Helical; Name=S3 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1601   1607       Extracellular (Potential).
FT   TRANSMEM   1608   1626       Helical; Name=S4 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1627   1645       Cytoplasmic (Potential).
FT   TRANSMEM   1646   1665       Helical; Name=S5 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1666   1737       Extracellular (Potential).
FT   TRANSMEM   1738   1763       Helical; Name=S6 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1764   2368       Cytoplasmic (Potential).
FT   REPEAT       65    365       I.
FT   REPEAT      475    719       II.
FT   REPEAT     1182   1465       III.
FT   REPEAT     1502   1765       IV.
FT   CA_BIND    1791   1802       By similarity.
FT   REGION      385    402       Binding to the beta subunit (By
FT                                similarity).
FT   COMPBIAS    729    734       Poly-Glu.
FT   COMPBIAS   1155   1158       Poly-Glu.
FT   SITE        320    320       Calcium ion selectivity and permeability
FT                                (By similarity).
FT   SITE        670    670       Calcium ion selectivity and permeability
FT                                (By similarity).
FT   SITE       1411   1411       Calcium ion selectivity and permeability
FT                                (By similarity).
FT   SITE       1600   1600       Binds to omega-Aga-IVA (By similarity).
FT   SITE       1707   1707       Calcium ion selectivity and permeability
FT                                (By similarity).
FT   MOD_RES     752    752       Phosphoserine.
FT   MOD_RES    1981   1981       Phosphoserine.
FT   MOD_RES    2027   2027       Phosphotyrosine.
FT   MOD_RES    2220   2220       Phosphoserine.
FT   MOD_RES    2273   2273       Phosphoserine.
FT   CARBOHYD    285    285       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1607   1607       N-linked (GlcNAc...) (Potential).
FT   VARIANT     649    649       P -> L (in tg).
FT   CONFLICT     79     79       S -> P (in Ref. 2; AAC52940).
FT   CONFLICT     82     82       L -> F (in Ref. 2; AAC52940).
FT   CONFLICT    884    884       P -> L (in Ref. 2; AAC52940).
FT   CONFLICT    888    888       E -> D (in Ref. 1; AAW56205).
FT   CONFLICT   1083   1083       N -> D (in Ref. 2; AAC52940).
FT   CONFLICT   1349   1349       L -> F (in Ref. 2; AAC52940).
FT   CONFLICT   1373   1373       L -> F (in Ref. 2; AAC52940).
FT   CONFLICT   2161   2161       P -> PH (in Ref. 1; AAW56205).
SQ   SEQUENCE   2368 AA;  267647 MW;  E7B573BA005E5CB1 CRC64;
     MARFGDEMPG RYGAGGGGSG PAAGVVVGAA GGRGAGGSRQ GGQPGAQRMY KQSMAQRART
     MALYNPIPVR QNCLTVNRSL FLFSEDNVVR KYAKKITEWP PFEYMILATI IANCIVLALE
     QHLPDDDKTP MSERLDDTEP YFIGIFCFEA GIKIVALGFA FHKGSYLRNG WNVMDFVVVL
     TGILATVGTE FDLRTLRAVR VLRPLKLVSG IPSLQVVLKS IMKAMIPLLQ IGLLLFFAIL
     IFAIIGLEFY MGKFHTTCFE EGTDDIQGES PAPCGTEEPA RTCPNGTKCQ PYWEGPNNGI
     TQFDNILFAV LTVFQCITME GWTDLLYNSN DASGNTWNWL YFIPLIIIGS FFMLNLVLGV
     LSGEFAKERE RVENRRAFLK LRRQQQIERE LNGYMEWISK AEEVILAEDE TDVEQRHPFD
     GALRRATLKK SKTDLLNPEE AEDQLADIAS VGSPFARASI KSAKLENSTF FHKKERRMRF
     YIRRMVKTQA FYWTVLSLVA LNTLCVAIVH YNQPEWLSDF LYYAEFIFLG LFMSEMFIKM
     YGLGTRPYFH SSFNCFDCGV IIGSIFEVIW AVIKPGTSFG ISVLRALRLL RIFKVTKYWA
     SLRNLVVSLL NSMKSIISLL FLLFLFIVVF ALLGMQLFGG QFNFDEGTPP TNFDTFPAAI
     MTVFQILTGE DWNEVMYDGI KSQGGVQGGM VFSIYFIVLT LFGNYTLLNV FLAIAVDNLA
     NAQELTKDEQ EEEEAANQKL ALQKAKEVAE VSPLSAANMS IAVKEQQKNQ KPTKSVWEQR
     TSEMRKQNLL ASREALYGDA AERWPTPYAR PLRPDVKTHL DRPLVVDPQE NRNNNTNKSR
     APEALRPTAR PRESARDPDA RRAWPGSPER APGREGPYGR ESEPQQREHA PPREHAPWDA
     DTERAKAGDA PRRHTHRPVA EGEPRRHRAR RRPGDEPDDR PERRPRPRDA TRPARAADGE
     GDDGERKRRH RHGPPAHDDR ERRHRRRKEN QGSGVPVSGP NLSTTRPIQQ DLGRQDLPLA
     EDLDNMKNNK LATGEPASPH DSLGHSGLPP SPAKIGNSTN PGPALATNPQ NAASRRTPNN
     PGNPSNPGPP KTPENSLIVT NPSSTQPNSA KTARKPEHMA VEIPPACPPL NHTVVQVNKN
     ANPDPLPKKE EEKKEEEEAD PGEDGPKPMP PYSSMFILST TNPLRRLCHY ILNLRYFEMC
     ILMVIAMSSI ALAAEDPVQP NAPRNNVLRY FDYVFTGVFT FEMVIKMIDL GLVLHQGAYF
     RDLWNILDFI VVSGALVAFA FTGNSKGKDI NTIKSLRVLR VLRPLKTIKR LPKLKAVFDC
     VVNSLKNVFN ILIVYMLFMF IFAVVAVQLF KGKFFHCTDE SKEFERDCRG KYLLYEKNEV
     KARDREWKKY EFHYDNVLWA LLTLFTVSTG EGWPQVLKHS VDATFENQGP SPGYRMEMSI
     FYVVYFVVFP FFFVNIFVAL IIITFQEQGD KMMEEYSLEK NERACIDFAI SAKPLTRHMP
     QNKQSFQYRM WQFVVSPPFE YTIMAMIALN TIVLMMKFYG ASVAYENALR VFNIVFTSLF
     SLECVLKVMA FGILNYFRDA WNIFDFVTVL GSITDILVTE FGNNFINLSF LRLFRAARLI
     KLLRQGYTIR ILLWTFVQSF KALPYVCLLI AMLFFIYAII GMQVFGNIGI DGEDEDSDED
     EFQITEHNNF RTFFQALMLL FRSATGEAWH NIMLSCLSGK PCDKNSGILT ADCGNEFAYF
     YFVSFIFLCS FLMLNLFVAV IMDNFEYLTR DSSILGPHHL DEYVRVWAEY DPAACGRIHY
     KDMYSLLRVI SPPLGLGKKC PHRVACKRLL RMDLPVADDN TVHFNSTLMA LIRTALDIKI
     AKGGADKQQM DAELRKEMMA IWPNLSQKTL DLLVTPHKST DLTVGKIYAA MMIMEYYRQS
     KAKKLQAMRE EQNRTPLMFQ RMEPPSPTQE GGPSQNALPS TQLDPGGGLM AHEGGMKESP
     SWVTQRAQEM FQKTGTWSPE RGPPIDMPNS QPNSQSVEMR EMGTDGYSDS EHYLPMEGQT
     RAASMPRLPA ENQRRRGRPR GNDLSTISDT SPMKRSASVL GPKARRLDDY SLERVPPEEN
     QRYHQRRRDR GHRTSERSLG RYTDVDTGLG TDLSMTTQSG DLPSKDRDQD RGRPKDRKHR
     PHHHHHHHHH HPPAPDRDRY AQERPDTGRA RAREQRWSRS PSEGREHTTH RQGSSSVSGS
     PAPSTSGTST PRRGRRQLPQ TPCTPRPLVS YSPAPRRPAA RRMAGPAAPP GGSPRGCRRA
     PRWPAHAPEG PRPRGADYTE PDSPREPPGG AHDPAPRSPR TPRAAGCASP RHGRRLPNGY
     YAGHGAPRPR TARRGAHDAY SESEDDWC
//
ID   ADCY8_MOUSE             Reviewed;        1249 AA.
AC   P97490;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Adenylate cyclase type 8;
DE            EC=4.6.1.1;
DE   AltName: Full=ATP pyrophosphate-lyase 8;
DE   AltName: Full=Adenylate cyclase type VIII;
DE   AltName: Full=Adenylyl cyclase 8;
DE   AltName: Full=Ca(2+)/calmodulin-activated adenylyl cyclase;
GN   Name=Adcy8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RA   Premont R.T.;
RT   "Cloning of mouse adenylyl cyclase type 8.";
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This is a membrane-bound, calcium-stimulable adenylyl
CC       cyclase. May be involved in learning, in memory and in drug
CC       dependence (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
CC   -!- COFACTOR: Binds 2 magnesium ions per subunit (By similarity).
CC   -!- ENZYME REGULATION: Activated by calcium/calmodulin.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
CC       cyclase family.
CC   -!- SIMILARITY: Contains 2 guanylate cyclase domains.
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DR   EMBL; U85021; AAB41885.1; -; mRNA.
DR   IPI; IPI00125645; -.
DR   UniGene; Mm.1425; -.
DR   ProteinModelPortal; P97490; -.
DR   SMR; P97490; 400-585, 969-1169.
DR   STRING; P97490; -.
DR   PhosphoSite; P97490; -.
DR   PRIDE; P97490; -.
DR   Ensembl; ENSMUST00000023007; ENSMUSP00000023007; ENSMUSG00000022376.
DR   UCSC; uc007vzo.1; mouse.
DR   MGI; MGI:1341110; Adcy8.
DR   eggNOG; roNOG05244; -.
DR   GeneTree; ENSGT00590000082802; -.
DR   HOGENOM; HBG445220; -.
DR   HOVERGEN; HBG050458; -.
DR   InParanoid; P97490; -.
DR   OrthoDB; EOG4QJRMD; -.
DR   BRENDA; 4.6.1.1; 244.
DR   ArrayExpress; P97490; -.
DR   Bgee; P97490; -.
DR   CleanEx; MM_ADCY8; -.
DR   Genevestigator; P97490; -.
DR   GermOnline; ENSMUSG00000022376; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007616; P:long-term memory; IGI:MGI.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   InterPro; IPR009398; Aden_cycl-like.
DR   Gene3D; G3DSA:3.30.70.1230; A/G_cyclase; 2.
DR   Pfam; PF06327; DUF1053; 1.
DR   Pfam; PF00211; Guanylate_cyc; 2.
DR   SMART; SM00044; CYCc; 2.
DR   SUPFAM; SSF55073; A/G_cyclase; 2.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 2.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; cAMP biosynthesis; Glycoprotein; Lyase; Magnesium;
KW   Membrane; Metal-binding; Nucleotide-binding; Repeat; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   1249       Adenylate cyclase type 8.
FT                                /FTId=PRO_0000195706.
FT   TOPO_DOM      1    180       Cytoplasmic (Potential).
FT   TRANSMEM    181    201       Helical; (Potential).
FT   TRANSMEM    210    230       Helical; (Potential).
FT   TRANSMEM    245    265       Helical; (Potential).
FT   TRANSMEM    272    292       Helical; (Potential).
FT   TRANSMEM    294    314       Helical; (Potential).
FT   TRANSMEM    319    339       Helical; (Potential).
FT   TOPO_DOM    340    713       Cytoplasmic (Potential).
FT   TRANSMEM    714    734       Helical; (Potential).
FT   TRANSMEM    736    756       Helical; (Potential).
FT   TRANSMEM    785    805       Helical; (Potential).
FT   TRANSMEM    829    849       Helical; (Potential).
FT   TRANSMEM    859    879       Helical; (Potential).
FT   TRANSMEM    892    912       Helical; (Potential).
FT   TOPO_DOM    913   1249       Cytoplasmic (Potential).
FT   METAL       417    417       Magnesium 1 (By similarity).
FT   METAL       417    417       Magnesium 2 (By similarity).
FT   METAL       418    418       Magnesium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       461    461       Magnesium 1 (By similarity).
FT   METAL       461    461       Magnesium 2 (By similarity).
FT   CARBOHYD    815    815       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    819    819       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    886    886       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   1249 AA;  140155 MW;  B2FE5670E9A74DAF CRC64;
     MELSDVHCLS GSEELYTIQP TPPVGDDGSG SRPQRLLWQT AVRHITEQRF IHGHRGGGCG
     GVSRKASNPA GSGPNHHAPQ LSSDSVLPLY SLGPGERAHN TGGTKVFPER SGSGSASGSG
     GGGDLGFLHL DCAPSNSDFF LNGGYSYRGV IFPTLRNSFK SRDLERLYQR YFLGQRRKSE
     VVMNVLDVLT KLTLLVLHLS LASAPMDPLK GILLGFFTGI EVVICALVVV RKDNTSHTYL
     QYSGVVTWVA MTTQILAAGL GYGLLGDGIG YVLFTLFATY SMLPLPLTWA ILAGLGTSLL
     QVTLQVLIPR LAVFSINQVL AQVVLFMCMN TAGIFISYLS DRAQRQAFLE TRRCVEARLR
     LETENQRQER LVLSVLPRFV VLEMINDMTN VEDEHLQHQF HRIYIHRYEN VSILFADVKG
     FTNLSTTLSA QELVRMLNEL FARFDRLAHE HHCLRIKILG DCYYCVSGLP EPRRDHAHCC
     VEMGLSMIKT IRFVRSRTKH DVDMRIGIHS GSVLCGVLGL RKWQFDVWSW DVDIANKLES
     GGIPGRIHIS KATLDCLNGD YNVEEGHGKE RNEFLRKHNI ETYLIKQPEE SLLCLPEDIV
     KESVSCSDRR NSGATFTEGS WSPELPFDNI VGKQNTLAAL TRNSINLLPN HLAQALHVQS
     GPEEINKRIE HTIDLRSGDK LRREHIKPFS LMFKDSSLEH KYSQMRDEVF KSNLVCAFIV
     LLFITAIQSL LPSSRLMPMT IQFSILIMLH SALVLITTAE DYKCLPLILR KTCCWINETY
     LARNVIIFAS ILINFLGAVL NILWCDFDKS IPLKNLTFNS SAVFTDICSY PEYFVFTGVL
     AMVTCAVFVR LNSVLKLAVL LIMIAIYALL TETIYAGLFL SYDNLNHSGE DFLGTKEASL
     LLMAMFLLAV FYHGQQLEYT ARLDFLWRVQ AKEEINEMKE LREHNENMLR NILPSHVARH
     FLEKDRDNEE LYSQSYDAVG VMFASIPGFA DFYSQTEMNN QGVECLRLLN EIIADFDELL
     GEDRFQDIEK IKTIGSTYMA VSGLSPEKQQ CEDKWGHLCA LADFSLALTE SIQEINKHSF
     NNFELRIGIS HGSVVAGVIG AKKPQYDIWG KTVNLASRMD STGVSGRIQV PEETYLILKD
     QGFAFDYRGE IYVKGISEQE GKIKTYFLLG RVQPNPFILP PRRLPGQYSL AAVVLGLVQS
     LNRQRQKQLL NENSNSGIIK SHYNRRTLLT PSGPEPGAQA EGTDKSDLP
//
ID   RGS14_MOUSE             Reviewed;         547 AA.
AC   P97492; Q9DCD1;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Regulator of G-protein signaling 14;
DE            Short=RGS14;
DE   AltName: Full=RAP1/RAP2-interacting protein;
GN   Name=Rgs14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RA   Janoueix-Lerosey I., Tavitian A., de Gunzburg J.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 166-547.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   STRUCTURE BY NMR OF 366-456.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the RAS-binding domain of mouse RGS14.";
RL   Submitted (NOV-2004) to the PDB data bank.
CC   -!- FUNCTION: Inhibits signal transduction by increasing the GTPase
CC       activity of G protein alpha subunits thereby driving them into
CC       their inactive GDP-bound form.
CC   -!- SUBCELLULAR LOCATION: Membrane (By similarity).
CC   -!- SIMILARITY: Contains 1 GoLoco domain.
CC   -!- SIMILARITY: Contains 2 RBD (Ras-binding) domains.
CC   -!- SIMILARITY: Contains 1 RGS domain.
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DR   EMBL; U85055; AAB41893.1; -; mRNA.
DR   EMBL; AK002891; BAB22436.1; -; mRNA.
DR   IPI; IPI00125649; -.
DR   UniGene; Mm.1426; -.
DR   PDB; 1WFY; NMR; -; A=366-456.
DR   PDBsum; 1WFY; -.
DR   ProteinModelPortal; P97492; -.
DR   SMR; P97492; 56-189, 303-459, 499-534.
DR   STRING; P97492; -.
DR   PhosphoSite; P97492; -.
DR   PRIDE; P97492; -.
DR   Ensembl; ENSMUST00000063771; ENSMUSP00000068731; ENSMUSG00000052087.
DR   MGI; MGI:1859709; Rgs14.
DR   eggNOG; roNOG05946; -.
DR   HOGENOM; HBG714402; -.
DR   HOVERGEN; HBG061568; -.
DR   InParanoid; P97492; -.
DR   OrthoDB; EOG4RR6HP; -.
DR   ArrayExpress; P97492; -.
DR   Bgee; P97492; -.
DR   CleanEx; MM_RGS14; -.
DR   Genevestigator; P97492; -.
DR   GermOnline; ENSMUSG00000052087; Mus musculus.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005819; C:spindle; IDA:MGI.
DR   GO; GO:0005096; F:GTPase activator activity; TAS:MGI.
DR   GO; GO:0005057; F:receptor signaling protein activity; IEA:InterPro.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; TAS:MGI.
DR   GO; GO:0007067; P:mitosis; IMP:MGI.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   InterPro; IPR003109; GoLoco_motif.
DR   InterPro; IPR003116; Raf-like_ras-bd.
DR   InterPro; IPR000342; Regulat_G_prot_signal.
DR   InterPro; IPR016137; Regulat_G_prot_signal_superfam.
DR   Pfam; PF02188; GoLoco; 1.
DR   Pfam; PF02196; RBD; 2.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00390; GoLoco; 1.
DR   SMART; SM00455; RBD; 2.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48097; Regulat_G_prot_signal_superfam; 1.
DR   PROSITE; PS50877; GOLOCO; 1.
DR   PROSITE; PS50898; RBD; 2.
DR   PROSITE; PS50132; RGS; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Membrane; Phosphoprotein; Repeat;
KW   Signal transduction inhibitor.
FT   CHAIN         1    547       Regulator of G-protein signaling 14.
FT                                /FTId=PRO_0000204218.
FT   DOMAIN       67    184       RGS.
FT   DOMAIN      303    374       RBD 1.
FT   DOMAIN      376    446       RBD 2.
FT   DOMAIN      500    522       GoLoco.
FT   MOD_RES      20     20       Phosphoserine (By similarity).
FT   MOD_RES      42     42       Phosphoserine (By similarity).
FT   MOD_RES      45     45       Phosphoserine (By similarity).
FT   MOD_RES     261    261       Phosphoserine (By similarity).
FT   MOD_RES     289    289       Phosphoserine.
FT   CONFLICT    210    210       Missing (in Ref. 2; BAB22436).
FT   CONFLICT    431    431       T -> N (in Ref. 2; BAB22436).
FT   STRAND      375    392
FT   STRAND      394    397
FT   TURN        398    402
FT   HELIX       403    406
FT   TURN        407    410
FT   TURN        413    415
FT   HELIX       433    435
FT   STRAND      436    439
FT   STRAND      441    443
FT   STRAND      451    454
SQ   SEQUENCE   547 AA;  59834 MW;  F1BDF29E5336EF75 CRC64;
     MPGKPKHLGV PNGRMVLAVS DGELTSTAGS QAQGEGRGSS LSIHSLPSGP SSPFSTEEQP
     VASWAQSFER LLQDPRGLAY FTEFLKKEFS AENVTFWKAC ERFQQIPASD TKQLAQEAHN
     IYHEFLSSQA LSPVNIDRQA WLSEEVLAQP RPDMFRAQQL QIFNLMKFDS YARFVKSPLY
     QECLLAEAEG RPLREPGSSH LGSPDTARKK PKLKPGKSLP LGVEELGQLP LAEGPCGRPL
     RKSFRREMTG GAMNSALRRE SQGSLNSSAS LDLGFLAFVS SKSESHRKSL GSGESESESR
     PGKYCCVYLP DGTASLALAR PGLTIRDMLA GICEKRGLSL PDIKVYLVGN EQKALVLDQD
     CTVLADQEVR LENRITFQLE LVGLERVVRI SAKPTKRLQE ALQPILAKHG LSLDQVVLHR
     PGEKQPMDLE TPVSSVASQT LVLDTPPDAK MSEARSISPC RSQGCLPRTQ TKDSHLPPSS
     SSLLVEDASS STGNRQTCDI EGLVELLNRV QSSGAHDQRG LLRKEDLVLP EFLQLPSQRP
     GSREAPP
//
ID   SMRC1_MOUSE             Reviewed;        1104 AA.
AC   P97496; Q7TS80; Q7TT29;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=SWI/SNF complex subunit SMARCC1;
DE   AltName: Full=BRG1-associated factor 155;
DE   AltName: Full=SWI/SNF complex 155 kDa subunit;
DE   AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily C member 1;
DE   AltName: Full=SWI3-related protein;
DE            Short=BAF155;
GN   Name=Smarcc1; Synonyms=Baf155, Srg3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   PubMed=9151708; DOI=10.1084/jem.185.10.1827;
RA   Jeon S.H., Kang M.G., Kim Y.H., Jin Y.H., Lee C., Chung H.-Y.,
RA   Kwon H., Park S.D., Seong R.H.;
RT   "A new mouse gene, SRG3, related to the SWI3 of Saccharomyces
RT   cerevisiae, is required for apoptosis induced by glucocorticoids in a
RT   thymoma cell line.";
RL   J. Exp. Med. 185:1827-1836(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-892 (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION.
RX   PubMed=11604513; DOI=10.1128/MCB.21.22.7787-7795.2001;
RA   Kim J.K., Huh S.-O., Choi H., Lee K.-S., Shin D., Lee C., Nam J.-S.,
RA   Kim H., Chung H., Lee H.W., Park S.D., Seong R.H.;
RT   "Srg3, a mouse homolog of yeast SWI3, is essential for early
RT   embryogenesis and involved in brain development.";
RL   Mol. Cell. Biol. 21:7787-7795(2001).
RN   [4]
RP   FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION BY MASS
RP   SPECTROMETRY, IDENTIFICATION IN THE NBAF AND NPBAF COMPLEXES, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=17640523; DOI=10.1016/j.neuron.2007.06.019;
RA   Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T.,
RA   Wu H., Aebersold R., Graef I.A., Crabtree G.R.;
RT   "An essential switch in subunit composition of a chromatin remodeling
RT   complex during neural development.";
RL   Neuron 55:201-215(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND SER-329, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309; SER-327; SER-329
RP   AND THR-336, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-300; SER-327 AND
RP   SER-329, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND SER-329, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Involved in transcriptional activation and repression of
CC       select genes by chromatin remodeling (alteration of DNA-nucleosome
CC       topology). May stimulate the ATPase activity of the catalytic
CC       subunit of the complex. Also involved in vitamin D-coupled
CC       transcription regulation via its association with the WINAC
CC       complex, a chromatin-remodeling complex recruited by vitamin D
CC       receptor (VDR), which is required for the ligand-bound VDR-
CC       mediated transrepression of the CYP27B1 gene (By similarity).
CC       Belongs to the neural progenitors-specific chromatin remodeling
CC       complex (npBAF complex) and the neuron-specific chromatin
CC       remodeling complex (nBAF complex). During neural development a
CC       switch from a stem/progenitor to a post-mitotic chromatin
CC       remodeling mechanism occurs as neurons exit the cell cycle and
CC       become committed to their adult state. The transition from
CC       proliferating neural stem/progenitor cells to post-mitotic neurons
CC       requires a switch in subunit composition of the npBAF and nBAF
CC       complexes. As neural progenitors exit mitosis and differentiate
CC       into neurons, npBAF complexes which contain ACTL6A/BAF53A and
CC       PHF10/BAF45A, are exchanged for homologous alternative
CC       ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-
CC       specific complexes (nBAF). The npBAF complex is essential for the
CC       self-renewal/proliferative capacity of the multipotent neural stem
CC       cells. The nBAF complex along with CREST plays a role regulating
CC       the activity of genes essential for dendrite growth.
CC   -!- SUBUNIT: Component of 6 multiprotein chromatin-remodeling
CC       complexes: Swi/Snf-A (BAF), Swi/Snf-B (PBAF), Brm, Brg1(I), WINAC
CC       and Brg1(II). Each of the five complexes contains a catalytic
CC       subunit (either SMARCA4 or SMARCA2), and at least SMARCE1,
CC       ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCC2 and SMARCB1. Other
CC       subunits specific to each of the complexes may also be present.
CC       Component of the BAF complex, which includes at least actin
CC       (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1,
CC       ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155,
CC       SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of
CC       SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle
CC       cells, the BAF complex also contains DPF3. May also interact with
CC       the SIN3A histone deacetylase transcription repressor complex in
CC       conjunction with SMARCA2 and SMARCA4. The minimal complex composed
CC       of SMARCC1 and SMARCA4 seems to be able to associate with cyclin
CC       such as CCNE1 or transcription factors such as KLF1 or GATA1.
CC       Component of the WINAC complex, at least composed of SMARCA2,
CC       SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A,
CC       BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B. Interacts with
CC       NR3C1 and SMARD1 (By similarity). Component of neural progenitors-
CC       specific chromatin remodeling complex (npBAF complex) composed of
CC       at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A,
CC       SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A,
CC       SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170,
CC       PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-
CC       specific chromatin remodeling complex (nBAF complex) composed of
CC       at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A,
CC       SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A,
CC       SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170,
CC       DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin.
CC   -!- INTERACTION:
CC       Q9Z0H3:Smarcb1; NbExp=2; IntAct=EBI-648047, EBI-689365;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P97496-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P97496-2; Sequence=VSP_012489;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in adult brain, testis and
CC       thymus.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in all organs except heart
CC       and liver (E12.5 and E14.5). The level of expression gradually
CC       diminishes as embryos develop, with expression restricted mostly
CC       to the CNS and thymus at E18.5. Expressed ubiquitously throughout
CC       the developing spinal cord, brain and other embryonic tissues at
CC       E10.5-E16.5.
CC   -!- SIMILARITY: Belongs to the SMARCC family.
CC   -!- SIMILARITY: Contains 1 SANT domain.
CC   -!- SIMILARITY: Contains 1 SWIRM domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB42085.1; Type=Frameshift; Positions=5, 32, 48, 563, 565, 679, 682;
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DR   EMBL; U85614; AAB42085.1; ALT_FRAME; mRNA.
DR   EMBL; BC052423; AAH52423.1; -; mRNA.
DR   EMBL; BC053064; AAH53064.1; -; mRNA.
DR   IPI; IPI00125662; -.
DR   IPI; IPI00515361; -.
DR   PIR; T30967; T30967.
DR   RefSeq; NP_033237.2; NM_009211.2.
DR   UniGene; Mm.85410; -.
DR   ProteinModelPortal; P97496; -.
DR   SMR; P97496; 454-538, 606-675.
DR   DIP; DIP-39986N; -.
DR   IntAct; P97496; 13.
DR   MINT; MINT-4084777; -.
DR   STRING; P97496; -.
DR   PhosphoSite; P97496; -.
DR   PRIDE; P97496; -.
DR   Ensembl; ENSMUST00000088716; ENSMUSP00000086094; ENSMUSG00000032481.
DR   GeneID; 20588; -.
DR   KEGG; mmu:20588; -.
DR   UCSC; uc009rtn.1; mouse.
DR   UCSC; uc009rtp.1; mouse.
DR   CTD; 20588; -.
DR   MGI; MGI:1203524; Smarcc1.
DR   eggNOG; roNOG08421; -.
DR   HOGENOM; HBG314815; -.
DR   HOVERGEN; HBG054849; -.
DR   InParanoid; P97496; -.
DR   OMA; YKKYVHA; -.
DR   OrthoDB; EOG4JHCF5; -.
DR   PhylomeDB; P97496; -.
DR   NextBio; 298891; -.
DR   ArrayExpress; P97496; -.
DR   Bgee; P97496; -.
DR   Genevestigator; P97496; -.
DR   GermOnline; ENSMUSG00000032481; Mus musculus.
DR   GO; GO:0071565; C:nBAF complex; IDA:UniProtKB.
DR   GO; GO:0071564; C:npBAF complex; IDA:UniProtKB.
DR   GO; GO:0005625; C:soluble fraction; IDA:MGI.
DR   GO; GO:0016514; C:SWI/SNF complex; IDA:MGI.
DR   GO; GO:0001741; C:XY body; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0006333; P:chromatin assembly or disassembly; IEA:InterPro.
DR   GO; GO:0006323; P:DNA packaging; TAS:MGI.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IDA:MGI.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0009887; P:organ morphogenesis; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR001357; BRCT.
DR   InterPro; IPR000953; Chromodomain.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR014778; Myb_DNA-bd.
DR   InterPro; IPR001005; SANT_DNA-bd.
DR   InterPro; IPR017884; SANT_eukarya.
DR   InterPro; IPR007526; SWIRM.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF00249; Myb_DNA-binding; 1.
DR   Pfam; PF04433; SWIRM; 1.
DR   SMART; SM00298; CHROMO; 1.
DR   SMART; SM00717; SANT; 1.
DR   SUPFAM; SSF52113; BRCT; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 2.
DR   PROSITE; PS51293; SANT; 1.
DR   PROSITE; PS50934; SWIRM; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Chromatin regulator; Coiled coil;
KW   Neurogenesis; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1104       SWI/SNF complex subunit SMARCC1.
FT                                /FTId=PRO_0000197116.
FT   DOMAIN      448    545       SWIRM.
FT   DOMAIN      617    668       SANT.
FT   COILED      909    945       Potential.
FT   COMPBIAS    326    333       Poly-Pro.
FT   COMPBIAS    768    862       Glu-rich.
FT   COMPBIAS    866    877       Poly-Ala.
FT   COMPBIAS    977   1104       Pro-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     300    300       Phosphoserine.
FT   MOD_RES     309    309       Phosphoserine.
FT   MOD_RES     318    318       Phosphoserine (By similarity).
FT   MOD_RES     327    327       Phosphoserine.
FT   MOD_RES     329    329       Phosphoserine.
FT   MOD_RES     334    334       Phosphothreonine (By similarity).
FT   MOD_RES     336    336       Phosphothreonine.
FT   MOD_RES     338    338       Phosphoserine (By similarity).
FT   MOD_RES     344    344       N6-acetyllysine (By similarity).
FT   MOD_RES     345    345       N6-acetyllysine (By similarity).
FT   MOD_RES     353    353       N6-acetyllysine (By similarity).
FT   MOD_RES     356    356       Phosphoserine (By similarity).
FT   MOD_RES     358    358       N6-acetyllysine (By similarity).
FT   MOD_RES     572    572       Phosphoserine (By similarity).
FT   MOD_RES     947    947       N6-acetyllysine (By similarity).
FT   VAR_SEQ    1074   1104       YPPPPQQQQPPPPADGVPPPPAPGPPASATP -> CK (in
FT                                isoform 2).
FT                                /FTId=VSP_012489.
FT   CONFLICT    132    132       G -> S (in Ref. 1; AAB42085).
FT   CONFLICT    468    468       R -> G (in Ref. 1; AAB42085).
FT   CONFLICT    498    498       R -> C (in Ref. 1; AAB42085).
FT   CONFLICT    512    512       R -> L (in Ref. 1; AAB42085).
FT   CONFLICT    883    883       L -> P (in Ref. 1; AAB42085).
FT   CONFLICT    891    891       I -> K (in Ref. 2; AAH53064).
FT   CONFLICT    952    952       R -> L (in Ref. 2; AAH52423).
FT   CONFLICT    984    984       A -> R (in Ref. 1; AAB42085).
SQ   SEQUENCE   1104 AA;  122890 MW;  9030545104B90CAF CRC64;
     MAATAGGGPG AAAGAVGAGG AAAASGLAVY RRKDGGPASK FWESPDTVSQ LDSVRVWLGK
     HYKKYVHADA PTNKTLAGLV VQLLQFQEDA FGKHVTNPAF TKLPAKCFMD FKAGGTLCHI
     LGAAYKYKNE QGWRRFDLQN PSRMDRNVEM FMNIEKTLVQ NNCLTRPNIY LIPDIDLKLA
     NKLKDIIKRH QGTFTDEKSK ASHHIYPYPS SQEDEEWLRP VMRRDKQVLV HWGFYPDSYD
     TWVHSNDVDA EIEDAPIPEK PWKVHVKWIL DTDVFNEWMN EEDYEVDENR KPVSFRQRIS
     TKNEEPVRSP ERRDRKASAN SRKRKPSPSP PPPTATESRK KSGKKGQASL YGKRRSQKEE
     DEQEDLTKDM EDPTPVPNIE EVVLPKNVNP KKDSENTPVK GGTVADLDEQ DEEAVTTGGK
     EDEDPSKGDP SRSVDPGEDN VTEQTNHIII PSYASWFDYN CIHVIERRAL PEFFNGKNKS
     KTPEIYLAYR NFMIDTYRLN PQEYLTSTAC RRNLTGDVCA VMRVHAFLEQ WGLVNYQVDP
     ESRPMAMGPP PTPHFNVLAD TPSGLVPLHL RSPQVPAAQQ MLNFPEKNKE KPIDLQNFGL
     RTDIYSKKTL AKSKGASAGR EWTEQETLLL LEALEMYKDD WNKVSEHVGS RTQDECILHF
     LRLPIEDPYL ENSDASLGPL AYQPVPFSQS GNPVMSTVAF LASVVDPRVA SAAAKAALEE
     FSRVREEVPL ELVEAHVKKV QEAARASGKV DPTYGLESSC IAGTGPDEPE KLEGSEEEKM
     ETDPDGQQPE KAENKVENES DEGDKIQDRE NEKNTEKEQD SDVSEDVKPE EKENEENKEL
     TDTCKERESD AGKKKVEHEI SEGNVATAAA AALASAATKA KHLAAVEERK IKSLVALLVE
     TQMKKLEIKL RHFEELETIM DREKEALEQQ RQQLLTERQN FHMEQLKYAE LRARQQMEQQ
     QQHGQTPQQA HQHTGGPGMA PLGATGHPGM MPHQQPPPYP LMHHQMPPPH PPQPGQIPGP
     GSMMPGQPMP GRMIPAVAAN IHPTGSGPTP PGMPPMPGNI LGPRVPLTAP NGMYPPPPQQ
     QQPPPPADGV PPPPAPGPPA SATP
//
ID   MYT1L_MOUSE             Reviewed;        1187 AA.
AC   P97500; A2RRK5; O08996; Q8C643; Q8C7L4; Q8CHB4;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   11-JAN-2011, entry version 72.
DE   RecName: Full=Myelin transcription factor 1-like protein;
DE            Short=MyT1-L;
DE            Short=MyT1L;
DE   AltName: Full=Neural zinc finger factor 1;
DE            Short=NZF-1;
DE   AltName: Full=Postmitotic neural gene 1 protein;
DE   AltName: Full=Zinc finger protein Png-1;
GN   Name=Myt1l; Synonyms=Kiaa1106, Nzf1, Png1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP   INDUCTION, AND DEVELOPMENTAL STAGE.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=97276971; PubMed=9130664;
RX   DOI=10.1002/(SICI)1096-9861(19970505)381:2<130::AID-CNE2>3.0.CO;2-4;
RA   Weiner J.A., Chun J.;
RT   "Png-1, a nervous system-specific zinc finger gene, identifies regions
RT   containing postmitotic neurons during mammalian embryonic
RT   development.";
RL   J. Comp. Neurol. 381:130-142(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
RX   MEDLINE=98038874; PubMed=9373037;
RX   DOI=10.1002/(SICI)1097-4547(19971015)50:2<272::AID-JNR16>3.0.CO;2-A;
RA   Kim J.G., Armstrong R.C., Agoston D.V., Robinsky A., Wiese C.,
RA   Nagle J., Hudson L.D.;
RT   "Myelin transcription factor 1 (Myt1) of the oligodendrocyte lineage,
RT   along with a closely related CCHC zinc finger, is expressed in
RT   developing neurons in the mammalian central nervous system.";
RL   J. Neurosci. Res. 50:272-290(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May function as a panneural transcription factor
CC       associated with neuronal differentiation. May play a role in the
CC       development of neurons and oligodendrogalia in the CNS.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=P97500-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P97500-2; Sequence=VSP_015728;
CC       Name=3;
CC         IsoId=P97500-3; Sequence=VSP_015726, VSP_015729, VSP_015730,
CC                                  VSP_015731;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=P97500-4; Sequence=VSP_015727, VSP_015728, VSP_015730,
CC                                  VSP_015731;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Brain.
CC   -!- DEVELOPMENTAL STAGE: Expression is restricted to and present
CC       throughout the embryonic CNS and developing peripheral neural
CC       structures. In the embryonic CNS, expression is restricted to
CC       postmitotic neuronal regions. During the neurogenetic period (E11-
CC       E17) expression is associated temporally and spatially with the
CC       known generation of the first cortical neurons with known
CC       gradients of neuron production. Expression continues in developing
CC       post-mitotic cortical neurons throughout embryonic development and
CC       is expressed within 2 days of neuronal induction in P19 cells.
CC   -!- INDUCTION: Up-regulated by retinoic acid.
CC   -!- SIMILARITY: Contains 6 C2HC-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC53457.1; Type=Frameshift; Positions=633, 644;
CC       Sequence=BAC41467.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U86338; AAC53157.1; -; mRNA.
DR   EMBL; AF004295; AAC53457.1; ALT_FRAME; mRNA.
DR   EMBL; AK049967; BAC34010.1; -; mRNA.
DR   EMBL; AK076608; BAC36413.1; -; mRNA.
DR   EMBL; AB093283; BAC41467.1; ALT_INIT; mRNA.
DR   EMBL; BC131677; AAI31678.1; -; mRNA.
DR   IPI; IPI00336829; -.
DR   IPI; IPI00405389; -.
DR   IPI; IPI00625709; -.
DR   IPI; IPI00653160; -.
DR   PIR; T30189; T30189.
DR   PIR; T46608; T46608.
DR   UniGene; Mm.253067; -.
DR   UniGene; Mm.418721; -.
DR   ProteinModelPortal; P97500; -.
DR   SMR; P97500; 31-56, 502-586, 899-1045.
DR   STRING; P97500; -.
DR   PhosphoSite; P97500; -.
DR   PRIDE; P97500; -.
DR   Ensembl; ENSMUST00000021009; ENSMUSP00000021009; ENSMUSG00000061911.
DR   Ensembl; ENSMUST00000076157; ENSMUSP00000075514; ENSMUSG00000061911.
DR   Ensembl; ENSMUST00000092649; ENSMUSP00000090319; ENSMUSG00000061911.
DR   UCSC; uc007ngi.1; mouse.
DR   MGI; MGI:1100511; Myt1l.
DR   HOGENOM; HBG445538; -.
DR   HOVERGEN; HBG006433; -.
DR   InParanoid; P97500; -.
DR   ArrayExpress; P97500; -.
DR   Bgee; P97500; -.
DR   CleanEx; MM_MYT1L; -.
DR   Genevestigator; P97500; -.
DR   GermOnline; ENSMUSG00000061911; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR013681; Myelin_TF.
DR   InterPro; IPR002515; Znf_C2HC.
DR   Pfam; PF08474; MYT1; 1.
DR   Pfam; PF01530; zf-C2HC; 6.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Developmental protein;
KW   Differentiation; DNA-binding; Metal-binding; Neurogenesis; Nucleus;
KW   Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1   1187       Myelin transcription factor 1-like
FT                                protein.
FT                                /FTId=PRO_0000096674.
FT   ZN_FING      28     58       C2HC-type 1.
FT   ZN_FING     505    535       C2HC-type 2.
FT   ZN_FING     549    579       C2HC-type 3.
FT   ZN_FING     904    934       C2HC-type 4.
FT   ZN_FING     953    983       C2HC-type 5.
FT   ZN_FING    1006   1036       C2HC-type 6.
FT   COILED     1058   1132       Potential.
FT   COMPBIAS     83    200       Asp/Glu-rich.
FT   COMPBIAS    688    721       Ser-rich.
FT   VAR_SEQ       1    597       Missing (in isoform 3).
FT                                /FTId=VSP_015726.
FT   VAR_SEQ       1    426       Missing (in isoform 4).
FT                                /FTId=VSP_015727.
FT   VAR_SEQ     494    495       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_015728.
FT   VAR_SEQ     598    605       SNQASDRV -> MTNRQYFP (in isoform 3).
FT                                /FTId=VSP_015729.
FT   VAR_SEQ     906    925       CPTPGCDGSGHITGNYASHR -> LPVQGPSAIDHLLMFSD
FT                                FLN (in isoform 3 and isoform 4).
FT                                /FTId=VSP_015730.
FT   VAR_SEQ     926   1187       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_015731.
FT   CONFLICT     24     25       AI -> L (in Ref. 2; AAC53457).
FT   CONFLICT     99     99       M -> V (in Ref. 2; AAC53457).
FT   CONFLICT    127    127       D -> AS (in Ref. 1).
FT   CONFLICT    172    172       Missing (in Ref. 2; AAC53457).
FT   CONFLICT    269    269       L -> S (in Ref. 2; AAC53457).
FT   CONFLICT    305    305       K -> R (in Ref. 2; AAC53457).
FT   CONFLICT    323    323       V -> A (in Ref. 2; AAC53457).
FT   CONFLICT    515    515       T -> N (in Ref. 3; BAC34010).
FT   CONFLICT    650    650       N -> K (in Ref. 3; BAC34010).
FT   CONFLICT    806    806       N -> S (in Ref. 3).
FT   CONFLICT   1072   1072       E -> G (in Ref. 2; AAC53457).
SQ   SEQUENCE   1187 AA;  132958 MW;  5CA1CD42182A8C09 CRC64;
     MDVDSEEKRH RTRSKGVRVP VEPAIQELFS CPTPGCDGSG HVSGKYARHR SVYGCPLAKK
     RKTQDKQPQE PAPKRKPFAV KADSSSVDEC YESDGTEDMD DKEEDDDEEF SEDNDEQGDD
     DDEDEVDRED EEEIEEEDDE DDDDDEDGDD VEEEEEDDDE EEEEEEEEEE NEDHQMSCTR
     IMQDTDKDDN NNDEYDNYDE LVAKSLLNLG KIAEDAAYRA RTESEMNSNT SNSLEDDSDK
     NENLGRKSEL SLDLDSDVVR ETVDSLKLLA QGHGVVLSEN ISDRSYAEGM SQQDSRNMNY
     VMLGKPMNNG LMEKMVEESD EEVCLSSLEC LRNQCFDLAR KLSETNPQDR SQPPNMSVRQ
     HVRQEDDFPG RTPDRSYSDM MNLMRLEEQL SPRSRTFSSC AKEDGCHERD DDTTSVNSDR
     SEEVFDMTKG NLTLLEKAIA LETERAKAMR EKMAMDAGRR DNLRSYEDQS PRQLAGEDRK
     SKSSDSHVKK PYYGKDPSRT EKRESKCPTP GCDGTGHVTG LYPHHRSLSG CPHKDRVPPE
     ILAMHENVLK CPTPGCTGRG HVNSNRNSHR SLSGCPIAAA EKLAKAQEKH QSCDVSKSNQ
     ASDRVLRPMC FVKQLEIPQY GYRNNVPTTT PRSNLAKELE KYSKTSFEYN SYDNHTYGKR
     AIAPKVQTRD ISPKGYDDAK RYCKNASPSS STTSSYAPSS SSNLSCGGGS SASSTCSKSS
     FDYTHDMEAA HMAATAILNL STRCREMPQN LSTKPQDLCT ARNPDMEVDE NGTLDLSMNK
     QRPRDSCCPV LTPLEPMSPQ QQAVMNSRCF QLSEGDCWDL PVDYTKMKPR RVDEDEPKEI
     TPEDLDPFQE ALEERRYPGE VTIPSPKPKY PQCKESKKDL ITLSGCPLAD KSIRSMLATS
     SQELKCPTPG CDGSGHITGN YASHRSLSGC PRAKKSGIRI AQSKEDKEDQ EPIRCPVPGC
     DGQGHITGKY ASHRSASGCP LAAKRQKDGY LNGSQFSWKS VKTEGMSCPT PGCDGSGHVS
     GSFLTHRSLS GCPRATSAMK KAKLSGEQML TIKQRASNGI ENDEEIKQLD EEIKELNESN
     SQMEADMIKL RTQITTMESN LKTIEEENKV IEQQNESLLH ELANLSQSLI HSLANIQLPH
     MDPINEQNFD AYVTTLTEMY TNQDRYQSPE NKALLENIKQ AVRGIQV
//
ID   ADA1B_MOUSE             Reviewed;         514 AA.
AC   P97717;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 2.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Alpha-1B adrenergic receptor;
DE   AltName: Full=Alpha-1B adrenoreceptor;
DE            Short=Alpha-1B adrenoceptor;
GN   Name=Adra1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RA   Cotecchia S., Lattion-Zellweger A.;
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 238-276.
RX   MEDLINE=96064818; PubMed=7595531;
RA   Alonso-Llamazares A., Zamanillo D., Casanova E., Ovalle S., Calvo P.,
RA   Chinchetru M.A.;
RT   "Molecular cloning of alpha 1d-adrenergic receptor and tissue
RT   distribution of three alpha 1-adrenergic receptor subtypes in mouse.";
RL   J. Neurochem. 65:2387-2392(1995).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-263 AND SER-266, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: This alpha-adrenergic receptor mediates its action by
CC       association with G proteins that activate a phosphatidylinositol-
CC       calcium second messenger system.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Adrenergic receptor subfamily. ADRA1B sub-subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Y12738; CAA73272.1; -; mRNA.
DR   EMBL; S80219; AAB47043.1; -; mRNA.
DR   IPI; IPI00314429; -.
DR   UniGene; Mm.39086; -.
DR   ProteinModelPortal; P97717; -.
DR   SMR; P97717; 49-363.
DR   STRING; P97717; -.
DR   PhosphoSite; P97717; -.
DR   PRIDE; P97717; -.
DR   Ensembl; ENSMUST00000067258; ENSMUSP00000070200; ENSMUSG00000050541.
DR   MGI; MGI:104774; Adra1b.
DR   eggNOG; roNOG13643; -.
DR   HOVERGEN; HBG106962; -.
DR   InParanoid; P97717; -.
DR   OrthoDB; EOG480HWT; -.
DR   ArrayExpress; P97717; -.
DR   Bgee; P97717; -.
DR   CleanEx; MM_ADRA1B; -.
DR   Genevestigator; P97717; -.
DR   GermOnline; ENSMUSG00000050541; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000299; C:integral to membrane of membrane fraction; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004937; F:alpha1-adrenergic receptor activity; IDA:MGI.
DR   GO; GO:0007512; P:adult heart development; IGI:MGI.
DR   GO; GO:0048148; P:behavioral response to cocaine; IMP:MGI.
DR   GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
DR   GO; GO:0016049; P:cell growth; IGI:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0045818; P:negative regulation of glycogen catabolic process; IMP:MGI.
DR   GO; GO:0035265; P:organ growth; IGI:MGI.
DR   GO; GO:0045819; P:positive regulation of glycogen catabolic process; IMP:MGI.
DR   GO; GO:0001996; P:positive regulation of heart rate by epinephrine-norepinephrine; IGI:MGI.
DR   GO; GO:0001997; P:positive regulation of the force of heart contraction by epinephrine-norepinephrine; IGI:MGI.
DR   GO; GO:0001975; P:response to amphetamine; IMP:MGI.
DR   GO; GO:0043278; P:response to morphine; IMP:MGI.
DR   GO; GO:0001987; P:vasoconstriction of artery involved in baroreceptor response to lowering of systemic arterial blood pressure; IMP:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR001115; Adrene_rcpt_A1B.
DR   InterPro; IPR002233; Adrnrgc_rcpt.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01103; ADRENERGICR.
DR   PRINTS; PR00556; ADRENRGCA1BR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Receptor; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN         1    514       Alpha-1B adrenergic receptor.
FT                                /FTId=PRO_0000069071.
FT   TOPO_DOM      1     45       Extracellular (By similarity).
FT   TRANSMEM     46     69       Helical; Name=1; (By similarity).
FT   TOPO_DOM     70     82       Cytoplasmic (By similarity).
FT   TRANSMEM     83    104       Helical; Name=2; (By similarity).
FT   TOPO_DOM    105    114       Extracellular (By similarity).
FT   TRANSMEM    115    140       Helical; Name=3; (By similarity).
FT   TOPO_DOM    141    160       Cytoplasmic (By similarity).
FT   TRANSMEM    161    183       Helical; Name=4; (By similarity).
FT   TOPO_DOM    184    200       Extracellular (By similarity).
FT   TRANSMEM    201    223       Helical; Name=5; (By similarity).
FT   TOPO_DOM    224    294       Cytoplasmic (By similarity).
FT   TRANSMEM    295    318       Helical; Name=6; (By similarity).
FT   TOPO_DOM    319    325       Extracellular (By similarity).
FT   TRANSMEM    326    350       Helical; Name=7; (By similarity).
FT   TOPO_DOM    351    514       Cytoplasmic (By similarity).
FT   COMPBIAS    370    377       Poly-Arg.
FT   MOD_RES     263    263       Phosphothreonine.
FT   MOD_RES     266    266       Phosphoserine.
FT   LIPID       364    364       S-palmitoyl cysteine (Potential).
FT   CARBOHYD     10     10       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     24     24       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     29     29       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     34     34       N-linked (GlcNAc...) (Potential).
FT   DISULFID    117    194       By similarity.
SQ   SEQUENCE   514 AA;  56418 MW;  17CFD10123DC2B29 CRC64;
     MNPDLDTGHN TSAPAHWGEL KDANFTGPNQ TSSNSTLPQL DVTRAISVGC LGAFILFAIV
     GNILVILSVA CNRHLRTPTN YFIVNLAIAD LLLSFTDLPF SATLEVLGYW VLGRIFCDIW
     AAVDVLCCTA SILSLCAISI DRYIGVRYSL QYPTLVTRRK AILALLSVWV LSTVISIGPL
     LGWKEPAPND DKECGVTEEP FYALFSSLGS FYIPLAVILV MYCRVYIVAK RTTKNLEAGV
     MKEMSNSKEL TLRIHSKNFH EDTLSSTKAK GHNPRSSIAV KLFKFSREKK AAKTLGIVVG
     MFILCWLPFF IALPLGSLFS TLKPPDAVFK VVFWLGYFNS CLNPIIYPCS SKEFKRAFMR
     ILGCQCRGGR RRRRRRRLGA CAYTYRPWTR GGSLERSQSR KDSLDDSGSC MSGSQRTLPS
     ASPSPGYLGR GTQPPVELCA FPEWKPGALL SLPEPPGRRG RLDSGPLFTF KLLGEPESPG
     TEGDASNGGC DTTTDLANGQ PGFKSNMPLA PGHF
//
ID   ADA1A_MOUSE             Reviewed;         466 AA.
AC   P97718; O54913;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   11-FEB-2002, sequence version 2.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Alpha-1A adrenergic receptor;
DE   AltName: Full=Alpha-1A adrenoreceptor;
DE            Short=Alpha-1A adrenoceptor;
DE   AltName: Full=Alpha-1C adrenergic receptor;
GN   Name=Adra1a; Synonyms=Adra1c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   STRAIN=CD-1; TISSUE=Brain, and Kidney;
RX   MEDLINE=98292316; PubMed=9630362; DOI=10.1038/sj.bjp.0701812;
RA   Xiao L., Scofield M.A., Jeffries W.B.;
RT   "Molecular cloning, expression and characterization of cDNA encoding a
RT   mouse alpha1a-adrenoceptor.";
RL   Br. J. Pharmacol. 124:213-221(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 197-280.
RC   TISSUE=Brain;
RX   MEDLINE=96064818; PubMed=7595531;
RA   Alonso-Llamazares A., Zamanillo D., Casanova E., Ovalle S., Calvo P.,
RA   Chinchetru M.A.;
RT   "Molecular cloning of alpha 1d-adrenergic receptor and tissue
RT   distribution of three alpha 1-adrenergic receptor subtypes in mouse.";
RL   J. Neurochem. 65:2387-2392(1995).
CC   -!- FUNCTION: This alpha-adrenergic receptor mediates its action by
CC       association with G proteins that activate a phosphatidylinositol-
CC       calcium second messenger system. Its effect is mediated by G(q)
CC       and G(11) proteins.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- PTM: Carboxyl-terminal Ser or Thr residues may be phosphorylated
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Adrenergic receptor subfamily. ADRA1A sub-subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB47044.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF031431; AAC02658.1; -; mRNA.
DR   EMBL; S80220; AAB47044.1; ALT_INIT; mRNA.
DR   IPI; IPI00128843; -.
DR   UniGene; Mm.57064; -.
DR   ProteinModelPortal; P97718; -.
DR   SMR; P97718; 23-341.
DR   STRING; P97718; -.
DR   PhosphoSite; P97718; -.
DR   PRIDE; P97718; -.
DR   Ensembl; ENSMUST00000054661; ENSMUSP00000053703; ENSMUSG00000045875.
DR   MGI; MGI:104773; Adra1a.
DR   eggNOG; roNOG12277; -.
DR   HOGENOM; HBG445348; -.
DR   HOVERGEN; HBG106962; -.
DR   InParanoid; P97718; -.
DR   OrthoDB; EOG40VVPS; -.
DR   ArrayExpress; P97718; -.
DR   Bgee; P97718; -.
DR   CleanEx; MM_ADRA1A; -.
DR   Genevestigator; P97718; -.
DR   GermOnline; ENSMUSG00000045875; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004937; F:alpha1-adrenergic receptor activity; IDA:MGI.
DR   GO; GO:0007200; P:activation of phospholipase C activity by G-protein coupled receptor protein signaling pathway coupled to IP3 second messenger; IDA:MGI.
DR   GO; GO:0007512; P:adult heart development; IGI:MGI.
DR   GO; GO:0016049; P:cell growth; IGI:MGI.
DR   GO; GO:0001985; P:negative regulation of heart rate involved in baroreceptor response to increased systemic arterial blood pressure; IMP:MGI.
DR   GO; GO:0001994; P:norepinephrine-epinephrine vasoconstriction involved in regulation of systemic arterial blood pressure; IMP:MGI.
DR   GO; GO:0035265; P:organ growth; IGI:MGI.
DR   GO; GO:0001996; P:positive regulation of heart rate by epinephrine-norepinephrine; IGI:MGI.
DR   GO; GO:0001997; P:positive regulation of the force of heart contraction by epinephrine-norepinephrine; IGI:MGI.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR001004; Adrene_rcpt_A1Cs.
DR   InterPro; IPR002233; Adrnrgc_rcpt.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01103; ADRENERGICR.
DR   PRINTS; PR00557; ADRENRGCA1AR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Receptor; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN         1    466       Alpha-1A adrenergic receptor.
FT                                /FTId=PRO_0000069064.
FT   TOPO_DOM      1     27       Extracellular (By similarity).
FT   TRANSMEM     28     51       Helical; Name=1; (By similarity).
FT   TOPO_DOM     52     64       Cytoplasmic (By similarity).
FT   TRANSMEM     65     88       Helical; Name=2; (By similarity).
FT   TOPO_DOM     89     99       Extracellular (By similarity).
FT   TRANSMEM    100    122       Helical; Name=3; (By similarity).
FT   TOPO_DOM    123    143       Cytoplasmic (By similarity).
FT   TRANSMEM    144    167       Helical; Name=4; (By similarity).
FT   TOPO_DOM    168    181       Extracellular (By similarity).
FT   TRANSMEM    182    205       Helical; Name=5; (By similarity).
FT   TOPO_DOM    206    273       Cytoplasmic (By similarity).
FT   TRANSMEM    274    297       Helical; Name=6; (By similarity).
FT   TOPO_DOM    298    305       Extracellular (By similarity).
FT   TRANSMEM    306    329       Helical; Name=7; (By similarity).
FT   TOPO_DOM    330    466       Cytoplasmic (By similarity).
FT   MOD_RES     215    215       Phosphoserine; by PKA (Potential).
FT   LIPID       345    345       S-palmitoyl cysteine (Potential).
FT   CARBOHYD      7      7       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     13     13       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     22     22       N-linked (GlcNAc...) (Potential).
FT   DISULFID     99    176       By similarity.
SQ   SEQUENCE   466 AA;  51763 MW;  3649A5A53DBD34DA CRC64;
     MVLLSENASE GSNCTHPPAQ VNISKAILLG VILGGLIIFG VLGNILVILS VACHRHLHSV
     THYYIVNLAV ADLLLTSTVL PFSAIFEILG YWAFGRVFCN IWAAVDVLCC TASIMGLCII
     SIDRYIGVSY PLRYPTIVTQ RRGVRALLCV WALSLVISIG PLFGWRQQAP EDETICQINE
     EPGYVLFSAL GSFYVPLTII LVMYCRVYVV AKRESRGLKS GLKTDKSDSE QVTLRIHRKN
     VPAEGSGVSS AKNKTHFSVR LLKFSREKKA AKTLGIVVGC FVLCWLPFFL VMPIGSFFPN
     FKPPETVFKI VFWLGYLNSC INPIIYPCSS QEFKKAFQNV LRIQCLRRRQ SSKHALGYTL
     HPPSQAVEEQ HRGMVRIPVG SGETFYKISK TDGVCEWKFF SSMPQGSARI TMPKDQSACT
     TARVRSKSFL QVCCCVGSST PRPEENHQVP TIKIHTISLG ENGEEV
//
ID   CPT1A_MOUSE             Reviewed;         773 AA.
AC   P97742; O35288; Q80SW3; Q8BP98; Q8C7H8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 4.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Carnitine O-palmitoyltransferase 1, liver isoform;
DE            Short=CPT1-L;
DE            EC=2.3.1.21;
DE   AltName: Full=Carnitine O-palmitoyltransferase I, liver isoform;
DE            Short=CPT I;
DE            Short=CPTI-L;
DE   AltName: Full=Carnitine palmitoyltransferase 1A;
GN   Name=Cpt1a; Synonyms=Cpt-1, Cpt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-773.
RC   STRAIN=ICR; TISSUE=Liver;
RX   MEDLINE=98345418; PubMed=9680378; DOI=10.1007/s003359900830;
RA   Cox K.B., Johnson K.R., Wood P.A.;
RT   "Chromosomal locations of the mouse fatty acid oxidation genes Cpt1a,
RT   Cpt1b, Cpt2, Acadvl, and metabolically related Crat gene.";
RL   Mamm. Genome 9:608-610(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 734-773.
RC   TISSUE=Heart;
RX   MEDLINE=96271017; PubMed=8830050;
RA   Uenaka R., Kuwajima M., Ono A., Matsuzawa Y., Hayakawa J., Inohara N.,
RA   Kagawa Y., Ohta S.;
RT   "Increased expression of carnitine palmitoyltransferase I gene is
RT   repressed by administering L-carnitine in the hearts of carnitine-
RT   deficient juvenile visceral steatosis mice.";
RL   J. Biochem. 119:533-540(1996).
CC   -!- CATALYTIC ACTIVITY: Palmitoyl-CoA + L-carnitine = CoA + L-
CC       palmitoylcarnitine.
CC   -!- ENZYME REGULATION: Inhibitors such as malonyl-CoA interact with
CC       its catalytic domain and not with an associated regulatory
CC       component (By similarity).
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the carnitine/choline acetyltransferase
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK050213; BAC34126.2; -; mRNA.
DR   EMBL; AK077454; BAC36808.1; -; mRNA.
DR   EMBL; BC038395; AAH38395.1; -; mRNA.
DR   EMBL; BC046383; AAH46383.1; -; mRNA.
DR   EMBL; AF017175; AAC31641.1; -; mRNA.
DR   EMBL; S82796; AAB39370.1; -; mRNA.
DR   IPI; IPI00330094; -.
DR   RefSeq; NP_038523.2; NM_013495.2.
DR   UniGene; Mm.18522; -.
DR   ProteinModelPortal; P97742; -.
DR   SMR; P97742; 168-767.
DR   STRING; P97742; -.
DR   PhosphoSite; P97742; -.
DR   PRIDE; P97742; -.
DR   Ensembl; ENSMUST00000025835; ENSMUSP00000025835; ENSMUSG00000024900.
DR   GeneID; 12894; -.
DR   KEGG; mmu:12894; -.
DR   CTD; 12894; -.
DR   MGI; MGI:1098296; Cpt1a.
DR   eggNOG; roNOG06319; -.
DR   HOGENOM; HBG717240; -.
DR   HOVERGEN; HBG003458; -.
DR   InParanoid; P97742; -.
DR   OMA; GYAEDGH; -.
DR   OrthoDB; EOG4TXBR8; -.
DR   PhylomeDB; P97742; -.
DR   BRENDA; 2.3.1.21; 244.
DR   NextBio; 282502; -.
DR   ArrayExpress; P97742; -.
DR   Bgee; P97742; -.
DR   CleanEx; MM_CPT1A; -.
DR   Genevestigator; P97742; -.
DR   GermOnline; ENSMUSG00000024900; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004095; F:carnitine O-palmitoyltransferase activity; IEA:EC.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000542; Carn_acyl_trans.
DR   PANTHER; PTHR22589; Carn_acyl_trans; 1.
DR   Pfam; PF00755; Carn_acyltransf; 1.
DR   PROSITE; PS00439; ACYLTRANSF_C_1; 1.
DR   PROSITE; PS00440; ACYLTRANSF_C_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Acyltransferase; Fatty acid metabolism; Lipid metabolism;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW   Transferase; Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    773       Carnitine O-palmitoyltransferase 1, liver
FT                                isoform.
FT                                /FTId=PRO_0000210160.
FT   TOPO_DOM      2     47       Cytoplasmic (Potential).
FT   TRANSMEM     48     73       Helical; (Potential).
FT   TOPO_DOM     74    102       Mitochondrial intermembrane (Potential).
FT   TRANSMEM    103    122       Helical; (Potential).
FT   TOPO_DOM    123    773       Cytoplasmic (Potential).
FT   REGION      555    567       Coenzyme A binding (By similarity).
FT   ACT_SITE    473    473       Proton acceptor (By similarity).
FT   BINDING     589    589       Carnitine (By similarity).
FT   BINDING     602    602       Carnitine (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     588    588       Phosphothreonine (By similarity).
FT   MOD_RES     604    604       Phosphothreonine (By similarity).
FT   MOD_RES     741    741       Phosphoserine (By similarity).
FT   MOD_RES     747    747       Phosphoserine (By similarity).
FT   CONFLICT    145    145       R -> C (in Ref. 2; AAH38395/AAH46383).
FT   CONFLICT    398    398       Y -> C (in Ref. 3; AAC31641).
FT   CONFLICT    531    531       E -> D (in Ref. 1; BAC36808).
FT   CONFLICT    630    630       F -> L (in Ref. 3; AAC31641).
FT   CONFLICT    732    732       I -> T (in Ref. 3; AAC31641).
FT   CONFLICT    760    760       D -> A (in Ref. 3; AAC31641).
SQ   SEQUENCE   773 AA;  88251 MW;  85C3D386FFD97C5E CRC64;
     MAEAHQAVAF QFTVTPDGID LRLSHEALKQ ICLSGLHSWK KKFIRFKNGI ITGVFPASPS
     SWLIVVVGVI SSMHTKVDPS LGMIAKINRT LDTTGRMSSQ TKNIVSGVLF GTGLWVAIIM
     TMRYSLKVLL SYHGWMFAEH GKMSRSTRIW MAMVKVFSGR KPMLYSFQTS LPRLPVPAVK
     DTVSRYLESV RPLMKEGDFQ RMTALAQDFA VNLGPKLQWY LKLKSWWATN YVSDWWEEYI
     YLRGRGPIMV NSNYYAMEML YITPTHIQAA RAGNTIHAIL LYRRTVDREE LKPIRLLGST
     IPLCSAQWER LFNTSRIPGE ETDTIQHVKD SRHIVVYHRG RYFKVWLYHD GRLLRPRELE
     QQMQQILDDT SEPQPGEAKL AALTAADRVP WAKCRQTYFA RGKNKQSLDA VEKAAFFVTL
     DESEQGYREE DPEASIDSYA KSLLHGRCFD RWFDKSITFV VFKNSKIGIN AEHSWADAPI
     VGHLWEYVMA TDVFQLGYSE DGHCKGDKNP NIPKPTRLQW DIPGECQEVI ETSLSSASFL
     ANDVDLHSFP FDTFGKGLIK KCRTSPDAFI QLALQLAHYK DMGKFCLTYE ASMTRLFREG
     RTETVRSCTT ESCNFVLAMM DPTTTAEQRF KLFKIACEKH QHLYRLAMTG AGIDRHLFCL
     YVVSKYLAVD SPFLKEVLSE PWRLSTSQTP QQQVELFDFE KYPDYVSCGG GFGPVADDGY
     GVSYIIVGEN FIHFHISSKF SSPETDSHRF GKHLRQAMMD IITLFGLTAN SKK
//
ID   GRM1_MOUSE              Reviewed;        1199 AA.
AC   P97772; Q6AXG4; Q9EPV6;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   11-APR-2003, sequence version 2.
DT   08-MAR-2011, entry version 106.
DE   RecName: Full=Metabotropic glutamate receptor 1;
DE            Short=mGluR1;
DE   Flags: Precursor;
GN   Name=Grm1; Synonyms=Gprc1a, Mglur1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=20050857; PubMed=10581402; DOI=10.1016/S0169-328X(99)00239-9;
RA   Zhu H., Ryan K., Chen S.;
RT   "Cloning of novel splice variants of mouse mGluR1.";
RL   Brain Res. Mol. Brain Res. 73:93-103(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 945-1127 (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RA   Watanabe M.;
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor for glutamate. The activity of this receptor is
CC       mediated by a G-protein that activates a phosphatidylinositol-
CC       calcium second messenger system. May participate in the central
CC       action of glutamate in the CNS, such as long-term potentiation in
CC       the hippocampus and long-term depression in the cerebellum (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer; disulfide-linked. The PPXXF motif binds
CC       HOMER1, HOMER2 and HOMER3. Interacts with SIAH1, RYR1, RYR2,
CC       ITPR1, SHANK1, SHANK3 and GRASP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=A;
CC         IsoId=P97772-1; Sequence=Displayed;
CC       Name=2; Synonyms=B;
CC         IsoId=P97772-2; Sequence=VSP_007186, VSP_007187;
CC       Name=3; Synonyms=E55;
CC         IsoId=P97772-3; Sequence=VSP_007184, VSP_007185;
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
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DR   EMBL; AF320126; AAG41991.2; -; mRNA.
DR   EMBL; BC067057; AAH67057.1; -; mRNA.
DR   EMBL; BC079566; AAH79566.1; -; mRNA.
DR   EMBL; U89891; AAB48099.1; -; mRNA.
DR   IPI; IPI00110402; -.
DR   IPI; IPI00281619; -.
DR   IPI; IPI00281620; -.
DR   RefSeq; NP_001107805.1; NM_001114333.2.
DR   RefSeq; NP_058672.1; NM_016976.3.
DR   UniGene; Mm.391904; -.
DR   UniGene; Mm.477053; -.
DR   ProteinModelPortal; P97772; -.
DR   SMR; P97772; 35-583.
DR   STRING; P97772; -.
DR   PhosphoSite; P97772; -.
DR   PRIDE; P97772; -.
DR   Ensembl; ENSMUST00000044306; ENSMUSP00000037255; ENSMUSG00000019828.
DR   Ensembl; ENSMUST00000105561; ENSMUSP00000101190; ENSMUSG00000019828.
DR   GeneID; 14816; -.
DR   KEGG; mmu:14816; -.
DR   UCSC; uc007ejh.1; mouse.
DR   UCSC; uc007eji.1; mouse.
DR   CTD; 14816; -.
DR   MGI; MGI:1351338; Grm1.
DR   GeneTree; ENSGT00580000081222; -.
DR   HOGENOM; HBG445787; -.
DR   HOVERGEN; HBG107965; -.
DR   InParanoid; P97772; -.
DR   OMA; GHILENP; -.
DR   OrthoDB; EOG4N5VW3; -.
DR   PhylomeDB; P97772; -.
DR   NextBio; 287019; -.
DR   ArrayExpress; P97772; -.
DR   Bgee; P97772; -.
DR   CleanEx; MM_GRM1; -.
DR   Genevestigator; P97772; -.
DR   GermOnline; ENSMUSG00000019828; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; TAS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; TAS:UniProtKB.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0001639; F:PLC activating metabotropic glutamate receptor activity; TAS:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0000187; P:activation of MAPK activity; IDA:UniProtKB.
DR   GO; GO:0000186; P:activation of MAPKK activity; IDA:UniProtKB.
DR   GO; GO:0007626; P:locomotory behavior; IMP:UniProtKB.
DR   GO; GO:0043408; P:regulation of MAPKKK cascade; IDA:UniProtKB.
DR   GO; GO:0051930; P:regulation of sensory perception of pain; IDA:UniProtKB.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:UniProtKB.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR000337; GPCR_3.
DR   InterPro; IPR011500; GPCR_3_9-Cys_dom.
DR   InterPro; IPR017978; GPCR_3_C.
DR   InterPro; IPR017979; GPCR_3_CS.
DR   InterPro; IPR000162; GPCR_3_mtglu_rcpt.
DR   InterPro; IPR001256; GPCR_3_mtglu_rcpt_1.
DR   InterPro; IPR019588; Metabotropic_Glu_rcpt_Homer-bd.
DR   Pfam; PF00003; 7tm_3; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF10606; GluR_Homer-bdg; 1.
DR   Pfam; PF07562; NCD3G; 1.
DR   PRINTS; PR00248; GPCRMGR.
DR   PRINTS; PR01051; MTABOTROPC1R.
DR   PRINTS; PR00593; MTABOTROPICR.
DR   PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; 1.
DR   PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; 1.
DR   PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
DR   PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW   Receptor; Signal; Transducer; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21   1199       Metabotropic glutamate receptor 1.
FT                                /FTId=PRO_0000012923.
FT   TOPO_DOM     21    593       Extracellular (Potential).
FT   TRANSMEM    594    614       Helical; Name=1; (Potential).
FT   TOPO_DOM    615    629       Cytoplasmic (Potential).
FT   TRANSMEM    630    650       Helical; Name=2; (Potential).
FT   TOPO_DOM    651    660       Extracellular (Potential).
FT   TRANSMEM    661    681       Helical; Name=3; (Potential).
FT   TOPO_DOM    682    706       Cytoplasmic (Potential).
FT   TRANSMEM    707    727       Helical; Name=4; (Potential).
FT   TOPO_DOM    728    751       Extracellular (Potential).
FT   TRANSMEM    752    772       Helical; Name=5; (Potential).
FT   TOPO_DOM    773    786       Cytoplasmic (Potential).
FT   TRANSMEM    787    807       Helical; Name=6; (Potential).
FT   TOPO_DOM    808    811       Extracellular (Potential).
FT   TRANSMEM    812    832       Helical; Name=7; (Potential).
FT   TOPO_DOM    833   1199       Cytoplasmic (Potential).
FT   COMPBIAS   1014   1041       Gln/Pro-rich.
FT   COMPBIAS   1073   1087       Gln/Pro-rich.
FT   COMPBIAS   1101   1135       Asp/Glu-rich (acidic).
FT   COMPBIAS   1147   1199       Ser-rich.
FT   MOD_RES     672    672       Phosphotyrosine (By similarity).
FT   MOD_RES    1119   1119       Phosphotyrosine (By similarity).
FT   CARBOHYD     98     98       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    223    223       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    397    397       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    515    515       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    747    747       N-linked (GlcNAc...) (Potential).
FT   DISULFID    140    140       Interchain (By similarity).
FT   VAR_SEQ     317    321       SDGWA -> RDSRN (in isoform 3).
FT                                /FTId=VSP_007184.
FT   VAR_SEQ     322   1199       Missing (in isoform 3).
FT                                /FTId=VSP_007185.
FT   VAR_SEQ     887    906       NSNGKSVSWSEPGGRQAPKG -> KKRQPEFSPSSQCPSAH
FT                                VQL (in isoform 2).
FT                                /FTId=VSP_007186.
FT   VAR_SEQ     907   1199       Missing (in isoform 2).
FT                                /FTId=VSP_007187.
SQ   SEQUENCE   1199 AA;  133212 MW;  FE5370AF160CC16E CRC64;
     MVRLLLIFFP MIFLEMSILP RMPDRKVLLA GASSQRSVAR MDGDVIIGAL FSVHHQPPAE
     KVPERKCGEI REQYGIQRVE AMFHTLDKIN ADPVLLPNIT LGSEIRDSCW HSSVALEQSI
     EFIRDSLISI RDEKDGLNRC LPDGQTLPPG RTKKPIAGVI GPGSSSVAIQ VQNLLQLFDI
     PQIAYSATSI DLSDKTLYKY FLRVVPSDTL QARAMLDIVK RYNWTYVSAV HTEGNYGESG
     MDAFKELAAQ EGLCIAHSDK IYSNAGEKSF DRLLRKLRER LPKARVVVCF CEGMTVRGLL
     SAMRRLGVVG EFSLIGSDGW ADRDEVIEGY EVEANGGITI KLQSPEVRSF DDYFLKLRLD
     TNTRNPWFPE FWQHRFQCRL PGHLLENPNF KKVCTGNESL EENYVQDSKM GFVINAIYAM
     AHGLQNMHHA LCPGYVGLCD AMKPIDGRKL LDFLIKSSFV GVSGEEVWFD EKGDAPGRYD
     IMNLQYTEAN RYDYVHVGTW HEGVLNIDDY KIQMNKSGMV RSVCSEPCLK GQIKVIRKGE
     VSCCWICTAC KENEFVQDEF TCRACDLGWW PNAELTGCEP ITIRYLEWSD IESIIAIAFS
     CLGILVTLFV TLIFVLYRDT PVVKSSSREL CYIILAGIFL GYVCPFTLIA KPTTTSCYLQ
     RLLVGLSSAM CYSALVTKTN RIARILAGSK KKICTRKPRF MSAWAQVIIA SILISVQLTL
     VVTLIIMEPP MPILSYPSIK EVYLICNTSN LGVVAPVGYN GLLIMSCTYY AFKTRNVPAN
     FNEAKYIAFT MYTTCIIWLA FVPIYFGSNY KIITTCFAVS LSVTVALGCM FTPKMYIIIA
     KPERNVRSAF TTSDVVRMHV GDGKLPCRSN TFLNIFRRKK PGAGNANSNG KSVSWSEPGG
     RQAPKGQHVW QRLSVHVKTN ETACNQTAVI KPLTKSYQGS GKSLTFSDAS TKTLYNVEEE
     DNTPSTHFSP PSSPSMVVHR RGPPVATTPP LPPHLSAEET PLFLADSVIP KGLPPPLPQQ
     QQQPPPQPPP QQPKSLMDQL QGVVTNFGSG IPDFHAVLAG PGTPGNGLRS LYPPPPPPQH
     LQMLPLQLST FREEPISPPG EDDDDDSSER FKLLQEFVYE REGNTEEDDL EEEEDLPAAS
     KLTPEDSPAL TPPSPFRDSV ASGSSVPSSP VSESVLCTPP NVTYASVILR DYKQSSSTL
//
ID   CRY1_MOUSE              Reviewed;         606 AA.
AC   P97784;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Cryptochrome-1;
GN   Name=Cry1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Brain, Keratinocyte, and Liver;
RX   MEDLINE=99030511; PubMed=9801304; DOI=10.1093/nar/26.22.5086;
RA   Kobayashi K., Kanno S., Smit B., van der Horst G.T.J., Takao M.,
RA   Yasui A.;
RT   "Characterization of photolyase/blue-light receptor homologs in mouse
RT   and human cells.";
RL   Nucleic Acids Res. 26:5086-5092(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RA   Kume K., Reppert S.M.;
RT   "Analysis of mouse cryptochromes.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N;
RC   TISSUE=Brain, Embryonic brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=9600923; DOI=10.1073/pnas.95.11.6097;
RA   Miyamoto Y., Sancar A.;
RT   "Vitamin B2-based blue-light photoreceptors in the retinohypothalamic
RT   tract as the photoactive pigments for setting the circadian clock in
RT   mammals.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:6097-6102(1998).
RN   [6]
RP   INTERACTION WITH PER1; PER2; PER3 AND TIMELESS, FUNCTION, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX   MEDLINE=99354985; PubMed=10428031; DOI=10.1016/S0092-8674(00)81014-4;
RA   Kume K., Zylka M.J., Sriram S., Shearman L.P., Weaver D.R., Jin X.,
RA   Maywood E.S., Hastings M.H., Reppert S.M.;
RT   "mCRY1 and mCRY2 are essential components of the negative limb of the
RT   circadian clock feedback loop.";
RL   Cell 98:193-205(1999).
RN   [7]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=10521578; DOI=10.1016/S0169-328X(99)00192-8;
RA   Miyamoto Y., Sancar A.;
RT   "Circadian regulation of cryptochrome genes in the mouse.";
RL   Brain Res. Mol. Brain Res. 71:238-243(1999).
RN   [8]
RP   INTERACTION WITH PER1 AND PER2, PHOSPHORYLATION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=11875063; DOI=10.1074/jbc.M111466200;
RA   Eide E.J., Vielhaber E.L., Hinz W.A., Virshup D.M.;
RT   "The circadian regulatory proteins BMAL1 and cryptochromes are
RT   substrates of casein kinase Iepsilon.";
RL   J. Biol. Chem. 277:17248-17254(2002).
RN   [9]
RP   INTERACTION WITH MAPK, PHOSPHORYLATION AT SER-247, AND MUTAGENESIS OF
RP   SER-247.
RX   PubMed=15298678; DOI=10.1111/j.1356-9597.2004.00758.x;
RA   Sanada K., Harada Y., Sakai M., Todo T., Fukada Y.;
RT   "Serine phosphorylation of mCRY1 and mCRY2 by mitogen-activated
RT   protein kinase.";
RL   Genes Cells 9:697-708(2004).
RN   [10]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16628007;
RA   Kondratov R.V., Kondratova A.A., Lee C., Gorbacheva V.Y.,
RA   Chernov M.V., Antoch M.P.;
RT   "Post-translational regulation of circadian transcriptional
RT   CLOCK(NPAS2)/BMAL1 complex by CRYPTOCHROMES.";
RL   Cell Cycle 5:890-895(2006).
RN   [11]
RP   FUNCTION, INTERACTION WITH PER1 AND PER2, AND SUBCELLULAR LOCATION.
RX   PubMed=16478995; DOI=10.1128/MCB.26.5.1743-1753.2006;
RA   Chaves I., Yagita K., Barnhoorn S., Okamura H., van der Horst G.T.J.,
RA   Tamanini F.;
RT   "Functional evolution of the photolyase/cryptochrome protein family:
RT   importance of the C terminus of mammalian CRY1 for circadian core
RT   oscillator performance.";
RL   Mol. Cell. Biol. 26:1743-1753(2006).
RN   [12]
RP   INTERACTION WITH FBXL3, AND UBIQUITINATION.
RX   PubMed=17462724; DOI=10.1016/j.cell.2007.04.030;
RA   Siepka S.M., Yoo S.H., Park J., Song W., Kumar V., Hu Y., Lee C.,
RA   Takahashi J.S.;
RT   "Circadian mutant Overtime reveals F-box protein FBXL3 regulation of
RT   cryptochrome and period gene expression.";
RL   Cell 129:1011-1023(2007).
RN   [13]
RP   INTERACTION WITH FBXL21, AND UBIQUITINATION.
RX   PubMed=18953409; DOI=10.1371/journal.pone.0003530;
RA   Dardente H., Mendoza J., Fustin J.M., Challet E., Hazlerigg D.G.;
RT   "Implication of the F-Box Protein FBXL21 in circadian pacemaker
RT   function in mammals.";
RL   PLoS ONE 3:E3530-E3530(2008).
CC   -!- FUNCTION: Blue light-dependent regulator of the circadian feedback
CC       loop. Inhibits CLOCK|NPAS2-ARNTL E box-mediated transcription.
CC       Acts, in conjunction with CRY2, in maintaining period length and
CC       circadian rhythmicity. Has no photolyase activity. Capable of
CC       translocating circadian clock core proteins such as PER proteins
CC       to the nucleus. May inhibit CLOCK|NPAS2-ARNTL transcriptional
CC       activity through stabilizing the unphosphorylated form of ARNTL.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- COFACTOR: Binds 1 5,10-methenyltetrahydrofolate non-covalently per
CC       subunit (By similarity).
CC   -!- SUBUNIT: Component of the circadian core oscillator, which
CC       includes the CRY proteins, CLOCK or NPAS2, ARNTL or ARNTL2, CSNK1D
CC       and/or CSNK1E, TIMELESS, and the PER proteins. Interacts with
CC       FBXL21 (By similarity). Interacts directly with TIMELESS and the
CC       PER proteins. Interacts directly with PER1 and PER2 C-terminal
CC       domains. Interaction with PER2 inhibits its ubiquitination and
CC       vice versa. Binds MAPK. Interacts with FBXL3.
CC   -!- INTERACTION:
CC       Q9WTL8:Arntl; NbExp=3; IntAct=EBI-1266607, EBI-644534;
CC       Q8C4V4:Fbxl3; NbExp=1; IntAct=EBI-1266607, EBI-1266589;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Transloctaed to the
CC       nucleus through interaction with other Clock proteins such as PER2
CC       or ARNTL.
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined including
CC       heart, brain, spleen, lung, liver, skeletal muscle, kidney and
CC       testis. Higher levels in brain, liver and testis. In the retina,
CC       highly expressed in the ganglion cell layer (GCL) and in the inner
CC       nuclear layer (INL). Evenly distributed in central and peripheral
CC       retina. In the brain, highly expressed in the suprachiasmatic
CC       nucleus (SCN). High levels in cerebral cortical layers
CC       particularly in the pyramidial cell layer of the hippocampus, the
CC       granular cell layer of the dentate gyrus (DG) and the pyramidal
CC       cell layer of the piriform cortex (PFC).
CC   -!- INDUCTION: In SCN, exhibits circadian rhythm expression with
CC       highest levels during the light phase at CT10. No detectable
CC       expression after 8 hours in the dark. Circadian oscillations also
CC       observed in liver, skeletal muscle and cerebellum, but not in
CC       testis.
CC   -!- PTM: Phosphorylation on Ser-247 by MAPK is important for the
CC       inhibition of CLOCK-ARNTL-mediated transcriptional activity.
CC       Phosphorylation by CSNK1E requires interaction with PER1 or PER2.
CC   -!- PTM: Ubiquitinated by the SCF(FBXL3) and SCF(FBXL21) complex,
CC       leading to its degradation (By similarity).
CC   -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC   -!- SIMILARITY: Contains 1 DNA photolyase domain.
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DR   EMBL; AB000777; BAA19175.1; -; mRNA.
DR   EMBL; AF156986; AAD39548.1; -; mRNA.
DR   EMBL; AK162460; BAE36931.1; -; mRNA.
DR   EMBL; BC022174; AAH22174.1; -; mRNA.
DR   EMBL; BC085499; AAH85499.1; -; mRNA.
DR   IPI; IPI00129123; -.
DR   RefSeq; NP_031797.1; NM_007771.3.
DR   UniGene; Mm.26237; -.
DR   ProteinModelPortal; P97784; -.
DR   SMR; P97784; 2-491.
DR   IntAct; P97784; 17.
DR   STRING; P97784; -.
DR   PhosphoSite; P97784; -.
DR   PRIDE; P97784; -.
DR   Ensembl; ENSMUST00000020227; ENSMUSP00000020227; ENSMUSG00000020038.
DR   GeneID; 12952; -.
DR   KEGG; mmu:12952; -.
DR   UCSC; uc007gle.1; mouse.
DR   CTD; 12952; -.
DR   MGI; MGI:1270841; Cry1.
DR   eggNOG; roNOG14206; -.
DR   GeneTree; ENSGT00500000044813; -.
DR   HOGENOM; HBG693486; -.
DR   HOVERGEN; HBG053470; -.
DR   InParanoid; P97784; -.
DR   OMA; FDTDGLP; -.
DR   OrthoDB; EOG4DBTDC; -.
DR   PhylomeDB; P97784; -.
DR   Reactome; REACT_24972; Circadian Clock (mouse).
DR   NextBio; 282662; -.
DR   ArrayExpress; P97784; -.
DR   Bgee; P97784; -.
DR   CleanEx; MM_CRY1; -.
DR   Genevestigator; P97784; -.
DR   GermOnline; ENSMUSG00000020038; Mus musculus.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0003913; F:DNA photolyase activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0007623; P:circadian rhythm; IDA:MGI.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR006050; DNA_photolyase_N.
DR   InterPro; IPR005101; Photolyase_FAD-bd/Cryptochr_C.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Pfam; PF00875; DNA_photolyase; 1.
DR   Pfam; PF03441; FAD_binding_7; 1.
DR   SUPFAM; SSF52425; DNA_photolyase_N; 1.
DR   SUPFAM; SSF48173; Photolyase_FAD-bd/Cryptochr_C; 1.
DR   PROSITE; PS00394; DNA_PHOTOLYASES_1_1; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Biological rhythms; Chromophore; Cytoplasm; FAD; Flavoprotein;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Photoreceptor protein;
KW   Receptor; Repressor; Sensory transduction; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN         1    606       Cryptochrome-1.
FT                                /FTId=PRO_0000261142.
FT   DOMAIN        3    178       DNA photolyase.
FT   REGION      211    488       FAD-binding.
FT   REGION      371    470       Required for inhibition of CLOCK-ARNTL-
FT                                mediated transcription.
FT   MOD_RES     247    247       Phosphoserine; by MAPK.
FT   MOD_RES     432    432       Phosphotyrosine (By similarity).
FT   MUTAGEN     247    247       S->A: Reduced MAPK-catalyzed in vitro
FT                                phosphorylation. No effect on inhibition
FT                                of CLOCK-ARNTL-mediated transcriptional
FT                                activity.
FT   MUTAGEN     247    247       S->D: Reduced inhibition of CLOCK-ARNTL-
FT                                mediated transcriptional activity.
SQ   SEQUENCE   606 AA;  68001 MW;  2F2B8DD53F0A9AF9 CRC64;
     MGVNAVHWFR KGLRLHDNPA LKECIQGADT IRCVYILDPW FAGSSNVGIN RWRFLLQCLE
     DLDANLRKLN SRLFVIRGQP ADVFPRLFKE WNITKLSIEY DSEPFGKERD AAIKKLATEA
     GVEVIVRISH TLYDLDKIIE LNGGQPPLTY KRFQTLVSKM EPLEMPADTI TSDVIGKCMT
     PLSDDHDEKY GVPSLEELGF DTDGLSSAVW PGGETEALTR LERHLERKAW VANFERPRMN
     ANSLLASPTG LSPYLRFGCL SCRLFYFKLT DLYKKVKKNS SPPLSLYGQL LWREFFYTAA
     TNNPRFDKME GNPICVQIPW DKNPEALAKW AEGRTGFPWI DAIMTQLRQE GWIHHLARHA
     VACFLTRGDL WISWEEGMKV FEELLLDADW SINAGSWMWL SCSSFFQQFF HCYCPVGFGR
     RTDPNGDYIR RYLPVLRGFP AKYIYDPWNA PEGIQKVAKC LIGVNYPKPM VNHAEASRLN
     IERMKQIYQQ LSRYRGLGLL ASVPSNSNGN GGLMGYAPGE NVPSCSSSGN GGLMGYAPGE
     NVPSCSGGNC SQGSGILHYA HGDSQQTHSL KQGRSSAGTG LSSGKRPSQE EDAQSVGPKV
     QRQSSN
//
ID   XRN1_MOUSE              Reviewed;        1719 AA.
AC   P97789; O35651; P97790; Q3TE44; Q3TRE9; Q3UQL5;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=5'-3' exoribonuclease 1;
DE            Short=mXRN1;
DE            EC=3.1.11.-;
DE   AltName: Full=Protein Dhm2;
DE   AltName: Full=Strand-exchange protein 1 homolog;
GN   Name=Xrn1; Synonyms=Dhm2, Exo, Sep1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RX   MEDLINE=97361754; PubMed=9218715; DOI=10.1016/S0378-1119(97)00053-X;
RA   Shobuike T., Sugano S., Yamashita T., Ikeda H.;
RT   "Cloning and characterization of mouse Dhm2 cDNA, a functional homolog
RT   of budding yeast SEP1.";
RL   Gene 191:161-166(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION IN RNA DECAY,
RP   DNA AND RNA BINDING, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=BALB/c; TISSUE=Testis;
RX   MEDLINE=97201457; PubMed=9049243; DOI=10.1083/jcb.136.4.761;
RA   Bashkirov V.I., Scherthan H., Solinger J.A., Buerstedde J.-M.,
RA   Heyer W.-D.;
RT   "A mouse cytoplasmic exoribonuclease (mXRN1) with preference for G4
RT   tetraplex substrates.";
RL   J. Cell Biol. 136:761-773(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-778, AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1261-1719 (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Heart, Hypothalamus, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   ASSOCIATION WITH ALPHA AND BETA TUBULINS, DEVELOPMENTAL STAGE, AND
RP   TISSUE SPECIFICITY.
RX   MEDLINE=22943231; PubMed=14580940; DOI=10.1016/S0306-4522(03)00487-1;
RA   Shimoyama Y., Morikawa Y., Ichihara M., Kodama Y., Fukuda N.,
RA   Hayashi H., Morinaga T., Iwashita T., Murakumo Y., Takahashi M.;
RT   "Identification of human SEP1 as a glial cell line-derived
RT   neurotrophic factor-inducible protein and its expression in the
RT   nervous system.";
RL   Neuroscience 121:899-906(2003).
CC   -!- FUNCTION: Major 5'-3' exoribonuclease involved in mRNA decay.
CC       Required for the 5'-3'-processing of the G4 tetraplex-containing
CC       DNA and RNA substrates. The kinetic of hydrolysis is faster for G4
CC       RNA tetraplex than for G4 DNA tetraplex and monomeric RNA
CC       tetraplex. Binds to RNA and DNA. Plays a role in replication-
CC       dependent histone mRNA degradation (By similarity).
CC   -!- SUBUNIT: Found in a mRNP complex with UPF1, UPF2, UPF3B and XRN1
CC       (By similarity). Associates with alpha and beta tubulins.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Discrete foci at the inner
CC       surface of the cell membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P97789-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P97789-2; Sequence=VSP_016697;
CC       Name=3;
CC         IsoId=P97789-3; Sequence=VSP_016696, VSP_016698;
CC   -!- TISSUE SPECIFICITY: Expressed in heart, brain (spinal cord, dorsal
CC       root and superior cervical ganglia, neurons of the cerebrum and
CC       brain stem), peripheral nerve fibers in the skin and intestine,
CC       spleen, lung, liver, skeletal muscle, kidney and testis.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryo between 7 and 17 dpc.
CC   -!- SIMILARITY: Belongs to the 5'-3' exonuclease family.
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DR   EMBL; D88026; BAA21563.1; -; mRNA.
DR   EMBL; X91617; CAA62819.1; -; mRNA.
DR   EMBL; X91617; CAA62820.1; -; mRNA.
DR   EMBL; AK142311; BAE25024.1; -; mRNA.
DR   EMBL; AK162848; BAE37081.1; -; mRNA.
DR   EMBL; AK169840; BAE41404.1; -; mRNA.
DR   IPI; IPI00129132; -.
DR   IPI; IPI00668938; -.
DR   IPI; IPI00677614; -.
DR   PIR; T30174; T30174.
DR   PIR; T30175; T30175.
DR   PIR; T30244; T30244.
DR   RefSeq; NP_036046.2; NM_011916.2.
DR   UniGene; Mm.291179; -.
DR   ProteinModelPortal; P97789; -.
DR   SMR; P97789; 1-607.
DR   STRING; P97789; -.
DR   PhosphoSite; P97789; -.
DR   PRIDE; P97789; -.
DR   Ensembl; ENSMUST00000034981; ENSMUSP00000034981; ENSMUSG00000032410.
DR   GeneID; 24127; -.
DR   KEGG; mmu:24127; -.
DR   UCSC; uc009rbx.1; mouse.
DR   UCSC; uc009rby.1; mouse.
DR   CTD; 24127; -.
DR   MGI; MGI:891964; Xrn1.
DR   eggNOG; roNOG13464; -.
DR   GeneTree; ENSGT00600000084422; -.
DR   HOGENOM; HBG716448; -.
DR   HOVERGEN; HBG094164; -.
DR   InParanoid; P97789; -.
DR   OrthoDB; EOG49S65H; -.
DR   PhylomeDB; P97789; -.
DR   NextBio; 304159; -.
DR   ArrayExpress; P97789; -.
DR   Bgee; P97789; -.
DR   CleanEx; MM_XRN1; -.
DR   Genevestigator; P97789; -.
DR   GermOnline; ENSMUSG00000032410; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0004534; F:5'-3' exoribonuclease activity; TAS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0007569; P:cell aging; NAS:UniProtKB.
DR   GO; GO:0071044; P:histone mRNA catabolic process; ISS:UniProtKB.
DR   GO; GO:0007126; P:meiosis; NAS:UniProtKB.
DR   GO; GO:0006396; P:RNA processing; TAS:UniProtKB.
DR   GO; GO:0000723; P:telomere maintenance; NAS:UniProtKB.
DR   InterPro; IPR016494; 5_3_exoribonuclease_1.
DR   InterPro; IPR004859; Put_53exo.
DR   Pfam; PF03159; XRN_N; 1.
DR   PIRSF; PIRSF006743; Exonuclease_Xnr1; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; DNA-binding; Exonuclease; Hydrolase;
KW   Nuclease; Phosphoprotein; RNA-binding.
FT   CHAIN         1   1719       5'-3' exoribonuclease 1.
FT                                /FTId=PRO_0000071393.
FT   MOD_RES    1173   1173       Phosphoserine (By similarity).
FT   MOD_RES    1176   1176       Phosphoserine (By similarity).
FT   VAR_SEQ    1436   1436       P -> PSKKL (in isoform 3).
FT                                /FTId=VSP_016696.
FT   VAR_SEQ    1568   1580       Missing (in isoform 2).
FT                                /FTId=VSP_016697.
FT   VAR_SEQ    1661   1719       PQESPPASSSSSQAAQPVSSHVETASQGHVGSQPRSAPSSS
FT                                KRKSRKLAVNFSVSKPSE -> EFPGWVHLPVTSLTYGLWW
FT                                RLPG (in isoform 3).
FT                                /FTId=VSP_016698.
FT   CONFLICT     99     99       G -> A (in Ref. 1; BAA21563).
FT   CONFLICT    172    172       E -> D (in Ref. 3; BAE25024).
FT   CONFLICT    193    193       D -> G (in Ref. 3; BAE25024).
FT   CONFLICT   1085   1085       M -> L (in Ref. 1; BAA21563).
FT   CONFLICT   1243   1243       T -> I (in Ref. 1; BAA21563).
FT   CONFLICT   1261   1261       I -> L (in Ref. 3; BAE41404).
SQ   SEQUENCE   1719 AA;  194307 MW;  4FE6C888E3FE2459 CRC64;
     MGVPKFYRWI SERYPCLSEV VKEHQIPEFD NLYLDMNGII HQCSHPNDDD VHFRISDDKI
     FTDIFHYLEV LFRIIKPRKV FFMAVDGVAP RAKMNQQRGR RFRSAKEAED KIKKAIEKGE
     TLPTEARFDS NCITPGTEFM ARLHEHLKYF VNMKISTDKS WQGVTIYFSG HETPGEGEHK
     IMEFIRSEKA KPDHDPNTRH CLYGLDADLI MLGLTSHEAH FSLLREEVRF GGKKTQRVCA
     PEETTFHLLH LSLMREYIDY EFSALKEKIT FKYDIEKIID DWILMGFLVG NDFIPHLPHL
     HINHDALPLL YGTYIAILPE LGGYINESGH LNLPRFERYL VKLSDFDREH FSEVFVDLKW
     FESKVGNKYL NEAAGAAAEE AKNCKEKRKP KGQENSLSWA ALDKSEGEGV ASRDNFEDET
     EDDDLFETEF RQYKRTYYMT KMGVDVVSDE FLANQAACYV QAIQWILHYY YHGVQSWSWY
     YPYHYAPFLS DIRSISTLKI HFELGKPFKP FEQLLAVLPS ASKNLLPTCY QHLMTSEDSP
     IIEYYPPDFK TDLNGKQQEW EAVVLIPFID ETRLLEAMET CNHSLKKEER KRNQHSECLM
     CWYDRDTEFT YSSPWPEKFP AIERCCTRYK MISLDAWRVD INKNKITRVD QKALYFCGFP
     TLKHIKHKFF LKKSGVQVFQ QSSRGENLML EISVNAEPDE LRIENIASAV LGKAVFVNWP
     HLEEARVVAV SDGETKFYIE EPPGTQKVYL GKTAPPSKVI QLTDKEQSNW TKEIQGISEQ
     YLRRKGIIIN ETSAVVYAQL LTGRKYQISQ NGEVRLEKQW SKQILPFVYQ TIVKDIRAFD
     SRFSNIKTLD DLFPPRTMVF MLGTPYYGCT GEVQDSGDLI TEGRIRVVFS IPCEPNLDAL
     IQNQHKYSIK YNPGYVLAGR LGVSGYLVSR FTGSIFIGRG SRRNPHGDHK ANVGLNLKFN
     KKNEEVPGYT KKVGNEWMYS SAAEQLLAEY IERAPELFSY IAKNSQEDVF YEDDIWPGEN
     ENGAEKVQEI ITWLKGHPVS TLSRSSCDLH ILDAAIVEKI EEEVEKCKQR KSNKKVRVTV
     KPHLMYRPLE QQHGVIPDRD AEFRLFDRVV NVRESFSVPV GLRGTVIGIK GASREADVLF
     EVLFDEEFPG GLTIRCSPGR GYRLPTSALV NLSHGSRCET GNQKLTAIVK PQPSVSHCSA
     APSGHLGGLN HSPQSPFLPT QVPTKGDDEF CNIWQSLQGA GKTQHLQPTV QEKGAVLPQE
     ISQVTEGHKS GFTDHSVRHQ QRKHDSQRKF KEEYKSPKAE CQSQKLSSKQ TSGGSARCSI
     KLLKRNESPG TSEAQKVVTS YPNAVHKPPS GIENFLASLN LSKENEAQLP HHGEPPDEAD
     LSPQSFAMKG TRMLKEILKI DSPDTRDSKN DMKKSDNEAT VSSRRDERGV SAHPKPTCHM
     NKPHGTNEFQ NVASVDSVCW PGQMPPVSTP VTELSRICSL VGMPQPDFSF LRTTQTMTVC
     QVKLSNGLLV HGPQCHSESE AKERAALFAL QQLGSLGVSF PLPPPIFTNY PPAVPPGAVP
     PVFTQPTANI MPSSSHLFGS VSWRPPVPVA GNAFHYPSYP GTMPLAGGVP GGVHSQFIPL
     QVTKKRVANR KNFENKEAQS SQATPLQTNK PGSSEATKMT PQESPPASSS SSQAAQPVSS
     HVETASQGHV GSQPRSAPSS SKRKSRKLAV NFSVSKPSE
//
ID   CXAR_MOUSE              Reviewed;         365 AA.
AC   P97792; O09052; Q3ULD0; Q91W66; Q99KG0; Q9DBJ8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   08-MAR-2011, entry version 103.
DE   RecName: Full=Coxsackievirus and adenovirus receptor homolog;
DE            Short=CAR;
DE            Short=mCAR;
DE   Flags: Precursor;
GN   Name=Cxadr; Synonyms=Car;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC   STRAIN=C3H/Mai;
RX   MEDLINE=97250541; PubMed=9096397; DOI=10.1073/pnas.94.7.3352;
RA   Tomko R.P., Xu R., Philipson L.;
RT   "HCAR and MCAR: the human and mouse cellular receptors for subgroup C
RT   adenoviruses and group B coxsackieviruses.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:3352-3356(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION AS A VIRUS
RP   RECEPTOR.
RC   STRAIN=C57BL/6J; TISSUE=Colon, and Liver;
RX   MEDLINE=97190109; PubMed=9036860; DOI=10.1126/science.275.5304.1320;
RA   Bergelson J.M., Cunningham J.A., Droguett G., Kurt-Jones E.,
RA   Krithivas A., Hong J.S., Horwitz M.S., Crowell R.L., Finberg R.W.;
RT   "Isolation of a common receptor for Coxsackie B viruses and
RT   adenoviruses 2 and 5.";
RL   Science 275:1320-1323(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION AS A VIRUS
RP   RECEPTOR.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   MEDLINE=98080429; PubMed=9420240;
RA   Bergelson J.M., Krithivas A., Celi L., Droguett G., Horwitz M.S.,
RA   Wickham T., Crowell R.L., Finberg R.W.;
RT   "The murine CAR homolog is a receptor for coxsackie B viruses and
RT   adenoviruses.";
RL   J. Virol. 72:415-419(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP   GLYCOSYLATION, AND FUNCTION.
RX   MEDLINE=20276029; PubMed=10814828; DOI=10.1016/S0169-328X(00)00036-X;
RA   Honda T., Saitoh H., Masuko M., Katagiri-Abe T., Tominaga K.,
RA   Kozakai I., Kobayashi K., Kumanishi T., Watanabe Y.G., Odani S.,
RA   Kuwano R.;
RT   "The coxsackievirus-adenovirus receptor protein as a cell adhesion
RT   molecule in the developing mouse brain.";
RL   Brain Res. Mol. Brain Res. 77:19-28(2000).
RN   [7]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=22648080; PubMed=12763576; DOI=10.1016/S0165-3806(03)00035-X;
RA   Hotta Y., Honda T., Naito M., Kuwano R.;
RT   "Developmental distribution of coxsackie virus and adenovirus receptor
RT   localized in the nervous system.";
RL   Brain Res. Dev. Brain Res. 143:1-13(2003).
RN   [8]
RP   INTERACTION WITH DNAJC7 AND HSP90AA1.
RX   PubMed=14573755; DOI=10.1124/mol.64.5.1069;
RA   Kobayashi K., Sueyoshi T., Inoue K., Moore R., Negishi M.;
RT   "Cytoplasmic accumulation of the nuclear receptor CAR by a
RT   tetratricopeptide repeat protein in HepG2 cells.";
RL   Mol. Pharmacol. 64:1069-1075(2003).
RN   [9]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15533241; DOI=10.1186/1471-2121-5-42;
RA   Shaw C.A., Holland P.C., Sinnreich M., Allen C., Sollerbrant K.,
RA   Karpati G., Nalbantoglu J.;
RT   "Isoform-specific expression of the Coxsackie and adenovirus receptor
RT   (CAR) in neuromuscular junction and cardiac intercalated discs.";
RL   BMC Cell Biol. 5:42-42(2004).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-323, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293 AND SER-300, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Component of the epithelial apical junction complex that
CC       is essential for the tight junction integrity. Proposed to
CC       function as a homophilic cell adhesion molecule. Recruits MPDZ to
CC       intercellular contact sites. Probably involved in transepithelial
CC       migration of polymorphonuclear leukocytes (PMN) through adhesive
CC       interactions with AMICA1/JAML located in the plasma membrane of
CC       PMN (By similarity).
CC   -!- FUNCTION: In vitro, acts as a receptor for group B
CC       coxsackieviruses and subgroup C of adenoviruses (AD2 and AD5).
CC   -!- SUBUNIT: Monomer. Probably homodimer formed by 2 molecules on
CC       adjacent cells. Interacts with LNX, MPDZ, BAIAP1, DLG4, PRKCABP,
CC       TJP1 and CTNNB1 (By similarity). Interacts with DNAJC7. Probably
CC       part of a complex containing CXADR, HSP90AA1 and DNAJC7.
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
CC       membrane protein (By similarity). Cell junction, adherens junction
CC       (By similarity). Cell junction, tight junction (By similarity).
CC       Basolateral cell membrane; Single-pass type I membrane protein (By
CC       similarity). Note=Localized at the intercellular contacts. In
CC       epithelial cells localizes to the apical junction complex composed
CC       of tight and adherens junctions. In airway epithelial cells
CC       localized to basolateral membrane but not to apical surface (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Single-pass type I
CC       membrane protein (By similarity). Cell junction, adherens junction
CC       (By similarity). Cell junction, tight junction (By similarity).
CC       Basolateral cell membrane; Single-pass type I membrane protein (By
CC       similarity). Note=Localized at the intercellular contacts. In
CC       epithelial cells localizes to the apical junction complex composed
CC       of tight and adherens junctions. In airway epithelial cells
CC       localized to basolateral membrane but not to apical surface (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 3: Secreted (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P97792-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P97792-2; Sequence=VSP_014829;
CC       Name=3;
CC         IsoId=P97792-3; Sequence=VSP_014827, VSP_014828;
CC   -!- TISSUE SPECIFICITY: Expressed in liver, kidney, heart, lung, and
CC       brain. In skeletal muscle is found at the neuromuscular junction.
CC       In cardiac muscle, isoform 1 and isoform 2 are found at
CC       intercalated disks.
CC   -!- DEVELOPMENTAL STAGE: Expression starts in the embryonic ectoderm
CC       in the uterus on E6.5. Then it is strongly expressed in the
CC       neuroepithelium of the neural tube, the developing brain and the
CC       spinal cord from E8.5 to postnatal day 7 (P7), in the cranial
CC       motor nerves from E9.5 to E11.5, and in the optic nerve from E13.5
CC       to P7. Expression increases until perinatal period and decreases
CC       postnatally. Expressed in the immature neuroepithelium including
CC       progenitor cells it still occurs in a few proliferating cells of
CC       the hippocampal dentate gyrus, the subventricular zone of the
CC       lateral ventricles, and the rostral migratory stream over P21.
CC       Also expressed in heart, kidney and liver of newborn mice.
CC   -!- DOMAIN: The Ig-like C2-type 1 domain mediates homodimerization and
CC       interaction with JAML (By similarity).
CC   -!- DOMAIN: The PDZ-binding motif mediates interaction with MPDZ and
CC       BAIAP1 (By similarity).
CC   -!- PTM: N-glycosylated.
CC   -!- PTM: Palmitoylated on Cys-259 and/or Cys-260; required for proper
CC       localization to the plasma membrane (By similarity).
CC   -!- SIMILARITY: Contains 2 Ig-like C2-type (immunoglobulin-like)
CC       domains.
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DR   EMBL; U90715; AAC53148.1; -; mRNA.
DR   EMBL; Y10320; CAA71368.1; -; mRNA.
DR   EMBL; Y11929; CAA72679.1; -; mRNA.
DR   EMBL; AK004908; BAB23660.2; -; mRNA.
DR   EMBL; AK145569; BAE26518.1; -; mRNA.
DR   EMBL; BC004680; AAH04680.1; -; mRNA.
DR   EMBL; BC016457; AAH16457.1; -; mRNA.
DR   IPI; IPI00270376; -.
DR   IPI; IPI00271453; -.
DR   IPI; IPI00474948; -.
DR   RefSeq; NP_001020363.1; NM_001025192.2.
DR   RefSeq; NP_034118.1; NM_009988.3.
DR   UniGene; Mm.66222; -.
DR   PDB; 3JZ7; X-ray; 2.19 A; A=20-233.
DR   PDB; 3MJ7; X-ray; 2.80 A; B=18-236.
DR   PDBsum; 3JZ7; -.
DR   PDBsum; 3MJ7; -.
DR   ProteinModelPortal; P97792; -.
DR   SMR; P97792; 25-233.
DR   MINT; MINT-253068; -.
DR   STRING; P97792; -.
DR   PhosphoSite; P97792; -.
DR   PRIDE; P97792; -.
DR   Ensembl; ENSMUST00000023572; ENSMUSP00000023572; ENSMUSG00000022865.
DR   Ensembl; ENSMUST00000114229; ENSMUSP00000109867; ENSMUSG00000022865.
DR   GeneID; 13052; -.
DR   KEGG; mmu:13052; -.
DR   UCSC; uc007zsm.1; mouse.
DR   UCSC; uc007zsn.1; mouse.
DR   UCSC; uc007zso.1; mouse.
DR   CTD; 13052; -.
DR   MGI; MGI:1201679; Cxadr.
DR   eggNOG; roNOG13169; -.
DR   GeneTree; ENSGT00600000084393; -.
DR   HOGENOM; HBG715825; -.
DR   HOVERGEN; HBG105787; -.
DR   InParanoid; P97792; -.
DR   OMA; EDFERAP; -.
DR   OrthoDB; EOG4894MW; -.
DR   PhylomeDB; P97792; -.
DR   NextBio; 282970; -.
DR   ArrayExpress; P97792; -.
DR   Bgee; P97792; -.
DR   CleanEx; MM_CXADR; -.
DR   Genevestigator; P97792; -.
DR   GermOnline; ENSMUSG00000022865; Mus musculus.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0048739; P:cardiac muscle fiber development; IMP:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0045216; P:cell-cell junction organization; IMP:MGI.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR   GO; GO:0060044; P:negative regulation of cardiac muscle cell proliferation; IMP:MGI.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell adhesion; Cell junction;
KW   Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor; Repeat;
KW   Secreted; Signal; Tight junction; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     19       Potential.
FT   CHAIN        20    365       Coxsackievirus and adenovirus receptor
FT                                homolog.
FT                                /FTId=PRO_0000014740.
FT   TOPO_DOM     20    237       Extracellular (Potential).
FT   TRANSMEM    238    258       Helical; (Potential).
FT   TOPO_DOM    259    365       Cytoplasmic (Potential).
FT   DOMAIN       20    136       Ig-like C2-type 1.
FT   DOMAIN      141    228       Ig-like C2-type 2.
FT   MOTIF       360    365       PDZ-binding (By similarity).
FT   MOD_RES     293    293       Phosphoserine.
FT   MOD_RES     300    300       Phosphoserine.
FT   MOD_RES     306    306       Phosphoserine (By similarity).
FT   MOD_RES     323    323       Phosphoserine.
FT   MOD_RES     332    332       Phosphoserine (By similarity).
FT   LIPID       259    259       S-palmitoyl cysteine (By similarity).
FT   LIPID       260    260       S-palmitoyl cysteine (By similarity).
FT   CARBOHYD    106    106       N-linked (GlcNAc...) (Potential).
FT   DISULFID     41    120       By similarity.
FT   DISULFID    162    212       By similarity.
FT   VAR_SEQ     139    164       VKPSGTRCFVDGSEEIGNDFKLKCEP -> GKSSFLLSTGV
FT                                EWGGGAELQGGREGG (in isoform 3).
FT                                /FTId=VSP_014827.
FT   VAR_SEQ     165    365       Missing (in isoform 3).
FT                                /FTId=VSP_014828.
FT   VAR_SEQ     340    365       VAAPNLSRMGAVPVMIPAQSKDGSIV -> FKYAYKTDGIT
FT                                VV (in isoform 2).
FT                                /FTId=VSP_014829.
FT   STRAND       26     32
FT   STRAND       37     39
FT   STRAND       54     59
FT   STRAND       62     65
FT   STRAND       68     74
FT   HELIX        85     87
FT   STRAND       91     94
FT   STRAND      105    107
FT   HELIX       112    114
FT   STRAND      118    123
FT   STRAND      129    138
FT   STRAND      144    149
FT   STRAND      158    166
FT   STRAND      172    177
FT   HELIX       186    191
FT   STRAND      194    199
FT   HELIX       204    206
FT   STRAND      210    215
FT   STRAND      221    225
SQ   SEQUENCE   365 AA;  39948 MW;  5445B4B52A34B2A2 CRC64;
     MARLLCFVLL CGIADFTSGL SITTPEQRIE KAKGETAYLP CKFTLSPEDQ GPLDIEWLIS
     PSDNQIVDQV IILYSGDKIY DNYYPDLKGR VHFTSNDVKS GDASINVTNL QLSDIGTYQC
     KVKKAPGVAN KKFLLTVLVK PSGTRCFVDG SEEIGNDFKL KCEPKEGSLP LQFEWQKLSD
     SQTMPTPWLA EMTSPVISVK NASSEYSGTY SCTVQNRVGS DQCMLRLDVV PPSNRAGTIA
     GAVIGTLLAL VLIGAILFCC HRKRREEKYE KEVHHDIRED VPPPKSRTST ARSYIGSNHS
     SLGSMSPSNM EGYSKTQYNQ VPSEDFERAP QSPTLAPAKV AAPNLSRMGA VPVMIPAQSK
     DGSIV
//
ID   SHPS1_MOUSE             Reviewed;         513 AA.
AC   P97797; O08907; O35924; O88555; O88556; P97796; Q8R559; Q9QX57;
AC   Q9WTN4;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   08-FEB-2011, entry version 108.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type substrate 1;
DE            Short=SHP substrate 1;
DE            Short=SHPS-1;
DE   AltName: Full=Brain Ig-like molecule with tyrosine-based activation motifs;
DE            Short=Bit;
DE   AltName: Full=CD172 antigen-like family member A;
DE   AltName: Full=Inhibitory receptor SHPS-1;
DE   AltName: Full=MyD-1 antigen;
DE   AltName: Full=Signal-regulatory protein alpha-1;
DE            Short=Sirp-alpha-1;
DE            Short=mSIRP-alpha1;
DE   AltName: Full=p84;
DE   AltName: CD_antigen=CD172a;
DE   Flags: Precursor;
GN   Name=Sirpa; Synonyms=Bit, Myd1, Ptpns1, Shps1, Sirp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain;
RX   MEDLINE=97223399; PubMed=9070220; DOI=10.1006/bbrc.1996.6047;
RA   Yamao T., Matozaki T., Amano K., Matsuda Y., Takahashi N., Ochi F.,
RA   Fujioka Y., Kasuga M.;
RT   "Mouse and human SHPS-1: molecular cloning of cDNAs and chromosomal
RT   localization of genes.";
RL   Biochem. Biophys. Res. Commun. 231:61-67(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS ALA-29; ARG-67;
RP   ARG-91; THR-96; SER-128; PRO-194 AND ASN-224.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=97230468; PubMed=9073522; DOI=10.1006/geno.1996.4581;
RA   Ohnishi H., Kubota M., Sano S.;
RT   "BIT (Bit) maps to mouse chromosome 2.";
RL   Genomics 40:504-506(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), PROTEIN SEQUENCE OF
RP   32-53 AND 422-433 (ISOFORM 2), VARIANTS ALA-29; ARG-91; THR-96 AND
RP   SER-128, GLYCOSYLATION, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Brain, and Cerebellum;
RX   MEDLINE=98012243; PubMed=9348339;
RA   Comu S., Weng W., Olinsky S., Ishwad P., Mi Z., Hempel J., Watkins S.,
RA   Lagenaur C.F., Narayanan V.;
RT   "The murine P84 neural adhesion molecule is SHPS-1, a member of the
RT   phosphatase-binding protein family.";
RL   J. Neurosci. 17:8702-8710(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), VARIANTS ALA-29;
RP   ARG-67; PRO-74; ALA-83; 86-TYR-VAL-87; ILE-90; ARG-91; THR-96;
RP   ALA-114; ILE-118; SER-128; PRO-194; ASN-224; PHE-351 AND ASP-365,
RP   GLYCOSYLATION, PHOSPHORYLATION AT TYROSINE RESIDUES, INTERACTION WITH
RP   PTPN6, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Fetal thymus;
RX   MEDLINE=98380500; PubMed=9712903; DOI=10.1074/jbc.273.35.22719;
RA   Veillette A., Thibaudeau E., Latour S.;
RT   "High expression of inhibitory receptor SHPS-1 and its association
RT   with protein tyrosine phosphatase SHP-1 in macrophages.";
RL   J. Biol. Chem. 273:22719-22728(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3),
RP   VARIANTS ALA-29; ARG-67; PRO-74; ALA-83; 86-TYR-VAL-87; ILE-90;
RP   ARG-91; THR-96; ALA-114; ILE-118; SER-128; PRO-194; ASN-224; PHE-351
RP   AND ASP-365, AND GLYCOSYLATION.
RC   STRAIN=129/SvJ, and C57BL/6; TISSUE=Brain, and Liver;
RX   MEDLINE=20053880; PubMed=10585853; DOI=10.1042/0264-6021:3440667;
RA   Sano S., Ohnishi H., Kubota M.;
RT   "Gene structure of mouse BIT/SHPS-1.";
RL   Biochem. J. 344:667-675(1999).
RN   [6]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 2), AND VARIANTS ALA-29; ARG-67; PRO-74;
RP   ALA-83; 86-TYR-VAL-87; ILE-90; ARG-91; THR-96; ALA-114; ILE-118;
RP   SER-128; PRO-194; ASN-224; PHE-351 AND ASP-365.
RC   STRAIN=ILS, and ISS;
RX   MEDLINE=21363810; PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT PRO-194.
RC   TISSUE=Placenta;
RA   Wang H., Chen Z., Ullrich A.;
RT   "Epidermal growth factor-induced association of SHP2 with mouse SIRP-
RT   alpha1.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=90152134; PubMed=2303162; DOI=10.1016/0012-1606(90)90249-I;
RA   Chuang W., Lagenaur C.F.;
RT   "Central nervous system antigen P84 can serve as a substrate for
RT   neurite outgrowth.";
RL   Dev. Biol. 137:219-232(1990).
RN   [9]
RP   GLYCOSYLATION, PHOSPHORYLATION BY JAK2 IN RESPONSE TO GROWTH HORMONE,
RP   AND INTERACTION WITH JAK2 AND PTPN11.
RX   MEDLINE=98175985; PubMed=9507023; DOI=10.1074/jbc.273.12.7112;
RA   Stofega M.R., Wang H., Ullrich A., Carter-Su C.;
RT   "Growth hormone regulation of SIRP and SHP-2 tyrosyl phosphorylation
RT   and association.";
RL   J. Biol. Chem. 273:7112-7117(1998).
RN   [10]
RP   INTERACTION WITH CD47, AND TISSUE SPECIFICITY.
RX   MEDLINE=99091586; PubMed=9872987; DOI=10.1074/jbc.274.2.559;
RA   Jiang P., Lagenaur C.F., Narayanan V.;
RT   "Integrin-associated protein is a ligand for the P84 neural adhesion
RT   molecule.";
RL   J. Biol. Chem. 274:559-562(1999).
RN   [11]
RP   INTERACTION WITH FGR.
RX   MEDLINE=20130295; PubMed=10662797; DOI=10.1084/jem.191.3.515;
RA   Gresham H.D., Dale B.M., Potter J.W., Chang P.W., Vines C.M.,
RA   Lowell C.A., Lagenaur C.F., Willman C.L.;
RT   "Negative regulation of phagocytosis in murine macrophages by the Src
RT   kinase family member, Fgr.";
RL   J. Exp. Med. 191:515-528(2000).
RN   [12]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-246, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Plasma;
RX   PubMed=16944957; DOI=10.1021/pr060186m;
RA   Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
RA   Gevaert K.;
RT   "Proteome-wide characterization of N-glycosylation events by diagonal
RT   chromatography.";
RL   J. Proteome Res. 5:2438-2447(2006).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-144; TYR-481 AND
RP   TYR-505, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Immunoglobulin-like cell surface receptor for CD47. Acts
CC       as docking protein and induces translocation of PTPN6, PTPN11 and
CC       other binding partners from the cytosol to the plasma membrane.
CC       Supports adhesion of cerebellar neurons, neurite outgrowth and
CC       glial cell attachment. May play a key role in intracellular
CC       signaling during synaptogenesis and in synaptic function. Involved
CC       in the negative regulation of receptor tyrosine kinase-coupled
CC       cellular responses induced by cell adhesion, growth factors or
CC       insulin. Mediates negative regulation of phagocytosis, mast cell
CC       activation and dendritic cell activation. CD47 binding prevents
CC       maturation of immature dendritic cells and inhibits cytokine
CC       production by mature dendritic cells (By similarity).
CC   -!- SUBUNIT: Binds PTPN11 when tyrosine-phosphorylated, except in
CC       macrophages, where it primarily binds PTPN6. Binds GRB2 vitro.
CC       Binds FGR. Binds JAK2 irrespective of its phosphorylation status
CC       and forms a stable complex. Binds SCAP1 and/or SCAP2. The
CC       resulting complex recruits FYB. Binds PTK2B (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1; Synonyms=a;
CC         IsoId=P97797-1; Sequence=Displayed;
CC       Name=2; Synonyms=a', Large;
CC         IsoId=P97797-2; Sequence=VSP_007032;
CC       Name=3; Synonyms=b, Small;
CC         IsoId=P97797-3; Sequence=VSP_007031;
CC   -!- TISSUE SPECIFICITY: Highly expressed in cerebral cortex, brain,
CC       spinal cord, cerebellum and spleen, and at much lower levels in
CC       kidney, thymus, heart, lung and liver. Within the cerebellum,
CC       highly expressed throughout the molecular layer, and in synaptic
CC       glomeruli in the granule cell layer. Detected in neurons of the
CC       hippocampus and dentate gyrus, and in olfactory bulb. Not detected
CC       in Purkinje cells. Highly expressed in the plexiform layers, optic
CC       fiber layer and the outer segments of the photoreceptor layer in
CC       the retina. Highly expressed in macrophages. Isoform 3 is detected
CC       at very low levels in all tissues tested.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in the CNS of embryos from
CC       day 7 to 17.
CC   -!- PTM: N-glycosylated.
CC   -!- PTM: Phosphorylated on tyrosine residues.
CC   -!- SIMILARITY: Contains 2 Ig-like C1-type (immunoglobulin-like)
CC       domains.
CC   -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC       domain.
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CC   -----------------------------------------------------------------------
DR   EMBL; D87967; BAA13520.1; -; mRNA.
DR   EMBL; D87968; BAA13521.1; -; mRNA.
DR   EMBL; D85785; BAA20376.1; -; mRNA.
DR   EMBL; U89694; AAB92591.1; -; mRNA.
DR   EMBL; AF072543; AAC24886.1; -; mRNA.
DR   EMBL; AF072544; AAC24887.1; -; mRNA.
DR   EMBL; AB024507; BAA89290.1; -; Genomic_DNA.
DR   EMBL; AB018194; BAA76555.1; -; mRNA.
DR   EMBL; AB024507; BAA89289.1; -; Genomic_DNA.
DR   EMBL; AF332079; AAK56107.1; -; mRNA.
DR   EMBL; AF332080; AAK56108.1; -; mRNA.
DR   EMBL; Y10349; CAA71375.1; -; mRNA.
DR   IPI; IPI00129158; -.
DR   IPI; IPI00221791; -.
DR   IPI; IPI00221792; -.
DR   PIR; JC5288; JC5288.
DR   PIR; JC5289; JC5289.
DR   RefSeq; NP_001171117.1; NM_001177646.1.
DR   RefSeq; NP_001171118.1; NM_001177647.1.
DR   RefSeq; NP_031573.2; NM_007547.3.
DR   UniGene; Mm.1682; -.
DR   PDB; 2YZ1; X-ray; 1.40 A; A/B=32-146.
DR   PDBsum; 2YZ1; -.
DR   ProteinModelPortal; P97797; -.
DR   SMR; P97797; 32-346.
DR   IntAct; P97797; 3.
DR   STRING; P97797; -.
DR   PhosphoSite; P97797; -.
DR   PRIDE; P97797; -.
DR   Ensembl; ENSMUST00000049262; ENSMUSP00000049022; ENSMUSG00000037902.
DR   Ensembl; ENSMUST00000099113; ENSMUSP00000096713; ENSMUSG00000037902.
DR   Ensembl; ENSMUST00000103202; ENSMUSP00000099491; ENSMUSG00000037902.
DR   GeneID; 19261; -.
DR   KEGG; mmu:19261; -.
DR   UCSC; uc008mib.1; mouse.
DR   CTD; 19261; -.
DR   MGI; MGI:108563; Sirpa.
DR   GeneTree; ENSGT00440000033339; -.
DR   HOVERGEN; HBG056632; -.
DR   InParanoid; P97797; -.
DR   ArrayExpress; P97797; -.
DR   Bgee; P97797; -.
DR   CleanEx; MM_SIRPA; -.
DR   Genevestigator; P97797; -.
DR   GermOnline; ENSMUSG00000037902; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; IDA:MGI.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0007015; P:actin filament organization; IMP:MGI.
DR   GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
DR   GO; GO:0006928; P:cellular component movement; IMP:MGI.
DR   GO; GO:0006911; P:phagocytosis, engulfment; IDA:MGI.
DR   GO; GO:0006910; P:phagocytosis, recognition; IDA:MGI.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; IDA:MGI.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003006; Ig/MHC_CS.
DR   InterPro; IPR003597; Ig_C1-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3.
DR   Pfam; PF07654; C1-set; 2.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00407; IGc1; 2.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS00290; IG_MHC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW   Phosphoprotein; Polymorphism; Repeat; SH3-binding; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     31
FT   CHAIN        32    513       Tyrosine-protein phosphatase non-receptor
FT                                type substrate 1.
FT                                /FTId=PRO_0000014942.
FT   TOPO_DOM     32    373       Extracellular (Potential).
FT   TRANSMEM    374    394       Helical; (Potential).
FT   TOPO_DOM    395    511       Cytoplasmic (Potential).
FT   DOMAIN       32    137       Ig-like V-type.
FT   DOMAIN      149    248       Ig-like C1-type 1.
FT   DOMAIN      255    343       Ig-like C1-type 2.
FT   MOTIF       440    443       SH2-binding (Potential).
FT   MOTIF       450    455       SH3-binding (Potential).
FT   MOTIF       464    467       SH2-binding (Potential).
FT   MOTIF       481    484       SH2-binding (Potential).
FT   MOTIF       505    508       SH2-binding (Potential).
FT   MOD_RES     144    144       Phosphotyrosine.
FT   MOD_RES     440    440       Phosphotyrosine; by Tyr-kinases
FT                                (Potential).
FT   MOD_RES     464    464       Phosphotyrosine; by Tyr-kinases
FT                                (Potential).
FT   MOD_RES     481    481       Phosphotyrosine; by Tyr-kinases (By
FT                                similarity).
FT   MOD_RES     505    505       Phosphotyrosine; by Tyr-kinases (By
FT                                similarity).
FT   CARBOHYD     54     54       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     92     92       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    168    168       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    180    180       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    205    205       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    209    209       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    246    246       N-linked (GlcNAc...).
FT   CARBOHYD    271    271       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    293    293       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    302    302       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    312    312       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    320    320       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    345    345       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    367    367       N-linked (GlcNAc...) (Potential).
FT   DISULFID     55    121       Potential.
FT   DISULFID    171    229       Potential.
FT   DISULFID    274    332       Potential.
FT   VAR_SEQ     147    364       Missing (in isoform 3).
FT                                /FTId=VSP_007031.
FT   VAR_SEQ     425    428       Missing (in isoform 2).
FT                                /FTId=VSP_007032.
FT   VARIANT      29     29       V -> A (in strain: BALB/c, C57BL/6 and
FT                                ILS).
FT   VARIANT      67     67       K -> R (in strain: BALB/c, C57BL/6 and
FT                                ILS).
FT   VARIANT      74     74       Q -> P (in strain: C57BL/6 and ILS).
FT   VARIANT      83     83       T -> A (in strain: C57BL/6 and ILS).
FT   VARIANT      86     87       HF -> YV (in strain: C57BL/6 and ILS).
FT   VARIANT      90     90       V -> I (in strain: C57BL/6 and ILS).
FT   VARIANT      91     91       T -> R (in strain: BALB/c, C57BL/6 and
FT                                ILS).
FT   VARIANT      96     96       A -> T (in strain: BALB/c, C57BL/6 and
FT                                ILS).
FT   VARIANT     114    114       E -> A (in strain: C57BL/6 and ILS).
FT   VARIANT     118    118       T -> I (in strain: C57BL/6 and ILS).
FT   VARIANT     128    128       P -> S (in strain: BALB/c, C57BL/6 and
FT                                ILS).
FT   VARIANT     194    194       H -> P (in strain: BALB/c, C57BL/6 and
FT                                ILS).
FT   VARIANT     224    224       H -> N (in strain: BALB/c, C57BL/6 and
FT                                ILS).
FT   VARIANT     351    351       L -> F (in strain: C57BL/6 and ILS).
FT   VARIANT     365    365       G -> D (in strain: C57BL/6 and ILS).
FT   CONFLICT      6      6       Missing (in Ref. 7; CAA71375).
FT   CONFLICT     10     10       R -> L (in Ref. 3; AAB92591).
FT   CONFLICT     32     34       KEL -> TEV (in Ref. 2; BAA20376).
FT   CONFLICT     52     52       V -> I (in Ref. 2; BAA20376).
FT   CONFLICT     57     57       L -> V (in Ref. 2; BAA20376).
FT   CONFLICT     74     77       QSRL -> KAGC (in Ref. 7; CAA71375).
FT   CONFLICT    126    126       K -> R (in Ref. 2; BAA20376 and 3;
FT                                AAB92591).
FT   CONFLICT    154    156       VSG -> YPV (in Ref. 7; CAA71375).
FT   CONFLICT    164    164       D -> Y (in Ref. 7; CAA71375).
FT   CONFLICT    263    263       S -> P (in Ref. 2; BAA20376).
FT   CONFLICT    276    276       A -> D (in Ref. 7; CAA71375).
FT   CONFLICT    448    449       EK -> RR (in Ref. 7; CAA71375).
FT   CONFLICT    454    458       RAPEP -> GSLEFL (in Ref. 7; CAA71375).
FT   CONFLICT    490    490       S -> N (in Ref. 2; BAA20376 and 3;
FT                                AAB92591).
FT   STRAND       40     45
FT   STRAND       51     53
FT   STRAND       56     58
FT   STRAND       66     73
FT   STRAND       77     82
FT   TURN         87     89
FT   STRAND       92     95
FT   STRAND       98    100
FT   STRAND      106    108
FT   HELIX       113    115
FT   STRAND      117    125
FT   STRAND      128    131
FT   STRAND      133    137
FT   STRAND      141    145
SQ   SEQUENCE   513 AA;  56425 MW;  2AFDDD5FA6C1EC7C CRC64;
     MEPAGPAPGR LGPLLLCLLL SASCFCTGVT GKELKVTQPE KSVSVAAGDS TVLNCTLTSL
     LPVGPIKWYR GVGQSRLLIY SFTGEHFPRV TNVSDATKRN NMDFSIRISN VTPEDAGTYY
     CVKFQKGPSE PDTEIQSGGG TEVYVLAKPS PPEVSGPADR GIPDQKVNFT CKSHGFSPRN
     ITLKWFKDGQ ELHHLETTVN PSGKNVSYNI SSTVRVVLNS MDVHSKVICE VAHITLDRSP
     LRGIANLSNF IRVSPTVKVT QQSPTSMNQV NLTCRAERFY PEDLQLIWLE NGNVSRNDTP
     KNLTKNTDGT YNYTSLFLVN SSAHREDVVF TCQVKHDQQP AITRNHTVLG LAHSSDQGSM
     QTFPGNNATH NWNVFIGVGV ACALLVVLLM AALYLLRIKQ KKAKGSTSST RLHEPEKNAR
     EITQVQSLIQ DTNDINDITY ADLNLPKEKK PAPRAPEPNN HTEYASIETG KVPRPEDTLT
     YADLDMVHLS RAQPAPKPEP SFSEYASVQV QRK
//
ID   NEO1_MOUSE              Reviewed;        1493 AA.
AC   P97798;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   08-MAR-2011, entry version 106.
DE   RecName: Full=Neogenin;
DE   Flags: Precursor;
GN   Name=Neo1; Synonyms=Ngn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC   TISSUE=Brain;
RX   MEDLINE=97407661; PubMed=9264410; DOI=10.1038/sj.onc.1201225;
RA   Keeling S.L., Gad J.M., Cooper H.M.;
RT   "Mouse neogenin, a DCC-like molecule, has four splice variants and is
RT   expressed widely in the adult mouse and during embryogenesis.";
RL   Oncogene 15:691-700(1997).
RN   [2]
RP   INTERACTION WITH RGMA.
RX   PubMed=17389603; DOI=10.1074/jbc.M610901200;
RA   Conrad S., Genth H., Hofmann F., Just I., Skutella T.;
RT   "Neogenin-RGMa signaling at the growth cone is bone morphogenetic
RT   protein-independent and involves RhoA, ROCK, and PKC.";
RL   J. Biol. Chem. 282:16423-16433(2007).
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221 AND ASN-501, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221; ASN-501 AND ASN-670,
RP   AND MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: May be involved as a regulatory protein in the
CC       transition of undifferentiated proliferating cells to their
CC       differentiated state. May also function as a cell adhesion
CC       molecule in a broad spectrum of embryonic and adult tissues.
CC   -!- SUBUNIT: Interacts with RGMA.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1;
CC         IsoId=P97798-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P97798-2; Sequence=VSP_002594;
CC       Name=3;
CC         IsoId=P97798-3; Sequence=VSP_002595;
CC         Note=Expression developmentally regulated;
CC       Name=4;
CC         IsoId=P97798-4; Sequence=VSP_002596;
CC         Note=Expression developmentally regulated;
CC       Name=5;
CC         IsoId=P97798-5; Sequence=VSP_002597;
CC         Note=Expression developmentally regulated;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- DEVELOPMENTAL STAGE: Expressed ubiquitously throughout the mid to
CC       late stages of gestation and in adult tissues. Strong expression
CC       is observed in the ventral region of the ventricular zone of the
CC       E15.5 mouse neural tube, as well as in the ventricular zones of
CC       the mesencephalon and rhombencephalon. Isoform 3 and isoform 4 are
CC       expressed at higher level compared to other isoforms between E11.5
CC       and E16.5.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. DCC family.
CC   -!- SIMILARITY: Contains 6 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 4 Ig-like C2-type (immunoglobulin-like)
CC       domains.
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DR   EMBL; Y09535; CAA70727.1; -; mRNA.
DR   IPI; IPI00129159; -.
DR   IPI; IPI00222049; -.
DR   IPI; IPI00222052; -.
DR   IPI; IPI00222053; -.
DR   IPI; IPI00222057; -.
DR   UniGene; Mm.42249; -.
DR   UniGene; Mm.461831; -.
DR   ProteinModelPortal; P97798; -.
DR   SMR; P97798; 57-1083.
DR   STRING; P97798; -.
DR   PhosphoSite; P97798; -.
DR   PRIDE; P97798; -.
DR   Ensembl; ENSMUST00000068664; ENSMUSP00000063656; ENSMUSG00000032340.
DR   Ensembl; ENSMUST00000114096; ENSMUSP00000109731; ENSMUSG00000032340.
DR   Ensembl; ENSMUST00000114098; ENSMUSP00000109733; ENSMUSG00000032340.
DR   UCSC; uc009pxk.1; mouse.
DR   MGI; MGI:1097159; Neo1.
DR   eggNOG; roNOG06017; -.
DR   GeneTree; ENSGT00590000082947; -.
DR   HOGENOM; HBG358293; -.
DR   HOVERGEN; HBG005455; -.
DR   InParanoid; P97798; -.
DR   OrthoDB; EOG4FR0QS; -.
DR   ArrayExpress; P97798; -.
DR   Bgee; P97798; -.
DR   CleanEx; MM_NEO1; -.
DR   Genevestigator; P97798; -.
DR   GermOnline; ENSMUSG00000032340; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; EXP:Reactome.
DR   GO; GO:0045296; F:cadherin binding; IDA:MGI.
DR   GO; GO:0004872; F:receptor activity; IPI:MGI.
DR   GO; GO:0030528; F:transcription regulator activity; IDA:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007520; P:myoblast fusion; IMP:MGI.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR010560; Neogenin_C.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 10.
DR   Pfam; PF00041; fn3; 6.
DR   Pfam; PF07679; I-set; 4.
DR   Pfam; PF06583; Neogenin_C; 1.
DR   SMART; SM00060; FN3; 6.
DR   SMART; SM00408; IGc2; 4.
DR   SUPFAM; SSF49265; FN_III-like; 6.
DR   PROSITE; PS50853; FN3; 6.
DR   PROSITE; PS50835; IG_LIKE; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW   Glycoprotein; Immunoglobulin domain; Membrane; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     36       Potential.
FT   CHAIN        37   1493       Neogenin.
FT                                /FTId=PRO_0000015044.
FT   TOPO_DOM     37   1136       Extracellular (Potential).
FT   TRANSMEM   1137   1157       Helical; (Potential).
FT   TOPO_DOM   1158   1493       Cytoplasmic (Potential).
FT   DOMAIN       63    158       Ig-like C2-type 1.
FT   DOMAIN      163    249       Ig-like C2-type 2.
FT   DOMAIN      254    347       Ig-like C2-type 3.
FT   DOMAIN      352    437       Ig-like C2-type 4.
FT   DOMAIN      470    563       Fibronectin type-III 1.
FT   DOMAIN      570    658       Fibronectin type-III 2.
FT   DOMAIN      664    759       Fibronectin type-III 3.
FT   DOMAIN      766    858       Fibronectin type-III 4.
FT   DOMAIN      884    980       Fibronectin type-III 5.
FT   DOMAIN      985   1082       Fibronectin type-III 6.
FT   COMPBIAS   1149   1153       Poly-Val.
FT   CARBOHYD     84     84       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    221    221       N-linked (GlcNAc...).
FT   CARBOHYD    337    337       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    501    501       N-linked (GlcNAc...).
FT   CARBOHYD    520    520       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    670    670       N-linked (GlcNAc...).
FT   CARBOHYD    746    746       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    940    940       N-linked (GlcNAc...) (Potential).
FT   DISULFID     85    140       By similarity.
FT   DISULFID    184    232       By similarity.
FT   DISULFID    281    331       By similarity.
FT   DISULFID    373    421       By similarity.
FT   VAR_SEQ     442    461       Missing (in isoform 2).
FT                                /FTId=VSP_002594.
FT   VAR_SEQ     863    878       Missing (in isoform 3).
FT                                /FTId=VSP_002595.
FT   VAR_SEQ    1086   1096       Missing (in isoform 4).
FT                                /FTId=VSP_002596.
FT   VAR_SEQ    1279   1331       Missing (in isoform 5).
FT                                /FTId=VSP_002597.
SQ   SEQUENCE   1493 AA;  163160 MW;  441DE919D5E17C0E CRC64;
     MAAEREAGRL LCTSSSRRCC PPPPLLLLLP LLLLLGRPAS GAAATKSGPR RQSQGASVRT
     FTPFYFLVEP VDTLSVRGSS VILNCSAYSE PSPNIEWKKD GTFLNLESDD RRQLLPDGSL
     FISNVVHSKH NKPDEGFYQC VATVDNLGTI VSRTAKLTVA GLPRFTSQPE PSSVYVGNSA
     ILNCEVNADL VPFVRWEQNR QPLLLDDRIV KLPSGTLVIS NATEGDGGLY RCIVESGGPP
     KFSDEAELKV LQDPEEIVDL VFLMRPSSMM KVTGQSAVLP CVVSGLPAPV VRWMKNEEVL
     DTESSGRLVL LAGGCLEISD VTEDDAGTYF CIADNGNKTV EAQAELTVQV PPGFLKQPAN
     IYAHESMDIV FECEVTGKPT PTVKWVKNGD VVIPSDNFKI VKEHNLQVLG LVKSDEGFYQ
     CIAENDVGNA QAGAQLIILE HDVAIPTLPP TSLTSATTDH LAPATTGPLP SAPRDVVASL
     VSTRFIKLTW RTPASDPHGD NLTYSVFYTK EGVDRERVEN TSQPGEMQVT IQNLMPATVY
     IFKVMAQNKH GSGESSAPLR VETQPEVQLP GPAPNIRAYA TSPTSITVTW ETPLSGNGEI
     QNYKLYYMEK GTDKEQDIDV SSHSYTINGL KKYTEYSFRV VAYNKHGPGV STQDVAVRTL
     SDVPSAAPQN LSLEVRNSKS IVIHWQPPSS TTQNGQITGY KIRYRKASRK SDVTETLVTG
     TQLSQLIEGL DRGTEYNFRV AALTVNGTGP ATDWLSAETF ESDLDETRVP EVPSSLHVRP
     LVTSIVVSWT PPENQNIVVR GYAIGYGIGS PHAQTIKVDY KQRYYTIENL DPSSHYVITL
     KAFNNVGEGI PLYESAVTRP HTDTSEVDLF VINAPYTPVP DPTPMMPPVG VQASILSHDT
     IRITWADNSL PKHQKITDSR YYTVRWKTNI PANTKYKNAN ATTLSYLVTG LKPNTLYEFS
     VMVTKGRRSS TWSMTAHGAT FELVPTSPPK DVTVVSKEGK PRTIIVNWQP PSEANGKITG
     YIIYYSTDVN AEIHDWVIEP VVGNRLTHQI QELTLDTPYY FKIQARNSKG MGPMSEAVQF
     RTPKADSSDK MPNDQALGSA GKGSRLPDLG SDYKPPMSGS NSPHGSPTSP LDSNMLLVII
     VSVGVITIVV VVVIAVFCTR RTTSHQKKKR AACKSVNGSH KYKGNCKDVK PPDLWIHHER
     LELKPIDKSP DPNPVMTDTP IPRNSQDITP VDNSMDSNIH QRRNSYRGHE SEDSMSTLAG
     RRGMRPKMMM PFDSQPPQPV ISAHPIHSLD NPHHHFHSSS LASPARSHLY HPSSPWPIGT
     SMSLSDRANS TESVRNTPST DTMPASSSQT CCTDHQDPEG ATSSSYLASS QEEDSGQSLP
     TAHVRPSHPL KSFAVPAIPP PGPPLYDPAL PSTPLLSQQA LEPSTFHSVK TASIGTLGRS
     RPPMPVVVPS APEVQETTRM LEDSESSYEP DELTKEMAHL EGLMKDLNAI TTA
//
ID   SMN_MOUSE               Reviewed;         288 AA.
AC   P97801; O09092;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Survival motor neuron protein;
GN   Name=Smn1; Synonyms=Smn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=97224505; PubMed=9070939; DOI=10.1006/geno.1996.4551;
RA   Viollet L., Bertrandy S., Brunialti A.L.B., Lefebvre S., Burlet P.,
RA   Clermont O., Cruaud C., Guenet J.-L., Munnich A., Melki J.;
RT   "cDNA isolation, expression, and chromosomal localization of the mouse
RT   survival motor neuron gene (Smn).";
RL   Genomics 40:185-188(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=97264340; PubMed=9110173;
RA   Didonato C.J., Chen X.N., Noya D., Korenberg J.R., Nadeau J.H.,
RA   Simard L.R.;
RT   "Cloning, characterization, and copy number of the murine survival
RT   motor neuron gene: homolog of the spinal muscular atrophy-determining
RT   gene.";
RL   Genome Res. 7:339-352(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=97420785; PubMed=9275227; DOI=10.1073/pnas.94.18.9920;
RA   Schrank B., Goetz R., Gunnersen J.M., Ure J.M., Toyka K.V.,
RA   Smith A.G., Sendtner M.;
RT   "Inactivation of the survival motor neuron gene, a candidate gene for
RT   human spinal muscular atrophy, leads to massive cell death in early
RT   mouse embryos.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:9920-9925(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH SYNCRIP, AND MUTAGENESIS OF GLU-131; SER-257;
RP   TYR-267; THR-269 AND GLY-274.
RX   PubMed=11773003; DOI=10.1093/hmg/11.1.93;
RA   Rossoll W., Kroening A.-K., Ohndorf U.-M., Steegborn C., Jablonka S.,
RA   Sendtner M.;
RT   "Specific interaction of Smn, the spinal muscular atrophy determining
RT   gene product, with hnRNP-R and gry-rbp/hnRNP-Q: a role for Smn in RNA
RT   processing in motor axons?";
RL   Hum. Mol. Genet. 11:93-105(2002).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-28, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-28, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: The SMN complex plays an essential role in spliceosomal
CC       snRNP assembly in the cytoplasm and is required for pre-mRNA
CC       splicing in the nucleus. It may also play a role in the metabolism
CC       of snoRNPs (By similarity).
CC   -!- SUBUNIT: Component of an import snRNP complex composed of KPNB1,
CC       RNUT1, SMN1 and ZNF259. Part of the core SMN complex that contains
CC       SMN1, SIP1/GEMIN2, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7,
CC       GEMIN8 and STRAP/UNRIP. Interacts with DDX20, FBL, NOLA1, RNUT1
CC       and with several spliceosomal snRNP core Sm proteins, including
CC       SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE and with ILF3. Interacts with
CC       OSTF1, LSM10 and LSM11 (By similarity). Interacts with SYNCRIP.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Localized in subnuclear structures next to
CC       coiled bodies, called Gemini of Cajal bodies (Gems) (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the SMN family.
CC   -!- SIMILARITY: Contains 1 Tudor domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U63294; AAC53057.1; -; mRNA.
DR   EMBL; U77714; AAC53144.1; -; mRNA.
DR   EMBL; Y12835; CAA73356.1; -; mRNA.
DR   EMBL; BC045158; AAH45158.1; -; mRNA.
DR   IPI; IPI00129918; -.
DR   RefSeq; NP_035550.1; NM_011420.2.
DR   UniGene; Mm.2025; -.
DR   ProteinModelPortal; P97801; -.
DR   SMR; P97801; 87-141.
DR   IntAct; P97801; 3.
DR   STRING; P97801; -.
DR   PhosphoSite; P97801; -.
DR   PRIDE; P97801; -.
DR   Ensembl; ENSMUST00000022147; ENSMUSP00000022147; ENSMUSG00000021645.
DR   GeneID; 20595; -.
DR   KEGG; mmu:20595; -.
DR   UCSC; uc007rqh.1; mouse.
DR   CTD; 20595; -.
DR   MGI; MGI:109257; Smn1.
DR   eggNOG; roNOG16132; -.
DR   HOGENOM; HBG713387; -.
DR   HOVERGEN; HBG000211; -.
DR   InParanoid; P97801; -.
DR   OMA; REEQNLS; -.
DR   OrthoDB; EOG4W9J54; -.
DR   PhylomeDB; P97801; -.
DR   NextBio; 298911; -.
DR   ArrayExpress; P97801; -.
DR   Bgee; P97801; -.
DR   CleanEx; MM_SMN1; -.
DR   Genevestigator; P97801; -.
DR   GermOnline; ENSMUSG00000021645; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR010304; Survival_motor_neuron.
DR   InterPro; IPR002999; Tudor.
DR   InterPro; IPR018351; Tudor_subgroup.
DR   Pfam; PF06003; SMN; 1.
DR   SMART; SM00333; TUDOR; 1.
DR   PROSITE; PS50304; TUDOR; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   RNA-binding; Spliceosome.
FT   CHAIN         1    288       Survival motor neuron protein.
FT                                /FTId=PRO_0000218904.
FT   DOMAIN       88    148       Tudor.
FT   REGION      274    288       Required for interaction with SYNCRIP (By
FT                                similarity).
FT   COMPBIAS    190    196       Poly-Pro.
FT   COMPBIAS    212    222       Poly-Pro.
FT   COMPBIAS    239    243       Poly-Pro.
FT   MOD_RES      22     22       Phosphothreonine (By similarity).
FT   MOD_RES      25     25       Phosphoserine.
FT   MOD_RES      28     28       Phosphoserine.
FT   MUTAGEN     131    131       E->K: Loss of interaction with SYNCRIP.
FT   MUTAGEN     257    257       S->I: Loss of interaction with SYNCRIP.
FT   MUTAGEN     267    267       Y->C: Loss of interaction with SYNCRIP.
FT   MUTAGEN     269    269       T->I: Loss of interaction with SYNCRIP.
FT   MUTAGEN     274    274       G->V: Loss of interaction with SYNCRIP.
SQ   SEQUENCE   288 AA;  31254 MW;  757B3074649F7458 CRC64;
     MAMGSGGAGS EQEDTVLFRR GTGQSDDSDI WDDTALIKAY DKAVASFKHA LKNGDICETP
     DKPKGTARRK PAKKNKSQKK NATTPLKQWK VGDKCSAVWS EDGCIYPATI TSIDFKRETC
     VVVYTGYGNR EEQNLSDLLS PTCEVANSTE QNTQENESQV STDDSEHSSR SLRSKAHSKS
     KAAPWTSFLP PPPPMPGSGL GPGKPGLKFN GPPPPPPLPP PPFLPCWMPP FPSGPPIIPP
     PPPISPDCLD DTDALGSMLI SWYMSGYHTG YYMGFRQNKK EGKCSHTN
//
ID   FUMH_MOUSE              Reviewed;         507 AA.
AC   P97807; Q99JL0; Q9DCX0;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 2.
DT   08-MAR-2011, entry version 107.
DE   RecName: Full=Fumarate hydratase, mitochondrial;
DE            Short=Fumarase;
DE            EC=4.2.1.2;
DE   AltName: Full=EF-3;
DE   Flags: Precursor;
GN   Name=Fh; Synonyms=Fh1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-507.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 178-282.
RX   MEDLINE=97184476; PubMed=9032278;
RA   Fu X., Kamps M.P.;
RT   "E2a-Pbx1 induces aberrant expression of tissue-specific and
RT   developmentally regulated genes when expressed in NIH 3T3
RT   fibroblasts.";
RL   Mol. Cell. Biol. 17:1503-1512(1997).
RN   [4]
RP   PROTEIN SEQUENCE OF 49-71; 85-97; 99-112; 129-157; 181-210; 231-258;
RP   266-283; 294-308; 348-368; 419-441; 445-464 AND 481-501, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63; LYS-112 AND LYS-474, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- CATALYTIC ACTIVITY: (S)-malate = fumarate + H(2)O.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; (S)-
CC       malate from fumarate: step 1/1.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform Mitochondrial: Mitochondrion.
CC   -!- SUBCELLULAR LOCATION: Isoform Cytoplasmic: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Mitochondrial;
CC         IsoId=P97807-1; Sequence=Displayed;
CC       Name=Cytoplasmic;
CC         IsoId=P97807-2; Sequence=VSP_018967;
CC         Note=Initiator Met-1 is removed. Contains a N-acetylalanine at
CC         position 2 (By similarity);
CC   -!- PTM: Isoform Cytoplasmic is acetylated at position 2 (By
CC       similarity).
CC   -!- PTM: Acetylation of Lys-474 is observed in liver mitochondria from
CC       fasted mice but not from fed mice.
CC   -!- MISCELLANEOUS: There are 2 substrate binding sites: the catalytic
CC       A site, and the non-catalytic B site that may play a role in the
CC       transfer of substrate or product between the active site and the
CC       solvent. Alternatively, the B site may bind allosteric effectors
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II fumarase/aspartase family.
CC       Fumarase subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC006048; AAH06048.1; -; mRNA.
DR   EMBL; AK002379; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; U72679; AAB51039.1; -; mRNA.
DR   IPI; IPI00129928; -.
DR   IPI; IPI00759940; -.
DR   UniGene; Mm.41502; -.
DR   ProteinModelPortal; P97807; -.
DR   SMR; P97807; 46-507.
DR   STRING; P97807; -.
DR   PhosphoSite; P97807; -.
DR   REPRODUCTION-2DPAGE; IPI00759940; -.
DR   REPRODUCTION-2DPAGE; P97807; -.
DR   PRIDE; P97807; -.
DR   Ensembl; ENSMUST00000027810; ENSMUSP00000027810; ENSMUSG00000026526.
DR   UCSC; uc007dtn.1; mouse.
DR   MGI; MGI:95530; Fh1.
DR   eggNOG; roNOG08582; -.
DR   HOGENOM; HBG284369; -.
DR   HOVERGEN; HBG002183; -.
DR   InParanoid; P97807; -.
DR   OrthoDB; EOG4F1X31; -.
DR   PhylomeDB; P97807; -.
DR   BRENDA; 4.2.1.2; 244.
DR   NextBio; 285416; -.
DR   ArrayExpress; P97807; -.
DR   Bgee; P97807; -.
DR   CleanEx; MM_FH1; -.
DR   Genevestigator; P97807; -.
DR   GermOnline; ENSMUSG00000026526; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0045239; C:tricarboxylic acid cycle enzyme complex; IEA:InterPro.
DR   GO; GO:0004333; F:fumarate hydratase activity; IEA:EC.
DR   GO; GO:0006106; P:fumarate metabolic process; IEA:InterPro.
DR   GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR005677; Fum_hydII.
DR   InterPro; IPR018951; Fumarase_C_C.
DR   InterPro; IPR000362; Fumarate_lyase.
DR   InterPro; IPR020557; Fumarate_lyase_CS.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   InterPro; IPR022761; Lyase1_N.
DR   Pfam; PF10415; FumaraseC_C; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; L-Aspartase-like; 1.
DR   TIGRFAMs; TIGR00979; fumC_II; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative initiation; Cytoplasm;
KW   Direct protein sequencing; Lyase; Mitochondrion; Phosphoprotein;
KW   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT       1     41       Mitochondrion (By similarity).
FT   CHAIN        42    507       Fumarate hydratase, mitochondrial.
FT                                /FTId=PRO_0000010323.
FT   REGION      173    176       B site (By similarity).
FT   REGION      183    185       Substrate binding (By similarity).
FT   BINDING     144    144       Substrate (By similarity).
FT   MOD_RES      63     63       N6-acetyllysine.
FT   MOD_RES      77     77       N6-acetyllysine (By similarity).
FT   MOD_RES     112    112       N6-acetyllysine.
FT   MOD_RES     289    289       N6-acetyllysine (By similarity).
FT   MOD_RES     474    474       N6-acetyllysine.
FT   MOD_RES     488    488       Phosphotyrosine (By similarity).
FT   VAR_SEQ       1     40       Missing (in isoform Cytoplasmic).
FT                                /FTId=VSP_018967.
FT   CONFLICT    183    183       S -> N (in Ref. 2; AK002379).
FT   CONFLICT    236    236       A -> T (in Ref. 2; AK002379).
FT   CONFLICT    429    429       E -> D (in Ref. 2; AK002379).
SQ   SEQUENCE   507 AA;  54371 MW;  44552D1BF9608BFA CRC64;
     MYRALRLLAR SRRLLRVPSA GAAVSGEATT LPRCAPNVAR MASQNSFRVE FDTFGELKVP
     TDKYYGAQTV RSTMNFKIGG ATERMPIPVI QAFGILKRAA AEVNQEYGLD PKIASAIMKA
     ADEVAEGKLN DHFPLVVWQT GSGTQTNMNV NEVISNRAIE MLGGELGSKK PVHPNDHVNK
     SQSSNDTFPT AMHIAAAVEV HKVLLPGLQK LHDALSAKSK EFAQVIKIGR THTQDAVPLT
     LGQEFSGYVQ QVQYAMVRIK AAMPRIYELA AGGTAVGTGL NTRIGFAEKV AAKVAALTGL
     PFVTAPNKFE ALAAHDALVE LSGAMNTAAC SLMKIANDIR FLGSGPRSGL GELILPENEP
     GSSIMPGKVN PTQCEAMTMV AAQVMGNHVA VTVGGSNGHF ELNVFKPMMI KNVLHSARLL
     GDASVSFTEN CVVGIQANTE RINKLMNESL MLVTALNPHI GYDKAAKIAK TAHKNGSTLK
     ETAIELGYLT AEQFDEWVKP KDMLGPK
//
ID   P97811_MOUSE            Unreviewed;       198 AA.
AC   P97811;
DT   01-MAY-1997, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1997, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   SubName: Full=Sodium channel 2;
DE   Flags: Fragment;
GN   Name=Accn2; Synonyms=mBNaC2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=97188490; PubMed=9037075; DOI=10.1073/pnas.94.4.1459;
RA   Garcia-Anoveros J., Derfler B.H., Neville-Golden J., Hyman B.T.,
RA   Corey D.P.;
RT   "BNaC1 and BNaC2 constitute a new family of human neuronal sodium
RT   channels related to degenerins and epithelial sodium channels.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:1459-1464(1997).
CC   -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel
CC       family.
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DR   EMBL; U78179; AAB48982.1; -; mRNA.
DR   IPI; IPI00346778; -.
DR   UniGene; Mm.440107; -.
DR   STRING; P97811; -.
DR   Ensembl; ENSMUST00000023758; ENSMUSP00000023758; ENSMUSG00000023017.
DR   Ensembl; ENSMUST00000109052; ENSMUSP00000104680; ENSMUSG00000023017.
DR   MGI; MGI:1194915; Accn2.
DR   eggNOG; roNOG04899; -.
DR   HOGENOM; HBG447044; -.
DR   HOVERGEN; HBG004150; -.
DR   InParanoid; P97811; -.
DR   ArrayExpress; P97811; -.
DR   Bgee; P97811; -.
DR   Genevestigator; P97811; -.
DR   GO; GO:0005887; C:integral to plasma membrane; IDA:MGI.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
DR   GO; GO:0022839; F:ion gated channel activity; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0005272; F:sodium channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0008306; P:associative learning; IMP:MGI.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IMP:MGI.
DR   GO; GO:0007613; P:memory; IMP:MGI.
DR   GO; GO:0046929; P:negative regulation of neurotransmitter secretion; IMP:MGI.
DR   GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR   GO; GO:0001101; P:response to acid; IDA:MGI.
DR   InterPro; IPR001873; Na+channel_ASC.
DR   PANTHER; PTHR11690; Na+channel_ASC; 1.
DR   Pfam; PF00858; ASC; 1.
DR   PRINTS; PR01078; AMINACHANNEL.
PE   2: Evidence at transcript level;
KW   Ion transport; Ionic channel; Membrane; Sodium; Sodium channel;
KW   Sodium transport; Transmembrane; Transmembrane helix; Transport.
FT   NON_TER       1      1
FT   NON_TER     198    198
SQ   SEQUENCE   198 AA;  22254 MW;  B0AF8D16395D15DE CRC64;
     MPGDAPYCTP EQYKECADPA LDFLVEKDQE YCVCEMPCNL TRYGKELSMV KIPSKASAKY
     LAKKFNKSEQ YIGENILVLD IFFEVLNYET IEQKKAYEIA GLLGDIGGQM GLFIGASILT
     VLELFDYAYE VIKHRLCRRG KCQKEAKRNS ADKGVALSLD DVKRHNPCES LRGHPAGMTY
     AANILPHHPA RGTFEDFA
//
ID   PLD2_MOUSE              Reviewed;         933 AA.
AC   P97813;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 2.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Phospholipase D2;
DE            Short=PLD 2;
DE            Short=mPLD2;
DE            EC=3.1.4.4;
DE   AltName: Full=Choline phosphatase 2;
DE   AltName: Full=PLD1C;
DE   AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D2;
GN   Name=Pld2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Embryo, and Neonatal brain;
RX   MEDLINE=97199446; PubMed=9395408; DOI=10.1016/S0960-9822(97)70090-3;
RA   Colley W.C., Sung T.-C., Roll R., Jenco J.M., Hammond S.M.,
RA   Altshuller Y.M., Bar-Sagi D., Morris A.J., Frohman M.A.;
RT   "Phospholipase D2, a distinct phospholipase D isoform with novel
RT   regulatory properties that provokes cytoskeletal reorganization.";
RL   Curr. Biol. 7:191-201(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129;
RX   MEDLINE=98228223; PubMed=9560313;
RA   Redina O.E., Frohman M.A.;
RT   "Organization and alternative splicing of the murine phospholipase D2
RT   gene.";
RL   Biochem. J. 331:845-851(1998).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=97439716; PubMed=9307024;
RA   Colley W.C., Altshuller Y.M., Sue-Ling C.K., Copeland N.G.,
RA   Gilbert D.J., Jenkins N.A., Branch K.D., Tsirka S.E., Bollag R.J.,
RA   Bollag W.B., Frohman M.A.;
RT   "Cloning and expression analysis of murine phospholipase D1.";
RL   Biochem. J. 326:745-753(1997).
RN   [4]
RP   PHOSPHORYLATION AT TYR-11, AND MUTAGENESIS OF TYR-11.
RX   MEDLINE=99057943; PubMed=9837959; DOI=10.1074/jbc.273.50.33722;
RA   Slaaby R., Jensen T., Hansen H.S., Frohman M.A., Seedorf K.;
RT   "PLD2 complexes with the EGF receptor and undergoes tyrosine
RT   phosphorylation at a single site upon agonist stimulation.";
RL   J. Biol. Chem. 273:33722-33727(1998).
CC   -!- FUNCTION: May have a role in signal-induced cytoskeletal
CC       regulation and/or endocytosis.
CC   -!- CATALYTIC ACTIVITY: A phosphatidylcholine + H(2)O = choline + a
CC       phosphatidate.
CC   -!- ENZYME REGULATION: Stimulated by phosphatidylinositol 4,5-
CC       bisphosphate. Is not responsive to either ADP-ribosylation factor-
CC       1 (ARF-1) or GTP-binding proteins such as RHOA.
CC   -!- SUBUNIT: Interacts with PIP5K1A (By similarity). Interacts with
CC       EGFR.
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=At least 3 isoforms are produced;
CC       Name=1;
CC         IsoId=P97813-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Highest levels in brain and lung.
CC   -!- DEVELOPMENTAL STAGE: Expressed at high levels in the hippocampus
CC       at the earliest time at which it is defined as a structure and
CC       also in ventricular neural cells as well as differentiating
CC       neurons outside of the ventricular region. Expressed during
CC       development in lower levels in mesenchymal cells derived from the
CC       neural crest that are destined to form bones of the skull.
CC   -!- PTM: Phosphorylated on Tyr-11; most likely by EGFR.
CC   -!- SIMILARITY: Belongs to the phospholipase D family.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 2 PLD phosphodiesterase domains.
CC   -!- SIMILARITY: Contains 1 PX (phox homology) domain.
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DR   EMBL; U87557; AAC53173.1; -; mRNA.
DR   EMBL; AF052294; AAC24519.1; -; Genomic_DNA.
DR   EMBL; AF052291; AAC24519.1; JOINED; Genomic_DNA.
DR   EMBL; AF052293; AAC24519.1; JOINED; Genomic_DNA.
DR   EMBL; AF052292; AAC24519.1; JOINED; Genomic_DNA.
DR   IPI; IPI00469217; -.
DR   RefSeq; NP_032902.1; NM_008876.2.
DR   UniGene; Mm.260177; -.
DR   ProteinModelPortal; P97813; -.
DR   SMR; P97813; 65-193.
DR   STRING; P97813; -.
DR   PhosphoSite; P97813; -.
DR   PRIDE; P97813; -.
DR   Ensembl; ENSMUST00000018429; ENSMUSP00000018429; ENSMUSG00000020828.
DR   GeneID; 18806; -.
DR   KEGG; mmu:18806; -.
DR   UCSC; uc007jvg.1; mouse.
DR   CTD; 18806; -.
DR   MGI; MGI:892877; Pld2.
DR   eggNOG; roNOG06155; -.
DR   HOVERGEN; HBG006650; -.
DR   OrthoDB; EOG49ZXNK; -.
DR   PhylomeDB; P97813; -.
DR   BRENDA; 3.1.4.4; 244.
DR   NextBio; 295114; -.
DR   ArrayExpress; P97813; -.
DR   Bgee; P97813; -.
DR   CleanEx; MM_PLD2; -.
DR   Genevestigator; P97813; -.
DR   GermOnline; ENSMUSG00000020828; Mus musculus.
DR   GO; GO:0031526; C:brush border membrane; IDA:MGI.
DR   GO; GO:0070290; F:NAPE-specific phospholipase D activity; IEA:EC.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0004630; F:phospholipase D activity; IEA:EC.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   GO; GO:0002031; P:G-protein coupled receptor internalization; IDA:MGI.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR015679; Phospholipase_D.
DR   InterPro; IPR001683; Phox.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   InterPro; IPR016555; PLipase_D_euk.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:3.30.1520.10; PX; 1.
DR   PANTHER; PTHR18896; Phospholipase_D; 1.
DR   Pfam; PF00614; PLDc; 2.
DR   Pfam; PF00787; PX; 1.
DR   PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00155; PLDc; 2.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; PX; 1.
DR   PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
DR   PROSITE; PS50035; PLD; 2.
DR   PROSITE; PS50195; PX; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; Lipid degradation; Membrane;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1    933       Phospholipase D2.
FT                                /FTId=PRO_0000218806.
FT   DOMAIN       65    195       PX.
FT   DOMAIN      203    311       PH.
FT   DOMAIN      437    464       PLD phosphodiesterase 1.
FT   DOMAIN      751    778       PLD phosphodiesterase 2.
FT   REGION      441    788       Catalytic.
FT   MOD_RES      11     11       Phosphotyrosine.
FT   MUTAGEN      11     11       Y->F: 2-fold increase in basal
FT                                phospholipase activity.
SQ   SEQUENCE   933 AA;  106168 MW;  BADE1E0DF2EAC9ED CRC64;
     MTVTQKNLFP YGDYLNSSQL HMEPDEVDTL REGEDPADRM HPYLAIYDLQ PLKAHPLVFA
     PGVPVIAQVV GTERYTSGSK VGTCTLYSVR LTHGDFTWTT KKKFRHFQEL HRDLQRHKVL
     MSLLPLARFA VTHSPAREAA AEDIPSLPRG GSEGSARHTA SKQKYLENYL NRLLTMSFYR
     NYHAMTEFLE VSQLSFIPDL GSKGLEGVIR KRSGGHRVPG FTFCGRDQVC YRWSKRWLVV
     KDSFLLYMRP ETGAISFVQL FDPGFEVQVG KRSTETRYGV RIDTSHRSLI LKCSSYRQAR
     WWGQEITELA QGSGRDFLQL HQHDSYAPPR PGTLARWFVN GAGYFAAVAD AILRAQEEIF
     ITDWWLSPEI YLKRPAHSDD WRLDIMLKRK AEEGVRVSIL LFKEVELALG INSGYSKRTL
     MLLHPNIKVM RHPDLVTLWA HHEKLLVVDQ VVAFLGGLDL AFGRWDDVQY RLTDLGDPSE
     PVHLQTPTLG SDPAATPDLS HNQFFWLGKD YSNLITKDWV QLDRPFEDFI DRETTPRMPW
     RDVGVVVHGV AARDLARHFI QRWNFTKTTK ARYKTPLYPY LLPKSTSTAN NLPFMIPGGQ
     CATVQVLRSV DRWSAGTLEN SILNAYLHTI RESQHFLYIE NQFFISCSDG RTVLNKVGDE
     IVDRILKAHE QGQCFRVYLL LPLLPGFEGD ISTGGGNSIQ AILHFTYRTL CRGEHSILHR
     LKAAMGTAWR DYMSICGLRT HGELGGHPIS ELIYIHSKML IADDRTVIIG SANINDRSLL
     GKRDSELAIL IKDTEMEPSL MDGVEYQAGR FALSLRKHCF SVILGANTWP DLDLRDPVCD
     DFFQLWQETA ENNATIYEQI FRCLPSNATR SLRALREYVA VESLATVSPS LAQSELAHIQ
     GHLVHFPLKF LEDESLLPPL GSKEGMIPLE VWT
//
ID   PPIP1_MOUSE             Reviewed;         415 AA.
AC   P97814; Q4V9R4;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Proline-serine-threonine phosphatase-interacting protein 1;
DE            Short=PEST phosphatase-interacting protein 1;
GN   Name=Pstpip1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH PTPN18,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   PHOSPHORYLATION.
RX   MEDLINE=97412181; PubMed=9265651; DOI=10.1083/jcb.138.4.845;
RA   Spencer S., Dowbenko D., Cheng J., Li W., Brush J., Utzig S.,
RA   Simanis V., Lasky L.A.;
RT   "PSTPIP: a tyrosine phosphorylated cleavage furrow-associated protein
RT   that is a substrate for a PEST tyrosine phosphatase.";
RL   J. Cell Biol. 138:845-860(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6NCr; TISSUE=Hematopoietic stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, INTERACTION WITH WAS, SUBCELLULAR LOCATION, PHOSPHORYLATION,
RP   AND MUTAGENESIS OF TYR-344 AND TYR-367.
RX   MEDLINE=98157976; PubMed=9488710; DOI=10.1074/jbc.273.10.5765;
RA   Wu Y., Spencer S.D., Lasky L.A.;
RT   "Tyrosine phosphorylation regulates the SH3-mediated binding of the
RT   Wiskott-Aldrich syndrome protein to PSTPIP, a cytoskeletal-associated
RT   protein.";
RL   J. Biol. Chem. 273:5765-5770(1998).
RN   [4]
RP   FUNCTION, INTERACTION WITH ABL1, PHOSPHORYLATION, AND MUTAGENESIS OF
RP   TYR-344 AND TYR-367.
RX   PubMed=11163214; DOI=10.1016/S1097-2765(00)00138-6;
RA   Cong F., Spencer S., Cote J.F., Wu Y., Tremblay M.L., Lasky L.A.,
RA   Goff S.P.;
RT   "Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine
RT   phosphatase to the c-Abl kinase to mediate Abl dephosphorylation.";
RL   Mol. Cell 6:1413-1423(2000).
RN   [5]
RP   FUNCTION, INTERACTION WITH PTPN12, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, PHOSPHORYLATION, AND MUTAGENESIS OF TYR-344 AND TYR-367.
RX   PubMed=11711533; DOI=10.1074/jbc.M106428200;
RA   Cote J.-F., Chung P.L., Theberge J.-F., Halle M., Spencer S.,
RA   Lasky L.A., Tremblay M.L.;
RT   "PSTPIP is a substrate of PTP-PEST and serves as a scaffold guiding
RT   PTP-PEST toward a specific dephosphorylation of WASP.";
RL   J. Biol. Chem. 277:2973-2986(2002).
RN   [6]
RP   FUNCTION, INTERACTION WITH CD2; CD2AP AND WAS, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=12530983; DOI=10.1016/S1074-7613(02)00516-2;
RA   Badour K., Zhang J., Shi F., McGavin M.K.H., Rampersad V., Hardy L.A.,
RA   Field D., Siminovitch K.A.;
RT   "The Wiskott-Aldrich syndrome protein acts downstream of CD2 and the
RT   CD2AP and PSTPIP1 adaptors to promote formation of the immunological
RT   synapse.";
RL   Immunity 18:141-154(2003).
CC   -!- FUNCTION: Involved in regulation of the actin cytoskeleton. May
CC       regulate the WAS actin-bundling activity. Bridges the interaction
CC       between ABL1 and PTPN18 leading to the ABL1 dephosphorylation. May
CC       play a role as a scaffold protein between PTPN12 and WAS, and
CC       allows PTPN12 to dephosphorylate WAS. Has the potential to
CC       physically couple CD2 and CD2AP to WAS. Acts downstream of CD2 and
CC       CD2AP to recruit WAS to the T-cell:APC contact site so as to
CC       promote the actin polymerization required for synapse induction
CC       during T-cell activation. Down-regulates CD2-stimulated adhesion
CC       through coupling PTPN12 to CD2.
CC   -!- SUBUNIT: Interacts with MEFV/pyrin (By similarity). Interacts with
CC       PTPN18/PTP HSCF, ABL1, PTPN12, CD2, CD2AP and WAS. Interacts with
CC       FASLG (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell
CC       projection, lamellipodium. Cytoplasm, perinuclear region. Cleavage
CC       furrow. Note=Colocalized with the cortical actin cytoskeleton
CC       during interphase, lamellipodia and actin-rich cytokinetic
CC       cleavage furrow. Colocalized with WAS to filamentous structures
CC       within the cytoplasm. Colocalized with PTPN12 in the cytoplasm and
CC       the perinuclear region. Colocalized with CD2AP and WAS in the
CC       actin cytoskeleton. Colocalized with CD2, CD2AP and WAS at the
CC       site of T-cell:APC contact.
CC   -!- TISSUE SPECIFICITY: Highly expressed in adult lung and spleen, and
CC       weakly expressed in testis, muscle, kidney, brain and heart.
CC       Highly expressed in spleen and thymus, moderately in lung, brain
CC       and muscle, and weakly expressed in heart and liver (at protein
CC       level).
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in the day 7 embryo (E7).
CC   -!- DOMAIN: The SH3 and coiled-coil domains are necessary for the
CC       interaction with MEFV (By similarity). The coiled domain mediates
CC       interaction with PTPN18, PTPN12 and CD2AP. The SH3 domain mediates
CC       interaction with WAS and ABL1.
CC   -!- PTM: Dephosphorylated on Tyr-344 by PTPN18, this event negatively
CC       regulates the association of PSTPIP1 with SH2 domain-containing
CC       proteins as tyrosine kinase. Phosphorylation of Tyr-344 is
CC       probably required for subsequent phosphorylation at other tyrosine
CC       residues. Phosphorylation is induced by activation of the EGFR and
CC       PDGFR in a ABL1 dependent manner. The phosphorylation regulates
CC       the interaction with WAS and with MEFV.
CC   -!- SIMILARITY: Contains 1 FCH domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; U87814; AAB48483.1; -; mRNA.
DR   EMBL; BC096761; AAH96761.1; -; mRNA.
DR   IPI; IPI00314743; -.
DR   RefSeq; NP_035323.2; NM_011193.2.
DR   UniGene; Mm.2534; -.
DR   ProteinModelPortal; P97814; -.
DR   SMR; P97814; 3-286, 357-415.
DR   MINT; MINT-444743; -.
DR   STRING; P97814; -.
DR   PhosphoSite; P97814; -.
DR   PRIDE; P97814; -.
DR   Ensembl; ENSMUST00000059206; ENSMUSP00000055823; ENSMUSG00000032322.
DR   GeneID; 19200; -.
DR   KEGG; mmu:19200; -.
DR   UCSC; uc009psu.1; mouse.
DR   CTD; 19200; -.
DR   MGI; MGI:1321396; Pstpip1.
DR   eggNOG; roNOG12876; -.
DR   GeneTree; ENSGT00530000063207; -.
DR   HOGENOM; HBG715569; -.
DR   HOVERGEN; HBG052960; -.
DR   InParanoid; P97814; -.
DR   OrthoDB; EOG4PZJ6T; -.
DR   NextBio; 295916; -.
DR   ArrayExpress; P97814; -.
DR   Bgee; P97814; -.
DR   Genevestigator; P97814; -.
DR   GermOnline; ENSMUSG00000032322; Mus musculus.
DR   GO; GO:0005826; C:actomyosin contractile ring; IDA:MGI.
DR   GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR   GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0001725; C:stress fiber; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IDA:MGI.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0019903; F:protein phosphatase binding; IDA:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0000910; P:cytokinesis; IC:MGI.
DR   InterPro; IPR001060; FCH.
DR   InterPro; IPR011254; Prismane-like.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR013315; Spectrin_alpha_SH3.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR01887; SPECTRNALPHA.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF56821; Prismane_like; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50133; FCH; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Phosphoprotein; SH3 domain.
FT   CHAIN         1    415       Proline-serine-threonine phosphatase-
FT                                interacting protein 1.
FT                                /FTId=PRO_0000058540.
FT   DOMAIN        5     82       FCH.
FT   DOMAIN      358    415       SH3.
FT   COILED       94    133       Potential.
FT   COILED      162    215       Potential.
FT   MOD_RES     344    344       Phosphotyrosine; by ABL1.
FT   MUTAGEN     344    344       Y->F: Complete loss of protein
FT                                phosphorylation.
FT   MUTAGEN     367    367       Y->F: No effect on phosphorylation.
FT   CONFLICT    301    301       I -> V (in Ref. 2; AAH96761).
SQ   SEQUENCE   415 AA;  47590 MW;  16C0329284D2739C CRC64;
     MMAQLQFRDA FWCRDFTAHT GYEVLLQRLL DGRKMCKDVE ELLRQRAQAE ERYGKELVQI
     ARKAGGQTEM NSLRTSFDSL KQQTENVGSA HIQLALALRE ELRSLEEFRE RQKEQRKKYE
     AIMDRVQKSK LSLYKKTMES KKAYDQKCRD ADDAEQAFER VSANGHQKQV EKSQNKAKQC
     KESATEAERV YRQNIEQLER ARTEWEQEHR TTCEAFQLQE FDRLTILRNA LWVHCNQLSM
     QCVKDDELYE EVRLTLEGCD VEGDINGFIQ SKSTGREPPA PVPYQNYYDR EVTPLIGSPS
     IQPSCGVIKR FSGLLHGSPK TTPSAPAAST ETLTPTPERN ELVYASIEVQ ATQGNLNSSA
     QDYRALYDYT AQNSDELDIS AGDILAVILE GEDGWWTVER NGQRGFVPGS YLEKL
//
ID   HN1_MOUSE               Reviewed;         154 AA.
AC   P97825;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Hematological and neurological expressed 1 protein;
GN   Name=Hn1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Erythroid cell;
RX   MEDLINE=97419275; PubMed=9271675; DOI=10.1007/s003359900540;
RA   Tang W., Lai Y.H., Han X.D., Wong P.M.C., Peters L.L., Chui D.H.K.;
RT   "Murine Hn1 on chromosome 11 is expressed in hemopoietic and brain
RT   tissues.";
RL   Mamm. Genome 8:695-696(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, and C57BL/6J;
RC   TISSUE=Bone marrow, Embryo, Fetal head, Fetal heart, Placenta, and
RC   Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49; SER-61; SER-85;
RP   SER-87; SER-88 AND SER-92, AND MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in yolk sac, fetal brain, brain,
CC       spleen and bone marrow.
CC   -!- SIMILARITY: Belongs to the HN1 family.
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DR   EMBL; U90123; AAB70094.1; -; mRNA.
DR   EMBL; AK152560; BAE31313.1; -; mRNA.
DR   EMBL; AK010057; BAB26672.1; -; mRNA.
DR   EMBL; AK013122; BAB28661.1; -; mRNA.
DR   EMBL; AK014212; BAB29208.1; -; mRNA.
DR   EMBL; AK159784; BAE35368.1; -; mRNA.
DR   EMBL; AK167466; BAE39550.1; -; mRNA.
DR   EMBL; AK167961; BAE39958.1; -; mRNA.
DR   EMBL; AK168632; BAE40492.1; -; mRNA.
DR   EMBL; BC003758; AAH03758.1; -; mRNA.
DR   IPI; IPI00314755; -.
DR   RefSeq; NP_032284.1; NM_008258.1.
DR   UniGene; Mm.1775; -.
DR   ProteinModelPortal; P97825; -.
DR   PhosphoSite; P97825; -.
DR   PRIDE; P97825; -.
DR   Ensembl; ENSMUST00000021083; ENSMUSP00000021083; ENSMUSG00000020737.
DR   GeneID; 15374; -.
DR   KEGG; mmu:15374; -.
DR   NMPDR; fig|10090.3.peg.25618; -.
DR   UCSC; uc007mhv.1; mouse.
DR   CTD; 15374; -.
DR   MGI; MGI:1096361; Hn1.
DR   GeneTree; ENSGT00390000000756; -.
DR   HOGENOM; HBG281461; -.
DR   HOVERGEN; HBG055006; -.
DR   InParanoid; P97825; -.
DR   OMA; GQSEEKP; -.
DR   OrthoDB; EOG444KMF; -.
DR   PhylomeDB; P97825; -.
DR   NextBio; 288022; -.
DR   ArrayExpress; P97825; -.
DR   Bgee; P97825; -.
DR   Genevestigator; P97825; -.
DR   GermOnline; ENSMUSG00000020737; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Acetylation; Nucleus; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    154       Hematological and neurological expressed
FT                                1 protein.
FT                                /FTId=PRO_0000054919.
FT   MOD_RES       2      2       N-acetylthreonine (By similarity).
FT   MOD_RES       8      8       N6-acetyllysine (By similarity).
FT   MOD_RES      49     49       Phosphoserine.
FT   MOD_RES      54     54       Phosphothreonine (By similarity).
FT   MOD_RES      61     61       Phosphoserine.
FT   MOD_RES      70     70       Phosphoserine (By similarity).
FT   MOD_RES      85     85       Phosphoserine.
FT   MOD_RES      87     87       Phosphoserine.
FT   MOD_RES      88     88       Phosphoserine.
FT   MOD_RES      92     92       Phosphoserine.
FT   MOD_RES     131    131       Phosphoserine (By similarity).
FT   MOD_RES     148    148       N6-acetyllysine (By similarity).
SQ   SEQUENCE   154 AA;  16081 MW;  F358F8F697ED221F CRC64;
     MTTTTTFKGV DPNSRNSSRV LRPPGGGSNF SLGFDEPAEQ PVRKNKMASN IFGTPEENPP
     SWAKSAGSKS SGGREDSESP GTQRSNSSEA SSGDFLDLKG EGDMHENVDT DFQANLAQME
     EKPVPAAPVP SPVAPAPVPS RRNPPGGKSS LVLG
//
ID   G3BP1_MOUSE             Reviewed;         465 AA.
AC   P97855;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Ras GTPase-activating protein-binding protein 1;
DE            Short=G3BP-1;
DE            EC=3.6.4.12;
DE            EC=3.6.4.13;
DE   AltName: Full=ATP-dependent DNA helicase VIII;
DE   AltName: Full=GAP SH3 domain-binding protein 1;
DE   AltName: Full=HDH-VIII;
GN   Name=G3bp1; Synonyms=G3bp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Saitoh H., Abe T.K., Masuko M., Tanaka H., Watanabe Y.G., Odani S.,
RA   Kuwano R.;
RT   "cDNA cloning of GAP SH3 binding protein from mouse brain.";
RL   Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 124-132; 334-351 AND 375-391, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=96220439; PubMed=8649363;
RA   Parker F., Maurier F., Delumeau I., Duchesne M., Faucher D.,
RA   Debussche L., Dugue A., Schweighoffer F., Tocque B.;
RT   "A Ras-GTPase-activating protein SH3-domain-binding protein.";
RL   Mol. Cell. Biol. 16:2561-2569(1996).
RN   [5]
RP   ENDORIBONUCLEASE ACTIVITY, AND PHOSPHORYLATION AT SER-149 AND SER-231.
RX   PubMed=11604510; DOI=10.1128/MCB.21.22.7747-7760.2001;
RA   Tourriere H., Gallouzi I.-E., Chebli K., Capony J.-P., Mouaikel J.,
RA   van der Geer P., Tazi J.;
RT   "RasGAP-associated endoribonuclease G3Bp: selective RNA degradation
RT   and phosphorylation-dependent localization.";
RL   Mol. Cell. Biol. 21:7747-7760(2001).
RN   [6]
RP   IDENTIFICATION IN A MRNP COMPLEX WITH IGF2BP1 AND ELAVL4.
RX   PubMed=15086518; DOI=10.1111/j.1471-4159.2004.02371.x;
RA   Atlas R., Behar L., Elliott E., Ginzburg I.;
RT   "The insulin-like growth factor mRNA binding-protein IMP-1 and the
RT   Ras-regulatory protein G3BP associate with tau mRNA and HuD protein in
RT   differentiated P19 neuronal cells.";
RL   J. Neurochem. 89:613-626(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-231 AND
RP   THR-266, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: May be a regulated effector of stress granule assembly.
CC       Phosphorylation-dependent sequence-specific endoribonuclease in
CC       vitro. Cleaves exclusively between cytosine and adenine and
CC       cleaves MYC mRNA preferentially at the 3'-UTR. ATP- and magnesium-
CC       dependent helicase. Unwinds preferentially partial DNA and RNA
CC       duplexes having a 17 bp annealed portion and either a hanging 3'
CC       tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA,
CC       RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts
CC       unidirectionally by moving in the 5' to 3' direction along the
CC       bound single-stranded DNA.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- COFACTOR: Magnesium. Required for helicase activity (By
CC       similarity).
CC   -!- SUBUNIT: Binds to the SH3 domain of Ras GTPase-activating protein
CC       (RASA1) in proliferating cells. No interaction in quiescent cells.
CC       Interacts with USP10, and may regulate it. Forms homodimers and
CC       oligomers (By similarity). Component of a TAU mRNP complex, at
CC       least composed of IGF2BP1, ELAVL4 and G3BP.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytosol (By similarity). Cell membrane (By similarity). Nucleus
CC       (By similarity). Note=Cytoplasmic in proliferating cells, can be
CC       recruited to the plasma membrane in exponentially growing cells
CC       (By similarity). Cytosolic and partially nuclear in resting cells.
CC       Recruited to stress granules (SGs) upon either arsenite or high
CC       temperature treatment. Recruitment to SGs is influenced by HRAS
CC       (By similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- DOMAIN: The NTF2 domain mediates multimerization (By similarity).
CC   -!- PTM: Phosphorylated exclusively on serine residues.
CC       Hyperphosphorylated in quiescent fibroblasts. Hypophosphorylation
CC       leads to a decrease in endoribonuclease activity. RASA1-dependent
CC       phosphorylation of Ser-149 induces a conformational change that
CC       prevents self-association. Dephosphorylation after HRAS activation
CC       is required for stress granule assembly. Ser-149 phosphorylation
CC       induces partial nuclear localization (By similarity).
CC   -!- SIMILARITY: Contains 1 NTF2 domain.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB001927; BAA19469.1; -; mRNA.
DR   EMBL; BC021156; AAH21156.1; -; mRNA.
DR   IPI; IPI00130095; -.
DR   RefSeq; NP_038744.1; NM_013716.2.
DR   UniGene; Mm.380129; -.
DR   UniGene; Mm.39631; -.
DR   UniGene; Mm.405739; -.
DR   ProteinModelPortal; P97855; -.
DR   SMR; P97855; 5-133, 337-415.
DR   STRING; P97855; -.
DR   PhosphoSite; P97855; -.
DR   PRIDE; P97855; -.
DR   Ensembl; ENSMUST00000018727; ENSMUSP00000018727; ENSMUSG00000018583.
DR   GeneID; 27041; -.
DR   KEGG; mmu:27041; -.
DR   UCSC; uc007izl.1; mouse.
DR   CTD; 27041; -.
DR   MGI; MGI:1351465; G3bp1.
DR   eggNOG; roNOG12019; -.
DR   HOVERGEN; HBG007211; -.
DR   InParanoid; P97855; -.
DR   OMA; FQSYGNV; -.
DR   OrthoDB; EOG4XWFZ0; -.
DR   PhylomeDB; P97855; -.
DR   NextBio; 304965; -.
DR   ArrayExpress; P97855; -.
DR   Bgee; P97855; -.
DR   Genevestigator; P97855; -.
DR   GermOnline; ENSMUSG00000018583; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002075; NTF2.
DR   InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF02136; NTF2; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50177; NTF2_DOMAIN; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cell membrane; Cytoplasm;
KW   Direct protein sequencing; DNA-binding; Endonuclease; Helicase;
KW   Hydrolase; Membrane; Methylation; Nuclease; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; RNA-binding; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    465       Ras GTPase-activating protein-binding
FT                                protein 1.
FT                                /FTId=PRO_0000194799.
FT   DOMAIN       11    133       NTF2.
FT   DOMAIN      338    413       RRM.
FT   COMPBIAS    144    225       Glu-rich.
FT   COMPBIAS    428    459       Gly-rich.
FT   MOD_RES     143    143       Phosphothreonine (By similarity).
FT   MOD_RES     149    149       Phosphoserine.
FT   MOD_RES     229    229       Phosphoserine (By similarity).
FT   MOD_RES     231    231       Phosphoserine.
FT   MOD_RES     266    266       Phosphothreonine.
FT   MOD_RES     371    371       Phosphoserine (By similarity).
FT   MOD_RES     374    374       N6-acetyllysine (By similarity).
FT   MOD_RES     433    433       Dimethylated arginine; alternate (By
FT                                similarity).
FT   MOD_RES     433    433       Omega-N-methylarginine; alternate (By
FT                                similarity).
FT   MOD_RES     445    445       Omega-N-methylated arginine (By
FT                                similarity).
FT   MOD_RES     458    458       Dimethylated arginine; alternate (By
FT                                similarity).
FT   MOD_RES     458    458       Omega-N-methylated arginine; alternate
FT                                (By similarity).
FT   MOD_RES     464    464       Omega-N-methylated arginine (By
FT                                similarity).
SQ   SEQUENCE   465 AA;  51829 MW;  EB213303D21B1D57 CRC64;
     MVMEKPSPLL VGREFVRQYY TLLNQAPDML HRFYGKNSSY AHGGLDSNGK PADAVYGQKE
     IHRKVMSQNF TNCHTKIRHV DAHATLNDGV VVQVMGLLSN NNQALRRFMQ TFVLAPEGSV
     ANKFYVHNDI FRYQDEVFGG FVTEPQEESE EEVEEPEERQ QTPEVVPDDS GTFYDQTVSN
     DLEEHLEEPV VEPEPEPEPE PEPEPVSDIQ EDKPEAALEE AAPDDVQKST SPAPADVAPA
     QEDLRTFSWA SVTSKNLPPS GAVPVTGTPP HVVKVPASQP RPESKPDSQI PPQRPQRDQR
     VREQRINIPP QRGPRPIREA GEPGDVEPRR MVRHPDSHQL FIGNLPHEVD KSELKDFFQN
     FGNVVELRIN SGGKLPNFGF VVFDDSEPVQ KVLSNRPIMF RGAVRLNVEE KKTRAAREGD
     RRDNRLRGPG GPRGGPSGGM RGPPRGGMVQ KPGFGVGRGI TTPRQ
//
ID   NFIB_MOUSE              Reviewed;         570 AA.
AC   P97863; P70252; P70253; P70254; Q9R1G4;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   11-JAN-2011, entry version 102.
DE   RecName: Full=Nuclear factor 1 B-type;
DE            Short=NF1-B;
DE            Short=Nuclear factor 1/B;
DE   AltName: Full=CCAAT-box-binding transcription factor;
DE            Short=CTF;
DE   AltName: Full=Nuclear factor I/B;
DE            Short=NF-I/B;
DE            Short=NFI-B;
DE   AltName: Full=TGGCA-binding protein;
GN   Name=Nfib;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   STRAIN=BALB/c; TISSUE=Liver, and Skeletal muscle;
RX   MEDLINE=97209336; PubMed=9056636;
RX   DOI=10.1002/(SICI)1097-0177(199703)208:3<313::AID-AJA3>3.3.CO;2-2;
RA   Chaudhry A.Z., Lyons G.E., Gronostajski R.M.;
RT   "Expression patterns of the four nuclear factor I genes during mouse
RT   embryogenesis indicate a potential role in development.";
RL   Dev. Dyn. 208:313-325(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ISOFORMS 1; 2 AND 3).
RC   STRAIN=NIH Swiss;
RX   MEDLINE=22456605; PubMed=12568726; DOI=10.1016/S0378-1119(02)01204-0;
RA   Gruender A., Qian F., Ebel T.T., Mincheva A., Lichter P., Kruse U.,
RA   Sippel A.E.;
RT   "Genomic organization, splice products and mouse chromosomal
RT   localization of genes for transcription factor Nuclear Factor One.";
RL   Gene 304:171-181(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-187.
RC   STRAIN=129;
RX   MEDLINE=99189145; PubMed=10087299; DOI=10.1007/s003359901008;
RA   Fletcher C.F., Jenkins N.A., Copeland N.G., Chaudhry A.Z.,
RA   Gronostajski R.M.;
RT   "Exon structure of the nuclear factor I DNA-binding domain from C.
RT   elegans to mammals.";
RL   Mamm. Genome 10:390-396(1999).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264; SER-292 AND
RP   SER-295, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Recognizes and binds the palindromic sequence 5'-
CC       TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in
CC       the origin of replication of adenovirus type 2. These proteins are
CC       individually capable of activating transcription and replication.
CC   -!- SUBUNIT: Binds DNA as a homodimer.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P97863-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P97863-2; Sequence=VSP_003547;
CC       Name=3;
CC         IsoId=P97863-3; Sequence=VSP_003548, VSP_003549;
CC   -!- TISSUE SPECIFICITY: Highest expression in lung, skeletal muscle
CC       and heart. Lower levels in liver, kidney and brain. Very low
CC       levels in testis and spleen.
CC   -!- SIMILARITY: Belongs to the CTF/NF-I family.
CC   -!- SIMILARITY: Contains 1 CTF/NF-I DNA-binding domain.
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DR   EMBL; U57634; AAB49929.1; -; mRNA.
DR   EMBL; Y07685; CAA68949.1; -; mRNA.
DR   EMBL; Y07686; CAA68950.1; -; mRNA.
DR   EMBL; Y07687; CAA68951.1; -; mRNA.
DR   EMBL; BC014290; AAH14290.1; -; mRNA.
DR   EMBL; AF111264; AAD39099.1; -; Genomic_DNA.
DR   IPI; IPI00130129; -.
DR   IPI; IPI00230656; -.
DR   IPI; IPI00230657; -.
DR   RefSeq; NP_001106680.1; NM_001113209.1.
DR   RefSeq; NP_032713.3; NM_008687.5.
DR   UniGene; Mm.317947; -.
DR   ProteinModelPortal; P97863; -.
DR   STRING; P97863; -.
DR   PhosphoSite; P97863; -.
DR   PRIDE; P97863; -.
DR   Ensembl; ENSMUST00000050872; ENSMUSP00000052863; ENSMUSG00000008575.
DR   Ensembl; ENSMUST00000075543; ENSMUSP00000074981; ENSMUSG00000008575.
DR   Ensembl; ENSMUST00000107250; ENSMUSP00000102871; ENSMUSG00000008575.
DR   GeneID; 18028; -.
DR   KEGG; mmu:18028; -.
DR   UCSC; uc008tkc.1; mouse.
DR   UCSC; uc008tkd.1; mouse.
DR   CTD; 18028; -.
DR   MGI; MGI:103188; Nfib.
DR   eggNOG; roNOG07919; -.
DR   HOGENOM; HBG445384; -.
DR   HOVERGEN; HBG006561; -.
DR   InParanoid; P97863; -.
DR   OMA; EKPLFSP; -.
DR   PhylomeDB; P97863; -.
DR   NextBio; 293099; -.
DR   ArrayExpress; P97863; -.
DR   Bgee; P97863; -.
DR   CleanEx; MM_NFIB; -.
DR   Genevestigator; P97863; -.
DR   GermOnline; ENSMUSG00000008575; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016563; F:transcription activator activity; IDA:MGI.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0030902; P:hindbrain development; IMP:MGI.
DR   GO; GO:0030324; P:lung development; IMP:MGI.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0010552; P:positive regulation of gene-specific transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   InterPro; IPR000647; CTF/NFI.
DR   InterPro; IPR020604; CTF/NFI_DNA-bd-dom.
DR   InterPro; IPR019739; CTF/NFI_DNA-bd_CS.
DR   InterPro; IPR019548; CTF/NFI_DNA-bd_N.
DR   InterPro; IPR003619; MAD_homology1_Dwarfin-type.
DR   PANTHER; PTHR11492; CTF_NFI; 1.
DR   Pfam; PF00859; CTF_NFI; 1.
DR   Pfam; PF03165; MH1; 1.
DR   Pfam; PF10524; NfI_DNAbd_pre-N; 1.
DR   SMART; SM00523; DWA; 1.
DR   PROSITE; PS00349; CTF_NFI_1; 1.
DR   PROSITE; PS51080; CTF_NFI_2; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; DNA replication; DNA-binding;
KW   Nucleus; Phosphoprotein; Transcription; Transcription regulation.
FT   CHAIN         1    570       Nuclear factor 1 B-type.
FT                                /FTId=PRO_0000100197.
FT   DNA_BIND      1    195       CTF/NF-I.
FT   MOD_RES      63     63       Phosphoserine.
FT   MOD_RES     264    264       Phosphoserine.
FT   MOD_RES     265    265       Phosphoserine (By similarity).
FT   MOD_RES     292    292       Phosphoserine.
FT   MOD_RES     295    295       Phosphoserine.
FT   MOD_RES     328    328       Phosphoserine (By similarity).
FT   MOD_RES     332    332       Phosphoserine (By similarity).
FT   VAR_SEQ     416    498       Missing (in isoform 2).
FT                                /FTId=VSP_003547.
FT   VAR_SEQ     416    420       PNSSG -> SWYLG (in isoform 3).
FT                                /FTId=VSP_003548.
FT   VAR_SEQ     421    570       Missing (in isoform 3).
FT                                /FTId=VSP_003549.
FT   VARIANT     131    131       D -> G (in strain: NIH Swiss).
SQ   SEQUENCE   570 AA;  63507 MW;  D94AB4400A2811CC CRC64;
     MMYSPICLTQ DEFHPFIEAL LPHVRAIAYT WFNLQARKRK YFKKHEKRMS KDEERAVKDE
     LLSEKPEIKQ KWASRLLAKL RKDIRQEYRE DFVLTVTGKK HPCCVLSNPD QKGKIRRIDC
     LRQADKVWRL DLVMVILFKG IPLESTDGER LMKSPHCTNP ALCVQPHHIT VSVKELDLFL
     AYYVQEQDSG QSGSPSHSDP AKNPPGYLED SFVKSGVFNV SELVRVSRTP ITQGTGVNFP
     IGEIPSQPYY HDMNSGVNLQ RSLSSPPSSK RPKTISIDEN MEPSPTGDFY PSPNSPAAGS
     RTWHERDQDM SSPTTMKKPE KPLFSSTSPQ DSSPRLSTFP QHHHPGIPGV AHSVISTRTP
     PPPSPLPFPT QAILPPAPSS YFSHPTIRYP PHLNPQDTLK NYVPSYDPSS PQTSQPNSSG
     QVVGKVPGHF TPVLAPSPHP SAVRPVTLTM TDTKPITTST EGEAASPTAT TYTASGTSQA
     NRYVGLSPRD PSFLHQQQLR ICDWTMNQNG RHLYPSTSED TLGITWQSPG TWASLVPFQV
     SNRTPILPAN VQNYGLNIIG EPFLQAETSN
//
ID   RBBP6_MOUSE             Reviewed;        1790 AA.
AC   P97868; P70287; Q3TTR9; Q3TUM7; Q3UMP7; Q4U217; Q7TT06; Q8BNY8;
AC   Q8R399;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 5.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=E3 ubiquitin-protein ligase RBBP6;
DE            EC=6.3.2.-;
DE   AltName: Full=Proliferation potential-related protein;
DE   AltName: Full=Protein P2P-R;
DE   AltName: Full=Retinoblastoma-binding protein 6;
DE   AltName: Full=p53-associated cellular protein of testis;
GN   Name=Rbbp6; Synonyms=P2pr, Pact;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 546-1148 (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1356-1790 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Corpora quadrigemina, Corpus striatum, Embryo, Head, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 154-1790 (ISOFORM 2), INTERACTION WITH
RP   RB1, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=BALB/c;
RX   MEDLINE=97188447; PubMed=9037032; DOI=10.1073/pnas.94.4.1212;
RA   Witte M.M., Scott R.E.;
RT   "The proliferation potential protein-related (P2P-R) gene with domains
RT   encoding heterogeneous nuclear ribonucleoprotein association and Rb1
RT   binding shows repressed expression during terminal differentiation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:1212-1217(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 204-1790 (ISOFORM 1), INTERACTION WITH
RP   TP53 AND RB1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Testis;
RX   PubMed=9010216; DOI=10.1038/sj.onc.1200825;
RA   Simons A., Melamed-Bessudo C., Wolkowicz R., Sperling J., Sperling R.,
RA   Eisenbach L., Rotter V.;
RT   "PACT: cloning and characterization of a cellular p53 binding protein
RT   that interacts with Rb.";
RL   Oncogene 14:145-155(1997).
RN   [6]
RP   SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=12064457; DOI=10.1002/jcp.10084;
RA   Gao S., Witte M.M., Scott R.E.;
RT   "P2P-R protein localizes to the nucleolus of interphase cells and the
RT   periphery of chromosomes in mitotic cells which show maximum P2P-R
RT   immunoreactivity.";
RL   J. Cell. Physiol. 191:145-154(2002).
RN   [7]
RP   ERRATUM.
RA   Gao S., Witte M.M., Scott R.E.;
RL   J. Cell. Physiol. 192:359-360(2002).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12384997; DOI=10.1002/jcp.10163;
RA   Gao S., Scott R.E.;
RT   "P2P-R protein overexpression restricts mitotic progression at
RT   prometaphase and promotes mitotic apoptosis.";
RL   J. Cell. Physiol. 193:199-207(2002).
RN   [9]
RP   INTERACTION WITH TP53.
RX   PubMed=14566974; DOI=10.1002/jcp.10381;
RA   Gao S., Scott R.E.;
RT   "Stable overexpression of specific segments of the P2P-R protein in
RT   human MCF-7 cells promotes camptothecin-induced apoptosis.";
RL   J. Cell. Physiol. 197:445-452(2003).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1272 AND SER-1278, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [11]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=17470788; DOI=10.1073/pnas.0701916104;
RA   Li L., Deng B., Xing G., Teng Y., Tian C., Cheng X., Yin X., Yang J.,
RA   Gao X., Zhu Y., Sun Q., Zhang L., Yang X., He F.;
RT   "PACT is a negative regulator of p53 and essential for cell growth and
RT   embryonic development.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7951-7956(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-771; SER-773; SER-862
RP   AND SER-1179, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-773; SER-1179 AND
RP   SER-1329, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which promotes
CC       ubiquitination of YBX1, leading to its degradation by the
CC       proteasome (By similarity). May play a role as a scaffold protein
CC       to promote the assembly of the p53/TP53-MDM2 complex, resulting in
CC       increase of MDM2-mediated ubiquitination and degradation of
CC       p53/TP53; may function as negative regulator of p53/TP53, leading
CC       to both apoptosis and cell growth retardation.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with MDM2 and YBX1 (By similarity). Interacts
CC       also with p53/TP53 and RB1.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Chromosome.
CC       Note=Colocalizes with mitotic chromosomes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P97868-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P97868-2; Sequence=VSP_018287;
CC       Name=3;
CC         IsoId=P97868-3; Sequence=VSP_018285, VSP_018286;
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis. Expressed at lower
CC       levels in brain, heart, kidney, liver, lung, skeletal muscle,
CC       spleen, thymus and tongue.
CC   -!- DEVELOPMENTAL STAGE: Expression is reduced during terminal
CC       differentiation. Expression is induced in the G2/M phase of the
CC       cell cycle (at protein level).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Early embryonic lethality before E7.5,
CC       accompanied by accumulation of p53 and widespread apoptosis.
CC   -!- SIMILARITY: Contains 1 CCHC-type zinc finger.
CC   -!- SIMILARITY: Contains 1 DWNN domain.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC72432.1; Type=Frameshift; Positions=176;
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DR   EMBL; AK045635; BAC32441.1; -; mRNA.
DR   EMBL; AK079129; BAC37553.1; -; mRNA.
DR   EMBL; AK081261; BAC38179.1; -; mRNA.
DR   EMBL; AK144758; BAE26051.1; -; mRNA.
DR   EMBL; AK160656; BAE35944.1; -; mRNA.
DR   EMBL; AK161231; BAE36255.1; -; mRNA.
DR   EMBL; AC125221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC025874; AAH25874.1; -; mRNA.
DR   EMBL; U83913; AAC72432.1; ALT_FRAME; mRNA.
DR   EMBL; U28789; AAB49620.1; -; mRNA.
DR   IPI; IPI00153709; -.
DR   IPI; IPI00551082; -.
DR   IPI; IPI00551482; -.
DR   PIR; T42727; T42727.
DR   RefSeq; NP_035377.2; NM_011247.2.
DR   RefSeq; NP_778188.1; NM_175023.3.
DR   UniGene; Mm.4480; -.
DR   ProteinModelPortal; P97868; -.
DR   SMR; P97868; 1-81, 160-207, 245-310.
DR   STRING; P97868; -.
DR   PhosphoSite; P97868; -.
DR   PRIDE; P97868; -.
DR   Ensembl; ENSMUST00000052135; ENSMUSP00000049528; ENSMUSG00000030779.
DR   Ensembl; ENSMUST00000071590; ENSMUSP00000071519; ENSMUSG00000030779.
DR   Ensembl; ENSMUST00000106453; ENSMUSP00000102061; ENSMUSG00000030779.
DR   GeneID; 19647; -.
DR   KEGG; mmu:19647; -.
DR   UCSC; uc009jow.1; mouse.
DR   UCSC; uc009joy.1; mouse.
DR   CTD; 19647; -.
DR   MGI; MGI:894835; Rbbp6.
DR   GeneTree; ENSGT00600000084530; -.
DR   HOVERGEN; HBG093889; -.
DR   InParanoid; P97868; -.
DR   OMA; GGRPGWE; -.
DR   OrthoDB; EOG44TP8G; -.
DR   PhylomeDB; P97868; -.
DR   NextBio; 296898; -.
DR   ArrayExpress; P97868; -.
DR   Bgee; P97868; -.
DR   CleanEx; MM_RBBP6; -.
DR   Genevestigator; P97868; -.
DR   GermOnline; ENSMUSG00000030779; Mus musculus.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR014891; DWNN_domain.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013084; Znf_CCH_retrovir.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:4.10.60.10; Znf_CCH_retrovir; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF08783; DWNN; 1.
DR   Pfam; PF04564; U-box; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   PROSITE; PS51282; DWNN; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Chromosome; Ligase; Metal-binding;
KW   Nucleus; Phosphoprotein; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1   1790       E3 ubiquitin-protein ligase RBBP6.
FT                                /FTId=PRO_0000234355.
FT   DOMAIN        4     76       DWNN.
FT   ZN_FING     160    177       CCHC-type.
FT   ZN_FING     260    301       RING-type; degenerate.
FT   REGION      983   1139       Interaction with RB1.
FT   REGION     1434   1544       Interaction with p53.
FT   MOD_RES       7      7       N6-acetyllysine (By similarity).
FT   MOD_RES     245    245       Phosphoserine (By similarity).
FT   MOD_RES     246    246       Phosphoserine (By similarity).
FT   MOD_RES     247    247       Phosphoserine (By similarity).
FT   MOD_RES     248    248       Phosphoserine (By similarity).
FT   MOD_RES     361    361       Phosphoserine (By similarity).
FT   MOD_RES     517    517       Phosphoserine (By similarity).
FT   MOD_RES     731    731       Phosphoserine (By similarity).
FT   MOD_RES     771    771       Phosphoserine.
FT   MOD_RES     773    773       Phosphoserine.
FT   MOD_RES     862    862       Phosphoserine.
FT   MOD_RES     874    874       Phosphoserine (By similarity).
FT   MOD_RES     985    985       Phosphothreonine (By similarity).
FT   MOD_RES    1179   1179       Phosphoserine.
FT   MOD_RES    1272   1272       Phosphothreonine.
FT   MOD_RES    1278   1278       Phosphoserine.
FT   MOD_RES    1329   1329       Phosphoserine.
FT   MOD_RES    1337   1337       Phosphothreonine (By similarity).
FT   MOD_RES    1469   1469       Phosphothreonine (By similarity).
FT   MOD_RES    1571   1571       N6-acetyllysine (By similarity).
FT   MOD_RES    1625   1625       Phosphoserine (By similarity).
FT   MOD_RES    1644   1644       Phosphoserine (By similarity).
FT   MOD_RES    1646   1646       Phosphoserine (By similarity).
FT   MOD_RES    1648   1648       Phosphoserine (By similarity).
FT   MOD_RES    1651   1651       Phosphoserine (By similarity).
FT   VAR_SEQ     102    123       IDDASASISLAQLTKTANLAEA -> VCKNTITLFLHNCFY
FT                                LYNVSVT (in isoform 3).
FT                                /FTId=VSP_018285.
FT   VAR_SEQ     124   1756       Missing (in isoform 3).
FT                                /FTId=VSP_018286.
FT   VAR_SEQ     653    686       Missing (in isoform 2).
FT                                /FTId=VSP_018287.
FT   CONFLICT    254    254       I -> F (in Ref. 5; AAB49620).
FT   CONFLICT    317    318       RQ -> GR (in Ref. 4; AAC72432).
FT   CONFLICT    341    341       P -> H (in Ref. 5; AAB49620).
FT   CONFLICT    418    418       S -> F (in Ref. 4; AAC72432).
FT   CONFLICT    421    421       V -> S (in Ref. 5; AAB49620).
FT   CONFLICT    580    580       P -> L (in Ref. 4; AAC72432).
FT   CONFLICT    595    595       P -> T (in Ref. 4; AAC72432).
FT   CONFLICT    615    622       PWVSSGVQ -> ACFSPGVP (in Ref. 4;
FT                                AAC72432).
FT   CONFLICT    629    629       I -> M (in Ref. 4; AAC72432).
FT   CONFLICT    636    636       P -> L (in Ref. 4; AAC72432).
FT   CONFLICT    647    647       R -> K (in Ref. 4; AAC72432).
FT   CONFLICT    689    689       S -> F (in Ref. 4; AAC72432).
FT   CONFLICT    703    703       Y -> D (in Ref. 4; AAC72432).
FT   CONFLICT    789    789       Q -> R (in Ref. 4; AAC72432).
FT   CONFLICT    940    940       R -> Q (in Ref. 1; BAE36255).
FT   CONFLICT    941    941       R -> RNEE (in Ref. 4; AAC72432).
FT   CONFLICT    956    958       ETS -> GKF (in Ref. 4; AAC72432).
FT   CONFLICT    963    963       E -> G (in Ref. 4; AAC72432).
FT   CONFLICT    978    978       L -> F (in Ref. 4; AAC72432).
FT   CONFLICT    982    982       D -> E (in Ref. 4; AAC72432).
FT   CONFLICT   1012   1012       K -> N (in Ref. 5; AAB49620).
FT   CONFLICT   1290   1290       K -> T (in Ref. 4; AAC72432).
FT   CONFLICT   1316   1316       Q -> H (in Ref. 4; AAC72432).
FT   CONFLICT   1564   1564       N -> I (in Ref. 4; AAC72432).
FT   CONFLICT   1581   1581       E -> D (in Ref. 4; AAC72432).
FT   CONFLICT   1591   1591       P -> L (in Ref. 4; AAC72432).
FT   CONFLICT   1596   1596       P -> L (in Ref. 4; AAC72432).
FT   CONFLICT   1604   1604       A -> V (in Ref. 4; AAC72432).
SQ   SEQUENCE   1790 AA;  199587 MW;  3909C30EB9DD2CE3 CRC64;
     MSCVHYKFSS KLNYDTVTFD GLHISLCDLK KQIMGREKLK AADSDLQITN AQTKEEYTDD
     NALIPKNSSV IVRRIPIGGV KSTSKTYVIS RTEPVMGTTK AIDDASASIS LAQLTKTANL
     AEANASEEDK IKAMMSQSGH EYDPINYMKK TLVGPPPPSY TCFRCGKPGH YIKNCPTNGD
     KNFESGPRIK KSTGIPRSFM MEVKDPNMKG AMLTNTGKYA IPTIDAEAYA IGKKEKPPFL
     PEEPSSSSEE DDPIPDELLC LICKDIMTDA VVIPCCGNSY CDECIRTALL ESDEHTCPTC
     HQNDVSPDAL IANKFLRQAV NNFKNETGYT KRLRKQLPPP PPPVPPPRPL MQRNLQPLMR
     SPISRQQDPL MIPVTSSSAH SAPSISSLTS NPSALAPSVS GNPSSAPAPV PDITATVSIS
     VHSEKSDGPF RDSDNKLLPA AALTSEHSKG ASSIAITALM EEKGYQVPVL GTPSLLGQSL
     LHGQLIPTTG PVRINAARPG GGRPGWEHSN KLGYLVSPPQ QIRRGERSCY RSINRGRHHS
     ERSQRTQGPS LPATPVFVPV PPPPLYPPPP HTLPLPPGVP PPQFSPQFPP GQPPPAGYSV
     PPPGFPPAPA NISTPWVSSG VQTAHSNTIP TTQAPPLSRE EFYREQRRLK EEEKKKSKLD
     EFTNDFAKEL MEYKKIQKER RRSFSRSKSP YSGSSYSRSS YTYSKSRSGS TRSRSYSRSF
     SRSHSRSYSR SPPYPRRGRG KSRNYRSRSR SHGYHRSRSR SPPYRRYHSR SRSPQAFRGQ
     SPTKRNVPQG ETEREYFNRY REVPPPYDIK AYYGRSVDFR DPFEKERYRE WERKYREWYE
     KYYKGYAVGA QPRPSANRED FSPERLLPLN IRNSPFTRGR REDYAAGQSH RNRNLGGNYP
     EKLSTRDSHN AKDNPKSKEK ESENVPGDGK GNKHKKHRKR RKGEESESFL NPELLETSRK
     CRESSGIDET KTDTLFVLPS RDDATPVRDE PMDAESITFK SVSDKDKREK DKPKVKSDKT
     KRKSDGSATA KKDNVLKPSK GPQEKVDGDR EKSPRSEPPL KKAKEEATKI DSVKPSSSSQ
     KDEKVTGTPR KAHSKSAKEH QEAKPAKDEK VKKDCSKDIK SEKPASKDEK AKKPEKNKLL
     DSKGEKRKRK TEEKSVDKDF ESSSMKISKV EGTEIVKPSP KRKMEGDVEK LERTPEKDKI
     ASSTTPAKKI KLNRETGKKI GNAENASTTK EPSEKLESTS SKIKQEKVKG KAKRKVAGSE
     GSSSTLVDYT STSSTGGSPV RKSEEKTDTK RTVIKTMEEY NNDNTAPAED VIIMIQVPQS
     KWDKDDFESE EEDVKTTQPI QSVGKPSSII KNVTTKPSAT AKYTEKESEQ PEKLQKLPKE
     ASHELMQHEL RSSKGSASSE KGRAKDREHS GSEKDNPDKR KSGAQPDKES TVDRLSEQGH
     FKTLSQSSKE TRTSEKHESV RGSSNKDFTP GRDKKVDYDS RDYSSSKRRD ERGELARRKD
     SPPRGKESLS GQKSKLREER DLPKKGAESK KSNSSPPRDK KPHDHKAPYE TKRPCEETKP
     VDKNSGKERE KHAAEARNGK ESSGGKLPCI PNPPDPPMEK ELAAGQVEKS AVKPKPQLSH
     SSRLSSDLTR ETDEAAFEPD YNESDSESNV SVKEEEAVAS ISKDLKEKTT EKAKESLTVA
     TASQPGADRS QSQSSPSVSP SRSHSPSGSQ TRSHSSSASS AGSQDSKKKK KKKEKKKHKK
     HKKHKKHKKH AGADGDVEKS QKHKHKKKKA KKNKDKEKEK DDQKVRSVTV
//
ID   SCN1B_MOUSE             Reviewed;         218 AA.
AC   P97952;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=Sodium channel subunit beta-1;
DE   Flags: Precursor;
GN   Name=Scn1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   MEDLINE=97165884; PubMed=9013777; DOI=10.1016/S0169-328X(96)00123-4;
RA   Grosson C.L.S., Cannon S.C., Corey D.P., Gusella J.F.;
RT   "Sequence of the voltage-gated sodium channel beta1-subunit in wild-
RT   type and in quivering mice.";
RL   Brain Res. Mol. Brain Res. 42:222-226(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98387156; PubMed=9721701;
RA   Kupershmidt S., Yang T., Roden D.M.;
RT   "Modulation of cardiac Na+ current phenotype by beta1-subunit
RT   expression.";
RL   Circ. Res. 83:441-447(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Crucial in the assembly, expression, and functional
CC       modulation of the heterotrimeric complex of the sodium channel.
CC       The subunit beta-1 can modulate multiple alpha subunit isoforms
CC       from brain, skeletal muscle, and heart. Its association with
CC       neurofascin may target the sodium channels to the nodes of Ranvier
CC       of developing axons and retain these channels at the nodes in
CC       mature myelinated axons (By similarity).
CC   -!- SUBUNIT: The voltage-sensitive sodium channel consists of an ion
CC       conducting pore forming alpha-subunit regulated by one or more
CC       beta-1, beta-2 and beta-3. Beta-1 and beta-3 are non-covalently
CC       associated with alpha, while beta-2 is covalently linked by
CC       disulfide bonds. Beta-1 or beta-3 subunits associate with
CC       neurofascin. Associates with SCN10A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the sodium channel auxiliary subunit SCN1B
CC       (TC 8.A.17) family.
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
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DR   EMBL; U46681; AAC53006.1; -; mRNA.
DR   EMBL; U85786; AAB49368.1; -; mRNA.
DR   EMBL; BC009652; AAH09652.1; -; mRNA.
DR   EMBL; BC039140; AAH39140.1; -; mRNA.
DR   IPI; IPI00131062; -.
DR   RefSeq; NP_035452.1; NM_011322.2.
DR   UniGene; Mm.1418; -.
DR   ProteinModelPortal; P97952; -.
DR   SMR; P97952; 28-152.
DR   STRING; P97952; -.
DR   PhosphoSite; P97952; -.
DR   PRIDE; P97952; -.
DR   Ensembl; ENSMUST00000098548; ENSMUSP00000096148; ENSMUSG00000019194.
DR   GeneID; 20266; -.
DR   KEGG; mmu:20266; -.
DR   UCSC; uc009gie.1; mouse.
DR   CTD; 20266; -.
DR   MGI; MGI:98247; Scn1b.
DR   eggNOG; roNOG16410; -.
DR   GeneTree; ENSGT00390000018560; -.
DR   HOGENOM; HBG717666; -.
DR   HOVERGEN; HBG056582; -.
DR   InParanoid; P97952; -.
DR   OMA; ISCKKRS; -.
DR   OrthoDB; EOG4X97JG; -.
DR   NextBio; 297939; -.
DR   ArrayExpress; P97952; -.
DR   Bgee; P97952; -.
DR   CleanEx; MM_SCN1B; -.
DR   Genevestigator; P97952; -.
DR   GermOnline; ENSMUSG00000019194; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005272; F:sodium channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013151; Immunoglobulin.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF00047; ig; 1.
DR   PROSITE; PS50835; IG_LIKE; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Ion transport;
KW   Ionic channel; Membrane; Signal; Sodium; Sodium channel;
KW   Sodium transport; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   SIGNAL        1     18       By similarity.
FT   CHAIN        19    218       Sodium channel subunit beta-1.
FT                                /FTId=PRO_0000014927.
FT   TOPO_DOM     19    160       Extracellular (Potential).
FT   TRANSMEM    161    182       Helical; (Potential).
FT   TOPO_DOM    183    218       Cytoplasmic (Potential).
FT   DOMAIN       22    150       Ig-like C2-type.
FT   CARBOHYD     93     93       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    110    110       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    114    114       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    135    135       N-linked (GlcNAc...) (Potential).
FT   DISULFID     40    121       Potential.
SQ   SEQUENCE   218 AA;  24650 MW;  5198F3383B0A8CA5 CRC64;
     MGTLLALVVG AALVSSAWGG CVEVDSDTEA VYGMTFKILC ISCKRRSETT AETFTEWTFR
     QKGTEEFVKI LRYENEVLQL EEDERFEGRV VWNGSRGTKD LQDLSIFITN VTYNHSGDYE
     CHVYRLLFFD NYEHNTSVVK KIHLEVVDKA NRDMASIVSE IMMYVLIVVL TIWLVAEMVY
     CYKKIAAATE AAAQENASEY LAITSESKEN CTGVQVAE
//
ID   APBA2_MOUSE             Reviewed;         750 AA.
AC   P98084; Q6PAJ2;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Amyloid beta A4 precursor protein-binding family A member 2;
DE   AltName: Full=Adapter protein X11beta;
DE   AltName: Full=Neuron-specific X11L protein;
DE   AltName: Full=Neuronal Munc18-1-interacting protein 2;
DE            Short=Mint-2;
GN   Name=Apba2; Synonyms=X11l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 70-750.
RC   TISSUE=Brain;
RX   MEDLINE=95235202; PubMed=7719031; DOI=10.1007/BF00350899;
RA   Duclos F., Koenig M.;
RT   "Comparison of primary structure of a neuron-specific protein, X11,
RT   between human and mouse.";
RL   Mamm. Genome 6:57-58(1995).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
CC   -!- FUNCTION: Putative function in synaptic vesicle exocytosis by
CC       binding to STXBP1, an essential component of the synaptic vesicle
CC       exocytotic machinery. May modulate processing of the beta-amyloid
CC       precursor protein (APP) and hence formation of beta-APP.
CC   -!- SUBUNIT: Part of a multimeric complex containing STXBP1 and
CC       syntaxin-1. Binds to the cytoplasmic domain of amyloid protein
CC       beta, and to the nuclear factor NF-kappa-B/p65 via its PDZ domain.
CC       Interacts with the amino-terminal domain of APBA2BP (By
CC       similarity).
CC   -!- INTERACTION:
CC       P12023:App; NbExp=1; IntAct=EBI-81669, EBI-78814;
CC   -!- TISSUE SPECIFICITY: Specifically expressed in neurons,
CC       predominantly of the cerebellum, hippocampus, and spinal cord.
CC       Lesser extent in neurons of the cerebral cortex and anterior
CC       thalmic nuclei.
CC   -!- DOMAIN: Composed of an N-terminal domain that binds STXBP1, a
CC       middle phosphotyrosine-binding domain (PID/PTB) that mediates
CC       binding with the cytoplasmic domain of the beta-amyloid precursor
CC       protein, and two C-terminal PDZ domains thought to attach proteins
CC       to the plasma membrane.
CC   -!- SIMILARITY: Contains 2 PDZ (DHR) domains.
CC   -!- SIMILARITY: Contains 1 PID domain.
CC   -!- CAUTION: Was originally (PubMed:15489334) thought to be the
CC       ortholog of human X11 (APBA1).
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC060269; AAH60269.1; -; mRNA.
DR   EMBL; BC057620; AAH57620.1; -; mRNA.
DR   EMBL; L34676; AAA73936.1; -; mRNA.
DR   IPI; IPI00344688; -.
DR   RefSeq; NP_031487.1; NM_007461.2.
DR   UniGene; Mm.4657; -.
DR   ProteinModelPortal; P98084; -.
DR   SMR; P98084; 365-534, 568-750.
DR   IntAct; P98084; 1.
DR   STRING; P98084; -.
DR   PhosphoSite; P98084; -.
DR   PRIDE; P98084; -.
DR   Ensembl; ENSMUST00000032732; ENSMUSP00000032732; ENSMUSG00000030519.
DR   GeneID; 11784; -.
DR   KEGG; mmu:11784; -.
DR   UCSC; uc009hgj.1; mouse.
DR   CTD; 11784; -.
DR   MGI; MGI:1261791; Apba2.
DR   eggNOG; roNOG05572; -.
DR   HOGENOM; HBG714692; -.
DR   HOVERGEN; HBG050523; -.
DR   InParanoid; P98084; -.
DR   OMA; QEQVCNG; -.
DR   OrthoDB; EOG41G33X; -.
DR   PhylomeDB; P98084; -.
DR   NextBio; 279597; -.
DR   ArrayExpress; P98084; -.
DR   Bgee; P98084; -.
DR   Genevestigator; P98084; -.
DR   GermOnline; ENSMUSG00000030519; Mus musculus.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IGI:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IGI:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0010468; P:regulation of gene expression; IGI:MGI.
DR   GO; GO:0007268; P:synaptic transmission; IGI:MGI.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00595; PDZ; 2.
DR   Pfam; PF00640; PID; 1.
DR   SMART; SM00228; PDZ; 2.
DR   SMART; SM00462; PTB; 1.
DR   SUPFAM; SSF50156; PDZ; 2.
DR   PROSITE; PS50106; PDZ; 2.
DR   PROSITE; PS01179; PID; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Protein transport; Repeat; Transport.
FT   CHAIN         1    750       Amyloid beta A4 precursor protein-binding
FT                                family A member 2.
FT                                /FTId=PRO_0000064617.
FT   DOMAIN      367    556       PID.
FT   DOMAIN      569    654       PDZ 1.
FT   DOMAIN      660    736       PDZ 2.
FT   REGION      185    271       STXBP1-binding.
FT   MOD_RES     209    209       Phosphoserine.
FT   MOD_RES     479    479       Phosphoserine (By similarity).
FT   MOD_RES     481    481       Phosphoserine (By similarity).
FT   CONFLICT    313    313       K -> M (in Ref. 2; AAA73936).
FT   CONFLICT    388    388       N -> T (in Ref. 2; AAA73936).
FT   CONFLICT    402    402       V -> A (in Ref. 2; AAA73936).
FT   CONFLICT    677    679       QNG -> RW (in Ref. 2; AAA73936).
FT   CONFLICT    688    690       GIA -> VLQ (in Ref. 2; AAA73936).
SQ   SEQUENCE   750 AA;  82758 MW;  FC231C966DB467DE CRC64;
     MAHRKRQSTA SSMLDHRARP GPIPHDQEPE SEDTELPLES YVPTGLELGT LRPESPTPEE
     QECHNHSPDG DSSSDYVNNT SEEEDYDEGL PEEEEGVTYY IRYCPEDDSY LEGMDCNGEE
     YIAHGAHPVD TDECQEAVED WTDSVGPHTH SHGAENSQEY PDGHLPIPED DPTVLEVHDQ
     EEDGHYCSSK ESYQDYYPPE TNGNTGGASP YRMRRGDGDL EEQEEDIDQI VAEIKMSLSM
     TSITSASEAS PEHMPELDPG DSTEACPPSD TGHGPGRQEA RPKSLNLPPE VKHPGDLQRG
     LKTKTRTPEE RPKWPQEQVC NGLEQPRKQQ RSDLNGPTDN NNIPETKKVA SFPSFVAVPG
     PCEAEDLIDG IIFAANYLGS TQLLSERNPS KNIRMMQAQE AVSRVKRMQK AAKIKKKANS
     EGDAQTLTEV DLFISTQRIK VLNADTQETM MDHALRTISY IADIGNIVVL MARRRMPRSA
     SQDCIETTPG AQEGKKQYKM ICHVFESEDA QLIAQSIGQA FSVAYQEFLR ANGINPEDLS
     QKEYSDIINT QEMYNDDLIH FSNSENCKEL QLEKHKGEIL GVVVVESGWG SILPTVILAN
     MMNGGPAARS GKLSIGDQIM SINGTSLVGL PLATCQGIIK GLKNQTQVKL NIVSCPPVTT
     VLIKRPDLKY QLGFSVQNGI ICSLMRGGIA ERGGVRVGHR IIEINGQSVV ATAHEKIVQA
     LSNSVGEIHM KTMPAAMFRL LTGQETPLYI
//
ID   CDS1_MOUSE              Reviewed;         461 AA.
AC   P98191; Q8CGZ1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Phosphatidate cytidylyltransferase 1;
DE            EC=2.7.7.41;
DE   AltName: Full=CDP-DAG synthase 1;
DE   AltName: Full=CDP-DG synthase 1;
DE   AltName: Full=CDP-diacylglycerol synthase 1;
DE            Short=CDS 1;
DE   AltName: Full=CDP-diglyceride pyrophosphorylase 1;
DE   AltName: Full=CDP-diglyceride synthase 1;
DE   AltName: Full=CTP:phosphatidate cytidylyltransferase 1;
GN   Name=Cds1; Synonyms=Cds;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Inglis S.L., Hunt D.M., Halford S.;
RT   "Isolation and characterization of murine Cds (CDP-diacylglycerol
RT   synthase) 1 and 2.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION.
RX   MEDLINE=98070552; PubMed=9407135; DOI=10.1074/jbc.272.52.33402;
RA   Lykidis A., Jackson P.D., Rock C.O., Jackowski S.;
RT   "The role of CDP-diacylglycerol synthetase and phosphatidylinositol
RT   synthase activity levels in the regulation of cellular
RT   phosphatidylinositol content.";
RL   J. Biol. Chem. 272:33402-33409(1997).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=99107812; PubMed=9889000; DOI=10.1006/geno.1998.5610;
RA   Volta M., Bulfone A., Gattuso C., Rossi E., Mariani M., Consalez G.G.,
RA   Zuffardi O., Ballabio A., Banfi S., Franco B.;
RT   "Identification and characterization of CDS2, a mammalian homolog of
RT   the Drosophila CDP-diacylglycerol synthase gene.";
RL   Genomics 55:68-77(1999).
CC   -!- FUNCTION: Provides CDP-diacylglycerol an important precursor for
CC       the synthesis of phosphatidylinositol (PtdIns),
CC       phosphatidylglycerol, and cardiolipin. Overexpression may amplify
CC       cellular signaling responses from cytokines. May also play an
CC       important role in the signal transduction mechanism of retina and
CC       neural cells (By similarity).
CC   -!- CATALYTIC ACTIVITY: CTP + phosphatidate = diphosphate + CDP-
CC       diacylglycerol.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CC       CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity). Note=Cytoplasmic aspect of the
CC       endoplasmic reticulum (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in the inner segment of the
CC       photoreceptor layer of adult retina.
CC   -!- DEVELOPMENTAL STAGE: Expressed in a structure probably
CC       corresponding to the thymic rudiment at embryonic day 12.5 of
CC       gestation (E12.5). No expression could be detected at earlier and
CC       later stages of embryonic development (E10.5 and E17.5).
CC   -!- SIMILARITY: Belongs to the CDS family.
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DR   EMBL; AF533367; AAO16167.2; -; mRNA.
DR   EMBL; BC055292; AAH55292.1; -; mRNA.
DR   IPI; IPI00229605; -.
DR   RefSeq; NP_775546.2; NM_173370.3.
DR   UniGene; Mm.46764; -.
DR   STRING; P98191; -.
DR   PhosphoSite; P98191; -.
DR   PRIDE; P98191; -.
DR   Ensembl; ENSMUST00000031273; ENSMUSP00000031273; ENSMUSG00000029330.
DR   GeneID; 74596; -.
DR   KEGG; mmu:74596; -.
DR   UCSC; uc008yio.1; mouse.
DR   CTD; 74596; -.
DR   MGI; MGI:1921846; Cds1.
DR   eggNOG; roNOG08599; -.
DR   GeneTree; ENSGT00390000016175; -.
DR   HOGENOM; HBG629124; -.
DR   HOVERGEN; HBG002485; -.
DR   InParanoid; P98191; -.
DR   OMA; KDFADTI; -.
DR   OrthoDB; EOG4V437K; -.
DR   PhylomeDB; P98191; -.
DR   BRENDA; 2.7.7.41; 244.
DR   NextBio; 341181; -.
DR   ArrayExpress; P98191; -.
DR   Bgee; P98191; -.
DR   CleanEx; MM_CDS1; -.
DR   Genevestigator; P98191; -.
DR   GermOnline; ENSMUSG00000029330; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:EC.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000374; PC_trans.
DR   InterPro; IPR016720; PC_Trfase_euk.
DR   Pfam; PF01148; CTP_transf_1; 1.
DR   PIRSF; PIRSF018269; PC_trans_euk; 1.
DR   PROSITE; PS01315; CDS; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Magnesium; Membrane; Nucleotidyltransferase;
KW   Phospholipid biosynthesis; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    461       Phosphatidate cytidylyltransferase 1.
FT                                /FTId=PRO_0000090714.
FT   TRANSMEM     96    116       Helical; (Potential).
FT   TRANSMEM    149    169       Helical; (Potential).
FT   TRANSMEM    183    203       Helical; (Potential).
FT   TRANSMEM    230    250       Helical; (Potential).
FT   TRANSMEM    279    299       Helical; (Potential).
FT   TRANSMEM    357    377       Helical; (Potential).
SQ   SEQUENCE   461 AA;  52875 MW;  B6AD0DB2124E0D71 CRC64;
     MLELRHRGGC PGPGGAGAPP PREGEAAGGD HETESTSDKE TDIDDRYGDL DARGDSDVPE
     VPPSSDRTPE ILKKALSGLS SRWKNWWIRG ILTLTMISLF FLIIYMGSFM LMLLVLGIQV
     KCFHEIITIG YRVYHSYDLP WFRTLSWYFL LCVNYFFYGE TVADYFATFV QREEQLQFLI
     RYHRFISFAL YLAGFCMFVL SLVKKHYRLQ FYMFAWTHVT LLITVTQSHL VIQNLFEGMI
     WFLVPISSVI CNDITAYLFG FFFGRTPLIK LSPKKTWEGF IGGFFSTVIF GFIAAYVLSK
     YQYFVCPVEY RSDVNSFVTE CEPSELFQLQ NYSLPPFLQA VLSRETVSLY PFQIHSIALS
     TFASLIGPFG GFFASGFKRA FKIKDFANTI PGHGGIMDRF DCQYLMATFV HVYITSFIRG
     PNPSKVLQQL LVLQPEQQLN IYRTLKIHLT EKGILQPTLK V
//
ID   GNPAT_MOUSE             Reviewed;         678 AA.
AC   P98192; Q9WUT6;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Dihydroxyacetone phosphate acyltransferase;
DE            Short=DAP-AT;
DE            Short=DHAP-AT;
DE            EC=2.3.1.42;
DE   AltName: Full=Acyl-CoA:dihydroxyacetonephosphateacyltransferase;
DE   AltName: Full=Glycerone-phosphate O-acyltransferase;
GN   Name=Gnpat; Synonyms=Dhapat;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Fibroblast;
RX   MEDLINE=99326186; PubMed=10395968; DOI=10.1016/S1388-1981(99)00081-5;
RA   Ofman R., Hogenhout E.M., Wanders R.J.A.;
RT   "Identification and characterization of the mouse cDNA encoding acyl-
RT   CoA:dihydroxyacetone phosphate acyltransferase.";
RL   Biochim. Biophys. Acta 1439:89-94(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99383224; PubMed=10456321; DOI=10.1016/S0014-5793(99)00968-0;
RA   Thai T.P., Rodemer C., Worsch J., Hunziker A., Gorgas K., Just W.W.;
RT   "Synthesis of plasmalogens in eye lens epithelial cells.";
RL   FEBS Lett. 456:263-268(1999).
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + glycerone phosphate = CoA +
CC       acylglycerone phosphate.
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid
CC       metabolism.
CC   -!- SUBUNIT: May be part of an heterotrimeric complex composed of DAP-
CC       AT, ADAP-S and a modified form of DAP-AT.
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane; Peripheral membrane
CC       protein; Matrix side (By similarity). Note=Exclusively localized
CC       to the lumenal side of the peroxisomal membrane (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in liver and testis. Lower
CC       levels in heart, brain, lung and kidney. Detected in spleen.
CC   -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity
CC       and may constitute the binding site for the phosphate moiety of
CC       the glycerol-3-phosphate (By similarity).
CC   -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
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DR   EMBL; AF110769; AAD55351.1; -; mRNA.
DR   EMBL; AJ132012; CAB41975.1; -; mRNA.
DR   IPI; IPI00126660; -.
DR   RefSeq; NP_034452.3; NM_010322.3.
DR   UniGene; Mm.29114; -.
DR   ProteinModelPortal; P98192; -.
DR   IntAct; P98192; 2.
DR   STRING; P98192; -.
DR   PhosphoSite; P98192; -.
DR   PRIDE; P98192; -.
DR   Ensembl; ENSMUST00000034466; ENSMUSP00000034466; ENSMUSG00000031985.
DR   GeneID; 14712; -.
DR   KEGG; mmu:14712; -.
DR   CTD; 14712; -.
DR   MGI; MGI:1343460; Gnpat.
DR   eggNOG; roNOG08043; -.
DR   HOGENOM; HBG445195; -.
DR   HOVERGEN; HBG051749; -.
DR   InParanoid; P98192; -.
DR   OMA; CYQIICK; -.
DR   OrthoDB; EOG4DJJW5; -.
DR   PhylomeDB; P98192; -.
DR   BRENDA; 2.3.1.42; 244.
DR   NextBio; 286715; -.
DR   ArrayExpress; P98192; -.
DR   Bgee; P98192; -.
DR   CleanEx; MM_GNPAT; -.
DR   Genevestigator; P98192; -.
DR   GermOnline; ENSMUSG00000031985; Mus musculus.
DR   GO; GO:0005782; C:peroxisomal matrix; TAS:MGI.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016287; F:glycerone-phosphate O-acyltransferase activity; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0016044; P:cellular membrane organization; IMP:MGI.
DR   GO; GO:0021587; P:cerebellum morphogenesis; IMP:MGI.
DR   GO; GO:0008611; P:ether lipid biosynthetic process; IMP:MGI.
DR   GO; GO:0030913; P:paranodal junction assembly; IMP:MGI.
DR   GO; GO:0007416; P:synapse assembly; IMP:MGI.
DR   InterPro; IPR002123; Acyltransferase.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Acyltransferase; Membrane; Peroxisome; Transferase.
FT   CHAIN         1    678       Dihydroxyacetone phosphate
FT                                acyltransferase.
FT                                /FTId=PRO_0000195247.
FT   MOTIF       161    166       HXXXXD motif.
FT   MOTIF       676    678       Microbody targeting signal (Potential).
FT   COMPBIAS      5      9       Poly-Ser.
FT   MOD_RES     641    641       N6-acetyllysine (By similarity).
SQ   SEQUENCE   678 AA;  76870 MW;  FA7245A2DDD174FF CRC64;
     MDVPSSSSSR FSVGSASPSS VLLYAKDLKK WDEFEDLLEE RRHISDFKFA MKCYTPPLYR
     GITPCKPGDI KSIVLSSEEI NYVIKQLSRE SLTGVDVLRE EASEILEEMS HKLRIGAIRF
     FAFVLSKIFK QIFSKVCVNE EGIQKLQRAV QEHPVVLLPS HRSYIDFLML SFILYSYDLP
     VPVIAAGMDF LGMRVVSELL RMSGAFFMRR TFGGNKLYWA VFSEYVKTML RCGYAPVEFF
     LEGTRSRAAK TLTPKFGLLN IVMEPFFKRE VFDTYFVPIS ISYDKILEES LYAYEILGVP
     KPKESTTGLL KARRILSENF GSIHVYFGDP VSLRSLAAGR LNRNTYNLVP RCIPQKQPED
     VQAFVTEVAY KMQLLQIENL ALSPWLLVVT ILLQNQLSMD FDALVEKTLW LKGVTQVFGG
     FLLWPDNKLP EEVVQSSILL HSNLASLVKD QVVLKMNSGS SQVVNGLVPE HIALLMCSAY
     RNQLLNIFAR PSLVALALHM TPGLRKEDVF SCFSFLRNVF SDEFIFLPGN TLRDFEEGCY
     LLCKAEAMQM AGKDIILTDK GTAVLQFLTS LFKPFVESYQ LLCRYLLHEE DYFGEKEYLV
     AARKFTRQLL DQGSSQCYDA LSSELQKNAL AAFVRLGVVE KKKVDSKYVY YVNGPATSKL
     EEMLGCKKPI GKPATAKL
//
ID   AT8A2_MOUSE             Reviewed;        1148 AA.
AC   P98200; B2RQF2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Probable phospholipid-transporting ATPase IB;
DE            EC=3.6.3.1;
DE   AltName: Full=ATPase class I type 8A member 2;
GN   Name=Atp8a2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR;
RX   MEDLINE=20473714; PubMed=11015572;
RA   Halleck M.S., Lawler J.F. Jr., Blackshaw S., Gao L., Nagarajan P.,
RA   Hacker C., Pyle S., Newman J.T., Nakanishi Y., Ando H., Weinstock D.,
RA   Williamson P.L., Schlegel R.A.;
RT   "Differential expression of putative transbilayer amphipath
RT   transporters.";
RL   Physiol. Genomics 1:139-150(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + phospholipid(In) = ADP +
CC       phosphate + phospholipid(Out).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Found in testis, heart and brain. Most
CC       abundant in testis. Also detected in fetal tissues.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       (TC 3.A.3) family. Type IV subfamily.
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DR   EMBL; AF156550; AAF09448.1; -; mRNA.
DR   EMBL; BC137896; AAI37897.1; -; mRNA.
DR   IPI; IPI00127464; -.
DR   RefSeq; NP_056618.1; NM_015803.2.
DR   UniGene; Mm.319599; -.
DR   ProteinModelPortal; P98200; -.
DR   SMR; P98200; 761-815.
DR   STRING; P98200; -.
DR   TCDB; 3.A.3.8.8; P-type ATPase (P-ATPase) superfamily.
DR   PRIDE; P98200; -.
DR   Ensembl; ENSMUST00000080368; ENSMUSP00000079238; ENSMUSG00000021983.
DR   GeneID; 50769; -.
DR   KEGG; mmu:50769; -.
DR   UCSC; uc007uet.1; mouse.
DR   CTD; 50769; -.
DR   MGI; MGI:1354710; Atp8a2.
DR   eggNOG; roNOG14737; -.
DR   GeneTree; ENSGT00570000078774; -.
DR   HOGENOM; HBG745019; -.
DR   HOVERGEN; HBG050601; -.
DR   InParanoid; P98200; -.
DR   OMA; ETKSRVM; -.
DR   OrthoDB; EOG4V9TPV; -.
DR   PhylomeDB; P98200; -.
DR   BRENDA; 3.6.3.1; 244.
DR   NextBio; 307683; -.
DR   ArrayExpress; P98200; -.
DR   Bgee; P98200; -.
DR   Genevestigator; P98200; -.
DR   GermOnline; ENSMUSG00000021983; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015662; F:ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004012; F:phospholipid-translocating ATPase activity; IEA:EC.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   InterPro; IPR023306; ATPase_cation_domN.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR023300; ATPase_P-typ_cyto_domA.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR006539; ATPase_P-typ_Plipid-transl.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Gene3D; G3DSA:2.70.150.10; ATPase_P-typ_cyto_domA; 2.
DR   Gene3D; G3DSA:3.40.1110.10; ATPase_P-typ_cyto_domN; 1.
DR   Gene3D; G3DSA:3.40.50.1000; HAD-like_dom; 2.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SUPFAM; SSF81660; ATPase_cation_domN; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Hydrolase; Magnesium; Membrane; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   1148       Probable phospholipid-transporting ATPase
FT                                IB.
FT                                /FTId=PRO_0000046363.
FT   TOPO_DOM      1     44       Cytoplasmic (Potential).
FT   TRANSMEM     45     66       Helical; (Potential).
FT   TOPO_DOM     67     71       Extracellular (Potential).
FT   TRANSMEM     72     94       Helical; (Potential).
FT   TOPO_DOM     95    276       Cytoplasmic (Potential).
FT   TRANSMEM    277    298       Helical; (Potential).
FT   TOPO_DOM    299    323       Extracellular (Potential).
FT   TRANSMEM    324    345       Helical; (Potential).
FT   TOPO_DOM    346    837       Cytoplasmic (Potential).
FT   TRANSMEM    838    858       Helical; (Potential).
FT   TOPO_DOM    859    870       Extracellular (Potential).
FT   TRANSMEM    871    890       Helical; (Potential).
FT   TOPO_DOM    891    920       Cytoplasmic (Potential).
FT   TRANSMEM    921    942       Helical; (Potential).
FT   TOPO_DOM    943    956       Extracellular (Potential).
FT   TRANSMEM    957    979       Helical; (Potential).
FT   TOPO_DOM    980    985       Cytoplasmic (Potential).
FT   TRANSMEM    986   1006       Helical; (Potential).
FT   TOPO_DOM   1007   1024       Extracellular (Potential).
FT   TRANSMEM   1025   1049       Helical; (Potential).
FT   TOPO_DOM   1050   1148       Cytoplasmic (Potential).
FT   ACT_SITE    388    388       4-aspartylphosphate intermediate (By
FT                                similarity).
FT   METAL       781    781       Magnesium (By similarity).
FT   METAL       785    785       Magnesium (By similarity).
FT   MOD_RES       5      5       Phosphothreonine.
SQ   SEQUENCE   1148 AA;  129417 MW;  A668D6F343CAAAB8 CRC64;
     MSRATSVGDQ LEAPARIIYL NQSHLNKFCD NRISTAKYSV LTFLPRFLYE QIRRAANAFF
     LFIALLQQIP DVSPTGRYTT LVPLVIILTI AGIKEIIEDF KRHKADNAVN KKKTIVLRNG
     MWHTIMWKEV AVGDIVKVLN GQYLPADMVL FSSSEPQGMC YVETANLDGE TNLKIRQGLS
     HTTDMQTRDV LMKLSGRIEC EGPNRHLYDF TGNLHLDGKS SVALGPDQIL LRGTQLRNTQ
     WVFGVVVYTG HDSKLMQNST KAPLKRSNVE KVTNVQILVL FGILLVMALV SSVGALFWNG
     SHGGKSWYIK KMDTNSDNFG YNLLTFIILY NNLIPISLLV TLEVVKYTQA LFINWDMDMY
     YIENDTPAMA RTSNLNEELG QVKYLFSDKT GTLTCNIMNF KKCSIAGVTY GHFPELAREQ
     SSDDFCRMTS CTNDSCDFND PRLLKNIEDQ HPTAPCIQEF LTLLAVCHTV VPEKDGDEII
     YQASSPDEAA LVKGAKKLGF VFTGRTPYSV IIEAMGQEQT FGILNVLEFS SDRKRMSVIV
     RLPSGQLRLY CKGADNVIFE RLSKDSKYME ETLCHLEYFA TEGLRTLCVA YADLSENEYE
     EWLKVYQEAS IILKDRAQRL EECYEIIEKN LLLLGATAIE DRLQAGVPET IATLLKAEIK
     IWVLTGDKQE TAINIGYSCR LVSQNMALIL LKEDSLDATR AAITQHCTDL GNLLGKENDV
     ALIIDGHTLK YALSFEVRRS FLDLALSCKA VICCRVSPLQ KSEIVDVVKK RVKAITLAIG
     DGANDVGMIQ TAHVGVGISG NEGMQATNNS DYAIAQFSYL EKLLLVHGAW SYNRVTKCIL
     YCFYKNVVLY IIELWFAFVN GFSGQILFER WCIGLYNVIF TALPPFTLGI FERSCTQESM
     LRFPQLYRIT QNAEGFNTKV FWGHCINALV HSLILFWVPM KALEHDTPVT SGHATDYLFV
     GNIVYTYVVV TVCLKAGLET TAWTKFSHLA VWGSMLIWLV FFGVYSTIWP TIPIAPDMKG
     QATMVLSSAY FWLGLFLVPT ACLIEDVAWR AAKHTCKKTL LEEVQELETK SRVMGKAMLR
     DSNGKRMNER DRLIKRLSRK TPPTLFRTGS IQQCVSHGYA FSQEEHGAVT QEEIVRAYDT
     TKENSRKK
//
ID   ARVC_MOUSE              Reviewed;         962 AA.
AC   P98203; Q6PGJ6; Q8BQ36; Q8BRF2; Q8C3U7; Q924L2; Q924L3; Q924L4;
AC   Q924L5;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 2.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Armadillo repeat protein deleted in velo-cardio-facial syndrome homolog;
GN   Name=Arvcf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4 AND 5).
RC   STRAIN=C57BL/6;
RA   Saint-Jore B., Puech A., Merscher S., Xu H., Kucherlapati R.,
RA   Skoultchi A.;
RT   "Developmental expression analysis of Arvcf, a candidate gene for
RT   velo-cardio-facial syndrome.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic ganglion, and Embryonic lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-962 (ISOFORM 3).
RX   MEDLINE=20512094; PubMed=11058098;
RA   Kaufmann U., Zuppinger C., Waibler Z., Rudiger M., Urbich C.,
RA   Martin B., Jockusch B.M., Eppenberger H., Starzinski-Powitz A.;
RT   "The armadillo repeat region targets ARVCF to cadherin-based cellular
RT   junctions.";
RL   J. Cell Sci. 113:4121-4135(2000).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-643, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Involved in protein-protein interactions at adherens
CC       junctions (By similarity).
CC   -!- SUBUNIT: Interacts (via the extreme C-terminus) with FRMPD2 (via
CC       the PDZ 2 domain).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1; Synonyms=A1;
CC         IsoId=P98203-1; Sequence=Displayed;
CC       Name=2; Synonyms=A2;
CC         IsoId=P98203-2; Sequence=VSP_014923;
CC       Name=3;
CC         IsoId=P98203-3; Sequence=VSP_014923, VSP_014924;
CC         Note=No experimental confirmation available;
CC       Name=4; Synonyms=B2;
CC         IsoId=P98203-4; Sequence=VSP_014922, VSP_014923;
CC       Name=5; Synonyms=B1;
CC         IsoId=P98203-5; Sequence=VSP_014922;
CC   -!- SIMILARITY: Belongs to the beta-catenin family.
CC   -!- SIMILARITY: Contains 10 ARM repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF286212; AAK64214.1; -; mRNA.
DR   EMBL; AF286213; AAK64215.1; -; mRNA.
DR   EMBL; AF286214; AAK64216.1; -; mRNA.
DR   EMBL; AF286215; AAK64217.1; -; mRNA.
DR   EMBL; AK044982; BAC32169.1; -; mRNA.
DR   EMBL; AK051627; BAC34696.1; -; mRNA.
DR   EMBL; AK084886; BAC39302.1; -; mRNA.
DR   EMBL; BC056980; AAH56980.1; -; mRNA.
DR   EMBL; AJ243418; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00127472; -.
DR   IPI; IPI00420926; -.
DR   IPI; IPI00620282; -.
DR   IPI; IPI00621122; -.
DR   IPI; IPI00625693; -.
DR   RefSeq; NP_258435.2; NM_033474.2.
DR   UniGene; Mm.293599; -.
DR   ProteinModelPortal; P98203; -.
DR   SMR; P98203; 355-852.
DR   STRING; P98203; -.
DR   PhosphoSite; P98203; -.
DR   PRIDE; P98203; -.
DR   Ensembl; ENSMUST00000090103; ENSMUSP00000087562; ENSMUSG00000000325.
DR   Ensembl; ENSMUST00000115611; ENSMUSP00000111274; ENSMUSG00000000325.
DR   Ensembl; ENSMUST00000115613; ENSMUSP00000111276; ENSMUSG00000000325.
DR   Ensembl; ENSMUST00000115614; ENSMUSP00000111278; ENSMUSG00000000325.
DR   Ensembl; ENSMUST00000115618; ENSMUSP00000111281; ENSMUSG00000000325.
DR   GeneID; 11877; -.
DR   KEGG; mmu:11877; -.
DR   UCSC; uc007ynl.1; mouse.
DR   UCSC; uc007ynm.1; mouse.
DR   UCSC; uc007ynq.1; mouse.
DR   UCSC; uc007yns.1; mouse.
DR   CTD; 11877; -.
DR   MGI; MGI:109620; Arvcf.
DR   eggNOG; roNOG07366; -.
DR   GeneTree; ENSGT00550000074290; -.
DR   HOVERGEN; HBG004284; -.
DR   OMA; ATYIRAT; -.
DR   OrthoDB; EOG4F1X2D; -.
DR   NextBio; 279903; -.
DR   ArrayExpress; P98203; -.
DR   Bgee; P98203; -.
DR   Genevestigator; P98203; -.
DR   GermOnline; ENSMUSG00000000325; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0016339; P:calcium-dependent cell-cell adhesion; TAS:MGI.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 2.
DR   Pfam; PF00514; Arm; 3.
DR   SMART; SM00185; ARM; 6.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Coiled coil; Phosphoprotein;
KW   Repeat.
FT   CHAIN         1    962       Armadillo repeat protein deleted in velo-
FT                                cardio-facial syndrome homolog.
FT                                /FTId=PRO_0000064295.
FT   REPEAT      350    389       ARM 1.
FT   REPEAT      392    431       ARM 2.
FT   REPEAT      435    469       ARM 3.
FT   REPEAT      470    510       ARM 4.
FT   REPEAT      528    567       ARM 5.
FT   REPEAT      577    623       ARM 6.
FT   REPEAT      647    687       ARM 7.
FT   REPEAT      700    739       ARM 8.
FT   REPEAT      740    782       ARM 9.
FT   REPEAT      783    827       ARM 10.
FT   COILED       11     46       Potential.
FT   MOTIF       608    624       Nuclear localization signal (Potential).
FT   MOD_RES     269    269       Phosphoserine.
FT   MOD_RES     643    643       Phosphothreonine.
FT   MOD_RES     864    864       Phosphoserine (By similarity).
FT   MOD_RES     871    871       Phosphoserine (By similarity).
FT   MOD_RES     872    872       Phosphothreonine (By similarity).
FT   VAR_SEQ       1     70       MEDCNVHSAASILASVKEQEARFERLTRALEQERRHVALQL
FT                                ERAQQPGMSSGGMVGSGQPLPMAWQQLVL -> MPAELR
FT                                (in isoform 4 and isoform 5).
FT                                /FTId=VSP_014922.
FT   VAR_SEQ     625    630       Missing (in isoform 2, isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_014923.
FT   VAR_SEQ     928    962       PDPGRKAPPPGPSRPSVRLVDAVGDTKPQPVDSWV -> VY
FT                                GQGVYCGPLEKAASTTCVPVSWLHVPASGALAQLFVLRDRI
FT                                EVAGRGPEGPPS (in isoform 3).
FT                                /FTId=VSP_014924.
FT   CONFLICT     72     72       E -> G (in Ref. 3; AAH56980).
FT   CONFLICT    372    372       P -> T (in Ref. 2; BAC39302).
FT   CONFLICT    504    504       R -> L (in Ref. 1; AAK64214/AAK64215/
FT                                AAK64216/AAK64217).
FT   CONFLICT    560    560       V -> E (in Ref. 2; BAC39302).
FT   CONFLICT    761    761       N -> K (in Ref. 2; BAC39302).
SQ   SEQUENCE   962 AA;  105066 MW;  8F43E9DC34709406 CRC64;
     MEDCNVHSAA SILASVKEQE ARFERLTRAL EQERRHVALQ LERAQQPGMS SGGMVGSGQP
     LPMAWQQLVL QEQSPGSQAS LATMPEAPEV LEETVTVEED PGTPTSHVSI VTSEDGTTRR
     TETKVTKTVK TVTTRTVRQV PLGPDGLPLL DGGPPLGSFA DGPLDRHYLL RGGGGPAATL
     SRTYHSSGGG FPDGPESRDI PSYGSLSRGL GVRPPRTGLL GPGPGDGCFT LPGRREAFPM
     GSESGPPSGR SLPEHFQAEP YGLEDDTRSL AADDEGGPDL EPDYSTATRR RPEYGRGLRA
     RAFEDTADDA GELIEERPPF PAATAPLAQP ERGSLGSLDR VVRRSPSVDS TRKEPRWRDP
     ELPEVLAMLR HPVDPVKANA AAYLQHLCFE NEGIKRRVRQ LRGLPLLVAL LDHPRAEVRR
     RACGALRNLS YGRDTDNKAA IRDCGGVPAL VRLLRAARDN EVRELVTGTL WNLSSYEPLK
     MVIIDHGLQT LTHEVIVPHS GWEREPNEDS KPRDAEWTTV FKNTSGCLRN VSSDGAEARR
     RLRECEGLVD ALLHALQSAV GRKDTDNKSV ENCVCIMRNL SYHVHKEVPG ADRYQEAEPG
     IPGSTTSQRR RKDDASCFGG KKAKEEWFHQ GKKDAEMDRN FDTLDLPKRT EAAKGFELLY
     QPEVVRLYLS LLTESRNFNT LEAAAGALQN LSAGNWTWAT YIRATVRKER GLPVLVELLQ
     SETDKVVRAV AIALRNLSLD QRNKDLIGSY AMTELVRNVR NAQAPAHPSA HLEEDTVVAV
     LNTIHEIVSD SLDNARSLLQ ARGVPALVAL VASSQSVREA KAASHVLQTV WSYKELRGAL
     QRDGWTKSRF QSASTAKGPK GTPSSGGFDD STLPLVDKSL DGEKSNTRDV IPMDTLGPDG
     YATVDRRERR TLGSDSTGDT SEKELLRPDP GRKAPPPGPS RPSVRLVDAV GDTKPQPVDS
     WV
//
ID   TBB5_MOUSE              Reviewed;         444 AA.
AC   P99024; B1B178; P05218; Q3TFB6; Q3THH9; Q3TIL1; Q3UAV4; Q3UF52;
AC   Q8WUC1; Q9CY33;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Tubulin beta-5 chain;
GN   Name=Tubb5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=87057644; PubMed=3782288; DOI=10.1083/jcb.103.5.1903;
RA   Wang D., Villasante A., Lewis S.A., Cowan N.J.;
RT   "The mammalian beta-tubulin repertoire: hematopoietic expression of a
RT   novel, heterologous beta-tubulin isotype.";
RL   J. Cell Biol. 103:1903-1910(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2;
RC   TISSUE=Bone marrow, Embryo, Kidney, Liver, Pituitary, Placenta,
RC   Spinal ganglion, Spleen, Sympathetic ganglion, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 3-19; 63-121; 163-174; 217-241; 242-276; 283-297;
RP   310-318; 321-359 AND 381-390, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 325-444.
RX   MEDLINE=85289512; PubMed=3839797; DOI=10.1083/jcb.101.3.852;
RA   Lewis S.A., Lee M.G.-S., Cowan N.J.;
RT   "Five mouse tubulin isotypes and their regulated expression during
RT   development.";
RL   J. Cell Biol. 101:852-861(1985).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15648052; DOI=10.1002/pmic.200401066;
RA   Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA   Hart G.W., Burlingame A.L.;
RT   "Quantitative analysis of both protein expression and serine /
RT   threonine post-translational modifications through stable isotope
RT   labeling with dithiothreitol.";
RL   Proteomics 5:388-398(2005).
RN   [8]
RP   POLYGLUTAMYLATION.
RX   PubMed=15890843; DOI=10.1126/science.1113010;
RA   Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M.,
RA   Temurak N., van Dijk J., Boucher D., van Dorsselaer A.,
RA   Suryavanshi S., Gaertig J., Edde B.;
RT   "Tubulin polyglutamylase enzymes are members of the TTL domain protein
RT   family.";
RL   Science 308:1758-1762(2005).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-340, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-340, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [11]
RP   POLYGLYCYLATION.
RX   PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA   Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M.,
RA   Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J.,
RA   Janke C.;
RT   "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT   polyglycylation.";
RL   Cell 137:1076-1087(2009).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. It
CC       binds two moles of GTP, one at an exchangeable site on the beta
CC       chain and one at a non-exchangeable site on the alpha-chain.
CC   -!- SUBUNIT: Dimer of alpha and beta chains.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in
CC       spleen, thymus and immature brain.
CC   -!- PTM: Some glutamate residues at the C-terminus are either
CC       polyglutamylated or polyglycylated. These 2 modifications occur
CC       exclusively on glutamate residues and result in either
CC       polyglutamate or polyglycine chains on the gamma-carboxyl group.
CC       Glycylation is mainly limited to tubulin incorporated into
CC       axonemes (cilia and flagella) whereas glutamylation is prevalent
CC       in neuronal cells, centrioles, axonemes, and the mitotic spindle.
CC       Both modifications can coexist on the same protein on adjacent
CC       residues, and lowering polyglycylation levels increases
CC       polyglutamylation, and reciprocally. The precise function of such
CC       modifications is still unclear but they are regulate the assembly
CC       and dynamics of axonemal microtubules.
CC   -!- SIMILARITY: Belongs to the tubulin family.
CC   -----------------------------------------------------------------------
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DR   EMBL; X04663; CAA28369.1; -; mRNA.
DR   EMBL; AK010960; BAB27292.1; -; mRNA.
DR   EMBL; AK011263; BAB27504.1; -; mRNA.
DR   EMBL; AK051164; BAC34541.1; -; mRNA.
DR   EMBL; AK051393; BAC34623.1; -; mRNA.
DR   EMBL; AK083327; BAC38866.1; -; mRNA.
DR   EMBL; AK146567; BAE27265.1; -; mRNA.
DR   EMBL; AK148978; BAE28709.1; -; mRNA.
DR   EMBL; AK151215; BAE30210.1; -; mRNA.
DR   EMBL; AK151670; BAE30596.1; -; mRNA.
DR   EMBL; AK160225; BAE35700.1; -; mRNA.
DR   EMBL; AK161575; BAE36471.1; -; mRNA.
DR   EMBL; AK165249; BAE38103.1; -; mRNA.
DR   EMBL; AK167691; BAE39738.1; -; mRNA.
DR   EMBL; AK167779; BAE39811.1; -; mRNA.
DR   EMBL; AK167808; BAE39835.1; -; mRNA.
DR   EMBL; AK167926; BAE39931.1; -; mRNA.
DR   EMBL; AK168271; BAE40217.1; -; mRNA.
DR   EMBL; AK169123; BAE40903.1; -; mRNA.
DR   EMBL; AK169210; BAE40982.1; -; mRNA.
DR   EMBL; AK169295; BAE41051.1; -; mRNA.
DR   EMBL; CR974451; CAO77890.1; -; Genomic_DNA.
DR   EMBL; BC003825; AAH03825.1; -; mRNA.
DR   EMBL; M28732; AAA40510.1; -; mRNA.
DR   IPI; IPI00117352; -.
DR   PIR; E25437; E25437.
DR   RefSeq; NP_035785.1; NM_011655.5.
DR   UniGene; Mm.273538; -.
DR   UniGene; Mm.472638; -.
DR   ProteinModelPortal; P99024; -.
DR   SMR; P99024; 2-427.
DR   STRING; P99024; -.
DR   PhosphoSite; P99024; -.
DR   SWISS-2DPAGE; P99024; -.
DR   REPRODUCTION-2DPAGE; IPI00117352; -.
DR   REPRODUCTION-2DPAGE; P99024; -.
DR   PRIDE; P99024; -.
DR   Ensembl; ENSMUST00000001566; ENSMUSP00000001566; ENSMUSG00000001525.
DR   GeneID; 22154; -.
DR   KEGG; mmu:22154; -.
DR   UCSC; uc008ciq.1; mouse.
DR   CTD; 22154; -.
DR   MGI; MGI:107812; Tubb5.
DR   eggNOG; roNOG14625; -.
DR   HOVERGEN; HBG000089; -.
DR   InParanoid; P99024; -.
DR   OMA; DQLARIN; -.
DR   OrthoDB; EOG4DFPNJ; -.
DR   PhylomeDB; P99024; -.
DR   Reactome; REACT_17056; Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding.
DR   NextBio; 302074; -.
DR   ArrayExpress; P99024; -.
DR   Bgee; P99024; -.
DR   CleanEx; MM_TUBB5; -.
DR   Genevestigator; P99024; -.
DR   GermOnline; ENSMUSG00000001525; Mus musculus.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005874; C:microtubule; IDA:MGI.
DR   GO; GO:0045298; C:tubulin complex; NAS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; NAS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:MGI.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; TAS:Reactome.
DR   GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR   GO; GO:0051225; P:spindle assembly; IDA:MGI.
DR   InterPro; IPR013838; Beta-tubulin_BS.
DR   InterPro; IPR002453; Beta_tubulin.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR023123; Tubulin_C.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   Gene3D; G3DSA:3.30.1330.20; Tubulin/FtsZ_2-layer-sand-dom; 1.
DR   Gene3D; G3DSA:1.10.287.600; Tubulin_C; 1.
DR   Gene3D; G3DSA:3.40.50.1440; Tubulin_FtsZ; 1.
DR   PANTHER; PTHR11588; Tubulin; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01163; BETATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF55307; Tub_FtsZ_C; 1.
DR   SUPFAM; SSF52490; Tubulin_FtsZ; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
DR   PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   GTP-binding; Isopeptide bond; Methylation; Microtubule;
KW   Nucleotide-binding; Phosphoprotein; Ubl conjugation.
FT   CHAIN         1    444       Tubulin beta-5 chain.
FT                                /FTId=PRO_0000048246.
FT   NP_BIND     140    146       GTP (Potential).
FT   MOD_RES      48     48       Phosphoserine (By similarity).
FT   MOD_RES      55     55       Phosphothreonine (By similarity).
FT   MOD_RES      58     58       N6-acetyllysine (By similarity).
FT   MOD_RES     318    318       Omega-N-methylarginine (By similarity).
FT   MOD_RES     340    340       Phosphotyrosine.
FT   MOD_RES     382    382       Phosphoserine.
FT   MOD_RES     429    429       Phosphothreonine (By similarity).
FT   CROSSLNK     58     58       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK    324    324       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CONFLICT     15     15       Q -> P (in Ref. 2; BAB27292).
FT   CONFLICT    114    114       D -> N (in Ref. 2; BAE40217).
FT   CONFLICT    143    143       T -> N (in Ref. 2; BAE28709).
FT   CONFLICT    264    264       H -> D (in Ref. 2; BAE40217).
FT   CONFLICT    307    307       H -> N (in Ref. 2; BAE39835).
FT   CONFLICT    357    357       P -> T (in Ref. 2; BAE40217).
FT   CONFLICT    400    400       G -> A (in Ref. 6; AAA40510).
SQ   SEQUENCE   444 AA;  49671 MW;  1E6CD0A36773A103 CRC64;
     MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLDRISVY YNEATGGKYV
     PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
     RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVV PSPKVSDTVV
     EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL
     RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQVFDAKNMM
     AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG
     LKMAVTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDATA EEEEDFGEEA EEEA
//
ID   RLA2_MOUSE              Reviewed;         115 AA.
AC   P99027; Q3TKY3; Q9CQ99; Q9CZJ8;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 3.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=60S acidic ribosomal protein P2;
GN   Name=Rplp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Head, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-10.
RC   TISSUE=Liver;
RA   Sanchez J.-C., Rouge V., Frutiger S., Hughes G., Yan J.X.,
RA   Hoogland C., Appel R.D., Binz P.-A., Hochstrasser D.F., Cowthorne M.;
RL   Submitted (AUG-1998) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-105, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-105, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-105, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-105, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-105, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-105, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-105, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-102 AND SER-105,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Plays an important role in the elongation step of
CC       protein synthesis.
CC   -!- SUBUNIT: P1 and P2 exist as dimers at the large ribosomal subunit.
CC   -!- SIMILARITY: Belongs to the ribosomal protein L12P family.
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DR   EMBL; AK002419; BAB22086.1; -; mRNA.
DR   EMBL; AK008344; BAB25616.1; -; mRNA.
DR   EMBL; AK010618; BAB27066.1; -; mRNA.
DR   EMBL; AK012402; BAB28217.1; -; mRNA.
DR   EMBL; AK012526; BAB28297.1; -; mRNA.
DR   EMBL; AK028140; BAC25768.1; -; mRNA.
DR   EMBL; AK028149; BAC25777.1; -; mRNA.
DR   EMBL; AK088737; BAC40539.1; -; mRNA.
DR   EMBL; AK134206; BAE22051.1; -; mRNA.
DR   EMBL; AK166774; BAE39010.1; -; mRNA.
DR   EMBL; BC012413; AAH12413.1; -; mRNA.
DR   IPI; IPI00139795; -.
DR   RefSeq; NP_080296.3; NM_026020.6.
DR   UniGene; Mm.380435; -.
DR   ProteinModelPortal; P99027; -.
DR   SMR; P99027; 1-59.
DR   STRING; P99027; -.
DR   PhosphoSite; P99027; -.
DR   SWISS-2DPAGE; P99027; -.
DR   REPRODUCTION-2DPAGE; IPI00139795; -.
DR   PRIDE; P99027; -.
DR   Ensembl; ENSMUST00000084434; ENSMUSP00000081474; ENSMUSG00000025508.
DR   Ensembl; ENSMUST00000106003; ENSMUSP00000101625; ENSMUSG00000025508.
DR   Ensembl; ENSMUST00000106004; ENSMUSP00000101626; ENSMUSG00000025508.
DR   GeneID; 67186; -.
DR   KEGG; mmu:67186; -.
DR   UCSC; uc009klf.1; mouse.
DR   CTD; 67186; -.
DR   MGI; MGI:1914436; Rplp2.
DR   eggNOG; roNOG17703; -.
DR   GeneTree; ENSGT00550000074828; -.
DR   HOGENOM; HBG744999; -.
DR   HOVERGEN; HBG014761; -.
DR   InParanoid; P99027; -.
DR   OMA; MKLIAAY; -.
DR   OrthoDB; EOG4F4SCS; -.
DR   PhylomeDB; P99027; -.
DR   NextBio; 323828; -.
DR   ArrayExpress; P99027; -.
DR   Bgee; P99027; -.
DR   CleanEx; MM_RPLP2; -.
DR   Genevestigator; P99027; -.
DR   GermOnline; ENSMUSG00000073013; Mus musculus.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006414; P:translational elongation; IEA:InterPro.
DR   InterPro; IPR001813; Ribosomal_60S.
DR   Pfam; PF00428; Ribosomal_60s; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Phosphoprotein;
KW   Ribonucleoprotein; Ribosomal protein.
FT   CHAIN         1    115       60S acidic ribosomal protein P2.
FT                                /FTId=PRO_0000157641.
FT   MOD_RES      16     16       Phosphoserine (By similarity).
FT   MOD_RES      17     17       Phosphoserine.
FT   MOD_RES      21     21       N6-acetyllysine (By similarity).
FT   MOD_RES      49     49       N6-acetyllysine (By similarity).
FT   MOD_RES      79     79       Phosphoserine (By similarity).
FT   MOD_RES      86     86       Phosphoserine (By similarity).
FT   MOD_RES     102    102       Phosphoserine.
FT   MOD_RES     105    105       Phosphoserine.
FT   CONFLICT     19     19       S -> N (in Ref. 1; BAB28297).
FT   CONFLICT     61     61       K -> R (in Ref. 1; BAB28297).
FT   CONFLICT     81     81       A -> T (in Ref. 1; BAB28297).
SQ   SEQUENCE   115 AA;  11651 MW;  AAF3FE3A0FA756BF CRC64;
     MRYVASYLLA ALGGNSSPSA KDIKKILDSV GIEADDDRLN KVISELNGKN IEDVIAQGVG
     KLASVPAGGA VAVSAAPGSA APAAGSAPAA AEEKKDEKKE ESEESDDDMG FGLFD
//
ID   QCR6_MOUSE              Reviewed;          89 AA.
AC   P99028; Q542K2; Q9CQP4;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 2.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Cytochrome b-c1 complex subunit 6, mitochondrial;
DE   AltName: Full=Complex III subunit 6;
DE   AltName: Full=Complex III subunit VIII;
DE   AltName: Full=Cytochrome c1 non-heme 11 kDa protein;
DE   AltName: Full=Mitochondrial hinge protein;
DE   AltName: Full=Ubiquinol-cytochrome c reductase complex 11 kDa protein;
DE   Flags: Precursor;
GN   Name=Uqcrh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Kidney, Oviduct, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 14-25.
RC   TISSUE=Liver;
RA   Sanchez J.-C., Rouge V., Frutiger S., Hughes G., Yan J.X.,
RA   Hoogland C., Appel R.D., Binz P.-A., Hochstrasser D.F., Cowthorne M.;
RL   Submitted (AUG-1998) to UniProtKB.
RN   [4]
RP   PROTEIN SEQUENCE OF 18-32; 45-54 AND 59-76, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-40, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-61, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: This is a component of the ubiquinol-cytochrome c
CC       reductase complex (complex III or cytochrome b-c1 complex), which
CC       is part of the mitochondrial respiratory chain. This protein may
CC       mediate formation of the complex between cytochromes c and c1 (By
CC       similarity).
CC   -!- SUBUNIT: The bc1 complex contains 11 subunits: 3 respiratory
CC       subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core
CC       proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight
CC       proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9,
CC       UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1) (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
CC   -!- SIMILARITY: Belongs to the UQCRH/QCR6 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK003266; BAB22681.1; -; mRNA.
DR   EMBL; AK003539; BAB22845.1; -; mRNA.
DR   EMBL; AK012552; BAB28312.1; -; mRNA.
DR   EMBL; AK018712; BAB31360.1; -; mRNA.
DR   EMBL; AK054005; BAC35617.1; -; mRNA.
DR   EMBL; AK088185; BAC40195.1; -; mRNA.
DR   EMBL; BC011388; AAH11388.1; -; mRNA.
DR   IPI; IPI00129516; -.
DR   RefSeq; NP_079917.1; NM_025641.3.
DR   UniGene; Mm.181721; -.
DR   ProteinModelPortal; P99028; -.
DR   SMR; P99028; 24-89.
DR   STRING; P99028; -.
DR   PhosphoSite; P99028; -.
DR   SWISS-2DPAGE; P99028; -.
DR   PRIDE; P99028; -.
DR   Ensembl; ENSMUST00000078676; ENSMUSP00000077744; ENSMUSG00000063882.
DR   GeneID; 66576; -.
DR   KEGG; mmu:66576; -.
DR   NMPDR; fig|10090.3.peg.10149; -.
DR   UCSC; uc008ufv.1; mouse.
DR   CTD; 66576; -.
DR   MGI; MGI:1913826; Uqcrh.
DR   HOGENOM; HBG714621; -.
DR   HOVERGEN; HBG001487; -.
DR   InParanoid; P99028; -.
DR   OMA; HKLFNSL; -.
DR   OrthoDB; EOG405S2P; -.
DR   NextBio; 322050; -.
DR   ArrayExpress; P99028; -.
DR   Bgee; P99028; -.
DR   CleanEx; MM_UQCRH; -.
DR   Genevestigator; P99028; -.
DR   GermOnline; ENSMUSG00000063882; Mus musculus.
DR   GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:InterPro.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:InterPro.
DR   InterPro; IPR003422; Ubol_cytC_Rdtase_hinge.
DR   InterPro; IPR023184; Ubol_cytC_Rdtase_hinge_dom.
DR   Gene3D; G3DSA:1.10.287.20; Ubol_cytC_Rdtase_hinge_dom; 1.
DR   PANTHER; PTHR15336; UCR_hinge; 1.
DR   Pfam; PF02320; UCR_hinge; 1.
DR   SUPFAM; SSF81531; Ubol_cytC_Rdtase_hinge_dom; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Disulfide bond;
KW   Electron transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Phosphoprotein; Respiratory chain;
KW   Transit peptide; Transport.
FT   TRANSIT       1     13       Mitochondrion.
FT   CHAIN        14     89       Cytochrome b-c1 complex subunit 6,
FT                                mitochondrial.
FT                                /FTId=PRO_0000035992.
FT   COMPBIAS     18     23       Poly-Glu.
FT   MOD_RES      40     40       N6-acetyllysine.
FT   MOD_RES      59     59       Phosphoserine (By similarity).
FT   MOD_RES      61     61       Phosphothreonine.
FT   MOD_RES      83     83       N6-acetyllysine (By similarity).
FT   DISULFID     35     79       By similarity.
FT   DISULFID     51     65       By similarity.
SQ   SEQUENCE   89 AA;  10435 MW;  6E588E3BDF743E7B CRC64;
     MGLEDERKML TGSGDPKEEE EEELVDPLTT VREHCEQLEK CVKARERLEL CDNRVSSRSQ
     TEEDCTEELF DFLHARDHCV AHKLFKNLK
//
ID   PRDX5_MOUSE             Reviewed;         210 AA.
AC   P99029; Q9QX45; Q9QZ75;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2002, sequence version 2.
DT   08-MAR-2011, entry version 105.
DE   RecName: Full=Peroxiredoxin-5, mitochondrial;
DE            EC=1.11.1.15;
DE   AltName: Full=Antioxidant enzyme B166;
DE            Short=AOEB166;
DE   AltName: Full=Liver tissue 2D-page spot 2D-0014IV;
DE   AltName: Full=PLP;
DE   AltName: Full=Peroxiredoxin V;
DE            Short=Prx-V;
DE   AltName: Full=Peroxisomal antioxidant enzyme;
DE   AltName: Full=Thioredoxin peroxidase PMP20;
DE   AltName: Full=Thioredoxin reductase;
DE   Flags: Precursor;
GN   Name=Prdx5; Synonyms=Prdx6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX   MEDLINE=20145535; PubMed=10679306; DOI=10.1006/bbrc.2000.2231;
RA   Zhou Y., Kok K.H., Chun A.C.S., Wong C.M., Wu H.W., Lin M.C.M.,
RA   Fung P.C.W., Kung H.-F., Jin D.-Y.;
RT   "Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-
RT   induced apoptosis.";
RL   Biochem. Biophys. Res. Commun. 268:921-927(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX   MEDLINE=99445545; PubMed=10514471; DOI=10.1074/jbc.274.42.29897;
RA   Yamashita H., Avraham S., Jiang S., London R., Van Veldhoven P.P.,
RA   Subramani S., Rogers R.A., Avraham H.;
RT   "Characterization of human and murine PMP20 peroxisomal proteins that
RT   exhibit antioxidant activity in vitro.";
RL   J. Biol. Chem. 274:29897-29904(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE, AND CHARACTERIZATION.
RC   STRAIN=C3H/HeJ; TISSUE=Lung;
RX   MEDLINE=99452929; PubMed=10521424; DOI=10.1074/jbc.274.43.30451;
RA   Knoops B., Clippe A., Bogard C., Arsalane K., Wattiez R., Hermans C.,
RA   Duconseille E., Falmagne P., Bernard A.;
RT   "Cloning and characterization of AOEB166, a novel mammalian
RT   antioxidant enzyme of the peroxiredoxin family.";
RL   J. Biol. Chem. 274:30451-30458(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=20218665; PubMed=10753630; DOI=10.1006/bbrc.2000.2430;
RA   Lee T.H., Kim S.J., Kang S.W., Lee K.K., Rhee S.G., Yu D.Y.;
RT   "Molecular cloning and characterization of the mouse Peroxiredoxin V
RT   gene.";
RL   Biochem. Biophys. Res. Commun. 270:356-362(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 50-61.
RC   TISSUE=Liver;
RA   Sanchez J.-C., Rouge V., Frutiger S., Hughes G.J., Yan J.X.,
RA   Hoogland C., Appel R.D., Binz P.-A., Hochstrasser D.F., Cowthorne M.;
RL   Submitted (AUG-1998) to UniProtKB.
RN   [8]
RP   PROTEIN SEQUENCE OF 72-79; 83-112 AND 145-172, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Reduces hydrogen peroxide and alkyl hydroperoxides with
CC       reducing equivalents provided through the thioredoxin system.
CC       Involved in intracellular redox signaling.
CC   -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Cytoplasm. Peroxisome.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Mitochondrial;
CC         IsoId=P99029-1; Sequence=Displayed;
CC       Name=Cytoplasmic+peroxisomal;
CC         IsoId=P99029-2; Sequence=VSP_018830;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- SIMILARITY: Belongs to the peroxiredoxin 2 family.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
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DR   EMBL; AF197951; AAF04855.1; -; mRNA.
DR   EMBL; AF124994; AAF27532.1; -; mRNA.
DR   EMBL; AF110733; AAG13450.1; -; mRNA.
DR   EMBL; AF208730; AAF21016.1; -; Genomic_DNA.
DR   EMBL; AF208729; AAF21016.1; JOINED; Genomic_DNA.
DR   EMBL; AK002383; BAB22058.1; -; mRNA.
DR   EMBL; AK003332; BAB22720.1; -; mRNA.
DR   EMBL; BC008174; AAH08174.1; -; mRNA.
DR   IPI; IPI00129517; -.
DR   IPI; IPI00759999; -.
DR   PIR; JC7239; JC7239.
DR   RefSeq; NP_036151.1; NM_012021.2.
DR   UniGene; Mm.279782; -.
DR   ProteinModelPortal; P99029; -.
DR   SMR; P99029; 50-210.
DR   STRING; P99029; -.
DR   PeroxiBase; 4453; MmPrxV.
DR   PhosphoSite; P99029; -.
DR   SWISS-2DPAGE; P99029; -.
DR   REPRODUCTION-2DPAGE; P99029; -.
DR   PRIDE; P99029; -.
DR   Ensembl; ENSMUST00000025904; ENSMUSP00000025904; ENSMUSG00000024953.
DR   GeneID; 54683; -.
DR   KEGG; mmu:54683; -.
DR   UCSC; uc008gjc.1; mouse.
DR   CTD; 54683; -.
DR   MGI; MGI:1859821; Prdx5.
DR   eggNOG; roNOG17057; -.
DR   HOGENOM; HBG493509; -.
DR   HOVERGEN; HBG053675; -.
DR   InParanoid; P99029; -.
DR   OMA; RFSMVIE; -.
DR   OrthoDB; EOG4PZJ7W; -.
DR   PhylomeDB; P99029; -.
DR   BRENDA; 1.11.1.15; 244.
DR   NextBio; 311536; -.
DR   ArrayExpress; P99029; -.
DR   Bgee; P99029; -.
DR   CleanEx; MM_PRDX5; -.
DR   CleanEx; MM_PRDX6; -.
DR   Genevestigator; P99029; -.
DR   GermOnline; ENSMUSG00000024953; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR017936; Thioredoxin-like.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative initiation; Antioxidant; Cytoplasm;
KW   Direct protein sequencing; Disulfide bond; Mitochondrion;
KW   Oxidoreductase; Peroxidase; Peroxisome; Redox-active center;
KW   Transit peptide.
FT   TRANSIT       1     48       Mitochondrion (Potential).
FT   CHAIN        49    210       Peroxiredoxin-5, mitochondrial.
FT                                /FTId=PRO_0000023795.
FT   DOMAIN       52    210       Thioredoxin.
FT   MOTIF       208    210       Microbody targeting signal (By
FT                                similarity).
FT   ACT_SITE     96     96       Cysteine sulfenic acid (-SOH)
FT                                intermediate (Potential).
FT   MOD_RES      79     79       N6-acetyllysine (By similarity).
FT   DISULFID     96    200       Redox-active (By similarity).
FT   VAR_SEQ       1     48       Missing (in isoform
FT                                Cytoplasmic+peroxisomal).
FT                                /FTId=VSP_018830.
FT   CONFLICT     55     55       G -> D (in Ref. 7; AA sequence).
FT   CONFLICT     83    102       GVLFGVPGAFTPGCSKTHLP -> VFCLESLGHLHLAVLRP
FT                                TA (in Ref. 4; AAF21016).
SQ   SEQUENCE   210 AA;  21897 MW;  E944104CC468BDD8 CRC64;
     MLQLGLRVLG CKASSVLRAS TCLAGRAGRK EAGWECGGAR SFSSSAVTMA PIKVGDAIPS
     VEVFEGEPGK KVNLAELFKG KKGVLFGVPG AFTPGCSKTH LPGFVEQAGA LKAKGAQVVA
     CLSVNDVFVI EEWGRAHQAE GKVRLLADPT GAFGKATDLL LDDSLVSLFG NRRLKRFSMV
     IDNGIVKALN VEPDGTGLTC SLAPNILSQL
//
ID   ITA4_MOUSE              Reviewed;        1039 AA.
AC   Q00651;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   30-NOV-2010, entry version 101.
DE   RecName: Full=Integrin alpha-4;
DE   AltName: Full=CD49 antigen-like family member D;
DE   AltName: Full=Integrin alpha-IV;
DE   AltName: Full=Lymphocyte Peyer patch adhesion molecules subunit alpha;
DE            Short=LPAM subunit alpha;
DE   AltName: Full=VLA-4 subunit alpha;
DE   AltName: CD_antigen=CD49d;
DE   Flags: Precursor;
GN   Name=Itga4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92064645; PubMed=1840602; DOI=10.1083/jcb.115.4.1149;
RA   Neuhaus H., Hu M.C.-T., Hemler M.E., Takada Y., Holzmann B.,
RA   Weissman I.L.;
RT   "Cloning and expression of cDNAs for the alpha subunit of the murine
RT   lymphocyte-Peyer's patch adhesion molecule.";
RL   J. Cell Biol. 115:1149-1158(1991).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1028, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1028, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1028, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Integrins alpha-4/beta-1 (VLA-4 or LPAM-2) and alpha-
CC       4/beta-7 (LPAM-1) are receptors for fibronectin. They recognize
CC       one or more domains within the alternatively spliced CS-1 and CS-5
CC       regions of fibronectin. They are also receptors for VCAM1.
CC       Integrin alpha-4/beta-1 recognizes the sequence Q-I-D-S in VCAM1.
CC       Integrin alpha-4/beta-7 is also a receptor for MADCAM1. It
CC       recognizes the sequence L-D-T in MADCAM1. On activated endothelial
CC       cells integrin VLA-4 triggers homotypic aggregation for most VLA-
CC       4-positive leukocyte cell lines. It may also participate in
CC       cytolytic T-cell interactions with target cells. Integrin alpha-
CC       4/beta-7 is also a receptor for MADCAM1. Mice homozygous for a
CC       null mutation of the alpha-4 subunit gene die by day E11-E14 from
CC       detachment and rupture of the epicardium and coronary arteries.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha
CC       subunit can sometimes be cleaved into two non-covalently
CC       associated fragments. Alpha-4 associates with either beta-1 or
CC       beta-7. Alpha-4 interacts with PXN, LPXN, and TGFB1I1/HIC5.
CC       Interacts with CSPG4 through CSPG4 chondroitin sulfate
CC       glycosaminoglycan (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Peyer patch homing cells.
CC   -!- DOMAIN: The SG1 motif is involved in binding to chondroitin
CC       sulfate glycosaminoglycan and cell adhesion (By similarity).
CC   -!- PTM: Phosphorylation on Ser-1028 inhibits PXN binding (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the integrin alpha chain family.
CC   -!- SIMILARITY: Contains 7 FG-GAP repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X53176; CAA37316.1; -; mRNA.
DR   IPI; IPI00121334; -.
DR   PIR; A41131; A41131.
DR   RefSeq; NP_034706.3; NM_010576.3.
DR   UniGene; Mm.31903; -.
DR   ProteinModelPortal; Q00651; -.
DR   SMR; Q00651; 205-472, 979-1017.
DR   STRING; Q00651; -.
DR   PhosphoSite; Q00651; -.
DR   PRIDE; Q00651; -.
DR   Ensembl; ENSMUST00000028395; ENSMUSP00000028395; ENSMUSG00000027009.
DR   GeneID; 16401; -.
DR   KEGG; mmu:16401; -.
DR   CTD; 16401; -.
DR   MGI; MGI:96603; Itga4.
DR   eggNOG; roNOG14785; -.
DR   HOGENOM; HBG447158; -.
DR   HOVERGEN; HBG004538; -.
DR   InParanoid; Q00651; -.
DR   ArrayExpress; Q00651; -.
DR   Bgee; Q00651; -.
DR   CleanEx; MM_ITGA4; -.
DR   Genevestigator; Q00651; -.
DR   GermOnline; ENSMUSG00000027009; Mus musculus.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR   GO; GO:0001968; F:fibronectin binding; IMP:MGI.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
DR   GO; GO:0016477; P:cell migration; IMP:MGI.
DR   GO; GO:0060710; P:chorio-allantoic fusion; IMP:MGI.
DR   GO; GO:0060324; P:face development; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion; IMP:MGI.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:MGI.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR013519; Int_alpha_beta-p.
DR   InterPro; IPR000413; Integrin_alpha.
DR   InterPro; IPR013649; Integrin_alpha-2.
DR   InterPro; IPR018184; Integrin_alpha_C_CS.
DR   Pfam; PF01839; FG-GAP; 2.
DR   Pfam; PF08441; Integrin_alpha2; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   SMART; SM00191; Int_alpha; 6.
DR   PROSITE; PS51470; FG_GAP; 7.
DR   PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell adhesion; Disulfide bond; Glycoprotein; Integrin;
KW   Membrane; Phosphoprotein; Receptor; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     40       Potential.
FT   CHAIN        41   1039       Integrin alpha-4.
FT                                /FTId=PRO_0000016245.
FT   TOPO_DOM     41    983       Extracellular (Potential).
FT   TRANSMEM    984   1007       Helical; (Potential).
FT   TOPO_DOM   1008   1039       Cytoplasmic (Potential).
FT   REPEAT       42    107       FG-GAP 1.
FT   REPEAT      117    184       FG-GAP 2.
FT   REPEAT      193    244       FG-GAP 3.
FT   REPEAT      245    300       FG-GAP 4.
FT   REPEAT      301    358       FG-GAP 5.
FT   REPEAT      362    419       FG-GAP 6.
FT   REPEAT      423    485       FG-GAP 7.
FT   CA_BIND     321    329       Potential.
FT   CA_BIND     384    392       Potential.
FT   CA_BIND     446    454       Potential.
FT   MOTIF       613    623       SG1.
FT   MOTIF      1010   1014       GFFKR motif.
FT   SITE        598    599       Cleavage.
FT   MOD_RES    1028   1028       Phosphoserine.
FT   CARBOHYD     86     86       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    105    105       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    145    145       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    236    236       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    487    487       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    525    525       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    545    545       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    633    633       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    652    652       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    667    667       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    813    813       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    828    828       N-linked (GlcNAc...) (Potential).
FT   DISULFID     98    108       By similarity.
FT   DISULFID    151    172       By similarity.
FT   DISULFID    190    205       By similarity.
FT   DISULFID    493    502       By similarity.
FT   DISULFID    508    564       By similarity.
FT   DISULFID    629    634       By similarity.
FT   DISULFID    705    718       By similarity.
FT   DISULFID    859    897       By similarity.
FT   DISULFID    904    909       By similarity.
SQ   SEQUENCE   1039 AA;  115696 MW;  C8C0BC611F7E9847 CRC64;
     MFSTKSAWLR NGGADQGPRG IALREAVMLL LYFGVPTGPS YNLDPENALL YQGPSGTLFG
     YSVVLHSHGS KRWLIVGAPT ASWLSNASVV NPGAIYRCGI RKNPNQTCEQ LQSGSPSGEP
     CGKTCLEERD NQWLGVTLSR QPGENGSIVT CGHRWKNIFY MKSDNKLPTG ICYVMPSDLR
     TELSKRMAPC YKDYTRKFGE NFASCQAGIS SFYTQDLIVM GAPGSSYWTG TVFVYNITTN
     QYKAFVDRQN QVKFGSYLGY SVGAGHFRSP HTTEVVGGAP QHEQIGKAYI FSIDENELNI
     VYEMKGKKLG SYFGASVCAV DLNADGFSDL LVGAPMQSTI REEGRVFVYI NSGMGAVMVE
     MERVLVGSDK YAARFGESIA NLGDIDNDGF EDIAIGAPQE DDLRGAVYIY NGRVDGISST
     YSQRIEGQQI SKSLRMFGQS ISGQIDADNN GYVDVAVGAF QSDSAVLLRT RPVVIVEASL
     SHPESVNRTK FDCTENGLPS VCMHLTLCFS YKGKEVPGYI VLFYNVSLDV HRKAESPSRF
     YFFSNGTSDV ITGSIRVSSS GEKCRTHQAF MRKDVRDILT PIHVEATYHL GHHVITKRNT
     EEFPPLQPIL QQKKEKDVIR KMINFARFCA YENCSADLQV SAKVGFLKPY ENKTYLAVGS
     MKTIMLNVSL FNAGDDAYET TLNVQLPTGL YFIKILDLEE KQINCEVTES SGIVKLACSL
     GYIYVDRLSR IDISFLLDVS SLSRAHEDLS ISVHASCENE GELDQVRDNR VTLTIPLRYE
     VMLTVHGLVN PTSFVYGSSE ENEPETCMAE KLNLTFHVIN TGISMAPNVS VKIMVPNSFL
     PQDDKLFNVL DVQTTTGQCH FKHYGRECTF AQQKGIAGTL TDIVKFLSKT DKRLLYCMKA
     DQHCLDFLCN FGKMESGKEA SVHIQLEGRP SILEMDETSS LKFEIKATAF PEPHPKVIEL
     NKDENVAHVF LEGLHHQRPK RHFTIIIITI SLLLGLIVLL LISCVMWKAG FFKRQYKSIL
     QEENRRDSWS YVNSKSNDD
//
ID   TYY1_MOUSE              Reviewed;         414 AA.
AC   Q00899;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   08-MAR-2011, entry version 100.
DE   RecName: Full=Transcriptional repressor protein YY1;
DE   AltName: Full=Delta transcription factor;
DE   AltName: Full=NF-E1;
DE   AltName: Full=UCR-motif DNA-binding protein;
DE   AltName: Full=Yin and yang 1;
DE            Short=YY-1;
GN   Name=Yy1; Synonyms=Ucrbp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92107191; PubMed=1309593;
RA   Flanagan J.R., Becker K.G., Ennist D.L., Gleason S.L., Driggers P.H.,
RA   Levi B.-Z., Appella E., Ozato K.;
RT   "Cloning of a negative transcription factor that binds to the upstream
RT   conserved region of Moloney murine leukemia virus.";
RL   Mol. Cell. Biol. 12:38-44(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   MEDLINE=93296177; PubMed=8516301; DOI=10.1073/pnas.90.12.5559;
RA   Safrany G., Perry R.P.;
RT   "Characterization of the mouse gene that encodes the delta/YY1/NF-
RT   E1/UCRBP transcription factor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:5559-5563(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92052178; PubMed=1946404; DOI=10.1073/pnas.88.21.9799;
RA   Hariharan N., Kelley D.E., Perry R.P.;
RT   "Delta, a transcription factor that binds to downstream elements in
RT   several polymerase II promoters, is a functionally versatile zinc
RT   finger protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:9799-9803(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Multifunctional transcription factor that exhibits
CC       positive and negative control on a large number of cellular and
CC       viral genes by binding to sites overlapping the transcription
CC       start site. May play an important role in development and
CC       differentiation. The function of YY1 as an activator or a
CC       repressor is specified by the presence of other proteins. Binds to
CC       the upstream conserved region (UCR) (5'-CGCCATTTT-3') of Moloney
CC       murine leukemia virus (MuLV).
CC   -!- SUBUNIT: Interacts with YAF2 through the region encompassing the
CC       first and second zinc fingers. Interacts with INO80 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus matrix. Note=Associated with the
CC       nuclear matrix.
CC   -!- SIMILARITY: Belongs to the YY transcription factor family.
CC   -!- SIMILARITY: Contains 4 C2H2-type zinc fingers.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; M73963; AAA40522.1; -; mRNA.
DR   EMBL; L13968; AAA40477.1; -; Genomic_DNA.
DR   EMBL; L13969; AAA40477.1; JOINED; Genomic_DNA.
DR   EMBL; L13965; AAA40477.1; JOINED; Genomic_DNA.
DR   EMBL; L13966; AAA40477.1; JOINED; Genomic_DNA.
DR   EMBL; L13967; AAA40477.1; JOINED; Genomic_DNA.
DR   EMBL; M74590; AAA37521.1; -; mRNA.
DR   EMBL; BC055899; AAH55899.1; -; mRNA.
DR   IPI; IPI00311892; -.
DR   PIR; A48273; A48273.
DR   RefSeq; NP_033563.2; NM_009537.3.
DR   UniGene; Mm.3868; -.
DR   UniGene; Mm.458511; -.
DR   ProteinModelPortal; Q00899; -.
DR   SMR; Q00899; 295-408.
DR   STRING; Q00899; -.
DR   PhosphoSite; Q00899; -.
DR   PRIDE; Q00899; -.
DR   Ensembl; ENSMUST00000021692; ENSMUSP00000021692; ENSMUSG00000021264.
DR   GeneID; 22632; -.
DR   KEGG; mmu:22632; -.
DR   UCSC; uc007pac.1; mouse.
DR   CTD; 22632; -.
DR   MGI; MGI:99150; Yy1.
DR   eggNOG; roNOG10052; -.
DR   HOGENOM; HBG713851; -.
DR   HOVERGEN; HBG006823; -.
DR   InParanoid; Q00899; -.
DR   OMA; PLVTDDP; -.
DR   OrthoDB; EOG4D26QN; -.
DR   NextBio; 303007; -.
DR   ArrayExpress; Q00899; -.
DR   Bgee; Q00899; -.
DR   CleanEx; MM_YY1; -.
DR   Genevestigator; Q00899; -.
DR   GermOnline; ENSMUSG00000021264; Mus musculus.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0031519; C:PcG protein complex; IDA:MGI.
DR   GO; GO:0005667; C:transcription factor complex; IDA:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0016566; F:specific transcriptional repressor activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009952; P:anterior/posterior pattern formation; IGI:MGI.
DR   GO; GO:0048593; P:camera-type eye morphogenesis; IGI:MGI.
DR   GO; GO:0010553; P:negative regulation of gene-specific transcription from RNA polymerase II promoter; IDA:MGI.
DR   InterPro; IPR017114; TF_Yin_yang.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 4.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   PIRSF; PIRSF037113; TF_Yin_yang; 1.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Repeat; Repressor; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    414       Transcriptional repressor protein YY1.
FT                                /FTId=PRO_0000047191.
FT   ZN_FING     296    320       C2H2-type 1.
FT   ZN_FING     325    347       C2H2-type 2.
FT   ZN_FING     353    377       C2H2-type 3.
FT   ZN_FING     383    407       C2H2-type 4.
FT   REGION      257    341       Involved in nuclear matrix association
FT                                (By similarity).
FT   REGION      333    371       Involved in repression of activated
FT                                transcription (By similarity).
FT   REGION      371    397       Involved in masking transactivation
FT                                domain (By similarity).
FT   COMPBIAS     43     53       Asp/Glu-rich (acidic).
FT   COMPBIAS     54     70       Gly-rich.
FT   COMPBIAS     71     82       Poly-His.
FT   COMPBIAS    161    170       Gly/Ser-rich.
FT   MOD_RES     120    120       Phosphoserine (By similarity).
FT   MOD_RES     184    184       Phosphoserine (By similarity).
FT   MOD_RES     247    247       Phosphoserine.
FT   MOD_RES     348    348       Phosphothreonine (By similarity).
FT   MOD_RES     378    378       Phosphothreonine (By similarity).
FT   CONFLICT    219    219       F -> S (in Ref. 3; AAA37521).
FT   CONFLICT    375    375       R -> G (in Ref. 3; AAA37521).
SQ   SEQUENCE   414 AA;  44717 MW;  C012378288E984F9 CRC64;
     MASGDTLYIA TDGSEMPAEI VELHEIEVET IPVETIETTV VGEEEEEDDD DEDGGGGDHG
     GGGGGHGHAG HHHHHHHHHH HHPPMIALQP LVTDDPTQVH HHQEVILVQT REEVVGGDDS
     DGLRAEDGFE DQILIPVPAP AGGDDDYIEQ TLVTVAAAGK SGGGASSGGG RVKKGGGKKS
     GKKSYLGGGA GAAGGGGADP GNKKWEQKQV QIKTLEGEFS VTMWSSDEKK DIDHETVVEE
     QIIGENSPPD YSEYMTGKKL PPGGIPGIDL SDPKQLAEFA RMKPRKIKED DAPRTIACPH
     KGCTKMFRDN SAMRKHLHTH GPRVHVCAEC GKAFVESSKL KRHQLVHTGE KPFQCTFEGC
     GKRFSLDFNL RTHVRIHTGD RPYVCPFDGC NKKFAQSTNL KSHILTHAKA KNNQ
//
ID   HNRL2_MOUSE             Reviewed;         745 AA.
AC   Q00PI9;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   RecName: Full=Heterogeneous nuclear ribonucleoprotein U-like protein 2;
DE   AltName: Full=MLF1-associated nuclear protein;
GN   Name=Hnrnpul2; Synonyms=Hnrpul2, Manp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH MLF1, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=129;
RX   PubMed=17008314; DOI=10.1074/jbc.M605401200;
RA   Winteringham L.N., Endersby R., Kobelke S., McCulloch R.K.,
RA   Williams J.H., Stillitano J., Cornwall S.M., Ingley E., Klinken S.P.;
RT   "Myeloid leukemia factor 1 associates with a novel heterogeneous
RT   nuclear ribonucleoprotein U-like molecule.";
RL   J. Biol. Chem. 281:38791-38800(2006).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159 AND SER-186, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SUBUNIT: Binds to MLF1 and retains it in the nucleus.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Contains 1 B30.2/SPRY domain.
CC   -!- SIMILARITY: Contains 1 SAP domain.
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DR   EMBL; DQ000354; AAY44301.1; -; mRNA.
DR   IPI; IPI00222208; -.
DR   UniGene; Mm.345134; -.
DR   ProteinModelPortal; Q00PI9; -.
DR   SMR; Q00PI9; 1-37, 450-579.
DR   PhosphoSite; Q00PI9; -.
DR   PRIDE; Q00PI9; -.
DR   Ensembl; ENSMUST00000096753; ENSMUSP00000094515; ENSMUSG00000071659.
DR   UCSC; uc008gng.1; mouse.
DR   MGI; MGI:1915943; Hnrnpul2.
DR   GeneTree; ENSGT00390000020210; -.
DR   HOGENOM; HBG446506; -.
DR   HOVERGEN; HBG061101; -.
DR   InParanoid; Q00PI9; -.
DR   OrthoDB; EOG4N30NM; -.
DR   ArrayExpress; Q00PI9; -.
DR   Bgee; Q00PI9; -.
DR   Genevestigator; Q00PI9; -.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0001906; P:cell killing; IEA:InterPro.
DR   InterPro; IPR001870; B302/SPRY.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR003034; SAP_DNA-bd.
DR   InterPro; IPR018355; SPla/RYanodine_receptor_sg.
DR   InterPro; IPR003877; SPRY_rcpt.
DR   InterPro; IPR010488; Zeta_toxin_P-loop_hydrolase.
DR   Pfam; PF02037; SAP; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF06414; Zeta_toxin; 1.
DR   SMART; SM00513; SAP; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50800; SAP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Nucleus; Phosphoprotein.
FT   CHAIN         1    745       Heterogeneous nuclear ribonucleoprotein
FT                                U-like protein 2.
FT                                /FTId=PRO_0000278143.
FT   DOMAIN        3     37       SAP.
FT   DOMAIN      224    417       B30.2/SPRY.
FT   COMPBIAS     75    239       Glu-rich.
FT   COMPBIAS    666    744       Tyr-rich.
FT   MOD_RES     136    136       Phosphoserine (By similarity).
FT   MOD_RES     159    159       Phosphoserine.
FT   MOD_RES     163    163       Phosphothreonine (By similarity).
FT   MOD_RES     166    166       Phosphoserine (By similarity).
FT   MOD_RES     183    183       Phosphoserine (By similarity).
FT   MOD_RES     186    186       Phosphoserine.
FT   MOD_RES     224    224       Phosphoserine (By similarity).
FT   MOD_RES     226    226       Phosphoserine (By similarity).
FT   MOD_RES     469    469       N6-acetyllysine (By similarity).
SQ   SEQUENCE   745 AA;  85000 MW;  27F800A03BAA2CE7 CRC64;
     MEVKRLKVTE LRSELQRRGL DSRGLKMDLA QRLQEALDAE MLEDEAGVGG AGPGGACKAE
     PRPVAASGGG PGGDEEEEDD DEEEDEEALL EDEDEEPPPA QALGQAAQPP PEPPETSAME
     AESEASDTPA EATAGSGGVN GGEEHDNGKG EEDGPEERSG DETPGSEAPG DKAVEEQGDD
     QDSEKSKPAG SDGERRGVKR QRDEKDEHGR AYYEFREEAY HSRSKSPPPP EEEAKDEEED
     QTLVNLDTYT SDLHFQISKD RYGGQPLFSE KFPTLWFGAR STYGVTKGKV CFEAKVTQNL
     PMKEGCTEVS LLRVGWSVDF SCSQLGEDEF SYGFDGRGLK AENGQFEEFG QTFGENDVIG
     CFANFETEEV ELSFSKNGED LGVAFRISKE SLADRALLPH VLCKNCVVEL NFGQKEEPFF
     PPPEEFVFIH AVPVEERVRT AVPPKTIEEC EVILMVGLPG SGKTQWALKY AKDNPERRYN
     VLGAETVLTQ MRMKGLEEPE MDPKSRDLLV QQASQCLSKL VQIASRSKRN FILDQCNVYN
     SGQRRKLLLF KTFSRKVVVV VPNEEDWKRR LELRKEVEGD DVPESIMLEM KANFSLPEKC
     DYMDEVTYGE LEKEEAQPIV TKYKEEARKL LPPSEKRTNR RNNRNKRNRQ NRSRGQGYVG
     GQRRGYDNRA YGQQYWGQSG NRGGYRNFYD RYRGDYERFY SRDYEYNRYR DYYRQYNRDW
     QNYYYHHQQD RDRYYRNYYG YQGYR
//
ID   PDE4D_MOUSE             Reviewed;         747 AA.
AC   Q01063; B2KF58; Q6TRH9; Q8C4Q7; Q8CG05;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=cAMP-specific 3',5'-cyclic phosphodiesterase 4D;
DE            EC=3.1.4.17;
DE   AltName: Full=DPDE3;
GN   Name=Pde4d;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c;
RX   MEDLINE=22718903; PubMed=12834813; DOI=10.1016/S0898-6568(03)00042-1;
RA   Wang D., Deng C., Bugaj-Gaweda B., Kwan M., Gunwaldsen C., Leonard C.,
RA   Xin X., Hu Y., Unterbeck A., De Vivo M.;
RT   "Cloning and characterization of novel PDE4D isoforms PDE4D6 and
RT   PDE4D7.";
RL   Cell. Signal. 15:883-891(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Chai H., Gaweda B., De Vivo M., Wang D.;
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 400-514.
RX   MEDLINE=92406782; PubMed=1326532;
RA   Repaske D.R., Swinnen J.V., Jin S.-L.C., van Wyk J.J., Conti M.;
RT   "A polymerase chain reaction strategy to identify and clone cyclic
RT   nucleotide phosphodiesterase cDNAs. Molecular cloning of the cDNA
RT   encoding the 63-kDa calmodulin-dependent phosphodiesterase.";
RL   J. Biol. Chem. 267:18683-18688(1992).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Hydrolyzes the second messenger cAMP, which is a key
CC       regulator of many important physiological processes (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Adenosine 3',5'-cyclic phosphate + H(2)O =
CC       adenosine 5'-phosphate.
CC   -!- COFACTOR: Binds 2 divalent metal cations per subunit. Site 1 may
CC       preferentially bind zinc ions, while site 2 has a preference for
CC       magnesium and/or manganese ions (By similarity).
CC   -!- ENZYME REGULATION: Inhibited by rolipram. Activated by
CC       phosphatidic acid (By similarity).
CC   -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC       3',5'-cyclic AMP: step 1/1.
CC   -!- SUBUNIT: Homodimer for the long isoforms. Isoforms with truncated
CC       N-termini are monomeric. Binds ARRB2. Interacts with PDE4DIP (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane. Cytoplasm,
CC       cytoskeleton. Cytoplasm, cytoskeleton, centrosome. Note=Found in
CC       the soluble fraction, associated with membranes, and associated
CC       with the cytoskeleton and the centrosome.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=PDE4D7;
CC         IsoId=Q01063-1; Sequence=Displayed;
CC       Name=2; Synonyms=PDE4D9;
CC         IsoId=Q01063-2; Sequence=VSP_012395, VSP_012396;
CC       Name=3;
CC         IsoId=Q01063-3; Sequence=VSP_012394, VSP_012397;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is detected in heart, brain, lung,
CC       kidney and testis.
CC   -!- INDUCTION: Up-regulated by cAMP and follicle-stimulating hormone
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
CC       family. PDE4 subfamily.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF536978; AAN10120.1; -; mRNA.
DR   EMBL; AY388962; AAQ90406.1; -; mRNA.
DR   EMBL; AK081466; BAC38226.1; -; mRNA.
DR   EMBL; CT025605; CAQ51656.1; -; Genomic_DNA.
DR   EMBL; AC161585; CAQ51656.1; JOINED; Genomic_DNA.
DR   EMBL; AC163650; CAQ51656.1; JOINED; Genomic_DNA.
DR   EMBL; M94541; AAA37368.1; ALT_TERM; mRNA.
DR   IPI; IPI00344583; -.
DR   IPI; IPI00466648; -.
DR   IPI; IPI00515366; -.
DR   RefSeq; NP_035186.1; NM_011056.3.
DR   UniGene; Mm.434429; -.
DR   ProteinModelPortal; Q01063; -.
DR   SMR; Q01063; 244-678.
DR   DIP; DIP-29706N; -.
DR   STRING; Q01063; -.
DR   PhosphoSite; Q01063; -.
DR   PRIDE; Q01063; -.
DR   Ensembl; ENSMUST00000074103; ENSMUSP00000073742; ENSMUSG00000021699.
DR   Ensembl; ENSMUST00000122041; ENSMUSP00000113488; ENSMUSG00000021699.
DR   GeneID; 238871; -.
DR   KEGG; mmu:238871; -.
DR   UCSC; uc007rvg.1; mouse.
DR   UCSC; uc007rvj.1; mouse.
DR   UCSC; uc007rvm.1; mouse.
DR   CTD; 238871; -.
DR   MGI; MGI:99555; Pde4d.
DR   GeneTree; ENSGT00550000074309; -.
DR   HOVERGEN; HBG108239; -.
DR   OMA; PLDPMAS; -.
DR   OrthoDB; EOG4ZGPBT; -.
DR   BRENDA; 3.1.4.17; 244.
DR   DrugBank; DB00131; Adenosine monophosphate.
DR   NextBio; 383911; -.
DR   ArrayExpress; Q01063; -.
DR   Bgee; Q01063; -.
DR   CleanEx; MM_PDE4D; -.
DR   Genevestigator; Q01063; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006198; P:cAMP catabolic process; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0006939; P:smooth muscle contraction; IMP:MGI.
DR   InterPro; IPR003607; Metal-dep_PHydrolase_HD_dom.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR023174; PDEase_CS.
DR   Gene3D; G3DSA:1.10.1300.10; PDEase_catalytic_dom; 1.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00471; HDc; 1.
DR   PROSITE; PS00126; PDEASE_I; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; cAMP; Cytoplasm; Cytoskeleton; Hydrolase;
KW   Membrane; Metal-binding; Phosphoprotein.
FT   CHAIN         1    747       cAMP-specific 3',5'-cyclic
FT                                phosphodiesterase 4D.
FT                                /FTId=PRO_0000198815.
FT   NP_BIND     401    405       cAMP (By similarity).
FT   ACT_SITE    401    401       Proton donor (By similarity).
FT   METAL       405    405       Divalent metal cation 1 (By similarity).
FT   METAL       441    441       Divalent metal cation 1 (By similarity).
FT   METAL       442    442       Divalent metal cation 1 (By similarity).
FT   METAL       442    442       Divalent metal cation 2 (By similarity).
FT   METAL       559    559       Divalent metal cation 1 (By similarity).
FT   BINDING     442    442       cAMP (By similarity).
FT   SITE        562    562       Binds AMP, but not cAMP (By similarity).
FT   MOD_RES      12     12       Phosphoserine (By similarity).
FT   MOD_RES      14     14       Phosphoserine (By similarity).
FT   MOD_RES      19     19       Phosphothreonine (By similarity).
FT   MOD_RES     129    129       Phosphoserine.
FT   MOD_RES     136    136       Phosphoserine (By similarity).
FT   MOD_RES     141    141       Phosphoserine (By similarity).
FT   MOD_RES     287    287       Phosphoserine (By similarity).
FT   VAR_SEQ       1    163       Missing (in isoform 3).
FT                                /FTId=VSP_012394.
FT   VAR_SEQ       1     69       Missing (in isoform 2).
FT                                /FTId=VSP_012395.
FT   VAR_SEQ      70     91       RPTSLPLKILPLIAVTSADSSG -> MSIIMKPRSRSTSSL
FT                                RTTEAVC (in isoform 2).
FT                                /FTId=VSP_012396.
FT   VAR_SEQ     164    208       PFAQVLASLRTVRNNFAALTNLQDRAPSKRSPMCNQPSINK
FT                                ATIT -> MKEQPSCAGTGHPSMAGYGRMAPFELAGGPVKR
FT                                LRTESSFPCLFA (in isoform 3).
FT                                /FTId=VSP_012397.
FT   CONFLICT    403    404       NI -> SR (in Ref. 5; AAA37368).
SQ   SEQUENCE   747 AA;  84563 MW;  68402163664B3676 CRC64;
     MERDTCDVLS RSKSASEETL HSCNEEEDPF RGMEPYLVRR LSSRSIQLPP LAFRQLEQAD
     LRSESENIPR PTSLPLKILP LIAVTSADSS GFDVDNGTSA GRSPLDPMTS PGSGLILQAN
     FVHSQRRESF LYRSDSDYDL SPKSMSRNSS IASDIHGDDL IVTPFAQVLA SLRTVRNNFA
     ALTNLQDRAP SKRSPMCNQP SINKATITEE AYQKLASETL EELDWCLDQL ETLQTRHSVS
     EMASNKFKRM LNRELTHLSE MSRSGNQVSE YISNTFLDKQ HEVEIPSPTQ KEKEKKKRPM
     SQISGVKKLM HSSSLTNSCI PRFGVKTEQE DVLAKELEDV NKWGLHVFRI AELSGNRPLT
     VIMHTIFQER DLLKTFKIPV DTLITYLMTL EDHYHADVAY HNNIHAADVV QSTHVLLSTP
     ALEAVFTDLE ILAAIFASAI HDVDHPGVSN QFLINTNSEL ALMYNDSSVL ENHHLAVGFK
     LLQEENCDIF QNLTKKQRQS LRKMVIDIVL ATDMSKHMNL LADLKTMVET KKVTSSGVLL
     LDNYSDRIQV LQNMVHCADL SNPTKPLQLY RQWTDRIMEE FFRQGDRERE RGMEISPMCD
     KHNASVEKSQ VGFIDYIVHP LWETWADLVH PDAQDILDTL EDNREWYQST IPQSPSPAPD
     DQEEGRQGQT EKFQFELTLE EDCESDTEKD SGSQVEEDTS CSDSKTLCTQ DSESTEIPLD
     EQVEEEAVAE EESQPETCVP DDCCPDT
//
ID   PDE1B_MOUSE             Reviewed;         535 AA.
AC   Q01065; O35384;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B;
DE            Short=Cam-PDE 1B;
DE            EC=3.1.4.17;
DE   AltName: Full=63 kDa Cam-PDE;
GN   Name=Pde1b; Synonyms=Pde1b1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=93066388; PubMed=1332068; DOI=10.1073/pnas.89.22.11079;
RA   Polli J.W., Kincaid R.L.;
RT   "Molecular cloning of DNA encoding a calmodulin-dependent
RT   phosphodiesterase enriched in striatum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:11079-11083(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 38-535.
RC   STRAIN=129/SvJ;
RX   MEDLINE=98325610; PubMed=9657856; DOI=10.1007/s003359900820;
RA   Reed T.M., Browning J.E., Blough R.I., Vorhees C.V., Repaske D.R.;
RT   "Genomic structure and chromosome location of the murine PDE1B
RT   phosphodiesterase gene.";
RL   Mamm. Genome 9:571-576(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 221-336.
RX   MEDLINE=92406782; PubMed=1326532;
RA   Repaske D.R., Swinnen J.V., Jin S.-L.C., van Wyk J.J., Conti M.;
RT   "A polymerase chain reaction strategy to identify and clone cyclic
RT   nucleotide phosphodiesterase cDNAs. Molecular cloning of the cDNA
RT   encoding the 63-kDa calmodulin-dependent phosphodiesterase.";
RL   J. Biol. Chem. 267:18683-18688(1992).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
CC   -!- FUNCTION: Cyclic nucleotide phosphodiesterase with a dual-
CC       specificity for the second messengers cAMP and cGMP, which are key
CC       regulators of many important physiological processes. Has a
CC       preference for cGMP as a substrate (By similarity).
CC   -!- CATALYTIC ACTIVITY: Nucleoside 3',5'-cyclic phosphate + H(2)O =
CC       nucleoside 5'-phosphate.
CC   -!- COFACTOR: Binds 2 divalent metal cations per subunit. Site 1 may
CC       preferentially bind zinc ions, while site 2 has a preference for
CC       magnesium and/or manganese ions (By similarity).
CC   -!- ENZYME REGULATION: Type I PDE are activated by the binding of
CC       calmodulin in the presence of Ca(2+).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
CC       family. PDE1 subfamily.
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DR   EMBL; L01695; AAA39902.1; -; mRNA.
DR   EMBL; AF023343; AAC96022.1; -; Genomic_DNA.
DR   EMBL; AF023340; AAC96022.1; JOINED; Genomic_DNA.
DR   EMBL; AF023341; AAC96022.1; JOINED; Genomic_DNA.
DR   EMBL; AF023342; AAC96022.1; JOINED; Genomic_DNA.
DR   EMBL; M94538; AAA37367.1; -; mRNA.
DR   IPI; IPI00118900; -.
DR   PIR; A46378; A46378.
DR   RefSeq; NP_032826.1; NM_008800.1.
DR   UniGene; Mm.390792; -.
DR   ProteinModelPortal; Q01065; -.
DR   SMR; Q01065; 71-501.
DR   STRING; Q01065; -.
DR   PhosphoSite; Q01065; -.
DR   PRIDE; Q01065; -.
DR   Ensembl; ENSMUST00000023132; ENSMUSP00000023132; ENSMUSG00000022489.
DR   GeneID; 18574; -.
DR   KEGG; mmu:18574; -.
DR   UCSC; uc007xyh.1; mouse.
DR   CTD; 18574; -.
DR   MGI; MGI:97523; Pde1b.
DR   eggNOG; roNOG13425; -.
DR   HOGENOM; HBG315720; -.
DR   HOVERGEN; HBG056120; -.
DR   InParanoid; Q01065; -.
DR   OMA; HSLISRF; -.
DR   OrthoDB; EOG4FXR79; -.
DR   PhylomeDB; Q01065; -.
DR   BRENDA; 3.1.4.17; 244.
DR   NextBio; 294424; -.
DR   ArrayExpress; Q01065; -.
DR   Bgee; Q01065; -.
DR   CleanEx; MM_PDE1B; -.
DR   Genevestigator; Q01065; -.
DR   GermOnline; ENSMUSG00000022489; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IMP:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   InterPro; IPR003607; Metal-dep_PHydrolase_HD_dom.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR023174; PDEase_CS.
DR   InterPro; IPR013706; PDEase_N.
DR   Gene3D; G3DSA:1.10.1300.10; PDEase_catalytic_dom; 2.
DR   Pfam; PF00233; PDEase_I; 1.
DR   Pfam; PF08499; PDEase_I_N; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00471; HDc; 1.
DR   PROSITE; PS00126; PDEASE_I; 1.
PE   1: Evidence at protein level;
KW   Calmodulin-binding; cAMP; cGMP; Cytoplasm; Hydrolase; Metal-binding;
KW   Phosphoprotein.
FT   CHAIN         1    535       Calcium/calmodulin-dependent 3',5'-cyclic
FT                                nucleotide phosphodiesterase 1B.
FT                                /FTId=PRO_0000198790.
FT   REGION       27     47       Calmodulin-binding (Potential).
FT   REGION      196    495       Catalytic (By similarity).
FT   ACT_SITE    222    222       Proton donor (By similarity).
FT   METAL       226    226       Divalent metal cation 1 (By similarity).
FT   METAL       262    262       Divalent metal cation 1 (By similarity).
FT   METAL       263    263       Divalent metal cation 1 (By similarity).
FT   METAL       263    263       Divalent metal cation 2 (By similarity).
FT   METAL       369    369       Divalent metal cation 1 (By similarity).
FT   MOD_RES     465    465       Phosphoserine.
FT   CONFLICT     38     38       L -> M (in Ref. 2).
FT   CONFLICT    224    224       Q -> R (in Ref. 3; AAA37367).
SQ   SEQUENCE   535 AA;  61226 MW;  F87A585537C8D1CD CRC64;
     MELSPRSPPE MLESDCPSPL ELKSAPSKKM WIKLRSLLRY MVKQLENGEV NIEELKKNLE
     YTASLLEAVY IDETRQILDT EDELRELRSD AVPSEVRDWL ASTFTQQTRA KGRRAEEKPK
     FRSIVHAVQA GIFVERMFRR TYTSVGPTYS TAVHNCLKNL DLWCFDVFSL NRAADDHALR
     TIVFELLTRH SLISRFKIPT VFLMSFLEAL ETGYGKYKNP YHNQIHAADV TQTVHCFLLR
     TGMVHCLSEI EVLAIIFAAA IHDYEHTGTT NSFHIQTKSE CAILYNDRSV LENHHISSVF
     RMMQDDEMNI FINLTKDEFA ELRALVIEMV LATDMSCHFQ QVKTMKTALQ QLERIDKSKA
     LSLLLHAADI SHPTKQWSVH SRWTKALMEE FFRQGDKEAE LGLPFSPLCD RTSTLVAQSQ
     IGFIDFIVEP TFSVLTDVAE KSVQPLADDD SKPKSQPSFQ WRQPSLDVDV GDPNPDVVSF
     RATWTKYIQE NKQKWKERAA SGITNQMSID ELSPCEEEAP SSPAEDEHNQ NGNLD
//
ID   NMDE2_MOUSE             Reviewed;        1482 AA.
AC   Q01097; Q9DCB2;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 3.
DT   08-MAR-2011, entry version 119.
DE   RecName: Full=Glutamate [NMDA] receptor subunit epsilon-2;
DE   AltName: Full=N-methyl D-aspartate receptor subtype 2B;
DE            Short=NMDAR2B;
DE            Short=NR2B;
DE   Flags: Precursor;
GN   Name=Grin2b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92310564; PubMed=1377365; DOI=10.1038/358036a0;
RA   Kutsuwada T., Kashiwabuchi N., Mori H., Sakimura K., Kushiya E.,
RA   Araki K., Meguro H., Masaki H., Kumanishi T., Arakawa M., Mishina M.;
RT   "Molecular diversity of the NMDA receptor channel.";
RL   Nature 358:36-41(1992).
RN   [2]
RP   SEQUENCE REVISION.
RA   Kutsuwada T., Kashiwabuchi N., Mori H., Sakimura K., Kushiya E.,
RA   Araki K., Meguro H., Masaki H., Kumanishi T., Arakawa M., Mishina M.;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-337.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION AT TYR-1472.
RX   MEDLINE=22339849; PubMed=12451687;
RA   Nakazawa T., Tezuka T., Yamamoto T.;
RT   "Regulation of NMDA receptor function by Fyn-mediated tyrosine
RT   phosphorylation.";
RL   Nihon Shinkei Seishin Yakurigaku Zasshi 22:165-167(2002).
RN   [5]
RP   IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3B.
RX   PubMed=12008020; DOI=10.1016/S0169-328X(02)00173-0;
RA   Matsuda K., Kamiya Y., Matsuda S., Yuzaki M.;
RT   "Cloning and characterization of a novel NMDA receptor subunit NR3B: a
RT   dominant subunit that reduces calcium permeability.";
RL   Brain Res. Mol. Brain Res. 100:43-52(2002).
RN   [6]
RP   IDENTIFICATION IN A COMPLEX WITH GRIN1 AND GRIN3B.
RX   PubMed=14602821;
RA   Matsuda K., Fletcher M., Kamiya Y., Yuzaki M.;
RT   "Specific assembly with the NMDA receptor 3B subunit controls surface
RT   expression and calcium permeability of NMDA receptors.";
RL   J. Neurosci. 23:10064-10073(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1166 AND SER-1303, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [8]
RP   INTERACTION WITH HIP1.
RX   PubMed=17329427; DOI=10.1523/JNEUROSCI.5175-06.2007;
RA   Metzler M., Gan L., Wong T.P., Liu L., Helm J., Liu L., Georgiou J.,
RA   Wang Y., Bissada N., Cheng K., Roder J.C., Wang Y.T., Hayden M.R.;
RT   "NMDA receptor function and NMDA receptor-dependent phosphorylation of
RT   huntingtin is altered by the endocytic protein HIP1.";
RL   J. Neurosci. 27:2298-2308(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-930; TYR-932; TYR-949;
RP   TYR-962; TYR-1039; TYR-1049; SER-1061; THR-1065; TYR-1070; TYR-1109;
RP   TYR-1155; TYR-1252; SER-1303 AND TYR-1304, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-917 AND SER-1303, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [11]
RP   INTERACTION WITH NETO1.
RX   PubMed=19243221; DOI=10.1371/journal.pbio.1000041;
RA   Ng D., Pitcher G.M., Szilard R.K., Sertie A., Kanisek M.,
RA   Clapcote S.J., Lipina T., Kalia L.V., Joo D., McKerlie C., Cortez M.,
RA   Roder J.C., Salter M.W., McInnes R.R.;
RT   "Neto1 is a novel CUB-domain NMDA receptor-interacting protein
RT   required for synaptic plasticity and learning.";
RL   PLoS Biol. 7:E41-E41(2009).
CC   -!- FUNCTION: NMDA receptor subtype of glutamate-gated ion channels
CC       with high calcium permeability and voltage-dependent sensitivity
CC       to magnesium. Mediated by glycine.
CC   -!- SUBUNIT: Forms heteromeric channel of a zeta subunit (GRIN1), a
CC       epsilon subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third
CC       subunit (GRIN3A or GRIN3B). Found in a complex with GRIN1 and
CC       GRIN3B. Found in a complex with GRIN1, GRIN3A and PPP2CB.
CC       Interacts with PDZ domains of INADL, DLG4 and MAGI3 (By
CC       similarity). Interacts with HIP1 and NETO1.
CC   -!- INTERACTION:
CC       Q80YE7:Dapk1; NbExp=3; IntAct=EBI-400125, EBI-2584874;
CC       Q62108:Dlg4; NbExp=2; IntAct=EBI-400125, EBI-300895;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Cell junction, synapse, postsynaptic cell membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel
CC       (TC 1.A.10.1) family. NR2B/GRIN2B subfamily.
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DR   EMBL; D10651; BAA01498.2; -; mRNA.
DR   EMBL; AK002963; BAB22483.1; -; mRNA.
DR   IPI; IPI00321320; -.
DR   PIR; I49704; I49704.
DR   RefSeq; NP_032197.3; NM_008171.3.
DR   UniGene; Mm.436649; -.
DR   ProteinModelPortal; Q01097; -.
DR   SMR; Q01097; 33-394, 404-802.
DR   DIP; DIP-31568N; -.
DR   IntAct; Q01097; 255.
DR   MINT; MINT-135847; -.
DR   STRING; Q01097; -.
DR   PhosphoSite; Q01097; -.
DR   PRIDE; Q01097; -.
DR   Ensembl; ENSMUST00000053880; ENSMUSP00000062284; ENSMUSG00000030209.
DR   Ensembl; ENSMUST00000111905; ENSMUSP00000107536; ENSMUSG00000030209.
DR   GeneID; 14812; -.
DR   KEGG; mmu:14812; -.
DR   UCSC; uc009elq.1; mouse.
DR   CTD; 14812; -.
DR   MGI; MGI:95821; Grin2b.
DR   eggNOG; roNOG10982; -.
DR   HOGENOM; HBG717736; -.
DR   HOVERGEN; HBG052635; -.
DR   InParanoid; Q01097; -.
DR   OrthoDB; EOG4Z8XVM; -.
DR   NextBio; 287003; -.
DR   ArrayExpress; Q01097; -.
DR   Bgee; Q01097; -.
DR   Genevestigator; Q01097; -.
DR   GermOnline; ENSMUSG00000030209; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0017146; C:N-methyl-D-aspartate selective glutamate receptor complex; IPI:MGI.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
DR   GO; GO:0005262; F:calcium channel activity; IMP:MGI.
DR   GO; GO:0004972; F:N-methyl-D-aspartate selective glutamate receptor activity; IMP:MGI.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR   GO; GO:0048266; P:behavioral response to pain; IMP:MGI.
DR   GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0007613; P:memory; IDA:MGI.
DR   GO; GO:0060079; P:regulation of excitatory postsynaptic membrane potential; IMP:MGI.
DR   GO; GO:0045471; P:response to ethanol; IMP:MGI.
DR   GO; GO:0007423; P:sensory organ development; IMP:MGI.
DR   GO; GO:0001964; P:startle response; IMP:MGI.
DR   GO; GO:0001967; P:suckling behavior; IMP:MGI.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR019594; Glu_rcpt_Glu/Gly-bd.
DR   InterPro; IPR001320; Iontro_glu_rcpt.
DR   InterPro; IPR001508; NMDA_rcpt.
DR   InterPro; IPR018884; NMDAR2_C.
DR   InterPro; IPR001638; SBP_bac_3.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF10565; NMDAR2_C; 1.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   PRINTS; PR00177; NMDARECEPTOR.
DR   SMART; SM00918; Lig_chan-Glu_bd; 1.
DR   SMART; SM00079; PBPe; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell junction; Cell membrane; Disulfide bond; Glycoprotein;
KW   Ion transport; Ionic channel; Ligand-gated ion channel; Magnesium;
KW   Membrane; Metal-binding; Phosphoprotein; Postsynaptic cell membrane;
KW   Receptor; Signal; Synapse; Transmembrane; Transmembrane helix;
KW   Transport; Zinc.
FT   SIGNAL        1     26       Potential.
FT   CHAIN        27   1482       Glutamate [NMDA] receptor subunit
FT                                epsilon-2.
FT                                /FTId=PRO_0000011578.
FT   TOPO_DOM     27    557       Extracellular (Potential).
FT   TRANSMEM    558    578       Helical; (Potential).
FT   TOPO_DOM    579    634       Cytoplasmic (Potential).
FT   TRANSMEM    635    655       Helical; (Potential).
FT   TOPO_DOM    656    817       Extracellular (Potential).
FT   TRANSMEM    818    838       Helical; (Potential).
FT   TOPO_DOM    839   1482       Cytoplasmic (Potential).
FT   MOTIF      1480   1482       PDZ-binding (By similarity).
FT   COMPBIAS    984    989       Poly-His.
FT   METAL       127    127       Zinc (By similarity).
FT   METAL       284    284       Zinc (By similarity).
FT   SITE        615    615       Functional determinant of NMDA receptors
FT                                (By similarity).
FT   MOD_RES     917    917       Phosphoserine.
FT   MOD_RES     930    930       Phosphoserine.
FT   MOD_RES     932    932       Phosphotyrosine.
FT   MOD_RES     949    949       Phosphotyrosine.
FT   MOD_RES     962    962       Phosphotyrosine.
FT   MOD_RES    1039   1039       Phosphotyrosine.
FT   MOD_RES    1049   1049       Phosphotyrosine.
FT   MOD_RES    1061   1061       Phosphoserine.
FT   MOD_RES    1065   1065       Phosphothreonine.
FT   MOD_RES    1070   1070       Phosphotyrosine.
FT   MOD_RES    1109   1109       Phosphotyrosine.
FT   MOD_RES    1155   1155       Phosphotyrosine.
FT   MOD_RES    1166   1166       Phosphoserine.
FT   MOD_RES    1252   1252       Phosphotyrosine.
FT   MOD_RES    1303   1303       Phosphoserine.
FT   MOD_RES    1304   1304       Phosphotyrosine.
FT   MOD_RES    1472   1472       Phosphotyrosine.
FT   CARBOHYD     74     74       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    341    341       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    348    348       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    444    444       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    491    491       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    542    542       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    688    688       N-linked (GlcNAc...) (Potential).
FT   DISULFID     86    321       By similarity.
FT   CONFLICT     99     99       L -> F (in Ref. 3; BAB22483).
SQ   SEQUENCE   1482 AA;  165959 MW;  B8C3FA10E9A4B36D CRC64;
     MKPSAECCSP KFWLVLAVLA VSGSKARSQK SAPSIGIAVI LVGTSDEVAI KDAHEKDDFH
     HLSVVPRVEL VAMNETDPKS IITRICDLMS DRKIQGVVLA DDTDQEAIAQ ILDFISAQTL
     TPILGIHGGS SMIMADKDES SMFFQFGPSI EQQASVMLNI MEEYDWYIFS IVTTYFPGYQ
     DFVNKIRSTI ENSFVGWELE EVLLLDMSLD DGDSKIQNQL KKLQSPIILL YCTKEEATYI
     FEVANSVGLT GYGYTWIVPS LVAGDTDTVP SEFPTGLISV SYDEWDYGLP ARVRDGIAII
     TTAASDMLSE HSFIPEPKSS CYNTHEKRIY QSNMLNRYLI NVTFEGRNLS FSEDGYQMHP
     KLVIILLNKE RKWERVGKWK DKSLQMKYYV WPRMCPETEE QEDDHLSIVT LEEAPFVIVE
     SVDPLSGTCM RNTVPCQKRI ISENKTDEEP GYIKKCCKGF CIDILKKISK SVKFTYDLYL
     VTNGKHGKKI NGTWNGMIGE VVMKRAYMAV GSLTINEERS EVVDFSVPFI ETGISVMVSR
     SNGTVSPSAF LEPFSADVWV MMFVMLLIVS AVAVFVFEYF SPVGYNRCLA DGREPGGPSF
     TIGKAIWLLW GLVFNNSVPV QNPKGTTSKI MVSVWAFFAV IFLASYTANL AAFMIQEEYV
     DQVSGLSDKK FQRPNDFSPP FRFGTVPNGS TERNIRNNYA EMHAYMGKFN QRGVDDALLS
     LKTGKLDAFI YDAAVLNYMA GRDEGCKLVT IGSGKVFAST GYGIAIQKDS GWKRQVDLAI
     LQLFGDGEME ELEALWLTGI CHNEKNEVMS SQLDIDNMAG VFYMLGAAMA LSLITFICEH
     LFYWQFRHCF MGVCSGKPGM VFSISRGIYS CIHGVAIEER QSVMNSPTAT MNNTHSNILR
     LLRTAKNMAN LSGVNGSPQS ALDFIRRESS VYDISEHRRS FTHSDCKSYN NPPCEENLFS
     DYISEVERTF GNLQLKDSNV YQDHYHHHHR PHSIGSTSSI DGLYDCDNPP FTTQPRSISK
     KPLDIGLPSS KHSQLSDLYG KFSFKSDRYS GHDDLIRSDV SDISTHTVTY GNIEGNAAKR
     RKQQYKDSLK KRPASAKSRR EFDEIELAYR RRPPRSPDHK RYFRDKEGLR DFYLDQFRTK
     ENSPHWEHVD LTDIYKERSD DFKRDSVSGG GPCTNRSHLK HGTGDKHGVV GGVPAPWEKN
     LTNVDWEDRS GGNFCRSCPS KLHNYSSTVA GQNSGRQACI RCEACKKAGN LYDISEDNSL
     QELDQPAAPV AVSSNASTTK YPQSPTNSKA QKKNRNKLRR QHSYDTFVDL QKEEAALAPR
     SVSLKDKGRF MDGSPYAHMF EMPAGESSFA NKSSVTTAGH HHNNPGSGYM LSKSLYPDRV
     TQNPFIPTFG DDQCLLHGSK SYFFRQPTVA GASKTRPDFR ALVTNKPVVS ALHGAVPGRF
     QKDICIGNQS NPCVPNNKNP RAFNGSSNGH VYEKLSSIES DV
//
ID   NMDE3_MOUSE             Reviewed;        1239 AA.
AC   Q01098;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Glutamate [NMDA] receptor subunit epsilon-3;
DE   AltName: Full=N-methyl D-aspartate receptor subtype 2C;
DE            Short=NMDAR2C;
DE            Short=NR2C;
DE   Flags: Precursor;
GN   Name=Grin2c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92310564; PubMed=1377365; DOI=10.1038/358036a0;
RA   Kutsuwada T., Kashiwabuchi N., Mori H., Sakimura K., Kushiya E.,
RA   Araki K., Meguro H., Masaki H., Kumanishi T., Arakawa M., Mishina M.;
RT   "Molecular diversity of the NMDA receptor channel.";
RL   Nature 358:36-41(1992).
RN   [2]
RP   SEQUENCE REVISION.
RA   Kashiwabuchi N.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NMDA receptor subtype of glutamate-gated ion channels
CC       possesses high calcium permeability and voltage-dependent
CC       sensitivity to magnesium. Mediated by glycine.
CC   -!- SUBUNIT: Interacts with PDZ domains of INADL and DLG4 (By
CC       similarity). Forms heteromeric channel of a zeta subunit (GRIN1),
CC       a epsilon subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third
CC       subunit (GRIN3A or GRIN3B).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Cell junction, synapse, postsynaptic cell membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel
CC       (TC 1.A.10.1) family. NR2C/GRIN2C subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D10694; BAA01536.1; -; mRNA.
DR   IPI; IPI00321321; -.
DR   PIR; I49705; I49705.
DR   RefSeq; NP_034480.2; NM_010350.2.
DR   UniGene; Mm.39090; -.
DR   ProteinModelPortal; Q01098; -.
DR   SMR; Q01098; 27-390, 401-799.
DR   MINT; MINT-104161; -.
DR   STRING; Q01098; -.
DR   PhosphoSite; Q01098; -.
DR   PRIDE; Q01098; -.
DR   Ensembl; ENSMUST00000003351; ENSMUSP00000003351; ENSMUSG00000020734.
DR   Ensembl; ENSMUST00000106554; ENSMUSP00000102164; ENSMUSG00000020734.
DR   GeneID; 14813; -.
DR   KEGG; mmu:14813; -.
DR   UCSC; uc007mgx.1; mouse.
DR   CTD; 14813; -.
DR   MGI; MGI:95822; Grin2c.
DR   GeneTree; ENSGT00540000070221; -.
DR   HOGENOM; HBG443877; -.
DR   HOVERGEN; HBG052636; -.
DR   InParanoid; Q01098; -.
DR   OMA; ARDMVTT; -.
DR   OrthoDB; EOG42RD6M; -.
DR   PhylomeDB; Q01098; -.
DR   NextBio; 287007; -.
DR   ArrayExpress; Q01098; -.
DR   Bgee; Q01098; -.
DR   Genevestigator; Q01098; -.
DR   GermOnline; ENSMUSG00000020734; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0017146; C:N-methyl-D-aspartate selective glutamate receptor complex; IPI:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005261; F:cation channel activity; IMP:MGI.
DR   GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0004972; F:N-methyl-D-aspartate selective glutamate receptor activity; IMP:MGI.
DR   GO; GO:0033058; P:directional locomotion; IGI:MGI.
DR   GO; GO:0042177; P:negative regulation of protein catabolic process; IGI:MGI.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR   GO; GO:0008104; P:protein localization; IGI:MGI.
DR   GO; GO:0060079; P:regulation of excitatory postsynaptic membrane potential; IMP:MGI.
DR   GO; GO:0009611; P:response to wounding; IGI:MGI.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR019594; Glu_rcpt_Glu/Gly-bd.
DR   InterPro; IPR001320; Iontro_glu_rcpt.
DR   InterPro; IPR001508; NMDA_rcpt.
DR   InterPro; IPR018884; NMDAR2_C.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR   Pfam; PF10565; NMDAR2_C; 1.
DR   PRINTS; PR00177; NMDARECEPTOR.
DR   SMART; SM00918; Lig_chan-Glu_bd; 1.
DR   SMART; SM00079; PBPe; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Cell junction; Cell membrane; Glycoprotein; Ion transport;
KW   Ionic channel; Ligand-gated ion channel; Magnesium; Membrane;
KW   Postsynaptic cell membrane; Receptor; Signal; Synapse; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     19       Potential.
FT   CHAIN        20   1239       Glutamate [NMDA] receptor subunit
FT                                epsilon-3.
FT                                /FTId=PRO_0000011581.
FT   TOPO_DOM     20    553       Extracellular (Potential).
FT   TRANSMEM    554    574       Helical; (Potential).
FT   TOPO_DOM    575    626       Cytoplasmic (Potential).
FT   TRANSMEM    627    647       Helical; (Potential).
FT   TOPO_DOM    648    814       Extracellular (Potential).
FT   TRANSMEM    815    835       Helical; (Potential).
FT   TOPO_DOM    836   1239       Cytoplasmic (Potential).
FT   MOTIF      1237   1239       PDZ-binding (By similarity).
FT   SITE        612    612       Functional determinant of NMDA receptors
FT                                (By similarity).
FT   CARBOHYD     70     70       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    337    337       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    438    438       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    539    539       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   1239 AA;  135420 MW;  793E8E731E20C3C9 CRC64;
     MGGALGPALL LTSLLGAWAG LGAGQGEQAV TVAVVFGSSG PLQAQARTRL TPQNFLDLPL
     EIQPLTIGVN NTNPSSILTQ ICGLLGAARV HGIVFEDNVD TEAVAQLLDF VSSQTHVPIL
     SISGGSAVVL TPKEPGSAFL QLGVSLEQQL QVLFKVLEEY DWSAFAVITS LHPGHALFLE
     GVRAVADASY LSWRLLDVLT LELGPGGPRA RTQRLLRQVD APVLVAYCSR EEAEVLFAEA
     AQAGLVGPGH VWLVPNLALG STDAPPAAFP VGLISVVTES WRLSLRQKVR DGVAILALGA
     HSYRRQYGTL PAPAGDCRSH PGPVSPAREA FYRHLLNVTW EGRDFSFSPG GYLVQPTMVV
     IALNRHRLWE MVGRWDHGVL YMKYPVWPRY STSLQPVVDS RHLTVATLEE RPFVIVESPD
     PGTGGCVPNT VPCRRQSNHT FSSGDITPYT KLCCKGFCID ILKKLAKVVK FSYDLYLVTN
     GKHGKRVRGV WNGMIGEVYY KRADMAIGSL TINEERSEII DFSVPFVETG ISVMVARSNG
     TVSPSAFLEP YSPAVWVMMF VMCLTVVAIT VFMFEYFSPV SYNQNLTKGK KSGGPSFTIG
     KSVWLLWALV FNNSVPIENP RGTTSKIMVL VWAFFAVIFL ASYTANLAAF MIQEQYIDTV
     SGLSDKKFQR PQDQYPPFRF GTVPNGSTER NIRSNYRDMH THMVKFNQRS VEDALTSLKM
     GKLDAFIYDA AVLNYMAGKD EGCKLVTIGS GKVFATTGYG IAMQKDSHWK RAIDLALLQF
     LGDGETQKLE TVWLSGICHN EKNEVMSSKL DIDNMAGVFY MLLVAMGLAL LVFAWEHLVY
     WKLRHSVPSS SQLDFLLAFS RGIYSCFNGV QSLPSPARPP SPDLTAGSAQ ANVLKMLQAA
     RDMVSTADVS GSLDRATRTI ENWGNNRRAP APTTSGPRSC TPGPPGQPSP SGWRPPGGGR
     TPLARRAPQP PARPATCAGS PQPDVSRASC RHAWDARWPV RVGHQGSHLS ASERRALPER
     SLLHAHCHYS SFPRAERSGR PFLPLFPEPP EPDDLPLLGP EQLARREALL RAAWARGPRP
     RHASLPSSVA EAFTRSNPLP ARCTGHACAC PCPQSRPSCR HVAQTQSLRL PSYREACVEG
     VPAGVAATWQ PRQHVCLHTH THLPFCWGTV CRHPPPCSSH SPWLIGTWEP PSHRGRTLGL
     GTGYRDSGVL EEVSREACGT QGFPRSCTWR RISSLESEV
//
ID   ADA2C_MOUSE             Reviewed;         458 AA.
AC   Q01337;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Alpha-2C adrenergic receptor;
DE   AltName: Full=Alpha-2 adrenergic receptor subtype C4;
DE   AltName: Full=Alpha-2C adrenoreceptor;
DE            Short=Alpha-2C adrenoceptor;
DE            Short=Alpha-2CAR;
GN   Name=Adra2c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92342131; PubMed=1353249;
RA   Link R.E., Daunt D.A., Barsh G., Chruscinski A.J., Kobilka B.K.;
RT   "Cloning of two mouse genes encoding alpha 2-adrenergic receptor
RT   subtypes and identification of a single amino acid in the mouse alpha
RT   2-C10 homolog responsible for an interspecies variation in antagonist
RT   binding.";
RL   Mol. Pharmacol. 42:16-27(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DBA/2;
RX   MEDLINE=93250567; PubMed=8387367;
RA   Chang Y.-H., Chang A.C., Chen W.-M., Chang N.-C.A.;
RT   "Molecular characterization of a murine homologue of alpha 2C4
RT   adrenoceptor subtype gene.";
RL   Biochem. Mol. Biol. Int. 29:467-474(1993).
CC   -!- FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine-
CC       induced inhibition of adenylate cyclase through the action of G
CC       proteins.
CC   -!- INTERACTION:
CC       Q14232:EIF2B1 (xeno); NbExp=1; IntAct=EBI-491121, EBI-491065;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Adrenergic receptor subfamily. ADRA2C sub-subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M99376; AAA37212.1; -; Genomic_DNA.
DR   EMBL; M97516; AAA37183.1; -; Genomic_DNA.
DR   IPI; IPI00850891; -.
DR   PIR; A48392; A48392.
DR   PIR; I49480; I49480.
DR   RefSeq; NP_031444.2; NM_007418.3.
DR   UniGene; Mm.407152; -.
DR   UniGene; Mm.57205; -.
DR   ProteinModelPortal; Q01337; -.
DR   SMR; Q01337; 52-449.
DR   IntAct; Q01337; 1.
DR   STRING; Q01337; -.
DR   PRIDE; Q01337; -.
DR   Ensembl; ENSMUST00000049545; ENSMUSP00000059705; ENSMUSG00000045318.
DR   GeneID; 11553; -.
DR   KEGG; mmu:11553; -.
DR   UCSC; uc009vdd.1; mouse.
DR   CTD; 11553; -.
DR   MGI; MGI:87936; Adra2c.
DR   eggNOG; maNOG18808; -.
DR   GeneTree; ENSGT00600000084199; -.
DR   HOGENOM; HBG445348; -.
DR   HOVERGEN; HBG106962; -.
DR   InParanoid; Q01337; -.
DR   OMA; SRSVEFF; -.
DR   OrthoDB; EOG4R502W; -.
DR   PhylomeDB; Q01337; -.
DR   NextBio; 459225; -.
DR   ArrayExpress; Q01337; -.
DR   Bgee; Q01337; -.
DR   CleanEx; MM_ADRA2C; -.
DR   Genevestigator; Q01337; -.
DR   GermOnline; ENSMUSG00000045318; Mus musculus.
DR   GO; GO:0004938; F:alpha2-adrenergic receptor activity; TAS:MGI.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR000735; Adren_rcpt_A2C.
DR   InterPro; IPR002233; Adrnrgc_rcpt.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01103; ADRENERGICR.
DR   PRINTS; PR00560; ADRENRGCA2CR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Phosphoprotein; Receptor; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    458       Alpha-2C adrenergic receptor.
FT                                /FTId=PRO_0000069106.
FT   TOPO_DOM      1     51       Extracellular (By similarity).
FT   TRANSMEM     52     76       Helical; Name=1; (By similarity).
FT   TOPO_DOM     77     88       Cytoplasmic (By similarity).
FT   TRANSMEM     89    114       Helical; Name=2; (By similarity).
FT   TOPO_DOM    115    124       Extracellular (By similarity).
FT   TRANSMEM    125    147       Helical; Name=3; (By similarity).
FT   TOPO_DOM    148    168       Cytoplasmic (By similarity).
FT   TRANSMEM    169    191       Helical; Name=4; (By similarity).
FT   TOPO_DOM    192    207       Extracellular (By similarity).
FT   TRANSMEM    208    231       Helical; Name=5; (By similarity).
FT   TOPO_DOM    232    379       Cytoplasmic (By similarity).
FT   TRANSMEM    380    403       Helical; Name=6; (By similarity).
FT   TOPO_DOM    404    416       Extracellular (By similarity).
FT   TRANSMEM    417    437       Helical; Name=7; (By similarity).
FT   TOPO_DOM    438    458       Cytoplasmic (By similarity).
FT   COMPBIAS    291    305       Arg-rich (basic).
FT   SITE        131    131       Implicated in ligand binding (By
FT                                similarity).
FT   SITE        214    214       Implicated in catechol agonist binding
FT                                and receptor activation (By similarity).
FT   SITE        218    218       Implicated in catechol agonist binding
FT                                and receptor activation (By similarity).
FT   CARBOHYD     19     19       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     33     33       N-linked (GlcNAc...) (Potential).
FT   DISULFID    124    202       By similarity.
FT   CONFLICT    196    196       G -> V (in Ref. 2; AAA37183).
FT   CONFLICT    296    296       G -> A (in Ref. 2).
FT   CONFLICT    298    298       L -> V (in Ref. 2).
SQ   SEQUENCE   458 AA;  49906 MW;  C0A8BDF0302BF1FB CRC64;
     MASPALAAAL AAAAAEGPNG SDAGEWGSGG GANASGTDWV PPPGQYSAGA VAGLAAVVGF
     LIVFTVVGNV LVVIAVLTSR ALRAPQNLFL VSLASADILV ATLVMPFSLA NELMAYWYFG
     QVWCGVYLAL DVLFCTSSIV HLCAISLDRY WSVTQAVEYN LKRTPRRVKA TIVAVWLISA
     VISFPPLVSF YRRPDGAAYP QCGLNDETWY ILSSCIGSFF APCLIMGLVY ARIYRVAKLR
     TRTLSEKRGP AGPDGASPTT ENGLGKAAGE NGHCAPPRTE VEPDESSAAE RRRRRGALRR
     GGRRREGAEG DTGSADGPGP GLAAEQGART ASRSPGPGGR LSRASSRSVE FFLSRRRRAR
     SSVCRRKVAQ AREKRFTFVL AVVMGVFVLC WFPFFFSYSL YGICREACQL PEPLFKFFFW
     IGYCNSSLNP VIYTVFNQDF RRSFKHILFR RRRRGFRQ
//
ID   ADA2A_MOUSE             Reviewed;         450 AA.
AC   Q01338;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Alpha-2A adrenergic receptor;
DE   AltName: Full=Alpha-2A adrenoreceptor;
DE            Short=Alpha-2A adrenoceptor;
DE            Short=Alpha-2AAR;
GN   Name=Adra2a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92342131; PubMed=1353249;
RA   Link R.E., Daunt D.A., Barsh G., Chruscinski A.J., Kobilka B.K.;
RT   "Cloning of two mouse genes encoding alpha 2-adrenergic receptor
RT   subtypes and identification of a single amino acid in the mouse alpha
RT   2-C10 homolog responsible for an interspecies variation in antagonist
RT   binding.";
RL   Mol. Pharmacol. 42:16-27(1992).
CC   -!- FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine-
CC       induced inhibition of adenylate cyclase through the action of G
CC       proteins.
CC   -!- INTERACTION:
CC       Q14232:EIF2B1 (xeno); NbExp=1; IntAct=EBI-491073, EBI-491065;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Adrenergic receptor subfamily. ADRA2A sub-subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M99377; AAA37213.1; -; Genomic_DNA.
DR   IPI; IPI00122276; -.
DR   PIR; I49481; I49481.
DR   UniGene; Mm.235195; -.
DR   ProteinModelPortal; Q01338; -.
DR   SMR; Q01338; 34-442.
DR   IntAct; Q01338; 2.
DR   STRING; Q01338; -.
DR   PhosphoSite; Q01338; -.
DR   PRIDE; Q01338; -.
DR   Ensembl; ENSMUST00000036700; ENSMUSP00000036203; ENSMUSG00000033717.
DR   UCSC; uc008hxi.1; mouse.
DR   MGI; MGI:87934; Adra2a.
DR   eggNOG; maNOG17874; -.
DR   HOVERGEN; HBG106962; -.
DR   InParanoid; Q01338; -.
DR   OrthoDB; EOG4R502W; -.
DR   PhylomeDB; Q01338; -.
DR   NextBio; 279038; -.
DR   ArrayExpress; Q01338; -.
DR   Bgee; Q01338; -.
DR   CleanEx; MM_ADRA2A; -.
DR   Genevestigator; Q01338; -.
DR   GermOnline; ENSMUSG00000033717; Mus musculus.
DR   GO; GO:0004938; F:alpha2-adrenergic receptor activity; TAS:MGI.
DR   GO; GO:0042596; P:fear response; IMP:MGI.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR001946; Adren_rcpt_A2A.
DR   InterPro; IPR002233; Adrnrgc_rcpt.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01103; ADRENERGICR.
DR   PRINTS; PR00558; ADRENRGCA2AR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Receptor; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN         1    450       Alpha-2A adrenergic receptor.
FT                                /FTId=PRO_0000069081.
FT   TOPO_DOM      1     33       Extracellular (By similarity).
FT   TRANSMEM     34     59       Helical; Name=1; (By similarity).
FT   TOPO_DOM     60     70       Cytoplasmic (By similarity).
FT   TRANSMEM     71     96       Helical; Name=2; (By similarity).
FT   TOPO_DOM     97    106       Extracellular (By similarity).
FT   TRANSMEM    107    129       Helical; Name=3; (By similarity).
FT   TOPO_DOM    130    149       Cytoplasmic (By similarity).
FT   TRANSMEM    150    173       Helical; Name=4; (By similarity).
FT   TOPO_DOM    174    192       Extracellular (By similarity).
FT   TRANSMEM    193    217       Helical; Name=5; (By similarity).
FT   TOPO_DOM    218    374       Cytoplasmic (By similarity).
FT   TRANSMEM    375    399       Helical; Name=6; (By similarity).
FT   TOPO_DOM    400    409       Extracellular (By similarity).
FT   TRANSMEM    410    430       Helical; Name=7; (By similarity).
FT   TOPO_DOM    431    450       Cytoplasmic (By similarity).
FT   SITE        113    113       Implicated in ligand binding (By
FT                                similarity).
FT   SITE        200    200       Implicated in catechol agonist binding
FT                                (By similarity).
FT   SITE        204    204       Implicated in catechol agonist binding
FT                                (By similarity).
FT   MOD_RES     297    297       Phosphoserine (By similarity).
FT   MOD_RES     298    298       Phosphoserine (By similarity).
FT   MOD_RES     299    299       Phosphoserine (By similarity).
FT   LIPID       442    442       S-palmitoyl cysteine (By similarity).
FT   CARBOHYD     10     10       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     14     14       N-linked (GlcNAc...) (Potential).
FT   DISULFID    106    188       By similarity.
SQ   SEQUENCE   450 AA;  48865 MW;  F07E225393AFA93B CRC64;
     MGSLQPDAGN SSWNGTEAPG GGTRATPYSL QVTLTLVCLA GLLMLFTVFG NVLVIIAVFT
     SRALKAPQNL FLVSLASADI LVATLVIPFS LANEVMGYWY FGKVWCEIYL ALDVLFCTSS
     IVHLCAISLD RYWSITQAIE YNLKRTPRRI KAIIVTVWVI SAVISFPPLI SIEKKGAGGG
     QQPAEPSCKI NDQKWYVISS SIGSFFAPCL IMILVYVRIY QIAKRRTRVP PSRRGPDACS
     APPGGADRRP NGLGPERGAG PTGAEAEPLP TQLNGAPGEP APAGPRDGDA LDLEESSSSE
     HAERPPGPRR PDRGPRAKGK TRASQVKPGD SLPRRGPGAA GPGASGSGHG EERGGGAKAS
     RWRGRQNREK RFTFVLAVVI GVFVVCWFPF FFTYTLIAVG CPVPSQLFNF FFWFGYCNSS
     LNPVIYTIFN HDFRRAFKKI LCRGDRKRIV
//
ID   ADCY6_MOUSE             Reviewed;        1165 AA.
AC   Q01341;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   08-MAR-2011, entry version 101.
DE   RecName: Full=Adenylate cyclase type 6;
DE            EC=4.6.1.1;
DE   AltName: Full=ATP pyrophosphate-lyase 6;
DE   AltName: Full=Adenylate cyclase type VI;
DE   AltName: Full=Adenylyl cyclase 6;
DE   AltName: Full=Ca(2+)-inhibitable adenylyl cyclase;
GN   Name=Adcy6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92357702; PubMed=1379717; DOI=10.1073/pnas.89.15.6716;
RA   Yoshimura M., Cooper D.M.F.;
RT   "Cloning and expression of a Ca(2+)-inhibitable adenylyl cyclase from
RT   NCB-20 cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:6716-6720(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-1165.
RX   MEDLINE=93076707; PubMed=1332848; DOI=10.1210/en.131.6.2774;
RA   Premont R.T., Jacobowitz O., Iyengar R.;
RT   "Lowered responsiveness of the catalyst of adenylyl cyclase to
RT   stimulation by GS in heterologous desensitization: a role for
RT   adenosine 3',5'-monophosphate-dependent phosphorylation.";
RL   Endocrinology 131:2774-2784(1992).
CC   -!- FUNCTION: Membrane-bound, calcium-inhibitable adenylyl cyclase.
CC   -!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
CC   -!- COFACTOR: Binds 2 magnesium ions per subunit (By similarity).
CC   -!- ENZYME REGULATION: Inhibition by calcium in the submicromolar
CC       concentration range.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Most abundant in heart but weakly detectable
CC       in brain, intestine, lung and spleen.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
CC       cyclase family.
CC   -!- SIMILARITY: Contains 2 guanylate cyclase domains.
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DR   EMBL; M93422; AAA37174.1; -; mRNA.
DR   EMBL; M96653; AAA37182.1; -; mRNA.
DR   IPI; IPI00122297; -.
DR   PIR; A49201; A49201.
DR   RefSeq; NP_031431.2; NM_007405.2.
DR   UniGene; Mm.157091; -.
DR   ProteinModelPortal; Q01341; -.
DR   SMR; Q01341; 362-550, 968-1160.
DR   STRING; Q01341; -.
DR   PhosphoSite; Q01341; -.
DR   PRIDE; Q01341; -.
DR   Ensembl; ENSMUST00000096224; ENSMUSP00000093939; ENSMUSG00000022994.
DR   GeneID; 11512; -.
DR   KEGG; mmu:11512; -.
DR   UCSC; uc007xmz.1; mouse.
DR   CTD; 11512; -.
DR   MGI; MGI:87917; Adcy6.
DR   eggNOG; roNOG11298; -.
DR   HOGENOM; HBG445220; -.
DR   HOVERGEN; HBG050458; -.
DR   InParanoid; Q01341; -.
DR   OrthoDB; EOG4255S0; -.
DR   BRENDA; 4.6.1.1; 244.
DR   NextBio; 278914; -.
DR   ArrayExpress; Q01341; -.
DR   Bgee; Q01341; -.
DR   CleanEx; MM_ADCY6; -.
DR   Genevestigator; Q01341; -.
DR   GermOnline; ENSMUSG00000022994; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:MGI.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   InterPro; IPR009398; Aden_cycl-like.
DR   Gene3D; G3DSA:3.30.70.1230; A/G_cyclase; 2.
DR   Pfam; PF06327; DUF1053; 1.
DR   Pfam; PF00211; Guanylate_cyc; 2.
DR   SMART; SM00044; CYCc; 2.
DR   SUPFAM; SSF55073; A/G_cyclase; 2.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 2.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; cAMP biosynthesis; Glycoprotein; Lyase; Magnesium;
KW   Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein; Repeat;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1   1165       Adenylate cyclase type 6.
FT                                /FTId=PRO_0000195700.
FT   TOPO_DOM      1    149       Cytoplasmic (Potential).
FT   TRANSMEM    150    166       Helical; (Potential).
FT   TRANSMEM    179    195       Helical; (Potential).
FT   TRANSMEM    212    228       Helical; (Potential).
FT   TRANSMEM    237    253       Helical; (Potential).
FT   TRANSMEM    257    273       Helical; (Potential).
FT   TRANSMEM    287    303       Helical; (Potential).
FT   TOPO_DOM    304    670       Cytoplasmic (Potential).
FT   TRANSMEM    671    688       Helical; (Potential).
FT   TRANSMEM    699    715       Helical; (Potential).
FT   TRANSMEM    740    756       Helical; (Potential).
FT   TOPO_DOM    757    816       Extracellular (Potential).
FT   TRANSMEM    817    833       Helical; (Potential).
FT   TRANSMEM    836    852       Helical; (Potential).
FT   TRANSMEM    894    910       Helical; (Potential).
FT   TOPO_DOM    911   1165       Cytoplasmic (Potential).
FT   METAL       382    382       Magnesium 1 (By similarity).
FT   METAL       382    382       Magnesium 2 (By similarity).
FT   METAL       383    383       Magnesium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       426    426       Magnesium 1 (By similarity).
FT   METAL       426    426       Magnesium 2 (By similarity).
FT   MOD_RES      53     53       Phosphoserine (By similarity).
FT   MOD_RES     573    573       Phosphoserine (By similarity).
FT   CARBOHYD    277    277       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    790    790       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    875    875       N-linked (GlcNAc...) (Potential).
FT   CONFLICT     47     47       K -> N (in Ref. 2; AAA37182).
FT   CONFLICT     76     76       G -> A (in Ref. 2; AAA37182).
FT   CONFLICT    508    509       GR -> RAG (in Ref. 2; AAA37182).
FT   CONFLICT    737    737       V -> G (in Ref. 2; AAA37182).
FT   CONFLICT    881    881       L -> Q (in Ref. 2; AAA37182).
FT   CONFLICT    990    990       V -> M (in Ref. 2; AAA37182).
SQ   SEQUENCE   1165 AA;  130319 MW;  24EE1BB45DF1E87E CRC64;
     MSWFSGLLVP KVDERKTAWG ERNGQKRPRH ANRASGFCAP RYMSCLKNAE PPSPTPAAHT
     RCPWQDEAFI RRAGPGRGVE LGLRSVALGF DDTEVTTPMG TAEVAPDTSP RSGPSCWHRL
     VQVFQSKQFR SAKLERLYQR YFFQMNQSSL TLLMAVLVLL MAVLLTFHAA PAQPQPAYVA
     LLTCASVLFV VLMVVCNRHS FRQDSMWVVS YVVLGILAAV QVGGALAANP HSPSAGLWCP
     VFFVYITYTL LPIRMRAAVL SGLGLSTLHL ILAWQLNSSD PFLWKQLGAN VVLFLCTNAI
     GVCTHYPAEV SQRQAFQETR GYIQARLHLQ HENRQQERLL LSVLPQHVAM EMKEDINTKK
     EDMMFHKIYI QKHDNVSILF ADIEGFTSLA SQCTAQELVM TLNELFARFD KLAAENHCLR
     IKILGDCYYC VSGLPEARAD HAHCCVEMGV DMIEAISLVR EVTGVNVNMR VGIHSGRVHC
     GVLGLRKWQF DVWSNDVTLA NHMEAGGGRR IHITRATLQY LNGDYEVEPG RGGERNAYLK
     EQCIETFLIL GASQKRKEEK AMLAKLQRTR ANSMEGLMPR WVPDRAFSRT KDSKAFRQMG
     IDDSSKDNRG AQDALNPEDE VDEFLGRAID ARSIDQLRKD HVRRFLLTFQ REDLEKKYSR
     KVDPRFGAYV ACALLVFCFI CFIQLLVFPY STLILGIYAA IFLLLLVTVL ICAVCSCGSF
     FPKALQRLSR NIVRSRVHST AVGIFSVLLV FISAIANMFT CNHTPIRTCA ARMLNLTPAD
     VTACHLQQLN YSLGLDAPLC EGTAPTCSFP EYFVGNVLLS LLASSVFLHI SSIGKLAMTF
     ILGFTYLVLL LLGPPAAIFD NYDLLLGVHG LASSNETFDG LDCPAVGRVA LKYMTPVILL
     VFALALYLHA QQVESTARLD FLWKLQATGE KEEMEELQAY NRRLLHNILP KDVAAHFLAR
     ERRNDELYYQ SCECVAVMFA SIANFSEFYV ELEANNEGVE CLRLLNEIIA DFDEIISEER
     FRQLEKIKTI GSTYMAASGL NASTYDQVGR SHITALADYA MRLMEQMKHI NEHSFNNFQM
     KIGLNMGPVV AGVIGARKPQ YDIWGNTVNV SSRMDSTGVP DRIQVTTDLY QVLAAKGYQL
     ECRGVVKVKG KGEMTTYFLN GGPSS
//
ID   NDKB_MOUSE              Reviewed;         152 AA.
AC   Q01768;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Nucleoside diphosphate kinase B;
DE            Short=NDK B;
DE            Short=NDP kinase B;
DE            EC=2.7.4.6;
DE   AltName: Full=Histidine protein kinase NDKB;
DE            EC=2.7.13.3;
DE   AltName: Full=P18;
DE   AltName: Full=nm23-M2;
GN   Name=Nme2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=92387389; PubMed=1325378; DOI=10.1016/0014-5793(92)80807-S;
RA   Urano T., Takamiya K., Furukawa K., Shiku H.;
RT   "Molecular cloning and functional expression of the second mouse
RT   nm23/NDP kinase gene, nm23-M2.";
RL   FEBS Lett. 309:358-362(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RA   Takeshi U.;
RL   Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 7-26; 57-66 AND 89-143, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   INTERACTION WITH CAPN8, AND TISSUE SPECIFICITY.
RX   PubMed=16476741; DOI=10.1074/jbc.M509244200;
RA   Hata S., Koyama S., Kawahara H., Doi N., Maeda T.,
RA   Toyama-Sorimachi N., Abe K., Suzuki K., Sorimachi H.;
RT   "Stomach-specific calpain, nCL-2, localizes in mucus cells and
RT   proteolyzes the beta-subunit of coatomer complex, beta-COP.";
RL   J. Biol. Chem. 281:11214-11224(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-94, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20884616; DOI=10.1074/jbc.M110.168070;
RA   Di L., Srivastava S., Zhdanova O., Sun Y., Li Z., Skolnik E.Y.;
RT   "Nucleoside diphosphate kinase B knock-out mice have impaired
RT   activation of the K+ channel KCa3.1, resulting in defective T cell
RT   activation.";
RL   J. Biol. Chem. 285:38765-38771(2010).
CC   -!- FUNCTION: Major role in the synthesis of nucleoside triphosphates
CC       other than ATP. The ATP gamma phosphate is transferred to the NDP
CC       beta phosphate via a ping-pong mechanism, using a phosphorylated
CC       active-site intermediate. Negatively regulates Rho activity by
CC       interacting with AKAP13/LBC. Exhibits histidine protein kinase
CC       activity (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + nucleoside diphosphate = ADP +
CC       nucleoside triphosphate.
CC   -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-
CC       phospho-L-histidine.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SUBUNIT: Hexamer of two different chains: A and B (A6, A5B, A4B2,
CC       A3B3, A2B4, AB5, B6). Interacts with AKAP13 (By similarity).
CC       Interacts with CAPN8.
CC   -!- INTERACTION:
CC       P09055:Itgb1; NbExp=2; IntAct=EBI-642573, EBI-644224;
CC       P26450:Pik3r1; NbExp=2; IntAct=EBI-642573, EBI-641764;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane.
CC   -!- TISSUE SPECIFICITY: Expressed in the base region of the oxyntic
CC       and pyloric mucosae.
CC   -!- DISRUPTION PHENOTYPE: Impaired activation of the K+ channel KCNN4,
CC       resulting in defective T cell activation.
CC   -!- SIMILARITY: Belongs to the NDK family.
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DR   EMBL; X68193; CAA48275.1; -; mRNA.
DR   EMBL; AK012447; BAB28246.1; -; mRNA.
DR   EMBL; BC066995; AAH66995.1; -; mRNA.
DR   EMBL; BC086892; AAH86892.1; -; mRNA.
DR   EMBL; BC086893; AAH86893.1; -; mRNA.
DR   IPI; IPI00127417; -.
DR   PIR; S29241; S29241.
DR   RefSeq; NP_001070997.1; NM_001077529.1.
DR   RefSeq; NP_032731.1; NM_008705.4.
DR   UniGene; Mm.1260; -.
DR   ProteinModelPortal; Q01768; -.
DR   SMR; Q01768; 2-152.
DR   IntAct; Q01768; 9.
DR   STRING; Q01768; -.
DR   PhosphoSite; Q01768; -.
DR   SWISS-2DPAGE; Q01768; -.
DR   PMMA-2DPAGE; Q01768; -.
DR   REPRODUCTION-2DPAGE; Q01768; -.
DR   PRIDE; Q01768; -.
DR   Ensembl; ENSMUST00000021217; ENSMUSP00000021217; ENSMUSG00000020857.
DR   Ensembl; ENSMUST00000072566; ENSMUSP00000103476; ENSMUSG00000020857.
DR   GeneID; 18103; -.
DR   KEGG; mmu:18103; -.
DR   UCSC; uc007kxs.1; mouse.
DR   CTD; 18103; -.
DR   MGI; MGI:97356; Nme2.
DR   eggNOG; roNOG13226; -.
DR   HOGENOM; HBG445152; -.
DR   HOVERGEN; HBG000423; -.
DR   InParanoid; Q01768; -.
DR   OMA; WFKADEI; -.
DR   OrthoDB; EOG4S1T8G; -.
DR   PhylomeDB; Q01768; -.
DR   BRENDA; 2.7.4.6; 244.
DR   NextBio; 293275; -.
DR   ArrayExpress; Q01768; -.
DR   Bgee; Q01768; -.
DR   Genevestigator; Q01768; -.
DR   GermOnline; ENSMUSG00000020857; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
DR   InterPro; IPR001564; Nucleoside_diP_kinase.
DR   InterPro; IPR023005; Nucleoside_diP_kinase_AS.
DR   Gene3D; G3DSA:3.30.70.141; NDK; 1.
DR   PANTHER; PTHR11349; Nuc_diP_kinase_core; 1.
DR   Pfam; PF00334; NDK; 1.
DR   PRINTS; PR01243; NUCDPKINASE.
DR   SMART; SM00562; NDK; 1.
DR   SUPFAM; SSF54919; NDK; 1.
DR   PROSITE; PS00469; NDP_KINASES; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cell membrane; Cytoplasm;
KW   Direct protein sequencing; Kinase; Magnesium; Membrane; Metal-binding;
KW   Nucleotide metabolism; Nucleotide-binding; Phosphoprotein;
KW   Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    152       Nucleoside diphosphate kinase B.
FT                                /FTId=PRO_0000137118.
FT   REGION        2     66       Interaction with AKAP13 (By similarity).
FT   ACT_SITE    118    118       Pros-phosphohistidine intermediate (By
FT                                similarity).
FT   BINDING      12     12       ATP (By similarity).
FT   BINDING      60     60       ATP (By similarity).
FT   BINDING      88     88       ATP (By similarity).
FT   BINDING      94     94       ATP (By similarity).
FT   BINDING     105    105       ATP (By similarity).
FT   BINDING     115    115       ATP (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      12     12       N6-acetyllysine (By similarity).
FT   MOD_RES      49     49       N6-acetyllysine (By similarity).
FT   MOD_RES      52     52       Phosphotyrosine (By similarity).
FT   MOD_RES      56     56       N6-acetyllysine (By similarity).
FT   MOD_RES      85     85       N6-acetyllysine (By similarity).
FT   MOD_RES      94     94       Phosphothreonine.
FT   MOD_RES     100    100       N6-acetyllysine (By similarity).
FT   MOD_RES     128    128       N6-acetyllysine (By similarity).
SQ   SEQUENCE   152 AA;  17363 MW;  1A5C3F84C1FFC83C CRC64;
     MANLERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVAMKF LRASEEHLKQ HYIDLKDRPF
     FPGLVKYMNS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRNIIHGS
     DSVESAEKEI HLWFKPEELI DYKSCAHDWV YE
//
ID   CAC1C_MOUSE             Reviewed;        2139 AA.
AC   Q01815; Q04476; Q61242; Q99242;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 113.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1C;
DE   AltName: Full=Calcium channel, L type, alpha-1 polypeptide, isoform 1, cardiac muscle;
DE   AltName: Full=MELC-CC;
DE   AltName: Full=Mouse brain class C;
DE            Short=MBC;
DE   AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.2;
GN   Name=Cacna1c; Synonyms=Cach2, Cacn2, Cacnl1a1, Cchl1a1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC   TISSUE=Brain;
RX   MEDLINE=93054582; PubMed=1385406;
RA   Ma W.-J., Holz R.W., Uhler M.D.;
RT   "Expression of a cDNA for a neuronal calcium channel alpha1 subunit
RT   enhances secretion from adrenal chromaffin cells.";
RL   J. Biol. Chem. 267:22728-22732(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1162-1455 (ISOFORMS 1 AND 2).
RC   STRAIN=ICR; TISSUE=Ovary;
RX   MEDLINE=91056091; PubMed=2173707;
RA   Perez-Reyes E., Wei X., Castellano A., Birnbaumer L.;
RT   "Molecular diversity of L-type calcium channels. Evidence for
RT   alternative splicing of the transcripts of three non-allelic genes.";
RL   J. Biol. Chem. 265:20430-20436(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 762-1070.
RA   Chaudhari N.;
RL   Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 265-2139 (ISOFORM 3).
RC   STRAIN=DBA/2J; TISSUE=Erythroleukemia;
RX   MEDLINE=95113873; PubMed=7814415; DOI=10.1074/jbc.270.1.483;
RA   Ma Y., Kobrinsky E., Marks A.R.;
RT   "Cloning and expression of a novel truncated calcium channel from non-
RT   excitable cells.";
RL   J. Biol. Chem. 270:483-493(1995).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-815, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   INTERACTION WITH CABP5, AND TISSUE SPECIFICITY.
RX   PubMed=18586882; DOI=10.1167/iovs.08-2236;
RA   Rieke F., Lee A., Haeseleer F.;
RT   "Characterization of Ca2+-binding protein 5 knockout mouse retina.";
RL   Invest. Ophthalmol. Vis. Sci. 49:5126-5135(2008).
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the
CC       entry of calcium ions into excitable cells and are also involved
CC       in a variety of calcium-dependent processes, including muscle
CC       contraction, hormone or neurotransmitter release, gene expression,
CC       cell motility, cell division and cell death. The isoform alpha-1C
CC       gives rise to L-type calcium currents. Long-lasting (L-type)
CC       calcium channels belong to the 'high-voltage activated' (HVA)
CC       group. They are blocked by dihydropyridines (DHP),
CC       phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA
CC       (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-
CC       GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA).
CC       Calcium channels containing the alpha-1C subunit play an important
CC       role in excitation-contraction coupling in the heart. Binding of
CC       calmodulin or CABP1 at the same regulatory sites results in an
CC       opposit effects on the channel function (By similarity).
CC   -!- SUBUNIT: Voltage-dependent calcium channels are multisubunit
CC       complexes, consisting of alpha-1, alpha-2, beta and delta subunits
CC       in a 1:1:1:1 ratio. The channel activity is directed by the pore-
CC       forming and voltage-sensitive alpha-1 subunit. In many cases, this
CC       subunit is sufficient to generate voltage-sensitive calcium
CC       channel activity. The auxiliary subunits beta and alpha-2/delta
CC       linked by a disulfide bridge regulate the channel activity.
CC       Interacts (via C-terminal CDB motif) with CABP5; in a calcium-
CC       dependent manner. Interacts with CABP1 and CACNA2D4 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell
CC       membrane (By similarity). Note=The interaction between RRAD and
CC       CACNB2 regulates its trafficking to the cell membrane (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1; Synonyms=CACH2A;
CC         IsoId=Q01815-1; Sequence=Displayed;
CC       Name=2; Synonyms=CACH2D;
CC         IsoId=Q01815-2; Sequence=VSP_000900, VSP_000901;
CC       Name=3; Synonyms=Truncated;
CC         IsoId=Q01815-3; Sequence=VSP_000896, VSP_000897, VSP_000898,
CC                                  VSP_000899, VSP_000901;
CC   -!- TISSUE SPECIFICITY: High expression in heart, followed by brain
CC       and spinal cord. Expressed in retina in rod bipolar cells.
CC   -!- DOMAIN: Each of the four internal repeats contains five
CC       hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one
CC       positively charged transmembrane segment (S4). S4 segments
CC       probably represent the voltage-sensor and are characterized by a
CC       series of positively charged amino acids at every third position.
CC   -!- DOMAIN: Binding of intracellular calcium through the EF-hand motif
CC       inhibits the opening of the channel (By similarity).
CC   -!- PTM: Phosphorylation by PKA activates the channel (By similarity).
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family. CACNA1C subfamily.
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DR   EMBL; L01776; AAB59633.1; -; mRNA.
DR   EMBL; M57973; AAA63291.1; -; mRNA.
DR   EMBL; L06233; AAA37351.1; -; mRNA.
DR   EMBL; U17869; AAA62612.1; -; mRNA.
DR   IPI; IPI00229513; -.
DR   IPI; IPI00277044; -.
DR   IPI; IPI00875159; -.
DR   PIR; A44467; A44467.
DR   RefSeq; NP_001153005.1; NM_001159533.1.
DR   UniGene; Mm.436656; -.
DR   ProteinModelPortal; Q01815; -.
DR   SMR; Q01815; 1560-1640.
DR   IntAct; Q01815; 3.
DR   MINT; MINT-103522; -.
DR   STRING; Q01815; -.
DR   TCDB; 1.A.1.11.6; voltage-gated ion channel (VIC) superfamily.
DR   PhosphoSite; Q01815; -.
DR   PRIDE; Q01815; -.
DR   Ensembl; ENSMUST00000075591; ENSMUSP00000075021; ENSMUSG00000051331.
DR   Ensembl; ENSMUST00000078320; ENSMUSP00000077433; ENSMUSG00000051331.
DR   Ensembl; ENSMUST00000112790; ENSMUSP00000108410; ENSMUSG00000051331.
DR   GeneID; 12288; -.
DR   KEGG; mmu:12288; -.
DR   UCSC; uc009dls.1; mouse.
DR   CTD; 12288; -.
DR   MGI; MGI:103013; Cacna1c.
DR   eggNOG; roNOG09300; -.
DR   GeneTree; ENSGT00590000082785; -.
DR   HOVERGEN; HBG050763; -.
DR   PhylomeDB; Q01815; -.
DR   ArrayExpress; Q01815; -.
DR   Bgee; Q01815; -.
DR   Genevestigator; Q01815; -.
DR   GermOnline; ENSMUSG00000051331; Mus musculus.
DR   GO; GO:0002095; C:caveolar macromolecular signaling complex; IDA:MGI.
DR   GO; GO:0043198; C:dendritic shaft; IDA:MGI.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0030315; C:T-tubule; TAS:MGI.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; TAS:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:MGI.
DR   GO; GO:0007628; P:adult walking behavior; IGI:MGI.
DR   GO; GO:0017156; P:calcium ion-dependent exocytosis; IMP:MGI.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0030252; P:growth hormone secretion; IDA:MGI.
DR   GO; GO:0030073; P:insulin secretion; IMP:MGI.
DR   GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR   GO; GO:0046620; P:regulation of organ growth; IMP:MGI.
DR   GO; GO:0019229; P:regulation of vasoconstriction; IMP:MGI.
DR   GO; GO:0060083; P:smooth muscle contraction involved in micturition; IMP:MGI.
DR   GO; GO:0007268; P:synaptic transmission; IMP:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005451; VDCC_L_a1csu.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   PANTHER; PTHR10037:SF47; LVDCCAlpha1C; 1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
DR   PRINTS; PR01635; LVDCCALPHA1C.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW   Cell membrane; Disulfide bond; Glycoprotein; Ion transport;
KW   Ionic channel; Membrane; Phosphoprotein; Repeat; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1   2139       Voltage-dependent L-type calcium channel
FT                                subunit alpha-1C.
FT                                /FTId=PRO_0000053929.
FT   TOPO_DOM      1    124       Cytoplasmic (Potential).
FT   TRANSMEM    125    143       Helical; Name=S1 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    144    160       Extracellular (Potential).
FT   TRANSMEM    161    181       Helical; Name=S2 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    182    193       Cytoplasmic (Potential).
FT   TRANSMEM    194    212       Helical; Name=S3 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    213    232       Extracellular (Potential).
FT   TRANSMEM    233    251       Helical; Name=S4 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    252    270       Cytoplasmic (Potential).
FT   TRANSMEM    271    290       Helical; Name=S5 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    291    380       Extracellular (Potential).
FT   TRANSMEM    381    405       Helical; Name=S6 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    406    524       Cytoplasmic (Potential).
FT   TRANSMEM    525    543       Helical; Name=S1 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    544    558       Extracellular (Potential).
FT   TRANSMEM    559    578       Helical; Name=S2 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    579    586       Cytoplasmic (Potential).
FT   TRANSMEM    587    605       Helical; Name=S3 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    606    615       Extracellular (Potential).
FT   TRANSMEM    616    634       Helical; Name=S4 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    635    653       Cytoplasmic (Potential).
FT   TRANSMEM    654    673       Helical; Name=S5 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    674    728       Extracellular (Potential).
FT   TRANSMEM    729    753       Helical; Name=S6 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    754    900       Cytoplasmic (Potential).
FT   TRANSMEM    901    919       Helical; Name=S1 of repeat III;
FT                                (Potential).
FT   TOPO_DOM    920    935       Extracellular (Potential).
FT   TRANSMEM    936    955       Helical; Name=S2 of repeat III;
FT                                (Potential).
FT   TOPO_DOM    956    967       Cytoplasmic (Potential).
FT   TRANSMEM    968    986       Helical; Name=S3 of repeat III;
FT                                (Potential).
FT   TOPO_DOM    987    993       Extracellular (Potential).
FT   TRANSMEM    994   1012       Helical; Name=S4 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1013   1031       Cytoplasmic (Potential).
FT   TRANSMEM   1032   1051       Helical; Name=S5 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1052   1141       Extracellular (Potential).
FT   TRANSMEM   1142   1166       Helical; Name=S6 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1167   1219       Cytoplasmic (Potential).
FT   TRANSMEM   1220   1238       Helical; Name=S1 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1239   1253       Extracellular (Potential).
FT   TRANSMEM   1254   1273       Helical; Name=S2 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1274   1281       Cytoplasmic (Potential).
FT   TRANSMEM   1282   1300       Helical; Name=S3 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1301   1324       Extracellular (Potential).
FT   TRANSMEM   1325   1343       Helical; Name=S4 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1344   1362       Cytoplasmic (Potential).
FT   TRANSMEM   1363   1382       Helical; Name=S5 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1383   1451       Extracellular (Potential).
FT   TRANSMEM   1452   1476       Helical; Name=S6 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1477   2139       Cytoplasmic (Potential).
FT   REPEAT      111    408       I.
FT   REPEAT      510    756       II.
FT   REPEAT      887   1169       III.
FT   REPEAT     1206   1479       IV.
FT   CA_BIND    1505   1516       By similarity.
FT   REGION      428    445       Binding to the beta subunit (By
FT                                similarity).
FT   COMPBIAS    654    660       Poly-Leu.
FT   COMPBIAS    768    774       Poly-Glu.
FT   COMPBIAS   1147   1153       Poly-Ile.
FT   SITE        363    363       Calcium ion selectivity and permeability
FT                                (By similarity).
FT   SITE        706    706       Calcium ion selectivity and permeability
FT                                (By similarity).
FT   SITE       1115   1115       Calcium ion selectivity and permeability
FT                                (By similarity).
FT   SITE       1416   1416       Calcium ion selectivity and permeability
FT                                (By similarity).
FT   MOD_RES     815    815       Phosphoserine.
FT   MOD_RES    1487   1487       Phosphoserine; by PKA (Potential).
FT   MOD_RES    1889   1889       Phosphoserine; by PKA (Potential).
FT   MOD_RES    1897   1897       Phosphoserine; by PKA (Potential).
FT   CARBOHYD    153    153       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    328    328       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1388   1388       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1439   1439       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1    264       Missing (in isoform 3).
FT                                /FTId=VSP_000896.
FT   VAR_SEQ     372    391       MQDAMGYELPWVYFVSLVIF -> VNDAVGRDWPWIYFVTL
FT                                III (in isoform 3).
FT                                /FTId=VSP_000897.
FT   VAR_SEQ     464    464       M -> RGAPAGLHDQKKGKFAWFSHSTETHV (in
FT                                isoform 3).
FT                                /FTId=VSP_000898.
FT   VAR_SEQ     932    951       Missing (in isoform 3).
FT                                /FTId=VSP_000899.
FT   VAR_SEQ    1277   1304       GYFSDPWNVFDFLIVIGSIIDVILSETN -> HYFCDAWNT
FT                                FDALIVVGSIVDIAITEVH (in isoform 2).
FT                                /FTId=VSP_000900.
FT   VAR_SEQ    1305   1315       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_000901.
FT   CONFLICT    310    310       E -> K (in Ref. 4; AAA62612).
FT   CONFLICT    477    477       E -> D (in Ref. 4; AAA62612).
FT   CONFLICT    555    555       V -> D (in Ref. 4; AAA62612).
FT   CONFLICT    811    812       AD -> GS (in Ref. 4; AAA62612).
FT   CONFLICT    822    822       N -> H (in Ref. 4; AAA62612).
FT   CONFLICT    825    825       D -> A (in Ref. 4; AAA62612).
FT   CONFLICT    831    831       N -> P (in Ref. 4; AAA62612).
FT   CONFLICT    837    841       HSNPD -> TPTQT (in Ref. 3; AAA37351).
FT   CONFLICT    934    938       GNADY -> FYFDI (in Ref. 3; AAA37351).
FT   CONFLICT    942    942       S -> T (in Ref. 3; AAA37351).
FT   CONFLICT    946    946       L -> I (in Ref. 3; AAA37351).
FT   CONFLICT    949    949       I -> A (in Ref. 3; AAA37351).
FT   CONFLICT    977    978       VS -> LC (in Ref. 4; AAA62612).
FT   CONFLICT   1065   1065       T -> A (in Ref. 4; AAA62612).
FT   CONFLICT   1507   1507       E -> K (in Ref. 4; AAA62612).
FT   CONFLICT   1525   1525       Q -> H (in Ref. 4; AAA62612).
FT   CONFLICT   1633   1633       K -> E (in Ref. 4; AAA62612).
FT   CONFLICT   1959   1959       G -> A (in Ref. 4; AAA62612).
FT   CONFLICT   1963   1964       RP -> ST (in Ref. 4; AAA62612).
FT   CONFLICT   1970   1970       T -> H (in Ref. 4; AAA62612).
FT   CONFLICT   1974   1974       E -> K (in Ref. 4; AAA62612).
FT   CONFLICT   2086   2086       A -> R (in Ref. 4; AAA62612).
FT   CONFLICT   2097   2097       F -> L (in Ref. 4; AAA62612).
FT   CONFLICT   2110   2110       A -> V (in Ref. 4; AAA62612).
SQ   SEQUENCE   2139 AA;  240138 MW;  B564C57A8644E165 CRC64;
     MVNENTRMYV PEENHQGSNY GSPRPAHANM NANAAAGLAP EHIPTPGAAL SWQAAIDAAR
     QAKLMGSAGN ATISTVSSTQ RKRQQYGKPK KQGGTTATRP PRALLCLTLK NPIRRACISI
     VEWKPFEIII LLTIFANCVA LAIYIPFPED DSNATNSNLE RVEYLFLIIF TVEAFLKVIA
     YGLLFHPNAY LRNGWNLLDF IIVVVGLFSA ILEQATKADG ANALGGKGAG FDVKALRAFR
     VLRPLRLVSG VPSLQVVLNS IIKAMVPLLH IALLVLFVII IYAIIGLELF MGKMHKTCYN
     QEGIIDVPAE EDPSPCALET GHGRQCQNGT VCKPGWDGPK HGITNFDNFA FAMLTVFQCI
     TMEGWTDVLY WMQDAMGYEL PWVYFVSLVI FGSFFVLNLV LGVLSGEFSK EREKAKARGD
     FQKLREKQQL EEDLKGYLDW ITQAEDIDPE NEDEGMDEDK PRNMSMPTSE TESVNTENVA
     GGDIEGENCG ARLAHRISKS KFSRYWRRWN RFCRRKCRAA VKSNVFYWLV IFLVFLNTLT
     IASEHYNQPH WLTEVQDTAN KALLALFTAE MLLKMYSLGL QAYFVSLFNR FDCFIVCGGI
     LETILVETKI MSPLGISVLR CVRLLRIFKI TRYWNSLSNL VASLLNSVRS IASLLLLLFL
     FIIIFSLLGM QLFGGKFNFD EMQTRRSTFD NFPQSLLTVF QILTGEDWNS VMYDGIMAYG
     GPSFPGMLVC IYFIILFICG NYILLNVFLA IAVDNLADAE SLTSAQKEEE EEKERKKLAR
     TASPEKKQEV MEKPAVEESK EEKIELKSIT ADGESPPTTK INMDDLQPSE NEDKSPHSNP
     DTAGEEDEEE PEMPVGPRPR PLSELHLKEK AVPMPEASAF FIFSPNNRFR LQCHRIVNDT
     IFTNLILFFI LLSSISLAAE DPVQHTSFRN HILGNADYVF TSIFTLEIIL KMTAYGAFLH
     KGSFCRNYFN ILDLLVVSVS LISFGIQSSA INVVKILRVL RVLRPLRAIN RAKGLKHVVQ
     CVFVAIRTIG NIVIVTTLLQ FMFACIGVQL FKGKLYTCSD SSKQTEAECK GNYITYKDGE
     VDHPIIQPRS WENSKFDFDN VLAAMMALFT VSTFEGWPEL LYRSIDSHTE DKGPIYNYRV
     EISIFFIIYI IIIAFFMMNI FVGFVIVTFQ EQGEQEYKNC ELDKNQRQCV EYALKARPLR
     RYIPKNQHQY KVWYVVNSTY FEYLMFVLIL LNTICLAMQH YGQSCLFKIA MNILNMLFTG
     LFTVEMILKL IAFKPKGYFS DPWNVFDFLI VIGSIIDVIL SETNPAEHTQ CSPSMSAEEN
     SRISITFFRL FRVMRLVKLL SRGEGIRTLL WTFIKSFQAL PYVALLIVML FFIYAVIGMQ
     VFGKIALNDT TEINRNNNFQ TFPQAVLLLF RCATGEAWQD IMLACMPGKK CAPESEPSNS
     TEGETPCGSS FAVFYFISFY MLCAFLIINL FVAVIMDNFD YLTRDWSILG PHHLDEFKRI
     WAEYDPEAKG RIKHLDVVTL LRRIQPPLGF GKLCPHRVAC KRLVSMNMPL NSDGTVMFNA
     TLFALVRTAL RIKTEGNLEQ ANEELRAIIK KIWKRTSMKL LDQVVPPAGD DEVTVGKFYA
     TFLIQEYFRK FKKRKEQGLV GKPSQRNALS LQAGLRTLHD IGPEIRRAIS GDLTAEEELD
     KAMKEAVSAA SEDDIFRRAG GLFGNHVTYY QSDSRGNFPQ TFATQRPLHI NKTGNNQADT
     ESPSHEKLVD STFTPSSYSS TGSNANINNA NNTALGRFPH PAGYSSTVST VEGHGPPLSP
     AVRVQEAAWK LSSKRCHSRE SQGATVNQEI FPDETRSVRM SEEAEYCSEP SLLSTDMFSY
     QEDEHRQLTC PEEDKREIQP SPKRSFLRSA SLGRRASFHL ECLKRQKDQG GDISQKTALP
     LHLVHHQALA VAGLSPLLQR SHSPTTFPRP CPTPPVTPGS RGRPLRPIPT LRLEGAESSE
     KLNSSFPSIH CSSWSEETTA CSGSSSMARR ARPVSLTVPS QAGAPGRQFH GSASSLVEAV
     LISEGLGQFA QDPKFIEVTT QELADACDMT IEEMENAADN ILSGGAQQSP NGTLLPFVNC
     RDPGQDRAVA PEDESCAYAL GRGRSEEALA DSRSYVSNL
//
ID   TERA_MOUSE              Reviewed;         806 AA.
AC   Q01853; Q3TFH9; Q3TIM2; Q3TXN9; Q6PI18; Q8BSR6; Q8CEG4;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 4.
DT   08-MAR-2011, entry version 117.
DE   RecName: Full=Transitional endoplasmic reticulum ATPase;
DE            Short=TER ATPase;
DE   AltName: Full=15S Mg(2+)-ATPase p97 subunit;
DE   AltName: Full=Valosin-containing protein;
DE            Short=VCP;
GN   Name=Vcp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 20-40; 295-309 AND
RP   425-438.
RC   STRAIN=MRL/LPR;
RX   MEDLINE=93010943; PubMed=1382975;
RA   Egerton M., Ashe O.R., Chen D., Druker B.J., Burgess W.H.,
RA   Samelson L.E.;
RT   "VCP, the mammalian homolog of cdc48, is tyrosine phosphorylated in
RT   response to T cell antigen receptor activation.";
RL   EMBO J. 11:3533-3540(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, and C57BL/6J; TISSUE=Bone marrow, Head, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 9-18; 26-53; 87-93; 96-109; 148-155; 192-210;
RP   218-231; 240-251; 278-287; 296-312; 324-336; 363-386; 454-502;
RP   513-524; 530-560; 600-614; 639-651; 669-677; 701-709; 714-732 AND
RP   754-766, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [6]
RP   INTERACTION WITH RNF19A.
RX   PubMed=15456787; DOI=10.1074/jbc.M406683200;
RA   Ishigaki S., Hishikawa N., Niwa J., Iemura S., Natsume T., Hori S.,
RA   Kakizuka A., Tanaka K., Sobue G.;
RT   "Physical and functional interaction between dorfin and valosin-
RT   containing protein that are colocalized in ubiquitylated inclusions in
RT   neurodegenerative disorders.";
RL   J. Biol. Chem. 279:51376-51385(2004).
RN   [7]
RP   ISGYLATION.
RX   PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA   Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA   Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT   "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT   human cells.";
RL   Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN   [8]
RP   INTERACTION WITH NGLY1.
RX   PubMed=16249333; DOI=10.1073/pnas.0507155102;
RA   Li G., Zhou X., Zhao G., Schindelin H., Lennarz W.J.;
RT   "Multiple modes of interaction of the deglycosylation enzyme, mouse
RT   peptide N-glycanase, with the proteasome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:15809-15814(2005).
RN   [9]
RP   ERRATUM.
RA   Li G., Zhou X., Zhao G., Schindelin H., Lennarz W.J.;
RL   Proc. Natl. Acad. Sci. U.S.A. 103:1153-1153(2006).
RN   [10]
RP   INTERACTION WITH NSFL1C-LIKE PROTEIN P37.
RX   PubMed=17141156; DOI=10.1016/j.devcel.2006.10.016;
RA   Uchiyama K., Totsukawa G., Puhka M., Kaneko Y., Jokitalo E.,
RA   Dreveny I., Beuron F., Zhang X., Freemont P., Kondo H.;
RT   "p37 is a p97 adaptor required for Golgi and ER biogenesis in
RT   interphase and at the end of mitosis.";
RL   Dev. Cell 11:803-816(2006).
RN   [11]
RP   PHOSPHOLIPID BINDING, AND MUTAGENESIS OF ARG-144.
RX   PubMed=17018057; DOI=10.1111/j.1742-4658.2006.05494.x;
RA   Shiozawa K., Goda N., Shimizu T., Mizuguchi K., Kondo N.,
RA   Shimozawa N., Shirakawa M., Hiroaki H.;
RT   "The common phospholipid-binding activity of the N-terminal domains of
RT   PEX1 and VCP/p97.";
RL   FEBS J. 273:4959-4971(2006).
RN   [12]
RP   INTERACTION WITH AMFR; SAKS1; RAD23B AND NGLY1.
RX   PubMed=16709668; DOI=10.1073/pnas.0602747103;
RA   Li G., Zhao G., Zhou X., Schindelin H., Lennarz W.J.;
RT   "The AAA ATPase p97 links peptide N-glycanase to the endoplasmic
RT   reticulum-associated E3 ligase autocrine motility factor receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:8348-8353(2006).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-458.
RX   MEDLINE=21111055; PubMed=11163219; DOI=10.1016/S1097-2765(00)00143-X;
RA   Zhang X., Shaw A., Bates P.A., Newman R.H., Gowen B., Orlova E.,
RA   Gorman M.A., Kondo H., Dokurno P., Lally J., Leonard G., Meyer H.,
RA   van Heel M., Freemont P.S.;
RT   "Structure of the AAA ATPase p97.";
RL   Mol. Cell 6:1473-1484(2000).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (4.7 ANGSTROMS).
RX   PubMed=12949490; DOI=10.1038/nsb972;
RA   DeLaBarre B., Brunger A.T.;
RT   "Complete structure of p97/valosin-containing protein reveals
RT   communication between nucleotide domains.";
RL   Nat. Struct. Biol. 10:856-863(2003).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS).
RX   PubMed=14643202; DOI=10.1016/j.jsb.2003.10.007;
RA   Huyton T., Pye V.E., Briggs L.C., Flynn T.C., Beuron F., Kondo H.,
RA   Ma J., Zhang X., Freemont P.S.;
RT   "The crystal structure of murine p97/VCP at 3.6A.";
RL   J. Struct. Biol. 144:337-348(2003).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 1-458.
RX   PubMed=14988733; DOI=10.1038/sj.emboj.7600139;
RA   Dreveny I., Kondo H., Uchiyama K., Shaw A., Zhang X., Freemont P.S.;
RT   "Structural basis of the interaction between the AAA ATPase p97/VCP
RT   and its adaptor protein p47.";
RL   EMBO J. 23:1030-1039(2004).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX   PubMed=15740751; DOI=10.1016/j.jmb.2005.01.060;
RA   DeLaBarre B., Brunger A.T.;
RT   "Nucleotide dependent motion and mechanism of action of p97/VCP.";
RL   J. Mol. Biol. 347:437-452(2005).
CC   -!- FUNCTION: Necessary for the fragmentation of Golgi stacks during
CC       mitosis and for their reassembly after mitosis. Involved in the
CC       formation of the transitional endoplasmic reticulum (tER). The
CC       transfer of membranes from the endoplasmic reticulum to the Golgi
CC       apparatus occurs via 50-70 nm transition vesicles which derive
CC       from part-rough, part-smooth transitional elements of the
CC       endoplasmic reticulum (tER). Vesicle budding from the tER is an
CC       ATP-dependent process. The ternary complex containing UFD1L, VCP
CC       and NPLOC4 binds ubiquitinated proteins and is necessary for the
CC       export of misfolded proteins from the ER to the cytoplasm, where
CC       they are degraded by the proteasome. The NPLOC4-UFD1L-VCP complex
CC       regulates spindle disassembly at the end of mitosis and is
CC       necessary for the formation of a closed nuclear envelope.
CC       Regulates E3 ubiquitin-protein ligase activity of RNF19A (By
CC       similarity).
CC   -!- SUBUNIT: Homohexamer. Forms a ring-shaped particle of 12.5 nm
CC       diameter, that displays 6-fold radial symmetry. Part of a ternary
CC       complex containing STX5A, NSFL1C and VCP. NSFL1C forms a
CC       homotrimer that binds to one end of a VCP homohexamer. The complex
CC       binds to membranes enriched in phosphatidylethanolamine-containing
CC       lipids and promotes Golgi membrane fusion. Binds to a heterodimer
CC       of NPLOC4 and UFD1L, binding to this heterodimer inhibits Golgi-
CC       membrane fusion. Interaction with VCIP135 leads to dissociation of
CC       the complex via ATP hydrolysis by VCP. Part of a ternary complex
CC       containing NPLOC4, UFD1L and VCP (By similarity). Interacts with
CC       SELS/VIMP and SYVN1, as well as with DERL1, DERL2 and DERL3; which
CC       probably transfer misfolded proteins from the ER to VCP. Interacts
CC       with SVIP (By similarity). Component of a complex required to
CC       couple retrotranslocation, ubiquitination and deglycosylation
CC       composed of NGLY1, SAKS1, AMFR, VCP and RAD23B. Directly interacts
CC       with UBXD2. Interacts with CASR (By similarity). Interacts with
CC       NSFL1C-like protein p37; the complex has membrane fusion activity
CC       and is required for Golgi and endoplasmic reticulum biogenesis.
CC       Interacts with UBXN6, UBE4B and YOD1. Interacts with clathrin (By
CC       similarity). Interacts with RNF103 (By similarity). Interacts with
CC       TRIM13 and TRIM21 (By similarity).
CC   -!- INTERACTION:
CC       Q9CVD2:Atxn3; NbExp=1; IntAct=EBI-80597, EBI-1784669;
CC       Q9BQE4:SELS (xeno); NbExp=3; IntAct=EBI-80597, EBI-398970;
CC       Q9ES00:Ube4b; NbExp=1; IntAct=EBI-80597, EBI-80579;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus.
CC   -!- DOMAIN: The N-terminal domain shows evolutionary conservation with
CC       that of PEX1, and is able to bind phospholipids with a preference
CC       for phosphatidylinositol mono- and biphosphates.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity). Phosphorylated by tyrosine kinases in response to T-
CC       cell antigen receptor activation.
CC   -!- PTM: ISGylated.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
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DR   EMBL; Z14044; CAA78412.1; -; mRNA.
DR   EMBL; AK028264; BAC25849.1; -; mRNA.
DR   EMBL; AK030751; BAC27119.1; -; mRNA.
DR   EMBL; AK149931; BAE29175.1; -; mRNA.
DR   EMBL; AK151109; BAE30119.1; -; mRNA.
DR   EMBL; AK151418; BAE30383.1; -; mRNA.
DR   EMBL; AK153249; BAE31840.1; -; mRNA.
DR   EMBL; AK159177; BAE34876.1; -; mRNA.
DR   EMBL; AK159509; BAE35141.1; -; mRNA.
DR   EMBL; AK167794; BAE39824.1; -; mRNA.
DR   EMBL; AK169140; BAE40919.1; -; mRNA.
DR   EMBL; AL672276; CAM14316.1; -; Genomic_DNA.
DR   EMBL; BC043053; AAH43053.1; -; mRNA.
DR   EMBL; BC049114; AAH49114.1; -; mRNA.
DR   IPI; IPI00622235; -.
DR   PIR; S25197; S25197.
DR   RefSeq; NP_033529.3; NM_009503.4.
DR   UniGene; Mm.245976; -.
DR   UniGene; Mm.262053; -.
DR   PDB; 1E32; X-ray; 2.90 A; A=1-458.
DR   PDB; 1R7R; X-ray; 3.60 A; A=1-806.
DR   PDB; 1S3S; X-ray; 2.90 A; A/B/C/D/E/F=1-458.
DR   PDB; 2PJH; NMR; -; B=21-213.
DR   PDB; 3CF0; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=463-763.
DR   PDB; 3CF1; X-ray; 4.40 A; A/B/C=1-806.
DR   PDB; 3CF2; X-ray; 3.50 A; A/B/C/D=1-806.
DR   PDB; 3CF3; X-ray; 4.25 A; A/B/C=1-806.
DR   PDBsum; 1E32; -.
DR   PDBsum; 1R7R; -.
DR   PDBsum; 1S3S; -.
DR   PDBsum; 2PJH; -.
DR   PDBsum; 3CF0; -.
DR   PDBsum; 3CF1; -.
DR   PDBsum; 3CF2; -.
DR   PDBsum; 3CF3; -.
DR   ProteinModelPortal; Q01853; -.
DR   SMR; Q01853; 17-763.
DR   DisProt; DP00435; -.
DR   DIP; DIP-29796N; -.
DR   IntAct; Q01853; 21.
DR   MINT; MINT-220770; -.
DR   STRING; Q01853; -.
DR   PhosphoSite; Q01853; -.
DR   REPRODUCTION-2DPAGE; Q01853; -.
DR   UCD-2DPAGE; Q01853; -.
DR   PRIDE; Q01853; -.
DR   Ensembl; ENSMUST00000030164; ENSMUSP00000030164; ENSMUSG00000028452.
DR   GeneID; 269523; -.
DR   KEGG; mmu:269523; -.
DR   CTD; 269523; -.
DR   MGI; MGI:99919; Vcp.
DR   eggNOG; roNOG06583; -.
DR   HOVERGEN; HBG001226; -.
DR   InParanoid; Q01853; -.
DR   OMA; YLAKVTH; -.
DR   OrthoDB; EOG45TCMK; -.
DR   PhylomeDB; Q01853; -.
DR   NextBio; 392876; -.
DR   ArrayExpress; Q01853; -.
DR   Bgee; Q01853; -.
DR   CleanEx; MM_VCP; -.
DR   Genevestigator; Q01853; -.
DR   GermOnline; ENSMUSG00000028452; Mus musculus.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0031593; F:polyubiquitin binding; IDA:BHF-UCL.
DR   GO; GO:0006919; P:activation of caspase activity; IDA:MGI.
DR   GO; GO:0070842; P:aggresome assembly; IGI:MGI.
DR   GO; GO:0030970; P:retrograde protein transport, ER to cytosol; ISS:UniProtKB.
DR   InterPro; IPR009010; Asp_de-COase-like_fold.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR005938; ATPase_AAA_CDC48.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR003338; ATPase_AAA_VAT_N.
DR   InterPro; IPR004201; Cell_division_protein_CDC48_2.
DR   InterPro; IPR015415; Vps4_C.
DR   Gene3D; G3DSA:2.40.40.20; Asp_decarboxylase-like_fold; 1.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF02933; CDC48_2; 1.
DR   Pfam; PF02359; CDC48_N; 1.
DR   Pfam; PF09336; Vps4_C; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF50692; Asp_decarb_fold; 1.
DR   TIGRFAMs; TIGR01243; CDC48; 1.
DR   PROSITE; PS00674; AAA; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Cytoplasm;
KW   Direct protein sequencing; Hydrolase; Lipid-binding;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Transport;
KW   Ubl conjugation; Ubl conjugation pathway.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    806       Transitional endoplasmic reticulum
FT                                ATPase.
FT                                /FTId=PRO_0000084573.
FT   NP_BIND     245    252       ATP (Potential).
FT   NP_BIND     518    525       ATP (Potential).
FT   REGION      797    806       Interaction with UBXN6 (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       3      3       Phosphoserine (By similarity).
FT   MOD_RES       7      7       Phosphoserine.
FT   MOD_RES      37     37       Phosphoserine (By similarity).
FT   MOD_RES     282    282       Phosphoserine (By similarity).
FT   MOD_RES     284    284       Phosphoserine (By similarity).
FT   MOD_RES     436    436       Phosphothreonine (By similarity).
FT   MOD_RES     457    457       Phosphoserine (By similarity).
FT   MOD_RES     509    509       Phosphothreonine (By similarity).
FT   MOD_RES     702    702       Phosphoserine (By similarity).
FT   MOD_RES     705    705       Phosphoserine (By similarity).
FT   MOD_RES     746    746       Phosphoserine (By similarity).
FT   MOD_RES     748    748       Phosphoserine (By similarity).
FT   MOD_RES     770    770       Phosphoserine (By similarity).
FT   MOD_RES     775    775       Phosphoserine (By similarity).
FT   MOD_RES     784    784       Phosphoserine (By similarity).
FT   MOD_RES     787    787       Phosphoserine (By similarity).
FT   MOD_RES     805    805       Phosphotyrosine (By similarity).
FT   MUTAGEN     144    144       R->A: Loss of phospholipid-binding.
FT   CONFLICT     73     73       S -> Y (in Ref. 2; BAC27119).
FT   CONFLICT    199    199       N -> Y (in Ref. 2; BAE39824).
FT   CONFLICT    206    206       I -> V (in Ref. 1; CAA78412).
FT   CONFLICT    359    359       R -> Q (in Ref. 2; BAC27119).
FT   CONFLICT    439    439       A -> T (in Ref. 2; BAE40919).
FT   CONFLICT    624    624       N -> S (in Ref. 2; BAE34876).
FT   CONFLICT    684    684       G -> V (in Ref. 2; BAC25849).
FT   STRAND       25     29
FT   STRAND       38     41
FT   HELIX        43     48
FT   STRAND       56     60
FT   STRAND       66     73
FT   STRAND       79     83
FT   HELIX        86     91
FT   STRAND       99    104
FT   STRAND      114    119
FT   HELIX       120    122
FT   TURN        123    125
FT   HELIX       130    133
FT   HELIX       135    139
FT   STRAND      144    147
FT   STRAND      151    156
FT   STRAND      159    176
FT   HELIX       203    205
FT   HELIX       211    225
FT   HELIX       227    232
FT   STRAND      240    244
FT   HELIX       251    261
FT   STRAND      265    269
FT   HELIX       271    274
FT   HELIX       281    295
FT   STRAND      298    305
FT   HELIX       306    308
FT   HELIX       312    315
FT   HELIX       321    333
FT   STRAND      341    348
FT   HELIX       350    352
FT   HELIX       355    357
FT   STRAND      365    368
FT   HELIX       374    383
FT   TURN        384    387
FT   HELIX       396    402
FT   HELIX       408    430
FT   HELIX       439    444
FT   HELIX       449    456
FT   HELIX       476    478
FT   HELIX       483    498
FT   HELIX       500    506
FT   STRAND      512    517
FT   STRAND      519    523
FT   HELIX       524    534
FT   STRAND      538    542
FT   HELIX       544    552
FT   HELIX       558    568
FT   STRAND      571    576
FT   HELIX       581    585
FT   TURN        586    590
FT   HELIX       599    609
FT   STRAND      615    624
FT   HELIX       626    628
FT   HELIX       631    634
FT   STRAND      641    644
FT   HELIX       650    661
FT   HELIX       672    677
FT   HELIX       684    706
FT   HELIX       733    740
FT   HELIX       749    762
SQ   SEQUENCE   806 AA;  89322 MW;  501B721D3A77BA8A CRC64;
     MASGADSKGD DLSTAILKQK NRPNRLIVDE AINEDNSVVS LSQPKMDELQ LFRGDTVLLK
     GKKRREAVCI VLSDDTCSDE KIRMNRVVRN NLRVRLGDVI SIQPCPDVKY GKRIHVLPID
     DTVEGITGNL FEVYLKPYFL EAYRPIRKGD IFLVRGGMRA VEFKVVETDP SPYCIVAPDT
     VIHCEGEPIK REDEEESLNE VGYDDIGGCR KQLAQIKEMV ELPLRHPALF KAIGVKPPRG
     ILLYGPPGTG KTLIARAVAN ETGAFFFLIN GPEIMSKLAG ESESNLRKAF EEAEKNAPAI
     IFIDELDAIA PKREKTHGEV ERRIVSQLLT LMDGLKQRAH VIVMAATNRP NSIDPALRRF
     GRFDREVDIG IPDATGRLEI LQIHTKNMKL ADDVDLEQVA NETHGHVGAD LAALCSEAAL
     QAIRKKMDLI DLEDETIDAE VMNSLAVTMD DFRWALSQSN PSALRETVVE VPQVTWEDIG
     GLEDVKRELQ ELVQYPVEHP DKFLKFGMTP SKGVLFYGPP GCGKTLLAKA IANECQANFI
     SIKGPELLTM WFGESEANVR EIFDKARQAA PCVLFFDELD SIAKARGGNI GDGGGAADRV
     INQILTEMDG MSTKKNVFII GATNRPDIID PAILRPGRLD QLIYIPLPDE KSRVAILKAN
     LRKSPVAKDV DLEFLAKMTN GFSGADLTEI CQRACKLAIR ESIESEIRRE RERQTNPSAM
     EVEEDDPVPE IRRDHFEEAM RFARRSVSDN DIRKYEMFAQ TLQQSRGFGS FRFPSGNQGG
     AGPSQGSGGG TGGSVYTEDN DDDLYG
//
ID   AQP1_MOUSE              Reviewed;         269 AA.
AC   Q02013; Q542P1; Q91VY8;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 101.
DE   RecName: Full=Aquaporin-1;
DE            Short=AQP-1;
DE   AltName: Full=Aquaporin-CHIP;
DE   AltName: Full=Delayed early response protein 2;
DE            Short=DER2;
DE   AltName: Full=Water channel protein for red blood cells and kidney proximal tubule;
GN   Name=Aqp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=92375060; PubMed=1508193;
RA   Lanahan A.A., Williams J.B., Sanders L.K., Nathans D.;
RT   "Growth factor-induced delayed early response genes.";
RL   Mol. Cell. Biol. 12:3919-3929(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Head, Inner ear, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-246 AND SER-247, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Forms a water-specific channel that provides the plasma
CC       membranes of red cells and kidney proximal tubules with high
CC       permeability to water, thereby permitting water to move in the
CC       direction of an osmotic gradient.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Erythrocytes and renal tubules.
CC   -!- DOMAIN: Aquaporins contain two tandem repeats each containing
CC       three membrane-spanning domains and a pore-forming loop with the
CC       signature motif Asn-Pro-Ala (NPA).
CC   -!- MISCELLANEOUS: Pharmacologically inhibited by submillimolar
CC       concentrations of mercury.
CC   -!- SIMILARITY: Belongs to the MIP/aquaporin (TC 1.A.8) family.
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DR   EMBL; L02914; AAB53928.1; -; mRNA.
DR   EMBL; AK081886; BAC38360.1; -; mRNA.
DR   EMBL; AK086688; BAC39719.1; -; mRNA.
DR   EMBL; AK157333; BAE34051.1; -; mRNA.
DR   EMBL; AK158226; BAE34412.1; -; mRNA.
DR   EMBL; AK158389; BAE34482.1; -; mRNA.
DR   EMBL; AK171627; BAE42573.1; -; mRNA.
DR   EMBL; AK172361; BAE42966.1; -; mRNA.
DR   EMBL; BC007125; AAH07125.1; -; mRNA.
DR   IPI; IPI00123183; -.
DR   PIR; B44499; B44499.
DR   RefSeq; NP_031498.1; NM_007472.2.
DR   UniGene; Mm.18625; -.
DR   ProteinModelPortal; Q02013; -.
DR   SMR; Q02013; 9-233.
DR   STRING; Q02013; -.
DR   PhosphoSite; Q02013; -.
DR   Ensembl; ENSMUST00000004774; ENSMUSP00000004774; ENSMUSG00000004655.
DR   GeneID; 11826; -.
DR   KEGG; mmu:11826; -.
DR   UCSC; uc009caq.1; mouse.
DR   CTD; 11826; -.
DR   MGI; MGI:103201; Aqp1.
DR   eggNOG; roNOG11397; -.
DR   HOGENOM; HBG705794; -.
DR   HOVERGEN; HBG000312; -.
DR   InParanoid; Q02013; -.
DR   OMA; PLERNQT; -.
DR   OrthoDB; EOG46T328; -.
DR   PhylomeDB; Q02013; -.
DR   NextBio; 279727; -.
DR   ArrayExpress; Q02013; -.
DR   Bgee; Q02013; -.
DR   CleanEx; MM_AQP1; -.
DR   Genevestigator; Q02013; -.
DR   GermOnline; ENSMUSG00000004655; Mus musculus.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:MGI.
DR   GO; GO:0000299; C:integral to membrane of membrane fraction; IDA:MGI.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:MGI.
DR   GO; GO:0020003; C:symbiont-containing vacuole; IDA:UniProtKB.
DR   GO; GO:0015079; F:potassium ion transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015250; F:water channel activity; TAS:MGI.
DR   GO; GO:0051458; P:adrenocorticotropin secretion; IMP:MGI.
DR   GO; GO:0048593; P:camera-type eye morphogenesis; IMP:MGI.
DR   GO; GO:0003094; P:glomerular filtration; IMP:MGI.
DR   GO; GO:0021670; P:lateral ventricle development; IEP:UniProtKB.
DR   GO; GO:0044241; P:lipid digestion; IMP:MGI.
DR   GO; GO:0085018; P:maintenance of symbiont-containing vacuole via substance secreted by host; IMP:UniProtKB.
DR   GO; GO:0072220; P:metanephric descending thin limb development; IEP:UniProtKB.
DR   GO; GO:0072239; P:metanephric glomerulus vasculature development; IEP:UniProtKB.
DR   GO; GO:0072230; P:metanephric proximal straight tubule development; IEP:UniProtKB.
DR   GO; GO:0072232; P:metanephric S2 development; IEP:UniProtKB.
DR   GO; GO:0070295; P:renal water absorption; IMP:MGI.
DR   GO; GO:0033363; P:secretory granule organization; IMP:MGI.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR   GO; GO:0042060; P:wound healing; IMP:MGI.
DR   InterPro; IPR012269; Aquaporin.
DR   InterPro; IPR023274; Aquaporin_1.
DR   InterPro; IPR023271; Aquaporin_like.
DR   InterPro; IPR000425; MIP.
DR   InterPro; IPR022357; MIP_CS.
DR   Gene3D; G3DSA:1.20.1080.10; MIP; 1.
DR   PANTHER; PTHR19139; MIP; 1.
DR   Pfam; PF00230; MIP; 1.
DR   PRINTS; PR02013; AQUAPORIN1.
DR   PRINTS; PR00783; MINTRINSICP.
DR   SUPFAM; SSF81338; MIP; 1.
DR   TIGRFAMs; TIGR00861; MIP; 1.
DR   PROSITE; PS00221; MIP; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Phosphoprotein; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    269       Aquaporin-1.
FT                                /FTId=PRO_0000063921.
FT   TOPO_DOM      2      7       Cytoplasmic (By similarity).
FT   TRANSMEM      8     36       Helical; Name=Helix 1; (By similarity).
FT   TOPO_DOM     37     48       Extracellular (By similarity).
FT   TRANSMEM     49     66       Helical; Name=Helix 2; (By similarity).
FT   TOPO_DOM     67     70       Cytoplasmic (By similarity).
FT   INTRAMEM     71     76       By similarity.
FT   INTRAMEM     77     84       Helical; Name=Helix B; (By similarity).
FT   TOPO_DOM     85     94       Cytoplasmic (By similarity).
FT   TRANSMEM     95    115       Helical; Name=Helix 3; (By similarity).
FT   TOPO_DOM    116    136       Extracellular (By similarity).
FT   TRANSMEM    137    155       Helical; Name=Helix 4; (By similarity).
FT   TOPO_DOM    156    166       Cytoplasmic (By similarity).
FT   TRANSMEM    167    183       Helical; Name=Helix 5; (By similarity).
FT   TOPO_DOM    184    186       Extracellular (By similarity).
FT   INTRAMEM    187    192       By similarity.
FT   INTRAMEM    193    200       Helical; Name=Helix E; (By similarity).
FT   TOPO_DOM    201    207       Extracellular (By similarity).
FT   TRANSMEM    208    228       Helical; Name=Helix 6; (By similarity).
FT   TOPO_DOM    229    269       Cytoplasmic (By similarity).
FT   MOTIF        76     78       NPA 1.
FT   MOTIF       192    194       NPA 2.
FT   COMPBIAS    159    162       Poly-Arg.
FT   SITE         56     56       Substrate discrimination (By similarity).
FT   SITE        180    180       Substrate discrimination (By similarity).
FT   SITE        189    189       Hg(2+)-sensitive residue (By similarity).
FT   SITE        195    195       Substrate discrimination (By similarity).
FT   MOD_RES     246    246       Phosphothreonine.
FT   MOD_RES     247    247       Phosphoserine.
FT   MOD_RES     262    262       Phosphoserine.
FT   CARBOHYD    205    205       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    190    190       G -> S (in Ref. 3; AAH07125).
SQ   SEQUENCE   269 AA;  28793 MW;  F0499724AD4AB5F6 CRC64;
     MASEIKKKLF WRAVVAEFLA MTLFVFISIG SALGFNYPLE RNQTLVQDNV KVSLAFGLSI
     ATLAQSVGHI SGAHLNPAVT LGLLLSCQIS ILRAVMYIIA QCVGAIVATA ILSGITSSLV
     DNSLGRNDLA HGVNSGQGLG IEIIGTLQLV LCVLATTDRR RRDLGGSAPL AIGLSVALGH
     LLAIDYTGCG INPARSFGSA VLTRNFSNHW IFWVGPFIGG ALAVLIYDFI LAPRSSDFTD
     RMKVWTSGQV EEYDLDADDI NSRVEMKPK
//
ID   UBA1_MOUSE              Reviewed;        1058 AA.
AC   Q02053; A6H6S6; P31253; Q542H8;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   08-MAR-2011, entry version 122.
DE   RecName: Full=Ubiquitin-like modifier-activating enzyme 1;
DE   AltName: Full=Ubiquitin-activating enzyme E1;
DE   AltName: Full=Ubiquitin-activating enzyme E1 X;
DE   AltName: Full=Ubiquitin-like modifier-activating enzyme 1 X;
GN   Name=Uba1; Synonyms=Sbx, Ube1, Ube1ax, Ube1x;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92380515; PubMed=1511901; DOI=10.1016/0378-1119(92)90200-9;
RA   Imai N., Kaneda S., Nagai Y., Seno T., Ayusawa D., Hanaoka F.,
RA   Yamao F.;
RT   "Cloning and sequence of a functionally active cDNA encoding the mouse
RT   ubiquitin-activating enzyme E1.";
RL   Gene 118:279-282(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Ovary, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 69-81; 90-97; 175-182; 227-239; 351-368; 375-384;
RP   386-411; 451-465; 471-485; 538-551; 559-581; 593-604; 636-671;
RP   679-693; 785-802; 844-851; 870-880; 890-923; 945-980 AND 1011-1021,
RP   AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 615-1058.
RC   STRAIN=129/Sv;
RX   MEDLINE=92086048; PubMed=1684224; DOI=10.1038/354483a0;
RA   Mitchell M.J., Woods D.R., Tucker P.K., Opp J.S., Bishop C.E.;
RT   "Homology of a candidate spermatogenic gene from the mouse Y
RT   chromosome to the ubiquitin-activating enzyme E1.";
RL   Nature 354:483-487(1991).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 655-763.
RC   STRAIN=BALB/c AnCr, and Lewis; TISSUE=Liver;
RX   MEDLINE=95230700; PubMed=7714913; DOI=10.1007/BF00166597;
RA   Chang B.H.-J., Li W.H.;
RT   "Estimating the intensity of male-driven evolution in rodents by using
RT   X-linked and Y-linked Ube 1 genes and pseudogenes.";
RL   J. Mol. Evol. 40:70-77(1995).
RN   [8]
RP   REGULATION OF EXPRESSION BY THE THYROID HORMONE RECEPTOR.
RX   MEDLINE=95023181; PubMed=7937138; DOI=10.1093/nar/22.20.4132;
RA   Caubin J., Iglesias T., Bernal J., Munoz A., Marquez G., Barbero J.L.,
RA   Zaballos A.;
RT   "Isolation of genomic DNA fragments corresponding to genes modulated
RT   in vivo by a transcription factor.";
RL   Nucleic Acids Res. 22:4132-4138(1994).
RN   [9]
RP   ISGYLATION.
RX   PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA   Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA   Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT   "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT   human cells.";
RL   Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-55, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-24; SER-31;
RP   SER-816; SER-820 AND SER-835, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 626-891.
RX   PubMed=15774460; DOI=10.1074/jbc.M502583200;
RA   Szczepanowski R.H., Filipek R., Bochtler M.;
RT   "Crystal structure of a fragment of mouse ubiquitin-activating
RT   enzyme.";
RL   J. Biol. Chem. 280:22006-22011(2005).
CC   -!- FUNCTION: Activates ubiquitin by first adenylating its C-terminal
CC       glycine residue with ATP, and thereafter linking this residue to
CC       the side chain of a cysteine residue in E1, yielding an ubiquitin-
CC       E1 thioester and free AMP.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Monomer. Interacts with GAN (via BTB domain).
CC   -!- INDUCTION: May be modulated by the thyroid hormone receptor.
CC   -!- PTM: ISGylated.
CC   -!- MISCELLANEOUS: There are two active sites within the E1 molecule,
CC       allowing it to accommodate two ubiquitin moieties at a time, with
CC       a new ubiquitin forming an adenylate intermediate as the previous
CC       one is transferred to the thiol site.
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA44465.1; Type=Frameshift; Positions=1033;
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DR   EMBL; D10576; BAA01433.1; -; mRNA.
DR   EMBL; AK088057; BAC40121.1; -; mRNA.
DR   EMBL; AK088528; BAC40405.1; -; mRNA.
DR   EMBL; AK143416; BAE25369.1; -; mRNA.
DR   EMBL; AK171667; BAE42599.1; -; mRNA.
DR   EMBL; AL807240; CAM23092.1; -; Genomic_DNA.
DR   EMBL; BC058630; AAH58630.1; -; mRNA.
DR   EMBL; BC145984; AAI45985.1; -; mRNA.
DR   EMBL; X62580; CAA44465.1; ALT_FRAME; mRNA.
DR   EMBL; U09051; AAC52169.1; -; Genomic_DNA.
DR   EMBL; U09055; AAC52171.1; -; Genomic_DNA.
DR   IPI; IPI00123313; -.
DR   PIR; I48756; I48756.
DR   PIR; I63168; I63168.
DR   PIR; JC1254; JC1254.
DR   RefSeq; NP_001129557.1; NM_001136085.1.
DR   RefSeq; NP_033483.1; NM_009457.3.
DR   UniGene; Mm.1104; -.
DR   PDB; 1Z7L; X-ray; 2.80 A; A/B/C=626-891.
DR   PDB; 2V31; NMR; -; A=202-312.
DR   PDBsum; 1Z7L; -.
DR   PDBsum; 2V31; -.
DR   ProteinModelPortal; Q02053; -.
DR   SMR; Q02053; 48-1057.
DR   STRING; Q02053; -.
DR   PhosphoSite; Q02053; -.
DR   PRIDE; Q02053; -.
DR   Ensembl; ENSMUST00000001989; ENSMUSP00000001989; ENSMUSG00000001924.
DR   Ensembl; ENSMUST00000089217; ENSMUSP00000086626; ENSMUSG00000001924.
DR   GeneID; 22201; -.
DR   KEGG; mmu:22201; -.
DR   UCSC; uc009stl.1; mouse.
DR   CTD; 22201; -.
DR   MGI; MGI:98890; Uba1.
DR   eggNOG; roNOG12963; -.
DR   GeneTree; ENSGT00390000016689; -.
DR   HOGENOM; HBG356508; -.
DR   HOVERGEN; HBG054199; -.
DR   InParanoid; Q02053; -.
DR   OMA; PANGMAK; -.
DR   OrthoDB; EOG4QZ7K4; -.
DR   PhylomeDB; Q02053; -.
DR   NextBio; 302189; -.
DR   ArrayExpress; Q02053; -.
DR   Bgee; Q02053; -.
DR   CleanEx; MM_UBA1; -.
DR   Genevestigator; Q02053; -.
DR   GermOnline; ENSMUSG00000001924; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008641; F:small protein activating enzyme activity; IEA:InterPro.
DR   GO; GO:0006464; P:protein modification process; IEA:InterPro.
DR   InterPro; IPR009036; Molybdenum_cofac_synth_MoeB.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR018965; Ub-activating_enz_e1_C.
DR   InterPro; IPR023280; Ub-like_act_enz_cat_cys_dom.
DR   InterPro; IPR000127; UBact_repeat.
DR   InterPro; IPR019572; Ubiquitin-activating_enzyme.
DR   InterPro; IPR018075; UBQ-activ_enz_E1.
DR   InterPro; IPR018074; UBQ-activ_enz_E1_AS.
DR   InterPro; IPR000011; UBQ/SUMO-activ_enz_E1-like.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 4.
DR   Gene3D; G3DSA:1.10.3240.10; Ub-like_act_enz_cat_cys_dom; 1.
DR   Pfam; PF00899; ThiF; 2.
DR   Pfam; PF09358; UBA_e1_C; 1.
DR   Pfam; PF10585; UBA_e1_thiolCys; 1.
DR   Pfam; PF02134; UBACT; 2.
DR   PRINTS; PR01849; UBIQUITINACT.
DR   SUPFAM; SSF69572; MoeB; 2.
DR   TIGRFAMs; TIGR01408; Ube1; 1.
DR   PROSITE; PS00536; UBIQUITIN_ACTIVAT_1; 1.
DR   PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Direct protein sequencing;
KW   Ligase; Nucleotide-binding; Phosphoprotein; Repeat; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   CHAIN         1   1058       Ubiquitin-like modifier-activating enzyme
FT                                1.
FT                                /FTId=PRO_0000194935.
FT   REPEAT       63    199       1-1.
FT   REPEAT      459    611       1-2.
FT   NP_BIND     478    507       ATP (By similarity).
FT   REGION       63    611       2 approximate repeats.
FT   ACT_SITE    632    632       Glycyl thioester intermediate (By
FT                                similarity).
FT   MOD_RES       4      4       Phosphoserine (By similarity).
FT   MOD_RES      13     13       Phosphoserine (By similarity).
FT   MOD_RES      21     21       Phosphoserine.
FT   MOD_RES      24     24       Phosphoserine.
FT   MOD_RES      31     31       Phosphoserine.
FT   MOD_RES      46     46       Phosphoserine.
FT   MOD_RES      55     55       Phosphotyrosine.
FT   MOD_RES     671    671       N6-acetyllysine (By similarity).
FT   MOD_RES     800    800       Phosphothreonine (By similarity).
FT   MOD_RES     810    810       Phosphoserine (By similarity).
FT   MOD_RES     816    816       Phosphoserine.
FT   MOD_RES     820    820       Phosphoserine.
FT   MOD_RES     835    835       Phosphoserine.
FT   MOD_RES     980    980       N6-acetyllysine (By similarity).
FT   CONFLICT    963    963       L -> V (in Ref. 6; CAA44465).
FT   STRAND      218    224
FT   STRAND      227    234
FT   STRAND      247    250
FT   STRAND      252    255
FT   HELIX       260    262
FT   STRAND      265    269
FT   STRAND      271    278
FT   STRAND      291    293
FT   HELIX       631    635
FT   HELIX       641    656
FT   HELIX       658    666
FT   HELIX       671    677
FT   HELIX       683    695
FT   TURN        696    698
FT   HELIX       703    718
FT   HELIX       720    728
FT   STRAND      740    742
FT   HELIX       759    775
FT   HELIX       784    792
FT   STRAND      809    811
FT   HELIX       824    832
FT   HELIX       836    838
FT   HELIX       858    872
FT   HELIX       880    886
SQ   SEQUENCE   1058 AA;  117809 MW;  95D8152ED5C8E037 CRC64;
     MSSSPLSKKR RVSGPDPKPG SNCSPAQSAL SEVSSVPTNG MAKNGSEADI DESLYSRQLY
     VLGHEAMKML QTSSVLVSGL RGLGVEIAKN IILGGVKAVT LHDQGTTQWA DLSSQFYLRE
     EDIGKNRAEV SQPRLAELNS YVPVTAYTGP LVEDFLSSFQ VVVLTNSPLE AQLRVGEFCH
     SRGIKLVVAD TRGLFGQLFC DFGEEMVLTD SNGEQPLSAM VSMVTKDNPG VVTCLDEARH
     GFETGDFVSF SEVQGMIQLN GCQPMEIKVL GPYTFSICDT SNFSDYIRGG IVSQVKVPKK
     ISFKSLPASL VEPDFVMTDF AKYSRPAQLH IGFQALHQFC ALHNQPPRPR NEEDATELVG
     LAQAVNARSP PSVKQNSLDE DLIRKLAYVA AGDLAPINAF IGGLAAQEVM KACSGKFMPI
     MQWLYFDALE CLPEDKEALT EEKCLPRQNR YDGQVAVFGS DFQEKLSKQK YFLVGAGAIG
     CELLKNFAMI GLGCGEGGEV VVTDMDTIEK SNLNRQFLFR PWDVTKLKSD TAAAAVRQMN
     PYIQVTSHQN RVGPDTERIY DDDFFQNLDG VANALDNIDA RMYMDRRCVY YRKPLLESGT
     LGTKGNVQVV IPFLTESYSS SQDPPEKSIP ICTLKNFPNA IEHTLQWARD EFEGLFKQPA
     ENVNQYLTDS KFVERTLRLA GTQPLEVLEA VQRSLVLQRP QTWGDCVTWA CHHWHTQYCN
     NIRQLLHNFP PDQLTSSGAP FWSGPKRCPH PLTFDVNNTL HLDYVMAAAN LFAQTYGLTG
     SQDRAAVASL LQSVQVPEFT PKSGVKIHVS DQELQSANAS VDDSRLEELK ATLPSPDKLP
     GFKMYPIDFE KDDDSNFHMD FIVAASNLRA ENYDISPADR HKSKLIAGKI IPAIATTTAA
     VVGLVCLELY KVVQGHQQLD SYKNGFLNLA LPFFGFSEPL AAPRHQYYNQ EWTLWDRFEV
     QGLQPNGEEM TLKQFLDYFK TEHKLEITML SQGVSMLYSF FMPAAKLKER LDQPMTEIVS
     RVSKRKLGRH VRALVLELCC NDESGEDVEV PYVRYTIR
//
ID   CTNB1_MOUSE             Reviewed;         781 AA.
AC   Q02248; Q922W1; Q9D335;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   08-MAR-2011, entry version 132.
DE   RecName: Full=Catenin beta-1;
DE   AltName: Full=Beta-catenin;
GN   Name=Ctnnb1; Synonyms=Catnb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92376536; PubMed=1509266; DOI=10.1126/science.257.5073.1142-a;
RA   Butz S., Stappert J., Weissig H., Kemler R.;
RT   "Plakoglobin and beta-catenin: distinct but closely related.";
RL   Science 257:1142-1144(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Colon, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary cancer;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
RX   PubMed=7982500; DOI=10.1016/0014-5793(94)01205-9;
RA   Butz S., Kemler R.;
RT   "Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell
RT   adhesion.";
RL   FEBS Lett. 355:195-200(1994).
RN   [5]
RP   INTERACTION WITH TCF7; TCF7L1; TCF7L2 AND LEF1.
RX   MEDLINE=98454908; PubMed=9783587; DOI=10.1038/26989;
RA   Roose J., Molenaar M., Peterson J., Hurenkamp J., Brantjes H.,
RA   Moerer P., van de Wetering M., Destree O., Clevers H.;
RT   "The Xenopus Wnt effector XTcf-3 interacts with Groucho-related
RT   transcriptional repressors.";
RL   Nature 395:608-612(1998).
RN   [6]
RP   INTERACTION WITH AXIN1.
RX   PubMed=10581160; DOI=10.1006/bbrc.1999.1760;
RA   Jho E., Lomvardas S., Costantini F.;
RT   "A GSK3beta phosphorylation site in axin modulates interaction with
RT   beta-catenin and Tcf-mediated gene expression.";
RL   Biochem. Biophys. Res. Commun. 266:28-35(1999).
RN   [7]
RP   INTERACTION WITH AXIN1.
RX   PubMed=15063782; DOI=10.1016/j.bbrc.2004.03.065;
RA   Kim S.I., Park C.S., Lee M.S., Kwon M.S., Jho E.H., Song W.K.;
RT   "Cyclin-dependent kinase 2 regulates the interaction of Axin with
RT   beta-catenin.";
RL   Biochem. Biophys. Res. Commun. 317:478-483(2004).
RN   [8]
RP   RECONSTITUTION OF THE E-CADHERIN/CATENIN ADHESION COMPLEX, AND LACK OF
RP   ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
RX   PubMed=16325582; DOI=10.1016/j.cell.2005.09.020;
RA   Yamada S., Pokutta S., Drees F., Weis W.I., Nelson W.J.;
RT   "Deconstructing the cadherin-catenin-actin complex.";
RL   Cell 123:889-901(2005).
RN   [9]
RP   INTERACTION WITH XIRP1.
RX   PubMed=17925400; DOI=10.1074/jbc.M707639200;
RA   Choi S., Gustafson-Wagner E.A., Wang Q., Harlan S.M., Sinn H.W.,
RA   Lin J.L.-C., Lin J.J.-C.;
RT   "The intercalated disc protein, mXin{alpha}, is capable of interacting
RT   with beta-catenin and bundling actin filaments.";
RL   J. Biol. Chem. 282:36024-36036(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-654, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [11]
RP   INTERACTION WITH SLC30A9.
RX   PubMed=17344318; DOI=10.1093/nar/gkm095;
RA   Chen Y.H., Yang C.K., Xia M., Ou C.Y., Stallcup M.R.;
RT   "Role of GAC63 in transcriptional activation mediated by beta-
RT   catenin.";
RL   Nucleic Acids Res. 35:2084-2092(2007).
RN   [12]
RP   REVIEW.
RX   MEDLINE=20145417; PubMed=10679188; DOI=10.1006/bbrc.1999.1860;
RA   Kikuchi A.;
RT   "Regulation of beta-catenin signaling in the Wnt pathway.";
RL   Biochem. Biophys. Res. Commun. 268:243-248(2000).
RN   [13]
RP   INTERACTION WITH BAIAP1.
RX   PubMed=10772923; DOI=10.1006/bbrc.2000.2471;
RA   Dobrosotskaya I.Y., James G.L.;
RT   "MAGI-1 interacts with beta-catenin and is associated with cell-cell
RT   adhesion structures.";
RL   Biochem. Biophys. Res. Commun. 270:903-909(2000).
RN   [14]
RP   INTERACTION WITH CTNNA3.
RX   MEDLINE=21474377; PubMed=11590244;
RA   Janssens B., Goossens S., Staes K., Gilbert B., van Hengel J.,
RA   Colpaert C., Bruyneel E., Mareel M., van Roy F.;
RT   "AlphaT-catenin: a novel tissue-specific beta-catenin-binding protein
RT   mediating strong cell-cell adhesion.";
RL   J. Cell Sci. 114:3177-3188(2001).
RN   [15]
RP   INTERACTION WITH TAX1BP3.
RX   PubMed=12874278; DOI=10.1074/jbc.M306324200;
RA   Kanamori M., Sandy P., Marzinotto S., Benetti R., Kai C.,
RA   Hayashizaki Y., Schneider C., Suzuki H.;
RT   "The PDZ protein tax-interacting protein-1 inhibits beta-catenin
RT   transcriptional activity and growth of colorectal cancer cells.";
RL   J. Biol. Chem. 278:38758-38764(2003).
RN   [16]
RP   INTERACTION WITH GLIS2, AND SUBCELLULAR LOCATION.
RX   PubMed=17289029; DOI=10.1016/j.febslet.2007.01.058;
RA   Kim Y.-S., Kang H.S., Jetten A.M.;
RT   "The Kruppel-like zinc finger protein Glis2 functions as a negative
RT   modulator of the Wnt/beta-catenin signaling pathway.";
RL   FEBS Lett. 581:858-864(2007).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-551 AND THR-556, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-551; SER-552 AND
RP   THR-556, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552 AND SER-675, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [20]
RP   LACK OF ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
RX   PubMed=18093941; DOI=10.1073/pnas.0710504105;
RA   Abe K., Takeichi M.;
RT   "EPLIN mediates linkage of the cadherin catenin complex to F-actin and
RT   stabilizes the circumferential actin belt.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:13-19(2008).
RN   [21]
RP   INTERACTION WITH TCF7L2 AND TNIK.
RX   PubMed=19816403; DOI=10.1038/emboj.2009.285;
RA   Mahmoudi T., Li V.S.W., Ng S.S., Taouatas N., Vries R.G.J.,
RA   Mohammed S., Heck A.J., Clevers H.;
RT   "The kinase TNIK is an essential activator of Wnt target genes.";
RL   EMBO J. 28:3329-3340(2009).
RN   [22]
RP   INTERACTION WITH SCRIB.
RX   PubMed=19458197; DOI=10.1091/mbc.E08-12-1172;
RA   Sun Y., Aiga M., Yoshida E., Humbert P.O., Bamji S.X.;
RT   "Scribble interacts with beta-catenin to localize synaptic vesicles to
RT   synapses.";
RL   Mol. Biol. Cell 20:3390-3400(2009).
RN   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [24]
RP   INTERACTION WITH TRPV4 AND CDH1.
RX   PubMed=20413591; DOI=10.1074/jbc.M110.103606;
RA   Sokabe T., Fukumi-Tominaga T., Yonemura S., Mizuno A., Tominaga M.;
RT   "The TRPV4 channel contributes to intercellular junction formation in
RT   keratinocytes.";
RL   J. Biol. Chem. 285:18749-18758(2010).
RN   [25]
RP   INTERACTION WITH VCL, AND MUTAGENESIS OF MET-8.
RX   PubMed=20086044; DOI=10.1242/jcs.056432;
RA   Peng X., Cuff L.E., Lawton C.D., DeMali K.A.;
RT   "Vinculin regulates cell-surface E-cadherin expression by binding to
RT   beta-catenin.";
RL   J. Cell Sci. 123:567-577(2010).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 150-665.
RX   MEDLINE=97442350; PubMed=9298899; DOI=10.1016/S0092-8674(00)80352-9;
RA   Huber A.H., Nelson W.J., Weis W.I.;
RT   "Three-dimensional structure of the armadillo repeat region of beta-
RT   catenin.";
RL   Cell 90:871-882(1997).
RN   [27]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 118-149 IN COMPLEX WITH
RP   CTNNA1.
RX   MEDLINE=20337986; PubMed=10882138; DOI=10.1016/S1097-2765(00)80447-5;
RA   Pokutta S., Weis W.I.;
RT   "Structure of the dimerization and beta-catenin-binding region of
RT   alpha-catenin.";
RL   Mol. Cell 5:533-543(2000).
RN   [28]
RP   X-RAY CRYSTALLOGRAPHY (2.0 AND 3.0 ANGSTROMS) OF 134-671 IN COMPLEX
RP   WITH PHOSPHORYLATED AND UNPHOSPHORYLATED CDH1.
RX   MEDLINE=21246507; PubMed=11348595; DOI=10.1016/S0092-8674(01)00330-0;
RA   Huber A.H., Weis W.I.;
RT   "The structure of the beta-catenin/E-cadherin complex and the
RT   molecular basis of diverse ligand recognition by beta-catenin.";
RL   Cell 105:391-402(2001).
RN   [29]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 134-671 IN COMPLEX WITH APC.
RX   MEDLINE=21564054; PubMed=11707392; DOI=10.1093/emboj/20.22.6203;
RA   Eklof Spink K., Fridman S.G., Weis W.I.;
RT   "Molecular mechanisms of beta-catenin recognition by adenomatous
RT   polyposis coli revealed by the structure of an APC-beta-catenin
RT   complex.";
RL   EMBO J. 20:6203-6212(2001).
RN   [30]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 134-671 IN COMPLEX WITH
RP   CTNNBIP1, AND INTERACTION WITH EP300.
RX   MEDLINE=22297629; PubMed=12408825; DOI=10.1016/S1097-2765(02)00631-7;
RA   Daniels D.L., Weis W.I.;
RT   "ICAT inhibits beta-catenin binding to Tcf/Lef-family transcription
RT   factors and the general coactivator p300 using independent structural
RT   modules.";
RL   Mol. Cell 10:573-584(2002).
CC   -!- FUNCTION: Involved in the regulation of cell adhesion. The
CC       majority of beta-catenin is localized to the cell membrane and is
CC       part of E-cadherin/catenin adhesion complexes which are proposed
CC       to couple cadherins to the actin cytoskeleton.
CC   -!- FUNCTION: Involved in signal transduction through the Wnt pathway.
CC       Nuclear beta-catenin it involved in transcriptional regulation by
CC       association with transcription factors of the TCF/LEF family.
CC   -!- SUBUNIT: Two separate complex-associated pools are found in the
CC       cytoplasm. The majority is present as component of an E-cadherin/
CC       catenin adhesion complex composed of at least E-cadherin/CDH1 and
CC       beta-catenin/CTNNB1, and possibly alpha-catenin/CTNNA1; the
CC       complex is located to adherens junctions. The stable association
CC       of CTNNA1 is controversial as CTNNA1 was shown not to bind to F-
CC       actin when assembled in the complex. Alternatively, the CTNNA1-
CC       containing complex may be linked to F-actin by other proteins such
CC       as LIMA1. Another cytoplasmic pool is part of a large complex
CC       containing AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes
CC       phosphorylation on N-terminal Ser and Thr residues and
CC       ubiquitination of CTNNB1 via BTRC and its subsequent degradation
CC       by the proteasome. Wnt-dependent activation of DVL antagonizes the
CC       action of GSK3B. When GSK3B activity is inhibited the complex
CC       dissociates, CTNNB1 is dephosphorylated and is no longer targeted
CC       for destruction. The stabilized protein translocates to the
CC       nucleus, where it binds TCF/LEF-1 family members, TBP, BCL9 and
CC       possibly also RUVBL1 and CHD8. Binds CTNNBIP and EP300. CTNNB1
CC       forms a ternary complex with LEF1 and EP300 that is disrupted by
CC       CTNNBIP1 binding (By similarity). Interacts with TAX1BP3 (via the
CC       PDZ domain); this interaction inhibits the transcriptional
CC       activity of CTNNB1. Interacts with AJAP1, BAIAP1, CARM1, CTNNA3,
CC       CXADR and PCDH11Y. Binds SLC9A3R1 (By similarity). Interacts with
CC       GLIS2. Interacts with SLC30A9. Interacts with XIRP1. Interacts
CC       with PTPRU (via the cytoplasmic juxtamembrane domain) and with EMD
CC       (By similarity). Interacts with SCRIB. Interacts with TNIK and
CC       TCF7L2. Interacts with SESTD1 and TRPC4 (By similarity). Interacts
CC       directly with AXIN1; the interaction is regulated by CDK2
CC       phosphorylation of AXIN1. Interacts with CAV1. Interacts with
CC       PTPRJ (By similarity). Interacts with TRPV4; the TRPV4 and CTNNB1
CC       complex can interact with CDH1. Interacts with VCL.
CC   -!- INTERACTION:
CC       P25054:APC (xeno); NbExp=3; IntAct=EBI-397872, EBI-727707;
CC       O15169:AXIN1 (xeno); NbExp=2; IntAct=EBI-397872, EBI-710484;
CC       P09803:Cdh1; NbExp=4; IntAct=EBI-397872, EBI-984420;
CC       P26231:Ctnna1; NbExp=1; IntAct=EBI-397872, EBI-647895;
CC       Q9NSA3:CTNNBIP1 (xeno); NbExp=3; IntAct=EBI-397872, EBI-747082;
CC       P27782:Lef1; NbExp=2; IntAct=EBI-397872, EBI-984464;
CC       P45984-1:MAPK9 (xeno); NbExp=1; IntAct=EBI-397872, EBI-713586;
CC       P26450:Pik3r1; NbExp=2; IntAct=EBI-397872, EBI-641764;
CC       P97458:Prop1; NbExp=2; IntAct=EBI-397872, EBI-937831;
CC       P49768:PSEN1 (xeno); NbExp=1; IntAct=EBI-397872, EBI-297277;
CC       P49769:Psen1; NbExp=1; IntAct=EBI-397872, EBI-990067;
CC       Q9DBG9:Tax1bp3; NbExp=4; IntAct=EBI-397872, EBI-1161647;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Nucleus.
CC       Cell junction, adherens junction (By similarity). Note=Cytoplasmic
CC       when it is unstabilized (high level of phosphorylation) or bound
CC       to CDH1. Translocates to the nucleus when it is stabilized (low
CC       level of phosphorylation). Interaction with GLIS2 promotes nuclear
CC       translocation. Interaction with EMD inhibits nuclear localization
CC       (By similarity).
CC   -!- PTM: Phosphorylation by GSK3B requires prior phosphorylation of
CC       Ser-45 by another kinase. Phosphorylation proceeds then from Thr-
CC       41 to Ser-33 (By similarity).
CC   -!- PTM: EGF stimulates tyrosine phosphorylation. Phosphorylation on
CC       Tyr-654 decreases CDH1 binding and enhances TBP binding (By
CC       similarity).
CC   -!- PTM: Ubiquitinated by a E3 ubiquitin ligase complex containing
CC       UBE2D1, SIAH1, CACYBP/SIP, SKP1A, APC and TBL1X (Probable). Its
CC       ubiquitination leads to its subsequent proteasomal degradation (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the beta-catenin family.
CC   -!- SIMILARITY: Contains 12 ARM repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH06739.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; M90364; AAA37280.1; -; mRNA.
DR   EMBL; AK035311; BAC29027.1; -; mRNA.
DR   EMBL; AK018515; BAB31250.1; -; mRNA.
DR   EMBL; BC006739; AAH06739.1; ALT_INIT; mRNA.
DR   EMBL; BC048153; AAH48153.1; -; mRNA.
DR   EMBL; BC053065; AAH53065.1; -; mRNA.
DR   IPI; IPI00125899; -.
DR   PIR; S35091; S35091.
DR   RefSeq; NP_001159374.1; NM_001165902.1.
DR   RefSeq; NP_031640.1; NM_007614.3.
DR   UniGene; Mm.291928; -.
DR   PDB; 1DOW; X-ray; 1.80 A; B=118-149.
DR   PDB; 1I7W; X-ray; 2.00 A; A/C=134-671.
DR   PDB; 1I7X; X-ray; 3.00 A; A/C=134-671.
DR   PDB; 1JPP; X-ray; 3.10 A; A/B=134-671.
DR   PDB; 1M1E; X-ray; 2.10 A; A=134-671.
DR   PDB; 1V18; X-ray; 2.10 A; A=134-671.
DR   PDB; 2BCT; X-ray; 2.90 A; A=150-665.
DR   PDB; 3BCT; X-ray; 2.10 A; A=193-662.
DR   PDB; 3OUW; X-ray; 2.91 A; A=134-671.
DR   PDB; 3OUX; X-ray; 2.40 A; A=134-671.
DR   PDBsum; 1DOW; -.
DR   PDBsum; 1I7W; -.
DR   PDBsum; 1I7X; -.
DR   PDBsum; 1JPP; -.
DR   PDBsum; 1M1E; -.
DR   PDBsum; 1V18; -.
DR   PDBsum; 2BCT; -.
DR   PDBsum; 3BCT; -.
DR   PDBsum; 3OUW; -.
DR   PDBsum; 3OUX; -.
DR   ProteinModelPortal; Q02248; -.
DR   SMR; Q02248; 19-44, 142-665.
DR   DisProt; DP00341; -.
DR   IntAct; Q02248; 75.
DR   MINT; MINT-103426; -.
DR   STRING; Q02248; -.
DR   PhosphoSite; Q02248; -.
DR   PRIDE; Q02248; -.
DR   Ensembl; ENSMUST00000007130; ENSMUSP00000007130; ENSMUSG00000006932.
DR   GeneID; 12387; -.
DR   KEGG; mmu:12387; -.
DR   UCSC; uc009scu.1; mouse.
DR   CTD; 12387; -.
DR   MGI; MGI:88276; Ctnnb1.
DR   eggNOG; roNOG10531; -.
DR   HOGENOM; HBG357527; -.
DR   HOVERGEN; HBG000919; -.
DR   InParanoid; Q02248; -.
DR   OMA; DSMQGLE; -.
DR   OrthoDB; EOG4FN4H2; -.
DR   PhylomeDB; Q02248; -.
DR   NextBio; 281106; -.
DR   PMAP-CutDB; Q02248; -.
DR   ArrayExpress; Q02248; -.
DR   Bgee; Q02248; -.
DR   CleanEx; MM_CTNNB1; -.
DR   Genevestigator; Q02248; -.
DR   GermOnline; ENSMUSG00000006932; Mus musculus.
DR   GO; GO:0043296; C:apical junction complex; IDA:MGI.
DR   GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR   GO; GO:0034747; C:Axin-APC-beta-catenin-GSK3B complex; IDA:MGI.
DR   GO; GO:0005813; C:centrosome; IDA:BHF-UCL.
DR   GO; GO:0005916; C:fascia adherens; IDA:MGI.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0031528; C:microvillus membrane; IDA:MGI.
DR   GO; GO:0034750; C:Scrib-APC-beta-catenin complex; IDA:BHF-UCL.
DR   GO; GO:0005667; C:transcription factor complex; IDA:MGI.
DR   GO; GO:0030018; C:Z disc; IDA:MGI.
DR   GO; GO:0045294; F:alpha-catenin binding; IPI:MGI.
DR   GO; GO:0045296; F:cadherin binding; IPI:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:MGI.
DR   GO; GO:0010843; F:promoter binding; IDA:MGI.
DR   GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR   GO; GO:0070491; F:repressing transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0003704; F:specific RNA polymerase II transcription factor activity; IDA:MGI.
DR   GO; GO:0016563; F:transcription activator activity; IDA:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR   GO; GO:0009948; P:anterior/posterior axis specification; IMP:MGI.
DR   GO; GO:0006915; P:apoptosis; IMP:MGI.
DR   GO; GO:0045453; P:bone resorption; IGI:MGI.
DR   GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI.
DR   GO; GO:0060070; P:canonical Wnt receptor signaling pathway; IDA:MGI.
DR   GO; GO:0001708; P:cell fate specification; IMP:MGI.
DR   GO; GO:0048469; P:cell maturation; IDA:MGI.
DR   GO; GO:0016337; P:cell-cell adhesion; IMP:MGI.
DR   GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR   GO; GO:0022009; P:central nervous system vasculogenesis; IMP:MGI.
DR   GO; GO:0009950; P:dorsal/ventral axis specification; IMP:MGI.
DR   GO; GO:0007398; P:ectoderm development; IMP:MGI.
DR   GO; GO:0035117; P:embryonic arm morphogenesis; IDA:MGI.
DR   GO; GO:0000578; P:embryonic axis specification; IDA:MGI.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR   GO; GO:0048617; P:embryonic foregut morphogenesis; IMP:MGI.
DR   GO; GO:0035050; P:embryonic heart tube development; IMP:MGI.
DR   GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
DR   GO; GO:0001711; P:endodermal cell fate commitment; IMP:MGI.
DR   GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; IMP:MGI.
DR   GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IMP:MGI.
DR   GO; GO:0060066; P:fallopian tube development; IMP:MGI.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0061198; P:fungiform papilla formation; IMP:MGI.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
DR   GO; GO:0035112; P:genitalia morphogenesis; IMP:MGI.
DR   GO; GO:0007403; P:glial cell fate determination; IDA:MGI.
DR   GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
DR   GO; GO:0060789; P:hair follicle placode formation; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
DR   GO; GO:0060479; P:lung cell differentiation; IMP:MGI.
DR   GO; GO:0060492; P:lung induction; IMP:MGI.
DR   GO; GO:0060484; P:lung-associated mesenchyme development; IMP:MGI.
DR   GO; GO:0030539; P:male genitalia development; IMP:MGI.
DR   GO; GO:0060916; P:mesenchymal cell proliferation involved in lung development; IMP:MGI.
DR   GO; GO:0003337; P:mesenchymal to epithelial transition involved in metanephros morphogenesis; IDA:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptosis; IGI:MGI.
DR   GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IGI:MGI.
DR   GO; GO:0045671; P:negative regulation of osteoclast differentiation; IMP:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0072079; P:nephron tubule formation; IMP:MGI.
DR   GO; GO:0042475; P:odontogenesis of dentine-containing tooth; IMP:MGI.
DR   GO; GO:0048599; P:oocyte development; IGI:MGI.
DR   GO; GO:0030316; P:osteoclast differentiation; IMP:MGI.
DR   GO; GO:0031016; P:pancreas development; IMP:MGI.
DR   GO; GO:0001569; P:patterning of blood vessels; IMP:MGI.
DR   GO; GO:0061047; P:positive regulation of branching involved in lung morphogenesis; IMP:MGI.
DR   GO; GO:2000017; P:positive regulation of determination of dorsal identity; IDA:MGI.
DR   GO; GO:0045603; P:positive regulation of endothelial cell differentiation; IMP:MGI.
DR   GO; GO:0060769; P:positive regulation of epithelial cell proliferation involved in prostate gland development; IMP:MGI.
DR   GO; GO:0045743; P:positive regulation of fibroblast growth factor receptor signaling pathway; IMP:MGI.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:MGI.
DR   GO; GO:0043410; P:positive regulation of MAPKKK cascade; IGI:MGI.
DR   GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IMP:MGI.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:MGI.
DR   GO; GO:0009954; P:proximal/distal pattern formation; IMP:MGI.
DR   GO; GO:0070602; P:regulation of centromeric sister chromatid cohesion; IMP:BHF-UCL.
DR   GO; GO:0042129; P:regulation of T cell proliferation; IMP:MGI.
DR   GO; GO:0072053; P:renal inner medulla development; IMP:MGI.
DR   GO; GO:0072054; P:renal outer medulla development; IMP:MGI.
DR   GO; GO:0072033; P:renal vesicle formation; IMP:MGI.
DR   GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR   GO; GO:0051145; P:smooth muscle cell differentiation; IMP:MGI.
DR   GO; GO:0050808; P:synapse organization; IMP:MGI.
DR   GO; GO:0007268; P:synaptic transmission; IMP:MGI.
DR   GO; GO:0048489; P:synaptic vesicle transport; IMP:MGI.
DR   GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR   GO; GO:0048538; P:thymus development; IMP:MGI.
DR   GO; GO:0060440; P:trachea formation; IMP:MGI.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR013284; Beta-catenin.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF00514; Arm; 5.
DR   PRINTS; PR01869; BCATNINFAMLY.
DR   SMART; SM00185; ARM; 12.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 9.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Cell adhesion; Cell junction; Cytoplasm;
KW   Cytoskeleton; Nucleus; Phosphoprotein; Repeat; Transcription;
KW   Transcription regulation; Ubl conjugation; Wnt signaling pathway.
FT   CHAIN         1    781       Catenin beta-1.
FT                                /FTId=PRO_0000064272.
FT   REPEAT      151    191       ARM 1.
FT   REPEAT      193    234       ARM 2.
FT   REPEAT      235    276       ARM 3.
FT   REPEAT      277    318       ARM 4.
FT   REPEAT      319    360       ARM 5.
FT   REPEAT      361    389       ARM 6.
FT   REPEAT      400    441       ARM 7.
FT   REPEAT      442    484       ARM 8.
FT   REPEAT      489    530       ARM 9.
FT   REPEAT      531    571       ARM 10.
FT   REPEAT      594    636       ARM 11.
FT   REPEAT      637    666       ARM 12.
FT   REGION        1     23       Interaction with VCL.
FT   REGION      772    781       Interaction with SCRIB.
FT   MOD_RES      23     23       Phosphoserine; by GSK3-beta (By
FT                                similarity).
FT   MOD_RES      29     29       Phosphoserine; by GSK3-beta (By
FT                                similarity).
FT   MOD_RES      33     33       Phosphoserine; by GSK3-beta (By
FT                                similarity).
FT   MOD_RES      37     37       Phosphoserine; by GSK3-beta (By
FT                                similarity).
FT   MOD_RES      41     41       Phosphothreonine; by GSK3-beta (By
FT                                similarity).
FT   MOD_RES      45     45       Phosphoserine (By similarity).
FT   MOD_RES      86     86       Phosphotyrosine; by CSK (By similarity).
FT   MOD_RES     191    191       Phosphoserine (By similarity).
FT   MOD_RES     551    551       Phosphothreonine.
FT   MOD_RES     552    552       Phosphoserine.
FT   MOD_RES     556    556       Phosphothreonine.
FT   MOD_RES     654    654       Phosphotyrosine.
FT   MOD_RES     675    675       Phosphoserine.
FT   MUTAGEN       8      8       M->P: Loss of interaction with VCL.
FT   CONFLICT    371    371       T -> I (in Ref. 2; BAB31250).
FT   CONFLICT    478    478       A -> T (in Ref. 2; BAB31250).
FT   CONFLICT    487    487       L -> F (in Ref. 2; BAB31250).
FT   HELIX       121    141
FT   TURN        145    148
FT   TURN        150    152
FT   HELIX       153    160
FT   HELIX       165    180
FT   HELIX       182    189
FT   HELIX       192    204
FT   HELIX       208    221
FT   HELIX       225    233
FT   HELIX       236    242
FT   HELIX       243    245
FT   HELIX       249    265
FT   HELIX       269    275
FT   HELIX       278    284
FT   HELIX       285    287
FT   HELIX       291    305
FT   HELIX       309    317
FT   HELIX       320    330
FT   HELIX       334    347
FT   HELIX       353    359
FT   HELIX       362    367
FT   TURN        368    371
FT   HELIX       375    389
FT   HELIX       399    408
FT   HELIX       414    428
FT   HELIX       432    440
FT   HELIX       443    454
FT   HELIX       458    471
FT   STRAND      473    475
FT   HELIX       478    487
FT   HELIX       491    496
FT   HELIX       504    517
FT   HELIX       521    523
FT   HELIX       524    529
FT   HELIX       532    547
FT   HELIX       566    580
FT   HELIX       584    592
FT   HELIX       596    602
FT   HELIX       608    621
FT   HELIX       625    632
FT   TURN        633    636
FT   HELIX       637    643
FT   HELIX       649    661
SQ   SEQUENCE   781 AA;  85471 MW;  D708F170A3FBED6E CRC64;
     MATQADLMEL DMAMEPDRKA AVSHWQQQSY LDSGIHSGAT TTAPSLSGKG NPEEEDVDTS
     QVLYEWEQGF SQSFTQEQVA DIDGQYAMTR AQRVRAAMFP ETLDEGMQIP STQFDAAHPT
     NVQRLAEPSQ MLKHAVVNLI NYQDDAELAT RAIPELTKLL NDEDQVVVNK AAVMVHQLSK
     KEASRHAIMR SPQMVSAIVR TMQNTNDVET ARCTAGTLHN LSHHREGLLA IFKSGGIPAL
     VKMLGSPVDS VLFYAITTLH NLLLHQEGAK MAVRLAGGLQ KMVALLNKTN VKFLAITTDC
     LQILAYGNQE SKLIILASGG PQALVNIMRT YTYEKLLWTT SRVLKVLSVC SSNKPAIVEA
     GGMQALGLHL TDPSQRLVQN CLWTLRNLSD AATKQEGMEG LLGTLVQLLG SDDINVVTCA
     AGILSNLTCN NYKNKMMVCQ VGGIEALVRT VLRAGDREDI TEPAICALRH LTSRHQEAEM
     AQNAVRLHYG LPVVVKLLHP PSHWPLIKAT VGLIRNLALC PANHAPLREQ GAIPRLVQLL
     VRAHQDTQRR TSMGGTQQQF VEGVRMEEIV EGCTGALHIL ARDVHNRIVI RGLNTIPLFV
     QLLYSPIENI QRVAAGVLCE LAQDKEAAEA IEAEGATAPL TELLHSRNEG VATYAAAVLF
     RMSEDKPQDY KKRLSVELTS SLFRTEPMAW NETADLGLDI GAQGEALGYR QDDPSYRSFH
     SGGYGQDALG MDPMMEHEMG GHHPGADYPV DGLPDLGHAQ DLMDGLPPGD SNQLAWFDTD
     L
//
ID   PLAK_MOUSE              Reviewed;         745 AA.
AC   Q02257; Q8CGD3;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 3.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Junction plakoglobin;
DE   AltName: Full=Desmoplakin III;
DE   AltName: Full=Desmoplakin-3;
GN   Name=Jup;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 125-745.
RX   MEDLINE=92376536; PubMed=1509266; DOI=10.1126/science.257.5073.1142-a;
RA   Butz S., Stappert J., Weissig H., Kemler R.;
RT   "Plakoglobin and beta-catenin: distinct but closely related.";
RL   Science 257:1142-1144(1992).
RN   [4]
RP   SEQUENCE REVISION TO 418 AND 420.
RA   Butz S.;
RL   Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   IDENTIFICATION IN AN E-CADHERIN/CATENIN ADHESION COMPLEX.
RX   PubMed=7982500; DOI=10.1016/0014-5793(94)01205-9;
RA   Butz S., Kemler R.;
RT   "Distinct cadherin-catenin complexes in Ca(2+)-dependent cell-cell
RT   adhesion.";
RL   FEBS Lett. 355:195-200(1994).
RN   [6]
RP   RECONSTITUTION OF THE E-CADHERIN/CATENIN ADHESION COMPLEX, AND LACK OF
RP   ACTIN-BINDING BY THE E-CADHERIN/CATENIN ADHESION COMPLEX.
RX   PubMed=16325582; DOI=10.1016/j.cell.2005.09.020;
RA   Yamada S., Pokutta S., Drees F., Weis W.I., Nelson W.J.;
RT   "Deconstructing the cadherin-catenin-actin complex.";
RL   Cell 123:889-901(2005).
RN   [7]
RP   FUNCTION.
RX   PubMed=19015309; DOI=10.1084/jem.20080406;
RA   Nottebaum A.F., Cagna G., Winderlich M., Gamp A.C., Linnepe R.,
RA   Polaschegg C., Filippova K., Lyck R., Engelhardt B., Kamenyeva O.,
RA   Bixel M.G., Butz S., Vestweber D.;
RT   "VE-PTP maintains the endothelial barrier via plakoglobin and becomes
RT   dissociated from VE-cadherin by leukocytes and by VEGF.";
RL   J. Exp. Med. 205:2929-2945(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Common junctional plaque protein. The membrane-
CC       associated plaques are architectural elements in an important
CC       strategic position to influence the arrangement and function of
CC       both the cytoskeleton and the cells within the tissue. The
CC       presence of plakoglobin in both the desmosomes and in the
CC       intermediate junctions suggests that it plays a central role in
CC       the structure and function of submembranous plaques. Acts as a
CC       substrate for VE-PTP and is required by it to stimulate VE-
CC       cadherin function in endothelial cells. Can replace beta-catenin
CC       in E-cadherin/catenin adhesion complexes which are proposed to
CC       couple cadherins to the actin cytoskeleton.
CC   -!- SUBUNIT: Homodimer. Component of an E-cadherin/ catenin adhesion
CC       complex composed of at least E-cadherin/CDH1 and gamma-
CC       catenin/JUP, and possibly alpha-catenin/CTNNA1; the complex is
CC       located to adherens junctions. The stable association of CTNNA1 is
CC       controversial as CTNNA1 was shown not to bind to F-actin when
CC       assembled in the complex. Interacts with MUC1. Interacts with
CC       CAV1. Interacts with PTPRJ (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, adherens junction. Cell
CC       junction, desmosome. Cytoplasm, cytoskeleton. Membrane; Peripheral
CC       membrane protein. Note=Cytoplasmic in a soluble and membrane-
CC       associated form.
CC   -!- SIMILARITY: Belongs to the beta-catenin family.
CC   -!- SIMILARITY: Contains 9 ARM repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK170934; BAE42126.1; -; mRNA.
DR   EMBL; BC040757; AAH40757.1; -; mRNA.
DR   EMBL; BC094461; AAH94461.1; -; mRNA.
DR   EMBL; M90365; AAB02885.1; -; mRNA.
DR   IPI; IPI00229475; -.
DR   PIR; S35092; S35092.
DR   RefSeq; NP_034723.1; NM_010593.1.
DR   UniGene; Mm.299774; -.
DR   ProteinModelPortal; Q02257; -.
DR   SMR; Q02257; 111-673.
DR   STRING; Q02257; -.
DR   PhosphoSite; Q02257; -.
DR   PRIDE; Q02257; -.
DR   Ensembl; ENSMUST00000001592; ENSMUSP00000001592; ENSMUSG00000001552.
DR   Ensembl; ENSMUST00000107403; ENSMUSP00000103026; ENSMUSG00000001552.
DR   GeneID; 16480; -.
DR   KEGG; mmu:16480; -.
DR   UCSC; uc007lkz.1; mouse.
DR   CTD; 16480; -.
DR   MGI; MGI:96650; Jup.
DR   GeneTree; ENSGT00570000078959; -.
DR   HOGENOM; HBG357527; -.
DR   HOVERGEN; HBG000919; -.
DR   InParanoid; Q02257; -.
DR   OMA; DDMDATY; -.
DR   OrthoDB; EOG4FR0R3; -.
DR   PhylomeDB; Q02257; -.
DR   NextBio; 289775; -.
DR   ArrayExpress; Q02257; -.
DR   Bgee; Q02257; -.
DR   CleanEx; MM_JUP; -.
DR   Genevestigator; Q02257; -.
DR   GermOnline; ENSMUSG00000001552; Mus musculus.
DR   GO; GO:0030057; C:desmosome; IDA:MGI.
DR   GO; GO:0030018; C:Z disc; IDA:MGI.
DR   GO; GO:0045294; F:alpha-catenin binding; IPI:MGI.
DR   GO; GO:0042153; F:RPTP-like protein binding; IPI:MGI.
DR   GO; GO:0016337; P:cell-cell adhesion; IMP:MGI.
DR   GO; GO:0002159; P:desmosome assembly; IMP:MGI.
DR   GO; GO:0043588; P:skin development; IMP:MGI.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR013284; Beta-catenin.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF00514; Arm; 5.
DR   PRINTS; PR01869; BCATNINFAMLY.
DR   SMART; SM00185; ARM; 12.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 9.
PE   1: Evidence at protein level;
KW   Acetylation; Cell adhesion; Cell junction; Cytoplasm; Cytoskeleton;
KW   Membrane; Phosphoprotein; Repeat.
FT   CHAIN         1    745       Junction plakoglobin.
FT                                /FTId=PRO_0000064279.
FT   REPEAT      132    171       ARM 1.
FT   REPEAT      216    255       ARM 2.
FT   REPEAT      258    297       ARM 3.
FT   REPEAT      342    381       ARM 4.
FT   REPEAT      383    420       ARM 5.
FT   REPEAT      423    464       ARM 6.
FT   REPEAT      470    510       ARM 7.
FT   REPEAT      512    551       ARM 8.
FT   REPEAT      574    613       ARM 9.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      20     20       Phosphotyrosine (By similarity).
FT   MOD_RES     182    182       Phosphoserine (By similarity).
FT   MOD_RES     660    660       Phosphotyrosine (By similarity).
FT   MOD_RES     665    665       Phosphoserine.
SQ   SEQUENCE   745 AA;  81801 MW;  9609619D94052FC5 CRC64;
     MEVMNLIEQP IKVTEWQQTY TYDSGIHSGV NTCVPSVSSK GIMDEDDACG RQYTLKKTTT
     YTQGVPQNQG DLEYQMSTTA RAKRVREAMC PGVSGEDSSL LLATQVEGQT TNLQRLAEPS
     QLLKSAIVHL INYQDDAELA TRALPELTKL LNDEDPVVVT KAAMIVNQLS KKEASRRALM
     GSPQLVAAVV RTMQNTSDLD TARCTTSILH NLSHHREGLL AIFKSGGIPA LVRMLSSPVE
     SVLFYAITTL HNLLLYQEGA KMAVRLADGL QKMVPLLNKN NPKFLAITTD CLQLLAYGNQ
     ESKLIILANG GPQGLVQIMR NYSYEKLLWT TSRVLKVLSV CPSNKPAIVE AGGMQALGKH
     LTSNSPRLVQ NCLWTLRNLS DVATKQEGLE SVLKILVNQL SVDDVNVLTC ATGTLSNLTC
     NNSKNKTLVT QNSGVEALIH AILRAGDKDD ITEPAVCALR HLTSRHPEAE MAQNSVRLNY
     GIPAIVKLLN QPNQWPLVKA TIGLIRNLAL CPANHAPLQE AAVIPRLVQL LVKAHQDAQR
     HVAAGTQQPY TDGVRMEEIV EGCTGALHIL ARDPMNRMEI FRLNTIPLFV QLLYSSVENI
     QRVAAGVLCE LAQDKEAADA IDAEGASAPL MELLHSRNEG TATYAAAVLF RISEDKNPDY
     RKRVSVELTN SLFKHDPAAW EAAQSMIPIN EPYADDMDAT YRPMYSSDVP LDPLDMHMDL
     DGDYPMDTYS DGLRPPYPTA DHMLA
//
ID   ANK1_MOUSE              Reviewed;        1862 AA.
AC   Q02357; P70440; P97446; P97941; Q3TZ35; Q3UH42; Q3UHP2; Q3UYY7;
AC   Q61302; Q61303; Q78E45;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Ankyrin-1;
DE            Short=ANK-1;
DE   AltName: Full=Erythrocyte ankyrin;
GN   Name=Ank1; Synonyms=Ank-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ER1).
RC   TISSUE=Erythrocyte;
RX   MEDLINE=92345717; PubMed=1386265; DOI=10.1007/BF00292156;
RA   White R.A., Birkenmeier C.S., Peters L.L., Barker J.E., Lux S.E.;
RT   "Murine erythrocyte ankyrin cDNA: highly conserved regions of the
RT   regulatory domain.";
RL   Mamm. Genome 3:281-285(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BR2; ER3 AND BR4).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=93252825; PubMed=8486643;
RA   Birkenmeier C.S., White R.A., Peters L.L., Hall E.J., Lux S.E.,
RA   Barker J.E.;
RT   "Complex patterns of sequence variation and multiple 5' and 3' ends
RT   are found among transcripts of the erythroid ankyrin gene.";
RL   J. Biol. Chem. 268:9533-9540(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MU7), TISSUE SPECIFICITY, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
RX   MEDLINE=98292497; PubMed=9628825; DOI=10.1006/geno.1998.5305;
RA   Birkenmeier C.S., Sharp J.J., Gifford E.J., Deveau S.A., Barker J.E.;
RT   "An alternative first exon in the distal end of the erythroid ankyrin
RT   gene leads to production of a small isoform containing an NH2-terminal
RT   membrane anchor.";
RL   Genomics 50:79-88(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS BR2; 5; 6 AND MU8).
RC   STRAIN=C57BL/6J; TISSUE=Forelimb, and Inner ear;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MU7).
RC   TISSUE=Heart, and Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RA   Birkenmeier C.B., Sharp J.J., Hall E.J., Deveau S.A., Barker J.E.;
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=9024692; DOI=10.1083/jcb.136.3.621;
RA   Zhou D., Birkenmeier C.S., Williams M.W., Sharp J.J., Barker J.E.,
RA   Bloch R.J.;
RT   "Small, membrane-bound, alternatively spliced forms of ankyrin 1
RT   associated with the sarcoplasmic reticulum of mammalian skeletal
RT   muscle.";
RL   J. Cell Biol. 136:621-631(1997).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-852 AND THR-862, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1069, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Attaches integral membrane proteins to cytoskeletal
CC       elements; binds to the erythrocyte membrane protein band 4.2, to
CC       Na-K ATPase, to the lymphocyte membrane protein GP85, and to the
CC       cytoskeletal proteins fodrin, tubulin, vimentin and desmin.
CC       Erythrocyte ankyrins also link spectrin (beta chain) to the
CC       cytoplasmic domain of the erythrocytes anion exchange protein;
CC       they retain most or all of these binding functions. In skeletal
CC       muscle, isoform Mu7 together with obscurin may provide a molecular
CC       link between the sarcoplasmic reticulum and myofibrils.
CC   -!- SUBUNIT: Interacts with a number of integral membrane proteins and
CC       cytoskeletal proteins. Binds SPTB/spectrin (beta chain) through a
CC       70 AA N-terminal region of the 62 kDa domain, and the C-terminal
CC       of SLC4A1/erythrocyte membrane protein band 3 through the ankyrin
CC       repeat region. Also interacts with TTN/titin. Isoform Mu7
CC       interacts with OBSN isoform 3/obscurin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform Er1: Cytoplasm, cytoskeleton (By
CC       similarity). Note=Probably the other erythrocyte (Er) isoforms,
CC       are located near the surface of erythrocytic plasma membrane (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform Mu7: Membrane (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform Mu8: Sarcoplasmic reticulum (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage, Alternative splicing; Named isoforms=8;
CC       Name=Er1;
CC         IsoId=Q02357-1; Sequence=Displayed;
CC         Note=Produced by alternative promoter usage;
CC       Name=Br2; Synonyms=Cb14/11;
CC         IsoId=Q02357-2; Sequence=VSP_018453, VSP_018455, VSP_018457;
CC         Note=Produced by alternative splicing of isoform Er1;
CC       Name=Er3; Synonyms=Er18;
CC         IsoId=Q02357-3; Sequence=VSP_018460;
CC         Note=Incomplete sequence. Produced by alternative splicing of
CC         isoform Er1;
CC       Name=Br4; Synonyms=Cb12;
CC         IsoId=Q02357-4; Sequence=VSP_018459;
CC         Note=Incomplete sequence. Produced by alternative splicing of
CC         isoform Er1;
CC       Name=5;
CC         IsoId=Q02357-5; Sequence=VSP_018454, VSP_018456;
CC         Note=Produced by alternative splicing of isoform Er1;
CC       Name=6;
CC         IsoId=Q02357-6; Sequence=VSP_018454, VSP_018455;
CC         Note=Produced by alternative splicing of isoform Er1;
CC       Name=Mu7; Synonyms=skAnk1;
CC         IsoId=Q02357-7; Sequence=VSP_018452, VSP_018458;
CC         Note=Produced by alternative promoter usage;
CC       Name=Mu8;
CC         IsoId=Q02357-8; Sequence=VSP_018452, VSP_018458, VSP_018460;
CC         Note=Produced by alternative splicing of isoform Mu7;
CC   -!- DOMAIN: The 55 kDa regulatory domain is involved in regulating
CC       binding of SPTB/spectrin (beta chain) and SLC4A1/erythrocyte
CC       membrane protein band 3 (By similarity).
CC   -!- DOMAIN: The ANK repeat region forms a spiral around a large
CC       central cavity and is involved in binding of ion transporters (By
CC       similarity).
CC   -!- PTM: Regulated by phosphorylation (By similarity).
CC   -!- PTM: Acylated by palmitic acid group(s) (By similarity).
CC   -!- SIMILARITY: Contains 23 ANK repeats.
CC   -!- SIMILARITY: Contains 1 death domain.
CC   -!- SIMILARITY: Contains 1 ZU5 domain.
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DR   EMBL; M84756; AAA37236.1; -; mRNA.
DR   EMBL; X69063; CAA48801.1; -; mRNA.
DR   EMBL; X69064; CAA48802.1; -; mRNA.
DR   EMBL; U73972; AAC24156.1; -; mRNA.
DR   EMBL; AK134267; BAE22074.1; -; mRNA.
DR   EMBL; AK147278; BAE27815.1; -; mRNA.
DR   EMBL; AK147597; BAE28015.1; -; mRNA.
DR   EMBL; AK158131; BAE34375.1; -; mRNA.
DR   EMBL; BC061219; AAH61219.1; -; mRNA.
DR   EMBL; U76758; AAB37323.1; -; Genomic_DNA.
DR   EMBL; U76758; AAB37324.1; -; Genomic_DNA.
DR   EMBL; U76758; AAB37325.1; -; Genomic_DNA.
DR   IPI; IPI00109307; -.
DR   IPI; IPI00119871; -.
DR   IPI; IPI00127163; -.
DR   IPI; IPI00474771; -.
DR   IPI; IPI00755019; -.
DR   IPI; IPI00755395; -.
DR   IPI; IPI00755993; -.
DR   IPI; IPI00757184; -.
DR   PIR; I49502; I49502.
DR   PIR; S37771; S37771.
DR   PIR; S37772; S37772.
DR   RefSeq; NP_001104253.1; NM_001110783.1.
DR   RefSeq; NP_112435.2; NM_031158.2.
DR   UniGene; Mm.334444; -.
DR   UniGene; Mm.476804; -.
DR   ProteinModelPortal; Q02357; -.
DR   SMR; Q02357; 2-808, 907-1064, 1396-1493.
DR   MINT; MINT-255055; -.
DR   STRING; Q02357; -.
DR   PhosphoSite; Q02357; -.
DR   PRIDE; Q02357; -.
DR   Ensembl; ENSMUST00000033947; ENSMUSP00000033947; ENSMUSG00000031543.
DR   Ensembl; ENSMUST00000072833; ENSMUSP00000072612; ENSMUSG00000031543.
DR   Ensembl; ENSMUST00000084037; ENSMUSP00000081050; ENSMUSG00000031543.
DR   Ensembl; ENSMUST00000084038; ENSMUSP00000081051; ENSMUSG00000031543.
DR   Ensembl; ENSMUST00000110685; ENSMUSP00000106313; ENSMUSG00000031543.
DR   Ensembl; ENSMUST00000110688; ENSMUSP00000106316; ENSMUSG00000031543.
DR   Ensembl; ENSMUST00000117662; ENSMUSP00000113531; ENSMUSG00000031543.
DR   GeneID; 11733; -.
DR   KEGG; mmu:11733; -.
DR   UCSC; uc009lee.1; mouse.
DR   UCSC; uc009lef.1; mouse.
DR   UCSC; uc009leg.1; mouse.
DR   UCSC; uc009lei.1; mouse.
DR   UCSC; uc009lel.1; mouse.
DR   UCSC; uc009lem.1; mouse.
DR   CTD; 11733; -.
DR   MGI; MGI:88024; Ank1.
DR   eggNOG; roNOG09288; -.
DR   GeneTree; ENSGT00600000084024; -.
DR   HOVERGEN; HBG004234; -.
DR   PhylomeDB; Q02357; -.
DR   NextBio; 279431; -.
DR   ArrayExpress; Q02357; -.
DR   Bgee; Q02357; -.
DR   CleanEx; MM_ANK1; -.
DR   Genevestigator; Q02357; -.
DR   GermOnline; ENSMUSG00000031543; Mus musculus.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0016529; C:sarcoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0048821; P:erythrocyte development; IMP:MGI.
DR   GO; GO:0015672; P:monovalent inorganic cation transport; IMP:MGI.
DR   GO; GO:0006779; P:porphyrin biosynthetic process; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR000488; Death.
DR   InterPro; IPR011029; DEATH-like.
DR   InterPro; IPR000906; ZU5.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 3.
DR   Gene3D; G3DSA:1.10.533.10; DEATH_like; 1.
DR   Pfam; PF00023; Ank; 18.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF00791; ZU5; 1.
DR   SMART; SM00248; ANK; 23.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00218; ZU5; 1.
DR   SUPFAM; SSF48403; ANK; 2.
DR   SUPFAM; SSF47986; DEATH_like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 20.
DR   PROSITE; PS50017; DEATH_DOMAIN; 1.
DR   PROSITE; PS51145; ZU5; 1.
PE   1: Evidence at protein level;
KW   Alternative promoter usage; Alternative splicing; ANK repeat;
KW   Cytoplasm; Cytoskeleton; Lipoprotein; Membrane; Phosphoprotein;
KW   Repeat; Sarcoplasmic reticulum.
FT   CHAIN         1   1862       Ankyrin-1.
FT                                /FTId=PRO_0000066884.
FT   REPEAT       40     69       ANK 1.
FT   REPEAT       73    102       ANK 2.
FT   REPEAT      106    135       ANK 3.
FT   REPEAT      139    168       ANK 4.
FT   REPEAT      170    197       ANK 5.
FT   REPEAT      201    230       ANK 6.
FT   REPEAT      234    263       ANK 7.
FT   REPEAT      267    296       ANK 8.
FT   REPEAT      300    329       ANK 9.
FT   REPEAT      333    362       ANK 10.
FT   REPEAT      366    395       ANK 11.
FT   REPEAT      399    428       ANK 12.
FT   REPEAT      432    461       ANK 13.
FT   REPEAT      465    494       ANK 14.
FT   REPEAT      498    527       ANK 15.
FT   REPEAT      531    560       ANK 16.
FT   REPEAT      564    593       ANK 17.
FT   REPEAT      597    626       ANK 18.
FT   REPEAT      630    659       ANK 19.
FT   REPEAT      663    692       ANK 20.
FT   REPEAT      696    725       ANK 21.
FT   REPEAT      729    758       ANK 22.
FT   REPEAT      762    791       ANK 23.
FT   DOMAIN      907   1014       ZU5.
FT   DOMAIN     1399   1483       Death.
FT   REGION        1    827       89 kDa domain.
FT   REGION     1387   1862       55 kDa regulatory domain.
FT   MOD_RES     830    830       Phosphoserine (By similarity).
FT   MOD_RES     852    852       Phosphoserine.
FT   MOD_RES     862    862       Phosphothreonine.
FT   MOD_RES    1069   1069       Phosphotyrosine.
FT   MOD_RES    1673   1673       Phosphothreonine (By similarity).
FT   MOD_RES    1675   1675       Phosphoserine (By similarity).
FT   VAR_SEQ       1   1707       Missing (in isoform Mu7 and isoform Mu8).
FT                                /FTId=VSP_018452.
FT   VAR_SEQ       1      5       MGFCK -> MAERPRRSGSDPA (in isoform Br2).
FT                                /FTId=VSP_018453.
FT   VAR_SEQ       1      4       MGFC -> MAQAAKQLKKIKDIEAQALQEQKEKEESNRKRR
FT                                NRSRDRKK (in isoform 5 and isoform 6).
FT                                /FTId=VSP_018454.
FT   VAR_SEQ     817    817       G -> GTAHISIMG (in isoform Br2 and
FT                                isoform 6).
FT                                /FTId=VSP_018455.
FT   VAR_SEQ    1510   1664       Missing (in isoform 5).
FT                                /FTId=VSP_018456.
FT   VAR_SEQ    1636   1665       Missing (in isoform Br2).
FT                                /FTId=VSP_018457.
FT   VAR_SEQ    1708   1780       SSWQEEVTQGPHSFQRRITTIQGPEPGALQEYEQVLVSTRE
FT                                HVQRGPPETGSPKAGKEPSLWAPESAFSQEVQ -> MWTFI
FT                                TQLLVTLVLLGFFLVSCQNVMHIVKGSLCFVLKHIHQELDK
FT                                ELGESEGLSDDEETISTRVVRRRVFLK (in isoform
FT                                Mu7 and isoform Mu8).
FT                                /FTId=VSP_018458.
FT   VAR_SEQ    1831   1831       V -> VIVEGPLADPGDLEADIESFMKLTKV (in
FT                                isoform Br4).
FT                                /FTId=VSP_018459.
FT   VAR_SEQ    1832   1862       ELRGSGLQPDLIEGRKGAQIVKRASLKRGKQ -> IVEGPL
FT                                ADPGDLEADIESFMKLTKDHTSTPKP (in isoform
FT                                Er3 and isoform Mu8).
FT                                /FTId=VSP_018460.
FT   CONFLICT    507    507       A -> T (in Ref. 3; BAE34375).
FT   CONFLICT    678    678       P -> L (in Ref. 1; AAA37236).
FT   CONFLICT    818    818       D -> G (in Ref. 3; BAE34375).
FT   CONFLICT   1098   1098       K -> N (in Ref. 2; CAA48801).
FT   CONFLICT   1481   1481       G -> V (in Ref. 2; CAA48801).
FT   CONFLICT   1541   1541       T -> A (in Ref. 3; BAE27815/BAE28015).
FT   CONFLICT   1644   1644       K -> R (in Ref. 3; BAE28015).
SQ   SEQUENCE   1862 AA;  204227 MW;  B5F3EBB447C3485D CRC64;
     MGFCKADAAT SFLRAARSGN LDKALDHLRN GVDINTCNQN GLNGLHLASK EGHVKMVVEL
     LHKEIILETT TKKGNTALHI AALAGQDEVV RELVNYGANV NAQSQKGFTP LYMAAQENHL
     EVVKFLLENG ANQNVATEDG FTPLAVALQQ GHENVVAHLI NYGTKGKVRL PALHIAARND
     DTRTAAVLLQ NDPNPDVLSK TGFTPLHIAA HYENLNVAQL LLNRGASVNF TPQNGITPLH
     IASRRGNVIM VRLLLDRGAQ IETRTKDELT PLHCAARNGH VRISEILLDH GAPIQAKTKN
     GLSPIHMAAQ GDHLDCVRLL LQYNAEIDDI TLDHLTPLHV AAHCGHHRVA KVLLDKGAKP
     NSRALNGFTP LHIACKKNHI RVMELLLKTG ASIDAVTESG LTPLHVASFM GHLPIVKNLL
     QRGASPNVSN VKVETPLHMA ARAGHTEVAK YLLQNKAKAN AKAKDDQTPL HCAARIGHTG
     MVKLLLENGA SPNLATTAGH TPLHTAAREG HVDTALALLE KEASQACMTK KGFTPLHVAA
     KYGKVRLAEL LLEHDAHPNA AGKNGLTPLH VAVHHNNLDI VKLLLPRGGS PHSPAWNGYT
     PLHIAAKQNQ IEVARSLLQY GGSANAESVQ GVTPLHLAAQ EGHTEMVALL LSKQANGNLG
     NKSGLTPLHL VSQEGHVPVA DVLIKHGVTV DATTRMGYTP LHVASHYGNI KLVKFLLQHQ
     ADVNAKTKLG YSPLHQAAQQ GHTDIVTLLL KNGASPNEVS SNGTTPLAIA KRLGYISVTD
     VLKVVTDETS VVLVSDKHRM SYPETVDEIL DVSEDEGDEL VGSKAERRDS RDVGEEKELL
     DFVPKLDQVV ESPAIPRIPC VTPETVVIRS EDQEQASKEY DEDSLIPSSP ATETSDNISP
     VASPVHTGFL VSFMVDARGG SMRGSRHNGL RVVIPPRTCA APTRITCRLV KPQKLNTPPP
     LAEEEGLASR IIALGPTGAQ FLSPVIVEIP HFASHGRGDR ELVVLRSENG SVWKEHKSRY
     GESYLDQILN GMDEELGSLE ELEKKRVCRI ITTDFPLYFV IMSRLCQDYD TIGPEGGSLR
     SKLVPLVQAT FPENAVTKKV KLALQAQPVP DELVTKLLGN QATFSPIVTV EPRRRKFHRP
     IGLRIPLPPS WTDNPRDSGE GDTTSLRLLC SVIGGTDQAQ WEDITGTTKL IYANECANFT
     TNVSARFWLS DCPRTAEAVH FATLLYKELT AVPYMAKFVI FAKMNDAREG RLRCYCMTDD
     KVDKTLEQHE NFVEVARSRD IEVLEGMPLF AELSGNLVPV KKAAQQRSFH FQSFRENRLA
     IPVKVRDSSR EPGGFLSFLR KTMKYEDTQH ILCHLNITMP PCTKGSGAED RRRTLTPLTL
     RYSILSESRL GFTSDTDRVE MRMAVIREHL GLSWAELARE LQFSVEDINR IRVENPNSLL
     DQSTALLTLW VDREGENAKM ENLYTALRNI DRSEIVNMLE GSGRQSRNLK PERRHGDREY
     SLSPSQVNGY SSLQDELLSP ASLQYALPSP LCADQYWNEV TVIDAIPLAA TEHDTMLEMS
     DMQVWSAGLT PSLVTAEDSS LECSKAEDSD AIPEWKLEGA HSEDTQGPEL GSQDLVEDDT
     VDSDATNGLA DLLGQEEGQR SEKKRQEVSG TEQDTETEVS LVSGQQRVHA RITDSPSVRQ
     VLDRSQARTL DWDKQGSTAV HPQEATQSSW QEEVTQGPHS FQRRITTIQG PEPGALQEYE
     QVLVSTREHV QRGPPETGSP KAGKEPSLWA PESAFSQEVQ GDELQNIPGE QVTEEQFTDE
     QGNIVTKKII RKVVRQVDSS GAIDTQQHEE VELRGSGLQP DLIEGRKGAQ IVKRASLKRG
     KQ
//
ID   NFIA_MOUSE              Reviewed;         532 AA.
AC   Q02780; P70250; P70251; Q3UUZ2; Q61960; Q8VBT5; Q9R1G5;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 108.
DE   RecName: Full=Nuclear factor 1 A-type;
DE            Short=NF1-A;
DE            Short=Nuclear factor 1/A;
DE   AltName: Full=CCAAT-box-binding transcription factor;
DE            Short=CTF;
DE   AltName: Full=Nuclear factor I/A;
DE            Short=NF-I/A;
DE            Short=NFI-A;
DE   AltName: Full=TGGCA-binding protein;
GN   Name=Nfia;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), AND PARTIAL
RP   NUCLEOTIDE SEQUENCE (ISOFORM 6).
RC   TISSUE=Brain;
RX   MEDLINE=91035434; PubMed=1699939;
RA   Inoue T., Tamura T.A., Furuichi T., Mikoshiba K.;
RT   "Isolation of complementary DNAs encoding a cerebellum-enriched
RT   nuclear factor I family that activates transcription from the mouse
RT   myelin basic protein promoter.";
RL   J. Biol. Chem. 265:19065-19070(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 7).
RC   STRAIN=C57BL/6J, and DBA/2J; TISSUE=Brain;
RX   MEDLINE=21975488; PubMed=11978849;
RA   Fehr C., Shirley R.L., Belknap J.K., Crabbe J.C., Buck K.J.;
RT   "Congenic mapping of alcohol and pentobarbital withdrawal liability
RT   loci to a <1 centimorgan interval of murine chromosome 4:
RT   identification of Mpdz as a candidate gene.";
RL   J. Neurosci. 22:3730-3738(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 5).
RC   STRAIN=NIH Swiss; TISSUE=Embryo;
RX   MEDLINE=22456605; PubMed=12568726; DOI=10.1016/S0378-1119(02)01204-0;
RA   Gruender A., Qian F., Ebel T.T., Mincheva A., Lichter P., Kruse U.,
RA   Sippel A.E.;
RT   "Genomic organization, splice products and mouse chromosomal
RT   localization of genes for transcription factor Nuclear Factor One.";
RL   Gene 304:171-181(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC   STRAIN=C57BL/6J; TISSUE=Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2-509 (ISOFORM 1).
RC   STRAIN=BALB/c;
RX   MEDLINE=97209336; PubMed=9056636;
RX   DOI=10.1002/(SICI)1097-0177(199703)208:3<313::AID-AJA3>3.3.CO;2-2;
RA   Chaudhry A.Z., Lyons G.E., Gronostajski R.M.;
RT   "Expression patterns of the four nuclear factor I genes during mouse
RT   embryogenesis indicate a potential role in development.";
RL   Dev. Dyn. 208:313-325(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-209.
RC   STRAIN=129;
RX   MEDLINE=99189145; PubMed=10087299; DOI=10.1007/s003359901008;
RA   Fletcher C.F., Jenkins N.A., Copeland N.G., Chaudhry A.Z.,
RA   Gronostajski R.M.;
RT   "Exon structure of the nuclear factor I DNA-binding domain from C.
RT   elegans to mammals.";
RL   Mamm. Genome 10:390-396(1999).
RN   [7]
RP   NITRATION [LARGE SCALE ANALYSIS] AT TYR-2 (ISOFORMS 1/5/7), AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16800626; DOI=10.1021/bi060474w;
RA   Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
RA   Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
RA   Squier T.C., Bigelow D.J.;
RT   "Endogenously nitrated proteins in mouse brain: links to
RT   neurodegenerative disease.";
RL   Biochemistry 45:8009-8022(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303; SER-310; SER-323
RP   AND SER-342, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Recognizes and binds the palindromic sequence 5'-
CC       TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in
CC       the origin of replication of adenovirus type 2. These proteins are
CC       individually capable of activating transcription and replication.
CC   -!- SUBUNIT: Binds DNA as a homodimer.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=2;
CC         IsoId=Q02780-1; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q02780-2; Sequence=VSP_003537, VSP_003544;
CC         Note=Nitrated on Tyr-2;
CC       Name=3;
CC         IsoId=Q02780-3; Sequence=VSP_003538;
CC       Name=4;
CC         IsoId=Q02780-4; Sequence=VSP_003539;
CC         Note=Incomplete sequence. Nitrated on Tyr-2;
CC       Name=5;
CC         IsoId=Q02780-5; Sequence=VSP_003537, VSP_003541;
CC         Note=Incomplete sequence;
CC       Name=6;
CC         IsoId=Q02780-6; Sequence=VSP_003540, VSP_003542, VSP_003543;
CC         Note=Incomplete sequence;
CC       Name=7;
CC         IsoId=Q02780-7; Sequence=VSP_003537;
CC         Note=Nitrated on Tyr-2;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the CTF/NF-I family.
CC   -!- SIMILARITY: Contains 1 CTF/NF-I DNA-binding domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; D90172; BAA20909.1; -; mRNA.
DR   EMBL; D90173; BAA14203.1; -; mRNA.
DR   EMBL; D90174; BAA14204.1; -; mRNA.
DR   EMBL; D90175; BAA14205.1; -; mRNA.
DR   EMBL; D90176; BAA14206.1; -; mRNA.
DR   EMBL; AF326554; AAL37400.1; -; mRNA.
DR   EMBL; AF326553; AAL37399.1; -; mRNA.
DR   EMBL; Y07690; CAA68954.1; -; mRNA.
DR   EMBL; Y07691; CAA68955.1; -; mRNA.
DR   EMBL; AK137731; BAE23481.1; -; mRNA.
DR   EMBL; AK052204; BAC34883.1; -; mRNA.
DR   EMBL; U57633; AAB49928.1; -; mRNA.
DR   EMBL; AF111263; AAD39098.1; -; Genomic_DNA.
DR   IPI; IPI00131415; -.
DR   IPI; IPI00229824; -.
DR   IPI; IPI00229825; -.
DR   IPI; IPI00229826; -.
DR   IPI; IPI00229827; -.
DR   IPI; IPI00310676; -.
DR   IPI; IPI00889946; -.
DR   PIR; B36596; B36596.
DR   RefSeq; NP_001116424.1; NM_001122952.1.
DR   RefSeq; NP_001116425.1; NM_001122953.1.
DR   RefSeq; NP_035035.1; NM_010905.3.
DR   UniGene; Mm.31274; -.
DR   UniGene; Mm.409646; -.
DR   STRING; Q02780; -.
DR   PhosphoSite; Q02780; -.
DR   PRIDE; Q02780; -.
DR   Ensembl; ENSMUST00000075448; ENSMUSP00000074899; ENSMUSG00000028565.
DR   Ensembl; ENSMUST00000097969; ENSMUSP00000095582; ENSMUSG00000028565.
DR   Ensembl; ENSMUST00000107061; ENSMUSP00000102676; ENSMUSG00000028565.
DR   Ensembl; ENSMUST00000107062; ENSMUSP00000102677; ENSMUSG00000028565.
DR   GeneID; 18027; -.
DR   KEGG; mmu:18027; -.
DR   UCSC; uc008ttq.1; mouse.
DR   UCSC; uc008ttt.1; mouse.
DR   UCSC; uc008ttu.1; mouse.
DR   UCSC; uc008ttv.1; mouse.
DR   CTD; 18027; -.
DR   MGI; MGI:108056; Nfia.
DR   eggNOG; roNOG08414; -.
DR   HOVERGEN; HBG006561; -.
DR   InParanoid; Q02780; -.
DR   OMA; XSPHATP; -.
DR   OrthoDB; EOG4ZKJM9; -.
DR   PhylomeDB; Q02780; -.
DR   NextBio; 293095; -.
DR   PMAP-CutDB; Q02780; -.
DR   ArrayExpress; Q02780; -.
DR   Bgee; Q02780; -.
DR   CleanEx; MM_NFIA; -.
DR   Genevestigator; Q02780; -.
DR   GermOnline; ENSMUSG00000028565; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0016563; F:transcription activator activity; IDA:MGI.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0010552; P:positive regulation of gene-specific transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   InterPro; IPR000647; CTF/NFI.
DR   InterPro; IPR020604; CTF/NFI_DNA-bd-dom.
DR   InterPro; IPR019739; CTF/NFI_DNA-bd_CS.
DR   InterPro; IPR019548; CTF/NFI_DNA-bd_N.
DR   InterPro; IPR003619; MAD_homology1_Dwarfin-type.
DR   PANTHER; PTHR11492; CTF_NFI; 1.
DR   Pfam; PF00859; CTF_NFI; 1.
DR   Pfam; PF03165; MH1; 1.
DR   Pfam; PF10524; NfI_DNAbd_pre-N; 1.
DR   SMART; SM00523; DWA; 1.
DR   PROSITE; PS00349; CTF_NFI_1; 1.
DR   PROSITE; PS51080; CTF_NFI_2; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; DNA replication; DNA-binding;
KW   Nitration; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    532       Nuclear factor 1 A-type.
FT                                /FTId=PRO_0000100192.
FT   DNA_BIND     24    217       CTF/NF-I.
FT   MOD_RES     281    281       Phosphoserine (By similarity).
FT   MOD_RES     288    288       Phosphoserine (By similarity).
FT   MOD_RES     303    303       Phosphoserine.
FT   MOD_RES     310    310       Phosphoserine.
FT   MOD_RES     323    323       Phosphoserine.
FT   MOD_RES     328    328       Phosphoserine (By similarity).
FT   MOD_RES     342    342       Phosphoserine.
FT   VAR_SEQ       1     32       MKLADSVMAGKASDGSIKWQLCYDISARTWWM -> MYSPL
FT                                CLTQ (in isoform 1, isoform 5 and isoform
FT                                7).
FT                                /FTId=VSP_003537.
FT   VAR_SEQ       1     32       MKLADSVMAGKASDGSIKWQLCYDISARTWWM -> VWFQQ
FT                                PLPFADLLPGNSIHTASPTCLTQ (in isoform 4).
FT                                /FTId=VSP_003539.
FT   VAR_SEQ       1     32       MKLADSVMAGKASDGSIKWQLCYDISARTWWM -> LSPPL
FT                                SPSRTHTHAHLQPAHRRARTPRRPAVMYSPLCLTQ (in
FT                                isoform 6).
FT                                /FTId=VSP_003540.
FT   VAR_SEQ       1     31       Missing (in isoform 3).
FT                                /FTId=VSP_003538.
FT   VAR_SEQ     339    381       Missing (in isoform 5).
FT                                /FTId=VSP_003541.
FT   VAR_SEQ     340    370       LPSPSTLKKSEKSGFSSPSPSQTSSLGTAFT -> EQSHKR
FT                                EGNGVCVWLCCHGRVVESSRYNGSA (in isoform 6).
FT                                /FTId=VSP_003542.
FT   VAR_SEQ     371    532       Missing (in isoform 6).
FT                                /FTId=VSP_003543.
FT   VAR_SEQ     476    532       Missing (in isoform 1).
FT                                /FTId=VSP_003544.
SQ   SEQUENCE   532 AA;  58553 MW;  3AECEEDCD65D28B3 CRC64;
     MKLADSVMAG KASDGSIKWQ LCYDISARTW WMDEFHPFIE ALLPHVRAFA YTWFNLQARK
     RKYFKKHEKR MSKEEERAVK DELLSEKPEV KQKWASRLLA KLRKDIRPEY REDFVLTVTG
     KKPPCCVLSN PDQKGKMRRI DCLRQADKVW RLDLVMVILF KGIPLESTDG ERLVKSPQCS
     NPGLCVQPHH IGVSVKELDL YLAYFVHAAD SSQSESPSQP SEADIKDQPE NGHLGFQDSF
     VTSGVFSVTE LVRVSQTPIA AGTGPNFSLS DLESSSYYSM SPGAMRRSLP STSSTSSTKR
     LKSVEDEMDS PGEEPFYTGQ GRSPGSGSQS SGWHEVEPGL PSPSTLKKSE KSGFSSPSPS
     QTSSLGTAFT QHHRPVITGP RASPHATPST LHFPTSPIIQ QPGPYFSHPA IRYHPQETLK
     EFVQLVCPDA GQQAGQVGFL NPNGSSQGKV HNPFLPTPML PPPPPPPMAR PVPLPMPDTK
     PPTTSTEGGA ASPTSPTYST PSTSPANRFV SVGPRDPSFV NIPQQTQSWY LG
//
ID   NUCB1_MOUSE             Reviewed;         459 AA.
AC   Q02819; Q3TU42; Q9CWA1; Q9D8J4; Q9DBL3;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2001, sequence version 2.
DT   08-MAR-2011, entry version 106.
DE   RecName: Full=Nucleobindin-1;
DE   AltName: Full=CALNUC;
DE   Flags: Precursor;
GN   Name=Nucb1; Synonyms=Nuc, Nucb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=92392352; PubMed=1520323; DOI=10.1016/S0006-291X(05)81503-7;
RA   Miura K., Titani K., Kurosawa Y., Kanai Y.;
RT   "Molecular cloning of nucleobindin, a novel DNA-binding protein that
RT   contains both a signal peptide and a leucine zipper structure.";
RL   Biochem. Biophys. Res. Commun. 187:375-380(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Corpus striatum, Head, Kidney, Liver, Pancreas, and
RC   Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION AT SER-85.
RX   PubMed=15378723; DOI=10.1002/rcm.1604;
RA   Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.;
RT   "Phosphoproteome analysis of mouse liver using immobilized metal
RT   affinity purification and linear ion trap mass spectrometry.";
RL   Rapid Commun. Mass Spectrom. 18:2169-2176(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Major calcium-binding protein of the Golgi. May have a
CC       role in calcium homeostasis (By similarity).
CC   -!- SUBUNIT: Interacts with GNAI2 and GNAI3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane;
CC       Peripheral membrane protein; Lumenal side. Cytoplasm. Note=A small
CC       fraction of the protein may be cytoplasmic. In lupus prone, but
CC       not in normal mice, at least part of it is in the serum where it
CC       induces the formation of autoantibodies including anti-DNA
CC       antibodies.
CC   -!- TISSUE SPECIFICITY: Lymphoid cells as well as other somatic cells,
CC       such as liver and kidney cells.
CC   -!- DOMAIN: The EF-hand domains are unfolded in the absence of Ca(2+)
CC       and fold upon Ca(2+) addition (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- MISCELLANEOUS: Discovered as DNA-binding protein in the serum of
CC       lupus-prone mice.
CC   -!- SIMILARITY: Belongs to the nucleobindin family.
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
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DR   EMBL; M96823; AAA39842.1; -; mRNA.
DR   EMBL; AK002630; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK004886; BAB23644.1; -; mRNA.
DR   EMBL; AK007976; BAB25383.1; -; mRNA.
DR   EMBL; AK140710; BAE24451.1; -; mRNA.
DR   EMBL; AK160981; BAE36129.1; -; mRNA.
DR   EMBL; AK164088; BAE37619.1; -; mRNA.
DR   EMBL; BC072554; AAH72554.1; -; mRNA.
DR   IPI; IPI00132314; -.
DR   PIR; JC1224; JC1224.
DR   RefSeq; NP_001157134.1; NM_001163662.1.
DR   RefSeq; NP_032775.1; NM_008749.2.
DR   UniGene; Mm.258923; -.
DR   ProteinModelPortal; Q02819; -.
DR   SMR; Q02819; 227-325.
DR   STRING; Q02819; -.
DR   PhosphoSite; Q02819; -.
DR   PRIDE; Q02819; -.
DR   Ensembl; ENSMUST00000033096; ENSMUSP00000033096; ENSMUSG00000030824.
DR   GeneID; 18220; -.
DR   KEGG; mmu:18220; -.
DR   UCSC; uc009gvm.1; mouse.
DR   CTD; 18220; -.
DR   MGI; MGI:97388; Nucb1.
DR   eggNOG; roNOG14168; -.
DR   HOGENOM; HBG713576; -.
DR   HOVERGEN; HBG052685; -.
DR   InParanoid; Q02819; -.
DR   OMA; LERGAPK; -.
DR   OrthoDB; EOG4N04F6; -.
DR   PhylomeDB; Q02819; -.
DR   NextBio; 293636; -.
DR   ArrayExpress; Q02819; -.
DR   Bgee; Q02819; -.
DR   CleanEx; MM_NUCB1; -.
DR   Genevestigator; Q02819; -.
DR   GermOnline; ENSMUSG00000030824; Mus musculus.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   1: Evidence at protein level;
KW   Calcium; Coiled coil; Cytoplasm; Direct protein sequencing;
KW   DNA-binding; Golgi apparatus; Membrane; Phosphoprotein; Repeat;
KW   Signal.
FT   SIGNAL        1     25       Potential.
FT   CHAIN        26    459       Nucleobindin-1.
FT                                /FTId=PRO_0000004163.
FT   DOMAIN      239    274       EF-hand 1.
FT   DOMAIN      291    326       EF-hand 2.
FT   DNA_BIND    171    217       Potential.
FT   CA_BIND     252    263       1 (By similarity).
FT   CA_BIND     304    315       2 (By similarity).
FT   REGION      227    320       Binds to GNAI2 and GNAI3 (By similarity).
FT   COILED      149    217       Potential.
FT   COILED      340    407       Potential.
FT   MOD_RES      81     81       Phosphoserine (By similarity).
FT   MOD_RES      85     85       Phosphoserine.
FT   MOD_RES     178    178       Phosphotyrosine (By similarity).
FT   MOD_RES     223    223       Phosphoserine (By similarity).
FT   MOD_RES     368    368       Phosphoserine.
FT   MOD_RES     371    371       Phosphothreonine (By similarity).
FT   MOD_RES     456    456       Phosphoserine.
FT   CONFLICT     42     42       E -> D (in Ref. 2; BAB25383).
FT   CONFLICT    146    146       H -> E (in Ref. 1; AA sequence).
FT   CONFLICT    151    151       R -> I (in Ref. 1; AA sequence).
FT   CONFLICT    390    393       Missing (in Ref. 1; AAA39842).
SQ   SEQUENCE   459 AA;  53409 MW;  1CC1102D216CC60B CRC64;
     MPTSVPRGAP FLLLPPLLML SAVLAVPVDR AAPPQEDSQA TETPDTGLYY HRYLQEVINV
     LETDGHFREK LQAANAEDIK SGKLSQELDF VSHNVRTKLD ELKRQEVSRL RMLLKAKMDA
     KQEPNLQVDH MNLLKQFEHL DPQNQHTFEA RDLELLIQTA TRDLAQYDAA HHEEFKRYEM
     LKEHERRRYL ESLGEEQRKE AERKLQEQQR RHREHPKVNV PGSQAQLKEV WEELDGLDPN
     RFNPKTFFIL HDINSDGVLD EQELEALFTK ELEKVYDPKN EEDDMREMEE ERLRMREHVM
     KNVDTNQDRL VTLEEFLAST QRKEFGDTGE GWKTVEMSPA YTEEELKRFE EELAAREAEL
     NARAQRLSQE TEALGRSQDR LEAQKRELQQ AVLQMEQRKQ QLQEQSAPPS KPDGQLQFRA
     DTDDAPVPAP AGDQKDVPAS EKKVPEQPPE LPQLDSQHL
//
ID   MARK3_MOUSE             Reviewed;         753 AA.
AC   Q03141; Q3TM40; Q3V1U3; Q8C6G9; Q8R375; Q9JKE4;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 2.
DT   08-MAR-2011, entry version 100.
DE   RecName: Full=MAP/microtubule affinity-regulating kinase 3;
DE            EC=2.7.11.1;
DE   AltName: Full=ELKL motif kinase 2;
DE            Short=EMK-2;
DE   AltName: Full=MPK-10;
GN   Name=Mark3; Synonyms=Emk2, Mpk10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RA   Darmon Y., Tornier C., Bessone S., Le Morvan V.;
RT   "Mouse EMK2 (ELKL motif kinase 2).";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Lung, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 168-753 (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 180-234.
RC   STRAIN=C57BL/6; TISSUE=Embryonic brain;
RX   MEDLINE=93096484; PubMed=1281307;
RA   Gilardi-Hebenstreit P., Nieto M.A., Frain M., Mattei M.-G.,
RA   Chestier A., Wilkinson D.G., Charnay P.;
RT   "An Eph-related receptor protein tyrosine kinase gene segmentally
RT   expressed in the developing mouse hindbrain.";
RL   Oncogene 7:2499-2506(1992).
RN   [5]
RP   STRUCTURE BY NMR OF 659-753.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of kinase associated domain 1 of mouse
RT   MAP/microtubule affinity-regulating kinase 3.";
RL   Submitted (MAR-2004) to the PDB data bank.
CC   -!- FUNCTION: Involved in the specific phosphorylation of microtubule-
CC       associated proteins for tau, MAP2 and MAP4. Phosphorylates CDC25C
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q03141-1; Sequence=Displayed;
CC       Name=2; Synonyms=ELKL motif kinase 2 short form;
CC         IsoId=Q03141-2; Sequence=VSP_016140;
CC       Name=3; Synonyms=ELKL motif kinase 2 long form;
CC         IsoId=Q03141-3; Sequence=VSP_016141;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. MARK subfamily.
CC   -!- SIMILARITY: Contains 1 KA1 (kinase-associated) domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 UBA domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH26445.1; Type=Erroneous initiation;
CC       Sequence=BAC35922.1; Type=Erroneous initiation;
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DR   EMBL; AF240783; AAF64456.1; -; mRNA.
DR   EMBL; AK075742; BAC35922.1; ALT_INIT; mRNA.
DR   EMBL; AK132247; BAE21056.1; -; mRNA.
DR   EMBL; AK166157; BAE38602.1; -; mRNA.
DR   EMBL; BC026445; AAH26445.1; ALT_INIT; mRNA.
DR   EMBL; X57244; CAA40520.1; -; mRNA.
DR   IPI; IPI00279494; -.
DR   IPI; IPI00312620; -.
DR   IPI; IPI00625061; -.
DR   PIR; S30496; S30496.
DR   RefSeq; NP_067491.2; NM_021516.4.
DR   RefSeq; NP_073712.2; NM_022801.4.
DR   UniGene; Mm.260504; -.
DR   UniGene; Mm.408955; -.
DR   UniGene; Mm.420865; -.
DR   PDB; 1UL7; NMR; -; A=659-753.
DR   PDB; 1V5S; NMR; -; A=674-753.
DR   PDBsum; 1UL7; -.
DR   PDBsum; 1V5S; -.
DR   ProteinModelPortal; Q03141; -.
DR   SMR; Q03141; 50-366, 657-753.
DR   STRING; Q03141; -.
DR   PhosphoSite; Q03141; -.
DR   PRIDE; Q03141; -.
DR   Ensembl; ENSMUST00000007555; ENSMUSP00000007555; ENSMUSG00000007411.
DR   Ensembl; ENSMUST00000075281; ENSMUSP00000074757; ENSMUSG00000007411.
DR   Ensembl; ENSMUST00000084953; ENSMUSP00000082017; ENSMUSG00000007411.
DR   GeneID; 17169; -.
DR   KEGG; mmu:17169; -.
DR   UCSC; uc007pdk.1; mouse.
DR   UCSC; uc007pdl.1; mouse.
DR   CTD; 17169; -.
DR   MGI; MGI:1341865; Mark3.
DR   eggNOG; roNOG09909; -.
DR   HOGENOM; HBG315019; -.
DR   HOVERGEN; HBG052453; -.
DR   InParanoid; Q03141; -.
DR   OMA; STIPDQR; -.
DR   OrthoDB; EOG4QFWCQ; -.
DR   PhylomeDB; Q03141; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 291458; -.
DR   ArrayExpress; Q03141; -.
DR   Bgee; Q03141; -.
DR   CleanEx; MM_MARK3; -.
DR   Genevestigator; Q03141; -.
DR   GermOnline; ENSMUSG00000007411; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR001772; Kinase-assoc_KA1.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   Gene3D; G3DSA:3.30.310.80; Kinase-assoc_KA1; 1.
DR   Pfam; PF02149; KA1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF103243; Kinase-assoc_KA1; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50032; KA1; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN         1    753       MAP/microtubule affinity-regulating
FT                                kinase 3.
FT                                /FTId=PRO_0000086305.
FT   DOMAIN       56    307       Protein kinase.
FT   DOMAIN      326    365       UBA.
FT   DOMAIN      695    744       KA1.
FT   NP_BIND      62     70       ATP (By similarity).
FT   COMPBIAS    374    412       Ser-rich.
FT   ACT_SITE    178    178       Proton acceptor (By similarity).
FT   BINDING      85     85       ATP (By similarity).
FT   MOD_RES       2      2       Phosphoserine (By similarity).
FT   MOD_RES       3      3       Phosphothreonine (By similarity).
FT   MOD_RES      42     42       Phosphoserine (By similarity).
FT   MOD_RES      61     61       Phosphothreonine (By similarity).
FT   MOD_RES     211    211       Phosphothreonine (By similarity).
FT   MOD_RES     340    340       Phosphotyrosine (By similarity).
FT   MOD_RES     341    341       Phosphoserine (By similarity).
FT   MOD_RES     374    374       Phosphoserine (By similarity).
FT   MOD_RES     376    376       Phosphoserine (By similarity).
FT   MOD_RES     377    377       Phosphoserine (By similarity).
FT   MOD_RES     378    378       Phosphoserine (By similarity).
FT   MOD_RES     379    379       Phosphoserine (By similarity).
FT   MOD_RES     380    380       Phosphoserine (By similarity).
FT   MOD_RES     383    383       Phosphoserine (By similarity).
FT   MOD_RES     397    397       Phosphothreonine (By similarity).
FT   MOD_RES     400    400       Phosphoserine (By similarity).
FT   MOD_RES     418    418       Phosphotyrosine (By similarity).
FT   MOD_RES     419    419       Phosphoserine (By similarity).
FT   MOD_RES     436    436       Phosphoserine (By similarity).
FT   MOD_RES     438    438       Phosphothreonine (By similarity).
FT   MOD_RES     455    455       Phosphoserine (By similarity).
FT   MOD_RES     456    456       Phosphoserine (By similarity).
FT   MOD_RES     469    469       Phosphoserine (By similarity).
FT   MOD_RES     494    494       Phosphoserine (By similarity).
FT   MOD_RES     499    499       Phosphoserine (By similarity).
FT   MOD_RES     536    536       Phosphothreonine (By similarity).
FT   MOD_RES     540    540       Phosphoserine (By similarity).
FT   MOD_RES     541    541       Phosphothreonine (By similarity).
FT   MOD_RES     543    543       Phosphoserine (By similarity).
FT   MOD_RES     545    545       Phosphoserine (By similarity).
FT   MOD_RES     549    549       Phosphothreonine (By similarity).
FT   MOD_RES     583    583       Phosphoserine (By similarity).
FT   MOD_RES     585    585       Phosphoserine (By similarity).
FT   MOD_RES     587    587       Phosphoserine (By similarity).
FT   MOD_RES     591    591       Phosphothreonine (By similarity).
FT   MOD_RES     598    598       Phosphoserine (By similarity).
FT   MOD_RES     601    601       Phosphoserine (By similarity).
FT   MOD_RES     639    639       Phosphoserine (By similarity).
FT   MOD_RES     643    643       Phosphoserine (By similarity).
FT   VAR_SEQ     615    638       Missing (in isoform 2).
FT                                /FTId=VSP_016140.
FT   VAR_SEQ     615    623       Missing (in isoform 3).
FT                                /FTId=VSP_016141.
FT   CONFLICT    333    333       D -> V (in Ref. 2; BAC35922).
FT   CONFLICT    496    496       N -> S (in Ref. 1; AAF64456).
FT   CONFLICT    511    511       S -> G (in Ref. 2; BAC35922).
FT   CONFLICT    684    684       D -> G (in Ref. 2; BAC35922).
FT   HELIX       672    685
FT   STRAND      689    692
FT   STRAND      698    702
FT   HELIX       707    709
FT   STRAND      711    719
FT   STRAND      721    735
FT   HELIX       737    750
SQ   SEQUENCE   753 AA;  84390 MW;  B597BDD0398617CF CRC64;
     MSTRTPLPTV NERDTENHIS HGDGRQEVTS RTGRSGARCR NSIASCADEQ PHIGNYRLLK
     TIGKGNFAKV KLARHILTGR EVAIKIIDKT QLNPTSLQKL FREVRIMKIL NHPNIVKLFE
     VIETEKTLYL IMEYASGGEV FDYLVAHGRM KEKEARAKFR QIVSAVQYCH QKRIVHRDLK
     AENLLLDADM NIKIADFGFS NEFTVGSKLD TFCGSPPYAA PELFQGKKYD GPEVDVWSLG
     VILYTLVSGS LPFDGQNLKE LRERVLRGKY RIPFYMSTDC ENLLKRFLVL NPVKRGTLEQ
     IMKDRWINAG HEEDELKPFV EPELDISDQK RIDIMVGMGY SQEEIQESLS KMKYDEITAT
     YLLLGRKSAE LDASDSSSSS NLSLAKVRPN SDLSNSTGQS PHHKGQRSVS SSQKQRRYSD
     HAGPAIPSVV AYPKRSQTST ADSDLKEDGI PSRKSSSSAV GGKGIAPASP MLGNAGNPNK
     ADIPERKKSP AVPSSNTASG GMTRRNTYVC SERCAADRHS VIQNGKENSA IPDERTPVAS
     THSISSATTP DRIRFPRGTA SRSTFHGQPR ERRTATYNGP PASPSLSHEA TPLSQTRSRG
     STNLFSKLTS KLTRRNMSFR FIKRLPTEYE RNGRYEGSSR NVSSEQKDEN REAKPRSLRF
     TWSMKTTSSM DPSDMMREIR KVLDANNCDY EQRERFLLFC VHGDGHAENL VQWEMEVCKL
     PRLSLNGVRF KRISGTSIAF KNIASKIANE LKL
//
ID   CDK7_MOUSE              Reviewed;         346 AA.
AC   Q03147; Q99KK3;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   08-MAR-2011, entry version 110.
DE   RecName: Full=Cyclin-dependent kinase 7;
DE            EC=2.7.11.22;
DE            EC=2.7.11.23;
DE   AltName: Full=39 kDa protein kinase;
DE   AltName: Full=CDK-activating kinase;
DE            Short=CAK;
DE   AltName: Full=CR4 protein kinase;
DE   AltName: Full=CRK4;
DE   AltName: Full=Cell division protein kinase 7;
DE   AltName: Full=P39 Mo15;
DE   AltName: Full=Protein-tyrosine kinase MPK-7;
DE   AltName: Full=TFIIH basal transcription factor complex kinase subunit;
GN   Name=Cdk7; Synonyms=Cdkn7, Crk4, Mo15, Mpk-7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Macrophage;
RX   MEDLINE=95021255; PubMed=7935441;
RA   Matsuoka M., Kato J.-Y., Fisher R.P., Morgan D.O., Sherr C.J.;
RT   "Activation of cyclin-dependent kinase 4 (cdk4) by mouse MO15-
RT   associated kinase.";
RL   Mol. Cell. Biol. 14:7265-7275(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CBA; TISSUE=Bone marrow;
RX   MEDLINE=95047496; PubMed=7959010; DOI=10.1016/0378-1119(94)90169-4;
RA   Stepanova L.Y., Ershler M., Belyavsky A.V.;
RT   "Sequence of the cDNA encoding murine CRK4 protein kinase.";
RL   Gene 149:321-324(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 139-154.
RC   STRAIN=C57BL/6; TISSUE=Embryonic brain;
RX   MEDLINE=93096484; PubMed=1281307;
RA   Gilardi-Hebenstreit P., Nieto M.A., Frain M., Mattei M.-G.,
RA   Chestier A., Wilkinson D.G., Charnay P.;
RT   "An Eph-related receptor protein tyrosine kinase gene segmentally
RT   expressed in the developing mouse hindbrain.";
RL   Oncogene 7:2499-2506(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 141-176.
RC   STRAIN=CBA; TISSUE=Bone marrow;
RX   MEDLINE=93185941; PubMed=8444355; DOI=10.1016/0378-1119(93)90411-U;
RA   Ershler M.A., Nagorskaya T.V., Visser J.W.M., Belyavsky A.V.;
RT   "Novel CDC2-related protein kinases produced in murine hematopoietic
RT   stem cells.";
RL   Gene 124:305-306(1993).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 141-176.
RC   STRAIN=CBA; TISSUE=Bone marrow;
RX   MEDLINE=93092802; PubMed=1459009;
RA   Ershler M.A., Nagorskaya T.V., Visser J.W.M., Belyavsky A.V.;
RT   "Identification of new protein kinase genes, similar to kinases of the
RT   cdc2 family and expressed in murine hematopoietic stem cells.";
RL   Dokl. Akad. Nauk SSSR 324:893-897(1992).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-170, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Cyclin-dependent kinases (CDKs) are activated by the
CC       binding to a cyclin and mediate the progression through the cell
CC       cycle. Each different complex controls a specific transition
CC       between two subsequent phases in the cell cycle. CDK7 is the
CC       catalytic subunit of the CDK-activating kinase (CAK) complex, a
CC       serine-threonine kinase. CAK activates the cyclin-associated
CC       kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation.
CC       CAK complexed to the core-TFIIH basal transcription factor
CC       activates RNA polymerase II by serine phosphorylation of the
CC       repetitive C-terminus domain (CTD) of its large subunit (POLR2A),
CC       allowing its escape from the promoter and elongation of the
CC       transcripts. Involved in cell cycle control and in RNA
CC       transcription by RNA polymerase II. Its expression and activity
CC       are constant throughout the cell cycle.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- CATALYTIC ACTIVITY: ATP + [DNA-directed RNA polymerase] = ADP +
CC       [DNA-directed RNA polymerase] phosphate.
CC   -!- ENZYME REGULATION: Phosphorylation at Thr-170 is required for
CC       enzymatic activity (By similarity).
CC   -!- SUBUNIT: Associates primarily with cyclin H and MAT1 to form the
CC       CAK complex. CAK can further associate with the core-TFIIH to form
CC       the TFIIH basal transcription factor. Interacts with PUF60 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. CDC2/CDKX subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; U11822; AAA64831.1; -; mRNA.
DR   EMBL; X74145; CAA52242.1; -; mRNA.
DR   EMBL; BC004605; AAH04605.1; -; mRNA.
DR   EMBL; BC068160; AAH68160.1; -; mRNA.
DR   EMBL; X57239; CAA40515.1; -; mRNA.
DR   EMBL; X65070; CAA46203.1; -; mRNA.
DR   IPI; IPI00129222; -.
DR   PIR; A56231; A56231.
DR   PIR; S30503; S30503.
DR   PIR; S34652; S34652.
DR   RefSeq; NP_034004.2; NM_009874.3.
DR   UniGene; Mm.259718; -.
DR   ProteinModelPortal; Q03147; -.
DR   SMR; Q03147; 13-311.
DR   STRING; Q03147; -.
DR   PhosphoSite; Q03147; -.
DR   PRIDE; Q03147; -.
DR   Ensembl; ENSMUST00000091299; ENSMUSP00000088845; ENSMUSG00000069089.
DR   GeneID; 12572; -.
DR   KEGG; mmu:12572; -.
DR   CTD; 12572; -.
DR   MGI; MGI:102956; Cdk7.
DR   eggNOG; roNOG12329; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG014652; -.
DR   InParanoid; Q03147; -.
DR   OMA; FMDTDLE; -.
DR   OrthoDB; EOG4KSPK0; -.
DR   PhylomeDB; Q03147; -.
DR   BRENDA; 2.7.11.22; 244.
DR   BRENDA; 2.7.11.23; 244.
DR   NextBio; 281682; -.
DR   ArrayExpress; Q03147; -.
DR   Bgee; Q03147; -.
DR   Genevestigator; Q03147; -.
DR   GermOnline; ENSMUSG00000069089; Mus musculus.
DR   GO; GO:0005675; C:holo TFIIH complex; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004693; F:cyclin-dependent protein kinase activity; IEA:EC.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; ISS:UniProtKB.
DR   GO; GO:0008353; F:RNA polymerase II carboxy-terminal domain kinase activity; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell division; Kinase; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Serine/threonine-protein kinase;
KW   Transcription; Transcription regulation; Transferase.
FT   CHAIN         1    346       Cyclin-dependent kinase 7.
FT                                /FTId=PRO_0000085792.
FT   DOMAIN       12    295       Protein kinase.
FT   NP_BIND      18     26       ATP (By similarity).
FT   ACT_SITE    137    137       Proton acceptor (By similarity).
FT   BINDING      41     41       ATP (By similarity).
FT   MOD_RES       7      7       Phosphoserine (By similarity).
FT   MOD_RES     164    164       Phosphoserine (By similarity).
FT   MOD_RES     169    169       Phosphotyrosine (By similarity).
FT   MOD_RES     170    170       Phosphothreonine.
FT   CONFLICT     11     12       RY -> HN (in Ref. 2; CAA52242).
FT   CONFLICT     20     20       E -> R (in Ref. 2; CAA52242).
FT   CONFLICT    100    136       Missing (in Ref. 3; AAH04605).
FT   CONFLICT    100    100       V -> L (in Ref. 2; CAA52242).
FT   CONFLICT    104    104       D -> H (in Ref. 2; CAA52242).
FT   CONFLICT    130    131       QH -> HN (in Ref. 2; CAA52242).
SQ   SEQUENCE   346 AA;  38968 MW;  455FFAB2CFEDEB3E CRC64;
     MAVDVKSRAK RYEKLDFLGE GQFATVYKAR DKNTNQIVAI KKIKLGHRSE AKDGINRTAL
     REIKLLQELS HPNIIGLLDA FGHKSNISLV FDFMETDLEV IIKDNSLVLT PSHIKAYMLM
     TLQGLEYLHQ HWILHRDLKP NNLLLDENGV LKLADFGLAK SFGSPNRAYT HQVVTRWYRA
     PELLFGARMY GVGVDMWAVG CILAELLLRV PFLPGDSDLD QLTRIFETLG TPTEEQWPDM
     CSLPDYVTFK SFPGVPLQHI FIAAGDDLLE LIQGLFLFNP CTRTTASQAL KTKYFSNRPG
     PTPGCQLPRP NCPVEALKEP ANPTVATKRK RAEALEQGIL PKKLIF
//
ID   ENAH_MOUSE              Reviewed;         802 AA.
AC   Q03173; P70430; P70431; P70432; P70433; Q5D053;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 2.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Protein enabled homolog;
DE   AltName: Full=NPC-derived proline-rich protein 1;
DE            Short=NDPP-1;
GN   Name=Enah; Synonyms=Mena, Ndpp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=93041923; PubMed=1420303; DOI=10.1016/0167-4781(92)90156-T;
RA   Sazuka T., Tomooka Y., Kathju S., Ikawa Y., Noda M., Kumar S.;
RT   "Identification of a developmentally regulated gene in the mouse
RT   central nervous system which encodes a novel proline rich protein.";
RL   Biochim. Biophys. Acta 1132:240-248(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), FUNCTION, TISSUE
RP   SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH PFN1.
RC   TISSUE=Brain;
RX   MEDLINE=97015079; PubMed=8861907; DOI=10.1016/S0092-8674(00)81341-0;
RA   Gertler F.B., Niebuhr K., Reinhard M., Wehland J., Soriano P.;
RT   "Mena, a relative of VASP and Drosophila Enabled, is implicated in the
RT   control of microfilament dynamics.";
RL   Cell 87:227-239(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH APBB1; NEDD4 AND YAP1.
RX   MEDLINE=98070482; PubMed=9407065; DOI=10.1074/jbc.272.52.32869;
RA   Ermekova K.S., Zambrano N., Linn H., Minopoli G., Gertler F.,
RA   Russo T., Sudol M.;
RT   "The WW domain of neural protein FE65 interacts with proline-rich
RT   motifs in Mena, the mammalian homolog of Drosophila enabled.";
RL   J. Biol. Chem. 272:32869-32877(1997).
RN   [5]
RP   FUNCTION, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   MEDLINE=99166867; PubMed=10069337; DOI=10.1016/S0896-6273(00)81092-2;
RA   Lanier L.M., Gates M.A., Witke W., Menzies A.S., Wehman A.M.,
RA   Macklis J.D., Kwiatkowski D., Soriano P., Gertler F.B.;
RT   "Mena is required for neurulation and commissure formation.";
RL   Neuron 22:313-325(1999).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-255 AND
RP   SER-637.
RX   PubMed=12134088; DOI=10.1091/mbc.E01-10-0102;
RA   Loureiro J.J., Rubinson D.A., Bear J.E., Baltus G.A.,
RA   Kwiatkowski A.V., Gertler F.B.;
RT   "Critical roles of phosphorylation and actin binding motifs, but not
RT   the central proline-rich region, for Ena/vasodilator-stimulated
RT   phosphoprotein (VASP) function during cell migration.";
RL   Mol. Biol. Cell 13:2533-2546(2002).
RN   [7]
RP   INTERACTION WITH ROBO4.
RC   STRAIN=FVB/N;
RX   PubMed=12941633; DOI=10.1016/S0012-1606(03)00258-6;
RA   Park K.W., Morrison C.M., Sorensen L.K., Jones C.A., Rao Y.,
RA   Chien C.-B., Wu J.Y., Urness L.D., Li D.Y.;
RT   "Robo4 is a vascular-specific receptor that inhibits endothelial
RT   migration.";
RL   Dev. Biol. 261:251-267(2003).
RN   [8]
RP   ALTERNATIVE SPLICING (ISOFORM 6), PHOSPHORYLATION AT TYR-557, AND
RP   INTERACTION WITH ABI1.
RX   PubMed=12672821; DOI=10.1074/jbc.M301447200;
RA   Tani K., Sato S., Sukezane T., Kojima H., Hirose H., Hanafusa H.,
RA   Shishido T.;
RT   "Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian
RT   enabled (Mena) by c-Abl kinase.";
RL   J. Biol. Chem. 278:21685-21692(2003).
RN   [9]
RP   INTERACTION WITH DNMBP.
RX   PubMed=14506234; DOI=10.1074/jbc.M308104200;
RA   Salazar M.A., Kwiatkowski A.V., Pellegrini L., Cestra G., Butler M.H.,
RA   Rossman K.L., Serna D.M., Sondek J., Gertler F.B., De Camilli P.;
RT   "Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology
RT   domains, links dynamin to regulation of the actin cytoskeleton.";
RL   J. Biol. Chem. 278:49031-49043(2003).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [11]
RP   FUNCTION, AND PHOSPHORYLATION AT SER-255.
RX   PubMed=15066263; DOI=10.1016/S0896-6273(04)00108-4;
RA   Lebrand C., Dent E.W., Strasser G.A., Lanier L.M., Krause M.,
RA   Svitkina T.M., Borisy G.G., Gertler F.B.;
RT   "Critical role of Ena/VASP proteins for filopodia formation in neurons
RT   and in function downstream of netrin-1.";
RL   Neuron 42:37-49(2004).
RN   [12]
RP   INTERACTION WITH APBB1IP.
RX   PubMed=15642358; DOI=10.1016/j.febslet.2004.10.110;
RA   Jenzora A., Behrendt B., Small J.V., Wehland J., Stradal T.E.;
RT   "PREL1 provides a link from Ras signalling to the actin cytoskeleton
RT   via Ena/VASP proteins.";
RL   FEBS Lett. 579:455-463(2005).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-112 IN COMPLEX WITH
RP   PRO-RICH PEPTIDE OF L.MONOCYTOGENES ACTA.
RX   MEDLINE=99268533; PubMed=10338211; DOI=10.1016/S0092-8674(00)80757-6;
RA   Prehoda K.E., Lee D.J., Lim W.A.;
RT   "Structure of the enabled/VASP homology 1 domain-peptide complex: a
RT   key component in the spatial control of actin assembly.";
RL   Cell 97:471-480(1999).
CC   -!- FUNCTION: Ena/VASP proteins are actin-associated proteins involved
CC       in a range of processes dependent on cytoskeleton remodeling and
CC       cell polarity such as axon guidance and lamellipodial and
CC       filopodial dynamics in migrating cells. ENAH induces the formation
CC       of F-actin rich outgrowths in fibroblasts. Acts synergistically
CC       with BAIAP2-alpha and downstream of NTN1 to promote filipodia
CC       formation. Required for actin-based mobility of Listeria
CC       monocytogenes.
CC   -!- SUBUNIT: Homotetramer (By similarity). Interacts with APBB1IP,
CC       APBB1, PFN1 and ROBO4. Isoforms, containing the polyproline-rich
CC       regions with PPLP motifs, bind the WW domain of APBB1IP. Isoforms,
CC       containing the PPSY motif, bind, in vitro, to the WW2 and WW3
CC       domains of NEDD4 and to the WW1 domain of YAP1. Binds the SH3
CC       domain of BAIAP2-alpha but only after the autoinhibitory region of
CC       BAIAP2-alpha has been blocked by interaction with CDC42.
CC       Interacts, via the EVH1/WH1 domain, with the Pro-rich domains from
CC       VCL, ZYX and Listeria monocytogenes actA and with the TES LIM
CC       domain. The TES LIM domain and the Pro-rich domains from VCL or
CC       ZYX compete for the same binding site. Interaction with ZYX is
CC       important for targeting ENAH to focal adhesions and enhances
CC       production of actin-rich structures at the apical surface of
CC       cells. Interacts, through the Pro-rich region, with the C-terminal
CC       SH3 domain of DNMPB. Binds GPHN (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton (By
CC       similarity). Cell projection, lamellipodium (By similarity). Cell
CC       projection, filopodium (By similarity). Cell junction, synapse (By
CC       similarity). Cell junction, focal adhesion (By similarity).
CC       Note=Targeted to the leading edge of lamellipodia and filopodia by
CC       MRL family members. Colocalizes at filopodial tips with a number
CC       of other proteins including vinculin and zyxlin. Colocalizes with
CC       N-WASP at the leading edge. Colocalizes with GPHN and PFN at
CC       synapses (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=5; Synonyms=Neural variant Mena+++, 140 kDa isoform;
CC         IsoId=Q03173-1; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q03173-2; Sequence=VSP_007255;
CC         Note=No experimental evidence available. Ref.1 (BAA01570)
CC         sequence differs from that shown due to several frameshifts;
CC       Name=2; Synonyms=Mena, 80 kDa isoform;
CC         IsoId=Q03173-3; Sequence=VSP_007259, VSP_007260;
CC       Name=3; Synonyms=Neural variant Mena+;
CC         IsoId=Q03173-4; Sequence=VSP_007259;
CC         Note=Phosphorylated during neural development;
CC       Name=4; Synonyms=Neural variant Mena++;
CC         IsoId=Q03173-5; Sequence=VSP_007257, VSP_007258;
CC       Name=6; Synonyms=Mena(S);
CC         IsoId=Q03173-6; Sequence=VSP_007259, VSP_007260, VSP_010565;
CC   -!- TISSUE SPECIFICITY: Expressed in heart and testis, lower levels in
CC       lung, skeletal muscle, kidney, pancreas and brain. Isoform 5 is
CC       expressed exclusively in the brain. Isoform 2 is expressed
CC       predominantly in brain, testis, ovary and fat. In the brain, both
CC       of these isoforms are more highly expressed in the hippocampus,
CC       cortex and midbrain, lowest levels in the striatum and cerebellum.
CC       Isoform 6 is expressed in brain and spleen.
CC   -!- DEVELOPMENTAL STAGE: In embryonic brains, isoform 2, isoform 3 and
CC       isoform 5 are expressed from E11. Expression of isoform 3
CC       decreases steadily and becomes almost undetectable by E16, while
CC       expression of isoform 5 begins to increase from E13 and peaks
CC       between E16 and E18. During brain development, isoform 2 is
CC       particularly expressed in the neuroepithelium, forebrain and
CC       somites at E8.5. By E10.5, expression is detected in the brain,
CC       dorsal root ganglia, branchial and pharyngeal arches, somites and
CC       limb buds. Isoform 5 is detected at this stage in regions of the
CC       developing CNS.
CC   -!- DOMAIN: The EVH2 domain is comprised of 3 regions. Block A is a
CC       thymosin-like domain required for G-actin binding. The KLKR motif
CC       within this block is essential for the G-actin binding and for
CC       actin polymerization. Block B is required for F-actin binding and
CC       subcellular location, and Block C for tetramerization.
CC   -!- PTM: NTN1-induced PKA phosphorylation on Ser-255 directly
CC       parallels the formation of filopodial protrusions.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the Ena/VASP family.
CC   -!- SIMILARITY: Contains 1 WH1 domain.
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DR   EMBL; D10727; BAA01570.1; ALT_FRAME; mRNA.
DR   EMBL; U72520; AAC52863.1; -; mRNA.
DR   EMBL; U72521; AAC52864.1; -; mRNA.
DR   EMBL; U72522; AAC52865.1; -; mRNA.
DR   EMBL; U72523; AAC52866.1; -; mRNA.
DR   EMBL; BC062927; AAH62927.1; -; mRNA.
DR   IPI; IPI00284242; -.
DR   IPI; IPI00284246; -.
DR   IPI; IPI00417165; -.
DR   IPI; IPI00468225; -.
DR   IPI; IPI00470077; -.
DR   IPI; IPI00621842; -.
DR   PIR; S27200; S27200.
DR   RefSeq; NP_001076589.1; NM_001083120.1.
DR   RefSeq; NP_001076590.1; NM_001083121.1.
DR   RefSeq; NP_032706.2; NM_008680.2.
DR   RefSeq; NP_034265.2; NM_010135.2.
DR   UniGene; Mm.389224; -.
DR   UniGene; Mm.87759; -.
DR   PDB; 1EVH; X-ray; 1.80 A; A=1-112.
DR   PDBsum; 1EVH; -.
DR   ProteinModelPortal; Q03173; -.
DR   SMR; Q03173; 1-113, 760-800.
DR   MINT; MINT-1215621; -.
DR   STRING; Q03173; -.
DR   PhosphoSite; Q03173; -.
DR   PRIDE; Q03173; -.
DR   Ensembl; ENSMUST00000078719; ENSMUSP00000077781; ENSMUSG00000022995.
DR   Ensembl; ENSMUST00000111024; ENSMUSP00000106653; ENSMUSG00000022995.
DR   Ensembl; ENSMUST00000111025; ENSMUSP00000106654; ENSMUSG00000022995.
DR   Ensembl; ENSMUST00000111030; ENSMUSP00000106659; ENSMUSG00000022995.
DR   GeneID; 13800; -.
DR   KEGG; mmu:13800; -.
DR   UCSC; uc007dxp.1; mouse.
DR   UCSC; uc007dxq.1; mouse.
DR   UCSC; uc007dxr.1; mouse.
DR   UCSC; uc007dxs.1; mouse.
DR   CTD; 13800; -.
DR   MGI; MGI:108360; Enah.
DR   eggNOG; roNOG07783; -.
DR   GeneTree; ENSGT00440000039080; -.
DR   HOGENOM; HBG282727; -.
DR   HOVERGEN; HBG006655; -.
DR   InParanoid; Q03173; -.
DR   OrthoDB; EOG437RF0; -.
DR   NextBio; 284558; -.
DR   ArrayExpress; Q03173; -.
DR   Bgee; Q03173; -.
DR   CleanEx; MM_ENAH; -.
DR   Genevestigator; Q03173; -.
DR   GermOnline; ENSMUSG00000022995; Mus musculus.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0030175; C:filopodium; IDA:MGI.
DR   GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0001725; C:stress fiber; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005522; F:profilin binding; IDA:UniProtKB.
DR   GO; GO:0017124; F:SH3 domain binding; IDA:MGI.
DR   GO; GO:0008154; P:actin polymerization or depolymerization; IDA:MGI.
DR   GO; GO:0007411; P:axon guidance; IMP:MGI.
DR   GO; GO:0006928; P:cellular component movement; IDA:UniProtKB.
DR   GO; GO:0046907; P:intracellular transport; IEA:InterPro.
DR   GO; GO:0001843; P:neural tube closure; IGI:MGI.
DR   InterPro; IPR000697; EVH1.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR000156; RanBP.
DR   InterPro; IPR014885; VASP_tetra.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF08776; VASP_tetra; 1.
DR   Pfam; PF00568; WH1; 1.
DR   SMART; SM00160; RanBD; 1.
DR   SMART; SM00461; WH1; 1.
DR   PROSITE; PS50229; WH1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Alternative splicing; Cell junction;
KW   Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Developmental protein; Differentiation; Neurogenesis; Phosphoprotein;
KW   Repeat; SH3-binding; Synapse.
FT   CHAIN         1    802       Protein enabled homolog.
FT                                /FTId=PRO_0000086972.
FT   DOMAIN        1    111       WH1.
FT   REPEAT      175    179       1.
FT   REPEAT      180    184       2.
FT   REPEAT      185    189       3.
FT   REPEAT      190    194       4.
FT   REPEAT      195    199       5.
FT   REPEAT      200    204       6.
FT   REPEAT      205    209       7.
FT   REGION      175    209       7 X 5 AA tandem repeats of [LM]-E-[QR]-
FT                                [EQ]-[QR].
FT   REGION      623    799       EVH2.
FT   REGION      623    643       EVH2 block A.
FT   REGION      674    691       EVH2 block B.
FT   REGION      765    799       EVH2 block C.
FT   COILED      154    258       Potential.
FT   COILED      767    797       Potential.
FT   MOTIF       632    635       KLKR.
FT   COMPBIAS    269    605       Pro-rich.
FT   MOD_RES     144    144       Phosphoserine.
FT   MOD_RES     255    255       Phosphoserine; by PKA.
FT   MOD_RES     557    557       Phosphotyrosine.
FT   MOD_RES     637    637       Phosphoserine (By similarity).
FT   MOD_RES     721    721       Phosphothreonine (By similarity).
FT   MOD_RES     734    734       Phosphothreonine (By similarity).
FT   MOD_RES     738    738       Phosphoserine (By similarity).
FT   MOD_RES     740    740       Phosphoserine (By similarity).
FT   VAR_SEQ       1    412       Missing (in isoform 1).
FT                                /FTId=VSP_007255.
FT   VAR_SEQ     117    135       Missing (in isoform 2, isoform 3 and
FT                                isoform 6).
FT                                /FTId=VSP_007259.
FT   VAR_SEQ     117    131       Missing (in isoform 4).
FT                                /FTId=VSP_007257.
FT   VAR_SEQ     132    135       CIFC -> VFYL (in isoform 4).
FT                                /FTId=VSP_007258.
FT   VAR_SEQ     259    500       Missing (in isoform 2 and isoform 6).
FT                                /FTId=VSP_007260.
FT   VAR_SEQ     561    594       Missing (in isoform 6).
FT                                /FTId=VSP_010565.
FT   MUTAGEN     255    255       S->A: No change in subcellular location
FT                                nor colocalization with vinculin at focal
FT                                adhesions nor with N-WASP at the leading
FT                                edge. Loss of cell mobility function;
FT                                when associated with A-637.
FT   MUTAGEN     255    255       S->D: No change in subcellular location
FT                                nor colocalization with vinculin at focal
FT                                adhesions nor with N-WASP at the leading
FT                                edge. No loss of cell mobility function;
FT                                when associated with D-637.
FT   MUTAGEN     637    637       S->A: No change in subcellular location
FT                                nor colocalization with vinculin at focal
FT                                adhesions nor with N-WASP at the leading
FT                                edge. No loss of cell mobility function.
FT                                when associated with A-255.
FT   MUTAGEN     637    637       S->D: No change in subcellular location
FT                                nor colocalization with vinculin at focal
FT                                adhesions nor with N-WASP at the leading
FT                                edge. No loss of cell mobility function.
FT                                when associated with D-255.
FT   CONFLICT    500    500       G -> A (in Ref. 1; BAA01570).
FT   STRAND        3     17
FT   TURN         18     21
FT   STRAND       22     25
FT   HELIX        26     28
FT   STRAND       33     40
FT   TURN         41     44
FT   STRAND       45     52
FT   TURN         53     55
FT   STRAND       58     64
FT   STRAND       74     81
FT   STRAND       86     93
FT   HELIX        94    111
SQ   SEQUENCE   802 AA;  85844 MW;  592BB975EE20F77F CRC64;
     MSEQSICQAR AAVMVYDDAN KKWVPAGGST GFSRVHIYHH TGNNTFRVVG RKIQDHQVVI
     NCAIPKGLKY NQATQTFHQW RDARQVYGLN FGSKEDANVF ASAMMHALEV LNSQEAAQSK
     VTATQDSTNL RCIFCGPTLP RQNSQLPAQV QNGPSQEELE IQRRQLQEQQ RQKELERERM
     ERERLERERL ERERLERERL EQEQLERQRQ EREHVERLER ERLERLERER QERERERLEQ
     LEREQVEWER ERRMSNAAPS SDSSLSSAPL PEYSSCQPPS APPPSYAKVI SAPVSDATPD
     YAVVTALPPT STPPTPPLRH AATRFATSLG SAFHPVLPHY ATVPRPLNKN SRPSSPVNTP
     SSQPPAAKSC AWPTSNFSPL PPSPPIMISS PPGKATGPRP VLPVCVSSPV PQMPPSPTAP
     NGSLDSVTYP VSPPPTSGPA APPPPPPPPP PPPPPPLPPP PLPPLASLSH CGSQASPPPG
     TPLASTPSSK PSVLPSPSAG APASAETPLN PELGDSSASE PGLQAASQPA ESPTPQGLVL
     GPPAPPPPPP LPSGPAYASA LPPPPGPPPP PPLPSTGPPP PPPPPPPLPN QAPPPPPPPP
     APPLPASGIF SGSTSEDNRP LTGLAAAIAG AKLRKVSRVE DGSFPGGGNT GSVSLASSKA
     DAGRGNGPLP LGGSGLMEEM SALLARRRRI AEKGSTIETE QKEDRNEDAE PITAKAPSTS
     TPEPTRKPWE RTNTMNGSKS PVISRPKSTP SSQPSANGVQ TEGLDYDRLK QDILDEMRKE
     LAKLKEELID AIRQELSKSN TA
//
ID   ATPA_MOUSE              Reviewed;         553 AA.
AC   Q03265; Q3TFN0; Q3THN8; Q3TPR0; Q3TPV3; Q3TZU3; Q3UIR7; Q543Y6;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   08-MAR-2011, entry version 122.
DE   RecName: Full=ATP synthase subunit alpha, mitochondrial;
DE   Flags: Precursor;
GN   Name=Atp5a1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=93191686; PubMed=7916601; DOI=10.1006/bbrc.1993.1195;
RA   Yotov W.V., St Arnaud R.;
RT   "Cloning and functional expression analysis of the alpha subunit of
RT   mouse ATP synthase.";
RL   Biochem. Biophys. Res. Commun. 191:142-148(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, C57BL/6J, and NOD;
RC   TISSUE=Heart, Hippocampus, Liver, Spinal cord, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 24-42; 46-83; 89-123; 133-161; 176-182; 195-204;
RP   208-214; 219-230; 241-252; 254-261; 263-270; 306-316; 323-329;
RP   335-347; 403-416; 435-463; 467-503; 507-527 AND 540-553.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B.,
RA   Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15648052; DOI=10.1002/pmic.200401066;
RA   Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA   Hart G.W., Burlingame A.L.;
RT   "Quantitative analysis of both protein expression and serine /
RT   threonine post-translational modifications through stable isotope
RT   labeling with dithiothreitol.";
RL   Proteomics 5:388-398(2005).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-132; LYS-230; LYS-239;
RP   LYS-261; LYS-305; LYS-427; LYS-498; LYS-531 AND LYS-539, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
CC       synthase or Complex V) produces ATP from ADP in the presence of a
CC       proton gradient across the membrane which is generated by electron
CC       transport complexes of the respiratory chain. F-type ATPases
CC       consist of two structural domains, F(1) - containing the
CC       extramembraneous catalytic core, and F(0) - containing the
CC       membrane proton channel, linked together by a central stalk and a
CC       peripheral stalk. During catalysis, ATP synthesis in the catalytic
CC       domain of F(1) is coupled via a rotary mechanism of the central
CC       stalk subunits to proton translocation. Subunits alpha and beta
CC       form the catalytic core in F(1). Rotation of the central stalk
CC       against the surrounding alpha(3)beta(3) subunits leads to
CC       hydrolysis of ATP in three separate catalytic sites on the beta
CC       subunits. Subunit alpha does not bear the catalytic high-affinity
CC       ATP-binding sites (By similarity).
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel. CF(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC       has three main subunits: a, b and c. Interacts with ATPAF2.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
CC       Note=Peripheral membrane protein.
CC   -!- PTM: Acetylation of Lys-132, Lys-230 and Lys-498 is observed in
CC       liver mitochondria from fasted mice but not from fed mice.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
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DR   EMBL; L01062; AAA37271.1; -; mRNA.
DR   EMBL; AK043976; BAC31722.1; -; mRNA.
DR   EMBL; AK076572; BAC36399.1; -; mRNA.
DR   EMBL; AK146797; BAE27439.1; -; mRNA.
DR   EMBL; AK150426; BAE29549.1; -; mRNA.
DR   EMBL; AK150843; BAE29901.1; -; mRNA.
DR   EMBL; AK151004; BAE30027.1; -; mRNA.
DR   EMBL; AK151128; BAE30136.1; -; mRNA.
DR   EMBL; AK151224; BAE30216.1; -; mRNA.
DR   EMBL; AK151920; BAE30798.1; -; mRNA.
DR   EMBL; AK152054; BAE30910.1; -; mRNA.
DR   EMBL; AK152890; BAE31573.1; -; mRNA.
DR   EMBL; AK157529; BAE34114.1; -; mRNA.
DR   EMBL; AK159540; BAE35167.1; -; mRNA.
DR   EMBL; AK159491; BAE35125.1; -; mRNA.
DR   EMBL; AK159758; BAE35349.1; -; mRNA.
DR   EMBL; AK160043; BAE35585.1; -; mRNA.
DR   EMBL; AK164110; BAE37632.1; -; mRNA.
DR   EMBL; AK164193; BAE37675.1; -; mRNA.
DR   EMBL; AK166709; BAE38962.1; -; mRNA.
DR   EMBL; AK166812; BAE39039.1; -; mRNA.
DR   EMBL; AK167159; BAE39300.1; -; mRNA.
DR   EMBL; AK167863; BAE39881.1; -; mRNA.
DR   EMBL; AK168198; BAE40158.1; -; mRNA.
DR   EMBL; AK168617; BAE40482.1; -; mRNA.
DR   EMBL; AK168879; BAE40697.1; -; mRNA.
DR   EMBL; AK168890; BAE40707.1; -; mRNA.
DR   EMBL; AK168932; BAE40744.1; -; mRNA.
DR   EMBL; AK169080; BAE40864.1; -; mRNA.
DR   EMBL; AK169084; BAE40868.1; -; mRNA.
DR   EMBL; AK169105; BAE40887.1; -; mRNA.
DR   EMBL; AK169142; BAE40921.1; -; mRNA.
DR   EMBL; AK169300; BAE41056.1; -; mRNA.
DR   EMBL; AK169308; BAE41063.1; -; mRNA.
DR   EMBL; AK169414; BAE41160.1; -; mRNA.
DR   EMBL; BC014854; AAH14854.1; -; mRNA.
DR   IPI; IPI00130280; -.
DR   PIR; JC1473; JC1473.
DR   RefSeq; NP_031531.1; NM_007505.2.
DR   UniGene; Mm.276137; -.
DR   ProteinModelPortal; Q03265; -.
DR   SMR; Q03265; 56-552.
DR   STRING; Q03265; -.
DR   PhosphoSite; Q03265; -.
DR   SWISS-2DPAGE; Q03265; -.
DR   REPRODUCTION-2DPAGE; IPI00130280; -.
DR   REPRODUCTION-2DPAGE; Q03265; -.
DR   UCD-2DPAGE; Q03265; -.
DR   PRIDE; Q03265; -.
DR   Ensembl; ENSMUST00000026495; ENSMUSP00000026495; ENSMUSG00000025428.
DR   GeneID; 11946; -.
DR   KEGG; mmu:11946; -.
DR   UCSC; uc008fru.1; mouse.
DR   CTD; 11946; -.
DR   MGI; MGI:88115; Atp5a1.
DR   eggNOG; roNOG06697; -.
DR   GeneTree; ENSGT00550000074846; -.
DR   HOVERGEN; HBG001536; -.
DR   InParanoid; Q03265; -.
DR   OMA; TKQTLNR; -.
DR   OrthoDB; EOG4ZCT48; -.
DR   PhylomeDB; Q03265; -.
DR   NextBio; 280057; -.
DR   ArrayExpress; Q03265; -.
DR   Bgee; Q03265; -.
DR   Genevestigator; Q03265; -.
DR   GermOnline; ENSMUSG00000025428; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IMP:MGI.
DR   GO; GO:0046933; F:hydrogen ion transporting ATP synthase activity, rotational mechanism; IMP:MGI.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   GO; GO:0009790; P:embryo development; IMP:MGI.
DR   GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR000194; ATPase_a/bsu_nucl-bd.
DR   InterPro; IPR005294; ATPase_F1-cplx_asu.
DR   InterPro; IPR018118; ATPase_F1/A1-cplx_a/bsu_N.
DR   InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C.
DR   InterPro; IPR004100; ATPase_F1/V1/A1-cplx_a/bsu_N.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF00306; ATP-synt_ab_C; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   SUPFAM; SSF47917; ATPase_a/b_C; 1.
DR   SUPFAM; SSF50615; ATPase_a/b_N; 1.
DR   TIGRFAMs; TIGR00962; atpA; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP synthesis; ATP-binding; CF(1);
KW   Direct protein sequencing; Hydrogen ion transport; Ion transport;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Nucleotide-binding; Phosphoprotein; Pyrrolidone carboxylic acid;
KW   Transit peptide; Transport.
FT   TRANSIT       1     43       Mitochondrion (By similarity).
FT   CHAIN        44    553       ATP synthase subunit alpha,
FT                                mitochondrial.
FT                                /FTId=PRO_0000002425.
FT   NP_BIND     212    219       ATP (By similarity).
FT   SITE        413    413       Required for activity (By similarity).
FT   MOD_RES      44     44       Pyrrolidone carboxylic acid (By
FT                                similarity).
FT   MOD_RES      76     76       Phosphoserine.
FT   MOD_RES     132    132       N6-acetyllysine.
FT   MOD_RES     161    161       N6-acetyllysine (By similarity).
FT   MOD_RES     230    230       N6-acetyllysine.
FT   MOD_RES     239    239       N6-acetyllysine.
FT   MOD_RES     261    261       N6-acetyllysine.
FT   MOD_RES     305    305       N6-acetyllysine.
FT   MOD_RES     427    427       N6-acetyllysine.
FT   MOD_RES     434    434       N6-acetyllysine (By similarity).
FT   MOD_RES     498    498       N6-acetyllysine.
FT   MOD_RES     506    506       N6-acetyllysine (By similarity).
FT   MOD_RES     531    531       N6-acetyllysine.
FT   MOD_RES     539    539       N6-acetyllysine.
FT   CONFLICT      3      3       S -> T (in Ref. 2; BAE37632).
FT   CONFLICT     63     63       D -> Y (in Ref. 2; BAE34114).
FT   CONFLICT    119    119       F -> L (in Ref. 2; BAE34114).
FT   CONFLICT    126    126       K -> N (in Ref. 2; BAE34114).
FT   CONFLICT    315    315       S -> Y (in Ref. 2; BAE34114).
FT   CONFLICT    321    321       Y -> C (in Ref. 2; BAE40868).
FT   CONFLICT    422    456       Missing (in Ref. 2; BAE27439).
FT   CONFLICT    486    486       A -> T (in Ref. 2; BAE40158).
SQ   SEQUENCE   553 AA;  59753 MW;  CF35B4FBA7ED431D CRC64;
     MLSVRVAAAV ARALPRRAGL VSKNALGSSF VGARNLHASN TRLQKTGTAE MSSILEERIL
     GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS GLKGMSLNLE PDNVGVVVFG
     NDKLIKEGDV VKRTGAIVDV PVGEELLGRV VDALGNAIDG KGPIGSKTRR RVGLKAPGII
     PRISVREPMQ TGIKAVDSLV PIGRGQRELI IGDRQTGKTS IAIDTIINQK RFNDGTDEKK
     KLYCIYVAIG QKRSTVAQLV KRLTDADAMK YTIVVSATAS DAAPLQYLAP YSGCSMGEYF
     RDNGKHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE RAAKMNDSFG
     GGSLTALPVI ETQAGDVSAY IPTNVISITD GQIFLETELF YKGIRPAINV GLSVSRVGSA
     AQTRAMKQVA GTMKLELAQY REVAAFAQFG SDLDAATQQL LSRGVRLTEL LKQGQYSPMA
     IEEQVAVIYA GVRGYLDKLE PSKITKFENA FLSHVISQHQ SLLGNIRSDG KISEQSDAKL
     KEIVTNFLAG FEP
//
ID   RUNX1_MOUSE             Reviewed;         451 AA.
AC   Q03347; O08598; Q62049; Q9ESB9; Q9ET65;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-FEB-2011, entry version 116.
DE   RecName: Full=Runt-related transcription factor 1;
DE   AltName: Full=Acute myeloid leukemia 1 protein;
DE   AltName: Full=Core-binding factor subunit alpha-2;
DE            Short=CBF-alpha-2;
DE   AltName: Full=Oncogene AML-1;
DE   AltName: Full=Polyomavirus enhancer-binding protein 2 alpha B subunit;
DE            Short=PEA2-alpha B;
DE            Short=PEBP2-alpha B;
DE   AltName: Full=SL3-3 enhancer factor 1 alpha B subunit;
DE   AltName: Full=SL3/AKV core-binding factor alpha B subunit;
GN   Name=Runx1; Synonyms=Aml1, Cbfa2, Pebp2ab;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Fibroblast;
RX   MEDLINE=93173528; PubMed=8437866;
RA   Bae S.-C., Yamaguchi-Iwai Y., Ogawa E., Maruyama M., Inuzuka M.,
RA   Kagoshima H., Shigesada K., Satake M., Ito Y.;
RT   "Isolation of PEBP2 alpha B cDNA representing the mouse homolog of
RT   human acute myeloid leukemia gene, AML1.";
RL   Oncogene 8:809-814(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Fibroblast;
RX   MEDLINE=94217721; PubMed=8164679;
RA   Bae S.-C., Ogawa E., Maruyama M., Oka H., Satake M., Shigesada K.,
RA   Jenkins N.A., Gilbert D.J., Copeland N.G., Ito Y.;
RT   "PEBP2 alpha B/mouse AML1 consists of multiple isoforms that possess
RT   differential transactivation potentials.";
RL   Mol. Cell. Biol. 14:3242-3252(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   STRAIN=BALB/c; TISSUE=Thymus;
RA   Calabi F.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RX   MEDLINE=20365846; PubMed=10903914; DOI=10.1006/bbrc.2000.3112;
RA   Tsuji K., Noda M.;
RT   "Identification and expression of a novel 3'-exon of mouse
RT   Runx1/Pebp2alphaB/Cbfa2/AML1 gene.";
RL   Biochem. Biophys. Res. Commun. 274:171-176(2000).
RN   [5]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC   STRAIN=129/Ola; TISSUE=Embryo;
RX   MEDLINE=21139761; PubMed=11243869; DOI=10.1006/bbrc.2001.4513;
RA   Fujita Y., Nishimura M., Taniwaki M., Abe T., Okuda T.;
RT   "Identification of an alternatively spliced form of the mouse
RT   AML1/RUNX1 gene transcript AML1c and its expression in early
RT   hematopoietic development.";
RL   Biochem. Biophys. Res. Commun. 281:1248-1255(2001).
RN   [6]
RP   PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING
RP   (ISOFORM 4).
RC   STRAIN=C57BL/6; TISSUE=Thymus;
RX   MEDLINE=21077029; PubMed=11203699; DOI=10.1006/dbio.2000.9991;
RA   Telfer J.C., Rothenberg E.V.;
RT   "Expression and function of a stem cell promoter for the murine
RT   CBFalpha2 gene: distinct roles and regulation in natural killer and T
RT   cell development.";
RL   Dev. Biol. 229:363-382(2001).
RN   [7]
RP   FUNCTION IN LIVER HEMATOPOIESIS.
RX   MEDLINE=96152661; PubMed=8565077; DOI=10.1016/S0092-8674(00)80986-1;
RA   Okuda T., van Deursen J., Hiebert S.W., Grosveld G., Downing J.R.;
RT   "AML1, the target of multiple chromosomal translocations in human
RT   leukemia, is essential for normal fetal liver hematopoiesis.";
RL   Cell 84:321-330(1996).
RN   [8]
RP   FUNCTION IN NECROSIS AND HEMORRHAGING.
RX   MEDLINE=96194989; PubMed=8622955; DOI=10.1073/pnas.93.8.3444;
RA   Wang Q., Stacy T., Binder M., Marin-Padilla M., Sharpe A.H.,
RA   Speck N.A.;
RT   "Disruption of the Cbfa2 gene causes necrosis and hemorrhaging in the
RT   central nervous system and blocks definitive hematopoiesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:3444-3449(1996).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 62-177 IN COMPLEX WITH
RP   CEBPB; CBFB AND DNA.
RX   MEDLINE=21268781; PubMed=11375505; DOI=10.1107/S0907444901003900;
RA   Tahirov T.H., Inoue-Bungo T., Sasaki M., Shiina M., Kimura K.,
RA   Sato K., Kumasaka T., Yamamoto M., Kamiya N., Ogata K.;
RT   "Crystallization and preliminary X-ray analyses of quaternary, ternary
RT   and binary protein-DNA complexes with involvement of AML1/Runx-
RT   1/CBFalpha Runt domain, CBFbeta and the C/EBPbeta bZip region.";
RL   Acta Crystallogr. D 57:850-853(2001).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 60-182 IN COMPLEX WITH
RP   CEBPB; CBFB AND DNA, AND MUTAGENESIS OF ARG-80; ASN-109; TYR-113;
RP   ARG-142; LYS-144; THR-149; VAL-170; ASP-171; ARG-174 AND ARG-177.
RX   MEDLINE=21157290; PubMed=11257229; DOI=10.1016/S0092-8674(01)00271-9;
RA   Tahirov T.H., Inoue-Bungo T., Morii H., Fujikawa A., Sasaki M.,
RA   Kimura K., Shiina M., Sato K., Kumasaka T., Yamamoto M., Ishii S.,
RA   Ogata K.;
RT   "Structural analyses of DNA recognition by the AML1/Runx-1 Runt domain
RT   and its allosteric control by CBFbeta.";
RL   Cell 104:755-767(2001).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 60-173.
RX   MEDLINE=22206943; PubMed=12217689; DOI=10.1016/S0022-2836(02)00702-7;
RA   Baeckstroem S., Wolf-Watz M., Grundstroem C., Haerd T.,
RA   Grundstroem T., Sauer U.H.;
RT   "The RUNX1 Runt domain at 1.25A resolution: a structural switch and
RT   specifically bound chloride ions modulate DNA binding.";
RL   J. Mol. Biol. 322:259-272(2002).
CC   -!- FUNCTION: CBF binds to the core site, 5'-PYGPYGGT-3', of a number
CC       of enhancers and promoters, including murine leukemia virus,
CC       polyomavirus enhancer, T-cell receptor enhancers, LCK, IL-3 and
CC       GM-CSF promoters. Essential for the development of normal
CC       hematopoiesis. Isoform 4 shows higher binding activities for
CC       target genes and binds TCR-beta-E2 and RAG-1 target site with
CC       threefold higher affinity than other isoforms. It is less
CC       effective in the context of neutrophil terminal differentiation.
CC       Acts synergistically with ELF4 to transactivate the IL-3 promoter
CC       and with ELF2 to transactivate the BLK promoter. Inhibits MYST4-
CC       dependent transcriptional activation (By similarity).
CC   -!- SUBUNIT: Heterodimer with CBFB. RUNX1 binds DNA as a monomer and
CC       through the Runt domain. DNA-binding is increased by
CC       heterodimerization. Interacts with TLE1 and THOC4. Interacts with
CC       ELF1, ELF2 and SPI1. Interacts via its Runt domain with the ELF4
CC       N-terminal region. Interaction with ELF2 isoform 2 (NERF-1a) may
CC       act to repress RUNX1-mediated transactivation. Interacts with
CC       MYST3 and MYST4. Interacts with SUV39H1, leading to abrogation of
CC       transactivating and DNA-binding properties of RUNX1 (By
CC       similarity). Interacts with YAP1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1; Synonyms=AML1-B, PEB2-alpha B1;
CC         IsoId=Q03347-1; Sequence=Displayed;
CC       Name=2; Synonyms=PEB2-alpha B2;
CC         IsoId=Q03347-2; Sequence=VSP_005932, VSP_005933;
CC       Name=3;
CC         IsoId=Q03347-3; Sequence=VSP_005931, VSP_005934;
CC       Name=4; Synonyms=AML1-C;
CC         IsoId=Q03347-4; Sequence=VSP_005930;
CC       Name=5;
CC         IsoId=Q03347-5; Sequence=VSP_005935, VSP_005936;
CC   -!- TISSUE SPECIFICITY: Isoform 4 is expressed at high levels in
CC       thymus, spleen and T-cell lines and at lower levels in myeloid
CC       cell lines and nonhematopoietic cells. Isoform 5 is expressed
CC       ubiquitously in lumbar vertebrae, brain, kidney, heart, muscle,
CC       ovary and osteoblast-like cell line MC3T3E1.
CC   -!- DEVELOPMENTAL STAGE: Differentially expressed during hematopoietic
CC       differentiation. Isoform AML1-B is readily detectable in
CC       undifferentiated embryonic stem (es) cells and peak expression is
CC       seen on day 6 of differentiation, followed by a gradual decline
CC       thereafter. Isoform AML1-C is undetectable in undifferentiated es
CC       cells, but is gradually up-regulated along with differentiation
CC       and reaches its highest levels on day 8 and this expression is
CC       maintained through day 12. Isoform 5 is expressed at high levels
CC       at 6-8 dpc and then levels decrease on 12 dpc. Isoform 4
CC       expression is high throughout T-cell development, declines with
CC       natural killer cell maturation, and appears to be transiently
CC       reduced and then restored during B-cell development.
CC   -!- DOMAIN: A proline/serine/threonine rich region at the C-terminus
CC       is necessary for transcriptional activation of target genes.
CC   -!- PTM: Phosphorylated in its C-terminus upon IL-6 treatment.
CC       Phosphorylation enhances interaction with MYST3 (By similarity).
CC   -!- PTM: Methylated (By similarity).
CC   -!- DISEASE: Note=Mice with an Runx1 lacking the DNA-binding region
CC       are found to die between embryonic days 11.5 to 12.5 due to
CC       hemorrhaging in the central nervous system. This hemorrhaging is
CC       preceded by necrosis and hematopoiesis is blocked.
CC   -!- SIMILARITY: Contains 1 Runt domain.
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DR   EMBL; D26532; BAA05535.1; -; mRNA.
DR   EMBL; D13802; BAA02960.1; -; mRNA.
DR   EMBL; X97306; CAA65976.1; -; mRNA.
DR   EMBL; AB046930; BAB08105.1; -; mRNA.
DR   EMBL; AF345649; AAK29784.1; -; mRNA.
DR   EMBL; AF193030; AAG32957.1; -; Genomic_DNA.
DR   IPI; IPI00131214; -.
DR   IPI; IPI00230038; -.
DR   IPI; IPI00230039; -.
DR   IPI; IPI00230040; -.
DR   IPI; IPI00230041; -.
DR   PIR; A56017; A56017.
DR   RefSeq; NP_033951.2; NM_009821.2.
DR   UniGene; Mm.4081; -.
DR   UniGene; Mm.470227; -.
DR   PDB; 1EAN; X-ray; 1.70 A; A=46-185.
DR   PDB; 1EAO; X-ray; 1.40 A; A/B=46-185.
DR   PDB; 1EAQ; X-ray; 1.25 A; A/B=46-185.
DR   PDB; 1HJB; X-ray; 3.00 A; C/F=60-182.
DR   PDB; 1HJC; X-ray; 2.65 A; A/D=60-182.
DR   PDB; 1IO4; X-ray; 3.00 A; C=60-182.
DR   PDB; 2J6W; X-ray; 2.60 A; A/B=46-185.
DR   PDBsum; 1EAN; -.
DR   PDBsum; 1EAO; -.
DR   PDBsum; 1EAQ; -.
DR   PDBsum; 1HJB; -.
DR   PDBsum; 1HJC; -.
DR   PDBsum; 1IO4; -.
DR   PDBsum; 2J6W; -.
DR   ProteinModelPortal; Q03347; -.
DR   SMR; Q03347; 60-173, 319-345.
DR   MINT; MINT-91306; -.
DR   STRING; Q03347; -.
DR   PhosphoSite; Q03347; -.
DR   PRIDE; Q03347; -.
DR   Ensembl; ENSMUST00000023673; ENSMUSP00000023673; ENSMUSG00000022952.
DR   Ensembl; ENSMUST00000113956; ENSMUSP00000109589; ENSMUSG00000022952.
DR   GeneID; 12394; -.
DR   KEGG; mmu:12394; -.
DR   UCSC; uc007zzi.1; mouse.
DR   UCSC; uc007zzk.1; mouse.
DR   CTD; 12394; -.
DR   MGI; MGI:99852; Runx1.
DR   eggNOG; roNOG07435; -.
DR   HOVERGEN; HBG060268; -.
DR   InParanoid; Q03347; -.
DR   NextBio; 281140; -.
DR   ArrayExpress; Q03347; -.
DR   Bgee; Q03347; -.
DR   CleanEx; MM_RUNX1; -.
DR   Genevestigator; Q03347; -.
DR   GermOnline; ENSMUSG00000022952; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0070491; F:repressing transcription factor binding; IPI:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0016563; F:transcription activator activity; ISS:UniProtKB.
DR   GO; GO:0048266; P:behavioral response to pain; IMP:MGI.
DR   GO; GO:0007417; P:central nervous system development; IMP:MGI.
DR   GO; GO:0060216; P:definitive hemopoiesis; IMP:MGI.
DR   GO; GO:0035162; P:embryonic hemopoiesis; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0001889; P:liver development; IMP:MGI.
DR   GO; GO:0048666; P:neuron development; IMP:MGI.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
DR   GO; GO:0030854; P:positive regulation of granulocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR   GO; GO:0032526; P:response to retinoic acid; IDA:BHF-UCL.
DR   GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR   InterPro; IPR013524; AML1/Runt_N.
DR   InterPro; IPR000040; AML1_Runt.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd.
DR   InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd.
DR   InterPro; IPR013711; RunxI.
DR   InterPro; IPR016554; TF_Runt-rel_RUNX.
DR   Gene3D; G3DSA:2.60.40.720; p53_RUNT_DNA_bd; 1.
DR   PANTHER; PTHR11950; AML1_Runt; 1.
DR   Pfam; PF00853; Runt; 1.
DR   Pfam; PF08504; RunxI; 1.
DR   PIRSF; PIRSF009374; TF_Runt-rel_RUNX; 1.
DR   PRINTS; PR00967; ONCOGENEAML1.
DR   SUPFAM; SSF49417; P53_like_DNA_bnd; 1.
DR   PROSITE; PS51062; RUNT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; DNA-binding;
KW   Methylation; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    451       Runt-related transcription factor 1.
FT                                /FTId=PRO_0000174656.
FT   DOMAIN       50    178       Runt.
FT   REGION       80     84       Interaction with DNA (By similarity).
FT   REGION      135    143       Interaction with DNA (By similarity).
FT   REGION      168    177       Interaction with DNA (By similarity).
FT   REGION      291    370       Interaction with MYST3 (By similarity).
FT   REGION      307    399       Interaction with MYST4 (By similarity).
FT   COMPBIAS    187    451       Pro/Ser/Thr-rich.
FT   BINDING     112    112       Chloride 1 (By similarity).
FT   BINDING     116    116       Chloride 1; via amide nitrogen (By
FT                                similarity).
FT   BINDING     139    139       Chloride 2 (By similarity).
FT   BINDING     170    170       Chloride 2; via amide nitrogen (By
FT                                similarity).
FT   MOD_RES      14     14       Phosphothreonine (By similarity).
FT   MOD_RES      21     21       Phosphoserine (By similarity).
FT   MOD_RES      24     24       N6-acetyllysine (By similarity).
FT   MOD_RES      43     43       N6-acetyllysine (By similarity).
FT   MOD_RES     249    249       Phosphoserine (By similarity).
FT   MOD_RES     266    266       Phosphoserine (By similarity).
FT   MOD_RES     268    268       Phosphoserine (By similarity).
FT   MOD_RES     276    276       Phosphoserine (By similarity).
FT   VAR_SEQ       1      5       MRIPV -> MASDSIFESFPSYPQCFMR (in isoform
FT                                4).
FT                                /FTId=VSP_005930.
FT   VAR_SEQ      92    182       VALGDVPDGTLVTVMAGNDENYSAELRNATAAMKNQVARFN
FT                                DLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGP
FT                                REPRRHRQK -> LLPEEGGGRSRWRSADGQSEPRGQRLRR
FT                                LLKGAACSRSLWSFSLSLGWGGDAALPWRPSGGSASEVSKR
FT                                EFF (in isoform 3).
FT                                /FTId=VSP_005931.
FT   VAR_SEQ     178    178       R -> N (in isoform 2).
FT                                /FTId=VSP_005932.
FT   VAR_SEQ     179    242       Missing (in isoform 2).
FT                                /FTId=VSP_005933.
FT   VAR_SEQ     183    451       Missing (in isoform 3).
FT                                /FTId=VSP_005934.
FT   VAR_SEQ     242    303       DARQIQPSPPWSYDQSYQYLGSITSSSVHPATPISPGRASG
FT                                MTSLSAELSSRLSTAPDLTAF -> KNPTEPTTLCLCWSPR
FT                                RRKHRGCQAFLGALRELLKPRSISWEPNEENAVPSAEYLYS
FT                                EKCGC (in isoform 5).
FT                                /FTId=VSP_005935.
FT   VAR_SEQ     304    451       Missing (in isoform 5).
FT                                /FTId=VSP_005936.
FT   MUTAGEN      80     80       R->A: Interferes with DNA-binding.
FT   MUTAGEN     109    109       N->A: Interferes with heterodimerization.
FT   MUTAGEN     113    113       Y->A: Interferes with heterodimerization.
FT   MUTAGEN     142    142       R->A: Interferes with DNA-binding.
FT   MUTAGEN     144    144       K->M: Interferes with DNA-binding.
FT   MUTAGEN     149    149       T->A: Interferes with heterodimerization.
FT   MUTAGEN     170    170       V->A: No effect.
FT   MUTAGEN     171    171       D->A: Interferes with DNA-binding.
FT   MUTAGEN     174    174       R->A: Interferes with DNA-binding.
FT   MUTAGEN     177    177       R->A: Interferes with DNA-binding.
FT   CONFLICT     37     38       GP -> A (in Ref. 3; CAA65976).
FT   HELIX        51     57
FT   TURN         59     61
FT   STRAND       70     72
FT   STRAND       77     80
FT   STRAND       90     95
FT   STRAND      102    109
FT   STRAND      112    115
FT   STRAND      117    119
FT   STRAND      121    125
FT   STRAND      128    130
FT   STRAND      146    152
FT   STRAND      154    156
FT   STRAND      158    161
FT   STRAND      166    171
SQ   SEQUENCE   451 AA;  48610 MW;  06B9E9BA01A6469C CRC64;
     MRIPVDASTS RRFTPPSTAL SPGKMSEALP LGAPDGGPAL ASKLRSGDRS MVEVLADHPG
     ELVRTDSPNF LCSVLPTHWR CNKTLPIAFK VVALGDVPDG TLVTVMAGND ENYSAELRNA
     TAAMKNQVAR FNDLRFVGRS GRGKSFTLTI TVFTNPPQVA TYHRAIKITV DGPREPRRHR
     QKLDDQTKPG SLSFSERLSE LEQLRRTAMR VSPHHPAPTP NPRASLNHST AFNPQPQSQM
     QDARQIQPSP PWSYDQSYQY LGSITSSSVH PATPISPGRA SGMTSLSAEL SSRLSTAPDL
     TAFGDPRQFP TLPSISDPRM HYPGAFTYSP PVTSGIGIGM SAMSSASRYH TYLPPPYPGS
     SQAQAGPFQT GSPSYHLYYG ASAGSYQFSM VGGERSPPRI LPPCTNASTG AALLNPSLPS
     QSDVVETEGS HSNSPTNMPP ARLEEAVWRP Y
//
ID   NMDE4_MOUSE             Reviewed;        1323 AA.
AC   Q03391;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   08-MAR-2011, entry version 102.
DE   RecName: Full=Glutamate [NMDA] receptor subunit epsilon-4;
DE   AltName: Full=N-methyl D-aspartate receptor subtype 2D;
DE            Short=NMDAR2D;
DE            Short=NR2D;
DE   Flags: Precursor;
GN   Name=Grin2d;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=93050214; PubMed=1385220; DOI=10.1016/0014-5793(92)81178-O;
RA   Ikeda K., Nagasawa M., Mori H., Araki K., Sakimura K., Watanabe M.,
RA   Inoue Y., Mishina M.;
RT   "Cloning and expression of the epsilon 4 subunit of the NMDA receptor
RT   channel.";
RL   FEBS Lett. 313:34-38(1992).
RN   [2]
RP   SEQUENCE REVISION.
RA   Ikeda K., Nagasawa M., Mori H., Araki K., Sakimura K., Watanabe M.,
RA   Inoue Y., Mishina M.;
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1313, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
CC   -!- FUNCTION: NMDA receptor subtype of glutamate-gated ion channels
CC       possesses high calcium permeability and voltage-dependent
CC       sensitivity to magnesium. Mediated by glycine.
CC   -!- SUBUNIT: Interacts with PDZ domains of INADL and DLG4 (By
CC       similarity). Forms heteromeric channel of a zeta subunit (GRIN1),
CC       a epsilon subunit (GRIN2A, GRIN2B, GRIN2C or GRIN2D) and a third
CC       subunit (GRIN3A or GRIN3B).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Cell junction, synapse, postsynaptic cell membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel
CC       (TC 1.A.10.1) family. NR2D/GRIN2D subfamily.
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DR   EMBL; D12822; BAA02254.1; -; mRNA.
DR   IPI; IPI00131279; -.
DR   PIR; S27224; S27224.
DR   UniGene; Mm.322594; -.
DR   ProteinModelPortal; Q03391; -.
DR   SMR; Q03391; 45-416, 427-826.
DR   STRING; Q03391; -.
DR   PhosphoSite; Q03391; -.
DR   PRIDE; Q03391; -.
DR   Ensembl; ENSMUST00000002848; ENSMUSP00000002848; ENSMUSG00000002771.
DR   UCSC; uc009gxm.1; mouse.
DR   MGI; MGI:95823; Grin2d.
DR   eggNOG; roNOG06546; -.
DR   GeneTree; ENSGT00540000070221; -.
DR   HOGENOM; HBG443877; -.
DR   HOVERGEN; HBG052637; -.
DR   InParanoid; Q03391; -.
DR   OrthoDB; EOG42RD6M; -.
DR   ArrayExpress; Q03391; -.
DR   Bgee; Q03391; -.
DR   Genevestigator; Q03391; -.
DR   GermOnline; ENSMUSG00000002771; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
DR   GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0004972; F:N-methyl-D-aspartate selective glutamate receptor activity; IDA:MGI.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR   GO; GO:0051930; P:regulation of sensory perception of pain; IMP:MGI.
DR   GO; GO:0001964; P:startle response; IMP:MGI.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR019594; Glu_rcpt_Glu/Gly-bd.
DR   InterPro; IPR001320; Iontro_glu_rcpt.
DR   InterPro; IPR001508; NMDA_rcpt.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR   PRINTS; PR00177; NMDARECEPTOR.
DR   SMART; SM00918; Lig_chan-Glu_bd; 1.
DR   SMART; SM00079; PBPe; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell junction; Cell membrane; Glycoprotein; Ion transport;
KW   Ionic channel; Ligand-gated ion channel; Magnesium; Membrane;
KW   Phosphoprotein; Postsynaptic cell membrane; Receptor; Signal; Synapse;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL        1     27       Potential.
FT   CHAIN        28   1323       Glutamate [NMDA] receptor subunit
FT                                epsilon-4.
FT                                /FTId=PRO_0000011584.
FT   TOPO_DOM     28    580       Extracellular (Potential).
FT   TRANSMEM    581    601       Helical; (Potential).
FT   TOPO_DOM    602    653       Cytoplasmic (Potential).
FT   TRANSMEM    654    674       Helical; (Potential).
FT   TOPO_DOM    675    841       Extracellular (Potential).
FT   TRANSMEM    842    862       Helical; (Potential).
FT   TOPO_DOM    863   1323       Cytoplasmic (Potential).
FT   MOTIF      1321   1323       PDZ-binding (By similarity).
FT   COMPBIAS    278    283       Poly-Gly.
FT   COMPBIAS    905    913       Poly-Pro.
FT   COMPBIAS   1030   1035       Poly-Ala.
FT   COMPBIAS   1197   1201       Poly-Pro.
FT   SITE        639    639       Functional determinant of NMDA receptors
FT                                (By similarity).
FT   MOD_RES    1313   1313       Phosphoserine.
FT   CARBOHYD     89     89       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    349    349       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    363    363       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    464    464       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    566    566       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   1323 AA;  142908 MW;  8AE9878F90DD0921 CRC64;
     MRGAGGPRGP RGPAKMLLLL ALACASPFPE EVPGPGAAGG GTGGARPLNV ALVFSGPAYA
     AEAARLGPAV AAAVRSPGLD VRPVALVLNG SDPRSLVLQL CDLLSGLRVH GVVFEDDSRA
     PAVAPILDFL SAQTSLPIVA VHGGAALVLT PKEKGSTFLQ LGSSTEQQLQ VIFEVLEEYD
     WTSFVAVTTR APGHRAFLSY IEVLTDGSLV GWEHRGALTL DPGAGEAVLG AQLRSVSAQI
     RLLFCAREEA EPVFRAAEEA GLTGPGYVWF MVGPQLAGGG GSGVPGEPLL LPGGAPLPAG
     LFAVRSAGWR DDLARRVAAG VAVVARGAQA LLRDYGFLPE LGHDCRAQNR THRGESLHRY
     FMNITWDNRD YSFNEDGFLV NPSLVVISLT RDRTWEVVGS WEQQTLRLKY PLWSRYGRFL
     QPVDDTQHLT VATLEERPFV IVEPADPISG TCIRDSVPCR SQLNRTHSPP PDAPRPEKRC
     CKGFCIDILK RLAHTIGFSY DLYLVTNGKH GKKIDGVWNG MIGEVFYQRA DMAIGSLTIN
     EERSEIVDFS VPFVETGISV MVARSNGTVS PSAFLEPYSP AVWVMMFVMC LTVVAVTVFI
     FEYLSPVGYN RSLATGKRPG GSTFTIGKSI WLLWALVFNN SVPVENPRGT TSKIMVLVWA
     FFAVIFLASY TANLAAFMIQ EEYVDTVSGL SDRKFQRPQE QYPPLKFGTV PNGSTEKNIR
     SNYPDMHSYM VRYNQPRVEE ALTQLKAGKL DAFIYDAAVL NYMARKDEGC KLVTIGSGKV
     FATTGYGIAL HKGSRWKRPI DLALLQFLGD DEIEMLERLW LSGICHNDKI EVMSSKLDID
     NMAGVFYMLL VAMGLSLLVF AWEHLVYWRL RHCLGPTHRM DFLLAFSRGM YSCCSAEAAP
     PPAKPPPPPQ PLPSPAYPAA RPPPGPAPFV PRERAAADRW RRAKGTGPPG GAALADGFHR
     YYGPIEPQGL GLGEARAAPR GAAGRPLSPP TTQPPQKPPP SYFAIVREQE PAEPPAGAFP
     GFPSPPAPPA AAAAAVGPPL CRLAFEDESP PAPSRWPRSD PESQPLLGGG AGGPSAGAPT
     APPPRRTAPP PCAYLDLEPS PSDSEDSESL GGASLGGLEP WWFADFPYPY AERLGPPPGR
     YWSVDKLGGW RAGSWDYLPP RGGPAWHCRH CASLELLPPP RHLSCSHDGL DGGWWAPPPP
     PWAAGPPAPR RARCGCPRPH PHRPRASHRA PAAAPHHHRH RRAAGGWDLP PPAPTSRSLE
     DLSSCPRAAP TRRLTGPSRH ARRCPHAAHW GPPLPTASHR RHRGGDLGTR RGSAHFSSLE
     SEV
//
ID   SCG2_MOUSE              Reviewed;         617 AA.
AC   Q03517; Q80Y79; Q9CW80;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Secretogranin-2;
DE   AltName: Full=Chromogranin-C;
DE   AltName: Full=Secretogranin II;
DE            Short=SgII;
DE   Contains:
DE     RecName: Full=Secretoneurin;
DE              Short=SN;
DE   Flags: Precursor;
GN   Name=Scg2; Synonyms=Chgc, Scg-2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=93106188; PubMed=1468571; DOI=10.1016/0014-5793(92)81509-K;
RA   Schimmel A., Braeunling O., Ruether U., Huttner W.B., Gerdes H.-H.;
RT   "The organisation of the mouse secretogranin II gene.";
RL   FEBS Lett. 314:375-380(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 119-516.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 184-216.
RX   MEDLINE=98316925; PubMed=9654353; DOI=10.1016/S0304-3940(98)00345-0;
RA   Leitner B., Schneitler C., Klocker H., Volknandt W., Zimmermann H.,
RA   Winkler H., Fischer-Colbrie R.;
RT   "Formation and sequence analysis of secretoneurin, a neuropeptide
RT   derived from secretogranin II, in mammalian, bird, reptile, amphibian
RT   and fish brains.";
RL   Neurosci. Lett. 248:105-108(1998).
RN   [4]
RP   PROTEIN SEQUENCE OF 452-463, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: Secretogranin-2 is a neuroendocrine secretory granule
CC       protein, which may be the precursor for other biologically active
CC       peptides.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Neuroendocrine and endocrine
CC       secretory granules.
CC   -!- MISCELLANEOUS: Binds calcium with a low-affinity.
CC   -!- SIMILARITY: Belongs to the chromogranin/secretogranin protein
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X68837; CAA48727.1; -; Genomic_DNA.
DR   EMBL; AK002953; BAB22476.2; -; mRNA.
DR   IPI; IPI00133418; -.
DR   PIR; S27389; S27389.
DR   RefSeq; NP_033155.1; NM_009129.2.
DR   UniGene; Mm.5038; -.
DR   ProteinModelPortal; Q03517; -.
DR   STRING; Q03517; -.
DR   PhosphoSite; Q03517; -.
DR   PRIDE; Q03517; -.
DR   Ensembl; ENSMUST00000049972; ENSMUSP00000062556; ENSMUSG00000050711.
DR   GeneID; 20254; -.
DR   KEGG; mmu:20254; -.
DR   UCSC; uc007bqr.1; mouse.
DR   CTD; 20254; -.
DR   MGI; MGI:103033; Scg2.
DR   eggNOG; roNOG15384; -.
DR   GeneTree; ENSGT00390000010895; -.
DR   HOGENOM; HBG280484; -.
DR   HOVERGEN; HBG054148; -.
DR   InParanoid; Q03517; -.
DR   OMA; IAYEDVV; -.
DR   PhylomeDB; Q03517; -.
DR   NextBio; 297905; -.
DR   ArrayExpress; Q03517; -.
DR   Bgee; Q03517; -.
DR   CleanEx; MM_SCG2; -.
DR   Genevestigator; Q03517; -.
DR   GermOnline; ENSMUSG00000050711; Mus musculus.
DR   GO; GO:0005615; C:extracellular space; ISS:HGNC.
DR   GO; GO:0042056; F:chemoattractant activity; ISS:HGNC.
DR   GO; GO:0005125; F:cytokine activity; ISS:HGNC.
DR   GO; GO:0001525; P:angiogenesis; IDA:HGNC.
DR   GO; GO:0048245; P:eosinophil chemotaxis; ISS:HGNC.
DR   GO; GO:0050930; P:induction of positive chemotaxis; ISS:HGNC.
DR   GO; GO:0000165; P:MAPKKK cascade; ISS:HGNC.
DR   GO; GO:0043066; P:negative regulation of apoptosis; ISS:HGNC.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISS:HGNC.
DR   InterPro; IPR001990; Granin.
DR   Pfam; PF01271; Granin; 1.
DR   PROSITE; PS00422; GRANINS_1; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Calcium; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Phosphoprotein; Secreted; Signal;
KW   Sulfation.
FT   SIGNAL        1     30       By similarity.
FT   CHAIN        31    617       Secretogranin-2.
FT                                /FTId=PRO_0000005455.
FT   PEPTIDE     184    216       Secretoneurin.
FT                                /FTId=PRO_0000005456.
FT   MOD_RES     153    153       Sulfotyrosine (By similarity).
FT   MOD_RES     532    532       Phosphoserine (By similarity).
FT   MOD_RES     533    533       Phosphoserine (By similarity).
FT   CONFLICT    238    238       T -> A (in Ref. 2; BAB22476).
SQ   SEQUENCE   617 AA;  70644 MW;  42D0D5D5546F4BDD CRC64;
     MAGAKAYRLG AVLLLIHLIF LISGAEAASF QRNQLLQKEP DLRLENVQKF PSPEMIRALE
     YIEKLRQQAH REESSPDYNP YQGVSVPLQL KENGEESHLA ESSRDALSED EWMRIILEAL
     RQAENEPPSA PKENKPYALN LEKNFPVDTP DDYETQQWPE RKLKHMRFPL MYEENSRENP
     FKRTNEIVEE QYTPQSLATL ESVFQELGKL TGPSNQKRER VDEEQKLYTD DEDDVYKTNN
     IAYEDVVGGE DWSPIEEKIE TQTQEEVRDS KENTEKNEQI NEEMKRSGQL GLPDEENRRE
     SKDQLSEDAS KVITYLRRLV NAVGSGRSQS GPNGDRAARL LQKPLDSQSI YQLIEISRNL
     QIPPEDLIEM LKAGEKPNGL VEPEQDLELA VDLDDIPEAD LDRPDMFQSK MLSKGGYPKA
     PGRGMVEALP DGLSVEDILN VLGMENVVNQ KSPYFPNQYS QDKALMRLPY GPGKSRANQI
     PKVAWIPDVE SRQAPYENLN DQELGEYLAR MLVKYPELLN TNQLKRVPSP VSSEDDLQEE
     EQLEQAIKEH LGPGSSQEME RLAKVSKRIP VGSLKNEDTP NRQYLDEDML LKVLEYLNQE
     QAEQGREHLA KRAMENM
//
ID   KCND1_MOUSE             Reviewed;         651 AA.
AC   Q03719; Q8CC68;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Potassium voltage-gated channel subfamily D member 1;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv4.1;
DE            Short=mShal;
GN   Name=Kcnd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Brain;
RX   MEDLINE=91239573; PubMed=2034678; DOI=10.1073/pnas.88.10.4386;
RA   Pak M.D., Baker K., Covarrubias M., Butler A., Ratcliffe A.,
RA   Salkoff L.;
RT   "mShal, a subfamily of A-type K+ channel cloned from mammalian
RT   brain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:4386-4390(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 145-647.
RC   STRAIN=C57BL/6J; TISSUE=Epididymis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   INTERACTION WITH KCNIP1.
RX   MEDLINE=21316019; PubMed=11423117; DOI=10.1016/S0014-5793(01)02560-1;
RA   Nakamura T.Y., Nandi S., Pountney D.J., Artman M., Rudy B.,
RA   Coetzee W.A.;
RT   "Different effects of the Ca(2+)-binding protein, KChIP1, on two Kv4
RT   subfamily members, Kv4.1 and Kv4.2.";
RL   FEBS Lett. 499:205-209(2001).
CC   -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated rapidly
CC       inactivating A-type potassium channels. May contribute to I(To)
CC       current in the heart and I(Sa) current in neurons. Channel
CC       properties are modulated by subunit assembly.
CC   -!- SUBUNIT: Homotetramer or heterotetramer with KCND2 and/or KCND3.
CC       Associates with the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and
CC       KCNIP4. Interacts with DPP10 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position.
CC   -!- SIMILARITY: Belongs to the potassium channel family. D (Shal)
CC       (TC 1.A.1.2) subfamily. Kv4.1/KCND1 sub-subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M64226; AAA39745.1; -; mRNA.
DR   EMBL; AK033805; BAC28480.1; -; mRNA.
DR   IPI; IPI00135598; -.
DR   PIR; A39372; A39372.
DR   RefSeq; NP_032449.1; NM_008423.1.
DR   UniGene; Mm.335968; -.
DR   ProteinModelPortal; Q03719; -.
DR   SMR; Q03719; 3-418.
DR   MINT; MINT-103872; -.
DR   STRING; Q03719; -.
DR   PRIDE; Q03719; -.
DR   Ensembl; ENSMUST00000009875; ENSMUSP00000009875; ENSMUSG00000009731.
DR   GeneID; 16506; -.
DR   KEGG; mmu:16506; -.
DR   NMPDR; fig|10090.3.peg.21169; -.
DR   UCSC; uc009sms.1; mouse.
DR   CTD; 16506; -.
DR   MGI; MGI:96671; Kcnd1.
DR   GeneTree; ENSGT00580000081431; -.
DR   HOGENOM; HBG315067; -.
DR   HOVERGEN; HBG106687; -.
DR   InParanoid; Q03719; -.
DR   OMA; PCGDRFP; -.
DR   OrthoDB; EOG473PQX; -.
DR   PhylomeDB; Q03719; -.
DR   NextBio; 289835; -.
DR   ArrayExpress; Q03719; -.
DR   Bgee; Q03719; -.
DR   Genevestigator; Q03719; -.
DR   GermOnline; ENSMUSG00000009731; Mus musculus.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003975; K_chnl_volt-dep_Kv4.
DR   InterPro; IPR004054; K_chnl_volt-dep_Kv4.1.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   InterPro; IPR021645; Shal-type.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   PANTHER; PTHR11537:SF15; KV41channel; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   Pfam; PF11601; Shal-type; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01516; KV41CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01497; SHALCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Ion transport; Ionic channel; Membrane; Metal-binding;
KW   Potassium; Potassium channel; Potassium transport; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel; Zinc.
FT   CHAIN         1    651       Potassium voltage-gated channel subfamily
FT                                D member 1.
FT                                /FTId=PRO_0000054062.
FT   TOPO_DOM      1    184       Cytoplasmic (Potential).
FT   TRANSMEM    185    205       Helical; Name=Segment S1; (Potential).
FT   TRANSMEM    227    247       Helical; Name=Segment S2; (Potential).
FT   TOPO_DOM    248    261       Cytoplasmic (Potential).
FT   TRANSMEM    262    282       Helical; Name=Segment S3; (Potential).
FT   TRANSMEM    292    312       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TOPO_DOM    313    325       Cytoplasmic (Potential).
FT   TRANSMEM    326    346       Helical; Name=Segment S5; (Potential).
FT   INTRAMEM    365    385       Pore-forming; Name=Segment H5;
FT                                (Potential).
FT   TRANSMEM    387    407       Helical; Name=Segment S6; (Potential).
FT   TOPO_DOM    408    651       Cytoplasmic (Potential).
FT   REGION        2     20       Interaction with KCNIP2 (By similarity).
FT   MOTIF       372    377       Selectivity filter (By similarity).
FT   METAL       104    104       Zinc (By similarity).
FT   METAL       131    131       Zinc (By similarity).
FT   METAL       132    132       Zinc (By similarity).
FT   CARBOHYD    355    355       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   651 AA;  71698 MW;  801DECC3C56C721F CRC64;
     MAAGVATWLP FARAAAVGWL PLAQQPLPPA PEVKASRGDE VLVVNVSGRR FETWKNTLDR
     YPDTLLGSSE KEFFYDAESG EYFFDRDPDM FRHVLNFYRT GRLHCPRQEC IQAFDEELAF
     YGLVPELVGD CCLEEYRDRK KENAERLAED EEAEQAGEGP ALPAGSSLRQ RLWRAFENPH
     TSTAALVFYY VTGFFIAVSV IANVVETIPC RGTPRWPSKE QSCGDRFPTA FFCMDTACVL
     IFTGEYLLRL FAAPSRCRFL RSVMSLIDVV AILPYYIGLF VPKNDDVSGA FVTLRVFRVF
     RIFKFSRHSQ GLRILGYTLK SCASELGFLL FSLTMAIIIF ATVMFYAEKG TSKTNFTSIP
     AAFWYTIVTM TTLGYGDMVP STIAGKIFGS ICSLSGVLVI ALPVPVIVSN FSRIYHQNQR
     ADKRRAQQKV RLARIRLAKS GTTNAFLQYK QNGGLEDSGS GDGQMLCVRS RSAFEQQHHH
     LLHCLEKTTC HEFTDELTFS EALGAVSLGG RTSRSTSVSS QPMGPGSLFS SCCSRRVNRR
     AIRLANSTAS VSRGSMQELD TLAGLRRSPA PQTRSSLNAK PHDSLDLNCD SRDFVAAIIS
     IPTPPANTPD ESQPSSPSGG GGSGGTPNTT LRNSSLGTPC LLPETVKISS L
//
ID   E2AK2_MOUSE             Reviewed;         515 AA.
AC   Q03963; Q61742; Q62026;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   08-MAR-2011, entry version 111.
DE   RecName: Full=Interferon-induced, double-stranded RNA-activated protein kinase;
DE            EC=2.7.11.1;
DE   AltName: Full=Eukaryotic translation initiation factor 2-alpha kinase 2;
DE            Short=eIF-2A protein kinase 2;
DE   AltName: Full=Interferon-inducible RNA-dependent protein kinase;
DE   AltName: Full=P1/eIF-2A protein kinase;
DE   AltName: Full=Protein kinase RNA-activated;
DE            Short=PKR;
DE   AltName: Full=Serine/threonine-protein kinase TIK;
DE   AltName: Full=p68 kinase;
GN   Name=Eif2ak2; Synonyms=Pkr, Prkr, Tik;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=91340757; PubMed=1714905;
RA   Icely P.L., Gros P., Bergeron J.J.M., Devault A., Afar D.E.H.,
RA   Bell J.C.;
RT   "TIK, a novel serine/threonine kinase, is recognized by antibodies
RT   directed against phosphotyrosine.";
RL   J. Biol. Chem. 266:16073-16077(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Mammary carcinoma;
RX   MEDLINE=92302260; PubMed=1351683; DOI=10.1073/pnas.89.12.5447;
RA   Feng G.S., Chong K., Kumar A., Williams B.R.G.;
RT   "Identification of double-stranded RNA-binding domains in the
RT   interferon-induced double-stranded RNA-activated p68 kinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:5447-5451(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DBA/2J; TISSUE=Liver;
RX   MEDLINE=94336673; PubMed=7914700; DOI=10.1073/pnas.91.17.7995;
RA   Tanaka H., Samuel C.E.;
RT   "Mechanism of interferon action: structure of the mouse PKR gene
RT   encoding the interferon-inducible RNA-dependent protein kinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:7995-7999(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DBA/2J; TISSUE=Liver;
RX   MEDLINE=95180736; PubMed=7533117; DOI=10.1016/0378-1119(94)00821-9;
RA   Tanaka H., Samuel C.E.;
RT   "Sequence of the murine interferon-inducible RNA-dependent protein
RT   kinase (PKR) deduced from genomic clones.";
RL   Gene 153:283-284(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   STRUCTURE BY NMR OF 1-171.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the first and second DSRM domain in interferon-
RT   induced, double-stranded RNA-activated protein kinase.";
RL   Submitted (NOV-2005) to the PDB data bank.
CC   -!- FUNCTION: Following activation by double-stranded RNA in the
CC       presence of ATP, the kinase becomes autophosphorylated and can
CC       catalyze the phosphorylation of the translation initiation factor
CC       EIF2S1, which leads to an inhibition of the initiation of protein
CC       synthesis. Double-stranded RNA is generated during the course of a
CC       viral infection.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Activity is markedly stimulated by manganese
CC       ions. Besides dsRNA, heparin is a potent activator of the kinase
CC       (By similarity).
CC   -!- SUBUNIT: Homodimer. Interacts with DNAJC3 and STRBP (By
CC       similarity).
CC   -!- INTERACTION:
CC       P35569:Irs1; NbExp=1; IntAct=EBI-2603444, EBI-400825;
CC       P35570:Irs1 (xeno); NbExp=1; IntAct=EBI-2603444, EBI-520230;
CC   -!- TISSUE SPECIFICITY: Expressed in heart, lung, brain, kidney,
CC       testes, thymus and bone marrow.
CC   -!- INDUCTION: By interferon.
CC   -!- PTM: Autophosphorylated on several Ser and Thr.
CC       Autophosphorylation apparently leads to the activation of the
CC       kinase (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. GCN2 subfamily.
CC   -!- SIMILARITY: Contains 2 DRBM (double-stranded RNA-binding) domains.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; M65029; AAA40150.1; -; mRNA.
DR   EMBL; M93567; AAA39885.1; -; mRNA.
DR   EMBL; U09928; AAC24729.1; -; Genomic_DNA.
DR   EMBL; U09914; AAC24729.1; JOINED; Genomic_DNA.
DR   EMBL; U09915; AAC24729.1; JOINED; Genomic_DNA.
DR   EMBL; U09916; AAC24729.1; JOINED; Genomic_DNA.
DR   EMBL; U09917; AAC24729.1; JOINED; Genomic_DNA.
DR   EMBL; U09918; AAC24729.1; JOINED; Genomic_DNA.
DR   EMBL; U09919; AAC24729.1; JOINED; Genomic_DNA.
DR   EMBL; U09920; AAC24729.1; JOINED; Genomic_DNA.
DR   EMBL; U09921; AAC24729.1; JOINED; Genomic_DNA.
DR   EMBL; U09922; AAC24729.1; JOINED; Genomic_DNA.
DR   EMBL; U09923; AAC24729.1; JOINED; Genomic_DNA.
DR   EMBL; U09924; AAC24729.1; JOINED; Genomic_DNA.
DR   EMBL; U09925; AAC24729.1; JOINED; Genomic_DNA.
DR   EMBL; U09926; AAC24729.1; JOINED; Genomic_DNA.
DR   EMBL; U09927; AAC24729.1; JOINED; Genomic_DNA.
DR   EMBL; AK028602; BAC26027.1; -; mRNA.
DR   IPI; IPI00138256; -.
DR   PIR; A59309; A59309.
DR   RefSeq; NP_035293.1; NM_011163.4.
DR   UniGene; Mm.378990; -.
DR   PDB; 1X48; NMR; -; A=96-171.
DR   PDB; 1X49; NMR; -; A=1-85.
DR   PDBsum; 1X48; -.
DR   PDBsum; 1X49; -.
DR   ProteinModelPortal; Q03963; -.
DR   SMR; Q03963; 1-171, 232-504.
DR   IntAct; Q03963; 3.
DR   STRING; Q03963; -.
DR   PhosphoSite; Q03963; -.
DR   PRIDE; Q03963; -.
DR   Ensembl; ENSMUST00000024884; ENSMUSP00000024884; ENSMUSG00000024079.
DR   GeneID; 19106; -.
DR   KEGG; mmu:19106; -.
DR   NMPDR; fig|10090.3.peg.3406; -.
DR   UCSC; uc008dph.1; mouse.
DR   CTD; 19106; -.
DR   MGI; MGI:1353449; Eif2ak2.
DR   eggNOG; roNOG11212; -.
DR   HOGENOM; HBG755398; -.
DR   HOVERGEN; HBG051430; -.
DR   InParanoid; Q03963; -.
DR   OMA; KHRIDGK; -.
DR   OrthoDB; EOG4548ZD; -.
DR   PhylomeDB; Q03963; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 295666; -.
DR   ArrayExpress; Q03963; -.
DR   Bgee; Q03963; -.
DR   Genevestigator; Q03963; -.
DR   GermOnline; ENSMUSG00000024079; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IDA:MGI.
DR   GO; GO:0033689; P:negative regulation of osteoblast proliferation; ISS:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR   GO; GO:0009615; P:response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IDA:MGI.
DR   GO; GO:0006926; P:virus-infected cell apoptosis; IDA:MGI.
DR   InterPro; IPR001159; Ds-RNA-bd.
DR   InterPro; IPR014720; dsRNA-bd-like.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   Gene3D; G3DSA:3.30.160.20; dsRNA-bd-like; 2.
DR   Pfam; PF00035; dsrm; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00358; DSRM; 2.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50137; DS_RBD; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Antiviral defense; ATP-binding; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Repeat; RNA-binding;
KW   Serine/threonine-protein kinase; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    515       Interferon-induced, double-stranded RNA-
FT                                activated protein kinase.
FT                                /FTId=PRO_0000085946.
FT   DOMAIN        8     76       DRBM 1.
FT   DOMAIN       95    162       DRBM 2.
FT   DOMAIN      242    504       Protein kinase.
FT   NP_BIND     248    256       ATP (By similarity).
FT   COMPBIAS    183    187       Poly-Ser.
FT   COMPBIAS    241    247       Asp/Glu-rich (acidic).
FT   ACT_SITE    376    376       Proton acceptor (By similarity).
FT   BINDING     271    271       ATP (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     419    419       Phosphoserine (By similarity).
FT   CONFLICT     52     52       P -> G (in Ref. 1; AAA40150).
FT   CONFLICT     60     60       Q -> T (in Ref. 1; AAA40150).
FT   CONFLICT     87     87       S -> C (in Ref. 1; AAA40150).
FT   CONFLICT    144    144       T -> I (in Ref. 2; AAA39885).
FT   CONFLICT    281    282       EH -> DR (in Ref. 2; AAA39885).
FT   CONFLICT    510    510       K -> E (in Ref. 1; AAA40150).
FT   CONFLICT    512    515       RNTC -> KHMLGPF (in Ref. 1).
FT   HELIX         8     20
FT   STRAND       24     33
FT   STRAND       35     37
FT   STRAND       39     48
FT   STRAND       54     58
FT   HELIX        59     74
FT   HELIX        96    106
FT   STRAND      111    115
FT   STRAND      119    123
FT   STRAND      126    134
FT   STRAND      136    144
FT   HELIX       145    162
SQ   SEQUENCE   515 AA;  58280 MW;  7A116F7D8DB9B847 CRC64;
     MASDTPGFYM DKLNKYRQMH GVAITYKELS TSGPPHDRRF TFQVLIDEKE FPEAKGRSKQ
     EARNAAAKLA VDILDNENKV DCHTSASEQG LFVGNYIGLV NSFAQKKKLS VNYEQCEPNS
     ELPQRFICKC KIGQTMYGTG SGVTKQEAKQ LAAKEAYQKL LKSPPKTAGT SSSVVTSTFS
     GFSSSSSMTS NGVSQSAPGS FSSENVFTNG LGENKRKSGV KVSPDDVQRN KYTLDARFNS
     DFEDIEEIGL GGFGQVFKAK HRIDGKRYAI KRVKYNTEKA EHEVQALAEL NHVNIVQYHS
     CWEGVDYDPE HSMSDTSRYK TRCLFIQMEF CDKGTLEQWM RNRNQSKVDK ALILDLYEQI
     VTGVEYIHSK GLIHRDLKPG NIFLVDERHI KIGDFGLATA LENDGKSRTR RTGTLQYMSP
     EQLFLKHYGK EVDIFALGLI LAELLHTCFT ESEKIKFFES LRKGDFSNDI FDNKEKSLLK
     KLLSEKPKDR PETSEILKTL AEWRNISEKK KRNTC
//
ID   KCRB_MOUSE              Reviewed;         381 AA.
AC   Q04447; Q3KQP4; Q3TKI3; Q3U5P5; Q3UF71; Q9CXK6;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Creatine kinase B-type;
DE            EC=2.7.3.2;
DE   AltName: Full=B-CK;
DE   AltName: Full=Creatine kinase B chain;
GN   Name=Ckb; Synonyms=Ckbb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=92155725; PubMed=1740343; DOI=10.1016/0888-7543(92)90383-4;
RA   van Deursen J., Schepens J., Peters W., Meijer D., Grosveld G.,
RA   Hendriks W., Wieringa B.;
RT   "Genetic variability of the murine creatine kinase B gene locus and
RT   related pseudogenes in different inbred strains of mice.";
RL   Genomics 12:340-349(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Pentecost B.T.;
RL   Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryonic head, Kidney, Sympathetic ganglion, and
RC   Wolffian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 12-43; 87-96; 108-130; 139-148; 157-172; 178-209;
RP   224-236; 253-265; 268-292 AND 320-381, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 354-381.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=87066742; PubMed=3641191; DOI=10.1093/nar/14.21.8690;
RA   Papenbrock T., Wille W.;
RT   "The 3' non-coding region of the mouse brain B creatine kinase mRNA: a
RT   sequence with exceptional homology among species.";
RL   Nucleic Acids Res. 14:8690-8690(1986).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15648052; DOI=10.1002/pmic.200401066;
RA   Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA   Hart G.W., Burlingame A.L.;
RT   "Quantitative analysis of both protein expression and serine /
RT   threonine post-translational modifications through stable isotope
RT   labeling with dithiothreitol.";
RL   Proteomics 5:388-398(2005).
RN   [8]
RP   NITRATION [LARGE SCALE ANALYSIS] AT TYR-269, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16800626; DOI=10.1021/bi060474w;
RA   Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
RA   Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
RA   Squier T.C., Bigelow D.J.;
RT   "Endogenously nitrated proteins in mouse brain: links to
RT   neurodegenerative disease.";
RL   Biochemistry 45:8009-8022(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-39 AND TYR-125, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between
CC       ATP and various phosphogens (e.g. creatine phosphate). Creatine
CC       kinase isoenzymes play a central role in energy transduction in
CC       tissues with large, fluctuating energy demands, such as skeletal
CC       muscle, heart, brain and spermatozoa.
CC   -!- CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine.
CC   -!- SUBUNIT: Dimer of identical or non-identical chains. With MM being
CC       the major form in skeletal muscle and myocardium, MB existing in
CC       myocardium, and BB existing in many tissues, especially brain.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC   -!- SIMILARITY: Contains 1 phosphagen kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 phosphagen kinase N-terminal domain.
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DR   EMBL; M74149; AAA37462.1; -; Genomic_DNA.
DR   EMBL; L09069; AAA37455.1; -; Genomic_DNA.
DR   EMBL; AK002467; BAB22121.1; -; mRNA.
DR   EMBL; AK014299; BAB29254.1; -; mRNA.
DR   EMBL; AK148885; BAE28690.1; -; mRNA.
DR   EMBL; AK152388; BAE31176.1; -; mRNA.
DR   EMBL; AK153484; BAE32032.1; -; mRNA.
DR   EMBL; AK166980; BAE39162.1; -; mRNA.
DR   EMBL; AK161990; BAE36669.1; -; mRNA.
DR   EMBL; AK167034; BAE39205.1; -; mRNA.
DR   EMBL; BC015271; AAH15271.1; -; mRNA.
DR   EMBL; BC106109; AAI06110.2; -; mRNA.
DR   EMBL; X04591; CAA28259.1; -; mRNA.
DR   IPI; IPI00136703; -.
DR   PIR; A42078; A42078.
DR   RefSeq; NP_067248.1; NM_021273.4.
DR   UniGene; Mm.16831; -.
DR   ProteinModelPortal; Q04447; -.
DR   SMR; Q04447; 6-381.
DR   STRING; Q04447; -.
DR   PhosphoSite; Q04447; -.
DR   REPRODUCTION-2DPAGE; Q04447; -.
DR   UCD-2DPAGE; Q04447; -.
DR   PRIDE; Q04447; -.
DR   Ensembl; ENSMUST00000001304; ENSMUSP00000001304; ENSMUSG00000001270.
DR   GeneID; 12709; -.
DR   KEGG; mmu:12709; -.
DR   UCSC; uc007pdn.1; mouse.
DR   CTD; 12709; -.
DR   MGI; MGI:88407; Ckb.
DR   eggNOG; roNOG15359; -.
DR   GeneTree; ENSGT00550000074561; -.
DR   HOGENOM; HBG445448; -.
DR   HOVERGEN; HBG001339; -.
DR   InParanoid; Q04447; -.
DR   OMA; LTPEMYA; -.
DR   OrthoDB; EOG4R7V9X; -.
DR   BRENDA; 2.7.3.2; 244.
DR   NextBio; 281980; -.
DR   ArrayExpress; Q04447; -.
DR   Bgee; Q04447; -.
DR   CleanEx; MM_CKB; -.
DR   Genevestigator; Q04447; -.
DR   GermOnline; ENSMUSG00000001270; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004111; F:creatine kinase activity; IEA:EC.
DR   InterPro; IPR000749; ATP-guanido_PTrfase.
DR   InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR   InterPro; IPR022415; ATP-guanido_PTrfase_cat_AS.
DR   InterPro; IPR022413; ATP-guanido_PTrfase_N.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   Gene3D; G3DSA:1.10.135.10; ATP-gua_Ptrans; 1.
DR   Gene3D; G3DSA:3.30.590.10; ATP-gua_Ptrans; 1.
DR   PANTHER; PTHR11547; ATP-gua_Ptrans; 1.
DR   Pfam; PF00217; ATP-gua_Ptrans; 1.
DR   Pfam; PF02807; ATP-gua_PtransN; 1.
DR   SUPFAM; SSF48034; ATP-gua_Ptrans; 1.
DR   PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR   PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
DR   PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Direct protein sequencing; Kinase; Nitration;
KW   Nucleotide-binding; Phosphoprotein; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    381       Creatine kinase B-type.
FT                                /FTId=PRO_0000211967.
FT   DOMAIN       11     98       Phosphagen kinase N-terminal.
FT   DOMAIN      125    367       Phosphagen kinase C-terminal.
FT   NP_BIND     128    132       ATP (By similarity).
FT   NP_BIND     320    325       ATP (By similarity).
FT   BINDING     191    191       ATP (By similarity).
FT   BINDING     236    236       ATP (By similarity).
FT   BINDING     292    292       ATP (By similarity).
FT   BINDING     335    335       ATP (By similarity).
FT   MOD_RES       4      4       Phosphoserine (By similarity).
FT   MOD_RES      35     35       Phosphothreonine (By similarity).
FT   MOD_RES      39     39       Phosphotyrosine.
FT   MOD_RES     125    125       Phosphotyrosine.
FT   MOD_RES     164    164       Phosphoserine.
FT   MOD_RES     199    199       Phosphoserine (By similarity).
FT   MOD_RES     269    269       Nitrated tyrosine.
FT   CONFLICT    143    143       P -> H (in Ref. 3; BAE28690).
FT   CONFLICT    217    217       I -> M (in Ref. 3; BAE39162).
SQ   SEQUENCE   381 AA;  42713 MW;  D901C5653054A490 CRC64;
     MPFSNSHNTQ KLRFPAEDEF PDLSSHNNHM AKVLTPELYA ELRAKCTPSG FTLDDAIQTG
     VDNPGHPYIM TVGAVAGDEE SYDVFKDLFD PIIEERHGGY QPSDEHKTDL NPDNLQGGDD
     LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLS GRYYALKSMT
     EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWIN EEDHLRVISM
     QKGGNMKEVF TRFCTGLTQI ETLFKSKNYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP
     HLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD RLGFSEVELV QMVVDGVKLL
     IEMEQRLEQG QAIDDLMPAQ K
//
ID   NPY1R_MOUSE             Reviewed;         382 AA.
AC   Q04573; Q61993;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Neuropeptide Y receptor type 1;
DE            Short=NPY1-R;
GN   Name=Npy1r;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Liver;
RX   MEDLINE=93106169; PubMed=1468559; DOI=10.1016/0014-5793(92)81490-D;
RA   Eva C., Oberto A., Sprengel R., Genazzani E.;
RT   "The murine NPY-1 receptor gene. Structure and delineation of tissue-
RT   specific expression.";
RL   FEBS Lett. 314:285-288(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96102072; PubMed=8530415; DOI=10.1074/jbc.270.50.30102;
RA   Nakamura M., Sakanaka C., Aoki Y., Ogasawara H., Tsuji T., Kodama H.,
RA   Matsumoto T., Shimizu T., Noma M.;
RT   "Identification of two isoforms of mouse neuropeptide Y-Y1 receptor
RT   generated by alternative splicing. Isolation, genomic structure, and
RT   functional expression of the receptors.";
RL   J. Biol. Chem. 270:30102-30110(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM NPY1-R ALPHA).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Receptor for neuropeptide Y and peptide YY.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=NPY1-R alpha;
CC         IsoId=Q04573-1; Sequence=Displayed;
CC       Name=NPY1-R beta;
CC         IsoId=Q04573-2; Sequence=VSP_001912, VSP_001913;
CC   -!- TISSUE SPECIFICITY: The alpha form is highly expressed in the
CC       brain, heart, kidney, spleen, skeletal muscle, and lung, whereas
CC       the beta receptor mRNA was not detected in these tissues. However,
CC       the beta form is expressed in mouse embryonic developmental stage
CC       (7 and 11 days), bone marrow cells and several hematopoietic cell
CC       lines.
CC   -!- DEVELOPMENTAL STAGE: The beta form is expressed in embryonic
CC       developmental stage (7 and 11 days). The beta form is an embryonic
CC       and a bone marrow form of NPY1-R, which decreases in the
CC       expression during development and differentiation.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
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DR   EMBL; Z18280; CAA79157.1; -; Genomic_DNA.
DR   EMBL; Z18281; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; D63818; BAA09887.1; -; mRNA.
DR   EMBL; D63819; BAA09888.1; -; mRNA.
DR   EMBL; BC051420; AAH51420.1; -; mRNA.
DR   IPI; IPI00138130; -.
DR   IPI; IPI00227890; -.
DR   PIR; S27388; S27388.
DR   RefSeq; NP_035064.1; NM_010934.4.
DR   UniGene; Mm.478263; -.
DR   UniGene; Mm.5112; -.
DR   ProteinModelPortal; Q04573; -.
DR   SMR; Q04573; 10-367.
DR   STRING; Q04573; -.
DR   PhosphoSite; Q04573; -.
DR   PRIDE; Q04573; -.
DR   Ensembl; ENSMUST00000039303; ENSMUSP00000045530; ENSMUSG00000036437.
DR   GeneID; 18166; -.
DR   KEGG; mmu:18166; -.
DR   UCSC; uc009lvt.1; mouse.
DR   CTD; 18166; -.
DR   MGI; MGI:104963; Npy1r.
DR   eggNOG; roNOG04131; -.
DR   HOGENOM; HBG713350; -.
DR   HOVERGEN; HBG105676; -.
DR   InParanoid; Q04573; -.
DR   OMA; SKYRSSE; -.
DR   OrthoDB; EOG473PRP; -.
DR   PhylomeDB; Q04573; -.
DR   NextBio; 293450; -.
DR   ArrayExpress; Q04573; -.
DR   Bgee; Q04573; -.
DR   CleanEx; MM_NPY1R; -.
DR   Genevestigator; Q04573; -.
DR   GermOnline; ENSMUSG00000036437; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001602; F:pancreatic polypeptide receptor activity; IDA:MGI.
DR   GO; GO:0001601; F:peptide YY receptor activity; IDA:MGI.
DR   GO; GO:0007631; P:feeding behavior; IMP:MGI.
DR   GO; GO:0006006; P:glucose metabolic process; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR000351; NPY1_rcpt.
DR   InterPro; IPR000611; NPY_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01013; NRPEPTIDEY1R.
DR   PRINTS; PR01012; NRPEPTIDEYR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
KW   Palmitate; Phosphoprotein; Receptor; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    382       Neuropeptide Y receptor type 1.
FT                                /FTId=PRO_0000069921.
FT   TOPO_DOM      1     33       Extracellular (Potential).
FT   TRANSMEM     34     54       Helical; Name=1; (Potential).
FT   TOPO_DOM     55     75       Cytoplasmic (Potential).
FT   TRANSMEM     76     96       Helical; Name=2; (Potential).
FT   TOPO_DOM     97    115       Extracellular (Potential).
FT   TRANSMEM    116    136       Helical; Name=3; (Potential).
FT   TOPO_DOM    137    153       Cytoplasmic (Potential).
FT   TRANSMEM    154    174       Helical; Name=4; (Potential).
FT   TOPO_DOM    175    210       Extracellular (Potential).
FT   TRANSMEM    211    231       Helical; Name=5; (Potential).
FT   TOPO_DOM    232    259       Cytoplasmic (Potential).
FT   TRANSMEM    260    280       Helical; Name=6; (Potential).
FT   TOPO_DOM    281    298       Extracellular (Potential).
FT   TRANSMEM    299    319       Helical; Name=7; (Potential).
FT   TOPO_DOM    320    382       Cytoplasmic (Potential).
FT   MOD_RES     367    367       Phosphoserine (By similarity).
FT   LIPID       337    337       S-palmitoyl cysteine (By similarity).
FT   CARBOHYD      2      2       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     11     11       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     17     17       N-linked (GlcNAc...) (Potential).
FT   DISULFID    112    197       By similarity.
FT   VAR_SEQ     304    307       CHLT -> LNMN (in isoform NPY1-R beta).
FT                                /FTId=VSP_001912.
FT   VAR_SEQ     308    382       Missing (in isoform NPY1-R beta).
FT                                /FTId=VSP_001913.
SQ   SEQUENCE   382 AA;  44015 MW;  CDCCF93E3ABB4D70 CRC64;
     MNSTLFSKVE NHSIHYNASE NSPLLAFEND DCHLPLAVIF TLALAYGAVI ILGVSGNLAL
     IIIILKQKEM RNVTNILIVN LSFSDLLVAV MCLPFTFVYT LMDHWVFGET MCKLNPFVQC
     VSITVSIFSL VLIAVERHQL IINPRGWRPN NRHAYIGITV IWVLAVASSL PFVIYQILTD
     EPFQNVSLAA FKDKYVCFDK FPSDSHRLSY TTLLLVLQYF GPLCFIFICY FKIYIRLKRR
     NNMMDKIRDS KYRSSETKRI NIMLLSIVVA FAVCWLPLTI FNTVFDWNHQ IIATCNHNLL
     FLLCHLTAMI STCVNPIFYG FLNKNFQRDL QFFFNFCDFR SRDDDYETIA MSTMHTDVSK
     TSLKQASPVA FKKISMNDNE KV
//
ID   NF1_MOUSE               Reviewed;        2841 AA.
AC   Q04690; Q61956; Q61957;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Neurofibromin;
DE   AltName: Full=Neurofibromatosis-related protein NF-1;
GN   Name=Nf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=93357730; PubMed=8353485; DOI=10.1093/hmg/2.6.645;
RA   Bernards A., Snijders A.J., Hannigan G.E., Murthy A.E., Gusella J.F.;
RT   "Mouse neurofibromatosis type 1 cDNA sequence reveals high degree of
RT   conservation of both coding and non-coding mRNA segments.";
RL   Hum. Mol. Genet. 2:645-650(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1178-1555, AND ALTERNATIVE SPLICING.
RX   MEDLINE=95047432; PubMed=7958951; DOI=10.1016/0378-1119(94)90695-5;
RA   Mantani A., Makasugi S., Yokota Y., Abe K., Ushio Y., Yamamura K.;
RT   "A novel isoform of the neurofibromatosis type-1 mRNA and a switch of
RT   isoforms during murine cell differentiation and proliferation.";
RL   Gene 148:245-251(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 1950-2568.
RX   MEDLINE=90384569; PubMed=2169593; DOI=10.1038/347291a0;
RA   Buchberg A.M., Cleveland L.S., Jenkins N.A., Copeland N.G.;
RT   "Sequence homology shared by neurofibromatosis type-1 gene and IRA-1
RT   and IRA-2 negative regulators of the RAS cyclic AMP pathway.";
RL   Nature 347:291-294(1990).
RN   [4]
RP   PROTEIN SEQUENCE OF 1973-1979, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2516, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2545 AND SER-2819, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Stimulates the GTPase activity of Ras. NF1 shows greater
CC       affinity for Ras GAP, but lower specific activity. May be a
CC       regulator of Ras activity.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=2; Synonyms=Type II;
CC         IsoId=Q04690-1; Sequence=Displayed;
CC       Name=1; Synonyms=Type I;
CC         IsoId=Q04690-2; Sequence=VSP_001633;
CC       Name=3;
CC         IsoId=Q04690-3; Sequence=VSP_001634, VSP_001635;
CC       Name=4;
CC         IsoId=Q04690-4; Sequence=VSP_001633, VSP_001634, VSP_001635;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is expressed predominantly in brain,
CC       spinal cord and testis. Isoform 2 is expressed predominantly in
CC       adrenal gland, kidney, ovary and lung. Isoform 3 is expressed
CC       predominantly in adrenal gland and isoform 4 is expressed mainly
CC       in the testis.
CC   -!- SIMILARITY: Contains 1 CRAL-TRIO domain.
CC   -!- SIMILARITY: Contains 1 Ras-GAP domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; L10369; AAA39806.1; -; Genomic_DNA.
DR   EMBL; L10367; AAA39806.1; JOINED; Genomic_DNA.
DR   EMBL; L10368; AAA39806.1; JOINED; Genomic_DNA.
DR   EMBL; L10370; AAA68132.1; -; mRNA.
DR   EMBL; X54924; CAA38690.1; -; mRNA.
DR   EMBL; D30730; BAA06395.1; -; mRNA.
DR   EMBL; D30731; BAA06396.1; -; mRNA.
DR   IPI; IPI00108783; -.
DR   IPI; IPI00223398; -.
DR   IPI; IPI00223399; -.
DR   IPI; IPI00223400; -.
DR   PIR; I53855; I53855.
DR   PIR; I54352; I54352.
DR   PIR; I67934; I67934.
DR   PIR; I68623; I68623.
DR   RefSeq; NP_035027.1; NM_010897.2.
DR   UniGene; Mm.255596; -.
DR   UniGene; Mm.438247; -.
DR   ProteinModelPortal; Q04690; -.
DR   SMR; Q04690; 1208-1552, 1583-1839.
DR   STRING; Q04690; -.
DR   PhosphoSite; Q04690; -.
DR   PRIDE; Q04690; -.
DR   Ensembl; ENSMUST00000071325; ENSMUSP00000071289; ENSMUSG00000020716.
DR   Ensembl; ENSMUST00000097941; ENSMUSP00000095554; ENSMUSG00000020716.
DR   Ensembl; ENSMUST00000108248; ENSMUSP00000103883; ENSMUSG00000020716.
DR   Ensembl; ENSMUST00000108251; ENSMUSP00000103886; ENSMUSG00000020716.
DR   GeneID; 18015; -.
DR   KEGG; mmu:18015; -.
DR   UCSC; uc007kkl.1; mouse.
DR   CTD; 18015; -.
DR   MGI; MGI:97306; Nf1.
DR   eggNOG; roNOG06361; -.
DR   GeneTree; ENSGT00550000074797; -.
DR   HOGENOM; HBG443611; -.
DR   HOVERGEN; HBG006486; -.
DR   InParanoid; Q04690; -.
DR   OMA; FWEISSQ; -.
DR   OrthoDB; EOG4MPHP6; -.
DR   PhylomeDB; Q04690; -.
DR   NextBio; 293049; -.
DR   ArrayExpress; Q04690; -.
DR   Bgee; Q04690; -.
DR   CleanEx; MM_NF1; -.
DR   Genevestigator; Q04690; -.
DR   GermOnline; ENSMUSG00000020716; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005096; F:GTPase activator activity; IMP:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR   GO; GO:0030325; P:adrenal gland development; IMP:MGI.
DR   GO; GO:0048844; P:artery morphogenesis; IMP:MGI.
DR   GO; GO:0048593; P:camera-type eye morphogenesis; IMP:MGI.
DR   GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR   GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR   GO; GO:0021897; P:forebrain astrocyte development; IMP:MGI.
DR   GO; GO:0048853; P:forebrain morphogenesis; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0001889; P:liver development; IMP:MGI.
DR   GO; GO:0000165; P:MAPKKK cascade; IMP:MGI.
DR   GO; GO:0001656; P:metanephros development; IMP:MGI.
DR   GO; GO:0022011; P:myelination in peripheral nervous system; IMP:MGI.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IGI:MGI.
DR   GO; GO:0048712; P:negative regulation of astrocyte differentiation; IMP:MGI.
DR   GO; GO:0030336; P:negative regulation of cell migration; IGI:MGI.
DR   GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IGI:MGI.
DR   GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IMP:MGI.
DR   GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:BHF-UCL.
DR   GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:MGI.
DR   GO; GO:0043409; P:negative regulation of MAPKKK cascade; IMP:MGI.
DR   GO; GO:0007406; P:negative regulation of neuroblast proliferation; IMP:MGI.
DR   GO; GO:0046929; P:negative regulation of neurotransmitter secretion; IGI:MGI.
DR   GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; IMP:MGI.
DR   GO; GO:0045671; P:negative regulation of osteoclast differentiation; IGI:MGI.
DR   GO; GO:0035021; P:negative regulation of Rac protein signal transduction; IGI:MGI.
DR   GO; GO:0042992; P:negative regulation of transcription factor import into nucleus; IMP:MGI.
DR   GO; GO:0021915; P:neural tube development; IGI:MGI.
DR   GO; GO:0001649; P:osteoblast differentiation; IMP:MGI.
DR   GO; GO:0014065; P:phosphatidylinositol 3-kinase cascade; IMP:MGI.
DR   GO; GO:0043473; P:pigmentation; IMP:MGI.
DR   GO; GO:0045762; P:positive regulation of adenylate cyclase activity; IMP:MGI.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IGI:MGI.
DR   GO; GO:0043525; P:positive regulation of neuron apoptosis; IMP:MGI.
DR   GO; GO:0032320; P:positive regulation of Ras GTPase activity; IMP:MGI.
DR   GO; GO:0007265; P:Ras protein signal transduction; IMP:MGI.
DR   GO; GO:0045124; P:regulation of bone resorption; IMP:MGI.
DR   GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IGI:MGI.
DR   GO; GO:0032228; P:regulation of synaptic transmission, GABAergic; IGI:MGI.
DR   GO; GO:0001666; P:response to hypoxia; IMP:MGI.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI.
DR   GO; GO:0048745; P:smooth muscle tissue development; IMP:MGI.
DR   GO; GO:0021510; P:spinal cord development; IMP:MGI.
DR   GO; GO:0048485; P:sympathetic nervous system development; IMP:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   GO; GO:0042060; P:wound healing; IMP:MGI.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR001251; CRAL-bd_TRIO_C.
DR   InterPro; IPR001936; RasGAP.
DR   InterPro; IPR023152; RasGAP_CS.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   Gene3D; G3DSA:1.10.506.10; RasGAP; 1.
DR   Pfam; PF00616; RasGAP; 1.
DR   SMART; SM00323; RasGAP; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 2.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
DR   PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Direct protein sequencing;
KW   GTPase activation; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   2841       Neurofibromin.
FT                                /FTId=PRO_0000056666.
FT   DOMAIN     1237   1453       Ras-GAP.
FT   DOMAIN     1582   1740       CRAL-TRIO.
FT   COMPBIAS   1354   1357       Poly-Ser.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     866    866       Phosphoserine (By similarity).
FT   MOD_RES     878    878       Phosphoserine (By similarity).
FT   MOD_RES    1583   1583       N6-acetyllysine (By similarity).
FT   MOD_RES    2190   2190       Phosphoserine (By similarity).
FT   MOD_RES    2478   2478       Phosphotyrosine (By similarity).
FT   MOD_RES    2498   2498       Phosphoserine (By similarity).
FT   MOD_RES    2516   2516       Phosphothreonine.
FT   MOD_RES    2517   2517       Phosphoserine (By similarity).
FT   MOD_RES    2523   2523       Phosphoserine (By similarity).
FT   MOD_RES    2525   2525       Phosphoserine (By similarity).
FT   MOD_RES    2545   2545       Phosphoserine.
FT   MOD_RES    2579   2579       Phosphotyrosine (By similarity).
FT   MOD_RES    2599   2599       Phosphoserine (By similarity).
FT   MOD_RES    2819   2819       Phosphoserine.
FT   MOD_RES    2831   2831       Phosphoserine (By similarity).
FT   VAR_SEQ    1373   1393       Missing (in isoform 1 and isoform 4).
FT                                /FTId=VSP_001633.
FT   VAR_SEQ    1394   1406       VVSQRFPQNSIGA -> VPKSSCFSCLNNRWLASASLRTAS
FT                                VP (in isoform 3 and isoform 4).
FT                                /FTId=VSP_001634.
FT   VAR_SEQ    1407   2841       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_001635.
SQ   SEQUENCE   2841 AA;  319596 MW;  06650BDCDC531002 CRC64;
     MAAHRPVEWV QAVVSRFDEQ LPIKTGQQNT HTKVSTEHNK ECLINISKYK FSLVISGLTT
     ILKNVNNMRI FGEAAEKNLY LSQLIILDTL EKCLAGQPKD TMRLDETMLV KQLLPEICHF
     LHTCREGNQH AAELRNSASG VLFSLSCNNF NAVFSRISTR LQELTVCSED NVDVHDIELL
     QYINVDCAKL KRLLKETAFK FKALKKVAQL AVINSLEKAF WNWVENYPDE FTKLYQIPQT
     DMAECAEKLF DLVDGFAEST KRKAAVWPLQ IILLILCPEI IQDISKDVVD ESNINKKLFL
     DSLRKALAGH GGSRQLTESA AIACVKLCKA STYINWEDNS VIFLLVQSMV VDLKNLLFNP
     SKPFSRGSQP ADVDLMIDCL VSCFRISPHN NQHFKICLAQ NSPSTFHYVL VNSLHRIITN
     SALDWWPKID AVYCHSVELR NMFGETLHKA VQGCGAHPAI RMAPSLTFKE KVTSLKFKEK
     PTDLETRSYK CLLLSMVKLI HADPKLLLCN PRKQGPETQS STAELITGLV QLVPQSHMPE
     VAQEAMEALL VLHQLDSIDL WNPDAPVETF WEISSQMLFY ICKKLTSHQM LSSTEILKWL
     REILICRNKF LLKNKQADRS SCHSLYLYGV GCEMSATGNT TQMSVDHDEF LRACTPGASL
     RKGRGNSSMD STAGCSGTPP ICRQAQTKLE VALYMFLWNP DTEAVLVAMS CFRHLCEEAD
     IRCGVDEVSV HNFLPNYNTF MEFASVSNMM STGRAALQKR VMALLRRIEH PTAGNIEAWE
     DTHAKWEQAT KLILNYPKAK MEDGQAAESL HKTIVKRRMS HVSGGGSIDL SDTDSLQEWI
     NMTGFLCALG GVCLQQRSSS GLATYSPPMG AVSERKGSMI SVMSSEGNID SPVSRFMDRL
     LSLMVCNHEK VGLQIRTNVK DLVGLELSPA LYPMLFNKLK NTISKFFDSQ GQVLLSDSNT
     QFVEQTIAIM KNLLDNHTEG SSEHLGQASI ETMMLNLVRY VRVLGNMVHA IQIKTKLCQL
     VEVMMARRDD LSFCQEMKFR NKMVEYLTDW VMGTSNQAAD DDIKCLTRDL DQASMEAVVS
     LLAGLPLQPE EGDGVELMEA KSQLFLKYFT LFMNLLNDCS EVEDENAQTG GRKRGMSRRL
     ASLRHCTVLA MSNLLNANVD SGLMHSIGLG YHKDLQTRAT FMEVLTKILQ QGTEFDTLAE
     TVLADRFERL VELVTMMGDQ GELPIAMALA NVVPCSQWDE LARVLVTLFD SRHLLYQLLW
     NMFSKEVELA DSMQTLFRGN SLASKIMTFC FKVYGATYLQ KLLDPLLRVI ITSSDWQHVS
     FEVDPTRLEP SESLEENQRN LLQMTEKFFH AIISSSSEFP SQLRSVCHCL YQATCHSLLN
     KATVKERKEN KKSVVSQRFP QNSIGAVGSA MFLRFINPAI VSPYEAGILD KKPPPRIERG
     LKLMSKVLQS IANHVLFTKE EHMRPFNDFV KSNFDLARRF FLDIASDCPT SDAVNHSLSF
     ISDGNVLALH RLLWNNQEKI GQYLSSNRDH KAVGRRPFDK MATLLAYLGP PEHKPVADTH
     WSSLNLTSSK FEEFMTRHQV HEKEEFKALK TLSIFYQAGT SKAGNPIFYY VARRFKTGQI
     NGDLLIYHVL LTLKPYYAKP YEIVVDLTHT GPSNRFKTDF LSKWFVVFPG FAYDNVSAVY
     IYNCNSWVRE YTKYHERLLT GLKGSKRLIF IDCPGKLAEH IEHEQQKLPA ATLALEEDLK
     VFHNALKLAH KDTKVSIKVG STAVQVTSAE RTKVLGQSVF LNDIYYASEI EEICLVDENQ
     FTLTIANQGT PLTFMHQECE AIVQSIIHIR TRWELSQPDS IPQHTKIRPK DVPGTLLNIA
     LLNLGSSDPS LRSAAYNLLC ALTCTFNLKI EGQLLETSGL CIPANNTLFI VSISKTLAAN
     EPHLTLEFLE ECISGFSKSS IELKHLCLEY MTPWLSNLVR FCKHNDDAKR QRVTAILDKL
     ITMTINEKQM YPSIQAKIWG SLGQITDLLD VVLDSFIKTS ATGGLGSIKA EVMADTAVAL
     ASGNVKLVSS KVIGRMCKII DKTCLSPTPT LEQHLMWDDI AILARYMLML SFNNSLDVAA
     HLPYLFHVVT FLVATGPLSL RASTHGLLIN IIHSLCTCSQ LHFSEETKQV LRLSLTEFSL
     PKFYLLFGIS KVKSAAVIAF RSSYRDRSFS PGSYERETFA LTSLETVTEA LLEIMEACMR
     DIPTCKWLDQ WTELAQRFAF QYNPSLQPRA LVVFGCISKR VSHGQIKQII RILSKALESC
     LKGPDTYNSQ VLIESTVIAL TKLQPLLNKD SPLHKALFWV AVAVLQLDEV NLYSAGTALL
     EQNLHTLDSL RIFNDKSPEE VFMAIRNPLE WHCKQMDHFV GLNFNSNFNF ALVGHLLKGY
     RHPSPAIVAR TVRILHTLLT LVNKHRNCDK FEVNTQSVAY LAALLTVSEE VRSRCSLKHR
     KSLLLTDISM ENVPMDTYPI HHGDPSYRTL KETQPWSSPK GSEGYLAATY PAVGQTSPRA
     RKSMSLDMGQ PSQANTKKLL GTRKSFDHLI SDTKAPKRQE MESGITTPPK MRRVAETDYE
     METQRIPSSQ QHPHLRKVSV SESNVLLDEE VLTDPKIQAL LLTVLATLVK YTTDEFDQRI
     LYEYLAEASV VFPKVFPVVH NLLDSKINTL LSLCQDPNLL NPIHGIVQSV VYHEESPPQY
     QTSYLQSFGF NGLWRFAGPF SKQTQIPDYA ELIVKFLDAL IDTYLPGIDE ETSEESLLTP
     TSPYPPALQS QLSITANLNL SNSMTSLATS QHSPGLDKEN VELSPTAGHC NSGRTRHGSA
     SQVQKQRSAG SFKRNSIKKI V
//
ID   CDK16_MOUSE             Reviewed;         496 AA.
AC   Q04735;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   08-MAR-2011, entry version 107.
DE   RecName: Full=Cyclin-dependent kinase 16;
DE            EC=2.7.11.22;
DE   AltName: Full=CRK5;
DE   AltName: Full=Cell division protein kinase 16;
DE   AltName: Full=PCTAIRE-motif protein kinase 1;
DE   AltName: Full=Serine/threonine-protein kinase PCTAIRE-1;
GN   Name=Cdk16; Synonyms=Crk5, Pctk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC   TISSUE=Fibroblast;
RX   MEDLINE=93064701; PubMed=1437147;
RA   Okuda T., Cleveland J.L., Downing J.R.;
RT   "PCTAIRE-1 and PCTAIRE-3, two members of a novel cdc2/CDC28-related
RT   protein kinase gene family.";
RL   Oncogene 7:2249-2258(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 290-325.
RC   STRAIN=CBA; TISSUE=Bone marrow;
RX   MEDLINE=93185941; PubMed=8444355; DOI=10.1016/0378-1119(93)90411-U;
RA   Ershler M.A., Nagorskaya T.V., Visser J.W.M., Belyavsky A.V.;
RT   "Novel CDC2-related protein kinases produced in murine hematopoietic
RT   stem cells.";
RL   Gene 124:305-306(1993).
RN   [4]
RP   INTERACTION WITH YWHAH; YWHAQ AND YWHAZ.
RX   MEDLINE=97340943; PubMed=9197417; DOI=10.1007/s004380050453;
RA   Sladeczek F., Camonis J.H., Burnol A.-F., Le Bouffant F.;
RT   "The Cdk-like protein PCTAIRE-1 from mouse brain associates with p11
RT   and 14-3-3 proteins.";
RL   Mol. Gen. Genet. 254:571-577(1997).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110 AND SER-153, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May play a role in signal transduction cascades in
CC       terminally differentiated cells.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Found in a complex containing CABLES1, CDK17 and TDRD7
CC       (By similarity). Interacts with YWHAH, YWHAQ and YWHAZ.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=Q04735-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=Q04735-2; Sequence=VSP_004801, VSP_004802;
CC   -!- TISSUE SPECIFICITY: Ubiquitous with highest levels in testis and
CC       brain, with longer form predominant in all tissues except the
CC       testis.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. CDC2/CDKX subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X69025; CAA48787.1; -; mRNA.
DR   EMBL; BC011069; AAH11069.1; -; mRNA.
DR   EMBL; X64606; CAA45890.1; -; mRNA.
DR   IPI; IPI00109670; -.
DR   IPI; IPI00228556; -.
DR   PIR; S30435; S30435.
DR   RefSeq; NP_035179.1; NM_011049.4.
DR   UniGene; Mm.102574; -.
DR   UniGene; Mm.392081; -.
DR   ProteinModelPortal; Q04735; -.
DR   SMR; Q04735; 162-472.
DR   STRING; Q04735; -.
DR   PhosphoSite; Q04735; -.
DR   PRIDE; Q04735; -.
DR   Ensembl; ENSMUST00000033380; ENSMUSP00000033380; ENSMUSG00000031065.
DR   GeneID; 18555; -.
DR   KEGG; mmu:18555; -.
DR   UCSC; uc009sto.1; mouse.
DR   CTD; 18555; -.
DR   MGI; MGI:97516; Cdk16.
DR   eggNOG; roNOG06036; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG014652; -.
DR   InParanoid; Q04735; -.
DR   OMA; FFSLGER; -.
DR   OrthoDB; EOG44BB24; -.
DR   PhylomeDB; Q04735; -.
DR   BRENDA; 2.7.11.22; 244.
DR   NextBio; 294376; -.
DR   ArrayExpress; Q04735; -.
DR   Bgee; Q04735; -.
DR   CleanEx; MM_PCTK1; -.
DR   Genevestigator; Q04735; -.
DR   GermOnline; ENSMUSG00000031065; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004693; F:cyclin-dependent protein kinase activity; IEA:EC.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    496       Cyclin-dependent kinase 16.
FT                                /FTId=PRO_0000086485.
FT   DOMAIN      165    446       Protein kinase.
FT   NP_BIND     171    179       ATP (By similarity).
FT   ACT_SITE    286    286       Proton acceptor (By similarity).
FT   BINDING     194    194       ATP (By similarity).
FT   MOD_RES      12     12       Phosphoserine (By similarity).
FT   MOD_RES      14     14       Phosphothreonine (By similarity).
FT   MOD_RES      36     36       Phosphoserine (By similarity).
FT   MOD_RES      42     42       Phosphoserine (By similarity).
FT   MOD_RES      65     65       Phosphoserine (By similarity).
FT   MOD_RES      78     78       Phosphoserine (By similarity).
FT   MOD_RES      82     82       Phosphoserine (By similarity).
FT   MOD_RES      86     86       Phosphoserine (By similarity).
FT   MOD_RES      88     88       Phosphothreonine (By similarity).
FT   MOD_RES      89     89       Phosphoserine (By similarity).
FT   MOD_RES      90     90       Phosphoserine (By similarity).
FT   MOD_RES      95     95       Phosphoserine (By similarity).
FT   MOD_RES     110    110       Phosphoserine.
FT   MOD_RES     119    119       Phosphoserine (By similarity).
FT   MOD_RES     135    135       Phosphothreonine (By similarity).
FT   MOD_RES     138    138       Phosphoserine (By similarity).
FT   MOD_RES     153    153       Phosphoserine.
FT   MOD_RES     155    155       Phosphoserine (By similarity).
FT   MOD_RES     175    175       Phosphothreonine (By similarity).
FT   MOD_RES     176    176       Phosphotyrosine (By similarity).
FT   MOD_RES     478    478       Phosphoserine (By similarity).
FT   MOD_RES     480    480       Phosphoserine (By similarity).
FT   VAR_SEQ       1     66       Missing (in isoform Short).
FT                                /FTId=VSP_004801.
FT   VAR_SEQ      67     67       P -> MYTNGYDEEIYYIGGKRVFLTPKAWPFPLPTP (in
FT                                isoform Short).
FT                                /FTId=VSP_004802.
SQ   SEQUENCE   496 AA;  55914 MW;  0746036524B1FB5F CRC64;
     MDRMKKIKRQ LSMTLRGGRG IDKTNGVPEQ IGLDESGGGG GSDLGEAPTR IAPGELRSVR
     GPLSSAPEIV HEDMKMGSDG ESDQASATSS DEVQSPVRVR MRNHPPRKIS TEDINKRLSL
     PADIRLPEGY LEKLTLNSPI FDKPLSRRLR RVSLSEIGFG KLETYIKLDK LGEGTYATVY
     KGKSKLTDNL VALKEIRLEH EEGAPCTAIR EVSLLKDLKH ANIVTLHDII HTEKSLTLVF
     EYLDKDLKQY LDDCGNVINM HNVKLFLFQL LRGLAYCHRQ KVLHRDLKPQ NLLINERGEL
     KLADFGLARA KSIPTKTYSN EVVTLWYRPP DILLGSTDYS TQIDMWGVGC IFYEMATGRP
     LFPGSTVEEQ LHFIFRILGT PTEETWPGIL SNEEFRTYNY PKYRAEALLS HAPRLDSDGA
     DLLTKLLQFE GRNRISAEDA RKHPFFLSLG ERIHKLPDTT SIFALKEVQL QKEANIRSTS
     MPDSGRPAFR VVDTEF
//
ID   YES_MOUSE               Reviewed;         541 AA.
AC   Q04736;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 122.
DE   RecName: Full=Proto-oncogene tyrosine-protein kinase Yes;
DE            EC=2.7.10.2;
DE   AltName: Full=Proto-oncogene c-Yes;
DE   AltName: Full=p61-Yes;
GN   Name=Yes1; Synonyms=Yes;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=93173515; PubMed=8437854;
RA   Klages S., Adam D., Eiseman E., Fargnoli J., Dymecki S.M.,
RA   Desiderio S.V., Bolen J.B.;
RT   "Molecular cloning and analysis of cDNA encoding the murine c-yes
RT   tyrosine protein kinase.";
RL   Oncogene 8:713-719(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 391-458.
RX   MEDLINE=94266162; PubMed=8206383; DOI=10.1016/0378-1119(94)90106-6;
RA   Hebert B., Bergeron J., Tijssen P., Potworowski E.F.;
RT   "Protein tyrosine kinases transcribed in a murine thymic medullary
RT   epithelial cell line.";
RL   Gene 143:257-260(1994).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-424, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-192; TYR-220; TYR-424
RP   AND TYR-535, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [6]
RP   STRUCTURE BY NMR OF 62-167.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the SH3_1 domain of Yamaguchi sarcoma viral (v-
RT   Yes) oncogene homolog 1.";
RL   Submitted (APR-2008) to the PDB data bank.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBUNIT: Interacts with FASLG (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity).
CC   -!- PTM: Autophosphorylated (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. SRC subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X67677; CAA47909.1; -; mRNA.
DR   EMBL; BC010594; AAH10594.1; -; mRNA.
DR   EMBL; L25762; AAA40020.1; -; mRNA.
DR   IPI; IPI00109672; -.
DR   PIR; I48318; S31645.
DR   RefSeq; NP_033561.1; NM_009535.2.
DR   UniGene; Mm.4558; -.
DR   PDB; 2YT6; NMR; -; A=71-167.
DR   PDBsum; 2YT6; -.
DR   ProteinModelPortal; Q04736; -.
DR   SMR; Q04736; 83-541.
DR   STRING; Q04736; -.
DR   PhosphoSite; Q04736; -.
DR   PRIDE; Q04736; -.
DR   Ensembl; ENSMUST00000072311; ENSMUSP00000072154; ENSMUSG00000014932.
DR   GeneID; 22612; -.
DR   KEGG; mmu:22612; -.
DR   UCSC; uc008wzs.1; mouse.
DR   CTD; 22612; -.
DR   MGI; MGI:99147; Yes1.
DR   eggNOG; roNOG07837; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG008761; -.
DR   InParanoid; Q04736; -.
DR   OMA; YEARTTD; -.
DR   OrthoDB; EOG4KKZ2S; -.
DR   BRENDA; 2.7.10.2; 244.
DR   NextBio; 302969; -.
DR   ArrayExpress; Q04736; -.
DR   Bgee; Q04736; -.
DR   Genevestigator; Q04736; -.
DR   GermOnline; ENSMUSG00000014932; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0015758; P:glucose transport; IDA:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Kinase; Lipoprotein; Myristate;
KW   Nucleotide-binding; Phosphoprotein; Proto-oncogene; SH2 domain;
KW   SH3 domain; Transferase; Tyrosine-protein kinase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    541       Proto-oncogene tyrosine-protein kinase
FT                                Yes.
FT                                /FTId=PRO_0000088182.
FT   DOMAIN       89    150       SH3.
FT   DOMAIN      156    253       SH2.
FT   DOMAIN      275    528       Protein kinase.
FT   NP_BIND     281    289       ATP (By similarity).
FT   ACT_SITE    394    394       Proton acceptor (By similarity).
FT   BINDING     303    303       ATP (By similarity).
FT   MOD_RES      11     11       Phosphoserine (By similarity).
FT   MOD_RES      26     26       Phosphoserine (By similarity).
FT   MOD_RES      32     32       Phosphotyrosine (By similarity).
FT   MOD_RES     109    109       Phosphoserine (By similarity).
FT   MOD_RES     192    192       Phosphotyrosine.
FT   MOD_RES     193    193       Phosphoserine (By similarity).
FT   MOD_RES     220    220       Phosphotyrosine.
FT   MOD_RES     221    221       Phosphotyrosine (By similarity).
FT   MOD_RES     334    334       Phosphotyrosine (By similarity).
FT   MOD_RES     343    343       Phosphotyrosine (By similarity).
FT   MOD_RES     424    424       Phosphotyrosine; by autocatalysis.
FT   MOD_RES     444    444       Phosphotyrosine (By similarity).
FT   MOD_RES     535    535       Phosphotyrosine.
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
FT   STRAND       93     98
FT   STRAND      115    120
FT   STRAND      127    132
FT   TURN        142    144
FT   STRAND      145    150
FT   HELIX       154    156
SQ   SEQUENCE   541 AA;  60630 MW;  9A773C39D2119EA6 CRC64;
     MGCIKSKENK SPAIKYTPEN LTEPVSPSAS HYGVEHATVA PTSSTKGASV NFNSLSMTPF
     GGSSGVTPFG GASSSFSVVS SSYPTGLTGG VTIFVALYDY EARTTEDLSF KKGERFQIIN
     NTEGDWWEAR SIATGKSGYI PSNYVVPADS IQAEEWYFGK MGRKDAERLL LNPGNQRGIF
     LVRESETTKG AYSLSIRDWD EVRGDNVKHY KIRKLDNGGY YITTRAQFDT LQKLVKHYTE
     HADGLCHKLT TVCPTVKPQT QGLAKDAWEI PRESLRLEVK LGQGCFGEVW MGTWNGTTKV
     AIKTLKPGTM MPEAFLQEAQ IMKKLRHDKL VPLYAVVSEE PIYIVTEFMS KGSLLDFLKE
     GDGKYLKLPQ LVDMAAQIAD GMAYIERMNY IHRDLRAANI LVGENLICKI ADFGLARLIE
     DNEYTARQGA KFPIKWTAPE AALYGRFTIK SDVWSFGILQ TELVTKGRVP YPGMVNREVL
     EQVERGYRMP CPQGCPESLH ELMNLCWKKD PDERPTFEYI QSFLEDYFTA TEPQYQPGEN
     L
//
ID   TOP1_MOUSE              Reviewed;         767 AA.
AC   Q04750; A2A4B7;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=DNA topoisomerase 1;
DE            EC=5.99.1.2;
DE   AltName: Full=DNA topoisomerase I;
GN   Name=Top1; Synonyms=Top-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=93216125; PubMed=8096488; DOI=10.1016/0378-1119(93)90331-V;
RA   Koiwai O., Yasui Y., Sakai Y., Watanabe T., Ishii K., Yanagihara S.,
RA   Andoh T.;
RT   "Cloning of the mouse cDNA encoding DNA topoisomerase I and
RT   chromosomal location of the gene.";
RL   Gene 125:211-216(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Hui C.-F., Lo C.K., Hwang J.;
RT   "Cloning and characterization of mouse topoisomerase I cDNA.";
RL   Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- FUNCTION: The reaction catalyzed by topoisomerases leads to the
CC       conversion of one topological isomer of DNA to another.
CC   -!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded
CC       DNA, followed by passage and rejoining.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm.
CC       Note=Diffuse nuclear localization with some enrichment in
CC       nucleoli. On CPT treatment, cleared from nucleoli into
CC       nucleoplasm. Sumolyated forms found in both nucleoplasm and
CC       nucleoli (By similarity).
CC   -!- PTM: Sumoylated. Lys-119 is the main site of sumoylation.
CC       Sumoylation plays a role in partitioning TOP1 between nucleoli and
CC       nucleoplasm. Levels are dramatically increased on camptothecin
CC       (CPT) treatment (By similarity).
CC   -!- MISCELLANEOUS: Eukaryotic topoisomerase I and II can relax both
CC       negative and positive supercoils, whereas prokaryotic enzymes
CC       relax only negative supercoils.
CC   -!- MISCELLANEOUS: When a topoisomerase transiently breaks a DNA
CC       backbone bond, it simultaneously forms a protein-DNA link, in
CC       which a tyrosyl oxygen in the enzyme is joined to a DNA phosphorus
CC       at one end of the enzyme-severed DNA strand.
CC   -!- SIMILARITY: Belongs to the eukaryotic type I topoisomerase family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D10061; BAA00950.1; -; mRNA.
DR   EMBL; L20632; AAA40466.1; -; mRNA.
DR   EMBL; AL590414; CAM20297.1; -; Genomic_DNA.
DR   EMBL; AL591673; CAM20297.1; JOINED; Genomic_DNA.
DR   EMBL; AL591673; CAM25349.1; -; Genomic_DNA.
DR   EMBL; AL590414; CAM25349.1; JOINED; Genomic_DNA.
DR   IPI; IPI00109764; -.
DR   PIR; JU0144; JU0144.
DR   RefSeq; NP_033434.2; NM_009408.2.
DR   UniGene; Mm.217233; -.
DR   ProteinModelPortal; Q04750; -.
DR   SMR; Q04750; 203-767.
DR   MINT; MINT-1868161; -.
DR   STRING; Q04750; -.
DR   PhosphoSite; Q04750; -.
DR   PRIDE; Q04750; -.
DR   Ensembl; ENSMUST00000109468; ENSMUSP00000105094; ENSMUSG00000070544.
DR   GeneID; 21969; -.
DR   KEGG; mmu:21969; -.
DR   UCSC; uc008nqy.1; mouse.
DR   CTD; 21969; -.
DR   MGI; MGI:98788; Top1.
DR   eggNOG; roNOG09781; -.
DR   HOGENOM; HBG521929; -.
DR   HOVERGEN; HBG007988; -.
DR   InParanoid; Q04750; -.
DR   OMA; ESVKFYY; -.
DR   OrthoDB; EOG4V170F; -.
DR   PhylomeDB; Q04750; -.
DR   BRENDA; 5.99.1.2; 244.
DR   NextBio; 301666; -.
DR   PMAP-CutDB; Q04750; -.
DR   ArrayExpress; Q04750; -.
DR   Bgee; Q04750; -.
DR   CleanEx; MM_TOP1; -.
DR   Genevestigator; Q04750; -.
DR   GermOnline; ENSMUSG00000070544; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043204; C:perikaryon; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase (ATP-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0003917; F:DNA topoisomerase type I activity; IDA:MGI.
DR   GO; GO:0006265; P:DNA topological change; IDA:MGI.
DR   GO; GO:0006268; P:DNA unwinding involved in replication; IEA:InterPro.
DR   GO; GO:0040016; P:embryonic cleavage; IMP:MGI.
DR   InterPro; IPR011010; DNA_brk_join_enz.
DR   InterPro; IPR013034; DNA_topo_domain1.
DR   InterPro; IPR018521; TopoI_AS.
DR   InterPro; IPR001631; TopoI_C.
DR   InterPro; IPR013499; TopoI_C_euk.
DR   InterPro; IPR014711; TopoI_cat_a-hlx-sub_euk.
DR   InterPro; IPR014727; TopoI_cat_a/b-sub_euk.
DR   InterPro; IPR013500; TopoI_cat_euk.
DR   InterPro; IPR008336; TopoI_DNA-bd_euk.
DR   InterPro; IPR013030; TopoI_DNA-bd_mixed-a/b_euk.
DR   InterPro; IPR009054; TopoI_insert_euk.
DR   Gene3D; G3DSA:3.90.15.10; TopoI_cat_a-hlx-sub_euk; 1.
DR   Gene3D; G3DSA:1.10.132.10; TopoI_cat_a/b-sub_euk; 1.
DR   Gene3D; G3DSA:1.10.10.41; TopoI_DNA-bd_a-hlx_euk; 1.
DR   Gene3D; G3DSA:2.170.11.10; TopoI_DNA-bd_mixed-a/b_euk; 2.
DR   Pfam; PF01028; Topoisom_I; 1.
DR   Pfam; PF02919; Topoisom_I_N; 1.
DR   PRINTS; PR00416; EUTPISMRASEI.
DR   SMART; SM00435; TOPEUc; 1.
DR   SUPFAM; SSF56349; DNA_brk_join_enz; 1.
DR   SUPFAM; SSF46596; Topismrse_insert; 1.
DR   SUPFAM; SSF56741; TopoI_DNA_bd_euk; 1.
DR   PROSITE; PS00176; TOPOISOMERASE_I_EUK; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Direct protein sequencing; DNA-binding;
KW   Isomerase; Isopeptide bond; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Topoisomerase; Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    767       DNA topoisomerase 1.
FT                                /FTId=PRO_0000145202.
FT   COMPBIAS     23    206       Lys-rich.
FT   ACT_SITE    725    725       O-(3'-phospho-DNA)-tyrosine intermediate
FT                                (By similarity).
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES     114    114       Phosphoserine (By similarity).
FT   MOD_RES     282    282       N6-acetyllysine (By similarity).
FT   CROSSLNK    105    105       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO)
FT                                (Probable).
FT   CROSSLNK    119    119       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    155    155       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO)
FT                                (Probable).
FT   CONFLICT     91     91       R -> P (in Ref. 2; AAA40466).
FT   CONFLICT    121    121       E -> D (in Ref. 1; BAA00950).
FT   CONFLICT    129    129       A -> V (in Ref. 2; AAA40466).
FT   CONFLICT    161    161       Missing (in Ref. 2; AAA40466).
FT   CONFLICT    167    167       S -> L (in Ref. 2; AAA40466).
FT   CONFLICT    277    277       R -> W (in Ref. 2; AAA40466).
FT   CONFLICT    292    292       E -> G (in Ref. 1; BAA00950).
FT   CONFLICT    522    522       G -> V (in Ref. 2; AAA40466).
FT   CONFLICT    533    533       G -> W (in Ref. 2; AAA40466).
FT   CONFLICT    762    762       D -> Y (in Ref. 2; AAA40466).
SQ   SEQUENCE   767 AA;  90876 MW;  4EA654244F07D5C1 CRC64;
     MSGDHLHNDS QIEADFRLND SHKHKDKHKD REHRHKEHKK DKDKDREKSK HSNSEHKDSE
     KKHKEKEKTK HKDGSSEKHK DKHKDRDKER RKEEKIRAAG DAKIKKEKEN GFSSPPRIKD
     EPEDDGYFAP PKEDIKPLKR LRDEDDADYK PKKIKTEDIK KEKKRKSEEE EDGKLKKPKN
     KDKDKKVAEP DNKKKKPKKE EEQKWKWWEE ERYPEGIKWK FLEHKGPVFA PPYEPLPESV
     KFYYDGKVMK LSPKAEEVAT FFAKMLDHEY TTKEIFRKNF FKDWRKEMTN DEKNTITNLS
     KCDFTQMSQY FKAQSEARKQ MSKEEKLKIK EENEKLLKEY GFCVMDNHRE RIANFKIEPP
     GLFRGRGNHP KMGMLKRRIM PEDIIINCSK DAKVPSPPPG HKWKEVRHDN KVTWLVSWTE
     NIQGSIKYIM LNPSSRIKGE KDWQKYETAR RLKKCVDKIR NQYREDWKSK EMKVRQRAVA
     LYFIDKLALR AGNEKEEGET ADTVGCCSLR VEHINLHPEL DGQEYVVEFD FPGKDSIRYY
     NKVPVEKRVF KNLQLFMENK QPEDDLFDRL NTGILNKHLQ DLMEGLTAKV FRTYNASITL
     QQQLKELTAP DENVPAKILS YNRANRAVAI LCNHQRAPPK TFEKSMMNLQ SKIDAKKDQL
     ADARRDLKSA KADAKVMKDA KTKKVVESKK KAVQRLEEQL MKLEVQATDR EENKQIALGT
     SKLNYLDPRI TVAWCKKWGV PIEKIYNKTQ REKFAWAIDM TDEDYEF
//
ID   SOX9_MOUSE              Reviewed;         507 AA.
AC   Q04887; Q8C7L2; Q91ZK2; Q99KQ0;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Transcription factor SOX-9;
GN   Name=Sox9; Synonyms=Sox-9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129;
RA   Lee H.-H.;
RT   "The gene expression of Sox9 in mouse genital ridges.";
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 113-168.
RX   MEDLINE=93181275; PubMed=8441686; DOI=10.1093/nar/21.3.744;
RA   Wright E.M., Snopek B., Koopman P.;
RT   "Seven new members of the Sox gene family expressed during mouse
RT   development.";
RL   Nucleic Acids Res. 21:744-744(1993).
CC   -!- FUNCTION: Plays an important role in the normal skeletal
CC       development. May regulate the expression of other genes involved
CC       in chondrogenesis by acting as a transcription factor for these
CC       genes (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- SIMILARITY: Contains 1 HMG box DNA-binding domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF421878; AAL16093.1; -; mRNA.
DR   EMBL; AK030187; BAC26830.1; -; mRNA.
DR   EMBL; AK049986; BAC34018.1; -; mRNA.
DR   EMBL; BC004064; AAH04064.1; -; mRNA.
DR   EMBL; BC023796; AAH23796.1; -; mRNA.
DR   EMBL; BC023808; AAH23808.1; -; mRNA.
DR   EMBL; BC023953; AAH23953.1; -; mRNA.
DR   EMBL; BC024958; AAH24958.1; -; mRNA.
DR   EMBL; BC034264; AAH34264.1; -; mRNA.
DR   EMBL; Z18958; CAA79483.1; -; mRNA.
DR   IPI; IPI00131219; -.
DR   PIR; S30243; S30243.
DR   PIR; S52469; S52469.
DR   RefSeq; NP_035578.3; NM_011448.4.
DR   UniGene; Mm.286407; -.
DR   UniGene; Mm.481669; -.
DR   ProteinModelPortal; Q04887; -.
DR   SMR; Q04887; 105-178.
DR   IntAct; Q04887; 1.
DR   STRING; Q04887; -.
DR   PhosphoSite; Q04887; -.
DR   PRIDE; Q04887; -.
DR   Ensembl; ENSMUST00000000579; ENSMUSP00000000579; ENSMUSG00000000567.
DR   GeneID; 20682; -.
DR   KEGG; mmu:20682; -.
DR   UCSC; uc007med.1; mouse.
DR   CTD; 20682; -.
DR   MGI; MGI:98371; Sox9.
DR   eggNOG; roNOG12759; -.
DR   HOVERGEN; HBG002061; -.
DR   InParanoid; Q04887; -.
DR   OMA; GAGHVWM; -.
DR   OrthoDB; EOG4TXBRZ; -.
DR   PhylomeDB; Q04887; -.
DR   NextBio; 299193; -.
DR   ArrayExpress; Q04887; -.
DR   Bgee; Q04887; -.
DR   CleanEx; MM_SOX9; -.
DR   Genevestigator; Q04887; -.
DR   GermOnline; ENSMUSG00000000567; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0010843; F:promoter binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0016563; F:transcription activator activity; IDA:MGI.
DR   GO; GO:0001502; P:cartilage condensation; IMP:MGI.
DR   GO; GO:0001708; P:cell fate specification; IMP:MGI.
DR   GO; GO:0071300; P:cellular response to retinoic acid; IDA:MGI.
DR   GO; GO:0060350; P:endochondral bone morphogenesis; IMP:MGI.
DR   GO; GO:0060517; P:epithelial cell proliferation involved in prostatic bud elongation; IMP:MGI.
DR   GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:MGI.
DR   GO; GO:0001942; P:hair follicle development; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0060729; P:intestinal epithelial structure maintenance; IMP:MGI.
DR   GO; GO:0019100; P:male germ-line sex determination; IMP:MGI.
DR   GO; GO:0030502; P:negative regulation of bone mineralization; IMP:MGI.
DR   GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IMP:MGI.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
DR   GO; GO:0045662; P:negative regulation of myoblast differentiation; IDA:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:MGI.
DR   GO; GO:0014032; P:neural crest cell development; IMP:MGI.
DR   GO; GO:0048709; P:oligodendrocyte differentiation; IMP:MGI.
DR   GO; GO:0030858; P:positive regulation of epithelial cell differentiation; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0042981; P:regulation of apoptosis; IMP:MGI.
DR   GO; GO:0060009; P:Sertoli cell development; IGI:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IGI:MGI.
DR   InterPro; IPR000910; HMG_HMG1/HMG2.
DR   InterPro; IPR009071; HMG_superfamily.
DR   InterPro; IPR022151; Sox_N.
DR   Gene3D; G3DSA:1.10.30.10; HMG-box; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   Pfam; PF12444; Sox_N; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Nucleus; Transcription; Transcription regulation.
FT   CHAIN         1    507       Transcription factor SOX-9.
FT                                /FTId=PRO_0000048741.
FT   DNA_BIND    105    173       HMG box.
FT   COMPBIAS    339    415       Gln/Pro-rich.
FT   COMPBIAS    342    346       Poly-Pro.
FT   CONFLICT     62     62       K -> R (in Ref. 2; BAC34018).
SQ   SEQUENCE   507 AA;  56077 MW;  01FC3B54FF329BDA CRC64;
     MNLLDPFMKM TDEQEKGLSG APSPTMSEDS AGSPCPSGSG SDTENTRPQE NTFPKGEPDL
     KKESEEDKFP VCIREAVSQV LKGYDWTLVP MPVRVNGSSK NKPHVKRPMN AFMVWAQAAR
     RKLADQYPHL HNAELSKTLG KLWRLLNESE KRPFVEEAER LRVQHKKDHP DYKYQPRRRK
     SVKNGQAEAE EATEQTHISP NAIFKALQAD SPHSSSGMSE VHSPGEHSGQ SQGPPTPPTT
     PKTDVQAGKV DLKREGRPLA EGGRQPPIDF RDVDIGELSS DVISNIETFD VNEFDQYLPP
     NGHPGVPATH GQVTYTGSYG ISSTAPTPAT AGHVWMSKQQ APPPPPQQPP QAPQAPQAPP
     QQQAPPQQPQ APQQQQAHTL TTLSSEPGQS QRTHIKTEQL SPSHYSEQQQ HSPQQISYSP
     FNLPHYSPSY PPITRSQYDY ADHQNSGSYY SHAAGQGSGL YSTFTYMNPA QRPMYTPIAD
     TSGVPSIPQT HSPQHWEQPV YTQLTRP
//
ID   CDK18_MOUSE             Reviewed;         451 AA.
AC   Q04899;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Cyclin-dependent kinase 18;
DE            EC=2.7.11.22;
DE   AltName: Full=Cell division protein kinase 18;
DE   AltName: Full=PCTAIRE-motif protein kinase 3;
DE   AltName: Full=Serine/threonine-protein kinase PCTAIRE-3;
GN   Name=Cdk18; Synonyms=Pctk3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fibroblast;
RX   MEDLINE=93064701; PubMed=1437147;
RA   Okuda T., Cleveland J.L., Downing J.R.;
RT   "PCTAIRE-1 and PCTAIRE-3, two members of a novel cdc2/CDC28-related
RT   protein kinase gene family.";
RL   Oncogene 7:2249-2258(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May play a role in signal transduction cascades in
CC       terminally differentiated cells.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- TISSUE SPECIFICITY: In brain, kidney, intestine and at a much
CC       lower level, in fetal tissues.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. CDC2/CDKX subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
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DR   EMBL; X69026; CAA48788.1; -; mRNA.
DR   EMBL; AK004998; BAB23732.1; -; mRNA.
DR   IPI; IPI00111168; -.
DR   PIR; S30436; S30436.
DR   RefSeq; NP_032821.1; NM_008795.2.
DR   UniGene; Mm.28130; -.
DR   ProteinModelPortal; Q04899; -.
DR   SMR; Q04899; 118-428.
DR   STRING; Q04899; -.
DR   PhosphoSite; Q04899; -.
DR   PRIDE; Q04899; -.
DR   Ensembl; ENSMUST00000027697; ENSMUSP00000027697; ENSMUSG00000026437.
DR   GeneID; 18557; -.
DR   KEGG; mmu:18557; -.
DR   UCSC; uc007coh.1; mouse.
DR   CTD; 18557; -.
DR   MGI; MGI:97518; Cdk18.
DR   eggNOG; maNOG16041; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG014652; -.
DR   InParanoid; Q04899; -.
DR   OMA; LQMESPD; -.
DR   PhylomeDB; Q04899; -.
DR   BRENDA; 2.7.11.22; 244.
DR   NextBio; 294380; -.
DR   ArrayExpress; Q04899; -.
DR   Bgee; Q04899; -.
DR   CleanEx; MM_PCTK3; -.
DR   Genevestigator; Q04899; -.
DR   GermOnline; ENSMUSG00000026437; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004693; F:cyclin-dependent protein kinase activity; IEA:EC.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    451       Cyclin-dependent kinase 18.
FT                                /FTId=PRO_0000086491.
FT   DOMAIN      121    402       Protein kinase.
FT   NP_BIND     127    135       ATP (By similarity).
FT   ACT_SITE    242    242       Proton acceptor (By similarity).
FT   BINDING     150    150       ATP (By similarity).
FT   MOD_RES      12     12       Phosphoserine (By similarity).
FT   MOD_RES      14     14       Phosphoserine (By similarity).
FT   MOD_RES      51     51       Phosphoserine (By similarity).
FT   MOD_RES      66     66       Phosphoserine.
FT   MOD_RES      75     75       Phosphoserine (By similarity).
FT   MOD_RES     109    109       Phosphoserine (By similarity).
FT   MOD_RES     111    111       Phosphoserine (By similarity).
FT   MOD_RES     120    120       Phosphothreonine (By similarity).
FT   MOD_RES     134    134       Phosphothreonine (By similarity).
FT   MOD_RES     449    449       Phosphoserine (By similarity).
SQ   SEQUENCE   451 AA;  51848 MW;  3FC500519714F7E0 CRC64;
     MNKMKNFKRR LSLSVPRPET IEESLAEFTE QFNQLHTQTN EDGTDEPEQL SPGMQYQQRQ
     NQRRFSMEDL NKRLSLPMDI RLPQEFLQKL QLENPGLPKP LTRMSRRASL SDIGFGKLET
     YVKLDKLGEG TYATVFKGRS KLTENLVALK EIRLEHEEGA PCTAIREVSL LKDLKHANIV
     TLHDLIHTDR SLTLVFEYLD SDLKQYLDHC GNLMNMHNVK IFMFQLLRGL AYCHHRKILH
     RDLKPQNLLI NERGELKLAD FGLARAKSVP TKTYSNEVVT LWYRPPDVLL GSTEYSTPID
     MWGVGCILYE MATGKPLFPG STVKEELHLI FRLLGTPTEE SWPGVTSISE FRAYNFPRYL
     PQPLLSHAPR LDTEGINLLS SLLLYESKSR MSAEAALNHP YFQSLGDRVH QLHDTASIFS
     LKEIQLQKDP GYRGLAFQHP GRGKSRRQSI F
//
ID   RAC2_MOUSE              Reviewed;         192 AA.
AC   Q05144; Q3TBC4; Q9D8X9;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Ras-related C3 botulinum toxin substrate 2;
DE   AltName: Full=Protein EN-7;
DE   AltName: Full=p21-Rac2;
DE   Flags: Precursor;
GN   Name=Rac2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=90265620; PubMed=2189110;
RA   Shirsat N.V., Pignolo R.J., Kreider B.L., Rovera G.;
RT   "A member of the ras gene superfamily is expressed specifically in T,
RT   B and myeloid hemopoietic cells.";
RL   Oncogene 5:769-772(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Plasma membrane-associated small GTPase which cycles
CC       between an active GTP-bound and inactive GDP-bound state. In
CC       active state binds to a variety of effector proteins to regulate
CC       cellular responses, such as secretory processes, phagocytose of
CC       apoptotic cells and epithelial cell polarization. Augments the
CC       production of reactive oxygen species (ROS) by NADPH oxidase.
CC   -!- ENZYME REGULATION: Regulated by guanine nucleotide exchange
CC       factors (GEFs) which promote the exchange of bound GDP for free
CC       GTP, GTPase activating proteins (GAPs) which increase the GTP
CC       hydrolysis activity, and GDP dissociation inhibitors which inhibit
CC       the dissociation of the nucleotide from the GTPase.
CC   -!- SUBUNIT: Interacts with DOCK2, which may activate it (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane; Lipid-
CC       anchor (By similarity). Note=Membrane-associated when activated
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
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DR   EMBL; X53247; CAA37337.1; -; mRNA.
DR   EMBL; AK007561; BAB25109.1; -; mRNA.
DR   EMBL; AK144136; BAE25721.1; -; mRNA.
DR   EMBL; AK171321; BAE42390.1; -; mRNA.
DR   EMBL; BC005455; AAH05455.1; -; mRNA.
DR   IPI; IPI00137618; -.
DR   PIR; A60194; A60194.
DR   RefSeq; NP_033034.1; NM_009008.3.
DR   UniGene; Mm.1972; -.
DR   ProteinModelPortal; Q05144; -.
DR   SMR; Q05144; 1-181.
DR   IntAct; Q05144; 1.
DR   STRING; Q05144; -.
DR   PhosphoSite; Q05144; -.
DR   PRIDE; Q05144; -.
DR   Ensembl; ENSMUST00000043214; ENSMUSP00000036384; ENSMUSG00000033220.
DR   GeneID; 19354; -.
DR   KEGG; mmu:19354; -.
DR   UCSC; uc007wpp.1; mouse.
DR   CTD; 19354; -.
DR   MGI; MGI:97846; Rac2.
DR   eggNOG; roNOG06989; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; Q05144; -.
DR   OMA; CPQPTRT; -.
DR   OrthoDB; EOG466VN1; -.
DR   PhylomeDB; Q05144; -.
DR   NextBio; 296391; -.
DR   ArrayExpress; Q05144; -.
DR   Bgee; Q05144; -.
DR   CleanEx; MM_RAC2; -.
DR   Genevestigator; Q05144; -.
DR   GermOnline; ENSMUSG00000033220; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IDA:MGI.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IDA:MGI.
DR   GO; GO:0030031; P:cell projection assembly; IDA:MGI.
DR   GO; GO:0006935; P:chemotaxis; IDA:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IGI:MGI.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003578; GTPase_Rho.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00174; RHO; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51420; RHO; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; GTP-binding; Lipoprotein; Membrane;
KW   Methylation; Nucleotide-binding; Prenylation.
FT   CHAIN         1    189       Ras-related C3 botulinum toxin substrate
FT                                2.
FT                                /FTId=PRO_0000042048.
FT   PROPEP      190    192       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000042049.
FT   NP_BIND      10     17       GTP (By similarity).
FT   NP_BIND      57     61       GTP (By similarity).
FT   NP_BIND     115    118       GTP (By similarity).
FT   MOTIF        32     40       Effector region (Potential).
FT   MOD_RES     147    147       N6-acetyllysine (By similarity).
FT   MOD_RES     189    189       Cysteine methyl ester (By similarity).
FT   LIPID       189    189       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   CONFLICT     60     60       G -> V (in Ref. 2; BAB25109).
SQ   SEQUENCE   192 AA;  21441 MW;  2A1F1266AB9D7705 CRC64;
     MQAIKCVVVG DGAVGKTCLL ISYTTNAFPG EYIPTVFDNY SANVMVDSKP VNLGLWDTAG
     QEDYDRLRPL SYPQTDVFLI CFSLVSPASY ENVRAKWFPE VRHHCPSTPI ILVGTKLDLR
     DDKDTIEKLK EKKLAPITYP QGLALAKDID SVKYLECSAL TQRGLKTVFD EAIRAVLCPQ
     PTRQQKRPCS LL
//
ID   MARK2_MOUSE             Reviewed;         776 AA.
AC   Q05512; Q3T9L3; Q6PDR4; Q8BR95;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 113.
DE   RecName: Full=Serine/threonine-protein kinase MARK2;
DE            EC=2.7.11.1;
DE   AltName: Full=ELKL motif kinase 1;
DE            Short=EMK-1;
DE   AltName: Full=MAP/microtubule affinity-regulating kinase 2;
GN   Name=Mark2; Synonyms=Emk;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Embryo;
RX   MEDLINE=93364122; PubMed=8358177; DOI=10.1007/BF00360595;
RA   Inglis J.D., Lee M., Hill R.E.;
RT   "Emk, a protein kinase with homologs in yeast maps to mouse chromosome
RT   19.";
RL   Mamm. Genome 4:401-403(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC   STRAIN=NOD; TISSUE=Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=129; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=10491259; DOI=10.1006/dbio.1999.9379;
RA   Bessone S., Vidal F., Le Bouc Y., Epelbaum J., Bluet-Pajot M.T.,
RA   Darmon M.;
RT   "EMK protein kinase-null mice: dwarfism and hypofertility associated
RT   with alterations in the somatotrope and prolactin pathways.";
RL   Dev. Biol. 214:87-101(1999).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-208 AND SER-453, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-208 AND SER-568, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; SER-483 AND SER-592,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Role in epithelial morphogenesis. Modulates the
CC       developmental decision to build a columnar versus a hepatic
CC       epithelial cell apparently by promoting a switch from a direct to
CC       a transcytotic mode of apical protein delivery. Essential for the
CC       asymmetric development of membrane domains of polarized epithelial
CC       cells. May play a role in hormone secretion in the pituitary
CC       and/or the hypothalamus.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activated by phosphorylation on Thr-208 by
CC       STK11 in complex with STE20-related adapter-alpha (STRAD alpha)
CC       pseudo kinase and CAB39 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       (By similarity). Note=Phosphorylated by PRKCZ in polarized
CC       epithelial cells, resulting in an interaction with Ywhaz which
CC       promotes relocation from the lateral to the apical membrane (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q05512-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q05512-2; Sequence=VSP_013341;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q05512-3; Sequence=VSP_013342;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q05512-4; Sequence=VSP_013342, VSP_022597;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in adult kidney and testis,
CC       lower levels in heart, brain, spleen, lung and liver. Expressed in
CC       the head and neural fold in 8 dpc embryos, the limb buds,
CC       telencephalic vesicles, eyes, branchial archs and heart at 11.5
CC       dpc, the ectoderm at 13 dpc and epiderm, hair and whisker
CC       follicles at 15 dpc.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. MARK subfamily.
CC   -!- SIMILARITY: Contains 1 KA1 (kinase-associated) domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 UBA domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC32312.1; Type=Frameshift; Positions=772;
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DR   EMBL; X70764; CAA50040.1; -; mRNA.
DR   EMBL; AK045329; BAC32312.1; ALT_FRAME; mRNA.
DR   EMBL; AK172444; BAE43007.1; -; mRNA.
DR   EMBL; BC058556; AAH58556.1; -; mRNA.
DR   IPI; IPI00111754; -.
DR   IPI; IPI00554855; -.
DR   IPI; IPI00554871; -.
DR   IPI; IPI00762727; -.
DR   PIR; I48609; I48609.
DR   RefSeq; NP_001073857.1; NM_001080388.1.
DR   RefSeq; NP_001073858.1; NM_001080389.1.
DR   RefSeq; NP_001073859.1; NM_001080390.1.
DR   RefSeq; NP_031954.2; NM_007928.2.
DR   UniGene; Mm.258986; -.
DR   ProteinModelPortal; Q05512; -.
DR   SMR; Q05512; 49-363, 680-776.
DR   STRING; Q05512; -.
DR   PhosphoSite; Q05512; -.
DR   PRIDE; Q05512; -.
DR   Ensembl; ENSMUST00000032556; ENSMUSP00000032556; ENSMUSG00000024969.
DR   Ensembl; ENSMUST00000032557; ENSMUSP00000032557; ENSMUSG00000024969.
DR   Ensembl; ENSMUST00000051711; ENSMUSP00000108969; ENSMUSG00000024969.
DR   GeneID; 13728; -.
DR   KEGG; mmu:13728; -.
DR   UCSC; uc008gks.1; mouse.
DR   UCSC; uc008gkt.1; mouse.
DR   CTD; 13728; -.
DR   MGI; MGI:99638; Mark2.
DR   eggNOG; roNOG09909; -.
DR   GeneTree; ENSGT00600000084258; -.
DR   HOVERGEN; HBG052453; -.
DR   InParanoid; Q05512; -.
DR   OrthoDB; EOG4C2H8X; -.
DR   PhylomeDB; Q05512; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 284516; -.
DR   ArrayExpress; Q05512; -.
DR   Bgee; Q05512; -.
DR   CleanEx; MM_MARK2; -.
DR   Genevestigator; Q05512; -.
DR   GermOnline; ENSMUSG00000024969; Mus musculus.
DR   GO; GO:0045180; C:basal cortex; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; ISS:UniProtKB.
DR   GO; GO:0007243; P:intracellular protein kinase cascade; ISS:UniProtKB.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   InterPro; IPR001772; Kinase-assoc_KA1.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   Gene3D; G3DSA:3.30.310.80; Kinase-assoc_KA1; 1.
DR   Pfam; PF02149; KA1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF103243; Kinase-assoc_KA1; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50032; KA1; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell membrane;
KW   Developmental protein; Differentiation; Kinase; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    776       Serine/threonine-protein kinase MARK2.
FT                                /FTId=PRO_0000086302.
FT   DOMAIN       53    304       Protein kinase.
FT   DOMAIN      323    362       UBA.
FT   DOMAIN      727    776       KA1.
FT   NP_BIND      59     67       ATP (By similarity).
FT   ACT_SITE    175    175       Proton acceptor (By similarity).
FT   BINDING      82     82       ATP (By similarity).
FT   MOD_RES      29     29       Phosphoserine (By similarity).
FT   MOD_RES      40     40       Phosphoserine.
FT   MOD_RES      42     42       Phosphothreonine (By similarity).
FT   MOD_RES      43     43       Phosphoserine (By similarity).
FT   MOD_RES     197    197       Phosphoserine (By similarity).
FT   MOD_RES     208    208       Phosphothreonine.
FT   MOD_RES     212    212       Phosphoserine (By similarity).
FT   MOD_RES     365    365       Phosphoserine (By similarity).
FT   MOD_RES     390    390       Phosphoserine (By similarity).
FT   MOD_RES     409    409       Phosphoserine (By similarity).
FT   MOD_RES     418    418       Phosphothreonine (By similarity).
FT   MOD_RES     419    419       Phosphoserine (By similarity).
FT   MOD_RES     421    421       Phosphoserine (By similarity).
FT   MOD_RES     422    422       Phosphotyrosine (By similarity).
FT   MOD_RES     453    453       Phosphoserine.
FT   MOD_RES     468    468       Phosphoserine (By similarity).
FT   MOD_RES     476    476       Phosphoserine (By similarity).
FT   MOD_RES     480    480       Phosphoserine (By similarity).
FT   MOD_RES     483    483       Phosphoserine.
FT   MOD_RES     490    490       Phosphoserine (By similarity).
FT   MOD_RES     530    530       Phosphoserine (By similarity).
FT   MOD_RES     566    566       Phosphoserine (By similarity).
FT   MOD_RES     568    568       Phosphoserine.
FT   MOD_RES     573    573       Phosphoserine (By similarity).
FT   MOD_RES     592    592       Phosphoserine.
FT   MOD_RES     593    593       Phosphothreonine; by PKC/PRKCZ (By
FT                                similarity).
FT   MOD_RES     616    616       Phosphoserine (By similarity).
FT   MOD_RES     618    618       Phosphoserine (By similarity).
FT   MOD_RES     628    628       Phosphoserine (By similarity).
FT   MOD_RES     655    655       Phosphothreonine (By similarity).
FT   MOD_RES     710    710       Phosphoserine (By similarity).
FT   VAR_SEQ     321    339       PDYKDPRRTELMVSMGYTR -> LTTGPRDRVDGVNGLHT
FT                                (in isoform 2).
FT                                /FTId=VSP_013341.
FT   VAR_SEQ     502    555       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_013342.
FT   VAR_SEQ     640    640       V -> VRRNLSFRFA (in isoform 4).
FT                                /FTId=VSP_022597.
FT   CONFLICT    161    162       SA -> LH (in Ref. 1; CAA50040).
FT   CONFLICT    368    368       L -> P (in Ref. 1; CAA50040).
FT   CONFLICT    760    760       S -> Y (in Ref. 2; BAC32312).
SQ   SEQUENCE   776 AA;  86306 MW;  533C8DE0B5EC507E CRC64;
     MSSARTPLPT LNERDTEQPT LGHLDSKPSS KSNMLRGRNS ATSADEQPHI GNYRLLKTIG
     KGNFAKVKLA RHILTGKEVA VKIIDKTQLN SSSLQKLFRE VRIMKVLNHP NIVKLFEVIE
     TEKTLYLVME YASGGEVFDY LVAHGRMKEK EARAKFRQIV SAVQYCHQKF IVHRDLKAEN
     LLLDADMNIK IADFGFSNEF TFGNKLDTFC GSPPYAAPEL FQGKKIDGPE VDVWSLGVIL
     YTLVSGSLPF DGQNLKELRE RVLRGKYRIP FYMSTDCENL LKKFLILNPS KRGTLEQIMK
     DRWMNVGHED DELKPYVEPL PDYKDPRRTE LMVSMGYTRE EIQDSLVGQR YNEVMATYLL
     LGYKSSELEG DTITLKPRPS ADLTNSSAPS PSHKVQRSVS ANPKQRRSSD QAVPAIPTSN
     SYSKKTQSNN AENKRPEEET GRKASSTAKV PASPLPGLDR KKTTPAPSTN SVLSTSTNRS
     RNSPLLDRAS LGQASIQNGK DSLTMPGSRA STASASAAVS AARPRQHQKS MSASVHPNKA
     SGLPPTESNC EVPRPSTAPQ RVPVASPSAH NISSSSGAPD RTNFPRGVSS RSTFHAGQLR
     QVRDQQNLPY GVTPASPSGH SQGRRGASGS IFSKFTSKFV RRNLNEPESK DRVETLRPHV
     VGSGGTDKDK EEFREAKPRS LRFTWSMKTT SSMEPNEMMR EIRKVLDANS CQSELHERYM
     LLCVHGTPGH ENFVQWEMEV CKLPRLSLNG VRFKRISGTS MAFKNIASKI ANELKL
//
ID   FABP5_MOUSE             Reviewed;         135 AA.
AC   Q05816;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 104.
DE   RecName: Full=Fatty acid-binding protein, epidermal;
DE   AltName: Full=Epidermal-type fatty acid-binding protein;
DE            Short=E-FABP;
DE   AltName: Full=Fatty acid-binding protein 5;
DE   AltName: Full=Keratinocyte lipid-binding protein;
DE   AltName: Full=Psoriasis-associated fatty acid-binding protein homolog;
DE            Short=PA-FABP;
GN   Name=Fabp5; Synonyms=Fabpe, Klbp, Mal1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Keratinocyte;
RX   MEDLINE=93352523; PubMed=8349619;
RA   Krieg P., Feil S., Fuerstenberger G., Bowden T.G.;
RT   "Tumor-specific overexpression of a novel keratinocyte lipid-binding
RT   protein. Identification and characterization of a cloned sequence
RT   activated during multistage carcinogenesis in mouse skin.";
RL   J. Biol. Chem. 268:17362-17369(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   MEDLINE=98332726; PubMed=9666100; DOI=10.1016/S0378-1119(98)00262-5;
RA   Bleck B., Hohoff C., Binas B., Rustow B., Dixkens C., Hameister H.,
RA   Boerchers T., Spener F.;
RT   "Cloning and chromosomal localisation of the murine epidermal-type
RT   fatty acid binding protein gene (Fabpe).";
RL   Gene 215:123-130(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=99013878; PubMed=9795232; DOI=10.1016/S0378-1119(98)00446-6;
RA   Hertzel A.V., Bernlohr D.A.;
RT   "Cloning and chromosomal location of the murine Keratinocyte lipid-
RT   binding protein gene.";
RL   Gene 221:235-243(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 13-24, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
CC   -!- FUNCTION: High specificity for fatty acids. Highest affinity for
CC       C18 chain length (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Most abundant in keratinocytes and also in
CC       stratified epithelia of epidermis and tongue. Relatively high
CC       levels found in adipose and mammary tissues and small amounts
CC       found in heart, brain, liver, spleen, muscle and lung.
CC   -!- DOMAIN: Forms a beta-barrel structure that accommodates
CC       hydrophobic ligands in its interior (By similarity).
CC   -!- SIMILARITY: Belongs to the calycin superfamily. Fatty-acid binding
CC       protein (FABP) family.
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DR   EMBL; X70100; CAA49703.1; -; mRNA.
DR   EMBL; AJ223066; CAA11069.1; -; Genomic_DNA.
DR   EMBL; AF061015; AAC82368.1; -; Genomic_DNA.
DR   EMBL; AF061014; AAC82368.1; JOINED; Genomic_DNA.
DR   EMBL; AK008782; BAB25890.1; -; mRNA.
DR   EMBL; AK011551; BAB27692.1; -; mRNA.
DR   EMBL; BC002008; AAH02008.1; -; mRNA.
DR   IPI; IPI00114162; -.
DR   PIR; A47497; A47497.
DR   RefSeq; NP_034764.1; NM_010634.2.
DR   UniGene; Mm.741; -.
DR   ProteinModelPortal; Q05816; -.
DR   SMR; Q05816; 3-135.
DR   STRING; Q05816; -.
DR   PhosphoSite; Q05816; -.
DR   REPRODUCTION-2DPAGE; Q05816; -.
DR   UCD-2DPAGE; Q05816; -.
DR   PRIDE; Q05816; -.
DR   Ensembl; ENSMUST00000029046; ENSMUSP00000029046; ENSMUSG00000027533.
DR   GeneID; 16592; -.
DR   KEGG; mmu:16592; -.
DR   UCSC; uc008opg.1; mouse.
DR   CTD; 16592; -.
DR   MGI; MGI:101790; Fabp5.
DR   eggNOG; roNOG16756; -.
DR   HOGENOM; HBG714759; -.
DR   HOVERGEN; HBG005633; -.
DR   InParanoid; Q05816; -.
DR   OMA; GMAMRKM; -.
DR   OrthoDB; EOG4V1724; -.
DR   NextBio; 290145; -.
DR   ArrayExpress; Q05816; -.
DR   Bgee; Q05816; -.
DR   CleanEx; MM_FABP5; -.
DR   Genevestigator; Q05816; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IMP:MGI.
DR   GO; GO:0015758; P:glucose transport; IMP:MGI.
DR   GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IGI:MGI.
DR   InterPro; IPR012674; Calycin.
DR   InterPro; IPR011038; Calycin-like.
DR   InterPro; IPR000463; Fatty_acid-bd.
DR   InterPro; IPR000566; Lipocln_cytosolic_FA-bd.
DR   Gene3D; G3DSA:2.40.128.20; Calycin; 1.
DR   PANTHER; PTHR11955; Fatty_acid_bd; 1.
DR   Pfam; PF00061; Lipocalin; 1.
DR   PRINTS; PR00178; FATTYACIDBP.
DR   SUPFAM; SSF50814; Calycin; 1.
DR   PROSITE; PS00214; FABP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Disulfide bond;
KW   Lipid-binding; Phosphoprotein; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    135       Fatty acid-binding protein, epidermal.
FT                                /FTId=PRO_0000067378.
FT   REGION      129    131       Fatty acid binding (By similarity).
FT   BINDING     109    109       Fatty acid (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     131    131       Phosphotyrosine (By similarity).
FT   DISULFID    120    127       By similarity.
SQ   SEQUENCE   135 AA;  15137 MW;  6A6C8DBEBB046185 CRC64;
     MASLKDLEGK WRLMESHGFE EYMKELGVGL ALRKMAAMAK PDCIITCDGN NITVKTESTV
     KTTVFSCNLG EKFDETTADG RKTETVCTFQ DGALVQHQQW DGKESTITRK LKDGKMIVEC
     VMNNATCTRV YEKVQ
//
ID   FMN1_MOUSE              Reviewed;        1466 AA.
AC   Q05860; A2AFY9; A2AFZ0; Q05859;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Formin-1;
DE   AltName: Full=Limb deformity protein;
GN   Name=Fmn1; Synonyms=Fmn, Ld;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Kidney, and Testis;
RX   MEDLINE=90363291; PubMed=2392150; DOI=10.1038/346850a0;
RA   Woychik R.P., Maas R.L., Zeller R., Vogt T.F., Leder P.;
RT   "'Formins': proteins deduced from the alternative transcripts of the
RT   limb deformity gene.";
RL   Nature 346:850-853(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), AND ALTERNATIVE SPLICING.
RC   TISSUE=Embryo;
RX   MEDLINE=92112033; PubMed=1339380;
RA   Grusby-Jackson L., Kuo A., Leder P.;
RT   "A variant limb deformity transcript expressed in the embryonic mouse
RT   limb defines a novel formin.";
RL   Genes Dev. 6:29-37(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   PHOSPHORYLATION, AND ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4 AND 5).
RX   MEDLINE=93296176; PubMed=8516300; DOI=10.1073/pnas.90.12.5554;
RA   Vogt T.F., Jackson-Grusby L., Rush J., Leder P.;
RT   "Formins: phosphoprotein isoforms encoded by the mouse limb deformity
RT   locus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:5554-5558(1993).
RN   [5]
RP   ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4 AND 5).
RX   MEDLINE=97224459; PubMed=9119367; DOI=10.1006/geno.1996.4519;
RA   Wang C.C., Chan D.C., Leder P.;
RT   "The mouse formin (Fmn) gene: genomic structure, novel exons, and
RT   genetic mapping.";
RL   Genomics 39:303-311(1997).
RN   [6]
RP   FUNCTION.
RX   PubMed=15198975; DOI=10.1101/gad.299904;
RA   Zuniga A., Michos O., Spitz F., Haramis A.-P.G., Panman L., Galli A.,
RA   Vintersten K., Klasen C., Mansfield W., Kuc S., Duboule D., Dono R.,
RA   Zeller R.;
RT   "Mouse limb deformity mutations disrupt a global control region within
RT   the large regulatory landscape required for Gremlin expression.";
RL   Genes Dev. 18:1553-1564(2004).
RN   [7]
RP   ALTERNATIVE SPLICING (ISOFORMS 5 AND 6), FUNCTION, SUBCELLULAR
RP   LOCATION, INTERACTION WITH ALPHA-CATENIN, AND TISSUE SPECIFICITY.
RX   PubMed=14647292; DOI=10.1038/ncb1075;
RA   Kobielak A., Pasolli H.A., Fuchs E.;
RT   "Mammalian formin-1 participates in adherens junctions and
RT   polymerization of linear actin cables.";
RL   Nat. Cell Biol. 6:21-30(2004).
RN   [8]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH TUBULIN.
RX   PubMed=16480715; DOI=10.1016/j.yexcr.2005.12.035;
RA   Zhou F., Leder P., Martin S.S.;
RT   "Formin-1 protein associates with microtubules through a peptide
RT   domain encoded by exon-2.";
RL   Exp. Cell Res. 312:1119-1126(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Plays a role in the formation of adherens junction and
CC       the polymerization of linear actin cables.
CC   -!- SUBUNIT: Interacts with alpha-catenin and may interact with
CC       tubulin.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cell junction, adherens
CC       junction. Cell membrane; Peripheral membrane protein; Cytoplasmic
CC       side. Note=Localization to the adherens junctions is alpha-
CC       catenin-dependent. Also localizes to F-actin bundles originating
CC       from adherens junctions.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytoskeleton.
CC       Note=Isoform 2 localizes to microtubules.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1; Synonyms=IA;
CC         IsoId=Q05860-1; Sequence=Displayed;
CC       Name=2; Synonyms=IB;
CC         IsoId=Q05860-2; Sequence=VSP_027216;
CC       Name=3; Synonyms=II;
CC         IsoId=Q05860-3; Sequence=VSP_001570;
CC       Name=4; Synonyms=III;
CC         IsoId=Q05860-4; Sequence=VSP_001571, VSP_001572;
CC       Name=5; Synonyms=IV;
CC         IsoId=Q05860-5; Sequence=VSP_027214, VSP_027215, VSP_027216;
CC       Name=6; Synonyms=V;
CC         IsoId=Q05860-6; Sequence=VSP_029424, VSP_029425, VSP_027216;
CC   -!- TISSUE SPECIFICITY: It is present in the adult kidney, testis,
CC       limb, ovary, brain, small intestine, salivary gland and harderian
CC       gland. Isoforms 1, 2 and 5 are detected in skin and keratinocytes.
CC       Isoform 5 is found throughout the embryo.
CC   -!- DEVELOPMENTAL STAGE: It is present throughout the embryo. In the
CC       developing limb bud, the protein is expressed in the apical
CC       ectodermal ridge and the mesenchymal compartment, predominantly in
CC       the posterior region. During kidney morphogenesis, expression is
CC       initially restricted to the epithelial compartment of the
CC       pronephros and mesonephros. Isoform 5 is found in the apical
CC       ectodermal ridge and the mesenchymal compartment of the developing
CC       limb bud.
CC   -!- PTM: Phosphorylated on serine and possibly threonine residues.
CC   -!- MISCELLANEOUS: Was originally thought to play a role in limb bud
CC       development based on the fact that limb deformity (ld) mutants are
CC       associated with Fmn1 gene disruption. However PubMed:15198975
CC       shows that limb deformity mutations rather affects Grem1 cis-
CC       regulatory regions localized in Fmn1 gene and that loss of Grem1
CC       (gremlin-1) expression is the cause of limb malformations.
CC   -!- SIMILARITY: Belongs to the formin homology family. Cappuccino
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 FH1 (formin homology 1) domain.
CC   -!- SIMILARITY: Contains 1 FH2 (formin homology 2) domain.
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DR   EMBL; X53599; CAA37668.1; -; mRNA.
DR   EMBL; X62379; CAA44244.1; -; mRNA.
DR   EMBL; AL672253; CAM14988.1; -; Genomic_DNA.
DR   EMBL; AL691437; CAM14988.1; JOINED; Genomic_DNA.
DR   EMBL; AL672253; CAM14989.1; -; Genomic_DNA.
DR   EMBL; AL691437; CAM14989.1; JOINED; Genomic_DNA.
DR   EMBL; AL691466; CAM14989.1; JOINED; Genomic_DNA.
DR   EMBL; AL691466; CAM18143.1; -; Genomic_DNA.
DR   EMBL; AL672253; CAM18143.1; JOINED; Genomic_DNA.
DR   EMBL; AL691437; CAM18143.1; JOINED; Genomic_DNA.
DR   EMBL; AL691437; CAM18583.1; -; Genomic_DNA.
DR   EMBL; AL672253; CAM18583.1; JOINED; Genomic_DNA.
DR   EMBL; AL691437; CAM18585.1; -; Genomic_DNA.
DR   EMBL; AL672253; CAM18585.1; JOINED; Genomic_DNA.
DR   EMBL; AL691466; CAM18585.1; JOINED; Genomic_DNA.
DR   IPI; IPI00114260; -.
DR   IPI; IPI00229709; -.
DR   IPI; IPI00229710; -.
DR   IPI; IPI00828355; -.
DR   IPI; IPI00828872; -.
DR   IPI; IPI00874986; -.
DR   PIR; S11515; S11515.
DR   PIR; S24407; S24407.
DR   RefSeq; NP_001036787.1; NM_001043322.1.
DR   RefSeq; NP_034360.2; NM_010230.2.
DR   UniGene; Mm.4938; -.
DR   PDB; 2JUP; NMR; -; P=881-888.
DR   PDB; 2RLY; NMR; -; P=874-881.
DR   PDB; 2RM0; NMR; -; P=880-888.
DR   PDBsum; 2JUP; -.
DR   PDBsum; 2RLY; -.
DR   PDBsum; 2RM0; -.
DR   ProteinModelPortal; Q05860; -.
DR   SMR; Q05860; 1057-1415.
DR   DIP; DIP-646N; -.
DR   STRING; Q05860; -.
DR   PhosphoSite; Q05860; -.
DR   PRIDE; Q05860; -.
DR   Ensembl; ENSMUST00000081349; ENSMUSP00000080093; ENSMUSG00000044042.
DR   Ensembl; ENSMUST00000099576; ENSMUSP00000097171; ENSMUSG00000044042.
DR   Ensembl; ENSMUST00000102547; ENSMUSP00000099606; ENSMUSG00000044042.
DR   Ensembl; ENSMUST00000110953; ENSMUSP00000106578; ENSMUSG00000044042.
DR   Ensembl; ENSMUST00000110955; ENSMUSP00000106580; ENSMUSG00000044042.
DR   GeneID; 14260; -.
DR   KEGG; mmu:14260; -.
DR   UCSC; uc008lpk.1; mouse.
DR   UCSC; uc008lpl.1; mouse.
DR   UCSC; uc008lpm.1; mouse.
DR   CTD; 14260; -.
DR   MGI; MGI:101815; Fmn1.
DR   GeneTree; ENSGT00560000076948; -.
DR   HOGENOM; HBG505628; -.
DR   HOVERGEN; HBG107922; -.
DR   InParanoid; Q05860; -.
DR   OMA; YENRAQK; -.
DR   OrthoDB; EOG4KWJSD; -.
DR   NextBio; 285597; -.
DR   ArrayExpress; Q05860; -.
DR   Bgee; Q05860; -.
DR   CleanEx; MM_FMN1; -.
DR   Genevestigator; Q05860; -.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR   GO; GO:0005912; C:adherens junction; IPI:MGI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0017124; F:SH3 domain binding; IPI:MGI.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0035136; P:forelimb morphogenesis; IMP:MGI.
DR   GO; GO:0010467; P:gene expression; IMP:MGI.
DR   GO; GO:0035137; P:hindlimb morphogenesis; IMP:MGI.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:MGI.
DR   GO; GO:0051127; P:positive regulation of actin nucleation; IDA:MGI.
DR   GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR   InterPro; IPR003104; Actin-bd_FH2/DRF_autoreg.
DR   InterPro; IPR015425; FH2_actin-bd.
DR   InterPro; IPR001265; Formin.
DR   Pfam; PF02181; FH2; 1.
DR   PRINTS; PR00828; FORMIN.
DR   SMART; SM00498; FH2; 1.
DR   SUPFAM; SSF101447; FH2_actin_bd; 1.
DR   PROSITE; PS51444; FH2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Alternative splicing; Cell junction;
KW   Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton; Membrane;
KW   Nucleus; Phosphoprotein.
FT   CHAIN         1   1466       Formin-1.
FT                                /FTId=PRO_0000194886.
FT   DOMAIN      870    970       FH1.
FT   DOMAIN      983   1435       FH2.
FT   REGION        1    624       Microtubule-binding.
FT   REGION      458    842       Mediates interaction with alpha-catenin.
FT   COILED      722    786       Potential.
FT   COMPBIAS    870    995       Pro-rich.
FT   MOD_RES     234    234       Phosphoserine.
FT   MOD_RES     520    520       Phosphoserine (By similarity).
FT   MOD_RES     524    524       Phosphoserine (By similarity).
FT   VAR_SEQ       1    682       Missing (in isoform 5).
FT                                /FTId=VSP_027214.
FT   VAR_SEQ       1    623       Missing (in isoform 6).
FT                                /FTId=VSP_029424.
FT   VAR_SEQ     624    624       P -> MVTTGSPPFNTMGACYRYNPRYGQPISVPKVWKCRH
FT                                RRSVTPDE (in isoform 6).
FT                                /FTId=VSP_029425.
FT   VAR_SEQ     625    722       Missing (in isoform 3).
FT                                /FTId=VSP_001570.
FT   VAR_SEQ     626    627       IA -> SV (in isoform 4).
FT                                /FTId=VSP_001571.
FT   VAR_SEQ     628   1466       Missing (in isoform 4).
FT                                /FTId=VSP_001572.
FT   VAR_SEQ     683    683       N -> MEEVGNSLSSRDVLEPDKSEAGLEMAQSILSKFSMK
FT                                SLFGFTNKLDSLEPEEEDAVLKAFRSLEGDPAPERGDPSKG
FT                                SDQPQAEAPVPPDLKNDGKSARAETGSEGSQGKGRSNTSSP
FT                                GYELSPATVSVDNEEVIWVRGTLVHTTSDSDSEDGDQEAEE
FT                                ESSLDTQKPTTVVLCEPSQEPKDRAGDSEENTDTGNTDDTE
FT                                LCAEESQRTLPETSSKLELGGDGSHPAEHSPRQDQAAEEGS
FT                                QIPPAATDQTVGALASTVSKREAPEEKPFQLPAFFSGLRVL
FT                                KKGATAEAGETITEIKPKDGDLALLKLTQRVQKSLGQGGPQ
FT                                TVKSPGRATDPKATPTLLEQLSQLLNIDMPRTEQKEADPEF
FT                                HGADEMGYSTDQESHKSPRDAHVQGGQVKARTPETALEAFK
FT                                ALFIRPPKKGSTADTSELEALKRKMKHEKESLRAVFERSKS
FT                                RPADSPSDPKS (in isoform 5).
FT                                /FTId=VSP_027215.
FT   VAR_SEQ    1250   1285       Missing (in isoform 2, isoform 5 and
FT                                isoform 6).
FT                                /FTId=VSP_027216.
FT   CONFLICT    220    220       V -> A (in Ref. 1; CAA37668).
FT   CONFLICT    776    776       G -> E (in Ref. 1; CAA37668 and 2;
FT                                CAA44244).
FT   CONFLICT    866    866       H -> Q (in Ref. 1; CAA37668 and 2;
FT                                CAA44244).
FT   CONFLICT    950    950       G -> GPP (in Ref. 1; CAA37668 and 2;
FT                                CAA44244).
SQ   SEQUENCE   1466 AA;  163581 MW;  5482F8AAB66CBF32 CRC64;
     MEGTHCTLQL HNPIAELCYI SFYLPKGEVR GFSYKGTVTL DRSNNAFHNC YQVREGPDIT
     SLSQQPNEHP GDIFFKQTPT KNILTELYKL TAEKERLLDS LLRSDNILGV SMGSQEGKLQ
     ELSVILATGD EYFQSAGNWR RELPVSSLIR RSTQENKKPR RSGRRRESPE ELRQKRTRRK
     GRGCQESAFQ MGKDQVCSSS SLSFRARPNL RLLEERGNLV PRGTLTSSLR RRESCPANIL
     RTPDADLAFG NSGRTSEDTD LEGPLSPDSS PTEVGDADVG GQLKSSHQQE PPQPNVSESH
     GKHAGAERWS SRTRKSKSLE RTCSKKPVSK VVAKIQEPSA PVKRIVRAHH DGKGRVAYGP
     ETQTEFIPKA DFLTLPGGET ETHSSGRLEE EQPGIKSLRS SAPERASITK EPASTEAAVN
     KVLRKVIESE KLDEATEGKR LGFSLNTRAT HTFPETRSQR KAGLPQSGHK FLLLDLPHTV
     GPDSPQPKCD EKKPTPQVPT ALGMVFNNSS PQSSAHKRLS PVPSPLSPRC PSPQQHHRIL
     LLPPLPSEGE VVFNEYPSRK NDVSSGFPSA DTLEPSSTTK VTETKGASPT SLRASQTWLV
     SEEASEKGLG PEKITAPPQH QLPPGIASEG FPCDNFKEQT AKDLPNKDGG VWVPGYRAGP
     PCPFLLHEEK EKTSRSELYL DLNPDQSPTE QDDRTPGRLQ AVWPPPKTKD TEEKVGLKYT
     EAEYQAAILH LKREHKEEIE TLQAQFELKT FHIRGEHALV TARLEEAIEN LKQQLGKRRE
     GCEEMRDVCI STDDDCSPKA FRNVCIQTDR ETFLKPCDAE SKATRSSQIV PKKLTISLTQ
     LSPSKDSKDI HAPFQTREGT SSSSQHKISP PAPPTPPPLP PPLIPPPPPL PPGLGPLPPA
     PPIPPVCPVS PPPPPPPPPP TPVPPSDGPP PPPPPPPPLP NVLALPNSGG PPPPPPPPPP
     GLAPPPPPGL SFGLSSSSSQ YPRKPAIEPS CPMKPLYWTR IQINDKSQDA APTLWDSLEE
     PHIRDTSEFE YLFSKDTTQQ KKKPLSEAYE KKNKVKKIIK LLDGKRSQTV GILISSLHLE
     MKDIQQAIFT VDDSVVDLET LAALYENRAQ EDELTKIRKY YETSKEEDLK LLDKPEQFLH
     ELAQIPNFAE RAQCIIFRAV FSEGITSLHR KVEIVTRASK GLLHMKSVKD ILALILAFGN
     YMNGGNRTRG QADGYSLEIL PKLKDVKSRD NGMNLVDYVV KYYLRYYDQC KHHDQEASCR
     GKDLFSLYFH IAVHPQRKSG LELKQEAGTD KSVFPLPEPQ DFFLASQVKF EDLLKDLRKL
     KRQLEASEQQ MKLVCKESPR EYLQPFKDKL EEFFKKAKKE HKMEESHLEN AQKSFETTVG
     YFGMKPKTGE KEVTPSYVFM VWFEFCSDFK TIWKRESKNI SKERLKMAQA SVSKLTSEKK
     VETKKINPTA SLKERLRQKE ASVATN
//
ID   PTPRG_MOUSE             Reviewed;        1442 AA.
AC   Q05909;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   08-MAR-2011, entry version 101.
DE   RecName: Full=Receptor-type tyrosine-protein phosphatase gamma;
DE            Short=Protein-tyrosine phosphatase gamma;
DE            Short=R-PTP-gamma;
DE            EC=3.1.3.48;
DE   Flags: Precursor;
GN   Name=Ptprg;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=93180796; PubMed=8382771;
RA   Barnea G., Silvennoinen O., Shaanan B., Honegger A.M., Canoll P.D.,
RA   D'Eustachio P., Morse B., Levy J.B., Laforgia S., Huebner K.,
RA   Musacchio J.M., Sap J., Schlessinger J.;
RT   "Identification of a carbonic anhydrase-like domain in the
RT   extracellular region of RPTP gamma defines a new subfamily of receptor
RT   tyrosine phosphatases.";
RL   Mol. Cell. Biol. 13:1497-1506(1993).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-115, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: Possesses tyrosine phosphatase activity (By similarity).
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Probable).
CC   -!- TISSUE SPECIFICITY: Detected in brain, lung, kidney, heart, liver,
CC       skeletal muscle, spleen and testes. It is developmentally
CC       regulated in the brain.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 5 subfamily.
CC   -!- SIMILARITY: Contains 1 alpha-carbonic anhydrase domain.
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC   -!- SIMILARITY: Contains 2 tyrosine-protein phosphatase domains.
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DR   EMBL; L09562; AAA40022.1; -; mRNA.
DR   IPI; IPI00114671; -.
DR   PIR; B48148; B48148.
DR   RefSeq; NP_033007.2; NM_008981.3.
DR   UniGene; Mm.431266; -.
DR   PDB; 3JXG; X-ray; 1.70 A; A/B/C/D=55-320.
DR   PDB; 3KLD; X-ray; 2.00 A; B=55-320.
DR   PDBsum; 3JXG; -.
DR   PDBsum; 3KLD; -.
DR   ProteinModelPortal; Q05909; -.
DR   SMR; Q05909; 57-320, 346-437, 823-1409.
DR   STRING; Q05909; -.
DR   PhosphoSite; Q05909; -.
DR   PRIDE; Q05909; -.
DR   Ensembl; ENSMUST00000022264; ENSMUSP00000022264; ENSMUSG00000021745.
DR   GeneID; 19270; -.
DR   KEGG; mmu:19270; -.
DR   UCSC; uc007sfm.1; mouse.
DR   CTD; 19270; -.
DR   MGI; MGI:97814; Ptprg.
DR   eggNOG; roNOG04461; -.
DR   GeneTree; ENSGT00600000084078; -.
DR   HOGENOM; HBG446367; -.
DR   HOVERGEN; HBG053760; -.
DR   InParanoid; Q05909; -.
DR   OrthoDB; EOG4FN4GW; -.
DR   PhylomeDB; Q05909; -.
DR   BRENDA; 3.1.3.48; 244.
DR   NextBio; 296154; -.
DR   ArrayExpress; Q05909; -.
DR   Bgee; Q05909; -.
DR   CleanEx; MM_PTPRG; -.
DR   Genevestigator; Q05909; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   InterPro; IPR001148; Carbonic_anhydrase_a-class_cat.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Gene3D; G3DSA:3.10.200.10; Euk_COanhd; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00194; PTPc; 2.
DR   SUPFAM; SSF51069; Euk_COanhd; 1.
DR   SUPFAM; SSF49265; FN_III-like; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Glycoprotein; Hydrolase; Membrane; Phosphoprotein;
KW   Protein phosphatase; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     19       By similarity.
FT   CHAIN        20   1442       Receptor-type tyrosine-protein
FT                                phosphatase gamma.
FT                                /FTId=PRO_0000025442.
FT   TOPO_DOM     20    733       Extracellular (Potential).
FT   TRANSMEM    734    759       Helical; (Potential).
FT   TOPO_DOM    760   1442       Cytoplasmic (Potential).
FT   DOMAIN       58    321       Alpha-carbonic anhydrase.
FT   DOMAIN      346    443       Fibronectin type-III.
FT   DOMAIN      845   1116       Tyrosine-protein phosphatase 1.
FT   DOMAIN     1147   1407       Tyrosine-protein phosphatase 2.
FT   REGION     1057   1063       Substrate binding (By similarity).
FT   ACT_SITE   1057   1057       Phosphocysteine intermediate (By
FT                                similarity).
FT   BINDING    1025   1025       Substrate (By similarity).
FT   BINDING    1101   1101       Substrate (By similarity).
FT   SITE       1348   1348       Ancestral active site.
FT   MOD_RES     115    115       Phosphothreonine.
FT   MOD_RES    1432   1432       Phosphoserine (By similarity).
FT   CARBOHYD    109    109       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    113    113       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    156    156       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    359    359       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    444    444       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    719    719       N-linked (GlcNAc...) (Potential).
FT   HELIX        71     73
FT   HELIX        90     92
FT   STRAND      103    105
FT   STRAND      116    119
FT   STRAND      124    127
FT   STRAND      133    135
FT   STRAND      143    151
FT   STRAND      163    165
FT   STRAND      171    179
FT   TURN        181    183
FT   HELIX       187    192
FT   STRAND      199    206
FT   HELIX       212    214
FT   HELIX       215    218
FT   STRAND      230    232
FT   HELIX       238    241
FT   STRAND      249    252
FT   STRAND      265    272
FT   STRAND      274    276
FT   HELIX       278    285
FT   STRAND      288    290
FT   STRAND      299    301
SQ   SEQUENCE   1442 AA;  161243 MW;  5887715568FBECD8 CRC64;
     MRRLLEPCWW ILFLKITSSV LHYVVCFPAL TEGYVGTLQE SRQDSSVQIR RRKASGDPYW
     AYSGAYGPEH WVTSSVSCGG SHQSPIDILD HHARVGDEYQ ELQLDGFDNE SSNKTWMKNT
     GKTVAILLKD DYFVSGAGLP GRFKAEKVEF HWGHSNGSAG SEHSVNGRRF PVEMQIFFYN
     PDDFDSFQTA ISENRIIGAM AIFFQVSPRD NSALDPIIHG LKGVVHHEKE TFLDPFILRD
     LLPASLGSYY RYTGSLTTPP CSEIVEWIVF RRPVPISYHQ LEAFYSIFTT EQQDHVKSVE
     YLRNNFRPQQ ALNDRVVSKS AVRDAWNHDL ADFLDNPLGT EASKVCSSPP IHMKVQPLNQ
     TALQVSWSQP ETIYHPPIMN YMISYSWTKN EDEKEKTFTK DSDKDLKATI SHVSPDSLYL
     FRVQAVCRND MRSDFSQTML FQANTTRIFQ GTRIVKTGVP TASPASSADM APISSGSSTW
     TSSGIPFSFV SMATGMGPSS SGSQATVASV VTSTLLAGLG FGGGGISSFP STVWPTRLPT
     ASAASKQAGR TVLATTEALA SPGPDVHSAP SKDSEGTEEG EKEEKSESED GEREHEEEEK
     DSEKKEKSEA THTAAESDRT APAPTPSSPH RTAAEGGHQT IPGRRQDHSA PATDQPGHVA
     PDLDPLVDTA TQVPPTATEE HYSGSDPRRP EMPSKKPMSR GDRFSEDSKF ITVNPAEKNT
     SGMLSRPSPG RMEWIIPLIV VSALTFVCLV LLIAVLVYWR GCNKIKSKGF PRRSREVPSS
     GERGEKGSRK CFQTAHFYVE DSSSPRVVPN ESVPIIPIPD DMEAIPVKQF GKHIGELYSN
     SQHGFSEDFE EVQRCTADMN ITAEHSNHPD NKHKNRYINI LAYDHSRVKL RPLPGKDSKH
     SDYINANYVD GYNKAKAYIA TQGPLKSTFE DFWRMIWEQN TGIIIMITNL VEKGRRKCDQ
     YWPTENTEEY GNIIVTLKST KVHACYTVRR LSVRNTKVKK GQKGNPKGRQ NERTVIQYHY
     TQWPDMGVPE YALPVLTFVR RSSAARMPDM GPVLVHCSAG VGRTGTYIVI DSMLQQIKDK
     STVNVLGFLK HIRTQRNYLV QTEEQYIFIH DALLEAILGK ETAVSSSQLH SYVNSILIPG
     VGGKTRLEKQ FKLITQCNAK YVECFSAQKE CNKEKNRNSS VVPAERARVG LAPLPGMKGT
     DYINASYIMG YYRSNEFIIT QHPLPHTTKD FWRMIWDHNA QIIVMLPDNQ SLAEDEFVYW
     PSREESMNCE AFTVTLISKD RLCLSNEEQI IIHDFILEAT QDDYVLEVRH FQCPKWPNPD
     APISSTFELI NVIKEEALTR DGPTIVHDEY GAVSAGMLCA LTTLSQQLEN ENAVDVFQVA
     KMINLMRPGV FTDIEQYQFV YKAMLSLIST KENGNGPMTG DKNGAVLTAE ESDPAESMES
     LV
//
ID   Q059Q1_MOUSE            Unreviewed;      1489 AA.
AC   Q059Q1;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   11-JAN-2011, entry version 42.
DE   SubName: Full=MCG18052, isoform CRA_b;
DE   SubName: Full=WD repeat domain 7;
GN   Name=Wdr7; ORFNames=mCG_18052;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC125573; AAI25574.1; -; mRNA.
DR   EMBL; BC137785; AAI37786.1; -; mRNA.
DR   EMBL; CH466528; EDL09715.1; -; Genomic_DNA.
DR   IPI; IPI00380997; -.
DR   RefSeq; NP_001014981.1; NM_001014981.1.
DR   UniGene; Mm.480708; -.
DR   ProteinModelPortal; Q059Q1; -.
DR   PRIDE; Q059Q1; -.
DR   Ensembl; ENSMUST00000072726; ENSMUSP00000072509; ENSMUSG00000040560.
DR   GeneID; 104082; -.
DR   KEGG; mmu:104082; -.
DR   UCSC; uc008fea.1; mouse.
DR   CTD; 104082; -.
DR   MGI; MGI:1860197; Wdr7.
DR   eggNOG; roNOG07420; -.
DR   HOVERGEN; HBG067501; -.
DR   InParanoid; Q059Q1; -.
DR   OMA; PENCSAR; -.
DR   PhylomeDB; Q059Q1; -.
DR   NextBio; 356481; -.
DR   ArrayExpress; Q059Q1; -.
DR   Bgee; Q059Q1; -.
DR   Genevestigator; Q059Q1; -.
DR   InterPro; IPR011047; Quino_AlcDH-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 5.
DR   Pfam; PF00400; WD40; 5.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50998; Quin_alc_DH_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 3.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE   2: Evidence at transcript level;
KW   Repeat; WD repeat.
SQ   SEQUENCE   1489 AA;  163450 MW;  444A5509758C9E63 CRC64;
     MAGNSLVLPI VLWGRKAPTH CISSILLTDD GGTIVTGCHD GQICLWDVSV ELEVNPRALL
     FGHTASITCL SKACASGDKR YTVSASANGE MCLWDVNDGR CIEFTKLACT HTGIQFYQFS
     VGNQQEGRLL CHGHYPEILV VDATSLEVLY SLVSKISPDW ISSMSIIRSQ RTQEDTVVAL
     SVTGILKVWI VTSEMSGMQD TEPIFEEESK PIYCQNCQSI SFCAFTQRSL LVVCSKYWRV
     FDAGDYSLLC SGPSENGQTW TGGDFVSADK VIIWTENGQS YIYKLPASCL PASDSFRSDV
     GKAVENLIPP VQHSLLDQKD KELVICPPVT RFFYGCKEYL HKLLIQGDSS GRLNIWNIAD
     IAEKQEADEG LKMTTCISLQ EAFDKLKPCP AGIIDQLSVI PNSNEPLKVT ASVYIPAHGR
     LVCGREDGSI IIVPATQTAI VQLLQGEHML RRGWPPHRTL RGHRNKVTCL LYPHQVSARY
     DQRYLISGGV DFSVIIWDIF SGEMKHIFCV HGGEITQLLV PPENCSARVQ HCICSVASDH
     SVGLLSLREK KCIMLASRHL FPIQVIKWRP SDDYLVVGCT DGSVYVWQMD TGALDRCAMG
     ITAVEILNAC DEAVPAAVDS LSHPAVNLKQ AMTRRSLAAL KNMAHHKLQT LATNLLASEA
     SDKGNLPKYS HNSLMVQAIK TNLTDPDIHV LFFDVEALII QLLTEEASRP NTALISPENL
     QKASGSSDKG GSFLTGKRAA VLFQQVKETI KENIKEHLLD EEEDEEEARR QSREDSDPEY
     RASKSKPLTL LEYNLTMDTA KLFMSCLHAW GLNEVLDEVC LDRLGMLKPH CTVSFGLLSR
     GGHMSLMLPG YNQAAGKLLH AKAEVGRKLP AAEGVGKGTY TVSRAVTTQH LLSIISLANT
     LMSMTNATFI GDHMKKGPTR PPRPGTPDLS KARDSPPPSS NIVQGQIKQA AAPVVSARSD
     ADHSGSDSAS PALPTCFLVN EGWSQLAAMH CVMLPDLLGL ERFRPPLLEM LARRWQDRCL
     EVREAAQALL LAELRRIEQA GRKETIDTWA PYLPQYMDHV ISPGVTAEAM QTMAAAPDAS
     GPEAKVQEEE HDLVDDDITA GCLSSVPQMK KISTSYEERR KQATAIVLLG VIGAEFGAEI
     EPPKLLTRPR SSSQIPEGFG LTSGGSNYSL ARHTCKALTY LLLQPPSPKL PPHSTIRRTA
     TDLIGRGFTV WEPYMDVSAV LMGLLELCAD AEKQLANITM GLPLSPAADS ARSARHALSL
     IATARPPAFI TTIAKEVHRH TALAANTQSQ QSIHTTTLAR AKGEILRVIE ILIEKMPTDV
     VDLLVEVMDI IMYCLEGSLV KKKGLQECFP AICRFYMVSY YERSHRIAVG ARHGSVALYD
     IRTGKCQTIH GHKGPITAVS FAPDGRYLAT YSNTDSHISF WQMNTSLLGS IGMLNSAPQL
     RCIKTYQVPP VQPASPGSHN ALKLARLIWT SNRNVILMAH DGKEHRFMV
//
ID   DNAL1_MOUSE             Reviewed;         190 AA.
AC   Q05A62; A0JLX1; Q9DAH9;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   08-MAR-2011, entry version 35.
DE   RecName: Full=Dynein light chain 1, axonemal;
GN   Name=Dnal1; Synonyms=Dnalc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION, AND TISSUE SPECIFICITY.
RX   PubMed=15845866; DOI=10.1165/rcmb.2004-0335OC;
RA   Horvath J., Fliegauf M., Olbrich H., Kispert A., King S.M.,
RA   Mitchison H., Zariwala M.A., Knowles M.R., Sudbrak R., Fekete G.,
RA   Neesen J., Reinhardt R., Omran H.;
RT   "Identification and analysis of axonemal dynein light chain 1 in
RT   primary ciliary dyskinesia patients.";
RL   Am. J. Respir. Cell Mol. Biol. 33:41-47(2005).
CC   -!- SUBUNIT: Interacts with DNAH5 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q05A62-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q05A62-2; Sequence=VSP_023984, VSP_023983;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q05A62-3; Sequence=VSP_023985;
CC   -!- TISSUE SPECIFICITY: Expressed in the respiratory epithelium of the
CC       upper airways and the ependymal cells lining the brain ventricles.
CC   -!- SIMILARITY: Belongs to the dynein light chain LC1-type family.
CC   -!- SIMILARITY: Contains 4 LRR (leucine-rich) repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI25395.2; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK005826; BAB24259.1; -; mRNA.
DR   EMBL; BC125392; AAI25393.1; -; mRNA.
DR   EMBL; BC125394; AAI25395.2; ALT_INIT; mRNA.
DR   EMBL; BG916281; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00118650; -.
DR   IPI; IPI00830422; -.
DR   IPI; IPI00831436; -.
DR   RefSeq; NP_083097.2; NM_028821.3.
DR   UniGene; Mm.101525; -.
DR   ProteinModelPortal; Q05A62; -.
DR   SMR; Q05A62; 1-189.
DR   STRING; Q05A62; -.
DR   PhosphoSite; Q05A62; -.
DR   PRIDE; Q05A62; -.
DR   Ensembl; ENSMUST00000046340; ENSMUSP00000037076; ENSMUSG00000042523.
DR   Ensembl; ENSMUST00000110295; ENSMUSP00000105924; ENSMUSG00000042523.
DR   GeneID; 105000; -.
DR   KEGG; mmu:105000; -.
DR   CTD; 105000; -.
DR   MGI; MGI:1921462; Dnalc1.
DR   eggNOG; roNOG15762; -.
DR   GeneTree; ENSGT00390000016904; -.
DR   HOGENOM; HBG522528; -.
DR   HOVERGEN; HBG081457; -.
DR   InParanoid; Q05A62; -.
DR   OrthoDB; EOG47PX70; -.
DR   NextBio; 357394; -.
DR   ArrayExpress; Q05A62; -.
DR   Bgee; Q05A62; -.
DR   CleanEx; MM_DNALC1; -.
DR   Genevestigator; Q05A62; -.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   Pfam; PF00560; LRR_1; 1.
DR   PROSITE; PS51450; LRR; 4.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Leucine-rich repeat; Repeat.
FT   CHAIN         1    190       Dynein light chain 1, axonemal.
FT                                /FTId=PRO_0000281131.
FT   REPEAT       33     55       LRR 1.
FT   REPEAT       56     79       LRR 2.
FT   REPEAT       81    100       LRR 3.
FT   REPEAT      101    124       LRR 4.
FT   VAR_SEQ       1     39       Missing (in isoform 3).
FT                                /FTId=VSP_023985.
FT   VAR_SEQ       1     14       Missing (in isoform 2).
FT                                /FTId=VSP_023984.
FT   VAR_SEQ      15     15       E -> M (in isoform 2).
FT                                /FTId=VSP_023983.
FT   CONFLICT    147    147       F -> L (in Ref. 1; BAB24259).
SQ   SEQUENCE   190 AA;  21465 MW;  7052EB49CDCE4A0B CRC64;
     MAKATTIKEA LSRWEEKTGQ KPSDAKEIKL YAQIPPIEKM DASLSTLGNC EKLSLSTNCI
     EKIANLNGLK NLRILSLGRN NIKNLNGLEA VGETLEELWI SYNFIEKLKG IHVMKKLKIL
     YMSNNLVKDW AEFLKLAELP CLEDLVFVGN PLEEKHSAEG NWIDEATKRV PKLKKLDGTP
     VIKEDEEEES
//
ID   DRP2_MOUSE              Reviewed;         957 AA.
AC   Q05AA6; Q61095; Q8C4R1;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   RecName: Full=Dystrophin-related protein 2;
DE            Short=DRP-2;
GN   Name=Drp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 391-862.
RX   MEDLINE=96225452; PubMed=8640231; DOI=10.1038/ng0696-223;
RA   Roberts R.G., Freeman T.C., Kendall E., Vetrie D.L.P., Dixon A.K.,
RA   Shaw-Smith C., Bone Q., Bobrow M.;
RT   "Characterization of DRP2, a novel human dystrophin homologue.";
RL   Nat. Genet. 13:223-226(1996).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-910, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Possibly involved in membrane-cytoskeleton interactions
CC       of the central nervous system (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (Probable).
CC   -!- SIMILARITY: Contains 2 spectrin repeats.
CC   -!- SIMILARITY: Contains 1 WW domain.
CC   -!- SIMILARITY: Contains 1 ZZ-type zinc finger.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK081426; BAC38217.1; -; mRNA.
DR   EMBL; AL672064; CAM27314.1; -; Genomic_DNA.
DR   EMBL; BC125345; AAI25346.1; -; mRNA.
DR   EMBL; BC125347; AAI25348.1; -; mRNA.
DR   EMBL; U43520; AAC52607.1; -; mRNA.
DR   IPI; IPI00830746; -.
DR   RefSeq; NP_034208.2; NM_010078.3.
DR   UniGene; Mm.121662; -.
DR   UniGene; Mm.477164; -.
DR   ProteinModelPortal; Q05AA6; -.
DR   SMR; Q05AA6; 344-659.
DR   STRING; Q05AA6; -.
DR   PRIDE; Q05AA6; -.
DR   Ensembl; ENSMUST00000113226; ENSMUSP00000108852; ENSMUSG00000000223.
DR   Ensembl; ENSMUST00000113228; ENSMUSP00000108854; ENSMUSG00000000223.
DR   GeneID; 13497; -.
DR   KEGG; mmu:13497; -.
DR   NMPDR; fig|10090.3.peg.22123; -.
DR   UCSC; uc009uga.1; mouse.
DR   CTD; 13497; -.
DR   MGI; MGI:107432; Drp2.
DR   HOVERGEN; HBG053790; -.
DR   PhylomeDB; Q05AA6; -.
DR   NextBio; 284029; -.
DR   ArrayExpress; Q05AA6; -.
DR   Bgee; Q05AA6; -.
DR   Genevestigator; Q05AA6; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR017433; Dystrophin-related_2.
DR   InterPro; IPR015153; EF-hand_dom_typ1.
DR   InterPro; IPR015154; EF-hand_dom_typ2.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   InterPro; IPR000433; Znf_ZZ.
DR   Pfam; PF09068; efhand_1; 1.
DR   Pfam; PF09069; efhand_2; 1.
DR   Pfam; PF00435; Spectrin; 1.
DR   Pfam; PF00397; WW; 1.
DR   Pfam; PF00569; ZZ; 1.
DR   PIRSF; PIRSF038205; Dystrophin-related_p2; 1.
DR   SMART; SM00150; SPEC; 2.
DR   SMART; SM00456; WW; 1.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF51045; WW_Rsp5_WWP; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Metal-binding; Phosphoprotein; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    957       Dystrophin-related protein 2.
FT                                /FTId=PRO_0000345015.
FT   REPEAT      102    179       Spectrin 1.
FT   REPEAT      231    337       Spectrin 2.
FT   DOMAIN      358    383       WW.
FT   ZN_FING     604    651       ZZ-type.
FT   MOD_RES     910    910       Phosphothreonine.
FT   CONFLICT    362    362       I -> F (in Ref. 1; BAC38217).
FT   CONFLICT    598    598       V -> VLHRV (in Ref. 4; AAC52607).
SQ   SEQUENCE   957 AA;  108050 MW;  B8F759D964118315 CRC64;
     MQPLVMQGCP YTLPRCHEWH AADRFHHSSS LRNTCPQPQV RAAVTIPAPP WDGAGDPCLS
     PKLLNGTVGA TGPLEPSAMN LCWNEIKKKS HNLRARLEAF SDLSGKLQLP LREIIDWLSQ
     KDEELSAQLP LQGDVALVQQ EKETHAAFME EVKSKGPYIS SVLESAQAFL SQHPFEELEE
     SQSESKDTSP RQRIQNLSRF VWKQATVASE LWEKLTARCV DQHRHIEHTL EHLLEIQGAM
     EELSSTLTQA EGVRATWEPI GDLFIDSLPE HIQAIKLFKE EFSPVKDGVK LVNDLAHQLA
     ISDVHLSMEN SRALEQINIR WKQLQVSVAE RLKQLQDAHR DFGPGSQHFL STSVQVPWER
     AISPNKVPYY INHQAQTTCW DHPKMTELYQ TLADLNNIKF SAYRTAMKLR RVQKALRLDL
     VTLTTALEIF NEHDLQASEH VMDVVEVIHC LTALYERLEE ERGILVNVPL CVDMSLNWLL
     NVFDSGRSGK MRALSFKTGI ACLCGTEVKE KLQYLFSQVA NSGSQCDQRH LGALLHEAIQ
     VPRQLGEVAA FGGSNVEPSV RSCFRFSTGK PVIEASQFLE WVNLEPQSMV WLAVLHRVTI
     AEQVKHQTKC SICRQCPIKG FRYRSLKQFN VDICQTCFLT GRASKGNKLH YPIMEYYTPT
     TSSENMRDFA TTLKNKFRSK QYFSKHPQRG YLPVQSVLES DCSETPASSP MLPHADTHSR
     IEHFASRLAE MESQNCSFFN DSLSPDDSID EDQYLLRHSS PITDREPAFG QQAPCSMATE
     SKGELEKILA HLEDENRILQ GELRRLKWQH EEAAEAPTLV EGSAEATPDH RNEELLAEAR
     ILRQHKSRLE TRMQILEDHN KQLESQLQRL RELLLQPPSE SDGNGSAGSS LASSPRQSEG
     SHPREKGQTT PDTEVADDVG SKSQDVSLCL EDIMEKLRHA FPSVRSSDVT ANTLLAS
//
ID   Q05BE2_MOUSE            Unreviewed;       444 AA.
AC   Q05BE2;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   08-FEB-2011, entry version 30.
DE   SubName: Full=Syt6 protein;
GN   Name=Syt6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 2 C2 domains.
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DR   EMBL; BC050760; AAH50760.1; -; mRNA.
DR   IPI; IPI00972901; -.
DR   UniGene; Mm.88818; -.
DR   ProteinModelPortal; Q05BE2; -.
DR   SMR; Q05BE2; 146-416.
DR   STRING; Q05BE2; -.
DR   Ensembl; ENSMUST00000090697; ENSMUSP00000088196; ENSMUSG00000027849.
DR   Ensembl; ENSMUST00000117221; ENSMUSP00000113373; ENSMUSG00000027849.
DR   Ensembl; ENSMUST00000118117; ENSMUSP00000112486; ENSMUSG00000027849.
DR   Ensembl; ENSMUST00000121834; ENSMUSP00000112997; ENSMUSG00000027849.
DR   UCSC; uc008qta.1; mouse.
DR   MGI; MGI:1859544; Syt6.
DR   eggNOG; roNOG14177; -.
DR   HOVERGEN; HBG005010; -.
DR   InParanoid; Q05BE2; -.
DR   ArrayExpress; Q05BE2; -.
DR   Bgee; Q05BE2; -.
DR   Genevestigator; Q05BE2; -.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0008021; C:synaptic vesicle; IEA:InterPro.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   InterPro; IPR001565; Synaptotagmin.
DR   Pfam; PF00168; C2; 2.
DR   PRINTS; PR00360; C2DOMAIN.
DR   PRINTS; PR00399; SYNAPTOTAGMN.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 2.
PE   2: Evidence at transcript level;
KW   Repeat.
SQ   SEQUENCE   444 AA;  50230 MW;  D07FE631C85AD276 CRC64;
     MPWRKKEASS PSSANPASET LQSPSSRGNM ADKLKDPSAL GFLEAAVKIS HTSPDIPAEV
     QMSVKEHIMR HTKLQRQTTE PASSTRHTSF KRHLPRQMHV SSVDYGNELP PAAAEQPTSI
     GRIKPELYKQ KSVDGDDAKS EAAKSCGKIN FSLRYDYESE TLIVRILKAF DLPAKDFCGS
     SDPYVKIYLL PDRKCKLQTR VHRKTLNPTF DENFHFPVPY EELADRKLHL SVFDFDRFSR
     HDMIGEVILD NLFEASDLSR ETSIWKDIQY ATSESVDLGE IMFSLCYLPT AGRLTLTVIK
     CRNLKAMDIT GYSDPYVKVS LLCDGRRLKK KKTTIKKNTL NPIYNEAIIF DIPPENMDQV
     SLLISVMDYD RVGHNEIIGV CRVGINAEGL GRDHWNEMLA YPRKPIAHWH SLVEVKKSFK
     EWQGRAASFD SESSCPSPKP PPTP
//
ID   Q05C77_MOUSE            Unreviewed;       148 AA.
AC   Q05C77;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   05-OCT-2010, entry version 21.
DE   SubName: Full=Ralbp1 protein;
DE   Flags: Fragment;
GN   Name=Ralbp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; BC028516; AAH28516.1; -; mRNA.
DR   IPI; IPI00808314; -.
DR   UniGene; Mm.17009; -.
DR   STRING; Q05C77; -.
DR   Ensembl; ENSMUST00000024905; ENSMUSP00000024905; ENSMUSG00000024096.
DR   MGI; MGI:108466; Ralbp1.
DR   eggNOG; roNOG05323; -.
DR   InParanoid; Q05C77; -.
DR   ArrayExpress; Q05C77; -.
DR   Bgee; Q05C77; -.
DR   Genevestigator; Q05C77; -.
PE   2: Evidence at transcript level;
FT   NON_TER     148    148
SQ   SEQUENCE   148 AA;  16816 MW;  41A522AFCEA29EBF CRC64;
     MTECFLPPSS SPSEHRRAEH GSGLTRTPSS EEISPTKFPG LYRTGEPSPP HDVLHEPPDT
     VSDDDKDHGK KKGKFKKKEK RTEGYAAFQE GSSGDEAESP SKVKRSKGIH VFKKPSFSKK
     KEKDFKIKEK PKEKKKKKKK KKKKKKKK
//
ID   Q05CA9_MOUSE            Unreviewed;       485 AA.
AC   Q05CA9;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   08-MAR-2011, entry version 25.
DE   SubName: Full=Prcc protein;
DE   Flags: Fragment;
GN   Name=Prcc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor. C3;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
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DR   EMBL; BC027831; AAH27831.1; -; mRNA.
DR   IPI; IPI00808201; -.
DR   UniGene; Mm.35089; -.
DR   STRING; Q05CA9; -.
DR   PRIDE; Q05CA9; -.
DR   Ensembl; ENSMUST00000005015; ENSMUSP00000005015; ENSMUSG00000004895.
DR   MGI; MGI:2137738; Prcc.
DR   eggNOG; roNOG14798; -.
DR   HOVERGEN; HBG002845; -.
DR   InParanoid; Q05CA9; -.
DR   OrthoDB; EOG4MSCZR; -.
DR   ArrayExpress; Q05CA9; -.
DR   Bgee; Q05CA9; -.
DR   Genevestigator; Q05CA9; -.
PE   1: Evidence at protein level;
FT   NON_TER     485    485
SQ   SEQUENCE   485 AA;  51891 MW;  E171ADF5927A00C6 CRC64;
     MSLVAYASSD DSEPDEPEPE PEPEEEDVAA PMPGPTLGGL FASLPAPKGP ALLPPPPQML
     APAFPPPLLL PPPTGDPRLQ PPPPLPFGLG GFPPPAGVSP AEAAGVGEGL GLPSPQGPGL
     SLPPAVGGVG PPLGLPKPKK RTEPVRIAAP ELQKGDSDSE EDEPAKKKVV LQGSGEGTGL
     SALLPQPKNL TVKETNRLLL PHAFSRKPSD ISSDAKPSRL ASKTKPASLA PVLGTTTTTP
     SPSAIKAAAK SAALQVTKQI TQEDDDSDEE VAPENFFSLP DKAEPPGVEP YPYPVPTVPE
     ELPPGTEPEP AFQDDAANAP LEFKMAAGSS GAPWMPKPGD DYSYNQFSTY GDANAAGAYY
     QDYYSGGYYP APDPALVPPQ EIAPDASFID DEAFKRLQGK RNRGREEINF VEIKGDDQLS
     GAQQWMTKSL TEEKTMKSFS KKKKKKKKKK KKKKKKKKKK KKKKKKKKKK KKKKKKKKKK
     KKKKK
//
ID   Q05CJ5_MOUSE            Unreviewed;       313 AA.
AC   Q05CJ5;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   SubName: Full=Atp2b1 protein;
DE   Flags: Fragment;
GN   Name=Atp2b1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
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DR   EMBL; BC024831; AAH24831.1; -; mRNA.
DR   IPI; IPI00875219; -.
DR   UniGene; Mm.166944; -.
DR   UniGene; Mm.471912; -.
DR   STRING; Q05CJ5; -.
DR   Ensembl; ENSMUST00000105284; ENSMUSP00000100921; ENSMUSG00000019943.
DR   MGI; MGI:104653; Atp2b1.
DR   eggNOG; roNOG14596; -.
DR   HOVERGEN; HBG082261; -.
DR   NextBio; 326102; -.
DR   ArrayExpress; Q05CJ5; -.
DR   Bgee; Q05CJ5; -.
DR   Genevestigator; Q05CJ5; -.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015662; F:ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006816; P:calcium ion transport; TAS:MGI.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023300; ATPase_P-typ_cyto_domA.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom.
DR   Gene3D; G3DSA:2.70.150.10; ATPase_P-typ_cyto_domA; 2.
DR   Gene3D; G3DSA:1.20.1110.10; ATPase_P-typ_TM_dom; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Membrane; Nucleotide-binding; Transmembrane;
KW   Transmembrane helix.
FT   NON_TER     313    313
SQ   SEQUENCE   313 AA;  33980 MW;  2BA5A43CFB8E2364 CRC64;
     MGDMANNSVA YSGVKNSLKE ANHDGDFGIT LTELRALMEL RSTDALRKIQ ESYGDVYGIC
     TKLKTSPNEG LSGNPADLER REAVFGKNFI PPKKPKTFLQ LVWEALQDVT LIILEIAAIV
     SLGLSFYQPP EGDNALCGEV SVGEEEGEGE TGWIEGAAIL LSVVCVVLVT AFNDWSKEKQ
     FRGLQSRIEQ EQKFTVIRGG QVIQIPVADI TVGDIAQVKY GDLLPADGIL IQGNDLKIDE
     SSLTGESDHV KKSLDKDPLL LSGTHVMEGS GRMVVTAVGV NSQTGIIFTL LGAGGEEEEK
     KDEKKKEKKK KKK
//
ID   Q05CM6_MOUSE            Unreviewed;       471 AA.
AC   Q05CM6;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   08-MAR-2011, entry version 31.
DE   SubName: Full=Ankrd12 protein;
DE   Flags: Fragment;
GN   Name=Ankrd12;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC023046; AAH23046.1; -; mRNA.
DR   IPI; IPI00330318; -.
DR   RefSeq; NP_001020743.1; NM_001025572.1.
DR   UniGene; Mm.34706; -.
DR   UniGene; Mm.441953; -.
DR   Ensembl; ENSMUST00000038116; ENSMUSP00000039035; ENSMUSG00000034647.
DR   GeneID; 106585; -.
DR   KEGG; mmu:106585; -.
DR   CTD; 106585; -.
DR   MGI; MGI:1914357; Ankrd12.
DR   eggNOG; roNOG12480; -.
DR   HOVERGEN; HBG059478; -.
DR   InParanoid; Q05CM6; -.
DR   OrthoDB; EOG4P8FH5; -.
DR   NextBio; 358286; -.
DR   ArrayExpress; Q05CM6; -.
DR   Bgee; Q05CM6; -.
DR   Genevestigator; Q05CM6; -.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 3.
DR   SMART; SM00248; ANK; 3.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
PE   2: Evidence at transcript level;
KW   ANK repeat; Repeat.
FT   NON_TER     471    471
SQ   SEQUENCE   471 AA;  52766 MW;  72D8F45120119AB6 CRC64;
     MPKSGFTKPV QSENSDSDSS MVERPYGRKS KDKIASYSKT SKIDRGDMGK EMREKPSMKR
     KLPFTVSPSR NEERDSDTDS DPGHTSENWG ERLISSYRTY SEKEGPEKKK TKKEAGTKKS
     TPVSILFGYP LSERKQMALL MQMTARDNSP DSTPSHPSQA TPAQKKTPSS SSRQKDKINK
     RNERGETPLH MAAIRGDVKQ VKELISLGAN VNVKDFAGWT PLHEACNVGY YDVAKILIAA
     GADVNTQGLD DDTPLHDSAS SGHRDIVKLL LRHGGNPFQA NKHGERPVDV AETEELELLL
     KREVPLSGDD ESYTDSEEAQ SVNPSSVDEN IDSETEKDSF VCGSKILPSK APLPSALDEY
     EFKDDDEEEI SKMIDDRHIL RKEQRRENES EAERSGLFAK QEKTFYSKSF KTKKQKPSRV
     LCSSTESSDE EGLQNRKIST ACSVAESSHP DMQAKKEYEY KQKGKVKKKK K
//
ID   IF2P_MOUSE              Reviewed;        1216 AA.
AC   Q05D44; Q3SYI4; Q3TQJ8; Q3UL37; Q3UM39; Q6PAI0; Q8CFF4; Q8CGD6;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   08-MAR-2011, entry version 35.
DE   RecName: Full=Eukaryotic translation initiation factor 5B;
DE            Short=eIF-5B;
DE   AltName: Full=Translation initiation factor IF-2;
GN   Name=Eif5b; Synonyms=If2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-771.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-402.
RC   STRAIN=FVB/N; TISSUE=Limb, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=22313332; PubMed=12426392; DOI=10.1093/emboj/cdf613;
RA   Bohnsack M.T., Regener K., Schwappach B., Saffrich R., Paraskeva E.,
RA   Hartmann E., Goerlich D.;
RT   "Exp5 exports eEF1A via tRNA from nuclei and synergizes with other
RT   transport pathways to confine translation to the cytoplasm.";
RL   EMBO J. 21:6205-6215(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-215, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179; SER-183; SER-184;
RP   SER-187; SER-191; SER-584; SER-585 AND SER-591, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-137; SER-139;
RP   SER-187; SER-191 AND SER-215, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-137; SER-165;
RP   SER-183; SER-184; SER-187 AND SER-191, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-215, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-137; SER-139
RP   AND SER-215, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Function in general translation initiation by promoting
CC       the binding of the formylmethionine-tRNA to ribosomes. Seems to
CC       function along with eIF-2 (By similarity).
CC   -!- SUBUNIT: Interacts with ANXA5 in a calcium and phospholipid-
CC       dependent manner (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the IF-2 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH18347.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAH37150.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAH40746.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAH60288.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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DR   EMBL; AC114583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK145146; BAE26259.1; -; mRNA.
DR   EMBL; AK145732; BAE26614.1; -; mRNA.
DR   EMBL; AK163527; BAE37384.1; -; mRNA.
DR   EMBL; BC018347; AAH18347.1; ALT_SEQ; mRNA.
DR   EMBL; BC037150; AAH37150.1; ALT_SEQ; mRNA.
DR   EMBL; BC040746; AAH40746.1; ALT_SEQ; mRNA.
DR   EMBL; BC060288; AAH60288.1; ALT_SEQ; mRNA.
DR   IPI; IPI00756424; -.
DR   RefSeq; NP_938045.2; NM_198303.2.
DR   UniGene; Mm.260943; -.
DR   ProteinModelPortal; Q05D44; -.
DR   SMR; Q05D44; 623-1215.
DR   STRING; Q05D44; -.
DR   PhosphoSite; Q05D44; -.
DR   PRIDE; Q05D44; -.
DR   Ensembl; ENSMUST00000027252; ENSMUSP00000027252; ENSMUSG00000026083.
DR   GeneID; 226982; -.
DR   KEGG; mmu:226982; -.
DR   CTD; 226982; -.
DR   MGI; MGI:2441772; Eif5b.
DR   HOVERGEN; HBG019036; -.
DR   InParanoid; Q05D44; -.
DR   OMA; FDRENIK; -.
DR   OrthoDB; EOG44BB1J; -.
DR   ArrayExpress; Q05D44; -.
DR   Bgee; Q05D44; -.
DR   Genevestigator; Q05D44; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000795; ProtSyn_GTP-bd.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR015760; TIF_IF2.
DR   InterPro; IPR023115; TIF_IF2_dom3.
DR   InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR   InterPro; IPR009000; Transl_elong_init/rib_B-barrel.
DR   Gene3D; G3DSA:3.40.50.10050; TIF_IF2_dom3; 1.
DR   PANTHER; PTHR23115:SF41; aIF-2; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF52156; TIF_IF2_dom3; 1.
DR   SUPFAM; SSF50447; Translat_factor; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; GTP-binding; Initiation factor;
KW   Nucleotide-binding; Phosphoprotein; Protein biosynthesis.
FT   CHAIN         1   1216       Eukaryotic translation initiation factor
FT                                5B.
FT                                /FTId=PRO_0000354071.
FT   NP_BIND     634    641       GTP (By similarity).
FT   COMPBIAS     39    452       Lys-rich.
FT   COMPBIAS    235    561       Glu-rich.
FT   MOD_RES      66     66       Phosphoserine (By similarity).
FT   MOD_RES     108    108       Phosphoserine (By similarity).
FT   MOD_RES     114    114       Phosphoserine.
FT   MOD_RES     137    137       Phosphoserine.
FT   MOD_RES     139    139       Phosphoserine.
FT   MOD_RES     165    165       Phosphoserine.
FT   MOD_RES     179    179       Phosphoserine.
FT   MOD_RES     183    183       Phosphoserine.
FT   MOD_RES     184    184       Phosphoserine.
FT   MOD_RES     187    187       Phosphoserine.
FT   MOD_RES     191    191       Phosphoserine.
FT   MOD_RES     215    215       Phosphoserine.
FT   MOD_RES     223    223       Phosphoserine (By similarity).
FT   MOD_RES     300    300       Phosphothreonine (By similarity).
FT   MOD_RES     553    553       Phosphoserine (By similarity).
FT   MOD_RES     556    556       Phosphoserine (By similarity).
FT   MOD_RES     584    584       Phosphoserine.
FT   MOD_RES     585    585       Phosphoserine.
FT   MOD_RES     587    587       Phosphoserine (By similarity).
FT   MOD_RES     591    591       Phosphoserine.
FT   MOD_RES     780    780       N6-acetyllysine (By similarity).
FT   MOD_RES     919    919       N6-acetyllysine (By similarity).
FT   MOD_RES    1164   1164       Phosphoserine (By similarity).
FT   CONFLICT    121    121       D -> N (in Ref. 2; BAE26259).
FT   CONFLICT    188    188       G -> C (in Ref. 2; BAE26259).
FT   CONFLICT    254    254       M -> L (in Ref. 2; BAE26259).
FT   CONFLICT    302    302       A -> V (in Ref. 2; BAE26259).
SQ   SEQUENCE   1216 AA;  137616 MW;  38D1C21648E4EAEC CRC64;
     MGKKQKNKSE DSTKDDTDLG ALAAEIEGAG AAKEQEPQKS KGKKKKEKKK QDFDENDILR
     ELEELSLEAQ GIRADRDAAA VKPTENNEEE SASKQDKKKK GQKGKKTSFD ENDSEELEDK
     DSKSKKTARP NSEAPLSGSE DADDSNKLSK KGKKAQKSTK KRDGSEEDED NSKRSKERSR
     VNSSGESGGE SDEFLQSRKG QKKNQKNKSV PTVDSGNEDD DSSFKIKTVA QKKAEKKERE
     KKKRDEEKAK LRKMKEKEEL EKGKKEQSKQ REPQKRPEEE VLTLRGTPDT GAASEEKGDT
     AAALEDDNEG DKKKKDKKKK KTEKDEKEKE KKKGPSKSTV KAIQEALAKL KEEEERQKRE
     EEERIKRLEE LEAKRKEEER LEQEKRERKK QKEKERKERL KKEGKLLTKS QREARARAEV
     TLRHLQAQGV EVPSKDSLPK KRPVYEDKKK KKTPQQLESK EVSETLEISA PVEAVDQGGP
     EKEETPPSVE PEEEEDTEDA GLDDWEAMAS DEEREKEGNM IHIEVEENPE EEEEEEEEEE
     EEESEDEEEE GDSEGSDGDE EDCKLSDEKD SGKAGDTKPS KDASSDSEYD SDDDRTKEER
     AYDKAKRRIE KRRLEHGKNV NTEKLRAPII CVLGHVDTGK TKILDKLRHT HVQDGEAGGI
     TQQIGATNVP LEAINEQTKM IKNFDRENVR IPGMLIIDTP GHESFSNLRN RGSSLCDIAI
     LVVDIMHGLE PQTIESINIL KSKKCPFIVA LNKIDRLYDW KKSPDSDVAV TLKKQKKNTK
     DEFEERAKAI IVEFAQQGLN AALFYENKDP RTFVSLVPTS AHTGDGMGSL IYLLVELTQT
     MLSKRLAHCE ELRAQVMEVK ALPGMGTTID VILINGRLKE GDTIIVPGVE GPIVTQIRGL
     LLPPPMKELR VKNQYEKHKE VEAAQGVKIL GKDLEKTLAG LPLLVAYKDD EIPVLKDELI
     HELKQTLNAI KLEEKGVYVQ ASTLGSLEAL LEFLKTSEVP YAGINIGPVH KKDVMKASVM
     LEHDPQYAVI LAFDVRIERD AQEMADSLGV RIFSAEIIYH LFDAFTKYRQ DYKKQKQEEF
     KHIAVFPCKM KILPQYIFNS RDPIVIGVTV EAGQVKQGTP MCVPSKNFVD IGIVTSIEIN
     HKQVDVAKKG QEVCVKIEPI PGESPKMFGR HFEATDILVS KISRQSIDAL KDWFRDEMQK
     SDWQLIVELK KVFEII
//
ID   ATP5I_MOUSE             Reviewed;          71 AA.
AC   Q06185; P70342;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=ATP synthase subunit e, mitochondrial;
DE            Short=ATPase subunit e;
GN   Name=Atp5i; Synonyms=Atp5k, Lfm-1, Lfm1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Mammary gland;
RX   MEDLINE=93135763; PubMed=7678489; DOI=10.1006/bbrc.1993.1026;
RA   Elliott T.S., Swartz D.A., Paisley E.A., Mangian H.J., Visek W.J.,
RA   Kaput J.;
RT   "F1F0-ATPase subunit e gene isolated in a screen for diet regulated
RT   genes.";
RL   Biochem. Biophys. Res. Commun. 190:167-174(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BALB/cJ;
RX   MEDLINE=96355443; PubMed=8702853; DOI=10.1074/jbc.271.34.20942;
RA   Swartz D.A., Park E.I., Visek W.J., Kaput J.;
RT   "The e subunit gene of murine F1F0-ATP synthase. Genomic sequence,
RT   chromosomal mapping, and diet regulation.";
RL   J. Biol. Chem. 271:20942-20948(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-12; 16-28 AND 60-71, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-32, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
CC       synthase or Complex V) produces ATP from ADP in the presence of a
CC       proton gradient across the membrane which is generated by electron
CC       transport complexes of the respiratory chain. F-type ATPases
CC       consist of two structural domains, F(1) - containing the
CC       extramembraneous catalytic core, and F(0) - containing the
CC       membrane proton channel, linked together by a central stalk and a
CC       peripheral stalk. During catalysis, ATP synthesis in the catalytic
CC       domain of F(1) is coupled via a rotary mechanism of the central
CC       stalk subunits to proton translocation. Part of the complex F(0)
CC       domain. Minor subunit located with subunit a in the membrane.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel. CF(0) seems to
CC       have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC   -!- TISSUE SPECIFICITY: Mammary gland, liver, kidney, heart, spleen,
CC       brain and lung.
CC   -!- SIMILARITY: Belongs to the ATPase e subunit family.
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DR   EMBL; S52977; AAB24947.1; -; mRNA.
DR   EMBL; U59283; AAC52713.1; -; Genomic_DNA.
DR   EMBL; BC028438; AAH28438.1; -; mRNA.
DR   IPI; IPI00111770; -.
DR   PIR; JC1412; JC1412.
DR   RefSeq; NP_031533.2; NM_007507.2.
DR   UniGene; Mm.136093; -.
DR   STRING; Q06185; -.
DR   PhosphoSite; Q06185; -.
DR   PRIDE; Q06185; -.
DR   Ensembl; ENSMUST00000049628; ENSMUSP00000051222; ENSMUSG00000050856.
DR   GeneID; 11958; -.
DR   KEGG; mmu:11958; -.
DR   UCSC; uc008yoa.1; mouse.
DR   CTD; 11958; -.
DR   MGI; MGI:106636; Atp5k.
DR   HOGENOM; HBG445273; -.
DR   HOVERGEN; HBG050613; -.
DR   InParanoid; Q06185; -.
DR   OMA; RYSALLV; -.
DR   OrthoDB; EOG45758D; -.
DR   PhylomeDB; Q06185; -.
DR   NextBio; 280081; -.
DR   ArrayExpress; Q06185; -.
DR   Bgee; Q06185; -.
DR   Genevestigator; Q06185; -.
DR   GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR008386; ATPase_F0-cplx_esu_mt.
DR   Pfam; PF05680; ATP-synt_E; 1.
PE   1: Evidence at protein level;
KW   ATP synthesis; CF(0); Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Phosphoprotein; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2     71       ATP synthase subunit e, mitochondrial.
FT                                /FTId=PRO_0000071685.
FT   MOD_RES      32     32       Phosphotyrosine.
FT   CONFLICT     13     13       F -> S (in Ref. 2; AAC52713).
FT   CONFLICT     48     48       K -> R (in Ref. 2; AAC52713).
SQ   SEQUENCE   71 AA;  8236 MW;  0379C3E14C098F12 CRC64;
     MVPPVQVSPL IKFGRYSALI IGMAYGAKRY SYLKPRAEEE RRIAAEEKKR LDELKRIERE
     LAEAQDDSIL K
//
ID   CLUS_MOUSE              Reviewed;         448 AA.
AC   Q06890;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Clusterin;
DE   AltName: Full=Apolipoprotein J;
DE            Short=Apo-J;
DE   AltName: Full=Clustrin;
DE   AltName: Full=Sulfated glycoprotein 2;
DE            Short=SGP-2;
DE   Contains:
DE     RecName: Full=Clusterin beta chain;
DE   Contains:
DE     RecName: Full=Clusterin alpha chain;
DE   Flags: Precursor;
GN   Name=Clu; Synonyms=Apoj, Msgp-2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   MEDLINE=93356785; PubMed=8352774; DOI=10.1006/bbrc.1993.1946;
RA   Lee K.-H., Ji Y.-M., Lim H.M., Lee S.-C., You K.-H.;
RT   "Molecular cloning and sequencing of sulfated glycoprotein-2 cDNA from
RT   testis of mouse: implications of two different mRNAs of SGP-2.";
RL   Biochem. Biophys. Res. Commun. 194:1175-1180(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Heart;
RX   MEDLINE=93359508; PubMed=8354695; DOI=10.1083/jcb.122.5.1119;
RA   French L.E., Chonn A., Ducrest D., Baumann B., Belin D., Wohlwend A.,
RA   Kiss J.Z., Sappino A.P., Tschopp J., Schifferli J.A.;
RT   "Murine clusterin: molecular cloning and mRNA localization of a gene
RT   associated with epithelial differentiation processes during
RT   embryogenesis.";
RL   J. Cell Biol. 122:1119-1130(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX   MEDLINE=94223204; PubMed=8169523;
RA   Jordan-Starck T.C., Lund S.D., Witte D.P., Aronow B.J., Ley C.A.,
RA   Stuart W.D., Swertfeger D.K., Clayton L.R., Sells S.F., Paigen B.;
RT   "Mouse apolipoprotein J: characterization of a gene implicated in
RT   atherosclerosis.";
RL   J. Lipid Res. 35:194-210(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Hodgdon B.A., Min B.H., Yan H., Farris J.A., Foster D.N.,
RA   Strauch A.R.;
RT   "Secretion of sulfated glycoprotein (clustrin) accompanies
RT   cytodifferentiation and structural remodeling of mouse BC3H1 myogenic
RT   cells.";
RL   Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-327, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Plasma;
RX   PubMed=16944957; DOI=10.1021/pr060186m;
RA   Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
RA   Gevaert K.;
RT   "Proteome-wide characterization of N-glycosylation events by diagonal
RT   chromatography.";
RL   J. Proteome Res. 5:2438-2447(2006).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-290, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Plasma;
RX   PubMed=17330941; DOI=10.1021/pr0604559;
RA   Bernhard O.K., Kapp E.A., Simpson R.J.;
RT   "Enhanced analysis of the mouse plasma proteome using cysteine-
RT   containing tryptic glycopeptides.";
RL   J. Proteome Res. 6:987-995(2007).
CC   -!- FUNCTION: Not yet clear. It is known to be expressed in a variety
CC       of tissues and it seems to be able to bind to cells, membranes and
CC       hydrophobic proteins. It has been associated with programmed cell
CC       death.
CC   -!- SUBUNIT: Antiparallel disulfide-linked heterodimer. Interacts with
CC       APOA1, CLUAP1 AND PON1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Most abundant in stomach, liver, brain, and
CC       testis, with intermediate levels in heart, ovary and kidney.
CC   -!- PTM: Extensively glycosylated with sulfated N-linked
CC       carbohydrates.
CC   -!- PTM: Phosphorylation sites are present in the extracelllular
CC       medium (By similarity).
CC   -!- SIMILARITY: Belongs to the clusterin family.
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DR   EMBL; D14077; BAA03162.1; -; mRNA.
DR   EMBL; L08235; AAA37422.1; -; mRNA.
DR   EMBL; S70244; AAB30623.1; -; mRNA.
DR   EMBL; L05670; AAA37284.1; -; mRNA.
DR   EMBL; BC075668; AAH75668.1; -; mRNA.
DR   IPI; IPI00320420; -.
DR   PIR; A40714; A40714.
DR   PIR; I56335; I56335.
DR   RefSeq; NP_038520.2; NM_013492.2.
DR   UniGene; Mm.200608; -.
DR   MINT; MINT-1176977; -.
DR   STRING; Q06890; -.
DR   PRIDE; Q06890; -.
DR   Ensembl; ENSMUST00000022616; ENSMUSP00000022616; ENSMUSG00000022037.
DR   GeneID; 12759; -.
DR   KEGG; mmu:12759; -.
DR   CTD; 12759; -.
DR   MGI; MGI:88423; Clu.
DR   eggNOG; roNOG17972; -.
DR   HOGENOM; HBG713762; -.
DR   HOVERGEN; HBG006908; -.
DR   InParanoid; Q06890; -.
DR   OMA; NGDRIDS; -.
DR   PhylomeDB; Q06890; -.
DR   NextBio; 282108; -.
DR   ArrayExpress; Q06890; -.
DR   Bgee; Q06890; -.
DR   CleanEx; MM_CLU; -.
DR   Genevestigator; Q06890; -.
DR   GermOnline; ENSMUSG00000022037; Mus musculus.
DR   GO; GO:0008219; P:cell death; IEA:InterPro.
DR   InterPro; IPR016016; Clusterin.
DR   InterPro; IPR000753; Clusterin-like.
DR   InterPro; IPR016015; Clusterin_C.
DR   InterPro; IPR016014; Clusterin_N.
DR   PANTHER; PTHR10970:SF1; Clusterin; 1.
DR   Pfam; PF01093; Clusterin; 1.
DR   PIRSF; PIRSF002368; Clusterin; 1.
DR   SMART; SM00035; CLa; 1.
DR   SMART; SM00030; CLb; 1.
DR   PROSITE; PS00492; CLUSTERIN_1; 1.
DR   PROSITE; PS00493; CLUSTERIN_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Phosphoprotein; Secreted; Signal.
FT   SIGNAL        1     21       By similarity.
FT   CHAIN        22    448       Clusterin.
FT                                /FTId=PRO_0000005535.
FT   CHAIN        22    226       Clusterin beta chain (By similarity).
FT                                /FTId=PRO_0000005536.
FT   CHAIN       227    447       Clusterin alpha chain (By similarity).
FT                                /FTId=PRO_0000005537.
FT   MOD_RES     393    393       Phosphoserine (By similarity).
FT   MOD_RES     395    395       Phosphoserine (By similarity).
FT   CARBOHYD    102    102       N-linked (GlcNAc...) (Probable).
FT   CARBOHYD    144    144       N-linked (GlcNAc...) (Probable).
FT   CARBOHYD    290    290       N-linked (GlcNAc...).
FT   CARBOHYD    327    327       N-linked (GlcNAc...).
FT   CARBOHYD    353    353       N-linked (GlcNAc...) (Probable).
FT   CARBOHYD    373    373       N-linked (GlcNAc...) (Probable).
FT   DISULFID    101    312       Interchain (between beta and alpha
FT                                chains) (By similarity).
FT   DISULFID    112    304       Interchain (between beta and alpha
FT                                chains) (By similarity).
FT   DISULFID    115    301       Interchain (between beta and alpha
FT                                chains) (By similarity).
FT   DISULFID    120    294       Interchain (between beta and alpha
FT                                chains) (By similarity).
FT   DISULFID    128    284       Interchain (between beta and alpha
FT                                chains) (By similarity).
FT   CONFLICT     10     10       L -> M (in Ref. 3; AAB30623).
FT   CONFLICT    335    336       RL -> TV (in Ref. 4; AAA37284).
FT   CONFLICT    350    350       K -> N (in Ref. 4; AAA37284).
SQ   SEQUENCE   448 AA;  51656 MW;  A860600A6F8D47F6 CRC64;
     MKILLLCVAL LLIWDNGMVL GEQEVSDNEL QELSTQGSRY INKEIQNAVQ GVKHIKTLIE
     KTNAERKSLL NSLEEAKKKK EDALEDTRDS EMKLKAFPEV CNETMMALWE ECKPCLKHTC
     MKFYARVCRS GSGLVGQQLE EFLNQSSPFY FWMNGDRIDS LLESDRQQSQ VLDAMQDSFA
     RASGIIDTLF QDRFFARELH DPHYFSPIGF PHKRPHFLYP KSRLVRSLMS PSHYGPPSFH
     NMFQPFFEMI HQAQQAMDVQ LHSPAFQFPD VDFLREGEDD RTVCKEIRRN STGCLKMKGQ
     CEKCQEILSV DCSTNNPAQA NLRQELNDSL QVAERLTEQY KELLQSFQSK MLNTSSLLEQ
     LNDQFNWVSQ LANLTQGEDK YYLRVSTVTT HSSDSEVPSR VTEVVVKLFD SDPITVVLPE
     EVSKDNPKFM DTVAEKALQE YRRKSRAE
//
ID   IBP5_MOUSE              Reviewed;         271 AA.
AC   Q07079;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   08-MAR-2011, entry version 107.
DE   RecName: Full=Insulin-like growth factor-binding protein 5;
DE            Short=IBP-5;
DE            Short=IGF-binding protein 5;
DE            Short=IGFBP-5;
DE   Flags: Precursor;
GN   Name=Igfbp5; Synonyms=Igfbp-5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Myoblast;
RX   MEDLINE=94042976; PubMed=7693664;
RA   James P.L., Jones S.B., Busby W.H. Jr., Clemmons D.R., Rotwein P.;
RT   "A highly conserved insulin-like growth factor-binding protein (IGFBP-
RT   5) is expressed during myoblast differentiation.";
RL   J. Biol. Chem. 268:22305-22312(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Spleen;
RX   MEDLINE=94307727; PubMed=7518410; DOI=10.1006/geno.1994.1195;
RA   Kou K., Jenkins N.A., Gilbert D.J., Copeland N.G., Rotwein P.;
RT   "Organization, expression, and chromosomal location of the mouse
RT   insulin-like growth factor binding protein 5 gene.";
RL   Genomics 20:412-418(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   MEDLINE=95121750; PubMed=7529732; DOI=10.1016/0303-7207(94)90051-5;
RA   Schuller A.G.P., Groffen C., van Neck J.W., Zwarthoff E.C.,
RA   Drop S.L.S.;
RT   "cDNA cloning and mRNA expression of the six mouse insulin-like growth
RT   factor binding proteins.";
RL   Mol. Cell. Endocrinol. 104:57-66(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: IGF-binding proteins prolong the half-life of the IGFs
CC       and have been shown to either inhibit or stimulate the growth
CC       promoting effects of the IGFs on cell culture. They alter the
CC       interaction of IGFs with their cell surface receptors.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Most abundant in kidney, uterus and
CC       gastrocnemius muscle.
CC   -!- SIMILARITY: Contains 1 IGFBP N-terminal domain.
CC   -!- SIMILARITY: Contains 1 thyroglobulin type-1 domain.
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DR   EMBL; L12447; AAC37636.1; -; mRNA.
DR   EMBL; U02025; AAC01750.1; -; Genomic_DNA.
DR   EMBL; U02023; AAC01750.1; JOINED; Genomic_DNA.
DR   EMBL; U02027; AAC01750.1; JOINED; Genomic_DNA.
DR   EMBL; U02024; AAC01750.1; JOINED; Genomic_DNA.
DR   EMBL; X81583; CAA57273.1; -; mRNA.
DR   EMBL; BC054812; AAH54812.1; -; mRNA.
DR   EMBL; BC057447; AAH57447.1; -; mRNA.
DR   IPI; IPI00114022; -.
DR   PIR; I48604; I48604.
DR   RefSeq; NP_034648.2; NM_010518.2.
DR   UniGene; Mm.405761; -.
DR   UniGene; Mm.466164; -.
DR   ProteinModelPortal; Q07079; -.
DR   SMR; Q07079; 24-104, 183-268.
DR   STRING; Q07079; -.
DR   MEROPS; I31.952; -.
DR   PhosphoSite; Q07079; -.
DR   PRIDE; Q07079; -.
DR   Ensembl; ENSMUST00000027377; ENSMUSP00000027377; ENSMUSG00000026185.
DR   GeneID; 16011; -.
DR   KEGG; mmu:16011; -.
DR   UCSC; uc007bkx.1; mouse.
DR   CTD; 16011; -.
DR   MGI; MGI:96440; Igfbp5.
DR   eggNOG; roNOG14945; -.
DR   HOGENOM; HBG443735; -.
DR   HOVERGEN; HBG002631; -.
DR   InParanoid; Q07079; -.
DR   OMA; YREQAKI; -.
DR   OrthoDB; EOG4RV2RZ; -.
DR   PhylomeDB; Q07079; -.
DR   NextBio; 288826; -.
DR   PMAP-CutDB; Q07079; -.
DR   ArrayExpress; Q07079; -.
DR   Bgee; Q07079; -.
DR   CleanEx; MM_IGFBP5; -.
DR   Genevestigator; Q07079; -.
DR   GermOnline; ENSMUSG00000026185; Mus musculus.
DR   GO; GO:0016942; C:insulin-like growth factor binding protein complex; IC:MGI.
DR   GO; GO:0001968; F:fibronectin binding; IDA:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0006006; P:glucose metabolic process; IMP:MGI.
DR   GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
DR   GO; GO:0060056; P:mammary gland involution; IMP:MGI.
DR   GO; GO:0043569; P:negative regulation of insulin-like growth factor receptor signaling pathway; IMP:MGI.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; IGI:MGI.
DR   GO; GO:0001649; P:osteoblast differentiation; IEP:BHF-UCL.
DR   GO; GO:0044342; P:type B pancreatic cell proliferation; IGI:MGI.
DR   GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IGI:MGI.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling cascade; IMP:MGI.
DR   GO; GO:0001558; P:regulation of cell growth; IGI:MGI.
DR   GO; GO:0010906; P:regulation of glucose metabolic process; IGI:MGI.
DR   GO; GO:0051146; P:striated muscle cell differentiation; IGI:MGI.
DR   InterPro; IPR009030; Growth_fac_rcpt.
DR   InterPro; IPR012213; IGFBP-5.
DR   InterPro; IPR000867; IGFBP-like.
DR   InterPro; IPR009168; IGFBP1-6.
DR   InterPro; IPR022321; IGFBP_1-6_chordata.
DR   InterPro; IPR017891; Insulin_GF-bd_Cys-rich_CS.
DR   InterPro; IPR000716; Thyroglobulin_1.
DR   Gene3D; G3DSA:4.10.800.10; Thyroglobulin_1; 1.
DR   PANTHER; PTHR11551:SF4; IGFBP-5; 1.
DR   PANTHER; PTHR11551; IGFBP1-6; 1.
DR   Pfam; PF00219; IGFBP; 1.
DR   Pfam; PF00086; Thyroglobulin_1; 1.
DR   PRINTS; PR01976; IGFBPFAMILY.
DR   PRINTS; PR01981; IGFBPFAMILY5.
DR   SMART; SM00121; IB; 1.
DR   SMART; SM00211; TY; 1.
DR   SUPFAM; SSF57184; Grow_fac_recept; 1.
DR   SUPFAM; SSF57610; Thyroglobulin_1; 1.
DR   PROSITE; PS00222; IGFBP_N_1; 1.
DR   PROSITE; PS51323; IGFBP_N_2; 1.
DR   PROSITE; PS00484; THYROGLOBULIN_1_1; 1.
DR   PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Growth factor binding;
KW   Secreted; Signal.
FT   SIGNAL        1     19       Potential.
FT   CHAIN        20    271       Insulin-like growth factor-binding
FT                                protein 5.
FT                                /FTId=PRO_0000014386.
FT   DOMAIN       22    102       IGFBP N-terminal.
FT   DOMAIN      188    262       Thyroglobulin type-1.
FT   DISULFID    191    218       By similarity.
FT   DISULFID    229    240       By similarity.
FT   DISULFID    242    262       By similarity.
FT   CONFLICT    112    112       Missing (in Ref. 2; AAC01750).
SQ   SEQUENCE   271 AA;  30372 MW;  F55A58729861F6F0 CRC64;
     MVISVVLLLL AAYAVPAQGL GSFVHCEPCD EKALSMCPPS PLGCELVKEP GCGCCMTCAL
     AEGQSCGVYT ERCAQGLRCL PRQDEEKPLH ALLHGRGVCL NEKSYGEQTK IERDSREHEE
     PTTSEMAEET YSPKVFRPKH TRISELKAEA VKKDRRKKLT QSKFVGGAEN TAHPRVIPAP
     EMRQESEQGP CRRHMEASLQ EFKASPRMVP RAVYLPNCDR KGFYKRKQCK PSRGRKRGIC
     WCVDKYGMKL PGMEYVDGDF QCHAFDSSNV E
//
ID   MPRI_MOUSE              Reviewed;        2483 AA.
AC   Q07113; Q61822; Q6LED1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   08-MAR-2011, entry version 102.
DE   RecName: Full=Cation-independent mannose-6-phosphate receptor;
DE            Short=CI Man-6-P receptor;
DE            Short=CI-MPR;
DE            Short=M6PR;
DE   AltName: Full=300 kDa mannose 6-phosphate receptor;
DE            Short=MPR 300;
DE   AltName: Full=Insulin-like growth factor 2 receptor;
DE   AltName: Full=Insulin-like growth factor II receptor;
DE            Short=IGF-II receptor;
DE   AltName: Full=M6P/IGF2 receptor;
DE            Short=M6P/IGF2R;
DE   AltName: CD_antigen=CD222;
DE   Flags: Precursor;
GN   Name=Igf2r;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=94245146; PubMed=8188212; DOI=10.1006/geno.1994.1021;
RA   Szebenyi G., Rotwein P.;
RT   "The mouse insulin-like growth factor II/cation-independent mannose 6-
RT   phosphate (IGF-II/MPR) receptor gene: molecular cloning and genomic
RT   organization.";
RL   Genomics 19:120-129(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX   MEDLINE=94252588; PubMed=8194771; DOI=10.1016/0378-1119(94)90282-8;
RA   Ludwig T., Tenscher K., Remmler J., Hoflack B., Lobel P.;
RT   "Cloning and sequencing of cDNAs encoding the full-length mouse
RT   mannose 6-phosphate/insulin-like growth factor II receptor.";
RL   Gene 142:311-312(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44 AND 93-106.
RC   STRAIN=129, and C57BL/6;
RX   MEDLINE=93214996; PubMed=8462104; DOI=10.1016/0092-8674(93)90160-R;
RA   Stoger R., Kubicka P., Liu C.G., Kafri T., Razin A., Cedar H.,
RA   Barlow D.P.;
RT   "Maternal-specific methylation of the imprinted mouse Igf2r locus
RT   identifies the expressed locus as carrying the imprinting signal.";
RL   Cell 73:61-71(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44.
RC   STRAIN=129/Sv;
RX   MEDLINE=96130821; PubMed=8584025; DOI=10.1210/me.9.11.1477;
RA   Liu Z., Mittanck D.W., Kim S., Rotwein P.;
RT   "Control of insulin-like growth factor-II/mannose 6-phosphate receptor
RT   gene transcription by proximal promoter elements.";
RL   Mol. Endocrinol. 9:1477-1487(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 435-488.
RC   TISSUE=Liver;
RX   MEDLINE=91170218; PubMed=1848553;
RA   Szebenyi G., Rotwein P.;
RT   "Differential regulation of mannose 6-phosphate receptors and their
RT   ligands during the myogenic development of C2 cells.";
RL   J. Biol. Chem. 266:5534-5539(1991).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1625-2045.
RC   STRAIN=C57BL/6;
RA   Matzner U.;
RL   Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2249-2483.
RC   STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX   MEDLINE=94042980; PubMed=8226743;
RA   Chen H.J., Remmler J., Delaney J.C., Messner D.J., Lobel P.;
RT   "Mutational analysis of the cation-independent mannose 6-
RT   phosphate/insulin-like growth factor II receptor. A consensus casein
RT   kinase II site followed by 2 leucines near the carboxyl terminus is
RT   important for intracellular targeting of lysosomal enzymes.";
RL   J. Biol. Chem. 268:22338-22346(1993).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2476, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2401 AND SER-2476, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2476, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2393; SER-2401; SER-2471
RP   AND SER-2476, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [12]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1532, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2401 AND SER-2476, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [14]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-740; ASN-1532 AND
RP   ASN-1750, AND MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Acts as a positive regulator of T-cell coactivation, by
CC       binding DPP4 (By similarity). Transport of phosphorylated
CC       lysosomal enzymes from the Golgi complex and the cell surface to
CC       lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind
CC       specifically to mannose-6-phosphate receptors in the Golgi
CC       apparatus and the resulting receptor-ligand complex is transported
CC       to an acidic prelyosomal compartment where the low pH mediates the
CC       dissociation of the complex. This receptor also binds IGF2.
CC   -!- SUBUNIT: Interacts with DPP4; the interaction is direct. Binds
CC       GGA1, GGA2 and GGA3. Binds HA-I and HA-II plasma membrane adapters
CC       (By similarity).
CC   -!- INTERACTION:
CC       P18242:Ctsd; NbExp=1; IntAct=EBI-2891155, EBI-738562;
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane; Single-pass type I
CC       membrane protein.
CC   -!- DOMAIN: Contains 15 repeating units of approximately 147 AA. The
CC       most highly conserved region within the repeat consists of a
CC       stretch of 13 AA that contains cysteines at both ends.
CC   -!- SIMILARITY: Belongs to the MRL1/IGF2R family.
CC   -!- SIMILARITY: Contains 1 fibronectin type-II domain.
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DR   EMBL; L22143; AAA39320.1; -; Genomic_DNA.
DR   EMBL; L22096; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22097; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22098; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22099; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22100; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22101; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22102; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22103; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22104; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22105; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22106; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22107; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22108; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22109; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22110; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22111; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22112; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22113; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22114; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22115; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22116; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22117; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22118; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22119; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22120; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22121; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22122; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22123; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22124; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22125; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22126; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22127; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22128; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22129; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22130; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22131; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22132; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22133; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22134; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22135; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22136; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22137; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22138; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22139; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22140; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22141; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; L22142; AAA39320.1; JOINED; Genomic_DNA.
DR   EMBL; U04710; AAA19568.1; -; mRNA.
DR   EMBL; L06445; AAA37921.1; -; Genomic_DNA.
DR   EMBL; L06446; AAA37922.1; -; Genomic_DNA.
DR   EMBL; U26348; AAA98844.1; -; Genomic_DNA.
DR   EMBL; M58586; AAA39483.1; -; Genomic_DNA.
DR   EMBL; X60389; CAA42940.1; -; mRNA.
DR   EMBL; L19500; AAA16037.1; -; mRNA.
DR   IPI; IPI00308971; -.
DR   PIR; A49617; A49617.
DR   PIR; I48922; I48922.
DR   RefSeq; NP_034645.2; NM_010515.2.
DR   UniGene; Mm.26553; -.
DR   ProteinModelPortal; Q07113; -.
DR   SMR; Q07113; 43-462, 621-2273.
DR   IntAct; Q07113; 2.
DR   MINT; MINT-200350; -.
DR   STRING; Q07113; -.
DR   PhosphoSite; Q07113; -.
DR   PRIDE; Q07113; -.
DR   Ensembl; ENSMUST00000024599; ENSMUSP00000024599; ENSMUSG00000023830.
DR   GeneID; 16004; -.
DR   KEGG; mmu:16004; -.
DR   UCSC; uc008aky.1; mouse.
DR   CTD; 16004; -.
DR   MGI; MGI:96435; Igf2r.
DR   eggNOG; roNOG12256; -.
DR   HOGENOM; HBG415990; -.
DR   HOVERGEN; HBG000334; -.
DR   InParanoid; Q07113; -.
DR   OMA; INICQPL; -.
DR   OrthoDB; EOG4G1MFG; -.
DR   NextBio; 288798; -.
DR   ArrayExpress; Q07113; -.
DR   Bgee; Q07113; -.
DR   CleanEx; MM_IGF2R; -.
DR   Genevestigator; Q07113; -.
DR   GermOnline; ENSMUSG00000023830; Mus musculus.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0030139; C:endocytic vesicle; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005641; C:nuclear envelope lumen; IDA:MGI.
DR   GO; GO:0001948; F:glycoprotein binding; ISS:UniProtKB.
DR   GO; GO:0005537; F:mannose binding; IDA:MGI.
DR   GO; GO:0051219; F:phosphoprotein binding; ISS:UniProtKB.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   InterPro; IPR000479; CIMR.
DR   InterPro; IPR000562; FN_type2_col-bd.
DR   InterPro; IPR013806; Kringle-like.
DR   InterPro; IPR009011; Man6P_isomerase_rcpt-bd.
DR   Gene3D; G3DSA:2.10.10.10; FN2; 1.
DR   Pfam; PF00878; CIMR; 14.
DR   Pfam; PF00040; fn2; 1.
DR   SMART; SM00059; FN2; 1.
DR   SUPFAM; SSF57440; Kringle-like; 1.
DR   SUPFAM; SSF50911; Man6php_recept; 15.
DR   PROSITE; PS00023; FN2_1; 1.
DR   PROSITE; PS51092; FN2_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Disulfide bond; Glycoprotein; Lysosome; Membrane;
KW   Phosphoprotein; Receptor; Repeat; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     35       Potential.
FT   CHAIN        36   2483       Cation-independent mannose-6-phosphate
FT                                receptor.
FT                                /FTId=PRO_0000019230.
FT   TOPO_DOM     36   2295       Lumenal (Potential).
FT   TRANSMEM   2296   2316       Helical; (Potential).
FT   TOPO_DOM   2317   2483       Cytoplasmic (Potential).
FT   REPEAT       35    184       1.
FT   REPEAT      185    339       2.
FT   REPEAT      340    484       3.
FT   REPEAT      485    637       4.
FT   REPEAT      638    776       5.
FT   REPEAT      777    943       6.
FT   REPEAT      945   1092       7.
FT   REPEAT     1093   1236       8.
FT   REPEAT     1237   1377       9.
FT   REPEAT     1378   1525       10.
FT   REPEAT     1526   1659       11.
FT   REPEAT     1660   1813       12.
FT   REPEAT     1814   2001       13.
FT   DOMAIN     1891   1937       Fibronectin type-II.
FT   REPEAT     2002   2130       14.
FT   REPEAT     2158   2282       15.
FT   MOD_RES    2342   2342       N6-acetyllysine (By similarity).
FT   MOD_RES    2393   2393       Phosphoserine.
FT   MOD_RES    2401   2401       Phosphoserine.
FT   MOD_RES    2471   2471       Phosphoserine.
FT   MOD_RES    2476   2476       Phosphoserine.
FT   CARBOHYD    107    107       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    395    395       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    430    430       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    537    537       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    575    575       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    620    620       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    740    740       N-linked (GlcNAc...).
FT   CARBOHYD    864    864       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    944    944       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1157   1157       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1239   1239       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1305   1305       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1358   1358       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1423   1423       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1532   1532       N-linked (GlcNAc...).
FT   CARBOHYD   1649   1649       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1750   1750       N-linked (GlcNAc...).
FT   CARBOHYD   1809   1809       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2078   2078       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2129   2129       N-linked (GlcNAc...) (Potential).
FT   DISULFID   1896   1920       By similarity.
FT   DISULFID   1910   1935       By similarity.
FT   CONFLICT     10     11       PS -> RP (in Ref. 2).
FT   CONFLICT     13     13       Missing (in Ref. 2).
FT   CONFLICT    209    209       D -> V (in Ref. 2; AAA19568).
FT   CONFLICT    456    457       DT -> VS (in Ref. 2).
FT   CONFLICT   1626   1631       TCTLFF -> GSTFFS (in Ref. 6; CAA42940).
FT   CONFLICT   1694   1695       MH -> TC (in Ref. 6; CAA42940).
FT   CONFLICT   1699   1699       C -> R (in Ref. 6; CAA42940).
FT   CONFLICT   1759   1759       C -> Y (in Ref. 2; AAA19568).
FT   CONFLICT   2028   2028       G -> V (in Ref. 6; CAA42940).
FT   CONFLICT   2032   2032       C -> S (in Ref. 6; CAA42940).
SQ   SEQUENCE   2483 AA;  273815 MW;  8F64F6189FD05CD1 CRC64;
     MRAVQLGPVP SGPRVALLPP LLLLLLLAAA GSAQAQAVDL DALCSYTWEA VDSKNNAVYK
     INVCGNVGIS SCGPTSAICM CDLKTENCRS VGDSLLRSSA RSLLEFNTTM GCQPSDSQHR
     IQTSITFLCG KTLGTPEFVT ATDCVHYFEW RTTAACKKDI FKADKEVPCY AFDDKLQKHD
     LNPLIKLNGG YLVDDSDPDT SLFINVCRDI DSLRDPSTQL RVCPAGTAAC LLKGNQAFDV
     GRPKEGLKLL SKDRLVLTYV KEEGEKPDFC NGHSPAVTVT FVCPSERREG TIPKLTAKSN
     CRYEVEWITE YACHRDYLQS ESCSLSSEQH DITIDLSPLA QYGGSPYVSD GREYTFFINV
     CGDTKVSLCN NKEAAVCQEK KADSTQVKIA GRHQNQTLRY SDGDLTLIYS GGDECSSGFQ
     RMSVINFECN KTAGKDGRGE PVFTGEVDCT YFFTWDTKYA CIKEKEDLLC GAINGKKRYD
     LSVLARHSES EQNWEAVDGS QAESEKYFFI NVCHRVLQEG KARNCPEDAA VCAVDKNGSK
     NLGKFVSSPT KEKGHIQLSY TDGDDCGSDK KISTNITLVC KPGDLESAPV LRAARSDGCF
     YEFEWHTAAA CVLSKTEGEN CTVLDAQAGF SFDLSLLTKK NGAYKVETEK YDFYINVCGP
     VSMDPCQSNS GACQVAKSGK SWNLGLSSTK LTYYDGMIQL SYRNGTPYNN EKHTPRATLI
     TFLCDRDAGV GFPEYQEEDN STYNFRWYTS YACPEEPLEC MVTDPSMMEQ YDLSSLVKSE
     GGSGGNWYAM ENSREHVTRR KYYLNVCRPL NPVPGCDRYA SACQMKYENH EGSLAETVSI
     SNLGVAKIGP VVEESGSLLL EYVNGSACTT SDGQLTTYST RIHLVCGRGF MNSHPIFTFN
     WECVVSFLWN TEAACPIQTI TETDQACSIR DPSSGFVFNL SPLNDSAQGH VVLGIGKTFV
     FNICGAMPAC GTVAGKPAYG CEAETQIEDI KDLRPQRPVG MERSLQLSAE GFLTLTYKGS
     SPSDRGTAFI IRFICNDDIY PGAPKFLHQD IDSTRGIRNT YFEFETALAC TPSLVDCQVT
     DPAGNEYDLS ALSMVRKPWT AVDTSAYGKR RHFYLSVCNP LPYIPGCHGI ALGSCMVSED
     NSFNLGVVQI SPQATGNGSL SILYVNGDRC GDQRFSTRIV FECAQTSGSP MFQFVNNCEY
     VFVWRTVEAC PVIREEGDNC QVKDPRHGNL YDLKPLGLND TIVSVGEYTY YLRVCGKLSS
     DVCSAHDGSK AVSSCQEKKG PQGFQKVAGL LSQKLTFENG LLKMNYTGGD TCHKVYQRST
     TIYFYCDRTT QKPVFLKETS DCSYMFEWRT QYACPPFNVT ECSVQDAAGN SIDLSSLSRY
     SDNWEAVTRT GATEHYLINV CKSLSPHAGT EPCPPEAAVC LLNGSKPVNL GKVRDGPQWT
     DGVTVLQYVD GDLCPDKIRR RSTIIRFTCS DNQVNSRPLF ISAVQDCEYT FSWPTPSACP
     VKSNTHDDCQ VTNPSTGHLF DLSSLSGRAG INASYSEKGL VFMSICEENE NCGPGVGACF
     GQTRISVGKA SKRLSYKDQV LQLVYENGSP CPSLSDLRYK SVISFVCRPE AGPTNRPMLI
     SLDKQTCTLF FSWHTPLACE QATECTVRNG SSIIDLSPLI HRTGGYEAYD ESEDDTSDTT
     PDFYINICQP LNPMHGVPCP AGASVCKVPV DGPPIDIGRV TGPPIFNPVA NEVYLNFESS
     THCLADRYMN YTSLITFHCK RGVSMGTPKL IRTNDCDFVF EWETPIVCPD EVKTQGCAVT
     DEQLLYSFNL TSLSTSTFKV TRDARTYSIG VCTAAAGLGQ EGCKDGGVCL LSGNKGASFG
     RLASMQLDYR HQDEAVILSY VNGDPCPPET DDGEPCVFPF IYKGKSYDEC VLEGRAKLWC
     SKTANYDRDH EWGFCRQTNS YRMSAIIFTC DESEDIGRPQ VFSEDRGCEV TFEWKTKVVC
     PPKKMECKFV QKHKTYDLRL LSSLTGSWDF VHEGNSYFIN LCQRVYKGPL DCSERASICK
     KSATGQVQVL GLVHTQKLEV IDETVIVTYS KGYPCGGNKT ASSVIELTCA KTVGRPAFKR
     FDSVSCTYYF YWYSRAACAV RPQEVTMVNG TLTNPVTGKS FSLGEIYFKL FSASGDMRTN
     GDNYLYEIQL SSITSSSYPA CAGANICQVK PNDQHFSRKV GTSDMTKYYV QDGDLDVVFT
     SSSKCGKDKT KSVSSTIFFH CDPLVKDGIP EFSHETADCQ YLFSWYTSAV CPLGVDFEDE
     SAGPEYKGLS ERSQAVGAVL SLLLVALTGC LLALLLHKKE RRETVINKLT SCCRRSSGVS
     YKYSKVSKEE ETDENETEWL MEEIQVPAPR LGKDGQENGH ITTKAVKAEA LSSLHGDDQD
     SEDEVLTVPE VKVHSGRGAE VESSQPLRNP QRKVLKEREG ERLGLVRGEK ARKGKFRPGQ
     RKPTAPAKLV SFHDDSDEDL LHI
//
ID   MTF1_MOUSE              Reviewed;         675 AA.
AC   Q07243;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Metal regulatory transcription factor 1;
DE   AltName: Full=MRE-binding transcription factor;
DE   AltName: Full=Transcription factor MTF-1;
GN   Name=Mtf1; Synonyms=Mtf-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=93223676; PubMed=8467794;
RA   Radtke F., Heuchel R., Georgiev O., Hergersberg M., Gariglio M.,
RA   Dembic Z., Schaffner W.;
RT   "Cloned transcription factor MTF-1 activates the mouse metallothionein
RT   I promoter.";
RL   EMBO J. 12:1355-1362(1993).
RN   [2]
RP   SEQUENCE REVISION.
RA   Radtke F.;
RL   Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Activates the metallothionein I promoter. Binds to the
CC       metal responsive element (MRE).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- SIMILARITY: Contains 6 C2H2-type zinc fingers.
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DR   EMBL; X71327; CAA50470.1; -; mRNA.
DR   IPI; IPI00115095; -.
DR   UniGene; Mm.272397; -.
DR   ProteinModelPortal; Q07243; -.
DR   SMR; Q07243; 91-313.
DR   STRING; Q07243; -.
DR   PhosphoSite; Q07243; -.
DR   PRIDE; Q07243; -.
DR   Ensembl; ENSMUST00000030723; ENSMUSP00000030723; ENSMUSG00000028890.
DR   Ensembl; ENSMUST00000106193; ENSMUSP00000101799; ENSMUSG00000028890.
DR   MGI; MGI:101786; Mtf1.
DR   eggNOG; roNOG08129; -.
DR   HOGENOM; HBG281825; -.
DR   HOVERGEN; HBG006412; -.
DR   InParanoid; Q07243; -.
DR   OrthoDB; EOG43BMP1; -.
DR   PhylomeDB; Q07243; -.
DR   ArrayExpress; Q07243; -.
DR   Bgee; Q07243; -.
DR   Genevestigator; Q07243; -.
DR   GermOnline; ENSMUSG00000028890; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0042156; F:zinc-mediated transcriptional activator activity; IDA:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0046686; P:response to cadmium ion; IMP:MGI.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 6.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 6.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Metal-binding; Nucleus; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    675       Metal regulatory transcription factor 1.
FT                                /FTId=PRO_0000047221.
FT   ZN_FING     139    163       C2H2-type 1.
FT   ZN_FING     169    193       C2H2-type 2.
FT   ZN_FING     199    223       C2H2-type 3.
FT   ZN_FING     228    252       C2H2-type 4.
FT   ZN_FING     258    282       C2H2-type 5.
FT   ZN_FING     288    312       C2H2-type 6.
FT   MOTIF       132    137       Nuclear localization signal (Potential).
FT   COMPBIAS    329    405       Asp-rich (acidic).
FT   COMPBIAS    406    506       Pro-rich.
SQ   SEQUENCE   675 AA;  72633 MW;  2FC27E0727D17FC6 CRC64;
     MGEHSPDDNI IFFKGEEDDL TPHDKMLRFV DDNGLVPSSS GTVYDRTTVL IEQDPGTLED
     DEDDGQCGEP LPFLVEGEEG FLIDQEAMSQ GYVQHIISPD QIHLTINPGS TPMPRNIEGA
     TLTLQSECPE TKRKEVKRYQ CTFEGCPRTY STAGNLRTHQ KTHRGEYTFV CNQEGCGKAF
     LTSYSLRIHV RVHTKEKPFE CDVQGCEKAF NTLYRLKAHQ RLHTGKTFNC ESQGCSKYFT
     TLSDLRKHIR THTGEKPFRC DHDGCGKAFA ASHHLKTHVR THTGERPFFC PSNGCEKTFS
     TQYSLKSHMK GHDNKGTAYS ALPQHNGSED TNHSLYLSEL GLLSTDSELQ ENSSSTQDQD
     LSTISPAIIF ESMFQNSDDP GIQDDPLQTA ALIDSFNGDA ESVIDVPPPA GNSASLSLPL
     VLQSGISEPP QPLLPATAPS APPPAPSLGP GSQPAAFGSP PALLQPPEVP VPHSTQFAAN
     HQEFLPHPQA PPQTIVPGLS VVAGAPASAA TVASAVAAPA PPQSTTEPLP AMVQTLPLGA
     NSVLTNNPTI TITPTPNTAI LQSSLVMGEQ NLQWILNGAT SSPQNQEQIQ QASKVEQVYF
     ATTVPVASGT GSSVQQIGLS VPVIIIKQEE ACQCQCACRD SAKERAAGRR KGCSSPPPPE
     PNPQPPDGPS LQLPP
//
ID   TLE3_MOUSE              Reviewed;         772 AA.
AC   Q08122; Q6PHP0; Q923A4;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 3.
DT   08-MAR-2011, entry version 104.
DE   RecName: Full=Transducin-like enhancer protein 3;
DE   AltName: Full=ESG;
DE   AltName: Full=Grg-3;
GN   Name=Tle3; Synonyms=Esg;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=CD-1;
RX   MEDLINE=93373944; PubMed=8365415;
RX   DOI=10.1111/j.1432-1033.1993.tb18151.x;
RA   Miyasaka H., Choudhury B.K., Hou E.W., Li S.S.-L.;
RT   "Molecular cloning and expression of mouse and human cDNA encoding AES
RT   and ESG proteins with strong similarity to Drosophila enhancer of
RT   split groucho protein.";
RL   Eur. J. Biochem. 216:343-352(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
RP   SPLICING (ISOFORM 3).
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 324-772 (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 42-772 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   INTERACTION WITH LEF1; TCF7; TCF7L1 AND TCF7L2.
RX   MEDLINE=21169341; PubMed=11266540; DOI=10.1093/nar/29.7.1410;
RA   Brantjes H., Roose J., van De Wetering M., Clevers H.;
RT   "All Tcf HMG box transcription factors interact with Groucho-related
RT   co-repressors.";
RL   Nucleic Acids Res. 29:1410-1419(2001).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND THR-328, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Transcriptional corepressor that binds to a number of
CC       transcription factors. Inhibits the transcriptional activation
CC       mediated by CTNNB1 and TCF family members in Wnt signaling. The
CC       effects of full-length TLE family members may be modulated by
CC       association with dominant-negative AES (By similarity). May play
CC       an important role during spermatogenesis.
CC   -!- SUBUNIT: Homooligomer and heterooligomer with other family
CC       members. Binds FOXA2 (By similarity). Binds LEF1, TCF7, TCF7L1 and
CC       TCF7L2.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=3;
CC         IsoId=Q08122-3; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q08122-1; Sequence=VSP_038441;
CC       Name=2;
CC         IsoId=Q08122-2; Sequence=VSP_007025;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q08122-4; Sequence=VSP_038442;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed only in testis.
CC   -!- SIMILARITY: Belongs to the WD repeat Groucho/TLE family.
CC   -!- SIMILARITY: Contains 7 WD repeats.
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DR   EMBL; X73360; CAA51770.1; -; mRNA.
DR   EMBL; AC126672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC006672; AAH06672.1; -; mRNA.
DR   EMBL; BC056465; AAH56465.1; -; mRNA.
DR   EMBL; AK031322; BAC27347.1; -; mRNA.
DR   IPI; IPI00466460; -.
DR   IPI; IPI00468606; -.
DR   IPI; IPI00845626; -.
DR   IPI; IPI00954352; -.
DR   PIR; S35681; S35681.
DR   RefSeq; NP_001077396.1; NM_001083927.1.
DR   RefSeq; NP_033415.2; NM_009389.2.
DR   UniGene; Mm.24255; -.
DR   UniGene; Mm.469199; -.
DR   ProteinModelPortal; Q08122; -.
DR   SMR; Q08122; 443-772.
DR   STRING; Q08122; -.
DR   PhosphoSite; Q08122; -.
DR   PRIDE; Q08122; -.
DR   Ensembl; ENSMUST00000034820; ENSMUSP00000034820; ENSMUSG00000032280.
DR   GeneID; 21887; -.
DR   KEGG; mmu:21887; -.
DR   UCSC; uc009pzp.1; mouse.
DR   CTD; 21887; -.
DR   MGI; MGI:104634; Tle3.
DR   eggNOG; roNOG06474; -.
DR   HOVERGEN; HBG004689; -.
DR   InParanoid; Q08122; -.
DR   OMA; HELDHRE; -.
DR   OrthoDB; EOG4MGS6V; -.
DR   ArrayExpress; Q08122; -.
DR   Bgee; Q08122; -.
DR   Genevestigator; Q08122; -.
DR   GermOnline; ENSMUSG00000032280; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR005617; Groucho/TLE_N.
DR   InterPro; IPR009146; Groucho_enhance.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF03920; TLE_N; 1.
DR   Pfam; PF00400; WD40; 6.
DR   PRINTS; PR01850; GROUCHOFAMLY.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Developmental protein;
KW   Differentiation; Nucleus; Phosphoprotein; Repeat; Repressor;
KW   Spermatogenesis; Transcription; Transcription regulation; WD repeat;
KW   Wnt signaling pathway.
FT   CHAIN         1    772       Transducin-like enhancer protein 3.
FT                                /FTId=PRO_0000051281.
FT   REPEAT      484    522       WD 1.
FT   REPEAT      530    569       WD 2.
FT   REPEAT      574    613       WD 3.
FT   REPEAT      616    655       WD 4.
FT   REPEAT      657    696       WD 5.
FT   REPEAT      698    737       WD 6.
FT   REPEAT      739    771       WD 7.
FT   REGION      199    268       CCN domain.
FT   MOTIF       225    228       Nuclear localization signal (Potential).
FT   COMPBIAS      1    131       Gln-rich.
FT   COMPBIAS    132    198       Gly/Pro-rich.
FT   COMPBIAS    269    451       Pro/Ser-rich.
FT   COMPBIAS    401    409       Poly-Ala.
FT   MOD_RES     201    201       Phosphoserine (By similarity).
FT   MOD_RES     203    203       Phosphoserine.
FT   MOD_RES     205    205       Phosphoserine (By similarity).
FT   MOD_RES     207    207       Phosphoserine (By similarity).
FT   MOD_RES     217    217       Phosphoserine (By similarity).
FT   MOD_RES     240    240       Phosphoserine (By similarity).
FT   MOD_RES     245    245       Phosphoserine (By similarity).
FT   MOD_RES     259    259       Phosphothreonine (By similarity).
FT   MOD_RES     263    263       Phosphoserine (By similarity).
FT   MOD_RES     267    267       Phosphoserine (By similarity).
FT   MOD_RES     285    285       Phosphothreonine (By similarity).
FT   MOD_RES     286    286       Phosphoserine (By similarity).
FT   MOD_RES     289    289       Phosphoserine (By similarity).
FT   MOD_RES     292    292       Phosphoserine (By similarity).
FT   MOD_RES     299    299       Phosphoserine (By similarity).
FT   MOD_RES     311    311       Phosphoserine (By similarity).
FT   MOD_RES     312    312       Phosphothreonine (By similarity).
FT   MOD_RES     317    317       Phosphoserine (By similarity).
FT   MOD_RES     319    319       Phosphothreonine (By similarity).
FT   MOD_RES     321    321       Phosphothreonine (By similarity).
FT   MOD_RES     328    328       Phosphothreonine.
FT   MOD_RES     334    334       Phosphothreonine (By similarity).
FT   MOD_RES     343    343       N6-acetyllysine (By similarity).
FT   MOD_RES     413    413       Phosphoserine (By similarity).
FT   VAR_SEQ       2      8       YPQGRHP -> CPCGLQ (in isoform 1).
FT                                /FTId=VSP_038441.
FT   VAR_SEQ     124    124       G -> GVRGLPNLPLT (in isoform 4).
FT                                /FTId=VSP_038442.
FT   VAR_SEQ     351    353       Missing (in isoform 2).
FT                                /FTId=VSP_007025.
FT   CONFLICT    545    545       R -> G (in Ref. 1; CAA51770).
FT   CONFLICT    559    559       W -> R (in Ref. 4; BAC27347).
SQ   SEQUENCE   772 AA;  83447 MW;  39735F2718A8D27A CRC64;
     MYPQGRHPAP HQPGQPGFKF TVAESCDRIK DEFQFLQAQY HSLKVEYDKL ANEKTEMQRH
     YVMYYEMSYG LNIEMHKQTE IAKRLNTILA QIMPFLSQEH QQQVAQAVER AKQVTMTELN
     AIIGQQQLQA QHLSHATHGP PVQLPPHPSG LQPPGIPPVT GSSSGLLALG ALGSQAHLAV
     KDEKNHHELD HRERESSTNN SVSPSESLRA SEKHRGSADY SMEAKKRKAE EKDSLSRYDS
     DGDKSDDLVV DVSNEDPATP RVSPAHSPPE NGLDKARGLK KDAPTSPASV ASSSSTPSSK
     TKDLGHNDKS STPGLKSNTP TPRNDAPTPG TSTTPGLRSM PGKPPGMDPI GIMASALRTP
     ITLTSSYPAP FAMMSHHEMN GSLTSPSAYA GLHNIPSQMS AAAAAAAAAY GRSPMVSFGA
     VGFDPHPPMR ATGLPSSLAS IPGGKPAYSF HVSADGQMQP VPFPHDALAG PGIPRHARQI
     NTLSHGEVVC AVTISNPTRH VYTGGKGCVK IWDISQPGSK SPISQLDCLN RDNYIRSCKL
     LPDGRTLIVG GEASTLTIWD LASPTPRIKA ELTSSAPACY ALAISPDAKV CFSCCSDGNI
     AVWDLHNQTL VRQFQGHTDG ASCIDISHDG TKLWTGGLDN TVRSWDLREG RQLQQHDFTS
     QIFSLGYCPT GEWLAVGMES SNVEVLHHTK PDKYQLHLHE SCVLSLKFAY CGKWFVSTGK
     DNLLNAWRTP YGASIFQSKE SSSVLSCDIS ADDKYIVTGS GDKKATVYEV IY
//
ID   DMWD_MOUSE              Reviewed;         665 AA.
AC   Q08274;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Dystrophia myotonica WD repeat-containing protein;
DE   AltName: Full=Dystrophia myotonica-containing WD repeat motif protein;
DE   AltName: Full=Protein DMR-N9;
GN   Name=Dmwd; Synonyms=Dm9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv; TISSUE=Brain;
RX   MEDLINE=95360003; PubMed=7633444; DOI=10.1093/hmg/4.5.843;
RA   Jansen G., Baechner D., Coerwinkel M., Wormskamp N., Hameister H.,
RA   Wieringa B.;
RT   "Structural organization and developmental expression pattern of the
RT   mouse WD-repeat gene DMR-N9 immediately upstream of the myotonic
RT   dystrophy locus.";
RL   Hum. Mol. Genet. 4:843-852(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 98-665.
RC   STRAIN=129; TISSUE=Brain;
RX   MEDLINE=93251003; PubMed=1302022; DOI=10.1038/ng0792-261;
RA   Jansen G., Mahadevan M.S., Amemiya C., Wormskamp N., Segers B.,
RA   Hendriks W., O'Hoy K., Baird S., Sabourin L., Lennon G., Jap P.L.,
RA   Iles D., Coerwinkel M., Hofker M., Carrano A.V., de Jong P.J.,
RA   Korneluk R.G., Wieringa B.;
RT   "Characterization of the myotonic dystrophy region predicts multiple
RT   protein isoform-encoding mRNAs.";
RL   Nat. Genet. 1:261-266(1992).
CC   -!- FUNCTION: Could have a regulatory function in meiosis.
CC   -!- TISSUE SPECIFICITY: Ubiquitous low expression in all tissues of
CC       the mouse embryo and enhanced expression in adult brain and
CC       testis.
CC   -!- DEVELOPMENTAL STAGE: Expression is seen very early in
CC       embryogenesis, 9.5 dpc in all parts of the embryo. Mid-gestation
CC       embryos (14.5 dpc) show high expression in all neural tissues such
CC       as telencephalon, retina and spinal cord. In the 16.5 day old
CC       embryo high expression is seen in the neural tissues, like
CC       telencephalon and mesencephalon and in the non-neural tissues,
CC       such as muscle tissues in the tongue and around the ribs. In the
CC       postnatal mouse highest expression is seen in the brain and
CC       testis.
CC   -!- SIMILARITY: Contains 5 WD repeats.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-16 is the initiator.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA86112.1; Type=Erroneous initiation;
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DR   EMBL; Z38011; CAA86112.1; ALT_INIT; Genomic_DNA.
DR   EMBL; Z38012; CAA86112.1; JOINED; Genomic_DNA.
DR   EMBL; Z38013; CAA86112.1; JOINED; Genomic_DNA.
DR   EMBL; Z38015; CAA86112.1; JOINED; Genomic_DNA.
DR   EMBL; S60312; AAC60663.1; -; mRNA.
DR   IPI; IPI00118428; -.
DR   PIR; I58106; I58106.
DR   UniGene; Mm.2852; -.
DR   ProteinModelPortal; Q08274; -.
DR   SMR; Q08274; 280-377, 593-621.
DR   STRING; Q08274; -.
DR   PhosphoSite; Q08274; -.
DR   PRIDE; Q08274; -.
DR   Ensembl; ENSMUST00000032570; ENSMUSP00000032570; ENSMUSG00000030410.
DR   UCSC; uc009fkk.1; mouse.
DR   MGI; MGI:94907; Dmwd.
DR   eggNOG; roNOG12498; -.
DR   GeneTree; ENSGT00390000007686; -.
DR   HOGENOM; HBG315568; -.
DR   HOVERGEN; HBG011270; -.
DR   InParanoid; Q08274; -.
DR   OrthoDB; EOG4PK27M; -.
DR   NextBio; 283795; -.
DR   ArrayExpress; Q08274; -.
DR   Bgee; Q08274; -.
DR   CleanEx; MM_DMWD; -.
DR   Genevestigator; Q08274; -.
DR   GermOnline; ENSMUSG00000030410; Mus musculus.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Repeat; WD repeat.
FT   CHAIN         1    665       Dystrophia myotonica WD repeat-containing
FT                                protein.
FT                                /FTId=PRO_0000050957.
FT   REPEAT      208    248       WD 1.
FT   REPEAT      279    318       WD 2.
FT   REPEAT      321    360       WD 3.
FT   REPEAT      363    445       WD 4.
FT   REPEAT      592    629       WD 5.
FT   MOD_RES     537    537       Phosphoserine (By similarity).
SQ   SEQUENCE   665 AA;  69843 MW;  A53AA9EB41A205FC CRC64;
     MAAGGAEGGP GPSAAMGDCA EIKSQFRTRE GFYKLLPGDA TRRSGPTSAQ TPAPPQPTQP
     PPGPAAASGP GAAGPASSPP PAGPGPGPAL PAVRLSLVRL GDPDGAGEPP STPSGLGAGG
     DRVCFNLGRE LYFYPGCCRS GSQRSIDLNK PIDKRIYKGT QPTCHDFNQF TAATETISLL
     VGFSAGQVQY LDLIKKDTSK LFNEERLIDK TKVTYLKWLP ESESLFLASH ASGHLYLYNV
     SHPCTSTPPQ YSLLKQGEGF AVYAAKSKAP RNPLAKWAVG EGPLNEFAFS PDGRHLACVS
     QDGCLRVFHF DSMLLRGLMK SYFGGLLCVC WSPDGRYVVT GGEDDLVTVW SFTEGRVVAR
     GHGHKSWVNA VAFDPYTTRA EEAASASADG DPSGEEEEPE VTSSDTGAPV SPLPKAGSIT
     YRFGSAGQDT QFCLWDLTED VLSPHPSLAR TRTLPGTPGA TPPASGSSRA GETGAGPLPR
     SLSRSNSLPH PAGGGKAGGP NASMEPGIPF SIGRFATLTL QERRDRGAEK EHKRYHSLGN
     ISRGGSGGNS SNDKLSGPAP RSRLDPAKVL GTALCPRIHE VPLLEPLVCK KIAQERLTVL
     LFLEDCIITA CQEGLICTWA RPGKAFTDEE TEAQAGQASW PRSPSKSVVE GISSQPGSSP
     SGTVV
//
ID   CALB2_MOUSE             Reviewed;         271 AA.
AC   Q08331; Q60964; Q9JM81;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 3.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Calretinin;
DE            Short=CR;
GN   Name=Calb2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Tanaka Y., Taki K., Eguchi N., Kaneko T.;
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 1-31.
RC   STRAIN=129/Sv;
RX   MEDLINE=98047070; PubMed=9387877; DOI=10.1016/S0169-328X(97)00143-5;
RA   Strauss K.I., Kuznicki J., Winsky L., Kawagoe J.I., Hammer M.,
RA   Jacobowitz D.M.;
RT   "The mouse calretinin gene promoter region: structural and functional
RT   components.";
RL   Brain Res. Mol. Brain Res. 49:175-187(1997).
RN   [4]
RP   PROTEIN SEQUENCE OF 27-50; 124-133; 179-189 AND 234-244, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Klug S., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 82-271.
RX   MEDLINE=94077721; PubMed=8255773; DOI=10.1093/nar/21.22.5171;
RA   Ellis J., Rogers J.;
RT   "Design and specificity of hammerhead ribozymes against calretinin
RT   mRNA.";
RL   Nucleic Acids Res. 21:5171-5178(1993).
CC   -!- FUNCTION: Calretinin is a calcium-binding protein which is
CC       abundant in auditory neurons.
CC   -!- SIMILARITY: Belongs to the calbindin family.
CC   -!- SIMILARITY: Contains 6 EF-hand domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; AB037969; BAA90701.1; -; Genomic_DNA.
DR   EMBL; BC017646; AAH17646.1; -; mRNA.
DR   EMBL; U34818; AAA84429.1; -; Genomic_DNA.
DR   EMBL; X73985; CAA52163.1; -; mRNA.
DR   IPI; IPI00119346; -.
DR   PIR; S41476; S41476.
DR   RefSeq; NP_031612.1; NM_007586.1.
DR   UniGene; Mm.2755; -.
DR   ProteinModelPortal; Q08331; -.
DR   SMR; Q08331; 10-268.
DR   STRING; Q08331; -.
DR   PhosphoSite; Q08331; -.
DR   UCD-2DPAGE; Q08331; -.
DR   PRIDE; Q08331; -.
DR   Ensembl; ENSMUST00000003754; ENSMUSP00000003754; ENSMUSG00000003657.
DR   GeneID; 12308; -.
DR   KEGG; mmu:12308; -.
DR   UCSC; uc009nko.1; mouse.
DR   CTD; 12308; -.
DR   MGI; MGI:101914; Calb2.
DR   eggNOG; roNOG08816; -.
DR   HOGENOM; HBG444505; -.
DR   HOVERGEN; HBG000855; -.
DR   InParanoid; Q08331; -.
DR   OMA; SSTEFME; -.
DR   OrthoDB; EOG48SGTQ; -.
DR   NextBio; 280848; -.
DR   ArrayExpress; Q08331; -.
DR   Bgee; Q08331; -.
DR   CleanEx; MM_CALB2; -.
DR   Genevestigator; Q08331; -.
DR   GermOnline; ENSMUSG00000003657; Mus musculus.
DR   GO; GO:0005921; C:gap junction; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   InterPro; IPR018248; EF-hand.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   Pfam; PF00036; efhand; 2.
DR   SMART; SM00054; EFh; 5.
DR   PROSITE; PS00018; EF_HAND_1; 5.
DR   PROSITE; PS50222; EF_HAND_2; 5.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Repeat.
FT   CHAIN         1    271       Calretinin.
FT                                /FTId=PRO_0000073480.
FT   DOMAIN       16     51       EF-hand 1.
FT   DOMAIN       63     98       EF-hand 2.
FT   DOMAIN      107    142       EF-hand 3.
FT   DOMAIN      151    186       EF-hand 4.
FT   DOMAIN      195    230       EF-hand 5.
FT   DOMAIN      235    270       EF-hand 6.
FT   CA_BIND      29     40       1 (Probable).
FT   CA_BIND      76     87       2; possibly ancestral (Probable).
FT   CA_BIND     120    131       3 (Probable).
FT   CA_BIND     164    175       4 (Probable).
FT   CA_BIND     208    219       5 (Probable).
FT   CA_BIND     251    262       6; possibly ancestral (Probable).
SQ   SEQUENCE   271 AA;  31373 MW;  C6376AD7130DAACD CRC64;
     MAGPQQQPPY LHLAELTASQ FLEIWKHFDA DGNGYIEGKE LENFFQELEK ARKGSGMMSK
     SDNFGEKMKE FMQKYDKNSD GKIEMAELAQ ILPTEENFLL CFRQHVGSSA EFMEAWRKYD
     TDRSGYIEAN ELKGFLSDLL KKANRPYDEP KLQEYTQTIL RMFDLNGDGK LGLSEMSRLL
     PVQENFLLKF QGMKLTSEEF NAIFTFYDKD GSGYIDENEL DALLKDLYEK NKKEMNIQQL
     TTYRKSVMSL AEAGKLYRKD LEIVLCSEPP V
//
ID   GATA4_MOUSE             Reviewed;         440 AA.
AC   Q08369; P97491; Q9QZK4;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 3.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Transcription factor GATA-4;
DE   AltName: Full=GATA-binding factor 4;
GN   Name=Gata4; Synonyms=Gata-4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=93204969; PubMed=8455608;
RA   Arceci R.J., King A.A., Simon M.C., Orkin S.H., Wilson D.B.;
RT   "Mouse GATA-4: a retinoic acid-inducible GATA-binding transcription
RT   factor expressed in endodermally derived tissues and heart.";
RL   Mol. Cell. Biol. 13:2235-2246(1993).
RN   [2]
RP   IDENTIFICATION OF PROBABLE FRAMESHIFTS.
RX   MEDLINE=94365018; PubMed=8083222;
RA   Laverriere A.C., Macneill C., Mueller C., Poelmann R.E., Burch J.B.E.,
RA   Evans T.;
RT   "GATA-4/5/6, a subfamily of three transcription factors transcribed in
RT   developing heart and gut.";
RL   J. Biol. Chem. 269:23177-23184(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Morrisey E.E., Parmacek M.S.;
RT   "Murine GATA-4 is expressed in heart and gut tissues.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X DBA/2; TISSUE=Heart;
RA   Katsuoka F., Motohashi H., Yamamoto M.;
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   CHARACTERIZATION.
RX   MEDLINE=95234034; PubMed=7717974;
RA   Bielinska M., Wilson D.B.;
RT   "Regulation of J6 gene expression by transcription factor GATA-4.";
RL   Biochem. J. 307:183-189(1995).
RN   [6]
RP   INTERACTION WITH NFATC4.
RX   PubMed=9568714; DOI=10.1016/S0092-8674(00)81573-1;
RA   Molkentin J.D., Lu J.-R., Antos C.L., Markham B., Richardson J.,
RA   Robbins J., Grant S.R., Olson E.N.;
RT   "A calcineurin-dependent transcriptional pathway for cardiac
RT   hypertrophy.";
RL   Cell 93:215-228(1998).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH NKX2-5.
RX   PubMed=9584153;
RA   Lee Y., Shioi T., Kasahara H., Jobe S.M., Wiese R.J., Markham B.E.,
RA   Izumo S.;
RT   "The cardiac tissue-restricted homeobox protein Csx/Nkx2.5 physically
RT   associates with the zinc finger protein GATA4 and cooperatively
RT   activates atrial natriuretic factor gene expression.";
RL   Mol. Cell. Biol. 18:3120-3129(1998).
RN   [8]
RP   INTERACTION WITH JARID2.
RX   PubMed=15542826; DOI=10.1128/MCB.24.23.10151-10160.2004;
RA   Kim T.-G., Chen J., Sadoshima J., Lee Y.;
RT   "Jumonji represses atrial natriuretic factor gene expression by
RT   inhibiting transcriptional activities of cardiac transcription
RT   factors.";
RL   Mol. Cell. Biol. 24:10151-10160(2004).
RN   [9]
RP   INTERACTION WITH LMCD1.
RX   PubMed=16199866; DOI=10.1128/MCB.25.20.8864-8873.2005;
RA   Rath N., Wang Z., Lu M.M., Morrisey E.E.;
RT   "LMCD1/Dyxin is a novel transcriptional cofactor that restricts GATA6
RT   function by inhibiting DNA binding.";
RL   Mol. Cell. Biol. 25:8864-8873(2005).
CC   -!- FUNCTION: Transcriptional activator. Binds to the consensus
CC       sequence 5'-AGATAG-3'. Regulates the expression of the HSP47/J6
CC       gene in F9 cells. Acts as a transcriptional activator of ANF in
CC       cooperation with NKX2-5.
CC   -!- SUBUNIT: Interacts with ZNF260 (By similarity). Interacts with the
CC       homeobox domain of NKX2-5 through its C-terminal zinc finger. Also
CC       interacts with JARID2 which represses its ability to activate
CC       transcription of ANF. Interacts with NFATC4 and LMCD1.
CC   -!- INTERACTION:
CC       Q62315:Jarid2; NbExp=2; IntAct=EBI-297008, EBI-493592;
CC       P42582:Nkx2-5; NbExp=3; IntAct=EBI-297008, EBI-297021;
CC       Q99593:TBX5 (xeno); NbExp=1; IntAct=EBI-297008, EBI-297043;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Heart, intestine, liver, primative endoderm
CC       and gonads.
CC   -!- INDUCTION: By retinoic acid.
CC   -!- SIMILARITY: Contains 2 GATA-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA37662.1; Type=Frameshift; Positions=6, 40, 69;
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DR   EMBL; M98339; AAA37662.1; ALT_FRAME; mRNA.
DR   EMBL; U85046; AAB42015.1; -; mRNA.
DR   EMBL; AF179424; AAD55266.1; -; mRNA.
DR   IPI; IPI00894774; -.
DR   PIR; A48099; A48099.
DR   RefSeq; NP_032118.2; NM_008092.3.
DR   UniGene; Mm.247669; -.
DR   ProteinModelPortal; Q08369; -.
DR   SMR; Q08369; 212-250, 264-319.
DR   DIP; DIP-33032N; -.
DR   IntAct; Q08369; 9.
DR   MINT; MINT-206005; -.
DR   STRING; Q08369; -.
DR   PhosphoSite; Q08369; -.
DR   PRIDE; Q08369; -.
DR   Ensembl; ENSMUST00000118022; ENSMUSP00000113891; ENSMUSG00000021944.
DR   GeneID; 14463; -.
DR   KEGG; mmu:14463; -.
DR   CTD; 14463; -.
DR   MGI; MGI:95664; Gata4.
DR   eggNOG; roNOG11790; -.
DR   HOVERGEN; HBG051703; -.
DR   OrthoDB; EOG4PK28S; -.
DR   ArrayExpress; Q08369; -.
DR   Bgee; Q08369; -.
DR   CleanEx; MM_GATA4; -.
DR   Genevestigator; Q08369; -.
DR   GermOnline; ENSMUSG00000021944; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0003705; F:sequence-specific enhancer binding RNA polymerase II transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0003704; F:specific RNA polymerase II transcription factor activity; IDA:MGI.
DR   GO; GO:0016563; F:transcription activator activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0003289; P:atrial septum primum morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0055007; P:cardiac muscle cell differentiation; IEP:BHF-UCL.
DR   GO; GO:0003215; P:cardiac right ventricle morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0007267; P:cell-cell signaling; IMP:MGI.
DR   GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IDA:MGI.
DR   GO; GO:0060540; P:diaphragm morphogenesis; TAS:BHF-UCL.
DR   GO; GO:0048557; P:embryonic digestive tract morphogenesis; IMP:MGI.
DR   GO; GO:0048617; P:embryonic foregut morphogenesis; IMP:MGI.
DR   GO; GO:0035054; P:embryonic heart tube anterior/posterior pattern formation; IMP:MGI.
DR   GO; GO:0003197; P:endocardial cushion development; IMP:BHF-UCL.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
DR   GO; GO:0001947; P:heart looping; IMP:BHF-UCL.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0060425; P:lung morphogenesis; TAS:BHF-UCL.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IDA:BHF-UCL.
DR   GO; GO:0051891; P:positive regulation of cardioblast differentiation; IEP:BHF-UCL.
DR   GO; GO:0010552; P:positive regulation of gene-specific transcription from RNA polymerase II promoter; IMP:BHF-UCL.
DR   GO; GO:0010575; P:positive regulation vascular endothelial growth factor production; IDA:BHF-UCL.
DR   GO; GO:0060043; P:regulation of cardiac muscle cell proliferation; IMP:MGI.
DR   GO; GO:0043627; P:response to estrogen stimulus; IDA:MGI.
DR   GO; GO:0032526; P:response to retinoic acid; IDA:BHF-UCL.
DR   GO; GO:0060395; P:SMAD protein signal transduction; IDA:MGI.
DR   GO; GO:0003281; P:ventricular septum development; IMP:BHF-UCL.
DR   InterPro; IPR008013; GATA_N.
DR   InterPro; IPR016375; TF_GATA_4/5/6.
DR   InterPro; IPR000679; Znf_GATA.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   Gene3D; G3DSA:3.30.50.10; Znf_NHR/GATA; 2.
DR   Pfam; PF00320; GATA; 2.
DR   Pfam; PF05349; GATA-N; 1.
DR   PIRSF; PIRSF003028; TF_GATA_4/5/6; 1.
DR   PRINTS; PR00619; GATAZNFINGER.
DR   SMART; SM00401; ZnF_GATA; 2.
DR   PROSITE; PS00344; GATA_ZN_FINGER_1; 2.
DR   PROSITE; PS50114; GATA_ZN_FINGER_2; 2.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    440       Transcription factor GATA-4.
FT                                /FTId=PRO_0000083414.
FT   ZN_FING     216    240       GATA-type 1.
FT   ZN_FING     270    294       GATA-type 2.
FT   COMPBIAS    118    126       Poly-Ala.
FT   COMPBIAS    174    181       Poly-Ala.
FT   COMPBIAS    275    279       Poly-Thr.
FT   COMPBIAS    354    359       Poly-Ser.
FT   MOD_RES     404    404       Phosphoserine (By similarity).
FT   CONFLICT     29     30       SA -> RT (in Ref. 1; AAA37662).
FT   CONFLICT    385    401       SVCVRPRALHPSSAVCS -> FSSVSGHGPSIHPVLSAL
FT                                (in Ref. 4; AAD55266).
SQ   SEQUENCE   440 AA;  44543 MW;  BBCC694AB5AB86DC CRC64;
     MYQSLAMAAN HGPPPGAYEA GGPGAFMHSA GAASSPVYVP TPRVPSSVLG LSYLQGGGSA
     AAAGTTSGGS SGAGPSGAGP GTQQGSPGWS QAGAEGAAYT PPPVSPRFSF PGTTGSLAAA
     AAAAAAREAA AYGSGGGAAG AGLAGREQYG RPGFAGSYSS PYPAYMADVG ASWAAAAAAS
     AGPFDSPVLH SLPGRANPGR HPNLDMFDDF SEGRECVNCG AMSTPLWRRD GTGHYLCNAC
     GLYHKMNGIN RPLIKPQRRL SASRRVGLSC ANCQTTTTTL WRRNAEGEPV CNACGLYMKL
     HGVPRPLAMR KEGIQTRKRK PKNLNKSKTP AGPAGETLPP SSGASSGNSS NATSSSSSSE
     EMRPIKTEPG LSSHYGHSSS MSQTSVCVRP RALHPSSAVC SKLSPQGYAS PVTQTSQASS
     KQDSWNSLVL ADSHGDIITA
//
ID   KCMA1_MOUSE             Reviewed;        1209 AA.
AC   Q08460; Q64703; Q8VHF1; Q9R196;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   08-MAR-2011, entry version 106.
DE   RecName: Full=Calcium-activated potassium channel subunit alpha-1;
DE   AltName: Full=BK channel;
DE   AltName: Full=BKCA alpha;
DE   AltName: Full=Calcium-activated potassium channel, subfamily M subunit alpha-1;
DE   AltName: Full=K(VCA)alpha;
DE   AltName: Full=KCa1.1;
DE   AltName: Full=Maxi K channel;
DE            Short=MaxiK;
DE   AltName: Full=Slo-alpha;
DE   AltName: Full=Slo1;
DE            Short=mSlo1;
DE   AltName: Full=Slowpoke homolog;
DE            Short=Slo homolog;
DE            Short=mSlo;
GN   Name=Kcnma1; Synonyms=Kcnma;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=95078823; PubMed=7987297; DOI=10.1093/hmg/3.8.1239;
RA   Pallanck L., Ganetzky B.;
RT   "Cloning and characterization of human and mouse homologs of the
RT   Drosophila calcium-activated potassium channel gene, slowpoke.";
RL   Hum. Mol. Genet. 3:1239-1243(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 26-1209 (ISOFORMS 2 AND 5), AND
RP   FUNCTION.
RC   TISSUE=Brain;
RX   MEDLINE=93318148; PubMed=7687074; DOI=10.1126/science.7687074;
RA   Butler A., Tsunoda S., McCobb D.P., Wei A., Salkoff L.;
RT   "mSlo, a complex mouse gene encoding 'maxi' calcium-activated
RT   potassium channels.";
RL   Science 261:221-224(1993).
RN   [3]
RP   MUTAGENESIS OF VAL-151.
RX   PubMed=16341213; DOI=10.1038/nn1602;
RA   Liu J., Asuncion-Chin M., Liu P., Dopico A.M.;
RT   "CaM kinase II phosphorylation of slo Thr107 regulates activity and
RT   ethanol responses of BK channels.";
RL   Nat. Neurosci. 9:41-49(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 66-1209 (ISOFORM 4).
RC   TISSUE=Pituitary anterior lobe;
RX   MEDLINE=99445262; PubMed=10517674; DOI=10.1210/me.13.10.1728;
RA   Shipston M.J., Duncan R.R., Clark A.G., Antoni F.A., Tian L.;
RT   "Molecular components of large conductance calcium-activated potassium
RT   (BK) channels in mouse pituitary corticotropes.";
RL   Mol. Endocrinol. 13:1728-1737(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 66-1209 (ISOFORM 3).
RC   STRAIN=NIH Swiss; TISSUE=Parotid gland;
RX   PubMed=12388098; DOI=10.1152/ajpcell.00044.2002;
RA   Nehrke K., Quinn C.C., Begenisich T.;
RT   "Molecular identification of Ca2+-activated K+ channels in parotid
RT   acinar cells.";
RL   Am. J. Physiol. 284:C535-C546(2003).
RN   [6]
RP   INTERACTION WITH KCNMB3.
RX   MEDLINE=20266164; PubMed=10804197;
RA   Weiger T.M., Holmqvist M.H., Levitan I.B., Clark F.T., Sprague S.,
RA   Huang W.-J., Ge P., Wang C., Lawson D., Jurman M.E., Glucksmann M.A.,
RA   Silos-Santiago I., DiStefano P.S., Curtis R.;
RT   "A novel nervous system beta subunit that downregulates human large
RT   conductance calcium-dependent potassium channels.";
RL   J. Neurosci. 20:3563-3570(2000).
RN   [7]
RP   MUTAGENESIS OF ARG-272; ARG-278; GLU-284 AND GLN-287.
RX   PubMed=11112549; DOI=10.1021/bi001509+;
RA   Cui J., Aldrich R.W.;
RT   "Allosteric linkage between voltage and Ca(2+)-dependent activation of
RT   BK-type mslo1 K(+) channels.";
RL   Biochemistry 39:15612-15619(2000).
RN   [8]
RP   CALCIUM-BINDING, AND MUTAGENESIS OF 992-ASP--ASP-996.
RX   PubMed=12149279;
RA   Bao L., Rapin A.M., Holmstrand E.C., Cox D.H.;
RT   "Elimination of the BK(Ca) channel's high-affinity Ca(2+)
RT   sensitivity.";
RL   J. Gen. Physiol. 120:173-189(2002).
RN   [9]
RP   MAGNESIUM-BINDING, AND MUTAGENESIS OF GLU-439; HIS-444; THR-461;
RP   GLN-462 AND GLU-464.
RX   PubMed=12192410; DOI=10.1038/nature00941;
RA   Shi J., Krishnamoorthy G., Yang Y., Hu L., Chaturvedi N., Harilal D.,
RA   Qin J., Cui J.;
RT   "Mechanism of magnesium activation of calcium-activated potassium
RT   channels.";
RL   Nature 418:876-880(2002).
RN   [10]
RP   CALCIUM-BINDING, MAGNESIUM-BINDING, AND MUTAGENESIS OF ASP-427;
RP   ASP-432; ASP-434 AND GLU-464.
RX   PubMed=12192411; DOI=10.1038/nature00956;
RA   Xia X.-M., Zeng X., Lingle C.J.;
RT   "Multiple regulatory sites in large-conductance calcium-activated
RT   potassium channels.";
RL   Nature 418:880-884(2002).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-711 AND THR-1061, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Potassium channel activated by both membrane
CC       depolarization or increase in cytosolic Ca(2+) that mediates
CC       export of K(+). It is also activated by the concentration of
CC       cytosolic Mg(2+). Its activation dampens the excitatory events
CC       that elevate the cytosolic Ca(2+) concentration and/or depolarize
CC       the cell membrane. It therefore contributes to repolarization of
CC       the membrane potential. Plays a key role in controlling
CC       excitability in a number of systems, such as regulation of the
CC       contraction of smooth muscle, the tuning of hair cells in the
CC       cochlea, regulation of transmitter release, and innate immunity.
CC       In smooth muscles, its activation by high level of Ca(2+), caused
CC       by ryanodine receptors in the sarcoplasmic reticulum, regulates
CC       the membrane potential. In cochlea cells, its number and kinetic
CC       properties partly determine the characteristic frequency of each
CC       hair cell and thereby helps to establish a tonotopic map. Kinetics
CC       of KCNMA1 channels are determined by alternative splicing,
CC       phosphorylation status and its combination with modulating beta
CC       subunits. Highly sensitive to both iberiotoxin (IbTx) and
CC       charybdotoxin (CTX).
CC   -!- ENZYME REGULATION: Ethanol and carbon monoxide-bound heme increase
CC       channel activation. Heme inhibits channel activation (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with LRRC26 (By similarity). Homotetramer;
CC       which constitutes the calcium-activated potassium channel.
CC       Interacts with beta subunits KCNMB1, KCNMB2, KCNMB3 and KCNMB4.
CC       Beta subunits are accessory, and modulate its activity.
CC   -!- INTERACTION:
CC       P63260:Actg1; NbExp=1; IntAct=EBI-1633915, EBI-351301;
CC       P48036:Anxa5; NbExp=1; IntAct=EBI-1633915, EBI-1184119;
CC       Q00623:Apoa1; NbExp=1; IntAct=EBI-1633915, EBI-1634106;
CC       P62204:Calm1; NbExp=1; IntAct=EBI-1633915, EBI-397460;
CC       P16858:Gapdh; NbExp=1; IntAct=EBI-1633915, EBI-444871;
CC       P84075:Hpca; NbExp=1; IntAct=EBI-1633915, EBI-2128343;
CC       O88952:Lin7c; NbExp=1; IntAct=EBI-1633915, EBI-821316;
CC       P27573:Mpz; NbExp=1; IntAct=EBI-1633915, EBI-1634589;
CC       P61982:Ywhag; NbExp=1; IntAct=EBI-1633915, EBI-359843;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC         Comment=May be partially controlled by hormonal stress.
CC         Additional isoforms seem to exist;
CC       Name=1;
CC         IsoId=Q08460-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q08460-2; Sequence=VSP_009960, VSP_009961, VSP_009962,
CC                                  VSP_009964, VSP_009965;
CC       Name=3;
CC         IsoId=Q08460-3; Sequence=VSP_009961, VSP_009964;
CC       Name=4; Synonyms=STREX-1;
CC         IsoId=Q08460-4; Sequence=VSP_009961, VSP_009963, VSP_009964;
CC       Name=5;
CC         IsoId=Q08460-5; Sequence=VSP_009959;
CC   -!- DOMAIN: The S0 segment is essential for the modulation by the
CC       accessory beta subunits KCNMB1, KCNMB2, KCNMB3 and KCNMB4.
CC   -!- DOMAIN: The S4 segment, which is characterized by a series of
CC       positively charged amino acids at every third position, is part of
CC       the voltage-sensor.
CC   -!- DOMAIN: The pore-forming domain (also referred as P region) is
CC       imbedded into the membrane, and forms the selectivity filter of
CC       the pore. It contains the signature sequence of potassium channels
CC       that displays selectivity to potassium.
CC   -!- DOMAIN: The RCK N-terminal domain mediates the
CC       homotetramerization, thereby promoting the assembly of monomers
CC       into functional potassium channel. It includes binding sites for
CC       Ca(2+) and Mg(2+).
CC   -!- DOMAIN: The calcium bowl constitutes one of the Ca(2+) sensors and
CC       probably acts as a Ca(2+)-binding site. There are however other
CC       Ca(2+) sensors regions required for activation of the channel.
CC   -!- DOMAIN: The heme-binding motif mediates inhibition of channel
CC       activation by heme. Carbon monoxide-bound heme leads to increased
CC       channel activation (By similarity).
CC   -!- PTM: Phosphorylated (Probable). Phosphorylation by kinases such as
CC       PKA and/or PKG. In smooth muscles, phosphorylation affects its
CC       activity.
CC   -!- MISCELLANEOUS: The protein was initially thought to contain two
CC       functionally distinct parts: The core channel (from the N-terminus
CC       to the S9 segment) that mediates the channel activity, and the
CC       cytoplasmic tail (from the S9 segment to the C-terminus) that
CC       mediates the calcium sensing. The situation is however more
CC       complex, since the core channel contains binding sites for Ca(2+)
CC       and Mg(2+).
CC   -!- SIMILARITY: Belongs to the potassium channel family. Calcium-
CC       activated (TC 1.A.1.3) subfamily. KCa1.1/KCNMA1 sub-subfamily.
CC   -!- SIMILARITY: Contains 1 RCK N-terminal domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA50215.1; Type=Erroneous initiation;
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DR   EMBL; U09383; AAA50215.1; ALT_INIT; mRNA.
DR   EMBL; L16912; AAA39746.1; -; mRNA.
DR   EMBL; AF156674; AAD49225.1; -; mRNA.
DR   EMBL; AF465244; AAL69971.1; -; mRNA.
DR   IPI; IPI00120643; -.
DR   IPI; IPI00410901; -.
DR   IPI; IPI00410903; -.
DR   IPI; IPI00410904; -.
DR   IPI; IPI00410905; -.
DR   PIR; A48206; A48206.
DR   PIR; I49017; I49017.
DR   RefSeq; NP_034740.2; NM_010610.2.
DR   UniGene; Mm.343607; -.
DR   UniGene; Mm.458374; -.
DR   ProteinModelPortal; Q08460; -.
DR   SMR; Q08460; 308-1155.
DR   DIP; DIP-46325N; -.
DR   IntAct; Q08460; 195.
DR   MINT; MINT-1203219; -.
DR   STRING; Q08460; -.
DR   PhosphoSite; Q08460; -.
DR   PRIDE; Q08460; -.
DR   Ensembl; ENSMUST00000065788; ENSMUSP00000065293; ENSMUSG00000063142.
DR   Ensembl; ENSMUST00000074983; ENSMUSP00000074511; ENSMUSG00000063142.
DR   Ensembl; ENSMUST00000112423; ENSMUSP00000108042; ENSMUSG00000063142.
DR   GeneID; 16531; -.
DR   KEGG; mmu:16531; -.
DR   UCSC; uc007sme.1; mouse.
DR   UCSC; uc007smh.1; mouse.
DR   UCSC; uc007smi.1; mouse.
DR   CTD; 16531; -.
DR   MGI; MGI:99923; Kcnma1.
DR   eggNOG; roNOG10812; -.
DR   GeneTree; ENSGT00530000063026; -.
DR   HOVERGEN; HBG052222; -.
DR   OrthoDB; EOG4QFWCD; -.
DR   NextBio; 289945; -.
DR   ArrayExpress; Q08460; -.
DR   Bgee; Q08460; -.
DR   Genevestigator; Q08460; -.
DR   GermOnline; ENSMUSG00000063142; Mus musculus.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR   GO; GO:0043195; C:terminal button; IDA:MGI.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IGI:MGI.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0060072; F:large conductance calcium-activated potassium channel activity; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:MGI.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0042491; P:auditory receptor cell differentiation; IMP:MGI.
DR   GO; GO:0048469; P:cell maturation; IMP:MGI.
DR   GO; GO:0060082; P:eye blink reflex; IMP:MGI.
DR   GO; GO:0045475; P:locomotor rhythm; IMP:MGI.
DR   GO; GO:0045794; P:negative regulation of cell volume; IMP:MGI.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR   GO; GO:0051260; P:protein homooligomerization; IDA:MGI.
DR   GO; GO:0019228; P:regulation of action potential in neuron; IMP:MGI.
DR   GO; GO:0032344; P:regulation of aldosterone metabolic process; IMP:MGI.
DR   GO; GO:0060087; P:relaxation of vascular smooth muscle; IMP:MGI.
DR   GO; GO:0001666; P:response to hypoxia; IDA:MGI.
DR   GO; GO:0046541; P:saliva secretion; IGI:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR   GO; GO:0060083; P:smooth muscle contraction involved in micturition; IMP:MGI.
DR   GO; GO:0007268; P:synaptic transmission; IMP:MGI.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003929; K_chnl_Ca-activ_BK_asu.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR003148; RCK_N.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF03493; BK_channel_a; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02254; TrkA_N; 1.
DR   PRINTS; PR01449; BKCHANNELA.
DR   PRINTS; PR00169; KCHANNEL.
DR   PROSITE; PS51201; RCK_N; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Ion transport; Ionic channel;
KW   Magnesium; Membrane; Metal-binding; Phosphoprotein; Potassium;
KW   Potassium channel; Potassium transport; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1   1209       Calcium-activated potassium channel
FT                                subunit alpha-1.
FT                                /FTId=PRO_0000054134.
FT   TOPO_DOM      1     86       Extracellular (Potential).
FT   TRANSMEM     87    107       Helical; Name=Segment S0; (Potential).
FT   TOPO_DOM    108    178       Cytoplasmic (Potential).
FT   TRANSMEM    179    199       Helical; Name=Segment S1; (Potential).
FT   TOPO_DOM    200    214       Extracellular (Potential).
FT   TRANSMEM    215    235       Helical; Name=Segment S2; (Potential).
FT   TOPO_DOM    236    239       Cytoplasmic (Potential).
FT   TRANSMEM    240    260       Helical; Name=Segment S3; (Potential).
FT   TOPO_DOM    261    264       Extracellular (Potential).
FT   TRANSMEM    265    285       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TOPO_DOM    286    300       Cytoplasmic (Potential).
FT   TRANSMEM    301    321       Helical; Name=Segment S5; (Potential).
FT   TOPO_DOM    322    335       Extracellular (Potential).
FT   INTRAMEM    336    358       Pore-forming; Name=P region; (Potential).
FT   TOPO_DOM    359    367       Extracellular (Potential).
FT   TRANSMEM    368    388       Helical; Name=Segment S6; (Potential).
FT   TOPO_DOM    389   1209       Cytoplasmic (Potential).
FT   DOMAIN      415    558       RCK N-terminal.
FT   REGION      556    576       Segment S7.
FT   REGION      613    633       Segment S8.
FT   REGION      681    685       Heme-binding motif.
FT   REGION      783    803       Segment S9.
FT   REGION     1005   1025       Segment S10.
FT   MOTIF       352    355       Selectivity for potassium.
FT   MOTIF       976    998       Calcium bowl.
FT   COMPBIAS      4     10       Poly-Gly.
FT   COMPBIAS     13     23       Poly-Gly.
FT   COMPBIAS     40     60       Poly-Ser.
FT   METAL       439    439       Magnesium (Probable).
FT   METAL       462    462       Magnesium (Probable).
FT   METAL       464    464       Magnesium (Probable).
FT   MOD_RES     569    569       Phosphoserine (By similarity).
FT   MOD_RES     711    711       Phosphoserine.
FT   MOD_RES    1059   1059       Phosphotyrosine (By similarity).
FT   MOD_RES    1061   1061       Phosphothreonine.
FT   VAR_SEQ       1     65       Missing (in isoform 5).
FT                                /FTId=VSP_009959.
FT   VAR_SEQ       1     50       MANGGGGGGGSSGGGGGGGGGSGLRMSSNIHANNLSLDASS
FT                                SSSSSSSSS -> MELEHPKSPPYP (in isoform 2).
FT                                /FTId=VSP_009960.
FT   VAR_SEQ     643    646       Missing (in isoform 2, isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_009961.
FT   VAR_SEQ     702    702       L -> LIYF (in isoform 2).
FT                                /FTId=VSP_009962.
FT   VAR_SEQ     702    702       L -> PKMSIYKRMRRACCFDCGRSERDCSCMSGRVRGNVD
FT                                TLERTFPLSSVSVNDCSTSFRAF (in isoform 4).
FT                                /FTId=VSP_009963.
FT   VAR_SEQ     948    974       Missing (in isoform 2, isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_009964.
FT   VAR_SEQ    1203   1209       RKEMVYR -> ATRMTRMGQAEKKWFTDEPDNAYPRNIQIK
FT                                PMSTHMANQINQYKSTSSLIPPIREVEDEC (in
FT                                isoform 2).
FT                                /FTId=VSP_009965.
FT   MUTAGEN     151    151       V->T: Loss of phosphorylation-independent
FT                                activation of channel activity by
FT                                ethanol. CaMK2-dependent phosphorylation
FT                                leads to populations of partially
FT                                phosphorylated tetramers with a range of
FT                                responses to ethanol from activation to
FT                                inhibition.
FT   MUTAGEN     272    272       R->Q: Alters the voltage-dependent
FT                                gating.
FT   MUTAGEN     278    278       R->Q: Alters the voltage-dependent
FT                                gating.
FT   MUTAGEN     284    284       E->R: Alters the voltage-dependent
FT                                gating; when associated with R-287.
FT   MUTAGEN     287    287       Q->R: Alters the voltage-dependent
FT                                gating; when associated with K-284.
FT   MUTAGEN     427    427       D->A: Does not affect sensitivity to
FT                                Ca(2+).
FT   MUTAGEN     432    432       D->A: Reduced sensitivity to Ca(2+).
FT   MUTAGEN     434    434       D->A: Does not affect sensitivity to
FT                                Ca(2+).
FT   MUTAGEN     439    439       E->A: Abolishes sensitivity to Mg(2+),
FT                                but not sensitivity to Ca(2+).
FT   MUTAGEN     444    444       H->G: Reduces sensitivity to Mg(2+), but
FT                                not sensitivity to Ca(2+).
FT   MUTAGEN     461    461       T->A: Reduces sensitivity to Mg(2+), but
FT                                not sensitivity to Ca(2+).
FT   MUTAGEN     462    462       Q->C: Reduces sensitivity to Mg(2+), but
FT                                not sensitivity to Ca(2+).
FT   MUTAGEN     464    464       E->D,A: Remains sensitive to Mg(2+).
FT   MUTAGEN     464    464       E->N: Abolishes sensitivity to Mg(2+),
FT                                but not sensitivity to Ca(2+).
FT   MUTAGEN     992    996       DDDPD->AAAAA: Alters calcium binding.
SQ   SEQUENCE   1209 AA;  134396 MW;  9E07ABF5DCFA62DF CRC64;
     MANGGGGGGG SSGGGGGGGG GSGLRMSSNI HANNLSLDAS SSSSSSSSSS SSSSSSSSSS
     VHEPKMDALI IPVTMEVPCD SRGQRMWWAF LASSMVTFFG GLFIILLWRT LKYLWTVCCH
     CGGKTKEAQK INNGSSQADG TLKPVDEKEE VVAAEVGWMT SVKDWAGVMI SAQTLTGRVL
     VVLVFALSIG ALVIYFIDSS NPIESCQNFY KDFTLQIDMA FNVFFLLYFG LRFIAANDKL
     WFWLEVNSVV DFFTVPPVFV SVYLNRSWLG LRFLRALRLI QFSEILQFLN ILKTSNSIKL
     VNLLSIFIST WLTAAGFIHL VENSGDPWEN FQNNQALTYW ECVYLLMVTM STVGYGDVYA
     KTTLGRLFMV FFILGGLAMF ASYVPEIIEL IGNRKKYGGS YSAVSGRKHI VVCGHITLES
     VSNFLKDFLH KDRDDVNVEI VFLHNISPNL ELEALFKRHF TQVEFYQGSV LNPHDLARVK
     IESADACLIL ANKYCADPDA EDASNIMRVI SIKNYHPKIR IITQMLQYHN KAHLLNIPSW
     NWKEGDDAIC LAELKLGFIA QSCLAQGLST MLANLFSMRS FIKIEEDTWQ KYYLEGVSNE
     MYTEYLSSAF VGLSFPTVCE LCFVKLKLLM IAIEYKSANR ESRSRKRILI NPGNHLKIQE
     GTLGFFIASD AKEVKRAFFY CKACHDDVTD PKRIKKCGCR RLEDEQPPTL SPKKKQRNGG
     MRNSPNTSPK LMRHDPLLIP GNDQIDNMDS NVKKYDSTGM FHWCAPKEIE KVILTRSEAA
     MTVLSGHVVV CIFGDVSSAL IGLRNLVMPL RASNFHYHEL KHIVFVGSIE YLKREWETLH
     NFPKVSILPG TPLSRADLRA VNINLCDMCV ILSANQNNID DTSLQDKECI LASLNIKSMQ
     FDDSIGVLQA NSQGFTPPGM DRSSPDNSPV HGMLRQPSIT TGVNIPIITE LAKPGKLPLV
     SVNQEKNSGT HILMITELVN DTNVQFLDQD DDDDPDTELY LTQPFACGTA FAVSVLDSLM
     SATYFNDNIL TLIRTLVTGG ATPELEALIA EENALRGGYS TPQTLANRDR CRVAQLALLD
     GPFADLGDGG CYGDLFCKAL KTYNMLCFGI YRLRDAHLST PSQCTKRYVI TNPPYEFELV
     PTDLIFCLMQ FDHNAGQSRA SLSHSSHSSQ SSSKKSSSVH SIPSTANRPN RPKSRESRDK
     QNRKEMVYR
//
ID   EPS8_MOUSE              Reviewed;         821 AA.
AC   Q08509;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Epidermal growth factor receptor kinase substrate 8;
GN   Name=Eps8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94008987; PubMed=8404850;
RA   Fazioli F., Minichiello L., Matoska V., Castagnino P., Miki T.,
RA   Wong W.T., di Fiore P.P.;
RT   "Eps8, a substrate for the epidermal growth factor receptor kinase,
RT   enhances EGF-dependent mitogenic signals.";
RL   EMBO J. 12:3799-3808(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH SHB.
RX   PubMed=7537362;
RA   Karlsson T., Songyang Z., Landgren E., Lavergne C., Di Fiore P.P.,
RA   Anafi M., Pawson T., Cantley L.C., Claesson-Welsh L., Welsh M.;
RT   "Molecular interactions of the Src homology 2 domain protein Shb with
RT   phosphotyrosine residues, tyrosine kinase receptors and Src homology 3
RT   domain proteins.";
RL   Oncogene 10:1475-1483(1995).
RN   [4]
RP   INTERACTION WITH LANCL1.
RX   PubMed=19528316; DOI=10.1101/gad.1789209;
RA   Zhang W., Wang L., Liu Y., Xu J., Zhu G., Cang H., Li X., Bartlam M.,
RA   Hensley K., Li G., Rao Z., Zhang X.C.;
RT   "Structure of human lanthionine synthetase C-like protein 1 and its
RT   interaction with Eps8 and glutathione.";
RL   Genes Dev. 23:1387-1392(2009).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 532-591, AND
RP   HOMODIMERIZATION.
RX   MEDLINE=97448677; PubMed=9303002; DOI=10.1038/nsb0997-739;
RA   Kishan K.V.R., Scita G., Wong W.T., di Fiore P.P., Newcomer M.E.;
RT   "The SH3 domain of Eps8 exists as a novel intertwined dimer.";
RL   Nat. Struct. Biol. 4:739-743(1997).
CC   -!- FUNCTION: Upon binding to EGF receptor enhances EGF-dependent
CC       mitogenic signals. Can bind multiple cellular targets.
CC   -!- SUBUNIT: Homodimer. Interacts with BAIAP2 (By similarity).
CC       Interacts with SHB and LANCL1.
CC   -!- INTERACTION:
CC       Q8IZP0:ABI1 (xeno); NbExp=2; IntAct=EBI-375596, EBI-375446;
CC       Q8CBW3:Abi1; NbExp=1; IntAct=EBI-375596, EBI-375511;
CC       Q9UQB8:BAIAP2 (xeno); NbExp=6; IntAct=EBI-375596, EBI-525456;
CC   -!- DOMAIN: The SH3 domain mediates interaction with SHB (By
CC       similarity).
CC   -!- PTM: Phosphorylated by several receptor tyrosine kinases.
CC   -!- SIMILARITY: Belongs to the EPS8 family.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; L21671; AAA16358.1; -; mRNA.
DR   EMBL; BC016890; AAH16890.1; -; mRNA.
DR   IPI; IPI00622390; -.
DR   PIR; S39983; S39983.
DR   UniGene; Mm.235346; -.
DR   UniGene; Mm.412332; -.
DR   PDB; 1AOJ; X-ray; 2.50 A; A/B=532-591.
DR   PDB; 1I07; X-ray; 1.80 A; A/B=532-591.
DR   PDB; 1I0C; X-ray; 2.00 A; A/B=532-591.
DR   PDBsum; 1AOJ; -.
DR   PDBsum; 1I07; -.
DR   PDBsum; 1I0C; -.
DR   ProteinModelPortal; Q08509; -.
DR   SMR; Q08509; 59-188, 532-590, 698-783.
DR   DIP; DIP-32858N; -.
DR   IntAct; Q08509; 12.
DR   STRING; Q08509; -.
DR   PhosphoSite; Q08509; -.
DR   PRIDE; Q08509; -.
DR   Ensembl; ENSMUST00000058210; ENSMUSP00000052776; ENSMUSG00000015766.
DR   Ensembl; ENSMUST00000100841; ENSMUSP00000098402; ENSMUSG00000015766.
DR   Ensembl; ENSMUST00000111878; ENSMUSP00000107509; ENSMUSG00000015766.
DR   Ensembl; ENSMUST00000111880; ENSMUSP00000107511; ENSMUSG00000015766.
DR   MGI; MGI:104684; Eps8.
DR   eggNOG; roNOG10217; -.
DR   HOVERGEN; HBG003090; -.
DR   InParanoid; Q08509; -.
DR   OrthoDB; EOG42V8FP; -.
DR   ArrayExpress; Q08509; -.
DR   Bgee; Q08509; -.
DR   Genevestigator; Q08509; -.
DR   GermOnline; ENSMUSG00000015766; Mus musculus.
DR   GO; GO:0017146; C:N-methyl-D-aspartate selective glutamate receptor complex; IDA:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:MGI.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR   GO; GO:0048149; P:behavioral response to ethanol; IMP:MGI.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR013625; PTB.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF08416; PTB; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Phosphoprotein; SH3 domain.
FT   CHAIN         1    821       Epidermal growth factor receptor kinase
FT                                substrate 8.
FT                                /FTId=PRO_0000086995.
FT   DOMAIN       69    129       PH; first part.
FT   DOMAIN      381    414       PH; second part.
FT   DOMAIN      532    591       SH3.
FT   COMPBIAS    210    213       Poly-Pro.
FT   COMPBIAS    322    325       Poly-Pro.
FT   COMPBIAS    421    440       Pro-rich.
FT   COMPBIAS    620    650       Pro-rich.
FT   COMPBIAS    658    663       Poly-Ser.
FT   MOD_RES     484    484       Phosphotyrosine (By similarity).
FT   MOD_RES     524    524       Phosphotyrosine (By similarity).
FT   MOD_RES     658    658       Phosphoserine (By similarity).
FT   MOD_RES     660    660       Phosphoserine (By similarity).
FT   MOD_RES     661    661       Phosphoserine (By similarity).
FT   MOD_RES     810    810       Phosphoserine (By similarity).
FT   MOD_RES     814    814       Phosphoserine (By similarity).
FT   STRAND      534    539
FT   STRAND      556    559
FT   HELIX       561    563
FT   STRAND      566    570
FT   STRAND      576    580
FT   HELIX       581    583
FT   STRAND      584    587
SQ   SEQUENCE   821 AA;  91738 MW;  6B9EB95DD22D910C CRC64;
     MNGHMSNRSS GYGVYPSQLN GYGSSPPYSQ MDREHSSRTS AKALYEQRKN YARDSVSSVS
     DVSQYRVEHL TTFVLDRKDA MITVEDGIRK LKLLDAKGKV WTQDMILQVD DRAVSLIDLE
     SKNELENFPL NTISHCQAVV HACSYDSILA LVCKEPTQSK PDLHLFQCDE VKANLISEDI
     ESAISDSKGG KQKRRPEALR MIAKADPGIP PPPRAPAPVP PGTVTQVDVR SRVAAWSAWA
     ADQGDFEKPR QYHEQEETPE MMAARIDRDV QILNHILDDI EFFITKLQKA AEAFSELSKR
     KKSKKSKRKG PGEGVLTLRA KPPPPDEFVD CFQKFKHGFN LLAKLKSHIQ NPSASDLVHF
     LFTPLNMVVQ ATGGPELASS VLSPLLTKDT VDFLNYTATA EERKLWMSLG DSWVKVRAEW
     PKEQFIPPYV PRFRNGWEPP MLNFMGAPTE QDMYQLAESV ANAEHQRKQD SKRLSTEHSN
     VSDYPPADGY AYSSSMYHRG PHADHGEAAM PFKSTPNHQV DRNYDAVKTQ PKKYAKSKYD
     FVARNSSELS VMKDDVLEIL DDRRQWWKVR NASGDSGFVP NNILDIMRTP ESGVGRADPP
     YTHTIQKQRT EYGLRSADTP SAPSPPPTPA PVPVPLPPSV PAPVSVPKVP ADVTRQNSSS
     SDSGGSIVRD SQRYKQLPVD RRKSQMEEVQ DELFQRLTIG RSAAQRKFHV PRQNVPVINI
     TYDSSPEEVK TWLQSKGFNP VTVNSLGVLN GAQLFSLNKD ELRSVCPEGA RVFNQITVQK
     AALEDSNGSS ELQEIMRRRQ EKISAAASDS GVESFDEGSS H
//
ID   FBLN1_MOUSE             Reviewed;         705 AA.
AC   Q08879; Q08878; Q8C3B1; Q91ZC9; Q922K8;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   09-MAY-2003, sequence version 2.
DT   08-MAR-2011, entry version 115.
DE   RecName: Full=Fibulin-1;
DE            Short=FIBL-1;
DE   AltName: Full=Basement-membrane protein 90;
DE            Short=BM-90;
DE   Flags: Precursor;
GN   Name=Fbln1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS C AND D), AND LIGANDS
RP   INTERACTION.
RX   MEDLINE=93358897; PubMed=8354280;
RX   DOI=10.1111/j.1432-1033.1993.tb18086.x;
RA   Pan T.-C., Kluge M., Zhang R.Z., Mayer U., Timpl R., Chu M.-L.;
RT   "Sequence of extracellular mouse protein BM-90/fibulin and its
RT   calcium-dependent binding to other basement-membrane ligands.";
RL   Eur. J. Biochem. 215:733-740(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RX   MEDLINE=21818451; PubMed=11829738; DOI=10.1042/0264-6021:3620041;
RA   Castoldi M., Chu M.-L.;
RT   "Structural and functional characterization of the human and mouse
RT   fibulin-1 gene promoters: role of Sp1 and Sp3.";
RL   Biochem. J. 362:41-50(2002).
RN   [5]
RP   PROTEIN SEQUENCE OF 30-53; 110-117; 231-243; 339-387; 434-439;
RP   469-476; 553-563 AND 574-581.
RX   PubMed=2249686; DOI=10.1111/j.1432-1033.1990.tb19383.x;
RA   Kluge M., Mann K., Dziadek M., Timpl R.;
RT   "Characterization of a novel calcium-binding 90-kDa glycoprotein (BM-
RT   90) shared by basement membranes and serum.";
RL   Eur. J. Biochem. 193:651-659(1990).
RN   [6]
RP   CHARACTERIZATION OF NID AFFINITY.
RX   MEDLINE=95147264; PubMed=7844816; DOI=10.1006/jmbi.1994.0020;
RA   Sasaki T., Kostka G., Goehring W., Wiedemann H., Mann K., Chu M.-L.,
RA   Timpl R.;
RT   "Structural characterization of two variants of fibulin-1 that differ
RT   in nidogen affinity.";
RL   J. Mol. Biol. 245:241-250(1995).
RN   [7]
RP   DEVELOPMENTAL STAGE.
RX   MEDLINE=97003230; PubMed=8850569;
RX   DOI=10.1002/(SICI)1097-0177(199603)205:3<348::AID-AJA13>3.0.CO;2-0;
RA   Zhang H.-Y., Timpl R., Sasaki T., Chu M.-L., Ekblom P.;
RT   "Fibulin-1 and fibulin-2 expression during organogenesis in the
RT   developing mouse embryo.";
RL   Dev. Dyn. 205:348-364(1996).
RN   [8]
RP   NID-BINDING SITE.
RC   STRAIN=129/Sv;
RX   MEDLINE=97446166; PubMed=9299350; DOI=10.1006/jmbi.1997.1244;
RA   Adam S., Goehring W., Wiedemann H., Chu M.-L., Timpl R., Kostka G.;
RT   "Binding of fibulin-1 to nidogen depends on its C-terminal globular
RT   domain and a specific array of calcium-binding epidermal growth
RT   factor-like (EG) modules.";
RL   J. Mol. Biol. 272:226-236(1997).
RN   [9]
RP   INTERACTION WITH LAMA2.
RX   MEDLINE=99146904; PubMed=10022829; DOI=10.1093/emboj/18.4.863;
RA   Talts J.F., Andac Z., Goehring W., Brancaccio A., Timpl R.;
RT   "Binding of the G domains of laminin alpha1 and alpha2 chains and
RT   perlecan to heparin, sulfatides, alpha-dystroglycan and several
RT   extracellular matrix proteins.";
RL   EMBO J. 18:863-870(1999).
RN   [10]
RP   INTERACTION WITH ACAN AND CSPG2.
RX   MEDLINE=99329059; PubMed=10400671; DOI=10.1074/jbc.274.29.20444;
RA   Aspberg A., Adam S., Kostka G., Timpl R., Heinegaard D.;
RT   "Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and
RT   versican.";
RL   J. Biol. Chem. 274:20444-20449(1999).
RN   [11]
RP   INTERACTION WITH NID.
RX   MEDLINE=21474010; PubMed=11589703;
RX   DOI=10.1046/j.0014-2956.2001.02437.x;
RA   Ries A., Goehring W., Fox J.W., Timpl R., Sasaki T.;
RT   "Recombinant domains of mouse nidogen-1 and their binding to basement
RT   membrane proteins and monoclonal antibodies.";
RL   Eur. J. Biochem. 268:5119-5128(2001).
RN   [12]
RP   DOWN-REGULATION BY GLUCOCORTICOIDS.
RX   MEDLINE=21600963; PubMed=11737251;
RX   DOI=10.1034/j.1600-0609.2001.5790528.x;
RA   Gu Y.-C., Talts J.F., Gullberg D., Timpl R., Ekblom M.;
RT   "Glucocorticoids down-regulate the extracellular matrix proteins
RT   fibronectin, fibulin-1 and fibulin-2 in bone marrow stroma.";
RL   Eur. J. Haematol. 67:176-184(2001).
RN   [13]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=21136579; PubMed=11238726;
RX   DOI=10.1046/j.1471-4159.2001.00144.x;
RA   Ohsawa I., Takamura C., Kohsaka S.;
RT   "Fibulin-1 binds the amino-terminal head of beta-amyloid precursor
RT   protein and modulates its physiological function.";
RL   J. Neurochem. 76:1411-1420(2001).
RN   [14]
RP   INTERACTION WITH E6, AND INHIBITION OF E6-MEDIATED TRANSFORMATION.
RX   MEDLINE=22188366; PubMed=12200142; DOI=10.1016/S0006-291X(02)02041-7;
RA   Du M., Fan X., Hong E., Chen J.J.;
RT   "Interaction of oncogenic papillomavirus E6 proteins with fibulin-1.";
RL   Biochem. Biophys. Res. Commun. 296:962-969(2002).
RN   [15]
RP   DEVELOPMENTAL STAGE.
RX   MEDLINE=21826618; PubMed=11836357; DOI=10.1136/jmg.39.2.98;
RA   Debeer P., Schoenmakers E.F.P.M., Twal W.O., Argraves W.S.,
RA   De Smet L., Fryns J.-P., Van De Ven W.J.M.;
RT   "The fibulin-1 gene (FBLN1) is disrupted in a t(12;22) associated with
RT   a complex type of synpolydactyly.";
RL   J. Med. Genet. 39:98-104(2002).
RN   [16]
RP   INTERACTION WITH FBLN7.
RX   PubMed=17699513; DOI=10.1074/jbc.M705847200;
RA   de Vega S., Iwamoto T., Nakamura T., Hozumi K., McKnight D.A.,
RA   Fisher L.W., Fukumoto S., Yamada Y.;
RT   "TM14 is a new member of the fibulin family (fibulin-7) that interacts
RT   with extracellular matrix molecules and is active for cell binding.";
RL   J. Biol. Chem. 282:30878-30888(2007).
CC   -!- FUNCTION: Incorporated into fibronectin-containing matrix fibers.
CC       May play a role in cell adhesion and migration along protein
CC       fibers within the extracellular matrix (ECM). Could be important
CC       for certain developmental processes and contribute to the
CC       supramolecular organization of ECM architecture, in particular to
CC       those of basement membranes.
CC   -!- SUBUNIT: Homomultimerizes and interacts with various extracellular
CC       matrix components such as FN1, LAMA1, LMA2, NID, ACAN, CSPG2 and
CC       type IV collagen. Interacts also with papillomavirus E6 proteins.
CC       Binding analysis demonstrated for isoform C a 100-fold stronger
CC       binding to the basement membrane protein NID than for isoform D.
CC       Interacts with FBLN7.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=D;
CC         IsoId=Q08879-1; Sequence=Displayed;
CC       Name=A;
CC         IsoId=Q08879-3; Sequence=Not described;
CC       Name=B;
CC         IsoId=Q08879-4; Sequence=Not described;
CC       Name=C;
CC         IsoId=Q08879-2; Sequence=VSP_001386;
CC         Note=Ref.1 (CAA50206) sequence is in conflict in position:
CC         571:E->A;
CC   -!- TISSUE SPECIFICITY: Detected in most organs (brain, heart, lung,
CC       spleen, liver and kidney). Neurons are the predominant source of
CC       production in the brain. Not expressed significantly by astrocytes
CC       or microglia.
CC   -!- DEVELOPMENTAL STAGE: The differential expression of the fibulin
CC       family contributes to the formation of molecularly distinct
CC       extracellular matrices already during early developmental stages
CC       of a large number of tissues. Increase expression at neonate stage
CC       in the brain. Expressed in interdigital regions of the handplate
CC       of a 12 dpc embryo and in the lateral perichondrial region.
CC       Similar expression persists in the 13 dpc handplate particularly
CC       in the perichondrial regions and apical aspects of the developing
CC       digits.
CC   -!- INDUCTION: Glucocorticoids suppressed mRNA expression and protein
CC       synthesis.
CC   -!- SIMILARITY: Belongs to the fibulin family.
CC   -!- SIMILARITY: Contains 3 anaphylatoxin-like domains.
CC   -!- SIMILARITY: Contains 9 EGF-like domains.
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DR   EMBL; X70854; CAA50207.1; -; mRNA.
DR   EMBL; X70853; CAA50206.1; -; mRNA.
DR   EMBL; AK086451; BAC39669.1; -; mRNA.
DR   EMBL; AK035388; BAC29054.1; -; mRNA.
DR   EMBL; BC007140; AAH07140.1; -; mRNA.
DR   EMBL; AY040588; AAK82944.1; -; Genomic_DNA.
DR   IPI; IPI00230432; -.
DR   IPI; IPI00322748; -.
DR   PIR; S34968; S34968.
DR   PIR; S78040; S78040.
DR   RefSeq; NP_034310.2; NM_010180.2.
DR   UniGene; Mm.297992; -.
DR   ProteinModelPortal; Q08879; -.
DR   SMR; Q08879; 137-609.
DR   MINT; MINT-245863; -.
DR   STRING; Q08879; -.
DR   PRIDE; Q08879; -.
DR   Ensembl; ENSMUST00000057410; ENSMUSP00000054583; ENSMUSG00000006369.
DR   Ensembl; ENSMUST00000109432; ENSMUSP00000105058; ENSMUSG00000006369.
DR   GeneID; 14114; -.
DR   KEGG; mmu:14114; -.
DR   UCSC; uc007xdb.1; mouse.
DR   UCSC; uc007xdc.1; mouse.
DR   CTD; 14114; -.
DR   MGI; MGI:95487; Fbln1.
DR   eggNOG; roNOG11942; -.
DR   GeneTree; ENSGT00600000084166; -.
DR   HOGENOM; HBG717835; -.
DR   HOVERGEN; HBG051559; -.
DR   InParanoid; Q08879; -.
DR   OMA; MDSATEQ; -.
DR   OrthoDB; EOG4NGGM2; -.
DR   PhylomeDB; Q08879; -.
DR   NextBio; 285170; -.
DR   ArrayExpress; Q08879; -.
DR   Bgee; Q08879; -.
DR   CleanEx; MM_FBLN1; -.
DR   Genevestigator; Q08879; -.
DR   GermOnline; ENSMUSG00000006369; Mus musculus.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016504; F:peptidase activator activity; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0030198; P:extracellular matrix organization; IDA:MGI.
DR   InterPro; IPR000020; Anaphylatoxin/fibulin.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR001881; EGF_Ca-bd.
DR   InterPro; IPR013091; EGF_Ca-bd_2.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR017048; Fibulin-1.
DR   Pfam; PF01821; ANATO; 2.
DR   Pfam; PF07645; EGF_CA; 8.
DR   PIRSF; PIRSF036313; Fibulin-1; 1.
DR   SMART; SM00104; ANATO; 3.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 7.
DR   PROSITE; PS01177; ANAPHYLATOXIN_1; 3.
DR   PROSITE; PS01178; ANAPHYLATOXIN_2; 3.
DR   PROSITE; PS00010; ASX_HYDROXYL; 4.
DR   PROSITE; PS00022; EGF_1; FALSE_NEG.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS01187; EGF_CA; 8.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Direct protein sequencing;
KW   Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW   Repeat; Secreted; Signal.
FT   SIGNAL        1     29
FT   CHAIN        30    705       Fibulin-1.
FT                                /FTId=PRO_0000007564.
FT   DOMAIN       36     76       Anaphylatoxin-like 1.
FT   DOMAIN       77    111       Anaphylatoxin-like 2.
FT   DOMAIN      112    144       Anaphylatoxin-like 3.
FT   DOMAIN      178    217       EGF-like 1.
FT   DOMAIN      218    263       EGF-like 2; calcium-binding (Potential).
FT   DOMAIN      264    309       EGF-like 3; calcium-binding (Potential).
FT   DOMAIN      310    357       EGF-like 4; calcium-binding (Potential).
FT   DOMAIN      358    400       EGF-like 5; calcium-binding (Potential).
FT   DOMAIN      401    442       EGF-like 6; calcium-binding (Potential).
FT   DOMAIN      443    482       EGF-like 7; calcium-binding (Potential).
FT   DOMAIN      483    526       EGF-like 8; calcium-binding (Potential).
FT   DOMAIN      527    580       EGF-like 9; calcium-binding (Potential).
FT   REGION      358    442       Self-association and FN1-binding (By
FT                                similarity).
FT   CARBOHYD     98     98       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    537    537       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    541    541       N-linked (GlcNAc...) (Potential).
FT   DISULFID     36     61       By similarity.
FT   DISULFID     37     68       By similarity.
FT   DISULFID     50     69       By similarity.
FT   DISULFID     78    109       By similarity.
FT   DISULFID     91    110       By similarity.
FT   DISULFID    112    136       By similarity.
FT   DISULFID    113    143       By similarity.
FT   DISULFID    126    144       By similarity.
FT   DISULFID    182    192       By similarity.
FT   DISULFID    188    201       By similarity.
FT   DISULFID    203    216       By similarity.
FT   DISULFID    222    235       By similarity.
FT   DISULFID    229    244       By similarity.
FT   DISULFID    250    262       By similarity.
FT   DISULFID    268    281       By similarity.
FT   DISULFID    275    290       By similarity.
FT   DISULFID    296    308       By similarity.
FT   DISULFID    314    327       By similarity.
FT   DISULFID    321    336       By similarity.
FT   DISULFID    343    356       By similarity.
FT   DISULFID    362    375       By similarity.
FT   DISULFID    369    384       By similarity.
FT   DISULFID    386    399       By similarity.
FT   DISULFID    405    417       By similarity.
FT   DISULFID    413    426       By similarity.
FT   DISULFID    428    441       By similarity.
FT   DISULFID    447    456       By similarity.
FT   DISULFID    452    465       By similarity.
FT   DISULFID    467    481       By similarity.
FT   DISULFID    487    500       By similarity.
FT   DISULFID    496    509       By similarity.
FT   DISULFID    511    525       By similarity.
FT   DISULFID    531    544       By similarity.
FT   DISULFID    538    553       By similarity.
FT   DISULFID    558    579       By similarity.
FT   VAR_SEQ     569    705       FRQEKTDTVRCIKSCRPNDEACVRDPVHTVSHTVISLPTFR
FT                                EFTRPEEIIFLRAVTPLYPANQADIIFDITEGNLRDSFDII
FT                                KRYEDGMTVGVVRQVRPIVGPFYAVLKLEMNYVLGGVVSHR
FT                                NVVNVHIFVSEYWF -> RCERLPCHENQECPRLPLRITYY
FT                                HLSFPTNIQVPAVVFRMGPSSAVPGDSMQLAITAGNEEGFF
FT                                TTRKVSHHSGVVALTKPIPEPRDLLLTVKMDLYRHGTVSSF
FT                                VAKLFIFVSAEL (in isoform C).
FT                                /FTId=VSP_001386.
FT   CONFLICT     30     30       D -> N (in Ref. 5; AA sequence).
FT   CONFLICT     40     40       G -> P (in Ref. 1; CAA50207).
FT   CONFLICT    363    363       S -> A (in Ref. 1; CAA50207).
FT   CONFLICT    385    385       E -> K (in Ref. 2; BAC39669).
FT   CONFLICT    553    553       C -> Q (in Ref. 5; AA sequence).
FT   CONFLICT    558    558       C -> Q (in Ref. 5; AA sequence).
SQ   SEQUENCE   705 AA;  78033 MW;  76C527A12E97D0E1 CRC64;
     MERPVPSRLV PLPLLLLSSL SLLAARANAD ISMEACCTDG NQMANQHRDC SLPYTSESKE
     CRMVQEQCCH NQLEELHCAT GINLASEPEG CASLHSYNSS LETIFIKRCC HCCMLGKASL
     ARDQTCEPIV MISYQCGLVF RACCVKAREN SDFVQGNGAD LQDPAKIPDE EDQEDPYLND
     RCRGGGPCKQ QCRDTGDEVI CSCFVGYQLQ SDGVSCEDIN ECITGSHNCR LGESCINTVG
     SFRCQRDSSC GTGYELTEDN NCKDIDECET GIHNCPPDFI CQNTLGSFRC RPKLQCKSGF
     IQDALGNCID INECLSISAP CPVGQTCINT EGSYTCQKNV PNCGRGYHLN EEGTRCVDVD
     ECSPPAEPCG KGHHCLNSPG SFRCECKAGF YFDGISRTCV DINECQRYPG RLCGHKCENT
     PGSFHCSCSA GFRLSVDGRS CEDVNECLNS PCSQECANVY GSYQCYCRRG YQLSDVDGVT
     CEDIDECALP TGGHICSYRC INIPGSFQCS CPSSGYRLAP NGRNCQDIDE CVTGIHNCSI
     NETCFNIQGS FRCLSFECPE NYRRSADTFR QEKTDTVRCI KSCRPNDEAC VRDPVHTVSH
     TVISLPTFRE FTRPEEIIFL RAVTPLYPAN QADIIFDITE GNLRDSFDII KRYEDGMTVG
     VVRQVRPIVG PFYAVLKLEM NYVLGGVVSH RNVVNVHIFV SEYWF
//
ID   SSRP1_MOUSE             Reviewed;         708 AA.
AC   Q08943; Q3U9Z2; Q3UJ75; Q4V9U4; Q8CGA6;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=FACT complex subunit SSRP1;
DE   AltName: Full=Facilitates chromatin transcription complex subunit SSRP1;
DE   AltName: Full=Recombination signal sequence recognition protein 1;
DE   AltName: Full=Structure-specific recognition protein 1;
DE   AltName: Full=T160;
GN   Name=Ssrp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=B-cell;
RX   MEDLINE=91342655; PubMed=1678855;
RA   Shirakata M., Hueppi K., Usada S., Okazaki K., Yoshida K., Sakano H.;
RT   "HMG1-related DNA-binding protein isolated with V-(D)-J recombination
RT   signal probes.";
RL   Mol. Cell. Biol. 11:4528-4536(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow, Heart, Liver, Stomach, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 589-708 (ISOFORM 1).
RC   STRAIN=C57BL/6J, and FVB/N-3; TISSUE=Mammary gland, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=12861016; DOI=10.1128/MCB.23.15.5301-5307.2003;
RA   Cao S., Bendall H., Hicks G.G., Nashabi A., Sakano H., Shinkai Y.,
RA   Gariglio M., Oltz E.M., Ruley H.E.;
RT   "The high-mobility-group box protein SSRP1/T160 is essential for cell
RT   viability in day 3.5 mouse embryos.";
RL   Mol. Cell. Biol. 23:5301-5307(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667; SER-668; SER-671;
RP   SER-672 AND SER-673, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-441, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444; SER-667 AND
RP   SER-668, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Component of the FACT complex, a general chromatin
CC       factor that acts to reorganize nucleosomes. The FACT complex is
CC       involved in multiple processes that require DNA as a template such
CC       as mRNA elongation, DNA replication and DNA repair. During
CC       transcription elongation the FACT complex acts as a histone
CC       chaperone that both destabilizes and restores nucleosomal
CC       structure. It facilitates the passage of RNA polymerase II and
CC       transcription by promoting the dissociation of one histone H2A-H2B
CC       dimer from the nucleosome, then subsequently promotes the
CC       reestablishment of the nucleosome following the passage of RNA
CC       polymerase II. The FACT complex is probably also involved in
CC       phosphorylation of 'Ser-392' of p53/TP53 via its association with
CC       CK2 (casein kinase II). Binds specifically to double-stranded DNA.
CC       Also acts as a transcriptional coactivator for p63/TP63.
CC   -!- SUBUNIT: Component of the FACT complex, a stable heterodimer of
CC       SSRP1 and SUPT16H. Also component of a CK2-SPT16-SSRP1 complex
CC       which forms following UV irradiation, composed of SSRP1, SUPT16H,
CC       CSNK2A1, CSNK2A2 and CSNK2B. Binds to histone H3-H4 tetramers, but
CC       not to intact nucleosomes. Interacts with isoform gamma of
CC       p63/TP63. Interacts with FYTTD1/UIF, SRF and NEK9 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Colocalizes with
CC       RNA polymerase II on chromatin. Recruited to actively transcribed
CC       loci (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q08943-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q08943-2; Sequence=VSP_019626;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated by CK2 following UV but not gamma irradiation.
CC       Phosphorylation inhibits its DNA-binding activity (By similarity).
CC   -!- PTM: Ubiquitinated. Polyubiquitinated following caspase cleavage
CC       resulting in degradation of the N-terminal ubiquitinated part of
CC       the cleaved protein (By similarity).
CC   -!- PTM: Sumoylated (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Embryos die soon after implantation while
CC       preimplantation blastocysts are defective for cell outgrowth.
CC   -!- SIMILARITY: Belongs to the SSRP1 family.
CC   -!- SIMILARITY: Contains 1 HMG box DNA-binding domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH42502.1; Type=Frameshift; Positions=697;
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DR   EMBL; S50213; AAB19500.2; -; mRNA.
DR   EMBL; AK146446; BAE27178.1; -; mRNA.
DR   EMBL; AK146585; BAE27280.1; -; mRNA.
DR   EMBL; AK146607; BAE27299.1; -; mRNA.
DR   EMBL; AK151584; BAE30524.1; -; mRNA.
DR   EMBL; AK158552; BAE34555.1; -; mRNA.
DR   EMBL; BC042502; AAH42502.1; ALT_FRAME; mRNA.
DR   EMBL; BC096682; AAH96682.1; -; mRNA.
DR   IPI; IPI00407571; -.
DR   IPI; IPI00652593; -.
DR   PIR; A41265; A41265.
DR   RefSeq; NP_001129553.1; NM_001136081.1.
DR   RefSeq; NP_892035.2; NM_182990.3.
DR   UniGene; Mm.219793; -.
DR   ProteinModelPortal; Q08943; -.
DR   SMR; Q08943; 3-107, 195-428.
DR   STRING; Q08943; -.
DR   PhosphoSite; Q08943; -.
DR   PRIDE; Q08943; -.
DR   Ensembl; ENSMUST00000028463; ENSMUSP00000028463; ENSMUSG00000027067.
DR   Ensembl; ENSMUST00000077798; ENSMUSP00000076971; ENSMUSG00000027067.
DR   GeneID; 20833; -.
DR   KEGG; mmu:20833; -.
DR   UCSC; uc008kju.1; mouse.
DR   CTD; 20833; -.
DR   MGI; MGI:107912; Ssrp1.
DR   GeneTree; ENSGT00550000074791; -.
DR   HOVERGEN; HBG002932; -.
DR   OrthoDB; EOG41VK2K; -.
DR   PhylomeDB; Q08943; -.
DR   NextBio; 299579; -.
DR   ArrayExpress; Q08943; -.
DR   Bgee; Q08943; -.
DR   CleanEx; MM_SSRP1; -.
DR   Genevestigator; Q08943; -.
DR   GermOnline; ENSMUSG00000027067; Mus musculus.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR000910; HMG_HMG1/HMG2.
DR   InterPro; IPR009071; HMG_superfamily.
DR   InterPro; IPR000969; SSrcognition.
DR   Gene3D; G3DSA:1.10.30.10; HMG-box; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   Pfam; PF03531; SSrecog; 1.
DR   PRINTS; PR00887; SSRCOGNITION.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Chromosome; DNA damage; DNA repair;
KW   DNA replication; DNA-binding; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    708       FACT complex subunit SSRP1.
FT                                /FTId=PRO_0000048607.
FT   DNA_BIND    547    615       HMG box.
FT   COMPBIAS    439    496       Asp/Glu-rich (acidic).
FT   COMPBIAS    497    511       Ser-rich.
FT   COMPBIAS    512    534       Arg/Lys-rich (basic).
FT   COMPBIAS    623    640       Arg/Lys-rich (basic).
FT   COMPBIAS    641    708       Ser-rich.
FT   SITE        450    451       Cleavage; by caspase-3 and/or caspase-7
FT                                (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      33     33       N6-acetyllysine (By similarity).
FT   MOD_RES      90     90       N6-acetyllysine (By similarity).
FT   MOD_RES     170    170       Phosphothreonine (By similarity).
FT   MOD_RES     233    233       N6-acetyllysine (By similarity).
FT   MOD_RES     311    311       Phosphotyrosine (By similarity).
FT   MOD_RES     413    413       N6-acetyllysine (By similarity).
FT   MOD_RES     441    441       Phosphotyrosine.
FT   MOD_RES     444    444       Phosphoserine.
FT   MOD_RES     510    510       Phosphoserine; by CK2 (By similarity).
FT   MOD_RES     554    554       Phosphotyrosine (By similarity).
FT   MOD_RES     561    561       Phosphoserine (By similarity).
FT   MOD_RES     657    657       Phosphoserine; by CK2 (By similarity).
FT   MOD_RES     659    659       Phosphoserine (By similarity).
FT   MOD_RES     667    667       Phosphoserine.
FT   MOD_RES     668    668       Phosphoserine.
FT   MOD_RES     671    671       Phosphoserine.
FT   MOD_RES     672    672       Phosphoserine.
FT   MOD_RES     673    673       Phosphoserine.
FT   MOD_RES     688    688       Phosphoserine; by CK2 (By similarity).
FT   VAR_SEQ     621    621       S -> SSKRDK (in isoform 2).
FT                                /FTId=VSP_019626.
FT   CONFLICT     27     28       RQ -> PS (in Ref. 1; AAB19500).
FT   CONFLICT     54     54       R -> P (in Ref. 1; AAB19500).
FT   CONFLICT    138    144       QCTTGKN -> SVPQARI (in Ref. 1; AAB19500).
FT   CONFLICT    156    156       A -> P (in Ref. 1; AAB19500).
FT   CONFLICT    589    590       SK -> HE (in Ref. 3; AAH96682).
FT   CONFLICT    604    604       R -> S (in Ref. 3; AAH96682).
SQ   SEQUENCE   708 AA;  80860 MW;  8259C1A6E9899843 CRC64;
     MAETLEFNDI FQEVKGSMND GRLRLSRQGI IFKNSKTGKV DNIQAGELTE GIWRRVALGH
     GLKLLTKNGH VYKYDGFRES EFEKLSDFFK THYRLELMEK DLCVKGWNWG TVKFGGQLLS
     FDIGDQPVFE IPLSNVSQCT TGKNEVTLEF HQNDDAEVSL MEVRFYVPPT QEDGVDPVEA
     FAQNVLSKAD VIQATGDAIC IFRELQCLTP RGRYDIRIYP TFLHLHGKTF DYKIPYTTVL
     RLFLLPHKDQ RQMFFVISLD PPIKQGQTRY HFLILLFSKD EDISLTLNMN EEEVEKRFEG
     RLTKNMSGSL YEMVSRVMKA LVNRKITVPG NFQGHSGAQC ITCSYKASSG LLYPLERGFI
     YVHKPPVHIR FDEISFVNFA RGTTTTRSFD FEIETKQGTQ YTFSSIEREE YGKLFDFVNA
     KKLNIKNRGL KEGINPGYDD YADSDEDQHD AYLERMKEEG KIREENANDS SDDSGEETDE
     SFNPGEEEED VAEEFDSNAS ASSSSNEGDS DREEKKREQL KRAKMAKDRK SRRKSSEAKK
     GKDPNAPKRP MSAYMLWLNA SREKIKSDHP GISITDLSKK AGEIWKGMSK EKKEEWDRKA
     EDARREYEKA MKEYEGGRGD SSKRDKSKKK KKVKAKMEKK STPSRGSSSK SSSRQLSDSF
     KSKEFVSSDE SSSGENKSKK KRRRSEDSEE ELASTPPSSE DSASGSDE
//
ID   Q08EB5_MOUSE            Unreviewed;      1304 AA.
AC   Q08EB5;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   11-JAN-2011, entry version 30.
DE   SubName: Full=Clasp2 protein;
GN   Name=Clasp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC117964; AAI17965.1; -; mRNA.
DR   IPI; IPI00407863; -.
DR   UniGene; Mm.222272; -.
DR   ProteinModelPortal; Q08EB5; -.
DR   SMR; Q08EB5; 1084-1290.
DR   STRING; Q08EB5; -.
DR   Ensembl; ENSMUST00000111838; ENSMUSP00000107469; ENSMUSG00000033392.
DR   UCSC; uc009rww.1; mouse.
DR   MGI; MGI:1923749; Clasp2.
DR   HOVERGEN; HBG079692; -.
DR   InParanoid; Q08EB5; -.
DR   OMA; SYVAMVI; -.
DR   ArrayExpress; Q08EB5; -.
DR   Bgee; Q08EB5; -.
DR   Genevestigator; Q08EB5; -.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IDA:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR   GO; GO:0016477; P:cell migration; IMP:MGI.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:MGI.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:MGI.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 3.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1304 AA;  142516 MW;  EEDC0E4E384408AC CRC64;
     MRRLICKRIC DYKSFDDEES VDGNRPSSAA SAFKVPAPKT PGNPVSSARK PGSAGGPKVG
     GPSKEGGAGA VDEDDFIKAF TDVPSVQIYS SRELEETLNK IREILSDDKH DWDQRANALK
     KIRSLLVAGA AQYDCFFQHL RLLDGALKLS AKDLRSQVVR EACITVAHLS TVLGNKFDHG
     AEAIVPTLFN LVPNSAKVMA TSGCAAIRFI IRHTHVPRLI PLITSNCTSK SVPVRRRSFE
     FLDLLLQEWQ THSLERHAAV LVETIKKGIH DADAEARVEA RKTYMGLRNH FPGEAETLYN
     SLEPSYQKSL QTYLKSSGSV ASLPQSDRSS SSSQESLNRP FSSKWSTANP STVAGRVSVG
     GSKANPLPGS LQRSRSDIDV NAAAGAKAHH AAGQAVRSGR LGAGALNPGS YASLEDTSDK
     MDGTASDDGR VRAKLSTPLV AVGNAKTDSR GRSRTKMVSQ SQRSSSPDKN EGSQSANTIG
     AGSRSGSPGR VLTTTALSTV SSGAQRVLVN SASAQKRSKI PRSQGCSREA SPSRLSVARS
     SRIPRPSVSQ GCSREASRES SRDTSPVRSF QPLGPGYGIS QSSRLSSSVS AMRVLNTGSD
     VEEAVADALL LGDIRTKKKP ARRRYESYGM HSDDDANSDA SSACSERSYS SRNGSIPTYM
     RQTEDVAEVL NRCASSNWSE RKEGLLGLQN LLKNQRTLSR VELKRLCEIF TRMFADPHGK
     VFSMFLETLV DFIQVHKDDL QDWLFVLLTQ LLKKMGADLL GSVQAKVQKA LDITRESFPN
     DLQFNILMRF TVDQTQTPSL KVKVAILKYI ETLAKQMDPR DFTNSSETRL AVSRVITWTT
     EPKSSDVRKA AQSVLISLFE LNTPEFTMLL GALPKTFQDG ATKLLHNHLR NTGNGTQSSM
     GSPLTRPTPR SPANWSSPLT SPTNTSQNTL SPSAFDYDTE NMNSEDIYSS LRGVTEAIQN
     FSFRSQEDMS EPVRRDPKKE DGDTICSGPG MSDPRAGGDA ADGSQPALDN KASLLHSMPL
     HSSPRSRDYN PYNYSDSISP FNKSALKEAM FDDDADQFPD DLSLDHSDLV AELLKELSNH
     NERIEERKIA LYELMKLTQE ESFSVWDEHF KTILLLLLET LGDKEPTIRA LALKVLKEIL
     RHQPARFKNY AELTVMKTLE AHKDPHKEVV RSAEEAASVL ATSISPEQCI KVLCPIIQTA
     DYPINLAAIK MQTKVIERVS KETLNMLLPE IMPGLIQGYD NSESSVRKAC VFCLVAVHAV
     IGDELKPHLS QLTGSKMKLL NLYIKRAQTG SAGADPTADV SGQS
//
ID   CHD8_MOUSE              Reviewed;        2582 AA.
AC   Q09XV5; Q3TV89; Q5I1Z2; Q6ZPM8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Chromodomain-helicase-DNA-binding protein 8;
DE            Short=CHD-8;
DE            EC=3.6.4.12;
DE   AltName: Full=ATP-dependent helicase CHD8;
DE   AltName: Full=Axis duplication inhibitor;
DE            Short=Duplin;
GN   Name=Chd8; Synonyms=Kiaa1564;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
RP   CTCF, AND SUBCELLULAR LOCATION.
RC   TISSUE=Embryo;
RX   PubMed=16949368; DOI=10.1016/j.molcel.2006.08.008;
RA   Ishihara K., Oshimura M., Nakao M.;
RT   "CTCF-dependent chromatin insulator is linked to epigenetic
RT   remodeling.";
RL   Mol. Cell 23:733-742(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), DISRUPTION PHENOTYPE, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=15367660; DOI=10.1128/MCB.24.19.8386-8394.2004;
RA   Nishiyama M., Nakayama K., Tsunematsu R., Tsukiyama T., Kikuchi A.,
RA   Nakayama K.I.;
RT   "Early embryonic death in mice lacking the beta-catenin-binding
RT   protein Duplin.";
RL   Mol. Cell. Biol. 24:8386-8394(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1730-2582.
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2020-2582.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1422 AND SER-1426, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH TP53 AND HISTONE
RP   H1.
RX   PubMed=19151705; DOI=10.1038/ncb1831;
RA   Nishiyama M., Oshikawa K., Tsukada Y.I., Nakagawa T., Iemura S.,
RA   Natsume T., Fan Y., Kikuchi A., Skoultchi A.I., Nakayama K.I.;
RT   "CHD8 suppresses p53-mediated apoptosis through histone H1 recruitment
RT   during early embryogenesis.";
RL   Nat. Cell Biol. 11:172-182(2009).
CC   -!- FUNCTION: DNA helicase that acts as a chromatin remodeling factor
CC       and regulates transcription. Acts as a transcription repressor by
CC       remodeling chromatin structure and recruiting histone H1 to target
CC       genes. Suppresses p53/TP53-mediated apoptosis by recruiting
CC       histone H1 and preventing p53/TP53 transactivation activity. Acts
CC       as a negative regulator of Wnt signaling pathway by regulating
CC       beta-catenin (CTNNB1) activity. Negatively regulates CTNNB1-
CC       targeted gene expression by being recruited specifically to the
CC       promoter regions of several CTNNB1 responsive genes. Involved in
CC       both enhancer blocking and epigenetic remodeling at chromatin
CC       boundary via its interaction with CTCF. Acts as a suppressor of
CC       STAT3 activity by suppressing the LIF-induced STAT3
CC       transcriptional activity. Also acts as a transcription activator
CC       via its interaction with ZNF143 by participating to efficient U6
CC       RNA polymerase III transcription.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Component of some MLL1/MLL complex, at least composed of
CC       the core components MLL, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as
CC       well as the facultative components C17orf49, CHD8, E2F6, HSP70,
CC       IN80C, KIAA1267, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20,
CC       PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6,
CC       TAF7, TAF9 and TEX10 (By similarity). Interacts with p53/TP53,
CC       histone H1, CTNNB1, CTCF and PIAS3. Component of a multiprotein
CC       complex of 900 kDa containing WDR5.
CC   -!- INTERACTION:
CC       Q61164:Ctcf; NbExp=3; IntAct=EBI-1169080, EBI-932785;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Localizes to the promoter
CC       regions of several CTNNB1-responsive genes. Also present at known
CC       CTCF target sites.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q09XV5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q09XV5-2; Sequence=VSP_036676, VSP_036677;
CC   -!- DEVELOPMENTAL STAGE: Expressed predominantly from early- to mid-
CC       stage mouse embryogenesis. Detected throughout embryos from E7.5
CC       to E9.5 but localizes predominantly in the brain, faces, branchial
CC       arches, limb buds, and tail buds of embryos at E10.5.
CC   -!- PTM: Sumoylated (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Death during early embryogenesis due to
CC       widespread apoptosis. Embryos manifest growth retardation from
CC       E5.5 and developmental arrest accompanied by massive apoptosis at
CC       E7.5. They develop into an egg cylinder but do not form a
CC       primitive streak or mesoderm. Mice lacking both Tp53 and Chd8
CC       ameliorate this developmental arrest.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. CHD8
CC       subfamily.
CC   -!- SIMILARITY: Contains 2 chromo domains.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98203.2; Type=Miscellaneous discrepancy; Note=Partially unspliced pre-RNA;
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DR   EMBL; DQ190419; ABB02259.1; -; mRNA.
DR   EMBL; AY863219; AAW56421.1; -; mRNA.
DR   EMBL; AK129393; BAC98203.2; ALT_SEQ; Transcribed_RNA.
DR   EMBL; AK160299; BAE35730.1; -; mRNA.
DR   IPI; IPI00858099; -.
DR   IPI; IPI00923681; -.
DR   RefSeq; NP_963999.2; NM_201637.2.
DR   UniGene; Mm.289934; -.
DR   ProteinModelPortal; Q09XV5; -.
DR   SMR; Q09XV5; 642-1348, 2304-2418.
DR   IntAct; Q09XV5; 3.
DR   STRING; Q09XV5; -.
DR   PhosphoSite; Q09XV5; -.
DR   PRIDE; Q09XV5; -.
DR   Ensembl; ENSMUST00000089752; ENSMUSP00000087184; ENSMUSG00000053754.
DR   GeneID; 67772; -.
DR   KEGG; mmu:67772; -.
DR   UCSC; uc007tot.1; mouse.
DR   CTD; 67772; -.
DR   MGI; MGI:1915022; Chd8.
DR   eggNOG; maNOG22665; -.
DR   GeneTree; ENSGT00560000077077; -.
DR   HOGENOM; HBG446013; -.
DR   HOVERGEN; HBG107676; -.
DR   InParanoid; Q09XV5; -.
DR   OMA; EAQVTQQ; -.
DR   OrthoDB; EOG4ZPDTC; -.
DR   PhylomeDB; Q09XV5; -.
DR   NextBio; 325525; -.
DR   ArrayExpress; Q09XV5; -.
DR   Bgee; Q09XV5; -.
DR   Genevestigator; Q09XV5; -.
DR   GO; GO:0000785; C:chromatin; IEA:InterPro.
DR   GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0008013; F:beta-catenin binding; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; ISS:UniProtKB.
DR   GO; GO:0035064; F:methylated histone residue binding; ISS:UniProtKB.
DR   GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
DR   GO; GO:0016563; F:transcription activator activity; ISS:UniProtKB.
DR   GO; GO:0016564; F:transcription repressor activity; IDA:UniProtKB.
DR   GO; GO:0043044; P:ATP-dependent chromatin remodeling; ISS:UniProtKB.
DR   GO; GO:0060070; P:canonical Wnt receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0006333; P:chromatin assembly or disassembly; IEA:InterPro.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptosis; IDA:UniProtKB.
DR   GO; GO:0030178; P:negative regulation of Wnt receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR   GO; GO:0045945; P:positive regulation of transcription from RNA polymerase III promoter; ISS:UniProtKB.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR006576; BRK_domain.
DR   InterPro; IPR000953; Chromodomain.
DR   InterPro; IPR016197; Chromodomain-like.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF07533; BRK; 2.
DR   Pfam; PF00385; Chromo; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00592; BRK; 2.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF54160; Chromodomain-like; 2.
DR   PROSITE; PS00598; CHROMO_1; FALSE_NEG.
DR   PROSITE; PS50013; CHROMO_2; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; FALSE_NEG.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; ATP-binding; Chromatin regulator;
KW   DNA-binding; Helicase; Hydrolase; Isopeptide bond; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Repeat; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation; Wnt signaling pathway.
FT   CHAIN         1   2582       Chromodomain-helicase-DNA-binding protein
FT                                8.
FT                                /FTId=PRO_0000367310.
FT   DOMAIN      644    711       Chromo 1.
FT   DOMAIN      726    792       Chromo 2.
FT   DOMAIN      825    999       Helicase ATP-binding.
FT   DOMAIN     1139   1290       Helicase C-terminal.
FT   NP_BIND     838    845       ATP (By similarity).
FT   MOTIF       950    953       DEAH box.
FT   COMPBIAS    292    412       Gln-rich.
FT   COMPBIAS   1777   1781       Poly-Arg.
FT   COMPBIAS   2070   2099       Ser-rich.
FT   COMPBIAS   2494   2509       His-rich.
FT   COMPBIAS   2539   2582       Asp-rich.
FT   MOD_RES     539    539       Phosphothreonine (By similarity).
FT   MOD_RES     552    552       Phosphoserine (By similarity).
FT   MOD_RES     555    555       Phosphoserine (By similarity).
FT   MOD_RES     564    564       Phosphoserine (By similarity).
FT   MOD_RES    1400   1400       Phosphothreonine (By similarity).
FT   MOD_RES    1422   1422       Phosphoserine.
FT   MOD_RES    1426   1426       Phosphoserine.
FT   MOD_RES    1978   1978       Phosphoserine (By similarity).
FT   MOD_RES    1995   1995       Phosphothreonine (By similarity).
FT   MOD_RES    1997   1997       Phosphoserine (By similarity).
FT   MOD_RES    2010   2010       Phosphoserine (By similarity).
FT   MOD_RES    2070   2070       Phosphoserine (By similarity).
FT   MOD_RES    2072   2072       Phosphoserine (By similarity).
FT   MOD_RES    2184   2184       Phosphoserine (By similarity).
FT   MOD_RES    2202   2202       Phosphoserine (By similarity).
FT   MOD_RES    2204   2204       Phosphoserine (By similarity).
FT   MOD_RES    2213   2213       Phosphoserine (By similarity).
FT   MOD_RES    2519   2519       Phosphoserine (By similarity).
FT   MOD_RES    2520   2520       Phosphoserine (By similarity).
FT   CROSSLNK    611    611       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   VAR_SEQ     745    751       PVIYYLV -> VSWARRT (in isoform 2).
FT                                /FTId=VSP_036676.
FT   VAR_SEQ     752   2582       Missing (in isoform 2).
FT                                /FTId=VSP_036677.
FT   CONFLICT     21     21       T -> A (in Ref. 2; AAW56421).
FT   CONFLICT   2020   2020       N -> S (in Ref. 3; BAC98203).
FT   CONFLICT   2298   2298       L -> V (in Ref. 3; BAC98203).
SQ   SEQUENCE   2582 AA;  290847 MW;  D9432500F6A8C329 CRC64;
     MADPIMDLFD DPNLFGLDSL TDDSFNQVTQ DPIEEALGLP SSLDSLDQMN QDGGGGDVGN
     SSASDLVPPP EETASTELPK ESTAPAPESL TLHDYTTQPT SQEQPAQPVL QTSTPTAGLL
     QVSKSQEILS QGNPFMGVSA TGVSPSNTGG QPSQSAPKIV ILKAPPNSSV TGTHVAQIQA
     QGITSTAQPL VAGTANGGKV TFTKVLTGTP LRPGVSIVSG NTVLATKVPG NQAAVQRIVQ
     PSRPVKQLVL QPVKGSAPAG NPGAAGPPLK PAVTLTSTPT QGESKRITLV LQQPQSGGPQ
     GHRHVVLGSL PGKIVLQGNQ LAALTQAKNA QGQPAKVVTI QLQVQQPQQK IQIVPQPPSS
     QPQPQPQPPP SAQPLTLSSV QQAQIMGPGQ NPGQRLSVPL KMVLQPQAGS SQGASSGLSV
     VKVLSASEVA ALSSPASCAP HTAGKTGMEE NRRLEHQKKQ EKANRIVAEA IARARARGEQ
     NIPRVLNEDE LPSVRPEEEG EKKRRKKSSG ERLKEEKPKK SKTAAASKTK GKSKLNTITP
     VVGKKRKRNT SSDNSDVEVM PAQSPREDEE SSIQKRRSNR QVKRKKYTED LDIKITDDEE
     EEEVDVTGPI KPEPILPEPV QEPDGETLPS MQFFVENPSE EDAAIVDKVL SMRVVKKELP
     SGQYTEAEEF FVKYKNYSYL HCEWATISQL EKDKRIHQKL KRFKTKMAQM RHFFHEDEEP
     FNPDYVEVDR ILDESHSVDK DNGEPVIYYL VKWCSLPYED STWELKEDVD EGKIREFKRI
     QSRHPELRRV NRPQANAWKK LELSHEYKNR NQLREYQLEG VNWLLFNWYN RQNCILADEM
     GLGKTIQSIA FLQEVYNVGI HGPFLVIAPL STITNWEREF NTWTEMNTIV YHGSLASRQM
     IQQYEMYCKD SRGRLIPGAY KFDALITTFE MILSDCPELR EIEWRCVIID EAHRLKNRNC
     KLLDSLKHMD LEHKVLLTGT PLQNTVEELF SLLHFLEPSQ FPSESEFLKD FGDLKTEEQV
     QKLQAILKPM MLRRLKEDVE KNLAPKQETI IEVELTNIQK KYYRAILEKN FSFLSKGAGH
     TNMPNLLNTM MELRKCCNHP YLINGAEEKI LMEFREACHI IPQDFHLQAM VRSAGKLVLI
     DKLLPKLKAG GHKVLIFSQM VRCLDILEDY LIQRRYLYER IDGRVRGNLR QAAIDRFSKP
     DSDRFVFLLC TRAGGLGINL TAADTCIIFD SDWNPQNDLQ AQARCHRIGQ SKAVKVYRLI
     TRNSYEREMF DKASLKLGLD KAVLQSMSGR DGNITGIQQF SKKEIEDLLR KGAYAAIMEE
     DDEGSKFCEE DIDQILLRRT TTITIESEGK GSTFAKASFV ASENRTDISL DDPNFWQKWA
     KKADLDMDLL NSKNNLVIDT PRVRKQTRHF STLKDDDLVE FSDLESEDDE RPRSRRHDRH
     HTYGRTDCFR VEKHLLVYGW GRWRDILSHG RFKRRMTERD VETICRAILV YCLLHYRGDE
     NIKSFIWDLI SPAENGKTKE LQNHSGLSIP VPRGRKGKKV KSQSTFDIHK ADWIRKYNPD
     TLFQDESYKK HLKHQCNKVL LRVRMLYYLR QEVIGDQAEK VLGGAIASEI DIWFPVVDQL
     EVPTTWWDSE ADKSLLIGVF KHGYEKYNTM RADPALCFLE KAGRPDDKAI AAEHRVLDNF
     SDLVEGIDFD KDCEDPEYKP LQGPPKDPDD EGDPLMMMDE EISVIDGEEA QVTQQPGHLF
     WPPGSALTAR LRRLVTAYQR SYKREQMKME AAERGDRRRR RCEAAFKLKE IARREKQQRW
     TRREQTDFYR VVSTFGVEYD PDNMQFHWDR FRTFARLDKK TDESLTKYFH GFVAMCRQVC
     RLPPAAGDEP PDPNLFIEPI TEERASRTLY RIELLRRLRE QVLCHPLLED RLALCQPPGL
     ELPKWWEPVR HDGELLRGAA RHGVSQTDCN IMQDPDFSFL AARMNYMQNH QAGASAASLS
     RCSTPLLHQQ CTSRTASPSP LRPDAPVEKS PEESTVQVPN LESLTLKLED EVVARSRLTS
     QDYEVRVGSS DTAPLSRSVP PVKLEDEDDS DSELDLSKLS PSSSSSSSSS SSSSSTDESE
     DEKEEKLTAD RSRPKLYDEE SLLSLTMSQD GFPNEDGEQM TPELLLLQER QRASEWPKDR
     VLINRIDLVC QAVLSGKWPS NRRSQEVTAG GILGPGNHLL DSPSLTPGED GDSPVPTPRS
     GSAASMAEEE ASAVTTAAAQ FTKLRRGMDE KEFTVQIKDE EGLKLTFQKH RLMANGVMGD
     GHPLFHKKKG NRKKLVELEV ECMEEPNHLD LDLETRIPVI NKVDGTLLVG DEAPRRAELE
     MWLQGHPEFA VDPRFLAYME ERRKQKWQRC KKNNKAELNC LGMEPVQPAN SRNGKKGHYA
     ETAFNRVLPG PVAPENSKKR VRRTRPDLSK MMALMQGGST GSLSLHNTFQ HSSSNLQSVS
     SLGHSSTTSA SLPFMPFVMG AAAPPHVDSS TMLHHHHHHP HPHHHHHHHP GLRTTGYPSS
     PATTTSGTAL RLPTLQPEDD DEEEDEEDDD LSQGYDSSER DFSLIDDPMM PANSDSSEDA
     DD
//
ID   CNNM1_MOUSE             Reviewed;         951 AA.
AC   Q0GA42; Q9JIQ6;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 5.
DT   08-MAR-2011, entry version 36.
DE   RecName: Full=Metal transporter CNNM1;
DE   AltName: Full=Ancient conserved domain-containing protein 1;
DE            Short=mACDP1;
DE   AltName: Full=Cyclin-M1;
DE   AltName: Full=Cyclin-like protein 1;
DE            Short=CLP-1;
GN   Name=Cnnm1; Synonyms=Acdp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-176.
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 257-951, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=14723793; DOI=10.1186/1471-2164-5-7;
RA   Wang C.-Y., Yang P., Shi J.-D., Purohit S., Guo D., An H., Gu J.-G.,
RA   Ling J., Dong Z., She J.-X.;
RT   "Molecular cloning and characterization of the mouse Acdp gene
RT   family.";
RL   BMC Genomics 5:7-7(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 342-951.
RC   STRAIN=Swiss; TISSUE=Testis;
RA   Chandran U., Laloraya M., Kumar P.G.;
RT   "Cyclin-like protein 1 (CLP-1) in mouse testis.";
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable metal transporter (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: In brain, it is present in hippocampus neurons
CC       (at protein level). Restricted to brain and testis. Highly
CC       expressed in brain, and weakly expressed in testis and kidney.
CC   -!- MISCELLANEOUS: Shares weak sequence similarity with the cyclin
CC       family, explaining its name. However it has no cyclin-like
CC       function in vivo.
CC   -!- SIMILARITY: Belongs to the ACDP family.
CC   -!- SIMILARITY: Contains 2 CBS domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF86371.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=AAF86371.1; Type=Frameshift; Positions=292;
CC       Sequence=ABI34706.3; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; AC140375; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BB645731; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AF202994; AAF86371.1; ALT_SEQ; mRNA.
DR   EMBL; DQ885890; ABI34706.3; ALT_INIT; mRNA.
DR   IPI; IPI00120943; -.
DR   RefSeq; NP_113573.2; NM_031396.2.
DR   UniGene; Mm.329864; -.
DR   ProteinModelPortal; Q0GA42; -.
DR   SMR; Q0GA42; 391-565.
DR   STRING; Q0GA42; -.
DR   PRIDE; Q0GA42; -.
DR   Ensembl; ENSMUST00000026195; ENSMUSP00000026195; ENSMUSG00000025189.
DR   GeneID; 83674; -.
DR   KEGG; mmu:83674; -.
DR   CTD; 83674; -.
DR   MGI; MGI:1891366; Cnnm1.
DR   eggNOG; roNOG09236; -.
DR   GeneTree; ENSGT00390000002383; -.
DR   HOGENOM; HBG715526; -.
DR   HOVERGEN; HBG074775; -.
DR   InParanoid; Q0GA42; -.
DR   OrthoDB; EOG42NHZS; -.
DR   NextBio; 350713; -.
DR   ArrayExpress; Q0GA42; -.
DR   Bgee; Q0GA42; -.
DR   CleanEx; MM_CNNM1; -.
DR   Genevestigator; Q0GA42; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000644; Cysta_beta_synth_core.
DR   InterPro; IPR002550; DUF21.
DR   Pfam; PF00571; CBS; 1.
DR   Pfam; PF01595; DUF21; 1.
DR   SMART; SM00116; CBS; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   1: Evidence at protein level;
KW   CBS domain; Cell membrane; Ion transport; Membrane; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    951       Metal transporter CNNM1.
FT                                /FTId=PRO_0000295759.
FT   TRANSMEM     23     43       Helical; (Potential).
FT   TRANSMEM    222    242       Helical; (Potential).
FT   TRANSMEM    282    302       Helical; (Potential).
FT   TRANSMEM    319    339       Helical; (Potential).
FT   DOMAIN      433    495       CBS 1.
FT   DOMAIN      502    568       CBS 2.
FT   CONFLICT    385    385       R -> P (in Ref. 4; ABI34706).
FT   CONFLICT    708    708       C -> F (in Ref. 3; AAF86371).
SQ   SEQUENCE   951 AA;  103980 MW;  F43F9F794C2C9830 CRC64;
     MAAAAAAAAA LGVRLRDCCS RGAVLLLFFS LSPRPPAAAA WLLGLRPEDT AGGRVSLEGG
     TLRAAEGTSF LLRVYFQPGP PVPAAPVPAP SLAPGENGTG DWAPRLVFIE EPPGAGGAAP
     SAVPTRPPGP QRCREQSDWA SDVEVLGPLR PGGVAGSALV QVRVRELRKG EAERGGAGGG
     GKLFSLCAWD GRAWHHHGAA GGFLLRVRPR LYGPGGDLLP PAWLRALGAL LLLALSALFS
     GLRLSLLSLD PVELRVLRNS GSAAEQEQAR RVQAVRGRGT HLLCTLLLGQ AGANAALAGW
     LYASLPPGVG DPGEDSGEAG VHFPWLPALV CTGAVFLGAE ICPYSVCSRH GLAIASHSVC
     LTRLLMAAAF PVCYPLGRLL DWALRQEIST FYTREKLLET LRAADPYSDL VKEELNIIQG
     ALELRTKVVE EVLTPLGDCF MLRSDAVLDF ATVSEILRSG YTRIPVYEGD QRHNIVDILF
     VKDLAFVDPD DCTPLLTVTR FYNRPLHCVF NDTRLDTVLE EFKKGKSHLA IVQRVNNEGE
     GDPFYEVMGI VTLEDIIEEI IKSEILDETD LYTDNRKKQR VPHRERRRHD FSLFKLSDSE
     IRVKISPQLL LATHRFMATE VEPFKSLYLS EKILLRLLKH PNVIQELKFD ERNKKAPEHY
     LYQRNRPVDY FVLLLQGKVE VEVGKEGLRF ENGAFTYYGV PAIMTSACSD NDVRKVGSLA
     GSSVFLNRSP SRCSGLNRSE SPNRERSDFG GSNTQLYSSS NNLYTPDYSV HILSDVQFVK
     ITRQQYQNAL TACHMDSSPQ SPDMEAFTDG DSTKAPTTRG TPQTPKDDPV LTLLSNRTSL
     PCSRSDGLRS PGEVVYLRME EMAFPQEEMP NFEEHRSQQV SLSPVAVPTT AASDPECCNI
     HLDPEASPCS SDSEENMGKK LLRTLSGRKR KKSADGERAS EENSNLTPLI T
//
ID   INF2_MOUSE              Reviewed;        1273 AA.
AC   Q0GNC1; Q14C56; Q499F7; Q6P9T3;
DT   14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=Inverted formin-2;
GN   Name=Inf2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, DOMAIN,
RP   ENZYME REGULATION, AND MUTAGENESIS OF LEU-1009; LEU-1010 AND LEU-1019.
RC   STRAIN=BALB/c;
RX   PubMed=16818491; DOI=10.1074/jbc.M604666200;
RA   Chhabra E.S., Higgs H.N.;
RT   "INF2 Is a WASP homology 2 motif-containing formin that severs actin
RT   filaments and accelerates both polymerization and depolymerization.";
RL   J. Biol. Chem. 281:26754-26767(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 546-1273 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 556-1273 (ISOFORM 1).
RC   STRAIN=C3H/He, and C57BL/6; TISSUE=Mesenchymal stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-909, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1216, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Severs actin filaments and accelerates their
CC       polymerization and depolymerization.
CC   -!- ENZYME REGULATION: Phosphate inhibits both the depolymerization
CC       and severing activities.
CC   -!- SUBUNIT: Interacts with profilin and actin at the FH1 and FH2
CC       domains respectively.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q0GNC1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q0GNC1-3; Sequence=VSP_021560;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The WH2 domain acts as the DAD (diaphanous autoregulatory)
CC       domain and binds to actin monomers.
CC   -!- DOMAIN: Regulated by autoinhibition due to intramolecular GBD-DAD
CC       binding.
CC   -!- DOMAIN: The severing activity is dependent on covalent attachment
CC       of the FH2 domain to the C-terminus.
CC   -!- SIMILARITY: Belongs to the formin homology family.
CC   -!- SIMILARITY: Contains 1 FH1 (formin homology 1) domain.
CC   -!- SIMILARITY: Contains 1 FH2 (formin homology 2) domain.
CC   -!- SIMILARITY: Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology
CC       3) domain.
CC   -!- SIMILARITY: Contains 1 WH2 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH60610.1; Type=Erroneous initiation;
CC       Sequence=AAH99931.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; DQ834374; ABI20145.1; -; mRNA.
DR   EMBL; BC060610; AAH60610.1; ALT_INIT; mRNA.
DR   EMBL; BC099931; AAH99931.1; ALT_INIT; mRNA.
DR   EMBL; BC115422; AAI15423.2; -; mRNA.
DR   EMBL; BC115423; AAI15424.2; -; mRNA.
DR   IPI; IPI00678133; -.
DR   IPI; IPI00762596; -.
DR   RefSeq; NP_940803.2; NM_198411.2.
DR   UniGene; Mm.250193; -.
DR   ProteinModelPortal; Q0GNC1; -.
DR   SMR; Q0GNC1; 5-332, 590-1022.
DR   STRING; Q0GNC1; -.
DR   PhosphoSite; Q0GNC1; -.
DR   PRIDE; Q0GNC1; -.
DR   Ensembl; ENSMUST00000101029; ENSMUSP00000098591; ENSMUSG00000037679.
DR   GeneID; 70435; -.
DR   KEGG; mmu:70435; -.
DR   UCSC; uc007pes.1; mouse.
DR   UCSC; uc007pet.1; mouse.
DR   CTD; 70435; -.
DR   MGI; MGI:1917685; Inf2.
DR   eggNOG; roNOG15594; -.
DR   GeneTree; ENSGT00560000076948; -.
DR   HOGENOM; HBG505533; -.
DR   HOVERGEN; HBG081794; -.
DR   InParanoid; Q0GNC1; -.
DR   OrthoDB; EOG49W2DN; -.
DR   NextBio; 331621; -.
DR   ArrayExpress; Q0GNC1; -.
DR   Bgee; Q0GNC1; -.
DR   Genevestigator; Q0GNC1; -.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   InterPro; IPR003104; Actin-bd_FH2/DRF_autoreg.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR010472; Drf_FH3.
DR   InterPro; IPR010473; Drf_GTPase-bd.
DR   InterPro; IPR015425; FH2_actin-bd.
DR   InterPro; IPR014768; GTPase-bd/formin_homology_3.
DR   InterPro; IPR003124; WH2_actin-bd.
DR   Pfam; PF06367; Drf_FH3; 1.
DR   Pfam; PF06371; Drf_GBD; 1.
DR   Pfam; PF02181; FH2; 1.
DR   Pfam; PF02205; WH2; 1.
DR   SMART; SM00498; FH2; 1.
DR   SMART; SM00246; WH2; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF101447; FH2_actin_bd; 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
DR   PROSITE; PS51082; WH2; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Coiled coil; Cytoplasm;
KW   Phosphoprotein.
FT   CHAIN         1   1273       Inverted formin-2.
FT                                /FTId=PRO_0000259890.
FT   DOMAIN        1    330       GBD/FH3.
FT   DOMAIN      421    564       FH1.
FT   DOMAIN      589    979       FH2.
FT   DOMAIN     1007   1022       WH2.
FT   COILED      907    984       Potential.
FT   COMPBIAS    421    563       Pro-rich.
FT   MOD_RES     909    909       Phosphoserine.
FT   MOD_RES    1172   1172       Phosphoserine (By similarity).
FT   MOD_RES    1173   1173       Phosphothreonine (By similarity).
FT   MOD_RES    1174   1174       Phosphoserine (By similarity).
FT   MOD_RES    1203   1203       Phosphothreonine (By similarity).
FT   MOD_RES    1212   1212       Phosphoserine (By similarity).
FT   MOD_RES    1216   1216       Phosphoserine.
FT   MOD_RES    1218   1218       Phosphoserine (By similarity).
FT   MOD_RES    1223   1223       Phosphothreonine (By similarity).
FT   MOD_RES    1225   1225       Phosphoserine (By similarity).
FT   MOD_RES    1226   1226       Phosphoserine (By similarity).
FT   MOD_RES    1228   1228       Phosphoserine (By similarity).
FT   MOD_RES    1230   1230       Phosphothreonine (By similarity).
FT   VAR_SEQ    1256   1273       EFVPDSDDIKAKRLCVIQ -> GLRSRPKAK (in
FT                                isoform 2).
FT                                /FTId=VSP_021560.
FT   MUTAGEN    1009   1009       L->A: Strongly inhibits depolymerization;
FT                                when associated with A-1010 and A-1019.
FT   MUTAGEN    1010   1010       L->A: Strongly inhibits depolymerization;
FT                                when associated with A-1009 and A-1019.
FT   MUTAGEN    1019   1019       L->A: Strongly inhibits depolymerization;
FT                                when associated with A-1009 and A-1010.
FT   CONFLICT   1038   1038       T -> A (in Ref. 2; AAH60610/AAI15423).
FT   CONFLICT   1167   1167       Q -> R (in Ref. 2; AAH60610/AAI15423).
SQ   SEQUENCE   1273 AA;  138560 MW;  C4438AD8A7041476 CRC64;
     MSVKEGAQRK WAALKEKLGP QDSDPTEANL ESAEPELCIR LLQMPSVVNY SGLRKRLESS
     DGGWMVQFLE QSGLDLLLEA LARLSGRGVA RISDALLQLT CISCVRAVMN SQQGIEYILS
     NQGYVRQLSQ ALDTSNVMVK KQVFELLAAL CIYSPEGHAL TLDALDHYKM VCSQQYRFSV
     IMSELSDSDN VPYVVTLLSV INAIILGPED LRSRAQLRSE FIGLQLLDIL TRLRDLEDAD
     LLIQLEAFEE AKAEDEEELQ RISDGINMNS HQEVFASLFH KVSCSPASAQ LLSVLQGLMH
     LEPAGRSGQL LWEALENLVN RAVLLASDAQ ACTLEEVVER LLSIKGRPRP SPLDKAHKSV
     QTNSVQNQGS SSQNTTTPTT KVEGQQPVVA SPCQHVGSIQ SSSVDIAPQP VALEQCITAL
     PLPTPPLSSS TPVLPPTPPP LPGPGATSPL PPPPPPLPPP LPGSGTTSPP PPPPPPPPLP
     PPLPGSGTIS PPPPPPPPPL PGTGAVSPPP PPPLPSLPDS HKTQPPPPPP PPLPGMCPVP
     PPPPLPRAGQ IPPPPPLPGF SVPSMMGGVE EIIVAQVDHS LGSAWVPSHR RVNPPTLRMK
     KLNWQKLPSN VARERNSMWA TLGSPCTAAV EPDFSSIEQL FSFPTAKPKE PSAAPARKEP
     KEVTFLDSKK SLNLNIFLKQ FKCSNEEVTS MIQAGDTSKF DVEVLKQLLK LLPEKHEIEN
     LRAFTEERAK LSNADQFYVL LLDIPCYPLR VECMMLCEGT AIVLDMVRPK AQLVLTACES
     LLTSQRLPVF CQLILKIGNF LNYGSHTGDA DGFKISTLLK LTETKSQQSR VTLLHHVLEE
     VEKSHPDLLQ LSRDLEPPSQ AAGINVEIIH SEASANLKKL LEAERKVSAS IPEVQKQYAE
     RLQASIEASQ ELDKVFDAIE QKKLELADYL CEDPQQLSLE DTFSTMKTFR DLFTRALKEN
     KDRKEQMAKA ERRKQQLAEE EARRPRDEDG KPIRKGPGKQ EEVCVIDALL ADIRKGFQLR
     KTARGRGDTE ASGRVAPTDP PKATEPATAS NPTQGTNHPA SEPLDTTAAD EPQGWDLVDA
     VTPSPQPSKE EDGPPALERR SSWYVDAIDF LDPEDTPDAQ PSEGVWPVTL GDGQALNPLE
     FSSNKPPGVK SSHQDATDPE ALWGVHQTEA DSTSEGPEDE AQRGQSTHLP RTGPGEDEDG
     EDTAPESALD TSLDRSFSED AVTDSSGSGT LPRVQGRVSK GTSKRRKKRP SRNQEEFVPD
     SDDIKAKRLC VIQ
//
ID   UNC79_MOUSE             Reviewed;        2596 AA.
AC   Q0KK59; Q0KK54; Q6L9U9; Q8CCC5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   08-MAR-2011, entry version 38.
DE   RecName: Full=Protein unc-79 homolog;
GN   Name=Kiaa1409; Synonyms=Unc79;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=BALB/cCrSlc; TISSUE=Brain;
RX   PubMed=16807365; DOI=10.1096/fj.06-5952fje;
RA   Nakayama M., Iida M., Koseki H., Ohara O.;
RT   "A gene-targeting approach for functional characterization of KIAA
RT   genes encoding extremely large proteins.";
RL   FASEB J. 20:1718-1720(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 740-2596.
RC   TISSUE=Brain;
RX   PubMed=14680840; DOI=10.1016/j.bbrc.2003.10.193;
RA   Nakayama M., Ohara O.;
RT   "A system using convertible vectors for screening soluble recombinant
RT   proteins produced in Escherichia coli from randomly fragmented
RT   cDNAs.";
RL   Biochem. Biophys. Res. Commun. 312:825-830(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2123-2596.
RC   STRAIN=C57BL/6J; TISSUE=Colon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1242, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   INTERACTION WITH NALCN AND UNC80.
RX   PubMed=19092807; DOI=10.1038/nature07579;
RA   Lu B., Su Y., Das S., Wang H., Wang Y., Liu J., Ren D.;
RT   "Peptide neurotransmitters activate a cation channel complex of NALCN
RT   and UNC-80.";
RL   Nature 457:741-744(2009).
CC   -!- FUNCTION: Component of the NALCN sodium channel complex, a cation
CC       channel activated either by neuropeptides substance P or
CC       neurotensin that controls neuronal excitability.
CC   -!- SUBUNIT: Interacts with NALCN and UNC80.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the unc-79 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC28287.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AB257853; BAF03196.1; -; mRNA.
DR   EMBL; AB257858; BAF03201.1; -; Genomic_DNA.
DR   EMBL; AB093296; BAD02453.1; -; mRNA.
DR   EMBL; AK033439; BAC28287.1; ALT_INIT; mRNA.
DR   IPI; IPI00668872; -.
DR   RefSeq; NP_001074486.2; NM_001081017.2.
DR   UniGene; Mm.387073; -.
DR   STRING; Q0KK59; -.
DR   PhosphoSite; Q0KK59; -.
DR   PRIDE; Q0KK59; -.
DR   Ensembl; ENSMUST00000101099; ENSMUSP00000098659; ENSMUSG00000021198.
DR   GeneID; 217843; -.
DR   UCSC; uc007ouw.1; mouse.
DR   MGI; MGI:2684729; Unc79.
DR   eggNOG; roNOG12212; -.
DR   HOGENOM; HBG505600; -.
DR   HOVERGEN; HBG082678; -.
DR   InParanoid; Q0KK59; -.
DR   OMA; PENDNTI; -.
DR   OrthoDB; EOG480HVR; -.
DR   ArrayExpress; Q0KK59; -.
DR   Bgee; Q0KK59; -.
DR   CleanEx; MM_9030205A07RIK; -.
DR   Genevestigator; Q0KK59; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1   2596       Protein unc-79 homolog.
FT                                /FTId=PRO_0000315619.
FT   TRANSMEM   2184   2204       Helical; (Potential).
FT   TRANSMEM   2426   2446       Helical; (Potential).
FT   MOD_RES    1242   1242       Phosphoserine.
SQ   SEQUENCE   2596 AA;  290740 MW;  2FA26FC00CF5377B CRC64;
     MSTKAEQFAS KIRYLQEYHN RVLHNIYPVP SGTDIANTLK YFSQTLLSIL SRTGKKENQD
     ASNLTVPMTM CLFPVPFPLT PSLRPQVSSI NPTVTRSLLY SVLRDAPSER GPQSRDAQLS
     DYPSLDYQGL YVTLVTLLDL VPLLQHGQHD LGQSIFYTTT CLLPFLNDDV LSTLPYTMIS
     TLATFPPFLH KDIIEYLSTS FLPMAILGSS GREGVPAHVN LSASSMLMIA MQYTSNPVYH
     CQLLECLMKY KQEVWKDLLY VIAYGPSQVK PPAVQMLFHY WPNLKPPGAI SEYRGLQYTA
     WNPIHCQHIE CHNAINKPAV KMCIDPSLSV ALGDKPPPLY LCEECSERIS GDHSEWLIDV
     LLPQAEISAI CQKKNCSSHV RRAVVTCFSA GCCGRHGNRP VRYCKRCHSN HHSNEVGATA
     ETHLYQTSPP PINTRECGAE ELVCAVEAVI SLLKEAEFHA EQREHELNRR RQLGLSSSHH
     SLDNTDFDNK DDDKHDQRLL SQFGIWFLVS LCTPSENTPT ESLARLVAMV FQWFHSTAYM
     MDDEVGSLVE KLKPQFVTKW LKTVCDVRFD VMVMCLLPKP MEFARVGGYW DKSCSTVTQL
     KEGLNRILCL IPYNVISQSV WECIMPEWLE AIRTEVPDNQ LKEFREVLSK MFDIELCPLP
     FSMEEMFGFI SCRFTGYPST VQEQALLWLH VLSELDITVP LQLLISMFSD GVNSVKELAN
     QRKSRANELA GNLASRRVSV ASDPGRRGQH NTLSPFHSPF QSPFRSPMRS PFRSPFKNFG
     HPGGRTIDFD CEDDDMNLNC FILMFDLLLK QMELQDDGIT MGLEHSLSKD IISIINNVFQ
     APWGGSHSCQ KDKKATECNL CQSSILCYQL ACELLERLAP KEESRLVEPT DSLEDSLLSS
     RPEFILGPEG EEEENPAAKH GENPGNRTVP SEHAAIKNDT ERKFCYQQLP VTLRLIYTIF
     QEMAKFEEPD ILFNMLNCLK ILCLHGECLY TARKDHPQFL AYIQDHMLIA SLWRVVKSEF
     SQLSSLAVPL LLHALSLPHG ADIFWTIING NFNSKDWKMR FEAVEKVAVI CRFLDIHSVT
     KNHLLKYSLA HAFCCFLTAV EDVNPAVATR AGLLLDTIKR PALQGLCLCL DFQFDTVVKD
     RPTILSKLLL LHFLKQDIPA LSWEFFVNRF ETLSLEAQLH LDCNKEFPFP TTITAVRTNV
     ANLSDAALWK IKRARFARNR QKSVRSLRDS VKGPAESKRA LSLPETLTSK IRQQSPENDN
     TIKDLLPEDA GIDHQTVHQL ITVLMKFMAR DESSAESDIS SAKAFNTVKR HLYVLLGYDQ
     QEGCFMIAPQ KMRLSTCFNA FIAGIAQVMD YNINLGKHLL PLVVQVLKYC SCPQLRHYFQ
     QPPRCSLWSL KPHIRQMWLK ALLVILYKYP YRDCDVSKTL LHLIHITVNT LNAQYHSCKP
     HATAGPLYTD NSNISRYSEK EKGEIELAEY RETGALQDSV LHCVREESIQ KKKLRSLKQK
     SLDIGNADSL LFTLDEHRRK SCIDRCDIDK PPAQAAYISQ RQNDHHGRSR QNSATRPDNT
     EIPKNPGTEG FQEIRRPVIP EVRLNCMETF EVRVDSPGKP APREDLDLID LSSDSTSGPE
     KHSILSTSDS DSLVFEPLPP LRIVESDEEE EMMNQGNGGA LGNNAASSPS IPSQPSVLSL
     STTPLVQVSV EDCSKDFSSK DSGNHQSASN EDSTIAALDD LTDSEELSKS EELREFASGS
     PLTLKQKRDL LQKSSAVPEM SVDYNPEPSP AEEKPGQTPT SGVKTVLLKV PEDGENLIES
     EKPNTSAESD TEQNPERKVE EDGAEESEFK IQIVPRQRKQ RKIAVSAIQR EYLDISFNIL
     DKLGEQKDPD PSAKGLSTLE MPRESSSAPT LEAGAPETSS HSSISKQIQP GKRQCNVPMC
     LNPDLEGQPL RTRGATKSSL LSAPSIASMF VPAPEEFTEE QPTVMADKCH DCGAILEEYD
     EETLGLAIVV LSTFIHLSPD LAAPLLLDIM QSVGRLASST TFSNQAESMM VPGNAAGVAK
     QFLRCIFHQL APNGIFPQLF QSAIKDGTFL RTLATSLMDF NELSSIAALS QLLEGLNNKK
     NLPAGGAMIR CLENIATFME ALPMDSPSSL WTTISNQFQT FFAKLPCVLP LKCSLDSSLR
     IMICLLKIPS TNATRSLLEP FSKLLSFVIQ NAVFTLAYLV ELCGLCYRAF TKERDKFYLS
     RSVVLELLQA LKLKSPLPDT NLLLLVQFIC ADAGTKLAES TILSKQMIAS VPGCGTAAME
     CIRQYVSEVL EFMADMHTLT KLKSHMKTCS QPLHEDTFGG HLKVGLAQIA AMEISRGNHR
     DNKAVIRYLP WLYHPPSAMQ QGPKEFIECV SHIRLLSWLL LGSLTHNAVC PNASSPCLPI
     PLDAGSHIAD HLIVILIGFP EQSKTCVLHM CSLFHAFIFA QLWTVYCEQS AVATNVQNQN
     EFSFTAILTA LEFWSRVTPS ILQLMAHNKV MVEMVCLHVI SLMEALQECN STIFVKLIPM
     WLPMIQSNTK HLSAGLQLRL QAIQNNVNHH SLRTLPGSGQ SSAGLAALRK WLQCTQFKMA
     QVEIQSSEAA SQFYPL
//
ID   UBX2B_MOUSE             Reviewed;         331 AA.
AC   Q0KL01; Q8BGY8; Q8CCQ0; Q9CZA8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=UBX domain-containing protein 2B;
DE   AltName: Full=NSFL1 cofactor p37;
DE   AltName: Full=p97 cofactor p37;
GN   Name=Ubxn2b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH VCP.
RX   PubMed=17141156; DOI=10.1016/j.devcel.2006.10.016;
RA   Uchiyama K., Totsukawa G., Puhka M., Kaneko Y., Jokitalo E.,
RA   Dreveny I., Beuron F., Zhang X., Freemont P., Kondo H.;
RT   "p37 is a p97 adaptor required for Golgi and ER biogenesis in
RT   interphase and at the end of mitosis.";
RL   Dev. Cell 11:803-816(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Head;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
CC   -!- FUNCTION: Adapter protein required for Golgi and endoplasmic
CC       reticulum biogenesis. Involved in Golgi and endoplasmic reticulum
CC       maintenance during interphase and in their reassembly at the end
CC       of mitosis. The complex formed with VCP has membrane fusion
CC       activity; membrane fusion activity requires USO1-GOLGA2 tethering
CC       and BET1L. VCPIP1 is also required, but not its deubiquitinating
CC       activity (By similarity).
CC   -!- SUBUNIT: Interacts with VCP. Does not bind ubiquitin.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm, cytosol
CC       (By similarity). Endoplasmic reticulum (By similarity). Golgi
CC       apparatus (By similarity).
CC   -!- SIMILARITY: Belongs to the NSFL1C family.
CC   -!- SIMILARITY: Contains 1 SEP domain.
CC   -!- SIMILARITY: Contains 1 UBX domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AB120715; BAF30880.1; -; mRNA.
DR   EMBL; AK012822; BAB28494.1; -; mRNA.
DR   EMBL; AK028268; BAC25851.1; -; mRNA.
DR   EMBL; AK032332; BAC27819.1; -; mRNA.
DR   EMBL; AK049018; BAC33515.1; -; mRNA.
DR   EMBL; AL772385; CAM21532.1; -; Genomic_DNA.
DR   EMBL; BC076632; AAH76632.1; -; mRNA.
DR   IPI; IPI00308198; -.
DR   RefSeq; NP_080810.2; NM_026534.2.
DR   UniGene; Mm.404043; -.
DR   UniGene; Mm.427021; -.
DR   ProteinModelPortal; Q0KL01; -.
DR   SMR; Q0KL01; 140-208, 215-331.
DR   PhosphoSite; Q0KL01; -.
DR   PRIDE; Q0KL01; -.
DR   Ensembl; ENSMUST00000029907; ENSMUSP00000029907; ENSMUSG00000028243.
DR   GeneID; 68053; -.
DR   KEGG; mmu:68053; -.
DR   CTD; 68053; -.
DR   MGI; MGI:1915303; Ubxn2b.
DR   eggNOG; maNOG06579; -.
DR   GeneTree; ENSGT00520000055567; -.
DR   HOGENOM; HBG717153; -.
DR   HOVERGEN; HBG054517; -.
DR   InParanoid; Q0KL01; -.
DR   OMA; ELYEDEM; -.
DR   OrthoDB; EOG49S66V; -.
DR   PhylomeDB; Q0KL01; -.
DR   NextBio; 326324; -.
DR   ArrayExpress; Q0KL01; -.
DR   Bgee; Q0KL01; -.
DR   Genevestigator; Q0KL01; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR012989; SEP_domain.
DR   InterPro; IPR001012; UBX.
DR   Pfam; PF08059; SEP; 1.
DR   Pfam; PF00789; UBX; 1.
DR   SMART; SM00553; SEP; 1.
DR   SMART; SM00166; UBX; 1.
DR   SUPFAM; SSF102848; SEP; 1.
DR   PROSITE; PS51399; SEP; 1.
DR   PROSITE; PS50033; UBX; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Endoplasmic reticulum; Golgi apparatus; Nucleus;
KW   Phosphoprotein.
FT   CHAIN         1    331       UBX domain-containing protein 2B.
FT                                /FTId=PRO_0000315229.
FT   DOMAIN      141    206       SEP.
FT   DOMAIN      252    329       UBX.
FT   MOD_RES      56     56       Phosphoserine (By similarity).
FT   MOD_RES      59     59       Phosphothreonine (By similarity).
FT   MOD_RES     231    231       Phosphoserine (By similarity).
FT   MOD_RES     232    232       Phosphothreonine (By similarity).
FT   MOD_RES     234    234       Phosphoserine (By similarity).
FT   MOD_RES     235    235       Phosphoserine.
FT   CONFLICT      8      8       E -> K (in Ref. 2; BAB28494).
FT   CONFLICT     23     23       S -> N (in Ref. 2; BAC27819).
FT   CONFLICT    164    164       S -> N (in Ref. 1; BAF30880).
SQ   SEQUENCE   331 AA;  37444 MW;  61AD4AD6FE784FFA CRC64;
     MAEGGRAEPE EQERGSSRPR PPSARDLQLA LAELYEDEMK CKSSKPDRST PATCRSPRTP
     PHRLYSGDHK YDGLHIVQPP TGKIVNELFK EAREHGAVPL NEATRSSRED KTKSFTGGGY
     RLGNSFYKRS EYIYGENQLQ DVQVLLKLWR NGFSLDDGEL RPYSDPTNAQ FLESVKRGET
     PLELQRLVHG AQVNLDMEDH QDQEYIKPRL RFKAFSGEGQ KLGSLTPEIV STPSSPEEED
     KSILNAAVLI DDSMPTTKIQ IRLADGSRLV QRFNSTHRIL DVRDFIVRSR PEFATTDFIL
     VTSFPSKELT DETVTLQEAD ILNTVILQQL K
//
ID   TRIO_MOUSE              Reviewed;        3102 AA.
AC   Q0KL02; Q3U522; Q6P9K6; Q80W23;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 3.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=Triple functional domain protein;
DE            EC=2.7.11.1;
GN   Name=Trio;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY,
RP   MUTAGENESIS OF GLN-1427 AND LEU-1435, AND SUBCELLULAR LOCATION.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16943433; DOI=10.1128/MCB.02474-05;
RA   Sun Y.-J., Nishikawa K., Yuda K., Wang Y.-L., Osaka H., Fukazawa N.,
RA   Naito A., Wada K., Aoki S.;
RT   "Solo/Trio8, a membrane-associated short isoform of Trio, modulates
RT   endosome dynamics and neurite elongation.";
RL   Mol. Cell. Biol. 26:6923-6935(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2062-3102 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1145-3102 (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2521-3102 (ISOFORM 4).
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2458, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Promotes the exchange of GDP by GTP. Together with
CC       leukocyte antigen-related (LAR) protein, it could play a role in
CC       coordinating cell-matrix and cytoskeletal rearrangements necessary
CC       for cell migration and cell growth (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts to form a complex with leukocyte antigen
CC       related protein (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Isoform 2 localizes to early
CC       endosomes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q0KL02-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q0KL02-2; Sequence=VSP_023308, VSP_023309;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q0KL02-3; Sequence=VSP_037863, VSP_037864, VSP_037865;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q0KL02-4; Sequence=VSP_037863;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Widespread in the brain, with more intense
CC       signals in the hippocampus, olfactory bulb, cortical layers and
CC       cerebellum. Isoform 2 is predominantly expressed in Purkinje
CC       neurons of brain.
CC   -!- DOMAIN: The N-terminal DBL/GEF domain specifically catalyzes
CC       nucleotide exchange for RAC1, leading to the activation of Jun
CC       kinase and the production of membrane ruffles. The second DBL/GEF
CC       domain is an exchange factor for rhoa and induces the formation of
CC       stress fibers (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family.
CC   -!- SIMILARITY: Contains 1 CRAL-TRIO domain.
CC   -!- SIMILARITY: Contains 2 DH (DBL-homology) domains.
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 2 SH3 domains.
CC   -!- SIMILARITY: Contains 4 spectrin repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE32258.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AB106872; BAF30811.1; -; mRNA.
DR   EMBL; AC107452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC116808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC120373; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC130219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC051169; AAH51169.1; -; mRNA.
DR   EMBL; BC060724; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK153924; BAE32258.1; ALT_INIT; mRNA.
DR   IPI; IPI00604947; -.
DR   IPI; IPI00605176; -.
DR   IPI; IPI00943997; -.
DR   IPI; IPI00944152; -.
DR   RefSeq; NP_001074771.1; NM_001081302.1.
DR   UniGene; Mm.479896; -.
DR   ProteinModelPortal; Q0KL02; -.
DR   SMR; Q0KL02; 217-445, 565-715, 754-1011, 1255-1594, 1655-1721, 1960-2291, 2558-2783, 2791-3089.
DR   STRING; Q0KL02; -.
DR   PhosphoSite; Q0KL02; -.
DR   PRIDE; Q0KL02; -.
DR   Ensembl; ENSMUST00000090247; ENSMUSP00000087714; ENSMUSG00000022263.
DR   Ensembl; ENSMUST00000100733; ENSMUSP00000098299; ENSMUSG00000022263.
DR   GeneID; 223435; -.
DR   KEGG; mmu:223435; -.
DR   CTD; 223435; -.
DR   MGI; MGI:1927230; Trio.
DR   eggNOG; roNOG06885; -.
DR   GeneTree; ENSGT00560000076675; -.
DR   HOGENOM; HBG714943; -.
DR   HOVERGEN; HBG108598; -.
DR   InParanoid; Q0KL02; -.
DR   OrthoDB; EOG4H462T; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 376714; -.
DR   ArrayExpress; Q0KL02; -.
DR   Bgee; Q0KL02; -.
DR   CleanEx; MM_TRIO; -.
DR   Genevestigator; Q0KL02; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR001251; CRAL-bd_TRIO_C.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:3.40.525.10; CRAL_bd_TRIO_C; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 2.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00621; RhoGEF; 2.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF00435; Spectrin; 4.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00325; RhoGEF; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SMART; SM00326; SH3; 2.
DR   SMART; SM00150; SPEC; 6.
DR   SUPFAM; SSF52087; CRAL_TRIO_C; 1.
DR   SUPFAM; SSF48065; DH-domain; 2.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50044; SH3; 2.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
DR   PROSITE; PS00741; DH_1; FALSE_NEG.
DR   PROSITE; PS50010; DH_2; 2.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Disulfide bond;
KW   Guanine-nucleotide releasing factor; Immunoglobulin domain; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Repeat;
KW   Serine/threonine-protein kinase; SH3 domain; Transferase.
FT   CHAIN         1   3102       Triple functional domain protein.
FT                                /FTId=PRO_0000278474.
FT   DOMAIN       65    210       CRAL-TRIO.
FT   REPEAT      218    338       Spectrin 1.
FT   REPEAT      340    446       Spectrin 2.
FT   REPEAT      566    672       Spectrin 3.
FT   REPEAT      673    784       Spectrin 4.
FT   REPEAT      907   1012       Spectrin 5.
FT   REPEAT     1138   1244       Spectrin 6.
FT   DOMAIN     1292   1467       DH 1.
FT   DOMAIN     1479   1591       PH 1.
FT   DOMAIN     1656   1721       SH3.
FT   DOMAIN     1969   2145       DH 2.
FT   DOMAIN     2157   2271       PH 2.
FT   DOMAIN     2688   2778       Ig-like C2-type.
FT   DOMAIN     2799   3053       Protein kinase.
FT   NP_BIND    2805   2813       ATP (By similarity).
FT   COMPBIAS    715    718       Poly-Gln.
FT   COMPBIAS   1845   1850       Poly-Ser.
FT   COMPBIAS   1951   1954       Poly-Ser.
FT   COMPBIAS   2292   2324       Gly-rich.
FT   COMPBIAS   2296   2557       Ser-rich.
FT   ACT_SITE   2918   2918       Proton acceptor (By similarity).
FT   BINDING    2828   2828       ATP (By similarity).
FT   MOD_RES    1545   1545       Phosphothreonine (By similarity).
FT   MOD_RES    1903   1903       Phosphothreonine (By similarity).
FT   MOD_RES    2282   2282       Phosphoserine (By similarity).
FT   MOD_RES    2458   2458       Phosphoserine.
FT   MOD_RES    2462   2462       Phosphoserine (By similarity).
FT   MOD_RES    2470   2470       Phosphoserine (By similarity).
FT   DISULFID   2709   2762       By similarity.
FT   VAR_SEQ    1890   1908       ASSRLLVRPTSSETPSAAE -> HYVDLCSVSVLAQFPYLS
FT                                I (in isoform 2).
FT                                /FTId=VSP_023308.
FT   VAR_SEQ    1909   3102       Missing (in isoform 2).
FT                                /FTId=VSP_023309.
FT   VAR_SEQ    2548   2548       G -> GS (in isoform 3 and isoform 4).
FT                                /FTId=VSP_037863.
FT   VAR_SEQ    2549   2568       EGSSSSNISTMLVTHEYTAV -> VRVPGSLRPSTPPPLSR
FT                                QLF (in isoform 3).
FT                                /FTId=VSP_037864.
FT   VAR_SEQ    2569   3102       Missing (in isoform 3).
FT                                /FTId=VSP_037865.
FT   MUTAGEN    1427   1427       Q->A: Abolishes Rac1 activation; when
FT                                associated with E-1435.
FT   MUTAGEN    1435   1435       L->E: Abolishes Rac1 activation; when
FT                                associated with A-1427.
FT   CONFLICT   2863   2863       E -> K (in Ref. 4; BAE32258).
SQ   SEQUENCE   3102 AA;  347861 MW;  8E8F7C44CB4F72D0 CRC64;
     MSGSSGGATA PAASSGPAAA ASAAGSGCGG GAGEGAEEAA KDLADIAAFF RSGFRKNDEM
     KAMDVLPILK EKVAYLSGGR DKRGGPILTF PARSNHDRIR QEDLRRLISY LACIPSEEVC
     KRGFTVIVDM RGSKWDSIKP LLKILQESFP CCIHIALIIK PDNFWQKQRT NFGSSKFEFE
     TNMVSLEGLT KVVDPSQLTP EFDGCLEYNH EEWIEIRVAF EEYISNAAHM LSRLEELQDV
     LAKKELPQDL EGARNMIDEH SQLKKKVIKA PIEDLDLEGQ KLLQRIQSSD SFPKKNSGSG
     NADLQNLLPK VSTMLDRLHS TRQHLHQMWH VRKLKLDQCF QLRLFEQDAE KMFDWITHNK
     GLFLNSYTEI GTSHPHAMEL QTQHNHFAMN CMNVYVNINR IMSVANRLVE SGHYASQQIK
     QIANQLEQEW KAFAAALDER STLLDMSSIF HQKAEKYMSN VDSWCKACGE VDLPSELQDL
     EDAIHHHQGI YEHITLAYSE VSQDGKSLLD KLQRPLTPGS SDSLTASANY SKAVHHVLDV
     IHEVLHHQRQ LENIWQHRKV RLHQRLQLCV FQQDVQQVLD WIENHGEAFL SKHTGVGKSL
     HRARALQKRH EDFEEVAQNT YTNADKLLEA AEQLAQTGEC DPEEIYQAAH QLEDRIQDFV
     RRVEQRKILL DMSVSFHTHV KELWTWLEEL QKELLDDVYA ESVEAVQDLI KRFGQQQQTT
     LQVTVNVIKE GEDLIQQLRD SAISSNKTPH NSSINHIETV LQQLDEAQSQ MEELFQERKI
     KLELFLQLRI FERDAIDIIS DLESWNDELS QQMNDFDTED LTIAEQRLQH HADKALTMNN
     LTFDVIHQGQ DLLQYVNEVQ ASGVELLCDR DVDMATRVQD LLEFLHEKQQ ELDLAAEQHR
     KHLEQCVQLR HLQAEVKQVL GWIRNGESML NAGLITASSL QEAEQLQREH EQFQHAIEKT
     HQSALQVQQK AEAMLQANHY DMDMIRDCAE KVASHWQQLM LKMEDRLKLV NASVAFYKTS
     EQVCSVLESL EQEYKREEDW CGGADKLGPN SETDHVTPMI SKHLEQKEAF LKACTLARRN
     ADVFLKYLHR NSVSMPGMVT HIKAPEQQVK NILNELFQRE NRVLHYWTMR KRRLDQCQQY
     VVFERSAKQA LEWIHDNGEF YLSTHTSTGS SIQHTQELLK EHEEFQITAK QTKERVKLLI
     QLADGFCEKG HAHAAEIKKC VTAVDKRYRD FSLRMEKYRT SLEKALGISS DSNKSSKSLQ
     LDIIPASIPG SEVKLRDAAH ELNEEKRKSA RRKEFIMAEL IQTEKAYVRD LRECMDTYLW
     EMTSGVEEIP PGIVNKELII FGNMQEIYEF HNNIFLKELE KYEQLPEDVG HCFVTWADKF
     QMYVTYCKNK PDSTQLILEH AGSYFDEIQQ RHGLANSISS YLIKPVQRIT KYQLLLKELL
     TCCEEGKGEI KDGLEVMLSV PKRANDAMHL SMLEGFDENI ESQGELILQE SFQVWDPKTL
     IRKGRERHLF LFEMSLVFSK EVKDSSGRSK YLYKSKLFTS ELGVTEHVEG DPCKFALWVG
     RTPTSDNKIV LKASSIENKQ DWIKHIREVI QERTVHLRGA LKEPIHIPKT APAARQKGRR
     DGEDLDSQGD GSSQPDTISI ASRTSQNTLD SDKLSGGCEL TVVIHDFTAC NSNELTIRRG
     QTVEVLERPH DKPDWCLVRT TDRSPAAEGL VPCGSLCIAH SRSSMEMEGI FNHKDSLSVS
     SNDASPPASV ASLQPHMIGA QSSPGPKRPG NTLRKWLTSP VRRLSSGKAD GHAKKLAHKH
     KKSREVRKSA DAGSQKDSDD SAATPQDETI EERGRNEGLS SGTLSKSSSS GMQSCGEEEG
     EEGADAVPLP PPMAIQQHSL LQPDSQDDKA SSRLLVRPTS SETPSAAELV SAIEELVKSK
     MALEDRPSSL LVDQGDSSSP SFNPSDNSLL SSSSPIDEME ERKCSSLKRR HYVLQELVET
     ERDYVRDLGC VVEGYMALMK EDGVPDDMKG KDKIVFGNIH QIYDWHRDFF LGELEKCLED
     PEKLGSLFVK HERRLHMYIV YCQNKPKSEH IVSEYIDTFF EDLKQRLGHR LQLTDLLIKP
     VQRIMKYQLL LKDFLKYSKK ASLDTSELEK AVEVMCIVPK RCNDMMNVGR LQGFDGKIVA
     QGKLLLQDTF LVTDQDAGLL PRCKERRVFL FEQIVIFSEP LDKKKGFSMP GFLFKNSIKV
     SCLCLEENVE SDPCKFALTS RTGDAVETFV LHSSSPSVRQ TWIHEINQIL ENQRNFLNAL
     TSPIEYQRNH SGGGGSGSGG SSGGGGGSGG SGASSGGSSS HGSGPSSCSS GPSSSRSRPS
     RIPQPVRHHP PMLVSSAASS QAEADKMSGM SAPSPSLPTP SSSLALEASL GQPSRLPLSG
     DSEGHERETE PIPKMKVMES PRKAPGSTSG TSQDGNTKDA RGNLGSLPLG KTRPGAVSPL
     NSPLSTTFPS PFGKEAFPPS SPLQKGGSFW SSIPASPASR PSSFTFPGDS DSLQRQTHRH
     AAPSKDTDRM STCSSASEQS VQSTQSNGEG SSSSNISTML VTHEYTAVKE DEINVYQGEV
     VQILASNQQN MFLVFRAATD QCPAAEGWIP GFVLGHTSAV IMENPDGTLK KSTSWHTALR
     LRKKSEKKDK DGKRDGKLEN GYRKPREGLS NKVSVKLLNP NYIYDVPPEF VIPLSEVTCE
     TGETVVFRCR VCGRPKASIT WKGPEHNTLN NDDHYSISYS DIGEATLKII GVSTEDDGIY
     TCIAVNDMGS ASSSASLRVL GPGSDGIVVT WKDNFDAFYS EVAELGRGRF AVVKKCDQKG
     TKRAVATKFV NKKLMKRDQV THELGILQNL QHPLLVSLLD TFETPTSYVL VLEMADQGRL
     LDCVVRWGSL TEGKVRAHLG EVLEAVRYLH NCRIAHLDLK PENILVDQSL AKPTIKLADF
     GDAVQLNTTY YIHQLLGNPE FAAPEIILGN PVSLTADTWS VGVLTYVLLS GVSPFLDDSV
     EETCLNICRL DFSFPEDYFQ GVSQKAKEFV CFLLQEDPAK RPSAALALQE QWLQAGNGSG
     KGTGVLDTSR LTSFIERRKH QNDVRPIRSI KNFLQSRLLP RV
//
ID   SOBP_MOUSE              Reviewed;         864 AA.
AC   Q0P5V2;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   08-MAR-2011, entry version 36.
DE   RecName: Full=Sine oculis-binding protein homolog;
DE   AltName: Full=Jackson circler protein 1;
GN   Name=Sobp; Synonyms=Jxc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cochlea;
RA   Calderon A., Chen Z., Noben-Trauth K.;
RT   "Mutations in Jxc1 cause cochlea malformation and deafness in the
RT   Jackson circler (jc) mouse mutant.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Implicated in development of the cochlea.
CC   -!- SIMILARITY: Belongs to the SOBP family.
CC   -!- SIMILARITY: Contains 2 FCS-type zinc fingers.
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DR   EMBL; DQ157775; ABA39879.1; -; mRNA.
DR   EMBL; BC059851; AAH59851.1; -; mRNA.
DR   IPI; IPI00396773; -.
DR   RefSeq; NP_780616.4; NM_175407.3.
DR   UniGene; Mm.153750; -.
DR   STRING; Q0P5V2; -.
DR   PRIDE; Q0P5V2; -.
DR   Ensembl; ENSMUST00000040275; ENSMUSP00000040072; ENSMUSG00000038248.
DR   GeneID; 109205; -.
DR   KEGG; mmu:109205; -.
DR   UCSC; uc007ezf.1; mouse.
DR   CTD; 109205; -.
DR   MGI; MGI:1924427; Sobp.
DR   HOGENOM; HBG444030; -.
DR   HOVERGEN; HBG062766; -.
DR   InParanoid; Q0P5V2; -.
DR   OMA; EHGRSEV; -.
DR   OrthoDB; EOG4GF3DV; -.
DR   NextBio; 361763; -.
DR   ArrayExpress; Q0P5V2; -.
DR   Bgee; Q0P5V2; -.
DR   CleanEx; MM_SOBP; -.
DR   Genevestigator; Q0P5V2; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR   PROSITE; PS51024; ZF_FCS; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Metal-binding; Repeat; Zinc; Zinc-finger.
FT   CHAIN         1    864       Sine oculis-binding protein homolog.
FT                                /FTId=PRO_0000312233.
FT   ZN_FING     142    180       FCS-type 1.
FT   ZN_FING     216    256       FCS-type 2.
FT   COMPBIAS    346    552       Pro-rich.
FT   COMPBIAS    695    745       Pro-rich.
SQ   SEQUENCE   864 AA;  91784 MW;  DB06CB90A9F6FDB2 CRC64;
     MAEMEKEGRP PENKRSRKPA HPVKREINEE MKNFAENTMN ELLGWYGYDK VELKDGEDIE
     FRSYTTDGES RQHISVLKEN SLPKPKLPED SVISSYNIST GYSGLATGNG LSDSPAGSKD
     HGNVPIIVPL IPPPFIKPPA EDDVSNVQIM CAWCQKVGIK RYSLSMGSEV KSFCSEKCFA
     ACRRAYFKRN KARDEDGRAE TFPQQHYAKE TPRLAFKNNC ELLVCDWCKH IRHTKEYLDF
     GDGERRLQFC SAKCLNQYKM DIFYKETQAN LPAGLCSTLH PHMESKAEGT GVQLLTPDSW
     NIPLTDARRK APSPVTAAGQ SQGPGPSSST TVSPSDTANC SVTKIPTPVP KSLPISETPS
     IPPVSVQPPA SIGPPLGVPP RSPPMVMTNR GPVPLPIFME QQIIQQIRPP FIRGPPHHAS
     NPNSPLSNPM LPGIGAPPGG PRNLGPTSSP MHRPMLSPHI HPPSTPTMPG NPPGLLPPPP
     PGAPLPSLPF PPVSMMPNGP MPVPQMMNFG LPSLAPLVPP PTLLVPYPVI VPLPVPIPIP
     IPIPHVNDSK PPNGFSSNGE SFVPSAPGDS SAAGGKAGGR SLSPRDSKQG SSKSADSPPG
     SSGQALSLAP AERGRGEVVD LTRRAGSPAG AGGQPGFAGV LHGPQDGVID LTVGHRARLH
     NVIHRALHAH VKAEREPGAA ERRTCGGCRD GHCSPPAAGD PGPGAPAGPE AAAACNVIVN
     GTRSAPAEAK GAEPPPEQPP PPAPPKKLLS SEEPVVNELE SVKENNCASN CHLDGEATKK
     LMGEEALAGG DKSDPNLNNP ADEDHAYALR MLPKTGCVIQ PVPKPAEKAA MTPCVISSPM
     LSAGPEDLEP PLKRRCLRIR NQNK
//
ID   S45A4_MOUSE             Reviewed;         785 AA.
AC   Q0P5V9; Q3TCG5; Q3V0B8; Q69ZR4; Q6PDG3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   RecName: Full=Solute carrier family 45 member 4;
GN   Name=Slc45a4; Synonyms=Kiaa1126;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 74-785 (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 312-785 (ISOFORM 1/3).
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q0P5V9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q0P5V9-2; Sequence=VSP_033544;
CC       Name=3;
CC         IsoId=Q0P5V9-3; Sequence=VSP_033543;
CC   -!- SIMILARITY: Belongs to the glycoside-pentoside-hexuronide (GPH)
CC       cation symporter transporter (TC 2.A.2) family.
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DR   EMBL; AK133269; BAE21586.1; -; mRNA.
DR   EMBL; AK170738; BAE41991.1; -; mRNA.
DR   EMBL; BC056501; AAH56501.1; -; mRNA.
DR   EMBL; BC058722; AAH58722.1; -; mRNA.
DR   EMBL; AK173104; BAD32382.1; -; mRNA.
DR   IPI; IPI00116805; -.
DR   IPI; IPI00894978; -.
DR   IPI; IPI00895022; -.
DR   RefSeq; NP_001028391.2; NM_001033219.3.
DR   RefSeq; NP_001161727.1; NM_001168255.1.
DR   UniGene; Mm.212813; -.
DR   ProteinModelPortal; Q0P5V9; -.
DR   PRIDE; Q0P5V9; -.
DR   Ensembl; ENSMUST00000076224; ENSMUSP00000075577; ENSMUSG00000079020.
DR   GeneID; 106068; -.
DR   KEGG; mmu:106068; -.
DR   UCSC; uc007wch.1; mouse.
DR   CTD; 106068; -.
DR   MGI; MGI:2146236; Slc45a4.
DR   eggNOG; roNOG04575; -.
DR   GeneTree; ENSGT00390000018882; -.
DR   HOGENOM; HBG445264; -.
DR   HOVERGEN; HBG108452; -.
DR   InParanoid; Q0P5V9; -.
DR   OMA; RRRRHMF; -.
DR   OrthoDB; EOG41G344; -.
DR   NextBio; 358046; -.
DR   Bgee; Q0P5V9; -.
DR   Genevestigator; Q0P5V9; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR011701; MFS_1.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    785       Solute carrier family 45 member 4.
FT                                /FTId=PRO_0000333804.
FT   TRANSMEM     64     84       Helical; (Potential).
FT   TRANSMEM     87    107       Helical; (Potential).
FT   TRANSMEM    124    144       Helical; (Potential).
FT   TRANSMEM    156    176       Helical; (Potential).
FT   TRANSMEM    197    217       Helical; (Potential).
FT   TRANSMEM    234    254       Helical; (Potential).
FT   TRANSMEM    525    545       Helical; (Potential).
FT   TRANSMEM    577    597       Helical; (Potential).
FT   TRANSMEM    609    629       Helical; (Potential).
FT   TRANSMEM    631    651       Helical; (Potential).
FT   TRANSMEM    683    703       Helical; (Potential).
FT   TRANSMEM    709    729       Helical; (Potential).
FT   MOD_RES     472    472       Phosphoserine (By similarity).
FT   VAR_SEQ       1    194       Missing (in isoform 3).
FT                                /FTId=VSP_033543.
FT   VAR_SEQ     204    204       A -> AGKAPLQAP (in isoform 2).
FT                                /FTId=VSP_033544.
FT   CONFLICT    174    174       D -> Y (in Ref. 1; BAE21586).
FT   CONFLICT    365    365       S -> G (in Ref. 1; BAE41991).
SQ   SEQUENCE   785 AA;  85765 MW;  EF87F734B39F5411 CRC64;
     MKMAPQNADS ESMQVQELPV PLPDPQKPRD PEAETQEETT SEGSIDRIPT RLWVMHGAVM
     FGREFCYAME TALVTPILLQ IGLPEKYYSL TWFLSPVLGL IFTPLIGSAS DRCTLSWGRR
     RPFILALCVG VLIGVALFLN GSAIGLALGD VPSRQPIGIV LTVLGVVVLD FSADATEGPI
     RAYLLDVVDS EEQDMALNIH AFSAGLGGAI GYVLGGLDWT QTFLGDWFQT QNQVLFFFAA
     VIFSVSVALH LFSIEEEQYS PQQDRGPEDP TLPGTSVQPG APAPASRLSS LGGGMQDGSP
     PFPDEVQSEH ELSLDYLDVD IVRSKSDSVL HMADATLDME PQLLFLHDIE PSIFQDASYP
     STPQSTSQEL LRAKLPRLST FLRESTKEDD TLLDNHLNEA KVPNGRGSPP INSLSRSKVD
     LKPSVTSGSM RRRRHMFHRQ ASSTFSYYGK IGSHCYRYRR ANAVVLIKPS RSMSDLYDLQ
     QRQRSRHRNQ SGATASSGDT ESEEGETETT VRLLWLSMLK MPKELMWLCL CHLLTWFSVI
     AEAVFYTDFM GQVIFKGNPQ APSNSTKWHA YNAGVKMGCW GLVIYAATGA ICSALLQKYL
     DNYDLSIRII YMLGTLGFSV GTAVMAMFPN VYVAMVTIST MGVVSMSISY CPYALLGHYH
     DIKEYVHHSP GNSKRGFGID CAILSCQVYI SQILVASALG GVVDAVNSIV VIPIVASVGS
     FLGFLTATFL VIYPEVSEEP KEEQKGLSSG PAGEGEGGAG SEKPTVLKLS RKGGLRGLVE
     TESMV
//
ID   ZCH18_MOUSE             Reviewed;         948 AA.
AC   Q0P678; Q3TKW3; Q52KI3; Q6KAL8; Q9CU64;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   08-MAR-2011, entry version 36.
DE   RecName: Full=Zinc finger CCCH domain-containing protein 18;
DE   AltName: Full=Nuclear protein NHN1;
GN   Name=Zc3h18; Synonyms=Nhn1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 225-948 (ISOFORM 1).
RC   TISSUE=Spleen;
RX   PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of FLJ genes:
RT   the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:127-135(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-92 AND SER-530,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-75; SER-528;
RP   SER-530; SER-838 AND SER-888, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483; SER-530; SER-847
RP   AND SER-863, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q0P678-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q0P678-2; Sequence=VSP_029456, VSP_029457;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 C3H1-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD21439.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK017933; BAB31010.3; -; mRNA.
DR   EMBL; AK166802; BAE39030.1; -; mRNA.
DR   EMBL; BC030495; AAH30495.1; -; mRNA.
DR   EMBL; BC094330; AAH94330.1; -; mRNA.
DR   EMBL; AK131189; BAD21439.1; ALT_INIT; mRNA.
DR   IPI; IPI00454026; -.
DR   IPI; IPI00648513; -.
DR   RefSeq; NP_001025164.1; NM_001029993.1.
DR   RefSeq; NP_001025165.1; NM_001029994.1.
DR   UniGene; Mm.241489; -.
DR   ProteinModelPortal; Q0P678; -.
DR   PhosphoSite; Q0P678; -.
DR   PRIDE; Q0P678; -.
DR   Ensembl; ENSMUST00000093073; ENSMUSP00000090761; ENSMUSG00000017478.
DR   GeneID; 76014; -.
DR   KEGG; mmu:76014; -.
DR   UCSC; uc009nsm.1; mouse.
DR   CTD; 76014; -.
DR   MGI; MGI:1923264; Zc3h18.
DR   GeneTree; ENSGT00580000081375; -.
DR   HOVERGEN; HBG103346; -.
DR   OrthoDB; EOG46T31J; -.
DR   NextBio; 344435; -.
DR   ArrayExpress; Q0P678; -.
DR   Bgee; Q0P678; -.
DR   CleanEx; MM_ZC3H18; -.
DR   Genevestigator; Q0P678; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR000571; Znf_CCCH.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Metal-binding; Nucleus;
KW   Phosphoprotein; Zinc; Zinc-finger.
FT   CHAIN         1    948       Zinc finger CCCH domain-containing
FT                                protein 18.
FT                                /FTId=PRO_0000311243.
FT   ZN_FING     215    241       C3H1-type.
FT   COILED      395    460       Potential.
FT   COILED      916    945       Potential.
FT   COMPBIAS      5    205       Glu-rich.
FT   COMPBIAS    255    292       Pro-rich.
FT   COMPBIAS    528    742       Ser-rich.
FT   MOD_RES      45     45       Phosphoserine (By similarity).
FT   MOD_RES      64     64       Phosphoserine (By similarity).
FT   MOD_RES      71     71       Phosphoserine.
FT   MOD_RES      75     75       Phosphoserine.
FT   MOD_RES      80     80       Phosphoserine (By similarity).
FT   MOD_RES      92     92       Phosphoserine.
FT   MOD_RES     105    105       Phosphothreonine (By similarity).
FT   MOD_RES     106    106       Phosphoserine (By similarity).
FT   MOD_RES     483    483       Phosphoserine.
FT   MOD_RES     528    528       Phosphoserine.
FT   MOD_RES     530    530       Phosphoserine.
FT   MOD_RES     595    595       Phosphoserine (By similarity).
FT   MOD_RES     597    597       Phosphoserine (By similarity).
FT   MOD_RES     599    599       Phosphoserine (By similarity).
FT   MOD_RES     600    600       Phosphoserine (By similarity).
FT   MOD_RES     601    601       Phosphoserine (By similarity).
FT   MOD_RES     603    603       Phosphoserine (By similarity).
FT   MOD_RES     605    605       Phosphoserine (By similarity).
FT   MOD_RES     607    607       Phosphothreonine (By similarity).
FT   MOD_RES     609    609       Phosphoserine (By similarity).
FT   MOD_RES     673    673       Phosphothreonine (By similarity).
FT   MOD_RES     838    838       Phosphoserine.
FT   MOD_RES     847    847       Phosphoserine.
FT   MOD_RES     852    852       Phosphoserine (By similarity).
FT   MOD_RES     863    863       Phosphoserine.
FT   MOD_RES     888    888       Phosphoserine.
FT   VAR_SEQ     226    317       GNCTWGMSCRFIHPGVNDKGNYSLITKAEPFPPNGAPPLGP
FT                                HPLMPANPWGGPVVDEILPPPPPEPPTESAWERGLRHAKEV
FT                                LKKATIRKEQ -> DVVTPLSTLLPPIPNSIPLRGQVKGTK
FT                                YPVFTLCCALKSPAPEARLLSPGSRAQLGRQQGGGLRDRTA
FT                                VALFSLVSLELGRRCRLRPWHCT (in isoform 2).
FT                                /FTId=VSP_029456.
FT   VAR_SEQ     318    948       Missing (in isoform 2).
FT                                /FTId=VSP_029457.
SQ   SEQUENCE   948 AA;  105694 MW;  A56716FF866C847B CRC64;
     MDVAESPELD PHSPEDEEQP ALSDDDILRE SGSEQDLDGA GERASDLEEE ENATRVQSQE
     ETRSDEEDRA SEPKSQDQDS EAHELSRGPA GSPCEEGDDV EEDGTSDLRD EASSVTRELD
     EHELDYDEEV PEEPAPAAQE EEAEKAGAEE EEEKGEGAPG EEGKPDVQSV GEQEPTEAAK
     EKKKEDDDGE IDDGEIDDDD LEEGEVKDPS DRKVRPRPTC RFFMKGNCTW GMSCRFIHPG
     VNDKGNYSLI TKAEPFPPNG APPLGPHPLM PANPWGGPVV DEILPPPPPE PPTESAWERG
     LRHAKEVLKK ATIRKEQEPD FEEKRFTVTI GEDDREFDKE NEVFRDWNSR VPRDVRDTTL
     EPYADPYYDY EIERFWRGGQ YENFRVQYTE AEPYHNYRER ERERERENRQ RERERERERD
     RERERRQRER ERERERERDK ERQRRKEEWE RERAKRDEKD RQHRDRDRDK DREKDKEKPK
     PRSPQPPSRQ AEPPKKESTS VGPQVKRADE WKDPWRRSKS PKKKLGVSVS PSRARRRRKT
     SASSASASNS SRSSSRSSSY SGSGSSRSRS RSSSYSSYSS RSSRHSSFSG SRSRSRSFSS
     SPSPSPTPSP HRPPVRTKGE PAPPPGKAGE KSIKKPAPPP APPQATKTTA PGPEPAKPGD
     LREARRKERQ TRTPPRRRTL SGSGSGSGSS YSGSSSRSRS LSVSSVSSVS SATSSSSSVH
     SVDSDDMYAD LASPVSSASS RSPTPAQTKK ERGKSKKEDG VREEKRRRDP SAQPPKSSKA
     PAGGKASQQA AAPQPAVPGQ PQQGSFVAHK EIKLTLLNKA ADKGSRKRYE PSDKDRQSPP
     AKKANLSPDR GSRDRKSGGR MGSPKPERQR GQNAKAPAAP ADRKRPLSPQ SKGSSKVTSV
     PGKATDTATA GTKSGKASTL SRREELLKQL KAVEDAIARK RAKIPGKV
//
ID   Q0P6B2_MOUSE            Unreviewed;       640 AA.
AC   Q0P6B2;
DT   19-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   19-SEP-2006, sequence version 1.
DT   08-MAR-2011, entry version 28.
DE   SubName: Full=Far upstream element (FUSE) binding protein 1;
DE   SubName: Full=Far upstream element (FUSE) binding protein 1, isoform CRA_c;
GN   Name=Fubp1; ORFNames=mCG_115545;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor. C3;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 4 KH domains.
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DR   EMBL; BC023780; AAH23780.1; -; mRNA.
DR   EMBL; CH466532; EDL11934.1; -; Genomic_DNA.
DR   IPI; IPI00123292; -.
DR   UniGene; Mm.278922; -.
DR   ProteinModelPortal; Q0P6B2; -.
DR   SMR; Q0P6B2; 90-171, 181-443.
DR   STRING; Q0P6B2; -.
DR   Ensembl; ENSMUST00000106121; ENSMUSP00000101727; ENSMUSG00000028034.
DR   UCSC; uc008rsx.1; mouse.
DR   MGI; MGI:1196294; Fubp1.
DR   eggNOG; roNOG10468; -.
DR   HOVERGEN; HBG000625; -.
DR   OrthoDB; EOG4STS4G; -.
DR   ArrayExpress; Q0P6B2; -.
DR   Bgee; Q0P6B2; -.
DR   Genevestigator; Q0P6B2; -.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   InterPro; IPR015096; DUF1897.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR004088; KH_type_1.
DR   InterPro; IPR018111; KH_type_1_subgr.
DR   Pfam; PF09005; DUF1897; 2.
DR   Pfam; PF00013; KH_1; 4.
DR   SMART; SM00322; KH; 4.
DR   PROSITE; PS50084; KH_TYPE_1; 4.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   640 AA;  67196 MW;  E374D6DCF1ECE804 CRC64;
     MADYSTVPPP SSGSAGGGGG GVVNDAFKDA LQRARQIAAK IGGDAGTSLN SNDYGYGGQK
     RPLEDGDQPD AKKVPPQNDS FGAQLPPMHQ QQSRSVMTEE YKVPDGMVGF IIGRGGEQIS
     RIQQESGCKI QIAPDSGGLP ERSCMLTGTP ESVQSAKRLL DQIVEKGRPA PGFHHGDGPG
     NAVQEIMIPA SKAGLVIGKG GETIKQLQER AGVKMVMIQD GPQNTGADKP LRITGDPYKV
     QQAKEMVLEL IRDQGGFREV RNEYGSRIGG NEGIDVPIPR FAVGIVIGRN GEMIKKIQND
     AGVRIQFKPD DGTTPDRIAQ ITGPPDRCQH AAEIITDLLR SVQAGNPGGP GPGGRGRGRG
     QGNWNMGPPG GLQEFNFIVP TGKTGLIIGK GGETIKSISQ QSGARIELQR SPPPNADPNM
     KLFTIRGTPQ QIDYARQLIE EKIGGPVNPL GPPVPHGPHG VPGPHGPPGP PGPGTPMGPY
     NPAPYNPGPP GPAPHGPPAP YAPQGWGNAY PHWQQQAPPD PAKAGADPNS AAWAAYYAHY
     YQQQAQPPPA APAGAPATTQ TNGQGDQQAP APAGQVDYTK AWEEYYKKMG QAVPAPAGAP
     PGGQPDYSAA WAEYYRQQAA YYAQTSPQGM PQHPPAPQGQ
//
ID   DACT3_MOUSE             Reviewed;         610 AA.
AC   Q0PHV7;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   08-MAR-2011, entry version 28.
DE   RecName: Full=Dapper homolog 3;
GN   Name=Dact3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=C57BL/6; TISSUE=Forebrain;
RX   PubMed=16881060; DOI=10.1002/dvdy.20917;
RA   Fisher D.A., Kivimaee S., Hoshino J., Suriben R., Martin P.-M.,
RA   Baxter N., Cheyette B.N.R.;
RT   "Three Dact gene family members are expressed during embryonic
RT   development and in the adult brains of mice.";
RL   Dev. Dyn. 235:2620-2630(2006).
CC   -!- TISSUE SPECIFICITY: Expressed in brain and uterus.
CC   -!- DEVELOPMENTAL STAGE: Expression peaks at E10.5, then declines.
CC       Expressed in the ventral region of maturing somites, limb bud and
CC       branchial arch mesenchyme, and in the developing central nervous
CC       system.
CC   -!- DOMAIN: The C-terminal PDZ-binding motif may mediate interaction
CC       with the PDZ domains of DSH (Dishevelled) family proteins (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the dapper family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; DQ832319; ABH03019.1; -; mRNA.
DR   IPI; IPI00754924; -.
DR   RefSeq; NP_001075124.1; NM_001081655.1.
DR   UniGene; Mm.381664; -.
DR   PhosphoSite; Q0PHV7; -.
DR   PRIDE; Q0PHV7; -.
DR   Ensembl; ENSMUST00000108493; ENSMUSP00000104133; ENSMUSG00000078794.
DR   GeneID; 629378; -.
DR   KEGG; mmu:629378; -.
DR   UCSC; uc009fij.1; mouse.
DR   CTD; 629378; -.
DR   MGI; MGI:3654828; Dact3.
DR   GeneTree; ENSGT00530000063890; -.
DR   HOGENOM; HBG283341; -.
DR   HOVERGEN; HBG081403; -.
DR   InParanoid; Q0PHV7; -.
DR   OMA; ACSSAER; -.
DR   OrthoDB; EOG4H9XMQ; -.
DR   NextBio; 421052; -.
DR   ArrayExpress; Q0PHV7; -.
DR   Bgee; Q0PHV7; -.
DR   Genevestigator; Q0PHV7; -.
PE   2: Evidence at transcript level;
KW   Coiled coil.
FT   CHAIN         1    610       Dapper homolog 3.
FT                                /FTId=PRO_0000264617.
FT   COILED       63     87       Potential.
FT   MOTIF       607    610       PDZ-binding (By similarity).
FT   COMPBIAS    255    260       Poly-Arg.
FT   COMPBIAS    351    476       Arg-rich.
SQ   SEQUENCE   610 AA;  63287 MW;  810AA0143B009EB2 CRC64;
     MIRAFSFPVS PERGRLRGWL EGSLAGLCEL HWLRERQEYR VQQALRLAQP GMGGAEAEDE
     EDAEEDEDAA AARRAAAALE EQLEALPGLI WDLGQQLGDL SLESGGLDQE SGRSSGFYED
     PSSTGGPDSP PSTFCGDSGF SGSGSYGRLG PSDPRGIYAS ERPKSLGDAS PSAPESVGAR
     VAVPRSFSAP YPTAAAGAET CSSAERRARA GPFLTPSPLH AVALRSPRPS GRVPCGSPDG
     AASRPLDGYI SALLRRRRRR GAGQPRTSPG GADGGARRQN GARPRPPEAS PPPGGARPAR
     EPSTERAWAA AWEAEVPPEP APPAAASPPS SPAEGRLVKA QYIPGAPAAS RGLPGRAARR
     RAPPLTRGRS VEQSPPRERP RAAGRRGRLA EPSGRRGSPR ARKAARSQSE TSLLGRAHAA
     PPPKYPTAER DEPRPPRPRR GPAPTPTVQA CRRWRSTAEI DAPDGRRPRA RVPAPRGPAP
     SPSAPPRRLL YGCAGSDSEC SAVGRPVPLG RRMPSGCAPG GYGESESSAS EGESPAFSSA
     SSDSDGSGGL VWPQQLVAAA GASPSGPGGA AGGGTPAGPA KVFVKIKASH ALKKKILRFR
     SGSLKVMTTV
//
ID   GRD2I_MOUSE             Reviewed;        1203 AA.
AC   Q0QWG9; Q6DID0; Q9ESJ5;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=Delphilin;
DE   AltName: Full=Glutamate receptor, ionotropic, delta 2-interacting protein 1;
GN   Name=Grid2ip;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP   INTERACTION WITH GRID2.
RC   STRAIN=BALB/c;
RX   MEDLINE=21683819; PubMed=11826110;
RA   Miyagi Y., Yamashita T., Fukaya M., Sonoda T., Okuno T., Yamada K.,
RA   Watanabe M., Nagashima Y., Aoki I., Okuda K., Mishina M., Kawamoto S.;
RT   "Delphilin: a novel PDZ and formin homology domain-containing protein
RT   that synaptically colocalizes and interacts with glutamate receptor
RT   delta 2 subunit.";
RL   J. Neurosci. 22:803-814(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
RP   PALMITOYLATION AT CYS-3 (ISOFORM 2), AND INTERACTION WITH GRID2.
RC   TISSUE=Cerebellum;
RX   PubMed=16835239; DOI=10.1074/jbc.M602044200;
RA   Matsuda K., Matsuda S., Gladding C.M., Yuzaki M.;
RT   "Characterization of the delta2 glutamate receptor-binding protein
RT   delphilin: splicing variants with differential palmitoylation and an
RT   additional PDZ domain.";
RL   J. Biol. Chem. 281:25577-25587(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-184 (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP   [MRNA] OF 1-183 (ISOFORM 3), INTERACTION WITH GRID2, DEVELOPMENTAL
RP   STAGE, AND SUBCELLULAR LOCATION.
RX   PubMed=16168524; DOI=10.1016/j.molbrainres.2005.08.006;
RA   Yamashita T., Miyagi Y., Ono M., Ito H., Watanabe K., Sonoda T.,
RA   Tsuzuki K., Ozawa S., Aoki I., Okuda K., Mishina M., Kawamoto S.;
RT   "Identification and characterization of a novel Delphilin variant with
RT   an alternative N-terminus.";
RL   Brain Res. Mol. Brain Res. 141:83-94(2005).
RN   [5]
RP   INTERACTION WITH GRID2.
RX   PubMed=17027646; DOI=10.1016/j.bbrc.2006.09.109;
RA   Sonoda T., Mochizuki C., Yamashita T., Watanabe-Kaneko K., Miyagi Y.,
RA   Shigeri Y., Yazama F., Okuda K., Kawamoto S.;
RT   "Binding of glutamate receptor delta2 to its scaffold protein,
RT   Delphilin, is regulated by PKA.";
RL   Biochem. Biophys. Res. Commun. 350:748-752(2006).
RN   [6]
RP   INTERACTION WITH GRID2.
RX   PubMed=17425562; DOI=10.1111/j.1460-9568.2007.05412.x;
RA   Kohda K., Kakegawa W., Matsuda S., Nakagami R., Kakiya N., Yuzaki M.;
RT   "The extreme C-terminus of GluRdelta2 is essential for induction of
RT   long-term depression in cerebellar slices.";
RL   Eur. J. Neurosci. 25:1357-1362(2007).
RN   [7]
RP   INTERACTION WITH SLC16A7.
RX   PubMed=17496809; DOI=10.1097/WNR.0b013e3280586821;
RA   Watanabe-Kaneko K., Sonoda T., Miyagi Y., Yamashita T., Okuda K.,
RA   Kawamoto S.;
RT   "The synaptic scaffolding protein Delphilin interacts with
RT   monocarboxylate transporter 2.";
RL   NeuroReport 18:489-493(2007).
CC   -!- FUNCTION: Postsynaptic scaffolding protein at the Purkinje cell
CC       synapse, where it may serve to link GRID2 with actin cytoskeleton
CC       and various signaling molecules.
CC   -!- SUBUNIT: Interacts with C-terminus of the glutamate receptor GRID2
CC       via PDZ domain. Isoform 2 interacts also with Profilin-2/PFN2 and
CC       with the monocarboxylate transporter SLC16A7 via PDZ domain. The
CC       interaction of isoform 2 with GRID2 is dependent on GRID2
CC       phosphorylation by PKA.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cell junction, synapse,
CC       postsynaptic cell membrane. Cell projection, dendritic spine.
CC       Note=Localized to the postsynaptic junction site of the parallel
CC       fiber-Purkinje cell synapse. Highly present in the dendritic
CC       spines.
CC   -!- SUBCELLULAR LOCATION: Isoform 3: Cell junction, synapse. Cell
CC       projection, dendritic spine. Cell membrane; Lipid-anchor
CC       (Potential). Note=Localized at the dendritic spines, but also in
CC       dendritic shafts apart fron spines.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=L-delphilin;
CC         IsoId=Q0QWG9-1; Sequence=Displayed;
CC         Note=Not palmytoylated;
CC       Name=2; Synonyms=S-delphilin, delphilin alpha;
CC         IsoId=Q0QWG9-2; Sequence=VSP_033275, VSP_033278;
CC         Note=Contains a S-palmitoyl cysteine at Cys-3. When Cys-3 is
CC         mutated to Ala-3, isoform 2 is not palmytoylated anymore;
CC       Name=3; Synonyms=delphilin beta;
CC         IsoId=Q0QWG9-3; Sequence=VSP_033276, VSP_033277;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is expressed in the cerebellum, but
CC       not in the cerebral cortex. Isoform 2 is expressed in the cell
CC       body of purkinge cells of the cerebellum and weakly expressed in
CC       the cerebrum and the brainstem as well as various nuclei of the
CC       thalamus. Isoform 2 is highly expressed in the cerebral cortex
CC       than in the cerebellum. Isoform 3 is expressed in the cerebellum
CC       and cerebrum.
CC   -!- DEVELOPMENTAL STAGE: Isoform 3 expression is maintained troughout
CC       cerebellar development, while isoform 2 expression gradually
CC       decrease following the first postnatal week.
CC   -!- DOMAIN: PDZ 1 domain is responsible for cytoplasmic clustering of
CC       isoform 1.
CC   -!- PTM: Isoform 2 is palmytoylated. Palmytoylation of isoform 2 is
CC       necessary for the enhanced cell surface expression of GRID2, and
CC       is also responsible for the accumulation of isoform 2 within
CC       dendritic spines. Isoform 1 and isoform 2 are differentially
CC       localized, probably modulating GRID2 signaling in neurons.
CC   -!- MISCELLANEOUS: Isoform 1 shows a punctate distribution troughout
CC       the cytoplasm when expressed in COS cells, whereas isoform 2 is
CC       enriched at the edges of the plasma membranes. When expressed in
CC       cultured hippocampal neurons, isoform 1 forms clusters mainly in
CC       the dendritic shafts, whereas isoform 2 is preferentially
CC       expressed in spines.
CC   -!- SIMILARITY: Contains 1 FH2 (formin homology 2) domain.
CC   -!- SIMILARITY: Contains 2 PDZ (DHR) domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; DQ193535; ABB04525.1; -; mRNA.
DR   EMBL; AF099933; AAG31020.1; -; mRNA.
DR   EMBL; BC075624; AAH75624.1; -; mRNA.
DR   EMBL; AY377834; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AY377835; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00463677; -.
DR   IPI; IPI00674912; -.
DR   IPI; IPI00880454; -.
DR   RefSeq; NP_001152793.1; NM_001159321.1.
DR   RefSeq; NP_579933.1; NM_133355.1.
DR   UniGene; Mm.197460; -.
DR   ProteinModelPortal; Q0QWG9; -.
DR   SMR; Q0QWG9; 8-80, 263-345, 814-1190.
DR   STRING; Q0QWG9; -.
DR   PRIDE; Q0QWG9; -.
DR   Ensembl; ENSMUST00000010969; ENSMUSP00000010969; ENSMUSG00000010825.
DR   Ensembl; ENSMUST00000110733; ENSMUSP00000106361; ENSMUSG00000010825.
DR   GeneID; 170935; -.
DR   KEGG; mmu:170935; -.
DR   UCSC; uc009akd.1; mouse.
DR   CTD; 170935; -.
DR   MGI; MGI:2176213; Grid2ip.
DR   eggNOG; maNOG12472; -.
DR   GeneTree; ENSGT00560000076948; -.
DR   HOGENOM; HBG446110; -.
DR   HOVERGEN; HBG107964; -.
DR   InParanoid; Q0QWG9; -.
DR   OMA; HRARFDE; -.
DR   OrthoDB; EOG4WM4SZ; -.
DR   NextBio; 370517; -.
DR   ArrayExpress; Q0QWG9; -.
DR   Bgee; Q0QWG9; -.
DR   Genevestigator; Q0QWG9; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0043197; C:dendritic spine; IDA:MGI.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; TAS:MGI.
DR   GO; GO:0060292; P:long term synaptic depression; IMP:MGI.
DR   GO; GO:0007216; P:metabotropic glutamate receptor signaling pathway; TAS:MGI.
DR   InterPro; IPR003104; Actin-bd_FH2/DRF_autoreg.
DR   InterPro; IPR015425; FH2_actin-bd.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF02181; FH2; 1.
DR   Pfam; PF00595; PDZ; 2.
DR   SMART; SM00498; FH2; 1.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF101447; FH2_actin_bd; 1.
DR   SUPFAM; SSF50156; PDZ; 2.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS50106; PDZ; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW   Lipoprotein; Membrane; Palmitate; Postsynaptic cell membrane; Repeat;
KW   Synapse.
FT   CHAIN         1   1203       Delphilin.
FT                                /FTId=PRO_0000331625.
FT   DOMAIN        1     79       PDZ 1.
FT   DOMAIN      268    345       PDZ 2.
FT   DOMAIN      812   1203       FH2.
FT   COMPBIAS    742    804       Pro-rich.
FT   VAR_SEQ       1    179       Missing (in isoform 2).
FT                                /FTId=VSP_033275.
FT   VAR_SEQ       1    172       Missing (in isoform 3).
FT                                /FTId=VSP_033276.
FT   VAR_SEQ     173    183       SEAQGPVLDNL -> MGKDQGFSRHF (in isoform
FT                                3).
FT                                /FTId=VSP_033277.
FT   VAR_SEQ     180    184       LDNLR -> MSCLG (in isoform 2).
FT                                /FTId=VSP_033278.
SQ   SEQUENCE   1203 AA;  132021 MW;  79AFAA7E869731C1 CRC64;
     MPATNQGWPE DFGFQLGGSG PCFVIEVAEG SSAHAGGLRP GDQILEVEGL AVGGLSRERI
     VRLARRCPRV PPSLGVLPGP EGGPTALTAA WLTRRFGRSL PLSRELLRLA GGPRPDAVHR
     ERRRKAQEFS CQVDDILGDR LTAKEQVFTA LKQFAAEQRV DELVWTLTLV LPSEAQGPVL
     DNLRIFIPKK HRARFDEVVS QGLLGKLCRA RRAQGAQRLR RSRSEERPER LLVSTRASAA
     PRRPDEPPPR KATSLLGGRT GPGGPRRTVR VYKGNKSFGF TLRGHGPVWI ESVLPGSPAE
     NASLKSGDRI LFLNGLDMRN CSHDKVVSML QGSGAMPTLV VEEGPVPFAS DSDSLDSPTR
     ASALTSLQWV ADILPSSIRV QGRTFSQQLD HLLTPPERYG VCRALERFFQ HRNIDTLIVD
     VYPVLDTPAK QVLWQFLYQL LTYEEQELCQ EKIACFLGYT AMTEPESSLD LEPESTPEPT
     PEPQPRSSLR ASSMCRRSLR SQGLETSLSC GPGDCPEMPL PLIPGERQAG DGTSLPETPN
     PKMMSAVYAE LESRLNSSFK GKIGTMSKSR ASPPVPSLVG TSGPRTLSGV SWPSDRLLPS
     PCYDPLCSGG LASPSSSESH PYASLDSSRA PSPQPGLGSI HADSPPSPDP IRPPSRRKLF
     AFSRPVRSRD TDRFLDALSE QLGPRLSIVD DFLTPENDYE EMSFHDDQGS FVTNERSSAS
     ECVSSSEEGS SLTYSSISDH IPPPPLSPPP PPPLPFHDPK PSSRTSDGPR GPPQSLTKPL
     TQINHPVPPP PPPPLPPPVP CAPPMLSRGV GHRRSETSHM SVKRLRWEQV ENSEGTIWGQ
     LGEDSDYDKL SDMVKYLDLE LHFGTQKPPK PVPGPEPFRK KEVVEILSHK KAYNTSILLA
     HLKLTPGELR QVLMSMEPRR LEPAHLAQLL LFAPDADEEQ RYQAFREAPG RLSEPDQFVL
     QMLSVPEYKT RLRSLHFQAT LQEKTEEIRG SLECLRQASL ELKNSRKLAK ILEFVLAMGN
     YLNDGQPKTN KTTGFKINFL TELNSTKTVD GKSTFLHILA KSLSQHFPEL LGFAQDLPTV
     PLAAKVNQRA LTGDLADLHD TVSEIQVACQ SMAPSSEDRF AVVMASFLET AQPALRALDG
     LQREAMEELG KALAFFGEDS KATTSEAFFG IFSEFMSKFE RALSDLQAGD GPRSSGMVSP
     LAW
//
ID   EXPH5_MOUSE             Reviewed;        1960 AA.
AC   Q0VAV2; Q3UNV5; Q6A034; Q812E3;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   08-MAR-2011, entry version 40.
DE   RecName: Full=Exophilin-5;
DE   AltName: Full=Synaptotagmin-like protein homolog lacking C2 domains b;
DE            Short=SlaC2-b;
DE            Short=Slp homolog lacking C2 domains b;
GN   Name=Exph5; Synonyms=Kiaa0624, Slac2b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Spleen;
RX   MEDLINE=22590467; PubMed=12590134; DOI=10.1074/jbc.M213090200;
RA   Fukuda M.;
RT   "Slp4-a/granuphilin-a inhibits dense-core vesicle exocytosis through
RT   interaction with the GDP-bound form of Rab27A in PC12 cells.";
RL   J. Biol. Chem. 278:15390-15396(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 338-1960.
RC   TISSUE=Pancreatic islet;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 749-1553.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   INTERACTION WITH RAB27A.
RX   MEDLINE=21883924; PubMed=11773082; DOI=10.1074/jbc.M112414200;
RA   Kuroda T.S., Fukuda M., Ariga H., Mikoshiba K.;
RT   "The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2
RT   functions as a novel Rab27A binding domain.";
RL   J. Biol. Chem. 277:9212-9218(2002).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May act as Rab effector protein and play a role in
CC       vesicle trafficking (By similarity).
CC   -!- SUBUNIT: Interacts with RAB27A.
CC   -!- INTERACTION:
CC       Q9ERI2:Rab27a; NbExp=1; IntAct=EBI-398327, EBI-398172;
CC   -!- SIMILARITY: Contains 1 RabBD (Rab-binding) domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AB098163; BAC57424.1; -; mRNA.
DR   EMBL; BC120905; AAI20906.1; -; mRNA.
DR   EMBL; AK172984; BAD32262.1; -; mRNA.
DR   EMBL; AK143980; BAE25642.1; -; mRNA.
DR   IPI; IPI00230008; -.
DR   RefSeq; NP_789816.2; NM_176846.3.
DR   UniGene; Mm.277540; -.
DR   ProteinModelPortal; Q0VAV2; -.
DR   SMR; Q0VAV2; 15-62.
DR   IntAct; Q0VAV2; 1.
DR   PhosphoSite; Q0VAV2; -.
DR   PRIDE; Q0VAV2; -.
DR   Ensembl; ENSMUST00000051014; ENSMUSP00000062632; ENSMUSG00000034584.
DR   GeneID; 320051; -.
DR   KEGG; mmu:320051; -.
DR   NMPDR; fig|10090.3.peg.20199; -.
DR   CTD; 320051; -.
DR   MGI; MGI:2443248; Exph5.
DR   eggNOG; roNOG08270; -.
DR   GeneTree; ENSGT00390000011087; -.
DR   HOGENOM; HBG127208; -.
DR   HOVERGEN; HBG067353; -.
DR   InParanoid; Q0VAV2; -.
DR   OMA; RDFEMIS; -.
DR   OrthoDB; EOG47PX51; -.
DR   PhylomeDB; Q0VAV2; -.
DR   Bgee; Q0VAV2; -.
DR   Genevestigator; Q0VAV2; -.
DR   GO; GO:0017137; F:Rab GTPase binding; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   InterPro; IPR010911; Rab-bd_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   PROSITE; PS50916; RABBD; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1   1960       Exophilin-5.
FT                                /FTId=PRO_0000355582.
FT   DOMAIN        7     63       RabBD.
FT   MOD_RES     336    336       Phosphoserine.
FT   MOD_RES    1693   1693       Phosphoserine (By similarity).
FT   CONFLICT   1717   1717       A -> V (in Ref. 3; BAD32262).
FT   CONFLICT   1936   1936       V -> D (in Ref. 1; BAC57424).
SQ   SEQUENCE   1960 AA;  217643 MW;  9D9864CA1396CB22 CRC64;
     MTKVPQGFDF SFLNEEEARK ILQVLERNEE LRRAEKDRIS KLQKTKRDIR WLQGATGEWF
     EEIQRKKFCN ETDVNQMLKP PLTYRLQKGM AKNDPMELQT PRSKSLINQK PSVSSRMSFR
     SSFASLFSFR RPAKETLKLQ SPRPNRCDER VRPSASVRGT ASAKIYNSPV GNQPVASVFV
     PKPAIMREES GMPPPWDASL LESEFFQVLD DLDNKLAQEQ SSGLMNTRVP FNYGSRTQFK
     LSHRNSHGHS TGRQQNYHSE TSNMSIYNIL RPGTPREGFK TFSPRTKTIY DMYRTREPRV
     LKEDFMQKNA FGSASLCFDS RQRSASPATG SFTARSLHFP ADTQNKSSFT PVRHQQSPKR
     TPLSSIIWNR SDASRHRQNQ EESLGVQAPM DIDPEEQYVS PRCFQESRRY EMCHSQNAYQ
     SYPLNVPVAN AMSPDTLENS ENMPFYRQSN PFARSFFSST FRQSREQRFG QNSFWSRQEE
     YSSWSDFPQS RGPFPSSDKD FEMFSVEANR APSVCSQGVP SQHWRSHSSG HGTYVFRGRE
     DSHCWRSDFQ TSPLESMDTS HVNENQHPPH FVTPVGFSIT DSSCHLQSSR LDSQQGYFPV
     EEAVDEDPYL CGKAQTPASS FRTPFPLSPD DGRESQSSSF PDSTATLQKI IPNKPDFLPI
     RNCTEVPVAC SHSTDSLSLT DTQPNIPVTE TNSEKDMDVS VSKDEQLNKT GQKSRPTGLP
     QYVLHTVISN DLPDFQNAHS RDSAQNDRYG FNAPATERSR RSPRVFSRKG TSQIHTTQRD
     QSNKLSKNKC FGGDRTLDSA ASPPFIQESG TATSLPSPNQ GCHQKTGSNE ESSNTIKNSH
     WCFESTANQK SQPSREPALL DLEQSLSTHS TNDSKLAPGH SISRAPLHVA SDAPQESFLD
     ARLVPSTTVF SRSLSDQDPG QEQREEKDKA TKSQDNQLAV NSTDNQESHD SPALPHDAVH
     CHPYSPFKNG RGKGRVRRRV SCIEKLTKTE RAAAPTREGS GCAEDQRSIK DPELSTVYCT
     LPRKPASFLI HSRQQESKGT VASVRNGPLP FQIKNKAEVP TGKSTSDKPS SPESVSDAAN
     AVSGTPKATK KMTDMKAIRS ASVRKGPLPF LIKRAISCPS GEPCSLAESD DRQKSSVLGM
     DASPVIPRPG GRIFNSLEGE PSFRESAFSE KELAQEHTGK DRELRAPRMG LFNPSKKTPE
     RLCATGSGKE SGRALHKFKT TSMFSVSGDE ENVNCLEVVS IYYTLPRKPS KKFCSLLQQY
     TQGTDSLRDA FQGETEALPN ALEIDELNCP AQVQSGIPPP QDPKMQVDSA PCCLSHSPES
     KDVSQLPDRE TSKSTLEEMT SVGPDVSLHR EEPTTKEISP SNVSKTAIDD SLSREKREKE
     LLRQILRAPL LHQEKGAGKE HTKSHQQPSK GGNSGPSGLP SRSEDNDENS QTRRDSGTCA
     GGMASGNGQY PWRDHMAAVV GDRSSRSQPR ETSGTTGSDC QNPTDKMLSD SESQAFALTP
     ALCKLQLAEE AQPGGAGLQS EASQAGSQET NTAEMRKVED EEHMLTRDQT LLPRGNNKNK
     TNTDETKDRY SGKHRLAAIS KASKRIPAKD LSPRKHVATI FSQSESESGF RRLSLYRPED
     NPLSPEPTVK ATESTDESSQ MNVDKSETLL QETTVSSPGP PGQPCHQKSA SILQPHLNGS
     PGVLETPPKS EGSKTQISGE LGAPAQLTLT SPLEKGAGHQ QRLSPPFPLE PTQKSTINSH
     CQLRHRSAPS PESEPEPHLY RSKSLKNFNV QSDLLCASHP PKARGRHFSE NTSIDNALSQ
     LSLEDGSFPN SGYNRRFKSS SELPASYESE SWTSYSNRTR GPKSTSSISR PIDYGIFGKE
     QQLAFLENVK RSLTQGRLWK PSFLKNPGFL KDDVLNASNL SQSELVNSPA GQAPEDGVFP
     SEPLNIYKDD PVEPLVSDWD TDTTTDDEYY LDEKDKESEL
//
ID   Q0VB45_MOUSE            Unreviewed;       425 AA.
AC   Q0VB45;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   SubName: Full=Potassium inwardly-rectifying channel, subfamily J, member 6;
GN   Name=Kcnj6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
CC       family.
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DR   EMBL; BC120794; AAI20795.1; -; mRNA.
DR   EMBL; BC125565; AAI25566.1; -; mRNA.
DR   IPI; IPI00227085; -.
DR   RefSeq; NP_034736.2; NM_010606.2.
DR   UniGene; Mm.328720; -.
DR   ProteinModelPortal; Q0VB45; -.
DR   SMR; Q0VB45; 56-380.
DR   STRING; Q0VB45; -.
DR   PRIDE; Q0VB45; -.
DR   Ensembl; ENSMUST00000099508; ENSMUSP00000097108; ENSMUSG00000043301.
DR   GeneID; 16522; -.
DR   KEGG; mmu:16522; -.
DR   UCSC; uc008abl.1; mouse.
DR   CTD; 16522; -.
DR   MGI; MGI:104781; Kcnj6.
DR   HOVERGEN; HBG006178; -.
DR   NextBio; 289901; -.
DR   ArrayExpress; Q0VB45; -.
DR   Bgee; Q0VB45; -.
DR   Genevestigator; Q0VB45; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015467; F:G-protein activated inward rectifier potassium channel activity; IDA:MGI.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR016449; K_chnl_inward-rec_Kir.
DR   InterPro; IPR001838; K_chnl_inward-rec_Kir-like.
DR   InterPro; IPR003275; K_chnl_inward-rec_Kir3.2.
DR   InterPro; IPR013521; K_chnl_inward-rec_Kir_Cr2.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   Gene3D; G3DSA:2.60.40.1400; IR_K+channel_cytopl; 1.
DR   PANTHER; PTHR11767; K+channel_IR; 1.
DR   PANTHER; PTHR11767:SF19; KIR32_channel; 1.
DR   Pfam; PF01007; IRK; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01328; KIR32CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; Ig_E-set; 1.
PE   2: Evidence at transcript level;
KW   Ion transport; Ionic channel; Membrane; Potassium;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
SQ   SEQUENCE   425 AA;  48680 MW;  A5C794AA063F0B78 CRC64;
     MTMAKLTESM TNVLEGDSMD QDVESPVAIH QPKLPKQARD DLPRHISRDR TKRKIQRYVR
     KDGKCNVHHG NVRETYRYLT DIFTTLVDLK WRFNLLIFVM VYTVTWLFFG MIWWLIAYIR
     GDMDHIEDPS WTPCVTNLNG FVSAFLFSIE TETTIGYGYR VITDKCPEGI ILLLIQSVLG
     SIVNAFMVGC MFVKISQPKK RAETLVFSTH AVISMRDGKL CLMFRVGDLR NSHIVEASIR
     AKLIKSKQTS EGEFIPLNQT DINVGYYTGD DRLFLVSPLI ISHEINQQSP FWEISKAQLP
     KEELEIVVIL EGMVEATGMT CQARSSYITS EILWGYRFTP VLTLEDGFYE VDYNSFHETY
     ETSTPSLSAK ELAELANRAE LPLSWSVSSK LNQHAELETE EEEKNPEELT ERNGDVANLE
     NESKV
//
ID   CL059_MOUSE             Reviewed;         186 AA.
AC   Q0VBF2;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   08-MAR-2011, entry version 37.
DE   RecName: Full=Uncharacterized protein C12orf59 homolog;
DE   Flags: Precursor;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
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DR   EMBL; BC120661; AAI20662.2; -; mRNA.
DR   EMBL; BC120663; AAI20664.2; -; mRNA.
DR   IPI; IPI00356687; -.
DR   RefSeq; NP_001074655.1; NM_001081186.1.
DR   UniGene; Mm.44237; -.
DR   PRIDE; Q0VBF2; -.
DR   Ensembl; ENSMUST00000032263; ENSMUSP00000032263; ENSMUSG00000030160.
DR   GeneID; 330428; -.
DR   KEGG; mmu:330428; -.
DR   UCSC; uc009efx.1; mouse.
DR   MGI; MGI:2442838; D630042F21Rik.
DR   eggNOG; roNOG15652; -.
DR   GeneTree; ENSGT00530000063999; -.
DR   HOGENOM; HBG283214; -.
DR   HOVERGEN; HBG099707; -.
DR   InParanoid; Q0VBF2; -.
DR   OMA; CCCLSRQ; -.
DR   OrthoDB; EOG479F88; -.
DR   NextBio; 399368; -.
DR   ArrayExpress; Q0VBF2; -.
DR   Bgee; Q0VBF2; -.
DR   CleanEx; MM_D630042F21RIK; -.
DR   Genevestigator; Q0VBF2; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Membrane; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     28       Potential.
FT   CHAIN        29    186       Uncharacterized protein C12orf59 homolog.
FT                                /FTId=PRO_0000294449.
FT   TRANSMEM     44     64       Helical; (Potential).
SQ   SEQUENCE   186 AA;  20312 MW;  2EA4E0D30C640641 CRC64;
     MFSLMTAWAQ VLMASGLFYF IQLPGARSEE NCVNTEHCLT TDWVHLWYIW LLVVVGALLL
     LCGLTSVCFR CCLSRPENGE DGAPPPYEVT VIAFDHDSTL QSTITSLQSV FGPAARRILA
     VAHAHSSLGQ LPSSVDTLPG YEEALRMSRF TVARCGQKVP DLPSVPEEKQ LPPTGKESPG
     TEPPSH
//
ID   CA095_MOUSE             Reviewed;         141 AA.
AC   Q0VBF8;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   08-MAR-2011, entry version 23.
DE   RecName: Full=Uncharacterized membrane protein C1orf95 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the SPEC3 family.
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DR   EMBL; BC120654; AAI20655.1; -; mRNA.
DR   EMBL; BC120656; AAI20657.1; -; mRNA.
DR   IPI; IPI00462375; -.
DR   RefSeq; NP_001074696.1; NM_001081227.1.
DR   UniGene; Mm.44791; -.
DR   PRIDE; Q0VBF8; -.
DR   Ensembl; ENSMUST00000136521; ENSMUSP00000119782; ENSMUSG00000053963.
DR   GeneID; 381310; -.
DR   KEGG; mmu:381310; -.
DR   UCSC; uc007dwh.1; mouse.
DR   MGI; MGI:2138735; 6330403A02Rik.
DR   GeneTree; ENSGT00390000008003; -.
DR   HOVERGEN; HBG080954; -.
DR   OrthoDB; EOG4QVCDD; -.
DR   NextBio; 401870; -.
DR   Bgee; Q0VBF8; -.
DR   CleanEx; MM_6330403A02RIK; -.
DR   Genevestigator; Q0VBF8; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    141       Uncharacterized membrane protein C1orf95
FT                                homolog.
FT                                /FTId=PRO_0000278636.
FT   TRANSMEM     51     71       Helical; (Potential).
FT   TRANSMEM     87    107       Helical; (Potential).
FT   COMPBIAS     11     20       Poly-Ala.
FT   COMPBIAS     26     29       Poly-Ser.
SQ   SEQUENCE   141 AA;  15005 MW;  204CC262DB0598E7 CRC64;
     MEPLHKDAET AAAAAAVAAA DPRGASSSSG VVVQVREKKG PLRAAIPYMP FPVAVICLFL
     NTFVPGLGTF VSAFTVLCGA RTDLPDRHVC CVFWLNIAAA LIQVLTAIVM VGWIMSIFWG
     MDMVILAISQ GYKDQGIPQQ L
//
ID   Q0VBL3_MOUSE            Unreviewed;       962 AA.
AC   Q0VBL3;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   SubName: Full=RNA binding motif protein 15;
GN   Name=Rbm15;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
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DR   EMBL; BC120590; AAI20591.1; -; mRNA.
DR   EMBL; BC137741; AAI37742.1; -; mRNA.
DR   IPI; IPI00340815; -.
DR   RefSeq; NP_001039272.1; NM_001045807.1.
DR   UniGene; Mm.27966; -.
DR   UniGene; Mm.472803; -.
DR   ProteinModelPortal; Q0VBL3; -.
DR   SMR; Q0VBL3; 444-528, 783-956.
DR   STRING; Q0VBL3; -.
DR   PRIDE; Q0VBL3; -.
DR   Ensembl; ENSMUST00000061772; ENSMUSP00000054424; ENSMUSG00000048109.
DR   GeneID; 229700; -.
DR   KEGG; mmu:229700; -.
DR   CTD; 229700; -.
DR   MGI; MGI:2443205; Rbm15.
DR   HOGENOM; HBG717522; -.
DR   HOVERGEN; HBG058366; -.
DR   InParanoid; Q0VBL3; -.
DR   OMA; MIIVRVF; -.
DR   PhylomeDB; Q0VBL3; -.
DR   NextBio; 379619; -.
DR   ArrayExpress; Q0VBL3; -.
DR   Bgee; Q0VBL3; -.
DR   Genevestigator; Q0VBL3; -.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0010553; P:negative regulation of gene-specific transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IDA:MGI.
DR   GO; GO:0001569; P:patterning of blood vessels; IMP:MGI.
DR   GO; GO:0060674; P:placenta blood vessel development; IMP:MGI.
DR   GO; GO:0007221; P:positive regulation of transcription of Notch receptor target; IDA:MGI.
DR   GO; GO:0048536; P:spleen development; IMP:MGI.
DR   GO; GO:0060412; P:ventricular septum morphogenesis; IMP:MGI.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR016194; SPOC-like.
DR   InterPro; IPR012921; SPOC_C.
DR   InterPro; IPR010912; SPOC_met.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 3.
DR   Gene3D; G3DSA:2.40.290.10; G3DSA:2.40.290.10; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF07744; SPOC; 1.
DR   SMART; SM00360; RRM; 3.
DR   SUPFAM; SSF100939; SPOC-like; 1.
DR   PROSITE; PS50102; RRM; 3.
DR   PROSITE; PS50917; SPOC; 1.
PE   1: Evidence at protein level;
SQ   SEQUENCE   962 AA;  105722 MW;  D740EDBF23279C5D CRC64;
     MRSAGREPLP RRSPRWRRAS PLCETSAGWR VSQLRRDDLR RPSTMKGKER SPVKPKRSRG
     GEDSSSRGER SKKLGGSGGS NGSSSGKTDS GGSRRSLHLD KSSSRGGSRE YETGGGSSSS
     RLHSYSSPST KNSSGGGESR SSSRGGGGES RSSGAASSAP GGGDGVEYKT LKISELGSQL
     SDEAVEDGLF HEFKRFGDVS VKISHLSGSG SGDERVAFVN FRRPEDARAA KHARGRLVLY
     DRPLKIEAVY VSRRRSRSPL DKDAYAPSSS VVGTSVGSHR HAPGGGGGQR SLSPGGAALG
     YRDYRLQQLA LGRLPPPPPP PLPRELERER DYPFYDRVRP AYSLEPRVGA GAGAAPFREV
     DEISPEDDQR ANRTLFLGNL DITVTENDLR RAFDRFGVIT EVDIKRPSRG QTSTYGFLKF
     ENLDMSHRAK LAMSGKIIIR NPIKIGYGKA TPTTRLWVGG LGPWVPLAAL AREFDRFGTI
     RTIDYRKGDS WAYIQYESLD AAHAAWTHMR GFPLGGPDRR LRVDFADTEH RYQQQYLQPL
     PLTHYELVTD TFGHRAPDPL RSARDRTPPL LYRDRDRDLY TDSDWVPPPP PVRERSARAA
     TSAVTAYEPL DSLDRRRDGW SLDRDRGDRD LPSSRDQPRK RRLPEESGGR HLDRSPESER
     PRKQRHCTPS PDRSPELSSN RDRYNSDNDR SSRLLLLERS SPVRDRRGSL EKSQSDKRDR
     KNSASAERDR KHRTAAPTEG KNPLKKEDRS DGNAPSASTS SSKQKPPSQK QDGGTAPVAA
     SSPKLCLAWQ GMLLLKNSNF PSNMHLLQGD LQVASSLLVE GSTGGKVAQL KITQRLRLDQ
     PKLDEVTRRI KVAGPNGYAI LLAVPGSSDS RSSSSSATSD TAASTQRPLR NLVSYLKQKQ
     AAGVISLPVG GNKDKENTGV LHAFPPCEFS QQFLDSPAKA LAKSEEDYLV MIIVRAKLVN
     SG
//
ID   K1644_MOUSE             Reviewed;         198 AA.
AC   Q0VBP7; Q6P5D2; Q6ZPK6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   RecName: Full=Uncharacterized protein KIAA1644;
DE   Flags: Precursor;
GN   Name=Kiaa1644;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98225.2; Type=Erroneous initiation;
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DR   EMBL; AK129415; BAC98225.2; ALT_INIT; Transcribed_RNA.
DR   EMBL; BC062953; AAH62953.2; -; mRNA.
DR   EMBL; BC119234; AAI19235.1; -; mRNA.
DR   EMBL; BC120551; AAI20552.1; -; mRNA.
DR   IPI; IPI00460680; -.
DR   RefSeq; NP_001156617.1; NM_001163145.1.
DR   UniGene; Mm.275387; -.
DR   Ensembl; ENSMUST00000080751; ENSMUSP00000079575; ENSMUSG00000062760.
DR   Ensembl; ENSMUST00000089026; ENSMUSP00000086420; ENSMUSG00000062760.
DR   GeneID; 72301; -.
DR   KEGG; mmu:72301; -.
DR   UCSC; uc007xca.1; mouse.
DR   MGI; MGI:1919551; 1810041L15Rik.
DR   eggNOG; maNOG17802; -.
DR   GeneTree; ENSGT00390000006791; -.
DR   HOGENOM; HBG713517; -.
DR   HOVERGEN; HBG108041; -.
DR   InParanoid; Q0VBP7; -.
DR   OrthoDB; EOG4M65JW; -.
DR   NextBio; 335946; -.
DR   ArrayExpress; Q0VBP7; -.
DR   Bgee; Q0VBP7; -.
DR   CleanEx; MM_1810041L15RIK; -.
DR   Genevestigator; Q0VBP7; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25    198       Uncharacterized protein KIAA1644.
FT                                /FTId=PRO_0000318952.
FT   TOPO_DOM     25     96       Extracellular (Potential).
FT   TRANSMEM     97    117       Helical; (Potential).
FT   TOPO_DOM    118    198       Cytoplasmic (Potential).
FT   CARBOHYD     52     52       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     94     94       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   198 AA;  22482 MW;  31F270096A928A54 CRC64;
     MTSCGQRSRN VLAVFSLLFP AVLSAHFRVC EPYTDHKGRY HFGFHCPRLS DNKTFVLCCH
     HNNTVFKYCC NETEFQAVMQ ANLTAGPEGY MHNNYTALLG VWIYGFFVLT LLVLDLLYYS
     AMNYDICKVY LTRWGIQGRW MKQDPRRWGN PARAPRPGQP APQPQPPPGT LPQAPQAVHT
     LRGDTHSPPL MTFQSSSA
//
ID   PPC1A_MOUSE             Reviewed;         271 AA.
AC   Q0VBU9;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   08-MAR-2011, entry version 39.
DE   RecName: Full=Phosphatidate phosphatase PPAPDC1A;
DE            EC=3.1.3.4;
DE   AltName: Full=Phosphatidic acid phosphatase type 2 domain-containing protein 1A;
GN   Name=Ppapdc1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Displays magnesium-independent phosphatidate phosphatase
CC       activity in vitro. Catalyzes the conversion of phosphatidic acid
CC       to diacylglycerol (By similarity).
CC   -!- CATALYTIC ACTIVITY: A 1,2-diacylglycerol 3-phosphate + H(2)O = a
CC       1,2-diacyl-sn-glycerol + phosphate.
CC   -!- ENZYME REGULATION: Inhibited by N-ethylmaleimide (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family.
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DR   EMBL; BC120497; AAI20498.1; -; mRNA.
DR   IPI; IPI00379132; -.
DR   RefSeq; NP_001074432.1; NM_001080963.1.
DR   UniGene; Mm.39184; -.
DR   ProteinModelPortal; Q0VBU9; -.
DR   PRIDE; Q0VBU9; -.
DR   Ensembl; ENSMUST00000094018; ENSMUSP00000091557; ENSMUSG00000070366.
DR   GeneID; 381925; -.
DR   KEGG; mmu:381925; -.
DR   UCSC; uc009jzl.1; mouse.
DR   CTD; 381925; -.
DR   MGI; MGI:2685936; Ppapdc1a.
DR   eggNOG; roNOG04356; -.
DR   GeneTree; ENSGT00510000046723; -.
DR   HOGENOM; HBG507117; -.
DR   HOVERGEN; HBG056764; -.
DR   InParanoid; Q0VBU9; -.
DR   OMA; FSFTEFL; -.
DR   OrthoDB; EOG4NGGNN; -.
DR   PhylomeDB; Q0VBU9; -.
DR   NextBio; 402755; -.
DR   ArrayExpress; Q0VBU9; -.
DR   Bgee; Q0VBU9; -.
DR   Genevestigator; Q0VBU9; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008195; F:phosphatidate phosphatase activity; IEA:EC.
DR   InterPro; IPR016118; P_Acid_Pase/Cl_peroxidase_N.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   Gene3D; G3DSA:1.20.144.10; P_Acid_Pase/Cl_peroxidase_N; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; AcPase_VanPerase; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    271       Phosphatidate phosphatase PPAPDC1A.
FT                                /FTId=PRO_0000286944.
FT   TRANSMEM      4     24       Helical; (Potential).
FT   TRANSMEM     49     69       Helical; (Potential).
FT   TRANSMEM     84    104       Helical; (Potential).
FT   TRANSMEM    142    162       Helical; (Potential).
FT   TRANSMEM    179    199       Helical; (Potential).
FT   TRANSMEM    202    222       Helical; (Potential).
FT   REGION      102    110       Phosphatase sequence motif I (By
FT                                similarity).
FT   REGION      143    146       Phosphatase sequence motif II (By
FT                                similarity).
FT   REGION      195    205       Phosphatase sequence motif III (By
FT                                similarity).
SQ   SEQUENCE   271 AA;  30444 MW;  944F8A1561DDA97B CRC64;
     MRELAIEIGV RALLFGVFVF TEFLDPFQRV IQPEEIWLYK NPLVQSDNIP TRLMFAISFL
     TPLAVICVVK IIRRTDKTEI KEAFLAVSLA LALNGVCTNT IKLIVGRPRP DFFYRCFPDG
     VMNSEMRCTG DPDLVSEGRK SFPSIHSSFA FSGLGFTTFY LAGKLHCFTE SGRGKSWRLC
     AAILPLYCAM MIALSRMCDY KHHWQDSFVG GVIGLIFAYI CYRQHYPPLA NTACHKPYVS
     LRVPTSLKKE ERPTADSAPS LPLEGITEGP V
//
ID   ZN800_MOUSE             Reviewed;         662 AA.
AC   Q0VEE6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=Zinc finger protein 800;
GN   Name=Znf800; Synonyms=Zfp800;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family.
CC   -!- SIMILARITY: Contains 7 C2H2-type zinc fingers.
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DR   EMBL; BC119236; AAI19237.1; -; mRNA.
DR   EMBL; BC119262; AAI19263.1; -; mRNA.
DR   IPI; IPI00357818; -.
DR   RefSeq; NP_001075147.1; NM_001081678.1.
DR   UniGene; Mm.84441; -.
DR   ProteinModelPortal; Q0VEE6; -.
DR   SMR; Q0VEE6; 227-317, 477-541, 610-639.
DR   PhosphoSite; Q0VEE6; -.
DR   PRIDE; Q0VEE6; -.
DR   Ensembl; ENSMUST00000035930; ENSMUSP00000039222; ENSMUSG00000039841.
DR   Ensembl; ENSMUST00000115320; ENSMUSP00000110975; ENSMUSG00000039841.
DR   Ensembl; ENSMUST00000115321; ENSMUSP00000110976; ENSMUSG00000039841.
DR   GeneID; 627049; -.
DR   KEGG; mmu:627049; -.
DR   UCSC; uc009bcm.1; mouse.
DR   CTD; 627049; -.
DR   MGI; MGI:1889334; Zfp800.
DR   eggNOG; roNOG17320; -.
DR   GeneTree; ENSGT00390000008140; -.
DR   HOGENOM; HBG714482; -.
DR   HOVERGEN; HBG106061; -.
DR   InParanoid; Q0VEE6; -.
DR   OMA; VSPKKSF; -.
DR   OrthoDB; EOG4J6RQD; -.
DR   NextBio; 419278; -.
DR   ArrayExpress; Q0VEE6; -.
DR   Bgee; Q0VEE6; -.
DR   CleanEx; MM_ZFP800; -.
DR   Genevestigator; Q0VEE6; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 2.
DR   SMART; SM00355; ZnF_C2H2; 7.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    662       Zinc finger protein 800.
FT                                /FTId=PRO_0000304411.
FT   ZN_FING      69     91       C2H2-type 1; degenerate.
FT   ZN_FING     231    254       C2H2-type 2.
FT   ZN_FING     288    311       C2H2-type 3.
FT   ZN_FING     357    382       C2H2-type 4.
FT   ZN_FING     484    506       C2H2-type 5.
FT   ZN_FING     517    540       C2H2-type 6.
FT   ZN_FING     616    638       C2H2-type 7.
FT   COMPBIAS     12     15       Poly-His.
FT   MOD_RES     318    318       Phosphoserine (By similarity).
FT   MOD_RES     320    320       Phosphothreonine (By similarity).
FT   MOD_RES     335    335       Phosphoserine (By similarity).
FT   MOD_RES     337    337       Phosphoserine (By similarity).
FT   MOD_RES     350    350       Phosphoserine (By similarity).
FT   MOD_RES     387    387       Phosphoserine (By similarity).
FT   MOD_RES     403    403       Phosphoserine (By similarity).
FT   MOD_RES     420    420       Phosphoserine.
FT   MOD_RES     424    424       Phosphoserine (By similarity).
FT   MOD_RES     453    453       Phosphoserine (By similarity).
FT   MOD_RES     455    455       Phosphoserine (By similarity).
FT   MOD_RES     460    460       Phosphoserine (By similarity).
FT   MOD_RES     593    593       Phosphoserine (By similarity).
SQ   SEQUENCE   662 AA;  74813 MW;  037359A69380D96D CRC64;
     MPLRDKYCQT DHHHHGCCEP VYILEPGDPP LLQQPVQTSK SGIQQIIECF RSGTKQLKHI
     LLKDVDTIFE CKLCRSLFRG LPNLITHKKF YCPPSLQMDD NLPDVNDKQS QAISDLLEAI
     YPRVDKREYI IKLEPIETNQ NAVFQYISRT DNPAEVTESS STPEQTEVQI QETSSEQLKA
     VPDADTEVEE AIEPPSIETV VDEAAAPTEE QPQESQADLE TSDSSDLGHQ LICCLCRKEF
     NSRRGVRRHI RKVHKKKMEE LKKYIETRKT PNQSSKGRSK SVLVSLSRSC PVCCKSFATK
     ANVRRHFDEV HRGLRRDSIT PDIATKPGQP LFLDSASPKK SFKTRKQKSS KAEYNLTACK
     CLLCKRKYSS QIMLKRHMQI VHKITLSGAN SKREKGPNNT ANSSEVKVEL ADSVESSPPS
     ITHSPQNELK GTNHSNEKKN TPATQKNKVK QDSESPKSAS PSAAGGQQKT RKPKLSAGFD
     FKQLYCKLCK RQFTSKQNLT KHIELHTDGN NIYVKFYKCP LCTYETRRKR DVIRHITVVH
     KKSSRYLGKI TASLEIRAIK KPIDFVLNKV AKRGPSREEA KHNDSKQDGT SNSPSKKYEV
     ADVGIEVKVT KNFSLHRCNK CGKAFAKKTY LEHHKKTHKA NATNSPEGNK TKGRSTRSKA
     LV
//
ID   CEP76_MOUSE             Reviewed;         659 AA.
AC   Q0VEJ0;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   08-MAR-2011, entry version 38.
DE   RecName: Full=Centrosomal protein of 76 kDa;
DE            Short=Cep76;
GN   Name=Cep76;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Centrosomal protein involved in regulation of centriole
CC       duplication. Required to limit centriole duplication to once per
CC       cell cycle by preventing centriole reduplication (By similarity).
CC   -!- SUBUNIT: Interacts with CEP110/CP110 and CEP97 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome (By
CC       similarity). Cytoplasm, cytoskeleton, centrosome, centriole (By
CC       similarity). Note=Does not localize along the ciliary axoneme (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the CEP76 family.
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DR   EMBL; CH466528; EDL09636.1; -; Genomic_DNA.
DR   EMBL; BC119216; AAI19217.1; -; mRNA.
DR   EMBL; BC119218; AAI19219.1; -; mRNA.
DR   IPI; IPI00761964; -.
DR   RefSeq; NP_001074542.1; NM_001081073.1.
DR   UniGene; Mm.111928; -.
DR   ProteinModelPortal; Q0VEJ0; -.
DR   STRING; Q0VEJ0; -.
DR   PhosphoSite; Q0VEJ0; -.
DR   PRIDE; Q0VEJ0; -.
DR   Ensembl; ENSMUST00000097542; ENSMUSP00000095149; ENSMUSG00000073542.
DR   GeneID; 225659; -.
DR   KEGG; mmu:225659; -.
DR   UCSC; uc008fmq.1; mouse.
DR   CTD; 225659; -.
DR   MGI; MGI:1923401; Cep76.
DR   eggNOG; roNOG11008; -.
DR   GeneTree; ENSGT00390000000781; -.
DR   HOGENOM; HBG282639; -.
DR   InParanoid; Q0VEJ0; -.
DR   OMA; MFACKYR; -.
DR   OrthoDB; EOG4PG60P; -.
DR   NextBio; 377766; -.
DR   ArrayExpress; Q0VEJ0; -.
DR   Bgee; Q0VEJ0; -.
DR   Genevestigator; Q0VEJ0; -.
DR   GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR   GO; GO:0046599; P:regulation of centriole replication; ISS:UniProtKB.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Phosphoprotein.
FT   CHAIN         1    659       Centrosomal protein of 76 kDa.
FT                                /FTId=PRO_0000378949.
FT   MOD_RES      83     83       Phosphoserine (By similarity).
SQ   SEQUENCE   659 AA;  74303 MW;  658CF10C0C3A74B5 CRC64;
     MSLPPEKASE LKQLIHQQLS KMDVHGRIRE ILAETIREEL APDQQHLSTE DLIKALRRRG
     IIDDVMKELN FVTDSVDQEL PSSPKQTVGF DKQSTLKKTN VDPTRRYLYL QVLGGKAFLE
     HLQEPEPLPG QICSTFTLCL HYRNQRFRSK PVPCACEPDF HDGFLLEVHR ESLGDGTRMA
     DSTTMLSISD PIHMVLIKTD IFGETTLVAS YFLEWRSVLG SENGVTNLTV ELMGVGTESK
     VSVGILNIKL EMYPPLSQTL SQEVVNTQLA LERQKTAEKE RLFLVYAKQW WREYLQIRPS
     HNSRLVKIFA QDENGINRPV CSYVKPLRAG RLLDTPRQAA RFVNVLGYER APVIGGGGKQ
     EQWCTLLAFL CRNKGDCEDH ANLLCSLLLG YGLEAFVCVG TKAKGAPHAW VMTCGTDGTI
     MFWESLTGHR YIHKPTNPDG PPLAEQPKPL YPYRTIGCVF NHQMFLGNCQ PSDAVETCIF
     DLNDESKWKP MSEEAIKSVC APGATTSLPP FPPLCASTID ASVTSNEIEM QLRLLVSEHR
     KDLGLTTVWE DQLSYLLSPA LASYEFERTT SISAGNEEFQ DAIRRAVPDG HTFKGFPIHF
     VYRNARRAFA TCLRSPFCEE IICCRGDQVR LAVRVRVFTY PESACAVWIM FACKYRSVL
//
ID   Q0VF55_MOUSE            Unreviewed;      1220 AA.
AC   Q0VF55;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   SubName: Full=ATPase, Ca++ transporting, plasma membrane 3;
GN   Name=Atp2b3; ORFNames=RP23-329M9.1-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Whitehead S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       family.
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DR   EMBL; BC118975; AAI18976.1; -; mRNA.
DR   EMBL; AL805924; CAM21053.1; -; Genomic_DNA.
DR   IPI; IPI00265299; -.
DR   RefSeq; NP_796210.2; NM_177236.3.
DR   UniGene; Mm.210095; -.
DR   ProteinModelPortal; Q0VF55; -.
DR   STRING; Q0VF55; -.
DR   PhosphoSite; Q0VF55; -.
DR   PRIDE; Q0VF55; -.
DR   Ensembl; ENSMUST00000088429; ENSMUSP00000085775; ENSMUSG00000031376.
DR   GeneID; 320707; -.
DR   KEGG; mmu:320707; -.
DR   UCSC; uc009tlz.1; mouse.
DR   CTD; 320707; -.
DR   MGI; MGI:1347353; Atp2b3.
DR   GeneTree; ENSGT00510000046331; -.
DR   HOGENOM; HBG456486; -.
DR   HOVERGEN; HBG061286; -.
DR   InParanoid; Q0VF55; -.
DR   OMA; MSTVIRM; -.
DR   OrthoDB; EOG4K9BBF; -.
DR   PhylomeDB; Q0VF55; -.
DR   NextBio; 397259; -.
DR   ArrayExpress; Q0VF55; -.
DR   Bgee; Q0VF55; -.
DR   Genevestigator; Q0VF55; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005388; F:calcium-transporting ATPase activity; IEA:InterPro.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   InterPro; IPR022141; ATP_Ca_trans_C.
DR   InterPro; IPR023306; ATPase_cation_domN.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR006408; ATPase_P-typ_Ca-transp_PMCA.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023300; ATPase_P-typ_cyto_domA.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Gene3D; G3DSA:2.70.150.10; ATPase_P-typ_cyto_domA; 1.
DR   Gene3D; G3DSA:3.40.1110.10; ATPase_P-typ_cyto_domN; 1.
DR   Gene3D; G3DSA:1.20.1110.10; ATPase_P-typ_TM_dom; 1.
DR   Pfam; PF12424; ATP_Ca_trans_C; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81660; ATPase_cation_domN; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01517; ATPase-IIB_Ca; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 4.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Hydrolase; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Transmembrane; Transmembrane helix; Transport.
SQ   SEQUENCE   1220 AA;  134360 MW;  016081F216656346 CRC64;
     MGDMANSSIE FHPKPQQQRE VPHVGGFGCT LAELRSLMEL RGAEALQKIQ EAYGDVSGLC
     RRLKTSPTEG LADNTNDLEK RRQIYGQNFI PPKQPKTFLQ LVWEALQDVT LIILEVAAIV
     SLGLSFYAPP GEESEACGNV SGGAEDEGEA EAGWIEGAAI LLSVICVVLV TAFNDWSKEK
     QFRGLQSRIE QEQKFTVIRN GQLLQVPVAA LVVGDIAQVK YGDLLPADGV LIQGNDLKID
     ESSLTGESDH VRKSADKDPM LLSGTHVMEG SGRMVVTAVG VNSQTGIIFT LLGAGGEEEE
     KKDKKGKQQD GAMDSSQTRA KKQDGAVAME MQPLKSAEGG EMEEREKKKA NVPKKEKSVL
     QGKLTKLAVQ IGKAGLVMSA ITVIILVLYF VIETFVVDGR VWLAECTPVY VQYFVKFFII
     GVTVLVVAVP EGLPLAVTIS LAYSVKKMMK DNNLVRHLDA CETMGNATAI CSDKTGTLTT
     NRMTVVQSYL GDTHYKEIPA PSALTPKILD LLVHAISINS AYTTKILPPE KEGALPRQVG
     NKTECALLGF VLDLKRDFQP VREQIPEDQL YKVYTFNSVR KSMSTVIRMP DGGFRLFSKG
     ASEILLKKCT NILNSNGELR GFRPRDRDDM VKKIIEPMAC DGLRTICIAY RDFSAIQEPD
     WDNENEVVGD LTCIAVVGIE DPVRPEVPEA IRKCQRAGIT VRMVTGDNIN TARAIAAKCG
     IIQPGEDFLC LEGKEFNRRI RNEKGEIEQE RLDKVWPKLR VLARSSPTDK HTLVKGIIDS
     TTGEQRQVVA VTGDGTNDGP ALKKADVGFA MGIAGTDVAK EASDIILTDD NFTSIVKAVM
     WGRNVYDSIS KFLQFQLTVN VVAVIVAFTG ACITQDSPLK AVQMLWVNLI MDTFASLALA
     TEPPTESLLL RKPYGRDKPL ISRTMMKNIL GHAVYQLTII FTLLFVGELF FDIDSGRNAP
     LHSPPSEHYT IIFNTFVMMQ LFNEINARKI HGERNVFDGI FSNPIFCTIV LGTFGIQIVI
     VQFGGKPFSC SPLSTEQWLW CLFVGVGELV WGQVIATIPT SQLKCLKEAG HGPGKDEMTD
     EELAEGEEEI DHAERELRRG QILWFRGLNR IQTQIRVVKA FRSSLYEGLE KPESKSCIHN
     FMATPEFLIN DYTHNIPLID DTDVDENEER LRAPPPPPPN QNNNAIDSGI YLTTHATKSA
     TSSAFSSRPG SPLHSMETSL
//
ID   Q0VF82_MOUSE            Unreviewed;       517 AA.
AC   Q0VF82;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   08-FEB-2011, entry version 20.
DE   SubName: Full=C330043M08Rik protein;
GN   Name=Fam188b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC118940; AAI18941.1; -; mRNA.
DR   IPI; IPI00785365; -.
DR   UniGene; Mm.268997; -.
DR   Ensembl; ENSMUST00000114365; ENSMUSP00000110005; ENSMUSG00000038022.
DR   MGI; MGI:3583959; Fam188b.
DR   GeneTree; ENSGT00530000063283; -.
DR   HOVERGEN; HBG057657; -.
DR   ArrayExpress; Q0VF82; -.
DR   Bgee; Q0VF82; -.
DR   Genevestigator; Q0VF82; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   517 AA;  58292 MW;  23DDE9B8400907D6 CRC64;
     MDSLYVEEVA ASLVREFLSR KGLNKTFVTM DQERPRCELS INSRNDLRKV LHLEFLYKEN
     KAKEKPLRTN LELITRYFLD NVGNTDNSES QEVPIPAIPV PKKNNKLPLR HSETTLVNIY
     DLSDEDTGRR TSWSEAGKAR HDSLDGDILG NFVSSKKPSH KSKAAHVDLG DSLPLVPAWE
     KVDQLHSSEP GIDVKKTMER TRPKSGLIVR GMMAGPVASS PQDSFRKRSL RRSSALSRKL
     QTPEEIQQQS EPFVHTPAYL GPQEVPDSSS DSVSRSPLGQ LNELSIEKPN VTSSSQGLSQ
     RDRPRLRSVS EDSPLGYNHT EGNSRMAQDQ LERAFKRQGV QPPSLRKNQL VSDRTDDKPD
     ALQLEDVEDE LIKEDIVLFP PPSMLKLQTV SKPIDLSLAK EIKTLLFGST FCCFSEEWKL
     QNFSFNDIAS LKYGIVQNKP AAALRCPEDS LPCPGHCRHP VASWRQRTSR GCTGFRNTAL
     QSNREIQSRW SLRNSTAFWK TIVPPLALFG DYLLSYK
//
ID   Q0VG47_MOUSE            Unreviewed;       357 AA.
AC   Q0VG47;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   30-NOV-2010, entry version 39.
DE   SubName: Full=Heterogeneous nuclear ribonucleoprotein A3;
DE   SubName: Full=Hnrpa3 protein;
DE   SubName: Full=MCG1305, isoform CRA_d;
DE   SubName: Full=MCG48756;
GN   Name=Hnrnpa3; Synonyms=Hnrpa3;
GN   ORFNames=RP23-374O4.1-001, mCG_1305, mCG_48756;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones, and Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Almeida-King J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC116250; AAI16251.1; -; mRNA.
DR   EMBL; BC116251; AAI16252.1; -; mRNA.
DR   EMBL; BC157919; AAI57920.1; -; mRNA.
DR   EMBL; BC158038; AAI58039.1; -; mRNA.
DR   EMBL; AL772404; CAM22490.1; -; Genomic_DNA.
DR   EMBL; CH466519; EDL27190.1; -; Genomic_DNA.
DR   EMBL; CH466519; EDL27191.1; -; Genomic_DNA.
DR   EMBL; CH466530; EDL35262.1; -; Genomic_DNA.
DR   IPI; IPI00269662; -.
DR   RefSeq; NP_444493.1; NM_053263.1.
DR   UniGene; Mm.316306; -.
DR   UniGene; Mm.331491; -.
DR   UniGene; Mm.379375; -.
DR   ProteinModelPortal; Q0VG47; -.
DR   SMR; Q0VG47; 7-188.
DR   STRING; Q0VG47; -.
DR   PRIDE; Q0VG47; -.
DR   Ensembl; ENSMUST00000111962; ENSMUSP00000107593; ENSMUSG00000059005.
DR   GeneID; 229279; -.
DR   KEGG; mmu:229279; -.
DR   CTD; 229279; -.
DR   eggNOG; roNOG15237; -.
DR   HOVERGEN; HBG002295; -.
DR   NextBio; 379374; -.
DR   ArrayExpress; Q0VG47; -.
DR   Bgee; Q0VG47; -.
DR   Genevestigator; Q0VG47; -.
DR   GO; GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   2: Evidence at transcript level;
KW   Ribonucleoprotein; Viral nucleoprotein; Virion.
SQ   SEQUENCE   357 AA;  37086 MW;  222DBB3DF00D2D7A CRC64;
     MEGHDPKEPE QLRKLFIGGL SFETTDDSLR EHFEKWGTLT DCVVMRDPQT KRSRGFGFVT
     YSCVEEVDAA MCARPHKVDG RVVEPKRAVS REDSVKPGAH LTVKKIFVGG IKEDTEEYNL
     RDYFEKYGKI ETIEVMEDRQ SGKKRGFAFV TFDDHDTVDK IVVQKYHTIN GHNCEVKKAL
     SKQEMQSAGS QRGRGGGSGN FMGRGGNFGG GGGNFGRGGN FGGRGGYGGG GGGSRGSYGG
     GDGGYNGFGG DGGNYGGGPG YSSRGGYGGG GPGYGNQGGG YGGGGGGYDG YNEGGNFGGG
     NYGGGGNYND FGNYSGQQQS NYGPMKGGSF GGRSSGSPYG GGYGSGGGSG GYGSRRF
//
ID   Q0VGB8_MOUSE            Unreviewed;       949 AA.
AC   Q0VGB8;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   11-JAN-2011, entry version 37.
DE   SubName: Full=Synaptic nuclear envelope 1;
GN   Name=Syne1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC110428; AAI10429.1; -; mRNA.
DR   IPI; IPI00816892; -.
DR   RefSeq; NP_071310.2; NM_022027.2.
DR   UniGene; Mm.331626; -.
DR   ProteinModelPortal; Q0VGB8; -.
DR   SMR; Q0VGB8; 589-699.
DR   STRING; Q0VGB8; -.
DR   PRIDE; Q0VGB8; -.
DR   Ensembl; ENSMUST00000095899; ENSMUSP00000093587; ENSMUSG00000019769.
DR   GeneID; 64009; -.
DR   KEGG; mmu:64009; -.
DR   UCSC; uc007egs.1; mouse.
DR   CTD; 64009; -.
DR   MGI; MGI:1927152; Syne1.
DR   eggNOG; roNOG13697; -.
DR   HOVERGEN; HBG056327; -.
DR   NextBio; 319851; -.
DR   ArrayExpress; Q0VGB8; -.
DR   Bgee; Q0VGB8; -.
DR   Genevestigator; Q0VGB8; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0040023; P:establishment of nucleus localization; IMP:MGI.
DR   InterPro; IPR012315; KASH.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Pfam; PF10541; KASH; 1.
DR   Pfam; PF00435; Spectrin; 4.
DR   SMART; SM00150; SPEC; 5.
DR   PROSITE; PS51049; KASH; 1.
PE   2: Evidence at transcript level;
KW   Repeat.
SQ   SEQUENCE   949 AA;  108779 MW;  40ABE338F614825E CRC64;
     MVVAEDLHGP RMAEDSSVDA DLPDCDCDVS RVKKLKETLV AVQQLDKNMG SLRTWLAHME
     SELAKPIVYD SCNSEEIQRK LNEQQELQRD IEKHSTGVAS VLNLCEVLLH DCDACATDAE
     CDSIQQATRN LDRRWRNICA MSMERRLKIE ETWRLWQKFL DDYSRFEDWL EVSERTAAFP
     SSSGVLYTVA KEELKKFEAF QRQVHESLTQ LELINKQYRR LARENRTDSA CSLRQMVHGG
     NQRWDDLQKR VTSILRRLKH FISQREEFET ARDSILVWLT EMDLQLTNIE HFSECDVQAK
     IKQLKAFQQE ISLNHNKIEQ IIAQGEQLIE KSEPLDAAVI EEELDELRRY CQEVFGRVER
     YHKKLIRLPL PDDHDLSDRE LDLEDSTALS DLRWQDPSAD GMPSPQPSSN PSLSLPQPLR
     SERSGRDTPA SVDSIPLEWD HDYDLSRDLE SASRTLPSED EEGEEDKEFY LRGAVGLSGD
     PSSLESQMRQ LDKALDDSRF QIQQTANILR SKTPTGPDLD TSYKGYMKLL GECSGSIDSV
     RRLEHKLAEE ESFPGFVNLN STETQTAGVI DRWELLQAQA MSKELRMKQN LQKWQQFNSD
     LNNIWAWLGE TEEELDRLQH LALSTDIHTI ESHIKKLKEL QKAVDHRKAI ILSINLCSSE
     FTQADSKESH DLQDRLSQMN GRWDRVCSLL EDWRGLLQDA LMQCQEFHEM SHALLLMLEN
     IDRRKNEIVP IDSTLDPETL QDHHKQLMQI KQELLKSQLR VASLQDMSRQ LLVNAEGSDC
     LEAKEKVHVI GNRLKLLLKE VSHHIKDLEK LLDMSSSQQD LSSWSSADEL DTSGSVSPTS
     GRSTPNRQKS PRGKCSLSQP GPSVSSPKSR STRDGSDSSR SDPRPERVGR AFLFRILRAA
     LPFQLLLLLL IGLTCLVPMS EKDYSCALSN NFARSFHPML RYTNGPPPL
//
ID   TANC1_MOUSE             Reviewed;        1856 AA.
AC   Q0VGY8; A2AUL4; A2AUL6; Q80VD2; Q8C0Q6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=Protein TANC1;
DE   AltName: Full=Tetratricopeptide repeat, ankyrin repeat and coiled-coil domain-containing protein 1;
GN   Name=Tanc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Head, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1665, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May be a scaffold component in the postsynaptic density
CC       (By similarity).
CC   -!- SUBUNIT: Interacts probably directly with DLG1, DLG4, HOMER1.
CC       Interacts with DLGAP1, INA, CAMK2A, GRIN2B and GRIA1. Interacts
CC       with TNIK (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane, postsynaptic density (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q0VGY8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q0VGY8-2; Sequence=VSP_030829, VSP_030830, VSP_030831;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated; probably by MINK1 and TNIK upon stimulation
CC       by RAP2A (By similarity).
CC   -!- SIMILARITY: Belongs to the TANC family.
CC   -!- SIMILARITY: Contains 11 ANK repeats.
CC   -!- SIMILARITY: Contains 3 TPR repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM27490.1; Type=Erroneous gene model prediction;
CC       Sequence=CAM27492.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK030022; BAC26741.1; -; mRNA.
DR   EMBL; AL929160; CAM27490.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL929160; CAM27492.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC079914; AAH79914.1; -; mRNA.
DR   EMBL; BC047437; AAH47437.1; -; mRNA.
DR   IPI; IPI00309636; -.
DR   IPI; IPI00349296; -.
DR   RefSeq; NP_938036.2; NM_198294.2.
DR   UniGene; Mm.27917; -.
DR   ProteinModelPortal; Q0VGY8; -.
DR   SMR; Q0VGY8; 374-425, 907-1269, 1286-1412.
DR   STRING; Q0VGY8; -.
DR   PhosphoSite; Q0VGY8; -.
DR   PRIDE; Q0VGY8; -.
DR   Ensembl; ENSMUST00000037526; ENSMUSP00000036003; ENSMUSG00000035168.
DR   GeneID; 66860; -.
DR   KEGG; mmu:66860; -.
DR   UCSC; uc008jtj.1; mouse.
DR   CTD; 66860; -.
DR   MGI; MGI:1914110; Tanc1.
DR   HOGENOM; HBG443929; -.
DR   HOVERGEN; HBG061464; -.
DR   InParanoid; Q0VGY8; -.
DR   OMA; IMDKTAR; -.
DR   PhylomeDB; Q0VGY8; -.
DR   NextBio; 322843; -.
DR   ArrayExpress; Q0VGY8; -.
DR   Bgee; Q0VGY8; -.
DR   Genevestigator; Q0VGY8; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 2.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
DR   Pfam; PF00023; Ank; 4.
DR   SMART; SM00248; ANK; 10.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 6.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ANK repeat; Cell junction; Cell membrane;
KW   Membrane; Phosphoprotein; Postsynaptic cell membrane; Repeat; Synapse;
KW   TPR repeat.
FT   CHAIN         1   1856       Protein TANC1.
FT                                /FTId=PRO_0000316960.
FT   REPEAT      893    925       ANK 1.
FT   REPEAT      931    960       ANK 2.
FT   REPEAT      964    993       ANK 3.
FT   REPEAT      997   1026       ANK 4.
FT   REPEAT     1037   1066       ANK 5.
FT   REPEAT     1075   1104       ANK 6.
FT   REPEAT     1108   1137       ANK 7.
FT   REPEAT     1141   1170       ANK 8.
FT   REPEAT     1174   1203       ANK 9.
FT   REPEAT     1207   1236       ANK 10.
FT   REPEAT     1240   1269       ANK 11.
FT   REPEAT     1286   1319       TPR 1.
FT   REPEAT     1333   1366       TPR 2.
FT   REPEAT     1368   1400       TPR 3.
FT   COMPBIAS    167    240       Ser-rich.
FT   COMPBIAS   1647   1686       Ser-rich.
FT   MOD_RES      60     60       Phosphoserine (By similarity).
FT   MOD_RES      63     63       Phosphoserine (By similarity).
FT   MOD_RES     204    204       Phosphoserine (By similarity).
FT   MOD_RES     211    211       Phosphoserine (By similarity).
FT   MOD_RES    1662   1662       Phosphoserine (By similarity).
FT   MOD_RES    1665   1665       Phosphoserine.
FT   VAR_SEQ       1    102       Missing (in isoform 2).
FT                                /FTId=VSP_030829.
FT   VAR_SEQ    1079   1092       ALTAAAGRGKVEIC -> GNYASSVCSQQPRA (in
FT                                isoform 2).
FT                                /FTId=VSP_030830.
FT   VAR_SEQ    1093   1856       Missing (in isoform 2).
FT                                /FTId=VSP_030831.
FT   CONFLICT    166    166       L -> M (in Ref. 1; BAC26741).
FT   CONFLICT    209    209       I -> N (in Ref. 1; BAC26741).
FT   CONFLICT   1102   1102       V -> L (in Ref. 3; AAH79914).
SQ   SEQUENCE   1856 AA;  200805 MW;  5CD2DD065C564E33 CRC64;
     MLKAVLKKSR EGGKGSKKEA GGDFGSETPA LSSSGDSPVN SLSTTEDTYR VSLAKGVSMS
     LPSSPLLPRQ SLLTQSRSNK KSPGPVRKPK YVESPRVPGD PVMIPFGEGS KPSEPSATEA
     KADNEPSCSP AAQELLTRLG FLLGEGIPSA THITIEDKNE AMCTALSQGI SPCSTLTSST
     ASPSTDSPCS TLNSCVSKTA ASKSPCETIS SPSSTLESKD SGIIATITSS SENDDRSGSS
     LEWNRDGSLR LGVQKGVLHD RRADNCSPVA EEETTGSAES VLPKAEPSAG DGPVPYPQSS
     GSLIMPRPNS VAATSSTKLE DLSYLDGQRN APLRTSIRLP WHNTAGGRAP EVKARFAPYK
     PQEILLKPLL FEVPSITTDS VFVGRDWLFH QIEENLRNTE LAENRGAVVV GSVGFGKTAI
     ISKLVALSCH GSRMRQIASS SPSLSPKSSD PTQDLPGTPL LSPSSSTSAL SVTRTPAGPG
     TADSQRPRED AVKYLASKVV AYHYCQADNT YTCLVPEFVH SIAALLCRSH QLAAYRDLLI
     KEPQLQSMLS LRSCVQDPVA AFKRGVLEPL TSLRNEQKIP EEEYIILIDG LNEAEFHKPD
     YGDTLSSFIT KIIPKFPTWL KLIVTVRANF QEIISALPFV KLSLDDFPDN KDIHSDLHAY
     VQHRVHSSQD ILSNISLNGK ADAALISKVS SHLVLRSLGS YLYLKLTLDL FQRGHLVIKS
     ASYKVVPVSL SELYLLQCNM KFMTQSAFDR ALPILNVALA SLHPMTDEQI FQAINAGHIQ
     GEQGWEDFQQ RMEALSCFLI KRRDKTRMFC HPSFREWLVW RADGESTAFL CEPRNGHALL
     AFMFSRQESK LNRQQTMELG HHILKAHIFK GLSKKTGVSS SHLQALWIGY STEGLSAALA
     SLRNLYTPNV KVSRLLILGG ANVNYRTEVL NNAPILCVQS HLGHEEVVTL LLEFGACLDG
     MSENGMNALC YAAAAGHMKL VCLLIKKGAR VDHLDKKGQC ALVHSALRGH SDILQYLLNC
     EWSAGPPQPG TLRKSQALQQ ALTAAASMGH SSVVQSLLGM AEEHEIEVNG TDTLWGETAL
     TAAAGRGKVE ICELLLERGA AVSRANRRGV PPLFCAARQG HWQVVRLLLD RGCDVNLSDK
     QGRTPLMVAS CEGHLSTVEF LLSKGAALSS LDKEGLSALS WACLKGHRAV VQYLVEEGAE
     IDQTDKNGRT PLDLAAFYGD AETVLYLVEK GAVIEHVDHS GMRPLDRAIG CRNTAVVVTL
     LRKGAKLGNA AWAMATSKPD ILIILLQKLV EEGNVMYKKG KMKEAAQRYQ YALRKFPREG
     LGEDMRPFNE LRVSLYLNLS RCRRKTNDFG LAEEFASKAL ELKPKSYEAF YARARAKRNS
     RQFLAALADL QEAVKLCPNN QEIKRLLARV EEECKQLQRN QQQKQQGPPP APANDSDNEE
     DAPASSLKDH FPIEEAEEED TSSQEESISP TPRSQPPPSV PSPYIRNLQE GLQSKGRSAS
     PQSRAGISKS LRETVAQSGL VMQPTKQAQI VKTNQHLGSG QSSMRNSSTK IQVSSQNPPP
     SPMPGRVSAA PAVSRNQHLE GTGPFTAGTG CGHFGDRLGA SQSLQLQRSE SGTAYPLPSK
     VKAAERLLAH ASVAVDMAPP NQGGPVSCSD VRHPASLSSS GSSGSPSSSI KMSSSTSSLT
     SSSSVSDGFK VQGPDSRIRD KGTTQVQGGT AEHRPRNTPF MGIMDKTARF QQQSNPPNRS
     WHCPVAEGLL TNTATAAGLQ SNSEKPTLKP GGYCSQAKPC SVPPLSMGVH NGAQVKELEE
     NKCQIPALCQ DNRITKGVPH LYPEGVSKQP LHVSTEAHRS HLTSAKPKRS FIESNV
//
ID   PSA_MOUSE               Reviewed;         920 AA.
AC   Q11011; Q3UZE0; Q5PR74; Q91VJ8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Puromycin-sensitive aminopeptidase;
DE            Short=PSA;
DE            EC=3.4.11.14;
DE   AltName: Full=Cytosol alanyl aminopeptidase;
DE            Short=AAP-S;
GN   Name=Npepps; Synonyms=Psa;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   MEDLINE=96070789; PubMed=7592939; DOI=10.1074/jbc.270.45.26931;
RA   Constam D.B., Tobler A.R., Rensing-Ehl A., Kemler I., Hersh L.B.,
RA   Fontana A.;
RT   "Puromycin-sensitive aminopeptidase. Sequence analysis, expression,
RT   and functional characterization.";
RL   J. Biol. Chem. 270:26931-26939(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-920.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=10407043;
RA   Osada T., Ikegami S., Takiguchi-Hayashi K., Yamazaki Y.,
RA   Katoh-Fukui Y., Higashinakagawa T., Sakaki Y., Takeuchi T.;
RT   "Increased anxiety and impaired pain response in puromycin-sensitive
RT   aminopeptidase gene-deficient mice obtained by a mouse gene-trap
RT   method.";
RL   J. Neurosci. 19:6068-6078(1999).
RN   [7]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=11376108; DOI=10.1210/me.15.6.882;
RA   Osada T., Watanabe G., Sakaki Y., Takeuchi T.;
RT   "Puromycin-sensitive aminopeptidase is essential for the maternal
RT   recognition of pregnancy in mice.";
RL   Mol. Endocrinol. 15:882-893(2001).
RN   [8]
RP   TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=11376114; DOI=10.1210/me.15.6.960;
RA   Osada T., Watanabe G., Kondo S., Toyoda M., Sakaki Y., Takeuchi T.;
RT   "Male reproductive defects caused by puromycin-sensitive
RT   aminopeptidase deficiency in mice.";
RL   Mol. Endocrinol. 15:960-971(2001).
RN   [9]
RP   NITRATION [LARGE SCALE ANALYSIS] AT TYR-465, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16800626; DOI=10.1021/bi060474w;
RA   Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
RA   Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
RA   Squier T.C., Bigelow D.J.;
RT   "Endogenously nitrated proteins in mouse brain: links to
RT   neurodegenerative disease.";
RL   Biochemistry 45:8009-8022(2006).
RN   [10]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=18209067;
RA   Towne C.F., York I.A., Neijssen J., Karow M.L., Murphy A.J.,
RA   Valenzuela D.M., Yancopoulos G.D., Neefjes J.J., Rock K.L.;
RT   "Puromycin-sensitive aminopeptidase limits MHC class I presentation in
RT   dendritic cells but does not affect CD8 T cell responses during viral
RT   infections.";
RL   J. Immunol. 180:1704-1712(2008).
CC   -!- FUNCTION: Aminopeptidase with broad substrate specificity for
CC       several peptides. Involved in proteolytic events essential for
CC       cell growth and viability. May act as regulator of neuropeptide
CC       activity. Plays a role in the antigen-processing pathway for MHC
CC       class I molecules. Involved in the N-terminal trimming of
CC       cytotoxic T cell epitope precursors. Digests the poly-Q peptides
CC       found in many cellular proteins.
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal amino acid,
CC       preferentially alanine, from a wide range of peptides, amides and
CC       arylamides.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- ENZYME REGULATION: Strongly inhibited by bestatin, leuhistin,
CC       actinonin, amastatin, 1,10-phenanthroline, DFP, PCMBS, Zn(2+),
CC       Cd(2+), Co(2+), Cu(2+), Hg(2+), EDTA and puromycin. Not inhibited
CC       by PMSF, and only slightly inhibited by leupeptin and aprotinin.
CC       Activity is increased by Mg(2+) and Ca(2+) (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Highest expression in brain,
CC       particularly the striatum and hippocampus. Expressed in Sertoli
CC       cells.
CC   -!- DISRUPTION PHENOTYPE: Mice exhibit dwarfism, increased anxiety,
CC       impaired pain responses and do not reproduce as well as wild-type
CC       mice. More MHC class I molecules are displayed on dendritic cell
CC       surfaces.
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-46 is the initiator.
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DR   EMBL; U35646; AAC52409.1; -; mRNA.
DR   EMBL; AL627445; CAM26998.1; -; Genomic_DNA.
DR   EMBL; CH466556; EDL16075.1; -; Genomic_DNA.
DR   EMBL; BC009653; AAH09653.1; -; mRNA.
DR   EMBL; BC086798; AAH86798.1; -; mRNA.
DR   EMBL; BC098212; AAH98212.1; -; mRNA.
DR   EMBL; AK133898; BAE21917.1; -; mRNA.
DR   IPI; IPI00130000; -.
DR   PIR; T10052; T10052.
DR   RefSeq; NP_032968.2; NM_008942.2.
DR   UniGene; Mm.29824; -.
DR   ProteinModelPortal; Q11011; -.
DR   SMR; Q11011; 48-916.
DR   STRING; Q11011; -.
DR   MEROPS; M01.010; -.
DR   PhosphoSite; Q11011; -.
DR   PRIDE; Q11011; -.
DR   Ensembl; ENSMUST00000001480; ENSMUSP00000001480; ENSMUSG00000001441.
DR   GeneID; 19155; -.
DR   KEGG; mmu:19155; -.
DR   CTD; 19155; -.
DR   MGI; MGI:1101358; Npepps.
DR   GeneTree; ENSGT00560000076993; -.
DR   HOGENOM; HBG515894; -.
DR   HOVERGEN; HBG106325; -.
DR   InParanoid; Q11011; -.
DR   OrthoDB; EOG4S7JP9; -.
DR   PhylomeDB; Q11011; -.
DR   ArrayExpress; Q11011; -.
DR   Bgee; Q11011; -.
DR   CleanEx; MM_NPEPPS; -.
DR   Genevestigator; Q11011; -.
DR   GermOnline; ENSMUSG00000001441; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_N.
DR   InterPro; IPR015568; Peptidase_M1_puromycin-sens.
DR   PANTHER; PTHR11533:SF33; Pept_M1_puromysin-sens; 1.
DR   PANTHER; PTHR11533; Peptidase_M1; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding;
KW   Metalloprotease; Nitration; Nucleus; Protease; Zinc.
FT   CHAIN         1    920       Puromycin-sensitive aminopeptidase.
FT                                /FTId=PRO_0000095117.
FT   MOTIF       727    731       Nuclear localization signal (Potential).
FT   ACT_SITE    354    354       By similarity.
FT   ACT_SITE    405    405       Proton donor (Potential).
FT   METAL       353    353       Zinc; catalytic (By similarity).
FT   METAL       357    357       Zinc; catalytic (By similarity).
FT   METAL       376    376       Zinc; catalytic (By similarity).
FT   MOD_RES      49     49       N6-acetyllysine (By similarity).
FT   MOD_RES     465    465       Nitrated tyrosine.
FT   CONFLICT    185    185       A -> P (in Ref. 1; AAC52409).
SQ   SEQUENCE   920 AA;  103325 MW;  BECF4139F074A356 CRC64;
     MWLAAAVPSL ARRLLLLGPP PPPLLLLLSR SSRRRRRLHS LGLAAMPEKR PFERLPAEVS
     PINYSLCLKP DLLDFTFEGK LEAAAQVRQA TNQIVMNCAD IDIITASYAP EGDEEIHATG
     FNYQNEDEKV TLSFPSTLQT GTGTLKIDFV GELNDKMKGF YRSRYTTPAG EVRYAAVTQF
     EATDARRAFP CWDEPAIKAT FDISLVVPKD RVALSNMNVI DRKPYPDDEN LVEVKFARTP
     VMSTYLVAFV VGEYDFVETR SKDGVCVRVY TPVGKAEQGK FALEVAAKTL PFYKDYFNVP
     YPLPKIDLIA IADFAAGAME NWGLVTYRET ALLIDPKNSC SSSRQWVALV VGHELAHQWF
     GNLVTMEWWT HLWLNEGFAS WIEYLCVDHC FPEYDIWTQF VSADYTRAQE LDALDNSHPI
     EVSVGHPSEV DEIFDAISYS KGASVIRMLH DYIGDKDFKK GMNMYLTKFQ QKNAATEDLW
     ESLESASGKP IAAVMNTWTK QMGFPLIYVE AEQVEDDRVL KLSQKKFCAS GPYGGEDCPQ
     WMVPITISTS EDPNQAKLKI LMDKPEMSVV LKNVKPDQWV KLNLGTVGFY RTQYSSAMLE
     SLLPGIRDLS LPPVDRLGLQ NDLFSLARAG IISTVEVLKV MEAFVNEPNY TVWSDLSCNL
     GILSTLLSHT DFYEEIQEFV KDVFSPIGER LGWDPKPGEG HLDALLRGLV LGKLGKAGHK
     ATLEEARRRF KEHVEGKQIL SADLRSPVYL TVLKHGDGAT LDIMLKLHKQ ADMQEEKNRI
     ERVLGATLSP ELIQKVLTFA LSEEVRPQDT VSVIGGVAGG SKHGRKAAWK FIKDNWEELH
     NRYQGGFLIS RLIKLSVEGF AVDKMAGEVK AFFESHPAPS AERTIQQCCE NILLNAAWLK
     RDADSIHQYL LQRKTSPPSV
//
ID   Q148U4_MOUSE            Unreviewed;      1299 AA.
AC   Q148U4;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   SubName: Full=Plekhg1 protein;
GN   Name=Plekhg1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
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DR   EMBL; BC117966; AAI17967.1; -; mRNA.
DR   IPI; IPI00886074; -.
DR   UniGene; Mm.150831; -.
DR   ProteinModelPortal; Q148U4; -.
DR   SMR; Q148U4; 22-325.
DR   PhosphoSite; Q148U4; -.
DR   Ensembl; ENSMUST00000042438; ENSMUSP00000040495; ENSMUSG00000040624.
DR   Ensembl; ENSMUST00000120274; ENSMUSP00000114056; ENSMUSG00000040624.
DR   Ensembl; ENSMUST00000136671; ENSMUSP00000119950; ENSMUSG00000040624.
DR   UCSC; uc007ehl.1; mouse.
DR   MGI; MGI:2676551; Plekhg1.
DR   eggNOG; roNOG04409; -.
DR   HOVERGEN; HBG053605; -.
DR   InParanoid; Q148U4; -.
DR   OrthoDB; EOG4ZKJKG; -.
DR   ArrayExpress; Q148U4; -.
DR   Bgee; Q148U4; -.
DR   Genevestigator; Q148U4; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1299 AA;  145993 MW;  81E43F07FB2D780D CRC64;
     MDTSGTPQTT ADSATSPKLL YVDRVVQEIL ETERTYVQDL KSIVEGYLEC IRDQTKLPLV
     TEDRAALFGN IQDIYHFNSE LLQDLENCEN DPVAIAECFV SKSEEFHIYT QYCTNYPRSV
     AVLTECMRNK ILTKFFRERQ ETLRHSLPLG SYLLKPVQRI LKYHLLLHEI ENHLDKATEG
     YDVVLDAIDT MQRVAWHIND MKRKHEHAVR LQEIQSLLTN WEGPDLTSYG ELVLEGTFRI
     QKAKKERTLF LLDQLLLITK KRDDTFTYKA HILCGNLMLV EVIPKEPLSF SVFHYKNPKL
     QHTVQAKSQQ DKRLWVLHLK RLILENHAAA AKIPAKAKQA ILEMDAIHYP GFCYSPEGEM
     KTPCGSAPHR LRRKSEPSSR SHKVLKTSET SQDIQKVSRE ESPSQLTSAV PAQRNCQPGS
     AAVINMLRGG GGVRSPWTDH HIRQRTDHHI RQPLFPSRRS PQENEDDDDD YQMFVPSFSS
     SDLNSTRLCE ENASSRPCSW HLGLIEPTEI SSSGHRIVRR ASSAGESNAC PPEVRIRDCD
     DSQYCPGRQL QNSPRPGGER GMTPYGSSVE LTIDDIDHVY DNISFEDLKL MVAKRDETEC
     SFSKPSRDSV RPKSTPELAF SKRQVSHSTS SLHSRKEAGL GGQEASTQSV HEHQEVEENI
     YDTIGLPDPP SMNLNHSSLH QPKRSTFLGL EADFACCDSL RPFVSQDSLQ FSEDDISYHQ
     GPSDTEYLSL LYDSPRCNLP IADKALSDKL SEEVDEIWND LENYIKKNED KSRDRLLAAF
     PVSKDDAPER LYVDSTHELG RDTGHATSML ALPTSQTFLL PGKSRVVRAS RANCSLDNDI
     ISTEGSFLSL NQLSLASDGP PVDNPYDLAN CSLPQTDPEN PDPGMEVTDK TKSRVFMMAR
     QYSQKIKKVN QILKVKSPEL EQPPSSQHRP SHKDLVAILE EKRQGGPAIG ARIAEYSQLY
     DQIVFRETPL KAQKDGWASP QGPTLHRPVS PPQAQGAGED WLWHSPYSNG ELADFSPQTE
     QDSKSKYPIT LESTTKIRPR QLSGACSVPS LQVSDPLLGS VQQRCSVVVS QPHKENSGQS
     PLYNSLGRKA ISAKPQPYSR PQSSSSILIN KSLDSINYPS ETETKQLLSS QKSPRGASQQ
     DLPSGLANSC QQDRGKRSDL TLQDSQKVLV VNRNLPLSAQ IATQNYFCNF KDPEGDEDDY
     VEIKSEEDEV RLDLSPRRGR KSDPQTPDPD CSDSICSHST PYSLKEPVSG RLGLPPYLTA
     CKDSDKLNDY LWRGPSPNQQ NIVQSLREKF QCLSSSSFA
//
ID   K1468_MOUSE             Reviewed;        1216 AA.
AC   Q148V7; Q148V6; Q6PAN5; Q6ZPQ2; Q8C9Z0; Q8CCT3; Q8CD48;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   08-MAR-2011, entry version 40.
DE   RecName: Full=LisH domain and HEAT repeat-containing protein KIAA1468;
GN   Name=Kiaa1468;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 8-1216 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb, Testis, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-22; THR-32;
RP   SER-180; THR-183 AND SER-186, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q148V7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q148V7-2; Sequence=VSP_030019;
CC       Name=3;
CC         IsoId=Q148V7-3; Sequence=VSP_030018, VSP_030020, VSP_030021;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 3 HEAT repeats.
CC   -!- SIMILARITY: Contains 1 LisH domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC30530.1; Type=Erroneous initiation;
CC       Sequence=BAC98178.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it is derived from pre-RNA;
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DR   EMBL; AK129368; BAC98178.1; ALT_SEQ; Transcribed_RNA.
DR   EMBL; AK031484; BAC27422.1; -; mRNA.
DR   EMBL; AK032147; BAC27723.1; -; mRNA.
DR   EMBL; AK040168; BAC30530.1; ALT_INIT; mRNA.
DR   EMBL; BC060194; AAH60194.1; -; mRNA.
DR   EMBL; BC117949; AAI17950.1; -; mRNA.
DR   EMBL; BC117950; AAI17951.1; -; mRNA.
DR   IPI; IPI00228693; -.
DR   IPI; IPI00622704; -.
DR   IPI; IPI00880223; -.
DR   RefSeq; NP_083625.1; NM_029349.1.
DR   RefSeq; NP_775279.2; NM_173187.3.
DR   UniGene; Mm.337339; -.
DR   ProteinModelPortal; Q148V7; -.
DR   SMR; Q148V7; 562-697, 1004-1029.
DR   STRING; Q148V7; -.
DR   PhosphoSite; Q148V7; -.
DR   PRIDE; Q148V7; -.
DR   Ensembl; ENSMUST00000039173; ENSMUSP00000039178; ENSMUSG00000026319.
DR   Ensembl; ENSMUST00000086721; ENSMUSP00000083926; ENSMUSG00000026319.
DR   GeneID; 227446; -.
DR   KEGG; mmu:227446; -.
DR   UCSC; uc007cgk.1; mouse.
DR   MGI; MGI:1922832; 2310035C23Rik.
DR   HOVERGEN; HBG062583; -.
DR   InParanoid; Q148V7; -.
DR   OrthoDB; EOG4N5VW1; -.
DR   NextBio; 378600; -.
DR   ArrayExpress; Q148V7; -.
DR   Bgee; Q148V7; -.
DR   CleanEx; MM_2310035C23RIK; -.
DR   Genevestigator; Q148V7; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000357; HEAT.
DR   InterPro; IPR021133; HEAT_type_2.
DR   InterPro; IPR006594; LisH_dimerisation.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 2.
DR   Pfam; PF02985; HEAT; 1.
DR   SMART; SM00667; LisH; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
DR   PROSITE; PS50896; LISH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Phosphoprotein;
KW   Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1216       LisH domain and HEAT repeat-containing
FT                                protein KIAA1468.
FT                                /FTId=PRO_0000313094.
FT   DOMAIN      255    287       LisH.
FT   REPEAT      601    639       HEAT 1.
FT   REPEAT      640    679       HEAT 2.
FT   REPEAT     1004   1042       HEAT 3.
FT   COILED      197    231       Potential.
FT   COILED      358    397       Potential.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      20     20       Phosphoserine.
FT   MOD_RES      22     22       Phosphoserine.
FT   MOD_RES      32     32       Phosphothreonine.
FT   MOD_RES      56     56       Phosphoserine (By similarity).
FT   MOD_RES     180    180       Phosphoserine.
FT   MOD_RES     182    182       Phosphoserine (By similarity).
FT   MOD_RES     183    183       Phosphothreonine.
FT   MOD_RES     186    186       Phosphoserine.
FT   MOD_RES     193    193       Phosphoserine (By similarity).
FT   MOD_RES     453    453       Phosphoserine (By similarity).
FT   VAR_SEQ      78    109       Missing (in isoform 3).
FT                                /FTId=VSP_030018.
FT   VAR_SEQ     205    228       Missing (in isoform 2).
FT                                /FTId=VSP_030019.
FT   VAR_SEQ     990   1000       LLVKGVNETLV -> VGYIILSCFYL (in isoform
FT                                3).
FT                                /FTId=VSP_030020.
FT   VAR_SEQ    1001   1216       Missing (in isoform 3).
FT                                /FTId=VSP_030021.
FT   CONFLICT     82     82       L -> P (in Ref. 2; BAC27422).
FT   CONFLICT    431    431       E -> K (in Ref. 2; BAC27422).
FT   CONFLICT   1202   1202       T -> A (in Ref. 2; BAC27422).
SQ   SEQUENCE   1216 AA;  134587 MW;  AFDC80110D00FA71 CRC64;
     MAAMAPGGGG SGSGVNPFLS DSDEDDDEVA ATEDRRAGLR LGAGVGLDPG SAGSLSPQDP
     MALGSSARPG LAVEMSAAPA ALGGSGETPA RLSIDAIAAQ LLRDQYLLTA LELHTELLES
     GRELPRLRDY FSNPGNFERQ SGTPPGMGAP GIPGASIVGG AGGREPSTTS GGGQLNRAGS
     ISTLDSLDFA RYSDDGNRET DERVAVLEFE LRKAKETIQA LRANLTKAAE HEVPLQERKN
     YKSSPEIQEP IKPLEKRALN FLVNEFLLKN NYKLTSITFS DENDDQDFEL WDDVGLNIPK
     PPDLLQLYRD FGNHQVTGKD LVDVASGVDE DELEALTPIL GNVPPTLDTP LPIENTLLVQ
     KLEDKISLLN NEKWSLMEQI RRLESEMDIL KAEHFATPAV GDSVQPSLVW SSQKDSEDNR
     QSPAVNSSDQ EKTKDVHLEI PDAADSFIPK ENSSGSFPRK EREELPPSSV SNKTTLHFDQ
     PNRKLSPAFH QALLSFCRMS ADSRLGSEVS RIADSEKSVM LMLGRCLPHI VPNVLLAKRE
     ELIPLILCTA CLHPEPKERD QLLHILFNLI KRPDDEQRQM ILTGCVAFAR HVGPTRVEAE
     LLPQCWEQIN HKYPERRLLV AESCGALAPY LPKEIRSSLV LSMLQQMLME DKADLVREAV
     IKSLGIIMGY IDDPDKYQQG FELLLSALGD PSERVVSATH QVFLPAYAAW TTELGNLQSH
     LIPTLLNKIE KLLREGEHGL DEHKLHMYLS ALQSLIPSLF ALVLQNAPFS SKAKLHGEVP
     HIEVTRFPRP MSPLQDVSTI IGSREQLAVL LQLYDYQLEH EGTTGWESLL WVVNQLLPQL
     IEIVGKINVT STACVHEFSR FFWRLCRTFG KIFTNTKVKP QFQEILRLSE ENIDSSAGNG
     VLTKATVPIY ATGVLTCYIQ EEDRKLLVGF LEDVMTLLSL SHAPLDSLKA SFVELGANPA
     YHELLLTVLW YGVVHTSALV RCTAARMFEL LVKGVNETLV AQRVVPALIT LSSDPEISVR
     IATIPAFGTI METVIQRELL ERVKMQLASF LEDPQYQDQH SLHTEVIRTF GRVGPNAEPR
     FRDEFVIPHL HKLALVNNLQ IVDSKKLDIA THLFEAYSAL SCCFISEDLM VNHFLPGLRC
     LRTDMEHLSP EHEVILSSMI KECEQKVENK TVQEPPGSMS IAASLVSEDT KTKFLNKMGQ
     LTTSGAMLAN VFQRKK
//
ID   FA83H_MOUSE             Reviewed;        1209 AA.
AC   Q148V8; Q8BZF6; Q8CI79; Q8R5C2; Q8R5D0;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=Protein FAM83H;
GN   Name=Fam83h;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515; SER-841; SER-926
RP   AND SER-1041, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=18252228; DOI=10.1016/j.ajhg.2007.09.020;
RA   Kim J.-W., Lee S.-K., Lee Z.H., Park J.-C., Lee K.-E., Lee M.-H.,
RA   Park J.-T., Seo B.-M., Hu J.C.-C., Simmer J.P.;
RT   "FAM83H mutations in families with autosomal-dominant hypocalcified
RT   amelogenesis imperfecta.";
RL   Am. J. Hum. Genet. 82:489-494(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-893, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522; SER-904; SER-926;
RP   SER-959 AND SER-970, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522; SER-948 AND
RP   SER-970, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May play a major role in the structural organization and
CC       calcification of developing enamel (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in tooth follicle, eye, liver and
CC       kidney.
CC   -!- SIMILARITY: Belongs to the FAM83 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH36149.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK035531; BAC29093.1; -; mRNA.
DR   EMBL; BC022937; AAH22937.1; -; mRNA.
DR   EMBL; BC023045; AAH23045.1; -; mRNA.
DR   EMBL; BC036149; AAH36149.1; ALT_INIT; mRNA.
DR   EMBL; BC117947; AAI17948.1; -; mRNA.
DR   EMBL; BC117948; AAI17949.1; -; mRNA.
DR   IPI; IPI00227516; -.
DR   RefSeq; NP_001161725.1; NM_001168253.1.
DR   RefSeq; NP_598848.2; NM_134087.2.
DR   UniGene; Mm.267178; -.
DR   ProteinModelPortal; Q148V8; -.
DR   PhosphoSite; Q148V8; -.
DR   PRIDE; Q148V8; -.
DR   Ensembl; ENSMUST00000060807; ENSMUSP00000059839; ENSMUSG00000046761.
DR   GeneID; 105732; -.
DR   KEGG; mmu:105732; -.
DR   NMPDR; fig|10090.3.peg.30107; -.
DR   CTD; 105732; -.
DR   MGI; MGI:2145900; Fam83h.
DR   eggNOG; roNOG08434; -.
DR   GeneTree; ENSGT00550000074310; -.
DR   HOGENOM; HBG714924; -.
DR   HOVERGEN; HBG107907; -.
DR   InParanoid; Q148V8; -.
DR   OMA; RHLEMDA; -.
DR   OrthoDB; EOG483D58; -.
DR   PhylomeDB; Q148V8; -.
DR   NextBio; 357852; -.
DR   ArrayExpress; Q148V8; -.
DR   Bgee; Q148V8; -.
DR   CleanEx; MM_AA409316; -.
DR   Genevestigator; Q148V8; -.
DR   GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR   InterPro; IPR012461; DUF1669.
DR   PANTHER; PTHR16181; DUF1669; 1.
DR   Pfam; PF07894; DUF1669; 1.
PE   1: Evidence at protein level;
KW   Biomineralization; Phosphoprotein.
FT   CHAIN         1   1209       Protein FAM83H.
FT                                /FTId=PRO_0000324489.
FT   MOD_RES     512    512       Phosphoserine (By similarity).
FT   MOD_RES     515    515       Phosphoserine.
FT   MOD_RES     522    522       Phosphoserine.
FT   MOD_RES     639    639       Phosphoserine (By similarity).
FT   MOD_RES     778    778       Phosphoserine (By similarity).
FT   MOD_RES     841    841       Phosphoserine.
FT   MOD_RES     871    871       Phosphoserine (By similarity).
FT   MOD_RES     873    873       Phosphothreonine (By similarity).
FT   MOD_RES     893    893       Phosphoserine.
FT   MOD_RES     904    904       Phosphoserine.
FT   MOD_RES     926    926       Phosphoserine.
FT   MOD_RES     937    937       Phosphoserine (By similarity).
FT   MOD_RES     948    948       Phosphoserine.
FT   MOD_RES     959    959       Phosphoserine.
FT   MOD_RES     970    970       Phosphoserine.
FT   MOD_RES     977    977       Phosphoserine (By similarity).
FT   MOD_RES    1035   1035       Phosphoserine (By similarity).
FT   MOD_RES    1041   1041       Phosphoserine.
FT   MOD_RES    1057   1057       Phosphoserine (By similarity).
FT   CONFLICT    873    873       T -> A (in Ref. 1; BAC29093).
SQ   SEQUENCE   1209 AA;  131115 MW;  1954B609EA75EF25 CRC64;
     MARRSQSSSQ GDNPLAPGYL PPHYKEYYRL AVDALTEGGP EAYNRFLASE GAPDFLCPEE
     LEHVSRHLQP PQYVAREPPE GTPSDVDMDG SSGTYWPVNS DQAVPELDLG WPLTFGFQGT
     EVTTLVQPPP PDSPSIKDEA RRMIRSAQQV VAVVMDMFTD VDLLSEVLEA AARRVPVYIL
     LDEMNAQHFL DMADKCRVNL HHVDFLRVRT VAGPTYYCRT GKSFKGHLKE KFLLVDCAVV
     MSGSYSFMWS FEKIHRSLAH VFQGELVSSF DEEFRILFAQ SEPLVPSAGA LARMDAYALA
     PYSGAGPLVG VPGVGAPTPF SFPKRAHLLF PPPREEGLGF PSFLDPDRHF LSAFRREELQ
     RMPGGALEPH TGLRPLARPT EAGPFGELAG PRGFFQSRHL EMDAFKRHSY ATPDGAGAVE
     NFAAARQVSR QTFLSHGDDF RFQTSHFQRD QLYQQHYQWD PQFAPARPQG LFEKLRAGRP
     GFADPDDFAL GAGHRFPELG ADVHQRLEYV PSSASREVRH GSDPAFGPSP RGLEPSGASR
     PNLGQRFPCQ ATLRQGLDTA SEAEPERRGG PEGRAGLRHW RLASYLSGCH GDGGEEGLPM
     EAEACEDEVL APGGRDLLPS AFRTPAAFPA KGPKPGSGSG GGDSSEREGP EETSLAKQDS
     FRSRLNPLIQ RSSRLRSSLI FASQAEGAVG TAAATTEKVQ LMHKEQTVSE TLGPSGEAVR
     SSASAKVAEL LEKYKGPARD PGGAGGAVTS SSHSKAVVSQ AWREEVVAPG GAGTERRSLE
     SCLLDLRDSF AQQLHQEAER HPGAASLTAA QLLDTLGGTD RLPSRFLSAQ GRSLSPQGRD
     SPPPEGLGTH QLPYSEPKGN PTPAYPERKG SPTPAYPERK GSPTPAYPER KGSPTPAYPE
     RKGSPTQAYP ERKGSPTSGF PNRRGSPTTG LMEQKGSPTS TYPDRRGSPV PPVPERRGSP
     VPPVPERRGS LTFAGESSKT GPTEEVSSGP MEVLRKGSLR LRQLLSPKNE RRGEDEGSFP
     TPQENGQPES PRRPSLSRGD STEAAAEERG SRVRLASATA NALYSSNLRD DTKAILEQIS
     AHGQKHRGVP APGPAHSSPD VGRPTTAGDL APDMSDKDKC SAIFRSDSLG TQGRLSRTLP
     GSAEERDRLL RRMESMRKEK RVYSRFEVFC KKDEAGSSGA GDNLADEDTR DSKMGKFVPK
     ILGTFKSKK
//
ID   MIPT3_MOUSE             Reviewed;         625 AA.
AC   Q149C2; Q538H5; Q80VQ3; Q9CS98;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   08-MAR-2011, entry version 38.
DE   RecName: Full=TRAF3-interacting protein 1;
DE   AltName: Full=Microtubule-interacting protein associated with TRAF3;
DE            Short=MIP-T3;
GN   Name=Traf3ip1; Synonyms=Mipt3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RA   Ma B., He C., Lee C., Elias J.A.;
RT   "Mus musculus microtubule-interacting protein that associates with
RT   TRAF3.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NMRI; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 142-625.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   SUBUNIT.
RX   PubMed=19253336; DOI=10.1002/cm.20346;
RA   Follit J.A., Xu F., Keady B.T., Pazour G.J.;
RT   "Characterization of mouse IFT complex B.";
RL   Cell Motil. Cytoskeleton 66:457-468(2009).
CC   -!- FUNCTION: Play an inhibitory role on IL13 signaling by binding to
CC       IL13RA1. Involved in suppression of IL13-induced STAT6
CC       phosphorylation, transcriptional activity and DNA-binding.
CC       Recruits TRAF3 and DISC1 to the microtubules (By similarity).
CC   -!- SUBUNIT: Interacts with IL13RA1. Binds to microtubules, TRAF3 and
CC       DISC1 (By similarity). Component of IFT complex B composed of
CC       IFT88, IFT57, TRAF3IP1, IFT52, IFT27, HSPB11 and IFT20.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Microtubules
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the TRAF3IP1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH46538.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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DR   EMBL; AY613437; AAT72918.1; -; mRNA.
DR   EMBL; BC046538; AAH46538.1; ALT_SEQ; mRNA.
DR   EMBL; BC117868; AAI17869.1; -; mRNA.
DR   EMBL; AK014457; BAB29364.1; -; mRNA.
DR   IPI; IPI00340806; -.
DR   RefSeq; NP_082994.1; NM_028718.2.
DR   UniGene; Mm.318430; -.
DR   UniGene; Mm.479296; -.
DR   ProteinModelPortal; Q149C2; -.
DR   SMR; Q149C2; 1-133.
DR   STRING; Q149C2; -.
DR   PhosphoSite; Q149C2; -.
DR   PRIDE; Q149C2; -.
DR   Ensembl; ENSMUST00000047242; ENSMUSP00000042391; ENSMUSG00000034292.
DR   GeneID; 74019; -.
DR   KEGG; mmu:74019; -.
DR   CTD; 74019; -.
DR   MGI; MGI:1921269; Traf3ip1.
DR   eggNOG; roNOG15824; -.
DR   GeneTree; ENSGT00560000077327; -.
DR   HOGENOM; HBG715085; -.
DR   HOVERGEN; HBG101388; -.
DR   InParanoid; Q149C2; -.
DR   OMA; RSKNSVE; -.
DR   OrthoDB; EOG40S0GB; -.
DR   NextBio; 339550; -.
DR   ArrayExpress; Q149C2; -.
DR   Bgee; Q149C2; -.
DR   Genevestigator; Q149C2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   InterPro; IPR018799; Microtubule/TRAF3/DISC1-bd.
DR   Pfam; PF10243; MIP-T3; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein.
FT   CHAIN         1    625       TRAF3-interacting protein 1.
FT                                /FTId=PRO_0000299545.
FT   REGION        1    322       Abolishes microtubules binding when
FT                                missing (By similarity).
FT   REGION      229    625       DISC1-interaction domain (By similarity).
FT   COILED      472    600       Potential.
FT   COMPBIAS    207    296       Arg-rich.
FT   MOD_RES     409    409       Phosphoserine.
FT   CONFLICT     52     52       L -> F (in Ref. 2; AAH46538).
FT   CONFLICT    313    313       R -> K (in Ref. 2; AAI17869).
FT   CONFLICT    371    371       K -> E (in Ref. 3; BAB29364).
SQ   SEQUENCE   625 AA;  71037 MW;  2790471DAE271F7D CRC64;
     MNAAVVRRTQ EALGKVIRRP PLTEKLLNKP PFRYLHDIIT EVIRITGFMK GLYTDAEMKS
     ENVKDKDAKI SFLQKAIDVV MMVSGEPLAA KPARIVAGHE PERTNELLQL IGKCCLSKLS
     SDEAVKRVLA GDKGDSRGRA QRTSKAQEPN NKSGKEEESR IHKEDKRSSE AKERSASAEH
     KQKEELKEDS KPREKERDKE KAKEADRDRH RDPDRDRNRD GEREKARARA KDRDRNNRDR
     DREAERDRER DRRSEGGKEK ERVKDRDRDR DKGRDRERRK SKNGEHTRDP DREKSRDADK
     PEKKSSSSGE ISRKLSDGSF KDVKAEMEAD ISVGASRSST LKPSKRRSKH SLEGDSPSDA
     EVEAGPAGQD KPEVMENAEV PSELPSSLRR IPRPGSARPA PPRVKRQEST ETLVVDRSGS
     GKTVSSVIID SQNSDNEDDE QFVVEAAPQL SEIADIDMVP SGELEDEEKH GGLVKKILET
     KKDYEKLQQS LKPGEKERSL IFESAWKKEK DIVSKEIEKL RVSIQTLCKS ALPLGKIMDY
     IQEDVDAMQN ELQLWHSENR QHAEALSQEQ SITDSAVEPL KAELSELEQQ IRDQQDKICA
     VKANILKNEE KIQKMVHSIN LSSRR
//
ID   PPM1J_MOUSE             Reviewed;         507 AA.
AC   Q149T7; Q810X6; Q9D7H6;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=Protein phosphatase 1J;
DE            EC=3.1.3.16;
DE   AltName: Full=Protein phosphatase 2C isoform zeta;
DE            Short=PP2C-zeta;
GN   Name=Ppm1j; Synonyms=Ppp2cz;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH UBE2I, AND TISSUE
RP   SPECIFICITY.
RX   MEDLINE=22520878; PubMed=12633878; DOI=10.1016/S0014-5793(03)00153-4;
RA   Kashiwaba M., Katsura K., Ohnishi M., Sasaki M., Tanaka H.,
RA   Nishimune Y., Kobayashi T., Tamura S.;
RT   "A novel protein phosphatase 2C family member (PP2Czeta) is able to
RT   associate with ubiquitin conjugating enzyme 9.";
RL   FEBS Lett. 538:197-202(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-507.
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- SUBUNIT: Interacts with UBE2I/UBC9.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in the testicular germ
CC       cells.
CC   -!- SIMILARITY: Belongs to the PP2C family.
CC   -!- SIMILARITY: Contains 1 PP2C-like domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB26156.1; Type=Erroneous initiation;
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DR   EMBL; AY184802; AAO72079.1; -; mRNA.
DR   EMBL; BC117498; AAI17499.1; -; mRNA.
DR   EMBL; BC121788; AAI21789.1; -; mRNA.
DR   EMBL; AK009235; BAB26156.1; ALT_INIT; mRNA.
DR   IPI; IPI00329932; -.
DR   RefSeq; NP_082258.2; NM_027982.2.
DR   UniGene; Mm.379204; -.
DR   ProteinModelPortal; Q149T7; -.
DR   STRING; Q149T7; -.
DR   PhosphoSite; Q149T7; -.
DR   PRIDE; Q149T7; -.
DR   Ensembl; ENSMUST00000002298; ENSMUSP00000002298; ENSMUSG00000002228.
DR   GeneID; 71887; -.
DR   KEGG; mmu:71887; -.
DR   NMPDR; fig|10090.3.peg.8729; -.
DR   UCSC; uc008quk.1; mouse.
DR   CTD; 71887; -.
DR   MGI; MGI:1919137; Ppm1j.
DR   eggNOG; roNOG08095; -.
DR   GeneTree; ENSGT00530000063231; -.
DR   HOGENOM; HBG315163; -.
DR   HOVERGEN; HBG105802; -.
DR   InParanoid; Q149T7; -.
DR   OMA; VCSSTLP; -.
DR   OrthoDB; EOG42JNRC; -.
DR   PhylomeDB; Q149T7; -.
DR   BRENDA; 3.1.3.16; 244.
DR   NextBio; 334852; -.
DR   ArrayExpress; Q149T7; -.
DR   Bgee; Q149T7; -.
DR   CleanEx; MM_PPM1J; -.
DR   Genevestigator; Q149T7; -.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:MGI.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
DR   InterPro; IPR001932; PP2C-like.
DR   InterPro; IPR014045; PP2C_N.
DR   InterPro; IPR015655; Protein_Pase_2C.
DR   Gene3D; G3DSA:3.60.40.10; PP2C-related; 3.
DR   PANTHER; PTHR13832; PP2C; 1.
DR   Pfam; PF00481; PP2C; 2.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-related; 1.
DR   PROSITE; PS01032; PP2C; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Hydrolase; Phosphoprotein; Protein phosphatase.
FT   CHAIN         1    507       Protein phosphatase 1J.
FT                                /FTId=PRO_0000289059.
FT   DOMAIN      119    499       PP2C-like.
FT   MOD_RES      75     75       Phosphoserine (By similarity).
FT   CONFLICT      5      5       V -> A (in Ref. 1; AAO72079).
FT   CONFLICT     61     62       Missing (in Ref. 1; AAO72079).
FT   CONFLICT     78     78       G -> GET (in Ref. 1; AAO72079).
SQ   SEQUENCE   507 AA;  55550 MW;  4754E503AA8A7FE2 CRC64;
     MLNRVRSAVA HLVSSGGTSS QRSKSPDLPN ATSAPPAAQE TPKSSREKPG NQVGAPQKTA
     ETTVSFSRPT FLQLSPGGLR RADDHAGRAV QSPPDTGRRL PWSTGYAEVI NAGKSRHNED
     QACCEVVYVE SRRSRSVTGV SREPSHNQGF CFYYWGLFDG HAGGGAAEMA SRLLHRHIRE
     QLKDLVEILK DPLPPPLCLP STPGTPGAPS PSQLVSPQSC WSPQKEVTHD SLIVGAIENA
     FHLMDEQMAR ERRGHQVEGG CCALVVLYLL GKMYVANAGD SRAIIVRNGE IIPMSREFTP
     ETERQRLQLL GFLKPELLGS EFTHLEFPRR VQPKELGQRM LYRDQNMTGW AYKKIEVEDL
     RFPLVCGEGK KARVMATIGV TRGLGDHNLK VCSSTLSIKP FLSCFPEVRV YDLTQYEHCP
     DDVLVLGTDG LWDVTNDSEV AATVDRVLSS YEPNDPSRYT ALAQALVLGA RGIPRDRGWR
     LPNNKLGSGD DISVFVIPLG GPGSSYS
//
ID   Q14AR7_MOUSE            Unreviewed;       204 AA.
AC   Q14AR7;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   SubName: Full=MCG6726, isoform CRA_f;
DE   SubName: Full=Novel protein (Possible orthologue of human C20orf20);
DE   SubName: Full=RIKEN cDNA 1600027N09 gene;
GN   Name=1600027N09Rik; Synonyms=RP23-74K21.4;
GN   ORFNames=RP23-74K21.4-001, mCG_6726;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Tracey A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC116732; AAI16733.1; -; mRNA.
DR   EMBL; BC116734; AAI16735.1; -; mRNA.
DR   EMBL; AL669926; CAM26815.1; -; Genomic_DNA.
DR   EMBL; CH466626; EDL07342.1; -; Genomic_DNA.
DR   IPI; IPI00720110; -.
DR   RefSeq; NP_082755.1; NM_028479.1.
DR   UniGene; Mm.426558; -.
DR   ProteinModelPortal; Q14AR7; -.
DR   STRING; Q14AR7; -.
DR   PRIDE; Q14AR7; -.
DR   Ensembl; ENSMUST00000029085; ENSMUSP00000029085; ENSMUSG00000027569.
DR   GeneID; 73247; -.
DR   KEGG; mmu:73247; -.
DR   UCSC; uc008ojh.1; mouse.
DR   MGI; MGI:1920497; 1600027N09Rik.
DR   eggNOG; roNOG16380; -.
DR   HOGENOM; HBG278922; -.
DR   HOVERGEN; HBG052509; -.
DR   InParanoid; Q14AR7; -.
DR   OrthoDB; EOG4TF0MG; -.
DR   NextBio; 337754; -.
DR   ArrayExpress; Q14AR7; -.
DR   Bgee; Q14AR7; -.
DR   Genevestigator; Q14AR7; -.
DR   GO; GO:0043189; C:H4/H2A histone acetyltransferase complex; IEA:InterPro.
DR   GO; GO:0045449; P:regulation of transcription; IEA:InterPro.
DR   InterPro; IPR012423; EAF7.
DR   PANTHER; PTHR13581; CT20; 1.
DR   Pfam; PF07904; CT20; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   204 AA;  22436 MW;  3CD4BB2A64C814EA CRC64;
     MGEAEVGGTG APGDKGPGEA APSPAEETVV WSPEVEVCLF HAMLGHKPVG VNRHFHMICI
     RDKFSQNIGR QVPSKVIWDH LSTMYDMQAL HESEILPFPN PERNFVLPDE IIQEVREGKV
     VIEEEMKEEM KEDVDPHSGA DDVFSSSGSL GKALEKSSKD KEKNSSDLGC KEGADKRKRS
     RVTDKVLTAN SNPSSPSAAK RRRT
//
ID   CDK12_MOUSE             Reviewed;        1484 AA.
AC   Q14AX6; A2A530; A2A531; Q6ZQ27;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Cyclin-dependent kinase 12;
DE            EC=2.7.11.22;
DE   AltName: Full=Cdc2-related kinase, arginine/serine-rich;
DE            Short=CrkRS;
DE   AltName: Full=Cell division cycle 2-related protein kinase 7;
DE            Short=CDC2-related protein kinase 7;
DE   AltName: Full=Cell division protein kinase 12;
GN   Name=Cdk12; Synonyms=Crk7, Crkrs, Kiaa0904;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 425-1484 (ISOFORM 3).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-278; TYR-318; SER-322;
RP   SER-324; SER-382; SER-384 AND THR-1071, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273; THR-889 AND
RP   SER-1079, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1079, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382 AND SER-384, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Involved in the regulation of alternative mRNA splicing
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts with CCNL1 and CCNL2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Nucleus speckle (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q14AX6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q14AX6-2; Sequence=VSP_030285, VSP_030287;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q14AX6-3; Sequence=VSP_030286;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. CDC2/CDKX subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AL591205; CAM21267.1; -; Genomic_DNA.
DR   EMBL; AL591205; CAM21268.1; -; Genomic_DNA.
DR   EMBL; AL591205; CAM21269.1; -; Genomic_DNA.
DR   EMBL; BC116645; AAI16646.1; -; mRNA.
DR   EMBL; AK129237; BAC98047.1; -; mRNA.
DR   IPI; IPI00321774; -.
DR   IPI; IPI00648022; -.
DR   IPI; IPI00649269; -.
DR   RefSeq; NP_001103096.1; NM_001109626.1.
DR   RefSeq; NP_001103098.1; NM_001109628.1.
DR   RefSeq; NP_081228.2; NM_026952.2.
DR   UniGene; Mm.260516; -.
DR   ProteinModelPortal; Q14AX6; -.
DR   SMR; Q14AX6; 720-1019.
DR   PhosphoSite; Q14AX6; -.
DR   PRIDE; Q14AX6; -.
DR   Ensembl; ENSMUST00000003203; ENSMUSP00000003203; ENSMUSG00000003119.
DR   Ensembl; ENSMUST00000107538; ENSMUSP00000103162; ENSMUSG00000003119.
DR   GeneID; 69131; -.
DR   KEGG; mmu:69131; -.
DR   NMPDR; fig|10090.3.peg.25190; -.
DR   UCSC; uc007lfs.1; mouse.
DR   CTD; 69131; -.
DR   MGI; MGI:1098802; Cdk12.
DR   HOGENOM; HBG282140; -.
DR   HOVERGEN; HBG050852; -.
DR   InParanoid; Q14AX6; -.
DR   OMA; DSYKKSP; -.
DR   OrthoDB; EOG498V0D; -.
DR   PhylomeDB; Q14AX6; -.
DR   BRENDA; 2.7.11.22; 244.
DR   NextBio; 328674; -.
DR   ArrayExpress; Q14AX6; -.
DR   Bgee; Q14AX6; -.
DR   CleanEx; MM_CRKRS; -.
DR   Genevestigator; Q14AX6; -.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004693; F:cyclin-dependent protein kinase activity; IEA:EC.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Kinase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1   1484       Cyclin-dependent kinase 12.
FT                                /FTId=PRO_0000314470.
FT   DOMAIN      723   1016       Protein kinase.
FT   NP_BIND     729    737       ATP (By similarity).
FT   COMPBIAS    137    393       Ser-rich.
FT   COMPBIAS    406    412       Poly-Ala.
FT   COMPBIAS    524    703       Pro-rich.
FT   COMPBIAS   1234   1276       Pro-rich.
FT   ACT_SITE    855    855       Proton acceptor (By similarity).
FT   BINDING     752    752       ATP (By similarity).
FT   MOD_RES      14     14       Phosphoserine (By similarity).
FT   MOD_RES      24     24       Phosphoserine (By similarity).
FT   MOD_RES      25     25       Phosphoserine (By similarity).
FT   MOD_RES      29     29       Phosphoserine (By similarity).
FT   MOD_RES      32     32       Phosphoserine (By similarity).
FT   MOD_RES      57     57       Phosphothreonine (By similarity).
FT   MOD_RES      62     62       Phosphoserine (By similarity).
FT   MOD_RES      73     73       Phosphotyrosine (By similarity).
FT   MOD_RES      77     77       Phosphoserine (By similarity).
FT   MOD_RES      78     78       Phosphoserine (By similarity).
FT   MOD_RES      80     80       Phosphoserine (By similarity).
FT   MOD_RES      82     82       Phosphothreonine (By similarity).
FT   MOD_RES      84     84       Phosphoserine (By similarity).
FT   MOD_RES     214    214       Phosphoserine (By similarity).
FT   MOD_RES     227    227       Phosphoserine (By similarity).
FT   MOD_RES     235    235       Phosphoserine (By similarity).
FT   MOD_RES     237    237       Phosphoserine (By similarity).
FT   MOD_RES     248    248       Phosphoserine (By similarity).
FT   MOD_RES     264    264       Phosphoserine (By similarity).
FT   MOD_RES     273    273       Phosphoserine.
FT   MOD_RES     275    275       Phosphoserine (By similarity).
FT   MOD_RES     278    278       Phosphotyrosine.
FT   MOD_RES     290    290       Phosphoserine (By similarity).
FT   MOD_RES     292    292       Phosphoserine (By similarity).
FT   MOD_RES     300    300       Phosphoserine (By similarity).
FT   MOD_RES     302    302       Phosphoserine (By similarity).
FT   MOD_RES     317    317       Phosphoserine (By similarity).
FT   MOD_RES     318    318       Phosphotyrosine.
FT   MOD_RES     319    319       Phosphoserine (By similarity).
FT   MOD_RES     322    322       Phosphoserine.
FT   MOD_RES     324    324       Phosphoserine.
FT   MOD_RES     331    331       Phosphoserine (By similarity).
FT   MOD_RES     332    332       Phosphoserine (By similarity).
FT   MOD_RES     333    333       Phosphoserine (By similarity).
FT   MOD_RES     340    340       Phosphoserine (By similarity).
FT   MOD_RES     342    342       Phosphoserine (By similarity).
FT   MOD_RES     344    344       Phosphoserine (By similarity).
FT   MOD_RES     381    381       Phosphoserine (By similarity).
FT   MOD_RES     382    382       Phosphoserine.
FT   MOD_RES     384    384       Phosphoserine.
FT   MOD_RES     392    392       Phosphoserine (By similarity).
FT   MOD_RES     399    399       Phosphoserine (By similarity).
FT   MOD_RES     419    419       Phosphoserine (By similarity).
FT   MOD_RES     422    422       Phosphoserine (By similarity).
FT   MOD_RES     501    501       N6-acetyllysine (By similarity).
FT   MOD_RES     511    511       Phosphothreonine (By similarity).
FT   MOD_RES     677    677       Phosphoserine (By similarity).
FT   MOD_RES     681    681       Phosphoserine (By similarity).
FT   MOD_RES     688    688       Phosphothreonine (By similarity).
FT   MOD_RES     888    888       Phosphotyrosine (By similarity).
FT   MOD_RES     889    889       Phosphothreonine.
FT   MOD_RES    1049   1049       Phosphoserine (By similarity).
FT   MOD_RES    1066   1066       Phosphothreonine (By similarity).
FT   MOD_RES    1070   1070       Phosphothreonine (By similarity).
FT   MOD_RES    1071   1071       Phosphothreonine.
FT   MOD_RES    1079   1079       Phosphoserine.
FT   MOD_RES    1240   1240       Phosphothreonine (By similarity).
FT   VAR_SEQ    1250   1258       ACPPHILPP -> GKQTGHESH (in isoform 2).
FT                                /FTId=VSP_030285.
FT   VAR_SEQ    1250   1258       Missing (in isoform 3).
FT                                /FTId=VSP_030286.
FT   VAR_SEQ    1259   1484       Missing (in isoform 2).
FT                                /FTId=VSP_030287.
FT   CONFLICT    425    427       ILP -> FCL (in Ref. 3; BAC98047).
SQ   SEQUENCE   1484 AA;  163681 MW;  5FCEE8D1903DF803 CRC64;
     MPNSERHGGK KDGSGGASGT SQPSSGGGSS NSRERHRLVS KHKRHKSKHS KDVGLVTPEA
     ASLGTIIKPL VEYDDISSDS DTFSDDTAFK SDRRENEERR GTDRSDRLHR HRHHQHRRSR
     DLLKTKQTEK EKNQEVSKSG SMKDRVSGSS KRSVEGSDDY GKAQLSKSGS KESRSSKMHK
     EKTRKERELK SGYKDRSKSH RKRETPKSYK TVASPKRRSR SPHRKWSDSS KQDDSPSGAS
     YGQDYDLSPP RSHTSSNYDS YKKSPGSTSR RQSISPPYKE PSAYQSSTRS PSPYSRRQRS
     VSPYSRRRSS SYERSGSYSG RSPSPYGRRR SSSPFLSKRS LSRSPLPSRK SMKSRSRSPA
     YSRHSSSHSK KKRSGSRSRH SSISPVRLPL NSSLGAELSR KKKERAAAAA AAKMDGKESK
     SSPIILPKKE KLEVKESGLE SKKLPRSIKS EKSTPDTELV TVAHSNPEVK HCLDTGKVRL
     DENLQKHPAK DLKAQGTKDV KPVAPKEVIV TSKETETSEK ETLPPLPTIT SPPPLPATTP
     PPQTPPLPPL PPLPAIPLQP PLPPPQPPFS QVPVSSTSIL PSSPHPRTST LSSQTNSQPP
     VQVSMKTQVS ITAAIPHLKT STLPPLPLPP LLPGDDDMDS PKETLPSKPA KKEKEQRTRH
     LLTDLPLPPE LPGGDPSPPD SPEPKAITPP QQPYKKRPKI CCPRYGERRQ TESDWGKRCV
     DKFDIIGIIG EGTYGQVYKA KDKDTGELVA LKKVRLDNEK EGFPITAIRE IKILRQLVHQ
     SVVNMKEIVT DKQDALDFKK DKGAFYLVFE YMDHDLMGLL ESGLVHFSED HIKSFMKQLM
     EGLDYCHKKN FLHRDIKCSN ILLNNSGQIK LADFGLARLY NSEESRPYTN KVITLWYRPP
     ELLLGEERYT PAIDVWSCGC ILGELFTKKP IFQANLELAQ LELISRLCGS PCPAVWPDVI
     KLPYFNTMKP KKQYRRRLRE EFSFIPSAAL DLLDHMLTLD PSKRCTAEQT LQSDFLKDVE
     LSKMAPPDLP HWQDCHELWS KKRRRQRQSG IVIEDPPPSK ASRKETTSGT TAEPVKNNSP
     APPQPAPVKA EPGPGDAVGL GDITQQLNQS ELAVLLNLLQ SQTDLSIPQM AQLLNIHSNP
     EMQQQLEALN QSISALTEAS SQQQDSESIA PEESLKEVPS VPVVLPPAEQ TTPEASNTPA
     DMQNVLAVLL SQLMKTQEPA GNLEENTNDK NSGPQGPRRT PTMPQEEAAA CPPHILPPEK
     RPPEPPGPPP PPPPPPLVEG DLSSAPQELN PAVTAALLQL LSQPEAEPPG HLPHEHQALR
     PMEYSTRSHP NRTYGNTDGP ETGFSSADTD ERSSGPALTE SLVQTPVKNR TFSGSVSHLG
     ESNSYQGTGS VQFPGDQDLR FTRVPLALHS VVGQPFLKSE GNSNSVVHAE TKLQNYGELG
     PGTTGANSSG TTLQWGGPAQ SYGKPYRGAA RVLPRGGRGR GVPY
//
ID   Q14AY1_MOUSE            Unreviewed;       649 AA.
AC   Q14AY1;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-FEB-2011, entry version 26.
DE   SubName: Full=Slc24a2 protein;
GN   Name=Slc24a2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC116637; AAI16638.1; -; mRNA.
DR   IPI; IPI00648345; -.
DR   UniGene; Mm.127296; -.
DR   Ensembl; ENSMUST00000107155; ENSMUSP00000102773; ENSMUSG00000037996.
DR   UCSC; uc008tmi.1; mouse.
DR   MGI; MGI:1923626; Slc24a2.
DR   GeneTree; ENSGT00560000076876; -.
DR   HOVERGEN; HBG054881; -.
DR   PhylomeDB; Q14AY1; -.
DR   ArrayExpress; Q14AY1; -.
DR   Bgee; Q14AY1; -.
DR   Genevestigator; Q14AY1; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005262; F:calcium channel activity; IDA:MGI.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
DR   GO; GO:0007612; P:learning; IMP:MGI.
DR   GO; GO:0060292; P:long term synaptic depression; IMP:MGI.
DR   GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
DR   GO; GO:0007613; P:memory; IMP:MGI.
DR   InterPro; IPR004481; K-dep_Na/Ca-exchanger-like.
DR   InterPro; IPR004837; NaCa_Exmemb.
DR   Pfam; PF01699; Na_Ca_ex; 2.
DR   TIGRFAMs; TIGR00367; K_NaCaexchng; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
SQ   SEQUENCE   649 AA;  72232 MW;  1EE3B7737103A489 CRC64;
     MDLHQSPTAR LLQKWCSHES PFGCRRHYNS RKKLKLIRVI GLVMGLVAVS TVPFSISAFT
     ETDSQSNRGE ASDMSGPRVA QGHRQRTLLD LNDKIRDYTP QPPASQEDQA ENSTEHTQGD
     YPKDIFSLEE RRKGAIILHV IGMIYMFIAL AIVCDEFFVP SLTVITEKLG ISDDVAGATF
     MAAGGSAPEL FTSLIGVFIA HSNVGIGTIV GSAVFNILFV IGMCALFSRE ILNLTWWPLF
     RDVSFYIVDL LMLITFFLDN VIMWWESLLL LTAYFAYVVF MKFNVQVERW VKQMISRNNV
     IKVTVPEAQA KSPTAGDKDG PTLPSKPRLQ RGGSSASLHN SLMRNSIFQL MIHTLDPLAE
     GRFREKASIL HKIAKKKCQV DENERQNGAA NHVEKIELPN STSTEVEMTP SSEASEPVQN
     GNLSHNIEAA DAPKATETAE EEDDQPLSLS WPTNTRKQAT FLIVFPIVFP LWITLPDVRK
     PASRKFFPIT FFGSITWIAV FSYLMVWWAH QVGETIGISE EIMGLTILAA GTSIPDLITS
     VIVARKGLGD MAVSSSVGSN IFDITVGLPL PWLLYTIIHR FSPVTVSSNG LFCAIVLLFI
     MLLFVILSIA LCKWRMNKIL GFIMFGLYFV FLVVSVLLED KVLVCPVSI
//
ID   Q14B01_MOUSE            Unreviewed;       337 AA.
AC   Q14B01;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAR-2011, entry version 40.
DE   SubName: Full=Ring finger protein 113A2;
GN   Name=Rnf113a2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
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DR   EMBL; BC116426; AAI16427.1; -; mRNA.
DR   IPI; IPI00110093; -.
DR   RefSeq; NP_079801.2; NM_025525.2.
DR   UniGene; Mm.24846; -.
DR   ProteinModelPortal; Q14B01; -.
DR   SMR; Q14B01; 258-325.
DR   GeneID; 66381; -.
DR   KEGG; mmu:66381; -.
DR   UCSC; uc007ofj.1; mouse.
DR   CTD; 66381; -.
DR   MGI; MGI:1913631; Rnf113a2.
DR   HOVERGEN; HBG060697; -.
DR   NextBio; 321505; -.
DR   Genevestigator; Q14B01; -.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Zinc; Zinc-finger.
SQ   SEQUENCE   337 AA;  38059 MW;  44EAEE377E22D229 CRC64;
     MAEQVSQGKS EDQVCTFLFK KPGRKGSAGR RKRPACDPES GESGSSSDEG CSVVRPEKKR
     AAHNPMIQKT SGSGKQKGAY CDLSSEEEEK AGNESLGVVY KSTRSAKPVG PEDMGATAVY
     ELDTEKERDA QAIFERSQKI QEELRGKEDD KIYRGINNYQ KYMKPKDTSM GNASSGMVRK
     GPIRAPEHLR ATVRWDYQPD ICKDYKETGF CGFGDSCKFL HDRSDYKHGW QIERELDEGR
     YGVYEDENYE VESDDEEIPF KCFICRQTFQ NPVVTKCKHY FCETCALQHF RTTPRCYVCE
     QQTHGVFNPA KELIAKLEKY RKAEGGASST PEDADGI
//
ID   KCNC2_MOUSE             Reviewed;         642 AA.
AC   Q14B80;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   RecName: Full=Potassium voltage-gated channel subfamily C member 2;
DE   AltName: Full=Voltage-gated potassium channel Kv3.2;
GN   Name=Kcnc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INTERACTION WITH KCNC1, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=12000114; DOI=10.1002/hipo.1104;
RA   Tansey E.P., Chow A., Rudy B., McBain C.J.;
RT   "Developmental expression of potassium-channel subunit Kv3.2 within
RT   subpopulations of mouse hippocampal inhibitory interneurons.";
RL   Hippocampus 12:137-148(2002).
RN   [3]
RP   FUNCTION.
RX   PubMed=17761775; DOI=10.1113/jphysiol.2007.141135;
RA   Kasten M.R., Rudy B., Anderson M.P.;
RT   "Differential regulation of action potential firing in adult murine
RT   thalamocortical neurons by Kv3.2, Kv1, and SK potassium and N-type
RT   calcium channels.";
RL   J. Physiol. (Lond.) 584:565-582(2007).
CC   -!- FUNCTION: Mediates the voltage-dependent potassium ion
CC       permeability of excitable membranes. Assuming opened or closed
CC       conformations in response to the voltage difference across the
CC       membrane, the protein forms a potassium-selective channel through
CC       which potassium ions may pass in accordance with their
CC       electrochemical gradient. Channel properties are modulated by
CC       subunit assembly.
CC   -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC       heterotetrameric complex of pore-forming subunits that can
CC       associate with modulating accessory subunits. Interacts with
CC       KCNC1, KCNE1, KCNE2 and KCNE3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Detected in hippocampus.
CC   -!- DEVELOPMENTAL STAGE: Not detectable in hippocampus from newborns.
CC       Detected at low levels in developing hippocampus from day 7 to 12.
CC       Levels are much increased after 14 days. Expressed at high and
CC       stable levels in hippocampus after 21 days (at protein level).
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position.
CC   -!- DOMAIN: The tail may be important in modulation of channel
CC       activity and/or targeting of the channel to specific subcellular
CC       compartments.
CC   -!- SIMILARITY: Belongs to the potassium channel family. C (Shaw)
CC       (TC 1.A.1.2) subfamily. Kv3.2/KCNC2 sub-subfamily.
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DR   EMBL; BC116289; AAI16290.1; -; mRNA.
DR   EMBL; BC116290; AAI16291.1; -; mRNA.
DR   IPI; IPI00457867; -.
DR   UniGene; Mm.336242; -.
DR   ProteinModelPortal; Q14B80; -.
DR   SMR; Q14B80; 4-485.
DR   STRING; Q14B80; -.
DR   PRIDE; Q14B80; -.
DR   Ensembl; ENSMUST00000092175; ENSMUSP00000089814; ENSMUSG00000035681.
DR   UCSC; uc007hao.1; mouse.
DR   MGI; MGI:96668; Kcnc2.
DR   GeneTree; ENSGT00580000081499; -.
DR   HOGENOM; HBG445693; -.
DR   HOVERGEN; HBG105862; -.
DR   InParanoid; Q14B80; -.
DR   OrthoDB; EOG4JQ3X8; -.
DR   ArrayExpress; Q14B80; -.
DR   Bgee; Q14B80; -.
DR   Genevestigator; Q14B80; -.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003974; K_chnl_volt-dep_Kv3.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 2.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02214; K_tetra; 2.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01498; SHAWCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Ion transport; Ionic channel; Membrane; Potassium;
KW   Potassium channel; Potassium transport; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    642       Potassium voltage-gated channel subfamily
FT                                C member 2.
FT                                /FTId=PRO_0000310417.
FT   TOPO_DOM      1    233       Cytoplasmic (Potential).
FT   TRANSMEM    234    254       Helical; Name=Segment S1; (Potential).
FT   TRANSMEM    287    307       Helical; Name=Segment S2; (Potential).
FT   TOPO_DOM    308    317       Cytoplasmic (Potential).
FT   TRANSMEM    318    338       Helical; Name=Segment S3; (Potential).
FT   TRANSMEM    350    372       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TOPO_DOM    373    385       Cytoplasmic (Potential).
FT   TRANSMEM    386    406       Helical; Name=Segment S5; (Potential).
FT   TRANSMEM    457    477       Helical; Name=Segment S6; (Potential).
FT   TOPO_DOM    478    642       Cytoplasmic (Potential).
FT   MOTIF       441    446       Selectivity filter (By similarity).
FT   COMPBIAS     56    103       Gly/Pro-rich (insert).
FT   CARBOHYD    263    263       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    270    270       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   642 AA;  70503 MW;  2B9B6D29A40A80E3 CRC64;
     MGKIESNERV ILNVGGTRHE TYRSTLKTLP GTRLALLASS EPQGDCLTAA GDKLQPLPPP
     LSPPPRPPPL SPVPSGCFEG GAGNCSSHGG NGGNGGSDHP GGGREFFFDR HPGVFAYVLN
     YYRTGKLHCP ADVCGPLFEE ELAFWGIDET DVEPCCWMTY RQHRDAEEAL DIFETPDLIG
     GDPGDDEDLA AKRLGIEDAA GLGGPDGKSG RWRKLQPRMW ALFEDPYSSR AARFIAFASL
     FFILVSITTF CLETHEAFNI VKNKTEPVIN GTSPVLQYEI ETDPALTYVE GVCVVWFTFE
     FLVRIVFSPN KLEFIKNLLN IIDFVAILPF YLEVGLSGLS SKAAKDVLGF LRVVRFVRIL
     RIFKLTRHFV GLRVLGHTLR ASTNEFLLLI IFLALGVLIF ATMIYYAERV GAQPNDPSAS
     EHTQFKNIPI GFWWAVVTMT TLGYGDMYPQ TWSGMLVGAL CALAGVLTIA MPVPVIVNNF
     GMYYSLAMAK QKLPRKRKKH IPPAPLASSP TFCKTELNMA CNSTQSDTCL GKENRLLEHN
     RSVLSGDDST GSEPPLSPPE RLPIRRSSTR DKNRRGETCF LLTTGDYTCA SDGGIRKGYE
     KSRSLNNIAG LAGNALRLSP VTSPYNSPCP LRRSRSPIPS IL
//
ID   MA6D1_MOUSE             Reviewed;         191 AA.
AC   Q14BB9; Q3TQE2; Q8C540;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   RecName: Full=MAP6 domain-containing protein 1;
DE   AltName: Full=21 kDa STOP-like protein;
DE            Short=SL21;
GN   Name=Map6d1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP   CALMODULIN.
RX   PubMed=16837464; DOI=10.1074/jbc.M603380200;
RA   Gory-Faure S., Windscheid V., Bosc C., Peris L., Proietto D.,
RA   Franck R., Denarier E., Job D., Andrieux A.;
RT   "STOP-like protein 21 is a novel member of the STOP family, revealing
RT   a Golgi localization of STOP proteins.";
RL   J. Biol. Chem. 281:28387-28396(2006).
CC   -!- FUNCTION: May have microtubule-stabilizing activity.
CC   -!- SUBUNIT: Interacts with calmodulin.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasm, cytoskeleton.
CC       Note=According to PubMed:16837464, it colocalizes with
CC       microtubules.
CC   -!- TISSUE SPECIFICITY: Expressed in brain. Found in neurons in
CC       primary cultures, but absent in glial cells.
CC   -!- PTM: Palmitoylated. Palmitoylation enhances association with
CC       microtubules (By similarity).
CC   -!- SIMILARITY: Belongs to the STOP family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC37698.1; Type=Frameshift; Positions=158, 183;
CC       Sequence=BAE37442.1; Type=Erroneous initiation;
CC       Sequence=BAE37442.1; Type=Frameshift; Positions=185;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK163656; BAE37442.1; ALT_INIT; mRNA.
DR   EMBL; AK079603; BAC37698.1; ALT_FRAME; mRNA.
DR   EMBL; BC116220; AAI16221.1; -; mRNA.
DR   EMBL; BC116221; AAI16222.1; -; mRNA.
DR   IPI; IPI00816921; -.
DR   RefSeq; NP_941001.2; NM_198599.2.
DR   UniGene; Mm.326383; -.
DR   PRIDE; Q14BB9; -.
DR   Ensembl; ENSMUST00000040880; ENSMUSP00000043332; ENSMUSG00000041205.
DR   GeneID; 208158; -.
DR   KEGG; mmu:208158; -.
DR   UCSC; uc007ypk.1; mouse.
DR   CTD; 208158; -.
DR   MGI; MGI:3607784; Map6d1.
DR   eggNOG; roNOG17300; -.
DR   GeneTree; ENSGT00530000063947; -.
DR   HOGENOM; HBG282495; -.
DR   HOVERGEN; HBG081946; -.
DR   InParanoid; Q14BB9; -.
DR   OMA; CCLARRW; -.
DR   OrthoDB; EOG4TMR37; -.
DR   NextBio; 372182; -.
DR   ArrayExpress; Q14BB9; -.
DR   Bgee; Q14BB9; -.
DR   CleanEx; MM_MAP6D1; -.
DR   Genevestigator; Q14BB9; -.
DR   GO; GO:0005801; C:cis-Golgi network; IDA:MGI.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005798; C:Golgi-associated vesicle; IDA:MGI.
DR   GO; GO:0005516; F:calmodulin binding; IPI:MGI.
DR   GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR   GO; GO:0018009; P:N-terminal peptidyl-L-cysteine N-palmitoylation; IDA:MGI.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:MGI.
DR   InterPro; IPR007882; STOP.
DR   PANTHER; PTHR14759; STOP; 1.
DR   Pfam; PF05217; STOP; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Golgi apparatus; Lipoprotein; Palmitate.
FT   CHAIN         1    191       MAP6 domain-containing protein 1.
FT                                /FTId=PRO_0000271916.
FT   LIPID         5      5       S-palmitoyl cysteine (By similarity).
FT   LIPID        10     10       S-palmitoyl cysteine (By similarity).
FT   LIPID        11     11       S-palmitoyl cysteine (By similarity).
FT   CONFLICT     24     24       V -> F (in Ref. 1; BAC37698).
SQ   SEQUENCE   191 AA;  20433 MW;  4B1186314324BD3A CRC64;
     MAWPCISRLC CLARRWNQLD RSDVAVPLTL HGYSDPGSEE SGADCSVSRG NPSVAGARES
     SRAVPLTQYQ RDFGVRTARA GSRDAAQERP SGPGGRRGQS SAPPTRTVYV LPVGDADAAV
     VATTSYRQEF QAWTGVKPSR STKARTARVV TTHSSGWDPS PGASFQVPEV RKFTPNPSAI
     FQTSAPQTLN V
//
ID   Q14BI1_MOUSE            Unreviewed;       711 AA.
AC   Q14BI1;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   11-JAN-2011, entry version 34.
DE   SubName: Full=Slc24a2 protein;
GN   Name=Slc24a2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
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DR   EMBL; BC115867; AAI15868.1; -; mRNA.
DR   IPI; IPI00775867; -.
DR   RefSeq; NP_001103710.1; NM_001110240.1.
DR   UniGene; Mm.127296; -.
DR   PRIDE; Q14BI1; -.
DR   Ensembl; ENSMUST00000107158; ENSMUSP00000102776; ENSMUSG00000037996.
DR   GeneID; 76376; -.
DR   KEGG; mmu:76376; -.
DR   UCSC; uc008tmj.1; mouse.
DR   CTD; 76376; -.
DR   MGI; MGI:1923626; Slc24a2.
DR   HOGENOM; HBG444187; -.
DR   HOVERGEN; HBG054881; -.
DR   InParanoid; Q14BI1; -.
DR   OMA; DLNDKIR; -.
DR   NextBio; 344997; -.
DR   ArrayExpress; Q14BI1; -.
DR   Bgee; Q14BI1; -.
DR   Genevestigator; Q14BI1; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005262; F:calcium channel activity; IDA:MGI.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
DR   GO; GO:0007612; P:learning; IMP:MGI.
DR   GO; GO:0060292; P:long term synaptic depression; IMP:MGI.
DR   GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
DR   GO; GO:0007613; P:memory; IMP:MGI.
DR   InterPro; IPR004481; K-dep_Na/Ca-exchanger-like.
DR   InterPro; IPR004837; NaCa_Exmemb.
DR   Pfam; PF01699; Na_Ca_ex; 2.
DR   TIGRFAMs; TIGR00367; K_NaCaexchng; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
SQ   SEQUENCE   711 AA;  78977 MW;  650D0AD1D02C524D CRC64;
     MDLHQSPTAR LLQKWCSHES PFGCRRHYNS RKKLKLIRVI GLVMGLVAVS TVPFSISAFT
     ETDSQSNRGE ASDMSGPRVA QGHRQRTLLD LNDKIRDYTP QPPASQEDQA ENSTEHTQGD
     YPKDIFSLEE RRKGAIILHV IGMIYMFIAL AIVCDEFFVP SLTVITEKLG ISDDVAGATF
     MAAGGSAPEL FTSLIGVFIA HSNVGIGTIV GSAVFNILFV IGMCALFSRE ILNLTWWPLF
     RDVSFYIVDL LMLITFFLDN VIMWWESLLL LTAYFAYVVF MKFNVQVERW VKQMISRNNV
     IKVTVPEAQA KLSEFPPASQ ADGRTACPTI TNDPDCQSLC FEVYPETARH GSCITNVNGE
     PLKEKTQNSC MEESPTAGDK DGPTLPSKPR LQRGGSSASL HNSLMRNSIF QLMIHTLDPL
     AEGRFREKAS ILHKIAKKKC QVDENERQNG AANHVEKIEL PNSTSTEVEM TPSSEASEPV
     QNGNLSHNIE AADAPKATET AEEEDDQPLS LSWPTNTRKQ ATFLIVFPIV FPLWITLPDV
     RKPASRKFFP ITFFGSITWI AVFSYLMVWW AHQVGETIGI SEEIMGLTIL AAGTSIPDLI
     TSVIVARKGL GDMAVSSSVG SNIFDITVGL PLPWLLYTII HRFSPVTVSS NGLFCAIVLL
     FIMLLFVILS IALCKWRMNK ILGFIMFGLY FVFLVVSVLL EDKVLVCPVS I
//
ID   GRM2_MOUSE              Reviewed;         872 AA.
AC   Q14BI2;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   08-MAR-2011, entry version 39.
DE   RecName: Full=Metabotropic glutamate receptor 2;
DE            Short=mGluR2;
DE   Flags: Precursor;
GN   Name=Grm2; Synonyms=Gprc1b, Mglur2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-470.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Receptor for glutamate. The activity of this receptor is
CC       mediated by a G-protein that inhibits adenylate cyclase activity.
CC       May mediate suppression of neurotransmission or may be involved in
CC       synaptogenesis or synaptic stabilization (By similarity).
CC   -!- SUBUNIT: Interacts with GRASP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC152452; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC115866; AAI15867.1; -; mRNA.
DR   IPI; IPI00762862; -.
DR   RefSeq; NP_001153825.1; NM_001160353.1.
DR   UniGene; Mm.410822; -.
DR   UniGene; Mm.424639; -.
DR   ProteinModelPortal; Q14BI2; -.
DR   SMR; Q14BI2; 23-558.
DR   MINT; MINT-6594401; -.
DR   PRIDE; Q14BI2; -.
DR   Ensembl; ENSMUST00000023959; ENSMUSP00000023959; ENSMUSG00000023192.
DR   GeneID; 108068; -.
DR   KEGG; mmu:108068; -.
DR   UCSC; uc009rkj.1; mouse.
DR   CTD; 108068; -.
DR   MGI; MGI:1351339; Grm2.
DR   eggNOG; maNOG06995; -.
DR   GeneTree; ENSGT00580000081222; -.
DR   HOVERGEN; HBG107965; -.
DR   ArrayExpress; Q14BI2; -.
DR   Bgee; Q14BI2; -.
DR   CleanEx; MM_GRM2; -.
DR   Genevestigator; Q14BI2; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005246; F:calcium channel regulator activity; IDA:MGI.
DR   GO; GO:0001641; F:group II metabotropic glutamate receptor activity; IDA:MGI.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR000337; GPCR_3.
DR   InterPro; IPR011500; GPCR_3_9-Cys_dom.
DR   InterPro; IPR017978; GPCR_3_C.
DR   InterPro; IPR017979; GPCR_3_CS.
DR   InterPro; IPR000162; GPCR_3_mtglu_rcpt.
DR   InterPro; IPR001458; GPCR_3_mtglu_rcpt_2.
DR   Pfam; PF00003; 7tm_3; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF07562; NCD3G; 1.
DR   PRINTS; PR00248; GPCRMGR.
DR   PRINTS; PR01052; MTABOTROPC2R.
DR   PRINTS; PR00593; MTABOTROPICR.
DR   PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; 1.
DR   PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; 1.
DR   PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
DR   PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Receptor; Signal; Transducer; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     18       Potential.
FT   CHAIN        19    872       Metabotropic glutamate receptor 2.
FT                                /FTId=PRO_0000306249.
FT   TOPO_DOM     19    568       Extracellular (Potential).
FT   TRANSMEM    569    589       Helical; Name=1; (Potential).
FT   TOPO_DOM    590    604       Cytoplasmic (Potential).
FT   TRANSMEM    605    625       Helical; Name=2; (Potential).
FT   TOPO_DOM    626    633       Extracellular (Potential).
FT   TRANSMEM    634    651       Helical; Name=3; (Potential).
FT   TOPO_DOM    652    679       Cytoplasmic (Potential).
FT   TRANSMEM    680    700       Helical; Name=4; (Potential).
FT   TOPO_DOM    701    726       Extracellular (Potential).
FT   TRANSMEM    727    747       Helical; Name=5; (Potential).
FT   TOPO_DOM    748    760       Cytoplasmic (Potential).
FT   TRANSMEM    761    781       Helical; Name=6; (Potential).
FT   TOPO_DOM    782    798       Extracellular (Potential).
FT   TRANSMEM    799    819       Helical; Name=7; (Potential).
FT   TOPO_DOM    820    872       Cytoplasmic (Potential).
FT   CARBOHYD    203    203       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    286    286       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    338    338       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    402    402       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    547    547       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   872 AA;  95887 MW;  FE1726B0684E256D CRC64;
     MESLLRFLAL LLLRGAVAEG PAKKVLTLEG DLVLGGLFPV HQKGGPAEEC GPVNEHRGIQ
     RLEAMLFALD RINRDPHLLP GVRLGAHILD SCSKDTHALE QALDFVRASL SRGADGSRHI
     CPDGSYATLS DAPTAITGVI GGSYSDVSIQ VANLLRLFQI PQISYASTSA KLSDKSRYDY
     FARTVPPDFF QAKAMAEILR FFNWTYVSTV ASEGDYGETG IEAFELEARA RNICVATSEK
     VGRAMSRAAF EGVVRALLQK PSARVAVLFT RSEDARELLA ATQRLNASFT WVASDGWGAL
     ESVVAGSERA AEGAITIELA SYPISDFASY FQNLDPWNNS RNPWFREFWE ERFRCSFRQR
     DCAAHSLRAV PFEQESKIMF VVNAVYAMAH ALHNMHRALC PNTTRLCDAM RPVNGRRLYK
     DFVLNVKFDA PFRPADTDDE VRFDRFGDGI GRYNIFTYLR AGNGRYRYQK VGYWAEGLTL
     DTSIIPWASP SAGTLPASRC SEPCLQNEVK SVQPGEVCCW LCIPCQPYEY RLDEFTCADC
     GLGYWPNASL TGCFELPQEY IRWGDAWAVG PVTIACLGAL ATLFVLGVFV RHNATPVVKA
     SGRELCYILL GGVFLCYCMT FIFIAKPSTA VCTLRRLGLG TAFSVCYSAL LTKTNRIARI
     FGGAREGAQR PRFISPASQV AICLALISGQ LLIVAAWLVV EAPGIGKETA PERREVVTLR
     CNHRDASMLG SLAYNVLLIA LCTLYAFKTR KCPENFNEAK FIGFTMYTTC IIWLAFLPIF
     YVTSSDYRVQ TTTMCVSVSL SGSVVLGCLF APKLHIILFQ PQKNVVSHRA PTSRFGSAAP
     RASANLGQGS GSQLVPTVCN GREVVDSTTS SL
//
ID   TDRD9_MOUSE             Reviewed;        1383 AA.
AC   Q14BI7; B1Q3J8; Q14AW6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 3.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=Putative ATP-dependent RNA helicase TDRD9;
DE            EC=3.6.4.13;
DE   AltName: Full=Tudor domain-containing protein 9;
GN   Name=Tdrd9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RA   Shoji M., Tanaka T., Kitamura K., Hosokawa M., Kato Y., Kondoh G.,
RA   Okawa K., Sasaki H., Chuma S., Nakatsuji N.;
RT   "Regulation of retroelement expression and genome dna methylation
RT   through conserved TDRD9/SPN-E function in the germline.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE
RP   SPECIFICITY, AND INTERACTION WITH PIWIL4.
RX   PubMed=20059948; DOI=10.1016/j.devcel.2009.10.012;
RA   Shoji M., Tanaka T., Hosokawa M., Reuter M., Stark A., Kato Y.,
RA   Kondoh G., Okawa K., Chujo T., Suzuki T., Hata K., Martin S.L.,
RA   Noce T., Kuramochi-Miyagawa S., Nakano T., Sasaki H., Pillai R.S.,
RA   Nakatsuji N., Chuma S.;
RT   "The TDRD9-MIWI2 complex is essential for piRNA-mediated
RT   retrotransposon silencing in the mouse male germline.";
RL   Dev. Cell 17:775-787(2009).
RN   [5]
RP   INTERACTION WITH PIWIL1 AND PIWIL4.
RX   PubMed=19584108; DOI=10.1101/gad.1814809;
RA   Vagin V.V., Wohlschlegel J., Qu J., Jonsson Z., Huang X., Chuma S.,
RA   Girard A., Sachidanandam R., Hannon G.J., Aravin A.A.;
RT   "Proteomic analysis of murine Piwi proteins reveals a role for
RT   arginine methylation in specifying interaction with Tudor family
RT   members.";
RL   Genes Dev. 23:1749-1762(2009).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=20011505; DOI=10.1371/journal.pgen.1000764;
RA   Aravin A.A., van der Heijden G.W., Castaneda J., Vagin V.V.,
RA   Hannon G.J., Bortvin A.;
RT   "Cytoplasmic compartmentalization of the fetal piRNA pathway in
RT   mice.";
RL   PLoS Genet. 5:E1000764-E1000764(2009).
CC   -!- FUNCTION: Probable ATP-binding RNA helicase which plays a central
CC       role during spermatogenesis by repressing transposable elements
CC       and prevent their mobilization, which is essential for the
CC       germline integrity. Acts via the piRNA metabolic process, which
CC       mediates the repression of transposable elements during meiosis by
CC       forming complexes composed of piRNAs and Piwi proteins and govern
CC       the methylation and subsequent repression of transposons. Its
CC       association with PIWIL4 and the piP-bodies suggests a
CC       participation in the secondary piRNAs metabolic process.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Interacts with piRNA-associated proteins PIWIL1 and
CC       PIWIL4.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Component of the
CC       nuage, also named P granule, a germ-cell-specific organelle
CC       required to repress transposon during meiosis. Specifically
CC       localizes to piP-bodies, a subset of the nuage which contains
CC       secondary piRNAs. PIWIL2 is required for its localization to piP-
CC       bodies.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q14BI7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q14BI7-2; Sequence=VSP_033554;
CC       Name=3;
CC         IsoId=Q14BI7-3; Sequence=VSP_033553, VSP_033555;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in reproductive
CC       organs. Detected in mitotic spermatogonia, meiotic spermatocytes
CC       (predominantly at the pachytene stage), haploid spermatids in the
CC       testis, and in growing oocytes in the ovary (at protein level).
CC   -!- DISRUPTION PHENOTYPE: Mice are viable but show male sterility with
CC       chromosome synapsis failure. In fetal testes, LINE-1 (L1)
CC       transposable elements derepression and an aberrant piRNA profile
CC       in prospermatogonia, followed by cognate DNA demethylation are
CC       observed.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 Tudor domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB362563; BAG15992.1; -; mRNA.
DR   EMBL; AC112520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC132623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC115831; AAI15832.1; -; mRNA.
DR   EMBL; BC116656; AAI16657.1; -; mRNA.
DR   IPI; IPI00749982; -.
DR   IPI; IPI00849630; -.
DR   IPI; IPI00914159; -.
DR   RefSeq; NP_083332.1; NM_029056.1.
DR   UniGene; Mm.60648; -.
DR   ProteinModelPortal; Q14BI7; -.
DR   SMR; Q14BI7; 119-788, 922-1021.
DR   STRING; Q14BI7; -.
DR   PRIDE; Q14BI7; -.
DR   Ensembl; ENSMUST00000079009; ENSMUSP00000078022; ENSMUSG00000054003.
DR   Ensembl; ENSMUST00000109765; ENSMUSP00000105387; ENSMUSG00000054003.
DR   GeneID; 74691; -.
DR   KEGG; mmu:74691; -.
DR   UCSC; uc007pei.1; mouse.
DR   CTD; 74691; -.
DR   MGI; MGI:1921941; Tdrd9.
DR   eggNOG; roNOG05137; -.
DR   GeneTree; ENSGT00550000074257; -.
DR   InParanoid; Q14BI7; -.
DR   OMA; ETSLMPP; -.
DR   OrthoDB; EOG4F4S96; -.
DR   NextBio; 341402; -.
DR   ArrayExpress; Q14BI7; -.
DR   Bgee; Q14BI7; -.
DR   Genevestigator; Q14BI7; -.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0071547; C:piP-body; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0043046; P:DNA methylation involved in gamete generation; IMP:UniProtKB.
DR   GO; GO:0009566; P:fertilization; IMP:UniProtKB.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0007140; P:male meiosis; IMP:UniProtKB.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0034587; P:piRNA metabolic process; IMP:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR008191; Maternal_tudor.
DR   InterPro; IPR002999; Tudor.
DR   InterPro; IPR018351; Tudor_subgroup.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00567; TUDOR; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00333; TUDOR; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50304; TUDOR; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Developmental protein;
KW   Differentiation; Helicase; Hydrolase; Meiosis; Nucleotide-binding;
KW   Nucleus; RNA-mediated gene silencing; Spermatogenesis.
FT   CHAIN         1   1383       Putative ATP-dependent RNA helicase
FT                                TDRD9.
FT                                /FTId=PRO_0000333814.
FT   DOMAIN      144    310       Helicase ATP-binding.
FT   DOMAIN      378    545       Helicase C-terminal.
FT   DOMAIN      945   1005       Tudor.
FT   NP_BIND     157    164       ATP (By similarity).
FT   MOTIF       256    259       DEAH box.
FT   VAR_SEQ       1    772       Missing (in isoform 3).
FT                                /FTId=VSP_033553.
FT   VAR_SEQ       1    401       Missing (in isoform 2).
FT                                /FTId=VSP_033554.
FT   VAR_SEQ     773    813       PKTTVVLKHIPPYGFLYYKQLQSLFRQCGQVKSIVFDGAKA
FT                                -> MDIGTKCTSQVAAGVTAWHLWRRSGPGRLADSEESCGV
FT                                PRA (in isoform 3).
FT                                /FTId=VSP_033555.
SQ   SEQUENCE   1383 AA;  155980 MW;  55946F4F639B5777 CRC64;
     MLRKLTVDQI NDWFTIGKTV TNVELLGLPP AFPAEAPREE VQRSEEVPNE DPTAQAQVPV
     KATAPARPAS TSGRSLSQRS SEMEYINKYR QLEEQELDIY GQDQPPSGPG LRSPLAKLSN
     VACIPETTYK YPDLPINRCK EEVISLIESN SVVIIHGATG SGKSTQLPQY VLDHYTQRSA
     FCNIVVTQPR KIGASSIARW ISKERSWTLG GLVGYQVGLE KIATEDTRLI YMTTGVLLQK
     IVSAKSLMEF THIFIDEVHE RTEEMDFLLL VVRKLLRTNS RFVKVVLMSA TINCKQFADY
     FAVPVQNKMN PAYVFEVEGK PHAIEEYYLN DLGHIYHSGL PYRLEEPVIT KDVYEVAVSL
     IQMFDDLDMK ESGNKTWSGA QFVSERSSVL VFLPGLGEIN YMHELLTNMI HKRLQVYPLH
     SSVTLEEQNN VFLSPVPGYR KIILSTNIAE SSVTVPDVKY VIDFCLTRTL VCDEDTNYQS
     LRLSWASKTS CDQRKGRAGR VSKGYCYRLI PRDFWDSAIP DHVVPEMLRC PLGSTILKVK
     LLDMGEPRAL LATALSPPSL SDIERTILLL KEVGALAVSG QREDENPHDG ELTFLGRVLA
     QLPVSQQLGK LVVLGHVFGC LDECLIIAAA LSLKNFFTMP FRQHLDGYRN KVHFSGSSRS
     DCLALVEAFR AWQACRQRGE LRRPKDELDW GRLNYIQIKR IREVAELYEE LKNRISQFNM
     FVGPHHPVLD QEYPYKQRFI LQVVLAGAFY PNYFTFGQPD EEMAVRELAG KDPKTTVVLK
     HIPPYGFLYY KQLQSLFRQC GQVKSIVFDG AKAFVEFSRN PTERFKTLPA VNLAVKMSQL
     KVSLELSVHA AEEIEGKVQG GSVSKLRNTR VNVDFQKQTV DPMQVSFNTL DRPRTVADLL
     LTIDVTEVVE VGHFWGYRID ERNAELLKQL TAEINRLELV PLPIHPHPDL VCLAPFTDYN
     KESYFRAQIL YVSGNSAEVF FVDYGNRSHV DLDLLREIPC QFLELPFQAL EFKICKMRPS
     AKSLICGEHW SGGAHGRFAA LVGGCPLLVK VFSIVHSVLH VDVYRYSGAQ DAVNVRDVLI
     REGYAELAEE SYESKQSYEV LKGFFAKSVD TMPDGSVSSP LKDDEKHLLR ILLESFASNR
     LGAPNCKAVL HGPFNPYELK CHSLTRISKF RCVWIEKESI NSVVISDSPA DLHQRMLVAA
     SLSVNETGST MLLRETSLMP HIPGLPALLS MLFAPVMELR VDREGKCYTG VLCGLGWNSA
     TEAPILPEHD IELAFDVRLN VEDIVEINIL RAAINKLVCD GPNGSKYLGP ERIAQLQENA
     RQKLLGLFCR LKPREKITPQ WHEKPYEWNQ VDPRLIMEQA EPEGSPGKST SLYQLHTPVV
     LSP
//
ID   PTCD3_MOUSE             Reviewed;         685 AA.
AC   Q14C51; Q3UKH5; Q5XG65; Q6P9N5; Q9CZ12;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   08-MAR-2011, entry version 36.
DE   RecName: Full=Pentatricopeptide repeat-containing protein 3, mitochondrial;
DE   Flags: Precursor;
GN   Name=Ptcd3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Bone, and Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (Potential).
CC   -!- SIMILARITY: Belongs to the PTCD3 family.
CC   -!- SIMILARITY: Contains 10 PPR (pentatricopeptide) repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB28668.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK013131; BAB28668.1; ALT_INIT; mRNA.
DR   EMBL; AK146005; BAE26826.1; -; mRNA.
DR   EMBL; BC060687; AAH60687.1; -; mRNA.
DR   EMBL; BC084595; AAH84595.1; -; mRNA.
DR   EMBL; BC115434; AAI15435.1; -; mRNA.
DR   IPI; IPI00338458; -.
DR   RefSeq; NP_081551.2; NM_027275.3.
DR   UniGene; Mm.30256; -.
DR   ProteinModelPortal; Q14C51; -.
DR   STRING; Q14C51; -.
DR   PhosphoSite; Q14C51; -.
DR   PRIDE; Q14C51; -.
DR   Ensembl; ENSMUST00000082094; ENSMUSP00000080743; ENSMUSG00000063884.
DR   GeneID; 69956; -.
DR   KEGG; mmu:69956; -.
DR   CTD; 69956; -.
DR   MGI; MGI:1917206; Ptcd3.
DR   HOVERGEN; HBG068809; -.
DR   InParanoid; Q14C51; -.
DR   OMA; HIPCLMP; -.
DR   OrthoDB; EOG4TF0JR; -.
DR   PhylomeDB; Q14C51; -.
DR   NextBio; 330679; -.
DR   ArrayExpress; Q14C51; -.
DR   Bgee; Q14C51; -.
DR   CleanEx; MM_PTCD3; -.
DR   Genevestigator; Q14C51; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   InterPro; IPR002885; Pentatricopeptide_repeat.
DR   TIGRFAMs; TIGR00756; PPR; 2.
DR   PROSITE; PS51375; PPR; 3.
PE   2: Evidence at transcript level;
KW   Acetylation; Mitochondrion; Repeat; Transit peptide.
FT   TRANSIT       1     10       Mitochondrion (Potential).
FT   CHAIN        11    685       Pentatricopeptide repeat-containing
FT                                protein 3, mitochondrial.
FT                                /FTId=PRO_0000305029.
FT   REPEAT      150    184       PPR 1.
FT   REPEAT      185    220       PPR 2.
FT   REPEAT      254    288       PPR 3.
FT   REPEAT      289    329       PPR 4.
FT   REPEAT      330    366       PPR 5.
FT   REPEAT      367    407       PPR 6.
FT   REPEAT      412    446       PPR 7.
FT   REPEAT      454    488       PPR 8.
FT   REPEAT      489    523       PPR 9.
FT   REPEAT      572    606       PPR 10.
FT   MOD_RES     127    127       N6-acetyllysine (By similarity).
FT   CONFLICT    279    279       T -> A (in Ref. 2; AAI15435).
FT   CONFLICT    563    563       S -> G (in Ref. 2; AAI15435).
FT   CONFLICT    589    589       S -> T (in Ref. 2; AAI15435).
FT   CONFLICT    603    603       K -> N (in Ref. 2; AAI15435).
FT   CONFLICT    605    605       I -> T (in Ref. 1; BAE26826).
SQ   SEQUENCE   685 AA;  77796 MW;  10BD1C0ACC348BAE CRC64;
     MAAAAVAARR LSFRSGLVLL QTTRGTGVCE PKVCCRFYAG TESLPKVEGS DITGIEEIVI
     PKKKTWDKVA VLQALASTVN RDPTAAPYVF HDDPYLIPTS ALESRSFLLA KKSGETAAKF
     IINSYPKYFQ KDIAEPHIPC LMPEYFEPQI EDVSEAALEE RIRLRKVRAS VDMFDQLLQA
     GTTVSLETTN SLLDLLCYYG DQEPPADYPF QQTEHLENLE EAAEENNQTS KMESGPWKAQ
     NNAERIFALM PEKNARSYCT MIRGMVKHRA YAQALNVYTE LLNNRLSADV YTFNALIEAK
     TFILNEKFEE KWNDILDLLK HMVAQKVKPN LQTFNTILKG LRKCYSLGRI PALQILREMK
     HIGIEPSLAT YHHIIHLFYP RDLSAIKMPS LIIYDIMNEL EGRTFSPQDL DDGRFFQLAM
     SVCSSLRDLE LAYQVHRLLN TGDNRKLVGH DPLRKVYYSK FFSLICSLEQ IDVTLKWYKD
     LIPSVFLPHY QIFIGLLQAL DVANRLELVP QIWKDSKEYS HTFRDALREE VLMLMARDKH
     PPELQVAFAD CAADIKSTYE DQSARQPAFD WPANPLQYIA VLFLRGGRSQ EAWKMLELFK
     KHKKIPRNEL LEEFMDTAKA SGSTALAIEV VKLASAFSLP IGESLAQRVV MDFTVDPEQK
     EALGNLTELN SSDGESSSDS DSDDK
//
ID   Q14CG6_MOUSE            Unreviewed;       437 AA.
AC   Q14CG6;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAR-2011, entry version 30.
DE   SubName: Full=Gpr165 protein;
GN   Name=Gpr165;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
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DR   EMBL; BC113184; AAI13185.1; -; mRNA.
DR   EMBL; BC113791; AAI13792.1; -; mRNA.
DR   IPI; IPI00135394; -.
DR   UniGene; Mm.256065; -.
DR   ProteinModelPortal; Q14CG6; -.
DR   STRING; Q14CG6; -.
DR   Ensembl; ENSMUST00000033554; ENSMUSP00000033554; ENSMUSG00000031210.
DR   UCSC; uc009tuq.1; mouse.
DR   MGI; MGI:1923456; Gpr165.
DR   eggNOG; roNOG10112; -.
DR   HOVERGEN; HBG083058; -.
DR   InParanoid; Q14CG6; -.
DR   OrthoDB; EOG4CVG6Z; -.
DR   ArrayExpress; Q14CG6; -.
DR   Bgee; Q14CG6; -.
DR   Genevestigator; Q14CG6; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; IEA:InterPro.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   G-protein coupled receptor; Membrane; Receptor; Transducer;
KW   Transmembrane.
SQ   SEQUENCE   437 AA;  49172 MW;  264ED4C81B2A181E CRC64;
     MGFGDELTPE ALSVPSGFDD LITSTTSQVL QAASNAGRNG MLSKMDKLAD HMSNSGDLAD
     TSGPLDLEIV SQDEQVQFWL VVGYTIVVFA AIIGNWVLNH IIMKYKRVHT ATGLFVVNIS
     VTNMMLALLS SPFTMVRYLC NSLVFGKMTC HLSRFAQYSC AYVTVMSMAA ISLDRHRVML
     YPLKARITPM QGNVCIIIIW IVSTCAALPH AVYQKLYQVE FGNTTEESAC LPSFPYTSKS
     TWKYLDLGTF LLFFILPLLV LVAVYGHVAK KLWIHDAVDD INIHTYICQR GKKKQTLKML
     MTVVLLYTIS WLPLNVYLVL LSSESISSHN GLYFFLHWLA ISSSCYNPYI YCWLSDSFRI
     EVQKVIMEIQ KMLLDKISRL RGEHRRLSSV SHSQTPGSVD PNPGVPKFPR FRDFDELPSP
     PPSPTVEISF LHSVPRV
//
ID   F171B_MOUSE             Reviewed;         825 AA.
AC   Q14CH0; Q8C756; Q8CAF3; Q8CBZ4; Q8CFT5;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 40.
DE   RecName: Full=Protein FAM171B;
DE   Flags: Precursor;
GN   Name=Fam171b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon, Hypothalamus, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-792, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-792, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q14CH0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q14CH0-2; Sequence=VSP_025343;
CC   -!- SIMILARITY: Belongs to the FAM171 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC28648.1; Type=Erroneous initiation;
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DR   EMBL; AK034250; BAC28648.1; ALT_INIT; mRNA.
DR   EMBL; AK038899; BAC30163.1; -; mRNA.
DR   EMBL; AK052508; BAC35021.1; -; mRNA.
DR   EMBL; AL772256; CAM15058.1; -; Genomic_DNA.
DR   EMBL; AL772301; CAM15058.1; JOINED; Genomic_DNA.
DR   EMBL; AL772301; CAM13684.1; -; Genomic_DNA.
DR   EMBL; AL772256; CAM13684.1; JOINED; Genomic_DNA.
DR   EMBL; BC038086; AAH38086.1; -; mRNA.
DR   EMBL; BC113787; AAI13788.1; -; mRNA.
DR   IPI; IPI00226492; -.
DR   IPI; IPI00845605; -.
DR   RefSeq; NP_780723.1; NM_175514.2.
DR   UniGene; Mm.330351; -.
DR   UniGene; Mm.436122; -.
DR   PhosphoSite; Q14CH0; -.
DR   PRIDE; Q14CH0; -.
DR   Ensembl; ENSMUST00000051454; ENSMUSP00000062702; ENSMUSG00000048388.
DR   GeneID; 241520; -.
DR   KEGG; mmu:241520; -.
DR   CTD; 241520; -.
DR   MGI; MGI:2444579; Fam171b.
DR   eggNOG; roNOG14734; -.
DR   GeneTree; ENSGT00530000063318; -.
DR   HOGENOM; HBG715100; -.
DR   HOVERGEN; HBG107876; -.
DR   InParanoid; Q14CH0; -.
DR   OMA; VPGTLNE; -.
DR   OrthoDB; EOG49P9XX; -.
DR   NextBio; 385037; -.
DR   ArrayExpress; Q14CH0; -.
DR   Bgee; Q14CH0; -.
DR   Genevestigator; Q14CH0; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR018890; Uncharacterised_FAM171.
DR   Pfam; PF10577; UPF0560; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Glycoprotein; Membrane; Phosphoprotein; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     32       Potential.
FT   CHAIN        33    825       Protein FAM171B.
FT                                /FTId=PRO_0000287149.
FT   TOPO_DOM     33    353       Extracellular (Potential).
FT   TRANSMEM    354    374       Helical; (Potential).
FT   TOPO_DOM    375    825       Cytoplasmic (Potential).
FT   COMPBIAS     43     59       Gln-rich.
FT   MOD_RES     777    777       Phosphoserine (By similarity).
FT   MOD_RES     792    792       Phosphoserine.
FT   CARBOHYD    109    109       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    114    114       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    214    214       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ      43     46       Missing (in isoform 2).
FT                                /FTId=VSP_025343.
FT   CONFLICT     66     66       G -> E (in Ref. 3; AAI13788).
SQ   SEQUENCE   825 AA;  92045 MW;  29F78257E8A8BCD6 CRC64;
     MARLCRRVPC ALLLGLAAVL LKARLVPAAA RAELSRSDLS LIQQQQQQQQ QQQLQEQKQR
     EEAEEGRPEV PGASSTLVAP VSVFMLKVQV NDIVSRQYLS QAVVEVFVNY SKTNSTVTRS
     NGAVLIKVPY QLGLSLTIVA YKDGYVLTSL PWKTGRMPIY SSVTLSLFPQ SQANIWLFED
     TVLITGKLAD AKSQPSVQFS KAFIKLPDNH HISNVTGYLT VLHQFLKVDS FLPATGVTYK
     SGLENVELTP HAAICVKIYS GGKELKVDGS IHVSLPLLHT SNIKIGDRIP AWTFDMNAGV
     WVHHGWGTVK EHNSHLIWTY DAPHLGYWIA APSPATLDFG INDDFQDITA YHTVFLTAIL
     GGTIVIIIGF FAILLCYCRG KCATPQKRER NITKLEILKR DQTTSTTHIN HISSVKTALK
     AEDKPQLFNA KTSSYSPQRK ETTKTEAEER ISMVKTRDNF KIYNEDVSFL SVNHNYSRNP
     TQSLEPSMGS KQPKHINNNL SPSLGDAQEE KRYLTGTEEV YGRSHIPEQL MHIYSQPIAI
     LQTSDLFSMP EQLHAAKSAT LPRKGQLVYG QLMEPVNREN FTQTLPKMPM HSHVQAPDAR
     EEDIVLEGQQ SLPSQTSDWS RYSNSLLESV SVPGTLNEAV VMTPFSSELQ GISEQTLLEL
     SKGKPPHPRA WFVSLDGKPV AQVRHSFIDL KKGKRTQSND TSLDSGVDMN EHQSSRKLER
     EKTFIKSMHQ PKILYLEDLD LSSSESGTTV CSPEDPALRH ILEGGSGVII EHPGEESPGR
     KSTVEDFEAN TSPTKKRGRP PPLAKRDSKT NIWKKREERP LIPLN
//
ID   Q14DQ3_MOUSE            Unreviewed;       795 AA.
AC   Q14DQ3;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAR-2011, entry version 42.
DE   SubName: Full=Mark1 protein;
GN   Name=Mark1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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CC   -----------------------------------------------------------------------
DR   EMBL; BC112400; AAI12401.1; -; mRNA.
DR   IPI; IPI00928064; -.
DR   RefSeq; NP_663490.2; NM_145515.2.
DR   UniGene; Mm.7445; -.
DR   ProteinModelPortal; Q14DQ3; -.
DR   SMR; Q14DQ3; 54-371, 699-795.
DR   STRING; Q14DQ3; -.
DR   Ensembl; ENSMUST00000027929; ENSMUSP00000027929; ENSMUSG00000026620.
DR   GeneID; 226778; -.
DR   KEGG; mmu:226778; -.
DR   CTD; 226778; -.
DR   MGI; MGI:2664902; Mark1.
DR   eggNOG; roNOG09909; -.
DR   HOVERGEN; HBG052453; -.
DR   InParanoid; Q14DQ3; -.
DR   ArrayExpress; Q14DQ3; -.
DR   Bgee; Q14DQ3; -.
DR   Genevestigator; Q14DQ3; -.
DR   InterPro; IPR001772; Kinase-assoc_KA1.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   Gene3D; G3DSA:3.30.310.80; Kinase-assoc_KA1; 1.
DR   Pfam; PF02149; KA1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF103243; Kinase-assoc_KA1; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50032; KA1; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding.
SQ   SEQUENCE   795 AA;  88316 MW;  7F38C25AE7338682 CRC64;
     MSARTPLPTV NERDTENHTS VDGYTETHIP PAKSSSRQNL PRCRNSITSA TDEQPHIGNY
     RLQKTIGKGN FAKVKLARHV LTGREVAVKI IDKTQLNPTS LQKLFREVRI MKILNHPNIV
     KLFEVIETEK TLYLVMEYAS GGEVFDYLVA HGRMKEKEAR AKFRQIVSAV QYCHQKCIVH
     RDLKAENLLL DADMNIKIAD FGFSNEFTVG NKLDTFCGSP PYAAPELFQG KKYDGPEVDV
     WSLGVILYTL VSGSLPFDGQ NLKELRERVL RGKYRIPFYM STDCENLLKK LLVLNPIKRG
     SLEQIMKDRW MNVGHEEEEL KPYSEPELDL SDAKRIDIMV TMGFARDEIN DALVSQKYDE
     VMATYILLGR KPPEFEGGES LSSGSLCQRS RPSSDLNNST LQSPAHLKVQ RSISANQKQR
     RFSDHAGPSI PPAVSYTKRP QANSVESEQK EEWGKDTARR LGSTTVGSKS EVTASPLVGP
     DRKKSTASPS NNVYSGGSMA RRNTYVCERS TDRYAALQNG RDSSLTEMSA SSMSSAGSTV
     ASAGPSARPR HQKSMSTSGH PIKVTLPTIK DGSEAYRPGA AQRVPAASPS AHSISASTPD
     RTHFPRGSSS RSTFHGEQLR ERRSAAYNGP PASPSHETGA FAHARRGTST GIISKITSKF
     VRRDPSEGEA SGRADTARGS SGDPKERDKD EGKEAKPRSL RFTWSMKTTS SMDPNDMLRE
     IRKVLDANTC DYEQKERFLL FCVHGDARQD SLVQWEMEVC KLPRLSLNGV RFKRISGTSI
     AFKNIASKIA NELKL
//
ID   DOK7_MOUSE              Reviewed;         504 AA.
AC   Q18PE0; Q3TCZ6; Q5FW70; Q8C8U7;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=Protein Dok-7;
DE   AltName: Full=Downstream of tyrosine kinase 7;
GN   Name=Dok7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP   LOCATION, INTERACTION WITH MUSK, DEVELOPMENTAL STAGE, DISRUPTION
RP   PHENOTYPE, AND MUTAGENESIS OF 158-ARG-ARG-159 AND ARG-174.
RC   STRAIN=C57BL/6;
RX   PubMed=16794080; DOI=10.1126/science.1127142;
RA   Okada K., Inoue A., Okada M., Murata Y., Kakuta S., Jigami T.,
RA   Kubo S., Shiraishi H., Eguchi K., Motomura M., Akiyama T., Iwakura Y.,
RA   Higuchi O., Yamanashi Y.;
RT   "The muscle protein Dok-7 is essential for neuromuscular
RT   synaptogenesis.";
RL   Science 312:1802-1805(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 19-504 (ISOFORM 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Probable muscle-intrinsic activator of MUSK that plays
CC       an essential role in neuromuscular synaptogenesis. Acts in aneural
CC       activation of MUSK and subsequent acetylcholine receptor (AchR)
CC       clustering in myotubes. Induces autophosphorylation of MUSK (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with the cytoplasmic part of MUSK.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC       Cell junction, synapse. Note=Accumulates at neuromuscular
CC       junctions.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q18PE0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q18PE0-2; Sequence=VSP_020636;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q18PE0-3; Sequence=VSP_020637;
CC         Note=No experimental confirmation available;
CC   -!- DEVELOPMENTAL STAGE: Expressed in the central region encompassing
CC       the endplate area of the diaphragm muscles at day 14.5 of
CC       embryonic development (E14.5), when AChRs cluster in a nerve- and
CC       agrinin-dependent manner.
CC   -!- DISRUPTION PHENOTYPE: Mice are immobile at birth and die shortly
CC       thereafter. They do not form neither acetylcholine receptor
CC       clusters nor neuromuscular synapses.
CC   -!- SIMILARITY: Contains 1 IRS-type PTB domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH89590.1; Type=Erroneous initiation;
CC       Sequence=BAC31923.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AB220919; BAE96740.1; -; mRNA.
DR   EMBL; AK044445; BAC31923.1; ALT_INIT; mRNA.
DR   EMBL; AK170454; BAE41809.1; -; mRNA.
DR   EMBL; BC089590; AAH89590.1; ALT_INIT; mRNA.
DR   IPI; IPI00227315; -.
DR   IPI; IPI00654307; -.
DR   IPI; IPI00788378; -.
DR   RefSeq; NP_766296.1; NM_172708.3.
DR   UniGene; Mm.205483; -.
DR   PDB; 3ML4; X-ray; 2.60 A; A/B/C/D=1-220.
DR   PDBsum; 3ML4; -.
DR   ProteinModelPortal; Q18PE0; -.
DR   SMR; Q18PE0; 3-239.
DR   STRING; Q18PE0; -.
DR   Ensembl; ENSMUST00000114270; ENSMUSP00000109909; ENSMUSG00000044716.
DR   Ensembl; ENSMUST00000114273; ENSMUSP00000109912; ENSMUSG00000044716.
DR   GeneID; 231134; -.
DR   KEGG; mmu:231134; -.
DR   UCSC; uc008xdk.1; mouse.
DR   UCSC; uc008xdl.1; mouse.
DR   UCSC; uc008xdm.1; mouse.
DR   CTD; 231134; -.
DR   MGI; MGI:3584043; Dok7.
DR   eggNOG; roNOG08431; -.
DR   GeneTree; ENSGT00390000015386; -.
DR   HOVERGEN; HBG080009; -.
DR   OMA; LLMLAYK; -.
DR   ArrayExpress; Q18PE0; -.
DR   Bgee; Q18PE0; -.
DR   CleanEx; MM_DOK7; -.
DR   Genevestigator; Q18PE0; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0005158; F:insulin receptor binding; IEA:InterPro.
DR   GO; GO:0007528; P:neuromuscular junction development; IDA:MGI.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:MGI.
DR   GO; GO:0043113; P:receptor clustering; IDA:MGI.
DR   InterPro; IPR002404; Insln_rcpt_S1.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Pfam; PF02174; IRS; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS51064; IRS_PTB; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW   Membrane; Synapse.
FT   CHAIN         1    504       Protein Dok-7.
FT                                /FTId=PRO_0000250372.
FT   DOMAIN        4    109       PH.
FT   DOMAIN      105    210       IRS-type PTB.
FT   COMPBIAS    246    358       Ser-rich.
FT   VAR_SEQ      34    178       DCLLMLVYKDKCERSKGLRERSSLTLEDICGLEPALPYEGL
FT                                AHTLAIICLSQAVMLGFDSHEAMCAWDTRIRYALGEVHRFH
FT                                VTVAPGTKLESGPATLHLCNDILVLARDIPPTVMGQWKLSD
FT                                LRRYGAVPNGFIFEGGTRCGYW -> G (in isoform
FT                                2).
FT                                /FTId=VSP_020636.
FT   VAR_SEQ     501    504       KPPP -> MATSSPGFTVTHPGSPGRVAADSPGPERPHSEM
FT                                PTYVNIPISPISRPQLHYMDLELPGASAGVRGASTSRYAQI
FT                                DIAATETAHRVGVRHAQTREERLPELEQRKKGP (in
FT                                isoform 3).
FT                                /FTId=VSP_020637.
FT   MUTAGEN     158    159       RR->AA: Abolishes interaction with MUSK
FT                                and function; when associated with A-174.
FT   MUTAGEN     174    174       R->A: Abolishes interaction with MUSK and
FT                                function; when associated with A-158 and
FT                                A-159.
SQ   SEQUENCE   504 AA;  53177 MW;  AB0FC717F6C1A5B2 CRC64;
     MTEAALVEGQ VKLRDGKKWK SRWLVLRKPS PVADCLLMLV YKDKCERSKG LRERSSLTLE
     DICGLEPALP YEGLAHTLAI ICLSQAVMLG FDSHEAMCAW DTRIRYALGE VHRFHVTVAP
     GTKLESGPAT LHLCNDILVL ARDIPPTVMG QWKLSDLRRY GAVPNGFIFE GGTRCGYWAG
     VFFLSSAEGE QMSFLFDCIV RGISPTKGPF GLRPVLPDPS SGGPSASEER VAQEALEALQ
     LEKRLSLLSH SGRPGSGGDD RSLSSSSSEA SHSDISASSR LTAWPEQSSS SAGTSQEGPG
     LVAAQGPGEA MLGASRPPLK PLRPRQLQEV GRQSSSDSGI ATGSHSSYSG SFSSYAGSNL
     DVWRAGEEFG SLLSLPPGAS APEPRLCACP PGAAEYQVPT SLRHHYDTPR SLRQAPRDPS
     PASQGSSDHG SATDLGGQAP TGCPSSWLGA RRRGQATEGP GSDAALPSPS PGESWEAGSP
     HAGPPPAFFL SCSICGGLKV KPPP
//
ID   Q19VH2_MOUSE            Unreviewed;       664 AA.
AC   Q19VH2;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   08-MAR-2011, entry version 40.
DE   SubName: Full=Actin-binding LIM protein 2;
GN   Name=Ablim2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Skeletal muscle;
RX   PubMed=17194709; DOI=10.1074/jbc.M607549200;
RA   Barrientos T., Frank D., Kuwahara K., Bezprozvannaya S., Pipes G.C.T.,
RA   Bassel-Duby R., Richardson J.A., Katus H.A., Olson E.N., Frey N.;
RT   "Two novel members of the ABLIM protein family, ABLIM-2 and -3,
RT   associate with STARS and directly bind F-actin.";
RL   J. Biol. Chem. 282:8393-8403(2007).
CC   -!- SIMILARITY: Contains 4 LIM zinc-binding domains.
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DR   EMBL; DQ413175; ABD83328.1; -; mRNA.
DR   IPI; IPI00762199; -.
DR   UniGene; Mm.254446; -.
DR   ProteinModelPortal; Q19VH2; -.
DR   SMR; Q19VH2; 23-286, 593-664.
DR   STRING; Q19VH2; -.
DR   Ensembl; ENSMUST00000129347; ENSMUSP00000123525; ENSMUSG00000029095.
DR   UCSC; uc008xei.1; mouse.
DR   MGI; MGI:2385758; Ablim2.
DR   GeneTree; ENSGT00570000079028; -.
DR   HOGENOM; HBG443863; -.
DR   HOVERGEN; HBG031499; -.
DR   InParanoid; Q19VH2; -.
DR   ArrayExpress; Q19VH2; -.
DR   Bgee; Q19VH2; -.
DR   Genevestigator; Q19VH2; -.
DR   GO; GO:0030016; C:myofibril; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:MGI.
DR   InterPro; IPR003128; Villin_headpiece.
DR   InterPro; IPR001781; Znf_LIM.
DR   Gene3D; G3DSA:1.10.950.10; VHP; 1.
DR   Gene3D; G3DSA:2.10.110.10; Znf_LIM; 3.
DR   Pfam; PF00412; LIM; 4.
DR   Pfam; PF02209; VHP; 1.
DR   SMART; SM00132; LIM; 4.
DR   SMART; SM00153; VHP; 1.
DR   SUPFAM; SSF47050; VHP; 1.
DR   PROSITE; PS51089; HP; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 4.
PE   2: Evidence at transcript level;
KW   LIM domain; Metal-binding; Zinc.
SQ   SEQUENCE   664 AA;  73590 MW;  5CFDD99F0F821DE7 CRC64;
     MSAVSQPQAA HAPLEKPAST AILCNTCGNV CKGEVLRVQN KYFHIRCFVC KACGCDLAEG
     GFFVRQGEHI CTRDYQRLYG TRCFSCDRFI EGEVVSALGK TYHPDCFVCA VCRLPFPPGD
     RVTFNGKECM CQKCSPPTLL GNSAHVAQGL RSCGGCGLEI KNGQALVALD KHWHLGCFKC
     KTCGKLLNAE YISKDGLPYC EADYHSKFGI RCDGCEKYIT GRVLEAGEKH YHPSCALCVR
     CGQMFSEGEE MYLQGSSIWH PACRQAARTE DKSKMHSSVC SQPCPGTLPC ALQETRTSSE
     SIVSVPASST SGSPSRVIYA KLGDEILDYR DLAALPKNKA IYNIDRPDMI SYSPYISHSA
     VGDRQSYGEG DQDDRSCKQC RTSSPSSAGS VSLGHYTPTS RSPQHYSRPA GTVSVGTSSC
     LSLSQHPSPT SVFRHHYIPY FRGSESGRST PSLSVHSDSR PPSSTYQQAP RHFHVPDTGV
     KDNIYRKPPI YKQHAARRLD VEDSSFDQDS RKKTTWLLLK GDADTRTNSP DLDSQSLSLS
     SGTDQEPLQR MAGDSLYSRF PYSKPDTLPG PRKDGLDLRN ANLAPCGADP DASWGTREYK
     IYPYDSLIVT NRIRVKLPKD VDRTRLERHL SPEEFQEVFG MSIEEFDRLA LWKRNDLKKK
     ALLF
//
ID   Q1A602_MOUSE            Unreviewed;       911 AA.
AC   Q1A602;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   SubName: Full=Non-muscle alpha-actinin 4;
GN   Name=Actn4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/cJ;
RX   PubMed=16751418;
RA   Zhao Z., Deocharan B., Scherer P.E., Ozelius L.J., Putterman C.;
RT   "Differential binding of cross-reactive anti-DNA antibodies to
RT   mesangial cells: the role of alpha-actinin.";
RL   J. Immunol. 176:7704-7714(2006).
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CC   -----------------------------------------------------------------------
DR   EMBL; DQ303410; ABC66068.1; -; mRNA.
DR   IPI; IPI00118899; -.
DR   UniGene; Mm.81144; -.
DR   ProteinModelPortal; Q1A602; -.
DR   SMR; Q1A602; 47-271, 286-758, 761-911.
DR   STRING; Q1A602; -.
DR   Ensembl; ENSMUST00000068045; ENSMUSP00000066068; ENSMUSG00000054808.
DR   MGI; MGI:1890773; Actn4.
DR   HOVERGEN; HBG050453; -.
DR   InParanoid; Q1A602; -.
DR   ArrayExpress; Q1A602; -.
DR   Bgee; Q1A602; -.
DR   Genevestigator; Q1A602; -.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR   GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR014837; EF-hand_Ca_insen.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 2.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF08726; efhand_Ca_insen; 1.
DR   Pfam; PF00435; Spectrin; 4.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM00150; SPEC; 4.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   2: Evidence at transcript level;
KW   Actin-binding; Calcium; Repeat.
SQ   SEQUENCE   911 AA;  104915 MW;  0C5FC2E43B5D8FD2 CRC64;
     MVDYHAANQA YQYGPSSGGN GTGGGGGMGD YMAQEDDWDR DLLLDPAWEK QQRKTFTAWC
     NSHLRKAGTQ IENIDEDFRD GLKLMLLLEV ISGERLPKPE RGKMRVHKIN NVNKALDFIA
     SKGVKLVSIG AEEIVDGNAK MTLGMIWTII LRFAIQDISV EETSAKEGLL LWCQRKTAPY
     KNVNVQNFHI SWKDGLAFNA LIHRHRPELI EYDKLRKDDP VTNLNNAFEV AEKYLDIPKM
     LDAEDIVNTA RPDEKAIMTY VSSFYHAFSG AQKAETAANR ICKVLAVNQE NEHLMEDYER
     LASDLLEWIR RTIPWLEDRV PQKTIQEMQQ KLEDFRDYRR VHKPPKVQEK CQLEINFNTL
     QTKLRLSNRP AFMPSEGRMV SDINNGWQHL EQAEKGYEEW LLNEIRRLER LDHLAEKFRQ
     KASIHEAWTD GKEAMLKHRD YETATLSDIK ALIRKHEAFE SDLAAHQDRV EQIAAIAQEL
     NELDYYDSHN VNTRCQKICD QWDNLGSLTH SRREALEKTE KQLETIDQLH LEYAKRAAPF
     NNWMESAMED LQDMFIVHTI EEIEGLISAH DQFKSTLPDA DREREAILAI HKEAQRIAES
     NHIKLSGSNP YTSVTPQIIN SKWEKVQQLV PKRDHALLEE QSKQQSNEHL RRQFASQANM
     VGPWIQTKME EIGRISIEMN GTLEDQLSHL KQYERSIVDY KPNLDLLEQQ HQLIQEALIF
     DNKHTNYTME HLRVGWEQLL TTIARTINEV ENQILTRDAK GISQEQMQEF RASFNHFDKD
     HGGALGPEEF KACLISLGYD VENDRQGDAE FNRIMSVVDP NHSGLVTFQA FIDFMSRETT
     DTDTADQVIA SFKVLAGDKN FITAEELRRE LPPDQAEYCI ARMAPYQGPD AAPGALDYKS
     FSTALYGESD L
//
ID   NSUN2_MOUSE             Reviewed;         757 AA.
AC   Q1HFZ0; A0PJD6; Q3U972; Q8BPG9; Q8CDF9; Q91YX9;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=tRNA (cytosine-5-)-methyltransferase NSUN2;
DE            EC=2.1.1.29;
DE   AltName: Full=Myc-induced SUN domain-containing protein;
DE   AltName: Full=NOL1/NOP2/Sun domain family member 2;
GN   Name=Nsun2; Synonyms=D13Wsu123e, Misu;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=16713953; DOI=10.1016/j.cub.2006.04.027;
RA   Frye M., Watt F.M.;
RT   "The RNA methyltransferase Misu (NSun2) mediates Myc-induced
RT   proliferation and is upregulated in tumors.";
RL   Curr. Biol. 16:971-981(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: RNA methyltransferase that methylates tRNAs, and
CC       possibly RNA polymerase III transcripts. Methylates cytosine to 5-
CC       methylcytosine (m5C) at position 34 of intron-containing
CC       tRNA(Leu)(CAA) precursors. Not able to modify tRNAs at positions
CC       48 or 49 (By similarity). May act downstream of Myc to regulate
CC       epidermal cell growth and proliferation.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-
CC       homocysteine + tRNA containing 5-methylcytosine.
CC   -!- SUBUNIT: Interacts with NPM1 and NCL during interphase;
CC       interaction is disrupted following phosphorylation at Ser-139 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm.
CC       Note=Concentrated in the nucleolus during interphase and
CC       distributed in the perichromosome and cytoplasm during mitosis.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q1HFZ0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q1HFZ0-2; Sequence=VSP_025969;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed at low level. Up-
CC       regulated in tumors.
CC   -!- DEVELOPMENTAL STAGE: In G1, it is predominantly found in the
CC       nucleol. During S phase, it is present at its highest level and is
CC       distributed more uniformly throughout the nucleus (at protein
CC       level).
CC   -!- INDUCTION: By Myc (at protein level).
CC   -!- PTM: Phosphorylated at Ser-139 by Aurora-B/STK12 during mitosis,
CC       leading to abolish methyltransferase activity and the interaction
CC       with NPM1 (By similarity).
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RsmB/NOP
CC       family. TRM4 subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH13625.1; Type=Erroneous initiation;
CC       Sequence=BAC36110.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; DQ490066; ABF29536.1; -; mRNA.
DR   EMBL; AK030124; BAC26795.1; -; mRNA.
DR   EMBL; AK075999; BAC36110.1; ALT_INIT; mRNA.
DR   EMBL; AK150631; BAE29720.1; -; mRNA.
DR   EMBL; AK151917; BAE30795.1; -; mRNA.
DR   EMBL; BC013625; AAH13625.1; ALT_INIT; mRNA.
DR   EMBL; BC025549; AAH25549.1; ALT_TERM; mRNA.
DR   IPI; IPI00850580; -.
DR   IPI; IPI00894870; -.
DR   RefSeq; NP_663329.3; NM_145354.4.
DR   UniGene; Mm.260009; -.
DR   ProteinModelPortal; Q1HFZ0; -.
DR   SMR; Q1HFZ0; 48-430.
DR   STRING; Q1HFZ0; -.
DR   PhosphoSite; Q1HFZ0; -.
DR   PRIDE; Q1HFZ0; -.
DR   Ensembl; ENSMUST00000022087; ENSMUSP00000022087; ENSMUSG00000021595.
DR   Ensembl; ENSMUST00000109699; ENSMUSP00000105321; ENSMUSG00000021595.
DR   GeneID; 28114; -.
DR   KEGG; mmu:28114; -.
DR   NMPDR; fig|10090.3.peg.28089; -.
DR   CTD; 28114; -.
DR   MGI; MGI:107252; Nsun2.
DR   eggNOG; roNOG05017; -.
DR   GeneTree; ENSGT00550000074937; -.
DR   HOGENOM; HBG315458; -.
DR   HOVERGEN; HBG106711; -.
DR   InParanoid; Q1HFZ0; -.
DR   OrthoDB; EOG4K9BBQ; -.
DR   PhylomeDB; Q1HFZ0; -.
DR   BRENDA; 2.1.1.29; 244.
DR   NextBio; 306674; -.
DR   ArrayExpress; Q1HFZ0; -.
DR   Bgee; Q1HFZ0; -.
DR   CleanEx; MM_NSUN2; -.
DR   Genevestigator; Q1HFZ0; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016428; F:tRNA (cytosine-5-)-methyltransferase activity; IEA:EC.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR001678; Fmu/NOL1/Nop2p.
DR   InterPro; IPR023267; RCMT.
DR   InterPro; IPR023270; RCMT_NCL1.
DR   Pfam; PF01189; Nol1_Nop2_Fmu; 1.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   PRINTS; PR02011; RCMTNCL1.
DR   PROSITE; PS01153; NOL1_NOP2_SUN; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Methyltransferase; Nucleus;
KW   Phosphoprotein; RNA-binding; S-adenosyl-L-methionine; Transferase;
KW   tRNA processing; tRNA-binding.
FT   CHAIN         1    757       tRNA (cytosine-5-)-methyltransferase
FT                                NSUN2.
FT                                /FTId=PRO_0000289224.
FT   REGION      184    190       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   ACT_SITE    321    321       Nucleophile (Potential).
FT   BINDING     215    215       S-adenosyl-L-methionine (By similarity).
FT   BINDING     242    242       S-adenosyl-L-methionine (By similarity).
FT   BINDING     268    268       S-adenosyl-L-methionine (By similarity).
FT   MOD_RES      23     23       Phosphoserine.
FT   MOD_RES     139    139       Phosphoserine (By similarity).
FT   MOD_RES     456    456       Phosphoserine (By similarity).
FT   MOD_RES     461    461       Phosphothreonine (By similarity).
FT   MOD_RES     473    473       Phosphoserine (By similarity).
FT   MOD_RES     592    592       Phosphoserine (By similarity).
FT   MOD_RES     723    723       Phosphoserine.
FT   VAR_SEQ       1     66       Missing (in isoform 2).
FT                                /FTId=VSP_025969.
FT   CONFLICT    206    206       F -> L (in Ref. 2; BAE30795/BAE29720).
FT   CONFLICT    253    253       V -> L (in Ref. 2; BAE30795/BAE29720).
FT   CONFLICT    482    482       S -> L (in Ref. 1; ABF29536 and 3;
FT                                AAH25549).
FT   CONFLICT    490    490       N -> I (in Ref. 1; ABF29536).
SQ   SEQUENCE   757 AA;  85452 MW;  73B06947DEC50298 CRC64;
     MGRRARGRRF QQPPQPEGEE DASDGGRKRG QAGWEGGYPE IVKENKLFEH YYQELKIVPE
     GEWDQFMESL REPLPATLRI TGYKSHAKEI LHCLKNKYFK ELEDLEVDGQ KVEVPQPLSW
     YPEELAWHTN LSRKILRKSP LLAKFHQFLV SETESGNISR QEAVSMIPPL LLNVEPHHKI
     LDMCAAPGSK TTQLIEMLHA DMSVPFPEGF VIANDVDNKR CYLLVHQAKR LSSPCIMVVN
     HDASSIPRLT VDVDGRKEIL FYDRILCDVP CSGDGTMRKN IDVWKKWTTL NSLQLHGLQL
     RIATRGAEQL AEGGRMVYST CSLNPVEDEA VIAALLEKSE GALELADVSA ELPGLKWMPG
     VSQWKVMTRD GQWFADWHEV PQGRHTQIRP TMFPPTDLEK LQAMHLERCL RILPHHQNTG
     GFFVAVLVKK APMPWNKRQP KVQNKSAEAR EPRVSSHVAA TEGNPSDQSE LESQMITGAG
     DSETAHNTEN TESNEKKDGV CGPPPSKKMK LFGFKEDPFV FIPEDDPLFP PIEKFYALDP
     SFPRMNLLTR TTEGKKRQLY MVSKELRNVL LNNSEKMKVI NTGIKVWCRN NSGEEFDCAF
     RLAQEGIYTL YPFINSRIIT VSMEDVKTLL TQENPFFRKL SSEAYSQVKD LAKGSVVLKY
     EPDSANPDTL QCPIVLCGWR GKASIRTFVP KNERLHYLRM MGLEVLGEKK KEGVILTNEN
     AASPEQPGDE DAKQTAQDPC VPDSVPGCDA AAAEPSR
//
ID   M3K13_MOUSE             Reviewed;         959 AA.
AC   Q1HKZ5; Q8BKN0;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Mitogen-activated protein kinase kinase kinase 13;
DE            EC=2.7.11.25;
GN   Name=Map3k13;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RA   Itoh A., Itoh T.;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 690-959.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Activates the JUN N-terminal pathway through activation
CC       of the MAP kinase kinase MAP2K7. Acts synergistically with PRDX3
CC       to regulate the activation of NF-kappa-B in the cytosol. This
CC       activation is kinase-dependent and involves activating the IKK
CC       complex, the IKBKB-containing complex that phosphorylates
CC       inhibitors of NF-kappa-B (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activated by autophosphorylation and
CC       homodimerization (By similarity).
CC   -!- SUBUNIT: Homodimer; forms dimers through the leucine-zipper motif.
CC       Interacts with the C-terminus of MAPK8IP1 through the kinase
CC       catalytic domain. Binds PRDX3. Associates with the IKK complex
CC       through the kinase domain.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC       protein (By similarity).
CC   -!- PTM: Autophosphorylated on serine and threonine residues (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; DQ480427; ABF19581.1; -; mRNA.
DR   EMBL; AK051378; BAC34618.1; -; mRNA.
DR   IPI; IPI00132644; -.
DR   RefSeq; NP_766409.2; NM_172821.3.
DR   UniGene; Mm.420837; -.
DR   UniGene; Mm.438136; -.
DR   ProteinModelPortal; Q1HKZ5; -.
DR   SMR; Q1HKZ5; 160-407.
DR   STRING; Q1HKZ5; -.
DR   PRIDE; Q1HKZ5; -.
DR   Ensembl; ENSMUST00000042065; ENSMUSP00000047388; ENSMUSG00000033618.
DR   GeneID; 71751; -.
DR   KEGG; mmu:71751; -.
DR   UCSC; uc007yrr.1; mouse.
DR   CTD; 71751; -.
DR   MGI; MGI:2444243; Map3k13.
DR   eggNOG; roNOG14999; -.
DR   GeneTree; ENSGT00600000084040; -.
DR   HOGENOM; HBG447061; -.
DR   HOVERGEN; HBG052383; -.
DR   InParanoid; Q1HKZ5; -.
DR   OMA; HRRGNSR; -.
DR   OrthoDB; EOG45MN4T; -.
DR   BRENDA; 2.7.11.25; 244.
DR   NextBio; 334401; -.
DR   ArrayExpress; Q1HKZ5; -.
DR   Bgee; Q1HKZ5; -.
DR   CleanEx; MM_MAP3K13; -.
DR   Genevestigator; Q1HKZ5; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:EC.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR017419; MAP3K12_MAP3K13.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PIRSF; PIRSF038165; MAPKKK12_MAPKKK13; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; Magnesium; Membrane; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Repeat;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    959       Mitogen-activated protein kinase kinase
FT                                kinase 13.
FT                                /FTId=PRO_0000277591.
FT   DOMAIN      167    408       Protein kinase.
FT   DOMAIN      432    453       Leucine-zipper 1.
FT   DOMAIN      485    506       Leucine-zipper 2.
FT   NP_BIND     173    181       ATP (By similarity).
FT   ACT_SITE    278    278       Proton acceptor (By similarity).
FT   BINDING     194    194       ATP (By similarity).
SQ   SEQUENCE   959 AA;  106987 MW;  18424BA1695DEDAE CRC64;
     MANPQEHLSC SSLPHLPLTE NKTSGGRNEL AAMGNHPSPK LPEDPQERGA IQSELMEITG
     SPISTTVLTS VSEDSRGQFE NSVLQLREQD ESEMTLSLGN SNTVDGENTN GPEDIKIQFS
     RSGSGSGGFL EGLFGCLRPV WNIIGKAYST DYKLQQQDTW EVPFEEISEL QWLGSGAQGA
     VFLGKFRAEE VAIKKVREQN ETDIKHLRKL KHPNIIAFKG VCTQAPCYCI IMEYCAHGQL
     YEVLRAGRKI TPRLLVDWST GIASGMNYLH LHKIIHRDLK SPNVLVTHTD AVKISDFGTS
     KELSDKSTKM SFAGTVAWMA PEVIRNEPVS EKVDIWSFGV VLWELLTGEI PYKDVDSSAI
     IWGVGSNSLH LPVPSTCPDG FKILMKQTWQ SKPRNRPSFR QTLMHLDIAS ADVLATPQET
     YFKSQAEWRE EVKKHFEKIK SEGTCIHRLD EELIRRRREE LRHALDIREH YERKLERANN
     LYMELSAIML QLEMREKELL KREQAVEKKY PGTYKRHPVR PIIHPNAMEK LMKRKGVPHK
     AGVQTKRPDL LRSEGIPSTE AVPTASPLSG SPKMSTASSR SRYRSKPRHR RGNSRGSHSD
     FAAILKTQPA QENSPHPTYM HHTQAQCASV HQHNPLQQQY QQIPPAQPQS RHPRLNAHGQ
     DIATCANNLR YFGPAAALRS PLSNHAQRQM PGSSPDLIST AMAADWRNSE LDQDQVGPWG
     CCQAEPYDPC FQCRPEHSGS LDVPTTEPVG RSPDLSSSPA HNPLSGNAQG SERTGANGFS
     GCQSGISHQF TPPMLPQKTR PLQKSGDDSS EEEGEVDSEV EFPRRQRPHR CISSYQSYST
     FSSENFSVSD GEEGNTSDHS NSPDESANRR QDRLAETLDD LLSQTPEAPI EISSHSDGLS
     DKECAVRRVK TQMSLGKLCA EERGYENPVQ FGDSDCDSSE GECSDATVRT SKNYSSATW
//
ID   S35F3_MOUSE             Reviewed;         421 AA.
AC   Q1LZI2; Q8BL51;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   08-MAR-2011, entry version 36.
DE   RecName: Full=Solute carrier family 35 member F3;
GN   Name=Slc35f3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Putative solute transporter (Potential).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the SLC35F solute transporter family.
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DR   EMBL; AK046359; BAC32690.1; -; mRNA.
DR   EMBL; BC115859; AAI15860.1; -; mRNA.
DR   EMBL; BC115965; AAI15966.1; -; mRNA.
DR   IPI; IPI00830284; -.
DR   RefSeq; NP_780643.2; NM_175434.3.
DR   UniGene; Mm.405238; -.
DR   UniGene; Mm.459322; -.
DR   PRIDE; Q1LZI2; -.
DR   Ensembl; ENSMUST00000108759; ENSMUSP00000104390; ENSMUSG00000057060.
DR   GeneID; 210027; -.
DR   KEGG; mmu:210027; -.
DR   UCSC; uc009nyt.1; mouse.
DR   CTD; 210027; -.
DR   MGI; MGI:2444426; Slc35f3.
DR   eggNOG; roNOG05665; -.
DR   GeneTree; ENSGT00390000008727; -.
DR   HOGENOM; HBG505578; -.
DR   HOVERGEN; HBG108446; -.
DR   InParanoid; Q1LZI2; -.
DR   OMA; VKQRYRE; -.
DR   OrthoDB; EOG4NP73M; -.
DR   NextBio; 372830; -.
DR   ArrayExpress; Q1LZI2; -.
DR   Bgee; Q1LZI2; -.
DR   CleanEx; MM_SLC35F3; -.
DR   Genevestigator; Q1LZI2; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000620; DMT.
DR   Pfam; PF00892; DUF6; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    421       Solute carrier family 35 member F3.
FT                                /FTId=PRO_0000307880.
FT   TRANSMEM     66     86       Helical; (Potential).
FT   TRANSMEM     98    118       Helical; (Potential).
FT   TRANSMEM    149    169       Helical; (Potential).
FT   TRANSMEM    179    199       Helical; (Potential).
FT   TRANSMEM    208    228       Helical; (Potential).
FT   TRANSMEM    232    252       Helical; (Potential).
FT   TRANSMEM    266    286       Helical; (Potential).
FT   TRANSMEM    305    325       Helical; (Potential).
FT   TRANSMEM    326    346       Helical; (Potential).
FT   TRANSMEM    352    372       Helical; (Potential).
FT   CONFLICT     86    109       LARLTFKTFDAPFTLTWFATNWNF -> ARQADFQDLRRTV
FT                                HPDVVCHQLEL (in Ref. 1; BAC32690).
FT   CONFLICT    153    153       K -> R (in Ref. 1; BAC32690).
SQ   SEQUENCE   421 AA;  46924 MW;  40259CC972850054 CRC64;
     MKKHSARVAP LSACNSPVLT LTKVEGEERP REPPGPAEAQ APAGTEAGGR TSRHNWTCSQ
     ERLKKVFWGV AVVFCVCASW AGSTQLARLT FKTFDAPFTL TWFATNWNFL FFPLYYAGHV
     CKSTEKQSMK QRYRECCRFF GDNGLTLKVF FTKAAPFGVL WTLTNYLYLH AIKKINATDV
     SVLFCCNKSF VFLLSWIVLR DRFMGVRIVA AILAIAGIVM MTYADGFHSH SVIGIALVVG
     SASMSALYKV LFKLLLGSAK FGEAALFLSI LGVFNILFIT CIPVILYFTR VEYWNSFDDI
     PWGNLCGFSI LLLTFNIVLN FGIAVTYPTL MSLGIVLSVP VNAVVDHYTS QIVFNGVRVI
     AIIIIGLGFL LLLLPEEWDV WLIKLLTRLK VRKKEETAES SGDLGTGPQS RSRRARPSFA
     R
//
ID   Q1LZK4_MOUSE            Unreviewed;       298 AA.
AC   Q1LZK4;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   08-MAR-2011, entry version 27.
DE   SubName: Full=4933403O08Rik protein;
DE   SubName: Full=Novel protein (4933403O08Rik);
DE   Flags: Fragment;
GN   Name=4933403O08Rik; Synonyms=RP23-466J17.1;
GN   ORFNames=RP23-466J17.1-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Holt K.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC115851; AAI15852.1; -; mRNA.
DR   EMBL; AL672309; CAM25232.1; -; Genomic_DNA.
DR   EMBL; AC021631; CAM25232.1; JOINED; Genomic_DNA.
DR   IPI; IPI00828521; -.
DR   UniGene; Mm.158538; -.
DR   Ensembl; ENSMUST00000132037; ENSMUSP00000119509; ENSMUSG00000079460.
DR   UCSC; uc009ude.1; mouse.
DR   MGI; MGI:1918280; 4933403O08Rik.
DR   GeneTree; ENSGT00530000067269; -.
DR   OrthoDB; EOG4WSWBC; -.
DR   ArrayExpress; Q1LZK4; -.
DR   Bgee; Q1LZK4; -.
DR   Genevestigator; Q1LZK4; -.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   298 AA;  33763 MW;  329598A7F9C611D4 CRC64;
     RERDRKQKQQ NLTLVTQQPT PEEYSRPGTP GNLWMESPEN AESPGSDDME VARSMYPFRE
     RSIFRRSWAE LLEAPLNSEG LHIIQTEHIH NEENRDMGCN KLTLQEENQV IPLPKDQHFQ
     ALQGPFPLLP ERPKLQRQRS RSLPRNSEVG GQYLNTPEFK GSAEETPFFP RDHNLLTEEN
     IKERHSMEGA WQRVIPSHSG EHFPIMPRFD NSSIQGNFGI PEDNSARPRG NMRIQSNVNT
     IPMVNVGIPI DNPQVLKGNT GVPRGSGFGV YMGNSGRPSG HVVSSPLIEL SKIGEHQL
//
ID   CPNE9_MOUSE             Reviewed;         553 AA.
AC   Q1RLL3; Q8C990;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   08-MAR-2011, entry version 30.
DE   RecName: Full=Copine-9;
DE   AltName: Full=Copine IX;
GN   Name=Cpne9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May function in membrane trafficking. Exhibits calcium-
CC       dependent phospholipid binding properties (By similarity).
CC   -!- SIMILARITY: Belongs to the copine family.
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -!- SIMILARITY: Contains 1 VWFA domain.
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DR   EMBL; AK042692; BAC31336.1; -; mRNA.
DR   EMBL; AK137422; BAE23347.1; -; mRNA.
DR   EMBL; BC115728; AAI15729.1; -; mRNA.
DR   IPI; IPI00313899; -.
DR   RefSeq; NP_733773.2; NM_170673.3.
DR   UniGene; Mm.65597; -.
DR   ProteinModelPortal; Q1RLL3; -.
DR   SMR; Q1RLL3; 13-261, 403-435.
DR   PRIDE; Q1RLL3; -.
DR   Ensembl; ENSMUST00000041203; ENSMUSP00000044416; ENSMUSG00000030270.
DR   GeneID; 211232; -.
DR   KEGG; mmu:211232; -.
DR   CTD; 211232; -.
DR   MGI; MGI:2443052; Cpne9.
DR   eggNOG; roNOG09421; -.
DR   HOGENOM; HBG464786; -.
DR   HOVERGEN; HBG066841; -.
DR   InParanoid; Q1RLL3; -.
DR   OrthoDB; EOG415GD5; -.
DR   NextBio; 373178; -.
DR   ArrayExpress; Q1RLL3; -.
DR   Bgee; Q1RLL3; -.
DR   CleanEx; MM_CPNE9; -.
DR   Genevestigator; Q1RLL3; -.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR010734; Copine.
DR   InterPro; IPR002035; VWF_A.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF07002; Copine; 1.
DR   SMART; SM00239; C2; 2.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS50234; VWFA; 1.
PE   2: Evidence at transcript level;
KW   Repeat.
FT   CHAIN         1    553       Copine-9.
FT                                /FTId=PRO_0000277584.
FT   DOMAIN        1    107       C2 1.
FT   DOMAIN      134    239       C2 2.
FT   DOMAIN      299    500       VWFA.
FT   COMPBIAS    262    268       Poly-Lys.
FT   COMPBIAS    536    541       Poly-Pro.
FT   CONFLICT    542    542       V -> A (in Ref. 1; BAE23347/BAC31336).
SQ   SEQUENCE   553 AA;  61852 MW;  6EB2ED4C79D34B7A CRC64;
     MSLSGASERS VPATKIEITV SCRNLLDLDT FSKSDPMVVL HTQSRASQEW REFGRTEVID
     NTLNPDFVRK FVLDYFFEEK QNLRFDVYNV DSKANISKPK DFLGQAFLAL GEVIGGQGSR
     VERPLTGVPG KKCGTILLTA EELSNCRDIA TMQLCANKLD KKDFFGKSDP FLVFYRSNED
     GTFTICHKTE VVKNTLNPVW QPFSIPVRAL CNGDYDRTVK IDVYDWDRDG SHDFIGEFTT
     SYRELSKAQN QFTVYEVLNP RKKCKKKKYT NSGTVTLLSF SVDSEFTFVD YIKGGTQLNF
     TVAIDFTASN GNPLQPTSLH YMSPYQLSAY AMALKAVGEI IQDYDSDKLF PAYGFGAKLP
     PEGRISHQFP LNNNDEDPNC AGIEGVLESY FQSLRTVQLY GPTYFAPVIN QVARAAAKIS
     DGSQYYVLLI ITDGVISDMT QTKEAIVSAS SLPMSIIIVG VGPAMFEAME ELDGDDVRVS
     SRGRYAERDI VQFVPFRDYV DRSGNQVLSM ARLAKDVLAE IPEQLLSYMR TRDIQPRPPP
     PVSPNPTPAP EQP
//
ID   Q1WWK3_MOUSE            Unreviewed;       222 AA.
AC   Q1WWK3;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   08-MAR-2011, entry version 42.
DE   SubName: Full=Hist1h1b protein;
DE   Flags: Fragment;
GN   Name=Hist1h1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the histone H1/H5 family.
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DR   EMBL; BC114579; AAI14580.1; -; mRNA.
DR   IPI; IPI00230133; -.
DR   RefSeq; NP_064418.1; NM_020034.1.
DR   UniGene; Mm.221314; -.
DR   ProteinModelPortal; Q1WWK3; -.
DR   STRING; Q1WWK3; -.
DR   Ensembl; ENSMUST00000080511; ENSMUSP00000079356; ENSMUSG00000058773.
DR   GeneID; 56702; -.
DR   KEGG; mmu:56702; -.
DR   CTD; 56702; -.
DR   MGI; MGI:1861461; Hist1h1b.
DR   HOVERGEN; HBG009035; -.
DR   InParanoid; Q1WWK3; -.
DR   OMA; TKKAAGG; -.
DR   NextBio; 313147; -.
DR   ArrayExpress; Q1WWK3; -.
DR   Bgee; Q1WWK3; -.
DR   Genevestigator; Q1WWK3; -.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007517; P:muscle organ development; IPI:MGI.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   InterPro; IPR005818; Histone_H1/H5.
DR   InterPro; IPR005819; Histone_H5.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF00538; Linker_histone; 1.
DR   PRINTS; PR00624; HISTONEH5.
DR   SMART; SM00526; H15; 1.
PE   2: Evidence at transcript level;
KW   Chromosome; DNA-binding; Nucleus.
FT   NON_TER       1      1
SQ   SEQUENCE   222 AA;  22445 MW;  769E5A90191756BB CRC64;
     SETAPAETAA PAPVEKSPAK KKTTKKAGAA KRKATGPPVS ELITKAVSAS KERGGVSLPA
     LKKALAAGGY DVEKNNSRIK LGLKSLVSKG TLVQTKGTGA SGSFKLNKKA ASGEAKPKAK
     KTGAAKAKKP AGATPKKPKK TAGAKKTVKK TPKKAKKPAA AGVKKVAKSP KKAKAAAKPK
     KAAKSPAKPK AVKSKASKPK VTKPKTAKPK AAKAKKAVSK KK
//
ID   Q27PY9_MOUSE            Unreviewed;       664 AA.
AC   Q27PY9;
DT   04-APR-2006, integrated into UniProtKB/TrEMBL.
DT   04-APR-2006, sequence version 1.
DT   08-MAR-2011, entry version 30.
DE   SubName: Full=Solute carrier family 8 sodium/calcium exchanger member 1 splicing variant 1.41;
GN   Name=Slc8a1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DDY;
RX   PubMed=17317768; DOI=10.1210/en.2006-1321;
RA   Li J.P., Kajiya H., Okamoto F., Nakao A., Iwamoto T., Okabe K.;
RT   "Three Na+/Ca2+ exchanger (NCX) variants are expressed in mouse
RT   osteoclasts and mediate calcium transport during bone resorption.";
RL   Endocrinology 148:2116-2125(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DDY;
RA   Li J.-P., Kajiya H., Okabe K.;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; DQ388998; ABD46717.1; -; mRNA.
DR   IPI; IPI00268433; -.
DR   UniGene; Mm.265834; -.
DR   ProteinModelPortal; Q27PY9; -.
DR   SMR; Q27PY9; 403-636.
DR   STRING; Q27PY9; -.
DR   PRIDE; Q27PY9; -.
DR   Ensembl; ENSMUST00000071424; ENSMUSP00000071371; ENSMUSG00000054640.
DR   UCSC; uc008drv.1; mouse.
DR   MGI; MGI:107956; Slc8a1.
DR   HOVERGEN; HBG006441; -.
DR   ArrayExpress; Q27PY9; -.
DR   Bgee; Q27PY9; -.
DR   Genevestigator; Q27PY9; -.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; TAS:MGI.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0030315; C:T-tubule; IDA:MGI.
DR   GO; GO:0005432; F:calcium:sodium antiporter activity; IDA:MGI.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   GO; GO:0002026; P:regulation of the force of heart contraction; IMP:MGI.
DR   InterPro; IPR003644; Calx_beta.
DR   InterPro; IPR001623; DnaJ_N.
DR   InterPro; IPR004836; Na_Ca_Ex.
DR   InterPro; IPR002987; NaCa_exhngr1.
DR   InterPro; IPR004837; NaCa_Exmemb.
DR   Pfam; PF03160; Calx-beta; 2.
DR   Pfam; PF01699; Na_Ca_ex; 1.
DR   PRINTS; PR01260; NACAEXCHNGR1.
DR   SMART; SM00237; Calx_beta; 2.
DR   TIGRFAMs; TIGR00845; caca; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
SQ   SEQUENCE   664 AA;  74330 MW;  A9031C2738BC3066 CRC64;
     MLRLSLPPNV SMGFRLVALV ALLFSHVDHI TADTEAETGG NETTECTGSY YCKKGVILPI
     WEPQDPSFGD KIARATVYFV AMVYMFLGVS IIADRFMSSI EVITSQEKEI TIKKPNGETT
     KTTVRIWNET VSNLTLMALG SSAPEILLSV IEVCGHNFTA GDLGPSTIVG SAAFNMFIII
     ALCVYVVPDG ETRKIKHLRV FFVTAAWSIF AYTWLYIILS VSSPGVVEVW EGLLTFFFFP
     ICVVFAWVAD RRLLFYKYVY KRYRAGKQRG MIIEHEGDRP ASKTEIEMDG KVVNSHVDNF
     LDGALVLEVD ERDQDDEEAR REMARILKEL KQKHPEKEIE QLIELANYQV LSQQQKSRAF
     YRIQATRLMT GAGNILKRHA ADQARKAVSM HEVNMEMAEN DPVSKIFFEQ GTYQCLENCG
     TVALTIMRRG GDLSTTVFVD FRTEDGTANA GSDYEFTEGT VIFKPGETQK EIRVGIIDDD
     IFEEDENFLV HLSNVRVSSD VSEDGILESN HASSIACLGS PSTATITIFD DDHAGIFTFE
     EPVTHVSESI GIMEVKVLRT SGARGNVIIP YKTIEGTARG GGEDFEDTCG ELEFQNDEIV
     KTISVKVIDD EEYEKNKTFF IEIGEPRLVE MSEKKGRSLP LEYLTVRNMR KSAVSPLCLR
     NQNG
//
ID   PHAR1_MOUSE             Reviewed;         580 AA.
AC   Q2M3X8; B1B1B5; B1B1B6; B1B1B7; Q80VL9; Q8C873;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   RecName: Full=Phosphatase and actin regulator 1;
GN   Name=Phactr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Corpus striatum;
RX   PubMed=16359841; DOI=10.1016/j.ygeno.2005.10.009;
RA   de Chaldee M., Brochier C., Van de Vel A., Caudy N., Luthi-Carter R.,
RA   Gaillard M.-C., Elalouf J.-M.;
RT   "Capucin: a novel striatal marker down-regulated in rodent models of
RT   Huntington disease.";
RL   Genomics 87:200-207(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   TISSUE=Eye, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-580 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
CC   -!- SUBUNIT: Binds PPP1CA and actin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell junction,
CC       synapse (By similarity). Note=Enriched at synapses (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q2M3X8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q2M3X8-2; Sequence=VSP_018559;
CC       Name=3;
CC         IsoId=Q2M3X8-3; Sequence=VSP_018559, VSP_018560;
CC   -!- SIMILARITY: Belongs to the phosphatase and actin regulator family.
CC   -!- SIMILARITY: Contains 4 RPEL repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH48407.1; Type=Erroneous initiation;
CC       Sequence=AAH61691.1; Type=Erroneous initiation;
CC       Sequence=BAC33272.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AY993932; AAY42814.1; -; mRNA.
DR   EMBL; CT025549; CAO78135.1; -; Genomic_DNA.
DR   EMBL; AC140415; CAO78135.1; JOINED; Genomic_DNA.
DR   EMBL; AC154505; CAO78135.1; JOINED; Genomic_DNA.
DR   EMBL; AC164878; CAO78135.1; JOINED; Genomic_DNA.
DR   EMBL; CT025549; CAO78137.1; -; Genomic_DNA.
DR   EMBL; AC140415; CAO78137.1; JOINED; Genomic_DNA.
DR   EMBL; AC154505; CAO78137.1; JOINED; Genomic_DNA.
DR   EMBL; AC164878; CAO78137.1; JOINED; Genomic_DNA.
DR   EMBL; CT025549; CAO78138.1; -; Genomic_DNA.
DR   EMBL; AC140415; CAO78138.1; JOINED; Genomic_DNA.
DR   EMBL; AC154505; CAO78138.1; JOINED; Genomic_DNA.
DR   EMBL; AC164878; CAO78138.1; JOINED; Genomic_DNA.
DR   EMBL; BC048407; AAH48407.1; ALT_INIT; mRNA.
DR   EMBL; BC061691; AAH61691.1; ALT_INIT; mRNA.
DR   EMBL; AK048208; BAC33272.1; ALT_INIT; mRNA.
DR   IPI; IPI00471281; -.
DR   IPI; IPI00719908; -.
DR   IPI; IPI00757547; -.
DR   RefSeq; NP_001005740.1; NM_001005740.1.
DR   RefSeq; NP_940811.2; NM_198419.3.
DR   UniGene; Mm.160124; -.
DR   STRING; Q2M3X8; -.
DR   PhosphoSite; Q2M3X8; -.
DR   PRIDE; Q2M3X8; -.
DR   Ensembl; ENSMUST00000066928; ENSMUSP00000066663; ENSMUSG00000054728.
DR   Ensembl; ENSMUST00000095844; ENSMUSP00000093527; ENSMUSG00000054728.
DR   Ensembl; ENSMUST00000110161; ENSMUSP00000105790; ENSMUSG00000054728.
DR   GeneID; 218194; -.
DR   KEGG; mmu:218194; -.
DR   UCSC; uc007qfn.1; mouse.
DR   UCSC; uc007qfo.1; mouse.
DR   UCSC; uc007qfq.1; mouse.
DR   CTD; 218194; -.
DR   MGI; MGI:2659021; Phactr1.
DR   eggNOG; roNOG06623; -.
DR   GeneTree; ENSGT00390000004420; -.
DR   HOVERGEN; HBG057352; -.
DR   OrthoDB; EOG4RV2R9; -.
DR   NextBio; 376178; -.
DR   ArrayExpress; Q2M3X8; -.
DR   Bgee; Q2M3X8; -.
DR   CleanEx; MM_PHACTR1; -.
DR   Genevestigator; Q2M3X8; -.
DR   GermOnline; ENSMUSG00000054728; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004018; RPEL_repeat.
DR   Pfam; PF02755; RPEL; 4.
DR   SMART; SM00707; RPEL; 4.
DR   PROSITE; PS51073; RPEL; 4.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Cell junction; Cytoplasm;
KW   Phosphoprotein; Protein phosphatase inhibitor; Repeat; Synapse.
FT   CHAIN         1    580       Phosphatase and actin regulator 1.
FT                                /FTId=PRO_0000235990.
FT   REPEAT      138    163       RPEL 1.
FT   REPEAT      422    447       RPEL 2.
FT   REPEAT      460    485       RPEL 3.
FT   REPEAT      498    523       RPEL 4.
FT   COMPBIAS    395    403       Poly-Glu.
FT   MOD_RES     104    104       Phosphothreonine.
FT   VAR_SEQ       1     34       MDYPKMDYFLDVESAHRLLDVESAQRFFYSQGAQ -> MCV
FT                                SLLLSPPPPFRLSPSPSLHLLLLS (in isoform 2
FT                                and isoform 3).
FT                                /FTId=VSP_018559.
FT   VAR_SEQ     221    221       P -> PVSEESPSASESGVLLSQDPSAKPVLFLPPKKSAAF
FT                                PGDHEETPVKQLSLHKQPPALPPKPTARIANHLT (in
FT                                isoform 3).
FT                                /FTId=VSP_018560.
SQ   SEQUENCE   580 AA;  66286 MW;  367DD2393117EC89 CRC64;
     MDYPKMDYFL DVESAHRLLD VESAQRFFYS QGAQARRATL LLPPTLMAAS SEDDIDRRPI
     RRVRSKSDTP YLAEARISFN LGAAEEVERL AAMRSDSLVP GTHTPPIRRR SKFANLGRIF
     KPWKWRKKKS EKFKHTSAAL ERKISMRQSR EELIKRGVLK EIYDKDGELS ISNEDDSLEN
     GQSLSSSQLS LPALSEMEPV PMPRDPCSYE VLQASDIMDG PDPGAPVKLP CLPVKLSPPL
     PPKKVLICMP VGGPELTLAS YAAQKSSQQA VAQHHHTVLP SQMQHQLQYG SHGQHLPSST
     GTLPMHPSGC RMIDELNKTL AMTMQRLESS EQRVPCSTSY HSSGLHSSDG ITKAGPMGLP
     EIRQVPTVVI ECDDNKENVP HEPDYEDSPC LYGREEEEEE EDEDDDASLY TSSLAMKVCR
     KDSLAIKLSN RPSKRELEEK NILPRQTDEE RLELRQQIGT KLTRRLSQRP TAEELEQRNI
     LKPRNEQEEQ EEKREIKRRL TRKLSQRPTV EELRERKILI RFSDYVEVAD AQDYDRRADK
     PWTRLTAADK AAIRKELNEF KSTEMEVHEL SRHLTRFHRP
//
ID   Q2NL45_MOUSE            Unreviewed;       308 AA.
AC   Q2NL45;
DT   07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   07-FEB-2006, sequence version 1.
DT   08-MAR-2011, entry version 35.
DE   SubName: Full=Olfr915 protein;
DE   Flags: Fragment;
GN   Name=Olfr915;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
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DR   EMBL; BC111098; AAI11099.1; -; mRNA.
DR   IPI; IPI00126515; -.
DR   RefSeq; NP_666996.2; NM_146785.2.
DR   UniGene; Mm.223210; -.
DR   ProteinModelPortal; Q2NL45; -.
DR   GeneID; 258781; -.
DR   KEGG; mmu:258781; -.
DR   CTD; 258781; -.
DR   MGI; MGI:3030749; Olfr915.
DR   HOVERGEN; HBG017625; -.
DR   Genevestigator; Q2NL45; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0004984; F:olfactory receptor activity; IEA:InterPro.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR000725; Olfact_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00245; OLFACTORYR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   G-protein coupled receptor; Membrane; Receptor; Transducer;
KW   Transmembrane.
FT   NON_TER       1      1
SQ   SEQUENCE   308 AA;  34626 MW;  9D1C524F19EC1084 CRC64;
     SENGSSVTEF ILVGLTKDPD LQCPLFVLFL VMYVLTVLGN LSLITLIVLN SHLPTPMYFF
     LFNLSLVDFW YSSVFTPKML MSFISEKNII SYRGCMAQLF FFSFFCISEC YVLTVMAYDR
     YVAICNPLLY NIVMSPKLCL NLILGSYIMA FSGAMAHTGC MLRLTFCDAN TINHYFCDIH
     PLLQLSCTSI YVNELEVFVV IGINIIVPTI TIFISYGFIL SSIFHISSKE GRSKAFSTCS
     SHIIAVSLFF GSGAFMYLKP SSAESMNESK VSSVFYTNTV PLLNPLIYSL RNKDVKIALI
     KTLSKRKC
//
ID   GSK3A_MOUSE             Reviewed;         490 AA.
AC   Q2NL51;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Glycogen synthase kinase-3 alpha;
DE            Short=GSK-3 alpha;
DE            EC=2.7.11.26;
GN   Name=Gsk3a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 227-490.
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH ARRB2.
RX   PubMed=16051150; DOI=10.1016/j.cell.2005.05.012;
RA   Beaulieu J.-M., Sotnikova T.D., Marion S., Lefkowitz R.J.,
RA   Gainetdinov R.R., Caron M.G.;
RT   "An Akt/beta-arrestin 2/PP2A signaling complex mediates dopaminergic
RT   neurotransmission and behavior.";
RL   Cell 122:261-273(2005).
CC   -!- FUNCTION: Implicated in the hormonal control of several regulatory
CC       proteins including glycogen synthase, MYB and the transcription
CC       factor JUN (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + [tau protein] = ADP + [tau protein]
CC       phosphate.
CC   -!- SUBUNIT: Monomer (By similarity). Interacts with ARRB2.
CC   -!- INTERACTION:
CC       P63087-1:Ppp1cc; NbExp=1; IntAct=EBI-1203218, EBI-450267;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. GSK-3 subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AC156992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC111032; AAI11033.1; -; mRNA.
DR   IPI; IPI00648141; -.
DR   RefSeq; NP_001026837.1; NM_001031667.1.
DR   UniGene; Mm.476745; -.
DR   ProteinModelPortal; Q2NL51; -.
DR   SMR; Q2NL51; 99-445.
DR   IntAct; Q2NL51; 1.
DR   STRING; Q2NL51; -.
DR   PhosphoSite; Q2NL51; -.
DR   PRIDE; Q2NL51; -.
DR   Ensembl; ENSMUST00000071739; ENSMUSP00000071654; ENSMUSG00000057177.
DR   GeneID; 606496; -.
DR   KEGG; mmu:606496; -.
DR   CTD; 606496; -.
DR   MGI; MGI:2152453; Gsk3a.
DR   eggNOG; roNOG13291; -.
DR   GeneTree; ENSGT00520000055635; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG014652; -.
DR   InParanoid; Q2NL51; -.
DR   OMA; DQQVEIS; -.
DR   OrthoDB; EOG4WH8KZ; -.
DR   PhylomeDB; Q2NL51; -.
DR   BRENDA; 2.7.11.26; 244.
DR   NextBio; 414454; -.
DR   PMAP-CutDB; Q2NL51; -.
DR   ArrayExpress; Q2NL51; -.
DR   Bgee; Q2NL51; -.
DR   CleanEx; MM_GSK3A; -.
DR   Genevestigator; Q2NL51; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
DR   GO; GO:0050321; F:tau-protein kinase activity; IEA:EC.
DR   GO; GO:0016477; P:cell migration; IGI:MGI.
DR   GO; GO:0071285; P:cellular response to lithium ion; IDA:MGI.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:MGI.
DR   GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    490       Glycogen synthase kinase-3 alpha.
FT                                /FTId=PRO_0000280395.
FT   DOMAIN      119    404       Protein kinase.
FT   NP_BIND     125    133       ATP (By similarity).
FT   COMPBIAS      3     98       Gly-rich.
FT   ACT_SITE    244    244       Proton acceptor (By similarity).
FT   BINDING     148    148       ATP (By similarity).
FT   MOD_RES       2      2       Phosphoserine (By similarity).
FT   MOD_RES      19     19       Phosphothreonine (By similarity).
FT   MOD_RES      20     20       Phosphoserine (By similarity).
FT   MOD_RES      39     39       Phosphoserine (By similarity).
FT   MOD_RES      41     41       Phosphoserine (By similarity).
FT   MOD_RES      63     63       Phosphoserine (By similarity).
FT   MOD_RES      65     65       Phosphoserine (By similarity).
FT   MOD_RES      72     72       Phosphoserine (By similarity).
FT   MOD_RES      77     77       Phosphoserine (By similarity).
FT   MOD_RES      84     84       Phosphothreonine (By similarity).
FT   MOD_RES      97     97       Phosphoserine (By similarity).
FT   MOD_RES     282    282       Phosphoserine (By similarity).
SQ   SEQUENCE   490 AA;  51661 MW;  739CDD86BBFB497B CRC64;
     MSGGGPSGGG PGGSGRARTS SFAEPGGGGG GGGGGPGGSA SGPGGTGGGK ASVGAMGGGV
     GASSSGGGPS GSGGGGSGGP GAGTSFPPPG VKLGRDSGKV TTVVATVGQG PERSQEVAYT
     DIKVIGNGSF GVVYQARLAE TRELVAIKKV LQDKRFKNRE LQIMRKLDHC NIVRLRYFFY
     SSGEKKDELY LNLVLEYVPE TVYRVARHFT KAKLITPIIY IKVYMYQLFR SLAYIHSQGV
     CHRDIKPQNL LVDPDTAVLK LCDFGSAKQL VRGEPNVSYI CSRYYRAPEL IFGATDYTSS
     IDVWSAGCVL AELLLGQPIF PGDSGVDQLV EIIKVLGTPT REQIREMNPN YTEFKFPQIK
     AHPWTKVFKS SKTPPEAIAL CSSLLEYTPS SRLSPLEACA HSFFDELRRL GAQLPNDRPL
     PPLFNFSPGE LSIQPSLNAI LIPPHLRSPA GPASPLTTSY NPSSQALTEA QTGQDWQPSD
     ATTATLASSS
//
ID   PSD3_MOUSE              Reviewed;        1037 AA.
AC   Q2PFD7; Q3TTA1; Q80TN6; Q80UZ7; Q8CEA6;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=PH and SEC7 domain-containing protein 3;
DE   AltName: Full=Exchange factor for ADP-ribosylation factor guanine nucleotide factor 6;
DE   AltName: Full=Pleckstrin homology and SEC7 domain-containing protein 3;
GN   Name=Psd3; Synonyms=Efa6d, Kiaa0942;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16707115; DOI=10.1016/j.brainres.2006.02.058;
RA   Sakagami H., Suzuki H., Kamata A., Owada Y., Fukunaga K., Mayanagi H.,
RA   Kondo H.;
RT   "Distinct spatiotemporal expression of EFA6D, a guanine nucleotide
RT   exchange factor for ARF6, among the EFA6 family in mouse brain.";
RL   Brain Res. 1093:1-11(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-729 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Skin, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 714-1037 (ISOFORM 4).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 823-1037 (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1000; SER-1001 AND
RP   SER-1009, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1009, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1009, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Guanine nucleotide exchange factor for ARF6.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane, postsynaptic density.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q2PFD7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q2PFD7-2; Sequence=VSP_029160;
CC       Name=3;
CC         IsoId=Q2PFD7-3; Sequence=VSP_029157, VSP_029159, VSP_029160;
CC       Name=4;
CC         IsoId=Q2PFD7-4; Sequence=VSP_029161;
CC       Name=5;
CC         IsoId=Q2PFD7-5; Sequence=VSP_029158;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC       liver. Present in brain, with highest levels in olfactory bulb,
CC       cortex, hippocampal pyramidal cell layer and cerebellar granule
CC       cell layer (at protein level).
CC   -!- DEVELOPMENTAL STAGE: Expressed only in spinal cord at E13. At E18
CC       and P0, appears weakly in forebrain. Expression in brain increases
CC       after birth and peaks at P10.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 SEC7 domain.
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DR   EMBL; AB220685; BAE73186.1; -; mRNA.
DR   EMBL; AK028684; BAC26065.1; -; mRNA.
DR   EMBL; AK161498; BAE36424.1; -; mRNA.
DR   EMBL; AK122405; BAC65687.1; -; mRNA.
DR   EMBL; BC042208; AAH42208.1; -; mRNA.
DR   IPI; IPI00407352; -.
DR   IPI; IPI00620507; -.
DR   IPI; IPI00676211; -.
DR   IPI; IPI00874973; -.
DR   IPI; IPI00875485; -.
DR   RefSeq; NP_081902.1; NM_027626.1.
DR   RefSeq; NP_084539.2; NM_030263.5.
DR   RefSeq; NP_808366.2; NM_177698.4.
DR   UniGene; Mm.32525; -.
DR   ProteinModelPortal; Q2PFD7; -.
DR   SMR; Q2PFD7; 546-977.
DR   PhosphoSite; Q2PFD7; -.
DR   PRIDE; Q2PFD7; -.
DR   Ensembl; ENSMUST00000093468; ENSMUSP00000091178; ENSMUSG00000030465.
DR   Ensembl; ENSMUST00000093469; ENSMUSP00000091179; ENSMUSG00000030465.
DR   GeneID; 234353; -.
DR   KEGG; mmu:234353; -.
DR   UCSC; uc009lwa.1; mouse.
DR   CTD; 234353; -.
DR   MGI; MGI:1918215; Psd3.
DR   GeneTree; ENSGT00570000079011; -.
DR   HOGENOM; HBG507097; -.
DR   HOVERGEN; HBG108299; -.
DR   InParanoid; Q2PFD7; -.
DR   OMA; HKTQRAN; -.
DR   OrthoDB; EOG4ZW597; -.
DR   NextBio; 382101; -.
DR   ArrayExpress; Q2PFD7; -.
DR   Bgee; Q2PFD7; -.
DR   CleanEx; MM_PSD3; -.
DR   Genevestigator; Q2PFD7; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IDA:MGI.
DR   GO; GO:0032011; P:ARF protein signal transduction; IC:MGI.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000904; Sec7.
DR   InterPro; IPR023394; SEC7_alpha_orthog.
DR   Gene3D; G3DSA:1.10.1000.11; G3DSA:1.10.1000.11; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF01369; Sec7; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00222; Sec7; 1.
DR   SUPFAM; SSF48425; Sec7; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50190; SEC7; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Coiled coil;
KW   Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Synapse.
FT   CHAIN         1   1037       PH and SEC7 domain-containing protein 3.
FT                                /FTId=PRO_0000309454.
FT   DOMAIN      515    723       SEC7.
FT   DOMAIN      774    887       PH.
FT   COILED      911    941       Potential.
FT   MOD_RES     759    759       Phosphoserine.
FT   MOD_RES    1000   1000       Phosphoserine.
FT   MOD_RES    1001   1001       Phosphoserine.
FT   MOD_RES    1009   1009       Phosphoserine.
FT   VAR_SEQ       1    518       Missing (in isoform 3).
FT                                /FTId=VSP_029157.
FT   VAR_SEQ       1     44       MEGRNAAAEPFVWVNSASAHSQSVAKAKYEFLFGKSEEKTP
FT                                DSS -> MGNCWSYSNLC (in isoform 5).
FT                                /FTId=VSP_029158.
FT   VAR_SEQ     519    530       TRGPQEIAFWGS -> MGIIMCLIYCYC (in isoform
FT                                3).
FT                                /FTId=VSP_029159.
FT   VAR_SEQ     684    684       Missing (in isoform 3 and isoform 2).
FT                                /FTId=VSP_029160.
FT   VAR_SEQ     919    966       Missing (in isoform 4).
FT                                /FTId=VSP_029161.
FT   CONFLICT    190    190       D -> E (in Ref. 2; BAC26065).
SQ   SEQUENCE   1037 AA;  114722 MW;  E6E3C240AC7A61E8 CRC64;
     MEGRNAAAEP FVWVNSASAH SQSVAKAKYE FLFGKSEEKT PDSSDHGGST LLPPTVTNEF
     PEYGTMEEGG EGLRASLDFD AKSPPCRLPG QQAVHLLAGQ DSILNSVTEG PNDAPQCHPQ
     EQSLQPIDSL ISALKATEAR IASGTFQATK VLDKDANFSV YQVDKELSTA SHKPQRAHRT
     FPVGPGKSPD IPLSAEVPTE ENLSLHIQED LSALLPEEAQ AHRSQITNYR RQGPLRVPES
     ACPVSSSSAG SHNPVDRVGA LREQRSDLGR EHPRGYDRGG SMGRQGRIKH VEFQGVEILW
     TGEEAESRHP PERTASPVSK EFAKRPSHSS PACGVCSTST HLTGDVWDET CKAPSERPGT
     SAGTLSPMPL GESGEDDVFL RESKEHLEEN FAIQGDKERI LDQEEHLRGD DDILGPGYTE
     DSTDVYSSQF ETILDNTSLY YSAESLETLY SEPDSYFSFE MPLTPMIQQR IKEGGQFLER
     TSVGGQHDVL SVSADGGIVM GYSAGITNGL HDSANSVYTR GPQEIAFWGS RDRCFAEGKT
     TGVDAGSEMG STDILEKETT ESLSNGTNSN VEAAKRLAKR LYHLDRFKRS DVAKHLGKNN
     EFSKLVAEEY LKFFDFTGMT LDQSLRYFLK AFSLVGETQE RERVLIHFSN RYFSCNPDTI
     TSKDGVHCLT CAMMLLNTDL HGHVNIGKKM TCQEFITNLQ GVNEGGDFSK DLLKALYNSI
     KNEKLEWAVD DEEKKKSPSE GTDEKANGTH PKTISRIGST TNPFLDIPHD PNAAVYKSGF
     LARKIHADMD GKKTPRGKRG WKTFYAVLKG TVLYLQKDEY KPEKSLSDED LKNAVSVHHA
     LASKATDYEK KPNVFKLKTA DWRVLLFQTQ SPEEMQGWIN KINCVAAVFS APPFPAAIGS
     QKKFSRPLLP ATTTKLSQEE QLKSHESKLK QITTELAEHR SYPPDKKVKA KDVDEYKLKD
     HYLEFEKTRY EIYVSVLKEG GKELLTTDGN EPVGLKKSHS SPSLNPDASP VTAKVKRNVS
     ERKDHRPETP GIKQKVT
//
ID   FAT4_MOUSE              Reviewed;        4981 AA.
AC   Q2PZL6; Q68FE0; Q8BM82; Q8CD68;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Protocadherin Fat 4;
DE   AltName: Full=FAT tumor suppressor homolog 4;
DE   AltName: Full=Fat-like cadherin protein FAT-J;
DE   Flags: Precursor;
GN   Name=Fat4; Synonyms=Fatj;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Qi C., Zhu Y.T., Hu L., Zhang Z., Rao S.M., Zhu Y.-J.;
RT   "Identification of Fat4 as the candidate tumor suppressor gene in
RT   breast cancers through random chromosome deletion.";
RL   Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1329-4981 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4473-4981 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2963-4981 (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4878, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=16059920; DOI=10.1002/dvdy.20515;
RA   Rock R., Schrauth S., Gessler M.;
RT   "Expression of mouse dchs1, fjx1, and fat-j suggests conservation of
RT   the planar cell polarity pathway identified in Drosophila.";
RL   Dev. Dyn. 234:747-755(2005).
RN   [6]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=18604206; DOI=10.1038/ng.179;
RA   Saburi S., Hester I., Fischer E., Pontoglio M., Eremina V.,
RA   Gessler M., Quaggin S.E., Harrison R., Mount R., McNeill H.;
RT   "Loss of Fat4 disrupts PCP signaling and oriented cell division and
RT   leads to cystic kidney disease.";
RL   Nat. Genet. 40:1010-1015(2008).
CC   -!- FUNCTION: May function in the regulation of planar cell polarity.
CC       Cadherins are cell-cell interaction molecules (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential). Note=In the kidney, localizes to primary
CC       cilia (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q2PZL6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q2PZL6-2; Sequence=VSP_032339, VSP_032340;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- DISRUPTION PHENOTYPE: Mice die at birth, with pups being runted,
CC       with a curved body axis and curly tails. In the inner ear,
CC       significant disruption in orientation of hair cells in all levels
CC       of the cochlea. Defects in the elongation of the cochlea and of
CC       the neural tube. During kidney development, oriented cell
CC       divisions and tubule elongation are disrupted, leading to cystic
CC       kidney disease.
CC   -!- SIMILARITY: Contains 34 cadherin domains.
CC   -!- SIMILARITY: Contains 6 EGF-like domains.
CC   -!- SIMILARITY: Contains 2 laminin G-like domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC27359.1; Type=Erroneous initiation;
CC       Sequence=BAC28751.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; DQ286572; ABB88946.1; -; mRNA.
DR   EMBL; AK031348; BAC27359.1; ALT_INIT; mRNA.
DR   EMBL; AK034552; BAC28751.1; ALT_INIT; mRNA.
DR   EMBL; BC079887; AAH79887.1; -; mRNA.
DR   IPI; IPI00228716; -.
DR   IPI; IPI00889310; -.
DR   UniGene; Mm.316210; -.
DR   HSSP; P15116; 1NCJ.
DR   ProteinModelPortal; Q2PZL6; -.
DR   SMR; Q2PZL6; 48-1415, 2170-2250, 2584-3613, 3803-4379, 4390-4495.
DR   PhosphoSite; Q2PZL6; -.
DR   PRIDE; Q2PZL6; -.
DR   Ensembl; ENSMUST00000061260; ENSMUSP00000061836; ENSMUSG00000046743.
DR   UCSC; uc008pbf.1; mouse.
DR   MGI; MGI:3045256; Fat4.
DR   eggNOG; roNOG06788; -.
DR   GeneTree; ENSGT00600000084230; -.
DR   HOGENOM; HBG355938; -.
DR   HOVERGEN; HBG104800; -.
DR   InParanoid; Q2PZL6; -.
DR   OrthoDB; EOG4HDSSK; -.
DR   ArrayExpress; Q2PZL6; -.
DR   Bgee; Q2PZL6; -.
DR   CleanEx; MM_FAT4; -.
DR   Genevestigator; Q2PZL6; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   InterPro; IPR006209; EGF.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR001881; EGF_Ca-bd.
DR   InterPro; IPR013091; EGF_Ca-bd_2.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR012680; Laminin_G_2.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 34.
DR   Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 3.
DR   Pfam; PF00028; Cadherin; 32.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF02210; Laminin_G_2; 2.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 34.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00282; LamG; 2.
DR   SUPFAM; SSF49313; Cadherin; 35.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS00232; CADHERIN_1; 22.
DR   PROSITE; PS50268; CADHERIN_2; 34.
DR   PROSITE; PS00022; EGF_1; 7.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 6.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell adhesion; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Phosphoprotein; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     42       Potential.
FT   CHAIN        43   4981       Protocadherin Fat 4.
FT                                /FTId=PRO_0000324638.
FT   TOPO_DOM     43   4505       Extracellular (Potential).
FT   TRANSMEM   4506   4526       Helical; (Potential).
FT   TOPO_DOM   4527   4981       Cytoplasmic (Potential).
FT   DOMAIN       44    135       Cadherin 1.
FT   DOMAIN      136    250       Cadherin 2.
FT   DOMAIN      251    353       Cadherin 3.
FT   DOMAIN      359    475       Cadherin 4.
FT   DOMAIN      476    582       Cadherin 5.
FT   DOMAIN      584    689       Cadherin 6.
FT   DOMAIN      690    793       Cadherin 7.
FT   DOMAIN      794    893       Cadherin 8.
FT   DOMAIN      894    996       Cadherin 9.
FT   DOMAIN      997   1100       Cadherin 10.
FT   DOMAIN     1101   1210       Cadherin 11.
FT   DOMAIN     1211   1315       Cadherin 12.
FT   DOMAIN     1316   1420       Cadherin 13.
FT   DOMAIN     1421   1529       Cadherin 14.
FT   DOMAIN     1529   1629       Cadherin 15.
FT   DOMAIN     1630   1740       Cadherin 16.
FT   DOMAIN     1741   1841       Cadherin 17.
FT   DOMAIN     1842   1944       Cadherin 18.
FT   DOMAIN     1945   2051       Cadherin 19.
FT   DOMAIN     2051   2154       Cadherin 20.
FT   DOMAIN     2155   2259       Cadherin 21.
FT   DOMAIN     2260   2364       Cadherin 22.
FT   DOMAIN     2365   2468       Cadherin 23.
FT   DOMAIN     2469   2569       Cadherin 24.
FT   DOMAIN     2570   2671       Cadherin 25.
FT   DOMAIN     2672   2775       Cadherin 26.
FT   DOMAIN     2775   2874       Cadherin 27.
FT   DOMAIN     2875   2985       Cadherin 28.
FT   DOMAIN     2986   3091       Cadherin 29.
FT   DOMAIN     3092   3196       Cadherin 30.
FT   DOMAIN     3197   3300       Cadherin 31.
FT   DOMAIN     3301   3406       Cadherin 32.
FT   DOMAIN     3407   3512       Cadherin 33.
FT   DOMAIN     3511   3622       Cadherin 34.
FT   DOMAIN     3804   3862       EGF-like 1.
FT   DOMAIN     3864   3900       EGF-like 2; calcium-binding (Potential).
FT   DOMAIN     3902   3938       EGF-like 3; calcium-binding (Potential).
FT   DOMAIN     3940   3976       EGF-like 4.
FT   DOMAIN     3977   4161       Laminin G-like 1.
FT   DOMAIN     4164   4200       EGF-like 5.
FT   DOMAIN     4219   4399       Laminin G-like 2.
FT   DOMAIN     4427   4464       EGF-like 6.
FT   MOD_RES    4878   4878       Phosphoserine.
FT   CARBOHYD     84     84       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    237    237       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    393    393       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    416    416       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    435    435       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    483    483       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    551    551       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    615    615       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    676    676       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    721    721       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    825    825       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    880    880       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    948    948       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1085   1085       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1101   1101       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1104   1104       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1225   1225       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1296   1296       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1389   1389       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1514   1514       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1828   1828       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1899   1899       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1967   1967       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2119   2119       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2387   2387       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2432   2432       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2923   2923       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2939   2939       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3038   3038       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3142   3142       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3219   3219       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3394   3394       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3479   3479       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3708   3708       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3760   3760       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   4019   4019       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   4269   4269       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   4314   4314       N-linked (GlcNAc...) (Potential).
FT   DISULFID   3808   3819       By similarity.
FT   DISULFID   3813   3850       By similarity.
FT   DISULFID   3852   3861       By similarity.
FT   DISULFID   3868   3879       By similarity.
FT   DISULFID   3873   3888       By similarity.
FT   DISULFID   3890   3899       By similarity.
FT   DISULFID   3906   3917       By similarity.
FT   DISULFID   3911   3926       By similarity.
FT   DISULFID   3928   3937       By similarity.
FT   DISULFID   3944   3955       By similarity.
FT   DISULFID   3949   3964       By similarity.
FT   DISULFID   3966   3975       By similarity.
FT   DISULFID   4135   4161       By similarity.
FT   DISULFID   4168   4179       By similarity.
FT   DISULFID   4173   4188       By similarity.
FT   DISULFID   4190   4199       By similarity.
FT   DISULFID   4366   4399       By similarity.
FT   DISULFID   4431   4442       By similarity.
FT   DISULFID   4436   4452       By similarity.
FT   DISULFID   4454   4463       By similarity.
FT   VAR_SEQ    1975   1978       VNSQ -> MSFL (in isoform 2).
FT                                /FTId=VSP_032339.
FT   VAR_SEQ    1979   4981       Missing (in isoform 2).
FT                                /FTId=VSP_032340.
SQ   SEQUENCE   4981 AA;  540343 MW;  5AC7C40F5C25A500 CRC64;
     MNLAANRAPG RRRLPLPSPS LCQLLRVWGL LSLLPGSARV QAAEQRQVFQ VMEEQPPGTL
     VGTIPTRPGF TYRLSESHAL FAINSSTGAL YTTATIDRES LPSDVVNLVV LSSSPTYPTE
     VRVLVRDLND NAPVFPDPSI VVTFKEDSGS GRQVILDTAT DSDIGSNGVD HHSYRIVSGN
     EAGRFRLDIT LNPSGEGAFL HLVSKGGLDR EVTPQYQLLV EVEDKGEPKR RGYLQVNVTV
     QDINDNPPVF GSSHYQAGVP EDAVVGSSVL QVAAADADEG TNADIRYRLQ DEGTPFQMDP
     ETGLITVREP LDFEARRQYS LTVQATDRGV PSLTGRAEAF IQLLDVNDND PVVKFRYFPA
     TSRYASVDEN AQVGTVVALL TVTDADSPAA NGNISVQILG GNEQRHFEVQ RSKVPNLSLI
     KVASALDRER IPSYNLTVSV SDNSGAPPTA EVQARSSVAS LVIFVNDIND HPPVFEQQVY
     RVNLSEEVPP GSYVSGVSAT DGDSGLNANL RYSIVSGNGL GWFHISEHSG LVTTSAAGGL
     DRELASQIVL NISARDQGVH PKVSYAQLVV TVLDVNDEKP VFSQPEGYEV SVVENAPTGT
     ELLVLGATDR DLGDNGTVRF SLQEAENDQR LFRLDPVSGR LSTASSLDRE EQAFYCLSIL
     ATDLGSPPQS STAQVNVSLL DINDNSPVFY PVQYFAHIQE NEPGGSYVTT VSATDPDMGP
     NGTVKYSISA GDRSRFQIHA KSGVISTKMA LDREEKTAYQ LQVVATDGGN LQSPNQAIVT
     VTVLDTQDNP PVFSQAAYSF VVFENVALGY HVGSVSATTM DLNANISYLI TTGDQRGMFA
     MNPVTGQLTT ASVIDREEQS FYQLKIVASG GAVTGDTVVN ITVKDLNDNA PHFLQAVESI
     NAVENWQAGH SIFQAKAVDP DEGVNGRVLY SLKQNPKNLF TINEQNGNIS LLGALDVHAG
     SYQVEIVASD MGVPQLSSSI LLTVYVHDVN DNPPVFDQIS YEVTLSESEP VNSRFFKVQA
     SDKDSGANGE IAYTITDGNN GDAFGIFPDG QLYIKSELDR ELQDRYVLLV VASDRAVEPL
     SATVNVTVLL EDVNDNRPLF NSTNYTFYFE EEQRAGSFVG KVSAVDKDFG PNGEVRYAFE
     VTQPNFELHA VTGEITSTHK FDRESLMRRR GTAVFSFTVT AMDRGLPQPL KDQATVHVYM
     KDINDNAPKF LKDFYQATVS ETATNLTQVL RVSASDVDEG SNGLIHYSIL KGNEERQFAI
     DSFSGQVTLV GKLDYEATSA YSLLIQAVDS GAIPLNSTCT LSIDILDEND NTPSFPKSTL
     FVDVLENMRI GELVSSVTAT DSDSGVNADL HYTITGSNNH GTFSISPNTG SIFLAKKLDF
     ETQSLYKLNI TAKDQGRPPR SSTMSVVIQV RDFNDNPPSF PPGDIFKSIV ENIPLGTSVI
     SVTAHDPDAD INGQLSYAII QQMPRGNHFS IDEVKGTIYT NAEIDREFAN LFELTVKAND
     QAVPIETRRY ALKNVTILVT DLNDNVPMFI SQNALAADPS AMIGSVLTTI MAADPDEGAN
     GEVEYEILNG DTDTFTVDRY SGDLRVASAL VPSQLIYNLI VSATDLGPER RKSTTELTVI
     LQGLDGPVFT QTKYITILKE GEPIGTNVIS IEAASPRGSE APVEYYIVSV RCEEKTVGRL
     FTIGRQTGVI QTAAILDREQ GACLYLVDVY AIEKSSAFPR TQRAEVEITL QDINDNPPVF
     PTDTLDLTVE ENIGDGSKIM QLTAMDADEG ANALVTYALI SGADDSFRID PESGDLIATK
     RLDREHRSKY SLLVRADDGL QSSDMRINIT ISDVNDHTPR FSRPVYSFDI PEDTTPGSLV
     AAILATDDDS GVNGEISYVV EEDDGDGVFF LNLVTGVFNL TRALDYETQQ YYILTVRAED
     GGGQSTTIRA YFNILDVNDN PPVFSMSSYS TSLMENLPLG STVLVFNVTD ADDGVNSQLS
     YSIASGDSLG QFAVDKHGVL KTLKALDRES QSFYNLVIQV HDLPQPPTSR FTSTAQVSII
     LLDVNDNPPM FLSPKLTYIP ENTPIDTVVF KAQATDPDSG PNSYIEYTLL NPSGNKFSIG
     TIDGEVHLTG ELDREEVSNY SLTVVATDKG QPPLSSSTEV VVMVLDINDN NPVFAQAMYR
     VQIKENILTG TDIIQVSAAD NDEGTNGQVR YGIVGGNTHQ EFRIDSVTGA ITVAKSLDRE
     TTPAYTLTVQ ATDRGSSPRT DSCTVAITLL DMNDFVPVFE LSPYSVNVPE NLGTLPRAIL
     QVVARDDDQG PNSQLSYVLL GGNEDNAFVL TASGELRVTQ SLDREARDHF VLVVTAADAG
     SPALTGTGTI NIIVDDINDN VPTFANNMYL TSIAEDARTG TDVLLVNASD ADAAANAVIS
     YSIIGGNSQF TINPSTGQII TSALLDRETK DNYTLVVVAS DAGSPESLSS STSVLVTITD
     VNDNPPRFQH HPYVTHIPSP TPPGSFVFAV TVTDADIGSN SELHYSLSGR NSEKFHIDPL
     RGAIMAAGPL SGASEVTFSV HVKDGGSFPK TDSTTVTVRF ANKADFPKVR AKEQTFMFPE
     NQPVGTLVTT ITGSSLRGET LSYYIASGNL GDTFQIDPLT GQVSISQPLD FEKIQKYVVW
     IEARDGGFPP FSSYEKLDIT VLDINDNAPT FEEDPFVSEI LENLSPRKIL TVSATDKDSG
     PNGQLDYEIV NGNQESSFTI NHATGEIRSI RPLDREKISH YELTVKSSDK GSPSQSTSVK
     VIISILDEND NAPRFSQIFS AYVSENSPLG YTVTRVTTSD EDIGINAISR YSIVDTSLPF
     TINPNTGDIV ISRPLNREDT DRYRIRVSAH DSGWTVSTDV TIFVTDINDN TPRFSRPSYY
     LDCPELPELG SRVTQVSATD PDEGSNGQVF YFIKSQSEYF RINATTGEIF NKQVLKYQNV
     SGFSNVNINR HSFIVTASDR GNPSLLSETT VTINTVDSND NPPQFLQNKY FTPVTKNVKV
     GTKLIKVTAV DDKDFGLNSE VEYFVSDGNH LGKFKLDNDT GWISIASSLV SDLNQNFLIR
     VTAKDKGNPP LSSQAVVHIT VTEENYHTPE FSQNHISATI PESHSIGSVV RTVSARDRDT
     AMNGLISYNI ISGNEEGIFA INSSTGVVTL AKALDYEMSS KHEMTISATD GGWVARTGYC
     SLTVSVIDVN DNSPVFVPDE FFPTVMENAP SGTTVIHLNA TDADSGANAV IAYTVQSSDS
     DLFVIDPNMG VITTQGFLDF ETKQSYHLTV KAFNVPDEEK CSFATVDIQL KGTNEYVPRF
     VSKLYYFEVS EAASRGTAVG EVFASDRDMG ADGEVHYLIF GNSRKKGFQI NKMTGQIYVS
     GLLDREKEER VSLKVLAKNF GNIRGADIDE VTVNITVLDA NDPPVFSLST YRVQISEGVP
     IGTHVTFVSA FDSDSIPSWS RFSYFIGSGN ENGAFSINPQ TGQITVTSGL DRESLPVYNL
     TVLAVDSGTP SATGSASLVV TLEDINDNGP VLTVSEGEVL ENKRPGTLVM TLQSTDPDLP
     PNQGPFNYYL LSTGPATNYF SLSTAGVLST TREIDREQIA DFYLSVVTRD SGAPQMSSTG
     TVHITVLDQN DNPSQSRTVE IFVNYYGNLF PGGTLGSVKP QDPDVLDSFH CSLTSGVTSL
     FSIPAGSCDL SSQPRSTDGT FDLTVVSSDG VHSTVTNNIR VFFAGFSNAT IDNSILLRVG
     VPTVKDFLTN HYLHFLRIAS SQLTGLGTAV QLYAAYEENN RTFLLAAVKR NNNQYVNPSG
     VATFFESIKE ILLRQSGVKV ESVDHDPCIH GPCQNGGSCL RRLAVGSALK IQESLPVIIV
     ANEPLQPSQC KCVPGYAGSW CEVDIDECLP APCHNGGTCH NLVGGFSCSC PEGFTGRACE
     RDINECLPSP CKHGAVCQNF PGGFNCVCKT GYTGKMCESS VNYCECNPCF NGGSCQSGVE
     SYYCHCPFGV FGKHCELNSY GFEELSYMEF PSLDPNNNYI YVKFATIKSH ALLLYNYDNQ
     TGERAEFLAL EIAEERLRFS YNLGSGTYKL TTMKKVSDGQ FHTVIARRAG MAASLTVDSC
     SENQEPGYCT VSNVAVSDDW TLDVQPNRVT VGGIRSLEPI LQRRGHVESH DFVGCVMEFA
     VNGRPLEPSQ ALAAQGILDQ CPRLEGTCAR NPCQHGGTCV DFWSWQQCQC MEGLTGKYCE
     KSVTPDTALS LEGKGRLDYH MSQSEKREYL LTQSIRDTTL EPFGVNSLEV KFRTRSENGI
     LIHIQESSNY TTVKIKNGKV HFTSDAGVAG KVERIIPEAY IADGHWHTFR ISKNGSITVL
     SVDRIHNRDI VHPTQDFGGI EVLSMSLGGI PPNQAHRDTQ TGFNGCIASV LYGGESLPFS
     GKHSLASISK TDPSVKIGCR GPNICASNPC WGDLLCINQW YAYKCVPPGD CASHPCQNGG
     SCEPGLLSGY TCSCPESHTG RTCETVVACL GVLCPQGKVC KAGSPGGHVC VQSQGPDEIS
     LPLWAVPAIV GSCATALALL VLSLILCNQC RGKMPKNPKE EKKPKEKKKK GSENVAFDDP
     DNIPPYGDDL AVRKQPEGNP KPDIIERENP YLIFDETDIP HNSETIPSAP LASPEQEIEH
     YDIDNASSIA PSDADIIQHY KQFRSHTPKF SIQRHSPLGF ARQSPMPLGA SSLTYQPSSY
     GQGLRTSSLS HSACPTPNPL SRHSPAPFSK PSAFYRNSPA RELHLPLRDG GTLEMHGDPC
     QPGMFNYATR LGRRSKSPQA MASHGSRPGS RLKQPIAQIP LESSPPVGLS IEEVERLNTP
     RPRNPSICSA DHGRSSSEED CRRPLSRTRN PADGIPAPES SSDSDSHDSF TCSEMEYDRE
     KPVVYTSRMP KLSQVNESDA DDEDNYGARL KPRRYHGRRA EGGPVGTPAA ASGAADSTLK
     LGQQAGNFNW DNLLNWGPGF GHYVDVFKDL ASLPEKAAGN EEGKSGAAKP AAKDGEAEQY
     V
//
ID   Q2Q7P0_MOUSE            Unreviewed;       591 AA.
AC   Q2Q7P0;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   SubName: Full=ENH1;
GN   Name=Pdlim5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CD; TISSUE=Brain;
RX   PubMed=16880269; DOI=10.1083/jcb.200511109;
RA   Camarata T., Bimber B., Kulisz A., Chew T.L., Yeung J., Simon H.G.;
RT   "LMP4 regulates Tbx5 protein subcellular localization and activity.";
RL   J. Cell Biol. 174:339-348(2006).
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 3 LIM zinc-binding domains.
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DR   EMBL; DQ177283; ABB03726.1; -; mRNA.
DR   IPI; IPI00653381; -.
DR   UniGene; Mm.117709; -.
DR   ProteinModelPortal; Q2Q7P0; -.
DR   SMR; Q2Q7P0; 11-94, 395-589.
DR   STRING; Q2Q7P0; -.
DR   Ensembl; ENSMUST00000029941; ENSMUSP00000029941; ENSMUSG00000028273.
DR   MGI; MGI:1927489; Pdlim5.
DR   eggNOG; roNOG12232; -.
DR   HOVERGEN; HBG051478; -.
DR   InParanoid; Q2Q7P0; -.
DR   ArrayExpress; Q2Q7P0; -.
DR   Bgee; Q2Q7P0; -.
DR   Genevestigator; Q2Q7P0; -.
DR   GO; GO:0030018; C:Z disc; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR001781; Znf_LIM.
DR   Gene3D; G3DSA:2.10.110.10; Znf_LIM; 3.
DR   Pfam; PF00412; LIM; 3.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00132; LIM; 3.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR   PROSITE; PS50106; PDZ; 1.
PE   2: Evidence at transcript level;
KW   LIM domain; Metal-binding; Zinc.
SQ   SEQUENCE   591 AA;  63300 MW;  9CCA5EC85F42AF9C CRC64;
     MSNYSVSLVG PAPWGFRLQG GKDFNMPLTI SSLKDGGKAS QAHVRIGDVV LSIDGISAQG
     MTHLEAQNKI KACTGSLNMT LQRASAAAKS EPVSVQKGEP KEVVKPVPIT SPAVSKVTST
     TNMAYNKAPR PFGSVSSPKV TSIPSPSSAF TPAHAATSSH ASPTPVAAAT PLHLSASGLH
     VSANLSADQC SSPPNTGKPA VNVPRQPTVT SVCSESAQEL AEGQRRGSQG DIKQQNGPPR
     KHIVERNTEF YHIPTHSDAS KKRLIEDTED WRPRTGTTQS RSFRILAQIT GTEHLTESEY
     DNTKKANSTQ EPSQQPASSG ASPLSASEGP ESPGSSRPAV AGLRSAAAFK PVGSTSVKSP
     SWQRPNQAAP STGRISNNAR SSGTGASVGP PQPSDQDTLV QRAEHIPAGK RTPMCAHCNQ
     VIRGPFLVAL GKSWHPEEFN CAHCKNTMAY IGFVEEKGAL YCELCYERSF APECGRCQRK
     ILGEVINALK QTWHVSCFVC VACGKPIRNN VFHLEDGEPY CETDYYALFG TICRGCEFPI
     EAGDMFLEAL GYTWHDTCFV CSVCCESLEG QTFFSKKDKP LCKKHAHSVN F
//
ID   P4K2A_MOUSE             Reviewed;         479 AA.
AC   Q2TBE6;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   RecName: Full=Phosphatidylinositol 4-kinase type 2-alpha;
DE            EC=2.7.1.67;
DE   AltName: Full=Phosphatidylinositol 4-kinase type II-alpha;
GN   Name=Pi4k2a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-51 AND SER-462,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-51, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Together with PI4K2B and the type III PI4Ks (PIK4CA and
CC       PIK4CB) it contributes to the overall PI4-kinase activity of the
CC       cell. The phosphorylation of phosphatidylinositol (PI) to PI4P is
CC       the first committed step in the generation of phosphatidylinositol
CC       4,5-bisphosphate (PIP2), a precursor of the second messenger
CC       inositol 1,4,5-trisphosphate (InsP3). Contributes to the
CC       production of InsP3 in stimulated cells (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol = ADP +
CC       1-phosphatidyl-1D-myo-inositol 4-phosphate.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane (By
CC       similarity). Membrane raft (By similarity). Note=Found in
CC       subdomains of the plasma membrane termed non-caveolar membrane
CC       rafts (By similarity).
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. Type II PI4K
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 PI3K/PI4K domain.
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DR   EMBL; BC110363; AAI10364.1; -; mRNA.
DR   IPI; IPI00121277; -.
DR   RefSeq; NP_663476.1; NM_145501.2.
DR   UniGene; Mm.117037; -.
DR   ProteinModelPortal; Q2TBE6; -.
DR   PhosphoSite; Q2TBE6; -.
DR   PRIDE; Q2TBE6; -.
DR   Ensembl; ENSMUST00000066778; ENSMUSP00000069284; ENSMUSG00000025178.
DR   GeneID; 84095; -.
DR   KEGG; mmu:84095; -.
DR   UCSC; uc008hnf.1; mouse.
DR   CTD; 84095; -.
DR   MGI; MGI:1934031; Pi4k2a.
DR   eggNOG; roNOG09606; -.
DR   GeneTree; ENSGT00390000010434; -.
DR   HOGENOM; HBG714361; -.
DR   HOVERGEN; HBG059542; -.
DR   InParanoid; Q2TBE6; -.
DR   OMA; QRFHRIG; -.
DR   OrthoDB; EOG4VT5X4; -.
DR   PhylomeDB; Q2TBE6; -.
DR   BRENDA; 2.7.1.67; 244.
DR   NextBio; 350886; -.
DR   ArrayExpress; Q2TBE6; -.
DR   Bgee; Q2TBE6; -.
DR   CleanEx; MM_PI4K2A; -.
DR   Genevestigator; Q2TBE6; -.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR   GO; GO:0004430; F:1-phosphatidylinositol 4-kinase activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR000403; PI3/4_kinase_cat.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   PROSITE; PS00915; PI3_4_KINASE_1; FALSE_NEG.
DR   PROSITE; PS00916; PI3_4_KINASE_2; FALSE_NEG.
DR   PROSITE; PS50290; PI3_4_KINASE_3; FALSE_NEG.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Transferase.
FT   CHAIN         1    479       Phosphatidylinositol 4-kinase type 2-
FT                                alpha.
FT                                /FTId=PRO_0000285159.
FT   DOMAIN      133    438       PI3K/PI4K.
FT   COMPBIAS     39     42       Poly-Ala.
FT   MOD_RES       5      5       Phosphoserine (By similarity).
FT   MOD_RES       9      9       Phosphoserine (By similarity).
FT   MOD_RES      44     44       Phosphoserine (By similarity).
FT   MOD_RES      47     47       Phosphoserine.
FT   MOD_RES      51     51       Phosphoserine.
FT   MOD_RES     462    462       Phosphoserine.
FT   MOD_RES     464    464       Phosphoserine (By similarity).
SQ   SEQUENCE   479 AA;  54258 MW;  1D7429AA7BF2918B CRC64;
     MDETSPLVSP ERAQPPEYTF PSGSGAHFPQ VPGGAVRVAA AAGSGPSPPC SPGHDRERQP
     LLDRARGAAA QGQTHTVAVQ AQALAAQAAV AAHAVQTHRE RNDFPEDPEF EVVVRQAEVA
     IECSIYPERI YQGSSGSYFV KDSQGRIVAV FKPKNEEPYG HLNPKWTKWL QKLCCPCCFG
     RDCLVLNQGY LSEAGASLVD QKLELNIVPR TKVVYLASET FNYSAIDRVK SRGKRLALEK
     VPKVGQRFNR IGLPPKVGSF QLFVEGYKDA DYWLRRFEAE PLPENTNRQL LLQFERLVVL
     DYIIRNTDRG NDNWLIKYDC PMDNSSCRDT DWVMVREPVI KVAAIDNGLA FPLKHPDSWR
     AYPFYWAWLP QAKVPFSQEI KDLILPKISD PNFIKDLEED LYELFKRDPG FDRGQFHKQI
     AVMRGQILNL TQALKDNKSP LHLVQMPPVI VETARSHQRS ASESYTQSFQ SRKPFFSWW
//
ID   Q2TJI6_MOUSE            Unreviewed;       353 AA.
AC   Q2TJI6;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   05-OCT-2010, entry version 21.
DE   SubName: Full=Protocadherin 7 isoform 4;
DE   Flags: Fragment;
GN   Name=Pcdh7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   PubMed=15905963; DOI=10.1007/s00018-005-5021-7;
RA   Vanhalst K., Kools P., Staes K., van Roy F., Redies C.;
RT   "delta-Protocadherins: a gene family expressed differentially in the
RT   mouse brain.";
RL   Cell. Mol. Life Sci. 62:1247-1259(2005).
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DR   EMBL; AY861419; AAX56109.1; -; mRNA.
DR   IPI; IPI00399971; -.
DR   UniGene; Mm.332387; -.
DR   UniGene; Mm.397491; -.
DR   STRING; Q2TJI6; -.
DR   Ensembl; ENSMUST00000094783; ENSMUSP00000092376; ENSMUSG00000029108.
DR   MGI; MGI:1860487; Pcdh7.
DR   HOVERGEN; HBG083852; -.
DR   ArrayExpress; Q2TJI6; -.
DR   Bgee; Q2TJI6; -.
DR   Genevestigator; Q2TJI6; -.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR013585; Protocadherin.
DR   Pfam; PF08374; Protocadherin; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   353 AA;  39043 MW;  BD98F3BAE7ECEC7B CRC64;
     YCRSKNKNGY EAGKKDHEDF FTPQQHDKSK KPKKDKKNKK SKQPLYSSIV TVEASKPNGQ
     RYDSVNEKLS DSPSMGRYRS VNGGPGSPDL ARHYKSSSPL PTVQLHPQSP TAGKKHQAVQ
     DLPPANTFVG AGDNISIGSD HCSEYSCQTS NKYSKQPFRR VTFSVVSQPQ DPHQGSLQSC
     YDSGLEESET PSSKSSSGPR LGALPLPEDN YERTTPDGSV GEAEHMENDS RPLPDVALTG
     KCTRECDEYG HSDSCWMPVR TSPERKKSQP KLSTFMPVDE RGSQEKLANG EAAIMGDRNR
     NLLNKKLTSS YETFSAASFS KNEEANPEDI PLTKTGEYKP SPVNTLTRRE VYL
//
ID   Q2TJI9_MOUSE            Unreviewed;       363 AA.
AC   Q2TJI9;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   08-FEB-2011, entry version 28.
DE   SubName: Full=Protocadherin 1 isoform 2;
DE   Flags: Fragment;
GN   Name=Pcdh1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c;
RX   PubMed=15905963; DOI=10.1007/s00018-005-5021-7;
RA   Vanhalst K., Kools P., Staes K., van Roy F., Redies C.;
RT   "delta-Protocadherins: a gene family expressed differentially in the
RT   mouse brain.";
RL   Cell. Mol. Life Sci. 62:1247-1259(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
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DR   EMBL; AY861416; AAX56106.1; -; mRNA.
DR   IPI; IPI00719927; -.
DR   UniGene; Mm.36560; -.
DR   UniGene; Mm.458851; -.
DR   STRING; Q2TJI9; -.
DR   PRIDE; Q2TJI9; -.
DR   Ensembl; ENSMUST00000115599; ENSMUSP00000111262; ENSMUSG00000051375.
DR   Ensembl; ENSMUST00000161701; ENSMUSP00000125576; ENSMUSG00000051375.
DR   UCSC; uc008ert.1; mouse.
DR   MGI; MGI:104692; Pcdh1.
DR   GeneTree; ENSGT00570000078935; -.
DR   HOVERGEN; HBG083852; -.
DR   ArrayExpress; Q2TJI9; -.
DR   Bgee; Q2TJI9; -.
DR   Genevestigator; Q2TJI9; -.
DR   GO; GO:0005911; C:cell-cell junction; TAS:MGI.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0016339; P:calcium-dependent cell-cell adhesion; TAS:MGI.
DR   GO; GO:0007156; P:homophilic cell adhesion; TAS:MGI.
DR   InterPro; IPR013585; Protocadherin.
DR   Pfam; PF08374; Protocadherin; 1.
PE   1: Evidence at protein level;
FT   NON_TER       1      1
SQ   SEQUENCE   363 AA;  39439 MW;  4A2251D23ECDC8CE CRC64;
     YCRQREAKSG YQAGKKETKD LYAPKPSGKA AKGSKSKGKK SKSPKPVKPV EDEDDTGLQK
     SLKFNLMSDA PGDSPRIHLP LNYPPGSPDL GRHYRSNSPL PSIQLQPQSP SASKKHQVVQ
     DLPPANTFVG TGDTTSTGSE QYSDYSYRTN PPKYPSKQLP HRRVTFSATS QAQELQDPSQ
     HSYYDSGLEE SETPSSKSSS GPRLGPLALP EDHYERTTPD GSIGEMEHPE NDLRPLPDVA
     MTGTCTRECS EFGHSDTCWM PGQSSPSRRT KSSALKLSTF VPYQDRGGQE PAGAGSPSPP
     EDRNTKTAPV RLLPSYSAFS HSSHDSCKDS ATLEEIPLTQ TSDFPPTATP ASAQTAAKRE
     IYL
//
ID   Q2VEB3_MOUSE            Unreviewed;      2064 AA.
AC   Q2VEB3;
DT   10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   10-JAN-2006, sequence version 1.
DT   05-OCT-2010, entry version 26.
DE   SubName: Full=A-kinase anchoring protein beta;
GN   Name=Akap6; Synonyms=Akapbeta;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Black Swiss;
RX   PubMed=16337591; DOI=10.1016/j.molcel.2005.10.013;
RA   Carlisle Michel J.J., Townley I.K., Dodge-Kafka K.L., Zhang F.,
RA   Kapiloff M.S., Scott J.D.;
RT   "Spatial restriction of PDK1 activation cascades by anchoring to
RT   mAKAPalpha.";
RL   Mol. Cell 20:661-672(2005).
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DR   EMBL; DQ233646; ABB60212.1; -; mRNA.
DR   IPI; IPI00663880; -.
DR   UniGene; Mm.310822; -.
DR   ProteinModelPortal; Q2VEB3; -.
DR   STRING; Q2VEB3; -.
DR   Ensembl; ENSMUST00000110722; ENSMUSP00000106350; ENSMUSG00000061603.
DR   MGI; MGI:3050566; Akap6.
DR   eggNOG; roNOG04507; -.
DR   HOVERGEN; HBG050480; -.
DR   InParanoid; Q2VEB3; -.
DR   ArrayExpress; Q2VEB3; -.
DR   Bgee; Q2VEB3; -.
DR   Genevestigator; Q2VEB3; -.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   SMART; SM00150; SPEC; 3.
PE   2: Evidence at transcript level;
KW   Kinase; Transferase.
SQ   SEQUENCE   2064 AA;  227180 MW;  88AF6F704A3E1738 CRC64;
     MTTSQAKTKS FDSWSYSEME KEFPELIRSV GLLTVATEPV PSSCGAANED SSQVILSEDH
     RGGHEEDGAL EPGEQLGSTL ETSSLGDTLT NAAEHPPETA NQDSTSSPQL GAKKSQPGPC
     EMMTPKRSIR DCFNYNEDSP TQPTLPKRGL FLKETLKNER RGSDGKGRVV DLKPELSRST
     PSLVEPPDRS KLCLVLQSSY PSSPSAASQS YECLHKVGIG NLENIVRSHI KEISSSLGRL
     TDCHKEKPRL KKPHKTLAEV SLCKIPKRGT GSGKQSENTR SSVVPTMVSP GAPKATARPA
     TDSASTTSGD TCHQRNRGGK LPAQSKASSS SPCSHSSESS LGSDNIKSPL PLLSKSQKGS
     PPAPCHATQN GQVVEAWYGS DEYLALPSHL KQTEVLALKL ENLTKLLPQK PRGETIQDID
     DWELSEMNSD SEIYPTYHIK KKHTRLGTVS PSSSSDIASS LGESIESGPL SDILSDEDLC
     MPLSGMKKFT DEKSERPSSS EKNESHSATK SALIQKLMKD IQHQDNYEAI WERIEVGFVN
     KLDEFIQWLN EAMETTENWT PPKAETDSLR LYLETHLSFK LNVDSHCALK EAVEEEGHQL
     LELIASHKAG LKDMLKMIAS QWKELQRQIK RQHSWILRAL DTIKAEILAT DVSVEDEEGT
     GSPKAEAQLC YLEAQRDAVE QMSLKLYSEQ YTSGSKRKEE FADMSKAHSV GSNGLLDFDS
     EYQELWDWLI DMESLVMDSH DLMMSEEQQQ HLYKRYSVEM SIRHLKKTEL LSKVEALKKG
     GLSLPNDILE KVDSINEKWE LLGKTLREKI QDTMAGHSGS GPRDLLSPES GSLVRQLEVR
     IKELKRWLRD TELFIFNSCL RQEKEGTSAE KQLQYFKSLC HEIKQRRRGV ASILRLCQHL
     LDDRDTCNLN ADHQPMQLII VNLERRWEAI VMQAVQWQTR LRKKMGKESE TLNVIDPGLM
     DLNGMSEDAL EWDETDISNK LISVHEESND LDQDLEPMVP TVKLEETHHK DSGYEEEAGD
     CGGSQYTSNI TAPSSPHIYQ VYSLHNVEFH EDSHTQFLKS SPKFTGTVQP TVLTKSLSKD
     SSFSSTKSLP DLLGGSSLVR PYSCQSGDLS QNSGSESGIV SEGDNEMPTN SDMSLFSMVD
     GSPSNPETQH LDPQMGDAAN VLEQKFKDEG ECIKLSSVSQ ASVSPVGCVN GKAGDLNSIT
     KHTTDCLGDE LQGKHEVFTF YDYSYLQGSK LKFPMIMKQP QSEKAHLEDP LLRGFYFDKK
     SCKPKHQTSE SQPDAPLHEK ILASAPHEMG RSSYKSSDIE KALTGIQNAR QLSLLSRSSS
     VESLSPGGDL FGLGIFKNGS DSLQRSTSLE SWLTSYKSNE DLFSCHSSGD ISVSSGSVGE
     LSKRTLDLLN RLENIQSPSE QKIKRSVSDI TLQSSSQKMS FSGQMSLDVA SSINEDSPAS
     LTELSSSDEL SLCSEDIVLH KNKVPESNAS FRKRLNRSVA DESDVNVSMI VNVSCTSACT
     DDEDDSDLLS SSTLTLTEEE LCLKDEDDDS SIATDDEIYE ESNLMSGLDY IKNELQTWIR
     PKLSLSREKK RPSVTDEIKV NKDGGSTERA NPSDTLDIEA LLNCSIKRLS ENNGNGKNPP
     RTHDLGTKGE NKKNTYDVTK DPHVADMENG NVESTPEREK EKPEIPEASA NLASNVKKIS
     ESKHDEYEAL MDGSDDSSVT GKEFGPPNDR HPPQIGADPQ HPERGDCTSV QNSCSGLLLE
     TGGGSRQDSD GLKSLSNDAP SVARNAAGCC LLEQNETEES ASISSSTSCC NCKPDVFHQK
     DDEDCSVHDF VKEIIDMAST ALKSKSQPES EVAAPTSLTQ IKEKVLEHSH RPIHLRKGDF
     YSYLSLSSHD SDCGEVTNYI DEKSNTPLPP DTVDSGLDDK EDVDCFFEAC VEDEPADEEA
     RLSSALPNES EVQDEAAKPE QMTASSSVFR DETDTVPLSG LSPQKGADDA KEGDGASHTS
     QGCVESAEPT TPPGKAKREG SSRKQSVSGT PEENAASAKP KIQAFSLNAK QPKGKAALYP
     SPQTLTCKEK LVSFHEDRHS NMHR
//
ID   EAF6_MOUSE              Reviewed;         191 AA.
AC   Q2VPQ9; B1ASC6; Q9D7J5;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   08-MAR-2011, entry version 38.
DE   RecName: Full=Chromatin modification-related protein MEAF6;
DE            Short=MYST/Esa1-associated factor 6;
DE   AltName: Full=Esa1-associated factor 6 homolog;
DE            Short=Protein EAF6 homolog;
GN   Name=Meaf6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Jaw, and Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex
CC       which is involved in transcriptional activation of select genes
CC       principally by acetylation of nucleosomal histone H4 and H2A. This
CC       modification may both alter nucleosome - DNA interactions and
CC       promote interaction of the modified histones with other proteins
CC       which positively regulate transcription. Component of the HBO1
CC       complex which has a histone H4-specific acetyltransferase
CC       activity, a reduced activity toward histone H3 and is responsible
CC       for the bulk of histone H4 acetylation in vivo. Component of the
CC       MOZ/MORF complex which has a histone H3 acetyltransferase activity
CC       (By similarity).
CC   -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex
CC       which contains the catalytic subunit KAT5 and the subunits EP400,
CC       TRRAP, BRD8, EPC1, DMAP1, RUVBL1, RUVBL2, ING3, actin, ACTL6A,
CC       MORF4L1, MORF4L2, MRGBP, YEATS4, VPS72 and MEAF6. Component of the
CC       HBO1 complex composed at least of ING4 or ING5, MYST2/HBO1, MEAF6,
CC       and one of PHF15, PHF16 and PHF17. Component of the MOZ/MORF
CC       complex composed at least of ING5, MYST3/MOZ, MYST4/MORF, MEAF6
CC       and one of BRPF1, BRD1/BRPF2 and BRPF3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q2VPQ9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q2VPQ9-2; Sequence=VSP_022452;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the EAF6 family.
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DR   EMBL; AK009177; BAB26123.1; -; mRNA.
DR   EMBL; AL626775; CAM20901.1; -; Genomic_DNA.
DR   EMBL; BC108404; AAI08405.1; -; mRNA.
DR   IPI; IPI00110388; -.
DR   IPI; IPI00648451; -.
DR   RefSeq; NP_081586.1; NM_027310.3.
DR   UniGene; Mm.291214; -.
DR   STRING; Q2VPQ9; -.
DR   PhosphoSite; Q2VPQ9; -.
DR   PRIDE; Q2VPQ9; -.
DR   Ensembl; ENSMUST00000055213; ENSMUSP00000053543; ENSMUSG00000028863.
DR   GeneID; 70088; -.
DR   KEGG; mmu:70088; -.
DR   UCSC; uc008urs.1; mouse.
DR   UCSC; uc008uru.1; mouse.
DR   CTD; 70088; -.
DR   MGI; MGI:1917338; Meaf6.
DR   eggNOG; roNOG16761; -.
DR   GeneTree; ENSGT00390000015257; -.
DR   OrthoDB; EOG4CRM1D; -.
DR   ArrayExpress; Q2VPQ9; -.
DR   Bgee; Q2VPQ9; -.
DR   CleanEx; MM_2310005N01RIK; -.
DR   Genevestigator; Q2VPQ9; -.
DR   GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
DR   GO; GO:0044154; P:histone H3-K14 acetylation; ISS:UniProtKB.
DR   GO; GO:0043983; P:histone H4-K12 acetylation; ISS:UniProtKB.
DR   GO; GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
DR   GO; GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR015418; Hist_AcTrfase_NuA4_cplx.
DR   Pfam; PF09340; NuA4; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Activator; Alternative splicing; Chromatin regulator;
KW   Coiled coil; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    191       Chromatin modification-related protein
FT                                MEAF6.
FT                                /FTId=PRO_0000272610.
FT   COILED       11     47       Potential.
FT   MOD_RES      69     69       N6-acetyllysine (By similarity).
FT   MOD_RES      74     74       N6-acetyllysine (By similarity).
FT   MOD_RES      91     91       N6-acetyllysine (By similarity).
FT   MOD_RES     118    118       Phosphoserine (By similarity).
FT   MOD_RES     120    120       Phosphothreonine (By similarity).
FT   MOD_RES     122    122       Phosphoserine (By similarity).
FT   MOD_RES     146    146       Phosphoserine (By similarity).
FT   VAR_SEQ     179    191       IDLKLNKKPRADY -> MNVSPQTGWHQLHL (in
FT                                isoform 2).
FT                                /FTId=VSP_022452.
SQ   SEQUENCE   191 AA;  21649 MW;  4B9EDC2812CFF1FD CRC64;
     MAMHNKTAPP QIPDTRRELA ELVKRKQELA ETLANLERQI YAFEGSYLED TQMYGNIIRG
     WDRYLTNQKN SNSKNDRRNR KFKEAERLFS KSSVTSAAAV SALAGVQDQL IEKREPGSGT
     ESDTSPDFHN QENEPAQEDP EDLDGSVQGV KPQKAASSTS SGSHHSSHKK RKNKNRHRID
     LKLNKKPRAD Y
//
ID   LRFN1_MOUSE             Reviewed;         766 AA.
AC   Q2WF71; Q460M4; Q8C1V9; Q99KT6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Leucine-rich repeat and fibronectin type III domain-containing protein 1;
DE   AltName: Full=Synaptic adhesion-like molecule 2;
DE   AltName: Full=Synaptic differentiation-enhancing molecule 1;
DE   Flags: Precursor;
GN   Name=Lrfn1; Synonyms=Salm2, Semo1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
RP   DLG4, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, GLYCOSYLATION,
RP   SUBCELLULAR LOCATION, AND TOPOLOGY.
RC   STRAIN=Swiss Webster;
RX   PubMed=16828986; DOI=10.1016/j.gene.2006.05.014;
RA   Morimura N., Inoue T., Katayama K., Aruga J.;
RT   "Comparative analysis of structure, expression and PSD95-binding
RT   capacity of Lrfn, a novel family of neuronal transmembrane proteins.";
RL   Gene 380:72-83(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c;
RX   PubMed=16495444; DOI=10.1523/JNEUROSCI.3799-05.2006;
RA   Wang C.Y., Chang K., Petralia R.S., Wang Y.X., Seabold G.K.,
RA   Wenthold R.J.;
RT   "A novel family of adhesion-like molecules that interacts with the
RT   NMDA receptor.";
RL   J. Neurosci. 26:2174-2183(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16630835; DOI=10.1016/j.neuron.2006.04.005;
RA   Ko J., Kim S., Chung H.S., Kim K., Han K., Kim H., Jun H.,
RA   Kaang B.-K., Kim E.;
RT   "SALM synaptic cell adhesion-like molecules regulate the
RT   differentiation of excitatory synapses.";
RL   Neuron 50:233-245(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   INTERACTION WITH LRFN1; LRFN2; LRFN3; LRFN4 AND LRFN5, AND MUTAGENESIS
RP   OF 760-GLU--VAL-766.
RX   PubMed=18227064; DOI=10.1074/jbc.M709456200;
RA   Seabold G.K., Wang P.Y., Chang K., Wang C.Y., Wang Y.X.,
RA   Petralia R.S., Wenthold R.J.;
RT   "The SALM family of adhesion-like molecules forms heteromeric and
RT   homomeric complexes.";
RL   J. Biol. Chem. 283:8395-8405(2008).
RN   [7]
RP   FUNCTION, AND MUTAGENESIS OF 760-GLU--VAL-766.
RX   PubMed=18585462; DOI=10.1016/j.mcn.2008.05.019;
RA   Wang P.Y., Seabold G.K., Wenthold R.J.;
RT   "Synaptic adhesion-like molecules (SALMs) promote neurite outgrowth.";
RL   Mol. Cell. Neurosci. 39:83-94(2008).
CC   -!- FUNCTION: Promotes neurite outgrowth in hippocampal neurons.
CC       Involved in the regulation and maintenance of excitatory synapses.
CC       Induces the clustering of excitatory postsynaptic proteins,
CC       including DLG4, DLGAP1, GRIA1 and GRIN1.
CC   -!- SUBUNIT: Can form heteromeric complexes with LRFN2, LRFN3, LRFN4
CC       and LRFN5. Forms homomeric complexes, but not across cell
CC       junctions. Interacts with DLG4. Interacts also with DLG1, DLG2,
CC       and DLG3 (By similarity). Interacts with 2 AMPA receptor subunits
CC       GRIA1 and GRIA2 and NMDA receptor subunit GRIN1.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity). Cell junction, synapse (By similarity).
CC       Cell junction, synapse, postsynaptic cell membrane, postsynaptic
CC       density (By similarity). Note=Detected in excitatory, but not
CC       inhibitory, synaptic plasma membrane (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q2WF71-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q2WF71-2; Sequence=VSP_033618, VSP_033619;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q2WF71-3; Sequence=VSP_033617;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in the brain, with a
CC       weak, but broad expression in the cerebral cortex and diencephalic
CC       nuclei. Also detected in other parts of the central nervous
CC       system, including the olfactory bulb, pons, cerebellum, and
CC       medulla oblongata, as well as in the peripheral nervous system,
CC       such as the ganglia of cranial nerves and the dorsal root ganglion
CC       during gestation.
CC   -!- DEVELOPMENTAL STAGE: Expression starts around 10.5 dpc. At 11.5
CC       dpc, broadly expressed in the telencephalic and diencephalic
CC       vesicles. This pattern of expression continues until 17.5 dpc.
CC   -!- DOMAIN: The PDZ-binding motif is required for neurite outgrowth
CC       promotion. This motif is also involved in DLG1-, DLG3- and DLG4-
CC       binding (By similarity).
CC   -!- PTM: Glycosylated.
CC   -!- SIMILARITY: Belongs to the LRFN family.
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC   -!- SIMILARITY: Contains 1 Ig-like (immunoglobulin-like) domain.
CC   -!- SIMILARITY: Contains 7 LRR (leucine-rich) repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC41123.1; Type=Frameshift; Positions=440;
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DR   EMBL; AB243740; BAE53711.1; -; mRNA.
DR   EMBL; DQ070870; AAZ20639.1; -; mRNA.
DR   EMBL; DQ314497; ABC40967.1; -; mRNA.
DR   EMBL; AK090175; BAC41123.1; ALT_FRAME; mRNA.
DR   EMBL; BC004018; AAH04018.1; -; mRNA.
DR   IPI; IPI00468602; -.
DR   IPI; IPI00855061; -.
DR   IPI; IPI00895406; -.
DR   RefSeq; NP_001135393.1; NM_001141921.1.
DR   RefSeq; NP_085039.2; NM_030562.2.
DR   UniGene; Mm.39201; -.
DR   HSSP; P21809; 2FT3.
DR   ProteinModelPortal; Q2WF71; -.
DR   SMR; Q2WF71; 34-391, 421-503.
DR   IntAct; Q2WF71; 1.
DR   STRING; Q2WF71; -.
DR   PhosphoSite; Q2WF71; -.
DR   PRIDE; Q2WF71; -.
DR   Ensembl; ENSMUST00000055110; ENSMUSP00000057645; ENSMUSG00000030600.
DR   Ensembl; ENSMUST00000108288; ENSMUSP00000103923; ENSMUSG00000030600.
DR   GeneID; 80749; -.
DR   KEGG; mmu:80749; -.
DR   UCSC; uc009fzc.1; mouse.
DR   CTD; 80749; -.
DR   MGI; MGI:2136810; Lrfn1.
DR   eggNOG; maNOG08035; -.
DR   GeneTree; ENSGT00600000084152; -.
DR   HOGENOM; HBG444166; -.
DR   HOVERGEN; HBG052352; -.
DR   InParanoid; Q2WF71; -.
DR   OMA; PRVSHVC; -.
DR   OrthoDB; EOG4TMR1K; -.
DR   NextBio; 350107; -.
DR   ArrayExpress; Q2WF71; -.
DR   Bgee; Q2WF71; -.
DR   Genevestigator; Q2WF71; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF07679; I-set; 1.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00369; LRR_TYP; 1.
DR   SMART; SM00082; LRRCT; 1.
DR   SUPFAM; SSF49265; FN_III-like; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51450; LRR; 6.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Disulfide bond;
KW   Glycoprotein; Immunoglobulin domain; Leucine-rich repeat; Membrane;
KW   Postsynaptic cell membrane; Repeat; Signal; Synapse; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     31       Potential.
FT   CHAIN        32    766       Leucine-rich repeat and fibronectin type
FT                                III domain-containing protein 1.
FT                                /FTId=PRO_0000334146.
FT   TOPO_DOM     32    536       Extracellular (Potential).
FT   TRANSMEM    537    557       Helical; (Potential).
FT   TOPO_DOM    558    766       Cytoplasmic (Potential).
FT   REPEAT       64     87       LRR 1.
FT   REPEAT       88    111       LRR 2.
FT   REPEAT      112    135       LRR 3.
FT   REPEAT      136    159       LRR 4.
FT   REPEAT      161    184       LRR 5.
FT   REPEAT      185    208       LRR 6.
FT   REPEAT      209    233       LRR 7.
FT   DOMAIN      299    386       Ig-like.
FT   DOMAIN      421    512       Fibronectin type-III.
FT   MOTIF       763    766       PDZ-binding.
FT   CARBOHYD     87     87       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    343    343       N-linked (GlcNAc...) (Potential).
FT   DISULFID    321    370       By similarity.
FT   VAR_SEQ     469    492       RMIPSTSQTFLVNDLAAGRAYDLC -> SSSCPGTHYVDQD
FT                                GLEIRVPLASA (in isoform 2).
FT                                /FTId=VSP_033618.
FT   VAR_SEQ     470    766       Missing (in isoform 3).
FT                                /FTId=VSP_033617.
FT   VAR_SEQ     493    766       Missing (in isoform 2).
FT                                /FTId=VSP_033619.
FT   MUTAGEN     760    766       Missing: Decreased promotion of neurite
FT                                outgrowth. No effect on homomeric
FT                                interactions.
FT   CONFLICT      9      9       G -> R (in Ref. 5; AAH04018).
FT   CONFLICT     31     31       G -> S (in Ref. 5; AAH04018).
FT   CONFLICT     87     87       N -> D (in Ref. 2; AAZ20639).
FT   CONFLICT    408    408       S -> F (in Ref. 4; BAC41123).
FT   CONFLICT    423    424       TS -> AT (in Ref. 5; AAH04018).
SQ   SEQUENCE   766 AA;  81945 MW;  316FE5D5BE48D3CE CRC64;
     MAPGPFSSGL FSPPPAALPF LLLLWAGASR GQPCPGRCIC QNVAPTLTML CAKTGLLFVP
     PAIDRRVVEL RLTDNFIAAV RRRDFANMTS LVHLTLSRNT IGQVAAGAFA DLRALRALHL
     DSNRLAEVRG DQLRGLGNLR HLILGNNQIR KVESAAFDAF LSTVEDLDLS YNNLEALPWE
     AVGQMVNLNT LTLDHNLIDH IAEGTFVQLH KLVRLDMTSN RLHKLPPDGL FLRSQGGGPK
     PPTPLTVSFG GNPLHCNCEL LWLRRLTRED DLETCATPEH LTDRYFWSIP EEEFLCEPPL
     ITRQAGGRAL VVEGQAVSLR CRAVGDPEPV VHWVAPDGRL LGNSSRTRVR GDGTLDVTIT
     TLRDSGTFTC IASNAAGEAT APVEVCVVPL PLMAPPPAAP PPLTEPGSSD IATPGRPGAN
     DSTSERRLVA AELTSSSVLI RWPAQRPVPG IRMYQVQYNS SADDSLVYRM IPSTSQTFLV
     NDLAAGRAYD LCVLAVYDDG ATALPATRVV GCVQFTTAGD PAPCRPLRAH FLGGTMIIAI
     GGVIVASVLV FIVLLMIRYK VYGDGDSRRI KGTSRTPPRV SHVCSQTNGA GAQQASAPPA
     PDRYEALREV AVPAAIEAKA MEAEATSTEL EVVLGRSLGG SATSLCLLPS EETSGEESRA
     MTGPRRSRSG ALGPPTSAPP TLALVPGGAP ARPRPQQRYS FDGDYGALFQ SHSYPRRARR
     TKRHRSTPHL DGAGGGAAGE DGDLGLGSAR ARLAFTSTEW MLESTV
//
ID   MSTO1_MOUSE             Reviewed;         556 AA.
AC   Q2YDW2; Q3TJ50; Q3TLZ1; Q3TQV9; Q922H6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   08-FEB-2011, entry version 42.
DE   RecName: Full=Protein misato homolog 1;
GN   Name=Msto1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Egg, Mammary gland, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Involved in the regulation of mitochondrial distribution
CC       and morphology (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q2YDW2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q2YDW2-2; Sequence=VSP_028057;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the misato family.
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DR   EMBL; AK163280; BAE37273.1; -; mRNA.
DR   EMBL; AK166236; BAE38651.1; -; mRNA.
DR   EMBL; AK167586; BAE39645.1; -; mRNA.
DR   EMBL; BC008103; AAH08103.1; -; mRNA.
DR   EMBL; BC108354; AAI08355.1; -; mRNA.
DR   IPI; IPI00123010; -.
DR   IPI; IPI00654224; -.
DR   RefSeq; NP_659147.2; NM_144898.2.
DR   UniGene; Mm.126870; -.
DR   UniGene; Mm.440405; -.
DR   ProteinModelPortal; Q2YDW2; -.
DR   PhosphoSite; Q2YDW2; -.
DR   PRIDE; Q2YDW2; -.
DR   Ensembl; ENSMUST00000087075; ENSMUSP00000084309; ENSMUSG00000068922.
DR   Ensembl; ENSMUST00000090941; ENSMUSP00000088459; ENSMUSG00000068922.
DR   GeneID; 229524; -.
DR   KEGG; mmu:229524; -.
DR   CTD; 229524; -.
DR   MGI; MGI:2385175; Msto1.
DR   eggNOG; roNOG16155; -.
DR   GeneTree; ENSGT00530000064067; -.
DR   HOVERGEN; HBG108151; -.
DR   NextBio; 379483; -.
DR   ArrayExpress; Q2YDW2; -.
DR   Bgee; Q2YDW2; -.
DR   CleanEx; MM_MSTO1; -.
DR   Genevestigator; Q2YDW2; -.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0043234; C:protein complex; IEA:InterPro.
DR   GO; GO:0048311; P:mitochondrion distribution; ISS:UniProtKB.
DR   GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR   InterPro; IPR019605; Misato_II_myosin-like.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   Gene3D; G3DSA:3.40.50.1440; Tubulin_FtsZ; 2.
DR   Pfam; PF10644; Misat_Myo_SegII; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   SUPFAM; SSF52490; Tubulin_FtsZ; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane.
FT   CHAIN         1    556       Protein misato homolog 1.
FT                                /FTId=PRO_0000304628.
FT   VAR_SEQ     364    475       Missing (in isoform 2).
FT                                /FTId=VSP_028057.
FT   CONFLICT     23     23       H -> D (in Ref. 1; BAE37273).
FT   CONFLICT    106    106       E -> D (in Ref. 1; BAE37273/BAE39645).
FT   CONFLICT    109    109       H -> Q (in Ref. 1; BAE37273/BAE39645 and
FT                                2; AAH08103).
FT   CONFLICT    228    228       G -> S (in Ref. 1; BAE38651).
FT   CONFLICT    365    365       V -> A (in Ref. 1; BAE38651).
FT   CONFLICT    553    553       S -> T (in Ref. 1; BAE38651).
SQ   SEQUENCE   556 AA;  61230 MW;  F7611F673290C3CC CRC64;
     MAGGAREVLT LQLGHFAGFV GAHWWNQQDA ALGRMAEDEE SPGELCPDVL YRTGRTLHGQ
     ETYTPRLILM DLKGSLNTLK EEGNLYRDRQ LEAAVAWQGK LSTHREDAHP KNPNLQGLLS
     AEGVRSSDGA WRAKLIQNIQ NGKENSIKVW SDFLRVHLHP RSICVIHKYH HDGETGRLEA
     FGQGESVLKE PRYLEELEDR LHFYVEECDY LQGFQLLCDL HDGFSGVGAK TAELLQDEYA
     GRGVLTWGLL PGPYSLGEPQ KNIYRLLNTA FGLVHLTGYS SFVCPLSLGG NLGLRPKPPV
     NFPSLHYDAT LPFHCSAILA TALDTVTVPY RLRSSMVTMA HLADVLSFSG KKVVTAEAII
     PFPLVRGQSL PDILTQLGEA TPWTSLSACG DSAGHRCFAQ SVVLRGIDRA SHTSKLNPGT
     PLPSALHACA SGEEVLAQYL QQQHPRVLSS SHLLLTPCKV APPYPHFFSS FSQKGLAMDS
     TPKGAAVQSI PVFGALRSTS SLHRTLGDLA EELSRLDLRR WASFMDAGVE QDDMEEMLHE
     LHRLAQCYQE GDSLSN
//
ID   S39A7_MOUSE             Reviewed;         476 AA.
AC   Q31125; Q3TVU6; Q9Z1W1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2001, sequence version 2.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Zinc transporter SLC39A7;
DE   AltName: Full=Histidine-rich membrane protein Ke4;
DE   AltName: Full=Solute carrier family 39 member 7;
GN   Name=Slc39a7; Synonyms=H2-Ke4, Hke4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=90097821; PubMed=2294398;
RA   St Jacques B., Han T.-H., Macmurray A., Shin H.-S.;
RT   "A putative transmembrane protein with histidine-rich charge clusters
RT   encoded in the H-2K/tw5 region of mice.";
RL   Mol. Cell. Biol. 10:138-145(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129/SvJ;
RA   Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L.,
RA   Hall J., Lasky S., Hood L.;
RT   "Sequence of the mouse major histocompatibility complex class II
RT   region.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Osteoclast;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-317, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Heart;
RX   PubMed=17451654; DOI=10.1016/j.bbrc.2007.04.015;
RA   Jeon H.B., Choi E.S., Yoon J.H., Hwang J.H., Chang J.W., Lee E.K.,
RA   Choi H.W., Park Z.-Y., Yoo Y.J.;
RT   "A proteomics approach to identify the ubiquitinated proteins in mouse
RT   heart.";
RL   Biochem. Biophys. Res. Commun. 357:731-736(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Probable).
CC   -!- TISSUE SPECIFICITY: Expressed abundantly in embryonic carcinoma
CC       cells, but weakly in adult tissues.
CC   -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC       KE4/Catsup subfamily.
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DR   EMBL; M32010; AAA37767.1; -; mRNA.
DR   EMBL; AF100956; AAC69903.1; -; Genomic_DNA.
DR   EMBL; AK159968; BAE35522.1; -; mRNA.
DR   IPI; IPI00118834; -.
DR   PIR; I49714; I49714.
DR   RefSeq; NP_001071177.1; NM_001077709.1.
DR   RefSeq; NP_032228.2; NM_008202.2.
DR   UniGene; Mm.18556; -.
DR   ProteinModelPortal; Q31125; -.
DR   IntAct; Q31125; 4.
DR   STRING; Q31125; -.
DR   PhosphoSite; Q31125; -.
DR   PRIDE; Q31125; -.
DR   Ensembl; ENSMUST00000025186; ENSMUSP00000025186; ENSMUSG00000024327.
DR   GeneID; 14977; -.
DR   KEGG; mmu:14977; -.
DR   UCSC; uc008cav.1; mouse.
DR   CTD; 14977; -.
DR   MGI; MGI:95909; Slc39a7.
DR   GeneTree; ENSGT00550000074174; -.
DR   HOGENOM; HBG715717; -.
DR   HOVERGEN; HBG001037; -.
DR   InParanoid; Q31125; -.
DR   OMA; DLAHNFT; -.
DR   OrthoDB; EOG46DM3M; -.
DR   PhylomeDB; Q31125; -.
DR   NextBio; 287346; -.
DR   ArrayExpress; Q31125; -.
DR   Bgee; Q31125; -.
DR   Genevestigator; Q31125; -.
DR   GermOnline; ENSMUSG00000024327; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046873; F:metal ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0006829; P:zinc ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR003689; ZIP.
DR   Pfam; PF02535; Zip; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Ion transport; Isopeptide bond; Membrane;
KW   Phosphoprotein; Transmembrane; Transmembrane helix; Transport;
KW   Ubl conjugation; Zinc; Zinc transport.
FT   CHAIN         1    476       Zinc transporter SLC39A7.
FT                                /FTId=PRO_0000213689.
FT   TRANSMEM      7     27       Helical; (Potential).
FT   TRANSMEM    146    166       Helical; (Potential).
FT   TRANSMEM    177    197       Helical; (Potential).
FT   TRANSMEM    222    242       Helical; (Potential).
FT   TRANSMEM    393    413       Helical; (Potential).
FT   TRANSMEM    417    437       Helical; (Potential).
FT   COMPBIAS     27    136       His-rich.
FT   COMPBIAS    252    274       His-rich.
FT   MOD_RES     283    283       Phosphoserine (By similarity).
FT   CARBOHYD    337    337       N-linked (GlcNAc...) (Potential).
FT   CROSSLNK    317    317       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CONFLICT    208    208       A -> T (in Ref. 3; BAE35522).
FT   CONFLICT    367    367       V -> L (in Ref. 1; AAA37767).
FT   CONFLICT    403    476       ACALLTEGGAVDSDVAGGAGPGWVLPFTAGGFIYVATVSVL
FT                                PELLREASPLQSLLEVLGLLGGVAMMVLIAHLE -> RVPF
FT                                SPREGQWTVTWQVVQVLAGSCHSLQADLST (in Ref.
FT                                1).
SQ   SEQUENCE   476 AA;  50657 MW;  48214438BE44919B CRC64;
     MTMGLRAPHW VAVGLLTWAA LGLLVAGHEG HGDLHKDVEE DFHGHSHGHS HEDFHHGHSH
     GHSHEDFHHG HGHTHESIWH GHAHSHDHGH SREELHHGHS HGHSHDSLHH GGHGHAHREH
     SHGTSREAGA PGIKHHLDTV TLWAYALGAT VLISAAPFFV LFLIPVESNS PRHRSLLQIL
     LSFASGGLLG DAFLHLIPHA LEPHSHHAPE QPGHGHSHSG QGPILSVGLW VLSGIVAFLV
     VEKFVRHVKG GHGHSHGHGD RHAHGDSHTH GDRHECSSKE KPSTEEEKEV GGLRKRRGGN
     TGPRDGPVKP QSPEEEKAGS DLRVSGYLNL AADLAHNFTD GLAIGASFRG GRGLGILTTM
     TVLLHEVPHE VGDFAILVQS GCSKKQAMRL QLVTAIGALA GTACALLTEG GAVDSDVAGG
     AGPGWVLPFT AGGFIYVATV SVLPELLREA SPLQSLLEVL GLLGGVAMMV LIAHLE
//
ID   CK087_MOUSE             Reviewed;         199 AA.
AC   Q32M26; Q8CC42;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   30-NOV-2010, entry version 37.
DE   RecName: Full=Uncharacterized protein C11orf87 homolog;
DE   Flags: Precursor;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC28535.1; Type=Frameshift; Positions=115;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK033979; BAC28535.1; ALT_FRAME; mRNA.
DR   EMBL; BC109328; AAI09329.1; -; mRNA.
DR   IPI; IPI00876200; -.
DR   RefSeq; NP_849237.2; NM_178906.4.
DR   UniGene; Mm.335160; -.
DR   ProteinModelPortal; Q32M26; -.
DR   PRIDE; Q32M26; -.
DR   GeneID; 330941; -.
DR   KEGG; mmu:330941; -.
DR   UCSC; uc009ply.1; mouse.
DR   MGI; MGI:2143099; AI593442.
DR   HOVERGEN; HBG098354; -.
DR   NextBio; 399633; -.
DR   CleanEx; MM_AI593442; -.
DR   Genevestigator; Q32M26; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR013836; CD34/Podocalyxin.
DR   Pfam; PF06365; CD34_antigen; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     23       Potential.
FT   CHAIN        24    199       Uncharacterized protein C11orf87 homolog.
FT                                /FTId=PRO_0000320197.
FT   TOPO_DOM     24     60       Extracellular (Potential).
FT   TRANSMEM     61     81       Helical; (Potential).
FT   TOPO_DOM     82    199       Cytoplasmic (Potential).
FT   CARBOHYD     19     19       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     26     26       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    105    106       CS -> WT (in Ref. 1; BAC28535).
SQ   SEQUENCE   199 AA;  20718 MW;  C48D626495315BB4 CRC64;
     MSARAPKELR LALPPCLLNR TFASHNASGG SSAGLRSSGA GGGTCITQVG QQLFQSFSST
     LVLIVLVTLI FCLLVLSLST FHIHKRRMKK RKMQRAQEEY ERDHCSGSHG GGGLPRAGVQ
     APTHGKETRL ERQPRDSAFC TPSNATSSSS SSSSSPGLLC QGPCAPPPPL PAPTPQGAPA
     ASSCLDTPGE GLLQTVVLS
//
ID   CNNM3_MOUSE             Reviewed;         713 AA.
AC   Q32NY4; A3KML7; Q3UFE5; Q7TSZ4; Q8C342; Q9JIM6;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   08-MAR-2011, entry version 43.
DE   RecName: Full=Metal transporter CNNM3;
DE   AltName: Full=Ancient conserved domain-containing protein 3;
DE            Short=mACDP3;
DE   AltName: Full=Cyclin-M3;
GN   Name=Cnnm3; Synonyms=Acdp3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 246-713 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 300-713 (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 300-713 (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=14723793; DOI=10.1186/1471-2164-5-7;
RA   Wang C.-Y., Yang P., Shi J.-D., Purohit S., Guo D., An H., Gu J.-G.,
RA   Ling J., Dong Z., She J.-X.;
RT   "Molecular cloning and characterization of the mouse Acdp gene
RT   family.";
RL   BMC Genomics 5:7-7(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 601-713 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 624-713 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Lung, and Sympathetic ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Probable metal transporter (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q32NY4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q32NY4-2; Sequence=VSP_027084;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
CC       brain, kidney, liver and heart.
CC   -!- MISCELLANEOUS: Shares weak sequence similarity with the cyclin
CC       family, explaining its name. However it has no cyclin-like
CC       function in vivo.
CC   -!- SIMILARITY: Belongs to the ACDP family.
CC   -!- SIMILARITY: Contains 2 CBS domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF86376.1; Type=Erroneous initiation;
CC       Sequence=AAI08418.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AC084391; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC052714; AAH52714.1; -; mRNA.
DR   EMBL; BC108417; AAI08418.1; ALT_INIT; mRNA.
DR   EMBL; BC132285; AAI32286.1; -; mRNA.
DR   EMBL; AF216964; AAF86376.1; ALT_INIT; mRNA.
DR   EMBL; AK087028; BAC39785.1; -; mRNA.
DR   EMBL; AK148549; BAE28616.1; -; mRNA.
DR   IPI; IPI00380795; -.
DR   IPI; IPI00653670; -.
DR   RefSeq; NP_001034640.1; NM_001039551.1.
DR   RefSeq; NP_444416.2; NM_053186.2.
DR   UniGene; Mm.256323; -.
DR   ProteinModelPortal; Q32NY4; -.
DR   SMR; Q32NY4; 290-455.
DR   PhosphoSite; Q32NY4; -.
DR   PRIDE; Q32NY4; -.
DR   Ensembl; ENSMUST00000001166; ENSMUSP00000001166; ENSMUSG00000001138.
DR   Ensembl; ENSMUST00000097776; ENSMUSP00000095383; ENSMUSG00000001138.
DR   GeneID; 94218; -.
DR   KEGG; mmu:94218; -.
DR   CTD; 94218; -.
DR   MGI; MGI:2151055; Cnnm3.
DR   eggNOG; roNOG05288; -.
DR   GeneTree; ENSGT00390000002383; -.
DR   HOGENOM; HBG715526; -.
DR   HOVERGEN; HBG074775; -.
DR   InParanoid; Q32NY4; -.
DR   OMA; RRWAGCA; -.
DR   OrthoDB; EOG4DR9C6; -.
DR   NextBio; 352195; -.
DR   ArrayExpress; Q32NY4; -.
DR   Bgee; Q32NY4; -.
DR   CleanEx; MM_CNNM3; -.
DR   Genevestigator; Q32NY4; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000644; Cysta_beta_synth_core.
DR   InterPro; IPR002550; DUF21.
DR   Pfam; PF01595; DUF21; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; CBS domain; Cell membrane; Glycoprotein;
KW   Ion transport; Membrane; Phosphoprotein; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN        29    713       Metal transporter CNNM3.
FT                                /FTId=PRO_0000295764.
FT   TRANSMEM      7     29       Helical; (Potential).
FT   TRANSMEM    137    157       Helical; (Potential).
FT   TRANSMEM    199    219       Helical; (Potential).
FT   TRANSMEM    227    247       Helical; (Potential).
FT   TRANSMEM    267    287       Helical; (Potential).
FT   DOMAIN      324    385       CBS 1.
FT   DOMAIN      392    458       CBS 2.
FT   MOD_RES     697    697       Phosphoserine (By similarity).
FT   MOD_RES     706    706       Phosphoserine.
FT   CARBOHYD     73     73       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     693    713       GSTNSRPSIPVEESPGRNPGV -> AFPVHLSLFGTLGNCS
FT                                (in isoform 2).
FT                                /FTId=VSP_027084.
FT   CONFLICT    463    464       SD -> Y (in Ref. 2; AAH52714).
SQ   SEQUENCE   713 AA;  76279 MW;  BDD9AA76620A96C0 CRC64;
     MAAAAAAVVG WLGWVLAAFC LGSTAGEAAP APGAGLLNFC TEEDSAPGAG SLRGRAAPEA
     TLCLRLFCSG LANSSWTWVA AEGAGCPEGG RATEPEEAAA PTGEWRALLR LRAEAGHPRS
     ALLAVRVEPG GGAAEEAAPP WALGLGAAGL LALAAVARGL QLSALALAPA EVQVLRESGS
     EAERAAARRL EPARRWAGCA LGALLLLASL AQAALAVLLY GAAGQRAVPA VLGCAGLVFL
     VGEVLPAAVS GRWALALAPR ALGLSRLAVL LTLPVALPVG QLLELAARPG RLRERVLELA
     RGGGDPYSDL SKGVLRSRTV EDVLTPLEDC FMLDSGTVLD FSVLASIMQS GHTRIPVYEE
     ERSNIVDMLY LKDLAIVEPE DCTPLSTITR FYNHPLHFVF NDTKLDAVLE EFKRGKSHLA
     IVQKVNNEGE GDPFYEVLGL VTLEDVIEEI IKSEILDESE DYSDTKVRKK TVALGAPLKR
     KEEFSLFKVS DDEYKVKISP QLLLATQRFL SREVDVFSPL RVSEKVLLHL LKHPSVNQEV
     TFDESNRLAA HHYLYQRSQP VDYFILILQG RVEVEIGKEG LKFENGAFTY YGVSALTAPS
     SAHQSPVSSR QLIRHDVQPE PADGTRSCTY CPDYTVRALS DLQLIKVTRL QYLNALLATR
     AQSLPPSPEN AELQAIPGSQ TRLLGDKSRE TAGSTNSRPS IPVEESPGRN PGV
//
ID   Q32NY6_MOUSE            Unreviewed;       420 AA.
AC   Q32NY6;
DT   06-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   06-DEC-2005, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   SubName: Full=Nuclear receptor subfamily 2, group F, member 1;
GN   Name=Nr2f1; ORFNames=RP23-471B6.1-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Jaw bone;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Glithero R.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the nuclear hormone receptor family.
CC   -!- SIMILARITY: Contains 1 nuclear receptor DNA-binding domain.
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DR   EMBL; BC108408; AAI08409.1; -; mRNA.
DR   EMBL; CT025642; CAO77858.1; -; Genomic_DNA.
DR   IPI; IPI00857154; -.
DR   RefSeq; NP_034281.2; NM_010151.2.
DR   UniGene; Mm.439653; -.
DR   ProteinModelPortal; Q32NY6; -.
DR   SMR; Q32NY6; 81-161, 184-405.
DR   STRING; Q32NY6; -.
DR   PRIDE; Q32NY6; -.
DR   Ensembl; ENSMUST00000091458; ENSMUSP00000089036; ENSMUSG00000069171.
DR   GeneID; 13865; -.
DR   KEGG; mmu:13865; -.
DR   UCSC; uc007rhe.1; mouse.
DR   CTD; 13865; -.
DR   MGI; MGI:1352451; Nr2f1.
DR   eggNOG; roNOG10739; -.
DR   HOVERGEN; HBG005606; -.
DR   InParanoid; Q32NY6; -.
DR   OMA; ASPMSAR; -.
DR   NextBio; 284760; -.
DR   ArrayExpress; Q32NY6; -.
DR   Bgee; Q32NY6; -.
DR   Genevestigator; Q32NY6; -.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030900; P:forebrain development; IDA:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0001764; P:neuron migration; IDA:MGI.
DR   InterPro; IPR003068; COUP_TF.
DR   InterPro; IPR008946; Nucl_hormone_rcpt_ligand-bd.
DR   InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd_core.
DR   InterPro; IPR001723; Str_hrmn_rcpt.
DR   InterPro; IPR013629; Znf_C4_C.
DR   InterPro; IPR001628; Znf_hrmn_rcpt.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   Gene3D; G3DSA:1.10.565.10; Nucl_hrmn_rcpt_lig_bd; 1.
DR   Gene3D; G3DSA:3.30.50.10; Znf_NHR/GATA; 1.
DR   Pfam; PF00104; Hormone_recep; 1.
DR   Pfam; PF00105; zf-C4; 1.
DR   Pfam; PF08420; zf-C4_C; 1.
DR   PRINTS; PR01282; COUPTNFACTOR.
DR   PRINTS; PR00398; STRDHORMONER.
DR   PRINTS; PR00047; STROIDFINGER.
DR   SMART; SM00430; HOLI; 1.
DR   SMART; SM00399; ZnF_C4; 1.
DR   SUPFAM; SSF48508; Str_ncl_receptor; 1.
DR   PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR   PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Receptor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
SQ   SEQUENCE   420 AA;  45899 MW;  B360CADBAB312908 CRC64;
     MAMVVSSWRD PQDDVAGGNP GGPNPAAQAA RGGGGGEQQQ AGSGAPHTPQ TPGQPGAPAT
     PGTAGDKGQG PPGSGQSQQH IECVVCGDKS SGKHYGQFTC EGCKSFFKRS VRRNLTYTCR
     ANRNCPIDQH HRNQCQYCRL KKCLKVGMRR EAVQRGRMPP TQPNPGQYAL TNGDPLNGHC
     YLSGYISLLL RAEPYPTSRY GSQCMQPNNI MGIENICELA ARLLFSAVEW ARNIPFFPDL
     QITDQVSLLR LTWSELFVLN AAQCSMPLHV APLLAAAGLH ASPMSADRVV AFMDHIRIFQ
     EQVEKLKALH VDSAEYSCLK AIVLFTSDAC GLSDAAHIES LQEKSQCALE EYVRSQYPNQ
     PSRFGKLLLR LPSLRTVSSS VIEQLFFVRL VGKTPIETLI RDMLLSGSSF NWPYMSIQCS
//
ID   OSBP1_MOUSE             Reviewed;         751 AA.
AC   Q3B7Z2; Q3V163; Q52KH7; Q570Y8;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Oxysterol-binding protein 1;
GN   Name=Osbp; Synonyms=Kiaa4220;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-751.
RC   STRAIN=C57BL/6;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 236-751.
RC   TISSUE=Pancreatic islet;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-137; SER-142;
RP   SER-182; THR-321; SER-323 AND SER-326, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-137 AND
RP   SER-295, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-137 AND
RP   SER-295, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Binds cholesterol and a range of oxysterols. Cholesterol
CC       binding promotes the formation of a complex with PP2A and a
CC       tyrosine phosphatase which dephosphorylate ERK1/2, whereas 25-
CC       hydroxycholesterol causes its disassembly. Regulates cholesterol
CC       efflux by decreasing ABCA1 stability (By similarity).
CC   -!- SUBUNIT: Homodimer or homotrimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus
CC       membrane; Peripheral membrane protein (By similarity). Note=When
CC       bound to oxysterols, translocates to the periphery of Golgi
CC       membranes (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3B7Z2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3B7Z2-2; Sequence=VSP_035281, VSP_035282;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The PH domain control cholesterol binding without
CC       affecting 25-hydroxycholesterol binding (By similarity).
CC   -!- DOMAIN: The second coiled-coil domain is required for interaction
CC       with the tyrosine phosphatase (By similarity).
CC   -!- SIMILARITY: Belongs to the OSBP family.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK132663; BAE21289.1; -; mRNA.
DR   EMBL; AC124464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC094342; AAH94342.1; -; mRNA.
DR   EMBL; BC107327; AAI07328.1; -; mRNA.
DR   EMBL; BC107328; AAI07329.1; -; mRNA.
DR   EMBL; AK220301; BAD90226.1; -; mRNA.
DR   IPI; IPI00755161; -.
DR   IPI; IPI00876514; -.
DR   RefSeq; NP_001028346.1; NM_001033174.1.
DR   UniGene; Mm.291279; -.
DR   ProteinModelPortal; Q3B7Z2; -.
DR   SMR; Q3B7Z2; 29-133.
DR   STRING; Q3B7Z2; -.
DR   PhosphoSite; Q3B7Z2; -.
DR   Ensembl; ENSMUST00000025590; ENSMUSP00000025590; ENSMUSG00000024687.
DR   GeneID; 76303; -.
DR   KEGG; mmu:76303; -.
DR   UCSC; uc008gtj.1; mouse.
DR   CTD; 76303; -.
DR   MGI; MGI:97447; Osbp.
DR   eggNOG; roNOG11286; -.
DR   GeneTree; ENSGT00550000074251; -.
DR   HOGENOM; HBG445378; -.
DR   HOVERGEN; HBG053374; -.
DR   InParanoid; Q3B7Z2; -.
DR   OrthoDB; EOG49S65T; -.
DR   NextBio; 344933; -.
DR   ArrayExpress; Q3B7Z2; -.
DR   Bgee; Q3B7Z2; -.
DR   Genevestigator; Q3B7Z2; -.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0008202; P:steroid metabolic process; IEA:InterPro.
DR   InterPro; IPR000648; Oxysterol-bd.
DR   InterPro; IPR018494; Oxysterol-bd_CS.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   PANTHER; PTHR10972; Oxysterol_bd; 1.
DR   Pfam; PF01237; Oxysterol_BP; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS01013; OSBP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW   Golgi apparatus; Lipid transport; Lipid-binding; Membrane;
KW   Phosphoprotein; Transport.
FT   CHAIN         1    751       Oxysterol-binding protein 1.
FT                                /FTId=PRO_0000349262.
FT   DOMAIN       32    125       PH.
FT   REGION      350    401       Sterol binding (By similarity).
FT   COILED      235    270       Potential.
FT   COILED      674    705       Potential.
FT   MOD_RES      47     47       N6-acetyllysine (By similarity).
FT   MOD_RES     134    134       Phosphoserine.
FT   MOD_RES     137    137       Phosphoserine.
FT   MOD_RES     142    142       Phosphoserine.
FT   MOD_RES     182    182       Phosphoserine.
FT   MOD_RES     295    295       Phosphoserine.
FT   MOD_RES     321    321       Phosphothreonine.
FT   MOD_RES     323    323       Phosphoserine.
FT   MOD_RES     326    326       Phosphoserine.
FT   MOD_RES     329    329       Phosphoserine (By similarity).
FT   MOD_RES     330    330       Phosphoserine (By similarity).
FT   MOD_RES     333    333       Phosphoserine (By similarity).
FT   VAR_SEQ       1    214       Missing (in isoform 2).
FT                                /FTId=VSP_035281.
FT   VAR_SEQ     215    218       AMIN -> MLQL (in isoform 2).
FT                                /FTId=VSP_035282.
SQ   SEQUENCE   751 AA;  84689 MW;  6DF309C13BAC5D32 CRC64;
     MAATELRGVA AGGPGSAPPA AGSGGSGAGG SGSAREGWLF KWTNYIKGYQ RRWFVLSNGL
     LSYYRSKAEM RHTCRGTINL ATANITVEDS CNFIISNGGA QTYHLKASSE VERQRWVTAL
     ELAKAKAVKM LAESDDSGDE ESVSQTDKTE LQSTLRTLSS KVEDLSTCND LIAKHGTALQ
     RSLSELESLK LPAESNEKIK QVNERATLFR ITSNAMINAC RDFLMLAQTH SKKWQKSLQY
     ERDQRIRLEE TLEQLAKQHN HLERAFRGAT VLPANPPGSA GSGKDQCCSG KGDMSDEDDE
     NEFFDAPEII TMPENLGHKR TGSNISGASS DVSLDEQYKH QLEETKKEKR TRIPYKPNYS
     LNLWSIMKNC IGKELSKIPM PVNFNEPLSM LQRLTEDLEY HELLDRAAKC ENSLEQLCYV
     AAFTVSSYST TVFRTSKPFN PLLGETFELD RLEENGYRSI CEQVSHHPPA AAHHAESKNG
     WTLRQEIKIT SKFRGKYLSI MPLGTIHCIF HSTGHHYTWK KVTTTVHNII VGKLWIDQSG
     EIDIVNHKTG DKCNLKFVPY SYFSRDVARK VTGEVTDPSG KVHFALLGTW DEKMDCFKVQ
     AASGENGGDA RQRGHEAEDS RVMLWKRNPL PKNAENMYYF SELALTLNAW EGGTAPTDSR
     LRPDQRLMEN GRWDEANAEK QRLEEKQRLS RKKREAEAAK ATEDGTPHDP YKALWFERKK
     DPVTRELTHI YSGEYWECKE KQDWGSCPDI F
//
ID   Q3KNZ1_MOUSE            Unreviewed;       790 AA.
AC   Q3KNZ1;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAR-2011, entry version 39.
DE   SubName: Full=Cadherin 6;
DE   SubName: Full=Cdh6 protein;
GN   Name=Cdh6; ORFNames=mCG_8950;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cadherins are calcium dependent cell adhesion proteins
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
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DR   EMBL; BC107008; AAI07009.1; -; mRNA.
DR   EMBL; CH466581; EDL03251.1; -; Genomic_DNA.
DR   IPI; IPI00775835; -.
DR   UniGene; Mm.57048; -.
DR   ProteinModelPortal; Q3KNZ1; -.
DR   SMR; Q3KNZ1; 54-375, 716-781.
DR   STRING; Q3KNZ1; -.
DR   Ensembl; ENSMUST00000036439; ENSMUSP00000037113; ENSMUSG00000039385.
DR   MGI; MGI:107435; Cdh6.
DR   HOVERGEN; HBG005217; -.
DR   InParanoid; Q3KNZ1; -.
DR   ArrayExpress; Q3KNZ1; -.
DR   Bgee; Q3KNZ1; -.
DR   Genevestigator; Q3KNZ1; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 5.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF01049; Cadherin_C; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 5.
DR   SUPFAM; SSF49313; Cadherin; 5.
DR   PROSITE; PS00232; CADHERIN_1; 3.
DR   PROSITE; PS50268; CADHERIN_2; 5.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell membrane; Membrane; Repeat;
KW   Transmembrane; Transmembrane helix.
SQ   SEQUENCE   790 AA;  88325 MW;  13225434DEBF2A8F CRC64;
     MRTYRYFLLL FWVGQPYPTF SNPLSKRTSG FPAKRKALEL SANSRNELSR SKRSWMWNQF
     FLLEEYTGSD YQYVGKLHSD QDRGDGSLKY ILSGDGAGDL FIINENTGDI QATKRLDREE
     KPVYILRAQA VNRRTGRPVE PESEFIIKIH DINDNEPIFT KDVYTATVPE MADVGTFVVQ
     VTATDADDPT YGNSAKVVYS ILQGQPYFSV ESETGIIKTA LLNMDRENRE QYQVVIQAKD
     MGGQMGGLSG TTTVNITLTD VNDNPPRFPQ STYQFKTPES SPPGTPIGRI KASDADVGEN
     AEIEYSITDG EGHEMFDVIT DQETQEGIIT VKKLLDFEKK KVYTLKVEAS NPHVEPRFLY
     LGPFKDSATV RIVVDDVDEP PVFSKLAYIL QIREDARINT TIGSVAAQDP DAARNPVKYS
     VDRHTDMDRI FNIDSGNGSI FTSKLLDRET LLWHNITVIA TEINNPKQSS RVPLYIKVLD
     VNDNAPEFAE FYETFVCEKA KADQLIQTLR AVDKDDPYSG HQFSFSLAPE AASGSNFTIQ
     DNKDNTAGIL TRKNGYNRHE MSTYLLPVVI SDNDYPVQSS TGTVTVRVCA CDHHGNMQSC
     HAEALIHPTG LSTGALVAIL LCIVILLVTV VLFAALRRQR KKEPLIISKE DIRDNIVSYN
     DEGGGEEDTQ AFDIGTLRNP EAMEDSKSRR DIVPEALFLP RRTPTARDNT DVRDFINQRL
     KENDTDPTAP PYDSLATYAY EGTGSVADSL SSLESVTTDG DQDYDYLSDW GPRFKKLADM
     YGGMDSDKDS
//
ID   PREX2_MOUSE             Reviewed;        1598 AA.
AC   Q3LAC4; Q3UQI2; Q3UU18; Q9CXD5;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   08-MAR-2011, entry version 44.
DE   RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 2 protein;
DE            Short=P-Rex2;
DE            Short=PtdIns(3,4,5)-dependent Rac exchanger 2;
DE   AltName: Full=DEP domain-containing protein 2;
GN   Name=Prex2; Synonyms=Depdc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   PubMed=15304343; DOI=10.1016/j.febslet.2004.06.096;
RA   Donald S., Hill K., Lecureuil C., Barnouin R., Krugmann S.,
RA   John Coadwell W., Andrews S.R., Walker S.A., Hawkins P.T.,
RA   Stephens L.R., Welch H.C.E.;
RT   "P-Rex2, a new guanine-nucleotide exchange factor for Rac.";
RL   FEBS Lett. 572:172-176(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-962 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 251-1598 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Head, Lung, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Functions as a RAC1 guanine nucleotide exchange factor
CC       (GEF), activating Rac proteins by exchanging bound GDP for free
CC       GTP. Its activity is synergistically activated by
CC       phosphatidylinositol-3,4,5-triphosphate and the beta gamma
CC       subunits of heterotrimeric G protein. Mediates the activation of
CC       RAC1 in a PI3K-dependent manner. May be an important mediator of
CC       Rac signaling, acting directly downstream of both G protein-
CC       coupled receptors and phosphoinositide 3-kinase (By similarity).
CC   -!- SUBUNIT: Interacts with RAC1 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3LAC4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3LAC4-2; Sequence=VSP_025164, VSP_025165;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: PH domain confers substrate specificity and recognition.
CC       Able to discriminate between RAC1, RHOA, and CDC42 (By
CC       similarity).
CC   -!- DOMAIN: DH domain alone was unable to confer substrate specificity
CC       and recognition (By similarity).
CC   -!- SIMILARITY: Contains 2 DEP domains.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 2 PDZ (DHR) domains.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB31066.1; Type=Frameshift; Positions=498, 500;
CC       Sequence=BAE25059.1; Type=Erroneous initiation;
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DR   EMBL; AM109952; CAJ33348.1; -; mRNA.
DR   EMBL; AK018093; BAB31066.1; ALT_SEQ; mRNA.
DR   EMBL; AK138884; BAE23811.1; -; mRNA.
DR   EMBL; AK142414; BAE25059.1; ALT_INIT; mRNA.
DR   IPI; IPI00785445; -.
DR   IPI; IPI00890914; -.
DR   RefSeq; NP_083801.1; NM_029525.1.
DR   UniGene; Mm.123247; -.
DR   HSSP; Q9ER22; 2DFK.
DR   ProteinModelPortal; Q3LAC4; -.
DR   SMR; Q3LAC4; 5-359, 372-457, 476-558, 589-736.
DR   STRING; Q3LAC4; -.
DR   PhosphoSite; Q3LAC4; -.
DR   PRIDE; Q3LAC4; -.
DR   Ensembl; ENSMUST00000027056; ENSMUSP00000027056; ENSMUSG00000048960.
DR   GeneID; 109294; -.
DR   KEGG; mmu:109294; -.
DR   UCSC; uc007ahs.1; mouse.
DR   CTD; 109294; -.
DR   MGI; MGI:1923385; Prex2.
DR   HOGENOM; HBG445637; -.
DR   HOVERGEN; HBG053677; -.
DR   InParanoid; Q3LAC4; -.
DR   OrthoDB; EOG42820Q; -.
DR   NextBio; 361887; -.
DR   ArrayExpress; Q3LAC4; -.
DR   Bgee; Q3LAC4; -.
DR   Genevestigator; Q3LAC4; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2.
DR   Pfam; PF00610; DEP; 2.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00049; DEP; 2.
DR   SMART; SM00228; PDZ; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   SUPFAM; SSF50156; PDZ; 2.
DR   PROSITE; PS50186; DEP; 2.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50106; PDZ; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Guanine-nucleotide releasing factor; Repeat.
FT   CHAIN         1   1598       Phosphatidylinositol 3,4,5-trisphosphate-
FT                                dependent Rac exchanger 2 protein.
FT                                /FTId=PRO_0000286796.
FT   DOMAIN       15    206       DH.
FT   DOMAIN      237    353       PH.
FT   DOMAIN      382    456       DEP 1.
FT   DOMAIN      483    558       DEP 2.
FT   DOMAIN      584    663       PDZ 1.
FT   DOMAIN      669    746       PDZ 2.
FT   VAR_SEQ     698    734       TVAAAAGLHPGQCIIKVNGINVSKETHASVIAHVTAC ->
FT                                ETFFAAASRSAPAGPLALPCPTEGSPQSARNGPLSLK (in
FT                                isoform 2).
FT                                /FTId=VSP_025164.
FT   VAR_SEQ     735   1598       Missing (in isoform 2).
FT                                /FTId=VSP_025165.
SQ   SEQUENCE   1598 AA;  181716 MW;  3D9B5CD4902C2E3D CRC64;
     MSDESAREVD KQLRLRVCVL SELQKTERDY VGTLEFLVSA FLHRMNQCAA AKVDKNVTEE
     TVKMLFSNIE EILIVHKEFL KVVEECLYPE PSAQQEVGAC FLHFKDKFRI YDEYCSNHEK
     AQKLLLELNK IRTIRTFLLN CMLLGGRKNT DVPLEGYLVT PIQRICKYPL LLKELLKRTP
     RRHSDYTAVM EALQAMKAVC SNINEAKRQM EKLEVLEEWQ AHIEGWEGSN ITDTCTEMLM
     CGVLMKISSG NIQERVFFLF DNLLVYCKRK HRRLKNSKAS TDGYRYVFRG RINTEVMEVE
     NVDDGTADFH SSGHIVVNGW KIHNTAKNKW FVCMAKSPEE KHEWFEAILK ERERRKGLKL
     GMEQDTWVMI SEQGEKLYKM MCKQGNLIKD RKRKLTTFPK CFLGSEFVSW LLEIGEIHRP
     EEGVHLGQAL LENGIIHHVT DKHQFKPEQM LYRFRYDDGT FYPRSEMQDV ISKGVRLYCR
     LHSLFTPVVR DKDYHLRTYK SVVMANKLID WLIAQGDCRT REEAMIFAVG LCDNGFMHHV
     LEKSEFKDEP LLFRFFADEE MEGSNMKHRL MKHDLKVVEN VIAKSLLIKS NEGSYGFGLE
     DKNKVPIIKL VEKGSNAEMA GMEVGKKIFA INGDLVFLRP FPEVDCFLKS CLNSRKPLRV
     LVSTKPRETV KIPDSADGLG FQIRGFGPSV VHAVGRGTVA AAAGLHPGQC IIKVNGINVS
     KETHASVIAH VTACRKYKRP MKQDSIQWVY DSLESAQEDI QKSHSKPPGD GAGDAFECKV
     EDVIDKFNTM AIIDGKKEHV SLTVDNVHLE YGVVYEYDST AGTKCNVVEK MVEPKGFFSL
     TAKILEALAK SDEHFVQNCT SLNSLNEVIA TDLQSKFTSM CSERIEHVCH RISSYGRFSR
     VLKNRAWPTF KQAKPKISPL HSSDFCPTNC HVNVMEVSYP KTSTSLGSAF GVQLDSRKHN
     SHDKENKSVE PGKLSPMVYI QHTITTMAAP SGLSLGHKDG HGLQYLLKEE DLETQDIYHK
     LLGKLQTALK EVEMSVCQID DLLSSITYSP KLERKTTECV TPMDSDNEKG ERNSKRVCFN
     VAGDEQEDSG HDTVSNRDSY SDCNSNRNSI ASFTSICSSQ CSSYFHSDEM DSGDELPISV
     RISHDKQDKI HTCLEQLFSQ IDSIITLLKG QAVIRPFDQT KYLTPGRGLQ EFQQEMEAKL
     SCPRRLRLHL KQDPWNLPSS IQALAQSIRK HAEEVKCRIL LALLEYSDSE TQLRRDMVFC
     QSLVATVCAF SEQLMAALNQ MFDNSKENEM ETCEASRRWL DQIANAGVLF HFQSLLSPNL
     KDEQAMLEDT LVALFDLEKV SFFFKPSEED PLVANVPLTY QVEGSRQALK VYFYMDSYHF
     EQLPQRLKNG GGFKIHPVLF SQALESMEGY CYRDNISVEE FQAQINTASL EKVKQYNQKL
     RAFYLDKSNS PPNTTSKAAY IDKLMKPLNA LDELYRLITS FIRSKRIAAC VNTPCSASGV
     GLLSVSSELC DRLGACHIIM CSSGVHRCTL SVTLEQTITL ARSHGLPPRY IMQAMDVMRK
     QGARVQNTAK NLGVRDRTPQ SAPRLYKLCE PPPPVGEE
//
ID   Q3LS20_MOUSE            Unreviewed;       538 AA.
AC   Q3LS20;
DT   25-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   SubName: Full=RIKEN cDNA 1700024D23, isoform CRA_c;
DE   SubName: Full=TREK-2 two-pore-domain K+ channel;
GN   Name=Kcnk10; ORFNames=mCG_22435;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NMRI; TISSUE=Cerebellum;
RX   PubMed=16354767;
RA   Czirjak G., Enyedi P.;
RT   "Zinc and mercuric ions distinguish TRESK from the other two-pore-
RT   domain K+ channels.";
RL   Mol. Pharmacol. 69:1024-1032(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the two pore domain potassium channel
CC       (TC 1.A.1.8) family.
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DR   EMBL; DQ185134; ABA28315.1; -; mRNA.
DR   EMBL; CH466549; EDL18934.1; -; Genomic_DNA.
DR   IPI; IPI00109820; -.
DR   UniGene; Mm.196158; -.
DR   ProteinModelPortal; Q3LS20; -.
DR   SMR; Q3LS20; 151-203, 254-318.
DR   PhosphoSite; Q3LS20; -.
DR   PRIDE; Q3LS20; -.
DR   Ensembl; ENSMUST00000085120; ENSMUSP00000082201; ENSMUSG00000033854.
DR   UCSC; uc007oqg.1; mouse.
DR   MGI; MGI:1919508; Kcnk10.
DR   eggNOG; roNOG11640; -.
DR   HOGENOM; HBG717586; -.
DR   HOVERGEN; HBG052234; -.
DR   InParanoid; Q3LS20; -.
DR   OMA; EQLNKHG; -.
DR   ArrayExpress; Q3LS20; -.
DR   Bgee; Q3LS20; -.
DR   Genevestigator; Q3LS20; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR013099; Ion_trans_2.
DR   InterPro; IPR003280; K_chnl_2pore.
DR   InterPro; IPR003976; K_chnl_2pore_TREK.
DR   Pfam; PF07885; Ion_trans_2; 2.
DR   PRINTS; PR01333; 2POREKCHANEL.
DR   PRINTS; PR01499; TREKCHANNEL.
PE   2: Evidence at transcript level;
KW   Ion transport; Ionic channel; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
SQ   SEQUENCE   538 AA;  59758 MW;  28FDF5DB6A17642B CRC64;
     MKFPIETPRK QVNWDPKVAV PAAAPPVCQP KSATNGHHPV PRLSISSRAT VVARMEGASQ
     GGLQTVMKWK TVVAIFVVVV VYLVTGGLVF RALEQPFESS QKNTIALEKA EFLRDHICVS
     PQELETLIQH ALDADNAGVS PVGNSSNSSS HWDLGSAFFF AGTVITTIGY GNIAPSTEGG
     KIFCILYAIF GIPLFGFLLA GIGDQLGTIF GKSIARVEKV FRKKQVSQTK IRVISTILFI
     LAGCIVFVTI PAVIFKYIEG WTALESIYFV VVTLTTVGFG DFVAGGNAGI NYREWYKPLV
     WFWILVGLAY FAAVLSMIGD WLRVLSKKTK EEVGEIKAHA AEWKANVTAE FRETRRRLSV
     EIHDKLQRAA TIRSMERRRL GLDQRAHSLD MLSPEKRSVF AALDTGRFKA SSQESINNRP
     NNLRLKGPEQ LTKHGQGASE DNIINKFGST SKLTKRKNKD LKKTLPEDVQ KIYKTFRNYS
     LDEEKKEDET EKMCNSDNSS TAMLTECIQQ QAEMENGMVP TDTKDQGLEN NSLLEDRN
//
ID   Q3T9V8_MOUSE            Unreviewed;      1239 AA.
AC   Q3T9V8;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 34.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Dctn1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; AK172261; BAE42912.1; -; mRNA.
DR   IPI; IPI00856500; -.
DR   UniGene; Mm.6919; -.
DR   ProteinModelPortal; Q3T9V8; -.
DR   SMR; Q3T9V8; 9-82.
DR   STRING; Q3T9V8; -.
DR   Ensembl; ENSMUST00000077407; ENSMUSP00000076623; ENSMUSG00000031865.
DR   UCSC; uc009cna.1; mouse.
DR   MGI; MGI:107745; Dctn1.
DR   HOVERGEN; HBG004956; -.
DR   ArrayExpress; Q3T9V8; -.
DR   Bgee; Q3T9V8; -.
DR   Genevestigator; Q3T9V8; -.
DR   GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR023092; CAP-Gly_CS.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   InterPro; IPR022157; Dynactin.
DR   Gene3D; G3DSA:2.30.30.190; CAP-Gly_domain; 1.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   Pfam; PF12455; Dynactin; 1.
DR   SUPFAM; SSF74924; CAP-Gly_domain; 1.
DR   PROSITE; PS00845; CAP_GLY_1; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1239 AA;  136878 MW;  BEBEE0C59198D521 CRC64;
     MSTEASARPL RVGSRVEVIG KGHRGTVAYV GATLFATGKW VGVILDEAKG KNDGTVQGRK
     YFTCDEGHGI FVRQSQIQVF EDGADTTSPE TPDSSASKVL KREGADAAAK TSKLPTRPAS
     TGVAGPSSSL GPSGSASAGE LSSSEPSTPA QTPLAAPIIP TPALTSPGAA PPLPSPSKEE
     EGLRAQVRDL EEKLETLRLK RSEDKAKLKE LEKHKIQLEQ VQEWKSKMQE QQADLQRRLK
     EARKEAKEAL EAKERYMEEM ADTADAIEMA TLDKEMAEER AESLQQEVEA LKERVDELTT
     DLEILKAEIE EKGSDGAASS YQLKQLEEQN ARLKDALVRM RDLSSSEKQE HVKLQKLMEK
     KNQELEVVWQ QRERLQEELS QAESTIDELK EQVDAALGAE EMVEMLTDRN LNLEEKVREL
     RETVGDLEAM NEMNDELQEN ARETELELRE QLDMAGARVR EAQKRVEAAQ ETVADYQQTI
     KKYRQLTAHL QDVNRELTNQ QEASVERQQQ PPPETFDFKI KFAETKAHAK AIEMELRQME
     VAQANRHMSL LTAFMPDSFL RPGGDHDCVL VLLLMPRLIC KAELIRKQAQ EKFDLSENCS
     ERPGLRGAAG EQLSFAAGLV YSLSLLQATL HRYEHALSQC SVDVYKKVGS LYPEMSAHER
     SLDFLIELLH KDQLDETVNV EPLTKAIKYY QHLYSIHLAE QPEDSTMQLA DHIKFTQSAL
     DCMGVEVGRL RAFLQGGQEA TDIALLLRDL ETSCSDTRQF CKKIRRRMPG TDAPGIPAAL
     AFGSQVSDTL LDCRKHLTWV VAVLQEVAAA AAQLIAPLAE NEGLPVAALE ELAFKASEQI
     YGSPSSSPYE CLRQSCTILI STMNKLATAM QEGEYDAERP PSKPPPVELR AAALRAEITD
     AEGLGLKLED RETVIKELKK SLKIKGEELS EANVRLSLLE KKLDSAAKDA DERIEKVQTR
     LDETQTLLRK KEKDFEETMD ALQADIDQLE AEKAELKQRL NSQSKRTIEG LRGPPPSGIA
     TLVSGIAGGG APGQAPGALP GPGLVKDSPL LLQQISAMRL HISQLQHENS ILRGAQMKAS
     LAALPPLHVA KLSLPPHEGP GGNLVAGALY RKTSQLLEKL NQLSTHTHVV DITRSSPAAK
     SPSAQLMEQV AQLKSLSDTI EKLKDEVLKE TVTQRPGATV PTDFATFPSS AFLRAKEEQQ
     DDTVYMGKVT FSCAAGLGQR HRLVLTQEQL HQLHSRLIS
//
ID   Q3TA69_MOUSE            Unreviewed;       607 AA.
AC   Q3TA69;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 38.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Rap1gds1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK172052; BAE42801.1; -; mRNA.
DR   IPI; IPI00653794; -.
DR   UniGene; Mm.28893; -.
DR   ProteinModelPortal; Q3TA69; -.
DR   STRING; Q3TA69; -.
DR   PRIDE; Q3TA69; -.
DR   Ensembl; ENSMUST00000098574; ENSMUSP00000096173; ENSMUSG00000028149.
DR   MGI; MGI:2385189; Rap1gds1.
DR   eggNOG; roNOG08899; -.
DR   HOGENOM; HBG444003; -.
DR   HOVERGEN; HBG001622; -.
DR   InParanoid; Q3TA69; -.
DR   ArrayExpress; Q3TA69; -.
DR   Bgee; Q3TA69; -.
DR   Genevestigator; Q3TA69; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 2.
DR   Pfam; PF00514; Arm; 4.
DR   SMART; SM00185; ARM; 5.
DR   SUPFAM; SSF48371; ARM-type_fold; 2.
DR   PROSITE; PS50176; ARM_REPEAT; 2.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   607 AA;  66075 MW;  A6EA430AC044A41F CRC64;
     MDNLSDTLKK LKITAADRTE GSLEGCLDCL LQALAQNNAE TSEKIQGSGI LQLFANLLTP
     QASCTAKVAD IIAEVAKNEF MRIPCVDAGL ISPLVQLLNS KDQEVLLQTG RALGNICYDS
     HEGRSAVDQA GGAQIVIDHL RSLCGRTDPA SEKLMTVFCG MLMNYSNEND SLQAQLISMG
     VIPTLVKLLG IHCHNAALTE MCLVAFGNLA ELESSKEQFA STNIAEELVK LFKKQIEHDK
     REMIFEVLAP LAENDAIKLQ LVEAGLVECL LEIVQQKVNS NKEDDVAELK TASDLMVLLL
     LGDESMQKLF EGGKGSVFQR VLSWIPSNNH QLQLAGALAI ANFARNDGNC IHMVDNGIVE
     KLMDLLDRHV EDGNVTVQHA ALSALRNLAI PVVNKAKMLS AGVTETVLKF LKSEMPPVQF
     KLLGTLRMLI DAQAEAAEQL GKNAKLVERL VEWCEAKDHA GVMGESNRLL SALIRHSKSK
     DVIKTIVQSG GIKHLVTMAT SEHVIMQNEA LVALALIAAL ELGPAEKDLA SAQLVQILHR
     LLADERSAPE IKYNSMVLIC ALMGSESLYK EVQDLAFLDV VSKLRSHENK SVAQQASLTE
     QRLTVES
//
ID   Q3TAH0_MOUSE            Unreviewed;       515 AA.
AC   Q3TAH0;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 29.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Spata2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK171852; BAE42698.1; -; mRNA.
DR   IPI; IPI00403313; -.
DR   UniGene; Mm.34342; -.
DR   Ensembl; ENSMUST00000057627; ENSMUSP00000057095; ENSMUSG00000047030.
DR   MGI; MGI:2146885; Spata2.
DR   eggNOG; roNOG15386; -.
DR   HOVERGEN; HBG057357; -.
DR   InParanoid; Q3TAH0; -.
DR   OrthoDB; EOG4P2Q24; -.
DR   ArrayExpress; Q3TAH0; -.
DR   Bgee; Q3TAH0; -.
DR   Genevestigator; Q3TAH0; -.
PE   1: Evidence at protein level;
SQ   SEQUENCE   515 AA;  57812 MW;  52968FF8ABA4CEF4 CRC64;
     MDTKYKDDLF RKYVQFHEGK VDTTPGNQQP GSDEYLRVAA ATLLSLHKVD PLYRFRLIQF
     YEVVESSLRS LSSSSLSALH CAFSMLETMA INLFLFPWKK EFRSIKTYTG PFVYYVKSTL
     LEKDIRAILR FMGYEPELGT VYKLKELVES LQVKMVSFEL FLAKVECEQM LGIHSQVKDK
     GYSELDVVAE RKGSTEDARG CSDALRRRAE SREHLTTSMA RVALQKSASE RAAKDYYKPR
     VTKPSRSVDA YDSYWESRKP PSKASLSLRK EPLAMDVGED LKDEIIRPSP SLLAMSSSPH
     GSPDDLSSIS SINGLGLLRS TYFSTQDDVD LYTDSEPRAT YRRQDALRPD VWLVKNDTHP
     IYHKRSPPTK ESALSKCQNC GLSCSSSLCQ RCDSVLVCPS ASKPSAFPSK ASVHDSLAHG
     APMREKYVGH QTQGLDRLAP VHSKPKPSTT ATSRCGFCNR AGATNTCTQC SKVSCDACLG
     AYHYDPCCRK SELHKFLPNS KLNYKSAPFS QLVYR
//
ID   Q3TAJ7_MOUSE            Unreviewed;       705 AA.
AC   Q3TAJ7;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-FEB-2011, entry version 39.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Als2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK171800; BAE42671.1; -; mRNA.
DR   IPI; IPI00309844; -.
DR   UniGene; Mm.272078; -.
DR   STRING; Q3TAJ7; -.
DR   Ensembl; ENSMUST00000027178; ENSMUSP00000027178; ENSMUSG00000026024.
DR   Ensembl; ENSMUST00000163058; ENSMUSP00000125753; ENSMUSG00000026024.
DR   UCSC; uc007bdl.1; mouse.
DR   MGI; MGI:1921268; Als2.
DR   GeneTree; ENSGT00600000084242; -.
DR   HOVERGEN; HBG097441; -.
DR   InParanoid; Q3TAJ7; -.
DR   ArrayExpress; Q3TAJ7; -.
DR   Bgee; Q3TAJ7; -.
DR   Genevestigator; Q3TAJ7; -.
DR   GO; GO:0043197; C:dendritic spine; IDA:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR   GO; GO:0016197; P:endosome transport; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
DR   GO; GO:0008104; P:protein localization; IMP:MGI.
DR   GO; GO:0001881; P:receptor recycling; IMP:MGI.
DR   GO; GO:0032313; P:regulation of Rab GTPase activity; IDA:MGI.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR   GO; GO:0016050; P:vesicle organization; IDA:MGI.
DR   InterPro; IPR003409; MORN.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR003123; VPS9.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF02493; MORN; 7.
DR   Pfam; PF02204; VPS9; 1.
DR   SMART; SM00698; MORN; 8.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS51205; VPS9; 1.
PE   2: Evidence at transcript level;
KW   Repeat.
FT   NON_TER       1      1
SQ   SEQUENCE   705 AA;  79613 MW;  AA55BE88DD249932 CRC64;
     DVFPLATLWA EPLSEEAGSV NGLKITTPEE QFTLISSTPQ EKTKWLRAIS QAVDQALRGT
     SDFPLYGGGS SVQRQEPPIS RSAKYTFYKD TRLKDATYDG RWLSGKPHGR GVLKWPDGKM
     YSGMFRNGLE DGYGEYRIPN KALNKEDHYV GHWKEGKMCG QGVYSYASGE VFEGCFQDNM
     RHGHGLLRSG KLTSSSPSMF IGQWVMDKKA GYGVFDDITR GEKYMGMWQD DVCQGNGVVV
     PQFGLYYEGN FHLNKMMGNG VLLSEDDTIY EGEFSDDWTL SGKGTLTMPH GDYIEGYFSG
     EWGSGIKITG TYFKPSLYES DKDKPKALKL GNLAVAADEK WRAVFEECWH QLGCESPGQG
     EVWKAWDNIA VALTTNRRQH KDSPEILSRS QTQTLESLEY IPQHIGAFSV EKYDDIKKYL
     IKACDTPLHP LGRLVETLVA VYRMTYVGVG ANRRLLQEAV KEIKSYLKRI FQLVRFLFPE
     LPEEGSTIPL SAPLPTGRRS FCTGKLDSRS ESPEPGYVVT SSGLLLPVLL PRLYPPLFML
     YALDNDREED IYWECVLRLN KQPDIALLGF LGVQKKFWPA TLSILGESKK VLSTTKDACF
     ASAVECLQQI STTFTPSDKL KVIQQTFEEI SQSVLASLQE DFLWSMDDLF PVFLYVVLRA
     RIRNLGSEVH LIEDLMDPFL QHGEQGIMFT TLKACYFQIQ REKLN
//
ID   Q3TB24_MOUSE            Unreviewed;       324 AA.
AC   Q3TB24;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 49.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Dnajb2; Synonyms=Dnajb10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Activated spleen;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Activated spleen;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Activated spleen;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Activated spleen;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Activated spleen;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK156083; BAE33579.1; -; mRNA.
DR   EMBL; AK171494; BAE42490.1; -; mRNA.
DR   IPI; IPI00223482; -.
DR   RefSeq; NP_001153355.1; NM_001159883.1.
DR   UniGene; Mm.480347; -.
DR   ProteinModelPortal; Q3TB24; -.
DR   SMR; Q3TB24; 1-69.
DR   STRING; Q3TB24; -.
DR   PhosphoSite; Q3TB24; -.
DR   PRIDE; Q3TB24; -.
DR   Ensembl; ENSMUST00000116582; ENSMUSP00000112281; ENSMUSG00000026203.
DR   GeneID; 56812; -.
DR   KEGG; mmu:56812; -.
DR   UCSC; uc007bon.1; mouse.
DR   CTD; 56812; -.
DR   MGI; MGI:1928739; Dnajb2.
DR   eggNOG; roNOG10077; -.
DR   GeneTree; ENSGT00600000084029; -.
DR   HOGENOM; HBG716471; -.
DR   HOVERGEN; HBG066998; -.
DR   InParanoid; Q3TB24; -.
DR   ArrayExpress; Q3TB24; -.
DR   Bgee; Q3TB24; -.
DR   Genevestigator; Q3TB24; -.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   InterPro; IPR001623; DnaJ_N.
DR   InterPro; IPR018253; Heat_shock_DnaJ_CS.
DR   InterPro; IPR003095; Hsp_DnaJ.
DR   InterPro; IPR003903; Ubiquitin-int_motif.
DR   Gene3D; G3DSA:1.10.287.110; DnaJ_N; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SMART; SM00726; UIM; 2.
DR   SUPFAM; SSF46565; DnaJ_N; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS50330; UIM; 1.
PE   2: Evidence at transcript level;
KW   Chaperone.
SQ   SEQUENCE   324 AA;  35593 MW;  C00006AAC12574FA CRC64;
     MASYYEILDV PRSASPDDIK KAYRKKALQW HPDKNPDNKE FAEKKFKEVA EAYEVLSDKH
     KREIYDRYGR EGLTGAGSGP SRSETGGAGP GFTFTFRSPE EVFREFFGSG DPFSELFDDL
     GVFSELQNQG PRLTGPFFTF SSSFPANSDF SSSSFSFSPG AGAFRSVSTS TTFVQGRRIT
     TRRIMENGQE RVEVEEDGQL KSVSINGVPD DLALGLELSR REQQPSVAPG LGVMQVRPTS
     LSRPPDHDLS EDEDLQLAMA YSLSEMEAAG QKPAGGRGAQ QRQHGQPKAQ HRDLDVGGTH
     KSVRGEAAKL SPSSEEKASR CHIL
//
ID   Q3TBV3_MOUSE            Unreviewed;       355 AA.
AC   Q3TBV3;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-FEB-2011, entry version 28.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=C78339;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK171039; BAE42204.1; -; mRNA.
DR   IPI; IPI00753544; -.
DR   UniGene; Mm.275934; -.
DR   Ensembl; ENSMUST00000091627; ENSMUSP00000089216; ENSMUSG00000069237.
DR   MGI; MGI:2145496; C78339.
DR   eggNOG; roNOG12341; -.
DR   GeneTree; ENSGT00390000007346; -.
DR   HOVERGEN; HBG054566; -.
DR   ArrayExpress; Q3TBV3; -.
DR   Bgee; Q3TBV3; -.
DR   Genevestigator; Q3TBV3; -.
DR   InterPro; IPR010432; RDD.
DR   Pfam; PF06271; RDD; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   355 AA;  38088 MW;  B52DC10005CC48C1 CRC64;
     MAEGPEEARS RPPEQDGSGG DHEPVPSEPG SPTTTVAATA AAPRSPALAS VASAVSEPEP
     QCELRKRRET GAEPPEAGDC EASDGPGRLS AREYSRQVHE WLWQSYCGYL TWHSGLAALP
     AYCGPPPPAX TGPQPAVPSP SSPPTPSSPH VQPSARAAPG TRVGSAAPAR TASDTGRQAG
     REYVIPSLAH RFMAEMVDFF ILFFIKATIV LSIMHLSGIK DISKFAMHYI IEEIDEDTSM
     EDLQKMMIVA LIYRLLVCFY EIICIWGAGG ATPGKFLLGL RVVTCDTSVL IAPSRVLVIP
     SSNVSITTST IRALIKNFSI ASFFPAFITL LFFQHNRTAY DIVAGTIVVK RNGVR
//
ID   Q3TC53_MOUSE            Unreviewed;       474 AA.
AC   Q3TC53;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   RecName: Full=Adenylyl cyclase-associated protein;
GN   Name=Cap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the CAP family.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK170901; BAE42104.1; -; mRNA.
DR   IPI; IPI00869430; -.
DR   UniGene; Mm.8687; -.
DR   ProteinModelPortal; Q3TC53; -.
DR   SMR; Q3TC53; 43-216, 318-474.
DR   STRING; Q3TC53; -.
DR   Ensembl; ENSMUST00000069533; ENSMUSP00000068260; ENSMUSG00000028656.
DR   Ensembl; ENSMUST00000106255; ENSMUSP00000101862; ENSMUSG00000028656.
DR   Ensembl; ENSMUST00000106257; ENSMUSP00000101864; ENSMUSG00000028656.
DR   MGI; MGI:88262; Cap1.
DR   HOVERGEN; HBG003080; -.
DR   InParanoid; Q3TC53; -.
DR   ArrayExpress; Q3TC53; -.
DR   Bgee; Q3TC53; -.
DR   Genevestigator; Q3TC53; -.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR   GO; GO:0001667; P:ameboidal cell migration; IMP:MGI.
DR   GO; GO:0000902; P:cell morphogenesis; IGI:MGI.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IMP:MGI.
DR   InterPro; IPR001837; Adenylate_cyclase-assoc_CAP.
DR   InterPro; IPR013912; Adenylate_cyclase-assoc_CAP_C.
DR   InterPro; IPR013992; Adenylate_cyclase-assoc_CAP_N.
DR   InterPro; IPR017901; C-CAP_CF_C-like.
DR   InterPro; IPR016098; CAP/MinC_C.
DR   InterPro; IPR018106; CAP_CS.
DR   InterPro; IPR006599; CARP_motif.
DR   Gene3D; G3DSA:2.160.20.70; CAP/MinC_C; 1.
DR   PANTHER; PTHR10652; CAP; 1.
DR   Pfam; PF08603; CAP_C; 1.
DR   Pfam; PF01213; CAP_N; 1.
DR   SMART; SM00673; CARP; 2.
DR   SUPFAM; SSF101278; Adenylate_cyclase-assoc_CAP_N; 1.
DR   SUPFAM; SSF69340; CARP; 1.
DR   PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
DR   PROSITE; PS01088; CAP_1; 1.
DR   PROSITE; PS01089; CAP_2; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   474 AA;  51605 MW;  7A2E875839279622 CRC64;
     MADMQNLVER LERAVGRLEA VSHTSDMHCG YGDSPSKGAV PYVQAFDSLL ANPVAEYLKM
     SKEIGGDVQK HAEMVHTGLK LERALLATAS QCQQPAGNKL SDLLAPISEQ IQEVITFREK
     NRGSKFFNHL SAVSESIQAL GWVALAAKPG PFVKEMNDAA MFYTNRVLKE YRDVDKKHVD
     WVRAYLSIWT ELQAYIKEFH TTGLAWSKTG PVAKELSGLP SGPSVGSGPP PPPPGPPPPP
     IPTSSGSDDS ASRSALFAQI NQGESITHAL KHVSDDMKTH KNPALKAQSG PVRSGPKPFS
     APKPQTSPSP KPATKKEPAL LELEGKKWRV ENQENVSNLV IDDTELKQVA YIYKCVNTTL
     QIKGKINSIT VDNCKKLGLV FDDVVGIVEI INSRDVKVQV MGKVPTISIN KTDGCHAYLS
     KNSLDCEIVS TKSSEMNVLI PTEGGDFNEF PVPEQFKTLW NGQKLVTTVT EIAG
//
ID   FAHD2_MOUSE             Reviewed;         313 AA.
AC   Q3TC72; Q8K0V8;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 47.
DE   RecName: Full=Fumarylacetoacetate hydrolase domain-containing protein 2A;
DE            EC=3.-.-.-;
GN   Name=Fahd2; Synonyms=Fahd2a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   PROTEIN SEQUENCE OF 108-125, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
CC   -!- FUNCTION: May have hydrolase activity (By similarity).
CC   -!- COFACTOR: Calcium (Probable).
CC   -!- COFACTOR: Magnesium (Probable).
CC   -!- SIMILARITY: Belongs to the FAH family.
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DR   EMBL; AK080868; BAC38052.1; -; mRNA.
DR   EMBL; AK170875; BAE42085.1; -; mRNA.
DR   EMBL; BC030182; AAH30182.1; -; mRNA.
DR   EMBL; AL731831; CAM13449.1; -; Genomic_DNA.
DR   IPI; IPI00121218; -.
DR   RefSeq; NP_083905.1; NM_029629.2.
DR   UniGene; Mm.288676; -.
DR   HSSP; Q5SJQ0; 1WZO.
DR   ProteinModelPortal; Q3TC72; -.
DR   SMR; Q3TC72; 27-313.
DR   STRING; Q3TC72; -.
DR   PhosphoSite; Q3TC72; -.
DR   REPRODUCTION-2DPAGE; IPI00121218; -.
DR   REPRODUCTION-2DPAGE; Q3TC72; -.
DR   PRIDE; Q3TC72; -.
DR   Ensembl; ENSMUST00000028848; ENSMUSP00000028848; ENSMUSG00000027371.
DR   GeneID; 68126; -.
DR   KEGG; mmu:68126; -.
DR   CTD; 68126; -.
DR   MGI; MGI:1915376; Fahd2a.
DR   eggNOG; roNOG08619; -.
DR   GeneTree; ENSGT00530000063832; -.
DR   HOGENOM; HBG729228; -.
DR   HOVERGEN; HBG104460; -.
DR   InParanoid; Q3TC72; -.
DR   OrthoDB; EOG4VDQ06; -.
DR   PhylomeDB; Q3TC72; -.
DR   NextBio; 326484; -.
DR   ArrayExpress; Q3TC72; -.
DR   Bgee; Q3TC72; -.
DR   Genevestigator; Q3TC72; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR002529; Fumarylacetoacetase_C-like.
DR   InterPro; IPR011234; Fumarylacetoacetase_C-rel.
DR   Gene3D; G3DSA:3.90.850.10; Fumarylacetoacetase_C-rel; 1.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   SUPFAM; SSF56529; Fumarylacetoacetase_C-rel; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Hydrolase; Magnesium;
KW   Metal-binding.
FT   CHAIN         1    313       Fumarylacetoacetate hydrolase domain-
FT                                containing protein 2A.
FT                                /FTId=PRO_0000289797.
FT   CONFLICT    106    106       E -> D (in Ref. 1; BAC38052, 2; AAH30182
FT                                and 3; CAM13449).
SQ   SEQUENCE   313 AA;  34690 MW;  BEB04730B0371E67 CRC64;
     MLGFGRRRLF SALLQVQKRP CQPSRNMRLV QFQAPHLEEP HLGLESGVGG GVVDLNAFDS
     TLPKTMVQFL EQGETTLSVA RRALATQLPV IPRSQVTFLA PVTRPEKVIC VGLNYADHCQ
     EQNVRVPKSP IIFSKFSSSI VGPYDEIILP PESKEVDWEV EMAVVIGKKG KHIKATDVMA
     HVAGFTVAHD VSARDWQMRN GKQWLLGKTF DTFCPLGPAL VTKDTIADPH NLKICCRVNG
     EVVQSSNTNQ MVFKTEYLIA WVSQFVTLYP GDLLLTGTPP GVGMFRKPPV FLKKGDEVQC
     EIEELGVIIN KVV
//
ID   F175B_MOUSE             Reviewed;         415 AA.
AC   Q3TCJ1; Q3TB08; Q8K0R4;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=BRISC complex subunit Abro1;
DE   AltName: Full=Abraxas brother protein 1;
DE   AltName: Full=Protein FAM175B;
GN   Name=Fam175b; Synonyms=Abro1, Kiaa0157;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 70-415.
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Component of the BRISC complex, a multiprotein complex
CC       that specifically cleaves 'Lys-63'-linked ubiquitin. May act as a
CC       central scaffold protein that assembles the various components of
CC       the BRISC complex (By similarity).
CC   -!- SUBUNIT: Component of the BRISC complex, at least composed of the
CC       FAM175B/ABRO1, BRCC3/BRCC36, BRE/BRCC45 and MERIT40/NBA1. Does not
CC       interact with BRCA1. Binds polyubiquitin (By similarity).
CC   -!- DOMAIN: The MPN-like region is similar to the MPN (JAB/Mov34)
CC       domain (By similarity).
CC   -!- SIMILARITY: Belongs to the FAM175 family. Abro1 subfamily.
CC   -!- CAUTION: Although strongly related to the FAM175A/CCDC98 protein,
CC       lacks the C-terminal pSXXF that constitutes a specific recognition
CC       motif for the BRCT domain of BRCA1.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK170704; BAE41965.1; -; mRNA.
DR   EMBL; AK171524; BAE42506.1; -; mRNA.
DR   EMBL; BC030838; AAH30838.2; -; mRNA.
DR   IPI; IPI00136758; -.
DR   RefSeq; NP_932134.2; NM_198017.2.
DR   UniGene; Mm.274824; -.
DR   ProteinModelPortal; Q3TCJ1; -.
DR   PhosphoSite; Q3TCJ1; -.
DR   PRIDE; Q3TCJ1; -.
DR   Ensembl; ENSMUST00000084497; ENSMUSP00000081541; ENSMUSG00000030965.
DR   GeneID; 109359; -.
DR   KEGG; mmu:109359; -.
DR   UCSC; uc009kcq.1; mouse.
DR   CTD; 109359; -.
DR   MGI; MGI:1926116; Fam175b.
DR   eggNOG; roNOG09494; -.
DR   GeneTree; ENSGT00530000063424; -.
DR   HOGENOM; HBG714253; -.
DR   HOVERGEN; HBG081817; -.
DR   InParanoid; Q3TCJ1; -.
DR   OMA; QITQRKN; -.
DR   OrthoDB; EOG4T1HMW; -.
DR   NextBio; 361963; -.
DR   ArrayExpress; Q3TCJ1; -.
DR   Bgee; Q3TCJ1; -.
DR   Genevestigator; Q3TCJ1; -.
DR   GermOnline; ENSMUSG00000030965; Mus musculus.
DR   GO; GO:0070552; C:BRISC complex; ISS:UniProtKB.
DR   GO; GO:0031593; F:polyubiquitin binding; ISS:UniProtKB.
DR   InterPro; IPR023238; FAM175.
DR   InterPro; IPR023240; FAM175_BRISC_cplx_Abro1_su.
DR   PRINTS; PR02053; BRISCABRO1.
DR   PRINTS; PR02051; PROTEINF175.
PE   2: Evidence at transcript level;
KW   Coiled coil; Phosphoprotein.
FT   CHAIN         1    415       BRISC complex subunit Abro1.
FT                                /FTId=PRO_0000050726.
FT   REGION        6    116       MPN-like (By similarity).
FT   COILED      215    266       Potential.
FT   MOD_RES     280    280       Phosphoserine (By similarity).
FT   MOD_RES     308    308       Phosphotyrosine (By similarity).
FT   MOD_RES     342    342       Phosphotyrosine (By similarity).
FT   MOD_RES     368    368       Phosphoserine (By similarity).
FT   MOD_RES     372    372       Phosphoserine (By similarity).
FT   MOD_RES     375    375       Phosphoserine (By similarity).
SQ   SEQUENCE   415 AA;  46943 MW;  C9CB374DA089AFA3 CRC64;
     MAASISGYTF SAVCFHSANS NADHEGFLLG EVRQEETFSI SDSQISNTEF LQVIEIHNHQ
     PCSQLFSFYD YASKVNEESL DRILKDRRKK VIGWYRFRRN TQQQMSYREQ VIHKQLTRIL
     GVPDLVFLLF SFISTANNST HALEYVLFRP NRRYNQRISL AIPNLGNTSQ QEYKVSSVPN
     TSQSYAKVIK EHGTDFFDKD GVMKDIRAIY QVYNALQEKV QAVCADVEKS ERVVESCQAE
     VNKLRRQITQ KKNEKEQERR LQQALLSRQM PSESLEPAFS PRMSYSGFSA EGRSTLAETE
     PSDPPPPYSD FHPNNQESTL SHSRMERSVF MPRPQAVGSS SYASTSGGLK FTGSGADLLP
     SQSAAGDSGE ESDDSDYENL IDPAESPHSE YSHSKNSRPS THPDEDPRNT QTSQI
//
ID   PSL1_MOUSE              Reviewed;         578 AA.
AC   Q3TD49; Q3TLQ8; Q3UG60; Q80VZ6;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Signal peptide peptidase-like 2B;
DE            Short=SPP-like 2B;
DE            Short=SPPL2b;
DE            EC=3.4.23.-;
GN   Name=Sppl2b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Dendritic cell, Mammary gland, and Melanoma;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 88-578 (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Functions as an intramembrane protease. Functions in
CC       ITM2B processing (By similarity).
CC   -!- SUBUNIT: Interacts with ITM2B (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3TD49-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3TD49-2; Sequence=VSP_018571, VSP_018572;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the peptidase A22B family.
CC   -!- SIMILARITY: Contains 1 PA (protease associated) domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK148109; BAE28349.1; -; mRNA.
DR   EMBL; AK166364; BAE38734.1; -; mRNA.
DR   EMBL; AK170375; BAE41755.1; -; mRNA.
DR   EMBL; BC052094; AAH52094.1; -; mRNA.
DR   IPI; IPI00312757; -.
DR   IPI; IPI00752386; -.
DR   RefSeq; NP_780404.2; NM_175195.3.
DR   UniGene; Mm.3285; -.
DR   ProteinModelPortal; Q3TD49; -.
DR   SMR; Q3TD49; 76-157.
DR   STRING; Q3TD49; -.
DR   MEROPS; A22.004; -.
DR   PRIDE; Q3TD49; -.
DR   Ensembl; ENSMUST00000035597; ENSMUSP00000036289; ENSMUSG00000035206.
DR   GeneID; 73218; -.
DR   KEGG; mmu:73218; -.
DR   UCSC; uc007gfc.1; mouse.
DR   UCSC; uc007gfd.1; mouse.
DR   MGI; MGI:1920468; 3110056O03Rik.
DR   eggNOG; maNOG08941; -.
DR   HOGENOM; HBG713902; -.
DR   HOVERGEN; HBG024193; -.
DR   InParanoid; Q3TD49; -.
DR   OMA; TPVMICV; -.
DR   OrthoDB; EOG4Q2DF6; -.
DR   PhylomeDB; Q3TD49; -.
DR   NextBio; 337685; -.
DR   ArrayExpress; Q3TD49; -.
DR   Bgee; Q3TD49; -.
DR   CleanEx; MM_3110056O03RIK; -.
DR   Genevestigator; Q3TD49; -.
DR   GermOnline; ENSMUSG00000035206; Mus musculus.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   InterPro; IPR006639; Peptidase_A22.
DR   InterPro; IPR007369; Peptidase_A22B_SPP.
DR   InterPro; IPR003137; Protease-assoc_domain.
DR   PANTHER; PTHR12174; Peptidase_A22B; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF04258; Peptidase_A22B; 1.
DR   SMART; SM00730; PSN; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Golgi apparatus; Hydrolase; Membrane; Protease;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    578       Signal peptide peptidase-like 2B.
FT                                /FTId=PRO_0000236076.
FT   TOPO_DOM      1    168       Cytoplasmic (Potential).
FT   TRANSMEM    169    189       Helical; (Potential).
FT   TRANSMEM    217    237       Helical; (Potential).
FT   TRANSMEM    240    260       Helical; (Potential).
FT   TRANSMEM    287    307       Helical; (Potential).
FT   TRANSMEM    342    362       Helical; (Potential).
FT   TRANSMEM    406    426       Helical; (Potential).
FT   TRANSMEM    439    459       Helical; (Potential).
FT   DOMAIN       49    149       PA.
FT   COMPBIAS     10     13       Poly-Leu.
FT   COMPBIAS    343    348       Poly-Leu.
FT   ACT_SITE    352    352       By similarity.
FT   ACT_SITE    414    414       By similarity.
FT   VAR_SEQ     499    504       KDAPQT -> VNTSLL (in isoform 2).
FT                                /FTId=VSP_018571.
FT   VAR_SEQ     505    578       Missing (in isoform 2).
FT                                /FTId=VSP_018572.
FT   CONFLICT    151    151       R -> H (in Ref. 1; BAE38734).
FT   CONFLICT    194    194       K -> KR (in Ref. 1; BAE41755).
FT   CONFLICT    319    319       D -> G (in Ref. 1; BAE41755).
FT   CONFLICT    514    514       P -> R (in Ref. 1; BAE38734).
FT   CONFLICT    541    541       A -> T (in Ref. 1; BAE38734).
FT   CONFLICT    549    549       D -> N (in Ref. 1; BAE38734).
SQ   SEQUENCE   578 AA;  63824 MW;  864ED8504F5B6873 CRC64;
     MAAARLAAAL LLLAAQVACE FGVLRVVSQT SRTRSRDYCI LYNPQWAHLP HDLSKVSLLK
     LRDLSTTQLC SYLDVPAEDF TNQIALVARG NCTFYEKVRL AQGSGAHGLL IVSKEKLVPP
     GGNKTQYEEI SIPVALLSHR DLQDIFRRFG REVMVALYAP SEPVMDYNMV IIFVMAVGTV
     AIGGYWAGSH DVKKYMKHKR DDGPEKQEDE AVDVTPVMIC VFVVMCCFML VLLYYFYDRL
     VYVIIGIFCL ASSTGLYSCL APFVRKLPFC TCRVPDNNLP YFHKRPQARM LLLALFCVTV
     SVVWGIFRNE DQWAWVLQDT LGIAFCLYML KTIRLPTFKA CTLLLLVLFI YDIFFVFITP
     FLTKSGNSIM VEVATGPSNS STHEKLPMVL KVPRLNTSPL SLCDRPFSLL GFGDILVPGL
     LVAYCHRFDI QVQSSRIYFV ACTIAYGLGL LVTFVALVLM QRGQPALLYL VPCTLLTSCT
     VALWRRELGA FWTGSGFAKD APQTPWAATQ GPVPPKAVGS SLSEQPPSEE LAKSPLSTEE
     AGAADPAKDP DNPVASPLSP SNGDEAQPIP VVKPETSA
//
ID   ROGDI_MOUSE             Reviewed;         287 AA.
AC   Q3TDK6; Q8BL37; Q922N4; Q923H8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   08-MAR-2011, entry version 38.
DE   RecName: Full=Protein rogdi homolog;
DE   AltName: Full=Leucine-zipper-containing LZF;
GN   Name=Rogdi; Synonyms=Lzf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND POSSIBLE FUNCTION.
RX   PubMed=11740862; DOI=10.1006/excr.2001.5394;
RA   Tulin E.E., Onoda N., Hasegawa M., Nosaka T., Nomura H., Kitamura T.;
RT   "Genetic approach and phenotype-based complementation screening for
RT   identification of stroma cell-derived proteins involved in cell
RT   proliferation.";
RL   Exp. Cell Res. 272:23-31(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Corpora quadrigemina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May act as a positive regulator of cell proliferation.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3TDK6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3TDK6-2; Sequence=VSP_030600;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q3TDK6-3; Sequence=VSP_030601;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the rogdi family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK71345.1; Type=Frameshift; Positions=3, 158, 167;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY036117; AAK71345.1; ALT_FRAME; mRNA.
DR   EMBL; AK046477; BAC32748.1; -; mRNA.
DR   EMBL; AK170144; BAE41595.1; -; mRNA.
DR   EMBL; BC006914; AAH06914.1; -; mRNA.
DR   IPI; IPI00399812; -.
DR   IPI; IPI00624881; -.
DR   IPI; IPI00882124; -.
DR   RefSeq; NP_573448.2; NM_133185.2.
DR   UniGene; Mm.27792; -.
DR   PRIDE; Q3TDK6; -.
DR   Ensembl; ENSMUST00000023191; ENSMUSP00000023191; ENSMUSG00000022540.
DR   Ensembl; ENSMUST00000090453; ENSMUSP00000087938; ENSMUSG00000022540.
DR   GeneID; 66049; -.
DR   KEGG; mmu:66049; -.
DR   UCSC; uc007ybk.1; mouse.
DR   CTD; 66049; -.
DR   MGI; MGI:1913299; Rogdi.
DR   eggNOG; maNOG06548; -.
DR   GeneTree; ENSGT00390000007164; -.
DR   HOGENOM; HBG716997; -.
DR   HOVERGEN; HBG087014; -.
DR   InParanoid; Q3TDK6; -.
DR   OMA; RNNQLLH; -.
DR   OrthoDB; EOG4DNF4X; -.
DR   NextBio; 320474; -.
DR   ArrayExpress; Q3TDK6; -.
DR   Bgee; Q3TDK6; -.
DR   CleanEx; MM_ROGDI; -.
DR   Genevestigator; Q3TDK6; -.
DR   GO; GO:0030097; P:hemopoiesis; IDA:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
DR   InterPro; IPR019386; Rogdi_leu_zipper-containing.
DR   PANTHER; PTHR13618; Rogdi_leu_zipper-containing; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing.
FT   CHAIN         1    287       Protein rogdi homolog.
FT                                /FTId=PRO_0000315665.
FT   VAR_SEQ      85     85       A -> ALPPGWLRRLGPQPSPHCIAGSQ (in isoform
FT                                2).
FT                                /FTId=VSP_030600.
FT   VAR_SEQ     205    287       QLHALQPTSTKNFRPAGGAVLHSPGAMFEWGSQRLEVSHVH
FT                                KVECVIPWLNDALVYFTVSLQLCQQLKDKIAVFSSYWSSRP
FT                                F -> HLFCDPTHL (in isoform 3).
FT                                /FTId=VSP_030601.
FT   CONFLICT    158    158       S -> N (in Ref. 1; AAK71345).
FT   CONFLICT    164    164       A -> T (in Ref. 1; AAK71345).
FT   CONFLICT    193    193       Y -> H (in Ref. 2; BAE41595).
SQ   SEQUENCE   287 AA;  32100 MW;  5F47C4A8073B1A04 CRC64;
     MATAMAASAA ERAVLEEEFR WLLHAEVHAV LRQLQDILKE ASLRFTLPGP STEGPAKQEN
     FILGSCGTDQ VKGTLTLQGD ALSQADVNLK MPRNNQLLHL AFREDKQWKL QQIQDARNHV
     SQAIYLLANR DESYQFKTGA EVLKLMDAVM LQLTRARSRL TTPATLTLPE IAASGLTRMF
     APTLPSDLLV NVYINLNKLC LTVYQLHALQ PTSTKNFRPA GGAVLHSPGA MFEWGSQRLE
     VSHVHKVECV IPWLNDALVY FTVSLQLCQQ LKDKIAVFSS YWSSRPF
//
ID   FAF2_MOUSE              Reviewed;         445 AA.
AC   Q3TDN2; Q3U9W2; Q80TP7; Q80W42;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=FAS-associated factor 2;
DE   AltName: Full=UBX domain-containing protein 8;
GN   Name=Faf2; Synonyms=Kiaa0887, Ubxd8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-445 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
CC   -!- FUNCTION: May play a role in the translocation of terminally
CC       misfolded proteins from the endoplasmic reticulum lumen to the
CC       cytoplasm and their degradation by the proteasome (By similarity).
CC   -!- SUBUNIT: Identified in a complex that contains SEL1L, OS9,
CC       FAF2/UBXD8, UBE2J1/UBC6E and AUP1. Interacts with YOD1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Lipid droplet (By
CC       similarity). Endoplasmic reticulum (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3TDN2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3TDN2-2; Sequence=VSP_019504;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 UBA domain.
CC   -!- SIMILARITY: Contains 1 UBX domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK151617; BAE30554.1; -; mRNA.
DR   EMBL; AK170111; BAE41569.1; -; mRNA.
DR   EMBL; BC046817; AAH46817.1; -; mRNA.
DR   EMBL; AK122394; BAC65676.1; -; mRNA.
DR   IPI; IPI00265386; -.
DR   IPI; IPI00761513; -.
DR   RefSeq; NP_848484.2; NM_178397.3.
DR   UniGene; Mm.194459; -.
DR   ProteinModelPortal; Q3TDN2; -.
DR   SMR; Q3TDN2; 2-56, 129-273, 353-445.
DR   STRING; Q3TDN2; -.
DR   PhosphoSite; Q3TDN2; -.
DR   PRIDE; Q3TDN2; -.
DR   Ensembl; ENSMUST00000026991; ENSMUSP00000026991; ENSMUSG00000025873.
DR   GeneID; 76577; -.
DR   KEGG; mmu:76577; -.
DR   UCSC; uc007qoq.1; mouse.
DR   UCSC; uc007qor.1; mouse.
DR   CTD; 76577; -.
DR   MGI; MGI:1923827; Faf2.
DR   eggNOG; roNOG13095; -.
DR   GeneTree; ENSGT00530000063422; -.
DR   HOGENOM; HBG445729; -.
DR   HOVERGEN; HBG101311; -.
DR   InParanoid; Q3TDN2; -.
DR   OMA; KYGRIHP; -.
DR   OrthoDB; EOG4BVRTS; -.
DR   PhylomeDB; Q3TDN2; -.
DR   NextBio; 345388; -.
DR   ArrayExpress; Q3TDN2; -.
DR   Bgee; Q3TDN2; -.
DR   Genevestigator; Q3TDN2; -.
DR   GermOnline; ENSMUSG00000025873; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005811; C:lipid particle; IEA:UniProtKB-SubCell.
DR   GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR   InterPro; IPR006577; UAS.
DR   InterPro; IPR009060; UBA-like.
DR   InterPro; IPR000449; UBA/transl_elong_EF1B_N.
DR   InterPro; IPR001012; UBX.
DR   Pfam; PF00627; UBA; 1.
DR   Pfam; PF00789; UBX; 1.
DR   SMART; SM00594; UAS; 1.
DR   SUPFAM; SSF46934; UBA_like; 1.
DR   PROSITE; PS50030; UBA; FALSE_NEG.
DR   PROSITE; PS50033; UBX; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW   Endoplasmic reticulum; Lipid droplet; Phosphoprotein;
KW   Unfolded protein response.
FT   CHAIN         1    445       FAS-associated factor 2.
FT                                /FTId=PRO_0000244065.
FT   DOMAIN       12     48       UBA.
FT   DOMAIN      357    439       UBX.
FT   COILED      275    350       Potential.
FT   MOD_RES      79     79       Phosphotyrosine (By similarity).
FT   MOD_RES     167    167       N6-acetyllysine (By similarity).
FT   VAR_SEQ      71     89       Missing (in isoform 2).
FT                                /FTId=VSP_019504.
FT   CONFLICT     72     72       Missing (in Ref. 2; AAH46817).
FT   CONFLICT    430    434       GLSHT -> DSATQ (in Ref. 1; BAE41569).
SQ   SEQUENCE   445 AA;  52471 MW;  F0FD0FC631148AE7 CRC64;
     MAAPEEQDLT QEQTEKLLQF QDLTGIESME QCRLALEQHN WNMEAAVQDR LNEQEGVPSV
     FNPPPARPLQ VNTADHRIYS YVVSRPQPRG LLGWGYYLIM LPFRFTYYTI LDIFRFALRF
     IRPDPRSRVT DPVGDIVSFM HSFEEKYGRA HPVFYQGTYS QALNDAKREL RFLLVYLHGD
     DHQDSDEFCR NALCAPEVIS LINSRMLFWA CSTNKPEGYR VSQALRENTY PFLAMIMLKD
     RRMTVVGRLE GLIQPDDLIN QLTFIMDANQ TYLVSERLER EERNQTQVLR QQQDEAYLAS
     LRADQEKERK KREEKERKRR KEEEVQQQKL AEERRRQNLQ EEKERKLECL PPEPSPDDPE
     SVKIIFKLPN DSRVERRFHF SQSLTVIHDF LFSLKESPEK FQIEANFPRR VLPCVPSEEW
     PNPPTLQEAG LSHTEVLFVQ DLTDE
//
ID   STT3B_MOUSE             Reviewed;         823 AA.
AC   Q3TDQ1; Q7TT24; Q921E3; Q99LL0; Q9D2V2;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B;
DE            Short=Oligosaccharyl transferase subunit STT3B;
DE            Short=STT3-B;
DE            EC=2.4.1.119;
DE   AltName: Full=B6dom1 antigen;
DE   AltName: Full=Source of immunodominant MHC-associated peptides;
GN   Name=Stt3b; Synonyms=Simp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, Czech II, and FVB/N;
RC   TISSUE=Brain, Mammary gland, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 770-778, AND VARIANT ASP-776.
RC   STRAIN=C57BL/6;
RX   MEDLINE=22326278; PubMed=12439619; DOI=10.1007/s00251-002-0502-4;
RA   McBride K., Baron C., Picard S., Martin S., Boismenu D., Bell A.,
RA   Bergeron J., Perreault C.;
RT   "The model B6dom1 minor histocompatibility antigen is encoded by a
RT   mouse homolog of the yeast STT3 gene.";
RL   Immunogenetics 54:562-569(2002).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495 AND SER-496, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495 AND SER-496, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495 AND SER-496, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495 AND SER-496, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-624 AND ASN-638, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Component of the N-oligosaccharyl transferase enzyme
CC       which catalyzes the transfer of a high mannose oligosaccharide
CC       from a lipid-linked oligosaccharide donor to an asparagine residue
CC       within an Asn-X-Ser/Thr consensus motif in nascent polypeptide
CC       chains. N-glycosylation occurs cotranslationally and the complex
CC       associates with the Sec61 complex at the channel-forming
CC       translocon complex that mediates protein translocation across the
CC       endoplasmic reticulum (ER). SST3B seems to be involved in complex
CC       substrate specificity (By similarity).
CC   -!- CATALYTIC ACTIVITY: Dolichyl diphosphooligosaccharide + protein L-
CC       asparagine = dolichyl diphosphate + a glycoprotein with the
CC       oligosaccharide chain attached by N-glycosyl linkage to protein L-
CC       asparagine.
CC   -!- SUBUNIT: Component of the oligosaccharyltransferase (OST) complex.
CC       OST seems to exist in different forms which contain at least RPN1,
CC       RPN2, OST48, DAD1, OSTC, KRTCAP2 and either STT3A or STT3B. OST
CC       can form stable complexes with the Sec61 complex or with both the
CC       Sec61 and TRAP complexes (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
CC   -!- POLYMORPHISM: In strains 129, C57BL/10, C57BL/6 and LP Glu-776
CC       correlates with a B6dom1-positive phenotype, Asp-776 is found in
CC       resistant strains. The B6dom1 minor histocompatibilty antigen
CC       (MiHA) is used as a model antigen in studying immunodominance.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH13054.2; Type=Erroneous initiation;
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DR   EMBL; AK018758; BAB31390.1; -; mRNA.
DR   EMBL; AK145674; BAE26582.1; -; mRNA.
DR   EMBL; AK154979; BAE32968.1; -; mRNA.
DR   EMBL; AK152899; BAE31580.1; -; mRNA.
DR   EMBL; AK170079; BAE41550.1; -; mRNA.
DR   EMBL; BC003206; AAH03206.1; -; mRNA.
DR   EMBL; BC013054; AAH13054.2; ALT_INIT; mRNA.
DR   EMBL; BC052433; AAH52433.1; -; mRNA.
DR   IPI; IPI00316469; -.
DR   RefSeq; NP_077184.2; NM_024222.2.
DR   UniGene; Mm.296158; -.
DR   ProteinModelPortal; Q3TDQ1; -.
DR   SMR; Q3TDQ1; 579-682.
DR   IntAct; Q3TDQ1; 1.
DR   STRING; Q3TDQ1; -.
DR   CAZy; GT66; Glycosyltransferase Family 66.
DR   PhosphoSite; Q3TDQ1; -.
DR   PRIDE; Q3TDQ1; -.
DR   Ensembl; ENSMUST00000035010; ENSMUSP00000035010; ENSMUSG00000032437.
DR   GeneID; 68292; -.
DR   KEGG; mmu:68292; -.
DR   UCSC; uc009ryp.1; mouse.
DR   CTD; 68292; -.
DR   MGI; MGI:1915542; Stt3b.
DR   eggNOG; roNOG09233; -.
DR   HOGENOM; HBG314442; -.
DR   HOVERGEN; HBG010606; -.
DR   InParanoid; Q3TDQ1; -.
DR   OrthoDB; EOG4VT5WM; -.
DR   PhylomeDB; Q3TDQ1; -.
DR   BRENDA; 2.4.1.119; 244.
DR   NextBio; 326937; -.
DR   ArrayExpress; Q3TDQ1; -.
DR   Bgee; Q3TDQ1; -.
DR   Genevestigator; Q3TDQ1; -.
DR   GermOnline; ENSMUSG00000032437; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008250; C:oligosaccharyltransferase complex; ISS:HGNC.
DR   GO; GO:0004579; F:dolichyl-diphosphooligosaccharide-protein glycotransferase activity; IEA:EC.
DR   GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISS:HGNC.
DR   InterPro; IPR003674; Oligo_trans_STT3.
DR   Pfam; PF02516; STT3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Endoplasmic reticulum;
KW   Glycoprotein; Membrane; Phosphoprotein; Polymorphism; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    823       Dolichyl-diphosphooligosaccharide--
FT                                protein glycosyltransferase subunit
FT                                STT3B.
FT                                /FTId=PRO_0000246002.
FT   TRANSMEM     62     82       Helical; (Potential).
FT   TRANSMEM    134    154       Helical; (Potential).
FT   TRANSMEM    166    186       Helical; (Potential).
FT   TRANSMEM    189    209       Helical; (Potential).
FT   TRANSMEM    240    256       Helical; (Potential).
FT   TRANSMEM    260    280       Helical; (Potential).
FT   TRANSMEM    289    309       Helical; (Potential).
FT   TRANSMEM    317    337       Helical; (Potential).
FT   TRANSMEM    348    368       Helical; (Potential).
FT   TRANSMEM    408    428       Helical; (Potential).
FT   TRANSMEM    438    458       Helical; (Potential).
FT   TRANSMEM    461    481       Helical; (Potential).
FT   TRANSMEM    535    555       Helical; (Potential).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      18     18       Phosphoserine (By similarity).
FT   MOD_RES      29     29       Phosphoserine (By similarity).
FT   MOD_RES     495    495       Phosphoserine.
FT   MOD_RES     496    496       Phosphoserine.
FT   CARBOHYD    624    624       N-linked (GlcNAc...).
FT   CARBOHYD    638    638       N-linked (GlcNAc...).
FT   VARIANT     776    776       E -> D (in strain: A.BY, B10.H7 and
FT                                C3H.SW; correlated with B6dom1-negative
FT                                phenotype).
FT   CONFLICT     43     43       S -> R (in Ref. 1; BAE41550 and 2;
FT                                AAH03206).
FT   CONFLICT    240    240       T -> I (in Ref. 1; BAE41550).
FT   CONFLICT    294    294       F -> L (in Ref. 1; BAB31390).
SQ   SEQUENCE   823 AA;  93246 MW;  BBC27DB07EE609D1 CRC64;
     MAEPSAPESK HKSSLNSSPW SGLMALGNSR HGHHGPGTQS ASSAAAPKPG PPAGLSGGLS
     QPAGWQSLLS FTILFLAWLA GFSSRLFAVI RFESIIHEFD PWFNYRSTHH LASHGFYEFL
     NWFDERAWYP LGRIVGGTVY PGLMITAGLI HWILNTLNIT VHIRDVCVFL APTFSGLTSI
     STFLLTRELW NQGAGLLAAC FIAIVPGYIS RSVAGSFDNE GIAIFALQFT YYLWVKSVKT
     GSVFWTMCCC LSYFYMVSAW GGYVFIINLI PLHVFVLLLM QRYSKRVYIA YSTFYIVGLI
     LSMQIPFVGF QPIRTSEHMA AAGVFALLQA YAFLQYLRDR LTKQEFQTLF FLGVSLAAGA
     VFLSVIYLTY TGYIAPWSGR FYSLWDTGYA KIHIPIIASV SEHQPTTWVS FFFDLHILVC
     TFPAGLWFCI KNINDERVFV ALYAISAVYF AGVMVRLMLT LTPVVCMLSA IAFSNVFEHY
     LGDDMKRENP PVEDSSDEDD KRNPGNLYDK AGKVRKHVTE QEKPEEGLGP NIKSIVTMLM
     LMLLMMFAVH CTWVTSNAYS SPSVVLASYN HDGTRNILDD FREAYFWLRQ NTDEHARVMS
     WWDYGYQIAG MANRTTLVDN NTWNNSHIAL VGKAMSSNET AAYKIMRSLD VDYVLVIFGG
     VIGYSGDDIN KFLWMVRIAE GEHPKDIREG DYFTQQGEFR VDKAGSPTLL NCLMYKMSYY
     RFGEMQLDFR TPPGFDRTRN AEIGNKDIKF KHLEEAFTSE HWLVRIYKVK APDNRETLGH
     KPRVTNIVPK QKYLSKKTTK RKRGYVKNKL VFKKGKKTSK KTV
//
ID   Q3TE01_MOUSE            Unreviewed;       582 AA.
AC   Q3TE01;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 33.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=C2cd2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK169902; BAE41447.1; -; mRNA.
DR   IPI; IPI00330753; -.
DR   UniGene; Mm.1465; -.
DR   STRING; Q3TE01; -.
DR   Ensembl; ENSMUST00000060801; ENSMUSP00000058669; ENSMUSG00000045975.
DR   MGI; MGI:1891883; C2cd2.
DR   eggNOG; roNOG09269; -.
DR   HOVERGEN; HBG098030; -.
DR   InParanoid; Q3TE01; -.
DR   OrthoDB; EOG4S4PGC; -.
DR   ArrayExpress; Q3TE01; -.
DR   Bgee; Q3TE01; -.
DR   Genevestigator; Q3TE01; -.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
PE   2: Evidence at transcript level;
FT   NON_TER     582    582
SQ   SEQUENCE   582 AA;  63810 MW;  FEF5C46E130DF89E CRC64;
     MGSWLSEVQW LFLVSLFVAA LGTVGLYLAQ WALAKARPPP RRRAEPDELR RRESDTLLSW
     ILTRDSWGNQ WQAAWVTALN YESEKRGGPL RLSFQKDPRP QSLQLTVEKV SSVVKSTQEK
     VVICHVVGET LQFLVSAGPA SATGSECQLY DVHLSPFHLK VEFHMEEKRE DIQIRWSFTH
     VPETAIKIQP QAPGENKALG VNMLSEALED LFKHLVNAAS PSVFLSTKPT QVKEAQSLQC
     PSSTAQEPCP PKPPRAHELK LQVKNIRVSL INHPGASGLS HVCVAQLNDP EQRFISTLVR
     NTTDLSWEEE FTFELNAKSK ELVLQISQDG CSSEGLLGIA TIHLDLFRKQ PNGPQTFRLI
     SGTEPDSLVL GSVTAEFSYV EPGELKSWPA PPPVSAAKIE KDRTVMPCGT VVTTVTAVKT
     KPRFDTGRAT PLNSESPVRT PVTVKVIEKD ISVQAISCHS APVSKTFSSS DTELLVLNGS
     DPVAEVAIRQ LSESSKLKLK SPRKKSTIII SGISKTSLSQ DHNAALMLDY AASMDSTNQG
     DATSALCHPE ATEASATTPP EENEPAQTLP ALKPRENDLD SW
//
ID   HP1B3_MOUSE             Reviewed;         554 AA.
AC   Q3TEA8; A2AM64; A2AM68; Q3TM38; Q3TU07; Q61688; Q8BT17; Q8C6H2;
AC   Q8C911; Q8VE06; Q99KR0; Q9DBI1;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-FEB-2011, entry version 48.
DE   RecName: Full=Heterochromatin protein 1-binding protein 3;
GN   Name=Hp1bp3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Cerebellum, Liver, Lung, Skin, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 43-324, FUNCTION, AND INTERACTION WITH
RP   CBX5.
RX   MEDLINE=97133299; PubMed=8978696;
RA   le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H.,
RA   Jeanmougin F., Losson R., Chambon P.;
RT   "A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic
RT   control of transcription by nuclear receptors.";
RL   EMBO J. 15:6701-6715(1996).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431; SER-443; SER-444
RP   AND SER-447, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Component of heterochromatin, may be involved in
CC       chromatin structure and function.
CC   -!- SUBUNIT: Interacts with CBX5.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Chromosome (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3TEA8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3TEA8-2; Sequence=VSP_034175;
CC       Name=3;
CC         IsoId=Q3TEA8-3; Sequence=VSP_034174;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 3 H15 (linker histone H1/H5 globular)
CC       domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC35912.1; Type=Frameshift; Positions=13, 313;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK004938; BAB23683.1; -; mRNA.
DR   EMBL; AK028181; BAC25794.1; -; mRNA.
DR   EMBL; AK043260; BAC31507.1; -; mRNA.
DR   EMBL; AK075725; BAC35912.1; ALT_FRAME; mRNA.
DR   EMBL; AK161041; BAE36164.1; -; mRNA.
DR   EMBL; AK166161; BAE38604.1; -; mRNA.
DR   EMBL; AK169740; BAE41340.1; -; mRNA.
DR   EMBL; AL807249; CAM18860.1; -; Genomic_DNA.
DR   EMBL; AL807249; CAM18863.1; -; Genomic_DNA.
DR   EMBL; BC004053; AAH04053.1; -; mRNA.
DR   EMBL; BC020024; AAH20024.1; -; mRNA.
DR   EMBL; X99642; CAA67961.1; -; mRNA.
DR   IPI; IPI00342766; -.
DR   IPI; IPI00649131; -.
DR   IPI; IPI00896020; -.
DR   RefSeq; NP_001116368.1; NM_001122896.1.
DR   RefSeq; NP_001116369.1; NM_001122897.1.
DR   RefSeq; NP_034600.2; NM_010470.2.
DR   UniGene; Mm.399941; -.
DR   ProteinModelPortal; Q3TEA8; -.
DR   SMR; Q3TEA8; 159-234, 255-330, 338-413.
DR   PRIDE; Q3TEA8; -.
DR   Ensembl; ENSMUST00000030541; ENSMUSP00000030541; ENSMUSG00000028759.
DR   GeneID; 15441; -.
DR   KEGG; mmu:15441; -.
DR   CTD; 15441; -.
DR   MGI; MGI:109369; Hp1bp3.
DR   GeneTree; ENSGT00510000047652; -.
DR   HOVERGEN; HBG097678; -.
DR   PhylomeDB; Q3TEA8; -.
DR   NextBio; 288226; -.
DR   ArrayExpress; Q3TEA8; -.
DR   Bgee; Q3TEA8; -.
DR   Genevestigator; Q3TEA8; -.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   InterPro; IPR005818; Histone_H1/H5.
DR   InterPro; IPR005819; Histone_H5.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 3.
DR   Pfam; PF00538; Linker_histone; 3.
DR   PRINTS; PR00624; HISTONEH5.
DR   SMART; SM00526; H15; 3.
DR   PROSITE; PS51504; H15; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Chromosome; DNA-binding; Nucleus;
KW   Phosphoprotein; Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    554       Heterochromatin protein 1-binding protein
FT                                3.
FT                                /FTId=PRO_0000339643.
FT   DOMAIN      159    234       H15 1.
FT   DOMAIN      255    330       H15 2.
FT   DOMAIN      337    413       H15 3.
FT   COMPBIAS     59    128       Glu-rich.
FT   COMPBIAS    432    441       Poly-Asp.
FT   COMPBIAS    455    554       Lys-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       6      6       Phosphoserine (By similarity).
FT   MOD_RES      51     51       Phosphothreonine.
FT   MOD_RES     134    134       Phosphothreonine (By similarity).
FT   MOD_RES     144    144       Phosphoserine (By similarity).
FT   MOD_RES     158    158       Phosphoserine (By similarity).
FT   MOD_RES     192    192       N6-acetyllysine (By similarity).
FT   MOD_RES     249    249       Phosphoserine (By similarity).
FT   MOD_RES     431    431       Phosphoserine.
FT   MOD_RES     443    443       Phosphoserine.
FT   MOD_RES     444    444       Phosphoserine.
FT   MOD_RES     447    447       Phosphoserine.
FT   VAR_SEQ       1     38       Missing (in isoform 3).
FT                                /FTId=VSP_034174.
FT   VAR_SEQ      67     79       Missing (in isoform 2).
FT                                /FTId=VSP_034175.
FT   CONFLICT     68     68       D -> N (in Ref. 1; BAE36164).
FT   CONFLICT    110    110       N -> S (in Ref. 4; CAA67961 and 3;
FT                                AAH20024).
FT   CONFLICT    111    111       K -> E (in Ref. 1; BAB23683).
FT   CONFLICT    174    174       C -> S (in Ref. 2; CAM18860/CAM18863).
FT   CONFLICT    197    197       G -> D (in Ref. 4; CAA67961 and 3;
FT                                AAH04053/AAH20024).
FT   CONFLICT    219    219       R -> K (in Ref. 4; CAA67961 and 3;
FT                                AAH04053/AAH20024).
FT   CONFLICT    247    247       Missing (in Ref. 1; BAC25794).
FT   CONFLICT    403    403       K -> R (in Ref. 1; BAE38604).
FT   CONFLICT    436    436       E -> D (in Ref. 3; AAH04053/AAH20024).
FT   CONFLICT    440    441       Missing (in Ref. 3; AAH04053).
FT   CONFLICT    547    547       K -> E (in Ref. 1; BAE36164).
SQ   SEQUENCE   554 AA;  60867 MW;  A49C4F7C42D1BE64 CRC64;
     MATDMSQGEL IHPKALPLIV GAQLIHADKL GEKAEDTTMP IRRAVNSTRE TPPKSKLAEG
     EEEKPEPDGS SEESISTVEE QENETPPATS SEAEQPKGEP ESGEKEENNN KSAEEPKKDE
     KDQSKEKEKK VKKTIPAWAT LSASQLARAQ RQTPMASSPR PKMDAILTEA IKACFQKTGA
     SVVAIRKYII HKYPSLGLER RGYLLKQALK RELNRGVIRQ VKGKGASGSF VVVQKSKPPQ
     KSKNRKKGSA LDPEPQVKLE DVLPLAFTRL CEPKEASYSL IRKYVSQYYP KLRVDIRPQL
     LKNALQRAVE RGQLEQITGK GASGTFQLKK SGEKPLLGGS LMEYAILSAI AAMNEPKTCS
     TTALKKYVLE NHPGANSNYQ MHLLKKTLQK CEKNGWLEQI SGKGFSGTFQ LSFPYYPSPG
     VLFPKKESGG SDDEDEDDDD DESSEDSEDE EPPPKRSLQK KTPAKSQGKT ASMKQRGSKP
     ARKVPAAQRG KVRPLPKKAP PKAKTPARKA RPSPSVIKKP SGSSSRKPIA SARKEAKLPG
     KGKSAMKKSF KTKK
//
ID   RN157_MOUSE             Reviewed;         685 AA.
AC   Q3TEL6; Q80T75;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   08-MAR-2011, entry version 40.
DE   RecName: Full=RING finger protein 157;
GN   Name=Rnf157; Synonyms=Kiaa1917;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 193-685 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 340-685 (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3TEL6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3TEL6-2; Sequence=VSP_021736, VSP_021737;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE41232.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AL645861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK169566; BAE41232.1; ALT_INIT; mRNA.
DR   EMBL; AK122571; BAC65853.1; -; mRNA.
DR   IPI; IPI00756544; -.
DR   IPI; IPI00808507; -.
DR   UniGene; Mm.426344; -.
DR   ProteinModelPortal; Q3TEL6; -.
DR   SMR; Q3TEL6; 273-319.
DR   PRIDE; Q3TEL6; -.
DR   Ensembl; ENSMUST00000100202; ENSMUSP00000097776; ENSMUSG00000052949.
DR   UCSC; uc007mky.1; mouse.
DR   MGI; MGI:2442484; Rnf157.
DR   GeneTree; ENSGT00390000009925; -.
DR   HOGENOM; HBG443876; -.
DR   HOVERGEN; HBG061762; -.
DR   InParanoid; Q3TEL6; -.
DR   OrthoDB; EOG4PVNZ7; -.
DR   ArrayExpress; Q3TEL6; -.
DR   Bgee; Q3TEL6; -.
DR   CleanEx; MM_RNF157; -.
DR   Genevestigator; Q3TEL6; -.
DR   GermOnline; ENSMUSG00000052949; Mus musculus.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Metal-binding; Zinc; Zinc-finger.
FT   CHAIN         1    685       RING finger protein 157.
FT                                /FTId=PRO_0000261615.
FT   ZN_FING     276    315       RING-type.
FT   COMPBIAS    431    537       Ser-rich.
FT   VAR_SEQ     592    592       I -> V (in isoform 2).
FT                                /FTId=VSP_021736.
FT   VAR_SEQ     642    685       EWQCAEHELGGRRPSARPRSPRGGLGKEASAFRIETVALPG
FT                                TYV -> TWQHEDNTVNCRHTQRRRLSSSSLEDPEENRPCV
FT                                WDPMAV (in isoform 2).
FT                                /FTId=VSP_021737.
SQ   SEQUENCE   685 AA;  74534 MW;  22B9382ECBA0E334 CRC64;
     MGALTSRQHA GVEEVDIPSN SVYRYPPKSG SYFASHFIMG GEKFDSTHPE GYLFGENSDL
     NFLGNRPVAF PYAAPPPQEP VKTLRSLINI RKDTLRLVKC AEEVKSHGEE AGKAKVHYNV
     EFTFDTDARV AITIYYQATE EFQNGIASYI PKDNSLQSET VHYKRGVFQQ FCLPSHTVDP
     SEWAEEELGF DLDREVYPLV VHAVVDEGDE YFGHCHVLLG TFEKHPDGTF CVKPLKQKQV
     VDGVSYLLQE IYGIENKYNT QDSKVAEDDV SDNSAECVVC LSDVRDTLIL PCRHLCLCNT
     CADTLRYQAN NCPICRLPFR ALLQIRAMRK KLGPLSPSSF NPIISSQTSD SEEHSSSENI
     PPGYEVVSLL EALNGPLTSS PAVPPLHVLG DGHLSGMLPS YGSDGYLPPV RTLSPLDRLS
     DCNNQGLKLK KSLSKSISQN SSVLHEEEDE RSCSESDTQL SQRLSVQHPE EGPDVTPESE
     NLTLSSSGAV DQSSCTGTPL SSTISSPEDP ASSSLAQSVM SMASSQISTD TVSSMSGSYI
     APGTEEEGEA LPSPRAASRA PSEGEETPAE SPDSNFAGLP AGEQDAEGND IIEEEDRSPV
     REDGQRTCAF LGMECDNNND FDVASVKALD NKLCSEVCLP GEWQCAEHEL GGRRPSARPR
     SPRGGLGKEA SAFRIETVAL PGTYV
//
ID   IQEC3_MOUSE             Reviewed;        1195 AA.
AC   Q3TES0; Q3UHP8; Q80TJ8;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=IQ motif and SEC7 domain-containing protein 3;
GN   Name=Iqsec3; Synonyms=Kiaa1110;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 285-1195.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1023, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-653, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=17981261; DOI=10.1016/j.bbrc.2007.10.041;
RA   Hattori Y., Ohta S., Hamada K., Yamada-Okabe H., Kanemura Y.,
RA   Matsuzaki Y., Okano H., Kawakami Y., Toda M.;
RT   "Identification of a neuron-specific human gene, KIAA1110, that is a
RT   guanine nucleotide exchange factor for ARF1.";
RL   Biochem. Biophys. Res. Commun. 364:737-742(2007).
CC   -!- FUNCTION: Acts as a guanine nucleotide exchange factor (GEF) for
CC       ARF1 (By similarity).
CC   -!- SUBUNIT: Interacts with DLG1 and DLG4 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed specifically in the adult brain, but
CC       not in the fetal brain at 14 dpc.
CC   -!- SIMILARITY: Belongs to the BRAG family.
CC   -!- SIMILARITY: Contains 1 IQ domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 SEC7 domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK147268; BAE27809.1; -; mRNA.
DR   EMBL; AK169437; BAE41178.1; -; mRNA.
DR   EMBL; AK122446; BAC65728.1; -; mRNA.
DR   IPI; IPI00330167; -.
DR   RefSeq; NP_001028526.1; NM_001033354.2.
DR   UniGene; Mm.299442; -.
DR   ProteinModelPortal; Q3TES0; -.
DR   SMR; Q3TES0; 651-984.
DR   PhosphoSite; Q3TES0; -.
DR   PRIDE; Q3TES0; -.
DR   Ensembl; ENSMUST00000046373; ENSMUSP00000038653; ENSMUSG00000040797.
DR   GeneID; 243621; -.
DR   KEGG; mmu:243621; -.
DR   UCSC; uc009dom.1; mouse.
DR   CTD; 243621; -.
DR   MGI; MGI:2677208; Iqsec3.
DR   eggNOG; roNOG14424; -.
DR   GeneTree; ENSGT00590000083058; -.
DR   HOGENOM; HBG713627; -.
DR   HOVERGEN; HBG056324; -.
DR   InParanoid; Q3TES0; -.
DR   OMA; GHSSTLM; -.
DR   OrthoDB; EOG49S65Q; -.
DR   NextBio; 385855; -.
DR   ArrayExpress; Q3TES0; -.
DR   Bgee; Q3TES0; -.
DR   CleanEx; MM_IQSEC3; -.
DR   Genevestigator; Q3TES0; -.
DR   GermOnline; ENSMUSG00000040797; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000904; Sec7.
DR   InterPro; IPR023394; SEC7_alpha_orthog.
DR   Gene3D; G3DSA:1.10.1000.11; G3DSA:1.10.1000.11; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF01369; Sec7; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00222; Sec7; 1.
DR   SUPFAM; SSF48425; Sec7; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
DR   PROSITE; PS50190; SEC7; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Phosphoprotein.
FT   CHAIN         1   1195       IQ motif and SEC7 domain-containing
FT                                protein 3.
FT                                /FTId=PRO_0000245611.
FT   DOMAIN      312    341       IQ.
FT   DOMAIN      648    841       SEC7.
FT   DOMAIN      854    987       PH.
FT   COILED       20     56       Potential.
FT   COMPBIAS     64    140       Pro-rich.
FT   COMPBIAS    575    581       Poly-Glu.
FT   COMPBIAS    602    607       Poly-Ser.
FT   COMPBIAS   1065   1178       Pro-rich.
FT   MOD_RES     653    653       Phosphothreonine.
FT   MOD_RES    1023   1023       Phosphoserine.
FT   CONFLICT    285    298       ASEYELSLDLKNKQ -> HRAEACLLRPGFPK (in Ref.
FT                                2; BAE41178).
FT   CONFLICT    382    382       P -> S (in Ref. 2; BAE41178).
FT   CONFLICT    722    722       D -> E (in Ref. 1; BAE27809).
SQ   SEQUENCE   1195 AA;  129119 MW;  3674AA84857DD438 CRC64;
     MESLLENPVR AVLYLKELTA IVQNQQSLIH TQRQRIDELE RRLDELSAEN RSLWEHQQLL
     QAQPPPGLVP PPPSAPLPAP AVTAPAAAAA QEPLQDHGQL IPASPEPPLQ HHGQLLAQPQ
     PAPSSRVQTP QSPHQHPVAP GAIADKEKER PSSCCAAAGA LLQHASPAAL GKGVLSRRPE
     NETVLHQFCC PAADTEQKPA CSDLASQSDG SCAQAGGGME DSVVAAVAAG RPSAHAPKAQ
     APELQQEEER PGAVGSPRAG PLRAASPGRQ QPALATALCS HTPAASEYEL SLDLKNKQIE
     MLEHKYGGHL VSRRAACTIQ TAFRQYQLSK NFEKIRNSLL ESRLPRRISL RKVRAPTAES
     LVAEKALLEG CGLLGLPLGR SPSLPPTFAG SLTELEDSFT EQVQSLAKSI DDALSTWSLK
     TMCSLQESGA YQLHQALHPS AGQPGLETEA AAREPESGPG SGDEAGGLPQ GHSGTLMMAF
     RDVTVQIANQ NISVSSSTAL SVANCLGAQT AQATAEPAAA QAEQEDTADQ EVSEVPASEQ
     MDPPSEDSEA AESRAQSAQE PAVAQAVVEE AVATEAEEEE EGAKQAGKGA EAEGGDNSEQ
     LSSSSASTKS AKSSSEASAA ASKEALQAVI LSLPRYHCEN PASCRSPTLS TDTLRKRLYR
     IGLNLFNINP DKGIQFLISR GFIPDTPIGV AHFLLQRKGL SRQMIGEFLG NSKKQFNRDV
     LDCVVDEMDF SNMELDEALR KFQAHIRVQG EAQKVERLIE AFSQRYCMCN PEVVQQFHNP
     DTIFILAFAI ILLNTDMYSP NIKPDRKMML EDFIRNLRGV DDGADIPREL VVGIYERIQQ
     KELKSNEDHV TYVTKVEKSI VGMKTVLSMP HRRLVCCSRL FEVTDVNKLQ KQAAHQREVF
     LFNDLLVILK LCPKKKSSFT YTFCKAVGLL GMRFHLFENE YYSHGITLAT PLSGSEKKQV
     LHFCALGSDE MQKFVEDLKE SIAEVTELEQ IRIEWELEKQ QGTKTLSVRS AGAQGDPQSK
     QGSPTAKREA MAGEKAAESS GEVSIHNRLQ TSQHSPKLGV ERGAPAPSPP TSPPPLPPDP
     QPSPLREQPP PLPLPPPTPP GTLVQCQQIV KVIVLDKPCL ARMEPLLSQA LSCYASSSSD
     SCGSTPLRGP GSPVKVIHQP PLPPPPPPYN HPHQFCPPGS MLLRRRYSSG SRSLV
//
ID   Q3TFD0_MOUSE            Unreviewed;       501 AA.
AC   Q3TFD0;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=Serine hydroxymethyltransferase;
DE            EC=2.1.2.1;
GN   Name=Shmt2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- FUNCTION: Interconversion of serine and glycine (By similarity).
CC   -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydrofolate + glycine +
CC       H(2)O = tetrahydrofolate + L-serine.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate pathway.
CC   -!- SIMILARITY: Belongs to the SHMT family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK169192; BAE40968.1; -; mRNA.
DR   IPI; IPI00454008; -.
DR   UniGene; Mm.29890; -.
DR   ProteinModelPortal; Q3TFD0; -.
DR   SMR; Q3TFD0; 39-500.
DR   STRING; Q3TFD0; -.
DR   Ensembl; ENSMUST00000026470; ENSMUSP00000026470; ENSMUSG00000025403.
DR   UCSC; uc007hjv.1; mouse.
DR   MGI; MGI:1277989; Shmt2.
DR   eggNOG; roNOG05069; -.
DR   HOVERGEN; HBG002807; -.
DR   InParanoid; Q3TFD0; -.
DR   OrthoDB; EOG4G4GQ7; -.
DR   PhylomeDB; Q3TFD0; -.
DR   ArrayExpress; Q3TFD0; -.
DR   Bgee; Q3TFD0; -.
DR   Genevestigator; Q3TFD0; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase_major_dom.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   InterPro; IPR001085; Ser_HO-MeTrfase.
DR   InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1.
DR   PANTHER; PTHR11680; Gly_HO-Metrfase; 1.
DR   Pfam; PF00464; SHMT; 1.
DR   PIRSF; PIRSF000412; SHMT; 1.
DR   SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR   PROSITE; PS00096; SHMT; 1.
PE   1: Evidence at protein level;
KW   One-carbon metabolism; Pyridoxal phosphate; Transferase.
SQ   SEQUENCE   501 AA;  55420 MW;  28C9E2E56C42DC78 CRC64;
     MVSFSLLRTT RRCGQLVCMA ARAQHSKVAQ TQAGEAAGGW TGQESLSDSD PEMWELLQRE
     KDRQCRGLEL IASENFCSRA ALEALGSCLN NKYSEGYPGK RYYGGAEVVD EIELLCQRRA
     LEAFDLDPAQ WGVNVQPYSG SPANLAAYTA LLQPHDRIMG LDLPDGGHLT HGYMSDVKRI
     SATSIFFESM PYKLNPQTGL IDYDQLALTA RLFRPRLIIA GTSAYARLID YARMREVCDE
     VRAHLLADMA HISGLVAAKV IPSPFKYADV VTTTTHKTLR GARSGLIFYR KGVRTVDPKT
     GKEIPYTFED RINFAVFPSL QGGPHNHAIA AVAVALKQAC TPMFREYSLQ VLRNAQAMAD
     ALLKRGYSLV SGGTDTHLVL VDLRPKGLDG ARAERVLELV SITANKNTCP GDRSAITPGG
     LRLGAPALTS RQFREDDFRR VVDFIDEGVN IGLEVKRKTA KLQDFKSFLL KDPETSQRLA
     NLRQQVEQFA RGFPMPGFDE R
//
ID   EEPD1_MOUSE             Reviewed;         569 AA.
AC   Q3TGW2; Q69ZC7; Q8K3B5; Q9D7J3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=Endonuclease/exonuclease/phosphatase family domain-containing protein 1;
GN   Name=Eepd1; Synonyms=Kiaa1706;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic intestine;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-106 AND SER-173,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SIMILARITY: Contains 1 HhH domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32517.1; Type=Erroneous initiation;
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DR   EMBL; AK173239; BAD32517.1; ALT_INIT; mRNA.
DR   EMBL; AK009180; BAB26125.1; -; mRNA.
DR   EMBL; AK168564; BAE40436.1; -; mRNA.
DR   EMBL; BC025571; AAH25571.1; -; mRNA.
DR   IPI; IPI00464138; -.
DR   RefSeq; NP_080465.3; NM_026189.3.
DR   UniGene; Mm.112977; -.
DR   ProteinModelPortal; Q3TGW2; -.
DR   SMR; Q3TGW2; 36-99, 132-195.
DR   PhosphoSite; Q3TGW2; -.
DR   PRIDE; Q3TGW2; -.
DR   Ensembl; ENSMUST00000040677; ENSMUSP00000047083; ENSMUSG00000036611.
DR   GeneID; 67484; -.
DR   KEGG; mmu:67484; -.
DR   UCSC; uc009opn.1; mouse.
DR   CTD; 67484; -.
DR   MGI; MGI:1914734; Eepd1.
DR   eggNOG; roNOG04988; -.
DR   GeneTree; ENSGT00390000009677; -.
DR   HOGENOM; HBG716385; -.
DR   HOVERGEN; HBG100313; -.
DR   InParanoid; Q3TGW2; -.
DR   OMA; EKANNPG; -.
DR   OrthoDB; EOG4CZBFK; -.
DR   NextBio; 324710; -.
DR   ArrayExpress; Q3TGW2; -.
DR   Bgee; Q3TGW2; -.
DR   Genevestigator; Q3TGW2; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   InterPro; IPR004509; Competence_ComEA_HhH.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   InterPro; IPR000445; HhH_motif.
DR   InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif.
DR   InterPro; IPR010994; RuvA_2-like.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   Pfam; PF00633; HHH; 1.
DR   SMART; SM00278; HhH1; 3.
DR   SUPFAM; SSF56219; Exo_endo_phos; 1.
DR   SUPFAM; SSF47781; RuvA_2_like; 1.
DR   TIGRFAMs; TIGR00426; ComEA_HHH; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    569       Endonuclease/exonuclease/phosphatase
FT                                family domain-containing protein 1.
FT                                /FTId=PRO_0000317262.
FT   DOMAIN       38     67       HhH.
FT   MOD_RES      16     16       Phosphoserine.
FT   MOD_RES      25     25       Phosphoserine.
FT   MOD_RES     106    106       Phosphoserine.
FT   MOD_RES     173    173       Phosphoserine.
FT   CONFLICT     30     30       F -> L (in Ref. 2; BAB26125).
FT   CONFLICT    389    389       A -> T (in Ref. 3; AAH25571).
SQ   SEQUENCE   569 AA;  62953 MW;  9B4A49C082A3715F CRC64;
     MGSTLGCHRS IPRDPSDLSH NRKFSAACNF SNILVNQERL NINTATEEEL MTLPGVTRAV
     ARSIVEYREY IGGFKKVEDL ALVSGVGATK LEQVKFEICV SSKGNSAQHS PSSLRRDLLA
     EQQPHHLTTT VPLTPRVNIN TATLAQLMSV RGLSEKMALS IVDYRREHGP FRSVEDLVRM
     DGINAAFLDR IRHQVFAERS RPPSTHTNGG LTFTAKPHPS PTSLSLQSED LDLPPGGPTQ
     IISMRPSVEA FGGMRDGRPV FRLATWNLQG CSVEKANNPG VREVVCMTLL ENSIKLLAVQ
     ELLDKEALEK FCTELNQPIL PNIRKWKGSR GCWRSIVAEK PSNQLQKGPC YSGFLWDTAA
     NVELRDIPGR ESSPSNGHAK AVGPSPFLAR FKVGSNDLTL VNLQLTALAL PGAENSSKNH
     SDGHRLLNFA LTLQETLKGE KDVVILGDFG QGPDSNDYDI LRREKFHHLV PAHTFTNIST
     RNPQGSKSVD NIWISKSLKK VFTGHWAVVR EGLTNPWIPD NWSWGGVASE HCPVLAELYM
     EKDWSKKEVP RNGNGVTLEP SEANIKHER
//
ID   Q3TH04_MOUSE            Unreviewed;       518 AA.
AC   Q3TH04;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 44.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Hspa8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Stomach;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Stomach;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Stomach;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Stomach;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Stomach;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Stomach;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Stomach;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Stomach;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
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DR   EMBL; AK168511; BAE40394.1; -; mRNA.
DR   IPI; IPI00323357; -.
DR   UniGene; Mm.290774; -.
DR   UniGene; Mm.336743; -.
DR   UniGene; Mm.351377; -.
DR   UniGene; Mm.412745; -.
DR   ProteinModelPortal; Q3TH04; -.
DR   STRING; Q3TH04; -.
DR   Ensembl; ENSMUST00000015800; ENSMUSP00000015800; ENSMUSG00000015656.
DR   MGI; MGI:105384; Hspa8.
DR   HOVERGEN; HBG051845; -.
DR   InParanoid; Q3TH04; -.
DR   Bgee; Q3TH04; -.
DR   Genevestigator; Q3TH04; -.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0042623; F:ATPase activity, coupled; IDA:MGI.
DR   GO; GO:0051082; F:unfolded protein binding; IPI:MGI.
DR   GO; GO:0051085; P:chaperone mediated protein folding requiring cofactor; IGI:MGI.
DR   GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR001023; Hsp70.
DR   InterPro; IPR013126; Hsp_70.
DR   PANTHER; PTHR19375; Hsp70; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding.
FT   NON_TER       1      1
SQ   SEQUENCE   518 AA;  56697 MW;  3D701B99AE64952D CRC64;
     EVAEAYLGKT VTNAVVTVPA YFNDSQRQAT KDAGTIAGLN VLRIINEPTA AAIAYGLDKK
     VGAERNVLIF DLGGGTFDVS ILTIEDGIFE VKSTAGDTHL GGEDFDNRMV NHFIAEFKRK
     HKKDISENKR AVRRLRTACE RAKRTLSSST QASIEIDSLY EGIDFYTSIT RARFEELNAD
     LFRGTLDPVE KALRDAKLDK SQIHDIVLVG GSTRIPKIQK LLQDFFNGKE LNKSINPDEA
     VAYGAAVQAA ILSGDKSENV QDLLLLDVTP LSLGIETAGG VMTVLIKRNT TIPTKQTQTF
     TTYSDNQPGV LIQVYEGERA MTKDNNLLGK FELTGIPPAP RGVPQIEVTF DIDANGILNV
     SAVDKSTGKE NKITITNDKG RLSKEDIERM VQEAEKYKAE DEKQRDKVSS KNSLESYAFN
     MKATVEDEKL QGKINDEDKQ KILDKCNEII SWLDKNQTAE KEEFEHQQKE LEKVCNPIIT
     KLYQSAGGMP GGMPGGFPGG GAPPSGGASS GPTIEEVD
//
ID   TTYH2_MOUSE             Reviewed;         532 AA.
AC   Q3TH73; Q3U103; Q3U8L3; Q6P9J3; Q920A8;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Protein tweety homolog 2;
DE            Short=mTTY2;
GN   Name=Ttyh2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=21481902; PubMed=11597145; DOI=10.1006/geno.2001.6629;
RA   Rae F.K., Hooper J.D., Eyre H.J., Sutherland G.R., Nicol D.L.,
RA   Clements J.A.;
RT   "TTYH2, a human homologue of the Drosophila melanogaster gene tweety,
RT   is located on 17q24 and upregulated in renal cell carcinoma.";
RL   Genomics 77:200-207(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Heart, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Probable large-conductance Ca(2+)-activated chloride
CC       channel. May play a role in Ca(2+) signal transduction. May be
CC       involved in cell proliferation and cell aggregation (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3TH73-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3TH73-2; Sequence=VSP_029768;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the tweety family.
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DR   EMBL; AF329682; AAL16785.1; -; mRNA.
DR   EMBL; AK152172; BAE31004.1; -; mRNA.
DR   EMBL; AK155166; BAE33089.1; -; mRNA.
DR   EMBL; AK156393; BAE33698.1; -; mRNA.
DR   EMBL; AK168408; BAE40325.1; -; mRNA.
DR   EMBL; AL663079; CAM19258.1; -; Genomic_DNA.
DR   EMBL; AL645484; CAM19258.1; JOINED; Genomic_DNA.
DR   EMBL; AL645484; CAM22870.1; -; Genomic_DNA.
DR   EMBL; AL663079; CAM22870.1; JOINED; Genomic_DNA.
DR   EMBL; BC060740; AAH60740.1; -; mRNA.
DR   IPI; IPI00420454; -.
DR   IPI; IPI00652708; -.
DR   RefSeq; NP_444503.2; NM_053273.2.
DR   RefSeq; XP_003085808.1; XM_003085760.1.
DR   RefSeq; XP_003085809.1; XM_003085761.1.
DR   UniGene; Mm.271934; -.
DR   UniGene; Mm.475167; -.
DR   PhosphoSite; Q3TH73; -.
DR   PRIDE; Q3TH73; -.
DR   Ensembl; ENSMUST00000045779; ENSMUSP00000037821; ENSMUSG00000034714.
DR   Ensembl; ENSMUST00000100242; ENSMUSP00000097813; ENSMUSG00000034714.
DR   GeneID; 100505117; -.
DR   GeneID; 117160; -.
DR   KEGG; mmu:100505117; -.
DR   KEGG; mmu:117160; -.
DR   NMPDR; fig|10090.3.peg.25574; -.
DR   UCSC; uc007mfm.1; mouse.
DR   CTD; 117160; -.
DR   MGI; MGI:2157091; Ttyh2.
DR   eggNOG; roNOG12538; -.
DR   GeneTree; ENSGT00390000010182; -.
DR   HOGENOM; HBG446200; -.
DR   HOVERGEN; HBG108621; -.
DR   InParanoid; Q3TH73; -.
DR   OMA; APWWVVW; -.
DR   OrthoDB; EOG49ZXP9; -.
DR   PhylomeDB; Q3TH73; -.
DR   NextBio; 369540; -.
DR   ArrayExpress; Q3TH73; -.
DR   Bgee; Q3TH73; -.
DR   CleanEx; MM_TTYH2; -.
DR   Genevestigator; Q3TH73; -.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   InterPro; IPR006990; Tweety.
DR   PANTHER; PTHR12424; Tweety; 1.
DR   Pfam; PF04906; Tweety; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Calcium; Cell membrane; Chloride;
KW   Chloride channel; Glycoprotein; Ion transport; Ionic channel;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    532       Protein tweety homolog 2.
FT                                /FTId=PRO_0000312247.
FT   TOPO_DOM      1     44       Extracellular (Potential).
FT   TRANSMEM     45     65       Helical; Name=1; (Potential).
FT   TOPO_DOM     66     87       Cytoplasmic (Potential).
FT   TRANSMEM     88    108       Helical; Name=2; (Potential).
FT   TOPO_DOM    109    213       Extracellular (Potential).
FT   TRANSMEM    214    234       Helical; Name=3; (Potential).
FT   TOPO_DOM    235    240       Cytoplasmic (Potential).
FT   TRANSMEM    241    261       Helical; Name=4; (Potential).
FT   TOPO_DOM    262    385       Extracellular (Potential).
FT   TRANSMEM    386    406       Helical; Name=5; (Potential).
FT   TOPO_DOM    407    532       Cytoplasmic (Potential).
FT   COMPBIAS    421    431       Poly-Asp.
FT   MOD_RES     199    199       Phosphothreonine (By similarity).
FT   CARBOHYD    283    283       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     421    482       Missing (in isoform 2).
FT                                /FTId=VSP_029768.
FT   CONFLICT     29     31       RVD -> DEY (in Ref. 1; AAL16785).
FT   CONFLICT    107    107       G -> V (in Ref. 2; BAE31004).
FT   CONFLICT    119    119       H -> R (in Ref. 2; BAE33698).
FT   CONFLICT    178    178       A -> E (in Ref. 4; AAH60740).
FT   CONFLICT    259    259       S -> F (in Ref. 4; AAH60740).
FT   CONFLICT    343    343       D -> R (in Ref. 1; AAL16785).
FT   CONFLICT    358    363       LHQLTA -> CTVDR (in Ref. 1; AAL16785).
SQ   SEQUENCE   532 AA;  59008 MW;  FC5B882F5FB7573A CRC64;
     MPAARVEYIA PWWVVWLHSV PHLGLRLQRV DSTFSPGDET YQESLLFLGV LAAIGLGLNL
     IFLTVYLVCT CCCRRDHTVQ TKQQESCCVT WTAVVAGLLC CAAVGVGFYG NSETNDGMHQ
     LIYSLDNANH TFSGMDELVS ANTQRMKVDL EQHLARLSEI IAARGDYIQT LKFMQQMAGN
     VVSQLSGLPV WREVTTQLTK LSHQTAYVEY YRWLSYLLLF ILDLVICLVT CLGLARRSKC
     LLASMLCCGI LTLILSWASL AADAAAAVGT SDFCMAPDIY ILNNTGSQIN SEVTRYYLHC
     SQSLISPFQQ SLTTFQRSLT TMQIQVGGLL QFAVPLFPTA EKDLLGIQLL LNNSEISLHQ
     LTAMLDCRGL HKDYLDALTG ICYDGIEGLL FLGLFSLLAA LAFSTLTCAG PRAWKYFINR
     DRDYDDIDDD DPFNPQARRI AAHNPTRGQL HSFCSYSSGL GSQCSLQPPS QTISNAPVSE
     YMNQAILFGG NPRYENVPLI GRGSPPPTYS PSMRPTYMSV ADEHLRHYEF PS
//
ID   AASD1_MOUSE             Reviewed;         412 AA.
AC   Q3THG9; Q3UWH8; Q8BVJ6; Q99JS9;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   08-FEB-2011, entry version 53.
DE   RecName: Full=Alanyl-tRNA editing protein Aarsd1;
DE   AltName: Full=Alanyl-tRNA deacylase alaX;
DE            Short=AlaX;
DE            Short=AlaXp-II;
DE   AltName: Full=Alanyl-tRNA synthetase domain-containing protein 1;
GN   Name=Aarsd1; Synonyms=Alax;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, and C57BL/6J;
RC   TISSUE=Embryonic head, and Embryonic testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   FUNCTION AS TRNA(ALA) EDITING PROTEIN.
RX   PubMed=18172502; DOI=10.1038/nature06454;
RA   Beebe K., Mock M., Merriman E., Schimmel P.;
RT   "Distinct domains of tRNA synthetase recognize the same base pair.";
RL   Nature 451:90-93(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Functions in trans to edit the amino acid moiety from
CC       incorrectly charged Ser-tRNA(Ala).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (Potential).
CC   -!- INTERACTION:
CC       Q62406-1:Irak1; NbExp=2; IntAct=EBI-646572, EBI-488313;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. Alax-L subfamily.
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DR   EMBL; AK078016; BAC37098.1; -; mRNA.
DR   EMBL; AK136332; BAE22937.1; -; mRNA.
DR   EMBL; AK168281; BAE40227.1; -; mRNA.
DR   EMBL; BC005711; AAH05711.1; -; mRNA.
DR   IPI; IPI00648549; -.
DR   RefSeq; NP_659078.1; NM_144829.1.
DR   UniGene; Mm.146283; -.
DR   ProteinModelPortal; Q3THG9; -.
DR   SMR; Q3THG9; 1-247.
DR   IntAct; Q3THG9; 4.
DR   STRING; Q3THG9; -.
DR   PhosphoSite; Q3THG9; -.
DR   PRIDE; Q3THG9; -.
DR   Ensembl; ENSMUST00000070395; ENSMUSP00000067912; ENSMUSG00000075528.
DR   GeneID; 69684; -.
DR   KEGG; mmu:69684; -.
DR   NMPDR; fig|10090.3.peg.25343; -.
DR   CTD; 69684; -.
DR   MGI; MGI:1916934; Aarsd1.
DR   GeneTree; ENSGT00510000046493; -.
DR   HOVERGEN; HBG080017; -.
DR   PhylomeDB; Q3THG9; -.
DR   NextBio; 330082; -.
DR   ArrayExpress; Q3THG9; -.
DR   Bgee; Q3THG9; -.
DR   CleanEx; MM_AARSD1; -.
DR   Genevestigator; Q3THG9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:InterPro.
DR   InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR   InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR   InterPro; IPR012947; tRNA_SAD.
DR   Pfam; PF01411; tRNA-synt_2c; 1.
DR   Pfam; PF07973; tRNA_SAD; 1.
DR   SMART; SM00863; tRNA_SAD; 1.
DR   SUPFAM; SSF55186; Thr/Ala-tRNA-synth_IIc_edit; 1.
DR   PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Metal-binding; Phosphoprotein; Protein biosynthesis; Zinc.
FT   CHAIN         1    412       Alanyl-tRNA editing protein Aarsd1.
FT                                /FTId=PRO_0000277466.
FT   METAL       109    109       Zinc (Potential).
FT   METAL       113    113       Zinc (Potential).
FT   METAL       209    209       Zinc (Potential).
FT   METAL       213    213       Zinc (Potential).
FT   MOD_RES     409    409       Phosphoserine.
FT   CONFLICT     80     80       D -> G (in Ref. 1; BAE22937).
FT   CONFLICT    175    175       L -> M (in Ref. 1; BAE40227).
FT   CONFLICT    292    292       L -> H (in Ref. 1; BAE22937).
SQ   SEQUENCE   412 AA;  44971 MW;  3FFD32304A379B44 CRC64;
     MAFLCQRDSY AREFTTTVVS CSPAELQTDA SGGKKEVLSG FHVVLEDTLL FPEGGGQPDD
     RGTINDISVL RVTRRGAQAD HFTESPLSPG SQVQVRVDWE RRFDHMQQHS GQHLITAVAD
     LLFGLKTTSW ELGRLRSVIE LDSPSVTAEQ VAAIEQSVNQ KIRDRLPVSV RELSLDDPEV
     EQVRGRGLPD DHAGPIRVVT IEGVDSNMCC GTHVSNLSDL QVIKILGTEK GKKNKSNLIF
     LAGNRVLKWM ERSHGSEKAL TSLLKCGVED HVEAVKKLQN ATKLLQKNNL NLLRDLAVHT
     AHSLRSSPAW GGVVTLHRKE GDSEFMNIIA NEIGSEETLL FLTVGDEKGA GLFLLAGPAE
     AVETLGPRVA EVLEGKGAGK KGRFQGKATK MSRRAEAQAL LQDYVSTQSA EE
//
ID   GUAA_MOUSE              Reviewed;         693 AA.
AC   Q3THK7; Q3TFR6; Q3TIH1; Q3UJ21; Q3V343; Q66JZ6;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=GMP synthase [glutamine-hydrolyzing];
DE            EC=6.3.5.2;
DE   AltName: Full=GMP synthetase;
DE   AltName: Full=Glutamine amidotransferase;
GN   Name=Gmps;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, C57BL/6J, DBA/2, and NOD;
RC   TISSUE=Eye, Heart, Kidney, Spinal cord, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 217-693.
RC   TISSUE=Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 536-548 AND 570-589, AND MASS SPECTROMETRY.
RC   TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Involved in the de novo synthesis of guanine nucleotides
CC       which are not only essential for DNA and RNA synthesis, but also
CC       provide GTP, which is involved in a number of cellular processes
CC       important for cell division (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + xanthosine 5'-phosphate + L-glutamine +
CC       H(2)O = AMP + diphosphate + GMP + L-glutamate.
CC   -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln
CC       route): step 1/1.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
CC   -!- SIMILARITY: Contains 1 GMP-binding domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE20667.1; Type=Frameshift; Positions=35;
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DR   EMBL; AK049755; BAE20667.1; ALT_FRAME; mRNA.
DR   EMBL; AK143197; BAE25299.1; -; mRNA.
DR   EMBL; AK146654; BAE27334.1; -; mRNA.
DR   EMBL; AK167857; BAE39875.1; -; mRNA.
DR   EMBL; AK168239; BAE40189.1; -; mRNA.
DR   EMBL; AK169043; BAE40832.1; -; mRNA.
DR   EMBL; AK169701; BAE41314.1; -; mRNA.
DR   EMBL; BC080685; AAH80685.1; -; mRNA.
DR   IPI; IPI00351252; -.
DR   RefSeq; NP_001028472.2; NM_001033300.2.
DR   UniGene; Mm.331051; -.
DR   UniGene; Mm.394565; -.
DR   UniGene; Mm.480477; -.
DR   ProteinModelPortal; Q3THK7; -.
DR   SMR; Q3THK7; 23-693.
DR   STRING; Q3THK7; -.
DR   PhosphoSite; Q3THK7; -.
DR   REPRODUCTION-2DPAGE; IPI00351252; -.
DR   PRIDE; Q3THK7; -.
DR   Ensembl; ENSMUST00000029405; ENSMUSP00000029405; ENSMUSG00000027823.
DR   GeneID; 229363; -.
DR   KEGG; mmu:229363; -.
DR   CTD; 229363; -.
DR   MGI; MGI:2448526; Gmps.
DR   eggNOG; roNOG15065; -.
DR   GeneTree; ENSGT00390000006591; -.
DR   HOGENOM; HBG391775; -.
DR   HOVERGEN; HBG005929; -.
DR   InParanoid; Q3THK7; -.
DR   OMA; VVNAAHS; -.
DR   OrthoDB; EOG4J6RQ9; -.
DR   BRENDA; 6.3.5.2; 244.
DR   NextBio; 379420; -.
DR   ArrayExpress; Q3THK7; -.
DR   Bgee; Q3THK7; -.
DR   CleanEx; MM_GMPS; -.
DR   Genevestigator; Q3THK7; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:EC.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006220; Anth_synthII.
DR   InterPro; IPR011702; GATASE.
DR   InterPro; IPR017926; GATASE_1.
DR   InterPro; IPR000991; GATase_class1_C.
DR   InterPro; IPR001674; GMP_synth_C.
DR   InterPro; IPR004739; GMP_synth_N.
DR   InterPro; IPR022310; NAD/GMP_synthase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Pfam; PF00117; GATase; 1.
DR   Pfam; PF00958; GMP_synt_C; 1.
DR   Pfam; PF02540; NAD_synthase; 1.
DR   PRINTS; PR00097; ANTSNTHASEII.
DR   PRINTS; PR00096; GATASE.
DR   TIGRFAMs; TIGR00888; guaA_Nterm; 1.
DR   PROSITE; PS51273; GATASE_TYPE_1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing;
KW   Glutamine amidotransferase; GMP biosynthesis; Ligase;
KW   Nucleotide-binding; Phosphoprotein; Purine biosynthesis.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    693       GMP synthase [glutamine-hydrolyzing].
FT                                /FTId=PRO_0000284365.
FT   DOMAIN       27    216       Glutamine amidotransferase type-1.
FT   NP_BIND     244    250       ATP (By similarity).
FT   ACT_SITE    104    104       For GATase activity (By similarity).
FT   ACT_SITE    190    190       For GATase activity (By similarity).
FT   ACT_SITE    192    192       For GATase activity (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       9      9       N6-acetyllysine (By similarity).
FT   MOD_RES     318    318       Phosphothreonine (By similarity).
FT   MOD_RES     332    332       Phosphoserine.
FT   MOD_RES     416    416       N6-acetyllysine (By similarity).
FT   CONFLICT    201    201       V -> I (in Ref. 1; BAE39875).
FT   CONFLICT    205    205       N -> Y (in Ref. 1; BAE39875).
FT   CONFLICT    265    265       V -> D (in Ref. 1; BAE39875).
FT   CONFLICT    356    356       S -> G (in Ref. 1; BAE40189).
FT   CONFLICT    359    359       P -> H (in Ref. 1; BAE40189).
FT   CONFLICT    359    359       P -> R (in Ref. 1; BAE39875).
FT   CONFLICT    363    363       Missing (in Ref. 1; BAE39875).
FT   CONFLICT    511    512       LL -> CC (in Ref. 1; BAE27334).
FT   CONFLICT    586    586       S -> G (in Ref. 1; BAE39875).
SQ   SEQUENCE   693 AA;  76723 MW;  854DBAD6A9C75A12 CRC64;
     MALCNGDSKP ENAGGDLKDG SHHYEGAVVI LDAGAQYGKV IDRRVRELFV QSEIFPLETP
     AFAIKEQGFR AIIISGGPNS VYAEDAPWFD PAIFTIGKPI LGICYGMQMM NKVFGGTVHK
     KSVREDGVFN ISMDNTCSLF RGLQKEEIVL LTHGDSVDKV ADGFKVVARS GNIVAGIANE
     SKKLYGVQFH PEVGLTENGK VILKNFLYDI AGCSGNFTVQ NRELECIREI KEKVGTSKVL
     VLLSGGVDST VCTALLNRAL NQDQVIAVHI DNGFMRKRES QSVEEALKKL GIQVKVINAA
     HSFYNGTTTL PISDEDRTPR KRISKTLNMT TSPEEKRKII GDTFVKIANE VIGEMSLKPE
     EVFLAQGTLR PDLIESASLV ASGKAELIKT HHNDTELIRK LREEGKVIEP LKDFHKDEVR
     ILGRELDLPE ELVSRHPFPG PGLAIRVICA EEPYICKDFP ETNNILKIVA DFSASVKKPH
     TLLQRVKACT TEEDQEKLMQ ITSLHSLNAF LLPIKTVGVQ GDCRSYSYVC GISSKDEPDW
     ESLIFLARLI PRMCHNINRV VYIFGPPVKE PPTDVTPTFL TTGVLSTLRQ ADFEAHNILR
     ESGFAGKISQ MPVILTPLHF DRDPLQKQPS CQRSVVIRTF ITSDFMTGVP ATPGNEIPVE
     VVLKMVTEIK KIPGISRIMY DLTSKPPGTT EWE
//
ID   Q3TI63_MOUSE            Unreviewed;       522 AA.
AC   Q3TI63;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 36.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Snx1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DBA/2;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DBA/2;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DBA/2;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DBA/2;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DBA/2;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DBA/2;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DBA/2;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DBA/2;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK167993; BAE39983.1; -; mRNA.
DR   IPI; IPI00876001; -.
DR   UniGene; Mm.271891; -.
DR   ProteinModelPortal; Q3TI63; -.
DR   SMR; Q3TI63; 142-269.
DR   STRING; Q3TI63; -.
DR   Ensembl; ENSMUST00000034946; ENSMUSP00000034946; ENSMUSG00000032382.
DR   MGI; MGI:1928395; Snx1.
DR   eggNOG; roNOG10131; -.
DR   HOVERGEN; HBG000618; -.
DR   InParanoid; Q3TI63; -.
DR   ArrayExpress; Q3TI63; -.
DR   Bgee; Q3TI63; -.
DR   Genevestigator; Q3TI63; -.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   InterPro; IPR001683; Phox.
DR   InterPro; IPR005329; Sorting_nexin_N.
DR   InterPro; IPR015404; Vps5_C.
DR   Gene3D; G3DSA:3.30.1520.10; PX; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF03700; Sorting_nexin; 1.
DR   Pfam; PF09325; Vps5; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; PX; 1.
DR   PROSITE; PS50195; PX; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   522 AA;  58999 MW;  DC91BEC1B7818CA2 CRC64;
     MASGGGGCSA SERLTPPFPG MDPESEGAAG GSEPEAGDSD TEGEDIFTGA AAATKPQSPK
     KTTSLFPIKN GSKENGIHED QDQEPQDLFA DATVELSLDS TQNNQKTMPG KTLTSHSPQE
     ATNSPKPQPS YEELEEEEQE DQFDLTVGIT DPEKIGDGMN AYVAYKVTTQ TSLPMFRSRQ
     LAVKRRFSDF LGLYEKLSEK HSQNGFIVPP QPEKSLIGMT KVKVGKEDSS SAEFLEKRRA
     ALERYLQRIV NHPTMLQDPD VREFLEKEEL PRAVGTQALS GAGLLKMFNK ATDAVSKMTI
     KMNESDIWFE EKLQEVECEE QRLRKLHAVV ETLVNHRKEL ALNTALFAKS LAMLGSSEDN
     TALSRALSQL AEVEEKIEQL HQEQANNDFF LLAELLSDYI RLLAIVRAAF DQRMKTWQRW
     QDAQATLQKK RESEARLLWA NKPDKLQQAK DEITEWESRV TQYERDFERI STVVRKEVTR
     FEKEKSKDFK NHVMKYLETL LHSQQQLAKY WEAFLPEAKA IS
//
ID   Q3TIJ9_MOUSE            Unreviewed;       375 AA.
AC   Q3TIJ9;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Actb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells (By similarity).
CC   -!- SIMILARITY: Belongs to the actin family.
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CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK167825; BAE39847.1; -; mRNA.
DR   IPI; IPI00110850; -.
DR   UniGene; Mm.328431; -.
DR   UniGene; Mm.391967; -.
DR   ProteinModelPortal; Q3TIJ9; -.
DR   SMR; Q3TIJ9; 2-375.
DR   STRING; Q3TIJ9; -.
DR   Ensembl; ENSMUST00000031564; ENSMUSP00000031564; ENSMUSG00000029580.
DR   HOVERGEN; HBG003771; -.
DR   InParanoid; Q3TIJ9; -.
DR   ArrayExpress; Q3TIJ9; -.
DR   Bgee; Q3TIJ9; -.
DR   Genevestigator; Q3TIJ9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004000; Actin-like.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding.
SQ   SEQUENCE   375 AA;  41667 MW;  7B0E20170B1D8B85 CRC64;
     MDDDIAALVV DNGSGMCKAG FAGGDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
     KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT
     QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL
     AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LGFEQEMATA ASSSSLEKSY
     ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS
     CGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
     EYDESGPSIV HRKCF
//
ID   RIC8A_MOUSE             Reviewed;         530 AA.
AC   Q3TIR3; Q3TEY3; Q99JW0; Q9ERR6;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Synembryn-A;
DE   AltName: Full=Protein Ric-8A;
GN   Name=Ric8a; Synonyms=Ric8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20439482; PubMed=10985349; DOI=10.1016/S0896-6273(00)00037-4;
RA   Miller K.G., Emerson M.D., McManus J.R., Rand J.B.;
RT   "RIC-8 (Synembryn): a novel conserved protein that is required for Gq
RT   alpha signaling in the C. elegans nervous system.";
RL   Neuron 27:289-299(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, DBA/2, and NOD; TISSUE=Aorta, Testis, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=12971991; DOI=10.1016/S1567-133X(03)00119-4;
RA   Tonissoo T., Meier R., Talts K., Plaas M., Karis A.;
RT   "Expression of ric-8 (synembryn) gene in the nervous system of
RT   developing and adult mouse.";
RL   Gene Expr. Patterns 3:591-594(2003).
RN   [5]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=16221497; DOI=10.1016/j.bbr.2005.08.025;
RA   Tonissoo T., Koks S., Meier R., Raud S., Plaas M., Vasar E., Karis A.;
RT   "Heterozygous mice with Ric-8 mutation exhibit impaired spatial memory
RT   and decreased anxiety.";
RL   Behav. Brain Res. 167:42-48(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-199, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Guanine nucleotide exchange factor (GEF), which can
CC       activate some, but not all, G-alpha proteins. Able to activate
CC       GNAI1, GNAO1 and GNAQ, but not GNAS by exchanging bound GDP for
CC       free GTP. Involved in regulation of microtubule pulling forces
CC       during mitotic movement of chromosomes by stimulating G(i)-alpha
CC       protein, possibly leading to release G(i)-alpha-GTP and NuMA
CC       proteins from the NuMA-GPSM2-G(i)-alpha-GDP complex. Also acts as
CC       an activator for G(q)-alpha (GNAQ) protein by enhancing the G(q)-
CC       coupled receptor-mediated ERK activation (By similarity).
CC   -!- SUBUNIT: Interacts with GDP-bound G alpha proteins GNAI1, GNAO1
CC       and GNAQ, and with GNA13 with lower affinity. Does not interact
CC       with G-alpha proteins when they are in complex with subunits beta
CC       and gamma (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: In adult brain, it is expressed in the
CC       neocortex, hippocampus and cerebellum as well as in the pineal
CC       gland and ependymal layer.
CC   -!- DEVELOPMENTAL STAGE: During the early development (E9.5-E12.0) it
CC       is expressed in the developing nervous system such as the cranial
CC       ganglia, neural tube, sympathetic chain and dorsal root ganglia.
CC       Also found in the lens, vomeronasal organ and endolymphatic sac.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Death during early embryonic development.
CC       Heterozygous mice exhibit impaired spatial memory and decreased
CC       anxiety.
CC   -!- SIMILARITY: Belongs to the synembryn family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF288813; AAG10200.1; -; mRNA.
DR   EMBL; AK031466; BAC27418.1; -; mRNA.
DR   EMBL; AK080192; BAC37844.1; -; mRNA.
DR   EMBL; AK155282; BAE33163.1; -; mRNA.
DR   EMBL; AK167746; BAE39783.1; -; mRNA.
DR   EMBL; AK169367; BAE41115.1; -; mRNA.
DR   EMBL; BC022917; AAH22917.1; -; mRNA.
DR   IPI; IPI00112639; -.
DR   RefSeq; NP_444424.1; NM_053194.4.
DR   UniGene; Mm.281916; -.
DR   ProteinModelPortal; Q3TIR3; -.
DR   STRING; Q3TIR3; -.
DR   PhosphoSite; Q3TIR3; -.
DR   PRIDE; Q3TIR3; -.
DR   Ensembl; ENSMUST00000026558; ENSMUSP00000026558; ENSMUSG00000025485.
DR   GeneID; 101489; -.
DR   KEGG; mmu:101489; -.
DR   NMPDR; fig|10090.3.peg.17903; -.
DR   UCSC; uc009kij.1; mouse.
DR   CTD; 101489; -.
DR   MGI; MGI:2141866; Ric8.
DR   eggNOG; roNOG05466; -.
DR   GeneTree; ENSGT00390000014700; -.
DR   HOGENOM; HBG443938; -.
DR   HOVERGEN; HBG054867; -.
DR   InParanoid; Q3TIR3; -.
DR   OMA; HRPARKF; -.
DR   OrthoDB; EOG40CHGV; -.
DR   PhylomeDB; Q3TIR3; -.
DR   NextBio; 354958; -.
DR   ArrayExpress; Q3TIR3; -.
DR   Bgee; Q3TIR3; -.
DR   Genevestigator; Q3TIR3; -.
DR   GermOnline; ENSMUSG00000025485; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR019318; Gua_nucleotide_exch_fac_Ric8.
DR   InterPro; IPR008376; Synembryn.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF10165; Ric8; 1.
DR   PRINTS; PR01802; SYNEMBRYN.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Guanine-nucleotide releasing factor; Phosphoprotein.
FT   CHAIN         1    530       Synembryn-A.
FT                                /FTId=PRO_0000235892.
FT   MOD_RES      30     30       Phosphoserine (By similarity).
FT   MOD_RES     199    199       Phosphothreonine.
FT   MOD_RES     434    434       Phosphotyrosine (By similarity).
FT   MOD_RES     435    435       Phosphoserine.
FT   MOD_RES     440    440       Phosphothreonine (By similarity).
FT   MOD_RES     501    501       Phosphoserine (By similarity).
FT   MOD_RES     522    522       Phosphoserine (By similarity).
FT   MOD_RES     523    523       Phosphoserine (By similarity).
FT   MOD_RES     527    527       Phosphoserine (By similarity).
FT   CONFLICT     87     87       Q -> R (in Ref. 2; BAE41115).
FT   CONFLICT    274    274       T -> A (in Ref. 2; BAE39783).
FT   CONFLICT    449    449       K -> E (in Ref. 2; BAE39783).
SQ   SEQUENCE   530 AA;  59847 MW;  D23AFC0442CCC815 CRC64;
     MEPRAVADAL ETGEEDAVTE ALRSFNREHS QSFTFDDAQQ EDRKRLAKLL VSVLEQGLSP
     KHRVTWLQTI RILSRDRSCL DSFASRQSLH ALACYADITV SEEPIPQSPD MDVLLESLKC
     LCNLVLSSPT AQMLAAEARL VVRLAERVGL YRKRSYPHEV QFFDLRLLFL LTALRTDVRQ
     QLFQELHGVR LLTDALELTL GVAPKENPPV MLPAQETERA MEILKVLFNI TFDSVKREVD
     EEDAALYRYL GTLLRHCVMV EAAGDRTEEF HGHTVNLLGN LPLKCLDVLL ALELHEGSLE
     FMGVNMDVIS ALLAFLEKRL HQTHRLKECV APVLNVLTEC ARMHRPARKF LKAQVLPPLR
     DVRTRPEVGD LLRNKLVRLM THLDTDVKRV AAEFLFVLCS ESVPRFIKYT GYGNAAGLLA
     ARGLMAGGRP EGQYSEDEDT DTEEYREAKA SINPVTGRVE EKPPNPMEGM TEEQKEHEAM
     KLVNMFDKLS RHRVIQPMGM SPRGHLTSLQ DAMCETMEGQ LSSDPDSDPD
//
ID   Q3TJE3_MOUSE            Unreviewed;       918 AA.
AC   Q3TJE3;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 39.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Hk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the hexokinase family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK167468; BAE39552.1; -; mRNA.
DR   IPI; IPI00468553; -.
DR   UniGene; Mm.196605; -.
DR   ProteinModelPortal; Q3TJE3; -.
DR   SMR; Q3TJE3; 1-911.
DR   STRING; Q3TJE3; -.
DR   Ensembl; ENSMUST00000099691; ENSMUSP00000097282; ENSMUSG00000037012.
DR   MGI; MGI:96103; Hk1.
DR   HOVERGEN; HBG005020; -.
DR   ArrayExpress; Q3TJE3; -.
DR   Bgee; Q3TJE3; -.
DR   Genevestigator; Q3TJE3; -.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004396; F:hexokinase activity; IDA:MGI.
DR   GO; GO:0006096; P:glycolysis; TAS:MGI.
DR   InterPro; IPR001312; Hexokinase.
DR   InterPro; IPR022673; Hexokinase_C.
DR   InterPro; IPR019807; Hexokinase_CS.
DR   InterPro; IPR022672; Hexokinase_N.
DR   PANTHER; PTHR19443; Hexokinase; 1.
DR   Pfam; PF00349; Hexokinase_1; 2.
DR   Pfam; PF03727; Hexokinase_2; 2.
DR   PRINTS; PR00475; HEXOKINASE.
DR   PROSITE; PS00378; HEXOKINASES; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Glycolysis; Kinase; Nucleotide-binding; Transferase.
SQ   SEQUENCE   918 AA;  102279 MW;  1B9C214B54849F10 CRC64;
     MIAAQLLAYY FTELKDDQVK KIDKYLYAMR LSDEILIDIL TRFKKEMKNG LSRDYNPTAS
     VKMLPTFVRS IPDGSEKGDF IALDLGGSSF RILRVQVNHE KSQNVSMESE VYDTPENIVH
     GSGSQLFDHV AECLGDFMEK RKIKDKKLPV GFTFSFPCRQ SKIDEAVLIT WTKRFKASGV
     EGADVVKLLN KAIKKRGDYD ANIVAVVNDT VGTMMTCGYD DQQCEVGLII GTGTNACYME
     ELRHIDLVEG DEGRMCINTE WGAFGDDGSL EDIRTEFDRE LDRGSLNPGK QLFEKMVSGM
     YMGELVRLIL VKMAKESLLF EGRITPELLT RGKFTTSDVA AIETDKEGVQ NAKEILTRLG
     VEPSHDDCVS VQHVCTIVSF RSANLVAATL GAILNRLRDN KGTPRLRTTV GVDGSLYKMH
     PQYSRRFNKT LRRLVPDSDV RFLLSESGSG KGAAMVTAVA YRLAEQHRQI EETLSHFRLS
     KQALMEVKKK LRSEMEMGLR KETNSRATVK MLPSYVRSIP DGTEHGDFLA LDLGGTNFRV
     LLVKIRSGKK RTVEMHNKIY SIPLEIMQGT GDELFDHIVS CISDFLDYMG IKGPRMPLGF
     TFSFPCKQTS LDCGILITWT KGFKATDCVG HDVATLLRDA VKRREEFDLD VVAVVNDTVG
     TMMTCAYEEP SCEIGLIVGT GSNACYMEEM KNVEMVEGNQ GQMCINMEWG AFGDNGCLDD
     IRTDFDKVVD EYSLNSGKQR FEKMISGMYL GEIVRNILID FTKKGFLFRG QISEPLKTRG
     IFETKFLSQI ESDRLALLQV RAILQQLGLN STCDDSILVK TVCGVVSKRA AQLCGAGMAA
     VVEKIRENRG LDHLNVTVGV DGTLYKLHPH FSRIMHQTVK ELSPKCTVSF LLSEDGSGKG
     AALITAVGVR LRGDPTNA
//
ID   SMCA4_MOUSE             Reviewed;        1613 AA.
AC   Q3TKT4; Q3TUD7; Q6AXG8;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Transcription activator BRG1;
DE            EC=3.6.4.-;
DE   AltName: Full=ATP-dependent helicase SMARCA4;
DE   AltName: Full=BRG1-associated factor 190A;
DE            Short=BAF190A;
DE   AltName: Full=Protein brahma homolog 1;
DE   AltName: Full=SNF2-beta;
DE   AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4;
GN   Name=Smarca4; Synonyms=Baf190a, Brg1, Snf2b, Snf2l4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   FUNCTION, FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION BY
RP   MASS SPECTROMETRY, IDENTIFICATION IN THE NBAF AND NPBAF COMPLEXES, AND
RP   INTERACTION WITH PHF10.
RX   PubMed=17640523; DOI=10.1016/j.neuron.2007.06.019;
RA   Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T.,
RA   Wu H., Aebersold R., Graef I.A., Crabtree G.R.;
RT   "An essential switch in subunit composition of a chromatin remodeling
RT   complex during neural development.";
RL   Neuron 55:201-215(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610 AND SER-613, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1419, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Transcriptional coactivator cooperating with nuclear
CC       hormone receptors to potentiate transcriptional activation. Also
CC       involved in vitamin D-coupled transcription regulation via its
CC       association with the WINAC complex, a chromatin-remodeling complex
CC       recruited by vitamin D receptor (VDR), which is required for the
CC       ligand-bound VDR-mediated transrepression of the CYP27B1 gene.
CC       Component of the CREST-BRG1 complex, a multiprotein complex that
CC       regulates promoter activation by orchestrating a calcium-dependent
CC       release of a repressor complex and a recruitment of an activator
CC       complex. In resting neurons, transcription of the c-FOS promoter
CC       is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC
CC       repressor complex. Upon calcium influx, RB1 is dephosphorylated by
CC       calcineurin, which leads to release of the repressor complex. At
CC       the same time, there is increased recruitment of CREBBP to the
CC       promoter by a CREST-dependent mechanism, which leads to
CC       transcriptional activation. The CREST-BRG1 complex also binds to
CC       the NR2B promoter, and activity-dependent induction of NR2B
CC       expression involves a release of HDAC1 and recruitment of CREBBP
CC       (By similarity). Belongs to the neural progenitors-specific
CC       chromatin remodeling complex (npBAF complex) and the neuron-
CC       specific chromatin remodeling complex (nBAF complex). During
CC       neural development a switch from a stem/progenitor to a post-
CC       mitotic chromatin remodeling mechanism occurs as neurons exit the
CC       cell cycle and become committed to their adult state. The
CC       transition from proliferating neural stem/progenitor cells to
CC       post-mitotic neurons requires a switch in subunit composition of
CC       the npBAF and nBAF complexes. As neural progenitors exit mitosis
CC       and differentiate into neurons, npBAF complexes which contain
CC       ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous
CC       alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits
CC       in neuron-specific complexes (nBAF). The npBAF complex is
CC       essential for the self-renewal/proliferative capacity of the
CC       multipotent neural stem cells. The nBAF complex along with CREST
CC       plays a role regulating the activity of genes essential for
CC       dendrite growth. SMARCA4/BAF190A may promote neural stem cell
CC       self-renewal/proliferation by enhancing Notch-dependent
CC       proliferative signals, while concurrently making the neural stem
CC       cell insensitive to SHH-dependent differentiating cues. Acts as a
CC       corepressor of ZEB1 to regulate E-cadherin transcription and is
CC       required for induction of epithelial-mesenchymal transition (EMT)
CC       by ZEB1 (By similarity).
CC   -!- SUBUNIT: Interacts with NR3C1, PGR, SMARD1, TOPBP1 and
CC       ZMIM2/ZIMP7. Component of the BAF complex, which includes at least
CC       actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2,
CC       SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57,
CC       SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, IKFZ1, and one
CC       or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C.
CC       Interacts directly with IKFZ1 in the BAF complex. In muscle cells,
CC       the BAF complex also contains DPF3. Component of the BAF53
CC       complex, at least composed of BAF53A, RUVBL1,
CC       SMARCA4/BRG1/BAF190A, and TRRAP, which preferentially acetylates
CC       histone H4 (and H2A) within nucleosomes. Component of the WINAC
CC       complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1,
CC       SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H,
CC       CHAF1A and TOP2B. Component of the CREST-BRG1 complex, at least
CC       composed of SMARCA4/BRG1/BAF190A, SS18L1/CREST, HDAC1, RB1 and
CC       SP1. Interacts with (via the bromodomain) with TERT; the
CC       interaction regulates Wnt-mediated signaling. Component of neural
CC       progenitors-specific chromatin remodeling complex (npBAF complex)
CC       composed of at least, ARID1A/BAF250A or ARID1B/BAF250B,
CC       SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B,
CC       SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155,
CC       SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and
CC       actin. Component of neuron-specific chromatin remodeling complex
CC       (nBAF complex) composed of at least, ARID1A/BAF250A or
CC       ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
CC       SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
CC       SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B,
CC       DPF3/BAF45C, ACTL6B/BAF53B and actin. Interacts with PHF10/BAF45A.
CC       Interacts with ZEB1 (via N-terminus) (By similarity).
CC   -!- INTERACTION:
CC       P06400:RB1 (xeno); NbExp=1; IntAct=EBI-1210244, EBI-491274;
CC       P13405:Rb1; NbExp=1; IntAct=EBI-1210244, EBI-971782;
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3TKT4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3TKT4-2; Sequence=VSP_038696;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC   -!- SIMILARITY: Contains 1 bromo domain.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 HSA domain.
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DR   EMBL; AK147285; BAE27821.1; -; mRNA.
DR   EMBL; AK160825; BAE36034.1; -; mRNA.
DR   EMBL; AK166837; BAE39059.1; -; mRNA.
DR   EMBL; BC079560; AAH79560.1; -; mRNA.
DR   EMBL; CH466522; EDL25209.1; -; Genomic_DNA.
DR   IPI; IPI00875789; -.
DR   IPI; IPI00955124; -.
DR   RefSeq; NP_001167549.1; NM_001174078.1.
DR   RefSeq; NP_001167550.1; NM_001174079.1.
DR   RefSeq; NP_035547.2; NM_011417.3.
DR   UniGene; Mm.286593; -.
DR   ProteinModelPortal; Q3TKT4; -.
DR   SMR; Q3TKT4; 738-1279, 1416-1535.
DR   IntAct; Q3TKT4; 11.
DR   STRING; Q3TKT4; -.
DR   PRIDE; Q3TKT4; -.
DR   Ensembl; ENSMUST00000034707; ENSMUSP00000034707; ENSMUSG00000032187.
DR   GeneID; 20586; -.
DR   KEGG; mmu:20586; -.
DR   UCSC; uc009ome.1; mouse.
DR   CTD; 20586; -.
DR   MGI; MGI:88192; Smarca4.
DR   HOVERGEN; HBG056636; -.
DR   OrthoDB; EOG418BMJ; -.
DR   PhylomeDB; Q3TKT4; -.
DR   ArrayExpress; Q3TKT4; -.
DR   Bgee; Q3TKT4; -.
DR   Genevestigator; Q3TKT4; -.
DR   GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR   GO; GO:0071565; C:nBAF complex; IDA:UniProtKB.
DR   GO; GO:0071564; C:npBAF complex; IDA:UniProtKB.
DR   GO; GO:0005719; C:nuclear euchromatin; IDA:MGI.
DR   GO; GO:0005726; C:perichromatin fibrils; IDA:MGI.
DR   GO; GO:0005625; C:soluble fraction; IDA:MGI.
DR   GO; GO:0016514; C:SWI/SNF complex; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; TAS:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR   GO; GO:0008134; F:transcription factor binding; IPI:MGI.
DR   GO; GO:0001832; P:blastocyst growth; IMP:MGI.
DR   GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
DR   GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR   GO; GO:0006338; P:chromatin remodeling; IMP:MGI.
DR   GO; GO:0060318; P:definitive erythrocyte differentiation; IMP:MGI.
DR   GO; GO:0010424; P:DNA methylation on cytosine within a CG sequence; IMP:MGI.
DR   GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
DR   GO; GO:0048562; P:embryonic organ morphogenesis; IMP:MGI.
DR   GO; GO:0048730; P:epidermis morphogenesis; IMP:MGI.
DR   GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0007403; P:glial cell fate determination; IMP:MGI.
DR   GO; GO:0060347; P:heart trabecula formation; IGI:MGI.
DR   GO; GO:0030902; P:hindbrain development; IMP:MGI.
DR   GO; GO:0043966; P:histone H3 acetylation; IMP:MGI.
DR   GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI.
DR   GO; GO:0001889; P:liver development; IMP:MGI.
DR   GO; GO:0006346; P:methylation-dependent chromatin silencing; IDA:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0006334; P:nucleosome assembly; TAS:MGI.
DR   GO; GO:0010552; P:positive regulation of gene-specific transcription from RNA polymerase II promoter; IMP:MGI.
DR   GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR   InterPro; IPR006576; BRK_domain.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR   InterPro; IPR013999; HAS_subgroup.
DR   InterPro; IPR014012; Helicase/SANT-assoc_DNA-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR006562; HSA.
DR   InterPro; IPR000330; SNF2_N.
DR   Gene3D; G3DSA:1.20.920.10; Bromodomain; 1.
DR   Pfam; PF07533; BRK; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07529; HSA; 1.
DR   Pfam; PF08880; QLQ; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00592; BRK; 1.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00573; HSA; 1.
DR   SMART; SM00951; QLQ; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51204; HSA; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Alternative splicing; ATP-binding;
KW   Bromodomain; Chromatin regulator; Helicase; Hydrolase; Neurogenesis;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   1613       Transcription activator BRG1.
FT                                /FTId=PRO_0000391343.
FT   DOMAIN      460    532       HSA.
FT   DOMAIN      766    931       Helicase ATP-binding.
FT   DOMAIN     1084   1246       Helicase C-terminal.
FT   DOMAIN     1443   1513       Bromo.
FT   NP_BIND     779    786       ATP (Potential).
FT   REGION        1    282       Necessary for interaction with
FT                                SS18L1/CREST (By similarity).
FT   MOTIF       881    884       DEGH box (By similarity).
FT   COMPBIAS      4    344       Pro-rich.
FT   COMPBIAS    663    672       Poly-Glu.
FT   COMPBIAS   1252   1370       Glu-rich.
FT   COMPBIAS   1531   1555       Glu-rich.
FT   SITE       1505   1506       Required for binding to 'Lys-15'-
FT                                acetylated histone 3 (By similarity).
FT   MOD_RES      11     11       Phosphothreonine (By similarity).
FT   MOD_RES     188    188       N6-acetyllysine (By similarity).
FT   MOD_RES     455    455       N6-acetyllysine (By similarity).
FT   MOD_RES     609    609       Phosphothreonine (By similarity).
FT   MOD_RES     610    610       Phosphoserine.
FT   MOD_RES     613    613       Phosphoserine.
FT   MOD_RES     655    655       Phosphoserine (By similarity).
FT   MOD_RES     657    657       Phosphoserine (By similarity).
FT   MOD_RES     660    660       Phosphoserine (By similarity).
FT   MOD_RES     662    662       Phosphoserine (By similarity).
FT   MOD_RES     695    695       Phosphoserine.
FT   MOD_RES     699    699       Phosphoserine (By similarity).
FT   MOD_RES     721    721       Phosphoserine (By similarity).
FT   MOD_RES    1349   1349       Phosphoserine (By similarity).
FT   MOD_RES    1419   1419       Phosphoserine.
FT   MOD_RES    1536   1536       Phosphoserine (By similarity).
FT   MOD_RES    1541   1541       Phosphoserine (By similarity).
FT   MOD_RES    1552   1552       Phosphoserine (By similarity).
FT   MOD_RES    1593   1593       Phosphoserine (By similarity).
FT   MOD_RES    1597   1597       Phosphoserine (By similarity).
FT   MOD_RES    1606   1606       Phosphoserine (By similarity).
FT   MOD_RES    1608   1608       Phosphoserine (By similarity).
FT   MOD_RES    1610   1610       Phosphoserine (By similarity).
FT   VAR_SEQ    1441   1441       D -> DS (in isoform 2).
FT                                /FTId=VSP_038696.
FT   CONFLICT   1355   1355       W -> WLKT (in Ref. 1; BAE36034).
SQ   SEQUENCE   1613 AA;  181427 MW;  C23804ED858F98FE CRC64;
     MSTPDPPLGG TPRPGPSPGP GPSPGAMLGP SPGPSPGSAH SMMGPSPGPP SAGHPMPTQG
     PGGYPQDNMH QMHKPMESMH EKGMPDDPRY NQMKGMGMRS GAHTGMAPPP SPMDQHSQGY
     PSPLGGSEHA SSPVPASGPS SGPQMSSGPG GAPLDGSDPQ ALGQQNRGPT PFNQNQLHQL
     RAQIMAYKML ARGQPLPDHL QMAVQGKRPM PGMQQQMPTL PPPSVSATGP GPGPGPGPGP
     GPGPAPPNYS RPHGMGGPNM PPPGPSGVPP GMPGQPPGGP PKPWPEGPMA NAAAPTSTPQ
     KLIPPQPTGR PSPAPPAVPP AASPVMPPQT QSPGQPAQPA PLVPLHQKQS RITPIQKPRG
     LDPVEILQER EYRLQARIAH RIQELENLPG SLAGDLRTKA TIELKALRLL NFQRQLRQEV
     VVCMRRDTAL ETALNAKAYK RSKRQSLREA RITEKLEKQQ KIEQERKRRQ KHQEYLNSIL
     QHAKDFREYH RSVTGKLQKL TKAVATYHAN TEREQKKENE RIEKERMRRL MAEDEEGYRK
     LIDQKKDKRL AYLLQQTDEY VANLTELVRQ HKAAQVAKEK KKKKKKKKAE NAEGQTPAIG
     PDGEPLDETS QMSDLPVKVI HVESGKILTG TDAPKAGQLE AWLEMNPGYE VAPRSDSEES
     GSEEEEEEEE EEQPQPAQPP TLPVEEKKKI PDPDSDDVSE VDARHIIENA KQDVDDEYGV
     SQALARGLQS YYAVAHAVTE RVDKQSALMV NGVLKQYQIK GLEWLVSLYN NNLNGILADE
     MGLGKTIQTI ALITYLMEHK RINGPFLIIV PLSTLSNWAY EFDKWAPSVV KVSYKGSPAA
     RRAFVPQLRS GKFNVLLTTY EYIIKDKHIL AKIRWKYMIV DEGHRMKNHH CKLTQVLNTH
     YVAPRRLLLT GTPLQNKLPE LWALLNFLLP TIFKSCSTFE QWFNAPFAMT GEKVDLNEEE
     TILIIRRLHK VLRPFLLRRL KKEVEAQLPE KVEYVIKCDM SALQRVLYRH MQAKGVLLTD
     GSEKDKKGKG GTKTLMNTIM QLRKICNHPY MFQHIEESFS EHLGFTGGIV QGLDLYRASG
     KFELLDRILP KLRATNHKVL LFCQMTSLMT IMEDYFAYRG FKYLRLDGTT KAEDRGMLLK
     TFNEPGSEYF IFLLSTRAGG LGLNLQSADT VIIFDSDWNP HQDLQAQDRA HRIGQQNEVR
     VLRLCTVNSV EEKILAAAKY KLNVDQKVIQ AGMFDQKSSS HERRAFLQAI LEHEEQDEEE
     DEVPDDETVN QMIARHEEEF DLFMRMDLDR RREEARNPKR KPRLMEEDEL PSWIIKDDAE
     VERLTCEEEE EKMFGRGSRH RKEVDYSDSL TEKQWLKAIE EGTLEEIEEE VRQKKSSRKR
     KRDSEAGSST PTTSTRSRDK DEESKKQKKR GRPPAEKLSP NPPNLTKKMK KIVDAVIKYK
     DSSGRQLSEV FIQLPSRKEL PEYYELIRKP VDFKKIKERI RNHKYRSLND LEKDVMLLCQ
     NAQTFNLEGS LIYEDSIVLQ SVFTSVRQKI EKEDDSEGEE SEEEEEGEEE GSESESRSVK
     VKIKLGRKEK AQDRLKGGRR RPSRGSRAKP VVSDDDSEEE QEEDRSGSGS EED
//
ID   Q3TL33_MOUSE            Unreviewed;       315 AA.
AC   Q3TL33;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 46.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Calu;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK166705; BAE38959.1; -; mRNA.
DR   IPI; IPI00399958; -.
DR   UniGene; Mm.392075; -.
DR   UniGene; Mm.466282; -.
DR   ProteinModelPortal; Q3TL33; -.
DR   STRING; Q3TL33; -.
DR   Ensembl; ENSMUST00000090481; ENSMUSP00000087967; ENSMUSG00000029767.
DR   MGI; MGI:1097158; Calu.
DR   HOGENOM; HBG388084; -.
DR   HOVERGEN; HBG002834; -.
DR   InParanoid; Q3TL33; -.
DR   ArrayExpress; Q3TL33; -.
DR   Bgee; Q3TL33; -.
DR   Genevestigator; Q3TL33; -.
DR   GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   SMART; SM00054; EFh; 5.
DR   PROSITE; PS00018; EF_HAND_1; 4.
DR   PROSITE; PS50222; EF_HAND_2; 6.
PE   2: Evidence at transcript level;
KW   Calcium.
SQ   SEQUENCE   315 AA;  37119 MW;  42D8C9EE02EE373A CRC64;
     MDLRQFLMCL SLCTAFALSK PTEKKDRVHH EPQLSDKVHN DAQNFDYDHD AFLGAEEAKS
     FDQLTPEESK ERLGMIVDKI DADKDGFVTE GELKSWIKHA QKKYIYDNVE NQWQEFDMNQ
     DGLISWDEYR NVTYGTYLDD PDPDDGFNYK QMMVRDERRF KMADKDGDLI ATKEEFTAFL
     HPEEYDYMKD IVVQETMEDI DKNADGFIDL EEYIGDMYSH DGNADEPEWV KTEREQFVEF
     RDKDRDGKMD KEETKDWILP SDYDHAEAEA RHLVYESDQN KDGKLTKEEI VDKYDLFVGS
     QATDFGEALV RHDEF
//
ID   Q3TL71_MOUSE            Unreviewed;       464 AA.
AC   Q3TL71;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 42.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Hnrnpk; Synonyms=Hnrpk;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 3 KH domains.
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DR   EMBL; AK166656; BAE38921.1; -; mRNA.
DR   IPI; IPI00224575; -.
DR   UniGene; Mm.142872; -.
DR   UniGene; Mm.470123; -.
DR   ProteinModelPortal; Q3TL71; -.
DR   SMR; Q3TL71; 41-217, 385-457.
DR   STRING; Q3TL71; -.
DR   Ensembl; ENSMUST00000116403; ENSMUSP00000112104; ENSMUSG00000021546.
DR   MGI; MGI:99894; Hnrnpk.
DR   HOGENOM; HBG713491; -.
DR   HOVERGEN; HBG051916; -.
DR   InParanoid; Q3TL71; -.
DR   ArrayExpress; Q3TL71; -.
DR   Bgee; Q3TL71; -.
DR   Genevestigator; Q3TL71; -.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR004088; KH_type_1.
DR   InterPro; IPR018111; KH_type_1_subgr.
DR   InterPro; IPR012987; ROK_N.
DR   Pfam; PF00013; KH_1; 3.
DR   Pfam; PF08067; ROKNT; 1.
DR   SMART; SM00322; KH; 3.
DR   PROSITE; PS50084; KH_TYPE_1; 3.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   464 AA;  51008 MW;  E3DAB85B2169DB8A CRC64;
     METEQPEETF PNTETNGEFG KRPAEDMEEE QAFKRSRNTD EMVELRILLQ SKNAGAVIGK
     GGKNIKALRT DYNASVSVPD SSGPERILSI SADIETIGEI LKKIIPTLEE GLQLPSPTAT
     SQLPLKSDAV ECLNYQHYKG SDFDCELRLL IHQSLAGGII GVKGAKIKEL RENTQTTIKL
     FQECCPHSTD RVVLIGGKPD RVVECIKIIL DLISESPIKG RAQPYDPNFY DETYDYGGFT
     MMFDDRRGRP VGFPMRGRGG FDRMPPGRGG RPMPPSRRDY DDMSPRRGPP PPPPGRGGRG
     GSRARNLPLP PPPPPRGGDL MAYDRRGRPG DHYDGMVGFS ADETWDSAID TWSPSEWQMA
     YEPQGGSGYD YSYAGGRGSY GDLGGPIITT QVTIPKDLAG SIIGKGGQRI KQIRHESGAS
     IKIDEPLEGS EDRIITITGT QDQIQNAQYL LQNSVKQYAD VEGF
//
ID   PRC2C_MOUSE             Reviewed;        2828 AA.
AC   Q3TLH4; Q05CS4; Q05DM5; Q3TKF3; Q3UXU5; Q4FZE4; Q66K03; Q6P3F4;
AC   Q80TK3; Q80YR0; Q8BMJ4; Q8C1K7; Q8CGH3;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   08-MAR-2011, entry version 38.
DE   RecName: Full=Protein PRRC2C;
DE   AltName: Full=BAT2 domain-containing protein 1;
DE   AltName: Full=HLA-B-associated transcript 2-like 2;
DE   AltName: Full=Proline-rich and coiled-coil-containing protein 2C;
GN   Name=Prrc2c; Synonyms=Bat2d, Bat2d1, Bat2l2, Kiaa1096;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-893 (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1-1103 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1-513 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, Mammary gland, and Wolffian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-589 (ISOFORM 2),
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-571 (ISOFORM 1),
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1283-1685, AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 2522-2793 (ISOFORM 5).
RC   STRAIN=C57BL/6J, Czech II, and FVB/N;
RC   TISSUE=Embryo, Jaw, Limb, Lung, Mammary tumor, and Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 904-2056.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1917, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-851; SER-897; SER-1217
RP   AND THR-2607, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100; SER-851 AND
RP   THR-2607, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2607, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q3TLH4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3TLH4-2; Sequence=VSP_035252;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q3TLH4-3; Sequence=VSP_035251;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q3TLH4-4; Sequence=VSP_035252, VSP_035253, VSP_035254;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q3TLH4-5; Sequence=VSP_035255;
CC         Note=No experimental confirmation available;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH06723.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAH21412.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAH37745.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAH80672.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAH99612.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=BAC27127.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK013732; BAC25414.1; -; mRNA.
DR   EMBL; AK030766; BAC27127.1; ALT_SEQ; mRNA.
DR   EMBL; AK135245; BAE22468.1; -; mRNA.
DR   EMBL; AK166509; BAE38818.1; -; mRNA.
DR   EMBL; AK167018; BAE39192.1; -; mRNA.
DR   EMBL; AC132867; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC118643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC006723; AAH06723.1; ALT_SEQ; mRNA.
DR   EMBL; BC021412; AAH21412.1; ALT_SEQ; mRNA.
DR   EMBL; BC037745; AAH37745.1; ALT_SEQ; mRNA.
DR   EMBL; BC050871; AAH50871.1; -; mRNA.
DR   EMBL; BC064009; AAH64009.1; -; mRNA.
DR   EMBL; BC080672; AAH80672.1; ALT_SEQ; mRNA.
DR   EMBL; BC099612; AAH99612.1; ALT_SEQ; mRNA.
DR   EMBL; AK122441; BAC65723.1; -; Transcribed_RNA.
DR   IPI; IPI00330171; -.
DR   IPI; IPI00659535; -.
DR   IPI; IPI00831515; -.
DR   IPI; IPI00903386; -.
DR   IPI; IPI00903422; -.
DR   UniGene; Mm.245446; -.
DR   Ensembl; ENSMUST00000028016; ENSMUSP00000028016; ENSMUSG00000040225.
DR   MGI; MGI:1913754; Prrc2c.
DR   eggNOG; roNOG13617; -.
DR   GeneTree; ENSGT00530000063496; -.
DR   HOVERGEN; HBG107491; -.
DR   InParanoid; Q3TLH4; -.
DR   OrthoDB; EOG43BMPT; -.
DR   ArrayExpress; Q3TLH4; -.
DR   Bgee; Q3TLH4; -.
DR   Genevestigator; Q3TLH4; -.
DR   InterPro; IPR009738; BAT2_N.
DR   Pfam; PF07001; BAT2_N; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Phosphoprotein.
FT   CHAIN         1   2828       Protein PRRC2C.
FT                                /FTId=PRO_0000349240.
FT   COILED      993   1024       Potential.
FT   COILED     1653   1679       Potential.
FT   COMPBIAS    379    438       Pro-rich.
FT   COMPBIAS    466    625       Glu-rich.
FT   COMPBIAS    528    677       Gln-rich.
FT   COMPBIAS    671    743       Pro-rich.
FT   COMPBIAS   1031   1060       Pro-rich.
FT   COMPBIAS   1312   1414       Arg-rich.
FT   COMPBIAS   1730   1737       Poly-Ala.
FT   COMPBIAS   1788   1791       Poly-Ser.
FT   COMPBIAS   2279   2568       Gln-rich.
FT   MOD_RES      27     27       N6-acetyllysine (By similarity).
FT   MOD_RES      47     47       N6-acetyllysine (By similarity).
FT   MOD_RES     100    100       Phosphoserine.
FT   MOD_RES     187    187       Phosphoserine (By similarity).
FT   MOD_RES     190    190       Phosphoserine (By similarity).
FT   MOD_RES     391    391       N6-acetyllysine (By similarity).
FT   MOD_RES     499    499       Phosphoserine (By similarity).
FT   MOD_RES     753    753       Phosphoserine (By similarity).
FT   MOD_RES     851    851       Phosphoserine.
FT   MOD_RES     897    897       Phosphoserine.
FT   MOD_RES    1213   1213       Phosphoserine (By similarity).
FT   MOD_RES    1215   1215       Phosphothreonine (By similarity).
FT   MOD_RES    1217   1217       Phosphoserine.
FT   MOD_RES    1220   1220       Phosphoserine (By similarity).
FT   MOD_RES    1917   1917       Phosphoserine.
FT   MOD_RES    1947   1947       Phosphoserine (By similarity).
FT   MOD_RES    2039   2039       Phosphoserine (By similarity).
FT   MOD_RES    2077   2077       Phosphoserine (By similarity).
FT   MOD_RES    2607   2607       Phosphothreonine.
FT   MOD_RES    2616   2616       Phosphothreonine (By similarity).
FT   MOD_RES    2620   2620       Phosphoserine (By similarity).
FT   VAR_SEQ       1    242       Missing (in isoform 3).
FT                                /FTId=VSP_035251.
FT   VAR_SEQ      37     37       T -> TVA (in isoform 2 and isoform 4).
FT                                /FTId=VSP_035252.
FT   VAR_SEQ     174    205       Missing (in isoform 4).
FT                                /FTId=VSP_035253.
FT   VAR_SEQ     206   2828       Missing (in isoform 4).
FT                                /FTId=VSP_035254.
FT   VAR_SEQ    2666   2744       Missing (in isoform 5).
FT                                /FTId=VSP_035255.
FT   CONFLICT    184    184       C -> S (in Ref. 1; BAC27127/BAE39192 and
FT                                3; AAH64009/AAH80672/AAH06723).
FT   CONFLICT    262    262       G -> V (in Ref. 1; BAC25414).
FT   CONFLICT    345    345       K -> E (in Ref. 1; BAC25414).
FT   CONFLICT    380    380       T -> A (in Ref. 1; BAC27127/BAE39192/
FT                                BAC25414 and 3; AAH64009/AAH80672/
FT                                AAH06723).
FT   CONFLICT    561    561       E -> K (in Ref. 3; AAH64009).
FT   CONFLICT    844    844       G -> E (in Ref. 1; BAC27127).
FT   CONFLICT   1360   1360       G -> E (in Ref. 3; AAH50871).
FT   CONFLICT   1489   1489       M -> K (in Ref. 3; AAH50871).
FT   CONFLICT   1684   1684       N -> K (in Ref. 3; AAH50871).
SQ   SEQUENCE   2828 AA;  308904 MW;  97A18D23B51AF7B1 CRC64;
     MSEKSGQSTK AKDGKKYATL SLFNTYKGKS LETQKTTARH GLQSLGKVGI SRRMPPPANL
     PSLKAENKGN DPNVNIVPKD GTGWASKQEQ HEEEKAPEVS PAQPKPGVAA PPEVAPAPKS
     WASNKQGGQG DGIQVNSQFQ QEFPSLQAAG DQEKKEKEAN DENYGPGPSL RPPNVACWRD
     GGKCAGSPSS DQDEKQLGQD ESTAITSEQN DILKVVEKRI ACGPPQAKLN GQQPALASQY
     RAMMPPYMFQ QYPRMAYPPL HGPMRFPPSL SEANKSLRGR GPPPSWASEP ERPSILSASE
     LKELDKFDNL DAEADEGWAG AQMEVDYTEQ LNFSDDDEQG STSPKESSSE DQTAKTPEST
     ENRKEVDEAS STKSSSQIPT QPPVTKSPYG KGPPFNQERG PSSHLPPPPK LLAQQHPPPP
     DRQIPGRQGP FPSKPPVPDN DEIWKQRRKQ QSEISAAVER ARKRREEEER RMEEQRKAAC
     AEKLKQLDEK LGIIEKQPSP EELREREREK ERERELEKEK ERELEKEQEK QREMERARQQ
     EKELEQQREK EQELQRLREQ EKEGEPKEQE KEEKVEPQEP VVEPATENQE SENNCKKEEE
     PIFTRQDSNR SEKETTQVVQ EAEPESGAQP RPGYFKQFQK SLPPRFQRQQ EQMKQQQWQQ
     QQQQQQQGVL PQTVPSQPSN GSVPPPPHRP LYQPMQPHPQ HLASMGFDPR WLMMQSYMDP
     RMISGRPAMD IPPIHPGMIP PKPLIRRDQM EGSPNSSESF EHIARSARDH GISLSEPRMM
     WGSDPYHAEP QQAATPKSAE ETGDARPETA MDHEHMTAAY PVEHSQLETH SKTDVARDST
     ETEGQKFLSR SLEDVKPRHV DTNTQSACFD VIDQKSLPTS AEERISALES QPARKRSVSH
     GSNHAQNAEE QRNEPSVSIP KVINRCMDSK ETVEKPEEKP RKDGFLRSSE GPKPEKVYKS
     KSETRWGPRP SSNRREEGND RPVRRSGPIK KPVLRDMKEE REQRKEKEGE KLEKVTEKVV
     KAEKPEKKDL PLPLPPPAPA QPQPQPLVSP PVQPEPEKPP STETSTLTQK PSQDEKPLEP
     VGSVQVEPVV KTVNQQSVAA PTVKEEKPPE KVINKDVGIE RSRPDSRLAV KKDSSLPTRT
     YWKEARDRDW FPDQGYRGRG RGEYYSRGRS YRGSYGGRGR GGRGHTREYP QYRDNKPRTE
     HVPSGPLRQR EESETRSESS DFEVVPKRRR QRGSETDTDS EVHESASDKD SVSKGKLPKR
     EERPENKKPV KPQSSFKPEN HVRIDNRPLE KPYIREEDKS KPGFLPKGEP TRRGRGGTFR
     RGGRDPGGRP SRPATLRRPA YRDNQWNTRQ AEPPKPEDGG PPRRHEQFMP IPADKRPPKF
     ERKFDPARER PRRQRPTRPP RQDKPPRFRR LREREAASKT SEVLVPSNGT ANNVVQEPVN
     PPADISGNKT PDLSNQNSSD QANEEWETAS ESSDFNERRE RDEKKNADMS SQAVVKAGES
     VLPPKREIAK RSFSSQRPGV DRQNRRGNNG PPKSGRNFSG PRNERRNGPP SKGGKRGPFD
     DQASGTAGAD PVSGNSAHHQ EGVPNGAGQK NSKDAAGKKR EDTKPGPKKP KEKVDALSQF
     DLNNYASVVI IDDHPEVTVI EDPQSNLNDD GFTEVVSKKQ QKRLQDEERR KKEEQVVQVW
     SKKNIGEKGR SQTSKLPPRF AKKQATGTQQ IQAPPSAPVP VSSSAPGLTA PAAAAPASTP
     APVPILASAT ALVPVSTPAP VLTSCPAPVP TSASAPVPAS TSSPVTASSS SQPSVPAPTP
     VLASASTTVS VPILTSASIP ILASALAPAT VSSPTPVVSA TAVPSISTPA VPASAPTASV
     PLAPASAAST VPPPGLDSAD PDPDPQTSPE STRLPSAQTS NGTDFVAAGK SMPTSQSHGS
     LTAELWDSKV AAPAVLNDIS KKLGPISPPQ PPSVSAWNKP LTSFGSATSS EGTRNGQESG
     VEIGIDTIQF GAPASNGNEN EVVPVLSEKA TDKVPEPKEQ RQKQPRAGPI KAQKLPDLSL
     VENKEHKPGP IGKERSLKNR KVKDAQQVEP EGQEKPSPAV VRSTDPETAK ETKAVSEMSA
     EIGAMISVSS AEYGSDAKES VTDYTTPSSS LPNTVATNNA KMEDTLVNNV PLPNTLPLPK
     RETIQQSSSL TSVPPTTFSL TFKMESARKA WENSPNLREK GSPVTSTAPP IVSGVSSSAS
     GPSTANYSSF SSASMPQIPV ASVTPTASLS GAGTYTTSSL STKSTTTSDP PNICKVKPQQ
     LQTSSLPSAS HFSQLSCMPS LIAQQQQSPQ VYVSQSAAAQ IPAFYMDTSH LFNTQHARLA
     PPSLAQQQGF QPGLSQPTSV QQIPIPIYAP LQGQHQAQLS LGAGPAVSQA QELFSSSIQP
     YRSQPAFMQS SLSQPSVVLS GTAIHNFPAV QHQELAKAQS GLAFQQTSNP QPIPILYDHQ
     LGQASGLGSS QLIDTHLLQA RANLTQASNL YSGQVQQPGQ TNFYNTAQSP SALQQVTVPL
     PASQLSLTNF GSTGQPLIAL PQTLQPQLQH TTPQAQAQSL SRPAQVSQPF RGLIPAGTQH
     SMMATTGKMS EMELKAFGSG IDIKPGTPPI GGRSTTPTSS PFRATSTSPN SQSSKMNSVV
     YQKQFQSAPA TVRMAQPFPA QFAPQILSQP NLVPPLVRAP HTNTFPAPVQ RPPMALASQM
     PPPLTTGLMS HARLPHVARG PCGSLSGVRG NQAQAALKAE QDLKAKQRAE VLQSTQRFFS
     EQQQNKQIGG KTQRVDSDTS NPETLSDPPG TCPEKVEEKP PPAPTITTKP VRTGPIKPQA
     IKTEETKS
//
ID   TPC10_MOUSE             Reviewed;        1259 AA.
AC   Q3TLI0; Q811H4;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   08-MAR-2011, entry version 36.
DE   RecName: Full=Trafficking protein particle complex subunit 10;
DE   AltName: Full=Trafficking protein particle complex subunit TMEM1;
DE   AltName: Full=Transport protein particle subunit TMEM1;
DE            Short=TRAPP subunit TMEM1;
GN   Name=Trappc10; Synonyms=Tmem1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-132.
RC   TISSUE=Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 404-1259.
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in vesicular transport from endoplasmic
CC       reticulum to Golgi (By similarity).
CC   -!- SUBUNIT: Part of the multisubunit TRAPP (transport protein
CC       particle) complex (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the TMEM1 family.
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DR   EMBL; AK166500; BAE38812.1; -; mRNA.
DR   EMBL; BC044902; AAH44902.1; -; mRNA.
DR   IPI; IPI00408734; -.
DR   UniGene; Mm.27539; -.
DR   STRING; Q3TLI0; -.
DR   PRIDE; Q3TLI0; -.
DR   Ensembl; ENSMUST00000000384; ENSMUSP00000000384; ENSMUSG00000000374.
DR   MGI; MGI:1336209; Trappc10.
DR   eggNOG; roNOG08093; -.
DR   GeneTree; ENSGT00390000003873; -.
DR   HOGENOM; HBG357950; -.
DR   HOVERGEN; HBG108593; -.
DR   InParanoid; Q3TLI0; -.
DR   OrthoDB; EOG4Q58NK; -.
DR   ArrayExpress; Q3TLI0; -.
DR   Bgee; Q3TLI0; -.
DR   Genevestigator; Q3TLI0; -.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   InterPro; IPR011990; TPR-like_helical.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 2.
PE   2: Evidence at transcript level;
KW   ER-Golgi transport; Golgi apparatus; Phosphoprotein; Transport.
FT   CHAIN         1   1259       Trafficking protein particle complex
FT                                subunit 10.
FT                                /FTId=PRO_0000331480.
FT   COMPBIAS   1019   1022       Poly-Pro.
FT   MOD_RES     439    439       Phosphoserine (By similarity).
FT   CONFLICT    683    683       S -> N (in Ref. 2; AAH44902).
FT   CONFLICT   1047   1047       T -> I (in Ref. 2; AAH44902).
SQ   SEQUENCE   1259 AA;  141589 MW;  C1176D7154B76A3D CRC64;
     MDAPEEPQPP VVYTMENKPI VTCAGDQNLF TSIYPTLSQQ LPREPMEWRR SYGRAPKMIH
     LESNFVQFKE ELLPKEGNKA LLTFPFLHIY WTECCDTEVY KATVKDDLTK WQNVLKAHSS
     VDWLIVVVEN DAKKKNKTNI LPRTSIVDKI RNDFCNKQSD RCVVLSDPLK DSSRTQESWN
     AFLTKLRTLL LMSFTKNLGK FEDDMRTLRE KRTEPGWSFC EYFMVQEELA FVFEMLQQFE
     DALVQYDELD ALFSQYVVNF GAGDGANWLT FFCQPVKSWN GLVLRKPIDM EKRELIQKQE
     ATLLDLRSYL FSRQCTLLLF LQRPWEVAQR ALELLHSCVQ ELKLLEVSVP PGALDCWVFL
     SCLEVLQRIE GCCDRAQIDS NIAHMVGLWS YAMEKLKSLG YLCGLVSEKG PNSEDLNRTV
     DLLAGLGAER PETANTAQSP YKKLQEALSS VEAFEKHYLD LSHATIEMYT SIGRIRSAKL
     VGKDLAEFYM RKRSPQKAEM YLQGALKNYL AEGWALPVTH TRKQLAECQK HLGQMENYLQ
     TSSLLASDHH LTEEERKYFC QEILSFASQQ EDNPGHKVVL PMHSFARLKD LHFDPPNAVV
     HAGGVLTVEI TVCSQMPIPV HVDQIAVNVH FSIEKNNYRK TAEWLTKHKT SNGIITFPAE
     ASLFPASQNS LPALELSEML ERSPSDNSLN TTGIICRNVH MLLRRQESGS SLEPPSGLAL
     EDGAHVLRCS SVTLQPGANK IAFKTQAKEP GTYTLRQLRA SVGPVWFVLA HIHPIVQYDV
     YSQEPQLHVE PLADSLLAGI PQKVKFTVTT GHYTVKNGDS LQLSNVEAML ILCQAENRAV
     VYSNSREECS TALLRIQSSD KVTSIGLPTA PAYHVIEFEL EVLSLPSAPA SGGDTSVPGT
     PELHRKQKDS QRAGHCMVTT DHKVSIDCPW SIYSTVIALT FSVPFRTEHS LLSAGTRKYV
     QVCVQNLSEL DFELSDSNLE DKGHATDLRL APLNTQSQQL IHSKQSVFFV WELTWTQEPP
     PPLHCQFSVG FSPASEEQLT VSLKPYTYEF QVENFFTLYS VRAEILPASG AEYCKTGSLC
     SLEVSITRLA DLLDVDKDEA LVESEDYFST KLMYEVVDNS SNWAVCGKSC GVIAMPLAAQ
     ATHRVHMEVM PLFAGYLPLP DVRLFKYLPH HSAHASQLDA DSWIENDSLS VDKHLDDQLD
     CSSLRSRGST HSTSSSEHKG LPMPRLQALP AGQVFNSSTG MQVLVIPSQD DHVLEVSVT
//
ID   Q3TMM5_MOUSE            Unreviewed;       473 AA.
AC   Q3TMM5;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 42.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Nono;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Lung;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Lung;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Lung;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Lung;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Lung;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Lung;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Lung;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Lung;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK165855; BAE38416.1; -; mRNA.
DR   IPI; IPI00320016; -.
DR   UniGene; Mm.280069; -.
DR   UniGene; Mm.475350; -.
DR   ProteinModelPortal; Q3TMM5; -.
DR   SMR; Q3TMM5; 69-208.
DR   STRING; Q3TMM5; -.
DR   Ensembl; ENSMUST00000033673; ENSMUSP00000033673; ENSMUSG00000031311.
DR   MGI; MGI:1855692; Nono.
DR   HOVERGEN; HBG009801; -.
DR   InParanoid; Q3TMM5; -.
DR   ArrayExpress; Q3TMM5; -.
DR   Bgee; Q3TMM5; -.
DR   Genevestigator; Q3TMM5; -.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   InterPro; IPR012975; NOPS.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   Pfam; PF08075; NOPS; 1.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   473 AA;  54546 MW;  F70A31D2187E9DEC CRC64;
     MQSNKAFNLE KQNHTPRKHH QHHHQQHHQQ QQQQQQQQPP PPIPANGQQA SSQNEGLTID
     LKNFRKPGEK TFTQRSRLFV GNLPTDITEE EMRKLFEKYG KAGEVFIHKD KGFGFIRLET
     RTLAEIAKVE LDNMPLRGKQ LRVRFACHSA SLTVRNLPQY VSNELLEEAF SVFGQVERAV
     VIVDDRGRPS GKGIVEFSGK PAARKALDRC SEGSFLLTTF PRPVTVEPMD QLDDEEGLPE
     KLVIKNQQFH KEREQPPRFA QPGSFEYEYA MRWKALIEME KQQQDQVDRN IKEAREKLEM
     EMEAARHEHQ VMLMRQDLMR RQEELRRMEE LHNQEVQKRK QLELRQEEER RRREEEMRRQ
     QEEMMRRQQE GFKGTFPDAR EQEIRMGQMA MGGAMGINNR GAMPPAPVPP GTPAPPGPAT
     MMPDGTLGLT PPTTERFGEA ATMEGIGAIG GTPPAFNRPA PGAEFAPNKR RRY
//
ID   Q3TMR9_MOUSE            Unreviewed;       307 AA.
AC   Q3TMR9;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 40.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Slc12a5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK165769; BAE38372.1; -; mRNA.
DR   IPI; IPI00653739; -.
DR   UniGene; Mm.252987; -.
DR   STRING; Q3TMR9; -.
DR   Ensembl; ENSMUST00000099092; ENSMUSP00000096690; ENSMUSG00000017740.
DR   MGI; MGI:1862037; Slc12a5.
DR   GeneTree; ENSGT00560000076892; -.
DR   HOVERGEN; HBG059319; -.
DR   ArrayExpress; Q3TMR9; -.
DR   Bgee; Q3TMR9; -.
DR   Genevestigator; Q3TMR9; -.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0015379; F:potassium:chloride symporter activity; IMP:MGI.
DR   GO; GO:0007612; P:learning; IMP:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR   GO; GO:0042493; P:response to drug; IMP:MGI.
DR   GO; GO:0007268; P:synaptic transmission; IMP:MGI.
DR   GO; GO:0040040; P:thermosensory behavior; IMP:MGI.
DR   InterPro; IPR004841; AA-permease_dom.
DR   InterPro; IPR000076; KCL_cotranspt.
DR   Pfam; PF00324; AA_permease; 1.
DR   PRINTS; PR01081; KCLTRNSPORT.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   307 AA;  32967 MW;  C2567B01F3FF33F3 CRC64;
     MLNNLTDCED GDGGANPGDG NPKESSPFIN STDTEKGREY DGRNMALFEE EMDTSPMVSS
     LLSGLANYTN LPQGSREHEE AENNEGGKKK PVQAPRMGTF MGVYLPCLQN IFGVILFLRL
     TWVVGIAGIM ESFCMVFICC SCTMLTAISM SAIATNGVVP AGGSYYMISR SLGPEFGGAV
     GLCFYLGTTF AGAMYILGTI EILLAYLFPA MAIFKAEDAS GEAAAMLNNM RVYGTCVLTC
     MATVVFVGVK YVNKFALVFL EPKAERTAAG AIKRLRCGQW QGWRATALLL GSSPSQGLMR
     TGHSSRQ
//
ID   Q3TN34_MOUSE            Unreviewed;      1009 AA.
AC   Q3TN34;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   SubName: Full=JRAB;
DE   SubName: Full=RIKEN cDNA A930021H16, isoform CRA_b;
GN   Name=Micall2; Synonyms=JRAB; ORFNames=mCG_121432;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16525024; DOI=10.1091/mbc.E05-09-0826;
RA   Terai T., Nishimura N., Kanda I., Yasui N., Sasaki T.;
RT   "JRAB/MICAL-L2 is a junctional Rab13-binding protein mediating the
RT   endocytic recycling of occludin.";
RL   Mol. Biol. Cell 17:2465-2475(2006).
CC   -!- SIMILARITY: Contains 1 LIM zinc-binding domain.
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CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; AK165558; BAE38255.1; -; mRNA.
DR   EMBL; AB182579; BAE86912.1; -; mRNA.
DR   EMBL; CH466529; EDL19139.1; -; Genomic_DNA.
DR   IPI; IPI00280103; -.
DR   RefSeq; NP_777275.2; NM_174850.3.
DR   UniGene; Mm.240510; -.
DR   ProteinModelPortal; Q3TN34; -.
DR   SMR; Q3TN34; 2-114, 185-248.
DR   IntAct; Q3TN34; 12.
DR   STRING; Q3TN34; -.
DR   PRIDE; Q3TN34; -.
DR   Ensembl; ENSMUST00000044642; ENSMUSP00000039707; ENSMUSG00000036718.
DR   GeneID; 231830; -.
DR   KEGG; mmu:231830; -.
DR   NMPDR; fig|10090.3.peg.12704; -.
DR   CTD; 231830; -.
DR   MGI; MGI:2444818; Micall2.
DR   eggNOG; roNOG11373; -.
DR   HOGENOM; HBG278151; -.
DR   HOVERGEN; HBG052476; -.
DR   InParanoid; Q3TN34; -.
DR   OMA; PTSKVPT; -.
DR   OrthoDB; EOG437RFV; -.
DR   ArrayExpress; Q3TN34; -.
DR   Bgee; Q3TN34; -.
DR   Genevestigator; Q3TN34; -.
DR   GO; GO:0005923; C:tight junction; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IDA:MGI.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR022735; DUF3585.
DR   InterPro; IPR001781; Znf_LIM.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 1.
DR   Gene3D; G3DSA:2.10.110.10; Znf_LIM; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF12130; DUF3585; 1.
DR   Pfam; PF00412; LIM; 1.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00132; LIM; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE   2: Evidence at transcript level;
KW   LIM domain; Metal-binding; Zinc.
SQ   SEQUENCE   1009 AA;  108288 MW;  3D059CD22B8BAF53 CRC64;
     MAAIKALQEW CRQQCEGYRD VSITNMTTSF RDGLAFCAIL HRHRPDLINF SALRKENIYE
     NNKLAFQVAE EQLGIPALLD AEDMVALKVP DRLSILTYVS QYYNYFHGRS PIGGMAGIKR
     PSSDSTEELS GKKGLSQPAK LPSPAQTQRS PLSPARTNPV VQRNEGGSQR PSPKAAPGTA
     GSSVSSICGV CGKHVHLVQR HLADGRLYHR SCFRCKQCSS TLHSGAYRAT GEPGVFVCTH
     HSSEVTSVSP KSSNLASRKP GGVTADTRPF GVSWTVQEAN GEGTPLRVRT AAWEHAGGNT
     TAKGFVQTEL KPPSTSQVHV GSSAGPKLPT ITVTTTSVTS KALTHVTNSS PIGWSSPAQS
     SPANFNSRPV VSPSARNTHL PGSQGQTASK GVKTQLNLNS ESSNTAVTPA WTSSASKTQQ
     AREKFFQTPP SAPAPASAPA PAPTSKVPTV VTVPTSKVPN VVTAPTSKVP TVVTVPTSKV
     PTVVSAPTSK VPTVVSAPTS KVPTVVNSTN SRVTTVVNAP TSKVPTVVSA TNGRVPTVVT
     AHTGRVPAVM NTSASKVSPV VDAPAQESSR EQALSVLRKA LPALTGSGTQ APNRSFPATS
     SVLVTLPKNE VPQKVPSDKL SALTTQTPNF TIKLEPSAPV NVGNTAVFLQ AGKKSPSISP
     RVGKTSVGSR PQAEVAGVKG PGPISQEGQE EGPEGWRARL KPVDKKTPAG RSLEQKEPVL
     AEPRIGDTSR KASSSSDSSV HITLTSIQHK RKPCPAGSGP SPAALSPSPS HRKKLAVPPS
     LDVSADWLQP EPKKQEDGTR SCKEEKSPTR WSRERSAVLD SGLAPPGEAV TSPVRLHPDY
     IPQEELQRQL QDIESQLDAL ELRGVELEKR LRAAEGDASE DSLMVDWFRL IHEKQLLLRL
     ESELMYKSKD QRLEEQQLDL QGELRRLMDK PEGLKSPQDR QREQELLSQY VNTVNDRSDI
     VDFLDEDRLR EQEEDQMLEN MIQNLGLQRK KSKSFLSKIW SSKSKSGQA
//
ID   Q3TN48_MOUSE            Unreviewed;       223 AA.
AC   Q3TN48;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Zfr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK165530; BAE38241.1; -; mRNA.
DR   IPI; IPI00762823; -.
DR   UniGene; Mm.158783; -.
DR   UniGene; Mm.416021; -.
DR   PhosphoSite; Q3TN48; -.
DR   Ensembl; ENSMUST00000117798; ENSMUSP00000113913; ENSMUSG00000034949.
DR   UCSC; uc007ggq.1; mouse.
DR   MGI; MGI:2143792; Zfr2.
DR   GeneTree; ENSGT00550000074528; -.
DR   HOGENOM; HBG713351; -.
DR   InParanoid; Q3TN48; -.
DR   OrthoDB; EOG4HX511; -.
DR   ArrayExpress; Q3TN48; -.
DR   Bgee; Q3TN48; -.
DR   Genevestigator; Q3TN48; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   223 AA;  22853 MW;  CE83D288F1724024 CRC64;
     MAASSSSGLA QGTNPSSSTQ SSSAFPLPAT GASYTVQFTP KMESTASLAL APASQLPAPG
     GGVAVGYSCS QPQASQGPTS SSQPRGPVPT SASAHQEDGH SYREKVTKSR TDSRERPARS
     LCRPGPSSRS PDSDSVSPGP QRPPPSSQRA PQKLQAPSPP PAPVGSDPWG GPVLGPWDPT
     FTSDALPFLD RLPKPKAGPR PPSMHYCEVC RVSCAGPQVR TGS
//
ID   Q3TNN8_MOUSE            Unreviewed;       334 AA.
AC   Q3TNN8;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 47.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Gucy1a2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
CC       cyclase family.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK165150; BAE38050.1; -; mRNA.
DR   IPI; IPI00469830; -.
DR   RefSeq; NP_001028494.1; NM_001033322.1.
DR   UniGene; Mm.435507; -.
DR   PRIDE; Q3TNN8; -.
DR   Ensembl; ENSMUST00000115733; ENSMUSP00000111398; ENSMUSG00000041624.
DR   GeneID; 234889; -.
DR   KEGG; mmu:234889; -.
DR   CTD; 234889; -.
DR   MGI; MGI:2660877; Gucy1a2.
DR   eggNOG; roNOG05091; -.
DR   HOVERGEN; HBG051715; -.
DR   InParanoid; Q3TNN8; -.
DR   OrthoDB; EOG495ZRF; -.
DR   ArrayExpress; Q3TNN8; -.
DR   Bgee; Q3TNN8; -.
DR   Genevestigator; Q3TNN8; -.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0030828; P:positive regulation of cGMP biosynthetic process; IMP:MGI.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   InterPro; IPR011645; Haem_no_assoc-bd.
DR   Gene3D; G3DSA:3.30.70.1230; A/G_cyclase; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07701; HNOBA; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; A/G_cyclase; 1.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE   2: Evidence at transcript level;
KW   Lyase; Nucleotide-binding.
FT   NON_TER       1      1
SQ   SEQUENCE   334 AA;  37475 MW;  1549E929C762A3D7 CRC64;
     NEDKVMEIKG QMIHVPESSA ILFLGSPCVD KLDELMGRGL HLSDIPIHDA TRDVILVGEQ
     AKAQDGLKKR MDKLKATLER THQALEEEKK KTVDLLYSIF PGDVAQQLWQ GQQVQARKFD
     DVTMLFSDIV GFTAICAQCT PMQVISMLNE LYTRFDHQCG LLDIYKVETI GDAYCVASGL
     HRKSLCHAKP IALMALKMME LSEEVLTPDG KAIQMRIGIH SGSVLAGVVG VRMPRYCLFG
     NNVTLASKFE SGSHPRRINV SPTTYQLLKR EDSFTFIPRS REELPDNFPK EIPGVCYFLE
     LRTDPKPPKP SLSSSRIKKV SYNIGTMFLR ETSL
//
ID   Q3TNU6_MOUSE            Unreviewed;       166 AA.
AC   Q3TNU6;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 22.
DE   SubName: Full=Putative uncharacterized protein;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Eyeball;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Eyeball;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Eyeball;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Eyeball;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Eyeball;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Eyeball;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Eyeball;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Eyeball;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK164986; BAE37991.1; -; mRNA.
DR   IPI; IPI00653632; -.
DR   Genevestigator; Q3TNU6; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   166 AA;  19416 MW;  462C72F802CE5DE2 CRC64;
     MTFVLKLPAS VFLEGGLQFH CKQSKYVLNK KSILVTGVIY GSKYDSKKHT ETIHKAYFYV
     WMCLHMCIHV HSVQKRHRQD TLVSRSRLHD LARLGFTWQL TKSVSHPCYS CSLPTHMFRL
     FTFPAQVDVF FSSVESAASW EVGWCWRRIY STQIFQEEGF PCLLLL
//
ID   Q3TPB6_MOUSE            Unreviewed;       981 AA.
AC   Q3TPB6;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 35.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Rab3gap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK164523; BAE37821.1; -; mRNA.
DR   IPI; IPI00749720; -.
DR   RefSeq; NP_848805.2; NM_178690.4.
DR   UniGene; Mm.476343; -.
DR   ProteinModelPortal; Q3TPB6; -.
DR   STRING; Q3TPB6; -.
DR   Ensembl; ENSMUST00000037649; ENSMUSP00000042070; ENSMUSG00000036104.
DR   GeneID; 226407; -.
DR   KEGG; mmu:226407; -.
DR   UCSC; uc007clc.1; mouse.
DR   CTD; 226407; -.
DR   MGI; MGI:2445001; Rab3gap1.
DR   eggNOG; roNOG04225; -.
DR   HOVERGEN; HBG079116; -.
DR   InParanoid; Q3TPB6; -.
DR   OMA; KHRGVEE; -.
DR   PhylomeDB; Q3TPB6; -.
DR   NextBio; 378122; -.
DR   ArrayExpress; Q3TPB6; -.
DR   Bgee; Q3TPB6; -.
DR   Genevestigator; Q3TPB6; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   981 AA;  110198 MW;  D74B8B22C3D58AEA CRC64;
     MAADSEPESE VFEITDFTTA SEWERFISKV EEVLNDWKLI GPSLGKPLEK GIFTSGTWEE
     RSDEISFADF RFSVTHHYLV QESPDKERKD EELEDAIPQS MQDLLCMNND FPPRAHCLVR
     WYGLREFVVI APAAHSDAVL SESKCNLLLS SISIALGNTG CQVPLFVQIH HKWRRMYMGE
     CQGPGVRTDF EMVHLRKVPS QYTHLSGLLD IFKSKIGCPL TPLPPVSIAI RLTYVLQDWQ
     QYFWPQQPPD IDALVGGEVG GLEFGKLPFG ACEDPISELH LATTWPHLTE GIIVDNDVYS
     DLDPVQAPHW SVRVRKADNP QCLLGDFVTE FLKICRRKES TDEILGRSTF EEEGREVADI
     THALSKLTEP APVPIHKLSV SNMVHTAKKK IRKHRGEESP LNSDVLNTIL LFLFPDAVSE
     KPLDGTTSID NSIPAPEAGD YTLYNQFKSA PSDSLTYKLA LCLCMINFYH GGLKGVAHLW
     QEFVLEMRFR WENNFLIPGL ASGSPDLRCC LLHQKLQMLN CCIERKKARD EGKKTSLSDS
     TTSAYPGDAG KTGGQLGLDH LRDTEKEKGE VGKSWDSWSD SEEEFFECLS DTEDLKGNGQ
     ESGKKGGPKE MANLKPEGRL HQHGKLTLLH NGEPLYIPVT QEPAPMTEDL LEEQSEVLAK
     LGTSAEGAHL RARMQSACLL SDMESFKAAN PGCFLEDFVR WYSPRDYIEE EVTDEKGNVV
     LKGELSARMK IPSNMWVEAW ETAKPVPARR QRRLFDDTRE AEKVLHYLAM QKPADLARHL
     LPCVIHAAVL KVKEEESLEN IPSVKKIIKQ IIAHSSKVLH FPNPEDKKLE EIILQITTVE
     AIIARARSLK AKFGTEKCEH EEEKEGLERF VSCLLEQPEV SVTGAGRGHA GRIIHKLFVN
     AQRAAAVALP EEELKKSGCP EERRQTLVSD FPPPAGRELI LRATVPRPAP YSKALPQRMY
     SVLTKEDFRL AGAFSSDTSF F
//
ID   Q3TPH5_MOUSE            Unreviewed;       429 AA.
AC   Q3TPH5;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 39.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Syt11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 2 C2 domains.
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DR   EMBL; AK164368; BAE37761.1; -; mRNA.
DR   IPI; IPI00380495; -.
DR   UniGene; Mm.379376; -.
DR   ProteinModelPortal; Q3TPH5; -.
DR   SMR; Q3TPH5; 156-428.
DR   STRING; Q3TPH5; -.
DR   Ensembl; ENSMUST00000090945; ENSMUSP00000088464; ENSMUSG00000068923.
DR   Ensembl; ENSMUST00000107505; ENSMUSP00000103129; ENSMUSG00000068923.
DR   UCSC; uc008pwl.1; mouse.
DR   MGI; MGI:1859547; Syt11.
DR   eggNOG; roNOG13789; -.
DR   HOVERGEN; HBG005010; -.
DR   InParanoid; Q3TPH5; -.
DR   PhylomeDB; Q3TPH5; -.
DR   ArrayExpress; Q3TPH5; -.
DR   Bgee; Q3TPH5; -.
DR   Genevestigator; Q3TPH5; -.
DR   GO; GO:0005887; C:integral to plasma membrane; IDA:MGI.
DR   GO; GO:0008021; C:synaptic vesicle; IEA:InterPro.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   InterPro; IPR001565; Synaptotagmin.
DR   Pfam; PF00168; C2; 2.
DR   PRINTS; PR00360; C2DOMAIN.
DR   PRINTS; PR00399; SYNAPTOTAGMN.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 2.
PE   2: Evidence at transcript level;
KW   Repeat.
SQ   SEQUENCE   429 AA;  48277 MW;  0C7D5A10E89CAB01 CRC64;
     MAEITNIRPS FDVSPVAAGL IGASVLVVCV SVTVFVWTCC HQQAEKKHKT PPYKFIHMLK
     GISIYPETLS NKKKIIKVRR DKDGPRRESG RGNLLINAES GLLSHDKDPR GPSPASCMDQ
     LPIKRDYGEE LRSPMTSLTP GESKATSPSS PEEDVMLGSL TFSVDYNFPK KALVVTIQEA
     HGLPVMDDQT QGSDPYIKMT ILPDKRHRVK TRVLRKTLDP VFDETFTFYG IPYSQLQDLV
     LHFLVLSFDR FSRDDVIGEV MVPLAGVDPS TGKVQLTRDI IKRNIQKCIS RGELQVSLSY
     QPVAQRMTVV VLKARHLPKM DITGLSDPYV KVNVYYGRKR IAKKKTHVKK CTLNPVFNES
     FIYDIPTDLL PDISIEFLVI DFDRTTKNEV VGRLILGAHS VTTSGAEHWR EVCESPRKPI
     AKWHSLSEY
//
ID   Q3TPP5_MOUSE            Unreviewed;       357 AA.
AC   Q3TPP5;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Dlg1; Synonyms=Dlgh1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SIMILARITY: Contains 2 PDZ (DHR) domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK164228; BAE37690.1; -; mRNA.
DR   IPI; IPI00668389; -.
DR   UniGene; Mm.382; -.
DR   STRING; Q3TPP5; -.
DR   Ensembl; ENSMUST00000131136; ENSMUSP00000115954; ENSMUSG00000022770.
DR   UCSC; uc007yxu.1; mouse.
DR   MGI; MGI:107231; Dlg1.
DR   GeneTree; ENSGT00560000076879; -.
DR   HOGENOM; HBG671982; -.
DR   HOVERGEN; HBG107814; -.
DR   InParanoid; Q3TPP5; -.
DR   ArrayExpress; Q3TPP5; -.
DR   Bgee; Q3TPP5; -.
DR   Genevestigator; Q3TPP5; -.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0031253; C:cell projection membrane; IDA:MGI.
DR   GO; GO:0001772; C:immunological synapse; IDA:MGI.
DR   GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR   GO; GO:0045121; C:membrane raft; IDA:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0032947; F:protein complex scaffold; IMP:MGI.
DR   GO; GO:0032147; P:activation of protein kinase activity; IMP:MGI.
DR   GO; GO:0042982; P:amyloid precursor protein metabolic process; IGI:MGI.
DR   GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI.
DR   GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
DR   GO; GO:0060022; P:hard palate development; IMP:MGI.
DR   GO; GO:0001771; P:immunological synapse formation; IMP:MGI.
DR   GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI.
DR   GO; GO:0031579; P:membrane raft organization; IMP:MGI.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
DR   GO; GO:0042130; P:negative regulation of T cell proliferation; IMP:MGI.
DR   GO; GO:0030432; P:peristalsis; IMP:MGI.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0008104; P:protein localization; IMP:MGI.
DR   GO; GO:0042391; P:regulation of membrane potential; IGI:MGI.
DR   GO; GO:0048608; P:reproductive structure development; IMP:MGI.
DR   GO; GO:0048745; P:smooth muscle tissue development; IMP:MGI.
DR   GO; GO:0042110; P:T cell activation; IMP:MGI.
DR   GO; GO:0002369; P:T cell cytokine production; IMP:MGI.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR019583; PDZ_assoc.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00595; PDZ; 2.
DR   Pfam; PF10600; PDZ_assoc; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00228; PDZ; 2.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50156; PDZ; 2.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50106; PDZ; 2.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
FT   NON_TER     357    357
SQ   SEQUENCE   357 AA;  38711 MW;  2339C0D6343EFC1C CRC64;
     KAVEALKEAG SIVRLYVKRR KPASEKIMEI KLIKGPKGLG FSIAGGVGNQ HIPGDNSIYV
     TKIIEGGAAH KDGKLQIGDK LLAVNSVCLE EVTHEEAVTA LKNTSDFVYL KVAKPTTSSQ
     SVDNYVSPSS CLGQTPTSPA RYSPISKAVL GDDEITREPR KVVLHRGSTG LGFNIVGGED
     GEGIFISFIL AGGPADLSGE LRKGDRIISV NSVDLRAASH EQAAAALKNA GQAVTIVAQY
     RPEEYSRFEA KIHDLREQMM NSSVSSGSGS LRTSQKRSLY VRALFDYDKT KDSGLPSQGL
     NFRFGDILHV INASDDEWWQ ARQVTPDGES DEVGVIPSKR RVEKKERARL KTVKFNS
//
ID   EXOC5_MOUSE             Reviewed;         708 AA.
AC   Q3TPX4;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   RecName: Full=Exocyst complex component 5;
DE   AltName: Full=Exocyst complex component Sec10;
GN   Name=Exoc5; Synonyms=Sec10l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Component of the exocyst complex involved in the docking
CC       of exocystic vesicles with fusion sites on the plasma membrane (By
CC       similarity).
CC   -!- SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3,
CC       EXOC4, EXOC5, EXOC6, EXOC7 and EXOC8 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the SEC10 family.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK164067; BAE37611.1; -; mRNA.
DR   IPI; IPI00876027; -.
DR   RefSeq; NP_997097.1; NM_207214.3.
DR   UniGene; Mm.31607; -.
DR   ProteinModelPortal; Q3TPX4; -.
DR   STRING; Q3TPX4; -.
DR   PhosphoSite; Q3TPX4; -.
DR   PRIDE; Q3TPX4; -.
DR   Ensembl; ENSMUST00000089858; ENSMUSP00000087302; ENSMUSG00000061244.
DR   GeneID; 105504; -.
DR   KEGG; mmu:105504; -.
DR   CTD; 105504; -.
DR   MGI; MGI:2145645; Exoc5.
DR   eggNOG; roNOG12453; -.
DR   HOGENOM; HBG383997; -.
DR   HOVERGEN; HBG055591; -.
DR   InParanoid; Q3TPX4; -.
DR   OrthoDB; EOG4PK277; -.
DR   ArrayExpress; Q3TPX4; -.
DR   Bgee; Q3TPX4; -.
DR   CleanEx; MM_EXOC5; -.
DR   Genevestigator; Q3TPX4; -.
DR   GermOnline; ENSMUSG00000061244; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0048278; P:vesicle docking; IEA:InterPro.
DR   InterPro; IPR009976; Sec10.
DR   PANTHER; PTHR12100; Sec10; 1.
DR   Pfam; PF07393; Sec10; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Exocytosis; Phosphoprotein; Protein transport;
KW   Transport.
FT   CHAIN         1    708       Exocyst complex component 5.
FT                                /FTId=PRO_0000118944.
FT   COILED       40    101       Potential.
FT   MOD_RES     122    122       Phosphothreonine (By similarity).
SQ   SEQUENCE   708 AA;  81796 MW;  271C897C51581356 CRC64;
     MATTAELFEE PFVADEYIER LVWRTPGGGS RGGPEAFDPK RLLEEFVNHI QELQIMDERI
     QRKVEKLEQQ CQKEAKEFAK KVQELQKSNQ VAFQHFQELD EHISYVATKV CHLGDQLEGV
     NTPRQRAVEA QKLMKYFNEF LDGELKSDVF TNSEKIKEAA DVIQKLHLIA QELPFDRFSE
     VKSKIASKYH DLECQLIQEF TSAQRRGEVS RMREVAAVLL HFKGYSHCID VYIKQCQEGA
     YLRNDIFEDA AILCQRVNKQ VGDIFSNPEA VLAKLIQSVF EIKLQSFVKD QLEECRKSDA
     EQYLKSLYDL YTRTTGLSSK LMEFNLGTDK QTFLSKLIKS IFISYLENYI EVEIGYLKSR
     SAMILQRYYD SKNHQKRSIG TGGIQDLKER IRQRTNLPLG PSIDTHGETF LSQEVVVNLL
     QETKQAFERC HRLSDPSDLP RNAFRIFTIL VEFLCIEHID YALETGLAGI PSSDSRNANL
     YFLDVVQQAN TIFHLFDKQF NDHLMPLISS SPKLSECLQK KKEIIEQMEM KLDTGIDRTL
     NCMIGQMKHI LAAEQKKTDF KPEDENNVLI QYTNACVKVC VYVRKQVEKI KNSMDGKNVD
     TVLMELGVRF HRLIYEHLQQ YSYSCMGDML AICDVAEYRK CAKDFKIPMV LHLFDTLHAL
     CNLLVVAPDN LKQVCSGEQL ANLDKNILHS FVQLRADYRS ARLARHFS
//
ID   Q3TQ02_MOUSE            Unreviewed;       524 AA.
AC   Q3TQ02;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   RecName: Full=Alkaline phosphatase;
DE            EC=3.1.3.1;
GN   Name=Alpl; Synonyms=Akp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
CC       phosphate.
CC   -!- SIMILARITY: Belongs to the alkaline phosphatase family.
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DR   EMBL; AK164002; BAE37583.1; -; mRNA.
DR   IPI; IPI00877320; -.
DR   RefSeq; NP_031457.2; NM_007431.2.
DR   UniGene; Mm.288186; -.
DR   ProteinModelPortal; Q3TQ02; -.
DR   SMR; Q3TQ02; 18-498.
DR   STRING; Q3TQ02; -.
DR   Ensembl; ENSMUST00000030551; ENSMUSP00000030551; ENSMUSG00000028766.
DR   GeneID; 11647; -.
DR   KEGG; mmu:11647; -.
DR   CTD; 11647; -.
DR   MGI; MGI:87983; Alpl.
DR   HOVERGEN; HBG007345; -.
DR   InParanoid; Q3TQ02; -.
DR   NextBio; 279245; -.
DR   ArrayExpress; Q3TQ02; -.
DR   Bgee; Q3TQ02; -.
DR   Genevestigator; Q3TQ02; -.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0004035; F:alkaline phosphatase activity; IDA:MGI.
DR   GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
DR   GO; GO:0046677; P:response to antibiotic; IDA:MGI.
DR   InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
DR   InterPro; IPR001952; Alkaline_phosphatase.
DR   InterPro; IPR018299; Alkaline_phosphatase_AS.
DR   InterPro; IPR017850; Alkaline_phosphatase_core.
DR   Gene3D; G3DSA:3.40.720.10; Alk_phosphtse; 1.
DR   Pfam; PF00245; Alk_phosphatase; 1.
DR   PRINTS; PR00113; ALKPHPHTASE.
DR   SMART; SM00098; alkPPc; 1.
DR   SUPFAM; SSF53649; Alkaline_phosphatase_core; 1.
DR   PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Phosphoprotein; Zinc.
SQ   SEQUENCE   524 AA;  57501 MW;  30C0FF789A313DA7 CRC64;
     MISPFLVLAI GTCLTNSFVP EKERDPSYWR QQAQETLKNA LKLQKLSTNV AKNVIMFLGD
     GMGVSTVTAA RILKGQLHHN TGEETRLEMD KFPFVALSKT YNTNAQVPDS AGTATAYLCG
     VKANEGTVGV SAATERTRCN TTQGNEVTSI LRWAKDAGKS VGIVTTTRVN HATPSAAYAH
     SADRDWYSDN EMPPEALSQG CKDIAYQLMH NIKDIDVIMG GGRKYMYPKN RTDVEYELDE
     KARGTRLDGL DLISIWKSFK PRHKHSHYVW NRTELLALDP TRVDYLLGLF EPGDMQYELN
     RNNLTDPSLS EMVEVALRIL TKNLKGFFLL VEGGRIDHGH HEGKAKQALH EAVEMDQAIG
     KAGAMTSQKD TLTVVTADHS HVFTFGGYTP RGNSIFGLAP MVSDTDKKPF TAILYGNGPG
     YKVVDGEREN VSMVDYAHNN YQAQSAVPLR HETHGGEDVA VFAKGPMAHL LHGVHEQNYI
     PHVMAYASCI GANLDHCAWA GSGSAPSPGA LLLPLAVLSL RTLF
//
ID   CI078_MOUSE             Reviewed;         289 AA.
AC   Q3TQI7;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   RecName: Full=Uncharacterized protein C9orf78 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-147, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-17, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-261, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
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DR   EMBL; AK163554; BAE37395.1; -; mRNA.
DR   IPI; IPI00115553; -.
DR   RefSeq; NP_659134.1; NM_144885.2.
DR   UniGene; Mm.235238; -.
DR   PRIDE; Q3TQI7; -.
DR   Ensembl; ENSMUST00000028205; ENSMUSP00000028205; ENSMUSG00000026851.
DR   GeneID; 227707; -.
DR   KEGG; mmu:227707; -.
DR   MGI; MGI:2385132; BC005624.
DR   eggNOG; roNOG07941; -.
DR   HOGENOM; HBG713379; -.
DR   HOVERGEN; HBG055019; -.
DR   InParanoid; Q3TQI7; -.
DR   OrthoDB; EOG4D7Z69; -.
DR   ArrayExpress; Q3TQI7; -.
DR   Bgee; Q3TQI7; -.
DR   CleanEx; MM_BC005624; -.
DR   Genevestigator; Q3TQI7; -.
DR   GermOnline; ENSMUSG00000026851; Mus musculus.
DR   InterPro; IPR010756; Hep_59.
DR   PANTHER; PTHR13486; Hep_59; 1.
DR   Pfam; PF07052; Hep_59; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    289       Uncharacterized protein C9orf78 homolog.
FT                                /FTId=PRO_0000227524.
FT   MOD_RES      15     15       Phosphoserine.
FT   MOD_RES      17     17       Phosphoserine.
FT   MOD_RES      24     24       Phosphoserine.
FT   MOD_RES     147    147       Phosphotyrosine.
FT   MOD_RES     253    253       Phosphothreonine (By similarity).
FT   MOD_RES     261    261       Phosphoserine.
SQ   SEQUENCE   289 AA;  33445 MW;  F4BF1AFCBE26EEFB CRC64;
     MRITGKTFRR RRADSESEED EQESEEVRLK LEETGEVQNL RKRPNGVSAA ALLVGEKVQE
     ETTLVDDPFQ MATGGMVDMK KLKERGKDKV SEEEDLHLGT SFSAETNRRD EDADMMKYIE
     TELKKRKGIV EQEEQKAKPK NAEDCLYELP ENIRVSSAKK TEEMLSNQML SGIPEVDLGI
     DAKIKNIIST EDAKARLLAE QQNKKKDSET SFVPTNMAVN YVQHNRFYHE ELNAPIRRNK
     EEPKARPLRV GDTEKPEPER SPPNRKRPAN EKATDDYHYE KFKKMNRRY
//
ID   Q3TQL4_MOUSE            Unreviewed;       679 AA.
AC   Q3TQL4;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 33.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Immt;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK163491; BAE37368.1; -; mRNA.
DR   IPI; IPI00381413; -.
DR   UniGene; Mm.235123; -.
DR   STRING; Q3TQL4; -.
DR   Ensembl; ENSMUST00000064062; ENSMUSP00000066181; ENSMUSG00000052337.
DR   Ensembl; ENSMUST00000114156; ENSMUSP00000109793; ENSMUSG00000052337.
DR   MGI; MGI:1923864; Immt.
DR   HOVERGEN; HBG039233; -.
DR   InParanoid; Q3TQL4; -.
DR   ArrayExpress; Q3TQL4; -.
DR   Bgee; Q3TQL4; -.
DR   Genevestigator; Q3TQL4; -.
DR   GO; GO:0031305; C:integral to mitochondrial inner membrane; IEA:InterPro.
DR   InterPro; IPR019133; Mt-IM_prot_Mitofilin.
DR   Pfam; PF09731; Mitofilin; 1.
PE   2: Evidence at transcript level;
FT   NON_TER     679    679
SQ   SEQUENCE   679 AA;  75473 MW;  0B624AA1196D1847 CRC64;
     MLRACQLSGV TVAAQSCLCG KFILRPLRPC RRYSTSSSSG LTAGKIAGAG LLFVGGGIGG
     TILYAKWDSH FRESVEKTIP YSDKLFGMVL GSAPYTVPLP KKPVQSGPLK ISSVSEVMKD
     SKLPVAQSQK TKGDTPASAA GDTLSVPAPA VQHEDTIKTE CPNTNEGKST SETTEEAFSS
     SVRERPPEEV AARLAQQEKQ EQVEMESLAK SLEDALNRTS SVTLQTITAQ NAAVQAVKAH
     SNILKTAMDN SEIAGEKKSA QWRTVEGALK ERRKAVDEAA DALLKAKEEL EKMKTIIEDA
     KKREIAGATP HITAAEGRLH NMIVDLDNVV KKVQAAQSEA KVVSQYHELV VQARDDFRKE
     LDSITPDITP GWKGMSISDL AGKLSTDDLN SLIAHAHRRI DQLNRELAQQ KATEKQHIEL
     ALEKHKLEEK RTFDSAVAKA LEHHRSEIQA EQDRKVEEVR DAMENEMRTQ LRRQAAAHTD
     HLRDVLKVQE QELKYEFEQG LSEKLSEQEL EFRRRSQEQM DSFTLDINTA YARLRGIEQA
     VQSHAVAEEE ARKAHQLWLS VEALKYSMKT SSAEMPTIPL GSAVEAIRVN CSDNEFTQAL
     TAAIPPESLT RGVYSEETLR ARFYAVQKLA RRVAMIDETR NSLYQYFLSY LQSLLLFPPK
     QLKPPAELYP EDINTFKLL
//
ID   Q3TQP6_MOUSE            Unreviewed;       552 AA.
AC   Q3TQP6;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Malic enzyme;
GN   Name=Me1; Synonyms=Mod1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
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DR   EMBL; AK163403; BAE37336.1; -; mRNA.
DR   IPI; IPI00881197; -.
DR   RefSeq; NP_001185862.1; NM_001198933.1.
DR   UniGene; Mm.148155; -.
DR   UniGene; Mm.378128; -.
DR   ProteinModelPortal; Q3TQP6; -.
DR   SMR; Q3TQP6; 6-535.
DR   STRING; Q3TQP6; -.
DR   Ensembl; ENSMUST00000034989; ENSMUSP00000034989; ENSMUSG00000032418.
DR   GeneID; 17436; -.
DR   UCSC; uc009qxr.1; mouse.
DR   MGI; MGI:97043; Me1.
DR   HOVERGEN; HBG000746; -.
DR   InParanoid; Q3TQP6; -.
DR   ArrayExpress; Q3TQP6; -.
DR   Bgee; Q3TQP6; -.
DR   Genevestigator; Q3TQP6; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005625; C:soluble fraction; IDA:MGI.
DR   GO; GO:0004473; F:malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) activity; IMP:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:InterPro.
DR   GO; GO:0051262; P:protein tetramerization; IDA:MGI.
DR   InterPro; IPR015884; Malic_enzyme_CS.
DR   InterPro; IPR012301; Malic_N.
DR   InterPro; IPR012302; Malic_NAD-bd.
DR   InterPro; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.10380; G3DSA:3.40.50.10380; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PIRSF; PIRSF000106; ME; 1.
DR   PRINTS; PR00072; MALOXRDTASE.
DR   SMART; SM00919; Malic_M; 1.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Oxidoreductase.
SQ   SEQUENCE   552 AA;  61481 MW;  5F8E86740072DC03 CRC64;
     MRLICEDLAF TLEERQQLNI HGLLPPCIIS QELQVLRIIK NFERLNSDFD RYLLLMDLQD
     RNEKLFYSVL MSDVEKFMPI VYTPTVGLAC QQYSLAFRKP RGLFISIHDK GHIASVLNAW
     PEDVVKAIVV TDGERILGLG DLGCNGMGIP VGKLALYTAC GGVNPQQCLP ITLDVGTENE
     ELLKDPLYIG LRHRRVRGPE YDAFLDEFME AASSKYGMNC LIQFEDFANR NAFRLLNKYR
     NKYCTFNDDI QGTASVAVAG LLAALRITKN KLSDQTVLFQ GAGEAALGIA HLVVMAMEKE
     GLSKENARKK IWLVDSKGLI VKGRASLTEE KEVFAHEHEE MKNLEAIVQK IKPTALIGVA
     AIGGAFTEQI LKDMAAFNER PIIFALSNPT SKAECSAEQC YKVTKGRAIF ASGSPFDPVT
     LPDGRTLFPG QGNNSYVFPG VALGVVACGL RHIDDKVFLT TAEVISQQVS DKHLQEGRLY
     PPLNTIRGVS LKIAVKIVQD AYKEKMATVY PEPQNKEEFV SSQMYSTNYD QILPDCYPWP
     AEVQKIQTKV NQ
//
ID   Q3TQS1_MOUSE            Unreviewed;       288 AA.
AC   Q3TQS1;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 36.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Larp1b; Synonyms=Larp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK163348; BAE37311.1; -; mRNA.
DR   IPI; IPI00654411; -.
DR   UniGene; Mm.435458; -.
DR   UniGene; Mm.46782; -.
DR   ProteinModelPortal; Q3TQS1; -.
DR   SMR; Q3TQS1; 163-254.
DR   PRIDE; Q3TQS1; -.
DR   Ensembl; ENSMUST00000099122; ENSMUSP00000096723; ENSMUSG00000037814.
DR   UCSC; uc008pcb.1; mouse.
DR   MGI; MGI:1914604; Larp1b.
DR   eggNOG; roNOG08002; -.
DR   GeneTree; ENSGT00390000000523; -.
DR   HOVERGEN; HBG060357; -.
DR   OrthoDB; EOG4C87T6; -.
DR   ArrayExpress; Q3TQS1; -.
DR   Bgee; Q3TQS1; -.
DR   Genevestigator; Q3TQS1; -.
DR   InterPro; IPR006630; Lupus_La_RNA-bd.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF05383; La; 1.
DR   SMART; SM00715; LA; 1.
DR   PROSITE; PS50961; HTH_LA; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   288 AA;  33320 MW;  9199685E364FDD66 CRC64;
     MANWPTPGEL VNTGSQSVIN QGNKKPQIRK EKEEKIEKRS NSESKENREA KLDGPTENIS
     EDEAQSSSQR KRGWRREREK RDDQDEVSSV RSEGGTIRGS TRGRGRGRGR GRGRGRGNPR
     LNFDYSYGYR EPGERTEQPF STELNTSMMY YYDDGTGVRV YPVEETLLKE YIKRQIEYYF
     STENLERDFF LRRKMDEQGF LPISLIAGFH RVQALTTNLN LILEALKDST EVEIVDEKMR
     KKIEPEKWPI PGPPPRNVPQ TDFSQLIDCP EFIPGQAFGS HTVRVMIY
//
ID   FNDC4_MOUSE             Reviewed;         231 AA.
AC   Q3TR08; Q810E5; Q9CYY4;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 47.
DE   RecName: Full=Fibronectin type III domain-containing protein 4;
DE   AltName: Full=Fibronectin type III repeat-containing protein 1;
DE   Flags: Precursor;
GN   Name=Fndc4; Synonyms=Fnmp1, Frcp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=129;
RX   PubMed=12384288; DOI=10.1016/S0378-1119(02)00828-4;
RA   Teufel A., Malik N., Mukhopadhyay M., Westphal H.;
RT   "Frcp1 and Frcp2, two novel fibronectin type III repeat containing
RT   genes.";
RL   Gene 297:79-83(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- TISSUE SPECIFICITY: Strongly expressed in liver.
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO85424.1; Type=Erroneous initiation;
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DR   EMBL; AF466728; AAO85424.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AK013203; BAB28710.2; -; mRNA.
DR   EMBL; AK163183; BAE37223.1; -; mRNA.
DR   IPI; IPI00319028; -.
DR   RefSeq; NP_071869.2; NM_022424.5.
DR   UniGene; Mm.292544; -.
DR   ProteinModelPortal; Q3TR08; -.
DR   SMR; Q3TR08; 5-137.
DR   STRING; Q3TR08; -.
DR   PRIDE; Q3TR08; -.
DR   Ensembl; ENSMUST00000041266; ENSMUSP00000047185; ENSMUSG00000038552.
DR   GeneID; 64339; -.
DR   KEGG; mmu:64339; -.
DR   NMPDR; fig|10090.3.peg.11403; -.
DR   UCSC; uc008wyd.1; mouse.
DR   CTD; 64339; -.
DR   MGI; MGI:1917195; Fndc4.
DR   eggNOG; roNOG16276; -.
DR   GeneTree; ENSGT00390000004923; -.
DR   HOGENOM; HBG715358; -.
DR   HOVERGEN; HBG067308; -.
DR   InParanoid; Q3TR08; -.
DR   OMA; TMASLMP; -.
DR   OrthoDB; EOG41RPW1; -.
DR   PhylomeDB; Q3TR08; -.
DR   NextBio; 320035; -.
DR   ArrayExpress; Q3TR08; -.
DR   Bgee; Q3TR08; -.
DR   CleanEx; MM_FNDC4; -.
DR   Genevestigator; Q3TR08; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF00041; fn3; 1.
DR   SMART; SM00060; FN3; 1.
DR   SUPFAM; SSF49265; FN_III-like; 1.
DR   PROSITE; PS50853; FN3; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     40       Potential.
FT   CHAIN        41    231       Fibronectin type III domain-containing
FT                                protein 4.
FT                                /FTId=PRO_0000271380.
FT   TOPO_DOM     41    163       Extracellular (Potential).
FT   TRANSMEM    164    184       Helical; (Potential).
FT   TOPO_DOM    185    231       Cytoplasmic (Potential).
FT   DOMAIN       43    132       Fibronectin type-III.
FT   CARBOHYD     48     48       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    143    143       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    126    126       G -> A (in Ref. 1; BAB28710).
SQ   SEQUENCE   231 AA;  24933 MW;  ABCC097E5251F14A CRC64;
     MPLAPPANSV ETMASLMPLS PYLSPTVLLL VSCDLGFVRA DRPPSPVNVT VTHLRANSAT
     VSWDVPEGNI VIGYSISQQR QNGPGQRVIR EVNTTTRACA LWGLAEDSDY TVQVRSIGLR
     GESPPGPRVH FRTLKGSDRL PSNSSSPGDI TVEGLDGERP LQTGEVVIIV VVLLMWAAVI
     GLFCRQYDII KDNDSNNNPK EKGKGPEQSP QGRPVGTTRQ KKSPSINTID V
//
ID   Q3TR26_MOUSE            Unreviewed;       453 AA.
AC   Q3TR26;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 33.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Heg1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK163128; BAE37205.1; -; mRNA.
DR   IPI; IPI00229031; -.
DR   UniGene; Mm.245741; -.
DR   UniGene; Mm.37138; -.
DR   eggNOG; maNOG23013; -.
DR   HOVERGEN; HBG070920; -.
DR   InParanoid; Q3TR26; -.
DR   ArrayExpress; Q3TR26; -.
DR   Genevestigator; Q3TR26; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   453 AA;  47429 MW;  83F47511D1D033E9 CRC64;
     MATPRAPRWP PPSLLLLLLL PLLLLPPAAP GARGSLPSPA HRTLLPVAGP LSPPGAGHTA
     PGPGVATRRG RSGRVPRGVS AALESLPESP SSSRSQRRIT PSQTESGTSL GFLERTRELP
     EEGTVHTQVA GTWVSRQASH PALEPGEPTV LSQKRNSSGQ EHSGPPFSWS QSHPPPSDHP
     SSSGSIKNGN NFTALQNPSV TQTKSMLITD TYTNGVPRTL RSLPVGXDPA DETEGFPEHS
     RLGITSMSVR SSPSVKDSRT NSGLTEHLGD GEGTELSTEN GYGLPSIHWQ SDAPSFGGRQ
     LASSSEAGDG RAMPLTEAVF RSDPSIGGGE STGRWILTKK KTSTDAAESS ALHPEAGGAG
     GLTQSSHAAQ QPRGGGEDSG MGGRSYAESS SSSSSTSSSE SLDSSAPLRE HSREFLVHGN
     RHRVLGCVWS FDLPKHTLGK EFHYSQAIIL LAD
//
ID   Q3TR92_MOUSE            Unreviewed;       479 AA.
AC   Q3TR92;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 49.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Kcnc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK162964; BAE37138.1; -; mRNA.
DR   IPI; IPI00653535; -.
DR   RefSeq; NP_001106210.1; NM_001112739.1.
DR   UniGene; Mm.249386; -.
DR   ProteinModelPortal; Q3TR92; -.
DR   STRING; Q3TR92; -.
DR   Ensembl; ENSMUST00000098442; ENSMUSP00000096041; ENSMUSG00000058975.
DR   Ensembl; ENSMUST00000160433; ENSMUSP00000124938; ENSMUSG00000058975.
DR   GeneID; 16502; -.
DR   KEGG; mmu:16502; -.
DR   CTD; 16502; -.
DR   MGI; MGI:96667; Kcnc1.
DR   GeneTree; ENSGT00580000081499; -.
DR   HOVERGEN; HBG105862; -.
DR   ArrayExpress; Q3TR92; -.
DR   Bgee; Q3TR92; -.
DR   Genevestigator; Q3TR92; -.
DR   GO; GO:0030673; C:axolemma; IDA:MGI.
DR   GO; GO:0032590; C:dendrite membrane; IDA:MGI.
DR   GO; GO:0032809; C:neuronal cell body membrane; IDA:MGI.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003974; K_chnl_volt-dep_Kv3.
DR   InterPro; IPR005403; K_chnl_volt-dep_Kv3.1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01581; KV31CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01498; SHAWCHANNEL.
PE   2: Evidence at transcript level;
KW   Ion transport; Ionic channel; Membrane; Potassium; Potassium channel;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport.
SQ   SEQUENCE   479 AA;  53660 MW;  AF1CC332775B60AC CRC64;
     MTYRQHRDAE EALDSFGGAP LDNSADDADA DGPGDSGDGE DELEMTKRLA LSDSPDGRPG
     GFWRRWQPRI WALFEDPYSS RYARYVAFAS LFFILVSITT FCLETHERFN PIVNKTEIEN
     VRNGTQVRYY REAETEAFLT YIEGVCVVWF TFEFLMRVVF CPNKVEFIKN SLNIIDFVAI
     LPFYLEVGLS GLSSKAAKDV LGFLRVVRFV RILRIFKLTR HFVGLRVLGH TLRASTNEFL
     LLIIFLALGV LIFATMIYYA ERIGAQPNDP SASEHTHFKN IPIGFWWAVV TMTTLGYGDM
     YPQTWSGMLV GALCALAGVL TIAMPVPVIV NNFGMYYSLA MAKQKLPKKK KKHIPRPPQL
     GSPNYCKSVV NSPHHSTQSD TCPLAQEEIL EINRADSKLN GEVAKAALAN EDCPHIDQAL
     TPDEGLPFTR SGTRERYGPC FLLSTGEYAC PPGGGMRKDL CKESPVIAKY MPTEAVRVT
//
ID   PLPL6_MOUSE             Reviewed;        1355 AA.
AC   Q3TRM4; Q7TQD6; Q9R114;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Neuropathy target esterase;
DE            EC=3.1.1.5;
DE   AltName: Full=Patatin-like phospholipase domain-containing protein 6;
GN   Name=Pnpla6; Synonyms=Nte;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=BALB/c;
RX   PubMed=10640712; DOI=10.1016/S0925-4773(99)00239-7;
RA   Moser M., Stempfl T., Li Y., Glynn P., Buttner R., Kretzschmar D.;
RT   "Cloning and expression of the murine sws/NTE gene.";
RL   Mech. Dev. 90:279-282(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=C57BL/6J; TISSUE=Bone;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION.
RX   PubMed=12640454; DOI=10.1038/ng1131;
RA   Winrow C.J., Hemming M.L., Allen D.M., Quistad G.B., Casida J.E.,
RA   Barlow C.;
RT   "Loss of neuropathy target esterase in mice links organophosphate
RT   exposure to hyperactivity.";
RL   Nat. Genet. 33:477-485(2003).
RN   [6]
RP   FUNCTION, ENZYME REGULATION, AND SUBCELLULAR LOCATION.
RX   PubMed=16963094; DOI=10.1016/j.taap.2006.08.002;
RA   Read D.J., Langford L., Barbour H.R., Forshaw P.J., Glynn P.;
RT   "Phospholipase B activity and organophosphorus compound toxicity in
RT   cultured neural cells.";
RL   Toxicol. Appl. Pharmacol. 219:190-195(2007).
CC   -!- FUNCTION: Phospholipase B that deacylates intracellular
CC       phosphatidylcholine (PtdCho), generating glycerophosphocholine
CC       (GroPtdCho). This deacylation occurs at both sn-2 and sn-1
CC       positions of PtdCho. Its specific chemical modification by certain
CC       organophosphorus (OP) compounds leads to distal axonopathy.
CC   -!- CATALYTIC ACTIVITY: 2-lysophosphatidylcholine + H(2)O =
CC       glycerophosphocholine + a carboxylate.
CC   -!- ENZYME REGULATION: Inhibited by a series a OPs such as mipafox
CC       (MPX), phenyl saligenin phosphate (PSP), phenyl dipentyl
CC       phosphinate (PDPP), diisopropyl fluorophosphate and paraoxon.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       type I membrane protein; Cytoplasmic side. Note=Anchored to the
CC       cytoplasmic face of the endoplasmic reticulum by its amino-
CC       terminal transmembrane segment.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q3TRM4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3TRM4-2; Sequence=VSP_026390;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q3TRM4-3; Sequence=VSP_026390, VSP_026391;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q3TRM4-4; Sequence=VSP_026392, VSP_026393;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed ubiquitously in brain of young mice.
CC       Reaching adulthood, there is a most prominent expression in
CC       Purkinje cells, granule cells and pyramidal neurons of the
CC       hippocampus and some large neurons in the medulla oblongata,
CC       nucleus dentatus and pons.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the embryonic respiratory
CC       system, different epithelial structures and strongly in the spinal
CC       ganglia, during the development.
CC   -!- PTM: Glycosylated (By similarity).
CC   -!- SIMILARITY: Belongs to the NTE family.
CC   -!- SIMILARITY: Contains 3 cyclic nucleotide-binding domains.
CC   -!- SIMILARITY: Contains 1 patatin domain.
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DR   EMBL; AF173829; AAD51700.1; -; mRNA.
DR   EMBL; AK162641; BAE37004.1; -; mRNA.
DR   EMBL; AC170806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC054789; AAH54789.1; -; mRNA.
DR   EMBL; BC056999; AAH56999.1; -; mRNA.
DR   IPI; IPI00128034; -.
DR   IPI; IPI00653809; -.
DR   IPI; IPI00849185; -.
DR   IPI; IPI00849302; -.
DR   RefSeq; NP_001116290.1; NM_001122818.1.
DR   RefSeq; NP_056616.2; NM_015801.2.
DR   UniGene; Mm.23085; -.
DR   ProteinModelPortal; Q3TRM4; -.
DR   SMR; Q3TRM4; 165-300, 505-599, 632-714.
DR   STRING; Q3TRM4; -.
DR   PhosphoSite; Q3TRM4; -.
DR   PRIDE; Q3TRM4; -.
DR   Ensembl; ENSMUST00000004681; ENSMUSP00000004681; ENSMUSG00000004565.
DR   Ensembl; ENSMUST00000111070; ENSMUSP00000106699; ENSMUSG00000004565.
DR   GeneID; 50767; -.
DR   KEGG; mmu:50767; -.
DR   UCSC; uc009krt.1; mouse.
DR   CTD; 50767; -.
DR   MGI; MGI:1354723; Pnpla6.
DR   eggNOG; roNOG13327; -.
DR   GeneTree; ENSGT00390000002533; -.
DR   HOGENOM; HBG382026; -.
DR   HOVERGEN; HBG053067; -.
DR   InParanoid; Q3TRM4; -.
DR   OMA; GDPVKPT; -.
DR   OrthoDB; EOG4P5K8B; -.
DR   BRENDA; 3.1.1.5; 244.
DR   NextBio; 307675; -.
DR   ArrayExpress; Q3TRM4; -.
DR   Bgee; Q3TRM4; -.
DR   CleanEx; MM_PNPLA6; -.
DR   Genevestigator; Q3TRM4; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:EC.
DR   GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009887; P:organ morphogenesis; IMP:MGI.
DR   GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPlipase.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR001423; Lysophospholipase_patatin_CS.
DR   InterPro; IPR002641; Patatin/PhospholipaseA2-rel.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 3.
DR   Pfam; PF00027; cNMP_binding; 3.
DR   Pfam; PF01734; Patatin; 1.
DR   SMART; SM00100; cNMP; 3.
DR   SUPFAM; SSF52151; Acyl_Trfase/lysoPlipase; 1.
DR   SUPFAM; SSF51206; cNMP_binding; 3.
DR   PROSITE; PS00888; CNMP_BINDING_1; FALSE_NEG.
DR   PROSITE; PS00889; CNMP_BINDING_2; FALSE_NEG.
DR   PROSITE; PS50042; CNMP_BINDING_3; 3.
DR   PROSITE; PS01237; UPF0028; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Endoplasmic reticulum; Glycoprotein; Hydrolase;
KW   Lipid degradation; Membrane; Phosphoprotein; Repeat; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   1355       Neuropathy target esterase.
FT                                /FTId=PRO_0000292200.
FT   TOPO_DOM      1     43       Lumenal (Potential).
FT   TRANSMEM     44     64       Helical; (Potential).
FT   TOPO_DOM     65   1355       Cytoplasmic (Potential).
FT   DOMAIN      961   1127       Patatin.
FT   NP_BIND     179    306       cNMP 1.
FT   NP_BIND     492    614       cNMP 2.
FT   NP_BIND     610    730       cNMP 3.
FT   MOTIF       992    996       GXSXG.
FT   ACT_SITE    994    994       By similarity.
FT   MOD_RES     338    338       Phosphoserine (By similarity).
FT   MOD_RES     345    345       Phosphothreonine (By similarity).
FT   MOD_RES     346    346       Phosphoserine (By similarity).
FT   MOD_RES     356    356       Phosphoserine (By similarity).
FT   MOD_RES     405    405       Phosphoserine (By similarity).
FT   CARBOHYD      9      9       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1     41       MGTPSHELNTTSSGAEVIQKTLEEGLGRRICVAQPVPFVPQ
FT                                -> MEAPLQTGM (in isoform 2 and isoform
FT                                3).
FT                                /FTId=VSP_026390.
FT   VAR_SEQ     448    448       R -> RTPTQ (in isoform 3).
FT                                /FTId=VSP_026391.
FT   VAR_SEQ    1123   1169       ADIARSMGAKTVIAIDVGSQDETDLSTYGDSLSGWWLLWKR
FT                                LNPWAD -> GKWLPTHICMDTYHQTHAHTDFCTCRLEGTG
FT                                LYEWRSSRGHTQLCTEL (in isoform 4).
FT                                /FTId=VSP_026392.
FT   VAR_SEQ    1170   1355       Missing (in isoform 4).
FT                                /FTId=VSP_026393.
FT   CONFLICT    240    240       E -> K (in Ref. 1; AAD51700).
SQ   SEQUENCE   1355 AA;  149537 MW;  813263C6A82083ED CRC64;
     MGTPSHELNT TSSGAEVIQK TLEEGLGRRI CVAQPVPFVP QVLGVMIGAG VAVLVTAVLI
     LLVVRRLRVQ KTPAPEGPRY RFRKRDKVLF YGRKIMRKVS QSTSSLVDTS VSTTSRPRMK
     KKLKMLNIAK KILRIQKETP TLQRKEPPPS VLEADLTEGD LANSHLPSEV LYMLKNVRVL
     GHFEKPLFLE LCRHMVFQRL GQGDYVFRPG QPDASIYVVQ DGLLELCLPG PDGKECVVKE
     VVPGDSVNSL LSILDVITGH QHPQRTVSAR AARDSTVLRL PVEAFSAVFT KYPESLVRVV
     QIIMVRLQRV TFLALHNYLG LTNELFSHEI QPLRLFPSPG LPTRTSPVRG SKRVVSTSGT
     EDTSKETSGR PLDSIGAPLP GPAGDPVKPT SLEAPPAPLL SRCISMPVDI SGLQGGPRSD
     FDMAYERGRI SVSLQEEASG GPQTASPREL REQPAGACEY SYCEDESATG GCPFGPYQGR
     QTSSIFEAAK RELAKLMRIE DPSLLNSRVL LHHAKAGTII ARQGDQDVSL HFVLWGCLHV
     YQRMIDKAEE VCLFVAQPGE LVGQLAVLTG EPLIFTLRAQ RDCTFLRISK SHFYEIMRAQ
     PSVVLSAAHT VAARMSPFVR QMDFAIDWTA VEAGRALYRQ GDRSDCTYIV LNGRLRSVIQ
     RGSGKKELVG EYGRGDLIGV VEALTRQPRA TTVHAVRDTE LAKLPEGTLG HIKRRYPQVV
     TRLIHLLSQK ILGNLQQLQG PFPGSGLSVP QHSELTNPAS NLSTVAILPV CAEVPMMAFT
     LELQHALQAI GPTLLLNSDV IRALLGASAL DSIQEFRLSG WLAQQEDAHR IVLYQTDTSL
     TPWTVRCLRQ ADCILIVGLG DQEPTVGQLE QMLENTAVRA LKQLVLLHRE EGPGPTRTVE
     WLNMRSWCSG HLHLRCPRRL FSRRSPAKLH ELYEKVFSRR ADRHSDFSRL ARVLTGNTIA
     LVLGGGGARG CSHIGVLKAL EEAGVPVDLV GGTSIGSFIG ALYAEERSAS RTKQRAREWA
     KSMTSVLEPV LDLTYPVTSM FTGSAFNRSI HRVFQDKQIE DLWLPYFNVT TDITASAMRV
     HKDGSLWRYV RASMTLSGYL PPLCDPKDGH LLMDGGYINN LPADIARSMG AKTVIAIDVG
     SQDETDLSTY GDSLSGWWLL WKRLNPWADK VKVPDMAEIQ SRLAYVSCVR QLEVVKSSSY
     CEYLRPSIDC FKTMDFGKFD QIYDVGYQYG KAVFGGWTRG EVIEKMLTDR RSTDLNESRR
     ADILAFPSSG FTDLAEIVSR IEPPTSYVSD GCADGEESDC LTEYEEDAGP DCSRDEGGSP
     EGASPSTASE VEEEKSTLRQ RRFLPQETPS SVADA
//
ID   HXK3_MOUSE              Reviewed;         922 AA.
AC   Q3TRM8; Q3TAX6; Q3UDP1; Q3UEA4;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Hexokinase-3;
DE            EC=2.7.1.1;
DE   AltName: Full=Hexokinase type III;
DE            Short=HK III;
GN   Name=Hk3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone, and Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-732, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- CATALYTIC ACTIVITY: ATP + D-hexose = ADP + D-hexose 6-phosphate.
CC   -!- ENZYME REGULATION: Hexokinase is an allosteric enzyme inhibited by
CC       its product Glc-6-P (By similarity).
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- DOMAIN: The N- and C-terminal halves of this hexokinase show
CC       extensive sequence similarity to each other. The catalytic
CC       activity is associated with the C-terminus while regulatory
CC       function is associated with the N-terminus.
CC   -!- MISCELLANEOUS: In vertebrates there are four major glucose-
CC       phosphorylating isoenzymes, designated hexokinase I, II, III and
CC       IV (glucokinase).
CC   -!- SIMILARITY: Belongs to the hexokinase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK149651; BAE29007.1; -; mRNA.
DR   EMBL; AK149992; BAE29220.1; -; mRNA.
DR   EMBL; AK154603; BAE32706.1; -; mRNA.
DR   EMBL; AK162637; BAE37000.1; -; mRNA.
DR   EMBL; AK171580; BAE42538.1; -; mRNA.
DR   IPI; IPI00751595; -.
DR   RefSeq; NP_001028417.1; NM_001033245.3.
DR   UniGene; Mm.267479; -.
DR   ProteinModelPortal; Q3TRM8; -.
DR   SMR; Q3TRM8; 2-918.
DR   STRING; Q3TRM8; -.
DR   PhosphoSite; Q3TRM8; -.
DR   PRIDE; Q3TRM8; -.
DR   Ensembl; ENSMUST00000052949; ENSMUSP00000051215; ENSMUSG00000025877.
DR   GeneID; 212032; -.
DR   KEGG; mmu:212032; -.
DR   UCSC; uc007qpr.1; mouse.
DR   CTD; 212032; -.
DR   MGI; MGI:2670962; Hk3.
DR   HOGENOM; HBG446386; -.
DR   HOVERGEN; HBG005020; -.
DR   InParanoid; Q3TRM8; -.
DR   OMA; TLISWTK; -.
DR   OrthoDB; EOG4R23T4; -.
DR   PhylomeDB; Q3TRM8; -.
DR   BRENDA; 2.7.1.1; 244.
DR   NextBio; 373427; -.
DR   ArrayExpress; Q3TRM8; -.
DR   Bgee; Q3TRM8; -.
DR   CleanEx; MM_HK3; -.
DR   Genevestigator; Q3TRM8; -.
DR   GermOnline; ENSMUSG00000025877; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004396; F:hexokinase activity; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR001312; Hexokinase.
DR   InterPro; IPR022673; Hexokinase_C.
DR   InterPro; IPR019807; Hexokinase_CS.
DR   InterPro; IPR022672; Hexokinase_N.
DR   PANTHER; PTHR19443; Hexokinase; 1.
DR   Pfam; PF00349; Hexokinase_1; 2.
DR   Pfam; PF03727; Hexokinase_2; 2.
DR   PRINTS; PR00475; HEXOKINASE.
DR   PROSITE; PS00378; HEXOKINASES; 2.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; ATP-binding; Glycolysis; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Repeat; Transferase.
FT   CHAIN         1    922       Hexokinase-3.
FT                                /FTId=PRO_0000197591.
FT   NP_BIND      93     98       ATP (Potential).
FT   NP_BIND     540    545       ATP (Potential).
FT   REGION        1    486       Regulatory.
FT   REGION      160    186       Glucose-binding (Potential).
FT   REGION      487    922       Catalytic.
FT   REGION      602    628       Glucose-binding (Potential).
FT   MOD_RES     732    732       Phosphothreonine.
FT   CONFLICT    203    203       A -> S (in Ref. 1; BAE37000).
FT   CONFLICT    384    384       Y -> C (in Ref. 1; BAE29220).
FT   CONFLICT    439    439       K -> E (in Ref. 1; BAE29220).
FT   CONFLICT    442    442       V -> I (in Ref. 1; BAE29007).
FT   CONFLICT    509    509       G -> E (in Ref. 1; BAE29007).
FT   CONFLICT    860    860       T -> A (in Ref. 1; BAE29007).
SQ   SEQUENCE   922 AA;  100101 MW;  38F4E024630C45E5 CRC64;
     MATIGPSGLH PGERASVCPH EGVPRPSGSL ELECLQQFKV TRTQLQQIQA SLLCSMEQAL
     KGQDSPAPSV RMLPTYVRST PHGTEQGDFL VLELGATGAS LRVLWVTLTG TKECRVEPRS
     REFVIPQEVI LGAGQQLFDF AARCLSEFLD AYPVENQGLK LGFNFSFPCH QTGLDRSTLI
     SWTKGFRCSG VEGQDVVQLL RDAIQRQGTY RIDVVAMVND TVGTMMGCEL GTRPCEVGLI
     VDTGTNACYM EEARHVAALD EDRGRTCVSI EWGSFYDEDA LGPVLTTFDS ALDRESLTPG
     AQRFEKMIGG LYLGELVRLV LVHLTQHGVL FDGCASPALL SQGCILLDHV AEMEDTATGT
     ARVHTILQDL GLSPRASDAE LVQYVCVAVC TRAAQLCAAA LAAVLSRLQH SREQQTLQVA
     VATGGRVFER HPRFLRILKE TVTLLAPNCD VSFIPSVDGG GRGVAMVTAV AARLAAHRRI
     LEETLAPFQL TLEQMTVVQA QMREAMIRGL QGEASSLRML PTYVRATPDG SERGDFLALD
     LGGTNFRVLL VRVAEGSVQI INQVYSIPEC RAQGSGQKLF DHIVDCIVDF QKRQGLSGQS
     LPLGFTFSFP CKQLGLDQGI LLNWTKGFNA SGCEGQDVVY LLREAIRRRQ AVELNVVAIV
     NDTVGTMMSC GYDDPRCEMG LIVGTGTNAC YMEELRNVAS VPGDSGLMCI NMEWGAFGDD
     GSLGTLSTRF DTSVDQASIN PGKQRFEKMI SGMYLGEIVR HILLHLTNLG VLFRGQKTQC
     LQARDIFKTK FLSEIESDSL ALRQVRAILE DLGLTLTSDD ALMVLEVCQA VSRRAAQLCG
     AGVAAVVEKI RENRGLQELT VSVGVDGTLY KLHPHFSKLV SATVRKLAPQ CTVTFLQSED
     GSGKGAALVT AVACRLTQMA HV
//
ID   MAP9_MOUSE              Reviewed;         646 AA.
AC   Q3TRR0; Q3UUD1; Q3UX85; Q3UXE7; Q5M8N8; Q6P8K1; Q8BMM4; Q8BYP7;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Microtubule-associated protein 9;
DE   AltName: Full=Aster-associated protein;
GN   Name=Map9; Synonyms=Asap, Mtap9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-493 (ISOFORM 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Egg, Hypothalamus, Pituitary, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-495.
RC   TISSUE=Pituitary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Involved in organization of the bipolar mitotic spindle.
CC       Required for bipolar spindle assembly, mitosis progression and
CC       cytokinesis. May act by stabilizing interphase microtubules (By
CC       similarity).
CC   -!- SUBUNIT: Binds to purified microtubules via its C-terminus (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton (By
CC       similarity). Cytoplasm, cytoskeleton, spindle (By similarity).
CC       Note=Localizes to microtubules in interphase, associates with the
CC       mitotic spindle during mitosis, localizes to the central body
CC       during cytokinesis (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3TRR0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3TRR0-2; Sequence=VSP_020039;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH61216.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAH87935.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AK147287; Type=Frameshift; Positions=84;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK030527; BAC27004.2; -; mRNA.
DR   EMBL; AK038737; BAC30117.1; -; mRNA.
DR   EMBL; AK135702; BAE22616.1; -; mRNA.
DR   EMBL; AK135823; BAE22678.1; -; mRNA.
DR   EMBL; AK138540; BAE23696.1; -; mRNA.
DR   EMBL; AK147287; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK162555; BAE36967.1; -; mRNA.
DR   EMBL; BC061216; AAH61216.1; ALT_SEQ; mRNA.
DR   EMBL; BC087935; AAH87935.1; ALT_SEQ; mRNA.
DR   IPI; IPI00457932; -.
DR   IPI; IPI00625151; -.
DR   RefSeq; NP_001074699.1; NM_001081230.1.
DR   UniGene; Mm.271269; -.
DR   STRING; Q3TRR0; -.
DR   PhosphoSite; Q3TRR0; -.
DR   PRIDE; Q3TRR0; -.
DR   Ensembl; ENSMUST00000091014; ENSMUSP00000088535; ENSMUSG00000033900.
DR   Ensembl; ENSMUST00000107727; ENSMUSP00000103355; ENSMUSG00000033900.
DR   GeneID; 213582; -.
DR   KEGG; mmu:213582; -.
DR   UCSC; uc008pow.1; mouse.
DR   CTD; 213582; -.
DR   MGI; MGI:2442208; Mtap9.
DR   eggNOG; roNOG12006; -.
DR   GeneTree; ENSGT00530000063789; -.
DR   HOVERGEN; HBG081953; -.
DR   InParanoid; Q3TRR0; -.
DR   OMA; RAEKKDK; -.
DR   OrthoDB; EOG42NJ09; -.
DR   NextBio; 374058; -.
DR   ArrayExpress; Q3TRR0; -.
DR   Bgee; Q3TRR0; -.
DR   CleanEx; MM_MTAP9; -.
DR   Genevestigator; Q3TRR0; -.
DR   GermOnline; ENSMUSG00000033900; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell cycle; Cell division; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Microtubule; Mitosis; Phosphoprotein.
FT   CHAIN         1    646       Microtubule-associated protein 9.
FT                                /FTId=PRO_0000247754.
FT   COILED      442    596       Potential.
FT   MOD_RES      12     12       Phosphotyrosine (By similarity).
FT   MOD_RES      15     15       Phosphoserine (By similarity).
FT   MOD_RES     132    132       Phosphoserine (By similarity).
FT   MOD_RES     257    257       Phosphoserine (By similarity).
FT   VAR_SEQ     429    458       Missing (in isoform 2).
FT                                /FTId=VSP_020039.
FT   CONFLICT    185    185       K -> P (in Ref. 1; BAE36967).
FT   CONFLICT    205    205       S -> H (in Ref. 1; BAE36967).
SQ   SEQUENCE   646 AA;  73511 MW;  F5309EDE68557839 CRC64;
     MSDEIFSTTL AYTKSPKATK RTSFQDELIR AITARSARQR SSEYSDDFDS DEIVSLGEFS
     DTSTDESLVR KKMNDFHISD DEEKNSPRLS FLKTKKVNRA ISNDALDSST PGSEGSSPDA
     QEDVTGDSLP KSQNDDREVG REIITVKPTP RMHPVKRSTS SGETSSGLDA DGHFKPSPQP
     RSMLKKSSHT EEGVRPGVDK EHSISEASAP TPSLPRQNGT ELQTEEKIYS ENLDLEDSLL
     QSLTSSSFKE SPGGCTSPGS QEKVPIKDHD GEPTEIWDSL LSNENEGSSV LVNCVTPELE
     QPKDGQVAAD DLEEEREKGG FTEDDLTTDP LLSTSPSVIT PTEPAEPAKK ANEDRNTKNK
     KTTNNRVSSA SGRLMTSEFL KRSGPTKRSP SAATSSHYLG SLKVLDQKQP RKQSLEPDKA
     DHIRAAVYQE WLEKKNVYLH EMHRIKRIES ENLRIQNEQK KAAKREEALA SFEAWKAMKE
     KEAKRIAAKK RLEEKNKKKT EEENAMRKGE ALQAFEKWKE KKLEYLKEKT RREKEYERAK
     KQKEEEAVAE KKKDSLTAFE KWSERKEALL KQKEKEKINE RRKEELKRAE KKDKDKQAIS
     EYEKWLEKKE RQERIERKQK KRHSFLESET HPPWSPPSRT APSKVF
//
ID   Q3TSN2_MOUSE            Unreviewed;       428 AA.
AC   Q3TSN2;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 31.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Synm; Synonyms=Dmn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK161935; BAE36643.1; -; mRNA.
DR   IPI; IPI00469184; -.
DR   UniGene; Mm.60526; -.
DR   STRING; Q3TSN2; -.
DR   Ensembl; ENSMUST00000074233; ENSMUSP00000073855; ENSMUSG00000030554.
DR   MGI; MGI:2661187; Synm.
DR   eggNOG; roNOG05821; -.
DR   InParanoid; Q3TSN2; -.
DR   ArrayExpress; Q3TSN2; -.
DR   Bgee; Q3TSN2; -.
DR   Genevestigator; Q3TSN2; -.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0060053; C:neurofilament cytoskeleton; IDA:MGI.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   428 AA;  46274 MW;  3ED4A5BA08D95686 CRC64;
     MWRTEQVTFG GPTAQVVEVS GDFSEAVSSE GASRSVRHIT LGPHQSQVST EVIFRGSVPT
     WQETGDTEKP GPVVLSVGAD ISGSGRMPGS ERSHTEKEIR FQGPVSGTAQ VGGNFATEES
     VGSQTFVRSL QLGPKEGFRE EIQFIAPIPD KVGWGEEDSE HTKVSLERAT SIQRIDIVPQ
     RYLASKQMAP QTLEFRDSED MVMVEGSAGT IQATHNFTSD REILQNKENT FQRVISGSPP
     DSVGDTGAEV TANVSRSFRH IQIGPTEEEP SEYFVTGRPV SKTFVLDGSV ASPGLVGGAD
     GGSTPCRIAL GPKETSFTFQ MDLSDTRAIR SWTRDTGSEV EAHGVSHRGG WRIAHSRDER
     VASTGSGASP GDAHQAPGEK GTEQAGFDKT VQLQRMVDQR SVASDEKKVA LLYLDNEEEE
     EEEGEGWF
//
ID   Q3TT81_MOUSE            Unreviewed;       322 AA.
AC   Q3TT81;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Pcbp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Ovary and uterus;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Ovary and uterus;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Ovary and uterus;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Ovary and uterus;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Ovary and uterus;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Ovary and uterus;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Ovary and uterus;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Ovary and uterus;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 3 KH domains.
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DR   EMBL; AK161527; BAE36444.1; -; mRNA.
DR   IPI; IPI00956778; -.
DR   RefSeq; NP_001096635.1; NM_001103165.1.
DR   RefSeq; NP_001096636.1; NM_001103166.1.
DR   RefSeq; NP_001167544.1; NM_001174073.1.
DR   RefSeq; NP_035172.2; NM_011042.2.
DR   UniGene; Mm.236513; -.
DR   ProteinModelPortal; Q3TT81; -.
DR   SMR; Q3TT81; 11-169, 243-315.
DR   Ensembl; ENSMUST00000108838; ENSMUSP00000104466; ENSMUSG00000056851.
DR   GeneID; 18521; -.
DR   KEGG; mmu:18521; -.
DR   CTD; 18521; -.
DR   MGI; MGI:108202; Pcbp2.
DR   HOVERGEN; HBG053520; -.
DR   ArrayExpress; Q3TT81; -.
DR   Bgee; Q3TT81; -.
DR   Genevestigator; Q3TT81; -.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR004088; KH_type_1.
DR   InterPro; IPR018111; KH_type_1_subgr.
DR   Pfam; PF00013; KH_1; 3.
DR   SMART; SM00322; KH; 3.
DR   PROSITE; PS50084; KH_TYPE_1; 3.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   322 AA;  33926 MW;  7DDD51D4F8BEB977 CRC64;
     MDTGVIEGGL NVTLTIRLLM HGKEVGSIIG KKGESVKKMR EESGARINIS EGNCPERIIT
     LAGPTNAIFK AFAMIIDKLE EDISSSMTNS TAASRPPVTL RLVVPASQCG SLIGKGGCKI
     KEIRESTGAQ VQVAGDMLPN STERAITIAG IPQSIIECVK QICVVMLETL SQSPPKGVTI
     PYRPKPSSSP VIFAGGQAYT IQGQYAIPQP DLTKLHQLAM QQSHFPMTHG NTGFSAGLDA
     SAQTTSHELT IPNDLIGCII GRQGAKINEI RQMSGAQIKI ANPVEGSTDR QVTITGSAAS
     ISLAQYLINV RLSSETGGMG SS
//
ID   YETS2_MOUSE             Reviewed;        1407 AA.
AC   Q3TUF7; Q6PGF8; Q80TI2; Q8CG86;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=YEATS domain-containing protein 2;
GN   Name=Yeats2; Synonyms=Kiaa1197;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-497.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-1407 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 991-1407 (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Component of the ATAC complex, a complex with histone
CC       acetyltransferase activity on histones H3 and H4 (By similarity).
CC   -!- SUBUNIT: Component of the ADA2A-containing complex (ATAC),
CC       composed of CSRP2BP, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5,
CC       YEATS2, CCDC101 and DR1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3TUF7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3TUF7-2; Sequence=VSP_017007, VSP_017008;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q3TUF7-3; Sequence=VSP_017006;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 YEATS domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH57045.1; Type=Erroneous initiation;
CC       Sequence=BAC65745.3; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it is derived from pre-RNA;
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DR   EMBL; AK160791; BAE36014.1; -; mRNA.
DR   EMBL; AK122463; BAC65745.3; ALT_SEQ; Transcribed_RNA.
DR   EMBL; BC042768; AAH42768.1; -; mRNA.
DR   EMBL; BC057045; AAH57045.1; ALT_INIT; mRNA.
DR   IPI; IPI00655073; -.
DR   IPI; IPI00672762; -.
DR   IPI; IPI00676162; -.
DR   RefSeq; NP_001028409.2; NM_001033237.2.
DR   RefSeq; NP_001139402.1; NM_001145930.1.
DR   UniGene; Mm.390895; -.
DR   ProteinModelPortal; Q3TUF7; -.
DR   SMR; Q3TUF7; 206-312.
DR   PhosphoSite; Q3TUF7; -.
DR   PRIDE; Q3TUF7; -.
DR   Ensembl; ENSMUST00000041176; ENSMUSP00000043342; ENSMUSG00000041215.
DR   Ensembl; ENSMUST00000090052; ENSMUSP00000087506; ENSMUSG00000041215.
DR   Ensembl; ENSMUST00000115560; ENSMUSP00000111222; ENSMUSG00000041215.
DR   GeneID; 208146; -.
DR   KEGG; mmu:208146; -.
DR   UCSC; uc007ypj.1; mouse.
DR   CTD; 208146; -.
DR   MGI; MGI:2447762; Yeats2.
DR   eggNOG; roNOG05977; -.
DR   GeneTree; ENSGT00530000063543; -.
DR   HOGENOM; HBG713990; -.
DR   HOVERGEN; HBG062745; -.
DR   InParanoid; Q3TUF7; -.
DR   OMA; PQGAILR; -.
DR   OrthoDB; EOG4QZ7K2; -.
DR   NextBio; 372166; -.
DR   ArrayExpress; Q3TUF7; -.
DR   Bgee; Q3TUF7; -.
DR   CleanEx; MM_YEATS2; -.
DR   Genevestigator; Q3TUF7; -.
DR   GermOnline; ENSMUSG00000041215; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR005033; YEATS.
DR   PANTHER; PTHR23195; YEATS; 1.
DR   Pfam; PF03366; YEATS; 1.
DR   PROSITE; PS51037; YEATS; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Nucleus; Phosphoprotein.
FT   CHAIN         1   1407       YEATS domain-containing protein 2.
FT                                /FTId=PRO_0000076367.
FT   DOMAIN      208    318       YEATS.
FT   COILED       54     80       Potential.
FT   COMPBIAS    792    828       Gly-rich.
FT   MOD_RES     118    118       Phosphoserine (By similarity).
FT   MOD_RES     144    144       Phosphoserine (By similarity).
FT   MOD_RES     446    446       Phosphoserine (By similarity).
FT   MOD_RES     462    462       Phosphoserine (By similarity).
FT   MOD_RES     464    464       Phosphoserine (By similarity).
FT   MOD_RES     472    472       Phosphoserine (By similarity).
FT   MOD_RES     517    517       Phosphoserine (By similarity).
FT   MOD_RES     519    519       Phosphothreonine (By similarity).
FT   MOD_RES     534    534       Phosphoserine (By similarity).
FT   MOD_RES     763    763       Phosphoserine (By similarity).
FT   VAR_SEQ       1     53       Missing (in isoform 3).
FT                                /FTId=VSP_017006.
FT   VAR_SEQ    1291   1305       NIKKEQEEKQEEMRF -> SASVVNLLFVCSKET (in
FT                                isoform 2).
FT                                /FTId=VSP_017007.
FT   VAR_SEQ    1306   1407       Missing (in isoform 2).
FT                                /FTId=VSP_017008.
FT   CONFLICT    310    310       L -> V (in Ref. 2; BAC65745).
FT   CONFLICT   1162   1162       K -> E (in Ref. 1; BAE36014).
FT   CONFLICT   1294   1294       K -> R (in Ref. 1; BAE36014).
SQ   SEQUENCE   1407 AA;  148950 MW;  E5530016D1846E2E CRC64;
     MSGIKRTIKE TDPDYEDVSV ALPNKRHKAI ESSARDAAVQ KIETIIKEQF ALEMKNKEHE
     IDVIDQRLIE ARRMMDKLRA CIVANYYASA GLLKVSEGLK TFDPMAFNHP AIKKFLESPS
     RSSSPTNQRS ETPSANHSES DSLSQHNDFL SDKDNNSNVD VEERPPSTGE QRPSRKAGRD
     TSSISGSHKR ELRNADLTGD ETSRLFVKKT IVVGNVSKYI PPDKREENDQ STHKWMVYVR
     GSRREPSINH FVKKVWFFLH PSYKPNDLVE VREPPFHLTR RGWGEFPVRV QVHFKDSQNK
     RIDIIHNLKL DRTYTGLQTL GAETVVDVEL HRHSLGEDSV YPQSSESDVC DAPPPTLTLP
     AAVKASAVAQ SPEPAAAAPV GEGFPETTEA ERHSTFYSLP SSLERTPTKV TTAQKVTFSS
     HGNSAFQPIA SSCKIVPQSQ VPNPESPGKS FQPITMSCKI VSGSPISTPS PSPLPRTPTS
     TPVHLKQGTA SSGVSNPHVI VDKPGQVIGA STPSTGSPTS KLPVASQASQ GTGSPIPKIH
     GSSFLTSTVK QEESLFASMP PLCPIGSHPK VQSPKAVTGG LGAFTKVIIK QEPGEAPHVS
     TTGAASQSAF PQYVTVKGGH MIAVSPQKQV ISAGEGTTQS PKIAPSKVVG VPVGSALPST
     VKQAVAISSG QILVAKASSS VTKAVGPKQV VTQGVAKAIV SGGGGTIVAQ PVQTLTKTQV
     TAAGPQKSGS QGSVMATLQL PATNLANLAN LPPGTKLYLT TNSKNPSGKG KLLLIPQGAI
     LRATNNANLQ SGSAAAGGSG SSGAGGGSGG GGGSGAGGTP STSGPGGGPQ HLTYTSYILK
     QTPQGTFLVG QPSPQTPGKQ LTTASVVQGT LGVSSSSAQG QQTLKVISGQ KTTLFTQAAT
     AGQASLLKLP DNTLKSVPAA PQLAKPGTTM LRVAGGVITA APSPAVAFSA NGAVHQSEGS
     TPVSSSVGSI IKTPGQPQVC VSQATMATCK GPAAVAGTAA SLVSAPSSIS GKATVSGLLK
     VHSAQSSPQQ AVLTIPSQLK PLSINTSGGV QTVLMPVNKV VQSFSTSKLP TTVLPISVPN
     QAAPSSAPVA IAKVKTEPET PGPNCISQEN QVAVKTEESS ELSNYVIKVD HLETIQQLLT
     AVVKKIPLIT AKGDDASCFS AKSLEQYYGW NIGKRRAAEW QRAMTVRKVL QEILEKNPRF
     HHLTPLKTKH IAHWCRCHGY TPPDPESLRH DGDSIEDVLT QIDSEPECLS SFSTADDLCR
     KLEDLQQFQK REPENEEEVD ILSLSEPLKT NIKKEQEEKQ EEMRFYLPPT PGSGFVGDIT
     QKIGITLQPV ALHRNMYASV VEDMILKATE QLVSDILRQA LAVGYQTASP NRIPKEITVS
     NIHQAICNIP FLDFLTNKHM GRLNEDQ
//
ID   CC136_MOUSE             Reviewed;        1136 AA.
AC   Q3TVA9; Q923E5;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   08-MAR-2011, entry version 44.
DE   RecName: Full=Coiled-coil domain-containing protein 136;
GN   Name=Ccdc136;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 257-1136 (ISOFORM 2).
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 396-1029 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3TVA9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3TVA9-2; Sequence=VSP_027846, VSP_027847, VSP_027848;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH06583.1; Type=Erroneous initiation;
CC       Sequence=BAE35710.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAE35710.1; Type=Erroneous termination; Positions=450; Note=Translated as Cys;
CC   -----------------------------------------------------------------------
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DR   EMBL; AC044807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC006583; AAH06583.1; ALT_INIT; mRNA.
DR   EMBL; AK160245; BAE35710.1; ALT_SEQ; mRNA.
DR   IPI; IPI00124212; -.
DR   IPI; IPI00856375; -.
DR   RefSeq; NP_663549.2; NM_145574.2.
DR   UniGene; Mm.251303; -.
DR   PhosphoSite; Q3TVA9; -.
DR   PRIDE; Q3TVA9; -.
DR   Ensembl; ENSMUST00000096084; ENSMUSP00000093789; ENSMUSG00000029769.
DR   GeneID; 232664; -.
DR   KEGG; mmu:232664; -.
DR   CTD; 232664; -.
DR   MGI; MGI:1918128; Ccdc136.
DR   eggNOG; roNOG14930; -.
DR   GeneTree; ENSGT00530000063197; -.
DR   HOGENOM; HBG506918; -.
DR   HOVERGEN; HBG107598; -.
DR   InParanoid; Q3TVA9; -.
DR   ArrayExpress; Q3TVA9; -.
DR   Bgee; Q3TVA9; -.
DR   CleanEx; MM_CCDC136; -.
DR   Genevestigator; Q3TVA9; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   1136       Coiled-coil domain-containing protein
FT                                136.
FT                                /FTId=PRO_0000300640.
FT   TRANSMEM   1112   1132       Helical; (Potential).
FT   COILED      293    631       Potential.
FT   COILED      681    730       Potential.
FT   COILED      839    972       Potential.
FT   COILED     1017   1057       Potential.
FT   COMPBIAS     15    140       Glu-rich.
FT   COMPBIAS    744    830       Ser-rich.
FT   VAR_SEQ     361    361       Missing (in isoform 2).
FT                                /FTId=VSP_027846.
FT   VAR_SEQ     917    951       IKELQTKLRELQLQYQASMDEQGRLLAVQEQLEGQ -> NM
FT                                FGMWKPMVFLAIAAVALYVLPNMRPQESEYYMK (in
FT                                isoform 2).
FT                                /FTId=VSP_027847.
FT   VAR_SEQ     952   1136       Missing (in isoform 2).
FT                                /FTId=VSP_027848.
FT   CONFLICT    412    412       S -> N (in Ref. 2; AAH06583).
SQ   SEQUENCE   1136 AA;  131930 MW;  6C289387FF214D41 CRC64;
     MQAMDGEVLL PALYEEEEEE EEEEEEVEEE QVEKGGSLGS LSMGKHRGLS LTETELEELR
     AQVLQLVAEL EETRELAGQH EDDSLELQGL LEDERLASAQ QAEVFTKQIQ QLQGELQHLR
     EEISLLEHEK ESELKEMEQE LHLAQAEIQN LRQAAADSAT EHESDIASLQ DDLCRLQNDL
     DDMERIRGDY EMEIASLRAE MELKTSEPSN LSISDFSGIQ DELHHLRERY NLLNEEYQAL
     RESNSSLTGQ LAELESDRTR RATERWLESH LLRSTMSSES QTSELDFPEP DPVMQLLRQQ
     LLGAEEQMQD MQDKCKNLYC ELEELQHHRR TSEEEQKRLQ RELKCAQNEV LRFQTSHSTQ
     QHEELKSRLC TLQQKYDASQ DEHSELLKVQ MQLETELQQL RLLRCTPVES QSEKELMCRL
     QKLQAQHQCS VNEKEQLLEV QHHLHDKLRC HESEVHRLRS MVDCLREKNE KNSGIHLQLQ
     EMKGLYQFSR DELERQKHMY DQLEQDFLLC QQELTELKSS QSLCEENGNC SNKCDALLAR
     LTELQDKFKA SQEEIGHLQM EQCELLEDQR RLQEEQGQLQ EELHRLTFPQ PKCGILQKSQ
     ELLSKLQDLC EMQLLYQNMQ EQQRKLTQNQ ECVLKEQLEA HKHLRGFKES HFQEVLANPQ
     DARGPKSSSC ENKFKVLMDQ LQALQVLYDT SQKQQEVLQR EHGRLMEERK RLQAELQLCM
     EEMQVLQTQS PMIKRSFEYC GKNSGSRAPS TENFHRSYES SIDENEGYQK SYVSSQPSTE
     TFLKSYDSST SANEAFEKSY CSSSTSVSYK KSYGSVSSGE TLHRSYASSS TDEDPAEPED
     LEHFEETVAK VLTKLQAVKA LYQVSQEEHC QLQQRMHRLL AKQKELTEEL QCCEKELREC
     MESLGKPLPP QSDKCEIKEL QTKLRELQLQ YQASMDEQGR LLAVQEQLEG QLQCCQEELR
     QLKENRPSIS SEARGKNVNK NMNKNANGVR NKKLSMACSE DLENGFENEK NLEVMLYYKA
     SQRRLDELMK EEKEIEEARK KEREKKAKKD LCKLATNPAA DPRAEPEPTE DEEENFEEYR
     EGEDESCEAA EEGNPLKLSE SKKPSPAPDP PIFSLPLVGL VVISALLWCW WAETSS
//
ID   PBIP1_MOUSE             Reviewed;         727 AA.
AC   Q3TVI8; Q3TD91; Q3TWL9; Q8R319;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=Pre-B-cell leukemia transcription factor-interacting protein 1;
DE   AltName: Full=Hematopoietic PBX-interacting protein;
GN   Name=Pbxip1; Synonyms=Hpip;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; SER-143 AND
RP   SER-144, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Regulator of pre-B-cell leukemia transcription factors
CC       (BPXs) function. Inhibits the binding of PBX1-HOX complex to DNA
CC       and blocks the transcriptional activity of E2A-PBX1. Tethers
CC       estrogen receptor-alpha (ESR1) to microtubules and allows them to
CC       influence estrogen receptors-alpha signaling (By similarity).
CC   -!- SUBUNIT: Interacts with ESR1, PBX1, PBX2 and PBX3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Nucleus (By similarity). Note=Shuttles between the nucleus and the
CC       cytosol. Mainly localized in the cytoplasm, associated with
CC       microtubules. Detected in small amounts in the nucleus (By
CC       similarity).
CC   -!- DOMAIN: The C-terminal domain (AA 443-731) contains a nuclear
CC       export signal (By similarity).
CC   -!- DOMAIN: Association to the cytoskeleton through a N-terminal
CC       leucine rich-domain (AA 190-218) (By similarity).
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK028858; BAC26157.1; -; mRNA.
DR   EMBL; AK159422; BAE35070.1; -; mRNA.
DR   EMBL; AK159448; BAE35092.1; -; mRNA.
DR   EMBL; AK159633; BAE35247.1; -; mRNA.
DR   EMBL; AK160103; BAE35630.1; -; mRNA.
DR   EMBL; AK170318; BAE41713.1; -; mRNA.
DR   EMBL; BC026838; AAH26838.1; -; mRNA.
DR   EMBL; BC027771; AAH27771.1; -; mRNA.
DR   EMBL; BC034200; AAH34200.1; -; mRNA.
DR   IPI; IPI00153644; -.
DR   RefSeq; NP_666243.1; NM_146131.2.
DR   UniGene; Mm.65906; -.
DR   ProteinModelPortal; Q3TVI8; -.
DR   IntAct; Q3TVI8; 2.
DR   STRING; Q3TVI8; -.
DR   PhosphoSite; Q3TVI8; -.
DR   PRIDE; Q3TVI8; -.
DR   Ensembl; ENSMUST00000038942; ENSMUSP00000040429; ENSMUSG00000042613.
DR   GeneID; 229534; -.
DR   KEGG; mmu:229534; -.
DR   CTD; 229534; -.
DR   MGI; MGI:2441670; Pbxip1.
DR   eggNOG; roNOG05579; -.
DR   GeneTree; ENSGT00530000063862; -.
DR   HOGENOM; HBG126255; -.
DR   HOVERGEN; HBG108234; -.
DR   InParanoid; Q3TVI8; -.
DR   OMA; ARLPWAG; -.
DR   OrthoDB; EOG40VVP5; -.
DR   PhylomeDB; Q3TVI8; -.
DR   NextBio; 379487; -.
DR   ArrayExpress; Q3TVI8; -.
DR   Bgee; Q3TVI8; -.
DR   Genevestigator; Q3TVI8; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Nucleus;
KW   Phosphoprotein.
FT   CHAIN         1    727       Pre-B-cell leukemia transcription factor-
FT                                interacting protein 1.
FT                                /FTId=PRO_0000306116.
FT   COILED      270    350       Potential.
FT   COILED      377    405       Potential.
FT   MOTIF       486    506       Nuclear localization signal (By
FT                                similarity).
FT   MOTIF       691    716       Nuclear localization signal (By
FT                                similarity).
FT   COMPBIAS    156    161       Poly-Arg.
FT   MOD_RES      45     45       Phosphoserine (By similarity).
FT   MOD_RES     142    142       Phosphoserine.
FT   MOD_RES     143    143       Phosphoserine.
FT   MOD_RES     144    144       Phosphoserine.
FT   MOD_RES     148    148       Phosphothreonine (By similarity).
FT   CONFLICT    120    120       E -> G (in Ref. 1; BAE35247).
FT   CONFLICT    410    410       W -> R (in Ref. 1; BAE35630/BAE41713/
FT                                BAE35247).
FT   CONFLICT    516    516       R -> H (in Ref. 1; BAE41713).
SQ   SEQUENCE   727 AA;  81164 MW;  D33539CF495B9222 CRC64;
     MASCPDSDNS WVLAGSENLP VETLGPEPRM DPESEGASQA LRDSSKADGK ELAGTLDGEE
     KLFQTESSQR ETAVLTESAA KGTLGADGHG TEAPGDTVVQ EDSQETPVAT SLGPDTQDLE
     SEIHPQNLPS SPRAVWKEHR CSSSDDDTDV DVEGLRRRRG REPSSSQPVV PVDVEDQAKG
     EGIGGELGIS LNMCFLGALV LLGLGILLFS GTLLEPETGP MEEAELQVFP ETGPETELVE
     TLGNRQDEIE HLQASSVPPD SVPSLQSMGF LLDKLAKENQ DIRLLQAQLQ AQKEELQSLL
     HQPKGLEEEN ARLREALQQG KTSHQALESE LQQLRARLQG LEANCVRGVD GVCLNWGGDP
     QDGKATKEQG HKGQEPDPSL LEQHKQLEAE AKALRQELQR QWQLLGSVHW DLQRGLRDAG
     RGAPAHPGLA ELGHMLAQTL QDLENQGINT GRSPNDSEAW HQKKPHTQSP REWGGKEKWR
     GGQRDQKAEH WKPRKEESGQ ERQRSWRDEG REHTGRWRED RLRADESGSR KDSKRQDPKV
     HPRKDGNSHS VERQKHSWGK DNSPDALSSW EELLRRKYRP PQGCSGVADC ARQEGLALFG
     VELAPVRQQE LASVLREYLS RLPWAGQLTK QLPLSPAYFG EDGIFRHDRL RFRDFVDALE
     DSLEEVALKQ TGDDDEVDDF EDFVFGHFFG DKALKKRSRK KEKHSWNPRV VGPREEHSRH
     PHHYHQG
//
ID   TM55B_MOUSE             Reviewed;         284 AA.
AC   Q3TWL2;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=Transmembrane protein 55B;
DE            EC=3.1.3.78;
DE   AltName: Full=PtdIns-4,5-P2 4-Ptase I;
DE   AltName: Full=Type I phosphatidylinositol 4,5-bisphosphate 4-phosphatase;
GN   Name=Tmem55b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of
CC       phosphatidylinositol 4,5-bisphosphate. Does not hydrolyze
CC       phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol
CC       3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4-
CC       bisphosphate, phosphatidylinositol 5-monophosphate,
CC       phosphatidylinositol 4-monophosphate and phosphatidylinositol 3-
CC       monophosphate (By similarity).
CC   -!- CATALYTIC ACTIVITY: 1-phosphatidyl-myo-inositol 4,5-bisphosphate +
CC       H(2)O = 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate.
CC   -!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-
CC       bisphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 5-phosphate
CC       + phosphate.
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane; Multi-pass membrane
CC       protein (By similarity). Lysosome membrane; Multi-pass membrane
CC       protein (By similarity).
CC   -----------------------------------------------------------------------
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DR   EMBL; AK144251; BAE25798.1; -; mRNA.
DR   EMBL; AK159641; BAE35254.1; -; mRNA.
DR   EMBL; BC106163; AAI06164.1; -; mRNA.
DR   IPI; IPI00356633; -.
DR   RefSeq; NP_001028443.1; NM_001033271.4.
DR   UniGene; Mm.239117; -.
DR   ProteinModelPortal; Q3TWL2; -.
DR   PhosphoSite; Q3TWL2; -.
DR   PRIDE; Q3TWL2; -.
DR   Ensembl; ENSMUST00000049312; ENSMUSP00000038276; ENSMUSG00000035953.
DR   GeneID; 219024; -.
DR   KEGG; mmu:219024; -.
DR   UCSC; uc007tma.1; mouse.
DR   CTD; 219024; -.
DR   MGI; MGI:2448501; Tmem55b.
DR   eggNOG; roNOG06529; -.
DR   GeneTree; ENSGT00390000003680; -.
DR   HOGENOM; HBG381966; -.
DR   HOVERGEN; HBG080409; -.
DR   InParanoid; Q3TWL2; -.
DR   OMA; GIYASWA; -.
DR   OrthoDB; EOG447FV8; -.
DR   NextBio; 376535; -.
DR   ArrayExpress; Q3TWL2; -.
DR   Bgee; Q3TWL2; -.
DR   CleanEx; MM_TMEM55B; -.
DR   Genevestigator; Q3TWL2; -.
DR   GermOnline; ENSMUSG00000035953; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR019178; Transmembrane_protein_55A/B.
DR   PANTHER; PTHR21014; Transmembrane_protein_55A/B; 1.
DR   Pfam; PF09788; Tmemb_55A; 1.
PE   1: Evidence at protein level;
KW   Endosome; Hydrolase; Lysosome; Membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    284       Transmembrane protein 55B.
FT                                /FTId=PRO_0000235234.
FT   TRANSMEM    219    239       Helical; (Potential).
FT   TRANSMEM    246    266       Helical; (Potential).
FT   MOTIF       140    146       CX5R motif.
FT   COMPBIAS     15     48       Gly-rich.
FT   ACT_SITE    140    140       By similarity.
FT   MOD_RES     169    169       Phosphoserine.
SQ   SEQUENCE   284 AA;  30047 MW;  6F85B05FBA3B908B CRC64;
     MAADGERSPL LSEAGDGGAG GNGLAGPGGS ATGPGGGLTP SAPPYGAGKH APPQAFPPFP
     EGHPAVLPGE DPPPYSPLTS PDSGSAPMIT CRVCQSPINV EGKMHQHVVK CGVCNEATPI
     KNAPPGKKYV RCPCNCLLIC KVTSQRIACP RPYCKRIINL GPVHPGPLSP EPQPMGVRVI
     CGHCKNTFLW TEFTDRTLAR CPHCRKVSSI GRRYPRKRCI CCFLLGLLLA VTATGLAFGT
     WKHAQQYGGI YAAWAFVILL AVLCLGRALY WACMKVSHPV QNFS
//
ID   CNNM2_MOUSE             Reviewed;         875 AA.
AC   Q3TWN3; A0PJF1; Q7TT07; Q8C8V4; Q9JIM8;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   08-MAR-2011, entry version 44.
DE   RecName: Full=Metal transporter CNNM2;
DE   AltName: Full=Ancient conserved domain-containing protein 2;
DE            Short=mACDP2;
DE   AltName: Full=Cyclin-M2;
GN   Name=Cnnm2; Synonyms=Acdp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-875 (ISOFORM 1).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary gland, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 27-36, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 176-875 (ISOFORM 1), AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=14723793; DOI=10.1186/1471-2164-5-7;
RA   Wang C.-Y., Yang P., Shi J.-D., Purohit S., Guo D., An H., Gu J.-G.,
RA   Ling J., Dong Z., She J.-X.;
RT   "Molecular cloning and characterization of the mouse Acdp gene
RT   family.";
RL   BMC Genomics 5:7-7(2004).
RN   [5]
RP   FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=15899945; DOI=10.1152/physiolgenomics.00058.2005;
RA   Goytain A., Quamme G.A.;
RT   "Functional characterization of ACDP2 (ancient conserved domain
RT   protein), a divalent metal transporter.";
RL   Physiol. Genomics 22:382-389(2005).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-111, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Divalent metal cation transporter. Mediates transport of
CC       divalent metal cations in an order of Mg(2+) > Co(2+) > Mn(2+) >
CC       Sr(2+) > Ba(2+) > Cu(2+) > Fe(2+).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3TWN3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3TWN3-2; Sequence=VSP_027081;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
CC       brain, kidney and liver. Not expressed in skeletal muscle and
CC       skin.
CC   -!- INDUCTION: By low Mg(2+) concentration.
CC   -!- MISCELLANEOUS: Shares weak sequence similarity with the cyclin
CC       family, explaining its name. However it has no cyclin-like
CC       function in vivo.
CC   -!- SIMILARITY: Belongs to the ACDP family.
CC   -!- SIMILARITY: Contains 2 CBS domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF86373.1; Type=Erroneous initiation;
CC       Sequence=AAH27387.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAH52513.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK044400; BAC31904.1; -; mRNA.
DR   EMBL; AK159616; BAE35233.1; -; mRNA.
DR   EMBL; BC027387; AAH27387.1; ALT_SEQ; mRNA.
DR   EMBL; BC052513; AAH52513.1; ALT_INIT; mRNA.
DR   EMBL; AF216961; AAF86373.1; ALT_INIT; mRNA.
DR   IPI; IPI00131762; -.
DR   IPI; IPI00762609; -.
DR   RefSeq; NP_001095941.1; NM_001102471.1.
DR   RefSeq; NP_291047.2; NM_033569.3.
DR   UniGene; Mm.306903; -.
DR   ProteinModelPortal; Q3TWN3; -.
DR   SMR; Q3TWN3; 408-581.
DR   STRING; Q3TWN3; -.
DR   TCDB; 9.A.40.3.1; HlyC/CorC (HCC) family.
DR   PRIDE; Q3TWN3; -.
DR   Ensembl; ENSMUST00000077666; ENSMUSP00000076850; ENSMUSG00000064105.
DR   GeneID; 94219; -.
DR   KEGG; mmu:94219; -.
DR   UCSC; uc008hue.1; mouse.
DR   CTD; 94219; -.
DR   MGI; MGI:2151054; Cnnm2.
DR   eggNOG; roNOG06423; -.
DR   GeneTree; ENSGT00390000002383; -.
DR   HOGENOM; HBG715526; -.
DR   HOVERGEN; HBG074775; -.
DR   InParanoid; Q3TWN3; -.
DR   OrthoDB; EOG405S0M; -.
DR   NextBio; 352201; -.
DR   ArrayExpress; Q3TWN3; -.
DR   Bgee; Q3TWN3; -.
DR   CleanEx; MM_CNNM2; -.
DR   Genevestigator; Q3TWN3; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000644; Cysta_beta_synth_core.
DR   InterPro; IPR002550; DUF21.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 2.
DR   Pfam; PF01595; DUF21; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; CBS domain; Cell membrane;
KW   Direct protein sequencing; Glycoprotein; Ion transport; Membrane;
KW   Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    875       Metal transporter CNNM2.
FT                                /FTId=PRO_0000295761.
FT   TRANSMEM     48     68       Helical; (Potential).
FT   TRANSMEM    251    271       Helical; (Potential).
FT   TRANSMEM    314    334       Helical; (Potential).
FT   TRANSMEM    339    359       Helical; (Potential).
FT   TRANSMEM    369    389       Helical; (Potential).
FT   DOMAIN      450    511       CBS 1.
FT   DOMAIN      518    584       CBS 2.
FT   CARBOHYD    111    111       N-linked (GlcNAc...).
FT   VAR_SEQ     721    742       Missing (in isoform 2).
FT                                /FTId=VSP_027081.
FT   CONFLICT    131    131       S -> G (in Ref. 1; BAC31904 and 2;
FT                                AAH27387).
FT   CONFLICT    664    664       C -> Y (in Ref. 2; AAH52513 and 4;
FT                                AAF86373).
SQ   SEQUENCE   875 AA;  96644 MW;  2EC494C6D6950F1C CRC64;
     MIGCGACEPE VKMAGGQAAA ALPTWKMAAR RSLSARGRGV LQAAAGRLLP LLLLSCCWGA
     GGCTAAGENE ETVIIGLRLE DTNDVSFMEG GALRVSERTR VKLRVYGQNI NNETWSRIAF
     TEHERRRHTP SERGLGGPAP PEPDSGPQRC GIRTSDIIIL PHIILNRRTS GIIEIEIKPL
     RKMEKSKSYY LCTSLSTPAL GAGGSGSASG TVGGKGGAGV AGLPPPPWAE TTWIYHDGED
     TKMIVGEEKK FLLPFWLQVI FISLLLCLSG MFSGLNLGLM ALDPMELRIV QNCGTEKEKN
     YAKRIEPVRR QGNYLLCSLL LGNVLVNTTL TILLDDIAGS GLVAVVVSTI GIVIFGEIVP
     QAICSRHGLA VGANTIFLTK FFMMMTFPAS YPVSKLLDCV LGQEIGTVYN REKLLEMLRV
     TDPYNDLVKE ELNIIQGALE LRTKTVEDVM TPLRDCFMIT GEAILDFNTM SEIMESGYTR
     IPVFEGERSN IVDLLFVKDL AFVDPDDCTP LKTITKFYNH PLHFVFNDTK LDAMLEEFKK
     GKSHLAIVQR VNNEGEGDPF YEVLGIVTLE DVIEEIIKSE ILDETDLYTD NRTKKKVAHR
     ERKQDFSAFK QTDSEMKVKI SPQLLLAMHR FLATEVEAFS PSQMSEKILL RLLKHPNVIQ
     ELKCDEKNKK APECYLYQRN KPVDYFVLIL QGKVEVEAGK EGMKFEASAF SYYGVMALTA
     SPVPLSLSRT FVVSRTEVLA AGSPGENKSP PRPCGLNHSD SLSRSDRIDA MTPTLGSSNN
     QLSSSFLQVY IPDYSVRALS DLQFVKISRQ QYQNALMASR MDKTPQSSDS ENTKIELTLT
     ELHDGLPDET ANLLNEQNCV SHNKANHSLH SEGAI
//
ID   Q3TWN8_MOUSE            Unreviewed;       795 AA.
AC   Q3TWN8;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Aldh18a1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK159610; BAE35228.1; -; mRNA.
DR   IPI; IPI00944043; -.
DR   UniGene; Mm.233117; -.
DR   ProteinModelPortal; Q3TWN8; -.
DR   SMR; Q3TWN8; 69-355, 362-793.
DR   STRING; Q3TWN8; -.
DR   Ensembl; ENSMUST00000025979; ENSMUSP00000025979; ENSMUSG00000025007.
DR   MGI; MGI:1888908; Aldh18a1.
DR   eggNOG; roNOG06553; -.
DR   HOVERGEN; HBG007911; -.
DR   InParanoid; Q3TWN8; -.
DR   ArrayExpress; Q3TWN8; -.
DR   Bgee; Q3TWN8; -.
DR   Genevestigator; Q3TWN8; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0004349; F:glutamate 5-kinase activity; IDA:MGI.
DR   GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:InterPro.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR000965; G-glutamylP_reductase.
DR   InterPro; IPR020593; G-glutamylP_reductase_CS.
DR   InterPro; IPR001057; Glu/AcGlu_kinase.
DR   InterPro; IPR005715; Glu_5kinase/COase_Synthase.
DR   InterPro; IPR019797; Glutamate_5-kinase_CS.
DR   InterPro; IPR005766; P5_carboxy_syn.
DR   Gene3D; G3DSA:3.40.1160.10; Aa_kinase; 1.
DR   Gene3D; G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 1.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 2.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036429; P5C_syn; 1.
DR   PRINTS; PR00474; GLU5KINASE.
DR   SUPFAM; SSF53633; Aa_kinase; 1.
DR   SUPFAM; SSF53720; Aldehyde_DH/Histidinol_DH; 1.
DR   TIGRFAMs; TIGR01092; P5CS; 1.
DR   TIGRFAMs; TIGR00407; proA; 1.
DR   TIGRFAMs; TIGR01027; proB; 1.
DR   PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
DR   PROSITE; PS01223; PROA; 1.
PE   2: Evidence at transcript level;
KW   Transferase.
SQ   SEQUENCE   795 AA;  87263 MW;  877DF0AD57376447 CRC64;
     MLRHMHRSGV QPFRQRLLPW VQSIAVPRSN RVQPSAIRHV RSWSNIPFIT VPLSRAHGKP
     FAHRSELKHA KRIVVKLGSA VVTRGDECGL ALGRLASIVE QVSVLQNQGR EMMLVTSGAV
     AFGKQRLRHE ILLSQSVRQA LHSGQNHLKE MAIPVLEARA CAAAGQSGLM ALYEAMFTQY
     SICAAQILVT NLDFHDEQKR RNLNGTLHEL LRMNIVPIVN TNDAVVPPAE PNSDLQGVNV
     ISVKDNDSLA ARLAVEKKTD LLIVLSDVEG LFDSPPGSDD AKLIDIFYPG DQQSVTFGTK
     SRVGLGGMEA KVKAALWALQ GGTSVVIANG THPKVSGHVI TDIVEGKKVG TFFSEVKPAG
     PTVEQQGEMA RSGGRMLATL EPEQRAEIIN HLADLLTDQR EEILLANKKD LEEAEGRLAS
     PLLKRLSLST SKLNSLAIGL RQIAASSQES VGRVLRRTRI AKNLELEQVT VPIGVLLVIF
     ESRPDCLPQV AALAIASGNG LLLKGGKEAA HSNRILHLLT QEALSIHGVK EAIQLVNTRE
     EVEDLCRLDK IIDLIIPRGS SQLVRDIQKA AKGIPVMGHS EGICHMYVDS EASVDKVTRL
     VRDSKCEYPA ACNALETLLI HRDLLRTPLF DQIIDMLRVE QVKIHAGPKF ASYLTFSPSE
     VKSLRTEYGD LEVCIEVVDS VQEAIDHIHK YGSSHTDVIV TENEKTAEFF LQHVDSACVF
     WNASTRFSDG YRFGLGAEVG ISTSRIHARG PVGLEGLLTT KWLLRGQDHV VSDFSEHGSL
     KYLHENLPVP QRNFS
//
ID   Q3TXK7_MOUSE            Unreviewed;       355 AA.
AC   Q3TXK7;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 50.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Gnai2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta, and Inner ear;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta, and Inner ear;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta, and Inner ear;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta, and Inner ear;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta, and Inner ear;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta, and Inner ear;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta, and Inner ear;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK157998; BAE34308.1; -; mRNA.
DR   EMBL; AK159222; BAE34909.1; -; mRNA.
DR   EMBL; AK167388; BAE39478.1; -; mRNA.
DR   IPI; IPI00652902; -.
DR   RefSeq; NP_032164.2; NM_008138.4.
DR   UniGene; Mm.196464; -.
DR   ProteinModelPortal; Q3TXK7; -.
DR   SMR; Q3TXK7; 5-354.
DR   STRING; Q3TXK7; -.
DR   PRIDE; Q3TXK7; -.
DR   Ensembl; ENSMUST00000055704; ENSMUSP00000057543; ENSMUSG00000032562.
DR   GeneID; 14678; -.
DR   KEGG; mmu:14678; -.
DR   UCSC; uc009rml.1; mouse.
DR   CTD; 14678; -.
DR   MGI; MGI:95772; Gnai2.
DR   HOVERGEN; HBG063184; -.
DR   InParanoid; Q3TXK7; -.
DR   OMA; AEEQGIM; -.
DR   PhylomeDB; Q3TXK7; -.
DR   NextBio; 286578; -.
DR   ArrayExpress; Q3TXK7; -.
DR   Bgee; Q3TXK7; -.
DR   Genevestigator; Q3TXK7; -.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; TAS:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0008283; P:cell proliferation; IPI:MGI.
DR   GO; GO:0007193; P:inhibition of adenylate cyclase activity by G-protein signaling pathway; IMP:MGI.
DR   GO; GO:0007213; P:muscarinic acetylcholine receptor signaling pathway; IMP:MGI.
DR   InterPro; IPR001408; Gprotein_alpha_I.
DR   InterPro; IPR001019; Gprotein_alpha_su.
DR   InterPro; IPR011025; GproteinA_insert.
DR   Gene3D; G3DSA:1.10.400.10; GproteinA_insert; 1.
DR   PANTHER; PTHR10218; Gprotein_alph_bd; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00441; GPROTEINAI.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF47895; Transducn_insert; 1.
PE   2: Evidence at transcript level;
KW   GTP-binding; Nucleotide-binding; Transducer.
SQ   SEQUENCE   355 AA;  40489 MW;  90AC64AFA713493E CRC64;
     MGCTVSAEDK AAAERSKMID KNLREDGEKA AREVKLLLLG AGESGKSTIV KQMKIIHEDG
     YSEEECRQYR AVVYSNTIQS IMAIVKAMGN LQIDFADPQR ADDARQLFAL SCAAEEQGML
     PEDLSGVIRR LWADHGVQAC FGRSREYQLN DSAAYYLNDL ERIAQSDYIP TQQDVLRTRV
     KTTGIVETHF TFKDLHFKMF DVGGQRSERK KWIHCFEGVT AIIFCVALSA YDLVLAEDEE
     MNRMHESMKL FDSICNNKWF TDTSIILFLN KKDLFEEKIT QSSLTICFPE YTGANKYDEA
     ASYIQSKFED LNKRKDTKEI YTHFTCATDT KNVQFVFDAV TDVIIKNNLK DCGLF
//
ID   PSMD1_MOUSE             Reviewed;         953 AA.
AC   Q3TXS7; B2RRP8;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 1;
DE   AltName: Full=26S proteasome regulatory subunit RPN2;
DE   AltName: Full=26S proteasome regulatory subunit S1;
GN   Name=Psmd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-273, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311 AND SER-315, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311 AND SER-315, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Acts as a regulatory subunit of the 26 proteasome which
CC       is involved in the ATP-dependent degradation of ubiquitinated
CC       proteins (By similarity).
CC   -!- SUBUNIT: Interacts with ADRM1 (By similarity).
CC   -!- SIMILARITY: Belongs to the proteasome subunit S1 family.
CC   -!- SIMILARITY: Contains 10 PC repeats.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK153386; BAE31950.1; -; mRNA.
DR   EMBL; AK159123; BAE34838.1; -; mRNA.
DR   EMBL; BC138526; AAI38527.1; -; mRNA.
DR   EMBL; BC138527; AAI38528.1; -; mRNA.
DR   IPI; IPI00267295; -.
DR   RefSeq; NP_081633.1; NM_027357.2.
DR   UniGene; Mm.280013; -.
DR   ProteinModelPortal; Q3TXS7; -.
DR   SMR; Q3TXS7; 6-32, 435-737.
DR   IntAct; Q3TXS7; 2.
DR   STRING; Q3TXS7; -.
DR   PhosphoSite; Q3TXS7; -.
DR   PRIDE; Q3TXS7; -.
DR   Ensembl; ENSMUST00000027432; ENSMUSP00000027432; ENSMUSG00000026229.
DR   Ensembl; ENSMUST00000113330; ENSMUSP00000108956; ENSMUSG00000026229.
DR   GeneID; 70247; -.
DR   KEGG; mmu:70247; -.
DR   UCSC; uc007buy.1; mouse.
DR   CTD; 70247; -.
DR   MGI; MGI:1917497; Psmd1.
DR   HOGENOM; HBG324892; -.
DR   HOVERGEN; HBG007543; -.
DR   InParanoid; Q3TXS7; -.
DR   OrthoDB; EOG4X97GG; -.
DR   PhylomeDB; Q3TXS7; -.
DR   NextBio; 331246; -.
DR   ArrayExpress; Q3TXS7; -.
DR   Bgee; Q3TXS7; -.
DR   Genevestigator; Q3TXS7; -.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR   InterPro; IPR016642; 26S_Psome_Rpn2.
DR   InterPro; IPR002015; APC_proteasome.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 2.
DR   Pfam; PF01851; PC_rep; 4.
DR   PIRSF; PIRSF015947; 26S_Psome_Rpn2; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein; Proteasome; Repeat.
FT   CHAIN         1    953       26S proteasome non-ATPase regulatory
FT                                subunit 1.
FT                                /FTId=PRO_0000231598.
FT   REPEAT      403    436       PC 1.
FT   REPEAT      441    474       PC 2.
FT   REPEAT      476    510       PC 3.
FT   REPEAT      511    545       PC 4.
FT   REPEAT      547    580       PC 5.
FT   REPEAT      581    616       PC 6.
FT   REPEAT      617    649       PC 7.
FT   REPEAT      651    685       PC 8.
FT   REPEAT      686    726       PC 9.
FT   REPEAT      729    761       PC 10.
FT   COMPBIAS    936    943       Poly-Glu.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      49     49       Phosphotyrosine (By similarity).
FT   MOD_RES     273    273       Phosphothreonine.
FT   MOD_RES     310    310       N6-acetyllysine (By similarity).
FT   MOD_RES     311    311       Phosphothreonine.
FT   MOD_RES     315    315       Phosphoserine.
SQ   SEQUENCE   953 AA;  105730 MW;  40A72A08CFC778E6 CRC64;
     MITSAAGIIS LLDEEEPQLK EFALHKLNAV VNDFWAEISE SVDKIEVLYE DEGFRSRQFA
     ALVASKVFYH LGAFEESLNY ALGAGDLFNV NDNSEYVETI IAKCIDHYTK QCVENADLPE
     GEKKPIDQRL EGIVNKMFQR CLDDHKYKQA IGIALETRRL DVFEKTILES NDVPGMLAYS
     LKLCMSLMQN KQFRNKVLRV LVKIYMNLEK PDFINVCQCL IFLDDPQAVS DILEKLVKED
     NLLMAYQICF DLYESASQQF LSSVIQNLRT VGTPIASVPG STNTGTVPGS EKDSDPMETE
     EKTASAVAGK TPDASPEPKD QTLKMIKILS GEMAIELHLQ FLIRNNNTDL MILKNTKDAV
     RNSVCHTATV IANSFMHCGT TSDQFLRDNL EWLARATNWA KFTATASLGV IHKGHEKEAL
     QLMATYLPKD TSPGSAYQEG GGLYALGLIH ANHGGDIIDY LLNQLKNASN DIVRHGGSLG
     LGLAAMGTAR QDVYDLLKTN LYQDDAVTGE AAGLALGLVM LGSKNAQAIE DMVGYAQETQ
     HEKILRGLAV GIALVMYGRM EEADALIESL CRDKDPILRR SGMYTVAMAY CGSGNNKAIR
     RLLHVAVSDV NDDVRRAAVE SLGFILFRTP EQCPSVVSLL SESYNPHVRY GAAMALGICC
     AGTGNKEAIN LLEPMTNDPV NYVRQGALIA SALIMIQQTE ITCPKVNQFR QLYSKVINDK
     HDDVMAKFGA ILAQGILDAG GHNVTISLQS RTGHTHMPSV VGVLVFTQFW FWFPLSHFLS
     LAYTPTCVIG LNKDLKMPKV QYKSNCKPST FAYPAPLEVP KEKEKEKVST AVLSITAKAK
     KKEKEKEKKE EEKMEVDEAE KKEEKEKKKE PEPNFQLLDN PARVMPAQLK VLSMTETCRY
     QPFKPLSIGG IIILKDTSED VEELVEPVAA HGPKIEEEEQ EPEPPEPFEY IDD
//
ID   VGLU1_MOUSE             Reviewed;         560 AA.
AC   Q3TXX4;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Vesicular glutamate transporter 1;
DE            Short=VGluT1;
DE   AltName: Full=Brain-specific Na(+)-dependent inorganic phosphate cotransporter;
DE   AltName: Full=Solute carrier family 17 member 7;
GN   Name=Slc17a7; Synonyms=Bnpi, Vglut1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   DEVELOPMENTAL STAGE.
RX   MEDLINE=22384312; PubMed=12384506; DOI=10.1074/jbc.M206738200;
RA   Schaefer M.K.-H., Varoqui H., Defamie N., Weihe E., Erickson J.D.;
RT   "Molecular cloning and functional identification of mouse vesicular
RT   glutamate transporter 3 and its expression in subsets of novel
RT   excitatory neurons.";
RL   J. Biol. Chem. 277:50734-50748(2002).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=15103023; DOI=10.1073/pnas.0401764101;
RA   Wojcik S.M., Rhee J.S., Herzog E., Sigler A., Jahn R., Takamori S.,
RA   Brose N., Rosenmund C.;
RT   "An essential role for vesicular glutamate transporter 1 (VGLUT1) in
RT   postnatal development and control of quantal size.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7158-7163(2004).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX   PubMed=15118123; DOI=10.1126/science.1097468;
RA   Fremeau R.T. Jr., Kam K., Qureshi T., Johnson J., Copenhagen D.R.,
RA   Storm-Mathisen J., Chaudhry F.A., Nicoll R.A., Edwards R.H.;
RT   "Vesicular glutamate transporters 1 and 2 target to functionally
RT   distinct synaptic release sites.";
RL   Science 304:1815-1819(2004).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16942593; DOI=10.1111/j.1471-4159.2006.04144.x;
RA   Herzog E., Takamori S., Jahn R., Brose N., Wojcik S.M.;
RT   "Synaptic and vesicular co-localization of the glutamate transporters
RT   VGLUT1 and VGLUT2 in the mouse hippocampus.";
RL   J. Neurochem. 99:1011-1018(2006).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=17611277; DOI=10.1523/JNEUROSCI.0815-07.2007;
RA   Johnson J., Fremeau R.T. Jr., Duncan J.L., Renteria R.C., Yang H.,
RA   Hua Z., Liu X., LaVail M.M., Edwards R.H., Copenhagen D.R.;
RT   "Vesicular glutamate transporter 1 is required for photoreceptor
RT   synaptic signaling but not for intrinsic visual functions.";
RL   J. Neurosci. 27:7245-7255(2007).
CC   -!- FUNCTION: Mediates the uptake of glutamate into synaptic vesicles
CC       at presynaptic nerve terminals of excitatory neural cells. May
CC       also mediate the transport of inorganic phosphate.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane. Membrane; Multi-pass membrane protein
CC       (Potential). Cell junction, synapse, synaptosome.
CC   -!- TISSUE SPECIFICITY: Expressed in the molecular layer of the
CC       cerebellum and in retina.
CC   -!- DEVELOPMENTAL STAGE: Expression in brain increases progressively
CC       from four days to adulthood.
CC   -!- DISRUPTION PHENOTYPE: Mice begin to die 3 weeks after birth. They
CC       exhibit a progressive neurological phenotype including blindness,
CC       loss of coordination and enhanced startle response. Glutamatergic
CC       neurotransmission is drastically reduced due to a decrease in the
CC       reserve pool of synaptic vesicles and reduced quantal size. Visual
CC       signaling from photoreceptors to retinal output neurons is
CC       impaired while photoentrainment and pupillary light responses
CC       remain intact.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       Sodium/anion cotransporter family. VGLUT subfamily.
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DR   EMBL; AK159064; BAE34790.1; -; mRNA.
DR   IPI; IPI00109153; -.
DR   RefSeq; NP_892038.2; NM_182993.2.
DR   UniGene; Mm.255631; -.
DR   ProteinModelPortal; Q3TXX4; -.
DR   STRING; Q3TXX4; -.
DR   PhosphoSite; Q3TXX4; -.
DR   PRIDE; Q3TXX4; -.
DR   Ensembl; ENSMUST00000085374; ENSMUSP00000082489; ENSMUSG00000070570.
DR   GeneID; 72961; -.
DR   KEGG; mmu:72961; -.
DR   UCSC; uc009gtx.1; mouse.
DR   CTD; 72961; -.
DR   MGI; MGI:1920211; Slc17a7.
DR   HOGENOM; HBG561587; -.
DR   HOVERGEN; HBG008834; -.
DR   InParanoid; Q3TXX4; -.
DR   OrthoDB; EOG4XWFXC; -.
DR   PhylomeDB; Q3TXX4; -.
DR   ArrayExpress; Q3TXX4; -.
DR   Bgee; Q3TXX4; -.
DR   Genevestigator; Q3TXX4; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0060076; C:excitatory synapse; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048786; C:presynaptic active zone; IDA:BHF-UCL.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019717; C:synaptosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0042137; P:sequestering of neurotransmitter; IMP:MGI.
DR   InterPro; IPR020846; Major_facilitator_SF.
DR   InterPro; IPR011701; MFS_1.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cytoplasmic vesicle; Ion transport; Membrane;
KW   Neurotransmitter transport; Sensory transduction; Sodium;
KW   Sodium transport; Symport; Synapse; Synaptosome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    560       Vesicular glutamate transporter 1.
FT                                /FTId=PRO_0000331612.
FT   TOPO_DOM      1     63       Cytoplasmic (Potential).
FT   TRANSMEM     64     84       Helical; (Potential).
FT   TOPO_DOM     85    116       Extracellular (Potential).
FT   TRANSMEM    117    137       Helical; (Potential).
FT   TOPO_DOM    138    140       Cytoplasmic (Potential).
FT   TRANSMEM    141    161       Helical; (Potential).
FT   TOPO_DOM    162    169       Extracellular (Potential).
FT   TRANSMEM    170    190       Helical; (Potential).
FT   TOPO_DOM    191    208       Cytoplasmic (Potential).
FT   TRANSMEM    209    229       Helical; (Potential).
FT   TOPO_DOM    230    236       Extracellular (Potential).
FT   TRANSMEM    237    257       Helical; (Potential).
FT   TOPO_DOM    258    302       Cytoplasmic (Potential).
FT   TRANSMEM    303    323       Helical; (Potential).
FT   TOPO_DOM    324    341       Extracellular (Potential).
FT   TRANSMEM    342    362       Helical; (Potential).
FT   TOPO_DOM    363    378       Cytoplasmic (Potential).
FT   TRANSMEM    379    399       Helical; (Potential).
FT   TOPO_DOM    400    401       Extracellular (Potential).
FT   TRANSMEM    402    422       Helical; (Potential).
FT   TOPO_DOM    423    435       Cytoplasmic (Potential).
FT   TRANSMEM    436    456       Helical; (Potential).
FT   TOPO_DOM    457    469       Extracellular (Potential).
FT   TRANSMEM    470    490       Helical; (Potential).
FT   TOPO_DOM    491    560       Cytoplasmic (Potential).
FT   COMPBIAS    530    556       Pro-rich.
SQ   SEQUENCE   560 AA;  61668 MW;  E9D6668F616A8304 CRC64;
     MEFRQEEFRK LAGRALGRLH RLLEKRQEGA ETLELSADGR PVTTHTRDPP VVDCTCFGLP
     RRYIIAIMSG LGFCISFGIR CNLGVAIVSM VNNSTTHRGG HVVVQKAQFN WDPETVGLIH
     GSFFWGYIVT QIPGGFICQK FAANRVFGFA IVATSTLNML IPSAARVHYG CVIFVRILQG
     LVEGVTYPAC HGIWSKWAPP LERSRLATTA FCGSYAGAVV AMPLAGVLVQ YSGWSSVFYV
     YGSFGIFWYL FWLLVSYESP ALHPSISEEE RKYIEDAIGE SAKLMNPVTK FNTPWRRFFT
     SMPVYAIIVA NFCRSWTFYL LLISQPAYFE EVFGFEISKV GLVSALPHLV MTIIVPIGGQ
     IADFLRSRHI MSTTNVRKLM NCGGFGMEAT LLLVVGYSHS KGVAISFLVL AVGFSGFAIS
     GFNVNHLDIA PRYASILMGI SNGVGTLSGM VCPIIVGAMT KHKTREEWQY VFLIASLVHY
     GGVIFYGVFA SGEKQPWAEQ EEMSEEKCGF VGHDQLAGSD ESEMEDEAEP PGAPPAPPPS
     YGATHSTVQP PRPPPPVRDY
//
ID   Q3TXY0_MOUSE            Unreviewed;       651 AA.
AC   Q3TXY0;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 38.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Crmp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK159049; BAE34784.1; -; mRNA.
DR   IPI; IPI00312527; -.
DR   UniGene; Mm.290995; -.
DR   ProteinModelPortal; Q3TXY0; -.
DR   STRING; Q3TXY0; -.
DR   Ensembl; ENSMUST00000114158; ENSMUSP00000109795; ENSMUSG00000029121.
DR   MGI; MGI:107793; Crmp1.
DR   HOVERGEN; HBG000806; -.
DR   InParanoid; Q3TXY0; -.
DR   OrthoDB; EOG48SGSP; -.
DR   ArrayExpress; Q3TXY0; -.
DR   Bgee; Q3TXY0; -.
DR   Genevestigator; Q3TXY0; -.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   InterPro; IPR006680; Amidohydro_1.
DR   InterPro; IPR011778; D-hydantoinase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Metalo_hydrolase; 2.
DR   TIGRFAMs; TIGR02033; D-hydantoinase; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   651 AA;  70245 MW;  3C5CA3BB626F1BFA CRC64;
     FAAVEGAYEN KTIDFDAYSV GRRGSARTPR SAGRPDAVGL PCPGGSEDTA SDVSEPSGSA
     VSSPGDRDDR PPALRIRCPA PRDLPLGRDN GQSDRLLIRG GRIINDDQSF YADVYLEDGL
     IKQIGENLIV PGGVKTIEAN GRMVIPGGID VNTYLQKPSQ GMTSADDFFQ GTKAALAGGT
     TMIIDHVVPE PGSSLLTSFE KWHEAADTKS CCDYSLHVDI TSWYDGVREE LEVLVQDKGV
     NSFQVYMAYK DLYQMSDSQL YEAFTFLKGL GAVILVHAEN GDLIAQEQKR ILEMGITGPE
     GHALSRPEEL EAEAVFRAIA IAGRINCPVY ITKVMSKSAA DIIALARKKG PLVFGEPIAA
     SLGTDGTHYW SKNWAKAAAF VTSPPLSPDP TTPDYLTSLL ACGDLQVTGS GHCPYSTAQK
     AVGKDNFTLI PEGVNGIEER MTVVWDKAVA TGKMDENQFV AVTSTNAAKI FNLYPRKGRI
     AVGSDADVVI WDPDKMKTIT AKSHKSTVEY NIFEGMECHG SPLVVISQGK IVFEDGNISV
     SKGMGRFIPR KPFPEHLYQR VRIRSKVFGL HSVSRGMYDG PVYEVPATPK HAAPAPSAKS
     SPSKHQPPPI RNLHQSNFSL SGAQIDDNNP RRTGHRIVAP PGGRSNITSL G
//
ID   Q3TXY2_MOUSE            Unreviewed;       271 AA.
AC   Q3TXY2;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   11-JAN-2011, entry version 37.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Tex264;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK159046; BAE34782.1; -; mRNA.
DR   IPI; IPI00651819; -.
DR   UniGene; Mm.22266; -.
DR   ProteinModelPortal; Q3TXY2; -.
DR   PRIDE; Q3TXY2; -.
DR   eggNOG; roNOG15878; -.
DR   HOVERGEN; HBG059535; -.
DR   Genevestigator; Q3TXY2; -.
DR   InterPro; IPR011256; Reg_factor_effector_bac.
DR   SUPFAM; SSF55136; Bac_reg_effector; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   271 AA;  29008 MW;  F80BD61670BA24A9 CRC64;
     MPDLLLLGLI GALTLLLLLT LLAFAGYSGL LTGVTVSAGS PPIRNITVAY KFHVGSYGDT
     GHLFTESCSI SPKLRSIAVY YDNPHTVPPE KCRCAVGSIL SEGEESPSPE LIHLYQKFGF
     KIFSFPAPSH VVIATFPYTT PISIWLAARR VHPALDTYIK ERKCRELAEA TDTQTDGTGA
     DTSDASSVSL DVRPGSRETS ATTLSPGAGN RGWDDGDNRS EHSYSESGAS GSSFEELDLE
     GEGPLGEPRL NPEAKLLGPP RELSTPERGE E
//
ID   F131B_MOUSE             Reviewed;         332 AA.
AC   Q3TY60; Q3TQE4; Q9D390;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 40.
DE   RecName: Full=Protein FAM131B;
GN   Name=Fam131b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Corpus striatum, Medulla oblongata, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-117, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-322, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-297 AND SER-322,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3TY60-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3TY60-2; Sequence=VSP_020994, VSP_020995;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the FAM131 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB31120.1; Type=Erroneous initiation;
CC       Sequence=BAC33149.1; Type=Erroneous initiation;
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DR   EMBL; AK047763; BAC33149.1; ALT_INIT; mRNA.
DR   EMBL; AK158869; BAE34703.1; -; mRNA.
DR   EMBL; AK163654; BAE37440.1; -; mRNA.
DR   EMBL; AK018206; BAB31120.1; ALT_INIT; mRNA.
DR   IPI; IPI00135561; -.
DR   IPI; IPI00762777; -.
DR   RefSeq; NP_001106798.1; NM_001113327.1.
DR   RefSeq; NP_083804.3; NM_029528.4.
DR   UniGene; Mm.234314; -.
DR   PhosphoSite; Q3TY60; -.
DR   PRIDE; Q3TY60; -.
DR   Ensembl; ENSMUST00000031891; ENSMUSP00000031891; ENSMUSG00000029861.
DR   Ensembl; ENSMUST00000095974; ENSMUSP00000093670; ENSMUSG00000029861.
DR   GeneID; 76156; -.
DR   KEGG; mmu:76156; -.
DR   UCSC; uc009bqu.1; mouse.
DR   UCSC; uc009bqv.1; mouse.
DR   CTD; 76156; -.
DR   MGI; MGI:1923406; Fam131b.
DR   GeneTree; ENSGT00390000015421; -.
DR   HOVERGEN; HBG081012; -.
DR   OMA; EVIAVDW; -.
DR   NextBio; 344683; -.
DR   ArrayExpress; Q3TY60; -.
DR   Bgee; Q3TY60; -.
DR   Genevestigator; Q3TY60; -.
DR   GermOnline; ENSMUSG00000029861; Mus musculus.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    332       Protein FAM131B.
FT                                /FTId=PRO_0000253033.
FT   COMPBIAS    283    286       Poly-Glu.
FT   MOD_RES      47     47       Phosphoserine.
FT   MOD_RES     114    114       Phosphoserine.
FT   MOD_RES     117    117       Phosphoserine.
FT   MOD_RES     297    297       Phosphoserine.
FT   MOD_RES     322    322       Phosphoserine.
FT   VAR_SEQ       1      1       M -> MGCIGSRTVGNEVIAVDWKGLKDVDQINM (in
FT                                isoform 2).
FT                                /FTId=VSP_020994.
FT   VAR_SEQ      19     30       Missing (in isoform 2).
FT                                /FTId=VSP_020995.
SQ   SEQUENCE   332 AA;  35958 MW;  4DD80BD549500783 CRC64;
     MDSTSSLHGS SLHRPSTEQT RTDFSWDGIN LSMEDTTSIL PKLKRNSNAY GIGALAKSSF
     SGISRSMKDH VTKPTAMGQG RVAHMIEWQG WGKAPTIQPQ HSHEAVRRDT DAYSDLSDGE
     KEARFLAGVM EQFAISEATL MAWSSMDGED MSVNSTQEPL DCNYSDNYQE LMESQDALAQ
     APMDGWPHSY VSQGMYCLGS SDAWEASDQS LIASPATGSY LGPAFDDSQP SLHDMGPSQP
     ASGYSAQEPP PLLGVDTDWA SEVGGVELAR GPVEEEKRPL APEEEEDAGC RDLESLSPRE
     DPEMSTALSR KVSDVTSSGV QSFDEEEGDA NN
//
ID   AIFM3_MOUSE             Reviewed;         605 AA.
AC   Q3TY86; Q0VBD6; Q4VAA4; Q8BWV0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Apoptosis-inducing factor 3;
DE            EC=1.-.-.-;
DE   AltName: Full=Apoptosis-inducing factor-like protein;
GN   Name=Aifm3; Synonyms=Aifl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=FVB/N; TISSUE=Brain, and Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Induces apoptosis through a caspase dependent pathway.
CC       Reduces mitochondrial membrane potential (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Note=Does not translocate to
CC       the nucleus upon induction of apoptosis (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3TY86-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3TY86-2; Sequence=VSP_021306;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q3TY86-3; Sequence=VSP_021304, VSP_021305;
CC   -!- DOMAIN: The Rieske domain induces apoptosis (By similarity).
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
CC   -!- SIMILARITY: Contains 1 Rieske domain.
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DR   EMBL; AK049928; BAC33988.1; -; mRNA.
DR   EMBL; AK158809; BAE34677.1; -; mRNA.
DR   EMBL; BC096476; AAH96476.1; -; mRNA.
DR   EMBL; BC120685; AAI20686.1; -; mRNA.
DR   IPI; IPI00312374; -.
DR   IPI; IPI00761718; -.
DR   IPI; IPI00798537; -.
DR   RefSeq; NP_780387.2; NM_175178.3.
DR   UniGene; Mm.40038; -.
DR   ProteinModelPortal; Q3TY86; -.
DR   SMR; Q3TY86; 69-172, 195-593.
DR   PRIDE; Q3TY86; -.
DR   Ensembl; ENSMUST00000023448; ENSMUSP00000023448; ENSMUSG00000022763.
DR   Ensembl; ENSMUST00000100128; ENSMUSP00000097704; ENSMUSG00000022763.
DR   Ensembl; ENSMUST00000115685; ENSMUSP00000111349; ENSMUSG00000022763.
DR   GeneID; 72168; -.
DR   KEGG; mmu:72168; -.
DR   UCSC; uc007ykw.1; mouse.
DR   UCSC; uc007ykx.1; mouse.
DR   UCSC; uc007yky.1; mouse.
DR   CTD; 72168; -.
DR   MGI; MGI:1919418; Aifm3.
DR   eggNOG; roNOG13392; -.
DR   GeneTree; ENSGT00530000063416; -.
DR   HOGENOM; HBG644911; -.
DR   HOVERGEN; HBG052926; -.
DR   InParanoid; Q3TY86; -.
DR   OMA; SRGRVRC; -.
DR   OrthoDB; EOG4STS46; -.
DR   NextBio; 335607; -.
DR   ArrayExpress; Q3TY86; -.
DR   Bgee; Q3TY86; -.
DR   Genevestigator; Q3TY86; -.
DR   GermOnline; ENSMUSG00000022763; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:HGNC.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0008656; F:caspase activator activity; ISS:HGNC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008635; P:activation of caspase activity by cytochrome c; ISS:HGNC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006917; P:induction of apoptosis; ISS:HGNC.
DR   GO; GO:0051882; P:mitochondrial depolarization; ISS:HGNC.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD-bd.
DR   InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   Gene3D; G3DSA:3.30.390.30; Pyr_redox_dim; 1.
DR   Gene3D; G3DSA:2.102.10.10; Rieske_reg; 1.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF55424; FAD/NAD-linked_reductase_dimer; 1.
DR   SUPFAM; SSF50022; Rieske_dom; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   2: Evidence at transcript level;
KW   2Fe-2S; Alternative splicing; Apoptosis; Electron transport; FAD;
KW   Flavoprotein; Iron; Iron-sulfur; Metal-binding; Mitochondrion;
KW   Oxidoreductase; Transport.
FT   CHAIN         1    605       Apoptosis-inducing factor 3.
FT                                /FTId=PRO_0000255661.
FT   DOMAIN       70    165       Rieske.
FT   NP_BIND     201    205       FAD (Potential).
FT   METAL       109    109       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL       111    111       Iron-sulfur (2Fe-2S); via pros nitrogen
FT                                (By similarity).
FT   METAL       128    128       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL       131    131       Iron-sulfur (2Fe-2S); via pros nitrogen
FT                                (By similarity).
FT   BINDING     235    235       FAD (Potential).
FT   BINDING     240    240       FAD (Potential).
FT   BINDING     270    270       FAD; via amide nitrogen and carbonyl
FT                                oxygen (Potential).
FT   BINDING     467    467       FAD (Potential).
FT   BINDING     514    514       FAD; via carbonyl oxygen (Potential).
FT   VAR_SEQ     494    500       RVAAQNM -> MASPEAS (in isoform 3).
FT                                /FTId=VSP_021304.
FT   VAR_SEQ     501    605       Missing (in isoform 3).
FT                                /FTId=VSP_021305.
FT   VAR_SEQ     587    593       Missing (in isoform 2).
FT                                /FTId=VSP_021306.
FT   CONFLICT    138    138       S -> T (in Ref. 1; BAC33988).
SQ   SEQUENCE   605 AA;  66792 MW;  D4811CB2B2CD0739 CRC64;
     MGGCFSKPKP VELKIEVVLP EKERGKEELS ASGKGSPRGY QGNGTARHFH AEERLPTPQP
     YPSPQDCVEA TVCHVKDLEN GQMREVELGW GKVLLVKDNG EFHALGHKCP HYGAPLVKGV
     LSRGRVRCPW HGACFNISTG DLEDFPGLDS LHKFQVKIEK EKVTIRASKQ ALQLQRRTKV
     MAKCISPSAG HSSSTNVLIV GAGAAGLVCA ETLRQEGFSD RIVLCTLDRH LPYDRAKLSK
     SLDAQPEQLA LRPKEFFRAY GIEMLTEAQV VTVDVRNKKV VFKDGFKLEY SKLLLAPGSS
     PKTLTCKGKD VENVFTIRTP EDANRVLRLA RGRNAVVVGA GFLGMEVAAY LTEKAHSVSV
     VELEETPFRR FLGERVGRAL MKMFENNRVK FYMQTEVSEL RAQEGKLQEV VLKSSKVLRA
     DVCVLGIGAV PATGFLRQSG IGLDSRGFIP VNKMMQTNVP GVFAAGDAVT FPLAWRNNRK
     VNIPHWQMAH AQGRVAAQNM LAQEAEINTV PYLWTAMFGK SLRYAGYGEG FDDVIIQGDL
     EELKFVAFYT KSDEVIAVAS MNYDPIVSKV AEVLASGRAI RKREVELFML HSKTGDMSWL
     TGKGS
//
ID   Q3TY88_MOUSE            Unreviewed;       983 AA.
AC   Q3TY88;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Trip12;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK158807; BAE34675.1; -; mRNA.
DR   IPI; IPI00623570; -.
DR   RefSeq; NP_598736.4; NM_133975.4.
DR   UniGene; Mm.209265; -.
DR   ProteinModelPortal; Q3TY88; -.
DR   STRING; Q3TY88; -.
DR   Ensembl; ENSMUST00000027421; ENSMUSP00000027421; ENSMUSG00000026219.
DR   GeneID; 14897; -.
DR   KEGG; mmu:14897; -.
DR   CTD; 14897; -.
DR   MGI; MGI:1309481; Trip12.
DR   InParanoid; Q3TY88; -.
DR   NextBio; 287187; -.
DR   ArrayExpress; Q3TY88; -.
DR   Bgee; Q3TY88; -.
DR   Genevestigator; Q3TY88; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR004170; WWE-dom.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 4.
DR   Pfam; PF02825; WWE; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50918; WWE; 1.
PE   2: Evidence at transcript level;
FT   NON_TER     983    983
SQ   SEQUENCE   983 AA;  106516 MW;  1F5D851DCBCADE1A CRC64;
     MSNRPNNNPG GSLRRSQRNT AGAQPQDDSI GGRSCSSSSA VIVPQPEDPD RANTSERQKT
     GQVPKKDNSR GVKRSASPDY NRTNSPSSAK KPRAFQHIES FSETNKPHSK SKKRHLDQEQ
     QLKSAQLPST SKAHTRKSVA AGSSRNQKRK RTESSCVKSG SGSESTGAEE RSAKPIKLAS
     KSATSAKAGC STITDSSSAA STSSSSSAIA SASSTVPAGA RVKQGKDQNK ARRSRSASSP
     SPRRSSREKE QSKTGGSSKF DWAARFSPKV SLPKTKLSLP GSSKSETSKP GPSGLQAKLA
     SLRKSTKKRS ESPPAELPSL RRSTRQKTTG SCASTSRRGS GLGKRGAAEA RRQEKMADPE
     SNQETVNSSA ARTDEAPQGA AASSSVAGAV GMTTSGESES DDSEMGRLQA LLEARGLPPH
     LFGPLGPRMS QLFHRTIGSG ASSKAQQLLQ GLQASDESQQ LQAVIEMCQL LVMGNEETLG
     GFPVKSVVPA LITLLQMEHN FDIMNHACRA LTYMMEALPR SSAVVVDAIP VFLEKLQVIQ
     CIDVAEQALT ALEMLSRRHS KAILQAGGLA DCLLYLEFFS INAQRNALAI AANCCQSITP
     DEFHFVADSL PLLTQRLTHQ DKKSVESTCL CFARLVDNFQ HEENLLQQVA SKDLLTNVQQ
     LLVVTPPILS SGMFIMVVRM FSLMCSNCPT LAVQLMKQNI AETLHFLLCG ASNGSCQEQI
     DLVPRSPQEL YELTSLICEL MPCLPKEGIF AVDTMLKKGN AQNTDGAIWQ WRDDRGLWHP
     YNRIDSRIIE AAHQVGEDEI SLSTLGRVYT IDFNSMQQIN EDTGTARAIQ RKPNPLANSN
     TSGYSELKKD DARAQLMKED PELAKSFIKT LFGVLYEVYS SSAGPAVRHK CLRAILRIIY
     FADAELLKDV LKNHAVSSHI ASMLSSQDLK IVVGALQMAE ILMQKLPDIF SVYFRREGVM
     HQVKHLAESE SLLTSPPKAC TNG
//
ID   LMTK2_MOUSE             Reviewed;        1471 AA.
AC   Q3TYD6; Q6PDK6; Q6ZPY9; Q8CA34;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=Serine/threonine-protein kinase LMTK2;
DE            EC=2.7.11.1;
DE   AltName: Full=Brain-enriched kinase;
DE   AltName: Full=Lemur tyrosine kinase 2;
DE   Flags: Precursor;
GN   Name=Lmtk2; Synonyms=Brek, Kiaa1079;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-632 AND 1263-1471.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 410-1471.
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1253-1471.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY, PHOSPHORYLATION, CHARACTERIZATION, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=15005709; DOI=10.1111/j.1356-9597.2004.00714.x;
RA   Kawa S., Fujimoto J., Tezuka T., Nakazawa T., Yamamoto T.;
RT   "Involvement of BREK, a serine/threonine kinase enriched in brain, in
RT   NGF signalling.";
RL   Genes Cells 9:219-232(2004).
CC   -!- FUNCTION: Phosphorylates PPP1C, phosphorylase b and CFTR (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts with PPP1C and inhibitor-2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- TISSUE SPECIFICITY: Mainly expressed in brain, especially in the
CC       olfactory bulb, olfactory tubercle, hippocampus, striatum,
CC       cerebellum and cerebral cortex. Weakly expressed in skeletal
CC       muscle and not expressed in liver.
CC   -!- DEVELOPMENTAL STAGE: Expression observed during all tested stages
CC       from embryonic day 18 (E18) to postnatal week 6, but it was
CC       especially high during the early postnatal stage (postnatal weeks
CC       0-2).
CC   -!- PTM: Autophosphorylated. Phosphorylated (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AK039738; BAC30433.1; -; mRNA.
DR   EMBL; AK158724; BAE34627.1; -; mRNA.
DR   EMBL; AK129279; BAC98089.2; -; mRNA.
DR   EMBL; BC058653; AAH58653.1; -; mRNA.
DR   IPI; IPI00135746; -.
DR   UniGene; Mm.288726; -.
DR   HSSP; P06213; 2AUH.
DR   ProteinModelPortal; Q3TYD6; -.
DR   SMR; Q3TYD6; 128-407.
DR   IntAct; Q3TYD6; 1.
DR   STRING; Q3TYD6; -.
DR   PhosphoSite; Q3TYD6; -.
DR   PRIDE; Q3TYD6; -.
DR   Ensembl; ENSMUST00000041804; ENSMUSP00000048238; ENSMUSG00000038970.
DR   UCSC; uc009alg.1; mouse.
DR   MGI; MGI:3036247; Lmtk2.
DR   eggNOG; roNOG08518; -.
DR   GeneTree; ENSGT00600000084075; -.
DR   HOGENOM; HBG446247; -.
DR   HOVERGEN; HBG081920; -.
DR   InParanoid; Q3TYD6; -.
DR   OrthoDB; EOG45755T; -.
DR   BRENDA; 2.7.11.1; 244.
DR   ArrayExpress; Q3TYD6; -.
DR   Bgee; Q3TYD6; -.
DR   CleanEx; MM_LMTK2; -.
DR   Genevestigator; Q3TYD6; -.
DR   GermOnline; ENSMUSG00000038970; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Glycoprotein; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Signal; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     26       Potential.
FT   CHAIN        27   1471       Serine/threonine-protein kinase LMTK2.
FT                                /FTId=PRO_0000259459.
FT   TRANSMEM     42     62       Helical; (Potential).
FT   DOMAIN      136    406       Protein kinase.
FT   NP_BIND     142    150       ATP (By similarity).
FT   ACT_SITE    264    264       Proton acceptor (By similarity).
FT   BINDING     167    167       ATP (By similarity).
FT   MOD_RES     924    924       Phosphoserine (By similarity).
FT   MOD_RES    1274   1274       Phosphoserine (By similarity).
FT   MOD_RES    1276   1276       Phosphoserine (By similarity).
FT   MOD_RES    1277   1277       Phosphoserine (By similarity).
FT   MOD_RES    1279   1279       Phosphoserine (By similarity).
FT   CARBOHYD    111    111       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    351    351       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    543    543       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1078   1078       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    421    421       L -> F (in Ref. 2; BAC98089).
SQ   SEQUENCE   1471 AA;  160474 MW;  F320C98D55AFD297 CRC64;
     MPGPPASPPP PMLLLLLLLT VGCARAAPLP QTGAGEVPVV EVPSLFVILS VCSLLILIVL
     IANCVSCCKD PEIDFKEFED NFDDEIDFTP PAEDTPSIQS PAEVFTLSVP NISLPAPSQF
     QASVEGLKSQ VARHSLNYIQ EIGSGWFGKV LLGETYTGTS VARVIVKELK VSASPKEQDT
     FLKSGEPYYI LQHPNVLQCV GQCVEAIPYL LVFEFCDLGD LKAYLHNEQE HVRGDSQTML
     LQRMACEIAA GLAAMHKLHF LHSDLALRNC YLTSDLNVKV GDYGIGFSRY KEDYIETDDK
     KVFPLRWTAP ELVTSFQDRL LTADQTKYSN IWSLGVTLWE LFNNAAQPYA NLSDLDVLNQ
     VIRERDMKLP KPQLEQPYSD RWYEVLQFCW LPPDKRPAAE DVHRLLTYLR MQSQRDSEVD
     LEQQWTALKP DTNSRDASSS AAFPILDHFA RDRLGREMEE VLTVTETSQG LSFEYVWEAA
     KHDHFDEQGR GHPDEALSYS SMFFPVEVFE NSLSDPGPGK QDDSGQEVPV RAPGVVPVFD
     AHNLSVGSDY YIQLEEKSSS NLGLDPPALL TTEVDKLERA GAEEPRTEED FFQSSAHPKE
     ASSTEDSRAT SIPGSPFNLF SDLDKADDLP SHQKIFDLME LNGVQADFKP AILSSSLDDP
     KDTCQSDKEK PHKLLDQGPL CLSESLLHQD HFDPLSVQEL SENFLFLQEK NLLKGSLTTK
     EQVSDLQTEL KNAGFTSALL ESPQRGSESS ELEFLENTLD FPLSQGDTRG QNEGAGVRRH
     SGTSPQASPA LLTEEGSPTA PTDPILKPEE TKSFRDVRVP EDSICLELGP DPVTVGVEIP
     ATDAKTLDGG NRPPDVTCQS KEALSLTNRH PILVNDITAQ GSVESCLPES RQDLQNEPFS
     EDPLSVSSLE KHSEAAETLN QLNSKAAPED AALASALSSD STSQDSLLED SLSTPIPTSE
     QSVETPDSLD SVDVREALLE SLGSHTPRKL LPPDKPADSG YETENLESPE WTLHPAPEGT
     ADSDAAAAGD SGHSSLPPNP VIVISDAGDG HRGAEGPPQS FTLGPQSSYR DSAYFSDNDS
     EPDKKPEEVP GTSANALVLV KGQSPPESVV PEESSDVREG CLEAPQDKPD QSRVSTLQNS
     CHSELQETLQ PTPADASRES CPVNDEASSP LSLLNSEPSS CDDLDTQEDR PCTLASTGTN
     TNELLAYMSS TLDKSLPSHL ESSKLKEPDI EGKYLGKLCV SGMLDLSEDG MDADEEDENS
     DDSDEDLRAF NLHSLSSESE DDTEHPVPII VSNDDGRHLR SLLKPSAAEA IEQLPEDWKK
     EKKAVTFFDD VTVYLFDQET PTKELGHCGG EAHGPGPSSP AASSSSPYLG RCMNSESSTD
     EEGGGFEWDD DFSPDPFMSK TTSLLGSKPS LQTSKYFSPP PPARSAEQSW PHVSPCSRFS
     ISPANIASFS LTHLTDSDIE QGGSSEDGDK D
//
ID   Q3TYK3_MOUSE            Unreviewed;       391 AA.
AC   Q3TYK3;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Nuclear factor 1;
GN   Name=Nfix;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Recognizes and binds the palindromic sequence 5'-
CC       TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in
CC       the origin of replication of adenovirus type 2. These proteins are
CC       individually capable of activating transcription and replication
CC       (By similarity).
CC   -!- SUBUNIT: Binds DNA as a homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the CTF/NF-I family.
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DR   EMBL; AK158568; BAE34560.1; -; mRNA.
DR   IPI; IPI00831062; -.
DR   RefSeq; NP_001075450.1; NM_001081981.1.
DR   UniGene; Mm.9394; -.
DR   STRING; Q3TYK3; -.
DR   PRIDE; Q3TYK3; -.
DR   Ensembl; ENSMUST00000109762; ENSMUSP00000105384; ENSMUSG00000001911.
DR   GeneID; 18032; -.
DR   KEGG; mmu:18032; -.
DR   UCSC; uc009mnd.1; mouse.
DR   CTD; 18032; -.
DR   MGI; MGI:97311; Nfix.
DR   GeneTree; ENSGT00390000009905; -.
DR   HOVERGEN; HBG006561; -.
DR   NextBio; 293113; -.
DR   ArrayExpress; Q3TYK3; -.
DR   Bgee; Q3TYK3; -.
DR   Genevestigator; Q3TYK3; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0016563; F:transcription activator activity; IDA:MGI.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   InterPro; IPR000647; CTF/NFI.
DR   InterPro; IPR020604; CTF/NFI_DNA-bd-dom.
DR   InterPro; IPR019739; CTF/NFI_DNA-bd_CS.
DR   InterPro; IPR019548; CTF/NFI_DNA-bd_N.
DR   InterPro; IPR003619; MAD_homology1_Dwarfin-type.
DR   PANTHER; PTHR11492; CTF_NFI; 1.
DR   Pfam; PF00859; CTF_NFI; 2.
DR   Pfam; PF03165; MH1; 1.
DR   Pfam; PF10524; NfI_DNAbd_pre-N; 1.
DR   SMART; SM00523; DWA; 1.
DR   PROSITE; PS00349; CTF_NFI_1; 1.
DR   PROSITE; PS51080; CTF_NFI_2; 1.
PE   2: Evidence at transcript level;
KW   Activator; DNA replication; DNA-binding; Nucleus; Transcription;
KW   Transcription regulation.
SQ   SEQUENCE   391 AA;  43594 MW;  9856B95AD96ACAE0 CRC64;
     MDEFHPFIEA LLPHVRAFSY TWFNLQARKR KYFKKHEKRM SKDEERAVKD ELLGEKPEIK
     QKWASRLLAK LRKDIRPEFR EDFVLTITGK KPPCCVLSNP DQKGKIRRID CLRQADKVWR
     LDLVMVILFK GIPLESTDGE RLYKSPQCSN PGLCVQPHHI GVTIKELDLY LAYFVHTPES
     GQSDSSNQQG DADIKPLPNG HLSFQDCFVT SGVWNVTELV RVSQTPVATA SGPNFSLADL
     ESPSYYNINQ VTLGRRSITS PPSTSTKRPK SIDDSEMESP VDDVFYPGTG RSPAAGSSQS
     SGWPNDVDAG SPRATASALH FPSTSIIQQS SPYFTHPTIR YHHHHGQDSL KEFVQFVCSD
     GSGQATGQHS QRQAPPLPTG LSASDPGTAT F
//
ID   TM88B_MOUSE             Reviewed;         173 AA.
AC   Q3TYP4; A2AD92;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   08-MAR-2011, entry version 40.
DE   RecName: Full=Transmembrane protein 88B;
GN   Name=Tmem88b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the TMEM88 family.
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DR   EMBL; AK158459; BAE34518.1; -; mRNA.
DR   EMBL; AL670236; CAM18385.1; -; Genomic_DNA.
DR   EMBL; CH466594; EDL15031.1; -; Genomic_DNA.
DR   EMBL; BC147318; AAI47319.1; -; mRNA.
DR   EMBL; BC147319; AAI47320.1; -; mRNA.
DR   IPI; IPI00648446; -.
DR   RefSeq; NP_001028566.2; NM_001033394.3.
DR   UniGene; Mm.384382; -.
DR   ProteinModelPortal; Q3TYP4; -.
DR   PRIDE; Q3TYP4; -.
DR   Ensembl; ENSMUST00000097742; ENSMUSP00000095349; ENSMUSG00000073680.
DR   GeneID; 320587; -.
DR   KEGG; mmu:320587; -.
DR   UCSC; uc008wes.1; mouse.
DR   CTD; 320587; -.
DR   MGI; MGI:2444329; Tmem88b.
DR   eggNOG; maNOG21610; -.
DR   GeneTree; ENSGT00510000047877; -.
DR   InParanoid; Q3TYP4; -.
DR   OMA; ASDTAPM; -.
DR   OrthoDB; EOG4RR6K1; -.
DR   NextBio; 397017; -.
DR   ArrayExpress; Q3TYP4; -.
DR   Bgee; Q3TYP4; -.
DR   Genevestigator; Q3TYP4; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    173       Transmembrane protein 88B.
FT                                /FTId=PRO_0000346447.
FT   TRANSMEM     31     51       Helical; (Potential).
FT   TRANSMEM     53     73       Helical; (Potential).
FT   TRANSMEM    107    127       Helical; (Potential).
FT   CONFLICT     45     45       G -> R (in Ref. 1; BAE34518, 3; EDL15031
FT                                and 4; AAI47319/AAI47320).
SQ   SEQUENCE   173 AA;  18549 MW;  B17F48C90F424114 CRC64;
     MSEQERETEE DEGVASDTAP MLPRRRPTDY HISVLAPILA TRGLGTLVLS GRALVGFLLH
     LLLPGTVFLL VLLPAAAVVY LGFLCHSRVH PAPGPRCRAL LSDRGSAALI VFGLLSLPPL
     VVLAAAARSL LVRRLRPALP DPARTPAPRR PPRSSGDLAD GHPDEDKQLC AWV
//
ID   Q3TYX4_MOUSE            Unreviewed;      1003 AA.
AC   Q3TYX4;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 50.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Mcc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
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DR   EMBL; AK158266; BAE34437.1; -; mRNA.
DR   IPI; IPI00129927; -.
DR   RefSeq; NP_001078842.1; NM_001085373.1.
DR   UniGene; Mm.312511; -.
DR   UniGene; Mm.427116; -.
DR   ProteinModelPortal; Q3TYX4; -.
DR   SMR; Q3TYX4; 19-89.
DR   STRING; Q3TYX4; -.
DR   PhosphoSite; Q3TYX4; -.
DR   Ensembl; ENSMUST00000089874; ENSMUSP00000087318; ENSMUSG00000071856.
DR   GeneID; 328949; -.
DR   KEGG; mmu:328949; -.
DR   UCSC; uc008euy.1; mouse.
DR   CTD; 328949; -.
DR   MGI; MGI:96930; Mcc.
DR   eggNOG; roNOG10653; -.
DR   GeneTree; ENSGT00530000063974; -.
DR   HOGENOM; HBG357807; -.
DR   HOVERGEN; HBG004762; -.
DR   InParanoid; Q3TYX4; -.
DR   OrthoDB; EOG4ZS92H; -.
DR   NextBio; 398498; -.
DR   ArrayExpress; Q3TYX4; -.
DR   Bgee; Q3TYX4; -.
DR   Genevestigator; Q3TYX4; -.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR019536; USH1C-bd_PDZ_domain.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF10506; MCC-bdg_PDZ; 3.
DR   SMART; SM00054; EFh; 2.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   1: Evidence at protein level;
KW   Calcium.
SQ   SEQUENCE   1003 AA;  112021 MW;  FAA665DFA287CCF3 CRC64;
     MAAASACNSS GGSSDTSSTG EEERLRRLFQ TCDGDGDGYI SRNDLLMVCR QLNMEESVAE
     IMNQLGSDEN GKISFQDFTR CHTQLVREIR KEEGDLSMKS DMSSTKRLSE RITSWPTSSD
     NSLGALSAAR ESWEDDSGAR DLQSPDLQSQ RPLQKLLEYG GSSLPQQAVL HKLLTHAPNF
     GTSTGGSYLE LASTLHLAAL ASLKGDIVEL NKRLQQTERE RDLLEKKLAK AQCEQSHLMR
     EHEDVQERTT LRYEERITEL HSIIAELNKK IDRLQGTTIR EEDEYSELRS ELSQSQQEVN
     EDSRSVDQDQ TSVSIPENQS TMVTADMDNC SDLNSELQRV LTGLESVVCG RKKSSCSLSV
     ADVDRHIEQL TTASEHCDLA IKTVEEIEGV LGRDLYPNLA EERSRWEKEL AGLREENESL
     TAMLCSKEEE LNRTKATMNA IREERDRLRR RVRELQTRLQ SVQATGPSSP GRLTPANRPI
     NPSTGELSTS SSSNDIPIAK IAERVKLSET RSESSSSDRP VLGSEISSIG VSSSVAEHLA
     HSLQDCSNIQ EIFQTLYSHG SAISESKIRE FEVETERLNS RIEHLKSQND LLTITLEECK
     SNAERMSMLV GKYESNATAL RLALQYSEQC IEAYELLLAL AESEQSLILG QFRAAGVGSS
     PGDQSGDENI TQMLKRAHDC RKTAENAAKA LLMKLDGSCG GAFAVAGCSV QPWESLSSNS
     HTSTTSSTAS SCDTEFTKED EQRLKDYIQQ LKNDRAAVKL TMLELESIHI DPLSYDVKPR
     GDSQRLDLEN AVLMQELMAM KEEMAELKAQ LYLLEKEKKA LELKLSTREA QEQAYLVHIE
     HLKSEVEEQK EQRTRSLSST SSSGKEKPGK ECADAASPAL SLAELRTNSD SELATEFANA
     IRREKKLKAR VQELVSALER LTKSSEIRHQ QSAEFVNDLK RANSNLVAAY EKAKKKHQNK
     LKKLESQMMA MVERHETQVR MLKQRIALLE EENSRPHTNE TSL
//
ID   Q3TZ77_MOUSE            Unreviewed;       263 AA.
AC   Q3TZ77;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 39.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Ephb3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; AK158043; BAE34333.1; -; mRNA.
DR   IPI; IPI00654071; -.
DR   UniGene; Mm.6972; -.
DR   ProteinModelPortal; Q3TZ77; -.
DR   SMR; Q3TZ77; 1-147.
DR   STRING; Q3TZ77; -.
DR   PRIDE; Q3TZ77; -.
DR   Ensembl; ENSMUST00000085925; ENSMUSP00000083089; ENSMUSG00000005958.
DR   MGI; MGI:104770; Ephb3.
DR   GeneTree; ENSGT00570000078802; -.
DR   ArrayExpress; Q3TZ77; -.
DR   Bgee; Q3TZ77; -.
DR   Genevestigator; Q3TZ77; -.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0008046; F:axon guidance receptor activity; IDA:MGI.
DR   GO; GO:0005005; F:transmembrane-ephrin receptor activity; TAS:MGI.
DR   GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IDA:MGI.
DR   GO; GO:0031290; P:retinal ganglion cell axon guidance; IDA:MGI.
DR   InterPro; IPR001090; Ephrin_rcpt_lig-bd.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   Pfam; PF01404; Ephrin_lbd; 1.
DR   SMART; SM00615; EPH_lbd; 1.
DR   SUPFAM; SSF49785; Gal_bind_like; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   263 AA;  28871 MW;  5192D66458ED4E1C CRC64;
     MDTKWVTSEL AWTSHPESGW EEVSGYDEAM NPIRTYQVCN VRESSQNNWL RTGFIWRREV
     QRVYVELKFT VRDCNSIPNI PGSCKETFNL FYYEADSDVA SASSPFWMEN PYVKVDTIAP
     DESFSRLDAG RVNTKASHSS PRPSRGLSPL RWSLPPAPAS LTLWRSLYHS SSTAMATGSG
     WCPSVPAPAL LAMSQPPRSP SAVPVLLGVT KQSKEKGPAS PVPPIAAPPR RLPASAPAII
     TSTVQTQTRP TAPAPRCHLH PGV
//
ID   Q3TZN6_MOUSE            Unreviewed;       642 AA.
AC   Q3TZN6;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 36.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Spnb2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Parthenogenote;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Parthenogenote;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Parthenogenote;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Parthenogenote;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Parthenogenote;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Parthenogenote;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Parthenogenote;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Parthenogenote;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK157727; BAE34172.1; -; mRNA.
DR   IPI; IPI00121892; -.
DR   RefSeq; NP_033286.2; NM_009260.2.
DR   RefSeq; NP_787030.2; NM_175836.2.
DR   UniGene; Mm.123110; -.
DR   UniGene; Mm.466085; -.
DR   ProteinModelPortal; Q3TZN6; -.
DR   STRING; Q3TZN6; -.
DR   Ensembl; ENSMUST00000102838; ENSMUSP00000099902; ENSMUSG00000020315.
DR   GeneID; 20742; -.
DR   KEGG; mmu:20742; -.
DR   CTD; 20742; -.
DR   MGI; MGI:98388; Spnb2.
DR   HOVERGEN; HBG099000; -.
DR   ArrayExpress; Q3TZN6; -.
DR   Bgee; Q3TZN6; -.
DR   Genevestigator; Q3TZN6; -.
DR   GO; GO:0032437; C:cuticular plate; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0007182; P:common-partner SMAD protein phosphorylation; IDA:MGI.
DR   GO; GO:0007184; P:SMAD protein import into nucleus; IDA:MGI.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 2.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF00435; Spectrin; 3.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00150; SPEC; 3.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
PE   2: Evidence at transcript level;
KW   Actin-binding; Repeat.
FT   NON_TER     642    642
SQ   SEQUENCE   642 AA;  75190 MW;  C0EE132C28EA6DFC CRC64;
     MELQRTSSIS GPLSPAYTGQ VPYNYNQLEG RFKQLQDERE AVQKKTFTKW VNSHLARVSC
     RITDLYTDLR DGRMLIKLLE VLSGERLPKP TKGRMRIHCL ENVDKALQFL KEQRVHLENM
     GSHDIVDGNH RLTLGLIWTI ILRFQIQDIS VETEDNKEKK SAKDALLLWC QMKTAGYPNV
     NIHNFTTSWR DGMAFNALIH KHRPDLIDFD KLKKSNAHYN LQNAFNLAEQ HLGLTKLLDP
     EDISVDHPDE KSIITYVVTY YHYFSKMKAL AVEGKRIGKV LDNAIETEKM IEKYESLASD
     LLEWIEQTII ILNNRKFANS LVGVQQQLQA FNTYRTVEKP PKFTEKGNLE VLLFTIQSKM
     RANNQKVYMP REGKLISDIN KAWERLEKAE HERELALRNE LIRQEKLEQL ARRFDRKAAM
     RETWLSENQR LVSQDNFGFD LPAVEAATKK HEAIETDIAA YEERVQAVVA VARELEAENY
     HDIKRITARK DNVIRLWEYL LELLRARRQR LEMNLGLQKI FQEMLYIMDW MDEMKVLLLS
     QDYGKHLLGV EDLLQKHALV EADIAIQAER VRGVNASAQK FATDGEGYKP CDPQVIRDRV
     AHMEFCYQEL CQLAAERRAR LEESRRLWKF FWEMAEEEGW IR
//
ID   Q3TZT4_MOUSE            Unreviewed;       420 AA.
AC   Q3TZT4;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-FEB-2011, entry version 37.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Inpp5a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK157558; BAE34123.1; -; mRNA.
DR   IPI; IPI00653599; -.
DR   UniGene; Mm.28308; -.
DR   ProteinModelPortal; Q3TZT4; -.
DR   STRING; Q3TZT4; -.
DR   PRIDE; Q3TZT4; -.
DR   Ensembl; ENSMUST00000097975; ENSMUSP00000095589; ENSMUSG00000025477.
DR   UCSC; uc009kfs.1; mouse.
DR   MGI; MGI:2686961; Inpp5a.
DR   eggNOG; roNOG08795; -.
DR   GeneTree; ENSGT00390000015226; -.
DR   HOVERGEN; HBG006102; -.
DR   ArrayExpress; Q3TZT4; -.
DR   Bgee; Q3TZT4; -.
DR   Genevestigator; Q3TZT4; -.
DR   GO; GO:0004437; F:inositol or phosphatidylinositol phosphatase activity; IEA:InterPro.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   InterPro; IPR000300; IPPc.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   SMART; SM00128; IPPc; 1.
DR   SUPFAM; SSF56219; Exo_endo_phos; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   420 AA;  48960 MW;  2D0B1CE3C72F1C9B CRC64;
     MQGLWGLPDQ LGVTFHVLLL CLSRKTWPGE SMLPENLQKN WLREFYQVLH THKPHFMALH
     CQEFGGKNYE ASMSHVDKFV KELLSSDAMK EYNRARVYLD ENYKSQEHFT ALGSFYFLHE
     SLKNIYQFDF KAKKYKKVTG KEIYSDTLES TPMLEKEKFP QDYFPECKWS RKGFIRTRWC
     IADCAFDLVN IHLFHDASNL VAWETSPSVY SGVRHKALGY VLDRIIDQRF EKVSYFVFGD
     FNFRLDSKSV VETLCTKATM QTVRAADTNE VVKLIFRESD NDRKVVLQLE KKLFDYFNQD
     VFRDNNGTAL LEFDKELSVF KDRLYELDIS FPPSYPYSED SSQGEQYMNT RCPAWCDRIL
     MSLSAKELVL KSESEEKVAT YDHIGPNVCM GDHKPVFLAF RIAPGAGKPH AHVHKCCVVQ
//
ID   Q3TZU9_MOUSE            Unreviewed;       467 AA.
AC   Q3TZU9;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 50.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Pvrl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC       domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK157513; BAE34108.1; -; mRNA.
DR   IPI; IPI00223489; -.
DR   UniGene; Mm.4341; -.
DR   ProteinModelPortal; Q3TZU9; -.
DR   STRING; Q3TZU9; -.
DR   Ensembl; ENSMUST00000108450; ENSMUSP00000104089; ENSMUSG00000062300.
DR   MGI; MGI:97822; Pvrl2.
DR   HOVERGEN; HBG019169; -.
DR   ArrayExpress; Q3TZU9; -.
DR   Bgee; Q3TZU9; -.
DR   Genevestigator; Q3TZU9; -.
DR   GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0001675; P:acrosome assembly; IMP:MGI.
DR   GO; GO:0032990; P:cell part morphogenesis; IMP:MGI.
DR   GO; GO:0007010; P:cytoskeleton organization; IMP:MGI.
DR   GO; GO:0051654; P:establishment of mitochondrion localization; IMP:MGI.
DR   GO; GO:0009566; P:fertilization; IMP:MGI.
DR   GO; GO:0043064; P:flagellum organization; IMP:MGI.
DR   GO; GO:0030382; P:sperm mitochondrion organization; IMP:MGI.
DR   GO; GO:0007289; P:spermatid nucleus differentiation; IMP:MGI.
DR   InterPro; IPR013162; CD80_C2-set.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR003596; Ig_V-set_sub.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3.
DR   Pfam; PF08205; C2-set_2; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00406; IGv; 1.
DR   PROSITE; PS50835; IG_LIKE; 3.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
SQ   SEQUENCE   467 AA;  50778 MW;  7356A90F65FA6859 CRC64;
     MARAAVLPPS RLSPTLPLLP LLLLLLQETG AQDVRVRVLP EVRGRLGGTV ELPCHLLPPT
     TERVSQVTWQ RLDGTVVAAF HPSFGVDFPN SQFSKDRLSF VRARPETNAD LRDATLAFRG
     LRVEDEGNYT CEFATFPNGT RRGVTWLRVI AQPENHAEAQ EVTIGPQSVA VARCVSTGGR
     PPARITWISS LGGEAKDTQE PGIQAGTVTI ISRYSLVPVG RADGVKVTCR VEHESFEEPI
     LLPVTLSVRY PPEVSISGYD DNWYLGRSEA ILTCDVRSNP EPTDYNWSTT SGVFPASAVA
     QGSQLLVHSV DRMVNTTFIC TATNAVGTGR AEQVILVRDT PQASRDVGPL VWGAVGGTLL
     VLLLAGGFLA LILLRGRRRR KSPGGGGNDG DRGSYDPKTQ VFGNGGPVFW RSASPEPMRP
     DGREEDEEEE EEMKAEEGLM LPPHESPKDD MESHLDGSLI SRRAVYV
//
ID   NOL9_MOUSE              Reviewed;         714 AA.
AC   Q3TZX8; A0PJC7; B1AS65; Q05A31; Q8BQE1; Q8C8L5; Q8C9A8; Q9D678;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Polynucleotide 5'-hydroxyl-kinase NOL9;
DE            EC=2.7.1.-;
DE   AltName: Full=Nucleolar protein 9;
GN   Name=Nol9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Cerebellum, Embryo, Neonatal skin, Spleen, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-524 (ISOFORMS 1/2/3).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Polynucleotide 5'-kinase involved in rRNA processing.
CC       The kinase activity is required for the processing of the 32S
CC       precursor into 5.8S and 28S rRNAs, more specifically for the
CC       generation of the major 5.8S(S) form. In vitro, has both DNA and
CC       RNA 5'-kinase activities. Probably binds RNA (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity).
CC       Note=Colocalizes with pre-60S rRNPs particles (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3TZX8-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q3TZX8-2; Sequence=VSP_053056, VSP_053057;
CC       Name=3;
CC         IsoId=Q3TZX8-3; Sequence=VSP_053058, VSP_053059;
CC   -!- SIMILARITY: Belongs to the Clp1 family. NOL9/GRC3 subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH24877.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK014568; BAB29433.1; -; mRNA.
DR   EMBL; AK042581; BAC31300.1; -; mRNA.
DR   EMBL; AK046761; BAC32857.1; -; mRNA.
DR   EMBL; AK050948; BAC34472.1; -; mRNA.
DR   EMBL; AK157398; BAE34079.1; -; mRNA.
DR   EMBL; AL611927; CAM24579.1; -; Genomic_DNA.
DR   EMBL; AL611927; CAM24580.1; -; Genomic_DNA.
DR   EMBL; CH466594; EDL14922.1; -; Genomic_DNA.
DR   EMBL; BC024877; AAH24877.1; ALT_SEQ; mRNA.
DR   EMBL; BC125432; AAI25433.1; -; mRNA.
DR   EMBL; BC132099; AAI32100.1; -; mRNA.
DR   IPI; IPI00625464; -.
DR   IPI; IPI00649815; -.
DR   IPI; IPI00874324; -.
DR   RefSeq; NP_001153071.1; NM_001159599.1.
DR   RefSeq; NP_083003.2; NM_028727.2.
DR   UniGene; Mm.275803; -.
DR   ProteinModelPortal; Q3TZX8; -.
DR   SMR; Q3TZX8; 315-352.
DR   PhosphoSite; Q3TZX8; -.
DR   PRIDE; Q3TZX8; -.
DR   Ensembl; ENSMUST00000084116; ENSMUSP00000081133; ENSMUSG00000028948.
DR   GeneID; 74035; -.
DR   KEGG; mmu:74035; -.
DR   UCSC; uc008vzd.1; mouse.
DR   CTD; 74035; -.
DR   MGI; MGI:1921285; Nol9.
DR   eggNOG; roNOG09090; -.
DR   GeneTree; ENSGT00390000012406; -.
DR   HOVERGEN; HBG058105; -.
DR   InParanoid; Q3TZX8; -.
DR   OMA; MDGLYTK; -.
DR   PhylomeDB; Q3TZX8; -.
DR   ArrayExpress; Q3TZX8; -.
DR   Bgee; Q3TZX8; -.
DR   Genevestigator; Q3TZX8; -.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0051731; F:polynucleotide 5'-hydroxyl-kinase activity; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000460; P:maturation of 5.8S rRNA; ISS:UniProtKB.
DR   InterPro; IPR010655; Pre-mRNA_cleavage_cplxII_Clp1.
DR   Pfam; PF06807; Clp1; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; ATP-binding; Kinase;
KW   Nucleotide-binding; Nucleus; RNA-binding; rRNA processing;
KW   Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    714       Polynucleotide 5'-hydroxyl-kinase NOL9.
FT                                /FTId=PRO_0000367432.
FT   NP_BIND     322    329       ATP (Potential).
FT   COMPBIAS      9     54       Arg-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   VAR_SEQ     627    627       I -> E (in isoform 3).
FT                                /FTId=VSP_053058.
FT   VAR_SEQ     628    714       Missing (in isoform 3).
FT                                /FTId=VSP_053059.
FT   VAR_SEQ     671    671       P -> L (in isoform 2).
FT                                /FTId=VSP_053056.
FT   VAR_SEQ     672    714       Missing (in isoform 2).
FT                                /FTId=VSP_053057.
FT   CONFLICT    101    101       A -> G (in Ref. 1; BAC31300).
FT   CONFLICT    225    225       D -> E (in Ref. 1; BAB29433 and 2;
FT                                CAM24579).
FT   CONFLICT    269    269       A -> S (in Ref. 1; BAC34472).
SQ   SEQUENCE   714 AA;  80840 MW;  E2FFC860BD488F5C CRC64;
     MAESEVLHRR APSRSSWLRV RKARPHLLLS RRGRRRFGVL TRVELRRLRR RLLRAHALGG
     DWKQVAPAGA HVAVKCKLRA RSRPAPRSPP TPSVPPAPCT ASATCSLLNP RNHSTPQSRA
     GRPVRKVSPN VTQPVRDLGS GRVLMMLPPG EGFTFSGICR VTCVYGQLEV YGHIINQGQP
     PQDVFSVYTH SYLTINGVPY AEPEKSEKAI RREIRALLKP YTKLDDRNWV VRYFPPLGSI
     MILERMQSRF VDFLKTYKCS SYVLLQENAP VRVNSEFTTL KKIGIRRQKR KKAICLSESG
     LCALEELVSV SCDGCPVILL CGACDIGKST FNRILINQLL NSIPGVDYLE CDLGQTEFTP
     PGCVALLTIT EPLLGPPYTH QRKPQRMVYY GKMNCYNDYE NYIDIVKYVF RDYKREFPLI
     INTMGWVSDN GLRLLVDLIR VLSPNYVVQL YSDRCKFTPT LTSEYVELTD GLYTKSKIKR
     YRGFEIPEFG DNLEFTYEEK ESSPLPVFTG HVLLSVHSEF LSSKNEKNRA KYNRIFRDLA
     VLGYLSQLML PVPESLSPLH SLTPYQVPFS AVAIRVLHAD VAPTHILYAV NASWVGLCRI
     VDDMKGYTRG PILLAQNPIC DCLGFGICRG IDMDKRTYHI LTPLPPEELK TVNCLLVGSI
     SIPHCIFQNQ PGPEGSVPYV TTDYNLNIPG ATEKIGEREY GKAFPRHKLR QRRK
//
ID   ESYT2_MOUSE             Reviewed;         845 AA.
AC   Q3TZZ7; B2RSN5; Q9D5Y7;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=Extended synaptotagmin-2;
DE            Short=E-Syt2;
GN   Name=Esyt2; Synonyms=D12Ertd551e, Fam62b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Retina, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662 AND SER-685, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-682 AND SER-685, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-685, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May play a role as calcium-regulated intrinsic membrane
CC       protein (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3TZZ7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3TZZ7-2; Sequence=VSP_023243;
CC   -!- SIMILARITY: Belongs to the extended synaptotagmin family.
CC   -!- SIMILARITY: Contains 3 C2 domains.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK014813; BAB29565.1; -; mRNA.
DR   EMBL; AK044360; BAC31884.1; -; mRNA.
DR   EMBL; AK157352; BAE34059.1; -; mRNA.
DR   EMBL; BC052440; AAH52440.1; -; mRNA.
DR   EMBL; BC054797; AAH54797.1; -; mRNA.
DR   EMBL; BC059230; AAH59230.1; -; mRNA.
DR   EMBL; BC138937; AAI38938.1; -; mRNA.
DR   IPI; IPI00266942; -.
DR   IPI; IPI00828672; -.
DR   RefSeq; NP_083007.2; NM_028731.5.
DR   UniGene; Mm.273755; -.
DR   HSSP; Q9JIR9; 2BWQ.
DR   ProteinModelPortal; Q3TZZ7; -.
DR   SMR; Q3TZZ7; 308-430, 459-552, 710-837.
DR   PhosphoSite; Q3TZZ7; -.
DR   PRIDE; Q3TZZ7; -.
DR   Ensembl; ENSMUST00000100986; ENSMUSP00000098548; ENSMUSG00000021171.
DR   GeneID; 52635; -.
DR   KEGG; mmu:52635; -.
DR   UCSC; uc007pho.1; mouse.
DR   CTD; 52635; -.
DR   MGI; MGI:1261845; Esyt2.
DR   eggNOG; roNOG04511; -.
DR   GeneTree; ENSGT00550000074417; -.
DR   HOGENOM; HBG446028; -.
DR   HOVERGEN; HBG055795; -.
DR   InParanoid; Q3TZZ7; -.
DR   OMA; ACDLPAW; -.
DR   OrthoDB; EOG4CRKZK; -.
DR   NextBio; 309245; -.
DR   ArrayExpress; Q3TZZ7; -.
DR   Bgee; Q3TZZ7; -.
DR   CleanEx; MM_D12ERTD551E; -.
DR   Genevestigator; Q3TZZ7; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   Pfam; PF00168; C2; 3.
DR   SMART; SM00239; C2; 3.
DR   SUPFAM; SSF49562; C2_CaLB; 3.
DR   PROSITE; PS50004; C2; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Membrane; Phosphoprotein; Repeat;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    845       Extended synaptotagmin-2.
FT                                /FTId=PRO_0000278259.
FT   TRANSMEM     52     72       Helical; (Potential).
FT   TRANSMEM    226    246       Helical; (Potential).
FT   DOMAIN      296    397       C2 1.
FT   DOMAIN      447    541       C2 2.
FT   DOMAIN      712    816       C2 3.
FT   COMPBIAS    660    663       Poly-Ser.
FT   MOD_RES     615    615       Phosphoserine (By similarity).
FT   MOD_RES     662    662       Phosphoserine.
FT   MOD_RES     663    663       Phosphoserine (By similarity).
FT   MOD_RES     667    667       Phosphoserine (By similarity).
FT   MOD_RES     679    679       Phosphoserine (By similarity).
FT   MOD_RES     682    682       Phosphoserine.
FT   MOD_RES     685    685       Phosphoserine.
FT   VAR_SEQ       1    487       Missing (in isoform 2).
FT                                /FTId=VSP_023243.
SQ   SEQUENCE   845 AA;  94139 MW;  988F3D97D7F3CF6C CRC64;
     MSSAGGEGPE AGPGRAGGRS EPEAPGSALS VDLPGLLGQL ARSFALLLPV YALGYLGLSF
     SWVLLALGLL AWCRRSRGLK ASRLCRALAL LEDEEQAVRL GVRACDLPAW VHFPDTERAE
     WLNKTVKHMW PFICQFIEKL FRETIEPAVR GANAHLSTFS FTKVDVGQQP LRVNGVKVYT
     ENVDKRQIIL DLQISFVGNC EIDLEIKRYF CRAGVKSIQI HGTMRVILEP LIGDMPLVGA
     LSIFFLRKPL LEINWTGLTN LLDIPGLNGL SDTIILDIIS NYLVLPNRIT VPLVSEVQIA
     QLRFPIPKGV LRIHFIEAQD LQGKDTYLKG LVKGKSDPYG IIRVGNQIFQ SKVIKENLSP
     KWNEVYEALV YEHPGQELEI ELFDEDPDKD DFLGSLMIDL IEVEKERLLD EWFTLDEVPK
     GKLHLKLEWL TLMPDAANLD KVLADIRADK DQASDGLSSA LLILYLDSAR NLPSGKKINS
     NPNPLVQMSV GHKAQESKIR YKTSEPVWEE NFTFFIHNPR RQDLEVEVKD EQHQCSLGSL
     RIPLSQLLTS DNMTINQRFQ LSNSGPNSTL KMKIALRVLH LEKQERPPDY QHSAQVKRPS
     VSKEGRKMPI KSQMSASPGT GGANTAPSTP VMGVDDKPAM EEKPQPPEAS PLGHRDLGRS
     SSSLLASPSH IAAKEPTPSI ASDISLPIAT QELRQRLRQL ENGTTLGQSP LGQIQLTIRH
     SSQRNKLIVV VHSCRNLIAF SEDGSDPYVR MYLLPDKRRS GRRKTHVSKK TLNPVFDQSF
     DFSVSLPEVQ RRTLDVAVKN SGGFLSKDKG LLGKVLVVLA SEELAKGWTQ WYDLTEDGTR
     PQVIT
//
ID   Q3U041_MOUSE            Unreviewed;       416 AA.
AC   Q3U041;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   11-JAN-2011, entry version 47.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Rad23b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK157252; BAE34014.1; -; mRNA.
DR   IPI; IPI00890867; -.
DR   UniGene; Mm.196846; -.
DR   ProteinModelPortal; Q3U041; -.
DR   SMR; Q3U041; 1-82, 184-231, 273-332, 372-416.
DR   STRING; Q3U041; -.
DR   Ensembl; ENSMUST00000030134; ENSMUSP00000030134; ENSMUSG00000028426.
DR   MGI; MGI:105128; Rad23b.
DR   HOVERGEN; HBG055042; -.
DR   InParanoid; Q3U041; -.
DR   ArrayExpress; Q3U041; -.
DR   Bgee; Q3U041; -.
DR   Genevestigator; Q3U041; -.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   GO; GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   InterPro; IPR004806; Rad23.
DR   InterPro; IPR006636; STI1_HS-bd.
DR   InterPro; IPR009060; UBA-like.
DR   InterPro; IPR000449; UBA/transl_elong_EF1B_N.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   InterPro; IPR000626; Ubiquitin.
DR   InterPro; IPR019955; Ubiquitin_supergroup.
DR   InterPro; IPR015360; XPC-bd.
DR   Gene3D; G3DSA:1.10.10.540; XPC-bd; 1.
DR   Pfam; PF00627; UBA; 2.
DR   Pfam; PF00240; ubiquitin; 1.
DR   Pfam; PF09280; XPC-binding; 1.
DR   PRINTS; PR01839; RAD23PROTEIN.
DR   SMART; SM00727; STI1; 1.
DR   SMART; SM00165; UBA; 2.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF46934; UBA_like; 2.
DR   SUPFAM; SSF101238; XPC-bd; 1.
DR   TIGRFAMs; TIGR00601; rad23; 1.
DR   PROSITE; PS50030; UBA; 2.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   416 AA;  43585 MW;  A11606A9CA257E56 CRC64;
     MQVTLKTLQQ QTFKIDIDPE ETVKALKEKI ESEKGKDAFP VAGQKLIYAG KILSDDTALK
     EYKIDEKNFV VVMVTKPKAV TTAVPATTQP SSTPSPTAVS SSPAVAAAQA PAPTPALPPT
     STPASTAPAS TTASSEPAPA GATQPEKPAE KPAQTPVLTS PAPADSTPGD SSRSNLFEDA
     TSALVTGQSY ENMVTEIMSM GYEREQVIAA LRASFNNPDR AVEYLLMGIP GDRESQAVVD
     PPPQAVSTGT PQSPAVAAAA ATTTATTTTT SGGHPLEFLR NQPQFQQMRQ IIQQNPSLLP
     ALLQQIGREN PQLLQQISQH QEHFIQMLNE PVQEAGSQGE GGGGGGGGGG GGGGGIAEAG
     SGHMNYIQVT PQEKEAIERL KALGFPEGLV IQAYFACEKN ENLAANFLLQ QNFDED
//
ID   Q3U063_MOUSE            Unreviewed;       893 AA.
AC   Q3U063;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Zfp281;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; AK157189; BAE33992.1; -; mRNA.
DR   IPI; IPI00116926; -.
DR   UniGene; Mm.62521; -.
DR   ProteinModelPortal; Q3U063; -.
DR   SMR; Q3U063; 253-363.
DR   STRING; Q3U063; -.
DR   Ensembl; ENSMUST00000047734; ENSMUSP00000039003; ENSMUSG00000041483.
DR   Ensembl; ENSMUST00000112046; ENSMUSP00000107677; ENSMUSG00000041483.
DR   MGI; MGI:3029290; Zfp281.
DR   eggNOG; roNOG14306; -.
DR   HOGENOM; HBG717076; -.
DR   HOVERGEN; HBG055321; -.
DR   InParanoid; Q3U063; -.
DR   OrthoDB; EOG4M3989; -.
DR   ArrayExpress; Q3U063; -.
DR   Bgee; Q3U063; -.
DR   Genevestigator; Q3U063; -.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 4.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   893 AA;  96676 MW;  A3FF71354871A482 CRC64;
     MKIGSGFLSG GGGPSSSGGS GSGGSSGSAS GGSGGGRRAE MEPTFPQSMV MFNHRLPPVT
     SFTRPAGTAA PPPQCVLSSS TSAAPAAEPP PPPAPDMTFK KEPAASAAAF PSQRTSWGFL
     QSLVSIKQEK PADPEEQPSH HHHHHHHYGG LFAGAEERSP GLGGGEGGSH GVIQDLSLLH
     QHAQQQPAQH HRDALLSSGS RTDEHGNQEP KQDANVKKAK RPKPESQGIK AKRKPSASSK
     PLVGEGEGAV LSPSQKPHIC DHCSAAFRSS YHLRRHVLIH TGERPFQCSQ CSMGFIQKYL
     LQRHEKIHSR EKPFGCDQCS MKFIQKYHME RHKRTHSGEK PYKCDTCQQY FSRTDRLLKH
     RRTCGEAIAK GAASAEPGSS NHNSMGNLAV LSQGNTSSSR RKSKSKSIAI ENKEHKTSKT
     NESQMSNNIN MQSYSVEMST VSTSGSIIGT GIDELQKRVP KLIFKKGSRK NADKSYLNFV
     SPLPDVVGQK SLSGKPGGSL GIVSNNSVET ISLLQSTSGK QGPISSNYDD AMQFSKKRRY
     LPTASSNSAF SINVGHMVSQ QSVIQSAGVS VLDNEAPLSL IDSSALNAEI KSCHDKSGIP
     DEVLQSILDQ YSGKSETQKE DPFNLTEPRV DLHTSGEHSE LVQEENLSPG TQTPSNDKTS
     MLQEYSKYLQ QAFEKSTNAG FTLGHGFQFV SLSSPLHNHT LFPEKQIYTT SPLECGFGQS
     VTSVLPSSLP KPPFGMLFGS QPGLYLSALD ATHQQLTPSQ ELDDLIDSQK NLETSSAFQS
     SSQKLTSQKE QQKNLESSTS FQIPSQELAS QIDPQKDIEP RTTYQIENFA QAFGSQFKSG
     SRVPMTFITN SNGEVDHRVR TSVSDFSGYT NMMSDVSEPC STRVKTPTSQ SYR
//
ID   TPPC9_MOUSE             Reviewed;        1148 AA.
AC   Q3U0M1; Q3UU81; Q69Z79; Q6NS50; Q8CD01; Q8CFV8; Q9D8R6;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   08-MAR-2011, entry version 40.
DE   RecName: Full=Trafficking protein particle complex subunit 9;
DE   AltName: Full=NIK- and IKBKB-binding protein;
GN   Name=Trappc9; Synonyms=Kiaa1882, Nibp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH
RP   IKBKB AND MAP3K14, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15951441; DOI=10.1074/jbc.M501670200;
RA   Hu W.-H., Pendergast J.S., Mo X.-M., Brambilla R., Bracchi-Ricard V.,
RA   Li F., Walters W.M., Blits B., He L., Schaal S.M., Bethea J.R.;
RT   "NIBP, a novel NIK and IKK(beta)-binding protein that enhances NF-
RT   (kappa)B activation.";
RL   J. Biol. Chem. 280:29233-29241(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Head, Pancreas, Spleen, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 593-1148 (ISOFORM 1).
RC   TISSUE=Spleen;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
CC   -!- FUNCTION: Functions as an activator of NF-kappa-B through
CC       increased phosphorylation of the IKK complex. May function in
CC       neuronal cells differentiation. May play a role in vesicular
CC       transport from endoplasmic reticulum to Golgi.
CC   -!- SUBUNIT: Part of the multisubunit TRAPP (transport protein
CC       particle) complex (By similarity). Interacts with IKBKB and
CC       MAP3K14; the interaction is direct.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network (By
CC       similarity). Endoplasmic reticulum (By similarity). Cytoplasm
CC       (Probable). Note=Processes and cell bodies of neurons.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q3U0M1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3U0M1-2; Sequence=VSP_034353;
CC       Name=3;
CC         IsoId=Q3U0M1-3; Sequence=VSP_034351, VSP_034352;
CC       Name=4;
CC         IsoId=Q3U0M1-4; Sequence=VSP_034353, VSP_034356;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q3U0M1-5; Sequence=VSP_034353, VSP_034354, VSP_034355;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in neurons of the pyramidal layer of
CC       the cortex, in spinal cord motor neurons and white matter neurons
CC       (at protein level).
CC   -!- SIMILARITY: Belongs to the NIBP family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB25242.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AY630620; AAV31909.1; -; mRNA.
DR   EMBL; AK007766; BAB25242.1; ALT_INIT; mRNA.
DR   EMBL; AK031788; BAC27550.1; -; mRNA.
DR   EMBL; AK138682; BAE23746.1; -; mRNA.
DR   EMBL; AK156739; BAE33831.1; -; mRNA.
DR   EMBL; BC034590; AAH34590.1; -; mRNA.
DR   EMBL; BC070463; AAH70463.1; -; mRNA.
DR   EMBL; AK173287; BAD32565.1; -; mRNA.
DR   IPI; IPI00454019; -.
DR   IPI; IPI00608085; -.
DR   IPI; IPI00621664; -.
DR   IPI; IPI00896049; -.
DR   IPI; IPI00896060; -.
DR   RefSeq; NP_001158113.1; NM_001164641.1.
DR   RefSeq; NP_001158114.1; NM_001164642.1.
DR   RefSeq; NP_001158115.1; NM_001164643.1.
DR   RefSeq; NP_083916.1; NM_029640.2.
DR   RefSeq; NP_850993.2; NM_180662.2.
DR   UniGene; Mm.158902; -.
DR   STRING; Q3U0M1; -.
DR   PhosphoSite; Q3U0M1; -.
DR   Ensembl; ENSMUST00000023276; ENSMUSP00000023276; ENSMUSG00000047921.
DR   Ensembl; ENSMUST00000063060; ENSMUSP00000056253; ENSMUSG00000047921.
DR   Ensembl; ENSMUST00000089770; ENSMUSP00000087202; ENSMUSG00000047921.
DR   GeneID; 76510; -.
DR   KEGG; mmu:76510; -.
DR   CTD; 76510; -.
DR   MGI; MGI:1923760; Trappc9.
DR   eggNOG; roNOG05327; -.
DR   GeneTree; ENSGT00390000006486; -.
DR   HOVERGEN; HBG108595; -.
DR   InParanoid; Q3U0M1; -.
DR   OMA; GDEISTN; -.
DR   OrthoDB; EOG4J3WG6; -.
DR   NextBio; 345300; -.
DR   ArrayExpress; Q3U0M1; -.
DR   Bgee; Q3U0M1; -.
DR   Genevestigator; Q3U0M1; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   InterPro; IPR013935; Transport_Trs120.
DR   Pfam; PF08626; Trs120; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Differentiation;
KW   Endoplasmic reticulum; Golgi apparatus; Phosphoprotein.
FT   CHAIN         1   1148       Trafficking protein particle complex
FT                                subunit 9.
FT                                /FTId=PRO_0000341587.
FT   MOD_RES     953    953       Phosphoserine (By similarity).
FT   VAR_SEQ       1    188       Missing (in isoform 3).
FT                                /FTId=VSP_034351.
FT   VAR_SEQ     189    194       GLDTDS -> MLLGLK (in isoform 3).
FT                                /FTId=VSP_034352.
FT   VAR_SEQ     286    294       Missing (in isoform 2, isoform 4 and
FT                                isoform 5).
FT                                /FTId=VSP_034353.
FT   VAR_SEQ     499    503       EKKDV -> ETLAT (in isoform 5).
FT                                /FTId=VSP_034354.
FT   VAR_SEQ     504   1148       Missing (in isoform 5).
FT                                /FTId=VSP_034355.
FT   VAR_SEQ     706   1148       Missing (in isoform 4).
FT                                /FTId=VSP_034356.
FT   CONFLICT    773    773       E -> D (in Ref. 3; AAH70463).
SQ   SEQUENCE   1148 AA;  128232 MW;  FB3C68229B691327 CRC64;
     MSVPDYMQCA EDHQTLLVVV QAVGIVSEEN FFRIYKRICS VSQLSVRDTQ RALFIRYRHH
     YPPENNEWGD FQTHRKVVGL ITITDCFSPK DWPQTFEKFH VQKEIYGSTL YDSRLFVFGL
     QGDVAEQPRP DVAFYPNYDD CDSVEKRIED FIESLFIVLE SKRLDRATDK SGDKIPLLCV
     PFEKKDFVGL DTDSRHYKKR CQGRMRKHVG DLCLQAGMLQ DALVHYHMSV ELLRSVNDFL
     WLGAALEGLC SASVIYHYPG GTGGKTGARR LQGSSLPSEA ANRHRPGAQE VLIDPGALTT
     NGINPDTSTE IGRAKNCLSP EDIIDKYKEA ISYYSKYKNA GVIELEACVK AVRVLAIQKR
     GMEASEFLQN AVYINLRQLS EEEKIQRYSI LSELYELIGF HRKSAFFKRV AAMQCVAPSI
     AEPGWRACYK LLLETLPGYS LSLDPKDFSK GTHRGWAAVQ MRLLHELVYA SRRMGNPALS
     VRHLSFLLQT MLDFLSDQEK KDVTQSLENY TAKCPGTMEP ITLPDGLTLP PVPFTKLPIV
     RCVKLLSLPT SLRPHKVKSL LGQSMSTKSP FIYSPIIAHN RGEERNKKID FQWVQGDVCE
     VQLMVYNPMP FELRVENMGL LTSGVEFESL PAALSLPAES GLYPVTLVGV PQTTGMITVN
     GYHTTVFGVF SDCLLDNLPG LKTGGSTVEV IPALPRLQIS TSLPRSARSL QPSAGDEIAT
     NVSVQLYNGE TQQLAVTLEN IGLEPLEQLE VTSKLLTTKE KLYGDFLSWK LEETLAQFPL
     QPGKVATFTI NIKAKLDFSC QENLLQDLSD DGISVSGFPL SSPFRQVVRP RVESRPTNPS
     EGSKTGDLGH VKTLEAVLNF KYSGGPGHVE GYYRNLSLGL HVEVEPSVFF TRVSTLPATS
     TRQCHLLLDV FNSTEHELTV CARNNSELVL HASECQRMAI QVDKFNFESV PESPGEKGHF
     ANLKQLEEER QEARGLEISS KLDIRWRIPS LKRSGEASVE GLLNQLILEH LQLAPLQWDV
     LVDGQPCDCE VAAACQVGDP VRLEVRLTNR SPRSVGPFAL TVVPFQDHQN GVHNYDLHDV
     ISFVGSSTFY LDTVQPSGQS TCLGALLFLY TGDFFLNIRF HEDCKSKELP PSWVCLPSVH
     VRALGAQA
//
ID   FUBP2_MOUSE             Reviewed;         748 AA.
AC   Q3U0V1; Q2VPQ6; Q6P2L2;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Far upstream element-binding protein 2;
DE            Short=FUSE-binding protein 2;
DE   AltName: Full=KH type-splicing regulatory protein;
DE            Short=KSRP;
GN   Name=Khsrp; Synonyms=Fubp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 198-748.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
CC   -!- FUNCTION: Binds to the dendritic targeting element and may play a
CC       role in mRNA trafficking. Part of a ternary complex that binds to
CC       the downstream control sequence (DCS) of the pre-mRNA. Mediates
CC       exon inclusion in transcripts that are subject to tissue-specific
CC       alternative splicing. May interact with single-stranded DNA from
CC       the far-upstream element (FUSE). May activate gene expression.
CC       Also involved in degradation of inherently unstable mRNAs that
CC       contain AU-rich elements (AREs) in their 3'-UTR, possibly by
CC       recruiting degradation machinery to ARE-containing mRNAs (By
CC       similarity).
CC   -!- SUBUNIT: Part of a ternary complex containing FUBP2, PTBP1, PTBP2
CC       and HNRPH1. Interacts with PARN (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity). Note=A small proportion is also found in the
CC       cytoplasm of neuronal cell bodies and dendrites (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Belongs to the KHSRP family.
CC   -!- SIMILARITY: Contains 4 KH domains.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK156541; BAE33750.1; -; mRNA.
DR   EMBL; BC064454; AAH64454.1; -; mRNA.
DR   EMBL; BC108414; AAI08415.1; -; mRNA.
DR   IPI; IPI00462934; -.
DR   RefSeq; NP_034743.3; NM_010613.3.
DR   UniGene; Mm.34296; -.
DR   HSSP; Q91WJ8; 1X4M.
DR   ProteinModelPortal; Q3U0V1; -.
DR   SMR; Q3U0V1; 131-504.
DR   STRING; Q3U0V1; -.
DR   PhosphoSite; Q3U0V1; -.
DR   PRIDE; Q3U0V1; -.
DR   Ensembl; ENSMUST00000007814; ENSMUSP00000007814; ENSMUSG00000007670.
DR   GeneID; 16549; -.
DR   KEGG; mmu:16549; -.
DR   UCSC; uc008ddr.1; mouse.
DR   CTD; 16549; -.
DR   MGI; MGI:1336214; Khsrp.
DR   HOGENOM; HBG385795; -.
DR   HOVERGEN; HBG000625; -.
DR   InParanoid; Q3U0V1; -.
DR   OrthoDB; EOG451DQX; -.
DR   NextBio; 290019; -.
DR   ArrayExpress; Q3U0V1; -.
DR   Bgee; Q3U0V1; -.
DR   CleanEx; MM_KHSRP; -.
DR   Genevestigator; Q3U0V1; -.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR015096; DUF1897.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR004088; KH_type_1.
DR   InterPro; IPR018111; KH_type_1_subgr.
DR   Pfam; PF09005; DUF1897; 2.
DR   Pfam; PF00013; KH_1; 4.
DR   SMART; SM00322; KH; 4.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 4.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; DNA-binding; mRNA processing; mRNA splicing;
KW   mRNA transport; Nucleus; Phosphoprotein; Repeat; RNA-binding;
KW   Transcription; Transcription regulation; Transport.
FT   CHAIN         1    748       Far upstream element-binding protein 2.
FT                                /FTId=PRO_0000298678.
FT   DOMAIN      145    209       KH 1.
FT   DOMAIN      234    300       KH 2.
FT   DOMAIN      323    387       KH 3.
FT   DOMAIN      425    492       KH 4.
FT   REPEAT      572    583       1.
FT   REPEAT      618    629       2.
FT   REPEAT      644    655       3.
FT   REPEAT      674    685       4.
FT   REGION      572    685       4 X 12 AA imperfect repeats.
FT   COMPBIAS      7     68       Gly/Pro-rich.
FT   COMPBIAS     69    497       Gly-rich.
FT   COMPBIAS    499    613       Ala/Gly/Pro-rich.
FT   MOD_RES       6      6       Phosphothreonine (By similarity).
FT   MOD_RES      88     88       N6-acetyllysine (By similarity).
FT   MOD_RES     101    101       Phosphothreonine (By similarity).
FT   MOD_RES     133    133       Phosphoserine (By similarity).
FT   MOD_RES     182    182       Phosphoserine.
FT   MOD_RES     185    185       Phosphoserine (By similarity).
FT   MOD_RES     275    275       Phosphoserine.
FT   MOD_RES     481    481       Phosphoserine (By similarity).
FT   MOD_RES     671    671       Phosphoserine (By similarity).
FT   CONFLICT    387    387       F -> I (in Ref. 2; AAI08415).
SQ   SEQUENCE   748 AA;  76809 MW;  6698EC09B435C6E4 CRC64;
     MSDYNTGGPP PGPPPPAGGG GGAAGAGGGP PPGPPGAGDR GGGGPGGGGP GGGGASGGPS
     QPPGGGGPGI RKDAFADAVQ RARQIAAKIG GDAATTVNNN TPDFGFGGQK RQLEDGDQPD
     SKKLASQGDS IGSQLGPIHP PPRTSMTEEY RVPDGMVGLI IGRGGEQINK IQQDSGCKVQ
     ISPDSGGLPE RSVSLTGAPE SVQKAKMMLD DIVSRGRGGP PGQFHDNANG GQNGTVQEIM
     IPAGKAGLVI GKGGETIKQL QERAGVKMIL IQDGSQNTNV DKPLRIIGDP YKVQQACEMV
     MDILRERDQG GFGDRNEYGS RVGGGIDVPV PRHSVGVVIG RSGEMIKKIQ NDAGVRIQFK
     QDDGTGPEKI AHIMGPPDRC EHAARIFNDL LQSLRSGPPG PPGAPGMPPG GRGRGRGQGN
     WGPPGGEMTF SIPTHKCGLV IGRGGENVKA INQQTGAFVE ISRQLPPNGD PNFKLFVIRG
     SPQQIDHAKQ LIEEKIEGPL CPVGPGPGGP GPAGPMGPFN PGPFNQGPPG APPHAGGPPP
     HQYPPQGWGN TYPQWQPPAP HDPNKAAAAA TDPNAAWAAY YSHYYQQPPG PVPGPAPAPA
     APPAQGEPPQ PPPTGQSDYT KAWEEYYKKI GQQPQQPGAP PQQDYTKAWE EYYKKQAQVA
     TGGGPGAPPG SQPDYSAAWA EYYRQQAAYY GQTPGPGGPQ PPPTQQGQQQ ASGNCHPPPP
     PFSFQPPATV HPALVGSAGN PFPCGVCP
//
ID   PAG1_MOUSE              Reviewed;         429 AA.
AC   Q3U1F9; Q8BFS1; Q9EQF3;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Phosphoprotein associated with glycosphingolipid-enriched microdomains 1;
DE   AltName: Full=Csk-binding protein;
DE   AltName: Full=Transmembrane phosphoprotein Cbp;
GN   Name=Pag1; Synonyms=Cbp, Pag;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20253245; PubMed=10790433; DOI=10.1084/jem.191.9.1591;
RA   Brdicka T., Pavlistova D., Bruyns E., Leo A., Korinek V.,
RA   Angelisova P., Scherer J., Shevchenko A., Shevchenko A., Hilgert I.,
RA   Cerny J., Drbal K., Kuramitsu Y., Horejsi V., Schraven B.;
RT   "Phosphoprotein associated with glycosphingolipid-enriched
RT   microdomains (PAG), a novel ubiquitously expressed transmembrane
RT   adaptor protein, binds the protein tyrosine kinase csk and is involved
RT   in regulation of T cell activation.";
RL   J. Exp. Med. 191:1591-1604(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   INTERACTION WITH SLC9A3R1, IDENTIFICATION IN A COMPLEX WITH SLC9A3R1
RP   AND MSN, MUTAGENESIS OF LEU-429, SUBCELLULAR LOCATION, AND
RP   PHOSPHORYLATION.
RX   PubMed=11777944;
RA   Itoh K., Sakakibara M., Yamasaki S., Takeuchi A., Arase H.,
RA   Miyazaki M., Nakajima N., Okada M., Saito T.;
RT   "Negative regulation of immune synapse formation by anchoring lipid
RT   raft to cytoskeleton through Cbp-EBP50-ERM assembly.";
RL   J. Immunol. 168:541-544(2002).
RN   [4]
RP   PHOSPHORYLATION AT TYR-314, INTERACTION WITH CSK, AND FUNCTION.
RX   PubMed=12218089;
RA   Yasuda K., Nagafuku M., Shima T., Okada M., Yagi T., Yamada T.,
RA   Minaki Y., Kato A., Tani-Ichi S., Hamaoka T., Kosugi A.;
RT   "Fyn is essential for tyrosine phosphorylation of Csk-binding
RT   protein/phosphoprotein associated with glycolipid-enriched
RT   microdomains in lipid rafts in resting T cells.";
RL   J. Immunol. 169:2813-2817(2002).
RN   [5]
RP   PALMITOYLATION.
RX   PubMed=12626544;
RA   Van Laethem F., Liang X., Andris F., Urbain J., Vandenbranden M.,
RA   Ruysschaert J.-M., Resh M.D., Stulnig T.M., Leo O.;
RT   "Glucocorticoids alter the lipid and protein composition of membrane
RT   rafts of a murine T cell hybridoma.";
RL   J. Immunol. 170:2932-2939(2003).
RN   [6]
RP   PHOSPHORYLATION AT TYR-314, MUTAGENESIS OF TYR-314, INTERACTION WITH
RP   CSK, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=12612075; DOI=10.1128/MCB.23.6.2017-2028.2003;
RA   Davidson D., Bakinowski M., Thomas M.L., Horejsi V., Veillette A.;
RT   "Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp,
RT   a lipid raft-associated transmembrane adaptor.";
RL   Mol. Cell. Biol. 23:2017-2028(2003).
RN   [7]
RP   FUNCTION, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX   PubMed=14645715; DOI=10.1073/pnas.2432139100;
RA   Shima T., Nada S., Okada M.;
RT   "Transmembrane phosphoprotein Cbp senses cell adhesion signaling
RT   mediated by Src family kinase in lipid rafts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:14897-14902(2003).
RN   [8]
RP   PHOSPHORYLATION AT TYR-314, AND INTERACTION WITH CSK.
RX   PubMed=14967142; DOI=10.1016/S1097-2765(04)00050-4;
RA   Zhang S.Q., Yang W., Kontaridis M.I., Bivona T.G., Wen G., Araki T.,
RA   Luo J., Thompson J.A., Schraven B.L., Philips M.R., Neel B.G.;
RT   "Shp2 regulates SRC family kinase activity and Ras/Erk activation by
RT   controlling Csk recruitment.";
RL   Mol. Cell 13:341-355(2004).
RN   [9]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=16166631; DOI=10.1128/MCB.25.19.8486-8495.2005;
RA   Xu S., Huo J., Tan J.E.-L., Lam K.-P.;
RT   "Cbp deficiency alters Csk localization in lipid rafts but does not
RT   affect T-cell development.";
RL   Mol. Cell. Biol. 25:8486-8495(2005).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-224, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-379, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-165; TYR-183; TYR-224
RP   AND SER-379, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Negatively regulates TCR (T-cell antigen receptor)-
CC       mediated signaling in T-cells and FCER1 (high affinity
CC       immunoglobulin epsilon receptor)-mediated signaling in mast cells.
CC       Promotes CSK activation and recruitment to lipid rafts, which
CC       results in LCK inhibition. Inhibits immunological synapse
CC       formation by preventing dynamic arrangement of lipid raft
CC       proteins. May be involved in cell adhesion signaling.
CC   -!- SUBUNIT: When phosphorylated, interacts with CSK. Interacts with
CC       SLC9A3R1/EBP50. In resting T-cells, part of a PAG1-SLC9A3R1-MSN
CC       complex which is disrupted upon TCR activation.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type III membrane
CC       protein. Note=Present in lipid rafts.
CC   -!- TISSUE SPECIFICITY: Present in T-cells (at protein level).
CC   -!- PTM: Palmitoylated.
CC   -!- PTM: Phosphorylated by FYN on Tyr-314 in resting T-cells; which
CC       promotes interaction with CSK. Dephosphorylated by PTPRC/CD45 upon
CC       TCR activation; which leads to CSK dissociation. May also be
CC       dephosphorylated by PTPN11. Hyperphosphorylated in mast cells upon
CC       FCER1 activation.
CC   -!- DISRUPTION PHENOTYPE: Mice are viable and do not show any
CC       developmental defect up to 20 months of age. They have normal T-
CC       cell development and normal T- and B-cell responses.
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DR   EMBL; AF250192; AAG44565.1; -; mRNA.
DR   EMBL; AK156000; BAE33539.1; -; mRNA.
DR   EMBL; AK040230; BAC30545.1; -; mRNA.
DR   EMBL; AK089329; BAC40842.1; -; mRNA.
DR   EMBL; AK172106; BAE42829.1; -; mRNA.
DR   IPI; IPI00307892; -.
DR   RefSeq; NP_001181960.1; NM_001195031.1.
DR   RefSeq; NP_444412.2; NM_053182.5.
DR   UniGene; Mm.214484; -.
DR   ProteinModelPortal; Q3U1F9; -.
DR   STRING; Q3U1F9; -.
DR   PhosphoSite; Q3U1F9; -.
DR   PRIDE; Q3U1F9; -.
DR   Ensembl; ENSMUST00000108384; ENSMUSP00000104021; ENSMUSG00000027508.
DR   GeneID; 94212; -.
DR   KEGG; mmu:94212; -.
DR   UCSC; uc008opc.1; mouse.
DR   CTD; 94212; -.
DR   MGI; MGI:2443160; Pag1.
DR   eggNOG; roNOG13481; -.
DR   GeneTree; ENSGT00390000002061; -.
DR   HOGENOM; HBG279366; -.
DR   HOVERGEN; HBG055052; -.
DR   InParanoid; Q3U1F9; -.
DR   OMA; VNKPGQS; -.
DR   OrthoDB; EOG4CRM0T; -.
DR   PhylomeDB; Q3U1F9; -.
DR   NextBio; 352171; -.
DR   ArrayExpress; Q3U1F9; -.
DR   Bgee; Q3U1F9; -.
DR   Genevestigator; Q3U1F9; -.
DR   GermOnline; ENSMUSG00000027508; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045121; C:membrane raft; TAS:HGNC.
DR   GO; GO:0005886; C:plasma membrane; TAS:HGNC.
DR   GO; GO:0005515; F:protein binding; IPI:HGNC.
DR   GO; GO:0035556; P:intracellular signal transduction; TAS:HGNC.
DR   GO; GO:0050868; P:negative regulation of T cell activation; IDA:HGNC.
PE   1: Evidence at protein level;
KW   Adaptive immunity; Cell membrane; Immunity; Lipoprotein; Membrane;
KW   Palmitate; Phosphoprotein; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    429       Phosphoprotein associated with
FT                                glycosphingolipid-enriched microdomains
FT                                1.
FT                                /FTId=PRO_0000083339.
FT   TOPO_DOM      1     17       Extracellular (Potential).
FT   TRANSMEM     18     38       Helical; Signal-anchor for type III
FT                                membrane protein; (Potential).
FT   TOPO_DOM     39    429       Cytoplasmic (Potential).
FT   REGION      314    317       Interaction with CSK.
FT   REGION      427    429       Interaction with SLC9A3R1.
FT   MOD_RES     165    165       Phosphotyrosine.
FT   MOD_RES     183    183       Phosphotyrosine.
FT   MOD_RES     224    224       Phosphotyrosine.
FT   MOD_RES     314    314       Phosphotyrosine; by FYN.
FT   MOD_RES     356    356       Phosphotyrosine (By similarity).
FT   MOD_RES     379    379       Phosphoserine.
FT   MOD_RES     386    386       Phosphotyrosine (By similarity).
FT   MOD_RES     414    414       Phosphotyrosine (By similarity).
FT   LIPID        39     39       S-palmitoyl cysteine (By similarity).
FT   LIPID        42     42       S-palmitoyl cysteine (By similarity).
FT   MUTAGEN     314    314       Y->F: Enhances TCR-mediated signaling.
FT   MUTAGEN     429    429       L->A: Abolishes interaction with SLC9A3R1
FT                                and effect on synapse formation.
FT   CONFLICT     58     58       L -> P (in Ref. 1; AAG44565).
FT   CONFLICT    287    287       H -> R (in Ref. 1; AAG44565).
FT   CONFLICT    360    360       K -> R (in Ref. 2; BAE33539).
SQ   SEQUENCE   429 AA;  46549 MW;  F5A95257B4C4DADC CRC64;
     MGPAGSVLSS GQMQMQMVLW GSLAAVAMFF LITFLVLLCS TCDREKKPRQ HSGDHENLMN
     VPSDKDMFSH SATSLTTDAL ASSEQNGVLT NGDILSEDST LTCMQHYEEV QTSASDLLDS
     QDSTGKAKCH QSRELPRIPP ENAVDEILTA RAADTELGPG VEGPYEVLKD SSSQENMVED
     CLYETVKEIK EVADKGQGGK SKSTSALKEL QGAPMEGKAD FAEYASVDRN KKCRHSANAE
     SILGTCSDLD EESPPPVPVK LLDENANLPQ EGGGQAEEQA AEGTGGHSKR FSSLSYKSRE
     EDPTLTEEEI SAMYSSVNKP GQSAHKPGPC MKGPESACHS MKGLPQRSSS SCNDLYATVK
     DFEKTPNSIS TLPPARRPSE EPEPDYEAIQ TLNREDEKVP LETNGHHVPK ESDYESIGDL
     QQCRDVTRL
//
ID   Q3U1G0_MOUSE            Unreviewed;       317 AA.
AC   Q3U1G0;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Evi5l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK155998; BAE33538.1; -; mRNA.
DR   IPI; IPI00756596; -.
DR   RefSeq; XP_003084801.1; XM_003084753.1.
DR   RefSeq; XP_003084802.1; XM_003084754.1.
DR   RefSeq; XP_003086721.1; XM_003086673.1.
DR   RefSeq; XP_003086722.1; XM_003086674.1.
DR   UniGene; Mm.437106; -.
DR   UniGene; Mm.480098; -.
DR   Ensembl; ENSMUST00000043710; ENSMUSP00000049266; ENSMUSG00000011832.
DR   Ensembl; ENSMUST00000086778; ENSMUSP00000083987; ENSMUSG00000011832.
DR   GeneID; 100503956; -.
DR   KEGG; mmu:100503956; -.
DR   UCSC; uc009kte.1; mouse.
DR   MGI; MGI:2442167; Evi5l.
DR   eggNOG; roNOG10165; -.
DR   GeneTree; ENSGT00550000074196; -.
DR   HOGENOM; HBG445866; -.
DR   InParanoid; Q3U1G0; -.
DR   OrthoDB; EOG4548Z6; -.
DR   ArrayExpress; Q3U1G0; -.
DR   Bgee; Q3U1G0; -.
DR   Genevestigator; Q3U1G0; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   317 AA;  35949 MW;  E6D7289FCC52BA28 CRC64;
     MQDKVLDMEK RNSSLPDENN VARLQEELKA LKVREGEAVA SARELKLQLQ ELSDTWQAHL
     SRGGRWKESP RKLVLGELQD ELMTVRLREA QALADGREWR QRVVELETQD NIHRNLLNRV
     EAERAALQEK LQYLAAQNKG LQTQLSESRR KQAEAECKSK EEVMAVRLRE ADSMAAVAEM
     RQRIAELEIQ REEGRIQGQL NHSDSSQYIR ELKDQIEELK TEVRLLKGPP TFEDPLAFDG
     LSLTRHLDED SLPSSDEELL GVGVGVGAAL QDPLYPLSPR DARFFRSLDR PAKDSEGSSD
     SDADELATPY SNQGLDN
//
ID   Q3U1G4_MOUSE            Unreviewed;       879 AA.
AC   Q3U1G4;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   11-JAN-2011, entry version 33.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Exoc1; Synonyms=Sec3l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK155980; BAE33534.1; -; mRNA.
DR   IPI; IPI00876325; -.
DR   UniGene; Mm.480388; -.
DR   STRING; Q3U1G4; -.
DR   Ensembl; ENSMUST00000049469; ENSMUSP00000046719; ENSMUSG00000036435.
DR   MGI; MGI:2445020; Exoc1.
DR   eggNOG; roNOG09067; -.
DR   HOVERGEN; HBG056730; -.
DR   ArrayExpress; Q3U1G4; -.
DR   Bgee; Q3U1G4; -.
DR   Genevestigator; Q3U1G4; -.
DR   InterPro; IPR019160; Exocyst_Exoc1.
DR   Pfam; PF09763; Sec3; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   879 AA;  100164 MW;  EAF17A1DB6462B30 CRC64;
     MTAIKHALQR DIFTPNDERL LSIVNVCKAG KKKKNCFLCA TVTTERPVQV KVVKVKKSDK
     GDFYKRQIAW ALRDLAVVDA KDAIKENPEF DLHFEKVYKW VASSTAEKNA FISCIWKLNQ
     RYLRKKIDFV NVSSQLLEES VPSGENQSVA GGDEEAVDEY QELNAREEQD IEIMMEGCEC
     AISNAEAFAE KLSRELQVLD GANIQSIMAS EKQVNTLMQL LDEALTEVDQ IELKLSSYEE
     MLQSVKEQMD QISESNHLIH LSNTNNVKLL SEIEFLVNHM DLAKGHIKAL QEGDLVSSRG
     IEACTNAADA LLQCMNVALR PGHDMLLAVK QQQQRFSDLR EHFARRLASH LNNVFVQQGH
     DQSSTLAQHS VELTLPNHHP FHRDLLRYAK LMEWLKSTDY GKYEGLTKNY MDYLSRLYER
     EIKDFFEVAK MKMTGTSKES KKFGLHGSSG KLTGSTSSLN KLSVQSSGSR RSQSSSLLDM
     GNMSASDLDV ADRTKFDKIF EQVLSELEPL CLAEQDFISK FFKLQQHQNM SASMTEAEDL
     DGGSLSRQHS SGTLLPVSSE KDMIRQMMIK IFRCIEPELN NLIALGDKVD SFNSLYMLVK
     MSHHVWTAQN VDPASFLSTT LGNVLVTVKR NFDKCISNQI RQMEEVKISK KSKVGILPFV
     AEFEEFAGLA ESIFKNAERR GDLDKAYTKL IRGVFINVEK VANESQKTPR DVVMMENFHH
     IFATLSRLKI SCLEAEKKEA KQKYTDHLQS YVIYSLGQPL EKLNHFFEGV EARVAQGIRE
     EEVSYQLAFN KQELRKVIKE YPGKEVKKGL DNLYKKVDKH LCEEENLLQV VWHSMQDEFI
     RQYKHFEGLI ARCYPGSGVT MEFTIQDILD YCSSIAQSH
//
ID   TFPT_MOUSE              Reviewed;         259 AA.
AC   Q3U1J1; Q9EP77;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=TCF3 fusion partner homolog;
DE   AltName: Full=Protein FB1;
DE   AltName: Full=Protein amida;
GN   Name=Tfpt; Synonyms=Amida;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6 X CBA; TISSUE=Lung;
RA   Brambillasca F., Mosna G., Privitera E.;
RT   "Mouse ortholog of human FB1.";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=ddY; TISSUE=Brain;
RA   Miki N., Miyamoto K., Taira E.;
RT   "Molecular cloning and functional analysis of mouse Amida.";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=NOD; TISSUE=Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Component of the chromatin-remodeling INO80 complex
CC       which, in addition to chromatin remodeling implicated in crucial
CC       functions such as DNA repair, checkpoint regulation, DNA
CC       replication, telomemere maintenance and chromosome segregation.
CC       Appears to promote apoptosis in a p53/TP53-independent manner (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with NOL3. Component of the chromatin-
CC       remodeling INO80 complex, at least composed of ACTL6A, ACTR5,
CC       ACTR8, RVBL1, RVBL2, INO80, INO80B, INO80C, INO80D and INO80E (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3U1J1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3U1J1-2; Sequence=VSP_021243;
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DR   EMBL; AF267988; AAG48243.1; -; mRNA.
DR   EMBL; AB035134; BAB17318.1; -; mRNA.
DR   EMBL; AK155925; BAE33506.1; -; mRNA.
DR   EMBL; BC024356; AAH24356.1; -; mRNA.
DR   RefSeq; NP_076013.1; NM_023524.1.
DR   UniGene; Mm.358730; -.
DR   IntAct; Q3U1J1; 1.
DR   STRING; Q3U1J1; -.
DR   PhosphoSite; Q3U1J1; -.
DR   PRIDE; Q3U1J1; -.
DR   Ensembl; ENSMUST00000058880; ENSMUSP00000053108; ENSMUSG00000006335.
DR   Ensembl; ENSMUST00000108641; ENSMUSP00000104281; ENSMUSG00000006335.
DR   GeneID; 69714; -.
DR   KEGG; mmu:69714; -.
DR   UCSC; uc009evf.1; mouse.
DR   UCSC; uc009evg.1; mouse.
DR   CTD; 69714; -.
DR   MGI; MGI:1916964; Tfpt.
DR   GeneTree; ENSGT00390000016605; -.
DR   HOGENOM; HBG283373; -.
DR   HOVERGEN; HBG056588; -.
DR   InParanoid; Q3U1J1; -.
DR   OMA; AGQFTIV; -.
DR   OrthoDB; EOG48PMMP; -.
DR   NextBio; 330158; -.
DR   ArrayExpress; Q3U1J1; -.
DR   Bgee; Q3U1J1; -.
DR   CleanEx; MM_TFPT; -.
DR   Genevestigator; Q3U1J1; -.
DR   GermOnline; ENSMUSG00000006335; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR   GO; GO:0006917; P:induction of apoptosis; ISS:UniProtKB.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Nucleus; Phosphoprotein.
FT   CHAIN         1    259       TCF3 fusion partner homolog.
FT                                /FTId=PRO_0000254582.
FT   MOD_RES     180    180       Phosphoserine (By similarity).
FT   MOD_RES     188    188       Phosphoserine (By similarity).
FT   MOD_RES     255    255       Phosphoserine (By similarity).
FT   VAR_SEQ     211    220       Missing (in isoform 2).
FT                                /FTId=VSP_021243.
SQ   SEQUENCE   259 AA;  28954 MW;  C5A0094DC93B356A CRC64;
     MELEQREGTM AAVGFEEFSA PPGSELALPP LFGGHILESE LETEVEFVSG GLGDSGLRER
     DEEEEAARGR RRRQRELNRR KYQALGRRCR EIEQVNERVL NRLHQVQRIT RRLQQERRFL
     MRVLDSYGDD YRDSQFTIVL EDDGSQGTDV PTPGNAENEP PEKEGLSPSQ RTTATLDPTS
     PAPGEGPSGR KRRRAPRVGA SLTPELAPVQ VGAEGWGQGV IKVEEDFGFE ADEALDSSWV
     SREPDKLLPY PTLASPPFD
//
ID   UEVLD_MOUSE             Reviewed;         471 AA.
AC   Q3U1V6; O08761; Q7TQD3;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 variant 3;
DE            Short=UEV-3;
DE   AltName: Full=EV and lactate/malate dehydrogenase domain-containing protein;
GN   Name=Uevld; Synonyms=Attp, Uev3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-169.
RC   TISSUE=Thymus;
RA   Burbelo P.D.;
RT   "Role of ATTP in signal transduction.";
RL   Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Possible negative regulator of polyubiquitination (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3U1V6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3U1V6-2; Sequence=VSP_023352, VSP_023353;
CC   -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin-
CC       conjugating enzyme family. UEV subfamily.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the LDH/MDH
CC       superfamily.
CC   -!- SIMILARITY: Contains 1 UEV (ubiquitin E2 variant) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB57699.1; Type=Frameshift; Positions=146;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK154536; BAE32661.1; -; mRNA.
DR   EMBL; AK155685; BAE33387.1; -; mRNA.
DR   EMBL; BC054796; AAH54796.1; -; mRNA.
DR   EMBL; U97571; AAB57699.1; ALT_FRAME; mRNA.
DR   IPI; IPI00271448; -.
DR   IPI; IPI00752075; -.
DR   RefSeq; NP_001035785.1; NM_001040695.1.
DR   UniGene; Mm.1999; -.
DR   HSSP; Q99816; 2F0R.
DR   ProteinModelPortal; Q3U1V6; -.
DR   SMR; Q3U1V6; 2-145, 182-471.
DR   STRING; Q3U1V6; -.
DR   PRIDE; Q3U1V6; -.
DR   Ensembl; ENSMUST00000094398; ENSMUSP00000091964; ENSMUSG00000043262.
DR   GeneID; 54122; -.
DR   KEGG; mmu:54122; -.
DR   UCSC; uc009gzr.1; mouse.
DR   CTD; 54122; -.
DR   MGI; MGI:1860490; Uevld.
DR   eggNOG; roNOG09872; -.
DR   GeneTree; ENSGT00550000074541; -.
DR   HOGENOM; HBG281551; -.
DR   HOVERGEN; HBG000462; -.
DR   InParanoid; Q3U1V6; -.
DR   OMA; AFPANRV; -.
DR   OrthoDB; EOG48WC1W; -.
DR   NextBio; 310905; -.
DR   ArrayExpress; Q3U1V6; -.
DR   Bgee; Q3U1V6; -.
DR   CleanEx; MM_UEVLD; -.
DR   Genevestigator; Q3U1V6; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0019787; F:small conjugating protein ligase activity; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:InterPro.
DR   GO; GO:0043687; P:post-translational protein modification; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:InterPro.
DR   GO; GO:0051246; P:regulation of protein metabolic process; IEA:InterPro.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   InterPro; IPR008883; UEV_N.
DR   Gene3D; G3DSA:3.90.110.10; lact_mal_DH; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   Pfam; PF05743; UEV; 1.
DR   PRINTS; PR00086; LLDHDRGNASE.
DR   SUPFAM; SSF56327; Lactate_DH/Glyco_hydro_4_C; 1.
DR   SUPFAM; SSF54495; UBQ-conjugat/RWD-like; 1.
DR   PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; FALSE_NEG.
DR   PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; FALSE_NEG.
DR   PROSITE; PS51322; UEV; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; NAD; Ubl conjugation pathway.
FT   CHAIN         1    471       Ubiquitin-conjugating enzyme E2 variant
FT                                3.
FT                                /FTId=PRO_0000278652.
FT   DOMAIN        2    145       UEV.
FT   NP_BIND     191    219       NAD (By similarity).
FT   COMPBIAS    210    215       Poly-Leu.
FT   VAR_SEQ     239    250       DLSASAHSKVVI -> GGDLHSQLFGRF (in isoform
FT                                2).
FT                                /FTId=VSP_023352.
FT   VAR_SEQ     251    471       Missing (in isoform 2).
FT                                /FTId=VSP_023353.
FT   CONFLICT     26     26       Missing (in Ref. 2; AAH54796).
FT   CONFLICT    134    134       K -> R (in Ref. 3; AAB57699).
FT   CONFLICT    166    169       VSDI -> LYCQ (in Ref. 3; AAB57699).
SQ   SEQUENCE   471 AA;  51681 MW;  650A5B9F0B5E5146 CRC64;
     MEFDCEGVRR LLGKYKFRDL TVEELKNVSV SFPHFRYSVD TYVFKDTSQK DLLNFTGTIP
     VMYQGKTYNI PIRFWILDSH PFAPPICFLK PTANMEISVG KHVDAKGRIY LPYLQNWSHP
     KSAIVGLIKE MIAKFQEELP LYSIPSSNEA QQVDLLAYIT KITEGVSDIN SRGWTNHENK
     ILNKITVVGS GDLGIACTLA ISAKGIADKL LLLDLSDGMS QGTMDLDIFN LPNVEISKDL
     SASAHSKVVI FTANSLGGSE SYLHAVQSNV DMFRALVPAL GHYSQHAVLL VASQPVEIMS
     YVTWKLSTFP ATRVVGIGCN LDSQRLQYII TSVLKVQTSG KEVWVVGEQG ENKVCSWSGR
     DGVLSPSSQA QLSSRAMELL KVKGQRSWSV GLSVADLVDT IINNKRKVHS VSTLAKGYYG
     LDNEVFLSLP CILGTGGVSE VIKTKAGEDT VTGTLQASAS SIHALQQQLE L
//
ID   M3K9_MOUSE              Reviewed;        1077 AA.
AC   Q3U1V8; Q8BIG8;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Mitogen-activated protein kinase kinase kinase 9;
DE            EC=2.7.11.25;
GN   Name=Map3k9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Activates the JUN N-terminal pathway.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Homodimerization via the leucine zipper domains
CC       is required for autophosphorylation and subsequent activation (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- PTM: Autophosphorylation on serine and threonine residues within
CC       the activation loop plays a role in enzyme activation. Thr-305 is
CC       likely to be the main autophosphorylation site.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK053843; BAC35552.1; -; mRNA.
DR   EMBL; AK155677; BAE33385.1; -; mRNA.
DR   IPI; IPI00465709; -.
DR   RefSeq; NP_001167578.1; NM_001174107.1.
DR   RefSeq; NP_796369.2; NM_177395.5.
DR   UniGene; Mm.35284; -.
DR   HSSP; O43639; 2FRW.
DR   ProteinModelPortal; Q3U1V8; -.
DR   SMR; Q3U1V8; 42-400.
DR   STRING; Q3U1V8; -.
DR   PhosphoSite; Q3U1V8; -.
DR   PRIDE; Q3U1V8; -.
DR   Ensembl; ENSMUST00000035987; ENSMUSP00000041819; ENSMUSG00000042724.
DR   GeneID; 338372; -.
DR   KEGG; mmu:338372; -.
DR   UCSC; uc007oco.1; mouse.
DR   CTD; 338372; -.
DR   MGI; MGI:2449952; Map3k9.
DR   eggNOG; roNOG12191; -.
DR   HOGENOM; HBG716519; -.
DR   HOVERGEN; HBG067662; -.
DR   InParanoid; Q3U1V8; -.
DR   OrthoDB; EOG4SN1MZ; -.
DR   BRENDA; 2.7.11.25; 244.
DR   ArrayExpress; Q3U1V8; -.
DR   Bgee; Q3U1V8; -.
DR   CleanEx; MM_MAP3K9; -.
DR   Genevestigator; Q3U1V8; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:EC.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR015785; MAPKKK-like.
DR   InterPro; IPR016231; MAPKKK9/10/11.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   PANTHER; PTHR23257:SF87; MAPKKK-like; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   PIRSF; PIRSF000556; MAPKKK9_11; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; Repeat;
KW   Serine/threonine-protein kinase; SH3 domain; Transferase.
FT   CHAIN         1   1077       Mitogen-activated protein kinase kinase
FT                                kinase 9.
FT                                /FTId=PRO_0000277825.
FT   DOMAIN       45    109       SH3.
FT   DOMAIN      137    405       Protein kinase.
FT   DOMAIN      423    444       Leucine-zipper 1.
FT   DOMAIN      458    479       Leucine-zipper 2.
FT   NP_BIND     143    151       ATP (By similarity).
FT   COMPBIAS     29     36       Poly-Glu.
FT   COMPBIAS    575    581       Poly-Glu.
FT   COMPBIAS   1011   1014       Poly-Ser.
FT   ACT_SITE    261    261       Proton acceptor (By similarity).
FT   BINDING     164    164       ATP (By similarity).
FT   MOD_RES     297    297       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     301    301       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     305    305       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     522    522       Phosphothreonine (By similarity).
FT   MOD_RES     526    526       Phosphoserine (By similarity).
FT   MOD_RES     528    528       Phosphothreonine (By similarity).
FT   MOD_RES     540    540       Phosphoserine (By similarity).
FT   MOD_RES     545    545       Phosphoserine (By similarity).
FT   MOD_RES     558    558       Phosphothreonine (By similarity).
FT   MOD_RES     622    622       Phosphoserine (By similarity).
FT   MOD_RES     663    663       Phosphoserine (By similarity).
FT   MOD_RES     885    885       Phosphothreonine (By similarity).
FT   MOD_RES     887    887       Phosphoserine (By similarity).
FT   MOD_RES     902    902       Phosphoserine (By similarity).
FT   MOD_RES     904    904       Phosphoserine (By similarity).
FT   MOD_RES     907    907       Phosphoserine (By similarity).
FT   MOD_RES     971    971       Phosphoserine (By similarity).
FT   CONFLICT    176    176       Q -> K (in Ref. 1; BAC35552).
FT   CONFLICT    284    284       E -> K (in Ref. 1; BAC35552).
SQ   SEQUENCE   1077 AA;  118806 MW;  C435648A4DD70480 CRC64;
     MESSRSLLGC LASATAAPPG DDATGAGAEE EEDEEEAAAE LGSHAALPYW TAVFEYEAAG
     EDELTLRLGD VVEVLSKDSQ VSGDEGWWTG QLNQRVGIFP SNYVTPRSAF SSRCQPGAED
     PSCYPPIQLL EIDFAELTLE EIIGIGGFGK VYRAFWAGDE VAVKAARHDP DEDISQTIEN
     VRQEAKLFAM LKHPNIIALR GVCLKEPNLC LVMEFARGGP LNRVLSGKRI PPDILVNWAV
     QIARGMNYLH DEAIVPIIHR DLKSSNILIL QKVENGDLSN KILEITDFGL AREWHRTTKM
     SAAGTYAWMA PEVIRASMFS KGSDVWSYGV LLWELLTGEV PFRGIDGLAV AYGVAMNKLA
     LPIPSTCPEP FAKLMEDCWN PDPHSRPSFT SILDQLTTIE ESGFFEMPKD SFHCLQDDWK
     HEIQEMFDQL RAKEKELRTW EEELTRAALQ QKNQEELLRR REQELAEREI DILERELNII
     IHQLCQEKPR VKKRKGKFRK SRLKLKDGNR ISLPSDFQHK FTVQASPTMD KRKSLISNRS
     SPPASPTIIP RLRAIQLTPG ESSKTWGRSS VVPKEEGEEE EKRAPKKKGR TWGPGTLGQK
     ELTSGDEGLK SLVDGYKQWS SSAPNLGKGP RSSPALPGFT SLMEIEDEDS EGPGSGENHQ
     QHSPNQSYLC IPFPRGEDGD GPSSDGVHEE PTPVNSATST PQLTPTNSLK RGGTHHRRCE
     VALLGCGAVL AATGLGFDLL EAGKCQLLPP EEPEPPAREE KKRREGLFQR ASRPRRSTSP
     PSRKLFKKEE PMTLLGDPSA SLTLLSLSSI SECNSTRSLL RSDSDEIVVY EMPVSPVEAP
     PLTQCTHNPL VNVRVERFKR DPNQSLTPTH VTLTAPTQPS GHRRTPSDGA LKPTAAPAVL
     GSRSPSSNGM SPSPGTGMLK TPSPSRDPGE FPRLPDPNVV FPPTPRRWNT QRDSTLERPK
     TLEFLPRPRP SANRQRLDPW WFVSPSHARS ASPANSSSTE TPSNLDSCFA SSSSTVEERP
     GLPALLPLQA GPLLPAERTL LDLDAEGQSQ DSTVPLCRAE LNAHGPSPYE IQQEFWS
//
ID   DEN4B_MOUSE             Reviewed;        1499 AA.
AC   Q3U1Y4; Q6NZJ7; Q6R5M4; Q80TZ2; Q80VU7; Q8CGE6; Q8R0E9;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=DENN domain-containing protein 4B;
DE   AltName: Full=Brain-specific gene 4 protein;
DE            Short=Brain specific protein 4;
GN   Name=Dennd4b; Synonyms=Bsg4, Bsp4, Kiaa0476;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J;
RA   Chen W., Zhang J., Chen R., Ci H.L., Li Y.P.;
RT   "Cloning and characterization of a novel mouse gene Bsg4 cDNA
RT   specifically expressed in brain.";
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-1499 (ISOFORM 3).
RC   STRAIN=FVB/N; TISSUE=Brain, Colon, Eye, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 594-1499.
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3U1Y4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3U1Y4-2; Sequence=VSP_028093, VSP_028094, VSP_028095,
CC                                  VSP_028097;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q3U1Y4-3; Sequence=VSP_028096;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 dDENN domain.
CC   -!- SIMILARITY: Contains 1 DENN domain.
CC   -!- SIMILARITY: Contains 1 MABP domain.
CC   -!- SIMILARITY: Contains 2 PPR (pentatricopeptide) repeats.
CC   -!- SIMILARITY: Contains 1 uDENN domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH66102.2; Type=Erroneous initiation;
CC       Sequence=BAC65576.3; Type=Miscellaneous discrepancy; Note=Wrong gene model based on unspliced pre-RNA;
CC       Sequence=BAE33359.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY512564; AAR97575.1; -; mRNA.
DR   EMBL; AK155638; BAE33359.1; ALT_INIT; mRNA.
DR   EMBL; BC026996; AAH26996.1; -; mRNA.
DR   EMBL; BC040460; AAH40460.1; -; mRNA.
DR   EMBL; BC049972; AAH49972.1; -; mRNA.
DR   EMBL; BC066102; AAH66102.2; ALT_INIT; mRNA.
DR   EMBL; AK122294; BAC65576.3; ALT_SEQ; Transcribed_RNA.
DR   IPI; IPI00153183; -.
DR   IPI; IPI00626451; -.
DR   IPI; IPI00762164; -.
DR   RefSeq; NP_958809.3; NM_201407.3.
DR   UniGene; Mm.30571; -.
DR   PhosphoSite; Q3U1Y4; -.
DR   PRIDE; Q3U1Y4; -.
DR   Ensembl; ENSMUST00000090888; ENSMUSP00000088404; ENSMUSG00000042404.
DR   Ensembl; ENSMUST00000098914; ENSMUSP00000096514; ENSMUSG00000042404.
DR   GeneID; 229541; -.
DR   KEGG; mmu:229541; -.
DR   UCSC; uc008qbx.1; mouse.
DR   CTD; 229541; -.
DR   MGI; MGI:2446201; Dennd4b.
DR   eggNOG; roNOG10380; -.
DR   GeneTree; ENSGT00550000074509; -.
DR   HOVERGEN; HBG058313; -.
DR   InParanoid; Q3U1Y4; -.
DR   OrthoDB; EOG44MXR8; -.
DR   NextBio; 379491; -.
DR   ArrayExpress; Q3U1Y4; -.
DR   Bgee; Q3U1Y4; -.
DR   CleanEx; MM_DENND4B; -.
DR   Genevestigator; Q3U1Y4; -.
DR   InterPro; IPR005112; dDENN.
DR   InterPro; IPR001194; DENN.
DR   InterPro; IPR023341; MABP.
DR   InterPro; IPR002885; Pentatricopeptide_repeat.
DR   InterPro; IPR005113; uDENN.
DR   Pfam; PF03455; dDENN; 1.
DR   Pfam; PF02141; DENN; 1.
DR   Pfam; PF03456; uDENN; 1.
DR   SMART; SM00801; dDENN; 1.
DR   SMART; SM00799; DENN; 1.
DR   SMART; SM00800; uDENN; 1.
DR   TIGRFAMs; TIGR00756; PPR; 1.
DR   PROSITE; PS50947; DDENN; 1.
DR   PROSITE; PS50211; DENN; 1.
DR   PROSITE; PS51498; MABP; 1.
DR   PROSITE; PS51375; PPR; 1.
DR   PROSITE; PS50946; UDENN; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Phosphoprotein; Repeat.
FT   CHAIN         1   1499       DENN domain-containing protein 4B.
FT                                /FTId=PRO_0000304679.
FT   DOMAIN       44    203       MABP.
FT   DOMAIN      206    279       UDENN.
FT   DOMAIN      313    497       DENN.
FT   DOMAIN      562    636       dDENN.
FT   REPEAT      775    811       PPR 1.
FT   REPEAT      812    846       PPR 2.
FT   COMPBIAS    886    921       Gln-rich.
FT   COMPBIAS   1104   1156       Ser-rich.
FT   MOD_RES     736    736       Phosphoserine (By similarity).
FT   VAR_SEQ       1    274       Missing (in isoform 2).
FT                                /FTId=VSP_028093.
FT   VAR_SEQ     275    276       AL -> MR (in isoform 2).
FT                                /FTId=VSP_028094.
FT   VAR_SEQ     502    502       Missing (in isoform 2).
FT                                /FTId=VSP_028095.
FT   VAR_SEQ     728    842       Missing (in isoform 3).
FT                                /FTId=VSP_028096.
FT   VAR_SEQ     910    920       Missing (in isoform 2).
FT                                /FTId=VSP_028097.
FT   CONFLICT    979    979       M -> V (in Ref. 4; BAC65576).
SQ   SEQUENCE   1499 AA;  164740 MW;  97E6D1AAF34990F0 CRC64;
     MAEERPPRLV DYFVVAGLAG NGAPIPEEKW VPEPTGPLRP PRPAEPITDV AVIARALGEE
     VPQGYTCIQT SAGGHPLELS AGLLGGTQPV ICYRRGRDKP PLVELGVLYE GKERPKLGFQ
     VLDTTPYSHS ANLAPPGPGH PRTYLMYRRA AEGAGLHALG ITDLCLVLPS KGEGTPHTYC
     RLPRNLNPGM WGPAVYLCYK VGLAKANTLV YEAELLGRYP EEDNEAFPLP ESVPVFCLPM
     GATIECWPAQ TKYPVPVFST FVLTGAAGDK VYGAALQFYE AFPRARLSER QARALGLMSA
     VERGRALGGR AVRSRRAIAV LSRWPAFPAF RAFLTFLYRY SVSGPHRLPL EAHISHFIHN
     VPFPSPQRPR ILVQMSPYDN LLLCQPVSSP LPLSGASFLQ LLQNLGPELA ITLLLAVLTE
     HKLLVHSLRP DLLTSVCEAL VSMIFPLHWQ CPYIPLCPLV LADVLSAPVP FIVGIHSSYF
     DLHDPPADVI CVDLDTNTLF QKEEKKPLSA RTLPRRPYKL LLATLTSLYQ QLDQTYTGPE
     EEASLEFLLT DYEAVCGRRT RLEREVQGAF LRFMACLLKG YRNFLRPLTQ APSEGSRDVD
     NLFYLQGFLK SRERSSHKLY SQLLHTQMFS QFIEECSFGS ARHAALEFFD SCVDKVHPEQ
     EKPEPTPLVE LEELSGSELT VFITPPEEPP VLEGSESTPQ YCYDGFPELK AELFESPQEQ
     QGALPVPGPS RSAPSSPAPR RTKQEMKVAQ RMAQKSATVP ELWARCLLGH CYGLWFLCLP
     AYVRSVPSRV RALHTAYHVL REMENRKVVL PDEVCYRVLM QLCSHYGQPV LSVRVMLEMR
     RAGIVPNTIT YGYYNKAVLE SKWPSGTPGG RLRWAKLRNV VLGAAQFRQP LKDRRQQQQQ
     QQQQQQQKQQ VAEQQKSGSS QTEPYLERPS PTRPLQRQTT WAGRSLREPS SPMGRLVKSG
     SLGSARGTQP TVEAGVAHMI EALGVLEPRG SPVPWQDGSL SDLSLTGEEM APGGSPGGSG
     SALSAQSTEA LEGISGRGSK TSGCQEEVGT PRKGLGARLQ QLLTPSRRAS ASRIPPPELP
     SDLPPAARRS PMDSLLWPRE RPGSTASESS ASLGSEWDIS ESSLSSLSLR RSSERLSDTP
     GAFQPPSLEI LMSSCSLCHA CDSLVYDEEI MAGWAPDDSN LNTTCPFCAC HFVPLLSVQT
     LDSRPSAPSP KSSLAGASGC KDAPAPGGPG PVLSDRRFCL ALDQPQLCNG HMGSASRRVE
     NGAWAYLSPL VLRKELESLV ENEGSEVLAL PELPAAHPII FWNLLWYFQR LRLPSVLPGL
     VLASCNGPPP SQLSQGPSPW LTPDPASVHV HLLWDVLTPD PNSCPPLYVL WRVHSQIPQR
     VVWPGPVPSC LSLALLESVL RHVGLNEVHK AVGLLLETLG PPPTGLHLQR GIYREILFLT
     MAALGKDHVD IVAFDKKYKS AFNKLASSMG KEELRQRRAQ MPTPKAIDCR KCFGAPLEC
//
ID   MAST3_MOUSE             Reviewed;        1321 AA.
AC   Q3U214; Q6A047;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Microtubule-associated serine/threonine-protein kinase 3;
DE            EC=2.7.11.1;
GN   Name=Mast3; Synonyms=Kiaa0561;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-786.
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 762-1156.
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 907-1321.
RC   TISSUE=Thymus;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1237 AND SER-1289, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1289, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SUBUNIT: Interacts with PTEN (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AK155568; BAE33328.1; -; mRNA.
DR   EMBL; BC024265; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK172971; BAD32249.1; -; mRNA.
DR   IPI; IPI00944008; -.
DR   RefSeq; NP_955012.2; NM_199308.2.
DR   UniGene; Mm.250731; -.
DR   HSSP; O75582; 1VZO.
DR   ProteinModelPortal; Q3U214; -.
DR   SMR; Q3U214; 200-694, 964-1060.
DR   PhosphoSite; Q3U214; -.
DR   PRIDE; Q3U214; -.
DR   Ensembl; ENSMUST00000037986; ENSMUSP00000046075; ENSMUSG00000031833.
DR   GeneID; 546071; -.
DR   KEGG; mmu:546071; -.
DR   UCSC; uc009mbq.1; mouse.
DR   CTD; 546071; -.
DR   MGI; MGI:2683541; Mast3.
DR   eggNOG; roNOG15399; -.
DR   HOGENOM; HBG445910; -.
DR   HOVERGEN; HBG052414; -.
DR   InParanoid; Q3U214; -.
DR   OrthoDB; EOG4SF957; -.
DR   PhylomeDB; Q3U214; -.
DR   BRENDA; 2.7.11.1; 244.
DR   Bgee; Q3U214; -.
DR   CleanEx; MM_MAST3; -.
DR   Genevestigator; Q3U214; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR015022; MA_Ser/thr_Kinase_dom.
DR   InterPro; IPR023142; MAST_pre-PK_dom.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF08926; DUF1908; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Magnesium; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1   1321       Microtubule-associated serine/threonine-
FT                                protein kinase 3.
FT                                /FTId=PRO_0000277823.
FT   DOMAIN      389    662       Protein kinase.
FT   DOMAIN      663    734       AGC-kinase C-terminal.
FT   DOMAIN      966   1054       PDZ.
FT   NP_BIND     395    403       ATP (By similarity).
FT   COMPBIAS     18    131       Ser-rich.
FT   COMPBIAS    836    841       Poly-Pro.
FT   COMPBIAS   1102   1175       Ser-rich.
FT   ACT_SITE    512    512       Proton acceptor (By similarity).
FT   BINDING     418    418       ATP (By similarity).
FT   MOD_RES     122    122       Phosphoserine (By similarity).
FT   MOD_RES     156    156       Phosphoserine (By similarity).
FT   MOD_RES     168    168       Phosphoserine (By similarity).
FT   MOD_RES     177    177       Phosphoserine (By similarity).
FT   MOD_RES     179    179       Phosphoserine (By similarity).
FT   MOD_RES     702    702       Phosphoserine (By similarity).
FT   MOD_RES     730    730       Phosphotyrosine (By similarity).
FT   MOD_RES     731    731       Phosphoserine (By similarity).
FT   MOD_RES     748    748       Phosphoserine (By similarity).
FT   MOD_RES     795    795       Phosphoserine (By similarity).
FT   MOD_RES     803    803       Phosphoserine (By similarity).
FT   MOD_RES     813    813       Phosphoserine (By similarity).
FT   MOD_RES     814    814       Phosphoserine (By similarity).
FT   MOD_RES    1237   1237       Phosphoserine.
FT   MOD_RES    1289   1289       Phosphoserine.
FT   CONFLICT    762    766       GDRGR -> DAWVG (in Ref. 2).
FT   CONFLICT   1148   1156       DTASPPNVS -> GGRALSLAL (in Ref. 2;
FT                                BC024265).
SQ   SEQUENCE   1321 AA;  144174 MW;  204D72924DA6A771 CRC64;
     MKSRREKLLI PALTLDLSPS SQSPCLLSPG SPCSPCSPSL GLQPWSCRSG NRKSLVVGTP
     SPTLSRPLSP LSVPTAGNSP LDSPRNFSAA AAISFPFARR ADGRRWSLAS LPSSGYGTNT
     PSSTVSSSSS SRERLHQLPF QPTADELRFL SKHFRSSESV VDEDGGRSPR LRPRSRSLSP
     ERTSGTFDNE IVMMNHVYRE RFPKATAQME GRLQDFLAAF APGDRLALAD GVLGFIHHQI
     VELARDCLAK SGEALVTSRY FLGMQDKLER LLQDAHERSD SAEVGFIVQL VRKLLIIISR
     PARLLECLEF DPEEFYHLLE AAEGQAREDQ GVKTDLPRYI IRQLGLAKDP LEEIQPLNDL
     DESQPPAPGS PESRGLGGPS RRKPCESDFE TIKLISNGAY GAVYLVRHRD TRQRFAIKKI
     NKQNLILRNQ IQQVFVERDI LTFAENPFVV GMFCSFETRR HLCMVMEYVE GGDCATLLKN
     MGPLPVDMAR MYFAETVLAL EYLHNYGIVH RDLKPDNLLI TSLGHIKLTD FGLSKIGLMS
     MATNLYEGHI EKDAREFVDK QVCGTPEYIA PEVIFRQGYG KPVDWWAMGV ILYEFLVGCV
     PFFGDTPEEL FGQVVSDEIM WPEGDEALPL DAQDLITRLL RQSPMDRLGT GGTHEVKQHP
     FFLALDWAGL LRHKAEFVPQ LEAEDDTSYF DTRSERYRHL GSEDDETNDE ESSTEIPQFS
     SCSHRFSKVY SSSEFLAVQP TPTFAERSFS EDREDGWGQS LGDRGRRLSA DLRLRSWTPA
     SSCQPSSCQT DRGPSPSLLS TISLDVMPKF AFSSEDEGAS SGPADPQKPV FILGEPDPPP
     PTTPVTPKPC NLSADTAVLS HARLRSNSTG ARHSTPRPLD AGRGRRLGGS RDPGPEKPRA
     SPGGSGGRVP KSASVSALSL IITADDGSGG PLMSPLSPRS LSSNPSSRDS SPSRDPSPVC
     GSLRPPIVIH SSGKKYGFSL RAIRVYMGDS DVYTVHHVVW SVEEGSPAQE AGLRAGDLIT
     HINGESVLGL VHMDVVELLL KSGNKISLRT TALENTSIKV GPARKNVAKG RMARRSKRSR
     RRETQDRRKS LFKRISKPSS VLHTSRSFSS GLQHSLSSSE SLPGSPTHSL SPSPTTPCRS
     PAPDAPTDTA SPPNVSPSSS SPASPATGHT RPSSLHGLAA KLGPPRHKSG RRKSTSSIPP
     SPLACPPVPT PPPRSPSPLP GHIPIPARSP RLRRGQSADK LGLGTSERLD GDGGRRARGA
     EAELVVMRRL HLSERRDSFK KQEAVQEVSF DEEPGPPRGV PKIAVQGAEA TPGTPGHARK
     D
//
ID   RN149_MOUSE             Reviewed;         394 AA.
AC   Q3U2C5; Q14BF0; Q8CGR2;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF149;
DE            EC=6.3.2.-;
DE   AltName: Full=Goliath-related E3 ubiquitin-protein ligase 4;
DE   AltName: Full=RING finger protein 149;
DE   Flags: Precursor;
GN   Name=Rnf149; Synonyms=Greul4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 113-394.
RC   STRAIN=CD-1;
RX   MEDLINE=22322926; PubMed=12435366; DOI=10.1006/dbio.2002.0814;
RA   Borchers A.G.M., Hufton A.L., Eldridge A.G., Jackson P.K.,
RA   Harland R.M., Baker J.C.;
RT   "The E3 ubiquitin ligase GREUL1 anteriorizes ectoderm during Xenopus
RT   development.";
RL   Dev. Biol. 251:395-408(2002).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3U2C5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3U2C5-2; Sequence=VSP_021734;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC       ubiquitin-conjugating enzyme (By similarity).
CC   -!- SIMILARITY: Contains 1 PA (protease associated) domain.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK155360; BAE33216.1; -; mRNA.
DR   EMBL; BC115968; AAI15969.1; -; mRNA.
DR   EMBL; AY155439; AAN75220.1; -; mRNA.
DR   IPI; IPI00340505; -.
DR   IPI; IPI00808180; -.
DR   UniGene; Mm.28614; -.
DR   HSSP; Q9H0F5; 1X4J.
DR   ProteinModelPortal; Q3U2C5; -.
DR   SMR; Q3U2C5; 28-193, 261-312.
DR   PRIDE; Q3U2C5; -.
DR   Ensembl; ENSMUST00000062525; ENSMUSP00000050388; ENSMUSG00000048234.
DR   UCSC; uc007atl.1; mouse.
DR   MGI; MGI:2677438; Rnf149.
DR   eggNOG; maNOG05557; -.
DR   GeneTree; ENSGT00550000074163; -.
DR   HOGENOM; HBG716731; -.
DR   HOVERGEN; HBG057659; -.
DR   InParanoid; Q3U2C5; -.
DR   OrthoDB; EOG44TP86; -.
DR   NextBio; 325301; -.
DR   ArrayExpress; Q3U2C5; -.
DR   Bgee; Q3U2C5; -.
DR   CleanEx; MM_RNF149; -.
DR   Genevestigator; Q3U2C5; -.
DR   GermOnline; ENSMUSG00000048234; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR003137; Protease-assoc_domain.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Ligase; Membrane; Metal-binding;
KW   Signal; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   SIGNAL        1     31       Potential.
FT   CHAIN        32    394       E3 ubiquitin-protein ligase RNF149.
FT                                /FTId=PRO_0000261612.
FT   TRANSMEM    197    217       Helical; (Potential).
FT   DOMAIN       66    171       PA.
FT   ZN_FING     265    306       RING-type; atypical.
FT   COMPBIAS    356    362       Poly-Ser.
FT   CARBOHYD     51     51       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    141    141       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    339    339       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1    145       Missing (in isoform 2).
FT                                /FTId=VSP_021734.
FT   CONFLICT    115    115       S -> T (in Ref. 3; AAN75220).
FT   CONFLICT    174    174       G -> E (in Ref. 1; BAE33216).
SQ   SEQUENCE   394 AA;  42539 MW;  70F3F904ECEFECE3 CRC64;
     MAARRRPAAG VGARDALAVL ALALCTPGVG GGALEWYSAM VSIEYVDPQS NLTVWSVSES
     GRFGESSLRE ERQGLVGVPR APAPAEGCAP DTRFVAPGAL GNAPWVALVA RGGCSFKDKV
     LAAARRNASA VVVYNLESNG NATEPMSHAG TGNIVVIMIS YPKGREIFDL VQKGIPVKMR
     IEIGTRHMQE FISGQSVVFV AIAFITMMII SLAWLIFYYI QRFLYTGSQF GSQNHRKETK
     KVIGQLPLHT VKHGEKGIDV DAENCAVCIE NFKVKDVIRI LPCKHIFHRI CIDPWLLDHR
     TCPMCKLDVI KALGYWGDPE DTQELPTPEA APGRVSVGNL SVTSQDEERS ESNLPSSSSS
     ESGPHRPCLK EDAGEDTALL GAGRSEPQHG GSIC
//
ID   Q3U2G2_MOUSE            Unreviewed;       842 AA.
AC   Q3U2G2;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   08-MAR-2011, entry version 33.
DE   SubName: Full=Heat shock protein 4;
DE   SubName: Full=Heat shock protein 4, isoform CRA_a;
GN   Name=Hspa4; ORFNames=RP23-337J7.3-001, mCG_113604;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE.
RA   Phillimore B.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK155305; BAE33178.1; -; mRNA.
DR   EMBL; AL596382; CAI25228.1; -; Genomic_DNA.
DR   EMBL; AL592489; CAI25228.1; JOINED; Genomic_DNA.
DR   EMBL; CH466575; EDL33601.1; -; Genomic_DNA.
DR   IPI; IPI00331556; -.
DR   RefSeq; NP_032326.3; NM_008300.3.
DR   UniGene; Mm.239865; -.
DR   ProteinModelPortal; Q3U2G2; -.
DR   SMR; Q3U2G2; 2-700.
DR   STRING; Q3U2G2; -.
DR   PRIDE; Q3U2G2; -.
DR   Ensembl; ENSMUST00000020630; ENSMUSP00000020630; ENSMUSG00000020361.
DR   GeneID; 15525; -.
DR   KEGG; mmu:15525; -.
DR   CTD; 15525; -.
DR   MGI; MGI:1342292; Hspa4.
DR   HOVERGEN; HBG047955; -.
DR   InParanoid; Q3U2G2; -.
DR   OMA; ICSPIIS; -.
DR   PhylomeDB; Q3U2G2; -.
DR   NextBio; 288440; -.
DR   ArrayExpress; Q3U2G2; -.
DR   Bgee; Q3U2G2; -.
DR   Genevestigator; Q3U2G2; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR001023; Hsp70.
DR   InterPro; IPR013126; Hsp_70.
DR   PANTHER; PTHR19375; Hsp70; 1.
DR   Pfam; PF00012; HSP70; 2.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding; Stress response.
SQ   SEQUENCE   842 AA;  94209 MW;  DB1C399060569570 CRC64;
     MSVVGIDLGF QSCYVAVARA GGIETIANEY SDRCTPACVS FGPKNRSIGA AAKSQVISNA
     KNTVQGFKRF HGRAFSDPFV EAEKSNLAYD IVQLPTGLTG IKVTYMEEER NFTTEQVTAM
     LLSKLKETAE SVLKKPVVDC VVSVPSFYTD AERRSVMDAT QIAGLNCLRL MNETTAVALA
     YGIYKQDLPA LEEKPRNVVF VDMGHSAYQV SVCAFNKGKL KVLATAFDTT LGGRKFDEVL
     VNHFCEEFGK KYKLDIKSKI RALLRLSQEC EKLKKLMSAN ASDLPLSIEC FMNDIDVSGT
     MNRGKFLEMC DDLLARVEPP LRSVLEQSKL KKEDIYAVEI VGGATRIPAV KEKISKFFGK
     ELSTTLNADE AVTRGCALQC AILSPAFKVR EFSITDVVPY PISLRWNSPA EEGLSDCEVF
     PKNHAAPFSK VLTFYRKEPF TLEAYYSSPQ DLPYPDPAIA QFSVQKVTPQ SDGSSSKVKV
     KVRVNVHGIF SVSSAALVEV HKSEESEEPM ETDQNAKEEE KMQVDQEEPH TEEQQQQPQT
     PAENKAESEE METSQAGSKD KKTDQPPQAK KAKVKTSTVD LPIESQLLWQ LDREMLGLYT
     ENEGKMIMQD KLEKERNDAK NAVEEYVYEM RDKLSGEYEK FVSEDDRNTF TLKLEDTENW
     LYEDGEDQPK QVYVDKLAEL KSLGQPIKTR FQESEERPKL FEELGKQIQQ YMKVISSFKN
     KEDQYEHLDA ADVTKVEKST NEAMEWMNSK LNLQNKQSLT VDPVVKTKEI EAKIKELTSI
     CSPIISKPKP KVEPPKEEPK HAEQNGPVDG QGDNPGSQAA EHGADTAVPS DGDKKLPEMD
     ID
//
ID   F193B_MOUSE             Reviewed;         892 AA.
AC   Q3U2K0; Q69Z63; Q8K1B4; Q8VCA1;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   08-MAR-2011, entry version 40.
DE   RecName: Full=Protein FAM193B;
GN   Name=Fam193b; Synonyms=Kiaa1931;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=FVB/N; TISSUE=Brain, Eye, Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3U2K0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3U2K0-2; Sequence=VSP_034782;
CC       Name=3;
CC         IsoId=Q3U2K0-3; Sequence=VSP_034781;
CC   -!- SIMILARITY: Belongs to the FAM193 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH25483.2; Type=Erroneous termination; Positions=743; Note=Translated as Lys;
CC       Sequence=BAD32581.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK173303; BAD32581.1; ALT_INIT; mRNA.
DR   EMBL; AK040568; BAC30629.1; -; mRNA.
DR   EMBL; AK155237; BAE33140.1; -; mRNA.
DR   EMBL; AC126408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC021381; AAH21381.1; -; mRNA.
DR   EMBL; BC023015; AAH23015.1; -; mRNA.
DR   EMBL; BC025483; AAH25483.2; ALT_SEQ; mRNA.
DR   IPI; IPI00469938; -.
DR   IPI; IPI00900448; -.
DR   IPI; IPI00900465; -.
DR   RefSeq; NP_001156353.1; NM_001162881.1.
DR   RefSeq; NP_663357.2; NM_145382.4.
DR   UniGene; Mm.35661; -.
DR   PhosphoSite; Q3U2K0; -.
DR   PRIDE; Q3U2K0; -.
DR   Ensembl; ENSMUST00000021957; ENSMUSP00000021957; ENSMUSG00000021495.
DR   GeneID; 212483; -.
DR   KEGG; mmu:212483; -.
DR   UCSC; uc007qrq.1; mouse.
DR   CTD; 212483; -.
DR   MGI; MGI:2385851; Fam193b.
DR   eggNOG; roNOG06979; -.
DR   GeneTree; ENSGT00390000000973; -.
DR   HOGENOM; HBG506750; -.
DR   HOVERGEN; HBG108049; -.
DR   InParanoid; Q3U2K0; -.
DR   OMA; AQASECP; -.
DR   OrthoDB; EOG4CVG6F; -.
DR   NextBio; 373580; -.
DR   ArrayExpress; Q3U2K0; -.
DR   Bgee; Q3U2K0; -.
DR   Genevestigator; Q3U2K0; -.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil.
FT   CHAIN         1    892       Protein FAM193B.
FT                                /FTId=PRO_0000344458.
FT   COILED      485    517       Potential.
FT   COMPBIAS    139    142       Poly-Glu.
FT   COMPBIAS    154    224       Ser-rich.
FT   COMPBIAS    247    355       Pro-rich.
FT   VAR_SEQ       1    449       Missing (in isoform 3).
FT                                /FTId=VSP_034781.
FT   VAR_SEQ       1    114       Missing (in isoform 2).
FT                                /FTId=VSP_034782.
SQ   SEQUENCE   892 AA;  95084 MW;  A56A7499A4D9E5F0 CRC64;
     MTRRRSRPSG GAGRRERARA AGLQKPQAPE PQPPPPSLEA GAGAGPPEVP AELDCDGPRE
     EEEPKLAPGP QVPPTSSQSV QTCCLLCHRE RKGWEEGPSQ NGLVLQGEKL PPDFMPKLVK
     NLLGEMPLWV CQSCRKSMEE EERQTGGDHA VAISLSHTSC KSQSCGGDSH SSSSSSSSSS
     SSSSSCHGNS GDWDPSSFLS AHKLSGLWNS PHSSGAVPGS SLGSPPAILG EAFPVSEHHQ
     HSDLTAPPNS PTGPPPHPAS LIPSHPGSFS SASYPPPLPT TPVAPFPAQA SECPMAAATA
     THPSGPCQSP HPPSTSMPLL KMPPPLSGCS HPCSGHCSGH CGGPLLPPPS SQPLPSTHSR
     DPGCKGHKFA HSGLACEADE GLGEEEDSSS ERSSCTSSST HPRDGKFCDC CYCEFFGHNA
     PLAAPTSRNY TEIREKLRSR LTRRKEELPM KGGTLGGIPG EPAVDHRDVD ELLEFINSTE
     PKVPNSARAA KRARHKLKKK EKEKARLATE ALKQVNRVSG SQEPRPARER LLEWPDQELD
     RVNSFLSSRL QEIKSTVKDS LCASLSMCEL SVESSGFKEG TVEAQTLTPS DLSGSSQKRP
     DINLDLSPLT LGSPQSHTLQ APSEPVPPWA ERRDPHPPPW TEVRGPPPGI PENGLVRRLN
     TVPNLSRVIW VKTPKPGNPS SEESSKEVPS CKQELSEPVA TGGKPKKSKR QGSQAKKTLA
     SPAPWSPANL EASGAKSQVS SPKQPSKGSE PAKVGSGAEP GEGSPGSRPG PIQADSPKTD
     KKGSSWQNWP GGAKARTLEQ ESEQTPGPAR PQSLSQGKGR SRRSRNKQEK SASSLDDVFL
     PKDLDGVEMD ETDREVEYFK RFCLDSAKQT RQKVAVNWTN FSLKKTTPST AQ
//
ID   Q3U2V9_MOUSE            Unreviewed;       312 AA.
AC   Q3U2V9;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 30.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Fam53a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK155077; BAE33031.1; -; mRNA.
DR   IPI; IPI00759959; -.
DR   UniGene; Mm.294695; -.
DR   Ensembl; ENSMUST00000045329; ENSMUSP00000045539; ENSMUSG00000037339.
DR   Ensembl; ENSMUST00000065119; ENSMUSP00000070770; ENSMUSG00000037339.
DR   Ensembl; ENSMUST00000101361; ENSMUSP00000098913; ENSMUSG00000037339.
DR   MGI; MGI:1919225; Fam53a.
DR   eggNOG; roNOG11023; -.
DR   HOVERGEN; HBG051537; -.
DR   InParanoid; Q3U2V9; -.
DR   OrthoDB; EOG42Z4QH; -.
DR   ArrayExpress; Q3U2V9; -.
DR   Bgee; Q3U2V9; -.
DR   Genevestigator; Q3U2V9; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   312 AA;  33419 MW;  E35D09B843AF3D17 CRC64;
     MDVGHFLDLH DSTGPPAAPP TKRHCRSLSE PEELARCRSP WRPGSSKVWT PISKRRCNSG
     GSATLQCCSG VGNPTLQGTL VPGLPRRPVS PAGPTSPLTP RPASASSGFV DGSEGSTSSG
     PPWLSTGPCP FSSRRRLSLS QEHLVDTGAC LPSASSTPTS TPELGRHHGL LRCRSQPCVL
     DGRRVRRKRR REEDARWTRP SLDFLKMTRT LKNSKSLCSL DYEDDEDDTQ EKTLVSSPCN
     SQGLVGIITP SSSPRIPRPG PDSPSIWASG EPEANPGEGG SSGDPSDWDS AGEEGIFPLD
     HGDLDLEQIE NN
//
ID   F117B_MOUSE             Reviewed;         584 AA.
AC   Q3U3E2; Q68EE3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=Protein FAM117B;
DE   AltName: Full=Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 13 protein homolog;
GN   Name=Fam117b; Synonyms=Als2cr13;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 150-584.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-444, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
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DR   EMBL; AK154812; BAE32846.1; -; mRNA.
DR   EMBL; BC080299; AAH80299.2; -; mRNA.
DR   IPI; IPI00461475; -.
DR   RefSeq; NP_001032814.1; NM_001037725.2.
DR   UniGene; Mm.480628; -.
DR   ProteinModelPortal; Q3U3E2; -.
DR   PhosphoSite; Q3U3E2; -.
DR   PRIDE; Q3U3E2; -.
DR   Ensembl; ENSMUST00000036540; ENSMUSP00000041671; ENSMUSG00000041040.
DR   GeneID; 72750; -.
DR   KEGG; mmu:72750; -.
DR   CTD; 72750; -.
DR   MGI; MGI:1920000; Fam117b.
DR   eggNOG; roNOG08109; -.
DR   GeneTree; ENSGT00390000005655; -.
DR   HOGENOM; HBG446570; -.
DR   HOVERGEN; HBG107860; -.
DR   InParanoid; Q3U3E2; -.
DR   OMA; MSQRVRR; -.
DR   OrthoDB; EOG4J6RRN; -.
DR   NextBio; 336864; -.
DR   ArrayExpress; Q3U3E2; -.
DR   Bgee; Q3U3E2; -.
DR   Genevestigator; Q3U3E2; -.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    584       Protein FAM117B.
FT                                /FTId=PRO_0000299534.
FT   COMPBIAS     15     95       Gly-rich.
FT   COMPBIAS    133    141       Poly-Pro.
FT   MOD_RES     214    214       Phosphothreonine (By similarity).
FT   MOD_RES     215    215       Phosphoserine (By similarity).
FT   MOD_RES     216    216       Phosphoserine (By similarity).
FT   MOD_RES     386    386       Phosphoserine (By similarity).
FT   MOD_RES     444    444       Phosphoserine.
SQ   SEQUENCE   584 AA;  61345 MW;  6925098BD41905AA CRC64;
     MSQRVRRNGS PTPAGALAGG AVGPPGGPGS RLQPMRATVP FQLKQQQQHG SPTRGGGGGG
     NNGGNGGASG PSGGGGSGGP RTASRSTSPT RGGGGSAAAR TSPTVATQTG ASVTSTRGTS
     PTRGTAPGAR SSPPRPQPPP PLLGTVSSPS SSPTHLWPSE VIAAPPSARV RHRRRSPEQG
     RPSAEKRSPS APVCKAGDKT HPPSSSSSSI IRRTSSLDTL AAPYLAGHWP RDIRGQAAPC
     MRDKATQTES AWAEEYEKKK GSHKRSSSWG STEQLKEIAK LRQQLQRSKH SSRHHRDKER
     QSPFHGNHAA INQSQAPAPK STLVPAGPIT KSSGSRFRNS VEGLNQEIEI IIKETGEKEE
     QLIPQDIPDG HRAPPPLAQR SSSTRSIDTQ TPGGADKGSN NSSRSQSVSP TSFLTISNEG
     SEESPCSADD LLADPRDKEN GNNSPLPKYA TSPKPNNSYM FKREPPEGCE RVKVFEECSP
     KQLHEIPAFY CPDKNKVNFI PKSGSAFCLV SILKPLLPTP DLTLKGSGHS LTVTTGMTTT
     LLQPISMASL STNTEQERVS RGTSTVLPSA SLHAPPEPIE EAEG
//
ID   LMF1_MOUSE              Reviewed;         574 AA.
AC   Q3U3R4; Q3TDV1; Q8BM33; Q8BY75; Q8VDX3; Q9CWX8;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   RecName: Full=Lipase maturation factor 1;
DE   AltName: Full=Transmembrane protein 112;
GN   Name=Lmf1; Synonyms=Tmem112;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Dendritic cell, Embryo, and Embryonic stem cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INVOLVEMENT IN CLD, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=17994020; DOI=10.1038/ng.2007.24;
RA   Peterfy M., Ben-Zeev O., Mao H.Z., Weissglas-Volkov D.,
RA   Aouizerat B.E., Pullinger C.R., Frost P.H., Kane J.P., Malloy M.J.,
RA   Reue K., Pajukanta P., Doolittle M.H.;
RT   "Mutations in LMF1 cause combined lipase deficiency and severe
RT   hypertriglyceridemia.";
RL   Nat. Genet. 39:1483-1487(2007).
RN   [4]
RP   SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY.
RX   PubMed=19783858; DOI=10.1074/jbc.M109.049395;
RA   Doolittle M.H., Neher S.B., Ben-Zeev O., Ling-Liao J., Gallagher C.M.,
RA   Hosseini M., Yin F., Wong H., Walter P., Peterfy M.;
RT   "Lipase maturation factor LMF1, membrane topology and interaction with
RT   lipase proteins in the endoplasmic reticulum.";
RL   J. Biol. Chem. 284:33623-33633(2009).
CC   -!- FUNCTION: Involved in the maturation of specific proteins in the
CC       endoplasmic reticulum. Required for maturation and transport of
CC       active lipoprotein lipase (LPL) through the secretory pathway.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q3U3R4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3U3R4-2; Sequence=VSP_022974;
CC       Name=3;
CC         IsoId=Q3U3R4-3; Sequence=VSP_022973;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q3U3R4-4; Sequence=VSP_022975, VSP_022976;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues synthesizing
CC       lipoprotein lipase (Lpl) and hepatic lipase (Lipc), including
CC       adipose tissue, skeletal muscle, heart, and liver. Expressed at
CC       higher levels in tissues that express little or no lipase activity
CC       such as testis and pancreas suggesting additional functions in
CC       these tissues.
CC   -!- DISEASE: Note=Defects in Lmf1 are the cause of combined lipase
CC       deficiency (cld). Cld is characterized by severe
CC       hypertriglyceridemia with accumulation of chylomicrons that
CC       gradually pack the lumina of capillaries and sinusoids. Severe
CC       hypertriglyceridemia causes an increase in blood viscosity,
CC       ischemia, and cyanosis, and the inability of tissues to access
CC       circulating triglycerides results in starvation, poor
CC       thermoregulation, and death 2 to 3 days after birth. The disorder
CC       is caused by a decrease in the activity of lipoprotein lipase
CC       (Lpl) and the related hepatic lipase (Lipc), caused by impaired
CC       maturation of nascent Lpl and hepatic lipase polypeptides in the
CC       endoplasmic reticulum.
CC   -!- SIMILARITY: Belongs to the lipase maturation factor family.
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DR   EMBL; AK010312; BAB26844.1; -; mRNA.
DR   EMBL; AK035119; BAC28952.1; -; mRNA.
DR   EMBL; AK041659; BAC31022.1; -; mRNA.
DR   EMBL; AK154622; BAE32721.1; -; mRNA.
DR   EMBL; AK169983; BAE41497.1; -; mRNA.
DR   EMBL; BC020104; AAH20104.1; -; mRNA.
DR   IPI; IPI00405437; -.
DR   IPI; IPI00828587; -.
DR   IPI; IPI00828677; -.
DR   IPI; IPI00828922; -.
DR   RefSeq; NP_083900.3; NM_029624.3.
DR   UniGene; Mm.12787; -.
DR   STRING; Q3U3R4; -.
DR   PRIDE; Q3U3R4; -.
DR   Ensembl; ENSMUST00000063344; ENSMUSP00000066682; ENSMUSG00000002279.
DR   Ensembl; ENSMUST00000115111; ENSMUSP00000110764; ENSMUSG00000002279.
DR   Ensembl; ENSMUST00000116641; ENSMUSP00000112340; ENSMUSG00000002279.
DR   GeneID; 76483; -.
DR   KEGG; mmu:76483; -.
DR   CTD; 76483; -.
DR   MGI; MGI:1923733; Lmf1.
DR   GeneTree; ENSGT00530000063702; -.
DR   HOGENOM; HBG443866; -.
DR   HOVERGEN; HBG101974; -.
DR   InParanoid; Q3U3R4; -.
DR   OMA; SFGWESQ; -.
DR   OrthoDB; EOG43FGWS; -.
DR   NextBio; 345228; -.
DR   ArrayExpress; Q3U3R4; -.
DR   Bgee; Q3U3R4; -.
DR   CleanEx; MM_LMF1; -.
DR   Genevestigator; Q3U3R4; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0034382; P:chylomicron remnant clearance; IMP:MGI.
DR   GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IMP:MGI.
DR   GO; GO:0051006; P:positive regulation of lipoprotein lipase activity; IDA:MGI.
DR   GO; GO:0033578; P:protein glycosylation in Golgi; IMP:MGI.
DR   GO; GO:0051604; P:protein maturation; IDA:MGI.
DR   GO; GO:0009306; P:protein secretion; IMP:MGI.
DR   GO; GO:0090181; P:regulation of cholesterol metabolic process; IMP:MGI.
DR   GO; GO:0090207; P:regulation of triglyceride metabolic process; IMP:MGI.
DR   InterPro; IPR009613; DUF1222.
DR   Pfam; PF06762; DUF1222; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endoplasmic reticulum; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    574       Lipase maturation factor 1.
FT                                /FTId=PRO_0000276740.
FT   TOPO_DOM      1     49       Cytoplasmic (Potential).
FT   TRANSMEM     50     72       Helical; (Potential).
FT   TOPO_DOM     73    127       Lumenal (Potential).
FT   TRANSMEM    128    151       Helical; (Potential).
FT   TOPO_DOM    152    207       Cytoplasmic (Potential).
FT   TRANSMEM    208    221       Helical; (Potential).
FT   TOPO_DOM    222    292       Lumenal (Potential).
FT   TRANSMEM    293    321       Helical; (Potential).
FT   TOPO_DOM    322    367       Cytoplasmic (Potential).
FT   TRANSMEM    368    388       Helical; (Potential).
FT   TOPO_DOM    389    574       Lumenal (Potential).
FT   VAR_SEQ       1    217       Missing (in isoform 3).
FT                                /FTId=VSP_022973.
FT   VAR_SEQ       1      7       Missing (in isoform 2).
FT                                /FTId=VSP_022974.
FT   VAR_SEQ     173    188       WESQLLETGFLGIFLS -> AQGAITSYPQSRTERE (in
FT                                isoform 4).
FT                                /FTId=VSP_022975.
FT   VAR_SEQ     189    574       Missing (in isoform 4).
FT                                /FTId=VSP_022976.
FT   CONFLICT    551    551       L -> Q (in Ref. 2; AAH20104).
SQ   SEQUENCE   574 AA;  65878 MW;  98ED20FA865ACDBB CRC64;
     MRPDSLVMAA PEGSLRKRKV GGAEHSPASQ PSLARDPADS PARLHTGTFW LTRIVLLRAL
     AFIYFVAFLV AFNQNKALIG DRGLLPCKLY LKNVQEYFQG STGWAAWTYA PTIMWLLDWS
     DMNFNLDLIA LLGLGISSFV LVTGCANMIL MTALWALYMS LVNVGQIWYS FGWESQLLET
     GFLGIFLSPL WTLSRLPKNT PTSQIVLWGF RWLIFRIMLG AGLIKVRGDK CWLDLTCMDF
     HYETQPVPNP IAYYLHRSPW WFHRFETLSN HFVELLVPFF LFLGRRMRIL HGVLQILFQV
     ILIISGNLSF LNWLTIVPSL ACFDDAALGF LFPSGPQGLK KQVLEIQRED TQRVQPKPRD
     RGCLVRQVVN ISLGILVAWL SVPVVINLLS SRQIMNTSFN PLRIVNTYGA FGSVTKERTE
     VILQGTVSPN ASAPDAVWED YEFKCKPGDP WRQPCLISPY HYRLDWLMWF AAFQTYEQNE
     WILHLAGKLL AGDSEALALL AVNPFEGRTP PRWIRGEHYR YKFSLPGGQH ATQGKWWIRK
     RIGPYFPPLR LEDLKEYFKT REWPLPEPPS RHTR
//
ID   Q3U417_MOUSE            Unreviewed;       969 AA.
AC   Q3U417;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 39.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Ppfibp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK154482; BAE32618.1; -; mRNA.
DR   IPI; IPI00480372; -.
DR   UniGene; Mm.103382; -.
DR   ProteinModelPortal; Q3U417; -.
DR   SMR; Q3U417; 593-672.
DR   STRING; Q3U417; -.
DR   PRIDE; Q3U417; -.
DR   Ensembl; ENSMUST00000016631; ENSMUSP00000016631; ENSMUSG00000016487.
DR   MGI; MGI:1914783; Ppfibp1.
DR   eggNOG; roNOG10071; -.
DR   HOVERGEN; HBG052331; -.
DR   ArrayExpress; Q3U417; -.
DR   Bgee; Q3U417; -.
DR   Genevestigator; Q3U417; -.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR011510; SAM_2.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 3.
DR   Pfam; PF00536; SAM_1; 2.
DR   Pfam; PF07647; SAM_2; 1.
DR   SMART; SM00454; SAM; 3.
DR   SUPFAM; SSF47769; SAM_homology; 3.
DR   PROSITE; PS50105; SAM_DOMAIN; 2.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   969 AA;  108538 MW;  0725911C5BEA56BB CRC64;
     MMSDASDMLA AALEQMDGII AGSKALEYSN GIFDCQSPTS PFMGSLRALH LVEDLRGLLE
     MMETDEKEGL RCQIPDSTAE VLIEWLQNQM TNGHLPGNGD VYQERLARLE NDKESLVLQV
     SVLTDQVEAQ GEKIRDLEFC LEEHREKLNA TEEMLQQELL SRTSLETQKL ELMAEISNLK
     LKLTAVEKDR LDYEDRFRDT EGLIQEINDL RLKVNEMDGE RLQYEKKLKS TKDELASLKE
     QLEEKECEVK RLQERLVCKA KGEGIEVLDR DIEVQKMKKA VESLMAANEE KERKIEDLRQ
     CLSRYRKMQD PAVLAQGQDS ECEGLFHSSS ISTLLDAQGF SDLERSTSST PGMGSPSRDP
     LHTSAPEEFH TSVLQASIPS LLPPSVDVET CEKPKLPTKP ETSFEEGDGR AILGAAAEVS
     LSDGVSTSSL QKSSSLGNLK KEASDGTDKA PTDSRTFGTL PPKVPGHEAS VDDNPFGTRK
     ARSSFGRGFF KIKSGKRTAS APNLAETEKE TAEHLNLAGT SRSKGSQGTS PFPMSPPSPD
     SRKKSRGIMR LFGKLRRSQS TTFNPDDMSE PEFKRGGTRA TAGPRLGWSR DLGQSNSDLD
     MPFAKWTKEQ VCSWLAEQGL GSYLSSGKHW IISGQTLLQA SQQDLEKELG IKHSLHRKKL
     QLALQALGSE EETNYGKLDF NWVTRWLDDI GLPQYKTQFD EGRVDGRMLH YMTVDDLLSL
     KVVSVLHHLS IKRAIQVLRI NNFEPNCLRR RPSDENSITP SEVQQWTNHR VMEWLRSVDL
     AEYAPNLRGS GVHGGLMVLE PRFNVETMAQ LLNIPPNKTL LRRHLATHFN LLIGAEAQHQ
     KRDAMELPDY VLLTATAKVK PKKLTFSNFG NLRKKKHEDG EEYVCPMELG QASGSSQKGF
     RPGLDMRLYE EDDLDRLEQM EDSEGTVRQI GAFSEGINNL THMLKEDDMF KDFAARSPSA
     SITDEDSNV
//
ID   Q3U542_MOUSE            Unreviewed;       440 AA.
AC   Q3U542;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 40.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Slc14a1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Thymus;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Thymus;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Thymus;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Thymus;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Thymus;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Thymus;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Thymus;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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DR   EMBL; AK153891; BAE32238.1; -; mRNA.
DR   IPI; IPI00652728; -.
DR   RefSeq; NP_001164481.1; NM_001171010.1.
DR   UniGene; Mm.33832; -.
DR   ProteinModelPortal; Q3U542; -.
DR   STRING; Q3U542; -.
DR   Ensembl; ENSMUST00000025433; ENSMUSP00000025433; ENSMUSG00000059336.
DR   Ensembl; ENSMUST00000160292; ENSMUSP00000125114; ENSMUSG00000059336.
DR   GeneID; 108052; -.
DR   KEGG; mmu:108052; -.
DR   UCSC; uc008fsd.1; mouse.
DR   CTD; 108052; -.
DR   MGI; MGI:1351654; Slc14a1.
DR   eggNOG; roNOG04220; -.
DR   HOGENOM; HBG446748; -.
DR   HOVERGEN; HBG000540; -.
DR   InParanoid; Q3U542; -.
DR   OMA; DSPTMVR; -.
DR   ArrayExpress; Q3U542; -.
DR   Bgee; Q3U542; -.
DR   Genevestigator; Q3U542; -.
DR   GO; GO:0016021; C:integral to membrane; TAS:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0015204; F:urea transmembrane transporter activity; IMP:MGI.
DR   GO; GO:0005372; F:water transmembrane transporter activity; IDA:MGI.
DR   InterPro; IPR004937; Urea_transporter.
DR   PANTHER; PTHR10464; Urea_transporter; 1.
DR   Pfam; PF03253; UT; 1.
DR   PIRSF; PIRSF016502; Urea_transporter; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   440 AA;  48338 MW;  BA248DED75D9772A CRC64;
     MNGQSLTGGT DDAHHGPLWI DPFGNRGDKA APEGFRRLSL ALAQRWREQE PEEEIAMEDS
     PTMVKVDRGE NQILSCRGRR CGFKVLGYVT GDMKEFANWL KDKPVVLQFM DWILRGISQV
     VFVSNPISGI LILVGLLVQN PWWALCGCVG TVVSTLTALL LSQDRSAIAA GLQGYNATLV
     GILMAVFSNK GDYFWWLIFP VSAMSMTCPV FSSALSSVLS KWDLPVFTLP FNMALSMYLS
     ATGHYNTFFP SKLFTPVSSV PNITWSELSA LELLKSLPVG VGQIYGCDNP WTGGIFLCAI
     LLSSPLMCLH AAIGSLLGVI AGLSLAAPFE DIYFGLWGFN SSLACIAIGG MFMALTWQTH
     LLALACALFT AYFGACMAHL MAVVHLPACT WSFCLATLLF LLLTTKNPNI YRMPLSKVTY
     SEENRIFYLQ NKKRMVESPL
//
ID   Q3U590_MOUSE            Unreviewed;       706 AA.
AC   Q3U590;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 37.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=C2cd2l; Synonyms=Tmem24;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK153804; BAE32190.1; -; mRNA.
DR   IPI; IPI00119785; -.
DR   RefSeq; NP_082185.2; NM_027909.2.
DR   UniGene; Mm.33869; -.
DR   STRING; Q3U590; -.
DR   Ensembl; ENSMUST00000065080; ENSMUSP00000065233; ENSMUSG00000032120.
DR   GeneID; 71764; -.
DR   KEGG; mmu:71764; -.
DR   UCSC; uc009pct.1; mouse.
DR   CTD; 71764; -.
DR   MGI; MGI:1919014; C2cd2l.
DR   eggNOG; roNOG08526; -.
DR   HOVERGEN; HBG058857; -.
DR   InParanoid; Q3U590; -.
DR   NextBio; 334437; -.
DR   ArrayExpress; Q3U590; -.
DR   Bgee; Q3U590; -.
DR   Genevestigator; Q3U590; -.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   706 AA;  76230 MW;  6B2ACD32996169E0 CRC64;
     MDPDWGQRDV GWAALLVLFA ASLITVLGWM LQYARGLWLS RADGGRDSRP ASAAEPGGSL
     RELGVWRSLL RLRATRTSTP EEAGVRGLLA SLFAFKSFRE NWQRAWVRAL NEQACRDGSS
     IQIAFEEIPQ LPPRASISHV TCVDQSERTM VLHCQLSAEE VRFPISVTQQ SPAAVSMETY
     HVTLTLPPTQ LEVSLEEIPD EGLLVSWAFT DRPELSLKVL PKLQTRERDE EQPELSTVEE
     LIKDAIVSTQ PAMMVNLRAC SAPGGLVPSE KPPTMSQAQP SIPRPTRLFL RQLRASHLGS
     ELGGTEELCC AAELDNPMQQ KWTKPMRAGP EVEWTEDLAL DLGPQSRELT LKVLRSSSCG
     DAELLGQATL PVGSPSRPMS RRQVCPLTPG PGKSLSPAAT VTAELHYEQG SPRNLGTPTS
     STPRPSITPT KKIELDRTIM PDGTVVTTVT TVQSRPRVDG KLDSPSRSPS KVEVTEKMTT
     VLSESSGPSN ASHSSSRESH LSNGLDPVAE TAIRQLTEPS GRAAKKTPTK RSTLIISGVS
     KVPIAQDELA LSLGYAASLE ASMQDDAGTS GGPSSPPSDP SATSPGPVDA LSSPTSVQEA
     DETTRSDISE RPSVDDVESE TGSTGALETG SLKDHKVSFL RSGTKLIFRR RPRQKEAGLS
     QSHDDLSNTT ATPSVRKKAG SFSRRLIKRF SFKSKPKANG NPSPQL
//
ID   PRIC1_MOUSE             Reviewed;         832 AA.
AC   Q3U5C7;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Prickle-like protein 1;
DE   Flags: Precursor;
GN   Name=Prickle1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-682, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Necessary for nuclear localization of REST. May serve as
CC       nuclear receptor (By similarity).
CC   -!- SUBUNIT: Interacts with REST (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane (By similarity). Cytoplasm,
CC       cytosol (By similarity). Note=A smaller amount is detected in the
CC       cytosol (By similarity).
CC   -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC   -!- SIMILARITY: Contains 3 LIM zinc-binding domains.
CC   -!- SIMILARITY: Contains 1 PET domain.
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DR   EMBL; AK153711; BAE32152.1; -; mRNA.
DR   EMBL; BC117892; AAI17893.1; -; mRNA.
DR   EMBL; BC117893; AAI17894.1; -; mRNA.
DR   IPI; IPI00406465; -.
DR   RefSeq; NP_001028389.1; NM_001033217.4.
DR   UniGene; Mm.480617; -.
DR   ProteinModelPortal; Q3U5C7; -.
DR   SMR; Q3U5C7; 124-308.
DR   STRING; Q3U5C7; -.
DR   PhosphoSite; Q3U5C7; -.
DR   PRIDE; Q3U5C7; -.
DR   Ensembl; ENSMUST00000048982; ENSMUSP00000049204; ENSMUSG00000036158.
DR   Ensembl; ENSMUST00000109255; ENSMUSP00000104878; ENSMUSG00000036158.
DR   GeneID; 106042; -.
DR   KEGG; mmu:106042; -.
DR   UCSC; uc007xja.1; mouse.
DR   CTD; 106042; -.
DR   MGI; MGI:1916034; Prickle1.
DR   eggNOG; roNOG13089; -.
DR   HOGENOM; HBG447030; -.
DR   HOVERGEN; HBG053679; -.
DR   InParanoid; Q3U5C7; -.
DR   OMA; CCLECET; -.
DR   OrthoDB; EOG4FBHS8; -.
DR   NextBio; 358030; -.
DR   ArrayExpress; Q3U5C7; -.
DR   Bgee; Q3U5C7; -.
DR   CleanEx; MM_PRICKLE1; -.
DR   Genevestigator; Q3U5C7; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR010442; PET_domain.
DR   InterPro; IPR001781; Znf_LIM.
DR   Gene3D; G3DSA:2.10.110.10; Znf_LIM; 3.
DR   Pfam; PF00412; LIM; 3.
DR   Pfam; PF06297; PET; 1.
DR   SMART; SM00132; LIM; 3.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR   PROSITE; PS51303; PET; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; LIM domain; Lipoprotein; Membrane; Metal-binding;
KW   Methylation; Nucleus; Phosphoprotein; Prenylation; Repeat; Zinc.
FT   CHAIN         1    829       Prickle-like protein 1.
FT                                /FTId=PRO_0000283027.
FT   PROPEP      830    832       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000396713.
FT   DOMAIN       14    122       PET.
FT   DOMAIN      124    188       LIM zinc-binding 1.
FT   DOMAIN      189    249       LIM zinc-binding 2.
FT   DOMAIN      250    313       LIM zinc-binding 3.
FT   COMPBIAS    817    822       Poly-Lys.
FT   MOD_RES     682    682       Phosphoserine.
FT   MOD_RES     829    829       Cysteine methyl ester (By similarity).
FT   LIPID       829    829       S-farnesyl cysteine (By similarity).
SQ   SEQUENCE   832 AA;  94131 MW;  8E664AAEA2E23CEA CRC64;
     MPLEMEPKMS KLVFGCQRSS TSDDDSGCAL EEYAWVPPGL RPEQIQLYFA CLPEEKVPYV
     NSPGEKHRIK QLLYQLPPHD NEVRYCQSLS EEEKKELQVF SAQRKKEALG RGTIKLLSRA
     VMHAVCEQCG LQMNGGEVAV FASRAGPGVC WHPSCFVCFT CNELLVDLIY FYQDGKIHCG
     RHHAELLKPR CSACDEIIFA DECTEAEGRH WHMKHFCCLE CETVLGGQRY IMKDGRPFCC
     GCFESLYAEY CETCGEHIGV DHAQMTYDGQ HWHATEACFS CAQCKASLLG CPFLPKQGQI
     YCSKTCSLGE DIHASDSSDS AFQSARSRDS RRSVRMGRSS RSADQCRQSL LLSPALNYKF
     PGLSGNADDT LSRKLDDVSL ASRQGAGFAN EEFWKARVEQ EASEDPEEWA EHEDYMTQLL
     LKFGDKNLFQ QQSSEVDPRA SEHWIPDNMV TNKPEVKPNH QGLASKKYQS DMYWAQSQDG
     LGDSAYGSHP GPASSRRLQE LDLDHGAAGY THDQSQWYED SLECLSDLKP EQSIRDSMDS
     LALSNITGAS VDGESKPRPS LYSLQNFEEI EAEDCEKMSN MGTLNSSMLH RSAESLQSLN
     SGLCPEKILP EEKPAHLPVL RRSKSQSRPQ QVKFSDDVID NGSYDIEIRQ PPMSERTRRR
     AYHFEERGSR PHHHRHRRSR KSRSDNALNL VTERKYSAKD RLRLYTPDNY EKFIQNKSAR
     ELQAYMQNAN LYSQYAHATS DYALQNPGMN RFLGLCGEDD DSWCSSSTSS SDSEEEGYFL
     GQPIPQPRPQ RFTYYTDDLS SPASALPTPQ FTQRTTKSKK KKGHKGKNCI IS
//
ID   ARHGG_MOUSE             Reviewed;         713 AA.
AC   Q3U5C8; Q501M8; Q8VCE8;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=Rho guanine nucleotide exchange factor 16;
DE   AltName: Full=Ephexin-4;
GN   Name=Arhgef16;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 206-713.
RC   STRAIN=FVB/N-3; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION.
RX   PubMed=15848799; DOI=10.1016/j.neuron.2005.01.030;
RA   Sahin M., Greer P.L., Lin M.Z., Poucher H., Eberhart J., Schmidt S.,
RA   Wright T.M., Shamah S.M., O'connell S., Cowan C.W., Hu L.,
RA   Goldberg J.L., Debant A., Corfas G., Krull C.E., Greenberg M.E.;
RT   "Eph-dependent tyrosine phosphorylation of ephexin1 modulates growth
RT   cone collapse.";
RL   Neuron 46:191-204(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234 AND TYR-585, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-111; SER-212 AND
RP   SER-234, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE32151.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; AK153708; BAE32151.1; ALT_INIT; mRNA.
DR   EMBL; BC020030; AAH20030.1; -; mRNA.
DR   EMBL; BC095966; AAH95966.1; -; mRNA.
DR   IPI; IPI00678935; -.
DR   RefSeq; NP_001106215.1; NM_001112744.1.
DR   UniGene; Mm.38481; -.
DR   ProteinModelPortal; Q3U5C8; -.
DR   SMR; Q3U5C8; 280-622, 632-692.
DR   STRING; Q3U5C8; -.
DR   PhosphoSite; Q3U5C8; -.
DR   PRIDE; Q3U5C8; -.
DR   Ensembl; ENSMUST00000030898; ENSMUSP00000030898; ENSMUSG00000029032.
DR   GeneID; 230972; -.
DR   KEGG; mmu:230972; -.
DR   UCSC; uc008wbr.1; mouse.
DR   CTD; 230972; -.
DR   MGI; MGI:2446219; Arhgef16.
DR   eggNOG; roNOG09215; -.
DR   GeneTree; ENSGT00550000074493; -.
DR   HOGENOM; HBG714039; -.
DR   HOVERGEN; HBG059167; -.
DR   InParanoid; Q3U5C8; -.
DR   OrthoDB; EOG4FXR77; -.
DR   NextBio; 380332; -.
DR   ArrayExpress; Q3U5C8; -.
DR   Bgee; Q3U5C8; -.
DR   CleanEx; MM_ARHGEF16; -.
DR   Genevestigator; Q3U5C8; -.
DR   GermOnline; ENSMUSG00000029032; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00741; DH_1; FALSE_NEG.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Guanine-nucleotide releasing factor; Phosphoprotein; SH3 domain.
FT   CHAIN         1    713       Rho guanine nucleotide exchange factor
FT                                16.
FT                                /FTId=PRO_0000233691.
FT   DOMAIN      288    472       DH.
FT   DOMAIN      505    624       PH.
FT   DOMAIN      633    693       SH3.
FT   MOD_RES       6      6       Phosphoserine.
FT   MOD_RES      41     41       Phosphoserine (By similarity).
FT   MOD_RES     111    111       Phosphoserine.
FT   MOD_RES     212    212       Phosphoserine.
FT   MOD_RES     231    231       Phosphoserine (By similarity).
FT   MOD_RES     234    234       Phosphoserine.
FT   MOD_RES     581    581       Phosphoserine (By similarity).
FT   MOD_RES     585    585       Phosphotyrosine.
FT   CONFLICT    538    538       L -> V (in Ref. 2; AAH20030/AAH95966).
SQ   SEQUENCE   713 AA;  80395 MW;  44EA7596FD3D5620 CRC64;
     MSQRHSDSSL DEKLLEYRFH AELRLDANGN PIPGLPMVRS SLKARANAAF EPDASEPLPP
     PPSPEDEEPP RPIVLSTQSP AALKMGTQQL IPKSLAVASK AKTKSPARHQ SFGAAVLSKE
     AARRNPQLFS APSFSLDDMD MDMVTTGNLR RNLRNQSYRA AMKGPGPPSS KGDSVQLGPK
     LQALAEEAAQ PPSRYPAKNK KTLGRKRAHK GSFKDDPQLY QEIRERGLNT SHESDDDILD
     EPSGPVGTQR ADTTIVVKSY RPAQLTWSQL PEVLESGVLD TLSTEERKRQ EAIFEILTSE
     FSYLHSLSIL VTEFLQSREL RATMTQTEHH HLFSNILDVM SASQKFFEAL EQRHKAQVCV
     EDISDILEDH AQHHFHPYIA YCSNEVYQQR TLQKLSNSNA AFRDVLKEIE KRPACGGLPM
     ISFLILPMQR VTRLPLLTDT LCLKTQGHPE RYKAASQALK AISKLVKQCN EGAHKMERTE
     QIYTLNMQLD FGKVKSLPLI SASRWLLKRG ELFLLEESSI FRKIASRPTC YLFLFNDLLV
     VTKKKSEESY LVQDYAQLDH VQVRKLEPSE PLLPGGSSRS SSVPYPFQVN LLHNSEGRQE
     QILLSSDSAS DRARWITALT YKERQWQGIT NKGELPQVEV TKAYFAKQAD EITLQQADIV
     LVLQEEDGWL HGERLRDGET GWFPESFAHS ITSRVAVEGN VRRMERLRVE TDV
//
ID   Q3U6A2_MOUSE            Unreviewed;       636 AA.
AC   Q3U6A2;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 37.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Rbm14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK153230; BAE31823.1; -; mRNA.
DR   IPI; IPI00404707; -.
DR   UniGene; Mm.276338; -.
DR   UniGene; Mm.441002; -.
DR   ProteinModelPortal; Q3U6A2; -.
DR   SMR; Q3U6A2; 1-198.
DR   STRING; Q3U6A2; -.
DR   HOVERGEN; HBG053180; -.
DR   Genevestigator; Q3U6A2; -.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   636 AA;  66126 MW;  DA636C71658AB548 CRC64;
     MKIFVGNVDG ADTTPEELAA LFAPYGTVMS CAVMKQFAFV HMRENAGAVR AIEALHGHEL
     RPGRALVVEM SRPRPLNTWK IFVGNVSAAC TSQELRSLFE RRGRVIECDV VKDYAFVHME
     KEADAKAAIA QLNGKEVKGK RINVELSTKG QKKGPALAIN STGGFDGQAR QPTPPFFGRD
     RSPLRRSPPR ASYVAPLTAQ PATYRAQPSV SLGAAYRAQP SASLGVGYRT QPMAAQAASY
     RAQPSVSLGA PYRGQLASPS SQSAAASSLG PYGGVQPSAS ALSTYGGQAA AASSLNSYGA
     QGSSLASYGN QPSSYGAQAA SSYGVRAAAS SYNTQGAASS LGSYGAQAAS YGAQSAASSL
     AYGAQAASYS AQPSASYSAQ SAPYAAQQAA SYSSQPAAYV AQPATAAAYA SQPAAYAAQA
     TTPMAGSYGA QPVVQTQLNS YGAQASIGLS GSYGAQSAAA ATGSYGAAAA YGAQPSATLA
     APYRTQSSAS LAASYAAQQH PQAAASYRGQ PGSAYDGTGQ PSAAYLSMSQ GAVANANSTP
     PPYERTRLSP PRASYDDPYK KAVAMSKRYG SDRRLAELSD YRRLSESQLS FRRSPTKSSL
     DYRRLPDAHS DYARYSGSYN DYLRAAQMHS GYQRRM
//
ID   ESYT1_MOUSE             Reviewed;        1092 AA.
AC   Q3U7R1; Q8C8R1; Q91X62; Q9CVH0; Q9Z1X5; Q9Z1X6;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Extended synaptotagmin-1;
DE            Short=E-Syt1;
DE   AltName: Full=Membrane-bound C2 domain-containing protein;
GN   Name=Esyt1; Synonyms=Fam62a, Mbc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-632 AND 955-1092 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Retina, and Small intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 392-1092 (ISOFORM 1).
RC   TISSUE=Mammary gland;
RX   MEDLINE=99280327; PubMed=10350628; DOI=10.1016/S0167-4838(99)00068-0;
RA   Morris N.J., Ross S.A., Neveu J.M., Lane W.S., Lienhard G.E.;
RT   "Cloning and preliminary characterization of a 121 kDa protein with
RT   multiple predicted C2 domains.";
RL   Biochim. Biophys. Acta 1431:525-530(1999).
CC   -!- FUNCTION: May play a role as calcium-regulated intrinsic membrane
CC       protein (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC       Endomembrane system; Multi-pass membrane protein (By similarity).
CC       Note=Localizes to intracellular membranes (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3U7R1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3U7R1-2; Sequence=VSP_018278, VSP_018279;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the extended synaptotagmin family.
CC   -!- SIMILARITY: Contains 5 C2 domains.
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DR   EMBL; AK008224; BAB25542.1; -; mRNA.
DR   EMBL; AK044656; BAC32020.1; -; mRNA.
DR   EMBL; AK152482; BAE31254.1; -; mRNA.
DR   EMBL; AK152554; BAE31308.1; -; mRNA.
DR   EMBL; BC011482; AAH11482.1; -; mRNA.
DR   EMBL; AF098633; AAD10189.1; -; mRNA.
DR   EMBL; AF098634; AAD10190.1; -; mRNA.
DR   IPI; IPI00128450; -.
DR   IPI; IPI00756325; -.
DR   RefSeq; NP_035973.1; NM_011843.2.
DR   UniGene; Mm.66056; -.
DR   ProteinModelPortal; Q3U7R1; -.
DR   SMR; Q3U7R1; 319-437, 468-570, 633-887, 955-1091.
DR   DIP; DIP-48746N; -.
DR   STRING; Q3U7R1; -.
DR   PhosphoSite; Q3U7R1; -.
DR   PRIDE; Q3U7R1; -.
DR   Ensembl; ENSMUST00000026427; ENSMUSP00000026427; ENSMUSG00000025366.
DR   Ensembl; ENSMUST00000105234; ENSMUSP00000100867; ENSMUSG00000025366.
DR   GeneID; 23943; -.
DR   KEGG; mmu:23943; -.
DR   UCSC; uc007hng.1; mouse.
DR   UCSC; uc007hnh.1; mouse.
DR   CTD; 23943; -.
DR   MGI; MGI:1344426; Esyt1.
DR   eggNOG; roNOG04137; -.
DR   GeneTree; ENSGT00550000074417; -.
DR   HOGENOM; HBG446028; -.
DR   HOVERGEN; HBG055795; -.
DR   InParanoid; Q3U7R1; -.
DR   OMA; SFLIRKP; -.
DR   OrthoDB; EOG44F68F; -.
DR   PhylomeDB; Q3U7R1; -.
DR   NextBio; 303753; -.
DR   ArrayExpress; Q3U7R1; -.
DR   Bgee; Q3U7R1; -.
DR   CleanEx; MM_MBC2; -.
DR   Genevestigator; Q3U7R1; -.
DR   GermOnline; ENSMUSG00000025366; Mus musculus.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   Pfam; PF00168; C2; 5.
DR   PRINTS; PR00360; C2DOMAIN.
DR   SMART; SM00239; C2; 5.
DR   SUPFAM; SSF49562; C2_CaLB; 5.
DR   PROSITE; PS50004; C2; 5.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Coiled coil; Membrane;
KW   Phosphoprotein; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN         1   1092       Extended synaptotagmin-1.
FT                                /FTId=PRO_0000234345.
FT   TRANSMEM     53     73       Helical; (Potential).
FT   TRANSMEM    235    255       Helical; (Potential).
FT   DOMAIN      306    407       C2 1.
FT   DOMAIN      455    548       C2 2.
FT   DOMAIN      621    722       C2 3.
FT   DOMAIN      772    864       C2 4.
FT   DOMAIN      950   1065       C2 5.
FT   COMPBIAS    910    921       Poly-Ser.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     804    804       N6-acetyllysine (By similarity).
FT   MOD_RES     809    809       Phosphotyrosine (By similarity).
FT   MOD_RES     951    951       Phosphoserine (By similarity).
FT   MOD_RES     997    997       Phosphotyrosine (By similarity).
FT   VAR_SEQ     852    893       VRGEGTGTLGSVSLPLSELLQEDQLCLDHWFALSGQGQVLM
FT                                R -> ACFIHLLFLFERGREQRTVFEFEVFGVNSFPPCGNL
FT                                WATAHS (in isoform 2).
FT                                /FTId=VSP_018278.
FT   VAR_SEQ     894   1092       Missing (in isoform 2).
FT                                /FTId=VSP_018279.
FT   CONFLICT    385    385       G -> R (in Ref. 2; BAC32020).
FT   CONFLICT    392    394       VFD -> IQH (in Ref. 3; AAD10190).
FT   CONFLICT    829    841       APVWEESASFLIR -> GFGLEAKIRHEGG (in Ref.
FT                                3; AAD10189).
SQ   SEQUENCE   1092 AA;  121554 MW;  71A397EC52DE6DA9 CRC64;
     MEHSPEEGAS PEPSGQPPAT DSTRDGGSGV PPAGPGAASE ALAVLTSFGR RLLVLVPVYL
     AGAAGLSVGF VLFGLALYLG WRRVRDGKER SLRAARQLLD DEERITAETL YMSHRELPAW
     VSFPDVEKAE WLNKIVAQVW PFLGQYMEKL LAETVAPAVR GANPHLQTFT FTRVELGEKP
     LRIIGVKVHP SQRKDQILLD LNVSYVGDVQ IDVEVKKYFC KAGVKGMQLH GVLRVILEPL
     TGDLPIVGAV SMFFIKRPTL DINWTGMTNL LDIPGLSSLS DTMIMDSIAA FLVLPNRLLV
     PLVPDLQDVA QLRSPLPRGI IRIHLLAARG LSSKDKYVKG LIEGKSDPYA LVRVGTQTFC
     SRVIDEELNP HWGETYEVIV HEVPGQEIEV EVFDKDPDKD DFLGRMKLDV GKVLQAGVLD
     NWYPLQGGQG QVHLRLEWLS LLPDAEKLDQ VLQWNRGITS RPEPPSAAIL VVYLDRAQDL
     PLKKGNKEPN PMVQLSVQDV TRESKATYST NSPVWEEAFR FFLQDPRSQE LDVQVKDDSR
     ALTLGALTLP LARLLTASEL TLDQWFQLSS SGPNSRLYMK LVMRILYLDY SEIRFPTVPG
     AQDWDRESLE TGSSVDAPPR PYHTTPNSHF GTENVLRIHV LEAQDLIAKD RFLGGLVKGK
     SDPYVKLKVA GKSFRTHVVR EDLNPRWNEV FEVIVTSIPG QELEIEVFDK DLDKDDFLGR
     YKVSLTTVLN SGFLDEWLTL EDVPSGRLHL RLERLTPRPT AAELEEVLQV NSLIQTQKSS
     ELAAALLSVF LERAEDLPLR KGTKPPSPYA TITVGETSHK TKTVSQSSAP VWEESASFLI
     RKPHAESLEL QVRGEGTGTL GSVSLPLSEL LQEDQLCLDH WFALSGQGQV LMRAQLGILV
     SQHSGVEAHS HSYSHSHSSS SLNDEPEALG GPTHPASPVL EVRHRLTHGD SPSEAPVGPL
     GQVKLTVWYH SDEQKLISII HSCRALRQNG RDLPDPYVSV LLLPDKNRST KRKTPQKKRT
     LNPEFNERFE WDLPLDGTLR RKLDVSVKSN SSFMSREREL LGKVQLDLAE IDLSQGAAQW
     YDLMDDRDKG GS
//
ID   Q3U832_MOUSE            Unreviewed;       723 AA.
AC   Q3U832;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 40.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Ccnt2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the cyclin family.
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DR   EMBL; AK152399; BAE31187.1; -; mRNA.
DR   IPI; IPI00654257; -.
DR   UniGene; Mm.268672; -.
DR   UniGene; Mm.392269; -.
DR   ProteinModelPortal; Q3U832; -.
DR   SMR; Q3U832; 7-259.
DR   STRING; Q3U832; -.
DR   PRIDE; Q3U832; -.
DR   Ensembl; ENSMUST00000027587; ENSMUSP00000027587; ENSMUSG00000026349.
DR   MGI; MGI:1920199; Ccnt2.
DR   eggNOG; roNOG04958; -.
DR   HOGENOM; HBG716334; -.
DR   HOVERGEN; HBG050843; -.
DR   InParanoid; Q3U832; -.
DR   OrthoDB; EOG40P469; -.
DR   PhylomeDB; Q3U832; -.
DR   ArrayExpress; Q3U832; -.
DR   Bgee; Q3U832; -.
DR   Genevestigator; Q3U832; -.
DR   InterPro; IPR006670; Cyclin.
DR   InterPro; IPR011028; Cyclin-like.
DR   InterPro; IPR013763; Cyclin-related.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR015429; Tscrpt_reg_cyclin.
DR   Gene3D; G3DSA:1.10.472.10; Cyclin_related; 1.
DR   PANTHER; PTHR10026; Trans_reg_cyclin; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   SMART; SM00385; CYCLIN; 2.
DR   SUPFAM; SSF47954; Cyclin_like; 1.
PE   2: Evidence at transcript level;
KW   Cyclin.
SQ   SEQUENCE   723 AA;  80236 MW;  D41F3F2E83442862 CRC64;
     MASGRGASSR WFFTREQLEN TPSRRCGVEA DEELSHRQQA ANLIQDMGQR LNVSQLTINT
     AIVYMHRFYM HHSFTKFNRN IISPTALFLA AKVEEQARKL EHVIKVAHAC LHPLEPLLDT
     KCDAYLQQTQ EMVLLETIML QTLGLEITIE HPHTDVVKCT QLVRASKDLA QTSYFMATNS
     LHLTTFCLQY KPTVIACVCI HLACKWSNWE IPVSTDGKHW WEYVDPTVTL ELLDELTHEF
     LQILEKTPSR LKRIRNWRAM AKKPKVDGQV SETPLLGSSL VQNSILVDSV TGVPANPSFQ
     KPSTSTFPAP IPLNSGSTSV QDSRASDNLS VLAAGMPSTS YSLSSHQEWP QHPDSARTDP
     VYTQKQEATL SGSQYISFQQ GPSMALHSGL HHRPDKVADH SSAKQEYTHK AGSSKHHGPI
     PATPGMLPQK MSLDKYREKR KLETLDVDTR DHYLAAHAEQ QHKHGPAQAV TGTSVTSPIK
     MKLPLTNSDR PEKHVAEKKE RSGSLKLRIP IPPPDKGPSK EELKMKIKVA SSERHSSSDE
     GSGKSKHSSP HISRDHKEKH KEHPANRHHS SHKYLHMHSG GSKHTADGMP PTVLRSPVGL
     GPEGVSSASS ARKKLHSSEA SHNHHSKMSK SSKSAGSSSS SSSVKQYLSS HSSVFNHPLP
     PPPPVTYQVG YGHLSTLVKL DKKPVEPHGP EANHEYSTSS QHMDYKDTFD MLDSLLSAQG
     MNM
//
ID   Q3U8W9_MOUSE            Unreviewed;       632 AA.
AC   Q3U8W9;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   11-JAN-2011, entry version 47.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Hnrnpr; Synonyms=Hnrpr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK152039; BAE30898.1; -; mRNA.
DR   IPI; IPI00128441; -.
DR   UniGene; Mm.31051; -.
DR   UniGene; Mm.443495; -.
DR   UniGene; Mm.475583; -.
DR   ProteinModelPortal; Q3U8W9; -.
DR   SMR; Q3U8W9; 333-457.
DR   STRING; Q3U8W9; -.
DR   Ensembl; ENSMUST00000084219; ENSMUSP00000081239; ENSMUSG00000066037.
DR   Ensembl; ENSMUST00000105850; ENSMUSP00000101476; ENSMUSG00000066037.
DR   MGI; MGI:1891692; Hnrnpr.
DR   HOGENOM; HBG713144; -.
DR   HOVERGEN; HBG051917; -.
DR   InParanoid; Q3U8W9; -.
DR   ArrayExpress; Q3U8W9; -.
DR   Bgee; Q3U8W9; -.
DR   Genevestigator; Q3U8W9; -.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   InterPro; IPR006535; HnRNP_R/Q_splicing_fac.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 3.
DR   Pfam; PF00076; RRM_1; 3.
DR   SMART; SM00360; RRM; 3.
DR   TIGRFAMs; TIGR01648; hnRNP-R-Q; 1.
DR   PROSITE; PS50102; RRM; 3.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   632 AA;  70878 MW;  BC07B5802830D099 CRC64;
     MANQVNGNAV QLKEEEEPMD TSSVTHTEHY KTLIEAGLPQ KVAERLDEIF QTGLVAYVDL
     DERAIDALRE FNEEGALSVL QQFKESDLSH VQNKSAFLCG VMKTYRQREK QGSKVQESTK
     GPDEAKIKAL LERTGYTLDV TTGQRKYGGP PPDSVYSGVQ PGIGTEVFVG KIPRDLYEDE
     LVPLFEKAGP IWDLRLMMDP LSGQNRGYAF ITFCGKEAAQ EAVKLCDSYE IRPGKHLGVC
     ISVANNRLFV GSIPKNKTKE NILEEFSKVT EGLVDVILYH QPDDKKKNRG FCFLEYEDHK
     SAAQARRRLM SGKVKVWGNV VTVEWADPVE EPDPEVMAKV KVLFVRNLAT TVTEEILEKS
     FSEFGKLERV KKLKDYAFVH FEDRGAAVKA MDEMNGKEIE GEEIEIVLAK PPDKKRKERQ
     AARQASRSTA YEDYYYHPPP RMSPPMRGRG RGGRGGYGYP PDYYGYEDYY DDYYGYDYHD
     YRGGYEDPYY GYDDGYAVRG RGGGRGGRGA PPPPRGRGAP PPRGRAGYSQ RGAPLGPPRG
     SRGGRGGPAQ QQRGRGSRGA RGNRGGNVGG KRKADGYNQP DSKRRQTNNQ QNWGSQPIAQ
     QPLQQGGDYS GNYGYNNDNQ EFYQDTYGQQ WK
//
ID   Q3U931_MOUSE            Unreviewed;       448 AA.
AC   Q3U931;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 46.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=G3bp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK151965; BAE30836.1; -; mRNA.
DR   IPI; IPI00331295; -.
DR   UniGene; Mm.290530; -.
DR   UniGene; Mm.473827; -.
DR   ProteinModelPortal; Q3U931; -.
DR   SMR; Q3U931; 5-139.
DR   STRING; Q3U931; -.
DR   Ensembl; ENSMUST00000113127; ENSMUSP00000108752; ENSMUSG00000029405.
DR   MGI; MGI:2442040; G3bp2.
DR   HOVERGEN; HBG007211; -.
DR   ArrayExpress; Q3U931; -.
DR   Bgee; Q3U931; -.
DR   Genevestigator; Q3U931; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006810; P:transport; IEA:InterPro.
DR   InterPro; IPR002075; NTF2.
DR   InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF02136; NTF2; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50177; NTF2_DOMAIN; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   448 AA;  50647 MW;  38F8EF25738C0299 CRC64;
     MVMEKPSPLL VGREFVRQYY TLLNKAPEYL HRFYGRNSSY VHGGVDASGK PQEAVYGQND
     IHHKVLSLNF SECHTKIRHV DAHATLSDGV VVQVMGLLSN SGQPERKFMQ TFVLAPEGSV
     PNKFYVHNDM FRYEDEVFGD SEPELDEESE DEVEEEQEDR QPSPEPVQEN ANSAYYDAHP
     VTNGIEEPLE ESSHEPEPEP ESETKTEELK PQVEEKHLEE LEEKSATPPP AEPASLPQEP
     PKPRVDAKPE VQSQPPRVRE QRPRERPGFP PRGPRPGRGD MEQNDSDNRR IIRYPDSQLF
     VGNLPHDIDE NELKEFFMSF GNVVELRINT KGVGGKLPNF GFVVFDDSEP VQRILIAKPI
     MFRGEVRLNV EEKKTRAARE RETRGGGDDR RDIRRNDRGP GGPRGIVGGG MMRDRDGRGP
     PPRGGMTQKL GSGRGTGQME GRFTGQRR
//
ID   Q3U955_MOUSE            Unreviewed;       452 AA.
AC   Q3U955;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 40.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Tmpo;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK151936; BAE30812.1; -; mRNA.
DR   IPI; IPI00828976; -.
DR   UniGene; Mm.159684; -.
DR   UniGene; Mm.439157; -.
DR   ProteinModelPortal; Q3U955; -.
DR   SMR; Q3U955; 1-158.
DR   STRING; Q3U955; -.
DR   Ensembl; ENSMUST00000072239; ENSMUSP00000072092; ENSMUSG00000019961.
DR   MGI; MGI:106920; Tmpo.
DR   HOVERGEN; HBG000166; -.
DR   ArrayExpress; Q3U955; -.
DR   Bgee; Q3U955; -.
DR   Genevestigator; Q3U955; -.
DR   GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0045449; P:regulation of transcription; IDA:MGI.
DR   InterPro; IPR003887; LEM.
DR   InterPro; IPR011015; LEM-like_dom.
DR   InterPro; IPR013146; Thymopoietin_LEM.
DR   Gene3D; G3DSA:1.10.720.40; LEM; 2.
DR   Pfam; PF03020; LEM; 1.
DR   Pfam; PF08198; Thymopoietin; 1.
DR   SMART; SM00540; LEM; 1.
DR   SUPFAM; SSF63451; LEM_like; 2.
DR   PROSITE; PS50954; LEM; 1.
DR   PROSITE; PS50955; LEM_LIKE; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   452 AA;  50471 MW;  BA859E532178E400 CRC64;
     MPEFLEDPSV LTKDKLKSEL VANNVTLPAG EQRKDVYVQL YLQHLTARNR PPLAAGANSK
     GPPDFSSDEE REPTPVLGSG ASVGRGRGAV RRKATKKTDK PRLEDKDDLD VTELSNEQLL
     DQLVRYGVNP GPIVGTTRKL YEKKLLKLRE QGTESRSSTP LPTVSSSAEN TRQNGSNDSD
     RYSDNDEDSK IELKLEKREP LKGRAKTPVT LKQRRTEHNQ SYSQAGVTET EWTSGSSTGG
     PLQALTREST RGSRRTPRKR VETSQHFRID GAVISESTPI AETIKASSNE SLVANRLTGN
     FKHASSILPI TEFSDITRRT PKKPLTRAEV GEKTEERRVD RDILKEMFPY EASTPTGISA
     SCRRPIKGAA GRPLELSDFR MEESFSSKYV PKYAPLADVK SEKTKKRRSV PMWIKMLLFA
     LVAVFLFLVY QAMETNQGNP FTNFLQDTKI SN
//
ID   Q3UBP6_MOUSE            Unreviewed;       375 AA.
AC   Q3UBP6;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Actb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells (By similarity).
CC   -!- SIMILARITY: Belongs to the actin family.
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DR   EMBL; AK150866; BAE29918.1; -; mRNA.
DR   IPI; IPI00110850; -.
DR   UniGene; Mm.328431; -.
DR   UniGene; Mm.391967; -.
DR   ProteinModelPortal; Q3UBP6; -.
DR   SMR; Q3UBP6; 2-375.
DR   STRING; Q3UBP6; -.
DR   Ensembl; ENSMUST00000031564; ENSMUSP00000031564; ENSMUSG00000029580.
DR   HOVERGEN; HBG003771; -.
DR   InParanoid; Q3UBP6; -.
DR   ArrayExpress; Q3UBP6; -.
DR   Bgee; Q3UBP6; -.
DR   Genevestigator; Q3UBP6; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004000; Actin-like.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding.
SQ   SEQUENCE   375 AA;  41769 MW;  5A85E54CA8EE48F3 CRC64;
     MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS
     KRGILTLKYP IEHGIITNWD DMEKIWHHTF YNELRVAPEE HPMLLTEAPL NPKANREKMT
     QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL
     AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY
     ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS
     GGTTMYPGIA DRMQKEVTAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ
     EYDESGPSIV HRKCF
//
ID   FOXK2_MOUSE             Reviewed;         651 AA.
AC   Q3UCQ1; A2AN27;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Forkhead box protein K2;
DE   AltName: Full=Cellular transcription factor ILF-1;
DE   AltName: Full=Interleukin enhancer-binding factor 1;
GN   Name=Foxk2; Synonyms=Ilf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 69-651 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=16376864; DOI=10.1016/j.brainres.2005.11.022;
RA   Wijchers P.J.E.C., Hoekman M.F.M., Burbach J.P.H., Smidt M.P.;
RT   "Identification of forkhead transcription factors in cortical and
RT   dopaminergic areas of the adult murine brain.";
RL   Brain Res. 1068:23-33(2006).
CC   -!- FUNCTION: Recognizes the core sequence 5'-TAAACA-3'. Binds to
CC       NFAT-like motifs (purine-rich) in the IL2 promoter (By
CC       similarity).
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UCQ1-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q3UCQ1-2; Sequence=VSP_052236;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in a wide range of adult brain
CC       regions, namely the piriform cortex, the major islands of Calleja
CC       and cells lining the lateral ventricles, the bed nucleus of stria
CC       terminalis, the paraventricular thalamic nucleus, habenula and all
CC       structures of the hippocampus. Also present in the hypothalamus,
CC       cerebral cortex and in the Purkinje cell layer in the cerebellum.
CC       Additionally expressed in dopamine neurons of the substantia and
CC       more sparsely in the ventral tegmental area.
CC   -!- DEVELOPMENTAL STAGE: At E12.5, expressed ubiquitously in the
CC       developing central nervous system. This pattern persists at E14.5
CC       and E16.5, with expression levels varying.
CC   -!- DOMAIN: The C-terminal part of the DNA-binding domain may
CC       contribute to DNA recognition specificity (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 FHA domain.
CC   -!- SIMILARITY: Contains 1 fork-head DNA-binding domain.
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DR   EMBL; AL808021; CAM21743.1; -; Genomic_DNA.
DR   EMBL; AK150439; BAE29561.1; -; mRNA.
DR   IPI; IPI00808277; -.
DR   IPI; IPI00854998; -.
DR   RefSeq; NP_001074401.2; NM_001080932.2.
DR   UniGene; Mm.209750; -.
DR   HSSP; Q01167; 2C6Y.
DR   ProteinModelPortal; Q3UCQ1; -.
DR   SMR; Q3UCQ1; 247-344.
DR   PhosphoSite; Q3UCQ1; -.
DR   PRIDE; Q3UCQ1; -.
DR   Ensembl; ENSMUST00000038442; ENSMUSP00000042001; ENSMUSG00000039275.
DR   Ensembl; ENSMUST00000106113; ENSMUSP00000101719; ENSMUSG00000039275.
DR   Ensembl; ENSMUST00000106114; ENSMUSP00000101720; ENSMUSG00000039275.
DR   GeneID; 68837; -.
DR   KEGG; mmu:68837; -.
DR   UCSC; uc007mvs.1; mouse.
DR   CTD; 68837; -.
DR   MGI; MGI:1916087; Foxk2.
DR   GeneTree; ENSGT00600000084380; -.
DR   HOGENOM; HBG402857; -.
DR   HOVERGEN; HBG051649; -.
DR   InParanoid; Q3UCQ1; -.
DR   OrthoDB; EOG4XD3QX; -.
DR   ArrayExpress; Q3UCQ1; -.
DR   Bgee; Q3UCQ1; -.
DR   CleanEx; MM_FOXK2; -.
DR   Genevestigator; Q3UCQ1; -.
DR   GermOnline; ENSMUSG00000039275; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR008984; SMAD_FHA_domain.
DR   InterPro; IPR001766; TF_fork_head.
DR   InterPro; IPR018122; TF_fork_head_CS.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:2.60.200.20; FHA; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   PANTHER; PTHR11829; Fork_box_protein; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF00250; Fork_head; 1.
DR   PRINTS; PR00053; FORKHEAD.
DR   SMART; SM00339; FH; 1.
DR   SMART; SM00240; FHA; 1.
DR   SUPFAM; SSF49879; SMAD_FHA; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS00657; FORK_HEAD_1; 1.
DR   PROSITE; PS00658; FORK_HEAD_2; 1.
DR   PROSITE; PS50039; FORK_HEAD_3; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; DNA-binding; Magnesium; Metal-binding; Nucleus;
KW   Phosphoprotein; Transcription.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    651       Forkhead box protein K2.
FT                                /FTId=PRO_0000261668.
FT   DOMAIN       48    119       FHA.
FT   DNA_BIND    249    344       Fork-head.
FT   REGION      291    309       DNA-binding; major groove (By
FT                                similarity).
FT   REGION      319    323       DNA-binding; minor groove (By
FT                                similarity).
FT   REGION      339    344       DNA-binding; minor groove (By
FT                                similarity).
FT   METAL       301    301       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       302    302       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       304    304       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       307    307       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   MOD_RES      24     24       Phosphoserine (By similarity).
FT   MOD_RES      55     55       Phosphoserine (By similarity).
FT   MOD_RES     230    230       Phosphoserine (By similarity).
FT   MOD_RES     389    389       Phosphoserine (By similarity).
FT   MOD_RES     419    419       Phosphoserine (By similarity).
FT   VAR_SEQ     517    586       Missing (in isoform 2).
FT                                /FTId=VSP_052236.
FT   CONFLICT    104    104       M -> L (in Ref. 1; CAM21743).
SQ   SEQUENCE   651 AA;  68464 MW;  2AD83C2AC41A8B40 CRC64;
     MAAAAALSGA GAPPAGGGAG GGGSPPGGWA VARLEGREFE YLMKKRSVTI GRNSSQGSVD
     VSMGHSSFIS RRHLEIFTPP GGGHSAAAPE PAQPRPDAGG DFYMRCLGKN GVFVDGVFQR
     RGAPPLQLPR VCTFRFPSTN IKITFTALSS EKREKQEAPE SPVKPVQPHI SPLTINIPDT
     MAHLISPLPS PTGTISAANS CPSSPRGAGS SGYKVGRVMP SDLSLMADNS QPENEKEASG
     GDSPKDDSKP PYSYAQLIVQ AITMAPDKQL TLNGIYTHIT KNYPYYRTAD KGWQNSIRHN
     LSLNRYFIKV PRSQEEPGKG SFWRIDPASE SKLVEQAFRK RRPRGVPCFR TPLGPLSSRS
     APASPNHAGV LSAHSSGAQT PESLSREGSP APLEPEPGAS QPKLAVIQEA RFAQSAPGSP
     LSSQPVLITV QRQLPPAIKP VTYTVATPVT TPTSQPPVVQ TVHVVHQIPA VSVTSVAGLA
     PANTYTVAGQ AVVTQAAVLA PPNPEPQENG DHREVRVKVE PVPAISPATL GAASRIIQTS
     QGTPVQTVTI VQQAPLGQHQ LPIKTVTQNG AHVVPMPTAV HSQVNNAAAS PLHMLATHAS
     ASASLPTKRQ NGDQAEQPEL KRVKAEDGES IVIALSVDAP PAAVREKAIQ N
//
ID   TTL12_MOUSE             Reviewed;         639 AA.
AC   Q3UDE2; Q7TPC3;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Tubulin--tyrosine ligase-like protein 12;
GN   Name=Ttll12;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=17499049; DOI=10.1016/j.molcel.2007.04.012;
RA   van Dijk J., Rogowski K., Miro J., Lacroix B., Edde B., Janke C.;
RT   "A targeted multienzyme mechanism for selective microtubule
RT   polyglutamylation.";
RL   Mol. Cell 26:437-448(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C3H/He; TISSUE=Osteoblast;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- TISSUE SPECIFICITY: Widely expressed with highest levels in brain,
CC       kidney, liver, lung, muscle and testis.
CC   -!- SIMILARITY: Contains 1 TTL domain.
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DR   EMBL; AM690756; CAM84333.1; -; mRNA.
DR   EMBL; AK150116; BAE29319.1; -; mRNA.
DR   EMBL; AL583887; CAO77935.1; -; Genomic_DNA.
DR   EMBL; BC055368; AAH55368.1; -; mRNA.
DR   IPI; IPI00379876; -.
DR   RefSeq; NP_898838.2; NM_183017.2.
DR   UniGene; Mm.46778; -.
DR   ProteinModelPortal; Q3UDE2; -.
DR   STRING; Q3UDE2; -.
DR   PhosphoSite; Q3UDE2; -.
DR   PRIDE; Q3UDE2; -.
DR   Ensembl; ENSMUST00000016901; ENSMUSP00000016901; ENSMUSG00000016757.
DR   GeneID; 223723; -.
DR   KEGG; mmu:223723; -.
DR   NMPDR; fig|10090.3.peg.30378; -.
DR   UCSC; uc007xbh.1; mouse.
DR   CTD; 223723; -.
DR   MGI; MGI:3039573; Ttll12.
DR   eggNOG; roNOG11813; -.
DR   GeneTree; ENSGT00390000006760; -.
DR   HOGENOM; HBG447213; -.
DR   HOVERGEN; HBG055617; -.
DR   InParanoid; Q3UDE2; -.
DR   OMA; PTFFNDV; -.
DR   OrthoDB; EOG4Q84X3; -.
DR   PhylomeDB; Q3UDE2; -.
DR   NextBio; 376848; -.
DR   ArrayExpress; Q3UDE2; -.
DR   Bgee; Q3UDE2; -.
DR   CleanEx; MM_TTLL12; -.
DR   Genevestigator; Q3UDE2; -.
DR   GO; GO:0004835; F:tubulin-tyrosine ligase activity; IEA:InterPro.
DR   GO; GO:0006464; P:protein modification process; IEA:InterPro.
DR   InterPro; IPR004344; Tub_tyr_ligase.
DR   PANTHER; PTHR12241; Tub_tyr_ligase; 1.
DR   Pfam; PF03133; TTL; 1.
DR   PROSITE; PS51221; TTL; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    639       Tubulin--tyrosine ligase-like protein 12.
FT                                /FTId=PRO_0000326166.
FT   DOMAIN      295    639       TTL.
FT   MOD_RES      11     11       Phosphoserine.
FT   CONFLICT     65     65       M -> K (in Ref. 4; AAH55368).
SQ   SEQUENCE   639 AA;  74043 MW;  584D72AA05BCA837 CRC64;
     MEIQSGPQPG SPGRAERLNA RLLDEFVSLH GPTLRASGVP ERLWGRLLHK LEHEVFDAGE
     MFGIMQVEEV EEAEDEAARE AQRKQPNPGG ELCYKVIVTS ESGVRADDPN SIFLIDHAWT
     CRVEHARKQL QQVPGLLHRM ANLMGIEFHG EVPSPEVVAL VLEEMWKFNQ TYQLAHGTAE
     EKVPVWYIMD EFGSRIQHSD MPSFATAPFF YMPQQVAYTL LWPLRDLDTG EEVTRDFAYG
     EADPLIRKCM LLPWAPADML DLSFSTPEPP AKYYQAILEE NKEKLPLAIS PVARPQGHVF
     RVHCDVQQVL GHLTHPRFTF TDSEADADIF FHFSHFKDYM KLSQESPQVL LNQFPCENLL
     TVKDCLASIA RRAGGPEGPP WLPRTFNLRT ELPQFVSYFQ HRERRGEDNH WICKPWNLAR
     SLDTHVTNNL HSIIRHREST PKVVSKYIES PVLFLREDVG NVKFDIRYIV LLRSVRPLRL
     FAYDVFWLRF SNRPFALDDL DDYEKHFTVM NYDPDVVLKQ VHYNEFIPQF EKQYPEFPWS
     DVQAEIFKAF TELFQVACAK PPPMGLCDYP SSRAMYAIDL MLNWDNHPDG KRVMQPQILE
     VNFNPDCERA CRYHPSFFND VFSTLFLDET DNCHVTRII
//
ID   Q3UDH4_MOUSE            Unreviewed;      1023 AA.
AC   Q3UDH4;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 36.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Sec24b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK150076; BAE29287.1; -; mRNA.
DR   IPI; IPI00331016; -.
DR   UniGene; Mm.192303; -.
DR   STRING; Q3UDH4; -.
DR   Ensembl; ENSMUST00000001079; ENSMUSP00000001079; ENSMUSG00000001052.
DR   MGI; MGI:2139764; Sec24b.
DR   HOVERGEN; HBG054850; -.
DR   InParanoid; Q3UDH4; -.
DR   OrthoDB; EOG4T782G; -.
DR   ArrayExpress; Q3UDH4; -.
DR   Bgee; Q3UDH4; -.
DR   Genevestigator; Q3UDH4; -.
DR   GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   InterPro; IPR007123; Gelsolin_dom.
DR   InterPro; IPR006900; Sec23/24_helical_dom.
DR   InterPro; IPR006896; Sec23/24_trunk_dom.
DR   InterPro; IPR012990; Sec23_24_beta_S.
DR   InterPro; IPR006895; Znf_Sec23_Sec24.
DR   Pfam; PF00626; Gelsolin; 1.
DR   Pfam; PF08033; Sec23_BS; 1.
DR   Pfam; PF04815; Sec23_helical; 1.
DR   Pfam; PF04811; Sec23_trunk; 1.
DR   Pfam; PF04810; zf-Sec23_Sec24; 1.
DR   SUPFAM; SSF81811; Sec23_helical; 1.
DR   SUPFAM; SSF82919; Znf_Sec23_Sec24; 1.
PE   2: Evidence at transcript level;
KW   Protein transport; Transport.
FT   NON_TER       1      1
SQ   SEQUENCE   1023 AA;  112069 MW;  5C96E95AA615A479 CRC64;
     PPPPPSQHQQ QQQQQQQQQQ QQQSHSGYSS LPWSGPALPP AQDSLIRNQM GSLATANSHP
     TNNENVQPPK SSSVVSTVLP GPSSTRMPPA PSHPVGPVPS APPPPEQMQT KGMQYGDYGN
     NQASSTATPL SSASDDEEEQ EEDEEAGVDS SSTTSSASPL PNSYDALEGG SYPDMHSSSA
     SSPVPDHALE PSPTLAQALS AAPTPPAAQP AKVAKPFGYG YPALQPAYQN AAPPPMPAAH
     PSGPAYTGYP QHYPGVNQLS SGLGGLSLQS SPQPESLRPV NLTQEKNILP PTPIWAPVPN
     LSAELSKLNC SPDSFRCTLT SIPQTQALLN KAKLPLGLLL HPFRDLTQLP VITSNTIVRC
     RSCRTYINPF VSFIDQRRWK CNLCYRVNDV PEEFLYNPLT RSYGEPHKRP EVQNSTVEFI
     ASSDYMLRPP QPAVYLFVLD VSHNAVEAGY LTVLCQSLLE NLDKLPGDSR TRIGFMTFDS
     TIHFYNLQEG LSQPQMLIVS DIDDVFLPTP DSLLVNLYES KELIKDLLNA LPSMFINTRE
     THSALGPALQ AAFKLMSPTG GRVSVFQTQL PSLGAGLLQS REDPNQRSST KVVHHLGPAT
     DFYKKLALDC SGQQTAVDLF LLSSQYSDLA SLACMSKYSA GCIFYYPSFH STHNPSRAEK
     LQKDLKRYLT RKIGFEAVMR IRCTKGLSMH TFHGNFFVRS NDLLSLANIN PDAGFAVQLS
     IEESLTDTAL VCFQTALLYT SSKGERRIRV HTLCLPVVSS LADVYAGVDV QAAVCLLANM
     AVDRSVSSSL SDARDALVNA VVDPLSAYSS AVASVPRSTL TAPSSLKLLP LYVLALLKQK
     AFRTGTSTRL DDRAYAMCQM KSQPLVHLMK MIHPNLYRID RLTDEGAIHV NDRVVPQPPL
     QKLSAEKLTR EGAFLMDCGS VFYIWVGKGC DSNFIENVLG YPDFASIPQK MTHLPELDTL
     PSERTRSFVT WLRDSRPLSP VLHLVKDESP AKTDFFQHLL EDRTEAALSY YEFLIHIQQQ
     VCK
//
ID   WDR41_MOUSE             Reviewed;         460 AA.
AC   Q3UDP0; Q8C4F1; Q8C8K5;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=WD repeat-containing protein 41;
GN   Name=Wdr41;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow, Cerebellum, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UDP0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UDP0-2; Sequence=VSP_016182, VSP_016183;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 6 WD repeats.
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DR   EMBL; AK046853; BAC32897.1; -; mRNA.
DR   EMBL; AK082348; BAC38474.1; -; mRNA.
DR   EMBL; AK149993; BAE29221.1; -; mRNA.
DR   IPI; IPI00227147; -.
DR   IPI; IPI00273318; -.
DR   RefSeq; NP_766178.2; NM_172590.2.
DR   UniGene; Mm.33856; -.
DR   ProteinModelPortal; Q3UDP0; -.
DR   SMR; Q3UDP0; 36-193, 221-256, 396-437.
DR   PhosphoSite; Q3UDP0; -.
DR   PRIDE; Q3UDP0; -.
DR   Ensembl; ENSMUST00000046437; ENSMUSP00000042664; ENSMUSG00000042015.
DR   Ensembl; ENSMUST00000056512; ENSMUSP00000055145; ENSMUSG00000042015.
DR   GeneID; 218460; -.
DR   KEGG; mmu:218460; -.
DR   CTD; 218460; -.
DR   MGI; MGI:2445123; Wdr41.
DR   eggNOG; roNOG10029; -.
DR   GeneTree; ENSGT00390000017026; -.
DR   HOGENOM; HBG282375; -.
DR   HOVERGEN; HBG079768; -.
DR   InParanoid; Q3UDP0; -.
DR   OMA; FFNMWGF; -.
DR   OrthoDB; EOG479F73; -.
DR   NextBio; 376304; -.
DR   ArrayExpress; Q3UDP0; -.
DR   Bgee; Q3UDP0; -.
DR   CleanEx; MM_WDR41; -.
DR   Genevestigator; Q3UDP0; -.
DR   GermOnline; ENSMUSG00000042015; Mus musculus.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 3.
DR   Pfam; PF00400; WD40; 4.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Repeat; WD repeat.
FT   CHAIN         1    460       WD repeat-containing protein 41.
FT                                /FTId=PRO_0000051391.
FT   REPEAT       40     79       WD 1.
FT   REPEAT       82    128       WD 2.
FT   REPEAT      131    168       WD 3.
FT   REPEAT      220    258       WD 4.
FT   REPEAT      321    359       WD 5.
FT   REPEAT      403    441       WD 6.
FT   VAR_SEQ     233    308       DTGFVTGSHVGELLIWDALDWTVQACERTFWSPTAQLDAQQ
FT                                EIKLFQKQNDISINHFTCDEENIFAAVGRGLYVYN -> GS
FT                                VLTMGSVLTTGSVLTIGSVLTTGSVLTMGSVLTTGSAADRR
FT                                LCADHGLCADRRLCADHGLCADCRRLCCPQALC (in
FT                                isoform 2).
FT                                /FTId=VSP_016182.
FT   VAR_SEQ     309    460       Missing (in isoform 2).
FT                                /FTId=VSP_016183.
FT   CONFLICT    135    135       T -> K (in Ref. 1; BAC32897).
SQ   SEQUENCE   460 AA;  51511 MW;  DADD97BFB0787D0F CRC64;
     MLRWLIGGGR EPQGLAEKAA LQTIGEDQGQ NPYTELLVLE AHRDIVRFLV RLDDFRFASA
     GDDGIIVVWN AQTGEKLLEL RGHTQKITAV IAFPPLDSCE ASSQLLLTAS ADRTVGVWDC
     DTGRQIQRVT CFQSTVKCLT VLQRLDIWLS GGSDLGVWNR KLDLLCKTSH LSDTGISALV
     EIPGNCVAAA VGRELIIFRL VTPTEELPEW DIIEVKRLLD HQDNILSLAN INDTGFVTGS
     HVGELLIWDA LDWTVQACER TFWSPTAQLD AQQEIKLFQK QNDISINHFT CDEENIFAAV
     GRGLYVYNLQ LKRVIACQKT AHDSNILHID KLPNRQLISC SEDGAVRMWE VREKQQLAAE
     PVPTGFFNMW GFGRVNKQAS QPVKKQEENV TTCSLELIGD LIGHSSSVEM FLYFEDHGLV
     TCSADHLIIL WKNGERESGV RSLKLFQKLE ENGDLYPESP
//
ID   HGNAT_MOUSE             Reviewed;         656 AA.
AC   Q3UDW8; Q3TWK5; Q8CBU7; Q8CIE1;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 47.
DE   RecName: Full=Heparan-alpha-glucosaminide N-acetyltransferase;
DE            EC=2.3.1.78;
DE   AltName: Full=Transmembrane protein 76;
GN   Name=Hgsnat; Synonyms=D8Ertd354e, Tmem76;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1/2).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-656 (ISOFORM 1/2).
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=16960811; DOI=10.1086/508068;
RA   Fan X., Zhang H., Zhang S., Bagshaw R.D., Tropak M.B., Callahan J.W.,
RA   Mahuran D.J.;
RT   "Identification of the gene encoding the enzyme deficient in
RT   mucopolysaccharidosis IIIC (Sanfilippo disease type C).";
RL   Am. J. Hum. Genet. 79:738-744(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-249, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-157, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Lysosomal acetyltransferase that acetylates the non-
CC       reducing terminal alpha-glucosamine residue of intralysosomal
CC       heparin or heparan sulfate, converting it into a substrate for
CC       luminal alpha-N-acetyl glucosaminidase.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + heparan sulfate alpha-D-
CC       glucosaminide = CoA + heparan sulfate N-acetyl-alpha-D-
CC       glucosaminide.
CC   -!- SUBUNIT: Homooligomer. Homooligomerization is necessary for enzyme
CC       activity (By similarity).
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane
CC       protein. Note=Colocalizes with the lysosomal marker LAMP2. The
CC       signal peptide is not cleaved upon translocation into the
CC       endoplasmic reticulum; the precursor is probably targeted to the
CC       lysosomes via the adapter protein complex-mediated pathway that
CC       involves tyrosine- and/or dileucine-based conserved amino acid
CC       motifs in the last C-terminus 16-amino acid domain (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UDW8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UDW8-2; Sequence=VSP_040505;
CC   -!- PTM: Undergoes intralysosomal proteolytic cleavage; occurs within
CC       the end of the first and/or the beginning of the second luminal
CC       domain and is essential for the activation of the enzyme (By
CC       similarity).
CC   -!- PTM: Glycosylated (By similarity).
CC   -!- MISCELLANEOUS: A signal sequence is predicted but has been shown
CC       not to be cleaved in the reticulum endoplasmic (By similarity).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH24084.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAC29006.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAE31601.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAE35261.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAE35603.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; AK035264; BAC29006.1; ALT_INIT; mRNA.
DR   EMBL; AK149883; BAE29143.1; -; mRNA.
DR   EMBL; AK152926; BAE31601.1; ALT_INIT; mRNA.
DR   EMBL; AK159649; BAE35261.1; ALT_INIT; mRNA.
DR   EMBL; AK160068; BAE35603.1; ALT_INIT; mRNA.
DR   EMBL; BC024084; AAH24084.1; ALT_INIT; mRNA.
DR   IPI; IPI00317488; -.
DR   RefSeq; NP_084160.1; NM_029884.1.
DR   UniGene; Mm.28326; -.
DR   STRING; Q3UDW8; -.
DR   PhosphoSite; Q3UDW8; -.
DR   PRIDE; Q3UDW8; -.
DR   Ensembl; ENSMUST00000037609; ENSMUSP00000040356; ENSMUSG00000037260.
DR   GeneID; 52120; -.
DR   KEGG; mmu:52120; -.
DR   UCSC; uc009lhg.1; mouse.
DR   CTD; 52120; -.
DR   MGI; MGI:1196297; Hgsnat.
DR   eggNOG; roNOG06099; -.
DR   GeneTree; ENSGT00390000001491; -.
DR   HOGENOM; HBG444972; -.
DR   HOVERGEN; HBG081599; -.
DR   InParanoid; Q3UDW8; -.
DR   OrthoDB; EOG4548Z7; -.
DR   NextBio; 308520; -.
DR   ArrayExpress; Q3UDW8; -.
DR   Bgee; Q3UDW8; -.
DR   CleanEx; MM_HGSNAT; -.
DR   Genevestigator; Q3UDW8; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR   GO; GO:0015019; F:heparan-alpha-glucosaminide N-acetyltransferase activity; IEA:EC.
DR   GO; GO:0007041; P:lysosomal transport; ISS:UniProtKB.
DR   GO; GO:0051259; P:protein oligomerization; ISS:UniProtKB.
DR   InterPro; IPR012429; DUF1624.
DR   InterPro; IPR006311; TAT_signal.
DR   Pfam; PF07786; DUF1624; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Alternative initiation; Disulfide bond; Glycoprotein;
KW   Lysosome; Membrane; Phosphoprotein; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    656       Heparan-alpha-glucosaminide N-
FT                                acetyltransferase.
FT                                /FTId=PRO_0000273154.
FT   TOPO_DOM      1    185       Lumenal, vesicle (Potential).
FT   TRANSMEM    186    206       Helical; (Potential).
FT   TOPO_DOM    207    268       Cytoplasmic (Potential).
FT   TRANSMEM    269    289       Helical; (Potential).
FT   TOPO_DOM    290    295       Lumenal, vesicle (Potential).
FT   TRANSMEM    296    316       Helical; (Potential).
FT   TOPO_DOM    317    338       Cytoplasmic (Potential).
FT   TRANSMEM    339    359       Helical; (Potential).
FT   TOPO_DOM    360    367       Lumenal, vesicle (Potential).
FT   TRANSMEM    368    388       Helical; (Potential).
FT   TOPO_DOM    389    413       Cytoplasmic (Potential).
FT   TRANSMEM    414    434       Helical; (Potential).
FT   TOPO_DOM    435    493       Lumenal, vesicle (Potential).
FT   TRANSMEM    494    514       Helical; (Potential).
FT   TOPO_DOM    515    522       Cytoplasmic (Potential).
FT   TRANSMEM    523    543       Helical; (Potential).
FT   TOPO_DOM    544    557       Lumenal, vesicle (Potential).
FT   TRANSMEM    558    578       Helical; (Potential).
FT   TOPO_DOM    579    585       Cytoplasmic (Potential).
FT   TRANSMEM    586    606       Helical; (Potential).
FT   TOPO_DOM    607    627       Lumenal, vesicle (Potential).
FT   TRANSMEM    628    648       Helical; (Potential).
FT   TOPO_DOM    649    656       Cytoplasmic (Potential).
FT   REGION      641    656       Lysosomal targeting region (By
FT                                similarity).
FT   ACT_SITE    290    290       By similarity.
FT   MOD_RES     234    234       Phosphoserine.
FT   MOD_RES     249    249       Phosphotyrosine.
FT   CARBOHYD    137    137       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    157    157       N-linked (GlcNAc...).
FT   DISULFID    146    455       By similarity.
FT   VAR_SEQ       1     32       Missing (in isoform 2).
FT                                /FTId=VSP_040505.
FT   CONFLICT     23     23       R -> H (in Ref. 2; AAH24084).
FT   CONFLICT     24     24       N -> S (in Ref. 2; AAH24084).
FT   CONFLICT    222    222       T -> A (in Ref. 2; AAH24084).
FT   CONFLICT    242    242       A -> G (in Ref. 1; BAE35261).
FT   CONFLICT    329    329       F -> L (in Ref. 1; BAE35261 and 2;
FT                                AAH24084).
SQ   SEQUENCE   656 AA;  72538 MW;  B8CCF6BBACD0A92A CRC64;
     MTGGSSSRRR RAEERSSAAG TERNSRREAV GGMGAGPALA ALLLAGSVLS ATLLAPGRRA
     EPDLDEKRNV ELKMDQALLL IHNELLGTSL TVYWKSDDCY QCTFQPLANV SHGGKPAKPS
     VAPVSVSTQH GSILQVNSTS EERAACRLEY KFGEFGNYSL LVQHASSGAN KIACDIIVNE
     NPVDSNLPVS IAFLVGLALI VAVSLLRLLL SLDDVNNWIS KTIASRETDR LINSELGSPS
     RADPLSADYQ PETRRSSANR LRCVDTFRGL ALVLMVFVNY GGGKYWYFKH SSWNGLTVAD
     LVFPWFVFIM GTSIFLSMTS ILQRGCSKFK LLGKIVWRSF LLICIGVIIV NPNYCLGPLS
     WDKVRIPGVL QRLGVTYFVV AVLEFFFWKP VPDSCTLESS CFSLRDITSS WPQWLTILTL
     ESIWLALTFF LPVPGCPTGY LGPGGIGDLG KYPHCTGGAA GYIDRLLLGD NHLYQHPSST
     VLYHTEVAYD PEGVLGTINS IVMAFLGVQA GKILVYYKDQ TKAILTRFAA WCCILGLISI
     VLTKVSANEG FIPINKNLWS ISYVTTLSCF AFFILLILYP VVDVKGLWTG TPFFYPGMNS
     ILVYVGHEVL ENYFPFQWKL ADEQSHKEHL IQNIVATALW VLIAYVLYKK KLFWKI
//
ID   Q3UDY9_MOUSE            Unreviewed;       492 AA.
AC   Q3UDY9;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 35.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Snx1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK149850; BAE29122.1; -; mRNA.
DR   IPI; IPI00876001; -.
DR   UniGene; Mm.271891; -.
DR   STRING; Q3UDY9; -.
DR   Ensembl; ENSMUST00000034946; ENSMUSP00000034946; ENSMUSG00000032382.
DR   MGI; MGI:1928395; Snx1.
DR   HOVERGEN; HBG000618; -.
DR   InParanoid; Q3UDY9; -.
DR   ArrayExpress; Q3UDY9; -.
DR   Bgee; Q3UDY9; -.
DR   Genevestigator; Q3UDY9; -.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   InterPro; IPR001683; Phox.
DR   InterPro; IPR005329; Sorting_nexin_N.
DR   InterPro; IPR015404; Vps5_C.
DR   Gene3D; G3DSA:3.30.1520.10; PX; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF03700; Sorting_nexin; 1.
DR   Pfam; PF09325; Vps5; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; PX; 1.
DR   PROSITE; PS50195; PX; 1.
PE   2: Evidence at transcript level;
FT   NON_TER     492    492
SQ   SEQUENCE   492 AA;  55487 MW;  99F248FC993A86EA CRC64;
     MASGGGGCSA SERLPPPFPG MDPESEGAAG GSEPEAGDSD TEGEDIFTGA AAATKPQSPK
     KTTSLFPIKN GSKENGIHED QDQEPQDLFA DATVELSLDS TQNNQKTMPG KTLTSHPPQE
     ATNSPKPQPS YEELEEEQED QFDLTVGITD PEKIGDGMNA YVAYKVTTQT SLPMFRSRQF
     AVKRRFSDFL GLYEKLSEKH SQNGFIVPPP PEKSLIGMTK VKVGKEDSSS AEFLEKRRAA
     LERYLQRIVN HPTMLQDPDV REFLEKEELP RAVGTQALSG AGLLKMFNKA TDAVSKMTIK
     MNESDIWFEE KLQEVECEEQ RLRKLHAVVE TLVNHRKELA LNTALFAKSL AMLGSSEDNT
     ALSRALSQLA EVEEKIEQLH QEQANNDFFL LVELLSDYIR LLAIVRAAFD QRMKTWQRWQ
     DAQATLQKKR ESEARLLWAN KPDKLQQAKD EITEWESRVT QYERDFERIS TVVRKEVTRF
     EKEKSKDFKN HV
//
ID   Q3UEA1_MOUSE            Unreviewed;      1034 AA.
AC   Q3UEA1;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 40.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Acly;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK149660; BAE29010.1; -; mRNA.
DR   IPI; IPI00126248; -.
DR   UniGene; Mm.282039; -.
DR   ProteinModelPortal; Q3UEA1; -.
DR   STRING; Q3UEA1; -.
DR   Ensembl; ENSMUST00000100457; ENSMUSP00000098025; ENSMUSG00000020917.
DR   Ensembl; ENSMUST00000107389; ENSMUSP00000103012; ENSMUSG00000020917.
DR   MGI; MGI:103251; Acly.
DR   HOVERGEN; HBG003318; -.
DR   InParanoid; Q3UEA1; -.
DR   ArrayExpress; Q3UEA1; -.
DR   Bgee; Q3UEA1; -.
DR   Genevestigator; Q3UEA1; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003878; F:ATP citrate synthase activity; TAS:MGI.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR   GO; GO:0006085; P:acetyl-CoA biosynthetic process; TAS:MGI.
DR   GO; GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR   InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR   InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
DR   InterPro; IPR002020; Citrate_synthase-like.
DR   InterPro; IPR016141; Citrate_synthase-like_core.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR005810; CoA_lig_alpha.
DR   InterPro; IPR005811; CoA_ligase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1.
DR   Gene3D; G3DSA:1.10.580.10; Citrate_synthase_lrg_a-sub; 1.
DR   Gene3D; G3DSA:1.10.230.10; Citrate_synthase_sm_a-sub; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:3.40.50.261; Succinyl-CoA_synth-like; 2.
DR   Pfam; PF08442; ATP-grasp_2; 1.
DR   Pfam; PF00285; Citrate_synt; 1.
DR   Pfam; PF02629; CoA_binding; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   SUPFAM; SSF48256; Citrate_synthase_core; 1.
DR   SUPFAM; SSF52210; CoA_ligase; 1.
DR   PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR   PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
PE   2: Evidence at transcript level;
FT   NON_TER    1034   1034
SQ   SEQUENCE   1034 AA;  113047 MW;  8EA986CD43ECF315 CRC64;
     MSAKAISEQT GKELLYKYIC TTSAIQNRFK YARVTPDTDW AHLLQDHPWL LSQSLVVKPD
     QLIKRRGKLG LVGVNLSLDG VKSWLKPRLG HEATVGKAKG FLKNFLIEPF VPHSQAEEFY
     VCIYATREGD YVLFHHEGGV DVGDVDAKAQ KLLVGVDEKL NTEDIKRHLL VHAPEDKKEV
     LASFISGLFN FYEDLYFTYL EINPLVVTKD GVYILDLAAK VDATADYICK VKWGDIEFPP
     PFGREAYPEE AYIADLDAKS GASLKLTLLN PKVRIWTMVA GGGASVVYSD TICDLGGVNE
     LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHPEGKILII GGSIANFTNV AATFKGIVRA
     IRDYQGPLKE HEVTIFVRRG GPNYQEGLRV MGEVGKTTGI PIHVFGTETH MTAIVGMALG
     HRPIPNQPPT AAHTANFLLN ASGSTSTPAP SRTASFSESR ADEVAPAKKA KPAMPQDSVP
     SPRSLQGKSA TLFSRHTKAI VWGMQTRAVQ GMLDFDYVCS RDEPSVAAMV YPFTGDHKQK
     FYWGHKEILI PVFKNMADAM KKHPEVDVLI NFASLRSAYD STMETMNYAQ IRTIAIIAEG
     IPEALTRKLI KKADQKGVTI IGPATVGGIK PGCFKIGNTG GMLDNILASK LYRPGSVAYV
     SRSGGMSNEL NNIISRTTDG VYEGVAIGGD RYPGSTFMDH VLRYQDTPGV KMIVVLGEIG
     GTEEYKICRG IKEGRLTKPV VCWCIGTCAT MFSSEVQFGH AGACANQASE TAVAKNQALK
     EAGVFVPRSF DELGEIIQSV YEDLVAKGAI VPAQEVPPPT VPMDYSWARE LGLIRKPASF
     MTSICDERGQ ELIYAGMPIT EVFKEEMGIG GVLGLLWFQR RLPKYSCQFI EMCLMVTADH
     GPAVSGAHNT IICARAGKDL VSSLSSGLLT IGDRFGGALD AAAKMFSKAF DSGIIPMEFV
     NKMKKEGKLI MGIGHRVKSI NNPDMRVQIL KDFVKQHFPA TPLLDYALEV EKITTSKKPN
     LILNVDGFIG VAFV
//
ID   Q3UEI5_MOUSE            Unreviewed;       823 AA.
AC   Q3UEI5;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-FEB-2011, entry version 33.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Akap13;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK149507; BAE28926.1; -; mRNA.
DR   IPI; IPI00896072; -.
DR   UniGene; Mm.216107; -.
DR   ProteinModelPortal; Q3UEI5; -.
DR   STRING; Q3UEI5; -.
DR   PRIDE; Q3UEI5; -.
DR   Ensembl; ENSMUST00000125771; ENSMUSP00000118138; ENSMUSG00000066406.
DR   UCSC; uc009hwq.1; mouse.
DR   MGI; MGI:2676556; Akap13.
DR   GeneTree; ENSGT00600000084265; -.
DR   ArrayExpress; Q3UEI5; -.
DR   Bgee; Q3UEI5; -.
DR   Genevestigator; Q3UEI5; -.
DR   InterPro; IPR018459; RII_binding_1.
DR   Pfam; PF10522; RII_binding_1; 1.
PE   2: Evidence at transcript level;
FT   NON_TER     823    823
SQ   SEQUENCE   823 AA;  87855 MW;  14F6B8CF5B3DDC91 CRC64;
     MGNTSPVGIG GEQEGSSPTA TLEVLSDSLL HNVDKAALVS DFTLPEEGVS VVVPESSTAL
     GQDGKDRAMS CSSVKEDVHS SEMSREDQRT PPSGQEIPGL CEKPMSALCA EEKAQQHTPS
     ACLKTETKDI KEVAPQVSLL TEGGAAKSLV PPRTSLSADS KQKASSTEQS GSSLLPSGLP
     GASEALHCNQ PSALDVVVEN TQFQGETNAC EVSRSAMEDV TVADASPATA EPRKKDASHC
     IKDIPISELL NQEKQMTPSL PEAFLDKGVT DLQEVITPEI EPLDCKRETL EGTDLNCATS
     NSKETPIEKP MQPLARDLPT ETGLSVINNN VPQADMKQVA QASIPAEESN ATTVSTQAAD
     VPTRADSIEE TATRIVEAVI RQVRASNALM AKVETQNPSL SSPETKQLEN AYTESACAFL
     PGETPQIEKT HEDTTGQCGA ETEEPEKIIL PESAPEMPDT RTGDEVDLLS RISAASEEEA
     VGNGAATPKM KQGPGTQAIN RESWCAIEPC PEAASLLASK QSSECRSFID VGLGTECASK
     EGMLQRVSGS ESDLFHSPSD EMDSIIFPKP EEEQLLCDTT GSSSSTDDTA SLDRHSSHGS
     DVSLPQTSKL NRSRNHQSAN GFFSPGVEAP ESRESESEPA GSGEMEEEEM DSITEVPANC
     SFLRSSMRSL SPFRRHSWGP GKNAASDAEM NQRSFSLEGL TGGGVGNKPS SSLEMSSANS
     SELRNPFGGE EQRNSLMSLS EEHLEPDQRQ HHRMFDQQTC YRSKQQGFNY CTSAISSPLT
     KSISLMTISH PGLDSSRPFH STSANLTESI TEENCNFLPP SPS
//
ID   Q3UEI6_MOUSE            Unreviewed;       386 AA.
AC   Q3UEI6;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   11-JAN-2011, entry version 36.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Serbp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK149505; BAE28925.1; -; mRNA.
DR   IPI; IPI00471477; -.
DR   RefSeq; NP_001107038.1; NM_001113566.1.
DR   UniGene; Mm.240490; -.
DR   UniGene; Mm.440861; -.
DR   STRING; Q3UEI6; -.
DR   PRIDE; Q3UEI6; -.
DR   Ensembl; ENSMUST00000042990; ENSMUSP00000039110; ENSMUSG00000036371.
DR   GeneID; 66870; -.
DR   KEGG; mmu:66870; -.
DR   CTD; 66870; -.
DR   MGI; MGI:1914120; Serbp1.
DR   HOVERGEN; HBG056357; -.
DR   InParanoid; Q3UEI6; -.
DR   NextBio; 322883; -.
DR   ArrayExpress; Q3UEI6; -.
DR   Bgee; Q3UEI6; -.
DR   Genevestigator; Q3UEI6; -.
DR   InterPro; IPR006861; HABP4_PAIRBP1-bd.
DR   Pfam; PF04774; HABP4_PAI-RBP1; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   386 AA;  42235 MW;  A22FB50BE68F72CB CRC64;
     MPGHLQEGFG CVVTNRFDQL FDDESDPFEV LKAAENKKKE AGGGGVGGPG AKSAAQAAAQ
     TNSNAAGKQL RKESQKDRKN PLPPSVGVAD KKEETQPPVA LKKEGIRRVG RRPDQQLQGD
     GKLIDRRAER RPPRERRFEK PLEEKGEGGE FSVDRPIIER PIRGRGGLGR GRGGRGRGMG
     RGDGFDSRGK REFDRHSGSD RSGLKHEDKR GGSGSHNWGT VKDELTDLDQ SNVTEETPEG
     EEHPVADTEN KENEVEEVKE EGPKEMTLDE WKAIQNKDRA KVEFNIRKPN EGADGQWKKG
     FVLHKSKSEE AHAEDSVMDH HFRKPANDIT SQLEINFGDL GRPGRGGRGG RGGRGRGGRP
     NRGSRTDKSS ASAPDVDDPE AFPALA
//
ID   Q3UF29_MOUSE            Unreviewed;       783 AA.
AC   Q3UF29;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 35.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Kcnn2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Sympathetic ganglion;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Sympathetic ganglion;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Sympathetic ganglion;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Sympathetic ganglion;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Sympathetic ganglion;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Sympathetic ganglion;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Sympathetic ganglion;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Sympathetic ganglion;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK149082; BAE28732.1; -; mRNA.
DR   IPI; IPI00467814; -.
DR   UniGene; Mm.458654; -.
DR   ProteinModelPortal; Q3UF29; -.
DR   SMR; Q3UF29; 517-729.
DR   STRING; Q3UF29; -.
DR   PhosphoSite; Q3UF29; -.
DR   Ensembl; ENSMUST00000066890; ENSMUSP00000067884; ENSMUSG00000054477.
DR   UCSC; uc008evd.1; mouse.
DR   MGI; MGI:2153182; Kcnn2.
DR   HOVERGEN; HBG052241; -.
DR   InParanoid; Q3UF29; -.
DR   ArrayExpress; Q3UF29; -.
DR   Bgee; Q3UF29; -.
DR   Genevestigator; Q3UF29; -.
DR   GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR   InterPro; IPR004178; CaM-bd_dom.
DR   InterPro; IPR013099; Ion_trans_2.
DR   InterPro; IPR015449; K_chnl_Ca-activ_SK.
DR   InterPro; IPR011996; K_chnl_Ca-activ_SK_con.
DR   InterPro; IPR003931; K_chnl_Ca-activ_SK_sub.
DR   PANTHER; PTHR10153; CaKChannelSK; 1.
DR   Pfam; PF02888; CaMBD; 1.
DR   Pfam; PF07885; Ion_trans_2; 1.
DR   Pfam; PF03530; SK_channel; 1.
DR   PRINTS; PR01451; SKCHANNEL.
DR   SUPFAM; SSF81327; CaM_bd; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   783 AA;  85636 MW;  21DAAAF63C4CB3DB CRC64;
     METPLQFQRG FFPEQPPPPP RSSHLHCQQQ QQSQDKPCAP FAPLPHPHHH PHLAHQQPGS
     GGSSPCLRCN SCASSGAPAA GAGAGDNLSL LLRTSSPGGA FRTRTSSPLS GSSCCCCCSS
     RRGSQLNVSE LTPSSHASAL RQQYAQQPAS ASQYHQCHSL QPATSPTGSL GSLGSGPPLS
     HHHHHPHPAH HQHHQPQARR ESNPFTEIAM SSCRYNGGVM RPLSNLSSSR RNLQEMDSEA
     QPLQPPASVV GGGGGASSPS AAAAASSSAP EIVVSKPEHN NSNNLALYGT GGGGSTGGGG
     GGSGHGSSSG TKSSKKKNQN IGYKLGHRRA LFEKRKRLSD YALIFGMFGI VVMVIETELS
     WGAYDKASLY SLALKCLISL STIILLGLII VYHAREIQLF MVDNGADDWR IAMTYERIFF
     ICLEILVCAI HPIPGNYTFT WTARLAFSYA PSTTTADVDI ILSIPMFLRL YLIARVMLLH
     SKLFTDASSR SIGALNKINF NTRFVMKTLM TICPGTVLLV FSISLWIIAA WTVRACERYH
     DQQDVTSNFL GAMWLISITF LSIGYGDMVP NTYCGKGVCL LTGIMGAGCT ALVVAVVARK
     LELTKAEKHV HNFMMDTQLT KRVKNAAANV LRETWLIYKN TKLVKKIDHA KVRKHQRKFL
     QAIHQLRSVK MEQRKLNDQA NTLVDLAKTQ NIMYDMISDL NERSEDFEKR IVTLETKLET
     LIGSIHALPG LISQTIRQQQ RDFIETQMEN YDKHVSYNAE RSRSSSRRRR SSSTAPPTSS
     ESS
//
ID   RNFT2_MOUSE             Reviewed;         445 AA.
AC   Q3UF64; Q8BXI9;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 2.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=RING finger and transmembrane domain-containing protein 2;
GN   Name=Rnft2; Synonyms=Tmem118;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata, and Sympathetic ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UF64-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UF64-2; Sequence=VSP_023467;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH57302.1; Type=Erroneous initiation;
CC       Sequence=BAC32896.1; Type=Erroneous initiation;
CC       Sequence=BAE28697.1; Type=Frameshift; Positions=421;
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DR   EMBL; AK046850; BAC32896.1; ALT_INIT; mRNA.
DR   EMBL; AK148930; BAE28697.1; ALT_FRAME; mRNA.
DR   EMBL; BC057302; AAH57302.1; ALT_INIT; mRNA.
DR   IPI; IPI00226695; -.
DR   IPI; IPI00652676; -.
DR   RefSeq; NP_001103372.1; NM_001109902.1.
DR   RefSeq; NP_766586.2; NM_172998.3.
DR   UniGene; Mm.320042; -.
DR   ProteinModelPortal; Q3UF64; -.
DR   SMR; Q3UF64; 381-426.
DR   PRIDE; Q3UF64; -.
DR   Ensembl; ENSMUST00000072529; ENSMUSP00000072343; ENSMUSG00000032850.
DR   Ensembl; ENSMUST00000121369; ENSMUSP00000113749; ENSMUSG00000032850.
DR   GeneID; 269695; -.
DR   KEGG; mmu:269695; -.
DR   CTD; 269695; -.
DR   MGI; MGI:2442859; Rnft2.
DR   HOVERGEN; HBG056546; -.
DR   OMA; VFCEECL; -.
DR   NextBio; 392981; -.
DR   ArrayExpress; Q3UF64; -.
DR   Bgee; Q3UF64; -.
DR   CleanEx; MM_RNFT2; -.
DR   Genevestigator; Q3UF64; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Membrane; Metal-binding; Transmembrane;
KW   Transmembrane helix; Zinc; Zinc-finger.
FT   CHAIN         1    445       RING finger and transmembrane domain-
FT                                containing protein 2.
FT                                /FTId=PRO_0000279509.
FT   TOPO_DOM      1    183       Extracellular (Potential).
FT   TRANSMEM    184    203       Helical; (Potential).
FT   TOPO_DOM    204    215       Cytoplasmic (Potential).
FT   TRANSMEM    216    236       Helical; (Potential).
FT   TOPO_DOM    237    256       Extracellular (Potential).
FT   TRANSMEM    257    277       Helical; (Potential).
FT   TOPO_DOM    278    330       Cytoplasmic (Potential).
FT   TRANSMEM    331    351       Helical; (Potential).
FT   TOPO_DOM    352    445       Extracellular (Potential).
FT   ZN_FING     385    423       RING-type.
FT   COMPBIAS    109    138       His-rich.
FT   VAR_SEQ      27     27       E -> ES (in isoform 2).
FT                                /FTId=VSP_023467.
FT   CONFLICT    147    147       P -> H (in Ref. 1; BAE28697).
SQ   SEQUENCE   445 AA;  48856 MW;  687984892639806F CRC64;
     MWLLAAHQVL RKMQRRHSSN TDNIPPERSR SQALSPEASV DEGGVFESLK AETASPPALF
     SGLAGGLPAS PFPAGLVLGS TAGGGDVFIP MPATRDEAGG RSAEGSTYHH RQAHHHFHHG
     AHRGGSLLQH VGGDHRGHSE EGVDEQPGTP APALSELKAV ISWLQKGLPF ILILLAKLCF
     QHKLGIAVCI GMASTFAYAN STLREQVSLK EKRSVLVILW ILAFLAGNTM YVLYTFSSQQ
     LYSSLIFLKP NLETLDFFDL LWIVGIADFV LKYITIALKC LIVALPKIIL AVKSKGKFYL
     VIEELSQLFR SLVPIQLWYK YIMGDDSSNS YFLGGVLIVL YSLCKSFDIC GRVGGLRKAL
     KLLCTSQNYG VRATGQQCTE AGAVCAICQA EFRDPMILLC QHVFCEECLC LWLDRERTCP
     LCRSVAVDTL RCWKDGATSA HLQVY
//
ID   Q3UFK1_MOUSE            Unreviewed;       184 AA.
AC   Q3UFK1;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Ccdc28a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK148447; BAE28559.1; -; mRNA.
DR   IPI; IPI00170039; -.
DR   RefSeq; NP_659069.2; NM_144820.3.
DR   UniGene; Mm.296565; -.
DR   PhosphoSite; Q3UFK1; -.
DR   PRIDE; Q3UFK1; -.
DR   Ensembl; ENSMUST00000080860; ENSMUSP00000079671; ENSMUSG00000059554.
DR   GeneID; 215814; -.
DR   KEGG; mmu:215814; -.
DR   UCSC; uc007eme.1; mouse.
DR   CTD; 215814; -.
DR   MGI; MGI:2443508; Ccdc28a.
DR   eggNOG; roNOG11665; -.
DR   GeneTree; ENSGT00500000044870; -.
DR   HOVERGEN; HBG061498; -.
DR   OMA; APIQHSF; -.
DR   OrthoDB; EOG4TXBSS; -.
DR   NextBio; 374857; -.
DR   ArrayExpress; Q3UFK1; -.
DR   Bgee; Q3UFK1; -.
DR   Genevestigator; Q3UFK1; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   184 AA;  20301 MW;  AB0A0B884327C83C CRC64;
     MEERKAKRKS PKSFSAHSTQ VVNAKKNAIP SSKSTGFSNP TSQSASQRPK LKRVMKEKNK
     PPGGEGKGAQ STPIQHSFLT DVSDVQEMER GLLSLLNDFH SGKLQAFGNE CSIEQMEHVR
     GMQEKLARLN LELYGELEEL PEDKRKAASD ANLDRLLSDL EELNSSIQKL HLADAQDVPN
     ASSS
//
ID   Q3UFQ5_MOUSE            Unreviewed;       287 AA.
AC   Q3UFQ5;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 33.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Ttc7b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
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CC   -----------------------------------------------------------------------
DR   EMBL; AK148363; BAE28505.1; -; mRNA.
DR   IPI; IPI00757517; -.
DR   UniGene; Mm.295441; -.
DR   ProteinModelPortal; Q3UFQ5; -.
DR   PhosphoSite; Q3UFQ5; -.
DR   Ensembl; ENSMUST00000062957; ENSMUSP00000052107; ENSMUSG00000033530.
DR   MGI; MGI:2144724; Ttc7b.
DR   eggNOG; roNOG05238; -.
DR   GeneTree; ENSGT00390000014400; -.
DR   HOGENOM; HBG444114; -.
DR   InParanoid; Q3UFQ5; -.
DR   OrthoDB; EOG4J3WGB; -.
DR   ArrayExpress; Q3UFQ5; -.
DR   Bgee; Q3UFQ5; -.
DR   Genevestigator; Q3UFQ5; -.
PE   1: Evidence at protein level;
SQ   SEQUENCE   287 AA;  32689 MW;  FB9F4C96D780D10E CRC64;
     MATRKAGSRL ETEIERCRSE CQWERIPELV KQLSAKLIAN DDMAELLLGE SKLEQHLKEK
     PLRQGASPRG PRPQLTEVRK HLTAALDRGN LKSEFLQESN LVMAKLTYVE GDYKEALNIY
     ARVGLDDLPL TAVPPYRLRM IAEAYATKGL CLEKLPVSSS TSNLHVDREQ DVITCYEKAG
     DIALLYLQEI ERVMLTNIQN RSPKPGPAPH DQELGFFLET GLQRAHVLYF KNGNLTRGVG
     RFRELLRAVE TRTTQNLRMT IARQLAEILL RGMCEQSYWS PLEEPPY
//
ID   LR16B_MOUSE             Reviewed;        1375 AA.
AC   Q3UFQ8; Q6KAP3;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=Leucine-rich repeat-containing protein 16B;
GN   Name=Lrrc16b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of FLJ genes:
RT   the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:127-135(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-898.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SIMILARITY: Belongs to the CARMIL family.
CC   -!- SIMILARITY: Contains 9 LRR (leucine-rich) repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD21414.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA;
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DR   EMBL; AK131164; BAD21414.1; ALT_SEQ; Transcribed_RNA.
DR   EMBL; AK148355; BAE28502.1; -; mRNA.
DR   IPI; IPI00553452; -.
DR   RefSeq; NP_001019816.1; NM_001024645.1.
DR   UniGene; Mm.151577; -.
DR   ProteinModelPortal; Q3UFQ8; -.
DR   SMR; Q3UFQ8; 188-667.
DR   PhosphoSite; Q3UFQ8; -.
DR   PRIDE; Q3UFQ8; -.
DR   Ensembl; ENSMUST00000076236; ENSMUSP00000075587; ENSMUSG00000022211.
DR   GeneID; 268747; -.
DR   KEGG; mmu:268747; -.
DR   CTD; 268747; -.
DR   MGI; MGI:2448573; Lrrc16b.
DR   eggNOG; roNOG14914; -.
DR   GeneTree; ENSGT00390000014487; -.
DR   HOGENOM; HBG715980; -.
DR   HOVERGEN; HBG108094; -.
DR   InParanoid; Q3UFQ8; -.
DR   OMA; NADTPEG; -.
DR   OrthoDB; EOG476JZK; -.
DR   NextBio; 392469; -.
DR   ArrayExpress; Q3UFQ8; -.
DR   Bgee; Q3UFQ8; -.
DR   CleanEx; MM_LRRC16B; -.
DR   Genevestigator; Q3UFQ8; -.
PE   2: Evidence at transcript level;
KW   Leucine-rich repeat; Repeat.
FT   CHAIN         1   1375       Leucine-rich repeat-containing protein
FT                                16B.
FT                                /FTId=PRO_0000324609.
FT   REPEAT      242    269       LRR 1.
FT   REPEAT      272    299       LRR 2.
FT   REPEAT      333    358       LRR 3.
FT   REPEAT      390    417       LRR 4.
FT   REPEAT      422    446       LRR 5.
FT   REPEAT      453    475       LRR 6.
FT   REPEAT      480    507       LRR 7.
FT   REPEAT      510    536       LRR 8.
FT   REPEAT      568    591       LRR 9.
FT   COMPBIAS    978   1097       Pro-rich.
FT   COMPBIAS   1204   1208       Poly-Pro.
SQ   SEQUENCE   1375 AA;  150416 MW;  A6963D11222F14C2 CRC64;
     MAKASVELTR ELQDSIRRCL SQGAVLQQHR VKLETKPKKF EDRVLALTSW RLHLFPLKVP
     AKVESSFNVL EIRAFNTLSQ NQILVETERG TVSMRLPSAE SVDQVTRHVS SALSKVCPGP
     GCLIRRGNAD TPEGPRDTSP NSETSTSTTH SVCGGFSETY AALCDYNGLH CREEVQWDVD
     TIYHAEDNRE FNLLDFSHLE SRDLALMVAA LAYNQWFTKL YCKDLRLGSE VLEQVLHTLS
     KSGSLEELVL DNAGLKTDFV QKLAGVFGEN GSCVLHALIL SHNPIEDKGF LSLSQQLLCF
     PTGLTKLCLA KTAISPRGLQ ALGQTFGANP AFASSLRYLD LSKNPGLLAT DEANALYSFL
     AQPNALVHLD LSGTDCAVDM LLGALLHGCC SHLTYLNLAR NSCSHRKGRE APPAFKQFFS
     SVYTLSHVNL SATRLPLEAL RALLQGLSLN SHLSDLHLDL SSCELRSAGA QALQEQLGAV
     TCIGSLDLSD NGFDSDLLTL VPALGKNKSL KHLFLGKNFN VKAKTLEEIL HKLVQLIQEE
     DCSLQSLSVA DSRLKLRTSI LINALGSNTC LAKVDLSGNG MEDIGAKMLS KALQINSSLR
     TILWDRNNTS ALGFLDIARA LESNHTLRFM SFPVSDISQA YRSAPERTED VWQKIQWCLV
     RNNHSQTCPQ EQAFRLQQGL VTSSAEQMLQ RLCGRVQEEV RALRLCPLEP VQDELLYARD
     LIKDAKNSRA LFPSLYELGH VLANDGPVRQ RLESVASEVS KAVDKELQVI LESMVSLTQE
     LCPVAMRVAE GHNKMLSNVA ERVTVPRNFI RGALLEQAGQ DIQNKLDEVK LSVVTYLTNS
     IVDEILQELY HSHKSLARHL TQLRTLSDPP GGASQGQDPS SRGRGRNHDH EETDDELGTN
     IDTMAIKKQK RCRKIRPVSA FISGSPQDME SQLGSLGIPP GWFSGLGASQ TTASGSWEGL
     SELPTHGYKL RHQTQGRPRP PRTTPPGPGR PSVPVPGPRQ ENGMATRLDE GLEDFFSRRV
     MDESSSYPRT LRTMRPGLSE PPLPPLQKKR RRGLFHFRRP RSFKGDRGPG SPTAGLLLPP
     PPPPPPTQES PPSPDPPSLG NNSSPCWSPE EESSLLPGFG GARGSSFCRK MGTERLEAGE
     GAPAPGTAQQ PRVHGGVALP GLGRTKGWSF DGKREGTDPD QEDSTQAWQK RRSSDDAGPG
     AWKPPPPPQS SKPSFSAMRR AEATWHIAEE SAANHSCQSP SPASQDGDEE KQGALFPERM
     VPTRNAKLQE PPIGPRPPKP VAVPRGRRAP QVPGGREETE SSSAAPGANK PRLRLGSQQD
     QEEPEGQGPT DQGRRTAPLK PKRTRRAQSC DKLEPDRRQP PDPTGVCGTS EPGTD
//
ID   FA59A_MOUSE             Reviewed;         876 AA.
AC   Q3UFT3; Q3TSA2; Q5DTF6; Q80V96;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Protein FAM59A;
GN   Name=Fam59a; Synonyms=Gm944, Kiaa4238;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 219-876 (ISOFORM 1).
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-496, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UFT3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UFT3-2; Sequence=VSP_023049, VSP_023050;
CC   -!- SIMILARITY: Belongs to the FAM59 family.
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90542.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK148318; BAE28477.1; -; mRNA.
DR   EMBL; AK162177; BAE36773.1; -; mRNA.
DR   EMBL; AK220564; BAD90542.1; ALT_INIT; mRNA.
DR   EMBL; BC049983; AAH49983.1; -; mRNA.
DR   IPI; IPI00113348; -.
DR   IPI; IPI00828249; -.
DR   RefSeq; NP_001028617.2; NM_001033445.2.
DR   UniGene; Mm.312276; -.
DR   ProteinModelPortal; Q3UFT3; -.
DR   SMR; Q3UFT3; 795-874.
DR   PhosphoSite; Q3UFT3; -.
DR   PRIDE; Q3UFT3; -.
DR   Ensembl; ENSMUST00000049260; ENSMUSP00000048914; ENSMUSG00000042680.
DR   GeneID; 381126; -.
DR   KEGG; mmu:381126; -.
DR   UCSC; uc008efg.1; mouse.
DR   CTD; 381126; -.
DR   MGI; MGI:2685790; Fam59a.
DR   eggNOG; roNOG12150; -.
DR   GeneTree; ENSGT00530000063834; -.
DR   HOGENOM; HBG445185; -.
DR   HOVERGEN; HBG060860; -.
DR   InParanoid; Q3UFT3; -.
DR   OrthoDB; EOG4J3WG9; -.
DR   NextBio; 401638; -.
DR   ArrayExpress; Q3UFT3; -.
DR   Bgee; Q3UFT3; -.
DR   CleanEx; MM_GM944; -.
DR   Genevestigator; Q3UFT3; -.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    876       Protein FAM59A.
FT                                /FTId=PRO_0000277648.
FT   DOMAIN      811    876       SAM.
FT   REGION       12    320       CABIT.
FT   COMPBIAS    491    566       Pro-rich.
FT   MOD_RES      74     74       Phosphotyrosine (By similarity).
FT   MOD_RES     453    453       Phosphotyrosine (By similarity).
FT   MOD_RES     496    496       Phosphothreonine.
FT   MOD_RES     701    701       Phosphotyrosine (By similarity).
FT   VAR_SEQ     578    578       I -> M (in isoform 2).
FT                                /FTId=VSP_023049.
FT   VAR_SEQ     579    876       Missing (in isoform 2).
FT                                /FTId=VSP_023050.
FT   CONFLICT    324    324       N -> H (in Ref. 2; BAD90542 and 3;
FT                                AAH49983).
FT   CONFLICT    652    652       H -> P (in Ref. 1; BAE36773 and 3;
FT                                AAH49983).
FT   CONFLICT    760    760       L -> Q (in Ref. 1; BAE36773).
SQ   SEQUENCE   876 AA;  97267 MW;  D39D24D9AD2DC81B CRC64;
     MDPAPSLGCS LKDVKWSPVA MPLDLLVSTY RLPQIARLDS GECVEGLREN DFLLIHSCRQ
     WTTITAHSLE EGHYVIGPKI EIPVHYAGQF KLLEQDRDIK EPVQYFNSVE EVAKAFPERV
     YVMEEITFNV KVASGECNED TEVYNITLCT GDELTLMGQA EILYAKTFKE KSRLNTIFKK
     IGKLNSISKL GKGKMPCLIC MNHRTNESIS LPFQCKGRFS TRSPLELQMQ EGEHTIRNIV
     EKTRLPVNVT VPSPPPRNPY DLHFIREGHR YKFVNIQTKT VVVCCVLRNN KILPMHFPLH
     LTVPKFSLPE HQVKGDMWPE TLVNHWLGIC QEQFDIDEYS RAVRDVKTDW NEDCKSPKKG
     RCSGHNHLPN SLSYARDELT QSFHRLSVCV YGNNLHGNSE VNLHGCRDLG GEWAPFPHDI
     LPYQDSGDSG SDYLFPEANE ESAGIPGKTE VPYEELWLEE GKPSRQPLTR SLSEKSRCDT
     LRGSTRSTCA PSSPPTPATL GATIKSSEIA LPPPPVPPKS EAVREECRLL NAPPVPPRSA
     KPLSTSPSIP PRTVKPVRPQ TRSPSPTLSY YSSGLHNIIT QSDTSPPNSA PVSCYPCTRV
     KSDSVDPKSP FGSPSAEALS SRLSWPNHYS GASENQTRSD FLLDPSRSYS YHRQKTPGTP
     KRTCPAPFDF EGCELLGSPP STTSAEFSSS GVPSCPKSAS YCLENSEDNS FAAGMTKQSV
     SCPALPPRAP KPVEQKATPE TSPLPLKIDG AEEDPTAGSL DLSEDQYFVR KGMQDIFSVS
     YPFSSPLHLQ LAPRSCGDGS PWQPPADLSG LSIEEVSKSL RFIGLSEDVI AFFVTEKIDG
     NLLVQLTEEI LSEDFKLSKL QVKKILQFIN GWRPKI
//
ID   Q3UFT4_MOUSE            Unreviewed;      1057 AA.
AC   Q3UFT4;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Ulk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK148317; BAE28476.1; -; mRNA.
DR   IPI; IPI00467843; -.
DR   UniGene; Mm.271898; -.
DR   ProteinModelPortal; Q3UFT4; -.
DR   SMR; Q3UFT4; 11-283.
DR   STRING; Q3UFT4; -.
DR   PRIDE; Q3UFT4; -.
DR   Ensembl; ENSMUST00000112410; ENSMUSP00000108029; ENSMUSG00000029512.
DR   MGI; MGI:1270126; Ulk1.
DR   HOGENOM; HBG446996; -.
DR   HOVERGEN; HBG000342; -.
DR   InParanoid; Q3UFT4; -.
DR   PhylomeDB; Q3UFT4; -.
DR   ArrayExpress; Q3UFT4; -.
DR   Bgee; Q3UFT4; -.
DR   Genevestigator; Q3UFT4; -.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:MGI.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0048675; P:axon extension; IMP:MGI.
DR   GO; GO:0021707; P:cerebellar granule cell differentiation; IMP:MGI.
DR   GO; GO:0048671; P:negative regulation of collateral sprouting; IMP:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR   GO; GO:0021933; P:radial glia guided migration of cerebellar granule cell; IMP:MGI.
DR   GO; GO:0007265; P:Ras protein signal transduction; IDA:MGI.
DR   GO; GO:0031623; P:receptor internalization; IMP:MGI.
DR   GO; GO:0051386; P:regulation of nerve growth factor receptor signaling pathway; IMP:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR022708; Ser/Thr_kinase_C.
DR   InterPro; IPR016237; Ser/Thr_prot_kin_STPK_Ulk-1/2.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF12063; DUF3543; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF000580; Ser/Thr_PK_STPK_ULK-1/2; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding.
SQ   SEQUENCE   1057 AA;  113097 MW;  BFED19CFE8BF0BFB CRC64;
     MEPGRGGVET VGKFEFSRKD LIGHGAFAVV FKGRHREKHD LEVAVKCINK KNLAKSQTLL
     GKEIKILKEL KHENIVALYD FQEMANSVYL VMEYCNGGDL ADYLHTMRTL SEDTVRLFLQ
     QIAGAMRLLH SKGIIHRDLK PQNILLSNPG GRRANPSNIR VKIADFGFAR YLQSNMMAAT
     LCGSPMYMAP EVIMSQHYDG KADLWSIGTI VYQCLTGKAP FQASSPQDLR LFYEKNKTLV
     PAIPRETSAP LRQLLLALLQ RNHKDRMDFD EFFHHPFLDA STPIKKSPPV PVPSYPSSGS
     GSSSSSSSAS NLASPPSLGE MPQLQKTLTS PADAAGFLQG SRDSGGSSKD SCDTDDFVMV
     PAQFPGDLVA EAVSAKPPPD SLLCSGSSLV ASAGLESHGR TPSPSPTCSS SPSPSGRPGP
     FSSNRYGASV PIPVPTQVHN YQRIEQNLQS PTQQQTARSS AIRRSGSTSP LGFGRASPSP
     PSHTDGAMLA RKLSLGGGRP YTPSPQATLF LPVGTIPERP SWSRVPSPQG ADVRVGRSPR
     PGSSVPEHSP RTTGLGCRLH SAPNLSDFHV VRPKLPKPPT DPLGATFSPP QTSAPQPCPG
     LQSCRPLRGS PKLPDFLQRS PLPPILGSPT KAGPSFDFPK TPSSQNLLTL LARQGVVMTP
     PRNRTLPDLS EASPFHGQQL GSGLRPAEDT RGPFGRSFST SRITDLLLKA AFGTQASDSG
     STDSLQEKPM EIAPSAGFGG TLHPGARGGG ASSPAPVVFT VGSPPSGATP PQSTRTRMFS
     VGSSSSLGST GSSSARHLVP GACGEAPELS APGHCCSLAD PLAANLEGAV TFEAPDLPEE
     TLMEQEHTET LHSLRFTLAF AQQVLEIAAL KGSASEAAGG PEYQLQESVV ADQISQLSRE
     WGFAEQLVLY LKVAELLSSG LQTAIDQIRA GKLCLSSTVK QVVRRLNELY KASVVSCQGL
     SLRLQRFFLD KQRLLDGIHG VTAERLILSH AVQMVQSAAL DEMFQHREGC VPRYHKALLL
     LEGLQHTLTD QADIENIAKC KLCIERRLSA LLSGVYA
//
ID   Q3UGC7_MOUSE            Unreviewed;       261 AA.
AC   Q3UGC7;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 47.
DE   SubName: Full=Eukaryotic translation initiation factor 3, subunit J;
DE   SubName: Full=MCG11598;
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Eif3j; Synonyms=Eif3s1; ORFNames=RP23-34E24.2-001, mCG_11598;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Liver, and Amnion;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Liver, and Amnion;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Liver, and Amnion;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Liver, and Amnion;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Liver, and Amnion;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Liver, and Amnion;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Liver, and Amnion;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Amnion;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RA   Martin S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [11]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK147154; BAE27721.1; -; mRNA.
DR   EMBL; AK148004; BAE28282.1; -; mRNA.
DR   EMBL; AK154934; BAE32935.1; -; mRNA.
DR   EMBL; AK161038; BAE36162.1; -; mRNA.
DR   EMBL; AL845457; CAM21780.1; -; Genomic_DNA.
DR   EMBL; CH466519; EDL28081.1; -; Genomic_DNA.
DR   IPI; IPI00556700; -.
DR   RefSeq; NP_653128.2; NM_144545.3.
DR   UniGene; Mm.458184; -.
DR   ProteinModelPortal; Q3UGC7; -.
DR   SMR; Q3UGC7; 145-214.
DR   STRING; Q3UGC7; -.
DR   PRIDE; Q3UGC7; -.
DR   Ensembl; ENSMUST00000028668; ENSMUSP00000028668; ENSMUSG00000027236.
DR   GeneID; 78655; -.
DR   KEGG; mmu:78655; -.
DR   UCSC; uc008mab.1; mouse.
DR   CTD; 78655; -.
DR   HOGENOM; HBG282796; -.
DR   HOVERGEN; HBG066230; -.
DR   InParanoid; Q3UGC7; -.
DR   OMA; DSWDADA; -.
DR   NextBio; 349286; -.
DR   ArrayExpress; Q3UGC7; -.
DR   Bgee; Q3UGC7; -.
DR   Genevestigator; Q3UGC7; -.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR023194; eIF3-like_dom.
DR   InterPro; IPR013906; eIF3_subunit.
DR   PANTHER; PTHR21681; eIF3_subunit; 1.
DR   Pfam; PF08597; eIF3_subunit; 1.
PE   2: Evidence at transcript level;
KW   Initiation factor; Protein biosynthesis.
SQ   SEQUENCE   261 AA;  29344 MW;  5BED22967289E651 CRC64;
     MAAAAAAAAA AGDSDSWDAD TFSMEDPVRK VAGGGTAGGD RWEGEDEDED VKDNWDDDDD
     ENKEEAEVKP EVKISEKKKI AEKIKEKERQ QKKRQEEIKK RLEEPEESKV LTPEEQLADK
     LRLKKLQEES DLELAKETFG VNNTVYGIDA MNPSSRDDFT EFGKLLKDKI TQYEKSLYYA
     SFLEALVRDV CISLEIDDLK KITNSLTVLC SEKQKQEKQS KAKKKKKGVV PGGGLKATMK
     DDLADYGGYE GGYVQDYEDF M
//
ID   Q3UGP0_MOUSE            Unreviewed;       363 AA.
AC   Q3UGP0;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Dclk1; Synonyms=Dcamkl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK147831; BAE28167.1; -; mRNA.
DR   IPI; IPI00856810; -.
DR   RefSeq; NP_001104523.1; NM_001111053.1.
DR   RefSeq; NP_001182467.1; NM_001195538.1.
DR   RefSeq; NP_064362.1; NM_019978.3.
DR   UniGene; Mm.393242; -.
DR   UniGene; Mm.472264; -.
DR   ProteinModelPortal; Q3UGP0; -.
DR   SMR; Q3UGP0; 49-154, 180-284.
DR   STRING; Q3UGP0; -.
DR   Ensembl; ENSMUST00000054237; ENSMUSP00000050034; ENSMUSG00000027797.
DR   Ensembl; ENSMUST00000089805; ENSMUSP00000087238; ENSMUSG00000027797.
DR   GeneID; 13175; -.
DR   KEGG; mmu:13175; -.
DR   CTD; 13175; -.
DR   MGI; MGI:1330861; Dclk1.
DR   HOVERGEN; HBG003790; -.
DR   InParanoid; Q3UGP0; -.
DR   NextBio; 283276; -.
DR   ArrayExpress; Q3UGP0; -.
DR   Bgee; Q3UGP0; -.
DR   Genevestigator; Q3UGP0; -.
DR   GO; GO:0048675; P:axon extension; IGI:MGI.
DR   GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IGI:MGI.
DR   GO; GO:0048813; P:dendrite morphogenesis; IGI:MGI.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IGI:MGI.
DR   InterPro; IPR017302; Doublecortin_chordata.
DR   InterPro; IPR003533; Doublecortin_dom.
DR   Gene3D; G3DSA:3.10.20.230; Doublecortin_dom; 2.
DR   Pfam; PF03607; DCX; 2.
DR   PIRSF; PIRSF037870; Doublin; 1.
DR   SMART; SM00537; DCX; 2.
DR   SUPFAM; SSF89837; Doublecortin_dom; 2.
DR   PROSITE; PS50309; DC; 2.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   363 AA;  40351 MW;  512642FBB66B2F5C CRC64;
     MSFGRDMELE HFDERDKAQR YSRGSRVNGL PSPTHSAHCS FYRTRTLQTL SSEKKAKKVR
     FYRNGDRYFK GIVYAISPDR FRSFEALLAD LTRTLSDNVN LPQGVRTIYT IDGLKKISSL
     DQLVEGESYV CGSIEPFKKL EYAKNVNPNW SVNVKTTSAS RAVSSLATAK GGPSEVRENK
     DFIRPKLVTI IRSGVKPRKA VRILLNKKTA HSFEQVLTDI TDAIKLDSGV VKRLYTLDGK
     QVMCLQDFFG DDDIFIACGP EKFRYQDDFL LDESECRVVK STSYTKIASA SRRGTTKSPG
     PSRRSKSPAS TSSVNGTPGS QLSTPRSGKS PSPSPTSPGS LRKQRDLYRP LSSDDLDSVG
     DSV
//
ID   F195B_MOUSE             Reviewed;          97 AA.
AC   Q3UGS4; Q8QZS4;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=Protein FAM195B;
GN   Name=Fam195b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-41, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SIMILARITY: Belongs to the FAM195 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH25536.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; AK147780; BAE28133.1; -; mRNA.
DR   EMBL; AL669855; CAM27054.1; -; Genomic_DNA.
DR   EMBL; CH466558; EDL34763.1; -; Genomic_DNA.
DR   EMBL; BC025536; AAH25536.1; ALT_INIT; mRNA.
DR   IPI; IPI00114944; -.
DR   RefSeq; NP_001028403.1; NM_001033231.2.
DR   UniGene; Mm.262300; -.
DR   PRIDE; Q3UGS4; -.
DR   Ensembl; ENSMUST00000034913; ENSMUSP00000034913; ENSMUSG00000061111.
DR   Ensembl; ENSMUST00000075027; ENSMUSP00000074544; ENSMUSG00000061111.
DR   GeneID; 192173; -.
DR   KEGG; mmu:192173; -.
DR   NMPDR; fig|10090.3.peg.25799; -.
DR   UCSC; uc007mtf.1; mouse.
DR   CTD; 192173; -.
DR   MGI; MGI:2384752; Fam195b.
DR   eggNOG; maNOG20955; -.
DR   GeneTree; ENSGT00530000064168; -.
DR   HOVERGEN; HBG059777; -.
DR   InParanoid; Q3UGS4; -.
DR   OMA; VRFIYEA; -.
DR   OrthoDB; EOG4FN4K7; -.
DR   NextBio; 371180; -.
DR   ArrayExpress; Q3UGS4; -.
DR   Bgee; Q3UGS4; -.
DR   Genevestigator; Q3UGS4; -.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1     97       Protein FAM195B.
FT                                /FTId=PRO_0000393955.
FT   MOD_RES      21     21       Phosphoserine.
FT   MOD_RES      41     41       Phosphotyrosine.
SQ   SEQUENCE   97 AA;  11101 MW;  50792192F1C63720 CRC64;
     MTSSPVSRVV YNGKRNSSPR SPTNSSEIFT PAHEENVRFI YEAWQGVERD LRSQLSSGER
     CLVEEYVEKV PNPSLKTFKP IDLSDLKRRN TQDAKKS
//
ID   Q3UGV7_MOUSE            Unreviewed;       489 AA.
AC   Q3UGV7;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-FEB-2011, entry version 41.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Ubxn7; Synonyms=AI196514, Ubxd7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK147730; BAE28100.1; -; mRNA.
DR   IPI; IPI00751399; -.
DR   UniGene; Mm.31275; -.
DR   ProteinModelPortal; Q3UGV7; -.
DR   SMR; Q3UGV7; 13-51, 130-265, 376-487.
DR   PRIDE; Q3UGV7; -.
DR   Ensembl; ENSMUST00000115151; ENSMUSP00000110804; ENSMUSG00000053774.
DR   UCSC; uc007yyr.1; mouse.
DR   MGI; MGI:2146388; Ubxn7.
DR   GeneTree; ENSGT00390000018687; -.
DR   HOGENOM; HBG714004; -.
DR   HOVERGEN; HBG057394; -.
DR   InParanoid; Q3UGV7; -.
DR   ArrayExpress; Q3UGV7; -.
DR   Bgee; Q3UGV7; -.
DR   Genevestigator; Q3UGV7; -.
DR   InterPro; IPR006577; UAS.
DR   InterPro; IPR009060; UBA-like.
DR   InterPro; IPR001012; UBX.
DR   InterPro; IPR017346; UCP037991_UAS_UBX.
DR   Pfam; PF00789; UBX; 1.
DR   PIRSF; PIRSF037991; UCP037991_UBX7/2; 1.
DR   SMART; SM00594; UAS; 1.
DR   SMART; SM00166; UBX; 1.
DR   SUPFAM; SSF46934; UBA_like; 1.
DR   PROSITE; PS50033; UBX; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   489 AA;  54842 MW;  EC73A406A9FDE49A CRC64;
     MAAHGGSAAS SALKGLIQQF TAITGTSESV GKHMLEACNN NLEMAVTMFL DGGGIAEEPS
     TSSASVSTVR PHTEEEVRAP IPQKQEILVE PEPLFGAPKR RRPARSIFDG FRDFQTETIR
     QEQELRNGGA IDKKLTTLAD LFRPPIDLMH KGSFETAKEC GQMQNKWLMI NIQNVQDFAC
     QCLNRDVWSN EAVKNIIREH FIFWQVYHDS EEGQRYIQFY KLGDFPYVSI LDPRTGQKLV
     EWHQLDVSSF LDQVTGFLGE HGQLDGLSSS PPKKCARSES LIDASEDSQL EAAIRASLQE
     THFDSAQAKQ DSRSDEESES ELFSGSEEFI SVCGSDEEEE VENLAKSRKS PHKDLGHRKE
     ENRRPLTEPP ARTEPGTATN HQGLPSMDSE VLEMSPEKSD GIVEGIDVNG PKAQLMLRYP
     DGKREQITLP EQAKLLALVK HVQSKGYPNE RFELLTNFPR RKLSHLDYDI TLQEAGLCPQ
     ETVFVQERN
//
ID   Q3UGX5_MOUSE            Unreviewed;      1921 AA.
AC   Q3UGX5;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Dlg5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SIMILARITY: Contains 4 PDZ (DHR) domains.
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CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; AK147699; BAE28082.1; -; mRNA.
DR   IPI; IPI00626101; -.
DR   RefSeq; NP_001156985.1; NM_001163513.1.
DR   RefSeq; NP_082002.1; NM_027726.1.
DR   UniGene; Mm.68971; -.
DR   ProteinModelPortal; Q3UGX5; -.
DR   SMR; Q3UGX5; 602-711, 1337-1434, 1598-1919.
DR   STRING; Q3UGX5; -.
DR   PhosphoSite; Q3UGX5; -.
DR   PRIDE; Q3UGX5; -.
DR   Ensembl; ENSMUST00000090398; ENSMUSP00000087879; ENSMUSG00000021782.
DR   GeneID; 71228; -.
DR   KEGG; mmu:71228; -.
DR   UCSC; uc007sqg.1; mouse.
DR   CTD; 71228; -.
DR   MGI; MGI:1918478; Dlg5.
DR   eggNOG; roNOG11635; -.
DR   HOGENOM; HBG443913; -.
DR   HOVERGEN; HBG081446; -.
DR   InParanoid; Q3UGX5; -.
DR   ArrayExpress; Q3UGX5; -.
DR   Bgee; Q3UGX5; -.
DR   Genevestigator; Q3UGX5; -.
DR   GO; GO:0005913; C:cell-cell adherens junction; IDA:MGI.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0042981; P:regulation of apoptosis; IEA:InterPro.
DR   InterPro; IPR001315; CARD.
DR   InterPro; IPR011029; DEATH-like.
DR   InterPro; IPR006907; DUF622.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF04822; DUF622; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF00595; PDZ; 4.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 4.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF47986; DEATH_like; 1.
DR   SUPFAM; SSF50156; PDZ; 4.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50209; CARD; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 4.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
SQ   SEQUENCE   1921 AA;  214382 MW;  410B5FA45E244589 CRC64;
     MEPQRRELLA QCQQSLAQAM TEVEAVLGLL EAAGALSPGE RRQLDEEAGG AKAELLLQLL
     LAKEQDHFQD LRAALEKTQP HLLPILYLNG VVGPPQSTEG AGSTYSVLSI MPSDSESSSS
     LSSVGTTGKA PSPPPLLTEQ QANDTVENLS IQLRLMTRER NELRKRLAFA THGATFDKRP
     YHRLNPDYER LKIQCVRAMS DLQSLQNQHT NALKRCEEVA KETDFYHTLH SRLLSDQTQL
     KDDVDMLRRE NGKLRRERNL LQQSWEDMKR LREEDQKEIG DLRAQQQQVL KHNGSSEILN
     KLYDTAMDKL EVVKKDYDAL RKRYSEKVAM HNSDLSRLEQ LGEENQRLQK QTEMLTQQRD
     TAIQLQHQCA LSLRRFETIH HELSKATAQN KDLQWEMELL QSELTELRSK QVKTAKESEK
     YKEERDAVYS EYKLIMSERD QVISELDKLQ TEVELAESKL KSSTSEKKAA SEEMEALRQI
     KDTVTMDAGR ANKEVEILRK QCKALCQELK EALQEADVAK CRRDWAFQER DKIVAERDSI
     RTLCDNLRRE RDRAVSELAE ALRSLDDTRK QKNDVSRELK ELKEQMECQL EKEARFRQLM
     AHSSHDSAID TDSMEWETEV VEFERETEDI DLKALGFDMA EGVNEPCFPG DCGIFVTKVD
     KGSIADGRLR VNDWLLRIND VDLINKDKKQ AIKALLNGEG AINMVVRRRK SLGGKVVTPL
     HINLSGQKDS GISLENGVYA AAVVPGSPAA KEGSLAVGDR IVAINGIALD NKSLNECESL
     LRSCQDSLTL SLLKVFPQSS SWSGQNIFEN IKDSDRMLSC RAHGPEVQAH NKRNLLQHNN
     STQTDIFYTD RLEDRKELGH SGGSSSFLHK PFSGSSSPVS PQACPSTSER SLNSFRSDTS
     AERGYGLVDM RSQRPLLSFE TEVGPCGAVE VPLDKIDPEG SNSGGPWPKA VLGSTSGPEK
     LSVYKKPKQR KSIFDPNTFK RPQTPPKIDY LLPGPGLTHS PQPSKRVGSL TPPKPPRRSD
     SIKFQHRLET SSESEATLVG SSPSTSPPSA PPPSMDPSEP THASPPRKAR VRIASSYHSE
     GDGDTSYLPA KKPCDEDLTS QKVDELGQKR RRPKSAPSFR PKISPVVIPA QCLEEQECVP
     AIGELSPEGQ EWSPYSPGHA SRHGNPLLYP NRPSVGTVPR SMTPGTTVGS ILRNPIYTVR
     SHRVLPCGSP PVPRDAGSQS LSPSVQHQGR LSLDLSHRAC SDYSEMRASQ GSNSLPSSAR
     LGSSSNLQFK AERIKIPLTP RYPRSVMGSD RGSLSHSECS TPPRSPLNID TLSSCSQPQT
     TASTLPRIAV NPSSHGERRK DRPFVEEPRH VKVQKGSEPL GISIVSGEKG GVYVSKVTLG
     SIAHQAGLEY GDQLLEFNGI NLRSATEQQA RLIIGQQCDT ITILAQYNPH IHQLNSHSRS
     SSHLDPAATP HSTLQGSSAG TPEHPSVIDP LMEQDEGPGT PPAKQSASST RSVGDTTKKT
     PDPRIVFIKK SQLDLGVHLC GGNLHGVFVA EVEDDSPAKG PDGLVPGDLI LEYGSLDMRS
     RTVEDVYVEM LKPKDSLRLK VQYRHEEFTR VKGLPGDSFY IRALYDRLAE VEPELSFKKD
     DILYVDDTLP QGVFGSWMAW QLDENAQKIQ RGQIPSKYVM DQEFSRRLSM SEVKDDNTAK
     TLSAAARRSF FRRKHKHKRS GSKDGKDLLA LDTFSNDSIP LFEDSVSLAY QRVQKVDCTS
     LRPVLLLGPL LDVVKEMLVN EAPGKFCRCP LEVMKASQQA IERGVKDCLF VDYKRRSGHF
     DVTTVASIKE ITEKNRHCLL DIAPHAIERL HHMHIYPIVI FIRYKSAKHI KEQRDPVYLR
     DKVTQRHSKE QFETAQKIDQ EYSRYFTGVV QGGALSSICT QILAMVSQEQ SKVLWIPACP
     P
//
ID   BIG3_MOUSE              Reviewed;        2170 AA.
AC   Q3UGY8; Q80TH0;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Brefeldin A-inhibited guanine nucleotide-exchange protein 3;
GN   Name=Arfgef3; Synonyms=Big3, D10Bwg1379e, Kiaa1244;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 503-2170.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1881, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1646, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Contains 1 SEC7 domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK147679; BAE28069.1; -; mRNA.
DR   EMBL; AK122475; BAC65757.1; -; mRNA.
DR   IPI; IPI00116462; -.
DR   RefSeq; NP_001028430.1; NM_001033258.4.
DR   UniGene; Mm.40491; -.
DR   UniGene; Mm.425612; -.
DR   UniGene; Mm.428163; -.
DR   ProteinModelPortal; Q3UGY8; -.
DR   PhosphoSite; Q3UGY8; -.
DR   PRIDE; Q3UGY8; -.
DR   Ensembl; ENSMUST00000019999; ENSMUSP00000019999; ENSMUSG00000019852.
DR   GeneID; 215821; -.
DR   KEGG; mmu:215821; -.
DR   UCSC; uc007emn.1; mouse.
DR   CTD; 215821; -.
DR   MGI; MGI:106387; D10Bwg1379e.
DR   eggNOG; roNOG10365; -.
DR   GeneTree; ENSGT00530000064150; -.
DR   HOGENOM; HBG506815; -.
DR   HOVERGEN; HBG107499; -.
DR   InParanoid; Q3UGY8; -.
DR   OMA; QLLYLEC; -.
DR   OrthoDB; EOG4CRKZ5; -.
DR   NextBio; 374865; -.
DR   ArrayExpress; Q3UGY8; -.
DR   Bgee; Q3UGY8; -.
DR   Genevestigator; Q3UGY8; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR   InterPro; IPR015403; DUF1981_SEC7_assoc.
DR   InterPro; IPR000904; Sec7.
DR   Pfam; PF09324; DUF1981; 1.
DR   SMART; SM00222; Sec7; 1.
DR   PROSITE; PS50190; SEC7; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1   2170       Brefeldin A-inhibited guanine nucleotide-
FT                                exchange protein 3.
FT                                /FTId=PRO_0000286672.
FT   TRANSMEM   1488   1508       Helical; (Potential).
FT   DOMAIN      579    792       SEC7.
FT   MOD_RES    1646   1646       Phosphoserine.
FT   MOD_RES    1881   1881       Phosphoserine.
FT   MOD_RES    1984   1984       Phosphoserine (By similarity).
SQ   SEQUENCE   2170 AA;  240091 MW;  D759EA53B747F56C CRC64;
     MEEILRKLQR DASGSKYKAI KESCTWALET LGGLDTVVKI PPHLLREKCL LPLQLALESK
     NVKLAQHALA GMQKLLSEER FVSMETDSDE KQLLNQILNA VKVTPSLNED LQVEVMKVLL
     CITYTPTFDM NGSAVLKIAE VCIETYTCSC HQRSINTAVR ATLSQMLGDL TLQLRQRQEN
     TIIENPDAPQ EFRSQGLTVE ALCDDVISVL AVLCEKLQAS INDSQQLQLL YLECILSVLS
     SSSSSMHLHR GFTDLIWKSL CPALVVILGN PIHDKTITSA HSTSTSTSME SDSASLGVSD
     HGRGSGCSCT APTLSGPVAR TIYYLAAELV RLVGSVDSMK PVLQSLYHRV LLYPPPQHRV
     EAIKIMKEIL GSPQRLYDLA GPSSIESEPR KRSISKRKSH LDLLKLIMDG MTEACIKGGI
     EACYAAVSCV CTLLGALDEL SQGKGLNDTQ VQQLLLRLEE LRDGAESSRD SMEINEADFR
     WQRRVLSSEH TPWESGNERS PDISISVTTD TGQTTLEGEL GQTTPEDHKN GLKSPAIQEG
     KGTMGKVSEP EAIDQPDVVQ RSHTVPYPDI TNFLSVDCRT RSYGSRYSES NFSVDDQDLS
     RTEFDSCDQY SMAAEKDSGR SDVSDIGSDN CSLADEEQTP RDYIGHRSLR TAALSLKLLK
     NQEADQHSAR LFIQSLEGLL PRLLALSSVE EVDSALQNFA STFCSGMMHS PGFDGGSSLS
     FQMLMNADSL YTAAHCALLL NLKLSHGDYY RKRPTVAPGM MKEFMKQVQT SGVLMVFSQA
     WLEELYHQVL DRNMLGEAGY WGSPEDNSLP LITMLTDIDG LESSAIGGQL MASASVESPF
     TQSRRLDDST VAGVAFARYI LVGCWKNLID TLSTPLTGRM AGSSKGLAFI LGAEGIKEQN
     QKERDAICMS LDGLRKAARL SCALGVAANC ASALAQMAAA SCVQEEKEER QSQEPSDALA
     QVKLKVEQKL EQMGKVQGVW LHTAHVLCMD AILSVGLEMG SHNPDCWPHV FRVCEYVGTL
     EHTHFSDGIS QPPLTIHQPQ KTSGSSGLLG EIEFKSSSQE QSLEQGPSLN TAPVVQPHSI
     QELVRECSRG RTSDFRGGSL SGNSAAKVVL SLSTQADRLF DDATDKLNLT ALGGFLYQLK
     KASQSQLFHS VTDTVDYSLT MPGEVKSTQD QKSALHLFRL GDAMLRIVRS KARPLLHVMR
     CWSLVAPHLV EAACHKERHV SQKAVSFIHD ILTEVLTDWS EPPHFHFNEA LFRPFERIMQ
     LELCDEDVQD QVVTSIGELV EVCSAQIQSG WRPLFSALET VRSGNKSEVK EYLVGDYSMG
     KGQAPVFDVF EAFLNTDNIQ VFANAATSYI MCLMKFVKGL GEVDCKEIGD CVPGAGATST
     DLCLPALDYL RRCSQLLAKI YKMPLKPIFL SGRLASLPRR LQEQSASSED GIESVLSDFD
     DDTGLIEVWI ILLEQLTAAV SNCPRQHQPP TLDLLFELLR DVTKTPGPGF GIYAVVHLLL
     PVMSLWLLRS HKDHSYWDVA SANFKHAIGL SCELVVEHIQ SFLHSDIRYE SMINTMLKDL
     FELLVVCVAK PTETISRVGC SCIRYVLVTA GPVFTEEMWR LACCALQDAF SATLKPVKDL
     LGCFHGGTEG FSGEGCQVRV AAPSSSPSAE AEYWRIRAMA QQVFMLDTQC SPKTPNNFDH
     AQSCQLIIEL PHDEKPNGHA KKSVSFREIV VSLLSHQVLL QNLYDILLEE FVKGPSPGEE
     KTVQVPDTKL AGFLRYISMQ NLAVIFDLLL DSYRTAREFD TSPGLKCLLK KVSGIGGAAN
     LYRQSAMSFN IYFHALVCAV LTNQETITAE QVKKVLFEEE ERSSDSSQQC SSEDEDIFEE
     TAQVSPPRGK EKRQWRARLP SLSVQPVSNA DWVWLVKRLH KLCMELCNHY IQMHLDLESS
     LEEPLTFKSD PFFILPSFQS ESSTPSTGGF SGKNTPSEDD RREHLSEPQS LRVGSGDMLM
     LPPSPKTEKK DPGRKKEWWE SAGNKICTMA ADKTISKLMT EYKKRRQPHN LPPFPKEVKV
     DKKGEPLGPR GPDSPLLQRP QHLIDQGQMR HSFSAGPELL RQEKRPRSGS TGSSLSVSVR
     DAEAQIQAWT NMVLTVLNQI QILPDQTFTA LQPAVFPCIS QLTCHVTDIR VRQAVREWLG
     RVGRVYDIIT
//
ID   Q3UGZ4_MOUSE            Unreviewed;      2388 AA.
AC   Q3UGZ4;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Spnb3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK147671; BAE28063.1; -; mRNA.
DR   IPI; IPI00134344; -.
DR   UniGene; Mm.329668; -.
DR   ProteinModelPortal; Q3UGZ4; -.
DR   SMR; Q3UGZ4; 49-291, 535-743, 1068-1377, 1912-2000, 2212-2333.
DR   STRING; Q3UGZ4; -.
DR   PhosphoSite; Q3UGZ4; -.
DR   PRIDE; Q3UGZ4; -.
DR   Ensembl; ENSMUST00000008991; ENSMUSP00000008991; ENSMUSG00000067889.
DR   MGI; MGI:1313261; Spnb3.
DR   eggNOG; roNOG09118; -.
DR   HOGENOM; HBG357452; -.
DR   HOVERGEN; HBG057912; -.
DR   InParanoid; Q3UGZ4; -.
DR   OrthoDB; EOG43FGW0; -.
DR   ArrayExpress; Q3UGZ4; -.
DR   Bgee; Q3UGZ4; -.
DR   Genevestigator; Q3UGZ4; -.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR016343; Spectrin_bsu.
DR   InterPro; IPR001605; Spectrin_PH.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00435; Spectrin; 17.
DR   PIRSF; PIRSF002297; Spectrin_beta_subunit; 1.
DR   PRINTS; PR00683; SPECTRINPH.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00150; SPEC; 17.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Repeat.
SQ   SEQUENCE   2388 AA;  270935 MW;  A2F811BA4A703004 CRC64;
     MSSTLSPTDF DSLEIQGQYS DINNRWDLPD SDWDNDSSSA RLFERSRIKA LADEREAVQK
     KTFTKWVNSH LARVTCRVGD LYSDLRDGRN LLRLLEVLSG ETLPKPTKGR MRIHCLENVD
     KALQFLKEQK VHLENMGSHD IVDGNHRLTL GLVWTIILRF QIQDISVETE DNKEKKSAKD
     ALLLWCQMKT AGYPNVNVHN FTTSWRDGLA FNAIVHKHRP DLLDFESLKK CNAHYNLQNA
     FNLAEKELGL TKLLDPEDVN VDQPDEKSII TYVATYYHYF SKMKALAVEG KRIGKVLDHA
     MEAEHLVEKY ESLASELLQW IEQTIVTLND RQLANSLSGV QNQLQSFNSY RTVEKPPKFT
     EKGNLEVLLF TIQSKLRANN QKVYTPREGR LISDINKAWE RLEKAEHERE LALRTELIRQ
     EKLEQLAARF DRKAAMRETW LSENQRLVSQ DNFGLELAAV EAAVRKHEAI ETDIVAYSGR
     VQAVDAVAAE LAAEHYHDIK RIAARQNNVA RLWDFLRQMV AARRERLLLN LELQKVFQDL
     LYLMDWMAEM KGRLQSQDLG KHLAGVEDLL QLHELVEADI AVQAERVRAV SASALRFCDP
     GKEYRPCDPQ LVSERVATLE QSYEALCELA ATRRARLEES RRLWRFLWEV GEAEAWVREQ
     QHLLASADTG RDLTGVLRLL NKHAALRGEM SGRLGPLKLT LEQGQQLVAE GHPGANQAST
     RAAELQAQWE RLEALAEERA QQLAQAASLY QFQADANDME AWLVDALRLV SSPEVGHDEF
     STQALARQHR ALEEEIRAHR PTLDALREQA AALPPALSHT PEVQGRVPTL EQHYEELQAR
     AGERARALEA ALAFYTMLSE AGACGLWVEE KEQWLNGLAL PERLEDLEVV QQRFETLEPE
     MNALAARVTA VNDIAEQLLK ASPPGKDRII GTQEQLNQRW QQFRSLADGK KAALTSALSI
     QNYHLECTET QAWMREKTKV IESTQGLGND LAGVLALQRK LAGTDRDLEP ISARVGELTQ
     EANALAAGHP AQAPAINTRL GEVQAGWEDL RATMRRREES LGEARRLQDF LRSLDDFQAW
     LGRTQTAVAS EEGPATLPEA EALLAQHAAL RGEVERAQSE YSRLRTLGEE VTRDQADPQC
     LFLRQRLEAL GTGWEELGRM WESRQGRLAQ AHGFQGFLRD ARQAEGVLSS QEYVLSHTEM
     PGTLQAADAA IKKLEDFMST MDANGERIRG LLEAGRQLVS KGNIHAEKIQ EKADSIEKRH
     RKNQEAVQQL LGRLRDNREQ QHFLQDCQEL RLWIDEKMLT AQDVSYDEAR NLHTKWQKHQ
     AFMAELAANK DWLDKVDKEG RELTLEKPEL KVVVSEKLED LHRRWDELET TTQAKARSLF
     DANRAELFAQ SCSALESWLE SLQAQLHSDD YGKDLTSVNI LLKKQQMLER EMAVREKEVE
     AIQAQAQALA QEDQSAGEVE RTSRAVEEKF RALCQPMKER CRRLHASREQ HQFHRDVEDE
     ILWVTERLPM ASSLEHGKDL PSVQLLMKKN QTLQKEIQGH EPRIADLKER QRTLGTAAAG
     PELAELQEMW KRLSHELELR GKRLEEALRA QQFYRDAAEA EAWMGEQELH MMGQEKAKDE
     LSAQAEVKKH QVLEQALADY AQTIKQLAAS SQDMIDHEHP ESTRLTIRQA QVDKLYASLK
     ELAGERRERL QEHLRLCQLR RELDDLEQWI QEREVVAASH ELGQDYEHVT MLRDKFREFS
     KDTSTIGQER VDSANALANG LIAGGHAARA TVAEWKDSLN EAWADLLELL DTRGQVLAAA
     YELQRFLHGA RQALARVQHK QQQLPDGTGR DLNAAEALQR RHCAYEHDIQ ALSTQVQQVQ
     DDGQRLQKAY AGDKAEEIGR HMQAVAEAWA QLQGSSAARR QLLLDTTDKF RFFKAVRELM
     LWMDGINLQM DAQERPRDVS SADLVIKNQQ GIKAEIEARA DRFSSCIDMG QELLARSHYA
     AEEISEKLSQ LQSRRQETAD KWQEKMDWLQ LVLEVLVFGR DAGMAEAWLC SQEPLVRSAE
     LGCTVDEVES LIKRHEAFQK SAVAWEERFS ALEKLTALEE RENERKRKRE EEERRKQPPT
     SEPMASQPEG SLVDGQRVPD TAWDGTQSKL PPSTQAPSVN GVCTDTDSSQ PLLEQQRLEQ
     SNVPEGPGSG TGDESSGPRG ERQTLPRGPA PSPMPQSRSS EAAHGATLPT RGPELSAQEQ
     MEGMLCRKQE MEAFNKKAAN RSWQNVYCVL RRGSLGFYKD ARAASAGVPY HGEVPVSLAR
     AQGSVAFDYR KRKHVFKLGL QDGKEYLFQA KDEAEMSSWL RVVNAAIATA SSAPGESEEP
     VVPSASRGLT RAMTMPPVSQ PEGSIVLRSK DGREREREKR FSFFKKNK
//
ID   Q3UH32_MOUSE            Unreviewed;      2724 AA.
AC   Q3UH32;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-FEB-2011, entry version 49.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Trrap;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 FAT domain.
CC   -!- SIMILARITY: Contains 1 FATC domain.
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DR   EMBL; AK147613; BAE28025.1; -; mRNA.
DR   IPI; IPI00330902; -.
DR   UniGene; Mm.273570; -.
DR   STRING; Q3UH32; -.
DR   Ensembl; ENSMUST00000100467; ENSMUSP00000098035; ENSMUSG00000045482.
DR   MGI; MGI:2153272; Trrap.
DR   HOVERGEN; HBG079283; -.
DR   ArrayExpress; Q3UH32; -.
DR   Bgee; Q3UH32; -.
DR   Genevestigator; Q3UH32; -.
DR   GO; GO:0000123; C:histone acetyltransferase complex; TAS:MGI.
DR   GO; GO:0005667; C:transcription factor complex; IDA:MGI.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR   GO; GO:0007093; P:mitotic cell cycle checkpoint; IMP:MGI.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003152; FATC.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000403; PI3/4_kinase_cat.
DR   InterPro; IPR003151; PIK-rel_kinase_FAT.
DR   InterPro; IPR014009; PIK_FAT.
DR   InterPro; IPR011990; TPR-like_helical.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 5.
DR   Gene3D; G3DSA:1.10.1070.11; PI3/4_kinase_cat; 1.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 3.
DR   Pfam; PF02259; FAT; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51189; FAT; 1.
DR   PROSITE; PS51190; FATC; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   2724 AA;  309408 MW;  33995BEB55CA790E CRC64;
     IILGSKERAC QLPLFSYIVE RLCACCYEQA WYAKLGGVVS IKFLMERLPL TWVLQNQQTF
     LKALLFVMMD LTGEVSNGAV AMAKTTLEQL LMRCATPLKD EERAEEIVLA QEKSFHHVTH
     DLVREVTSPN STVRKQAMHS LQVLSQVTGK SVTVIMEPHK EVLQDMVPPK KHLLRHQPAN
     AQIGLMEGNT FCTTLQPRLF TMDLNVVEHK VFYTELLNLC EAEDSALTKL PCYKSLPSLV
     PLRIAALNAL AACNYLPQSR EKIIAALFKA LNSTNSELQE AGEACMRKFL EGATIEVDQI
     HTHMRPLLMM LGDYRSLTLN VVNRLTSVTR LFPNSFNDKF CDQMMQHLRK WMEVVVITHK
     GGQRSDGNEM KICSAIINLF HLIPAAPQTL VKPLLEVVMK TERAMLIEAG SPFREPLIKF
     LTRHPSQTVE LFMMEATLND PQWSRMFMSF LKHKDARPLR DVLAANPNRF ITLLLPGGAQ
     TAVRPGSPST SNMRLDLQFQ AIKIISIIVK NDDAWLASQH SLVSQLRRVW VSETFQERHR
     KENMAATNWK EPKLLAFCLL NYCKRNYGDI ELLFQLLRAF TGRFLCNMTF LKEYMEEEIP
     KNYSIAQKRA LFFRFVEFND PNFGDELKAK VLQHILNPAF LYSFEKGEGE QLLGPPNPEG
     DNPESITSVF ITKVLDPEKQ ADMLDSLRIY LLQYATLLVE HAPHHIHDNN KNRNSKLRRL
     MTFAWPCLLS KACVDPACKY SGHLLLAHII AKFAIHKKIV LQVFHSLLKA HAMEARAIVR
     QAMAILTPAV PARMEDGHQM LTHWTRKIIV EEGHTVPQLV HILHLIVQHF KVYYPVRHHL
     VQHMVSAMQR LGFTPSVTIE QRRLAVDLSE VVIKWELQRI KDQQPDSDMD PNSSGEGVNS
     VSIKRGLSVD SAQEVKRFRA ATGAISAVFG RSQSLPGADS LLAKPIDKQH TDTVVNFLIR
     VACQVNDNTN TAGSPGEVLS RRCVNLLKTA LRPDMWCKSE LKLQWFDKLL MTVEQPNQVN
     YGNICTGLEV LNFLLTVLQS PAILSSFKPL QRGIAACMTC GNTKVLRAVH SLLSRLMSIF
     PTEPSTSSVA SKYEELECLY AAVGKVIYEG LTNYEKATSA NPSQLFGTLM ILKSACCNNP
     SYIDRLISVF MRSLQKMVRE HLNPQTASGS TEATAAGTSE LVMLSLDLVK TRLAVMSMEM
     RKNFIQTILT SLIEKSPDAK ILRAVVKIVE EWVKNNSPMA ANQTPTLREK SILLVKMMTY
     IEKRFPEDLE LNAQFLDLVN YVYRDEALSG SELTAKLEPA FLSGLRCAQP LIRAKFFEVF
     DNSMKRRVYE RLLYVTCSQN WEAMGSHFWI KQCIELLLAV CEKSTAIGTS CQGAMLPSIT
     NVINLADSHD RAAFAMVTHV KQEPRERENS ESKEEDVEID IELAPGDQTS TPKTKELSEK
     DIGNQLHMLT NRHDKFLDTL REVKTGALLS AFVQLCHIST TLAEKTWVQL FPRLWKILSD
     RQQHALAGEI SPFLCSGSHQ VQRDCQPSAL NCFVEAMSQC VPPIPMRPCV LKYLGKTHNL
     WFRSTLMLEH QAFEKGLSLP IKPKQTTEFY EQESITPPQQ EILDSLAELY SLLQEEDMWA
     GLWQKRCKFS ETATAIAYEQ HGFFEQAQES YEKAMDKAKK EHERSNASPA IFPEYQLWED
     HWIRCSKELN QWEALTEFGQ SKGHINPYLV LECAWRVSNW TAMKEALVQV EVSCPKEMAW
     KVNMYRGYLA ICHPEEQQLS FIERLVEMAS SLAIREWRRL PHVVSHVHTP LLQAAQQIIE
     LQEAAQINAG LQPTNLGRNN SLHDMKTVVK TWRNRLPIVS DDLSHWSSVF MWRQHHYQAI
     VTAYENSSHH DPSSNNAMLG VHASASAIIQ YGKIARKQGL VNVALDILSR IHTIPTVPIV
     DCFQKIRQQV KCYLQLAGVM GKNECMQGLE VIESTNLKYF TKEMTAEFYA LKGMFLAQIN
     KSEEANKAFS AAVQMHDVLV KAWAMWGDYL ESIFVKERQL HLGVSAITCY LHACRHQNES
     KSRKYLAKVL WLLSFDDDKN TLADAVDKYC IGVPPIQWLA WIPQLLTCLV GSEGKLLLNL
     ISQVGRVCPQ AVYFPIRTLY LTLKIEQRER YKSDSGQQQP SSACNQSHSA SDPGPIRATA
     PMWRCSRIMH MQRELHPTLL SSLEGIVDQM VWFRENWHEE VLRQLQQGLA KCYSVAFEKS
     GAVSDAKITP HTLNFVKKLV STFGVGLENV SNVSTMFSSA ASESLARRAQ ATAQDPVFQK
     LKGQFTTDFD FSVPGSMKLH NLISKLKKWI KILEAKTKQL PKFFLIEEKC RFLSNFSAQT
     AEVEIPGEFL MPKPTHYYIK IARFMPRVEI VQKHNTAARR LHIRGHNGKI YPYLVMNDAC
     LTESRREERV LQLLRLLNPC LEKRKETTKR HLFFTVPRVV AVSPQMRLVE DNPSSLSLVE
     IYKQRCAKKG IEHDNPISRY YDRLATVQAR GTQASHQVLR DILKEVQSNM VPRSMLKEWA
     LHTFPNATDY WTFRKMFTIQ LALIGFAEFV LHLNRLNPEM LQIAQDTGKL NVAYFRFDIN
     DATGDLDANR PVPFRLTPNI SEFLTTIGVS GPLTASMIAV ARCFAQPNFK VDGVLKTVLR
     DEIIAWHKKT QEDTSSPLSA AGQPENMDSQ QLVSLVQKAV TAIMTRLHNL AQFDGGESKV
     NTLVAAANSL DNLCRMDPAW HPWL
//
ID   SDK1_MOUSE              Reviewed;        2193 AA.
AC   Q3UH53; Q3UFD1; Q6PAL2; Q6V3A4; Q8BMC2; Q8BZI1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Protein sidekick-1;
DE   Flags: Precursor;
GN   Name=Sdk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=FVB/N;
RX   PubMed=15213259; DOI=10.1097/01.ASN.0000128975.28958.C2;
RA   Kaufman L., Hayashi K., Ross M.J., Ross M.D., Klotman P.E.;
RT   "Sidekick-1 is upregulated in glomeruli in HIV-associated
RT   nephropathy.";
RL   J. Am. Soc. Nephrol. 15:1721-1730(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Sympathetic ganglion, Urinary bladder, and Wolffian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-2193 (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Cell adhesion protein that guides axonal terminals to
CC       specific synapses in developing neurons (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UH53-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UH53-2; Sequence=VSP_017520, VSP_017521;
CC         Note=No experimental confirmation available;
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in many fetal tissues,
CC       inlcuding kidney but shows markedly lower expression in adult
CC       organs. Expression in kidney is high throughout development with
CC       maximal expression occurring near birth.
CC   -!- SIMILARITY: Contains 13 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 6 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC28069.1; Type=Erroneous initiation;
CC       Sequence=BAC28986.1; Type=Erroneous initiation;
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DR   EMBL; AY353236; AAQ57662.1; -; mRNA.
DR   EMBL; AK032883; BAC28069.1; ALT_INIT; mRNA.
DR   EMBL; AK035225; BAC28986.1; ALT_INIT; mRNA.
DR   EMBL; AK147578; BAE28004.1; -; mRNA.
DR   EMBL; AK148648; BAE28630.1; -; mRNA.
DR   EMBL; BC060237; AAH60237.1; -; mRNA.
DR   IPI; IPI00420682; -.
DR   IPI; IPI00466076; -.
DR   RefSeq; NP_808547.3; NM_177879.5.
DR   UniGene; Mm.151931; -.
DR   UniGene; Mm.406697; -.
DR   ProteinModelPortal; Q3UH53; -.
DR   SMR; Q3UH53; 83-1554, 1559-1981.
DR   STRING; Q3UH53; -.
DR   PhosphoSite; Q3UH53; -.
DR   PRIDE; Q3UH53; -.
DR   Ensembl; ENSMUST00000074546; ENSMUSP00000074133; ENSMUSG00000039683.
DR   Ensembl; ENSMUST00000085774; ENSMUSP00000082928; ENSMUSG00000039683.
DR   GeneID; 330222; -.
DR   KEGG; mmu:330222; -.
DR   UCSC; uc009ail.1; mouse.
DR   UCSC; uc009ain.1; mouse.
DR   CTD; 330222; -.
DR   MGI; MGI:2444413; Sdk1.
DR   eggNOG; roNOG04747; -.
DR   HOGENOM; HBG402851; -.
DR   HOVERGEN; HBG080083; -.
DR   InParanoid; Q3UH53; -.
DR   OMA; QISWEVY; -.
DR   OrthoDB; EOG4CNQQ4; -.
DR   NextBio; 399244; -.
DR   ArrayExpress; Q3UH53; -.
DR   Bgee; Q3UH53; -.
DR   CleanEx; MM_SDK1; -.
DR   Genevestigator; Q3UH53; -.
DR   GermOnline; ENSMUSG00000039683; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013151; Immunoglobulin.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 19.
DR   Pfam; PF00041; fn3; 13.
DR   Pfam; PF07679; I-set; 4.
DR   Pfam; PF00047; ig; 2.
DR   SMART; SM00060; FN3; 13.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 4.
DR   SUPFAM; SSF49265; FN_III-like; 13.
DR   PROSITE; PS50853; FN3; 13.
DR   PROSITE; PS50835; IG_LIKE; 5.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell adhesion; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1      ?       Potential.
FT   CHAIN         ?   2193       Protein sidekick-1.
FT                                /FTId=PRO_0000226976.
FT   TOPO_DOM      ?   1991       Extracellular (Potential).
FT   TRANSMEM   1992   2012       Helical; (Potential).
FT   TOPO_DOM   2013   2193       Cytoplasmic (Potential).
FT   DOMAIN       86    168       Ig-like C2-type 1.
FT   DOMAIN      173    259       Ig-like C2-type 2.
FT   DOMAIN      275    363       Ig-like C2-type 3.
FT   DOMAIN      368    458       Ig-like C2-type 4.
FT   DOMAIN      462    551       Ig-like C2-type 5.
FT   DOMAIN      556    645       Ig-like C2-type 6.
FT   DOMAIN      650    743       Fibronectin type-III 1.
FT   DOMAIN      750    846       Fibronectin type-III 2.
FT   DOMAIN      851    949       Fibronectin type-III 3.
FT   DOMAIN      954   1045       Fibronectin type-III 4.
FT   DOMAIN     1052   1150       Fibronectin type-III 5.
FT   DOMAIN     1155   1253       Fibronectin type-III 6.
FT   DOMAIN     1258   1353       Fibronectin type-III 7.
FT   DOMAIN     1360   1452       Fibronectin type-III 8.
FT   DOMAIN     1459   1554       Fibronectin type-III 9.
FT   DOMAIN     1560   1677       Fibronectin type-III 10.
FT   DOMAIN     1683   1779       Fibronectin type-III 11.
FT   DOMAIN     1784   1878       Fibronectin type-III 12.
FT   DOMAIN     1885   1978       Fibronectin type-III 13.
FT   COMPBIAS     68     76       Poly-Leu.
FT   CARBOHYD    123    123       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    253    253       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    283    283       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    532    532       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    545    545       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    554    554       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    764    764       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    803    803       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    864    864       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    997    997       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1006   1006       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1264   1264       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1315   1315       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1636   1636       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1730   1730       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1801   1801       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1875   1875       N-linked (GlcNAc...) (Potential).
FT   DISULFID    108    151       By similarity.
FT   DISULFID    297    344       By similarity.
FT   DISULFID    390    440       By similarity.
FT   DISULFID    483    535       By similarity.
FT   DISULFID    577    629       By similarity.
FT   VAR_SEQ       1    260       Missing (in isoform 2).
FT                                /FTId=VSP_017520.
FT   VAR_SEQ     261    265       LSVAR -> MDRSG (in isoform 2).
FT                                /FTId=VSP_017521.
FT   CONFLICT   1009   1009       M -> T (in Ref. 1; AAQ57662).
FT   CONFLICT   1888   1888       P -> L (in Ref. 2; BAE28630).
FT   CONFLICT   1957   1957       E -> G (in Ref. 2; BAC28986).
FT   CONFLICT   2038   2038       L -> Q (in Ref. 2; BAE28630).
SQ   SEQUENCE   2193 AA;  240306 MW;  C22752D48DC4B137 CRC64;
     MARARPSVAG GGVAAPPERA GPGRPRRSRT GHHCDPECPG LRAAPRTPGP GAGRRAAKLR
     PGRGWWALLL LQLHLLRALA QDDVAPYFKT EPGLPQIHLE GNRLVLTCLA EGSWPLEFKW
     IRNDSELTTY SSEYKYIIPS LQKLDAGFYR CVVRNRMGAL LQRKSEIQVA YMGNFMDTDQ
     RKTVSQGHAA LLNLLPIVSC PQPQVTWFRE GHKIIPSSRI AITLENQLVI LATTASDAGA
     YYVQAVNEKN GENKTSPFIH LSVARDTGTH EAMAPIIVVA PGNRSVVAGS SETTLECIAN
     ARPVEELSVH WKRNGVRLTS GLHSYGRRLT ITNPTSADTG MYVCEATLRG STFEPARARA
     FLSIIEPPYF TAEPESRILG EVEETMDIPC RAMGVPLPTL QWYKDAVPLS KLQNPRYKVL
     PSGGLHIQKL SPEDSGIFQC FASNEGGEVQ THTYLDVTNI APAFTQRPVD TTVTDGMTAV
     LRCEVSGAPK PAITWKRGNH ILASGSVRIP RFMLLESGGL RIAPVFIQDA GNYTCYAANT
     EASVNASAML TVWNRTSIVH PPEDRVVIKG TTATLCCGAT HDPRTSLRYV WKKDNVVITA
     SSSSRIVVEK DGSLVISQTW SGDIGDYTCE IISEGGSDSR TARLEVIELP HPPQNLLASL
     SPARSHSVTL SWVRPFDGNS PVLYYIVQVS ENNSPWKVHL SNVGPEMTGV TVSGLTPART
     YQFRVCAVNQ VGKGQYSTET SRLMLPEEPP SAPPKNIVAS GRTNQSIMVQ WQPPPETEHN
     GVLRGYILRY RLAGLPGEHQ QRNISSPEVN YCLVTDLIIW TQYEIQVAAY NGAGLGVFSR
     AVTEYTLQGV PTAPPQNVQA EAVNSTTVHF LWNPPPQQFI NGINQGYKLL AWPADAPETV
     TVVTIAPDFH GIHHGYITNL KKFTAYFTSV LCFTTPGDGP PSSPQLVWTH EDKPGAVGHL
     SFTEILDTSL KVSWQEPLER NGIIMGYQIS WEVYGRNDSR LTHTLNSTMH EYKIQGLSSL
     TTYTIDVAAL TAAGVGVTTS STISSGVPPD LPGAPSNLVI SNISPRSATL QFRPGYDGKT
     AICRWIVEGQ VGAIGDEEEW VTLYEEENEP DAQMLEIPNL TPYTHYRFRM RQVNIVGPSP
     FSQSSRVIQT LQAPPDVAPT SLTVRTASET SLRLRWVPLP DSQYNGNPES VGYRVKYWRS
     DQPSSALAQV VSDRLERELT IEELEEWTEY ELRMQAFNAI GAGPWSELVR GRTRESVPSA
     APENVSAEAV SSTQILLTWA SVPEQDQNGL ILGYKVLYCA KDLDPEPRSH VVRGNHTQSA
     LLAGLRKFVV YELQVLAFTR IGNGVPSSPL ILERTKDDTP GPPVRLVFPE VRLTAVRIVW
     QPPEEPNGVI LGYQIAYRLA SGSPHTFTTV EVGATVRQFT ATELAPESAY IFRLSAKTRQ
     GWGEPLEATV ITTEKRERPA PPRELLVPQA EVTARSLRLQ WVPGSDGASP IRYFTVQVRE
     LPGGEWQTYS SSISHEATAC AVERLRPFTS YKLRLKATND IGDSDFSAET EAVTTLQDVP
     GEPPGSVSAT PHTTSSVLIQ WQPPRDESLN GLLQGYRIYY RELESETGMS PEPKTLKSPS
     ALRAELTAQS SFKTVNSSSS LTTYELTHLK KYRRYEVIMT AYNIIGESPA SVPVEVFVGE
     AAPAMAPQNV QVTPLTASQL EVTWDPPPPE SQNGNIQGYK VYYWEADSRN ETEKMKVLFL
     PEPVVKIKDL TSHTKYLISI SAFNAAGDGP KSDPCQGRTH QAAPGPPSFL AFSEITSTTL
     NVSWGEPSAA NGILQGYRVV YEPLAPVQGV SKVVTVDVKG NWQRWLKVRD LTKGVTYFFR
     VQARTIAYGP ELQANVTAGP AEGSPGSPRN VLVTKSASEL TLQWTEGNAG TTPTTGYVIE
     ARPSDEGLWD MFAKDIPRSA TSYTVDLDKL RQGVTYEFRV VAVNKAGFGE PSRPSIAVSA
     QAEAPFYEEW WFLLVMALSS LLLILLVVFV LVLHGQSKKY KSCSTGKGIS NMEETVTLDN
     GGFAALELNS RHLNVKSTFS KKNGTRSPPR PSPGGLHYSD EDICNKYNGA VLTESVNLKE
     KSVDGSESEA SDSDYEEALP KHSFVNHYMS DPTYYNSWKR RPPAAAPHRY EAVAGAEAGP
     HLHTVITTQS AGGVYTPAGP GARAPLTGFS SFV
//
ID   DIP2B_MOUSE             Reviewed;        1574 AA.
AC   Q3UH60; Q8C1W5; Q8CDG9; Q8CHA2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Disco-interacting protein 2 homolog B;
DE            Short=DIP2 homolog B;
GN   Name=Dip2b; Synonyms=Kiaa1463;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and C57BL/6J; TISSUE=Brain, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 614-1574.
RC   TISSUE=Brain;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-152 AND SER-202,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UH60-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UH60-2; Sequence=VSP_031278, VSP_031279;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the DIP2 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC41112.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK030064; BAC26764.1; -; mRNA.
DR   EMBL; AK090139; BAC41112.1; ALT_INIT; mRNA.
DR   EMBL; AK147562; BAE27997.1; -; mRNA.
DR   EMBL; AB093297; BAC41479.1; -; mRNA.
DR   IPI; IPI00331314; -.
DR   IPI; IPI00761420; -.
DR   RefSeq; NP_001152833.1; NM_001159361.1.
DR   UniGene; Mm.243658; -.
DR   ProteinModelPortal; Q3UH60; -.
DR   SMR; Q3UH60; 335-808, 985-1574.
DR   PhosphoSite; Q3UH60; -.
DR   PRIDE; Q3UH60; -.
DR   Ensembl; ENSMUST00000100203; ENSMUSP00000097777; ENSMUSG00000023026.
DR   GeneID; 239667; -.
DR   KEGG; mmu:239667; -.
DR   UCSC; uc007xqq.1; mouse.
DR   CTD; 239667; -.
DR   MGI; MGI:2145977; Dip2b.
DR   eggNOG; roNOG07765; -.
DR   GeneTree; ENSGT00390000005268; -.
DR   HOGENOM; HBG717784; -.
DR   HOVERGEN; HBG026594; -.
DR   InParanoid; Q3UH60; -.
DR   OMA; FYDERIV; -.
DR   OrthoDB; EOG4KSPHX; -.
DR   PhylomeDB; Q3UH60; -.
DR   NextBio; 384228; -.
DR   ArrayExpress; Q3UH60; -.
DR   Bgee; Q3UH60; -.
DR   Genevestigator; Q3UH60; -.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0008134; F:transcription factor binding; IEA:InterPro.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR010506; DMAP1-bd.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF06464; DMAP_binding; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1   1574       Disco-interacting protein 2 homolog B.
FT                                /FTId=PRO_0000318737.
FT   COMPBIAS    226    231       Poly-Ser.
FT   COMPBIAS   1116   1119       Poly-Ala.
FT   COMPBIAS   1501   1504       Poly-Val.
FT   COMPBIAS   1532   1538       Poly-Val.
FT   MOD_RES       9      9       Phosphoserine (By similarity).
FT   MOD_RES      50     50       Phosphoserine (By similarity).
FT   MOD_RES      53     53       Phosphoserine (By similarity).
FT   MOD_RES      70     70       Phosphothreonine (By similarity).
FT   MOD_RES      99     99       Phosphoserine.
FT   MOD_RES     139    139       Phosphothreonine (By similarity).
FT   MOD_RES     144    144       Phosphoserine (By similarity).
FT   MOD_RES     145    145       Phosphoserine (By similarity).
FT   MOD_RES     147    147       Phosphoserine (By similarity).
FT   MOD_RES     152    152       Phosphoserine.
FT   MOD_RES     202    202       Phosphoserine.
FT   MOD_RES     523    523       Phosphoserine (By similarity).
FT   VAR_SEQ       1    233       Missing (in isoform 2).
FT                                /FTId=VSP_031278.
FT   VAR_SEQ     234    263       PANIDLPPSGIVKGMHKGSNRSSLMDTADG -> MVGFHRR
FT                                CCELTVEKRSSTREEGAWVAFPC (in isoform 2).
FT                                /FTId=VSP_031279.
FT   CONFLICT    303    304       GI -> V (in Ref. 1; BAC26764).
SQ   SEQUENCE   1574 AA;  171126 MW;  915CE0332029FE45 CRC64;
     MAERGLEPSP AAVAALPPEV RAQLAELELE LSEGDITQKG YEKKRSKLLS PYSPQTQETD
     SIGQKERNQT PAPTAAQTSA PSKYHRSRSG GARDERYRSD IHTEAVQAAL AKHKEQKMAL
     PMPTKRRSTF VQSPADACTP PDTSSASEDE GSLRRQAALS AALQQSLQNA ESWINRSIQG
     SSTSSSASST LSHGEVKGTS GSLADVFANT RIENVSAPPD VTATTSSSSS SLRPANIDLP
     PSGIVKGMHK GSNRSSLMDT ADGVPVNSRV STKIQQLLNT LKRPKRPPLK EFFVDDSEEI
     VEGIPQPDPN QPKPEGRQMT PVKGEPLGVI CNWPPALESA LQRWGSTQAK CPCLTGLDVT
     GKPVYTLTYG KLWSRSLKLA YTLLNKLGTK NEPVLKPGDR VALVYPNNDP VMFMVAFYGC
     LLAEVIPVPI EVPLTRKDAG GQQIGFLLGS CGIALALTSE ICLKGLPKTQ NGEIVQFKGW
     PRLKWVVTDS KYLSKPPKDW QPHISPAGTE PAYIEYKTSK EGSVMGVTVS RLAMLSQCQA
     LSQACNYSEG ETVVNVLDFK KDAGLWHGMF ANVMNKMHTI SVPYSVMKTC PLSWVQRVHA
     HKAKVALVKC RDLHWAMMAH RDQRDVSLSS LRMLIVTDGA NPWSVSSCDA FLSLFQSHGL
     KPEAICPCAT SAEAMTVAIR RPGVPGAPLP GRAILSMNGL SYGVIRVNTE DKNSALTVQD
     VGHVMPGGMM CIVKPDGLPQ LCRTDEIGEI CVSSRTGGMM YFGLAGVTKN TFEVIPVTSS
     GSPVGDVPFI RSGLLGFVGP GSLVFVVGKM DGLLMVSGRR HNADDIVATG LAVESIKTVY
     RGRIAVFSVS VFYDERIVVV AEQRPDASEE DSFQWMSRVL QAIDSIHQVG VYCLALVPAN
     TLPKTPLGGI HISQTKQLFL EGSLHPCNIL MCPHTCVTNL PKPRQKQPGV GPASVMVGNL
     VAGKRIAQAA GRDLGQIEEN DLVRKHQFLA EILQWRAQAT PDHVLFMLLN AKGTTVCTAS
     CLQLHKRAER IASVLGDKGH LNAGDNVVLL YPPGIELIAA FYGCLYAGCI PVTVRPPHAQ
     NLTATLPTVR MVVDVSKAAC VLTTQTLMRL LKSREAAAAV DVKTWPAIID TDDLPRKRLP
     QLYKPPTPEM LAYLDFSVST TGMLTGVKMS HSAVNALCRA IKLQCELYSS RQIAICLDPY
     CGLGFALWCL CSVYSGHQSV LIPPMELENN LFLWLATVNQ YKIRDTFCSY SVMELCTKGL
     GNQVEVLKTR GINLSCIRTC VVVAEERPRV SLQQSFSKLF KDIGLSPRAV STTFGSRVNV
     AICLQGTSGP DPTTVYVDLK SLRHDRVRLV ERGAPQSLLL SESGKILPGV KVVIVNPETK
     GPVGDSHLGE IWVNSPHTAS GYYTIYDSET LQADHFNTRL SFGDAAQTLW ARTGYLGFVR
     RTELTAATGE RHDALYVVGA LDETLELRGL RYHPIDIETS VSRVHRSIAE CAVFTWTNLL
     VVVVELCGSE QEALDLVPLV TNVVLEEHYL IVGVVVVVDP GVVPINSRGE KQRMHLRDSF
     LADQLDPIYV AYNM
//
ID   Q3UH88_MOUSE            Unreviewed;       681 AA.
AC   Q3UH88;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 53.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Agap1; Synonyms=Centg2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK147521; BAE27969.1; -; mRNA.
DR   IPI; IPI00652802; -.
DR   UniGene; Mm.291135; -.
DR   ProteinModelPortal; Q3UH88; -.
DR   SMR; Q3UH88; 6-115, 221-416, 434-651.
DR   STRING; Q3UH88; -.
DR   Ensembl; ENSMUST00000074945; ENSMUSP00000074478; ENSMUSG00000055013.
DR   UCSC; uc007byy.1; mouse.
DR   MGI; MGI:2653690; Agap1.
DR   eggNOG; roNOG13144; -.
DR   GeneTree; ENSGT00600000084361; -.
DR   HOVERGEN; HBG054045; -.
DR   OrthoDB; EOG479F6D; -.
DR   ArrayExpress; Q3UH88; -.
DR   Bgee; Q3UH88; -.
DR   Genevestigator; Q3UH88; -.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR001164; ArfGAP.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR020849; Ras_small_GTPase.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF57863; ArfGAP; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   2: Evidence at transcript level;
KW   ANK repeat; GTP-binding; Nucleotide-binding; Repeat.
SQ   SEQUENCE   681 AA;  75054 MW;  25A8EF42F565F416 CRC64;
     MKGAPPEAQF AMWVDAVIFV FSLEDEISFQ TVYHYYSRMA NYRNTSEIPL VLVGTQDAIS
     STNPRVIDDV RARKLSNDLK RCTYYETCAT YGLNVERVFQ DVAQKIVATR KKQQLSIGPC
     KSLPNSPSHS SVCSAQVSAV HISQTSNGGG SLSDYSSSVP STPSTSQKEL RIDVPPTANT
     PTPVRKQSKR RSNLFTSRKG SDPDKEKKGL ESRADSIGSG RAIPIKQGML LKRSGKSLNK
     EWKKKYVTLC DNGVLTYHPS LHDYMQNVHG KEIDLLRTTV KVPGKRPPRA TSACAPISSP
     KTNGLAKDMS SLHISPNSDT GLGDSVCSSP SISSSTSPKL DPPPSPHANR KKHRRKKSTS
     NFKADGLSGT AEEQEENLEF IIVSLTGQTW HFEATTYEER DAWVQAIESQ ILASLQSCES
     SKNKSRLTSQ SEAMALQSIR NMRGNSHCVD CDTQNPNWAS LNLGALMCIE CSGIHRNLGT
     HLSRVRSLDL DDWPMELIKV MSSIGNELAN SVWEEGSQGR TKPSLDSTRE EKERWIRAKY
     EQKLFLAPLP CTEFSLGQQL LRATAEEDLR TVILLLAHGS RDEVNETCGE GDGRTALHLA
     CRKGNVVLAQ LLIWYGVDVM ARDAHGNTAL AYARQASSQE CIDVLLQYGC PDERFVLMAT
     PNLSRKSNSR NNSSGRAPSV I
//
ID   Q3UH89_MOUSE            Unreviewed;       801 AA.
AC   Q3UH89;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 39.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Pcdhb19;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Potential calcium-dependent cell-adhesion protein. May
CC       be involved in the establishment and maintenance of specific
CC       neuronal connections in the brain (By similarity).
CC   -!- SIMILARITY: Contains 6 cadherin domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK147520; BAE27968.1; -; mRNA.
DR   IPI; IPI00314590; -.
DR   RefSeq; NP_444374.2; NM_053144.2.
DR   UniGene; Mm.118311; -.
DR   ProteinModelPortal; Q3UH89; -.
DR   SMR; Q3UH89; 34-137, 140-339.
DR   Ensembl; ENSMUST00000059571; ENSMUSP00000053326; ENSMUSG00000043313.
DR   GeneID; 93890; -.
DR   KEGG; mmu:93890; -.
DR   CTD; 93890; -.
DR   MGI; MGI:2136757; Pcdhb19.
DR   eggNOG; roNOG07110; -.
DR   HOGENOM; HBG447181; -.
DR   HOVERGEN; HBG054878; -.
DR   InParanoid; Q3UH89; -.
DR   OrthoDB; EOG4SXNBX; -.
DR   ArrayExpress; Q3UH89; -.
DR   Bgee; Q3UH89; -.
DR   Genevestigator; Q3UH89; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR013164; Cadherin_N.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 6.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF08266; Cadherin_2; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 6.
DR   SUPFAM; SSF49313; Cadherin; 5.
DR   PROSITE; PS00232; CADHERIN_1; 5.
DR   PROSITE; PS50268; CADHERIN_2; 6.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell membrane; Membrane; Repeat;
KW   Transmembrane; Transmembrane helix.
SQ   SEQUENCE   801 AA;  87904 MW;  FCE6DB6D2F7121E6 CRC64;
     MENQEGLYLQ TRQVLLLFVF LGMSQAHSEA GRLSVVEEML SGALVGNLVK DLGLQVDELS
     AREAQVASSD NKLPLQLNIN TGDLLLSEPL DREELCGSTE PCVLHFQVLL KNPLKILQAE
     LQVTDVNDNS PVFLEKEMVL EIPENSPVGA VFLLESAIDL DVGINAVKSY EISQNSHFHV
     TMRVNPDGRK YPELVLDKAL DYEEQHELRL ILTALDGGTP PRSGTALVRV EVIDINDNSP
     EFDHMFYEVT VPENSMLGSL LITASAWDLD SGINGEVSYA FSHASEDIRK TFAINEHSGE
     IRLKGYLDFE TTESYSIIIK ATDRGGLFGK STVRIQVMDV NDNFPEIIVS SFISPIPENT
     AETLVMIFSI RDKDSGENGK MVCTIPEGLP FVLKSSIENY YHLETDGALD RESIAEYNIT
     ISVTDLGTPR LTTQHTIIVQ VADINDNAPT FTQTSYTMFF HENNSPALHI GTISATDSDA
     GSNAHITYSL MSAQDLQMAL SSLISINADN GQLFALRALD YEVLQAFEFQ VGATDRGSPA
     LSSQALVRVV VLDDNDNAPF VLYPMQNASA PCTELLPRAA EPGYLVTKVV AVDRDSGQNA
     WLSFQLLKAT EPGLFSVWAH NGEVRTTRLL SERDAPKHRL LLLVKDNGDP PRSASVTLHV
     LVVDGFSQPY LPLPEVARNP AHEEDALTLY LVTALASVSS LFLLSVMLFV GVRLCRRARA
     ASLGGCTVPE GHFPDHLMGI NSAGTLSQSY QYEVCLMGGS GTNEFRFLKP VSPNLQPQFP
     GKEIEESSTL RNSFGLFRDC N
//
ID   Q3UH93_MOUSE            Unreviewed;      1925 AA.
AC   Q3UH93;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 52.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Plxnd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 Sema domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK147513; BAE27964.1; -; mRNA.
DR   IPI; IPI00471022; -.
DR   RefSeq; NP_080652.2; NM_026376.3.
DR   UniGene; Mm.3085; -.
DR   ProteinModelPortal; Q3UH93; -.
DR   SMR; Q3UH93; 889-984, 1548-1653.
DR   STRING; Q3UH93; -.
DR   PhosphoSite; Q3UH93; -.
DR   PRIDE; Q3UH93; -.
DR   Ensembl; ENSMUST00000015511; ENSMUSP00000015511; ENSMUSG00000030123.
DR   GeneID; 67784; -.
DR   KEGG; mmu:67784; -.
DR   CTD; 67784; -.
DR   MGI; MGI:2154244; Plxnd1.
DR   HOGENOM; HBG716170; -.
DR   HOVERGEN; HBG053404; -.
DR   InParanoid; Q3UH93; -.
DR   OMA; CSSLYEE; -.
DR   OrthoDB; EOG49CQ6S; -.
DR   PhylomeDB; Q3UH93; -.
DR   NextBio; 325553; -.
DR   ArrayExpress; Q3UH93; -.
DR   Bgee; Q3UH93; -.
DR   Genevestigator; Q3UH93; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IC:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0017154; F:semaphorin receptor activity; IPI:MGI.
DR   GO; GO:0060666; P:dichotomous subdivision of terminal units involved in salivary gland branching; IDA:MGI.
DR   GO; GO:0001569; P:patterning of blood vessels; IMP:MGI.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002909; IPT_TIG_rcpt.
DR   InterPro; IPR003659; Plexin-like.
DR   InterPro; IPR016201; Plexin-like_fold.
DR   InterPro; IPR013548; Plexin_cytoplasmic_RasGAP_dom.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR001627; Semaphorin/CD100_Ag.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 4.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF08337; Plexin_cytopl; 1.
DR   Pfam; PF01437; PSI; 2.
DR   Pfam; PF01403; Sema; 2.
DR   Pfam; PF01833; TIG; 3.
DR   SMART; SM00429; IPT; 3.
DR   SMART; SM00423; PSI; 3.
DR   SMART; SM00630; Sema; 1.
DR   SUPFAM; SSF81296; Ig_E-set; 3.
DR   SUPFAM; SSF103575; Plexin-like_fold; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   SUPFAM; SSF101912; Sema; 1.
DR   PROSITE; PS51004; SEMA; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
SQ   SEQUENCE   1925 AA;  211608 MW;  7385B372DC53AF2E CRC64;
     MARRAAGGAP PSARAAAAVP LRPRPHSRGP GLLPLPLLLL LGAARAGALE IQRRFPSPTP
     TNNFALDGTA GTVYLAAVNR LYQLSSANLS LEAEATVGPV PDSPLCHAPQ LPQASCEHPR
     RLTDNYNKIL QLDPGQGLVV ACGSIYQGLC QLRRRGNISA LAVSFPPAAP TAEPVTVFPS
     MLNVAANHPN ASTVGLVLPP TSGTGGSRLL VGATYTGFGS AFFPRNRSLE DHRFENTPEI
     AIRSLDARGD LAKLFTFDLN PSDDNILKIK QGAKEQHKLG FVRAFLHPAV PPHSAQPYAY
     LALNSEARAG DKDSQARSLL ARICLPRGAG GDAKKLTESY IQLGLQCAGG AGRGDLYSRL
     VSVFPAREQF FAVFERPQGA PGARNAPAAL CAFRFDDVQA AIRAARTACF VEPAPDVVAV
     LDSVVQGTGP ACESKRNIQL QPEQLDCGAA HLQHPLTILQ PLRASPVFRA PGLTAVAVAS
     ANNYTAVFLG TATGRLLKIS LNESMQVVSR RVLTVAYGEP VHHVMQFDPM DPGYLYLMTS
     HQMARVKVAA CEVHSTCGDC VGAADAYCGW CTLETRCTLQ QDCTNSSQPH FWTSASEGPS
     RCPAMTVLPS EIDVHRDYTG MILQISGSLP SLSGMEMACD YGNGVRTVAR VPGPAYDHQI
     AYCNLLPRAQ FPSFPAGQDH VTVEMSVRVK GHNIVSANFT IYDCSRIGQV YPHTACTSCL
     STQWPCSWCI QLHSCVSNQS QCQDSPNPTS PQDCPQILPS PLAPVPTGGS QDILVPLTKA
     TFFHGSSLEC SFGLEESFEA VWANNSLVRC NQVVLHTTQK SQVFPLSLKL KGPPDRFLDS
     PNPMTVVVYN CAMGSPDCSQ CLGREDLGHL CVWNDGCRLR GPLQPLPGTC PAPEIRAIEP
     LSGPLDGGTL LTIRGRNLGR RLSDVAHGVW IGSVACEPLA DRYTVSEEIV CATGPAAGAF
     SDVVTVNVSK EGRSREQFSY VLPTVHSLEP SMGPKAGGTR ITIHGSDLNV GSMLQVLVND
     TDPCTDLTRT ATSITCTVPG GTLPSPVPVC VRFESRGCVH GNLTFWYMQN PVITAISPGR
     SPVSGGRTIT VAGERFHMVQ NVSMAVHHIG REPTFCKVLN STLITCPSPG ALSNASAPVD
     FFINGRAYAD EAAEELLDPA EAQRGSRFRL DYLPNPQFST AKREKWIKHH PGEPLTLVIH
     KEQDSLGLES HEYHIKIGQV SCDIQIISDR VIHCSVNESL GTAEGQLPIT IQVGNFNQTI
     ATLQLGGSET AIVVSIVICS VLLLLSVVAL FVFCTKSRRA ERYWQKTLLQ MEEMESQIRE
     EIRKGFAELQ TDMTDLTKEL NRSQGIPFLE YKHFVTRTFF PKCSSLYEER YVLPSKTLNS
     QGGSPPQETH PLLGEWNIPE HCRPSMEEGI SLFSSLLNNK HFLIVFVHAL EQQKDFAVRD
     RCSLASLLTI ALHGKLEYYT SIMKELLVDL IDASAAKNPK LMLRRTESVV EKMLTNWMSI
     CMYGCLRETV GEPFFLLLCA IKQQINKGSI DAITGKARYT LNEEWLLREN IEAKPRNLNV
     SFQGCGMDSL SVRAMDTDTL TQVKEKILEA FCKNVPYSQW PRAEDVDLEW FASSTQSYVL
     RDLDDTSVVE DGRKKLNTLA HYKIPEGASL AMSLTDKKDS TLGRVKDLDT EKYFHLVLPT
     DELVEPKKSH RQSHRKKVLP EIYLTRLLST KGTLQKFLDD LFKAILSIRE DKPPLAVKYF
     FDFLEEQAEK RGISDPDTLH IWKTNSLPLR FWVNILKNPQ FVFDIEKTDH IDACLSVIAQ
     AFIDACSISD LQLGKDSPTN KLLYAKEIPE YRKTVQRYYK QIQDMTPLSE QEMNAHLAEE
     SRKYQNEFNT NVAMAEIYKY AKRYRPQIMA ALEANPTARR TQLQHKFEQV VALMENNIYE
     CYSEA
//
ID   Q3UH98_MOUSE            Unreviewed;       833 AA.
AC   Q3UH98;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Acap3; Synonyms=Centb5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK147505; BAE27959.1; -; mRNA.
DR   IPI; IPI00466479; -.
DR   UniGene; Mm.219591; -.
DR   ProteinModelPortal; Q3UH98; -.
DR   SMR; Q3UH98; 3-360, 403-826.
DR   PRIDE; Q3UH98; -.
DR   Ensembl; ENSMUST00000105584; ENSMUSP00000101209; ENSMUSG00000029033.
DR   MGI; MGI:2153589; Acap3.
DR   HOGENOM; HBG314594; -.
DR   HOVERGEN; HBG050889; -.
DR   InParanoid; Q3UH98; -.
DR   ArrayExpress; Q3UH98; -.
DR   Bgee; Q3UH98; -.
DR   Genevestigator; Q3UH98; -.
DR   GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR001164; ArfGAP.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF57863; ArfGAP; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   ANK repeat; Repeat.
SQ   SEQUENCE   833 AA;  92762 MW;  AFE644F09CCD816B CRC64;
     MTVEFEECIK DSPRFRATID EVETDVVEIE AKLDKLVKLC SGMIEAGKAY VTTNRLFVSG
     VRDLSQQCQG DTVISECLQR FGDSLQEMVN YHTILFDQAQ RSVRQQLHNF AKEDVRKFKE
     TKKQFDKVRE DMELSLVRNA QAPRHRPHEV EEATGALTVT RKCFRHLALD YVLQINVLQA
     KKKFEILDSM LSFMHAQYSF FQQGYSLLHQ LDPYMKKLAA ELDQLVIDSA VEKREMERKH
     AAIQQRTLLQ DFSYDEPKVE FDVDAPSGVV MEGYLFKRAS NAFKTWNRRW FSIQNSQLVY
     QKKLKDALTV VVDDLRLCSV KPCEDIERRF CFEVVSPTKS CMLQADSEKL RQAWVQAVQA
     SIASAYRESP DSCYSERLDR TASPSTSSID STTDSRERGV KGESVLQRVQ SVAGNSQCGD
     CGQPDPRWAS INLGVLLCIE CSGIHRSLGV HCSKVRSLTL DSWEPELLKL MCELGNSTVN
     QIYEAQCEGP GVRKPTASSS RQDKEAWIKD KYVEKKFLRK LTSAPAREPP RRWRAQKCQR
     PHSSPHAPTT RRKVRLEPVL PSVAALSSAA TMERKFRRDS LFCPDELDSL FSYFDAGAAG
     AGPRSLSSDS GLGGSSDGSS DVLAFGTGSV VDSVTEEEGA ESEESSSEVD GEAEAWSLAD
     VRELHPGLLA HQAARTRDLP ALAAALAHGA EVNWADAADE GKTPLVQAVL GGSLIVCEFL
     LQNGADVNQR DSLGRAPLHH ATLLGRTGQV CLFLKRGADQ HALDQEQQDP LTIAVQAANA
     DIVTLLRLAR MAEEMREAEA PPGQPGPLPG SSPTELQYRR CIQEFIGLHL EES
//
ID   SHSA6_MOUSE             Reviewed;         525 AA.
AC   Q3UH99;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 38.
DE   RecName: Full=Protein shisa-6 homolog;
DE   Flags: Precursor;
GN   Name=Shisa6; Synonyms=Gm879;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- SIMILARITY: Belongs to the shisa family.
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DR   EMBL; AK147504; BAE27958.1; -; mRNA.
DR   IPI; IPI00380894; -.
DR   RefSeq; NP_001030046.1; NM_001034874.3.
DR   UniGene; Mm.351764; -.
DR   ProteinModelPortal; Q3UH99; -.
DR   PhosphoSite; Q3UH99; -.
DR   PRIDE; Q3UH99; -.
DR   Ensembl; ENSMUST00000066679; ENSMUSP00000071025; ENSMUSG00000053930.
DR   GeneID; 380702; -.
DR   KEGG; mmu:380702; -.
DR   UCSC; uc007jlm.1; mouse.
DR   CTD; 380702; -.
DR   MGI; MGI:2685725; Shisa6.
DR   eggNOG; roNOG04428; -.
DR   GeneTree; ENSGT00510000047247; -.
DR   HOGENOM; HBG444407; -.
DR   HOVERGEN; HBG108632; -.
DR   InParanoid; Q3UH99; -.
DR   OMA; HRPPREM; -.
DR   NextBio; 401129; -.
DR   ArrayExpress; Q3UH99; -.
DR   Bgee; Q3UH99; -.
DR   CleanEx; MM_GM879; -.
DR   Genevestigator; Q3UH99; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     30       Potential.
FT   CHAIN        31    525       Protein shisa-6 homolog.
FT                                /FTId=PRO_0000326155.
FT   TOPO_DOM     31    180       Extracellular (Potential).
FT   TRANSMEM    181    201       Helical; (Potential).
FT   TOPO_DOM    202    525       Cytoplasmic (Potential).
FT   COMPBIAS     31     93       Ala-rich.
FT   CARBOHYD     37     37       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     62     62       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   525 AA;  58426 MW;  1F9706B52F0F3C47 CRC64;
     MALRRLLLPP LLLSLLLSLA SLHLPPGADA ARGRSGNRTL NAGAVGGRRA GGALARGGRE
     LNSTARASGV PEAGSRRGQS AAAAAAAAAA ASATVTYETC WGYYDVSGQY DKEFECNNSE
     SGYLYCCGTC YYRFCCKKRH EKLDQRQCTN YQSPVWVQTP STKVVSPGPE NKYDPEKDKT
     NFTVYITCGV IAFVIVAGVF AKVSYDKAHR PPREMNIHRA LADILRQQGP IPIAHCERET
     ISAIDTSPKE NTPVRSTSKN HYTPVRTAKQ TPGDRQYNHP ILSSATQTPT HEKPRMNNIL
     TSATEPYDLS FSRSYQNLAH LPPSYESAVK TNPSKYSSLK RLTDKEADEY YMRRRHLPDL
     AARGTLPLNV IQMSQQKPLP RERPRRPIRA MSQDRVLSPR RGLPDEFGMP YDRILSDEQL
     LSTERLHSQD PLLSPERTAF PEQSLSRAIS HTDVFVSTPV LDRYRMTKMH SHPSASNNSY
     ATLGQSQTAA KRHAFASRRH NTVEQLHYIP GHHTCYTASK TEVTV
//
ID   Q3UHB2_MOUSE            Unreviewed;      1808 AA.
AC   Q3UHB2;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Tsc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK147487; BAE27945.1; -; mRNA.
DR   IPI; IPI00230482; -.
DR   UniGene; Mm.30435; -.
DR   ProteinModelPortal; Q3UHB2; -.
DR   SMR; Q3UHB2; 1508-1725.
DR   STRING; Q3UHB2; -.
DR   PRIDE; Q3UHB2; -.
DR   Ensembl; ENSMUST00000097374; ENSMUSP00000094987; ENSMUSG00000002496.
DR   UCSC; uc008axb.1; mouse.
DR   MGI; MGI:102548; Tsc2.
DR   HOVERGEN; HBG018005; -.
DR   ArrayExpress; Q3UHB2; -.
DR   Bgee; Q3UHB2; -.
DR   Genevestigator; Q3UHB2; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0071889; F:14-3-3 protein binding; IDA:MGI.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IGI:MGI.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase cascade; IMP:MGI.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; IMP:MGI.
DR   GO; GO:0051898; P:negative regulation of protein kinase B signaling cascade; IGI:MGI.
DR   GO; GO:0032007; P:negative regulation of TOR signaling cascade; IMP:MGI.
DR   GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR   GO; GO:0014065; P:phosphatidylinositol 3-kinase cascade; IMP:MGI.
DR   GO; GO:0050918; P:positive chemotaxis; IMP:MGI.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR   GO; GO:0006606; P:protein import into nucleus; IMP:MGI.
DR   GO; GO:0043491; P:protein kinase B signaling cascade; IGI:MGI.
DR   GO; GO:0030100; P:regulation of endocytosis; IMP:MGI.
DR   GO; GO:0046626; P:regulation of insulin receptor signaling pathway; IMP:MGI.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0001666; P:response to hypoxia; IMP:MGI.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000331; Rap_GAP.
DR   InterPro; IPR003913; Tuberin.
DR   InterPro; IPR018515; Tuberin-type_domain.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 3.
DR   Pfam; PF02145; Rap_GAP; 1.
DR   Pfam; PF03542; Tuberin; 1.
DR   PRINTS; PR01431; TUBERIN.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50085; RAPGAP; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1808 AA;  201371 MW;  4DCA687B08F2DEFB CRC64;
     MAKPTSKDSG LKEKFKILLG LGTSRPNPRC AEGKQTEFII TSEILRELSG ECGLNNRIRM
     IGQICDVAKT KKLEEHAVEA LWKAVSDLLQ PERPPEARHA VLTLLKAIVQ GQGDRLGVLR
     ALFFKVIKDY PSNEDLHERL EVFKALTDNG RHITYLEEEL AEFVLQWMDV GLSSEFLLVL
     VNLVKFNSCY LDEYIASMVH MICLLCIRTV SSVDIEVSLQ VLDAVVCYNC LPAESLPLFI
     ITLCRTINVK ELCEPCWKLM RNLLGTHLGH SAIYNMCRIM EDRSYMEDAP LLRGAVFFVG
     MALWGAHRLY SLKNSPTSVL PSFYEAMTCP NEVVSYEIVL SITRLIKKYR KELQAVTWDI
     LLDIIERLLQ QLQNLDSPEL KTIVHDLLTT VEELCDQNEF HGSQERYYEL VESYADQRPE
     SSLLNLISYR AQSIHPAKDG WIQNLQLLME RFFRNECRSA VRIKVLDVLS FVLLINRQFY
     EEELINSVVI SQLSHIPEDK DHQVRKLATQ LLVDLAEGCH THHFNSLLDI IEKVMARSLS
     PPPELEERDL AMHSASLEDV KTAVLGLLVI LQTKLYTLPA SHATRVYESL ISHIQLHYKH
     GYSLPIASSI RLQAFDFLLL LRADSLHRLG LPNKDGVVRF SPYCLCDCME LDRASEKKAS
     GPLSPPTGPP SPVPMGPAVR LGYLPYSLLF RVLLQCLKQE SDWKVLKLVL SRLPESLRYK
     VLIFTSPCSV DQLSSALCSM LSAPKTLERL RGTPEGFSRT DLHLAVVPVL TALISYHNYL
     DKTRQREMVY CLEQGLIYRC ASQCVVALAI CSVEMPDIII KALPVLVVKL THISATASMA
     IPLLEFLSTL ARLPHLYRNF AAEQYASVFA ISLPYTNPSK FNQYIVCLAH HVIAMWFIRC
     RLPFRKDFVP YITKGLRSNV LLSFDDTPEK DSFRARSTSL NERPKSLRIA RAPKQGLNNS
     PPVKEFKESC AAEAFRCRSI SVSEHVVRSR IQTSLTSASL GSADENSMAQ ADDNLKNLHL
     ELTETCLDMM ARYVFSNFTA VPKRSPVGEF LLAGGRTKTW LVGNKLVTVT TSVGTGTRSL
     LGLDSGDLQG GSDSSSDPST HVRQTKEAPA KLESQAGQQV SRGARDRVRS MSGGHGLRVG
     VLDTSAPYSP GGSASLGPQT AVAAKPEKPP AGAQLPTAEK TNLAAYVPLL TQGWAEILVR
     RPTGNTSWLM SLENPLSPFS SDINNMPLQE LSNALMAAER FKEHRDTALY KSLSVPAAGT
     AKPPTLPRSN TVASFSSLYQ PSCQGQLHRS VSWADSAMVL EEGSPGETQV PVEPPELEDF
     EAALGTDRHC QRPDTYSRSS SASSQEEKSH LEELAAGGIP IERAISSEGA RPAVDLSFQP
     SQPLSKSSSS PELQTLQDIL GDLGDKIDIG RLSPEAKVRS QSGILDGEAA TWSATGEESR
     ITVPPEGPLP SSSPRSPSGL RPRGYTISDS APSRRGKRVE RDNFKSRAAA SSAEKVPGIN
     PSFVFLQLYH SPFFGDESNK PILLPNESFE RSVQLLDQIP SYDTHKIAVL YVGEGQSSSE
     LAILSNEHGS YRYTEFLTGL GRLIELKDCQ PDKVYLGGLD VCGEDGQFTY CWHDDIMQAV
     FHIATLMPTK DVDKHRCDKK RHLGNDFVSI IYNDSGEDFK LGTIKGQFNF VHVIITPLDY
     KCNLLTLQCR KDMEGLVDTS VAKIVSDRNL SFVARQMALH ANMASQVHHS RSNPTDIYPS
     KWIARLRHIK RLRQRIREEV HYSNPSLPLM HPPAHTKAPA QAPEATPTYE TGQRKRLISS
     VDDFTEFV
//
ID   Q3UHB8_MOUSE            Unreviewed;       706 AA.
AC   Q3UHB8;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 36.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Gm1568;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
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DR   EMBL; AK147473; BAE27939.1; -; mRNA.
DR   IPI; IPI00421140; -.
DR   RefSeq; NP_001008423.2; NM_001008423.2.
DR   UniGene; Mm.29367; -.
DR   ProteinModelPortal; Q3UHB8; -.
DR   PhosphoSite; Q3UHB8; -.
DR   PRIDE; Q3UHB8; -.
DR   Ensembl; ENSMUST00000073251; ENSMUSP00000072982; ENSMUSG00000062961.
DR   GeneID; 380768; -.
DR   KEGG; mmu:380768; -.
DR   UCSC; uc007obh.1; mouse.
DR   MGI; MGI:2686414; Gm1568.
DR   eggNOG; maNOG16763; -.
DR   HOGENOM; HBG125231; -.
DR   HOVERGEN; HBG062226; -.
DR   InParanoid; Q3UHB8; -.
DR   OMA; ERAQRAN; -.
DR   OrthoDB; EOG45DWPT; -.
DR   PhylomeDB; Q3UHB8; -.
DR   NextBio; 401213; -.
DR   ArrayExpress; Q3UHB8; -.
DR   Bgee; Q3UHB8; -.
DR   Genevestigator; Q3UHB8; -.
PE   1: Evidence at protein level;
SQ   SEQUENCE   706 AA;  79857 MW;  566BCD2DB34E641C CRC64;
     MVDPVPEEEK EGAEPGGSEG DEATASEPPD AQGAQQPAAS SASASAAAPR KAEVPCGAEG
     GRREQSPLLH LDLFNFACPE AEGSRYVLTS PRSLEACARC AVKPVELLPR ALADLVREAP
     GRSMRVATGL YEAYEAERLA KLQQCRAERE RIMREEKRRL FTPKGPAAAP ASASASASAS
     ALSGGSSSSC SSSSSLPASP ASRVARRTSP SPPARSRPPP AGSRTGRKSH SLDSLSRRRD
     GALSSESGAS SSSYSGESLR ELRWPPRASA RNSCPAGSAS SAPNPLGRPS ALALVPLTAR
     SFSLGDLSHS PQTAQHVERI VRQVRAERGL RGVPERDRKI AALMLARHQE ERLLLEQRAA
     AHGQWEQQRV RAEQRREREE REKQRALERG RRAWAAQVEE RRGRRGREER EAARRRQQQC
     ERSEERRREL AERQGLLRRE RVERAARDDR LRKLQQEQNL KQREEGRQEG RERAELVRRE
     RAQRAARARE RQEGQLQREK RELSRAERAR HEALLRGRVR QQQEEREGLR SSLEASLGRA
     QENYEQLQEQ RARELRERAR REELQGRRAK EAAERKEREH QAHLEALARA GERRLQHAAQ
     VAEEAVQQKA RRVVQTRLEK ERAQRANKEK VERDEDCRRR ELLQAIGRKL ERSEQLSRER
     RSALESARST ARASFHVREK VREETNTRSF DRMVREAQLH ASLDRK
//
ID   TNR6C_MOUSE             Reviewed;        1690 AA.
AC   Q3UHC0; Q3UZ61; Q80TB6; Q8BXF9;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   08-FEB-2011, entry version 52.
DE   RecName: Full=Trinucleotide repeat-containing gene 6C protein;
GN   Name=Tnrc6c; Synonyms=Kiaa1582;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and C57BL/6J; TISSUE=Brain, Cerebellum, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 329-1690.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1002, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: Plays a role in RNA-mediated gene silencing by micro-
CC       RNAs (miRNAs). Required for miRNA-dependent translational
CC       repression of complementary mRNAs by argonaute family proteins (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with one or more of the argonaute family
CC       proteins EIF2C1/AGO1, EIF2C2/AGO2, EIF2C3/AGO3 and EIF2C4/AGO4 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the GW182 family.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -!- SIMILARITY: Contains 1 UBA domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE27937.1; Type=Erroneous initiation;
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DR   EMBL; AK047249; BAC33005.1; -; mRNA.
DR   EMBL; AK134064; BAE21997.1; -; mRNA.
DR   EMBL; AK147471; BAE27937.1; ALT_INIT; mRNA.
DR   EMBL; AK122529; BAC65811.1; -; mRNA.
DR   IPI; IPI00337947; -.
DR   RefSeq; NP_932139.2; NM_198022.2.
DR   UniGene; Mm.40272; -.
DR   UniGene; Mm.473244; -.
DR   ProteinModelPortal; Q3UHC0; -.
DR   SMR; Q3UHC0; 923-993, 1509-1587.
DR   STRING; Q3UHC0; -.
DR   PhosphoSite; Q3UHC0; -.
DR   PRIDE; Q3UHC0; -.
DR   Ensembl; ENSMUST00000026658; ENSMUSP00000026658; ENSMUSG00000025571.
DR   Ensembl; ENSMUST00000106344; ENSMUSP00000101951; ENSMUSG00000025571.
DR   GeneID; 217351; -.
DR   KEGG; mmu:217351; -.
DR   UCSC; uc007mni.1; mouse.
DR   CTD; 217351; -.
DR   MGI; MGI:2443265; Tnrc6c.
DR   eggNOG; roNOG11538; -.
DR   GeneTree; ENSGT00410000025966; -.
DR   HOVERGEN; HBG062594; -.
DR   InParanoid; Q3UHC0; -.
DR   NextBio; 375797; -.
DR   ArrayExpress; Q3UHC0; -.
DR   Bgee; Q3UHC0; -.
DR   CleanEx; MM_TNRC6C; -.
DR   Genevestigator; Q3UHC0; -.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   InterPro; IPR019486; Argonaute_hook_dom.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR009060; UBA-like.
DR   InterPro; IPR000449; UBA/transl_elong_EF1B_N.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF10427; Ago_hook; 1.
DR   Pfam; PF00627; UBA; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF46934; UBA_like; 1.
DR   PROSITE; PS50102; RRM; FALSE_NEG.
DR   PROSITE; PS50030; UBA; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Phosphoprotein; RNA-binding; RNA-mediated gene silencing;
KW   Translation regulation.
FT   CHAIN         1   1690       Trinucleotide repeat-containing gene 6C
FT                                protein.
FT                                /FTId=PRO_0000278527.
FT   DOMAIN      928    973       UBA.
FT   DOMAIN     1565   1632       RRM.
FT   REGION        1   1037       Sufficient for interaction with argonaute
FT                                family proteins (By similarity).
FT   REGION     1371   1690       Sufficient for translational repression
FT                                when tethered to a target mRNA (By
FT                                similarity).
FT   COILED     1156   1214       Potential.
FT   COMPBIAS     57     60       Poly-Ser.
FT   COMPBIAS    204    430       Gly-rich.
FT   COMPBIAS    904    910       Poly-Ser.
FT   COMPBIAS   1215   1248       Pro-rich.
FT   MOD_RES     714    714       Phosphoserine (By similarity).
FT   MOD_RES    1002   1002       Phosphoserine.
FT   CONFLICT   1521   1521       L -> P (in Ref. 1; BAE21997).
SQ   SEQUENCE   1690 AA;  175775 MW;  4788764371891904 CRC64;
     MATGSAQSSF PSHLKKTNGS HGTNGALVQS PSNQSALGAG GTNGNGGVAR VWGVATSSSS
     GLAHCSVGGG DGKMDNMIGD GRSQNCWGAS NSNAGINLNL NPNANPAAWP VLGHEGTVAT
     GNPSSICSPV SAIGQNMGSQ NGNPVGALGA WGNLLPQESA EPQTSTSQNV SFSVQPQNLN
     TDGPNNTNPM NSSPNPINAM QTNGLPNWGM AVGMGAIIPP HLQGLPGANG SSVSQGSGSG
     GEGMGSSVWG LSPGNPATGS TNCGFSQGNG DTVNSALSAK QNGSSSAVQK EGNGGNAWDS
     GPPAGPGILA WGRGSGTNGI GNIHSGAWGH PSRSSSNGVN GEWGKPPNQH SSSDISGKGS
     TGWDSASAAS QTPALQPGSE HMNSWAKATS SGTTASEGSS DGSGNHNEGS TGREGTGEGR
     RRDKGVLDQG HIQLPRNDLD PRVLSNSGWG QTPVKQNTAW EFEESPRSER KNDNGTEAWG
     SIATQPSNSG GKTDGSIMNS TNTSSVSGWV SSPPAAVPAN TSWGDSNNKA PSGPGVWGDS
     ISSTAVNNAA ATKSGHAWSG TVNQEDKSPT WGEPQKPKSQ NWGDGQRANP AWSTGAGDWA
     DSSSVLGHLG DGKKNGSGWD ADGNRSGSGW NDATRCGTSG WGSGTNAKVN PGTNWGESLK
     PGPQQNWAHK PQDNNVSNWG GAASVKQTGT GWIGGPLPVK QKDSSEATGW EEPSPPSIRR
     KMEIDDGTSA WGDPSTYNNK TVNMWDRNNP VIQSSTTAPA TPTTPTSSST THRAETPPSH
     QAGTQLNRSP LLGPVSSGWG EMPSVHSKAE NSWGEPSSPC TLVDNGTAAW GKPPSSGSGW
     DHPAEPVVPF GRASAPAAAP ALCKPASKSM QEGWGSGADE MNLGTSQWED EDGDMWNNAA
     SQESSSSCSS WGNTSKKGLQ KGMKTPGKQD EAWIMSRLIK QLTDMGFPRE PAEEALKSNS
     MNLDQAMSAL LEKKVDMDKR GLGMTDYNGM VTKPLGCRPP ISKESSMDRP TFLDKLTLSF
     SNQDGGLVEE PTTSPFLPSP SLKLPLSNSA LPSQALGGVA SGLGMQNLNS SRQIPSGNLG
     VFGNSGAAQA RTMQQPPVQP LNSSQPSLRA QVPQFLSPQV QAQLLQFAAK NIGLSPALLT
     SPINPQHMTM LNQLYQLQLA YQRLQIQQQM LQAQRNVSGP MRQQEQQVAR TITNLQQQIQ
     QHQRQLAQAL LVKQPPPPPP PPHLSLHPSA GKSGMESFPP PPQAPGLPDL QTKEQQSSPN
     TFAPYPLAGL NPNMNVNSID MSSGLSVKDP SQSQSRLPQW THPNSMGNLS SAASPLDQNP
     SKHGAIPGGL SIGPPGKSSI DDSYGRYDLI QNSESPASPP VAVPHSWSRA KSDSDKISNG
     SSISWPPEFH PGVPWKGLQN IDPENDPDVT PGSVPTGPTI NTTIQDVNRY LLKSGGKLSD
     IKSTWSSGPA SHTQASLSHE LWKVPRNTTA PTRPPPGLAN PKPSSTWGTS PLGWTSSYSS
     GSAWSTDTSG RTSSWLVLRN LTPQIDGSTL RTLCLQHGPL ITFHLNLTQG NAVVRYSSKE
     EAAKAQKSLH MCVLGNTTIL AEFAGEEEVN RFLAQGQALP PTSSWQSSSG GSQPRLGTSG
     STHGLVRSDT AHWNTPCLSG KGSSELLWGG VPQYSSSLWG PPSAEDARVI GSPTPLNTLL
     PGDLLSGESI
//
ID   DAB2P_MOUSE             Reviewed;        1189 AA.
AC   Q3UHC7; A2AUW9; A2AUX2; B7ZD28; Q3TPD5; Q3UH44; Q6JTV1; Q80T97;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Disabled homolog 2-interacting protein;
DE            Short=DAB2-interacting protein;
GN   Name=Dab2ip; Synonyms=Kiaa1743;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), ALTERNATIVE
RP   SPLICING, AND TISSUE SPECIFICITY.
RC   STRAIN=129S6/SvEvTac; TISSUE=Spleen;
RX   PubMed=16629596; DOI=10.1089/dna.2006.25.232;
RA   Chen H., Karam J.A., Schultz R., Zhang Z., Duncan C., Hsieh J.-T.;
RT   "Cloning of mouse Dab2ip gene, a novel member of the RasGTPase-
RT   activating protein family and characterization of its regulatory
RT   region in prostate.";
RL   DNA Cell Biol. 25:232-245(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 328-1189 (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-702, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-978, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Functions as a Ras GTPase-activating protein. Through
CC       its interaction with MAP3K5 disrupts the association of MAP3K5
CC       with the inhibitory 14-3-3 complex. Mediates TNF/TRAF2-induced
CC       MAP3K5-JNK activation, while it inhibits CHUK-NF-kappa-B
CC       signaling. May act as a tumor suppressor gene (By similarity).
CC   -!- SUBUNIT: Interacts with MAP3K5, preferentially with its 'Ser-966'
CC       dephosphorylated form. On plasma membrane, exists in an inactive
CC       form complexed with TNFR1. In response to TNF, dissociates from
CC       TNFR1 complex, tranlocates to cytoplasm and forms part of an
CC       intracellular signaling complex comprising TRADD, RALBP1, TRAF2
CC       and MAP3K5. Binding to MAP3K5 is induced by TNF. Interacts with
CC       DAB1 and DAB2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral
CC       membrane protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3UHC7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UHC7-2; Sequence=VSP_020956;
CC       Name=3;
CC         IsoId=Q3UHC7-3; Sequence=VSP_020957;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in the brain, salivary gland,
CC       and testis; moderate expression in kidney and heart. Low
CC       expression in the lung, seminal vesicle, ventral prostate,
CC       epididymis, liver, and bladder. Very low expression in the
CC       coagulation gland and skeleton muscles. Lowest expression seen in
CC       spleen.
CC   -!- DOMAIN: C2 and GAP domains constitutively bind to MAP3K5 and
CC       facilitate the release of 14-3-3 from MAP3K5. The C2 domain is
CC       critical for MAP3K5 binding (By similarity).
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 Ras-GAP domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAQ77379.1; Type=Erroneous initiation;
CC       Sequence=AAQ77380.1; Type=Erroneous initiation;
CC       Sequence=AAQ77381.1; Type=Erroneous initiation;
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DR   EMBL; AY305656; AAQ77379.1; ALT_INIT; mRNA.
DR   EMBL; AY305657; AAQ77380.1; ALT_INIT; mRNA.
DR   EMBL; AY305658; AAQ77381.1; ALT_INIT; mRNA.
DR   EMBL; AK147464; BAE27930.1; -; mRNA.
DR   EMBL; AK147593; BAE28013.1; -; mRNA.
DR   EMBL; AK164475; BAE37801.1; -; mRNA.
DR   EMBL; AL929241; CAX15340.1; -; Genomic_DNA.
DR   EMBL; AL929241; CAM25773.2; -; Genomic_DNA.
DR   EMBL; AL929241; CAM25777.1; -; Genomic_DNA.
DR   EMBL; BC118530; AAI18531.1; -; mRNA.
DR   EMBL; AK122548; BAC65830.1; -; mRNA.
DR   IPI; IPI00420622; -.
DR   IPI; IPI00753148; -.
DR   IPI; IPI00755543; -.
DR   RefSeq; NP_001001602.2; NM_001001602.2.
DR   RefSeq; NP_001107596.1; NM_001114124.1.
DR   UniGene; Mm.29629; -.
DR   HSSP; P21359; 1NF1.
DR   ProteinModelPortal; Q3UHC7; -.
DR   SMR; Q3UHC7; 144-202, 212-315, 329-662.
DR   MINT; MINT-136025; -.
DR   STRING; Q3UHC7; -.
DR   PhosphoSite; Q3UHC7; -.
DR   PRIDE; Q3UHC7; -.
DR   Ensembl; ENSMUST00000091010; ENSMUSP00000088532; ENSMUSG00000026883.
DR   Ensembl; ENSMUST00000112992; ENSMUSP00000108616; ENSMUSG00000026883.
DR   GeneID; 69601; -.
DR   KEGG; mmu:69601; -.
DR   UCSC; uc008jkp.1; mouse.
DR   UCSC; uc008jks.1; mouse.
DR   CTD; 69601; -.
DR   MGI; MGI:1916851; Dab2ip.
DR   GeneTree; ENSGT00600000084217; -.
DR   HOVERGEN; HBG006492; -.
DR   InParanoid; Q3UHC7; -.
DR   OMA; QSMSILP; -.
DR   OrthoDB; EOG473PQJ; -.
DR   NextBio; 329884; -.
DR   ArrayExpress; Q3UHC7; -.
DR   Bgee; Q3UHC7; -.
DR   Genevestigator; Q3UHC7; -.
DR   GermOnline; ENSMUSG00000026883; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0070059; P:apoptosis in response to endoplasmic reticulum stress; IMP:BHF-UCL.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IMP:BHF-UCL.
DR   GO; GO:0035414; P:negative regulation of catenin import into nucleus; IMP:BHF-UCL.
DR   GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:BHF-UCL.
DR   GO; GO:0071901; P:negative regulation of protein serine/threonine kinase activity; IMP:BHF-UCL.
DR   GO; GO:0043065; P:positive regulation of apoptosis; IMP:BHF-UCL.
DR   GO; GO:0043507; P:positive regulation of JUN kinase activity; IMP:BHF-UCL.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR021887; DUF3498.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001936; RasGAP.
DR   InterPro; IPR023152; RasGAP_CS.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.10.506.10; RasGAP; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF12004; DUF3498; 1.
DR   Pfam; PF00616; RasGAP; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00323; RasGAP; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50004; C2; FALSE_NEG.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW   GTPase activation; Membrane; Phosphoprotein; Tumor suppressor.
FT   CHAIN         1   1189       Disabled homolog 2-interacting protein.
FT                                /FTId=PRO_0000252408.
FT   DOMAIN      101    202       PH.
FT   DOMAIN      200    295       C2.
FT   DOMAIN      371    563       Ras-GAP.
FT   COILED     1025   1159       Potential.
FT   COMPBIAS      8     52       Arg-rich.
FT   COMPBIAS    112    117       Poly-Ala.
FT   COMPBIAS    867    870       Poly-Ala.
FT   COMPBIAS    903    948       Pro-rich.
FT   MOD_RES     702    702       Phosphoserine.
FT   MOD_RES     747    747       Phosphoserine (By similarity).
FT   MOD_RES     978    978       Phosphoserine.
FT   MOD_RES     992    992       Phosphoserine (By similarity).
FT   MOD_RES     995    995       Phosphoserine (By similarity).
FT   MOD_RES    1168   1168       Phosphoserine (By similarity).
FT   VAR_SEQ       1    124       Missing (in isoform 2).
FT                                /FTId=VSP_020956.
FT   VAR_SEQ     990   1040       Missing (in isoform 3).
FT                                /FTId=VSP_020957.
SQ   SEQUENCE   1189 AA;  131726 MW;  E3AF3FDA71FF96C3 CRC64;
     MSAGGNARKS TGRPSYYYRL LRRPRLQRQR SRSRSRTRPA RESPQERPGS RRSLPGSMSE
     KNPSMEPSAS TPFRVTGFLS RRLKGSIKRT KSQPKLDRNH SFRHILPGFR SAAAAAADNE
     RSHLMPRLKE SRSHESLLSP SSAVEALDLS MEEEVIIKPV HSSILGQDYC FEVTTSSGSK
     CFSCRSAAER DKWMENLRRA VHPNKDNSRR VEHILKLWVI EAKDLPAKKK YLCELCLDDV
     LYARTTSKLK TDNVFWGEHF EFHNLPPLRT VTVHLYRETD KKKKKERNSY LGLVSLPAAS
     VAGRQFVEKW YPVVTPNPKG GKGPGPMIRI KARYQTVSIL PMEMYKEFAE HITNHYLGLC
     AALEPILSAK TKEEMASALV HILQSTGKVK DFLTDLMMSE VDRCGDNEHL IFRENTLATK
     AIEEYLKLVG QKYLQDALGE FIKALYESDE NCEVDPSKCS SADLPEHQGN LKMCCELAFC
     KIINSYCVFP RELKEVFASW RQECSSRGRP DISERLISAS LFLRFLCPAI MSPSLFNLLQ
     EYPDDRTART LTLIAKVTQN LANFAKFGSK EEYMSFMNQF LEHEWTNMQR FLLEISNPET
     LSNTAGFEGY IDLGRELSSL HSLLWEAVSQ LDQSVVSKLG PLPRILRDVH TALSTPGSGQ
     LPGTNDLAST PGSGSSSVSA GLQKMVIEND LSGLIDFTRL PSPTPENKDL FFVTRSSGVQ
     PSPARSSSYS EANEPDLQMA NGSKSLSMVD LQDARTLDGE AGSPVGPDAL PADGQVPATQ
     LLAGWPARAA PVSLAGLATV RRAVPTPTTP GTSEGAPGRP QLLAPLSFQN PVYQMAAGLP
     LSPRGLGDSG SEGHSSLSSH SNSEELAAAA KLGSFSTAAE ELARRPGELA RRQMSLTEKG
     GQPTVPRQNS AGPQRRIDQP PPPPPPPPPA PRGRTPPTLL STLQYPRPSS GTLASASPDW
     AGPGTRLRQQ SSSSKGDSPE LKPRAMHKQG PSPVSPNALD RTAAWLLTMN AQLLEDEGLG
     PDPPHRDRLR SKEELSQAEK DLAVLQDKLR ISTKKLEEYE TLFKCQEETT QKLVLEYQAR
     LEEGEERLRR QQEDKDIQMK GIISRLMSVE EELKKDHAEM QAAVDSKQKI IDAQEKRIAS
     LDAANARLMS ALTQLKERYS MQARNGVSPT NPTKLQITEN GEFRNSSNC
//
ID   BAI1_MOUSE              Reviewed;        1582 AA.
AC   Q3UHD1; Q3UH36; Q8CGM0;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=Brain-specific angiogenesis inhibitor 1;
DE   Flags: Precursor;
GN   Name=Bai1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND INTERACTION WITH PHYHIP.
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=21143048; PubMed=11245925; DOI=10.1016/S0169-328X(01)00004-3;
RA   Koh J.T., Lee Z.H., Ahn K.Y., Kim J.-K., Bae C.S., Kim H.-H.,
RA   Kee H.J., Kim K.K.;
RT   "Characterization of mouse brain-specific angiogenesis inhibitor 1
RT   (BAI1) and phytanoyl-CoA alpha-hydroxylase-associated protein 1, a
RT   novel BAI1-binding protein.";
RL   Brain Res. Mol. Brain Res. 87:223-237(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF 1255-1268, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   FUNCTION.
RX   PubMed=11875720; DOI=10.1038/sj.bjc.6600067;
RA   Duda D.G., Sunamura M., Lozonschi L., Yokoyama T., Yatsuoka T.,
RA   Motoi F., Horii A., Tani K., Asano S., Nakamura Y., Matsuno S.;
RT   "Overexpression of the p53-inducible brain-specific angiogenesis
RT   inhibitor 1 suppresses efficiently tumour angiogenesis.";
RL   Br. J. Cancer 86:490-496(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1276 AND SER-1467, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH ELMO1 AND DOCK1.
RX   PubMed=17960134; DOI=10.1038/nature06329;
RA   Park D., Tosello-Trampont A.-C., Elliott M.R., Lu M., Haney L.B.,
RA   Ma Z., Klibanov A.L., Mandell J.W., Ravichandran K.S.;
RT   "BAI1 is an engulfment receptor for apoptotic cells upstream of the
RT   ELMO/Dock180/Rac module.";
RL   Nature 450:430-434(2007).
CC   -!- FUNCTION: Likely to be a potent inhibitor of angiogenesis in brain
CC       and may play a significant role as a mediator of the p53 signal in
CC       suppression of glioblastoma. May function in cell adhesion and
CC       signal transduction in the brain (By similarity).
CC   -!- SUBUNIT: Interacts with MAGI1, MAGI3, BAIAP2 and PHYHIP (By
CC       similarity). Interacts with ELMO1 and DOCK1. When bound to ELMO1
CC       and DOCK1, it may act as a module to promote the engulfment.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity). Note=Likely to be concentrated at cell-cell
CC       adhesion sites (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UHD1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UHD1-2; Sequence=Not described;
CC         Note=Observed very weakly in the kidney, skeletal muscle, skin,
CC         stomach, thymus and brain from embryonic day 18. By neonatal day
CC         1, the expression is targeted only to the brain;
CC   -!- TISSUE SPECIFICITY: Specifically expressed in brain.
CC   -!- DEVELOPMENTAL STAGE: Observed only on embryonic brain not in other
CC       tissues.
CC   -!- DOMAIN: The TSP1 repeats inhibit in vivo angiogenesis in rat
CC       cornea induced by BFGF.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       LN-TM7 subfamily.
CC   -!- SIMILARITY: Contains 1 GPS domain.
CC   -!- SIMILARITY: Contains 5 TSP type-1 domains.
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DR   EMBL; AY168408; AAN86966.1; -; mRNA.
DR   EMBL; AK147494; BAE27949.1; -; mRNA.
DR   EMBL; AK147456; BAE27923.1; -; mRNA.
DR   EMBL; AK147459; BAE27926.1; -; mRNA.
DR   EMBL; AK147607; BAE28021.1; -; mRNA.
DR   IPI; IPI00229528; -.
DR   RefSeq; NP_778156.2; NM_174991.3.
DR   UniGene; Mm.43133; -.
DR   ProteinModelPortal; Q3UHD1; -.
DR   SMR; Q3UHD1; 217-519, 522-576.
DR   STRING; Q3UHD1; -.
DR   PhosphoSite; Q3UHD1; -.
DR   PRIDE; Q3UHD1; -.
DR   Ensembl; ENSMUST00000042035; ENSMUSP00000046097; ENSMUSG00000034730.
DR   GeneID; 107831; -.
DR   KEGG; mmu:107831; -.
DR   UCSC; uc007wco.1; mouse.
DR   CTD; 107831; -.
DR   MGI; MGI:1933736; Bai1.
DR   eggNOG; roNOG11919; -.
DR   HOGENOM; HBG714232; -.
DR   HOVERGEN; HBG004813; -.
DR   InParanoid; Q3UHD1; -.
DR   OMA; DSKPEKQ; -.
DR   OrthoDB; EOG4SF955; -.
DR   NextBio; 359547; -.
DR   ArrayExpress; Q3UHD1; -.
DR   Bgee; Q3UHD1; -.
DR   CleanEx; MM_BAI1; -.
DR   Genevestigator; Q3UHD1; -.
DR   GermOnline; ENSMUSG00000034730; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:InterPro.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:InterPro.
DR   InterPro; IPR022624; DUF3497.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR008077; GPCR_2_brain-spec_angio_inhib.
DR   InterPro; IPR001879; GPCR_2_extracellular_dom.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR000203; GPS_dom.
DR   InterPro; IPR000884; Thrombospondin_1_rpt.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF12003; DUF3497; 1.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF02793; HRM; 1.
DR   Pfam; PF00090; TSP_1; 5.
DR   PRINTS; PR01694; BAIPRECURSOR.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   SMART; SM00303; GPS; 1.
DR   SMART; SM00008; HormR; 1.
DR   SMART; SM00209; TSP1; 5.
DR   SUPFAM; SSF82895; TSP1; 5.
DR   PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG.
DR   PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; FALSE_NEG.
DR   PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
DR   PROSITE; PS50092; TSP1; 5.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     33       Potential.
FT   CHAIN        34   1582       Brain-specific angiogenesis inhibitor 1.
FT                                /FTId=PRO_0000245046.
FT   TOPO_DOM     34    948       Extracellular (Potential).
FT   TRANSMEM    949    969       Helical; Name=1; (Potential).
FT   TOPO_DOM    970    980       Cytoplasmic (Potential).
FT   TRANSMEM    981   1001       Helical; Name=2; (Potential).
FT   TOPO_DOM   1002   1008       Extracellular (Potential).
FT   TRANSMEM   1009   1029       Helical; Name=3; (Potential).
FT   TOPO_DOM   1030   1052       Cytoplasmic (Potential).
FT   TRANSMEM   1053   1073       Helical; Name=4; (Potential).
FT   TOPO_DOM   1074   1093       Extracellular (Potential).
FT   TRANSMEM   1094   1114       Helical; Name=5; (Potential).
FT   TOPO_DOM   1115   1136       Cytoplasmic (Potential).
FT   TRANSMEM   1137   1157       Helical; Name=6; (Potential).
FT   TOPO_DOM   1158   1166       Extracellular (Potential).
FT   TRANSMEM   1167   1187       Helical; Name=7; (Potential).
FT   TOPO_DOM   1188   1582       Cytoplasmic (Potential).
FT   DOMAIN      261    315       TSP type-1 1.
FT   DOMAIN      354    407       TSP type-1 2.
FT   DOMAIN      409    462       TSP type-1 3.
FT   DOMAIN      467    520       TSP type-1 4.
FT   DOMAIN      522    575       TSP type-1 5.
FT   DOMAIN      881    938       GPS.
FT   MOTIF       231    233       Cell attachment site (Potential).
FT   COMPBIAS   1382   1449       Pro-rich.
FT   MOD_RES    1276   1276       Phosphoserine.
FT   MOD_RES    1467   1467       Phosphoserine.
FT   CARBOHYD     64     64       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    401    401       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    607    607       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    692    692       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    844    844       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    877    877       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    881    881       N-linked (GlcNAc...) (Potential).
FT   DISULFID    273    309       By similarity.
FT   DISULFID    277    314       By similarity.
FT   DISULFID    288    299       By similarity.
FT   DISULFID    366    400       By similarity.
FT   DISULFID    370    406       By similarity.
FT   DISULFID    381    390       By similarity.
FT   DISULFID    421    456       By similarity.
FT   DISULFID    425    461       By similarity.
FT   DISULFID    436    446       By similarity.
FT   DISULFID    479    514       By similarity.
FT   DISULFID    483    519       By similarity.
FT   DISULFID    494    504       By similarity.
FT   DISULFID    534    569       By similarity.
FT   DISULFID    538    574       By similarity.
FT   DISULFID    549    559       By similarity.
FT   CONFLICT    264    264       W -> L (in Ref. 1; AAN86966).
FT   CONFLICT    275    286       RDCGGGLQTRTR -> AGLRGRPANSNP (in Ref. 1;
FT                                AAN86966).
FT   CONFLICT    300    300       E -> K (in Ref. 1; AAN86966).
FT   CONFLICT    821    821       D -> G (in Ref. 2; BAE28021).
SQ   SEQUENCE   1582 AA;  173297 MW;  6D1AA6D46E2E223B CRC64;
     MRGQAAAPGP IWILAPLLLL LLLLGRWARA ASGADIGPGT EQCTTLVQGK FFGYFSAAAV
     FPANASRCSW TLRNPDPRRY TLYMKVAKAP APCSGPGRVR TYQFDSFLES TRTYLGVESF
     DEVLRLCDSS APLAFLQASK QFLQMQRQQP PQDGDLGPQG EFPSSSDDFS VEYLVVGNRN
     PSHAACQMLC RWLDACLAGS RSSHPCGIMQ TPCACLGGDV GDPASSPLVP RGDVCLRDGV
     AGGPENCLTS LTQDRGGHGS AGGWKLWSLW GECTRDCGGG LQTRTRTCLP TLGVEGGGCE
     GVLEEGRLCN RKACGPTGRS SSRSQSLRST DARRREEFGD ELQQFGFPSP QTGDPAAEEW
     SPWSVCSSTC GEGWQTRTRF CVSSSYSTQC SGPLREQRLC NNSAVCPVHG AWDEWSPWSL
     CSSTCGRGFR DRTRTCRPPQ FGGNPCEGPE KQTKFCNIAL CPGRAVDGNW NEWSSWSTCS
     ASCSQGRQQR TRECNGPSYG GAECQGHWVE TRDCFLQQCP VDGKWQAWAS WGSCSVTCGG
     GSQRRERVCS GPFFGGAACQ GPQDEYRQCG AQRCPEPHEI CDEDNFGAVV WKETPAGEVA
     AVRCPRNATG LILRRCELDE EGIAFWEPPT YIRCVSIDYR NIQMMTREHL AKAQRGLPGE
     GVSEVIQTLL EISQDGTSYS GDLLSTIDVL RNMTEIFRRA YYSPTPGDVQ NFVQIISNLL
     AEENRDKWEE AQLMGPNAKE LFRLVEDFVD VIGFRMKDLR DAYQVTDNLV LSIHKLPASG
     ATDISFPMKG WRATGDWAKV PEDRVTVSKS VFSTGLAEAD DSSVFVVGTV LYRNLGSFLA
     LQRNTTVLNS KVISVTVKPP PRSLLTPLEI EFAHMYNGTT NQTCILWDET DGPSSSAPPQ
     LGPWSWRGCR TVPLDALRTR CLCDRLSTFA ILAQLSADAT MDKVTVPSVT LIVGCGVSSL
     TLLMLVIIYV SVWRYIRSER SVILINFCLS IISSNALILI GQTQTRNKVV CTLVAAFLHF
     FFLSSFCWVL TEAWQSYMAV TGRLRSRLVR KRFLCLGWGL PALVVAISVG FTKAKGYSTM
     NYCWLSLEGG LLYAFVGPAA AVVLVNMVIG ILVFNKLVSK DGITDKKLKE RAGASLWSSC
     VVLPLLALTW MSAVLAVTDR RSALFQILFA VFDSLEGFVI VMVHCILRRE VQDAVKCRVV
     DRQEEGNGDS GGSFQNGHAQ LMTDFEKDVD LACRSVLNKD IAACRTATIT GTFKRPSLPE
     EEKMKLAKGP PPTFNSLPAN VSKLHLHGSP RYPGGPLPDF PNHSLTLKKD KAPKSSFIGD
     GDIFKKLDSE LSRAQEKALD TSYVILPTAT ATLRPKPKEE PKYSINIDQM PQTRLIHLSM
     APDASFPTRS PPAREPPGGA PPEVPPVQPP PPPPPPPPPP QQPIPPPPTL EPAPPSLGDT
     GEPAAHPGPS SGAGAKNENV ATLSVSSLER RKSRYAELDF EKIMHTRKRH QDMFQDLNRK
     LQHAAEKEKE VPGADSKPEK QQTPNKRAWE SLRKPHGTPA WVKKELEPLP PSPLELRSVE
     WEKAGATIPL VGQDIIDLQT EV
//
ID   MTUS2_MOUSE             Reviewed;        1353 AA.
AC   Q3UHD3; B9EKJ2; Q7TPP7; Q8CHD2; Q9CY74;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   RecName: Full=Microtubule-associated tumor suppressor candidate 2 homolog;
DE   AltName: Full=Cardiac zipper protein;
DE   AltName: Full=Microtubule plus-end tracking protein TIP150;
DE            Short=Tracking protein of 150 kDa;
GN   Name=Mtus2; Synonyms=Cazip, Kiaa0774, Tip150;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 201-1353 (ISOFORM 2).
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [4]
RP   ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX   PubMed=19806667; DOI=10.1002/dvdy.22107;
RA   Du Puy L., Beqqali A., Monshouwer-Kloots J., Haagsman H.P.,
RA   Roelen B.A., Passier R.;
RT   "CAZIP, a novel protein expressed in the developing heart and nervous
RT   system.";
RL   Dev. Dyn. 238:2903-2911(2009).
CC   -!- FUNCTION: Binds microtubules. Together with MAPRE1 may target the
CC       microtubule depolymerase KIF2C to the plus-end of microtubules.
CC       May regulate the dynamics of microtubules at their growing distal
CC       tip (By similarity).
CC   -!- SUBUNIT: Homodimer. Interacts with KIF2C and MAPRE1; the
CC       interaction is direct and probably targets MTUS2 and KIF2C to
CC       microtubules (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Associated
CC       with the microtubule network at the growing distal tip (the plus-
CC       end) of microtubules (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q3UHD3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UHD3-2; Sequence=VSP_023547;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q3UHD3-3; Sequence=VSP_023545, VSP_023546;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q3UHD3-4; Sequence=VSP_023544, VSP_023548;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in heart from early embryonic
CC       development onwards. Later during embryonic development, expressed
CC       in brain and nervous system, in limb buds and in the epithelium
CC       lining the bronchia of the lung. Detected in adult brain, heart
CC       and eye, but not detected in other adult tissues examined.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the MTUS1
CC       family.
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DR   EMBL; AK019985; BAB31952.1; -; mRNA.
DR   EMBL; AK147457; BAE27924.1; -; mRNA.
DR   EMBL; BC055016; AAH55016.1; -; mRNA.
DR   EMBL; BC150942; AAI50943.1; -; mRNA.
DR   EMBL; AB093263; BAC41447.2; -; Unassigned_RNA.
DR   IPI; IPI00380426; -.
DR   IPI; IPI00474096; -.
DR   IPI; IPI00830557; -.
DR   IPI; IPI00830839; -.
DR   RefSeq; NP_084196.4; NM_029920.7.
DR   UniGene; Mm.244177; -.
DR   ProteinModelPortal; Q3UHD3; -.
DR   PhosphoSite; Q3UHD3; -.
DR   PRIDE; Q3UHD3; -.
DR   Ensembl; ENSMUST00000085554; ENSMUSP00000082690; ENSMUSG00000029651.
DR   Ensembl; ENSMUST00000085558; ENSMUSP00000082694; ENSMUSG00000029651.
DR   Ensembl; ENSMUST00000110515; ENSMUSP00000106144; ENSMUSG00000029651.
DR   Ensembl; ENSMUST00000110518; ENSMUSP00000106147; ENSMUSG00000029651.
DR   GeneID; 77521; -.
DR   KEGG; mmu:77521; -.
DR   UCSC; uc009aon.1; mouse.
DR   CTD; 77521; -.
DR   MGI; MGI:1915388; Mtus2.
DR   eggNOG; roNOG12859; -.
DR   GeneTree; ENSGT00390000006245; -.
DR   HOGENOM; HBG402886; -.
DR   InParanoid; Q3UHD3; -.
DR   OMA; RSTFGNE; -.
DR   OrthoDB; EOG4S1T7T; -.
DR   NextBio; 347048; -.
DR   ArrayExpress; Q3UHD3; -.
DR   Bgee; Q3UHD3; -.
DR   CleanEx; MM_C130038G02RIK; -.
DR   Genevestigator; Q3UHD3; -.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Microtubule.
FT   CHAIN         1   1353       Microtubule-associated tumor suppressor
FT                                candidate 2 homolog.
FT                                /FTId=PRO_0000280112.
FT   REGION      626    964       Mediates interaction with MAPRE1 (By
FT                                similarity).
FT   REGION      786   1134       Localization to the growing distal tip of
FT                                microtubules (By similarity).
FT   REGION      786    874       Sufficient for interaction with KIF2C (By
FT                                similarity).
FT   COILED      976   1319       Potential.
FT   VAR_SEQ       1   1201       Missing (in isoform 4).
FT                                /FTId=VSP_023544.
FT   VAR_SEQ       1   1005       Missing (in isoform 3).
FT                                /FTId=VSP_023545.
FT   VAR_SEQ    1006   1023       AIQGFDALAVSTKHFFGK -> MGHHCCKPYICLQCLDKT
FT                                (in isoform 3).
FT                                /FTId=VSP_023546.
FT   VAR_SEQ    1118   1154       Missing (in isoform 2).
FT                                /FTId=VSP_023547.
FT   VAR_SEQ    1202   1210       RKTTEEQLE -> MSLRTWARH (in isoform 4).
FT                                /FTId=VSP_023548.
SQ   SEQUENCE   1353 AA;  147356 MW;  BFBFF33BA1A91B43 CRC64;
     MSVPLAPKKS CFGQLRDHRE GAKNNNESIL RTGDTNANQI MLEVSSSCDE AKSRDLDDEL
     GNSNLSRPQY HSHFQKEPLH LQGFGKGSQA GSTSQRESQA SLTVHRQLSE EHAVKRGALQ
     APQCVQGPSL SSWRNAVGQA SPEASAKKDA EIPRHIPKDK LAKTLDNEEL KRASSCSAAA
     GSVPPTDLQP VQLDTLGPQD HVPARGEGPQ RTPASHSPGK GFSPGEGTSE GNSVYLPKPS
     TSEAKGSSPS DTKMEGPHGL DVYNERITHA ELTPSSASAS KENPGLRHPE VCLGQGTGKS
     KVELKSVQPR NEEGLTSAQA QGPGCHEERS MSPVERQELL EKAYREATSQ GNSSHRQLGV
     RRGSSLEEMT GVSAGVEGSQ QATPTLSAAP AGEAGTRLTG KMSAGVGRMA RETASGQTAP
     DVGQAAPVRR DPTESVPSEV SGEERRLGSG NSGSTKLLAS GPSAGGSRTD TSGLLSPRGS
     NLEARKGKEM VAENRNLLEN AAQTDNTPAG VDSAFSTPAP LLHPETTVNS SHHPTPPGSS
     SQELGVFSGD TGSPSVASPP TDGGQVLNTS PKVPDRTTCS SGIPKPPTHP KDTPSSQEAR
     EKLETEKMEE RAEAKPILMP KPKHVRPKII TYIRRNPQAL SQGDASLVPV GLPYAPPTCG
     MPLPQEEKAA SRDLQPSANM YEKLKPDLQK PRVFPSGLMV SGIKPPAHHF SQMSEKFLQE
     VADHPGKEEF CSPPYTHYEV PPTFYRSAML LKPQLGLGAM SRLPSTKSRI LIASQRSSAS
     AIHPPGSLTT AASFYGSDPS DLKKASNSNA AKASLPKSGL RPPGYSRLPA AKLAAFGFVR
     SSSISAVPSS QSLDSVQPEQ SRPVTRSTFG NEEQAPLKQA LPSKDTPKGA GRAAPASSSN
     ATTPRRSLLP APKSTSTPAG AKKELQKDPE AKKPAVSSPK RTASAATKPH SPGYPKQRTS
     APRNEFPPKP DLQAREAERQ LAQRLRDRCE WQARQLGLAR RELKKAIQGF DALAVSTKHF
     FGKSERALAK EKELSIELAN IRDEVAFNTA KCEKLQKEKE TLERRFEEEL RRLGWQQQAE
     VQELQERLQQ QFQAESARLQ AEHQDQLLRM RCQHQEQVED ITASHEAALL EMENNHTVAI
     TILQDDHDHK VQELMSTHEF EKKELEENFE KLRLTLQDQV DTLTFQSQSL RDRARRFEEA
     LRKTTEEQLE IALAPYQHLE EDMQSLKQVL EMKNQQIHLQ EKKIIELEKL VEKNIILEER
     IQVLQQQNED LKARIDQNTV VTRQLSEENA NLQEYVEKET QEKKRLSRTN EELLWKLQTG
     DPTSPIKLSP TSPVYRGSSS GPSSPARVST TPR
//
ID   SNX27_MOUSE             Reviewed;         539 AA.
AC   Q3UHD6; Q7TQL6; Q80TZ1; Q9CYB5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Sorting nexin-27;
GN   Name=Snx27; Synonyms=Kiaa0488;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-526 (ISOFORM 2).
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-526 (ISOFORM 1).
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=17351151; DOI=10.1074/mcp.M700047-MCP200;
RA   Rincon E., Santos T., Avila-Flores A., Albar J.P., Lalioti V., Lei C.,
RA   Hong W., Merida I.;
RT   "Proteomics identification of sorting nexin 27 as a diacylglycerol
RT   kinase zeta-associated protein: new diacylglycerol kinase roles in
RT   endocytic recycling.";
RL   Mol. Cell. Proteomics 6:1073-1087(2007).
RN   [5]
RP   INTERACTION WITH HT4R.
RX   PubMed=15466885; DOI=10.1242/jcs.01379;
RA   Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W.,
RA   Marin P., Dumuis A., Bockaert J.;
RT   "New sorting nexin (SNX27) and NHERF specifically interact with the 5-
RT   HT4a receptor splice variant: roles in receptor targeting.";
RL   J. Cell Sci. 117:5367-5379(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Involved in endocytic trafficking (By similarity). In T
CC       lymphocytes, participates in endocytic recycling pathway. Recruits
CC       PSCDBP and HT4R to early endosomes (By similarity).
CC   -!- SUBUNIT: Interacts with PSCDBP. Isoforms 1 and 2 directly interact
CC       with DGKZ (By similarity). Isoforms 1 and 2 interact with HT4R
CC       isoform 5-HTA(A). Interacts with MCC (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Early endosome. Note=In
CC       T lymphocytes, recruited from the cytosol to sorting endosomes by
CC       phosphoinositide-3-kinase products (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=SNX27a;
CC         IsoId=Q3UHD6-1; Sequence=Displayed;
CC       Name=2; Synonyms=SNX27b;
CC         IsoId=Q3UHD6-2; Sequence=VSP_030540;
CC   -!- TISSUE SPECIFICITY: Expressed in cells of hematopoietic origin.
CC   -!- DOMAIN: The PDZ domain mediates the interaction with DGKZ, PSCDBP
CC       and HT4R and is responsible for vesicular localization (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 PX (phox homology) domain.
CC   -!- SIMILARITY: Contains 1 Ras-associating domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB30966.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAB30966.1; Type=Erroneous termination; Positions=258; Note=Translated as Glu;
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DR   EMBL; AK017836; BAB30966.1; ALT_SEQ; mRNA.
DR   EMBL; AK147452; BAE27921.1; -; mRNA.
DR   EMBL; AK122296; BAC65578.1; -; mRNA.
DR   EMBL; BC053495; AAH53495.1; -; mRNA.
DR   IPI; IPI00111320; -.
DR   IPI; IPI00756736; -.
DR   RefSeq; NP_001075953.1; NM_001082484.1.
DR   RefSeq; NP_083997.1; NM_029721.1.
DR   UniGene; Mm.28160; -.
DR   HSSP; Q64512; 1VJ6.
DR   ProteinModelPortal; Q3UHD6; -.
DR   SMR; Q3UHD6; 39-133, 159-267.
DR   STRING; Q3UHD6; -.
DR   PhosphoSite; Q3UHD6; -.
DR   PRIDE; Q3UHD6; -.
DR   Ensembl; ENSMUST00000029783; ENSMUSP00000029783; ENSMUSG00000028136.
DR   Ensembl; ENSMUST00000107283; ENSMUSP00000102904; ENSMUSG00000028136.
DR   GeneID; 76742; -.
DR   KEGG; mmu:76742; -.
DR   CTD; 76742; -.
DR   MGI; MGI:1923992; Snx27.
DR   GeneTree; ENSGT00530000063147; -.
DR   HOGENOM; HBG377841; -.
DR   HOVERGEN; HBG059206; -.
DR   InParanoid; Q3UHD6; -.
DR   OMA; ILEVNHV; -.
DR   OrthoDB; EOG4NCMCG; -.
DR   NextBio; 345727; -.
DR   ArrayExpress; Q3UHD6; -.
DR   Bgee; Q3UHD6; -.
DR   CleanEx; MM_SNX27; -.
DR   Genevestigator; Q3UHD6; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR001683; Phox.
DR   InterPro; IPR000159; Ras-assoc.
DR   Gene3D; G3DSA:3.30.1520.10; PX; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF00788; RA; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF64268; PX; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50195; PX; 1.
DR   PROSITE; PS50200; RA; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Endosome; Phosphoprotein;
KW   Protein transport; Transport.
FT   CHAIN         1    539       Sorting nexin-27.
FT                                /FTId=PRO_0000315357.
FT   DOMAIN       41    134       PDZ.
FT   DOMAIN      159    267       PX.
FT   DOMAIN      271    360       Ras-associating.
FT   MOD_RES      49     49       Phosphoserine.
FT   VAR_SEQ     525    539       NIFQMARSQQRDVAT -> EY (in isoform 2).
FT                                /FTId=VSP_030540.
SQ   SEQUENCE   539 AA;  60989 MW;  0EF5B84253A90B4D CRC64;
     MADEDGEGIH PSAPHRNGGG GGGSGLHCAG NGGGGGGGPR VVRIVKSESG YGFNVRGQVS
     EGGQLRSING ELYAPLQHVS AVLPGGAADR AGVRKGDRIL EVNGVNVEGA THKQVVDLIR
     AGEKELILTV LSVPPHEADN LDPSDDSLGQ SFYDYTEKQA VPISVPTYKH VEQNGEKFVV
     YNVYMAGRQL CSKRYREFAI LHQNLKREFA NFTFPRLPGK WPFSLSEQQL DARRRGLEEY
     LEKVCSIRVI GESDIMQEFL SESDENYNGV SDVELRVALP DGTTVTVRVK KNSTTDQVYQ
     AIAAKVGMDS TTVNYFALFE VINHSFVRKL APNEFPHKLY VQNYTSAVPG TCLTIRKWLF
     TTEEEVLLND NDLAVTYFFH QAVDDVKKGY IKAEEKSYQL QKLHEQRKMV MYLNMLRTCE
     GYNEIIFPHC ACDSRRKGHV ITAISITHFK LHACTEEGQL ENQVIAFEWD EMQRWDTDEE
     GMAFCFEYAR GEKKPRWVKI FTPYFNYMHE CFERVFCELK WRKENIFQMA RSQQRDVAT
//
ID   Q3UHD8_MOUSE            Unreviewed;       982 AA.
AC   Q3UHD8;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Dlgap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK147448; BAE27919.1; -; mRNA.
DR   IPI; IPI00649710; -.
DR   UniGene; Mm.311840; -.
DR   UniGene; Mm.367369; -.
DR   STRING; Q3UHD8; -.
DR   PRIDE; Q3UHD8; -.
DR   Ensembl; ENSMUST00000060072; ENSMUSP00000052858; ENSMUSG00000003279.
DR   Ensembl; ENSMUST00000133983; ENSMUSP00000116716; ENSMUSG00000003279.
DR   MGI; MGI:1346065; Dlgap1.
DR   GeneTree; ENSGT00550000074473; -.
DR   HOVERGEN; HBG018957; -.
DR   PhylomeDB; Q3UHD8; -.
DR   ArrayExpress; Q3UHD8; -.
DR   Bgee; Q3UHD8; -.
DR   Genevestigator; Q3UHD8; -.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0007268; P:synaptic transmission; TAS:MGI.
DR   InterPro; IPR005026; GKAP.
DR   Pfam; PF03359; GKAP; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   982 AA;  109390 MW;  9518AAB72BB13EE9 CRC64;
     MKGLSGSRSH HHGITCEAAC DSLSHHSDHK PYLLSPVDHH PADHPYYTQR NSFQAECVGP
     FSDPLASSTF PRRHYTSQQE LKDESALVPR TLATKANRLP TNLLDQFERQ LPLSRDGYHT
     LQYKRTAVEH RSDSPGRIRH LVHSVQKLFT KSHSLEGPSK GSVNGGKASP DESQTLRYGK
     RSKSKERRSE SKARSNASNA SPTSPSWWSS DDNLDGDMCL YHTPSGVMTM GRCPDRSASQ
     YFMEAYNTIS EQAVKASRSN NDIKCSTCAN LPVTLDAPLL KKSAWSSTLT VSRAREVYQK
     ASVNMDQAMV KSEACQQERS CQYLQVPQDE WSGYTPRGKD DEIPCRRMRS GSYIKAMGDE
     DSGDSDTSPK PSPKVAARRE SYLKATQPSL TELTTLKISN EHSPKLQIRS HSYLRAVSEV
     SINRSLDSLD PAGLLTSPKF RSRNESYMRA MSTISQVSEM EVNGQFESVC ESVFSELESQ
     AVEALDLPLP GCFRMRSHSY VRAIEKGCSQ DDECVSLRSS SPPRTTTTVR TIQSSTVSSC
     ITTYKKTPPP VPPRTTTKPF ISITAQSSTE SAQDAYMDGQ GQRGDMISQS GLSNSTESLD
     SMKALTAAIE AANAQIHGPA SQHMGSNAAA VTTTTTIATV TTEDRKKDFK KNRCLSIGIQ
     VDDAEEPEKM AESKTSNKFQ SVGVQVEEEK CFRRFTRSNS VTTAVQADLD FHDNLENSLE
     SIEDNSCPGP MARQFSRDAS TSTVSIQGSG NHYHACAADD DFDTDFDPSI LPPPDPWIDS
     ITEDPLEAVQ RSVCHRDGHW FLKLLQAERD RMEGWCKLME REERENNLPE DILGKIRTAV
     GSAQLLMAQK FYQFRELCEE NLNPNAHPRP TSQDLAGFWD MLQLSIENIS MKFDELHQLK
     ANNWKQMDPL DKKERRAPPP VPKKPAKGPA PLIRERSLES SQRQEARKRL MAAKRAASVR
     QNSATESAES IEIYIPEAQT RL
//
ID   AGAP2_MOUSE             Reviewed;        1186 AA.
AC   Q3UHD9; Q5DU45;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2;
DE            Short=AGAP-2;
DE   AltName: Full=Centaurin-gamma-1;
DE            Short=Cnt-g1;
DE   AltName: Full=Phosphatidylinositol-3-kinase enhancer;
DE            Short=PIKE;
GN   Name=Agap2; Synonyms=Centg1, Kiaa0167;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 138-1186 (ISOFORM 2).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149 AND SER-262, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-632; SER-802; SER-859
RP   AND SER-921, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: GTPase-activating protein (GAP) for ARF1 and ARF5, which
CC       also shows strong GTPase activity. Participates in the prevention
CC       of neuronal apoptosis by enhancing PI3 kinase activity. Aids the
CC       coupling of metabotropic glutamate receptor 1 (GRM1) to
CC       cytoplasmic PI3 kinase by interacting with Homer scaffolding
CC       proteins, and also seems to mediate anti-apoptotic effects of NGF
CC       by activating nuclear PI3 kinase (By similarity).
CC   -!- ENZYME REGULATION: GAP activity is stimulated by
CC       phosphatidylinositol 4,5-bisphosphate (PIP2) and, to a lesser
CC       extent, by phosphatidylinositol 3,4,5-trisphosphate (PIP3).
CC       Phosphatidic acid potentiates PIP2 stimulation (By similarity).
CC   -!- SUBUNIT: Interacts with EPB41L1, PLCG1, NF2, HOMER1 and HOMER2 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UHD9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UHD9-2; Sequence=VSP_018542;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: G domain binds GTP and has GTPase activity.
CC   -!- DOMAIN: Arf-GAP domain interacts with G domain and may regulate
CC       its GTPase activity.
CC   -!- DOMAIN: PH domain binds phospholipids and is required for nuclear
CC       targeting.
CC   -!- SIMILARITY: Belongs to the centaurin gamma-like family.
CC   -!- SIMILARITY: Contains 2 ANK repeats.
CC   -!- SIMILARITY: Contains 1 Arf-GAP domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK147446; BAE27918.1; -; mRNA.
DR   EMBL; AK220325; BAD90236.1; -; mRNA.
DR   IPI; IPI00349020; -.
DR   IPI; IPI00754509; -.
DR   RefSeq; NP_001028435.1; NM_001033263.4.
DR   UniGene; Mm.336761; -.
DR   ProteinModelPortal; Q3UHD9; -.
DR   SMR; Q3UHD9; 396-570, 668-908, 925-1144.
DR   STRING; Q3UHD9; -.
DR   PhosphoSite; Q3UHD9; -.
DR   PRIDE; Q3UHD9; -.
DR   Ensembl; ENSMUST00000039259; ENSMUSP00000043466; ENSMUSG00000025422.
DR   Ensembl; ENSMUST00000105254; ENSMUSP00000100889; ENSMUSG00000025422.
DR   GeneID; 216439; -.
DR   KEGG; mmu:216439; -.
DR   UCSC; uc007hhx.1; mouse.
DR   UCSC; uc007hhy.1; mouse.
DR   CTD; 216439; -.
DR   MGI; MGI:3580016; Agap2.
DR   eggNOG; roNOG08988; -.
DR   GeneTree; ENSGT00600000084361; -.
DR   HOGENOM; HBG505242; -.
DR   HOVERGEN; HBG054045; -.
DR   InParanoid; Q3UHD9; -.
DR   OMA; PKAVINS; -.
DR   OrthoDB; EOG45QHCN; -.
DR   NextBio; 375150; -.
DR   ArrayExpress; Q3UHD9; -.
DR   Bgee; Q3UHD9; -.
DR   Genevestigator; Q3UHD9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0060749; P:mammary gland alveolus development; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptosis; IMP:MGI.
DR   GO; GO:0046427; P:positive regulation of JAK-STAT cascade; IMP:MGI.
DR   GO; GO:0033601; P:positive regulation of mammary gland epithelial cell proliferation; IGI:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:MGI.
DR   GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR001164; ArfGAP.
DR   InterPro; IPR013684; MIRO-like.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR020851; Small_GTPase.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF08477; Miro; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF57863; ArfGAP; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ANK repeat; Cytoplasm; GTP-binding;
KW   GTPase activation; Metal-binding; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Repeat; Zinc; Zinc-finger.
FT   CHAIN         1   1186       Arf-GAP with GTPase, ANK repeat and PH
FT                                domain-containing protein 2.
FT                                /FTId=PRO_0000235913.
FT   DOMAIN      670    904       PH.
FT   DOMAIN      925   1045       Arf-GAP.
FT   REPEAT     1084   1113       ANK 1.
FT   REPEAT     1117   1146       ANK 2.
FT   NP_BIND     407    414       GTP (Potential).
FT   NP_BIND     451    455       GTP (Potential).
FT   NP_BIND     509    512       GTP (Potential).
FT   ZN_FING     940    963       C4-type.
FT   REGION        1     23       Interaction with EPB41L1 (By similarity).
FT   REGION      180    225       Interactions with HOMER1 and NF2 (By
FT                                similarity).
FT   REGION      262    384       Interaction with PLCG1 (By similarity).
FT   REGION      399    566       G domain.
FT   MOD_RES     149    149       Phosphoserine.
FT   MOD_RES     262    262       Phosphoserine.
FT   MOD_RES     629    629       Phosphothreonine (By similarity).
FT   MOD_RES     632    632       Phosphoserine.
FT   MOD_RES     802    802       Phosphoserine.
FT   MOD_RES     859    859       Phosphoserine.
FT   MOD_RES     921    921       Phosphoserine.
FT   VAR_SEQ     847    866       Missing (in isoform 2).
FT                                /FTId=VSP_018542.
FT   CONFLICT    381    381       T -> A (in Ref. 2; BAD90236).
SQ   SEQUENCE   1186 AA;  124511 MW;  E9B4F3EDB66CBEC8 CRC64;
     MSRGAGALQR RTTTYLISLT LVKLESVPPP PPSPSAAAAG APGARGSEPR DPGSPRGSEE
     PGKKRHERLF HRQDALWIST SSAGTGGAEP PALSPAPASP ARPVSPAPGR RLSLWAAPPG
     PPLSGGLSPD SKPGGAPSSS RRPLLSSPSW GGPEPEGRTG GGVPGSSSPH PGTGSRRLKV
     APPPPAPKPF KTVTTSGAKA GGGKGAGSRL SWPESEGKPR VKGSKSTAGT GASAAAAGGG
     GSAAVTTSGG VGAGAGTRGK LSPRKGKSKT LDNSDLHPGP SAGSPPLTVP AIPVPATSVT
     ATSTQPLGPA PPITLEPPAP GLKRGREGGR ASTRDRKMLK FISGIFTKST GGPPGPGPLP
     GPQGLSSSSG SRELLGAELR TSPKAVVNSQ EWTLSRSIPE LRLGVLGDVR SGKSSLIHRF
     LTGSYQVLEK IESEQYKKEM LVDGQTHLVL IREEAGAPDA KFSGWADAVI FVFSLEDESS
     FQAVSRLHGQ LSSLRGEGRG GLALALVGTQ DRISASSPRV VGDARARALC TDMKRCSYYE
     TCATYGLNVD RVFQEVAQKV VTLRKQQQLL AACKSLPSSP SHSAASTPVA GQASNGGHTS
     DYSSSLPSSP NVGHRELRAE AAAVAGLSTP GSLHRAAKRR TSLFANRRGS DAEKRSLDSR
     GETTGSGRAI PIKQSFLLKR SGNSLNKEWK KKYVTLSSNG FLLYHPSIND YIHSTHGKEM
     DLLRTTVKVP GKRPPRAISA FGPSASINGL VKDMSTVQMG EGPEASTPMP SPSPSPSSLQ
     LPTDQTSKHL LKPDRNLARA LSTDCTPSGD LSPLSREPPP SPMVKKQRRK KLSTPSKTEG
     SAVQAEAKRK MWKLKSFGSL RNIYKAEENF EFLIVSSTGQ TWHFEAASFE ERDAWVQAIE
     SQILASLQCC ESSKVKLRTD SQSEAVAIQA IRNAKGNSTC VDCGAPNPTW ASLNLGALIC
     IECSGIHRNL GTHLSRVRSL DLDDWPRELT LVLTAIGNDT ANRVWESDTR GRAKPTRDSS
     REERESWIRA KYEQLLFLAP LGTTEEPLGR QLWAAVEAQD VAAVLLLLAH ARHGPLDTSV
     EDPQLRSPLH LAAELAHVVI TQLLLWYGAD VAARDAQGRT ALFYARQAGS QLCADILLQH
     GCPGEGGSTA TTPSAATTPS ITATPSPRRR SSAASLGRVD TTIALV
//
ID   PITM3_MOUSE             Reviewed;         974 AA.
AC   Q3UHE1; A6QRE8; Q3UH22; Q5RIT9;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Membrane-associated phosphatidylinositol transfer protein 3;
DE   AltName: Full=Phosphatidylinositol transfer protein, membrane-associated 3;
DE            Short=PITPnm 3;
DE   AltName: Full=Pyk2 N-terminal domain-interacting receptor 1;
DE            Short=NIR-1;
GN   Name=Pitpnm3; Synonyms=Nir1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Catalyzes the transfer of phosphatidylinositol and
CC       phosphatidylcholine between membranes (in vitro). Binds calcium
CC       ions (By similarity).
CC   -!- SUBUNIT: Interacts with PTK2B via its C-terminus (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane
CC       protein (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UHE1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UHE1-2; Sequence=VSP_017966;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI
CC       transfer class IIA subfamily.
CC   -!- SIMILARITY: Contains 1 DDHD domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK147444; BAE27916.1; -; mRNA.
DR   EMBL; AK147630; BAE28035.1; -; mRNA.
DR   EMBL; BX119911; CAI24476.1; -; Genomic_DNA.
DR   EMBL; BX119911; CAO78012.1; -; Genomic_DNA.
DR   IPI; IPI00604878; -.
DR   IPI; IPI00751770; -.
DR   RefSeq; NP_001020098.1; NM_001024927.2.
DR   RefSeq; NP_001075110.1; NM_001081641.1.
DR   UniGene; Mm.351793; -.
DR   ProteinModelPortal; Q3UHE1; -.
DR   SMR; Q3UHE1; 758-854.
DR   PhosphoSite; Q3UHE1; -.
DR   PRIDE; Q3UHE1; -.
DR   Ensembl; ENSMUST00000075258; ENSMUSP00000074737; ENSMUSG00000040543.
DR   Ensembl; ENSMUST00000108508; ENSMUSP00000104148; ENSMUSG00000040543.
DR   GeneID; 327958; -.
DR   KEGG; mmu:327958; -.
DR   NMPDR; fig|10090.3.peg.24614; -.
DR   UCSC; uc007jya.1; mouse.
DR   UCSC; uc007jyb.1; mouse.
DR   CTD; 327958; -.
DR   MGI; MGI:2685726; Pitpnm3.
DR   GeneTree; ENSGT00550000074351; -.
DR   HOGENOM; HBG444305; -.
DR   HOVERGEN; HBG052733; -.
DR   InParanoid; Q3UHE1; -.
DR   OMA; CAMSYLT; -.
DR   OrthoDB; EOG49P9XQ; -.
DR   PhylomeDB; Q3UHE1; -.
DR   NextBio; 398035; -.
DR   ArrayExpress; Q3UHE1; -.
DR   Bgee; Q3UHE1; -.
DR   CleanEx; MM_PITPNM3; -.
DR   Genevestigator; Q3UHE1; -.
DR   GermOnline; ENSMUSG00000040543; Mus musculus.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004177; DDHD.
DR   InterPro; IPR023214; HAD-like_dom.
DR   InterPro; IPR013209; LNS2.
DR   Gene3D; G3DSA:3.40.50.1000; HAD-like_dom; 1.
DR   Pfam; PF02862; DDHD; 1.
DR   Pfam; PF08235; LNS2; 1.
DR   SMART; SM00775; LNS2; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   PROSITE; PS51043; DDHD; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Lipid-binding; Membrane; Metal-binding;
KW   Phosphoprotein.
FT   CHAIN         1    974       Membrane-associated phosphatidylinositol
FT                                transfer protein 3.
FT                                /FTId=PRO_0000232744.
FT   DOMAIN      390    594       DDHD.
FT   COMPBIAS    279    327       Ser-rich.
FT   MOD_RES      30     30       Phosphoserine (By similarity).
FT   MOD_RES      31     31       Phosphoserine (By similarity).
FT   MOD_RES     413    413       Phosphothreonine (By similarity).
FT   MOD_RES     495    495       Phosphoserine.
FT   MOD_RES     907    907       Phosphoserine (By similarity).
FT   MOD_RES     928    928       Phosphoserine (By similarity).
FT   VAR_SEQ      77     92       Missing (in isoform 2).
FT                                /FTId=VSP_017966.
FT   CONFLICT    849    849       S -> N (in Ref. 1; BAE27916).
SQ   SEQUENCE   974 AA;  106462 MW;  285A581AFDE92626 CRC64;
     MAKAGSAGGP SPGGGAPWHL RNVLSDSVES SDDEFFDARE EVAEGKNAIL IGMSQWSSND
     LVEQIETIGK LDERQGDGAT ACTSSILQEK QRELYRVSLR RQRFPAQGSI EIHEDGEEGC
     SQRSCKTHVL LLVLHGGNVL DTGSGDPSCK AADIHTFSSV LEKVMRAHFP AALGHILIKF
     VPCPAICSEA FSLVSNLNPY SHDEGCLGTS QDHVPLAALP LLAISSPQYQ DAVATVIERA
     NHIYGEFLKS SDGIGFNGQV CLIGDCVGGL LAFDAICYSA GPSGDSPGSS SRKGSISSTQ
     DTPVVVEEDC SLASSKRLSK SNVDVSSGVE DEDPKRPLPR KQSDSSTYDC EAITQHHAFL
     SSIHSSVLKD EAEAPAAGTP QLSEVSLGRF DFDVSDFFLF GSPLGLVLAM RRTVLPGIDG
     FQMRPACSQV YSFFHCADPS ASRLEPLLEP KFHLVPPVSV PRYQRFPLGD GQSLLLADAL
     HTHSPLFLEG SSRGSPPLLD APASPPQAPR FQRTERRLSK GSSHSDSSES SDSLAPMGAS
     RITAKWWGTK RIDYALYCPD VLTAFPTVAL PHLFHASYWE STDVVAFILR QVMRYESASV
     KESTGLDPTA LSPANPREKW LRKRTQVKLR NVTANHRAND VIAAEDGPQV LVGRFMYGPL
     DMVALTGEKV DILVMTEPSS GRWVHLDTEI TNNSGRITYN VPRPRRLGVG VYPVKMVVRG
     DQTCAMSYLT VLPRGMECVV FSIDGSFAAS VSIMGSDPKV RPGAVDVVRH WQDLGYMILY
     ITGRPDMQKQ RVVSWLSQHN FPQGMIFFSD GLVHDPLRQK AIFLRNLMQE CFIKITAAYG
     STKDISVYSV LGLPASQIFI VGRSTKKYQT QCQFLSEGYA AHLAALEASH RSRPKKNNSR
     MILRKGSFGL HAQPEFLRKR NHLRRTMSVQ QPDPPAANPK PERAQSQPES DKDHERPLPA
     LSWARGPPKF ESVP
//
ID   Q3UHE7_MOUSE            Unreviewed;      1628 AA.
AC   Q3UHE7;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Kif21a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the kinesin-like protein family.
CC   -!- SIMILARITY: Contains 1 kinesin-motor domain.
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DR   EMBL; AK147436; BAE27910.1; -; mRNA.
DR   IPI; IPI00869453; -.
DR   RefSeq; NP_001102511.1; NM_001109041.1.
DR   UniGene; Mm.41379; -.
DR   UniGene; Mm.481341; -.
DR   ProteinModelPortal; Q3UHE7; -.
DR   SMR; Q3UHE7; 9-379.
DR   STRING; Q3UHE7; -.
DR   GeneID; 16564; -.
DR   KEGG; mmu:16564; -.
DR   UCSC; uc007xhu.1; mouse.
DR   CTD; 16564; -.
DR   MGI; MGI:109188; Kif21a.
DR   HOVERGEN; HBG052247; -.
DR   NextBio; 290065; -.
DR   Genevestigator; Q3UHE7; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR009053; Prefoldin.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:3.40.850.10; kinesin_motor; 1.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF00400; WD40; 6.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF46579; Prefoldin; 1.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_DOMAIN1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_DOMAIN2; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Microtubule; Motor protein; Nucleotide-binding; Repeat;
KW   WD repeat.
SQ   SEQUENCE   1628 AA;  181402 MW;  22A13292E64B1070 CRC64;
     MLGAADESSV RVAVRIRPQL AKEKIEGCHI CTSVTPGEPQ VFLGKDKAFT FDYVFDIDSQ
     QEQIYTQCIE KLIEGCFEGY NATVFAYGQT GAGETYTMGT GFDVNIMEEE QGIISRAVRH
     LFKSIDEKKT SAIKNGLPPP EFKVNAQFLE LYNEEVLDLF DTTRDIDAKN KKSNIRIHED
     STGGIYTVGV TTRTVNTEPE MMQCLKLGAL SRTTASTQMN VQSSRSHAIF TIHVCQTRVC
     PQTDAENATD NKLISESSPM NEFETLTAKF HFVDLAGSER LKRTGATGER AKEGISINCG
     LLALGNVISA LGDKSKRATH VPYRDSKLTR LLQDSLGGNS QTIMIACVSP SDRDFMETLN
     TLKYANRARN IKNKVMVNQD RASQQINALR SEITRLQMEL MEYKTGKRII DEEGVESIND
     MFHENAMLQT ENNNLRVRIK AMQETVDALR ARITQLVSEQ ANQVLARAGE GNEEISNMIH
     SYIKEIEDLR AKLLESEAVN ENLRKNLTRA TARSPYFSAS SAFSPTILSS DKETIEIIDL
     AKKDLEKLKR KEKKKKKSVA GKDDNADTDQ EKKEEKGVSE KENNELDVEE NQEVSDHEDE
     EEEEEDEEEE DDIEGEESSD ESDSESDEKA NYQADLANIT CEIAIKQKLI DELENSQKRL
     QTLKKQYEEK LMMLQHKIRD TQLERDQVLQ NLGSVESYSE EKAKKVKCEY EKKLHAMNKE
     LQRLQTAQKE HARLLKNQSQ YEKQLKKLQQ DVMEMKKTKV RLMKQMKEEQ EKARLTESRR
     NREIAQLKKD QRKRDHQLRL LEAQKRNQEV VLRRKTEEVT ALRRQVRPMS DKVAGKVTRK
     LSSSESPAPD TGSSAASGEA DTSRPGTQQK MRIPVARVQA LPTPTTNGTR KKYQRKGFTG
     RVFTSKTARM KWQLLERRVT DIIMQKMTIS NMEADMNRLL RQREELTKRR EKLSKRREKI
     VKESGEGDKS VANIIEEMES LTANIDYIND SIADCQANIM QMEEAKEEGE TLDVTAVINA
     CTLTEARYLL DHFLSMGINK GLQAAQKEAQ IKVLEGRLKQ TEITSATQNQ LLFHMLKEKA
     ELNPELDALL GHALQDLDGA PPENEEDSSE EDGPLHSPGS EGSTLSSDLM KLCGEVKPKN
     KARRRTTTQM ELLYADSSEV ASDTSAGDAS LSGPLAPVAE GQEIGMNTET SGTSTRDKEL
     LAPSGLPSKI GSISDSGASE TSLSPPSSPP SRPRNELNVF NRLTVPQGTP SVQQDKSDES
     DSSLSEVHSR STRRGIINPF PACKGVRASP LQCVHIAEGH TKAVLCVDST DDLLFTGSKD
     RTCKVWNLVT GQEIMSLGVH PNNVVSVKYC NYTSLVFTVS TSYIKVWDIR ESAKCIRTLT
     SSGQVTLGEA CSASTSRTVA IPSGESQINQ IALNPTGTFL YAASGNAVRM WDLKRFQSTG
     KLTGHLGPVM CLTVDQISNG QDLIITGSKD HYIKMFDVTE GALGTVSPTH NFEPPHYDGI
     EALAIQGDNL FSGSRDNGIK KWDLAQKGLL QQVPNAHKDW VCALGLVPGH PVLLSGCRGG
     ILKLWNVDTF VPVGEMRGHD SPINAICVNS THVFTAADDR TVRIWKAHNL QDGQLSDTGD
     LGEDIASN
//
ID   ZEP2_MOUSE              Reviewed;        2430 AA.
AC   Q3UHF7; O55140; Q3UVD4; Q3UVH5;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Transcription factor HIVEP2;
DE   AltName: Full=Human immunodeficiency virus type I enhancer-binding protein 2 homolog;
DE   AltName: Full=Myc intron-binding protein 1;
DE            Short=MIBP-1;
GN   Name=Hivep2; Synonyms=Mibp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH TCF4, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Brain;
RX   MEDLINE=99223602; PubMed=10207097;
RA   Doerflinger U., Pscherer A., Moser M., Ruemmele P., Schuele R.,
RA   Buettner R.;
RT   "Specific activation of SSTR-2 promoter by SEF-2 and MIBP-1.";
RL   Mol. Cell. Biol. 19:3736-3747(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and C57BL/6J;
RC   TISSUE=Brain, Cerebellum, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Specifically binds to the DNA sequence 5'-GGGACTTTCC-3'
CC       which is found in the enhancer elements of numerous viral
CC       promoters such as those of SV40, CMV, or HIV1. In addition,
CC       related sequences are found in the enhancer elements of a number
CC       of cellular promoters, including those of the class I MHC,
CC       interleukin-2 receptor, somatostatin receptor II, and interferon-
CC       beta genes. It may act in T-cell activation (By similarity).
CC   -!- SUBUNIT: Interacts with TCF4.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed in heart, lung, skeletal muscle and
CC       liver. In the brain expressed in cerebral cortex, hippocampus,
CC       corpora amygdala and cerebellar cortex.
CC   -!- DEVELOPMENTAL STAGE: At E13.5 and E15.5 expressed in anterior
CC       neural tube over primordial frontal cortex, spinal cord, dorsal
CC       root glanglia and developing skeletal muscle.
CC   -!- SIMILARITY: Contains 4 C2H2-type zinc fingers.
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DR   EMBL; Y15907; CAA75868.1; -; mRNA.
DR   EMBL; AK137291; BAE23294.1; -; mRNA.
DR   EMBL; AK137384; BAE23336.1; -; mRNA.
DR   EMBL; AK147244; BAE27792.1; -; mRNA.
DR   EMBL; AK147419; BAE27900.1; -; mRNA.
DR   IPI; IPI00115900; -.
DR   RefSeq; NP_034567.2; NM_010437.2.
DR   UniGene; Mm.42157; -.
DR   ProteinModelPortal; Q3UHF7; -.
DR   SMR; Q3UHF7; 188-244, 1782-1838.
DR   STRING; Q3UHF7; -.
DR   PhosphoSite; Q3UHF7; -.
DR   PRIDE; Q3UHF7; -.
DR   Ensembl; ENSMUST00000015645; ENSMUSP00000015645; ENSMUSG00000015501.
DR   GeneID; 15273; -.
DR   KEGG; mmu:15273; -.
DR   NMPDR; fig|10090.3.peg.13386; -.
DR   UCSC; uc007elg.1; mouse.
DR   CTD; 15273; -.
DR   MGI; MGI:1338076; Hivep2.
DR   eggNOG; roNOG09168; -.
DR   GeneTree; ENSGT00530000063161; -.
DR   HOGENOM; HBG444719; -.
DR   HOVERGEN; HBG007119; -.
DR   InParanoid; Q3UHF7; -.
DR   OMA; RKKCFLV; -.
DR   OrthoDB; EOG4VT5W8; -.
DR   PhylomeDB; Q3UHF7; -.
DR   NextBio; 287901; -.
DR   ArrayExpress; Q3UHF7; -.
DR   Bgee; Q3UHF7; -.
DR   Genevestigator; Q3UHF7; -.
DR   GermOnline; ENSMUSG00000015501; Mus musculus.
DR   GO; GO:0005667; C:transcription factor complex; TAS:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; TAS:MGI.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   InterPro; IPR022755; Znf_C2H2_jaz.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 4.
DR   Pfam; PF12171; zf-C2H2_jaz; 1.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   1: Evidence at protein level;
KW   DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW   Repeat; Transcription; Transcription regulation; Ubl conjugation;
KW   Zinc; Zinc-finger.
FT   CHAIN         1   2430       Transcription factor HIVEP2.
FT                                /FTId=PRO_0000047372.
FT   REPEAT     2037   2040       1.
FT   REPEAT     2043   2046       2.
FT   REPEAT     2055   2058       3.
FT   REPEAT     2067   2070       4.
FT   REPEAT     2073   2076       5.
FT   REPEAT     2090   2093       6.
FT   REPEAT     2096   2099       7.
FT   REPEAT     2102   2105       8.
FT   REPEAT     2114   2117       9.
FT   REPEAT     2129   2132       10.
FT   ZN_FING     189    211       C2H2-type 1.
FT   ZN_FING     217    239       C2H2-type 2.
FT   ZN_FING    1783   1805       C2H2-type 3.
FT   ZN_FING    1811   1835       C2H2-type 4.
FT   REGION     2037   2132       10 X 4 AA tandem repeats of S-P-[RGMKC]-
FT                                [RK].
FT   MOTIF       929    935       Nuclear localization signal (Potential).
FT   COMPBIAS    942    974       Ser-rich.
FT   COMPBIAS   1499   1569       Ser-rich.
FT   COMPBIAS   1883   1907       Asp/Glu-rich (acidic).
FT   COMPBIAS   2057   2132       Arg-rich.
FT   MOD_RES    2055   2055       Phosphoserine (By similarity).
FT   MOD_RES    2061   2061       Phosphoserine (By similarity).
FT   CROSSLNK   2076   2076       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CONFLICT    572    572       G -> E (in Ref. 1; CAA75868).
FT   CONFLICT    661    661       S -> P (in Ref. 1; CAA75868).
FT   CONFLICT    749    749       D -> N (in Ref. 1; CAA75868).
FT   CONFLICT    762    762       S -> G (in Ref. 1; CAA75868).
FT   CONFLICT   1112   1112       S -> P (in Ref. 1; CAA75868).
FT   CONFLICT   1211   1211       P -> S (in Ref. 1; CAA75868).
FT   CONFLICT   1223   1223       A -> G (in Ref. 1; CAA75868).
FT   CONFLICT   1496   1496       C -> S (in Ref. 1; CAA75868).
FT   CONFLICT   2001   2001       D -> E (in Ref. 2; BAE23294).
FT   CONFLICT   2091   2091       P -> A (in Ref. 1; CAA75868).
FT   CONFLICT   2122   2122       M -> L (in Ref. 1; CAA75868).
FT   CONFLICT   2263   2263       S -> C (in Ref. 2; BAE23336).
FT   CONFLICT   2294   2294       T -> A (in Ref. 2; BAE23294).
FT   CONFLICT   2314   2314       T -> A (in Ref. 1; CAA75868).
SQ   SEQUENCE   2430 AA;  266705 MW;  265694210C8A7024 CRC64;
     MDTGDTALGQ KATSRSGETD SVSGRWRQEQ SAVLKMSTFS SQEGPRQPQI DPEQIGNAAS
     AQLFGSGKLA SPGEGLHQVT EKQYPPHRPS PYPCQHSLSF PQHSLSQGMT HSHKPHQSLE
     GPPWLFPGPL PSVASEDLFP FPMHGHSGGY PRKKISNLNP AYSQYSQKSI EQAEDAHKKE
     HKPKKPGKYI CPYCSRACAK PSVLKKHIRS HTGERPYPCI PCGFSFKTKS NLYKHRKSHA
     HAIKAGLVPF TESSVSKLDL EAGFIDVEAE IHSDGEQSTD TDEESSLFAE ASDKVSPGPP
     VPLDIASRGG YHGSLEESLG GPMKVPILII PKSGIPLASE GSQYLSSEML PNPSLNAKAD
     DSHTVKQKLA LRLSEKKGQD SEPSLNLLSP HSKGSTDSGY FSRSESAEQQ ISPPNTNAKS
     YEEIIFGKYC RLSPRNTLSV TPTGQERTAM GRRGIMEPLP HLNTRLEVKM FEDPISQLNP
     SKGEMDPGQI NMLKTTKFNS ECRQPQAIPS SVRNEGKPYP GNFLGSNPML LEAPVDSSPL
     IRSNSMPTSS ATNLSVPPSL RGSHSFDERM TGSDDVFYPG TVGIPPQRML RRQAAFELPS
     VQEGHMESEH PARVSKGLAS PSLKEKKLLP GDRPGYDYDV CRKPYKKWED SETLKQSYLG
     SFKQGGEYFM DPSVPVQGVP TMFGTTCENR KRRKEKSVGD EEDVPMICGG MGNAPVGMMS
     SEYDPKLQDG GRSGFAMTAH ESLAHGHSDR LDPARPQLPS RSPSLGSEDL PLAADPDKMT
     DLGKKPPGNV ISVIQHTNSL SRPNSFERSE STEMVACPQD KTPSPAETCD SEVLEAPVSP
     EWAPPGDGGE SGSKPTPSQQ VPQHSYHAQP RLVRQHNIQV PEIRVTEEPD KPEKEKEAPT
     KEPEKPVEEF QWPQRSETLS QLPAEKLPPK KKRLRLADLE HSSGESSFES TGTGLSRSPS
     QESNLSHSSS FSMSFDREET VKLTAPPKQD ESGKHSEFLT VPAGSYSLSV PGHHHQKEMR
     RCSSEQMPCP HPTEVPEIRS KSFDYGNLSH APVAGTSPST LSPSRERKKC FLVRQASFSG
     SPEIAQGEAG VDPSVKQEHM EHLHAGLRAA WSSVLPPLPG DDPGKQVGTC GPLSSGPPLH
     LTQQQIMHMD SQESLRNPLI QPTSYMTSKH LPEQPHLFPH QDAVPFSPIQ NALFQFQYPT
     VCMVHLPAQQ PPWWQTHFPH PFAPHPQNSY SKPPFQADLH SSYPLEHVAE HTGKKSADYP
     HAKEQTYPCY SGTSGLHSKN LPLKFPSDPG SKSTETPTEQ LLREDFASEN AGPLQSLPGT
     VVPVRIQTHV PSYGSVMYTS ISQILGQNSP AIVICKVDEN MTQRTLVTNA AMQGIGLNIA
     QVLGQHTGLE KYPLWKVPQT LPLGLESSIP LCLPSTSDNA ASLGGSKRML SPASSLELFM
     ETKQQKRVKE EKMYGQIVEE LSAVELTNSD IKKGLSRPQK PQLVRQGCAS EPKDGCFQSR
     SSSFSSLSPS SSQDHPSASG PFPPNREILP GSRAPPRRKF SGPSESRESS DELDMDETSS
     DMSMSPQSSA LPTGGGQQEE EGKARKLPVS MLVHMASGPG GNVANSTLLF TDVADFQQIL
     QFPSLRTTTT VSWCFLNYTK PSFVQQATFK SSVYASWCIS SCNPNPSGLN TKTTLALLRS
     KQKITAEIYT LAAMHRPGAG KLTSSSVWKQ FAQMKPDAPF LFGNKLERKL AGNVLKERGK
     GEIHGDKDLG SKQTEPIRIK IFEGGYKSNE DYVYVRGRGR GKYICEECGI RCKKPSMLKK
     HIRTHTDVRP YVCKLCNFAF KTKGNLTKHM KSKAHMKKCL ELGVSMTSVD DTETEEAENM
     EELHKTSEKH SMSGISTDHQ FSDAEESDGE DGDDNDDDDE DDDDFDDQGD LTPKTRSRST
     SPQPPRFSSL PVNVGAVAHG VPSDSSLGHS SLISYLVTLP SIQVTQLMTP SDSCDDTQMT
     EYQRLFQSKS TDSEPDKDRL DIPSSMDEEA MLSSEPSSSP RDFSPSSYRS SPGYDSSPCR
     DNSPKRYLIP KGDLSPRRHL SPRRDLSPMR HLSPRKEAAL RREMSQGDAS PRRHLSPRRP
     LSPGKDITAR RDLSPRRERR YMTTIRAPSP RRALYPNPPL SMGQYLQTEP IVLGPPNLRR
     GIPQVPYFSL YGDQEGAYEH HGSSLFPEGP TDYVFSHLPL HSQQQVRAPI PMVPVGGIQM
     VHSLPPALSG LHPPPTLPLP TEGSEEKKGA PGEAFAKDPY ILSRRHEKQA PQVLQSSGLP
     SSPSSPRLLM KQSTSEDSLN STEREQEENI QTCTKAIASL RIATEEAALL GADPPTWVQE
     SPQKPLESAH VSIRHFGGPE PGQPCTSAAH PDLHDGEKDT FGTSQTAVAH PTFYSKSSVD
     EKRVDFQSSK ELSLSTEEGN EPSPEKNQLH
//
ID   K0913_MOUSE             Reviewed;        1832 AA.
AC   Q3UHH1; B2RX90; Q5U4B9; Q6PCY6; Q80Y41; Q8CE12; Q8CHC3; Q9D789;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   RecName: Full=Zinc finger SWIM domain-containing protein KIAA0913;
GN   Name=Kiaa0913;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 64-1832 (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 622-1832 (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 769-1559.
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q3UHH1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UHH1-2; Sequence=VSP_029595;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q3UHH1-3; Sequence=VSP_029598;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q3UHH1-4; Sequence=VSP_029592, VSP_029599, VSP_029600;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q3UHH1-5; Sequence=VSP_029593, VSP_029594, VSP_029596,
CC                                  VSP_029597;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 SWIM-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB26298.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK009454; BAB26298.1; ALT_INIT; mRNA.
DR   EMBL; AK029263; BAC26361.1; -; mRNA.
DR   EMBL; AK147398; BAE27886.1; -; mRNA.
DR   EMBL; BC059058; AAH59058.1; -; mRNA.
DR   EMBL; BC085161; AAH85161.1; -; mRNA.
DR   EMBL; BC049362; AAH49362.1; -; mRNA.
DR   EMBL; BC151046; AAI51047.1; -; mRNA.
DR   EMBL; BC151056; AAI51057.1; -; mRNA.
DR   EMBL; BC151173; AAI51174.1; -; mRNA.
DR   EMBL; AB093273; BAC41457.3; -; mRNA.
DR   IPI; IPI00467933; -.
DR   IPI; IPI00877187; -.
DR   IPI; IPI00877196; -.
DR   IPI; IPI00877202; -.
DR   IPI; IPI00877263; -.
DR   RefSeq; NP_082272.1; NM_027996.2.
DR   UniGene; Mm.275082; -.
DR   STRING; Q3UHH1; -.
DR   PhosphoSite; Q3UHH1; -.
DR   PRIDE; Q3UHH1; -.
DR   Ensembl; ENSMUST00000022358; ENSMUSP00000022358; ENSMUSG00000021819.
DR   GeneID; 268721; -.
DR   KEGG; mmu:268721; -.
DR   UCSC; uc007sko.1; mouse.
DR   MGI; MGI:1919156; 2310021P13Rik.
DR   eggNOG; maNOG11060; -.
DR   GeneTree; ENSGT00390000012572; -.
DR   HOVERGEN; HBG092246; -.
DR   InParanoid; Q3UHH1; -.
DR   OMA; GEDVKWL; -.
DR   OrthoDB; EOG4KWJRX; -.
DR   NextBio; 392447; -.
DR   ArrayExpress; Q3UHH1; -.
DR   Bgee; Q3UHH1; -.
DR   CleanEx; MM_2310021P13RIK; -.
DR   Genevestigator; Q3UHH1; -.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR007527; Znf_SWIM.
DR   PROSITE; PS50966; ZF_SWIM; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Metal-binding; Phosphoprotein; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1832       Zinc finger SWIM domain-containing
FT                                protein KIAA0913.
FT                                /FTId=PRO_0000311803.
FT   ZN_FING     172    208       SWIM-type.
FT   COMPBIAS     56     65       Poly-Gly.
FT   COMPBIAS   1145   1206       Ser-rich.
FT   COMPBIAS   1474   1477       Poly-Ala.
FT   COMPBIAS   1496   1653       Pro-rich.
FT   MOD_RES     564    564       Phosphoserine.
FT   MOD_RES    1042   1042       Phosphoserine (By similarity).
FT   MOD_RES    1044   1044       Phosphoserine (By similarity).
FT   VAR_SEQ       1    895       Missing (in isoform 4).
FT                                /FTId=VSP_029592.
FT   VAR_SEQ       1    121       Missing (in isoform 5).
FT                                /FTId=VSP_029593.
FT   VAR_SEQ     122    126       LYSCL -> MKRTF (in isoform 5).
FT                                /FTId=VSP_029594.
FT   VAR_SEQ     669    702       Missing (in isoform 2).
FT                                /FTId=VSP_029595.
FT   VAR_SEQ     770    771       LF -> RG (in isoform 5).
FT                                /FTId=VSP_029596.
FT   VAR_SEQ     772   1832       Missing (in isoform 5).
FT                                /FTId=VSP_029597.
FT   VAR_SEQ     806    812       Missing (in isoform 3).
FT                                /FTId=VSP_029598.
FT   VAR_SEQ    1707   1734       VNYVHQFCVGAAKGVLSPFVLQEIVMET -> NTSPPQDHC
FT                                PPVSLPFLSQTSFLALTQS (in isoform 4).
FT                                /FTId=VSP_029599.
FT   VAR_SEQ    1735   1832       Missing (in isoform 4).
FT                                /FTId=VSP_029600.
FT   CONFLICT    599    599       G -> E (in Ref. 1; BAC26361).
FT   CONFLICT   1317   1318       QA -> KS (in Ref. 3; BAC41457).
FT   CONFLICT   1664   1664       R -> L (in Ref. 2; AAH59058).
SQ   SEQUENCE   1832 AA;  197061 MW;  30BD7C1D3157F93B CRC64;
     MELMFAEWED GERFSFEDSD RFEEDSLCSF ISEAESLCQN WRGWRKQSAG PNSPTGGGGG
     GGSGGTRTRD GLVIPLVELS AKQVAFHIPF EVVEKVYPPV PEQLQLRIAF WSFPENEEDI
     RLYSCLANGS ADEFQRGDQL FRMRAVKDPL QIGFHLSATV VPPQMVPPKG AYNVAVMFDR
     CRVTSCSCTC GAGAKWCTHV VALCLFRIHN ASAVCLRAPV SESLSRLQRD QLQKFAQYLI
     SELPQQILPT AQRLLDELLS SQSTAINTVC GAPDPTAGPS ASDQSTWYLD ESTLTDNIKK
     TLHKFCGPSP VVFSDVNSMY LSSTEPPAAA EWACLLRPLR GREPEGVWNL LSIVREMFKR
     RDSNAAPLLE ILTDQCLTYE QITGWWYSVR TSASHSSASG HTGRSNGQSE VAAHACASMC
     DEMVTLWRLA VLDPALSPQR RRELCAQLRQ WQLKVIENVK RGQHKKTLER LFPGFRPAVE
     ACYFNWEEAY PLPGVTYSGT DRKLALCWAR ALPARPGASR SGGLEESRPR PLPTEPAVRP
     KEPGAKRKGL GEGISSQRGP RRLSAEGGDK ALHKMGPSGG KAKVLGGTGS GGKSSAGSGS
     KRRLSSEDSS LEPDLAEMSL DDSSLALGAE ASTFGGFPES PPPCPSSVGS RGPSTFLPEP
     PDTYEEDAGV YFSEGPEPPT ASADHPGLLP GEVCTRDDLP STDDSGSGLH KTKEAAPAVG
     EEDDDYQAYY LNAQDGAGGE EEKAEGGTGE EHDLFAGLKP LEQESRMEVL FACAEALHAH
     GYSNEASRLT VELAQDLLAN PPDLKVEPPP AKGKKNKVST SRQTWVATNT LTKAAFLLTV
     LSERPEHHSL AFRVGMFALE LQRPPASTKA LEVKLAYQES EVAALLKKIP RGPSEMSTIR
     CRAEELREGT LCDYRPVLPL MLASFIFDVL CAPVVSLTGS RPPSRNWTNE MPGDEELGFE
     AAVAALGMKT TVSEAEHPLL CEGTRREKGD LALALMITYK DDQAKLKKIL DKLLDRESQT
     HKPQTLSSFY SSSRPATANQ RSPSKHGAPS APGALQPLTS SSAGPAQPGN VAGAGPGPTE
     GFTEKNVPES SPHSPCEGLP PEAALTPRPE GKVPSRLALG SRGGYNGRGW GSPGRPKKKH
     TGMASIDSSA PETTSDSSPT LSRRPLRGGW APTSWGRGQD SDSISSSSSD SLGSSSSSGS
     RRASASGGAR AKTVDVGRCY KGRRPESHAP HVPNQPSEAA AHFYFELAKT VLIKAGGNSS
     TSIFTHPSSS GGHQGPHRNL HLCAFEIGLY ALGLHNFVSP NWLSRTYSSH VSWITGQAME
     IGSAALTILV ECWDGHLTPP EVASLADRAS RARDSNMVRA AAELALSCLP HAHALNPNEI
     QRALVQCKEQ DNLMLEKACM AVEEAAKGGG VYPEVLFEVA HQWFWLYEET AGGSSTAREG
     ATSCSGSGMR AAGEAGRGLP EGRGAPGTEP VTVAAAAVTA AATVVPVISV GSSLYPGPGL
     GHGHSPGLHP YTALQPHLPC SPQYLTHPAH PAHPMPHMPR PAVFPVPSSA YPQGVHPAFL
     GAQYPYSVTP PSLAATAVSF PVPSMAPITV HPYHTEPGLP LPTSVALSSV HPASTFPAIQ
     GASLPALTTQ PSPLVSGGFP PPEEETHSQP VNPHSLHHLH AAYRVGMLAL EMLGRRAHND
     HPNNFSRSPP YTDDVKWLLG LAAKLGVNYV HQFCVGAAKG VLSPFVLQEI VMETLQRLNP
     IHAHNHLRAP AFHQLVQRCQ QAYMQYIHHR LIHLTPADYD DFVNAIRSAR SAFCLTPMGM
     MQFNDILQNL KRSKQTKELW QRVSLEITTF SP
//
ID   F190B_MOUSE             Reviewed;         833 AA.
AC   Q3UHI0; B2RT11; Q2NKY3; Q3TA20; Q6ZPX3; Q9DAD5;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 40.
DE   RecName: Full=Protein FAM190B;
DE   AltName: Full=Granule cell antiserum positive protein 14;
DE   AltName: Full=Protein GCAP14;
GN   Name=Fam190b; Synonyms=Gcap14, Kiaa1128;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 454-833 (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 57-728 (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-451, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=95107034; PubMed=7808216; DOI=10.1016/0169-328X(94)90152-X;
RA   Kambouris M., Triarhou L.C., Dlouhy S.R., Sangameswaran L., Luo F.,
RA   Ghetti B., Hodes M.E.;
RT   "Novel cDNA clones obtained by antibody screening of a mouse
RT   cerebellar cDNA expression library.";
RL   Brain Res. Mol. Brain Res. 25:183-191(1994).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3UHI0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UHI0-2; Sequence=VSP_029183;
CC       Name=3;
CC         IsoId=Q3UHI0-3; Sequence=VSP_029182, VSP_029183;
CC   -!- TISSUE SPECIFICITY: Expressed in cerebellar granule cells.
CC       Expressed in adult cerebrum, adult liver and neonatal cerebellum
CC       (at protein level).
CC   -!- SIMILARITY: Belongs to the FAM190 family.
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DR   EMBL; AK005931; BAB24323.1; -; mRNA.
DR   EMBL; AK147383; BAE27877.1; -; mRNA.
DR   EMBL; AK172153; BAE42850.1; -; mRNA.
DR   EMBL; BC111465; AAI11466.1; -; mRNA.
DR   EMBL; BC139090; AAI39091.1; -; mRNA.
DR   EMBL; AK129295; BAC98105.1; -; mRNA.
DR   IPI; IPI00118494; -.
DR   IPI; IPI00606737; -.
DR   IPI; IPI00874434; -.
DR   RefSeq; NP_081321.1; NM_027045.1.
DR   RefSeq; NP_082683.2; NM_028407.3.
DR   UniGene; Mm.27621; -.
DR   ProteinModelPortal; Q3UHI0; -.
DR   PhosphoSite; Q3UHI0; -.
DR   PRIDE; Q3UHI0; -.
DR   Ensembl; ENSMUST00000067700; ENSMUSP00000068550; ENSMUSG00000058690.
DR   Ensembl; ENSMUST00000090024; ENSMUSP00000087478; ENSMUSG00000058690.
DR   Ensembl; ENSMUST00000111893; ENSMUSP00000107524; ENSMUSG00000058690.
DR   GeneID; 72972; -.
DR   KEGG; mmu:72972; -.
DR   UCSC; uc007tbo.1; mouse.
DR   CTD; 72972; -.
DR   MGI; MGI:101859; Gcap14.
DR   HOGENOM; HBG505268; -.
DR   InParanoid; Q3UHI0; -.
DR   OMA; QTHRPRP; -.
DR   OrthoDB; EOG4PZJ62; -.
DR   NextBio; 337251; -.
DR   ArrayExpress; Q3UHI0; -.
DR   Bgee; Q3UHI0; -.
DR   CleanEx; MM_GCAP14; -.
DR   Genevestigator; Q3UHI0; -.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Phosphoprotein.
FT   CHAIN         1    833       Protein FAM190B.
FT                                /FTId=PRO_0000309462.
FT   COILED      711    747       Potential.
FT   COMPBIAS    603    615       His-rich.
FT   MOD_RES     224    224       Phosphoserine.
FT   MOD_RES     314    314       Phosphotyrosine (By similarity).
FT   MOD_RES     451    451       Phosphoserine.
FT   VAR_SEQ       1    533       Missing (in isoform 3).
FT                                /FTId=VSP_029182.
FT   VAR_SEQ     775    833       GGYCAPSFSPWQGSFQGMPRTVPPHRRQTSSTTAFQQPSQI
FT                                YRPRPGKTNKATTYRGPQ -> PQVLQPSSSLPRSTDHAQG
FT                                KLIKPQRTEAHSDYTVQGVCPGGAHPDGSCTHGLQQDNSRG
FT                                LQERPSSSSPQLTVDVVKYIPSETDLSMTLDAQEPHHLAEK
FT                                KPSDLQFVTPPPQTPSQSSTVDQTKRGGRNQCPQPKSLQLL
FT                                KPSNLSSLTPPPDSDSSPSRTSTCKKAPGITPCHSKHQPTS
FT                                NQNNPANHLNLKTSKLRPPSGSFKQKQISNPQVEPQNFQAK
FT                                TSIPRPLARPKELHAPHSGLHSGDCVASNRYSRLPKPKIH
FT                                (in isoform 2 and isoform 3).
FT                                /FTId=VSP_029183.
FT   CONFLICT     61     61       S -> P (in Ref. 3; BAC98105).
FT   CONFLICT     94     94       E -> D (in Ref. 3; BAC98105).
FT   CONFLICT    108    108       H -> Y (in Ref. 1; BAE42850).
FT   CONFLICT    129    129       T -> A (in Ref. 3; BAC98105).
FT   CONFLICT    181    181       S -> P (in Ref. 3; BAC98105).
FT   CONFLICT    212    212       I -> M (in Ref. 3; BAC98105).
FT   CONFLICT    307    307       A -> N (in Ref. 1; BAE42850 and 3;
FT                                BAC98105).
FT   CONFLICT    353    353       V -> I (in Ref. 3; BAC98105).
FT   CONFLICT    382    382       N -> S (in Ref. 3; BAC98105).
FT   CONFLICT    424    424       N -> K (in Ref. 3; BAC98105).
FT   CONFLICT    433    433       M -> V (in Ref. 3; BAC98105).
FT   CONFLICT    449    449       F -> L (in Ref. 3; BAC98105).
FT   CONFLICT    460    460       S -> G (in Ref. 3; BAC98105).
FT   CONFLICT    479    479       H -> Q (in Ref. 1; BAE42850).
SQ   SEQUENCE   833 AA;  92932 MW;  18C871932C925CA8 CRC64;
     MEEKTQIKTF LGSKLPKYGM KSVRSTLQPM PNGATVTLLG TSKSSNVKSY IKNNGSDCSL
     SHSFNWRKTN KYQLGSQNTA ELNNIQSTHD KLIEPEQHAP APGTLDGHGI KGGLKSASLF
     TSKLARPSTM FVSSAEELSQ KSFSGPSNLG KFTKGTLLGR TSYSSVNAKS HLNAFYGNRS
     SGNVQKPRVN SCASRSSSGE SLAQSPDNAK SITCEKMVRS QSFSHSIQNV FLPPSSITRS
     HSFNRAVDLT KPYQNQQLPV RVPLRSGMLT RSSLQSEVLN GNEHVGFGFN RPYAAAGKKL
     ALSNGPAVSS TLVYRMAHPP LLKSSRPPFS GPMTVDSNKN PPADMCVEEE GMVSAQDSSP
     GKDQELIENE SYRRDNDQTG KNESKVRYLS DDVDDISLSS LSSSDKNDLS EDFSDDFIDL
     EDSNRTRITP EEMTLKEEKH ESRPSKDIFD SPKESEQAFS KAEEWIDISV SDRSECTKHT
     SGNNLISPDT DYRAGSSFEL SPSDSSDGTY MWDEEGLEPI GSVHPVGSYE SSEMNSIDIL
     NNLESCDLED DDLMLDVDLP EDAPLENVEC DNMNRFDRTD RNVRQSQDGF WKRPPQRWSG
     QDHYHLSHPG HYHHHGQSDL SRGSPYRESP LGHFESYGGT PFFQAQKMFV DVPDNTVILD
     EMTLRHMVQD CTAVKTQLLK LKRLLHQHDG SGSLHDVQLS LPSSPEPEDG DQIYKNEDLL
     NEITQLKEEI KKKDEKIQLL EQQLATRCNC QQKSKEEKCT YADKYTQTPW RRIPGGYCAP
     SFSPWQGSFQ GMPRTVPPHR RQTSSTTAFQ QPSQIYRPRP GKTNKATTYR GPQ
//
ID   AAK1_MOUSE              Reviewed;         959 AA.
AC   Q3UHJ0; Q3TY53; Q6ZPZ6; Q80XP6;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=AP2-associated protein kinase 1;
DE            EC=2.7.11.1;
DE   AltName: Full=Adaptor-associated kinase 1;
GN   Name=Aak1; Synonyms=Kiaa1048;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 417-959 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 473-959 (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; THR-604; THR-618;
RP   SER-621; SER-635; SER-650; SER-729; SER-935 AND SER-936, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635; THR-638 AND
RP   SER-650, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-354, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-604; THR-618; SER-622
RP   AND SER-635, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Phosphorylates the AP2M1/mu2 subunit of the adaptor
CC       protein complex 2 (AP-2). May play a role in regulating aspects of
CC       clathrin-mediated endocytosis (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Stimulated by clathrin (By similarity).
CC   -!- SUBUNIT: Interacts with alpha-adaptin and AP-2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC       similarity). Cell membrane; Peripheral membrane protein (By
CC       similarity). Membrane, clathrin-coated pit (By similarity).
CC       Note=Active when found in clathrin-coated pits at the plasma
CC       membrane (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UHJ0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UHJ0-2; Sequence=VSP_020670;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Autophosphorylated (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AK147363; BAE27867.1; -; mRNA.
DR   EMBL; AK158879; BAE34710.1; -; mRNA.
DR   EMBL; AK129272; BAC98082.1; -; mRNA.
DR   EMBL; BC043125; AAH43125.1; -; mRNA.
DR   IPI; IPI00356608; -.
DR   IPI; IPI00458612; -.
DR   RefSeq; NP_001035195.1; NM_001040106.2.
DR   RefSeq; NP_808430.2; NM_177762.6.
DR   UniGene; Mm.221038; -.
DR   ProteinModelPortal; Q3UHJ0; -.
DR   SMR; Q3UHJ0; 34-315.
DR   PhosphoSite; Q3UHJ0; -.
DR   PRIDE; Q3UHJ0; -.
DR   Ensembl; ENSMUST00000003710; ENSMUSP00000003710; ENSMUSG00000057230.
DR   Ensembl; ENSMUST00000089519; ENSMUSP00000086948; ENSMUSG00000057230.
DR   GeneID; 269774; -.
DR   KEGG; mmu:269774; -.
DR   UCSC; uc009css.1; mouse.
DR   UCSC; uc009cst.1; mouse.
DR   CTD; 269774; -.
DR   MGI; MGI:1098687; Aak1.
DR   eggNOG; roNOG15358; -.
DR   GeneTree; ENSGT00510000046552; -.
DR   HOGENOM; HBG506474; -.
DR   HOVERGEN; HBG080803; -.
DR   InParanoid; Q3UHJ0; -.
DR   OMA; EGKHPEK; -.
DR   OrthoDB; EOG4Q2DF0; -.
DR   PhylomeDB; Q3UHJ0; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 393024; -.
DR   ArrayExpress; Q3UHJ0; -.
DR   Bgee; Q3UHJ0; -.
DR   Genevestigator; Q3UHJ0; -.
DR   GermOnline; ENSMUSG00000057230; Mus musculus.
DR   GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell membrane; Coated pit; Kinase;
KW   Membrane; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    959       AP2-associated protein kinase 1.
FT                                /FTId=PRO_0000250579.
FT   DOMAIN       46    315       Protein kinase.
FT   NP_BIND      52     60       ATP (By similarity).
FT   COMPBIAS     22     25       Poly-Gly.
FT   COMPBIAS    397    612       Gln-rich.
FT   COMPBIAS    656    661       Poly-Ala.
FT   ACT_SITE    176    176       Proton acceptor (By similarity).
FT   BINDING      74     74       ATP (By similarity).
FT   MOD_RES      14     14       Phosphoserine (By similarity).
FT   MOD_RES      18     18       Phosphoserine (By similarity).
FT   MOD_RES      20     20       Phosphoserine (By similarity).
FT   MOD_RES      21     21       Phosphoserine.
FT   MOD_RES     221    221       Phosphothreonine (By similarity).
FT   MOD_RES     222    222       Phosphothreonine (By similarity).
FT   MOD_RES     234    234       Phosphotyrosine (By similarity).
FT   MOD_RES     235    235       Phosphoserine (By similarity).
FT   MOD_RES     327    327       Phosphoserine (By similarity).
FT   MOD_RES     354    354       Phosphothreonine.
FT   MOD_RES     389    389       Phosphothreonine (By similarity).
FT   MOD_RES     441    441       Phosphothreonine (By similarity).
FT   MOD_RES     448    448       Phosphothreonine (By similarity).
FT   MOD_RES     604    604       Phosphothreonine.
FT   MOD_RES     616    616       Phosphoserine (By similarity).
FT   MOD_RES     618    618       Phosphothreonine.
FT   MOD_RES     621    621       Phosphoserine.
FT   MOD_RES     622    622       Phosphoserine.
FT   MOD_RES     635    635       Phosphoserine.
FT   MOD_RES     638    638       Phosphothreonine.
FT   MOD_RES     640    640       Phosphoserine (By similarity).
FT   MOD_RES     648    648       Phosphoserine (By similarity).
FT   MOD_RES     650    650       Phosphoserine.
FT   MOD_RES     651    651       Phosphothreonine (By similarity).
FT   MOD_RES     666    666       Phosphoserine (By similarity).
FT   MOD_RES     668    668       Phosphoserine (By similarity).
FT   MOD_RES     670    670       Phosphothreonine (By similarity).
FT   MOD_RES     672    672       Phosphothreonine (By similarity).
FT   MOD_RES     674    674       Phosphoserine (By similarity).
FT   MOD_RES     676    676       Phosphoserine (By similarity).
FT   MOD_RES     679    679       Phosphothreonine (By similarity).
FT   MOD_RES     680    680       Phosphoserine (By similarity).
FT   MOD_RES     688    688       Phosphoserine (By similarity).
FT   MOD_RES     729    729       Phosphoserine.
FT   MOD_RES     935    935       Phosphoserine.
FT   MOD_RES     936    936       Phosphoserine.
FT   VAR_SEQ     509    589       Missing (in isoform 2).
FT                                /FTId=VSP_020670.
FT   CONFLICT     79     79       N -> K (in Ref. 1; BAE27867).
FT   CONFLICT    686    686       N -> S (in Ref. 2; BAC98082).
SQ   SEQUENCE   959 AA;  103346 MW;  B7D666EFD56D097A CRC64;
     MKKFFDSRRE QGSSGLGSGS SGGGGSSSGL GSGYIGRVFG IGRQQVTVDE VLAEGGFALV
     FLVRTSNGVK CALKRMFVNN EHDLQVCKRE IQIMRDLSGH KNIVGYIDSS INNVSSGDVW
     EVLILMDFCR GGQVVNLMNQ RLQTGFTENE VLQIFCDTCE AVARLHQCKT PIIHRDLKVE
     NILLHDRGHY VLCDFGSATN KFQNPQAEGV NAVEDEIKKY TTLSYRAPEM VNLYSGKIIT
     TKADIWALGC LLYKLCYFTL PFGESQVAIC DGSFTIPDNS RYSQDMHCLI RYMLEPDPDK
     RPDIYQVSYF SFKLLKKECP VPNVQNSPIP AKLPEPVKAS EAAVKKTQPK ARLTDPIPTT
     ETSIAPRQRP KAGQTQPNPG ILPIQPALTP RKRATVQPLP QAAGPSNQPG LLPSVSQPKA
     QATPSQPLQS SQPKQPQAPP TPQQTPATQT QGLPTQAQAT PQHQQQHLLK QQQQQQQQPQ
     QPTAPPQPAG TFYQQQQQQQ QQQAQTQQFQ AVHPAAQQPV TAQFPVGSQG GAQQQLMQNF
     YHQQQQQQQQ QQQLMAQQAA LQQKTAVVVP QSQAQPATAP QAAAAQEPGQ IQAPVRQQPK
     VQTTPPPTIQ GQKVGSLTPP SSPKTQRAGH RRILSDVTHS AVFGVPASKS TQLLQAAAAE
     ASLNKSKSAT TTPSGSPRTS QQNVSNASEG STWNPFDDDN FSKLTAEELL NKDFAKLGEG
     KLPEKLGGSA ESLIPGFQPT QGDAFTTPSF SAGTAEKRKG GQAVDSGIPL LSVSDPFIPL
     QVPDAPEKLI EGLKSPDTSL LLPDLLPMTD PFGSTSDAVI DKADVAVESL IPGLEPPVAQ
     RLPSQTESVT SNRTDSLTGE DSLLDCSLLS NPTAGLLEEF APIALSAPTH KAAEDSNLIS
     GFGVAEGSEK VAEDEFDPIP VLITKNTQGG HSRNSSGSSE SSLPNLARSL LLVDQLIDL
//
ID   Q3UHJ6_MOUSE            Unreviewed;       766 AA.
AC   Q3UHJ6;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 46.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Iqsec3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK147351; BAE27861.1; -; mRNA.
DR   IPI; IPI00606415; -.
DR   UniGene; Mm.299442; -.
DR   ProteinModelPortal; Q3UHJ6; -.
DR   SMR; Q3UHJ6; 353-706.
DR   Ensembl; ENSMUST00000051049; ENSMUSP00000086421; ENSMUSG00000040797.
DR   MGI; MGI:2677208; Iqsec3.
DR   GeneTree; ENSGT00590000083058; -.
DR   HOVERGEN; HBG056324; -.
DR   ArrayExpress; Q3UHJ6; -.
DR   Bgee; Q3UHJ6; -.
DR   Genevestigator; Q3UHJ6; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000904; Sec7.
DR   InterPro; IPR023394; SEC7_alpha_orthog.
DR   Gene3D; G3DSA:1.10.1000.11; G3DSA:1.10.1000.11; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF01369; Sec7; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00222; Sec7; 1.
DR   SUPFAM; SSF48425; Sec7; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS50190; SEC7; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   766 AA;  83953 MW;  2E51F2AE58874078 CRC64;
     MLEHKYGGHL VSRRAACTIQ TAFRQYQLSK NFEKIRNSLL ESRLPRRISL RKVRAPTAES
     LVAEKALLEG CGLLGLPLGR SPSLPPTFAG SLTELEDSFT EQVQSLAKSI DDALSTWSLK
     TMCSLQESGA YQLHQALHPS AGQPGLETEA AAREPESGPG SGDEAGGLPQ GHSGTLMMAF
     RDVTVQIANQ NISVSSSTAL SVANCLGAQT AQATAEPAAA QAEQEDTADQ EVSEVPASEQ
     MDPPSEDSEA AESRAQSAQE PAVAQAVVEE AVATEAEEEE EGAKQAGKGA EAEGGDNSEQ
     LSSSSASTKS AKSSSEASAA ASKEALQAVI LSLPRYHCEN PASCRSPTLS TDTLRKRLYR
     IGLNLFNINP DKGIQFLISR GFIPDTPIGV AHFLLQRKGL SRQMIGEFLG NSKKQFNRDV
     LDCVVDEMDF SNMELDEALR KFQAHIRVQG EAQKVERLIE AFSQRYCMCN PEVVQQFHNP
     DTIFILAFAI ILLNTDMYSP NIKPDRKMML EDFIRNLRGV DDGADIPREL VVGIYERIQQ
     KELKSNEDHV TYVTKVEKSI VGMKTVLSMP HRRLVCCSRL FEVTDVNKLQ KQAAHQREVF
     LFNDLLVILK LCPKKKSSFT YTFCKAVGLL GMRFHLFENE YYSHGITLAT PLSGSEKKQV
     LHFCALGSDE MQKFVEDLKE SIAEVTELEQ IRIEWELEKQ QGTKTLSVRS AGAQGDPQSK
     QGSPTAKREA MAGEKAAESS GEVLINASPA RLTILPISRD TIKSYC
//
ID   MYCT_MOUSE              Reviewed;         637 AA.
AC   Q3UHK1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Proton myo-inositol cotransporter;
DE            Short=H(+)-myo-inositol cotransporter;
DE            Short=Hmit;
DE   AltName: Full=H(+)-myo-inositol symporter;
GN   Name=Slc2a13;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: H(+)-myo-inositol cotransporter. Can also transport
CC       related stereoisomers (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC       transporter (TC 2.A.1.1) family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE27856.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; AK147341; BAE27856.1; ALT_INIT; mRNA.
DR   IPI; IPI00120751; -.
DR   RefSeq; NP_001028805.2; NM_001033633.3.
DR   UniGene; Mm.360596; -.
DR   ProteinModelPortal; Q3UHK1; -.
DR   PhosphoSite; Q3UHK1; -.
DR   PRIDE; Q3UHK1; -.
DR   Ensembl; ENSMUST00000036723; ENSMUSP00000037298; ENSMUSG00000036298.
DR   Ensembl; ENSMUST00000109283; ENSMUSP00000104906; ENSMUSG00000036298.
DR   GeneID; 239606; -.
DR   KEGG; mmu:239606; -.
DR   NMPDR; fig|10090.3.peg.30472; -.
DR   UCSC; uc007xhy.1; mouse.
DR   CTD; 239606; -.
DR   MGI; MGI:2146030; Slc2a13.
DR   HOGENOM; HBG744444; -.
DR   HOVERGEN; HBG031722; -.
DR   InParanoid; Q3UHK1; -.
DR   OMA; IFWAYNF; -.
DR   OrthoDB; EOG4S7JPS; -.
DR   PhylomeDB; Q3UHK1; -.
DR   NextBio; 384195; -.
DR   ArrayExpress; Q3UHK1; -.
DR   Bgee; Q3UHK1; -.
DR   Genevestigator; Q3UHK1; -.
DR   GermOnline; ENSMUSG00000036298; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0022891; F:substrate-specific transmembrane transporter activity; IEA:InterPro.
DR   InterPro; IPR020846; Major_facilitator_SF.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   InterPro; IPR005828; Sub_transporter.
DR   InterPro; IPR003663; Sugar/inositol_transpt.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   Pfam; PF00083; Sugar_tr; 2.
DR   PRINTS; PR00171; SUGRTRNSPORT.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
DR   TIGRFAMs; TIGR00879; SP; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR   PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    637       Proton myo-inositol cotransporter.
FT                                /FTId=PRO_0000261317.
FT   TOPO_DOM      1     65       Cytoplasmic (Potential).
FT   TRANSMEM     66     86       Helical; Name=1; (Potential).
FT   TOPO_DOM     87    114       Extracellular (Potential).
FT   TRANSMEM    115    135       Helical; Name=2; (Potential).
FT   TOPO_DOM    136    137       Cytoplasmic (Potential).
FT   TRANSMEM    138    158       Helical; Name=3; (Potential).
FT   TOPO_DOM    159    167       Extracellular (Potential).
FT   TRANSMEM    168    188       Helical; Name=4; (Potential).
FT   TOPO_DOM    189    201       Cytoplasmic (Potential).
FT   TRANSMEM    202    222       Helical; Name=5; (Potential).
FT   TOPO_DOM    223    228       Extracellular (Potential).
FT   TRANSMEM    229    249       Helical; Name=6; (Potential).
FT   TOPO_DOM    250    313       Cytoplasmic (Potential).
FT   TRANSMEM    314    334       Helical; Name=7; (Potential).
FT   TOPO_DOM    335    352       Extracellular (Potential).
FT   TRANSMEM    353    373       Helical; Name=8; (Potential).
FT   TOPO_DOM    374    382       Cytoplasmic (Potential).
FT   TRANSMEM    383    403       Helical; Name=9; (Potential).
FT   TOPO_DOM    404    497       Extracellular (Potential).
FT   TRANSMEM    498    518       Helical; Name=10; (Potential).
FT   TOPO_DOM    519    538       Cytoplasmic (Potential).
FT   TRANSMEM    539    559       Helical; Name=11; (Potential).
FT   TOPO_DOM    560    562       Extracellular (Potential).
FT   TRANSMEM    563    583       Helical; Name=12; (Potential).
FT   TOPO_DOM    584    637       Cytoplasmic (Potential).
FT   MOD_RES     629    629       Phosphoserine (By similarity).
FT   MOD_RES     634    634       Phosphoserine (By similarity).
FT   CARBOHYD    422    422       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    447    447       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    474    474       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   637 AA;  69062 MW;  CF13253E46E934D2 CRC64;
     MSRKASEDVE YTLRSLSSLM GERRRRQPEP GAPGGERSLL AAESAASLQG AELERAARRQ
     FQRDETPAFV YAAAAFSALG GFLFGYDTGV VSGAMLLLRR QMRLGAMWQE LLVSGAVGAA
     AVAALAGGAL NGALGRRSAI LLASALCTVG SAVLAAAANK ETLLAGRLVV GLGIGIASMT
     VPVYIAEVSP PNLRGRLVTI NTLFITGGQF FASVVDGAFS YLQKDGWRYM LGLAAIPAVI
     QFLGFLFLPE SPRWLIQKGQ TQKARRILSQ MRGNQTIDEE YDSIRNSIEE EEKEATAAGP
     IICRMLSYPP TRRALVVGCG LQMFQQLSGI NTIMYYSATI LQMSGVEDDR LAIWLASITA
     FTNFIFTLVG VWLVEKVGRR KLTFGSLAGT TVALIILALG FLLSAQVSPR VTFRPTTPSD
     QNTTCTGYSY CNECMLDPDC GFCYKINGSA VIDSSCVPVN KASTTEAAWG RCDNETKFKA
     EGAHWAYSFC PTPYSWTALV GLVLYLVFFA PGMGPMPWTV NSEIYPLWAR STGNACSAGI
     NWIFNVLVSL TFLHTAEYLT YYGAFFLYAG FAAVGLLFVY GCLPETKGKK LEEIESLFDH
     RLCSCGAADS DEGRYIEYIR VKGSNYHLSD NDASDVE
//
ID   TEN4_MOUSE              Reviewed;        2771 AA.
AC   Q3UHK6; O70465; Q3TSI0; Q3UH52; Q80TF5; Q9WTS7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Teneurin-4;
DE            Short=Ten-4;
DE   AltName: Full=Downstream of CHOP4;
DE   AltName: Full=Protein Odd Oz/ten-m homolog 4;
DE   AltName: Full=Tenascin-M4;
DE            Short=Ten-m4;
GN   Name=Odz4; Synonyms=Doc4, Kiaa1302, Tnm4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=NIH Swiss;
RX   MEDLINE=98315054; PubMed=9649432; DOI=10.1093/emboj/17.13.3619;
RA   Wang X.-Z., Kuroda M., Sok J., Batchvarova N., Kimmel R., Chung P.,
RA   Zinszner H., Ron D.;
RT   "Identification of novel stress-induced genes downstream of chop.";
RL   EMBO J. 17:3619-3630(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   PubMed=10225957; DOI=10.1083/jcb.145.3.563;
RA   Oohashi T., Zhou X.-H., Feng K., Richter B., Moergelin M., Perez M.T.,
RA   Su W.D., Chiquet-Ehrismann R., Rauch U., Faessler R.;
RT   "Mouse ten-m/Odz is a new family of dimeric type II transmembrane
RT   proteins expressed in many tissues.";
RL   J. Cell Biol. 145:563-577(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Muellerian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1574-2771.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1707 AND ASN-2190, AND
RP   MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: May function as a cellular signal transducer.
CC   -!- SUBUNIT: Homodimer; disulfide-linked (Probable).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane
CC       protein (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q3UHK6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UHK6-2; Sequence=VSP_021405, VSP_021407, VSP_021408;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q3UHK6-3; Sequence=VSP_021404, VSP_021405, VSP_021406;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q3UHK6-4; Sequence=VSP_021404;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: EGF-like domains 2 and 5 which have an odd number of
CC       cysteines might enable the formation of intermolecular disulfide
CC       bonds.
CC   -!- DOMAIN: Cytoplasmic proline-rich regions could serve as docking
CC       domains for intracellular SH3-containing proteins.
CC   -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC   -!- SIMILARITY: Contains 8 EGF-like domains.
CC   -!- SIMILARITY: Contains 5 NHL repeats.
CC   -!- SIMILARITY: Contains 1 teneurin N-terminal domain.
CC   -!- SIMILARITY: Contains 23 YD repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF059485; AAC31807.1; -; mRNA.
DR   EMBL; AB025413; BAA77399.1; -; mRNA.
DR   EMBL; AK147579; BAE28005.1; -; mRNA.
DR   EMBL; AK147329; BAE27851.1; -; mRNA.
DR   EMBL; AK162046; BAE36695.1; -; mRNA.
DR   EMBL; AK122490; BAC65772.1; -; mRNA.
DR   IPI; IPI00157497; -.
DR   IPI; IPI00754819; -.
DR   IPI; IPI00798441; -.
DR   IPI; IPI00798616; -.
DR   PIR; T14271; T14271.
DR   RefSeq; NP_035988.2; NM_011858.3.
DR   UniGene; Mm.254610; -.
DR   UniGene; Mm.391678; -.
DR   ProteinModelPortal; Q3UHK6; -.
DR   SMR; Q3UHK6; 568-871, 1349-1377, 1469-1504, 1529-1567.
DR   STRING; Q3UHK6; -.
DR   PRIDE; Q3UHK6; -.
DR   Ensembl; ENSMUST00000050858; ENSMUSP00000058525; ENSMUSG00000048078.
DR   Ensembl; ENSMUST00000084996; ENSMUSP00000082066; ENSMUSG00000048078.
DR   Ensembl; ENSMUST00000107166; ENSMUSP00000102784; ENSMUSG00000048078.
DR   Ensembl; ENSMUST00000107169; ENSMUSP00000102787; ENSMUSG00000048078.
DR   GeneID; 23966; -.
DR   KEGG; mmu:23966; -.
DR   UCSC; uc009iio.1; mouse.
DR   UCSC; uc009iip.1; mouse.
DR   UCSC; uc009iiq.1; mouse.
DR   CTD; 23966; -.
DR   MGI; MGI:2447063; Odz4.
DR   GeneTree; ENSGT00580000081247; -.
DR   HOGENOM; HBG444169; -.
DR   HOVERGEN; HBG080306; -.
DR   InParanoid; Q3UHK6; -.
DR   NextBio; 303833; -.
DR   ArrayExpress; Q3UHK6; -.
DR   Bgee; Q3UHK6; -.
DR   CleanEx; MM_ODZ4; -.
DR   Genevestigator; Q3UHK6; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR022385; Rhs_assc_core.
DR   InterPro; IPR009471; Ten_N.
DR   InterPro; IPR006530; YD.
DR   Gene3D; G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 2.
DR   Pfam; PF07974; EGF_2; 4.
DR   Pfam; PF05593; RHS_repeat; 1.
DR   Pfam; PF06484; Ten_N; 2.
DR   SMART; SM00181; EGF; 7.
DR   SUPFAM; SSF49464; CarboxypepD_reg; 1.
DR   TIGRFAMs; TIGR03696; Rhs_assc_core; 1.
DR   TIGRFAMs; TIGR01643; YD_repeat_2x; 5.
DR   PROSITE; PS00022; EGF_1; 8.
DR   PROSITE; PS01186; EGF_2; 7.
DR   PROSITE; PS50026; EGF_3; 5.
DR   PROSITE; PS51125; NHL; FALSE_NEG.
DR   PROSITE; PS51361; TENEURIN_N; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Membrane; Repeat; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN         1   2771       Teneurin-4.
FT                                /FTId=PRO_0000259509.
FT   TOPO_DOM      1    345       Cytoplasmic (Potential).
FT   TRANSMEM    346    366       Helical; (Potential).
FT   TOPO_DOM    367   2771       Extracellular (Potential).
FT   DOMAIN        1    341       Teneurin N-terminal.
FT   DOMAIN      564    595       EGF-like 1.
FT   DOMAIN      596    626       EGF-like 2.
FT   DOMAIN      628    660       EGF-like 3.
FT   DOMAIN      661    692       EGF-like 4.
FT   DOMAIN      694    727       EGF-like 5.
FT   DOMAIN      728    759       EGF-like 6.
FT   DOMAIN      760    789       EGF-like 7.
FT   DOMAIN      790    833       EGF-like 8.
FT   REPEAT     1218   1261       NHL 1.
FT   REPEAT     1266   1310       NHL 2.
FT   REPEAT     1336   1380       NHL 3.
FT   REPEAT     1395   1446       NHL 4.
FT   REPEAT     1525   1568       NHL 5.
FT   REPEAT     1578   1597       YD 1.
FT   REPEAT     1614   1634       YD 2.
FT   REPEAT     1677   1696       YD 3.
FT   REPEAT     1697   1719       YD 4.
FT   REPEAT     1889   1908       YD 5.
FT   REPEAT     1930   1948       YD 6.
FT   REPEAT     1949   1969       YD 7.
FT   REPEAT     1976   1993       YD 8.
FT   REPEAT     1994   2015       YD 9.
FT   REPEAT     2016   2033       YD 10.
FT   REPEAT     2036   2056       YD 11.
FT   REPEAT     2059   2079       YD 12.
FT   REPEAT     2087   2106       YD 13.
FT   REPEAT     2112   2129       YD 14.
FT   REPEAT     2130   2156       YD 15.
FT   REPEAT     2158   2171       YD 16.
FT   REPEAT     2172   2195       YD 17.
FT   REPEAT     2198   2218       YD 18.
FT   REPEAT     2219   2239       YD 19.
FT   REPEAT     2241   2261       YD 20.
FT   REPEAT     2273   2293       YD 21.
FT   REPEAT     2295   2315       YD 22.
FT   REPEAT     2341   2382       YD 23.
FT   COMPBIAS    179    184       Poly-Pro.
FT   CARBOHYD    469    469       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    942    942       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1261   1261       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1611   1611       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1707   1707       N-linked (GlcNAc...).
FT   CARBOHYD   1743   1743       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1801   1801       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1886   1886       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1987   1987       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2190   2190       N-linked (GlcNAc...).
FT   CARBOHYD   2330   2330       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2648   2648       N-linked (GlcNAc...) (Potential).
FT   DISULFID    568    578       By similarity.
FT   DISULFID    572    583       By similarity.
FT   DISULFID    585    594       By similarity.
FT   DISULFID    603    614       By similarity.
FT   DISULFID    616    625       By similarity.
FT   DISULFID    632    643       By similarity.
FT   DISULFID    637    648       By similarity.
FT   DISULFID    650    659       By similarity.
FT   DISULFID    664    675       By similarity.
FT   DISULFID    669    680       By similarity.
FT   DISULFID    682    691       By similarity.
FT   DISULFID    702    715       By similarity.
FT   DISULFID    717    726       By similarity.
FT   DISULFID    731    741       By similarity.
FT   DISULFID    735    746       By similarity.
FT   DISULFID    748    757       By similarity.
FT   DISULFID    762    772       By similarity.
FT   DISULFID    766    777       By similarity.
FT   DISULFID    779    788       By similarity.
FT   DISULFID    802    812       By similarity.
FT   DISULFID    806    821       By similarity.
FT   DISULFID    823    832       By similarity.
FT   VAR_SEQ       1      1       M -> MEPDHSALSAARAQFVDVEEREPEAM (in
FT                                isoform 3 and isoform 4).
FT                                /FTId=VSP_021404.
FT   VAR_SEQ     164    164       T -> TGAPLHCSSASSTPIEQSPSPPPSPPANESQRRLLG
FT                                NGVAQPTPDSDSEEEFVPNSFLVKSGSASLGVAAN (in
FT                                isoform 2 and isoform 3).
FT                                /FTId=VSP_021405.
FT   VAR_SEQ     251    283       Missing (in isoform 3).
FT                                /FTId=VSP_021406.
FT   VAR_SEQ     791    799       Missing (in isoform 2).
FT                                /FTId=VSP_021407.
FT   VAR_SEQ    1269   1275       Missing (in isoform 2).
FT                                /FTId=VSP_021408.
FT   CONFLICT    136    137       TR -> EK (in Ref. 3; BAE36695).
FT   CONFLICT    152    164       LTLTDTEHENTET -> EKSGSASLGVAAN (in Ref.
FT                                3; BAE36695).
FT   CONFLICT    240    240       L -> V (in Ref. 1; AAC31807).
FT   CONFLICT    244    244       N -> K (in Ref. 1; AAC31807).
FT   CONFLICT    247    247       L -> V (in Ref. 1; AAC31807).
FT   CONFLICT    261    261       L -> W (in Ref. 1; AAC31807).
FT   CONFLICT    271    271       L -> F (in Ref. 1; AAC31807).
FT   CONFLICT    276    276       H -> R (in Ref. 1; AAC31807).
FT   CONFLICT    286    286       L -> F (in Ref. 1; AAC31807).
FT   CONFLICT    422    429       KPSSLFPE -> RVAALSVL (in Ref. 3;
FT                                BAE36695).
FT   CONFLICT    493    493       F -> L (in Ref. 1; AAC31807).
FT   CONFLICT    780    780       S -> T (in Ref. 1; AAC31807).
FT   CONFLICT    895    895       S -> P (in Ref. 2; BAA77399).
FT   CONFLICT   1013   1013       C -> R (in Ref. 1; AAC31807).
FT   CONFLICT   1039   1039       E -> G (in Ref. 3; BAE28005).
FT   CONFLICT   1077   1077       L -> V (in Ref. 1; AAC31807).
FT   CONFLICT   1133   1133       L -> F (in Ref. 2; BAA77399).
FT   CONFLICT   1457   1457       H -> Q (in Ref. 1; AAC31807).
FT   CONFLICT   1743   1743       N -> H (in Ref. 1; AAC31807).
FT   CONFLICT   1746   1746       A -> G (in Ref. 1; AAC31807).
FT   CONFLICT   1831   1831       R -> P (in Ref. 1; AAC31807).
FT   CONFLICT   1875   1875       L -> F (in Ref. 1; AAC31807).
FT   CONFLICT   1952   1952       N -> D (in Ref. 3; BAE28005).
FT   CONFLICT   2144   2144       T -> S (in Ref. 1; AAC31807).
FT   CONFLICT   2160   2160       I -> T (in Ref. 1; AAC31807).
FT   CONFLICT   2256   2256       K -> R (in Ref. 3; BAE28005).
FT   CONFLICT   2262   2262       F -> S (in Ref. 1; AAC31807).
FT   CONFLICT   2330   2330       N -> S (in Ref. 1; AAC31807).
FT   CONFLICT   2657   2657       V -> M (in Ref. 1; AAC31807, 2; BAA77399
FT                                and 4; BAC65772).
SQ   SEQUENCE   2771 AA;  308425 MW;  15EF31E25A171FD0 CRC64;
     MDVKERKPYR SLTRRRDAER RYTSSSADSE EGKGPQKSYS SSETLKAYDQ DARLAYGSRV
     KDMVPQEAEE FCRTGTNFTL RELGLGEMTP PHGTLYRTDI GLPHCGYSMG ASSDADLEAD
     TVLSPEHPVR LWGRSTRSGR SSCLSSRANS NLTLTDTEHE NTETDHPSSL QNHPRLRTPP
     PPLPHAHTPN QHHAASINSL NRGNFTPRSN PSPAPTDHSL SGEPPAGSAQ EPTHAQDNWL
     LNSNIPLETR NLGKQPFLGT LQDNLIEMDI LSASRHDGAY SDGHFLFKPG GTSPLFCTTS
     PGYPLTSSTV YSPPPRPLPR STFSRPAFNL KKPSKYCNWK CAALSAILIS ATLVILLAYF
     VAMHLFGLNW HLQPMEGQMQ MYEITEDTAS SWPVPTDVSL YPSGGTGLET PDRKGKGAAE
     GKPSSLFPED SFIDSGEIDV GRRASQKIPP GTFWRSQVFI DHPVHLKFNV SLGKAALVGI
     YGRKGLPPSH TQFDFVELLD GRRLLTQEAR SLEGPQRQSR GPVPPSSHET GFIQYLDSGI
     WHLAFYNDGK ESEVVSFLTT AIESVDNCPS NCYGNGDCIS GTCHCFLGFL GPDCGRASCP
     VLCSGNGQYM KGRCLCHSGW KGAECDVPTN QCIDVACSSH GTCIMGTCIC NPGYKGESCE
     EVDCMDPTCS SRGVCVRGEC HCSVGWGGTN CETPRATCLD QCSGHGTFLP DTGLCNCDPS
     WTGHDCSIEI CAADCGGHGV CVGGTCRCED GWMGAACDQR ACHPRCAEHG TCRDGKCECS
     PGWNGEHCTI AHYLDRVVKE GCPGLCNGNG RCTLDLNGWH CVCQLGWRGT GCDTSMETGC
     GDGKDNDGDG LVDCMDPDCC LQPLCHVNPL CLGSPDPLDI IQETQAPVSQ QNLNSFYDRI
     KFLVGRDSTH SIPGENPFDG GHACVIRGQV MTSDGTPLVG VNISFINNPL FGYTISRQDG
     SFDLVTNGGI SIILRFERAP FITQEHTLWL PWDRFFVMET IVMRHEENEI PSCDLSNFAR
     PNPVVSPSPL TSFASSCAEK GPIVPEIQAL QEEIVIAGCK MRLSYLSSRT PGYKSVLRIS
     LTHPTIPFNL MKVHLMVAVE GRLFRKWFAA APDLSYYFIW DKTDVYNQKV FGLSEAFVSV
     GYEYESCPDL ILWEKRTAVL QGYEIDASKL GGWSLDKHHA LNIQSGILHK GNGENQFVSQ
     QPPVIGSIMG NGRRRSISCP SCNGLADGNK LLAPVALTCG SDGSLYVGDF NYIRRIFPSG
     NVTNILEMRN KDFRHSHSPA HKYYLATDPM SGAVFLSDTN SRRVFKVKST TVVKDLVKNS
     EVVAGTGDQC LPFDDTRCGD GGKATEATLT NPRGITVDKF GLIYFVDGTM IRRVDQNGII
     STLLGSNDLT SARPLSCDSV MEISQVRLEW PTDLAINPMD NSLYVLDNNV VLQISENHQV
     RIVAGRPMHC QVPGIDHFLL SKVAIHATLE SATALAVSHN GVLYIAETDE KKINRIRQVT
     TSGEISLVAG APSGCDCKND ANCDCFSGDD GYAKDAKLNT PSSLAVCADG ELYVADLGNI
     RIRFIRKNKP FLNTQNMYEL SSPIDQELYL FDTSGKHLYT QSLPTGDYLY NFTYTGDGDI
     THITDNNGNM VNVRRDSTGM PLWLVVPDGQ VYWVTMGTNS ALRSVTTQGH ELAMMTYHGN
     SGLLATKSNE NGWTTFYEYD SFGRLTNVTF PTGQVSSFRS DTDSSVHVQV ETSSKDDVTI
     TTNLSASGAF YTLLQDQVRN SYYIGADGSL RLLLANGMEV ALQTEPHLLA GTVNPTVGKR
     NVTLPIDNGL NLVEWRQRKE QARGQVTVFG RRLRVHNRNL LSLDFDRVTR TEKIYDDHRK
     FTLRILYDQA GRPSLWSPSS RLNGVNVTYS PGGHIAGIQR GIMSERMEYD QAGRITSRIF
     ADGKMWSYTY LEKSMVLHLH SQRQYIFEFD KNDRLSSVTM PNVARQTLET IRSVGYYRNI
     YQPPEGNASV IQDFTEDGHL LHTFYLGTGR RVIYKYGKLS KLAETLYDTT KVSFTYDETA
     GMLKTVNLQN EGFTCTIRYR QIGPLIDRQI FRFTEEGMVN ARFDYNYDNS FRVTSMQAVI
     NETPLPIDLY RYDDVSGKTE QFGKFGVIYY DINQIITTAV MTHTKHFDAY GRMKEVQYEI
     FRSLMYWMTV QYDNMGRVVK KELKVGPYAN TTRYSYEYDA DGQLQTVSIN DKPLWRYSYD
     LNGNLHLLSP GNSARLTPLR YDLRDRITRL GDVQYKMDED GFLRQRGGDV FEYNSAGLLI
     KAYNRASGWS VRYRYDGLGR RVSSKSSHSH HLQFFYADLT NPTKVTHLYN HSSSEITSLY
     YDLQGHLFAM ELSSGDEFYI ACDNIGTPLA VFSGTGLMIK QILYTAYGEI YMDTNPNFQI
     IIGYHGGLYD PLTKLVHMGR RDYDVLAGRW TSPDHELWKR LSSNSIVPFH LYMFKNNNPI
     SNSQDIKCFM TDVNSWLLTF GFQLHNVIPG YPKPDTDAME PSYELVHTQM KTQEWDNSKS
     ILGVQCEVQK QLKAFVTLER FDQLYGSTIT SCQQAPETKK FASSGSIFGK GVKFALKDGR
     VTTDIISVAN EDGRRIAAIL NNAHYLENLH FTIDGVDTHY FVKPGPSEGD LAILGLSGGR
     RTLENGVNVT VSQINTVLSG RTRRYTDIQL QYRALCLNTR YGTTVDEEKV RVLELARQRA
     VRQAWAREQQ RLREGEEGLR AWTDGEKQQV LNTGRVQGYD GFFVTSVEQY PELSDSANNI
     HFMRQSEMGR R
//
ID   CAMKV_MOUSE             Reviewed;         512 AA.
AC   Q3UHL1; Q8VD20;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=CaM kinase-like vesicle-associated protein;
GN   Name=Camkv;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-470, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-154, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-414; THR-446; THR-449
RP   AND SER-452, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Does not appear to have detectable kinase activity.
CC   -!- COFACTOR: Calcium (By similarity).
CC   -!- SUBUNIT: Interacts with calmodulin, in the presence of calcium (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       (By similarity). Cytoplasmic vesicle membrane; Peripheral membrane
CC       protein (By similarity). Note=Predominantly observed in
CC       association with the plasma membrane of soma and in neurites, both
CC       axons and dendrites. May be associated with vesicular structures
CC       (By similarity).
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AK147323; BAE27846.1; -; mRNA.
DR   EMBL; BC017634; AAH17634.1; -; mRNA.
DR   EMBL; BC111033; AAI11034.1; -; mRNA.
DR   IPI; IPI00122486; -.
DR   RefSeq; NP_663596.1; NM_145621.2.
DR   UniGene; Mm.274540; -.
DR   HSSP; Q9HBH9; 2AC5.
DR   ProteinModelPortal; Q3UHL1; -.
DR   SMR; Q3UHL1; 18-291.
DR   STRING; Q3UHL1; -.
DR   PhosphoSite; Q3UHL1; -.
DR   PRIDE; Q3UHL1; -.
DR   Ensembl; ENSMUST00000035700; ENSMUSP00000040430; ENSMUSG00000032936.
DR   GeneID; 235604; -.
DR   KEGG; mmu:235604; -.
DR   UCSC; uc009rnk.1; mouse.
DR   CTD; 235604; -.
DR   MGI; MGI:2384296; Camkv.
DR   eggNOG; roNOG04034; -.
DR   GeneTree; ENSGT00600000084207; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108055; -.
DR   InParanoid; Q3UHL1; -.
DR   OMA; KEYFLFL; -.
DR   OrthoDB; EOG49079C; -.
DR   NextBio; 382777; -.
DR   ArrayExpress; Q3UHL1; -.
DR   Bgee; Q3UHL1; -.
DR   CleanEx; MM_CAMKV; -.
DR   Genevestigator; Q3UHL1; -.
DR   GermOnline; ENSMUSG00000032936; Mus musculus.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasmic vesicle; Membrane; Phosphoprotein.
FT   CHAIN         1    512       CaM kinase-like vesicle-associated
FT                                protein.
FT                                /FTId=PRO_0000250095.
FT   DOMAIN       24    286       Protein kinase.
FT   COMPBIAS    335    490       Ala-rich.
FT   MOD_RES     154    154       Phosphotyrosine.
FT   MOD_RES     414    414       Phosphothreonine.
FT   MOD_RES     446    446       Phosphothreonine.
FT   MOD_RES     449    449       Phosphothreonine.
FT   MOD_RES     452    452       Phosphoserine.
FT   MOD_RES     470    470       Phosphothreonine.
FT   CONFLICT    479    479       D -> G (in Ref. 1; BAE27846).
SQ   SEQUENCE   512 AA;  54819 MW;  CFEFD4C43CC889A9 CRC64;
     MPFGCVTLGD KKNYNQPSEV TDRYDLGQVI KTEEFCEIFR AKDKTTGKLH TCKKFQKRDG
     RKVRKAAKNE IGILKMVKHP NILQLVDVFV TRKEYFIFLE LATGREVFDW ILDQGYYSER
     DTSNVVRQVL EAVAYLHSLK IVHRNLKLEN LVYYNRLKNS KIVISDFHLA KLENGLIKEP
     CGTPEYLAPE VVGRQRYGRP VDCWAIGVIM YILLSGNPPF YEEVEEDDYE NHDKNLFRKI
     LAGDYEFDSP YWDDISQAAK DLVTRLMEVE QDQRITAEEA ISHEWISGNA ASDKNIKDGV
     CAQIEKNFAR AKWKKAVRVT TLMKRLRAPE QSGTAATQSA SDAATPGAAG GAIAAAAAAA
     AAGGAASASG ASATAATEGG AGCAAKSDDI ASADRSATPA TDGSATPATD GSVTPATDGS
     ITPATDGSVT PATDRSATPA TDGRATPATE ESTVPATQSS ALPAAKAAAT PEPAVAQPDS
     TALEGATGQA PPSSKGEEAT GCAQESQRVE TS
//
ID   DOP2_MOUSE              Reviewed;        2295 AA.
AC   Q3UHQ6; Q3UH78; Q80TN8;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 2.
DT   08-MAR-2011, entry version 37.
DE   RecName: Full=Protein dopey-2;
GN   Name=Dopey2; Synonyms=Kiaa0933;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 740-2295 (ISOFORMS 1/2).
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=12767918; DOI=10.1016/S0006-291X(03)00867-2;
RA   Lopes C., Chettouh Z., Delabar J.-M., Rachidi M.;
RT   "The differentially expressed C21orf5 gene in the medial temporal-lobe
RT   system could play a role in mental retardation in Down syndrome and
RT   transgenic mice.";
RL   Biochem. Biophys. Res. Commun. 305:915-924(2003).
CC   -!- FUNCTION: May be involved in protein traffic between late Golgi
CC       and early endosomes (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UHQ6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UHQ6-2; Sequence=VSP_027430;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in liver, heart and brain.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in developing nervous
CC       system.
CC   -!- SIMILARITY: Belongs to the dopey family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK147255; BAE27801.1; -; mRNA.
DR   EMBL; AK147536; BAE27979.1; -; mRNA.
DR   EMBL; AK122403; BAC65685.1; -; mRNA.
DR   IPI; IPI00556808; -.
DR   IPI; IPI00856745; -.
DR   RefSeq; NP_080976.1; NM_026700.2.
DR   RefSeq; NP_081569.1; NM_027293.1.
DR   UniGene; Mm.23230; -.
DR   PhosphoSite; Q3UHQ6; -.
DR   PRIDE; Q3UHQ6; -.
DR   Ensembl; ENSMUST00000045004; ENSMUSP00000044437; ENSMUSG00000022946.
DR   GeneID; 70028; -.
DR   KEGG; mmu:70028; -.
DR   CTD; 70028; -.
DR   MGI; MGI:1917278; Dopey2.
DR   HOGENOM; HBG403045; -.
DR   HOVERGEN; HBG051222; -.
DR   InParanoid; Q3UHQ6; -.
DR   OrthoDB; EOG4D52WS; -.
DR   NextBio; 330857; -.
DR   ArrayExpress; Q3UHQ6; -.
DR   Bgee; Q3UHQ6; -.
DR   CleanEx; MM_DOPEY2; -.
DR   Genevestigator; Q3UHQ6; -.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR007249; Dopey_N.
DR   Pfam; PF04118; Dopey_N; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1   2295       Protein dopey-2.
FT                                /FTId=PRO_0000297949.
FT   MOD_RES     934    934       Phosphoserine (By similarity).
FT   MOD_RES    1657   1657       Phosphoserine (By similarity).
FT   VAR_SEQ       1    118       Missing (in isoform 2).
FT                                /FTId=VSP_027430.
FT   CONFLICT    721    721       Y -> H (in Ref. 1; BAE27979).
FT   CONFLICT    791    791       W -> G (in Ref. 1; BAE27801).
FT   CONFLICT   1251   1251       T -> S (in Ref. 1; BAE27801).
FT   CONFLICT   1876   1876       S -> TG (in Ref. 1; BAE27979).
FT   CONFLICT   1881   1881       S -> P (in Ref. 1; BAE27801).
SQ   SEQUENCE   2295 AA;  257509 MW;  776785303AECCB77 CRC64;
     MDPEEQELLN DYRYRSYSSV IEKALRNFES SSEWADLISS LGKLNKALQS NLKYSLLPRR
     LIISKRLAQC LHPALPSGVH LKALETYEII FKIVGTKWLA KDLFLYSCGL FPLLAYAAMS
     VRPVLLGLYE KYFLPLQKLL LPSLQAFLVG LLPGLEEGSE IYERTDALLL RLSVVVGREV
     FYAALWGSVL TSPSIRLPAS LFVVNHISRD SPGKEQKCML GTDYQLTVRS LCASLLDANV
     LVQRNNLEII LFFFPFYTCL DPEERAIPLL RRDVVHILSA ATQTLLRRDM SLNRRLYAWL
     LGSDIKGNTI VPKSEISNSY EDQCSYFFDK YSKDLLVEAL AEILHQKFLD ADLEERHHAY
     LKPFRILVSL LDKPEIGPQV VENLFLEVIR AFYSYCHDVL GSDLKLSYTQ SGNPLISTIK
     ENRHASEIVK TVNLLVSSLS SDFLWDYMAR RFEACFRPVT QTTAIGEAIS PPPTVSELCT
     LLVFLLDVIP LELYSEVQTQ YLPQVLGCLL QPLAEEVEAL SLPELTHALK TCFKVLSKVQ
     MPPSYLDLEP SSGNSSPVKG RNSGIAMETE AVVAGDEEPS FPPLKSEDSG IGLSASSPEL
     SEHLRVPRVS AERDDIWKKD GTMQATFLCI QELIANFASK NIFAASLTVS GEENKPEEPP
     GKGNKGQTQS TEHPGRKSSW DPKPITVPQF KQMLSDLFTV RGSPFKTRSS ESLSSVPSSP
     YRKAATEWGV DQVVVELVGS KEDCREALAA ACHLLLDCAT FPVYLSEEET EQLCETLFQT
     PGASDCSFPP WLKSLMTICC CVSDCSLQNI AIATLLEVIN HSQSLALVIE DKMKRYKTSG
     NNPFFGKLQM VTVPPIAPGI LKVIAEKTDF YQRVARVLWN QLNKETREHH ITCVELFYRL
     HCLAPTANIC EDIICHALLD PDKGTRLEAL FRFSVIWHLT REIQGSRVTS HNRSFDRSLF
     VVLDSLACTD GAISAAAQGW LVRALSLGDV ARILEPMLLL LLQPKTQRTS IQCLKQENSA
     EDLHRWFNRK KPTCKEACGE SEPQEGAPEE RLPRGQFTTV DREAIWAEVE KEPEKCPPRS
     DLSEEDLPYY VDLPDRMTSG GGDSSEHTES ADTSSGHTDS ENTSTFSSPS HDLQDLSHEE
     NCCAPIPIGG RAYSKRAALL AAFQPESPRS NARLSLVRAD SDKTQASESF SSDEEADVEL
     QAITTSRLLK QQREKQETVE ALFKHILLYL QPYDSQRVLY AFSVLEAVLK TNPKEFIEAV
     SRTGIDTSST AHLNLISNLL ARHQEALIGQ SFYGKLQTQA PNVCPHSLLI ELLTYLCLSF
     LRSYYPCYLK VCHRDILGNR DVQVKSVEVL IRITAQLVSM AKSAEGKNTE FIHSLLQRCK
     VQEFVLLSLS ASMYTSQKRY GLATADRGGR LLAEDSLFEE SLINLGQDQI WSEHPLQIEL
     LKLLQALIVL EHHLGQGQEE AETQPALSRE WQRALNFQQA IGAMQYVQPH PLTSQGLLVS
     AVVRGLQPAY GYGMHPAWVS LVTHSLPYFG KSLGWTVTPF VIQICKNLDD LVKQYESESV
     KFTISTTSKK ENISPDYPLT LLEGLTTISH FCLLEQPTQH KKTAAVSDPI NLRNAKNAIL
     EELPRIVNTM ALIWNVLRKE ETQKRPVDLL GATKGSSSVY FKTTKTIRQK ILDLLNPLTG
     HLGVQLIAAV ATVWNRKQAR RHSKTKMVPV ANTSQHTLVD LVCALSTLQT DSVLQLVKEV
     VKRPAQIKGD EKSPLVDIPV LQFCYAFIQR LSIPDLQEAF PSLLGVLKEA AQLNLAPPGY
     FLLLSMLNDF VTRTPNLESK KDQKDLQEIT QRILEAVGTI AGSSLEQTSW LSRNLEVKAQ
     PQVSLEESDA EDDVHSAAEA STMVSASAPS VYSVQALSLL AEVLASLLDM VYRSDEKEKA
     VPLISRLLYY VFPYLRNHSA YNAPSFRAGA QLLSSLSGYA YTKRAWKKEV LELFLDPAFF
     QMDTSCVHWK SVIDHLLTHE KTMFKDLMNM QSSSLKLFSS FEQKAMLLKR QAFAVFSGEL
     DQYHLYLPLI QERLTDNLRV GQTSIVAGQM FLFFRVLLLR ISPQHLTSLW PIMVSELIQT
     FIQLEEDLKE EDESRNSHKS NRIKAPVADG NGSAGRVLSP SDLTMYLSAC KFLDTALAFP
     PDKMPLFQIY RWAFVPEVDT EHPAFLSELE ENHQECRPHT VRILELLRSR YGEIGSSDEI
     TRKKEFPLLR QHSVSCIRQL IPFFTTLNCA FKTQSQLPAD VPGTAAPECP VTENPRVLRQ
     LEECVEQDFL EHPEC
//
ID   Q3UHT7_MOUSE            Unreviewed;       977 AA.
AC   Q3UHT7;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 28.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Erc2; Synonyms=D14Ertd171e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK147213; BAE27770.1; -; mRNA.
DR   IPI; IPI00420931; -.
DR   UniGene; Mm.318004; -.
DR   STRING; Q3UHT7; -.
DR   Ensembl; ENSMUST00000100776; ENSMUSP00000098339; ENSMUSG00000040640.
DR   UCSC; uc007stz.1; mouse.
DR   MGI; MGI:1098749; Erc2.
DR   HOVERGEN; HBG051496; -.
DR   ArrayExpress; Q3UHT7; -.
DR   Bgee; Q3UHT7; -.
DR   Genevestigator; Q3UHT7; -.
DR   InterPro; IPR019323; CAZ_cplx_RIM-bd_prot.
DR   Pfam; PF10174; Cast; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   977 AA;  113057 MW;  CF69832DB4B936C9 CRC64;
     MYGSARTISN LEGSPSRSPR LPRSPRLGHR RTSSGGGGGT GKTLSMENIQ SLNAAYATSG
     PMYLSDHEGV ASTTYPKGTM TLGRATNRAV YGGRVTAMGS SPNIASAGLS HTDVLSYTDQ
     HGGLSGSSHH HHHQVPSMLR QVRDSTMLDL QAQLKELQRE NDLLRKELDI KDSKLGSSMN
     SIKTFWSPEL KKERVLRKEE AARMSVLKEQ MRVSHEENQL LDARRTKHLQ LTIQALQDEL
     RTQRDLNHLL QQESGNRGAE HFTIELTEEN FRRLQAEHDR QAKELFLLRK TLEEMELRIE
     TQKQTLNARD ESIKKLLEML QSKGLPSKSL EDDNERTRRM AEAESQVSHL EVILDQKEKE
     NIHLREELHR RSQLQPEPAK TKALQTVIEM KDTKIASLER NIRDLEDEVQ MLKANGVLNT
     EDREEEIKQI EVYKSHSKFM KTKIDQLKQE LSKKESELLA LQTKLETLSN QNSDCKQHIE
     VLKESLTAKE QRAAILQTEV DALRLRLEEK ESFLNKKTKQ LQDLTEEKGT LAGEIRDMKD
     MLEVKERKIN VLQKKIENLQ EQLRDKDKQL TNLKDRVKSL QTDSSNTDTA LATLEEALSE
     KERIIERLKE QRERDDRERL EEIESFRKEN KDLKEKVNAL QAELTEKESS LIDLKEHASS
     LASAGLKRDS KLKSLEIAIE QKKEECNKLE AQLKKQAEQL FNQMYNPAHN IEDDSRMNPE
     FADRLKQLDK EASYYRDECG KAQAEVDRLL EILKEVENEK NDKDKKIAEL ESLTLRHMKD
     QNKKVANLKY NQQLEKKKNA QLLEEVRRRE DSMVDNSQHL QIEELMNALE KTRQELDATK
     ARLASTQQSL AEKEAHLANL RIERRKQLEE ILEMKQEALL AAISEKDANI ALLELSASKK
     KKTQEEVMAL KREKDRLVHQ LKQQTQNRMK LMADNYDEDH HHYHHHHHHH HHRSPGRSQH
     SNHRPSPDQD DEEGIWA
//
ID   K0802_MOUSE             Reviewed;        1945 AA.
AC   Q3UHU5; Q6PAM2; Q80TR7;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=Uncharacterized protein KIAA0802;
GN   Name=Kiaa0802;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1362-1913 (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-741, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3UHU5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UHU5-2; Sequence=VSP_023555;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q3UHU5-3; Sequence=VSP_023556;
CC         Note=No experimental confirmation available;
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DR   EMBL; AK147205; BAE27762.1; -; mRNA.
DR   EMBL; BC060225; AAH60225.1; -; mRNA.
DR   EMBL; AK122373; BAC65655.1; -; mRNA.
DR   IPI; IPI00406086; -.
DR   IPI; IPI00624581; -.
DR   IPI; IPI00761706; -.
DR   RefSeq; NP_001107570.1; NM_001114098.1.
DR   RefSeq; NP_766551.3; NM_172963.4.
DR   UniGene; Mm.33421; -.
DR   UniGene; Mm.456506; -.
DR   ProteinModelPortal; Q3UHU5; -.
DR   PhosphoSite; Q3UHU5; -.
DR   PRIDE; Q3UHU5; -.
DR   Ensembl; ENSMUST00000036760; ENSMUSP00000039075; ENSMUSG00000052105.
DR   Ensembl; ENSMUST00000086693; ENSMUSP00000083899; ENSMUSG00000052105.
DR   Ensembl; ENSMUST00000097291; ENSMUSP00000094894; ENSMUSG00000052105.
DR   Ensembl; ENSMUST00000112716; ENSMUSP00000108336; ENSMUSG00000052105.
DR   GeneID; 68617; -.
DR   KEGG; mmu:68617; -.
DR   UCSC; uc008djv.1; mouse.
DR   MGI; MGI:1915867; 1110012J17Rik.
DR   eggNOG; roNOG08195; -.
DR   GeneTree; ENSGT00530000063889; -.
DR   HOGENOM; HBG716993; -.
DR   HOVERGEN; HBG080205; -.
DR   InParanoid; Q3UHU5; -.
DR   OMA; DLRCQLQ; -.
DR   OrthoDB; EOG4XWFWZ; -.
DR   NextBio; 327568; -.
DR   ArrayExpress; Q3UHU5; -.
DR   Bgee; Q3UHU5; -.
DR   CleanEx; MM_1110012J17RIK; -.
DR   Genevestigator; Q3UHU5; -.
DR   InterPro; IPR021507; DUF3166.
DR   Pfam; PF11365; DUF3166; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Phosphoprotein.
FT   CHAIN         1   1945       Uncharacterized protein KIAA0802.
FT                                /FTId=PRO_0000280114.
FT   COILED      320    396       Potential.
FT   COILED      424    712       Potential.
FT   COILED     1120   1196       Potential.
FT   COILED     1229   1270       Potential.
FT   COMPBIAS     42    174       Pro-rich.
FT   COMPBIAS    848    853       Poly-Gly.
FT   COMPBIAS   1357   1360       Poly-Glu.
FT   MOD_RES      84     84       Phosphoserine (By similarity).
FT   MOD_RES     424    424       Phosphoserine (By similarity).
FT   MOD_RES     541    541       Phosphoserine (By similarity).
FT   MOD_RES     610    610       Phosphoserine (By similarity).
FT   MOD_RES     613    613       Phosphothreonine (By similarity).
FT   MOD_RES     614    614       Phosphoserine (By similarity).
FT   MOD_RES     677    677       Phosphoserine (By similarity).
FT   MOD_RES     741    741       Phosphoserine.
FT   MOD_RES     768    768       Phosphoserine (By similarity).
FT   MOD_RES     897    897       Phosphothreonine (By similarity).
FT   MOD_RES     913    913       Phosphoserine (By similarity).
FT   MOD_RES    1371   1371       Phosphoserine (By similarity).
FT   MOD_RES    1403   1403       Phosphothreonine (By similarity).
FT   MOD_RES    1407   1407       Phosphoserine (By similarity).
FT   MOD_RES    1413   1413       Phosphotyrosine (By similarity).
FT   MOD_RES    1501   1501       Phosphoserine (By similarity).
FT   MOD_RES    1577   1577       Phosphoserine (By similarity).
FT   MOD_RES    1582   1582       Phosphoserine (By similarity).
FT   MOD_RES    1586   1586       Phosphoserine (By similarity).
FT   MOD_RES    1655   1655       Phosphoserine (By similarity).
FT   MOD_RES    1661   1661       Phosphothreonine (By similarity).
FT   MOD_RES    1669   1669       Phosphothreonine (By similarity).
FT   MOD_RES    1673   1673       Phosphoserine (By similarity).
FT   MOD_RES    1675   1675       Phosphoserine (By similarity).
FT   MOD_RES    1677   1677       Phosphoserine (By similarity).
FT   MOD_RES    1799   1799       Phosphoserine (By similarity).
FT   MOD_RES    1801   1801       Phosphoserine (By similarity).
FT   MOD_RES    1917   1917       Phosphothreonine (By similarity).
FT   MOD_RES    1919   1919       Phosphoserine (By similarity).
FT   MOD_RES    1923   1923       Phosphoserine (By similarity).
FT   VAR_SEQ       1    514       Missing (in isoform 2).
FT                                /FTId=VSP_023555.
FT   VAR_SEQ    1882   1945       ELPCSALAPSLEPCFSRPERPANRRLPSRWAPPSPTASQSQ
FT                                SPGHPMSMEEHGEEDPPEEKPHL -> NQTVLLTAPWGL
FT                                (in isoform 3).
FT                                /FTId=VSP_023556.
SQ   SEQUENCE   1945 AA;  213862 MW;  7785C70146349A03 CRC64;
     METLNGPAGG GAPDTKPQPA GQHHRHHHLH PLAERRRLHR APSPARPFLK DLHTRPATAT
     PSAGRAPTPA APRSPSLAGK APPSPGPPAA PGRLSRRSGV VPGAKDKPPP GAGARSAGGA
     KAVPGTRRAA RAGPAEPLSR VGRPTGAEPP PAVAKGRKTK RGPGTPPARA VVPPARASRV
     PAVTLSVTSV AGCRINHTDS SSDLSDCASE PLSDEQRLLP AASSDAESGT GSSDREPIRG
     APTPSSGSRG PPPGSPEPPI LLAAPPVASA CLGGRSSPGG ASTGSPGPGS QEDVGGRAPP
     ERTILGTSKE PSLGEQPRLL VVAEEEELLR EMEELRSEND YLKDELDELR AEMEEMRDSY
     LEEDGYQLQE LRRELDRANK NCRILQYRLR KAEQKSLKVA ETGQVDGELI RSLEQDLKVA
     KDVSVRLHHE LETVEEKRAK AEDDNETLRQ QMIEVEVSRQ ALQNEVERLR ESSLKRRGSR
     EMYKEKKLVN QDDSADLKCQ LQFVKEEASL MRKKMAKLGR EKDELEQELQ KYKSLYGDVD
     SPLPTGEAGG PPSTREAELK LRLKLVEEEA SILGRKIVEL EVENRGLKAE MEDIRVQHER
     EGTGRDHVPS TPTSPFGDSM ESSTELRRHL QFVEEEAELL RRSISEIEDH NRQLTHELSK
     FKFEPHQESG WLGDGVSKGP AASVPLQEEL KSARLQIDEL SGKVLKLQCE NRLLLSNAQR
     GDLAAHLGLR APSPRDSDAE SDAGKKESDG EEGRLPQPKR EGPVGGESDS EDMFEKTSGF
     GSGKPSEASE PCPAELLRVR EDTECLVTIK LEAQRLERTV ERLISDTDGF IHDSGLRGNG
     LASPGVQGGG GEGNSPSEPH LLETINVRMK AFRKELQAFL EQMSRIVDGL SPLSHLTESS
     SFLSTVTSVS RDSPIGTLGK ELGPDLQSKL REQLEWQLNQ DRGDEREGLR LRATRELHRR
     ADGDSGSHHG LGGQSCFNLE MEEDHLYALR WKELEMHSLA LQNTLHKRTW SDEKNLLQQE
     LRSLKQNIFL FYVKLRWLLK HWRQGKQMEE GGEDLEESEH PENVPGLAEL GVQGVHQTDG
     IDQEDADQGC SLPMGEHAPH SLVQISEHGS RLQSSDGGPL NKQVVENQQL FRALKALLED
     FRSELREDEH ARLRLQQQYA SDKAAWDVEW AVLKCRLEQL EEKTEKSLGE LDSSAEGKGA
     LKKEREVHQK LLADSHSLVM DLRWQIHHRE KNWNREKVEL LERLDSERQE WGRQKEELLW
     RVEQLQKEKS PRRSGSFLCS RREDDTRPYP HQGSLHSSRP VSMWPCEDAD SIPFEDRPLS
     KLKESDRCSA SENLYLDALS LDDDPGDPPP LRNCLAEEEE SRKGNLQRAV SVSCMSEFQR
     LMDVSPFLPE KGLPSAGSKE DVTPPLSPDD LKYIEEFHSN DWDYASPRAE ADRPPDPWAD
     RTEMGRVGHE ATTEPCPDPS WYLTTSVTMT TDTMTSPEHC QKQPLRTHVL TEQSGVHVLH
     SPPAIRRVDS IASGGEGRSR ADPEGPFPMS RARGNLADAK GGHPEPVLNR WPCTPPRHPR
     DCVEGSLRPL DRPICPSLGF ASPLNSLDMS KNMSDDMKEV AFSVRNAICA GPAEPHVRDM
     ACQTNGSRTA GTQTIQTISV GLQTEALRAS GVTSSPHKCL TPKAGGGTTP VSSPSRSLRS
     RQVAPAIEKV QAKFERTCCS PKYGSPKLQR KPLSKADQPN SRTSPGIPQK GFSESAWARS
     TTTRESPVHT TINDGLSSLF NIIDHSPIGV RAGSRSRSAE PRQELGPGQE TGTSSRGRSP
     SPLGVGSETF REEGGESTPV RQDLSAPPGY TLTENVARIL NKKLLEHALK EERKQASHGS
     SGLTSDSHTG EPVPAEPGSM EELPCSALAP SLEPCFSRPE RPANRRLPSR WAPPSPTASQ
     SQSPGHPMSM EEHGEEDPPE EKPHL
//
ID   Q3UHU8_MOUSE            Unreviewed;       962 AA.
AC   Q3UHU8;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Gtf2i;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK147201; BAE27759.1; -; mRNA.
DR   IPI; IPI00229538; -.
DR   RefSeq; NP_001074218.1; NM_001080749.1.
DR   UniGene; Mm.261570; -.
DR   UniGene; Mm.412191; -.
DR   ProteinModelPortal; Q3UHU8; -.
DR   SMR; Q3UHU8; 104-197, 319-414, 426-516, 531-609, 691-783, 818-918.
DR   STRING; Q3UHU8; -.
DR   PRIDE; Q3UHU8; -.
DR   Ensembl; ENSMUST00000111260; ENSMUSP00000106891; ENSMUSG00000060261.
DR   GeneID; 14886; -.
DR   KEGG; mmu:14886; -.
DR   UCSC; uc008zvq.1; mouse.
DR   CTD; 14886; -.
DR   MGI; MGI:1202722; Gtf2i.
DR   HOVERGEN; HBG051856; -.
DR   NextBio; 287171; -.
DR   ArrayExpress; Q3UHU8; -.
DR   Bgee; Q3UHU8; -.
DR   Genevestigator; Q3UHU8; -.
DR   InterPro; IPR004212; GTF2I.
DR   InterPro; IPR016659; TF_II-I.
DR   Gene3D; G3DSA:3.90.1460.10; GTF2I; 6.
DR   Pfam; PF02946; GTF2I; 6.
DR   PIRSF; PIRSF016441; TF_II-I; 1.
DR   PROSITE; PS51139; GTF2I; 6.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   962 AA;  108350 MW;  942BB9ACF1F54A9F CRC64;
     MAQVVMSALP AEDEESSESR MVVTFLMSAL ESMCKELAKS KAEVACIAVY ETDVFVVGTE
     RGRAFVNTRK DFQKDFVKYC VEEEEKAAEM HKMKSTTQAN RMSVDAVEIE TLRKTVEDYF
     CFCYGKALGK STVVPVPYEK MLRDQSAVVV QGLPEGVAFK HPEHYDLATL KWILENKAGI
     SFIIKRPFLE PKKHLGGRVL AAEAERSMLS PSGSCGPIKV KTEPTEDSGI SLEMAAVTVK
     EESEDPDYYQ YNIQGSHHSS EGNEGTEVEV PAEDDDYSPP TKRLKSTEPP PPPPVPEPAN
     AGKRKVREFN FEKWNARITD LRKQVEELFE RKYAQAIKAK GPVTIPYPLF QSHVEDLYVE
     GLPEGIPFRR PSTYGIPRLE RILLAKERIR FVIKKHELLN STREDLQLDK PASGVKEEWY
     ARITKLRKMV DQLFCKKFAE ALGSTEAKAV PYQKFEAHPN DLYVEGLPEN IPFRSPSWYG
     IPRLEKIIQV GNRIKFVIKR PELLTHSTTE VTQPRTNTPV KEDWNVRITK LRKQVEEIFN
     LKFAQALGLT EAVKVPYPVF ESNPEFLYVE GLPEGIPFRS PTWFGIPRLE RIVRGSNKIK
     FVVKKPELVV SYLPPGMASK INTKALQSPK RPRSPGSNSK VPEIEVTVEG PNNSSPQTSA
     VRTPTQTNGS NVPFKPRGRE FSFEAWNAKI TDLKQKVENL FNEKCGEALG LKQAVKVPFA
     LFESFPEDFY VEGLPEGVPF RRPSTFGIPR LEKILRNKAK IKFIIKKPEM FETAIKESTS
     SKSPPIFLSG KINSSPNVNT TASGVEDLNI IQVTIPDDDN ERLSKVEKAR QLREQVNDLF
     SRKFGEAIGM GFPVKVPYRK ITINPGCVVV DGMPPGVSFK APSYLEISSM RRILDSAEFI
     KFTVIRPFPG LVINNQLVDQ NESEGPVIQE SAEASQLEVP VTEEIKETDG SSQIKQEPDP
     TW
//
ID   NOL8_MOUSE              Reviewed;        1147 AA.
AC   Q3UHX0; Q059P5; Q504M4; Q8CDJ7; Q9CUR0;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 2.
DT   08-MAR-2011, entry version 47.
DE   RecName: Full=Nucleolar protein 8;
GN   Name=Nol8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic liver, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-716 AND SER-783, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-870 AND SER-872, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1063; SER-1064 AND
RP   SER-1065, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Plays an essential role in the survival of diffuse-type
CC       gastric cancer cells. May be involved in regulation of gene
CC       expression at the post-transcriptional level or in ribosome
CC       biogenesis in cancer cells (By similarity).
CC   -!- SUBUNIT: Interacts with the GTP form of RRAGA, RRAGC and RRAGD.
CC       Interacts with NIP7 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UHX0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UHX0-2; Sequence=VSP_052057;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated (Probable).
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB29660.1; Type=Erroneous initiation;
CC       Sequence=BAC26701.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK029961; BAC26701.1; ALT_INIT; mRNA.
DR   EMBL; AK147172; BAE27736.1; -; mRNA.
DR   EMBL; AK014994; BAB29660.1; ALT_INIT; mRNA.
DR   EMBL; BC094941; AAH94941.1; -; mRNA.
DR   EMBL; BC125575; AAI25576.1; -; mRNA.
DR   EMBL; BC125579; AAI25580.1; -; mRNA.
DR   IPI; IPI00461536; -.
DR   IPI; IPI00670802; -.
DR   UniGene; Mm.258915; -.
DR   ProteinModelPortal; Q3UHX0; -.
DR   SMR; Q3UHX0; 4-88.
DR   STRING; Q3UHX0; -.
DR   PhosphoSite; Q3UHX0; -.
DR   PRIDE; Q3UHX0; -.
DR   Ensembl; ENSMUST00000021824; ENSMUSP00000021824; ENSMUSG00000021392.
DR   MGI; MGI:1918180; Nol8.
DR   GeneTree; ENSGT00390000004860; -.
DR   HOGENOM; HBG445372; -.
DR   HOVERGEN; HBG057565; -.
DR   InParanoid; Q3UHX0; -.
DR   OrthoDB; EOG4VDPXR; -.
DR   ArrayExpress; Q3UHX0; -.
DR   Bgee; Q3UHX0; -.
DR   CleanEx; MM_NOL8; -.
DR   Genevestigator; Q3UHX0; -.
DR   GermOnline; ENSMUSG00000021392; Mus musculus.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Nucleus; Phosphoprotein;
KW   RNA-binding.
FT   CHAIN         1   1147       Nucleolar protein 8.
FT                                /FTId=PRO_0000239444.
FT   DOMAIN        8     89       RRM.
FT   COILED      868    898       Potential.
FT   COILED      937    963       Potential.
FT   COMPBIAS   1093   1096       Poly-Phe.
FT   MOD_RES     298    298       Phosphoserine (By similarity).
FT   MOD_RES     300    300       Phosphoserine (By similarity).
FT   MOD_RES     306    306       Phosphoserine (By similarity).
FT   MOD_RES     364    364       Phosphoserine (By similarity).
FT   MOD_RES     367    367       Phosphothreonine (By similarity).
FT   MOD_RES     662    662       Phosphoserine (By similarity).
FT   MOD_RES     716    716       Phosphoserine.
FT   MOD_RES     783    783       Phosphoserine.
FT   MOD_RES     819    819       Phosphoserine (By similarity).
FT   MOD_RES     820    820       Phosphoserine (By similarity).
FT   MOD_RES     825    825       Phosphoserine (By similarity).
FT   MOD_RES     827    827       Phosphoserine (By similarity).
FT   MOD_RES     870    870       Phosphoserine.
FT   MOD_RES     872    872       Phosphoserine.
FT   MOD_RES    1063   1063       Phosphoserine.
FT   MOD_RES    1064   1064       Phosphoserine.
FT   MOD_RES    1065   1065       Phosphoserine.
FT   MOD_RES    1080   1080       Phosphoserine (By similarity).
FT   VAR_SEQ       1    848       Missing (in isoform 2).
FT                                /FTId=VSP_052057.
FT   CONFLICT    383    383       S -> R (in Ref. 1; BAC26701).
FT   CONFLICT    482    482       D -> G (in Ref. 1; BAE27736).
SQ   SEQUENCE   1147 AA;  128635 MW;  53949DB71021DB38 CRC64;
     MQGNREMKRL FVGGLGQGIS ETDLQNQFGR FGEVSDVEII TRKDDQGNSQ KVFAYVNIQI
     TEADLKKCMS ILNKTKWKGG TLQIQLAKES FLHRLAQERE DAKAKKEKST TGNPTLLEKM
     GAVDFHMKAV PGTEVPGHKN WVVSKFGRVL PVLHLKNQQK HKIMKYDPSK YCHNIKKIPE
     NLTETTPIAE LTWELEGGND PMSKKRRGEF SDFHIPPQKV KKVQKSNDPM ESKVSNIGLR
     TNQVMEKNKS THPVTAHGTA PSTVNPSKQL LVSSSGTQKP KHVVFHNSDF EIIWNKSSMS
     DDDVDSEDEL KMMIAKEENR EKPGHSSVNE SEHDTFEVVR DDFKSNIHKL SSSVSLGNNH
     EYDSSDTDEI IAMKTKNAKV KNSAESSQPE RTVSKKSSFQ KIEPSNDCIK VQGINSNKES
     ALCHGVKFVN PKFPPDSSGS DSEESEEDEE YKVLMENCPR VSLTLADLEQ LAGSHRKFPG
     KDSETNGPQN DSHCKFDTTS KNPKTSGDLY NGRQQCILPE EIVASLLEDE NTYSKQKSEE
     DILKPKFQAF KGIGCLYAKE SVDKTLKENI AFNTGGGHHS SLKHEDHNRS LMENGSKCVN
     GSSSKLTSCQ PAKKVNDPNH IQPPKRQCTF ENQNHKVMSS TSCDKGSTNP LPGPLPLKAK
     TSLHLSANSH KVDSDGDACH WPESRKALEK ERTNLSNLES LEKSSKVSPR EDPQKSPAGF
     SLSDSNASCI NAKDKQAEDN QKRLAALAAW QKAREVQKKL VHSALANLDG HPEDKKTHIV
     FASDNESETE ETSTQEQSCP EKELMKESVS KSPGKLFDSS DDEDSDSKED STRFSIKPQF
     EGRAGQKLMD LQSQFGSDER FRMDSRFLES DSEDEKKELN EDKVNEDELA AEKKKTLNVV
     QSVLNINVNN PTNKGSVAAK KFKDIVHYDP TKHDHAIYER KQEDKEKESK ATRKKKKEEA
     EKLPEVSQDM YYNIAADLKE IFQSMSNTDE KEEDVPRTEA GAREGTGKIR NAETLACEPE
     QTTGFTFSFF DSATKDEKDA TYRIELVKHG KIVCPNDPRF QDSSSEEEDI AEEADHSKPS
     PGEAVPENEA IRFFFFSEND DRLRGSNLFW SGMGGSISRN SWEARTSSLL LECRKKHKEA
     KRKVKAN
//
ID   HAP28_MOUSE             Reviewed;         181 AA.
AC   Q3UHX2; A0JLS1; Q3KQJ5;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=28 kDa heat- and acid-stable phosphoprotein;
DE   AltName: Full=PDGF-associated protein;
DE            Short=PAP;
DE   AltName: Full=PDGFA-associated protein 1;
DE            Short=PAP1;
GN   Name=Pdap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-181.
RC   STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND SER-63, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-60 AND SER-63,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-60 AND SER-63,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-63, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-63, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-63 AND TYR-70,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- PTM: Phosphorylated by several kinases in vitro. In vivo, can be
CC       phosphorylated by CK2.
CC   -!- SIMILARITY: Belongs to the PDAP1 family.
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DR   EMBL; AK147170; BAE27734.1; -; mRNA.
DR   EMBL; BC007162; AAH07162.1; -; mRNA.
DR   EMBL; BC106168; AAI06169.1; -; mRNA.
DR   IPI; IPI00352475; -.
DR   RefSeq; NP_001028485.1; NM_001033313.3.
DR   UniGene; Mm.188851; -.
DR   STRING; Q3UHX2; -.
DR   PhosphoSite; Q3UHX2; -.
DR   PRIDE; Q3UHX2; -.
DR   Ensembl; ENSMUST00000031627; ENSMUSP00000031627; ENSMUSG00000029623.
DR   GeneID; 231887; -.
DR   KEGG; mmu:231887; -.
DR   UCSC; uc009ame.1; mouse.
DR   CTD; 231887; -.
DR   MGI; MGI:2448536; Pdap1.
DR   eggNOG; roNOG17603; -.
DR   GeneTree; ENSGT00390000018509; -.
DR   HOGENOM; HBG316925; -.
DR   HOVERGEN; HBG000319; -.
DR   InParanoid; Q3UHX2; -.
DR   OMA; GRVRQYT; -.
DR   OrthoDB; EOG480HZ9; -.
DR   PhylomeDB; Q3UHX2; -.
DR   NextBio; 380851; -.
DR   ArrayExpress; Q3UHX2; -.
DR   Bgee; Q3UHX2; -.
DR   CleanEx; MM_PDAP1; -.
DR   Genevestigator; Q3UHX2; -.
DR   GermOnline; ENSMUSG00000029623; Mus musculus.
DR   InterPro; IPR019380; Casein_kinase_sb_PP28.
DR   Pfam; PF10252; PP28; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein.
FT   CHAIN         1    181       28 kDa heat- and acid-stable
FT                                phosphoprotein.
FT                                /FTId=PRO_0000083898.
FT   MOD_RES      17     17       Phosphotyrosine (By similarity).
FT   MOD_RES      19     19       Phosphoserine (By similarity).
FT   MOD_RES      48     48       Phosphoserine.
FT   MOD_RES      57     57       Phosphoserine.
FT   MOD_RES      60     60       Phosphoserine.
FT   MOD_RES      63     63       Phosphoserine.
FT   MOD_RES      70     70       Phosphotyrosine.
FT   MOD_RES     132    132       N6-acetyllysine (By similarity).
FT   MOD_RES     176    176       Phosphoserine (By similarity).
SQ   SEQUENCE   181 AA;  20605 MW;  C9A74B7C41174F87 CRC64;
     MPKGGRKGGH KGRVRQYTSP EEIDAQLQAE KQKANEEDEQ EEGGDGASGD PKKEKKSLDS
     DESEDEDDDY QQKRKGVEGL IDIENPNRVA QTTKKVTQLD LDGPKELSRR EREEIEKQKA
     KERYMKMHLA GKTEQAKADL ARLAIIRKQR EEAARKKEEE RKAKDDATLS GKRMQSLSLN
     K
//
ID   Q3UI39_MOUSE            Unreviewed;       838 AA.
AC   Q3UI39;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-FEB-2011, entry version 43.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Snap91;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 ENTH (epsin N-terminal homology) domain.
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DR   EMBL; AK147087; BAE27667.1; -; mRNA.
DR   IPI; IPI00653617; -.
DR   UniGene; Mm.281651; -.
DR   UniGene; Mm.472993; -.
DR   ProteinModelPortal; Q3UI39; -.
DR   SMR; Q3UI39; 19-281.
DR   STRING; Q3UI39; -.
DR   PRIDE; Q3UI39; -.
DR   Ensembl; ENSMUST00000098495; ENSMUSP00000096096; ENSMUSG00000033419.
DR   MGI; MGI:109132; Snap91.
DR   GeneTree; ENSGT00390000008805; -.
DR   HOVERGEN; HBG049391; -.
DR   ArrayExpress; Q3UI39; -.
DR   Bgee; Q3UI39; -.
DR   Genevestigator; Q3UI39; -.
DR   GO; GO:0030118; C:clathrin coat; IEA:InterPro.
DR   GO; GO:0030276; F:clathrin binding; IEA:InterPro.
DR   GO; GO:0005545; F:1-phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0048268; P:clathrin coat assembly; IEA:InterPro.
DR   InterPro; IPR011417; ANTH.
DR   InterPro; IPR014712; Clathrin_Pinositid-bd_GAT-like.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR013809; Epsin-like_N.
DR   Gene3D; G3DSA:1.25.40.90; ENTH_VHS; 1.
DR   Gene3D; G3DSA:1.20.58.150; Pinositid-bd_clathrin_GAT-like; 1.
DR   Pfam; PF07651; ANTH; 1.
DR   SMART; SM00273; ENTH; 1.
DR   SUPFAM; SSF48464; ENTH_VHS; 1.
DR   PROSITE; PS50942; ENTH; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   838 AA;  86066 MW;  C387BA5CEFA24499 CRC64;
     MSGQTLTDRI AAAQYSVTGS AVARAVCKAT THEVMGPKKK HLDYLIQATN ETNVNIPQMA
     DTLFERATNS SWVVVFKALV TTHHLMVHGN ERFIQYLASR NTLFNLSNFL DKSGSHGYDM
     STFIRRYSRY LNEKAFSYRQ MAFDFARVKK GADGVMRTMV PEKLLKSMPI LQGQIDALLE
     FDVHPNELTN GVINAAFMLL FKDLIKLFAC YNDGVINLLE KFFEMKKGQC KDALEIYKRF
     LTRMTRVSEF LKVAEQVGID KGDIPDLTQA PSSLMETLEQ HLNTLEGKKP GNKSGAPSPL
     SKSPPATTVT SPNSTPAKTI DTSPPVDIFA TASAAAPVSS AKPSSDLLDL QPDFSGAAAG
     AAAPVVPPSG GATAWGDSLA ALSSVPCEAP ISDPFAPEPS PPTTTTEPAS ASASTTTAVT
     AVTTEVDLFG DAFAASPGEA PAASEGATAP ATPAPVAAAL DACSGNDPFA PSEGSAEAAP
     ELDLFAMKPP ETSAPVVTPT ASTAPPVPAT APSPAPTAVA ATAATTTAAA AATTTATTSA
     AAATTAAAPP ALDIFGDLFD SAPEVAAAPK PDAAPSIDLF GTDAFSSPPR GASPVPESSL
     TADLLSVDAF AAPSPASTAS PAKAESSGVI DLFGGFGGSF MAPSTTPVTP AQNNLLQPSF
     EAAFGTTPST SSSSSFDPSV FDGLGDLLMP TMAPSGQPAP VSMVPPSPAM AASKGLGSDL
     DSSLASLVGN LGISGTTSKK GDLQWNAGEK KLTGGANWQP KVTPATWSAG VPPPPSGTGM
     TMMSQQPVMF AQPMMRPPFG AAAVPGTQLS PSPTPATQSP KKPPAKDPLA DLNIKDFL
//
ID   RHG17_MOUSE             Reviewed;         846 AA.
AC   Q3UIA2; Q3UDP7; Q8BGD1; Q99LH3; Q99N39; Q99N40;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Rho GTPase-activating protein 17;
DE   AltName: Full=Neuron-associated developmentally-regulated protein;
DE            Short=Nadrin;
DE   AltName: Full=Rho-type GTPase-activating protein 17;
GN   Name=Arhgap17;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   MEDLINE=20538431; PubMed=10967100; DOI=10.1074/jbc.M004069200;
RA   Harada A., Furuta B., Takeuchi K., Itakura M., Takahashi M., Umeda M.;
RT   "Nadrin, a novel neuron-specific GTPase-activating protein involved in
RT   regulated exocytosis.";
RL   J. Biol. Chem. 275:36885-36891(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Bone, Bone marrow, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Rho GTPase-activating protein involved in the
CC       maintenance of tight junction by regulating the activity of CDC42,
CC       thereby playing a central role in apical polarity of epithelial
CC       cells. Specifically acts as a GTPase activator for the CDC42
CC       GTPase by converting it to an inactive GDP-bound state. The
CC       complex formed with AMOT acts by regulating the uptake of polarity
CC       proteins at tight junctions, possibly by deciding whether tight
CC       junction transmembrane proteins are recycled back to the plasma
CC       membrane or sent elsewhere. Participates in the Ca(2+)-dependent
CC       regulation of exocytosis, possibly by catalyzing GTPase activity
CC       of Rho family proteins and by inducing the reorganization of the
CC       cortical actin filaments. Acts as a GTPase activitor in vitro for
CC       RAC1 (By similarity).
CC   -!- SUBUNIT: Component of a complex whose core is composed of
CC       ARHGAP17, AMOT, MPP5/PALS1, INADL/PATJ and PARD3/PAR3. Interacts
CC       with SLC9A3R1, FNBP1, TRIP10, CAPZA (CAPZA1, CAPZA2 or CAPZA3),
CC       CAPZB, CD2AP and SH3KBP1/CIN85 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC       similarity). Cytoplasm (By similarity). Cell junction, tight
CC       junction (By similarity). Note=Associates with membranes and
CC       concentrates at sites of cell-cell contact (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=Nadrin-1;
CC         IsoId=Q3UIA2-1; Sequence=Displayed;
CC       Name=2; Synonyms=Nadrin-2;
CC         IsoId=Q3UIA2-2; Sequence=VSP_023690;
CC       Name=3;
CC         IsoId=Q3UIA2-3; Sequence=VSP_023690, VSP_023691;
CC       Name=4;
CC         IsoId=Q3UIA2-4; Sequence=VSP_023690, VSP_023692;
CC   -!- DOMAIN: The BAR domain mediates the interaction with the coiled
CC       coil domain of AMOT, leading to its recruitment to tight junctions
CC       (By similarity).
CC   -!- SIMILARITY: Contains 1 BAR domain.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB060553; BAB43862.1; -; mRNA.
DR   EMBL; AB060554; BAB43863.1; -; mRNA.
DR   EMBL; AK036468; BAC29443.1; -; mRNA.
DR   EMBL; AK036617; BAC29508.1; -; mRNA.
DR   EMBL; AK147010; BAE27604.1; -; mRNA.
DR   EMBL; AK149986; BAE29214.1; -; mRNA.
DR   EMBL; AK152266; BAE31084.1; -; mRNA.
DR   EMBL; BC003259; AAH03259.1; -; mRNA.
DR   IPI; IPI00320905; -.
DR   IPI; IPI00408189; -.
DR   IPI; IPI00830381; -.
DR   IPI; IPI00830672; -.
DR   RefSeq; NP_001116112.1; NM_001122640.1.
DR   RefSeq; NP_001116113.1; NM_001122641.1.
DR   RefSeq; NP_001116114.1; NM_001122642.1.
DR   RefSeq; NP_001116115.1; NM_001122643.1.
DR   RefSeq; NP_653112.2; NM_144529.2.
DR   UniGene; Mm.403318; -.
DR   ProteinModelPortal; Q3UIA2; -.
DR   SMR; Q3UIA2; 4-444.
DR   STRING; Q3UIA2; -.
DR   PhosphoSite; Q3UIA2; -.
DR   PRIDE; Q3UIA2; -.
DR   Ensembl; ENSMUST00000098060; ENSMUSP00000095668; ENSMUSG00000030766.
DR   Ensembl; ENSMUST00000106442; ENSMUSP00000102050; ENSMUSG00000030766.
DR   GeneID; 70497; -.
DR   KEGG; mmu:70497; -.
DR   NMPDR; fig|10090.3.peg.17590; -.
DR   UCSC; uc009jpi.1; mouse.
DR   CTD; 70497; -.
DR   MGI; MGI:1917747; Arhgap17.
DR   eggNOG; roNOG10358; -.
DR   GeneTree; ENSGT00600000084016; -.
DR   HOGENOM; HBG446214; -.
DR   HOVERGEN; HBG000015; -.
DR   InParanoid; Q3UIA2; -.
DR   OrthoDB; EOG4GB75X; -.
DR   PhylomeDB; Q3UIA2; -.
DR   NextBio; 331751; -.
DR   ArrayExpress; Q3UIA2; -.
DR   Bgee; Q3UIA2; -.
DR   CleanEx; MM_ARHGAP17; -.
DR   Genevestigator; Q3UIA2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR004148; BAR.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF03114; BAR; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00721; BAR; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS51021; BAR; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell junction; Cytoplasm;
KW   GTPase activation; Membrane; Phosphoprotein; SH3-binding;
KW   Tight junction.
FT   CHAIN         1    846       Rho GTPase-activating protein 17.
FT                                /FTId=PRO_0000280463.
FT   DOMAIN       14    246       BAR.
FT   DOMAIN      252    442       Rho-GAP.
FT   MOTIF       730    743       SH3-binding (Potential).
FT   COMPBIAS    636    782       Pro-rich.
FT   COMPBIAS    674    690       Poly-Gln.
FT   MOD_RES     161    161       Phosphoserine.
FT   MOD_RES     295    295       N6-acetyllysine (By similarity).
FT   MOD_RES     575    575       Phosphoserine (By similarity).
FT   VAR_SEQ     497    574       Missing (in isoform 2, isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_023690.
FT   VAR_SEQ     805    846       TNSRVSESLRSIFPEIHSDLASKEVPGHILLDIDNDTESTA
FT                                L -> ALPGALTGGEGFQN (in isoform 3).
FT                                /FTId=VSP_023691.
FT   VAR_SEQ     805    846       TNSRVSESLRSIFPEIHSDLASKEVPGHILLDIDNDTESTA
FT                                L -> V (in isoform 4).
FT                                /FTId=VSP_023692.
FT   CONFLICT    207    207       E -> K (in Ref. 1; BAB43862/BAB43863).
FT   CONFLICT    250    250       F -> I (in Ref. 2; BAE29214).
FT   CONFLICT    593    593       N -> D (in Ref. 1; BAB43862/BAB43863).
FT   CONFLICT    674    676       Missing (in Ref. 3; AAH03259).
SQ   SEQUENCE   846 AA;  92202 MW;  3D12B030B41E6987 CRC64;
     MKKQFNRMKQ LANQTVGRAE KTEVLSEDLL QIERRLDTVR SMCHHSHKRL IACFQGQHGT
     DAERRHKKLP LTALAQNMQE ASAQLEESLL GKMLETCGDA ENQLALELSQ HEVFVEKEIM
     DPLYGIAEVE IPNIQKQRKQ LARLVLDWDS VRARWNQAHK SSGTNFQGLP SKIDTLKEEM
     DEAGNKVEQC KDQLAADMYN FMAKEGEYGK FFVTLLEAQA DYHRKALAVL EKALPEMRAH
     QDKWAEKPAF GTPLEEHLKR SGREIALPIE ACVMLLLETG MKEEGLFRIG AGASKLKKLK
     AALDCSTSHL DEFYSDPHAV AGALKSYLRE LPEPLMTFSL YEEWTQVASV QDQDKKLQYL
     WTTCQKLPPQ NFVNFRYLIK FLAKLAQTSD VNKMTPSNIA IVLGPNLLWA KQEGTLAEIA
     AATSVHVVAV IEPIIQHADW FFPGEVEFNV SEAFVPLATP NSNHSSHTGN DSDSGTLERK
     RPASMAVMEG DLVKKESFGV KLMDFQAHRR GGTLNRKHIA PAFQPPLPPT DGNALAPAGP
     EPPSQSSRAD SSSGGGPVFS STGILEQGLS PGDSSPPKPK DSVSAAVPAA GRNSNQMTTV
     PNQAQTGGNS HQLSVSTPHS AAGPSPHTLR RAVKKPAPAP PKPGNLPPGH PGGQSSPGTG
     TSPKPSARSP SPPQQQQQQQ QQQQQQQQQQ TPGMRRCSSS LPPIQAPSHP PPQPPTQPRL
     GEQGPEPGPT PPQTPTPPST PPLAKQNPSQ SETTQLHGTL PRPRPVPKPR NRPSVPPPPH
     PPGTHTVDGG LTSSVPTASR IVTDTNSRVS ESLRSIFPEI HSDLASKEVP GHILLDIDND
     TESTAL
//
ID   Q3UID0_MOUSE            Unreviewed;      1130 AA.
AC   Q3UID0;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-FEB-2011, entry version 45.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Smarcc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK146971; BAE27576.1; -; mRNA.
DR   IPI; IPI00651846; -.
DR   RefSeq; NP_001107568.1; NM_001114096.1.
DR   UniGene; Mm.417338; -.
DR   ProteinModelPortal; Q3UID0; -.
DR   SMR; Q3UID0; 414-517, 620-685.
DR   STRING; Q3UID0; -.
DR   PRIDE; Q3UID0; -.
DR   Ensembl; ENSMUST00000099131; ENSMUSP00000096734; ENSMUSG00000025369.
DR   GeneID; 68094; -.
DR   KEGG; mmu:68094; -.
DR   UCSC; uc007hmy.1; mouse.
DR   CTD; 68094; -.
DR   MGI; MGI:1915344; Smarcc2.
DR   eggNOG; roNOG08421; -.
DR   GeneTree; ENSGT00390000018166; -.
DR   HOVERGEN; HBG054849; -.
DR   PhylomeDB; Q3UID0; -.
DR   NextBio; 326404; -.
DR   ArrayExpress; Q3UID0; -.
DR   Bgee; Q3UID0; -.
DR   Genevestigator; Q3UID0; -.
DR   GO; GO:0000785; C:chromatin; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0006333; P:chromatin assembly or disassembly; IEA:InterPro.
DR   GO; GO:0045449; P:regulation of transcription; IEA:InterPro.
DR   InterPro; IPR001357; BRCT.
DR   InterPro; IPR000953; Chromodomain.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR014778; Myb_DNA-bd.
DR   InterPro; IPR001005; SANT_DNA-bd.
DR   InterPro; IPR017884; SANT_eukarya.
DR   InterPro; IPR007526; SWIRM.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF00249; Myb_DNA-binding; 1.
DR   Pfam; PF04433; SWIRM; 1.
DR   SMART; SM00298; CHROMO; 1.
DR   SMART; SM00717; SANT; 1.
DR   SUPFAM; SSF52113; BRCT; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 2.
DR   PROSITE; PS51293; SANT; 1.
DR   PROSITE; PS50934; SWIRM; 1.
PE   2: Evidence at transcript level;
KW   Nucleus.
SQ   SEQUENCE   1130 AA;  124677 MW;  6AE80F4EE72AA257 CRC64;
     MAVRKKDGGP NVKYYEAADT VTQFDNVRLW LGKNYKKYIQ AEPPTNKSLS SLVVQLLQFQ
     EEVFGKHVSN APLTKLPIKC FLDFKAGGSL CHILAAAYKF KSDQGWRRYD FQNPSRMDRN
     VEMFMTIEKS LVQNNCLSRP NIFLCPEIEP KLLGKLKDIV KRHQGTISED KSNASHVVYP
     VPGNLEEEEW VRPVMKRDKQ VLLHWGYYPD SYDTWIPASE IEASVEDAPT PEKPRKVHAK
     WILDTDTFNE WMNEEDYEVS DDKSPVSRRK KISAKTLTDE VNSPDSDRRD KKGGNYKKRK
     RSPSPSPTPE AKKKNAKKGP STPYTKSKRG HREEEQEDLT KDMDEPSPVP NVEEVTLPKT
     VNTKKDSESA PVKGGTMTDL DEQDDESMET TGKDEDENST GNKGEQTKNP DLHEDNVTEQ
     THHIIIPSYA AWFDYNSVHA IERRALPEFF NGKNKSKTPE IYLAYRNFMI DTYRLNPQEY
     LTSTACRRNL AGDVCAIMRV HAFLEQWGLI NYQVDAESRP TPMGPPPTSH FHVLADTPSG
     LVPLQPKPPQ GRQVDADTKA GRKGKELDDL VPETAKGKPE LQSSASQQML NFPEKGKEKP
     ADMQNFGLRT DMYTKKNVPS KSKAAASATR EWTEQETLLL LEALEMYKDD WNKVSEHVGS
     RTQDECILHF LRLPIEDPYL EDSEASLGPL AYQPIPFSQS GNPVMSTVAF LASVVDPRVA
     SAAAKSALEE FSKMKEEVPT ALVEAHVRKV EEAAKVTGKA DPAFGLESSG IAGTASDEPE
     RIEESGTEEA RPEGQAADEK KEPKEPREGG GAVEEEAKEE ISEVPKKDEE KGKEGDSEKE
     SEKSDGDPIV DPEKDKEPTE GQEEVLKEVA EPEGERKTKV ERDIGEGNLS TAAAAALAAA
     AVKAKHLAAV EERKIKSLVA LLVETQMKKL EIKLRHFEEL ETIMDREREA LEYQRQQLLA
     DRQAFHMEQL KYAEMRARQQ HFQQMHQQQQ QQPPTLPPGS QPIPPTGAAG PPTVHGLAVP
     PAAVASAPPG SGAPPGSLGP SEQIGQAGTT AGPQQPQQAG APQPGAVPPG VPPPGPHGPS
     PFPNQPTPPS MMPGAVPGSG HPGVADPGTP LPPDPTAPSP GTVTPVPPPQ
//
ID   PKHA7_MOUSE             Reviewed;        1118 AA.
AC   Q3UIL6; B6RSP2; B6RSP3; Q3TUE4; Q5XG70; Q8BYE3;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=Pleckstrin homology domain-containing family A member 7;
DE            Short=PH domain-containing family A member 7;
DE   AltName: Full=Heart adapter protein 1;
GN   Name=Plekha7; Synonyms=Hadp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 6).
RC   STRAIN=C57BL/6;
RA   Wythe J.D., Urness L.D., Jones C.A., Jurynec M., Grunwald D.J.,
RA   MacRae C.A., Li D.Y.;
RT   "HADP1, a novel pleckstrin homology domain protein, is required for
RT   cardiac contractility in zebrafish.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Head, Stomach, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-542 AND SER-609, AND
RP   MASS SPECTROMETRY.
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-364; SER-533; SER-542;
RP   SER-900 AND SER-904, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Required for zonula adherens biogenesis and maintenance.
CC       Acts via its interaction with KIAA1543/Nezha, which anchors
CC       microtubules at their minus-ends to zonula adherens, leading to
CC       recruit KIFC3 kinesin to junctional site (By similarity).
CC   -!- SUBUNIT: Interacts with KIAA1543/Nezha and CTNND1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, adherens junction (By
CC       similarity). Cytoplasm, cytoskeleton, centrosome (By similarity).
CC       Note=Localizes to zonula adherens, recruited via its interaction
CC       with CTNND1 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q3UIL6-1; Sequence=Displayed;
CC       Name=2; Synonyms=HADP1a;
CC         IsoId=Q3UIL6-2; Sequence=VSP_025596;
CC       Name=3;
CC         IsoId=Q3UIL6-3; Sequence=VSP_025595;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q3UIL6-4; Sequence=VSP_025593, VSP_025596;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q3UIL6-5; Sequence=VSP_025594;
CC         Note=No experimental confirmation available;
CC       Name=6; Synonyms=HADP1b;
CC         IsoId=Q3UIL6-6; Sequence=VSP_039544, VSP_025596;
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 2 WW domains.
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DR   EMBL; EU380771; ACB38003.1; -; mRNA.
DR   EMBL; EU380772; ACB38004.1; -; mRNA.
DR   EMBL; AK040271; BAC30557.1; -; mRNA.
DR   EMBL; AK146866; BAE27490.1; -; mRNA.
DR   EMBL; AK160810; BAE36027.1; -; mRNA.
DR   EMBL; BC084587; AAH84587.1; -; mRNA.
DR   IPI; IPI00624550; -.
DR   IPI; IPI00845648; -.
DR   IPI; IPI00845725; -.
DR   IPI; IPI00845781; -.
DR   IPI; IPI00845848; -.
DR   IPI; IPI00968912; -.
DR   RefSeq; NP_766331.1; NM_172743.2.
DR   UniGene; Mm.3741; -.
DR   HSSP; Q8CFI0; 1WR7.
DR   ProteinModelPortal; Q3UIL6; -.
DR   SMR; Q3UIL6; 2-87, 156-281.
DR   STRING; Q3UIL6; -.
DR   PRIDE; Q3UIL6; -.
DR   Ensembl; ENSMUST00000084664; ENSMUSP00000081714; ENSMUSG00000045659.
DR   Ensembl; ENSMUST00000106605; ENSMUSP00000102216; ENSMUSG00000045659.
DR   GeneID; 233765; -.
DR   KEGG; mmu:233765; -.
DR   UCSC; uc009jiz.1; mouse.
DR   CTD; 233765; -.
DR   MGI; MGI:2445094; Plekha7.
DR   eggNOG; roNOG10260; -.
DR   GeneTree; ENSGT00530000063012; -.
DR   HOVERGEN; HBG108254; -.
DR   InParanoid; Q3UIL6; -.
DR   OMA; YSPAEED; -.
DR   OrthoDB; EOG4Z0B4V; -.
DR   NextBio; 381815; -.
DR   ArrayExpress; Q3UIL6; -.
DR   Bgee; Q3UIL6; -.
DR   Genevestigator; Q3UIL6; -.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005915; C:zonula adherens; ISS:UniProtKB.
DR   GO; GO:0070097; F:delta-catenin binding; ISS:UniProtKB.
DR   GO; GO:0090136; P:epithelial cell-cell adhesion; ISS:UniProtKB.
DR   GO; GO:0045218; P:zonula adherens maintenance; ISS:UniProtKB.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF51045; WW_Rsp5_WWP; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Phosphoprotein; Repeat.
FT   CHAIN         1   1118       Pleckstrin homology domain-containing
FT                                family A member 7.
FT                                /FTId=PRO_0000287693.
FT   DOMAIN        8     41       WW 1.
FT   DOMAIN       53     86       WW 2.
FT   DOMAIN      163    281       PH.
FT   REGION      535    693       Interaction with CTNND1 (By similarity).
FT   COILED      697    798       Potential.
FT   COILED     1064   1091       Potential.
FT   COMPBIAS    564    596       Pro-rich.
FT   COMPBIAS    842    939       Pro-rich.
FT   MOD_RES     364    364       Phosphotyrosine.
FT   MOD_RES     533    533       Phosphoserine.
FT   MOD_RES     542    542       Phosphoserine.
FT   MOD_RES     601    601       Phosphoserine (By similarity).
FT   MOD_RES     609    609       Phosphoserine.
FT   MOD_RES     900    900       Phosphoserine.
FT   MOD_RES     904    904       Phosphoserine.
FT   MOD_RES     906    906       Phosphothreonine (By similarity).
FT   VAR_SEQ       1    236       Missing (in isoform 4).
FT                                /FTId=VSP_025593.
FT   VAR_SEQ       1    177       Missing (in isoform 5).
FT                                /FTId=VSP_025594.
FT   VAR_SEQ       1    105       Missing (in isoform 3).
FT                                /FTId=VSP_025595.
FT   VAR_SEQ       1     73       MAAAVGRDTLPEHWSYGVCRDGRVFFINDQLRCTTWLHPRT
FT                                GEPVNSGHMIRSDLPRGWEEGFTEEGASFFID -> MEPWR
FT                                CPPRDARPAALGFWGEPLAVCS (in isoform 6).
FT                                /FTId=VSP_039544.
FT   VAR_SEQ    1116   1118       SVC -> SWKREQEFDLQLLERAAQGDRKDKEEGWLKVQAT
FT                                PVMELDLEPQDYDLDISRELSKPEKVSIPERYVELDPEEPP
FT                                SLEELQARYQKAEKIRNILARSSMCNLQPLGQDRNSLADLD
FT                                SQLQEQERIINISYALASEASKRSKQVAAQAITDP (in
FT                                isoform 2, isoform 4 and isoform 6).
FT                                /FTId=VSP_025596.
SQ   SEQUENCE   1118 AA;  126742 MW;  6CCCE91B582ED368 CRC64;
     MAAAVGRDTL PEHWSYGVCR DGRVFFINDQ LRCTTWLHPR TGEPVNSGHM IRSDLPRGWE
     EGFTEEGASF FIDHNQQTTT FRHPVTGQFS SENSEYVLRE EPHPHMSKPE RNQRPSSMVS
     ETSTAGTTST LEAKPGPKIV KSSSKVHSFG KRDQAIRRNL NVPVVVRGWL HKQDSSGMRL
     WKRRWFVLAD YCLFYYKDSR EEAVLGSIPL PSYVISPVAP EDRISRKYSF KAVHTGMRAL
     IYSTTTAGSQ MEHSGMRTYY FSADTLEDMN AWVRAMNQAA QVLSRSSLRR DVDKVERQAM
     PQANHTDACQ ECGHVGPGHS RDCPRRGYED SYGFNRREQE EERFRAQRDP LEGRRDRSKA
     RSPYLPAEED ALFVDLPGGP RGQQAQPQRA EKNGVPPYGL GEQNGTNGYQ RTAPPRANPE
     KHSQRKTGLA QAEHWTKAQK GDGRSLPLDQ TLPRQGPSQP LSFPENYQSL PKSTRHLSGS
     SSPPPRNLPS DYKYAQDRAS HLKMSSEERR AHRDGTVWQL YEWQQRQQFR HGSPTAPIGA
     GSPEFTEQGR SRSLLEVPRS ISVPPSPSDI PPPGPPRPFP PRRPHTPAER VTVKPPEQRR
     SVDISLGGSP RKARGHAAKN SSHVDRRSMP SMGYMTHTVS APSLHGKSAD DTYLQLKKDL
     EYLDLKMTGR DLLKDRSLKP MKIAESDIDV KLSIFCEQDR ILQDLEDKIR ALKENKDQLE
     SVLEVLHRQT EQYRDQPQHL EKITCQQRLL QEDLVHIRAE LCRESTEMEN AWNEYLKLEK
     DVEQLKQTLQ EQHRRAFFFQ EKSQIQKDLW RIEDVMAGLS ANKENYRVLV GSVKNPERKT
     VPLFPHPSVP SLSPTESKPA LQPSPPTSPV RTPLEVRLFP QLQTYVPYRP HPPQLRKVMS
     PLQSPTKAKP QAEDEAPPRP PLPELYSPED QPPAVPPLPR EATIIRHTSV RGLKRQSDER
     KRDREQGQCV NGDLKVELRS YVSEPELASL SGDVPQPSLS LVGSESRYQT LPGRGLSGST
     SRLQQSSTIA PYVTLRRGLN AENSSATFSR PKSALERLYS GDHQRGKMSA EEQLERMKRH
     QKALVRERKR TLSQGEKTGL LSARYLSQPL PGDLGSVC
//
ID   Q3UIS9_MOUSE            Unreviewed;       907 AA.
AC   Q3UIS9;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   11-JAN-2011, entry version 50.
DE   SubName: Full=Epidermal growth factor receptor pathway substrate 15-like 1;
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Eps15l1; ORFNames=mCG_18932;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK146781; BAE27427.1; -; mRNA.
DR   EMBL; CH466525; EDL10796.1; -; Genomic_DNA.
DR   IPI; IPI00890139; -.
DR   RefSeq; NP_031970.2; NM_007944.3.
DR   UniGene; Mm.288894; -.
DR   ProteinModelPortal; Q3UIS9; -.
DR   SMR; Q3UIS9; 11-105, 121-214, 267-360.
DR   STRING; Q3UIS9; -.
DR   PRIDE; Q3UIS9; -.
DR   Ensembl; ENSMUST00000006439; ENSMUSP00000006439; ENSMUSG00000006276.
DR   GeneID; 13859; -.
DR   KEGG; mmu:13859; -.
DR   NMPDR; fig|10090.3.peg.18754; -.
DR   UCSC; uc009mfr.1; mouse.
DR   CTD; 13859; -.
DR   MGI; MGI:104582; Eps15l1.
DR   HOVERGEN; HBG005591; -.
DR   InParanoid; Q3UIS9; -.
DR   PhylomeDB; Q3UIS9; -.
DR   NextBio; 284738; -.
DR   ArrayExpress; Q3UIS9; -.
DR   Bgee; Q3UIS9; -.
DR   Genevestigator; Q3UIS9; -.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR000261; EPS15_homology.
DR   InterPro; IPR003903; Ubiquitin-int_motif.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 3.
DR   SMART; SM00054; EFh; 3.
DR   SMART; SM00027; EH; 3.
DR   SMART; SM00726; UIM; 2.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 4.
DR   PROSITE; PS50031; EH; 3.
DR   PROSITE; PS50330; UIM; 2.
PE   2: Evidence at transcript level;
KW   Receptor.
SQ   SEQUENCE   907 AA;  99309 MW;  B5AF1A89B445E8A7 CRC64;
     MAAPLVPLSQ QIPGGNPLYE SYYKQVDPAY TGRVGASEAA LFLKKSGLSD IILGKIWDLA
     DPEGKGFLDK QGFYVALRLV ACAQSGHEVT LSSLSLTMPP PKFHDTSSPL MATQSSAETH
     WAVRVEEKAK FDGIFESLLP VNGLLSGDKV KPVLMNSKLP LDVLGRVWDL SDIDKDGHLD
     RDEFAVAMHL VYRALEKEPV PSILPPPLIP PSKRKKTVFA GAVPVLPASP PPKDSLRSTP
     SHGSVSSLNS TGSLSPKHSV KQPPVAWVVP VADKMRFDEI FLKTDLDLDG YVSGQEVKEI
     FMHSGLTQNL LAHIWALADT RQTGKLSKEQ FALAMYFIQQ KVSKGIDPPQ VLSPDMVPPS
     ERGTPIPDSS STLASGEFTG VKELDDISQE IAQLQREKYS LEQDIREKEE AIRQKTSEVQ
     ELQNDLDRET SSLQELEAQK QDAQDRLDEM DQQKAKLRDM LSDVRQKCQD ETQTISSLKT
     QIQSQESDLK SQEDDLNRAK SELNRLQQEE TQLEQSIQAG RAQLETILRS LKCTQDDINQ
     ARSKLSQLQE SHLEAHRSLE QYDQVPDGVS GTSLPDLATL NEGILLAERG GFGAMDDPFK
     NKALLFSNNS QELHPDPFQA EDPFKSDPFK GADPFKGDPF QSDPFSEQQT AATDPFGGDP
     FKESDPFHSS SSDDFFKKQT KNDPFTSDPF TKNPSLPSKL DPFESSDPFS SSSISSKGSD
     PFGTLDPFGS SSFSSAEGFA DFSQMSKPPP SGPFSSSLGG TGFSDDPFKS KQDTPALPPK
     KPAPPRPKPP SGQSTPVSQL GSSDFPESPD PFQPLGADSG DPFQNKKGFG DPFSGKDPFA
     PSSSAKPPKT SSSGFADFTS FGNEEQQLAW AKRESEKAEQ ERLARLRRQE QEDLELAIAL
     SKADMPA
//
ID   Q3UIX3_MOUSE            Unreviewed;       802 AA.
AC   Q3UIX3;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 36.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Pkp4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Amnion;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Amnion;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Amnion;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Amnion;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Amnion;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Amnion;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Amnion;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Amnion;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK146720; BAE27383.1; -; mRNA.
DR   IPI; IPI00757327; -.
DR   RefSeq; NP_080637.1; NM_026361.2.
DR   RefSeq; NP_780673.2; NM_175464.2.
DR   UniGene; Mm.260938; -.
DR   STRING; Q3UIX3; -.
DR   Ensembl; ENSMUST00000037903; ENSMUSP00000042249; ENSMUSG00000026991.
DR   GeneID; 227937; -.
DR   KEGG; mmu:227937; -.
DR   UCSC; uc008jsz.1; mouse.
DR   CTD; 227937; -.
DR   MGI; MGI:109281; Pkp4.
DR   HOVERGEN; HBG004284; -.
DR   NextBio; 378870; -.
DR   ArrayExpress; Q3UIX3; -.
DR   Bgee; Q3UIX3; -.
DR   Genevestigator; Q3UIX3; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF00514; Arm; 2.
DR   SMART; SM00185; ARM; 4.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 2.
PE   2: Evidence at transcript level;
FT   NON_TER     802    802
SQ   SEQUENCE   802 AA;  88125 MW;  BDB8094B9E3BC881 CRC64;
     MPAPEQGSLV EEGQPQTHQE AVSTGPGMEP ETTATTILAS VKEQELQFQR LTRELEVERQ
     IVASQLERCR LGAESPSIAS TSSTEKSFPW RSTDVPNPGV SKPRVSDTIH PNNYLIRTEP
     EQGTLYSPEQ TSLHERSLGN SRSSTQMNSY SDSGYQEAGS FHNSQTVNKA DSRQHPFTGS
     TSNHVVRTSR AEGQTLVQPS VANRAMRRVS SVPSRAQSPS YVTSTGVSPS RGSLRTSLGS
     GFGSPSVTDS RPLNPSAYSS STLPAQRAAS PYSQRPASPT AVRRVGSVTS RQTSNPNGPV
     PQYQTTTRVG SPLTLTDAQT RVASPSQGQV GSSSPKRSGM TAVPQHLGPS LQRTVHDMDQ
     FGQQQYDIYE RMVPPRPDSL TGLRSSYASQ HSQLGQELRS AVSPDLHITP IYEGRTYYSP
     VYRSPNHGTV ELQGSQTALY RTGSVGIGNL QRTSSQRSTL TYQRNNYALN TAATYAEPYR
     PVQYRVQECS YNRLQHTGPA DDGATRSPSI DSIQKDPSTL KGVIHCLQTS VVFWEFAWRD
     PELPEVIHML QHQFPSVQAN AAAYLQHLCF GDNKVKMEVY RLGGIKHLVD LLDHRVLEVQ
     KNACGALRNL VFGKSTDENK IAMKNVGGIP ALLRLLRKSI DAEVRELVTG VLWNLSSCDA
     VKMTIIRDAL STLTNTVIVP HSGWNNSSFD DDHKIKFQTS LVLRNTTGCL RNLSSAGEEA
     RKQMRSCEGL VDSLLYVIHT CVNTSDYDSK TVENCVCTLR NLSYRLELEV PQARLLGLNE
     LDDLLGKESP SKDSEPSCWG KK
//
ID   EDC4_MOUSE              Reviewed;        1406 AA.
AC   Q3UJB9; Q3U6U8; Q7TS78; Q8R223;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 2.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Enhancer of mRNA-decapping protein 4;
GN   Name=Edc4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-880; SER-884 AND
RP   SER-892, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: In the process of mRNA degradation, seems to play a role
CC       in mRNA decapping. Component of a complex containing DCP2 and
CC       DCP1A which functions in decapping of ARE-containing mRNAs.
CC       Promotes complex formation between DCP1A and DCP2. Enhances the
CC       catalytic activity of DCP2 (in vitro) (By similarity).
CC   -!- SUBUNIT: Part of a decapping complex consisting of DCP1A, DCP2,
CC       EDC3, EDC4 and probably DDX6. Part of a complex consisting of
CC       DCP1A, EDC3, EDC4 and DDX6. Part of a complex consisting of DCP1B,
CC       EDC3, EDC4 and DDX6. Interacts with DCP2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body (By similarity). Nucleus
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UJB9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UJB9-2; Sequence=VSP_023413;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the WD repeat EDC4 family.
CC   -!- SIMILARITY: Contains 4 WD repeats.
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DR   EMBL; AK146527; BAE27236.1; -; mRNA.
DR   EMBL; AK152963; BAE31626.1; -; mRNA.
DR   EMBL; BC022641; AAH22641.1; -; mRNA.
DR   EMBL; BC053081; AAH53081.1; -; mRNA.
DR   IPI; IPI00330066; -.
DR   IPI; IPI00831141; -.
DR   RefSeq; NP_853625.1; NM_181594.2.
DR   UniGene; Mm.28979; -.
DR   ProteinModelPortal; Q3UJB9; -.
DR   SMR; Q3UJB9; 292-395, 1270-1400.
DR   STRING; Q3UJB9; -.
DR   PhosphoSite; Q3UJB9; -.
DR   PRIDE; Q3UJB9; -.
DR   Ensembl; ENSMUST00000040254; ENSMUSP00000039134; ENSMUSG00000036270.
DR   GeneID; 234699; -.
DR   KEGG; mmu:234699; -.
DR   UCSC; uc009nel.1; mouse.
DR   CTD; 234699; -.
DR   MGI; MGI:2446249; Edc4.
DR   eggNOG; roNOG11634; -.
DR   GeneTree; ENSGT00510000047791; -.
DR   HOGENOM; HBG716468; -.
DR   HOVERGEN; HBG053855; -.
DR   InParanoid; Q3UJB9; -.
DR   OrthoDB; EOG42JNQK; -.
DR   NextBio; 382293; -.
DR   ArrayExpress; Q3UJB9; -.
DR   Bgee; Q3UJB9; -.
DR   CleanEx; MM_EDC4; -.
DR   Genevestigator; Q3UJB9; -.
DR   GO; GO:0000932; C:cytoplasmic mRNA processing body; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
DR   SMART; SM00320; WD40; 3.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Nucleus;
KW   Phosphoprotein; Repeat; WD repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1406       Enhancer of mRNA-decapping protein 4.
FT                                /FTId=PRO_0000278963.
FT   REPEAT      174    214       WD 1.
FT   REPEAT      230    277       WD 2.
FT   REPEAT      295    334       WD 3.
FT   REPEAT      342    393       WD 4.
FT   COILED      971   1030       Potential.
FT   COMPBIAS    609    683       Ser-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       6      6       Phosphoserine (By similarity).
FT   MOD_RES     125    125       N6-acetyllysine (By similarity).
FT   MOD_RES     680    680       Phosphoserine (By similarity).
FT   MOD_RES     727    727       Phosphoserine (By similarity).
FT   MOD_RES     729    729       Phosphoserine (By similarity).
FT   MOD_RES     731    731       Phosphothreonine (By similarity).
FT   MOD_RES     733    733       Phosphoserine (By similarity).
FT   MOD_RES     738    738       Phosphoserine (By similarity).
FT   MOD_RES     745    745       Phosphoserine (By similarity).
FT   MOD_RES     785    785       Phosphoserine (By similarity).
FT   MOD_RES     814    814       Phosphoserine (By similarity).
FT   MOD_RES     826    826       Phosphothreonine (By similarity).
FT   MOD_RES     849    849       Phosphoserine (By similarity).
FT   MOD_RES     876    876       Phosphoserine (By similarity).
FT   MOD_RES     880    880       Phosphoserine.
FT   MOD_RES     884    884       Phosphoserine.
FT   MOD_RES     892    892       Phosphoserine.
FT   MOD_RES     897    897       Phosphoserine (By similarity).
FT   MOD_RES    1072   1072       Phosphoserine (By similarity).
FT   MOD_RES    1077   1077       Phosphothreonine (By similarity).
FT   VAR_SEQ     849    864       Missing (in isoform 2).
FT                                /FTId=VSP_023413.
FT   CONFLICT    591    591       E -> K (in Ref. 2; AAH53081).
FT   CONFLICT    772    772       N -> D (in Ref. 2; AAH53081).
FT   CONFLICT   1152   1152       E -> G (in Ref. 1; BAE27236/BAE31626).
SQ   SEQUENCE   1406 AA;  152484 MW;  F89969FDD9EF0725 CRC64;
     MASCASIDIE DATQHLRDIL KLDRPAGGSN AESQRPSSAY NGDLNGLLVP DPLSSGDGNS
     TNKPGIRTMP PINLQEKQVI CLSGDDSSTC IGILAKEVEI VASSDSSISS KARGSNKVKI
     QPVAKYDWEQ KYYYGNLIAV SNSFLAYAIR AANNGSAMVR VISVSTSERT LLKGFTGSVA
     DLAFAHLNSP QLACLDEAGN LFVWRLALVK GKIQEEILVH IRQPEGTALN HFRRIIWCPF
     IPEESEDCCE ESSPTVALLH EDRAEVWDLD MLRSSHNTWP VDVSQIKQGF IVVKGHSTCL
     SEGALSPDGT VLATASHDGF VKFWQIYIEG QDEPRCLHEW KPHDGRPLSC LLFCDNHKKQ
     DPEVPFWRFL ITGADQNREL KMWCTVSWTC LQTIRFSPDI FSSVSVPPSL KVCLDLSAEY
     LILSDVQRKV LYVMELLQNQ DEGRACFSSI SEFLLTHPVL SFGIQVVSRC RLRHTEVLPA
     EEENDSLGTE SSHGAGALES AAGVLIKLFC VHTKALQDVQ IRFQPQLNPD VVAPLSTHTA
     HEDFTFGESR PELGSEGLAS AAHGSQPDLR RIVELPAPAD FLSLSSETKP ELMTPDAFMT
     PTASLQQISA SPSSSSSSSS SSSSSSSSSS SSLTAVSAVS SSSAMDPSLP RPPEELTLSP
     KLQLDGSLTL NSSSSSLQAS PRSLLPGLLP GPADKLISKG PGQVSTAASA LSLDLQEVEP
     LGLPQASPSR TRSPDVISSA STALSQDIPE IASEALSRGF GSSVPEGLIE PNSMASAASA
     LHLLSPRPRQ GPELGSQLGL DGGPGDGDRH STPSLLEAAL TQEVATPDSQ VWPTAPDITR
     ETCSTLTESP RNGLQEKHKS LAFHRPPYHL LQQRDSQDTS AEQSDHDDEV ASLASASGGF
     GSKIPTPRLP SKDWKTKGSP RTSPKLKRKS KKDDGDSAVG SRLTEHQVAE PPEDWPALIW
     QQQRELAELW HNQEELLQRL CAQLEGLQST VTDHVERALE TRHEQEQRRL ERALAEGQQR
     GGQLQEQLTQ QLSQALSSAV AGRLERSVRD EIKKTVPPCV SRSLEPVAGQ LSNSVATKLT
     AVEGSMKENI SKLLKSKNLT DAIARAAADT LQGPMQAAYR EAFQSVVLPA FEKSCQAMFQ
     QINDSFRLGT QEYLQQLESH MKSRKAREQE AREPVLAQLR GLVSTLQSAT EQMAATVSSS
     VRAEVQHQLH VAVGSLQESI LAQVQRIVKG EVSVALKEQQ ATVTSSIMQA MRSAAGTPVP
     SAHLDCQAQQ AHILQLLQQG HLNQAFQQAL TAADLNLVLY VCETVDPAQV FGQPPCPLSQ
     PVLLSLIQQL ASDLGTRSDL KLSYLEEAVM HLDHSDPITR DHMGSVMAQV RQKLFQFLQA
     DPHNSLSKAA RRLSLMLHGL VTPSLP
//
ID   UBP19_MOUSE             Reviewed;        1360 AA.
AC   Q3UJD6; Q3TAC9; Q3TUE6; Q6P9T0; Q80TP5; Q80ZW5;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 19;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 19;
DE   AltName: Full=Ubiquitin thiolesterase 19;
DE   AltName: Full=Ubiquitin-specific-processing protease 19;
GN   Name=Usp19; Synonyms=Kiaa0891;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Fetal brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Head, Kidney, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 395-1360 (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Deubiquitinating enzyme that regulates the degradation
CC       of various proteins. Deubiquitinates and prevents proteasomal
CC       degradation of RNF123 which in turn stimulates CDKN1B ubiquitin-
CC       dependent degradation thereby playing a role in cell
CC       proliferation. Involved in decreased protein synthesis in
CC       atrophying skeletal muscle. Modulates transcription of major
CC       myofibrillar proteins. Also involved in turnover of endoplasmic-
CC       reticulum-associated degradation (ERAD) substrates (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- SUBUNIT: Interacts with and stabilizes RNF123 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UJD6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UJD6-2; Sequence=VSP_026769, VSP_026770;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 2 CS domains.
CC   -!- SIMILARITY: Contains 1 MYND-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65678.4; Type=Erroneous initiation;
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DR   EMBL; AK122396; BAC65678.4; ALT_INIT; mRNA.
DR   EMBL; AK146504; BAE27219.1; -; mRNA.
DR   EMBL; AK160807; BAE36025.1; -; mRNA.
DR   EMBL; AK171942; BAE42739.1; -; mRNA.
DR   EMBL; BC046824; AAH46824.1; -; mRNA.
DR   EMBL; BC060613; AAH60613.1; -; mRNA.
DR   IPI; IPI00420483; -.
DR   IPI; IPI00457619; -.
DR   RefSeq; NP_001161843.1; NM_001168371.2.
DR   RefSeq; NP_001161844.1; NM_001168372.2.
DR   RefSeq; NP_001161845.1; NM_001168373.2.
DR   RefSeq; NP_082080.3; NM_027804.4.
DR   RefSeq; NP_663382.2; NM_145407.3.
DR   UniGene; Mm.289706; -.
DR   UniGene; Mm.479684; -.
DR   HSSP; P40818; 2GFO.
DR   ProteinModelPortal; Q3UJD6; -.
DR   SMR; Q3UJD6; 306-444, 532-722.
DR   STRING; Q3UJD6; -.
DR   MEROPS; C19.024; -.
DR   PhosphoSite; Q3UJD6; -.
DR   PRIDE; Q3UJD6; -.
DR   Ensembl; ENSMUST00000006854; ENSMUSP00000006854; ENSMUSG00000006676.
DR   Ensembl; ENSMUST00000085044; ENSMUSP00000082119; ENSMUSG00000006676.
DR   GeneID; 71472; -.
DR   KEGG; mmu:71472; -.
DR   CTD; 71472; -.
DR   MGI; MGI:1918722; Usp19.
DR   eggNOG; roNOG11044; -.
DR   GeneTree; ENSGT00600000084034; -.
DR   HOVERGEN; HBG061889; -.
DR   OrthoDB; EOG4NVZJG; -.
DR   PhylomeDB; Q3UJD6; -.
DR   BRENDA; 3.1.2.15; 244.
DR   NextBio; 333851; -.
DR   ArrayExpress; Q3UJD6; -.
DR   Bgee; Q3UJD6; -.
DR   CleanEx; MM_USP19; -.
DR   Genevestigator; Q3UJD6; -.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
DR   InterPro; IPR007052; CS-like_domain.
DR   InterPro; IPR017447; CS_domain.
DR   InterPro; IPR015054; DUF1872.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19.
DR   InterPro; IPR002893; Znf_MYND.
DR   Pfam; PF04969; CS; 1.
DR   Pfam; PF08959; DUF1872; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF01753; zf-MYND; 1.
DR   SUPFAM; SSF49764; HSP20_chap; 2.
DR   PROSITE; PS51203; CS; 2.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; 1.
DR   PROSITE; PS50235; UCH_2_3; 1.
DR   PROSITE; PS01360; ZF_MYND_1; 1.
DR   PROSITE; PS50865; ZF_MYND_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Endoplasmic reticulum; Hydrolase; Membrane;
KW   Metal-binding; Phosphoprotein; Protease; Repeat; Thiol protease;
KW   Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1360       Ubiquitin carboxyl-terminal hydrolase 19.
FT                                /FTId=PRO_0000295157.
FT   TOPO_DOM      1   1333       Cytoplasmic (Potential).
FT   TRANSMEM   1334   1354       Helical; (Potential).
FT   TOPO_DOM   1355   1360       Lumenal (Potential).
FT   DOMAIN       51    140       CS 1.
FT   DOMAIN      322    424       CS 2.
FT   ZN_FING     833    875       MYND-type.
FT   COMPBIAS    524    530       Poly-Glu.
FT   ACT_SITE    548    548       Nucleophile (By similarity).
FT   ACT_SITE   1207   1207       Proton acceptor (By similarity).
FT   MOD_RES    1284   1284       Phosphoserine (By similarity).
FT   VAR_SEQ    1286   1340       ASRIWQELEAEEEMVPEGPGPLGPWGPQDWVGPPPRGPTTP
FT                                DEGCLRYFVLGTVA -> GLGPGQAPEVAPTRTAPERFAPP
FT                                VDRPAPTYSNMEEVD (in isoform 2).
FT                                /FTId=VSP_026769.
FT   VAR_SEQ    1341   1360       Missing (in isoform 2).
FT                                /FTId=VSP_026770.
FT   CONFLICT    140    140       L -> LK (in Ref. 2; BAE42739).
FT   CONFLICT    142    142       P -> S (in Ref. 3; AAH60613).
FT   CONFLICT    430    431       Missing (in Ref. 2; BAE42739).
FT   CONFLICT    669    669       A -> T (in Ref. 2; BAE42739).
FT   CONFLICT   1058   1058       D -> E (in Ref. 2; BAE42739).
SQ   SEQUENCE   1360 AA;  150549 MW;  FE9C3020D2CD9AED CRC64;
     MSAGASATGP RRGPPGLEEA TSKKKQKDRA NLESKDGDAR RVSLPRKEPT KDELLLDWRQ
     SADEVIVKLR VGTGPVRLED VDAAFTDTDC VVRLPDGRQW GGVFFAEIQS SCTKVQARKG
     GLLQLVLPKK VPLLTWPSLL KPLGTQELVP GLQCQENGQE LSPIALEPGS EPRRAKQEAR
     NQKRAQGRGE VGSGAGPGTQ AGPSAKRAVH LRRGPEGEGS MDGPGPQGDA PSFLSDSATQ
     VEAEEKLCAP PMNTQTSLLS SEKSLALLTV EKTVSPRNDP VAPVMVQDRD PEPEQEDQVK
     EEMALGADPT ALVEEPESMV NLAFVKNDSY EKGPDSVVVH VYVKEIRRDS SRVLFREQDF
     TLIFQTRDGN FLRLHPGCGP HTIFRWQVKL RNLIEPEQCT FCFTASRIDI CLRKRQSQRW
     GGLEAPATRG AVGGAKVAVP TGPTPLDSTP PGGGPHPLTG QEEARAVEKE KPKARSEDSG
     LDGVVARTPL EHVAPKPDPH LASPKPTCMV PPMPHSPVSG DSVEEDEEEE KKVCLPGFTG
     LVNLGNTCFM NSVIQSLSNT RELRDFFHDR SFEAEINYNN PLGTGGRLAI GFAVLLRALW
     KGTHQAFQPS KLKAIVASKA SQFTGYAQHD AQEFMAFLLD GLHEDLNRIQ NKPYTETVDS
     DGRPDEVVAE EAWQRHKMRN DSFIVDLFQG QYKSKLVCPV CAKVSITFDP FLYLPVPLPQ
     KQKVLPIFYF AREPHSKPIK FLVSVSKENS SASEVLDSLS QSVHVKPENL RLAEVIKNRF
     HRVFLPSHSL DAVSPTDVLL CFELLSPELA KERVVVLEVQ QRPQVPSIPI SKCAACQRKQ
     QSEEEKLKRC TRCYRVGYCN QFCQKTHWPD HKGLCRPENI GYPFLVSVPA SRLTYARLAQ
     LLEGYARYSV SVFQPPFQPG RMALESQSPG CTTLLSTSSL EAGDSEREPI QPSELQLVTP
     VAEGDTGAHR VWPPADRGPV PSTSGLSSEM LASGPIEGCP LLAGERVSRP EAAVPGYQHS
     SESVNTHTPQ FFIYKIDASN REQRLEDKGE TPLELGDDCS LALVWRNNER LQEFVLVASK
     ELECAEDPGS AGEAARAGHF TLDQCLNLFT RPEVLAPEEA WYCPQCKQHR EASKQLLLWR
     LPNVLIVQLK RFSFRSFIWR DKINDLVEFP VRNLDLSKFC IGQKEEQLPS YDLYAVINHY
     GGMIGGHYTA CARLPNDRSS QRSDVGWRLF DDSTVTTVDE SQVVTRYAYV LFYRRRNSPV
     ERPPRASHSE HHPDLGPAAE AAASQASRIW QELEAEEEMV PEGPGPLGPW GPQDWVGPPP
     RGPTTPDEGC LRYFVLGTVA ALVALVLNVF YPLVSQSRWR
//
ID   Q3UJQ2_MOUSE            Unreviewed;       105 AA.
AC   Q3UJQ2;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 34.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Hmgcs1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DBA/2;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DBA/2;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DBA/2;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DBA/2;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DBA/2;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DBA/2;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DBA/2;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DBA/2;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK146351; BAE27103.1; -; mRNA.
DR   IPI; IPI00331707; -.
DR   UniGene; Mm.61526; -.
DR   STRING; Q3UJQ2; -.
DR   Ensembl; ENSMUST00000100285; ENSMUSP00000097858; ENSMUSG00000079828.
DR   Ensembl; ENSMUST00000112117; ENSMUSP00000107745; ENSMUSG00000079301.
DR   InParanoid; Q3UJQ2; -.
DR   ArrayExpress; Q3UJQ2; -.
DR   Genevestigator; Q3UJQ2; -.
DR   GO; GO:0004421; F:hydroxymethylglutaryl-CoA synthase activity; IEA:InterPro.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR013746; HMG_CoA_synt_C.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF08540; HMG_CoA_synt_C; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   105 AA;  11802 MW;  3190526C63FEA392 CRC64;
     TCVAPDVFAE NMKLREDTHH LADYIPQCSI DSLFEGTWYL VRVDEKHRRT YARRPFTNDH
     SLDEGMGLVH SNTATEHIPS PAKKVPRLPA TSAESESAVI SDGEH
//
ID   RMD3_MOUSE              Reviewed;         470 AA.
AC   Q3UJU9; A9UN03; Q3U5Y8; Q3UB61; Q6P8M2; Q7TNF2;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Regulator of microtubule dynamics protein 3;
DE            Short=RMD-3;
DE            Short=mRMD-3;
DE   AltName: Full=Protein FAM82A2;
DE   AltName: Full=Protein FAM82C;
GN   Name=Fam82a2; Synonyms=Fam82c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION.
RX   PubMed=18070910; DOI=10.1083/jcb.200705108;
RA   Oishi K., Okano H., Sawa H.;
RT   "RMD-1, a novel microtubule-associated protein, functions in
RT   chromosome segregation in Caenorhabditis elegans.";
RL   J. Cell Biol. 179:1149-1162(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-212, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May participate in differentiation and apoptosis of
CC       keratinocytes. Overexpression induces apoptosis (By similarity).
CC   -!- SUBUNIT: Interacts with PTPN2 (By similarity). Interacts with
CC       microtubules (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane
CC       protein (By similarity). Cytoplasm (By similarity). Nucleus (By
CC       similarity). Cytoplasm, cytoskeleton, spindle (By similarity).
CC       Cytoplasm, cytoskeleton, spindle pole (By similarity). Note=In
CC       interphase localizes in the cytoplasm, and during mitosis
CC       localizes to the spindle microtubules and spindle poles (By
CC       similarity).
CC   -!- DOMAIN: The transmembrane region is required for mitochondrial
CC       localization (By similarity).
CC   -!- SIMILARITY: Belongs to the FAM82/RMD family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH55754.1; Type=Erroneous initiation;
CC       Sequence=AAH61186.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=FAA00420.1; Type=Erroneous initiation;
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DR   EMBL; AK146299; BAE27056.1; -; mRNA.
DR   EMBL; AK151090; BAE30103.1; -; mRNA.
DR   EMBL; AK153369; BAE31937.1; -; mRNA.
DR   EMBL; AK153322; BAE31902.1; -; mRNA.
DR   EMBL; AL772264; CAM45949.1; -; Genomic_DNA.
DR   EMBL; BC055754; AAH55754.1; ALT_INIT; mRNA.
DR   EMBL; BC061186; AAH61186.1; ALT_SEQ; mRNA.
DR   EMBL; BR000695; FAA00420.1; ALT_INIT; mRNA.
DR   IPI; IPI00678532; -.
DR   RefSeq; NP_001028308.1; NM_001033136.3.
DR   UniGene; Mm.475909; -.
DR   ProteinModelPortal; Q3UJU9; -.
DR   SMR; Q3UJU9; 398-469.
DR   PhosphoSite; Q3UJU9; -.
DR   PRIDE; Q3UJU9; -.
DR   Ensembl; ENSMUST00000094695; ENSMUSP00000092283; ENSMUSG00000070730.
DR   GeneID; 67809; -.
DR   KEGG; mmu:67809; -.
DR   CTD; 67809; -.
DR   MGI; MGI:1915059; Fam82a2.
DR   GeneTree; ENSGT00530000063162; -.
DR   HOGENOM; HBG755399; -.
DR   HOVERGEN; HBG072518; -.
DR   InParanoid; Q3UJU9; -.
DR   OMA; EVRSHME; -.
DR   OrthoDB; EOG4PG61R; -.
DR   PhylomeDB; Q3UJU9; -.
DR   NextBio; 325611; -.
DR   ArrayExpress; Q3UJU9; -.
DR   Bgee; Q3UJU9; -.
DR   CleanEx; MM_1200015F23RIK; -.
DR   Genevestigator; Q3UJU9; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   InterPro; IPR011990; TPR-like_helical.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Coiled coil; Cytoplasm; Cytoskeleton; Differentiation;
KW   Membrane; Microtubule; Mitochondrion; Nucleus; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    470       Regulator of microtubule dynamics protein
FT                                3.
FT                                /FTId=PRO_0000287511.
FT   TRANSMEM     13     35       Helical; (Potential).
FT   COILED       91    125       Potential.
FT   MOD_RES      44     44       Phosphoserine (By similarity).
FT   MOD_RES      46     46       Phosphoserine.
FT   MOD_RES      50     50       Phosphoserine.
FT   MOD_RES     189    189       Phosphoserine.
FT   MOD_RES     212    212       Phosphoserine.
FT   CONFLICT    210    210       K -> R (in Ref. 1; BAE31902/BAE31937).
FT   CONFLICT    224    224       A -> S (in Ref. 3; AAH61186).
FT   CONFLICT    254    254       K -> E (in Ref. 1; BAE27056 and 3;
FT                                AAH61186).
SQ   SEQUENCE   470 AA;  52029 MW;  BA82C57843985A1B CRC64;
     MSRLGALGGS RAGLGLLLGT AAGLGFLCVL YSQRWKRTQR HGRSHSLPNS LDYAQASERG
     RQVTQFRAIP GEAGDAAILP SLSQEGQEKV LDRLDFVLTS LMALRREVEE LQRSLQGLAG
     EIVGEVRSHI EENQRVARRR RFPFARERSD STGSSSVYFT ASSGAALTDA ESEGGYTTAN
     AESDYERDSD KESGDAEDEV SCETVRMGRK DSLDLDVEAA SSPAAAALEE DDSSGREDVQ
     LVLLQADELH QGSKQDKREG FQLLLNNKLA YGSRQDFLWR LARAYSDMSD LTEEESGKKS
     YALNGKEEAE AALKKGDESA ACHLWYAVLC GQLAEHEGIS KRIQSGFSFK EHVDKAIELQ
     PEDPRGHFLL GRWCYQVSHL NWLEKKTATA LFESPLSATV QDALQSFLKA EELQPGFSKA
     GRVYISKCYR ELGKNSEARK WMKLAQELPD VTNEDSAFQK DLEELEVILG
//
ID   Q3UJW4_MOUSE            Unreviewed;       341 AA.
AC   Q3UJW4;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Rnf113a1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
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DR   EMBL; AK146283; BAE27041.1; -; mRNA.
DR   IPI; IPI00172174; -.
DR   UniGene; Mm.307182; -.
DR   ProteinModelPortal; Q3UJW4; -.
DR   SMR; Q3UJW4; 256-317.
DR   Ensembl; ENSMUST00000046433; ENSMUSP00000042569; ENSMUSG00000036537.
DR   MGI; MGI:1917192; Rnf113a1.
DR   eggNOG; maNOG05319; -.
DR   HOGENOM; HBG738163; -.
DR   HOVERGEN; HBG060697; -.
DR   InParanoid; Q3UJW4; -.
DR   OrthoDB; EOG4P2Q2P; -.
DR   PhylomeDB; Q3UJW4; -.
DR   ArrayExpress; Q3UJW4; -.
DR   Bgee; Q3UJW4; -.
DR   Genevestigator; Q3UJW4; -.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Zinc; Zinc-finger.
SQ   SEQUENCE   341 AA;  38475 MW;  5A09675759C856C8 CRC64;
     MAEQLSPGNS TRQVCTFLFK KPGRKGAAGR RKRRLCDAGS GDSCSSSDEG SSVVRPEKKQ
     ATHNQMIQKT RGSAKQKATY GGLSSEDENE PEGLGVVYKS TRSAKPVGPE DMGATAVYEL
     DTEKDRDAQS IFERSQKIQE ELRGKEDDKI YRGINNYQKY VKPKDTSMGN ASSGMVRKGP
     IRAPEHLRAT VRWDYQPDIC KDYKETGFCG FGDSCKFLHD RSDYKHGWQI ERELDEGRYG
     VYEDENYEVG SDDEEIPFKC FICRQTFQNP VVTKCRHYFC ERCALQHFRT TSRCYVCDQQ
     TNGVFNPAKE LIAKLGKHRA EAEGGVSDSL EDIEESPVSI I
//
ID   TAXB1_MOUSE             Reviewed;         814 AA.
AC   Q3UKC1; Q91YT6; Q9CVF0; Q9DC45;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 44.
DE   RecName: Full=Tax1-binding protein 1 homolog;
GN   Name=Tax1bp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Lung, Placenta, and Small intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH TNFAIP3.
RX   MEDLINE=99361984; PubMed=10435631; DOI=10.1038/sj.onc.1202787;
RA   de Valck D., Jin D.-Y., Heyninck K., van de Craen M., Contreras R.,
RA   Fiers W., Jeang K.-T., Beyaert R.;
RT   "The zinc finger protein A20 interacts with a novel anti-apoptotic
RT   protein which is cleaved by specific caspases.";
RL   Oncogene 18:4182-4190(1999).
RN   [4]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=15509224; DOI=10.1111/j.1525-142X.2004.04050.x;
RA   Lehoczky J.A., Williams M.E., Innis J.W.;
RT   "Conserved expression domains for genes upstream and within the HoxA
RT   and HoxD clusters suggests a long-range enhancer existed before
RT   cluster duplication.";
RL   Evol. Dev. 6:423-430(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619 AND SER-693, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Inhibits TNF-induced apoptosis by mediating the TNFAIP3
CC       anti-apoptotic activity. Degraded by caspase-3-like family
CC       proteins upon TNF-induced apoptosis. May also play a role in the
CC       pro-inflammatory cytokine IL-1 signaling cascade (By similarity).
CC   -!- SUBUNIT: Homooligomer. Interacts with TRAF6 in a IL-1-dependent
CC       manner. Interacts with STARD13 (By similarity). Interacts with
CC       TNFAIP3.
CC   -!- DEVELOPMENTAL STAGE: Expressed at E11.5 and E12.5 in distal limb
CC       and genital bud.
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DR   EMBL; AK004574; BAB23383.1; -; mRNA.
DR   EMBL; AK008528; BAB25721.1; -; mRNA.
DR   EMBL; AK146076; BAE26880.1; -; mRNA.
DR   EMBL; BC014798; AAH14798.1; -; mRNA.
DR   IPI; IPI00321802; -.
DR   RefSeq; NP_080092.2; NM_025816.3.
DR   UniGene; Mm.389757; -.
DR   ProteinModelPortal; Q3UKC1; -.
DR   IntAct; Q3UKC1; 2.
DR   STRING; Q3UKC1; -.
DR   PhosphoSite; Q3UKC1; -.
DR   PRIDE; Q3UKC1; -.
DR   Ensembl; ENSMUST00000080723; ENSMUSP00000079548; ENSMUSG00000004535.
DR   GeneID; 52440; -.
DR   KEGG; mmu:52440; -.
DR   UCSC; uc009byz.1; mouse.
DR   CTD; 52440; -.
DR   MGI; MGI:1289308; Tax1bp1.
DR   eggNOG; roNOG12943; -.
DR   GeneTree; ENSGT00530000063216; -.
DR   HOGENOM; HBG444849; -.
DR   HOVERGEN; HBG053034; -.
DR   InParanoid; Q3UKC1; -.
DR   OMA; CVLAFQG; -.
DR   OrthoDB; EOG4JDH65; -.
DR   NextBio; 308956; -.
DR   ArrayExpress; Q3UKC1; -.
DR   Bgee; Q3UKC1; -.
DR   Genevestigator; Q3UKC1; -.
DR   GermOnline; ENSMUSG00000004535; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   InterPro; IPR012852; CoCoA.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   Pfam; PF07888; CALCOCO1; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
PE   1: Evidence at protein level;
KW   Apoptosis; Coiled coil; Phosphoprotein.
FT   CHAIN         1    814       Tax1-binding protein 1 homolog.
FT                                /FTId=PRO_0000234555.
FT   REGION      320    420       Oligomerization (By similarity).
FT   COILED      144    623       Potential.
FT   MOD_RES     619    619       Phosphoserine.
FT   MOD_RES     693    693       Phosphoserine.
FT   CONFLICT    328    328       C -> S (in Ref. 1; BAB23383).
FT   CONFLICT    368    368       Q -> P (in Ref. 1; BAB23383).
FT   CONFLICT    429    429       H -> Y (in Ref. 1; BAE26880).
FT   CONFLICT    658    658       P -> T (in Ref. 1; BAB23383).
FT   CONFLICT    751    751       V -> A (in Ref. 2; AAH14798).
FT   CONFLICT    764    764       P -> H (in Ref. 1; BAB25721).
SQ   SEQUENCE   814 AA;  93630 MW;  828A1FC7D61A06B7 CRC64;
     MTSFQEVQLQ TSNFAHVIFQ NVAKSYLPNA HLECHYTLTP YIHPHSKDWV GIFKVGWSTA
     RDYYTFLWSP MPEHYVEGST VNCVLAFQGY YLPNDDGEFY QFCYVTHKGE IRGASTPFQF
     RAASPVEELL TMEDEGNSDM LVVTTKAGLL ELKIEKTLKE KEELLKLIAV LEKETAQLRE
     QVGRMERELS QEKGRCEQLQ AEQKGLLEVS QSLRVENEEF MKRYSDATAK VQQLEEDIVS
     VTHKAIEKET DLDSLKDKLR KAQHEREQLE CQLQTEKDEK ELYKVHLKNT EIENTKLVSE
     IQTLKNLDGN KESMITHFKE EISKLQSCLA DKENLYRALL LTTSNKEDTL FLKEQLRKAE
     EQVQATRQEL IFLTKELSDA VNVRDKTMAD LHTARLENER VKKQLADTLA ELQLHAVKKD
     QEKTDTLEHE LRREVEDLKL RLQMAADHYR EKFKECQRLQ KQINKLSDQA ASTNSVFTKK
     MGSQQKVNDA SINTDPAAST SASAVDVKPA ASCAETGFDM STKDHVCEMT KEIAEKIEKY
     NKCKQLLQDE KTKCNKYAEE LAKMELKWKE QVKIAENVKL ELAEVEDNYK VQLAEKEKEI
     NGLASYLENL SREKELTKSL EDQKGRKLEG QSPQQVSRCL NTCSEQNGLL PPLSSAQPVL
     QYGNPYSAQE TRDGADGAFY PDEIQRPPVR VPSWEDNVVC SQPARNLSRP DGLEDPEDSR
     EDENVPIPPD PANQHLRSHG AGFCFDSSFD VHKKCPLCEL MFPPNYDQTK FEEHVESHWK
     VCPMCSEQFP PDYDQQGFER HVQTHFDQNV LNFD
//
ID   Q3UKG2_MOUSE            Unreviewed;      1006 AA.
AC   Q3UKG2;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Gm1614;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Amnion;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Amnion;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Amnion;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Amnion;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Amnion;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Amnion;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Amnion;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Amnion;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
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DR   EMBL; AK146021; BAE26839.1; -; mRNA.
DR   IPI; IPI00653542; -.
DR   UniGene; Mm.297784; -.
DR   ProteinModelPortal; Q3UKG2; -.
DR   PhosphoSite; Q3UKG2; -.
DR   Ensembl; ENSMUST00000097619; ENSMUSP00000095224; ENSMUSG00000073600.
DR   MGI; MGI:2686460; Gm1614.
DR   eggNOG; maNOG17341; -.
DR   GeneTree; ENSGT00480000042875; -.
DR   InParanoid; Q3UKG2; -.
DR   OMA; RWATYLE; -.
DR   OrthoDB; EOG4DR9BR; -.
DR   ArrayExpress; Q3UKG2; -.
DR   Bgee; Q3UKG2; -.
DR   Genevestigator; Q3UKG2; -.
PE   1: Evidence at protein level;
FT   NON_TER       1      1
SQ   SEQUENCE   1006 AA;  106420 MW;  EA35454DC53030A9 CRC64;
     LAPLALPGLS RRLPAPAGRQ DSSGSSGSYH TAPGSPEPPD VGPDTEGRGT WLWVAPGRGA
     GAQPVLSVSA QNSRQQHGSG SGFPRGPGSG PLPPRPQLRM LPSGEMEVIF GAGPLFNRSD
     AEDLQEQQLM APTFSSPQLP GPASPASVSS QPQVPDGGSR WATYLELPPR EPSPAVSGQY
     ECVEVALEER SAPVRPRTVP KRQIELRPRP RSPSQDSRAP RPRLLLRTGS LDESLSRLQA
     AAGIVQTALA RKLGSAVPAP SNVTFKSTAK PESTTNSQET TDSTRVLLEE AKSRPPRAHD
     NSSSARVPRP WPSLRERAIR RDKPAPGTEP LGPVSSSIFL QSEEKPHQAY KQESKTQFPR
     ETPDRTVPRA RSPPFHSRGS RVVPSRVVRP RSPSPPQQAP NGSPHNPPQP SKIVWRRSSP
     AFPGGTSSAW ENRNASVEEV VSRRTPSPPP LPQWTQGVAR VGNPCPEAPL VWKVPNSRGG
     DAVGLSRDSS LPALLPREAP HPIETRTPSP GETWSPVVQG ASTALHQEAM NGLTQELEPP
     TPSAPATPEL TEALCLLSLE NAGIAVRGGQ RSPDVDTPEQ PRSHLTSTLD DDVCPEAVGS
     GEAASERPRV TIPRPRDVRK MVKTTYAPSF PAGTPGSGLP APPADTCGED GDASKTHKLP
     ALESPAPAHY TSIFLKDFLP VVPHPYESPE PSLHATPKDA SQSSGVPRRR AENSTAKPFA
     RSEIRLPGAL AFGQRREKTP SVQRRGPGGE NPDAEAQRLV RDPEGRTSPL GGARTSTQCS
     PLESTGTRPP RPGSPQACPN SSLRAAPELE TPLVAPATAV QAPLLPDHPA TAARAAAPFP
     RAASAPPTDR LPPASSLGRR PPGAAPAGKV LVDPESGRYY FVEAPRQPRL RLLFDPESGQ
     YVEVLLPPSP SPSRQPRQPY APLALGPGLY PPAYGPISGP SLSPLSPNLS ALGSLQLPWA
     PEAGPLEGMY YMPLSGTPSP APPMLFCAPP SSSGPIQSSK GSVFPL
//
ID   Q3UKP6_MOUSE            Unreviewed;       522 AA.
AC   Q3UKP6;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 52.
DE   SubName: Full=Brain-specific angiogenesis inhibitor 1-associated protein 2;
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Baiap2; ORFNames=RP23-390H16.1-003;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RA   Holt K.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RA   Matthews L.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK145924; BAE26755.1; -; mRNA.
DR   EMBL; AL953913; CAM22925.1; -; Genomic_DNA.
DR   EMBL; AL929234; CAM22925.1; JOINED; Genomic_DNA.
DR   EMBL; AL929234; CAM27715.1; -; Genomic_DNA.
DR   EMBL; AL953913; CAM27715.1; JOINED; Genomic_DNA.
DR   IPI; IPI00124778; -.
DR   RefSeq; NP_001032843.1; NM_001037754.3.
DR   RefSeq; NP_001032844.2; NM_001037755.3.
DR   RefSeq; NP_570932.2; NM_130862.4.
DR   UniGene; Mm.197534; -.
DR   ProteinModelPortal; Q3UKP6; -.
DR   SMR; Q3UKP6; 1-248, 379-441.
DR   STRING; Q3UKP6; -.
DR   PRIDE; Q3UKP6; -.
DR   Ensembl; ENSMUST00000075180; ENSMUSP00000074674; ENSMUSG00000025372.
DR   GeneID; 108100; -.
DR   KEGG; mmu:108100; -.
DR   CTD; 108100; -.
DR   MGI; MGI:2137336; Baiap2.
DR   HOVERGEN; HBG054462; -.
DR   NextBio; 360066; -.
DR   ArrayExpress; Q3UKP6; -.
DR   Bgee; Q3UKP6; -.
DR   Genevestigator; Q3UKP6; -.
DR   GO; GO:0008093; F:cytoskeletal adaptor activity; IEA:InterPro.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:InterPro.
DR   GO; GO:0046847; P:filopodium assembly; IEA:InterPro.
DR   GO; GO:0007266; P:Rho protein signal transduction; TAS:MGI.
DR   InterPro; IPR013606; IRSp53/MIM_homology_IMD.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:1.20.1270.80; IRSp53/MIM_homology_IMD; 1.
DR   Pfam; PF08397; IMD; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS51338; IMD; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   522 AA;  57596 MW;  8E65752157FD3F99 CRC64;
     MSLSRSEEMH RLTENVYKTI MEQFNPSLRN FIAMGKNYEK ALAGVTFAAK GYFDALVKMG
     ELASESQGSK ELGDVLFQMA EVHRQIQNQL EETLKSFHNE LLTQLEQKVE LDSRYLSAAL
     KKYQTEQRSK GDALDKCQAE LKKLRKKSQG SKNPQKYSDK ELQYIDAISN KQGELENYVS
     DGYKTALTEE RRRFCFLVEK QCAVAKNSAA YHSKGKELLA QKLPLWQQAC ADPNKIPDRA
     VQLMQQMANS NGSILPSALS ASKSNLVISD PIPGAKPLPV PPELAPFVGR MSAQENVPVM
     NGVAGPDSED YNPWADRKAA QPKSLSPPQS QSKLSDSYSN TLPVRKSVTP KNSYATTENK
     TLPRSSSMAA GLERNGRMRV KAIFSHAAGD NSTLLSFKEG DLITLLVPEA RDGWHYGESE
     KTKMRGWFPF SYTRVLDSDG SDRLHMSLQQ GKSSSTGNLL DKDDLALPPP DYGTSSRAFP
     TQTAGTFKQR PYSVAVPAFS QGLDDYGARS VSSGSGTLVS TV
//
ID   Q3UL40_MOUSE            Unreviewed;      1033 AA.
AC   Q3UL40;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   11-JAN-2011, entry version 32.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Tacc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK145721; BAE26610.1; -; mRNA.
DR   IPI; IPI00816988; -.
DR   RefSeq; NP_996738.2; NM_206856.3.
DR   UniGene; Mm.86322; -.
DR   ProteinModelPortal; Q3UL40; -.
DR   Ensembl; ENSMUST00000098004; ENSMUSP00000095613; ENSMUSG00000030852.
DR   GeneID; 57752; -.
DR   KEGG; mmu:57752; -.
DR   UCSC; uc009kaj.1; mouse.
DR   CTD; 57752; -.
DR   MGI; MGI:1928899; Tacc2.
DR   HOVERGEN; HBG055954; -.
DR   ArrayExpress; Q3UL40; -.
DR   Bgee; Q3UL40; -.
DR   Genevestigator; Q3UL40; -.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR   GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR   GO; GO:0022027; P:interkinetic nuclear migration; IMP:MGI.
DR   GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR   GO; GO:0032886; P:regulation of microtubule-based process; IMP:MGI.
DR   GO; GO:0030953; P:spindle astral microtubule organization; IDA:MGI.
DR   InterPro; IPR007707; TACC.
DR   PANTHER; PTHR13924; TACC; 1.
DR   Pfam; PF05010; TACC; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   1033 AA;  112182 MW;  66C03F5F073CFA49 CRC64;
     FCAATFPEPF GEPAPAPRRC PGKVCFSWVL PRRDCARLRG LILSGGLWWL CPGRKAATLR
     ASPDHPGATP SAARASPAPL APEHTASAPS AAGPGVEVTP TASPQHLAKN EPRSSDSEEA
     FETPESTTPV KAPPAPPPSP PEVTPEPEVI DPPAPEEPGC ISEPPVVVPD GPRSSESVEG
     SPFRPSHSSS AVFDEDKPIA SSGTYNLDFD SIELVDNFQS LEPCSADSKG QECKVSTRRK
     STESVPPSKS TLSRSLSLQA SDFDGASCPG SPEAGTLTTD ACGTGSNSAS STLKRTKKTR
     PPSLKKKQAT KKPTETPPVK ETQQEPGEES PVPSEEHLAP ETKTESATPE GAGCTLSDDT
     PLESPAVPTA TCPLTLESAE DVSPLVSGGG RVQNSPPVGR KSVPLTTASE AVEVTLSDSG
     GQEDLPAKGL SVRLEFDYSE DKGSWESQQE NAPPTKKIGK KPVAKMPLRR PKMKKTPEKL
     DNTPASPPRS PTEPSDTPIA KGTYTFDIDK WDDPNFNPFS STSKMQESPK LSQQSYNFDP
     DACEESLDPF KASSKTPSSP SKSPASFEIP ASTTEADGDG LNKPAKKKKT PLKTVKKSPK
     RSPLSDPPSQ DPTPAATPEA PSAISTVVHA TDEEKLAVTS QKWTCMTVDL DADKQDFPQP
     SDLSNFVNET KFNSPSEELD YRNSYEIEYM EKLGSSLPQD DDTPKKQALY LMFDTPQESP
     VKSPPVRMSD SPTPCSGSSF EDTEALVNAA TKLQHPVARG LPSSQEPLLQ VPEKPSQKEL
     EAMALGTPAE AIEIREAAHP PDVSISKTAL YSRIGSTEVE KPPGLLFQQP DLDSALQVAR
     AEVIAKEREV SEWRDKYEES RREVVEMRKI VAEYEKTIAQ MIEDEQREKS ISHQTVQQLV
     LEKEQALADL NSVEKSLADL FRRYEKMKEV LEGFRKNEEV LKKCAQEYLS RVKKEEQRYQ
     ALKVHAEEKL DRANAEIAQV RGKAQQEQAA YQASLRKEQL RVDALERTLE QKNKEIEELT
     KICDELIAKM GKS
//
ID   Q3ULG4_MOUSE            Unreviewed;       379 AA.
AC   Q3ULG4;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-FEB-2011, entry version 40.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Psmd4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK145524; BAE26484.1; -; mRNA.
DR   IPI; IPI00381291; -.
DR   UniGene; Mm.2261; -.
DR   ProteinModelPortal; Q3ULG4; -.
DR   SMR; Q3ULG4; 196-308.
DR   STRING; Q3ULG4; -.
DR   PRIDE; Q3ULG4; -.
DR   Ensembl; ENSMUST00000071664; ENSMUSP00000071589; ENSMUSG00000005625.
DR   UCSC; uc008qhs.1; mouse.
DR   MGI; MGI:1201670; Psmd4.
DR   GeneTree; ENSGT00530000064050; -.
DR   HOGENOM; HBG738415; -.
DR   HOVERGEN; HBG000425; -.
DR   InParanoid; Q3ULG4; -.
DR   OMA; EQIAFAM; -.
DR   ArrayExpress; Q3ULG4; -.
DR   Bgee; Q3ULG4; -.
DR   Genevestigator; Q3ULG4; -.
DR   InterPro; IPR007198; Ssl1-like.
DR   InterPro; IPR003903; Ubiquitin-int_motif.
DR   InterPro; IPR002035; VWF_A.
DR   Pfam; PF04056; Ssl1; 1.
DR   Pfam; PF02809; UIM; 2.
DR   SMART; SM00726; UIM; 2.
DR   SMART; SM00327; VWA; 1.
DR   PROSITE; PS50330; UIM; 2.
DR   PROSITE; PS50234; VWFA; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   379 AA;  41046 MW;  9D3DC705FACF4AEE CRC64;
     MVLESTMVCV DNSEYMRNGD FLPTRLQAQQ DAVNIVCHSK TRSNPENNVG LITLANDCEV
     LTTLTPDTGR ILSKLHTVQP KGKITFCTGI RVAHLALKHR QGKNHKMRII AFVGSPVEDN
     EKDLVKLAKR LKKEKVNVDI INFGEEEVNT EKLTAFVNTL NGKDGTGSHL VTVPPGPSLA
     DALISSPILA GEGGAMLGLG ASDFEFGVDP SADPELALAL RVSMEEQRQR QEEEARRAAA
     ASAAEAGIAT PGTEGERDSD DALLKMTINQ QEFGRPGLPD LSSMTEEEQI AYAMQMSLQG
     TEFSQESADM DASSAMDTSD PVKEEDDYDV MQDPEFLQSV LENLPGVDPN NAAIRSVMGA
     LASQATKDGK NDKKEEEKK
//
ID   Q3ULJ6_MOUSE            Unreviewed;       742 AA.
AC   Q3ULJ6;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Tyrosine-protein kinase receptor;
DE            EC=2.7.10.1;
DE   Flags: Fragment;
GN   Name=Kit;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. CSF-1/PDGF receptor subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AK145462; BAE26452.1; -; mRNA.
DR   IPI; IPI00120590; -.
DR   UniGene; Mm.247073; -.
DR   STRING; Q3ULJ6; -.
DR   Ensembl; ENSMUST00000144270; ENSMUSP00000116465; ENSMUSG00000005672.
DR   MGI; MGI:96677; Kit.
DR   HOVERGEN; HBG005735; -.
DR   InParanoid; Q3ULJ6; -.
DR   ArrayExpress; Q3ULJ6; -.
DR   Bgee; Q3ULJ6; -.
DR   Genevestigator; Q3ULJ6; -.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0005020; F:stem cell factor receptor activity; IDA:MGI.
DR   GO; GO:0006935; P:chemotaxis; TAS:MGI.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
DR   GO; GO:0048066; P:developmental pigmentation; IMP:MGI.
DR   GO; GO:0035234; P:germ cell programmed cell death; IGI:MGI.
DR   GO; GO:0006687; P:glycosphingolipid metabolic process; IMP:MGI.
DR   GO; GO:0007243; P:intracellular protein kinase cascade; IDA:MGI.
DR   GO; GO:0002320; P:lymphoid progenitor cell differentiation; IGI:MGI.
DR   GO; GO:0002573; P:myeloid leukocyte differentiation; IMP:MGI.
DR   GO; GO:0002318; P:myeloid progenitor cell differentiation; IGI:MGI.
DR   GO; GO:0043069; P:negative regulation of programmed cell death; IMP:MGI.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IGI:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR   GO; GO:0043406; P:positive regulation of MAP kinase activity; IGI:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; TAS:MGI.
DR   GO; GO:0048070; P:regulation of developmental pigmentation; IGI:MGI.
DR   GO; GO:0007286; P:spermatid development; IMP:MGI.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   InterPro; IPR001824; Tyr_prot_kinase_rcpt_3_CS.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00240; RECEPTOR_TYR_KIN_III; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Immunoglobulin domain; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Receptor; Repeat; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   NON_TER       1      1
SQ   SEQUENCE   742 AA;  83292 MW;  3AD8659A873142F9 CRC64;
     CTIKDVSTSV NSMWLKMNPQ PQHIAQVKHN SWHRGDFNYE RQETLTISSA RVDDSGVFMC
     YANNTFGSAN VTTTLKVVEK GFINISPVKN TTVFVTDGEN VDLVVEYEAY PKPEHQQWIY
     MNRTSANKGK DYVKSDNKSN IRYVNQLRLT RLKGTEGGTY TFLVSNSDAS ASVTFNVYVN
     TKPEILTYDR LINGMLQCVA EGFPEPTIDW YFCTGAEQRC TTPVSPVDVQ VQNVSVSPFG
     KLVVQSSIDS SVFRHNGTVE CKASNDVGKS SAFFNFAFKE QIQAHTLFTP LLIGFVVAAG
     AMGIIVMVLT YKYLQKPMYE VQWKVVEEIN GNNYVYIDPT QLPYDHKWEF PRNRLSFGKT
     LGAGAFGKVV EATAYGLIKS DAAMTVAVKM LKPSAHLTER EALMSELKVL SYLGNHMNIV
     NLLGACTVGG PTLVITEYCC YGDLLNFLRR KRDSFIFSKQ EEQAEAALYK NLLHSTEPSC
     DSSNEYMDMK PGVSYVVPTK TDKRRSARID SYIERDVTPA IMEDDELALD LDDLLSFSYQ
     VAKGMAFLAS KNCIHRDLAA RNILLTHGRI TKICDFGLAR DIRNDSNYVV KGNARLPVKW
     MAPESIFSCV YTFESDVWSY GIFLWELFSL GSSPYPGMPV DSKFYKMIKE GFRMVSPEHA
     PAEMYDVMKT CWDADPLKRP TFKQVVQLIE KQISDSTKHI YSNLANCNPN PENPVVVDHS
     VRVNSVGSSA SSTQPLLVHE DA
//
ID   Q3ULP2_MOUSE            Unreviewed;       560 AA.
AC   Q3ULP2;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Wdr20a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK145389; BAE26406.1; -; mRNA.
DR   IPI; IPI00153206; -.
DR   UniGene; Mm.435546; -.
DR   ProteinModelPortal; Q3ULP2; -.
DR   PhosphoSite; Q3ULP2; -.
DR   Ensembl; ENSMUST00000095410; ENSMUSP00000093059; ENSMUSG00000037957.
DR   MGI; MGI:1916891; Wdr20a.
DR   eggNOG; roNOG12498; -.
DR   HOVERGEN; HBG011270; -.
DR   InParanoid; Q3ULP2; -.
DR   OrthoDB; EOG49S65W; -.
DR   ArrayExpress; Q3ULP2; -.
DR   Bgee; Q3ULP2; -.
DR   Genevestigator; Q3ULP2; -.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
DR   Pfam; PF00400; WD40; 2.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Repeat; WD repeat.
SQ   SEQUENCE   560 AA;  61998 MW;  BAE1FF1026FC9B17 CRC64;
     MNEIKTQFTT REGLYKLLQH SEYSRPNRVP FNSQGSNPVR VSFVNLNDQS GNGDRLCFNV
     GRELYFYIYK GVRKAADLSK PIDKRIYKGT QPTCHDFNLL TATAEGVSLL VGFSAGQVQL
     IDPIKKETSK LFNEERLIDK SRVTCVKWVP GSESLFLVAH SSGNMYLYNV EHTCGTTAPH
     YQLLKQGESF AVHTCKSKST RNPLLKWTVG EGALNEFAFS PDGKFLACVS QDGFLRVFNF
     DSVELHGTMK SYFGGLLCVC WSPDGKYIVT GGEDDLVTVW SFLDCRVIAR GHGHKSWVSV
     VAFDPYTTSV EESDPMEFSG SDEDFQDLLH FGRDRANSTQ SRLSKRNSTD SRPVSVTYRF
     GSVGQDTQLC LWDLTEDILF PHQPLSRART HTNVMNATSP PAGSNGNSVT TPGNSVPPPL
     PRSNSLPHSA VSNAASKGSV MDGAIASGVS KFATLSLHDR KERHHEKDHK RNHSMGHISS
     KSSDKLNLVT KAKTDPAKTL GTSLCPRMED VPLLEPLICK EIAHERLTVL VFLEDCIVTA
     CQEGFICTWA RPGKVVSFNP
//
ID   Q3UM33_MOUSE            Unreviewed;       428 AA.
AC   Q3UM33;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Histone deacetylase;
DE            EC=3.5.1.98;
GN   Name=Hdac3; ORFNames=mCG_128932;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD Type 1
CC       subfamily.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC139300; AAI39301.1; -; mRNA.
DR   EMBL; BC139301; AAI39302.1; -; mRNA.
DR   EMBL; AK145158; BAE26265.1; -; mRNA.
DR   EMBL; CH466528; EDL10110.1; -; Genomic_DNA.
DR   IPI; IPI00135456; -.
DR   RefSeq; NP_034541.2; NM_010411.2.
DR   UniGene; Mm.20521; -.
DR   ProteinModelPortal; Q3UM33; -.
DR   SMR; Q3UM33; 6-369.
DR   STRING; Q3UM33; -.
DR   PRIDE; Q3UM33; -.
DR   Ensembl; ENSMUST00000043498; ENSMUSP00000037981; ENSMUSG00000024454.
DR   GeneID; 15183; -.
DR   KEGG; mmu:15183; -.
DR   UCSC; uc008erl.1; mouse.
DR   CTD; 15183; -.
DR   MGI; MGI:1343091; Hdac3.
DR   HOGENOM; HBG396919; -.
DR   HOVERGEN; HBG057112; -.
DR   InParanoid; Q3UM33; -.
DR   OMA; HDVPSDL; -.
DR   PhylomeDB; Q3UM33; -.
DR   NextBio; 287697; -.
DR   ArrayExpress; Q3UM33; -.
DR   Bgee; Q3UM33; -.
DR   Genevestigator; Q3UM33; -.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0032922; P:circadian regulation of gene expression; IGI:MGI.
DR   GO; GO:0016575; P:histone deacetylation; IMP:MGI.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IDA:MGI.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IGI:MGI.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR003084; His_deacetylse_1.
DR   Gene3D; G3DSA:3.40.800.20; His_deacetylse; 1.
DR   PANTHER; PTHR10625; His_deacetylse; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   PRINTS; PR01271; HISDACETLASE.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Hydrolase; Nucleus; Transcription;
KW   Transcription regulation.
SQ   SEQUENCE   428 AA;  48821 MW;  1CB84DE250C3BB2C CRC64;
     MAKTVAYFYD PDVGNFHYGA GHPMKPHRLA LTHSLVLHYG LYKKMIVFKP YQASQHDMCR
     FHSEDYIDFL QRVSPTNMQG FTKSLNAFNV GDDCPVFPGL FEFCSRYTGA SLQGATQLNN
     KICDIAINWA GGLHHAKKFE ASGFCYVNDI VIGILELLKY HPRVLYIDID IHHGDGVQEA
     FYLTDRVMTV SFHKYGNYFF PGTGDMYEVG AESGRYYCLN VPLRDGIDDQ SYKHLFQPVI
     SQVVDFYQPT CIVLQCGADS LGCDRLGCFN LSIRGHGECV EYVKSFNIPL LVLGGGGYTV
     RNVARCWTYE TSLLVEEAIS EELPYSEYFE YFAPDFTLHP DVSTRIENQN SRQYLDQIRQ
     TIFENLKMLN HAPSVQIHDV PADLLTYDRT DEADAEERGP EENYSRPEAP NEFYDGDHDN
     DKESDVEI
//
ID   PP1R7_MOUSE             Reviewed;         361 AA.
AC   Q3UM45; Q9CV31; Q9Z105;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 2.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 7;
DE   AltName: Full=Protein phosphatase 1 regulatory subunit 22;
GN   Name=Ppp1r7; Synonyms=Sds22;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   MEDLINE=99248062; PubMed=10231361;
RX   DOI=10.1046/j.1432-1327.1999.00344.x;
RA   Ceulemans H., Van Eynde A., Perez-Callejon E., Beullens M.,
RA   Stalmans W., Bollen M.;
RT   "Structure and splice products of the human gene encoding sds22, a
RT   putative mitotic regulator of protein phosphatase-1.";
RL   Eur. J. Biochem. 262:36-42(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/SvJ;
RA   Ceulemans H., Stalmans W., Bollen M.;
RT   "Cloning, genomic structure and splice products of the mouse PPP1R7
RT   gene, encoding sds22, a putative mitotic regulator of protein
RT   phosphatase-1.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 224-242 AND 246-256, AND MASS SPECTROMETRY.
RC   TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=12972598; DOI=10.1128/MCB.23.19.6780-6789.2003;
RA   Katschinski D.M., Marti H.H., Wagner K.F., Shibata J., Eckhardt K.,
RA   Martin F., Depping R., Paasch U., Gassmann M., Ledermann B.,
RA   Desbaillets I., Wenger R.H.;
RT   "Targeted disruption of the mouse PAS domain serine/threonine kinase
RT   PASKIN.";
RL   Mol. Cell. Biol. 23:6780-6789(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-27, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Regulatory subunit of protein phosphatase 1 (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with PPP1CA, PPP1CB and PPP1CC/PPP1G (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed with high level in testis.
CC       Expression increases during puberty. Expressed in spermatids and
CC       probably also in spermatozoa.
CC   -!- SIMILARITY: Belongs to the SDS22 family.
CC   -!- SIMILARITY: Contains 10 LRR (leucine-rich) repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB26554.1; Type=Frameshift; Positions=255;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF067129; AAK08624.1; -; Genomic_DNA.
DR   EMBL; AF222867; AAK00624.1; -; mRNA.
DR   EMBL; AK009870; BAB26554.1; ALT_FRAME; mRNA.
DR   EMBL; AK145136; BAE26253.1; -; mRNA.
DR   EMBL; AK162517; BAE36954.1; -; mRNA.
DR   EMBL; BC013524; AAH13524.1; -; mRNA.
DR   IPI; IPI00129319; -.
DR   RefSeq; NP_075689.1; NM_023200.2.
DR   UniGene; Mm.88704; -.
DR   ProteinModelPortal; Q3UM45; -.
DR   SMR; Q3UM45; 73-359.
DR   STRING; Q3UM45; -.
DR   PhosphoSite; Q3UM45; -.
DR   REPRODUCTION-2DPAGE; Q3UM45; -.
DR   PRIDE; Q3UM45; -.
DR   Ensembl; ENSMUST00000027494; ENSMUSP00000027494; ENSMUSG00000026275.
DR   GeneID; 66385; -.
DR   KEGG; mmu:66385; -.
DR   UCSC; uc007cdv.1; mouse.
DR   CTD; 66385; -.
DR   MGI; MGI:1913635; Ppp1r7.
DR   eggNOG; roNOG10798; -.
DR   GeneTree; ENSGT00550000074291; -.
DR   HOGENOM; HBG526095; -.
DR   HOVERGEN; HBG082161; -.
DR   InParanoid; Q3UM45; -.
DR   OMA; DATFVRF; -.
DR   OrthoDB; EOG4894MX; -.
DR   PhylomeDB; Q3UM45; -.
DR   NextBio; 321517; -.
DR   ArrayExpress; Q3UM45; -.
DR   Bgee; Q3UM45; -.
DR   Genevestigator; Q3UM45; -.
DR   GermOnline; ENSMUSG00000026275; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003603; U2A'_phosphoprotein32A_C.
DR   Pfam; PF00560; LRR_1; 2.
DR   SMART; SM00446; LRRcap; 1.
DR   PROSITE; PS51450; LRR; 12.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Leucine-rich repeat; Nucleus;
KW   Phosphoprotein; Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    361       Protein phosphatase 1 regulatory subunit
FT                                7.
FT                                /FTId=PRO_0000239614.
FT   REPEAT       98    120       LRR 1.
FT   REPEAT      121    144       LRR 2.
FT   REPEAT      145    164       LRR 3.
FT   REPEAT      165    186       LRR 4.
FT   REPEAT      187    210       LRR 5.
FT   REPEAT      212    230       LRR 6.
FT   REPEAT      231    252       LRR 7.
FT   REPEAT      253    275       LRR 8.
FT   REPEAT      277    298       LRR 9.
FT   REPEAT      321    344       LRR 10.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      24     24       Phosphoserine.
FT   MOD_RES      27     27       Phosphoserine.
FT   CONFLICT     39     39       G -> S (in Ref. 3; BAE26253).
FT   CONFLICT     54     54       D -> E (in Ref. 3; BAE26253).
FT   CONFLICT     97     97       V -> L (in Ref. 3; BAE26253).
SQ   SEQUENCE   361 AA;  41292 MW;  A31206AFB3BD0F30 CRC64;
     MAAERGAGQQ QSQEMMEVDR RVESEESGDE EGKKHGGGGI VANLSEQSLK DGVDRGAEDP
     EEEHELAVDM ETINLDRDAE DVDLTHYRIG KIEGLEVLKK VKSLCLRQNL IKCIENLEEL
     QSLRELDLYD NQIKKIENLE ALTELEVLDI SFNMLRNIEG IDKLTQLKKL FLVNNKINKI
     ENISNLHQLQ MLELGSNRIR AIENIDTLTN LESLFLGKNK ITKLQNLDAL TNLTVLSVQS
     NRLAKIEGLQ SLVNLRELYL SNNGIEVIEG LENNNKLTML DIASNRIKKI ENISHLTELQ
     EFWMNDNLLE SWSDLDELKG ARSLETVYLE RNPLQKDPQY RRKVMLALPS VRQIDATYVR
     F
//
ID   SMCR8_MOUSE             Reviewed;         935 AA.
AC   Q3UMB5; Q5U4H2; Q8BNG6; Q8C704;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=Smith-Magenis syndrome chromosomal region candidate gene 8 protein homolog;
GN   Name=Smcr8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Embryonic germ cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=21992818; PubMed=11997338; DOI=10.1101/gr.73702;
RA   Bi W., Yan J., Stankiewicz P., Park S.-S., Walz K., Boerkoel C.F.,
RA   Potocki L., Shaffer L.G., Devriendt K., Nowaczyk M.J.M., Inoue K.,
RA   Lupski J.R.;
RT   "Genes in a refined Smith-Magenis syndrome critical deletion interval
RT   on chromosome 17p11.2 and the syntenic region of the mouse.";
RL   Genome Res. 12:713-728(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488; SER-491 AND
RP   SER-497, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UMB5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UMB5-2; Sequence=VSP_025488;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK052754; BAC35133.1; -; mRNA.
DR   EMBL; AK083739; BAC39010.1; -; mRNA.
DR   EMBL; AK145010; BAE26183.1; -; mRNA.
DR   EMBL; AL596215; CAI35265.1; -; Genomic_DNA.
DR   EMBL; BC085095; AAH85095.1; -; mRNA.
DR   IPI; IPI00223251; -.
DR   IPI; IPI00845621; -.
DR   RefSeq; NP_001078909.1; NM_001085440.1.
DR   RefSeq; NP_780700.1; NM_175491.4.
DR   UniGene; Mm.57726; -.
DR   ProteinModelPortal; Q3UMB5; -.
DR   PhosphoSite; Q3UMB5; -.
DR   PRIDE; Q3UMB5; -.
DR   Ensembl; ENSMUST00000056907; ENSMUSP00000055926; ENSMUSG00000049323.
DR   Ensembl; ENSMUST00000102667; ENSMUSP00000099728; ENSMUSG00000049323.
DR   GeneID; 237782; -.
DR   KEGG; mmu:237782; -.
DR   CTD; 237782; -.
DR   MGI; MGI:2444720; Smcr8.
DR   eggNOG; roNOG14173; -.
DR   GeneTree; ENSGT00390000010052; -.
DR   HOGENOM; HBG717547; -.
DR   HOVERGEN; HBG058947; -.
DR   InParanoid; Q3UMB5; -.
DR   OMA; DYLDMDM; -.
DR   OrthoDB; EOG49CQ76; -.
DR   PhylomeDB; Q3UMB5; -.
DR   NextBio; 383494; -.
DR   ArrayExpress; Q3UMB5; -.
DR   Bgee; Q3UMB5; -.
DR   Genevestigator; Q3UMB5; -.
DR   InterPro; IPR021713; Folliculin.
DR   Pfam; PF11704; Folliculin; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    935       Smith-Magenis syndrome chromosomal region
FT                                candidate gene 8 protein homolog.
FT                                /FTId=PRO_0000287470.
FT   MOD_RES     416    416       Phosphoserine (By similarity).
FT   MOD_RES     464    464       Phosphoserine (By similarity).
FT   MOD_RES     466    466       Phosphoserine (By similarity).
FT   MOD_RES     467    467       Phosphoserine (By similarity).
FT   MOD_RES     470    470       Phosphoserine (By similarity).
FT   MOD_RES     486    486       Phosphoserine (By similarity).
FT   MOD_RES     488    488       Phosphoserine.
FT   MOD_RES     491    491       Phosphoserine.
FT   MOD_RES     493    493       Phosphothreonine (By similarity).
FT   MOD_RES     497    497       Phosphoserine.
FT   VAR_SEQ     786    935       Missing (in isoform 2).
FT                                /FTId=VSP_025488.
FT   CONFLICT      7      7       V -> A (in Ref. 3; AAH85095).
FT   CONFLICT    291    291       A -> T (in Ref. 1; BAE26183).
FT   CONFLICT    360    360       V -> A (in Ref. 1; BAE26183).
FT   CONFLICT    506    506       V -> I (in Ref. 1; BAE26183).
SQ   SEQUENCE   935 AA;  104957 MW;  6950CE4A0C50D8EE CRC64;
     MISAPDVVAF TKEDEYEEEP YNEPALPEEY SVPLFPYASQ GANPWSKLSG AKFSRDFILI
     SEFSEQVGPQ PLLTIPNDTK VFGTFDLNYF SLRIMSVDYQ ASFVGHPPGS AYPKLNFVED
     SKVVLGDSKE GAFAYVHHLT LYDLEARGFV RPFCMAYISA DQHKIMQQFQ ELSAEFSKAS
     ECLKMGNRKA FAGELEKKLK DLDYTRTVLH TETEIQKKAN DKGFYSSQAI EKANELANVE
     KSIIEHQDLL RQIRSYPRQK TKIPDLQPGD TEHTQDQADQ VSTTSNPEES ANADLYTCRP
     AYTPKLIKAK STKCFDKKLK TLEELCDTEY FTQTLAQLSH IEHMFRGDLC YLLTSQIDRV
     LRKQQPITNF LFEDFVEVDD RMEKQENVPS QPSQDRLPPK PVEECPIPKV LISVGSYKSS
     VESVLIKMEQ ELGDEEYTGV EATEARSFDP QENLDYLDMD MKGSISSGES IEVLGTEKSA
     SVLSKSDSQA SLTVPLSPHV VRSKAVSHRT ISEDSIEVLS TCPSEALIPD DFKASYPSAI
     NEEEAYADNE GAIHFQASAG SPEPDETQEG NLENIPSQID SSCCIGKESE GHLVPLPTPA
     YTLSDEDSVV SIPPQRYIQK DQGLHVDFGV ENTDPSPRDN SCEMFPAYEL DPSCLLASRD
     VSKMSLDNYS DTTSYMGSAA STSSDRIPSA PPAGLSSERH KKRAGQNALK FIRQYPFAHP
     AIYSLLSGRT LVVLGEDETI VRKLVTALSI FVPNYGCYAK PVKHWISSPL HIMDFQKWKL
     IGLQRVASPA NVGTLHTLSR YSRYTSILDL DSKTLRCPLY RGTLVPRLAD HRTQIKRGST
     YYLHVQSMLT QLCSKAFLYT FCHHLHLPAH SEETQEAVAS RQTSFLKLNL GLVNEDIRVV
     QYLAELLKLH YMQESPGTTH PLLRFDYVPS FLYKI
//
ID   WAHS7_MOUSE             Reviewed;        1173 AA.
AC   Q3UMB9; Q3TTQ9; Q6ZPZ7; Q8CAK8; Q8CGK0;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   08-MAR-2011, entry version 40.
DE   RecName: Full=WASH complex subunit 7;
GN   Name=Kiaa1033;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1145 AND 818-1173.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus, Mammary gland, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-1145.
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 124-1173.
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [5]
RP   FUNCTION.
RX   PubMed=19922875; DOI=10.1016/j.devcel.2009.09.010;
RA   Derivery E., Sousa C., Gautier J.J., Lombard B., Loew D., Gautreau A.;
RT   "The Arp2/3 activator WASH controls the fission of endosomes through a
RT   large multiprotein complex.";
RL   Dev. Cell 17:712-723(2009).
CC   -!- FUNCTION: Component of the WASH complex, a complex present at the
CC       surface of endosomes that recruits and activates the Arp2/3
CC       complex to induce actin polymerization. The WASH complex plays a
CC       key role in the fission of tubules that serve as transport
CC       intermediates during endosome sorting.
CC   -!- SUBUNIT: Component of the WASH complex, composed of F-actin-
CC       capping protein subunit alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-
CC       capping protein subunit beta (CAPZB), WASH1, FAM21, KIAA1033,
CC       KIAA0196 and CCDC53 (By similarity).
CC   -!- SIMILARITY: Belongs to the WASHS7 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE36266.1; Type=Erroneous initiation;
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DR   EMBL; AC153508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK038582; BAC30055.1; -; mRNA.
DR   EMBL; AK145000; BAE26179.1; -; mRNA.
DR   EMBL; AK161247; BAE36266.1; ALT_INIT; mRNA.
DR   EMBL; AK166233; BAE38648.1; -; mRNA.
DR   EMBL; BC020314; AAH20314.1; ALT_SEQ; mRNA.
DR   EMBL; AK129269; BAC98079.1; -; mRNA.
DR   IPI; IPI00831049; -.
DR   RefSeq; NP_001028547.2; NM_001033375.2.
DR   UniGene; Mm.278577; -.
DR   PhosphoSite; Q3UMB9; -.
DR   PRIDE; Q3UMB9; -.
DR   Ensembl; ENSMUST00000038388; ENSMUSP00000039322; ENSMUSG00000034560.
DR   GeneID; 319277; -.
DR   KEGG; mmu:319277; -.
DR   UCSC; uc007gkj.1; mouse.
DR   MGI; MGI:2441787; A230046K03Rik.
DR   eggNOG; roNOG04207; -.
DR   GeneTree; ENSGT00390000002524; -.
DR   HOGENOM; HBG445798; -.
DR   HOVERGEN; HBG106578; -.
DR   InParanoid; Q3UMB9; -.
DR   OMA; FQTMYEH; -.
DR   OrthoDB; EOG4N04D4; -.
DR   NextBio; 394515; -.
DR   ArrayExpress; Q3UMB9; -.
DR   Bgee; Q3UMB9; -.
DR   CleanEx; MM_A230046K03RIK; -.
DR   Genevestigator; Q3UMB9; -.
DR   GO; GO:0071203; C:WASH complex; ISS:UniProtKB.
DR   GO; GO:0016197; P:endosome transport; IMP:UniProtKB.
PE   2: Evidence at transcript level;
KW   Coiled coil; Phosphoprotein.
FT   CHAIN         1   1173       WASH complex subunit 7.
FT                                /FTId=PRO_0000282576.
FT   COILED       27     56       Potential.
FT   MOD_RES       7      7       Phosphoserine (By similarity).
SQ   SEQUENCE   1173 AA;  136370 MW;  B4473C932FAE26AF CRC64;
     MAVDTLSPDW DFDRVDDGSQ KIHAEVQLKN YGRFLEEYTS QLRRIEDALD DLIGDVWDFN
     LDPIALKLLP YEQSSLLELI KTENKVLNKV ITVYAALCCE IKKLKYEAET KFYNGLLFYG
     EGATDSSMVE GDCQIQMGRF VSFLQELSCF VTRCYEVVMN VIHQLAALYI SNKIGPKIIE
     TTGVHFQTMY EHLGELLTVL LTLDEIVDNH VTLKDHWTMY KRLLKSVHHN PSKFGIQEEK
     LKPFEKFLLK LEGQLLDGMI FQACIEQQFD SLNGGISVSK NSTFAEEFAH SIRSIFANVE
     AKLGEPSEID QRDKYVGICG LFVLHFQIFR TVDKKFYKSL LDICKKVPAI TLTANIIWFP
     DNFLIHKMPA AAKLLDRKSL QAIKIHRDTF LQQKAQSLNK DVQSYYVFVS SWMMKMESML
     SKEQRMDTFA EDLTNRCNVF IQGFLYAYSI STIIKTTMNL YMSMQKPMTK TSVKALCRLI
     ELLKAIEHMF YRRSMVVADS VSHITQHLQH QALSSISVAK KRVISDKKYS EQRLDVLSAL
     VLAENTLNGP STKQRRLIVS LALSVGTQMK TFKDEELFPL QVVMKKLDLI SELRERVQAQ
     CDCCFLYWHR AVFPIYLDDV YENAVDAARL HYMFSALRDC VPAMMHSRHL ESHELLLDCY
     DKEIMDILNE HLLDKLCKEI EKDLRLSVHT HLKLDDRNPF KVGRKDLALF FSLNPIRFFN
     RFIDIRAYVT HYLDKTFYNL TTVALHDWAT YSEMRNLATQ RYGLVMTEAH LPSQTLEQGL
     DVLEIMRNIH IFVSRYLYNL NNQIFIERTS NNKHLNTINI RHIANSIRTH GTGIMNTTVN
     FTYQFLKKKF YIFSQFMYDE HIKSRLIKDI RFFREIKDQN DHKYPFDRAE KFNRGIRKLG
     ITPEGQSYLD QFRQLISQIG NAMGYIRMIR SGGLHCSSNA IRFVPDLEDI VSFEELVKEE
     GLAEETLRAA RHLDSVLSDH TRNSAEGTEY FKMLVDVFAP EFRRPKNIHL RNFYIIVPPL
     TLNFVEHSIS CKEKLNKKNK LGAAFTDDGF AMGVAYTLKL LDQYQEFDSL HWFQSVREKY
     IKEIRAVAKQ QNVQSTSQDE KLLQTMNLTQ KRLEVYLQEF ELLYFSLSSA RIFFRADKTA
     AEENQEKKEK EEETKTSNGD GPESTVSADP VVK
//
ID   Q3UMF9_MOUSE            Unreviewed;       409 AA.
AC   Q3UMF9;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   SubName: Full=Novel protein;
DE   SubName: Full=Putative uncharacterized protein;
DE   SubName: Full=RIKEN cDNA 6230409E13, isoform CRA_c;
GN   Name=6230409E13Rik; Synonyms=RP23-416G5.2;
GN   ORFNames=RP23-416G5.2-001, mCG_2927;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mammary gland;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RA   Tracey A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [11]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE.
RA   Lad H.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK144924; BAE26139.1; -; mRNA.
DR   EMBL; AL772187; CAM22887.1; -; Genomic_DNA.
DR   EMBL; AL772278; CAM22887.1; JOINED; Genomic_DNA.
DR   EMBL; AL772278; CAM23750.1; -; Genomic_DNA.
DR   EMBL; AL772187; CAM23750.1; JOINED; Genomic_DNA.
DR   EMBL; CH466538; EDL05547.1; -; Genomic_DNA.
DR   IPI; IPI00750314; -.
DR   RefSeq; NP_780443.2; NM_175234.4.
DR   UniGene; Mm.159689; -.
DR   ProteinModelPortal; Q3UMF9; -.
DR   PhosphoSite; Q3UMF9; -.
DR   PRIDE; Q3UMF9; -.
DR   Ensembl; ENSMUST00000029908; ENSMUSP00000029908; ENSMUSG00000028246.
DR   GeneID; 76132; -.
DR   KEGG; mmu:76132; -.
DR   UCSC; uc008sdl.1; mouse.
DR   MGI; MGI:1923382; 6230409E13Rik.
DR   eggNOG; roNOG07280; -.
DR   HOGENOM; HBG446359; -.
DR   HOVERGEN; HBG074915; -.
DR   InParanoid; Q3UMF9; -.
DR   OMA; YGGIMAG; -.
DR   OrthoDB; EOG4X3H1H; -.
DR   NextBio; 344653; -.
DR   ArrayExpress; Q3UMF9; -.
DR   Bgee; Q3UMF9; -.
DR   Genevestigator; Q3UMF9; -.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   Gene3D; G3DSA:1.20.1050.10; GST_C_like; 1.
DR   SUPFAM; SSF47616; GST_C_like; 1.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   409 AA;  46811 MW;  6F283C2D1DB9CA3F CRC64;
     MHWGVGFASS RPCVVDLSWN QSISFFGWWA GSEEPFSFYG DIIAFPLQDY GGIMAGLGSD
     PWWKKTLYLT GGALLAAAAY LLHELLVIRK QQELDSKDAI ILHQFARPNN GVPSLSPFCL
     KMETYLRMAD LPYQNYFGGK LSAQGKMPWI EYNNEKVSGT EFIIDFLEEK LGVNLNKSLG
     PHERAVSRAV TKMVEEHFYW TLAYCQWVDN LNETRKMLSL SGGGPFSNLL RWVVCHITKG
     IVKREMHGHG IGRFSEEEIY MLMEKDMRSL AGLLGDKKYI MGPKLSTLDA TVFGHLAQAM
     WTLPGTRPER LIKGELINLA MYCERIRRKF WPEWHHDDDN TIYESEESSE GSKTHTPMLD
     FSFYSRTETF EDEGAENSFS RTPDTDFTGH SLFDSDVEMD DYTDHEQCK
//
ID   LRCH2_MOUSE             Reviewed;         773 AA.
AC   Q3UMG5; A2AMN8; Q7TNP9; Q80TC9;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Leucine-rich repeat and calponin homology domain-containing protein 2;
GN   Name=Lrch2; Synonyms=Kiaa1495;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 48-456 (ISOFORM 1).
RC   TISSUE=Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 318-773 (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 496-773 (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3UMG5-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q3UMG5-2; Sequence=VSP_021041;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q3UMG5-3; Sequence=VSP_021042;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC   -!- SIMILARITY: Contains 9 LRR (leucine-rich) repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65798.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC       Sequence=CAM22136.1; Type=Erroneous initiation;
CC       Sequence=CAM24878.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AL671981; CAM22136.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL807780; CAM22136.1; JOINED; Genomic_DNA.
DR   EMBL; AL807780; CAM24878.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL671981; CAM24878.1; JOINED; Genomic_DNA.
DR   EMBL; AK144916; BAE26133.1; -; mRNA.
DR   EMBL; BC056180; AAH56180.2; -; mRNA.
DR   EMBL; AK122516; BAC65798.1; ALT_SEQ; mRNA.
DR   IPI; IPI00330136; -.
DR   IPI; IPI00380329; -.
DR   IPI; IPI00758078; -.
DR   RefSeq; NP_001074642.1; NM_001081173.1.
DR   UniGene; Mm.30506; -.
DR   ProteinModelPortal; Q3UMG5; -.
DR   SMR; Q3UMG5; 97-297, 655-766.
DR   PhosphoSite; Q3UMG5; -.
DR   PRIDE; Q3UMG5; -.
DR   Ensembl; ENSMUST00000033647; ENSMUSP00000033647; ENSMUSG00000031290.
DR   Ensembl; ENSMUST00000035921; ENSMUSP00000037778; ENSMUSG00000031290.
DR   Ensembl; ENSMUST00000112819; ENSMUSP00000108438; ENSMUSG00000031290.
DR   GeneID; 210297; -.
DR   KEGG; mmu:210297; -.
DR   UCSC; uc009unk.1; mouse.
DR   CTD; 210297; -.
DR   MGI; MGI:2147870; Lrch2.
DR   GeneTree; ENSGT00590000082932; -.
DR   HOVERGEN; HBG052350; -.
DR   InParanoid; Q3UMG5; -.
DR   OMA; CYRKLHH; -.
DR   NextBio; 372922; -.
DR   ArrayExpress; Q3UMG5; -.
DR   Bgee; Q3UMG5; -.
DR   Genevestigator; Q3UMG5; -.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF00560; LRR_1; 4.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00369; LRR_TYP; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS51450; LRR; 8.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Leucine-rich repeat; Repeat.
FT   CHAIN         1    773       Leucine-rich repeat and calponin homology
FT                                domain-containing protein 2.
FT                                /FTId=PRO_0000253483.
FT   REPEAT       95    118       LRR 1.
FT   REPEAT      119    141       LRR 2.
FT   REPEAT      142    164       LRR 3.
FT   REPEAT      165    187       LRR 4.
FT   REPEAT      189    209       LRR 5.
FT   REPEAT      210    232       LRR 6.
FT   REPEAT      233    255       LRR 7.
FT   REPEAT      257    276       LRR 8.
FT   REPEAT      277    301       LRR 9.
FT   DOMAIN      650    763       CH.
FT   COMPBIAS      6     52       Gly-rich.
FT   VAR_SEQ     496    517       Missing (in isoform 2).
FT                                /FTId=VSP_021041.
FT   VAR_SEQ     589    605       Missing (in isoform 3).
FT                                /FTId=VSP_021042.
FT   CONFLICT    455    455       P -> L (in Ref. 2; BAE26133).
SQ   SEQUENCE   773 AA;  84989 MW;  7C8A85C41AF749FF CRC64;
     MAASQGGGGN SGGGGCSGGG SGGGGGAAGG GGGGGGGGGG GAGAGGGGGC GGTVAVPIPV
     PTLFGQPFPN GPQWHPGSLQ PQHTVRSLDR ALEEAGNSGI LSLSGRKLRE FPGSGYDLTD
     TTQADLSRNR FTEIPSDVWL FAPLETLNLY HNCIKTIPEA IKNLQMLTYL NISRNLLSTL
     PKYLFDLPLK VLVVSNNKLV SIPEEIGKLK DLMELDVSCN EIQVLPQQMG KLHSLKELNI
     RRNNLHVLPD ELGDLPLVKL DFSCNKVTEI PVCYRKLHHL QVIILDNNPL QVPPAQICLK
     GKVHIFKYLN IQACCRMDKK PDSLDLPSLN KRMPSQPLTD SMEDFYPNKN HGPDSGIGSD
     NGEKRLSTTE PSDDDTISLH SQVSESNREQ TSRNDSHITG SKPDSQKDQE VYDFIDPNTE
     DVAVPEEGDT HIGSFVSFLK GKEKSSEKSQ KNEEPPNEKK VDKEQLLPEE EDDDLKEVTD
     LRKIAAQLLK QEQKNRILNH STSVMRNKLK QTVECEKSVP ADEGNSPLSP LAWQPLENQK
     DQIVDQQWPE SQPIIWQNEE RRRSKQIRKE YFKYKSTRKN SSGNENEEQE SDNAHMSAQS
     PVSSEEYDRS DGFSHGPFGL KPRSAFSRAS RQEYGAADPG FTMRRKMEHL REEREQIRQL
     RNNLESRLKV ILPDDIGAAL MDGVVLCHLA NHIRPRSVAS IHVPSPAVPK LSMAKCRRNV
     ENFLDACKKL GVSQERLCLP HHILEERGLV KVGVTVQALL ELPTTKASQL SMA
//
ID   ANR27_MOUSE             Reviewed;        1048 AA.
AC   Q3UMR0; Q6KAU0; Q6P1F9; Q7TNY8; Q8BUD2; Q91W65;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Ankyrin repeat domain-containing protein 27;
DE   AltName: Full=VPS9 domain-containing protein;
DE   AltName: Full=VPS9-ankyrin-repeat protein;
GN   Name=Ankrd27; Synonyms=Varp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RAB21,
RP   SUBCELLULAR LOCATION, AND FUNCTION.
RC   STRAIN=BALB/c; TISSUE=Testis;
RX   PubMed=16525121; DOI=10.1242/jcs.02810;
RA   Zhang X., He X., Fu X.-Y., Chang Z.;
RT   "Varp is a Rab21 guanine nucleotide exchange factor and regulates
RT   endosome dynamics.";
RL   J. Cell Sci. 119:1053-1062(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 371-1048 (ISOFORM 3).
RC   TISSUE=Embryonic tail;
RX   PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of FLJ genes:
RT   the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:127-135(2004).
CC   -!- FUNCTION: May be a Rab21 guanine exchange factor and regulate
CC       endosome dynamics.
CC   -!- SUBUNIT: Interacts with RAB21 and RAB5A, with a strong preference
CC       for RAB21.
CC   -!- INTERACTION:
CC       P35282:Rab21; NbExp=1; IntAct=EBI-1993429, EBI-1993555;
CC       Q8QZZ8:Rab38; NbExp=2; IntAct=EBI-1993429, EBI-1993463;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Mainly localized to early
CC       endosomes in the perinuclear region.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3UMR0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UMR0-2; Sequence=VSP_022792;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q3UMR0-3; Sequence=VSP_022791;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 11 ANK repeats.
CC   -!- SIMILARITY: Contains 1 VPS9 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP94281.1; Type=Frameshift; Positions=920, 929;
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AY336500; AAP94281.1; ALT_FRAME; mRNA.
DR   EMBL; AK085796; BAC39537.1; -; mRNA.
DR   EMBL; AK144733; BAE26038.1; -; mRNA.
DR   EMBL; BC016493; AAH16493.1; -; mRNA.
DR   EMBL; BC065093; AAH65093.1; -; mRNA.
DR   EMBL; AK131117; BAD21367.1; -; Transcribed_RNA.
DR   IPI; IPI00313603; -.
DR   IPI; IPI00410862; -.
DR   IPI; IPI00462512; -.
DR   RefSeq; NP_663608.3; NM_145633.3.
DR   RefSeq; NP_839994.1; NM_178263.3.
DR   UniGene; Mm.272620; -.
DR   HSSP; Q9WUD2; 2ETA.
DR   ProteinModelPortal; Q3UMR0; -.
DR   SMR; Q3UMR0; 151-364, 396-896.
DR   IntAct; Q3UMR0; 6.
DR   STRING; Q3UMR0; -.
DR   PhosphoSite; Q3UMR0; -.
DR   PRIDE; Q3UMR0; -.
DR   Ensembl; ENSMUST00000040844; ENSMUSP00000041751; ENSMUSG00000034867.
DR   Ensembl; ENSMUST00000085536; ENSMUSP00000082671; ENSMUSG00000034867.
DR   Ensembl; ENSMUST00000085538; ENSMUSP00000082673; ENSMUSG00000034867.
DR   GeneID; 245886; -.
DR   KEGG; mmu:245886; -.
DR   UCSC; uc009gkd.1; mouse.
DR   CTD; 245886; -.
DR   MGI; MGI:2444103; Ankrd27.
DR   eggNOG; roNOG14243; -.
DR   GeneTree; ENSGT00580000081629; -.
DR   HOGENOM; HBG713582; -.
DR   HOVERGEN; HBG080845; -.
DR   InParanoid; Q3UMR0; -.
DR   OMA; CLFKHIA; -.
DR   OrthoDB; EOG48PMJG; -.
DR   NextBio; 387000; -.
DR   ArrayExpress; Q3UMR0; -.
DR   Bgee; Q3UMR0; -.
DR   CleanEx; MM_ANKRD27; -.
DR   Genevestigator; Q3UMR0; -.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR003123; VPS9.
DR   InterPro; IPR013995; VPS9_sub.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 5.
DR   Pfam; PF00023; Ank; 8.
DR   Pfam; PF02204; VPS9; 1.
DR   SMART; SM00248; ANK; 8.
DR   SMART; SM00167; VPS9; 1.
DR   SUPFAM; SSF48403; ANK; 2.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 8.
DR   PROSITE; PS51205; VPS9; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ANK repeat; Cytoplasm; GTPase activation;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1   1048       Ankyrin repeat domain-containing protein
FT                                27.
FT                                /FTId=PRO_0000274557.
FT   DOMAIN      233    371       VPS9.
FT   REPEAT      396    426       ANK 1.
FT   REPEAT      462    491       ANK 2.
FT   REPEAT      495    524       ANK 3.
FT   REPEAT      528    557       ANK 4.
FT   REPEAT      564    593       ANK 5.
FT   REPEAT      597    627       ANK 6.
FT   REPEAT      668    698       ANK 7.
FT   REPEAT      742    771       ANK 8.
FT   REPEAT      775    804       ANK 9.
FT   REPEAT      808    837       ANK 10.
FT   REPEAT      841    870       ANK 11.
FT   MOD_RES    1022   1022       Phosphothreonine (By similarity).
FT   VAR_SEQ     630    670       Missing (in isoform 3).
FT                                /FTId=VSP_022791.
FT   VAR_SEQ     670    724       Missing (in isoform 2).
FT                                /FTId=VSP_022792.
FT   CONFLICT    281    310       QQKLLCLRKVVQLMTQSPSQRVNLETMCAD -> TAEAAVP
FT                                EEGGPAHDTISQPESELGDHVCR (in Ref. 2;
FT                                BAC39537).
FT   CONFLICT    371    372       TP -> PQ (in Ref. 4; BAD21367).
FT   CONFLICT    373    377       DAEGF -> VRSPC (in Ref. 3; AAH16493).
FT   CONFLICT    601    601       P -> Q (in Ref. 2; BAE26038).
FT   CONFLICT    609    609       K -> KV (in Ref. 4; BAD21367).
FT   CONFLICT    730    730       S -> P (in Ref. 1; AAP94281).
SQ   SEQUENCE   1048 AA;  116809 MW;  63636820D0CC4D2C CRC64;
     MALYDEDLLK NPFYLALQKW RPDLCSKVAQ IHGIVLVPCR GSLPGSVQAS CQFESYVLVP
     TEGHFQTLDG KAVVIEGNRI KLGAGFACLL SVPILFEETF YNEKEESFSI LCIAHPLERR
     ETSEEPSAPA DPFSLKTIED VREFLGRHSE KFDKNIASFH RTFRECERKS LRHHIDSVNA
     LYTKCLQQLL RDSHLKVLAK QEAQMNLMKQ AVEMYVHHDI YDLIFKYVGT MEASEDAAFN
     KITRSLQDLQ QKDIGVKPEF SFNIPRAKRE LGQLNKCTSP QQKLLCLRKV VQLMTQSPSQ
     RVNLETMCAD DLLSVLLYLL VKTEIPNWMA NLSYIKNFRF SSSAKDELGY CLTSVEAAIE
     YIRQGSLSTK TPDAEGFGDR LFLKQRMNLL SQMTSTPIDC LFKHIASGNQ KEVERLLSQD
     DQDKDAMQKM CHPLCSCEDC EKLISGRLND PSVVTPFSRD DRGQTPLHVA ALCGQASLID
     FLVSKGAVVN ATDYHGSTPL HLACQKGFQS VTLLLLHYKA STEVQDNNGN TPLHLACTYG
     QEDCVKALVY YDVQACRLDI GNEKGDTALH IAARWGYEGI IETLLQNGAP TAVQNRLKET
     PLKCALNSKI LSIMEAHHLS SDRRPRPSEV PAQSPTRSVD SISQGSSTSS FSSISVSFRQ
     EEVKKDYREV EKLLRAVADG DLEMVRYLLE WTEDDLDDVE DAISTVDLEF CHPLCQCPKC
     APAQKLARIS ANGLSVNVTN QDGFSPLHMA ALHGRTDLVP LLLKHGAYSG ARNTSQAVPL
     HLACQQGHFQ VAKCLLDSNA KPNKKDLSGN TPLICACSAG HHEVAALLLQ HGASINACNN
     KGNTALHEAV MGRHTLVVEL LLFYGASVDI LNKRQYTAAD CAEQDSKIME LLQVVPGCVA
     SLDSVEEADH EGYVTVEIRR KWNPKMYNLP EEPLRRQFCL INPGGRFQER TSRETMGRDR
     SVPDLAGRSL QEPEKQRVTG KQSDLSDLSR YQTSEEGNKG LPERPVSRQA APGHRPMVRR
     HTVNDAAILQ VPEVTVHLTT HEASVPQS
//
ID   HDGR2_MOUSE             Reviewed;         669 AA.
AC   Q3UMU9; O35540; Q3UIH6; Q99L92;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   RecName: Full=Hepatoma-derived growth factor-related protein 2;
DE            Short=HRP-2;
GN   Name=Hdgfrp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Testis;
RX   MEDLINE=97445118; PubMed=9299445; DOI=10.1006/bbrc.1997.7233;
RA   Izumoto Y., Kuroda T., Harada H., Kishimoto T., Nakamura H.;
RT   "Hepatoma-derived growth factor belongs to a gene family in mice
RT   showing significant homology in the amino terminus.";
RL   Biochem. Biophys. Res. Commun. 238:26-32(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Heart, Lung, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366 AND SER-367, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366 AND SER-367, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366; SER-367; THR-389;
RP   SER-391; SER-392; SER-393 AND SER-395, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-620; SER-628; SER-635;
RP   SER-659 AND SER-661, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231; SER-233; SER-235;
RP   SER-366; SER-367; THR-389; SER-391; SER-392; SER-393; SER-395;
RP   SER-450; SER-635 AND SER-640, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366 AND SER-367, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366 AND SER-367, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3UMU9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UMU9-2; Sequence=VSP_031118, VSP_031119;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q3UMU9-3; Sequence=VSP_031117;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the HDGF family.
CC   -!- SIMILARITY: Contains 1 PWWP domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D63850; BAA22896.1; -; mRNA.
DR   EMBL; AK143616; BAE25467.1; -; mRNA.
DR   EMBL; AK144669; BAE25999.1; -; mRNA.
DR   EMBL; AK146813; BAE27453.1; -; mRNA.
DR   EMBL; AK146918; BAE27530.1; -; mRNA.
DR   EMBL; BC003741; AAH03741.1; -; mRNA.
DR   IPI; IPI00116442; -.
DR   IPI; IPI00875101; -.
DR   IPI; IPI00885518; -.
DR   PIR; JC5662; JC5662.
DR   RefSeq; NP_032259.1; NM_008233.2.
DR   UniGene; Mm.279188; -.
DR   ProteinModelPortal; Q3UMU9; -.
DR   SMR; Q3UMU9; 2-93.
DR   STRING; Q3UMU9; -.
DR   PhosphoSite; Q3UMU9; -.
DR   PRIDE; Q3UMU9; -.
DR   Ensembl; ENSMUST00000002911; ENSMUSP00000002911; ENSMUSG00000002833.
DR   GeneID; 15193; -.
DR   KEGG; mmu:15193; -.
DR   UCSC; uc008dau.1; mouse.
DR   CTD; 15193; -.
DR   MGI; MGI:1194492; Hdgfrp2.
DR   eggNOG; roNOG11090; -.
DR   GeneTree; ENSGT00530000063013; -.
DR   HOGENOM; HBG269480; -.
DR   HOVERGEN; HBG099722; -.
DR   InParanoid; Q3UMU9; -.
DR   OMA; TPEKKTV; -.
DR   OrthoDB; EOG4WWRKK; -.
DR   PhylomeDB; Q3UMU9; -.
DR   NextBio; 287723; -.
DR   ArrayExpress; Q3UMU9; -.
DR   Bgee; Q3UMU9; -.
DR   CleanEx; MM_HDGFRP2; -.
DR   Genevestigator; Q3UMU9; -.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003702; F:RNA polymerase II transcription factor activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   GO; GO:0006354; P:transcription elongation, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR021567; LEDGF.
DR   InterPro; IPR000313; PWWP.
DR   InterPro; IPR017923; TFIIS_N.
DR   Gene3D; G3DSA:1.20.930.10; TFIIS_N_fun-typ; 1.
DR   Pfam; PF11467; LEDGF; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   SMART; SM00293; PWWP; 1.
DR   PROSITE; PS50812; PWWP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Phosphoprotein.
FT   CHAIN         1    669       Hepatoma-derived growth factor-related
FT                                protein 2.
FT                                /FTId=PRO_0000317644.
FT   DOMAIN        7     64       PWWP.
FT   COILED      550    575       Potential.
FT   COMPBIAS    142    271       Ser-rich.
FT   COMPBIAS    322    363       Arg-rich.
FT   MOD_RES      39     39       N6-acetyllysine (By similarity).
FT   MOD_RES     229    229       Phosphoserine (By similarity).
FT   MOD_RES     231    231       Phosphoserine.
FT   MOD_RES     233    233       Phosphoserine.
FT   MOD_RES     235    235       Phosphoserine.
FT   MOD_RES     239    239       Phosphoserine (By similarity).
FT   MOD_RES     366    366       Phosphoserine.
FT   MOD_RES     367    367       Phosphoserine.
FT   MOD_RES     389    389       Phosphothreonine.
FT   MOD_RES     391    391       Phosphoserine.
FT   MOD_RES     392    392       Phosphoserine.
FT   MOD_RES     393    393       Phosphoserine.
FT   MOD_RES     395    395       Phosphoserine.
FT   MOD_RES     450    450       Phosphoserine.
FT   MOD_RES     454    454       Phosphoserine (By similarity).
FT   MOD_RES     603    603       Phosphoserine (By similarity).
FT   MOD_RES     620    620       Phosphoserine.
FT   MOD_RES     628    628       Phosphoserine.
FT   MOD_RES     629    629       Phosphoserine (By similarity).
FT   MOD_RES     635    635       Phosphoserine.
FT   MOD_RES     640    640       Phosphoserine.
FT   MOD_RES     659    659       Phosphoserine.
FT   MOD_RES     661    661       Phosphoserine.
FT   VAR_SEQ     224    225       KK -> KKHPTGYACPQ (in isoform 3).
FT                                /FTId=VSP_031117.
FT   VAR_SEQ     226    226       Missing (in isoform 2).
FT                                /FTId=VSP_031118.
FT   VAR_SEQ     635    635       Missing (in isoform 2).
FT                                /FTId=VSP_031119.
SQ   SEQUENCE   669 AA;  74291 MW;  01228985D4616848 CRC64;
     MPHAFKPGDL VFAKMKGYPH WPARIDDIAD GAVKPPPNKY PIFFFGTHET AFLGPKDLFP
     YDKCKDKYGK PNKRKGFNEG LWEIQNNPHA SYSAPPPVSS SDSEAPEADL GCGSDVDKDK
     ESRRVMTVTA VTTTATSDRM ESDSDSDKSS DHSGLKRKTP VLKVSVSKRA RRASSDLDQA
     SVSPSEEDSE SPSESEKTSD QDFTPEKKTA ARPPRRGPLG GRKKKKVPSA SDSDSKADSD
     GAKEEPVVTA QPSPSSSSSS SSSSSSDSDV SVKKPPRGRK PAEKPPPKPR GRRPKPERPP
     STSSSDSDSD SGEVDRISEW KRRDEERRRE LEARRRREQE EELRRLREQE REEKERRKER
     AERGGSSGEE LEDEEPVKKR SRKARGRGTP SSSDSEPEGE LGKEGKKLAK KSQLPGSESA
     RKPGQKEKRG RPDEKPRARP VKVERTRKRS EGLSLERKGE KKKEPSVEER LQKLHSEIKF
     ALKVDNPDVR KCLSALEELG TLQVTSQILQ KNTDVVATLK KIRRYKANKD VMAKAAEVYT
     RLKSRVLGPK VEALQKVNKA GAEKERADNE KLEEQPGEQA PRELAEDEPS TDRSAPVNGE
     ATSQKGENME DRAQEDGQDS EDGPRGGSSE ELHDSPRDNS DPAKPGNERQ DHERTRLASE
     SANDDNEDS
//
ID   GP162_MOUSE             Reviewed;         588 AA.
AC   Q3UN16; O88835;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Probable G-protein coupled receptor 162;
GN   Name=Gpr162;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=98112780; PubMed=9445485;
RA   Ansari-Lari M.A., Oeltjen J.C., Schwartz S., Zhang Z., Muzny D.M.,
RA   Lu J., Gorrell J.H., Chinault A.C., Belmont J.W., Miller W.,
RA   Gibbs R.A.;
RT   "Comparative sequence analysis of a gene-rich cluster at human
RT   chromosome 12p13 and its syntenic region in mouse chromosome 6.";
RL   Genome Res. 8:29-40(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Orphan receptor.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC002397; AAC36011.1; -; Genomic_DNA.
DR   EMBL; AK134941; BAE22348.1; -; mRNA.
DR   EMBL; AK144354; BAE25846.1; -; mRNA.
DR   EMBL; AK144543; BAE25932.1; -; mRNA.
DR   EMBL; BC031437; AAH31437.1; -; mRNA.
DR   IPI; IPI00135177; -.
DR   RefSeq; NP_038561.1; NM_013533.3.
DR   UniGene; Mm.2514; -.
DR   ProteinModelPortal; Q3UN16; -.
DR   PhosphoSite; Q3UN16; -.
DR   PRIDE; Q3UN16; -.
DR   Ensembl; ENSMUST00000046893; ENSMUSP00000038536; ENSMUSG00000038390.
DR   GeneID; 14788; -.
DR   KEGG; mmu:14788; -.
DR   UCSC; uc009dsg.1; mouse.
DR   CTD; 14788; -.
DR   MGI; MGI:1315214; Gpr162.
DR   eggNOG; maNOG22361; -.
DR   GeneTree; ENSGT00390000017213; -.
DR   HOGENOM; HBG716108; -.
DR   HOVERGEN; HBG080132; -.
DR   InParanoid; Q3UN16; -.
DR   OMA; RDPTQVK; -.
DR   OrthoDB; EOG4FBHSK; -.
DR   PhylomeDB; Q3UN16; -.
DR   NextBio; 286919; -.
DR   ArrayExpress; Q3UN16; -.
DR   Bgee; Q3UN16; -.
DR   CleanEx; MM_GPR162; -.
DR   Genevestigator; Q3UN16; -.
DR   GermOnline; ENSMUSG00000038390; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR022347; GPCR_153/162.
DR   InterPro; IPR022348; GPCR_162.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01991; GPR153GPR162.
DR   PRINTS; PR01993; GPR162.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; FALSE_NEG.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Receptor; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN         1    588       Probable G-protein coupled receptor 162.
FT                                /FTId=PRO_0000069648.
FT   TOPO_DOM      1     17       Extracellular (Potential).
FT   TRANSMEM     18     38       Helical; Name=1; (Potential).
FT   TOPO_DOM     39     49       Cytoplasmic (Potential).
FT   TRANSMEM     50     70       Helical; Name=2; (Potential).
FT   TOPO_DOM     71     91       Extracellular (Potential).
FT   TRANSMEM     92    112       Helical; Name=3; (Potential).
FT   TOPO_DOM    113    133       Cytoplasmic (Potential).
FT   TRANSMEM    134    154       Helical; Name=4; (Potential).
FT   TOPO_DOM    155    174       Extracellular (Potential).
FT   TRANSMEM    175    195       Helical; Name=5; (Potential).
FT   TOPO_DOM    196    275       Cytoplasmic (Potential).
FT   TRANSMEM    276    296       Helical; Name=6; (Potential).
FT   TOPO_DOM    297    303       Extracellular (Potential).
FT   TRANSMEM    304    324       Helical; Name=7; (Potential).
FT   TOPO_DOM    325    588       Cytoplasmic (Potential).
FT   CARBOHYD     86     86       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    346    346       S -> Y (in Ref. 2; BAE25932).
SQ   SEQUENCE   588 AA;  64148 MW;  C51E3BD59BF82D70 CRC64;
     MARGGLGAEE ASLRSNALSW LACGLLALLA NAWIILSISA KQQKHKPLEL LLCFLAGTHI
     LMAAVPLTTF AVVQLRRQAS SDYDWNESIC KVFVSTYYTL ALATCFTVAS LSYHRMWMVR
     WPVNYRLSNA KKQALHAVMG IWMVSFILST LPSIGWHNNG ERYYARGCQF IVSKIGLGFG
     VCFSLLLLGG IVMGLVCVAI TFYQTLWARP RRARQARRAG GSVGTKAGGL GGLGTRPAFE
     VPAIVVEDTR GKRRSSLDGS ESAKTSLQVT NLVSAIVFLY DSLTGVPILV VSFFSLKSDS
     APPWMVLAVL WCSMAQTLLL PSFIWSCERY RADVRTVWEQ CVAIMSEDDG DDDGTCDDYT
     DGRVCKIRFD ANGATGSGSR DPTQVKLLPG RHMLFPPLER VHYLQVPLSR RLSHDETNIF
     STPRAPGSFL HKWSSSDDIR ILPAQSRALG GPPEYLGQRH RLEDEEDEEE AEGGGLASLR
     QFLESGVLGS GGGPPRGPGF FREEITTFID ETPLPSPTAS PGPSPRRPRP LGFSPRRLSL
     GSPDSRAVGL PLGLSAGRRC SLTGSEGSSR AWGRPWGPGN PIFPQLTL
//
ID   SKAP2_MOUSE             Reviewed;         358 AA.
AC   Q3UND0; Q8BK74; Q9Z2K4;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Src kinase-associated phosphoprotein 2;
DE   AltName: Full=Pyk2/RAFTK-associated protein;
DE   AltName: Full=SKAP55 homolog;
DE            Short=SKAP-HOM;
DE   AltName: Full=Src family-associated phosphoprotein 2;
DE   AltName: Full=Src kinase-associated phosphoprotein 55-related protein;
DE   AltName: Full=Src-associated adapter protein with PH and SH3 domains;
GN   Name=Skap2; Synonyms=Prap, Ra70, Saps, Scap2, Skap55r;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
RP   SUBCELLULAR LOCATION, INDUCTION, POSSIBLE INTERACTION WITH FYN; HCK
RP   AND LYN, PHOSPHORYLATION AT TYR-260, MUTAGENESIS OF TYR-260, AND
RP   FUNCTION.
RC   TISSUE=Testis;
RX   PubMed=11063873; DOI=10.1016/S0301-472X(00)00537-3;
RA   Curtis D.J., Jane S.M., Hilton D.J., Dougherty L., Bodine D.M.,
RA   Begley C.G.;
RT   "Adaptor protein SKAP55R is associated with myeloid differentiation
RT   and growth arrest.";
RL   Exp. Hematol. 28:1250-1259(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RA   Lee J.-S., Suh K.S., Burr J.G.;
RT   "Mouse Saps, Src-associated adaptor protein with PH and SH3 domain.";
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RA   Momoi T., Urase K., Mukasa T., Fujita E., Kouroku Y., Miho Y.,
RA   Soyama A., Momoi M.Y.;
RT   "RA70, retinoic acid responsive gene, is expressed specifically in
RT   spermatocyte in mouse testis.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Lymph node;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 1-12.
RC   TISSUE=T-cell;
RX   MEDLINE=98427289; PubMed=9755858; DOI=10.1016/S0014-5793(98)01040-0;
RA   Marie-Cardine A., Verhagen A.M., Eckerskorn C., Schraven B.;
RT   "SKAP-HOM, a novel adaptor protein homologous to the FYN-associated
RT   protein SKAP55.";
RL   FEBS Lett. 435:55-60(1998).
RN   [7]
RP   PROTEIN SEQUENCE OF 93-114; 129-139 AND 147-158, PHOSPHORYLATION,
RP   INTERACTION WITH FYB, IDENTIFICATION IN A COMPLEX WITH FYB AND PTPNS1,
RP   AND IDENTIFICATION IN A COMPLEX WITH FYB AND LILRB3.
RX   PubMed=11207596; DOI=10.1046/j.1462-5822.2000.00061.x;
RA   Black D.S., Marie-Cardine A., Schraven B., Bliska J.B.;
RT   "The Yersinia tyrosine phosphatase YopH targets a novel adhesion-
RT   regulated signalling complex in macrophages.";
RL   Cell. Microbiol. 2:401-414(2000).
RN   [8]
RP   INTERACTION WITH PTPNS1, AND IDENTIFICATION IN A COMPLEX WITH FYB AND
RP   PTPNS1.
RX   MEDLINE=99401000; PubMed=10469599; DOI=10.1016/S0960-9822(99)80401-1;
RA   Timms J.F., Swanson K.D., Marie-Cardine A., Raab M., Rudd C.E.,
RA   Schraven B., Neel B.G.;
RT   "SHPS-1 is a scaffold for assembling distinct adhesion-regulated
RT   multi-protein complexes in macrophages.";
RL   Curr. Biol. 9:927-930(1999).
RN   [9]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=12893833; DOI=10.1074/jbc.M213217200;
RA   Takahashi T., Yamashita H., Nagano Y., Nakamura T., Ohmori H.,
RA   Avraham H., Avraham S., Yasuda M., Matsumoto M.;
RT   "Identification and characterization of a novel Pyk2/related adhesion
RT   focal tyrosine kinase-associated protein that inhibits alpha-synuclein
RT   phosphorylation.";
RL   J. Biol. Chem. 278:42225-42233(2003).
RN   [10]
RP   TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH ACTIN, AND
RP   FUNCTION.
RX   PubMed=15894167; DOI=10.1016/j.cellsig.2004.11.009;
RA   Bourette R.P., Therier J., Mouchiroud G.;
RT   "Macrophage colony-stimulating factor receptor induces tyrosine
RT   phosphorylation of SKAP55R adaptor and its association with actin.";
RL   Cell. Signal. 17:941-949(2005).
RN   [11]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=16135797; DOI=10.1128/MCB.25.18.8052-8063.2005;
RA   Togni M., Swanson K.D., Reimann S., Kliche S., Pearce A.C.,
RA   Simeoni L., Reinhold D., Wienands J., Neel B.G., Schraven B.,
RA   Gerber A.;
RT   "Regulation of in vitro and in vivo immune functions by the cytosolic
RT   adaptor protein SKAP-HOM.";
RL   Mol. Cell. Biol. 25:8052-8063(2005).
RN   [12]
RP   PHOSPHORYLATION AT TYR-75; TYR-197 AND TYR-260, AND MASS SPECTROMETRY.
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [13]
RP   INTERACTION WITH FYB.
RX   PubMed=17003372; DOI=10.1182/blood-2006-05-022301;
RA   Kasirer-Friede A., Moran B., Nagrampa-Orje J., Swanson K.,
RA   Ruggeri Z.M., Schraven B., Neel B.G., Koretzky G., Shattil S.J.;
RT   "ADAP is required for normal alphaIIb-beta3 activation by VWF/GP Ib-
RT   IX-V and other agonists.";
RL   Blood 109:1018-1025(2007).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-75; TYR-151 AND TYR-260,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 14-222.
RA   Tang Y., Swanson K.D., Neel B.G., Eck M.J.;
RT   "Structural basis for the dimerization and phosphoinositide
RT   specificity of the src kinase-associated phosphoproteins SKAP55 and
RT   SKAP-HOM.";
RL   Submitted (JUL-2005) to the PDB data bank.
CC   -!- FUNCTION: May be involved in B-cell and macrophage adhesion
CC       processes. In B-cells, may act by coupling the B-cell receptor
CC       (BCR) to integrin activation. May play a role in src signaling
CC       pathway.
CC   -!- SUBUNIT: Interacts with LAT, GRB2, PTK2B and PRAM1 (By
CC       similarity). Interacts with FYB, which is required for SKAP2
CC       protein stability. Interacts with PTPNS1. Part of a complex
CC       consisting of SKAP2, FYB and PTPNS1. Part of a complex consisting
CC       of SKAP2, FYB and LILRB3. May interact with actin. May interact
CC       with FYN, HCK and LYN. Interacts with FASLG (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Membrane ruffles of
CC       macrophages. Perikarya and dendrites from neurons.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UND0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UND0-2; Sequence=VSP_022184;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in kidney, lung, liver, spleen, bone
CC       marrow and testis. Present in T-cells, B-cells, and all cells of
CC       the myelomonocytic lineage. Present in all brain regions, with
CC       highest levels in neurons from the Purkinje cell layer,
CC       hippocampal gyrus, cortex and substantia nigra (at protein level).
CC   -!- INDUCTION: By IL-6 in myeloid cells.
CC   -!- DOMAIN: The SH3 domain interacts with FYB and PTK2B (By
CC       similarity).
CC   -!- PTM: Phosphorylated by FYN on Tyr-260. In case of infection with
CC       Y.pseudotuberculosis, dephosphorylated by bacterial phosphatase
CC       yopH.
CC   -!- DISRUPTION PHENOTYPE: Mice are healthy and do not display any
CC       obvious abnormality. They have normal T-cell, platelet and
CC       macrophage function, but show reduced levels of spontaneous
CC       immunoglobulins in the serum, and defects in B-cell proliferation.
CC   -!- SIMILARITY: Belongs to the SKAP family.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF051324; AAC99297.1; -; mRNA.
DR   EMBL; AB014485; BAA77253.1; -; mRNA.
DR   EMBL; AK076000; BAC36111.1; -; mRNA.
DR   EMBL; AK144289; BAE25817.1; -; mRNA.
DR   EMBL; BC003711; AAH03711.1; -; mRNA.
DR   IPI; IPI00131212; -.
DR   IPI; IPI00817026; -.
DR   RefSeq; NP_061243.1; NM_018773.2.
DR   UniGene; Mm.221479; -.
DR   UniGene; Mm.392558; -.
DR   PDB; 1U5E; X-ray; 2.60 A; A/B=14-222.
DR   PDB; 1U5F; X-ray; 1.90 A; A=111-248.
DR   PDB; 1U5G; X-ray; 2.10 A; A/B/C/D=103-222.
DR   PDB; 2OTX; X-ray; 2.60 A; A/B=14-222.
DR   PDBsum; 1U5E; -.
DR   PDBsum; 1U5F; -.
DR   PDBsum; 1U5G; -.
DR   PDBsum; 2OTX; -.
DR   ProteinModelPortal; Q3UND0; -.
DR   SMR; Q3UND0; 14-222, 299-355.
DR   IntAct; Q3UND0; 1.
DR   MINT; MINT-263820; -.
DR   STRING; Q3UND0; -.
DR   PhosphoSite; Q3UND0; -.
DR   PRIDE; Q3UND0; -.
DR   Ensembl; ENSMUST00000078214; ENSMUSP00000077342; ENSMUSG00000059182.
DR   GeneID; 54353; -.
DR   KEGG; mmu:54353; -.
DR   UCSC; uc009bxv.1; mouse.
DR   UCSC; uc009bxw.1; mouse.
DR   CTD; 54353; -.
DR   MGI; MGI:1889206; Skap2.
DR   eggNOG; roNOG08273; -.
DR   GeneTree; ENSGT00390000017856; -.
DR   HOGENOM; HBG715157; -.
DR   HOVERGEN; HBG052827; -.
DR   InParanoid; Q3UND0; -.
DR   OMA; YQFTAAS; -.
DR   OrthoDB; EOG4ZKJMX; -.
DR   PhylomeDB; Q3UND0; -.
DR   NextBio; 311138; -.
DR   ArrayExpress; Q3UND0; -.
DR   Bgee; Q3UND0; -.
DR   CleanEx; MM_SKAP2; -.
DR   Genevestigator; Q3UND0; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0042113; P:B cell activation; IEA:UniProtKB-KW.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; B-cell activation; Cytoplasm;
KW   Direct protein sequencing; Phosphoprotein; SH3 domain.
FT   CHAIN         1    358       Src kinase-associated phosphoprotein 2.
FT                                /FTId=PRO_0000270180.
FT   DOMAIN      116    219       PH.
FT   DOMAIN      296    357       SH3.
FT   MOD_RES      75     75       Phosphotyrosine.
FT   MOD_RES     151    151       Phosphotyrosine.
FT   MOD_RES     197    197       Phosphotyrosine.
FT   MOD_RES     260    260       Phosphotyrosine; by FYN.
FT   MOD_RES     324    324       Phosphotyrosine (By similarity).
FT   VAR_SEQ      22     28       Missing (in isoform 2).
FT                                /FTId=VSP_022184.
FT   MUTAGEN     260    260       Y->F: Abolishes interaction with FYN,
FT                                phosphorylation by FYN, and effects on
FT                                cell growth.
FT   CONFLICT     16     16       E -> K (in Ref. 4; BAE25817).
FT   CONFLICT    104    104       N -> P (in Ref. 7; AA sequence).
FT   HELIX       111    113
FT   STRAND      115    126
FT   STRAND      136    145
FT   STRAND      148    154
FT   STRAND      161    165
FT   STRAND      170    173
FT   HELIX       183    185
FT   STRAND      186    190
FT   STRAND      196    200
FT   HELIX       204    217
SQ   SEQUENCE   358 AA;  40712 MW;  B66973A656E44E05 CRC64;
     MPNPSCTSSP GPLPEEIRNL LADVETFVAD TLKGENLSKK AKEKRESLIK KIKDVKSVYL
     QEFQDKGDAE DGDEYDDPFA GPADTISLAS ERYDKDDDGP SDGNQFPPIA AQDLPFVIKA
     GYLEKRRKDH SFLGFEWQKR WCALSKTVFY YYGSDKDKQQ KGEFAIDGYD VRMNNTLRKD
     GKKDCCFEIC APDKRIYQFT AASPKDAEEW VQQLKFILQD LGSDVIPEDD EERGELYDDV
     DHPAAVSSPQ RSQPIDDEIY EELPEEEEDT ASVKMDEQGK GSRDSVHHTS GDKSTDYANF
     YQGLWDCTGA LSDELSFKRG DVIYILSKEY NRYGWWVGEM KGAIGLVPKA YLMEMYDI
//
ID   GRIN1_MOUSE             Reviewed;         932 AA.
AC   Q3UNH4; Q6PGF9; Q9QZY2;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=G protein-regulated inducer of neurite outgrowth 1;
DE            Short=GRIN1;
GN   Name=Gprin1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 92-932, TISSUE SPECIFICITY, INTERACTION
RP   WITH GNAI1; GNAO1 AND GNAZ, SUBCELLULAR LOCATION, AND FUNCTION.
RC   TISSUE=Brain;
RX   MEDLINE=99410430; PubMed=10480904; DOI=10.1074/jbc.274.38.26931;
RA   Chen L.T., Gilman A.G., Kozasa T.;
RT   "A candidate target for G protein action in brain.";
RL   J. Biol. Chem. 274:26931-26938(1999).
RN   [4]
RP   PROTEIN SEQUENCE OF 312-325; 774-787 AND 813-833, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   INTERACTION WITH GNAO1, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP   923-CYS-CYS-924, AND PALMITOYLATION AT CYS-923 AND CYS-924.
RX   PubMed=15585744; DOI=10.1124/mol.104.003913;
RA   Nakata H., Kozasa T.;
RT   "Functional characterization of Galphao signaling through G protein-
RT   regulated inducer of neurite outgrowth 1.";
RL   Mol. Pharmacol. 67:695-702(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-795, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182; SER-190; SER-495;
RP   THR-575; SER-691; SER-693; SER-714 AND THR-795, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: May be involved in neurite outgrowth.
CC   -!- SUBUNIT: Interacts with activated forms of GNAI1, GNAO1 and GNAZ.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Cell
CC       projection, growth cone (By similarity). Note=Highly enriched in
CC       growth cone.
CC   -!- TISSUE SPECIFICITY: Expressed specifically in brain (at protein
CC       level).
CC   -!- PTM: Palmitoylation on Cys-923 and/or Cys-924 is required for
CC       membrane targeting.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD55371.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK138306; BAE23617.1; -; mRNA.
DR   EMBL; AK144210; BAE25773.1; -; mRNA.
DR   EMBL; BC057044; AAH57044.1; -; mRNA.
DR   EMBL; AF146569; AAD55371.1; ALT_INIT; mRNA.
DR   IPI; IPI00138232; -.
DR   RefSeq; NP_036144.2; NM_012014.3.
DR   UniGene; Mm.41812; -.
DR   ProteinModelPortal; Q3UNH4; -.
DR   STRING; Q3UNH4; -.
DR   PhosphoSite; Q3UNH4; -.
DR   PRIDE; Q3UNH4; -.
DR   Ensembl; ENSMUST00000099506; ENSMUSP00000097106; ENSMUSG00000069227.
DR   GeneID; 26913; -.
DR   KEGG; mmu:26913; -.
DR   UCSC; uc007qpa.1; mouse.
DR   CTD; 26913; -.
DR   MGI; MGI:1349455; Gprin1.
DR   eggNOG; roNOG13129; -.
DR   GeneTree; ENSGT00570000079168; -.
DR   HOGENOM; HBG125270; -.
DR   HOVERGEN; HBG081574; -.
DR   InParanoid; Q3UNH4; -.
DR   OMA; CPSQQKA; -.
DR   NextBio; 304789; -.
DR   ArrayExpress; Q3UNH4; -.
DR   Bgee; Q3UNH4; -.
DR   Genevestigator; Q3UNH4; -.
DR   GermOnline; ENSMUSG00000069227; Mus musculus.
DR   GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0051219; F:phosphoprotein binding; IDA:MGI.
DR   GO; GO:0031175; P:neuron projection development; IDA:MGI.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell projection; Direct protein sequencing;
KW   Lipoprotein; Membrane; Palmitate; Phosphoprotein.
FT   CHAIN         1    932       G protein-regulated inducer of neurite
FT                                outgrowth 1.
FT                                /FTId=PRO_0000235978.
FT   REGION      821    932       Interaction with GNAO1.
FT   MOD_RES     182    182       Phosphoserine.
FT   MOD_RES     190    190       Phosphoserine.
FT   MOD_RES     495    495       Phosphoserine.
FT   MOD_RES     575    575       Phosphothreonine.
FT   MOD_RES     691    691       Phosphoserine.
FT   MOD_RES     693    693       Phosphoserine.
FT   MOD_RES     714    714       Phosphoserine.
FT   MOD_RES     780    780       Phosphoserine (By similarity).
FT   MOD_RES     795    795       Phosphothreonine.
FT   LIPID       923    923       S-palmitoyl cysteine (Probable).
FT   LIPID       924    924       S-palmitoyl cysteine (Probable).
FT   MUTAGEN     923    924       CC->AA: Abolishes membrane targeting.
FT   CONFLICT    215    215       E -> G (in Ref. 3; AAD55371).
FT   CONFLICT    458    458       K -> R (in Ref. 1; BAE25773).
SQ   SEQUENCE   932 AA;  95496 MW;  2AB823F6A8CBF311 CRC64;
     MRDCCSSPKA IPAPPRHALD QSLGMDPRHT SSSGAAEGAS CSERPAGSLA CPSPNCSPLP
     ETPRAHGALT SDNSGTTLFG KPEPMSSAEA TPTASEIRNP VFSGKMDGNS LKQADSTSTR
     KEEAGSLRNE ESMLKGKAEP MIYGKGEPGT VGRVDCTASG AENSGSLGKV DMPCSSKVDI
     VSPGGDNAGS LRKVETISSG KMDPKTENVM HSRRERPGST GEGDLVSLRE NDMKPPDNTD
     SASTKKTDPE FSGKLTPGSS GKTELVSSVT VAPVTSENVN PVCSGGAGPA AVGNSETLSS
     VKKDPQLLGK KEAVSSGEGG SVSVRMAETV SARQPEGMFP AKTDSTSSNS TGPSGRADPV
     SLRNSELVSP VKPERLSSGQ AERVSLVKTE TLSSGKEDPR SSRRVDHTTV TGNMQTSQKG
     NPESSGKTDL GSSSSGDTRS LGTWGSLSAA KAEVTEGKGD PQPWKKASLP ASEKTDPLAS
     SKAGSASQGK AETVSPGEVD AMTLGKTVPT SSGKTALVSP GKVDLMTSER AEGIPELQAS
     EKGNPVNSTR VDTGATGSTE PKSGVKVITQ IPGATSPGKV ETPSLQKEQP QLSEKTDPSR
     KVDPPTTVEP VSLGKADSAS PSPRKAESQT SAKTVPQAPD KATSSLRQSD GTPYSSAQPQ
     RDTRSIGSLP EREPSASTSQ KDLAAAAAQK SPSAEAAAPP PGPRTRDNFT KAPSWDAGAP
     PPREDAGTQA GAQACVSVAV SPMSPQDGAG GPAFSFQAAP RAPSPAPRPP SRRDAGLQVS
     LGAAETRSVA TGPMTPQAAA PPAVPPVFPE VRVRPGSVLA AALAPQEATE PVRDVSWDEK
     GMTWEVYGAS MEVEVLGMAI QKHLERQIEE HGRQGAPAPA PPPAVRAGPG RAGSVRTAPA
     EGAAKRPPGL FRALLQSVRR PRCCSRAGPT AE
//
ID   Q3UP61_MOUSE            Unreviewed;       872 AA.
AC   Q3UP61;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Dlg1; Synonyms=Dlgh1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC   -!- SIMILARITY: Contains 3 PDZ (DHR) domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK143780; BAE25536.1; -; mRNA.
DR   IPI; IPI00408668; -.
DR   UniGene; Mm.382; -.
DR   ProteinModelPortal; Q3UP61; -.
DR   SMR; Q3UP61; 4-63, 189-515, 551-872.
DR   STRING; Q3UP61; -.
DR   Ensembl; ENSMUST00000023454; ENSMUSP00000023454; ENSMUSG00000022770.
DR   UCSC; uc007yxr.1; mouse.
DR   MGI; MGI:107231; Dlg1.
DR   HOVERGEN; HBG107814; -.
DR   ArrayExpress; Q3UP61; -.
DR   Bgee; Q3UP61; -.
DR   Genevestigator; Q3UP61; -.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0031253; C:cell projection membrane; IDA:MGI.
DR   GO; GO:0001772; C:immunological synapse; IDA:MGI.
DR   GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR   GO; GO:0045121; C:membrane raft; IDA:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0019902; F:phosphatase binding; ISS:UniProtKB.
DR   GO; GO:0032947; F:protein complex scaffold; IMP:MGI.
DR   GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR   GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR   GO; GO:0032147; P:activation of protein kinase activity; IMP:MGI.
DR   GO; GO:0042982; P:amyloid precursor protein metabolic process; IGI:MGI.
DR   GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI.
DR   GO; GO:0016337; P:cell-cell adhesion; ISS:UniProtKB.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
DR   GO; GO:0001935; P:endothelial cell proliferation; ISS:UniProtKB.
DR   GO; GO:0060022; P:hard palate development; IMP:MGI.
DR   GO; GO:0001771; P:immunological synapse formation; IMP:MGI.
DR   GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI.
DR   GO; GO:0031579; P:membrane raft organization; IMP:MGI.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
DR   GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0042130; P:negative regulation of T cell proliferation; IMP:MGI.
DR   GO; GO:0030432; P:peristalsis; IMP:MGI.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0008104; P:protein localization; IMP:MGI.
DR   GO; GO:0042391; P:regulation of membrane potential; IGI:MGI.
DR   GO; GO:0048608; P:reproductive structure development; IMP:MGI.
DR   GO; GO:0048745; P:smooth muscle tissue development; IMP:MGI.
DR   GO; GO:0042110; P:T cell activation; IMP:MGI.
DR   GO; GO:0002369; P:T cell cytokine production; IMP:MGI.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR004172; L27.
DR   InterPro; IPR015143; L27_1.
DR   InterPro; IPR016313; M-assoc_guanylate_kinase.
DR   InterPro; IPR019590; MAGUK_PEST_N.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR019583; PDZ_assoc.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF09058; L27_1; 1.
DR   Pfam; PF10608; MAGUK_N_PEST; 1.
DR   Pfam; PF00595; PDZ; 3.
DR   Pfam; PF10600; PDZ_assoc; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   PIRSF; PIRSF001741; MAGUK_DLGH; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00569; L27; 1.
DR   SMART; SM00228; PDZ; 3.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50156; PDZ; 3.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS51022; L27; 1.
DR   PROSITE; PS50106; PDZ; 3.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   872 AA;  96790 MW;  0CD78C2BD8691DD1 CRC64;
     MPVRKQDTQR ALHLLEEYRS KLSQTEDRQL RSSIERVINI FQSNLFQALI DIQEFYEVTL
     LDNPKCVDHS KQCEPVQPVT TWEIASLPST AVTSETLPGS LGPPVEKYRY QDEEVLPPEH
     ISPQVTNEVL GPELVHVSEK NLSEIENVHG FVSHSHISPI KANPPPVLVN TDSLETPTYV
     NGTDADYGYE EITLERGNSG LGFSIAGGTD NPHIGDDSSI FITKIITGGA AAQDGRLRVN
     DCILRVNEAD VRDVTHSKAV EALKEAGSIV RLYVKRRKPA SEKIMEIKLI KGPKGLGFSI
     AGGVGNQHIP GDNSIYVTKI IEGGAAHKDG KLQIGDKLLA VNSVCLEEVT HEEAVTALKN
     TSDFVYLKVA KPTSMYINDG YAPPDITNSS SQSVDNHVSP SSCLGQTPTS PARYSPISKA
     VLGDDEITRE PRKVVLHRGS TGLGFNIVGG EDGEGIFISF ILAGGPADLS GELRKGDRII
     SVNSVDLRAA SHEQAAAALK NAGQAVTIVA QYRPEEYSRF EAKIHDLREQ MMNSSVSSGS
     GSLRTSQKRS LYVRALFDYD KTKDSGLPSQ GLNFRFGDIL HVINASDDEW WQARQVTPDG
     ESDEVGVIPS KRRVEKKERA RLKTVKFNSK TRGDKGEIPD DMGSKGLKHV TSNASDSESS
     YRGQEEYVLS YEPVNQQEVN YTRPVIILGP MKDRVNDDLI SEFPDKFGSC VPHTTRPKRD
     YEVDGRDYHF VTSREQMEKD IQEHKFIEAG QYNNHLYGTS VQSVRAVAEK GKHCILDVSG
     NAIKRLQIAQ LYPISIFIKP KSMENIMEMN KRLTEEQARK TFERAMKLEQ EFTEHFTAIV
     QGDTLEDIYN QVKQIIEEQS GPYIWVPAKE KL
//
ID   ZCCHV_MOUSE             Reviewed;         946 AA.
AC   Q3UPF5; Q9CTU4; Q9DBS7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   RecName: Full=Zinc finger CCCH-type antiviral protein 1;
GN   Name=Zc3hav1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Amnion, Cecum, Lung, Spleen, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-508, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-508 AND SER-553, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Induces an innate immunity to viral infections by
CC       preventing the accumulation of viral RNAs in the cytoplasm. Seems
CC       to recruit the RNA processing exosome to degrade the target RNAs.
CC       Inhibits alphavirus and filovirus replication (By similarity).
CC   -!- SUBUNIT: Interacts with EXOSC5 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Localizes in the cytoplasm at steady state, but
CC       shuttles between nucleus and cytoplasm in a XPO1-dependent manner
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UPF5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UPF5-2; Sequence=VSP_033213, VSP_033214;
CC   -!- DOMAIN: The second and fourth zinc fingers are involved in binding
CC       to specific viral RNAs (By similarity).
CC   -!- SIMILARITY: Contains 2 C3H1-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 PARP catalytic domain.
CC   -!- SIMILARITY: Contains 1 WWE domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK004770; BAB23549.1; -; mRNA.
DR   EMBL; AK080334; BAC37881.1; -; mRNA.
DR   EMBL; AK143568; BAE25440.1; -; mRNA.
DR   EMBL; AK169402; BAE41148.1; -; mRNA.
DR   EMBL; AK172379; BAE42974.1; -; mRNA.
DR   EMBL; AK020263; BAB32047.2; -; mRNA.
DR   IPI; IPI00136572; -.
DR   IPI; IPI00163030; -.
DR   RefSeq; NP_082697.1; NM_028421.1.
DR   RefSeq; NP_083140.1; NM_028864.2.
DR   UniGene; Mm.25243; -.
DR   ProteinModelPortal; Q3UPF5; -.
DR   SMR; Q3UPF5; 70-124, 816-926.
DR   PhosphoSite; Q3UPF5; -.
DR   Ensembl; ENSMUST00000031850; ENSMUSP00000031850; ENSMUSG00000029826.
DR   GeneID; 78781; -.
DR   KEGG; mmu:78781; -.
DR   UCSC; uc009bjz.1; mouse.
DR   CTD; 78781; -.
DR   MGI; MGI:1926031; Zc3hav1.
DR   eggNOG; roNOG10039; -.
DR   GeneTree; ENSGT00600000084343; -.
DR   HOVERGEN; HBG050384; -.
DR   OrthoDB; EOG4HHP1P; -.
DR   NextBio; 349482; -.
DR   ArrayExpress; Q3UPF5; -.
DR   Bgee; Q3UPF5; -.
DR   Genevestigator; Q3UPF5; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009615; P:response to virus; IEA:UniProtKB-KW.
DR   InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR   InterPro; IPR004170; WWE-dom.
DR   InterPro; IPR000571; Znf_CCCH.
DR   Pfam; PF00644; PARP; 1.
DR   PROSITE; PS51059; PARP_CATALYTIC; 1.
DR   PROSITE; PS50918; WWE; 1.
DR   PROSITE; PS50103; ZF_C3H1; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Antiviral defense; Cytoplasm; Metal-binding;
KW   Nucleus; Phosphoprotein; Repeat; RNA-binding; Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    946       Zinc finger CCCH-type antiviral protein
FT                                1.
FT                                /FTId=PRO_0000331461.
FT   DOMAIN      684    771       WWE.
FT   DOMAIN      805    946       PARP catalytic.
FT   ZN_FING      73     86       C3H1-type 1.
FT   ZN_FING      87    113       C3H1-type 1.
FT   ZN_FING     150    172       C3H1-type 3.
FT   ZN_FING     173    194       C3H1-type 2.
FT   REGION      224    254       Binding to EXOSC5 (By similarity).
FT   MOTIF        69     76       Nuclear localization signal (By
FT                                similarity).
FT   MOTIF       283    290       Nuclear export signal (By similarity).
FT   MOTIF       412    413       Nuclear localization signal (Potential).
FT   COMPBIAS    572    576       Poly-Met.
FT   MOD_RES     257    257       Phosphoserine (By similarity).
FT   MOD_RES     269    269       Phosphoserine.
FT   MOD_RES     273    273       Phosphoserine (By similarity).
FT   MOD_RES     324    324       Phosphoserine.
FT   MOD_RES     350    350       Phosphoserine.
FT   MOD_RES     425    425       Phosphoserine (By similarity).
FT   MOD_RES     440    440       Phosphothreonine (By similarity).
FT   MOD_RES     508    508       Phosphotyrosine.
FT   MOD_RES     553    553       Phosphoserine.
FT   VAR_SEQ     789    789       D -> E (in isoform 2).
FT                                /FTId=VSP_033213.
FT   VAR_SEQ     790    946       Missing (in isoform 2).
FT                                /FTId=VSP_033214.
SQ   SEQUENCE   946 AA;  106688 MW;  BE2EFE5FBC6062EA CRC64;
     MTDPEVFCFI TKILCAHGGR MTLEELLGEI SLPEAQLYEL LKAAGPDRFV LLETGDQAGI
     TRSVVATTRA RVCRRKYCQR PCDSLHLCKL NLLGRCHYAQ SQRNLCKYSH DVLSEQNFQV
     LKNHELSGLN QEELAVLLVQ SDPFFMPEIC KSYKGEGRKQ ICGQPQPCER LHICEHFTRG
     NCSYLNCLRS HNLMDRKVLA IMREHGLSSD VVQNIQDICN NKHTRRNPPS MRAPHPHRRG
     GAHRDRSKSR DRFHHNSLEV LSTVSPLGSG PPSPDVTGCK DPLEDVSADV TQKFKYLGTQ
     DRAQLSSVSS KAAGVRGPSQ MRASQEFLED GDPDGLFSRN RSDSSTSRTS AAGFPLVAAQ
     RNEAGAMKMG MPSGHHVEVK GKNEDIDRVP FLNSYIDGVT MEEATVSGIL GKRATDNGLE
     EMILSSNHQK SVAKTQDPQT AGRITDSGQD TAFLHSKYEE NPAWPGTSTH NGPNGFSQIM
     DETPNVSKSS PTGFGIKSAV TGGKEAVYSG VQSLRSHVLA MPGETTTPVQ GSNRLPPSPL
     SSSTSHRVAA SGSPGKSSTH ASVSPASEPS RMMMMMSDPA EYSLCYIVNP VSPRMDDHGL
     KEICLDHLYR GCQQVNCNKN HFHLPYRWQL FILPTWMDFQ DMEYIERAYC DPQIEIIVIE
     KHRINFKKMT CDSYPIRRLS TPSFVEKTLN SVFTTKWLWY WRNELNEYTQ YGHESPSHTS
     SEINSAYLES FFHSCPRGVL QFHAGSQNYE LSFQGMIQTN IASKTQRHVV RRPVFVSSKD
     VEQKRRGPDH QPVMPQADAL TLFSSPQRNA STVSSNEYEF IELNNQDEEY AKISEQFKAS
     MKQFKIVTIK RIWNQKLWDT FERKKQKMKN KTEMFLFHAV GRIHMDYICK NNFEWILHGN
     REIRYGKGLC WRRENCDSSH AHGFLEMPLA SLGRTASLDS SGLQRK
//
ID   ARH40_MOUSE             Reviewed;        1517 AA.
AC   Q3UPH7; Q3U1X1; Q3UGT7; Q3UYX3; Q6KAS1; Q6PD04; Q6PDY3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=Rho guanine nucleotide exchange factor 40;
DE   AltName: Full=Protein SOLO;
GN   Name=Arhgef40; Synonyms=Solo;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of FLJ genes:
RT   the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:127-135(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-593 (ISOFORM 4).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1130-1517 (ISOFORM 6).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=16143467; DOI=10.1016/j.gene.2005.06.025;
RA   Tse S.-W., Broderick J.A., Wei M.-L., Luo M.-H., Smith D.,
RA   McCaffery P., Stamm S., Andreadis A.;
RT   "Identification, expression analysis, genomic organization and
RT   cellular location of a novel protein with a RhoGEF domain.";
RL   Gene 359:63-72(2005).
CC   -!- FUNCTION: May act as a guanine nucleotide exchange factor (GEF)
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=Concentrated
CC       in the perinuclear region (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q3UPH7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UPH7-2; Sequence=VSP_030387, VSP_030388;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q3UPH7-3; Sequence=VSP_030387;
CC       Name=4;
CC         IsoId=Q3UPH7-4; Sequence=VSP_030384;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q3UPH7-5; Sequence=VSP_030385, VSP_030386;
CC         Note=No experimental confirmation available;
CC       Name=6;
CC         IsoId=Q3UPH7-6; Sequence=VSP_030387, VSP_030389;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed but enriched in brain.
CC       In brain it is expressed at higher level in olfactory bulb and
CC       cerebellum and peaks perinatally (from E16 to P0.5).
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH58405.1; Type=Erroneous initiation;
CC       Sequence=BAD21386.1; Type=Erroneous initiation;
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DR   EMBL; AK131136; BAD21386.1; ALT_INIT; mRNA.
DR   EMBL; AK134295; BAE22088.1; -; mRNA.
DR   EMBL; AK143527; BAE25418.1; -; mRNA.
DR   EMBL; AK147761; BAE28120.1; -; mRNA.
DR   EMBL; AK155659; BAE33372.1; -; mRNA.
DR   EMBL; BC058405; AAH58405.1; ALT_INIT; mRNA.
DR   EMBL; BC059018; AAH59018.1; -; mRNA.
DR   IPI; IPI00626688; -.
DR   IPI; IPI00654133; -.
DR   IPI; IPI00761379; -.
DR   IPI; IPI00881371; -.
DR   IPI; IPI00882016; -.
DR   IPI; IPI00882367; -.
DR   RefSeq; NP_001139393.1; NM_001145921.1.
DR   RefSeq; NP_001139394.1; NM_001145922.1.
DR   RefSeq; NP_937892.2; NM_198249.4.
DR   UniGene; Mm.9239; -.
DR   ProteinModelPortal; Q3UPH7; -.
DR   SMR; Q3UPH7; 1075-1373.
DR   PhosphoSite; Q3UPH7; -.
DR   PRIDE; Q3UPH7; -.
DR   Ensembl; ENSMUST00000089769; ENSMUSP00000087201; ENSMUSG00000004562.
DR   Ensembl; ENSMUST00000093813; ENSMUSP00000091331; ENSMUSG00000004562.
DR   GeneID; 268739; -.
DR   KEGG; mmu:268739; -.
DR   UCSC; uc007tnr.1; mouse.
DR   CTD; 268739; -.
DR   MGI; MGI:2685515; E130112L23Rik.
DR   eggNOG; roNOG08491; -.
DR   GeneTree; ENSGT00560000077135; -.
DR   HOVERGEN; HBG108500; -.
DR   InParanoid; Q3UPH7; -.
DR   OMA; RMERKRS; -.
DR   OrthoDB; EOG4J117G; -.
DR   NextBio; 392461; -.
DR   ArrayExpress; Q3UPH7; -.
DR   Bgee; Q3UPH7; -.
DR   CleanEx; MM_E130112L23RIK; -.
DR   Genevestigator; Q3UPH7; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   PROSITE; PS00741; DH_1; FALSE_NEG.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Cytoplasm;
KW   Guanine-nucleotide releasing factor; Phosphoprotein.
FT   CHAIN         1   1517       Rho guanine nucleotide exchange factor
FT                                40.
FT                                /FTId=PRO_0000314823.
FT   DOMAIN     1083   1251       DH.
FT   DOMAIN     1263   1370       PH.
FT   COILED      754    792       Potential.
FT   COMPBIAS    402    472       Glu-rich.
FT   COMPBIAS    550    553       Poly-Pro.
FT   COMPBIAS    964    967       Poly-Arg.
FT   MOD_RES     262    262       Phosphoserine (By similarity).
FT   MOD_RES     367    367       Phosphothreonine (By similarity).
FT   MOD_RES     929    929       Phosphoserine (By similarity).
FT   MOD_RES     959    959       Phosphoserine (By similarity).
FT   VAR_SEQ       1    192       Missing (in isoform 4).
FT                                /FTId=VSP_030384.
FT   VAR_SEQ     537    537       G -> Q (in isoform 5).
FT                                /FTId=VSP_030385.
FT   VAR_SEQ     538   1517       Missing (in isoform 5).
FT                                /FTId=VSP_030386.
FT   VAR_SEQ    1413   1460       Missing (in isoform 2, isoform 3 and
FT                                isoform 6).
FT                                /FTId=VSP_030387.
FT   VAR_SEQ    1504   1504       Q -> QAWLRGIK (in isoform 2).
FT                                /FTId=VSP_030388.
FT   VAR_SEQ    1505   1517       SHSRALSDPTTPL -> AWLRGIKVRDQKQS (in
FT                                isoform 6).
FT                                /FTId=VSP_030389.
FT   CONFLICT    381    381       A -> T (in Ref. 1; BAD21386 and 2;
FT                                BAE33372).
FT   CONFLICT    392    392       E -> K (in Ref. 2; BAE22088).
FT   CONFLICT    501    501       N -> D (in Ref. 1; BAD21386 and 2;
FT                                BAE33372).
FT   CONFLICT    862    862       A -> V (in Ref. 1; BAD21386).
FT   CONFLICT   1108   1108       L -> P (in Ref. 1; BAD21386).
SQ   SEQUENCE   1517 AA;  165132 MW;  63A0F5900AC42D2E CRC64;
     MEPEPVEDCV QSTLAALYPP FEATAPTLLG QVFQVVERTY QEDALRYTLD FLVPAKHLLA
     KVQQEACAQY SGFLFFHEGW PLCLHEQVVV QLAALPWQLL RPGDFYLQVV PSAAQAPRLA
     LKCLAPGGGR VQELPVPSEA CAYLFTPEWL QGINKDRPTG RLSTCLLSAP SGIQRLPWAE
     LVCPRFVHKE GLMVGHQPST LPPELPSGPP GLPSSPLPEE VLGTRSPGDG HNAPAEGPEG
     EYVELLEVTL PVRGSPVDAE ASGLSRTRTV PARKSTGGKG RHRRHRAWMN QKGLGSRDQD
     GTRPPGEGSS TGASSDSPSG AEADPDATAL QASEPPAEAL GEAPESCLLS GEAVGGVGQG
     AEGPPGTPRR TGKGNRRKKR AAGRGAGSRG GEGTSLSPRD KEETRQQEVL VSLPSPSEQE
     PAECSLVKEK EDSGKQESES KEELKPADEK EPARPEDYEP PEEEIRESEK EELTPQCTAG
     STGPEWFPSE PSTQPLETVQ NVKGDSLPEE TPPVSVLDDP VVAWDLMASG FFVLTGGVDQ
     TGRALLTITP PPPCLPEESS PSQETLSTAL RYLHSLLRPD LQLLGLTILL DLRKAPPLPP
     ALLPALSQLQ DSGEPPLIQR LVILIHEDPP AELCGFQGAE LLSEKDLKRV AKPEELQWDL
     GGHRDLSPNH WAEIHQEVAR LCTLCQGVLT SVRQAIEELE GTAEPKEEEA VGMPEPLQKV
     LADPRLTALQ RNGGAILMRL RSAHSSKLEG PGPAELYQEV DEAIHQLVRL SNLRVQQQEE
     RQRLRQVQQV LQWLSGPGEE QLASFSMPGN SLSVLQETEL RFRAFSTEVQ ERLVQAREAL
     ALEEDLTSQK VLDIFEQRLE QAESGLHRAL RLQRFFQQAH EWVDEGSARL AGAGSGREAL
     LAALALRRAP EPSAGTFQEM RALALDLGSP AALREWGRCR ARCQELERRI QQQLGEEASP
     RSHRRRRADS ASSAGAQHGA HSPSPSLSSL LLPSSPGPRA APSHCSLTPC GEDYEEEGLE
     LAPETDGRPP RAVLIRGLEV TSTEVVDRTC SPREHVLLGR AGGPDGPWGI GTPRMERKRS
     ISAQQRLVSE LIACEQEYVT TLNEPVPLPG PELTPELRCT WAAALSVRER LRSFHGTHFL
     QELQGCAAHP LRIGACFLRH GDQFNLYAQF VKHRHKLESG LAALTPSVKG SMESSPCLPR
     ALQQPLEQLA RYGQLLEELL REAGPELSSE RQALRAAVQL LQEQEARGRD LLAVEAVRGC
     EIDLKEQGQL LHRDPFTVIC GRKKCLRHVF LFEDLLLFSK LKGSEGGSET FVYKQAFKTA
     DMGLTENIGD SGLCFELWFR RRRAREAYTL QATSPETKLK WTSSIAQLLW RQAAHNKELR
     VQQMVSMGIG NKPFLDIKAL GERTLSALLT GRAARTRASV AVSSFEHAGP SLPGLSPGAC
     SLPARVEEEA WDLDVKQISL ASETLDSSGD VSPGPRNSPS LQPPSPGSST PALTSGGILG
     LSRQSHSRAL SDPTTPL
//
ID   SC31A_MOUSE             Reviewed;        1230 AA.
AC   Q3UPL0; Q3UYH3; Q6IQZ3; Q7TQJ7; Q811J4;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Protein transport protein Sec31A;
DE   AltName: Full=SEC31-like protein 1;
DE   AltName: Full=SEC31-related protein A;
GN   Name=Sec31a; Synonyms=Sec31l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 286-1230 (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-612 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Component of the coat protein complex II (COPII) which
CC       promotes the formation of transport vesicles from the endoplasmic
CC       reticulum (ER). The coat has two main functions, the physical
CC       deformation of the endoplasmic reticulum membrane into vesicles
CC       and the selection of cargo molecules (By similarity).
CC   -!- SUBUNIT: COPII is composed of at least 5 proteins: the SEC23/24
CC       complex, the SEC13/31 complex and SAR1. Interacts with PDCD6 in a
CC       calcium-dependent manner (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasmic
CC       vesicle, COPII-coated vesicle membrane; Peripheral membrane
CC       protein; Cytoplasmic side (By similarity). Endoplasmic reticulum
CC       membrane; Peripheral membrane protein (By similarity).
CC       Note=Associates with membranes in a GTP-dependent manner (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3UPL0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UPL0-2; Sequence=VSP_026753;
CC       Name=3;
CC         IsoId=Q3UPL0-3; Sequence=VSP_026752;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the WD repeat SEC31 family.
CC   -!- SIMILARITY: Contains 7 WD repeats.
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DR   EMBL; BC043942; AAH43942.1; -; mRNA.
DR   EMBL; BC054358; AAH54358.1; -; mRNA.
DR   EMBL; BC071249; AAH71249.1; -; mRNA.
DR   EMBL; AK134681; BAE22239.1; -; mRNA.
DR   EMBL; AK143455; BAE25385.1; -; mRNA.
DR   IPI; IPI00403027; -.
DR   IPI; IPI00853859; -.
DR   IPI; IPI00938457; -.
DR   RefSeq; NP_081245.1; NM_026969.1.
DR   UniGene; Mm.18634; -.
DR   UniGene; Mm.403586; -.
DR   ProteinModelPortal; Q3UPL0; -.
DR   SMR; Q3UPL0; 4-412.
DR   STRING; Q3UPL0; -.
DR   PhosphoSite; Q3UPL0; -.
DR   PRIDE; Q3UPL0; -.
DR   Ensembl; ENSMUST00000067989; ENSMUSP00000070702; ENSMUSG00000035325.
DR   Ensembl; ENSMUST00000094578; ENSMUSP00000092157; ENSMUSG00000035325.
DR   Ensembl; ENSMUST00000112922; ENSMUSP00000108544; ENSMUSG00000035325.
DR   GeneID; 69162; -.
DR   KEGG; mmu:69162; -.
DR   UCSC; uc008yhk.1; mouse.
DR   CTD; 69162; -.
DR   MGI; MGI:1916412; Sec31a.
DR   GeneTree; ENSGT00390000003175; -.
DR   HOGENOM; HBG355108; -.
DR   HOVERGEN; HBG055626; -.
DR   InParanoid; Q3UPL0; -.
DR   OrthoDB; EOG4WDDB3; -.
DR   ArrayExpress; Q3UPL0; -.
DR   Bgee; Q3UPL0; -.
DR   CleanEx; MM_SEC31A; -.
DR   Genevestigator; Q3UPL0; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 4.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW   Endoplasmic reticulum; ER-Golgi transport; Membrane; Phosphoprotein;
KW   Protein transport; Repeat; Transport; WD repeat.
FT   CHAIN         1   1230       Protein transport protein Sec31A.
FT                                /FTId=PRO_0000295148.
FT   REPEAT       64    111       WD 1.
FT   REPEAT      120    160       WD 2.
FT   REPEAT      166    206       WD 3.
FT   REPEAT      209    254       WD 4.
FT   REPEAT      258    298       WD 5.
FT   REPEAT      301    342       WD 6.
FT   REPEAT      673    714       WD 7.
FT   REGION      161    470       Interaction with SEC13 (By similarity).
FT   REGION      799   1123       Interaction with PDCD6 (By similarity).
FT   COMPBIAS    832   1101       Pro-rich.
FT   MOD_RES     526    526       Phosphoserine.
FT   MOD_RES     531    531       Phosphoserine (By similarity).
FT   MOD_RES     798    798       Phosphoserine (By similarity).
FT   MOD_RES    1171   1171       Phosphothreonine (By similarity).
FT   MOD_RES    1173   1173       Phosphoserine (By similarity).
FT   VAR_SEQ       1    923       Missing (in isoform 3).
FT                                /FTId=VSP_026752.
FT   VAR_SEQ     503    541       Missing (in isoform 2).
FT                                /FTId=VSP_026753.
FT   CONFLICT    820    820       S -> P (in Ref. 1; AAH54358).
SQ   SEQUENCE   1230 AA;  133569 MW;  B6119EFDEF121A76 CRC64;
     MKLKEIDRTA MQAWSPAQNH PIYLATGTSA QQLDATFSTN ASLEIFELDL SDPSLDMKSC
     ATFSSSHRYH KLIWGPHKMD SKGDVSGVLI AGGENGNIIL YDPSKIIAGD KEVVIAQKDK
     HTGPVRALDV NIFQTNLVAS GANESEIYIW DLNNFATPMT PGAKTQPPED ISCIAWNRQV
     QHILASASPS GRATVWDLRK NEPIIKVSDH SNRMHCSGLA WHPDVATQMV LASEDDRLPV
     IQMWDLRFAS SPLRVLENHA RGILAVAWSM ADPELLLSCG KDAKILCSNP NTGEVLYELP
     TNTQWCFDIQ WCPRNPAVLS AASFDGRISV YSIMGGSIDG LRQKQVDKLS SSFGNLDPFG
     TGQPLPPLQI PQQSAQHSIV LPLKKPPKWI RRPVGASFSF GGKLVTFESV AVPLQQGAEQ
     QRRQPVFISQ VVTEKDFLNR SAQLQHAVQS QGFIGYCQKK IEASQTEFEK NVWSFLKVNF
     EEDSRGKYLE LLGYRKEDLG QKIALALNKV DGPDVALKDS DQVAQSDGEE SPAAEEQLLG
     ERIKEEKQEC DFLPSAGGTF NISVSGDIDG LITRALLTGN FESAVDLCLH DNRMADAIIL
     AIAGGQELLA QTQKKYFAKS QSKITRLITA VVMKNWREIV ESCDLKNWRE ALAAVLTYAK
     PDEFSALCDL LGTRLEREGD SLLRTQACLC YICAGNVERL VACWTKAQDG SSPLSLQDLI
     EKVVILRKAV QLTQALDTNT VGALLAEKMS QYASLLAAQG SIAAALAFLP DNTNQPNIVQ
     LRDRLCKAQG KPVSGQESSQ SPYERQPLSK GRPGPVAGHS QMPRVQTQQY YPHGENPPPP
     GFIMQGNVIP NPAAPLPTAP GHMPSQLPPY PQPQPYQPAQ QYSFGTGGAA AYRPQQPVAP
     PASNAYPNTP YISPVASYSG QPQMYTAQQA SSPTSSSAAS FPPPSSGASF QHGGPGAPPS
     SSAYALPPGT TGTPPAASEL PASQRTENQS FQDQASILEG PQNGWNDPPA LNRVPKKKKM
     PENFMPPVPI TSPIMNPSGD PQSQGLQQQP STPGPLSSHA SFPQQHLAGG QPFHGVQQPL
     AQTGMPPSFS KPNTEGAPGA PIGNTIQHVQ ALPTEKITKK PIPEEHLILK TTFEDLIQRC
     LSSATDPQTK RKLDDASKRL EFLYDKLREQ TLSPTIINGL HSIARSIETR NYSEGLSVHT
     HIVSTSNFSE TSAFMPVLKV VLSQASKLGV
//
ID   Q3UPL4_MOUSE            Unreviewed;       356 AA.
AC   Q3UPL4;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-FEB-2011, entry version 33.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Jakmip2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK143449; BAE25381.1; -; mRNA.
DR   IPI; IPI00944045; -.
DR   UniGene; Mm.134602; -.
DR   STRING; Q3UPL4; -.
DR   Ensembl; ENSMUST00000097589; ENSMUSP00000095196; ENSMUSG00000024502.
DR   MGI; MGI:1923467; Jakmip2.
DR   eggNOG; roNOG13757; -.
DR   GeneTree; ENSGT00390000002812; -.
DR   HOVERGEN; HBG054249; -.
DR   ArrayExpress; Q3UPL4; -.
DR   Bgee; Q3UPL4; -.
DR   Genevestigator; Q3UPL4; -.
PE   2: Evidence at transcript level;
FT   NON_TER     356    356
SQ   SEQUENCE   356 AA;  41423 MW;  34AE5F24BABA1A05 CRC64;
     MSKKGRNKGE KPEALIVALQ AANEDLRTKL TDIQIELHQE KSKVSKLERE KTQEAKRIRE
     LEQRKHTVLV TELKAKLHEE KMKELQAVRE NLIKQHEQEM SRTVKVRDGE IQRLKSALCA
     LRDGSSDKVR TALTIEAREE ARKQFDAERL KLLQEITDLK TAKKQVDEAL SNMIQADKIK
     AGDLRSEHQS HQEAISKIKW ESERDIRRLM DEIKAKDRII FSLEKELETQ TGYVQKLQLQ
     KEALDEQLFL VKEAECNMSS PKREIPGRAG DGSEHCSSPD LRRNQKRIAE LNATIRKLED
     RNTLLGDERN ELLKRVRETE KQCKPLLERN KCLAKRNDEL MVSLQRMEEK LKAVTK
//
ID   CK096_MOUSE             Reviewed;         249 AA.
AC   Q3UPL5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   30-NOV-2010, entry version 25.
DE   RecName: Full=Uncharacterized protein C11orf96 homolog;
DE   AltName: Full=Protein Ag2 homolog;
GN   Name=Ag2; Synonyms=Gm13889;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 27-249.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-179 AND THR-218, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
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DR   EMBL; AL772372; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK143447; BAE25380.1; -; mRNA.
DR   IPI; IPI00654146; -.
DR   RefSeq; NP_001138506.1; NM_001145034.1.
DR   UniGene; Mm.272498; -.
DR   PhosphoSite; Q3UPL5; -.
DR   PRIDE; Q3UPL5; -.
DR   GeneID; 620695; -.
DR   KEGG; mmu:620695; -.
DR   MGI; MGI:3652053; Gm13889.
DR   HOVERGEN; HBG100438; -.
DR   Genevestigator; Q3UPL5; -.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    249       Uncharacterized protein C11orf96 homolog.
FT                                /FTId=PRO_0000320642.
FT   COMPBIAS     54    119       Pro-rich.
FT   MOD_RES     179    179       Phosphothreonine.
FT   MOD_RES     196    196       Phosphoserine (By similarity).
FT   MOD_RES     218    218       Phosphothreonine.
SQ   SEQUENCE   249 AA;  27072 MW;  594B8D27B07B11A5 CRC64;
     MAFAVIRACS RVGRGGLYKR LGGPPRGTRR QRQRPRQGRQ GASRSIAEQR SAAPRPPTGP
     PARYPSPAAS ARASEARRHP AADLDPPPGE PQAVASRGTP EPRPPPESPG APPPPGSAPA
     DGAMAAAKPG ELMGICSSYQ AVMPHFVCLT DEFPQPVRPA KLPKGKGRLR RPRQSRFKTQ
     PVTFDEIQEV EEEGVSPMEE EKAKKSFLQS LECLRRSTQS LSLQREPLGQ LQTEEQPGLQ
     RLRLGPVRR
//
ID   IQGA2_MOUSE             Reviewed;        1575 AA.
AC   Q3UQ44;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Ras GTPase-activating-like protein IQGAP2;
GN   Name=Iqgap2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1389, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Binds to activated CDC42 and RAC1 but does not seem to
CC       stimulate their GTPase activity. Associates with calmodulin.
CC   -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC   -!- SIMILARITY: Contains 3 IQ domains.
CC   -!- SIMILARITY: Contains 1 Ras-GAP domain.
CC   -!- SIMILARITY: Contains 1 WW domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AK147360; Type=Frameshift; Positions=408;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK142813; BAE25199.1; -; mRNA.
DR   EMBL; AK147360; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00406193; -.
DR   RefSeq; NP_081987.1; NM_027711.1.
DR   UniGene; Mm.38878; -.
DR   HSSP; P21359; 1NF1.
DR   ProteinModelPortal; Q3UQ44; -.
DR   SMR; Q3UQ44; 25-188, 875-1252, 1477-1571.
DR   STRING; Q3UQ44; -.
DR   PhosphoSite; Q3UQ44; -.
DR   PRIDE; Q3UQ44; -.
DR   Ensembl; ENSMUST00000068603; ENSMUSP00000067685; ENSMUSG00000021676.
DR   GeneID; 544963; -.
DR   KEGG; mmu:544963; -.
DR   UCSC; uc007rmo.1; mouse.
DR   CTD; 544963; -.
DR   MGI; MGI:2449975; Iqgap2.
DR   HOGENOM; HBG445894; -.
DR   HOVERGEN; HBG052143; -.
DR   InParanoid; Q3UQ44; -.
DR   OMA; EQINYYD; -.
DR   OrthoDB; EOG4P8FH6; -.
DR   NextBio; 412173; -.
DR   ArrayExpress; Q3UQ44; -.
DR   Bgee; Q3UQ44; -.
DR   Genevestigator; Q3UQ44; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005099; F:Ras GTPase activator activity; IEA:InterPro.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001936; RasGAP.
DR   InterPro; IPR000593; RasGAP_C.
DR   InterPro; IPR023152; RasGAP_CS.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 1.
DR   Gene3D; G3DSA:1.10.506.10; RasGAP; 2.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF00612; IQ; 2.
DR   Pfam; PF00616; RasGAP; 1.
DR   Pfam; PF03836; RasGAP_C; 1.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00015; IQ; 3.
DR   SMART; SM00323; RasGAP; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS50096; IQ; 3.
DR   PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Calmodulin-binding; Phosphoprotein; Repeat.
FT   CHAIN         1   1575       Ras GTPase-activating-like protein
FT                                IQGAP2.
FT                                /FTId=PRO_0000354074.
FT   DOMAIN       41    156       CH.
FT   DOMAIN      594    627       WW.
FT   DOMAIN      690    719       IQ 1.
FT   DOMAIN      720    749       IQ 2.
FT   DOMAIN      750    779       IQ 3.
FT   DOMAIN      917   1150       Ras-GAP.
FT   MOD_RES      16     16       Phosphoserine.
FT   MOD_RES    1389   1389       Phosphoserine.
FT   MOD_RES    1471   1471       N6-acetyllysine (By similarity).
FT   MOD_RES    1474   1474       N6-acetyllysine (By similarity).
FT   CONFLICT   1275   1275       K -> R (in Ref. 1; BAE25199).
FT   CONFLICT   1447   1447       K -> E (in Ref. 1; BAE25199).
SQ   SEQUENCE   1575 AA;  180528 MW;  5EF176042E4D158F CRC64;
     MPHEELPSLQ RPRYGSIVDD ERLSAEEMDE RRRQNIAYEY LCHLEEAKRW MEVCLVEELP
     PTTELEEGLR NGVYLAKLAK FFAPKMVSEK KIYDVEQTRY KKSGLHFRHT DNTVQWLRAM
     EAIGLPKIFY PETTDVYDRK NIPRMIYCIH ALSLYLFKLG IAPQIQDLLG KVDFTEEEIS
     NMRKELEKYG IQMPAFSKIG GILANELSVD EAALHAAVIA INEAIEKGVA KQTIITLRNP
     NAVLTCVDDS LSQEYQKELW EAKKKKEESA KLKNSCISEE ERDAYEELLT QAEIQSNIST
     VNRMAAVDHI NAVLQEGDPE NTLLALKKPE AQLPAVYPFA AVMYQNELFN LQKQNTSNYL
     AHEELLIAVE MLSAVALLNQ ALESSDLVAV QNQLRSPTIG FNNLDEAHVD RYADALLSVK
     QEALSQGQDT LSWNEIQNCI DMINNQIQEE NDRMVVLGYI NEAIDAGNPL KTLDTLLLPT
     ANIRDVDPDC AQHYQDVLFY TKSQKLGDPK NVSKVLWLDE IQQAINEANV DENRAKQWVT
     LVVDVNECLD RKQSDHILTA LKSSPSNIHN ILPECANKYY DTLVKAKESK TDNESSEGSW
     VTLNVQEKYN YYYNTDSKEG SWVPPELCLS KESWLTGEEI EDIVEEVTSD YIREKLWSAS
     EDLLVRFEAT TLGPALREEF EARKAFLYEQ TESVVKIQAF WKGFKQRQEY LHRQQVFAGN
     VDSVVKIQSW FRMVTARKSY LSRLRYFEDH KNEIVKIQSL LRASKARDDY KALVGSENPP
     LTVIRKFVYL LDQSDLDFQE ELEVARLREE VVTKIRANQQ LEKDLNLMDI KIGLLVKNRI
     TLEDVISHRK KLNKKKGGEI EILNNTDNKG IKSLSKERRK TLETYQQLFY LLQTKPSYLA
     KLIFQMPQNK STKFMDTVIF TLYNYASNQR EEYLLLKLFK TALEEEIKSK VDQVQDIVTG
     NPTVIKMVVS FNRGARGQNT LRQLLAPVVK EIIEDKALVI NTNPVEVYKA WVNQLETQTG
     EASKLPYDVT TEQALTYPEV KNKLEASIEN LRKVTDKVLG SIISSLDLLP YGLRYIAKVL
     KNSIREKFPD ATEEELLKIV GNLLYYRYMN PAIVAPDGFD IIDMTAGGQI NSNQRRNLGS
     VAKVLQHAAS NKLFEGENEH LSSMNNYLSE TYQEFRKYFQ EACDVPEPEE KFNMDKYTDL
     VTVSKPVIYI SIEEIINTHL LLLEHQDAIA TEKSDLLNEL LESLGEVPTV ESFLGEGAVD
     PNDPNKENTL NQLSKTEISL SLTSKYDVKD GEAVDGRSLM IKTKKLIIDV TRNQPGSTLT
     EILETPATGQ QELEHAKDME SRAVVDSRTP EEGKQSQAVI EDARLPLEQK KRKIQRNLRT
     LEQTGHVSSK NKYQDILNEI AKDIRNQRIH RKLRKAELSK LQQTLNALNK KAAFYEDQIN
     YYDTYIKTCV DNLKRKNSRR SIKLDGKAEP KGTKRVKPVR YTAAKLHDKG VLLGIDDLQT
     NQFKNVMFDI IATEDMGIFD VRSKFLGVEM EKVQLNIQDL LQMQYEGVAV MKMFDKVKVN
     VNLLIYLLNK KFYGK
//
ID   Q3UQA0_MOUSE            Unreviewed;       498 AA.
AC   Q3UQA0;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   11-JAN-2011, entry version 39.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Il6st;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK142637; BAE25142.1; -; mRNA.
DR   IPI; IPI00120155; -.
DR   UniGene; Mm.4364; -.
DR   ProteinModelPortal; Q3UQA0; -.
DR   STRING; Q3UQA0; -.
DR   Ensembl; ENSMUST00000070731; ENSMUSP00000064205; ENSMUSG00000021756.
DR   MGI; MGI:96560; Il6st.
DR   HOVERGEN; HBG052119; -.
DR   InParanoid; Q3UQA0; -.
DR   ArrayExpress; Q3UQA0; -.
DR   Bgee; Q3UQA0; -.
DR   Genevestigator; Q3UQA0; -.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005977; P:glycogen metabolic process; IMP:MGI.
DR   GO; GO:0048711; P:positive regulation of astrocyte differentiation; IMP:MGI.
DR   GO; GO:0008593; P:regulation of Notch signaling pathway; IDA:MGI.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Pfam; PF00041; fn3; 1.
DR   SMART; SM00060; FN3; 2.
DR   SUPFAM; SSF49265; FN_III-like; 2.
DR   PROSITE; PS50853; FN3; 2.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   498 AA;  55421 MW;  702EF2BDF18C7094 CRC64;
     TAAYSVVNLK AFPKDNLLWV EWTPPPKPVS KYILEWCVLS ENAPCVEDWQ QEDATVNRTH
     LRGRLLESKC YQITVTPVFA TGPGGSESLK AYLKQAAPAR GPTVRTKKVG KNEAVLAWDQ
     IPVDDQNGFI RNYSISYRTS VGKEMVVHVD SSHTEYTLSS LSSDTLYMVR MAAYTDEGGK
     DGPEFTFTTP KFAQGEIEAI VVPVCLAFLL TTLLGVLFCF NKRDLIKKHI WPNVPDPSKS
     HIAQWSPHTP PRHNFNSKDQ MYSDGNFTDV SVVEIEANNK KPCPDDLKSV DLFKKEKVST
     EGHSSGIGGS SCMSSSRPSI SSNEENESAQ STASTVQYST VVHSGYRHQV PSVQVFSRSE
     STQPLLDSEE RPEDLQLVDS VDGGDEILPR QPYFKQNCSQ PEACPEISHF ERSNQVLSGN
     EEDFVRLKQQ QVSDHISQPY GSEQRRLFQE GSTADALGTG ADGQMERFES VGMETTIDEE
     IPKSYLPQTV RQGGYMPQ
//
ID   FCHO2_MOUSE             Reviewed;         809 AA.
AC   Q3UQN2; Q3UJ91; Q7TMS9; Q8C0I2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 44.
DE   RecName: Full=FCH domain only protein 2;
GN   Name=Fcho2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Amnion, Heart, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-402; SER-403
RP   AND SER-508, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May play a role in membrane remodeling by imposing and
CC       stabilizing particular membrane curvatures (By similarity).
CC   -!- SUBUNIT: Homodimer; disulfide-linked (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3UQN2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UQN2-2; Sequence=VSP_021912, VSP_021913;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q3UQN2-3; Sequence=VSP_021914, VSP_021915;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 FCH domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH52456.1; Type=Erroneous initiation;
CC       Sequence=AAH53718.1; Type=Erroneous initiation;
CC       Sequence=BAC27226.1; Type=Erroneous initiation;
CC       Sequence=BAC27226.1; Type=Frameshift; Positions=11;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK031041; BAC27226.1; ALT_INIT; mRNA.
DR   EMBL; AK142282; BAE25007.1; -; mRNA.
DR   EMBL; AK146566; BAE27264.1; -; mRNA.
DR   EMBL; BC052456; AAH52456.1; ALT_INIT; mRNA.
DR   EMBL; BC053718; AAH53718.1; ALT_INIT; mRNA.
DR   IPI; IPI00762033; -.
DR   IPI; IPI00816870; -.
DR   IPI; IPI00816923; -.
DR   RefSeq; NP_766179.2; NM_172591.3.
DR   UniGene; Mm.23928; -.
DR   ProteinModelPortal; Q3UQN2; -.
DR   SMR; Q3UQN2; 3-274.
DR   DIP; DIP-29489N; -.
DR   STRING; Q3UQN2; -.
DR   PhosphoSite; Q3UQN2; -.
DR   PRIDE; Q3UQN2; -.
DR   Ensembl; ENSMUST00000040340; ENSMUSP00000042959; ENSMUSG00000041685.
DR   Ensembl; ENSMUST00000109403; ENSMUSP00000105030; ENSMUSG00000041685.
DR   GeneID; 218503; -.
DR   KEGG; mmu:218503; -.
DR   UCSC; uc007rpb.1; mouse.
DR   CTD; 218503; -.
DR   MGI; MGI:3505790; Fcho2.
DR   GeneTree; ENSGT00510000046419; -.
DR   HOGENOM; HBG358275; -.
DR   HOVERGEN; HBG081524; -.
DR   InParanoid; Q3UQN2; -.
DR   OrthoDB; EOG4C87S0; -.
DR   NextBio; 376323; -.
DR   ArrayExpress; Q3UQN2; -.
DR   Bgee; Q3UQN2; -.
DR   CleanEx; MM_FCHO2; -.
DR   Genevestigator; Q3UQN2; -.
DR   GermOnline; ENSMUSG00000041685; Mus musculus.
DR   InterPro; IPR001060; FCH.
DR   InterPro; IPR018808; SAFF_domain.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF10291; SAFF; 1.
DR   SMART; SM00055; FCH; 1.
DR   PROSITE; PS50133; FCH; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Disulfide bond; Phosphoprotein.
FT   CHAIN         1    809       FCH domain only protein 2.
FT                                /FTId=PRO_0000266006.
FT   DOMAIN        4     85       FCH.
FT   COILED       87    156       Potential.
FT   COMPBIAS    444    447       Poly-Ser.
FT   COMPBIAS    507    518       Poly-Ser.
FT   MOD_RES     387    387       Phosphoserine (By similarity).
FT   MOD_RES     394    394       Phosphoserine.
FT   MOD_RES     402    402       Phosphoserine.
FT   MOD_RES     403    403       Phosphoserine.
FT   MOD_RES     487    487       Phosphoserine (By similarity).
FT   MOD_RES     508    508       Phosphoserine.
FT   MOD_RES     509    509       Phosphoserine (By similarity).
FT   MOD_RES     510    510       Phosphoserine (By similarity).
FT   DISULFID    147    147       Interchain (with C-273) (By similarity).
FT   DISULFID    273    273       Interchain (with C-147) (By similarity).
FT   VAR_SEQ     392    394       RHS -> GFL (in isoform 2).
FT                                /FTId=VSP_021912.
FT   VAR_SEQ     395    809       Missing (in isoform 2).
FT                                /FTId=VSP_021913.
FT   VAR_SEQ     404    414       NEELTKSKPSS -> SKFDIGIGYFM (in isoform
FT                                3).
FT                                /FTId=VSP_021914.
FT   VAR_SEQ     415    809       Missing (in isoform 3).
FT                                /FTId=VSP_021915.
FT   CONFLICT     13     13       E -> K (in Ref. 1; BAC27226).
SQ   SEQUENCE   809 AA;  88734 MW;  79FA8C2AFE6B606B CRC64;
     MVMAHFVENF WGEKNNGFDV LYHNMKHGQI STKELADFVR ERATIEEAYS RSMTKLAKSA
     SNYSQLGTFA PMWDVFKTST EKLANCHLDL VRKLQELIKE VQKYGEEQVK SHKKTKEEVA
     GTLEAVQAIQ NITQALQKSK ENYTAKCVEQ ERLKKEGATQ REIEKAAVKS KKATDTYKLY
     VEKYALTKAD FEQKMTETAQ KFQDIEETHL IHIKEIIGSL SNAVKEIHLQ IGQVHEEFIN
     NMANTTIESL IQKFAESKGT GKERPGLIEF EECDPASAVE GIKPRKRKTF ALPGIIKKEK
     DAESVECPDA DSLNIPDVDE EGFSIKPEAN QNDTKENHFY SSSDSDSEDE EPKRYRIEIK
     PAHPNNLHHT MASLDELKVS IGNITLSPAV SRHSPVQMNR NSSNEELTKS KPSSLPTEKG
     TNDLLAWDPL FGSSLESSSA PLTSSSSARP TTPLSLGTLV PPPRPASRPK LASGKLSGIN
     EIPRPFSPPV TSNTSPPPTA PLARAESSSS ISSSASLSAA NTPTVGVSRG PSPVSLGNQD
     TLPVAIALTE SVNAYFKGAD PTKCIVKITG DVTISFPSGI IKVFTSNPSP AVLCFRVKNI
     SRLEQILPNS QLVFSDPSQC DSNTKDFWMN MQAVTIYLKK LSEQNPAASY YNVDVLKYQV
     SSNGIQSTPL NLATYWKCSA STTDLRVDYK YNPEAMVAPS VLSNIQVVVP VDGGVTNMQS
     LPPAIWNAEQ MKAFWKLSGI SEKSDSGGSG SLRAKFDLSE GPSKPTTLAV QFLSEGNTLS
     GVDIELVGTG YRLSLVKKRF ATGRYLADC
//
ID   Q3UQP3_MOUSE            Unreviewed;       518 AA.
AC   Q3UQP3;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   SubName: Full=Zinc finger and BTB domain containing 3;
GN   Name=Zbtb3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
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CC   -----------------------------------------------------------------------
DR   EMBL; BC119186; AAI19187.1; -; mRNA.
DR   EMBL; BC119188; AAI19189.1; -; mRNA.
DR   EMBL; AK142256; BAE24996.1; -; mRNA.
DR   IPI; IPI00652610; -.
DR   RefSeq; NP_001091707.1; NM_001098237.1.
DR   RefSeq; NP_598520.1; NM_133759.3.
DR   UniGene; Mm.23423; -.
DR   ProteinModelPortal; Q3UQP3; -.
DR   SMR; Q3UQP3; 1-121.
DR   PRIDE; Q3UQP3; -.
DR   Ensembl; ENSMUST00000088094; ENSMUSP00000085415; ENSMUSG00000071661.
DR   GeneID; 75291; -.
DR   KEGG; mmu:75291; -.
DR   UCSC; uc008gnb.1; mouse.
DR   CTD; 75291; -.
DR   MGI; MGI:1922541; Zbtb3.
DR   eggNOG; roNOG05258; -.
DR   HOVERGEN; HBG059113; -.
DR   InParanoid; Q3UQP3; -.
DR   OMA; HIRKAHN; -.
DR   PhylomeDB; Q3UQP3; -.
DR   NextBio; 342652; -.
DR   ArrayExpress; Q3UQP3; -.
DR   Bgee; Q3UQP3; -.
DR   Genevestigator; Q3UQP3; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR013069; BTB_POZ.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 2.
DR   Pfam; PF00651; BTB; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   2: Evidence at transcript level;
KW   Metal-binding; Nucleus; Zinc.
SQ   SEQUENCE   518 AA;  55901 MW;  79D62A5BB424E081 CRC64;
     MEFPEHSQQL LQSLREQRSQ GFLCDCTVMV GSTQFLAHRA VLASCSPFFQ LFYKERELDK
     RDLVCIHNEI VTAPAFGLLL DFMYAGQLAL RGDTPLEDVL AAASYLHMND IVKVCKQRLQ
     ARALAEADST KKEEETNPAS LEFLSGSSRG PQPLLASVEP SARWNKEEWK GPATPLPIAH
     PADEPPVSGG ADTTQPSMEV DSSHLRAPPP PVADVSVSLA SPSSSTETIP VNYFSSGLPG
     VSVEPLTPLD VVPESLRVVE PRDTGGPLQG FYPPAPAPPP APAPVLSQAP APVEAELVQV
     KVEAIVISDE EADLSEEQPH RSEGLFPPGG AVYGGQPSQA EAFEEPGATG LEEVGPSDHF
     LPPESHLPYH LLPGPGQYHR GLVTSPLPAP AALHEPLYPP PEYEAAQGSF GNFTEDVPTC
     KTCGKTFSCS YTLRRHATVH TRERPYECRY CLRSYTQSGD LYRHIRKAHN EDLAKRSKPD
     PEASTILGVQ PLSGSQTTER HSSGGGGPPK EFALGPKN
//
ID   Q3UR42_MOUSE            Unreviewed;       735 AA.
AC   Q3UR42;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-FEB-2011, entry version 48.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Dhx9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK141824; BAE24846.1; -; mRNA.
DR   IPI; IPI00339468; -.
DR   UniGene; Mm.20000; -.
DR   STRING; Q3UR42; -.
DR   Ensembl; ENSMUST00000042141; ENSMUSP00000038135; ENSMUSG00000042699.
DR   UCSC; uc007daa.1; mouse.
DR   MGI; MGI:108177; Dhx9.
DR   GeneTree; ENSGT00550000074257; -.
DR   HOVERGEN; HBG039429; -.
DR   InParanoid; Q3UR42; -.
DR   ArrayExpress; Q3UR42; -.
DR   Bgee; Q3UR42; -.
DR   Genevestigator; Q3UR42; -.
DR   GO; GO:0005730; C:nucleolus; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0034605; P:cellular response to heat; IDA:MGI.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR001159; Ds-RNA-bd.
DR   InterPro; IPR014720; dsRNA-bd-like.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   Gene3D; G3DSA:3.30.160.20; dsRNA-bd-like; 2.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00035; dsrm; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00358; DSRM; 2.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS50137; DS_RBD; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   2: Evidence at transcript level;
FT   NON_TER     735    735
SQ   SEQUENCE   735 AA;  82471 MW;  1B31EC77C19AAB53 CRC64;
     MGDIKNFLYA WCGKRKMTPA YEIRAVGNKN RQKFMCEVRV EGFNYAGMGN STNKKDAQSN
     AARDFVNYLV RINEVKSEEV PAVGIVPPPP ILSDTSDSTA SAAEGLPAPM GGPLPPHLAL
     KAEAENNSGV ESSGYGSPGP TWDRGANLKD YYSRKEEQEV QATLESEEVD LNAGLHGNWT
     LENAKARLNQ YFQKEKIQGE YKYTQVGPDH NRSFIAEMTI YIKQLGRRIF AREHGSNKKL
     AAQSCALSLV RQLYHLGVIE AYSGLTKKKE GERVEPYKVF LSPDLELQLQ NVVQELDLEI
     VPPPVDPSMP VILNIGKLAH FEPSQRQNAV GVVPWSPPQS NWNPWTSSNI DEGPLAYAST
     EQISMDLKNE LTYQMEQDHN LQSVLQEREL LPVKKFEAEI LEAISSNSVV IIRGATGCGK
     TTQVPQYILD DFIQNDRAAE CNIVVTQPRR ISAVAVAERV AYERGEEPGK SCGYSVRFES
     ILPRPHASIM FCTVGVLLRK LEAGIRGISH VIVDEIHERD INTDFLLVVL RDVVLAYPEV
     RIVLMSATID TTMFCEYFFN CPIIEVYGRT FPVQEYFLED CIQMTQFIPP PKDKKKKDKE
     DDGGEDDDAN CNLICGDEYG PETKLSMSQL NEKETPFELI EALLKYIETL NVPGAVLVFL
     PGWNLIYTMQ KHLENNSHFG SHRYQILPLH SQIPREEQRK VFDPVPDGVT KVILSTNIAE
     TSITINDVVY VIDSC
//
ID   VW5B2_MOUSE             Reviewed;        1248 AA.
AC   Q3UR50; Q2TB01; Q80WS8; Q8BR57;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=von Willebrand factor A domain-containing protein 5B2;
GN   Name=Vwa5b2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1067-1248 (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3UR50-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UR50-2; Sequence=VSP_034144, VSP_034145;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q3UR50-5; Sequence=VSP_034141, VSP_034146;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 VIT domain.
CC   -!- SIMILARITY: Contains 1 VWFA domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI10636.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
CC       Sequence=AAI25017.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK045595; BAC32429.1; -; mRNA.
DR   EMBL; AK141799; BAE24838.1; -; mRNA.
DR   EMBL; AC087898; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC110635; AAI10636.1; ALT_SEQ; mRNA.
DR   EMBL; BC125016; AAI25017.1; ALT_SEQ; mRNA.
DR   IPI; IPI00224056; -.
DR   IPI; IPI00762078; -.
DR   IPI; IPI00896040; -.
DR   RefSeq; NP_001138425.1; NM_001144953.1.
DR   RefSeq; NP_872574.2; NM_182636.4.
DR   UniGene; Mm.40539; -.
DR   ProteinModelPortal; Q3UR50; -.
DR   PRIDE; Q3UR50; -.
DR   Ensembl; ENSMUST00000096197; ENSMUSP00000093911; ENSMUSG00000046613.
DR   Ensembl; ENSMUST00000100074; ENSMUSP00000097652; ENSMUSG00000046613.
DR   GeneID; 328643; -.
DR   KEGG; mmu:328643; -.
DR   UCSC; uc007yqb.1; mouse.
DR   CTD; 328643; -.
DR   MGI; MGI:2681859; Vwa5b2.
DR   eggNOG; maNOG15637; -.
DR   GeneTree; ENSGT00530000063006; -.
DR   HOVERGEN; HBG077219; -.
DR   InParanoid; Q3UR50; -.
DR   OMA; QCDRALE; -.
DR   OrthoDB; EOG4CZBF4; -.
DR   NextBio; 398382; -.
DR   ArrayExpress; Q3UR50; -.
DR   Bgee; Q3UR50; -.
DR   Genevestigator; Q3UR50; -.
DR   InterPro; IPR013694; VIT.
DR   InterPro; IPR002035; VWF_A.
DR   SMART; SM00327; VWA; 1.
DR   PROSITE; PS51468; VIT; 1.
DR   PROSITE; PS50234; VWFA; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing.
FT   CHAIN         1   1248       von Willebrand factor A domain-containing
FT                                protein 5B2.
FT                                /FTId=PRO_0000339303.
FT   DOMAIN        1    138       VIT.
FT   DOMAIN      354    527       VWFA.
FT   VAR_SEQ       1    944       Missing (in isoform 3).
FT                                /FTId=VSP_034141.
FT   VAR_SEQ     574    602       GQEPGWQSLAGSVFPSPEEVLSATSPGTE -> VGLGWGIP
FT                                GGPGGRKSLYLTRSLSLLRIL (in isoform 2).
FT                                /FTId=VSP_034144.
FT   VAR_SEQ     603   1248       Missing (in isoform 2).
FT                                /FTId=VSP_034145.
FT   VAR_SEQ     945    989       VDATTREVLPGALQVWSSDPAELSGMSASQDQLAAAPLSTA
FT                                VHSK -> MSASQDQLAAAPLSTAVHSKGRAQMQWIGHRWA
FT                                LDHLLVLGDPTV (in isoform 3).
FT                                /FTId=VSP_034146.
SQ   SEQUENCE   1248 AA;  133414 MW;  15918846B4268369 CRC64;
     MPGLYCPTSW TPLPLTDSCV RAYAKGPCLS LRARLTYHNP QPQPVEGVFV YPLAEAEVVS
     GFEAEAAGRR VSFQLHSRRR SQAACCRALG PGLGTSTPRR CAQGHLVLNL AQARSTLVLP
     TGLVAAAGTM TVTLCSSREL PSRPDGVMHV ALPTVFTPLA QPNLPGSPRS PGLCDDSPTS
     CFGVGSPEEE RPTWEQPTAT PDVFSGPARC PAPYTFSFEM LVTGPCLLAG LESPSHALRA
     DALPHASSAA TIRVTLAEGH QCDRALEILL HPSEPHQPHL MLETGSLSSA EYEAQVRARH
     DFQRLQQRDS GGERQVWFLQ RRFHKDILLN PVLVLNFCPD LSSKPGHLNA ATRELLFLLD
     GSGAGHKDAI VLAVKSLPAQ TLVNLAIFGT LVQPLFPESR PCSDDTVQLI CESIETLQTV
     NGPPDMLAVL DWALGQPQHR AYPRQMFLIT AASPTAATTH QALEFMRWHR GAARCFSFAL
     APACRQLLHD LSVLSRGQAY FLRPGERLQP KLVQALRKAL EPALSDISVD WFVPDAVEAL
     LTPREIPALY PGDQLLGYCS LFRVDGFRSH ALGGQEPGWQ SLAGSVFPSP EEVLSATSPG
     TEPTHTTEPL GTGTVSAELS SPWAVGDSEQ SMEALTDPVM DPGPNPSSDT AIWRRIFQSS
     YIREQYVLTH CSASPEPGPG STCSSESPGS QGPGSPSGSR PLDPPSQQGC RSLAWVEPAG
     SRSCPLPVPP PSPFKVGAMS AEVLGRRQRA ALAGRSLSSP SGRANPVPGR ARHPSLDAIP
     DGLGPEPGQQ LGQGLDDSGN LLSPAPLDWD MLMEPSFLFK PVPSSAESAP PAECLPPQAP
     RCHVVIRALC GEQPMCWEVG VGLEELWGPG DGSQPESLPM REAAWDQALH RLTAASVVQD
     NEQLALRGRA ETRAEQGRVR RSWLRAIQTS KVSSAPSCFT CPVAVDATTR EVLPGALQVW
     SSDPAELSGM SASQDQLAAA PLSTAVHSKG HQGGCSAGAW DLDLNDNSKS ALGEPISPTG
     DHHGLPHQPP ASSRLSLGRH RRLCSSNKGQ THENSNDGSN HDYLPLVRLQ EAPGSFRLDE
     PFCAAVCIPQ ERLCRASPFA AHRASLSPTS ASSPWAFLSP GIGQGDSATA SCSQSPSSGS
     EGPGQVDSGR GSDTEASEGM ERQDSSDLRG RTWATAVALA WLEHRCAAAF GEWELTASKA
     DCWLRAQHLP DGLDLTALKA AARGLFLLLR HWDQNLQLHL LCYSPSNV
//
ID   TGFA1_MOUSE             Reviewed;         860 AA.
AC   Q3UR70; Q8BKN4;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=Transforming growth factor-beta receptor-associated protein 1;
DE            Short=TGF-beta receptor-associated protein 1;
DE            Short=TRAP-1;
DE            Short=TRAP1;
GN   Name=Tgfbrap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Osteoclast, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Plays a role in the TGF-beta/activin signaling pathway.
CC       It associates with inactive heteromeric TGF-beta and activin
CC       receptor complexes, mainly through the type II receptor, and is
CC       released upon activation of signaling. May recruit SMAD4 to the
CC       vicinity of the receptor complex and facilitate its interaction
CC       with receptor-regulated Smads, such as SMAD2 (By similarity).
CC   -!- SUBUNIT: Interacts with TGFBR2 and ACVR2B; in the absence of
CC       ligand stimulation. Interacts with TGFBR1, ACVRL1, BMPR1A and
CC       ACVR1B; in the absence of ligand stimulation and to a less extent.
CC       Interacts with SMAD4; the interaction seems to be mutually
CC       exclusive with the interaction of SMAD4 and phosphorylated SMAD2.
CC       May interact with ALOX5 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Colocalizes with TGF-beta
CC       receptors in the absence of signaling (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UR70-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UR70-2; Sequence=VSP_034944, VSP_034945;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the TRAP1 family.
CC   -!- SIMILARITY: Contains 1 CNH domain.
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DR   EMBL; AK051333; BAC34606.1; -; mRNA.
DR   EMBL; AK141742; BAE24818.1; -; mRNA.
DR   EMBL; AK159332; BAE34997.1; -; mRNA.
DR   EMBL; CH466589; EDK96916.1; -; Genomic_DNA.
DR   EMBL; BC138866; AAI38867.1; -; mRNA.
DR   EMBL; BC138867; AAI38868.1; -; mRNA.
DR   IPI; IPI00222627; -.
DR   IPI; IPI00754904; -.
DR   RefSeq; NP_001013043.1; NM_001013025.2.
DR   UniGene; Mm.246069; -.
DR   ProteinModelPortal; Q3UR70; -.
DR   STRING; Q3UR70; -.
DR   PRIDE; Q3UR70; -.
DR   Ensembl; ENSMUST00000095014; ENSMUSP00000092624; ENSMUSG00000070939.
DR   GeneID; 73122; -.
DR   KEGG; mmu:73122; -.
DR   UCSC; uc007ave.1; mouse.
DR   CTD; 73122; -.
DR   MGI; MGI:2447427; Tgfbrap1.
DR   eggNOG; roNOG07294; -.
DR   GeneTree; ENSGT00530000063596; -.
DR   HOGENOM; HBG358305; -.
DR   HOVERGEN; HBG108563; -.
DR   InParanoid; Q3UR70; -.
DR   OMA; SHPPLHE; -.
DR   OrthoDB; EOG4GTKC8; -.
DR   NextBio; 337509; -.
DR   ArrayExpress; Q3UR70; -.
DR   Bgee; Q3UR70; -.
DR   Genevestigator; Q3UR70; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005083; F:small GTPase regulator activity; IEA:InterPro.
DR   InterPro; IPR001180; Citron.
DR   InterPro; IPR019452; VPS39/TGF_beta_rcpt-assoc_1.
DR   InterPro; IPR019453; VPS39/TGF_beta_rcpt-assoc_2.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF10366; Vps39_1; 1.
DR   Pfam; PF10367; Vps39_2; 1.
DR   PROSITE; PS50219; CNH; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Phosphoprotein.
FT   CHAIN         1    860       Transforming growth factor-beta receptor-
FT                                associated protein 1.
FT                                /FTId=PRO_0000345406.
FT   DOMAIN       24    297       CNH.
FT   MOD_RES     855    855       Phosphoserine (By similarity).
FT   VAR_SEQ     231    247       MFATVAGISQRAPVHWS -> EEGWGSLLMAPASCLLS
FT                                (in isoform 2).
FT                                /FTId=VSP_034944.
FT   VAR_SEQ     248    860       Missing (in isoform 2).
FT                                /FTId=VSP_034945.
SQ   SEQUENCE   860 AA;  97303 MW;  B86BD77735D04C7B CRC64;
     MMNIKAFTLV SAVERELLMG DRDHISIECV ECCGRNLYVG TNDCFIYHFL LEEKAMPTGT
     ATFVATKQLH RHLGFKKPVN ELCAASALNR LLVLCDNSIT LVNMLNLEPV PSGARIKGAT
     TFAVNESPVN GDPFCVEVCI ISVKRRTVQM FLVYEDRVQI VKEVSTPEQP LAVAVDGYFL
     CLALTTQYII LNYSTGLSQD LFPYCSEEKP PIVKRIGRQE FLLAGPGGLG MFATVAGISQ
     RAPVHWSENV IGAAVCFPYV IALDDEFITV HSMLDQQQKQ TLPFKEGHIL QDFEGRVIVA
     TSKGVYILVP LPLEKQIQDL LANRRVEEAL VLAKGARRNI PKEKFQVMYR RILQQAGFIQ
     FAQLQFLEAK ELFRSSQLDV RELISLYPFL LPTSSSFTRS HPPLHEYADL NQLTQGDQEK
     MAKCKRFLMS YLNEIRSTEV ANGYKEDIDT ALLKLYAEAD HDSLLDLLVT ENFCLLTDSA
     AWLEKHKKYF ALGLLYHYNK QDASAVQLWV NIVNGDIQDS TRSDLYEYIV DFLTYCLDQE
     LVWTHADWLL QKSEEIGVQI FTKRPLDEQQ QTSFNPDNII SSLKKYPKAL VKYLEHLVID
     RRLQKEEYHT HLAILYLEEV LRQRVSTGGK DVEATETQAK LRRLLQKSDL YRVHLLKEKV
     QGAGLPMESA ILHGKLGEHE KALHILVHEM GDFSAAEDYC LWSSEGQGAA CRQRLFHTLL
     AMYLRAGPSA QDLTVAAVDL LNHHAREFDV TQVLQLLPDT WSVQLLCPFL MGAMRDSIHA
     RRTTQVALGL AKSENLIYMY DKMKLKGNAV RLSERELCQL CQNPFGEPVF VRYPNGGLVH
     THCAASRHTA PSSPSPGTRT
//
ID   SLMAP_MOUSE             Reviewed;         845 AA.
AC   Q3URD3; Q3TLP0; Q3UIZ6; Q6ZPL8; Q8VC86; Q9EQ03;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Sarcolemmal membrane-associated protein;
DE            Short=Sarcolemmal-associated protein;
GN   Name=Slmap; Synonyms=Kiaa1601, Slap;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), ALTERNATIVE SPLICING, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Spleen;
RX   PubMed=10986292; DOI=10.1074/jbc.M007682200;
RA   Wielowieyski P.A., Sevinc S., Guzzo R., Salih M., Wigle J.T.,
RA   Tuana B.S.;
RT   "Alternative splicing, expression, and genomic structure of the 3'
RT   region of the gene encoding the sarcolemmal-associated proteins
RT   (SLAPs) defines a novel class of coiled-coil tail-anchored membrane
RT   proteins.";
RL   J. Biol. Chem. 275:38474-38481(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Fetal heart, Hippocampus, Lung, and Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PROTEIN SEQUENCE OF 744-759, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   INTERACTION WITH MYOSIN, HOMODIMERIZATION, AND SUBCELLULAR LOCATION.
RX   PubMed=15591093; DOI=10.1152/ajpheart.01015.2004;
RA   Guzzo R.M., Salih M., Moore E.D., Tuana B.S.;
RT   "Molecular properties of cardiac tail-anchored membrane protein SLMAP
RT   are consistent with structural role in arrangement of excitation-
RT   contraction coupling apparatus.";
RL   Am. J. Physiol. 288:H1810-H1819(2005).
RN   [7]
RP   FUNCTION, HOMODIMERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND DEVELOPMENTAL STAGE.
RX   PubMed=15086317; DOI=10.1042/BJ20031723;
RA   Guzzo R.M., Wigle J., Salih M., Moore E.D., Tuana B.S.;
RT   "Regulated expression and temporal induction of the tail-anchored
RT   sarcolemmal-membrane-associated protein is critical for myoblast
RT   fusion.";
RL   Biochem. J. 381:599-608(2004).
RN   [8]
RP   SUBCELLULAR LOCATION, AND ALERNATIVE SPLICING.
RX   PubMed=15126628; DOI=10.1242/jcs.01079;
RA   Guzzo R.M., Sevinc S., Salih M., Tuana B.S.;
RT   "A novel isoform of sarcolemmal membrane-associated protein (SLMAP) is
RT   a component of the microtubule organizing centre.";
RL   J. Cell Sci. 117:2271-2281(2004).
CC   -!- FUNCTION: May play a role during myoblast fusion.
CC   -!- SUBUNIT: Homodimer. Interacts with myosin.
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Single-pass type
CC       IV membrane protein (By similarity). Cytoplasm, myofibril,
CC       sarcomere, M-band. Cytoplasm, myofibril, sarcomere, Z-disk.
CC       Note=Membrane-associated. Distributed in the transverse tubules
CC       and near the junctional sarcoplasmic reticulum (By similarity).
CC       Detected along the Z- and M-lines in cardiomyocytes (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm, cytoskeleton,
CC       centrosome. Note=Localizes to the centrosomes in a microtubule-
CC       dependent manner.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, cytoskeleton,
CC       centrosome. Note=Localizes to the centrosomes in a microtubule-
CC       dependent manner.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q3URD3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3URD3-2; Sequence=VSP_021517, VSP_021518;
CC       Name=3;
CC         IsoId=Q3URD3-3; Sequence=VSP_021514;
CC       Name=4;
CC         IsoId=Q3URD3-4; Sequence=VSP_021514, VSP_021518;
CC       Name=5;
CC         IsoId=Q3URD3-5; Sequence=VSP_021515, VSP_021516;
CC   -!- TISSUE SPECIFICITY: Expressed in proliferating myoblasts and
CC       differentiated myotubes (at protein level). Expressed in
CC       myoblasts, cardiac and skeletal muscles.
CC   -!- DEVELOPMENTAL STAGE: Expressed in atrial and ventricular chambers
CC       of the primitive heart at 9 dpc. Expressed in somites at 11 dpc.
CC       Expressed in atrial and ventricular chambers and interventricular
CC       and interatrial septum at 13 dpc. Expressed in myotubes between 13
CC       and 15 dpc. Expressed in skeletal muscles at 18 dpc.
CC   -!- SIMILARITY: Belongs to the SLMAP family.
CC   -!- SIMILARITY: Contains 1 FHA domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG41950.1; Type=Erroneous initiation;
CC       Sequence=BAC98213.1; Type=Erroneous initiation;
CC       Sequence=BAE24755.1; Type=Frameshift; Positions=Several;
CC       Sequence=BAE27359.1; Type=Erroneous initiation;
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DR   EMBL; AF304451; AAG41950.1; ALT_INIT; mRNA.
DR   EMBL; AK129403; BAC98213.1; ALT_INIT; mRNA.
DR   EMBL; AK141597; BAE24755.1; ALT_SEQ; mRNA.
DR   EMBL; AK146685; BAE27359.1; ALT_INIT; mRNA.
DR   EMBL; AK164911; BAE37961.1; -; mRNA.
DR   EMBL; AK166396; BAE38752.1; -; mRNA.
DR   EMBL; BC021457; AAH21457.1; -; mRNA.
DR   IPI; IPI00121581; -.
DR   IPI; IPI00623400; -.
DR   IPI; IPI00624363; -.
DR   IPI; IPI00755791; -.
DR   IPI; IPI00798436; -.
DR   RefSeq; NP_114397.3; NM_032008.3.
DR   UniGene; Mm.36769; -.
DR   ProteinModelPortal; Q3URD3; -.
DR   SMR; Q3URD3; 28-112.
DR   STRING; Q3URD3; -.
DR   PhosphoSite; Q3URD3; -.
DR   PRIDE; Q3URD3; -.
DR   Ensembl; ENSMUST00000038522; ENSMUSP00000046956; ENSMUSG00000021870.
DR   Ensembl; ENSMUST00000100798; ENSMUSP00000098361; ENSMUSG00000021870.
DR   Ensembl; ENSMUST00000100800; ENSMUSP00000098363; ENSMUSG00000021870.
DR   Ensembl; ENSMUST00000112331; ENSMUSP00000107950; ENSMUSG00000021870.
DR   GeneID; 83997; -.
DR   KEGG; mmu:83997; -.
DR   UCSC; uc007ssq.1; mouse.
DR   UCSC; uc007ssr.1; mouse.
DR   UCSC; uc007sss.1; mouse.
DR   CTD; 83997; -.
DR   MGI; MGI:1933549; Slmap.
DR   eggNOG; roNOG11450; -.
DR   GeneTree; ENSGT00530000063197; -.
DR   HOGENOM; HBG716393; -.
DR   HOVERGEN; HBG082442; -.
DR   InParanoid; Q3URD3; -.
DR   OMA; ELHNSQK; -.
DR   NextBio; 350862; -.
DR   ArrayExpress; Q3URD3; -.
DR   Bgee; Q3URD3; -.
DR   CleanEx; MM_SLMAP; -.
DR   Genevestigator; Q3URD3; -.
DR   GermOnline; ENSMUSG00000021870; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IDA:MGI.
DR   GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR   GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR001363; Prot_inh_fetuin_CS.
DR   InterPro; IPR008984; SMAD_FHA_domain.
DR   Gene3D; G3DSA:2.60.200.20; FHA; 1.
DR   Pfam; PF00498; FHA; 1.
DR   SMART; SM00240; FHA; 1.
DR   SUPFAM; SSF49879; SMAD_FHA; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell membrane; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane;
KW   Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    845       Sarcolemmal membrane-associated protein.
FT                                /FTId=PRO_0000259663.
FT   TOPO_DOM      1    819       Cytoplasmic (Potential).
FT   TRANSMEM    820    840       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   TOPO_DOM    841    845       Extracellular (Potential).
FT   DOMAIN       28     85       FHA.
FT   REGION        1    163       Necessary for targeting to centrosomes.
FT   COILED      167    202       Potential.
FT   COILED      231    388       Potential.
FT   COILED      506    816       Potential.
FT   MOD_RES      29     29       N6-acetyllysine (By similarity).
FT   MOD_RES     148    148       Phosphoserine (By similarity).
FT   VAR_SEQ       1    483       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_021514.
FT   VAR_SEQ       1    348       Missing (in isoform 5).
FT                                /FTId=VSP_021515.
FT   VAR_SEQ     396    434       GIQVDDFLPKINGSTEKEHLLSKSGGDCTFIHQFLECQK
FT                                -> E (in isoform 5).
FT                                /FTId=VSP_021516.
FT   VAR_SEQ     414    434       Missing (in isoform 2).
FT                                /FTId=VSP_021517.
FT   VAR_SEQ     816    845       KPWPWMPMLAALVAVTAMVLYVPGLARASP -> PSILQPV
FT                                PAVFIGLFLAFLFWCFGPLW (in isoform 2 and
FT                                isoform 4).
FT                                /FTId=VSP_021518.
FT   CONFLICT    682    682       E -> G (in Ref. 1; AAG41950).
FT   CONFLICT    696    697       EN -> GD (in Ref. 1; AAG41950).
SQ   SEQUENCE   845 AA;  96933 MW;  FC73049C382CA17F CRC64;
     MPSALAIFTC RPNSHPFQER HVYLDEPIKI GRSVARCRPA QNNATFDCKV LSRNHALVWF
     DHKTSKFYLQ DTKSSNGTFI NSQRLSRGSE ESPPCEILSG DIIQFGVDVT ENTRKVTHGC
     IVSTIKLFLP DGMEARLRSD VIHAPLPSPV DKVAANTPSM YSQELFQLSQ YLQEALHREQ
     MLEQKLATLQ RLLAITQEAS DTSWQALIDE DRLLSRLEVM GNQLQACSKN QTEDSLRKEL
     IALQEDKHSY ETTAKESLRR VLQEKIEVVR KLSEVERSLS NTEDECTHLK EMNERTQEEL
     RELANKYNGA VNEIKDLSDK LKVAEGKQEE IQQKGQAEKK ELQTKIDEME EKEQELQAKI
     EALQADNDFT NERLTALQVR LEHLQEKTLK ECSSLGIQVD DFLPKINGST EKEHLLSKSG
     GDCTFIHQFL ECQKKLMVQG HLTKVVEESK LSKENQAKAK ESDLSDTLSP SKEKSSDDTT
     DAQMDEQDLN EPLAKVSLLK DDLQGTQSET EAKQDIQHLR KELVEAQELA RTSKQKCFEL
     QALLEEERKA YRNQVEESAK QIQVLQVQLQ KLHMDMENLQ EEKDTEISST RDKLLSAQDE
     ILLLRQAAAE AVSERDTDFV SLQEELKKVR AELEGWRKAA SEYENEIRSL QSSFQLRCQQ
     CEDQQREEAT RLQGELEKLK KEWDVLETEC HSLKKENVLL SSELQRQEKE LHNSQKQSFE
     LTSDLSILQM TRKELEKQVG SLKEQHLRDA ADLKTLLSKA ENQAKDVQKE YEKTQTVLSE
     LKLKFEMTEQ EKQSITDELK QCKDNLKLLR EKGNNKPWPW MPMLAALVAV TAMVLYVPGL
     ARASP
//
ID   TET1_MOUSE              Reviewed;        2007 AA.
AC   Q3URK3; Q6ZPK2; Q9CY36;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   08-MAR-2011, entry version 35.
DE   RecName: Full=Methylcytosine dioxygenase TET1;
DE            EC=1.14.11.n2;
DE   AltName: Full=CXXC-type zinc finger protein 6;
DE   AltName: Full=Ten-eleven translocation 1 gene protein homolog;
GN   Name=Tet1; Synonyms=Cxxc6, Kiaa1676;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 655-1066 AND 1773-2007.
RC   STRAIN=C57BL/6J; TISSUE=Liver, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1351-1946.
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND MUTAGENESIS OF HIS-1620 AND ASP-1622.
RX   PubMed=20639862; DOI=10.1038/nature09303;
RA   Ito S., D'Alessio A.C., Taranova O.V., Hong K., Sowers L.C., Zhang Y.;
RT   "Role of Tet proteins in 5mC to 5hmC conversion, ES-cell self-renewal
RT   and inner cell mass specification.";
RL   Nature 466:1129-1133(2010).
CC   -!- FUNCTION: Dioxygenase that catalyzes the conversion of
CC       methylcytosine (5mC) to 5-hydroxymethylcytosine (hmC). Plays a
CC       role in embryonic stem (ES) cell maintenance and inner cell mass
CC       (ICM) cell specification, possibly by participating in DNA
CC       demethylation. Specifically binds 5mC, a minor base in mammalian
CC       DNA found in repetitive DNA elements that is crucial for
CC       retrotransposon silencing and mammalian development. 5mC is
CC       present in ES cells and is enriched in the brain, especially in
CC       Purkinje neurons. The clear function of hmC is still unclear but
CC       it could constitute an intermediate component in cytosine
CC       demethylation. A role of hmC in DNA demethylation is supported by
CC       TET1 function in ES cell maintenance, which is required to prevent
CC       NANOG hypermethylation and maintain NANOG expression in ES cells.
CC   -!- CATALYTIC ACTIVITY: Methylcytosine + 2-oxoglutarate + O(2) = 5-
CC       hydroxymethylcytosine + succinate + CO(2).
CC   -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Present in embryonic stem cells (ES cells).
CC   -!- SIMILARITY: Belongs to the TET family.
CC   -!- SIMILARITY: Contains 1 CXXC-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB27288.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAC98231.1; Type=Miscellaneous discrepancy; Note=Partially unspliced pre-RNA;
CC   -----------------------------------------------------------------------
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DR   EMBL; AC166359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK010953; BAB27288.1; ALT_INIT; mRNA.
DR   EMBL; AK141438; BAE24685.1; -; mRNA.
DR   EMBL; AK129421; BAC98231.1; ALT_SEQ; Transcribed_RNA.
DR   IPI; IPI00551511; -.
DR   RefSeq; NP_081660.1; NM_027384.1.
DR   UniGene; Mm.479241; -.
DR   ProteinModelPortal; Q3URK3; -.
DR   SMR; Q3URK3; 568-626.
DR   STRING; Q3URK3; -.
DR   PhosphoSite; Q3URK3; -.
DR   PRIDE; Q3URK3; -.
DR   Ensembl; ENSMUST00000099674; ENSMUSP00000097266; ENSMUSG00000075009.
DR   GeneID; 52463; -.
DR   KEGG; mmu:52463; -.
DR   CTD; 52463; -.
DR   MGI; MGI:1098693; Tet1.
DR   eggNOG; roNOG09810; -.
DR   GeneTree; ENSGT00590000083613; -.
DR   HOGENOM; HBG446385; -.
DR   InParanoid; Q3URK3; -.
DR   OrthoDB; EOG4HT8SM; -.
DR   ArrayExpress; Q3URK3; -.
DR   Bgee; Q3URK3; -.
DR   Genevestigator; Q3URK3; -.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR   GO; GO:0070579; F:methylcytosine dioxygenase activity; IDA:UniProtKB.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW.
DR   GO; GO:0043566; F:structure-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0080111; P:DNA demethylation; IMP:UniProtKB.
DR   GO; GO:0001826; P:inner cell mass cell differentiation; IMP:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0019827; P:stem cell maintenance; IMP:UniProtKB.
DR   InterPro; IPR002857; Znf_CXXC.
DR   Pfam; PF02008; zf-CXXC; 1.
DR   PROSITE; PS51058; ZF_CXXC; 1.
PE   1: Evidence at protein level;
KW   Dioxygenase; DNA-binding; Iron; Metal-binding; Nucleus;
KW   Oxidoreductase; Zinc; Zinc-finger.
FT   CHAIN         1   2007       Methylcytosine dioxygenase TET1.
FT                                /FTId=PRO_0000377549.
FT   ZN_FING     567    608       CXXC-type.
FT   METAL      1620   1620       Iron; catalytic (Probable).
FT   METAL      1622   1622       Iron; catalytic (Probable).
FT   METAL      1907   1907       Iron; catalytic (By similarity).
FT   BINDING    1922   1922       2-oxoglutarate (By similarity).
FT   MUTAGEN    1620   1620       H->Y: Loss of enzyme activity; when
FT                                associated with A-1622.
FT   MUTAGEN    1622   1622       D->A: Loss of enzyme activity; when
FT                                associated with Y-1620.
SQ   SEQUENCE   2007 AA;  219261 MW;  C563672511ACFFC6 CRC64;
     MSRSRPAKPS KSVKTKLQKK KDIQMKTKTS KQAVRHGASA KAVNPGKPKQ LIKRRDGKKE
     TEDKTPTPAP SFLTRAGAAR MNRDRNQVLF QNPDSLTCNG FTMALRRTSL SWRLSQRPVV
     TPKPKKVPPS KKQCTHNIQD EPGVKHSEND SVPSQHATVS PGTENGEQNR CLVEGESQEI
     TQSCPVFEER IEDTQSCISA SGNLEAEISW PLEGTHCEEL LSHQTSDNEC TSPQECAPLP
     QRSTSEVTSQ KNTSNQLADL SSQVESIKLS DPSPNPTGSD HNGFPDSSFR IVPELDLKTC
     MPLDESVYPT ALIRFILAGS QPDVFDTKPQ EKTLITTPEQ VGSHPNQVLD ATSVLGQAFS
     TLPLQWGFSG ANLVQVEALG KGSDSPEDLG AITMLNQQET VAMDMDRNAT PDLPIFLPKP
     PNTVATYSSP LLGPEPHSST SCGLEVQGAT PILTLDSGHT PQLPPNPESS SVPLVIAANG
     TRAEKQFGTS LFPAVPQGFT VAAENEVQHA PLDLTQGSQA APSKLEGEIS RVSITGSADV
     KATAMSMPVT QASTSSPPCN STPPMVERRK RKACGVCEPC QQKANCGECT YCKNRKNSHQ
     ICKKRKCEVL KKKPEATSQA QVTKENKRPQ REKKPKVLKT DFNNKPVNGP KSESMDCSRR
     GHGEEEQRLD LITHPLENVR KNAGGMTGIE VEKWAPNKKS HLAEGQVKGS CDANLTGVEN
     PQPSEDDKQQ TNPSPTFAQT IRNGMKNVHC LPTDTHLPLN KLNHEEFSKA LGNNSSKLLT
     DPSNCKDAMS VTTSGGECDH LKGPRNTLLF QKPGLNCRSG AEPTIFNNHP NTHSAGSRPH
     PPEKVPNKEP KDGSPVQPSL LSLMKDRRLT LEQVVAIEAL TQLSEAPSES SSPSKPEKDE
     EAHQKTASLL NSCKAILHSV RKDLQDPNVQ GKGLHHDTVV FNGQNRTFKS PDSFATNQAL
     IKSQGYPSSP TAEKKGAAGG RAPFDGFENS HPLPIESHNL ENCSQVLSCD QNLSSHDPSC
     QDAPYSQIEE DVAAQLTQLA STINHINAEV RNAESTPESL VAKNTKQKHS QEKRMVHQKP
     PSSTQTKPSV PSAKPKKAQK KARATPHANK RKKKPPARSS QENDQKKQEQ LAIEYSKMHD
     IWMSSKFQRF GQSSPRSFPV LLRNIPVFNQ ILKPVTQSKT PSQHNELFPP INQIKFTRNP
     ELAKEKVKVE PSDSLPTCQF KTESGGQTFA EPADNSQGQP MVSVNQEAHP LPQSPPSNQC
     ANIMAGAAQT QFHLGAQENL VHQIPPPTLP GTSPDTLLPD PASILRKGKV LHFDGITVVT
     EKREAQTSSN GPLGPTTDSA QSEFKESIMD LLSKPAKNLI AGLKEQEAAP CDCDGGTQKE
     KGPYYTHLGA GPSVAAVREL METRFGQKGK AIRIEKIVFT GKEGKSSQGC PVAKWVIRRS
     GPEEKLICLV RERVDHHCST AVIVVLILLW EGIPRLMADR LYKELTENLR SYSGHPTDRR
     CTLNKKRTCT CQGIDPKTCG ASFSFGCSWS MYFNGCKFGR SENPRKFRLA PNYPLHEKQL
     EKNLQELATV LAPLYKQMAP VAYQNQVEYE EVAGDCRLGN EEGRPFSGVT CCMDFCAHSH
     KDIHNMHNGS TVVCTLIRAD GRDTNCPEDE QLHVLPLYRL ADTDEFGSVE GMKAKIKSGA
     IQVNGPTRKR RLRFTEPVPR CGKRAKMKQN HNKSGSHNTK SFSSASSTSH LVKDESTDFC
     PLQASSAETS TCTYSKTASG GFAETSSILH CTMPSGAHSG ANAAAGECTG TVQPAEVAAH
     PHQSLPTADS PVHAEPLTSP SEQLTSNQSN QQLPLLSNSQ KLASCQVEDE RHPEADEPQH
     PEDDNLPQLD EFWSDSEEIY ADPSFGGVAI APIHGSVLIE CARKELHATT SLRSPKRGVP
     FRVSLVFYQH KSLNKPNHGF DINKIKCKCK KVTKKKPADR ECPDVSPEAN LSHQIPSRVA
     STLTRDNVVT VSPYSLTHVA GPYNRWV
//
ID   Q3URP7_MOUSE            Unreviewed;       145 AA.
AC   Q3URP7;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 36.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Dnajc21;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
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DR   EMBL; AK141303; BAE24641.1; -; mRNA.
DR   IPI; IPI00755714; -.
DR   UniGene; Mm.297862; -.
DR   ProteinModelPortal; Q3URP7; -.
DR   PhosphoSite; Q3URP7; -.
DR   Ensembl; ENSMUST00000136591; ENSMUSP00000116865; ENSMUSG00000044224.
DR   MGI; MGI:1925371; Dnajc21.
DR   eggNOG; roNOG08324; -.
DR   OrthoDB; EOG4PG617; -.
DR   ArrayExpress; Q3URP7; -.
DR   Bgee; Q3URP7; -.
DR   Genevestigator; Q3URP7; -.
PE   1: Evidence at protein level;
SQ   SEQUENCE   145 AA;  17357 MW;  E784B746F65911FE CRC64;
     MEKENKKIRD RARKEKNELV RQLVAFIRKR DKRVQAHRKL VEEQNAEKAR KAEEMRRQQK
     LKQAKLAEQY REQSWMTMAN LEKELQEMEA RYEKEFGDGS DENEVEDQEP RNGLDGKDSE
     EAEEAELYQD LYCPACDKSF KTEKA
//
ID   CCD51_MOUSE             Reviewed;         406 AA.
AC   Q3URS9; Q4QQL1; Q9CXS1;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Coiled-coil domain-containing protein 51;
GN   Name=Ccdc51;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3URS9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3URS9-2; Sequence=VSP_025801;
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DR   EMBL; AK014056; BAB29135.1; -; mRNA.
DR   EMBL; AK137013; BAE23205.1; -; mRNA.
DR   EMBL; AK141240; BAE24609.1; -; mRNA.
DR   EMBL; BC098221; AAH98221.2; -; mRNA.
DR   EMBL; BC116786; AAI16787.1; -; mRNA.
DR   EMBL; BC116788; AAI16789.1; -; mRNA.
DR   IPI; IPI00110708; -.
DR   IPI; IPI00850529; -.
DR   RefSeq; NP_079965.2; NM_025689.4.
DR   UniGene; Mm.128227; -.
DR   ProteinModelPortal; Q3URS9; -.
DR   STRING; Q3URS9; -.
DR   PRIDE; Q3URS9; -.
DR   Ensembl; ENSMUST00000026735; ENSMUSP00000026735; ENSMUSG00000025645.
DR   GeneID; 66658; -.
DR   KEGG; mmu:66658; -.
DR   UCSC; uc009rrx.1; mouse.
DR   CTD; 66658; -.
DR   MGI; MGI:1913908; Ccdc51.
DR   eggNOG; roNOG12247; -.
DR   GeneTree; ENSGT00390000001709; -.
DR   HOGENOM; HBG716394; -.
DR   HOVERGEN; HBG100936; -.
DR   InParanoid; Q3URS9; -.
DR   OMA; WWDRYEE; -.
DR   OrthoDB; EOG4W0XDF; -.
DR   NextBio; 322295; -.
DR   ArrayExpress; Q3URS9; -.
DR   Bgee; Q3URS9; -.
DR   CleanEx; MM_CCDC51; -.
DR   Genevestigator; Q3URS9; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    406       Coiled-coil domain-containing protein 51.
FT                                /FTId=PRO_0000288869.
FT   TRANSMEM    199    219       Helical; (Potential).
FT   TRANSMEM    383    403       Helical; (Potential).
FT   COILED      109    162       Potential.
FT   VAR_SEQ       1     31       Missing (in isoform 2).
FT                                /FTId=VSP_025801.
FT   CONFLICT    160    160       R -> W (in Ref. 2; AAH98221).
SQ   SEQUENCE   406 AA;  45132 MW;  D734FCFF6716354D CRC64;
     MTGCSPVFAM QHVVGVPRIL VRRTFLGTDV TMTRTLCSPG PREKRPEAAA LGLFHRLPEL
     GRTLSHTVRH QAASTAKAWW DRYEEFVGLN EVREAQGNVT EAEKVFMVAR GLVREAREGL
     EAQQTKLKEV RDRLDRVSRE DNQYLELATL EHRMLQEEKR LRIAYLRAED SEREKFSLFS
     AAVRESHEKE RTRAERTKNW SLIGSVLGAL IGVAGSTYVN RVRLQELKAL LLEAQKGPAS
     LQEAIREQAS SYSLQQKDLQ DLMMDLRGLV HAEQGQGSGS PTGSSTRGKD IDGLSATMKE
     QLRHSRQVYS CLEGLREQLD GLEKTCSQMA GVLQLAQAPA HPGTVGPVDG ALPSSLLEHG
     SVILALSEME QRLEAQANRN TVSSTLVTCV TFLATLPLLY MLFKTS
//
ID   PEG3_MOUSE              Reviewed;        1571 AA.
AC   Q3URU2; O54978; Q3TQ69; Q5EBP7; Q61138; Q6GQS0; Q80U47; Q8R5N0;
AC   Q9QX53;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Paternally-expressed gene 3 protein;
DE   AltName: Full=ASF-1;
GN   Name=Peg3; Synonyms=Kiaa0287, Pw1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   MEDLINE=96154192; PubMed=8563758; DOI=10.1038/ng0296-186;
RA   Kuroiwa Y., Kaneko-Ishino T., Kagitani F., Kohda T., Li L.-L.,
RA   Tada M., Suzuki R., Yokoyama M., Shiroishi T., Wakana S., Barton S.C.,
RA   Ishino F., Surani M.A.;
RT   "Peg3 imprinted gene on proximal chromosome 7 encodes for a zinc
RT   finger protein.";
RL   Nat. Genet. 12:186-190(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=B6C3H F1;
RX   MEDLINE=21160571; PubMed=11260267;
RX   DOI=10.1046/j.1365-2443.2001.00412.x;
RA   Kohda T., Asai A., Kuroiwa Y., Kobayashi S., Aisaka K., Nagashima G.,
RA   Yoshida M.C., Kondo Y., Kagiyama N., Kirino T., Kaneko-Ishino T.,
RA   Ishino F.;
RT   "Tumour suppressor activity of human imprinted gene PEG3 in a glioma
RT   cell line.";
RL   Genes Cells 6:237-247(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Head;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-352 (ISOFORM 1).
RX   MEDLINE=20171374; PubMed=10704281; DOI=10.1006/geno.1999.6103;
RA   Li L.-L., Szeto I.Y.-Y., Cattanach B.M., Ishino F., Surani M.A.;
RT   "Organization and parent-of-origin-specific methylation of imprinted
RT   Peg3 gene on mouse proximal chromosome 7.";
RL   Genomics 63:333-340(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-1571 (ISOFORM 1), SUBCELLULAR
RP   LOCATION, SUBUNIT, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=129/Sv; TISSUE=Limb bud;
RX   MEDLINE=96400442; PubMed=8806818; DOI=10.1006/dbio.1996.0172;
RA   Relaix F., Weng X., Marazzi G., Yang E., Copeland N.G., Jenkins N.,
RA   Spence S.E., Sassoon D.;
RT   "Pw1, a novel zinc finger gene implicated in the myogenic and neuronal
RT   lineages.";
RL   Dev. Biol. 177:383-396(1996).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH TRAF2.
RX   PubMed=9500555; DOI=10.1038/ng0398-287;
RA   Relaix F., Wei X.-J., Wu X., Sassoon D.A.;
RT   "Peg3/Pw1 is an imprinted gene involved in the TNF-NFkappaB signal
RT   transduction pathway.";
RL   Nat. Genet. 18:287-291(1998).
RN   [9]
RP   FUNCTION.
RX   PubMed=10195900; DOI=10.1126/science.284.5412.330;
RA   Li L.-L., Keverne E.B., Aparicio S.A., Ishino F., Barton S.C.,
RA   Surani M.A.;
RT   "Regulation of maternal behavior and offspring growth by paternally
RT   expressed Peg3.";
RL   Science 284:330-333(1999).
RN   [10]
RP   FUNCTION, INDUCTION, AND INTERACTION WITH SIAH1A AND SIAH2.
RX   PubMed=10681424; DOI=10.1073/pnas.040378897;
RA   Relaix F., Wei X., Li W., Pan J., Lin Y., Bowtell D.D., Sassoon D.A.,
RA   Wu X.;
RT   "Pw1/Peg3 is a potential cell death mediator and cooperates with
RT   Siah1a in p53-mediated apoptosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:2105-2110(2000).
RN   [11]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=21231143; PubMed=11331620; DOI=10.1093/hmg/10.10.1093;
RA   Hiby S.E., Lough M., Keverne E.B., Surani M.A., Loke Y.W., King A.;
RT   "Paternal monoallelic expression of PEG3 in the human placenta.";
RL   Hum. Mol. Genet. 10:1093-1100(2001).
RN   [12]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=11943780; DOI=10.1074/jbc.M201907200;
RA   Johnson M.D., Wu X., Aithmitti N., Morrison R.S.;
RT   "Peg3/Pw1 is a mediator between p53 and Bax in DNA damage-induced
RT   neuronal death.";
RL   J. Biol. Chem. 277:23000-23007(2002).
CC   -!- FUNCTION: Induces apoptosis in cooperation with SIAH1A. Acts as a
CC       mediator between p53/TP53 and BAX in a neuronal death pathway that
CC       is activated by DNA damage. Acts synergistically with TRAF2 and
CC       inhibits TNF induced apoptosis through activation of NF-kappa-B.
CC       Plays a role in regulating maternal behavior and offspring growth.
CC   -!- SUBUNIT: Homodimer. Interacts with SIAH1A and SIAH2. Interacts
CC       with TRAF2.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3URU2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3URU2-2; Sequence=VSP_020375, VSP_020376, VSP_020377;
CC   -!- TISSUE SPECIFICITY: Brain, glial cells, neurons, skeletal muscle,
CC       uterus and placenta. In the placenta it found in all trophoblast
CC       cells.
CC   -!- DEVELOPMENTAL STAGE: Strongly expressed upon gastrulation and
CC       subsequently becomes restricted to skeletal muscle and subregions
CC       of the CNS. At E9.5, expressed in the branchial arches, somites
CC       and gut but little in the heart and neural tissues. At E12.5
CC       strongly expressed in the cranial skeleton, tongue, vertebral
CC       cartilage, pituitary and the luminal epithelium.
CC   -!- INDUCTION: Induced during p53/TP53 mediated apoptosis. Up-
CC       regulated by DNA damage in cortical neurons in the presence of
CC       p53/TP53.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family.
CC   -!- SIMILARITY: Contains 12 C2H2-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 SCAN box domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC52770.1; Type=Frameshift; Positions=Several;
CC       Sequence=BAB85589.1; Type=Frameshift; Positions=Several;
CC       Sequence=BAC65520.2; Type=Erroneous initiation;
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DR   EMBL; AF038939; AAB96922.1; -; mRNA.
DR   EMBL; AB003040; BAB85589.1; ALT_FRAME; mRNA.
DR   EMBL; AK141217; BAE24595.1; -; mRNA.
DR   EMBL; AK163845; BAE37516.1; -; mRNA.
DR   EMBL; AK122238; BAC65520.2; ALT_INIT; Transcribed_RNA.
DR   EMBL; BC072661; AAH72661.1; -; mRNA.
DR   EMBL; BC085183; AAH85183.1; -; mRNA.
DR   EMBL; BC089344; AAH89344.1; -; mRNA.
DR   EMBL; AF105266; AAF16868.1; -; Genomic_DNA.
DR   EMBL; AF105264; AAF16868.1; JOINED; Genomic_DNA.
DR   EMBL; AF105265; AAF16868.1; JOINED; Genomic_DNA.
DR   EMBL; U48804; AAC52770.1; ALT_FRAME; Genomic_DNA.
DR   IPI; IPI00330240; -.
DR   IPI; IPI00462561; -.
DR   PIR; T14155; T14155.
DR   PIR; T30173; T30173.
DR   RefSeq; NP_032843.2; NM_008817.2.
DR   UniGene; Mm.389800; -.
DR   ProteinModelPortal; Q3URU2; -.
DR   SMR; Q3URU2; 283-544, 1021-1335, 1478-1571.
DR   STRING; Q3URU2; -.
DR   PRIDE; Q3URU2; -.
DR   Ensembl; ENSMUST00000051209; ENSMUSP00000050750; ENSMUSG00000002265.
DR   Ensembl; ENSMUST00000086313; ENSMUSP00000083493; ENSMUSG00000002265.
DR   GeneID; 18616; -.
DR   KEGG; mmu:18616; -.
DR   UCSC; uc009fbw.1; mouse.
DR   CTD; 18616; -.
DR   MGI; MGI:104748; Peg3.
DR   eggNOG; roNOG06404; -.
DR   GeneTree; ENSGT00440000037819; -.
DR   HOVERGEN; HBG079943; -.
DR   InParanoid; Q3URU2; -.
DR   OMA; EHQKARA; -.
DR   OrthoDB; EOG4894KN; -.
DR   PhylomeDB; Q3URU2; -.
DR   NextBio; 294556; -.
DR   ArrayExpress; Q3URU2; -.
DR   Bgee; Q3URU2; -.
DR   CleanEx; MM_PEG3; -.
DR   Genevestigator; Q3URU2; -.
DR   GermOnline; ENSMUSG00000002265; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 10.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 12.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Cytoplasm; Metal-binding; Nucleus;
KW   Repeat; Zinc; Zinc-finger.
FT   CHAIN         1   1571       Paternally-expressed gene 3 protein.
FT                                /FTId=PRO_0000249229.
FT   REPEAT      942    946       1-1.
FT   REPEAT      967    971       1-2.
FT   REPEAT      987    991       2-1.
FT   REPEAT      992    996       1-3.
FT   REPEAT      997   1001       2-2.
FT   REPEAT     1002   1006       1-4.
FT   REPEAT     1007   1011       2-3.
FT   REPEAT     1012   1016       1-5.
FT   REPEAT     1017   1021       1-6.
FT   REPEAT     1022   1026       1-7.
FT   REPEAT     1027   1031       1-8.
FT   REPEAT     1032   1036       1-9.
FT   REPEAT     1047   1051       1-10.
FT   ZN_FING     325    347       C2H2-type 1.
FT   ZN_FING     378    400       C2H2-type 2.
FT   ZN_FING     436    458       C2H2-type 3.
FT   ZN_FING     520    542       C2H2-type 4.
FT   ZN_FING     850    872       C2H2-type 5.
FT   ZN_FING    1091   1113       C2H2-type 6.
FT   ZN_FING    1147   1169       C2H2-type 7.
FT   ZN_FING    1209   1231       C2H2-type 8.
FT   ZN_FING    1266   1289       C2H2-type 9.
FT   ZN_FING    1317   1339       C2H2-type 10; degenerate.
FT   ZN_FING    1488   1510       C2H2-type 11.
FT   ZN_FING    1547   1569       C2H2-type 12.
FT   REGION      199    265       10 X 5 AA repeat of P-H-X-X-E.
FT   REGION      199    265       3 X 5 AA repeat of P-H-D-D-K.
FT   COMPBIAS    228    231       Poly-Ser.
FT   COMPBIAS    695    698       Poly-Ser.
FT   COMPBIAS    771    774       Poly-Ser.
FT   VAR_SEQ     989   1048       Missing (in isoform 2).
FT                                /FTId=VSP_020375.
FT   VAR_SEQ    1202   1254       PAVSGSAIRCRQCGQGFIHSSALNEHMRQHRDNEIMEQSEL
FT                                SDEIFIQGLALT -> ASSLPNSSGTTTPKFTRMSPMSMGP
FT                                PTPMPPFSPSPSGSTSHCTNAKIAASPS (in isoform
FT                                2).
FT                                /FTId=VSP_020376.
FT   VAR_SEQ    1255   1571       Missing (in isoform 2).
FT                                /FTId=VSP_020377.
FT   CONFLICT      5      5       E -> G (in Ref. 1 and 2).
FT   CONFLICT    156    156       T -> A (in Ref. 1; AAB96922).
FT   CONFLICT    321    321       G -> W (in Ref. 2; BAB85589).
FT   CONFLICT    351    351       N -> T (in Ref. 6).
FT   CONFLICT    370    371       KG -> RS (in Ref. 1 and 2).
FT   CONFLICT    382    382       E -> V (in Ref. 2; BAB85589).
FT   CONFLICT    403    403       E -> R (in Ref. 7).
FT   CONFLICT    567    568       Missing (in Ref. 7).
FT   CONFLICT    570    570       K -> E (in Ref. 2; BAB85589).
FT   CONFLICT    608    608       R -> G (in Ref. 2; BAB85589).
FT   CONFLICT    614    614       F -> S (in Ref. 2; BAB85589).
FT   CONFLICT    645    645       K -> E (in Ref. 2; BAB85589).
FT   CONFLICT    648    648       F -> L (in Ref. 1; AAB96922).
FT   CONFLICT    660    660       Y -> C (in Ref. 1; AAB96922).
FT   CONFLICT    669    669       G -> A (in Ref. 7).
FT   CONFLICT    712    712       E -> K (in Ref. 7).
FT   CONFLICT    736    737       ND -> MN (in Ref. 2; BAB85589).
FT   CONFLICT    856    856       G -> R (in Ref. 7).
FT   CONFLICT    979    979       D -> V (in Ref. 1; AAB96922).
FT   CONFLICT   1011   1011       K -> E (in Ref. 7).
FT   CONFLICT   1051   1051       E -> Q (in Ref. 5; AAH89344).
FT   CONFLICT   1123   1123       E -> G (in Ref. 7).
FT   CONFLICT   1171   1171       Missing (in Ref. 3; BAC65520).
FT   CONFLICT   1181   1181       D -> Y (in Ref. 1 and 2).
FT   CONFLICT   1401   1401       N -> I (in Ref. 1 and 2).
SQ   SEQUENCE   1571 AA;  178932 MW;  915E13EF0751C6EE CRC64;
     MYHHEDDTNS DMNSDDDMSR SGRETPPPRP SHAFGSERDL ERRGRSRDVE PRDRWPYTRN
     PRSRLPQRDL SLPVMSRPHF GLDRDDDRRS MDYESRSQDA ESYQNVVELK EDKKPQNPIQ
     DNLENYRKLL SLGVQLAEDD RHSHMTQGHS SRSKRTAYPS TSRGLKPMPE AKKPSHRRGI
     CEDESSHGVI MEKFIKDVAR NPKSGRAREL NERPPPRFPR PNDNWKDSSS SRRESVIQER
     GYEGSAFRGG FRFNADLASR SRALERKRRY HFDSDERGSG HEHKSCVRKK PFECGAEMRQ
     AMSMGNLNSP SFSESQSIDF GANPYVCDEC GRQFSVISEF VEHQIMHTRE NLYEYGESFI
     HSVAVNEVQK GQGGGKRFEC KECGETFSRS AALAEHRQIH AREYLAECRD QEDEETIMPS
     PTFSELQKMY GKDKFYECKV CKETFLHSSA LIEHQKIHGR GNSDDRDNER ERERDRLRAR
     AREQRERERE RERERELGEP FLTCPNFNEF RKMYRKDKIY ECKVCGESFL HLSSLREHQK
     IHTRGNPFEN KSRMCEETFV PSQSLRRRQK TYREKLFDFN NARDALMGNS DSSEHQKNRS
     RRNFFEGRGF EKPFVESQKS HTITRPPENK DDDKPFTISV NPNDKLKFPI MENGSQGKSY
     ERSVIHSLGS AEAQKSHGGL GFSKPRPVAE SSTQSSSSIY YPRAHSGGNT YEGKEYKDSI
     IHSLPAPRPL KRHRANDHIQ CDEGGESSIY IPDIINKGRK IPAREDAYEG SSSSNYHTPN
     VSRAEPPSLS GESHDSKQDV TFSVPSSSVR EHQKARAKKK YIEPRNNETS VIHSLPFGEL
     LAGHRRAKFF ECQECGEAFA RRSELIEHQK IHDRERPSGS RHYERSVIRS LAPSDPQTSY
     AQERFIQEQV RKFRAFGQRS TTSNNLSVQK IYAQETFNAE EPHDKETHGQ KIHDKEPYGK
     EPSGKEPHGD EPQDKEPLDQ EMRSEEPHDD KPHGQEPHDD KPHGQEPHDD KPHGQEPHGD
     EPHGQEPHGD EPHDKEPIDQ EMRSEEPHSE ESHGDEPHGE ESHGQEKVED ATIQASVSEE
     HQKDDAGDAI YECQDCGLGF TDLNDLTSHQ DTHSRKALVD SREYAHSEVH AHSVSEFEKK
     CSGEKLYECP KCGESFIHSS LLFEHQRVHE QDQLYSVKAC DDAFIALLPV RPRRNCTVER
     NPAVSGSAIR CRQCGQGFIH SSALNEHMRQ HRDNEIMEQS ELSDEIFIQG LALTEYQGSE
     TEEKLFECTI CGECFFTAKQ LGDHHTKVHK DEPYEYGPSY THASFLTEPL RKHIPLYECK
     DCGQSFLDDT VIAERMVFHP EREGGSEIVA ATAQEVEANV LIPQEVLRIQ GSNAEAAEPE
     VEAAEPEVEA AEPEVEAAEP NGEAEGPDGE AAEPDGEAEQ PNGEAEQPNG DADEPDGAGI
     EDPEERADEP EEDVEEPEGD ADEPDGADIE DPEEEGEDQE IEVEEPYYNC HECAETFASS
     SAFGEHLKSH ASVIIFEPAN APGECSGYIE RASTSAGGAE QADDKYFKCD VCGQLFNDRL
     SLARHQNSHT G
//
ID   Q3URY3_MOUSE            Unreviewed;       213 AA.
AC   Q3URY3;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 24.
DE   SubName: Full=Putative uncharacterized protein;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK141057; BAE24554.1; -; mRNA.
DR   IPI; IPI00651856; -.
DR   STRING; Q3URY3; -.
DR   PRIDE; Q3URY3; -.
DR   Genevestigator; Q3URY3; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   213 AA;  21677 MW;  F121E2F8A3DE386F CRC64;
     MLPRTKYNRF RNDSVTSVDD LLHSLSVSGS GGKVSAEPAA SPYLVSGEAL RKAPDDGPGS
     LGHLLHKVSH LKLSSSGLRG LSSAARERAG ARLSGSCSAP SLAAPDGGSA TPGSRAPAAS
     MSATRKSRAG DEPLPRPPRG APHTSDQVLG PGVTYVVKVG NPSTLLGGGL GDRVRWGGGS
     QGWGQMSFSE APGFRDKPQG TQTTVGCEEI SPP
//
ID   ZNF48_MOUSE             Reviewed;         591 AA.
AC   Q3US17; Q3UFP3; Q8R0V0; Q921H7;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Zinc finger protein 48;
DE   AltName: Full=Zinc finger protein 553;
GN   Name=Znf48; Synonyms=Zfp48, Zfp553, Znf553;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, Head, and Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family.
CC   -!- SIMILARITY: Contains 12 C2H2-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH12403.1; Type=Erroneous initiation;
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DR   EMBL; AK049208; BAC33610.1; -; mRNA.
DR   EMBL; AK140924; BAE24520.1; -; mRNA.
DR   EMBL; AK146581; BAE27277.1; -; mRNA.
DR   EMBL; AK148378; BAE28517.1; -; mRNA.
DR   EMBL; BC012403; AAH12403.1; ALT_INIT; mRNA.
DR   EMBL; BC026401; AAH26401.1; -; mRNA.
DR   IPI; IPI00153287; -.
DR   RefSeq; NP_666313.1; NM_146201.1.
DR   UniGene; Mm.258371; -.
DR   ProteinModelPortal; Q3US17; -.
DR   SMR; Q3US17; 79-566.
DR   PhosphoSite; Q3US17; -.
DR   PRIDE; Q3US17; -.
DR   Ensembl; ENSMUST00000056232; ENSMUSP00000060967; ENSMUSG00000045598.
DR   Ensembl; ENSMUST00000106312; ENSMUSP00000101919; ENSMUSG00000045598.
DR   GeneID; 233887; -.
DR   KEGG; mmu:233887; -.
DR   UCSC; uc009jur.1; mouse.
DR   CTD; 233887; -.
DR   MGI; MGI:2384725; Zfp553.
DR   eggNOG; roNOG10507; -.
DR   GeneTree; ENSGT00530000063542; -.
DR   HOGENOM; HBG717200; -.
DR   HOVERGEN; HBG018163; -.
DR   InParanoid; Q3US17; -.
DR   OMA; QPHVCGF; -.
DR   OrthoDB; EOG48PMJW; -.
DR   PhylomeDB; Q3US17; -.
DR   NextBio; 381915; -.
DR   ArrayExpress; Q3US17; -.
DR   Bgee; Q3US17; -.
DR   CleanEx; MM_ZFP553; -.
DR   Genevestigator; Q3US17; -.
DR   GermOnline; ENSMUSG00000045598; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 12.
DR   Pfam; PF00096; zf-C2H2; 5.
DR   SMART; SM00355; ZnF_C2H2; 12.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    591       Zinc finger protein 48.
FT                                /FTId=PRO_0000234587.
FT   ZN_FING      83    105       C2H2-type 1.
FT   ZN_FING     111    133       C2H2-type 2.
FT   ZN_FING     163    185       C2H2-type 3.
FT   ZN_FING     191    213       C2H2-type 4.
FT   ZN_FING     246    268       C2H2-type 5.
FT   ZN_FING     274    296       C2H2-type 6.
FT   ZN_FING     302    324       C2H2-type 7.
FT   ZN_FING     330    352       C2H2-type 8.
FT   ZN_FING     423    445       C2H2-type 9.
FT   ZN_FING     451    473       C2H2-type 10.
FT   ZN_FING     516    538       C2H2-type 11.
FT   ZN_FING     544    566       C2H2-type 12.
FT   COMPBIAS    364    426       Pro-rich.
FT   CONFLICT      6      6       G -> E (in Ref. 1; BAE24520).
FT   CONFLICT    194    194       G -> V (in Ref. 1; BAE28517).
FT   CONFLICT    503    503       S -> F (in Ref. 1; BAE28517).
SQ   SEQUENCE   591 AA;  64599 MW;  EE070D2692FA4A73 CRC64;
     MEASPGDEFE HSPQERDGPE IKEEEQLAPT LQVGNTSLKP DGIQCWDDLW DRREGLGKRQ
     PRDPVPRILG EPRWGQGSND RAAVCGECGK SFRQMSDLVK HQRTHTGEKP YKCGVCGKGF
     GDSSARIKHQ RTHTGEKAYR VRPPAPGPPK MPRSRIPAGE RPTICGECGK SFRQSSDLVK
     HQRTHTGEKP YKCGICGKGF GDSSARIKHQ RTHRGDQLPR PVVPRRQPSP AAPAAPHRPK
     AQDKPYICTD CGKRFVLSCS LLSHQRSHLG PKPFGCDVCG KEFARGSDLV KHLRVHTGEK
     PYLCPECGKG FADSSARVKH LRTHSGQRPH ACPECNRSFS LSSTLLRHRL THVEPQDFSL
     AAYPVVPLIP SPPPPPLGTS PSLTPRSPSH SSDGPFGLPG LEPEPGGPQA GEPPPPLAGD
     KPHKCPECGK GFRRSSDLVK HHRVHTGEKP YLCPECGKGF ADSSARVKHL RTHQGERTRP
     PPPPSTLLRP HNPPGSVPIV PQSRVQGRPS GPSQLHVCGF CGKEFPRSSD LVKHRRTHTG
     EKPYKCAECG KGFGDSSARI KHQRGHLALK PFGVGDGPPR PLKEESPAGL E
//
ID   PLCL1_MOUSE             Reviewed;        1096 AA.
AC   Q3USB7; Q3TSM9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Inactive phospholipase C-like protein 1;
DE            Short=PLC-L1;
DE   AltName: Full=Phospholipase C-related but catalytically inactive protein;
DE            Short=PRIP;
GN   Name=Plcl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION AT THR-94, AND MUTAGENESIS OF THR-94.
RX   PubMed=15306641; DOI=10.1523/JNEUROSCI.1323-04.2004;
RA   Terunuma M., Jang I.S., Ha S.H., Kittler J.T., Kanematsu T.,
RA   Jovanovic J.N., Nakayama K.I., Akaike N., Ryu S.H., Moss S.J.,
RA   Hirata M.;
RT   "GABAA receptor phospho-dependent modulation is regulated by
RT   phospholipase C-related inactive protein type 1, a novel protein
RT   phosphatase 1 anchoring protein.";
RL   J. Neurosci. 24:7074-7084(2004).
RN   [3]
RP   FUNCTION.
RX   PubMed=16854455; DOI=10.1016/j.advenzreg.2006.01.006;
RA   Yanagihori S., Terunuma M., Koyano K., Kanematsu T., Ho Ryu S.,
RA   Hirata M.;
RT   "Protein phosphatase regulation by PRIP, a PLC-related catalytically
RT   inactive protein -- implications in the phospho-modulation of the
RT   GABAA receptor.";
RL   Adv. Enzyme Regul. 46:203-222(2006).
RN   [4]
RP   FUNCTION.
RX   PubMed=17301177; DOI=10.1523/JNEUROSCI.3155-06.2007;
RA   Mizokami A., Kanematsu T., Ishibashi H., Yamaguchi T., Tanida I.,
RA   Takenaka K., Nakayama K.I., Fukami K., Takenawa T., Kominami E.,
RA   Moss S.J., Yamamoto T., Nabekura J., Hirata M.;
RT   "Phospholipase C-related inactive protein is involved in trafficking
RT   of gamma2 subunit-containing GABA(A) receptors to the cell surface.";
RL   J. Neurosci. 27:1692-1701(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-557, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Involved in an inositol phospholipid-based intracellular
CC       signaling cascade. Shows no PLC activity to phosphatidylinositol
CC       4,5-bisphosphate and phosphatidylinositol. Component in the
CC       phospho-dependent endocytosis process of GABA A receptor. Acts as
CC       a inhibitor of PPP1C (By similarity). Involved in the assembly
CC       and/or the trafficking of gamma-2 subunit-containing GABA A
CC       receptors.
CC   -!- SUBUNIT: Interacts with PPP2CA, Ins(1,4,5)P3, Ins(1,4,5,6)P4
CC       GABARAP, GABA receptor beta subunits, GABA receptor gamma-2
CC       subunits and PPP1C (By similarity). May form a ternary complex
CC       with GABA receptor beta subunit and GABARAP. The formation of a
CC       ternary complex with GABA receptor beta subunit and GABARAP could
CC       be the key step for facilitating the association of GABARAP with
CC       the GABA receptor gamma-2 subunit and to allow it to be
CC       transported at the right destination.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- PTM: Phosphorylated by the catalytic subunit of PKA.
CC       Phosphorylation of Thr-94 resulted in dissociation of PPP1C from
CC       PRIP1.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 PI-PLC X-box domain.
CC   -!- SIMILARITY: Contains 1 PI-PLC Y-box domain.
CC   -!- CAUTION: The PI-PLC X-box lacks the essential His at position 459
CC       which is replaced by a Asn and is predicted to be inactive.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK140530; BAE24416.1; -; mRNA.
DR   EMBL; AK161943; BAE36646.1; -; mRNA.
DR   IPI; IPI00128145; -.
DR   RefSeq; NP_001108135.1; NM_001114663.1.
DR   UniGene; Mm.194183; -.
DR   ProteinModelPortal; Q3USB7; -.
DR   SMR; Q3USB7; 110-855.
DR   STRING; Q3USB7; -.
DR   PhosphoSite; Q3USB7; -.
DR   PRIDE; Q3USB7; -.
DR   Ensembl; ENSMUST00000042986; ENSMUSP00000037854; ENSMUSG00000038349.
DR   GeneID; 227120; -.
DR   KEGG; mmu:227120; -.
DR   UCSC; uc007ban.1; mouse.
DR   CTD; 227120; -.
DR   MGI; MGI:3036262; Plcl1.
DR   eggNOG; roNOG08466; -.
DR   GeneTree; ENSGT00570000078720; -.
DR   HOGENOM; HBG527074; -.
DR   HOVERGEN; HBG108265; -.
DR   InParanoid; Q3USB7; -.
DR   OrthoDB; EOG40ZQWV; -.
DR   NextBio; 378488; -.
DR   ArrayExpress; Q3USB7; -.
DR   Bgee; Q3USB7; -.
DR   CleanEx; MM_PLCL1; -.
DR   Genevestigator; Q3USB7; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0050811; F:GABA receptor binding; TAS:MGI.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:InterPro.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0007610; P:behavior; IMP:MGI.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR015359; Phospholipase_C_EF-hand-like.
DR   InterPro; IPR001711; Phospholipase_C_Pinositol-sp_Y.
DR   InterPro; IPR001192; Pinositol_Phospholipase-C.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:3.20.20.190; PLC-like_Pdiesterase_TIM-brl; 2.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF09279; efhand_like; 1.
DR   Pfam; PF00388; PI-PLC-X; 1.
DR   Pfam; PF00387; PI-PLC-Y; 1.
DR   PRINTS; PR00390; PHPHLIPASEC.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00148; PLCXc; 1.
DR   SMART; SM00149; PLCYc; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF51695; PLC-like_Pdiesterase_TIM-brl; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Phosphoprotein; Transducer.
FT   CHAIN         1   1096       Inactive phospholipase C-like protein 1.
FT                                /FTId=PRO_0000319415.
FT   DOMAIN      114    224       PH.
FT   DOMAIN      399    543       PI-PLC X-box.
FT   DOMAIN      586    702       PI-PLC Y-box.
FT   DOMAIN      709    814       C2.
FT   REGION       83    222       Interaction with PPP1C (By similarity).
FT   REGION      544    568       Interaction with GABA A beta subunit (By
FT                                similarity).
FT   COILED     1040   1060       Potential.
FT   MOD_RES      94     94       Phosphothreonine; by PKA.
FT   MOD_RES      96     96       Phosphoserine; by PKA.
FT   MOD_RES     557    557       Phosphothreonine.
FT   MUTAGEN      94     94       T->A: Decreased level of phosphorylation.
FT                                Loss of phosphorylation; when associated
FT                                with A-96.
FT   MUTAGEN      96     96       S->A: Decreased level of phosphorylation.
FT                                Loss of phosphorylation; when associated
FT                                with A-94.
FT   CONFLICT    116    116       M -> I (in Ref. 1; BAE36646).
SQ   SEQUENCE   1096 AA;  122672 MW;  DE11ADB8D0591578 CRC64;
     MAEGAASREA PAPLDVAGGE DDPRAGADAA SGDAPPPALG GRMRDRRSGV ALPGAAGVPA
     DSEAGLLEAA RATPRRSSII KDPSNQKCGG RKKTVSFSSM PSEKKISSAH DCISFMQAGC
     ELKKVRPNSR IYNRFFTLDT DLQALRWEPS KKDLEKAKLD ISAIKEIRLG KNTETFRNNG
     LADQICEDCA FSILHGENYE SLDLVANSAD VANIWVSGLR YLVSRSKQPL DFIEGNQNTP
     RFMWLKTVFE AADVDGNGIM LEDTSVELIK QLNPTLKESK IRLKFKEIQK SKEKLTTRVT
     EEEFCEAFCE LCTRPEVYFL LVQISKNKEY LDANDLMLFL EAEQGVTHIT EDMCLDIIRR
     YELSEDGRQK GFLAIDGFTQ YLLSPECDIF DPEQKKVAQD MTQPLSHYYI NASHNTYLIE
     DQFRGPADIN GYVRALKMGC RSIELDVSDG PDNEPILCNR NNMAMHLSFR SVLEVINKFA
     FVASEYPLIL CLGNHCSLPQ QKVMAQQMKK VFGEKLYTEA PLSSESYLPS PEKLKNMIIV
     KGKKLPSESD LLEGEVTDED EEAEMSRRMS GDYNGEQKHI WLCRELSDLV SICKSVQHRD
     FELSMKTQNY WEMCSFSETE ASRIANEYPE DFVNYNKKFL SRVYPSAMRI DSSNLNPQDF
     WNCGCQIVAM NFQTPGPMMD LHTGWFLQNG GCGYVLRPSI MRDEVSYFSA NTKGIVPGVS
     PLVLHIKIIS GQNFPKPKGA CAKGDVIDPY VCVEIHGIPA DCCEQRTKTV QQNSDNPIFD
     ETFEFQVNLP ELTMVRFVIL DDDYIGDEFI GQYTIPFECL QPGYRHVPLR SFVGDIMEHV
     TLFVHIAITN RSGGGKPQKR SLSVRMGKKV REYTMLRNIG LKTIDDIFKI AVHPLREAID
     MRENMQNAIV SVKELCGLPP IASLKQCLLT LSSRLITSDS TPSVSLVMKD CFPYLEPLGA
     IPNVQKRMLA AYDLMIQESR VLIEMADTVQ EKIVQCQKAG MEFHEELHNL GAKEGLKGRK
     LNKAIESFAW NITVLKGQGD LLKNAKNEAV ENIKQIQLAC LSCGLSKGPG GGSEAKGKRS
     LEAIEEKESS EENGKL
//
ID   F196A_MOUSE             Reviewed;         422 AA.
AC   Q3USH1; B2RY32;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 38.
DE   RecName: Full=Protein FAM196A;
GN   Name=Fam196a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the FAM196 family.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK140373; BAE24361.1; -; mRNA.
DR   EMBL; BC158077; AAI58078.1; -; mRNA.
DR   EMBL; BC158080; AAI58081.1; -; mRNA.
DR   IPI; IPI00851098; -.
DR   UniGene; Mm.323610; -.
DR   UniGene; Mm.450655; -.
DR   ProteinModelPortal; Q3USH1; -.
DR   Ensembl; ENSMUST00000097984; ENSMUSP00000095598; ENSMUSG00000073805.
DR   UCSC; uc009kdz.1; mouse.
DR   MGI; MGI:3605068; Fam196a.
DR   eggNOG; roNOG06614; -.
DR   GeneTree; ENSGT00530000063787; -.
DR   HOGENOM; HBG443902; -.
DR   HOVERGEN; HBG064694; -.
DR   InParanoid; Q3USH1; -.
DR   OMA; QQIVPHT; -.
DR   OrthoDB; EOG47M1XX; -.
DR   ArrayExpress; Q3USH1; -.
DR   Bgee; Q3USH1; -.
DR   Genevestigator; Q3USH1; -.
PE   2: Evidence at transcript level;
KW   Coiled coil.
FT   CHAIN         1    422       Protein FAM196A.
FT                                /FTId=PRO_0000329447.
FT   COILED      344    370       Potential.
SQ   SEQUENCE   422 AA;  46222 MW;  65836FDBE3B0774E CRC64;
     MVSKDSGRCI LTTPEREVEP AACLALEMRY ALDPNRQIKK RNKALQVRFK DICEAQNEQR
     DTQLSSGPLG EKREAKAVSC RVAYRKYMTV PARRSIPNVT KSTGVQTSPD LRKCYQTFPL
     DRKKGSLKGL PAADAFKSQN NGFLADSKEK SEAGPMEEPR PCSAGRIHKT TALVFHSNEH
     VNALGQPSGV NCAELCKSPD VLGYPEAVLQ NSRPPSEEPI HQLQGRAKLD RGTLDSEEPA
     PLTHGRVFKT EVATVYPPAI STRAPEPGLS NSAAASQWSL CPADEEQRRA AHLNGLQAST
     GSAVACSTPV QYLSPECSEQ PLQNQPSPTA GIGDEEHQQI VPHTEVVDLK AQLQVMENLI
     SSSQETIKVL LGVIQELEKG EAHREGLSYR TGQDTANCDT CRNSACIIYR YVNILFPLCY
     SE
//
ID   Q3USH5_MOUSE            Unreviewed;       845 AA.
AC   Q3USH5;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 36.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Sfswap; Synonyms=Sfrs8, Srsf8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Adipose;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Adipose;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Adipose;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Adipose;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Adipose;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Adipose;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Adipose;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Adipose;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
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DR   EMBL; AK140369; BAE24357.1; -; mRNA.
DR   IPI; IPI00274030; -.
DR   RefSeq; NP_758480.2; NM_172276.3.
DR   UniGene; Mm.288714; -.
DR   STRING; Q3USH5; -.
DR   Ensembl; ENSMUST00000053737; ENSMUSP00000062413; ENSMUSG00000029439.
DR   GeneID; 231769; -.
DR   KEGG; mmu:231769; -.
DR   CTD; 231769; -.
DR   MGI; MGI:101760; Sfswap.
DR   eggNOG; roNOG11666; -.
DR   HOGENOM; HBG278218; -.
DR   HOVERGEN; HBG079184; -.
DR   InParanoid; Q3USH5; -.
DR   OrthoDB; EOG4ZW59T; -.
DR   NextBio; 380743; -.
DR   ArrayExpress; Q3USH5; -.
DR   Bgee; Q3USH5; -.
DR   Genevestigator; Q3USH5; -.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   InterPro; IPR019147; Splice_fac_sup-white-apricot.
DR   InterPro; IPR000061; Surp.
DR   Pfam; PF09750; DRY_EERY; 1.
DR   Pfam; PF01805; Surp; 2.
DR   SMART; SM00648; SWAP; 2.
DR   PROSITE; PS50128; SURP; 2.
PE   1: Evidence at protein level;
FT   NON_TER     845    845
SQ   SEQUENCE   845 AA;  93499 MW;  8669C20AA563EB3F CRC64;
     MYGAGGGRAK PERKGGVKEE AGPGGTGTGG NRVELLVFGY ACKLFRDDER ALAQEQGQHL
     IPWMGDPKIL IDRYDGRGHL HDLSAYDAEY ATWNRDYQLS EEEARVEALC DEERYLALHT
     DLLEEEARQE EEYKRLSEAL AEDGNYSAVG FTYGSDYYDP SEPTEEEEPS KQREKNEAEN
     LEENEEPFIA PLGLSVPSDV ELPPTAKMHA IIERTANFVC KQGAQFEIML KAKQARNSQF
     DFLRFDHYLN PYYKFIQKAM KEGRYTVLAE SKNEEKKKSG PTSDNEEEDD EEDGSYLHPS
     LFASKKSSRL EELMKPLKVV DPDHPLAALV RKAQADSSAP APPTADGTPA QPSQVEYTAD
     STVAAMYYSY YMLPDGTYCL APPPPGIDVA TYYSTLPAGV TVSSSPGVTT TVPPPPGTTP
     PPPPTTAEPS SGVTSTTTTT SALAPVAIIP PPPDIQPVID KLAEYVARNG LKFETSVRAK
     NDQRFEFLQP WHQYNAYYEF KKQFFLQKEG GGSTQAASTA EEAPTETAVE ESGEAGEDGA
     PEGMAETGGR GSGKKEAGSS KSTVDGKLVK ASFAPISFAI KAKENDLLPL EKNRVKLDDD
     SEEDEESREC QESTSSVANP SPAAAPPSVA VEEKKPQLTQ EELEAKQAKQ KLEDRLAAAA
     REKLAQASKE SKEKQLQAER KRKAALFLQT LKNPLPEAEV GKLEESTFGV EDTGVMPCPL
     LVGGRTLPIL EGKPPERPSN RCRDPPREEE REKKKKKHKK RSRTRSRSPK YHSSSKPRSR
     SHSKAKHSLP SAYRTVRRSR SRSRSPRRRA HSPERRREER SVPTAYRMSG SPGVSRKRTR
     SRSPH
//
ID   FCSD2_MOUSE             Reviewed;         740 AA.
AC   Q3USJ8; Q3UQZ2; Q6P9R0; Q80TS2;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=FCH and double SH3 domains protein 2;
DE   AltName: Full=SH3 multiple domains protein 3;
GN   Name=Fchsd2; Synonyms=Kiaa0769, Sh3md3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION.
RX   PubMed=15067381;
RA   Katoh M., Katoh M.;
RT   "Identification and characterization of human FCHSD1 and FCHSD2 genes
RT   in silico.";
RL   Int. J. Mol. Med. 13:749-754(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBUNIT: Interacts with CASK and MAGI1. CASK inhibits interaction
CC       with MAGI1 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3USJ8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3USJ8-2; Sequence=VSP_023171;
CC       Name=3;
CC         IsoId=Q3USJ8-3; Sequence=VSP_023170, VSP_023171;
CC   -!- SIMILARITY: Contains 1 FCH domain.
CC   -!- SIMILARITY: Contains 2 SH3 domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65650.1; Type=Erroneous initiation;
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DR   EMBL; AK122368; BAC65650.1; ALT_INIT; mRNA.
DR   EMBL; AK140322; BAE24333.1; -; mRNA.
DR   EMBL; AK141949; BAE24896.1; -; mRNA.
DR   EMBL; BC060647; AAH60647.1; -; mRNA.
DR   IPI; IPI00330221; -.
DR   IPI; IPI00762440; -.
DR   IPI; IPI00828617; -.
DR   RefSeq; NP_001139482.1; NM_001146010.1.
DR   RefSeq; NP_950177.2; NM_199012.2.
DR   UniGene; Mm.263041; -.
DR   HSSP; P10686; 1Y0M.
DR   ProteinModelPortal; Q3USJ8; -.
DR   SMR; Q3USJ8; 460-630.
DR   STRING; Q3USJ8; -.
DR   PhosphoSite; Q3USJ8; -.
DR   PRIDE; Q3USJ8; -.
DR   Ensembl; ENSMUST00000032931; ENSMUSP00000032931; ENSMUSG00000030691.
DR   Ensembl; ENSMUST00000098250; ENSMUSP00000095850; ENSMUSG00000030691.
DR   GeneID; 207278; -.
DR   KEGG; mmu:207278; -.
DR   CTD; 207278; -.
DR   MGI; MGI:2448475; Fchsd2.
DR   GeneTree; ENSGT00510000046732; -.
DR   HOVERGEN; HBG063540; -.
DR   OMA; QLTREYN; -.
DR   OrthoDB; EOG43R3M6; -.
DR   NextBio; 371920; -.
DR   ArrayExpress; Q3USJ8; -.
DR   Bgee; Q3USJ8; -.
DR   CleanEx; MM_FCHSD2; -.
DR   Genevestigator; Q3USJ8; -.
DR   InterPro; IPR001060; FCH.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00018; SH3_1; 2.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 2.
DR   SUPFAM; SSF50044; SH3; 2.
DR   PROSITE; PS50133; FCH; 1.
DR   PROSITE; PS50002; SH3; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Phosphoprotein; Repeat; SH3 domain.
FT   CHAIN         1    740       FCH and double SH3 domains protein 2.
FT                                /FTId=PRO_0000278215.
FT   DOMAIN        8     74       FCH.
FT   DOMAIN      469    530       SH3 1.
FT   DOMAIN      567    629       SH3 2.
FT   COILED      356    397       Potential.
FT   COMPBIAS    718    721       Poly-Pro.
FT   MOD_RES     683    683       Phosphoserine.
FT   VAR_SEQ       1     38       Missing (in isoform 3).
FT                                /FTId=VSP_023170.
FT   VAR_SEQ     308    308       T -> TSLKAAQLVDIELSPVSALRMTIAE (in
FT                                isoform 2 and isoform 3).
FT                                /FTId=VSP_023171.
FT   CONFLICT    350    350       N -> D (in Ref. 2; BAE24333).
SQ   SEQUENCE   740 AA;  84282 MW;  31BB6275D922AE8E CRC64;
     MQPPPRKVKV TQELRNIQGE QMTKLQAKHQ AECDLLEDMR TFSQKKAAIE REYAQGIQKL
     ASQYLKRDWP GIKTDDRNDY RSMYPVWKSF LEGTMQVAQS RINICENYKN FISEPARAVR
     SLKEQQLKRC VDQLTKIQTE LQETVKDLVK GKKKYFETEQ MAHAVREKAD IEAKSKLSLF
     QSRISLQKAS VKLKARRSEC NTKATHARND YLLTLAAANA HQDRYYQTDL VNIMKALDGN
     VYDHLKDYLI AFSRTELETC QAIQNTFQFL LENSSKVVRD YNLQLFLQEN AVFHKPQPFQ
     FQPCDSDTSR QLESETGTTE EHSLNKEARK WATRVAREHK NIVHQQRVLN ELECHGVALS
     EQSRAELEQK IDEARESIRK AEIIKLKAEA RLDLLKQIGV SVDTWLKSAM NQVMEELENE
     RWARPPAVTS NGTLHSLNAD AEREEGEEFE DNMDVFDDSS SSPSGTLRNY PLTCKVVYSY
     KASQPDELTI EEHEVLEVIE DGDMEDWVKA RNKVGQVGYV PEKYLQFPTS NSLLSMLQSL
     AALDSRSHTS SNSTEAELVS GSLNGDASVC FVKALYDYEG QTDDELSFPE GAIIRILNKE
     NQDDDGFWEG EFSGRIGVFP SVLVEELSAS ENGDTPWTRE IQISPSPKPH TSLPPLPLYD
     QPPSSPYPSP DKRSSQFFPR SPSANENSLH AESPGFSQAS RQTPDTSYGK LRPVRAAPPP
     PTQNHRRTTE KMEDVEITLV
//
ID   Q3UT39_MOUSE            Unreviewed;       499 AA.
AC   Q3UT39;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 35.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Arid1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK139800; BAE24141.1; -; mRNA.
DR   IPI; IPI00420572; -.
DR   UniGene; Mm.133401; -.
DR   STRING; Q3UT39; -.
DR   Ensembl; ENSMUST00000077329; ENSMUSP00000076554; ENSMUSG00000069729.
DR   Ensembl; ENSMUST00000092723; ENSMUSP00000090398; ENSMUSG00000069729.
DR   Ensembl; ENSMUST00000115799; ENSMUSP00000111465; ENSMUSG00000069729.
DR   MGI; MGI:1926129; Arid1b.
DR   eggNOG; roNOG07001; -.
DR   HOGENOM; HBG403164; -.
DR   HOVERGEN; HBG075244; -.
DR   InParanoid; Q3UT39; -.
DR   OrthoDB; EOG4G7BXG; -.
DR   ArrayExpress; Q3UT39; -.
DR   Bgee; Q3UT39; -.
DR   Genevestigator; Q3UT39; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR021906; DUF3518.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF12031; DUF3518; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   499 AA;  55260 MW;  9AB8B52CFBEE2C59 CRC64;
     DSEKIESEGK SSPALAAPDA SVDPKETPKQ ASKFDKLPIK IVKKNKLFVV DRSDKLGRVQ
     EFSSGLLHWQ LGGGDTTEHI QTHFESKMEI PPRRRPPPPL SSTGKKKELE GKGDSEEQPE
     KSIIATIDDV LSARPGALPE DTNPGPQTDS GKFPFGIQQA KSHRNIRLLE DEPRSRDETP
     LCTIAHWQDS LAKRCICVSN IVRSLSFVPG NDAEMSKHPG LVLILGKLIL LHHEHPERKR
     APQTYEKEED EDKGVACSKD EWWWDCLEVL RDNTLVTLAN ISGQLDLSAY TESICLPILD
     GLLHWMVCPS AEAQDPFPTV GPNSVLSPQR LVLETLCKLS IQDNNVDLIL ATPPFSRQEK
     FYATLVRYVG DRKNPVCREM SMALLSNLAQ GDTLAARAIA VQKGSIGNLI SFLEDGVTMA
     QYQQSQHNLM HMQPPPLEPP SVDMMCRAAK ALLAMARVDE NRSEFLLHEG RLLDISISAV
     LNSLVASVIC DVLFQIGQL
//
ID   SRBS2_MOUSE             Reviewed;        1180 AA.
AC   Q3UTJ2; Q3USC6; Q80TS1; Q8BJL6; Q8BJU3; Q8BLW9; Q8BX47; Q8CHU0;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   08-FEB-2011, entry version 44.
DE   RecName: Full=Sorbin and SH3 domain-containing protein 2;
DE   AltName: Full=Arg/Abl-interacting protein 2;
DE            Short=ArgBP2;
GN   Name=Sorbs2; Synonyms=Argbp2, Kiaa0777;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 6),
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-532 (ISOFORM 1),
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 229-313 (ISOFORM 7), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1097-1180 (ISOFORM 5).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Aorta, Brain cortex, Cerebellum, Embryoid bodies, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 162-1180 (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-829, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; THR-451 AND SER-456.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40; SER-130; SER-358;
RP   SER-378; SER-379; SER-382; SER-1097 AND SER-1098, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239 AND SER-339, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Adapter protein that plays a role in the assembling of
CC       signaling complexes, being a link between ABL kinases and actin
CC       cytoskeleton. Can form complex with ABL1 and CBL, thus promoting
CC       ubiquitination and degradation of ABL1 or with AKT1 and PAK1, thus
CC       mediating AKT1-mediated activation of PAK1 (By similarity).
CC   -!- SUBUNIT: Interacts with ABL, CBL, DNM1, DNM2, FLOT1, MLLT4/afadin,
CC       PTK2B/PYK2, SAPAP, SPTAN1, SYNJ1, SYNJ2, VCL/vinculin, WASF,
CC       ABL1/c-Abl, ABL2/v-Abl/Arg, ACTN, AKT1, CBL, PALLD and PAK1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region (By
CC       similarity). Cytoplasm, myofibril, sarcomere, Z-disk (By
CC       similarity). Cell junction, focal adhesion (By similarity).
CC       Cytoplasm, cytoskeleton (By similarity). Note=Found at the Z-disk
CC       sarcomeres, stress fibers, dense bodies and focal adhesion (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=1;
CC         IsoId=Q3UTJ2-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q3UTJ2-2; Sequence=VSP_034802, VSP_034803;
CC         Note=No experimental confirmation available. Contains
CC         phosphoserine at position 353 and at position 355;
CC       Name=3;
CC         IsoId=Q3UTJ2-3; Sequence=VSP_034800, VSP_034802, VSP_034809,
CC                                  VSP_034810;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q3UTJ2-4; Sequence=VSP_034800, VSP_034809;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q3UTJ2-5; Sequence=VSP_034801, VSP_034802, VSP_034804,
CC                                  VSP_034809, VSP_034811;
CC         Note=No experimental confirmation available. Contains
CC         phosphoserine at position 322, at position 330, at position 332
CC         and at position 350;
CC       Name=6;
CC         IsoId=Q3UTJ2-6; Sequence=VSP_034801, VSP_034802, VSP_034805,
CC                                  VSP_034808;
CC         Note=No experimental confirmation available;
CC       Name=7;
CC         IsoId=Q3UTJ2-7; Sequence=VSP_034806, VSP_034807;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Ubiquitinated by CBL (By similarity).
CC   -!- SIMILARITY: Contains 3 SH3 domains.
CC   -!- SIMILARITY: Contains 1 SoHo domain.
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DR   EMBL; AK041051; BAC30799.1; -; mRNA.
DR   EMBL; AK049030; BAC33518.1; -; mRNA.
DR   EMBL; AK079130; BAC37554.1; -; mRNA.
DR   EMBL; AK083429; BAC38913.1; -; mRNA.
DR   EMBL; AK139388; BAE23988.1; -; mRNA.
DR   EMBL; AK140498; BAE24407.1; -; mRNA.
DR   EMBL; BC039163; AAH39163.1; -; mRNA.
DR   EMBL; AK122369; BAC65651.1; -; mRNA.
DR   IPI; IPI00405462; -.
DR   IPI; IPI00673886; -.
DR   IPI; IPI00900398; -.
DR   IPI; IPI00900438; -.
DR   IPI; IPI00900461; -.
DR   IPI; IPI00900464; -.
DR   IPI; IPI00923680; -.
DR   RefSeq; NP_766340.3; NM_172752.3.
DR   UniGene; Mm.211096; -.
DR   UniGene; Mm.447653; -.
DR   ProteinModelPortal; Q3UTJ2; -.
DR   SMR; Q3UTJ2; 947-1180.
DR   STRING; Q3UTJ2; -.
DR   Ensembl; ENSMUST00000037085; ENSMUSP00000040790; ENSMUSG00000031626.
DR   Ensembl; ENSMUST00000067065; ENSMUSP00000070720; ENSMUSG00000031626.
DR   Ensembl; ENSMUST00000067107; ENSMUSP00000067641; ENSMUSG00000031626.
DR   GeneID; 234214; -.
DR   KEGG; mmu:234214; -.
DR   CTD; 234214; -.
DR   MGI; MGI:1924574; Sorbs2.
DR   eggNOG; roNOG06783; -.
DR   GeneTree; ENSGT00550000074287; -.
DR   HOVERGEN; HBG108509; -.
DR   NextBio; 382063; -.
DR   Bgee; Q3UTJ2; -.
DR   Genevestigator; Q3UTJ2; -.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR000108; p67phox.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR003127; Sorb.
DR   InterPro; IPR007087; Znf_C2H2.
DR   Pfam; PF00018; SH3_1; 2.
DR   Pfam; PF07653; SH3_2; 1.
DR   Pfam; PF02208; Sorb; 1.
DR   PRINTS; PR00499; P67PHOX.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 3.
DR   SMART; SM00459; Sorb; 1.
DR   SUPFAM; SSF50044; SH3; 3.
DR   PROSITE; PS50002; SH3; 3.
DR   PROSITE; PS50831; SOHO; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cytoplasm; Cytoskeleton;
KW   Phosphoprotein; Repeat; SH3 domain; Ubl conjugation.
FT   CHAIN         1   1180       Sorbin and SH3 domain-containing protein
FT                                2.
FT                                /FTId=PRO_0000344478.
FT   DOMAIN      166    230       SoHo.
FT   DOMAIN      943   1002       SH3 1.
FT   DOMAIN     1018   1079       SH3 2.
FT   DOMAIN     1121   1180       SH3 3.
FT   COMPBIAS    720    731       His-rich.
FT   COMPBIAS   1011   1014       Poly-Pro.
FT   MOD_RES      27     27       Phosphoserine.
FT   MOD_RES      40     40       Phosphoserine.
FT   MOD_RES     130    130       Phosphoserine.
FT   MOD_RES     239    239       Phosphoserine.
FT   MOD_RES     339    339       Phosphoserine.
FT   MOD_RES     357    357       Phosphothreonine (By similarity).
FT   MOD_RES     358    358       Phosphoserine.
FT   MOD_RES     378    378       Phosphoserine.
FT   MOD_RES     379    379       Phosphoserine.
FT   MOD_RES     381    381       Phosphoserine (By similarity).
FT   MOD_RES     382    382       Phosphoserine.
FT   MOD_RES     451    451       Phosphothreonine.
FT   MOD_RES     456    456       Phosphoserine.
FT   MOD_RES     829    829       Phosphoserine.
FT   MOD_RES    1097   1097       Phosphoserine.
FT   MOD_RES    1098   1098       Phosphoserine.
FT   VAR_SEQ       4     34       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_034800.
FT   VAR_SEQ      45     67       Missing (in isoform 5 and isoform 6).
FT                                /FTId=VSP_034801.
FT   VAR_SEQ     211    211       P -> PDEDTDMYNTPYTYNA (in isoform 2,
FT                                isoform 3, isoform 5 and isoform 6).
FT                                /FTId=VSP_034802.
FT   VAR_SEQ     308    308       P -> PPPLPPTPTPVPREPSRKPLSVSPSTDGLRSPSPPP
FT                                RSCVPAPRPSAPDLSPTRTGRINPADIDLENEPWYKFFSEL
FT                                EFGHPPPKKALDYVQDHSSGVSNE (in isoform 2).
FT                                /FTId=VSP_034803.
FT   VAR_SEQ     308    308       P -> PPPLPPTPTPVPREPSRKPLSVSPSTDGLRSPSPPP
FT                                RSCVPAPCPSAPDLSPTRPPKKALDYVQDHSSGVSNE (in
FT                                isoform 5).
FT                                /FTId=VSP_034804.
FT   VAR_SEQ     309    316       VSIYQSSI -> RSVSSRPL (in isoform 6).
FT                                /FTId=VSP_034805.
FT   VAR_SEQ     311    313       IYQ -> PCH (in isoform 7).
FT                                /FTId=VSP_034806.
FT   VAR_SEQ     314   1180       Missing (in isoform 7).
FT                                /FTId=VSP_034807.
FT   VAR_SEQ     317   1180       Missing (in isoform 6).
FT                                /FTId=VSP_034808.
FT   VAR_SEQ     388    914       Missing (in isoform 3, isoform 4 and
FT                                isoform 5).
FT                                /FTId=VSP_034809.
FT   VAR_SEQ    1126   1180       FQALYNYTPRNEDELELRESDVVDVMEKCDDGWFVGTSRRT
FT                                KFFGTFPGNYVKRL -> LQ (in isoform 3).
FT                                /FTId=VSP_034810.
FT   VAR_SEQ    1126   1135       Missing (in isoform 5).
FT                                /FTId=VSP_034811.
FT   CONFLICT    249    249       V -> A (in Ref. 2; AAH39163).
FT   CONFLICT    944    944       E -> EV (in Ref. 1; BAE24407).
SQ   SEQUENCE   1180 AA;  132349 MW;  99ECA798E95A092E CRC64;
     MNTDSGGCAR KRAAMSVTLT SVKRVQSSPN LLAAGRESQS PDSAWRSYND RNPETLNGDA
     TYSSLAAKGF RSVRPNLQDK RSPTQSQITI NGNSGGAVSP VSYYQRPFSP SAYSLPASLN
     SSIIMQHGRS LDSAETYSQH AQSLDGTMGS SIPLYRSSEE EKRVTVIKAP HYPGIGPVDE
     SGIPTAIRTT VDRPKDWYKT MFKQIHMVHK PGLYNSPYSA QSHPAAKTQT YRPLSKSHSD
     NGTDAFKEVP SPVPPPHVPP RPRDQSSTLK HDWDPPDRKV DTRKFRSEPR SIFEYEPGKS
     SILQHERPVS IYQSSIDRSL ERPSSSASMA GDFRKRRKSE PAVGPLRGLG DQSSSRTSPG
     RADLPGSSST FTKSFISSSP SSPSRAQGGD DSKMCPPLCS YSGLNGTPSG ELECCNAYRQ
     HLDVPGDSQR AITFKNGWQM ARQNAEIWSS TEETVSPKIK SRSCDDLLND DCDSFPDPKT
     KSESMGSLLC EEDSKESCPM TWASPYIQEV CGNSRSRLKH RSAHNAPGFL KMYKKMHRIN
     RKDLMNSEVI CSVKSRILQY EKEQQHRGLL HGWSQSSTEE VPRDVVPTRI SEFEKLIQKS
     KSMPNLGDEM LSPITLEPPQ NGLCPKRRFS IESLLEEETQ VRHPSQGQRS CKSNTLVPIH
     IEVTSDEQPR THMEFSDSDQ DGVVSDHSDY VHVEGSSFCS ESDFDHFSFT SSESFYGSSH
     HHHHHHHHHR HLISSCKGRC PASYTRFTTM LKHERAKHEN MDRPRRQEMD PGLSKLAFLV
     SPVPFRRKKI LTPQKQTEKA KCKASVVEAL DSALKDICDQ IKAEKRRGSL PDNSILHRLI
     SELLPQIPER NSSLHALKRS PMHQPFHPLP PDGASHCPLY QNDCGRMPHS ASFPDVDTTS
     NYHAQDYGSA LSLQDHESPR SYSSTLTDLG RSASRERRGT PEKEKLPAKA VYDFKAQTSK
     ELSFKKGDTV YILRKIDQNW YEGEHHGRVG IFPISYVEKL TPPEKAQPAR PPPPVQPGEI
     GEAIAKYNFN ADTNVELSLR KGDRIILLKR VDQNWYEGKI PGTNRQGIFP VSYVEVVKRN
     AKGAEDYPDP PLPHSYSSDR IYTLSSNKPQ RPGFSHENIQ GGGEPFQALY NYTPRNEDEL
     ELRESDVVDV MEKCDDGWFV GTSRRTKFFG TFPGNYVKRL
//
ID   Q3UTP5_MOUSE            Unreviewed;       921 AA.
AC   Q3UTP5;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Slc8a3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK139260; BAE23935.1; -; mRNA.
DR   IPI; IPI00655009; -.
DR   RefSeq; NP_001161392.1; NM_001167920.1.
DR   RefSeq; NP_536688.2; NM_080440.3.
DR   UniGene; Mm.443748; -.
DR   ProteinModelPortal; Q3UTP5; -.
DR   SMR; Q3UTP5; 396-675.
DR   STRING; Q3UTP5; -.
DR   Ensembl; ENSMUST00000064594; ENSMUSP00000063258; ENSMUSG00000079055.
DR   GeneID; 110893; -.
DR   KEGG; mmu:110893; -.
DR   CTD; 110893; -.
DR   MGI; MGI:107976; Slc8a3.
DR   eggNOG; roNOG06049; -.
DR   HOVERGEN; HBG006441; -.
DR   InParanoid; Q3UTP5; -.
DR   OrthoDB; EOG4H4633; -.
DR   Bgee; Q3UTP5; -.
DR   Genevestigator; Q3UTP5; -.
DR   GO; GO:0005887; C:integral to plasma membrane; IC:MGI.
DR   GO; GO:0005432; F:calcium:sodium antiporter activity; IEA:InterPro.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   InterPro; IPR003644; Calx_beta.
DR   InterPro; IPR004836; Na_Ca_Ex.
DR   InterPro; IPR004837; NaCa_Exmemb.
DR   Pfam; PF03160; Calx-beta; 2.
DR   Pfam; PF01699; Na_Ca_ex; 2.
DR   PRINTS; PR01259; NACAEXCHNGR.
DR   SMART; SM00237; Calx_beta; 2.
DR   TIGRFAMs; TIGR00845; caca; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
SQ   SEQUENCE   921 AA;  102441 MW;  72D3D72DA85DBF2D CRC64;
     MAWLRLQPLT SAFLHFGLVT FVLFLNCFRT EGGDSGDVPS AGQNNESCSG SSECKEGVIL
     PIWYPENPSL GDKIARVIVY FVALIYMFLG VSIIADRFMA SIEVITSQER EVTIKKPNGE
     TSTTTIRVWN ETVSNLTLMA LGSSAPEILL SLIEVCGHGF IAGDLGPSTI VGSAAFNMFI
     IIGICVYVIP DGETRKIKHL RVFFVTAAWS IFAYIWLYMI LAVFSPGVVQ VWEGLLTLFF
     FPVCVLLAWV ADKRLLFYKY MHKKYRTDKH RGIIIETEGD HPKGIEMDGK MMNSHFLDGN
     FTPLEGKEVD ESRREMIRIL KDLKQKHPEK DLDQLVEMAN YYALSHQQKS RAFYRIQATR
     MMTGAGNILK KHAAEQAKKT SSMSEVHTDE PEDFASKVFF DPCSYQCLEN CGAVLLTVVR
     KGGDISKTMY VDYKTEDGSA NAGADYEFTE GTVVLKPGET QKEFSVGIID DDIFEEDEHF
     FVRLSNVRVE EEQLAEGMLP AILNSLPLPR AVLASPCVAT VTILDDDHAG IFTFECDTIH
     VSESIGVMEV KVLRTSGARG TVIVPFRTVE GTAKGGGEDF EDAYGELEFK NDETVKTIRV
     KIVDEEEYER QENFFIALGE PKWMERGISE VTDRKLTVEE EEAKRIAEMG KPVLGEHPKL
     EVIIEESYEF KSTVDKLIKK TNLALVVGTH SWRDQFMEAI TVSAGGDEDE DESGEERLPS
     CFDYVMHFLT VFWKVLFACV PPTEYCHGWA CFVVSILIIG MLTAIIGDLA SHFGCTIGLK
     DSVTAVVFVA FGTSVPDTFA SKAAALQDVY ADASIGNVTG SNAVNVFLGI GLAWSVAAIY
     WAMQGQEFHV SAGTLAFSVT LFTIFAFVCL SVLLYRRRPH LGGELGGPRG CKLATTWLFV
     SLWLLYILFA TLEAYCYIKG F
//
ID   CDKL5_MOUSE             Reviewed;         938 AA.
AC   Q3UTQ8; Q05BK3; Q8BWI8;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Cyclin-dependent kinase-like 5;
DE            EC=2.7.11.22;
GN   Name=Cdkl5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-788 (ISOFORM 2).
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Mediates phosphorylation of MECP2 (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts with MECP2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UTQ8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UTQ8-2; Sequence=VSP_022968, VSP_022969;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Autophosphorylated (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. CDC2/CDKX subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK052380; BAC34965.1; -; mRNA.
DR   EMBL; AK139220; BAE23922.1; -; mRNA.
DR   EMBL; BC042705; AAH42705.1; -; mRNA.
DR   IPI; IPI00381416; -.
DR   IPI; IPI00828430; -.
DR   UniGene; Mm.443717; -.
DR   HSSP; P24941; 2B55.
DR   ProteinModelPortal; Q3UTQ8; -.
DR   SMR; Q3UTQ8; 10-301.
DR   STRING; Q3UTQ8; -.
DR   PhosphoSite; Q3UTQ8; -.
DR   PRIDE; Q3UTQ8; -.
DR   Ensembl; ENSMUST00000087104; ENSMUSP00000084342; ENSMUSG00000031292.
DR   UCSC; uc009utr.1; mouse.
DR   MGI; MGI:1278336; Cdkl5.
DR   eggNOG; roNOG05798; -.
DR   GeneTree; ENSGT00600000084046; -.
DR   HOGENOM; HBG443739; -.
DR   HOVERGEN; HBG050863; -.
DR   InParanoid; Q3UTQ8; -.
DR   OMA; PVPRRVG; -.
DR   OrthoDB; EOG43R3M2; -.
DR   PhylomeDB; Q3UTQ8; -.
DR   BRENDA; 2.7.11.22; 244.
DR   ArrayExpress; Q3UTQ8; -.
DR   Bgee; Q3UTQ8; -.
DR   CleanEx; MM_CDKL5; -.
DR   Genevestigator; Q3UTQ8; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004693; F:cyclin-dependent protein kinase activity; IEA:EC.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    938       Cyclin-dependent kinase-like 5.
FT                                /FTId=PRO_0000275897.
FT   DOMAIN       13    297       Protein kinase.
FT   NP_BIND      19     27       ATP (By similarity).
FT   COMPBIAS    784    789       Poly-Lys.
FT   ACT_SITE    135    135       Proton acceptor (By similarity).
FT   BINDING      42     42       ATP (By similarity).
FT   MOD_RES     171    171       Phosphotyrosine (By similarity).
FT   MOD_RES     306    306       Phosphoserine (By similarity).
FT   MOD_RES     377    377       Phosphoserine (By similarity).
FT   MOD_RES     407    407       Phosphoserine (By similarity).
FT   MOD_RES     476    476       Phosphoserine (By similarity).
FT   MOD_RES     488    488       Phosphoserine (By similarity).
FT   MOD_RES     529    529       Phosphoserine (By similarity).
FT   MOD_RES     646    646       Phosphoserine (By similarity).
FT   MOD_RES     681    681       Phosphoserine (By similarity).
FT   MOD_RES     720    720       Phosphoserine (By similarity).
FT   MOD_RES     726    726       Phosphoserine (By similarity).
FT   MOD_RES     761    761       Phosphoserine (By similarity).
FT   VAR_SEQ       1    401       Missing (in isoform 2).
FT                                /FTId=VSP_022968.
FT   VAR_SEQ     402    410       IPHLLSPKE -> MPLIPASKK (in isoform 2).
FT                                /FTId=VSP_022969.
SQ   SEQUENCE   938 AA;  105489 MW;  3502580AF9A48DDD CRC64;
     MKIPNIGNVM NKFEILGVVG EGAYGVVLKC RHKETHEIVA IKKFKDSEEN EEVKETTLRE
     LKMLRTLKQE NIVELKEAFR RRGKLYLVFE YVEKNMLELL EEMPNGVPPE KVKSYIYQLI
     KAIHWCHKND IVHRDIKPEN LLISHNDVLK LCDFGFARNL SEGNNANYTE YVATRWYRSP
     ELLLGAPYGK SVDMWSVGCI LGELSDGQPL FPGESEIDQL FTIQKVLGPL PSEQMKLFYS
     NPRFHGLRFP AVNHPQSLER RYLGILNSVL LDLMKNLLKL DPADRYLTEQ CLNHPTFQTQ
     RLLDRSPSRS TKRKPYHVES STLSNRNQST KGAALQTHHR SNSKDIQNLS VGLPRAEEGL
     PANESFLNGN LAGATLSPMH TKTYQASTQP GSSSKDLTNN NIPHLLSPKE AKSKTEFDFN
     IDTKPSEGPG TKYLKSSTRS QQNRHSFMES SQSKAGTLQP SEKQSRHSYI DTIPQSSRSP
     SYRTKAKSHG ALSDSKSVSN LSEARAQITE TNTSRYFPSS CLDLNSPTSP TPTRHTDTRT
     LLSPSGRNNR NEGTLDSRRT TTRHSKTMEE LKLPEHMDSS HSHSLSAPHE SFSYGLGYTS
     PFSSQQRPHR HSMYVTRDKV RAKGLDGSLS IGQGMAARAN SLQLLSPQPG EQLPPEMTVA
     RPSVKESSRE GASSFHTRQK SEGGVYHDPH SDDGTAPKEN RHLYNDPVPR RVGSFYRVPS
     PRPDNSFHEN NVSTRVSSLP SDSSSGTNHS KRQPGFDPWK SPENISHADQ LKEKEKQGFF
     RSMKKKKKKT QTVPNTDGPD LLTLQKAIHS SSTASSRPKE WRPEKLSDLQ TQSQPLKSLR
     KLLHLSSSTN HPASSDPRFQ PLTAQQAKNS FSEIRIHPLS QATGGSSNIR QEPTPKGRPA
     LQLPGSSLLR YNGWKHSRSR SSQPDEVIFL ASHEKWKQ
//
ID   CG043_MOUSE             Reviewed;         580 AA.
AC   Q3UTZ3; Q8JZV2;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 38.
DE   RecName: Full=Uncharacterized protein C7orf43 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 138-580.
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH37034.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK138960; BAE23836.1; -; mRNA.
DR   EMBL; BC037034; AAH37034.1; ALT_INIT; mRNA.
DR   IPI; IPI00277271; -.
DR   RefSeq; NP_694801.2; NM_153161.3.
DR   UniGene; Mm.164493; -.
DR   PhosphoSite; Q3UTZ3; -.
DR   PRIDE; Q3UTZ3; -.
DR   Ensembl; ENSMUST00000048421; ENSMUSP00000046898; ENSMUSG00000036948.
DR   GeneID; 231807; -.
DR   KEGG; mmu:231807; -.
DR   UCSC; uc009aff.1; mouse.
DR   MGI; MGI:2385896; BC037034.
DR   eggNOG; roNOG15082; -.
DR   GeneTree; ENSGT00390000014725; -.
DR   HOGENOM; HBG446758; -.
DR   HOVERGEN; HBG081127; -.
DR   InParanoid; Q3UTZ3; -.
DR   OrthoDB; EOG4B2SX2; -.
DR   NextBio; 380765; -.
DR   ArrayExpress; Q3UTZ3; -.
DR   Bgee; Q3UTZ3; -.
DR   CleanEx; MM_BC037034; -.
DR   Genevestigator; Q3UTZ3; -.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    580       Uncharacterized protein C7orf43 homolog.
FT                                /FTId=PRO_0000280345.
FT   COMPBIAS     54    134       Gly-rich.
FT   MOD_RES     517    517       Phosphoserine.
FT   MOD_RES     541    541       Phosphothreonine (By similarity).
FT   MOD_RES     546    546       Phosphoserine (By similarity).
SQ   SEQUENCE   580 AA;  62780 MW;  A2150EF9236E59E9 CRC64;
     MESQCDYSMY FPAVPLPPRA ELTGDPGRYR ALPRRNHLYL GETVRFLLVL RCRGSVGAGV
     GGGAGLASRG AWTELATSLA ALASVSAGGA LPGCGSAGDQ DADPPGGGDP GGGGLFRGCS
     PLLTHGQGPA TSGGATTLPV EEPIVSTDEV IFPLTVSLDR LPPGTPKAKI VVTVWKREVE
     APEVRDQGYL RLLQTRSPGE TFRGEQSAFK AQVSTLLTLL PPPVLKCRQF TVAGKHLTVL
     KVLNSSSQEE ISIWDIRILP NFNASYLPVM PDGSVLLVDN VCHQSGEVSM GSFCRLPGTS
     GYFPCPLSAL EEHNFLFQLR GGEQPPPGAK EGLEVPLIAV VQWSTPKLPF TQSIYTHYRL
     PSVRLDRPCF VMTASCESPV RTYERFTVTY TLLNNLQDFL AVRLVWTPEH AQAGKQLCEE
     ERRAMQAALD SIVCHTPLNN LGFSRKGSAL TFSVAFQALR TGLFELSQHM KLKLQFTASV
     SHPPPEARPL SRKSSPSSPA VRDLVERHQA SLGRSQSFSH QQPSRSHLMR SGSVMERRAI
     TPPVASPVGR PLYLPPDKAV LSLDKIAKRE CKVLVVEPVK
//
ID   Q3UU61_MOUSE            Unreviewed;       337 AA.
AC   Q3UU61;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   11-JAN-2011, entry version 36.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=St3gal1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK138747; BAE23767.1; -; mRNA.
DR   IPI; IPI00108849; -.
DR   UniGene; Mm.248334; -.
DR   UniGene; Mm.461082; -.
DR   STRING; Q3UU61; -.
DR   Ensembl; ENSMUST00000092640; ENSMUSP00000090307; ENSMUSG00000013846.
DR   Ensembl; ENSMUST00000110074; ENSMUSP00000105701; ENSMUSG00000013846.
DR   MGI; MGI:98304; St3gal1.
DR   HOVERGEN; HBG054227; -.
DR   InParanoid; Q3UU61; -.
DR   ArrayExpress; Q3UU61; -.
DR   Bgee; Q3UU61; -.
DR   Genevestigator; Q3UU61; -.
DR   GO; GO:0030173; C:integral to Golgi membrane; IEA:InterPro.
DR   GO; GO:0008373; F:sialyltransferase activity; IEA:InterPro.
DR   GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR   InterPro; IPR001675; Glyco_trans_29.
DR   InterPro; IPR012163; Sialyl_trans.
DR   Pfam; PF00777; Glyco_transf_29; 1.
DR   PIRSF; PIRSF005557; Sialyl_trans; 1.
PE   2: Evidence at transcript level;
KW   Glycosyltransferase; Golgi apparatus; Membrane; Transferase;
KW   Transmembrane; Transmembrane helix.
SQ   SEQUENCE   337 AA;  39064 MW;  E65A41702EC4B245 CRC64;
     MRRKTLKYLT FFLLFIFLTS FVLNYSNTGV PSAWFPKQML LELSENFRRF IKSQPCTCRQ
     CISQDKVSYW FDQRFNKTMQ PLLTVHNALM EEDTYRWWLR LQRERKPNNL SDTVKELFRL
     VPGNVDPMLN KRLVGCRRCA VVGNSGNLKD SSYGPEIDSH DFVLRMNKAP TVGFEADVGS
     RTTHHLVYPE SFRELGENVN MVLVPFKTTD LQWVISATTT GTITHTYVPV PPKIKVKQEK
     ILIYHPAFIK YVFDNWLQGH GRYPSTGILS IIFSIHICDE VDLYGFGADS KGNWHHYWEN
     NPSAGAFRKT GVHDGDFEYN ITTTLAAINK IRIFKGR
//
ID   MRCKA_MOUSE             Reviewed;        1719 AA.
AC   Q3UU96; B2RY49; Q4V9U7; Q6ZQA9; Q8R495;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   08-FEB-2011, entry version 52.
DE   RecName: Full=Serine/threonine-protein kinase MRCK alpha;
DE            EC=2.7.11.1;
DE   AltName: Full=CDC42-binding protein kinase alpha;
GN   Name=Cdc42bpa; Synonyms=Kiaa0451;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1451-1719.
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-752 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 736-1006.
RA   Behrend E.N., Kemppainen R.J.;
RT   "MRCK-alpha interacts with Dexras1.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1376-1719.
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1532 AND SER-1638, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May act as a downstream effector of CDC42 in
CC       cytoskeletal reorganization. Contributes to the actomyosin
CC       contractility required for cell invasion, through the regulation
CC       of MYPT1 and thus MLC2 phosphorylation (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Maintained in an inactive, closed conformation
CC       by an interaction between the kinase domain and the negative
CC       autoregulatory C-terminal coiled-coil region. Agonist binding to
CC       the phorbol ester binding site disrupts this, releasing the kinase
CC       domain to allow N-terminus-mediated dimerization and kinase
CC       activation by transautophosphorylation (By similarity).
CC   -!- SUBUNIT: Homodimer and homotetramer via the coiled coil regions.
CC       Interacts tightly with GTP-bound but not GDP-bound CDC42 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=Displays a
CC       dispersed punctate distribution and concentrates along the cell
CC       periphery, especially at the leading edge and cell-cell junction.
CC       This concentration is PH-domain dependent (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UU96-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UU96-2; Sequence=VSP_023679, VSP_023680;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. DMPK subfamily.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 CNH domain.
CC   -!- SIMILARITY: Contains 1 CRIB domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AC125380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC132436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC096679; AAH96679.1; -; mRNA.
DR   EMBL; BC158095; AAI58096.1; -; mRNA.
DR   EMBL; AK138649; BAE23731.1; -; mRNA.
DR   EMBL; AF492452; AAM10976.1; -; mRNA.
DR   EMBL; AK129148; BAC97958.1; -; mRNA.
DR   IPI; IPI00605819; -.
DR   IPI; IPI00652736; -.
DR   UniGene; Mm.259655; -.
DR   HSSP; Q28021; 2F2U.
DR   ProteinModelPortal; Q3UU96; -.
DR   SMR; Q3UU96; 12-409, 999-1049, 1070-1192.
DR   STRING; Q3UU96; -.
DR   PhosphoSite; Q3UU96; -.
DR   PRIDE; Q3UU96; -.
DR   Ensembl; ENSMUST00000097450; ENSMUSP00000095059; ENSMUSG00000026490.
DR   Ensembl; ENSMUST00000097452; ENSMUSP00000095061; ENSMUSG00000026490.
DR   UCSC; uc007dvs.1; mouse.
DR   MGI; MGI:2441841; Cdc42bpa.
DR   GeneTree; ENSGT00600000084128; -.
DR   HOVERGEN; HBG055933; -.
DR   PhylomeDB; Q3UU96; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 378317; -.
DR   ArrayExpress; Q3UU96; -.
DR   Bgee; Q3UU96; -.
DR   CleanEx; MM_CDC42BPA; -.
DR   Genevestigator; Q3UU96; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005083; F:small GTPase regulator activity; IEA:InterPro.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR   GO; GO:0007097; P:nuclear migration; IMP:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR001180; Citron.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR014930; Myotonic_dystrophy_kinase_coil.
DR   InterPro; IPR000095; PAK_box_Rho-bd.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF08826; DMPK_coil; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   ProDom; PD011252; Myotonic_dystrophy_kinase_coil; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00285; PBD; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Coiled coil; Cytoplasm; Kinase;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1   1719       Serine/threonine-protein kinase MRCK
FT                                alpha.
FT                                /FTId=PRO_0000280455.
FT   DOMAIN       77    343       Protein kinase.
FT   DOMAIN      344    414       AGC-kinase C-terminal.
FT   DOMAIN     1069   1188       PH.
FT   DOMAIN     1214   1486       CNH.
FT   DOMAIN     1558   1571       CRIB.
FT   NP_BIND      83     91       ATP (By similarity).
FT   ZN_FING     999   1049       Phorbol-ester/DAG-type.
FT   COILED      437    670       Potential.
FT   COILED      713    820       Potential.
FT   COILED      880    943       Potential.
FT   COMPBIAS   1596   1711       Ser-rich.
FT   ACT_SITE    201    201       Proton acceptor (By similarity).
FT   BINDING     106    106       ATP (By similarity).
FT   MOD_RES     222    222       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     234    234       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     240    240       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES    1532   1532       Phosphoserine.
FT   MOD_RES    1638   1638       Phosphoserine.
FT   MOD_RES    1706   1706       Phosphoserine (By similarity).
FT   MOD_RES    1708   1708       Phosphoserine (By similarity).
FT   VAR_SEQ       1    104       Missing (in isoform 2).
FT                                /FTId=VSP_023679.
FT   VAR_SEQ     550    630       Missing (in isoform 2).
FT                                /FTId=VSP_023680.
FT   CONFLICT   1451   1453       VYS -> HEG (in Ref. 2; AAH96679).
FT   CONFLICT   1535   1535       V -> F (in Ref. 2; AAH96679).
FT   CONFLICT   1612   1612       G -> V (in Ref. 5; BAC97958).
SQ   SEQUENCE   1719 AA;  195536 MW;  362101C884240865 CRC64;
     MSGEVRLRQL EQFILDGPAQ TNGQCFSVET LLDILICLYD ECNNSPLRRE KNILEYLEWA
     KPFTSKVKQM RLHREDFEIL KVIGRGAFGE VAVVKLKNAD KVFAMKILNK WEMLKRAETA
     CFREERDVLV NGDSKWITTL HYAFQDDNNL YLVMDYYVGG DLLTLLSKFE DRLPEEMARF
     YLAEMVIAID SVHQLHYVHR DIKPDNILMD MNGHIRLADF GSCLKLMEDG TVQSSVAVGT
     PDYISPEILQ AMEDGKGRYG PECDWWSLGV CMYEMLYGET PFYAESLVET YGKIMNHKER
     FQFPAQVTDV SENAKDLIRR LICSREHRLG QNGIEDFKKH PFFSGIDWDN IRNCEAPYIP
     EVSSPTDTSN FDVDDDCLKN SETMPPPTHT AFSGHHLPFV GFTYTSSCVL SDRSCLRVTA
     GPTSLDLDVS VQRTLDNNLA TEAYERRIKR LEQEKLELTR KLQESTQTVQ ALQYSTVDGP
     LTASKDLEIK SLKEEIEKLR KQVAEVNHLE QQLEEANSVR RELDDAFRQI KASEKQIKTL
     QQEREELNKE LVQASERLKN QSKELKDAHC QRKLAMQEFM EINERLTELH TQKQKLARHV
     RDKEEEVDLV MQKAESLRQE LRRAERAKKE LEVHTEALIA EASKDKKLRE QSEHYSKQLE
     NELEGLKQKQ ISYSPGICSI EHQQEITKLK TDLEKKSIFY EEEISKREGI HASEIKNLKK
     ELHDSEGQQL ALNKEILVLK DKLEKTRRES QSEREEFENE FKQQYEREKV LLTEENKKLT
     SELDKLTSLY ESLSLRNQHL EEEVKDLADK KESVAHWEAQ ITEIIQWVSD EKDARGYLQA
     LASKMTEELE ALRNSSLGTR ATDMPWKMRR FAKLDMSARL ELQSALDAEI RAKQAIQEEL
     NKVKASNILT ECKLKDSEKK NLELLSEIEQ LIKDTEELRS EKGIEHQDSQ HSFLAFLNTP
     TDALDQFEIA DCAPLPAHTP TLRKKGCPAS TGFPPKRKTH QFFVKSFTAP TKCHQCTSLM
     VGLIRQGCSC EVCGFSCHIT CVNKAPTVCP VPPEQTKGPL GIDPQKGVGT AYEGHVRIPK
     PAGVKKGWQR ALAVVCDFKL FLYDIAEGKA SQPTSVISQV IDMRDEEFSV SSVLASDVIH
     ASRKDIPCIF RVTASQLSAP SNKCSILMLA DSENERSKWV GVLSELHKIL KKNKFRDRSV
     YVPKEAYDST LPLIKTTQAA AIIDHERIAL GNEEGLFVVH VTKDEIVRVG DNKKIHQIEL
     IPSDQLVAVI SGRNRHVRLF PMSALDGRET DFYKLAETKG CQTIAAGKVR HGALSCLCVA
     MKRQVLCYEL FQSKTRHRKF KEIQVPCNVQ WMAIFSEHLC VGFQSGFLRY PLNGEGGPCN
     MLHSNDHTLS FISHQPMDAL CAVEISNKEY LLCFNSIGIY TDCQGRRSRQ QELMWPANPS
     SCCYNAPYLS VYSENAVDIF DVNSMEWIQT LPLKKVRPLN TEGSLNLLGL ETIRLIYFKN
     KMAEGDELVV PETSDNSRKQ MVRNINNKRR YSFRVPEEER MQQRREMLRD PEMRNKLISN
     PTNFNHIAHM GPGDGIQILK DLPMNPRPQE SRTVFSGSVS IPSITKSRPE PGRSMSASSG
     LSARSSAQNG SALKREFSGG SYNTKRQPMP SPSEGSLSSG GMDQGSDAPA RDYDGEDSDS
     PRHSTASNSS NLSSPPSPIS PQKTKSLSLE STDRGSWDP
//
ID   Q3UUD2_MOUSE            Unreviewed;       288 AA.
AC   Q3UUD2;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 44.
DE   SubName: Full=MCG113144;
DE   SubName: Full=Putative uncharacterized protein;
DE   SubName: Full=Sprouty homolog 3 (Drosophila);
GN   Name=Spry3; ORFNames=mCG_113144;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [11]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC132135; AAI32136.1; -; mRNA.
DR   EMBL; BC132137; AAI32138.1; -; mRNA.
DR   EMBL; AK138539; BAE23695.1; -; mRNA.
DR   EMBL; CH466822; EDL07806.1; -; Genomic_DNA.
DR   IPI; IPI00346138; -.
DR   RefSeq; NP_001025464.1; NM_001030293.2.
DR   UniGene; Mm.297666; -.
DR   ProteinModelPortal; Q3UUD2; -.
DR   STRING; Q3UUD2; -.
DR   PRIDE; Q3UUD2; -.
DR   Ensembl; ENSMUST00000076951; ENSMUSP00000076219; ENSMUSG00000061654.
DR   GeneID; 236576; -.
DR   KEGG; mmu:236576; -.
DR   UCSC; uc009uyn.1; mouse.
DR   CTD; 236576; -.
DR   MGI; MGI:1345188; Spry3.
DR   eggNOG; roNOG07900; -.
DR   GeneTree; ENSGT00390000003535; -.
DR   HOGENOM; HBG444143; -.
DR   HOVERGEN; HBG003544; -.
DR   InParanoid; Q3UUD2; -.
DR   OMA; NQRCLCS; -.
DR   OrthoDB; EOG408N92; -.
DR   NextBio; 383014; -.
DR   ArrayExpress; Q3UUD2; -.
DR   Bgee; Q3UUD2; -.
DR   Genevestigator; Q3UUD2; -.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:InterPro.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR   InterPro; IPR007875; Sprouty.
DR   Pfam; PF05210; Sprouty; 1.
DR   PROSITE; PS51227; SPR; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   288 AA;  31363 MW;  19A3F311D5F8351E CRC64;
     MDATVIDELQ QILPIEQLRS THASNDYVER PPAPCKQALS SPSLIVQTHK SDWSLATMPT
     ALPRSISQCH QLQPLPQHLS QSSISSSMSQ STTASDQRLL ASITPSPSGQ SIIRTQPGAG
     AHPKVDGALK GEAEQSVGHS SDHLFICEEC GRCKCVPCTA VRPLPSCWMC NQRCLCSAES
     LLDYGTCLCC VKGLFYHCST DDEDNCADEP CSCGPSSCFI RWAAMSLISL FLPCLCCYLP
     TRGCLHMCQQ GYDSLRRPGC RCKRHTNTVC RKISSSSSPF PKAQEKSV
//
ID   Q3UUE0_MOUSE            Unreviewed;       409 AA.
AC   Q3UUE0;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Ahnak2; Synonyms=AI450948;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
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DR   EMBL; AK138503; BAE23687.1; -; mRNA.
DR   IPI; IPI00850843; -.
DR   UniGene; Mm.313169; -.
DR   UniGene; Mm.394208; -.
DR   ProteinModelPortal; Q3UUE0; -.
DR   PRIDE; Q3UUE0; -.
DR   Ensembl; ENSMUST00000124526; ENSMUSP00000114522; ENSMUSG00000072812.
DR   UCSC; uc007pff.1; mouse.
DR   MGI; MGI:2144831; Ahnak2.
DR   eggNOG; maNOG19274; -.
DR   GeneTree; ENSGT00530000063716; -.
DR   InParanoid; Q3UUE0; -.
DR   OMA; CFHVVLP; -.
DR   OrthoDB; EOG41G33J; -.
DR   ArrayExpress; Q3UUE0; -.
DR   Bgee; Q3UUE0; -.
DR   Genevestigator; Q3UUE0; -.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   1: Evidence at protein level;
FT   NON_TER     409    409
SQ   SEQUENCE   409 AA;  45922 MW;  4EA3ED50664B0A5B CRC64;
     MCDCFHVVLP TWPGAPGSVS GRQLQQREPE AETEDDSVTE GPAGEIIRPR PQGSSPVYEY
     TAEGAGFGGQ ENSQGRHSSS GRRRSWWKRG SGDSAAFTSM SHPEESTEVT LKTDVESGAS
     GYSVTGGGDQ GIFVKQVLKD SSAAKLFNLR EGDQLLSATI FFDHMKYEDA LKILQYSEPY
     KVQFRIKRKL SASKGEEGAV QHSQQGQENQ DKDIADGCME TPTKTLEEAG DRERLISKSR
     DGHHRRTQDR FSWPKFQTLR SKQRAGPRRS HSSSEASEHR ETRDMSPTST DTEVHRTADR
     QERNTGEGRR RRRFLNLRFG MTSGQSPDTS EQKGKDPKDR RGDAGALDGC PTQEDDTKDR
     EVAVEGQRKD KKETTGYMSE KTTQKNMREN YYSMEKDIPG KIDLKTDRH
//
ID   AN34B_MOUSE             Reviewed;         508 AA.
AC   Q3UUF8; Q4VA01; Q8BVH7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Ankyrin repeat domain-containing protein 34B;
DE   AltName: Full=Dendritic protein of 58 kDa;
GN   Name=Ankrd34b; Synonyms=Dp58;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, INDUCTION, AND PHOSPHORYLATION.
RX   PubMed=15358210; DOI=10.1016/j.bbrc.2004.06.106;
RA   Al-Shaibi N., Ghosh S.K.;
RT   "A novel phosphoprotein is induced during bone marrow commitment to
RT   dendritic cells.";
RL   Biochem. Biophys. Res. Commun. 321:26-30(2004).
RN   [4]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP   PHOSPHORYLATION.
RX   PubMed=17485271; DOI=10.2741/2284;
RA   Al-Shaibi N., King M.W., Duong T., Ghosh S.K.;
RT   "DP58, an inducible myeloid protein, is constitutively expressed in
RT   murine neuronal nuclei.";
RL   Front. Biosci. 12:2947-2956(2007).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- TISSUE SPECIFICITY: Specifically and constitutively expressed in
CC       brain (at protein level).
CC   -!- INDUCTION: Up-regulated in bone marrow upon differentiation (at
CC       protein level).
CC   -!- PTM: Phosphorylated.
CC   -!- SIMILARITY: Belongs to the ANKRD34 family.
CC   -!- SIMILARITY: Contains 4 ANK repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH96609.1; Type=Frameshift; Positions=199;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK078203; BAC37170.1; -; mRNA.
DR   EMBL; AK138465; BAE23669.1; -; mRNA.
DR   EMBL; BC096609; AAH96609.1; ALT_FRAME; mRNA.
DR   EMBL; BC119312; AAI19313.1; -; mRNA.
DR   EMBL; BC119314; AAI19315.1; -; mRNA.
DR   IPI; IPI00225874; -.
DR   RefSeq; NP_780664.2; NM_175455.4.
DR   UniGene; Mm.213623; -.
DR   ProteinModelPortal; Q3UUF8; -.
DR   SMR; Q3UUF8; 7-140.
DR   PRIDE; Q3UUF8; -.
DR   Ensembl; ENSMUST00000061594; ENSMUSP00000054330; ENSMUSG00000045034.
DR   GeneID; 218440; -.
DR   KEGG; mmu:218440; -.
DR   NMPDR; fig|10090.3.peg.28227; -.
DR   UCSC; uc007rkn.1; mouse.
DR   CTD; 218440; -.
DR   MGI; MGI:2443245; Ankrd34b.
DR   eggNOG; roNOG04431; -.
DR   GeneTree; ENSGT00390000012355; -.
DR   HOGENOM; HBG444529; -.
DR   HOVERGEN; HBG100441; -.
DR   InParanoid; Q3UUF8; -.
DR   OMA; VIIITTA; -.
DR   OrthoDB; EOG4VQ9P2; -.
DR   PhylomeDB; Q3UUF8; -.
DR   NextBio; 376284; -.
DR   ArrayExpress; Q3UUF8; -.
DR   Bgee; Q3UUF8; -.
DR   CleanEx; MM_ANKRD34B; -.
DR   Genevestigator; Q3UUF8; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 2.
DR   SMART; SM00248; ANK; 4.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
PE   1: Evidence at protein level;
KW   ANK repeat; Cytoplasm; Nucleus; Phosphoprotein; Repeat.
FT   CHAIN         1    508       Ankyrin repeat domain-containing protein
FT                                34B.
FT                                /FTId=PRO_0000319103.
FT   REPEAT        9     38       ANK 1.
FT   REPEAT       42     79       ANK 2.
FT   REPEAT       83    113       ANK 3.
FT   REPEAT      117    146       ANK 4.
FT   CONFLICT    401    401       S -> F (in Ref. 1; BAC37170).
SQ   SEQUENCE   508 AA;  55417 MW;  A8CC87D45E3F01BF CRC64;
     MDEGSEVSTD GNSLIKAVHQ SRLRLTRLLL EGGAYINESN DRGETPLMIA CKTKHVDQQS
     VGRAKMVKYL LENSADPNIQ DKSGKSALMH ACLERAGPEV VSLLLKSGAD LSLQDHSGYS
     ALVYAINAED RDTLKVLLSA CQAKGKEVII ITTAKSPSGR HTTQHHLNMP PADMDGSHPP
     ATPSEIDIKT ASLPLSYSSE TDLTLFGFKD KELCGGSDNT WDPDSPPRKP VIATNGPKLS
     QAPAWIKSTP SLKHQARVAS LQEELQDITP EEEIAYKTNA LALSKRFITR HQSIDVKDTA
     HLLRAFDQVN SRKMSYDEIN YHSLFPEGSQ TSVEIPTDRD PDSNQIFAST LKSIVQKRNS
     GANHYSSDSQ LAEGVTPPTV EDGKAAKKKI FAPSPSLLSG SKELVEPAPP GPLSRRNHAV
     LERRGSGAFP LDHSLAQSRP GFLPPLNVNP HPPITDIGVN NKICGLLSCG QKALMPTAPI
     FPKEFKTKKM LLRRQSLQTE QIKQLVNF
//
ID   TBC24_MOUSE             Reviewed;         561 AA.
AC   Q3UUG6; A5D6Q7; Q3TTZ8; Q3UH11; Q6ZPW4; Q8BH92; Q8BNF2; Q8C3C6;
AC   Q8C3W8;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=TBC1 domain family member 24;
GN   Name=Tbc1d24; Synonyms=Kiaa1171;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain, Head, Heart, Hypothalamus, Skin, Spinal cord, and
RC   Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=20727515; DOI=10.1016/j.ajhg.2010.07.020;
RA   Falace A., Filipello F., La Padula V., Vanni N., Madia F.,
RA   De Pietri Tonelli D., de Falco F.A., Striano P., Dagna Bricarelli F.,
RA   Minetti C., Benfenati F., Fassio A., Zara F.;
RT   "TBC1D24, an ARF6-interacting protein, is mutated in familial
RT   infantile myoclonic epilepsy.";
RL   Am. J. Hum. Genet. 87:365-370(2010).
CC   -!- FUNCTION: May act as a GTPase-activating protein for Rab family
CC       protein(s). Involved in neuronal projections development, probably
CC       through a negative modulation of ARF6 function.
CC   -!- SUBUNIT: Interacts with ARF6 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=Partially
CC       expressed at the plasma membrane (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UUG6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UUG6-2; Sequence=VSP_025702;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, particularly at the level
CC       of the cortex and the hippocampus.
CC   -!- SIMILARITY: Contains 1 Rab-GAP TBC domain.
CC   -!- SIMILARITY: Contains 1 TLD domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC39035.1; Type=Frameshift; Positions=113;
CC       Sequence=BAC98114.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK129304; BAC98114.1; ALT_INIT; mRNA.
DR   EMBL; AK049306; BAC33671.1; -; mRNA.
DR   EMBL; AK049754; BAC33904.1; -; mRNA.
DR   EMBL; AK083833; BAC39035.1; ALT_FRAME; mRNA.
DR   EMBL; AK084693; BAC39255.1; -; mRNA.
DR   EMBL; AK086293; BAC39644.1; -; mRNA.
DR   EMBL; AK138431; BAE23659.1; -; mRNA.
DR   EMBL; AK147647; BAE28046.1; -; mRNA.
DR   EMBL; AK161054; BAE36174.1; -; mRNA.
DR   EMBL; BC080845; AAH80845.1; -; mRNA.
DR   EMBL; BC094417; AAH94417.1; -; mRNA.
DR   IPI; IPI00453827; -.
DR   IPI; IPI00761259; -.
DR   RefSeq; NP_001157319.1; NM_001163847.1.
DR   RefSeq; NP_001157320.1; NM_001163848.1.
DR   RefSeq; NP_001157321.1; NM_001163849.1.
DR   RefSeq; NP_001157322.1; NM_001163850.1.
DR   RefSeq; NP_001157323.1; NM_001163851.1.
DR   RefSeq; NP_001157324.1; NM_001163852.1.
DR   RefSeq; NP_001157325.1; NM_001163853.1.
DR   RefSeq; NP_775278.3; NM_173186.4.
DR   UniGene; Mm.301585; -.
DR   ProteinModelPortal; Q3UUG6; -.
DR   STRING; Q3UUG6; -.
DR   PhosphoSite; Q3UUG6; -.
DR   PRIDE; Q3UUG6; -.
DR   Ensembl; ENSMUST00000040474; ENSMUSP00000036458; ENSMUSG00000036473.
DR   Ensembl; ENSMUST00000097376; ENSMUSP00000094989; ENSMUSG00000036473.
DR   GeneID; 224617; -.
DR   KEGG; mmu:224617; -.
DR   UCSC; uc008auq.1; mouse.
DR   CTD; 224617; -.
DR   MGI; MGI:2443456; Tbc1d24.
DR   GeneTree; ENSGT00410000025739; -.
DR   HOVERGEN; HBG068667; -.
DR   InParanoid; Q3UUG6; -.
DR   OMA; GHCDTFN; -.
DR   OrthoDB; EOG43BMNK; -.
DR   NextBio; 377251; -.
DR   ArrayExpress; Q3UUG6; -.
DR   Bgee; Q3UUG6; -.
DR   CleanEx; MM_TBC1D24; -.
DR   Genevestigator; Q3UUG6; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005097; F:Rab GTPase activator activity; IEA:InterPro.
DR   GO; GO:0032313; P:regulation of Rab GTPase activity; IEA:InterPro.
DR   InterPro; IPR000195; RabGAP/TBC_dom.
DR   InterPro; IPR006571; TLDc.
DR   Pfam; PF00566; TBC; 1.
DR   SMART; SM00164; TBC; 1.
DR   SMART; SM00584; TLDc; 1.
DR   SUPFAM; SSF47923; RabGAP_TBC; 1.
DR   PROSITE; PS50086; TBC_RABGAP; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Cytoplasm; GTPase activation.
FT   CHAIN         1    561       TBC1 domain family member 24.
FT                                /FTId=PRO_0000288505.
FT   DOMAIN       45    236       Rab-GAP TBC.
FT   DOMAIN      368    556       TLD.
FT   MOD_RES     288    288       N6-acetyllysine (By similarity).
FT   MOD_RES     314    314       N6-acetyllysine (By similarity).
FT   MOD_RES     319    319       N6-acetyllysine (By similarity).
FT   VAR_SEQ     322    327       Missing (in isoform 2).
FT                                /FTId=VSP_025702.
FT   CONFLICT      3      3       P -> H (in Ref. 2; BAE23659).
FT   CONFLICT     14     14       K -> R (in Ref. 2; BAE36174).
FT   CONFLICT    266    266       K -> E (in Ref. 2; BAC39644).
FT   CONFLICT    308    308       E -> G (in Ref. 2; BAC39255).
FT   CONFLICT    471    471       S -> G (in Ref. 1; BAC98114).
FT   CONFLICT    505    505       N -> I (in Ref. 2; BAE28046).
SQ   SEQUENCE   561 AA;  63236 MW;  1C35837B82FF093E CRC64;
     MDPPGYNCFV DKDKMDASIQ DLGPKELNCT ELQELKQLAR QGYWAQSHTL RGKVYQRLIR
     DIPCRTVTPD ASVYSDIVGK IVGKHSSSSL PLPEFVDNTQ VPTYCLNTRG EGAVRKILLC
     IANQFPDISF CPALPAVVAL LLHYSIDEAE CFEKACRILS CNDPTKKLID QSFLAFESSC
     MTFGDLVNKY CQAAHKLMVA VSEDVLQVYS DWQRWLFGEL PLNYFARVFD VFLVEGYKVL
     YRVALAILKF FHKVRAGQPL ESDNVKQDIR MFVKDIAKTV SPEKLLEKAF AIRLFSRKEI
     QLLQMANEKA LRQKGITVKQ KSVSLSKRQF VHLAVHAENF HSEIVSVKEM RDIWSWIPER
     FALCQPLLLF SSLQHGYSLS RFYFQCEGHE PTLLLIKTTQ KEVCGAYLST DWSERTKFGG
     KLGFFGTGEC FVFRLQPEVQ RYEWVVIKHP ELTKATSLKS SEAAGSSSLI SHCSSDPADR
     LSPFLAARHF NLPSKTESMF MAGGNDCLII GGGGGQALYV DGDLNRGRTG HCDTFNNQPL
     CSENFLIAAV EAWGFQDPDT E
//
ID   STRAA_MOUSE             Reviewed;         431 AA.
AC   Q3UUJ4; Q6VEU7; Q9D0G8;
DT   14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=STE20-related kinase adapter protein alpha;
DE            Short=STRAD alpha;
DE   AltName: Full=STE20-related adapter protein;
GN   Name=Strada; Synonyms=Lyk5, Strad;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J;
RA   Zhou G., Wang J., Zhang Y.;
RT   "Cloning of mouse protein kinase LYK5.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: In complex with CAB39, binds to and activates STK11.
CC       Relocates STK11 from the nucleus to the cytoplasm. Plays an
CC       essential role in STK11-mediated G1 cell cycle arrest (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3UUJ4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UUJ4-2; Sequence=VSP_052217, VSP_052218;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q3UUJ4-3; Sequence=VSP_052217;
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY341872; AAQ24157.1; -; mRNA.
DR   EMBL; AY341878; AAQ24162.1; -; mRNA.
DR   EMBL; AK011451; BAB27626.1; -; mRNA.
DR   EMBL; AK138358; BAE23631.1; -; mRNA.
DR   EMBL; BC058517; AAH58517.1; -; mRNA.
DR   IPI; IPI00649437; -.
DR   IPI; IPI00649998; -.
DR   IPI; IPI00807906; -.
DR   RefSeq; NP_082402.1; NM_028126.2.
DR   UniGene; Mm.403722; -.
DR   ProteinModelPortal; Q3UUJ4; -.
DR   SMR; Q3UUJ4; 60-431.
DR   PhosphoSite; Q3UUJ4; -.
DR   PRIDE; Q3UUJ4; -.
DR   Ensembl; ENSMUST00000007444; ENSMUSP00000007444; ENSMUSG00000069631.
DR   Ensembl; ENSMUST00000103072; ENSMUSP00000099361; ENSMUSG00000069631.
DR   Ensembl; ENSMUST00000106871; ENSMUSP00000102484; ENSMUSG00000069631.
DR   GeneID; 72149; -.
DR   KEGG; mmu:72149; -.
DR   UCSC; uc007lyf.1; mouse.
DR   UCSC; uc007lyg.1; mouse.
DR   CTD; 72149; -.
DR   MGI; MGI:1919399; Strada.
DR   GeneTree; ENSGT00580000081442; -.
DR   HOGENOM; HBG715330; -.
DR   HOVERGEN; HBG055069; -.
DR   InParanoid; Q3UUJ4; -.
DR   OMA; NGTVPCL; -.
DR   OrthoDB; EOG4WSW9P; -.
DR   NextBio; 335570; -.
DR   ArrayExpress; Q3UUJ4; -.
DR   Bgee; Q3UUJ4; -.
DR   CleanEx; MM_2610019A05RIK; -.
DR   Genevestigator; Q3UUJ4; -.
DR   GermOnline; ENSMUSG00000069631; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0032147; P:activation of protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006611; P:protein export from nucleus; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell cycle; Cytoplasm; Nucleus; Phosphoprotein.
FT   CHAIN         1    431       STE20-related kinase adapter protein
FT                                alpha.
FT                                /FTId=PRO_0000260037.
FT   DOMAIN       69    379       Protein kinase.
FT   MOD_RES      46     46       Phosphoserine (By similarity).
FT   MOD_RES     419    419       Phosphothreonine; by STK11 (By
FT                                similarity).
FT   VAR_SEQ       5     41       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_052217.
FT   VAR_SEQ     370    381       Missing (in isoform 2).
FT                                /FTId=VSP_052218.
SQ   SEQUENCE   431 AA;  48236 MW;  6E4B14CC9B2B1D7D CRC64;
     MSFLVSKPER IRRWVSEKFI VEGLRDLELF GEQPPGDTRR KANEASSESI ASFSKPEMMS
     SFLPEGGCYE LLTIIGKGFE DLMTVNLARY KPTGEYVTVR RINLEACSNE MVTFLQGELH
     VSKLFSHPNI VPYRATFIAD NELWVVTSFM AYGSAKDLIG THFMDGMNEL AIAYILQGVL
     KALDYIHHMG YVHRSVKASH ILISTDGKVY LSGLRSNLSM ISHGQRQRAV HDFPKYSIKV
     LPWLSPEVLQ QNLQGYDAKS DIYSVGITAC ELANGHVPFK DMPATQMLLE KLNGTVPCLL
     DTSTIPAEEL TMSPSRSIAN PGLNDSLAAG SLRPSNGDSP SHPYHRTFSP HFHNFVEQCL
     QRNPDARPNA STLLNHSFFK QIKRRASEAL PELLRPVTPI TNFEGSQSQD HSGIFGLVTN
     LEDLEVDDWE F
//
ID   Q3UUK5_MOUSE            Unreviewed;      1042 AA.
AC   Q3UUK5;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 40.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Ppp1r9a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
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DR   EMBL; AK138313; BAE23620.1; -; mRNA.
DR   IPI; IPI00336313; -.
DR   UniGene; Mm.332901; -.
DR   STRING; Q3UUK5; -.
DR   Ensembl; ENSMUST00000035813; ENSMUSP00000046906; ENSMUSG00000032827.
DR   MGI; MGI:2442401; Ppp1r9a.
DR   eggNOG; roNOG13918; -.
DR   HOVERGEN; HBG005213; -.
DR   InParanoid; Q3UUK5; -.
DR   OrthoDB; EOG4S4PFV; -.
DR   ArrayExpress; Q3UUK5; -.
DR   Bgee; Q3UUK5; -.
DR   Genevestigator; Q3UUK5; -.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; IDA:MGI.
DR   GO; GO:0043197; C:dendritic spine; IDA:MGI.
DR   GO; GO:0030175; C:filopodium; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007015; P:actin filament organization; IPI:MGI.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR011510; SAM_2.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   2: Evidence at transcript level;
FT   NON_TER    1042   1042
SQ   SEQUENCE   1042 AA;  116497 MW;  4BEF90A169372141 CRC64;
     MLKAESSGER TTLRSASPHR NAYRTEFQAL KSTFDKPKSD GEQKTKEGEG SQQSRGRKYG
     SNVNRIKNLF MQMGMEPSEN AAIIAKTRGK GRPSSPQRRM KPKEFVEKTD GSVVKLESSV
     SERISRFDTM HDGPSYAKFT ETRKMFERSV HESGQNHRYS PKKEKGGGTE PQDEWGGSKS
     NRGSSDSLDS LSPRTEAVSP TVSQLSAVFE NSEPPGALTS GKAESADYSV TGHYPLNLPS
     VTVTNLDTFG RLKDSNSKPP SNKQDTDTED AQKSDAVPVP EVAQKGTSLA SLPSEESQLS
     TEAEDVTTAQ PEALDSTDKD SPEEPSAENQ AMPKSHILSP RNEPLEDAEA NVVGSERAQH
     QKKDLTGGDL TSPDASASSC GREVPEDSNS FESSHVYMHS DYNVYRVRSR YNSDWGETGT
     EQDEEEDSDE NNYYQPDMEY SEIVGLPEEE EIPANRKIKF SCAPIKVFNT YSNEDYDRRN
     DDVDPVAASA EYELEKRVEK LELFPVELEK DEDGLGISII GMGVGADAGL EKLGIFVKTV
     TDGGAAQRDG RIQVNDQIVE VDGISLVGVT QNFAATVLRN TKGNVRFVIG REKPGQVSEV
     AQLISQTLEQ ERRQRELLER HYAQYDADDD ETGEYATDEE EDEGGPILPS GDVAIEVFEL
     PENEDMFSPS DLDTSKLSHK FKELQIKHAV TEAEIQKLKT KLQAAENEKV RWELEKNQLQ
     QNIEENKERM LKLESYWIEA QTLCHTVNEH LKETQSQYQA LEKKYNKAKK LIKDFQQKEL
     DFIKRQEVER KKREEVEKAH LLEVQGLQVR IRDLEAEVFR LLKQNGTQVN NNNNIFERRP
     SPGEVSKGDT MENVEVKQTS CQDGLSQDLN EAVPETERLD SKALKTRAQL SVKNRRQRPT
     RTRLYDSVSS TDGEDSLERK NFTFNDDFSP SSTSSADLSG LGAEPKTPGL SQSLALSSDE
     SLDMIDDEIL DDGQSPKHTQ SQNRAVHEWS VQQVSRWLMS LSLDQYVPEF SAQSISGEQL
     LQLDGNKLKA LGMTSSQDRA LV
//
ID   Q3UUN5_MOUSE            Unreviewed;       407 AA.
AC   Q3UUN5;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   11-JAN-2011, entry version 44.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Pten;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK138234; BAE23590.1; -; mRNA.
DR   IPI; IPI00652977; -.
DR   UniGene; Mm.245395; -.
DR   UniGene; Mm.444861; -.
DR   ProteinModelPortal; Q3UUN5; -.
DR   SMR; Q3UUN5; 59-355.
DR   STRING; Q3UUN5; -.
DR   PRIDE; Q3UUN5; -.
DR   HOVERGEN; HBG000239; -.
DR   Genevestigator; Q3UUN5; -.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030165; F:PDZ domain binding; IEA:InterPro.
DR   GO; GO:0016314; F:phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity; IEA:InterPro.
DR   GO; GO:0051800; F:phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity; IEA:InterPro.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR   GO; GO:0030336; P:negative regulation of cell migration; IEA:InterPro.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IEA:InterPro.
DR   GO; GO:0051895; P:negative regulation of focal adhesion assembly; IEA:InterPro.
DR   GO; GO:0051898; P:negative regulation of protein kinase B signaling cascade; IEA:InterPro.
DR   GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   GO; GO:0031647; P:regulation of protein stability; IEA:InterPro.
DR   InterPro; IPR017361; Bifunc_PIno_P3_Pase/Pase_PTEN.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR014019; Phosphatase_tensin-typ.
DR   InterPro; IPR014020; Tensin_phosphatase_C2-dom.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   Pfam; PF00782; DSPc; 1.
DR   Pfam; PF10409; PTEN_C2; 1.
DR   PIRSF; PIRSF038025; PTEN; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   PROSITE; PS51182; C2_TENSIN; 1.
DR   PROSITE; PS51181; PPASE_TENSIN; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PE   1: Evidence at protein level;
SQ   SEQUENCE   407 AA;  46893 MW;  CFFA22CA270BB80E CRC64;
     MLNGAGLDQA FKMSLPRRAR IGASVGPVRS SAGYKKAEDE MSRATSVGDQ LEAPARIIYL
     NQSHLNKFCD NRIRCAERHY DTAKFNCRVA QYPFEDHNPP QLELIKPFCE DLDQWLSEDD
     NHVAAIHCKA GKGRTGVMIC AYLLHRGKFL KAQEALDFYG EVRTRDKKGV TIPSQRRYVY
     YYSYLLKNHL DYRPVALLFH KMMFETIPMF SGGTCNPQFV VCQLKVKIYS SNSGPTRRED
     KFMYFEFPQP LPVCGDIKVE FFHKQNKMLK KDKMFHFWVN TFFIPGPEET SEKVENGSLC
     DQEIDSICSI ERADNDKEYL VLTLTKNDLD KANKDKANRY FSPNFKVKLY FTKTVEEPSN
     PEASSSTSVT PDVSDNEPDH YRYSDTTDSD PENEPFDEDQ HSQITKV
//
ID   K22O_MOUSE              Reviewed;         594 AA.
AC   Q3UV17;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Keratin, type II cytoskeletal 2 oral;
DE   AltName: Full=Keratin-76;
DE            Short=K76;
DE   AltName: Full=Type-II keratin Kb9;
GN   Name=Krt76;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Probably contributes to terminal cornification (By
CC       similarity).
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC   -!- MISCELLANEOUS: There are two types of cytoskeletal and
CC       microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to
CC       basic; 56-70 kDa).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK137676; BAE23456.1; -; mRNA.
DR   IPI; IPI00346834; -.
DR   RefSeq; NP_001028349.1; NM_001033177.2.
DR   UniGene; Mm.195788; -.
DR   ProteinModelPortal; Q3UV17; -.
DR   SMR; Q3UV17; 163-200, 209-316, 333-478.
DR   PhosphoSite; Q3UV17; -.
DR   PRIDE; Q3UV17; -.
DR   Ensembl; ENSMUST00000100179; ENSMUSP00000097754; ENSMUSG00000075402.
DR   GeneID; 77055; -.
DR   KEGG; mmu:77055; -.
DR   UCSC; uc007xue.1; mouse.
DR   CTD; 77055; -.
DR   MGI; MGI:1924305; Krt76.
DR   eggNOG; maNOG07683; -.
DR   GeneTree; ENSGT00560000076943; -.
DR   HOGENOM; HBG715391; -.
DR   HOVERGEN; HBG013015; -.
DR   InParanoid; Q3UV17; -.
DR   OMA; RDSSEGY; -.
DR   OrthoDB; EOG40ZQXX; -.
DR   NextBio; 346392; -.
DR   ArrayExpress; Q3UV17; -.
DR   Bgee; Q3UV17; -.
DR   Genevestigator; Q3UV17; -.
DR   GO; GO:0045095; C:keratin filament; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR016044; F.
DR   InterPro; IPR001664; IF.
DR   InterPro; IPR018039; Intermediate_filament_CS.
DR   InterPro; IPR003054; Keratin_II.
DR   PANTHER; PTHR23239; IF; 1.
DR   PANTHER; PTHR23239:SF18; Keratin_II; 1.
DR   Pfam; PF00038; Filament; 1.
DR   PRINTS; PR01276; TYPE2KERATIN.
DR   PROSITE; PS00226; IF; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Intermediate filament; Keratin.
FT   CHAIN         1    594       Keratin, type II cytoskeletal 2 oral.
FT                                /FTId=PRO_0000361693.
FT   REGION        1    164       Head.
FT   REGION      165    476       Rod.
FT   REGION      165    200       Coil 1A.
FT   REGION      201    221       Linker 1.
FT   REGION      222    313       Coil 1B.
FT   REGION      314    337       Linker 12.
FT   REGION      338    476       Coil 2.
FT   REGION      477    594       Tail.
FT   COMPBIAS     37    136       Gly-rich.
FT   COMPBIAS    489    593       Ser-rich.
SQ   SEQUENCE   594 AA;  62845 MW;  00998F2B496DF612 CRC64;
     MSRQACKKSF SCGSQGFSGH SAVVSGSSRS SCVARSGAAS GGACGFRSGA GSLGSHSLYS
     LGGSKSISIS VAAGGSRAGG FSGGRSSCGS GFGSGYGGSL GGSRGMGAGF GGPSGFGGAG
     GFGRPGSFGP GSCPGGIQEV TINQSLLQPL NVEIDPQIGQ VKAQEREQIK TLNNKFASFI
     DKVRFLEQQN KVLETKWELL QQQTIRSGSG PQNLEPFFES YISCLRKQLD SLLGAKGSLE
     GELKSMQDLV EDFKKKYEEE INRRTAAENE FVGLKKDVDG AFMNKVELQA KVDSLTDEIN
     FLRTLYDMEL SQIQSHVSDT SVVLSMDNNR CLDLDSIIAE VKAQYEDIAQ KSKAEAEALY
     QTKLGELQTT AGRHGDDLRS TKSEIMDLNR MIQRLRAEIE NVKKQNTNMQ TSIAEAEQRG
     ERALKDADTK FQDLQVALQK AKEDMARLLK EYQELMNVKL ALDVEIATYR KLLEGEECRL
     SGEFQNAVSI SVVSNVTSTS SSGSFRGTGG SNYGGDSSGR SGGSSSSSSR GSSSRGSSGS
     RLGSGGSISV SQQRMGFNSG GSQTSVGSSY KSGRGGSSSV QFSQTTSSSQ QRSK
//
ID   TMTC1_MOUSE             Reviewed;         942 AA.
AC   Q3UV71; Q8BQV5;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Transmembrane and TPR repeat-containing protein 1;
GN   Name=Tmtc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Bone, and Corpora quadrigemina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UV71-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UV71-2; Sequence=VSP_023618;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the TMTC family.
CC   -!- SIMILARITY: Contains 10 TPR repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC32703.1; Type=Frameshift; Positions=294;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK046396; BAC32703.1; ALT_FRAME; mRNA.
DR   EMBL; AK137545; BAE23402.1; -; mRNA.
DR   IPI; IPI00224050; -.
DR   IPI; IPI00653264; -.
DR   RefSeq; NP_945318.2; NM_198967.5.
DR   UniGene; Mm.137858; -.
DR   ProteinModelPortal; Q3UV71; -.
DR   SMR; Q3UV71; 518-938.
DR   STRING; Q3UV71; -.
DR   PhosphoSite; Q3UV71; -.
DR   PRIDE; Q3UV71; -.
DR   Ensembl; ENSMUST00000060095; ENSMUSP00000056353; ENSMUSG00000030306.
DR   Ensembl; ENSMUST00000100772; ENSMUSP00000098335; ENSMUSG00000030306.
DR   GeneID; 387314; -.
DR   KEGG; mmu:387314; -.
DR   UCSC; uc009etj.1; mouse.
DR   CTD; 387314; -.
DR   MGI; MGI:3039590; Tmtc1.
DR   eggNOG; roNOG09392; -.
DR   GeneTree; ENSGT00550000074327; -.
DR   HOGENOM; HBG388379; -.
DR   HOVERGEN; HBG106148; -.
DR   InParanoid; Q3UV71; -.
DR   OrthoDB; EOG41C6VN; -.
DR   NextBio; 405818; -.
DR   ArrayExpress; Q3UV71; -.
DR   Bgee; Q3UV71; -.
DR   Genevestigator; Q3UV71; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR013618; DUF1736.
DR   InterPro; IPR001440; TPR-1.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR013105; TPR_2.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 3.
DR   Pfam; PF08409; DUF1736; 1.
DR   Pfam; PF00515; TPR_1; 1.
DR   Pfam; PF07719; TPR_2; 2.
DR   SMART; SM00028; TPR; 10.
DR   PROSITE; PS50005; TPR; 10.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Membrane; Repeat; TPR repeat; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    942       Transmembrane and TPR repeat-containing
FT                                protein 1.
FT                                /FTId=PRO_0000280289.
FT   TRANSMEM     21     41       Helical; (Potential).
FT   TRANSMEM    110    130       Helical; (Potential).
FT   TRANSMEM    142    159       Helical; (Potential).
FT   TRANSMEM    160    180       Helical; (Potential).
FT   TRANSMEM    197    217       Helical; (Potential).
FT   TRANSMEM    332    352       Helical; (Potential).
FT   TRANSMEM    374    394       Helical; (Potential).
FT   TRANSMEM    415    435       Helical; (Potential).
FT   TRANSMEM    442    462       Helical; (Potential).
FT   TRANSMEM    464    484       Helical; (Potential).
FT   TRANSMEM    499    519       Helical; (Potential).
FT   REPEAT      543    576       TPR 1.
FT   REPEAT      577    607       TPR 2.
FT   REPEAT      608    641       TPR 3.
FT   REPEAT      642    675       TPR 4.
FT   REPEAT      676    709       TPR 5.
FT   REPEAT      710    742       TPR 6.
FT   REPEAT      743    776       TPR 7.
FT   REPEAT      811    844       TPR 8.
FT   REPEAT      849    882       TPR 9.
FT   REPEAT      883    916       TPR 10.
FT   VAR_SEQ     534    571       Missing (in isoform 2).
FT                                /FTId=VSP_023618.
FT   CONFLICT    171    171       A -> P (in Ref. 1; BAC32703).
FT   CONFLICT    300    300       T -> P (in Ref. 1; BAC32703).
SQ   SEQUENCE   942 AA;  105815 MW;  182BEAB355566DF9 CRC64;
     MLVTRGDRGG GERAPSRRPR CGLVPAGAAA LLAGASCLCY GRSLRGEFVH DDVWAIVNNP
     DVRPGTPLRW AIFANDFWGK GLADSTSHKS YRPLCVLSFR LNIFLTGMNP FYFHAVNVIL
     HCLVTLVLMY TCDKTVFKNR GLAFVTALLF AVHPVHTEAV AGIVGRADVL ACLLFLLAFL
     SYQRSLDQGC AGQCFPTTAS PFFLLLSLFL GTCAMLVKET GITVFGVCLV YDLFSPSHKQ
     DKLSNGAVCQ HSSGQPGSPQ PSSQQAHPHR ESRKQRFPHK DSWGGCHSPL PPEPKSSGFT
     MSPRAMWSLM RCLTGSTNRN FLLTLRPFLK RAILVISYVT VILYFRLWIM GGTMPLFSEQ
     DNPASFSPYI LTRFLTYSYL LAFNVWLLLA PITLCYDWQV GSIPLVETIW DVRNLATILL
     AVVMALLSLH CVAAFKRLEH KEVLAGLLFL VFPFIPASNL FFRVGFVVAE RVLYMPSMGY
     CILFVHGLSK LCAGLSRCGA TSLMASTVLL LLLFSWKTVK QNEIWLSRES LFRSGVQTLP
     HNAKVHYNYA NFLKDQGRNK EAIYHYRTAL KLYPRHASAL NNLGTLTKDM AEAKMYYQKA
     LQLHPQHNRA LFNLGNLLKS QEKTEEAIML LKESIKYGPD FADAYSSLAS LLAEQERFKE
     AEDIYQAGIK NCPDSSDLHN NYAVFLVDSG FPEKAVAHYQ QAIQLSPSHH VAVVNLGRLY
     RSLGENSKAE EWYRRALKVA RTAEVLSPLG ALYYNTGRHK EALEVYREAV SLQPSQRELR
     LALAQVLAVM GQTKEAEKIT SHIVSEEPRC LECYRLLSAI HSKQEHHGKA LEAIEKALQL
     KPKDPKVISE LFFTKGNQLR EQNLLDKAFE SYEAAVTLDP DQAQAWMNMG GIRHIQGSYV
     SARAYYERAL KLVPDSKLLK ENLAKLDRLE RRLQEVRERD QT
//
ID   KSR2_MOUSE              Reviewed;         959 AA.
AC   Q3UVC0;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 47.
DE   RecName: Full=Kinase suppressor of Ras 2;
GN   Name=Ksr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-330.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Location-regulated scaffold connecting MEK to RAF.
CC       Blocks MAP3K8 kinase activity and MAP3K8-mediated signaling. Acts
CC       as a negative regulator of MAP3K3-mediated activation of ERK, JNK
CC       and NF-kappa-B pathways, inhibiting MAP3K3-mediated interleukin-8
CC       production (By similarity).
CC   -!- SUBUNIT: Interacts with MAP2K1, MAP3K8, MAPK, RAS and RAF (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane;
CC       Peripheral membrane protein (By similarity).
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
CC   -!- PTM: Phosphorylated on Ser-484 by MARK3 (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family.
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AC113299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC113303; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC114617; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK137433; BAE23350.1; -; mRNA.
DR   IPI; IPI00750597; -.
DR   RefSeq; NP_001030045.1; NM_001034873.2.
DR   UniGene; Mm.437947; -.
DR   ProteinModelPortal; Q3UVC0; -.
DR   SMR; Q3UVC0; 667-943.
DR   PhosphoSite; Q3UVC0; -.
DR   PRIDE; Q3UVC0; -.
DR   Ensembl; ENSMUST00000111949; ENSMUSP00000107580; ENSMUSG00000061578.
DR   GeneID; 333050; -.
DR   KEGG; mmu:333050; -.
DR   UCSC; uc008zfu.1; mouse.
DR   CTD; 333050; -.
DR   MGI; MGI:3610315; Ksr2.
DR   eggNOG; roNOG06517; -.
DR   GeneTree; ENSGT00600000084040; -.
DR   HOVERGEN; HBG052293; -.
DR   InParanoid; Q3UVC0; -.
DR   OrthoDB; EOG43JC41; -.
DR   CleanEx; MM_KSR2; -.
DR   Genevestigator; Q3UVC0; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   SMART; SM00109; C1; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Membrane; Metal-binding; Phosphoprotein; Zinc; Zinc-finger.
FT   CHAIN         1    959       Kinase suppressor of Ras 2.
FT                                /FTId=PRO_0000286965.
FT   DOMAIN      676    941       Protein kinase.
FT   ZN_FING     413    457       Phorbol-ester/DAG-type.
FT   COMPBIAS    171    294       Pro-rich.
FT   COMPBIAS    520    563       Pro-rich.
FT   METAL       414    414       Zinc 1 (By similarity).
FT   METAL       426    426       Zinc 2 (By similarity).
FT   METAL       429    429       Zinc 2 (By similarity).
FT   METAL       439    439       Zinc 1 (By similarity).
FT   METAL       442    442       Zinc 1 (By similarity).
FT   METAL       447    447       Zinc 2 (By similarity).
FT   METAL       450    450       Zinc 2 (By similarity).
FT   METAL       457    457       Zinc 1 (By similarity).
FT   MOD_RES     484    484       Phosphoserine; by MARK3 (By similarity).
SQ   SEQUENCE   959 AA;  108572 MW;  5A56146F4C6E8AA2 CRC64;
     MDEENMTKSE EQQPLSLQKA LQQCELVQNM IDLSISNLEG LRTKCAASND LTQKEIRTLE
     SKLVKYFSRQ LSCKKKVALQ ERNAELDGFP QLRHWFRIVD VRKEVLEEIS PDQLSLEDLL
     EMTDEQVCET VEKYGANQEE CARLNASLSC LRNVHKSGGN LSKQDWIIQW PTTEPGQESN
     PVCPPEPSPW IRTHLSQSPR VQTKCPQHFC PTSPTPGTPV YTQVDRLTVD AYPNLCPPPP
     PLESGHRSLP PSPRQRHVVR TPPRTPNIVT TVTPPGTPPM RRKNKLKPPG TPPPSSRKLI
     HLIPGFTALH RSKSHEFQLG NRVDEANTPK AKKKSKPLNL KIHSGVGSCE NIPAQQRSPL
     LSERSLRSFF VGHGPFLPST PPVHTEANFS ANTLSVPRWS PQIPRRDLGN SIKHRFSTKY
     WMSQTCTVCG KGMLFGLKCK NCKLKCHNKC TKEAPPCHLL IIHRGDSLCC FYPTDPARLV
     RTESVPCDIN NPVRKPARYS DLHISQTLPK TNKINKDHIP VPYQPDSSSN PSSTTSSTPS
     SPAPPLPPSA TPPSPLHPSP QCPRQKKNFN LPASHYYKYK QQFIFPDVVP VPETPTRAPQ
     VILHPVTSNT ILEGNPLLQI EVEPTSENEE SHNEAEESED EFEEMNLSLL SARSFPRKAS
     QTSIFLQEWD IPFEQLEIGE LIGKGRFGQV YHGRWHGEVA IRLIDIERDN EDQLKAFKRE
     VMAYRQTRHE NVVLFMGACM SPPHLAIITS LCKGRTLYSV VRDAKIVLDV NKTRQIAQEI
     VKGMGYLHAK GILHKDLKSK NVFYDNGKVV ITDFGLFSIS GVLQAGRRDD KLRIQNGWLC
     HLAPEIIRQL SPDTEEDKLP FSKHSDVFAL GTIWYELHAR EWPFKTQPAE AIIWQMGTGM
     KPNLSQIGMG KEISDILLFC WAFEQEERPT FTKLMDMLEK LPKRNRRLSH PGHFWKSAE
//
ID   FFR_MOUSE               Reviewed;         782 AA.
AC   Q3UVL4; Q0VF89; Q0VF90; Q3UK22; Q9CXM6;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   08-MAR-2011, entry version 44.
DE   RecName: Full=Protein fat-free homolog;
GN   Name=Ffr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J, and DBA/2; TISSUE=Head, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Required for both Golgi structure and vesicular
CC       trafficking, and ultimately lipid transport (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3UVL4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UVL4-2; Sequence=VSP_036128, VSP_036129;
CC       Name=3;
CC         IsoId=Q3UVL4-3; Sequence=VSP_036126, VSP_036127;
CC   -!- SIMILARITY: Belongs to the fat-free family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI18932.1; Type=Frameshift; Positions=558;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK014229; BAB29217.1; -; mRNA.
DR   EMBL; AK137155; BAE23255.1; -; mRNA.
DR   EMBL; AK146211; BAE26981.1; -; mRNA.
DR   EMBL; AC131692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466612; EDL33203.1; -; Genomic_DNA.
DR   EMBL; BC118930; AAI18931.1; -; mRNA.
DR   EMBL; BC118931; AAI18932.1; ALT_FRAME; mRNA.
DR   IPI; IPI00110493; -.
DR   IPI; IPI00652882; -.
DR   IPI; IPI00785407; -.
DR   RefSeq; NP_001074510.1; NM_001081041.1.
DR   UniGene; Mm.227361; -.
DR   ProteinModelPortal; Q3UVL4; -.
DR   STRING; Q3UVL4; -.
DR   PhosphoSite; Q3UVL4; -.
DR   PRIDE; Q3UVL4; -.
DR   Ensembl; ENSMUST00000025711; ENSMUSP00000025711; ENSMUSG00000024797.
DR   GeneID; 68505; -.
DR   KEGG; mmu:68505; -.
DR   UCSC; uc008ghb.1; mouse.
DR   MGI; MGI:1915755; 1110014N23Rik.
DR   eggNOG; roNOG10006; -.
DR   GeneTree; ENSGT00390000001738; -.
DR   HOGENOM; HBG314794; -.
DR   HOVERGEN; HBG107916; -.
DR   InParanoid; Q3UVL4; -.
DR   OMA; LMDSETD; -.
DR   OrthoDB; EOG49W2DW; -.
DR   ArrayExpress; Q3UVL4; -.
DR   Bgee; Q3UVL4; -.
DR   Genevestigator; Q3UVL4; -.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR016159; Cullin_repeat-like_dom.
DR   InterPro; IPR014812; Vps51.
DR   Pfam; PF08700; Vps51; 1.
DR   SUPFAM; SSF74788; Cullin_repeat-like; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Golgi apparatus; Lipid transport;
KW   Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1    782       Protein fat-free homolog.
FT                                /FTId=PRO_0000358913.
FT   COILED      116    148       Potential.
FT   COILED      270    292       Potential.
FT   MOD_RES      18     18       Phosphoserine (By similarity).
FT   VAR_SEQ     120    140       DTIRKMKNDFRKMEDEMDRLA -> GDPTGTHSSVLHHPHQ
FT                                VLTPC (in isoform 3).
FT                                /FTId=VSP_036126.
FT   VAR_SEQ     141    782       Missing (in isoform 3).
FT                                /FTId=VSP_036127.
FT   VAR_SEQ     482    577       GEFCSQGVREGLIVGFIRSMCQTAQSFCDSPGEKGGATPPA
FT                                LLLLLSRLCLDYETATISYILTLTDEQFLVQDQSPVTPVST
FT                                LCAEARETARRLLT -> VCCPLALLIRSADWPSSSLLLVF
FT                                GEPWDMSPAPHNTVSSTLRVESHSQEAVWRRKCYAAGLKLE
FT                                GYQGPHCCQPYHRGSEAGWGGLWRRVKAKREE (in
FT                                isoform 2).
FT                                /FTId=VSP_036128.
FT   VAR_SEQ     578    782       Missing (in isoform 2).
FT                                /FTId=VSP_036129.
FT   CONFLICT    265    265       A -> P (in Ref. 1; BAE26981).
FT   CONFLICT    339    339       A -> D (in Ref. 1; BAE23255).
FT   CONFLICT    409    409       H -> R (in Ref. 1; BAE26981).
FT   CONFLICT    422    422       L -> M (in Ref. 1; BAE26981).
SQ   SEQUENCE   782 AA;  86187 MW;  377198219AAF5F6C CRC64;
     MAAAAAVGPG LGSGPGDSPE GPEADAPERR RKAHGMLKLY YGLSEGEVAG HPAGPDPLDP
     TDLNGAHFDP EVYLDKLRRE CPLAQLMDSE TDMVRQIRAL DSDMQTLVYE NYNKFISATD
     TIRKMKNDFR KMEDEMDRLA TNMAVITNFS ARISATLQDR HERITKLAGV HALLRKLQFL
     FELPSRLTKC VELGAYGQAV RYQGRARAVL QQYQHLPSFR AIQDDCQVIT ARLAQQLRQR
     FREGCSGAPE QAECVELLLA LGEPAEELCE EFLAHARGRL EEELSSLEAE LGPSPPAPDV
     LEFTDRGGNG FVGGLCQVAA AYQELFAAQG PAGAEKLAAF AQELGGRYFA LVERRLAQEQ
     GGSDNSLLVR ALDRFHRRLR APGALLAAAG LSESATEIVE RVARERLSHH LQGLKAAFLS
     SLTDVRQALA APRLAGKEGP SLAELLANVA SSILSHIKTS LASVHLFTAK EVSFSNKPYF
     RGEFCSQGVR EGLIVGFIRS MCQTAQSFCD SPGEKGGATP PALLLLLSRL CLDYETATIS
     YILTLTDEQF LVQDQSPVTP VSTLCAEARE TARRLLTHYV KVQGLVISQM LRKSVETRDW
     LSTLEPRNVR AVMKRVVEDT TAIDVQVGLL YEEGVRKAQS SDSSKRTFSV YSSSRQQGRY
     APSYTPSAPM DTNLLSNIQK LFSERIDVFS PVEFNKVSVL TGIIKISLKT LLECVRLRTF
     GRFGLQQVQV DCHFLQLYLW RFVADEELVH LLLDEVVASA ALRCPDPVPM EPSVVEVICE
     RG
//
ID   TTBK2_MOUSE             Reviewed;        1243 AA.
AC   Q3UVR3; A2AW12; Q3TSR6; Q3UFW0; Q571D1; Q8BKA4; Q924U8;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-FEB-2011, entry version 50.
DE   RecName: Full=Tau-tubulin kinase 2;
GN   Name=Ttbk2; Synonyms=Kiaa0847, Ttbk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Eye, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreatic islet;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-320, AND FUNCTION.
RC   TISSUE=Brain;
RX   MEDLINE=21157358; PubMed=11257498; DOI=10.1016/S0014-5793(01)02256-6;
RA   Tomizawa K., Omori A., Ohtake A., Sato K., Takahashi M.;
RT   "Tau-tubulin kinase phosphorylates tau at Ser-208 and Ser-210, sites
RT   found in paired helical filament-tau.";
RL   FEBS Lett. 492:221-227(2001).
CC   -!- FUNCTION: Serine/threonine kinase which is able to phosphorylate
CC       tau on serines.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UVR3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UVR3-2; Sequence=VSP_018276;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC       protein kinase family.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90183.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK053820; BAC35540.1; -; mRNA.
DR   EMBL; AK137024; BAE23206.1; -; mRNA.
DR   EMBL; AK148269; BAE28449.1; -; mRNA.
DR   EMBL; AK161858; BAE36609.1; -; mRNA.
DR   EMBL; AK220258; BAD90183.1; ALT_INIT; mRNA.
DR   EMBL; AL935168; CAM21401.1; -; Genomic_DNA.
DR   EMBL; AB046593; BAB62004.2; -; mRNA.
DR   IPI; IPI00222562; -.
DR   IPI; IPI00754147; -.
DR   RefSeq; NP_001020027.1; NM_001024856.2.
DR   RefSeq; NP_001020028.1; NM_001024857.2.
DR   RefSeq; NP_542966.2; NM_080788.3.
DR   UniGene; Mm.275698; -.
DR   ProteinModelPortal; Q3UVR3; -.
DR   SMR; Q3UVR3; 14-299.
DR   STRING; Q3UVR3; -.
DR   PhosphoSite; Q3UVR3; -.
DR   PRIDE; Q3UVR3; -.
DR   Ensembl; ENSMUST00000028740; ENSMUSP00000028740; ENSMUSG00000090100.
DR   Ensembl; ENSMUST00000057135; ENSMUSP00000055032; ENSMUSG00000090100.
DR   Ensembl; ENSMUST00000085840; ENSMUSP00000083001; ENSMUSG00000090100.
DR   GeneID; 140810; -.
DR   KEGG; mmu:140810; -.
DR   UCSC; uc008lww.1; mouse.
DR   CTD; 140810; -.
DR   MGI; MGI:2155779; Ttbk2.
DR   GeneTree; ENSGT00600000084076; -.
DR   HOVERGEN; HBG061812; -.
DR   InParanoid; Q3UVR3; -.
DR   PhylomeDB; Q3UVR3; -.
DR   NextBio; 370009; -.
DR   ArrayExpress; Q3UVR3; -.
DR   Bgee; Q3UVR3; -.
DR   CleanEx; MM_TTBK1; -.
DR   Genevestigator; Q3UVR3; -.
DR   GermOnline; ENSMUSG00000027284; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1   1243       Tau-tubulin kinase 2.
FT                                /FTId=PRO_0000234343.
FT   DOMAIN       21    284       Protein kinase.
FT   NP_BIND      27     35       ATP (By similarity).
FT   COMPBIAS    307    311       Poly-Thr.
FT   COMPBIAS   1099   1242       Ser-rich.
FT   ACT_SITE    141    141       Proton acceptor (By similarity).
FT   BINDING      50     50       ATP (By similarity).
FT   MOD_RES     786    786       Phosphoserine (By similarity).
FT   VAR_SEQ    1091   1243       LRRYKVLGSSNSDSDLFSRLAQILQNGSQKSRSTTQCKSPG
FT                                SPHNPKTPPKSPVVPRRSPSASPRSSSLPRTSSSSPSRAGR
FT                                PHHDQRSSSPHLGRSKSPPSHSGSSSSRRSCQQEHCKPSKN
FT                                GPKGSGSLHHHSTSSKTPPGKSKPASKLSR -> PGSPQAV
FT                                HLITLLQGPGNQRKAPRRPAGLAGWADLPGPPEPHPSRTRP
FT                                VVQRSIPVAGSAPPGCPWRECACSVASERLHRDGGRFRVAA
FT                                ARRGAGRSRRAVDRAQHPEFGG (in isoform 2).
FT                                /FTId=VSP_018276.
FT   CONFLICT    192    192       Y -> C (in Ref. 4; BAB62004).
FT   CONFLICT    196    196       N -> D (in Ref. 4; BAB62004).
FT   CONFLICT    228    228       K -> E (in Ref. 4; BAB62004).
FT   CONFLICT    317    320       LHTR -> CTPA (in Ref. 4; BAB62004).
FT   CONFLICT    490    490       P -> L (in Ref. 2; BAE28449).
FT   CONFLICT    500    500       H -> R (in Ref. 2; BAE28449).
FT   CONFLICT    591    591       G -> V (in Ref. 2; BAE28449).
FT   CONFLICT    890    890       R -> G (in Ref. 2; BAE28449).
SQ   SEQUENCE   1243 AA;  136770 MW;  978D68D7BC7A535E CRC64;
     MSGGGEQPDI LSVGILVKER WKVLRKIGGG GFGEIYDALD MLTRENVALK VESAQQPKQV
     LKMEVAVLKK LQGKDHVCRF IGCGRNDRFN YVVMQLQGRN LADLRRSQSR GTFTISTTLR
     LGKQILESIE SIHSVGFLHR DIKPSNFAMG RFPSTCRKCF MLDFGLARQF TNSCGDVRPP
     RAVAGFRGTV RYASINAHRN REMGRHDDLW SLFYMLVEFV VGQLPWRKIK DKEQVGSIKE
     RYDHRLMLKH LPPEFSTFLD HISSLDYFTK PDYQLLTSVF DNSIKTFGVI ESDPFDWEKS
     GTDGSLTTTT TSATPQLHTR LTPAAIGIAN ATPIPGDLLR ENTDEVFPDE QLSDGENGIP
     VGVSPDKLPG SLGHPRPQEK DVWEEMDINK NKIKLGICKA ATEEENSHGQ VNGILNAPSL
     GSPIRVRSEI TQPDRDVPLV RKLRSIHSFE LEKRLTLEPK PDTDKFLETC MEKMQKDSSA
     GKEPVPPALP HKPCVPVVTH TDHIWHYDDE YLPDASKPAS ANTPEQADGG GSNGFIAVNL
     SSCKQEVDSK EWVIVDKEQD LQDFRTNEVL GHKTTGSPSD EEPEVLQVLE GSPQDEKIQV
     GPWTDNHHLK KESSGVVLAL SAECPATAAS ELYTDRLDLQ AGAASQFITV TPTSPMEAQA
     EGPLTAITIP RPSVASTQST SGSFHYGPQP EKKDLQPLEP TVELYSPREN FSGLVVTEGE
     LASGGSRVDL GLQIDHTGHD MLPNMRDGDT SQDLGPKDPP DHNRLAVKEF EHLPGETEER
     SLLLGSENED ERLSKGQHCI EVSSPGELVT AERAQLAATE PLHVSETQNC SVLPNQDKTH
     EIMKLLAVGT SEISPQAIDP HAEGQIGQMA AMQKNKLFKD DGIQSESLPR QQGDLSAFLH
     QEGKREKVVP RNGELYHCVS ENEHGPPTRK DMLRSSFVTR HSRIPVLAQE IDSTFESSSA
     ISAKEKLLQK KAYQPEIVKL LVEKRQFKSF LGDLSSASDK LIEEKLAAVP VPFSEEEVFA
     PFSRLAADSH LSRSVEDSFL SPIISQARKS KIPRPVSWVS TDQINGSASP QFLPRPPPGK
     PPVRPGVEAR LRRYKVLGSS NSDSDLFSRL AQILQNGSQK SRSTTQCKSP GSPHNPKTPP
     KSPVVPRRSP SASPRSSSLP RTSSSSPSRA GRPHHDQRSS SPHLGRSKSP PSHSGSSSSR
     RSCQQEHCKP SKNGPKGSGS LHHHSTSSKT PPGKSKPASK LSR
//
ID   GRM5_MOUSE              Reviewed;        1203 AA.
AC   Q3UVX5;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   11-JAN-2011, entry version 47.
DE   RecName: Full=Metabotropic glutamate receptor 5;
DE            Short=mGluR5;
DE   Flags: Precursor;
GN   Name=Grm5; Synonyms=Gprc1e, Mglur5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- FUNCTION: Receptor for glutamate. The activity of this receptor is
CC       mediated by a G-protein that activates a phosphatidylinositol-
CC       calcium second messenger system and generates a calcium-activated
CC       chloride current (By similarity).
CC   -!- SUBUNIT: The PPXXF motif binds HOMER1, HOMER2 and HOMER3.
CC       Interacts with RYR1, RYR2, ITPR1, SHANK1 and SHANK3 (By
CC       similarity). Interacts with SIAH1 and GRASP. Interacts with NCDN
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UVX5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UVX5-2; Sequence=VSP_028519, VSP_028520;
CC   -!- MISCELLANEOUS: Activated by quisqualate > glutamate > ibotenate >
CC       trans-1- aminocyclopentyl-1,3-dicarboxylate.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
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DR   EMBL; AK136840; BAE23144.1; -; mRNA.
DR   EMBL; AC113033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC113115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC116820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC149088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC163218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00659932; -.
DR   IPI; IPI00867815; -.
DR   RefSeq; NP_001137306.1; NM_001143834.1.
DR   UniGene; Mm.235018; -.
DR   UniGene; Mm.477931; -.
DR   ProteinModelPortal; Q3UVX5; -.
DR   SMR; Q3UVX5; 26-569.
DR   STRING; Q3UVX5; -.
DR   PhosphoSite; Q3UVX5; -.
DR   PRIDE; Q3UVX5; -.
DR   Ensembl; ENSMUST00000061910; ENSMUSP00000051133; ENSMUSG00000049583.
DR   Ensembl; ENSMUST00000107263; ENSMUSP00000102884; ENSMUSG00000049583.
DR   GeneID; 108071; -.
DR   KEGG; mmu:108071; -.
DR   UCSC; uc009ifp.1; mouse.
DR   CTD; 108071; -.
DR   MGI; MGI:1351342; Grm5.
DR   HOVERGEN; HBG107965; -.
DR   Bgee; Q3UVX5; -.
DR   CleanEx; MM_GRM5; -.
DR   Genevestigator; Q3UVX5; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0001639; F:PLC activating metabotropic glutamate receptor activity; TAS:MGI.
DR   GO; GO:0007612; P:learning; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IGI:MGI.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR000337; GPCR_3.
DR   InterPro; IPR011500; GPCR_3_9-Cys_dom.
DR   InterPro; IPR017978; GPCR_3_C.
DR   InterPro; IPR017979; GPCR_3_CS.
DR   InterPro; IPR000162; GPCR_3_mtglu_rcpt.
DR   InterPro; IPR000202; GPCR_3_mtglu_rcpt_5.
DR   InterPro; IPR019588; Metabotropic_Glu_rcpt_Homer-bd.
DR   Pfam; PF00003; 7tm_3; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF10606; GluR_Homer-bdg; 1.
DR   Pfam; PF07562; NCD3G; 1.
DR   PRINTS; PR00248; GPCRMGR.
DR   PRINTS; PR01055; MTABOTROPC5R.
DR   PRINTS; PR00593; MTABOTROPICR.
DR   PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; 1.
DR   PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; 1.
DR   PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
DR   PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Receptor; Signal; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     18       Potential.
FT   CHAIN        19   1203       Metabotropic glutamate receptor 5.
FT                                /FTId=PRO_0000306853.
FT   TOPO_DOM     19    581       Extracellular (Potential).
FT   TRANSMEM    582    602       Helical; Name=1; (Potential).
FT   TOPO_DOM    603    615       Cytoplasmic (Potential).
FT   TRANSMEM    616    636       Helical; Name=2; (Potential).
FT   TOPO_DOM    637    643       Extracellular (Potential).
FT   TRANSMEM    644    665       Helical; Name=3; (Potential).
FT   TOPO_DOM    666    692       Cytoplasmic (Potential).
FT   TRANSMEM    693    713       Helical; Name=4; (Potential).
FT   TOPO_DOM    714    737       Extracellular (Potential).
FT   TRANSMEM    738    758       Helical; Name=5; (Potential).
FT   TOPO_DOM    759    772       Cytoplasmic (Potential).
FT   TRANSMEM    773    793       Helical; Name=6; (Potential).
FT   TOPO_DOM    794    797       Extracellular (Potential).
FT   TRANSMEM    798    818       Helical; Name=7; (Potential).
FT   TOPO_DOM    819   1203       Cytoplasmic (Potential).
FT   COMPBIAS    121    124       Poly-Glu.
FT   COMPBIAS   1046   1049       Poly-Ser.
FT   COMPBIAS   1199   1202       Poly-Ser.
FT   CARBOHYD     88     88       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    209    209       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    377    377       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    381    381       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    444    444       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    733    733       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     303    303       S -> R (in isoform 2).
FT                                /FTId=VSP_028519.
FT   VAR_SEQ     304   1203       Missing (in isoform 2).
FT                                /FTId=VSP_028520.
SQ   SEQUENCE   1203 AA;  131865 MW;  2A09D7EC272ED23C CRC64;
     MVLLLILSVL LLKEDVRGSA QSSERRVVAH MPGDIIIGAL FSVHHQPTVD KVHERKCGAV
     REQYGIQRVE AMLHTLERIN SDPTLLPNIT LGCEIRDSCW HSAVALEQSI EFIRDSLISS
     EEEEGLVRCV DGSSSFRSKK PIVGVIGPGS SSVAIQVQNL LQLFNIPQIA YSATSMDLSD
     KTLFKYFMRV VPSDAQQARA MVDIVKRYNW TYVSAVHTEG NYGESGMEAF KDMSAKEGIC
     IAHSYKIYSN AGEQSFDKLL KKLRSHLPKA RVVACFCEGM TVRGLLMAMR RLGLAGEFLL
     LGSDGWADRY DVTDGYQREA VGGITIKLQS PDVKWFDDYY LKLRPETNLR NPWFQEFWQH
     RFQCRLEGFA QENSKYNKTC NSSLTLRTHH VQDSKMGFVI NAIYSMAYGL HNMQMSLCPG
     YAGLCDAMKP IDGRKLLDSL MKTNFTGVSG DMILFDENGD SPGRYEIMNF KEMGKDYFDY
     INVGSWDNGE LKMDDDEVWS KKNNIIRSVC SEPCEKGQIK VIRKGEVSCC WTCTPCKENE
     YVFDEYTCKA CQLGSWPTDD LTGCDLIPVQ YLRWGDPEPI AAVVFACLGL LATLFVTVIF
     IIYRDTPVVK SSSRELCYII LAGICLGYLC TFCLIAKPKQ IYCYLQRIGI GLSPAMSYSA
     LVTKTNRIAR ILAGSKKKIC TKKPRFMSAC AQLVIAFILI CIQLGIIVAL FIMEPPDIMH
     DYPSIREVYL ICNTTNLGVV TPLGYNGLLI LSCTFYAFKT RNVPANFNEA KYIAFTMYTT
     CIIWLAFVPI YFGSNYKIIT MCFSVSLSAT VALGCMFVPK VYIILAKPER NVRSAFTTST
     VVRMHVGDGK SSSAASRSSS LVNLWKRRGS SGETLRYKDR RLAQHKSEIE CFTPKGSMGN
     GGRATMSSSN GKSVTWAQNE KSTRGQHLWQ RLSVHINKKE NPNQTAVIKP FPKSTESRGQ
     GAGAGGGSGP GAAGAGSAGC TATGGPEPPD AGPKALYDVA EAEERFPAAA RPRSPSPIST
     LSHLAGSAGR TDDDAPSLHS ETAARSSSSQ GSLMEQISSV VTRFTANITE LNSMMLSTAA
     APGPPGTPIC SSYLIPKEIQ LPTTMTTFAE IQPLPAIEVT GGAQPATGPS PAQETPAGAE
     AAPGKPDLEE LVALTPPSPF RDSVDSGSTT PNSPVSESAL CIPSSPKYDT LIIRDYTQSS
     SSL
//
ID   NIBAN_MOUSE             Reviewed;         926 AA.
AC   Q3UW53; A0PJB3; Q3TD68; Q6PE79; Q9ESL7;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=Protein Niban;
DE   AltName: Full=Protein FAM129A;
GN   Name=Fam129a; Synonyms=Niban;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Dendritic cell, Epididymis, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N-3;
RC   TISSUE=Mammary tumor, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2-926.
RX   MEDLINE=20546198; PubMed=11011112;
RA   Majima S., Kajino K., Fukuda T., Otsuka F., Hino O.;
RT   "A novel gene 'Niban' upregulated in renal carcinogenesis: cloning by
RT   the cDNA-amplified fragment length polymorphism approach.";
RL   Jpn. J. Cancer Res. 91:869-874(2000).
RN   [4]
RP   FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17588536; DOI=10.1016/j.bbrc.2007.06.021;
RA   Sun G.D., Kobayashi T., Abe M., Tada N., Adachi H., Shiota A.,
RA   Totsuka Y., Hino O.;
RT   "The endoplasmic reticulum stress-inducible protein Niban regulates
RT   eIF2alpha and S6K1/4E-BP1 phosphorylation.";
RL   Biochem. Biophys. Res. Commun. 360:181-187(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578 AND SER-601, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601 AND SER-755, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Regulates phosphorylation of a number of proteins
CC       involved in translation regulation including EIF2A, EIF4EBP1 and
CC       RPS6KB1. May be involved in the endoplasmic reticulum stress
CC       response.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- INDUCTION: By endoplasmic reticulum stress-inducing agents such as
CC       tunicamycin and thapsigargin in liver, kidney and cerebrum.
CC   -!- DISRUPTION PHENOTYPE: No obvious phenotypic abnormalities but mice
CC       show increased phosphorylation of Eif2a and decreased
CC       phosphorylation of Eif4ebp1 and Rps6kb1.
CC   -!- MISCELLANEOUS: 'Niban' means 'second' in Japanese.
CC   -!- SIMILARITY: Belongs to the Niban family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH21332.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAH58234.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=AAI37844.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAB17052.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAC26641.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK029847; BAC26641.1; ALT_SEQ; mRNA.
DR   EMBL; AK136597; BAE23066.1; -; mRNA.
DR   EMBL; AK170347; BAE41736.1; -; mRNA.
DR   EMBL; BC021332; AAH21332.1; ALT_SEQ; mRNA.
DR   EMBL; BC058234; AAH58234.2; ALT_INIT; mRNA.
DR   EMBL; BC137843; AAI37844.1; ALT_INIT; mRNA.
DR   EMBL; AB049355; BAB17052.1; ALT_INIT; mRNA.
DR   IPI; IPI00113389; -.
DR   RefSeq; NP_071301.2; NM_022018.3.
DR   UniGene; Mm.157700; -.
DR   ProteinModelPortal; Q3UW53; -.
DR   STRING; Q3UW53; -.
DR   PhosphoSite; Q3UW53; -.
DR   PRIDE; Q3UW53; -.
DR   Ensembl; ENSMUST00000148810; ENSMUSP00000115822; ENSMUSG00000026483.
DR   GeneID; 63913; -.
DR   KEGG; mmu:63913; -.
DR   CTD; 63913; -.
DR   MGI; MGI:2137237; Fam129a.
DR   eggNOG; roNOG11334; -.
DR   GeneTree; ENSGT00530000063284; -.
DR   HOGENOM; HBG715459; -.
DR   HOVERGEN; HBG108186; -.
DR   InParanoid; Q3UW53; -.
DR   OMA; KMEPCYT; -.
DR   OrthoDB; EOG4MGS71; -.
DR   ArrayExpress; Q3UW53; -.
DR   Bgee; Q3UW53; -.
DR   Genevestigator; Q3UW53; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:UniProtKB.
DR   GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; Stress response; Translation regulation.
FT   CHAIN         1    926       Protein Niban.
FT                                /FTId=PRO_0000355583.
FT   MOD_RES     578    578       Phosphoserine.
FT   MOD_RES     601    601       Phosphoserine.
FT   MOD_RES     755    755       Phosphoserine.
FT   CONFLICT      2      4       GGS -> ASA (in Ref. 3; BAB17052).
FT   CONFLICT    437    437       R -> G (in Ref. 2; AAH21332).
FT   CONFLICT    608    608       P -> Q (in Ref. 1; BAE41736).
FT   CONFLICT    651    651       V -> E (in Ref. 2; AAH21332).
FT   CONFLICT    680    680       T -> S (in Ref. 2; AAH21332).
FT   CONFLICT    693    693       P -> S (in Ref. 2; AAH21332).
FT   CONFLICT    705    705       K -> E (in Ref. 2; AAH21332).
FT   CONFLICT    911    911       V -> L (in Ref. 1; BAE23066).
SQ   SEQUENCE   926 AA;  102649 MW;  D41F603AF127673C CRC64;
     MGGSASSQLD EGKCAYIRGK TEASIKNFSP YYSRQYSVAF CNHVRSEVEQ QRDLTSQFLK
     TKPPLEPGTV LYEAELSQFA EDIRKWKDRY IVIKNDFAVE SYESKEAYQR GAVPKSRILP
     AGGKVLTSEE EYSLLSDKHF PDPTASSEKN SQPFVLLPKA FPVYLWQPYL RHGYFCFHEA
     AEQQKFSALL NDCIRHLNHD YMKQTTFEAQ AFLEAVQFFR QEKGHYGSWE MTTGDEVQVL
     SKLVMEELLP TLQTDLLPKL KGKKNDRKRA WFGLLEEAYN LVQHQVSEGL NALKEECRAL
     TKDLEGTIRS DMDQIVTSKN FLTGKIRAMV AQPAEQCCGE SVQPFLASIL EELMGPVSSG
     FSEVRALFEK EVDELSQSFH ATQDSAQLKE GLQQLMKLPL DSVKMEPCYT KVTLLPERLL
     DLQSRFRFPH VDLVVQRTQN YMQELMENAV FTFEQLLSPY LQGEASRIPV AIEKVKLRVL
     KQYDYDSSTI RKKIFQEALI QITLPTVQKA LASTCKPELQ KYEQFIFADH TNMIHVENVY
     EEILYEILLD ETLKVITEAA ILKKHNLFED NMALPSESVS SLTDLKTAMG SNQASPARRV
     SAILPGAPDN ELPSNEVFQE PEEKKEQPGV PGSLAISASS CPSGGDGQVS VDHSAGGPLT
     VENTAGPLSS HLSEVEAGGT LKDEEPTCQS PEPSAVPGSL KELKKLLTVT VSVESAPVVE
     NDIHNGTPVP QENIKEEESK IHPEASHPAA IQQDSCEERE VREKEAQPLE AEAPGVDLGI
     LPEGRGSTSQ STSGGLTENT SCPGPIEEPF EAQEPAEKVL PAIVSTEDSP QAGGEAEHSV
     TVTPQEDATL SSNPICPMES NEVAQASGDQ EVLGGEDSSA LGMDTEQVND THEHACQWLV
     EDTLSTDILA VHDFDVSSPE QPSEEW
//
ID   Q3UW66_MOUSE            Unreviewed;       297 AA.
AC   Q3UW66;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 39.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Mpst;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cecum;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cecum;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cecum;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cecum;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cecum;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cecum;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cecum;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cecum;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 2 rhodanese domains.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK136571; BAE23053.1; -; mRNA.
DR   IPI; IPI00604945; -.
DR   RefSeq; NP_001155964.1; NM_001162492.1.
DR   RefSeq; NP_001155965.1; NM_001162493.1.
DR   RefSeq; NP_619611.3; NM_138670.3.
DR   UniGene; Mm.294215; -.
DR   ProteinModelPortal; Q3UW66; -.
DR   SMR; Q3UW66; 4-294.
DR   STRING; Q3UW66; -.
DR   PhosphoSite; Q3UW66; -.
DR   PRIDE; Q3UW66; -.
DR   Ensembl; ENSMUST00000043865; ENSMUSP00000043061; ENSMUSG00000071711.
DR   GeneID; 246221; -.
DR   KEGG; mmu:246221; -.
DR   NMPDR; fig|10090.3.peg.30213; -.
DR   UCSC; uc007wpe.1; mouse.
DR   CTD; 246221; -.
DR   MGI; MGI:2179733; Mpst.
DR   eggNOG; roNOG13491; -.
DR   HOVERGEN; HBG002345; -.
DR   PhylomeDB; Q3UW66; -.
DR   ArrayExpress; Q3UW66; -.
DR   Bgee; Q3UW66; -.
DR   Genevestigator; Q3UW66; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IEA:InterPro.
DR   GO; GO:0008272; P:sulfate transport; IEA:InterPro.
DR   InterPro; IPR001763; Rhodanese-like.
DR   InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR   Gene3D; G3DSA:3.40.250.10; Rhodanese-like; 2.
DR   Pfam; PF00581; Rhodanese; 2.
DR   SMART; SM00450; RHOD; 2.
DR   SUPFAM; SSF52821; Rhodanese-like; 2.
DR   PROSITE; PS00380; RHODANESE_1; 1.
DR   PROSITE; PS00683; RHODANESE_2; 1.
DR   PROSITE; PS50206; RHODANESE_3; 2.
PE   2: Evidence at transcript level;
KW   Transferase.
SQ   SEQUENCE   297 AA;  33097 MW;  9D316B9AD9344D0A CRC64;
     MAAPQLFRAL VSAQWVAEAL KAPRSSQPLK LLDASWYLPK LGRDARREFE ERHIPGAAFF
     DIDRCSDHTS PYDHMLPNAT HFADYAGSLG VSAATHVVIY DDSDQGLYSA PRVWWMFRAF
     GHHSVSLLDG GFRHWLNQNL PISSGKSHSE PAEFSAQLDP SFIKTHEDIL ENLDARRFQV
     VDARAAGRFQ GTQPEPRDGI EPGHIPGSVN IPFTEFLTNE GLEKSPEEIK RLFKEKKVDL
     SKPLVATCGS GVTACHVVLG AFLCGKSDVP VYDGSWVEWY MRAQPEHIIS EGRGKTQ
//
ID   Q3UWD7_MOUSE            Unreviewed;       716 AA.
AC   Q3UWD7;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-FEB-2011, entry version 58.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Egf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Colon;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Colon;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Colon;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Colon;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Colon;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Colon;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Colon;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Colon;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK136439; BAE22978.1; -; mRNA.
DR   IPI; IPI00890244; -.
DR   UniGene; Mm.252481; -.
DR   UniGene; Mm.480769; -.
DR   ProteinModelPortal; Q3UWD7; -.
DR   SMR; Q3UWD7; 2-242, 250-289, 346-528.
DR   STRING; Q3UWD7; -.
DR   Ensembl; ENSMUST00000029653; ENSMUSP00000029653; ENSMUSG00000028017.
DR   UCSC; uc008rig.1; mouse.
DR   MGI; MGI:95290; Egf.
DR   InParanoid; Q3UWD7; -.
DR   ArrayExpress; Q3UWD7; -.
DR   Bgee; Q3UWD7; -.
DR   Genevestigator; Q3UWD7; -.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005154; F:epidermal growth factor receptor binding; IDA:MGI.
DR   GO; GO:0000186; P:activation of MAPKK activity; IDA:MGI.
DR   GO; GO:0048754; P:branching morphogenesis of a tube; IDA:MGI.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:MGI.
DR   GO; GO:0060749; P:mammary gland alveolus development; IGI:MGI.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
DR   GO; GO:0021940; P:positive regulation of cerebellar granule cell precursor proliferation; IDA:MGI.
DR   GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR006209; EGF.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR001881; EGF_Ca-bd.
DR   InterPro; IPR013091; EGF_Ca-bd_2.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   Gene3D; G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF07645; EGF_CA; 2.
DR   Pfam; PF00058; Ldl_recept_b; 3.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00135; LY; 5.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 4.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS51120; LDLRB; 5.
PE   2: Evidence at transcript level;
KW   EGF-like domain; Membrane; Repeat; Transmembrane; Transmembrane helix.
SQ   SEQUENCE   716 AA;  77941 MW;  CC1CA29F49966D98 CRC64;
     MHFDGTDYKV LLSRQMGMVF ALDYDPVESK IYFAQTALKW IERANMDGSQ RERLITEGVD
     TLEGLALDWI GRRIYWTDSG KSVVGGSDLS GKHHRIIIQE RISRPRGIAV HPRARRLFWT
     DVGMSPRIES ASLQGSDRVL IASSSLLEPS GITIDYLTDT LYWCDTKRSV IEMANLDGSK
     RRRLIQNDVG HPFSLAVFED HLWVSDWAIP SVIRVNKRTG QNRVRLQGSM LKPSSLVVVH
     PLAKPGADPC LYRNGGCEHI CQESLGTARC LCREGFVKAW DGKMCLPQDY PILSGENADL
     SKEVTSLSNS TQAEVPDDDG TESSTLVAEI MVSGMNYEDD CGPGGCGSHA RCVSDGETAE
     CQCLKGFARD GNLCSDIDEC VLARSDCPST SSRCINTEGG YVCRCSEGYE GDGISCFDID
     ECQRGAHNCG ENAACTNTEG GYNCTCAGRP SSPGLSCPDS TAPSLLGEDG HHLDRNSYPG
     CPSSYDGYCL NGGVCMHIES LDSYTCNCVI GYSGDRCQTR DLRWWELRHA GYGQKHDIMV
     VAVCMVALVL LLVLGMWGTY YYRTRKQLSN PPKNPCDEPS GSVSSSGPNS SSGAAVASCP
     QPWFVVLEKH QDPKNGSLPA DGTNGAVVDA GLSPSLQLGS VHLTSWRQKP HIDGMGTGQS
     CWIPPSSDRG PQEIEGNSHL PSYRPVGPEK LHSLQSANGS CHERAPDLPR QTEPVQ
//
ID   Q3UWL8_MOUSE            Unreviewed;       134 AA.
AC   Q3UWL8;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   SubName: Full=Prefoldin 4;
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Pfdn4; ORFNames=RP23-43J11.1-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=In vitro fertilized eggs;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=In vitro fertilized eggs;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=In vitro fertilized eggs;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=In vitro fertilized eggs;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=In vitro fertilized eggs;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=In vitro fertilized eggs;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=In vitro fertilized eggs;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=In vitro fertilized eggs;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RA   Wood J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK136249; BAE22896.1; -; mRNA.
DR   EMBL; AL954701; CAM24417.1; -; Genomic_DNA.
DR   IPI; IPI00378557; -.
DR   RefSeq; NP_001103622.1; NM_001110152.2.
DR   RefSeq; NP_001186831.1; NM_001199902.1.
DR   UniGene; Mm.28808; -.
DR   STRING; Q3UWL8; -.
DR   PhosphoSite; Q3UWL8; -.
DR   PRIDE; Q3UWL8; -.
DR   Ensembl; ENSMUST00000063682; ENSMUSP00000070596; ENSMUSG00000052033.
DR   GeneID; 109054; -.
DR   KEGG; mmu:109054; -.
DR   UCSC; uc008oce.1; mouse.
DR   CTD; 109054; -.
DR   MGI; MGI:1923512; Pfdn4.
DR   eggNOG; roNOG16365; -.
DR   HOGENOM; HBG398530; -.
DR   HOVERGEN; HBG005034; -.
DR   InParanoid; Q3UWL8; -.
DR   OMA; NLEDACE; -.
DR   OrthoDB; EOG4K0QPS; -.
DR   PhylomeDB; Q3UWL8; -.
DR   NextBio; 361612; -.
DR   ArrayExpress; Q3UWL8; -.
DR   Bgee; Q3UWL8; -.
DR   Genevestigator; Q3UWL8; -.
DR   GO; GO:0016272; C:prefoldin complex; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   InterPro; IPR002777; PFD_beta-like.
DR   InterPro; IPR009053; Prefoldin.
DR   InterPro; IPR016661; Prefoldin_su-4.
DR   Pfam; PF01920; Prefoldin_2; 1.
DR   PIRSF; PIRSF016477; Prefoldin_subunit_4; 1.
DR   SUPFAM; SSF46579; Prefoldin; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   134 AA;  15238 MW;  C3C3D49EE66DA186 CRC64;
     MAATMKKAAA EDVNVTFEDQ QKINKFARNT SRITELKEEI EVKKKHLQNL EDACDDIMLA
     DDDCLMIPYQ IGDVFISHSQ EETQEMLEDA KKTLQEEIDA LESRVASIQR VLADLKVQLY
     AKFGSNINLE ADES
//
ID   Q3UX51_MOUSE            Unreviewed;       664 AA.
AC   Q3UX51;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-FEB-2011, entry version 38.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Atxn2; Synonyms=Sca2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=In vitro fertilized eggs;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=In vitro fertilized eggs;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=In vitro fertilized eggs;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=In vitro fertilized eggs;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=In vitro fertilized eggs;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=In vitro fertilized eggs;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=In vitro fertilized eggs;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=In vitro fertilized eggs;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK135879; BAE22712.1; -; mRNA.
DR   IPI; IPI00970289; -.
DR   UniGene; Mm.260900; -.
DR   STRING; Q3UX51; -.
DR   Ensembl; ENSMUST00000051950; ENSMUSP00000056715; ENSMUSG00000042605.
DR   Ensembl; ENSMUST00000111762; ENSMUSP00000107392; ENSMUSG00000042605.
DR   UCSC; uc008zkf.1; mouse.
DR   MGI; MGI:1277223; Atxn2.
DR   GeneTree; ENSGT00530000063565; -.
DR   HOVERGEN; HBG050623; -.
DR   InParanoid; Q3UX51; -.
DR   ArrayExpress; Q3UX51; -.
DR   Bgee; Q3UX51; -.
DR   Genevestigator; Q3UX51; -.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR   GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:MGI.
DR   InterPro; IPR009818; Ataxin-2_C.
DR   Pfam; PF07145; PAM2; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   664 AA;  70657 MW;  F0BAC2F9AB68977F CRC64;
     VSAGRGSMSS GLEFVSHNPP SEAAAPPVAR TSPAGGTWSS VVSGVPRLSP KTHRPRSPRQ
     SSIGNSPSGP VLASPQAGII PAEAVSMPVP AASPTPASPA SNRALTPSIE AKDSRLQDQR
     QNSPAGSKEN VKASETSPSF SKADNKGMSP VVSEHRKQID DLKKFKNDFR LQPSSTSESM
     DQLLSKNREG EKSRDLIKDK TEASAKDSFI DSSSSSSNCT SGSSKTNSPS ISPSMLSNAE
     HKRGPEVTSQ GVQTSSPACK QEKDDREEKK DTTEQVRKST LNPNAKEFNP RSFSQPKPST
     TPTSPRPQAQ PSPSMVGHQQ PAPVYTQPVC FAPNMMYPVP VSPGVQPLYP IPMTPMPVNQ
     AKTYRAGKVP NMPQQRQDQH HQSTMMHPAS AAGPPIVATP PAYSTQYVAY SPQQFPNQPL
     VQHVPHYQSQ HPHVYSPVIQ GNARMMAPPA HAQPGLVSSS AAQFGAHEQT HAMYVSTGSL
     AQQYAHPNAA LHPHTPHPQP SATPTGQQQS QHGGSHPAPS PVQHHQHQAA QALHLASPQQ
     QSAIYHAGLA PTPPSMTPAS NTQSPQSSFP AAQQTVFTIH PSHVQPAYTT PPHMAHVPQA
     HVQSGMVPSH PTAHAPMMLM TTQPPGGPQA ALAQSALQPI PVSTTAHFPY MTHPSVQAHH
     QQQL
//
ID   FA81A_MOUSE             Reviewed;         364 AA.
AC   Q3UXZ6; Q8BQV1; Q8C548; Q8R3B5; Q9D369;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=Protein FAM81A;
GN   Name=Fam81a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Corpora quadrigemina, Hypothalamus, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the FAM81 family.
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DR   EMBL; AK018282; BAB31146.1; -; mRNA.
DR   EMBL; AK044090; BAC31769.1; -; mRNA.
DR   EMBL; AK046408; BAC32712.1; -; mRNA.
DR   EMBL; AK079541; BAC37676.1; -; mRNA.
DR   EMBL; AK135091; BAE22417.1; -; mRNA.
DR   EMBL; BC025646; AAH25646.1; -; mRNA.
DR   IPI; IPI00469163; -.
DR   RefSeq; NP_084060.1; NM_029784.2.
DR   UniGene; Mm.44355; -.
DR   PRIDE; Q3UXZ6; -.
DR   Ensembl; ENSMUST00000034749; ENSMUSP00000034749; ENSMUSG00000032224.
DR   GeneID; 76886; -.
DR   KEGG; mmu:76886; -.
DR   UCSC; uc009qnu.1; mouse.
DR   CTD; 76886; -.
DR   MGI; MGI:1924136; Fam81a.
DR   eggNOG; roNOG10625; -.
DR   GeneTree; ENSGT00390000004985; -.
DR   HOGENOM; HBG283539; -.
DR   HOVERGEN; HBG081513; -.
DR   InParanoid; Q3UXZ6; -.
DR   OMA; SARNWLQ; -.
DR   OrthoDB; EOG466VM5; -.
DR   PhylomeDB; Q3UXZ6; -.
DR   NextBio; 346003; -.
DR   ArrayExpress; Q3UXZ6; -.
DR   Bgee; Q3UXZ6; -.
DR   CleanEx; MM_6430514L14RIK; -.
DR   Genevestigator; Q3UXZ6; -.
DR   GermOnline; ENSMUSG00000032224; Mus musculus.
PE   2: Evidence at transcript level;
KW   Coiled coil.
FT   CHAIN         1    364       Protein FAM81A.
FT                                /FTId=PRO_0000265120.
FT   COILED       75    107       Potential.
FT   COILED      158    189       Potential.
FT   COILED      261    287       Potential.
FT   CONFLICT     31     31       E -> K (in Ref. 1; BAE22417).
FT   CONFLICT     32     32       D -> K (in Ref. 1; BAC37676).
FT   CONFLICT     43     64       ALVEHAFRIKDDIVSSLQKMQN -> GTGWSMASGFKMKSS
FT                                QFGKKCRI (in Ref. 1; BAC37676).
FT   CONFLICT     68     68       G -> S (in Ref. 1; BAC37676).
FT   CONFLICT    122    139       QLSGLGDLRGRVARCDAS -> HSLAWEISEEELQSATPT
FT                                (in Ref. 1; BAB31146).
FT   CONFLICT    189    189       S -> Y (in Ref. 1; BAC32712).
SQ   SEQUENCE   364 AA;  41710 MW;  78CA6C1F25CB7B42 CRC64;
     MHLRRVKTMP RHSQSLTMAP YSSVSLVEQL EDRILCHEKT TAALVEHAFR IKDDIVSSLQ
     KMQNKGGGDR LARLFLEEHI RNITAIVKQL NRDIEVLQEQ IRARDNISYG TNSALKTLEM
     RQLSGLGDLR GRVARCDASI ARLSAEHKST YEGLQHLNKE QQAAKLILET KIKDAEGQIS
     QLLSRVDLSI SEQSTKLKMS HRDSNHQLQL LDTKFKGTVE ELSNQILSAR SWLQQEQERI
     EKELLQKIDH LSLIVKENSG ANERDVEKKL SQMSARLDKI EESQKRNAEG QRKPDEEKVH
     GRISKLELQM TEDMKEMKAE VNAGFSAIYE SIGSLRQVLE AKMKLDRDQL QKQIQQMQKP
     ETAM
//
ID   KDM5A_MOUSE             Reviewed;        1690 AA.
AC   Q3UXZ9; Q3TM94; Q3UMI5; Q66JZ3;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Lysine-specific demethylase 5A;
DE            EC=1.14.11.-;
DE   AltName: Full=Histone demethylase JARID1A;
DE   AltName: Full=Jumonji/ARID domain-containing protein 1A;
DE   AltName: Full=Retinoblastoma-binding protein 2;
DE            Short=RBBP-2;
GN   Name=Kdm5a; Synonyms=Jarid1a, Rbp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1552.
RC   STRAIN=C57BL/6J; TISSUE=Lung, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1099.
RC   STRAIN=C57BL/6J; TISSUE=Germ cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 1538-1546, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17320163; DOI=10.1016/j.cell.2007.02.013;
RA   Klose R.J., Yan Q., Tothova Z., Yamane K., Erdjument-Bromage H.,
RA   Tempst P., Gilliland D.G., Zhang Y., Kaelin W.G. Jr.;
RT   "The retinoblastoma binding protein RBP2 is an H3K4 demethylase.";
RL   Cell 128:889-900(2007).
RN   [6]
RP   FUNCTION.
RX   PubMed=17320161; DOI=10.1016/j.cell.2007.02.003;
RA   Christensen J., Agger K., Cloos P.A.C., Pasini D., Rose S.,
RA   Sennels L., Rappsilber J., Hansen K.H., Salcini A.E., Helin K.;
RT   "RBP2 belongs to a family of demethylases, specific for tri-and
RT   dimethylated lysine 4 on histone 3.";
RL   Cell 128:1063-1076(2007).
RN   [7]
RP   SUBCELLULAR LOCATION, DOMAIN GSGFP MOTIF, AND INTERACTION WITH SUZ12.
RX   PubMed=20064375; DOI=10.1016/j.cell.2009.12.002;
RA   Peng J.C., Valouev A., Swigut T., Zhang J., Zhao Y., Sidow A.,
RA   Wysocka J.;
RT   "Jarid2/Jumonji coordinates control of PRC2 enzymatic activity and
RT   target gene occupancy in pluripotent cells.";
RL   Cell 139:1290-1302(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1111, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-
CC       4' of histone H3, thereby playing a central role in histone code.
CC       Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36',
CC       H3 'Lys-79' or H4 'Lys-20'. Demethylates trimethylated and
CC       dimethylated but not monomethylated H3 'Lys-4'. May stimulate
CC       transcription mediated by nuclear receptors. Involved in
CC       transcriptional regulation of Hox proteins during cell
CC       differentiation. May participate in transcriptional repression of
CC       cytokines such as CXCL12.
CC   -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity).
CC   -!- SUBUNIT: Interacts with RB1, ESR1, MYC, MYCN and LMO2 (By
CC       similarity). Interacts with SUZ12; the interaction is direct.
CC   -!- INTERACTION:
CC       Q80U70:Suz12; NbExp=2; IntAct=EBI-2531441, EBI-2526494;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity). Nucleus.
CC       Note=Occupies promoters of genes involved in RNA metabolism and
CC       mitochondrial function.
CC   -!- DOMAIN: The GSGFP motif is required for the interaction with
CC       SUZ12.
CC   -!- DISRUPTION PHENOTYPE: Mice are grossly normal, except that they
CC       exhibit behavioral abnormalities when held upside down by the
CC       tail, and slight hematological defects.
CC   -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC   -!- SIMILARITY: Contains 1 ARID domain.
CC   -!- SIMILARITY: Contains 1 JmjC domain.
CC   -!- SIMILARITY: Contains 1 JmjN domain.
CC   -!- SIMILARITY: Contains 3 PHD-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE22414.1; Type=Erroneous initiation;
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DR   EMBL; AC155720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC078896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK135085; BAE22414.1; ALT_INIT; mRNA.
DR   EMBL; AK144877; BAE26113.1; -; mRNA.
DR   EMBL; AK166055; BAE38548.1; -; mRNA.
DR   EMBL; BC080691; AAH80691.1; ALT_TERM; mRNA.
DR   IPI; IPI00849089; -.
DR   RefSeq; NP_666109.2; NM_145997.2.
DR   UniGene; Mm.404761; -.
DR   UniGene; Mm.463658; -.
DR   ProteinModelPortal; Q3UXZ9; -.
DR   SMR; Q3UXZ9; 84-175, 290-620, 1161-1222, 1608-1659.
DR   IntAct; Q3UXZ9; 2.
DR   STRING; Q3UXZ9; -.
DR   PhosphoSite; Q3UXZ9; -.
DR   PRIDE; Q3UXZ9; -.
DR   Ensembl; ENSMUST00000100996; ENSMUSP00000098558; ENSMUSG00000030180.
DR   GeneID; 214899; -.
DR   KEGG; mmu:214899; -.
DR   UCSC; uc009dni.1; mouse.
DR   CTD; 214899; -.
DR   MGI; MGI:2136980; Kdm5a.
DR   eggNOG; roNOG11427; -.
DR   InParanoid; Q3UXZ9; -.
DR   NextBio; 374501; -.
DR   ArrayExpress; Q3UXZ9; -.
DR   Bgee; Q3UXZ9; -.
DR   CleanEx; MM_RBP2; -.
DR   Genevestigator; Q3UXZ9; -.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR001606; ARID/BRIGHT_DNA-bd.
DR   InterPro; IPR013637; PLU-1.
DR   InterPro; IPR013129; TF_JmjC.
DR   InterPro; IPR003347; TF_JmjC_AAH.
DR   InterPro; IPR003349; TF_JmjN.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR004198; Znf_C5HC2.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:1.10.150.60; ARID; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 3.
DR   Pfam; PF01388; ARID; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF02375; JmjN; 1.
DR   Pfam; PF00628; PHD; 2.
DR   Pfam; PF08429; PLU-1; 1.
DR   Pfam; PF02928; zf-C5HC2; 1.
DR   SMART; SM00501; BRIGHT; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SMART; SM00545; JmjN; 1.
DR   SMART; SM00249; PHD; 3.
DR   SUPFAM; SSF46774; ARID; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 3.
DR   PROSITE; PS51011; ARID; 1.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS51183; JMJN; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 2.
DR   PROSITE; PS50016; ZF_PHD_2; 3.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Developmental protein; Dioxygenase;
KW   Direct protein sequencing; Iron; Metal-binding; Nucleus;
KW   Oxidoreductase; Phosphoprotein; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1   1690       Lysine-specific demethylase 5A.
FT                                /FTId=PRO_0000292411.
FT   DOMAIN       19     60       JmjN.
FT   DOMAIN       84    174       ARID.
FT   DOMAIN      437    603       JmjC.
FT   ZN_FING     293    343       PHD-type 1.
FT   ZN_FING    1153   1210       PHD-type 2.
FT   ZN_FING    1599   1653       PHD-type 3.
FT   REGION     1622   1690       Interaction with LMO2 (By similarity).
FT   MOTIF       419    423       GSGFP motif.
FT   COMPBIAS   1484   1579       Lys-rich.
FT   METAL       483    483       Iron; catalytic (By similarity).
FT   METAL       486    486       Iron; catalytic (By similarity).
FT   METAL       571    571       Iron; catalytic (By similarity).
FT   MOD_RES    1111   1111       Phosphoserine.
FT   MOD_RES    1331   1331       Phosphoserine (By similarity).
FT   MOD_RES    1343   1343       Phosphothreonine (By similarity).
FT   MOD_RES    1345   1345       Phosphoserine (By similarity).
FT   MOD_RES    1598   1598       Phosphoserine (By similarity).
FT   MOD_RES    1603   1603       Phosphoserine (By similarity).
FT   MOD_RES    1666   1666       Phosphoserine (By similarity).
FT   CONFLICT     10     10       A -> S (in Ref. 2; BAE38548).
FT   CONFLICT     14     14       V -> R (in Ref. 2; BAE38548).
FT   CONFLICT     17     17       P -> A (in Ref. 2; BAE38548).
FT   CONFLICT     24     24       P -> A (in Ref. 2; BAE38548).
FT   CONFLICT    544    544       V -> A (in Ref. 2; BAE38548).
FT   CONFLICT   1272   1272       A -> P (in Ref. 2; BAE22414).
SQ   SEQUENCE   1690 AA;  192216 MW;  EFCF56AAAA51F0FC CRC64;
     MASVGPGGYA AEFVPPPECP VFEPSWEEFT DPLSFIGRIR PFAEKTGICK IRPPKDWQPP
     FACEVKTFRF TPRVQRLNEL EAMTRVRLDF LDQLAKFWEL QGSTLKIPVV ERKILDLYAL
     SKIVASKGGF EIVTKEKKWS KVGSRLGYLP GKGTGSLLKS HYERILYPYE LFQSGVSLMG
     VQMPDLDLKE KVEAEVLSTD IQPSPERGTR MNIPPKRTRR VKSQSDSGEV NRNTELKKLQ
     IFGAGPKVVG LAVGAKDKED EVTRRRKVTN RSDAFNMQMR QRKGTLSVNF VDLYVCMFCG
     RGNNEDKLLL CDGCDDSYHT FCLLPPLPDV PKGDWRCPKC VAEECNKPRE AFGFEQAVRE
     YTLQSFGEMA DNFKSDYFNM PVHMVPTELV EKEFWRLVSS IEEDVIVEYG ADISSKDFGS
     GFPKKDGQRK MLPEEEEYAL SGWNLNNMPV LEQSVLAHIN VDISGMKVPW LYVGMCFSSF
     CWHIEDHWSY SINYLHWGEP KTWYGVPSHA AEQLEEVMRE LAPELFESQP DLLHQLVTIM
     NPNVLMEHGV PVYRTNQCAG EFVVTFPRAY HSGFNQGYNF AEAVNFCTAD WLPIGRQCVN
     HYRRLRRHCV FSHEELIFKM AADPECLDVG LAAMVCKELT LMTEEETRLR ESVVQMGVVM
     SEEEVFELVP DDERQCSACR TTCFLSALTC SCNPERLVCL YHPTDLCSCP MQNKCLRYRY
     PLEDLPSLLY GVKVRAQSYD TWVNRVTEAL SASFNHKKDL IELRVMLEDA EDRKYPENDL
     FRKLRDAVKE AETCGSVAQL LLSKKQKHRQ SSDSGKTRTK LTVEELKAFV QQLVSLPCVI
     SQTRQVKNLL DDVEEFHERA QEAMMDETPD SSKLQMLIDM GSSLYVELPE LPRLKQELQQ
     ARWLDEVRLT LSDPQQVTLD VMKKLIDSGV GLAPHHAVEK AMAELQELLT VSERWEEKAK
     VCLQARPRHS MANLENIVNE AKNIPAFLPN VLSLKEALQK AREWTAKVEA IQSGNNYAYL
     EQLESLSAKG RPIPVRLDAL PQVESQVAAA RAWRERTGRT FLKKNSSHTL LQVLSPRTDI
     GVYGSGKNRR KKVKEIIEKE KEKDLDLEPL SDLEEGLEES RDTAMVVAVF KEREQKEIEA
     MHSLRAANLA KMTIVERIEE VKFCICRKTA SGFMLQCELC KDWFHNSCVP LPKSSSQKKG
     SSWQAKDVKF LCPLCMRSRR PRLETILSLL VSLQKLPVRL PEGEALQCLT ERAMSWQDKA
     RQALATDELS SALAKLSVLS QRMVEQAARE KTEKIISAEL QKAAANPDLQ GHLPSFQQSA
     FNRVVSSVSS SPHQTMDYDD EETDSDEDIR ETYGYDMKDT ASVKSSSSLE PNLFCDEEIP
     IKSEEVVTHM WTAPSFCAEH AYSSASKSCS QGSSTPRKQP RKSPLVPRSL EPPVLELSPG
     AKAQLEELMM VGDLLEVSLD ETQHIWRILQ ATHPPSEDRF LHIMEDDSIE EKPLKMKGKD
     SSEKKRKRKL EKVEQLFGEG KQKTKELKKI DKPKKKKLKL NVDKSKELNK LAKKLAKEEE
     RKKKKEKAAA AKVELVKEST EKKRERKVLD IPSKYDWSGA EESDDENAVC AAQNCQRPCK
     DKVDWVQCDG GCDEWFHQVC VGVSAEMAEN EDYICINCAK KQGPDSPGQA PPPPFLMSYK
     LPMEDLKETS
//
ID   Q3UY32_MOUSE            Unreviewed;       136 AA.
AC   Q3UY32;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 35.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Snapin; Synonyms=Snapap;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK135006; BAE22381.1; -; mRNA.
DR   IPI; IPI00130554; -.
DR   UniGene; Mm.331182; -.
DR   STRING; Q3UY32; -.
DR   Ensembl; ENSMUST00000149884; ENSMUSP00000122090; ENSMUSG00000001018.
DR   MGI; MGI:1333745; Snapin.
DR   eggNOG; roNOG16190; -.
DR   HOVERGEN; HBG056744; -.
DR   InParanoid; Q3UY32; -.
DR   ArrayExpress; Q3UY32; -.
DR   Bgee; Q3UY32; -.
DR   Genevestigator; Q3UY32; -.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   InterPro; IPR017246; Snapin.
DR   PIRSF; PIRSF037631; Snapin; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   136 AA;  14962 MW;  C8190DAAD2C8F1FA CRC64;
     MAAADSAAVS GAGTPVAGPT GRDLFAEGLL EFLRPAVQQL DSHVHAVRES QVELREQIDN
     LATELCRINE DQKVALDLDP YVKKLLNARR RVVLVNNILQ NAQERLRRLN HSVAKETARR
     RAMLDSGVYP PGSPSK
//
ID   Q3UY58_MOUSE            Unreviewed;       181 AA.
AC   Q3UY58;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-FEB-2011, entry version 49.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Farp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- SIMILARITY: Contains 1 FERM domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK134958; BAE22355.1; -; mRNA.
DR   IPI; IPI00853863; -.
DR   UniGene; Mm.223980; -.
DR   Ensembl; ENSMUST00000026635; ENSMUSP00000026635; ENSMUSG00000025555.
DR   Ensembl; ENSMUST00000135010; ENSMUSP00000116985; ENSMUSG00000025555.
DR   MGI; MGI:2446173; Farp1.
DR   eggNOG; roNOG14658; -.
DR   GeneTree; ENSGT00600000084063; -.
DR   HOVERGEN; HBG096318; -.
DR   InParanoid; Q3UY58; -.
DR   ArrayExpress; Q3UY58; -.
DR   Bgee; Q3UY58; -.
DR   Genevestigator; Q3UY58; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0019898; C:extrinsic to membrane; IEA:InterPro.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR000798; Ez/rad/moesin.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   1: Evidence at protein level;
FT   NON_TER     181    181
SQ   SEQUENCE   181 AA;  20389 MW;  665579ECD3633CC5 CRC64;
     MGEIEQKPTP ASRLGAPENS GISTLERGQK PPPTPSGKLM TVKIQMLDDT QEAFEVPQRA
     PGKVLFDAVC NHLNLVEGDY FGLEFPDHRK IVVWLDLLKP IVKQIRRPKH VVVKFVVKFF
     PPDHTQLQEE LTRYLFALQV KQDLAQGRLT CNDTSAALLI SHIVKSEIGD FDEALDREHL
     A
//
ID   Q3UY82_MOUSE            Unreviewed;       251 AA.
AC   Q3UY82;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 28.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Rprd2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK134893; BAE22331.1; -; mRNA.
DR   IPI; IPI00762512; -.
DR   UniGene; Mm.196275; -.
DR   Ensembl; ENSMUST00000090791; ENSMUSP00000088297; ENSMUSG00000028106.
DR   Ensembl; ENSMUST00000098855; ENSMUSP00000096454; ENSMUSG00000028106.
DR   UCSC; uc008qla.1; mouse.
DR   MGI; MGI:1922387; Rprd2.
DR   eggNOG; roNOG07446; -.
DR   InParanoid; Q3UY82; -.
DR   ArrayExpress; Q3UY82; -.
DR   Bgee; Q3UY82; -.
DR   Genevestigator; Q3UY82; -.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   251 AA;  25901 MW;  A6476F8B37932AFB CRC64;
     NRVNNLKKKL DQLKSTLPDP EESPVPSPSM DAPSPTGSES PFQGMGGEEP QSPAMESDKS
     ATPEPVTDNR DVEDMELSDV EDDGSKIIVE DRKEKPVEKP AVSTGVPTKS TESVSKASPC
     APPSVPTTAA PLLPKPLSTA LLSPSPTLVL PNLANVDLAK ISSILSSLTS VMKNTGVSSA
     SRPSPGIPTS PSNLSSGLKT PAPATTPSHN PLANILSKVE ITPESILSAL SKTQTQSAPA
     LQGKLTCARG T
//
ID   PPM1H_MOUSE             Reviewed;         513 AA.
AC   Q3UYC0; Q3UD05; Q3V3H5; Q3V3Y7; Q571C9; Q7TMU7; Q8BYE6;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 47.
DE   RecName: Full=Protein phosphatase 1H;
DE            EC=3.1.3.16;
GN   Name=Ppm1h; Synonyms=Kiaa1157;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow, Head, Medulla oblongata, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Pancreatic islet;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 90-513 (ISOFORM 1).
RC   STRAIN=C57BL/6NCr; TISSUE=Hematopoietic stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UYC0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UYC0-2; Sequence=VSP_025121, VSP_025122;
CC   -!- SIMILARITY: Belongs to the PP2C family.
CC   -!- SIMILARITY: Contains 1 PP2C-like domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90185.1; Type=Erroneous initiation;
CC       Sequence=BAE29457.1; Type=Erroneous initiation;
CC       Sequence=BAE43270.1; Type=Erroneous initiation;
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DR   EMBL; AK029461; BAE43270.1; ALT_INIT; mRNA.
DR   EMBL; AK040194; BAC30536.1; -; mRNA.
DR   EMBL; AK040207; BAE43308.1; -; mRNA.
DR   EMBL; AK134804; BAE22292.1; -; mRNA.
DR   EMBL; AK150309; BAE29457.1; ALT_INIT; mRNA.
DR   EMBL; AK220260; BAD90185.1; ALT_INIT; mRNA.
DR   EMBL; BC052910; AAH52910.1; -; mRNA.
DR   IPI; IPI00620040; -.
DR   IPI; IPI00845733; -.
DR   RefSeq; NP_001103688.1; NM_001110218.1.
DR   RefSeq; NP_795893.2; NM_176919.4.
DR   UniGene; Mm.478875; -.
DR   ProteinModelPortal; Q3UYC0; -.
DR   PhosphoSite; Q3UYC0; -.
DR   PRIDE; Q3UYC0; -.
DR   Ensembl; ENSMUST00000067918; ENSMUSP00000066561; ENSMUSG00000034613.
DR   GeneID; 319468; -.
DR   KEGG; mmu:319468; -.
DR   UCSC; uc007hgh.1; mouse.
DR   CTD; 319468; -.
DR   MGI; MGI:2442087; Ppm1h.
DR   eggNOG; roNOG04840; -.
DR   GeneTree; ENSGT00530000063231; -.
DR   HOVERGEN; HBG105802; -.
DR   InParanoid; Q3UYC0; -.
DR   OMA; SPDEVEC; -.
DR   OrthoDB; EOG4PG60S; -.
DR   BRENDA; 3.1.3.16; 244.
DR   NextBio; 394782; -.
DR   ArrayExpress; Q3UYC0; -.
DR   Bgee; Q3UYC0; -.
DR   CleanEx; MM_PPM1H; -.
DR   Genevestigator; Q3UYC0; -.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR001932; PP2C-like.
DR   InterPro; IPR014045; PP2C_N.
DR   InterPro; IPR015655; Protein_Pase_2C.
DR   Gene3D; G3DSA:3.60.40.10; PP2C-related; 3.
DR   PANTHER; PTHR13832; PP2C; 1.
DR   Pfam; PF00481; PP2C; 2.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-related; 1.
DR   PROSITE; PS01032; PP2C; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; Phosphoprotein; Protein phosphatase.
FT   CHAIN         1    513       Protein phosphatase 1H.
FT                                /FTId=PRO_0000286604.
FT   DOMAIN      136    506       PP2C-like.
FT   MOD_RES     118    118       Phosphoserine.
FT   MOD_RES     123    123       Phosphoserine.
FT   MOD_RES     210    210       Phosphoserine (By similarity).
FT   MOD_RES     220    220       Phosphoserine.
FT   MOD_RES     223    223       Phosphothreonine (By similarity).
FT   MOD_RES     418    418       Phosphotyrosine (By similarity).
FT   MOD_RES     421    421       Phosphoserine (By similarity).
FT   VAR_SEQ     466    469       YTLA -> FVPL (in isoform 2).
FT                                /FTId=VSP_025121.
FT   VAR_SEQ     470    513       Missing (in isoform 2).
FT                                /FTId=VSP_025122.
FT   CONFLICT     90     93       THNE -> EVIP (in Ref. 3; AAH52910).
FT   CONFLICT    130    130       L -> R (in Ref. 2; BAD90185).
FT   CONFLICT    168    168       H -> P (in Ref. 3; AAH52910).
FT   CONFLICT    198    198       T -> A (in Ref. 1; BAE43308).
FT   CONFLICT    260    260       S -> G (in Ref. 1; BAE29457).
FT   CONFLICT    456    456       P -> L (in Ref. 3; AAH52910).
SQ   SEQUENCE   513 AA;  56380 MW;  27885A4519A0F0DB CRC64;
     MLTRVKSAVA NFMGGIMAGS SGSEHGGSGC GGSDLPLRFP YGRPEFLGLS QDEVECSADH
     IARPILILKE TRRLPWATGY AEVINAGKST HNEDQASCEV LTVKKKAGTI TSTPNRNSKR
     RSSLPNGEGL QLKENSESEG ISCHYWSLFD GHAGSGAAVV ASRLLQHHIT QQLQDIVEIL
     KNSAILPPTC LGEEPESTPA HGRTLTRAAS LRGGVGAPGS PSTPPTRFFT EKKIPHECLV
     IGALESAFKE MDLQIERERS AYNISGGCTA LIVVCLLGKL YVANAGDSRA IIIRNGEIIP
     MSSEFTPETE RQRLQYLAFM QPHLLGNEFT HLEFPRRVQR KELGKKMLYR DFNMTGWAYK
     TIEDDDLKFP LIYGEGKKAR VMATIGVTRG LGDHDLKVHD SNIYIKPFLS SAPEVRVYDL
     SRYEHGADDV LILATDGLWD VLSNEEVAEA ITQFLPNCDP DDPHRYTLAA QDLVMRARGV
     LKDRGWRISN DRLGSGDDIS VYVIPLIHGN KLS
//
ID   RGL3_MOUSE              Reviewed;         709 AA.
AC   Q3UYI5; Q6KAR7; Q8BKD3; Q924M8; Q9DBL8; Q9JID4;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Ral guanine nucleotide dissociation stimulator-like 3;
DE            Short=RalGDS-like 3;
DE   AltName: Full=RalGDS-related effector protein of M-Ras;
DE   AltName: Full=Ras pathway modulator;
DE            Short=RPM;
GN   Name=Rgl3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
RP   RIT1 AND HRAS, DOMAIN, AND TISSUE SPECIFICITY.
RX   MEDLINE=20418060; PubMed=10869344; DOI=10.1074/jbc.M002241200;
RA   Shao H., Andres D.A.;
RT   "A novel RalGEF-like protein, RGL3, as a candidate effector for rit
RT   and Ras.";
RL   J. Biol. Chem. 275:26914-26924(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
RP   HRAS AND MRAS, AND TISSUE SPECIFICITY.
RX   MEDLINE=21214408; PubMed=11313946; DOI=10.1038/sj.onc.1204053;
RA   Ehrhardt G.R., Korherr C., Wieler J.S., Knaus M., Schrader J.W.;
RT   "A novel potential effector of M-Ras and p21 Ras negatively regulates
RT   p21 Ras-mediated gene induction and cell growth.";
RL   Oncogene 20:188-197(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Eye, Liver, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 180-684 (ISOFORM 1).
RC   STRAIN=ICR; TISSUE=Embryonic tail;
RX   PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of FLJ genes:
RT   the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:127-135(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 362-368, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506; SER-510; SER-568
RP   AND SER-572, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Guanine nucleotide exchange factor (GEF) for Ral-A.
CC       Potential effector of GTPase HRas and Ras-related protein M-Ras.
CC       Negatively regulates Elk-1-dependent gene induction downstream of
CC       HRas and MEKK1.
CC   -!- SUBUNIT: Interacts with GTP-bound forms of RIT1, HRAS and MRAS.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UYI5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UYI5-2; Sequence=VSP_028471, VSP_028472, VSP_028473,
CC                                  VSP_028474;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in
CC       the liver and kidney.
CC   -!- DOMAIN: The Ras-associating domain plays a central role in the
CC       activation of Ral-A GDP/GTP exchange activity.
CC   -!- SIMILARITY: Contains 1 N-terminal Ras-GEF domain.
CC   -!- SIMILARITY: Contains 1 Ras-associating domain.
CC   -!- SIMILARITY: Contains 1 Ras-GEF domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC35425.1; Type=Frameshift; Positions=36;
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DR   EMBL; AF237669; AAF78208.1; -; mRNA.
DR   EMBL; AF239661; AAK91126.1; -; mRNA.
DR   EMBL; AK004876; BAB23634.1; -; mRNA.
DR   EMBL; AK053550; BAC35425.1; ALT_FRAME; mRNA.
DR   EMBL; AK134654; BAE22227.1; -; mRNA.
DR   EMBL; AK131140; BAD21390.1; -; Transcribed_RNA.
DR   IPI; IPI00119850; -.
DR   IPI; IPI00312702; -.
DR   RefSeq; NP_076111.2; NM_023622.4.
DR   UniGene; Mm.110594; -.
DR   ProteinModelPortal; Q3UYI5; -.
DR   SMR; Q3UYI5; 58-511, 609-698.
DR   STRING; Q3UYI5; -.
DR   PhosphoSite; Q3UYI5; -.
DR   PRIDE; Q3UYI5; -.
DR   Ensembl; ENSMUST00000045193; ENSMUSP00000038791; ENSMUSG00000040146.
DR   Ensembl; ENSMUST00000045726; ENSMUSP00000035726; ENSMUSG00000040146.
DR   GeneID; 71746; -.
DR   KEGG; mmu:71746; -.
DR   CTD; 71746; -.
DR   MGI; MGI:1918996; Rgl3.
DR   eggNOG; roNOG07224; -.
DR   GeneTree; ENSGT00560000076759; -.
DR   HOGENOM; HBG444535; -.
DR   HOVERGEN; HBG005864; -.
DR   InParanoid; Q3UYI5; -.
DR   OMA; AHSDLGS; -.
DR   OrthoDB; EOG4TXBRM; -.
DR   NextBio; 334391; -.
DR   ArrayExpress; Q3UYI5; -.
DR   Bgee; Q3UYI5; -.
DR   Genevestigator; Q3UYI5; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0008321; F:Ral guanyl-nucleotide exchange factor activity; IDA:MGI.
DR   GO; GO:0017016; F:Ras GTPase binding; IDA:MGI.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:MGI.
DR   InterPro; IPR000159; Ras-assoc.
DR   InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR   InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR   InterPro; IPR008937; Ras_GEF.
DR   InterPro; IPR001895; RasGRF_CDC25.
DR   Gene3D; G3DSA:1.10.840.10; RasGRF_CDC25; 1.
DR   PANTHER; PTHR23113; Ras_GEF; 1.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   SMART; SM00314; RA; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00229; RasGEFN; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS00720; RASGEF; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50212; RASGEF_NTER; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing;
KW   Guanine-nucleotide releasing factor; Phosphoprotein.
FT   CHAIN         1    709       Ral guanine nucleotide dissociation
FT                                stimulator-like 3.
FT                                /FTId=PRO_0000306800.
FT   DOMAIN       64    201       N-terminal Ras-GEF.
FT   DOMAIN      248    503       Ras-GEF.
FT   DOMAIN      612    699       Ras-associating.
FT   REGION      611    706       Interaction with HRAS, MRAS and RIT1.
FT   COMPBIAS    114    123       Pro-rich.
FT   COMPBIAS    535    598       Pro-rich.
FT   MOD_RES     506    506       Phosphoserine.
FT   MOD_RES     510    510       Phosphoserine.
FT   MOD_RES     568    568       Phosphoserine.
FT   MOD_RES     572    572       Phosphoserine.
FT   VAR_SEQ       1     99       Missing (in isoform 2).
FT                                /FTId=VSP_028471.
FT   VAR_SEQ     100    125       RAFVPTARVLGFLLPPPPPPPPPPAG -> MAPCTASPCGG
FT                                SAASARPQRGLEKAR (in isoform 2).
FT                                /FTId=VSP_028472.
FT   VAR_SEQ     442    442       G -> V (in isoform 2).
FT                                /FTId=VSP_028473.
FT   VAR_SEQ     443    709       Missing (in isoform 2).
FT                                /FTId=VSP_028474.
FT   CONFLICT    179    179       A -> V (in Ref. 1; AAF78208).
FT   CONFLICT    321    321       R -> K (in Ref. 3; BAB23634).
FT   CONFLICT    478    478       I -> N (in Ref. 3; BAE22227).
FT   CONFLICT    613    613       A -> T (in Ref. 3; BAC35425).
FT   CONFLICT    626    626       N -> K (in Ref. 3; BAC35425).
SQ   SEQUENCE   709 AA;  77945 MW;  60F7CEA71873E609 CRC64;
     MERTAGKELA LAPLQDWGEE TEDGAVYSVS LRRQRSQRST PERSGEGQTP IPATDTFLHY
     RTSKVRALRA ARLERLVHEL VSGDREQDPG FVPAFLATHR AFVPTARVLG FLLPPPPPPP
     PPPAGVDSKR TEGQDLNFSK NLRAVVSVLG SWLRNHPQDF RDPPDHQNLG NVRIFLGWAA
     PGGAEAREAE KLLEDFLKEA KGEQTEEEKR LAWSGPPRIA QTPGSEFAED CVEEEGPSSE
     GPELLDFSVD DVAEQLTLMD VELFLRVRSC ECLGSMWSQR DRPGAAGISP TVRATVAQFN
     TVTGCVLGSV LAAPGLAASQ RAQRIEKWIR IAQRCRELRN FSSLRAILSA LQSNPIYRLK
     RSWGAVSREP LSVFRKLSQI FSDEDNHLSS RAILSQEETT EDDDCPSGSL PSKLPPGPVP
     YLGTFLTDLV MLDTALPDTL KGNLINFEKR RKEWEILARI QQLQQRCQRY SLSPRPPILA
     ALRAQRQLSE EQSYRVSRVI EPPAASCPSS PRIRRRISLT KRLSAKLSRE KNSSPGGSPG
     DPSSPTSSVS PGSPPSSPRN REPPPPGSPP ASPGPQSPST KLSLTMDPPG PWPVTLTPSS
     SRVPLLGQQT SEARVIRVSI NNNHGNLYRS ILLTCQDKAP SVVQRALEKH NVPQPWARDY
     QLFQVLPGDR ELLIPDGANV FYAMSPAAPG DFLLRRKEGT GHTLSASPT
//
ID   NCBP1_MOUSE             Reviewed;         790 AA.
AC   Q3UYV9; B1AWH4; Q3TEM1; Q7TNE8;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 2.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Nuclear cap-binding protein subunit 1;
DE   AltName: Full=80 kDa nuclear cap-binding protein;
DE            Short=CBP80;
DE            Short=NCBP 80 kDa subunit;
GN   Name=Ncbp1; Synonyms=Cbp80;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   IDENTIFICATION IN A U SNRNA EXPORT COMPLEX WITH RNUXA/PHAX; NCBP2;
RP   RAN; XPO1 AND M7G-CAPPED RNA.
RX   MEDLINE=20246506; PubMed=10786834; DOI=10.1016/S0092-8674(00)80829-6;
RA   Ohno M., Segref A., Bachi A., Wilm M., Mattaj I.W.;
RT   "PHAX, a mediator of U snRNA nuclear export whose activity is
RT   regulated by phosphorylation.";
RL   Cell 101:187-198(2000).
RN   [6]
RP   INTERACTION WITH RNUXA/PHAX.
RX   PubMed=11333016; DOI=10.1017/S1355838201002278;
RA   Segref A., Mattaj I.W., Ohno M.;
RT   "The evolutionarily conserved region of the U snRNA export mediator
RT   PHAX is a novel RNA-binding domain that is essential for U snRNA
RT   export.";
RL   RNA 7:351-360(2001).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   FUNCTION IN MIRNAS BIOGENESIS, AND INTERACTION WITH SRRT AND DROSHA.
RX   PubMed=19632182; DOI=10.1016/j.cell.2009.04.046;
RA   Gruber J.J., Zatechka D.S., Sabin L.R., Yong J., Lum J.J., Kong M.,
RA   Zong W.-X., Zhang Z., Lau C.-K., Rawlings J., Cherry S., Ihle J.N.,
RA   Dreyfuss G., Thompson C.B.;
RT   "Ars2 links the nuclear cap-binding complex to RNA interference and
RT   cell proliferation.";
RL   Cell 138:328-339(2009).
CC   -!- FUNCTION: Component of the cap-binding complex (CBC), which binds
CC       co-transcriptionally to the 5' cap of pre-mRNAs and is involved in
CC       various processes such as pre-mRNA splicing, translation
CC       regulation, nonsense-mediated mRNA decay, RNA-mediated gene
CC       silencing (RNAi) by microRNAs (miRNAs) and mRNA export. The CBC
CC       complex is involved in mRNA export from the nucleus via its
CC       interaction with THOC4/ALY, leading to the recruitment of the mRNA
CC       export machinery to the 5' end of mRNA and to mRNA export in a 5'
CC       to 3' direction through the nuclear pore. The CBC complex is also
CC       involved in mediating U snRNA and intronless mRNAs export from the
CC       nucleus. The CBC complex is essential for a pioneer round of mRNA
CC       translation, before steady state translation when the CBC complex
CC       is replaced by cytoplasmic cap-binding protein eIF4E. The pioneer
CC       round of mRNA translation mediated by the CBC complex plays a
CC       central role in nonsense-mediated mRNA decay (NMD), NMD only
CC       taking place in mRNAs bound to the CBC complex, but not on eIF4E-
CC       bound mRNAs. The CBC complex enhances NMD in mRNAs containing at
CC       least one exon-junction complex (EJC) via its interaction with
CC       UPF1, promoting the interaction between UPF1 and UPF2. The CBC
CC       complex is also involved in 'failsafe' NMD, which is independent
CC       of the EJC complex, while it does not participate in Staufen-
CC       mediated mRNA decay (SMD). During cell proliferation, the CBC
CC       complex is also involved in microRNAs (miRNAs) biogenesis via its
CC       interaction with SRRT/ARS2 and is required for miRNA-mediated RNA
CC       interference. The CBC complex also acts as a negative regulator of
CC       PARN, thereby acting as an inhibitor of mRNA deadenylation. In the
CC       CBC complex, NCBP1/CBP80 does not bind directly capped RNAs
CC       (m7GpppG-capped RNA) but is required to stabilize the movement of
CC       the N-terminal loop of NCBP2/CBP20 and lock the CBC into a high
CC       affinity cap-binding state with the cap structure.
CC   -!- SUBUNIT: Component of the nuclear cap-binding complex (CBC), a
CC       heterodimer composed of NCBP1/CBP80 and NCBP2/CBP20 that interacts
CC       with m7GpppG-capped RNA. Heterodimer with NCBP2. Is part of the
CC       exon junction complex (EJC) containing NCBP1, NCBP2, RNPS1, RBM8A,
CC       SRRM1, NXF1, UPF3B, UPF2, THOC4 and/or REFBP2. Identified in a
CC       mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG,
CC       HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU,
CC       HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4,
CC       PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2,
CC       YBX1 and untranslated mRNAs. Interacts with SRRT/ARS2, EIF4G2,
CC       HNRNPF, IGF2BP1, HNRNPH1, KIAA0427/CTIF, PARN, DROSHA, UPF1 and
CC       THOC4. May interact with EIF4G1; the interaction is however
CC       controversial (By similarity). Found in a U snRNA export complex
CC       with RNUXA/PHAX, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-
CC       capped RNA. Interaction with RNUXA/PHAX.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity). Note=Localized in cytoplasmic mRNP granules
CC       containing untranslated mRNAs (By similarity).
CC   -!- SIMILARITY: Belongs to the NCBP1 family.
CC   -!- SIMILARITY: Contains 1 MIF4G domain.
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DR   EMBL; AK134334; BAE22102.1; -; mRNA.
DR   EMBL; AK169557; BAE41227.1; -; mRNA.
DR   EMBL; AL929438; CAM14995.1; -; Genomic_DNA.
DR   EMBL; AL732615; CAM14995.1; JOINED; Genomic_DNA.
DR   EMBL; AL732615; CAM17033.1; -; Genomic_DNA.
DR   EMBL; AL929438; CAM17033.1; JOINED; Genomic_DNA.
DR   EMBL; CH466565; EDL02380.1; -; Genomic_DNA.
DR   EMBL; BC055777; AAH55777.1; -; mRNA.
DR   EMBL; BC138898; AAI38899.1; -; mRNA.
DR   IPI; IPI00458056; -.
DR   RefSeq; NP_001028373.2; NM_001033201.3.
DR   UniGene; Mm.389536; -.
DR   ProteinModelPortal; Q3UYV9; -.
DR   SMR; Q3UYV9; 2-790.
DR   STRING; Q3UYV9; -.
DR   PhosphoSite; Q3UYV9; -.
DR   PRIDE; Q3UYV9; -.
DR   Ensembl; ENSMUST00000030014; ENSMUSP00000030014; ENSMUSG00000028330.
DR   GeneID; 433702; -.
DR   KEGG; mmu:433702; -.
DR   UCSC; uc008stk.1; mouse.
DR   CTD; 433702; -.
DR   MGI; MGI:1891840; Ncbp1.
DR   GeneTree; ENSGT00390000001733; -.
DR   HOGENOM; HBG378185; -.
DR   HOVERGEN; HBG080328; -.
DR   InParanoid; Q3UYV9; -.
DR   OMA; LICRVGE; -.
DR   OrthoDB; EOG4RXXZK; -.
DR   NextBio; 408905; -.
DR   ArrayExpress; Q3UYV9; -.
DR   Bgee; Q3UYV9; -.
DR   Genevestigator; Q3UYV9; -.
DR   GermOnline; ENSMUSG00000028330; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0030529; C:ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0006370; P:mRNA capping; ISS:UniProtKB.
DR   GO; GO:0006379; P:mRNA cleavage; ISS:UniProtKB.
DR   GO; GO:0006406; P:mRNA export from nucleus; ISS:UniProtKB.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISS:UniProtKB.
DR   GO; GO:0031442; P:positive regulation of mRNA 3'-end processing; ISS:UniProtKB.
DR   GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR016021; MIF4-like_typ_1/2/3.
DR   InterPro; IPR015172; MIF4G-like_typ-1.
DR   InterPro; IPR015174; MIF4G-like_typ-2.
DR   InterPro; IPR003890; MIF4G-like_typ-3.
DR   Gene3D; G3DSA:1.25.40.180; MIF4-like_typ_1/2/3; 4.
DR   Pfam; PF02854; MIF4G; 1.
DR   Pfam; PF09088; MIF4G_like; 1.
DR   Pfam; PF09090; MIF4G_like_2; 1.
DR   SMART; SM00543; MIF4G; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Cytoplasm; mRNA capping; mRNA processing;
KW   mRNA splicing; mRNA transport; Nonsense-mediated mRNA decay; Nucleus;
KW   Phosphoprotein; RNA-mediated gene silencing; Translation regulation;
KW   Transport.
FT   CHAIN         1    790       Nuclear cap-binding protein subunit 1.
FT                                /FTId=PRO_0000239779.
FT   DOMAIN       28    240       MIF4G.
FT   COILED      643    713       Potential.
FT   MOTIF         3     20       Nuclear localization signal (Potential).
FT   MOD_RES       7      7       Phosphoserine (By similarity).
FT   MOD_RES      21     21       Phosphothreonine (By similarity).
FT   MOD_RES      22     22       Phosphoserine.
FT   MOD_RES     204    204       N6-acetyllysine (By similarity).
FT   MOD_RES     674    674       Phosphoserine (By similarity).
FT   MOD_RES     698    698       N6-acetyllysine (By similarity).
FT   CONFLICT    319    319       H -> R (in Ref. 1; BAE22102).
FT   CONFLICT    443    443       S -> R (in Ref. 1; BAE22102).
FT   CONFLICT    453    453       L -> I (in Ref. 1; BAE22102).
FT   CONFLICT    574    574       K -> Q (in Ref. 1; BAE22102).
SQ   SEQUENCE   790 AA;  91927 MW;  BE27F89BDBC19CF2 CRC64;
     MSRRRHSYEN DGGQPHKRRK TSDANETEDH LESLICKVGE KSACSLESNL EGLAGVLEAD
     LPNYKSKILR LLCTVARLLP EKLTIYTTLV GLLNARNYNF GGEFVEAMIR QLKESLKANN
     YNEAVYLVRF LSDLVNCHVI AAPSMVAMFE NFVSVTQEED VPQVRRDWYV YAFLSSLPWV
     GKELYEKKDA EMDRIFSTTE SYLKRRQKTH VPMLQVWTAD KPHPQEEYLD CLWAQIQKLK
     KDRWQERHIL RPYLAFDSIL CEALQHNLPP FTPPPHTEDS VYPMPRVIFR MFDYTDDPEG
     PVMPGSHSVE RFVIEENLHC IIKSYWKERK TCAAQLVSYP GKNKIPLNYH IVEVIFAELF
     QLPAPPHIDV MYTTLLIELC KLQPGSLPQV LAQATEMLYM RLDTMSTTCV DRFINWFSHH
     LSNFQFRWSW EDWSDCLTQD LESPKPKFVR EVLEKCMRLS YHQHILDIVP PTFSALCPAN
     PTCIYKYGDE SSNSLPGHSV ALCLSVAFKS KATNDEIFSI LKDVPNPNQV DDDDEGFRFN
     PLKIEVFVQT LLHLAAKSFS HSFSALAKFH EVFKTLAESD KGKLHVLRVM FEVWRNHPQM
     IAVLVDKMIR TQIVDCAAVA NWIFSSELSR DFTRLFVWEI LHSTIRKMNK HVLKIQKELE
     EAKEKLARQH KRRSDDDDRS SDRKDGALEE QIERLQEKVE AAQSEQKNLF LVIFQRFIMI
     LTEHLVRCET DGTSILTPWY KNCIERLQQI FLQHHQTIQQ YMVTLENLLF TAELDPHILA
     VFQQFCALQA
//
ID   Q3UYW7_MOUSE            Unreviewed;       830 AA.
AC   Q3UYW7;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Bms1; Synonyms=Bms1l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK134315; BAE22094.1; -; mRNA.
DR   IPI; IPI00453860; -.
DR   UniGene; Mm.25269; -.
DR   STRING; Q3UYW7; -.
DR   Ensembl; ENSMUST00000032237; ENSMUSP00000032237; ENSMUSG00000030138.
DR   MGI; MGI:2446132; Bms1.
DR   eggNOG; roNOG13882; -.
DR   HOVERGEN; HBG023890; -.
DR   InParanoid; Q3UYW7; -.
DR   OrthoDB; EOG4KWJS4; -.
DR   ArrayExpress; Q3UYW7; -.
DR   Bgee; Q3UYW7; -.
DR   Genevestigator; Q3UYW7; -.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:InterPro.
DR   InterPro; IPR012948; AARP2CN.
DR   InterPro; IPR000795; ProtSyn_GTP-bd.
DR   Pfam; PF08142; AARP2CN; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   SMART; SM00785; AARP2CN; 1.
PE   2: Evidence at transcript level;
KW   GTP-binding; Nucleotide-binding.
FT   NON_TER     830    830
SQ   SEQUENCE   830 AA;  92720 MW;  03A41F52F4DDB79E CRC64;
     METKDHKKHR KKHSGPKAEK KKKRHLQDLQ LGDEEDARKR NPKAFAVQSA VRMARSFHRT
     QDLKTKKHHI PVVDRTPLEP PPIVVVVMGP PKVGKSTLIR CLIRNFTRQK LSEIRGPVTI
     VSGKKRRLTI IECGCDINVM IDLAKVADLV LMLIDASFGF EMETFEFLNI CQVHGFPKIM
     GVLTHLDSFK HNKQLKKTKK RLKHRFWTEV YPGAKLFYLS GMVHGEYQNQ EIHNLGRFIT
     VMKFRPLTWQ TSHPYILADR MEDLTNPEAI RTNVKCDRKV SLYGYLRGAY LKNNSQIHMP
     GVGDFVASDV SFLPDPCALP EQQKKRCLNE KEKLVYAPLS GVGGVLYDKD AVYVDLGGSH
     GFQAAEETGP THELVQSLIS THASIDAKMA SSRVTLFSDS KPLGSEDIDN QGLWMPKEEK
     QVDVETGRVR RKAIFGDTED ESGDEESEDE EDMSEADGME PGSSDDEAEE AEEEGAESSS
     GNYMMGRGRK RPKLEEQEED SEADSPAFAD SDDDLERSSG GEEEAEEADE SSADGASTGE
     RDAGECGSVG EASEESPSAA HQWRPHADAQ KPSPVRKAAL TTSDSGHCTA EEAFPSEDES
     EDSELSAEEE DSDHREVRGK LAHPLRDSGQ KPASESLVDE TSDIESLLKE EEEYKEDNSS
     SVETSGALKW KEDLSRKAAE AFLRQQQAAP NLRKLIYGTV TEDNEDEDGD PAEELGGLFH
     VSQPDRGCKH KADSLDCSRF PVEAPHDWDL EEVMNSIRDC FVTGKWEDDK DAAKILAEEE
     ELYGDFEDLE TGDVHKGKPG PDTQSEDIEE EEVKEETDPS EEESARKKHL
//
ID   RBM40_MOUSE             Reviewed;         514 AA.
AC   Q3UZ01; Q3TTZ2; Q69Z94; Q80VS9; Q91YJ1; Q9CSC1;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=RNA-binding protein 40;
DE   AltName: Full=RNA-binding motif protein 40;
DE   AltName: Full=RNA-binding region-containing protein 3;
GN   Name=Rnpc3; Synonyms=Kiaa1839, Rbm40;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Skin, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 53-514 (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
CC   -!- FUNCTION: RNA-binding protein involved in pre-mRNA splicing.
CC       Participates in pre-mRNA U12-dependent splicing. Binds to the 3'-
CC       stem-loop of m(7)G-capped U12 snRNA (By similarity).
CC   -!- SUBUNIT: Component of the U11/U12 snRNPs that are part of the U12-
CC       type spliceosome. Found in a complex with m(7)G-capped U12 snRNA.
CC       Interacts with PDCD7 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UZ01-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UZ01-2; Sequence=VSP_029402;
CC   -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH16603.1; Type=Erroneous initiation;
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DR   EMBL; AK013288; BAB28770.3; -; mRNA.
DR   EMBL; AK134241; BAE22060.1; -; mRNA.
DR   EMBL; AK161063; BAE36180.1; -; mRNA.
DR   EMBL; BC016603; AAH16603.1; ALT_INIT; mRNA.
DR   EMBL; BC043695; AAH43695.1; -; mRNA.
DR   EMBL; AK173272; BAD32550.1; -; mRNA.
DR   IPI; IPI00831482; -.
DR   IPI; IPI00831582; -.
DR   RefSeq; NP_001033785.1; NM_001038696.1.
DR   RefSeq; NP_080319.2; NM_026043.3.
DR   UniGene; Mm.316928; -.
DR   HSSP; Q96IZ5; 2CPX.
DR   ProteinModelPortal; Q3UZ01; -.
DR   SMR; Q3UZ01; 23-104, 387-504.
DR   PRIDE; Q3UZ01; -.
DR   Ensembl; ENSMUST00000092154; ENSMUSP00000089792; ENSMUSG00000027981.
DR   Ensembl; ENSMUST00000106536; ENSMUSP00000102146; ENSMUSG00000027981.
DR   GeneID; 67225; -.
DR   KEGG; mmu:67225; -.
DR   CTD; 67225; -.
DR   MGI; MGI:1914475; Rnpc3.
DR   eggNOG; roNOG17654; -.
DR   GeneTree; ENSGT00530000063786; -.
DR   HOGENOM; HBG314728; -.
DR   HOVERGEN; HBG057088; -.
DR   InParanoid; Q3UZ01; -.
DR   OMA; RIMFDIR; -.
DR   OrthoDB; EOG46DM34; -.
DR   PhylomeDB; Q3UZ01; -.
DR   NextBio; 323936; -.
DR   ArrayExpress; Q3UZ01; -.
DR   Bgee; Q3UZ01; -.
DR   CleanEx; MM_RNPC3; -.
DR   Genevestigator; Q3UZ01; -.
DR   GO; GO:0005689; C:U12-type spliceosomal complex; ISS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Nucleus; Phosphoprotein; Repeat; RNA-binding.
FT   CHAIN         1    514       RNA-binding protein 40.
FT                                /FTId=PRO_0000311113.
FT   DOMAIN       27    102       RRM 1.
FT   DOMAIN      418    501       RRM 2.
FT   COMPBIAS    196    233       Pro-rich.
FT   MOD_RES     108    108       Phosphoserine (By similarity).
FT   VAR_SEQ     497    497       Missing (in isoform 2).
FT                                /FTId=VSP_029402.
FT   CONFLICT     41     41       E -> K (in Ref. 1; BAE22060).
FT   CONFLICT    261    261       M -> T (in Ref. 1; BAB28770).
FT   CONFLICT    422    422       V -> E (in Ref. 1; BAE22060).
SQ   SEQUENCE   514 AA;  57972 MW;  0FB772119ED29A0D CRC64;
     MAGPEPPMPL SRGGPGSASL SPPRGDRTLL VRHLPAELTA EEKEDLLKYF GAQSVRVLSD
     KGRLKHTAFA TFPNEKAAIK ALTRLHQLKL LGHTLVVEFA KEQDRVHSPC STSNTEKKKR
     LDDTVENDKE KKEPDILTVE NGIAPNHGLT FPLNSCLKYM YPPPSSTILA NIVNALASVP
     KFYVQVLHLM NKMNLPTPFG PITARPPMYE DYMPLHAPLP PTSPQPPEEP PLPDEDEDLS
     SKESEYESSD EEDRQRMNRL MELANLQPKR PKTEKPRHVR KKRKIKDMLN IPSSASHSLH
     PVLLPSDVFD QPQSVGNKKI EFNISTNMPA AFNKDLETQP NNEEENSDSP DTGLDSNTGF
     GKIFPKPNLN ITEEITEDSD EIPSQFISRK ELEKGRISRE EMETLSVFRS YEPGEPNCRI
     YVKNLARHVQ EKDLKFIFGR YVDFSSETQR IMFDIRLMKE GRMKGQAFVG LPNEKAAAKA
     LKEANGYVLF GKPMVVQFAR SARPKQDSKE GKRK
//
ID   Q3UZ81_MOUSE            Unreviewed;       624 AA.
AC   Q3UZ81;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Il16;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 2 PDZ (DHR) domains.
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DR   EMBL; AK134007; BAE21977.1; -; mRNA.
DR   IPI; IPI00930865; -.
DR   UniGene; Mm.10137; -.
DR   ProteinModelPortal; Q3UZ81; -.
DR   SMR; Q3UZ81; 398-624.
DR   STRING; Q3UZ81; -.
DR   Ensembl; ENSMUST00000001792; ENSMUSP00000001792; ENSMUSG00000001741.
DR   MGI; MGI:1270855; Il16.
DR   GeneTree; ENSGT00590000082971; -.
DR   HOVERGEN; HBG000100; -.
DR   InParanoid; Q3UZ81; -.
DR   ArrayExpress; Q3UZ81; -.
DR   Bgee; Q3UZ81; -.
DR   Genevestigator; Q3UZ81; -.
DR   GO; GO:0005622; C:intracellular; IDA:MGI.
DR   GO; GO:0005125; F:cytokine activity; IDA:MGI.
DR   GO; GO:0050930; P:induction of positive chemotaxis; IDA:MGI.
DR   GO; GO:0030595; P:leukocyte chemotaxis; IDA:MGI.
DR   InterPro; IPR020450; Interleukin-16.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF00595; PDZ; 2.
DR   PRINTS; PR01931; INTRLEUKIN16.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; PDZ; 2.
DR   PROSITE; PS50106; PDZ; 2.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   624 AA;  66433 MW;  01EC116F349B816E CRC64;
     MDYSFDITAE DPWVRISDCI KNLFSPIMSE NHSHTPLQPN TSLGEEDGTQ GCPEGGLSKM
     DAANGAPRVY KSADGSTVKK GPPVAPKPAW FRQSLKGLRN RAPDPRRPPE VASAIQPTPV
     SRDPPGPQPQ ASSSIRQRIS SFENFGSSQL PDRGVQRLSL QPSSGETTKF PGKQDGGRFS
     GLLGQGATVT AKHRQTEVES MSTTFPNSSE VRDPGLPESP PPGQRPSTKA LSPDPLLRLL
     TTQSEDTQGP GLKMPSQRAR SFPLTRTQSC ETKLLDEKAS KLYSISSQLS SAVMKSLLCL
     PSSVSCGQIT CIPKERVSPK SPCNNSSAAE GFGEAMASDT GFSLNLSELR EYSEGLTEPG
     ETEDRNHCSS QAGQSVISLL SAEELEKLIE EVRVLDEATL KQLDSIHVTI LHKEEGAGLG
     FSLAGGADLE NKVITVHRVF TNGLASQGGT IQKGNEVLSI NGKSLKGATH NDALAILRQA
     RDPRQAVIVT RRTTVEATHD LNSSTDSTAS ASAASDISVE SKEATVCTVT LEKTSAGLGF
     SLEGGKGSLH GDKPLTINRI FKGTEQGEMV QPGDEILQLA GTAVQGLTRF EAWNVIKALP
     DGPVTIVIRR TSLQCKQTTA SADS
//
ID   CPZIP_MOUSE             Reviewed;         412 AA.
AC   Q3UZA1; Q3TAD8; Q3TBC2; Q3TGA5; Q8R3A0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 33.
DE   RecName: Full=CapZ-interacting protein;
DE   AltName: Full=Protein kinase substrate CapZIP;
GN   Name=Rcsd1; Synonyms=Capzip;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Inner ear, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Stress-induced phosphorylation of CAPZIP may regulate
CC       the ability of F-actin-capping protein to remodel actin filament
CC       assembly (By similarity).
CC   -!- SUBUNIT: Interacts with CAPZA2 and CAPZB (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3UZA1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3UZA1-2; Sequence=VSP_031649;
CC   -!- PTM: Dephosphorylation results in its dissociation from CAPZA2 (By
CC       similarity).
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DR   EMBL; AK133961; BAE21956.1; -; mRNA.
DR   EMBL; AK158429; BAE34505.1; -; mRNA.
DR   EMBL; AK168816; BAE40643.1; -; mRNA.
DR   EMBL; AK171323; BAE42392.1; -; mRNA.
DR   EMBL; AK171914; BAE42730.1; -; mRNA.
DR   EMBL; BC025872; AAH25872.1; -; mRNA.
DR   IPI; IPI00153710; -.
DR   IPI; IPI00652534; -.
DR   RefSeq; NP_001033935.1; NM_001038846.1.
DR   RefSeq; NP_848708.2; NM_178593.3.
DR   UniGene; Mm.265552; -.
DR   PhosphoSite; Q3UZA1; -.
DR   PRIDE; Q3UZA1; -.
DR   Ensembl; ENSMUST00000040357; ENSMUSP00000043724; ENSMUSG00000040723.
DR   Ensembl; ENSMUST00000097474; ENSMUSP00000095082; ENSMUSG00000040723.
DR   GeneID; 226594; -.
DR   KEGG; mmu:226594; -.
DR   NMPDR; fig|10090.3.peg.1394; -.
DR   UCSC; uc007djj.1; mouse.
DR   CTD; 226594; -.
DR   MGI; MGI:2676394; Rcsd1.
DR   eggNOG; maNOG17338; -.
DR   GeneTree; ENSGT00510000049038; -.
DR   HOGENOM; HBG283859; -.
DR   HOVERGEN; HBG106582; -.
DR   InParanoid; Q3UZA1; -.
DR   OrthoDB; EOG47M1ZQ; -.
DR   PhylomeDB; Q3UZA1; -.
DR   NextBio; 378253; -.
DR   ArrayExpress; Q3UZA1; -.
DR   Bgee; Q3UZA1; -.
DR   CleanEx; MM_RCSD1; -.
DR   Genevestigator; Q3UZA1; -.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Phosphoprotein.
FT   CHAIN         1    412       CapZ-interacting protein.
FT                                /FTId=PRO_0000320263.
FT   MOD_RES      81     81       N6-acetyllysine (By similarity).
FT   MOD_RES     105    105       Phosphoserine (By similarity).
FT   MOD_RES     108    108       Phosphoserine; by MAPK12 and MAPK13 (By
FT                                similarity).
FT   MOD_RES     116    116       Phosphoserine (By similarity).
FT   MOD_RES     120    120       Phosphoserine (By similarity).
FT   MOD_RES     123    123       Phosphoserine (By similarity).
FT   MOD_RES     177    177       Phosphoserine (By similarity).
FT   MOD_RES     179    179       Phosphoserine; by MAPKAPK2 and MAPKAPK3
FT                                (By similarity).
FT   VAR_SEQ      36     65       Missing (in isoform 2).
FT                                /FTId=VSP_031649.
FT   CONFLICT    115    115       V -> I (in Ref. 2; AAH25872).
FT   CONFLICT    120    120       S -> G (in Ref. 1; BAE40643).
FT   CONFLICT    162    162       R -> K (in Ref. 1; BAE40643).
FT   CONFLICT    208    208       A -> P (in Ref. 2; AAH25872).
FT   CONFLICT    233    233       W -> R (in Ref. 1; BAE34505/BAE42730 and
FT                                2; AAH25872).
FT   CONFLICT    286    286       T -> I (in Ref. 1; BAE34505/BAE42730).
FT   CONFLICT    303    303       T -> A (in Ref. 2; AAH25872).
FT   CONFLICT    328    328       R -> S (in Ref. 1; BAE34505/BAE42730).
FT   CONFLICT    365    365       P -> R (in Ref. 1; BAE34505/BAE42730).
FT   CONFLICT    400    400       V -> A (in Ref. 1; BAE42392).
SQ   SEQUENCE   412 AA;  44114 MW;  650569CFA9083EFD CRC64;
     MEERPSETNS NVDSSAQPSV AQLAGRFREH AAVARETPAS KPTRRKPPCS LPLFPPKVEL
     GQNGEEKSPS GASHPPKIKV KSSPLIEKLQ ANLAFDPAAL LPGASPKSPG LKAIVSPFHS
     PPSTPSSPGI RSHPSEAEEV PVSFDQPPEG THLPSYNKVR TRGSIKRRPP SRRFRRSQSD
     CGDFRDYRAV EPSQENGARE ENGDDVFASK SKDPGSPQLN QEAMADGVEG TPWSAEKPRR
     RNTCNSTEKP EELVRTPEEA NAGEKVGQNP DTASQGHPEV QAPSQTGSPE AENGCGSPRE
     ETTPGEHTDT GKATEGTASE ERVADEDRLG QKSPDANMPE EEGVVREKAP QTSSGKAEGT
     TIAEPDTKQK EEAPLEPSCS PGADHAAGEI TSEIQNEKAV SMDDIPIEDT RM
//
ID   Q3UZA4_MOUSE            Unreviewed;       536 AA.
AC   Q3UZA4;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 53.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Tcf12;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 basic helix-loop-helix (bHLH) domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK133958; BAE21953.1; -; mRNA.
DR   IPI; IPI00403983; -.
DR   RefSeq; NP_035674.2; NM_011544.3.
DR   UniGene; Mm.171615; -.
DR   UniGene; Mm.480117; -.
DR   ProteinModelPortal; Q3UZA4; -.
DR   SMR; Q3UZA4; 433-506.
DR   STRING; Q3UZA4; -.
DR   PRIDE; Q3UZA4; -.
DR   Ensembl; ENSMUST00000064957; ENSMUSP00000066198; ENSMUSG00000032228.
DR   GeneID; 21406; -.
DR   KEGG; mmu:21406; -.
DR   UCSC; uc009qpe.1; mouse.
DR   CTD; 21406; -.
DR   MGI; MGI:101877; Tcf12.
DR   HOVERGEN; HBG003854; -.
DR   ArrayExpress; Q3UZA4; -.
DR   Bgee; Q3UZA4; -.
DR   Genevestigator; Q3UZA4; -.
DR   GO; GO:0005667; C:transcription factor complex; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0016563; F:transcription activator activity; IDA:MGI.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   InterPro; IPR011598; HLH_DNA-bd.
DR   InterPro; IPR001092; HLH_DNA-bd_dom.
DR   Gene3D; G3DSA:4.10.280.10; HLH_DNA_bd; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; HLH_basic; 1.
DR   PROSITE; PS50888; HLH; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   536 AA;  57986 MW;  5E0F8B94AEF06862 CRC64;
     MYCAYPVPGM GNNSLMYYYN GKTVYAPSPN SDDFNRESPS YPSPKPPTSM FASTFFMQDG
     THSSSDLWSS SNGMSQPGFG GILGTSTSHM SQSSSYGSLH SHDRLSYPPH SVSPTDINTS
     LPPMSSFHRG STSSSPYVAA SHTPPINGSD SILGTRGNAA GSSQTGDALG KALASIYSPD
     HTSSSFPSNP STPVGSPSPL TGTSQWPRAG GQAPSSPSYE NSLHSLKNRV EQQLHEHLQD
     AMSFLKDVCE QSRMEDRLDR LDDAIHVLRN HAVGPSTSLP TSHSDIHSLL GPSHNASIGN
     LNSNYGGSSL VTNSRSASMV GTHWEDSVSL NGNHSVLSST VAASNTELNH KTPENFRGGV
     QNQSGSVVPT EIKTENKEKD ENLHEPPSSD DMKSDDESSQ KDIKVSSRGR TSSTNEDEDL
     NPEQKIEREK ERRMANNARE RLRVRDINEA FKELGRMCQL HLKSEKPQTK LLILHQAVAV
     ILSLEQQVRE RNLNPKAACL KRREEEKVSA ASAEPPNTLP GAHPGLSEST NPMGHL
//
ID   Q3UZE5_MOUSE            Unreviewed;       692 AA.
AC   Q3UZE5;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Tcf4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 basic helix-loop-helix (bHLH) domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK133885; BAE21912.1; -; mRNA.
DR   IPI; IPI00652159; -.
DR   UniGene; Mm.4269; -.
DR   ProteinModelPortal; Q3UZE5; -.
DR   SMR; Q3UZE5; 591-664.
DR   STRING; Q3UZE5; -.
DR   Ensembl; ENSMUST00000066717; ENSMUSP00000067318; ENSMUSG00000053477.
DR   MGI; MGI:98506; Tcf4.
DR   eggNOG; roNOG08508; -.
DR   GeneTree; ENSGT00510000046438; -.
DR   HOGENOM; HBG713543; -.
DR   HOVERGEN; HBG003854; -.
DR   InParanoid; Q3UZE5; -.
DR   ArrayExpress; Q3UZE5; -.
DR   Bgee; Q3UZE5; -.
DR   Genevestigator; Q3UZE5; -.
DR   GO; GO:0005667; C:transcription factor complex; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR   GO; GO:0030528; F:transcription regulator activity; IEA:InterPro.
DR   GO; GO:0030282; P:bone mineralization; IGI:MGI.
DR   GO; GO:0060070; P:canonical Wnt receptor signaling pathway; IMP:MGI.
DR   GO; GO:0060325; P:face morphogenesis; IGI:MGI.
DR   GO; GO:0048625; P:myoblast cell fate commitment; IMP:MGI.
DR   GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0042475; P:odontogenesis of dentine-containing tooth; IGI:MGI.
DR   InterPro; IPR011598; HLH_DNA-bd.
DR   InterPro; IPR001092; HLH_DNA-bd_dom.
DR   Gene3D; G3DSA:4.10.280.10; HLH_DNA_bd; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; HLH_basic; 1.
DR   PROSITE; PS50888; HLH; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   692 AA;  73710 MW;  094A29413ABFCA1F CRC64;
     MHHQQRMAAL GTDKELSDLL DFSAMFSPPV SSGKNGPTSL ASGHFTGSSD AGVHKMPGLG
     GSVLPTGNLA DVEDRSSSGS WGTGGHPSPS RNYGDGTPYD HMTSRDLGSH DNLSPPFVNS
     RIQSKTERGS YSSYGRENVQ GCHQQSLLGG DMDMGNPGTL SPTKPGSQYY QYSSNNARRR
     PLHSSAMEVQ TKKVRKVPPG LPSSVYAPSA STADYNRDSP GYPSSKPAAS TFPSSFLMQD
     GHHSSDPWSS SSGMNQPGYG GMLGNSSHIP QSSSYCSLHP HERLSYPSHS SEDINSSLPP
     MSTFHRSGTN HYSTSSCTPP ANGTDSIMAN RGTGAAGSSQ TGDALGKALA SIYSPDHTNN
     SFSSNPSTPV GSPPSLSAGT AVWSRNGGQA SSSPNYEGPL HSLQSRIEDR LERLDDAIHV
     LRNHAVGPST AVPGGHGDMH GIMGPSHNGA MGSLGSGYGT SLLSANRHSL MVGAHREDGV
     ALRGSHSLLP NQVPVPQLPV QSATSPDLNP PQDPYRGMPP GLQGQSVSSG SSEIKSDDEG
     DENLQDTKSS EDKKLDDDKK DIKSITRSRS SNNDDEDLTP EQKAEREKER RMANNARERL
     RVRDINEAFK ELGRMVQLHL KSDKPQTKLL ILHQAVAVIL SLEQQVRERN LNPKAACLKR
     REEEKVSSEP PPLSLAGPHP GMGDAANHMG QM
//
ID   Q3UZI6_MOUSE            Unreviewed;       703 AA.
AC   Q3UZI6;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   11-JAN-2011, entry version 34.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Noc2l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK133834; BAE21871.1; -; mRNA.
DR   IPI; IPI00828463; -.
DR   RefSeq; NP_067278.2; NM_021303.2.
DR   UniGene; Mm.423051; -.
DR   UniGene; Mm.480639; -.
DR   GeneID; 57741; -.
DR   KEGG; mmu:57741; -.
DR   CTD; 57741; -.
DR   MGI; MGI:1931051; Noc2l.
DR   HOVERGEN; HBG029261; -.
DR   PhylomeDB; Q3UZI6; -.
DR   NextBio; 313867; -.
DR   Genevestigator; Q3UZI6; -.
DR   InterPro; IPR005343; UPF0120.
DR   PANTHER; PTHR12687; UPF0120; 1.
DR   Pfam; PF03715; Noc2; 1.
PE   2: Evidence at transcript level;
FT   NON_TER     703    703
SQ   SEQUENCE   703 AA;  80456 MW;  CB0D517E4224DA81 CRC64;
     MAASRAPRRR LEDLSVDEFL ASGFESGSES ELEGAAEAAA EERRARGAAW NRERRGARTS
     PGPAGRPRKG RASEHKDQLS RLKDRDPEFY KFLQENDRRL LDFSDSDSSA EEEEPFHSLP
     DTLEEASETE EDGGEDSDAL PRGLRSKKNE PVPVTLAMVE RWRQGSRHHL SPRLFHEVVQ
     AFRAAVATTQ GEQEAAETCR FQVADSAVFN ALVTFCIRDL CGCLQKLLFG KTPKDSNRLL
     PSSSPLWGKL RVDVKTYLSA VVQLVACLAE ATVSAAVLQH ISSLVPYYLT FPKQCRMLLK
     RMVVLWSTGE ESLRVLAFLV LIRVCRHKKE AFLGPILKQM YIMYVRNCKF TSPSTLPLIS
     FMQRTLTEML ALDPSVSYQH AFLYIRQLAV HLRNAMTAGK KETHQSVYNW QYVHCLYLWC
     RVLSTLGSSE ILQPLLYPLS QIIIGCIKLL PTARFYPLRM HCVRALTLLS QTIGTFIPVL
     PFILEIFQQV DFNRRPGRMS SKPINFSVIL KLSSTNLQEK AYRDGLLEQL CDLTLEYLHS
     QAHSIAFPEL VLPTVLQLKS FLRECKVANY CRQVRQLLEK VQENAQHIQS LRQSATFSVS
     DQMAVDAWEK QVREEGTPLT RYYGHWKKLR DREIQLEISG KERLEDLNFP EIKRRKVEDR
     KDEDRKELKD LFELDSSEGE DSTDFFERGV PRLPEAHQGL KED
//
ID   Q3UZK5_MOUSE            Unreviewed;       607 AA.
AC   Q3UZK5;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 50.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Akap13;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK133803; BAE21852.1; -; mRNA.
DR   IPI; IPI00752332; -.
DR   UniGene; Mm.216107; -.
DR   STRING; Q3UZK5; -.
DR   PRIDE; Q3UZK5; -.
DR   Ensembl; ENSMUST00000094307; ENSMUSP00000091865; ENSMUSG00000066406.
DR   UCSC; uc009hww.1; mouse.
DR   MGI; MGI:2676556; Akap13.
DR   HOVERGEN; HBG050566; -.
DR   ArrayExpress; Q3UZK5; -.
DR   Bgee; Q3UZK5; -.
DR   Genevestigator; Q3UZK5; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR015721; RhoGEF-like.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   PANTHER; PTHR22825; RhoGEF_like; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Zinc.
FT   NON_TER     607    607
SQ   SEQUENCE   607 AA;  69192 MW;  86304F6FECCC0677 CRC64;
     MSVKWGRLPE VPLITVRFTG LKHGQEKEKE KDKIKEKEKD SKEKEKDKKT FNGHTFSPIP
     IVGPISCSQC MKPFTNKDAY TCAGCGAFVH KGCRENLASC AKVKMKQPKG SLQAHDTSSL
     PTVIMRNKSS QPKERPRSAV LLADEATAAP VFTNRRSQQS VSLSKSVSIQ NITGVGNDEN
     MSNTWKFLSH STDSLNKICK VNESTESLTD EGVGTDMNEG QLMGDFESDS KQLEAESWSR
     TVDSKFLKQQ KKDVVKRQEV IYELMQTELH HIRTLKIMSD VYSRGMMTDL LFEQQMVEKL
     FPCLDELISI HSQFFQRILE RKKESLVDKS EKNFLIKRIG DVLVSQFSGE SAERLKKTYG
     KFCGQHNQSV NYFKDLYTKD KRFQAFVKKK MSSSVVRRLG IPECILLVTQ RITKYPVLFQ
     RILQCTKDNE VEQEDLTQSL SLVKDVIGAV DSKVASYEKK VRLGEIYTKT DSKSIMRMKS
     GQMFAKEDLR RKKLVRDGSV FLKSTTGRLK EVQAVLLTDI LVFLQEKDQK YVFASLDHKS
     TVISLKKLIV REVAHEEKGL FLISMGVKDP EMVEVHASSR EERNSWIQII QDTINSLNRD
     EDEGIPS
//
ID   TTC9A_MOUSE             Reviewed;         219 AA.
AC   Q3V038; B2RTC7; Q3TTA0; Q6A0A0; Q8K336;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=Tetratricopeptide repeat protein 9A;
DE            Short=TPR repeat protein 9A;
GN   Name=Ttc9; Synonyms=Kiaa0227, Ttc9a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the TTC9 family.
CC   -!- SIMILARITY: Contains 3 TPR repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH28891.1; Type=Erroneous initiation;
CC       Sequence=BAD32196.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK172918; BAD32196.1; ALT_INIT; mRNA.
DR   EMBL; AK133456; BAE21667.1; -; mRNA.
DR   EMBL; AK161499; BAE36425.1; -; mRNA.
DR   EMBL; BC028891; AAH28891.1; ALT_INIT; mRNA.
DR   EMBL; BC139242; AAI39243.1; -; mRNA.
DR   EMBL; BC139244; AAI39245.1; -; mRNA.
DR   IPI; IPI00720235; -.
DR   RefSeq; NP_001028321.1; NM_001033149.2.
DR   UniGene; Mm.130002; -.
DR   HSSP; Q9H3U1; 2DBA.
DR   ProteinModelPortal; Q3V038; -.
DR   SMR; Q3V038; 46-189.
DR   PRIDE; Q3V038; -.
DR   Ensembl; ENSMUST00000036116; ENSMUSP00000048590; ENSMUSG00000042734.
DR   GeneID; 69480; -.
DR   KEGG; mmu:69480; -.
DR   UCSC; uc007ocm.1; mouse.
DR   CTD; 69480; -.
DR   MGI; MGI:1916730; Ttc9.
DR   eggNOG; roNOG16193; -.
DR   GeneTree; ENSGT00390000016022; -.
DR   HOGENOM; HBG505588; -.
DR   HOVERGEN; HBG062451; -.
DR   InParanoid; Q3V038; -.
DR   OMA; NAELECY; -.
DR   OrthoDB; EOG4Q2DGG; -.
DR   NextBio; 329570; -.
DR   ArrayExpress; Q3V038; -.
DR   Bgee; Q3V038; -.
DR   CleanEx; MM_TTC9; -.
DR   Genevestigator; Q3V038; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   InterPro; IPR001440; TPR-1.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
DR   Pfam; PF00515; TPR_1; 1.
DR   SMART; SM00028; TPR; 3.
DR   PROSITE; PS50005; TPR; 1.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   2: Evidence at transcript level;
KW   Repeat; TPR repeat.
FT   CHAIN         1    219       Tetratricopeptide repeat protein 9A.
FT                                /FTId=PRO_0000294470.
FT   REPEAT       56     89       TPR 1.
FT   REPEAT      125    160       TPR 2.
FT   REPEAT      161    194       TPR 3.
SQ   SEQUENCE   219 AA;  24351 MW;  95949287036C10FD CRC64;
     MERKGLAARS SGNPSPPALG EGPRPVPPPC VPSGGGAPER GQAGTAAEPA ELIRRAHEFK
     SQGAQCYKDK KFREAIGKYH RALLELKGLL PSQEERDARP ASSAGVPKSS RLSEEQSKTV
     EAIEIDCYNS LAACLLQAEL VNYERVKEYC LKVLKKEGEN FKALYRSGVA FYHLGDYDKA
     LYYLKEARTR QPTDTNVIRY IQLTEMKLSR CSQREKEAM
//
ID   ZMAT1_MOUSE             Reviewed;         714 AA.
AC   Q3V0C1; A2AFB3; Q5DTV1; Q8BI78;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Zinc finger matrin-type protein 1;
GN   Name=Zmat1; Synonyms=Kiaa1789;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-688 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 95-714 (ISOFORM 2).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3V0C1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3V0C1-2; Sequence=VSP_029535;
CC       Name=3;
CC         IsoId=Q3V0C1-3; Sequence=VSP_029534, VSP_029535;
CC   -!- SIMILARITY: Contains 2 matrin-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC32933.1; Type=Frameshift; Positions=442, 478;
CC       Sequence=CAM26540.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK046974; BAC32933.1; ALT_FRAME; mRNA.
DR   EMBL; AK133258; BAE21583.1; -; mRNA.
DR   EMBL; AL672063; CAM26540.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AK220419; BAD90465.1; -; mRNA.
DR   IPI; IPI00554978; -.
DR   IPI; IPI00762771; -.
DR   IPI; IPI00875666; -.
DR   UniGene; Mm.336238; -.
DR   ProteinModelPortal; Q3V0C1; -.
DR   SMR; Q3V0C1; 79-185.
DR   PRIDE; Q3V0C1; -.
DR   Ensembl; ENSMUST00000064659; ENSMUSP00000066815; ENSMUSG00000052676.
DR   Ensembl; ENSMUST00000087501; ENSMUSP00000084776; ENSMUSG00000052676.
DR   Ensembl; ENSMUST00000113185; ENSMUSP00000108810; ENSMUSG00000052676.
DR   MGI; MGI:2442284; Zmat1.
DR   eggNOG; roNOG05490; -.
DR   GeneTree; ENSGT00510000047024; -.
DR   HOGENOM; HBG127435; -.
DR   HOVERGEN; HBG099654; -.
DR   InParanoid; Q3V0C1; -.
DR   OMA; VENQLPH; -.
DR   OrthoDB; EOG4VX265; -.
DR   ArrayExpress; Q3V0C1; -.
DR   Bgee; Q3V0C1; -.
DR   CleanEx; MM_ZMAT1; -.
DR   Genevestigator; Q3V0C1; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   PROSITE; PS50171; ZF_MATRIN; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; DNA-binding; Metal-binding; Nucleus; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    714       Zinc finger matrin-type protein 1.
FT                                /FTId=PRO_0000311349.
FT   ZN_FING      89    119       Matrin-type 1.
FT   ZN_FING     230    254       Matrin-type 2.
FT   COMPBIAS    611    614       Poly-Arg.
FT   COMPBIAS    616    695       Lys-rich.
FT   VAR_SEQ       1    226       Missing (in isoform 3).
FT                                /FTId=VSP_029534.
FT   VAR_SEQ     258    272       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_029535.
FT   CONFLICT    145    145       C -> R (in Ref. 2; BAD90465).
FT   CONFLICT    178    178       H -> R (in Ref. 1; BAE21583).
FT   CONFLICT    341    341       E -> G (in Ref. 1; BAC32933).
SQ   SEQUENCE   714 AA;  84176 MW;  1E64EB7E49B62029 CRC64;
     MHQQAATSSR CQGWSPRYQG WSPRFQGWSP RFHGWNPRFR GWNPHCRGWS PCFQGWSPRC
     QTFPPKINRI SSNYPTCDGQ EQPAYFTDNF CKPCGVVLQH ESERISHFES EIHAQNVKFF
     FQMHGEQSEV PGRKVNMHAG NSQVCSSGEV NRNNFTDLHN MSFDSLAAAP SHYVGKSHSP
     TQNQSLEEHD QVSPSTCSPK MDEPNTTPAP PPFLKSVIVK PPPAYRMRTY VCHICSITFT
     SLHMFRSHMQ GTEHQIKRAQ HLWTHWQCTQ LLESHVINQV KNSKKMQESC QAECGDDIKM
     KKSRELEPKG HFREMEDNYM EAQAHEYREM VDSRPRHKML EQTLPLENFW AHPGPYNDSR
     ALEEQLPHNL PAESKTYDSF QDELEDYIKG QKARGLDPNT SFRRMSESYR YRDQRYRERV
     DSEHRQRPCE ERFSFEAPQT YQQEYSASPV EGQSPHWLPS HSKRRNDDFQ NEFDDYNKVQ
     ESRESEPKTS FRRMDSSFET HNYEEMVDRR SSHTMFEEGL PCETFQTYTD PYSSAQAVEN
     TLPHCLPAYE NQPSLDAESH YQLTTEEFSE MPASLSLSQQ EDNPSSYNVD YDIYKHLPSN
     DNASAHETSH RRRRQKRKRH LEEGKERPEK EQSKHKRKRS YQDKDLDKDK LIKQSKREED
     KAGVSSEKTK HRRKKRKHET SSEKEERKHK KEKKKSVEER TEEEILWDES ILGF
//
ID   GARL3_MOUSE             Reviewed;        1038 AA.
AC   Q3V0G7; Q8BNH8; Q8CC22;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=GTPase-activating Rap/Ran-GAP domain-like protein 3;
GN   Name=Garnl3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 188-197, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3V0G7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3V0G7-2; Sequence=VSP_029746, VSP_029747;
CC   -!- SIMILARITY: Belongs to the GARNL3 family.
CC   -!- SIMILARITY: Contains 1 CNH domain.
CC   -!- SIMILARITY: Contains 1 Rap-GAP domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC38990.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK034068; BAC28570.1; -; mRNA.
DR   EMBL; AK083673; BAC38990.1; ALT_INIT; mRNA.
DR   EMBL; AK133163; BAE21537.1; -; mRNA.
DR   EMBL; AL731852; CAM22321.1; -; Genomic_DNA.
DR   EMBL; BC132143; AAI32144.1; -; mRNA.
DR   IPI; IPI00474258; -.
DR   IPI; IPI00874528; -.
DR   RefSeq; NP_849219.2; NM_178888.4.
DR   UniGene; Mm.41290; -.
DR   ProteinModelPortal; Q3V0G7; -.
DR   SMR; Q3V0G7; 110-438.
DR   PRIDE; Q3V0G7; -.
DR   Ensembl; ENSMUST00000043162; ENSMUSP00000047283; ENSMUSG00000038860.
DR   Ensembl; ENSMUST00000102810; ENSMUSP00000099874; ENSMUSG00000038860.
DR   GeneID; 99326; -.
DR   KEGG; mmu:99326; -.
DR   UCSC; uc008jhj.1; mouse.
DR   CTD; 99326; -.
DR   MGI; MGI:2139309; Garnl3.
DR   GeneTree; ENSGT00550000074284; -.
DR   HOGENOM; HBG358147; -.
DR   HOVERGEN; HBG059186; -.
DR   InParanoid; Q3V0G7; -.
DR   OMA; TSEANPE; -.
DR   OrthoDB; EOG4X0MRJ; -.
DR   NextBio; 353877; -.
DR   ArrayExpress; Q3V0G7; -.
DR   Bgee; Q3V0G7; -.
DR   CleanEx; MM_GARNL3; -.
DR   Genevestigator; Q3V0G7; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005083; F:small GTPase regulator activity; IEA:InterPro.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR001180; Citron.
DR   InterPro; IPR000331; Rap_GAP.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF02145; Rap_GAP; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS50085; RAPGAP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing; GTPase activation;
KW   Phosphoprotein.
FT   CHAIN         1   1038       GTPase-activating Rap/Ran-GAP domain-like
FT                                protein 3.
FT                                /FTId=PRO_0000312216.
FT   DOMAIN      214    430       Rap-GAP.
FT   DOMAIN      512    824       CNH.
FT   MOD_RES     851    851       Phosphothreonine (By similarity).
FT   VAR_SEQ       1     45       Missing (in isoform 2).
FT                                /FTId=VSP_029746.
FT   VAR_SEQ      46     48       VNL -> MKS (in isoform 2).
FT                                /FTId=VSP_029747.
FT   CONFLICT    529    529       T -> A (in Ref. 1; BAC38990).
SQ   SEQUENCE   1038 AA;  115437 MW;  94E4B7A37AF5ADF6 CRC64;
     MDPLTKGSCG SQLAQTLLWK AKSSLSFGIQ PLQTWPTKDP ELESQVNLSV SEDLGCRRGD
     FSRKHYGSVE LLISSDADGA IQRAGRFRVE NGSTDESAAA LPGTWRRTDV HLENPEYHTR
     WYFKYFLGQV HQNYIGNDAE KSPFFLSVTL SDQNNQRVPQ YRAILWRKTG TQKICLPYSP
     TKTLSVKSIL SAMNLDKFEK GPREIFHPEI QKDLLVLEEQ EGSVNFKFGV LFAKDGQLTD
     DEMFSNEIGS EAFQKFLNLL GDTITLKGWT GYRGGLDTKN NTTGINSVYT VYQGHEVMFH
     VSTMLPYSKE NRQQVERKRH IGNDIVTIVF QEGEESSPAF KPSMIRSHFT HIFALVRYDQ
     QNDNYRLKIF SEESVPLFGP PLPSPPVFTD HQEFRDFLLV KLINGEKATL ETPTFAQKRR
     RTLDMLIRSL YQDLMPDLHK NMLNRRSFSD VLPESPKSAR KKEEARQAEF VRIGQALKLK
     SIVRGDAPSS LAASGMCKKE PWEPQCFCCN FPHEAVCADP WGQALLVSTD AGVLLVDDDL
     PSVPVFDRTL PVKQIHVLET LDLLVLRADK GKDARLFVFR LSAVQKGLDG RQTGRSRSDC
     RENKLEKTKG CHLYAINTHH SRELRIVVAI RNKLLLITRK PHNKPSGVPG VSLLSPLSES
     PVEEFQYIRE ICLCDSPAVM ALVDGPTEES DNLICVAYRH QFDVVNESTG EAFRLHHVEA
     NKVNFVAAID VYEDGEAGLL LCYNYSCIYK KVCPFNGGSF LLQPSASDFQ FCWNQAPYAI
     VCAFPYLLAF TTDSMEIRLV VNGNLVHTAV VPQLQLVASR SDIYFTAATT VHEGSSGGSS
     KGASAHTSPQ TPPARDTPLF PSSLGEGEIQ SKNLYKIPLR NLVGRSIERP LKSPLVSKVI
     TPPTSIGLGV AAIPVTHSLS LSRMEIKEIA SRTRRELLGL SDDGGTKTEG APRAKSKTRK
     RLEESQGGPK PETVRSASSD RIPSGILESP ASEANPEGHN HWASSEQDAG VDKEGSPGSG
     SSPFQLMASS EEDIIDLK
//
ID   PRR7_MOUSE              Reviewed;         269 AA.
AC   Q3V0I2;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 39.
DE   RecName: Full=Proline-rich protein 7;
DE   AltName: Full=Synaptic proline-rich membrane protein;
GN   Name=Prr7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBUNIT: Found in a postsynaptic membrane complex with DLG4 and
CC       GRIN1. Interacts with DLG4. Interacts preferentially to the PDZ3
CC       domain of DLG4 and to lesser degree to PDZ2 but not to the PDZ1
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type III membrane
CC       protein (Potential). Cell junction, synapse, postsynaptic cell
CC       membrane (By similarity). Note=Enriched in post-synaptic plasma
CC       membrane and postsynaptic densities (PSD). Accumulates in spines
CC       along with synapse maturation and colocalizes with DLG4 in a
CC       punctate pattern (By similarity).
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK133129; BAE21522.1; -; mRNA.
DR   IPI; IPI00132812; -.
DR   RefSeq; NP_001025467.1; NM_001030296.4.
DR   UniGene; Mm.315457; -.
DR   ProteinModelPortal; Q3V0I2; -.
DR   STRING; Q3V0I2; -.
DR   PhosphoSite; Q3V0I2; -.
DR   PRIDE; Q3V0I2; -.
DR   Ensembl; ENSMUST00000046533; ENSMUSP00000046776; ENSMUSG00000034686.
DR   GeneID; 432763; -.
DR   KEGG; mmu:432763; -.
DR   UCSC; uc007qrb.1; mouse.
DR   CTD; 432763; -.
DR   MGI; MGI:3487246; Prr7.
DR   eggNOG; roNOG15716; -.
DR   GeneTree; ENSGT00390000001559; -.
DR   HOGENOM; HBG268103; -.
DR   HOVERGEN; HBG095664; -.
DR   InParanoid; Q3V0I2; -.
DR   OMA; PSWTDSE; -.
DR   OrthoDB; EOG4M65JX; -.
DR   PhylomeDB; Q3V0I2; -.
DR   NextBio; 407978; -.
DR   Bgee; Q3V0I2; -.
DR   Genevestigator; Q3V0I2; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR021684; Uncharacterised_WW-bd.
DR   Pfam; PF11669; WBP-1; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Membrane; Postsynaptic cell membrane;
KW   Signal-anchor; Synapse; Transmembrane; Transmembrane helix.
FT   CHAIN         1    269       Proline-rich protein 7.
FT                                /FTId=PRO_0000328650.
FT   TOPO_DOM      1      9       Extracellular (Potential).
FT   TRANSMEM     10     30       Helical; Signal-anchor for type III
FT                                membrane protein; (Potential).
FT   TOPO_DOM     31    269       Cytoplasmic (Potential).
FT   MOTIF       267    269       PDZ-binding (Potential).
FT   COMPBIAS     69    160       Pro-rich.
SQ   SEQUENCE   269 AA;  30354 MW;  CBEDCF9596CC40B8 CRC64;
     MVMSQGTYTF LTCFAGFWLI WGLIVLLCCF CSFLRRRLKR RQEERLREQN LRALELEPLE
     LEGSLAGSPP GLAPPPPPHR SRLEAPVHAH SHVHVHPLLH HGPAPPHAHP HPHHHALPHP
     PPPHLAVPPR PWSYPRQAES DMSKPPCYEE AVLMAEPPPP YSEVLTDTRG LYRKIVTPFL
     SRRDSAEKQE QPPPSYKPLF LDRGYTSALH LPSAPRPAAP CPALCLQAER SRRVFPSWTD
     SELSSREPLE HGAWRLPVSI PLFGRTTAV
//
ID   AL2S4_MOUSE             Reviewed;         427 AA.
AC   Q3V0J1; Q3TIS2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 40.
DE   RecName: Full=Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 4 protein homolog;
GN   Name=Als2cr4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Placenta, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
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DR   EMBL; AK133112; BAE21513.1; -; mRNA.
DR   EMBL; AK167733; BAE39774.1; -; mRNA.
DR   IPI; IPI00652649; -.
DR   RefSeq; NP_001032901.1; NM_001037812.2.
DR   UniGene; Mm.261275; -.
DR   ProteinModelPortal; Q3V0J1; -.
DR   PhosphoSite; Q3V0J1; -.
DR   PRIDE; Q3V0J1; -.
DR   Ensembl; ENSMUST00000094918; ENSMUSP00000092523; ENSMUSG00000038079.
DR   GeneID; 381259; -.
DR   KEGG; mmu:381259; -.
DR   UCSC; uc007bdd.1; mouse.
DR   CTD; 381259; -.
DR   MGI; MGI:2138365; Als2cr4.
DR   eggNOG; roNOG10487; -.
DR   GeneTree; ENSGT00390000005159; -.
DR   HOGENOM; HBG716686; -.
DR   HOVERGEN; HBG060391; -.
DR   InParanoid; Q3V0J1; -.
DR   OMA; ELMFSSD; -.
DR   OrthoDB; EOG4PRSRG; -.
DR   NextBio; 401788; -.
DR   ArrayExpress; Q3V0J1; -.
DR   Bgee; Q3V0J1; -.
DR   Genevestigator; Q3V0J1; -.
DR   GermOnline; ENSMUSG00000038079; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    427       Amyotrophic lateral sclerosis 2
FT                                chromosomal region candidate gene 4
FT                                protein homolog.
FT                                /FTId=PRO_0000076170.
FT   TRANSMEM    252    272       Helical; (Potential).
FT   TRANSMEM    290    310       Helical; (Potential).
FT   TRANSMEM    325    345       Helical; (Potential).
FT   TRANSMEM    375    395       Helical; (Potential).
FT   CONFLICT      2     14       RDDSGPPLEEDQA -> GKKQVVSEPQ (in Ref. 1;
FT                                BAE39774).
FT   CONFLICT     29     49       Missing (in Ref. 1; BAE39774).
SQ   SEQUENCE   427 AA;  47343 MW;  A8612DBBCE7FA7E1 CRC64;
     MRDDSGPPLE EDQARPPRAL PPVPSAIQVC SSFVENNSRM DQQDDLVGED DIPLSHPKKK
     KSRTKSSLAT ASSEGHAEPV VNRRAEGSEP PAAELKEHPE APAPRRQKKI RPPPELETSL
     TERPSSPSLL RNENGIDAEP REEAVIPKPR RKAKKTQPAE PQYASELGVE DEDILTDEQS
     TLEHHSRFTA PTGVSQPVGK VFVEKSRRFQ AADRSELIKT TENIDVSMDV KPSWTTRDVA
     LSVHRAFRMV GLFSHGFLAG CAVWNTVVIY VLAGDQLSNV SNLLQQYKPL AYPFQSLLYL
     LLALSTVSAF DRTDFAKISV AIRNFLALEP TALASFLYFT ALILSLSQQM TSDRIHLYEP
     SVNGSLWAAE AEEPILVPWI IVNLVVALLV GLSWLFLSYR PGMDLSEELM FFSDVDEHPE
     TGTKASP
//
ID   Q3V0N1_MOUSE            Unreviewed;       375 AA.
AC   Q3V0N1;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Paqr9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK133021; BAE21473.1; -; mRNA.
DR   IPI; IPI00667086; -.
DR   RefSeq; NP_940806.2; NM_198414.2.
DR   UniGene; Mm.151485; -.
DR   PRIDE; Q3V0N1; -.
DR   Ensembl; ENSMUST00000079597; ENSMUSP00000078547; ENSMUSG00000064225.
DR   GeneID; 75552; -.
DR   KEGG; mmu:75552; -.
DR   UCSC; uc009rbf.1; mouse.
DR   CTD; 75552; -.
DR   MGI; MGI:1922802; Paqr9.
DR   eggNOG; roNOG13622; -.
DR   HOVERGEN; HBG053506; -.
DR   InParanoid; Q3V0N1; -.
DR   OMA; SYPFALR; -.
DR   PhylomeDB; Q3V0N1; -.
DR   NextBio; 343338; -.
DR   ArrayExpress; Q3V0N1; -.
DR   Bgee; Q3V0N1; -.
DR   Genevestigator; Q3V0N1; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   InterPro; IPR004254; HlyIII-related.
DR   PANTHER; PTHR20855; HlyIII_related; 1.
DR   Pfam; PF03006; HlyIII; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   375 AA;  42741 MW;  673047F8770A3D02 CRC64;
     MPRRLQQRGA GVKGPPASTS RRSHPASASA PRSPPAATTK PLLRWDEVPD DFVECFILSG
     YRRLPCTAQE CLASVLKPTN ETLNFWTHFI PLLLFLSKFC RLFFLGGSDV PFHHPWLLPL
     WCYASGVLLT FAMSCTAHVF SCLSLRLRAA FFYLDYASIS YYGFGSTVAY YYYLLPSLSL
     LDARVMTPYV QQRLGWHVDC TRLIAVYRAL VLPVAFVLAV ACTVACCKSR TDWCSYPFAL
     RTFVFVMPLS MACPIMLESW LFDLRGENPT LFVHFYRRYF WLVVAAFFNV SKIPERIQPG
     LFDIIGHSHQ LFHIFTFLSI YDQVYYVEEG LRQFLQAPPA APTFSGTVGY MLLLVVCLGL
     VIRKFLNSTE FCSKK
//
ID   Q3V0V7_MOUSE            Unreviewed;       225 AA.
AC   Q3V0V7;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 38.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Chd2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
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DR   EMBL; AK132861; BAE21396.1; -; mRNA.
DR   IPI; IPI00845761; -.
DR   UniGene; Mm.34539; -.
DR   UniGene; Mm.34955; -.
DR   STRING; Q3V0V7; -.
DR   Ensembl; ENSMUST00000038366; ENSMUSP00000038545; ENSMUSG00000025788.
DR   MGI; MGI:2448567; Chd2.
DR   HOVERGEN; HBG085986; -.
DR   InParanoid; Q3V0V7; -.
DR   ArrayExpress; Q3V0V7; -.
DR   Bgee; Q3V0V7; -.
DR   Genevestigator; Q3V0V7; -.
PE   1: Evidence at protein level;
SQ   SEQUENCE   225 AA;  25753 MW;  CA8DDCAA3AF04D08 CRC64;
     MWLPTKNFFH AGCLVCSPQN RIYITIAKGK GPGKRRGPTI KISGVQVNVK SIIQHEEEFE
     MLHKSIPVDP EEKKKYCLTC RVKAAHFDVE WGVEDDSRLL LGIYEHGYGN WELIKTDPEL
     KLTDKILPVE TDKKPQGKQL QTRVDYLLKL LRKGLEKKGT VASGEEAKLK KRKPRVKKEN
     KAPRLKDEHG LEPASPRHSD NPSEEGEVKK QTRKPRLRNV RFSAS
//
ID   MFHA1_MOUSE             Reviewed;        1048 AA.
AC   Q3V1N1; Q3TAN2; Q8C4N5;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   08-MAR-2011, entry version 47.
DE   RecName: Full=Malignant fibrous histiocytoma-amplified sequence 1 homolog;
GN   Name=Mfhas1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-1048.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Head, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SIMILARITY: Contains 15 LRR (leucine-rich) repeats.
CC   -!- SIMILARITY: Contains 1 Roc domain.
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DR   EMBL; AC129082; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC129211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK081646; BAC38281.1; -; mRNA.
DR   EMBL; AK132349; BAE21119.1; -; mRNA.
DR   EMBL; AK171731; BAE42636.1; -; mRNA.
DR   IPI; IPI00669835; -.
DR   RefSeq; NP_001074748.1; NM_001081279.1.
DR   UniGene; Mm.103246; -.
DR   HSSP; P07359; 1GWB.
DR   ProteinModelPortal; Q3V1N1; -.
DR   SMR; Q3V1N1; 9-543, 618-643.
DR   STRING; Q3V1N1; -.
DR   PhosphoSite; Q3V1N1; -.
DR   PRIDE; Q3V1N1; -.
DR   Ensembl; ENSMUST00000037666; ENSMUSP00000044135; ENSMUSG00000070056.
DR   GeneID; 52065; -.
DR   KEGG; mmu:52065; -.
DR   UCSC; uc009lla.1; mouse.
DR   CTD; 52065; -.
DR   MGI; MGI:1098644; Mfhas1.
DR   eggNOG; roNOG12679; -.
DR   GeneTree; ENSGT00600000084050; -.
DR   HOGENOM; HBG445269; -.
DR   HOVERGEN; HBG108130; -.
DR   InParanoid; Q3V1N1; -.
DR   OMA; FFQRDAS; -.
DR   OrthoDB; EOG4CVG64; -.
DR   NextBio; 308456; -.
DR   ArrayExpress; Q3V1N1; -.
DR   Bgee; Q3V1N1; -.
DR   Genevestigator; Q3V1N1; -.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR020859; ROC_GTPase.
DR   Pfam; PF00560; LRR_1; 7.
DR   SMART; SM00369; LRR_TYP; 2.
DR   PROSITE; PS51450; LRR; 12.
DR   PROSITE; PS51424; ROC; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Leucine-rich repeat; Phosphoprotein; Repeat.
FT   CHAIN         1   1048       Malignant fibrous histiocytoma-amplified
FT                                sequence 1 homolog.
FT                                /FTId=PRO_0000308610.
FT   REPEAT       26     56       LRR 1.
FT   REPEAT       58     81       LRR 2.
FT   REPEAT       82    105       LRR 3.
FT   REPEAT      107    129       LRR 4.
FT   REPEAT      130    153       LRR 5.
FT   REPEAT      155    175       LRR 6.
FT   REPEAT      176    199       LRR 7.
FT   REPEAT      201    222       LRR 8.
FT   REPEAT      224    245       LRR 9.
FT   REPEAT      246    267       LRR 10.
FT   REPEAT      269    291       LRR 11.
FT   REPEAT      292    314       LRR 12.
FT   REPEAT      316    337       LRR 13.
FT   REPEAT      338    359       LRR 14.
FT   DOMAIN      399    645       Roc.
FT   REPEAT      870    893       LRR 15.
FT   MOD_RES     443    443       Phosphotyrosine (By similarity).
FT   MOD_RES     451    451       Phosphoserine (By similarity).
FT   MOD_RES     464    464       Phosphoserine (By similarity).
FT   MOD_RES     597    597       N6-acetyllysine (By similarity).
FT   CONFLICT    133    133       L -> M (in Ref. 2; BAE42636).
FT   CONFLICT    362    362       R -> P (in Ref. 2; BAE42636).
FT   CONFLICT    635    635       R -> Q (in Ref. 2; BAE42636).
SQ   SEQUENCE   1048 AA;  116599 MW;  9FE71A05E80544C0 CRC64;
     MAGQDSGNLK TVRLWRDAAL RARKLRSNLR QLTLSCPGAG GDPLESPDAP QLVLPANIGD
     IEVLNLGNNG LEDVPEGLGS ALGSLRVLVL RRNRFARLPP AVAELGHHLT ELDVSHNRLT
     ILGAEVVSAL RELRKLNLSH NQLPALPAQL GALAHLEELD VSFNRLAHLP DSFSCLNHLR
     TLDVDHNQLT AFPQQLLQLA ALEELDVSSN RLRGLPEDIS ALRALKILWL SGAELGTLPR
     GFCELASLES LMLDNNGLQA LPDEFSRLQR LKMLNLSSNL FEEFPAALLP LAGLEELYLS
     RNQLTSVPSL IAGLGRLLTL WLDNNRIRYL PDSIVELTGL EELVLQGNQI AVLPDNFGQL
     SRVGLWKIKD NPLIQPPYEV CMKGIPYIAA YQKELAHSQP AVQPRLKLLL MGHKAAGKTL
     LRHCLTEDKV EGGQGGGDKE KSYLPFPPLG SKGIEVTSWT ADASRGLRFI VYDLAGDESY
     EVIQPFFLSP GALYVLVVNL ATYEPRCFPT TVGSFLHRVG ARVPHAVVCI VGTHADLCGE
     RELEEKCLDI HRQIALQEKN DAEGLSHLAK VVDEALARDF ELRSASPHAA YYGVSDKNLR
     RRKAHFQYLL NHRLQILSPV LPVSCRDPLQ LQRLRDKLLS VAEHREIFPN LHRVLPRSWQ
     VLEELHFQPP QAQRLWLSWW DSARLGLQAG LTEDRLQSAL SYLHESGKLL YFEDSPALKE
     HVFHNLTRLI DILNVFFQRD ASLLLHKLLL GTNGEGEGEG ESFPTIAVPS PGQDPLRATQ
     LHHYVEGFLL HGLLPAHIIR LLLKPHVQAQ QDLQLLLELL EKMGLCYCLN KPKGKPLNGS
     AAWYKFPCYV QNEVPHAEAW INGTNLAGQS FVAEQLQIEY SFPFTFPPGL FARYSVQINS
     HVVHRSDGKF QIFAYRGKVP VVVSYRPAKG VLQPDTLSIA SHASLPNIWT AWQAITPLVE
     ELNVLLQEWP GLHYTVHILC SKCLKRGSPN PHAFPGELLS QPRPEGVAEI ICPKNGSERV
     NVALVYPPTP TVISPCSKKN VGEKHRNQ
//
ID   Q3V1N5_MOUSE            Unreviewed;       544 AA.
AC   Q3V1N5;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Heca;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK132340; BAE21115.1; -; mRNA.
DR   IPI; IPI00380838; -.
DR   RefSeq; NP_001028604.1; NM_001033432.3.
DR   UniGene; Mm.276430; -.
DR   UniGene; Mm.473073; -.
DR   ProteinModelPortal; Q3V1N5; -.
DR   STRING; Q3V1N5; -.
DR   PhosphoSite; Q3V1N5; -.
DR   PRIDE; Q3V1N5; -.
DR   Ensembl; ENSMUST00000037879; ENSMUSP00000040707; ENSMUSG00000039879.
DR   GeneID; 380629; -.
DR   KEGG; mmu:380629; -.
DR   UCSC; uc007elw.1; mouse.
DR   CTD; 380629; -.
DR   MGI; MGI:2685715; Heca.
DR   GeneTree; ENSGT00500000044928; -.
DR   HOGENOM; HBG715557; -.
DR   HOVERGEN; HBG049012; -.
DR   InParanoid; Q3V1N5; -.
DR   OMA; LQCFYEW; -.
DR   NextBio; 401036; -.
DR   ArrayExpress; Q3V1N5; -.
DR   Bgee; Q3V1N5; -.
DR   Genevestigator; Q3V1N5; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   544 AA;  59117 MW;  6DF8DC593B69E280 CRC64;
     MPNPKNSKGG RKNKRANSSG DEQENGAGAL AAAGATGAAA GGALAAAAAG CGAASPGAVG
     TGGAAGPGGA GTGAANATVA AGAAAAGDAK NGAPCATPLI CSFGRPVDLE KDDYQKVVCN
     NEHCPCSTWM HLQCFYEWES SILVQFNCIG RARSWNEKQC RQNMWTKKGY DLAFRFCSCR
     CGQGHLKKDT DWYQVKRMQD EKKKKSGSEK NTARPPGEAG EEAKKGRALN KPQKGLNHDL
     PRRHSMDRQN SQEKTVGSAA YGARSPCGSP GQSPPTGYSI LSPAHFSGPR SSRYLGEFLK
     NAIHLEPHKK AVPGGHVFRN AHFDYSSAGL SVHRAGHFDT PVQFLRRLDL SELLTHIPRH
     KLNTFHVRME DDAQVGQGED LRKFILAALS ASHRNVVNCA LCHRALPVFE QFPLVDGTLF
     LSPSRHDEIE YDVPCHLQGR LMHLYAVCVD CLEGVHKIIC IKCKSRWDGS WHQLGTMYTY
     DILAASPCCQ ARLNCKHCGK PVIDVRIGMQ YFSEYSNVQQ CPHCGNLDYH FVKPFSSFKV
     LEAY
//
ID   ESF1_MOUSE              Reviewed;         845 AA.
AC   Q3V1V3;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=ESF1 homolog;
DE   AltName: Full=ABT1-associated protein;
GN   Name=Esf1; Synonyms=Abtap;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 783-791, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-77; SER-79;
RP   SER-82; SER-686; SER-688 AND SER-689, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686; SER-688 AND
RP   SER-689, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686 AND SER-688, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; THR-305; SER-306;
RP   SER-307; SER-651; SER-657; SER-688 AND SER-689, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: May constitute a novel regulatory system for basal
CC       transcription. Negatively regulates ABT1 (By similarity).
CC   -!- SUBUNIT: Interacts with ABT1. Forms a complex with ABT1 and
CC       suppresses the ABT1-induced activation of polymerase II-directed
CC       transcription in mammalian cells (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity). Nucleus,
CC       nucleoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the ESF1 family.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK132230; BAE21046.1; -; mRNA.
DR   IPI; IPI00169521; -.
DR   RefSeq; NP_001074559.1; NM_001081090.1.
DR   UniGene; Mm.21228; -.
DR   ProteinModelPortal; Q3V1V3; -.
DR   STRING; Q3V1V3; -.
DR   PhosphoSite; Q3V1V3; -.
DR   PRIDE; Q3V1V3; -.
DR   Ensembl; ENSMUST00000046030; ENSMUSP00000036523; ENSMUSG00000045624.
DR   GeneID; 66580; -.
DR   KEGG; mmu:66580; -.
DR   UCSC; uc008mpn.1; mouse.
DR   CTD; 66580; -.
DR   MGI; MGI:1913830; Esf1.
DR   HOGENOM; HBG356818; -.
DR   HOVERGEN; HBG051149; -.
DR   InParanoid; Q3V1V3; -.
DR   OMA; VSDARFQ; -.
DR   OrthoDB; EOG4MKNFT; -.
DR   PhylomeDB; Q3V1V3; -.
DR   NextBio; 322060; -.
DR   ArrayExpress; Q3V1V3; -.
DR   Bgee; Q3V1V3; -.
DR   Genevestigator; Q3V1V3; -.
DR   GermOnline; ENSMUSG00000045624; Mus musculus.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR012580; NUC153.
DR   Pfam; PF08159; NUC153; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Direct protein sequencing; Nucleus; Phosphoprotein;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    845       ESF1 homolog.
FT                                /FTId=PRO_0000233166.
FT   COILED      775    803       Potential.
FT   COMPBIAS     87    212       Lys-rich.
FT   COMPBIAS    231    329       Glu-rich.
FT   COMPBIAS    561    740       Lys-rich.
FT   MOD_RES      75     75       Phosphoserine.
FT   MOD_RES      77     77       Phosphoserine.
FT   MOD_RES      79     79       Phosphoserine.
FT   MOD_RES      82     82       Phosphoserine.
FT   MOD_RES      90     90       Phosphoserine (By similarity).
FT   MOD_RES     156    156       Phosphoserine.
FT   MOD_RES     200    200       Phosphoserine (By similarity).
FT   MOD_RES     290    290       Phosphoserine (By similarity).
FT   MOD_RES     292    292       Phosphoserine (By similarity).
FT   MOD_RES     305    305       Phosphothreonine.
FT   MOD_RES     306    306       Phosphoserine.
FT   MOD_RES     307    307       Phosphoserine.
FT   MOD_RES     651    651       Phosphoserine.
FT   MOD_RES     657    657       Phosphoserine.
FT   MOD_RES     686    686       Phosphoserine.
FT   MOD_RES     688    688       Phosphoserine.
FT   MOD_RES     689    689       Phosphoserine.
FT   MOD_RES     729    729       Phosphoserine (By similarity).
SQ   SEQUENCE   845 AA;  98048 MW;  8EB7F2C2CFB997F5 CRC64;
     MSSKQEIMDD QRFRRVSKDP RFWEMPEKER KVKIDKRFRA MFHDKKFKLN YAVDKRGRPI
     SHSTTEDLKR FYDLSDSDSD LSDEESKILS QKKAKQKKKQ TKKEAKSIEK PIEEKKKETK
     KTDQKDSINK HDLNNSERVQ KMKNSQKPQK IDSEISPKKD NEEFLQNKKK KRGTTDLSVE
     ALPKGKLRTK DSSTSEMVKS STMSSSKAKR EKQSVVPVIM AKDNDGKMPD EDALEEDSDS
     ASELGSDEES EDEIISDGKT SADEDESEEE DEEEEEDSEE EEEEEEEDES DSGPDLARGK
     GNVETSSEDE DDLADLFPEE PGFEHAWREL DKDAPRADEI TRRLAVCNMD WDRLKAKDLL
     ALFNSFKPKG GVVFSVKIYP SEFGKERMKE EQVQGPVELL SIPEDAPEKD WASREKLRDY
     QFKRLKYYYA VAECDSPETA SKIYEDCDGL EFESSCSFID LRFIPDDITF DDEPKDVALE
     VDLTAYKPKY FTSAAMGTST VEITWDETDH ERITTLNRKF KKDELLDMDF QAYLASSSED
     EEEVEEAPEG EEGVNIGEDG KTKKSQKDDE EQIAKYRQLL QVIQEKEKKG KENDMEMEIK
     WVPGLKESAE EMVKNKLEGK DKLTPWEQFL EKKKEKKRLK KKQKALAEED SEDELPSDVD
     FNDPYFAEEV KKIGIKKKSM KSAKDSASSE EETDLEKQKA EMALLVMDEE EDSKKHFNYD
     KIVEHQNLSK KKKKQLMKKK ELVEDDFEVN VSDARFQAMY TSHLFNLDPS DPNFKKTKAM
     EKILEEKARH RERKEELLIQ AVERAQQDTG KPTQKQPMDP ALSMLIKSVK NKTEQFQARK
     KQRVK
//
ID   Q3V2X2_MOUSE            Unreviewed;      1181 AA.
AC   Q3V2X2;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-FEB-2011, entry version 40.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Kidins220;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK083260; BAE43383.1; -; mRNA.
DR   IPI; IPI00876533; -.
DR   UniGene; Mm.250641; -.
DR   UniGene; Mm.475357; -.
DR   STRING; Q3V2X2; -.
DR   Ensembl; ENSMUST00000110933; ENSMUSP00000106558; ENSMUSG00000036333.
DR   UCSC; uc007nfc.1; mouse.
DR   MGI; MGI:1924730; Kidins220.
DR   GeneTree; ENSGT00600000084024; -.
DR   HOVERGEN; HBG058824; -.
DR   PhylomeDB; Q3V2X2; -.
DR   ArrayExpress; Q3V2X2; -.
DR   Bgee; Q3V2X2; -.
DR   Genevestigator; Q3V2X2; -.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR011646; KAP_NTPase.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 3.
DR   Pfam; PF07693; KAP_NTPase; 1.
DR   SMART; SM00248; ANK; 7.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 6.
PE   2: Evidence at transcript level;
KW   ANK repeat; Repeat.
FT   NON_TER       1      1
SQ   SEQUENCE   1181 AA;  132116 MW;  07B3C488B5F36E87 CRC64;
     TPLVWAARKG HLECVKHLLA MGADVDQEGA NSMTALIVAV KGGYTQSVKE ILKRNPNVNL
     TDKDGNTALM IASKEGHIEI VQDLLDAGTY VNIPDRSGDT VLIGAVRGGH VEIVRALLQK
     YADIDIRGQD NKTALYWAVE KGNATMVRDI LQCNPDTEIC TKDGETPLIK ATKMRNIEVV
     ELLLDKGARV SAVDKKGDTP LHVAIRGRSR RLAELLLRNP KDGRLLYRPN KAGETPYNID
     CSHQKSILTQ IFGARHLSPT GTDGDMLGYD LYSSALADIL SEPTMQPPIC VGLYAQWGSG
     KSFLLKKLED EMKTFAGQQI EPLFQFSWLI VFLILLLCGG LGLVFAFTVD TNLAIAVSLS
     FLALLYIFFI VIYFGGRQEG ESWNWAWALS TRLARHIGYL ELLFKLMFVN PPELPEQTTK
     ALPVRFLFTD YNRLSSVGGE TSLAEMIATL SDACEREFGF LATRLFRVFK TEDSQGKKKW
     KKTCCLPSFI IFLFIVGCII AGITLLAIFR VDPKHLTVNA ILISIASIVG LAFVLNCRTW
     WQVLDSLLNS QRKRLHSAAS KLHKLKSEGF MKVLKCEVEL MARMAKTIDS FTQNQTRLVV
     IIDGLDACEQ DKVLQMLDTV RVLFSKGPFI AIFASDPHII IKAINQNLNS VLRDSNINGH
     DYMRNIVHLP VFLNSRGLSN ARKFLVTSAT NGDISCSEAT GVQEDADRRV SQNSLGEMTK
     LGSKTALNRR DTYRRRQMQR TITRQMSFDL TKLLVTEDWF SDISPQTMRR LLNIVSVTGR
     LLRANQITFN WDRLASWINL TEQWPYRTSW LILYLGETEG IPDQMTLKTI YERISKNIPT
     TKDVEPLLEI DGDIRNFEVF LSSRTPVLVA RDVKTFLPCT VNLDPKLREI IADVRAAREQ
     INIGGLAYPP LPLHEAPPRP PSGYSQPASV CSSSASFNGP FPGGVVSPQP HSSYYSGLSG
     PQHPFYNRPF FAPYLYTPRY YPGGSQHLIS RSSVKTSLPR DQNNGLASVP ATGTSLLLSS
     MTVDIVCEKL RQIEGLDQGM LPQYCTTIKK ANINGRVLAQ CNIDELKKEM AMNFGDWHLF
     RSMVLEMRSV ENQVVPEDPR FLNENSSAPV AHGESARRTS HSELPHTELS SQTPYTLNFS
     FEELNTLGLD EGAPRHSNLS WQEENAAPVL DRQRFRRSSL N
//
ID   GNAT3_MOUSE             Reviewed;         354 AA.
AC   Q3V3I2;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Guanine nucleotide-binding protein G(t) subunit alpha-3;
DE   AltName: Full=Gustducin alpha-3 chain;
GN   Name=Gnat3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-310.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=8657284; DOI=10.1038/381796a0;
RA   Wong G.T., Gannon K.S., Margolskee R.F.;
RT   "Transduction of bitter and sweet taste by gustducin.";
RL   Nature 381:796-800(1996).
RN   [4]
RP   DISRUPTION PHENOTYPE, AND TRANSGENE.
RX   PubMed=10407021;
RA   Wong G.T., Ruiz-Avila L., Margolskee R.F.;
RT   "Directing gene expression to gustducin-positive taste receptor
RT   cells.";
RL   J. Neurosci. 19:5802-5809(1999).
RN   [5]
RP   FUNCTION, AND SUBUNIT.
RX   MEDLINE=20040713; PubMed=10570481; DOI=10.1038/15981;
RA   Huang L., Shanker Y.G., Dubauskaite J., Zheng J.Z., Yan W.,
RA   Rosenzweig S., Spielman A.I., Max M., Margolskee R.F.;
RT   "Ggamma13 colocalizes with gustducin in taste receptor cells and
RT   mediates IP3 responses to bitter denatonium.";
RL   Nat. Neurosci. 2:1055-1062(1999).
RN   [6]
RP   FUNCTION.
RX   PubMed=11245589;
RA   Yan W., Sunavala G., Rosenzweig S., Dasso M., Brand J.G.,
RA   Spielman A.I.;
RT   "Bitter taste transduced by PLC-beta(2)-dependent rise in IP(3) and
RT   alpha-gustducin-dependent fall in cyclic nucleotides.";
RL   Am. J. Physiol. 280:C742-C751(2001).
RN   [7]
RP   DISRUPTION PHENOTYPE, AND TRANSGENE.
RX   PubMed=11447270; DOI=10.1073/pnas.151235798;
RA   Ruiz-Avila L., Wong G.T., Damak S., Margolskee R.F.;
RT   "Dominant loss of responsiveness to sweet and bitter compounds caused
RT   by a single mutation in alpha-gustducin.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:8868-8873(2001).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=14637165; DOI=10.1016/j.bbrc.2003.10.137;
RA   Kim M.-R., Kusakabe Y., Miura H., Shindo Y., Ninomiya Y., Hino A.;
RT   "Regional expression patterns of taste receptors and gustducin in the
RT   mouse tongue.";
RL   Biochem. Biophys. Res. Commun. 312:500-506(2003).
RN   [9]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=14586025;
RA   Caicedo A., Pereira E., Margolskee R.F., Roper S.D.;
RT   "Role of the G-protein subunit alpha-gustducin in taste cell responses
RT   to bitter stimuli.";
RL   J. Neurosci. 23:9947-9952(2003).
RN   [10]
RP   DEVELOPMENTAL STAGE.
RX   MEDLINE=22989846; PubMed=14627646;
RA   Grillet N., Dubreuil V., Dufour H.D., Brunet J.-F.;
RT   "Dynamic expression of RGS4 in the developing nervous system and
RT   regulation by the neural type-specific transcription factor Phox2b.";
RL   J. Neurosci. 23:10613-10621(2003).
RN   [11]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=15342734; DOI=10.1523/JNEUROSCI.2441-04.2004;
RA   He W., Yasumatsu K., Varadarajan V., Yamada A., Lem J., Ninomiya Y.,
RA   Margolskee R.F., Damak S.;
RT   "Umami taste responses are mediated by alpha-transducin and alpha-
RT   gustducin.";
RL   J. Neurosci. 24:7674-7680(2004).
RN   [12]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16933139; DOI=10.1007/s00429-006-0112-2;
RA   Zhang G.-H., Deng S.-P., Li L.-L., Li H.-T.;
RT   "Developmental change of alpha-gustducin expression in the mouse
RT   fungiform papilla.";
RL   Anat. Embryol. (Berl.) 211:625-630(2006).
RN   [13]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=16740645; DOI=10.1093/chemse/bjj062;
RA   Danilova V., Damak S., Margolskee R.F., Hellekant G.;
RT   "Taste responses to sweet stimuli in alpha-gustducin knockout and
RT   wild-type mice.";
RL   Chem. Senses 31:573-580(2006).
RN   [14]
RP   TISSUE SPECIFICITY.
RX   PubMed=17290008; DOI=10.1152/ajpgi.00504.2006;
RA   Sutherland K., Young R.L., Cooper N.J., Horowitz M., Blackshaw L.A.;
RT   "Phenotypic characterization of taste cells of the mouse small
RT   intestine.";
RL   Am. J. Physiol. 292:G1420-G1428(2007).
RN   [15]
RP   TISSUE SPECIFICITY.
RX   PubMed=17229761; DOI=10.1093/chemse/bjl053;
RA   Stone L.M., Barrows J., Finger T.E., Kinnamon S.C.;
RT   "Expression of T1Rs and gustducin in palatal taste buds of mice.";
RL   Chem. Senses 32:255-262(2007).
RN   [16]
RP   TISSUE SPECIFICITY.
RX   PubMed=17021831; DOI=10.1007/s00359-006-0168-8;
RA   Fehr J., Meyer D., Widmayer P., Borth H.C., Ackermann F., Wilhelm B.,
RA   Gudermann T., Boekhoff I.;
RT   "Expression of the G-protein alpha-subunit gustducin in mammalian
RT   spermatozoa.";
RL   J. Comp. Physiol. A 193:21-34(2007).
RN   [17]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17724330; DOI=10.1073/pnas.0706890104;
RA   Jang H.-J., Kokrashvili Z., Theodorakis M.J., Carlson O.D., Kim B.-J.,
RA   Zhou J., Kim H.H., Xu X., Chan S.L., Juhaszova M., Bernier M.,
RA   Mosinger B., Margolskee R.F., Egan J.M.;
RT   "Gut-expressed gustducin and taste receptors regulate secretion of
RT   glucagon-like peptide-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:15069-15074(2007).
RN   [18]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=17724332; DOI=10.1073/pnas.0706678104;
RA   Margolskee R.F., Dyer J., Kokrashvili Z., Salmon K.S., Ilegems E.,
RA   Daly K., Maillet E.L., Ninomiya Y., Mosinger B., Shirazi-Beechey S.P.;
RT   "T1R3 and gustducin in gut sense sugars to regulate expression of Na+-
RT   glucose cotransporter 1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:15075-15080(2007).
CC   -!- FUNCTION: Guanine nucleotide-binding protein (G protein) alpha
CC       subunit playing a prominent role in bitter and sweet taste
CC       transduction as well as in umami (monosodium glutamate,
CC       monopotassium glutamate, and inosine monophosphate) taste
CC       transduction. Transduction by this alpha subunit involves coupling
CC       of specific cell-surface receptors with a cGMP-phosphodiesterase;
CC       Activation of phosphodiesterase lowers intracellular levels of
CC       cAMP and cGMP which may open a cyclic nucleotide-suppressible
CC       cation channel leading to influx of calcium, ultimately leading to
CC       release of neurotransmitter. Indeed, denatonium and strychnine
CC       induce transient reduction in cAMP and cGMP in taste tissue,
CC       whereas this decrease is inhibited by GNAT3 antibody. Gustducin
CC       heterotrimer transduces response to bitter and sweet compounds via
CC       regulation of phosphodiesterase for alpha subunit, as well as via
CC       activation of phospholipase C for beta and gamma subunits, with
CC       ultimate increase inositol trisphosphate and increase of
CC       intracellular Calcium. GNAT3 can functionally couple to taste
CC       receptors to transmit intracellular signal: receptor heterodimer
CC       TAS1R2/TAS1R3 senses sweetness and TAS1R1/TAS1R3 transduces umami
CC       taste, whereas the T2R family GPCRs act as bitter sensors.
CC       Functions also as lumenal sugar sensors in the gut to control the
CC       expression of the Na+-glucose transporter SGLT1 in response to
CC       dietaty sugar, as well as the secretion of Glucagon-like peptide-
CC       1, GLP-1 and glucose-dependent insulinotropic polypeptide, GIP.
CC       Thus, may modulate the gut capacity to absorb sugars, with
CC       implications in malabsorption syndromes and diet-related disorders
CC       including diabetes and obesity.
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and
CC       gamma, respectively GNAT3, GNB1 and GNG13 for Gustducin
CC       heterotrimer for bitter taste transduction. The alpha chain
CC       contains the guanine nucleotide binding site. Gustducin
CC       heterotrimer may also be composed of GNAT3, GNB3 and GNG13.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in taste buds (sensory organs of
CC       clustered epithelial cells) of the circumvallate and fungiform
CC       papillae of the tongue as well as in palatal taste buds at protein
CC       level. Expressed in enteroendocrine cells of the gut, such as in
CC       subsets of enteroendocrine cells in the midjejunum and brush
CC       cells. Detected also in spermatozoa.
CC   -!- DEVELOPMENTAL STAGE: From week 1 to 7, the number of cells
CC       expressing GNAT3 in single taste buds increases within fungiform
CC       papilla; by week 7, the number reached the value found in adults.
CC       Expressed in cell bodies and axons of facial motor neurons at
CC       E10.5.
CC   -!- PTM: Potential N-myristoylation may anchor alpha-subunit to the
CC       inner surface of plasma membrane (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice are not affected in their tasting
CC       ability for salty (NaCl) and sour (HCl) stimuli, which are known
CC       not to be mediated by G proteins; but, they exhibit a significant
CC       reduction in the ability to taste the bitter compounds denatonium
CC       and quinine as well as the sweet compounds sucrose and SC45647, a
CC       guanidine sweetener. The incidence of cells responding to bitter
CC       stimulus is also reduced by seventy per cent. The residual
CC       behavorial response to bitter and sweet taste in these deficient
CC       mice suggests that there is alternative mechanism to compensate.
CC       However, transgenic expression of Gnat3 in these deficient mice
CC       restores responsiveness to both bitter and sweet compounds,
CC       whereas expression of mutated 'Gly-352' transgene do not.
CC       Furthermore, in wild-type mice, this mutated transgene acts as
CC       dominant-negative by inhibition of endogenous Gnat3 interactions
CC       with taste receptors. Mice show less preference for acesulfame-K,
CC       dulcin, fructose, D-phenylalanine, L-proline, D-tryptophan,
CC       saccharin, sweetener SC45647 and sucrose; Furthermore, in their
CC       gut, sugar or sweeteners do not increase SGLT1 expression and
CC       glucose-absorptive capacity compared to wild-type mice and the
CC       ingestion of glucose reveals deficiencies in secretion of GLP-1
CC       and regulation of plasma insulin and glucose. Mice lacking GNAT3
CC       show less preference for umami compounds such as monosodium
CC       glutamate (MSG) and no preference for inosine monophosphate (IMP)
CC       whereas wild-type mice strongly prefer IMP. The response to umami
CC       signals implicates the anteriorly placed taste buds of the tongue,
CC       and not the posterior part.
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; AC129572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK040065; BAE20568.1; -; mRNA.
DR   IPI; IPI00347770; -.
DR   RefSeq; NP_001074612.1; NM_001081143.1.
DR   UniGene; Mm.332230; -.
DR   HSSP; P10824; 1AGR.
DR   ProteinModelPortal; Q3V3I2; -.
DR   SMR; Q3V3I2; 12-354.
DR   STRING; Q3V3I2; -.
DR   PRIDE; Q3V3I2; -.
DR   Ensembl; ENSMUST00000030561; ENSMUSP00000030561; ENSMUSG00000028777.
DR   GeneID; 242851; -.
DR   KEGG; mmu:242851; -.
DR   CTD; 242851; -.
DR   MGI; MGI:3588268; Gnat3.
DR   eggNOG; maNOG05766; -.
DR   GeneTree; ENSGT00560000076725; -.
DR   HOGENOM; HBG444960; -.
DR   HOVERGEN; HBG063184; -.
DR   InParanoid; Q3V3I2; -.
DR   OMA; IIHKNGY; -.
DR   OrthoDB; EOG47D9GD; -.
DR   PhylomeDB; Q3V3I2; -.
DR   NextBio; 385586; -.
DR   Bgee; Q3V3I2; -.
DR   Genevestigator; Q3V3I2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IDA:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; IDA:MGI.
DR   GO; GO:0050913; P:sensory perception of bitter taste; IMP:MGI.
DR   GO; GO:0050916; P:sensory perception of sweet taste; IMP:MGI.
DR   GO; GO:0050917; P:sensory perception of umami taste; IMP:MGI.
DR   InterPro; IPR001408; Gprotein_alpha_I.
DR   InterPro; IPR001019; Gprotein_alpha_su.
DR   InterPro; IPR011025; GproteinA_insert.
DR   Gene3D; G3DSA:1.10.400.10; GproteinA_insert; 1.
DR   PANTHER; PTHR10218; Gprotein_alph_bd; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00441; GPROTEINAI.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF47895; Transducn_insert; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; GTP-binding; Lipoprotein; Myristate; Nucleotide-binding;
KW   Transducer.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    354       Guanine nucleotide-binding protein G(t)
FT                                subunit alpha-3.
FT                                /FTId=PRO_0000342672.
FT   NP_BIND      40     47       GTP (By similarity).
FT   NP_BIND     200    204       GTP (By similarity).
FT   NP_BIND     269    272       GTP (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
SQ   SEQUENCE   354 AA;  40316 MW;  05DBC95DAC356CEF CRC64;
     MGSGISSESK ESARRSKELE KKLQEDAERD ARTVKLLLLG AGESGKSTIV KQMKIIHKNG
     YSKQECMEFK AVIYSNTLQS ILAIVKAMAT LGIDYVNPRS REDQEQLHSM ANTLEDGDMT
     PQLAEIIKRL WGDPGIQACF ERASEYQLND SAAYYLNDLD RLTAPGYVPN EQDVLHSRVK
     TTGIIETQFS FKDLNFRMFD VGGQRSERKK WIHCFEGVTC IIFCAALSAY DMVLVEDEEV
     NRMHESLHLF NSICNHKYFA TTSIVLFLNK KDLFQEKVAK VHLSICFPEY TGPNTFEDAG
     NYIKNQFLDL NLKKEDKEIY SHMTCATDTQ NVKFVFDAVT DIIIKENLKD CGLF
//
ID   PACS2_MOUSE             Reviewed;         862 AA.
AC   Q3V3Q7; Q80TW2; Q80VG3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   RecName: Full=Phosphofurin acidic cluster sorting protein 2;
DE            Short=PACS-2;
DE   AltName: Full=PACS1-like protein;
GN   Name=Pacs2; Synonyms=Kiaa0602, Pacs1l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-862.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 647-862.
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Multifunctional sorting protein that controls the
CC       endoplasmic reticulum (ER)-mitochondria communication, including
CC       the apposition of mitochondria with the ER and ER homeostasis. In
CC       addition, in response to apoptic inducer, translocates BIB to
CC       mitochondria, which initiates a sequence of events including the
CC       formation of mitochondrial truncated BID, the release of
CC       cytochrome c, the activation of caspase-3 thereby causing cell
CC       death. May also involved in ion channel trafficking, directing
CC       acidic cluster-containing ion channels to distict subcellular
CC       compartements (By similarity).
CC   -!- SUBUNIT: Interacts with BID and PKD2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Mitochondrion
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the PACS family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK036581; BAE20504.1; -; mRNA.
DR   EMBL; AK122326; BAC65608.1; -; mRNA.
DR   EMBL; BC043302; AAH43302.1; -; mRNA.
DR   IPI; IPI00341619; -.
DR   UniGene; Mm.35754; -.
DR   STRING; Q3V3Q7; -.
DR   PhosphoSite; Q3V3Q7; -.
DR   PRIDE; Q3V3Q7; -.
DR   Ensembl; ENSMUST00000019147; ENSMUSP00000019147; ENSMUSG00000021143.
DR   UCSC; uc007pfp.1; mouse.
DR   MGI; MGI:1924399; Pacs2.
DR   eggNOG; roNOG08262; -.
DR   HOVERGEN; HBG053488; -.
DR   OrthoDB; EOG4MSCXN; -.
DR   ArrayExpress; Q3V3Q7; -.
DR   Bgee; Q3V3Q7; -.
DR   CleanEx; MM_PACS2; -.
DR   Genevestigator; Q3V3Q7; -.
DR   GermOnline; ENSMUSG00000021143; Mus musculus.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   InterPro; IPR019381; Phosphofurin_acidic_CS-1.
DR   Pfam; PF10254; Pacs-1; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Endoplasmic reticulum; Mitochondrion; Phosphoprotein.
FT   CHAIN         1    862       Phosphofurin acidic cluster sorting
FT                                protein 2.
FT                                /FTId=PRO_0000259512.
FT   COMPBIAS    274    279       Poly-Asp.
FT   COMPBIAS    658    710       Ser-rich.
FT   MOD_RES     313    313       Phosphoserine.
FT   MOD_RES     319    319       Phosphoserine (By similarity).
FT   CONFLICT     56     68       EKELLSVVIAVKM -> GQVETDLALTFSL (in Ref.
FT                                2; BAC65608).
FT   CONFLICT    122    122       L -> V (in Ref. 2; BAC65608).
FT   CONFLICT    250    250       S -> P (in Ref. 2; BAC65608).
SQ   SEQUENCE   862 AA;  94936 MW;  789901C7FE800CC7 CRC64;
     MAERGRLGLP GAPGALNTPV PMNLFATWEV DGSSPSCVPR LCSLTLKKLA VLRELEKELL
     SVVIAVKMQY PHFLKREGNK LQIMLQRRKR YKNRTILGYK TLAAGSINMA EVMQHPSEGG
     QLLSLCSSIK EASVKVAEIW IVSLSSQPID HEDSAMQAGP KTKSTDNYSE EEYESFSSEQ
     EASDDAVQGQ DLDEDDFDVG KPKKQRRSIV RTTSMTRQQN FKQKVVALLR RFKVSEEVLD
     SEQDPAEHVS EVEEDLDLLY DTLDVENPSD SGPDMDDDDS VLSTPKPKLR PYFEGLSHSS
     SQTEIGSIHS ARSHREPPSP ADVPEKTRSL GGKQQLSDSV SDTVALSAAV PREPSGQPED
     SPEAETSTLD VFTEKLPPSG RIIKTESLVI PSTRSESKPA GRRGRSTSLK ERQPARPQNE
     RANSLDNERC PDTRSQLQIP RKTVYDQLNH ILISDDQLPE NIILVNTSDW QGQFLSDVLQ
     KHTLPVVCTC SAADVQAAFS TIVSRIQRYC NCNSQPPTPV KIAVAGAQHY LSAILRLFVE
     QLSHKTPDWL GYMRFLIIPL GSHPVARYLG SVDYRYNNFF QDLAWRDLFN KLEAQSSVQD
     TPDIVSRITQ YISGANCAHQ LPIAEAMLTY KQKSPDEESS QRFIPFVGVV KVGIVEPSSA
     TSGDSDDAAP SSSSILSSTP PSASTSPAAK EASPTPPSSP SVSGGLSSPS QGVGAELMGL
     QVDYWTAAQP ADRKRDAEKK DMPTTKNTLK CTFRSLQVSR LPSSGEAAAT PTMSMTVVTK
     EKNKKVMFLP KKTKDKEVES KSQCIEGISR LICTAKHQQN MLRVLIDGVE CSDVKFFQLA
     AQWSSHVKHF PICIFGHSKA TF
//
ID   C1TM_MOUSE              Reviewed;         977 AA.
AC   Q3V3R1; Q3TVQ0; Q3V402; Q80V98; Q8CAL0; Q8K2N5;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   08-MAR-2011, entry version 47.
DE   RecName: Full=Monofunctional C1-tetrahydrofolate synthase, mitochondrial;
DE            EC=6.3.4.3;
DE   AltName: Full=Formyltetrahydrofolate synthetase;
DE   Flags: Precursor;
GN   Name=Mthfd1l; Synonyms=Fthfsdc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 167-977.
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION.
RX   PubMed=15611115; DOI=10.1074/jbc.M409380200;
RA   Christensen K.E., Patel H., Kuzmanov U., Mejia N.R., MacKenzie R.E.;
RT   "Disruption of the mthfd1 gene reveals a monofunctional 10-
RT   formyltetrahydrofolate synthetase in mammalian mitochondria.";
RL   J. Biol. Chem. 280:7597-7602(2005).
RN   [4]
RP   STRUCTURE BY NMR OF 510-573.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the insertion region (510-573) of FTHFS domain
RT   from mouse methylenetetrahydrofolate dehydrogenase (NADP+ dependent)
RT   1-like protein.";
RL   Submitted (OCT-2007) to the PDB data bank.
CC   -!- FUNCTION: May provide the missing metabolic reaction required to
CC       link the mitochondria and the cytoplasm in the mammalian model of
CC       one-carbon folate metabolism in embryonic an transformed cells
CC       complementing thus the enzymatic activities of MTHFD2.
CC   -!- CATALYTIC ACTIVITY: ATP + formate + tetrahydrofolate = ADP +
CC       phosphate + 10-formyltetrahydrofolate.
CC   -!- PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- DOMAIN: This monofunctional enzyme consists of two major domains:
CC       an N-terminal inactive methylene-THF dehydrogenase and
CC       cyclohydrolase domain and an active larger formyl-THF synthetase
CC       C-terminal domain.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       tetrahydrofolate dehydrogenase/cyclohydrolase family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the formate--
CC       tetrahydrofolate ligase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH30437.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK038579; BAC30053.1; -; mRNA.
DR   EMBL; AK028211; BAE20438.1; -; mRNA.
DR   EMBL; AK036284; BAE20500.1; -; mRNA.
DR   EMBL; AK160025; BAE35568.1; -; mRNA.
DR   EMBL; BC030437; AAH30437.1; ALT_INIT; mRNA.
DR   EMBL; BC049936; AAH49936.1; -; mRNA.
DR   IPI; IPI00875833; -.
DR   RefSeq; NP_001164256.1; NM_001170785.1.
DR   RefSeq; NP_001164257.1; NM_001170786.1.
DR   RefSeq; NP_758512.3; NM_172308.4.
DR   UniGene; Mm.184752; -.
DR   PDB; 2EO2; NMR; -; A=510-573.
DR   PDBsum; 2EO2; -.
DR   ProteinModelPortal; Q3V3R1; -.
DR   SMR; Q3V3R1; 65-338, 370-976.
DR   STRING; Q3V3R1; -.
DR   PhosphoSite; Q3V3R1; -.
DR   REPRODUCTION-2DPAGE; Q3V3R1; -.
DR   Ensembl; ENSMUST00000043735; ENSMUSP00000036178; ENSMUSG00000040675.
DR   Ensembl; ENSMUST00000105585; ENSMUSP00000101210; ENSMUSG00000040675.
DR   Ensembl; ENSMUST00000117291; ENSMUSP00000112870; ENSMUSG00000040675.
DR   Ensembl; ENSMUST00000120585; ENSMUSP00000112897; ENSMUSG00000040675.
DR   GeneID; 270685; -.
DR   KEGG; mmu:270685; -.
DR   CTD; 270685; -.
DR   MGI; MGI:1924836; Mthfd1l.
DR   eggNOG; roNOG07951; -.
DR   GeneTree; ENSGT00600000084426; -.
DR   HOGENOM; HBG677721; -.
DR   HOVERGEN; HBG004916; -.
DR   InParanoid; Q3V3R1; -.
DR   OrthoDB; EOG4ZCT3W; -.
DR   NextBio; 393373; -.
DR   ArrayExpress; Q3V3R1; -.
DR   Bgee; Q3V3R1; -.
DR   Genevestigator; Q3V3R1; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004329; F:formate-tetrahydrofolate ligase activity; IEA:EC.
DR   GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000559; Formate_THF_ligase.
DR   InterPro; IPR020628; Formate_THF_ligase_CS.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR000672; THF_DH/CycHdrlase.
DR   InterPro; IPR020630; THF_DH/CycHdrlase_cat_dom.
DR   InterPro; IPR020631; THF_DH/CycHdrlase_NAD-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF01268; FTHFS; 1.
DR   Pfam; PF00763; THF_DHG_CYH; 1.
DR   Pfam; PF02882; THF_DHG_CYH_C; 1.
DR   PRINTS; PR00085; THFDHDRGNASE.
DR   PROSITE; PS00721; FTHFS_1; 1.
DR   PROSITE; PS00722; FTHFS_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Ligase; Mitochondrion;
KW   Nucleotide-binding; One-carbon metabolism; Transit peptide.
FT   TRANSIT       1     31       Mitochondrion (Potential).
FT   CHAIN        32    977       Monofunctional C1-tetrahydrofolate
FT                                synthase, mitochondrial.
FT                                /FTId=PRO_0000343178.
FT   NP_BIND     422    429       ATP (By similarity).
FT   REGION       32    347       Methylenetetrahydrofolate dehydrogenase
FT                                and cyclohydrolase.
FT   REGION      348    977       Formyltetrahydrofolate synthetase.
FT   MOD_RES     173    173       N6-acetyllysine (By similarity).
FT   MOD_RES     188    188       N6-acetyllysine (By similarity).
FT   CONFLICT    137    137       D -> N (in Ref. 1; BAE35568).
FT   CONFLICT    279    279       V -> A (in Ref. 1; BAE35568 and 2;
FT                                AAH30437/AAH49936).
FT   CONFLICT    353    353       Q -> H (in Ref. 1; BAE35568).
FT   CONFLICT    369    369       T -> N (in Ref. 1; BAE20500).
FT   CONFLICT    419    419       I -> V (in Ref. 1; BAC30053).
FT   CONFLICT    422    422       T -> S (in Ref. 1; BAE35568).
FT   CONFLICT    632    632       V -> A (in Ref. 1; BAE35568).
FT   CONFLICT    963    963       D -> G (in Ref. 1; BAE20438).
FT   HELIX       514    521
FT   HELIX       533    541
FT   TURN        549    551
FT   HELIX       554    562
SQ   SEQUENCE   977 AA;  105729 MW;  7275EF6F9A4292D6 CRC64;
     MSVRLPLLLR QLGRQQLPSG PACRLRELCR SGSRSSSSGG GDPEGLRGRR LQDGQTFSSH
     GPGNPEAPGM DSIVRDVIHN SKEVLSLLQE KNPAFKPVLV VIQAGDDNLM KDMNQNLAKE
     AGLDITHICL PPDSGEDEII DEILKINEDP RVHGLTLQIS EDSLSNKVLN ALKPEKDVDG
     VTDINLGKLV RGDAPECFVS PLAKAAVELV EKSGITLDGK KVLVVGAHGP LEAALQWLFQ
     RKGSMTMSCP WATPQLPDKL READIVVLGS PKPEEIPAVW IPSGTTILNC FHDFLSGKLS
     GGSPGVPVDK LIAEESVSLL AAALRIQNMV SSGRRWLREQ QHRRWRLHCL KLQPLSPVPS
     DIEISRGQTP KAVDVLAKEI GLLADEIEIY GKSKAKVQLS LLERLKDQTD GKYVLVAGIT
     PTPLGEGKST VTIGLVQALT AHLKVNSFAC LRQPSQGPTF GVKGGAAGGG YAQVIPMEEF
     NLHLTGDIHA ITAANNLLAA AIDTRILHES TQTDKALYNR LVPLVNGVRE FSEIQLSRLK
     KLGIHKTDPS TLTEEEVRKF ARLNIDPATI TWQRVLDTND RFLRKITIGQ GSTEKGYSRQ
     AQFDIAVASE IMAVLALTDS LTDMKERLGR MVVASDKDGQ PVTAEDLGVT GALTVLMKDA
     IKPNLMQTLE GTPVFVHAGP FANIAHGNSS VLADKIALKL VGEEGFVVTE AGFGADIGME
     KFFNIKCRAS GLVPNVVVLV ATVRALKMHG GGPSVTAGVP LKKEYTEENI QLVADGCCNL
     QKQIQIAQLF GVPVVVALNV FKTDTRAEID LVCELAKRAG AFDAVPCYHW SAGGKGSVDL
     ARAVREAANK RSRFQFLYDV QLPIVEKIRV IAQTVYGAKD IELSPEAQSK IDRYTQQGFG
     NLPICMAKTH LSLSHEPDKK GVPRDFTLPI SDVRASIGAG FIYPLVGTMS TMPGLPTRPC
     FYDIDLDTET EQVKGLF
//
ID   Q3V3S8_MOUSE            Unreviewed;       497 AA.
AC   Q3V3S8;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Ppp2r5b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK034167; BAE20490.1; -; mRNA.
DR   IPI; IPI00356872; -.
DR   UniGene; Mm.118076; -.
DR   ProteinModelPortal; Q3V3S8; -.
DR   SMR; Q3V3S8; 65-437.
DR   STRING; Q3V3S8; -.
DR   Ensembl; ENSMUST00000025695; ENSMUSP00000025695; ENSMUSG00000024777.
DR   MGI; MGI:2388480; Ppp2r5b.
DR   eggNOG; maNOG18849; -.
DR   HOGENOM; HBG602178; -.
DR   HOVERGEN; HBG000009; -.
DR   InParanoid; Q3V3S8; -.
DR   OrthoDB; EOG4M65HP; -.
DR   PhylomeDB; Q3V3S8; -.
DR   ArrayExpress; Q3V3S8; -.
DR   Bgee; Q3V3S8; -.
DR   Genevestigator; Q3V3S8; -.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:InterPro.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0008601; F:protein phosphatase type 2A regulator activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002554; PP2A_B56.
DR   PANTHER; PTHR10257; B56; 1.
DR   Pfam; PF01603; B56; 1.
DR   PIRSF; PIRSF028043; PP2A_B56; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   497 AA;  57370 MW;  9A260CE0DE5BF6D2 CRC64;
     METKLPPAST PTSPSSPGLS PVPPPDKVDG FSRRSLRRAR PRRSHSSSQF RYQSNQQELT
     PLPLLKDVPA SELHELLSRK LAQCGVMFDF LDCVADLKGK EVKRAALNEL VECVGCTRGV
     LIEPVYPDII RMISVNIFRT LPPSENPEFD PEEDEPNLEP SWPHLQLVYE FFLRFLESPD
     FQPSVAKRYV DQKFVLMLLE LFDSEDPRER EYLKTILHRV YGKFLGLRAY IRKQCNHIFL
     RFIYELEHFN GVAELLEILG SIINGFALPL KTEHKQFLVR VLIPLHSVKS LSVFHAQLAY
     CVVQFLEKDA TLTEHVIRGL LKYWPKTCTQ KEVMFLGEME EILDVIEPSQ FVKIQEPLFK
     QVARCVSSPH FQVAERALYF WNNEYILSLI EDNCHTVLPA VFGTLYQVSK EHWNQTIVSL
     IYNVLKTFME MNGKLFDELT ASYKLEKQQE QQKAQERREL WRGLEELRLR RLQGTQGAKE
     APVPRPTPQV AASGGQS
//
ID   LR16C_MOUSE             Reviewed;        1296 AA.
AC   Q3V3V9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   08-MAR-2011, entry version 40.
DE   RecName: Full=Leucine-rich repeat-containing protein 16C;
DE   AltName: Full=RGD, leucine-rich repeat, tropomodulin and proline-rich-containing protein;
GN   Name=Rltpr; Synonyms=Lrrc16c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3V3V9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3V3V9-2; Sequence=VSP_032634, VSP_032635;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 15 LRR (leucine-rich) repeats.
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DR   EMBL; AK031012; BAE20471.1; -; mRNA.
DR   EMBL; AC152826; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00355099; -.
DR   IPI; IPI00889268; -.
DR   RefSeq; NP_001028492.1; NM_001033320.2.
DR   UniGene; Mm.471640; -.
DR   ProteinModelPortal; Q3V3V9; -.
DR   SMR; Q3V3V9; 209-642.
DR   PhosphoSite; Q3V3V9; -.
DR   PRIDE; Q3V3V9; -.
DR   Ensembl; ENSMUST00000062574; ENSMUSP00000052322; ENSMUSG00000050357.
DR   GeneID; 234695; -.
DR   KEGG; mmu:234695; -.
DR   UCSC; uc009ndo.1; mouse.
DR   CTD; 234695; -.
DR   MGI; MGI:2685431; Rltpr.
DR   GeneTree; ENSGT00390000014487; -.
DR   HOVERGEN; HBG108095; -.
DR   OrthoDB; EOG4RV2QN; -.
DR   Bgee; Q3V3V9; -.
DR   Genevestigator; Q3V3V9; -.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Leucine-rich repeat; Phosphoprotein; Repeat.
FT   CHAIN         1   1296       Leucine-rich repeat-containing protein
FT                                16C.
FT                                /FTId=PRO_0000326239.
FT   REPEAT       63     87       LRR 1.
FT   REPEAT       88    110       LRR 2.
FT   REPEAT      248    271       LRR 3.
FT   REPEAT      273    296       LRR 4.
FT   REPEAT      305    328       LRR 5.
FT   REPEAT      363    386       LRR 6.
FT   REPEAT      395    415       LRR 7.
FT   REPEAT      426    448       LRR 8.
FT   REPEAT      453    477       LRR 9.
FT   REPEAT      480    506       LRR 10.
FT   REPEAT      515    538       LRR 11.
FT   REPEAT      542    565       LRR 12.
FT   REPEAT      570    594       LRR 13.
FT   REPEAT      598    621       LRR 14.
FT   REPEAT      836    859       LRR 15.
FT   REGION      507    601       Tropomodulin-like.
FT   COMPBIAS   1199   1296       Pro-rich.
FT   MOD_RES    1008   1008       Phosphoserine (By similarity).
FT   MOD_RES    1134   1134       Phosphoserine (By similarity).
FT   VAR_SEQ       1    603       Missing (in isoform 2).
FT                                /FTId=VSP_032634.
FT   VAR_SEQ     873    928       VLLRKRNGTPSWQLRGKMQSRRLGRLHAVAEKHWAAGPRDT
FT                                PASAVYQRVDVCVGW -> DESSSWKWLEPSNCFHLVSSLH
FT                                GAAEEAERDPELAAPGEDAEPQAGPSARGSPSPAAPGPPAG
FT                                PLPRMDLPPAGQPLRHPTRARPRPRRQHHHRPPPGGPQ
FT                                (in isoform 2).
FT                                /FTId=VSP_032635.
SQ   SEQUENCE   1296 AA;  141372 MW;  9FB10DA18A26BCAA CRC64;
     MAQTPDDISC ELRGEITRFL WPKEAELLLK TWLPQEGAEQ SHILALLRWR AYLLHTCLPL
     RVDCTFSYLE VQAMALQETP PRVTFELESL PELVLEFPCV AALEQLAQHV AAAIKKVFPR
     STLGKLFRKP TPSSLLARLE RSHPLESTIP SSPCGGFLET YEALCDYNGF PFREEIQWDV
     DTIYHRQGCR HFCLGDFSHF GSRDLALSVA ALSYNLWFRR LSCEDMKLSL EVSEQILHMT
     SQSSYLEELV LEACGLRGDF VRRLAQALAG HFNSGLRELS LSGNLLDDRG MRALGRALAT
     NATFDSTLTH LDLSGNPGAL GPSQDSGGLY TFLSRPNVLA YLNLAGTDAT LGTLFTALAG
     GCCSSLTHLE ASRNIFSRMK SQAAPAALQR FLGGTRMLRH LGLAGCKLPP EALRALLEGL
     ALNTQIHDLH LDLSACELRS VGAQVIQDLV CDAGALSSLD LSDNGFGSDM VTLVLAIGRS
     RSLKHVALGR NFNVRCKETL DDVLHRIAQL MQDDDCPLQS LSVAESRLKQ GASILIRALG
     TNPKLTALDI SGNAIGDAGA KMLAKALRVN TRLRSVIWDR NNTSALGLLD VAQALEQNHS
     LKSMPLPLND VTQAHRSRPE LTTRAVHQIQ ACLWRNNQVD STSDLKPCLQ PLGLISDHSE
     QEVNELCQSV QEHMELLGCG AGPQGEVAVH QAEDAIQNAN FSLSILPILY EAGRSPSHHW
     QLQQKLESLL GQVGEICRQD IQDFTQTTLD TTRSLCPQML QTPGWRKQLE GVLVGSGGLP
     ELLPEHLLQD AFSRLRDMRL SITGTLAESI VAQALAGLHA ARDRLVERLT QQAPVTMAPA
     VPPLGGNELS PLETGGLEEL FFPTEKEEER EKVLLRKRNG TPSWQLRGKM QSRRLGRLHA
     VAEKHWAAGP RDTPASAVYQ RVDVCVGWVP PALLQEGNGL TARVDEGVEE FFSKRLIQQD
     HFWAPEEDPA TEGGATPVPR TLRKKLGTLF AFKKPRSTRG PRPDLETSPG AAARARKSTL
     GDLLRPPARP GRGEEPGGAE GGTSSPDPAR RNRPRYTRES KAYSMILLPA EEEAAVGTRP
     DKRRPLERGD TELAPSFEQR VQVMLQRIGV SRASGGAESK RKQSKDGEIK KAGSDGDIMD
     SSTETPPISI KSRTHSVSAD PSCRPGPGGQ GPESATWKTL GQQLNAELRG RGWGQQDGPG
     PPSPCPSPSP RRTSPAPDIL SLPEDPCLGP RNEERPLRLQ RSPVLKRRPK LEAPPSPSLG
     SGLGSKPLPP YPTEPSSPER SPPSPATDQR GGGPNP
//
ID   Q3V4D5_MOUSE            Unreviewed;       225 AA.
AC   Q3V4D5;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   30-NOV-2010, entry version 43.
DE   SubName: Full=N-acetyltransferase ARD1 homolog;
DE   SubName: Full=N-acetyltransferase ARD1 homolog (S. cerevisiae), isoform CRA_b;
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Naa10; Synonyms=Ard1, Ard1a;
GN   ORFNames=RP23-252M19.3-002, mCG_8092;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RA   Adachi J., Aizawa K., Akahira S., Akimura T., Arai A., Aono H.,
RA   Arakawa T., Bono H., Carninci P., Fukuda S., Fukunishi Y., Furuno M.,
RA   Hanagaki T., Hara A., Hayatsu N., Hiramoto K., Hiraoka T., Hori F.,
RA   Imotani K., Ishii Y., Itoh M., Izawa M., Kasukawa T., Kato H.,
RA   Kawai J., Kojima Y., Konno H., Kouda M., Koya S., Kurihara C.,
RA   Matsuyama T., Miyazaki A., Nishi K., Nomura K., Numazaki R., Ohno M.,
RA   Okazaki Y., Okido T., Owa C., Saito H., Saito R., Sakai C., Sakai K.,
RA   Sano H., Sasaki D., Shibata K., Shibata Y., Shinagawa A., Shiraki T.,
RA   Sogabe Y., Suzuki H., Tagami M., Tagawa A., Takahashi F., Tanaka T.,
RA   Tejima Y., Toya T., Yamamura T., Yasunishi A., Yoshida K., Yoshino M.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE.
RA   Johnson C.;
RL   Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK003806; BAE43151.1; -; mRNA.
DR   EMBL; AL672002; CAM18721.1; -; Genomic_DNA.
DR   EMBL; CH466650; EDL29856.1; -; Genomic_DNA.
DR   IPI; IPI00758413; -.
DR   RefSeq; NP_001171436.1; NM_001177965.1.
DR   UniGene; Mm.246654; -.
DR   ProteinModelPortal; Q3V4D5; -.
DR   SMR; Q3V4D5; 1-151.
DR   STRING; Q3V4D5; -.
DR   PRIDE; Q3V4D5; -.
DR   Ensembl; ENSMUST00000114389; ENSMUSP00000110031; ENSMUSG00000031388.
DR   GeneID; 56292; -.
DR   KEGG; mmu:56292; -.
DR   UCSC; uc009tnh.1; mouse.
DR   CTD; 56292; -.
DR   MGI; MGI:1915255; Naa10.
DR   HOVERGEN; HBG050561; -.
DR   PhylomeDB; Q3V4D5; -.
DR   ArrayExpress; Q3V4D5; -.
DR   Bgee; Q3V4D5; -.
DR   Genevestigator; Q3V4D5; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR000182; AcTrfase_GCN5-related_dom.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   Gene3D; G3DSA:3.40.630.30; Acyl_CoA_acyltransferase; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; Acyl_CoA_acyltransferase; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   2: Evidence at transcript level;
KW   Transferase.
SQ   SEQUENCE   225 AA;  24821 MW;  614220DFB5427C00 CRC64;
     MNIRNARPED LMNMQHCNLL CLPENYQMKY YFYHGLSWPQ LSYIAEDENG KIVGYVLAKM
     EEDPDDVPHG HITSLAVKRS HRRLGLAQKL MDQASRAMIE NFNAKYVSLH VRKSNRAALH
     LYSNTLNFQI SEVEPKYYAD GEDAYAMKRD LTQMADEPAS GPGSSCLLSG DLGPVSFHPL
     PSGLLAAAEA APGAEGKGQA HGSGGLGEQS GEQRQRASEL RRGLS
//
ID   Q3ZAQ4_MOUSE            Unreviewed;       839 AA.
AC   Q3ZAQ4;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   08-MAR-2011, entry version 46.
DE   SubName: Full=Autophagy 9-like 1 protein;
DE   SubName: Full=Autophagy protein 9;
GN   Name=Atg9a; Synonyms=Apg9l1, Atg9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Carson A.R., Yamada T., Nakabayashi K., Scherer S.W.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BalbC;
RA   Botti J., Djavaheri-Mergny M., Codogno P., Oriol R.;
RT   "Phylogeny and biochemistry of the autophagy protein beclin 1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AM085510; CAJ30208.1; -; mRNA.
DR   EMBL; BK004020; DAA05201.1; -; mRNA.
DR   IPI; IPI00750217; -.
DR   RefSeq; NP_001003917.2; NM_001003917.3.
DR   UniGene; Mm.479951; -.
DR   STRING; Q3ZAQ4; -.
DR   PhosphoSite; Q3ZAQ4; -.
DR   PRIDE; Q3ZAQ4; -.
DR   Ensembl; ENSMUST00000040689; ENSMUSP00000047449; ENSMUSG00000033124.
DR   GeneID; 245860; -.
DR   KEGG; mmu:245860; -.
DR   UCSC; uc007bnz.1; mouse.
DR   CTD; 245860; -.
DR   MGI; MGI:2138446; Atg9a.
DR   HOGENOM; HBG315812; -.
DR   HOVERGEN; HBG050539; -.
DR   InParanoid; Q3ZAQ4; -.
DR   OMA; FELMQFL; -.
DR   NextBio; 386964; -.
DR   ArrayExpress; Q3ZAQ4; -.
DR   Bgee; Q3ZAQ4; -.
DR   Genevestigator; Q3ZAQ4; -.
DR   GO; GO:0005776; C:autophagic vacuole; IDA:MGI.
DR   InterPro; IPR007241; Autophagy-rel_prot_9.
DR   PANTHER; PTHR13038; APG9; 1.
DR   Pfam; PF04109; APG9; 1.
PE   1: Evidence at protein level;
SQ   SEQUENCE   839 AA;  94425 MW;  1294E3B9231F1973 CRC64;
     MAQFDTEYQR LEASYSDSPP GEEDLLVHVA EGSKSPWHHI ENLDLFFSRV YNLHQKNGFT
     CMLIGEMFEL MQFLFVVAFT TFLVSCVDYD ILFANKMVNH SLHPTEPVKV TLPDAFLPAQ
     VCSARIQENG SLITILVIAG VFWIHRLIKF IYNICCYWEI HSFYLHALRI PMSALPYCTW
     QEVQARIVQT QKEHQICIHK RELTELDIYH RILRFQNYMV ALVNKSLLPL RFRLPGLGEV
     VFFTRGLKYN FELILFWGPG SLFLNEWSLK AEYKRGGQRL ELAQRLSNRI LWIGIANFLL
     CPLILIWQIL YAFFSYAEVL KREPGALGAR CWSLYGRCYL RHFNELEHEL QSRLNRGYKP
     ASKYMNCFLS PLLTLLAKNG AFFAGSILAV LIALTIYDED VLAVEHVLTT VTLLGVTVTV
     CRSFIPDQHM VFCPEQLLRV ILAHIHYMPD HWQGNAHRSQ TRDEFAQLFQ YKAVFILEEL
     LSPIVTPLIL IFCLRPRALE IIDFFRNFTV EVVGVGDTCS FAQMDVRQHG HPQWLSGGQT
     EASVYQQAED GKTELSLMHF AITNPGWQPP RESTAFLGFL KEQVQRDGAA AGLAQGGLLP
     ENALFTSIQS LQSESEPLSL IANVVAGSSC RGPSLSRDLQ GSRHRADVAS ALRSFSPLQP
     GAAPQGRVPS TMTGSGVDAR TASSGSSVWE GQLQSLVLSE YASTEMSLHA LYMHQLHKQQ
     TQAEPERHVW HRRESDESGE SAPEEGGEGA RAPQPIPRSA SYPCATPRPG APETTALHGG
     FQRRYGGITD PGTVPRGPSH FSRLPLGGWA EDGQPASRHP EPVPEEGSED ELPPQVHKV
//
ID   VEZA_MOUSE              Reviewed;         780 AA.
AC   Q3ZK22; A0M8X3; Q3ZK21; Q8BY12; Q8BYB4; Q8BZB5;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   08-FEB-2011, entry version 40.
DE   RecName: Full=Vezatin;
GN   Name=Vezt;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), DEVELOPMENTAL STAGE,
RP   SUBCELLULAR LOCATION, AND FUNCTION.
RC   STRAIN=129S2/SvPas;
RX   PubMed=16199027; DOI=10.1016/j.ydbio.2005.09.004;
RA   Hyenne V., Louvet-Vallee S., El-Amraoui A., Petit C., Maro B.,
RA   Simmler M.-C.;
RT   "Vezatin, an ubiquitous adherens junction protein, is required for
RT   mouse blastocyst morphogenesis.";
RL   Dev. Biol. 287:180-191(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), DISRUPTION PHENOTYPE, AND
RP   FUNCTION.
RC   STRAIN=129S2/SvPas;
RX   PubMed=17452094; DOI=10.1016/j.mod.2007.03.004;
RA   Hyenne V., Souilhol C., Cohen-Tannoudji M., Cereghini S., Petit C.,
RA   Langa F., Maro B., Simmler M.-C.;
RT   "Conditional knock-out reveals that zygotic vezatin-null mouse embryos
RT   die at implantation.";
RL   Mech. Dev. 124:449-462(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=17379651; DOI=10.1530/REP-06-0271;
RA   Hyenne V., Harf J.C., Latz M., Maro B., Wolfrum U., Simmler M.-C.;
RT   "Vezatin, a ubiquitous protein of adherens cell-cell junctions, is
RT   exclusively expressed in germ cells in mouse testis.";
RL   Reproduction 133:563-574(2007).
CC   -!- FUNCTION: Plays a pivotal role in the establishment of adherens
CC       junctions and their maintenance in adult life. Required for
CC       morphogenesis of the preimplantation embryo, and for the
CC       implantation process.
CC   -!- SUBUNIT: Interacts with myosin VIIa and the cadherin-catenins
CC       complex (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Cell junction, adherens junction. Nucleus. Cytoplasmic vesicle,
CC       secretory vesicle, acrosome.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=2.4;
CC         IsoId=Q3ZK22-1; Sequence=Displayed;
CC       Name=2; Synonyms=0.8;
CC         IsoId=Q3ZK22-2; Sequence=VSP_035268, VSP_035269, VSP_035270;
CC       Name=3; Synonyms=1.9;
CC         IsoId=Q3ZK22-3; Sequence=VSP_035272, VSP_035273;
CC       Name=4;
CC         IsoId=Q3ZK22-4; Sequence=VSP_035271, VSP_035274;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Isoform 1, isoform 2 and isoform 3 are
CC       expressed in testis. In the seminiferous epithelium, present
CC       exclusively in the acrosome of spermatids (at protein level).
CC   -!- DEVELOPMENTAL STAGE: Present in oocytes and at every embryonic
CC       stage (at protein level).
CC   -!- DISRUPTION PHENOTYPE: Embryos die at the time of implantation
CC       because of a defect in intercellular adhesion.
CC   -!- SIMILARITY: Belongs to the vezatin family.
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DR   EMBL; AY753561; AAX12551.1; -; mRNA.
DR   EMBL; AY753562; AAX12552.1; -; mRNA.
DR   EMBL; DQ025533; AAY87458.1; -; mRNA.
DR   EMBL; AK036017; BAC29277.1; -; mRNA.
DR   EMBL; AK041354; BAC30915.1; -; mRNA.
DR   EMBL; AK042540; BAC31287.1; -; mRNA.
DR   EMBL; BC056428; AAH56428.1; -; mRNA.
DR   IPI; IPI00282470; -.
DR   IPI; IPI00885231; -.
DR   IPI; IPI00885458; -.
DR   IPI; IPI00885798; -.
DR   RefSeq; NP_766126.2; NM_172538.4.
DR   UniGene; Mm.256845; -.
DR   STRING; Q3ZK22; -.
DR   PhosphoSite; Q3ZK22; -.
DR   PRIDE; Q3ZK22; -.
DR   Ensembl; ENSMUST00000047711; ENSMUSP00000037955; ENSMUSG00000036099.
DR   GeneID; 215008; -.
DR   KEGG; mmu:215008; -.
DR   CTD; 215008; -.
DR   MGI; MGI:2143698; Vezt.
DR   eggNOG; roNOG10839; -.
DR   GeneTree; ENSGT00390000003290; -.
DR   HOVERGEN; HBG108656; -.
DR   OMA; RLWRTAK; -.
DR   ArrayExpress; Q3ZK22; -.
DR   Bgee; Q3ZK22; -.
DR   Genevestigator; Q3ZK22; -.
DR   GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0002142; C:stereocilia ankle link complex; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0016337; P:cell-cell adhesion; IMP:MGI.
DR   GO; GO:0043009; P:chordate embryonic development; IMP:MGI.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Coiled coil;
KW   Cytoplasmic vesicle; Developmental protein; Membrane; Nucleus;
KW   Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    780       Vezatin.
FT                                /FTId=PRO_0000349248.
FT   TRANSMEM    140    160       Helical; (Potential).
FT   TRANSMEM    162    182       Helical; (Potential).
FT   COILED      430    467       Potential.
FT   COMPBIAS     32     35       Poly-Ser.
FT   COMPBIAS    704    711       Poly-Ala.
FT   COMPBIAS    764    767       Poly-Glu.
FT   MOD_RES     667    667       Phosphoserine.
FT   VAR_SEQ     239    307       SAACSFNKAAQHPGQHLIGLRKAVYRTVRANFQAARLATLY
FT                                MLKNYPLNSESDNVTNYICVVPFKELGL -> LLR (in
FT                                isoform 2).
FT                                /FTId=VSP_035268.
FT   VAR_SEQ     311    342       EDQISEEEARNLTDGFSLPALKVLFQLWVAQS -> DEWLC
FT                                AQPVLRQVYQMLGLVSFLTFTHIMDLT (in isoform
FT                                2).
FT                                /FTId=VSP_035269.
FT   VAR_SEQ     343    780       Missing (in isoform 2).
FT                                /FTId=VSP_035270.
FT   VAR_SEQ     611    639       AVLTSLSPVDPVESVSNSEPPMNSDTEKV -> EWTFNWIH
FT                                HAGHGGTVIPARWLRQGGSGV (in isoform 4).
FT                                /FTId=VSP_035271.
FT   VAR_SEQ     611    617       AVLTSLS -> GVKAEWN (in isoform 3).
FT                                /FTId=VSP_035272.
FT   VAR_SEQ     618    780       Missing (in isoform 3).
FT                                /FTId=VSP_035273.
FT   VAR_SEQ     640    780       Missing (in isoform 4).
FT                                /FTId=VSP_035274.
FT   CONFLICT     57     57       R -> K (in Ref. 1; AAX12552/AAX12551 and
FT                                2; AAY87458).
FT   CONFLICT     74     74       S -> P (in Ref. 1; AAX12552/AAX12551 and
FT                                2; AAY87458).
FT   CONFLICT    177    177       F -> L (in Ref. 1; AAX12552/AAX12551 and
FT                                2; AAY87458).
FT   CONFLICT    358    358       S -> T (in Ref. 1; AAX12552).
FT   CONFLICT    390    390       D -> E (in Ref. 1; AAX12552/AAX12551).
SQ   SEQUENCE   780 AA;  87987 MW;  AB8D244A6EDBDCEE CRC64;
     MTPEFDEEVV FENSPLYQYL QDLGHTDFEI CSSSSPKPEK CLTTEGPQPP PTRVLQRQGI
     LLKLTETIKS WTFSSQHSKK DDLLHKLDTG FRLDSLHTIL QQEVLLQEDV ELLELLDASI
     LSAGQPQQES GHLPTLCSLA TPNTWDVSLL FAFISLLIMF PTCWIVSSWL VWGIILFLYL
     IIRVLKLWRT AKLQMTLKKY RVRLEDMAAN SRAFTNLVRK SLRLIQETEV ISRGFTLVSA
     ACSFNKAAQH PGQHLIGLRK AVYRTVRANF QAARLATLYM LKNYPLNSES DNVTNYICVV
     PFKELGLGLS EDQISEEEAR NLTDGFSLPA LKVLFQLWVA QSSEFFRRLA LLLSTANSPS
     GPLLTAALLP HHILCDVTQG LPHAHSACLD ELKRSYEFFR YFETQHQSVP QRLSKTPQKS
     RELSNVHTAV RSLQLHLKAL LNEVIILEDE LEKLVCTKET QELLSEAYPI LEQKLKLIEP
     HVQASNSCWE EAISQVDKLL RRNTDKKGKP GVACENPHCT AEPLVRPALH IEDRDPIPEE
     QELEAYVDDI DIESEFRKDD FYHLSQEDRE RQKREQEESR RVLQELKSVL GFKASEAERQ
     KWKQLLFSDH AVLTSLSPVD PVESVSNSEP PMNSDTEKVN SNATEEETSK PCAGDKEDSR
     TEYVCDSPTE GPSKDTSADT GLLLPGAEET MCHQHESEAK SPQAAAAGAT APPTPRDTLQ
     LSIKQRLARL QLPPEFTFSA GLAAEVAARS LSFTTMQEQT FGDEEEEQLV EGGENEVEEK
//
ID   Q45FE1_MOUSE            Unreviewed;       178 AA.
AC   Q45FE1;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAR-2011, entry version 29.
DE   SubName: Full=Regulator of G-protein signaling 7 isoform B;
DE   Flags: Fragment;
GN   Name=Rgs7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RA   Liu W., He W., Wensel T.G.;
RT   "Differential distribution and PKC-sensitivity of neuronal RGS7 splice
RT   variants.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 RGS domain.
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DR   EMBL; DQ139289; AAZ67137.1; -; mRNA.
DR   IPI; IPI00649532; -.
DR   UniGene; Mm.7956; -.
DR   STRING; Q45FE1; -.
DR   Ensembl; ENSMUST00000097459; ENSMUSP00000095068; ENSMUSG00000026527.
DR   UCSC; uc007dth.1; mouse.
DR   MGI; MGI:1346089; Rgs7.
DR   ArrayExpress; Q45FE1; -.
DR   Bgee; Q45FE1; -.
DR   Genevestigator; Q45FE1; -.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005096; F:GTPase activator activity; TAS:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; IDA:MGI.
DR   InterPro; IPR000342; Regulat_G_prot_signal.
DR   InterPro; IPR016137; Regulat_G_prot_signal_superfam.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48097; Regulat_G_prot_signal_superfam; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   178 AA;  20704 MW;  624A09F91E3122D6 CRC64;
     ASKEPSQQRV KRWGFGMDEA LKDPVGREQF LKFLESEFSS ENLRFWLAVE DLKRRPIREV
     PSRVQEIWQE FLAPGAPSAI NLDSKSYDKT TQNVKEPGRY TFEDAQEHIY KLMKSDSYPR
     FIRSSAYQEL LQAKRKSGNS MDRRTSLEKF AQNVGRNLPI FPCHKNCTPT LRASTNLL
//
ID   Q497G1_MOUSE            Unreviewed;       384 AA.
AC   Q497G1;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 2.
DT   05-OCT-2010, entry version 31.
DE   SubName: Full=Solute carrier family 14 (Urea transporter), member 1;
GN   Name=Slc14a1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6NCr; TISSUE=Hematopoietic Stem Cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC100570; AAI00571.2; -; mRNA.
DR   IPI; IPI00652728; -.
DR   UniGene; Mm.33832; -.
DR   STRING; Q497G1; -.
DR   Ensembl; ENSMUST00000025433; ENSMUSP00000025433; ENSMUSG00000059336.
DR   Ensembl; ENSMUST00000091813; ENSMUSP00000089421; ENSMUSG00000059336.
DR   Ensembl; ENSMUST00000160292; ENSMUSP00000125114; ENSMUSG00000059336.
DR   Ensembl; ENSMUST00000160639; ENSMUSP00000125367; ENSMUSG00000059336.
DR   MGI; MGI:1351654; Slc14a1.
DR   HOVERGEN; HBG000540; -.
DR   InParanoid; Q497G1; -.
DR   ArrayExpress; Q497G1; -.
DR   Bgee; Q497G1; -.
DR   Genevestigator; Q497G1; -.
DR   GO; GO:0016021; C:integral to membrane; TAS:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0015204; F:urea transmembrane transporter activity; IMP:MGI.
DR   GO; GO:0005372; F:water transmembrane transporter activity; IDA:MGI.
DR   InterPro; IPR004937; Urea_transporter.
DR   PANTHER; PTHR10464; Urea_transporter; 1.
DR   Pfam; PF03253; UT; 1.
DR   PIRSF; PIRSF016502; Urea_transporter; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   384 AA;  42098 MW;  06D69FA66B35CBB8 CRC64;
     MEDSPTMVKV DRGENQILSC RGRRCGFKVL GYVTGDMKEF ANWLKDKPVA LQFMDWILRG
     ISQVVFVSNP ISGILILVGL LVQNPWWALC GCVGTVVSTL TALLLSQDRS AIAAGLQGYN
     ATLVGILMAV FSNKGDYFWW LIFPVSAMSM TCPVFSSALS SVLSKWDLPV FTLPFNMALS
     MYLSATGHYN TFFPSKLFTP VSSVPNITWS ELSALELLKS LPVGVGQIYG CDNPWTGGIF
     LCAILLSSPL MCLHAAIGSL LGVIAGLSLA APFEDIYFGL WGFNSSLACI AIGGMFMALT
     WQTHLLALAC ALFTAYFGAC MAHLMAVVHL PACTWSFCLA TLLFLLLTTK NPNIYRMPLS
     KVTYSEENRI FYLQNKKRMV ESPL
//
ID   FOXN3_MOUSE             Reviewed;         457 AA.
AC   Q499D0; Q8C5N8; Q9CU83;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Forkhead box protein N3;
DE   AltName: Full=Checkpoint suppressor 1;
GN   Name=Foxn3; Synonyms=Ches1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129/Sv X 129SvCp; TISSUE=Embryonic stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 46-457.
RC   STRAIN=C57BL/6J; TISSUE=Embryonic testis, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Acts as a transcriptional repressor. May be involved in
CC       DNA damage-inducible cell cycle arrests (checkpoints) (By
CC       similarity).
CC   -!- SUBUNIT: Interacts through its C-terminus with the C-terminus of
CC       SNW1/SKIP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- SIMILARITY: Contains 1 fork-head DNA-binding domain.
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DR   EMBL; BC099971; AAH99971.1; -; mRNA.
DR   EMBL; AK017346; BAB30701.1; -; mRNA.
DR   EMBL; AK077921; BAC37064.1; -; mRNA.
DR   IPI; IPI00136780; -.
DR   RefSeq; NP_899009.2; NM_183186.2.
DR   UniGene; Mm.341972; -.
DR   UniGene; Mm.480620; -.
DR   ProteinModelPortal; Q499D0; -.
DR   SMR; Q499D0; 119-193.
DR   PhosphoSite; Q499D0; -.
DR   PRIDE; Q499D0; -.
DR   Ensembl; ENSMUST00000046859; ENSMUSP00000036035; ENSMUSG00000033713.
DR   Ensembl; ENSMUST00000085108; ENSMUSP00000082189; ENSMUSG00000033713.
DR   GeneID; 71375; -.
DR   KEGG; mmu:71375; -.
DR   UCSC; uc007ors.1; mouse.
DR   CTD; 71375; -.
DR   MGI; MGI:1918625; Foxn3.
DR   eggNOG; roNOG05210; -.
DR   GeneTree; ENSGT00600000084145; -.
DR   HOGENOM; HBG447372; -.
DR   HOVERGEN; HBG051654; -.
DR   InParanoid; Q499D0; -.
DR   OMA; CYRGSSF; -.
DR   OrthoDB; EOG4N30NV; -.
DR   PhylomeDB; Q499D0; -.
DR   NextBio; 333663; -.
DR   ArrayExpress; Q499D0; -.
DR   Bgee; Q499D0; -.
DR   CleanEx; MM_FOXN3; -.
DR   Genevestigator; Q499D0; -.
DR   GermOnline; ENSMUSG00000033713; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR001766; TF_fork_head.
DR   InterPro; IPR018122; TF_fork_head_CS.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF00250; Fork_head; 1.
DR   PRINTS; PR00053; FORKHEAD.
DR   SMART; SM00339; FH; 1.
DR   PROSITE; PS00657; FORK_HEAD_1; 1.
DR   PROSITE; PS00658; FORK_HEAD_2; 1.
DR   PROSITE; PS50039; FORK_HEAD_3; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; DNA-binding; Nucleus; Phosphoprotein; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    457       Forkhead box protein N3.
FT                                /FTId=PRO_0000245102.
FT   DNA_BIND    114    210       Fork-head.
FT   COMPBIAS    308    358       Ser-rich.
FT   MOD_RES      85     85       Phosphoserine.
SQ   SEQUENCE   457 AA;  50345 MW;  52B473A3954C42B0 CRC64;
     MGPVMPASKK AESSGISVSS GLSQRYRGSG FSKALQEDDD LDFPLPDIRL EEGAMEDEEL
     TNLNWLHESK NLLKSFGESV LRSVSPVQDL DDDTPPSPAH SDMPYDARQN PNCKPPYSFS
     CLIFMAIEDS PTKRLPVKDI YNWILEHFPY FANAPTGWKN SVRHNLSLNK CFKKVDKERS
     QSIGKGSLWC IDPEYRQNLI QALKKTPYHP PPTPQAYQST SGPPIWPGST FFKRNGALLQ
     VSPGVIQNGA RVLSRGLFPG VRPLPITPIG MTAAIRNSIT SCRMRTESEP PCGSPVVSGD
     PKEDHNYSSA KSSTARSTSP TSDSISSSSS SADDHYEFAT KGSQEGSEGS FQSHESHSEP
     EEEDRKPSPK EGKDALGDSG YASQHKKRQH FAKARKVPSD TLPLKKRRTE KPPESDDEEM
     KEAAGSLLHL AGIRSCLNNI TNRTAKGQKE QKETAKN
//
ID   STOX2_MOUSE             Reviewed;         926 AA.
AC   Q499E5; B2RR59; Q3TRF0; Q497F9; Q6ZPS3; Q8CDI1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   08-MAR-2011, entry version 34.
DE   RecName: Full=Storkhead-box protein 2;
GN   Name=Stox2; Synonyms=Kiaa1392;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=CD-1; TISSUE=Brain, and Neural stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q499E5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q499E5-2; Sequence=VSP_030075, VSP_030076;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q499E5-3; Sequence=VSP_030074, VSP_030075, VSP_030076;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98156.1; Type=Erroneous initiation;
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DR   EMBL; AK129346; BAC98156.1; ALT_INIT; mRNA.
DR   EMBL; AK030015; BAC26735.1; -; mRNA.
DR   EMBL; AK162847; BAE37080.1; -; mRNA.
DR   EMBL; BC099949; AAH99949.1; -; mRNA.
DR   EMBL; BC100572; AAI00573.1; -; mRNA.
DR   EMBL; BC100573; AAI00574.1; -; mRNA.
DR   EMBL; BC138237; AAI38238.1; -; mRNA.
DR   EMBL; BC138238; AAI38239.1; -; mRNA.
DR   IPI; IPI00467354; -.
DR   IPI; IPI00875460; -.
DR   IPI; IPI00880803; -.
DR   RefSeq; NP_001107783.1; NM_001114311.1.
DR   RefSeq; NP_780371.3; NM_175162.4.
DR   UniGene; Mm.23973; -.
DR   ProteinModelPortal; Q499E5; -.
DR   PhosphoSite; Q499E5; -.
DR   PRIDE; Q499E5; -.
DR   Ensembl; ENSMUST00000079195; ENSMUSP00000078190; ENSMUSG00000038143.
DR   Ensembl; ENSMUST00000110367; ENSMUSP00000105996; ENSMUSG00000038143.
DR   GeneID; 71069; -.
DR   KEGG; mmu:71069; -.
DR   CTD; 71069; -.
DR   MGI; MGI:1918319; Stox2.
DR   eggNOG; roNOG04674; -.
DR   GeneTree; ENSGT00520000055589; -.
DR   HOGENOM; HBG506664; -.
DR   HOVERGEN; HBG061105; -.
DR   InParanoid; Q499E5; -.
DR   OrthoDB; EOG4S7JPB; -.
DR   NextBio; 332943; -.
DR   ArrayExpress; Q499E5; -.
DR   Bgee; Q499E5; -.
DR   CleanEx; MM_STOX2; -.
DR   Genevestigator; Q499E5; -.
DR   GO; GO:0009790; P:embryo development; ISS:UniProtKB.
DR   GO; GO:0001893; P:maternal placenta development; ISS:UniProtKB.
DR   InterPro; IPR019391; Storkhead-box_winged-helix.
DR   Pfam; PF10264; Stork_head; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing.
FT   CHAIN         1    926       Storkhead-box protein 2.
FT                                /FTId=PRO_0000313631.
FT   VAR_SEQ       1     62       Missing (in isoform 3).
FT                                /FTId=VSP_030074.
FT   VAR_SEQ     863    863       T -> N (in isoform 2 and isoform 3).
FT                                /FTId=VSP_030075.
FT   VAR_SEQ     864    926       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_030076.
FT   CONFLICT    122    122       T -> A (in Ref. 3; AAH99949).
FT   CONFLICT    167    167       R -> G (in Ref. 3; AAI00573/AAI00574).
FT   CONFLICT    235    235       P -> T (in Ref. 2; BAC26735).
FT   CONFLICT    526    526       S -> L (in Ref. 3; AAH99949).
FT   CONFLICT    671    671       V -> A (in Ref. 3; AAI00573/AAI00574).
SQ   SEQUENCE   926 AA;  102757 MW;  7560AC720C798D96 CRC64;
     MKKTRSTTLR RAWPSSDFSD RASDRMRSRS EKDYRLHKRF PAAFAPQASR GYMTSGDVSP
     ISMSPISQSQ FIPLGEILCL AISAMNSARK PVTQEALMEH LTTCFPGVPT PSQEILRHTL
     NTLVRERKIY PTPDGYFIVT PQTYFITPSL IRTNSKWYHL DERVPDRSQC TSPQPGTITP
     SASGCVRERT LPRKHCDSCH CCREDVHSMH ASTLQRKSAK DCKDPYCPPP LCQVPPTEKS
     KSTINFSYKT ETLSKPKDGE KQSKKFGLKL FRLSFKKDKT KQLANFSAQF PPEEWPLRDE
     DTPTTIPREV EMEIIRRINP DLTVENVMRH TALMKKLEEE KAHRSKAGSS AHHSGRSKKS
     RTHRKSHGKS RSHSKTRVSK GDPSDGSHLD IPGEREYEFC DPLTRAPREG CFIIEHKGDN
     FIMHSNTNVI ESHFPMTPEW DVSGELAKRR TEMPFPEPSR GSSHSKVHRS HSHTQDRRSR
     NERSNKAKER SRSMDNSKGP LGASSLGTPE DLAEGCSQDD QTPSQSYIDD STLRPAQTIG
     HQRAHIPSAS YKEVCIPEIV GGSKEPSSAC SLLEPGKTPE SMPSYGELSP CPAKTAVDDY
     FQCNTSSETV LTAPSPLGKN KEDHDTLTLV EGVKKLSPSE RQTPHSSREP VGHKEESPKG
     PGGGPAASGG VAEGLANGRL VQHHSAEPSS LDKRKEIFSK DTLFKPLHST LSVNSYHKSS
     LSLLKSHPKS PVDTLPGRCE KLEPSLGTSA AQAMPPSQRQ QEPGGNQEAS FDYYNVSDDD
     DSEEGANKNA EEEKNRDDVG TMQWLLEREK ERDLQRKFEK NLTLLTPKET DSSSNQRATH
     SARLDSMDSS SITVDSGFNS PRTRESLASN TSSIVESNRR QNPALSPAHG GAGPTFNFRA
     STDPPTSEAE KLQKPSNCLQ ASVTSV
//
ID   Q499W6_MOUSE            Unreviewed;       591 AA.
AC   Q499W6;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAR-2011, entry version 29.
DE   SubName: Full=Grip2 protein;
DE   Flags: Fragment;
GN   Name=Grip2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 3 PDZ (DHR) domains.
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DR   EMBL; BC099701; AAH99701.1; -; mRNA.
DR   IPI; IPI00929852; -.
DR   UniGene; Mm.333264; -.
DR   STRING; Q499W6; -.
DR   PhosphoSite; Q499W6; -.
DR   Ensembl; ENSMUST00000162300; ENSMUSP00000124709; ENSMUSG00000030098.
DR   MGI; MGI:2681173; Grip2.
DR   eggNOG; roNOG05721; -.
DR   GeneTree; ENSGT00390000013494; -.
DR   HOGENOM; HBG506549; -.
DR   HOVERGEN; HBG051841; -.
DR   InParanoid; Q499W6; -.
DR   OrthoDB; EOG4J9MZ7; -.
DR   Bgee; Q499W6; -.
DR   Genevestigator; Q499W6; -.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF00595; PDZ; 3.
DR   SMART; SM00228; PDZ; 3.
DR   SUPFAM; SSF50156; PDZ; 3.
DR   PROSITE; PS50106; PDZ; 3.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   591 AA;  63704 MW;  601946BD29D08707 CRC64;
     EAVRIQRSEQ LHRWDPSAPS CHSPRPSHCR APTWAAGGPD QSRSVSSTPF SSPTMNPAFP
     CANASTLPRG PMSPRTTAGR RRQRRKEHRS SLSLASSTVG PGGQIVHTET TEVVLCGDPL
     SGFGLQLQGG IFATETLSSP PLVRFIEPDS PAERCGLLQV GDRVLAINGI ATEDGTMEEA
     NQLLRDAALA RKVVLEIEFD VAESVIPSSG TFHVKLPKRR GVELGITISS ASRKRGEPLI
     ISDIKKGSVA HRTGTLEPGD KLLAIDNIRL DHCPMEDAVQ ILRQCEDLVK LKIRKDEDNS
     DEQESSGAVS YTVELKRYGG PLGITISGTE EPFDPIIISG LTKRGLAERT GAIHVGDRIL
     AINSVSLKGR PLSEAIHLLQ VAGETVTLKI KKQLDRPLLP RQSGSLSEAS DVDEDPPEAL
     KGGLLATRFS PAVPSVDSAV ESWGSSATDG GFGGTGSYTP QVAVRSVTPQ EWRPSRLKSS
     PPPLEPRRTS YTPGPSDESF PEEEGDWEPP MSPAPGPARE EGFWRVLGEA LEDLESCGQS
     ELLRELEASI MTGTVHSVAV DGRPGSRPWR RSREVRTSPE DLQELLLPTP L
//
ID   SHAN3_MOUSE             Reviewed;        1805 AA.
AC   Q4ACU6; Q69ZD8;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 2.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=SH3 and multiple ankyrin repeat domains protein 3;
DE            Short=Shank3;
DE   AltName: Full=Proline-rich synapse-associated protein 2;
DE            Short=ProSAP2;
DE   AltName: Full=SPANK-2;
GN   Name=Shank3; Synonyms=Kiaa1650;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 76-1805, AND INTERACTION WITH GRIA1.
RX   PubMed=16606358; DOI=10.1111/j.1471-4159.2006.03831.x;
RA   Uchino S., Wada H., Honda S., Nakamura Y., Ondo Y., Uchiyama T.,
RA   Tsutsumi M., Suzuki E., Hirasawa T., Kohsaka S.;
RT   "Direct interaction of post-synaptic density-95/Dlg/ZO-1 domain-
RT   containing synaptic molecule Shank3 with GluR1 alpha-amino-3-hydroxy-
RT   5-methyl-4-isoxazole propionic acid receptor.";
RL   J. Neurochem. 97:1203-1214(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 950-1805.
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-197; TYR-630 AND
RP   TYR-639, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450; SER-856 AND
RP   SER-1709, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Seems to be an adapter protein in the postsynaptic
CC       density (PSD) of excitatory synapses that interconnects receptors
CC       of the postsynaptic membrane including NMDA-type and metabotropic
CC       glutamate receptors via complexes with GKAP/PSD-95 and Homer,
CC       respectively, and the actin-based cytoskeleton. May play a role in
CC       the structural and functional organization of the dendritic spine
CC       and synaptic junction (By similarity).
CC   -!- SUBUNIT: May homomultimerize via its SAM domain. Interacts with
CC       BAIAP2 (By similarity). Interacts with DLGAP1/GKAP, MGLUR1A and
CC       MGLUR5 C-termini via its PDZ domain. Interacts (via PDZ domain)
CC       with PROSAPIP1 (via C-terminus) (By similarity). Interacts with
CC       HOMER1, HOMER2, HOMER3 and CCTN/cortactin SH3 domain (By
CC       similarity). Is part of a complex with DLG4/PSD-95 and DLGAP1/GKAP
CC       (By similarity). Interacts with DBNL. Interacts with the GRIA1
CC       subunit of AMPA receptor through the SH3-PDZ domain.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell junction, synapse. Cell
CC       junction, synapse, postsynaptic cell membrane, postsynaptic
CC       density. Note=Postsynaptic density of neuronal cells. Extends into
CC       the region subjacent to the PSD.
CC   -!- SIMILARITY: Belongs to the SHANK family.
CC   -!- SIMILARITY: Contains 6 ANK repeats.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-76 is the initiator.
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DR   EMBL; AC122401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC137513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB231013; BAE16756.1; -; mRNA.
DR   EMBL; AK173228; BAD32506.1; -; mRNA.
DR   IPI; IPI00351827; -.
DR   RefSeq; NP_067398.2; NM_021423.3.
DR   UniGene; Mm.146855; -.
DR   HSSP; Q9JLU4; 2F3N.
DR   ProteinModelPortal; Q4ACU6; -.
DR   SMR; Q4ACU6; 194-415, 546-606, 638-740, 1739-1802.
DR   STRING; Q4ACU6; -.
DR   PhosphoSite; Q4ACU6; -.
DR   PRIDE; Q4ACU6; -.
DR   Ensembl; ENSMUST00000109309; ENSMUSP00000104932; ENSMUSG00000022623.
DR   GeneID; 58234; -.
DR   KEGG; mmu:58234; -.
DR   UCSC; uc007xha.1; mouse.
DR   CTD; 58234; -.
DR   MGI; MGI:1930016; Shank3.
DR   eggNOG; roNOG12929; -.
DR   GeneTree; ENSGT00510000046474; -.
DR   HOGENOM; HBG715321; -.
DR   HOVERGEN; HBG054027; -.
DR   InParanoid; Q4ACU6; -.
DR   OMA; GRFPRST; -.
DR   OrthoDB; EOG48PMJ9; -.
DR   NextBio; 314265; -.
DR   ArrayExpress; Q4ACU6; -.
DR   Bgee; Q4ACU6; -.
DR   CleanEx; MM_SHANK3; -.
DR   Genevestigator; Q4ACU6; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0001838; P:embryonic epithelial tube formation; IGI:MGI.
DR   GO; GO:0000165; P:MAPKKK cascade; IGI:MGI.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00248; ANK; 5.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Cell junction; Cell membrane; Coiled coil; Cytoplasm;
KW   Membrane; Phosphoprotein; Postsynaptic cell membrane; Repeat;
KW   SH3 domain; Synapse.
FT   CHAIN         1   1805       SH3 and multiple ankyrin repeat domains
FT                                protein 3.
FT                                /FTId=PRO_0000291257.
FT   REPEAT      223    253       ANK 1.
FT   REPEAT      257    286       ANK 2.
FT   REPEAT      290    320       ANK 3.
FT   REPEAT      324    353       ANK 4.
FT   REPEAT      357    386       ANK 5.
FT   REPEAT      390    420       ANK 6.
FT   DOMAIN      545    604       SH3.
FT   DOMAIN      645    739       PDZ.
FT   DOMAIN     1742   1805       SAM.
FT   COILED     1569   1589       Potential.
FT   MOTIF      1485   1491       SH3-binding (Potential).
FT   COMPBIAS      6     15       Poly-Ala.
FT   COMPBIAS    510    537       Pro-rich.
FT   COMPBIAS    752    755       Poly-Pro.
FT   COMPBIAS    888   1424       Pro-rich.
FT   MOD_RES     197    197       Phosphotyrosine.
FT   MOD_RES     450    450       Phosphoserine.
FT   MOD_RES     469    469       Phosphoserine.
FT   MOD_RES     630    630       Phosphotyrosine.
FT   MOD_RES     639    639       Phosphotyrosine.
FT   MOD_RES     856    856       Phosphoserine.
FT   MOD_RES    1234   1234       Phosphoserine (By similarity).
FT   MOD_RES    1238   1238       Phosphoserine (By similarity).
FT   MOD_RES    1309   1309       Phosphothreonine (By similarity).
FT   MOD_RES    1328   1328       Phosphoserine (By similarity).
FT   MOD_RES    1709   1709       Phosphoserine.
SQ   SEQUENCE   1805 AA;  192218 MW;  AC678B7C98FCCEC7 CRC64;
     MQLNRAAVAA AAAPAEPPEP LSPALAPAPA PPGPLPRSAV GGALAGGQGG PGRRAESPCA
     PLSAGNSPGP GASTGMDGPG ASAVVVRVGI PDLQQTKCLR LDPTAPVWAA KQRVLCALNH
     SLQDALNYGL FQPPSRGRAG KFLDEERLLQ DYPPNLDTPL PYLEFRYKRR VYAQNLIDDK
     QFAKLHTKAN LKKFMDYVQL HSTDKVARLL DKGLDPNFHD PDSGECPLSL AAQLDNATDL
     LKVLRNGGAH LDFRTRDGLT AVHCATRQRN AGALTTLLDL GASPDYKDSR GLTPLYHSAL
     GGGDALCCEL LLHDHAQLGT TDENGWQEIH QACRFGHVQH LEHLLFYGAN MGAQNASGNT
     ALHICALYNQ ESCARVLLFR GANKDVRNYN SQTAFQVAII AGNFELAEVI KTHKDSDVVP
     FRETPSYAKR RRLAGPSGLA SPRPLQRSAS DINLKGDQPA ASPGPTLRSL PHQLLLQRLQ
     EEKDRDRDGE LENDISGPSA GRGGHNKISP SGPGGSGPAP GPGPASPAPP APPPRGPKRK
     LYSAVPGRKF IAVKAHSPQG EGEIPLHRGE AVKVLSIGEG GFWEGTVKGR TGWFPADCVE
     EVQMRQYDTR HETREDRTKR LFRHYTVGSY DSLTSHSDYV IDDKVAILQK RDHEGFGFVL
     RGAKAETPIE EFTPTPAFPA LQYLESVDVE GVAWRAGLRT GDFLIEVNGV NVVKVGHKQV
     VGLIRQGGNR LVMKVVSVTR KPEEDGARRR APPPPKRAPS TTLTLRSKSM TAELEELASI
     RRRKGEKLDE ILAVAAEPTL RPDIADADSR AATVKQRPTS RRITPAEISS LFERQGLPGP
     EKLPGSLRKG IPRTKSVGED EKLASLLEGR FPRSTSMQDT VREGRGIPPP PQTAPPPPPA
     PYYFDSGPPP TFSPPPPPGR AYDTVRSSFK PGLEARLGAG AAGLYDPSTP LGPLPYPERQ
     KRARSMIILQ DSAPEVGDVP RPAPAATPPE RPKRRPRPSG PDSPYANLGA FSASLFAPSK
     PQRRKSPLVK QLQVEDAQER AALAVGSPGP VGGSFAREPS PTHRGPRPGS LDYSSGEGLG
     LTFGGPSPGP VKERRLEERR RSTVFLSVGA IEGSPPSADL PSLQPSRSID ERLLGTGATT
     GRDLLLPSPV SALKPLVGGP SLGPSGSTFI HPLTGKPLDP SSPLALALAA RERALASQTP
     SRSPTPVHSP DADRPGPLFV DVQTRDSERG PLASPAFSPR SPAWIPVPAR REAEKPPREE
     RKSPEDKKSM ILSVLDTSLQ RPAGLIVVHA TSNGQEPSRL GAEEERPGTP ELAPAPMQAA
     AVAEPMPSPR AQPPGSIPAD PGPGQGSSEE EPELVFAVNL PPAQLSSSDE ETREELARIG
     LVPPPEEFAN GILLTTPPPG PGPLPTTVPS PASGKPSSEL PPAPESAADS GVEEADTRSS
     SDPHLETTST ISTVSSMSTL SSESGELTDT HTSFADGHTF LLEKPPVPPK PKLKSPLGKG
     PVTFRDPLLK QSSDSELMAQ QHHAASTGLA SAAGPARPRY LFQRRSKLWG DPVESRGLPG
     PEDDKPTVIS ELSSRLQQLN KDTRSLGEEP VGGLGSLLDP AKKSPIAAAR LFSSLGELST
     ISAQRSPGGP GGGASYSVRP SGRYPVARRA PSPVKPASLE RVEGLGAGVG GAGRPFGLTP
     PTILKSSSLS IPHEPKEVRF VVRSVSARSR SPSPSPLPSP SPGSGPSAGP RRPFQQKPLQ
     LWSKFDVGDW LESIHLGEHR DRFEDHEIEG AHLPALTKED FVELGVTRVG HRMNIERALR
     QLDGS
//
ID   F1892_MOUSE             Reviewed;         290 AA.
AC   Q4FZH1;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   08-MAR-2011, entry version 38.
DE   RecName: Full=Protein FAM189A2;
GN   Name=Fam189a2; Synonyms=Gm967;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thyroid;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SIMILARITY: Belongs to the FAM189 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH99492.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; BC099492; AAH99492.1; ALT_INIT; mRNA.
DR   IPI; IPI00884545; -.
DR   RefSeq; NP_001107646.1; NM_001114174.1.
DR   UniGene; Mm.426078; -.
DR   PhosphoSite; Q4FZH1; -.
DR   PRIDE; Q4FZH1; -.
DR   Ensembl; ENSMUST00000096164; ENSMUSP00000093878; ENSMUSG00000071604.
DR   GeneID; 381217; -.
DR   KEGG; mmu:381217; -.
DR   CTD; 381217; -.
DR   MGI; MGI:2685813; Fam189a2.
DR   eggNOG; roNOG09304; -.
DR   GeneTree; ENSGT00530000063335; -.
DR   HOGENOM; HBG282656; -.
DR   InParanoid; Q4FZH1; -.
DR   OrthoDB; EOG46T31R; -.
DR   NextBio; 401735; -.
DR   ArrayExpress; Q4FZH1; -.
DR   Bgee; Q4FZH1; -.
DR   CleanEx; MM_GM967; -.
DR   Genevestigator; Q4FZH1; -.
DR   GermOnline; ENSMUSG00000071604; Mus musculus.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    290       Protein FAM189A2.
FT                                /FTId=PRO_0000089699.
FT   MOD_RES     280    280       Phosphoserine.
SQ   SEQUENCE   290 AA;  32209 MW;  89171B27C4449521 CRC64;
     MNRRMVGSDV IPLPHIYGAR IKGVEVFCPL DPPPPYEAVV SQTDQEQESS FQMPEGPETA
     ASPAEPVCMQ ITQGGALTNT TGEENTSGST PIPTLVQPPR SRRALPLLRT RSKSDPVLHH
     SEERATPVLS CEAATQTERR LDLATVTLRR GTRPRASRCR PRSLIDYRSY IDTKLLVARF
     LEQSSCSMTP DIHELVENIK SVLKSDEGHM EEAITSASFL EQIMAPSQPS TSQAQELSWR
     RQPGLLHLRS CGDLSTFSLT ARPRAERRPQ QRAEAERPHS LIGVIRETVL
//
ID   OXR1_MOUSE              Reviewed;         866 AA.
AC   Q4KMM3; Q5FWW1; Q99L06; Q99MK1; Q99MP4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 3.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=Oxidation resistance protein 1;
DE   AltName: Full=Protein C7;
GN   Name=Oxr1; Synonyms=C7, Gm1238;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION,
RP   AND TISSUE SPECIFICITY.
RX   MEDLINE=21134317; PubMed=11237729; DOI=10.1006/bbrc.2001.4345;
RA   Fischer H., Zhang X.U., O'Brien K.P., Kylsten P., Engvall E.;
RT   "C7, a novel nucleolar protein, is the mouse homologue of the
RT   Drosophila late puff product L82 and an isoform of human OXR1.";
RL   Biochem. Biophys. Res. Commun. 281:795-803(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC   STRAIN=CD-1; TISSUE=Mammary gland, and Neural stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-204, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: May be involved in protection from oxidative damage.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). Nucleus,
CC       nucleolus. Note=According to PubMed:11237729 it is nucleolar.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q4KMM3-1; Sequence=Displayed;
CC       Name=2; Synonyms=C7B;
CC         IsoId=Q4KMM3-2; Sequence=VSP_039015;
CC       Name=3; Synonyms=C7A;
CC         IsoId=Q4KMM3-3; Sequence=VSP_039015, VSP_039016;
CC       Name=4;
CC         IsoId=Q4KMM3-4; Sequence=VSP_039016;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and testis.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the OXR1 family.
CC   -!- SIMILARITY: Contains 1 GRAM domain.
CC   -!- SIMILARITY: Contains 1 LysM repeat.
CC   -!- SIMILARITY: Contains 1 TLD domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH03927.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=AAH98491.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAE34619.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF324899; AAK30368.1; -; mRNA.
DR   EMBL; AF333985; AAK29400.1; -; mRNA.
DR   EMBL; AK158703; BAE34619.1; ALT_INIT; mRNA.
DR   EMBL; BC003927; AAH03927.1; ALT_INIT; mRNA.
DR   EMBL; BC089183; AAH89183.1; -; mRNA.
DR   EMBL; BC098491; AAH98491.1; ALT_INIT; mRNA.
DR   IPI; IPI00117929; -.
DR   IPI; IPI00277552; -.
DR   IPI; IPI00956919; -.
DR   IPI; IPI00957111; -.
DR   RefSeq; NP_001123635.1; NM_001130163.1.
DR   RefSeq; NP_001123636.1; NM_001130164.1.
DR   RefSeq; NP_001123637.1; NM_001130165.1.
DR   RefSeq; NP_001123638.1; NM_001130166.1.
DR   RefSeq; NP_570955.1; NM_130885.2.
DR   UniGene; Mm.254267; -.
DR   ProteinModelPortal; Q4KMM3; -.
DR   SMR; Q4KMM3; 98-143.
DR   STRING; Q4KMM3; -.
DR   PRIDE; Q4KMM3; -.
DR   Ensembl; ENSMUST00000022918; ENSMUSP00000022918; ENSMUSG00000022307.
DR   Ensembl; ENSMUST00000090096; ENSMUSP00000087554; ENSMUSG00000022307.
DR   Ensembl; ENSMUST00000110297; ENSMUSP00000105926; ENSMUSG00000022307.
DR   GeneID; 170719; -.
DR   KEGG; mmu:170719; -.
DR   UCSC; uc007voz.1; mouse.
DR   UCSC; uc007vpa.1; mouse.
DR   CTD; 170719; -.
DR   MGI; MGI:2179326; Oxr1.
DR   GeneTree; ENSGT00410000025363; -.
DR   HOVERGEN; HBG065488; -.
DR   OMA; DTGNDSA; -.
DR   OrthoDB; EOG47D9FW; -.
DR   PhylomeDB; Q4KMM3; -.
DR   ArrayExpress; Q4KMM3; -.
DR   Bgee; Q4KMM3; -.
DR   CleanEx; MM_OXR1; -.
DR   Genevestigator; Q4KMM3; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005730; C:nucleolus; IDA:MGI.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   InterPro; IPR004182; GRAM.
DR   InterPro; IPR018392; Peptidoglycan-bd_lysin.
DR   InterPro; IPR002482; Peptidoglycan-bd_Lysin_sg.
DR   InterPro; IPR006571; TLDc.
DR   Pfam; PF02893; GRAM; 1.
DR   Pfam; PF01476; LysM; 1.
DR   SMART; SM00257; LysM; 1.
DR   SMART; SM00584; TLDc; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Mitochondrion; Nucleus; Phosphoprotein.
FT   CHAIN         1    866       Oxidation resistance protein 1.
FT                                /FTId=PRO_0000231646.
FT   REPEAT      100    142       LysM.
FT   DOMAIN      213    268       GRAM.
FT   DOMAIN      730    865       TLD.
FT   COMPBIAS    205    208       Poly-Glu.
FT   MOD_RES     201    201       Phosphoserine (By similarity).
FT   MOD_RES     202    202       Phosphoserine (By similarity).
FT   MOD_RES     204    204       Phosphoserine.
FT   MOD_RES     518    518       Phosphoserine (By similarity).
FT   VAR_SEQ       1     88       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_039015.
FT   VAR_SEQ     646    672       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_039016.
FT   CONFLICT    107    109       SLN -> PLY (in Ref. 1; AAK29400).
FT   CONFLICT    156    156       L -> H (in Ref. 1; AAK29400).
FT   CONFLICT    308    308       S -> A (in Ref. 3; AAH89183/AAH98491).
FT   CONFLICT    435    437       TEV -> PEI (in Ref. 3; AAH89183/
FT                                AAH98491).
FT   CONFLICT    451    451       S -> L (in Ref. 3; AAH89183/AAH98491).
FT   CONFLICT    814    814       D -> G (in Ref. 3; AAH98491).
SQ   SEQUENCE   866 AA;  95912 MW;  15FB6B37144B1668 CRC64;
     MSVSNLSWLK KKSQSVDITA PGFNPLGGAG KQAPQASKPP APKTPIIEEE QNNSANTQKH
     PSRKSELKRF YTIDTGQKKT LDKKDGRRMS FQKPKGTIEY TVESRDSLNS IALKFDTTPN
     ELVQLNKLFS RAVVTGQVLY VPDPEYVSSV ESSPSLSPVS PLSPTSSEAE FDKTTTPDVA
     HPKEAPPAST VSGIRPARVV SSTSEEEEAF TEKFLKINCK YITIGKGTVS GVLLVTPNNI
     MFDPHKTDPL VQENGCEEYG IMCPMEEVMS AAMYKEILDS KIKESLPIEL DQLSGRGSCH
     SKKATGVSAE DADPRARDQG NDSASTAPRS TEESLSEDAF TESELSPIRE ELLSSEPRQE
     KSSDASSESV QTVSQMEVQS LTATSEAANV PDRTSSNPGA LSHETGLSGL ETATKGGDKA
     TESLQEVSGP KEQSTEVKGQ DNQDSSHQES SLQQEAGEDS VSSGETVELK EKPAVLKDQQ
     GQELKRDSET EVEELRKLWK THSMQQAKQQ RDTIQQVSQR ESKHSSAAAD AHGEGSSLLK
     EKRRHRLHKF LCLRVGKPMR KTFVSQASAT MQQYAQRDKK HEYWFAVPQE RTDHLYAFFI
     QWSPEIYAED SGEYTREPGF IVVKKMDESE ANEAPAGEAA AREWEVVSVA EYHRRIDALN
     TEELRTLCRR LQITTREDIN SKQVAPAKAD LEPESFRPNL SDPSELLLPD QIEKLTKHLP
     PRTIGYPWTL VYGTGKHGTS LKTLYRTMTG LDTPVLMVIK DSDGQVFGAL ASEPFKVSDG
     FYGTGETFVF TFCPEFEVFK WTGDNMFFIK GDMDSLAFGG GGGEFALWLD GDLYHGRSHS
     CKTFGNHTLS KKEDFFIQDI EIWAFE
//
ID   Q4KMN6_MOUSE            Unreviewed;       570 AA.
AC   Q4KMN6;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   08-MAR-2011, entry version 36.
DE   SubName: Full=Pcdhgc3 protein;
GN   Name=Pcdhgc3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 6 cadherin domains.
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CC   -----------------------------------------------------------------------
DR   EMBL; BC098457; AAH98457.1; -; mRNA.
DR   IPI; IPI00626467; -.
DR   UniGene; Mm.247203; -.
DR   ProteinModelPortal; Q4KMN6; -.
DR   SMR; Q4KMN6; 31-303.
DR   STRING; Q4KMN6; -.
DR   PRIDE; Q4KMN6; -.
DR   HOVERGEN; HBG054878; -.
DR   Genevestigator; Q4KMN6; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR013164; Cadherin_N.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 2.
DR   Pfam; PF00028; Cadherin; 2.
DR   Pfam; PF08266; Cadherin_2; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 2.
DR   SUPFAM; SSF49313; Cadherin; 2.
DR   PROSITE; PS00232; CADHERIN_1; 2.
DR   PROSITE; PS50268; CADHERIN_2; 2.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell membrane; Membrane; Repeat;
KW   Transmembrane; Transmembrane helix.
SQ   SEQUENCE   570 AA;  61463 MW;  3423BBCCD82CDE5C CRC64;
     MVAEARSSGL VSPWRTVGVL LLLAALTEAS TIIHYEILEE RERGFPVGNV VTDLGLDLGS
     LSARRLRVVS GASRRFFEVK VQVSDINDNP PQSSQSSYDV YVEENNLPGV PILNLSVWDP
     DAPPNARLSF FLLEPGAETG LVSRYFTINR DNGVLTTLVP LDYEDQREFQ LTAHINDGGT
     PVLATNISVN VFVTDRNDNA PQVLYPRPGQ SSVEMLPRGT AAGHVVSRVV GWDADAGHNA
     WLSYSLLGAP NQSLFAVGLH TGQISTARPI QDTDSPRQIL TVLISDSGEP LLSTTATLTV
     SVTEESPEAR AEFPSGSAPR EQNKNLTFYL LLSLILVSVG FAVTVLGVII FKVYKWKRSR
     DLYRAPVSSL YRTPGPSLHA DAVRGGLMPP HLYHQVYLTT DSRRSDPLLK KPGAASPLAS
     RQNTLRSCDP VFYRQVLGAE SAPPGQQAPP NTDWRFSQAQ RPGTSGSQNG DETGTWPNNQ
     FDTEMLQAMI LASASEAADG SSTLGGGAGT MGLSARYGPQ FTLQHVPDYR QNVYIPGSNA
     TLTNAAGKRD GKAPAGGNGN KKKSGKKEKK
//
ID   UN13A_MOUSE             Reviewed;        1712 AA.
AC   Q4KUS2; Q3UHG2;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Protein unc-13 homolog A;
DE   AltName: Full=Munc13-1;
GN   Name=Unc13a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Wang X., Honsbein A., Kilimann M.W.;
RT   "Mouse Munc13-1 sequence.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-1712.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=10440375; DOI=10.1038/22768;
RA   Augustin I., Rosenmund C., Suedhof T.C., Brose N.;
RT   "Munc13-1 is essential for fusion competence of glutamatergic synaptic
RT   vesicles.";
RL   Nature 400:457-461(1999).
RN   [4]
RP   FUNCTION.
RX   PubMed=12070347; DOI=10.1073/pnas.122623799;
RA   Varoqueaux F., Sigler A., Rhee J.-S., Brose N., Enk C., Reim K.,
RA   Rosenmund C.;
RT   "Total arrest of spontaneous and evoked synaptic transmission but
RT   normal synaptogenesis in the absence of Munc13-mediated vesicle
RT   priming.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9037-9042(2002).
RN   [5]
RP   FUNCTION.
RX   PubMed=15988013; DOI=10.1128/MCB.25.14.5973-5984.2005;
RA   Varoqueaux F., Sons M.S., Plomp J.J., Brose N.;
RT   "Aberrant morphology and residual transmitter release at the Munc13-
RT   deficient mouse neuromuscular synapse.";
RL   Mol. Cell. Biol. 25:5973-5984(2005).
RN   [6]
RP   FUNCTION.
RX   PubMed=16697276; DOI=10.1016/j.cmet.2006.04.012;
RA   Kang L., He Z., Xu P., Fan J., Betz A., Brose N., Xu T.;
RT   "Munc13-1 is required for the sustained release of insulin from
RT   pancreatic beta cells.";
RL   Cell Metab. 3:463-468(2006).
RN   [7]
RP   FUNCTION.
RX   PubMed=16644700; DOI=10.2337/db05-1263;
RA   Kwan E.P., Xie L., Sheu L., Nolan C.J., Prentki M., Betz A., Brose N.,
RA   Gaisano H.Y.;
RT   "Munc13-1 deficiency reduces insulin secretion and causes abnormal
RT   glucose tolerance.";
RL   Diabetes 55:1421-1429(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [9]
RP   FUNCTION, AND MUTAGENESIS OF HIS-563.
RX   PubMed=17267576; DOI=10.1523/JNEUROSCI.4908-06.2007;
RA   Basu J., Betz A., Brose N., Rosenmund C.;
RT   "Munc13-1 C1 domain activation lowers the energy barrier for synaptic
RT   vesicle fusion.";
RL   J. Neurosci. 27:1200-1210(2007).
RN   [10]
RP   FUNCTION.
RX   PubMed=17639022; DOI=10.2337/db06-1207;
RA   Kwan E.P., Xie L., Sheu L., Ohtsuka T., Gaisano H.Y.;
RT   "Interaction between Munc13-1 and RIM is critical for glucagon-like
RT   peptide-1 mediated rescue of exocytotic defects in Munc13-1 deficient
RT   pancreatic beta-cells.";
RL   Diabetes 56:2579-2588(2007).
RN   [11]
RP   INTERACTION WITH FBXO45.
RX   PubMed=19996097; DOI=10.1074/jbc.M109.046284;
RA   Tada H., Okano H.J., Takagi H., Shibata S., Yao I., Matsumoto M.,
RA   Saiga T., Nakayama K.I., Kashima H., Takahashi T., Setou M., Okano H.;
RT   "Fbxo45, a novel ubiquitin ligase, regulates synaptic activity.";
RL   J. Biol. Chem. 285:3840-3849(2010).
CC   -!- FUNCTION: Plays a role in vesicle maturation during exocytosis as
CC       a target of the diacylglycerol second messenger pathway. Involved
CC       in neurotransmitter release by acting in synaptic vesicle priming
CC       prior to vesicle fusion and participates in the activity-dependent
CC       refilling of readily releasable vesicle pool (RRP). Essential for
CC       synaptic vesicle maturation in most excitatory/glutamatergic but
CC       not inhibitory/GABA-mediated synapses. Also involved in secretory
CC       granule priming in insulin secretion.
CC   -!- SUBUNIT: Interacts with the N-termini of STX1A and/or STX1B1 and
CC       DOC2A. Interacts with BSN. Interacts with RIMS1 which recruits
CC       UNC13A to the active zone. Forms homodimers via its first C2
CC       domain. Also interacts via this domain with the zinc finger domain
CC       of RIMS2. Part of a complex consisting of ERC2, RIMS1 and UNC13A.
CC       Also part of a complex consisting of UNC13A, RIMS2 and RAB3A (By
CC       similarity). Interacts with FBXO45 (via SRY domain); leading to
CC       the degradation of UNC13A by the proteasome.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane;
CC       Peripheral membrane protein (By similarity). Cell junction,
CC       synapse, presynaptic cell membrane; Peripheral membrane protein
CC       (By similarity). Note=Localized to the active zone of presynaptic
CC       density. Translocated to the plasma membrane in response to
CC       phorbol ester binding (By similarity).
CC   -!- DOMAIN: The C2 domains are not involved in calcium-dependent
CC       phospholipid binding (By similarity).
CC   -!- DOMAIN: The C-terminal region containing both MHD domains and the
CC       third C2 domain is required for synaptic vesicle priming activity
CC       (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice display normal synapse formation but
CC       abnormal synaptic vesicle maturation and die shortly after birth.
CC       Heterozygotes exhibit impaired insulin secretion and abnormal
CC       glucose tolerance.
CC   -!- SIMILARITY: Contains 3 C2 domains.
CC   -!- SIMILARITY: Contains 1 MHD1 (MUNC13 homology domain 1) domain.
CC   -!- SIMILARITY: Contains 1 MHD2 (MUNC13 homology domain 2) domain.
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
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DR   EMBL; AY753536; AAX09281.1; -; mRNA.
DR   EMBL; AK147408; BAE27895.1; -; mRNA.
DR   IPI; IPI00405121; -.
DR   RefSeq; NP_001025044.2; NM_001029873.2.
DR   UniGene; Mm.334606; -.
DR   HSSP; Q62768; 2CJT.
DR   ProteinModelPortal; Q4KUS2; -.
DR   SMR; Q4KUS2; 2-128, 563-612, 683-815, 1554-1651.
DR   PhosphoSite; Q4KUS2; -.
DR   PRIDE; Q4KUS2; -.
DR   Ensembl; ENSMUST00000030170; ENSMUSP00000030170; ENSMUSG00000034799.
DR   GeneID; 382018; -.
DR   KEGG; mmu:382018; -.
DR   UCSC; uc009meh.1; mouse.
DR   CTD; 382018; -.
DR   MGI; MGI:3051532; Unc13a.
DR   eggNOG; roNOG08136; -.
DR   GeneTree; ENSGT00580000081383; -.
DR   HOVERGEN; HBG057340; -.
DR   OrthoDB; EOG4GTKC1; -.
DR   Bgee; Q4KUS2; -.
DR   CleanEx; MM_UNC13A; -.
DR   Genevestigator; Q4KUS2; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019992; F:diacylglycerol binding; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0050435; P:beta-amyloid metabolic process; IMP:MGI.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0016188; P:synaptic vesicle maturation; IMP:MGI.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   InterPro; IPR010439; Ca-dep_secretion_activator.
DR   InterPro; IPR014770; Munc13_1.
DR   InterPro; IPR014772; Munc13_dom-2.
DR   InterPro; IPR019558; Munc13_subgr_dom-2.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00168; C2; 3.
DR   Pfam; PF06292; DUF1041; 1.
DR   Pfam; PF10540; Membr_traf_MHD; 1.
DR   PRINTS; PR00360; C2DOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00239; C2; 3.
DR   SUPFAM; SSF49562; C2_CaLB; 3.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS51258; MHD1; 1.
DR   PROSITE; PS51259; MHD2; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Coiled coil; Cytoplasm; Exocytosis;
KW   Membrane; Metal-binding; Phosphoprotein; Repeat; Synapse; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1712       Protein unc-13 homolog A.
FT                                /FTId=PRO_0000306285.
FT   DOMAIN        1     79       C2 1.
FT   DOMAIN      672    778       C2 2.
FT   DOMAIN     1102   1245       MHD1.
FT   DOMAIN     1354   1521       MHD2.
FT   DOMAIN     1541   1646       C2 3.
FT   ZN_FING     562    612       Phorbol-ester/DAG-type.
FT   COILED      321    360       Potential.
FT   COMPBIAS    321    448       Glu-rich.
FT   METAL       576    576       Zinc 1 (By similarity).
FT   METAL       579    579       Zinc 1 (By similarity).
FT   METAL       593    593       Zinc 2 (By similarity).
FT   METAL       596    596       Zinc 2 (By similarity).
FT   METAL       604    604       Zinc 1 (By similarity).
FT   METAL       612    612       Zinc 2 (By similarity).
FT   MOD_RES     244    244       Phosphoserine.
FT   MUTAGEN     563    563       H->V: Reduces number of fusion-competent
FT                                vesicles in neurons.
FT   CONFLICT    127    127       F -> I (in Ref. 2; BAE27895).
FT   CONFLICT    479    479       E -> D (in Ref. 2; BAE27895).
SQ   SEQUENCE   1712 AA;  193796 MW;  176DF3541BBBAAD6 CRC64;
     MSLLCVGVKK AKFDGAQEKF NTYVTLKVQN VKSTTIAVRG SQPSWEQDFM FEINRLDLGL
     TVEVWNKGLI WDTMVGTVWI PLRTIRQSNE EGPGEWLTLD SQAIMADSEI CGTKDPTFHR
     ILLDAHFELP LDIPEEEARY WAKKLEQLNA MRDQDEYSFQ DQQDKPLPVP SSQCCNWNYF
     GWGEQNDDPD SAVDDRDSDY RSETSNSIPP PYYTTSQPNA SVHQYSVRPP PLGSRESYSD
     SMHSYEEFSE PRALSPTGSS RYASSGELSQ GSSQLSEDFD PDEHSLQGSE LDDERDRDSY
     HSCHSSVSYH KDSPRWDQDD EDLEDLEDLE DEELPEEEEE LEEEGEEELE EEDLEEEEEV
     PDDLASYTQQ EDTTVAEPKE FKRISFPTAA PQKDDKVSAV PTEAPEVAKG IPKAATPEEK
     AAAERAQEAE PPKSEESFRS REEEEGQEGQ DAMSRAKANW LRAFNKVRMQ LQEARGEGEM
     SKSLWFKGGP GGGLIIIDSM PDIRKRKPIP LVSDLAMSLV QSRKAGITSA LASSTLNNEE
     LKNHVYKKTL QALIYPISCT TPHNFEVWTA TTPTYCYECE GLLWGIARQG MRCTECGVKC
     HEKCQDLLNA DCLQRAAEKS SKHGAEDRTQ NIIMVLKDRM KIRERNKPEI FELIQEIFAV
     TKSAHTQQMK AVKQSVLDGT SKWSAKISIT VVCAQGLQAK DKTGSSDPYV TVQVGKTKKR
     TKTIYGNLNP VWEENFHFEC HNSSDRIKVR VWDEDDDIKS RVKQRFKRES DDFLGQTIIE
     VRTLSGEMDV WYNLDKRTDK SAVSGAIRLH ISVEIKGEEK VAPYHVQYTC LHENLFHFVT
     DVQNNGVVKI PDAKGDDAWK VYYDETAQEI VDEFAMRYGV ESIYQAMTHF ACLSSKYMCP
     GVPAVMSTLL ANINAYYAHT TASTNVSASD RFAASNFGKE RFVKLLDQLH NSLRIDLSMY
     RNNFPASSPE RLQDLKSTVD LLTSITFFRM KVQELQSPPR ASQVVKDCVK ACLNSTYEYI
     FNNCHELYGR EYQTDPAKKG EVPPEEQGPS IKNLDFWSKL ITLIVSIIEE DKNSYTPCLN
     QFPQELNVGK ISAEVMWSLF AQDMKYAMEE HDKHRLCKSA DYMNLHFKVK WLYNEYVAEL
     PTFKDRVPEY PAWFEPFVIQ WLDENEEVSR DFLHGALERD KKDGFQQTSE HALFSCSVVD
     VFSQLNQSFE IIKKLECPDP QIVGHYMRRF AKTISNVLLQ YADIVSKDFA SYCSKEKEKV
     PCILMNNTQQ LRVQLEKMFE AMGGKELDAE ASGTLKELQV KLNNVLDELS HVFATSFQPH
     IEECVRQMGD ILSQVKGTGN VPASACSSVA QDADNVLQPI MDLLDSNLTL FAKICEKTVL
     KRVLKELWKL VMNTMEKTIV LPPLTDQTMI GTLLRKHGKG LEKGRVKLPS HSDGTQMIFN
     AAKELGQLSK LKDHMVREEA KSLTPKQCAV VELALDTIKQ YFHAGGVGLK KTFLEKSPDL
     QSLRYALSLY TQATDLLIKT FVQTQSAQGS GVEDPVGEVS VHVELFTHPG TGEQKVTVKV
     VAANDLKWQT SGIFRPFIEV NIVGPQLSDK KRKFATKSKN NSWAPKYNES FQFSLSADAG
     PECYELQVCV KDYCFAREDR TVGLAVLQLR ELAQRGSAAC WLPLGRRIHM DDTGLTVLRI
     LSQRSNDEVA KEFVKLKSDT RSAEEGGAAP AP
//
ID   ARAP1_MOUSE             Reviewed;        1452 AA.
AC   Q4LDD4; B2RUJ3; Q3UDD2; Q3US99; Q58ET6; Q6PEQ9; Q6ZQ48;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 2.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 1;
DE   AltName: Full=Centaurin-delta-2;
DE            Short=Cnt-d2;
GN   Name=Arap1; Synonyms=Centd2, Kiaa0782;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RA   Krugmann S., Coadwell J., Stephens L.R., Hawkins P.T.;
RT   "ARAP1 splice variants in man and mouse.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Bone, Bone marrow macrophage, and Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1320-1452 (ISOFORM 2/3).
RC   STRAIN=FVB/N; TISSUE=Brain, and Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 295-1452 (ISOFORM 2/3).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
CC   -!- FUNCTION: Phosphatidylinositol-3,4,5-trisphosphate-dependent
CC       GTPase-activating protein that modulates actin cytoskeleton
CC       remodeling by regulating ARF and RHO family members. Is activated
CC       by phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3)
CC       binding. Can be activated by phosphatidylinositol-3,4-bisphosphate
CC       (PtdIns(3,4,5)P2) binding, albeit with lower efficiency. Has a
CC       preference for ARF1 and ARF5 (By similarity).
CC   -!- SUBUNIT: Interacts with TNFRSF10A (By similarity).
CC   -!- INTERACTION:
CC       P25095:Agtr1 (xeno); NbExp=2; IntAct=EBI-764994, EBI-764979;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus,
CC       Golgi stack membrane; Peripheral membrane protein (By similarity).
CC       Cell membrane (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q4LDD4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q4LDD4-2; Sequence=VSP_053048;
CC       Name=3;
CC         IsoId=Q4LDD4-3; Sequence=VSP_053047, VSP_053048;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 Arf-GAP domain.
CC   -!- SIMILARITY: Contains 4 PH domains.
CC   -!- SIMILARITY: Contains 1 Ras-associating domain.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
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DR   EMBL; AJ621558; CAF21318.1; -; mRNA.
DR   EMBL; AK137455; BAE23358.1; -; mRNA.
DR   EMBL; AK140646; BAE24434.1; -; mRNA.
DR   EMBL; AK150132; BAE29329.1; -; mRNA.
DR   EMBL; BC057922; AAH57922.1; -; mRNA.
DR   EMBL; BC091762; AAH91762.1; -; mRNA.
DR   EMBL; BC141179; AAI41180.1; -; mRNA.
DR   EMBL; AK129213; BAC98023.1; -; mRNA.
DR   IPI; IPI00377288; -.
DR   IPI; IPI00407609; -.
DR   IPI; IPI00761865; -.
DR   RefSeq; NP_001035200.1; NM_001040111.1.
DR   RefSeq; NP_001035201.1; NM_001040112.1.
DR   RefSeq; NP_081456.2; NM_027180.3.
DR   RefSeq; NP_932764.1; NM_198096.1.
DR   UniGene; Mm.277687; -.
DR   HSSP; Q8WZ64; 2COD.
DR   ProteinModelPortal; Q4LDD4; -.
DR   SMR; Q4LDD4; 9-66, 324-434, 439-531, 537-854, 962-1141, 1172-1262.
DR   IntAct; Q4LDD4; 2.
DR   STRING; Q4LDD4; -.
DR   PhosphoSite; Q4LDD4; -.
DR   PRIDE; Q4LDD4; -.
DR   Ensembl; ENSMUST00000084896; ENSMUSP00000081958; ENSMUSG00000032812.
DR   Ensembl; ENSMUST00000107011; ENSMUSP00000102625; ENSMUSG00000032812.
DR   GeneID; 69710; -.
DR   KEGG; mmu:69710; -.
DR   UCSC; uc009iol.1; mouse.
DR   CTD; 69710; -.
DR   MGI; MGI:1916960; Arap1.
DR   eggNOG; roNOG06197; -.
DR   GeneTree; ENSGT00600000084201; -.
DR   HOVERGEN; HBG106625; -.
DR   InParanoid; Q4LDD4; -.
DR   OMA; LISHLYC; -.
DR   ArrayExpress; Q4LDD4; -.
DR   Bgee; Q4LDD4; -.
DR   Genevestigator; Q4LDD4; -.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0010843; F:promoter binding; ISS:UniProtKB.
DR   GO; GO:0070412; F:R-SMAD binding; ISS:BHF-UCL.
DR   GO; GO:0005100; F:Rho GTPase activator activity; ISS:UniProtKB.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0008134; F:transcription factor binding; ISS:BHF-UCL.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045941; P:positive regulation of transcription; ISS:UniProtKB.
DR   GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR   GO; GO:0007184; P:SMAD protein import into nucleus; ISS:UniProtKB.
DR   GO; GO:0060395; P:SMAD protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR   InterPro; IPR001164; ArfGAP.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000159; Ras-assoc.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 4.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF00169; PH; 3.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 5.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF57863; ArfGAP; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 4.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasm; Golgi apparatus;
KW   GTPase activation; Membrane; Metal-binding; Phosphoprotein; Repeat;
KW   Zinc; Zinc-finger.
FT   CHAIN         1   1452       Arf-GAP with Rho-GAP domain, ANK repeat
FT                                and PH domain-containing protein 1.
FT                                /FTId=PRO_0000367029.
FT   DOMAIN        6     70       SAM.
FT   DOMAIN      329    421       PH 1.
FT   DOMAIN      442    531       PH 2.
FT   DOMAIN      537    662       Arf-GAP.
FT   DOMAIN      745    852       PH 3.
FT   DOMAIN      956   1141       Rho-GAP.
FT   DOMAIN     1174   1263       Ras-associating.
FT   DOMAIN     1276   1398       PH 4.
FT   ZN_FING     552    575       C4-type.
FT   MOD_RES     232    232       Phosphoserine (By similarity).
FT   MOD_RES     234    234       Phosphotyrosine (By similarity).
FT   MOD_RES     344    344       Phosphoserine (By similarity).
FT   MOD_RES     345    345       Phosphotyrosine (By similarity).
FT   MOD_RES     430    430       Phosphoserine (By similarity).
FT   MOD_RES     739    739       Phosphotyrosine (By similarity).
FT   MOD_RES     740    740       Phosphoserine (By similarity).
FT   MOD_RES    1270   1270       Phosphotyrosine (By similarity).
FT   MOD_RES    1437   1437       Phosphoserine (By similarity).
FT   VAR_SEQ       1    248       Missing (in isoform 3).
FT                                /FTId=VSP_053047.
FT   VAR_SEQ    1322   1332       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_053048.
FT   CONFLICT    153    153       P -> S (in Ref. 3; AAI41180).
FT   CONFLICT    280    280       S -> A (in Ref. 3; AAI41180).
FT   CONFLICT    924    924       V -> G (in Ref. 1; CAF21318).
FT   CONFLICT   1331   1331       T -> R (in Ref. 3; AAH57922).
SQ   SEQUENCE   1452 AA;  162276 MW;  1606F3534555D4F6 CRC64;
     MAEGYDAALS VAEWLRALHL EQYTALFEQH GLVWATECQG LSDAGLLDMG MHLPGHRRRI
     LAGLHRAHAP PVPLPRPAPR PVPMKRHIFR SPPVPVTPPE PPPTAGEDEG LPAAPPIPPR
     RSCLPPACFT PTSTAAPDPV LPPLPAKRHL VEPSVPPVPP RTGPPYPQAS LLAKEELLLP
     SVSPRSQPEP AETPSTLLPA FPQGPLQPPS PPPCPPVIPP KPPRLLPEFD DSDYDDVPEE
     GPGAPASVMT KEEPLPSRVP RAVRVASLLS EGEELSGDDS EDDDDHAYEG IPNGGWPTSG
     LNPPLRSLIP DLPLHPMDEL PGGPTPITPV IKAGWLDKNP PQGSYIYQKR WVRLDADYLR
     YFDSNKDAYS KRFVPVACIC RVAPIGDQKF EVITNNRTFA FRAESDVERN EWMQALQQAV
     VEHRARFRLS SASVLGVRGS EQPDRAGSLE LRGFKNKLYV AVTGDKVQLY KNLEEFHLGI
     GITFIDMNVG NVKEVDRRSF DLTTPYRIFS FSADSELEKE QWLEAMQGAI AEALSTSEVA
     ERIWAAAPNR FCADCGAAQP DWASINLCVV ICKRCAGEHR GLGAGVSKVR SLKMDRKVWT
     EALIQLFLHL GNGPGNHFWA ANVPPSEALE PSSSPGARRY HLEAKYREGK YRRYHPLFGN
     QEELDKALCA AVTTTDLAET QALLGCGAGV SCFSGDPAAP TPLALAEQAG QTLQMEFLRN
     NQSTEVPRLD SVKPLEKHYS VTLPTVSHSG FLYKTASAGK PLQDRRAREE FSRRWCVLSD
     GVLSYYENER AVTPNGEIRA SEIVCLAVSP LDTHGFEHTF EVYTEGERLY LFGLENAELA
     HEWVKCIAKA FVPPLAEDLL ARDFERLGRL PCKAGLSLQQ AQEGWFALTG SELRAVFPEG
     PWEEPLQLRK LQELSIQGDS ENQVLVLVER RRTLYIQGER RLDFMAWLGV IQKAAASLGD
     TLSEQQLGDS DIPVIVYRCV DYITQCGLTS EGIYRKCGQT SKTQRLLDSL RQDARSVHLK
     EGEQHVDDVS SALKRFLRDL PDGLFTRAQR LAWLEASEIE DEEEKISRYR ELLVHLPPVN
     RATVKALISH LYCVQCFSDT NQMNTHNLAI VFGPTLFQTD GQDYKAGKVV EDLINHYVVV
     FSVDEEELRK QREEVTAIVK MRVAGTASGT QHAGDFICTV YLEEKKVETE QHVKIPASMT
     AEELTLEILD RRNVSIREKD YWTCFEVNEK EEAERPLHFA EKVLPIVHGL GIDSHLVVKK
     YQSMEAMLLY LASRVGDTKH GMMKFREDRS LLGLGLPSGG FHDRYFILNS SCLRLYKEVR
     SQRPWSGAPE TSHRPEKEWP VKSLKVYLGV KKKLRPPTCW GFTVVHETEK HEKQQWYLCC
     DTQMELREWF ATFLSVQHDG LVWPSEPSRV SRAVPEVRMG SVSLIPLRGS ENEMRRSVAA
     FTADPLSLLR HV
//
ID   Q4LG64_MOUSE            Unreviewed;       883 AA.
AC   Q4LG64;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   08-MAR-2011, entry version 49.
DE   SubName: Full=AMPA-selective glutamate receptor 2 flip type;
GN   Name=Gria2; Synonyms=glur-2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DdY; TISSUE=Spinal cord;
RA   Nishizawa M., Ito S.;
RT   "Expression of AMPA-selective glutamate receptors in mouse spinal
RT   cord.";
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AB111957; BAE06155.1; -; mRNA.
DR   IPI; IPI00845711; -.
DR   RefSeq; NP_001077275.1; NM_001083806.1.
DR   UniGene; Mm.220224; -.
DR   ProteinModelPortal; Q4LG64; -.
DR   SMR; Q4LG64; 412-527, 652-794.
DR   STRING; Q4LG64; -.
DR   PRIDE; Q4LG64; -.
DR   Ensembl; ENSMUST00000107745; ENSMUSP00000103374; ENSMUSG00000033981.
DR   GeneID; 14800; -.
DR   KEGG; mmu:14800; -.
DR   UCSC; uc008pob.1; mouse.
DR   CTD; 14800; -.
DR   MGI; MGI:95809; Gria2.
DR   HOVERGEN; HBG051839; -.
DR   NextBio; 286957; -.
DR   ArrayExpress; Q4LG64; -.
DR   Bgee; Q4LG64; -.
DR   Genevestigator; Q4LG64; -.
DR   GO; GO:0032281; C:alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex; IDA:MGI.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IDA:MGI.
DR   GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:MGI.
DR   GO; GO:0007268; P:synaptic transmission; IDA:MGI.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR019594; Glu_rcpt_Glu/Gly-bd.
DR   InterPro; IPR001320; Iontro_glu_rcpt.
DR   InterPro; IPR001508; NMDA_rcpt.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR   PRINTS; PR00177; NMDARECEPTOR.
DR   SMART; SM00918; Lig_chan-Glu_bd; 1.
DR   SMART; SM00079; PBPe; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Ion transport; Ionic channel;
KW   Ligand-gated ion channel; Membrane; Postsynaptic cell membrane;
KW   Receptor; Synapse; Transmembrane; Transmembrane helix; Transport.
SQ   SEQUENCE   883 AA;  98846 MW;  C019FACB4F1BA3AE CRC64;
     MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ FSTSEFRLTP
     HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI TSFCGTLHVS FITPSFPTDG
     THPFVIQMRP DLKGALLSLI EYYQWDKFAY LYDSDRGLST LQAVLDSAAE KKWQVTAINV
     GNINNDKKDE TYRSLFQDLE LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL
     GFTDGDLLKI QFGGANVSGF QIVDYDDSLV SKFIERWSTL EEKEYPGAHT ATIKYTSALT
     YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ VQVEGLSGNI
     KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT ELPSGNDTSG LENKTVVVTT
     ILESPYVMMK KNHEMLEGNE RYEGYCVDLA AEIAKHCGFK YKLTIVGDGK YGARDADTKI
     WNGMVGELVY GKADIAIAPL TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD
     PLAYEIWMCI VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF
     SLGAFMRQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM VSPIESAEDL
     SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP SVFVRTTAEG VARVRKSKGK
     YAYLLESTMN EYIEQRKPCD TMKVGGNLDS KGYGIATPKG SSLRTPVNLA VLKLSEQGVL
     DKLKNKWWYD KGECGAKDSG SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR
     AEAKRMKVAK NAQNINPSSS QNSQNFATYK EGYNVYGIES VKI
//
ID   P5I11_MOUSE             Reviewed;         189 AA.
AC   Q4QQM4; Q3UQL4;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=Tumor protein p53-inducible protein 11;
DE   AltName: Full=Transformation related protein 53 inducible protein 11;
DE   AltName: Full=p53-induced gene 11 protein;
GN   Name=Trp53i11; Synonyms=Pig11, Tp53i11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE25025.1; Type=Frameshift; Positions=126, 135;
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DR   EMBL; AK142316; BAE25025.1; ALT_FRAME; mRNA.
DR   EMBL; AL691472; CAM17745.1; -; Genomic_DNA.
DR   EMBL; CH466519; EDL27616.1; -; Genomic_DNA.
DR   EMBL; BC048398; AAH48398.1; -; mRNA.
DR   EMBL; BC098206; AAH98206.1; -; mRNA.
DR   IPI; IPI00342407; -.
DR   RefSeq; NP_001020417.1; NM_001025246.1.
DR   UniGene; Mm.41033; -.
DR   ProteinModelPortal; Q4QQM4; -.
DR   PhosphoSite; Q3UQL4; -.
DR   PRIDE; Q4QQM4; -.
DR   Ensembl; ENSMUST00000090554; ENSMUSP00000088042; ENSMUSG00000068735.
DR   Ensembl; ENSMUST00000111266; ENSMUSP00000106897; ENSMUSG00000068735.
DR   GeneID; 277414; -.
DR   KEGG; mmu:277414; -.
DR   UCSC; uc008lfq.1; mouse.
DR   CTD; 277414; -.
DR   MGI; MGI:2670995; Trp53i11.
DR   GeneTree; ENSGT00390000017249; -.
DR   HOGENOM; HBG713538; -.
DR   HOVERGEN; HBG054028; -.
DR   InParanoid; Q4QQM4; -.
DR   OMA; QVGRKPK; -.
DR   OrthoDB; EOG4PG61K; -.
DR   NextBio; 393766; -.
DR   ArrayExpress; Q4QQM4; -.
DR   Bgee; Q4QQM4; -.
DR   Genevestigator; Q4QQM4; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    189       Tumor protein p53-inducible protein 11.
FT                                /FTId=PRO_0000395041.
FT   TOPO_DOM      1     63       Cytoplasmic (Potential).
FT   TRANSMEM     64     84       Helical; (Potential).
FT   TOPO_DOM     85    108       Extracellular (Potential).
FT   TRANSMEM    109    129       Helical; (Potential).
FT   TOPO_DOM    130    130       Cytoplasmic (Potential).
FT   TRANSMEM    131    151       Helical; (Potential).
FT   TOPO_DOM    152    155       Extracellular (Potential).
FT   TRANSMEM    156    176       Helical; (Potential).
FT   TOPO_DOM    177    189       Cytoplasmic (Potential).
FT   COMPBIAS    177    180       Poly-Tyr.
FT   MOD_RES      14     14       Phosphoserine.
SQ   SEQUENCE   189 AA;  20911 MW;  67E7BBCD4FFCF090 CRC64;
     MAGKQPPPLM KKHSQTDLVS RLKTRKILGV GGEDDDGEVH RSKISQVLGN EIKFAVREPL
     GLRVWQFLSA MLFSSVAIMA LALPDQLYDA VFDGAEVTSK TPIRLYGGAL LSISLIMWNA
     LYTAEKVIIR WTLLTEACYF GVQSLVVTAT LAETGLMSLG TVLLLASRLL FVIVSIYYYY
     QVGRKPKKV
//
ID   FA73A_MOUSE             Reviewed;         600 AA.
AC   Q4QQM5; Q8BR91; Q8C3S6; Q8C8P4;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   08-MAR-2011, entry version 40.
DE   RecName: Full=Protein FAM73A;
GN   Name=Fam73a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, Lung, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q4QQM5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q4QQM5-2; Sequence=VSP_024881, VSP_024882;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q4QQM5-3; Sequence=VSP_024880;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the FAM73 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC32059.1; Type=Frameshift; Positions=26;
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DR   EMBL; AK044739; BAC32059.1; ALT_FRAME; mRNA.
DR   EMBL; AK045347; BAC32322.1; -; mRNA.
DR   EMBL; AK085017; BAC39340.1; -; mRNA.
DR   EMBL; BC098205; AAH98205.1; -; mRNA.
DR   IPI; IPI00225194; -.
DR   IPI; IPI00404369; -.
DR   IPI; IPI00845798; -.
DR   RefSeq; NP_001155847.1; NM_001162375.1.
DR   RefSeq; NP_777357.2; NM_174868.4.
DR   UniGene; Mm.135018; -.
DR   PRIDE; Q4QQM5; -.
DR   Ensembl; ENSMUST00000068243; ENSMUSP00000068261; ENSMUSG00000054942.
DR   Ensembl; ENSMUST00000073089; ENSMUSP00000072836; ENSMUSG00000054942.
DR   GeneID; 215708; -.
DR   KEGG; mmu:215708; -.
DR   UCSC; uc008rte.1; mouse.
DR   CTD; 215708; -.
DR   MGI; MGI:1924567; Fam73a.
DR   eggNOG; roNOG07665; -.
DR   GeneTree; ENSGT00390000008565; -.
DR   HOGENOM; HBG507162; -.
DR   HOVERGEN; HBG106606; -.
DR   InParanoid; Q4QQM5; -.
DR   OMA; KILPWEP; -.
DR   OrthoDB; EOG4WQ124; -.
DR   PhylomeDB; Q4QQM5; -.
DR   NextBio; 374815; -.
DR   ArrayExpress; Q4QQM5; -.
DR   Bgee; Q4QQM5; -.
DR   CleanEx; MM_C030011O14RIK; -.
DR   Genevestigator; Q4QQM5; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR019392; DUF2217.
DR   Pfam; PF10265; DUF2217; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    600       Protein FAM73A.
FT                                /FTId=PRO_0000285647.
FT   TRANSMEM     15     32       Helical; (Potential).
FT   TRANSMEM     38     58       Helical; (Potential).
FT   COMPBIAS    160    163       Poly-Asp.
FT   VAR_SEQ     302    365       Missing (in isoform 3).
FT                                /FTId=VSP_024880.
FT   VAR_SEQ     490    506       ISDGFFAHFYAICEHVS -> VKLTMPQTPPQFILCGF
FT                                (in isoform 2).
FT                                /FTId=VSP_024881.
FT   VAR_SEQ     507    600       Missing (in isoform 2).
FT                                /FTId=VSP_024882.
FT   CONFLICT    321    321       F -> L (in Ref. 1; BAC39340).
SQ   SEQUENCE   600 AA;  67536 MW;  F29D8E90E4835B71 CRC64;
     MSDETVSRSQ FSLKTYAVRV FALPVSWYYS LSQIKFSPVA KKLFMVTAVS AVSVIFLAHH
     FKRRRGKQKG KVLPWEPEHL LLEHTRRAAS EKGSSCSSSR QNLTLSLSST KEKGSQCCNY
     PNGGLLSRYS GSAQSLGSVQ SVNSCHSCAC GNSNSWDKAD DDDIRLVNIP VTTPENLYLM
     GMELFEEALR RWEQALTFRS RQAEDEACSS VKLGAGDAIA EESVDDIISS EFIHKLEALL
     QRAYRLQEEF EATLGGSDPN SIANDTDKDT DMSLRETMDE LGLPDAMNMD SADLFASATE
     LAEQREAQQT FSLESFCPCP FYEEAMHLVE EGKIYSRVLR TEMLECLGDS DFLAKLHCIR
     QAFQLILAEA DNRSFLAESG RKILSALIVK ARKNPKKFQD VFDEMINFLE QTDHWDSTEL
     ELAARGVKNL NFYDVVLDFI LMDSFEDLEN PPTSIQSVVN NRWLNSSFKE SAVASSCWSV
     LKQKRQQMKI SDGFFAHFYA ICEHVSPVLA WGFLGPRNSL YDLCCFFKNQ VLFFLKDIFD
     FEKVRYSSID TLAEDLTHLL IRRTELLVTC LGADALRHAT TCTSGHSHAV PTALLEAKVQ
//
ID   Q4QQN3_MOUSE            Unreviewed;       321 AA.
AC   Q4QQN3;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   08-MAR-2011, entry version 38.
DE   SubName: Full=AU042671 protein;
DE   Flags: Fragment;
GN   Name=Gm15800; Synonyms=AU042671;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 HECT (E6AP-type E3 ubiquitin-protein
CC       ligase) domain.
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DR   EMBL; BC098193; AAH98193.1; -; mRNA.
DR   IPI; IPI00762814; -.
DR   UniGene; Mm.184589; -.
DR   UniGene; Mm.481359; -.
DR   Ensembl; ENSMUST00000042614; ENSMUSP00000048345; ENSMUSG00000042744.
DR   Ensembl; ENSMUST00000119892; ENSMUSP00000112647; ENSMUSG00000042744.
DR   MGI; MGI:3647820; Gm15800.
DR   eggNOG; roNOG12294; -.
DR   HOVERGEN; HBG067115; -.
DR   InParanoid; Q4QQN3; -.
DR   OrthoDB; EOG4SF951; -.
DR   ArrayExpress; Q4QQN3; -.
DR   Bgee; Q4QQN3; -.
DR   Genevestigator; Q4QQN3; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0006464; P:protein modification process; IEA:InterPro.
DR   InterPro; IPR000569; HECT.
DR   Pfam; PF00632; HECT; 1.
DR   SUPFAM; SSF56204; HECT; 1.
DR   PROSITE; PS50237; HECT; 1.
PE   2: Evidence at transcript level;
KW   Ubl conjugation pathway.
FT   NON_TER       1      1
SQ   SEQUENCE   321 AA;  36161 MW;  A52BE1D25FF16C1D CRC64;
     SSAVNKNKGK YILTPSPITY GEEQLLHFLG QLLGIAIRAD VPLPLDLLPS FWKTLVGEPL
     DPDQDLQEAD ILTYNYVKKF ESINDESELE ALCAEIASQH LATESPEGPK PCCRFTYLTM
     TGEEVELCSR GRHIPVAWEN KDIYAAAIRS LRLRELQNME CVTAVRAGLG SIIPLQLLTT
     LSPLEMELRT CGLPYINLEF LKAHTMYQVG LMETDQHIEL FWGALEMFTQ EELCKFIKFA
     CNQERIPFTC PCKDGGPDTA HVPPYPMKIA PPDGTAGPPD SRYIRVETCM FMIKLPQYSS
     LETMLEKLRC AIHYREDPLS G
//
ID   ATAD5_MOUSE             Reviewed;        1826 AA.
AC   Q4QY64; Q3TMG5; Q3UW85; Q3V306; Q3V3T9; Q5SSK4; Q8BUH4; Q8CGG7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   08-FEB-2011, entry version 53.
DE   RecName: Full=ATPase family AAA domain-containing protein 5;
DE   AltName: Full=Chromosome fragility-associated gene 1 protein;
GN   Name=Atad5; Synonyms=Frag1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
RP   RAD9A AND RB1, AND TISSUE SPECIFICITY.
RX   PubMed=15983387; DOI=10.1073/pnas.0504222102;
RA   Ishii H., Inageta T., Mimori K., Saito T., Sasaki H., Isobe M.,
RA   Mori M., Croce C.M., Huebner K., Ozawa K., Furukawa Y.;
RT   "Frag1, a homolog of alternative replication factor C subunits, links
RT   replication stress surveillance with apoptosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:9655-9660(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-762 AND 1463-1826 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cecum, Eye, Lung, Stomach, and Wolffian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-472 (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Involved in DNA damage response. Involved in a RAD9A-
CC       related damage checkpoint, a pathway that is important in
CC       determining whether DNA damage is compatible with cell survival or
CC       whether it requires cell elimination by apoptosis. Modulates the
CC       RAD9A interaction with BCL2 and thereby induces DNA damages-
CC       induced apoptosis.
CC   -!- SUBUNIT: Interacts with RB1 predominantly in G1 phase via its
CC       LXCXE motif. Interacts with RAD9A in growing cells. The
CC       interaction with RAD9A is reduced after exposure to DNA
CC       replication-inhibiting agents.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q4QY64-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q4QY64-2; Sequence=VSP_031098, VSP_031099;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed ubiquitously in all cell lines like
CC       teratocarcinoma, cell lymphoma, lymphoma.
CC   -!- INDUCTION: Down-regulated by DNA replication-inhibiting agents.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. ATR
CC       may stimulate the RAD9A dissociation (By similarity).
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH38279.2; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=CAI24765.1; Type=Erroneous gene model prediction;
CC       Sequence=CAI25200.1; Type=Erroneous gene model prediction;
CC       Sequence=CAI26037.1; Type=Erroneous gene model prediction;
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DR   EMBL; AY557610; AAT52048.1; -; mRNA.
DR   EMBL; AK032814; BAE20483.1; -; mRNA.
DR   EMBL; AK053857; BAE20694.1; -; mRNA.
DR   EMBL; AK085211; BAC39389.2; -; mRNA.
DR   EMBL; AK136531; BAE23031.1; -; mRNA.
DR   EMBL; AK165945; BAE38477.1; -; mRNA.
DR   EMBL; AL591113; CAI24765.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL663057; CAI24765.1; JOINED; Genomic_DNA.
DR   EMBL; AL672178; CAI24765.1; JOINED; Genomic_DNA.
DR   EMBL; AL672178; CAI25200.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL591113; CAI25200.1; JOINED; Genomic_DNA.
DR   EMBL; AL663057; CAI25200.1; JOINED; Genomic_DNA.
DR   EMBL; AL663057; CAI26037.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL591113; CAI26037.1; JOINED; Genomic_DNA.
DR   EMBL; AL672178; CAI26037.1; JOINED; Genomic_DNA.
DR   EMBL; BC038279; AAH38279.2; ALT_SEQ; mRNA.
DR   IPI; IPI00408664; -.
DR   IPI; IPI00885914; -.
DR   RefSeq; NP_001025027.1; NM_001029856.2.
DR   UniGene; Mm.89551; -.
DR   HSSP; P38630; 1SXJ.
DR   ProteinModelPortal; Q4QY64; -.
DR   SMR; Q4QY64; 1036-1149.
DR   STRING; Q4QY64; -.
DR   PhosphoSite; Q4QY64; -.
DR   PRIDE; Q4QY64; -.
DR   Ensembl; ENSMUST00000017694; ENSMUSP00000017694; ENSMUSG00000017550.
DR   GeneID; 237877; -.
DR   KEGG; mmu:237877; -.
DR   UCSC; uc007klg.1; mouse.
DR   CTD; 237877; -.
DR   MGI; MGI:2442925; Atad5.
DR   eggNOG; roNOG05763; -.
DR   GeneTree; ENSGT00530000064195; -.
DR   HOVERGEN; HBG101177; -.
DR   InParanoid; Q4QY64; -.
DR   OMA; LDVYNAV; -.
DR   NextBio; 383540; -.
DR   ArrayExpress; Q4QY64; -.
DR   Bgee; Q4QY64; -.
DR   CleanEx; MM_ATAD5; -.
DR   CleanEx; MM_FRAG1; -.
DR   Genevestigator; Q4QY64; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   GO; GO:0006974; P:response to DNA damage stimulus; IEA:UniProtKB-KW.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   Pfam; PF00004; AAA; 1.
DR   SMART; SM00382; AAA; 1.
DR   PROSITE; PS00674; AAA; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; DNA damage; Nucleotide-binding;
KW   Nucleus; Phosphoprotein.
FT   CHAIN         1   1826       ATPase family AAA domain-containing
FT                                protein 5.
FT                                /FTId=PRO_0000317619.
FT   NP_BIND    1119   1126       ATP (Potential).
FT   MOTIF      1415   1419       LXCXE motif.
FT   MOD_RES      44     44       Phosphoserine (By similarity).
FT   MOD_RES     366    366       Phosphoserine (By similarity).
FT   MOD_RES     603    603       Phosphoserine (By similarity).
FT   MOD_RES     642    642       Phosphoserine (By similarity).
FT   MOD_RES     652    652       Phosphoserine (By similarity).
FT   MOD_RES     653    653       Phosphothreonine (By similarity).
FT   MOD_RES     801    801       Phosphoserine (By similarity).
FT   MOD_RES    1103   1103       Phosphoserine (By similarity).
FT   MOD_RES    1104   1104       Phosphoserine (By similarity).
FT   VAR_SEQ     775    814       KMKIAPLFLAKRTKRAAIPVFDLDESSQDSSEQTQDCDVQ
FT                                -> NWIHYCFMDTLLLSTVLWITIHKCLGAIHPEYSGVLSQ
FT                                KS (in isoform 2).
FT                                /FTId=VSP_031098.
FT   VAR_SEQ     815   1826       Missing (in isoform 2).
FT                                /FTId=VSP_031099.
FT   CONFLICT    330    330       P -> H (in Ref. 2; BAE38477).
SQ   SEQUENCE   1826 AA;  203909 MW;  8830CAF65BCDDA81 CRC64;
     MVGVLSMAAA AAPLPVKDYE IEPCKKRRKD DDNSSCETIT KYLSPIGKTG DKVFSPPKPS
     NILHYFRKTS LTTEKPQSTK AYKIKPSPPL LVGNSKDCKT PLEVFSNREF KRKRKRVSLS
     SQLNDIKIQD ECPVEISNND SKEDGGLSDC VESSASVSLY KEHVEVLAES IEDSRNQPNT
     KSSKKKVNPK QCTTKSDDRI LRKRKRSKVT GQSESVPLAD ELSLPEDGGK DSKLTKPSLA
     EENDSRTHAT KRADLKESTI TVSYEEFVKS HKAAKVEEIP DPAVPACVPS GPGEAVKSGS
     EGELSGSCEP SPQLHLKTVT VLAQVHPTPP KKKGKIPPIF LKQKQPELEN SLSDPENEQP
     VQKRKSNVVI QEGQLELAVL EAWNSEASVP KCSMEERQQF MRAFRQPPPD TLKNGFKKPL
     EKQKDPSEKS VHEGDSSSEK IIENPNIQRV SSQGCLQSHA DRGSFPKEKS KKPNKKGKKT
     RTTAGGNREE NIQKEKTAFS LKDEQDQNSL RRSVRQKSEV LKSNALLNSE NLVCEDTAHD
     SVQMSLCNRN KSRSSSTPTR DMVTHHRAEP GSSLEYVSTR QPIRRSLRSC STPATNALGG
     TESEDAQDTI PVKASTPKSA RTSEKHNLYT AELIIVSSDS ESPIRMKFTR ISTPKKSKKS
     SKKSETTEEE LTSQKKKANS TSKNISKAKE LIEEAKAFQI GGSKTEETVV PLRRSSRHQA
     RSAKEKSPEI DDSVIVIDSS PTSIREPEKS QKKLQNLNDV LGKKLNKSSK NVPGKMKIAP
     LFLAKRTKRA AIPVFDLDES SQDSSEQTQD CDVQFKAKRD FLMSGLPDLL KRQIAKKAAA
     LDVYNAVSTS FQRVVHVQQK DDEYWLWHLK PPSCPLLTEF KELNTKVTDL SEYVVAFGEF
     STLNPNPRSN PAAVMMRTRK DFTKEVRNLL LEEIKCSNPE FSLEKYFPLL LKKRIEHQVL
     CEGHGKQASP QLQPDVSQKE TKRKQVATGN QKSKRKRQNE YSVSPEEMKG RSKDLDERIS
     SSCTNLDPSR DSGTEDMLWT EKYQPQNSNE LIGNELAVKK LHSWLKDWKR RAELEERHNL
     KGKRDEKEEG ILDLSDSTDF KGSSDDEENR LCNTVLITGP TGVGKTAAVY ACAQELGFKI
     FEVNASSQRS GRQILSQLKE ATQSHQVDKQ GVNSQKPCFF NNYNIGKSPK KLNSPGKVVT
     SPRKLPPSSP KTSGQKRALL PKTLANYFKV SSKSKSNDDV GALMGDDKGV KNSSLEQRQL
     IQTKSTNANN SHIKDVGAEE SNRKKATSLI LFEEVDVIFD EDAGFLNAVK TFMATTKRPV
     ILTTSDPTFS LVFDGCFEEI NFSIPSLLNV ASYLQVICLV ENFRTDFKDF VTLLTANACD
     IRKSILYLQF WIRSGGGILE ERPLSHCREN SRNTLVCSED GSDANINSKK PKRNRVALPR
     CDTGCAEALF GLKNIASPSQ DLLSLLKHKI TTKEEWQKLI QVLTEFHVQN IDLLHSNLEV
     ILPLPVHVVP DVRGAYGFPV TTQASAPASM GHLTRKQSKD QPLRKSQKRK QKKMVILDDS
     DLFDTGLDFS GELPSLSPAP SLSVEDNIRR DSNPEIKTQN SGFKPHSVPQ PPKTLAEKKC
     CMLVSHCLNS LSEFMENMSF IDALLTDPGE QNELGRSAFH WTNGRVKSGL CDEFSLENRD
     RWAPQSAGEL KATAEALSFT ECSSTISKAL ESLNSCKQLE RDPTNELTVC VSQRRHDACF
     RQSAANLDNA DKRMAVIKSV FSSRSFLTLG NKQASIIDYL PTLRNICRTE KLKEQEKNKR
     RFLHYFEGIH LEIPEETITT LAADFP
//
ID   Q4U256_MOUSE            Unreviewed;      1961 AA.
AC   Q4U256;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   08-MAR-2011, entry version 44.
DE   SubName: Full=Ankyrin 3;
GN   Name=Ank3;
OS   Mus musculus domesticus (western European house mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10092;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   MEDLINE=95340633; PubMed=7615634; DOI=10.1083/jcb.130.2.313;
RA   Peters L.L., John K.M., Lu F.M., Eicher E.M., Higgins A., Yialamas M.,
RA   Turtzo L.C., Otsuka A.J., Lux S.E.;
RT   "Ank3 (epithelial ankyrin), a widely distributed new member of the
RT   ankyrin gene family and the major ankyrin in kidney, is expressed in
RT   alternatively spliced forms, including forms that lack the repeat
RT   domain.";
RL   J. Cell Biol. 130:313-330(1995).
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DR   EMBL; L40632; AAB01607.1; -; mRNA.
DR   UniGene; Mm.235960; -.
DR   ProteinModelPortal; Q4U256; -.
DR   SMR; Q4U256; 61-825, 1468-1572.
DR   IntAct; Q4U256; 1.
DR   HOVERGEN; HBG004234; -.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR000488; Death.
DR   InterPro; IPR011029; DEATH-like.
DR   InterPro; IPR000906; ZU5.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 3.
DR   Gene3D; G3DSA:1.10.533.10; DEATH_like; 1.
DR   Pfam; PF00023; Ank; 20.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF00791; ZU5; 1.
DR   SMART; SM00248; ANK; 22.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00218; ZU5; 1.
DR   SUPFAM; SSF48403; ANK; 2.
DR   SUPFAM; SSF47986; DEATH_like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 21.
DR   PROSITE; PS50017; DEATH_DOMAIN; 1.
DR   PROSITE; PS51145; ZU5; 1.
PE   2: Evidence at transcript level;
KW   ANK repeat; Repeat.
SQ   SEQUENCE   1961 AA;  214145 MW;  911E8163149BEADB CRC64;
     MSEEPKEKPA KPAHRKRKGK KSDANASYLR AARAGHLEKA LDYIKNGVDV NICNQNGLNA
     LHLASKEGHV EVVSELLQRE ANVDAATKKG NTALHIASLA GQAEVVKVLV TNGANVNAQS
     QNGFTPLYMA AQENHLEVVR FLLDNGASQS LATEDGFTPL AVALQQGHDQ VVSLLLENDT
     KGKVRLPALH IAARKDDTKA AALLLQNDTN ADVESKSGFT PLHIAAHYGN INVATLLLNR
     AAAVDFTARN DITPLHVASK RGNANMVKLL LDRGAKIDAK TRDGLTPLHC GARSGHEQVV
     EMLLDRSAPI LSKTKNGLSP LHMATQGDHL NCVQLLLQHN VPVDDVTNDY LTALHVAAHC
     GHYKVAKVLL DKKASPNAKA LNGFTPLHIA CKKNRIRVME LLLKHGASIQ AVTESGLTPI
     HVAAFMGHVN IVSQLMHHGA SPNTTNVRGE TALHMAARSG QAEVVRYLVQ DGAQVEAKAK
     DDQTPLHISA RLGKADIVQQ LLQQGASPNA ATTSGYTPLH LAAREGHEDV AAFLLDHGAS
     LSITTKKGFT PLHVAAKYGK LEVASLLLQK SASPDAAGKS GLTPLHVAAH YDNQKVALLL
     LDQGASPHAA AKNGYTPLHI AAKKNQMDIA TSLLEYGADA NAVTRQGIAS VHLAAQEGHV
     DMVSLLLSRN ANVNLSNKSG LTPLHLAAQE DRVNVAEVLV NQGAHVDAQT KMGYTPLHVG
     CHYGNIKIVN FLLQHSAKVN AKTKNGYTAL HQAAQQGHTH IINVLLQNNA SPNELTVNGN
     TALAIARRLG YISVVDTLKV VTEEIMTTTT ITEKHKMNVP ETMNEVLDMS DDEVRKASAP
     EKLSDGEYIS DGEEGDKCTW FKIPKVQEVL VKSEDAITGD TDKYLGPQDL KELGDDSLPA
     EGYVGFSLGA RSASLRSFSS DRSYTLNRSS YARDSMMIEE LLVPSKEQHL TFTREFDSDS
     LRHYSWAADT LDNVNLVSSP VHSGFLVSFM VDARGGSMRG SRHHGMRIII PPRKCTAPTR
     ITCRLVKRHK LANPPPMVEG EGLASRLVEM GPAGAQFLGP VIVEIPHFGS MRGKERELIV
     LRSENGETWK EHQFDSKNED LAELLNGMDE ELDSPEELGT KRICRIITKD FPQYFAVVSR
     IKQESNQIGP EGGILSSTTV PLVQASFPEG ALTKRIRVGL QAQPVPEETV KKILGNKATF
     SPIVTVEPRR RKFHKPITMT IPVPPPSGEG VSNGYKGDAT PNLRLLCSIT GGTSPAQWED
     ITGTTPLTFI KDCVSFTTNV SARFWLADCH QVLETVGLAS QLYRELICVP YMAKFVVFAK
     TNDPVESSLR CFCMTDDRVD KTLEQQENFE EVARSKDIEV LEGKPIYVDC YGNLAPLTKG
     GQQLVFNFYS FKENRLPFSI KIRDTSQEPC GRLSFLKEPK TTKGLPQTAV CNLNITLPAH
     KKAEKADRRQ SFASLALRKR YSYLTEPSMS PQSPCERTDI RMAIVADHLG LSWTELAREL
     NFSVDEINQI RVENPNSLIS QSFMLLKKWV TRDGKNATTD ALTSVLTKIN RIDIVTLLEG
     PIFDYGNISG TRSFADENNV FHDPVDGHPS FQVELETPMG LYWTPPNPFQ QDDHFSDISS
     IESPFRTPSR LSDGLVPSQG NIEHPTGGPP VVTAEDTSLE DSKMDDSVTV TDPADPLDVD
     ESQLKDLCQS ECAQCWASVP GIPNDGRQAE PLRPQTRKVG MSSEQQEKGK SGPDEEVTED
     KVKSLFEDIQ LEEVEAEEMT EDQGQAMLNR VQRAELAMSS LAGWQNETPS GSLESPAQAR
     RLTGGLLDRL DDSSDQARDS ITSYLTGEPG KIEANGNHTA EVIPEAKAKP YFPESQNDIG
     KQSIKENLKP KTHGCGRTEE PVSPLTAYQK SLEETSKLVI EDAPKPCVPV GMKKMTRTTA
     DGKARLNLQE EEGSTRSEPK QGEGYKVKTK KEIRNVEKKT H
//
ID   HERC2_MOUSE             Reviewed;        4836 AA.
AC   Q4U2R1; O88473; Q3TRJ8; Q3TS47; Q3TST2; Q3UFQ6; Q3URH7; Q5DU32;
AC   Q7TPR5; Q80VV7; Q9QYT1; Q9Z168; Q9Z171;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=E3 ubiquitin-protein ligase HERC2;
DE            EC=6.3.2.-;
DE   AltName: Full=HECT domain and RCC1-like domain-containing protein 2;
GN   Name=Herc2; Synonyms=Jdf2, Kiaa0393, Rjs;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   DISEASE.
RC   STRAIN=C57BL/6;
RX   MEDLINE=98356175; PubMed=9689098; DOI=10.1073/pnas.95.16.9436;
RA   Lehman A.L., Nakatsu Y., Ching A., Bronson R.T., Oakey R.J.,
RA   Keiper-Hyrnko N., Finger J.N., Durham-Pierre D., Horton D.B.,
RA   Newton J.M., Lyon M.F., Brilliant M.H.;
RT   "A very large novel protein with diverse functional motifs is
RT   deficient in rjs (runty, jerky, sterile) mice.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:9436-9441(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DISEASE.
RX   MEDLINE=99138701; PubMed=9949213; DOI=10.1093/hmg/8.3.533;
RA   Ji Y., Walkowicz M.J., Buiting K., Johnson D.K., Tarvin R.E.,
RA   Rinchik E.M., Horsthemke B., Stubbs L., Nicholls R.D.;
RT   "The ancestral gene for transcribed, low-copy repeats in the Prader-
RT   Willi/Angelman region encodes a large protein implicated in protein
RT   trafficking, which is deficient in mice with neuromuscular and
RT   spermiogenic abnormalities.";
RL   Hum. Mol. Genet. 8:533-542(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 953-1553; 1845-2470 AND
RP   4123-4836.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord, Testis, and Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2966-4836 (ISOFORM 1).
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3618-4836 (ISOFORM 2).
RC   STRAIN=C57BL/6, and Czech II;
RC   TISSUE=Mammary gland, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   DISEASE.
RX   MEDLINE=99373249; PubMed=10441737; DOI=10.1007/s003359901106;
RA   Walkowicz M., Ji Y., Ren X., Horsthemke B., Russell L.B., Johnson D.,
RA   Rinchik E.M., Nicholls R.D., Stubbs L.;
RT   "Molecular characterization of radiation- and chemically induced
RT   mutations associated with neuromuscular tremors, runting, juvenile
RT   lethality, and sperm defects in jdf2 mice.";
RL   Mamm. Genome 10:870-878(1999).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2929, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that regulates ubiquitin-
CC       dependent retention of repair proteins on damaged chromosomes.
CC       Recruited to sites of DNA damage in response to ionizing radiation
CC       (IR) and facilitates the assembly of UBE2N and RNF8 promoting DNA
CC       damage-induced formation of 'Lys-63'-linked ubiquitin chains. Acts
CC       as a mediator of binding specificity between UBE2N and RNF8.
CC       Involved in the maintainance of RNF168 levels. E3 ubiquitin-
CC       protein ligase that promotes the ubiquitination and proteosomal
CC       degradation of XPA which influences the circadian oscillation of
CC       DNA excision repair activity (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts (when phosphorylated at Thr-4829) with RNF8
CC       (via FHA domain); this interaction increases after ionising
CC       radiation (IR) treatment. Interacts with XPA (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Recruited to sites of DNA damage in response to
CC       ionising radiation (IR) via its interaction with RNF8 (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q4U2R1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q4U2R1-2; Sequence=VSP_051975;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highest levels are found in brain and testis
CC       with lower levels in heart, lung, liver, skeletal muscle and
CC       kidney. Little expression detected in spleen.
CC   -!- PTM: Phosphorylation at Thr-4829 is required for interaction with
CC       RNF8.
CC   -!- DISEASE: Note=Defects in Herc2 are the cause of the runty, jerky,
CC       sterile phenotype (rjs), also known as the juvenile development
CC       and fertility phenotype (jfd2), which is characterized by reduced
CC       size, jerky gait, fertility problems including spermatocyte and
CC       oocyte abnormalities, defective maternal behavior and reduced
CC       lifespan with juvenile lethality.
CC   -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.
CC   -!- SIMILARITY: Contains 1 DOC domain.
CC   -!- SIMILARITY: Contains 1 HECT (E6AP-type E3 ubiquitin-protein
CC       ligase) domain.
CC   -!- SIMILARITY: Contains 1 MIB/HERC2 domain.
CC   -!- SIMILARITY: Contains 19 RCC1 repeats.
CC   -!- SIMILARITY: Contains 7 WD repeats.
CC   -!- SIMILARITY: Contains 1 ZZ-type zinc finger.
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DR   EMBL; AF061529; AAC31431.1; -; mRNA.
DR   EMBL; AF071173; AAD08658.1; -; mRNA.
DR   EMBL; AK141515; BAE24711.1; -; mRNA.
DR   EMBL; AK148361; BAE28504.1; -; mRNA.
DR   EMBL; AK161826; BAE36593.1; -; mRNA.
DR   EMBL; AK162270; BAE36828.1; -; mRNA.
DR   EMBL; AK162708; BAE37031.1; -; mRNA.
DR   EMBL; AK220338; BAD90404.1; -; mRNA.
DR   EMBL; BC044667; AAH44667.1; -; mRNA.
DR   EMBL; BC054829; AAH54829.1; -; mRNA.
DR   IPI; IPI00309574; -.
DR   IPI; IPI00314989; -.
DR   RefSeq; NP_034548.2; NM_010418.2.
DR   UniGene; Mm.20929; -.
DR   ProteinModelPortal; Q4U2R1; -.
DR   SMR; Q4U2R1; 426-779, 1204-1288, 1868-1929, 2554-2632, 2701-2756, 2777-2914, 2961-3326, 3862-4320, 4393-4791.
DR   STRING; Q4U2R1; -.
DR   PhosphoSite; Q4U2R1; -.
DR   PRIDE; Q4U2R1; -.
DR   Ensembl; ENSMUST00000041015; ENSMUSP00000035719; ENSMUSG00000030451.
DR   Ensembl; ENSMUST00000076226; ENSMUSP00000075579; ENSMUSG00000030451.
DR   GeneID; 15204; -.
DR   KEGG; mmu:15204; -.
DR   UCSC; uc009hdv.1; mouse.
DR   CTD; 15204; -.
DR   MGI; MGI:103234; Herc2.
DR   eggNOG; roNOG13681; -.
DR   GeneTree; ENSGT00590000082801; -.
DR   HOVERGEN; HBG081598; -.
DR   InParanoid; Q4U2R1; -.
DR   OrthoDB; EOG41C6V9; -.
DR   PhylomeDB; Q4U2R1; -.
DR   NextBio; 287753; -.
DR   ArrayExpress; Q4U2R1; -.
DR   Bgee; Q4U2R1; -.
DR   Genevestigator; Q4U2R1; -.
DR   GermOnline; ENSMUSG00000030451; Mus musculus.
DR   GO; GO:0005680; C:anaphase-promoting complex; IEA:InterPro.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IEA:InterPro.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   InterPro; IPR004939; Ananphase-promot_cplx_su10_DOC.
DR   InterPro; IPR006624; Beta-propeller_rpt_TECPR.
DR   InterPro; IPR021097; CPH_domain.
DR   InterPro; IPR001199; Cyt_B5.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR000569; HECT.
DR   InterPro; IPR010606; Mib_Herc2.
DR   InterPro; IPR000408; Reg_chr_condens.
DR   InterPro; IPR009091; Reg_csome_cond/b-lactamase_inh.
DR   InterPro; IPR014722; Transl_SH3-like_sub.
DR   InterPro; IPR000433; Znf_ZZ.
DR   Gene3D; G3DSA:3.10.120.10; Cyt_B5; 1.
DR   Gene3D; G3DSA:2.130.10.30; Reg_csome_cond/b-lactamase_inh; 3.
DR   Gene3D; G3DSA:2.30.30.30; Ribosomal_L2; 1.
DR   Pfam; PF03256; APC10; 1.
DR   Pfam; PF11515; Cul7; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF06701; MIB_HERC2; 1.
DR   Pfam; PF00415; RCC1; 18.
DR   Pfam; PF00569; ZZ; 1.
DR   PRINTS; PR00633; RCCNDNSATION.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00706; TECPR; 4.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF55856; Cyt_B5; 1.
DR   SUPFAM; SSF49785; Gal_bind_like; 1.
DR   SUPFAM; SSF56204; HECT; 1.
DR   SUPFAM; SSF50985; RCC1/BLIP-II; 3.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; FALSE_NEG.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR   PROSITE; PS51284; DOC; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS51416; MIB_HERC2; 1.
DR   PROSITE; PS00625; RCC1_1; FALSE_NEG.
DR   PROSITE; PS00626; RCC1_2; FALSE_NEG.
DR   PROSITE; PS50012; RCC1_3; 19.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR   PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; DNA damage; DNA repair;
KW   Ligase; Metal-binding; Nucleus; Phosphoprotein; Repeat;
KW   Ubl conjugation pathway; WD repeat; Zinc; Zinc-finger.
FT   CHAIN         1   4836       E3 ubiquitin-protein ligase HERC2.
FT                                /FTId=PRO_0000229740.
FT   REPEAT        3     46       WD 1.
FT   REPEAT      287    328       WD 2.
FT   REPEAT      491    530       WD 3.
FT   REPEAT      514    569       RCC1 1.
FT   REPEAT      570    621       RCC1 2.
FT   REPEAT      624    675       RCC1 3.
FT   REPEAT      676    727       RCC1 4.
FT   REPEAT      705    744       WD 4.
FT   REPEAT      729    779       RCC1 5.
FT   DOMAIN     1208   1284       Cytochrome b5 heme-binding.
FT   DOMAIN     1860   1933       MIB/HERC2.
FT   DOMAIN     2760   2937       DOC.
FT   REPEAT     2959   3010       RCC1 6.
FT   REPEAT     3011   3065       RCC1 7.
FT   REPEAT     3066   3117       RCC1 8.
FT   REPEAT     3097   3134       WD 5.
FT   REPEAT     3118   3169       RCC1 9.
FT   REPEAT     3172   3223       RCC1 10.
FT   REPEAT     3225   3275       RCC1 11.
FT   REPEAT     3276   3327       RCC1 12.
FT   REPEAT     3928   3969       WD 6.
FT   REPEAT     3953   4004       RCC1 13.
FT   REPEAT     4006   4058       RCC1 14.
FT   REPEAT     4060   4110       RCC1 15.
FT   REPEAT     4112   4164       RCC1 16.
FT   REPEAT     4166   4216       RCC1 17.
FT   REPEAT     4218   4268       RCC1 18.
FT   REPEAT     4243   4285       WD 7.
FT   REPEAT     4270   4320       RCC1 19.
FT   DOMAIN     4459   4796       HECT.
FT   ZN_FING    2703   2750       ZZ-type.
FT   COILED      948    981       Potential.
FT   ACT_SITE   4764   4764       Glycyl thioester intermediate (By
FT                                similarity).
FT   MOD_RES    1578   1578       Phosphoserine (By similarity).
FT   MOD_RES    1589   1589       Phosphoserine (By similarity).
FT   MOD_RES    1943   1943       Phosphoserine (By similarity).
FT   MOD_RES    1945   1945       Phosphothreonine (By similarity).
FT   MOD_RES    2455   2455       Phosphoserine (By similarity).
FT   MOD_RES    2929   2929       Phosphoserine.
FT   MOD_RES    4812   4812       Phosphoserine (By similarity).
FT   MOD_RES    4813   4813       Phosphoserine (By similarity).
FT   MOD_RES    4816   4816       Phosphoserine (By similarity).
FT   MOD_RES    4829   4829       Phosphothreonine (By similarity).
FT   VAR_SEQ    3637   3672       Missing (in isoform 2).
FT                                /FTId=VSP_051975.
FT   CONFLICT    692    692       H -> L (in Ref. 1; AAC31431).
FT   CONFLICT    724    724       V -> A (in Ref. 1; AAC31431).
FT   CONFLICT    747    747       G -> R (in Ref. 1; AAC31431).
FT   CONFLICT    756    756       F -> L (in Ref. 1; AAC31431).
FT   CONFLICT    929    929       P -> R (in Ref. 1; AAC31431).
FT   CONFLICT   1114   1114       N -> S (in Ref. 1; AAC31431 and 3;
FT                                BAE24711).
FT   CONFLICT   1235   1235       D -> G (in Ref. 1; AAC31431 and 3;
FT                                BAE24711).
FT   CONFLICT   2348   2348       A -> P (in Ref. 1; AAC31431).
FT   CONFLICT   2470   2470       G -> S (in Ref. 3; BAE36828).
FT   CONFLICT   2523   2523       E -> D (in Ref. 1; AAC31431).
FT   CONFLICT   2567   2567       Y -> F (in Ref. 1; AAC31431).
FT   CONFLICT   2572   2572       V -> L (in Ref. 1; AAC31431).
FT   CONFLICT   3095   3095       Q -> E (in Ref. 1; AAC31431 and 4;
FT                                BAD90404).
FT   CONFLICT   3107   3107       Y -> C (in Ref. 1; AAC31431 and 4;
FT                                BAD90404).
FT   CONFLICT   3114   3114       P -> A (in Ref. 1; AAC31431 and 4;
FT                                BAD90404).
FT   CONFLICT   3161   3161       S -> T (in Ref. 1; AAC31431).
FT   CONFLICT   3385   3386       VV -> LL (in Ref. 1; AAC31431 and 4;
FT                                BAD90404).
FT   CONFLICT   3508   3508       V -> A (in Ref. 1; AAC31431 and 4;
FT                                BAD90404).
FT   CONFLICT   4069   4069       E -> K (in Ref. 4; BAD90404).
FT   CONFLICT   4187   4187       C -> S (in Ref. 1; AAC31431).
FT   CONFLICT   4604   4604       P -> S (in Ref. 3; BAE36593).
FT   CONFLICT   4716   4716       T -> A (in Ref. 1; AAC31431).
FT   CONFLICT   4723   4723       R -> C (in Ref. 2; AAD08658).
FT   CONFLICT   4730   4730       R -> S (in Ref. 1; AAC31431).
FT   CONFLICT   4752   4752       N -> Y (in Ref. 1; AAC31431).
FT   CONFLICT   4790   4790       C -> S (in Ref. 1; AAC31431).
SQ   SEQUENCE   4836 AA;  527530 MW;  B939F17D3089AD61 CRC64;
     MPSESFCLAA QSRLDSKWLK TDIQLAFTRD GLCGLWNEMV KDGEIVYTGT ELAQNRELPL
     RKDDGVDAQS GTKKEDLNDK EKKEEEETPA PVYRAKSILE SWVWGRQPDV NELKECLSVL
     VKEQQALAVQ SATTTLSALR LKQRLVILER YFIALNRTVF QENVKVKWKS SSISVPPTEK
     KSARPTGRGV EGLARVGSRA ALSFAFAFLR RAWRSGEDAD LCSELLQESL DALRALPEAS
     LFDESTVSSV WLEVVERATR FLRSVVTGDV HGTPGTKGPG GVPLQDQHLA LAILLELAVQ
     RGTLSQMLSA ILLLLQLWDS GAQETDNERS AQGTSAPLLP LLQRFQSIIC SKDVPHTESD
     MHLLSGPLSP NESFLRYLTL PQDNELAIDL RQTAVVVMAH LDRLATPCMP PLCSSPTSHK
     GSLQEVIGWG LIGWKYYANV IGPIQCEGLA SLGVMQVACA EKRFLILSRN GRVYTQAYNS
     DMLAPQLVQG LASRNIVKIA AHSDGHHYLA LAATGEVYSW GCGDGGRLGH GDTVPLEEPK
     VISAFSGKQA GKHVVHIACG STYSAAITAE GELYTWGRGN YGRLGHGSSE DEAIPMLVAG
     LKGLKVIDVA CGSGDAQTLA VTENGQVWSW GDGDYGKLGR GGSDGCKTPK LIEKLQDLDV
     IKVRCGSQFS IALTKDGQVY SWGKGDNQRL GHGTEEHVRY PKLLEGLQGK KVIDVAAGST
     HCLVLTEDSE VHSWGSNDQC QHFDTLGVTK PEPTAFPGLD SKHIVGIACG PAQSFAWSSC
     SEWSIGLRVP FVVDICSMTF EQLDLLLRQV SEGMDGTADW PPPQEKECMA VATLNLLRLQ
     LHAAISHQVD PEFLGLGLGS VLLNSLKQTV VTLASSAGVL STVQSAAQAV LQSGWSVLLP
     TAEERARALS ALLPCTVSGN EVNISPGRPF MIDLLVGSLM ADGGLESALN AAITAEIQDI
     EAKKEAQKEK EIDEQEASAS TFHRSRTPLD KDLINTGIYE SSGKQCLPLV QLIQQLLRNI
     ASQTVARLKD VARRISSCLD FEQQSCERSA SLDLLLRFQR LLISKLYPGE KIGPISDTSS
     PELMGVGSLL KKYTALVCTH IGDILPVAAS IASNSWQHFA EVACVMEGDF TGVLLPELVV
     SIVLLLSKNA SLMQEAGAIP LLGGLLEHLD RFNHLAPGKE RDDHEELAWP GIMESFFTGQ
     NCRNNEEVTL IRKADLENHN KDGGFWTVID GKVYDIKDFQ TQSLTGNSIL AQFAGEDPVV
     ALEAALQFED TQESMHAFCV GQYLEPDQEV VTIPDLGSLS SPLIDTERNL GLLLGLHASY
     LAMSTPLSPV EVECAKWLQS SIFSGGLQTS QIHYSYNEEK DEDHCSSPGG TPISKSRLCS
     HRWALGDHSQ AFLQAIADNN IQDYNVKDFL CQIERYCRQC HLTTPITFPP EHPVEEVGRL
     LLCCLLKHED LGHVALSLVH VGTLGIEQVK HRTLPKSVVD VCRVVYQAKC SLIKTHQEQG
     RSYKEVCAPV IERLRFLFNE LRPAVCSDLS IMSKFKLLGS LPRWRRIAQK IIRERRKKRV
     PKKPESIDSE EKIGNEESDL EEACVLPHSP INVDKRPISM KSPKDKWQPL LNTVTGVHKY
     KWLKQNVQGL YPQSALLNTI VEFALKEEPV DVEKMRKCLL KQLERAEVRL EGIDTILKLA
     AKSFLLPSVQ YAMFCGWQRL IPEGIDIGEP LTDCLRDVDL IPPFNRMLLE VTFGKLYAWA
     VQNIRSVLMD ASARFKELGI QPVPLQTITN ENPAGPSLGT IPQARFLLVM LSMLTLQHGA
     NNLDLLLNSG TLALTQTALR LIGPTCDSVE DDMNASARGA SATVLEETRK ETAPVQLPVS
     GPELAAMMKI GTRVMRGVDW KWGDQDGPPP GLGRVIGELG EDGWIRVQWD TGSTNSYRMG
     KEGKYDLKLV ELPVSSQPSA EDSDTEDDSE AEQGERNIHP TAMMLTSVIN LLQTLCLSVG
     VHADIMQSEA TKTLCGLLRM LVESGTTDKP APPDRLVARE QHRSWCTLGF VRSIALTPQA
     CGALSSPRWI TLLMKVVEGH APFTAASLQR QILAVHLLQA VLPSWDKTER ARDMKCLVEK
     LFGFLGSLLT TCSSDVPLLR ESTLRKRRAR PQASLTATHS STLAEEVVGL LRTLHSLTQW
     NGLINKYINS QLCSVTQSYA GKTSERAQLE DYFPDSENLE VGGLMAVLAV IGGIDGRLRL
     GGQVMHDEFG EGTVTRITPK GRITVQFCDM RMCRVCPLNQ LKPLPAVAFS VNNLPFTEPM
     LSVWAELVNL AGSKLEKHKT KKSAKPAFAG QVDLDLLRSQ QLKLYILKAG RALLSHQDKL
     RQILSQPAVQ GTGTLQTDDG AAASPDLGDM SPEGPQPPMI LLQQLLSSAT QPSPVKAIFD
     KQELEAAALA LCQCLAVEST HPSSPGCEDC SSSEATTPVS VQHIHLARAK KRRQSPAPAL
     PIVVQLMEMG FPRKNIEFAL KSLTGTSGNA SGLPGVEALV GWLLDHSDVQ VTEFSDAETL
     SDEYSDEEVV EDVDDTPYPV AAGAVVTESQ TYKKRADFLS NDDYAVYVRE NVQVGMMVRC
     CRTYEEVCEG DVGKVIKLDR DGLHDLNVQC DWQQKGGTYW VRYIHVELIG YPPPSSSSHI
     KIGDKVRVKA SVTTPKYKWG SVTHQSVGLV KAFSANGKDI IVDFPQQSHW TGLLSEMELV
     PSIHPGVTCD GCQTFPINGS RFKCRNCDDF DFCETCFKTK KHNTRHTFGR INEPGQSAVF
     CGRSGKQLKR CHSSQPGMLL DSWSRMVKSL NVSSSVNQAS RLIDGSEPCW QSSGSQGKHW
     IRLEIFPDVL VHRLKMIVDP ADSSYMPSLV VVSGGNSLNN LIELKTININ QTDTTVPLLS
     DCAEYHRYIE IAIKQCRSSG IDCKIHGLIL LGRIRAEEED LAAVPFLASD NEEEEDDKGS
     TGSLIRKKTP GLESTATIRT KVFVWGLNDK DQLGGLKGSK IKVPSFSETL SALNVVQVAG
     GSKSLFAVTV EGKVYSCGEA TNGRLGLGMS SGTVPIPRQI TALSSYVVKK VAVHSGGRHA
     TALTVDGKVF SWGEGDDGKL GHFSRMNCDK PRLIQALKTK RIRDIAYGSS HSAPLTSSGE
     LYTWGLGEYG RLGHGDNTTQ LKPKMVKVLL GHRVIQVACG SRDAQTLALT DEGLVFSWGD
     GDFGKLGRGG SEGCNIPQNI ERLNGQGVCQ IECGAQFSLA LTKSGVVWTW GKGDYFRLGH
     GSDVHVRKPQ VVEGLRGKKI VHVAVGALHC LAVTDSGQVY AWGDNDHGQQ GNGTTTVNRK
     PTLVQGLEGQ KITRVACGSS HSVAWTTVDV ATPSVHEPVL FQTARDPLGA SYLGVPSDAD
     SSSSSNKISG ANNCKPNRPS LAKIVVSLEG NLAKQQALSH ILTALQIMYA RDAVVGALMP
     AGMLAPVECP SFSSSAPASD VSAMASPMHM EDSTLAADLE DRLSPNLWQE KREIVSSEDA
     VTPSAVTPSA PSASSRPFIP VTDDPGAVSI IAETMTKTKE DVESQNKTSG PEPQSLDEFT
     SLLIPDDTRV VVELLKLSVC SRAGDKGREV LSAVLSGMGT AYPQVADMLL ELCVTELEDV
     ATDSQSGRLS SQPVVVESSH PYTDDTSTSG TVKIPGAEGL RVEFDRQCST ERRHDPLTVM
     DGVNRIVSVR SGREWSDWSS ELRIPGDELK WKFISDGSVN GWGWRFTVYP IMPAAGPKDL
     LSDRCVLSCP SMDLVTCLLD FRLNLTSNRS IVPRLAASLA ACAQLSALAA SHRMWALQRL
     RRLLTTEFGQ SININRLLGE NDGESRALSF TGSALAALVK GLPEALQRQF EYEDPIVRGG
     KQLLHSPFFK VLVALACDLE LDTLPCCAET HKWAWFRRYC MASRVAVALD KRTPLPRLFL
     DEVAKKIREL MADSESMDVL HESHSIFKRE QDEQLVQWMN RRPDDWTLSA GGSGTIYGWG
     HNHRGQLGGI EGAKVKVPTP CEALATLRPV QLIGGEQTLF AVTADGKLYA TGYGAGGRLG
     IGGTESVSTP TLLESIQHVF IKKVAVNSGG KHCLALSSEG EVYSWGEAED GKLGHGNRSP
     CDRPRVIESL RGIEVVDVAA GGAHSACVTA AGDLYTWGKG RYGRLGHSDS EDQLKPKLVE
     ALQGHRVIDI ACGSGDAQTL CLTDDDTVWS WGDGDYGKLG RGGSDGCKVP MKIDSLTGLG
     VVKVECGSQF SVALTKSGAV YTWGKGDYHR LGHGSDDHVR RPRQVQGLQG KKVIAIATGS
     LHCVCCTEDG EVYTWGDNDE GQLGDGTTNA IQRPRLVAAL QGKKVNRVAC GSAHTLAWST
     SKPASAGKLP AQVPMEYNHL QEIPIIALRN RLLLLHHISE LFCPCIPMFD LEGSLDETGL
     GPSVGFDTLR GILISQGKEA AFRKVVQATM VRDRQHGPVV ELNRIQVKRS RSKGGLAGPD
     GTKSVFGQMC AKMSSFSPDS LLLPHRVWKV KFVGESVDDC GGGYSESIAE ICEELQNGLT
     PLLIVTPNGR DESGANRDCY LLNPATRAPV HCSMFRFLGV LLGIAIRTGS PLSLNLAEPV
     WKQLAGMSLT IADLSEVDKD FIPGLMYIRD NEATSEEFEA MSLPFTVPSA SGQDIQLSSK
     HTHITLDNRA EYVRLAINYR LHEFDEQVAA VREGMARVVP VPLLSLFTGY ELETMVCGSP
     DIPLHLLKSV ATYKGIEPSA SLVQWFWEVM ESFSNTERSL FLRFVWGRTR LPRTIADFRG
     RDFVIQVLDK YNPPDHFLPE SYTCFFLLKL PRYSCKQVLE EKLKYAIHFC KSIDTDDYAR
     IALTGEPAAD DSSEDSDNED ADSFASDSTQ DYLTGH
//
ID   SR1IP_MOUSE             Reviewed;         153 AA.
AC   Q4V9W2; Q05CD6; Q8CGG6; Q9CRM9; Q9CRR4; Q9CXR0;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Protein SREK1IP1;
DE   AltName: Full=SFRS12-interacting protein 1;
DE   AltName: Full=SREK1-interacting protein 1;
GN   Name=Srek1ip1; Synonyms=Sfrs12ip1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Muellerian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain, Eye, Mammary gland, and Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Possible splicing regulator involved in the control of
CC       cellular survival (By similarity).
CC   -!- SUBUNIT: Interacts with SREK1/SFRS12 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q4V9W2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q4V9W2-2; Sequence=VSP_029642;
CC   -!- SIMILARITY: Contains 1 CCHC-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB29157.1; Type=Erroneous termination; Positions=152; Note=Translated as Lys;
CC       Sequence=BAB31175.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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DR   EMBL; AK014102; BAB29157.1; ALT_SEQ; mRNA.
DR   EMBL; AK018357; BAB31175.1; ALT_SEQ; mRNA.
DR   EMBL; AK020113; BAB31999.3; -; mRNA.
DR   EMBL; BC027133; AAH27133.1; -; mRNA.
DR   EMBL; BC038302; AAH38302.1; -; mRNA.
DR   EMBL; BC096661; AAH96661.1; -; mRNA.
DR   EMBL; BC116993; AAI16994.1; -; mRNA.
DR   EMBL; BC116999; AAI17000.1; -; mRNA.
DR   IPI; IPI00110655; -.
DR   IPI; IPI00807850; -.
DR   RefSeq; NP_080351.2; NM_026075.2.
DR   UniGene; Mm.125465; -.
DR   PhosphoSite; Q4V9W2; -.
DR   PRIDE; Q4V9W2; -.
DR   Ensembl; ENSMUST00000022230; ENSMUSP00000022230; ENSMUSG00000021716.
DR   GeneID; 67288; -.
DR   KEGG; mmu:67288; -.
DR   UCSC; uc007rtm.1; mouse.
DR   CTD; 67288; -.
DR   MGI; MGI:1914538; Srek1ip1.
DR   eggNOG; roNOG17897; -.
DR   GeneTree; ENSGT00510000047710; -.
DR   HOVERGEN; HBG104841; -.
DR   InParanoid; Q4V9W2; -.
DR   OMA; NKDNVRA; -.
DR   OrthoDB; EOG4PG62P; -.
DR   NextBio; 324124; -.
DR   ArrayExpress; Q4V9W2; -.
DR   Bgee; Q4V9W2; -.
DR   CleanEx; MM_SFRS12IP1; -.
DR   Genevestigator; Q4V9W2; -.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR001878; Znf_CCHC.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Metal-binding; mRNA processing; mRNA splicing;
KW   Phosphoprotein; Zinc; Zinc-finger.
FT   CHAIN         1    153       Protein SREK1IP1.
FT                                /FTId=PRO_0000311923.
FT   ZN_FING      13     30       CCHC-type.
FT   COMPBIAS     76    141       Lys-rich.
FT   MOD_RES      45     45       Phosphoserine (By similarity).
FT   MOD_RES      46     46       Phosphoserine (By similarity).
FT   MOD_RES      47     47       Phosphothreonine (By similarity).
FT   MOD_RES      48     48       Phosphoserine (By similarity).
FT   MOD_RES      49     49       Phosphoserine (By similarity).
FT   MOD_RES      52     52       Phosphoserine (By similarity).
FT   VAR_SEQ      69    153       RINEEEEKKKEKSREKIKLKKRRKRSYSSATEEDSAKQKKQ
FT                                KYQKKEKKKEKKNKSKKGKHHKKEKKKRKKEKRSSPYHSEL
FT                                TKK -> SKPWFLPTVLF (in isoform 2).
FT                                /FTId=VSP_029642.
FT   CONFLICT    119    119       E -> K (in Ref. 2; AAH38302).
FT   CONFLICT    139    140       KE -> RG (in Ref. 1; BAB29157).
SQ   SEQUENCE   153 AA;  18151 MW;  B42AA17FBC299448 CRC64;
     MAVPGCNKDN VRAGCRKCGY PGHLTFECRN FLRVDPKRDI VLDVSSTSSE DSDEENEELN
     KLQALQEKRI NEEEEKKKEK SREKIKLKKR RKRSYSSATE EDSAKQKKQK YQKKEKKKEK
     KNKSKKGKHH KKEKKKRKKE KRSSPYHSEL TKK
//
ID   PDS5B_MOUSE             Reviewed;        1446 AA.
AC   Q4VA53; Q3TNZ4; Q7TSS4; Q80TM8; Q8BJ18; Q8BLH6; Q8BX77;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Sister chromatid cohesion protein PDS5 homolog B;
DE   AltName: Full=Androgen-induced proliferation inhibitor;
DE   AltName: Full=Androgen-induced prostate proliferative shutoff-associated protein AS3;
GN   Name=Pds5b; Synonyms=Aprin, As3, Kiaa0979;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Brain;
RA   Geck P., Maffini M., Sonnenschein C., Soto A.M.;
RT   "The AS3 proliferative arrest gene has an ancient eukaryotic heritage
RT   and shows highly conserved functional domains in mice.";
RL   Proc. Annu. Meet. Am. Assoc. Cancer Res. 43:987-987(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 625-1446 (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1092-1446 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, Head, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 256-1446 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1356, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1356, AND MASS
RP   SPECTROMETRY.
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1356, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1166; SER-1257 AND
RP   SER-1356, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1281 AND SER-1381, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Regulator of sister chromatid cohesion in mitosis which
CC       may stabilize cohesin complex association with chromatin. May
CC       couple sister chromatid cohesion during mitosis to DNA
CC       replication. Cohesion ensures that chromosome partitioning is
CC       accurate in both meiotic and mitotic cells and plays an important
CC       role in DNA repair. Plays a role in androgen-induced proliferative
CC       arrest in prostate cells (By similarity).
CC   -!- SUBUNIT: Interacts with the cohesin complex. Interacts with RAD21;
CC       the interaction is direct. Interacts with WAPAL (via FGF motifs)
CC       or CDCA5 (via the FGF motif); the interaction is direct, cohesin-
CC       dependent and competitive (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q4VA53-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q4VA53-2; Sequence=VSP_052403, VSP_052405, VSP_052406;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q4VA53-3; Sequence=VSP_052404;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in prostate.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the PDS5 family.
CC   -!- SIMILARITY: Contains 3 A.T hook DNA-binding domains.
CC   -!- SIMILARITY: Contains 1 HEAT repeat.
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DR   EMBL; AY102267; AAM52216.1; -; mRNA.
DR   EMBL; AK041682; BAC31031.1; -; mRNA.
DR   EMBL; AK045159; BAC32242.1; -; mRNA.
DR   EMBL; AK048706; BAC33427.1; -; mRNA.
DR   EMBL; AK164853; BAE37943.1; -; mRNA.
DR   EMBL; BC096539; AAH96539.1; -; mRNA.
DR   EMBL; AK122414; BAC65696.1; -; mRNA.
DR   IPI; IPI00317401; -.
DR   IPI; IPI00776026; -.
DR   IPI; IPI00845638; -.
DR   RefSeq; NP_780519.3; NM_175310.6.
DR   UniGene; Mm.32959; -.
DR   ProteinModelPortal; Q4VA53; -.
DR   SMR; Q4VA53; 366-415.
DR   STRING; Q4VA53; -.
DR   PhosphoSite; Q4VA53; -.
DR   PRIDE; Q4VA53; -.
DR   Ensembl; ENSMUST00000016569; ENSMUSP00000016569; ENSMUSG00000034021.
DR   Ensembl; ENSMUST00000038900; ENSMUSP00000038421; ENSMUSG00000034021.
DR   GeneID; 100710; -.
DR   KEGG; mmu:100710; -.
DR   UCSC; uc009auh.1; mouse.
DR   CTD; 100710; -.
DR   MGI; MGI:2140945; Pds5b.
DR   eggNOG; roNOG09271; -.
DR   GeneTree; ENSGT00390000012488; -.
DR   HOVERGEN; HBG108241; -.
DR   InParanoid; Q4VA53; -.
DR   OMA; EERQSGN; -.
DR   OrthoDB; EOG46T30N; -.
DR   PhylomeDB; Q4VA53; -.
DR   NextBio; 354602; -.
DR   ArrayExpress; Q4VA53; -.
DR   Bgee; Q4VA53; -.
DR   Genevestigator; Q4VA53; -.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007064; P:mitotic sister chromatid cohesion; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 5.
DR   SMART; SM00384; AT_hook; 3.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell cycle; Cell division; Mitosis;
KW   Nucleus; Phosphoprotein; Repeat.
FT   CHAIN         1   1446       Sister chromatid cohesion protein PDS5
FT                                homolog B.
FT                                /FTId=PRO_0000287425.
FT   REPEAT      383    419       HEAT.
FT   DNA_BIND   1247   1259       A.T hook 1.
FT   DNA_BIND   1285   1297       A.T hook 2.
FT   DNA_BIND   1370   1382       A.T hook 3.
FT   MOD_RES    1136   1136       N6-acetyllysine (By similarity).
FT   MOD_RES    1162   1162       Phosphoserine (By similarity).
FT   MOD_RES    1165   1165       Phosphoserine (By similarity).
FT   MOD_RES    1166   1166       Phosphoserine.
FT   MOD_RES    1176   1176       Phosphoserine (By similarity).
FT   MOD_RES    1182   1182       Phosphoserine (By similarity).
FT   MOD_RES    1191   1191       Phosphoserine (By similarity).
FT   MOD_RES    1255   1255       Phosphoserine (By similarity).
FT   MOD_RES    1257   1257       Phosphoserine.
FT   MOD_RES    1281   1281       Phosphoserine.
FT   MOD_RES    1299   1299       Phosphothreonine (By similarity).
FT   MOD_RES    1356   1356       Phosphoserine.
FT   MOD_RES    1365   1365       Phosphothreonine (By similarity).
FT   MOD_RES    1368   1368       Phosphothreonine (By similarity).
FT   MOD_RES    1377   1377       Phosphoserine (By similarity).
FT   MOD_RES    1381   1381       Phosphoserine.
FT   VAR_SEQ       1    529       Missing (in isoform 2).
FT                                /FTId=VSP_052403.
FT   VAR_SEQ    1206   1206       L -> LVR (in isoform 3).
FT                                /FTId=VSP_052404.
FT   VAR_SEQ    1207   1230       SELEKPRSRKKAPVTDPEEKLGMD -> VRVRCLVGRVMRL
FT                                LIVIVLVIFAL (in isoform 2).
FT                                /FTId=VSP_052405.
FT   VAR_SEQ    1231   1446       Missing (in isoform 2).
FT                                /FTId=VSP_052406.
FT   CONFLICT    496    496       W -> R (in Ref. 1; AAM52216).
FT   CONFLICT    966    966       I -> T (in Ref. 1; AAM52216).
FT   CONFLICT    978    978       A -> S (in Ref. 1; AAM52216).
SQ   SEQUENCE   1446 AA;  164419 MW;  3540041DE3C7FCBE CRC64;
     MAHSKTRTND GKITYPPGVK EISDKISKEE MVRRLKMVVK TFMDMDQDSE EEKELYLNLA
     LHLASDFFLK HPDKDVRLLV ACCLADIFRI YAPEAPYTSP DKLKDIFMFI TRQLKGLEDT
     KSPQFNRYFY LLENIAWVKS YNICFELEDS NEIFTQLYRT LFSVINNGHN QKVHMHMVDL
     MSSIICEGDT VSQELLDTVL VNLVPAHKNL NKQAYDLAKA LLKRTAQAIE PYITNFFNQV
     LMLGKTSISD LSEHVFDLIL ELYNIDSHLL LSVLPQLEFK LKSNDNEERL QVVKLLAKMF
     GAKDSELASQ NKPLWQCYLG RFNDIHVPIR LECVKFASHC LMNHPDLAKD LTEYLKVRSH
     DPEEAIRHDV IVSIVTAAKK DILLVNDHLL NFVRERTLDK RWRVRKEAMM GLAQIYKKYS
     LQSAAGKDAA KQISWVKDKL LHIYYQNSID DRLLVERIFA QYMVPHNLET TERMKCLYYL
     YATLDLNAVK ALNEMWKCQN LLRHQVKDLL DLIKQPKTDA SVKAIFSKVM VITRNLPDPG
     KAQDFMKKFT QVLEDDEKIR KQLEALVSPT CSCKQAEGCV REITKKLGNP KQPTNPFLEM
     IKFLLERIAP VHIDTESISA LIKQVNKSID GTADDEDEGV PTDQAIRAGL ELLKVLSFTH
     PISFHSAETF ESLLACLKMD DEKVAEAALQ IFKNTGSKIE EDFPHIRSAL LPVLHHKSKK
     GPPRQAKYAI HCIHAIFSSK ETQFAQIFEP LHKSLDPSNL EHLITPLVTI GHIALLAPDQ
     FAAPLKSLVA TFIVKDLLMN DRLPGKKTTK LWVPDEEVSP ETMVKIQAIK MMVRWLLGMK
     NNHSKSGTST LRLLTTILHS DGDLTEQGKI SKPDMSRLRL AAGSAIVKLA QEPCYHEIIT
     LEQYQLCALA INDECYQVRQ VFAQKLHKGL SRLRLPLEYM AICALCAKDP VKERRAHARQ
     CLVKNITVRR EYLKQHAAVS EKLLSLLPEY VVPYTIHLLA HDPDYVKVQD IEQLKDVKEC
     LWFVLEILMA KNENNSHAFI RKMVENIKQT KDAQGPDDTK MNEKLYTVCD VAMNIIMSKS
     TTYSLESPKD PVLPARFFTQ PDKNFSNTKN YLPPEMKSFF TPGKPKTANV LGAVNKPLSS
     AGKQSQTKSS RMETVSNASS SSNPSSPGRI KGRLDSSEMD HSENEDYTMS SPLPGKKSDK
     REDPDLSELE KPRSRKKAPV TDPEEKLGMD DLTKLVQEQK PKGSQRGRKR GRTASDSDEQ
     QWPEEKRHKE ELLENEDEQN SPPKKGKRGR PPKPLGGGTS KEEPTMKTSK KGNKKKLVPP
     VVDDDEEEER QIGNTEHKSK SKQHRTSKRA QQRAESPETS AVESTQSTPQ KGRGRPSKAP
     SPSQPPKKIR VGRSKQVATK ENDSSEEMDV LQASSPVSDD TTQEGAEEED ISVGNVRRRS
     SKRERR
//
ID   Q4VA57_MOUSE            Unreviewed;       854 AA.
AC   Q4VA57;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   30-NOV-2010, entry version 30.
DE   SubName: Full=Fry protein;
DE   Flags: Fragment;
GN   Name=Fry;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC096532; AAH96532.1; -; mRNA.
DR   IPI; IPI00850365; -.
DR   RefSeq; NP_766475.2; NM_172887.2.
DR   UniGene; Mm.216590; -.
DR   UniGene; Mm.412151; -.
DR   UniGene; Mm.454348; -.
DR   STRING; Q4VA57; -.
DR   Ensembl; ENSMUST00000087204; ENSMUSP00000084454; ENSMUSG00000056602.
DR   GeneID; 320365; -.
DR   KEGG; mmu:320365; -.
DR   CTD; 320365; -.
DR   MGI; MGI:2443895; Fry.
DR   HOVERGEN; HBG067116; -.
DR   InParanoid; Q4VA57; -.
DR   ArrayExpress; Q4VA57; -.
DR   Bgee; Q4VA57; -.
DR   Genevestigator; Q4VA57; -.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   854 AA;  95687 MW;  EA69D78222123700 CRC64;
     ERIAQVCLEE KNPKLSNLAH VMTLYKTHSY TRDCATWVNV VCRYLHEAYA DITLNMVTYL
     AELLEKGLPS MQQPLLQVIY SLLSYMDLSV VPVKQFNMEV LKTIEKYVQS IHWREALNIL
     KLVVSRSASL VLPSYQHSDL SKIELHRVWT SASKELPGKT LDFHFDISET PIIGRRYDEL
     QNSSGRDGKP RAMAVTRSAS STSSGSNSNV LVPVSWKRPQ YSQKRTKEKL VHVLSLCGQE
     VGLSKNPSVI FSSCGDLDLP EHQTSLVSSE DGPREQENMD DTNSEQQFRV FRDFDFLDVE
     LEDGEELQGE SMDNFNWGVR RRSLDSLDKC DMQILEERQL SRSTPSLNKM SHEDSDESSE
     EDLTASQILE HSDLIMNLSP SEEANPMELL TSACDSAPAD PHSFNTRMAN FEASLPDINN
     LQISEGSKAE AVPEEEDTTV HEDDLSSSIN ELPAAFECSD SFSLDMTEAE EKGNRGLDQY
     TLASFGEGDR GVSPPPSPFF SAILAAFQPA ACDDAEEAWR SHINQLMCDS DGSCAVYTFH
     VFSSLFKNIQ KRFCFLTCDA ASYLGDNLRG IGSKFVSSSQ MLTSCSECPT PFVDAETLLS
     CGLLDKLKFS VLELQEYLDT YNNRKEATLS WLANCKATFA GGSRDGVITC QPGDSEEKQM
     ESLAQLELCQ RLYKLHFQLL LLYQSYCKLI GQVHEVSSVP ELLNMSRELS DLKRNLKEAT
     AAIATDPLYI EGAWSEPTFT STEAAIQSML ECLKNNELGK ALRQIKECRS LWPNDIFGSS
     SDDEVQTLLN IYFRHQTLGQ TGTYALVGSN HSLTEICTKL MELNMEIRDM IRRAQNYRVL
     TAFLPDSSVS GTSL
//
ID   DSCL1_MOUSE             Reviewed;        2053 AA.
AC   Q4VA61;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   08-MAR-2011, entry version 43.
DE   RecName: Full=Down syndrome cell adhesion molecule-like protein 1 homolog;
DE   Flags: Precursor;
GN   Name=Dscaml1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 723-2053.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=19945391; DOI=10.1016/j.neuron.2009.09.027;
RA   Fuerst P.G., Bruce F., Tian M., Wei W., Elstrott J., Feller M.B.,
RA   Erskine L., Singer J.H., Burgess R.W.;
RT   "DSCAM and DSCAML1 function in self-avoidance in multiple cell types
RT   in the developing mouse retina.";
RL   Neuron 64:484-497(2009).
CC   -!- FUNCTION: Cell adhesion molecule that plays a role in neuronal
CC       self-avoidance. Promotes repulsion between specific neuronal
CC       processes of either the same cell or the same subtype of cells.
CC       Promotes both isoneuronal self-avoidance for creating an orderly
CC       neurite arborization in retinal rod bipolar cells and
CC       heteroneuronal self-avoidance to maintain mosaic spacing between
CC       AII amacrine cells.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- TISSUE SPECIFICITY: In the retina, expressed in the rod
CC       photoreceptors, AII amacrine cells and rod bipolar cells (at
CC       protein level).
CC   -!- DISRUPTION PHENOTYPE: The inner nuclear and inner plexiform layers
CC       in the retina are disorganised at postnatal day 20 (P20). AII
CC       amacrine cell populations are randomly distributed or pulled into
CC       clumps and rod bipolar show fasciculated dendrites.
CC   -!- SIMILARITY: Contains 6 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 10 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH96527.1; Type=Erroneous initiation;
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DR   EMBL; AC119237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC159893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC174644; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC126804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC096527; AAH96527.1; ALT_INIT; mRNA.
DR   IPI; IPI00762484; -.
DR   UniGene; Mm.325499; -.
DR   ProteinModelPortal; Q4VA61; -.
DR   SMR; Q4VA61; 23-1570.
DR   STRING; Q4VA61; -.
DR   Ensembl; ENSMUST00000034592; ENSMUSP00000034592; ENSMUSG00000032087.
DR   UCSC; uc009pga.1; mouse.
DR   MGI; MGI:2150309; Dscaml1.
DR   InParanoid; Q4VA61; -.
DR   OrthoDB; EOG40GCPX; -.
DR   ArrayExpress; Q4VA61; -.
DR   Bgee; Q4VA61; -.
DR   Genevestigator; Q4VA61; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070593; P:dendrite self-avoidance; IMP:UniProtKB.
DR   GO; GO:0007162; P:negative regulation of cell adhesion; IMP:UniProtKB.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 17.
DR   Pfam; PF00041; fn3; 6.
DR   Pfam; PF07679; I-set; 8.
DR   SMART; SM00060; FN3; 6.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 7.
DR   SUPFAM; SSF49265; FN_III-like; 6.
DR   PROSITE; PS50853; FN3; 6.
DR   PROSITE; PS50835; IG_LIKE; 9.
PE   1: Evidence at protein level;
KW   Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Neurogenesis; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     18       Potential.
FT   CHAIN        19   2053       Down syndrome cell adhesion molecule-like
FT                                protein 1 homolog.
FT                                /FTId=PRO_0000392480.
FT   TOPO_DOM     19   1591       Extracellular (Potential).
FT   TRANSMEM   1592   1612       Helical; (Potential).
FT   TOPO_DOM   1613   2053       Cytoplasmic (Potential).
FT   DOMAIN       19    119       Ig-like C2-type 1.
FT   DOMAIN      115    217       Ig-like C2-type 2.
FT   DOMAIN      226    310       Ig-like C2-type 3.
FT   DOMAIN      314    396       Ig-like C2-type 4.
FT   DOMAIN      408    501       Ig-like C2-type 5.
FT   DOMAIN      506    586       Ig-like C2-type 6.
FT   DOMAIN      596    685       Ig-like C2-type 7.
FT   DOMAIN      690    784       Ig-like C2-type 8.
FT   DOMAIN      788    885       Ig-like C2-type 9.
FT   DOMAIN      887    980       Fibronectin type-III 1.
FT   DOMAIN      986   1085       Fibronectin type-III 2.
FT   DOMAIN     1090   1186       Fibronectin type-III 3.
FT   DOMAIN     1191   1283       Fibronectin type-III 4.
FT   DOMAIN     1278   1377       Ig-like C2-type 10.
FT   DOMAIN     1380   1474       Fibronectin type-III 5.
FT   DOMAIN     1479   1569       Fibronectin type-III 6.
FT   COMPBIAS   1948   2016       Pro-rich.
FT   CARBOHYD     79     79       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    368    368       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    471    471       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    666    666       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    710    710       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    809    809       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1144   1144       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1162   1162       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1345   1345       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1561   1561       N-linked (GlcNAc...) (Potential).
FT   DISULFID     47    103       By similarity.
FT   DISULFID    146    198       By similarity.
FT   DISULFID    247    294       By similarity.
FT   DISULFID    336    386       By similarity.
FT   DISULFID    429    485       By similarity.
FT   DISULFID    526    575       By similarity.
FT   DISULFID    617    669       By similarity.
FT   DISULFID    711    767       By similarity.
FT   DISULFID    810    867       By similarity.
FT   DISULFID   1311   1363       By similarity.
SQ   SEQUENCE   2053 AA;  224240 MW;  0C0806C47D7ADCD6 CRC64;
     MWLVTFLLLL DSLHKARPED VGTSLYFVND SLQHVTFSSS VGVVVPCPAA GSPSAALRWY
     LATGDDIYDV PHIRHVHANG TLQLFPFSPS AFNSFIHDND YFCTAENAAG KIRSPNIRIK
     AVFREPYTVR VEDQRSMRGN VAVFKCLIPS SVQEYVSVVS WEKDTVSITP ENRFFITSHG
     GLYISDVQKE DALSTYRCIT QHKYSGETRQ SNGARLSVTD PAESIPTILD GFHSQEVWTG
     HSVELPCAAS GYPIPAIRWL KDGRPLPADS RWAKRITGLT ISDLRTEDSG TYICEVTNTF
     GSAEANGILT VIDPLHVTLT PKKLKTGIGS TVILSCALTG SPEFTIRWYR NTELVLPGEA
     ISIRGLSNET LLISSAQKSH SGAYQCFATR KAQTAQDFAI IVLEDGTPRI VSSFSEKVVN
     PGEQFSLMCA AKGAPPPTVT WALDDEPVVR DGSHRTNQYT MSDGTTISHM NVTGPQIRDG
     GVYRCTARNS VGSAEYQARI NVRGPPSIRA MRNITAVAGR DTLINCRVIG YPYYSIKWYK
     DALLLPDNHR QVVFENGTLK LTDVQKGMDE GEYLCSVLIQ PQLSISQSVH VAVKVPPLIQ
     PFEFPPASIG QLLYIPCVVS SGDMPIRITW RKDGQVIISG SGVTIESKEF MSSLQISSVS
     LKHNGNYTCI ASNAAATVSR ERQLIVRVPP RFVVQPNNQD GIYGKAGVLN CSVDGYPPPK
     VMWKHAKGSG NPQQYHPVPL TGRIQILPNS SLLIRHVLEE DIGYYLCQAS NGVGTDISKA
     MFLTVKIPAM ITSHPNTTIA IKGHPKELNC TARGERPIII RWEKGDTVID PDRVMRYAIA
     TKDNGDEVVS TLKLKPADRG DSVFFSCHAI NSYGEDRGLI QLTVQEPPDP PELEIREVKA
     RSMNLRWTQR FDGNSIITGF DIEYKNKSDS WDFKQSTRNI SPTINQANIV DLHPASVYSI
     RMYSFNKIGR SEPSKELTIS TEEAAPDGPP MDVTLQPVTS QSIQVTWKAP KKELQNGVIR
     GYQIGYRENS PGSNGQYSIV EMKATGDSEV YTLDNLKKFA QYGVVVQAFN RAGTGPSSSE
     INATTLEDVP SQPPENVRAL SITSDVAVIS WSEPPRSTLN GVLKGYRVIF WSLYVDGEWG
     EMQNVTTTRE RVELRGMEKF TNYSVQVLAY TQAGDGVRSS VLYIQTKEDV PGPPAGIKAV
     PSSASSVVVS WLPPTKPNGV IRKYTIFCSS PGSGQPAPSE YETSPEQLFY RIAHLNRGQQ
     YLLWVAAVTS AGRGNSSEKV TIEPAGKAPA KIISFGGTVT TPWMKDVRLP CNSVGDPAPA
     VKWTKDSEDS AIPVSLDGHR LIHTNGTLLL RAVKAEDSGY YTCTATNTGG FDTIIVNLLV
     QVPPDQPRLT VSKTSASSIT LTWIPGDNGG SSIRGFVLQY SVDNSEEWKD VFISSSERSF
     KLDSLKCGTW YKVKLAAKNS VGSGRISEII EAKTHGREPS FSKDQHLFTH INSTHARLNL
     QGWNNGGCPI TAIVLEYRPK GTWAWQGVRA NSSTEVFLTE LREATWYELR MRACNSAGCG
     NETAQFATLD YDGSTIPPIK SAQGEGDDVK KLFTIGCPVI LATLGVALLF VVRKKRKEKR
     LKRLRDAKSL AEMLISKNNR SFDTPVKGPP QGPRLHIDIP RVQLLIEDKE GIKQLGDDKA
     TIPVTDAEFS QAVNPQSFCT GVSLHHPALI QSTGPLIDMS DIRPGTNPVS RKNVKSAHST
     RNRYSSQWTL TKCQASTPAR TLTSDWRTVG SQHGVTVTES DSYSASLSQD TDKGRNSMVS
     TESASSTYEE LARAYEHAKL EEQLQHAKFE ITECFISDSS SDQMTTGTNE NADSMTSMST
     PSEPGICRFT ASPPKPQDAD RGKNVAVPIP HRANKSDYCN LPLYTKSEAF FRKADGREPC
     PVVPPREASM RNLTRAYHTQ ARHLTLDPAS KPLGLPHPGA TAATATATLP QRTLAMPAPP
     AGTAPPAPGP TPSEPSAAPS AAPPAPSTEP PRAGGPHTKM GGSRDSLLEM STPGVGRSQK
     QGAGAYSKSY TLV
//
ID   Q4VA93_MOUSE            Unreviewed;       672 AA.
AC   Q4VA93;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   SubName: Full=Prkca protein;
DE   SubName: Full=Protein kinase C, alpha;
GN   Name=Prkca; ORFNames=RP23-145G23.2-001, mCG_140727;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C3H/He mice; TISSUE=Osteoblast;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RA   Brown A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RA   Holt K.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RA   Hall R.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [11]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [12]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [13]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [14]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [15]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC096493; AAH96493.1; -; mRNA.
DR   EMBL; AK147084; BAE27664.1; -; mRNA.
DR   EMBL; AL645535; CAM15234.1; -; Genomic_DNA.
DR   EMBL; AL607041; CAM15234.1; JOINED; Genomic_DNA.
DR   EMBL; AL645963; CAM15234.1; JOINED; Genomic_DNA.
DR   EMBL; AL607041; CAM24252.1; -; Genomic_DNA.
DR   EMBL; AL645535; CAM24252.1; JOINED; Genomic_DNA.
DR   EMBL; AL645963; CAM24252.1; JOINED; Genomic_DNA.
DR   EMBL; AL645963; CAM26857.1; -; Genomic_DNA.
DR   EMBL; AL607041; CAM26857.1; JOINED; Genomic_DNA.
DR   EMBL; AL645535; CAM26857.1; JOINED; Genomic_DNA.
DR   EMBL; CH466558; EDL34340.1; -; Genomic_DNA.
DR   IPI; IPI00884460; -.
DR   RefSeq; NP_035231.2; NM_011101.3.
DR   UniGene; Mm.222178; -.
DR   ProteinModelPortal; Q4VA93; -.
DR   SMR; Q4VA93; 37-292, 336-666.
DR   STRING; Q4VA93; -.
DR   PRIDE; Q4VA93; -.
DR   Ensembl; ENSMUST00000059595; ENSMUSP00000062392; ENSMUSG00000050965.
DR   GeneID; 18750; -.
DR   KEGG; mmu:18750; -.
DR   UCSC; uc007mbe.1; mouse.
DR   CTD; 18750; -.
DR   MGI; MGI:97595; Prkca.
DR   HOVERGEN; HBG108317; -.
DR   InParanoid; Q4VA93; -.
DR   OMA; INITPEY; -.
DR   PhylomeDB; Q4VA93; -.
DR   NextBio; 294917; -.
DR   PMAP-CutDB; Q4VA93; -.
DR   ArrayExpress; Q4VA93; -.
DR   Bgee; Q4VA93; -.
DR   Genevestigator; Q4VA93; -.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004698; F:calcium-dependent protein kinase C activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
DR   GO; GO:0002062; P:chondrocyte differentiation; IDA:MGI.
DR   GO; GO:0000188; P:inactivation of MAPK activity; IMP:MGI.
DR   GO; GO:0008629; P:induction of apoptosis by intracellular signals; IMP:MGI.
DR   GO; GO:0050930; P:induction of positive chemotaxis; IMP:MGI.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IGI:MGI.
DR   GO; GO:0046325; P:negative regulation of glucose import; IMP:MGI.
DR   GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IMP:MGI.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:MGI.
DR   GO; GO:0030593; P:neutrophil chemotaxis; IMP:MGI.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; IMP:MGI.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:MGI.
DR   GO; GO:0006937; P:regulation of muscle contraction; IMP:MGI.
DR   GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
DR   GO; GO:0002026; P:regulation of the force of heart contraction; IMP:MGI.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR014375; Protein_kinase_C_a/b/g.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   PIRSF; PIRSF000550; PKC_alpha; 1.
DR   PRINTS; PR00360; C2DOMAIN.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Metal-binding; Nucleotide-binding; Repeat;
KW   Serine/threonine-protein kinase; Transferase; Zinc.
SQ   SEQUENCE   672 AA;  76824 MW;  948E297ADEC39012 CRC64;
     MADVYPANDS TASQDVANRF ARKGALRQKN VHEVKDHKFI ARFFKQPTFC SHCTDFIWGF
     GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPDTDDPRS KHKFKIHTYG SPTFCDHCGS
     LLYGLIHQGM KCDTCDMNVH KQCVINVPSL CGMDHTEKRG RIYLKAEVTD EKLHVTVRDA
     KNLIPMDPNG LSDPYVKLKL IPDPKNESKQ KTKTIRSTLN PQWNESFTFK LKPSDKDRRL
     SVEIWDWDRT TRNDFMGSLS FGVSELMKMP ASGWYKLLNQ EEGEYYNVPI PEGDEEGNME
     LRQKFEKAKL GPAGNKVISP SEDRKQPSNN LDRVKLTDFN FLMVLGKGSF GKVMLADRKG
     TEELYAIKIL KKDVVIQDDD VECTMVEKRV LALLDKPPFL TQLHSCFQTV DRLYFVMEYV
     NGGDLMYHIQ QVGKFKEPQA VFYAAEISIG LFFLHKRGII YRDLKLDNVM LDSEGHIKIA
     DFGMCKEHMM DGVTTRTFCG TPDYIAPEII AYQPYGKSVD WWAYGVLLYE MLAGQPPFDG
     EDEDELFQSI MEHNVSYPKS LSKEAVSICK GLMTKHPAKR LGCGPEGERD VREHAFFRRI
     DWEKLENREI QPPFKPKVCG KGAENFDKFF TRGQPVLTPP DQLVIANIDQ SDFEGFSYVN
     PQFVHPILQS AV
//
ID   Q4VA98_MOUSE            Unreviewed;       681 AA.
AC   Q4VA98;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   SubName: Full=Zfp219 protein;
DE   SubName: Full=Zinc finger protein 219, isoform CRA_b;
GN   Name=Zfp219; ORFNames=mCG_18709;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor. C3;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC096486; AAH96486.1; -; mRNA.
DR   EMBL; CH466659; EDL42266.1; -; Genomic_DNA.
DR   IPI; IPI00469594; -.
DR   UniGene; Mm.475652; -.
DR   ProteinModelPortal; Q4VA98; -.
DR   STRING; Q4VA98; -.
DR   Ensembl; ENSMUST00000067549; ENSMUSP00000068184; ENSMUSG00000049295.
DR   UCSC; uc007tnv.1; mouse.
DR   MGI; MGI:1917140; Zfp219.
DR   eggNOG; roNOG10869; -.
DR   HOVERGEN; HBG054187; -.
DR   InParanoid; Q4VA98; -.
DR   OrthoDB; EOG45B1FZ; -.
DR   ArrayExpress; Q4VA98; -.
DR   Bgee; Q4VA98; -.
DR   Genevestigator; Q4VA98; -.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 6.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   681 AA;  73227 MW;  1F800A4242213E13 CRC64;
     MGAVGWSETR AGERRFPCPV CGKRFRFNSI LALHLRAHPG AQAFQCPHCG HRAAQRALLR
     SHLRTHQPER PRSPAARLLL ELEERALLRE ARLGRARSSG GMQSSPAAEG LARPQVPSSS
     AFRCPFCKGK FRTSAERERH LHILHRPWKC SLCSFGSSQE EELLHHSLTA HGASERPLAA
     TSTPEPPPPP QQEPRSALEP EPEPEPRPEP DREANPAPTP APPEEPPAPP EFRCQVCGQS
     FTQSWFLKGH MRKHKASFDH ACPVCGRCFK EPWFLKNHMK VHTSKLGPLR APGPGSAPAR
     APQPPDLSLL AYEPLGPALL LAPAPAPAER REPPSLLGYL SVRAGEVRPN GEGADPGGGR
     SYGGFRPLPS ALPNRARRHR TEEPEEEEEV VEAEEESWAR GRSLGSLTSL HPNPGEGSGQ
     PAPAAGTQAR STATQEENGL LVGGTRSEAG RGATGKDCPF CGKSFRSAHH LKVHLRVHTG
     ERPYKCPHCD YAGTQSGSLK YHLQRHHREQ RSSAGPGPPP EPPPPSQRGS LQPQSGAKPT
     QASATWVEGT ASTRPPSSST GPGSRRKPAS PGRTLRNGRG GEAEPLDLSL RAGPGGEAGA
     GGALHRCLFC PFATGAPELM ALHLQVHHSR RARGRRQPRA DTSPTYVRAP SGETPPSPPL
     EEEGSPGLSR SGEAGLGGQE R
//
ID   TAPT1_MOUSE             Reviewed;         564 AA.
AC   Q4VBD2; Q8CDI4;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 2.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=Transmembrane anterior posterior transformation protein 1;
GN   Name=Tapt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 174-564.
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 254-564.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=17151244; DOI=10.1534/genetics.106.065177;
RA   Howell G.R., Shindo M., Murray S., Gridley T., Wilson L.A.,
RA   Schimenti J.C.;
RT   "Mutation of a ubiquitously expressed mouse transmembrane protein
RT   (Tapt1) causes specific skeletal homeotic transformations.";
RL   Genetics 175:699-707(2007).
CC   -!- FUNCTION: May act as a downstream effector of Hoxc8 possibly by
CC       transducing or transmitting extracellular information required for
CC       axial skeletal patterning during development.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Expressed throughout embryo.
CC   -!- DISRUPTION PHENOTYPE: Mice die during perinatal development and
CC       are the cause of the L5Jcs1 phenotype. They exhibit posterior-to-
CC       anterior transformations of the vertebral column midsection,
CC       similar to mice deficient for Hoxc8 and Hoxc9.
CC   -!- SIMILARITY: Belongs to the TAPT1 family.
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DR   EMBL; AC103621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC096038; AAH96038.1; -; mRNA.
DR   EMBL; AK030002; BAC26728.1; -; mRNA.
DR   IPI; IPI00270496; -.
DR   RefSeq; NP_776125.2; NM_173764.3.
DR   UniGene; Mm.30688; -.
DR   ProteinModelPortal; Q4VBD2; -.
DR   STRING; Q4VBD2; -.
DR   PhosphoSite; Q4VBD2; -.
DR   PRIDE; Q4VBD2; -.
DR   Ensembl; ENSMUST00000055128; ENSMUSP00000062110; ENSMUSG00000046985.
DR   GeneID; 231225; -.
DR   KEGG; mmu:231225; -.
DR   CTD; 231225; -.
DR   MGI; MGI:2683537; Tapt1.
DR   eggNOG; roNOG04389; -.
DR   GeneTree; ENSGT00390000010628; -.
DR   HOGENOM; HBG444221; -.
DR   HOVERGEN; HBG108546; -.
DR   InParanoid; Q4VBD2; -.
DR   OMA; TLGFYES; -.
DR   OrthoDB; EOG4WM4TM; -.
DR   NextBio; 380461; -.
DR   ArrayExpress; Q4VBD2; -.
DR   Bgee; Q4VBD2; -.
DR   Genevestigator; Q4VBD2; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048706; P:embryonic skeletal system development; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   InterPro; IPR008010; Membrane_Tatp1/CMV_rcpt.
DR   PANTHER; PTHR13317; DUF747_CMV_rcpt; 1.
DR   Pfam; PF05346; DUF747; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Developmental protein; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    564       Transmembrane anterior posterior
FT                                transformation protein 1.
FT                                /FTId=PRO_0000328873.
FT   TRANSMEM    108    128       Helical; (Potential).
FT   TRANSMEM    154    176       Helical; (Potential).
FT   TRANSMEM    233    253       Helical; (Potential).
FT   TRANSMEM    332    352       Helical; (Potential).
FT   TRANSMEM    400    420       Helical; (Potential).
FT   TRANSMEM    429    449       Helical; (Potential).
FT   COMPBIAS     11     38       Gly-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
SQ   SEQUENCE   564 AA;  63894 MW;  97D28BC7970C61C2 CRC64;
     MAGVCDAAAP GEGGGGGADG PERTGRGEAE QPGGGGHGPA PQHTETLGFY ESDRRREKRR
     GRAELSLLRF LSAELTRGYF LEHNEAKYTE RRERVYTCMR IPRELEKLMF FGIFLCLDAF
     LYVFTLLPLR VFLALFRLLT LPCYGLRDRR LLQPAQVCDI LKGVILVICY FMMHYVDYSM
     MYHLIRGQSV IKLYIIYNML EVADRLFSSF GQDILDALYW TATEPKERKR AHIGVIPHFF
     MAVLYVFLHA ILIMVQATTL NVAFNSHNKS LLTIMMSNNF VEIKGSVFKK FEKNNLFQMS
     NSDIKERFTN YVLLLIVCLR NMEQFSWNPD HLWVLFPDVC MVIASEIAVD IVKHAFITKF
     NDITADVYSE YRASLAFDLV SSRQKNAYTD YSDSVARRMG FIPLPLAVLL IRVVTSSIKV
     QGILSYACVI LFYFGLISLK ILNSIVLLGK SCQYVKEAKM EEKLFNPPPA STPGKPSSKS
     QSKGKPSQGL STEENLSASV TSQPGHQKEN VIPLLVTSNS DQFLTTPDGD EKDITQENSE
     LKHRSSKKDL LEIDRFTICG NRID
//
ID   PHAR4_MOUSE             Reviewed;         694 AA.
AC   Q501J7; A2ALG0; Q5DTM4; Q6DI97; Q8C7U9;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 40.
DE   RecName: Full=Phosphatase and actin regulator 4;
GN   Name=Phactr4; Synonyms=Kiaa4120;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SUBUNIT: Binds PPP1CA and actin (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q501J7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q501J7-2; Sequence=VSP_025440;
CC       Name=3;
CC         IsoId=Q501J7-3; Sequence=VSP_025439;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the phosphatase and actin regulator family.
CC   -!- SIMILARITY: Contains 3 RPEL repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90294.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK049209; BAC33611.1; -; mRNA.
DR   EMBL; AK220496; BAD90294.1; ALT_INIT; mRNA.
DR   EMBL; AL805897; CAM26521.1; -; Genomic_DNA.
DR   EMBL; AL805897; CAM26523.1; -; Genomic_DNA.
DR   EMBL; BC075672; AAH75672.1; -; mRNA.
DR   EMBL; BC096033; AAH96033.1; -; mRNA.
DR   IPI; IPI00400381; -.
DR   IPI; IPI00625118; -.
DR   IPI; IPI00648030; -.
DR   RefSeq; NP_001155269.1; NM_001161797.1.
DR   RefSeq; NP_780515.2; NM_175306.4.
DR   UniGene; Mm.158361; -.
DR   PhosphoSite; Q501J7; -.
DR   PRIDE; Q501J7; -.
DR   Ensembl; ENSMUST00000084170; ENSMUSP00000081185; ENSMUSG00000066043.
DR   Ensembl; ENSMUST00000084249; ENSMUSP00000081270; ENSMUSG00000066043.
DR   Ensembl; ENSMUST00000102568; ENSMUSP00000099628; ENSMUSG00000066043.
DR   GeneID; 100169; -.
DR   KEGG; mmu:100169; -.
DR   CTD; 100169; -.
DR   MGI; MGI:2140327; Phactr4.
DR   GeneTree; ENSGT00390000004420; -.
DR   HOVERGEN; HBG108247; -.
DR   OMA; HRPSEPE; -.
DR   OrthoDB; EOG4PNXH9; -.
DR   NextBio; 354299; -.
DR   ArrayExpress; Q501J7; -.
DR   Bgee; Q501J7; -.
DR   CleanEx; MM_PHACTR4; -.
DR   Genevestigator; Q501J7; -.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004018; RPEL_repeat.
DR   Pfam; PF02755; RPEL; 3.
DR   SMART; SM00707; RPEL; 3.
DR   PROSITE; PS51073; RPEL; 3.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Phosphoprotein;
KW   Protein phosphatase inhibitor; Repeat.
FT   CHAIN         1    694       Phosphatase and actin regulator 4.
FT                                /FTId=PRO_0000287307.
FT   REPEAT       63     88       RPEL 1.
FT   REPEAT      575    600       RPEL 2.
FT   REPEAT      613    638       RPEL 3.
FT   COMPBIAS    221    355       Pro-rich.
FT   COMPBIAS    368    371       Poly-Ser.
FT   COMPBIAS    471    474       Poly-Glu.
FT   COMPBIAS    519    523       Poly-Asp.
FT   MOD_RES     118    118       Phosphoserine.
FT   MOD_RES     129    129       Phosphoserine (By similarity).
FT   MOD_RES     145    145       Phosphoserine (By similarity).
FT   MOD_RES     148    148       Phosphoserine (By similarity).
FT   MOD_RES     335    335       Phosphoserine (By similarity).
FT   MOD_RES     337    337       Phosphoserine (By similarity).
FT   MOD_RES     420    420       Phosphoserine (By similarity).
FT   MOD_RES     425    425       Phosphothreonine (By similarity).
FT   MOD_RES     436    436       Phosphoserine (By similarity).
FT   MOD_RES     549    549       Phosphoserine (By similarity).
FT   MOD_RES     620    620       Phosphoserine (By similarity).
FT   VAR_SEQ       1      5       MEDPS -> MGQADVSRPVNPDAV (in isoform 3).
FT                                /FTId=VSP_025439.
FT   VAR_SEQ      64     90       Missing (in isoform 2).
FT                                /FTId=VSP_025440.
FT   CONFLICT    212    212       T -> K (in Ref. 1; BAC33611).
FT   CONFLICT    224    224       A -> S (in Ref. 3; AAH96033).
SQ   SEQUENCE   694 AA;  76632 MW;  3AEB17E6A390DD29 CRC64;
     MEDPSEEAEQ PSGDPGMGMD SVEAGDTTPP TKRKSKFSAL GKIFKPWKWR KKKSSDKFKE
     TSEVLERKIS MRKPREELVK RGVLLEDPEQ DGEDSGKLSH AALKNGHTTP IGSARSSSPV
     LVEEEPERSL RNLTPEEESK KRLGSTGSQP NSEAEPGPEH APKQPLLPPK RPLSSSCEAK
     EVPAGSTARS VSSTSGSTTV TSAATTAATD MTKTVKSFVG PTPAPAPAPR TLPAAPASAN
     TAATTTAPAK QPPIPPPKPA QRNSNPIIAE LSQAMNSGTV LSKPSPPLPP KRGIPSTSIP
     SLEPAASFTT KTANDQREKT VSLCLEPPLI IPPSSPSPPL PTHIPPEPPR SPLVPAKTFQ
     IVPEVEFSSS SDLFQDISQQ EDQKTEVPKK IQDQSFGESH IPSRLPPLPL HIRIQQALTS
     PLPVTPPLEG THRAHSLLFE NSDSFSEDTG TLGRTRSLPI TIEMLKVPDD EEEEQTCPFV
     EDVTSTSATP SLPLCLREEE KESDSDSEGP IKYRDEEEDD DDDESHQSAL ANRVKRKDTL
     AMKLSSRPSE PETNLNSWPR KSKEEWNEIR HQIGNTLIRR LSQRPTAEEL EQRNILQPKN
     EADRQAEKRE IKRRLTRKLS QRPTVAELLA RKILRFNEYV EVTDAHDYDR RADKPWTKLT
     PADKAAIRKE LNEFKSSEME VHVDSKHFTR YHRP
//
ID   RAB26_MOUSE             Reviewed;         260 AA.
AC   Q504M8;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   08-FEB-2011, entry version 55.
DE   RecName: Full=Ras-related protein Rab-26;
GN   Name=Rab26;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Participates in exocrine secretion: regulates the
CC       secretion of acinar granules in the parotid gland (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (By similarity).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR   EMBL; BC094931; AAH94931.1; -; mRNA.
DR   IPI; IPI00671283; -.
DR   RefSeq; NP_796349.1; NM_177375.1.
DR   UniGene; Mm.266033; -.
DR   ProteinModelPortal; Q504M8; -.
DR   SMR; Q504M8; 62-258.
DR   STRING; Q504M8; -.
DR   PRIDE; Q504M8; -.
DR   Ensembl; ENSMUST00000035797; ENSMUSP00000046089; ENSMUSG00000079657.
DR   GeneID; 328778; -.
DR   KEGG; mmu:328778; -.
DR   UCSC; uc008awu.1; mouse.
DR   CTD; 328778; -.
DR   MGI; MGI:2443284; Rab26.
DR   GeneTree; ENSGT00600000084225; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; Q504M8; -.
DR   OMA; HERVVKR; -.
DR   PhylomeDB; Q504M8; -.
DR   NextBio; 398424; -.
DR   ArrayExpress; Q504M8; -.
DR   Bgee; Q504M8; -.
DR   CleanEx; MM_RAB26; -.
DR   Genevestigator; Q504M8; -.
DR   GermOnline; ENSMUSG00000052752; Mus musculus.
DR   GO; GO:0031226; C:intrinsic to plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0035272; P:exocrine system development; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0017157; P:regulation of exocytosis; ISS:UniProtKB.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; GTP-binding; Lipoprotein; Membrane; Nucleotide-binding;
KW   Prenylation; Protein transport; Transport.
FT   CHAIN         1    260       Ras-related protein Rab-26.
FT                                /FTId=PRO_0000121219.
FT   NP_BIND      74     82       GTP (By similarity).
FT   NP_BIND     123    127       GTP (By similarity).
FT   NP_BIND     181    184       GTP (By similarity).
FT   NP_BIND     211    213       GTP (By similarity).
FT   MOTIF        97    105       Effector region (By similarity).
FT   LIPID       257    257       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   LIPID       258    258       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   260 AA;  28619 MW;  3657E725B1D004E8 CRC64;
     MSRKKTPKSK GGSEPATSTL PAAAAATNGP RLAHPRTVRP GPEAPPNGPP QSIRPSLGST
     GDFYDVAFKV MLVGDSGVGK TCLLVRFKDG AFLAGTFIST VGIDFRNKVL DVDGMKVKLQ
     IWDTAGQERF RSVTHAYYRD AHALLLLYDI TNKDSFDNIQ AWLTEIQEYA QQDVVLMLLG
     NKVDSTQDRV VKREDGEKLA KEYGLPFMET SARTGLNVDL AFTAIAKELK QRSAKAPSEP
     RFRLHDYVKR EGRGVSCCRL
//
ID   ANR28_MOUSE             Reviewed;        1053 AA.
AC   Q505D1;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A;
DE            Short=PP6-ARS-A;
DE            Short=Serine/threonine-protein phosphatase 6 regulatory subunit ARS-A;
DE   AltName: Full=Ankyrin repeat domain-containing protein 28;
DE   AltName: Full=Phosphatase interactor targeting protein hnRNP K;
DE            Short=PITK;
GN   Name=Ankrd28;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=16564677; DOI=10.1016/j.cellsig.2006.01.019;
RA   Kwiek N.C., Thacker D.F., Datto M.B., Megosh H.B., Haystead T.A.J.;
RT   "PITK, a PP1 targeting subunit that modulates the phosphorylation of
RT   the transcriptional regulator hnRNP K.";
RL   Cell. Signal. 18:1769-1778(2006).
CC   -!- FUNCTION: Putative regulatory subunit of protein phospatase 6
CC       (PP6) that may be involved in the recognition of phosphoprotein
CC       substrates. Involved in the PP6-mediated dephosphorylation of
CC       NFKBIE opposing its degradation in response to TNF-alpha.
CC       Selectively inhibits the phosphatase activity of PPP1C. Targets
CC       PPP1C to modulate HNRPK phosphorylation (By similarity).
CC   -!- SUBUNIT: Protein phospatase 6 (PP6) holoenzyme is proposed to be a
CC       heterotrimeric complex formed by the catalytic subunit, a SAPS
CC       domain-containing subunit (PP6R) and an ankyrin repeat-domain
CC       containing regulatory subunit (ARS). Interacts with PPP1C and
CC       HNRPK. Interacts with PPP6C, PPP6R1 and PPP6R3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Note=Seems to be
CC       excluded from nucleoli (By similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed (at protein level).
CC   -!- SIMILARITY: Contains 27 ANK repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC094609; AAH94609.1; -; mRNA.
DR   EMBL; BC051456; AAH51456.1; -; mRNA.
DR   IPI; IPI00405443; -.
DR   RefSeq; NP_001019775.1; NM_001024604.2.
DR   UniGene; Mm.37660; -.
DR   ProteinModelPortal; Q505D1; -.
DR   SMR; Q505D1; 8-1036.
DR   STRING; Q505D1; -.
DR   PhosphoSite; Q505D1; -.
DR   PRIDE; Q505D1; -.
DR   Ensembl; ENSMUST00000014640; ENSMUSP00000014640; ENSMUSG00000014496.
DR   GeneID; 105522; -.
DR   KEGG; mmu:105522; -.
DR   UCSC; uc007sya.1; mouse.
DR   CTD; 105522; -.
DR   MGI; MGI:2145661; Ankrd28.
DR   eggNOG; roNOG10296; -.
DR   HOGENOM; HBG443784; -.
DR   HOVERGEN; HBG067697; -.
DR   InParanoid; Q505D1; -.
DR   OMA; DMLNDSD; -.
DR   OrthoDB; EOG4NCMCR; -.
DR   PhylomeDB; Q505D1; -.
DR   NextBio; 357754; -.
DR   ArrayExpress; Q505D1; -.
DR   Bgee; Q505D1; -.
DR   CleanEx; MM_ANKRD28; -.
DR   Genevestigator; Q505D1; -.
DR   GermOnline; ENSMUSG00000014496; Mus musculus.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 4.
DR   Pfam; PF00023; Ank; 18.
DR   SMART; SM00248; ANK; 28.
DR   SUPFAM; SSF48403; ANK; 3.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 24.
PE   1: Evidence at protein level;
KW   Acetylation; ANK repeat; Nucleus; Phosphoprotein; Repeat.
FT   CHAIN         1   1053       Serine/threonine-protein phosphatase 6
FT                                regulatory ankyrin repeat subunit A.
FT                                /FTId=PRO_0000244571.
FT   REPEAT       40     69       ANK 1.
FT   REPEAT       73    102       ANK 2.
FT   REPEAT      106    135       ANK 3.
FT   REPEAT      139    168       ANK 4.
FT   REPEAT      172    201       ANK 5.
FT   REPEAT      205    234       ANK 6.
FT   REPEAT      238    267       ANK 7.
FT   REPEAT      271    301       ANK 8.
FT   REPEAT      305    334       ANK 9.
FT   REPEAT      338    367       ANK 10.
FT   REPEAT      371    400       ANK 11.
FT   REPEAT      404    433       ANK 12.
FT   REPEAT      437    466       ANK 13.
FT   REPEAT      470    500       ANK 14.
FT   REPEAT      504    534       ANK 15.
FT   REPEAT      549    578       ANK 16.
FT   REPEAT      582    611       ANK 17.
FT   REPEAT      616    645       ANK 18.
FT   REPEAT      652    681       ANK 19.
FT   REPEAT      685    714       ANK 20.
FT   REPEAT      718    747       ANK 21.
FT   REPEAT      755    786       ANK 22.
FT   REPEAT      788    817       ANK 23.
FT   REPEAT      822    851       ANK 24.
FT   REPEAT      855    885       ANK 25.
FT   REPEAT      889    918       ANK 26.
FT   REPEAT      925    954       ANK 27.
FT   COMPBIAS    987    990       Poly-Ser.
FT   MOD_RES      73     73       N6-acetyllysine (By similarity).
FT   MOD_RES      84     84       Phosphoserine.
FT   MOD_RES    1007   1007       Phosphoserine (By similarity).
FT   MOD_RES    1011   1011       Phosphoserine (By similarity).
SQ   SEQUENCE   1053 AA;  112898 MW;  D7649AF1D1F22F62 CRC64;
     MAFLKLRDQP SLVQAIFNGD PDEVRALIFK KEDVNFQDNE KRTPLHAAAY LGDAEIIELL
     ILSGARVNAK DSKWLTPLHR AVASCSEEAV QILLKHSADV NARDKNWQTP LHIAAANKAV
     KCAESLVPLL SNVNVSDRAG RTALHHAAFS GHGEMVKLLL SRGANINAFD KKDRRAIHWA
     AYMGHIEVVK LLVSHGAEVT CKDKKSYTPL HAAASSGMIS VVKYLLDLGV DMNEPNAYGN
     TPLHVACYNG QDVVVNELID CGANVNQKNE KGFTPLHFAA ASTHGALCLE LLVGNGADVN
     MKSKDGKTPL HMTALHGRFS RSQTIIQSGA VIDCEDKNGN TPLHIAARYG HELLINTLIT
     SGADTAKRGI HGMFPLHLAA LSGFSDCCRK LLSSGFDIDT PDDFGRTCLH AAAAGGNLEC
     LNLLLNTGAD FNKKDKFGRS PLHYAAANCN YQCLFALVGS GASVNDLDER GCTPLHYAAT
     SDTDGKCLEY LLRNDANPGI RDKQGYNAVH YSAAYGHRLC LQLIASETPL DVLMETSGTD
     MLSDSDNRAT ISPLHLAAYH GHHQALEVLV QSLLDLDVRN SSGRTPLDLA AFKGHVECVD
     VLINQGASIL VKDYVLKRTP IHAAATNGHS ECLRLLIGNA EPQNAVDIQD GNGQTPLMLS
     VLNGHTDCVY SLLNKGANVD AKDKWGRTAL HRGAVTGHEE CVDALLQHGA KCLLRDSRGR
     TPIHLSAACG HIGVLGALLQ SATSVDANPA VVDNHGYTAL HWACYNGHET CVELLLEQDV
     FQKIDGNAFS PLHCAVINDN EGAAEMLIDS LGASIVNATD SKGRTPLHAA AFTDHVECLQ
     LLLSQNAQVN SADSTGKTPL MMAAENGQTN TVEMLVSSAS ADLTLQDKSK NTALHLACGK
     GHETSALLIL EKITDRNLIN ATNAALQTPL HVAARNGLTM VVQELLGKGA SVLAVDENGY
     TPALACAPNK DVADCLALIL ATMMPVSSSS PLTSLTFNAI NRYTNTSKTV SFEALPIMRN
     EASSYCSFNN IGGEQEYLYT DVDELNDSDS ETY
//
ID   TRI67_MOUSE             Reviewed;         768 AA.
AC   Q505D9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Tripartite motif-containing protein 67;
GN   Name=Trim67;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity). Note=Microtubule-associated (By
CC       similarity).
CC   -!- SIMILARITY: Contains 2 B box-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 B30.2/SPRY domain.
CC   -!- SIMILARITY: Contains 1 COS domain.
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC094596; AAH94596.1; -; mRNA.
DR   IPI; IPI00944093; -.
DR   RefSeq; NP_941034.2; NM_198632.2.
DR   UniGene; Mm.422769; -.
DR   HSSP; Q9C026; 2DB8.
DR   ProteinModelPortal; Q505D9; -.
DR   SMR; Q505D9; 1-35, 192-341, 497-591.
DR   STRING; Q505D9; -.
DR   PRIDE; Q505D9; -.
DR   Ensembl; ENSMUST00000041106; ENSMUSP00000040601; ENSMUSG00000036913.
DR   GeneID; 330863; -.
DR   KEGG; mmu:330863; -.
DR   CTD; 330863; -.
DR   MGI; MGI:3045323; Trim67.
DR   eggNOG; roNOG04384; -.
DR   GeneTree; ENSGT00560000076722; -.
DR   HOGENOM; HBG403027; -.
DR   HOVERGEN; HBG062305; -.
DR   InParanoid; Q505D9; -.
DR   OMA; ATLCEQC; -.
DR   OrthoDB; EOG46HG97; -.
DR   ArrayExpress; Q505D9; -.
DR   Bgee; Q505D9; -.
DR   CleanEx; MM_TRIM67; -.
DR   Genevestigator; Q505D9; -.
DR   GermOnline; ENSMUSG00000036913; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001870; B302/SPRY.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR017903; COS_domain.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003877; SPRY_rcpt.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 2.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 2.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
DR   SUPFAM; SSF49265; FN_III-like; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS51262; COS; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50119; ZF_BBOX; 2.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Metal-binding; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    768       Tripartite motif-containing protein 67.
FT                                /FTId=PRO_0000256865.
FT   DOMAIN      435    493       COS.
FT   DOMAIN      498    589       Fibronectin type-III.
FT   DOMAIN      574    765       B30.2/SPRY.
FT   ZN_FING       7     42       RING-type; degenerate.
FT   ZN_FING     201    248       B box-type 1; degenerate.
FT   ZN_FING     285    327       B box-type 2.
FT   COILED      332    369       Potential.
FT   COMPBIAS     55     59       Poly-Ala.
FT   COMPBIAS    134    137       Poly-Ala.
FT   COMPBIAS    147    151       Poly-Ser.
FT   COMPBIAS    194    201       Poly-Ala.
SQ   SEQUENCE   768 AA;  82760 MW;  5C59C4A62A79C436 CRC64;
     MEEELKCPVC GSLFREPIIL PCSHNVCLPC ARTIAVQTPD GEQHLPPPLL LSRGAAAAAT
     PPDQDAAAGA TSGGAGANTA GGLGGGATGG GDHADKLSLY SETDSGYGSY TPSLKSPNGV
     RVLPMVPAPP GSSAAAARGA ACSSLCSSSS SITCPQCHRS ASLDHRGLRG FQRNRLLEGI
     VQRYQQGRGV VPGAAAAPAV AICQLCDRTP PEPAATLCEQ CDVLYCATCQ LKCHPSRGPF
     AKHRLVQPPP PPTPPEATPA VTGTSTASSA GGCRSPGGAG ASAPRKFPTC PEHEMENYSM
     YCVSCRSPVC YMCLEEGRHS KHEVKPLGAT WKQHKAQLSQ ALNGVSDKAK EAKEFLVQLK
     NILQQIQENG LDYEACLVAQ CDALVDALTR QKAKLLTKVT KEREHKLKMV WDQINHCTLK
     LRQSTGLMEY CLEVIKEDDP SGFLQISDAL IKRVQTSQEQ WVKGALEPKV SAEFDLTLDS
     EPLLQAIHQL DFVQMKLPPV PLLQLEKCCT RNNSVTLAWR TPPFTHSPAE GYILELDDGD
     GGQFREVYVG KETLCTIDGL HFNSTYNARV KAFNSSGVGP YSKTVVLQTS DVAWFTFDPN
     SGHRDIILSN DNQTATCSSY DDRVVLGTAA FSKGVHYWEL HVDRYDNHPD PAFGVARASV
     VKDMMLGKDD KAWAMYVDNN RSWFMHCNSH TNRTEGGVCK GATVGVLLDL NKHTLTFFIN
     GQQQGPTAFS HVDGVFMPAL SLNRNVQVTL HTGLEVPTNL GRPKLSGN
//
ID   LRC47_MOUSE             Reviewed;         581 AA.
AC   Q505F5; Q3U380; Q6ZPW2; Q9CUZ0;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Leucine-rich repeat-containing protein 47;
GN   Name=Lrrc47; Synonyms=Kiaa1185;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 61-581.
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- SIMILARITY: Contains 8 LRR (leucine-rich) repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK013512; BAB28889.1; -; mRNA.
DR   EMBL; AK154897; BAE32909.1; -; mRNA.
DR   EMBL; BC094573; AAH94573.1; -; mRNA.
DR   EMBL; AK129306; BAC98116.1; -; mRNA.
DR   IPI; IPI00138089; -.
DR   RefSeq; NP_957678.1; NM_201226.1.
DR   UniGene; Mm.260690; -.
DR   ProteinModelPortal; Q505F5; -.
DR   SMR; Q505F5; 21-241, 317-577.
DR   PhosphoSite; Q505F5; -.
DR   REPRODUCTION-2DPAGE; Q505F5; -.
DR   PRIDE; Q505F5; -.
DR   Ensembl; ENSMUST00000030894; ENSMUSP00000030894; ENSMUSG00000029028.
DR   GeneID; 72946; -.
DR   KEGG; mmu:72946; -.
DR   NMPDR; fig|10090.3.peg.10999; -.
DR   UCSC; uc008way.1; mouse.
DR   CTD; 72946; -.
DR   MGI; MGI:1920196; Lrrc47.
DR   eggNOG; roNOG11749; -.
DR   GeneTree; ENSGT00530000063489; -.
DR   HOGENOM; HBG314933; -.
DR   HOVERGEN; HBG066309; -.
DR   InParanoid; Q505F5; -.
DR   OMA; ADNCLRE; -.
DR   OrthoDB; EOG4FTW0M; -.
DR   PhylomeDB; Q505F5; -.
DR   NextBio; 337191; -.
DR   ArrayExpress; Q505F5; -.
DR   Bgee; Q505F5; -.
DR   CleanEx; MM_LRRC47; -.
DR   Genevestigator; Q505F5; -.
DR   GermOnline; ENSMUSG00000029028; Mus musculus.
DR   GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR005146; B3/B4_tRNA-bd.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   Pfam; PF03483; B3_4; 1.
DR   Pfam; PF00560; LRR_1; 4.
DR   SMART; SM00873; B3_4; 1.
DR   SMART; SM00369; LRR_TYP; 3.
DR   PROSITE; PS51450; LRR; 6.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Leucine-rich repeat; Phosphoprotein; Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    581       Leucine-rich repeat-containing protein
FT                                47.
FT                                /FTId=PRO_0000223927.
FT   REPEAT       76     99       LRR 1.
FT   REPEAT      100    124       LRR 2.
FT   REPEAT      130    153       LRR 3.
FT   REPEAT      155    177       LRR 4.
FT   REPEAT      180    202       LRR 5.
FT   REPEAT      203    226       LRR 6.
FT   REPEAT      228    250       LRR 7.
FT   REPEAT      557    580       LRR 8.
FT   COILED      401    436       Potential.
FT   COMPBIAS      2      7       Poly-Ala.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     293    293       Phosphoserine.
FT   MOD_RES     430    430       Phosphoserine (By similarity).
FT   MOD_RES     519    519       Phosphoserine (By similarity).
FT   MOD_RES     521    521       Phosphothreonine (By similarity).
FT   CONFLICT    312    312       H -> Y (in Ref. 1; BAE32909).
FT   CONFLICT    487    487       S -> N (in Ref. 3; BAC98116).
SQ   SEQUENCE   581 AA;  63590 MW;  A82B2503E1E41EF0 CRC64;
     MAAAAMAVSE AWPELELAER ERRRELLLTG PGLEERVKAA GGRLPPRLFT LPLLHYLEVS
     GCGSLRAPGP GLAQGLPQLH SLVLRRNALG PGLSPELGPL PALRVLDLSG NALETLPPGE
     GLGPAEPPGL PQLQSLNLSG NRLRELPADL ARCAPRLQSL NLTGNRLDAF PPELFRPGAL
     PLLSELAAAD NCLRELSPDI AHLASLKTLD LSNNQLTEIP AELADCPKLK EINFRGNRLR
     DKRLEKMVGG CQTKSILEYL RAGGRGGRSK GRQEASEKED RKKRRERKQH RESGEGEEEV
     ADSARLMLKV LHVSENPTPL TVRVSPEVKD VRPYIVGAIV RGMDLQPGNA LRRFLNSQTK
     LHDDLCEKRT AATIATHDLQ AVRGPLLYAA RPPEDLKIVP LGRKEAKAKE LVRQLQLEAE
     EQRKQKKRQS VSGLHRYLHL LDGKENYPCL VDAEGDVISF PPITNSEKTK IKKTTCNLFL
     EVTSATSLQL CKDIMDSLIL RMAELSKSTS ENKEEDMLSG TEADAGCGLS DPNLTLSSGK
     DGQCPLVVEQ VRVVDLEGSL KVVYPSKTDL ITLPPHVTVV R
//
ID   KCTD8_MOUSE             Reviewed;         476 AA.
AC   Q50H33; Q8BR74; Q8C4C2; Q8C906; Q8C9B0; Q8CAA9;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   08-MAR-2011, entry version 39.
DE   RecName: Full=BTB/POZ domain-containing protein KCTD8;
GN   Name=Kctd8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RA   Odeh H.M., Mitchem K.L., Kohrman D.C.;
RT   "Conserved paralogous segments on mouse chromosome 5 and 18.";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Corpora quadrigemina, and Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, INTERACTION WITH GABRB1 AND GABRB2, AND TETRAMERIZATION.
RX   PubMed=20400944; DOI=10.1038/nature08964;
RA   Schwenk J., Metz M., Zolles G., Turecek R., Fritzius T., Bildl W.,
RA   Tarusawa E., Kulik A., Unger A., Ivankova K., Seddik R., Tiao J.Y.,
RA   Rajalu M., Trojanova J., Rohde V., Gassmann M., Schulte U., Fakler B.,
RA   Bettler B.;
RT   "Native GABA(B) receptors are heteromultimers with a family of
RT   auxiliary subunits.";
RL   Nature 465:231-235(2010).
CC   -!- FUNCTION: Auxiliary subunit of GABA-B receptors that determine the
CC       pharmacology and kinetics of the receptor response. Increases
CC       agonist potency and markedly alter the G-protein signaling of the
CC       receptors by accelerating onset and promoting desensitization.
CC   -!- SUBUNIT: Interacts as a tetramer with GABRB1 and GABRB2.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, presynaptic cell
CC       membrane (By similarity). Cell junction, synapse, postsynaptic
CC       cell membrane (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q50H33-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q50H33-2; Sequence=VSP_020761, VSP_020762;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
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DR   EMBL; AY615967; AAU25822.1; -; mRNA.
DR   EMBL; AK039167; BAC30262.2; -; mRNA.
DR   EMBL; AK042569; BAC31296.1; -; mRNA.
DR   EMBL; AK043351; BAC31527.1; -; mRNA.
DR   EMBL; AK045439; BAC32368.1; -; mRNA.
DR   EMBL; AK082563; BAC38532.1; -; mRNA.
DR   EMBL; BC116940; AAI16941.1; -; mRNA.
DR   EMBL; BC116942; AAI16943.1; -; mRNA.
DR   IPI; IPI00227455; -.
DR   IPI; IPI00474244; -.
DR   RefSeq; NP_780728.3; NM_175519.5.
DR   UniGene; Mm.478547; -.
DR   ProteinModelPortal; Q50H33; -.
DR   SMR; Q50H33; 9-167.
DR   PhosphoSite; Q50H33; -.
DR   PRIDE; Q50H33; -.
DR   Ensembl; ENSMUST00000054095; ENSMUSP00000055326; ENSMUSG00000037653.
DR   GeneID; 243043; -.
DR   KEGG; mmu:243043; -.
DR   NMPDR; fig|10090.3.peg.11677; -.
DR   UCSC; uc008xqj.1; mouse.
DR   CTD; 243043; -.
DR   MGI; MGI:2443804; Kctd8.
DR   eggNOG; roNOG04378; -.
DR   GeneTree; ENSGT00600000084079; -.
DR   HOGENOM; HBG445337; -.
DR   HOVERGEN; HBG052218; -.
DR   InParanoid; Q50H33; -.
DR   OMA; LATMFSP; -.
DR   OrthoDB; EOG4MKNGT; -.
DR   PhylomeDB; Q50H33; -.
DR   NextBio; 385637; -.
DR   ArrayExpress; Q50H33; -.
DR   Bgee; Q50H33; -.
DR   Genevestigator; Q50H33; -.
DR   GermOnline; ENSMUSG00000037653; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   PROSITE; PS50097; BTB; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Membrane;
KW   Postsynaptic cell membrane; Synapse.
FT   CHAIN         1    476       BTB/POZ domain-containing protein KCTD8.
FT                                /FTId=PRO_0000251482.
FT   DOMAIN       44    122       BTB.
FT   VAR_SEQ     325    346       PPQKIVSPKQEHEDRKRDKVTD -> KETAQRNCFSHFIHH
FT                                MRVDGKA (in isoform 2).
FT                                /FTId=VSP_020761.
FT   VAR_SEQ     347    476       Missing (in isoform 2).
FT                                /FTId=VSP_020762.
FT   CONFLICT     45     45       V -> I (in Ref. 2; BAC31296).
FT   CONFLICT     82     83       GA -> RAP (in Ref. 2; BAC31296).
FT   CONFLICT    149    149       K -> E (in Ref. 2; BAC38532).
FT   CONFLICT    159    159       E -> K (in Ref. 2; BAC30262).
FT   CONFLICT    206    206       D -> Y (in Ref. 2; BAC32368).
FT   CONFLICT    359    359       S -> Y (in Ref. 2; BAC32368).
FT   CONFLICT    412    412       N -> K (in Ref. 2; BAC31527).
SQ   SEQUENCE   476 AA;  52768 MW;  26EC9C5A673A53DF CRC64;
     MALKDTGSGG STILPISEMV SASSSPGAPL AAAPGPCAPS PFPEVVELNV GGQVYVTKHS
     TLLSVPDSTL ASMFSPSSPR GGARRRGDLP RDSRARFFID RDGFLFRYVL DYLRDKQLAL
     PEHFPEKERL LREAEFFQLT DLVKLLSPKV TKQNSLNDEC CQSDLEDNVS QGSSDALLLR
     GAAAGAPSGS GAHGVSGVVG GGSAPDKRSG FLTLGYRGSY TTVRDNQADA KFRRVARIMV
     CGRIALAKEV FGDTLNESRD PDRQPEKYTS RFYLKFTYLE QAFDRLSEAG FHMVACNSSG
     TAAFVNQYRD DKIWSSYTEY IFFRPPQKIV SPKQEHEDRK RDKVTDKGSE SGTSCNELST
     SSCDSHSEAS TPQDNPANTQ QAAAHQPNTL TLDRPSRKAP VQWMPPPDKR RNSELFQSLI
     SKSRETNLSK KKVCEKLSVE EEMKKCIQDF KKIHIPDCFP ERKRQWQSEL LQKYGL
//
ID   Q50HX0_MOUSE            Unreviewed;       215 AA.
AC   Q50HX0;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   08-MAR-2011, entry version 46.
DE   SubName: Full=RAB14 protein;
GN   Name=Rab14; Synonyms=rab14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SAMR1/TA; TISSUE=Brain;
RA   Zhang C., Yang T., Liu G., Chen Q.;
RT   "The rab14 and its variant coexist in SAM mice.";
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR   EMBL; AJ968959; CAI92129.1; -; mRNA.
DR   IPI; IPI00126042; -.
DR   UniGene; Mm.198264; -.
DR   ProteinModelPortal; Q50HX0; -.
DR   SMR; Q50HX0; 7-173.
DR   STRING; Q50HX0; -.
DR   Ensembl; ENSMUST00000028238; ENSMUSP00000028238; ENSMUSG00000026878.
DR   MGI; MGI:1915615; Rab14.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; Q50HX0; -.
DR   ArrayExpress; Q50HX0; -.
DR   Bgee; Q50HX0; -.
DR   Genevestigator; Q50HX0; -.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   2: Evidence at transcript level;
KW   GTP-binding; Nucleotide-binding.
SQ   SEQUENCE   215 AA;  23910 MW;  526A6B98E1B044A6 CRC64;
     MATAPYNYSY IFKYIIIGDM GVGKSCLLHQ FTEKKFMADC PHTIGVEFGT RIIEVSGQKI
     KLQIWDTAGQ ERFRAVTRSY YRGAAGALMV YDITRRSTYN HLSSWLTDAR NLTNPNTVII
     LIGNKADLEA QRDVTYEEAK QFAEENGLLF LEASAKTGEN VEDAFLEAAK KIYQNIQDGS
     LDLDAAESGV QHKPSAPQGG RLISEPQPQR EGCGC
//
ID   PA24E_MOUSE             Reviewed;         875 AA.
AC   Q50L42; Q8BX44;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Cytosolic phospholipase A2 epsilon;
DE            Short=cPLA2-epsilon;
DE            EC=3.1.1.4;
DE   AltName: Full=Phospholipase A2 group IVE;
GN   Name=Pla2g4e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J;
RX   PubMed=15866882; DOI=10.1074/jbc.M413711200;
RA   Ohto T., Uozumi N., Hirabayashi T., Shimizu T.;
RT   "Identification of novel cytosolic phospholipase A(2)s, murine
RT   cPLA(2)delta, epsilon, and zeta, which form a gene cluster with
RT   cPLA(2)beta.";
RL   J. Biol. Chem. 280:24576-24583(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Calcium-dependent phospholipase A2 that selectively
CC       hydrolyzes glycerophospholipids in the sn-2 position.
CC   -!- CATALYTIC ACTIVITY: Phosphatidylcholine + H(2)O = 1-
CC       acylglycerophosphocholine + a carboxylate.
CC   -!- ENZYME REGULATION: Stimulated by cytosolic Ca(2+) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Lysosome membrane;
CC       Peripheral membrane protein; Cytoplasmic side (Potential).
CC       Note=Translocates to lysosomal membranes in a calcium-dependent
CC       fashion.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q50L42-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q50L42-2; Sequence=VSP_019884, VSP_019885, VSP_019886;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in heart, skeletal
CC       muscle, testis and thyroid. Expressed at lower level in brain and
CC       stomach.
CC   -!- DOMAIN: The N-terminal C2 domain associates with lipid membranes
CC       upon calcium binding. It modulates enzyme activity by presenting
CC       the active site to its substrate in response to elevations of
CC       cytosolic Ca(2+) (By similarity).
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 PLA2c domain.
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DR   EMBL; AB195277; BAD98153.1; -; mRNA.
DR   EMBL; AK049063; BAC33531.1; -; mRNA.
DR   IPI; IPI00226464; -.
DR   IPI; IPI00775845; -.
DR   RefSeq; NP_808513.2; NM_177845.4.
DR   UniGene; Mm.330505; -.
DR   ProteinModelPortal; Q50L42; -.
DR   SMR; Q50L42; 76-869.
DR   STRING; Q50L42; -.
DR   PRIDE; Q50L42; -.
DR   Ensembl; ENSMUST00000090071; ENSMUSP00000087525; ENSMUSG00000050211.
DR   GeneID; 329502; -.
DR   KEGG; mmu:329502; -.
DR   UCSC; uc008lvf.1; mouse.
DR   UCSC; uc008lvg.1; mouse.
DR   CTD; 329502; -.
DR   MGI; MGI:1919144; Pla2g4e.
DR   eggNOG; maNOG04037; -.
DR   GeneTree; ENSGT00550000074489; -.
DR   HOGENOM; HBG444615; -.
DR   HOVERGEN; HBG080412; -.
DR   InParanoid; Q50L42; -.
DR   OMA; CFHYPKY; -.
DR   OrthoDB; EOG48D0TQ; -.
DR   PhylomeDB; Q50L42; -.
DR   BRENDA; 3.1.1.4; 244.
DR   NextBio; 398788; -.
DR   ArrayExpress; Q50L42; -.
DR   Bgee; Q50L42; -.
DR   CleanEx; MM_PLA2G4E; -.
DR   Genevestigator; Q50L42; -.
DR   GermOnline; ENSMUSG00000050211; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004623; F:phospholipase A2 activity; IDA:MGI.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPlipase.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR002642; Lysophospholipase_cat_dom.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF01735; PLA2_B; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00022; PLAc; 1.
DR   SUPFAM; SSF52151; Acyl_Trfase/lysoPlipase; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS51210; PLA2C; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Calcium; Cytoplasm; Hydrolase;
KW   Lipid degradation; Lysosome; Membrane; Metal-binding.
FT   CHAIN         1    875       Cytosolic phospholipase A2 epsilon.
FT                                /FTId=PRO_0000247026.
FT   DOMAIN       68    168       C2.
FT   DOMAIN      332    875       PLA2c.
FT   ACT_SITE    420    420       Nucleophile (By similarity).
FT   ACT_SITE    708    708       Proton acceptor (By similarity).
FT   VAR_SEQ       1    243       Missing (in isoform 2).
FT                                /FTId=VSP_019884.
FT   VAR_SEQ     584    599       LWSSIFSLNLLDAWNL -> DSLRYSAPERARPAFD (in
FT                                isoform 2).
FT                                /FTId=VSP_019885.
FT   VAR_SEQ     600    875       Missing (in isoform 2).
FT                                /FTId=VSP_019886.
FT   CONFLICT    513    513       R -> K (in Ref. 2; BAC33531).
SQ   SEQUENCE   875 AA;  100157 MW;  74A628C1E1A2CDEA CRC64;
     MQSIPHSDEA DVAGMTHASE GHHGLGTSML VPKNPQGEED SKLGRNCSGF EDAQDPQTAV
     PSSPLLSMAS CSSQEGSSPC HLLTVRIIGM KNVRQADILS QTDCFVTLWL PTASQKKLKT
     RTISNCLHPE WDESFTFQIQ TQVKNVLELS VCDEDTLTQN DHLLTVLYDL SKLCLRNKTH
     VKFPLNPEGM EELEVEFLLE ENFSSSETLI TNGVLVSRQV SCLEVHAESR RPRKRKKNKD
     LLVMVTDSFE NTQRVPPCQE PCYPNSACFH YPKYSQPQLY AEAPKSHCNF RLCCCGTHRN
     DPVCQPLNCL SDGQVTTLPV GENYELHMKS SPCSDTLDVR LGFSLCQEEV EFVQKRKMVV
     AKTLSQMLQL EEGLHEDEVP IIAIMATGGG TRSMVSLYGH LLGLQKLNFL DASTYITGLS
     GATWTMATLY SDPEWSSKNL ETVVFEARRH VVKDKMPALF PDQLYKWRED LQKHSQEGYK
     TTFTDFWGKL IEYSLGDKKN ECKLSDQRAA LCRGQNPLPI YLTINVKDDV SNQDFREWFE
     FSPYEVGMQK YGAFIPSELF GSEFFMGRLM KRIPEPEMCY MLGLWSSIFS LNLLDAWNLS
     HTSEEFFYRW TRERLHDIED DPILPEIPRC DDNPLETTVV IPTTWLSNTF REILTRRPFV
     SEFHNFLYGM QLHTDYLQNR QFSMWKDTVL DTFPNQLTQF AKHLNLLDTA FFVNSSYAPL
     LRPERKVDLI IHLNYCAGSQ TKPLKQTCEY CTEQKIPFPS FSILEDDNSL KECYVMENPQ
     EPDAPIVAYF PLISDTFQKY KAPGVERSPD ELELGQLNIY GPKSPYATKE LTYTEAAFDK
     LVKLSEYNIL NNRDKLIQAL RLAMEKKRMR SQCPS
//
ID   C2CD3_MOUSE             Reviewed;        2323 AA.
AC   Q52KB6; Q3UFQ3; Q80V48; Q8BXE5;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   08-FEB-2011, entry version 39.
DE   RecName: Full=C2 domain-containing protein 3;
GN   Name=C2cd3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-402 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 379-2323 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 71-2323 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1232-2323 (ISOFORM 3).
RC   STRAIN=129, and C57BL/6; TISSUE=Head, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q52KB6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q52KB6-2; Sequence=VSP_029449, VSP_029450;
CC       Name=3;
CC         IsoId=Q52KB6-3; Sequence=VSP_029451, VSP_029452;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH94430.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK047412; BAC33048.1; -; mRNA.
DR   EMBL; AK148365; BAE28507.1; -; mRNA.
DR   EMBL; BC046408; AAH46408.1; -; mRNA.
DR   EMBL; BC094430; AAH94430.1; ALT_INIT; mRNA.
DR   IPI; IPI00674192; -.
DR   IPI; IPI00875529; -.
DR   IPI; IPI00875926; -.
DR   RefSeq; NP_001017985.2; NM_001017985.2.
DR   UniGene; Mm.276374; -.
DR   ProteinModelPortal; Q52KB6; -.
DR   SMR; Q52KB6; 1658-1743.
DR   STRING; Q52KB6; -.
DR   PhosphoSite; Q52KB6; -.
DR   PRIDE; Q52KB6; -.
DR   Ensembl; ENSMUST00000051777; ENSMUSP00000062637; ENSMUSG00000047248.
DR   GeneID; 277939; -.
DR   KEGG; mmu:277939; -.
DR   CTD; 277939; -.
DR   MGI; MGI:2142166; C2cd3.
DR   GeneTree; ENSGT00510000048072; -.
DR   HOGENOM; HBG714076; -.
DR   HOVERGEN; HBG107544; -.
DR   InParanoid; Q52KB6; -.
DR   NextBio; 393858; -.
DR   ArrayExpress; Q52KB6; -.
DR   Bgee; Q52KB6; -.
DR   CleanEx; MM_C2CD3; -.
DR   Genevestigator; Q52KB6; -.
DR   GO; GO:0005932; C:microtubule basal body; IDA:MGI.
DR   GO; GO:0007420; P:brain development; IMP:MGI.
DR   GO; GO:0042384; P:cilium assembly; IMP:MGI.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR   GO; GO:0001947; P:heart looping; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0021997; P:neural plate axis specification; IMP:MGI.
DR   GO; GO:0021915; P:neural tube development; IMP:MGI.
DR   GO; GO:0016485; P:protein processing; IMP:MGI.
DR   GO; GO:0030162; P:regulation of proteolysis; IDA:MGI.
DR   GO; GO:0008589; P:regulation of smoothened signaling pathway; IGI:MGI.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   Pfam; PF00168; C2; 2.
DR   SMART; SM00239; C2; 5.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Phosphoprotein; Repeat.
FT   CHAIN         1   2323       C2 domain-containing protein 3.
FT                                /FTId=PRO_0000311240.
FT   DOMAIN     1168   1306       C2 1.
FT   DOMAIN     1603   1709       C2 2.
FT   MOD_RES    1114   1114       Phosphothreonine (By similarity).
FT   MOD_RES    2106   2106       Phosphoserine (By similarity).
FT   VAR_SEQ    1941   1943       DLQ -> GDY (in isoform 2).
FT                                /FTId=VSP_029449.
FT   VAR_SEQ    1944   2323       Missing (in isoform 2).
FT                                /FTId=VSP_029450.
FT   VAR_SEQ    2114   2130       QPAQGSPSQSGVCEGGA -> CPEALSPQTLLHPSQPS
FT                                (in isoform 3).
FT                                /FTId=VSP_029451.
FT   VAR_SEQ    2131   2323       Missing (in isoform 3).
FT                                /FTId=VSP_029452.
FT   CONFLICT    483    483       Q -> K (in Ref. 1; BAC33048).
FT   CONFLICT    587    587       G -> E (in Ref. 1; BAC33048).
SQ   SEQUENCE   2323 AA;  255274 MW;  6932D35D906E056E CRC64;
     MKQRKGQGPG GGRGRKKRGL SDISPSTSLP PLVEGQLRCF LKLTINKVVW KIAKPPTSVL
     VRVRWWGETS DGTLFCPRDA LQTEPKAVRT TTRYGIRCGP KQFTSYLTDM AVLVLEVITK
     FDHLPVGRVQ ISGLAQLSPT HQINGFFTIV SPASKKLGEL QVSLALEPLS ETYDSYKPLP
     ATEVTKNVLL SERELRENTE SSNTQSMIPS RSCRGPAIKI DGKELAGHSS RSTTPRGKDH
     LYFAENSDAV KGSLCGLQQH LNQGTNVETI TLRGKAPQKQ LSLLNSSEFQ PQISTVAKSH
     SDSCILSSNT PPAKDLLSAL LEQGNKLRNA MLISAMNSNP DTSMLLDKVP PPMTEAIPRS
     SALNSSENHF KGHSADHLLP LADTGAIQLL LGSAELSQGH FWNGLGSPPD SPTPGSDEYC
     SSDLNDPQYD QSLLENLFYT VPKSDVGTSE LPSEDDGVEP SRTMNQSKAS GRSKVVESKE
     QKQKRAAVKK SRNPIDQQEL SRTPGHTPAM SLSVDRLALL GRVHSVRIIV ETMGVPPDSP
     HMTPSRKNFA GKPPKPTAAK KRTFFVEYHF PVGFSKSGLG KTALITGVVR LASSKITDGV
     VKFQQRFVCP VEFGGPMIEH WWDSNLIFQI YAKKTPQKKP EVIGSASLPL RAVIQSELLS
     FSSQLPVQQE NGLSSLGPLK VTMELVLGHK DFTGISAKLS SSTQPAPVSA ATSSDTILPE
     TGQDTACTRN PQSSNKIHEE TTKKTQNLVL PDQESANSVA SNSSIFMAVP SCNLVHQING
     SNKESGLLLH VLLMVPDGKD FVFGEREKQP SCNVYLNCKL FSTEEVTRSV VSWGTAQPVF
     NFSQVIPVSL TSKCLERLKN NVMIIETWNK VRSPGQDKLL GLVKLPLHQF YMSFKDPKIS
     RLLLDARYPV VAVDSYMPVI DVFSGHQNGS LRVFLAMGSS AQIMMLQRLK NEEGTLPPFS
     PRPAHFLDQP PVASVAMPEK QGTRLMEHHF EFCVAMVKGL MPLQATVWGE ADCYVQYYFP
     FQDSQPSVLQ GPDFLENGIT LKPFRTSTTL CVPDPVFNSE HHHSLLLPTD VPVQRLLLSA
     FSSQGLVPGG GVQFEVWCRY YYPNVRDQMV AKGTLPLSRV CAMVTMQYRE DVGMQSFNLP
     LTSRLEHSKE LKNQSSGFLD VGLRYRRSPR TAEGILAARA VSISVHIIRA CGLQAAAKAL
     AEQEPALQFS ATVGVNASVT AHLSFLPKGE QRQTRPVACS FCPEFSHHIE FPCNLVTQHC
     SGEACFLAEL LEFAEIIFAI YHENTKSVSD ITSIQSCKDY LLGIVKVPTK DLLVKRSGIT
     GWYPVILPED KGLPQDLDLM QKIVGGLELS VSFAHPGDRE RVLEAAELLG WSFESIPKDL
     VKKEEEVPAT VTISTPRLWL PIHCVLLAGH MNIHKNTYCY LRYKLYNQEA FWTPLRKPKE
     STNKNQVLIT FKASKRAEVT RSQSLLWYFR EEKLEIQVWR AYGNDNLERP HQTDSWIGSA
     YVDLSRLGEK SPRTLTISGV YPLFGRNASD LSGAALRIHV LLSPLSPHTE PARELDSMDC
     SSHSESEQHP RKSDALQLSP PHVLQTSPTS TQVHGNSAAA QVCPAQEGPP ELAGTFAVSI
     LVERAMHLSL KGSPLTDRKV SVPSCCVSFA TATELSPVYT HVVENTDSPI WGFHQQARLS
     KELLLDPHQT LVFKVWHKGD EERVVGFASV DLSPLLSGFQ FICGWYNITD FSGECQGQIK
     VAISPMESLM HLKEERQARR GIDTPGALIP LFSALSFPAS AGCDAFPRPI ARHVEGQLAH
     TSPKEDGLSS PARNGAIRSQ AARHEEHVQN IRRFHESLQH GEAVLTSDEK LTTAPSSSHT
     SILTSLRKNL SELDEIQKYF SQKLSKPFLP FSSQSSPAVS QSQESQRDPV AAGTGRQDPE
     NQCILEKSNH LVSQVSSLIS DLQTLTRGSQ AALTSQQARS RSRAVTTIPD AQGTEAAGEG
     STTLEEPLAG AIEASTDSLP PPVEEPSKGG GMLHESLEQT MPITRVQSID DTEVGPDYSD
     EDYEEDIIEP RTLNEITTVT DRTSPWSSFM SDMSEVLSPQ PTEVQREGPS CPPEPFPREE
     LKVKSSPQKA VSPQPAQGSP SQSGVCEGGA YKIEVEDLAS AKPQPVPSLT FSEAQEGSDS
     VGWRASQINQ VRKPMPEMLA ESEAFSSEFS DSSESFETFP LHLPSQSKRE DYKDSPAVRQ
     KQVPTGSEVS TRQTLLLPEP VVVPNFFLPP QQLEASLRMI SHSPGLPPAA TTDQDKSEAT
     RGALAQRPCR PRPYSIPPNL PEEETRRIAR IFSSQYSKKT EET
//
ID   SPIR1_MOUSE             Reviewed;         598 AA.
AC   Q52KF3; Q6PDJ5; Q80V45;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   RecName: Full=Protein spire homolog 1;
GN   Name=Spire1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 314-598 (ISOFORM 3).
RC   STRAIN=129, and C57BL/6; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15053972; DOI=10.1016/j.modgep.2003.11.006;
RA   Schumacher N., Borawski J.M., Leberfinger C.B., Gessler M.,
RA   Kerkhoff E.;
RT   "Overlapping expression pattern of the actin organizers Spir-1 and
RT   formin-2 in the developing mouse nervous system and the adult brain.";
RL   Gene Expr. Patterns 4:249-255(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305; SER-306 AND
RP   SER-308, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305; SER-306 AND
RP   SER-308, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Acts as a actin nucleation factor, remains associated
CC       with the slow-growing pointed end of the new filament. Involved in
CC       vesicle transport processes providing a novel link between actin
CC       organization and intracellular transport (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Cytoplasm, perinuclear region (By similarity). Note=Punctate spots
CC       in perinuclear region and cytoplasm, co-localised with Rab11 (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q52KF3-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q52KF3-2; Sequence=VSP_052596;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q52KF3-3; Sequence=VSP_038300;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in the developing nervous system and
CC       in the adult brain, specifically the Purkinje cells of the
CC       cerebellum, in neuronal cells in the CA1, CA2 and CA3 fields of
CC       the hippocampus and granular layer of the dentate gyrus.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryos and adults.
CC   -!- DOMAIN: Binds to actin monomers via the WH2 domain (By
CC       similarity).
CC   -!- DOMAIN: The Spir-box targets binding to intracellular membrane
CC       structures (By similarity).
CC   -!- SIMILARITY: Belongs to the spire family.
CC   -!- SIMILARITY: Contains 1 KIND domain.
CC   -!- SIMILARITY: Contains 2 WH2 domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH58669.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC046486; AAH46486.2; -; mRNA.
DR   EMBL; BC058669; AAH58669.1; ALT_INIT; mRNA.
DR   EMBL; BC094375; AAH94375.1; -; mRNA.
DR   IPI; IPI00380020; -.
DR   IPI; IPI00420800; -.
DR   IPI; IPI00874319; -.
DR   UniGene; Mm.208723; -.
DR   ProteinModelPortal; Q52KF3; -.
DR   SMR; Q52KF3; 399-469.
DR   PhosphoSite; Q52KF3; -.
DR   PRIDE; Q52KF3; -.
DR   Ensembl; ENSMUST00000082243; ENSMUSP00000080871; ENSMUSG00000024533.
DR   UCSC; uc008fml.1; mouse.
DR   MGI; MGI:1915416; Spire1.
DR   GeneTree; ENSGT00390000003058; -.
DR   HOVERGEN; HBG058898; -.
DR   OrthoDB; EOG44J2HS; -.
DR   ArrayExpress; Q52KF3; -.
DR   Bgee; Q52KF3; -.
DR   CleanEx; MM_SPIRE1; -.
DR   Genevestigator; Q52KF3; -.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0048193; P:Golgi vesicle transport; IDA:MGI.
DR   InterPro; IPR011019; KIND.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS51377; KIND; 1.
DR   PROSITE; PS51082; WH2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW   Phosphoprotein; Repeat; Transport.
FT   CHAIN         1    598       Protein spire homolog 1.
FT                                /FTId=PRO_0000309571.
FT   DOMAIN        1     73       KIND.
FT   DOMAIN      147    165       WH2 1.
FT   DOMAIN      211    228       WH2 2.
FT   REGION      398    418       Spir-box.
FT   MOD_RES     305    305       Phosphoserine.
FT   MOD_RES     306    306       Phosphoserine.
FT   MOD_RES     308    308       Phosphoserine.
FT   VAR_SEQ     238    238       L -> LA (in isoform 2).
FT                                /FTId=VSP_052596.
FT   VAR_SEQ     388    388       L -> LVPRITGVWPRTPFRPLFSTIQTASLLSSHPFEAAM
FT                                FGVAGAMYYLFERAFTSRWKPSK (in isoform 3).
FT                                /FTId=VSP_038300.
SQ   SEQUENCE   598 AA;  68450 MW;  3E0D490F47CF568B CRC64;
     MANTVEADGS KDEGYEAADE GPEDEDGEKR SISAIRSYQD VMKICAAHLP TESEAPNHYQ
     AVCRALFAET MELHTFLTKI KSAKENLKKI QEMEKGDESS TDLEDLKNAD WARFWVQVMR
     DLRNGVKLKK VQQRQYNPLP IEYQLTPYEM LMDDIRCKRY TLRKVMVNGD VPPRLKKSAH
     EVILDFIRSR PPLNPVSARK LKPTPPRPRS LHERILEEIK AERKLRPVSP EEIRRSRLVR
     PLSMSHSFDL SDVTTPESPK NVGESSMVNG GLTSQTKENG LSAAQQGSAQ RKRLLKAPTL
     AELDSSDSEE EKSLHKSTSS SSASPSLYED PVLEAMCSRK KPPKFLPISS TPQPERRQPP
     QRRHSIEKET PTNVRQFLPP SRQSSRSLEE FCYPVECLAL TVEEVMHIRQ VLVKAELEKY
     QQYKDVYTAL KKGKLCFCCR TRRFSFFTWS YTCQFCKRPV CSQCCKKMRL PSKPYSTLPI
     FSLGPSALQR GESCSRSEKP STSHHRPLRS IARFSTKSRS VDKSDEELQF PKELMEDWST
     MEVCVDCKKF ISEIISSSRR SLVLANKRAR LKRKTQSFYM SSAGPSEYCP SERTINEI
//
ID   SRRM1_MOUSE             Reviewed;         946 AA.
AC   Q52KI8; O70495; Q9CVG5;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Serine/arginine repetitive matrix protein 1;
DE   AltName: Full=Plenty-of-prolines 101;
GN   Name=Srrm1; Synonyms=Pop101;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RA   Vayssiere B.M., Camonis J.H.;
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, and NMRI; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-265 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-572 AND SER-574, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461; SER-463; SER-591;
RP   THR-593; THR-600; SER-602; THR-913 AND SER-915, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-572, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461; SER-463; SER-723;
RP   SER-725; SER-731; SER-733; SER-810; SER-816; SER-822 AND SER-915, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387; SER-391; SER-427;
RP   SER-429; SER-448; SER-616; SER-624; SER-626; SER-635; SER-810 AND
RP   SER-814, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-209; SER-211;
RP   SER-220; SER-260; SER-387; SER-389; SER-391; THR-404; SER-427;
RP   SER-429; SER-448; SER-461; SER-463; SER-561; SER-563; SER-572;
RP   SER-574; SER-591; THR-593; THR-600; SER-602; SER-624; SER-626;
RP   THR-633; SER-635; SER-645; SER-647; SER-655; SER-657; SER-672;
RP   SER-702; SER-704; SER-723; SER-725; SER-766; THR-768; SER-779;
RP   SER-781; SER-784; SER-793; SER-795; SER-797; SER-832 AND SER-915, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260; SER-387; SER-427;
RP   SER-429; SER-694; SER-702; SER-704; SER-779 AND SER-781, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; SER-260; SER-572;
RP   SER-574; SER-616; SER-714; SER-723; SER-725; SER-731; SER-810;
RP   SER-816; SER-822; THR-913 AND SER-915, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Part of pre- and post-splicing multiprotein mRNP
CC       complexes. Involved in numerous pre-mRNA processing events.
CC       Promotes constitutive and exonic splicing enhancer (ESE)-dependent
CC       splicing activation by bridging together sequence-specific (SR
CC       family proteins, SFRS4, SFRS5 and TRA2B/SFRS10) and basal snRNP
CC       (SNRP70 and SNRPA1) factors of the spliceosome. Stimulates mRNA
CC       3'-end cleavage independently of the formation of an exon junction
CC       complex. Binds both pre-mRNA and spliced mRNA 20-25 nt upstream of
CC       exon-exon junctions. Binds RNA and DNA with low sequence
CC       specificity and has similar preference for either double- or
CC       single-stranded nucleic acid substrates (By similarity).
CC   -!- SUBUNIT: Identified in the spliceosome C complex, at least
CC       composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23,
CC       DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1,
CC       GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK,
CC       HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1,
CC       PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B,
CC       PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2,
CC       SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2,
CC       SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2,
CC       SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8. Found
CC       in a pre-mRNA splicing complex with SFRS4, SFRS5, SNRP70, SNRPA1,
CC       SRRM1 and SRRM2. Found in a pre-mRNA exonic splicing enhancer
CC       (ESE) complex with SNRP70, SNRPA1, SRRM1 and TRA2B/SFRS10. Found
CC       in a mRNA splicing-dependent exon junction complex (EJC) with DEK,
CC       PRPF8, NCBP1, RBM8A, RNPS1, SRRM1 and THOC4. Interacts with BAT1,
CC       CPSF1, RBM8A, RNPS1, and THOC4. Seems to be a compound of RNA
CC       export complexes that are released from speckles in a ATP-
CC       dependent manner (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus matrix (By similarity). Nucleus
CC       speckle (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q52KI8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q52KI8-2; Sequence=VSP_016524, VSP_016525;
CC   -!- SIMILARITY: Belongs to the splicing factor SR family.
CC   -!- SIMILARITY: Contains 1 PWI domain.
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DR   EMBL; AF062655; AAC17422.1; -; mRNA.
DR   EMBL; BC094322; AAH94322.1; -; mRNA.
DR   EMBL; AK008284; BAB25575.1; -; mRNA.
DR   IPI; IPI00118438; -.
DR   IPI; IPI00605037; -.
DR   RefSeq; NP_058079.2; NM_016799.3.
DR   UniGene; Mm.1963; -.
DR   ProteinModelPortal; Q52KI8; -.
DR   SMR; Q52KI8; 27-134.
DR   STRING; Q52KI8; -.
DR   PhosphoSite; Q52KI8; -.
DR   PRIDE; Q52KI8; -.
DR   Ensembl; ENSMUST00000030613; ENSMUSP00000030613; ENSMUSG00000028809.
DR   Ensembl; ENSMUST00000105862; ENSMUSP00000101488; ENSMUSG00000028809.
DR   GeneID; 51796; -.
DR   KEGG; mmu:51796; -.
DR   UCSC; uc008vge.1; mouse.
DR   CTD; 51796; -.
DR   MGI; MGI:1858303; Srrm1.
DR   GeneTree; ENSGT00580000081375; -.
DR   HOGENOM; HBG402935; -.
DR   HOVERGEN; HBG054044; -.
DR   InParanoid; Q52KI8; -.
DR   NextBio; 308036; -.
DR   ArrayExpress; Q52KI8; -.
DR   Bgee; Q52KI8; -.
DR   CleanEx; MM_SRRM1; -.
DR   Genevestigator; Q52KI8; -.
DR   GermOnline; ENSMUSG00000028809; Mus musculus.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR002483; PWI.
DR   Gene3D; G3DSA:1.20.1390.10; PWI; 1.
DR   Pfam; PF01480; PWI; 1.
DR   SMART; SM00311; PWI; 1.
DR   SUPFAM; SSF101233; PWI; 1.
DR   PROSITE; PS51025; PWI; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; DNA-binding; mRNA processing;
KW   mRNA splicing; Nucleus; Phosphoprotein; RNA-binding; Spliceosome.
FT   CHAIN         1    946       Serine/arginine repetitive matrix protein
FT                                1.
FT                                /FTId=PRO_0000076327.
FT   DOMAIN       27    126       PWI.
FT   REGION        1    156       Necessary for mRNA 3'-end cleavage and
FT                                cytoplasmic accumulation (By similarity).
FT   REGION        1    151       Necessary for DNA and RNA-binding (By
FT                                similarity).
FT   REGION      298    707       Necessary for speckles and matrix
FT                                localization (By similarity).
FT   COMPBIAS    163    767       Arg-rich.
FT   COMPBIAS    276    500       Ser-rich.
FT   COMPBIAS    309    415       Pro-rich.
FT   COMPBIAS    562    839       Pro-rich.
FT   COMPBIAS    850    876       Lys-rich.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      10     10       Phosphoserine (By similarity).
FT   MOD_RES     140    140       N6-acetyllysine (By similarity).
FT   MOD_RES     186    186       Phosphoserine (By similarity).
FT   MOD_RES     187    187       Phosphoserine (By similarity).
FT   MOD_RES     196    196       Phosphoserine (By similarity).
FT   MOD_RES     198    198       Phosphoserine (By similarity).
FT   MOD_RES     200    200       Phosphoserine (By similarity).
FT   MOD_RES     207    207       Phosphoserine.
FT   MOD_RES     209    209       Phosphoserine.
FT   MOD_RES     211    211       Phosphoserine.
FT   MOD_RES     220    220       Phosphoserine.
FT   MOD_RES     260    260       Phosphoserine.
FT   MOD_RES     290    290       Phosphoserine (By similarity).
FT   MOD_RES     387    387       Phosphoserine.
FT   MOD_RES     389    389       Phosphoserine.
FT   MOD_RES     391    391       Phosphoserine.
FT   MOD_RES     400    400       Phosphoserine (By similarity).
FT   MOD_RES     404    404       Phosphothreonine.
FT   MOD_RES     427    427       Phosphoserine.
FT   MOD_RES     429    429       Phosphoserine.
FT   MOD_RES     433    433       Phosphothreonine (By similarity).
FT   MOD_RES     434    434       Phosphoserine (By similarity).
FT   MOD_RES     448    448       Phosphoserine.
FT   MOD_RES     450    450       Phosphoserine (By similarity).
FT   MOD_RES     461    461       Phosphoserine.
FT   MOD_RES     463    463       Phosphoserine.
FT   MOD_RES     476    476       Phosphoserine (By similarity).
FT   MOD_RES     522    522       Phosphoserine (By similarity).
FT   MOD_RES     524    524       Phosphoserine (By similarity).
FT   MOD_RES     526    526       Phosphoserine (By similarity).
FT   MOD_RES     528    528       Phosphoserine (By similarity).
FT   MOD_RES     530    530       Phosphoserine (By similarity).
FT   MOD_RES     539    539       Phosphoserine (By similarity).
FT   MOD_RES     561    561       Phosphoserine.
FT   MOD_RES     563    563       Phosphoserine.
FT   MOD_RES     572    572       Phosphoserine.
FT   MOD_RES     574    574       Phosphoserine.
FT   MOD_RES     591    591       Phosphoserine.
FT   MOD_RES     593    593       Phosphothreonine.
FT   MOD_RES     600    600       Phosphothreonine.
FT   MOD_RES     602    602       Phosphoserine.
FT   MOD_RES     616    616       Phosphoserine.
FT   MOD_RES     623    623       Phosphotyrosine (By similarity).
FT   MOD_RES     624    624       Phosphoserine.
FT   MOD_RES     626    626       Phosphoserine.
FT   MOD_RES     633    633       Phosphothreonine.
FT   MOD_RES     635    635       Phosphoserine.
FT   MOD_RES     645    645       Phosphoserine.
FT   MOD_RES     647    647       Phosphoserine.
FT   MOD_RES     655    655       Phosphoserine.
FT   MOD_RES     657    657       Phosphoserine.
FT   MOD_RES     672    672       Phosphoserine.
FT   MOD_RES     684    684       Phosphoserine (By similarity).
FT   MOD_RES     694    694       Phosphoserine.
FT   MOD_RES     702    702       Phosphoserine.
FT   MOD_RES     704    704       Phosphoserine.
FT   MOD_RES     712    712       Phosphothreonine (By similarity).
FT   MOD_RES     713    713       Phosphoserine (By similarity).
FT   MOD_RES     714    714       Phosphoserine.
FT   MOD_RES     723    723       Phosphoserine.
FT   MOD_RES     725    725       Phosphoserine.
FT   MOD_RES     731    731       Phosphoserine.
FT   MOD_RES     733    733       Phosphoserine.
FT   MOD_RES     736    736       Phosphothreonine (By similarity).
FT   MOD_RES     743    743       Phosphoserine (By similarity).
FT   MOD_RES     745    745       Phosphothreonine (By similarity).
FT   MOD_RES     756    756       Phosphoserine (By similarity).
FT   MOD_RES     758    758       Phosphoserine (By similarity).
FT   MOD_RES     766    766       Phosphoserine.
FT   MOD_RES     768    768       Phosphothreonine.
FT   MOD_RES     779    779       Phosphoserine.
FT   MOD_RES     781    781       Phosphoserine.
FT   MOD_RES     784    784       Phosphoserine.
FT   MOD_RES     789    789       Phosphoserine (By similarity).
FT   MOD_RES     791    791       Phosphoserine (By similarity).
FT   MOD_RES     793    793       Phosphoserine.
FT   MOD_RES     795    795       Phosphoserine.
FT   MOD_RES     797    797       Phosphoserine.
FT   MOD_RES     810    810       Phosphoserine.
FT   MOD_RES     814    814       Phosphoserine.
FT   MOD_RES     816    816       Phosphoserine.
FT   MOD_RES     818    818       Phosphoserine (By similarity).
FT   MOD_RES     819    819       Phosphothreonine (By similarity).
FT   MOD_RES     822    822       Phosphoserine.
FT   MOD_RES     832    832       Phosphoserine.
FT   MOD_RES     834    834       Phosphothreonine (By similarity).
FT   MOD_RES     836    836       Phosphoserine (By similarity).
FT   MOD_RES     838    838       Phosphoserine (By similarity).
FT   MOD_RES     843    843       Phosphoserine (By similarity).
FT   MOD_RES     913    913       Phosphothreonine.
FT   MOD_RES     915    915       Phosphoserine.
FT   MOD_RES     936    936       Phosphoserine (By similarity).
FT   VAR_SEQ     733    755       Missing (in isoform 2).
FT                                /FTId=VSP_016524.
FT   VAR_SEQ     911    946       KETESEAEDDNLDDLERHLREKALRSMRKAQVSPQS -> E
FT                                VFTPPLPAV (in isoform 2).
FT                                /FTId=VSP_016525.
FT   CONFLICT    187    187       S -> Y (in Ref. 3; BAB25575).
FT   CONFLICT    521    521       H -> L (in Ref. 1; AAC17422).
FT   CONFLICT    851    851       K -> R (in Ref. 1; AAC17422).
SQ   SEQUENCE   946 AA;  106892 MW;  20238B1C882DD9CC CRC64;
     MDAGFFRGTS AEQDNRFSNK QKKLLKQLKF AECLEKKVDM SKVNLEVIKP WITKRVTEIL
     GFEDDVVIEF IFNQLEVKNP DSKMMQINLT GFLNGKNARE FMGELWPLLL SAQENIAGIP
     SAFLELKKEE IKQRQIEQEK LASLKKQDED KDKRDKEEKE SSREKRERSR SPRRRKSRSP
     SPRRRSSPVR RERKRSHSRS PRHRTKSRSP SPAPEKKEKS PELPEPSVRM KDSSVQEATS
     TSDILKAPKP EPVPEPKEPS PEKNSKKEKE KTRPRSRSRS KSRSRTRSRS PSHTRPRRRH
     RSRSRSYSPR RRPSPRRRPS PRRRTPPRRM PPPPRHRRSR SPGRRRRRSS ASLSGSSSSS
     SSSRSRSPPK KPPKRTSSPP RKTRRLSPSA SPPRRRHRPS SPATPPPKTR HSPTPQQSNR
     TRKSRVSVSP GRTSGKVTKH KGTEKRESPS PAPKPRKVEL SESEEDKGSK MAAADSVQQR
     RQYRRQNQQS SSDSGSSSTS EDERPKRSHV KNGEVGRRRR HSPSRSASPS PRKRQKETSP
     RMQMGKRWQS PVTKSSRRRR SPSPPPARRR RSPSPAPPPP PPPPPPRRRR SPTPPPRRRT
     PSPPPRRRSP SPRRYSPPIQ RRYSPSPPPK RRTASPPPPP KRRASPSPPP KRRVSHSPPP
     KQRSPTVTKR RSPSLSSKHR KGSSPGRSTR EARSPQPNKR HSPSPRPRAP QTSSPPPVRR
     GASASPQGRQ SPSPSTRPIR RVSRTPEPKK IKKAASPSTR PIRRVSRTPE PKKIKKAASP
     SPQSVRRVSS SRSVSGSPEP AAKKPPAPPS PVQSQSPSTN WSPAVPAKKA KSPTPSLSPA
     RNSDQEGGGK KKKKKKDKKH KKDKKHKKHK KHKKEKAVTI ATPATAAPAA VSAATTTSAQ
     EEPAAAPEPR KETESEAEDD NLDDLERHLR EKALRSMRKA QVSPQS
//
ID   Q52KJ6_MOUSE            Unreviewed;       469 AA.
AC   Q52KJ6;
DT   24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   24-MAY-2005, sequence version 1.
DT   08-MAR-2011, entry version 26.
DE   SubName: Full=Gpr123 protein;
DE   Flags: Fragment;
GN   Name=Gpr123;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC094311; AAH94311.1; -; mRNA.
DR   IPI; IPI00605298; -.
DR   UniGene; Mm.39863; -.
DR   STRING; Q52KJ6; -.
DR   Ensembl; ENSMUST00000026548; ENSMUSP00000026548; ENSMUSG00000025475.
DR   MGI; MGI:1277167; Gpr123.
DR   eggNOG; roNOG06129; -.
DR   HOVERGEN; HBG062926; -.
DR   InParanoid; Q52KJ6; -.
DR   OrthoDB; EOG4M65HR; -.
DR   ArrayExpress; Q52KJ6; -.
DR   Bgee; Q52KJ6; -.
DR   Genevestigator; Q52KJ6; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:InterPro.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR   Pfam; PF00002; 7tm_2; 1.
DR   PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Receptor; Transmembrane; Transmembrane helix.
FT   NON_TER       1      1
SQ   SEQUENCE   469 AA;  51401 MW;  16A6609CD33FDD97 CRC64;
     NIYKQVTKKA LPCPGADQPP YPKQPLLRFY LISGGVPFII CGVTAATNIR NYGTEDEDVA
     YCWMAWEPSL GAFYGPAAFI ALVTCVYFLC TYVQLRRHPE RRYELRERTE EQQRLAVPES
     GHRHGVRPGT PPTCDALAAS QLQNEHSFKA QLRAAAFTLF LFTATWTFGA LAVSQGHFLD
     MIFSCLYGAF CVTLGLFVLI HHCAKREDVW QCWWSCCPSR GDTSTTKPGA HPTLDANGDA
     LGHTACLQDS PCPGKLRGFG HPPASHCKMT NLQAAQGHVS CLSPATPCCA KMHCEQLMEE
     EAAHIHMAEE DVYPHDPHLH DPHLHRCLKG RTKSHYFSRH QAAAAEREYA YHIPSSLDGS
     PHSSRSESPT SSLEGPMGMH TLACCAQADP FPMVSQPEGG DTSPGLYGCP PHLSPGPAHL
     EMLRRTQSLP FGGPSQNGLL QGDVREGLPF GTDGTGNIRT GPWKNETTV
//
ID   LRIG2_MOUSE             Reviewed;        1054 AA.
AC   Q52KR2; Q69ZY8;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Leucine-rich repeats and immunoglobulin-like domains protein 2;
DE            Short=LIG-2;
DE   Flags: Precursor;
GN   Name=Lrig2; Synonyms=Kiaa0806;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein (By similarity). Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q52KR2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q52KR2-2; Sequence=VSP_014993;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 3 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SIMILARITY: Contains 16 LRR (leucine-rich) repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32308.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK173030; BAD32308.1; ALT_INIT; mRNA.
DR   EMBL; BC094228; AAH94228.1; -; mRNA.
DR   IPI; IPI00605095; -.
DR   IPI; IPI00649164; -.
DR   RefSeq; NP_001020238.1; NM_001025067.1.
DR   UniGene; Mm.34855; -.
DR   ProteinModelPortal; Q52KR2; -.
DR   SMR; Q52KR2; 41-493, 497-785.
DR   STRING; Q52KR2; -.
DR   PhosphoSite; Q52KR2; -.
DR   PRIDE; Q52KR2; -.
DR   Ensembl; ENSMUST00000046316; ENSMUSP00000035999; ENSMUSG00000032913.
DR   Ensembl; ENSMUST00000106793; ENSMUSP00000102405; ENSMUSG00000032913.
DR   GeneID; 269473; -.
DR   KEGG; mmu:269473; -.
DR   NMPDR; fig|10090.3.peg.8726; -.
DR   UCSC; uc008que.1; mouse.
DR   CTD; 269473; -.
DR   MGI; MGI:2443718; Lrig2.
DR   eggNOG; roNOG06371; -.
DR   GeneTree; ENSGT00600000084148; -.
DR   HOGENOM; HBG315254; -.
DR   HOVERGEN; HBG052353; -.
DR   InParanoid; Q52KR2; -.
DR   OMA; IWVIVIY; -.
DR   OrthoDB; EOG41NTKF; -.
DR   PhylomeDB; Q52KR2; -.
DR   NextBio; 392862; -.
DR   ArrayExpress; Q52KR2; -.
DR   Bgee; Q52KR2; -.
DR   Genevestigator; Q52KR2; -.
DR   GermOnline; ENSMUSG00000032913; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3.
DR   Pfam; PF07679; I-set; 3.
DR   Pfam; PF00560; LRR_1; 3.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 2.
DR   SMART; SM00369; LRR_TYP; 2.
DR   SMART; SM00082; LRRCT; 1.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS51450; LRR; 15.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Cytoplasm; Disulfide bond;
KW   Glycoprotein; Immunoglobulin domain; Leucine-rich repeat; Membrane;
KW   Phosphoprotein; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     39       Potential.
FT   CHAIN        40   1054       Leucine-rich repeats and immunoglobulin-
FT                                like domains protein 2.
FT                                /FTId=PRO_0000014830.
FT   TRANSMEM    807    827       Helical; (Potential).
FT   REPEAT       18     41       LRR 1.
FT   REPEAT       73     95       LRR 2.
FT   REPEAT       96    120       LRR 3.
FT   REPEAT      122    141       LRR 4.
FT   REPEAT      142    165       LRR 5.
FT   REPEAT      166    188       LRR 6.
FT   REPEAT      190    213       LRR 7.
FT   REPEAT      215    236       LRR 8.
FT   REPEAT      237    260       LRR 9.
FT   REPEAT      262    284       LRR 10.
FT   REPEAT      285    308       LRR 11.
FT   REPEAT      309    332       LRR 12.
FT   REPEAT      333    356       LRR 13.
FT   REPEAT      358    383       LRR 14.
FT   REPEAT      384    407       LRR 15.
FT   REPEAT      408    431       LRR 16.
FT   DOMAIN      497    596       Ig-like C2-type 1.
FT   DOMAIN      601    690       Ig-like C2-type 2.
FT   DOMAIN      695    784       Ig-like C2-type 3.
FT   MOD_RES     905    905       Phosphotyrosine (By similarity).
FT   MOD_RES     911    911       Phosphotyrosine (By similarity).
FT   CARBOHYD     90     90       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    120    120       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    172    172       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    188    188       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    273    273       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    440    440       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    467    467       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    513    513       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    570    570       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    588    588       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    686    686       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    727    727       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1024   1024       N-linked (GlcNAc...) (Potential).
FT   DISULFID    518    579       By similarity.
FT   DISULFID    622    674       By similarity.
FT   DISULFID    716    765       By similarity.
FT   VAR_SEQ      79    436       Missing (in isoform 2).
FT                                /FTId=VSP_014993.
FT   CONFLICT    843    849       Missing (in Ref. 1; BAD32308).
SQ   SEQUENCE   1054 AA;  117863 MW;  334B7250E2DF168E CRC64;
     MAAAPRGIWE QRRLGCGLGP LARLLILAQA LRLLPAARAG LCPAPCACRL PLLDCSRRKL
     PAPSWRALSG PLPSDISSLD LSHNRLSNWN NTLESQTLQE VKMNYNELTE IPYFGEPTPN
     ITLLSLVHNL IPEINAEAFE LYSALESLDL SSNIISEIKT SSFPRMSLKY LNLSNNRIST
     LEAGCFDNLS DSLLVVKLNR NRISMIPPKV FKLPHLQFLE LKRNRIKIVE GLTFQGLDSL
     RSLKMQRNGI SKLKDGAFFG LNNMEELELE HNNLTGVNKG WLYGLRMLQQ LYMSQNAIEK
     ISPDAWEFCQ RLSELDLSYN QLTRLDESAF VGLSLLERLN LGDNRVTHIA DGVFRFLSNL
     QTLDLRNNDI SWAIEDASEA FSGLKSLTKL ILQGNRIKSV TQKAFIGLES LEYLDLNNNA
     IMSIQENAFS QTHLKGLVLN TSSLLCDCHL KWLLQWLVDN NFHHSVNVSC AHPEWLAGQS
     ILNVDLKDFV CDDFLKPQIR THPESTIALR GVNVTLTCTA VSSSDSPMST IWRKDSEILY
     DVDIENFVRY RQQDGEALEY TSVLRLFSVN FTDEGKYQCI VTNHFGSNYS QKAKLTVNEM
     PSFLKTPMDL TIRTGAMARL ECAAEGHPTP QISWQKDGGT DFPAARERRM HVMPEDDVFF
     IANVKIEDMG IYSCMAQNIA GGLSANASLT VLETPSFIRP LEDKTVTRGE TAVLQCIAGG
     SPAPRLNWTK DDGPLLVTER HFFAAANQLL IIVDAGLEDA GKYTCLMSNT LGTERGHIYL
     NVISSPNCDS SQSSIGHEDD GWTTVGIVII VVVCCVVGTS LIWVIVIYHM RRKNEDYSIT
     NTEELNLPAD IPSYLSSQGT LSEPQEGYSN SEAGSHQQLM PPANGYTHRG TDGGAGTRVI
     CSDCYDNANI YSRTREYCPY TYIAEEDVLD QALSSLMVQM PKETFLSHPP QDAANLESLI
     PSAEREPAAF PTNHERMTEN LPFSQRSSEI FQRPLWNMNR ELGLLPFSQQ PVLESPELTE
     RDPNCSSPVT CRRLHDHAFD FSRTRIIQDG TEGT
//
ID   PRUN2_MOUSE             Reviewed;        3084 AA.
AC   Q52KR3; Q501M3; Q6A079; Q8BW65; Q8BYM6; Q9D217;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Protein prune homolog 2;
DE   AltName: Full=BNIP2 motif-containing molecule at the C-terminal region 1;
GN   Name=Prune2; Synonyms=Bmcc1, Kiaa0367;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 5), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2724-3084 (ISOFORM 6).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Hypothalamus, Oviduct, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1874-3084 (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Embryonic stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INDUCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=16288218; DOI=10.1038/sj.onc.1209225;
RA   Machida T., Fujita T., Ooo M.L., Ohira M., Isogai E., Mihara M.,
RA   Hirato J., Tomotsune D., Hirata T., Fujimori M., Adachi W.,
RA   Nakagawara A.;
RT   "Increased expression of proapoptotic BMCC1, a novel gene with the
RT   BNIP2 and Cdc42GAP homology (BCH) domain, is associated with favorable
RT   prognosis in human neuroblastomas.";
RL   Oncogene 25:1931-1942(2006).
CC   -!- FUNCTION: May play an important role in regulating
CC       differentiation, survival and aggressiveness of the tumor cells
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q52KR3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q52KR3-2; Sequence=VSP_022905, VSP_022906, VSP_022908;
CC       Name=3;
CC         IsoId=Q52KR3-3; Sequence=VSP_022905, VSP_022908;
CC       Name=4;
CC         IsoId=Q52KR3-4; Sequence=VSP_022905, VSP_039358;
CC       Name=5;
CC         IsoId=Q52KR3-5; Sequence=VSP_039356, VSP_039357;
CC       Name=6;
CC         IsoId=Q52KR3-6; Sequence=VSP_039358;
CC   -!- DEVELOPMENTAL STAGE: In the embryo specifically expressed in
CC       neural tube and neural crest-related tissues. At E10.5, highly
CC       expressed in neural tube and pharyngeal arches which are derived
CC       from neural crest. Expression is more restricted in the later
CC       stages of development. At E12.5, expressed in spinal cord,
CC       hindbrain, midbrain, forebrain and dorsal root ganglia (DRG).
CC       Although the expression at E14.5 is similar to those in E12.5, the
CC       regions expressing in hindbrain, spinal cord and forebrain at
CC       E14.5 are more dorsally restricted than at E12.5.
CC   -!- INDUCTION: Down-regulated after nerve growth factor (NGF)-induced
CC       differentiation, and up-regulated during the NGF-depletion-induced
CC       apoptosis.
CC   -!- SIMILARITY: Belongs to the PPase class C family. Prune subfamily.
CC   -!- SIMILARITY: Contains 1 CRAL-TRIO domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH94224.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAD32217.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC       Sequence=BAE41506.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; AK172939; BAD32217.1; ALT_INIT; mRNA.
DR   EMBL; AK020727; BAB32192.1; -; mRNA.
DR   EMBL; AK038997; BAC30198.1; -; mRNA.
DR   EMBL; AK054190; BAC35688.1; -; mRNA.
DR   EMBL; AK165582; BAE38273.1; -; mRNA.
DR   EMBL; AK170001; BAE41506.1; ALT_INIT; mRNA.
DR   EMBL; AC126674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC128703; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC147026; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC094224; AAH94224.1; ALT_INIT; mRNA.
DR   EMBL; BC095978; AAH95978.1; -; mRNA.
DR   IPI; IPI00313517; -.
DR   IPI; IPI00622823; -.
DR   IPI; IPI00761264; -.
DR   IPI; IPI00828778; -.
DR   IPI; IPI00874972; -.
DR   IPI; IPI00968392; -.
DR   RefSeq; NP_851993.3; NM_181348.4.
DR   UniGene; Mm.257354; -.
DR   UniGene; Mm.480716; -.
DR   ProteinModelPortal; Q52KR3; -.
DR   STRING; Q52KR3; -.
DR   PhosphoSite; Q52KR3; -.
DR   PRIDE; Q52KR3; -.
DR   Ensembl; ENSMUST00000044176; ENSMUSP00000044880; ENSMUSG00000039126.
DR   Ensembl; ENSMUST00000087689; ENSMUSP00000084977; ENSMUSG00000039126.
DR   Ensembl; ENSMUST00000099594; ENSMUSP00000097189; ENSMUSG00000039126.
DR   GeneID; 353211; -.
DR   KEGG; mmu:353211; -.
DR   UCSC; uc008gxg.1; mouse.
DR   CTD; 353211; -.
DR   MGI; MGI:1925004; Prune2.
DR   eggNOG; roNOG05278; -.
DR   GeneTree; ENSGT00420000029688; -.
DR   HOVERGEN; HBG081161; -.
DR   InParanoid; Q52KR3; -.
DR   OMA; EPSEIND; -.
DR   OrthoDB; EOG4XPQGH; -.
DR   ArrayExpress; Q52KR3; -.
DR   Bgee; Q52KR3; -.
DR   CleanEx; MM_A230083H22RIK; -.
DR   Genevestigator; Q52KR3; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   InterPro; IPR022181; Bcl2-/adenovirus-E1B.
DR   InterPro; IPR001251; CRAL-bd_TRIO_C.
DR   InterPro; IPR004097; DHHA2.
DR   Gene3D; G3DSA:3.40.525.10; CRAL_bd_TRIO_C; 1.
DR   Pfam; PF12496; BNIP2; 1.
DR   Pfam; PF00650; CRAL_TRIO; 1.
DR   Pfam; PF02833; DHHA2; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SUPFAM; SSF52087; CRAL_TRIO_C; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Apoptosis; Cytoplasm.
FT   CHAIN         1   3084       Protein prune homolog 2.
FT                                /FTId=PRO_0000274881.
FT   DOMAIN     2879   3040       CRAL-TRIO.
FT   MOTIF       109    111       DHH motif (By similarity).
FT   VAR_SEQ       1   2749       Missing (in isoform 2, isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_022905.
FT   VAR_SEQ     252    263       DYLLHGNITSDL -> VRKSGHSPLARG (in isoform
FT                                5).
FT                                /FTId=VSP_039356.
FT   VAR_SEQ     264   3084       Missing (in isoform 5).
FT                                /FTId=VSP_039357.
FT   VAR_SEQ    2893   2893       G -> GGDS (in isoform 2).
FT                                /FTId=VSP_022906.
FT   VAR_SEQ    3034   3075       KYDEEKSFKRSVRLDEELREASEAAKTSCLYNDPEMSSMEK
FT                                D -> N (in isoform 4 and isoform 6).
FT                                /FTId=VSP_039358.
FT   VAR_SEQ    3035   3046       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_022908.
FT   CONFLICT    132    132       E -> K (in Ref. 2; BAB32192).
FT   CONFLICT    146    146       S -> F (in Ref. 2; BAB32192).
FT   CONFLICT    156    156       A -> V (in Ref. 2; BAB32192).
FT   CONFLICT   2724   2724       M -> L (in Ref. 2; BAE41506).
FT   CONFLICT   2740   2740       L -> P (in Ref. 2; BAE41506).
FT   CONFLICT   2939   2939       A -> V (in Ref. 4; AAH95978).
SQ   SEQUENCE   3084 AA;  339516 MW;  FAF4C3D4DFC6893A CRC64;
     MEEFLQRAKS KLDRSKQLEQ VHAVIGPKSC DLDSLISAFT YAYFLDKVSP PGVLCLPVLN
     IPRTEFNYFT ETRFILEELN IPESFHIFRD EINLHQLNDE GKLSITLVGS HVLGSEDRTL
     ESAVVRVINP GEQSDGELGF PETSSSLVLK ELLREAPELI TQQLAHLLRG SILFTWMSMD
     PELPEKQEEI LSILEEQFPN LPPRDDIINV LQESQLSAQG LSLEQTMLKD LKELSDGEIK
     VAISTVNMTL EDYLLHGNIT SDLKAFTDKF GFDVLILISS FTWEEQQRQQ IAVYSQNLEL
     CSQICCELEE SQNPCLELEP FECGCDEILV YQQEDPSVTS DQVFLLLKEV INRRCAEMVS
     NSRTSSTEAV AGSAPLSQGS SGIMELYGSD IEPQPSSVNF IENPPELNDS NQAQADGNID
     LVSPDSGLAT IRSSRSSKES SVFLSDDSPV GDGGAPHHSL LPGFDSYSPI PEGIVAEEHA
     HSGEHSEHFD LFNFDSAPIA SEQSQPSSHS ADYSPEDDFP NSDSSEGNLS AGPKGLGEMG
     INMSNYSSSS LLSEAGKDSL VEFDEEFIQR QESSGDNSER NLSLTCFAGE EPSSPERLKN
     PGKMIPPTPM NSFVEISPSN EEPTPLYPED IIQNAIDTGH LGPPQARARC RSWWGGLEID
     SKNVVDTWNA SEQESVFQSP EPWKDPKPEP VERRTSDSTF QPKSLEFSKS DPWESEFGQP
     ELGNKEAQDQ KEESLQYQHL PTVRPHLTDA SPHGTNHLIE DFAALWHSGH SPTTMPEPWG
     NPTDAGEAAV TMSFPTWGAF DKEEDNADTL KNTWNLHPTN NETPSGQEPS EWAMGQSGFS
     FPAADLLDNP LIEVNKDAAP EIWGKNNSSK DTSLTSGSPT SDLGQTWNNS KLPGEDQNGL
     VDPKATGKVY EKEGSWSLFE ESAKKRGADV LAPWEDSFLS YKCSDYSASN IGEDSVPSPL
     DTNYSTSDSY TSPTYAGDEK EIANKPVDKD NGFEAKDAEF PAEGLEVLAT SSQQSQRNRI
     GSGPGNLDMW ALPHTEDKPE GNDAHHPDSD ALKTEHAEDK NASMEDDVRE SSPSSYDDPS
     MMRLYEANRQ LTLLHSNTNS RQAAPDSLDT WNRVTLEDTQ STATISDMDN DLDWDDCSGG
     VAISGDGQAE GYIAANSEPE TRFSVKQLEP WGTEHQEANQ VDWDLSASAE PTGDPGPSEY
     QTLNEKTGQL IANSIWDSVM GDKNMPSFRL PSPPNTVDME HGTWPSESPR HSNGKDSHML
     EASRLSESGG LTSQPVNQDT WGDSQGDTAS SVTGLASPEH FAQSDPWTGH TYGQSESEIE
     GLVASDCEHL DKEAALGSGV NGAPWAFGKK PRDQEFSSSD AFEHQDISSA SGKISSLSVT
     SSPQSEEPGE ALEVEKEPFI LDSLAVQTET FTWDLQSKDT HEESLVDHRN LGEANTTLDR
     INPMKNRPLS GMELEKTEAC TILKPERANG KLLYESSQDF GVWDGPMDSD VWDSHISYET
     AMNSTGQRTE ERSLEALSPG NYDRDSLSSG CTHSSASSPD LHDSSVALSS WTYGPSAEHQ
     KENHDDANKQ IHQESELFTT EAHVDVITEM KDFVENREDG FGKMSNQEDP QFPEIPNDPF
     NSGPSSSSSS LGADKYSEYS HAYQEGDLTT KRQEENELGF LEIVEPEGTR IISTSSGSGN
     DSGGDEELLE KELHLATVAQ SEAGACTSLH EPAFSATEHS KPEFSVFVGS LESIEKENKS
     SPFSDSQQSS PGQWILSPLM QADTQDTCKE ETRAAETGTM DTTWHGSAST EAKNGDPDKL
     EMLGFSADST EWWNAGAQEG RANAGMSAEE LSNSEGELEP TSPVFQNAGP WSLPIQNDSE
     PVDTGSTNPF RGKLKSPVLD SHGDKSQEKL WNIQPKQLDS DANQLSQLVI LDQMKDKDSG
     QQTAMSPAAG DLPAETLTQG QGRESMLSVW DRAEPALTHR DENGCVSTGV SPTECQQENQ
     WEPEKPYLSH VTHSSTPTEN ALESNAPTQL MRKLDSDWNS PSPSEPQHNF VPDILHGNFE
     EGGQLASASP DLWMDVKQPF SFKVDSENPD ILTHCDHDSN SQASSSPDVC HDSEGEQKME
     KHTAVYLGLE VEPSEFSLTE PNMNDEPTWE PEQESLPHNS ELHSEHAMPL PPIDSQNDIN
     NSSKPASSRS SPEPSDMRGD NNTSVTSMEE DTNPEVEAVD SVTIPGHFPR SEDADTFEAH
     QEVSVEVDDS WVSKDLCPES QTGTRALLDC EQPFASESPA VLTDIFLTSD TCLDVSEAAL
     DHSFSDASGL NTSTGTIDDM SKLTLSEGHP ETPVDGDAGK QDVCSSEASW GDFEYDAMGQ
     NIDEELMREP EHFLYGGDLP SEESALKQSL TPYTPPFDLS YLTEPTGCTE TAQGAESPGD
     ESLGSDAAEM LLSALPDHRE EDKAETNIRK PRYQMTVLHI HEDPEALSSP VGGTGSNNES
     SPSNIDWEIE TDNSDSPAGG DMKPPNGKEI LELEEDEKVI PTKGPKQTEL EYKEEKQPEQ
     SEDHQVLAVD YILVSHEKDS PLKPEAREAR ENIPELEQLS IGSRETGLPE TQLSGTPDTC
     QSEFLNDVKV HSAERMSSSS NHESASLENP AQDQSWMVLS HSEVGDPPTE TRDSGPESPG
     RTPEPFLSLS LDKGPKSQVL ERNKPLNSLA LEEVAGLSSQ SRNIERQGQA GLDAVPTQAA
     THDNEWEMLS PQLSRKNRNP PQEMEEETQC PEPGPRKPRL KGPPSEDEGM DIHFEEGVLS
     PSAADMRPEP PNSLDLNGSH PRRIKLTAPN INLSLDQSEG SILSDDNLDS PDEIDINVDE
     LDTPDEADSF EYTNHEDPTA NKSSGQESES IPEYTAEEER EDNRLWRTVV IGEQEQRIDM
     KVIEPYRRVI SHGGYYGDGL NAIIVFAACF LPDSSRADYH YVMENLFLYV ISTLELMVAE
     DYMIVYLNGA TPRRKMPGLG WMKKCYQMID RRLRKNLKSF IIVHPSWFIR TILAVTRPFI
     SSKFSSKIKY VTSLSELSGL IPMDCIHIPE SIIKYDEEKS FKRSVRLDEE LREASEAAKT
     SCLYNDPEMS SMEKDIDMKL KEKP
//
ID   Q542T4_MOUSE            Unreviewed;       154 AA.
AC   Q542T4;
DT   24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   24-MAY-2005, sequence version 1.
DT   08-FEB-2011, entry version 49.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Mbp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK079621; BAC37705.1; -; mRNA.
DR   IPI; IPI00223379; -.
DR   RefSeq; NP_001020427.1; NM_001025256.2.
DR   UniGene; Mm.252063; -.
DR   UniGene; Mm.454459; -.
DR   STRING; Q542T4; -.
DR   PRIDE; Q542T4; -.
DR   Ensembl; ENSMUST00000080658; ENSMUSP00000079488; ENSMUSG00000041607.
DR   Ensembl; ENSMUST00000152071; ENSMUSP00000115409; ENSMUSG00000041607.
DR   GeneID; 17196; -.
DR   KEGG; mmu:17196; -.
DR   UCSC; uc008ftx.1; mouse.
DR   CTD; 17196; -.
DR   MGI; MGI:96925; Mbp.
DR   GeneTree; ENSGT00390000014772; -.
DR   HOVERGEN; HBG008347; -.
DR   NextBio; 291554; -.
DR   PMAP-CutDB; Q542T4; -.
DR   ArrayExpress; Q542T4; -.
DR   Bgee; Q542T4; -.
DR   Genevestigator; Q542T4; -.
DR   GO; GO:0033269; C:internode region of axon; IDA:MGI.
DR   GO; GO:0043209; C:myelin sheath; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0019911; F:structural constituent of myelin sheath; IEA:InterPro.
DR   GO; GO:0042552; P:myelination; IDA:MGI.
DR   InterPro; IPR000548; Myelin_BP.
DR   PANTHER; PTHR11429; Myelin_BP; 1.
DR   Pfam; PF01669; Myelin_MBP; 2.
DR   PRINTS; PR00212; MYELINMBP.
DR   PROSITE; PS00569; MYELIN_MBP; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   154 AA;  17225 MW;  00F1F10ECF90421B CRC64;
     MASQKRPSQR SKYLATASTM DHARHGFLPR HRDTGILDSI GRFFSGDRGA PKRGSGKVPW
     LKQSRSPLPS HARSRPGLCH MYKDSHTRTT HYGSLPQKSQ HGRTQDENPV VHFFKNIVTP
     RTPPPSQGKG RGLSLSRFSW GGRDSRSGSP MARR
//
ID   Q547J4_MOUSE            Unreviewed;       372 AA.
AC   Q547J4;
DT   24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   24-MAY-2005, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   RecName: Full=Microtubule-associated protein;
GN   Name=Mapt; ORFNames=RP23-136D4.1-001, mCG_11217;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ISS, and ILS;
RX   MEDLINE=21363810; PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ISS, and ILS;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RA   Peck A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 4 Tau/MAP repeats.
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DR   EMBL; AF483518; AAL90792.1; -; mRNA.
DR   EMBL; AF483519; AAL90793.1; -; mRNA.
DR   EMBL; AL593843; CAM14796.1; -; Genomic_DNA.
DR   EMBL; CH466558; EDL34210.1; -; Genomic_DNA.
DR   IPI; IPI00331265; -.
DR   RefSeq; NP_034968.3; NM_010838.3.
DR   UniGene; Mm.1287; -.
DR   ProteinModelPortal; Q547J4; -.
DR   STRING; Q547J4; -.
DR   PRIDE; Q547J4; -.
DR   Ensembl; ENSMUST00000106992; ENSMUSP00000102605; ENSMUSG00000018411.
DR   GeneID; 17762; -.
DR   KEGG; mmu:17762; -.
DR   UCSC; uc007lwh.1; mouse.
DR   CTD; 17762; -.
DR   MGI; MGI:97180; Mapt.
DR   HOVERGEN; HBG000991; -.
DR   NextBio; 292453; -.
DR   ArrayExpress; Q547J4; -.
DR   Bgee; Q547J4; -.
DR   Genevestigator; Q547J4; -.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0035085; C:cilium axoneme; IDA:MGI.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:InterPro.
DR   InterPro; IPR002955; Tau_protein.
DR   InterPro; IPR001084; Tau_tubulin-bd.
DR   Pfam; PF00418; Tubulin-binding; 4.
DR   PRINTS; PR01261; TAUPROTEIN.
DR   PROSITE; PS00229; TAU_MAP_1; 4.
DR   PROSITE; PS51491; TAU_MAP_2; 4.
PE   2: Evidence at transcript level;
KW   Microtubule; Repeat.
SQ   SEQUENCE   372 AA;  38961 MW;  B9427D315AD962B7 CRC64;
     MADPRQEFDT MEDHAGDYTL LQDQEGDMDH GLKAEEAGIG DTPNQEDQAA GHVTQARVAS
     KDRTGNDEKK AKGADGKTGA KIATPRGAAS PAQKGTSNAT RIPAKTTPSP KTPPGSGEPP
     KSGERSGYSS PGSPGTPGSR SRTPSLPTPP TREPKKVAVV RTPPKSPSAS KSRLQTAPVP
     MPDLKNVRSK IGSTENLKHQ PGGGKVQIIN KKLDLSNVQS KCGSKDNIKH VPGGGSVQIV
     YKPVDLSKVT SKCGSLGNIH HKPGGGQVEV KSEKLDFKDR VQSKIGSLDN ITHVPGGGNK
     KIETHKLTFR ENAKAKTDHG AEIVYKSPVV SGDTSPRHLS NVSSTGSIDM VDSPQLATLA
     DEVSASLAKQ GL
//
ID   TR150_MOUSE             Reviewed;         951 AA.
AC   Q569Z6;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Thyroid hormone receptor-associated protein 3;
DE   AltName: Full=Thyroid hormone receptor-associated protein complex 150 kDa component;
DE            Short=Trap150;
GN   Name=Thrap3; Synonyms=Trap150;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Head;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-572, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-572 AND SER-935, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248 AND SER-253, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248; SER-253; SER-315;
RP   SER-320; THR-324; SER-679; SER-924; SER-935 AND THR-937, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243 AND SER-679, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-53; SER-55;
RP   SER-264; SER-268; SER-315; SER-320; SER-403; SER-405; SER-572; SER-860
RP   AND SER-924, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; SER-134; SER-238;
RP   SER-243; SER-248; SER-379; SER-572; SER-679; SER-695 AND SER-924, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243; SER-248; SER-253;
RP   SER-572 AND SER-679, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Plays a role in transcriptional coactivation (By
CC       similarity).
CC   -!- SUBUNIT: Subunit of the large multiprotein complex TRAP (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -----------------------------------------------------------------------
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DR   EMBL; BC092239; AAH92239.1; -; mRNA.
DR   IPI; IPI00556768; -.
DR   RefSeq; NP_666265.3; NM_146153.3.
DR   UniGene; Mm.236211; -.
DR   UniGene; Mm.29813; -.
DR   ProteinModelPortal; Q569Z6; -.
DR   STRING; Q569Z6; -.
DR   PhosphoSite; Q569Z6; -.
DR   PRIDE; Q569Z6; -.
DR   Ensembl; ENSMUST00000080919; ENSMUSP00000079722; ENSMUSG00000043962.
DR   GeneID; 230753; -.
DR   KEGG; mmu:230753; -.
DR   UCSC; uc008usv.1; mouse.
DR   CTD; 230753; -.
DR   MGI; MGI:2442637; Thrap3.
DR   HOGENOM; HBG279030; -.
DR   HOVERGEN; HBG054554; -.
DR   InParanoid; Q569Z6; -.
DR   OMA; KMKEKGS; -.
DR   OrthoDB; EOG4NKBVJ; -.
DR   NextBio; 380111; -.
DR   ArrayExpress; Q569Z6; -.
DR   Bgee; Q569Z6; -.
DR   CleanEx; MM_THRAP3; -.
DR   Genevestigator; Q569Z6; -.
DR   GermOnline; ENSMUSG00000043962; Mus musculus.
DR   GO; GO:0016592; C:mediator complex; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; ATP-binding; Methylation; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Receptor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    951       Thyroid hormone receptor-associated
FT                                protein 3.
FT                                /FTId=PRO_0000235980.
FT   NP_BIND     549    556       ATP (Potential).
FT   COMPBIAS      7    339       Ser-rich.
FT   COMPBIAS     12    161       Arg-rich.
FT   MOD_RES       2      2       Phosphoserine (By similarity).
FT   MOD_RES      17     17       Dimethylated arginine (By similarity).
FT   MOD_RES      51     51       Phosphoserine.
FT   MOD_RES      53     53       Phosphoserine.
FT   MOD_RES      55     55       Phosphoserine.
FT   MOD_RES     119    119       Phosphoserine.
FT   MOD_RES     134    134       Phosphoserine.
FT   MOD_RES     207    207       Phosphoserine (By similarity).
FT   MOD_RES     211    211       Phosphoserine (By similarity).
FT   MOD_RES     221    221       N6-acetyllysine (By similarity).
FT   MOD_RES     233    233       Phosphoserine (By similarity).
FT   MOD_RES     238    238       Phosphoserine.
FT   MOD_RES     240    240       Phosphoserine (By similarity).
FT   MOD_RES     243    243       Phosphoserine.
FT   MOD_RES     248    248       Phosphoserine.
FT   MOD_RES     253    253       Phosphoserine.
FT   MOD_RES     264    264       Phosphoserine.
FT   MOD_RES     268    268       Phosphoserine.
FT   MOD_RES     310    310       Phosphoserine (By similarity).
FT   MOD_RES     315    315       Phosphoserine.
FT   MOD_RES     320    320       Phosphoserine.
FT   MOD_RES     324    324       Phosphothreonine.
FT   MOD_RES     328    328       Phosphotyrosine (By similarity).
FT   MOD_RES     379    379       Phosphoserine.
FT   MOD_RES     398    398       N6-acetyllysine (By similarity).
FT   MOD_RES     403    403       Phosphoserine.
FT   MOD_RES     405    405       Phosphoserine.
FT   MOD_RES     452    452       N6-acetyllysine (By similarity).
FT   MOD_RES     505    505       Phosphoserine (By similarity).
FT   MOD_RES     516    516       N6-acetyllysine (By similarity).
FT   MOD_RES     531    531       Phosphoserine (By similarity).
FT   MOD_RES     532    532       Phosphoserine (By similarity).
FT   MOD_RES     559    559       Phosphoserine (By similarity).
FT   MOD_RES     572    572       Phosphoserine.
FT   MOD_RES     669    669       Phosphoserine (By similarity).
FT   MOD_RES     679    679       Phosphoserine.
FT   MOD_RES     681    681       Phosphoserine (By similarity).
FT   MOD_RES     682    682       Phosphothreonine (By similarity).
FT   MOD_RES     695    695       Phosphoserine.
FT   MOD_RES     706    706       N6-acetyllysine (By similarity).
FT   MOD_RES     808    808       N6-acetyllysine (By similarity).
FT   MOD_RES     829    829       Phosphothreonine (By similarity).
FT   MOD_RES     860    860       Phosphoserine.
FT   MOD_RES     924    924       Phosphoserine.
FT   MOD_RES     935    935       Phosphoserine.
FT   MOD_RES     937    937       Phosphothreonine.
SQ   SEQUENCE   951 AA;  108178 MW;  40DF483027363B4E CRC64;
     MSKTNKSKSG SRSSRSRSAS RSRSRSFSKS RSRSRSVSRS RKRRLSSRSR SRSYSPAHNR
     ERNHPRVYQN RDFRGHNRGY RRPYYFRGRN RGFYPWGQYN RGGYGNYRSN WQNYRQAYSP
     RRGRSRSRSP KRRSPSPRSR SHSRNSDKSS SDRSRRSSSS RSSSNHSRVE SSKRKSTKEK
     KSSSKDSRPS QAAGDNQGDE AKEQTFSGGT SQDIKGSESS KPWPDATTYG AGSASRASVS
     DLSPRERSPA LKSPLQSVVV RRRSPRPSPV PKPSPPLSNA SQMGSSMSGG AGYQSGAHQG
     QFDHGSGSLS PSKKSPVGKS PPATGSAYGS SQKEESAASG GAAYSKRYLE EQKTENGKDK
     EQKQTNADKE KLKEKGGFSD ADVKMKSDPF APKTDSEKPF RGSQSPKRYK LRDDFEKKMA
     DFHKEELDEH DKDKSKGRKE PEFDDEPKFM SKVIAGASKN QEEEKSGKWE SLHTGKEKQR
     KAEEMEDEPF TERSRKEERG GSKRSESGHR GFVPEKNFRV TAYKAVQEKS SSPPPRKTSE
     SRDKLGSKGD FSSGKSSFSI TREAQVNVRM DSFDEDLARP SGLLAQERKL CRDLVHSNKK
     EQEFRSIFQH IQSAQSQRSP SELFAQHIVT IVHHVKEHHF GSSGMTLHER FTKYLKRGNE
     QEAAKNKKSP EIHRRIDISP STFRKHGLTH EELKSPREPG YKAEGKYKDD PVDLRLDIER
     RKKHKERDLK RGKSRESVDS RDSSHSRERS TEKTEKTHKG SKKQKKHRRA RDRSRSSSSS
     SQSSHSYKAE EYPEEAEERE ESTSGFDKSR LGTKDFVGPN ERGGRARGTF QFRARGRGWG
     RGNYSGNNNN NSNNDFQKRS REEEWDPEYT PKSKKYYLHD DREGEGSDKW MGRGRGRGAF
     PRGRGRFMFR KSSTSPKWAH DKFSGEEGEI EDDESGTENR EEKDSLQPSA E
//
ID   SCN2B_MOUSE             Reviewed;         215 AA.
AC   Q56A07;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Sodium channel subunit beta-2;
DE   Flags: Precursor;
GN   Name=Scn2b; Synonyms=Gm183;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 99-107, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Crucial in the assembly, expression, and functional
CC       modulation of the heterotrimeric complex of the sodium channel.
CC       The subunit beta-2 causes an increase in the plasma membrane
CC       surface area and in its folding into microvilli. Interacts with
CC       TNR may play a crucial role in clustering and regulation of
CC       activity of sodium channels at nodes of Ranvier (By similarity).
CC   -!- SUBUNIT: The sodium channel consists of a pore-forming alpha
CC       subunit, beta-1 and beta-2 subunits. Beta-1 is non-covalently
CC       associated with alpha, while beta-2 is covalently linked by
CC       disulfide bonds. Interaction with SCN10A and TNR (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Belongs to the sodium channel auxiliary subunit SCN2B
CC       (TC 8.A.17) family.
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
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CC   -----------------------------------------------------------------------
DR   EMBL; BC092225; AAH92225.1; -; mRNA.
DR   IPI; IPI00356063; -.
DR   RefSeq; NP_001014761.1; NM_001014761.2.
DR   UniGene; Mm.229373; -.
DR   UniGene; Mm.477575; -.
DR   ProteinModelPortal; Q56A07; -.
DR   SMR; Q56A07; 36-151.
DR   STRING; Q56A07; -.
DR   PhosphoSite; Q56A07; -.
DR   PRIDE; Q56A07; -.
DR   Ensembl; ENSMUST00000093855; ENSMUSP00000091377; ENSMUSG00000070304.
DR   GeneID; 72821; -.
DR   KEGG; mmu:72821; -.
DR   UCSC; uc009pfg.1; mouse.
DR   CTD; 72821; -.
DR   MGI; MGI:106921; Scn2b.
DR   GeneTree; ENSGT00530000062830; -.
DR   HOGENOM; HBG716687; -.
DR   HOVERGEN; HBG003443; -.
DR   InParanoid; Q56A07; -.
DR   OMA; EEMFLQF; -.
DR   OrthoDB; EOG402WTM; -.
DR   NextBio; 336983; -.
DR   ArrayExpress; Q56A07; -.
DR   Bgee; Q56A07; -.
DR   CleanEx; MM_SCN2B; -.
DR   Genevestigator; Q56A07; -.
DR   GermOnline; ENSMUSG00000070304; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR021157; Cyt_c1_TM_anchor_C.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR000920; Myelin_P0.
DR   Gene3D; G3DSA:1.20.5.100; Cyt_c1_TM_anchor_C; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF07686; V-set; 1.
DR   PRINTS; PR00213; MYELINP0.
DR   SMART; SM00409; IG; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Ion transport; Ionic channel; Membrane; Signal;
KW   Sodium; Sodium channel; Sodium transport; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   SIGNAL        1     29       By similarity.
FT   CHAIN        30    215       Sodium channel subunit beta-2.
FT                                /FTId=PRO_0000045177.
FT   TOPO_DOM     30    159       Extracellular (Potential).
FT   TRANSMEM    160    180       Helical; (Potential).
FT   TOPO_DOM    181    215       Cytoplasmic (Potential).
FT   DOMAIN       32    154       Ig-like C2-type.
FT   CARBOHYD     42     42       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     66     66       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     74     74       N-linked (GlcNAc...) (Potential).
FT   DISULFID     55    127       Potential.
SQ   SEQUENCE   215 AA;  24228 MW;  38C1687665924FD7 CRC64;
     MHRDAWLPRP AFSLTGLSLF FSLVPPGRSM EVTAPTTLSV LNGSDTRLPC TFNSCYTVNH
     KQFSLNWTYQ ECNNCTEEMF LQFRMKIINL KLERFGDRVE FSGNPSKYDV SVTLKNVQLE
     DEGIYNCYIT NPPDRHRGHG KIYLQVLLEV PPERDSTVAV IVGASVGGFL AVVILVLMVV
     KCVRRKKEQK LSTDDLKTEE EGKMDGEGNA EDGTK
//
ID   GPKOW_MOUSE             Reviewed;         488 AA.
AC   Q56A08; A0JLW7; A2AEU7; Q6P5V0; Q8C1C3;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   08-MAR-2011, entry version 41.
DE   RecName: Full=G patch domain and KOW motifs-containing protein;
DE   AltName: Full=Protein MOS2 homolog;
GN   Name=Gpkow;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-488.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION.
RX   PubMed=16271871; DOI=10.1016/j.cub.2005.09.038;
RA   Zhang Y., Cheng Y.T., Bi D., Palma K., Li X.;
RT   "MOS2, a protein containing G-patch and KOW motifs, is essential for
RT   innate immunity in Arabidopsis thaliana.";
RL   Curr. Biol. 15:1936-1942(2005).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the MOS2 family.
CC   -!- SIMILARITY: Contains 1 G-patch domain.
CC   -!- SIMILARITY: Contains 2 KOW domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH92224.2; Type=Erroneous initiation;
CC       Sequence=AAI20680.1; Type=Erroneous initiation;
CC       Sequence=AAI25336.1; Type=Erroneous initiation;
CC       Sequence=BAC25949.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK028433; BAC25949.1; ALT_INIT; mRNA.
DR   EMBL; AL671995; CAM13581.1; -; Genomic_DNA.
DR   EMBL; BC062646; AAH62646.1; -; mRNA.
DR   EMBL; BC092224; AAH92224.2; ALT_INIT; mRNA.
DR   EMBL; BC120679; AAI20680.1; ALT_INIT; mRNA.
DR   EMBL; BC125335; AAI25336.1; ALT_INIT; mRNA.
DR   IPI; IPI00309815; -.
DR   RefSeq; NP_776108.2; NM_173747.3.
DR   UniGene; Mm.148753; -.
DR   ProteinModelPortal; Q56A08; -.
DR   SMR; Q56A08; 363-479.
DR   PhosphoSite; Q56A08; -.
DR   PRIDE; Q56A08; -.
DR   Ensembl; ENSMUST00000049896; ENSMUSP00000076178; ENSMUSG00000031148.
DR   GeneID; 209416; -.
DR   KEGG; mmu:209416; -.
DR   UCSC; uc009sma.1; mouse.
DR   CTD; 209416; -.
DR   MGI; MGI:1859610; Gpkow.
DR   eggNOG; roNOG11383; -.
DR   GeneTree; ENSGT00390000015154; -.
DR   HOGENOM; HBG283647; -.
DR   HOVERGEN; HBG080241; -.
DR   InParanoid; Q56A08; -.
DR   OMA; SFGFSRT; -.
DR   NextBio; 372663; -.
DR   ArrayExpress; Q56A08; -.
DR   Bgee; Q56A08; -.
DR   CleanEx; MM_GPKOW; -.
DR   Genevestigator; Q56A08; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   InterPro; IPR000467; G_patch.
DR   InterPro; IPR005824; KOW.
DR   Pfam; PF01585; G-patch; 1.
DR   Pfam; PF00467; KOW; 1.
DR   SMART; SM00443; G_patch; 1.
DR   SMART; SM00739; KOW; 2.
DR   PROSITE; PS50174; G_PATCH; 1.
PE   2: Evidence at transcript level;
KW   Nucleus; Repeat.
FT   CHAIN         1    488       G patch domain and KOW motifs-containing
FT                                protein.
FT                                /FTId=PRO_0000280563.
FT   DOMAIN      164    210       G-patch.
FT   DOMAIN      231    258       KOW 1.
FT   DOMAIN      401    428       KOW 2.
SQ   SEQUENCE   488 AA;  53832 MW;  BCF1E648CA7CDD4B CRC64;
     MAGRESPPPS APSMAPISFG FTRTSVRRRL ADLGDSERQA PEEKDFLATV EGRKLQSVNP
     PEAPKELVIP LIQNGSRRQP LSKNPKPSSE TSTVLMSDGV LSQAVKELIE ESKKSLEERE
     NAGVDPTLTI PMIQKGCTPI EEGSDSEPQA ETVPEEADYE AVPVEAYGLA MLRGMGWKPG
     KGIGNTFSQV VKPRVNSIRP KGLGLGANRM EAQDLASVGS HHPPRPDGDR ENDKEGQPQG
     LMHGRAVVVL SGPYRGLYGK VEGLDPDNVR AMVRLAVGNR IVTVSEYCLR PVSQQEFDSH
     TSKPGHVSQT STEQQNRATG TASSLKAAQN QEDSKRRQKG SEKKRKHSPD RQDGPVPKTE
     KAAPRNKHWL HRDLRVRFID KLHKSGRYYN TKMTIEDVLS PDTCVCRTDE GRVLEDVRED
     MLETLIPKGE GHRVMVVLGP HAGKVGLLRS RDRAQSHALV QLRRENQVVE LHYNAICQYM
     GPGDSDED
//
ID   ZN608_MOUSE             Reviewed;        1511 AA.
AC   Q56A10; Q6ZPU8; Q8BIG5; Q8BJ06;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   RecName: Full=Zinc finger protein 608;
GN   Name=Znf608; Synonyms=Kiaa1281, Zfp608;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 861-1511 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, and FVB/N-3; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1260-1511 (ISOFORM 2).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q56A10-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q56A10-2; Sequence=VSP_023667, VSP_023668;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q56A10-3; Sequence=VSP_023665, VSP_023666;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 C2H2-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC36234.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK047979; BAC33204.1; -; mRNA.
DR   EMBL; AK076178; BAC36234.1; ALT_INIT; mRNA.
DR   EMBL; BC092219; AAH92219.1; -; mRNA.
DR   EMBL; AK129321; BAC98131.1; -; mRNA.
DR   IPI; IPI00460711; -.
DR   IPI; IPI00469437; -.
DR   IPI; IPI00830242; -.
DR   RefSeq; NP_786927.2; NM_175751.4.
DR   UniGene; Mm.192984; -.
DR   STRING; Q56A10; -.
DR   PhosphoSite; Q56A10; -.
DR   PRIDE; Q56A10; -.
DR   Ensembl; ENSMUST00000064763; ENSMUSP00000068192; ENSMUSG00000052713.
DR   GeneID; 269023; -.
DR   KEGG; mmu:269023; -.
DR   UCSC; uc008eyc.1; mouse.
DR   CTD; 269023; -.
DR   MGI; MGI:2442338; Zfp608.
DR   HOGENOM; HBG717404; -.
DR   HOVERGEN; HBG054557; -.
DR   InParanoid; Q56A10; -.
DR   OMA; RKNKPPM; -.
DR   OrthoDB; EOG4PRSPV; -.
DR   NextBio; 392648; -.
DR   ArrayExpress; Q56A10; -.
DR   Bgee; Q56A10; -.
DR   CleanEx; MM_ZFP608; -.
DR   Genevestigator; Q56A10; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   SMART; SM00355; ZnF_C2H2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Metal-binding; Phosphoprotein;
KW   Zinc; Zinc-finger.
FT   CHAIN         1   1511       Zinc finger protein 608.
FT                                /FTId=PRO_0000280421.
FT   ZN_FING     552    577       C2H2-type.
FT   COILED      277    303       Potential.
FT   COMPBIAS    140    263       Gly-rich.
FT   COMPBIAS    309    314       Poly-Pro.
FT   COMPBIAS    440    443       Poly-Ala.
FT   MOD_RES     626    626       Phosphoserine (By similarity).
FT   MOD_RES     635    635       Phosphothreonine (By similarity).
FT   MOD_RES     870    870       Phosphoserine (By similarity).
FT   VAR_SEQ     388    423       VLVVNVTWRNKTYVGTLLDCTKHDWAPPRFCESPTS -> K
FT                                YVLFLFISLCPLLHDVSLSICEGNLFSLWFERIER (in
FT                                isoform 3).
FT                                /FTId=VSP_023665.
FT   VAR_SEQ     424   1511       Missing (in isoform 3).
FT                                /FTId=VSP_023666.
FT   VAR_SEQ    1432   1455       PVEKASTEREREAERERDRHSPFS -> VSLLLLVVKRPCL
FT                                VGEGRQETEQS (in isoform 2).
FT                                /FTId=VSP_023667.
FT   VAR_SEQ    1456   1511       Missing (in isoform 2).
FT                                /FTId=VSP_023668.
FT   CONFLICT    931    932       AK -> PN (in Ref. 1; BAC36234).
FT   CONFLICT    987    987       Q -> H (in Ref. 1; BAC36234).
FT   CONFLICT   1039   1039       K -> N (in Ref. 1; BAC36234).
FT   CONFLICT   1436   1436       A -> G (in Ref. 1; BAC36234).
FT   CONFLICT   1449   1449       D -> G (in Ref. 1; BAC36234).
FT   CONFLICT   1490   1490       V -> G (in Ref. 1; BAC36234).
SQ   SEQUENCE   1511 AA;  162345 MW;  4331F1298053D5AC CRC64;
     MSVNVSTAGK GVDPNTVDTY DSGDDWEIGV GNLIIDLDAD LEKDRQKFEM NNSTNTTTNT
     TKDCGGPASN GTCSTSALAD GLKFASVQPS APQGNSHKET SKSKVKRAKT SKDANKSLPS
     AALYGIPEIS STGKRQEVQG RPGEATGMNS ALGQSVSGGG SSNPNSNGTS TGTSAATAGA
     GSCGKSKEEK PGKSHSSRGA KRDKDAARSR KEKHDLLQGH QNGGGGQAPS GGHLYGFGTK
     SNGSGASPFH CGGAGSGSVG AAGEVSKTAP DSTLMGNSML VKKEEEEEES HRRIKKLKTE
     KVDPLFTVPA PPPPIASSLA PQIPPSYFPP SSSNIAAPVE QLLVRTRSVG VNTCEVGVVT
     EPECLGPCEP GTSVNLEGIV WHETEEGVLV VNVTWRNKTY VGTLLDCTKH DWAPPRFCES
     PTSDLEMRGG RGRGKRARSA AAAPGSEVSF TESRGLQSKN RGGANGKGRR GSLNASGRRT
     PPNCAAEDIK ASPSSTNKRK NKPPMELDLN SSSEDSKPGK RVRTNSRSTP TTPQGKPETT
     FLDQGCSSPV LIDCPHPNCN KKYKHINGLR YHQAHAHLDP ENKLEFEPDS EDKISDCEEA
     LSNVALECNE SSTSVSSYDQ TKAPGSPGAG NPPGTPKGKR EHVSNGPGPI IGSKTGKNSG
     KKRGLNNELN NLPVISNMTA ALDICSATDS NLTAEMPKLE AEGLIDKKSL GDKEKGKKAN
     NCKMDKNLSK LKSARPIAPA PAPTPPQLIA IPTAAFTSTT TGTIPGLPSL TTTVVQATPK
     SPPLKPIQPK PTIMGEPITV NPALVSLKDR KKKEKRKLKD KEGKETGGPK MDAKLGKLEE
     AKAASKDLSG HFLKDHLGKS EGLANGLSES QESRMASIKA EADKVYTFTD NAPSPSIGSA
     SRMECSTLVN GQAPMAPLHV LTQNGAESAA AKTSSPAYSD ISDAADDGGS DSRSEGMRSK
     ASSPSDTFSN KDGVVKGHPS TSAQPSQLKE SHSPYYHGYE PYYSPSYMHP GQVGAPAAGN
     GGSTQGMKIK KESEEDAEKK DKAEQLESKK VDHTSAPLQP QHQSVITQRH PALAQSLYYG
     QYAYGLYMDQ KSLMATSPAY RQQYEKYYED QRLAEQKMAQ SGRGDCERKA ELPLKELGKE
     DNKQKNMPSA TISKAPSTPE PNKNHSKLGP SVPNKTEETG KSQLLSSHQQ QLQADSFKAK
     QMENHQLIKE AVEMKSVMDS MKQTGVDPTS RFKQDPESRT WHHYVYQPKY LDQQKPEELD
     REKKLKEDSP RKTPNKESGV SSLPVSLTNI KEEPKEGKRP DSQSVEENKL KNDDRKTPVN
     WKDSRGTRVA VSSPMSQHQS YIQYLHAYPY PQMYDPSHPA YRAVSPVLMH SYPGAYLSPG
     FHYPVYGKMS GREEAEKVNT SPSINTKTAS EAKALDLLQH HANQYRSKSP APVEKASTER
     EREAERERDR HSPFSQRHLH THHHTHVGMG YPLIPGQYDP FQGLTSAALV ASQQVAAQAS
     ASGMFPAQRR E
//
ID   DPTOR_MOUSE             Reviewed;         409 AA.
AC   Q570Y9; Q3UM00; Q3UT08;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=DEP domain-containing mTOR-interacting protein;
DE   AltName: Full=DEP domain-containing protein 6;
GN   Name=Deptor; Synonyms=Depdc6, Kiaa4200;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Pancreatic islet;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Seino S., Nishimura M.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Egg, and Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235; SER-238 AND
RP   SER-287, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Negative regulator of the mTORC1 and mTORC2 signaling
CC       pathways. Inhibits the kinase activity of both complexes (By
CC       similarity).
CC   -!- SUBUNIT: Interacts (via PDZ domain) with MTOR; interacts with MTOR
CC       within both mammalian target of rapamycin complexes mTORC1 and
CC       mTORC2 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q570Y9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q570Y9-2; Sequence=VSP_024648;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q570Y9-3; Sequence=VSP_024649;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylation weakens interaction with MTOR within mTORC1
CC       and mTORC2 (By similarity).
CC   -!- SIMILARITY: Contains 2 DEP domains.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90225.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; AK220300; BAD90225.1; ALT_INIT; mRNA.
DR   EMBL; AK139888; BAE24172.1; -; mRNA.
DR   EMBL; AK145208; BAE26298.1; -; mRNA.
DR   IPI; IPI00652239; -.
DR   IPI; IPI00652416; -.
DR   IPI; IPI00749646; -.
DR   RefSeq; NP_001033026.1; NM_001037937.2.
DR   RefSeq; NP_663445.2; NM_145470.2.
DR   UniGene; Mm.295397; -.
DR   UniGene; Mm.393497; -.
DR   HSSP; Q9WV48; 1Q3O.
DR   ProteinModelPortal; Q570Y9; -.
DR   SMR; Q570Y9; 33-121, 137-223, 327-405.
DR   PhosphoSite; Q570Y9; -.
DR   PRIDE; Q570Y9; -.
DR   Ensembl; ENSMUST00000023056; ENSMUSP00000023056; ENSMUSG00000022419.
DR   Ensembl; ENSMUST00000096433; ENSMUSP00000094167; ENSMUSG00000022419.
DR   Ensembl; ENSMUST00000100660; ENSMUSP00000098225; ENSMUSG00000022419.
DR   GeneID; 97998; -.
DR   KEGG; mmu:97998; -.
DR   UCSC; uc007vrz.1; mouse.
DR   CTD; 97998; -.
DR   MGI; MGI:2146322; Deptor.
DR   eggNOG; roNOG09182; -.
DR   GeneTree; ENSGT00520000055667; -.
DR   HOGENOM; HBG444411; -.
DR   HOVERGEN; HBG056008; -.
DR   InParanoid; Q570Y9; -.
DR   OMA; ESHDSPF; -.
DR   OrthoDB; EOG4CNQRD; -.
DR   NextBio; 353230; -.
DR   ArrayExpress; Q570Y9; -.
DR   Bgee; Q570Y9; -.
DR   CleanEx; MM_DEPDC6; -.
DR   Genevestigator; Q570Y9; -.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2.
DR   Pfam; PF00610; DEP; 2.
DR   SMART; SM00049; DEP; 2.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50186; DEP; 2.
DR   PROSITE; PS50106; PDZ; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Phosphoprotein; Repeat.
FT   CHAIN         1    409       DEP domain-containing mTOR-interacting
FT                                protein.
FT                                /FTId=PRO_0000284785.
FT   DOMAIN       36    119       DEP 1.
FT   DOMAIN      146    219       DEP 2.
FT   DOMAIN      330    407       PDZ.
FT   COMPBIAS    235    299       Ser-rich.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     235    235       Phosphoserine.
FT   MOD_RES     238    238       Phosphoserine.
FT   MOD_RES     241    241       Phosphothreonine (By similarity).
FT   MOD_RES     244    244       Phosphoserine (By similarity).
FT   MOD_RES     258    258       Phosphoserine (By similarity).
FT   MOD_RES     259    259       Phosphothreonine (By similarity).
FT   MOD_RES     263    263       Phosphoserine (By similarity).
FT   MOD_RES     265    265       Phosphoserine (By similarity).
FT   MOD_RES     282    282       Phosphoserine (By similarity).
FT   MOD_RES     283    283       Phosphoserine (By similarity).
FT   MOD_RES     287    287       Phosphoserine.
FT   MOD_RES     293    293       Phosphoserine (By similarity).
FT   MOD_RES     297    297       Phosphoserine (By similarity).
FT   MOD_RES     298    298       Phosphoserine (By similarity).
FT   MOD_RES     299    299       Phosphoserine (By similarity).
FT   VAR_SEQ       1     40       MEEGSSGGSGSSDSNAGGSGGVQQRELERMAEVLVTGEQL
FT                                -> MKQAFLVVLRHSISEDRLPPLSVITSGC (in
FT                                isoform 2).
FT                                /FTId=VSP_024648.
FT   VAR_SEQ     368    409       VCQFVVSVNGLNVLNVDYRTVSNLILTGPRTIVMEVMEELD
FT                                C -> DTGTESRKIVTSRLAWATWQDLMGGKVGGDAIPI
FT                                (in isoform 3).
FT                                /FTId=VSP_024649.
FT   CONFLICT     11     11       S -> G (in Ref. 2; BAE26298).
FT   CONFLICT    125    125       A -> P (in Ref. 2; BAE26298).
FT   CONFLICT    128    128       S -> N (in Ref. 2; BAE26298).
FT   CONFLICT    149    149       T -> I (in Ref. 2; BAE26298).
SQ   SEQUENCE   409 AA;  46120 MW;  072062418DADDF8E CRC64;
     MEEGSSGGSG SSDSNAGGSG GVQQRELERM AEVLVTGEQL RLRLHEEKVI KDRRHHLKTY
     PNCFVAKELI DWLIEHKEAS DRETAIKLMQ KLADRGIIHH VCDEHKEFKD VKLFYRFRKD
     DGTFALDSEV KAFMRGQRLY EKLMSPETTL LQPREEEGVK YERTFMASEF LDWLVQEGEA
     TTRKEAEQLC HRLMDHGIIQ HVSNKHPFVD SNLLYQFRMN FRRRRRLMEL LNETSPSSQE
     THDSPFCLRK QSHDSRKSTS FMSVSPSKEI KIVSAVRRSS MSSCGSSGYF SSSPTLSSSP
     PVLCNPKSVL KRPVTSEELL TPGAPYARKT FTIVGDAVGW GFVVRGSKPC HIQAVDPSGP
     AAAAGMKVCQ FVVSVNGLNV LNVDYRTVSN LILTGPRTIV MEVMEELDC
//
ID   Q571D3_MOUSE            Unreviewed;      1234 AA.
AC   Q571D3;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   08-MAR-2011, entry version 28.
DE   SubName: Full=MKIAA0478 protein;
DE   Flags: Fragment;
GN   Name=Zbtb40; Synonyms=mKIAA0478;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Adult pancreatic islet;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Seino S., Nishimura M.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the Coding Sequences of Mouse Homologues of KIAA Gene.
RT   The Complete Nucleotide Sequences of Mouse KIAA-homologous cDNAs
RT   Identified by Screening of Terminal sequences of cDNA Clones Randomly
RT   Sampled from Size-Fractionated Libraries..";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK220256; BAD90181.1; -; mRNA.
DR   IPI; IPI00468021; -.
DR   UniGene; Mm.31068; -.
DR   STRING; Q571D3; -.
DR   Ensembl; ENSMUST00000049583; ENSMUSP00000061899; ENSMUSG00000060862.
DR   MGI; MGI:2682254; Zbtb40.
DR   eggNOG; roNOG06886; -.
DR   HOVERGEN; HBG058697; -.
DR   InParanoid; Q571D3; -.
DR   OrthoDB; EOG4SQWVW; -.
DR   ArrayExpress; Q571D3; -.
DR   Bgee; Q571D3; -.
DR   Genevestigator; Q571D3; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 2.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 6.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 13.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 12.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   1234 AA;  135730 MW;  B0E53CD80C292D2A CRC64;
     RARGRRQGQS HSMELPSYSQ QLLLQLYALC KEQRFCDCTI SVGNKEFALL LEMTYTGKLP
     VGKHNFSKII SLADSLQMFD VAVSCKNLLT NLVNCSVQGQ VVRDVSVLSS EAGNKESEKP
     QVEALSSEGA EEPSSSPEVS AVPAGPEKAK TQDVINIATQ EINADPPVAQ EVQVAAEITG
     ATPHTAEVCS PSPVGQIPSE TKEVNTEAEC ETKQDQLTLL LEHESVFSDA ALLTPDTLRR
     LAGCSEIEGP QKETIIECLT SEGGSSAFQR ILDKVHDGSL DVQVALSLVR LYQESTPAEK
     VSQIQPEGSA GEGKTLSVLL LEHKEDLIQC VTQLRPIVEF LETAKEEFLP DSEKRVIQSC
     CEGRTPKEMI ENLLHRVTEE KTLPAKSLVK LLQAVRTAFP NLDLLLDNLQ KGAGSAGTTG
     LARVSCESEW TDEPRPVCIP ADRVDGSSPS PDAYGAELLR KYHENLSEIL IDNQVLLKVI
     SRMQSLAPGD REVMQTLVKQ GSGSGGFSSL MLAALERQTL SATAIWQLLL AVEETETRPL
     NLLLEEVGKE PGAGAFFRAV TAPESTVLEA ILRHSKLLRE AIQQTAGCER LSSEEEHLAE
     TVQEMLSISS ETVSPEASLR AVLSKAMEKS VSASVVCHLL CSVHKSFPGL QPLMQELAHV
     GFLTKESGEE RWKVTDGLHP GAKDKVEEVA KATGEDCQAN EQKEQGEPGP VPEQPEKDTS
     ASPDSAKKSF VCKACDKSFH FYCRLKVHMK RCRVAKSRQV QSEEGSETKG SEKGLEKQQP
     DARGTGGEPD APKKKKKRLP VTCDLCGREF AHASGMQYHK LTEHFDEKPF SCEECGAKFA
     ANSTLKNHLR LHTGDRPFMC KHCLMTFTQA SALAYHTKKK HSEGKMYACQ YCDAVFAQSI
     ELSRHVRTHT GDKPYVCRDC GKGFRQANGL SIHLHTFHTD IEDPYDCKKC RMSFSTLQDH
     RKHIHEVHAK EYHPCPTCGK IFSAPSMLER HMVTHVGGKP FSCGICNKAY QQLSGLWYHN
     RTHHPDVFAA QNHRSPKFSS LQCSSCDKTF SNTVEHKKHI KTEHTDVKFH ECDQCKELFP
     TPALLQVHVK CQHSGSQPFR CLYCAATFRF PGALQHHVTT EHFKQSESTF PCELCGELFT
     SQAQLDSHLE SEHPKVAGTE SQAAASRMVQ VIRAPEPAAP AEQVITLEET QLAGSQVFVT
     LPDSQTSQNS SELVAVTVED LLDGTVTLIC GEAK
//
ID   SG223_MOUSE             Reviewed;        1179 AA.
AC   Q571I4; Q8CB68;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=Tyrosine-protein kinase SgK223;
DE            EC=2.7.10.2;
DE   AltName: Full=Sugen kinase 223;
GN   Name=Sgk223; Synonyms=D8Ertd82e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90130.1; Type=Erroneous initiation;
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DR   EMBL; AK036672; BAC29528.1; -; mRNA.
DR   EMBL; AK220205; BAD90130.1; ALT_INIT; mRNA.
DR   EMBL; BC089024; AAH89024.1; -; mRNA.
DR   IPI; IPI00228233; -.
DR   RefSeq; NP_766499.2; NM_172911.3.
DR   UniGene; Mm.244971; -.
DR   ProteinModelPortal; Q571I4; -.
DR   STRING; Q571I4; -.
DR   PhosphoSite; Q571I4; -.
DR   PRIDE; Q571I4; -.
DR   Ensembl; ENSMUST00000060045; ENSMUSP00000061532; ENSMUSG00000050271.
DR   Ensembl; ENSMUST00000110492; ENSMUSP00000106118; ENSMUSG00000050271.
DR   GeneID; 244418; -.
DR   KEGG; mmu:244418; -.
DR   UCSC; uc009llf.1; mouse.
DR   CTD; 244418; -.
DR   MGI; MGI:1196223; D8Ertd82e.
DR   eggNOG; roNOG06791; -.
DR   GeneTree; ENSGT00460000041554; -.
DR   HOGENOM; HBG283453; -.
DR   HOVERGEN; HBG055817; -.
DR   InParanoid; Q571I4; -.
DR   OrthoDB; EOG4C2H9K; -.
DR   BRENDA; 2.7.10.2; 244.
DR   NextBio; 386268; -.
DR   ArrayExpress; Q571I4; -.
DR   Bgee; Q571I4; -.
DR   CleanEx; MM_D8ERTD82E; -.
DR   Genevestigator; Q571I4; -.
DR   GermOnline; ENSMUSG00000050271; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:EC.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; Transferase;
KW   Tyrosine-protein kinase.
FT   CHAIN         1   1179       Tyrosine-protein kinase SgK223.
FT                                /FTId=PRO_0000263009.
FT   DOMAIN      751   1102       Protein kinase.
FT   NP_BIND     757    765       ATP (By similarity).
FT   COMPBIAS    422    426       Poly-Glu.
FT   COMPBIAS    494    499       Poly-Pro.
FT   COMPBIAS    701    731       Ser-rich.
FT   ACT_SITE    930    930       Proton acceptor (By similarity).
FT   BINDING     808    808       ATP (By similarity).
FT   MOD_RES     196    196       Phosphotyrosine (By similarity).
FT   MOD_RES     477    477       Phosphoserine (By similarity).
FT   MOD_RES     526    526       Phosphoserine (By similarity).
FT   CONFLICT     48     48       D -> Y (in Ref. 2; BAD90130).
FT   CONFLICT     66     66       R -> C (in Ref. 2; BAD90130).
FT   CONFLICT    298    298       G -> S (in Ref. 2; BAD90130).
FT   CONFLICT    309    309       T -> I (in Ref. 2; BAD90130).
FT   CONFLICT    318    318       V -> M (in Ref. 2; BAD90130).
FT   CONFLICT    347    347       Missing (in Ref. 1; BAC29528 and 3;
FT                                AAH89024).
FT   CONFLICT    592    592       A -> V (in Ref. 2; BAD90130).
FT   CONFLICT    667    667       G -> E (in Ref. 2; BAD90130).
FT   CONFLICT    945    945       S -> I (in Ref. 2; BAD90130).
FT   CONFLICT    966    966       A -> V (in Ref. 2; BAD90130).
SQ   SEQUENCE   1179 AA;  126640 MW;  9A6A6872251F7F77 CRC64;
     MTSSCPKGPR PCTSPQPLRE SLPSEDDSDQ RCSPSGDSEG GEYCSILDCC PESKDAVHST
     EGSGRRGGDC SPTCREQGPR TRPTEEEKQG LSFPRECCGQ GSTANPPRLG PKKPSLNSEA
     ASSSDGLSCG SSRSGASSPF APHLENDYCS LVKEPASGKQ QDLSGHFLTS GKCVGQAAEL
     QPASLLRDPV QPEPIYAESA KRKKAAPGPP RPEPKKEQVP AGHSQGQVWT GDTWIQKTPP
     SWSQDREGAN PAPQVATTIT VIAAHPEEDH RTIYLSSPDS AVGVQWPRGP SNQDLQAGEE
     EPLVAQGLTS RESHPHNVTE NTAKEKPAIP PKLSKSSPGG SPVSPAAPPL TDHSDGNTGG
     SSVGPQLLSR VPANLTSSCH TNGVATAGDS AKCPPPATSS SVLDQRRPRY QTGAWSRQCR
     IEEEEEVGQE LSQSWGRELE NGTADHSNSS TWHRLHPIDG TSGQNSKTNS GMSKSASFAF
     EFPKDRGRLE AFSPPPPPPK SRHLLKMNKS SSDLEKVSQS SAESLSPSFR GAHVSFTTGS
     TDSLASDSRP CSDGGPSYEP THSPTISGKK LFAPVPFPSG STEDVSPGGG PAQPPPLPQK
     KIVSRAASSP DGFFWTQGSP KPRTASPKLN LSHSETNVCA HDEPPFNCSL NSGNRSHHVF
     SSSEPLGKAF KGNAPWAPAL GLANSKGGCG SPSLQCRAAT STSSSQLSVS SQASSSSTQL
     QLHSLLSSIS SKEGTYAKLG GLYTQSLARL VTKCEDLFMG GQKKELRFNE NYWSLFKLTC
     NKPCCDSGDA IYYCATCSED PGSIYAVKIC KTPEPKSASY CSPSVPVHFN IQQDCGHFVA
     SVPSSMLASP DTSSKDTAPA VSPQPPAQEQ DCVVVITREV PHQTASDFVR DSMASHRAEP
     EVYERRVCFL LLQLCNGLEH LKEHGIIHRD LCLENLLLAH CNPQSSPGPS ATPTVPTTTS
     RCPSAAPAAT TACQGGPGEK QLPRLIISNF LKAKQKPGGT TNLQQKKSQA RLAPEIVSAS
     QYRKFDEFQT GILIYELLHQ PNPFEVRAQL RERDYRREDL PPLPTLSLYS PGLQQLAHLL
     LEADPIKRIR IGEAKRVLQC LLWGPRRELV EQPCTSEEVL CNTLHNWIDM KRALMMMKFA
     EKAVDRRRGV ELEDWLCCQY LASAEPGALL QSLKLLQLL
//
ID   Q571K0_MOUSE            Unreviewed;       562 AA.
AC   Q571K0;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   08-MAR-2011, entry version 40.
DE   SubName: Full=MKIAA4187 protein;
DE   Flags: Fragment;
GN   Name=Dlg1; Synonyms=Dlgh1, mKIAA4187;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Embryonic tail;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the Coding Sequences of Mouse Homologues of KIAA Gene.
RT   The Complete Nucleotide Sequences of Mouse KIAA-homologous cDNAs
RT   Identified by Screening of Terminal sequences of cDNA Clones Randomly
RT   Sampled from Size-Fractionated Libraries..";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 3 PDZ (DHR) domains.
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DR   EMBL; AK220189; BAD90374.1; -; mRNA.
DR   IPI; IPI00553807; -.
DR   UniGene; Mm.382; -.
DR   ProteinModelPortal; Q571K0; -.
DR   STRING; Q571K0; -.
DR   Ensembl; ENSMUST00000023454; ENSMUSP00000023454; ENSMUSG00000022770.
DR   Ensembl; ENSMUST00000115207; ENSMUSP00000110862; ENSMUSG00000022770.
DR   MGI; MGI:107231; Dlg1.
DR   eggNOG; roNOG08565; -.
DR   HOVERGEN; HBG107814; -.
DR   ArrayExpress; Q571K0; -.
DR   Bgee; Q571K0; -.
DR   Genevestigator; Q571K0; -.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0031253; C:cell projection membrane; IDA:MGI.
DR   GO; GO:0001772; C:immunological synapse; IDA:MGI.
DR   GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR   GO; GO:0045121; C:membrane raft; IDA:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0032947; F:protein complex scaffold; IMP:MGI.
DR   GO; GO:0032147; P:activation of protein kinase activity; IMP:MGI.
DR   GO; GO:0042982; P:amyloid precursor protein metabolic process; IGI:MGI.
DR   GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI.
DR   GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
DR   GO; GO:0060022; P:hard palate development; IMP:MGI.
DR   GO; GO:0001771; P:immunological synapse formation; IMP:MGI.
DR   GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI.
DR   GO; GO:0031579; P:membrane raft organization; IMP:MGI.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
DR   GO; GO:0042130; P:negative regulation of T cell proliferation; IMP:MGI.
DR   GO; GO:0030432; P:peristalsis; IMP:MGI.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0008104; P:protein localization; IMP:MGI.
DR   GO; GO:0042391; P:regulation of membrane potential; IGI:MGI.
DR   GO; GO:0048608; P:reproductive structure development; IMP:MGI.
DR   GO; GO:0048745; P:smooth muscle tissue development; IMP:MGI.
DR   GO; GO:0042110; P:T cell activation; IMP:MGI.
DR   GO; GO:0002369; P:T cell cytokine production; IMP:MGI.
DR   InterPro; IPR004172; L27.
DR   InterPro; IPR015143; L27_1.
DR   InterPro; IPR019590; MAGUK_PEST_N.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR019583; PDZ_assoc.
DR   Pfam; PF09058; L27_1; 1.
DR   Pfam; PF10608; MAGUK_N_PEST; 1.
DR   Pfam; PF00595; PDZ; 3.
DR   Pfam; PF10600; PDZ_assoc; 1.
DR   SMART; SM00569; L27; 1.
DR   SMART; SM00228; PDZ; 3.
DR   SUPFAM; SSF50156; PDZ; 3.
DR   PROSITE; PS51022; L27; 1.
DR   PROSITE; PS50106; PDZ; 3.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   562 AA;  61333 MW;  AECB270D2555A844 CRC64;
     FWRKMPVRKQ DTQRALHLLE EYRSKLSQTE DRQLRSSIER VINIFQSNLF QALIDIQEFY
     EVTLLDNPKC VDHSKQCEPV QPVTTWEIAS LPSTAVTSET LPGSLSPPVE KYRYQDEEVL
     PPEHISPQVT NEVLGPELVH VSEKNLSEIE NVHGFVSHSH ISPIKANPPP VLVNTDSLET
     PTYVNGTDAD YEYEEITLER GNSGLGFSIA GGTDNPHIGD DSSIFITKII TGGAAAQDGR
     LRVNDCILRV NEADVRDVTH SKAVEALKEA GSIVRLYVKR RKPASEKIME IKLIKGPKGL
     GFSIAGGVGN QHIPGDNSIY VTKIIEGGAA HKDGKLQIGD KLLAVNSVCL EEVTHEEAVT
     ALKNTSDFVY LKVAKPTTSS QSVDNHVSPS SCLGQTPTSP ARYSPISKAV LGDDEITREP
     RKVVLHRGST GLGFNIVGGE DGEGIFISFI LAGGPADLSG ELRKGDRIIS VNSVDLRAAS
     HEQAAAALKN AGQAVTIVAQ YRPEEYSRFE AKIHDLREQM MNSSVSSGSG SLRTSQKRSL
     YVSLEPSLIM TRLRTAGFPV KD
//
ID   TAB3_MOUSE              Reviewed;         716 AA.
AC   Q571K4;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=TGF-beta-activated kinase 1 and MAP3K7-binding protein 3;
DE   AltName: Full=Mitogen-activated protein kinase kinase kinase 7-interacting protein 3;
DE   AltName: Full=TAK1-binding protein 3;
DE            Short=TAB-3;
DE   AltName: Full=TGF-beta-activated kinase 1-binding protein 3;
GN   Name=Tab3; Synonyms=Kiaa4135, Map3k7ip3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Adapter linking MAP3K7/TAK1 and TRAF6 or TRAF2. Mediator
CC       of MAP3K7 activation, respectively in the IL-1 and TNF signaling
CC       pathways. Plays a role in activation of NF-kappa-B and AP1
CC       transcription factor (By similarity).
CC   -!- SUBUNIT: Interacts with TAB1, TAB2, MAP3K7, TRAF2 and TRAF6. The
CC       minimal TAB3-containing complex (TAB1-MAP3K7-TAB3) appears not to
CC       contain TAB2. However, it seems sensible to consider that TAB2 may
CC       also join this complex and may act in a cooperative manner with
CC       TAB3. Interacts with WDR34 (via the WD domains). Interacts with
CC       RBCK1 (By similarity).
CC   -!- PTM: Phosphorylated (By similarity).
CC   -!- PTM: Ubiquitinated; following IL1 stimulation or TRAF6
CC       overexpression (By similarity).
CC   -!- SIMILARITY: Contains 1 CUE domain.
CC   -!- SIMILARITY: Contains 1 RanBP2-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90370.1; Type=Erroneous initiation;
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DR   EMBL; AK220185; BAD90370.1; ALT_INIT; mRNA.
DR   IPI; IPI00606905; -.
DR   RefSeq; NP_080005.2; NM_025729.4.
DR   UniGene; Mm.119646; -.
DR   PDB; 3A9K; X-ray; 1.40 A; C=688-716.
DR   PDBsum; 3A9K; -.
DR   ProteinModelPortal; Q571K4; -.
DR   SMR; Q571K4; 4-57, 688-716.
DR   STRING; Q571K4; -.
DR   PhosphoSite; Q571K4; -.
DR   PRIDE; Q571K4; -.
DR   Ensembl; ENSMUST00000048250; ENSMUSP00000039668; ENSMUSG00000035476.
DR   GeneID; 66724; -.
DR   KEGG; mmu:66724; -.
DR   UCSC; uc009trt.1; mouse.
DR   CTD; 66724; -.
DR   MGI; MGI:1913974; Tab3.
DR   eggNOG; roNOG07438; -.
DR   GeneTree; ENSGT00530000063642; -.
DR   HOGENOM; HBG714653; -.
DR   HOVERGEN; HBG056952; -.
DR   InParanoid; Q571K4; -.
DR   OMA; QGPVPHY; -.
DR   OrthoDB; EOG4XD3QR; -.
DR   NextBio; 322481; -.
DR   ArrayExpress; Q571K4; -.
DR   Bgee; Q571K4; -.
DR   Genevestigator; Q571K4; -.
DR   GermOnline; ENSMUSG00000035476; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR003892; CUE.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   Pfam; PF02845; CUE; 1.
DR   Pfam; PF00641; zf-RanBP; 1.
DR   SMART; SM00546; CUE; 1.
DR   SMART; SM00547; ZnF_RBZ; 1.
DR   PROSITE; PS51140; CUE; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
DR   PROSITE; PS50199; ZF_RANBP2_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Metal-binding; Phosphoprotein;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1    716       TGF-beta-activated kinase 1 and MAP3K7-
FT                                binding protein 3.
FT                                /FTId=PRO_0000226973.
FT   DOMAIN        8     51       CUE.
FT   ZN_FING     686    716       RanBP2-type.
FT   COILED      521    564       Potential.
FT   COMPBIAS    152    455       Pro-rich.
FT   COMPBIAS    508    513       Poly-Ser.
FT   COMPBIAS    661    666       Poly-Ala.
FT   MOD_RES      60     60       Phosphoserine (By similarity).
FT   MOD_RES     408    408       Phosphothreonine (By similarity).
FT   MOD_RES     412    412       Phosphoserine (By similarity).
FT   MOD_RES     496    496       Phosphoserine (By similarity).
FT   TURN        694    696
FT   TURN        708    710
SQ   SEQUENCE   716 AA;  79029 MW;  65B3FCC60C4A1CB1 CRC64;
     MAQNSPQLDI QVLHDLRQRF PEIPEGVVSQ CMLQNNNNLE ACCRALSQES SKYLYMEYHS
     PEDNRMNRNR LLHINLGIHS PSSYHPGDGA HLNGGRTLVH SSSDGHIDPQ HTAGKQLICL
     VQEPHSAPAV VAATPNYNPF FMNEQNRSAA TPPSQPPQQP SSMQTGMNPS AMQGPSPPPP
     PPSYMHIPRY STNPITVTVS QNLPSGQTVP RALQILPQIP SNLYGSPGSI FIRQTSQSSS
     GRQTPQNAPW QSSPQGPVPH YSQRPLPVYP HQQNYQPSQY SPKQQQIPQS VYHSPPPSQC
     PSPFSSPQHQ VQPPQLGHPS SHVFMPPSPS TTPPHLYQQG PPSYQKPGSH SVAYLPYTAS
     SLPKGSMKKI EITVEPSQRP GTAITRSPSP ISNQPSPRNQ HSLYTATTPP SSSPSRGISS
     QPKPPFSVNP VYITYTQPTG PSCAPSPSPR VIPNPTTVFK ITVGRATTEN LLNLVDQEER
     SAAPEPIQPI SVIPGSGGEK GNHKYQRSSS SGSDDYAYTQ ALLLHQRARM ERLAKQLKLE
     KEELERLKAE VNSMEHDLMQ RRLRRVSCTT AIPTPEEMTR LRSTNRQLQI NVDCTLKEVD
     LLQSRGNFDP KAINNFYDHI EPGPVVPPKP SKKDSSDSCA IERKARRISV TSKAPVDIHD
     AQAAAADEHL SICKQSARTQ PRDEDYEGAP WNCDSCTFLN HPALNRCEQC EMPRYT
//
ID   JIP4_MOUSE              Reviewed;        1321 AA.
AC   Q58A65; Q3UH77; Q3UHF0; Q58VQ4; Q5NC70; Q5NC78; Q6A057; Q6PAS3;
AC   Q8CJC2;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=C-Jun-amino-terminal kinase-interacting protein 4;
DE            Short=JIP-4;
DE            Short=JNK-interacting protein 4;
DE   AltName: Full=JNK-associated leucine-zipper protein;
DE            Short=JLP;
DE   AltName: Full=JNK/SAPK-associated protein 2;
DE            Short=JSAP2;
DE   AltName: Full=Mitogen-activated protein kinase 8-interacting protein 4;
DE   AltName: Full=Sperm-associated antigen 9;
GN   Name=Spag9; Synonyms=Jip4, Jsap2, Kiaa0516, Mapk8ip4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH
RP   MAX; MAPK8; MAPK14; MAP3K3; MYC AND MAP2K4, AND SUBCELLULAR LOCATION.
RX   MEDLINE=22295031; PubMed=12391307; DOI=10.1073/pnas.232310199;
RA   Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.;
RT   "JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules
RT   and transcription factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), FUNCTION, INTERACTION WITH
RP   KNS2 AND MAPK8, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   PHOSPHORYLATION.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=15767678; DOI=10.1128/MCB.25.7.2733-2743.2005;
RA   Kelkar N., Standen C.L., Davis R.J.;
RT   "Role of the JIP4 scaffold protein in the regulation of mitogen-
RT   activated protein kinase signaling pathways.";
RL   Mol. Cell. Biol. 25:2733-2743(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RA   Takamatsu N., Tochigi M., Ito M., Odama Y., Xu P., Nakabeppu Y.,
RA   Yoshioka K., Shiba T.;
RT   "JSAP2, a novel member of the JSAP1 JNK scaffold protein family.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
RP   SPLICING.
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   INTERACTION WITH KNS2, AND INDUCTION.
RX   PubMed=15987681; DOI=10.1074/jbc.M505499200;
RA   Nguyen Q., Lee C.M., Le A., Reddy E.P.;
RT   "JLP associates with kinesin light chain 1 through a novel leucine
RT   zipper-like domain.";
RL   J. Biol. Chem. 280:30185-30191(2005).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730 AND SER-733, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244; THR-292 AND
RP   SER-733, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND SER-730, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-217 AND THR-365, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: The JNK-interacting protein (JIP) group of scaffold
CC       proteins selectively mediates JNK signaling by aggregating
CC       specific components of the MAPK cascade to form a functional JNK
CC       signaling module.
CC   -!- SUBUNIT: Homooligomer. Interacts with MAX, MAPK8, MAPK14, MAPK10,
CC       MAPK14, MAP3K3, MYC, KNS2, and MAP2K4. Interaction with KNS2 is
CC       important in the formation of ternary complex with MAPK8.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
CC       Note=Perinuclear distribution in response to stress signals such
CC       as UV radiation.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q58A65-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q58A65-2; Sequence=VSP_018228;
CC       Name=3;
CC         IsoId=Q58A65-3; Sequence=VSP_018226, VSP_018227, VSP_018228,
CC                                  VSP_018229;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q58A65-4; Sequence=VSP_018226, VSP_018227, VSP_018228,
CC                                  VSP_018230;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q58A65-5; Sequence=VSP_018227, VSP_018228;
CC         Note=No experimental confirmation available;
CC       Name=6;
CC         IsoId=Q58A65-6; Sequence=VSP_018225, VSP_018228;
CC   -!- TISSUE SPECIFICITY: Isoform 6 is highly expressed in brain,
CC       kidney, liver, heart.
CC   -!- INDUCTION: Up-regulated during neuronal differentiation.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity). Phosphorylated by MAPK8 and MAPK14.
CC   -!- SIMILARITY: Belongs to the JIP scaffold family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32239.1; Type=Erroneous initiation;
CC       Sequence=CAI35376.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF327451; AAN61564.1; -; mRNA.
DR   EMBL; AY823270; AAX19462.1; -; mRNA.
DR   EMBL; AB047782; BAD93176.1; -; mRNA.
DR   EMBL; AK172961; BAD32239.1; ALT_INIT; mRNA.
DR   EMBL; AK147431; BAE27907.1; -; mRNA.
DR   EMBL; AK147537; BAE27980.1; -; mRNA.
DR   EMBL; AL662838; CAI35367.1; -; Genomic_DNA.
DR   EMBL; AL662838; CAI35375.1; -; Genomic_DNA.
DR   EMBL; AL662838; CAI35376.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC060100; AAH60100.1; -; mRNA.
DR   EMBL; BC094670; AAH94670.1; -; mRNA.
DR   IPI; IPI00462746; -.
DR   IPI; IPI00475034; -.
DR   IPI; IPI00626409; -.
DR   IPI; IPI00648688; -.
DR   IPI; IPI00753495; -.
DR   IPI; IPI00754112; -.
DR   RefSeq; NP_001020599.1; NM_001025428.1.
DR   RefSeq; NP_001020600.1; NM_001025429.1.
DR   RefSeq; NP_001020601.1; NM_001025430.1.
DR   RefSeq; NP_001186134.1; NM_001199205.1.
DR   RefSeq; NP_081845.2; NM_027569.2.
DR   UniGene; Mm.260737; -.
DR   ProteinModelPortal; Q58A65; -.
DR   SMR; Q58A65; 406-466.
DR   STRING; Q58A65; -.
DR   PhosphoSite; Q58A65; -.
DR   PRIDE; Q58A65; -.
DR   Ensembl; ENSMUST00000024979; ENSMUSP00000024979; ENSMUSG00000020859.
DR   Ensembl; ENSMUST00000041956; ENSMUSP00000042271; ENSMUSG00000020859.
DR   Ensembl; ENSMUST00000075695; ENSMUSP00000075115; ENSMUSG00000020859.
DR   Ensembl; ENSMUST00000092778; ENSMUSP00000090453; ENSMUSG00000020859.
DR   Ensembl; ENSMUST00000103169; ENSMUSP00000099458; ENSMUSG00000020859.
DR   GeneID; 70834; -.
DR   KEGG; mmu:70834; -.
DR   UCSC; uc007kxx.1; mouse.
DR   UCSC; uc007kxy.1; mouse.
DR   UCSC; uc007kxz.1; mouse.
DR   UCSC; uc007kya.1; mouse.
DR   UCSC; uc007kyd.1; mouse.
DR   CTD; 70834; -.
DR   MGI; MGI:1918084; Spag9.
DR   eggNOG; roNOG14624; -.
DR   GeneTree; ENSGT00600000084097; -.
DR   HOVERGEN; HBG024110; -.
DR   InParanoid; Q58A65; -.
DR   OrthoDB; EOG4QJRMF; -.
DR   Reactome; REACT_21350; Activation of p38 alpha/beta MAPK.
DR   NextBio; 332372; -.
DR   ArrayExpress; Q58A65; -.
DR   Bgee; Q58A65; -.
DR   CleanEx; MM_SPAG9; -.
DR   Genevestigator; Q58A65; -.
DR   GermOnline; ENSMUSG00000020859; Mus musculus.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008432; F:JUN kinase binding; IDA:MGI.
DR   GO; GO:0019894; F:kinesin binding; IDA:MGI.
DR   GO; GO:0048273; F:mitogen-activated protein kinase p38 binding; IDA:MGI.
DR   GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IPI:MGI.
DR   GO; GO:0007257; P:activation of JUN kinase activity; IDA:MGI.
DR   GO; GO:0000187; P:activation of MAPK activity; IDA:MGI.
DR   GO; GO:0090074; P:negative regulation of protein homodimerization activity; IDA:MGI.
DR   GO; GO:0043410; P:positive regulation of MAPKKK cascade; IGI:MGI.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:MGI.
DR   GO; GO:0051260; P:protein homooligomerization; IDA:MGI.
DR   GO; GO:0051146; P:striated muscle cell differentiation; IGI:MGI.
DR   InterPro; IPR019143; JNK/Rab-associated_protein-1_N.
DR   InterPro; IPR011044; Quino_amine_DH_bsu.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF09744; Jnk-SapK_ap_N; 1.
DR   SUPFAM; SSF50969; Amine_DH_B_like; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW   Phosphoprotein.
FT   CHAIN         1   1321       C-Jun-amino-terminal kinase-interacting
FT                                protein 4.
FT                                /FTId=PRO_0000234077.
FT   COILED       66    166       Potential.
FT   COILED      408    534       Potential.
FT   COILED      724    758       Potential.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     109    109       Phosphoserine (By similarity).
FT   MOD_RES     183    183       Phosphoserine (By similarity).
FT   MOD_RES     185    185       Phosphoserine (By similarity).
FT   MOD_RES     203    203       Phosphoserine.
FT   MOD_RES     217    217       Phosphothreonine.
FT   MOD_RES     226    226       Phosphothreonine (By similarity).
FT   MOD_RES     238    238       Phosphoserine (By similarity).
FT   MOD_RES     244    244       Phosphothreonine.
FT   MOD_RES     265    265       Phosphoserine (By similarity).
FT   MOD_RES     268    268       Phosphoserine (By similarity).
FT   MOD_RES     276    276       Phosphothreonine (By similarity).
FT   MOD_RES     292    292       Phosphothreonine.
FT   MOD_RES     311    311       Phosphoserine (By similarity).
FT   MOD_RES     329    329       Phosphoserine (By similarity).
FT   MOD_RES     332    332       Phosphoserine (By similarity).
FT   MOD_RES     365    365       Phosphothreonine.
FT   MOD_RES     387    387       Phosphoserine (By similarity).
FT   MOD_RES     388    388       Phosphoserine (By similarity).
FT   MOD_RES     391    391       Phosphoserine (By similarity).
FT   MOD_RES     418    418       Phosphothreonine (By similarity).
FT   MOD_RES     586    586       Phosphothreonine (By similarity).
FT   MOD_RES     594    594       Phosphoserine (By similarity).
FT   MOD_RES     595    595       Phosphothreonine (By similarity).
FT   MOD_RES     728    728       Phosphoserine (By similarity).
FT   MOD_RES     730    730       Phosphoserine.
FT   MOD_RES     732    732       Phosphoserine (By similarity).
FT   MOD_RES     733    733       Phosphoserine.
FT   MOD_RES    1144   1144       Phosphoserine (By similarity).
FT   MOD_RES    1264   1264       Phosphothreonine (By similarity).
FT   VAR_SEQ       1    165       Missing (in isoform 6).
FT                                /FTId=VSP_018225.
FT   VAR_SEQ       1    143       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_018226.
FT   VAR_SEQ     144    196       RLEEREAELKKEYNALHQRHTEMIHNYMEHLERTKLHQLSG
FT                                SDQLEATAHSRI -> MNPGCMLLFVFGFVGGAVVINSAIL
FT                                VSLSVLLLVHFSISTGVPALTQNLPRIL (in isoform
FT                                3, isoform 4 and isoform 5).
FT                                /FTId=VSP_018227.
FT   VAR_SEQ     248    261       Missing (in isoform 2, isoform 3, isoform
FT                                4, isoform 5 and isoform 6).
FT                                /FTId=VSP_018228.
FT   VAR_SEQ     405    405       G -> GEYSG (in isoform 3).
FT                                /FTId=VSP_018229.
FT   VAR_SEQ    1175   1175       T -> TVILHQGRLLGLRA (in isoform 4).
FT                                /FTId=VSP_018230.
FT   CONFLICT    241    241       R -> C (in Ref. 1; AAN61564).
FT   CONFLICT    453    453       E -> A (in Ref. 1; AAN61564).
FT   CONFLICT    468    468       E -> G (in Ref. 5; BAE27980).
FT   CONFLICT    705    705       S -> T (in Ref. 3; BAD93176).
FT   CONFLICT   1114   1114       L -> P (in Ref. 5; BAE27907).
SQ   SEQUENCE   1321 AA;  146219 MW;  93A6E97A62E0E92C CRC64;
     MELEDGVVYQ EEPGGSGAVM SERVSGLAGS IYREFERLIG RYDEEVVKEL MPLVVAVLEN
     LDSVFAQDQE HQVELELLRD DNEQLITQYE REKALRKHAE EKFIEFEDSQ EQEKKDLQTR
     VESLESQTRQ LELKAKNYAD QISRLEEREA ELKKEYNALH QRHTEMIHNY MEHLERTKLH
     QLSGSDQLEA TAHSRIRKER PISLGIFPLP AGDGLLTPDT QKGGETPGSE QWKFQELSQP
     RSHTSLKVSH SPEPPKAVEQ EDELSDISQG GSKATTPAST ANSDVSAIPP DTPSKEDNEG
     FVKGTDTSNK SEISKHIEVQ VAQETRNVST ESGENEEKSE VQAIIESTPE LDMDKDLSGY
     KGSSTPTKGI ENKAFDRNTE SLFEELSSAG SGLIGDVDEG ADLLGMGREV ENLILENTQL
     LETKNALNVV KNDLIAKVDE LTCEKDVLQG ELEAVKQAKL KLEDKNRELE EELRKARAEA
     EDARQKAKDD DDSDIPTAQR KRFTRVEMAR VLMERNQYKE RLMELQEAVR WTEMIRASRE
     NPAMQEKKRS SIWQFFSRLF SSSSNATKKP EPPVNLKYNA PTSHVTPSVK KRSSTLSQLP
     GDKSKAFDFL SEETEASLAS RREQKREQYR QVKAHVQKED GRVQAFGWSL PQKYKQVANG
     QGETKMKNLP VPVYLRPLDE KDASMKLWCA VGVNLSGGKT RDGGSVVGAS VFYKDIAGLD
     TEGSKQRSAS QSSLDKLDQE LKEQQKEFKN QEELSSQVWI CTSTHSTTKV IIIDAVQPGN
     ILDSFTVCNS HVLCIASVPG ARETDYPAGE ELSESGQVDK ASLCGSMTSN SSAEMDSLLG
     GITVVGCSTE GLTGAATSPS TNGASPVIEK PPEMETENSE VDENIPTAEE ATEATEGNAG
     STEDTVDISQ PGVYTEHVFT DPLGVQIPED LSPVFQSSND SDVYKDQISV LPNEQDLARE
     EAQKMSSLLP TMWLGAQNGC LYVHSSVAQW RKCLHSIKLK DSILSIVHVK GIVLVALADG
     TLAIFHRGVD GQWDLSNYHL LDLGRPHHSI RCMTVVHDKV WCGYRNKIYV VQPKAMKIEK
     SFDAHPRKES QVRQLAWVGD GVWVSIRLDS TLRLYHAHTY QHLQDVDIEP YVSKMLGTGK
     LGFSFVRITA LMVSCNRLWV GTGNGVIISI PLTETNKTSG TPGNRPGSVI RVYGDENSDK
     VTPGTFIPYC SMAHAQLCFH GHRDAVKFFV AVPGQVISPQ SSSGGADLTA DKAGSSAQEP
     SSQTPLKSML VISGGEGYID FRMGDEGGES ELLGEDLPLE PSVTKAERSH LIVWQVMCGN
     E
//
ID   MIMIT_MOUSE             Reviewed;         168 AA.
AC   Q59J78; Q14A56; Q80VX9;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=Mimitin, mitochondrial;
DE   AltName: Full=Myc-induced mitochondrial protein;
DE            Short=MMTN;
DE   AltName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 2;
DE   AltName: Full=NDUFA12-like protein;
DE   Flags: Precursor;
GN   Name=Ndufaf2; Synonyms=Ndufa12l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15774466; DOI=10.1074/jbc.M501231200;
RA   Tsuneoka M., Teye K., Arima N., Soejima M., Otera H., Ohashi K.,
RA   Koga Y., Fujita H., Shirouzu K., Kimura H., Koda Y.;
RT   "A novel Myc-target gene, mimitin, that is involved in cell
RT   proliferation of esophageal squamous cell carcinoma.";
RL   J. Biol. Chem. 280:19977-19985(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RA   Li X., Jin Y., Yue W., Yan W., Liu Y.;
RT   "A candidate gene related to development of cleft palate.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Acts as a molecular chaperone for mitochondrial complex
CC       I assembly (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the complex I NDUFA12 subunit family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAP33449.1; Type=Frameshift; Positions=39;
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DR   EMBL; AB183434; BAD91206.1; -; mRNA.
DR   EMBL; AY262012; AAP33449.1; ALT_FRAME; mRNA.
DR   EMBL; BC116975; AAI16976.1; -; mRNA.
DR   EMBL; BC116977; AAI16978.1; -; mRNA.
DR   IPI; IPI00330551; -.
DR   RefSeq; NP_001120818.1; NM_001127346.1.
DR   UniGene; Mm.276040; -.
DR   STRING; Q59J78; -.
DR   PRIDE; Q59J78; -.
DR   Ensembl; ENSMUST00000022206; ENSMUSP00000022206; ENSMUSG00000068184.
DR   GeneID; 75597; -.
DR   KEGG; mmu:75597; -.
DR   UCSC; uc007ruu.1; mouse.
DR   CTD; 75597; -.
DR   MGI; MGI:1922847; Ndufaf2.
DR   eggNOG; roNOG09765; -.
DR   GeneTree; ENSGT00390000002743; -.
DR   HOGENOM; HBG713500; -.
DR   HOVERGEN; HBG054904; -.
DR   InParanoid; Q59J78; -.
DR   OMA; GNKYYYV; -.
DR   OrthoDB; EOG4K3KXK; -.
DR   NextBio; 343458; -.
DR   ArrayExpress; Q59J78; -.
DR   Bgee; Q59J78; -.
DR   Genevestigator; Q59J78; -.
DR   GermOnline; ENSMUSG00000068184; Mus musculus.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   InterPro; IPR007763; NADH_UbQ_OxRdtase_17.2kDa_su.
DR   PANTHER; PTHR12910; Complex1_17_2kD; 1.
DR   Pfam; PF05071; NDUFA12; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Mitochondrion; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    168       Mimitin, mitochondrial.
FT                                /FTId=PRO_0000020055.
SQ   SEQUENCE   168 AA;  19628 MW;  DB45BAF7DF4D7AD7 CRC64;
     MSWWSGVWRS VWSALSREVR EHVGTDHLGN KYYYVAEYKN WRGQTIREKR IVEAANRKEV
     DYEAGDIPTE WEAWIRRTRK TPPTMEEILK NEKYREEIKI KSQDFYEKDK LGKETSEELL
     PSPTATQVKG HASAPYFGRE EPSVAPTSTG KTFQPGSWTP EDGKRQSQ
//
ID   Q5BKS2_MOUSE            Unreviewed;       476 AA.
AC   Q5BKS2;
DT   12-APR-2005, integrated into UniProtKB/TrEMBL.
DT   12-APR-2005, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   SubName: Full=Protein phosphatase 1B, magnesium dependent, beta isoform;
GN   Name=Ppm1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the PP2C family.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC090963; AAH90963.1; -; mRNA.
DR   IPI; IPI00118736; -.
DR   UniGene; Mm.249695; -.
DR   ProteinModelPortal; Q5BKS2; -.
DR   STRING; Q5BKS2; -.
DR   Ensembl; ENSMUST00000080217; ENSMUSP00000079107; ENSMUSG00000061130.
DR   MGI; MGI:101841; Ppm1b.
DR   HOVERGEN; HBG053647; -.
DR   InParanoid; Q5BKS2; -.
DR   ArrayExpress; Q5BKS2; -.
DR   Bgee; Q5BKS2; -.
DR   Genevestigator; Q5BKS2; -.
DR   GO; GO:0008287; C:protein serine/threonine phosphatase complex; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   InterPro; IPR001932; PP2C-like.
DR   InterPro; IPR012911; PP2C_C.
DR   InterPro; IPR000222; PP2C_Mn2_Asp60_BS.
DR   InterPro; IPR014045; PP2C_N.
DR   InterPro; IPR015655; Protein_Pase_2C.
DR   Gene3D; G3DSA:3.60.40.10; PP2C-related; 1.
DR   Gene3D; G3DSA:1.10.10.430; PP2C_C; 1.
DR   PANTHER; PTHR13832; PP2C; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   Pfam; PF07830; PP2C_C; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-related; 1.
DR   SUPFAM; SSF81601; PP2C_C; 1.
DR   PROSITE; PS01032; PP2C; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Metal-binding; Protein phosphatase.
SQ   SEQUENCE   476 AA;  52024 MW;  B73AA1767C594B60 CRC64;
     MGAFLDKPKT EKHNAHGAGN GLRYGLSSMQ GWRVEMEDAH TAVVGIPHGL DNWSFFAVYD
     GHAGSRVANY CSTHLLEHIT TNEDFRAADK SGSALEPSVE SVKTGIRTGF LKIDEYMRNF
     SDLRNGMDRS GSTAVGVMVS PTHMYFINCG DSRAVLCRNG QVCFSTQDHK PCNPVEKERI
     QNAGGSVMIQ RVNGSPVSRA LGDYDYKCVD GKGPTEQLVS PEPEVYEIVR AEEDEFVVLA
     CDGIWDVMSN EELCEFVKSR LEVSDDLENV CNWVVDTCLH KGSRDNMSVV LVCFSNAPKV
     SEEAVKRDSE LDKHLESRVE EIMQKSGEEG MPDLAHVMRI LSAENIPNLP PGGGLAGKRH
     VIEAVYSRLN PHKDNDGASD EAEEGGSQGK LVEALRQMRV NHRGNYRQLL EEMLTSYRLA
     KVEGEESPAD PAAAAASSNS DGGNPVAMQE RDTEGGPAGL DSRNEDAGTK RSAENI
//
ID   PEX1_MOUSE              Reviewed;        1284 AA.
AC   Q5BL07; Q3UEC7; Q9CU85;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Peroxisome biogenesis factor 1;
DE   AltName: Full=Peroxin-1;
GN   Name=Pex1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-505 AND 795-1284 (ISOFORM
RP   1).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHOLIPID BINDING, AND MUTAGENESIS OF ARG-135 AND LYS-174.
RX   PubMed=17018057; DOI=10.1111/j.1742-4658.2006.05494.x;
RA   Shiozawa K., Goda N., Shimizu T., Mizuguchi K., Kondo N.,
RA   Shimozawa N., Shirakawa M., Hiroaki H.;
RT   "The common phospholipid-binding activity of the N-terminal domains of
RT   PEX1 and VCP/p97.";
RL   FEBS J. 273:4959-4971(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1212, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1212, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 3-181.
RX   PubMed=15328346; DOI=10.1074/jbc.M407837200;
RA   Shiozawa K., Maita N., Tomii K., Seto A., Goda N., Akiyama Y.,
RA   Shimizu T., Shirakawa M., Hiroaki H.;
RT   "Structure of the N-terminal domain of PEX1 AAA-ATPase.
RT   Characterization of a putative adaptor-binding domain.";
RL   J. Biol. Chem. 279:50060-50068(2004).
CC   -!- FUNCTION: Required for stability of PEX5 and protein import into
CC       the peroxisome matrix. Anchored by PEX26 to peroxisome membranes,
CC       possibly to form heteromeric AAA ATPase complexes required for the
CC       import of proteins into peroxisomes (By similarity).
CC   -!- SUBUNIT: Interacts directly with PEX6. Interacts indirectly with
CC       PEX26, via its interaction with PEX6 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Peroxisome
CC       membrane (By similarity). Note=Associated with peroxisomal
CC       membranes (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5BL07-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5BL07-2; Sequence=VSP_028131;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The N-terminal domain shows evolutionary conservation with
CC       that of VCP, and is able to bind phospholipids with a preference
CC       for phosphatidylinositol monophosphates.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
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DR   EMBL; BC090845; AAH90845.1; -; mRNA.
DR   EMBL; AK017309; BAB30684.1; -; mRNA.
DR   EMBL; AK149599; BAE28984.1; -; mRNA.
DR   IPI; IPI00136789; -.
DR   IPI; IPI00653755; -.
DR   RefSeq; NP_082053.1; NM_027777.1.
DR   UniGene; Mm.379196; -.
DR   PDB; 1WLF; X-ray; 2.05 A; A=3-181.
DR   PDBsum; 1WLF; -.
DR   ProteinModelPortal; Q5BL07; -.
DR   SMR; Q5BL07; 13-179, 408-1253.
DR   STRING; Q5BL07; -.
DR   PhosphoSite; Q5BL07; -.
DR   PRIDE; Q5BL07; -.
DR   Ensembl; ENSMUST00000006061; ENSMUSP00000006061; ENSMUSG00000005907.
DR   Ensembl; ENSMUST00000121291; ENSMUSP00000113304; ENSMUSG00000005907.
DR   GeneID; 71382; -.
DR   KEGG; mmu:71382; -.
DR   UCSC; uc008whf.1; mouse.
DR   CTD; 71382; -.
DR   MGI; MGI:1918632; Pex1.
DR   eggNOG; roNOG10224; -.
DR   GeneTree; ENSGT00550000075032; -.
DR   HOGENOM; HBG444889; -.
DR   HOVERGEN; HBG008169; -.
DR   InParanoid; Q5BL07; -.
DR   OMA; QLHLLQN; -.
DR   OrthoDB; EOG4JM7P2; -.
DR   NextBio; 333669; -.
DR   ArrayExpress; Q5BL07; -.
DR   Bgee; Q5BL07; -.
DR   CleanEx; MM_PEX1; -.
DR   Genevestigator; Q5BL07; -.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   InterPro; IPR009010; Asp_de-COase-like_fold.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR015343; Peroxisome_synth_fac_1_a/b.
DR   InterPro; IPR015342; PEX-1N.
DR   Gene3D; G3DSA:2.40.40.20; Asp_decarboxylase-like_fold; 1.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF09262; PEX-1N; 1.
DR   Pfam; PF09263; PEX-2N; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF50692; Asp_decarb_fold; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Cytoplasm;
KW   Isopeptide bond; Lipid-binding; Membrane; Nucleotide-binding;
KW   Peroxisome; Peroxisome biogenesis; Peroxisome biogenesis disorder;
KW   Phosphoprotein; Protein transport; Repeat; Transport; Ubl conjugation.
FT   CHAIN         1   1284       Peroxisome biogenesis factor 1.
FT                                /FTId=PRO_0000304931.
FT   NP_BIND     600    607       ATP (Potential).
FT   NP_BIND     882    889       ATP (Potential).
FT   MOD_RES    1182   1182       Phosphoserine (By similarity).
FT   MOD_RES    1212   1212       Phosphoserine.
FT   CROSSLNK    834    834       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   VAR_SEQ     413    452       Missing (in isoform 2).
FT                                /FTId=VSP_028131.
FT   MUTAGEN     135    135       R->A: Loss of phospholipid-binding.
FT   MUTAGEN     174    174       K->A: No effect on phospholipid-binding.
FT   STRAND       15     22
FT   STRAND       25     27
FT   STRAND       29     31
FT   HELIX        33     38
FT   STRAND       47     53
FT   STRAND       56     58
FT   STRAND       60     62
FT   STRAND       73     77
FT   HELIX        78     83
FT   STRAND       91     96
FT   STRAND      104    112
FT   HELIX       113    121
FT   HELIX       126    133
FT   STRAND      142    150
FT   STRAND      152    162
FT   STRAND      165    168
FT   STRAND      174    177
SQ   SEQUENCE   1284 AA;  141428 MW;  29B6C9B6E93FA6EF CRC64;
     MWSSDRLAGA GSGGAVVTVA FTNARDCFLH LPRRLVAQLH LLQNQAIEVA SDHQPTYLSW
     VEGRHFNDQS ENVAEINRQV GQKLGLSSGD QVFLRPCSHV VSCQQVEVEP LSADDWEILE
     LHAISLEQHL LDQIRIVFPK AVVPIWVDQQ TYIFIQIVTL MPAAPYGRLE TNTKLLIQPK
     TRQAKESTFP KEGDAHGQVH SYGREQKGLS KELQTRQLHT NSEGITASNG RDPKVPGGPL
     KPSWWAVLGS MLSFGPDSKQ ESAWGSLELG AFKNMQSQAA PLEGTFRVCQ VQPPSARTTT
     ATSVFHKHCT AHVFPWDQEY FDVEPSFTVT YGKLVKLHSP KQQQDKSKQG VLLPDKEKQL
     SKSPDHKQIS SNRSEEAAEA CVLKVVWNGL EELKNATEFT ESLELLHRGK VWIPDDLRKR
     LNIEMHAVVR ITPLETTPKI PRSLKLQPRE NLPKDVNEET IKTVFSSWVQ QSATTMLPLV
     ISKEERIKLE IKDGLREFSL STVHSQEKEK EEGKTVFVLS SILLQKISVQ VLLEPMIKEE
     QSAEIDFLLP SLTLSSLGGV SALGASAMEH ITHSLLGRPL SRQLMALVAG LRNGALLITG
     GKGSGKSTFA KAICKEAQDT LDARVETVDC KALRGKRLES IQKALEVAFS EAAWRQPSVI
     LLDDLDLIAG LPSVPEQEHS PEAVQSQRLA HALNDMIKEF VSTGSLVALI ATSQLQQSLH
     PSLVSAQGIH TFQCVQHLQP PNPEQRCEIL HSVVKNKLGC DISNFPDLDL QCIAKDTEAF
     VARDFTVLVD RAIHSSLSRQ HSSSREDLTL TTSDFQKALR GFLPASLRNV NLHKPRDLGW
     DKIGGLHEVR QILMDTIQLP AKYPELFANL PIRQRTGILL YGPPGTGKTL LAGVVARESG
     MNFISIKGPE LLSKYIGASE QAVRDVFIRA QAAKPCILFF DEFESIAPRR GHDNTGVTDR
     VVNQLLTQLD GVEGLQGVYV LAATSRPDLI DPALLRPGRL DKCVYCPPPD QVSRLEILTV
     LSKSLALADD VDLQHVASVT DSFTGADLKA LLYNAQLEAL QGRLLPSGLP DGGSSSDSDL
     SLSSMVFLNH SSGSDDSAGD GECGLEQSLL SLEMSEILPD ESKFNMYRLY FGSSYESELG
     NGTPSDLSSH CLSAPSSVTQ DLPAAPGKDP LFTQHPVFRT PSQEGCQDLT QEQRDQLRAE
     ISIIKGRYRS QSGEDESLNQ PGPIKTTFAI SQAHLMTALA HTRPSISEDE GKEFAELYEN
     FQNPKKRKNQ SGTVFRTGQK VTLA
//
ID   TUT7_MOUSE              Reviewed;        1491 AA.
AC   Q5BLK4; A1A4B1; Q3V3V7; Q8CIH3;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 3.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Terminal uridylyltransferase 7;
DE            Short=TUTase 7;
DE            EC=2.7.7.52;
DE   AltName: Full=Zinc finger CCHC domain-containing protein 6;
GN   Name=Zcchc6; Synonyms=Kiaa1711, Tut7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 110-1378.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Uridylyltransferase that mediates the terminal
CC       uridylation of some specific RNAs. Not involved in uridylation of
CC       precursor let-7 (pre-let-7) miRNA. Does not play a role in
CC       replication-dependent histone mRNA degradation (By similarity).
CC   -!- CATALYTIC ACTIVITY: UTP + RNA(n) = diphosphate + RNA(n+1).
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC   -!- SIMILARITY: Contains 3 CCHC-type zinc fingers.
CC   -!- SIMILARITY: Contains 2 PAP-associated domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH23438.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAH23880.1; Type=Erroneous initiation;
CC       Sequence=BAE20473.1; Type=Erroneous initiation;
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CC   -----------------------------------------------------------------------
DR   EMBL; BC023880; AAH23880.1; ALT_INIT; mRNA.
DR   EMBL; BC043111; AAH43111.1; -; mRNA.
DR   EMBL; BC023438; AAH23438.1; ALT_SEQ; mRNA.
DR   EMBL; AK031043; BAE20473.1; ALT_INIT; mRNA.
DR   IPI; IPI00262966; -.
DR   RefSeq; NP_705766.3; NM_153538.3.
DR   UniGene; Mm.233082; -.
DR   ProteinModelPortal; Q5BLK4; -.
DR   SMR; Q5BLK4; 995-1306.
DR   PhosphoSite; Q5BLK4; -.
DR   PRIDE; Q5BLK4; -.
DR   Ensembl; ENSMUST00000079643; ENSMUSP00000078588; ENSMUSG00000035248.
DR   GeneID; 214290; -.
DR   KEGG; mmu:214290; -.
DR   CTD; 214290; -.
DR   MGI; MGI:2387179; Zcchc6.
DR   GeneTree; ENSGT00550000074490; -.
DR   HOGENOM; HBG281061; -.
DR   InParanoid; Q5BLK4; -.
DR   OMA; CPEDFKR; -.
DR   OrthoDB; EOG40VVNP; -.
DR   NextBio; 374248; -.
DR   ArrayExpress; Q5BLK4; -.
DR   Bgee; Q5BLK4; -.
DR   CleanEx; MM_ZCCHC6; -.
DR   Genevestigator; Q5BLK4; -.
DR   GermOnline; ENSMUSG00000035248; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0050265; F:RNA uridylyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0031123; P:RNA 3'-end processing; ISS:UniProtKB.
DR   InterPro; IPR002058; PAP_assoc.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013084; Znf_CCH_retrovir.
DR   InterPro; IPR001878; Znf_CCHC.
DR   Gene3D; G3DSA:4.10.60.10; Znf_CCH_retrovir; 3.
DR   Pfam; PF03828; PAP_assoc; 2.
DR   Pfam; PF00098; zf-CCHC; 3.
DR   SMART; SM00355; ZnF_C2H2; 1.
DR   SMART; SM00343; ZnF_C2HC; 3.
DR   PROSITE; PS50158; ZF_CCHC; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Nucleotidyltransferase; Phosphoprotein; Repeat;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN         1   1491       Terminal uridylyltransferase 7.
FT                                /FTId=PRO_0000150958.
FT   DOMAIN      551    600       PAP-associated 1.
FT   DOMAIN     1230   1282       PAP-associated 2.
FT   ZN_FING     959    976       CCHC-type 1.
FT   ZN_FING    1341   1358       CCHC-type 2.
FT   ZN_FING    1447   1464       CCHC-type 3.
FT   COMPBIAS     20     23       Poly-Asp.
FT   COMPBIAS    791    933       Glu-rich.
FT   COMPBIAS   1363   1366       Poly-Arg.
FT   ACT_SITE   1056   1056       By similarity.
FT   MOD_RES      64     64       Phosphothreonine (By similarity).
FT   MOD_RES     132    132       Phosphoserine.
FT   MOD_RES     172    172       Phosphoserine (By similarity).
FT   CONFLICT    960    960       V -> L (in Ref. 1; AAH23438).
FT   CONFLICT    982    982       Q -> R (in Ref. 2; BAE20473).
FT   CONFLICT   1338   1338       P -> L (in Ref. 1; AAH43111).
FT   CONFLICT   1343   1343       C -> Y (in Ref. 2; BAE20473).
FT   CONFLICT   1472   1491       LSSKYMTQGRASVKRTQQES -> AFT (in Ref. 1;
FT                                AAH43111).
SQ   SEQUENCE   1491 AA;  169103 MW;  C574FCAC3781B3CC CRC64;
     MGDTAKPYFV KRTKDRGIID DDDFRRGHPQ QDYLIMDDYA KGHSSKMEKG LPKKKISPGN
     YGNTPRKGLY GVSSNPYAFK NPIYSQPAWM NDNHKDQNKK WLSDELAGNA DSWREFKPGP
     RIPVISRSRK ESFQESDDAY RWQEGRGCRA VRRLFQKDLS SLEAMSEMEA GSPENKKQRS
     RPRKPRRTRT EDSEQDGDLD GPVIDESVLS TKELLGLQQA EERLKRDCID RLKRRPRNCP
     TAKYTCKLCD ALIDSIPFAH KHIKEKRHKK NLKEKQEEEL LTTLPPPAPS QIHAVGSAID
     RVVQEFGLHS ENLDQRLEIK RVMESVFRHK LPDCSLRLYG SSCSRLGFRD SDVNIDVQFP
     AVMSQPDVLL LVQECLKNSD SFIDVDADFH ARVPVVVCRD KQSGLLCKVS AGNENAWLTT
     KHLTALGKLE PRLVPLVIAF RYWAKLCSID RPEEGGLPPY VFALMAVFFL QQRKEPLLPV
     YLGSWIEEFS LNKLGNFSLK DVEKDSVVWE YTDNSTGDTS SAKEEAPKET AAKKGQVPLT
     FNIKHQPSVP VGQLWVELLR FYALEFNLAD LVISIRVKEL ISRESKDWPK KRIAIEDPYS
     VKRNVARTLN NQPVFEYILH CLRTTYKYFA LPHKVTKPNL TKPPSPVTCV SDPYREAKNG
     GPEPQATNID KLGNAAVAQD PGVQTSGDCR AQLVTLKNTT EEVGSPAKEK TGGVHIPAHQ
     ESSGCVQAEV SCEGLEDATA ELPETGSDNE EVRRKTKHPL STDDQGLSSS KHPELQNCGS
     LCGLQADNTL ELVAEECNSC ASLDNKAEVN EERIEGAEEL EEAAALSCFS PSVQSRTSAA
     MHFDDEEEEE EEEEEEEPRL SINLTEDEEG VANEHQVDSR YAGSGEEDAL SEEDDLAEPA
     KGEDTGECGE NVGGTLLIDL NRITLKEESF PEEDLPGDQS EFFYEFRKLT FTKGKSPTVV
     CSLCKREGHL KKDCPEDFKR VQLEPLPPLT PKFSNILDQV CVQCYKDFSP TIVEDQAREH
     IRQNLESFIK QDFPGTKLSL FGSSKNGFGF KQSDLDVCMT INGHETAEGL DCVRTIEELA
     RVLRKHSGLR NILPITTAKV PIVKFFHLRS GLEVDISLYN TLALHNTRLL SAYSAIDPRV
     KYLCYTMKVF TKMCDIGDAS RGSLSSYAYT LMVLYFLQQR SPPVIPVLQE IYKGEKKPEI
     LVDGWNIYFF DQINELPTCW PEYGKNTEPV GQLWLGLLRF YTEEFDFKEH VISIRRKSLL
     TTFKKQWTSK YIVIEDPFDL NHNLGAGLSR KMTNFIMKAF INGRRVFGIP VKGFPKDNPS
     KLAYFFDPDV LTEGELAPND RCCRICGKIG HFMKDCPMRR KVRRRRDQED TPNQRYSESK
     EKRSKEDKEI QNKYTEKEVS TKEDKLTPCA AAKAKPVRAA VDLGREKLLR TPTEKWKRQD
     DRDSREKRCF ICGREGHIKK ECPQFKGSPG SLSSKYMTQG RASVKRTQQE S
//
ID   STB5L_MOUSE             Reviewed;        1185 AA.
AC   Q5DQR4; Q3TSM3; Q3UVG2; Q5DQR1; Q5DQR2; Q5DQR3; Q8BS52;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Syntaxin-binding protein 5-like;
DE   AltName: Full=Lethal(2) giant larvae protein homolog 4;
DE   AltName: Full=Tomosyn-2;
GN   Name=Stxbp5l; Synonyms=Llgl4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3 AND 4), AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=129/Ola;
RX   PubMed=15659226; DOI=10.1111/j.1471-4159.2004.02890.x;
RA   Groffen A.J.A., Jacobsen L., Schut D., Verhage M.;
RT   "Two distinct genes drive expression of seven tomosyn isoforms in the
RT   mammalian brain, sharing a conserved structure with a unique variable
RT   domain.";
RL   J. Neurochem. 92:554-568(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5; 6 AND 7).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588; SER-590; THR-593
RP   AND SER-598, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: May play a role in vesicle trafficking and exocytosis
CC       (Potential).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). Cell membrane;
CC       Peripheral membrane protein (Potential). Membrane; Peripheral
CC       membrane protein (Potential). Note=Cytoplasmic, and associated
CC       with vesicular membranes and the plasma membrane (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=1; Synonyms=Tomosyn-2 isoform xb;
CC         IsoId=Q5DQR4-1; Sequence=Displayed;
CC       Name=2; Synonyms=Tomosyn-2 isoform m;
CC         IsoId=Q5DQR4-2; Sequence=VSP_016296;
CC       Name=3; Synonyms=Tomosyn-2 isoform b;
CC         IsoId=Q5DQR4-3; Sequence=VSP_016295;
CC       Name=4; Synonyms=Tomosyn-2 isoform s;
CC         IsoId=Q5DQR4-4; Sequence=VSP_016295, VSP_016296;
CC       Name=5;
CC         IsoId=Q5DQR4-5; Sequence=VSP_016295, VSP_016297, VSP_016298;
CC       Name=6;
CC         IsoId=Q5DQR4-6; Sequence=VSP_016299;
CC       Name=7;
CC         IsoId=Q5DQR4-7; Sequence=VSP_016300;
CC   -!- TISSUE SPECIFICITY: Detected in hippocampus and cerebellum.
CC   -!- SIMILARITY: Belongs to the WD repeat L(2)GL family.
CC   -!- SIMILARITY: Contains 1 v-SNARE coiled-coil homology domain.
CC   -!- SIMILARITY: Contains 14 WD repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; AY542354; AAT68171.1; -; Genomic_DNA.
DR   EMBL; AY542328; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542329; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542331; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542330; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542332; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542334; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542336; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542338; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542340; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542349; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542348; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542347; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542346; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542345; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542344; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542343; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542342; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542341; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542353; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542352; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542351; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542350; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542339; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542337; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542335; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542333; AAT68171.1; JOINED; Genomic_DNA.
DR   EMBL; AY542354; AAT68172.1; -; Genomic_DNA.
DR   EMBL; AY542328; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542329; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542330; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542332; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542335; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542334; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542333; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542331; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542336; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542345; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542344; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542343; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542342; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542341; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542340; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542339; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542338; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542337; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542353; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542352; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542351; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542350; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542349; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542347; AAT68172.1; JOINED; Genomic_DNA.
DR   EMBL; AY542354; AAT68173.1; -; Genomic_DNA.
DR   EMBL; AY542328; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542329; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542331; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542332; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542330; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542333; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542335; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542337; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542340; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542349; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542348; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542347; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542345; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542338; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542344; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542343; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542342; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542341; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542353; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542352; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542351; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542350; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542339; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542336; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542334; AAT68173.1; JOINED; Genomic_DNA.
DR   EMBL; AY542354; AAT68174.1; -; Genomic_DNA.
DR   EMBL; AY542329; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542330; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542328; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542331; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542333; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542335; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542337; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542346; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542345; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542344; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542343; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542342; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542341; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542340; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542339; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542338; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542353; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542352; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542351; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542350; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542349; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542347; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542336; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542334; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542332; AAT68174.1; JOINED; Genomic_DNA.
DR   EMBL; AY542324; AAT68175.1; -; mRNA.
DR   EMBL; AY542325; AAT68176.1; -; mRNA.
DR   EMBL; AY542326; AAT68177.1; -; mRNA.
DR   EMBL; AY542327; AAT68178.1; -; mRNA.
DR   EMBL; AK035159; BAC28964.1; -; mRNA.
DR   EMBL; AK137325; BAE23307.1; -; mRNA.
DR   EMBL; AK161955; BAE36652.1; -; mRNA.
DR   IPI; IPI00309953; -.
DR   IPI; IPI00555072; -.
DR   IPI; IPI00555114; -.
DR   IPI; IPI00656181; -.
DR   IPI; IPI00656218; -.
DR   IPI; IPI00656258; -.
DR   IPI; IPI00656281; -.
DR   RefSeq; NP_001108083.1; NM_001114611.1.
DR   RefSeq; NP_001108084.1; NM_001114612.1.
DR   RefSeq; NP_001108085.1; NM_001114613.1.
DR   RefSeq; NP_766028.2; NM_172440.3.
DR   UniGene; Mm.403226; -.
DR   UniGene; Mm.80170; -.
DR   ProteinModelPortal; Q5DQR4; -.
DR   SMR; Q5DQR4; 206-283, 515-543, 1121-1177.
DR   STRING; Q5DQR4; -.
DR   PhosphoSite; Q5DQR4; -.
DR   PRIDE; Q5DQR4; -.
DR   Ensembl; ENSMUST00000096074; ENSMUSP00000093779; ENSMUSG00000022829.
DR   Ensembl; ENSMUST00000114778; ENSMUSP00000110426; ENSMUSG00000022829.
DR   Ensembl; ENSMUST00000114787; ENSMUSP00000110435; ENSMUSG00000022829.
DR   Ensembl; ENSMUST00000114789; ENSMUSP00000110437; ENSMUSG00000022829.
DR   Ensembl; ENSMUST00000114790; ENSMUSP00000110438; ENSMUSG00000022829.
DR   GeneID; 207227; -.
DR   KEGG; mmu:207227; -.
DR   UCSC; uc007zds.1; mouse.
DR   UCSC; uc007zdt.1; mouse.
DR   UCSC; uc007zdu.1; mouse.
DR   UCSC; uc007zdv.1; mouse.
DR   UCSC; uc007zdw.1; mouse.
DR   UCSC; uc007zdx.1; mouse.
DR   UCSC; uc007zdy.1; mouse.
DR   CTD; 207227; -.
DR   MGI; MGI:2443815; Stxbp5l.
DR   eggNOG; roNOG08974; -.
DR   GeneTree; ENSGT00390000000018; -.
DR   HOVERGEN; HBG083064; -.
DR   InParanoid; Q5DQR4; -.
DR   OMA; IRTSYQS; -.
DR   PhylomeDB; Q5DQR4; -.
DR   NextBio; 371908; -.
DR   ArrayExpress; Q5DQR4; -.
DR   Bgee; Q5DQR4; -.
DR   CleanEx; MM_STXBP5L; -.
DR   Genevestigator; Q5DQR4; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000664; Lethal2_giant.
DR   InterPro; IPR013905; Lgl_C.
DR   InterPro; IPR013577; LLGL2.
DR   InterPro; IPR001388; Synaptobrevin.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 3.
DR   Pfam; PF08596; Lgl_C; 1.
DR   Pfam; PF08366; LLGL; 1.
DR   Pfam; PF00400; WD40; 2.
DR   PRINTS; PR00962; LETHAL2GIANT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS50892; V_SNARE; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 3.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW   Exocytosis; Membrane; Phosphoprotein; Protein transport; Repeat;
KW   Transport; WD repeat.
FT   CHAIN         1   1185       Syntaxin-binding protein 5-like.
FT                                /FTId=PRO_0000051248.
FT   REPEAT       73    106       WD 1.
FT   REPEAT      113    152       WD 2.
FT   REPEAT      157    193       WD 3.
FT   REPEAT      212    246       WD 4.
FT   REPEAT      252    284       WD 5.
FT   REPEAT      306    348       WD 6.
FT   REPEAT      356    390       WD 7.
FT   REPEAT      412    489       WD 8.
FT   REPEAT      517    628       WD 9.
FT   REPEAT      642    704       WD 10.
FT   REPEAT      831    888       WD 11.
FT   REPEAT      897    968       WD 12.
FT   REPEAT      973   1017       WD 13.
FT   REPEAT     1031   1054       WD 14.
FT   DOMAIN     1120   1180       v-SNARE coiled-coil homology.
FT   MOD_RES     588    588       Phosphoserine.
FT   MOD_RES     590    590       Phosphoserine.
FT   MOD_RES     593    593       Phosphothreonine.
FT   MOD_RES     598    598       Phosphoserine.
FT   VAR_SEQ     157   1185       Missing (in isoform 7).
FT                                /FTId=VSP_016300.
FT   VAR_SEQ     467   1185       Missing (in isoform 6).
FT                                /FTId=VSP_016299.
FT   VAR_SEQ     703    727       DNFCMRGLSNFYPDLTKRIRTSYQS -> G (in
FT                                isoform 3, isoform 4 and isoform 5).
FT                                /FTId=VSP_016295.
FT   VAR_SEQ     749    805       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_016296.
FT   VAR_SEQ    1006   1025       SLPSLRPMLDVNYLPLTDMR -> RYMVYLLLTDNHNNASK
FT                                VKW (in isoform 5).
FT                                /FTId=VSP_016297.
FT   VAR_SEQ    1026   1185       Missing (in isoform 5).
FT                                /FTId=VSP_016298.
SQ   SEQUENCE   1185 AA;  131844 MW;  0F797A5CF20E05DC CRC64;
     MKKFNFRKVL DGLTASSPGS GSSSGSNSGG AGSGSVHPGG TAGLPREEIQ ESLTSDYFQI
     CKTVRHGFPY QPTALAFDPV QKILAIGTRT GAIRILGRPG VDCYCQHESG AAVLQLQFLI
     NEGALVSASS DDTLHLWNLR QKRPAILHSL KFNRERITYC HLPFQSKWLY VGTERGNTHI
     VNIESFILSG YVIMWNKAIE LSTKTHPGPV VHLSDSPRDE GKLLIGYENG TVVFWDLKSK
     RAELRVYYDE AIHSIDWHHE GKQFMCSHSD GSLTLWNLKS PSRPFQTTVP HGKSQREGRK
     SESCKPILKV EYKTCRNSEP FIIFSGGLSY DKACRRPSLT IMHGKAITVL EMDHPIVEFL
     TLCETPYPNE FQEPYAVAVL LEKDLIVVDL TQTNFPIFEN PYPMDIHESP VTCTAYFADC
     PPDLILVLYS IGVKHKKQGY SNKEWPVSGG AWNLGAQTYP EIIITGHADG TIKFWDASAM
     TLQMLYKLKT SKVFEKQKAG EGKQTCELVE EDPFAVQMIY WCPESRIFCV SGVSAYVIIY
     KFSRHEVTTE IVSLEVRLQC DVEDIITPEP ETSPPFPDLS SQLPPSRSLS GSTNTVSSEG
     VTKDSIPCLS VKTRPVRMPP GYQADLVIQL VWVDGEPPQQ ITSLSISSAY GIVAFGNCTG
     LVVVDFIQKT VLLSMGTIDL YRSSDLYQRQ PRSPRKNRQF IADNFCMRGL SNFYPDLTKR
     IRTSYQSLTE LNDSPVPLEL ERCKSPTSDH VNGHCTSPTS QSCSSGKRLS SADVSKVNRW
     GPGRPPFRKA QSAACMEISL PVTTEETREN SYNRSRSSSI SSIDKDSKEA ITALYFMESF
     ARKNDSTVSP CLFVGTSLGM VVLISLNLPS SDEQRFTEPV VVLPSGTFLS LKGAVLTFSC
     MDRTGSLMQP PYEVWRDPNN TDENEKTWKR KLVMNYSSSS QEMGDHQYTI ICSEKQAKVF
     SLPSQTCLYV HNITETSFIL QADVVVMCNS ACLACFCANG HIMIMSLPSL RPMLDVNYLP
     LTDMRIARTF CFTNEGQALY LVSPTEIQRL TYSQEMCDNI QDMLGDLFTP IETPEAQNRG
     FLKGLFGGSG QTFDREELFG EASAGKASRS LAQHIPGPGS IEGMKGAAGG VMGELTRARI
     ALDERGQRLG ELEEKTAGMM TSAEAFSKHA HELMLKYKDK KWYQF
//
ID   Q5DTG5_MOUSE            Unreviewed;      1123 AA.
AC   Q5DTG5;
DT   29-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   29-MAR-2005, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   SubName: Full=MKIAA4228 protein;
DE   Flags: Fragment;
GN   Name=Zfhx3; Synonyms=Atbf1, mKIAA4228;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the Coding Sequences of Mouse Homologues of KIAA Gene.
RT   The Complete Nucleotide Sequences of Mouse KIAA-homologous cDNAs
RT   Identified by Screening of Terminal sequences of cDNA Clones Randomly
RT   Sampled from Size-Fractionated Libraries..";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
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DR   EMBL; AK220555; BAD90323.1; -; mRNA.
DR   IPI; IPI00475055; -.
DR   UniGene; Mm.416972; -.
DR   UniGene; Mm.477670; -.
DR   ProteinModelPortal; Q5DTG5; -.
DR   STRING; Q5DTG5; -.
DR   Ensembl; ENSMUST00000043896; ENSMUSP00000044612; ENSMUSG00000038872.
DR   MGI; MGI:99948; Zfhx3.
DR   eggNOG; roNOG04812; -.
DR   InParanoid; Q5DTG5; -.
DR   ArrayExpress; Q5DTG5; -.
DR   Bgee; Q5DTG5; -.
DR   Genevestigator; Q5DTG5; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001356; Homeobox.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 2.
DR   Pfam; PF00046; Homeobox; 2.
DR   SMART; SM00389; HOX; 2.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   SUPFAM; SSF46689; Homeodomain_like; 2.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 2.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Homeobox; Nucleus.
FT   NON_TER       1      1
SQ   SEQUENCE   1123 AA;  120392 MW;  A1E1323C6F03706F CRC64;
     QIPASSATSP STPTSTMNTL KRKLEEKASA SPGENDSGTG GEEPQRDKRL RTTITPEQLE
     ILYQKYLLDS NPTRKMLDHI AHEVGLKKRV VQVWFQNTRA RERKGQFRAV GPAQAHRRCP
     FCRALFKAKT ALEAHIRSRH WHEAKRAGYN LTLSAMLLDC DGGLQMKGDI FDGTSFSHLP
     PSSSDGQGVP LSPVSKTMEL SPRTLLSPSS IKVEGIEDFE SPSMSSVNLN FDQTKLDNDD
     CSSVNTAITD TTTGDEGNAD NDSATGIATE TKSSAPNEGL TKAAMMAMSE YEDRLSSGLV
     SPAPSFYSKE YDNEGTVDYS ETSSLADPCS PSPGASGSAG KSGDGGDRPG QKRFRTQMTN
     LQLKVLKSCF NDYRTPTMLE CEVLGNDIGL PKRVVQVWFQ NARAKEKKSK LSMAKHFGIN
     QTSYEGPKTE CTLCGIKYSA RLSVRDHIFS QQHISKVKDT IGSQLDKEKE YFDPATVRQL
     MAQQELDRIK KANEVLGLAA QQQGMFDNAP LQALNLPTTY PALQGIPPVL LPGLNSPSLP
     GFTPANTALT SPKPNLMGLP STTVPSPGLP TSGLPNKPSS ASLSSPTPAQ ATMAMAPQPP
     PQPQQPQPPV QQPPPPPAAQ QIPAPQLTPQ QQRKDKDGEK GKEKEKAHKG KGEPLPVPKK
     EKGEAPPAAT ATISAPLPAM EYAVDPAQLQ ALQAALTSDP TALLTSQFLP YFVPGFSPYY
     APQIPGALQS GYLQPMYGME GLFPYSPALS QALMGLSPGS LLQQYQQYQQ SLQEAIQQQQ
     QQQQQQQQQQ QQQQRQLQQQ QQQQQQKVQQ QQQQQQQPKA SQTPVPQGPA SPDKDPAKES
     PKPEEQKNVP REVSPLLPKP PEEPEAESKS ASADSLCDPF IVPKVQYKLV CRKCQAGFGD
     EEAARSHLKS LCCFGQSVVN LQEMVLHVPT GSGGGGGGGG GSGGGGGSYH CLACESALCG
     EEALSQHLES ALHKHRTITR AARNAKEHPS LLPHSACFPD PSTASTSQSA AHSNDSPPPP
     SAAPSSSASP HASRKSWPPV GSRASAAKPP SFPPLSSSST VTSSSCSTSG VQPSMPTDDY
     SEESDTDLSQ KSDGPASPVE GPKDPSCPKD SGLTSVGTDT FRL
//
ID   Q5DTI3_MOUSE            Unreviewed;       320 AA.
AC   Q5DTI3;
DT   29-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   29-MAR-2005, sequence version 1.
DT   08-MAR-2011, entry version 36.
DE   SubName: Full=MKIAA4194 protein;
DE   Flags: Fragment;
GN   Name=Syt2; Synonyms=mKIAA4194;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the Coding Sequences of Mouse Homologues of KIAA Gene.
RT   The Complete Nucleotide Sequences of Mouse KIAA-homologous cDNAs
RT   Identified by Screening of Terminal sequences of cDNA Clones Randomly
RT   Sampled from Size-Fractionated Libraries..";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 2 C2 domains.
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DR   EMBL; AK220537; BAD90531.1; -; mRNA.
DR   IPI; IPI00129622; -.
DR   UniGene; Mm.5102; -.
DR   ProteinModelPortal; Q5DTI3; -.
DR   STRING; Q5DTI3; -.
DR   Ensembl; ENSMUST00000027721; ENSMUSP00000027721; ENSMUSG00000026452.
DR   Ensembl; ENSMUST00000121990; ENSMUSP00000112438; ENSMUSG00000026452.
DR   MGI; MGI:99666; Syt2.
DR   HOVERGEN; HBG108530; -.
DR   InParanoid; Q5DTI3; -.
DR   ArrayExpress; Q5DTI3; -.
DR   Bgee; Q5DTI3; -.
DR   Genevestigator; Q5DTI3; -.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0008021; C:synaptic vesicle; IEA:InterPro.
DR   GO; GO:0042598; C:vesicular fraction; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   InterPro; IPR001565; Synaptotagmin.
DR   Pfam; PF00168; C2; 2.
DR   PRINTS; PR00360; C2DOMAIN.
DR   PRINTS; PR00399; SYNAPTOTAGMN.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 2.
PE   2: Evidence at transcript level;
KW   Repeat.
FT   NON_TER       1      1
SQ   SEQUENCE   320 AA;  36063 MW;  8AADA18399B7823E CRC64;
     KGMKNAMNMK DMKGGQDDDD AETGLTEGEG EGEEEKEPEN LGKLQFSLDY DFQANQLTVG
     VLQAAELPAL DMGGTSDPYV KVFLLPDKKK KYETKVHRKT LNPAFNETFT FKVPYQELGG
     KTLVMAIYDF DRFSKHDIIG EVKVPMNTVD LGQPIEEWRD LQGGEKEEPE KLGDICTSLR
     YVPTAGKLTV CILEAKNLKK MDVGGLSDPY VKIHLMQNGK RLKKKKTTVK KKTLNPYFNE
     SFSFEIPFEQ IQKVQVVVTV LDYDKLGKNE AIGKIFVGSN ATGTELRHWS DMLANPRRPI
     AQWHSLKPEE EVDALLGKNK
//
ID   MYPN_MOUSE              Reviewed;        1315 AA.
AC   Q5DTJ9; Q7TPW5; Q8BZ76;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Myopalladin;
GN   Name=Mypn; Synonyms=Kiaa4170;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-754.
RC   STRAIN=C57BL/6J; TISSUE=Bone;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1053-1315.
RC   STRAIN=C57BL/6J; TISSUE=Blastocyst;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Component of the sarcomere that tethers together nebulin
CC       (skeletal muscle) and nebulette (cardiac muscle) to alpha-actinin,
CC       at the Z lines (By similarity).
CC   -!- SUBUNIT: Interacts with TTN/titin, NEB, NEBL, ACTN2 and CARP (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus (By similarity).
CC       Cytoplasm, myofibril, sarcomere. Note=Bound to sarcomere both at
CC       the Z-line periphery and in the central I-band region.
CC   -!- SIMILARITY: Belongs to the myotilin/palladin family.
CC   -!- SIMILARITY: Contains 5 Ig-like (immunoglobulin-like) domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90521.1; Type=Erroneous initiation;
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DR   EMBL; AK220521; BAD90521.1; ALT_INIT; mRNA.
DR   EMBL; AK036458; BAC29439.1; -; mRNA.
DR   EMBL; BC052872; AAH52872.1; -; mRNA.
DR   IPI; IPI00929815; -.
DR   RefSeq; NP_892037.2; NM_182992.2.
DR   UniGene; Mm.259767; -.
DR   ProteinModelPortal; Q5DTJ9; -.
DR   SMR; Q5DTJ9; 264-533, 935-1294.
DR   STRING; Q5DTJ9; -.
DR   PhosphoSite; Q5DTJ9; -.
DR   PRIDE; Q5DTJ9; -.
DR   Ensembl; ENSMUST00000095580; ENSMUSP00000093240; ENSMUSG00000020067.
DR   GeneID; 68802; -.
DR   KEGG; mmu:68802; -.
DR   UCSC; uc007fjy.1; mouse.
DR   CTD; 68802; -.
DR   MGI; MGI:1916052; Mypn.
DR   eggNOG; roNOG13559; -.
DR   GeneTree; ENSGT00590000083007; -.
DR   HOGENOM; HBG564663; -.
DR   HOVERGEN; HBG059166; -.
DR   InParanoid; Q5DTJ9; -.
DR   OMA; ETIPFTR; -.
DR   OrthoDB; EOG4ZKJKH; -.
DR   ArrayExpress; Q5DTJ9; -.
DR   Bgee; Q5DTJ9; -.
DR   CleanEx; MM_MYPN; -.
DR   Genevestigator; Q5DTJ9; -.
DR   GermOnline; ENSMUSG00000020067; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 5.
DR   Pfam; PF07679; I-set; 5.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 4.
DR   PROSITE; PS50835; IG_LIKE; 5.
PE   2: Evidence at transcript level;
KW   Actin-binding; Coiled coil; Cytoplasm; Disulfide bond;
KW   Immunoglobulin domain; Nucleus; Phosphoprotein; Repeat.
FT   CHAIN         1   1315       Myopalladin.
FT                                /FTId=PRO_0000240490.
FT   DOMAIN      267    357       Ig-like 1.
FT   DOMAIN      432    528       Ig-like 2.
FT   DOMAIN      941   1025       Ig-like 3.
FT   DOMAIN     1068   1157       Ig-like 4.
FT   DOMAIN     1167   1257       Ig-like 5.
FT   COILED      219    240       Potential.
FT   COMPBIAS    779    852       Pro-rich.
FT   MOD_RES      99     99       Phosphoserine (By similarity).
FT   MOD_RES     249    249       Phosphothreonine (By similarity).
FT   MOD_RES     253    253       Phosphoserine (By similarity).
FT   MOD_RES     754    754       Phosphoserine (By similarity).
FT   MOD_RES     809    809       Phosphoserine (By similarity).
FT   MOD_RES     814    814       Phosphoserine (By similarity).
FT   MOD_RES     924    924       Phosphoserine (By similarity).
FT   DISULFID    288    339       By similarity.
FT   DISULFID    453    512       By similarity.
FT   DISULFID   1089   1141       By similarity.
FT   CONFLICT   1120   1120       E -> G (in Ref. 3; AAH52872).
SQ   SEQUENCE   1315 AA;  144114 MW;  3CBA735F63983B3F CRC64;
     MQEDSIEAST SISQLLRESY LAETRHRGDN ERSRAEPSSN PFHFSGPGAA EGGGPEDLPD
     LSAFLSQEEL DESVNLARLA INHDPLERVD EAQARKRLSS DQTKHASKPS FEPAFHQDSS
     RGPASPKDSP PETKRPQYSS ETQSKKVFLN KAADFIEELS SLFKAHSSKR IRPRACKNHK
     SKTESQNKVL QENSPTFSDL TERRERASVP IPIPADSRDN ELNHAIEQRE AKRREAELAA
     GEAAAGDSTP GSSPSSLYYE EPLGQPPRFT QKLRSREVPE GSRVQLDCIV VGIPPPQVRW
     YCEGKELENS PDIHIVQAGN LHSLTIAEAF EEDTGRYSCF ASNIYGTDST SAEIYIEGVS
     SSDSEGDPNK EEMNRIQKPN EVSSPPTTSA AIPPAAEAQP LAAQPRVSTV QQCQSPTNYL
     QGLNGKPIIA APVFTKMLQN LSASEGQLVV FECRVKGAPS PKVEWYREGT LIEDSPDFRI
     LQKKPRSMAE PEEICTLVIA EVFSEDSGCF TCTASNKYGT VSSIAQLDVR GNEDISDNGA
     LHSANSTTNP AVAEHQPSPL NPQPLSEEQP PKPKLEGVLV NHNEPRSSSR IGLRVHFNLP
     EDDKDMEASS GSGAANTSQT RPNSFPERFN GQEARIPEPS SPIKEPPPVL AKPKLDSTQL
     QQLHNQVLLE QQQLQNTSPS SPKESLHMSA LNSAPPAVTI SSKQVKGPAP QMFNLARPKH
     FFPASSTSTA TVSPSSSPVF TLSNTPQTIQ RTVSKESLLM AHPSTQGRSP GGLSIQNEPA
     PPSPAEPAAP PTAAYSIPSG NQFQPHCVSP TPVSPTGRIQ NPVAFLSSVL PSLPSIPPTN
     AMGLPKSAPS VPSQGLMKKT TKAPQAVSDD YIRETKNSVI LDLGKKVNFG DVRSHQQEYK
     ISSFEQRLMN EIEFRLERTP VDESDDEIEH DEIPTGKCIA PIFDKRLKHF RVTEGSPVTF
     TCKIVGIPVP KVYWFKDGKQ ISKRNEHCKM RREGDGTCSL HIESTHGDDD GNYTIMAANP
     QGRISCSGHL MVQGLPIRSR LSPALSHRGR SRMQERDKEP LQERFFRPHF LQAPGDMVAH
     EGRLCRLDCK VSGLPPPELT WLLNGQPVLP DASHKMLVRE TGVHSLLIDP LTQRDAGTYT
     CVATNKTGQN SFSLELTVVA KEVKKAPVIL EKLQNSGVPE GHPVRLEGRV IGMPPPVFYW
     KKDNETIPFT RERISMHQDT TGYVCLLIQP AKKSDAGWYT LSAKNEAGIV SCTARLDIYA
     QWHQQIPTPI SIRPSGSRYG SLTSKGLDIF SAFSSVESTM LYSCTSRSVV ESDEL
//
ID   Q5DTL1_MOUSE            Unreviewed;      1022 AA.
AC   Q5DTL1;
DT   29-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   29-MAR-2005, sequence version 1.
DT   30-NOV-2010, entry version 43.
DE   SubName: Full=MKIAA4150 protein;
DE   Flags: Fragment;
GN   Name=Golga2; Synonyms=mKIAA4150;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the Coding Sequences of Mouse Homologues of KIAA Gene.
RT   The Complete Nucleotide Sequences of Mouse KIAA-homologous cDNAs
RT   Identified by Screening of Terminal sequences of cDNA Clones Randomly
RT   Sampled from Size-Fractionated Libraries..";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
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DR   EMBL; AK220509; BAD90300.1; -; mRNA.
DR   IPI; IPI00755997; -.
DR   RefSeq; NP_001074437.1; NM_001080968.1.
DR   RefSeq; NP_598613.2; NM_133852.2.
DR   UniGene; Mm.106376; -.
DR   ProteinModelPortal; Q5DTL1; -.
DR   STRING; Q5DTL1; -.
DR   Ensembl; ENSMUST00000100194; ENSMUSP00000097768; ENSMUSG00000002546.
DR   GeneID; 99412; -.
DR   KEGG; mmu:99412; -.
DR   UCSC; uc008jev.1; mouse.
DR   CTD; 99412; -.
DR   MGI; MGI:2139395; Golga2.
DR   HOGENOM; HBG505627; -.
DR   HOVERGEN; HBG051752; -.
DR   InParanoid; Q5DTL1; -.
DR   NextBio; 353919; -.
DR   ArrayExpress; Q5DTL1; -.
DR   Bgee; Q5DTL1; -.
DR   Genevestigator; Q5DTL1; -.
DR   GO; GO:0005801; C:cis-Golgi network; IDA:MGI.
PE   1: Evidence at protein level;
FT   NON_TER       1      1
SQ   SEQUENCE   1022 AA;  115668 MW;  FEFAF8135AD8C1CC CRC64;
     GFPPPRPGMS EETRQSKLAA AKKKLREYQQ KNSPGVPAGA KKKKKIKNGH SPERPTASDC
     QSPENIKDIL KVLVSDLNRS NGVSLPPLDK RKVPTDHIAP APPTAATDTM FLGVTPSPDA
     DLTQSHDAGN CSNLMEETKT FSSTESLRQL SQQLNGLVSE STSYINGEGL TSSNMKELEN
     RYQELAVALD SSYVTNKQLS STIEELKQQN QDTLDQLEKE KKDYQQKLAK EQGSLREQLQ
     VHIQTIGILV SEKAELQTAL AHTQQAARQK AGESEDLASR LQSSRQRVGE LERTLSTVST
     QQKQADRYNK DLTKERDALK LELYKNSKSN EDLRQQNSEL EEKLRVLVAE KAAAQLGVEE
     LQKKLEMSEL LLQQFSSQSS AAGGNEQLQH AMEERAQLET HVSQLMESLK QLQVERDQYA
     ENLKGESAMW QQRVQQMAEQ VHTLKEEKEH RERQVQELET SLAALRSQME EPPPPEPPAG
     PSEAEEQLQG EVEQLHKELE RLTGQLRAQV QDNESLSHLN REQEGRLLEL EREAQRWSEQ
     AEERKQILES MQSDRTTISR ALSQNRELKE QLAELQNGFV RLTNENMEIT SALQSEQHVK
     KELARKLGEL QERLGELKET VELKSQEAQG LQEQRDQCLS HLQQYAAAYQ QHLAAYEQLT
     SEKEAIHKQL LLQTQLMDQL QHEEVQGKMA AELARQELQE AQERLKATSQ ENQQLQAQLS
     LLVLPGEGDV DQEEEDEEVP QSSLAIPEDL DSREAMVAFF NAAIARAEEE QARLRVQLKE
     QKARCRSLSH LAAPVQSKLE KEAVVPRNVD DSASEESNQA LHVAMEKLQS RFLEVMQEKV
     ELKERVEELE HCCIQLSGET DTIGEYIALY QNQRAVLKAR HLEKEEYISR LAQDKEEMKV
     KLLELQELVL RLVNERNEWQ GKFLAVSQNP GDVLTPVPTG SQEFGAADQQ DDLREVSLAD
     DIEPAQGEAG VPAPHENPTA QQIMQLLREI QNPRERPGLG SNPCIPFFYR ADENDEVKIM
     VV
//
ID   S4A10_MOUSE             Reviewed;        1118 AA.
AC   Q5DTL9; Q8CFS3; Q9EST0;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Sodium-driven chloride bicarbonate exchanger;
DE   AltName: Full=Solute carrier family 4 member 10;
GN   Name=Slc4a10; Synonyms=Kiaa4136, Ncbe;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE
RP   SPECIFICITY.
RX   MEDLINE=20519648; PubMed=10993873; DOI=10.1074/jbc.C000456200;
RA   Wang C.-Z., Yano H., Nagashima K., Seino S.;
RT   "The Na+-driven Cl-/HCO3- exchanger. Cloning, tissue distribution, and
RT   functional characterization.";
RL   J. Biol. Chem. 275:35486-35490(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=14592810; DOI=10.1152/ajpcell.00240.2003;
RA   Praetorius J., Nejsum L.N., Nielsen S.;
RT   "A SCL4A10 gene product maps selectively to the basolateral plasma
RT   membrane of choroid plexus epithelial cells.";
RL   Am. J. Physiol. 286:C601-C610(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Electrogenic sodium/bicarbonate cotransporter in
CC       exchange for intracellular chloride. Plays an important role in
CC       regulating intracellular pH.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Note=Localizes to the basolateral membrane (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5DTL9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5DTL9-2; Sequence=VSP_019654;
CC   -!- TISSUE SPECIFICITY: Expressed in pancreatic islets and in the
CC       brain, in the epithelial cells of the choroid plexus.
CC   -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90511.1; Type=Erroneous initiation;
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DR   EMBL; AB033759; BAB17922.1; -; mRNA.
DR   EMBL; AK220501; BAD90511.1; ALT_INIT; mRNA.
DR   EMBL; BC039226; AAH39226.1; -; mRNA.
DR   IPI; IPI00555118; -.
DR   IPI; IPI00752501; -.
DR   RefSeq; NP_291030.2; NM_033552.2.
DR   UniGene; Mm.314497; -.
DR   ProteinModelPortal; Q5DTL9; -.
DR   SMR; Q5DTL9; 115-455, 493-534, 953-985.
DR   STRING; Q5DTL9; -.
DR   TCDB; 2.A.31.2.3; anion exchanger (AE) family.
DR   PhosphoSite; Q5DTL9; -.
DR   PRIDE; Q5DTL9; -.
DR   Ensembl; ENSMUST00000102735; ENSMUSP00000099796; ENSMUSG00000026904.
DR   Ensembl; ENSMUST00000112480; ENSMUSP00000108099; ENSMUSG00000026904.
DR   GeneID; 94229; -.
DR   KEGG; mmu:94229; -.
DR   UCSC; uc008jve.1; mouse.
DR   UCSC; uc008jvf.1; mouse.
DR   CTD; 94229; -.
DR   MGI; MGI:2150150; Slc4a10.
DR   GeneTree; ENSGT00560000076851; -.
DR   HOGENOM; HBG355640; -.
DR   HOVERGEN; HBG004326; -.
DR   InParanoid; Q5DTL9; -.
DR   OMA; LLTQYSC; -.
DR   OrthoDB; EOG45B1DS; -.
DR   PhylomeDB; Q5DTL9; -.
DR   NextBio; 352235; -.
DR   ArrayExpress; Q5DTL9; -.
DR   Bgee; Q5DTL9; -.
DR   Genevestigator; Q5DTL9; -.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0006885; P:regulation of pH; IDA:MGI.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR011531; HCO3_transpt_C.
DR   InterPro; IPR013769; HCO3_transpt_cyt.
DR   InterPro; IPR003020; HCO3_transpt_euk.
DR   InterPro; IPR003024; Na/HCO3_transpt.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   Gene3D; G3DSA:3.40.1100.10; HCO3_transpt_cyt; 2.
DR   PANTHER; PTHR11453; HCO3_transpt_euk; 1.
DR   Pfam; PF07565; Band_3_cyto; 1.
DR   Pfam; PF00955; HCO3_cotransp; 1.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   PRINTS; PR01232; NAHCO3TRSPRT.
DR   SUPFAM; SSF55804; PTrfase/Anion_transptr; 1.
DR   TIGRFAMs; TIGR00834; ae; 1.
DR   PROSITE; PS00219; ANION_EXCHANGER_1; FALSE_NEG.
DR   PROSITE; PS00220; ANION_EXCHANGER_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Antiport; Cell membrane; Ion transport;
KW   Membrane; Phosphoprotein; Sodium; Sodium transport; Symport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1   1118       Sodium-driven chloride bicarbonate
FT                                exchanger.
FT                                /FTId=PRO_0000245241.
FT   TOPO_DOM      1    509       Cytoplasmic (Potential).
FT   TRANSMEM    510    530       Helical; (Potential).
FT   TOPO_DOM    531    538       Extracellular (Potential).
FT   TRANSMEM    539    559       Helical; (Potential).
FT   TOPO_DOM    560    562       Cytoplasmic (Potential).
FT   TRANSMEM    563    583       Helical; (Potential).
FT   TOPO_DOM    584    596       Extracellular (Potential).
FT   TRANSMEM    597    617       Helical; (Potential).
FT   TOPO_DOM    618    626       Cytoplasmic (Potential).
FT   TRANSMEM    627    647       Helical; (Potential).
FT   TOPO_DOM    648    720       Extracellular (Potential).
FT   TRANSMEM    721    741       Helical; (Potential).
FT   TOPO_DOM    742    762       Cytoplasmic (Potential).
FT   TRANSMEM    763    783       Helical; (Potential).
FT   TOPO_DOM    784    809       Extracellular (Potential).
FT   TRANSMEM    810    830       Helical; (Potential).
FT   TOPO_DOM    831    855       Cytoplasmic (Potential).
FT   TRANSMEM    856    876       Helical; (Potential).
FT   TOPO_DOM    877    912       Extracellular (Potential).
FT   TRANSMEM    913    933       Helical; (Potential).
FT   TOPO_DOM    934    935       Cytoplasmic (Potential).
FT   TRANSMEM    936    956       Helical; (Potential).
FT   TOPO_DOM    957    998       Extracellular (Potential).
FT   TRANSMEM    999   1019       Helical; (Potential).
FT   TOPO_DOM   1020   1118       Cytoplasmic (Potential).
FT   MOD_RES      89     89       Phosphoserine.
FT   MOD_RES     238    238       Phosphoserine (By similarity).
FT   VAR_SEQ     287    316       Missing (in isoform 2).
FT                                /FTId=VSP_019654.
FT   CONFLICT    239    239       F -> L (in Ref. 1; BAB17922).
FT   CONFLICT    256    256       Missing (in Ref. 3; AAH39226).
FT   CONFLICT    345    345       T -> A (in Ref. 1; BAB17922).
FT   CONFLICT    487    487       I -> M (in Ref. 1; BAB17922).
FT   CONFLICT    796    797       RD -> IY (in Ref. 1; BAB17922).
SQ   SEQUENCE   1118 AA;  125817 MW;  85E3110C976978A7 CRC64;
     MEIKDQGAQM EPLLPTRNDE EAVVDRGGTR SILKTHFEKE DLEGHRTLFI GVHVPLGGRK
     SHRRHRHRGH KHRKRDRERD SGLEDGRESP SFDTPSQRVQ FILGTEDDDE EHLPHDLFTE
     LDEICWREGE DAEWRETARW LKFEEDVEDG GERWSKPYVA TLSLHSLFEL RSCILNGTVL
     LDMHANTIEE IADMVLDQQV SSGQLNEDVR HRVHEALMKQ HHHQNQKKLA NRIPIVRSFA
     DIGKKQSEPN SMDKNAGQVV SPQSAPACAE NKNDVSRENS TVDFSKGLGG QQKGHTSPCG
     MKQRLDKGPP HQQEREVDLH FMKKIPPGAE ASNILVGELE FLDRTVVAFV RLSPAVLLQG
     LAEVPIPSRF LFILLGPLGK GQQYHEIGRS IATLMTDEVF HDVAYKAKDR NDLVSGIDEF
     LDQVTVLPPG EWDPSIRIEP PKNVPSQEKR KIPAVPNGTA AHGEAEPHGG HSGPELQRTG
     RIFGGLILDI KRKAPFFWSD FRDAFSLQCL ASFLFLYCAC MSPVITFGGL LGEATEGRIS
     AIESLFGASM TGIAYSLFGG QPLTILGSTG PVLVFEKILF KFCKEYGLSY LSLRASIGLW
     TATLCIILVA TDASSLVCYI TRFTEEAFAS LICIIFIYEA LEKLFELSET YPINMHNDLE
     LLTQYSCNCM EPHSPSNDTL KEWRESNLSA SDIIWGNLTV SECRSLHGEY VGRACGHGHP
     YVPDVLFWSV ILFFSTVTMS ATLKQFKTSR YFPTKVRSIV SDFAVFLTIL CMVLIDYAIG
     IPSPKLQVPS VFKPTRDDRG WFVTPLGPNP WWTIIAAIIP ALLCTILIFM DQQITAVIIN
     RKEHKLKKGC GYHLDLLMVA VMLGVCSIMG LPWFVAATVL SITHVNSLKL ESECSAPGEQ
     PKFLGIREQR VTGLMIFILM GSSVFMTSIL KFIPMPVLYG VFLYMGASSL KGIQLFDRIK
     LFWMPAKHQP DFIYLRHVPL RKVHLFTVIQ MSCLGLLWII KVSRAAIVFP MMVLALVFVR
     KLMDFLFTKR ELSWLDDLMP ESKKKKLEDA EKEEEQSMLA MEDEGTVQLP LEGHYRDDPS
     VINISDEMSK TAMWGNLLVT ADNSKEKESR FPSKSSPS
//
ID   BRE1A_MOUSE             Reviewed;         973 AA.
AC   Q5DTM8; A2AIR3; Q3UT10; Q3V350; Q7TT11; Q8BKA8; Q8BKN8; Q8BUF7;
AC   Q8BVU4;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=E3 ubiquitin-protein ligase BRE1A;
DE            Short=BRE1-A;
DE            EC=6.3.2.-;
DE   AltName: Full=RING finger protein 20;
GN   Name=Rnf20; Synonyms=Bre1a, Kiaa4116;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-607 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-616 (ISOFORM 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Egg, Eye, Head, Kidney, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that mediates
CC       monoubiquitination of 'Lys-120' of histone H2B. H2B 'Lys-120'
CC       ubiquitination gives a specific tag for epigenetic transcriptional
CC       activation and is also prerequisite for histone H3 'Lys-4' and
CC       'Lys-79' methylation. Forms a ubiquitin ligase complex in
CC       cooperation with the E2 enzyme UBE2E1/UBCH6. It thereby plays a
CC       central role in histone code and gene regulation. Required for
CC       transcriptional activation of Hox genes. Recruited to the MDM2
CC       promoter, probably by being recruited by p53/TP53, and thereby
CC       acts as a transcriptional coactivator (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Homodimer. Component of the RNF20/40 complex at least
CC       composed of 2 copies of RNF20/BRE1A, 2 copies of RNF40/BRE1B and
CC       UBE2E1/UBCH6. Interacts with p53/TP53 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5DTM8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5DTM8-2; Sequence=VSP_016679;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the BRE1 family.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90290.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK220492; BAD90290.1; ALT_INIT; mRNA.
DR   EMBL; AL732521; CAM14732.1; -; Genomic_DNA.
DR   EMBL; BC052482; AAH52482.1; -; mRNA.
DR   EMBL; AK048862; BAE43337.1; -; mRNA.
DR   EMBL; AK051278; BAC34590.2; -; mRNA.
DR   EMBL; AK053783; BAC35521.1; -; mRNA.
DR   EMBL; AK076501; BAC36367.1; -; mRNA.
DR   EMBL; AK085436; BAC39446.1; -; mRNA.
DR   EMBL; AK139883; BAE24170.1; -; mRNA.
DR   IPI; IPI00380766; -.
DR   IPI; IPI00648519; -.
DR   RefSeq; NP_001156735.1; NM_001163263.1.
DR   RefSeq; NP_892044.1; NM_182999.2.
DR   UniGene; Mm.24765; -.
DR   ProteinModelPortal; Q5DTM8; -.
DR   SMR; Q5DTM8; 914-970.
DR   STRING; Q5DTM8; -.
DR   PhosphoSite; Q5DTM8; -.
DR   PRIDE; Q5DTM8; -.
DR   Ensembl; ENSMUST00000029989; ENSMUSP00000029989; ENSMUSG00000028309.
DR   Ensembl; ENSMUST00000098079; ENSMUSP00000095685; ENSMUSG00000028309.
DR   GeneID; 109331; -.
DR   KEGG; mmu:109331; -.
DR   UCSC; uc008swa.1; mouse.
DR   CTD; 109331; -.
DR   MGI; MGI:1925927; Rnf20.
DR   GeneTree; ENSGT00390000002866; -.
DR   HOVERGEN; HBG080312; -.
DR   InParanoid; Q5DTM8; -.
DR   OMA; KQDPEDL; -.
DR   OrthoDB; EOG49W2DV; -.
DR   PhylomeDB; Q5DTM8; -.
DR   NextBio; 361921; -.
DR   ArrayExpress; Q5DTM8; -.
DR   Bgee; Q5DTM8; -.
DR   CleanEx; MM_RNF20; -.
DR   Genevestigator; Q5DTM8; -.
DR   GermOnline; ENSMUSG00000028309; Mus musculus.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Chromatin regulator; Coiled coil;
KW   Ligase; Metal-binding; Nucleus; Phosphoprotein;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    973       E3 ubiquitin-protein ligase BRE1A.
FT                                /FTId=PRO_0000055837.
FT   ZN_FING     920    959       RING-type.
FT   COILED       43     90       Potential.
FT   COILED      168    378       Potential.
FT   COILED      429    896       Potential.
FT   MOD_RES     136    136       Phosphoserine (By similarity).
FT   MOD_RES     138    138       Phosphoserine.
FT   MOD_RES     314    314       Phosphotyrosine (By similarity).
FT   MOD_RES     348    348       N6-acetyllysine (By similarity).
FT   MOD_RES     540    540       Phosphoserine (By similarity).
FT   MOD_RES     553    553       Phosphoserine (By similarity).
FT   VAR_SEQ     100    249       Missing (in isoform 2).
FT                                /FTId=VSP_016679.
FT   CONFLICT    199    199       V -> L (in Ref. 4; BAC36367).
FT   CONFLICT    506    506       S -> F (in Ref. 4; BAC36367).
FT   CONFLICT    540    540       S -> F (in Ref. 4; BAC36367).
FT   CONFLICT    607    607       D -> G (in Ref. 4; BAE43337).
SQ   SEQUENCE   973 AA;  113520 MW;  6A89582C7ECD556C CRC64;
     MSGIGNKRAA GEPGTSMPPE KKTAVEDSGT TVETIKLGGV SSTEELDIRT LQSKNRKLAE
     MLDQRQAIED ELREHIEKLE RRQATDDASL LIVNRYWSQF DENIRIILKR YDLDQGLGDL
     LTERKALVVP EPEPDSDSNQ ERKDDRERGD GQEPAFSFLA TLASSSSEEM ESQLQERVES
     SRRAVSQIVT VYDKLQEKVD LLSRKLNSGD NLIVEEAVQE LNSFLAQENV RLQELTDLLQ
     EKHHTMSQEF CKLQGKVETA ESRVSVLESM IDDLQWDIDK IRKREQRLNR HLAEVLERVN
     SKGYKVYGAG SSLYGGTITI NARKFEEMNA ELEENKELAQ NRHCELEKLR QDFEEVTTQN
     EKLKVELRSA VEEVVKETPE YRCMQSQFSV LYNESLQLKA HLDEARTLLH GTRGTHQRQV
     ELIERDEVSL HKKLRTEVIQ LEDTLAQVRK EYEMLRIEFE QTLAANEQAG PINREMRHLI
     SSLQNHNHQL KGEVLRYKRK LREAQSDLNK TRLRSGSALL QSQSSTEDPK DEPTELKQDS
     EDLATHSSAL KASQEDEVKS KRDEEERERE RREKERERER EREKEKERER EKQKLKESEK
     ERDSVKDKEK GKHDDGRKKE AEIIKQLKIE LKKAQESQKE MKLLLDMYRS APKEQRDKVQ
     LMAAEKKSKA ELEDLRQRLK DLEDKEKKEN KKMADEDALR KIRAVEEQIE YLQKKLAMAK
     QEEEALLSEM DVTGQAFEDM QEQNIRLMQQ LREKDDANFK LMSERIKSNQ IHKLLKEEKE
     ELADQVLTLK TQVDAQLQVV RKLEEKEHLL QSNIGTGEKE LGLRTQALEM NKRKAMEAAQ
     LADDLKAQLE LAQKKLHDFQ DEIVENSVTK EKDLFNFKRA QEDISRLRRK LETTKKPDNV
     PKCDEILMEE IKDYKARLTC PCCNMRKKDA VLTKCFHVFC FECVKTRYDT RQRKCPKCNA
     AFGANDFHRI YIG
//
ID   JKIP3_MOUSE             Reviewed;         844 AA.
AC   Q5DTN8; Q0VDR4; Q0VDR5; Q9CU41;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   08-MAR-2011, entry version 40.
DE   RecName: Full=Janus kinase and microtubule-interacting protein 3;
DE   AltName: Full=Neuroendocrine long coiled-coil protein 2;
GN   Name=Jakmip3; Synonyms=Kiaa4091, Necc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-437 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17572408; DOI=10.1016/j.febslet.2007.06.002;
RA   Cruz-Garcia D., Vazquez-Martinez R., Peinado J.R., Anouar Y.,
RA   Tonon M.C., Vaudry H., Castano J.P., Malagon M.M.;
RT   "Identification and characterization of two novel (neuro)endocrine
RT   long coiled-coil proteins.";
RL   FEBS Lett. 581:3149-3156(2007).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5DTN8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5DTN8-2; Sequence=VSP_032000, VSP_032002, VSP_032003;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q5DTN8-3; Sequence=VSP_032001, VSP_032002, VSP_032003;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the JAKMIP family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90506.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK220482; BAD90506.1; ALT_INIT; mRNA.
DR   EMBL; BC119557; AAI19558.1; -; mRNA.
DR   EMBL; BC119558; AAI19559.1; -; mRNA.
DR   EMBL; AK018189; BAB31115.2; -; mRNA.
DR   IPI; IPI00406578; -.
DR   IPI; IPI00785376; -.
DR   IPI; IPI00889277; -.
DR   RefSeq; NP_082984.1; NM_028708.1.
DR   UniGene; Mm.334298; -.
DR   UniGene; Mm.389979; -.
DR   PRIDE; Q5DTN8; -.
DR   Ensembl; ENSMUST00000068273; ENSMUSP00000065675; ENSMUSG00000056856.
DR   Ensembl; ENSMUST00000106111; ENSMUSP00000101717; ENSMUSG00000056856.
DR   GeneID; 74004; -.
DR   KEGG; mmu:74004; -.
DR   CTD; 74004; -.
DR   MGI; MGI:1921254; Jakmip3.
DR   eggNOG; roNOG13474; -.
DR   GeneTree; ENSGT00390000002812; -.
DR   HOGENOM; HBG443926; -.
DR   HOVERGEN; HBG054249; -.
DR   InParanoid; Q5DTN8; -.
DR   OrthoDB; EOG4Z62N2; -.
DR   ArrayExpress; Q5DTN8; -.
DR   Bgee; Q5DTN8; -.
DR   Genevestigator; Q5DTN8; -.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Golgi apparatus.
FT   CHAIN         1    844       Janus kinase and microtubule-interacting
FT                                protein 3.
FT                                /FTId=PRO_0000323012.
FT   COILED        8    259       Potential.
FT   COILED      289    421       Potential.
FT   COILED      493    621       Potential.
FT   COILED      688    833       Potential.
FT   VAR_SEQ     212    285       Missing (in isoform 2).
FT                                /FTId=VSP_032000.
FT   VAR_SEQ     212    283       Missing (in isoform 3).
FT                                /FTId=VSP_032001.
FT   VAR_SEQ     535    535       T -> V (in isoform 2 and isoform 3).
FT                                /FTId=VSP_032002.
FT   VAR_SEQ     536    844       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_032003.
FT   CONFLICT    229    229       L -> F (in Ref. 3; BAB31115).
SQ   SEQUENCE   844 AA;  98715 MW;  39541A48498106C4 CRC64;
     MSKKGAGSRA KGDKAETLAA LQAANEELRA KLTDIQIELQ QEKSKVSKVE REKSQELKQV
     REHEQRKHAV LVTELKTKLH EEKMKELQAV REALLRQHEA ELLRVIKIKD NENQRLQALL
     NTLRDGAPDK VKTVLLCEAK EEAKKGFEVE KVKMQQEISE LKGAKKQVEE ALTMVIQADK
     IKAAEIRSVY HLHQEEITRI KKECEREIRR LMEEIRFKDR AVFVLERELG VQAGHAQRLQ
     LQKEALDEQL SQAKEAERHP GSPRRELPYA SGAGDASDHS GSPEQQLDEK DARRFQLKIA
     ELSAIIRKLE DRNALLSEER NELLKRLREA ESQYKPLLDK NKRLTRKNED LSHTLRRIES
     KLKFVTQENI EMRQRAGIIR RPSSLNDLDQ SQDEREIDFL KLQIVEQQNL IDELSKTLET
     AGYVKSVLER DKLLRYRKQR KKMAKLPKPV VVETFFGYDE EASLESDGSS ISYQTDRTDQ
     TPCTPEDDLE EGMAKEETEL RFRQLTMEYQ ALQRAYALLQ EQVGGTLDAE REVKTREQLQ
     AEIQRAQTRV EDLEKALAEQ GQDMKWIEEK QALYRRNQEL VEKIKQMETE EARLKHEVQD
     AKDQNELLEF RILELEERER KSPAINFHHT PFVDGKSPLQ VYCEAEGVTD ILVTELMKKL
     DILGDNANLT NEEQVVVIQA RTVLTLAEKW LQRIEETESA LQRKMVDLES EKELFSKQKG
     YLDEELDYRK QALDQAHKHI LELEAMLYDA LQQEAGAKVA ELLSEEEREK LKVAVEQWKR
     QVMSELRERD AQILRERMEL LQIAQQRIKE LEERIETQKR QIKELEEKFL FLFLFFSLAF
     ILWS
//
ID   Q5DTP4_MOUSE            Unreviewed;       615 AA.
AC   Q5DTP4;
DT   29-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   29-MAR-2005, sequence version 1.
DT   08-MAR-2011, entry version 30.
DE   SubName: Full=MKIAA4082 protein;
DE   Flags: Fragment;
GN   Name=Dennd4a; Synonyms=AI115600, mKIAA4082;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the Coding Sequences of Mouse Homologues of KIAA Gene.
RT   The Complete Nucleotide Sequences of Mouse KIAA-homologous cDNAs
RT   Identified by Screening of Terminal sequences of cDNA Clones Randomly
RT   Sampled from Size-Fractionated Libraries..";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
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DR   EMBL; AK220476; BAD90501.1; -; mRNA.
DR   IPI; IPI00554827; -.
DR   UniGene; Mm.222473; -.
DR   PRIDE; Q5DTP4; -.
DR   Ensembl; ENSMUST00000089035; ENSMUSP00000086435; ENSMUSG00000035492.
DR   MGI; MGI:2142979; Dennd4a.
DR   eggNOG; maNOG09206; -.
DR   GeneTree; ENSGT00550000074509; -.
DR   OrthoDB; EOG4M65GS; -.
DR   ArrayExpress; Q5DTP4; -.
DR   Bgee; Q5DTP4; -.
DR   Genevestigator; Q5DTP4; -.
DR   InterPro; IPR002885; Pentatricopeptide_repeat.
DR   TIGRFAMs; TIGR00756; PPR; 1.
PE   1: Evidence at protein level;
FT   NON_TER       1      1
SQ   SEQUENCE   615 AA;  68547 MW;  4094BDB12FFEEDC8 CRC64;
     GNSVIPRVSI IRDARAEERL CLFTSQLVLQ VCYRILMQLC GQYDQPVLAV RVLFEMQKAG
     IDPNAITYGY YNKAVLESTW PSRSRSGYFL WTKVRNVVLG VAQFKRALKK HPHLPQTALS
     GGRSDLGYNS LSKDNVRREG PSTEDIQGEK EKRGSDSSSL SENESTKGSA ECLPTLSYQR
     ASTIVRLNGA HNDSAGKTSG ECEESTPELL LMPSLEDTNE AQTTPSRCFR KRHKSDDGSH
     LQQQMPWGSR NRNLSGGVLM GFMLNRTNQE TSPGEMVEKL GADAKILSNV ISKSTRPNSL
     DIGKPPARSK RDSLEKESSD DDTPFHGSNC LDKVESPVIF DLEDLDTETD GSKVGGVAAQ
     NPKRLQRRNS SFSVKPSEKT DVVTGFDPLS LLVAETEQQQ KVEEEEDEDD NKSVSTPSAR
     RNLAEEIEMY MNNMSSPLTS RTPSIDLQRA CDDKLTNKKS PTLVKACRRS SLPPNSPRPV
     RLTKSKSYTK SEERPRDRLW SSPAFSPTCP FREGSQETLA HSSPSFNLDT LLVPKLDVLR
     HSVFTAGKGV AEKASKWYSR FTMYTTSSKV GLWAFAASVS RLHHSHLQLS YEHICLNHSP
     YIQLIQDNEG FLKIF
//
ID   PSD1_MOUSE              Reviewed;        1024 AA.
AC   Q5DTT2; B2RS07; Q3TY69;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   08-MAR-2011, entry version 41.
DE   RecName: Full=PH and SEC7 domain-containing protein 1;
DE   AltName: Full=Pleckstrin homology and SEC7 domain-containing protein 1;
GN   Name=Psd; Synonyms=Kiaa2011, Psd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 254-1024 (ISOFORM 1).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-720, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Guanine nucleotide exchange factor for ARF6 (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5DTT2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5DTT2-2; Sequence=VSP_033637, VSP_033638;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the PSD family.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 SEC7 domain.
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DR   EMBL; AC114539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK158851; BAE34694.1; -; mRNA.
DR   EMBL; BC138652; AAI38653.1; -; mRNA.
DR   EMBL; AK220438; BAD90268.1; -; Transcribed_RNA.
DR   IPI; IPI00464335; -.
DR   IPI; IPI00762615; -.
DR   RefSeq; NP_082903.2; NM_028627.2.
DR   UniGene; Mm.268532; -.
DR   HSSP; Q15438; 1BC9.
DR   ProteinModelPortal; Q5DTT2; -.
DR   SMR; Q5DTT2; 558-976.
DR   STRING; Q5DTT2; -.
DR   PhosphoSite; Q5DTT2; -.
DR   PRIDE; Q5DTT2; -.
DR   Ensembl; ENSMUST00000041391; ENSMUSP00000039728; ENSMUSG00000037126.
DR   Ensembl; ENSMUST00000096029; ENSMUSP00000093729; ENSMUSG00000037126.
DR   GeneID; 73728; -.
DR   KEGG; mmu:73728; -.
DR   UCSC; uc008htc.1; mouse.
DR   CTD; 73728; -.
DR   MGI; MGI:1920978; Psd.
DR   HOVERGEN; HBG106661; -.
DR   InParanoid; Q5DTT2; -.
DR   OMA; PPQVGAD; -.
DR   OrthoDB; EOG4CNQQM; -.
DR   PhylomeDB; Q5DTT2; -.
DR   NextBio; 338913; -.
DR   ArrayExpress; Q5DTT2; -.
DR   Bgee; Q5DTT2; -.
DR   Genevestigator; Q5DTT2; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000904; Sec7.
DR   InterPro; IPR023394; SEC7_alpha_orthog.
DR   InterPro; IPR001605; Spectrin_PH.
DR   Gene3D; G3DSA:1.10.1000.11; G3DSA:1.10.1000.11; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF01369; Sec7; 1.
DR   PRINTS; PR00683; SPECTRINPH.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00222; Sec7; 1.
DR   SUPFAM; SSF48425; Sec7; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50190; SEC7; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil;
KW   Guanine-nucleotide releasing factor; Phosphoprotein.
FT   CHAIN         1   1024       PH and SEC7 domain-containing protein 1.
FT                                /FTId=PRO_0000334161.
FT   DOMAIN      512    706       SEC7.
FT   DOMAIN      756    869       PH.
FT   COILED      898    924       Potential.
FT   COILED      956    983       Potential.
FT   COMPBIAS     18     94       Pro-rich.
FT   COMPBIAS    432    466       Pro-rich.
FT   COMPBIAS    739    744       Poly-Ser.
FT   MOD_RES     720    720       Phosphoserine.
FT   VAR_SEQ       1    631       Missing (in isoform 2).
FT                                /FTId=VSP_033637.
FT   VAR_SEQ     632    697       FSQRYFQCNPEALSSEDGAHTLTCALMLLNTDLHGHNIGKR
FT                                MTCGDFIGNLEGLNDGGDFPRELLK -> MIGVNSIHSSAG
FT                                RLRSRSLCSVRYGRTHRGAETLCYGWPQRSRSLKPVLYTDL
FT                                VVSRLQSRKKKKA (in isoform 2).
FT                                /FTId=VSP_033638.
SQ   SEQUENCE   1024 AA;  109687 MW;  207A889E6D16CC99 CRC64;
     MAQGAMRFCS EGDCAISPPR CPRRWLPEGP VPQSPPASMY GSTGSLIRRV VGPGPRGRDL
     GRVTAPCTPL RAPPSPHIAP SPWGPSSPTG QPPPGAQSSV VIFRFVEKAS VRPLNGLPAS
     GGLSRSWDLG GISAPRPTPA LGPGCNRKLR LEASTSDPLP AGGGSVLPGS RDPSRGPLVP
     PQIGADGLYS SLPNGLGGTP EHLAMHFRGP ADTGFLNQGD TWSSPREVSS HAQRIARAKW
     EFFYGSLDAP SSGAKPPEQV LPSRGVGSKQ GSGVAVGRAA KYSETDLDKV PLRCYRETDI
     DEVLAEREEA DSAIESQPSS EGPHGTAQPP ASRPSPCPGP SSSLGSGNED DEAGGEEDVD
     DEVFEASEGA RPGDHMPHSG LLKSPVPFLL GTSPSADGPD SFSCVFEAIL ESHRAKGTSY
     SSLASLEALA SPGPTQSPFF TFEMPPQPPA PRPDPPAPAP LAPLEPDSGT SSAADGPWTQ
     RREVEESDAG ATLAPRKELP SPSHSEDSFG LGAAPLGSEP PLSQLVSDSD SELDSTERLA
     LGSTDTLSNG QKADLEAAQR LAKRLYRLDG FRKADVARHL GKNNDFSKLV AGEYLKFFVF
     TGMTLDQALR VFLKELALMG ETQERERVLA HFSQRYFQCN PEALSSEDGA HTLTCALMLL
     NTDLHGHNIG KRMTCGDFIG NLEGLNDGGD FPRELLKALY SSIKNEKLQW AIDEEELRRS
     LSELADPNPK VIKRVSGGSG SSSSPFLDLT PEPGAAVYKH GALVRKVHAD PDCRKTPRGK
     RGWKSFHGIL KGMILYLQKE EYQPGKALSE AELKNAISIH HALATRASDY SKRPHVFYLR
     TADWRVFLFQ APSLEQMQSW ITRINVVAAM FSAPPFPAAV SSQKKFSRPL LPSAATRLSQ
     EEQVRTHEAK LKAMASELRE HRAAHLGKKA RGKEADEQRQ KEAYLEFEKS RYGTYAALLR
     VKMKAASEEL DTIEAALAQA GSTEDGCPPP HSSPSLRPKP TSQPRAQRPG SETRAGAGST
     RPKP
//
ID   AF1L2_MOUSE             Reviewed;         825 AA.
AC   Q5DTU0; Q8BID1; Q8K2G0;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   08-FEB-2011, entry version 59.
DE   RecName: Full=Actin filament-associated protein 1-like 2;
DE            Short=AFAP1-like protein 2;
GN   Name=Afap1l2; Synonyms=Kiaa1914;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-56 AND TYR-413, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-345, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May play a role in a signaling cascade by enhancing the
CC       kinase activity of SRC. Contributes to SRC-regulated transcription
CC       activation (By similarity).
CC   -!- SUBUNIT: Interacts with SRC. Interacts with LCK when tyrosine
CC       phosphorylated (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5DTU0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5DTU0-2; Sequence=VSP_014257;
CC   -!- PTM: Tyrosine phosphorylated (by SRC) (By similarity).
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH31515.1; Type=Erroneous initiation;
CC       Sequence=BAC39879.1; Type=Frameshift; Positions=701;
CC       Sequence=BAD90264.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK087449; BAC39879.1; ALT_FRAME; mRNA.
DR   EMBL; AK220430; BAD90264.1; ALT_INIT; mRNA.
DR   EMBL; BC031515; AAH31515.1; ALT_INIT; mRNA.
DR   IPI; IPI00169899; -.
DR   IPI; IPI00608072; -.
DR   RefSeq; NP_001171267.1; NM_001177796.1.
DR   RefSeq; NP_001171268.1; NM_001177797.1.
DR   RefSeq; NP_666214.1; NM_146102.2.
DR   UniGene; Mm.226284; -.
DR   ProteinModelPortal; Q5DTU0; -.
DR   SMR; Q5DTU0; 178-272, 354-443.
DR   PhosphoSite; Q5DTU0; -.
DR   PRIDE; Q5DTU0; -.
DR   Ensembl; ENSMUST00000111584; ENSMUSP00000107210; ENSMUSG00000025083.
DR   Ensembl; ENSMUST00000118800; ENSMUSP00000113745; ENSMUSG00000025083.
DR   GeneID; 226250; -.
DR   KEGG; mmu:226250; -.
DR   UCSC; uc008hzm.1; mouse.
DR   UCSC; uc008hzn.1; mouse.
DR   CTD; 226250; -.
DR   MGI; MGI:2147658; Afap1l2.
DR   eggNOG; roNOG04870; -.
DR   GeneTree; ENSGT00390000003998; -.
DR   HOVERGEN; HBG106875; -.
DR   OMA; APYQWPS; -.
DR   NextBio; 378068; -.
DR   ArrayExpress; Q5DTU0; -.
DR   Bgee; Q5DTU0; -.
DR   CleanEx; MM_AFAP1L2; -.
DR   Genevestigator; Q5DTU0; -.
DR   GermOnline; ENSMUSG00000025083; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Pfam; PF00169; PH; 2.
DR   SMART; SM00233; PH; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Phosphoprotein; Repeat.
FT   CHAIN         1    825       Actin filament-associated protein 1-like
FT                                2.
FT                                /FTId=PRO_0000050806.
FT   DOMAIN      175    271       PH 1.
FT   DOMAIN      353    447       PH 2.
FT   COILED      657    754       Potential.
FT   MOD_RES      56     56       Phosphotyrosine.
FT   MOD_RES     345    345       Phosphothreonine.
FT   MOD_RES     383    383       Phosphotyrosine (By similarity).
FT   MOD_RES     413    413       Phosphotyrosine.
FT   MOD_RES     673    673       Phosphotyrosine (By similarity).
FT   MOD_RES     674    674       Phosphothreonine (By similarity).
FT   VAR_SEQ       1      6       MERYKA -> MERYKAQGCCCLVVQRRILQVSAS (in
FT                                isoform 2).
FT                                /FTId=VSP_014257.
FT   CONFLICT    124    124       Y -> N (in Ref. 1; BAC39879).
SQ   SEQUENCE   825 AA;  92175 MW;  E0D929590FED4764 CRC64;
     MERYKALEQL LTELDDFLKV LDQENLSSAA VLKKSGLSEL LRLYTKSSSS DEEYIYMNKV
     SVNGEQNSAS PDKVPEEQGP LTNGEPSQHS SAPQKSLPDL PPPKMIPERK QPTVPKIESP
     EGYYEEAEPF DRSINEDGEA VSSSYESYDE DENSKGKAAP YQWPSPEASI ELMRDARICA
     FLWRKKWLGQ WAKQLCVIRD TRLLCYKSSK DHSPQLDVNL RGSSVVHKEK QVRKKGHKLK
     ITPMNADVIV LGLQSKDQAE QWLRVIQEVS GLPSEGASEG NQYTPDAQRL NCQKPDIAEK
     YLSAAEYGIT INGHPEIPET KDVKKKCSAG LKLSNLMNLG RKKSTSLEPP ERSLETSSYL
     NVLVNSQWKS RWCFVRDSHL HFYQDRNRSK VAQQPLSLVG CDVLPDPSPD HLYSFRILHN
     GEELAKLEAK SSEEMGHWLG LLLSESGSKT DPEELTYDYV DAERVSCIVS AAKTSLLLMQ
     RKFSEPNTYI DGLPSRDCQD DLYDDVEVSE LIAVVEPAEE AAPAVDANSG SEPDRVYLDL
     TPVKSFLHSS SEAQAQASLP AVPHQDDVAE TLTVDPKPGT TPEEPHTESP GDPEVQQRQP
     EVQESSEPIE PTPRITMVKL QAEQQRISFP ANCPDTMASA PIAASPPVKE KLRVTSAEIK
     LGKNRTEAEV KRYTEEKERL ERSKEEIRGH LAQLRREKRE LKETLLRCTD KGVLAKLEQT
     LKKIDEECRM EESRRVDLEL SIMEVKDNLK KAEAGPVTLG TTVDTTHLDN MSPRPQPKAA
     TPNPPPDSTP VNSASVLKNR PLSVMVTGKG TVLQKAKEWE KKGAS
//
ID   K1462_MOUSE             Reviewed;        1320 AA.
AC   Q5DTX6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   08-MAR-2011, entry version 40.
DE   RecName: Full=Uncharacterized protein KIAA1462;
GN   Name=Kiaa1462; Synonyms=Gm328;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 563-1320.
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1223; SER-1245 AND
RP   SER-1248, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
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DR   EMBL; AC147227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK220394; BAD90447.1; -; mRNA.
DR   IPI; IPI00129924; -.
DR   RefSeq; NP_001075432.1; NM_001081963.1.
DR   UniGene; Mm.33179; -.
DR   PhosphoSite; Q5DTX6; -.
DR   PRIDE; Q5DTX6; -.
DR   Ensembl; ENSMUST00000037029; ENSMUSP00000038613; ENSMUSG00000033960.
DR   GeneID; 240185; -.
DR   KEGG; mmu:240185; -.
DR   NMPDR; fig|10090.3.peg.3541; -.
DR   MGI; MGI:2685174; 9430020K01Rik.
DR   eggNOG; roNOG07956; -.
DR   GeneTree; ENSGT00390000015348; -.
DR   HOGENOM; HBG282634; -.
DR   HOVERGEN; HBG095900; -.
DR   InParanoid; Q5DTX6; -.
DR   OMA; QEKLASP; -.
DR   OrthoDB; EOG43JC3V; -.
DR   NextBio; 384497; -.
DR   ArrayExpress; Q5DTX6; -.
DR   Bgee; Q5DTX6; -.
DR   CleanEx; MM_9430020K01RIK; -.
DR   Genevestigator; Q5DTX6; -.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1   1320       Uncharacterized protein KIAA1462.
FT                                /FTId=PRO_0000314186.
FT   COMPBIAS    254    416       Pro-rich.
FT   COMPBIAS    838    841       Poly-Glu.
FT   MOD_RES     499    499       Phosphoserine (By similarity).
FT   MOD_RES     756    756       Phosphoserine (By similarity).
FT   MOD_RES    1223   1223       Phosphoserine.
FT   MOD_RES    1245   1245       Phosphoserine.
FT   MOD_RES    1248   1248       Phosphoserine.
FT   MOD_RES    1270   1270       Phosphoserine (By similarity).
SQ   SEQUENCE   1320 AA;  144798 MW;  2317F13096AFE1E7 CRC64;
     MYSVEDLLIS HGYKPARDAA APCEDKSERC RSTRTGPRAG QGLLNGYKDG ATAHTHSRTS
     LGTGHVSNSE NRISRPRGHR EHQSTSRTPE ARFLNQPSLA WSSQPQSGRD DIYWSRGRQE
     GSGSLCPRDW KELESRGMAQ AYSLPVHVRE NLWEVAGRTE HVMKNAIWEE ELRMQDMSLE
     SWKKPRELGR QASDGDGRKR PQEKFEGLYP FVHGEHTSQN RKKSQSLPRA LSPKSLNFTE
     IPVPLHDGHI TGVPKVPPYP PSFPSPSEPM RNLEKASSSG PFPRPKFGKP LKTPCYSSHS
     QPRGEGGFQD HQHRDPRGSY PTRSKDPSHE LGMLDPGLEP PVYVPPPSYR SPPQHIPNPY
     LEDPVPRHVS SNQSQQQVPE KPETSCPLPS GSLAARDLYD AMPGSPPQGL PPQPYPIATH
     GGSIQYIPFD DPRIRHIKLA QPPEFYEEAK LDDTSYNPGL LTTQEPAIGK RQYDDAPSVP
     RGPTPSPVNE QSSAFVHSSP RWLQGQLPLG IGPGGFHGQT EHHVMGGLTT NVTDIKAEGH
     ASSPQPQSEG TCKTYTKLRK FETGVQSKKS SKKKSNATIF CLVSIPVKSE SLVLATDTNN
     NDFKLVADKT RGLCQGSALQ EQSLLSMSST DLELQALMGS MAWRRTSPRQ GLRESEDGQI
     DDPRILHLIK PKELQASSPW PGHQYRDQQT QTSFHEDSKS SQLLPATKPG EASNVAPTPT
     CPDTTASEVC LHTALAFSDQ NQKPSVPHLQ GQTSLSPSRN SAFSRTSSAI NQASMSKGTS
     DQLPGANPVP KPEVVKGEST TGQCNSTQLF GQFLLKPVSR RPWDLISQLE SFNKELQEEE
     ESHGGSGSED SEAEQPEDCA DSRTKSWALQ GTRTAQQPAG LALENVASPD RRLNDSQSWN
     EEPKPGHSSV HPQSLGPSQE EGSRGVPVQW ADGSLTAEQK SQEDLNGMCE RDFSPRPVSR
     IAPIDTKAAP LYCLSEPRGS QELTKFGDAV GSVQLGRETP TQVGNGGDTE VLPCVLLPLA
     DKYRGHSTPD FRSLELTLGQ EQNAYKLECL DLENTVEVLP SESLQERAER ILGIEVAVES
     LLPSARRTEQ SQLPEPDASA CNPSSSREDS SHSLALPVGP KVATDAFYGR RKCGWTESPL
     FVGERAPQAS ICSDVDGFPT SQATSPEPGK KDEEAKAPFK STLFHFMEKS TNVVGPEKRL
     RNPSKVVENL QEKLVSPPKK ADSVHLIRMR EVNSLSQMRC LSSKSADSVE EPDPLKVIKS
     SAWLSEGLTS LGGKDEAWQA GHLPSVSQNE NGHPEVPRDK MSDQDLWCAD SYDPSRVERV
//
ID   Q5DTX9_MOUSE            Unreviewed;       411 AA.
AC   Q5DTX9;
DT   29-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   29-MAR-2005, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   SubName: Full=MKIAA1435 protein;
DE   Flags: Fragment;
GN   Name=Wdfy1; Synonyms=mKIAA1435;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the Coding Sequences of Mouse Homologues of KIAA Gene.
RT   The Complete Nucleotide Sequences of Mouse KIAA-homologous cDNAs
RT   Identified by Screening of Terminal sequences of cDNA Clones Randomly
RT   Sampled from Size-Fractionated Libraries..";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK220391; BAD90445.1; -; mRNA.
DR   IPI; IPI00754723; -.
DR   RefSeq; NP_001104749.1; NM_001111279.1.
DR   UniGene; Mm.293273; -.
DR   ProteinModelPortal; Q5DTX9; -.
DR   Ensembl; ENSMUST00000113512; ENSMUSP00000109140; ENSMUSG00000073643.
DR   Ensembl; ENSMUST00000113513; ENSMUSP00000109141; ENSMUSG00000073643.
DR   Ensembl; ENSMUST00000113514; ENSMUSP00000109142; ENSMUSG00000073643.
DR   Ensembl; ENSMUST00000113515; ENSMUSP00000109143; ENSMUSG00000073643.
DR   GeneID; 69368; -.
DR   KEGG; mmu:69368; -.
DR   UCSC; uc007bqu.1; mouse.
DR   CTD; 69368; -.
DR   MGI; MGI:1916618; Wdfy1.
DR   eggNOG; roNOG12101; -.
DR   HOGENOM; HBG380283; -.
DR   HOVERGEN; HBG054128; -.
DR   InParanoid; Q5DTX9; -.
DR   OrthoDB; EOG41ZF9T; -.
DR   NextBio; 329250; -.
DR   ArrayExpress; Q5DTX9; -.
DR   Bgee; Q5DTX9; -.
DR   Genevestigator; Q5DTX9; -.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 3.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF00400; WD40; 5.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 3.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Repeat; WD repeat; Zinc.
FT   NON_TER       1      1
SQ   SEQUENCE   411 AA;  46348 MW;  07D0F9AC64CD1C65 CRC64;
     NMAAEIHSRP QSSRPVLLSK IEGHQDAVTA ALLIPKEDGV ITASEDRTIR VWLKRDSGQY
     WPSIYHTMAS PCSAMAYHHD SRRIFVGQDN GAVMEFHVSE DFNKMNFIKT YPAHQNRVSA
     IIFSLSAEWV ISTGHDKCVS WMCTRSGNML GRHFFSSWAS CLQYDLDTQH AFVGDYSGQI
     TLLKLEQNTC SVITTLKGHE GSIACLWWDP IQRLLFSGAS DNSVIMWDIG GRKGRTLLLQ
     GHHDRVQSLC YLQLTRQLVS CSADGGIAVW NMDVSREEAP QWLESDSCQK CEQPFFWNIK
     QMWDTKTLGL RQHHCRKCGQ AVCGKCSSKR SSYPVMGFEF QVRVCDSCYD SIKDEDRTSL
     ATFHEGKHNI SHMSMDIARG LMVTCGTDRV VKIWDMTPVV GCSLATGFSP H
//
ID   KCD16_MOUSE             Reviewed;         427 AA.
AC   Q5DTY9; Q78Y50;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=BTB/POZ domain-containing protein KCTD16;
GN   Name=Kctd16; Synonyms=Gm1267, Kiaa1317;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-427.
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 317-427.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 AND SER-389, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-112, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [6]
RP   FUNCTION, INTERACTION WITH GABRB1 AND GABRB2, TETRAMERIZATION,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=20400944; DOI=10.1038/nature08964;
RA   Schwenk J., Metz M., Zolles G., Turecek R., Fritzius T., Bildl W.,
RA   Tarusawa E., Kulik A., Unger A., Ivankova K., Seddik R., Tiao J.Y.,
RA   Rajalu M., Trojanova J., Rohde V., Gassmann M., Schulte U., Fakler B.,
RA   Bettler B.;
RT   "Native GABA(B) receptors are heteromultimers with a family of
RT   auxiliary subunits.";
RL   Nature 465:231-235(2010).
CC   -!- FUNCTION: Auxiliary subunit of GABA-B receptors that determine the
CC       pharmacology and kinetics of the receptor response. Increases
CC       agonist potency and markedly alter the G-protein signaling of the
CC       receptors by accelerating onset and promoting desensitization.
CC   -!- SUBUNIT: Interacts as a tetramer with GABRB1 and GABRB2.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, presynaptic cell
CC       membrane. Cell junction, synapse, postsynaptic cell membrane.
CC       Note=Colocalizes with GABRB1.
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, mainly in the
CC       hippocampus.
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
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DR   EMBL; AC098707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC127249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK220381; BAD90438.1; -; mRNA.
DR   EMBL; AK005863; BAB24283.1; -; mRNA.
DR   IPI; IPI00675985; -.
DR   RefSeq; NP_080411.1; NM_026135.1.
DR   UniGene; Mm.441493; -.
DR   UniGene; Mm.76366; -.
DR   HSSP; Q63881; 1NN7.
DR   ProteinModelPortal; Q5DTY9; -.
DR   SMR; Q5DTY9; 19-128.
DR   PhosphoSite; Q5DTY9; -.
DR   PRIDE; Q5DTY9; -.
DR   Ensembl; ENSMUST00000091927; ENSMUSP00000089547; ENSMUSG00000051401.
DR   GeneID; 383348; -.
DR   KEGG; mmu:383348; -.
DR   UCSC; uc008ete.1; mouse.
DR   CTD; 383348; -.
DR   MGI; MGI:1914659; Kctd16.
DR   eggNOG; roNOG10578; -.
DR   GeneTree; ENSGT00600000084079; -.
DR   HOGENOM; HBG445337; -.
DR   HOVERGEN; HBG052218; -.
DR   InParanoid; Q5DTY9; -.
DR   OMA; TLVSIPH; -.
DR   OrthoDB; EOG4MKNGT; -.
DR   NextBio; 403829; -.
DR   ArrayExpress; Q5DTY9; -.
DR   Bgee; Q5DTY9; -.
DR   Genevestigator; Q5DTY9; -.
DR   GermOnline; ENSMUSG00000051401; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   PROSITE; PS50097; BTB; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Synapse.
FT   CHAIN         1    427       BTB/POZ domain-containing protein KCTD16.
FT                                /FTId=PRO_0000248594.
FT   DOMAIN       25     98       BTB.
FT   MOD_RES     112    112       Phosphotyrosine.
FT   MOD_RES     130    130       Phosphoserine.
FT   MOD_RES     389    389       Phosphoserine.
FT   CONFLICT    317    317       Q -> E (in Ref. 3; BAB24283).
SQ   SEQUENCE   427 AA;  48972 MW;  C19AFA955BD30585 CRC64;
     MALSGNCSRY YPRDQGAAVP NSFPEVIELN VGGQVYFTRH STLISIPHSL LWKMFSPKRD
     TANDLAKDSK GRFFIDRDGF LFRYILDYLR DRQVVLPDHF PERGRLKREA EYFQLPDLVK
     LLAPEDVKQS PDEFCHSDFE DASQGSDTRI CPPSSLLPHD RKWGFITVGY RGSCTLGREG
     QADAKFRRVP RILVCGRISL AKEVFGETLN ESRDPDRAPE RYTSRFYLKF KHLERAFDML
     SECGFHMVAC NSSVTASFVN QYTEDKIWSS YTEYVFYREP SRWSSSHCDC CCKNGKGDKG
     ESGTSCNDLS TSSCDSQSEA SSPQETVICG PVTRQSNIQT LDRPIKKGPV QLIQQSEMRR
     KSDLLRTLTS GSRESNISSK KKAAKEKLSI EEELEKCIQD FLKIKIPDRF PERKHPWQSE
     LLRKYHL
//
ID   Q5DU06_MOUSE            Unreviewed;       753 AA.
AC   Q5DU06;
DT   29-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   29-MAR-2005, sequence version 1.
DT   08-FEB-2011, entry version 37.
DE   SubName: Full=MKIAA1030 protein;
DE   Flags: Fragment;
GN   Name=Igsf9b; Synonyms=Gm508, mKIAA1030;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the Coding Sequences of Mouse Homologues of KIAA Gene.
RT   The Complete Nucleotide Sequences of Mouse KIAA-homologous cDNAs
RT   Identified by Screening of Terminal sequences of cDNA Clones Randomly
RT   Sampled from Size-Fractionated Libraries..";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
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DR   EMBL; AK220364; BAD90425.1; -; mRNA.
DR   IPI; IPI00463186; -.
DR   UniGene; Mm.335029; -.
DR   ProteinModelPortal; Q5DU06; -.
DR   PhosphoSite; Q5DU06; -.
DR   Ensembl; ENSMUST00000037531; ENSMUSP00000036353; ENSMUSG00000034275.
DR   Ensembl; ENSMUST00000133213; ENSMUSP00000117017; ENSMUSG00000034275.
DR   UCSC; uc009oqm.1; mouse.
DR   MGI; MGI:2685354; Igsf9b.
DR   eggNOG; roNOG06014; -.
DR   GeneTree; ENSGT00530000063887; -.
DR   HOGENOM; HBG506099; -.
DR   HOVERGEN; HBG088669; -.
DR   InParanoid; Q5DU06; -.
DR   Bgee; Q5DU06; -.
DR   Genevestigator; Q5DU06; -.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF00041; fn3; 1.
DR   SMART; SM00060; FN3; 1.
DR   SUPFAM; SSF49265; FN_III-like; 1.
DR   PROSITE; PS50853; FN3; 1.
PE   1: Evidence at protein level;
FT   NON_TER       1      1
SQ   SEQUENCE   753 AA;  81377 MW;  6B1F58CC25087001 CRC64;
     TAYQFSVLAQ NRLGTSAFSE VVTVNTLAFP VTTPEPLVLV TPPRCLTANR TQQGVLLSWL
     PPANHSFPID RYIMEFRVGE RWEMLDDAIP GTDGDFFAKD LSQDTWYEFR VLAVMQDLIS
     EPSNIAGVSS TDIFPQPDLT DDGLARPVLA GIVATICFLA AAILFSTLAA CFVNKQRKRK
     LKRKKDPPLS ITHCRKSLES PLSSGKVSPE SIRTLRAPSE SSDDQGQPAA KRMLSPTREK
     ELSLYKKTKR AISSRKYSVA KAEAEAEATT PIELISRGPD GRFVMGPSEM EPSVKGRRIE
     GFPFAEETDM YPEFRQSDEE NEDPLVPTSV AALKPQLTPM SSSQDSYLPP PAYSPRFQPR
     GLEGPSGLGG RLQATGQARP PAPRPFQHGQ YYGYLSSSSP GEVEPPPFYM PEVGSPLSSV
     MSSPPLHTEG PFGHPTIPEE NGENASNSTL PLTQTPTGGR SPEPWGRPEF PFGGLETPAM
     MFPHQLHPCD VAESLQPKAC LPRGLPPAPL QVPAAYPGML SLEAPKGWVG KSPGRGPIPA
     PPATKWQERP MQPLVSQGQL RHTSQGMGIP VLPYPEPAEP GGHGGPSTFG LDTRWYEPQP
     RPRPSPRQAR RAEPSLHQVV LQPSRLSPLT QSPLSSRTGS PELAARARPR PGLLQQAEMS
     EITLQPPAAV SFSRKSTPSS TGSPSQSSRS GSPSYRPTMG FTTLATGYPS PPPGPAPPAP
     GDTLDVFGQT PSPRRMGEEP LRPEPPTTLP TSG
//
ID   IQEC2_MOUSE             Reviewed;        1478 AA.
AC   Q5DU25;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=IQ motif and SEC7 domain-containing protein 2;
GN   Name=Iqsec2; Synonyms=Kiaa0522;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 833-1478.
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; TYR-89; TYR-611;
RP   TYR-923 AND TYR-1119, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383 AND SER-402, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- SIMILARITY: Belongs to the BRAG family.
CC   -!- SIMILARITY: Contains 1 IQ domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 SEC7 domain.
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DR   EMBL; AC083816; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK220345; BAD90410.1; -; mRNA.
DR   IPI; IPI00758248; -.
DR   RefSeq; NP_001108136.1; NM_001114664.1.
DR   UniGene; Mm.33027; -.
DR   ProteinModelPortal; Q5DU25; -.
DR   SMR; Q5DU25; 739-1075.
DR   STRING; Q5DU25; -.
DR   PhosphoSite; Q5DU25; -.
DR   PRIDE; Q5DU25; -.
DR   Ensembl; ENSMUST00000080074; ENSMUSP00000078978; ENSMUSG00000041115.
DR   GeneID; 245666; -.
DR   KEGG; mmu:245666; -.
DR   UCSC; uc009upy.1; mouse.
DR   CTD; 245666; -.
DR   MGI; MGI:3528396; Iqsec2.
DR   eggNOG; roNOG05999; -.
DR   GeneTree; ENSGT00590000083058; -.
DR   HOVERGEN; HBG056324; -.
DR   ArrayExpress; Q5DU25; -.
DR   Bgee; Q5DU25; -.
DR   CleanEx; MM_IQSEC2; -.
DR   Genevestigator; Q5DU25; -.
DR   GermOnline; ENSMUSG00000041115; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000904; Sec7.
DR   InterPro; IPR023394; SEC7_alpha_orthog.
DR   Gene3D; G3DSA:1.10.1000.11; G3DSA:1.10.1000.11; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF01369; Sec7; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00222; Sec7; 1.
DR   SUPFAM; SSF48425; Sec7; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
DR   PROSITE; PS50190; SEC7; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Phosphoprotein.
FT   CHAIN         1   1478       IQ motif and SEC7 domain-containing
FT                                protein 2.
FT                                /FTId=PRO_0000245609.
FT   DOMAIN      337    366       IQ.
FT   DOMAIN      736    929       SEC7.
FT   DOMAIN      941   1075       PH.
FT   COILED       23     74       Potential.
FT   COMPBIAS    299    302       Poly-Glu.
FT   COMPBIAS    513    656       Pro-rich.
FT   COMPBIAS   1164   1471       Pro-rich.
FT   COMPBIAS   1229   1241       His-rich.
FT   MOD_RES      82     82       Phosphoserine.
FT   MOD_RES      89     89       Phosphotyrosine.
FT   MOD_RES     383    383       Phosphoserine.
FT   MOD_RES     402    402       Phosphoserine.
FT   MOD_RES     611    611       Phosphotyrosine.
FT   MOD_RES     923    923       Phosphotyrosine.
FT   MOD_RES    1119   1119       Phosphotyrosine.
FT   CONFLICT    833    833       H -> L (in Ref. 2; BAD90410).
FT   CONFLICT   1110   1110       M -> L (in Ref. 2; BAD90410).
FT   CONFLICT   1279   1279       S -> P (in Ref. 2; BAD90410).
SQ   SEQUENCE   1478 AA;  161851 MW;  058A91952F9F7E04 CRC64;
     MEAGSGPPGG PGSESPNRAV EYLLELNNII ESQQQLLETQ RRRIEELEGQ LDQLTQENRD
     LREESQLHRG ELHRDPLGAR DSPGRESQYQ NLRETQFHHR ELRESQFHQA SRDVGYPNRD
     GAYQNREAIY RDKEREASYQ LQDTTGYTAR ERDVAQCHLH HENPALGRER GGREAGPAHP
     GREKEAGYSA AVGVGQRPPR ERGQLSRGAS RSSSPGAGGG HSTSTSTSPA TTLQRKVEGD
     APGSDLSTAV DSPGSQPPYR LSQLPPTSSH MGGPPAGVGL PWAQRARLQP ASVALRKQEE
     EEIKRSKALS DSYELSTDLQ DKKVEMLERK YGGSFLSRRA ARTIQTAFRQ YRMNKNFERL
     RSSASESRMS RRIILSNMRM QFSFEEYEKA QNPAYFEGKP ASLDEGAMAG ARSHRLERGL
     PYGGSCGGGI DGGGSSVTTS GEFSNDITEL EDSFSKQVRS LAESIDEALN CHPSGPMSEE
     PGSAQLEKRE SKEQQEDSSA TSFSDLPLYL DDPVPPPSPE RLPSTEPPPQ GRPEFWAPAP
     LPPVPPPMPP GTREDGSREE GTRRGPGCLE CRDFRLRAAH LPLLTIEPPS DSSVDLSDRS
     DRGSVHRQLV YEADGCSPHG TLKHKGPPGR APIPHRHYPA PEGPAPAPPG PLPPAPNSGT
     GPSGVAGGRR LGKCEAAGEN SDGGDNESLE SSSNSNETIN CSSGSSSRDS LREPPATGLC
     KQTYQRETRH SWDSPAFNND VVQRRHYRIG LNLFNKKPEK GIQYLIERGF LSDTPVGVAH
     FILERKGLSR QMIGEFLGNR QKQFNRDVLE CVVDEMDFSS MDLDDALRKF QSHIRVQGEA
     QKVERLIEAF SQRYCVCNPA LVRQFRNPDT IFILAFAIIL LNTDMYSPSV KAERKMKLDD
     FIKNLRGVDN GEDIPRDLLV GIYQRIQGRE LRTNDDHVSQ VQAVERMIVG KKPVLSLPHR
     RLVCCCQLYE VPDPNRPQRL GLHQREVFLF NDLLVVTKIF QKKKILVTYS FRQSFPLVEM
     HMQLFQNSYY QFGIKLLSAV PGGERKVLII FNAPSLQDRL RFTSDLRESI AEVQEMEKYR
     VESELEKQKG MMRPNASQPG GAKDSVNGTM ARSSLEDTYG AGDGLKRGAL SSSLRDLSDA
     GKRGRRNSVG SLDSTIEGSV ISSPRPHQRM PPPPPPPPPE EYKSQRPVSN SSSFLGSLFG
     SKRGKGPFQM PPPPTGQASA SSSSASSTHH HHHHHHHGHS HGGLGVLPDG QSKLQALHAQ
     YCQGPGPAPP PYLPPQQPSL PPPPQQPPPL PQLGSIPPPP ASAPPVGPHR HFHAHGPVPG
     PQHYTLGRPG RAPRRGAGGH PQFAPHGRHP LHQPTSPLPL YSPAPQHPPA HKQGPKHFIF
     SHHPQMMPAA GAAGGPGSRP PGGSYSHPHH PQSPLSPHSP IPPHPSYPPL PPPSPHTPHS
     PLPPTSPHGP LHASGPPGTA NPPSANPKAK PSRISTVV
//
ID   PCX2_MOUSE              Reviewed;        2122 AA.
AC   Q5DU28; A2RT20; Q8BRN0; Q8C2V1; Q8CDD2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   08-FEB-2011, entry version 37.
DE   RecName: Full=Pecanex-like protein 2;
GN   Name=Pcnxl2; Synonyms=Kiaa0435;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-2122 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex, Ovary, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 182-2122 (ISOFORM 3).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 735-2122 (ISOFORM 1).
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in tumorigenesis (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q5DU28-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5DU28-2; Sequence=VSP_033613, VSP_033616;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q5DU28-3; Sequence=VSP_033614, VSP_033615;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q5DU28-4; Sequence=VSP_033612;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the pecanex family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK030215; BAC26849.1; -; mRNA.
DR   EMBL; AK043903; BAC31698.1; -; mRNA.
DR   EMBL; AK087907; BAC40038.1; -; mRNA.
DR   EMBL; AC105066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC151909; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC132334; AAI32335.2; -; mRNA.
DR   EMBL; AK220342; BAD90408.1; -; mRNA.
DR   IPI; IPI00224827; -.
DR   IPI; IPI00309888; -.
DR   IPI; IPI00885927; -.
DR   IPI; IPI00894721; -.
DR   RefSeq; NP_780770.2; NM_175561.3.
DR   UniGene; Mm.145535; -.
DR   ProteinModelPortal; Q5DU28; -.
DR   STRING; Q5DU28; -.
DR   PhosphoSite; Q5DU28; -.
DR   PRIDE; Q5DU28; -.
DR   Ensembl; ENSMUST00000047239; ENSMUSP00000042294; ENSMUSG00000060212.
DR   Ensembl; ENSMUST00000120589; ENSMUSP00000113111; ENSMUSG00000060212.
DR   GeneID; 270109; -.
DR   KEGG; mmu:270109; -.
DR   CTD; 270109; -.
DR   MGI; MGI:2445010; Pcnxl2.
DR   eggNOG; maNOG18147; -.
DR   GeneTree; ENSGT00390000013164; -.
DR   HOGENOM; HBG564661; -.
DR   HOVERGEN; HBG108237; -.
DR   InParanoid; Q5DU28; -.
DR   NextBio; 393216; -.
DR   ArrayExpress; Q5DU28; -.
DR   Bgee; Q5DU28; -.
DR   Genevestigator; Q5DU28; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR007735; Pecanex.
DR   Pfam; PF05041; Pecanex_C; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1   2122       Pecanex-like protein 2.
FT                                /FTId=PRO_0000333966.
FT   TRANSMEM     36     53       Helical; (Potential).
FT   TRANSMEM     60     82       Helical; (Potential).
FT   TRANSMEM    825    845       Helical; (Potential).
FT   TRANSMEM    849    869       Helical; (Potential).
FT   TRANSMEM    882    902       Helical; (Potential).
FT   TRANSMEM    933    953       Helical; (Potential).
FT   TRANSMEM    976    998       Helical; (Potential).
FT   TRANSMEM   1010   1030       Helical; (Potential).
FT   TRANSMEM   1080   1100       Helical; (Potential).
FT   TRANSMEM   1105   1125       Helical; (Potential).
FT   TRANSMEM   1174   1194       Helical; (Potential).
FT   TRANSMEM   1218   1238       Helical; (Potential).
FT   TRANSMEM   1245   1265       Helical; (Potential).
FT   TRANSMEM   1270   1290       Helical; (Potential).
FT   TRANSMEM   1305   1325       Helical; (Potential).
FT   COMPBIAS   1922   2048       Ser-rich.
FT   MOD_RES     972    972       Phosphoserine (By similarity).
FT   MOD_RES     975    975       Phosphoserine (By similarity).
FT   CARBOHYD    288    288       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    556    556       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1393   1393       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1534   1534       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1802   1802       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2039   2039       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1   1443       Missing (in isoform 4).
FT                                /FTId=VSP_033612.
FT   VAR_SEQ       1   1067       Missing (in isoform 2).
FT                                /FTId=VSP_033613.
FT   VAR_SEQ    1073   1121       KDVLRSDLVICSAAAVLSFAVSASTVFLSLRPFLSIVLFAL
FT                                AGTVGLIT -> VRPQHGKTACHRGPCLSAGMKLPGYSELA
FT                                GSGKAGGGPWVQSRLISRDT (in isoform 3).
FT                                /FTId=VSP_033614.
FT   VAR_SEQ    1122   2122       Missing (in isoform 3).
FT                                /FTId=VSP_033615.
FT   VAR_SEQ    1452   1452       G -> GC (in isoform 2).
FT                                /FTId=VSP_033616.
SQ   SEQUENCE   2122 AA;  234128 MW;  49D31B483000EA97 CRC64;
     MASQVLQLLR QGVWAALTGG WYHDPEHSKF TNSCHLYLWL FLLLLPLALH LAFPPNVLTA
     LFYCGSVTIF FAVIKLISYR LHLMFDKGEA IQHRSPRKRS KRKPEGEASS QHTARHKNPS
     NNRQIHSTKK EEPRGSLTTP PLCCSSRGQS VHSQHSSGPL ELPAQETVED LKGVVLSEDQ
     PEALASSTSP GMKSESLPAS QGRTPEPTPR PACPLKPVTT ELFTARKGKE SGGTAQRPAR
     HRSESGLVNP GALKKLPQLS LSQYDLLETD ISFQPWGSEH SVLLPQPNCT QGATRAQPQN
     RSPQDSLSSS CCQCNTVLAK PTEEELTRTS GQVELPLNQE VVDSDGEVAV TLIDTSQPGE
     PLSLHEPIKI VITMSSTQNS ISDLESSLHL RVTSSDRTSV RSSAESAGSG GAGPADPEQV
     RIPLITLELT EDGGGRGVSC SEGNGGERTP ERMEVMSPDR CSGSGPGDGS PTPGSTLATL
     TPRVDPESEG SKEGQANLDP ASCKSSHEKR HARVLSVDSG TDVFLSRSTK EVVSDGEKPI
     PTSKSDLEAK EGQIPNESNF LEFVSLLESI STSKVVAPDS PAEQKGASQG PEGHASPGTK
     EEAVENEKPN GRDPKPGKPD LPSQDPANGS PVFTQPAKSA ALFQGSRQRH IIYRVTSQQD
     SSVLQVISGP ETSVQEEMSL DAMHVFIDEH GEVRSCYLKS GNQKEGSSQH PPLNPDCVSH
     ARGILLSSSS STATGSPDPS SGDPAVSALQ QQLLLMVARR TQSETPRHVS QDLEDSSRSS
     AQGKFNREQF YKFIVFPGKW IKVWYDRLTL LALLDRTEDV KENMVAVLLS VLVSLLGFLT
     LNRGFCRDLW VLLFCLVMAS CQYSLLKSVQ PDPASPIHGH NQIIAYSRPI YFCMLCSLIL
     LLDAGAKAKH PPSYVVYGLK LFTPETLQAV RDHLIVFLCC FPAISLLGLF PQINTFCTYL
     LEQIDMLLFG GSAVSGITSA VYSVGRSVLA AALLHAFCFS AVKEPWSTQH IPALFSAFCG
     LLVALSYHLS RQSSDPSVLL SFIQCKLLPK CLHQNLEESA TDPLPQRMKD SVKDVLRSDL
     VICSAAAVLS FAVSASTVFL SLRPFLSIVL FALAGTVGLI THHLLPQLRK HHPWMWISHP
     VLRSKEYQQR EARDIAHLMW FERLYVWLQC FEKYLLYPAI VLNALTLDAF SISNYRRLGT
     HWDIFLMITA GMKLLRTSFC NPVHQFANLG FTVIFFHFDY KDISESFLLD FFMVSIVFTK
     LGDLLQKLQF VLAYVAPWQM AWGSSFHVFA QLFAIPHSAM LFFQTFATSI FSTPLSPFLG
     SVIFITSYVR PVKFWERSYN TRRMDNSNTR LAVQMERDPG SDDNNLNSIF YEHLTRTLQE
     SLCGDLVLGR WGNYSSGDCF ILASDDLNAF VHLIEIGNGL VTFQLRGLEF RGTYCQQREV
     EAIMEGDEDD RGCCCCKPGH LPHLLSCNAA FHLRWLTWEI TRTQYILEGY SIIDNNAATM
     LQVYDLRRVL IRYYVKSIIY YMVTSPKLVS WVKNESLLKS LQPFAKWHHI ERDLAMFNIN
     IDDDYVPCLQ GITRASYCNV FLEWIQYCAG KRQELSKTLE HVDSDEDSAL VTLAFALCIL
     GRRALGTAAH NMAMSLDSFL YGLHALFKGD FRVTARDEWV FADMDLLHKV VVPAIRMSLK
     LHQDQFTCPD EYEDPAVLYE AIRSFAKKVV ICHEGDPAWR GAMLSNKEEL LTLRHVVDEG
     ADEYKVIMLH RGFLSFKVIK VNKECVRGLW AGQQQELIFL RNRNPERGSI QNNKQVLRNL
     INSSCDQPLG YPMYVSPLTT SYLGTHKQLQ SVWGGPVTLN RVRTWFQTRW LRMRKDCSVG
     QRSGGGNIED GEGGAVPSAG GGSAPNGESR DGSTEQPRKG GTQQWSSPRG EAQRAGRRKG
     RSQSVQAHSA ISQRPPTLSS SGPILESHQA FLQTSTSVHE LAQRPSGSRL SLHTSAASLH
     SQPPPVTTTG HLSVRERAEA LIRSSLGSST SSTLSFLFGK RSFSSALVIS GLSAAEGGNT
     SDTQSSSSVN IVMGPSARAA GHAARHFSEP CEPTDSPEQG QLQDGRLAEA MEENLGVLCR
     RASQEDMGLD DTASQQSTSD EQ
//
ID   SPT13_MOUSE             Reviewed;         656 AA.
AC   Q5DU57; Q3TZ09;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Spermatogenesis-associated protein 13;
GN   Name=Spata13;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 80-656 (ISOFORM 1).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5DU57-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5DU57-2; Sequence=VSP_023287;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK158193; BAE34401.1; -; mRNA.
DR   EMBL; AC151835; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC114000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK220313; BAD90389.1; -; mRNA.
DR   IPI; IPI00828808; -.
DR   IPI; IPI00938498; -.
DR   RefSeq; NP_001028444.1; NM_001033272.1.
DR   UniGene; Mm.149776; -.
DR   HSSP; Q9ER22; 2DFK.
DR   ProteinModelPortal; Q5DU57; -.
DR   SMR; Q5DU57; 138-593.
DR   STRING; Q5DU57; -.
DR   PhosphoSite; Q5DU57; -.
DR   PRIDE; Q5DU57; -.
DR   Ensembl; ENSMUST00000022566; ENSMUSP00000022566; ENSMUSG00000021990.
DR   GeneID; 219140; -.
DR   KEGG; mmu:219140; -.
DR   UCSC; uc007ufd.1; mouse.
DR   CTD; 219140; -.
DR   MGI; MGI:104838; Spata13.
DR   eggNOG; roNOG07659; -.
DR   GeneTree; ENSGT00600000084023; -.
DR   HOVERGEN; HBG050568; -.
DR   InParanoid; Q5DU57; -.
DR   OMA; DEVHLFC; -.
DR   OrthoDB; EOG44MXRM; -.
DR   ArrayExpress; Q5DU57; -.
DR   Bgee; Q5DU57; -.
DR   CleanEx; MM_SPATA13; -.
DR   Genevestigator; Q5DU57; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; SH3 domain.
FT   CHAIN         1    656       Spermatogenesis-associated protein 13.
FT                                /FTId=PRO_0000278449.
FT   DOMAIN      151    210       SH3.
FT   DOMAIN      244    428       DH.
FT   DOMAIN      459    565       PH.
FT   COMPBIAS     24     27       Poly-Arg.
FT   VAR_SEQ       1    352       Missing (in isoform 2).
FT                                /FTId=VSP_023287.
SQ   SEQUENCE   656 AA;  75257 MW;  B85BB725EC3059E2 CRC64;
     MHPASVTTTS QDPCAPSGSC RGGRRRRPIS VIGGVSFYGN TQVEDVENLL VQPAARPPVP
     AHQVPPYKAV SARLRPFTFS QSTPIGLDRV GRRRQMKTSN VSSDGGAESS ALVDDNGSEE
     DFSYEELCQA NPRYLQPGGE QLAINELISD GSVVCAEALW DHVTMDDQEL GFKAGDVIQV
     LEASNKDWWW GRNEDKEAWF PASFVRLRVN QEELPENCSS SHGEEQDEDT SKARHKHPES
     QQQMRTNVIQ EIMNTERVYI KHLKDICEGY IRQCRKHTGM FTVAQLATIF GNIEDIYKFQ
     RKFLKDLEKQ YNKEEPHLSE IGSCFLEHQE GFAIYSEYCN NHPGACVELS NLMKHSKYRH
     FFEACRLLQQ MIDIALDGFL LTPVQKICKY PLQLAELLKY TTQEHGDYNN IKAAYEAMKN
     VACLINERKR KLESIDKIAR WQVSIVGWEG LDILDRSSEL IHSGELTKIT RQGKSQQRIF
     FLFDHQLVSC KKDLLRRDML YYKGRMDMDE VELVDVEDGR DKDWSLSLRN AFKLVSKATD
     EVHLFCARKQ EDKARWLQAY ADERRRVQED QQMGMEIPEN QKKLAMLNAQ KAGHGKSKGY
     NSCPVAPPHQ SLPPLHQRHI TVPTSIPQQQ VFALAEPKRK PSIFWHTFHK LTPFRK
//
ID   RASF5_MOUSE             Reviewed;         413 AA.
AC   Q5EBH1; O70407; Q6KAR0; Q8C2E8;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Ras association domain-containing protein 5;
DE   AltName: Full=New ras effector 1;
DE   AltName: Full=Regulator for cell adhesion and polarization enriched in lymphoid tissues;
DE            Short=RAPL;
GN   Name=Rassf5; Synonyms=Nore1, Rapl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH HRAS1.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=98157929; PubMed=9488663; DOI=10.1074/jbc.273.10.5439;
RA   Vavvas D., Li X., Avruch J., Zhang X.F.;
RT   "Identification of Nore1 as a potential Ras effector.";
RL   J. Biol. Chem. 273:5439-5442(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=BALB/c; TISSUE=Spleen;
RX   MEDLINE=22770734; PubMed=12845325; DOI=10.1038/ni950;
RA   Katagiri K., Maeda A., Shimonaka M., Kinashi T.;
RT   "RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion
RT   through spatial regulation of LFA-1.";
RL   Nat. Immunol. 4:741-748(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Natural killer cell;
RX   PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of FLJ genes:
RT   the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:127-135(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   FUNCTION IN APOPTOSIS, AND INTERACTION WITH STK4; HRAS1 AND KRAS.
RX   PubMed=11864565; DOI=10.1016/S0960-9822(02)00683-8;
RA   Khokhlatchev A., Rabizadeh S., Xavier R., Nedwidek M., Chen T.,
RA   Zhang X.F., Seed B., Avruch J.;
RT   "Identification of a novel Ras-regulated proapoptotic pathway.";
RL   Curr. Biol. 12:253-265(2002).
RN   [7]
RP   SELF-ASSOCIATION, AND INTERACTION WITH RSSF1; HRAS1; KRAS; RRAS;
RP   RRAS2; MRAS; RAP1B; RAP2A AND RALA.
RX   PubMed=11857081; DOI=10.1038/sj.onc.1205192;
RA   Ortiz-Vega S., Khokhlatchev A., Nedwidek M., Zhang X.F., Dammann R.,
RA   Pfeifer G.P., Avruch J.;
RT   "The putative tumor suppressor RASSF1A homodimerizes and
RT   heterodimerizes with the Ras-GTP binding protein Nore1.";
RL   Oncogene 21:1381-1390(2002).
RN   [8]
RP   ERRATUM.
RA   Ortiz-Vega S., Khokhlatchev A., Nedwidek M., Zhang X.F., Dammann R.,
RA   Pfeifer G.P., Avruch J.;
RL   Oncogene 21:1943-1943(2002).
RN   [9]
RP   STRUCTURE BY NMR OF 95-166, AND SUBUNIT.
RX   PubMed=16698549; DOI=10.1016/j.str.2006.03.008;
RA   Harjes E., Harjes S., Wohlgemuth S., Mueller K.H., Krieger E.,
RA   Herrmann C., Bayer P.;
RT   "GTP-Ras disrupts the intramolecular complex of C1 and RA domains of
RT   Nore1.";
RL   Structure 14:881-888(2006).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 200-357 OF MUTANT ASP-302 IN
RP   COMPLEX WITH HRAS, MUTAGENESIS OF CYS-220; LEU-221; PHE-234; LYS-236;
RP   ASP-280; LYS-283; GLN-284; LYS-302 AND LYS-303, AND INTERACTION WITH
RP   RAP1A.
RX   PubMed=18596699; DOI=10.1038/emboj.2008.125;
RA   Stieglitz B., Bee C., Schwarz D., Yildiz O., Moshnikova A.,
RA   Khokhlatchev A., Herrmann C.;
RT   "Novel type of Ras effector interaction established between tumour
RT   suppressor NORE1A and Ras switch II.";
RL   EMBO J. 27:1995-2005(2008).
CC   -!- FUNCTION: Potental tumor suppressor. Seems to be involved in
CC       lymphocyte adhesion by linking RAP1A activation upon T cell
CC       receptor or chemokine stimulation to integrin activation. Isoform
CC       2 stimulates lymphocyte polarization and the patch-like
CC       distribution of ITGAL/LFA-1, resulting in an enhanced adhesion to
CC       ICAM1. Together with RAP1A may participate in regulation of
CC       microtubule growth. The association of isoform 2 with activated
CC       RAP1A is required for directional movement of endothelial cells
CC       during wound healing (By similarity). May be involved in
CC       regulation of Ras apoptotic function. The RASSF5-STK4 complex may
CC       mediate HRAS1 and KRAS induced apoptosis.
CC   -!- SUBUNIT: Interacts directly with activated HRAS1; a RASSF5-STK4
CC       complex probably associates with activated HRAS1. Interacts with
CC       KRAS. Probably interacts with Ras-like GTPases RRAS, RRAS2, MRAS,
CC       RAP1B, RAP2A and RALA. Can self-associate. Interacts with RSSF1
CC       isoform A. The RSSF1 isoform A-RSSF5 heterodimer probably mediates
CC       the association of RSSF1 with HRAS1. Isoform 2 interacts with
CC       activated RAP1A and ITGAL/LFA-1. Binds STK4/MST1, inhibiting STK4
CC       autoactivation (By similarity).
CC   -!- INTERACTION:
CC       Q61411:Hras1; NbExp=2; IntAct=EBI-960530, EBI-400273;
CC       P20701:ITGAL (xeno); NbExp=1; IntAct=EBI-960530, EBI-961214;
CC       P62834:RAP1A (xeno); NbExp=1; IntAct=EBI-960530, EBI-491414;
CC       Q9JI11:Stk4; NbExp=1; IntAct=EBI-960530, EBI-1181352;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity). Note=Isoform 2 is mainly located in
CC       the perinuclear region of unstimulated primary T cells. Upon
CC       stimulation translocates to the leading edge and colocalizes with
CC       ITGAL/LFA-1 in the peripheral zone of the immunological synapse.
CC       Isoform 2 is localized to growing microtubules in vascular
CC       endothelial cells and is dissociated from microtubules by
CC       activated RAP1A (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5EBH1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5EBH1-2; Sequence=VSP_019368, VSP_019369;
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC   -!- SIMILARITY: Contains 1 Ras-associating domain.
CC   -!- SIMILARITY: Contains 1 SARAH domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD21397.1; Type=Erroneous initiation;
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DR   EMBL; AF053959; AAC08580.1; -; mRNA.
DR   EMBL; AY261333; AAP83361.1; -; mRNA.
DR   EMBL; AK131147; BAD21397.1; ALT_INIT; mRNA.
DR   EMBL; AK088751; BAC40546.1; -; mRNA.
DR   EMBL; AK155534; BAE33312.1; -; mRNA.
DR   EMBL; AK155869; BAE33472.1; -; mRNA.
DR   EMBL; BC089605; AAH89605.1; -; mRNA.
DR   IPI; IPI00118113; -.
DR   IPI; IPI00404645; -.
DR   RefSeq; NP_061220.2; NM_018750.3.
DR   UniGene; Mm.248291; -.
DR   PDB; 1RFH; NMR; -; A=108-166.
DR   PDB; 2FNF; NMR; -; X=95-166.
DR   PDB; 3DDC; X-ray; 1.80 A; B=200-357.
DR   PDBsum; 1RFH; -.
DR   PDBsum; 2FNF; -.
DR   PDBsum; 3DDC; -.
DR   ProteinModelPortal; Q5EBH1; -.
DR   SMR; Q5EBH1; 108-166, 200-357.
DR   DIP; DIP-29107N; -.
DR   IntAct; Q5EBH1; 36.
DR   MINT; MINT-5177821; -.
DR   STRING; Q5EBH1; -.
DR   PhosphoSite; Q5EBH1; -.
DR   PRIDE; Q5EBH1; -.
DR   Ensembl; ENSMUST00000027688; ENSMUSP00000027688; ENSMUSG00000026430.
DR   Ensembl; ENSMUST00000068564; ENSMUSP00000067011; ENSMUSG00000026430.
DR   GeneID; 54354; -.
DR   KEGG; mmu:54354; -.
DR   UCSC; uc007cnc.1; mouse.
DR   UCSC; uc007cnd.1; mouse.
DR   CTD; 54354; -.
DR   MGI; MGI:1926375; Rassf5.
DR   eggNOG; roNOG14929; -.
DR   GeneTree; ENSGT00390000003367; -.
DR   HOGENOM; HBG443714; -.
DR   HOVERGEN; HBG054362; -.
DR   InParanoid; Q5EBH1; -.
DR   OMA; LHISSVT; -.
DR   OrthoDB; EOG4640C5; -.
DR   PhylomeDB; Q5EBH1; -.
DR   NextBio; 311142; -.
DR   ArrayExpress; Q5EBH1; -.
DR   Bgee; Q5EBH1; -.
DR   Genevestigator; Q5EBH1; -.
DR   GermOnline; ENSMUSG00000026430; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000159; Ras-assoc.
DR   InterPro; IPR011524; SARAH.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00788; RA; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00314; RA; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50951; SARAH; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Apoptosis; Cytoplasm;
KW   Cytoskeleton; Metal-binding; Microtubule; Phosphoprotein;
KW   Tumor suppressor; Zinc; Zinc-finger.
FT   CHAIN         1    413       Ras association domain-containing protein
FT                                5.
FT                                /FTId=PRO_0000240402.
FT   DOMAIN      265    359       Ras-associating.
FT   DOMAIN      361    408       SARAH.
FT   ZN_FING     117    165       Phorbol-ester/DAG-type.
FT   MOD_RES     268    268       Phosphothreonine (By similarity).
FT   MOD_RES     347    347       Phosphothreonine (By similarity).
FT   VAR_SEQ       1    142       Missing (in isoform 2).
FT                                /FTId=VSP_019368.
FT   VAR_SEQ     143    188       ALRCANCKFTCHSECRSLIQLDCRQKGGPALDRRSPESTLT
FT                                PTLNQ -> MTVDSSMSSGYCSLDEELEDCFFTAKTTFFRN
FT                                LQSKQPSK (in isoform 2).
FT                                /FTId=VSP_019369.
FT   MUTAGEN     220    220       C->A: Reduced interaction with HRAS.
FT   MUTAGEN     220    220       C->D: Strongly reduced interaction with
FT                                HRAS.
FT   MUTAGEN     221    221       L->A,D: Strongly reduced interaction with
FT                                HRAS.
FT   MUTAGEN     234    234       F->A: Reduced interaction with HRAS.
FT   MUTAGEN     236    236       K->A: Reduced interaction with HRAS.
FT   MUTAGEN     280    280       D->A: Reduced interaction with HRAS.
FT   MUTAGEN     283    283       K->A: Very strong reduction of the
FT                                interaction with HRAS.
FT   MUTAGEN     284    284       Q->A: Reduced interaction with HRAS.
FT   MUTAGEN     302    302       K->D: Reduced specificity for HRAS and
FT                                diminished discrimination between HRAS
FT                                and RAP1A.
FT   MUTAGEN     303    303       K->A: Strongly reduced interaction with
FT                                HRAS.
FT   CONFLICT    179    179       E -> G (in Ref. 1; AAC08580).
FT   CONFLICT    251    257       IRPQSIY -> SGPSPSM (in Ref. 1; AAC08580).
FT   TURN        133    135
FT   STRAND      137    139
FT   TURN        147    149
FT   HELIX       155    158
SQ   SEQUENCE   413 AA;  46714 MW;  E6FF7DDE6BECB180 CRC64;
     MASPAIGQRP YPLLLDPEPP RYLQSLGGTE PPPPARPRRC IPTALIPAAG ASEDRGGRRS
     GRRDPEPTPR DCRHARPVRP GLQPRLRLRP GSHRPRDVRS IFEQPQDPRV LAERGEGHRF
     VELALRGGPG WCDLCGREVL RQALRCANCK FTCHSECRSL IQLDCRQKGG PALDRRSPES
     TLTPTLNQNV CKAVEETQHP PTIQEIKQKI DSYNSREKHC LGMKLSEDGT YTGFIKVHLK
     LRRPVTVPAG IRPQSIYDAI KEVNPAATTD KRTSFYLPLD AIKQLHISST TTVSEVIQGL
     LKKFMVVDNP QKFALFKRIH KDGQVLFQKL SIADYPLYLR LLAGPDTDVL SFVLKENETG
     EVEWDAFSIP ELQNFLTILE KEEQDKIHQL QKKYNKFRQK LEEALRESQG KPG
//
ID   ERMIN_MOUSE             Reviewed;         281 AA.
AC   Q5EBJ4; Q3UVY3; Q5DTZ8; Q8C5L8; Q9CTR3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Ermin;
DE   AltName: Full=Juxtanodin;
DE            Short=JN;
GN   Name=Ermn; Synonyms=Kiaa1189;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16421295; DOI=10.1523/JNEUROSCI.4317-05.2006;
RA   Brockschnieder D., Sabanay H., Riethmacher D., Peles E.;
RT   "Ermin, a myelinating oligodendrocyte-specific protein that regulates
RT   cell morphology.";
RL   J. Neurosci. 26:757-762(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Diencephalon, Medulla oblongata, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Plays a role in cytoskeletal rearrangements during the
CC       late wrapping and/or compaction phases of myelinogenesis as well
CC       as in maintenance and stability of myelin sheath in the adult. May
CC       play an important role in late-stage oligodendroglia maturation,
CC       myelin/Ranvier node formation during CNS development, and in the
CC       maintenance and plasticity of related structures in the mature CNS
CC       (By similarity).
CC   -!- SUBUNIT: Binds actin.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- TISSUE SPECIFICITY: Brain and spinal cord. Exclusively expressed
CC       by the oligodendrocytes. Appears at a late stage during
CC       myelination, and in the mature nerves, it is localized to the
CC       outer cytoplasmic lip of the myelin sheath and the paranodal
CC       loops.
CC   -!- DEVELOPMENTAL STAGE: Weakly detectable in the first 3 postnatal
CC       days, but increases during the initial 2 weeks after birth.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC37121.1; Type=Frameshift; Positions=206, 224, 263;
CC       Sequence=BAD90431.1; Type=Erroneous initiation;
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DR   EMBL; DQ334270; ABC67250.1; -; mRNA.
DR   EMBL; AK220372; BAD90431.1; ALT_INIT; mRNA.
DR   EMBL; AK020733; BAB32193.1; -; mRNA.
DR   EMBL; AK078089; BAC37121.1; ALT_FRAME; mRNA.
DR   EMBL; AK136820; BAE23136.1; -; mRNA.
DR   EMBL; AK137305; BAE23300.1; -; mRNA.
DR   EMBL; AL928564; CAM18782.1; -; Genomic_DNA.
DR   EMBL; BC089515; AAH89515.1; -; mRNA.
DR   EMBL; BC090670; AAH90670.1; -; mRNA.
DR   IPI; IPI00624843; -.
DR   RefSeq; NP_084248.2; NM_029972.3.
DR   UniGene; Mm.91712; -.
DR   ProteinModelPortal; Q5EBJ4; -.
DR   SMR; Q5EBJ4; 209-278.
DR   STRING; Q5EBJ4; -.
DR   PhosphoSite; Q5EBJ4; -.
DR   PRIDE; Q5EBJ4; -.
DR   Ensembl; ENSMUST00000090940; ENSMUSP00000088458; ENSMUSG00000026830.
DR   GeneID; 77767; -.
DR   KEGG; mmu:77767; -.
DR   UCSC; uc008jsh.1; mouse.
DR   CTD; 77767; -.
DR   MGI; MGI:1925017; Ermn.
DR   eggNOG; roNOG16053; -.
DR   GeneTree; ENSGT00390000005845; -.
DR   HOGENOM; HBG506358; -.
DR   HOVERGEN; HBG102710; -.
DR   InParanoid; Q5EBJ4; -.
DR   OMA; EWLGFRK; -.
DR   OrthoDB; EOG4N04FN; -.
DR   PhylomeDB; Q5EBJ4; -.
DR   NextBio; 347511; -.
DR   ArrayExpress; Q5EBJ4; -.
DR   Bgee; Q5EBJ4; -.
DR   CleanEx; MM_ERMN; -.
DR   Genevestigator; Q5EBJ4; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0030175; C:filopodium; IDA:MGI.
DR   GO; GO:0033269; C:internode region of axon; IDA:MGI.
DR   GO; GO:0043209; C:myelin sheath; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0033270; C:paranode region of axon; IDA:MGI.
DR   GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR   GO; GO:0007015; P:actin filament organization; IDA:MGI.
DR   GO; GO:0001763; P:morphogenesis of a branching structure; IDA:MGI.
DR   GO; GO:0031344; P:regulation of cell projection organization; IDA:MGI.
DR   GO; GO:0008360; P:regulation of cell shape; IDA:MGI.
PE   1: Evidence at protein level;
KW   Actin-binding; Cytoplasm; Cytoskeleton.
FT   CHAIN         1    281       Ermin.
FT                                /FTId=PRO_0000314749.
FT   REGION      262    281       Binds actin.
FT   COMPBIAS    170    221       Glu-rich.
FT   CONFLICT     97     97       L -> P (in Ref. 3; BAE23136).
FT   CONFLICT    169    169       D -> DE (in Ref. 2; BAD90431).
FT   CONFLICT    171    171       E -> G (in Ref. 3; BAC37121).
SQ   SEQUENCE   281 AA;  32148 MW;  0D457492AAEB18CB CRC64;
     MTDTPETLSG TECNGDRPPE NGQQPSSQTR QETTDADETQ AYYKVEPSLE DLPAKENQEE
     TGNTKGNILP KGPEDEKILN ENPEENLFVV HQAIKDLSLQ EISAEDMAFR EGHPWKKIPP
     NSSNLEVSRQ KERTAQQQLE QRGDASTTEI EWLGFQKSRP VDILHSKCDE EEEEEEEVWN
     EEINEEDVDE CAEEEDEVRV IEFKRKHREG SPLKEESLAR EDSPLGSPGS QPGTPDEQPV
     FGKKGDIARN SYSRYNTISY RKIRKGNTKQ RIDEFESMMH L
//
ID   Q5EBQ0_MOUSE            Unreviewed;       284 AA.
AC   Q5EBQ0;
DT   15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2005, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   SubName: Full=Putative uncharacterized protein;
DE   SubName: Full=Voltage-dependent anion channel 3;
GN   Name=Vdac3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Bone marrow;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Bone marrow;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Bone marrow;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Bone marrow;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Bone marrow;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Bone marrow;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Bone marrow;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Heart;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC089336; AAH89336.1; -; mRNA.
DR   EMBL; AK146957; BAE27565.1; -; mRNA.
DR   EMBL; AK150828; BAE29890.1; -; mRNA.
DR   EMBL; AK168815; BAE40642.1; -; mRNA.
DR   EMBL; AK169099; BAE40882.1; -; mRNA.
DR   IPI; IPI00122548; -.
DR   RefSeq; NP_001185927.1; NM_001198998.1.
DR   UniGene; Mm.227704; -.
DR   STRING; Q5EBQ0; -.
DR   PRIDE; Q5EBQ0; -.
DR   Ensembl; ENSMUST00000110715; ENSMUSP00000106343; ENSMUSG00000008892.
DR   GeneID; 22335; -.
DR   MGI; MGI:106922; Vdac3.
DR   GeneTree; ENSGT00390000011336; -.
DR   HOGENOM; HBG396026; -.
DR   HOVERGEN; HBG054036; -.
DR   InParanoid; Q5EBQ0; -.
DR   OMA; CFSLGSN; -.
DR   PhylomeDB; Q5EBQ0; -.
DR   ArrayExpress; Q5EBQ0; -.
DR   Bgee; Q5EBQ0; -.
DR   Genevestigator; Q5EBQ0; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:InterPro.
DR   GO; GO:0008308; F:voltage-gated anion channel activity; IEA:InterPro.
DR   GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR   GO; GO:0007612; P:learning; IMP:MGI.
DR   GO; GO:0007270; P:nerve-nerve synaptic transmission; IMP:MGI.
DR   InterPro; IPR001925; Porin_Euk.
DR   Pfam; PF01459; Porin_3; 1.
DR   PRINTS; PR00185; EUKARYTPORIN.
DR   PROSITE; PS00558; EUKARYOTIC_PORIN; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane beta strand; Transport.
SQ   SEQUENCE   284 AA;  30884 MW;  33B6AA4D4E07A41D CRC64;
     MCNTPTYCDL GKAAKDVFNK GYGFGMVKID LKTKSCSGVM EFSTSGHAYT DTGKASGNLE
     TKYKVCNYGL TFTQKWNTDN TLGTEISWEN KLAEGLKLTL DTIFVPNTGK KSGKLKASYR
     RDCFSLGSNV DIDFSGPTIY GWAVLAFEGW LAGYQMSFDT AKSKLSQNNF ALGYKAADFQ
     LHTHVNDGTE FGGSIYQKVN ERIETSINLA WTAGSNNTRF GIAAKYKLDC RTSLSAKVNN
     ASLIGLGYTQ TLRPGVKLTL SALIDGKNFN AGGHKVGLGF ELEA
//
ID   AAPK1_MOUSE             Reviewed;         559 AA.
AC   Q5EG47;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=5'-AMP-activated protein kinase catalytic subunit alpha-1;
DE            Short=AMPK subunit alpha-1;
DE            EC=2.7.11.1;
GN   Name=Prkaa1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-559.
RC   STRAIN=C57BL/6N; TISSUE=Muscle;
RA   Xie X., Chen Y.;
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   ENZYME REGULATION, AND PHOSPHORYLATION AT THR-183.
RX   PubMed=16054095; DOI=10.1016/j.cmet.2005.05.009;
RA   Hawley S.A., Pan D.A., Mustard K.J., Ross L., Bain J., Edelman A.M.,
RA   Frenguelli B.G., Hardie D.G.;
RT   "Calmodulin-dependent protein kinase kinase-beta is an alternative
RT   upstream kinase for AMP-activated protein kinase.";
RL   Cell Metab. 2:9-19(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184 AND SER-508, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Responsible for the regulation of fatty acid synthesis
CC       by phosphorylation of acetyl-CoA carboxylase. It also regulates
CC       cholesterol synthesis via phosphorylation and inactivation of
CC       hormone-sensitive lipase and hydroxymethylglutaryl-CoA reductase.
CC       Appears to act as a metabolic stress-sensing protein kinase
CC       switching off biosynthetic pathways when cellular ATP levels are
CC       depleted and when 5'-AMP rises in response to fuel limitation
CC       and/or hypoxia. This is a catalytic subunit (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: Binding of AMP results in allosteric
CC       activation, inducing phosphorylation on Thr-183 by STK11 in
CC       complex with STE20-related adapter-alpha (STRAD alpha) pseudo
CC       kinase and CAB39. Also activated by phosphorylation by CAMKK2
CC       triggered by a rise in intracellular calcium ions, without
CC       detectable changes in the AMP/ATP ratio.
CC   -!- SUBUNIT: Heterotrimer of an alpha catalytic subunit, a beta and a
CC       gamma non-catalytic subunits. Interacts with FNIP1 and FNIP2 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. SNF1 subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AC131919; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC135079; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY885266; AAW79567.1; -; mRNA.
DR   IPI; IPI00556823; -.
DR   RefSeq; NP_001013385.3; NM_001013367.3.
DR   UniGene; Mm.207004; -.
DR   ProteinModelPortal; Q5EG47; -.
DR   SMR; Q5EG47; 21-347, 407-559.
DR   STRING; Q5EG47; -.
DR   PRIDE; Q5EG47; -.
DR   Ensembl; ENSMUST00000051186; ENSMUSP00000063166; ENSMUSG00000050697.
DR   GeneID; 105787; -.
DR   KEGG; mmu:105787; -.
DR   CTD; 105787; -.
DR   MGI; MGI:2145955; Prkaa1.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG050432; -.
DR   InParanoid; Q5EG47; -.
DR   OMA; YICKNGK; -.
DR   OrthoDB; EOG4BK53H; -.
DR   PhylomeDB; Q5EG47; -.
DR   BRENDA; 2.7.11.1; 244.
DR   ArrayExpress; Q5EG47; -.
DR   Bgee; Q5EG47; -.
DR   Genevestigator; Q5EG47; -.
DR   GermOnline; ENSMUSG00000050697; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0019395; P:fatty acid oxidation; IMP:MGI.
DR   GO; GO:0006006; P:glucose metabolic process; IMP:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cholesterol biosynthesis; Fatty acid biosynthesis;
KW   Kinase; Lipid synthesis; Magnesium; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Steroid biosynthesis;
KW   Sterol biosynthesis; Transferase.
FT   CHAIN         1    559       5'-AMP-activated protein kinase catalytic
FT                                subunit alpha-1.
FT                                /FTId=PRO_0000085590.
FT   DOMAIN       27    279       Protein kinase.
FT   NP_BIND      33     41       ATP (By similarity).
FT   ACT_SITE    150    150       Proton acceptor (By similarity).
FT   BINDING      56     56       ATP (By similarity).
FT   MOD_RES      32     32       Phosphothreonine (By similarity).
FT   MOD_RES     183    183       Phosphothreonine; by STK11 (By
FT                                similarity).
FT   MOD_RES     184    184       Phosphoserine.
FT   MOD_RES     187    187       Phosphoserine (By similarity).
FT   MOD_RES     355    355       Phosphothreonine (By similarity).
FT   MOD_RES     356    356       Phosphoserine (By similarity).
FT   MOD_RES     382    382       Phosphothreonine (By similarity).
FT   MOD_RES     397    397       Phosphoserine (By similarity).
FT   MOD_RES     441    441       Phosphotyrosine (By similarity).
FT   MOD_RES     442    442       Phosphotyrosine (By similarity).
FT   MOD_RES     467    467       Phosphoserine (By similarity).
FT   MOD_RES     476    476       Phosphoserine (By similarity).
FT   MOD_RES     486    486       Phosphoserine (By similarity).
FT   MOD_RES     488    488       Phosphothreonine (By similarity).
FT   MOD_RES     490    490       Phosphothreonine (By similarity).
FT   MOD_RES     496    496       Phosphoserine (By similarity).
FT   MOD_RES     502    502       Phosphoserine (By similarity).
FT   MOD_RES     506    506       Phosphoserine (By similarity).
FT   MOD_RES     508    508       Phosphoserine.
FT   MOD_RES     520    520       Phosphoserine (By similarity).
FT   MOD_RES     522    522       Phosphothreonine (By similarity).
FT   MOD_RES     523    523       Phosphoserine (By similarity).
FT   MOD_RES     524    524       Phosphoserine (By similarity).
FT   MOD_RES     527    527       Phosphoserine (By similarity).
FT   CONFLICT     11     12       Missing (in Ref. 2; AAW79567).
SQ   SEQUENCE   559 AA;  63929 MW;  08632503663D395B CRC64;
     MRRLSSWRKM ATAEKQKHDG RVKIGHYILG DTLGVGTFGK VKVGKHELTG HKVAVKILNR
     QKIRSLDVVG KIRREIQNLK LFRHPHIIKL YQVISTPSDI FMVMEYVSGG ELFDYICKNG
     RLDEKESRRL FQQILSGVDY CHRHMVVHRD LKPENVLLDA HMNAKIADFG LSNMMSDGEF
     LRTSCGSPNY AAPEVISGRL YAGPEVDIWS SGVILYALLC GTLPFDDDHV PTLFKKICDG
     IFYTPQYLNP SVISLLKHML QVDPMKRAAI KDIREHEWFK QDLPKYLFPE DPSYSSTMID
     DEALKEVCEK FECSEEEVLS CLYNRNHQDP LAVAYHLIID NRRIMNEAKD FYLATSPPDS
     FLDDHHLTRP HPERVPFLVA ETPRARHTLD ELNPQKSKHQ GVRKAKWHLG IRSQSRPNDI
     MAEVCRAIKQ LDYEWKVVNP YYLRVRRKNP VTSTFSKMSL QLYQVDSRTY LLDFRSIDDE
     ITEAKSGTAT PQRSGSISNY RSCQRSDSDA EAQGKPSDVS LTSSVTSLDS SPVDVAPRPG
     SHTIEFFEMC ANLIKILAQ
//
ID   Q5F226_MOUSE            Unreviewed;      4351 AA.
AC   Q5F226;
DT   15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2005, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   SubName: Full=FAT tumor suppressor homolog 2 (Drosophila);
DE   SubName: Full=MCG1445;
GN   Name=Fat2; ORFNames=RP24-239D8.6-001, mCG_1445;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Phillimore B.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL713870; CAI52049.1; -; Genomic_DNA.
DR   EMBL; CH466575; EDL33495.1; -; Genomic_DNA.
DR   IPI; IPI00343214; -.
DR   RefSeq; NP_001025159.1; NM_001029988.2.
DR   UniGene; Mm.339363; -.
DR   ProteinModelPortal; Q5F226; -.
DR   SMR; Q5F226; 1041-1234, 2262-2377, 2790-2902, 3022-3105, 3330-3524, 3778-3927, 3955-4035.
DR   STRING; Q5F226; -.
DR   PhosphoSite; Q5F226; -.
DR   PRIDE; Q5F226; -.
DR   Ensembl; ENSMUST00000068853; ENSMUSP00000067556; ENSMUSG00000055333.
DR   Ensembl; ENSMUST00000108864; ENSMUSP00000104492; ENSMUSG00000055333.
DR   GeneID; 245827; -.
DR   KEGG; mmu:245827; -.
DR   UCSC; uc007izf.1; mouse.
DR   CTD; 245827; -.
DR   MGI; MGI:2685369; Fat2.
DR   HOGENOM; HBG444162; -.
DR   HOVERGEN; HBG005641; -.
DR   InParanoid; Q5F226; -.
DR   OMA; IDKDSGP; -.
DR   NextBio; 386938; -.
DR   ArrayExpress; Q5F226; -.
DR   Bgee; Q5F226; -.
DR   Genevestigator; Q5F226; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   InterPro; IPR006209; EGF.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR012680; Laminin_G_2.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 33.
DR   Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 1.
DR   Pfam; PF00028; Cadherin; 28.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF02210; Laminin_G_2; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 33.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00282; LamG; 1.
DR   SUPFAM; SSF49313; Cadherin; 33.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
DR   PROSITE; PS00232; CADHERIN_1; 13.
DR   PROSITE; PS50268; CADHERIN_2; 32.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; EGF-like domain; Membrane; Repeat;
KW   Transmembrane.
SQ   SEQUENCE   4351 AA;  480109 MW;  72F9DADAAA5467D5 CRC64;
     MTLVLLGVAM VLLHRAACEK PLEETITPLT WRFTHSLYNA TIYENSAPKT YVESPVKMGM
     YLAEPHWVVK YRIISGDAAG VFKTEEHVVG NFCFLRIRTK SSNTALLNRE VRDSYTLVVQ
     ASDKSLEFEA LTQVVVHILD QNDLKPLFSP PSYRFTISED RPLKSPICKV TATDADLGQN
     AEFYYAFNAR SEVFAIHPTS GVVTVAGKLN VTWRGKYELQ VLAVDRMRKI SEGNGFGNLA
     PLVIYVEPVH RKPPVITLVV LNPPEGDEGD IYATVTVDTN GSGAEVDSLE VVGGDPGKYF
     KVLKSYAQGN EFNLVAVRDI NWAEHLHGFN ISLQTHSRSR FPSRSIIRAF HLPPYTLANL
     RFEKAVYRVK LSEFSPPGSR VALVRVTTAL PTLRYALKPS SGSTVFKLNA RTGLITTTKP
     VDFHEQNQYQ LHVKTSLGQA TTTVIIDIVD CNNHAPVFNR SSYEGTLDEN IPPGTSVLTV
     TATDQDHGDN GHITYSIAGP KAVPFSIDPY LGVISTTKSM DYELMKRIYT FRVRASDWGS
     PFRQEKEVSV SLRLKNLNDN QPMFEEVNCT VSLRQDAPVG KSIMAVSAID MDELQNLKYE
     IVSGNEQDYF HLNHFSGVIS LKRSFMNLTA VRPTVYSLKI TASDGKNYAS PTTLKVTVVK
     DPRSEVPVQC DKTGVLTHIT KTILQSAGLQ GQEMGEEDFT SLGNYQINHH APQFEDHFPQ
     SIDILEQVPV NTPLAHLAAT DPDPGFHGRL VYVIADGNEE GCFDIELETG LLTVAAALDY
     ETTSFYVLNV TVYDLGTPPK SSWKLLTVTV KDWNDKPPRF PPGGYQLTIS EDTEVGTTVA
     ELKTRDTDSE DNGRVRYTLL TPTEKFSLHP LTGELVVTGQ LDRESEPQYI LKAEARDQPT
     KGHQLFSVTD VIVTLEDIND NPPQCITEHS SLKVPEDMPL GTVLTFLDAS DPDLGPAGEV
     KYILVDDVHG TFRVDPMTGA LSLEKELDFE RRAGYNLSFW ASDSGRPLAR RTLCHVEVLV
     MDVNENLHSP HFSSFVYQGQ VQENSPAGTQ VMVVTAQDDD SGLDGELQYF LRAGTGLEAF
     SINQDTGMLE TLAPLDREFT PYYWLTVLAV DRGSVPLSAV TEVYIEVTDI NDNIPSMSRP
     VFYPSVKEDA PLGTSVLQLE AWDPDFSSQG KLTFNLTSGN HMGHFIVHPF TGLLSTAKQL
     DRENKDEYVL EVTVQDNGDP PLRSTSRVVV CVLDVNDNSP MFSHKLFNVR LSERLSPLSP
     EPVYRLVASD PDEGLNGSIT YSIEESDEES FRIDPVTGVV SSSSTFAAGE YNILTIKATD
     SGQPALSTSV RLHIEWIPQP RPSSIPLSFD ESHYSFAVME TDPVNHMLGV ISVEGRPGLF
     WFHISDGDKD MDFDIEKTTG SIVIARPLDT RRKSSYNLTV EVTDGFHTIA TQVHILMIAN
     INHHRPQFLQ DHYDIRVPQD TLPGVELLRV QATDQDHGKG LIYTIHSSRD PGSANLFQLD
     PSSGVLVTVG TLDLHSGPSQ HILTVMVRDQ EMPIKRNFVW VTIHVEDGNL HSPHFTQPRY
     EANVPDTTTP GTELLQVRAV DADRGANAEV HYSFLKGNSE GFFNIDSLLG IITVAQRLDH
     VHLNRHALTV KAEDQGSPQR HDLAMVVVHV HPSDSSAPIF SKDEYFIEIP ESVPIGSPIL
     LISAASSSDV TYELREGNKN SVFSMNSYSG LISTQKRLDH EKVSSYQLKI RGSNMAGVFT
     EVVALVYIID ENDNAPAFLK STFVGHISEA APLHSLILGE DNSPLVIRAS DSDQEANSLL
     VYKILEPEAL KFFKIDPSMG TLTITSELDY ETTPLFQFSI YVHDQGTPIL FAPRSARVII
     HVRDVNDSPP RFSEQIYEVA VVEPIHPGME LLTVQAEDND SKVTYSIKTS NTDEAVTIHP
     ITGQISVVNP AALRLFPKLN IRAFDGLYQD TAVVKISLTQ ALDKSLQFDQ DIYRARVTEN
     TPHSNVLVIL GVHGNHLNDT LSYFLLNGTD LFHMVKSAGV LQTRGVTFDR EQQDTHEVAV
     EVRDNRVPRR VAQALVRVSV EDVNDNIPEF QHLPYYTVIQ DGTEPGDVLF QVSATDKDLG
     ANGTVTYGFA EDYAYFRIDP YVGDISLKKP FDYQALNKYH LRVTARDAGT PPLQTEVEVH
     VTVRNKSNPL FQSPYYKVKV PENITLYTPI LHTQARSPEG LRLIYNIVEE EPLMLFTTDF
     KTGVLTVTGP LDYESKNKHV FTVRATDTAL GSFSEATVEV LVEDINDNPP TFSQLVYSTS
     VSEGSPAQTP VIQLLASDQD SGQNQDVSYQ IVEDGSDVSK FFRINGSTGE MFTIQELDYE
     AHQHFRVKVR ATDRGDPPLT GETLVVVNVS DINDNPPEFR EPQYEANVSE LATCGHLVLK
     VQALDPDIGD TSRLEYLILS GNQDRHFSIN STSGIISMFN LCKKQLDSSY NLRVGASDGV
     FQATVPVYIN TTNANKYSPE FQQNVYEAEL AENAKVGTKV IELLAIDKDS GPYGTVDYTI
     INKLAGERFF INPSGQITTL QKLDRENSTE RVIAIKIMAR DGGGKVAFCT VKIILTDEND
     NAPQFKASGY TVSIPSNVSR DSPIIQVLAY DADEGRNADV TYSVDSTEDL AEEIIEVNPT
     TGVVKVKESL VGLENKAVDF NIKAQDGGPP HWDSLVPVRL QVVPNEIPLP KFSEPLYTFS
     ASEDLPEGSE IGSVKAVAAQ DPIIYSLVQG TTPESNSDDV FSLDQDTGVL KVKKAMDHES
     TKWYQIDLMA HCPHEDTDLV SLVSVNIQVE DVNDNRPVFE ADPYKAFLTE NMPGGTTVIQ
     VTANDQDTGS DGQVSYRLSV EPGSNIHQLF AVDSESGWIT TLQELDCETQ QTYRFYVVAF
     DHGQTIQLSS QALVEVSITD ENDNPPRFAS EDYRGSVVEN NEPGELVATL KTLDADISEQ
     NRQVTCYITE GDPLGQFSIS QVGDEWRITS RKTLDREHIA KYLLRITASD GKFQASVPVE
     VFVLDINDNS PQCSQLLYTG KVREDVTPGH FILKVSAIDV DMDTNAQITY SLHGPGAQEF
     KLDPHTGELT TLSVLDRERK DVYNLVAKAT DGGGQSCQAE VTLHIEDVND NAPRFFPSHC
     AVAVFDNTTV KTPVAVVFAR DPDQGVNAQV VYSLTDSADG QFSIDATSGV IRLEKPLQVR
     SSSAVELTVR ASDLGTPIPL STLGTVTVSI VGLEDYLPIF LNSEHSTQVP EDALIDMEVL
     YLATLTRPGS EKTGYHITGG NEQGKFRLDA HTGILYVNGS LDFETNPKYF LSIECSRKSS
     SSLSDVTTIV INVTDVNEHH PRFTHDLYTV RVLENAIVGD VILTVSASDD DGPVNSVITY
     SLVGGNQLGH FTIDPKKGKL QVAKALDWEQ TPSYSLRIRA TDSGQPPLHE DTEVAVEVVD
     VNDNPPRFFQ LNYSTAVQEN SPIGIKVLQL ILDDPDSPQN GPPYFFRITE GNTGSVFRVT
     PDGWLVTAGS LSRRAQEWYQ LHIEVSDSGL PPLSSSTLVR VHITEQSRYP PSTLPLEIFI
     TKGEEEFQGG MVGKIHATDR DPQDTLTYSL DREGSLGKYF TVGASDGKII ASQGLPRGRY
     LFNVTVSDGT FTTTTGVHVH VWHMGQEAPQ QAVWLGFHQL TPEELVSDHW RNLQRFLSNI
     LDIKRANIHL ASLQPAEVTA GVDVLLAFEG HSGTSYDLQE LASAIAHSAK EMEHSVGIQM
     RSALPVVPCQ GPSCQDQTCQ ETVSLEPRVG PSYSTARLSI LTPRHHLGKN CSCNGTTWRF
     SGQSYMRYRP LEAQNWQIHF YLKTLQPWAL LMFTNETASI SLKLANGFLH LEYRCPGGFY
     GNLSSHRPVN DGQWHSMLLE ERDTSVHLLV DITDNTSLVI PEECQGLRTE RHLLLGGLVP
     SNPSSNVSLG FEGCLDAVVV NSERLELLGH RKKMAGYLET WALSQCCWPG TTCSQNPCLN
     GGSCSPALGS GYLCRCPPLF SGRNCELGRE NCTSAPCQEG GTCVSSPEGT SCSCPHPYTG
     DRCEMEARGC SGGHCLITPE IKRGDWGQQE FLVIIVALPL LIIATVGLLL YCRRCKSHKP
     VAMEDPDLLA RSIGVDTQAS PAIELDPLNA GSCNDLNQLE PSKTSVPNEL VTFGPSSKQR
     PMVCSVPPRL PPAVVSSHPG HEPIIKRTWS GEELVYPSGA AVWPPTYSRK EHWEYPHPEA
     MQGPLPPSPR RHVSPAVMPD PAGLYGGFPF PLELENKRAP LPPRYSNQNL EDLIPPRPPS
     PREHLLAPCL NEYTAISYYH SQFRQGGGGP CLAEGGYKGV SMRLSRAGPS YADCEVNGGP
     APGRSQPRAP PNYEGSDMVE SDYGSCEEVM F
//
ID   Q5F272_MOUSE            Unreviewed;       184 AA.
AC   Q5F272;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   05-OCT-2010, entry version 16.
DE   SubName: Full=Cannabinoid receptor interacting protein 1;
DE   Flags: Fragment;
GN   Name=Cnrip1; ORFNames=RP23-348N2.3-002;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Tracey A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL606466; CAI51923.1; -; Genomic_DNA.
DR   IPI; IPI00648948; -.
DR   UniGene; Mm.425666; -.
DR   PRIDE; Q5F272; -.
DR   Ensembl; ENSMUST00000131515; ENSMUSP00000122150; ENSMUSG00000044629.
DR   MGI; MGI:1917505; Cnrip1.
DR   HOVERGEN; HBG056498; -.
DR   PhylomeDB; Q5F272; -.
DR   Bgee; Q5F272; -.
DR   Genevestigator; Q5F272; -.
PE   4: Predicted;
FT   NON_TER     184    184
SQ   SEQUENCE   184 AA;  20726 MW;  FB30F33D1A99055A CRC64;
     MGDLPGLVRL SIALRIQPND GPVFFKVDGQ RFGQNRTIKL LTGSSYKVEV KIKPTTLQVE
     NISIGGVLVP LELKGKEPDG ERVVYTGIYD TEGVAPTKSG ERQPIQITMP VSPSCGCGDM
     ASEQRNCRGR NHYFFTNKER CAGASFYGNR VQFPSWTCEK RERVIFTDAF FFHERLTFKK
     IKIK
//
ID   NUFP2_MOUSE             Reviewed;         692 AA.
AC   Q5F2E7; Q3TCE2; Q3V195; Q80TF1;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Nuclear fragile X mental retardation-interacting protein 2;
DE   AltName: Full=82 kDa FMRP-interacting protein;
DE            Short=82-FIP;
DE   AltName: Full=FMRP-interacting protein 2;
GN   Name=Nufip2; Synonyms=Kiaa1321;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Dendritic cell, Embryo, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=22721714; PubMed=12837692; DOI=10.1093/hmg/ddg181;
RA   Bardoni B., Castets M., Huot M.-E., Schenck A., Adinolfi S.,
RA   Corbin F., Pastore A., Khandjian E.W., Mandel J.-L.;
RT   "82-FIP, a novel FMRP (fragile X mental retardation protein)
RT   interacting protein, shows a cell cycle-dependent intracellular
RT   localization.";
RL   Hum. Mol. Genet. 12:1689-1698(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-213 AND
RP   SER-215, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Binds RNA (By similarity).
CC   -!- SUBUNIT: Interacts with FMRP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localized in both
CC       nucleus and cytoplasm in most neurons. In the cortex, distributed
CC       in a diffuse way in the nucleus and in the cytoplasm. Localized in
CC       the cytoplasm in neurons of the dentate gyrus in the olfactive
CC       bulb, in the ependymal epithelium and in the granular layer of the
CC       cerebellum. In Purkinje cells, distributed in both cell
CC       compartments and in nuclear dots adjacent to the nucleolus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5F2E7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5F2E7-2; Sequence=VSP_019729;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65776.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK122494; BAC65776.1; ALT_INIT; mRNA.
DR   EMBL; AK132603; BAE21256.1; -; mRNA.
DR   EMBL; AK152336; BAE31134.1; -; mRNA.
DR   EMBL; AK160601; BAE35905.1; -; mRNA.
DR   EMBL; AK170764; BAE42015.1; -; mRNA.
DR   EMBL; AL591136; CAI51880.1; -; Genomic_DNA.
DR   IPI; IPI00330146; -.
DR   IPI; IPI00761357; -.
DR   RefSeq; NP_001019376.1; NM_001024205.2.
DR   UniGene; Mm.428996; -.
DR   STRING; Q5F2E7; -.
DR   PhosphoSite; Q5F2E7; -.
DR   PRIDE; Q5F2E7; -.
DR   Ensembl; ENSMUST00000036677; ENSMUSP00000049412; ENSMUSG00000037857.
DR   Ensembl; ENSMUST00000100802; ENSMUSP00000098365; ENSMUSG00000037857.
DR   GeneID; 68564; -.
DR   KEGG; mmu:68564; -.
DR   UCSC; uc007khd.1; mouse.
DR   CTD; 68564; -.
DR   MGI; MGI:1915814; Nufip2.
DR   eggNOG; roNOG14606; -.
DR   GeneTree; ENSGT00440000038328; -.
DR   HOVERGEN; HBG065794; -.
DR   OMA; RPKGKHA; -.
DR   OrthoDB; EOG42JNRF; -.
DR   NextBio; 327462; -.
DR   ArrayExpress; Q5F2E7; -.
DR   Bgee; Q5F2E7; -.
DR   Genevestigator; Q5F2E7; -.
DR   GermOnline; ENSMUSG00000037857; Mus musculus.
DR   GO; GO:0005634; C:nucleus; ISS:HGNC.
DR   GO; GO:0042788; C:polysomal ribosome; ISS:HGNC.
DR   GO; GO:0003723; F:RNA binding; ISS:HGNC.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein.
FT   CHAIN         1    692       Nuclear fragile X mental retardation-
FT                                interacting protein 2.
FT                                /FTId=PRO_0000245522.
FT   COMPBIAS     12     61       His-rich.
FT   COMPBIAS    373    414       Ser-rich.
FT   MOD_RES      88     88       Phosphothreonine (By similarity).
FT   MOD_RES     113    113       Phosphoserine.
FT   MOD_RES     114    114       Phosphoserine (By similarity).
FT   MOD_RES     141    141       N6-acetyllysine (By similarity).
FT   MOD_RES     213    213       Phosphoserine.
FT   MOD_RES     215    215       Phosphoserine.
FT   MOD_RES     217    217       Phosphoserine (By similarity).
FT   MOD_RES     219    219       Phosphotyrosine (By similarity).
FT   MOD_RES     220    220       Phosphothreonine (By similarity).
FT   MOD_RES     221    221       Phosphothreonine (By similarity).
FT   MOD_RES     570    570       Phosphoserine (By similarity).
FT   MOD_RES     605    605       Phosphoserine (By similarity).
FT   MOD_RES     626    626       Phosphoserine.
FT   MOD_RES     628    628       Phosphothreonine (By similarity).
FT   MOD_RES     634    634       Phosphoserine (By similarity).
FT   MOD_RES     649    649       Phosphoserine.
FT   MOD_RES     689    689       Phosphoserine (By similarity).
FT   VAR_SEQ     676    692       DPKRIITYNEAMDSPDQ -> VFCLCVYMYTYVHHVMSLHG
FT                                RERTLDPLELALHWS (in isoform 2).
FT                                /FTId=VSP_019729.
FT   CONFLICT     52     52       Missing (in Ref. 2; BAE42015).
FT   CONFLICT     57     57       Q -> R (in Ref. 2; BAE42015).
SQ   SEQUENCE   692 AA;  75657 MW;  3E295AC111814564 CRC64;
     MEEKPGQPQP QHHHSHHHPH HHPQQQQQQQ SHHHHHYYFY NHSHNHHHHH HHQQPHQYLQ
     HGAEGSPKAQ PKPLKHEQKH TLQQHQETPK KKTGYGEING NAGEREISLK SLSSDEATNP
     ISRVLNGNQQ VVETSLKQTV KTSTFGKAGI KTKNFIQKNS MDKKNGKSYE NKSGETQAVD
     KTDTIAIPNG VITSSSGYIT NGYMSKGADN DGSGSESGYT TPKKRKARRN SAKGCENLNL
     VQDKIMQETS VPALKQGLET LKPDYSEQKG MRVDGSKPIW KYETGPGGTS RGKPAMGDVL
     RKSSDIKPGL SSKKFDDRPK GKHASAAASK EDSWTLFKPP PVFPVDNSSA KIVPKISYAS
     KVKENLNKTV QNSSVSPSSS SSSSSTGETQ TQSSSRLSQV PMSALKSVTS ASFSNGPVLA
     GTDGSVYPSG GQPLLTTAAN TLTPISTGTD SVLQDMSLAS AAVEQIKSSL FIYPSNMQTV
     LLSAQVDLPS QTDQQNLGDI FQNQWGLSFI NEPSAGPETV IGKSSDHKVM EVTFQGEYPA
     TLVSQGAEII PSGTEHPVFP KAYELEKRTS PQVLGHILKP GTTESGALSL DPSHIGDLQK
     ADTSSQGALV FLSKDYEIEN QNPLASPTNT LLGSAKEQRY QRGLERNDSW GSFDLRAAIV
     YHTKEMESIW NLQKQDPKRI ITYNEAMDSP DQ
//
ID   TAOK1_MOUSE             Reviewed;        1001 AA.
AC   Q5F2E8; Q69ZL2; Q8JZX2; Q91VG7;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Serine/threonine-protein kinase TAO1;
DE            EC=2.7.11.1;
DE   AltName: Full=Thousand and one amino acid protein 1;
GN   Name=Taok1; Synonyms=Kiaa1361;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 437-1001.
RC   STRAIN=FVB/N; TISSUE=Mammary gland, and Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 657-1001.
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-421, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-965, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Phosphorylates MKK3. Activates the p38 MAP kinase
CC       pathway through the specific activation of the upstream MKK3
CC       kinase (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Self-associates. Interacts with MKK3. Interacts with
CC       MAP3K7 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- PTM: Autophosphorylated (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH16522.1; Type=Erroneous initiation;
CC       Sequence=BAD32434.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL591136; CAI51877.1; -; Genomic_DNA.
DR   EMBL; BC016522; AAH16522.1; ALT_INIT; mRNA.
DR   EMBL; BC034906; AAH34906.1; -; mRNA.
DR   EMBL; AK173156; BAD32434.1; ALT_INIT; mRNA.
DR   IPI; IPI00126860; -.
DR   RefSeq; NP_659074.2; NM_144825.2.
DR   UniGene; Mm.454081; -.
DR   ProteinModelPortal; Q5F2E8; -.
DR   SMR; Q5F2E8; 12-365.
DR   STRING; Q5F2E8; -.
DR   PhosphoSite; Q5F2E8; -.
DR   PRIDE; Q5F2E8; -.
DR   Ensembl; ENSMUST00000017435; ENSMUSP00000017435; ENSMUSG00000017291.
DR   Ensembl; ENSMUST00000058496; ENSMUSP00000055470; ENSMUSG00000017291.
DR   GeneID; 216965; -.
DR   KEGG; mmu:216965; -.
DR   UCSC; uc007khc.1; mouse.
DR   CTD; 216965; -.
DR   MGI; MGI:1914490; Taok1.
DR   GeneTree; ENSGT00600000084021; -.
DR   HOGENOM; HBG382294; -.
DR   HOVERGEN; HBG088996; -.
DR   InParanoid; Q5F2E8; -.
DR   OMA; RASEPQS; -.
DR   OrthoDB; EOG41VK27; -.
DR   PhylomeDB; Q5F2E8; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 375476; -.
DR   ArrayExpress; Q5F2E8; -.
DR   Bgee; Q5F2E8; -.
DR   CleanEx; MM_TAOK1; -.
DR   Genevestigator; Q5F2E8; -.
DR   GermOnline; ENSMUSG00000017291; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Coiled coil; Cytoplasm; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1   1001       Serine/threonine-protein kinase TAO1.
FT                                /FTId=PRO_0000086729.
FT   DOMAIN       28    281       Protein kinase.
FT   NP_BIND      34     42       ATP (By similarity).
FT   COILED      458    651       Potential.
FT   COILED      754    877       Potential.
FT   COMPBIAS    330    334       Poly-Glu.
FT   ACT_SITE    151    151       Proton acceptor (By similarity).
FT   BINDING      57     57       ATP (By similarity).
FT   MOD_RES       9      9       Phosphoserine.
FT   MOD_RES      43     43       Phosphotyrosine (By similarity).
FT   MOD_RES     177    177       Phosphoserine (By similarity).
FT   MOD_RES     181    181       Phosphoserine (By similarity).
FT   MOD_RES     421    421       Phosphoserine.
FT   MOD_RES     445    445       Phosphoserine (By similarity).
FT   MOD_RES     480    480       Phosphothreonine (By similarity).
FT   MOD_RES     669    669       Phosphothreonine (By similarity).
FT   MOD_RES     958    958       Phosphoserine (By similarity).
FT   MOD_RES     959    959       Phosphoserine (By similarity).
FT   MOD_RES     965    965       Phosphoserine.
SQ   SEQUENCE   1001 AA;  116050 MW;  59DF437EAB8127C2 CRC64;
     MPSTNRAGSL KDPEIAELFF KEDPEKLFTD LREIGHGSFG AVYFARDVRT NEVVAIKKMS
     YSGKQSTEKW QDIIKEVKFL QRIKHPNSIE YKGCYLREHT AWLVMEYCLG SASDLLEVHK
     KPLQEVEIAA ITHGALQGLA YLHSHTMIHR DIKAGNILLT EPGQVKLADF GSASMASPAN
     SFVGTPYWMA PEVILAMDEG QYDGKVDVWS LGITCIELAE RKPPLFNMNA MSALYHIAQN
     ESPTLQSNEW SDYFRNFVDS CLQKIPQDRP TSEELLKHMF VLRERPETVL IDLIQRTKDA
     VRELDNLQYR KMKKLLFQEA HNGPAVEAQE EEEEQDHGVG RTGTVNSVGS NQSIPSMSIS
     ASSQSSSVNS LPDASDDKSE LDMMEGDHTV MSNSSVIHLK PEEENYQEEG DPRTRASDPQ
     SPPQVSRHKS HYRNREHFAT IRTASLVTRQ MQEHEQDSEL REQMSGYKRM RRQHQKQLMT
     LENKLKAEMD EHRLRLDKDL ETQRNNFAAE MEKLIKKHQA AMEKEAKVMA NEEKKFQQHI
     QAQQKKELNS FLESQKREYK LRKEQLKEEL NENQSTPKKE KQEWLSKQKE NIQHFQAEEE
     ANLLRRQRQY LELECRRFKR RMLLGRHNLE QDLVREELNK RQTQKDLEHA MLLRQHESMQ
     ELEFRHLNTI QKMRCELIRL QHQTELTNQL EYNKRREREL RRKHVMEVRQ QPKSLKSKEL
     QIKKQFQDTC KIQTRQYKAL RNHLLETTPK SEHKAVLKRL KEEQTRKLAI LAEQYDHSIN
     EMLSTQALRL DEAQEAECQV LKMQLQQELE LLNAYQSKIK MQAEAQHDRE LRELEQRVSL
     RRALLEQKIE EEMLALQNER TERIRSLLER QAREIEAFDS ESMRLGFSNM VLSNLSPEAF
     SHSYPGASSW SHNPTGGPGP HWGHPMGGTP QAWGHPMQGG PQPWGHPSGP MQGVPRGSSM
     GVRNSPQALR RTASGGRTEQ GMSRSTSVTS QISNGSHMSY T
//
ID   Q5F4S6_MOUSE            Unreviewed;      1699 AA.
AC   Q5F4S6;
DT   15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2005, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   SubName: Full=Transient receptor potential cation channel, subfamily M, member 3;
GN   Name=Trpm3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129/SvJ x C57BL/6J;
RX   PubMed=15824111; DOI=10.1074/jbc.M503092200;
RA   Oberwinkler J., Lis A., Giehl K., Flockerzi V., Philipp S.;
RT   "Alternative splicing switches the divalent cation selectivity of
RT   TRPM3 channels.";
RL   J. Biol. Chem. 280:22540-22548(2005).
CC   -----------------------------------------------------------------------
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DR   EMBL; AJ544536; CAD67496.1; -; mRNA.
DR   IPI; IPI00655008; -.
DR   RefSeq; NP_001030316.1; NM_001035239.2.
DR   RefSeq; NP_001030317.1; NM_001035240.2.
DR   RefSeq; NP_001030318.1; NM_001035241.2.
DR   RefSeq; NP_001030320.1; NM_001035243.2.
DR   UniGene; Mm.131943; -.
DR   UniGene; Mm.397699; -.
DR   UniGene; Mm.440339; -.
DR   STRING; Q5F4S6; -.
DR   Ensembl; ENSMUST00000074770; ENSMUSP00000074328; ENSMUSG00000052387.
DR   GeneID; 226025; -.
DR   KEGG; mmu:226025; -.
DR   UCSC; uc008gzn.1; mouse.
DR   CTD; 226025; -.
DR   MGI; MGI:2443101; Trpm3.
DR   HOVERGEN; HBG055663; -.
DR   OrthoDB; EOG47SSCV; -.
DR   PhylomeDB; Q5F4S6; -.
DR   NextBio; 377921; -.
DR   ArrayExpress; Q5F4S6; -.
DR   Bgee; Q5F4S6; -.
DR   Genevestigator; Q5F4S6; -.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005216; F:ion channel activity; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR005821; Ion_trans.
DR   Pfam; PF00520; Ion_trans; 1.
PE   2: Evidence at transcript level;
KW   Ion transport; Ionic channel; Membrane; Receptor; Transmembrane;
KW   Transport.
SQ   SEQUENCE   1699 AA;  193712 MW;  BF1409BD9F0F216F CRC64;
     MGKKWRDAGE LERGCSDRED SAESRRRSRS ASRGRFAESW KRLSSKQGST KRSGLPAQQT
     PAQKSWIERA FYKRECVHII PSTKDPHRCC CGRLIGQHVG LTPSISVLQN EKNESRLSRN
     DIQSEKWSIS KHTQLSPTDA FGTIEFQGGG HSNKAMYVRV SFDTKPDLLL HLMTKEWQLE
     LPKLLISVHG GLQNFELQPK LKQVFGKGLI KAAMTTGAWI FTGGVNTGVI RHVGDALKDH
     ASKSRGKICT IGIAPWGIVE NQEDLIGRDV VRPYQTMSNP MSKLTVLNSM HSHFILADNG
     TTGKYGAEVK LRRQLEKHIS LQKINTRIGQ GVPVVALIVE GGPNVISIVL EYLRDTPPVP
     VVVCDGSGRA SDILAFGHKY SEEGGLINES LRDQLLVTIQ KTFTYTRTQA QHLFIILMEC
     MKKKELITVF RMGSEGHQDI DLAILTALLK GANASAPDQL SLALAWNRVD IARSQIFIYG
     QQWPVGSLEQ AMLDALVLDR VDFVKLLIEN GVSMHRFLTI SRLEELYNTR HGPSNTLYHL
     VRDVKKGNLP PDYRISLIDI GLVIEYLMGG AYRCNYTRKR FRTLYHNLFG PKRDDIPLRR
     GRKTTKKREE EVDIDLDDPE INHFPFPFHE LMVWAVLMKR QKMALFFWQH GEEAMAKALV
     ACKLCKAMAH EASENDMVDD ISQELNHNSR DFGQLAVELL DQSYKQDEQL AMKLLTYELK
     NWSNATCLQL AVAAKHRDFI AHTCSQMLLT DMWMGRLRMR KNSGLKVILG ILLPPSILSL
     EFKNKDDMPY MTQAQEIHLQ EKEPEEPEKP TKEKDEEDME LTAMLGRSNG ESSRKKDEEE
     VQSRHRLIPV GRKIYEFYNA PIVKFWFYTL AYIGYLMLFN YIVLVKMERW PSTQEWIVIS
     YIFTLGIEKM REILMSEPGK LLQKVKVWLQ EYWNVTDLIA ILLFSVGMIL RLQDQPFRSD
     GRVIYCVNII YWYIRLLDIF GVNKYLGPYV MMIGKMMIDM MYFVIIMLVV LMSFGVARQA
     ILFPNEEPSW KLAKNIFYMP YWMIYGEVFA DQIDPPCGQN ETREDGKTIQ LPPCKTGAWI
     VPAIMACYLL VANILLVNLL IAVFNNTFFE VKSISNQVWK FQRYQLIMTF HERPVLPPPL
     IIFSHMTMIF QHVCCRWRKH ESDQDERDYG LKLFITDDEL KKVHDFEEQC IEEYFREKDD
     RFNSSNDERI RVTSERVENM SMRLEEVNER EHSMKASLQT VDIRLAQLED LIGRMATALE
     RLTGLERAES NKIRSRTSSD CTDAAYIVRQ SSFNSQEGNT FKLQESIDPA GEETISPTSP
     TLMPRMRSHS FYSVNVKDKG GIEKLESIFK ERSLSLHRAT SSHSVAKEPK APAAPANTLA
     IVPDSRRPSS CIDIYVSAMD ELHCDIEPLD NSMNILGLGE PSFSALAPST TPSSSAYATL
     APTDRPPSRS IDFEDLTSMD TRSFSSDYTH LPECQNPWDT DPPTYHTIER SKSSRYLATT
     PFLLEEAPIV KSHSFMFSPS RSYYANFGVP VKTAEYTSIT DCIDTRCVNA PQAIADRATF
     PGGLGDKVED LSCCHPEREA ELSHPSSDSE ENEARGQRAA NPISSQEAEN ADRTLSNNIT
     VPKIERANSY SAEEPNVPYA HTRKSFSISD KLDRQRNTAS LRNPFQRSKS SKPEGRGDSL
     SMRRLSRTSA FHSFESKHN
//
ID   UNKL_MOUSE              Reviewed;         727 AA.
AC   Q5FWH2; Q6RUT6; Q9DBK4;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=RING finger protein unkempt-like;
DE   AltName: Full=Putative E3 ubiquitin-protein ligase UNKL;
DE            EC=6.3.2.-;
GN   Name=Unkl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3).
RA   Brathwaite M., Waeltz P., Dudekula D., Nagaraja R.;
RT   "Genomic sequence analysis in the mouse t-complex region.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 26-727 (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY (ISOFORM 3).
RX   PubMed=20148946; DOI=10.1111/j.1742-4658.2010.07575.x;
RA   Lores P., Visvikis O., Luna R., Lemichez E., Gacon G.;
RT   "The SWI/SNF protein BAF60b is ubiquitinated through a signalling
RT   process involving Rac GTPase and the RING finger protein Unkempt.";
RL   FEBS J. 277:1453-1464(2010).
CC   -!- FUNCTION: May participate in a protein complex showing an E3
CC       ligase activity regulated by Rac1. Ubiquitination is directed
CC       towards itself and possibly other substrates, such as
CC       Baf60b/Smarcd2. Intrinsic E3 ligase activity has not been proven
CC       (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with the GTP-bound form of Rac1. Interacts with
CC       Baf60b/Smarcd2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Primarily localized in the cytoplasm but has the
CC       ability to shuttle between the nucleus and the cytoplasm (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=3;
CC         IsoId=Q5FWH2-3; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q5FWH2-1; Sequence=VSP_039444;
CC       Name=2;
CC         IsoId=Q5FWH2-2; Sequence=VSP_039445, VSP_039446, VSP_039447;
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- DOMAIN: Although this protein contains a RING domain, intrinsic E3
CC       ligase activity has not been proven (By similarity).
CC   -!- PTM: Ubiquitination is enhanced by activated Rac1. The presence of
CC       the RING finger domain is not essential for ubiquitination to
CC       occur (By similarity).
CC   -!- SIMILARITY: Belongs to the unkempt family.
CC   -!- SIMILARITY: Contains 4 C3H1-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK004898; BAB23653.1; -; mRNA.
DR   EMBL; AY491413; AAS21649.1; -; Genomic_DNA.
DR   EMBL; BC089378; AAH89378.1; -; mRNA.
DR   EMBL; BC059910; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00119815; -.
DR   IPI; IPI00421283; -.
DR   IPI; IPI00876101; -.
DR   RefSeq; NP_001183953.1; NM_001197024.1.
DR   RefSeq; NP_083065.1; NM_028789.3.
DR   UniGene; Mm.267353; -.
DR   ProteinModelPortal; Q5FWH2; -.
DR   SMR; Q5FWH2; 78-318, 681-727.
DR   Ensembl; ENSMUST00000015271; ENSMUSP00000015271; ENSMUSG00000015127.
DR   Ensembl; ENSMUST00000039734; ENSMUSP00000039670; ENSMUSG00000015127.
DR   Ensembl; ENSMUST00000115158; ENSMUSP00000110811; ENSMUSG00000015127.
DR   GeneID; 74154; -.
DR   KEGG; mmu:74154; -.
DR   CTD; 74154; -.
DR   MGI; MGI:1921404; Unkl.
DR   eggNOG; roNOG05427; -.
DR   GeneTree; ENSGT00390000012005; -.
DR   HOVERGEN; HBG094136; -.
DR   InParanoid; Q5FWH2; -.
DR   OrthoDB; EOG4QRH3P; -.
DR   ArrayExpress; Q5FWH2; -.
DR   Bgee; Q5FWH2; -.
DR   CleanEx; MM_UNKL; -.
DR   Genevestigator; Q5FWH2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR001841; Znf_RING.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00356; ZnF_C3H1; 4.
DR   PROSITE; PS50103; ZF_C3H1; 4.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Ligase; Metal-binding; Nucleus;
KW   Repeat; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    727       RING finger protein unkempt-like.
FT                                /FTId=PRO_0000278668.
FT   ZN_FING      75    104       C3H1-type 1.
FT   ZN_FING     115    145       C3H1-type 2.
FT   ZN_FING     243    277       C3H1-type 3.
FT   ZN_FING     285    313       C3H1-type 4.
FT   ZN_FING     686    721       RING-type.
FT   COMPBIAS      7     11       Poly-Ala.
FT   COMPBIAS     61     64       Poly-Arg.
FT   COMPBIAS    327    562       Ser-rich.
FT   VAR_SEQ       1    496       Missing (in isoform 1).
FT                                /FTId=VSP_039444.
FT   VAR_SEQ       1    412       Missing (in isoform 2).
FT                                /FTId=VSP_039445.
FT   VAR_SEQ     413    419       NTVGAVI -> MRPPTLP (in isoform 2).
FT                                /FTId=VSP_039446.
FT   VAR_SEQ     449    524       Missing (in isoform 2).
FT                                /FTId=VSP_039447.
FT   CONFLICT    629    629       K -> T (in Ref. 2; AAS21649).
SQ   SEQUENCE   727 AA;  79636 MW;  4A5A50A449BE9C8E CRC64;
     MPSVSKAAAA ALSGSPPQTE KPTHYRYLKE FRTEQCSLFL QHKCSQHRPF TCFHWHFLNQ
     RRRRPLRRRD GTFNYSPDIY CSKYDEATGL CPDGDECPYL HRTTGDTERK YHLRYYKTGT
     CIHETDARGH CVKNGLHCAF AHGPLDLRPP VCDIRELQAQ EALQNGQLSG GDGVPDLQPG
     VLASQAMIEK ILGEDPRWQD SNFVLGSYKT EQCPKPPRLC RQGYACPHYH NSRDRRRNPR
     RFQYRSTPCP SVKHGDEWGE PSRCDGGDSC QYCHSRTEQQ FHPEIYKSTK CNDMRQTGYC
     PRGPFCAFAH TEKSLAMVNE WSCRDLSSNS TSAYSSQPGS AKRKDSPSEG SQKATEDSKQ
     NHLAVFSVAH PLAHSISSSV ASSLASSTGS GSSSPTTLPT LPARALPLDP AGNTVGAVIG
     SALDLRLSDI NIASLDKDLE EQDLGLTGPR SLAGSAPVTI PGSLPRSPSL HSSSSLSTSP
     LSSLSQSLSG PLVSSAMTPP QQPPPLRSEP ATLGSAASSY SSLGLNGVPG SIWDFVSGSF
     SPSPSPILNS GPSASSSASP NSAELARVRR QLDEAKRKIR QWEESWQQVK QACDAWQREA
     QEAKERARVA DSDRQLALQR KEEVEAKVKQ LQEELEGLGL SSLPGLQSLG DISDIPLPKL
     HSLQSKLRLD LEAVDGVIFQ LRAKQCVACQ ERAHGTVLRP CQHRVLCEPC AASTPECPYC
     KGQPLPW
//
ID   RHG01_MOUSE             Reviewed;         439 AA.
AC   Q5FWK3; Q8C3X5; Q923D8;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Rho GTPase-activating protein 1;
DE   AltName: Full=Rho-type GTPase-activating protein 1;
GN   Name=Arhgap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-65, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
CC   -!- FUNCTION: GTPase activator for the Rho, Rac and Cdc42 proteins,
CC       converting them to the putatively inactive GDP-bound state. Cdc42
CC       seems to be the preferred substrate (By similarity).
CC   -!- SUBUNIT: Found in a complex with XPO7, EIF4A1, ARHGAP1, VPS26A,
CC       VPS29, VPS35 and SFN. Interacts with BNIPL (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Contains 1 CRAL-TRIO domain.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK084622; BAC39233.1; -; mRNA.
DR   EMBL; AL714023; CAM14522.1; -; Genomic_DNA.
DR   EMBL; AL691489; CAM14522.1; JOINED; Genomic_DNA.
DR   EMBL; AL691489; CAM16488.1; -; Genomic_DNA.
DR   EMBL; AL714023; CAM16488.1; JOINED; Genomic_DNA.
DR   EMBL; BC006592; AAH06592.1; -; mRNA.
DR   EMBL; BC089306; AAH89306.1; -; mRNA.
DR   IPI; IPI00404970; -.
DR   RefSeq; NP_001139374.1; NM_001145902.1.
DR   RefSeq; NP_666236.3; NM_146124.4.
DR   UniGene; Mm.22413; -.
DR   UniGene; Mm.463444; -.
DR   HSSP; Q07960; 1RGP.
DR   ProteinModelPortal; Q5FWK3; -.
DR   SMR; Q5FWK3; 233-431.
DR   STRING; Q5FWK3; -.
DR   PhosphoSite; Q5FWK3; -.
DR   PRIDE; Q5FWK3; -.
DR   Ensembl; ENSMUST00000070873; ENSMUSP00000067283; ENSMUSG00000027247.
DR   Ensembl; ENSMUST00000090614; ENSMUSP00000088105; ENSMUSG00000027247.
DR   Ensembl; ENSMUST00000111329; ENSMUSP00000106961; ENSMUSG00000027247.
DR   Ensembl; ENSMUST00000111330; ENSMUSP00000106962; ENSMUSG00000027247.
DR   Ensembl; ENSMUST00000111331; ENSMUSP00000106963; ENSMUSG00000027247.
DR   GeneID; 228359; -.
DR   KEGG; mmu:228359; -.
DR   UCSC; uc008kwi.1; mouse.
DR   CTD; 228359; -.
DR   MGI; MGI:2445003; Arhgap1.
DR   HOVERGEN; HBG054433; -.
DR   InParanoid; Q5FWK3; -.
DR   OrthoDB; EOG4XPQG3; -.
DR   PhylomeDB; Q5FWK3; -.
DR   NextBio; 378968; -.
DR   ArrayExpress; Q5FWK3; -.
DR   Bgee; Q5FWK3; -.
DR   CleanEx; MM_ARHGAP1; -.
DR   Genevestigator; Q5FWK3; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0001726; C:ruffle; IDA:MGI.
DR   GO; GO:0030675; F:Rac GTPase activator activity; IDA:MGI.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0043087; P:regulation of GTPase activity; IDA:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR001251; CRAL-bd_TRIO_C.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Gene3D; G3DSA:3.40.525.10; CRAL_bd_TRIO_C; 1.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF00650; CRAL_TRIO; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SUPFAM; SSF52087; CRAL_TRIO_C; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; GTPase activation; Phosphoprotein;
KW   SH3-binding.
FT   CHAIN         1    439       Rho GTPase-activating protein 1.
FT                                /FTId=PRO_0000323607.
FT   DOMAIN       63    218       CRAL-TRIO.
FT   DOMAIN      244    431       Rho-GAP.
FT   MOTIF       228    238       SH3-binding (By similarity).
FT   SITE        282    282       Involved in G-protein binding to GAPs (By
FT                                similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      51     51       Phosphoserine (By similarity).
FT   MOD_RES      65     65       Phosphotyrosine.
FT   MOD_RES      80     80       N6-acetyllysine (By similarity).
FT   MOD_RES     212    212       N6-acetyllysine (By similarity).
FT   CONFLICT    168    168       K -> Q (in Ref. 1; BAC39233).
FT   CONFLICT    257    257       D -> E (in Ref. 3; AAH06592).
SQ   SEQUENCE   439 AA;  50411 MW;  D8FD1E14C6BE32D3 CRC64;
     MDPLSELQDD LTLDDTSQAL NQLKLASIDE KNWPSDEMPD FPKSDDSKSS SPEPVTHLKW
     DDPYYDIARH QIVEVAGDDK YGRKIIVFSA CRMPPSHQLD HSKLLGYLKH TLDQYVESDY
     TLLYLHHGLT SDNKPSLSWL RDAYREFDRK YKKNIKALYI VHPTMFIKTL LILFKPLISF
     KFGRKIFYVN YLSELSEHVK LEQLGIPRQV LKYDDFLKST QKSPATAPKP MPPRPPLPNQ
     QFGVSLQHLQ EKSPGQDPIP IVLRETVAYL QAHALTTEGI FRRSANTQVV REVQQKYNMG
     LPVDFDQYNE LHLPAVILKT FLRELPEPLL TFDLYPHVVG FLNIDESQRV EVTQQVLQTL
     PEENYQVLHF LTAFLVQISA HCDQNKMTNT NLAVVFGPNL LWAKDAAITL KAINPINTFT
     KFLLDHQGEL FPSTDAQGV
//
ID   XKR7_MOUSE              Reviewed;         580 AA.
AC   Q5GH64; A2ATH3;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   08-MAR-2011, entry version 40.
DE   RecName: Full=XK-related protein 7;
GN   Name=Xkr7; Synonyms=Xrg7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Huang C.-H., Chen Y.;
RT   "A superfamily of XK-related genes (XRG) widely expressed in
RT   vertebrates and invertebrates.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the XK family.
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DR   EMBL; AY534253; AAT07102.1; -; mRNA.
DR   EMBL; AL928862; CAM27195.1; -; Genomic_DNA.
DR   IPI; IPI00354563; -.
DR   RefSeq; NP_001011732.1; NM_001011732.1.
DR   UniGene; Mm.376111; -.
DR   PhosphoSite; Q5GH64; -.
DR   PRIDE; Q5GH64; -.
DR   Ensembl; ENSMUST00000037235; ENSMUSP00000049346; ENSMUSG00000042631.
DR   GeneID; 228787; -.
DR   KEGG; mmu:228787; -.
DR   UCSC; uc008nha.1; mouse.
DR   CTD; 228787; -.
DR   MGI; MGI:3526711; Xkr7.
DR   GeneTree; ENSGT00530000062854; -.
DR   HOGENOM; HBG713827; -.
DR   HOVERGEN; HBG055841; -.
DR   InParanoid; Q5GH64; -.
DR   OMA; LVCVVAS; -.
DR   OrthoDB; EOG4BCDMR; -.
DR   PhylomeDB; Q5GH64; -.
DR   NextBio; 379140; -.
DR   Genevestigator; Q5GH64; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR018629; Transport_prot_XK.
DR   Pfam; PF09815; XK-related; 1.
DR   SMART; SM00015; IQ; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    580       XK-related protein 7.
FT                                /FTId=PRO_0000190789.
FT   TRANSMEM     59     79       Helical; (Potential).
FT   TRANSMEM     89    109       Helical; (Potential).
FT   TRANSMEM    260    280       Helical; (Potential).
FT   TRANSMEM    303    323       Helical; (Potential).
FT   TRANSMEM    326    346       Helical; (Potential).
FT   TRANSMEM    355    375       Helical; (Potential).
FT   TRANSMEM    384    404       Helical; (Potential).
FT   TRANSMEM    415    435       Helical; (Potential).
SQ   SEQUENCE   580 AA;  64302 MW;  F3291FABF4C5A826 CRC64;
     MAAKSDGAAA VAGPGPEGPA GADRGGAGGR GEAAAGIAGP GPVEAGCPGP RYELRDCCWV
     LCALLVFFSD GATDLWLAAS YYLQGQSTYF GLTLLFVLLP SLVVQLLSFR WFVYDYSEPA
     GTPGPAVSTK DSDIVGAAIS TKDSAVAFRT KEGSAELVPR PAPSSAGTYR RRCCRLCVWL
     LQTLVHLLQL GQVWRYLRAL YLGLQSRWRG ERLRRHFYWQ MLFESADVSM LRLLETFLRS
     APQLVLQLSL LVHRGREPEL LTALSISASL VSLAWTLASY QKVLRDSRDD KRPLSYKGAV
     VQVLWHLFTI AARTLAFALF ASVYKLYFGI FIVAHWCIMT FWVIQGETDF CMSKWEEIIY
     NMVVGIIYIF CWFNVKEGRS RRRVTLYYCI VLLENAALTG FWYSSRNFST DFYSLILVCV
     VASSFALGIF FMCVYYCLLH PNGPMLGPQA PGCIFPEAPG PCGPPADAIT SPPRSLPRTT
     GTERDGVAVG GERAGTPTLP VFQVRPGLPP TPVARPLRTE GPVIRIDLPR KKYPAWDAHF
     IDRRLRKTIL ALEYSSPATP RLQYRSMGTS QELLEYETTV
//
ID   XKR4_MOUSE              Reviewed;         647 AA.
AC   Q5GH67;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=XK-related protein 4;
GN   Name=Xkr4; Synonyms=Xrg4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Huang C.-H., Chen Y.;
RT   "A superfamily of XK-related genes (XRG) widely expressed in
RT   vertebrates and invertebrates.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the XK family.
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DR   EMBL; AY534250; AAT07099.1; -; mRNA.
DR   IPI; IPI00357068; -.
DR   RefSeq; NP_001011874.1; NM_001011874.1.
DR   UniGene; Mm.169928; -.
DR   UniGene; Mm.454496; -.
DR   ProteinModelPortal; Q5GH67; -.
DR   PhosphoSite; Q5GH67; -.
DR   PRIDE; Q5GH67; -.
DR   Ensembl; ENSMUST00000070533; ENSMUSP00000070648; ENSMUSG00000051951.
DR   GeneID; 497097; -.
DR   KEGG; mmu:497097; -.
DR   NMPDR; fig|10090.3.peg.1; -.
DR   UCSC; uc007aeu.1; mouse.
DR   CTD; 497097; -.
DR   MGI; MGI:3528744; Xkr4.
DR   GeneTree; ENSGT00530000062854; -.
DR   HOGENOM; HBG713827; -.
DR   HOVERGEN; HBG055841; -.
DR   InParanoid; Q5GH67; -.
DR   OMA; VGTDVWL; -.
DR   OrthoDB; EOG4XPQFM; -.
DR   PhylomeDB; Q5GH67; -.
DR   NextBio; 411780; -.
DR   ArrayExpress; Q5GH67; -.
DR   Bgee; Q5GH67; -.
DR   Genevestigator; Q5GH67; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR018629; Transport_prot_XK.
DR   Pfam; PF09815; XK-related; 1.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    647       XK-related protein 4.
FT                                /FTId=PRO_0000190778.
FT   TRANSMEM    112    132       Helical; (Potential).
FT   TRANSMEM    142    162       Helical; (Potential).
FT   TRANSMEM    245    265       Helical; (Potential).
FT   TRANSMEM    303    323       Helical; (Potential).
FT   TRANSMEM    328    348       Helical; (Potential).
FT   TRANSMEM    362    382       Helical; (Potential).
FT   TRANSMEM    393    415       Helical; (Potential).
FT   TRANSMEM    425    445       Helical; (Potential).
FT   TRANSMEM    454    474       Helical; (Potential).
FT   TRANSMEM    484    504       Helical; (Potential).
FT   MOD_RES      87     87       Phosphoserine.
FT   MOD_RES     645    645       Phosphothreonine (By similarity).
FT   MOD_RES     646    646       Phosphothreonine (By similarity).
SQ   SEQUENCE   647 AA;  71503 MW;  1E3E0D073E983231 CRC64;
     MAAKSDGRLK MKKSSDVAFT PLQNSDNSGS VQGLAPGLPS GSGAEDTEAA GGGCCPDGGG
     CSRCCCCCAG SGGSAGSGGS GGGGRGSGAG SAALCLRLGR EQRRYSLWDC LWILAAVAVY
     FADVGTDIWL AVDYYLRGQR WWFGLTLFFV VLGSLSVQVF SFRWFVHDFS TEDSSTTTTS
     SCQQPGADCK TVVSSGSAAG EGEVRPSTPQ RQASNASKSN IAATNSGSNS NGATRTSGKH
     RSASCSFCIW LLQSLIHILQ LGQIWRYLHT IYLGIRSRQS GESGRWRFYW KMVYEYADVS
     MLHLLATFLE SAPQLVLQLC IIVQTHSLQA LQGFTAAASL VSLAWALASY QKALRDSRDD
     KKPISYMAVI IQFCWHFFTI AARVITFALF ASVFQLYFGI FIVLHWCIMT FWIVHCETEF
     CITKWEEIVF DMVVGIIYIF SWFNVKEGRT RCRLFIYYFV ILLENTALSA LWYLYKAPQI
     ADAFAIPALC VVFSSFLTGV VFMLMYYAFF HPNGPRFGQS PSCACDDPAT AFSLPPEVAT
     STLRSISNNR SVASDRDQKF AERDGCVPVF QVRPTAPPTP SSRPPRIEES VIKIDLFRNR
     YPAWERHVLD RSLRKAILAF ECSPSPPRLQ YKDDALIQER LEYETTL
//
ID   VP13A_MOUSE             Reviewed;        3166 AA.
AC   Q5H8C4; Q3UQG7; Q3UX03; Q5DU08; Q80YV7; Q8C722;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   08-MAR-2011, entry version 44.
DE   RecName: Full=Vacuolar protein sorting-associated protein 13A;
DE   AltName: Full=Chorea-acanthocytosis protein homolog;
DE   AltName: Full=Chorein;
GN   Name=Vps13a; Synonyms=Chac, Kiaa0986;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DISRUPTION PHENOTYPE.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15686477; DOI=10.1111/j.1471-4159.2004.02924.x;
RA   Tomemori Y., Ichiba M., Kusumoto A., Mizuno E., Sato D., Muroya S.,
RA   Nakamura M., Kawaguchi H., Yoshida H., Ueno S., Nakao K., Nakamura K.,
RA   Aiba A., Katsuki M., Sano A.;
RT   "A gene-targeted mouse model for chorea-acanthocytosis.";
RL   J. Neurochem. 92:759-766(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-368; 875-1696 AND
RP   1896-2816.
RC   STRAIN=C57BL/6J; TISSUE=Egg, Kidney, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2141-3166 (ISOFORM 2).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2477-3166 (ISOFORM 1).
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2233 AND THR-2234, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: May play a role in the control of protein cycling
CC       through the trans-Golgi network to early and late endosomes,
CC       lysosomes and plasma membrane (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5H8C4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5H8C4-2; Sequence=VSP_052241, VSP_052242;
CC   -!- DISRUPTION PHENOTYPE: Mice show defects in motor coordination,
CC       social investigation, erythrocyte morphology as well as size and
CC       morphology of the striatum. Provides a mouse model for chorea-
CC       acanthocytosis (CHAC) with a mild phenotype and late adult onset.
CC   -!- SIMILARITY: Belongs to the VPS13 family.
CC   -!- SIMILARITY: Contains 6 TPR repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE22761.1; Type=Miscellaneous discrepancy; Note=Intron retention;
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DR   EMBL; AB115421; BAD89296.1; -; mRNA.
DR   EMBL; AK052697; BAC35101.1; -; mRNA.
DR   EMBL; AK135983; BAE22761.1; ALT_SEQ; mRNA.
DR   EMBL; AK142462; BAE25075.1; -; mRNA.
DR   EMBL; AK220362; BAD90423.1; -; mRNA.
DR   EMBL; BC050055; AAH50055.1; -; mRNA.
DR   IPI; IPI00420394; -.
DR   IPI; IPI00762748; -.
DR   RefSeq; NP_766616.2; NM_173028.3.
DR   UniGene; Mm.211963; -.
DR   STRING; Q5H8C4; -.
DR   PhosphoSite; Q5H8C4; -.
DR   PRIDE; Q5H8C4; -.
DR   Ensembl; ENSMUST00000068156; ENSMUSP00000068716; ENSMUSG00000046230.
DR   Ensembl; ENSMUST00000112873; ENSMUSP00000108494; ENSMUSG00000046230.
DR   GeneID; 271564; -.
DR   KEGG; mmu:271564; -.
DR   UCSC; uc008gwv.1; mouse.
DR   CTD; 271564; -.
DR   MGI; MGI:2444304; Vps13a.
DR   HOGENOM; HBG402793; -.
DR   HOVERGEN; HBG079736; -.
DR   InParanoid; Q5H8C4; -.
DR   OMA; LPKTFEA; -.
DR   OrthoDB; EOG45QHC8; -.
DR   PhylomeDB; Q5H8C4; -.
DR   NextBio; 393478; -.
DR   ArrayExpress; Q5H8C4; -.
DR   Bgee; Q5H8C4; -.
DR   CleanEx; MM_VPS13A; -.
DR   Genevestigator; Q5H8C4; -.
DR   GermOnline; ENSMUSG00000046230; Mus musculus.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0007399; P:nervous system development; IMP:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0035176; P:social behavior; IMP:MGI.
DR   InterPro; IPR015412; Autophagy-rel_C.
DR   InterPro; IPR009543; VPSAP.
DR   Pfam; PF09333; ATG_C; 1.
DR   Pfam; PF06650; DUF1162; 1.
DR   PROSITE; PS50005; TPR; FALSE_NEG.
DR   PROSITE; PS50293; TPR_REGION; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein; Protein transport; Repeat;
KW   TPR repeat; Transport.
FT   CHAIN         1   3166       Vacuolar protein sorting-associated
FT                                protein 13A.
FT                                /FTId=PRO_0000262948.
FT   REPEAT      212    245       TPR 1.
FT   REPEAT      373    406       TPR 2.
FT   REPEAT     1806   1840       TPR 3.
FT   REPEAT     1999   2034       TPR 4.
FT   REPEAT     2716   2750       TPR 5.
FT   REPEAT     2852   2890       TPR 6.
FT   MOD_RES    2233   2233       Phosphotyrosine.
FT   MOD_RES    2234   2234       Phosphothreonine.
FT   VAR_SEQ    3056   3061       VMENGR -> ASKSLI (in isoform 2).
FT                                /FTId=VSP_052241.
FT   VAR_SEQ    3062   3166       Missing (in isoform 2).
FT                                /FTId=VSP_052242.
SQ   SEQUENCE   3166 AA;  359401 MW;  68EFBB87EF7833B0 CRC64;
     MVFESVVVEV LNRFLGDYVV NLDESQLSLG IWKGAVALKN LVIKENALHE LDVPFKVKVG
     HIGSLKLKIP WKNLYTQPVE AVLEEIFLLI VPSSRIQYDP IKEEKQLMET KQQELKRIEK
     AKQKVFDKEK PREEKQDTFT EKLVTQIIQN LQVQISSIHI RYEDDITNGD KPLSFGISLQ
     NISLQTTDQY WIPCLHDNTE KLVRKLIRLD NLFAYWNVNS EMFYLNDYDE SLKALKNGIV
     NENIVPEGYD FVFRPISASA KLQMNRRSDF DFSDPKINLA VDLHTIAIEF NKPQYFSLME
     LLESIDMMTQ NQPYRKFKPS VPLHLHAKEW WAYAIHSILE VNVCPSLRMW SWEHIRNHRY
     KMKRYREFYK KKLTSKKPSP EILMSLEELE KTLDVFNITI ARQQAEVEAK KAGYKIYKEG
     VKDPEDNAGW FGWLWTWSES NANQQQDVKP GILEEMLTPE EKSLLYEAIG YSETAVDPTL
     PKTFEALKFF VHLKSMSIVL RENHQKPELL NVVVEGLSTS VVQRPGAQAI KFETKIDSFH
     ITGLPDDFKK PHLLSSLDDT SLLQITFEIN PLNETVAQRC TIEAEPLEII YDARTVNSIV
     EFFRPPKDVH LAQLTSVTLT KLEEFRAKTA TGLLYVIETQ KVLDLRINVK ASYVIVPQYG
     NFSPTSNLLL LDLGHLKVSS KRRSLLPDVR PSEASLEDIM HRAYDSFDIQ LTSIQLLYSR
     VGDNWKEARK LNVSTQHILI PMHVNVELSK AMVFMDIKMP KFKISGKLPL VSLRISDKKL
     QGIMELLGSI PKPEPVTDVS APARSFQIQA SALPVSHISQ KLIPLLEQPV TEDDSEEEFF
     DAPCSPLEEC PQVSCRDKCT RQKKLQKKDC VMNLIQLRMR FEVAEVSIQF YHLVGDCELP
     VLEMGALGLG TEAEFRTFDL KGSAFLKELW LKCPEYLDEN KKPVYLITTL DNTMEDLLTL
     EFMKVEKNAP NLNSTYNNVL QLIKVNFSSL DIHLHTEALL NTMNYLNNIL PELREKSASV
     SAAEPEDKGD IIKKLALKLP TNEDIITLQL LAELSCLQIF IQDQKQNISE IKIEGLDSEM
     IMKPLVTEIN AKLRNIIVLD SDKMAIYKKA LYITGKEVFS FKMISYMDAT AGYAYTDMSV
     VDIRVHLTVG CIEVVFITKF LYSILAFIDN FQAVKDALAE ATVQAAEMAA DGVKELARKS
     SRFALDVNIK APVVLIPQSP VSQNVFVADF GLITMKNIFV TVTETQSNIP PVIDLITIKL
     SKMRLYRSQF RNDTYQEVLD LLLPLNLEVI VERNLSWEWY KEVPCFNIKA QLKPMEFILS
     QEDLTTVFQT LHGNIWYGQD LSAPSSANKD PETMTSGVTS PPDHSPATVV TAAVVEVHPQ
     ASQAHTMLNV SFQTDYLTMA LYSPGPDEAS FTDVRDPSLE LAEFKLENII SSLKIYTDDS
     TVFSFSVKNC ILDDKRSHVM KATPRMIGLT VGFDKKDMVD IKYRKIKTFV VTDAVVQEMY
     VCASVEFLMT VAHIFFDAYM TSTALETSVQ TRTTREAPAQ ELGKWEMNIL IKNPEIVFVA
     DMTRNDAPAL VITTQCEICC KGEPTSNTVT AAIKDLQVRA CPFLPVKRKG KVTTVLQPCD
     LFYQATQLGR DPQMIDISVK SLTLKVSPVI INTIITITSA LYTTKETVPE ENTSNIAHLW
     DKKDTKNLKM WFLEESNESE KVVPTNEVMP GGETLNLRID SIFIVLEAGI GHRTVPMLLA
     KACFSGESKN WLSLINLHCH LELEVHYYNE MFGVWEPLLE PLEIDQTDDF RPWNLGIKMK
     KKAKEAIVES DSEAENYKVP EYKTAISFYS RDQLNITLSK CGLVMLNNLV EAFTEAATGS
     SSVFLRDLAP FMIFNSLGLT VSVSPSDSFS VLNVPLAKSY ELKNDESLSM DYVRTKDNDH
     FNAMTSLSSK LFFILLTPAN HSVADKIPLT KVGRRLYTVR HRESGVERSI ICQIDTVEGS
     KKVTIRSPVQ IKNHFSIPIS VFEGDTLLGI ASPENEFNIP LASYRSSLSL VPEDQDYQLC
     EGIDFEEIIK YDGQLLKKKC RSTNPSKKSF VINIVPEKDN LASLSVYSED GWDLPYVLHL
     WPPILIRNLL PYKVAYYIEG IENTVVTLSE GHSSQIYNVE MDQAKLHLKL LDYLNHDWKS
     EFYIRSSQQD INFINFTCLT EMEKSDLDIA IHMTYNTGQT VVAFHSPYWM VNKTNRMLQY
     KADGIHRKHP PNYTKPVLFS FQPNHFFNNN KVQLMVTDSE LSDQFSIDTV GSHGAIRCKG
     LKMEYQVGVT INLSSFNITR IVTFIPFYMI KNKSKYHISV AEEGSDKWLS LDLEQSIPFW
     PENASNILLI QVERSEDPPK RIYFNKQDNC ILLRLNNELG GIIAEVNLAE HSTVITFSDY
     HDGAATFLLI NHTKSDPVQY NQSSLGEIED SLPPGKAVYY TWADPVGSRK LKWSCGQSYG
     EVTHKDDMMT PISVGKKTIY LVSFFEGLQR IILFTEDPRV FKVTYESEKA ELAELEVVLA
     LQDVGISLVN NYTKQEVAYI GITSSDVVWE AKPKKKARWK PMSVKHTEKL EKEFREYTEA
     SPLEDKVVEL DNIPVRLTPS GNDMKILQPH VIPVRRNYLP ALKVEYNTSA HQSSFRIQIY
     RIQIQNQIHG AIFPFVFYPI KPPRSVTMDS APKPFTDVSI VMRSAGHSQI SRIKYFKVLI
     QEMDLSLDLG FVYALADLVT KAEVTEKTEV EHFHKDVEAF EQEYEVVSSV DQSQVNLFEY
     FHISPIKLHL SVSLSSGRDE AKDSEQHGGL IPVHSLNLLL KSIGATLTDV QDVVFKLAFF
     ELNYQFHTTS ELQSEVIRHY SKQAIKQMYV LILGLDVLGN PFGLIREFSE GVEAFFYEPY
     QGAIQGPEEF VEGMALGLKA LVGGAVGGLA GAASKITSAM AKGVAAMTMD EDYQQKRREA
     MNKQPAGLRE GITRGGKGLV SGFVSGITGI VTKPIKGAQK EGAAGFFKGV GKGLVGAVTR
     PTGGIIDMAS STFQGIKRAT ETSEVESLRP PRFFNEDGVI RPYRLRDGSG NQMLQVMENG
     RFAKYKYFTH VMINKTDMFM ITRRGVLFVT KGTFGQLTCE WQYTFDEFTK EPFIVHGRRL
     RIEAKERVKS VFHAKEFGKI VNFKTPEDAR WILTKLEEAR EPSPRL
//
ID   TAF3_MOUSE              Reviewed;         932 AA.
AC   Q5HZG4; Q3U490; Q3UWX2; Q8BIU8; Q99JH4;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   30-NOV-2010, entry version 59.
DE   RecName: Full=Transcription initiation factor TFIID subunit 3;
DE   AltName: Full=140 kDa TATA box-binding protein-associated factor;
DE   AltName: Full=TBP-associated factor 3;
DE   AltName: Full=Transcription initiation factor TFIID 140 kDa subunit;
DE            Short=TAF(II)140;
DE            Short=TAF140;
DE            Short=TAFII-140;
DE            Short=TAFII140;
GN   Name=Taf3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH TAF10.
RC   TISSUE=Embryonic carcinoma;
RX   MEDLINE=21332116; PubMed=11438666;
RX   DOI=10.1128/MCB.21.15.5109-5121.2001;
RA   Gangloff Y.G., Pointud J.-C., Thuault S., Carre L., Romier C.,
RA   Muratoglu S., Brand M., Tora L., Couderc J.-L., Davidson I.;
RT   "The TFIID components human TAFII140 and Drosophila BIP2 (TAFII155)
RT   are novel metazoan homologues of yeast TAFII47 containing a histone
RT   fold and a PHD finger.";
RL   Mol. Cell. Biol. 21:5109-5121(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, Egg, and Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Head;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TBPL2.
RX   PubMed=17704303; DOI=10.1101/gad.1583407;
RA   Deato M.D.E., Tjian R.;
RT   "Switching of the core transcription machinery during myogenesis.";
RL   Genes Dev. 21:2137-2149(2007).
CC   -!- FUNCTION: Transcription factor TFIID is one of the general factors
CC       required for accurate and regulated initiation by RNA polymerase
CC       II. TFIID is a multimeric protein complex that plays a central
CC       role in mediating promoter responses to various activators and
CC       repressors. Required in complex with TBPL2 for the differentiation
CC       of myoblasts into myocytes. The complex replaces TFIID at specific
CC       promoters at an early stage in the differentiation process.
CC   -!- SUBUNIT: Belongs to the TFIID complex which is composed of TATA
CC       binding protein (TBP) and a number of TBP-associated factors
CC       (TAFs). Interacts with TAF10 via histone fold. Interacts with
CC       TAF13, TBP, SAP130 and GCN5L2 (By similarity). Interacts with
CC       TBPL2.
CC   -!- INTERACTION:
CC       Q6SJ95:Tbpl2; NbExp=2; IntAct=EBI-1561080, EBI-1571412;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5HZG4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5HZG4-2; Sequence=VSP_019736, VSP_019737;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the TAF3 family.
CC   -!- SIMILARITY: Contains 1 PHD-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH89030.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AJ292189; CAC34476.1; -; mRNA.
DR   EMBL; AK084574; BAC39218.1; -; mRNA.
DR   EMBL; AK136045; BAE22792.1; -; mRNA.
DR   EMBL; AK154372; BAE32543.1; -; mRNA.
DR   EMBL; BC089030; AAH89030.1; ALT_INIT; mRNA.
DR   IPI; IPI00756399; -.
DR   IPI; IPI00757994; -.
DR   RefSeq; NP_082024.2; NM_027748.3.
DR   UniGene; Mm.86343; -.
DR   PDB; 2K16; NMR; -; A=857-924.
DR   PDB; 2K17; NMR; -; A=857-924.
DR   PDBsum; 2K16; -.
DR   PDBsum; 2K17; -.
DR   ProteinModelPortal; Q5HZG4; -.
DR   SMR; Q5HZG4; 857-924.
DR   DIP; DIP-46032N; -.
DR   IntAct; Q5HZG4; 20.
DR   STRING; Q5HZG4; -.
DR   PhosphoSite; Q5HZG4; -.
DR   PRIDE; Q5HZG4; -.
DR   Ensembl; ENSMUST00000026888; ENSMUSP00000026888; ENSMUSG00000025782.
DR   GeneID; 209361; -.
DR   KEGG; mmu:209361; -.
DR   UCSC; uc008ihk.1; mouse.
DR   UCSC; uc008ihl.1; mouse.
DR   CTD; 209361; -.
DR   MGI; MGI:2388097; Taf3.
DR   HOGENOM; HBG713530; -.
DR   HOVERGEN; HBG083188; -.
DR   InParanoid; Q5HZG4; -.
DR   OMA; NFPYISS; -.
DR   PhylomeDB; Q5HZG4; -.
DR   NextBio; 372647; -.
DR   ArrayExpress; Q5HZG4; -.
DR   Bgee; Q5HZG4; -.
DR   Genevestigator; Q5HZG4; -.
DR   GermOnline; ENSMUSG00000025782; Mus musculus.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003702; F:RNA polymerase II transcription factor activity; TAS:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:MGI.
DR   InterPro; IPR006565; BTP.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF07524; Bromo_TP; 1.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00576; BTP; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Metal-binding;
KW   Nucleus; Phosphoprotein; Transcription; Transcription regulation;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    932       Transcription initiation factor TFIID
FT                                subunit 3.
FT                                /FTId=PRO_0000245529.
FT   ZN_FING     867    917       PHD-type.
FT   COMPBIAS    136    141       Poly-Glu.
FT   COMPBIAS    163    168       Poly-Glu.
FT   COMPBIAS    221    367       Pro-rich.
FT   COMPBIAS    508    749       Lys-rich.
FT   COMPBIAS    782    834       Pro-rich.
FT   MOD_RES     183    183       Phosphoserine (By similarity).
FT   MOD_RES     199    199       Phosphoserine (By similarity).
FT   MOD_RES     229    229       Phosphoserine (By similarity).
FT   MOD_RES     243    243       Phosphoserine (By similarity).
FT   MOD_RES     266    266       N6-acetyllysine (By similarity).
FT   MOD_RES     267    267       Phosphoserine (By similarity).
FT   MOD_RES     291    291       Phosphoserine (By similarity).
FT   MOD_RES     297    297       Phosphoserine (By similarity).
FT   MOD_RES     301    301       Phosphoserine (By similarity).
FT   MOD_RES     365    365       Phosphothreonine (By similarity).
FT   MOD_RES     411    411       Phosphoserine (By similarity).
FT   MOD_RES     412    412       Phosphoserine (By similarity).
FT   MOD_RES     414    414       Phosphoserine (By similarity).
FT   MOD_RES     416    416       Phosphoserine (By similarity).
FT   MOD_RES     502    502       Phosphothreonine (By similarity).
FT   MOD_RES     779    779       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1    741       Missing (in isoform 2).
FT                                /FTId=VSP_019736.
FT   VAR_SEQ     742    747       KHKHEK -> MYKFPQ (in isoform 2).
FT                                /FTId=VSP_019737.
FT   CONFLICT    545    545       R -> G (in Ref. 2; BAE32543).
FT   CONFLICT    721    721       K -> E (in Ref. 2; BAE22792).
FT   STRAND      857    860
FT   STRAND      862    864
FT   STRAND      866    868
FT   TURN        871    873
FT   STRAND      882    884
FT   STRAND      886    893
FT   HELIX       894    897
FT   STRAND      905    907
FT   TURN        912    914
FT   HELIX       915    918
SQ   SEQUENCE   932 AA;  105115 MW;  8061D8E599A650EE CRC64;
     MCESYSRSLL RVSVAQICQA LGWDSVQLSA CHLLTDVLQR YLQQLGRGCH RYSELYGRTD
     PILDDVGEAF QLMGVNLHEL EDYIHNIEPV TFPHQIPSFP VSKNNVLQFP QPGSKDAEER
     KDYIPDYLPP IVSSQEEEEE EQVPTDGGTS AEAMQVPLEE DDEMEEEEVI NDENFLGKRP
     LDSPEVEEMP SMKRPRLLST KGDSLDVVLL EAREPLSSIN PQKTPPVLSP VRVQDRADLA
     PPSPQPPMLA PFAKSQLPIA KPLETKSFTP KTKTKASSPG QKTKSPKAAL SPARLGSPIR
     SPKTIPKEKK SPGRSKSPKS PKSPKIVAHV PQTPVRPETP NRTPSAMVVE KTVKETIPVM
     KPTQTPPEVV KLNIEMQPKK PVVTDKTIDD SIDAVIARAC AEREPDPFEF SSGSESEGDT
     FTSPKRISGS ECATPKASTS SNNFTKSLAT PLPLSSGTSS SDNSWTMDAS IDEVVRKAKL
     GAPSNMPPTF PYISSPSISP PTPEPLHKGY EEKAKLPSSV DVKKKLKKEL KTKLKKKEKQ
     RDRERERERN KERSKEKDKM REREKEKEAG KELKYPWREL MKDEDSDPYK FKIKEFEDID
     AAKVRLKDGI VRREREKHKD KKKDRERSKR EKDKRERERL KEKNREDKIK APPTQLVLPP
     KEMALPLFSP SAVRVPAMLP AFSPMLPEKL FEEKEKPKEK ERKKDKKEKK KKKEKEKEKE
     KKEREREKER REREKREKEK EKHKHEKIKV EPVIPAPSPV IPRLTLRVGA GQDKIVISKV
     VPAPEAKPAP SLNRPKTPPP APVPIPVRVS PTPLQPPLLT QAAVCPALMP SPAPALSGIG
     SAKAPVRSVV TETVSTYVIR DEWGNQIWIC PGCNKPDDGS PMIGCDDCDD WYHWPCVGIM
     AAPPEEMQWF CPKCANKIKK DKKHKKRKHR AH
//
ID   C2C4C_MOUSE             Reviewed;         419 AA.
AC   Q5HZI2; Q8CDK0;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=C2 calcium-dependent domain-containing protein 4C;
DE   AltName: Full=Nuclear-localized factor 3;
DE   AltName: Full=Protein FAM148C;
GN   Name=C2cd4cC2CD4 family; Synonyms=Fam148c, Nlf3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the C2CD4 family.
CC   -!- SIMILARITY: Contains 1 C2 domain.
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DR   EMBL; AK029946; BAC26694.1; -; mRNA.
DR   EMBL; BC089008; AAH89008.1; -; mRNA.
DR   IPI; IPI00318140; -.
DR   RefSeq; NP_001162095.1; NM_001168624.1.
DR   RefSeq; NP_941016.2; NM_198614.3.
DR   UniGene; Mm.334207; -.
DR   ProteinModelPortal; Q5HZI2; -.
DR   SMR; Q5HZI2; 304-417.
DR   PhosphoSite; Q5HZI2; -.
DR   PRIDE; Q5HZI2; -.
DR   Ensembl; ENSMUST00000059699; ENSMUSP00000059433; ENSMUSG00000045912.
DR   GeneID; 237397; -.
DR   KEGG; mmu:237397; -.
DR   NMPDR; fig|10090.3.peg.13979; -.
DR   UCSC; uc007fzb.1; mouse.
DR   CTD; 237397; -.
DR   MGI; MGI:2685084; C2cd4c.
DR   eggNOG; maNOG07700; -.
DR   GeneTree; ENSGT00530000063888; -.
DR   HOGENOM; HBG445403; -.
DR   HOVERGEN; HBG056001; -.
DR   InParanoid; Q5HZI2; -.
DR   OMA; ATRHVIQ; -.
DR   OrthoDB; EOG42NJ10; -.
DR   PhylomeDB; Q5HZI2; -.
DR   NextBio; 383336; -.
DR   ArrayExpress; Q5HZI2; -.
DR   Bgee; Q5HZI2; -.
DR   Genevestigator; Q5HZI2; -.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   Pfam; PF00168; C2; 1.
DR   SMART; SM00239; C2; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   PROSITE; PS50004; C2; 1.
PE   2: Evidence at transcript level;
FT   CHAIN         1    419       C2 calcium-dependent domain-containing
FT                                protein 4C.
FT                                /FTId=PRO_0000293735.
FT   DOMAIN      305    409       C2.
FT   CONFLICT    120    120       E -> D (in Ref. 1; BAC26694).
FT   CONFLICT    139    139       P -> H (in Ref. 1; BAC26694).
SQ   SEQUENCE   419 AA;  44614 MW;  DF5C310C69A52920 CRC64;
     MRKTNMWFLE RLRGSGENGA SRGEAGDKSS KGPLYSNVLT PDKIPDFFIP PKLPSGPTEA
     EGQADLGPST SEQNLASPGP RRAPRSPRLP AKLASESRSL LKAATRHVIQ IESAEDWTAE
     EATNADPQAQ GAMSLPSVPK AQTSYGFATL AESPHTRRKE SLFHSEHGAL AQVGSPGAGR
     RRAGAKGNGG DGGSREVGGA LMSPSRYFSG GESDTGSSAE SSPFGSPLLS RSVSLLKGFA
     QDSQAKVSQL KQSVGRHGSL SADDSTPDTS PGVRRRLSRR ATPEPGPESG QAPRGEHTVK
     MGTRGSVRLL AEYEAAQARL RVRLLAAEGL YDRPCDARSI NCCVGLCLVP GKLQKQRSTI
     IKNSRHPIFN EDFFFDGLGP ASVRKLALRI KVVNKGSSLK RDTLLGEEEL PLTSLLPFL
//
ID   Q5HZI5_MOUSE            Unreviewed;      1157 AA.
AC   Q5HZI5;
DT   15-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2005, sequence version 1.
DT   08-FEB-2011, entry version 48.
DE   SubName: Full=Protocadherin 17;
GN   Name=Pcdh17;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 6 cadherin domains.
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DR   EMBL; BC089004; AAH89004.1; -; mRNA.
DR   IPI; IPI00356667; -.
DR   RefSeq; NP_001013775.2; NM_001013753.2.
DR   UniGene; Mm.153643; -.
DR   ProteinModelPortal; Q5HZI5; -.
DR   SMR; Q5HZI5; 18-139, 141-579.
DR   STRING; Q5HZI5; -.
DR   PhosphoSite; Q5HZI5; -.
DR   PRIDE; Q5HZI5; -.
DR   Ensembl; ENSMUST00000071370; ENSMUSP00000071325; ENSMUSG00000035566.
DR   GeneID; 219228; -.
DR   KEGG; mmu:219228; -.
DR   UCSC; uc007uto.1; mouse.
DR   CTD; 219228; -.
DR   MGI; MGI:2684924; Pcdh17.
DR   GeneTree; ENSGT00560000076797; -.
DR   HOGENOM; HBG447181; -.
DR   HOVERGEN; HBG054878; -.
DR   InParanoid; Q5HZI5; -.
DR   NextBio; 376647; -.
DR   ArrayExpress; Q5HZI5; -.
DR   Bgee; Q5HZI5; -.
DR   Genevestigator; Q5HZI5; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR013164; Cadherin_N.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 6.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF08266; Cadherin_2; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 6.
DR   SUPFAM; SSF49313; Cadherin; 6.
DR   PROSITE; PS00232; CADHERIN_1; 5.
DR   PROSITE; PS50268; CADHERIN_2; 6.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell membrane; Membrane; Repeat;
KW   Transmembrane; Transmembrane helix.
SQ   SEQUENCE   1157 AA;  126133 MW;  A2A7C8B656845112 CRC64;
     MYLSICCCFL LWAPALTLKN LNYSVPEEQG AGTVIGNIGK DARLQPGLPP AERGSGSGRS
     KSGSYRVLEN SAPHLLDVDA DSGLLYTKQR IDRESLCRHN AKCQLSLEVF ANDKEICMIK
     VEIQDINDNA PSFPSDQIEM DISENAAPGT RFPLTSAHDP DAGENGLRTY LLTRDDHGLF
     ALDVKSRGDG TKFPELVIQK ALDRELQNHH TLVLTALDGG EPPRSATVQI NVKVIDSNDN
     SPVFEAPSYL VELPENAPLG TVVIDLNATD ADEGPNGEVL YSFSSYVPDR VRELFSIDPK
     TGLIRVKGNL DYEENGMLEI DVQARDLGPN PIPAHCKVTV KLIDRNDNAP SIGFVSVRQG
     ALSEAAPPGT VIALVRVTDR DSGKNGQLQC RVLGGGGTGG GLGGPGSVPF KLEENYDNFY
     TVVTDRPLDR ETQDDYNVTI VARDGGSPPL NSTKSFAVKI LDENDNPPRF TKGLYVLQVH
     ENNIPGEYLG SVLAQDPDLG QNGTVSYSIL PSHIGDVSIY TYVSVNPTNG AIYALRSFNY
     EQTKAFEFKV LAKDSGAPAH LESNATVRVT VLDVNDNAPV IVLPTLQNDT AELQVPRNAG
     LGYLVSTVRA LDSDFGESGR LTYEIVDGND DHLFEIDPSS GEIRTLHPFW EDVTPVVELV
     VKVTDHGKPT LSAVAKLIIR SVSGSLPEGV PRVNGEQHHW DMSLPLIVTL STISIILLAA
     MITIAVKCKR ENKEIRTYNC RIAEYSHPQL GGGKGKKKKI NKNDIMLVQS EVEERNAMNV
     MNVVSSPSLA TSPMYFDYQT RLPLSSPRSE VMYLKPASNN LTVPQGHAGC HTSFTGQGTN
     SSETPATRMS IIQTDNFPAE PNYMGSRQQF VQSSSTFKDP ERASLRDSGH GDSDQADSDQ
     DTNKGSCCDM SVREALKMKT TSTKSQPLEQ EPEECINCTD ECRVLGHSDR CWMPQFPAAN
     QAENADYRTN LFVPTVEANV ETETYETVNP TGKKTFCTFG KDKREHTILI ANVKPYLKAK
     RALSPLLQEV PSASSSPTKA CIEPCASTKG SLDGCEAKPG PLAEASSSYL PTDSQYPSPS
     KQPRDPSFMA SDQMARVFAD VHSRARRASS EMGAVLEQLE QPNRDLGRES VDAEEVVREI
     DKLLQDCRGN DPVAVRK
//
ID   F189B_MOUSE             Reviewed;         669 AA.
AC   Q5HZJ5;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   08-MAR-2011, entry version 40.
DE   RecName: Full=Protein FAM189B;
GN   Name=Fam189b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBUNIT: May interact with WWOX (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the FAM189 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC088990; AAH88990.1; -; mRNA.
DR   IPI; IPI00553283; -.
DR   RefSeq; NP_001014995.1; NM_001014995.1.
DR   UniGene; Mm.274708; -.
DR   ProteinModelPortal; Q5HZJ5; -.
DR   PhosphoSite; Q5HZJ5; -.
DR   PRIDE; Q5HZJ5; -.
DR   Ensembl; ENSMUST00000041913; ENSMUSP00000039261; ENSMUSG00000032657.
DR   GeneID; 68521; -.
DR   KEGG; mmu:68521; -.
DR   UCSC; uc008pxy.1; mouse.
DR   CTD; 68521; -.
DR   MGI; MGI:1915771; Fam189b.
DR   eggNOG; roNOG07534; -.
DR   HOGENOM; HBG126253; -.
DR   HOVERGEN; HBG051081; -.
DR   InParanoid; Q5HZJ5; -.
DR   OMA; GKVCVCC; -.
DR   OrthoDB; EOG41JZC0; -.
DR   NextBio; 327372; -.
DR   ArrayExpress; Q5HZJ5; -.
DR   Bgee; Q5HZJ5; -.
DR   Genevestigator; Q5HZJ5; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR007237; CD20-like.
DR   Pfam; PF04103; CD20; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    669       Protein FAM189B.
FT                                /FTId=PRO_0000393335.
FT   TRANSMEM     34     54       Helical; (Potential).
FT   TRANSMEM     67     87       Helical; (Potential).
FT   TRANSMEM     91    111       Helical; (Potential).
FT   TRANSMEM    174    194       Helical; (Potential).
FT   COMPBIAS    244    250       Poly-Pro.
FT   COMPBIAS    386    490       Pro-rich.
FT   CARBOHYD    160    160       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   669 AA;  72016 MW;  092E34F205AFEDA2 CRC64;
     MMPSPSDSSR SLTSRPSTRG LTHLRLHRPW LQALLTLGLA QVLLGILVIT FSMVASSVTT
     TESIKRSCPS WAGFSLAFSG LVGIVSWKRP FTLVISFFSL LSVLCVMLSM AGSVLSCKNA
     QLARDFRECS MEGKVCVCCP PIPLHRPCPE WGQELKVALN STCDEARGAL KNLLFSVCGL
     TICAAIICTL SAIVCCVQIF SLDLVHMQLA PERSVSGPLG PLACTSSPPA PLLHTMLDLE
     EFVPPVPPPP YYPPEYTCSS ETDAQSITYN GSMDSPVPLY PTDCPPSYEA VMGLRRDSQA
     TLFDPQLHDG SCVCERVASI VDVSMDSGSL VLSAIGDLPG GSSPSEDSCL LELQGSVRSV
     DYVLFRSIQR SRAGYCLSLD CGLRGPFEDS PLPRRPPRAA RSYSCSAPEA PPPLGAPTAA
     RSCHRLEGWP PWVGPCFPEL RRRVPRGGSR SAAPPPARAP ARRFSDSSGS LTPPGHRPPH
     RTPPPPLLLP RSHSDPGITT SSDIADFRDL YTKVLEEEAA SVSSADTGLC SEACLFRLAR
     CPSPKLLRAR SAEKRRPVPT FQKVPLPSGP TPAHSLGDLK GSWPGRGLVT RFLQLSRRSP
     DPTGTGAHGY KQVRRSPWGR PGRESLHLRS CGDLSSGSSL RRLLSARRLE HGIRPHSLSL
     NGGSRETGL
//
ID   NRSN2_MOUSE             Reviewed;         202 AA.
AC   Q5HZK2; A2AS81; Q3USR0;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=Neurensin-2;
GN   Name=Nrsn2; Synonyms=Gm123;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16527258; DOI=10.1016/j.brainres.2006.01.085;
RA   Nakanishi K., Ida M., Suzuki H., Kitano C., Yamamoto A., Mori N.,
RA   Araki M., Taketani S.;
RT   "Molecular characterization of a transport vesicle protein Neurensin-
RT   2, a homologue of Neurensin-1, expressed in neural cells.";
RL   Brain Res. 1081:1-8(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in maintenance and/or transport of
CC       vesicles.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- TISSUE SPECIFICITY: Expressed specifically in brain where it is
CC       widely expressed, with highest levels of expression in thalamus
CC       and hypothalamus. In brain, found in neural cell bodies and
CC       detected in many regions of the limbic system, such as the septum
CC       nucleus, horizontal and vertical limbs of the diagonal band,
CC       hippocampus, amygdaloid nucleus, and habernula nucleus. Also
CC       localizes to small vesicles found in the perinuclear region of
CC       Neuro2a and PC12 cells.
CC   -!- DEVELOPMENTAL STAGE: In cerebral cortex first detected at E15.5
CC       with increasing levels of expression observed during postnatal
CC       stages.
CC   -!- SIMILARITY: Belongs to the VMP family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE24271.1; Type=Frameshift; Positions=40;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK140190; BAE24271.1; ALT_FRAME; mRNA.
DR   EMBL; AL928568; CAM23206.1; -; Genomic_DNA.
DR   EMBL; BC088982; AAH88982.1; -; mRNA.
DR   IPI; IPI00350858; -.
DR   RefSeq; NP_001009948.1; NM_001009948.1.
DR   UniGene; Mm.330667; -.
DR   PRIDE; Q5HZK2; -.
DR   Ensembl; ENSMUST00000079278; ENSMUSP00000078260; ENSMUSG00000059361.
DR   GeneID; 228777; -.
DR   KEGG; mmu:228777; -.
DR   UCSC; uc008nfh.1; mouse.
DR   CTD; 228777; -.
DR   MGI; MGI:2684969; Nrsn2.
DR   GeneTree; ENSGT00530000063877; -.
DR   HOGENOM; HBG126037; -.
DR   HOVERGEN; HBG080467; -.
DR   InParanoid; Q5HZK2; -.
DR   OMA; SVQTIQP; -.
DR   OrthoDB; EOG4GMTZ0; -.
DR   PhylomeDB; Q5HZK2; -.
DR   NextBio; 379128; -.
DR   ArrayExpress; Q5HZK2; -.
DR   Bgee; Q5HZK2; -.
DR   CleanEx; MM_NRSN2; -.
DR   Genevestigator; Q5HZK2; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0030133; C:transport vesicle; IDA:UniProtKB.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    202       Neurensin-2.
FT                                /FTId=PRO_0000270585.
FT   TRANSMEM     65     85       Helical; (Potential).
FT   TRANSMEM    116    136       Helical; (Potential).
SQ   SEQUENCE   202 AA;  22415 MW;  9C68F26BD372980C CRC64;
     MSCSRPCVCS HGTSVEESTW YGFDFYPNLF YNDWLGTTTL PYNPERIPIR YINRPWPSLC
     WKVTVAVASL FLLLGVAALT TGYAVPPKLE LVNESKFSSM EDPVADYNQA LMTCRVVGAT
     LCGVAGIMLA VCLFLIASGW MFQDIKAEPL VTETDSPVEV FRDEPEKLSP AFHETSSQSP
     FLTPPSPFGQ QSVQTSQPQR DL
//
ID   S38AA_MOUSE             Reviewed;        1090 AA.
AC   Q5I012; A2AMZ5; Q3TVW4; Q641M1; Q80ZZ4; Q8C1Y0; Q8CCR5; Q9D8J3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   08-MAR-2011, entry version 44.
DE   RecName: Full=Putative sodium-coupled neutral amino acid transporter 10;
GN   Name=Slc38a10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 5 AND 6).
RC   STRAIN=C57BL/6J; TISSUE=Kidney, Olfactory bulb, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 353-1090 (ISOFORM 3).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, Colon, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-441 AND SER-887, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: Putative sodium-dependent amino acid/proton antiporter
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q5I012-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5I012-2; Sequence=VSP_031333;
CC       Name=3;
CC         IsoId=Q5I012-3; Sequence=VSP_031332;
CC       Name=4;
CC         IsoId=Q5I012-4; Sequence=VSP_031332, VSP_031333;
CC       Name=5;
CC         IsoId=Q5I012-5; Sequence=VSP_031329, VSP_031330;
CC         Note=No experimental confirmation available;
CC       Name=6;
CC         IsoId=Q5I012-6; Sequence=VSP_031328, VSP_031331;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2
CC       family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH43299.1; Type=Erroneous initiation;
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DR   EMBL; AK007977; BAB25384.1; -; mRNA.
DR   EMBL; AK032245; BAC27777.1; -; mRNA.
DR   EMBL; AK090050; BAC41066.1; -; mRNA.
DR   EMBL; AK159948; BAE35504.1; -; mRNA.
DR   EMBL; AL807824; CAM22601.1; -; Genomic_DNA.
DR   EMBL; AL807824; CAM22602.1; -; Genomic_DNA.
DR   EMBL; AL807824; CAM22603.1; -; Genomic_DNA.
DR   EMBL; AL807824; CAM22604.1; -; Genomic_DNA.
DR   EMBL; BC043299; AAH43299.1; ALT_INIT; mRNA.
DR   EMBL; BC082300; AAH82300.1; -; mRNA.
DR   EMBL; BC088811; AAH88811.1; -; mRNA.
DR   IPI; IPI00111582; -.
DR   IPI; IPI00228647; -.
DR   IPI; IPI00404588; -.
DR   IPI; IPI00649374; -.
DR   IPI; IPI00885760; -.
DR   IPI; IPI00886114; -.
DR   RefSeq; NP_001158270.1; NM_001164798.1.
DR   RefSeq; NP_001158271.1; NM_001164799.1.
DR   RefSeq; NP_001158272.1; NM_001164800.1.
DR   RefSeq; NP_001158273.1; NM_001164801.1.
DR   RefSeq; NP_001158274.1; NM_001164802.1.
DR   RefSeq; NP_077211.4; NM_024249.5.
DR   UniGene; Mm.253403; -.
DR   ProteinModelPortal; Q5I012; -.
DR   PRIDE; Q5I012; -.
DR   Ensembl; ENSMUST00000045402; ENSMUSP00000048675; ENSMUSG00000061306.
DR   Ensembl; ENSMUST00000053692; ENSMUSP00000057615; ENSMUSG00000061306.
DR   Ensembl; ENSMUST00000076697; ENSMUSP00000075989; ENSMUSG00000061306.
DR   Ensembl; ENSMUST00000103018; ENSMUSP00000099307; ENSMUSG00000061306.
DR   GeneID; 72055; -.
DR   KEGG; mmu:72055; -.
DR   UCSC; uc007mrx.1; mouse.
DR   CTD; 72055; -.
DR   MGI; MGI:1919305; Slc38a10.
DR   GeneTree; ENSGT00550000074222; -.
DR   HOVERGEN; HBG097690; -.
DR   InParanoid; Q5I012; -.
DR   OMA; YSETHTE; -.
DR   OrthoDB; EOG4QRH38; -.
DR   NextBio; 335328; -.
DR   ArrayExpress; Q5I012; -.
DR   Bgee; Q5I012; -.
DR   CleanEx; MM_SLC38A10; -.
DR   Genevestigator; Q5I012; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR013057; AA_transpt_TM.
DR   Pfam; PF01490; Aa_trans; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Amino-acid transport; Ion transport; Membrane;
KW   Phosphoprotein; Sodium; Sodium transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1   1090       Putative sodium-coupled neutral amino
FT                                acid transporter 10.
FT                                /FTId=PRO_0000318976.
FT   TRANSMEM      9     31       Helical; (Potential).
FT   TRANSMEM     36     58       Helical; (Potential).
FT   TRANSMEM     84    104       Helical; (Potential).
FT   TRANSMEM    123    143       Helical; (Potential).
FT   TRANSMEM    153    173       Helical; (Potential).
FT   TRANSMEM    229    249       Helical; (Potential).
FT   TRANSMEM    272    292       Helical; (Potential).
FT   TRANSMEM    323    343       Helical; (Potential).
FT   TRANSMEM    345    365       Helical; (Potential).
FT   TRANSMEM    378    398       Helical; (Potential).
FT   MOD_RES     441    441       Phosphoserine.
FT   MOD_RES     887    887       Phosphoserine.
FT   VAR_SEQ     378    428       VVLWVGLGILVVSTLTTLSVTEEAPLDLTQEARSGHRGDAE
FT                                GAMKVEAARL -> DLESCRRQPSGRGCLGLSDMGGATLTT
FT                                VPGPEVRANQRGMSGRAPGFISTC (in isoform 6).
FT                                /FTId=VSP_031328.
FT   VAR_SEQ     378    408       VVLWVGLGILVVSTLTTLSVTEEAPLDLTQE -> GLPTEP
FT                                WLSWYSLYRPGWPRTQGSPDSHPEC (in isoform 5).
FT                                /FTId=VSP_031329.
FT   VAR_SEQ     409   1090       Missing (in isoform 5).
FT                                /FTId=VSP_031330.
FT   VAR_SEQ     429   1090       Missing (in isoform 6).
FT                                /FTId=VSP_031331.
FT   VAR_SEQ     678    685       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_031332.
FT   VAR_SEQ     745    745       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_031333.
FT   CONFLICT    295    295       A -> T (in Ref. 1; BAC27777).
SQ   SEQUENCE   1090 AA;  117194 MW;  15321AFC6FCDBDA9 CRC64;
     MTAASTSKWG LITNVVNSIV GVSVLTMPFC FKQCGIVLGA LLLVFCSWMT HQSCMFLVKS
     ASLSKRRTYA GLAFHAYGKA GKMLVETSMI GLMLGSCITF YVVIGDLGSN FFAPLLGLQV
     TRTVRVFLLF AVSLFIVLPL SLQRNMMASI QSFSAMALLF YTVFMFVIVL SSLKHGLFSG
     QWLRQVSYIR WEGVFRCVPI FGMSFACQSQ VLPTYDSLDE PSVKTMSSIF ASSLNVVTAF
     YVMVGFFGYV SFTDATTGNV LIHFPSNPVT EMIRVGFVMS VAVGFPMMIL PCRQALNTLL
     FEQQQKDGTF AAGGYMPPLR FKVLTLSVVF GTMVGGVMIP NVETILGFTG ATMGSLICFI
     CPALIYKKAH KNAPSAQVVL WVGLGILVVS TLTTLSVTEE APLDLTQEAR SGHRGDAEGA
     MKVEAARLSV QDPVVVVAED SQEKLKPAED KEVLEQAQIK GPVDVPGGEA PKEKQEAAQL
     DRPGQGIAVP MGEAHRHEPP IPHDKVVVDE GQDQEGPEEK KPPPRLPDEG DPAGRGQGAP
     PLPESEKEKQ EPERGGEGKR PGQVLAVGET EHPQKVPEAN GQPPVQPRKE DSRPGNRDPQ
     PAAQARDSVE LKALAADDGR EPAQKAGGAL WKPVESAAES DAGGKAGLPV QRPEAAEQRE
     KKEAEQQGGD QAGSKLEAEI KKLVAEAGRA EMLDHAVLLQ VIQEQQVQQK RLLDQQEKLL
     AVIEEQHKEI RQQRQEGEED KPKPADVQPE PGVAVLRGQE EEAEHAGETL GDDPSQPLQP
     VLGAPRGRPA PSQDMGQHLP GEVKVLPGRD LADLPAGGSE TEPQGAPIDL REDPKAAIKA
     AGAGKELVPG DLEAVHKAAP PEVPKSPEKQ VAKAVAGQRQ DVFGEGSEER KETGKEAMAP
     GADTQKEAVQ PLVGAEAKDT KSRQSGPTKA PVQTQAKFHP EPQAIFDTGQ GSHPEVRSEA
     PRAVHIPPEE QHKGKGGAAI QEAKQRPDPN SGPKLAVPAG QKPENAKPNR DLKVQAGSDL
     RRRRRDLASH PEQELAPKDG VIISFNSLPN VQVNDLRSAL DTQLRQAAGA ALQVVHSRQI
     KQLSGDLEEA
//
ID   Q5ICG5_MOUSE            Unreviewed;       697 AA.
AC   Q5ICG5;
DT   19-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   19-SEP-2006, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   SubName: Full=Acyl-CoA synthetase long-chain family member 6;
DE   SubName: Full=Long chain acyl-CoA synthetase 6 isoform 3;
GN   Name=Acsl6; ORFNames=RP23-297J14.1-011;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=15629433; DOI=10.1016/j.bbrc.2004.11.141;
RA   Lee E.J., Kim H.C., Cho Y.Y., Byun S.J., Lim J.M., Ryoo Z.Y.;
RT   "Alternative promotion of the mouse acyl-CoA synthetase 6 (mAcsl6)
RT   gene mediates the expression of multiple transcripts with 5'-end
RT   heterogeneity: genetic organization of mAcsl6 variants.";
RL   Biochem. Biophys. Res. Commun. 327:84-93(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Harrison E.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RA   Collins J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY786360; AAW33883.1; -; mRNA.
DR   EMBL; AY786362; AAW33885.1; -; mRNA.
DR   EMBL; AL596127; CAI51897.1; -; Genomic_DNA.
DR   EMBL; AL603822; CAI51897.1; JOINED; Genomic_DNA.
DR   EMBL; AL603822; CAO78122.1; -; Genomic_DNA.
DR   EMBL; AL596127; CAO78122.1; JOINED; Genomic_DNA.
DR   IPI; IPI00262693; -.
DR   RefSeq; NP_001028771.1; NM_001033599.1.
DR   UniGene; Mm.267478; -.
DR   ProteinModelPortal; Q5ICG5; -.
DR   STRING; Q5ICG5; -.
DR   PRIDE; Q5ICG5; -.
DR   Ensembl; ENSMUST00000101211; ENSMUSP00000098771; ENSMUSG00000020333.
DR   Ensembl; ENSMUST00000101213; ENSMUSP00000098773; ENSMUSG00000020333.
DR   Ensembl; ENSMUST00000108902; ENSMUSP00000104530; ENSMUSG00000020333.
DR   Ensembl; ENSMUST00000108904; ENSMUSP00000104532; ENSMUSG00000020333.
DR   GeneID; 216739; -.
DR   KEGG; mmu:216739; -.
DR   UCSC; uc007ixt.1; mouse.
DR   CTD; 216739; -.
DR   MGI; MGI:894291; Acsl6.
DR   eggNOG; roNOG07192; -.
DR   HOVERGEN; HBG050452; -.
DR   InParanoid; Q5ICG5; -.
DR   PhylomeDB; Q5ICG5; -.
DR   NextBio; 375272; -.
DR   ArrayExpress; Q5ICG5; -.
DR   Bgee; Q5ICG5; -.
DR   Genevestigator; Q5ICG5; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007405; P:neuroblast proliferation; IDA:MGI.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   Pfam; PF00501; AMP-binding; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   697 AA;  77970 MW;  F4B43D9114732C60 CRC64;
     MQTQEILRIL RLPELSDLGQ FFRSLSATTL VSVGALAAVL AYWLTHRPKA LQPPCNLLKQ
     SEEVEDGGGA RRSVIGGCTQ LLTHYYDDAR TMYQVFRRGL SISGNGPCLG FRKPEQPYQW
     LSYQEVAKRA EFLGSGLLQH DCKVGTEQFV GVFAQNRPEW IIAELACYTY SMVVVPLYDT
     LGPGSISYII NTADICTVIV DKPHKATLLL EHVERKETPG LKLVILMEPF EDALRERGKK
     CGVDIKSMQA IEDCGRENHH APVPPRPDDL SIVCFTSGTT GNPKGAMLTH GNVVADFSGF
     LKVTESQWAP TCADVHFSYL PLAHMFERMV QSVVYCHGGR VGFFQGDIRL LSDDMKALRP
     TIFPVVPRLL NRMYDKIFHQ ADTSLKRWLL EFAAKRKQAE VRSGIIRNNS IWDELFFNKI
     QASLGGHVRM IVTGAAPASP TVLGFLRAAL GCQVYEGYGQ TECTAGCTFT TPGDWTSGHV
     GAPLPCNHIK LVDAEELNYW TCKGEGEICV KGPNVFKGYL KDEDRTKEAL DSDGWLHTGD
     IGKWLPEGTL KIIDRKKHIF KLAQGEYVAP EKIENIYIRS EPVAQIYVHG DSLKAFLVGI
     VVPDPEVMPS WAQKKGIEGT YQELCMKKEL KKAILDDMVM LGKESGLHSF EQVKAIYIHC
     DMFSVQNGLL TPTLKAKRPE LREYFKKQIE ELYLVSV
//
ID   COBL_MOUSE              Reviewed;        1337 AA.
AC   Q5NBX1; Q5NBX2; Q60859; Q6PAT4; Q7TQM9; Q80TV4; Q8C7Q0; Q8CE81;
AC   Q8CIM4;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=Protein cordon-bleu;
GN   Name=Cobl; Synonyms=Kiaa0633;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=CD-1; TISSUE=Brain;
RX   MEDLINE=22873732; PubMed=14512015; DOI=10.1016/S0012-1606(03)00323-3;
RA   Carroll E.A., Gerrelli D., Gasca S., Berg E., Beier D.R., Copp A.J.,
RA   Klingensmith J.;
RT   "Cordon-bleu is a conserved gene involved in neural tube formation.";
RL   Dev. Biol. 262:16-31(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic spinal cord, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
RP   SPLICING.
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 734-1337.
RC   STRAIN=C57BL/6, and Czech II; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 64-448, AND TISSUE SPECIFICITY.
RC   STRAIN=CD-1; TISSUE=Brain;
RX   MEDLINE=96083059; PubMed=7586755; DOI=10.1002/dvg.1020170206;
RA   Gasca S., Hill D.P., Klingensmith J., Rossant J.;
RT   "Characterization of a gene trap insertion into a novel gene, cordon-
RT   bleu, expressed in axial structures of the gastrulating mouse
RT   embryo.";
RL   Dev. Genet. 17:141-154(1995).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-272, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- INTERACTION:
CC       P68135:ACTA1 (xeno); NbExp=1; IntAct=EBI-1550138, EBI-367540;
CC       Q9Z0W5:Pacsin1 (xeno); NbExp=2; IntAct=EBI-1550138, EBI-1550185;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q5NBX1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5NBX1-2; Sequence=VSP_021615, VSP_021618;
CC       Name=3;
CC         IsoId=Q5NBX1-3; Sequence=VSP_021614;
CC       Name=4;
CC         IsoId=Q5NBX1-4; Sequence=VSP_021619, VSP_021620;
CC       Name=5;
CC         IsoId=Q5NBX1-5; Sequence=VSP_021616, VSP_021617;
CC   -!- TISSUE SPECIFICITY: Detected in embryonic neural tube.
CC   -!- SIMILARITY: Contains 3 WH2 domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH23264.1; Type=Frameshift; Positions=1291;
CC       Sequence=BAC65616.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AY308745; AAP74341.1; -; mRNA.
DR   EMBL; AK122334; BAC65616.1; ALT_INIT; mRNA.
DR   EMBL; AK028833; BAC26144.1; -; mRNA.
DR   EMBL; AK049730; BAC33896.1; -; mRNA.
DR   EMBL; AL669822; CAI35985.1; -; Genomic_DNA.
DR   EMBL; AL713914; CAI35985.1; JOINED; Genomic_DNA.
DR   EMBL; AL669822; CAI35986.1; -; Genomic_DNA.
DR   EMBL; AL713914; CAI35986.1; JOINED; Genomic_DNA.
DR   EMBL; AL713914; CAI36022.1; -; Genomic_DNA.
DR   EMBL; AL669822; CAI36022.1; JOINED; Genomic_DNA.
DR   EMBL; AL713914; CAI36023.1; -; Genomic_DNA.
DR   EMBL; AL669822; CAI36023.1; JOINED; Genomic_DNA.
DR   EMBL; BC023264; AAH23264.1; ALT_FRAME; mRNA.
DR   EMBL; BC060061; AAH60061.1; -; mRNA.
DR   EMBL; U26967; AAA92362.1; -; mRNA.
DR   IPI; IPI00330247; -.
DR   IPI; IPI00623041; -.
DR   IPI; IPI00808291; -.
DR   IPI; IPI00808541; -.
DR   IPI; IPI00808590; -.
DR   RefSeq; NP_766084.3; NM_172496.3.
DR   UniGene; Mm.22847; -.
DR   HSSP; Q6IQ33; 2DAJ.
DR   ProteinModelPortal; Q5NBX1; -.
DR   SMR; Q5NBX1; 149-234.
DR   IntAct; Q5NBX1; 4.
DR   STRING; Q5NBX1; -.
DR   PhosphoSite; Q5NBX1; -.
DR   PRIDE; Q5NBX1; -.
DR   Ensembl; ENSMUST00000046755; ENSMUSP00000045693; ENSMUSG00000020173.
DR   Ensembl; ENSMUST00000109651; ENSMUSP00000105278; ENSMUSG00000020173.
DR   GeneID; 12808; -.
DR   KEGG; mmu:12808; -.
DR   NMPDR; fig|10090.3.peg.23295; -.
DR   UCSC; uc007ibd.1; mouse.
DR   UCSC; uc007ibf.1; mouse.
DR   CTD; 12808; -.
DR   MGI; MGI:105056; Cobl.
DR   GeneTree; ENSGT00530000063608; -.
DR   HOVERGEN; HBG081301; -.
DR   InParanoid; Q5NBX1; -.
DR   OMA; SVGQSCG; -.
DR   OrthoDB; EOG4R23TC; -.
DR   NextBio; 282252; -.
DR   ArrayExpress; Q5NBX1; -.
DR   Bgee; Q5NBX1; -.
DR   CleanEx; MM_COBL; -.
DR   Genevestigator; Q5NBX1; -.
DR   GermOnline; ENSMUSG00000020173; Mus musculus.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0001843; P:neural tube closure; IGI:MGI.
DR   InterPro; IPR019025; Cordon-bleu_domain.
DR   InterPro; IPR003124; WH2_actin-bd.
DR   Pfam; PF09469; Cobl; 1.
DR   Pfam; PF02205; WH2; 3.
DR   SMART; SM00246; WH2; 3.
DR   PROSITE; PS51082; WH2; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein; Repeat.
FT   CHAIN         1   1337       Protein cordon-bleu.
FT                                /FTId=PRO_0000260492.
FT   DOMAIN     1185   1205       WH2 1.
FT   DOMAIN     1225   1245       WH2 2.
FT   DOMAIN     1313   1333       WH2 3.
FT   MOTIF       323    328       KKRRAP 1.
FT   MOTIF       356    361       KKRRAP 2.
FT   COMPBIAS     22     25       Poly-Pro.
FT   COMPBIAS    361    433       Pro-rich.
FT   COMPBIAS   1277   1293       Pro-rich.
FT   MOD_RES     235    235       Phosphoserine.
FT   MOD_RES     272    272       Phosphoserine.
FT   MOD_RES     372    372       Phosphoserine (By similarity).
FT   MOD_RES     816    816       Phosphoserine (By similarity).
FT   MOD_RES     826    826       Phosphoserine.
FT   VAR_SEQ       1     16       Missing (in isoform 3).
FT                                /FTId=VSP_021614.
FT   VAR_SEQ     262    286       Missing (in isoform 2).
FT                                /FTId=VSP_021615.
FT   VAR_SEQ     345    349       ASLSS -> VPLLV (in isoform 5).
FT                                /FTId=VSP_021616.
FT   VAR_SEQ     350   1337       Missing (in isoform 5).
FT                                /FTId=VSP_021617.
FT   VAR_SEQ     391    448       GVGRQVPQKPPRGTARGPPQLVLPPPPPYPPPDTDVTEPVT
FT                                FPGEGAGSETSELRPKL -> V (in isoform 2).
FT                                /FTId=VSP_021618.
FT   VAR_SEQ     448    469       LSLPLGPGSHCSMGGVSQVPAE -> RTCLLLPFQLCVDHL
FT                                SFWSLLV (in isoform 4).
FT                                /FTId=VSP_021619.
FT   VAR_SEQ     470   1337       Missing (in isoform 4).
FT                                /FTId=VSP_021620.
FT   CONFLICT     10     10       K -> Q (in Ref. 3; BAC33896).
FT   CONFLICT     18     18       K -> R (in Ref. 3; BAC33896).
FT   CONFLICT     45     45       L -> M (in Ref. 3; BAC26144).
FT   CONFLICT    112    112       T -> N (in Ref. 1; AAP74341).
FT   CONFLICT    128    128       N -> S (in Ref. 3; BAC26144).
FT   CONFLICT    801    801       L -> F (in Ref. 1; AAP74341).
FT   CONFLICT    914    914       Q -> R (in Ref. 4; BAC65616).
FT   CONFLICT   1010   1010       V -> I (in Ref. 5; AAH23264).
FT   CONFLICT   1112   1112       L -> V (in Ref. 5; AAH23264).
FT   CONFLICT   1205   1205       T -> V (in Ref. 1; AAP74341).
FT   CONFLICT   1285   1285       P -> T (in Ref. 1; AAP74341 and 5;
FT                                AAH23264).
SQ   SEQUENCE   1337 AA;  143865 MW;  F4A8D3250294A277 CRC64;
     MDAPRALAAK PPTGRKMKAR APPPPGKPAA QNVHSEQKLP HDATLGSQQS LVYMKEALQN
     STLDITVVLP SGLEKQSVVS GSHAMMDLLV ELCLQNHLNP SHHVLEIWSS ETQQPLSFKP
     NTLIGSLNVH TVLLKEKVPE ERVKPGLTKA PEKSVRLVVN YLRTQKAVVR VSPEVPLQNI
     LPVICAKCEV NPEHVILLRD NVAGEELELS KSLNELGIKE LYAWDNRREM FRKSSLGNDE
     TDKEKKKFLG FFKANKRSNS KAEHLGLSGA DSDEDPAKSA SGGDLNGCVT TPNSPSLHSR
     SLTLGPSLSL GNISGVSMKS DMKKRRAPPP PSPKLLGQDK VSEKASLSSQ ADLQKKKRRA
     PAPPPPQQPP PSPVVPNRKE DKEENRKSTV GVGRQVPQKP PRGTARGPPQ LVLPPPPPYP
     PPDTDVTEPV TFPGEGAGSE TSELRPKLSL PLGPGSHCSM GGVSQVPAES EETASEDTTE
     DSGVMSSPSD AISLDSQQDS MRSKDKWSTD QEDGSDQDLA GTPELGPQKS PSWGKSGSGS
     SILRTEKATM PTNDDEDLFI TGHLHQTLAE LDEDLEGMEE NYETDTSSLT NSVNGVSNHS
     LQEAIIPDSG VDDIPVTFIG EVSDEPFDSG LFSSRCNNAT TFNTGSIASQ RSHLSPSQTE
     HSQPFVRTSR KEPDPSPPSQ DNRKRNQPTL ANTSENENPV ETDPTVTSLV SKLLIDDPKA
     KDKGKVHGSS HSEKTQAGHG INSLRVNPRD GKDESSNSAP PPWSHHGQAL GGSYGLKYGL
     TTYKIVPPKS EMRCYDRDVS LSTGAIKIDE LGNLVSPHMN GSRTISPPSA VVETDTPPIG
     KVKEFWRRNS MEKYLNGPAE CTIKRAPSTT ITATPEKPQQ DNGMKAAFTV TTPQQQPASQ
     EYGAHLEEER SRPQSAVSCS VKVPASNPTD ITFLKPQRRT SSQYVASAIA KKMGPPKVHA
     DVVRPHKATT EQCHEEAKLA RSPPTRKDDA APNLHSEARQ HEHGTNQSSV CLPSNPGVQL
     PAGGHPKVEV NSTYGKSSTQ DYPAAVHRNS YFLPGRSSHR DRVSVGQSCG FNEKQTTSNQ
     KANSTSNFSQ ALDKAHPPPL LLAEARDSGR ILMNGSARTP GNCEPPHSPK ESTLTSYIIL
     QTEEKPSSLS TDGQDADDTL PSSIFGPKKK FKPVIQRPLP KDVSLHSALM EAIHSSGGRE
     KLRKTAEQTS EGRPKKPSYV EAESERSALL AAIRGHSGTL SLRKVSSLAS EELQSFRNAA
     LGAPGLDKPQ QEDLGLPPPP ALPPPPAPAP QAPSASVTVS RFSTGTPSNS VNARQALMDA
     IRSGTGAARL RKVPLLV
//
ID   Q5NCM5_MOUSE            Unreviewed;       634 AA.
AC   Q5NCM5;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   SubName: Full=Epsin 2;
GN   Name=Epn2; ORFNames=RP23-155J3.7-006;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Lovell J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 ENTH (epsin N-terminal homology) domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AL604029; CAI24191.1; -; Genomic_DNA.
DR   IPI; IPI00464280; -.
DR   UniGene; Mm.139695; -.
DR   UniGene; Mm.436466; -.
DR   ProteinModelPortal; Q5NCM5; -.
DR   SMR; Q5NCM5; 1-158.
DR   STRING; Q5NCM5; -.
DR   PRIDE; Q5NCM5; -.
DR   Ensembl; ENSMUST00000093020; ENSMUSP00000090699; ENSMUSG00000001036.
DR   Ensembl; ENSMUST00000108712; ENSMUSP00000104352; ENSMUSG00000001036.
DR   MGI; MGI:1333766; Epn2.
DR   HOVERGEN; HBG006690; -.
DR   InParanoid; Q5NCM5; -.
DR   OMA; RPNGDWS; -.
DR   PhylomeDB; Q5NCM5; -.
DR   ArrayExpress; Q5NCM5; -.
DR   Bgee; Q5NCM5; -.
DR   Genevestigator; Q5NCM5; -.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR013809; Epsin-like_N.
DR   InterPro; IPR001026; Epsin_dom_N.
DR   InterPro; IPR003903; Ubiquitin-int_motif.
DR   Gene3D; G3DSA:1.25.40.90; ENTH_VHS; 1.
DR   Pfam; PF01417; ENTH; 1.
DR   SMART; SM00273; ENTH; 1.
DR   SMART; SM00726; UIM; 2.
DR   SUPFAM; SSF48464; ENTH_VHS; 1.
DR   PROSITE; PS50942; ENTH; 1.
DR   PROSITE; PS50330; UIM; 2.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   634 AA;  67786 MW;  E18EF4C31BE3C2DA CRC64;
     MTTSSIRRQM KNIVNNYSEA EIKVREATSN DPWGPSSSLM TEIADLTYNV VAFSEIMSMV
     WKRLNDHGKN WRHVYKALTL LDYLIKTGSE RVAQQCRENI FAIQTLKDFQ YIDRDGKDQG
     INVREKSKQL VALLKDEERL KVERVQALKT KERMAQVATG VGSNQITFGR GSSQPNLSTS
     YSEQEYGKAG GSPASYHGSP EASLCPQHRT GAMLGQSEEL QPLSQRHPCL PHLGLASHPN
     GDWAQPCLTC DRAARATSPR VSSELEQARP QTSGEEELQL QLALAMSREV AEQEERLRRG
     DDLRLQMALE ESRRDTVKVP KKKEPGSHSQ QTTLLDLMDA LPSSGPVTQK TEPWSAGASA
     NQTNPWGGTV APSNITDPWP SFGTKPAASV DPWGVPTTAS TQSVPKNSDP WAASQQPASN
     AGKTTDAWGA AKPSSASGSF ELFSNFNGTV KDDFSEFDNL RTSKKPAESG ASVPPQDSRT
     TSPDLFESQS LTSASSKPSS ARKTPESFLG PNAALVNLDS LVTKPAPPAQ SLNPFLAPGA
     AAPAPVNPFQ VNQPQPLTLN QLRGSPVLGS SASFGSGPGV ETVAPMTSVA PHSSVGASGS
     SLTPLGPTAM NMVGSVGIPP SAAQSTGTTN PFLL
//
ID   NEUL4_MOUSE             Reviewed;        1563 AA.
AC   Q5NCX5; Q3U090; Q5NCX4; Q69ZA2; Q8R1V5;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   08-MAR-2011, entry version 40.
DE   RecName: Full=Neuralized-like protein 4;
GN   Name=Neurl4; Synonyms=Kiaa1787;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-1563 (ISOFORM 1).
RC   STRAIN=NOD; TISSUE=Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 142-1563 (ISOFORM 2).
RC   TISSUE=Embryo;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 936-1563.
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5NCX5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5NCX5-2; Sequence=VSP_027564;
CC   -!- SIMILARITY: Contains 6 NHR (neuralized homology repeat) domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI35150.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL596185; CAI35149.1; -; Genomic_DNA.
DR   EMBL; AL596185; CAI35150.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AK157107; BAE33965.1; -; mRNA.
DR   EMBL; AK173264; BAD32542.1; -; mRNA.
DR   EMBL; BC023037; AAH23037.1; -; mRNA.
DR   IPI; IPI00648294; -.
DR   IPI; IPI00857074; -.
DR   RefSeq; NP_001013432.1; NM_001013414.2.
DR   UniGene; Mm.268347; -.
DR   ProteinModelPortal; Q5NCX5; -.
DR   SMR; Q5NCX5; 38-207, 320-484, 521-686, 717-884, 913-1085, 1129-1293.
DR   STRING; Q5NCX5; -.
DR   PhosphoSite; Q5NCX5; -.
DR   PRIDE; Q5NCX5; -.
DR   Ensembl; ENSMUST00000061837; ENSMUSP00000053235; ENSMUSG00000047284.
DR   GeneID; 216860; -.
DR   KEGG; mmu:216860; -.
DR   UCSC; uc007jsn.1; mouse.
DR   CTD; 216860; -.
DR   MGI; MGI:1921092; Neurl4.
DR   HOGENOM; HBG358208; -.
DR   InParanoid; Q5NCX5; -.
DR   OMA; PPERLNF; -.
DR   NextBio; 375412; -.
DR   ArrayExpress; Q5NCX5; -.
DR   Bgee; Q5NCX5; -.
DR   CleanEx; MM_0610025P10RIK; -.
DR   Genevestigator; Q5NCX5; -.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR006573; Neu_Z.
DR   Pfam; PF07177; Neuralized; 6.
DR   SMART; SM00588; NEUZ; 6.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 2.
DR   PROSITE; PS51065; NHR; 6.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Phosphoprotein; Repeat.
FT   CHAIN         1   1563       Neuralized-like protein 4.
FT                                /FTId=PRO_0000299106.
FT   DOMAIN       43    209       NHR 1.
FT   DOMAIN      319    486       NHR 2.
FT   DOMAIN      522    688       NHR 3.
FT   DOMAIN      718    886       NHR 4.
FT   DOMAIN      915   1087       NHR 5.
FT   DOMAIN     1132   1295       NHR 6.
FT   MOD_RES     504    504       Phosphoserine (By similarity).
FT   MOD_RES     909    909       Phosphoserine (By similarity).
FT   MOD_RES    1146   1146       Phosphoserine (By similarity).
FT   VAR_SEQ     245    266       Missing (in isoform 2).
FT                                /FTId=VSP_027564.
FT   CONFLICT   1247   1247       L -> M (in Ref. 2; BAE33965).
SQ   SEQUENCE   1563 AA;  167637 MW;  65F86EC95429B6C0 CRC64;
     MAAGSGGSGG SGAGPGPGPG PGGGGGPGSS GPGLGSGGGL GGGGELHPRT GRLVSLSACG
     RTARRQQPGQ EFNHGLVLSR EPLRDGRVFT VRIDRKVNSW SGSIEIGVTA LDPSVLDFPS
     SATGLKGGSW VVSGCSVLRD GRSVLEEYGQ DLDQLVEGDR VGVERTATGE LRLWVNGRDC
     GVAATGLPAR VWAVVDLYGK CTQITVLPSE PGFSPPTPVP TPPLEPLAPP EDSALLEQGT
     SVDEAFMVSP AQARPETFPN SLDSHNDFAS MELSEVVSNA ILSAYNGGLL NVSLSSPPAG
     DGLASSGPAT SPILTSNDAL LFHEKCGTLI KLSNNNKTAE RRRPLDEFNN GVVMTNRPLR
     DNEMFEIRID KLVDKWSGSI EIGVTTHNPN SLEYPATMTN LQSGTIMMSG CGILTNGKGT
     RREYCEFSLD ELQEGDHIGL TRKSNSALHF FINGIDQGVA TPLTPPVVYG VVDLYGMAVK
     VTIVHNNNHS DRLRRNNAIL RALSPEGALR RAAPAAQAEP ERLLFHPNCG QKAAITHEGR
     TALRPHATDD FNHGVVLSSR ALRDGEVFQV RIDKMVDKWA GSIEIGVTTH NPAYLQLPST
     MTNLRSGTWM MTGNGVMHNG TTILDEYGHN LDRLKAGDTV GVVRREDGTL HFFVNGMTQG
     PAAWNVPPGV YAVVDLYGQA AQATIVDDVE VPPVSEPLPE GNNQMSPSSP SSAAGGSDLR
     FHQLHGSNAV ITNGGRTALR HNCRSEFNDA IVISNRALRD GELFEIVIQK MVDRWSGSIE
     AGVTAIRPED LEFPNTMTDI DYDTWMLSGT AIMQDGNTMR NNYGCDLDAL GTGARIGMMR
     TAKGDLHYFI NGQDQGAACS GLPPGKEVYA VVDLYGQCVQ VSITNATGPM DNSLATSNTA
     TEKSFPLHSP VAGVAHRFHS MCGKNVTLEE DGTRAVRVAG YAHGLVFSTK ELKAEEVFEV
     KVEELDEKWA GSLRLGLTTL APEDMGPGAG SGPGLPPSLP ELRTKTTWMV SSCEVRRDGH
     LQRMNYGRNL ERLGVGSRVG IRRCADDTMH ILVDGEDMGP AAAGIAKNVW AVLDLYGPVR
     SVAIVSSTRL EEPEGTQPPS PSSDTGSEVE EDDEVEEQGL RGQNQVGIVP TALEFLENHG
     KNILLSNGNR TATRVASYNQ GIVVISQPLV PHMLVQVRID FLNRQWTSSL VLGVITCPPE
     RLNFPASACA LKRAAWLLRG RGVFHNGLKI CEKFGPNLDT CPEGTILGLR LDSSGGLHLH
     INGVDQGVAV PDVPQPCHAL VDLYGQCEQV TIVSPDPGTA SGKIAGTQGD MEKADMVDGI
     KESVCWGPPP AASPLKSCEY HALCSRFQEL LLLPEDYFMP PPKRSLCYCE SCRKLRGDEA
     HRRRGEPPRE YALPFGWCRF NLRVNPHLEA GTLTKKWHMA YHGSSVAVVR RVLDRGELGA
     GTTSILSCRP LKGEPGVGFE EPGENCAPPR EEQPPPVLLS PSLQYAGAEM LASKVQFRDP
     KSQRTHQAQV AFQVCVRPGS YTPGPPSAAL RELPDQHFSP SELEWVTKEK GATLLYALLV
     RVE
//
ID   K1211_MOUSE             Reviewed;        1207 AA.
AC   Q5PR69; Q80TH6; Q8C7K8; Q8C7R0; Q8C9F2; Q8CDM6;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   08-FEB-2011, entry version 35.
DE   RecName: Full=Uncharacterized protein KIAA1211;
GN   Name=Kiaa1211;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 347-1207 (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 496-1207 (ISOOFRM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 818-1207 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 862-1207 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, Spinal cord, Testis, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5PR69-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5PR69-2; Sequence=VSP_034472;
CC         Note=No experimental confirmation available;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC33846.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC166328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC086807; AAH86807.1; -; mRNA.
DR   EMBL; AK122469; BAC65751.1; -; mRNA.
DR   EMBL; AK029850; BAC26643.1; -; mRNA.
DR   EMBL; AK042228; BAC31199.1; -; mRNA.
DR   EMBL; AK049629; BAC33846.1; ALT_INIT; mRNA.
DR   EMBL; AK050000; BAC34025.1; -; mRNA.
DR   IPI; IPI00351485; -.
DR   IPI; IPI00896687; -.
DR   RefSeq; NP_001157265.1; NM_001163793.1.
DR   UniGene; Mm.101504; -.
DR   UniGene; Mm.449998; -.
DR   PhosphoSite; Q5PR69; -.
DR   Ensembl; ENSMUST00000048811; ENSMUSP00000039677; ENSMUSG00000036377.
DR   GeneID; 320827; -.
DR   KEGG; mmu:320827; -.
DR   MGI; MGI:2444817; C530008M17Rik.
DR   GeneTree; ENSGT00530000064039; -.
DR   HOVERGEN; HBG108030; -.
DR   Bgee; Q5PR69; -.
DR   Genevestigator; Q5PR69; -.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1   1207       Uncharacterized protein KIAA1211.
FT                                /FTId=PRO_0000342476.
FT   COMPBIAS    101    104       Poly-Ser.
FT   COMPBIAS    210    525       Glu-rich.
FT   COMPBIAS    844    847       Poly-Lys.
FT   MOD_RES     132    132       Phosphoserine (By similarity).
FT   MOD_RES     552    552       Phosphoserine (By similarity).
FT   MOD_RES     555    555       Phosphothreonine (By similarity).
FT   MOD_RES     850    850       Phosphoserine (By similarity).
FT   MOD_RES     949    949       Phosphothreonine (By similarity).
FT   MOD_RES     953    953       Phosphoserine (By similarity).
FT   MOD_RES    1016   1016       Phosphoserine (By similarity).
FT   VAR_SEQ    1034   1036       Missing (in isoform 2).
FT                                /FTId=VSP_034472.
FT   CONFLICT   1105   1105       L -> V (in Ref. 4; BAC31199).
FT   CONFLICT   1140   1140       R -> T (in Ref. 4; BAC34025).
SQ   SEQUENCE   1207 AA;  132272 MW;  BD44DEA750D423C5 CRC64;
     MGARAFSHDS IFIPDGGAES EQTVQAMSQD NILGKVKTLQ RQLGKNIKFG QRPSNAIPMK
     KAGSTDASSE EDFVLTSPME IVTQQDIVPS DTENKSSDTP SSSSPLNLPE AGSDMEEKVA
     PVKPSRPKRH LSSAGTIESV NLDAIPLAIA RLDNSAARHK LAVKPKNQRV SRKHRWLAQD
     RQNEPGSFES QSSLDQNGQL GEDKHIWHGE EPEPLESHEE KRLHEEYWRE LEAKCKRQKA
     EAAEKRRQEE QRRQALERRL WEESLRQELL EEEEEGEEEE EVKEEGEEGE EVGLQPRAGK
     VPPEEGHQSG PEEQRCTEQE LGGADDPARL EAEERRREQE EAERQAEKLR QRDAESQEEE
     LRQREAERQR AQEEDAKGML QEEEEEAKRI EELKGKETPE PLVEEGPQSP EGESQPWLTD
     DADQRSPLQR DLEKPGERER EDLESAGQRE IAEEPRGEGE PAEQSGDLDA HCGGVDGEGK
     ETAQTDSPQP QERQMEGTPA PEENEATAAD IDRKVEELRW QEVDERQTMP RPYTFQVSSG
     SRQILFPKVN LSPVTPAKDA SLAPAAQEPP APRGAASHAL PSALSIPHTA ILVTGAQLCG
     PAVNLSQIKD TACKSLLGLS EEKRPMDVPT VESRAGSGKS RPAPESPSNA AALAEWASIR
     SRILKNSEGD QRGDREPARA GDEPVPRARC DSRGNVRRTP PVNAKFSIMP AWQKFSDSGA
     ETFRQSLDGE SGRKKPGLAP SEETAPQPHA AAQQEVSQEP PDTTDGCKFA KDLPSFLVPG
     LPSPQKAASR TESTTTLDSE TTSDVGNPDP AMPGGEEKAS PFGIKLRRTN YSLRFHCDQQ
     AEQKKKKRHS STGDSVGGAT PATGSVSGES EPEATFLKHG PSLPQERKPA LSPRKDSAES
     HSSGHYVAVA QSGLPPASGQ TPAPEQDRAV SKMPSMQKPA LAPKPASQTP PSSPLSKLSR
     PHLVELLARR AGKLDSEPSE TAKESSDNQP PSPSLPEELK GQKRDEKDVP EKKPASPPLP
     AGQQERPSLI PETGRKEKPV LQSRHSLDGS KVTEKVETAQ PLWITLALQK QKGFREQQAT
     REERKQAREA KQAEKLSKET VSVSLQPGSS RASKTAPVHK PAAPSEEKKP ETAVSRLQRR
     EQLKKSNTLP TSVTVEISDS APSAALVKDV TKRFSTPDAA PVSTEPAWLA LAKRKAKAWS
     DCPQIIK
//
ID   DIRA2_MOUSE             Reviewed;         199 AA.
AC   Q5PR73;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=GTP-binding protein Di-Ras2;
DE   AltName: Full=Distinct subgroup of the Ras family member 2;
GN   Name=Diras2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Displays low GTPase activity and exist predominantly in
CC       the GTP-bound form (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Di-Ras
CC       family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC086799; AAH86799.1; -; mRNA.
DR   IPI; IPI00126551; -.
DR   RefSeq; NP_001019645.1; NM_001024474.2.
DR   UniGene; Mm.29362; -.
DR   ProteinModelPortal; Q5PR73; -.
DR   SMR; Q5PR73; 6-176.
DR   PhosphoSite; Q5PR73; -.
DR   PRIDE; Q5PR73; -.
DR   Ensembl; ENSMUST00000057442; ENSMUSP00000055416; ENSMUSG00000047842.
DR   GeneID; 68203; -.
DR   KEGG; mmu:68203; -.
DR   UCSC; uc007qmv.1; mouse.
DR   CTD; 68203; -.
DR   MGI; MGI:1915453; Diras2.
DR   GeneTree; ENSGT00560000076632; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; Q5PR73; -.
DR   OMA; AKKWKCA; -.
DR   OrthoDB; EOG46MBKP; -.
DR   PhylomeDB; Q5PR73; -.
DR   NextBio; 326698; -.
DR   ArrayExpress; Q5PR73; -.
DR   Bgee; Q5PR73; -.
DR   CleanEx; MM_DIRAS2; -.
DR   Genevestigator; Q5PR73; -.
DR   GermOnline; ENSMUSG00000047842; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003577; GTPase_Ras.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR020849; Ras_small_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00173; RAS; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation.
FT   CHAIN         1    196       GTP-binding protein Di-Ras2.
FT                                /FTId=PRO_0000191652.
FT   PROPEP      197    199       Removed in mature form (Potential).
FT                                /FTId=PRO_0000370779.
FT   NP_BIND      14     21       GTP (By similarity).
FT   NP_BIND      33     39       GTP (By similarity).
FT   NP_BIND      61     65       GTP (By similarity).
FT   NP_BIND     121    124       GTP (By similarity).
FT   MOTIF        36     44       Effector region (Potential).
FT   MOD_RES     196    196       Cysteine methyl ester (Potential).
FT   LIPID       196    196       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   199 AA;  22498 MW;  C1A69D3145C3EACD CRC64;
     MPEQSNDYRV AVFGAGGVGK SSLVLRFVKG TFRESYIPTV EDTYRQVISC DKSICTLQIT
     DTTGSHQFPA MQRLSISKGH AFILVYSITS RQSLEELKPI YEQICEIKGD VESIPIMLVG
     NKCDESPNRE VQSSEAEALA RTWKCAFMET SAKLNHNVKE LFQELLNLEK RRTVSLQIDG
     KKSKQQKRKE KLKGKCVVM
//
ID   Q5PRE9_MOUSE            Unreviewed;      2387 AA.
AC   Q5PRE9;
DT   04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT   04-JAN-2005, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   SubName: Full=Ncor1 protein;
GN   Name=Ncor1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC086657; AAH86657.1; -; mRNA.
DR   IPI; IPI00551272; -.
DR   RefSeq; NP_035438.2; NM_011308.2.
DR   UniGene; Mm.271814; -.
DR   UniGene; Mm.460227; -.
DR   ProteinModelPortal; Q5PRE9; -.
DR   SMR; Q5PRE9; 434-487, 625-682.
DR   STRING; Q5PRE9; -.
DR   Ensembl; ENSMUST00000101067; ENSMUSP00000098628; ENSMUSG00000018501.
DR   GeneID; 20185; -.
DR   KEGG; mmu:20185; -.
DR   UCSC; uc007jix.1; mouse.
DR   CTD; 20185; -.
DR   MGI; MGI:1349717; Ncor1.
DR   HOVERGEN; HBG052587; -.
DR   Bgee; Q5PRE9; -.
DR   Genevestigator; Q5PRE9; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005667; C:transcription factor complex; IPI:MGI.
DR   GO; GO:0017053; C:transcriptional repressor complex; IPI:MGI.
DR   GO; GO:0035033; F:histone deacetylase regulator activity; IDA:MGI.
DR   GO; GO:0046965; F:retinoid X receptor binding; IDA:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0046966; F:thyroid hormone receptor binding; IDA:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; IGI:MGI.
DR   GO; GO:0016564; F:transcription repressor activity; IDA:MGI.
DR   GO; GO:0002361; P:CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; IMP:MGI.
DR   GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
DR   GO; GO:0032922; P:circadian regulation of gene expression; IGI:MGI.
DR   GO; GO:0060318; P:definitive erythrocyte differentiation; IMP:MGI.
DR   GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase cascade; IMP:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:MGI.
DR   GO; GO:0031065; P:positive regulation of histone deacetylation; IDA:MGI.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IGI:MGI.
DR   GO; GO:0021794; P:thalamus development; IMP:MGI.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR014778; Myb_DNA-bd.
DR   InterPro; IPR001005; SANT_DNA-bd.
DR   InterPro; IPR017884; SANT_eukarya.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Pfam; PF00249; Myb_DNA-binding; 1.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF46689; Homeodomain_like; 2.
DR   PROSITE; PS51293; SANT; 2.
PE   2: Evidence at transcript level;
KW   Nucleus.
SQ   SEQUENCE   2387 AA;  264125 MW;  70C0E85EEBB5E63F CRC64;
     MSSSGYPPNQ GAFSTEQSRY PSHSVQYTFP STRHQQEFAV PDYRSSHIEV SQASQLLQQQ
     QQQQQLRRRP SLLSEFHPGS DRPQERRTGY EQFHSGPSPV DHDSLESKRP RLEPVSDAHF
     QRVSAAVLPL VHSLPEGLRS SADAKKDSAF GSKHEAPSSP LAGQPCGDDQ NASPSKLSKE
     ELIQSMDRVD REIAKVEQQI LKLKKKQQQL EEEAAKPPEP EKPVSPPPVE QKHRSIVQII
     YDENRKKAEE AHKIFEGLGP KVELPLYNQP SDTKVYHENI KTNQVMRKKL ILFFKRRNHA
     RKQREQKICQ RYDQLMEAWE KKVDRIENNP RRKAKESKTR EYYEKQFPEI RKQREQQERF
     QRVGQRGAGL SATIARSEHE ISEIIDGLSE QENNEKQMRQ LSVIPPMMFD AEQRRVKFIN
     MNGLMEDPMK VYKDRQFMNV WTDHEKEIFK DKFIQHPKNF GLIASYLERK SVPDCVLYYY
     LTKKNENYKA LVRRNYGKRR GRNQQIARPS QEEKVEEKEE DKAEKTEKKE EEKKDDEEKD
     DKEDSKETTK EKDRTEATAE EPEEREQVTP RGRKTANSQG RRKGRVTRSM TSEAAAANAA
     AAATEEPPPP LPPPPEPIST EPVETSRWTE EEMEVAKKGL VEHGRNWAAI AKMVGTKSEA
     QCKNFYFNYK RRHNLDNLLQ QHKQKVSRAV VASRKPREER DVSQCESVAS TVSAQEDEDI
     EASNEEENPE DSEAVPTTKP AERESVEAQV TDSASAETAE PMDVDHEECG AEGSSVLDPP
     APTKADSVDP EMQVPENTAS KGEGDAKERD LESTSEKTEA RDEDVVVAEQ IERPEPQSDD
     DSSATCSADE GVDGEPERQR VFPMDAKPSL LTPPGSILIS SPIKPNPLDL PQLQHRAAVI
     PPMVSCTPCN IPIGTPVSGY ALYQRHIKAM HESALLEEQR QRQEQVDLEC RSSTSPCSTS
     KSPNREWEVL QPAPHQVITN LPEGVRLPTT RPTRPPPPLI PSSKTTVASE KPSFIMGGSI
     SQGTPGTYLS SHNQAYPQEA PKPSVGSISL GLPRQQESTK AAPLTYIKQE EFSPRSQNSQ
     PEGLLVRAQH EGTAGAVQEG SITRGTPASK ISVETISSLR GSITQGTPAL PQAGIPTEAL
     VKGPVSRMPI EESSPEKVRE EAASKGHVIY EGKSGHILSY DNIKNAREGT RSPRTAHEMS
     LKRSYEAVEG SIKQGLICRA LPRGSPHSDL KERTVLSGSI MQGTPRATAE SFEDGLKYPK
     QIKRESPPIR AFEGAITKGK PYDGITTIKE MGRSIHEIPR QDILTQESRK TPEVVQSTRP
     IIEGSISQGT PIKFDNNSGQ SAIKHNVKSL ITGPSKLPRG MLEIVPENIK VVERGKYEDV
     KAGEPVRARH TSVVSSGPSV LRSTLHEAPK AQLSPGLYDD SSARRTPVSY QNTISRGSPM
     MNRTSDVSSS KSASHERKST LTPTQRESIP AKSPVPGVDP VVSHSPFDPH HRSSAAGEVY
     RSHLPTHLDP AMPFHRALDP AAAAYLLQRQ LSPTPGYPSQ YQLYAMENTR QTILNDYITS
     QQMQVNLRPD VTRGLSPREQ PLGLPYPATR GIIDLTNMPP TILVPHAGGT STPPMDRITY
     IPGTQVTFPP RPYNAASLSP GHPTHLAAAA SAERERERER EKERERERER ERERERERIA
     AAPADLYLRP GSEQPGRPGS HGYVRSPSPS VRTQETILQQ RPSVFQGTNG TSVITPLDPT
     AQLRIMPLPS GGPSISQGLP ASRYNTAADA LAALVDAAAS APQMDVSKTK ESKHEAARLE
     ENLRSRSAAV SEQQQLEQKN LEVEKRSVQC VCTSSALPSG KAQPHASVVY SEAGKDKGPP
     PKSRYEEELR TRGKTTITAA NFIDVIITRQ IASDKDARER GSQSSDSSSS LSSHRYETAS
     DAIEVISPAS SPAPPQEKPQ AYQPDMVKAN QAENESTRQY EGPLHHYRSQ QESPSPQQQP
     PLPPSSQSEG MGQVPRTHRL ITLADHICQI ITQDFARNQV PSQPSTSTFQ TSPSALSSTP
     VRTKTSSRYS PESQSQTVLH PRPGPRVSPE NLVDKSRGSR PGKSPERSHI PSEPYEPISP
     PQGPAVHEKQ DSMLLLSQRG VDPAEQRSDS RSPGSISYLP SFFTKLESTS PMVKSKKQEI
     FRKLNSSGGG DSDMAAAQPG TEIFNLPAVT TSGAVSSRSH SFADPASNLG LEDIIRKALM
     GSFDDKVEDH GVVMSHPVGI MPGSASTSVV TSSEARRDEG EPSPHAGVCK PKLINKSNSR
     KSKSPIPGQS YLGTERPSSV SSVHSEGDYH RQTPGWAWED RPSSTGSTQF PYNPLTIRML
     SSTPPTQIAC APSAITQAAP HQQNRIWERE PAPLLSAQYE TLSDSDD
//
ID   MDC1_MOUSE              Reviewed;        1707 AA.
AC   Q5PSV9; Q52KG1; Q5U4D3; Q6ZQH7;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Mediator of DNA damage checkpoint protein 1;
GN   Name=Mdc1; Synonyms=Kiaa0170;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], INTERACTION WITH H2AFX AND NBN, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=15611643;
RA   Lee A.C., Fernandez-Capetillo O., Pisupati V., Jackson S.P.,
RA   Nussenzweig A.;
RT   "Specific association of mouse MDC1/NFBD1 with NBS1 at sites of DNA-
RT   damage.";
RL   Cell Cycle 4:177-182(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 693-1707.
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438; SER-442; THR-444
RP   AND SER-918, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND SER-593, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Required for checkpoint mediated cell cycle arrest in
CC       response to DNA damage within both the S phase and G2/M phases of
CC       the cell cycle. May serve as a scaffold for the recruitment of DNA
CC       repair and signal transduction proteins to discrete foci of DNA
CC       damage marked by 'Ser-139' phosphorylation of histone H2AFX. Also
CC       required for downstream events subsequent to the recruitment of
CC       these proteins. These include phosphorylation and activation of
CC       the ATM, CHEK1/CHK1 and CHEK2/CHK2/CDS1 kinases, and stabilization
CC       of TP53 and apoptosis. ATM and CHEK2 may also be activated
CC       independently by a parallel pathway mediated by TP53BP1 (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with several proteins involved in the DNA
CC       damage response, although not all these interactions may be
CC       direct. Interacts with CHEK2/CHK2/CDS1, which requires ATM-
CC       mediated phosphorylation within the FHA domain of CHEK2. Interacts
CC       constitutively with the BRCA1-BARD1 complex, SMC1A and TP53BP1.
CC       Interacts with ATM and FANCD2, and these interactions are reduced
CC       upon DNA damage. Also interacts with the PRKDC complex, composed
CC       of XRCC6/KU70, XRCC5/KU80 and PRKDC/XRCC7. This interaction may be
CC       required for PRKDC autophosphorylation, which is essential for DNA
CC       double strand break (DSB) repair. When phosphorylated by ATM,
CC       interacts with RNF8 (via FHA domain). Interacts with CEP164. When
CC       phosphorylated, interacts with APTX (via FHA-like domain) (By
CC       similarity). Interacts with H2AFX, which requires phosphorylation
CC       of H2AFX. Interacts with the MRN complex, composed of
CC       MRE11A/MRE11, RAD50, and NBN.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Associated with chromatin.
CC       Relocalizes to discrete nuclear foci following DNA damage, this
CC       requires phosphorylation of H2AFX. Colocalizes with APTX at sites
CC       of DNA double-strand breaks (By similarity).
CC   -!- DOMAIN: Tandemly repeated BRCT domains are characteristic of
CC       proteins involved in DNA damage signaling. In MDC1, these repeats
CC       are required for localization to chromatin which flanks sites of
CC       DNA damage marked by 'Ser-139' phosphorylation of H2AFX (By
CC       similarity).
CC   -!- PTM: Phosphorylated upon exposure to ionizing radiation (IR),
CC       ultraviolet radiation (UV), and hydroxyurea (HU). Phosphorylation
CC       in response to IR requires ATM, NBN, and possibly CHEK2. Also
CC       phosphorylated during the G2/M phase of the cell cycle and during
CC       activation of the mitotic spindle checkpoint (By similarity).
CC   -!- SIMILARITY: Contains 2 BRCT domains.
CC   -!- SIMILARITY: Contains 1 FHA domain.
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DR   EMBL; AY826432; AAV85449.1; -; Genomic_DNA.
DR   EMBL; BC085140; AAH85140.1; -; mRNA.
DR   EMBL; BC094363; AAH94363.1; -; mRNA.
DR   EMBL; AK129074; BAC97884.1; -; mRNA.
DR   IPI; IPI00753701; -.
DR   RefSeq; NP_001010833.2; NM_001010833.2.
DR   UniGene; Mm.218511; -.
DR   ProteinModelPortal; Q5PSV9; -.
DR   SMR; Q5PSV9; 29-130, 1509-1703.
DR   STRING; Q5PSV9; -.
DR   PhosphoSite; Q5PSV9; -.
DR   PRIDE; Q5PSV9; -.
DR   Ensembl; ENSMUST00000082337; ENSMUSP00000080949; ENSMUSG00000061607.
DR   GeneID; 240087; -.
DR   KEGG; mmu:240087; -.
DR   UCSC; uc008cir.1; mouse.
DR   CTD; 240087; -.
DR   MGI; MGI:3525201; Mdc1.
DR   eggNOG; maNOG15866; -.
DR   GeneTree; ENSGT00600000084454; -.
DR   HOGENOM; HBG125625; -.
DR   HOVERGEN; HBG080567; -.
DR   InParanoid; Q5PSV9; -.
DR   OrthoDB; EOG43BMN6; -.
DR   NextBio; 384441; -.
DR   ArrayExpress; Q5PSV9; -.
DR   Bgee; Q5PSV9; -.
DR   CleanEx; MM_MDC1; -.
DR   Genevestigator; Q5PSV9; -.
DR   GermOnline; ENSMUSG00000061607; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   InterPro; IPR001357; BRCT.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR008984; SMAD_FHA_domain.
DR   Gene3D; G3DSA:2.60.200.20; FHA; 1.
DR   Pfam; PF00498; FHA; 1.
DR   SMART; SM00292; BRCT; 2.
DR   SMART; SM00240; FHA; 1.
DR   SUPFAM; SSF52113; BRCT; 2.
DR   SUPFAM; SSF49879; SMAD_FHA; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell cycle; Coiled coil; DNA damage; DNA repair; Nucleus;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1   1707       Mediator of DNA damage checkpoint protein
FT                                1.
FT                                /FTId=PRO_0000096318.
FT   DOMAIN       54    105       FHA.
FT   DOMAIN     1510   1588       BRCT 1.
FT   DOMAIN     1609   1700       BRCT 2.
FT   REGION        1    150       Interaction with CHEK2 (By similarity).
FT   REGION        2    222       Interaction with the MRN complex (By
FT                                similarity).
FT   COMPBIAS    995   1394       Pro-rich.
FT   MOD_RES     168    168       Phosphoserine.
FT   MOD_RES     176    176       Phosphoserine (By similarity).
FT   MOD_RES     298    298       Phosphoserine (By similarity).
FT   MOD_RES     300    300       Phosphothreonine (By similarity).
FT   MOD_RES     313    313       Phosphoserine (By similarity).
FT   MOD_RES     315    315       Phosphothreonine (By similarity).
FT   MOD_RES     325    325       Phosphothreonine (By similarity).
FT   MOD_RES     360    360       Phosphoserine (By similarity).
FT   MOD_RES     362    362       Phosphothreonine (By similarity).
FT   MOD_RES     385    385       Phosphoserine (By similarity).
FT   MOD_RES     387    387       Phosphothreonine (By similarity).
FT   MOD_RES     398    398       Phosphoserine (By similarity).
FT   MOD_RES     438    438       Phosphoserine.
FT   MOD_RES     442    442       Phosphoserine.
FT   MOD_RES     444    444       Phosphothreonine.
FT   MOD_RES     492    492       Phosphoserine (By similarity).
FT   MOD_RES     504    504       Phosphoserine (By similarity).
FT   MOD_RES     593    593       Phosphoserine.
FT   MOD_RES     607    607       Phosphothreonine (By similarity).
FT   MOD_RES     609    609       Phosphothreonine (By similarity).
FT   MOD_RES     614    614       Phosphothreonine (By similarity).
FT   MOD_RES     732    732       Phosphoserine.
FT   MOD_RES     735    735       Phosphoserine (By similarity).
FT   MOD_RES     750    750       Phosphoserine (By similarity).
FT   MOD_RES     769    769       N6-acetyllysine (By similarity).
FT   MOD_RES     885    885       Phosphoserine (By similarity).
FT   MOD_RES     894    894       Phosphoserine (By similarity).
FT   MOD_RES     918    918       Phosphoserine.
FT   MOD_RES     991    991       Phosphoserine (By similarity).
FT   MOD_RES    1056   1056       Phosphothreonine (By similarity).
FT   MOD_RES    1212   1212       Phosphothreonine (By similarity).
FT   MOD_RES    1234   1234       Phosphothreonine (By similarity).
FT   MOD_RES    1352   1352       Phosphothreonine (By similarity).
FT   MOD_RES    1359   1359       Phosphoserine (By similarity).
FT   MOD_RES    1375   1375       Phosphothreonine (By similarity).
FT   CONFLICT    396    396       E -> EE (in Ref. 2; AAH94363).
SQ   SEQUENCE   1707 AA;  184670 MW;  F6ECCD30BBED265D CRC64;
     MESTQVIDWD AEEEEETELS SGSLGYSVEP IGQLRLFSGT HGPERDFPLY LGKNVVGRSP
     DCSVALPFPS ISKQHAVIEI SAWNKAPILQ DCGSLNGTQI VKPPRVLPPG VSHRLRDQEL
     ILFADFPCQY HRLDVPPPLV PRSLLTIEKT PRIRIESQNS RVLLAADSEE EGDFPSGRCV
     ANGQRNTASP SATVVPESDE EVSSPAPSVP GPSSPFGLGS DTDEEQGQQP GVEESSLADS
     SGAAGEAEQP EANGTTAGIQ AQPTEHKLKD TKVKKEAGRA GVSDGSVLER SPTLGEDSDT
     EVDEDHKPGF ADSETDVEEE RIPVTPPVAP VKKNQVLLAV GIGDPEAPGV AHLQDCLAGS
     GTDVEDKTAL DVPLERNHTP MVINSDTDEE EEEEEEVSAA LTLAHLKERG IGLWSRDPGA
     EEVKSQPQVL VEQSQSASGR DSDTDVEEES SGRKREIIPD SPMDVDEALT VTQPESQPPR
     RPNDADEYMD MSSPGSHLVV NQASFAVVGK TRAQVEEEVP GPSVILGEKH QVPLEGAQPP
     EEAWETAVQE GSSSPEAAAS VRPSQQPVAE DAGTECATAV SEQESTLEVR SQSGSPAAPV
     EQVVIHTDTS GDPTLPQREG AQTPTGRERE AHVGRTKSAK ECCDAEPEDL CLPATQCFVE
     GESQHPEAVQ SLENEPTQLF PCTLPQEPGP SHLSLQTPGA DTLDVPWEVL ATQPFCLREQ
     SETSELHEAH GSQPSLPREP PGHQHLVHTS PVHTELLRIE GREIQTVEKA MGIPKEMADR
     MTPEREPLER EIRGRTENSE RDVIGEELIQ GTKDREPKKV LARDSQRKEA DKDLEGNRES
     LEVEIEMSKD SQKRERKVEK PEPKREWEPA DLEVTPDRGV TEEGSHDQKG QIASLTLKPG
     VGVKDLEGLA SAPIITGSQA DGGKGDPLSP GRQQRGRLSC QTTPAGKASR GDPEPPDHCL
     FSSVPEASTQ SLLTSQSQKQ STPQPLFSTS SSEIPLPESL HTKPNVRPRR SSRMTPSPHS
     SAALKPNTTC PTNQPAASRP TSRPTRGRAN RSSTRTPELI VPVDPELQPS TSTEQPVIPK
     LTSQVTEGRV QMPEPLLTGP EIQSPTSTEQ SVTPDRKPRA TRGRPSKSPN KTPEPLISTG
     PELQPPTSIE QPVIPKPTSR VTRGRPRKSS VRTPESVVST GPELQPLTSI EQPVIPEPRA
     TRGRPSKSSI KTPESVVPTG PELQPLTSAK QPVTPNLTSR ASRGRSSKSI RTPEPVVQTG
     PEFHPSTSTE QPDTREPSSQ ARTRRSAVKT PEASVPTTPE LQPFTSKKQP APKPTALVTQ
     GRTYKPSTED CESVGPVAPD FEPSTSTDHL VTPKVTDQSL TLQSSPLSAS PVSSTPDLKP
     PVPIAQPVTP EPIPQANHQR KRRAAGKQGS RTVPLGHKSY SALSEPEPQS SASQSSGASE
     ADSPRQKRPR RQASQKTVVI KEEPVETEVK EEPQETAIPT PEKRKRDHAE EVTQGKPTRS
     RRTKPNQETA PKVLFTGVMD SRGERAVLAL GGSLASSVNE ASHLVTDRIR RTVKFLCALG
     KGIPILSLNW LYQSRKAGCF LPPDDYLVTD PEQEKNFSFS LRDSLCRARE RRLLEDYEIH
     VTPGVQPPPP QMGEIISCCG GTFLPSMPHS YKLHRVIITC TEDLPRCAIP SRLGLPLLSP
     EFLLTGVLKQ EATPEAFVLS NLEMSST
//
ID   OSBP2_MOUSE             Reviewed;         908 AA.
AC   Q5QNQ6; Q8CF21;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Oxysterol-binding protein 2;
GN   Name=Osbp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 462-908.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Binds 7-ketocholesterol (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the OSBP family.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AL691413; CAI25066.1; -; Genomic_DNA.
DR   EMBL; AL731853; CAI25066.1; JOINED; Genomic_DNA.
DR   EMBL; AL731853; CAI51858.1; -; Genomic_DNA.
DR   EMBL; AL691413; CAI51858.1; JOINED; Genomic_DNA.
DR   EMBL; AK007088; BAC25163.1; -; mRNA.
DR   IPI; IPI00453962; -.
DR   RefSeq; NP_690031.2; NM_152818.2.
DR   UniGene; Mm.61022; -.
DR   ProteinModelPortal; Q5QNQ6; -.
DR   SMR; Q5QNQ6; 180-275.
DR   STRING; Q5QNQ6; -.
DR   PRIDE; Q5QNQ6; -.
DR   Ensembl; ENSMUST00000070552; ENSMUSP00000068652; ENSMUSG00000020435.
DR   GeneID; 74309; -.
DR   KEGG; mmu:74309; -.
DR   UCSC; uc007htq.1; mouse.
DR   CTD; 74309; -.
DR   MGI; MGI:1921559; Osbp2.
DR   HOGENOM; HBG445378; -.
DR   HOVERGEN; HBG053374; -.
DR   InParanoid; Q5QNQ6; -.
DR   OMA; GEMACVY; -.
DR   OrthoDB; EOG49S65T; -.
DR   PhylomeDB; Q5QNQ6; -.
DR   NextBio; 340415; -.
DR   ArrayExpress; Q5QNQ6; -.
DR   Bgee; Q5QNQ6; -.
DR   CleanEx; MM_OSBP2; -.
DR   Genevestigator; Q5QNQ6; -.
DR   GermOnline; ENSMUSG00000020435; Mus musculus.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0008202; P:steroid metabolic process; IEA:InterPro.
DR   InterPro; IPR000648; Oxysterol-bd.
DR   InterPro; IPR018494; Oxysterol-bd_CS.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   PANTHER; PTHR10972; Oxysterol_bd; 1.
DR   Pfam; PF01237; Oxysterol_BP; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS01013; OSBP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Lipid transport; Lipid-binding; Membrane; Transport.
FT   CHAIN         1    908       Oxysterol-binding protein 2.
FT                                /FTId=PRO_0000223481.
FT   DOMAIN      179    271       PH.
SQ   SEQUENCE   908 AA;  101353 MW;  7CF33E2F411906D5 CRC64;
     MGKAAALSRG GGCAGRSRGL SSLFTVVPCL SCHTAAPGMN SSAFGSGPAS KPQLQPVQAP
     ERELLSKQVC QPISEPASRS EPGSQTTSVP RPSGVGQESE LQGLWPGSEN GTRSVSIIKA
     SPELAMPSPL QSTVGSLPVT KPESKLVPKT QSFLRQGQAK ISVGTPVSGI GVQMVSPPLD
     SYKGWLLKWT NYLKGYQRRW FVLGNGLLSY YRNQGEMAHT CRATINLAST HFETEDSCGI
     LLCNGARTYH LKASSEVDRQ HWITALELAK AKAIRVMKTQ SDDSGDDDEE PAAPADNSEL
     HHTLKTLSLK LNDLSTCNDL IAKHGAALQR SLNELDSLKI PSECGEKLKV VNERATLFRI
     TSNAMINACR DFLELAETHS RKWQRALNYE QEQRVHLEET IEQLAKQHNS LERAFCNTPG
     GPASSSKSFS EGSFLTSKGE NSEEDEDTEY FDAMEDSTSF ITVVTEAKED RKPESGPGTT
     TVDWTSADNV LDGASFMPKN SCKVKRRVRI PDKPNYSLNL WSIMKNCIGR ELSRIPMPVN
     FNEPLSMLQR LTEDLEYHHL LDKAVNCTSS VEQMCLVAAF SVSSYSTTVH RIAKPFNPML
     GETFELDRME DMGLRSLCEQ VSHHPPSAAH HVFSKHGWSL WQEITIASKF RGKYISIMPL
     GAIHLEFQAS GNHYVWRKST STVHNIIVGK LWIDQSGDIE IVNHKTKDRC QLKFVPYSYF
     SKEAARKVTG VVSDSQGKAH YVLSGSWDDQ MECSKIVHSS PSSDGRQKTV YQTLPAKLLW
     RKYPLPENAE NMYYFSELAL TLNEQEDGVA PTDSRLRPDQ RLMERGRWDE ANTEKQRLEE
     KQRLSRRRRL ESCTAGCGGE EEKESDGYVP LWFEKRLDPL TGEMACMYKG GYWEAKEKKD
     WHMCPNIF
//
ID   SMG7_MOUSE              Reviewed;        1138 AA.
AC   Q5RJH6; Q63ZW5; Q6ZQF3;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Protein SMG7;
DE   AltName: Full=EST1-like protein C;
DE   AltName: Full=SMG-7 homolog;
GN   Name=Smg7; Synonyms=Est1c, Kiaa0250;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Embryonic germ cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Plays a role in nonsense-mediated mRNA decay. Recruits
CC       RENT1 to cytoplasmic mRNA decay bodies (By similarity).
CC   -!- SUBUNIT: Part of a complex that contains SMG5, SMG7, PPP2CA, a
CC       short isoform of UPF3A and phosphorylated UPF1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Predominantly cytoplasmic, and nuclear. Shuttles
CC       between nucleus and cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5RJH6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5RJH6-2; Sequence=VSP_016577;
CC       Name=3;
CC         IsoId=Q5RJH6-3; Sequence=VSP_016578, VSP_016579;
CC   -!- SIMILARITY: Contains 2 TPR repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97911.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK129101; BAC97911.1; ALT_INIT; mRNA.
DR   EMBL; BC082789; AAH82789.1; -; mRNA.
DR   EMBL; BC086651; AAH86651.1; -; mRNA.
DR   IPI; IPI00420598; -.
DR   IPI; IPI00471242; -.
DR   IPI; IPI00678743; -.
DR   RefSeq; NP_001005507.1; NM_001005507.2.
DR   RefSeq; NP_001153728.1; NM_001160256.1.
DR   RefSeq; NP_001153729.1; NM_001160257.1.
DR   UniGene; Mm.270775; -.
DR   ProteinModelPortal; Q5RJH6; -.
DR   SMR; Q5RJH6; 1-496.
DR   STRING; Q5RJH6; -.
DR   PhosphoSite; Q5RJH6; -.
DR   PRIDE; Q5RJH6; -.
DR   Ensembl; ENSMUST00000043560; ENSMUSP00000041241; ENSMUSG00000042772.
DR   Ensembl; ENSMUST00000073441; ENSMUSP00000073144; ENSMUSG00000042772.
DR   Ensembl; ENSMUST00000111836; ENSMUSP00000107467; ENSMUSG00000042772.
DR   GeneID; 226517; -.
DR   KEGG; mmu:226517; -.
DR   UCSC; uc007czn.1; mouse.
DR   UCSC; uc007czo.1; mouse.
DR   UCSC; uc007czp.1; mouse.
DR   CTD; 226517; -.
DR   MGI; MGI:2682334; Smg7.
DR   GeneTree; ENSGT00560000077120; -.
DR   HOVERGEN; HBG056330; -.
DR   OMA; FGPIGTP; -.
DR   OrthoDB; EOG4X97GD; -.
DR   NextBio; 378192; -.
DR   PMAP-CutDB; Q5RJH6; -.
DR   ArrayExpress; Q5RJH6; -.
DR   Bgee; Q5RJH6; -.
DR   Genevestigator; Q5RJH6; -.
DR   GermOnline; ENSMUSG00000042772; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:HGNC.
DR   GO; GO:0005634; C:nucleus; ISS:HGNC.
DR   GO; GO:0051721; F:protein phosphatase 2A binding; ISS:HGNC.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR   InterPro; IPR019458; EST1.
DR   InterPro; IPR011990; TPR-like_helical.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
DR   Pfam; PF10374; EST1; 1.
DR   PROSITE; PS50005; TPR; FALSE_NEG.
DR   PROSITE; PS50293; TPR_REGION; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Nonsense-mediated mRNA decay;
KW   Nucleus; Phosphoprotein; Repeat; TPR repeat.
FT   CHAIN         1   1138       Protein SMG7.
FT                                /FTId=PRO_0000076325.
FT   REPEAT      152    185       TPR 1.
FT   REPEAT      187    219       TPR 2.
FT   COMPBIAS    599    794       Gln/Pro-rich.
FT   COMPBIAS    923   1016       Ser-rich.
FT   MOD_RES     519    519       Phosphoserine (By similarity).
FT   MOD_RES     732    732       Phosphoserine.
FT   MOD_RES     848    848       Phosphoserine (By similarity).
FT   VAR_SEQ       1      9       MSLQSAQYL -> MRTENLKSEEHLKSSNI (in
FT                                isoform 2).
FT                                /FTId=VSP_016577.
FT   VAR_SEQ     566    566       V -> VRRDCSKGVTVTQEDGQKDSSKRRAETKRCTLGKLQ
FT                                ETGKQSVAVQV (in isoform 3).
FT                                /FTId=VSP_016578.
FT   VAR_SEQ     866    915       Missing (in isoform 3).
FT                                /FTId=VSP_016579.
FT   CONFLICT    552    552       P -> S (in Ref. 1; BAC97911).
SQ   SEQUENCE   1138 AA;  126841 MW;  330576E241E35AD4 CRC64;
     MSLQSAQYLR QAEVLKAEMT DSKLGPAEVW TSRQALQDLY QKMLVTDLEY ALDKKVEQDL
     WNHAFKNQIT TLQGQAKNRA NPNRSEVQAN LSLFLEAASG FYTQLLQELC TVFNVDLPCR
     VKSSQLGIIS NKQTHSSTIV KPQSSSCSYI CQHCLVHLGD IARYRNQTSQ AESYYRHAAQ
     LVPSNGQPYN QLAILASSKG DHLTTIFYYC RSIAVKFPFP AASTNLQKAL SKALESRDEL
     KTKWGVSDFI KAFIKFHGHV YLSKSLEKLS PLREKLEEQF KRLLFQKAFN SQQLVHVTVI
     NLFQLHHLRD FSNETEQHSY SQDEQLCWTQ LLALFMSFLG ILCKCPLQND SQESNNAYPL
     PAVKVSMDWL RLRPRVFQEA VVDERQYIWP WLISLLNSFH PREDDLSNTN ATPLPEEFEL
     QGFLALRPSF RNLDFSKGHQ GITGDKEGQQ RRIRQQRLIS IGKWIADNQP RLIQCENEVG
     KLLFITEIPE LILEDPSEAK ENLILQETSV VESLATDGSP GLKSVLSTGR NPSNSCDSGE
     KPVVTFKENI KPREVNQGRS FPPKEVKSQT ELRKTPVSEA RKTPVTQTPS QTSNSQFIPI
     HHPGAFPPLP SRPGFPPPTY VIPPPVAFSM GSGYTFPAGV SVPGTFLQST AHSPAGNQVQ
     AGKQSHIPYS QQRPSGPGPM NQGPQQSQPP SQPPLTSLPA QPTAQSTSQL QVQALAQQQQ
     SPTKVIPALG KSPPHHSGFQ QYQQADASKQ LWNPPQVQSP LGKIMPVKQS YYLQTQDPIK
     LFEPSLQPPV IQQQPLEKKM KPFPMEPYNH NPSEVKVPEF YWDSSYSMAD NRAVMAQQPN
     MDRRSKRSPG VFRPEQDPVP RMPFEDPKSS PLLPPDLLKS LAALEEEEEL IFSNPPDLYP
     ALLGPLASLP GRSLFKSLLE KPSELMSHSS SFLSLTGFSV NQERYPNSSM FNEVYGKNLT
     TSSKAELNPS VASQETSLYS LFEGTPWSPS LPASSDHSTP ASQSPHSSNP SSLPSSPPTH
     NHNSAPFSNF GPIGTPDNRD RRPADRWKTD KPAMGGFGVD YLSATSSSES SWHQASTPSG
     TWTGHGPSME DSSAVLMESL KSIWSSSMMH PGPSALEQLL MQQKQKQQRG QGAMNPPH
//
ID   BRSK1_MOUSE             Reviewed;         778 AA.
AC   Q5RJI5; Q699J6;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=BR serine/threonine-protein kinase 1;
DE            EC=2.7.11.1;
DE   AltName: Full=Serine/threonine-protein kinase SAD-B;
GN   Name=Brsk1; Synonyms=Gm1100;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=15705853; DOI=10.1126/science.1107403;
RA   Kishi M., Pan Y.A., Crump J.G., Sanes J.R.;
RT   "Mammalian SAD kinases are required for neuronal polarization.";
RL   Science 307:929-932(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Required for the polarization of forebrain neurons which
CC       endows axons and dendrites with distinct properties, possibly by
CC       locally regulating phosphorylation of microtubule-associated
CC       proteins. May be involved in the regulation of G2/M arrest in
CC       response to UV- or methyl methane sulfonate (MMS)-induced, but not
CC       IR-induced, DNA damage. Phosphorylates WEE1 and CDC25B in vitro
CC       and CDC25C in vitro and in vivo (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activated by phosphorylation on Thr-189 by
CC       STK11 in complex with STE20-related adapter-alpha (STRAD alpha)
CC       pseudo kinase and CAB39 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Nuclear in the absence of DNA damage.
CC       Translocated to the nucleus in response to UV- or MMS-induced DNA
CC       damage (By similarity).
CC   -!- TISSUE SPECIFICITY: Present in the gray matter of the brain and
CC       spinal cord (at protein level). Expressed in the nervous system,
CC       distributed within the brain and spinal cord of embryonic and
CC       postnatal animals.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. AMPK subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 UBA domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY533671; AAT08446.1; -; mRNA.
DR   EMBL; BC086636; AAH86636.1; -; mRNA.
DR   IPI; IPI00515701; -.
DR   RefSeq; NP_001003920.2; NM_001003920.3.
DR   RefSeq; NP_001162044.1; NM_001168572.1.
DR   UniGene; Mm.297064; -.
DR   HSSP; P06782; 2EUE.
DR   ProteinModelPortal; Q5RJI5; -.
DR   SMR; Q5RJI5; 27-290.
DR   IntAct; Q5RJI5; 1.
DR   STRING; Q5RJI5; -.
DR   PhosphoSite; Q5RJI5; -.
DR   PRIDE; Q5RJI5; -.
DR   Ensembl; ENSMUST00000048248; ENSMUSP00000039517; ENSMUSG00000035390.
DR   GeneID; 381979; -.
DR   KEGG; mmu:381979; -.
DR   UCSC; uc009eyf.1; mouse.
DR   CTD; 381979; -.
DR   MGI; MGI:2685946; Brsk1.
DR   eggNOG; roNOG10787; -.
DR   GeneTree; ENSGT00570000078909; -.
DR   HOGENOM; HBG715635; -.
DR   HOVERGEN; HBG007240; -.
DR   InParanoid; Q5RJI5; -.
DR   OMA; DEKNGAQ; -.
DR   OrthoDB; EOG479F6K; -.
DR   PhylomeDB; Q5RJI5; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 402808; -.
DR   ArrayExpress; Q5RJI5; -.
DR   Bgee; Q5RJI5; -.
DR   CleanEx; MM_BRSK1; -.
DR   Genevestigator; Q5RJI5; -.
DR   GermOnline; ENSMUSG00000035390; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0030010; P:establishment of cell polarity; IGI:MGI.
DR   GO; GO:0031572; P:G2/M transition DNA damage checkpoint; ISS:UniProtKB.
DR   GO; GO:0030182; P:neuron differentiation; IGI:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0009411; P:response to UV; ISS:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    778       BR serine/threonine-protein kinase 1.
FT                                /FTId=PRO_0000260829.
FT   DOMAIN       34    285       Protein kinase.
FT   DOMAIN      314    356       UBA.
FT   NP_BIND      40     48       ATP (By similarity).
FT   COMPBIAS    492    540       Pro-rich.
FT   ACT_SITE    156    156       Proton acceptor (By similarity).
FT   BINDING      63     63       ATP (By similarity).
FT   MOD_RES     189    189       Phosphothreonine (By similarity).
FT   MOD_RES     193    193       Phosphoserine (By similarity).
FT   MOD_RES     447    447       Phosphoserine (By similarity).
FT   MOD_RES     508    508       Phosphoserine (By similarity).
FT   MOD_RES     563    563       Phosphoserine (By similarity).
FT   CONFLICT     23     24       Missing (in Ref. 1; AAT08446).
SQ   SEQUENCE   778 AA;  85155 MW;  A35C86293A958D99 CRC64;
     MSSGSKEGGG GSPAYHLPHP HPHPPQHAQY VGPYRLEKTL GKGQTGLVKL GVHCITGQKV
     AVKIVNREKL SESVLMKVER EIAILKLIEH PHVLKLHDVY ENKKYLYLVL EHVSGGELFD
     YLVKKGRLTP KEARKFFRQI VSALDFCHSY SICHRDLKPE NLLLDEKNNI RIADFGMASL
     QVGDSLLETS CGSPHYACPE VIKGEKYDGR RADMWSCGVI LFALLVGALP FDDDNLRQLL
     EKVKRGVFHM PHFIPPDCQS LLRGMIEVEP EKRLSLEQIQ KHPWYLGGKH EPDPCLEPAP
     GRRVAMRSLP SNGELDPDVL ESMASLGCFR DRERLHRELR SEEENQEKMI YYLLLDRKER
     YPSCEDQDLP PRNDVDPPRK RVDSPMLSRH GKRRPERKSM EVLSITDAGS GGSPVPTRRA
     LEMAQHSQRS RSVSGASTGL SSSPLSSPRS PVFSFSPEPG AGDEARGGGS PTSKTQTLPS
     RGPRGGGAGE QPPPPSARST PLPGPPGSPR SSGGTPLHSP LHTPRASPTG TPGTTPPPSP
     GGGVGGAAWR SRLNSIRNSF LGSPRFHRRK MQVPTAEEMS SLTPESSPEL AKRSWFGNFI
     SLDKEEQIFL VLKDKPLSSI KADIVHAFLS IPSLSHSVLS QTSFRAEYKA SGGPSVFQKP
     VRFQVDISSS EGPEPSPRRD GSSGGGIYSV TFTLISGPSR RFKRVVETIQ AQLLSTHDQP
     SVQALADEKN GAQTRPAGTP PRSLQPPPGR SDPDLSSSPR RGPPKDKKLL ATNGTPLP
//
ID   ISLR2_MOUSE             Reviewed;         745 AA.
AC   Q5RKR3; C8XPY9; Q6ZPQ3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Immunoglobulin superfamily containing leucine-rich repeat protein 2;
DE   AltName: Full=Leucine-rich repeat domain and immunoglobulin domain-containing axon extension protein;
DE   Flags: Precursor;
GN   Name=Islr2; Synonyms=Kiaa1465, Linx;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, INTERACTION WITH NTRK1,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=C57BL/6;
RX   PubMed=19755105; DOI=10.1016/j.neuron.2009.07.031;
RA   Mandai K., Guo T., StHillaire C., Meabon J.S., Kanning K.C.,
RA   Bothwell M., Ginty D.D.;
RT   "LIG family receptor tyrosine kinase-associated proteins modulate
RT   growth factor signals during neural development.";
RL   Neuron 63:614-627(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Required for axon extension during neural development.
CC   -!- SUBUNIT: Homomultimer. Interacts with NTRK1/TRKA.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: At E11.5, expressed in spinal nerves, their
CC       roots and the ventral spinal cord. At E12.5, detected in the
CC       ventral spinal cord, dorsal root ganglia (DRG), dorsal and ventral
CC       roots and sympathetic chain ganglia. At E12.5, expressed in almost
CC       all motor neurons which also express RET and in almost all DRG
CC       sensory neurons which also express NTRK1. At E18.5, expressed only
CC       in a subset of NTRK1-expressing neurons but still expressed in
CC       nearly all RET-expressing neurons.
CC   -!- DISRUPTION PHENOTYPE: Sensory and motor neuron axonal projection
CC       defects.
CC   -!- SIMILARITY: Contains 1 Ig-like (immunoglobulin-like) domain.
CC   -!- SIMILARITY: Contains 5 LRR (leucine-rich) repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98177.1; Type=Erroneous initiation;
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DR   EMBL; EU497918; ACC99423.1; -; mRNA.
DR   EMBL; AK129367; BAC98177.1; ALT_INIT; mRNA.
DR   EMBL; BC059068; AAH59068.1; -; mRNA.
DR   EMBL; BC096531; AAH96531.1; -; mRNA.
DR   IPI; IPI00420535; -.
DR   RefSeq; NP_001155007.1; NM_001161535.1.
DR   RefSeq; NP_001155008.1; NM_001161536.1.
DR   RefSeq; NP_001155009.1; NM_001161537.1.
DR   RefSeq; NP_001155010.1; NM_001161538.1.
DR   RefSeq; NP_001155011.1; NM_001161539.1.
DR   RefSeq; NP_001155012.1; NM_001161540.1.
DR   RefSeq; NP_001155013.1; NM_001161541.1.
DR   RefSeq; NP_796167.2; NM_177193.5.
DR   UniGene; Mm.186499; -.
DR   HSSP; Q9BZR6; 1OZN.
DR   ProteinModelPortal; Q5RKR3; -.
DR   SMR; Q5RKR3; 17-376.
DR   STRING; Q5RKR3; -.
DR   PRIDE; Q5RKR3; -.
DR   Ensembl; ENSMUST00000060035; ENSMUSP00000055604; ENSMUSG00000051243.
DR   Ensembl; ENSMUST00000114144; ENSMUSP00000109781; ENSMUSG00000051243.
DR   GeneID; 320563; -.
DR   KEGG; mmu:320563; -.
DR   UCSC; uc009pwl.1; mouse.
DR   CTD; 320563; -.
DR   MGI; MGI:2444277; Islr2.
DR   eggNOG; roNOG10011; -.
DR   GeneTree; ENSGT00600000084069; -.
DR   HOGENOM; HBG713685; -.
DR   HOVERGEN; HBG100863; -.
DR   InParanoid; Q5RKR3; -.
DR   OMA; PRLQWQL; -.
DR   OrthoDB; EOG4QC14W; -.
DR   PhylomeDB; Q5RKR3; -.
DR   NextBio; 396975; -.
DR   ArrayExpress; Q5RKR3; -.
DR   Bgee; Q5RKR3; -.
DR   Genevestigator; Q5RKR3; -.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0045773; P:positive regulation of axon extension; IMP:UniProtKB.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR000372; LRR-contain_N.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Pfam; PF00560; LRR_1; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00369; LRR_TYP; 1.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00013; LRRNT; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51450; LRR; 5.
PE   1: Evidence at protein level;
KW   Cell membrane; Developmental protein; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Leucine-rich repeat; Membrane; Neurogenesis;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     19       Potential.
FT   CHAIN        20    745       Immunoglobulin superfamily containing
FT                                leucine-rich repeat protein 2.
FT                                /FTId=PRO_0000317499.
FT   TOPO_DOM     20    589       Extracellular (Potential).
FT   TRANSMEM    590    610       Helical; (Potential).
FT   TOPO_DOM    611    745       Cytoplasmic (Potential).
FT   REPEAT       50     73       LRR 1.
FT   REPEAT       75     97       LRR 2.
FT   REPEAT       98    121       LRR 3.
FT   REPEAT      122    145       LRR 4.
FT   REPEAT      146    169       LRR 5.
FT   DOMAIN      233    372       Ig-like.
FT   CARBOHYD     52     52       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     73     73       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    121    121       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    338    338       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    365    365       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    474    474       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    563    563       N-linked (GlcNAc...) (Potential).
FT   DISULFID    260    356       By similarity.
FT   CONFLICT    460    460       G -> D (in Ref. 2; BAC98177).
SQ   SEQUENCE   745 AA;  79758 MW;  D224B2F1B6DE8B28 CRC64;
     MGPFGALCLA WALLGVVRAC PEPCACVDKY AHQFADCAYK ELREVPEGLP ANVTTLSLSA
     NKITVLRRGA FVNVTQVTSL WLAHSEVRTV ESGALAVLSQ LKNLDLSHNL ISNFPWSDLR
     NLSALQLLKM NHNRLGSLPR DALGALPDLR SLRINNNRLR TLEPGTFDAL SALSHLQLYH
     NPFHCSCGLV WLQAWAASTR VSLPEPDSIA CASPPELQGV PVHRLPALPC APPSVRLSAE
     PPPEAPGTPL RAGLAFMLHC VAEGHPTPRL QWQLQIPGGT VVLVPPVLSK EEDGGDKVED
     GEGDGDEDLP TQTEAPTPTP APAWPAPPAT PRFLALANGS LLVPLLSAKE AGIYTCRAHN
     ELGTNSTSLR VTVAAAGPPK HAPGTGEEPD AQVPTSERKA TTKGRSNSVL PFKPEGKTKG
     QGLARVSVLG EIEAELEETD EGEQMEGQIP ADPMGEKHCG HGDPSRYVSN HAFNQSSDLK
     PHVFELGVIA LDVAEREARV QLTPLAARWG PGPDGASGAR RPGRRPLRLL YLCPAGGGTA
     VQWSRVEEGV NAYWFRGLRP GTNYSVCLAL AGEACHVQVV FSTKKELPSL LVIVTVSVFL
     LVLATVPLLG AACCHLLAKH PGKPYRLILR PQAPDPMEKR IAADFDPRAS YLESEKSYPA
     RGEAGGEEPE EVPEEGLDED VEQGDPSGDL QREESLAGCS LVESQSKANQ EEFEAGSEYS
     DRLPLGAEAV NIAQEINGNY RQTAG
//
ID   Q5RL55_MOUSE            Unreviewed;       836 AA.
AC   Q5RL55;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 47.
DE   SubName: Full=ATP-binding cassette, sub-family F (GCN20), member 1;
GN   Name=Abcf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3;
RC   TISSUE=Mammary tumor. MMTV-LTR/INT3 model. 5 month old mouse. Taken by
RC   biopsy.;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
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DR   EMBL; BC046965; AAH46965.1; -; mRNA.
DR   IPI; IPI00762360; -.
DR   UniGene; Mm.329022; -.
DR   ProteinModelPortal; Q5RL55; -.
DR   STRING; Q5RL55; -.
DR   PRIDE; Q5RL55; -.
DR   Ensembl; ENSMUST00000043757; ENSMUSP00000036881; ENSMUSG00000038762.
DR   MGI; MGI:1351658; Abcf1.
DR   HOVERGEN; HBG050440; -.
DR   InParanoid; Q5RL55; -.
DR   PhylomeDB; Q5RL55; -.
DR   ArrayExpress; Q5RL55; -.
DR   Bgee; Q5RL55; -.
DR   Genevestigator; Q5RL55; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Nucleotide-binding.
SQ   SEQUENCE   836 AA;  94816 MW;  7BEB0B89E23622C0 CRC64;
     MPKGPKQQPP EPEWIGDGEG TSPADKVVKK GKKDKKTKKT FFEELAVEDK QAGEEEKLQK
     EKEQQQQQQQ QKKKRDTRKG RRKKDVDDDS DERVLMERLK QLSVPASDEE DEVPAPIPRG
     RKKAKGGNVF EALIQDDSEE EEEEEENRVL KPAKPEKNRI NKAVAEEPPG LRSKKGKEEK
     SKGKAKSKPA AADSEGEEEE DTAKEKEPPQ QGKDRDKKEA EQGSGEEKEE KEGDLKANDP
     YANLSKKEKK KLKKQMDYER QVESLKAANA AENDFSVSQA EVSSRQAMLE NASDIKLEKF
     SISAHGKELF VNADLYIVAG RRYGLVGPNG KGKTTLLKHI ANRALSIPPN IDVLLCEQEV
     VADETPAVQA VLRADTKRLR LLEEERRLQG QLEQGDDTAA EKLEKVYEEL RATGAAAAEA
     KARRILAGLG FDPEMQNRPT QKFSGGWRMR VSLARALFME PTLLMLDEPT NHLDLNAVIW
     LNNYLQGWRK TLLIVSHDQG FLDDVCTDII HLDTQRLHYY RGNYMTFKKM YQQKQKELLK
     QYEKQEKKLK ELKAGGKSTK QAEKQTKEVL TRKQQKCRRK NQDEESQEPP ELLKRPKEYT
     VRFTFPDPPP LSPPVLGLHG VTFGYEGQKP LFKNLDFGID MDSRICIVGP NGVGKSTLLL
     LLTGKLTPTN GEMRKNHRLK IGFFNQQYAE QLHMEETPTE YLQRSFNLPY QDARKCLGRF
     GLESHAHTIQ ICKLSGGQKA RVVFAELACR EPDVLILDEP TNNLDIESID ALGEAINDYK
     GAVIVVSHDA RLITETNCQL WVVEEQGVSQ IDGDFDDYKR EVLEALGEVM VNRPRD
//
ID   GRDN_MOUSE              Reviewed;        1873 AA.
AC   Q5SNZ0; Q5M6X2; Q5M6X4; Q5M6X5; Q5SNZ1; Q8C486; Q8CFU7;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Girdin;
DE   AltName: Full=Akt phosphorylation enhancer;
DE            Short=APE;
DE   AltName: Full=Coiled-coil domain-containing protein 88A;
DE   AltName: Full=G alpha-interacting vesicle-associated protein;
DE            Short=GIV;
DE   AltName: Full=Girders of actin filament;
DE   AltName: Full=Hook-related protein 1;
DE            Short=HkRP1;
GN   Name=Ccdc88a; Synonyms=Grdn, Kiaa1212;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH
RP   AKT1, AND TISSUE SPECIFICITY.
RC   TISSUE=Embryo;
RX   PubMed=15753085; DOI=10.1074/jbc.M500586200;
RA   Anai M., Shojima N., Katagiri H., Ogihara T., Sakoda H., Onishi Y.,
RA   Ono H., Fujishiro M., Fukushima Y., Horike N., Viana A., Kikuchi M.,
RA   Noguchi N., Takahashi S., Takata K., Oka Y., Uchijima Y., Kurihara H.,
RA   Asano T.;
RT   "A novel protein kinase B (PKB)/AKT-binding protein enhances PKB
RT   kinase activity and regulates DNA synthesis.";
RL   J. Biol. Chem. 280:18525-18535(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1086-1873 (ISOFORMS 2/3).
RC   STRAIN=C57BL/6; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1623-1873.
RC   STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   SUBUNIT, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15882442; DOI=10.1111/j.1600-0854.2005.00289.x;
RA   Simpson F., Martin S., Evans T.M., Kerr M., James D.E., Parton R.G.,
RA   Teasdale R.D., Wicking C.;
RT   "A novel hook-related protein family and the characterization of hook-
RT   related protein 1.";
RL   Traffic 6:442-458(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1560; THR-1561;
RP   SER-1562; SER-1677; SER-1704 AND SER-1840, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   REVIEW.
RX   PubMed=17185515; DOI=10.1196/annals.1377.016;
RA   Enomoto A., Ping J., Takahashi M.;
RT   "Girdin, a novel actin-binding protein, and its family of proteins
RT   possess versatile functions in the Akt and Wnt signaling pathways.";
RL   Ann. N. Y. Acad. Sci. 1086:169-184(2006).
RN   [8]
RP   FUNCTION, INTERACTION WITH DISC1 AND AKT PROTEINS, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=19778506; DOI=10.1016/j.neuron.2009.08.008;
RA   Kim J.Y., Duan X., Liu C.Y., Jang M.H., Guo J.U., Pow-anpongkul N.,
RA   Kang E., Song H., Ming G.L.;
RT   "DISC1 regulates new neuron development in the adult brain via
RT   modulation of AKT-mTOR signaling through KIAA1212.";
RL   Neuron 63:761-773(2009).
CC   -!- FUNCTION: Essential for the integrity of the actin cytoskeleton
CC       and for cell migration. Required for formation of actin stress
CC       fibers and lamellipodia. May be involved in membrane sorting in
CC       the early endosome (By similarity). Plays a role as a key
CC       modulator of the AKT-mTOR signaling pathway controlling the tempo
CC       of the process of newborn neurons integration during adult
CC       neurogenesis, including correct neuron positioning, dendritic
CC       development and synapse formation. Enhances phosphoinositide 3-
CC       kinase (PI3K)-dependent phosphorylation and kinase activity of
CC       AKT1/PKB, but does not possess kinase activity itself.
CC       Phosphorylation of AKT1/PKB thereby induces the phosphorylation of
CC       downstream effectors GSK3 and FOXO1/FKHR, and regulates DNA
CC       replication and cell proliferation.
CC   -!- SUBUNIT: Homodimer. The non-phosphorylated form interacts with
CC       phosphatidylinositol 4-phosphate [Pi(4)P] and weakly with
CC       phosphatidylinositol 3-phosphate [Pi(3)P] (By similarity).
CC       Interacts with microtubules. Interacts AKT1/PKB (via C-terminus).
CC       Interacts (via C-terminus) with DISC1; the interaction is direct.
CC       Interacts with AKT proteins; the interaction is inhibited in
CC       presence of DISC1.
CC   -!- SUBCELLULAR LOCATION: Membrane. Cell membrane. Cytoplasm, cytosol.
CC       Cytoplasmic vesicle. Cell projection, lamellipodium (By
CC       similarity). Note=Localizes to the cell membrane through
CC       interaction with phosphoinositides (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5SNZ0-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q5SNZ0-2; Sequence=VSP_052411;
CC       Name=3;
CC         IsoId=Q5SNZ0-3; Sequence=VSP_052410, VSP_052411;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in the dentate gyrus, pyramidal cell
CC       layer of hippocampal regions CA1 and CA3 at postnatal 15.
CC       Expressed highly in neurons. Weakly in neuron progenitors (at
CC       protein level). Expressed in the dentate granule cell layer of the
CC       hippocampus. Expressed highly in the adult testis, moderately in
CC       the brain and at a low level in the spleen, lungs and fat.
CC   -!- DEVELOPMENTAL STAGE: Temporally and spatially restricted during
CC       embryogenesis. At E10.5, expressed in the branchial arches, nasal
CC       processes, limbs, somites and dorsal root ganglia. At E11.5,
CC       expression persists at these sites in addition to the eye and
CC       fore-, mid- and hindbrain. By E12.5, expressed in the interdigital
CC       mesenchyme of the limbs. At E13.5, expression in the limbs flanks
CC       the digits and also appears in a subset of tendons in the hind-
CC       and forelimbs.
CC   -!- PTM: Phosphorylation is induced by epidermal growth factor (EGF)
CC       in a phosphoinositide 3-kinase (PI3K)-dependent manner.
CC       Phosphorylation by AKT1/PKB is necessary for the delocalization
CC       from the cell membrane and for cell migration (By similarity).
CC   -!- SIMILARITY: Belongs to the CCDC88 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH37020.1; Type=Erroneous initiation;
CC       Sequence=CAI24877.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
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DR   EMBL; AB087827; BAD98263.1; -; mRNA.
DR   EMBL; AL935054; CAI24877.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL935054; CAI24878.1; -; Genomic_DNA.
DR   EMBL; BX284634; CAI24878.1; JOINED; Genomic_DNA.
DR   EMBL; BX284634; CAI35999.1; -; Genomic_DNA.
DR   EMBL; BX284634; CAI36000.1; -; Genomic_DNA.
DR   EMBL; BX284634; CAI36001.1; -; Genomic_DNA.
DR   EMBL; AL935054; CAI36001.1; JOINED; Genomic_DNA.
DR   EMBL; BX284634; CAI36002.1; -; Genomic_DNA.
DR   EMBL; BC037020; AAH37020.1; ALT_INIT; mRNA.
DR   EMBL; AK082771; BAC38612.1; -; mRNA.
DR   IPI; IPI00461244; -.
DR   IPI; IPI00551498; -.
DR   IPI; IPI00648605; -.
DR   RefSeq; NP_789811.2; NM_176841.3.
DR   UniGene; Mm.338284; -.
DR   UniGene; Mm.441367; -.
DR   HSSP; P25054; 1DEB.
DR   ProteinModelPortal; Q5SNZ0; -.
DR   SMR; Q5SNZ0; 13-169.
DR   STRING; Q5SNZ0; -.
DR   PhosphoSite; Q5SNZ0; -.
DR   PRIDE; Q5SNZ0; -.
DR   Ensembl; ENSMUST00000040182; ENSMUSP00000048978; ENSMUSG00000032740.
DR   GeneID; 108686; -.
DR   KEGG; mmu:108686; -.
DR   UCSC; uc007igw.1; mouse.
DR   CTD; 108686; -.
DR   MGI; MGI:1925177; Ccdc88a.
DR   GeneTree; ENSGT00570000078853; -.
DR   HOVERGEN; HBG057867; -.
DR   OMA; EGTRARS; -.
DR   OrthoDB; EOG4W6NV4; -.
DR   PhylomeDB; Q5SNZ0; -.
DR   NextBio; 361223; -.
DR   Bgee; Q5SNZ0; -.
DR   CleanEx; MM_CCDC88A; -.
DR   Genevestigator; Q5SNZ0; -.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR   GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0043422; F:protein kinase B binding; IPI:UniProtKB.
DR   GO; GO:0032148; P:activation of protein kinase B activity; IDA:UniProtKB.
DR   GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR   GO; GO:0016044; P:cellular membrane organization; ISS:UniProtKB.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0042127; P:regulation of cell proliferation; IMP:UniProtKB.
DR   GO; GO:0006275; P:regulation of DNA replication; IMP:UniProtKB.
DR   GO; GO:0010975; P:regulation of neuron projection development; IDA:UniProtKB.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0031929; P:TOR signaling cascade; IDA:UniProtKB.
DR   InterPro; IPR008636; HOOK.
DR   Pfam; PF05622; HOOK; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cell projection; Coiled coil;
KW   Cytoplasm; Cytoplasmic vesicle; DNA replication; Membrane;
KW   Neurogenesis; Phosphoprotein.
FT   CHAIN         1   1873       Girdin.
FT                                /FTId=PRO_0000287430.
FT   REGION     1390   1408       Phosphoinositide-binding (By similarity).
FT   COILED      196    425       Potential.
FT   COILED      458   1232       Potential.
FT   COILED     1268   1385       Potential.
FT   MOD_RES    1387   1387       Phosphoserine (By similarity).
FT   MOD_RES    1417   1417       Phosphoserine; by PKB/AKT1 (By
FT                                similarity).
FT   MOD_RES    1560   1560       Phosphothreonine.
FT   MOD_RES    1561   1561       Phosphothreonine.
FT   MOD_RES    1562   1562       Phosphoserine.
FT   MOD_RES    1677   1677       Phosphoserine.
FT   MOD_RES    1704   1704       Phosphoserine.
FT   MOD_RES    1839   1839       Phosphoserine (By similarity).
FT   MOD_RES    1840   1840       Phosphoserine.
FT   VAR_SEQ    1000   1054       Missing (in isoform 3).
FT                                /FTId=VSP_052410.
FT   VAR_SEQ    1463   1491       MVALKRLPFLRNRPKDKDKMKACYRRSMS -> T (in
FT                                isoform 2 and isoform 3).
FT                                /FTId=VSP_052411.
FT   CONFLICT    952    952       Missing (in Ref. 2; CAI35999).
FT   CONFLICT   1086   1089       LQRQ -> PRVR (in Ref. 3; AAH37020).
SQ   SEQUENCE   1873 AA;  215918 MW;  0E827E3D9336161F CRC64;
     MENEIFTPLL EQFMTSPLVT WVKTFGPLAA GNGTNLDEYV ALVDGVFLNQ VMLQINPKSE
     SQRVNKKVNN DASLRIHNLS ILVKQIKFYY QETLQQLIMM PLPDILIIGK NPFSEQGTEE
     VKKLLLLLLG CAVQCQKKEE FIEKIQGLDF DTKAAVAAHI QEVTHNQENV FDLQWMEVTD
     MSQEDIEPLL KNMVSHLRRL IDERDEHSET IVELSEERDG VHFLPHASSS AQSPCGSPGM
     KRTESRQHLS VELADAKAKI RRLRQELEEK TEQLLDCKQE LEQIEVELKR LQQENMNLLS
     DARSARMYRD ELDALREKAV RVDKLESELS RYKERLHDIE FYKARVEELK EDNQVLLETK
     TMLEDQLEGT RARSDKLHEL EKENLQLKAK LHDMEMERDM DRKKIEELME ENMTLEMAQK
     QSMDESLHLG WELEQISRTS ELAEAPQKSL GHEVNELTSS KLLKLEMENQ SLTKTVEELR
     STADSAAGST SKILKVEKEN QRLNKKVEIL ENEIIQEKQS LQNCQNLSKD LMKEKAQLEK
     TIETLRENSE RQIKILEQEN EHLNQTVSSL RQRSQISAEA RVKDIEKENK ILHESIKETC
     GKLSKIEFEK RQMKKELELY KEKGERAEEL ENELNHLGKE NELLQKKITN LKITCEKLET
     LEQENSELER ENRKFKKTLD SFKNLTFQLE SLEKENSQLD EENLELRRSV ESLKCASMRM
     AQLQLENKEL ESEKEQLRKG LELMRASFKK TERLEVSYQG LDTENQRLQK ALENSNKKIQ
     QLESELQDLE MENQTLQKSL EELKISSKRL EQLEKENKSL EQETSQLEKD KKQLEKENKR
     LRQQAEIKDT TLEENNVKIG NLEKENKTLF KEINVYKESC VRLKELEKEN KELVKRATID
     IKTLVTLRED LVSEKLKTQQ MNNDLEKLTH ELEKIGLNKE RLLHDEQSTD DSRYKLLESK
     LESTLKKSLE IKEEKIAALE ARLEESTNYN QQLRHELKTV KKNYEALKQR QDEERMVQSS
     IPVSGEDDKW GRESQEATRE LLKVKDRLIE VERNNATLQA EKQALKTQLK QLETQNNNLQ
     AQILALQRQT VSLQEQNTTL QTQNAKLQVE NSTLNSQSTS LMNQNAQLLI QQSSLENENE
     SIMKEREDLK SLYDALIKDH EKLELLHERQ ASEYESLISK HGTLKSAHKN LEVEHKDLED
     RYNQLLKQKG QLEDLEKMIK TEQEKMLLES KNHEVVASEY KKLCGENDRL NYTYSQLLKE
     TEILQMDHKN LKSVLNNSKL EQTRLEAEFS KLKEQYQQLD ITSTKLNNQC ELLSQLKGNL
     EEENRHLLDQ IQTLMLQNRT LLEQNMESKD LFHVEQRQYI DKLNELRRQK EKLEEKIMDQ
     YKFYDPSPPR RRGNWITLKM RKLIKSKKDI NRERQKSLTL TPTRSDSSEG FLQLPHQDSQ
     DSSSVGSNSL EDGQTLGTKK SSMVALKRLP FLRNRPKDKD KMKACYRRSM SMNDLVQSMV
     LAGGQWTGST ENLEVPDDIS TGKRRKELGA MAFSTTAINF STVNSSAAFR SKQLVNNKDT
     TSFEDISPQG ISDDSSTGSR VHASRPASLD SGRTSTSNSN NNASLHEVKA GAVNIQSRPQ
     SHSSGDFSLL HDHETWSSSG SSPIQYLKRQ TRSSPMLQHK ISETIESRAH HKMKAGSPGS
     EVVTLQQFLE ESNKLTSIQL KSSSQENLLD EVMKSLSVSS DFLGKDKPVS CTLARSVSGK
     TPGDFYDRRT TKPEFLRTGP QKTEDAYTIS SAGKPTPSTQ GKIKLVKETS VSRQSKDSNP
     YATLPRASSV ISTAEGTTRR TSIHDFLSKD SRLPVSVDSS PPTAGSSSTT ASNVNKVQES
     RNSKSRSREQ QSS
//
ID   CC85A_MOUSE             Reviewed;         500 AA.
AC   Q5SP85; Q69Z68; Q6NZL9; Q8BGZ5; Q8BLC5; Q8VCC5;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Coiled-coil domain-containing protein 85A;
GN   Name=Ccdc85a; Synonyms=Kiaa1912;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 86-500 (ISOFORM 1).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5SP85-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SP85-2; Sequence=VSP_022283;
CC       Name=3;
CC         IsoId=Q5SP85-3; Sequence=VSP_022280, VSP_022283;
CC   -!- SIMILARITY: Belongs to the CCDC85 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC39790.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact. May result from internal priming due to genomic poly-A tracts;
CC       Sequence=BAC39795.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact. May result from internal priming due to genomic poly-A tracts;
CC       Sequence=BAD32576.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK173298; BAD32576.1; ALT_INIT; mRNA.
DR   EMBL; AK045568; BAC32419.1; -; mRNA.
DR   EMBL; AK087049; BAC39790.1; ALT_SEQ; mRNA.
DR   EMBL; AK087070; BAC39795.1; ALT_SEQ; mRNA.
DR   EMBL; AL929280; CAI25983.1; -; Genomic_DNA.
DR   EMBL; BX255910; CAI25983.1; JOINED; Genomic_DNA.
DR   EMBL; AL929280; CAI25984.1; -; Genomic_DNA.
DR   EMBL; BX255910; CAI25541.1; -; Genomic_DNA.
DR   EMBL; AL929280; CAI25541.1; JOINED; Genomic_DNA.
DR   EMBL; BC020949; AAH20949.1; -; mRNA.
DR   EMBL; BC066065; AAH66065.1; -; mRNA.
DR   IPI; IPI00222785; -.
DR   IPI; IPI00463395; -.
DR   IPI; IPI00816917; -.
DR   RefSeq; NP_001160133.1; NM_001166661.1.
DR   RefSeq; NP_001160134.1; NM_001166662.1.
DR   RefSeq; NP_853555.2; NM_181577.4.
DR   UniGene; Mm.93759; -.
DR   ProteinModelPortal; Q5SP85; -.
DR   STRING; Q5SP85; -.
DR   PhosphoSite; Q5SP85; -.
DR   PRIDE; Q5SP85; -.
DR   Ensembl; ENSMUST00000042534; ENSMUSP00000044649; ENSMUSG00000032878.
DR   Ensembl; ENSMUST00000093253; ENSMUSP00000090941; ENSMUSG00000032878.
DR   Ensembl; ENSMUST00000109502; ENSMUSP00000105128; ENSMUSG00000032878.
DR   GeneID; 216613; -.
DR   KEGG; mmu:216613; -.
DR   NMPDR; fig|10090.3.peg.23370; -.
DR   UCSC; uc007igk.1; mouse.
DR   UCSC; uc007igl.1; mouse.
DR   UCSC; uc007igm.1; mouse.
DR   CTD; 216613; -.
DR   MGI; MGI:2445069; Ccdc85a.
DR   eggNOG; roNOG09413; -.
DR   GeneTree; ENSGT00390000003531; -.
DR   HOGENOM; HBG713862; -.
DR   HOVERGEN; HBG060368; -.
DR   InParanoid; Q5SP85; -.
DR   OMA; DHHKHHA; -.
DR   OrthoDB; EOG4ZPDVW; -.
DR   NextBio; 375230; -.
DR   ArrayExpress; Q5SP85; -.
DR   Bgee; Q5SP85; -.
DR   CleanEx; MM_CCDC85A; -.
DR   Genevestigator; Q5SP85; -.
DR   InterPro; IPR019359; DUF2216_coiled-coil.
DR   Pfam; PF10226; DUF2216; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil.
FT   CHAIN         1    500       Coiled-coil domain-containing protein
FT                                85A.
FT                                /FTId=PRO_0000271105.
FT   COILED       38    104       Potential.
FT   COILED      132    171       Potential.
FT   COILED      404    429       Potential.
FT   COMPBIAS    219    369       His-rich.
FT   VAR_SEQ     179    206       Missing (in isoform 3).
FT                                /FTId=VSP_022280.
FT   VAR_SEQ     432    471       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_022283.
FT   CONFLICT    161    161       K -> E (in Ref. 2; BAC32419).
SQ   SEQUENCE   500 AA;  54483 MW;  550E0F41FAD59DEC CRC64;
     MSKAAGGSAP AAESCPSAPA GASTPTGVDD LSKVTDEELL QWSKEELIRS LRRAEAEKVS
     AMLDHSNLIR EVNRRLQLHL GEIRGLKDIN QKLQEDNQEL RDLCCFLDDD RQKGKRVSRE
     WQRLGRYTAG VMHKEVALYL QKLKELEVKQ EEVVKENMEL KELCMLLDEE KGVGCAGSRC
     SIDSQASLCQ LVASATPYVR DVGDGSSTSS TGSTDSPDHH KHHASGGSPE HLQKPRSEGS
     PEHTKHRSTS PEHLHKPRAS GTPDHSKALK GPSPEHHKPL CKGSPEQQRH PHPGSSPEVL
     PKHVLSGSPE HFQKHRPGGS PEHTRHSGGS PEHLQKHALG GSLEHLPRAR GTSPEHLKQH
     YGASPDHKHA SGSGGSGGGS REGTLRRPAQ EDSSSHHRNV YSGMNESTLS YVRQLEARVR
     QLEEENRMLP QGSFRLSSGA DGNNSSLNSP ASFSGHTTPS QQPEPVVHSL KVVWRKLGDA
     AGSCPGIRQH LSGNQYKGPM
//
ID   CYFP2_MOUSE             Reviewed;        1253 AA.
AC   Q5SQX6; Q3UH21; Q3UHS8; Q8BSW0; Q8CHA9; Q924D3; Q9R181;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=Cytoplasmic FMR1-interacting protein 2;
DE   AltName: Full=p53-inducible protein 121;
GN   Name=Cyfip2; Synonyms=Kiaa1168, Pir121;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH FMR1; FXR1 AND
RP   FXR2, AND SUBCELLULAR LOCATION.
RX   MEDLINE=21352978; PubMed=11438699; DOI=10.1073/pnas.151231598;
RA   Schenck A., Bardoni B., Moro A., Bagni C., Mandel J.-L.;
RT   "A highly conserved protein family interacting with the fragile X
RT   mental retardation protein (FMRP) and displaying selective
RT   interactions with FMRP-related proteins FXR1P and FXR2P.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:8844-8849(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, Kidney, and Pituitary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-367.
RX   MEDLINE=99380159; PubMed=10449408; DOI=10.1093/emboj/18.16.4424;
RA   Saller E., Tom E., Brunori M., Otter M., Estreicher A., Mack D.H.,
RA   Iggo R.;
RT   "Increased apoptosis induction by 121F mutant p53.";
RL   EMBO J. 18:4424-4437(1999).
RN   [6]
RP   RNA EDITING OF POSITION 320.
RX   PubMed=15731336; DOI=10.1093/nar/gki239;
RA   Levanon E.Y., Hallegger M., Kinar Y., Shemesh R., Djinovic-Carugo K.,
RA   Rechavi G., Jantsch M.F., Eisenberg E.;
RT   "Evolutionarily conserved human targets of adenosine to inosine RNA
RT   editing.";
RL   Nucleic Acids Res. 33:1162-1168(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-108, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Involved in T-cell adhesion and p53-dependent induction
CC       of apoptosis (By similarity). Does not bind RNA.
CC   -!- SUBUNIT: Interacts with FMR1, FXR1 AND FXR2. Component of the
CC       WAVE1 complex composed of ABI2, CYFIP2, C3orf10/HSPC300, NCKAP1
CC       and WASF1/WAVE1. CYFIP2 binds to activated RAC1 which causes the
CC       complex to dissociate, releasing activated WASF1. The complex can
CC       also be activated by NCK1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
CC       Cell junction, synapse, synaptosome. Note=Highly expressed in the
CC       perinuclear region. Enriched in synaptosomes.
CC   -!- RNA EDITING: Modified_positions=320; Note=Partially edited.
CC       Editing appears to be brain-specific.
CC   -!- SIMILARITY: Belongs to the CYFIP family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC41472.2; Type=Erroneous initiation;
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DR   EMBL; AF334144; AAK81821.1; -; mRNA.
DR   EMBL; AB093288; BAC41472.2; ALT_INIT; mRNA.
DR   EMBL; AK030397; BAC26942.1; -; mRNA.
DR   EMBL; AK147224; BAE27779.1; -; mRNA.
DR   EMBL; AK147586; BAE28010.1; -; mRNA.
DR   EMBL; AK147632; BAE28036.1; -; mRNA.
DR   EMBL; AL662806; CAI24844.2; -; Genomic_DNA.
DR   EMBL; AL713958; CAI24844.2; JOINED; Genomic_DNA.
DR   EMBL; AL713958; CAI25371.2; -; Genomic_DNA.
DR   EMBL; AL662806; CAI25371.2; JOINED; Genomic_DNA.
DR   EMBL; AF162472; AAD45803.1; -; mRNA.
DR   IPI; IPI00405625; -.
DR   RefSeq; NP_598530.2; NM_133769.2.
DR   UniGene; Mm.154358; -.
DR   STRING; Q5SQX6; -.
DR   PhosphoSite; Q5SQX6; -.
DR   PRIDE; Q5SQX6; -.
DR   Ensembl; ENSMUST00000093166; ENSMUSP00000090854; ENSMUSG00000020340.
DR   GeneID; 76884; -.
DR   KEGG; mmu:76884; -.
DR   CTD; 76884; -.
DR   MGI; MGI:1924134; Cyfip2.
DR   eggNOG; roNOG09488; -.
DR   HOVERGEN; HBG053209; -.
DR   InParanoid; Q5SQX6; -.
DR   OMA; EFHKQSF; -.
DR   OrthoDB; EOG4R7V8X; -.
DR   PhylomeDB; Q5SQX6; -.
DR   NextBio; 345997; -.
DR   ArrayExpress; Q5SQX6; -.
DR   Bgee; Q5SQX6; -.
DR   CleanEx; MM_CYFIP2; -.
DR   Genevestigator; Q5SQX6; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR   GO; GO:0019717; C:synaptosome; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0006915; P:apoptosis; ISS:UniProtKB.
DR   GO; GO:0016337; P:cell-cell adhesion; ISS:UniProtKB.
DR   InterPro; IPR008081; Cytoplasmic_FMR1-int.
DR   InterPro; IPR016536; Cytoplasmic_FMR1-int_sub.
DR   PANTHER; PTHR12195; FragX_IP; 1.
DR   Pfam; PF05994; FragX_IP; 1.
DR   PIRSF; PIRSF008153; FMR1_interacting; 1.
DR   PRINTS; PR01698; CYTOFMRPINTP.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Cell adhesion; Cell junction; Cytoplasm;
KW   Phosphoprotein; RNA editing; Synapse; Synaptosome.
FT   CHAIN         1   1253       Cytoplasmic FMR1-interacting protein 2.
FT                                /FTId=PRO_0000279710.
FT   MOD_RES     108    108       Phosphotyrosine.
FT   MOD_RES    1037   1037       N6-acetyllysine (By similarity).
FT   VARIANT     320    320       K -> E (in RNA edited version).
FT   CONFLICT     76     76       G -> V (in Ref. 3; BAC26942).
FT   CONFLICT    229    229       E -> G (in Ref. 3; BAE27779).
FT   CONFLICT    242    242       V -> A (in Ref. 3; BAE27779).
FT   CONFLICT    678    678       L -> P (in Ref. 3; BAC26942).
FT   CONFLICT   1080   1080       L -> P (in Ref. 3; BAC26942).
SQ   SEQUENCE   1253 AA;  145659 MW;  321011BF830F424E CRC64;
     MTTHVTLEDA LSNVDLLEEL PLPDQQPCIE PPPSSIMYQA NFDTNFEDRN AFVTGIARYI
     EQATVHSSMN EMLEEGHDYA VMLYTWRSCS RAIPQVKCNE QPNRVEIYEK TVEVLEPEVT
     KLMKFMYFQR KAIERFCSEV KRLCHAERRK DFVSEAYLLT LGKFINMFAV LDELKNMKCS
     VKNDHSAYKR AAQFLRKMAD PQSIQESQNL SMFLANHNRI TQCLHQQLEV IPGYEELLAD
     IVNICVDYYE NKMYLTPSEK HMLLKVMGFG LYLMDGNVSN IYKLDAKKRI NLSKIDKFFK
     QLQVVPLFGD MQIELARYIK TSAHYEENKS KWTCTQSSIS PQYNICEQMV QIRDDHIRFI
     SELARYSNSE VVTGSGLDSQ KSDEEYRELF DLALRGLQLL SKWSAHVMEV YSWKLVHPTD
     KFCNKDCPGT AEEYERATRY NYTSEEKFAF VEVIAMIKGL QVLMGRMESV FNQAIRNTIY
     AALQDFAQVT LREPLRQAVR KKKNVLISVL QAIRKTICDW EGGREPPNDP CLRGEKDPKG
     GFDIKVPRRA VGPSSTQLYM VRTMLESLIA DKSGSKKTLR SSLDGPIVLA IEDFHKQSFF
     FTHLLNISEA LQQCCDLSQL WFREFFLELT MGRRIQFPIE MSMPWILTDH ILETKEPSMM
     EYVLYPLDLY NDSAYYALTK FKKQFLYDEI EAEVNLCFDQ FVYKLADQIF AYYKAMAGSV
     LLDKRFRAEC KNYGVIIPYP PSNRYETLLK QRHVQLLGRS IDLNRLITQR ISAAMYKSLD
     QAISRFESED LTSIVELEWL LEINRLTHRL LCKHMTLDSF DAMFREANHN VSAPYGRITL
     HVFWELNFDF LPNYCYNGST NRFVRTAIPF TQEPQRDKPA NVQPYYLYGS KPLNIAYSHI
     YSSYRNFVGP PHFKTICRLL GYQGIAVVME ELLKIVKSLL QGTILQYVKT LIEVMPKICR
     LPRHEYGSPG ILEFFHHQLK DIIEYAELKT DVFQSLREVG NAILFCLLIE QALSQEEVCD
     LLHAAPFQNI LPRVYIKEGE RLEVRMKRLE AKYAPLHLVP LIERLGTPQQ IAIAREGDLL
     TKERLCCGLS MFEVILTRIR SYLQDPIWRG PPPTNGVMHV DECVEFHRLW SAMQFVYCIP
     VGTNEFTAEQ CFGDGLNWAG CSIIVLLGQQ RRFDLFDFCY HLLKVQRQDG KDEIIKNVPL
     KKMADRIRKY QILNNEVFAI LNKYMKSVET DSSTVEHVRC FQPPIHQSLA TTC
//
ID   Q5SQX7_MOUSE            Unreviewed;       947 AA.
AC   Q5SQX7;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 2.
DT   05-OCT-2010, entry version 36.
DE   SubName: Full=Cytoplasmic FMR1 interacting protein 2;
DE   Flags: Fragment;
GN   Name=Cyfip2; ORFNames=RP23-370F7.1-002;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Pearce A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL713958; CAI25370.2; -; Genomic_DNA.
DR   EMBL; AL662806; CAI25370.2; JOINED; Genomic_DNA.
DR   IPI; IPI00622497; -.
DR   UniGene; Mm.154358; -.
DR   STRING; Q5SQX7; -.
DR   Ensembl; ENSMUST00000093165; ENSMUSP00000090853; ENSMUSG00000020340.
DR   Ensembl; ENSMUST00000142017; ENSMUSP00000119801; ENSMUSG00000020340.
DR   MGI; MGI:1924134; Cyfip2.
DR   HOVERGEN; HBG053209; -.
DR   ArrayExpress; Q5SQX7; -.
DR   Bgee; Q5SQX7; -.
DR   Genevestigator; Q5SQX7; -.
DR   InterPro; IPR008081; Cytoplasmic_FMR1-int.
DR   PANTHER; PTHR12195; FragX_IP; 1.
DR   Pfam; PF05994; FragX_IP; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   947 AA;  109780 MW;  7B6F939B059E6947 CRC64;
     WTCTQSSISP QYNICEQMVQ IRDDHIRFIS ELARYSNSEV VTGSGLDSQK SDEEYRELFD
     LALRGLQLLS KWSAHVMEVY SWKLVHPTDK FCNKDCPGTA EEYERATRYN YTSEEKFAFV
     EVIAMIKGLQ VLMGRMESVF NQAIRNTIYA ALQDFAQVTL REPLRQAVRK KKNVLISVLQ
     AIRKTICDWE GGREPPNDPC LRGEKDPKGG FDIKVPRRAV GPSSTQACQW SPRALFHPTG
     GTQGRRGCRS LLYMVRTMLE SLIADKSGSK KTLRSSLDGP IVLAIEDFHK QSFFFTHLLN
     ISEALQQCCD LSQLWFREFF LELTMGRRIQ FPIEMSMPWI LTDHILETKE PSMMEYVLYP
     LDLYNDSAYY ALTKFKKQFL YDEIEAEVNL CFDQFVYKLA DQIFAYYKAM AGSVLLDKRF
     RAECKNYGVI IPYPPSNRYE TLLKQRHVQL LGRSIDLNRL ITQRISAAMY KSLDQAISRF
     ESEDLTSIVE LEWLLEINRL THRLLCKHMT LDSFDAMFRE ANHNVSAPYG RITLHVFWEL
     NFDFLPNYCY NGSTNRFVRT AIPFTQEPQR DKPANVQPYY LYGSKPLNIA YSHIYSSYRN
     FVGPPHFKTI CRLLGYQGIA VVMEELLKIV KSLLQGTILQ YVKTLIEVMP KICRLPRHEY
     GSPGILEFFH HQLKDIIEYA ELKTDVFQSL REVGNAILFC LLIEQALSQE EVCDLLHAAP
     FQNILPRVYI KEGERLEVRM KRLEAKYAPL HLVPLIERLG TPQQIAIARE GDLLTKERLC
     CGLSMFEVIL TRIRSYLQDP IWRGPPPTNG VMHVDECVEF HRLWSAMQFV YCIPVGTNEF
     TAEQCFGDGL NWAGCSIIVL LGQQRRFDLF DFCYHLLKVQ RQDGKDEIIK NVPLKKMADR
     IRKYQILNNE VFAILNKYMK SVETDSSTVE HVRCFQPPIH QSLATTC
//
ID   TM1L2_MOUSE             Reviewed;         507 AA.
AC   Q5SRX1; A0JP66; Q5SRX7; Q5SRY0; Q6P5D7; Q8C6J0; Q8C935; Q8CB51;
AC   Q8R4H1;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=TOM1-like protein 2;
DE   AltName: Full=Target of Myb-like protein 2;
GN   Name=Tom1l2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=21992818; PubMed=11997338; DOI=10.1101/gr.73702;
RA   Bi W., Yan J., Stankiewicz P., Park S.-S., Walz K., Boerkoel C.F.,
RA   Potocki L., Shaffer L.G., Devriendt K., Nowaczyk M.J.M., Inoue K.,
RA   Lupski J.R.;
RT   "Genes in a refined Smith-Magenis syndrome critical deletion interval
RT   on chromosome 17p11.2 and the syntenic region of the mouse.";
RL   Genome Res. 12:713-728(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 5).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Lung, Ovary, and Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Probable role in protein transport. May regulate growth
CC       factor-induced mitogenic signaling (By similarity).
CC   -!- SUBUNIT: Interacts with clathrin, SRC and TOLLIP (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q5SRX1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SRX1-2; Sequence=VSP_023396;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q5SRX1-3; Sequence=VSP_023397, VSP_023398;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q5SRX1-4; Sequence=VSP_023395, VSP_023399;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q5SRX1-5; Sequence=VSP_023393, VSP_023394;
CC         Note=May be produced at very low levels due to a premature stop
CC         codon in the mRNA, leading to nonsense-mediated mRNA decay. No
CC         experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed. Splicing pattern
CC       displays tissue specific variation.
CC   -!- DOMAIN: The GAT domain mediates interaction with TOLLIP (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the TOM1 family.
CC   -!- SIMILARITY: Contains 1 GAT domain.
CC   -!- SIMILARITY: Contains 1 VHS domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF467887; AAL77033.1; -; mRNA.
DR   EMBL; AK036788; BAC29576.1; -; mRNA.
DR   EMBL; AK043095; BAC31458.1; -; mRNA.
DR   EMBL; AK054531; BAC35813.1; -; mRNA.
DR   EMBL; AK166040; BAE38537.1; -; mRNA.
DR   EMBL; AL596090; CAI24070.1; -; Genomic_DNA.
DR   EMBL; AL669954; CAI24070.1; JOINED; Genomic_DNA.
DR   EMBL; AL596090; CAI24071.1; -; Genomic_DNA.
DR   EMBL; AL669954; CAI24071.1; JOINED; Genomic_DNA.
DR   EMBL; AL596090; CAI24072.1; -; Genomic_DNA.
DR   EMBL; AL669954; CAI24072.1; JOINED; Genomic_DNA.
DR   EMBL; AL669954; CAI25761.1; -; Genomic_DNA.
DR   EMBL; AL596090; CAI25761.1; JOINED; Genomic_DNA.
DR   EMBL; AL669954; CAI25762.1; -; Genomic_DNA.
DR   EMBL; AL596090; CAI25762.1; JOINED; Genomic_DNA.
DR   EMBL; AL669954; CAI25763.1; -; Genomic_DNA.
DR   EMBL; AL596090; CAI25763.1; JOINED; Genomic_DNA.
DR   EMBL; BC062947; AAH62947.2; -; mRNA.
DR   EMBL; BC127266; AAI27267.1; -; mRNA.
DR   IPI; IPI00322033; -.
DR   IPI; IPI00406886; -.
DR   IPI; IPI00409418; -.
DR   IPI; IPI00621485; -.
DR   IPI; IPI00648853; -.
DR   RefSeq; NP_001034181.1; NM_001039092.3.
DR   RefSeq; NP_001034182.1; NM_001039093.1.
DR   RefSeq; NP_694720.2; NM_153080.2.
DR   UniGene; Mm.218875; -.
DR   HSSP; O60784; 1ELK.
DR   ProteinModelPortal; Q5SRX1; -.
DR   SMR; Q5SRX1; 2-153, 182-311.
DR   PhosphoSite; Q5SRX1; -.
DR   PRIDE; Q5SRX1; -.
DR   Ensembl; ENSMUST00000063998; ENSMUSP00000069280; ENSMUSG00000000538.
DR   Ensembl; ENSMUST00000064019; ENSMUSP00000063414; ENSMUSG00000000538.
DR   Ensembl; ENSMUST00000095254; ENSMUSP00000092884; ENSMUSG00000000538.
DR   Ensembl; ENSMUST00000102682; ENSMUSP00000099743; ENSMUSG00000000538.
DR   Ensembl; ENSMUST00000102683; ENSMUSP00000099744; ENSMUSG00000000538.
DR   GeneID; 216810; -.
DR   KEGG; mmu:216810; -.
DR   UCSC; uc007jfq.1; mouse.
DR   CTD; 216810; -.
DR   MGI; MGI:2443306; Tom1l2.
DR   eggNOG; roNOG05310; -.
DR   GeneTree; ENSGT00600000084107; -.
DR   HOVERGEN; HBG025068; -.
DR   InParanoid; Q5SRX1; -.
DR   OMA; RSVQNAS; -.
DR   OrthoDB; EOG447FT4; -.
DR   PhylomeDB; Q5SRX1; -.
DR   NextBio; 375336; -.
DR   ArrayExpress; Q5SRX1; -.
DR   Bgee; Q5SRX1; -.
DR   CleanEx; MM_TOM1L2; -.
DR   Genevestigator; Q5SRX1; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR004152; GAT.
DR   InterPro; IPR014645; TOM1.
DR   InterPro; IPR002014; VHS.
DR   InterPro; IPR018205; VHS_subgroup.
DR   Gene3D; G3DSA:1.25.40.90; ENTH_VHS; 1.
DR   Pfam; PF03127; GAT; 1.
DR   Pfam; PF00790; VHS; 1.
DR   PIRSF; PIRSF036948; TOM1; 1.
DR   SMART; SM00288; VHS; 1.
DR   SUPFAM; SSF48464; ENTH_VHS; 1.
DR   PROSITE; PS50909; GAT; 1.
DR   PROSITE; PS50179; VHS; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1    507       TOM1-like protein 2.
FT                                /FTId=PRO_0000278791.
FT   DOMAIN       20    152       VHS.
FT   DOMAIN      219    307       GAT.
FT   MOTIF       329    334       Clathrin-binding.
FT   MOD_RES     160    160       Phosphoserine (By similarity).
FT   MOD_RES     164    164       Phosphothreonine (By similarity).
FT   MOD_RES     192    192       Phosphotyrosine (By similarity).
FT   MOD_RES     200    200       Phosphotyrosine (By similarity).
FT   MOD_RES     404    404       Phosphotyrosine (By similarity).
FT   MOD_RES     479    479       Phosphoserine.
FT   VAR_SEQ     260    286       ELNRTCRAMQHRIVELISRVSNEEVTE -> VFQVCPSTAH
FT                                ESNRETCELLVWRFLEK (in isoform 5).
FT                                /FTId=VSP_023393.
FT   VAR_SEQ     287    507       Missing (in isoform 5).
FT                                /FTId=VSP_023394.
FT   VAR_SEQ     427    450       IPVAQPSVMDDIEVWLRTDLKGDD -> EMYGNACLSAWQG
FT                                RRRLPGPPGLE (in isoform 4).
FT                                /FTId=VSP_023395.
FT   VAR_SEQ     427    446       Missing (in isoform 2).
FT                                /FTId=VSP_023396.
FT   VAR_SEQ     427    440       IPVAQPSVMDDIEV -> VGLHTCVLPTVFWR (in
FT                                isoform 3).
FT                                /FTId=VSP_023397.
FT   VAR_SEQ     441    507       Missing (in isoform 3).
FT                                /FTId=VSP_023398.
FT   VAR_SEQ     451    507       Missing (in isoform 4).
FT                                /FTId=VSP_023399.
FT   CONFLICT     42     42       E -> K (in Ref. 4; AAH62947).
FT   CONFLICT    131    131       S -> G (in Ref. 2; BAC29576).
FT   CONFLICT    414    414       A -> T (in Ref. 1; AAL77033).
FT   CONFLICT    418    418       D -> G (in Ref. 2; BAC31458).
SQ   SEQUENCE   507 AA;  55663 MW;  BE1A56C6EFEE7F25 CRC64;
     MEFLLGNPFS TPVGQCLEKA TDGSLQSEDW TLNMEICDII NETEEGPKDA IRALKKRLSG
     NRNYREVMLA LTVLETCVKN CGHRFHLLVA NRDFIDSVLV KIISPKNNPP TIVQDKVLAL
     IQAWADAFRS SPDLTGVVHI YEELKRRGIE FPMADLDALS PIHTPQRSVP EMDPAATIPR
     SQTQPRTTAG TYSSPPPASY STLQAPALSV TGPITANSEQ IARLRSELDI VRGNTKVMSE
     MLTEMVPGQE DSSDLELLQE LNRTCRAMQH RIVELISRVS NEEVTEELLH VNDDLNNVFL
     RYERFERYRS GRSVQNASNG VLSEVTEDNL IDLGPGSPAV VSPMVGSTAP PSSLSSQLAG
     LDLGTESVSG TLSSLQQCKP QDGFDMFAQT RGNSLAEQRK TVTYEDPQAV GGLASALDNR
     KQNSEMIPVA QPSVMDDIEV WLRTDLKGDD LEEGVTSEEF DKFLEERAKA AETVPDLPSP
     PTEAPAPASN TSTRKKPERS DDALFAL
//
ID   DHR13_MOUSE             Reviewed;         376 AA.
AC   Q5SS80; Q14BH2; Q8BMX8;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=Dehydrogenase/reductase SDR family member 13;
DE            EC=1.1.-.-;
DE   Flags: Precursor;
GN   Name=Dhrs13;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357 AND SER-361, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
CC   -!- FUNCTION: Putative oxidoreductase (Potential).
CC   -!- SUBCELLULAR LOCATION: Secreted (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5SS80-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SS80-2; Sequence=VSP_029641;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC25347.1; Type=Frameshift; Positions=254, 256, 270, 290;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK011939; BAC25347.1; ALT_FRAME; mRNA.
DR   EMBL; AL669840; CAI25703.1; -; Genomic_DNA.
DR   EMBL; BC115881; AAI15882.1; -; mRNA.
DR   IPI; IPI00223154; -.
DR   IPI; IPI00877282; -.
DR   RefSeq; NP_899109.2; NM_183286.2.
DR   UniGene; Mm.390342; -.
DR   HSSP; Q28960; 1N5D.
DR   ProteinModelPortal; Q5SS80; -.
DR   SMR; Q5SS80; 30-283.
DR   PRIDE; Q5SS80; -.
DR   Ensembl; ENSMUST00000021187; ENSMUSP00000021187; ENSMUSG00000020834.
DR   GeneID; 70451; -.
DR   KEGG; mmu:70451; -.
DR   UCSC; uc007khu.1; mouse.
DR   CTD; 70451; -.
DR   MGI; MGI:1917701; Dhrs13.
DR   GeneTree; ENSGT00570000078948; -.
DR   HOGENOM; HBG750976; -.
DR   HOVERGEN; HBG078800; -.
DR   InParanoid; Q5SS80; -.
DR   OMA; WLVLRTP; -.
DR   PhylomeDB; Q5SS80; -.
DR   NextBio; 331649; -.
DR   ArrayExpress; Q5SS80; -.
DR   Bgee; Q5SS80; -.
DR   CleanEx; MM_DHRS13; -.
DR   Genevestigator; Q5SS80; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PROSITE; PS00061; ADH_SHORT; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; NAD; NADP; Oxidoreductase; Phosphoprotein;
KW   Secreted; Signal.
FT   SIGNAL        1     25       Potential.
FT   CHAIN        26    376       Dehydrogenase/reductase SDR family member
FT                                13.
FT                                /FTId=PRO_0000311921.
FT   NP_BIND      43     49       NAD or NADP (By similarity).
FT   COMPBIAS    317    330       Asp/Glu-rich.
FT   ACT_SITE    197    197       Proton acceptor (By similarity).
FT   BINDING     170    170       Substrate (Potential).
FT   MOD_RES     357    357       Phosphoserine.
FT   MOD_RES     361    361       Phosphoserine.
FT   VAR_SEQ       1     91       Missing (in isoform 2).
FT                                /FTId=VSP_029641.
FT   CONFLICT    240    240       P -> R (in Ref. 1; BAC25347).
SQ   SEQUENCE   376 AA;  40745 MW;  B4C77A8058948865 CRC64;
     MEMLLLGAGL LLGAYVLVYY NLVKAPSCGG IGSLRGRTVV VTGANSGIGK MTALELARRG
     ARVVLACRSR ERGEAAAFDL RQESGNNEVI FMALDLASLA SVQAFATAFL SSEPRLDVLI
     HNAGISSCGR TRETFNLLLR VNHVGPFLLT HLLLPRLRSC APSRVVIVSS AAHRRGRLDF
     TRLDCPVVGW QQELRAYADS KLANVLFARE LATQLEGTGV TCYAAHPGPV NSELFLRHLP
     GWLRPILRPL AWLVLRAPQG GAQTPLYCAL QEGIEPLSGR YFANCHVEEV SPAARDDQAA
     QRLWKATKKL AGLAPGDDDD DPDEEPEPED PRAPSSQSAP SPEKTTVSGP SHSYQGSQDL
     SKLTQRRIQV KDEPTP
//
ID   ZZEF1_MOUSE             Reviewed;        2924 AA.
AC   Q5SSH7; Q499C8; Q6ZQC5; Q8C710; Q8CI54;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Zinc finger ZZ-type and EF-hand domain-containing protein 1;
GN   Name=Zzef1; Synonyms=Kiaa0399;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2202-2924 (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Liver, and Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2642-2924 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2407, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1464, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1538, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1538, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5SSH7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SSH7-2; Sequence=VSP_025876;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q5SSH7-3; Sequence=VSP_025877;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 DOC domain.
CC   -!- SIMILARITY: Contains 1 EF-hand domain.
CC   -!- SIMILARITY: Contains 2 ZZ-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH37463.1; Type=Erroneous initiation;
CC       Sequence=AAH99976.1; Type=Erroneous initiation;
CC       Sequence=BAC97941.1; Type=Erroneous initiation;
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DR   EMBL; AK129131; BAC97941.1; ALT_INIT; mRNA.
DR   EMBL; AL663082; CAI25190.1; -; Genomic_DNA.
DR   EMBL; BC037463; AAH37463.1; ALT_INIT; mRNA.
DR   EMBL; BC099976; AAH99976.1; ALT_INIT; mRNA.
DR   EMBL; AK052734; BAC35122.1; -; mRNA.
DR   IPI; IPI00340123; -.
DR   IPI; IPI00849568; -.
DR   IPI; IPI00849942; -.
DR   RefSeq; NP_001039001.1; NM_001045536.2.
DR   UniGene; Mm.272030; -.
DR   ProteinModelPortal; Q5SSH7; -.
DR   SMR; Q5SSH7; 220-380, 1779-1824, 1826-1861.
DR   PhosphoSite; Q5SSH7; -.
DR   PRIDE; Q5SSH7; -.
DR   Ensembl; ENSMUST00000069395; ENSMUSP00000068790; ENSMUSG00000055670.
DR   GeneID; 195018; -.
DR   KEGG; mmu:195018; -.
DR   UCSC; uc007jzl.1; mouse.
DR   CTD; 195018; -.
DR   MGI; MGI:2444286; Zzef1.
DR   eggNOG; roNOG04477; -.
DR   GeneTree; ENSGT00600000084528; -.
DR   HOGENOM; HBG355282; -.
DR   HOVERGEN; HBG108782; -.
DR   InParanoid; Q5SSH7; -.
DR   OMA; KRKTVKD; -.
DR   OrthoDB; EOG4QFWC9; -.
DR   ArrayExpress; Q5SSH7; -.
DR   Bgee; Q5SSH7; -.
DR   CleanEx; MM_ZZEF1; -.
DR   Genevestigator; Q5SSH7; -.
DR   GO; GO:0005680; C:anaphase-promoting complex; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IEA:InterPro.
DR   InterPro; IPR004939; Ananphase-promot_cplx_su10_DOC.
DR   InterPro; IPR000859; CUB.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR000433; Znf_ZZ.
DR   Gene3D; G3DSA:2.60.120.290; CUB; 1.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF03256; APC10; 1.
DR   Pfam; PF00569; ZZ; 2.
DR   SMART; SM00291; ZnF_ZZ; 2.
DR   SUPFAM; SSF49785; Gal_bind_like; 1.
DR   PROSITE; PS51284; DOC; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Metal-binding; Phosphoprotein;
KW   Zinc; Zinc-finger.
FT   CHAIN         1   2924       Zinc finger ZZ-type and EF-hand domain-
FT                                containing protein 1.
FT                                /FTId=PRO_0000289001.
FT   DOMAIN      111    146       EF-hand.
FT   DOMAIN      226    405       DOC.
FT   ZN_FING    1775   1823       ZZ-type 1.
FT   ZN_FING    1824   1870       ZZ-type 2.
FT   MOD_RES    1464   1464       Phosphoserine.
FT   MOD_RES    1475   1475       Phosphoserine (By similarity).
FT   MOD_RES    1509   1509       Phosphoserine (By similarity).
FT   MOD_RES    1518   1518       Phosphoserine (By similarity).
FT   MOD_RES    1519   1519       Phosphothreonine (By similarity).
FT   MOD_RES    1538   1538       Phosphoserine.
FT   MOD_RES    2407   2407       Phosphoserine.
FT   MOD_RES    2630   2630       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1   2840       Missing (in isoform 3).
FT                                /FTId=VSP_025877.
FT   VAR_SEQ    2664   2697       VRESKHSYNNNTSFEDKVHIPGAIYLSIKFDPQR -> C
FT                                (in isoform 2).
FT                                /FTId=VSP_025876.
FT   CONFLICT   2670   2670       S -> P (in Ref. 4; BAC35122).
FT   CONFLICT   2697   2697       R -> C (in Ref. 4; BAC35122).
SQ   SEQUENCE   2924 AA;  328312 MW;  35E1B0C9981C4B78 CRC64;
     MGNAPSNSSE DEAAAAGGEG WSPHQDWAAD SGTTPGPGPA AAVLPSAAAL LEPARLREAA
     AALRPAPPCE SLVSRHHGAL LRWLEERLGR GEESVTLEQF RELLEARGAG CSGEQFEEAF
     AQFDAEGDGT VDAENMLEAL KNSSGANLQG ELSHVIRQLQ ACSLVPGFID IFSESKEGLG
     IHSSMILRFL HRNRISSMVI PYPMLDHCNN MCTMRSSVLK ESLDQLVQKE KESPGDLARS
     PEMDKLKSVT KCYAYIETSS NPADIYRMTN GETSSYWQSD GSARSHWIRL KMKPDVVLRH
     LSIAVAATDQ SYMPQQVTVA VGRSASDLQE VRDVHIPSNV TGYVTLLENA NISQLYVQIN
     IKRCLSDGCD TRIHGLRAVG FQRVKKSGVS VSDASAIWYW SLLTSLVTAS METNPAFVQT
     VLHNTQKALQ HMPPLSLSPG STDFSTFLSP NVLEEVDSFL IRITSCCSTP EVELTLLAFA
     LARGSIAKVM SSLCTITDHL DTQYDASSLI SSMASVRQNL LLKYGKPLQL TLQACDVKGK
     EDKSGPENLL VEPWTRDGFL TETGKTRAST IFSTGSDSAF QVTQIRIMVR RGGIGAQCGL
     VFAYNSPSNK FHAEEHFKRF EKYDKWKLQE LRQFVKSRIG CSSDDLGEDD PIGWFELEEE
     WDEADVKLQQ CRVAKFLMVK FLCTRQESAE RLGVQGLSIS GYLRPARAEA EQSILYAHCR
     RDTENIHGAT LLLRTLQFIQ QLSHDLMQQK ESGLKHKSFL DFAGLDLQIF WKFYSKLKQN
     RREECICAQT LLLKLLQSCF SVLQGDPQAA SEEEKPTAQR SEGIQAAKEL YTHLCNVVDK
     PNGNSMPMEI LKQEVRNTLL NGAAIFFPDR QTRRSQLFTM MKSVTEHERK QSLQLTFHSL
     CTYFSDKDPG GLLLLPEKSD LATMNTSEVL AVMNTLLSVA ARECELLMLN RSHGAVGSVL
     FSLFWSVQGS LLSWCFLQLK STDAAAKELA MDLIEKYVGQ FLASMRVILE SLLSQYSGKT
     IVEKLCNSVF SMAARQLVIF LLDFCTLDVS HCTLLREFST LTELLKKLCS DPEGGLSKLD
     VETWQQEQPV VLHTWTKEST HNYENNCHEV SVFISPGATY FEVEFDERCE TEKRYDYLEF
     TDSRGGKTRY DTKVGTYKWP KKVTFKDGPR LQFLFHSDSS NNEWGYKFTV TAYGLPDVAV
     SWGLDLQLLV SRLMGRLASQ CMALKSVHQL GSNMAVSQAK LTSVLNSPLW KPVFRHQICP
     ELELEASWPT HPHKDGKEVK NIPDDPCRHF LLDFAQSEPA QNFCGPYSEL FKGFIQACRK
     QAPKTDIVAG STIDQAVNAT FAALVYRTPD LYEKLQKYVN SGGKIALTEE FSQVYSLADG
     IRIWMLEMKQ KSLLSLGNDS EEKRGLEAAE VNPESLAKEC IQKSLLLLKF LPMSKSSKEN
     CDKLETVDET DHLQPLDRRQ RTSSVVEEHF QGSASPTEAA TPAAGDRSPA LEIQPKLLPS
     SGPCVAEVST AEEPSPPSTP TRRPPFTRGR LRLLSFRSME ETRPVPTVKE KYPVLKDVMD
     FIKDQSLSHE SVVKVLSLRK AQGQSILEVL RIIQYCTESL GQPHCFHPPY ILFLLELLTC
     QKDFTNYFGH LEGCGADLHR EIRDTYYQLV LFLVKAIKRF SSINDRSLLP ALSCVQTALL
     HLLDMGWEPS DLAFFVDIQL PDLLMNMSQE NISVHDSVIS QWSEEDELAD AKQNSEWMDE
     CQDGMFEAWY EKIAQEDPEK QRKMHMFIAR YCDLLNVDIS CDGCDEIAPW HRYRCLQCSD
     MDLCKTCFLG GVKPEGHGDD HEMVNMEFTC DHCQGLIIGR RMNCNVCDDF DLCYGCYTAK
     KYSYGHLPTH SITAHPMVTI RISDRQRLIQ PYIHNYSWLL FAALALYSAH LTSTEQVDGE
     QLDPQARTNA ATLRSQCMQL VGDCLMKAHQ GKGLKALALL GVLPDGDSTS ENQALPVTVS
     FQASEEQADA GLLVPCNGKR AADTEVRPLD YKQKKKAGED LSIVKDPSCQ TQVSDAPASA
     HVPPGLPDAE HPEVSAQVLV EEKAITPNPE QVFAECSQKR ILGLLAAMLP PIKSGPTVPL
     IDLEHVLPLM FQVVISNAGH LNETYHLTLG LLGQLIIRLQ PAEVDAAVMK VLSAKHNLRV
     GLDWACSMAE ILRSLNNAPL WRDVIATFTD HCIKQLPFQL KHTNIFTLLV LVGFPQVLCV
     GTRCVYMDNA NEPHNVIILK HFTEKNRAVI VDVKTRKRKT VKDYQLVQKG GGQECGTSQS
     QLSQYSQHFA FIASHLLQTS MDSHCPEAVE ATWVLSLALK GLYKTLKAHG FEETHATFLQ
     TDLLKLLVKK CSKGTGFSKT WLLRDLEILS IMLYSSKKEI NTLAEHGDLE LDERGDQEEE
     LDRPVSSPGE AEQKKLDPLE NLDEPTRICF LMAHDALNAP LHILRAIYEL QMKKTDSFFL
     EVQKRFDGDE LTTDERIRSL AQRWQPSRSL RLEEQSAKAV DTDMIILPCL SRPARSDQAT
     PESNPVTQKL ISSTESELQQ SYAKQRRSKS AALLHKELNC KSKRAIRDYL FRVNEATSVL
     YARHVLASLL AEWPGHVPVS EDILELSGPA HMTYILDMFM QLEEKHQWEK ILQKVLQGCR
     ENMLGTMALA ACQFMEEPGM EVQVRESKHS YNNNTSFEDK VHIPGAIYLS IKFDPQRNTE
     EGCDELAMSS SSDFQQDRHN FSGSQQKWKD FELPGDTLYY RFTSDMSNTE WGYRFTVTAG
     HLGRFQTGFE ILKQMLSEER VVPHLALGKI WEWLVGVACR QTGHQRLKAI HLLLRIVQCC
     SHSDLCDLGL LKPLWQLFTH MEYGLFEDVT QPGILLPLHR ALTELFFVTE NRAQELGLLQ
     EYLLALTTED HLLRCAAQAL QNIAAISLAI NYPNKATRLW NVEC
//
ID   ABR_MOUSE               Reviewed;         859 AA.
AC   Q5SSL4; Q3U5G0; Q3UQJ6; Q3UY38; Q5SYJ5; Q5SYJ7; Q5SYJ8; Q5SYJ9;
AC   Q6PCY1; Q6PDH3;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Active breakpoint cluster region-related protein;
GN   Name=Abr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-407 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Lung, Olfactory bulb, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: GTPase-activating protein for RAC and CDC42. Promotes
CC       the exchange of RAC or CDC42-bound GDP by GTP, thereby activating
CC       them (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q5SSL4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SSL4-2; Sequence=VSP_035905;
CC       Name=3;
CC         IsoId=Q5SSL4-3; Sequence=VSP_035903, VSP_035906;
CC       Name=4;
CC         IsoId=Q5SSL4-4; Sequence=VSP_035904;
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI24542.3; Type=Erroneous gene model prediction;
CC       Sequence=CAQ11499.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK134993; BAE22375.1; -; mRNA.
DR   EMBL; AK142364; BAE25044.1; -; mRNA.
DR   EMBL; AK153615; BAE32119.1; -; mRNA.
DR   EMBL; AL591143; CAI24541.2; -; Genomic_DNA.
DR   EMBL; AL663050; CAI24541.2; JOINED; Genomic_DNA.
DR   EMBL; AL591143; CAI24542.3; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL663050; CAI24542.3; JOINED; Genomic_DNA.
DR   EMBL; AL591143; CAI24543.2; -; Genomic_DNA.
DR   EMBL; AL663050; CAI24543.2; JOINED; Genomic_DNA.
DR   EMBL; AL591143; CAI24545.1; -; Genomic_DNA.
DR   EMBL; AL663050; CAI24545.1; JOINED; Genomic_DNA.
DR   EMBL; AL591143; CAI24547.2; -; Genomic_DNA.
DR   EMBL; AL663050; CAI25860.1; -; Genomic_DNA.
DR   EMBL; AL591143; CAI25860.1; JOINED; Genomic_DNA.
DR   EMBL; AL663050; CAQ11498.1; -; Genomic_DNA.
DR   EMBL; AL591143; CAQ11498.1; JOINED; Genomic_DNA.
DR   EMBL; AL663050; CAQ11499.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL591143; CAQ11499.1; JOINED; Genomic_DNA.
DR   EMBL; AL663050; CAQ11500.1; -; Genomic_DNA.
DR   EMBL; AL591143; CAQ11500.1; JOINED; Genomic_DNA.
DR   EMBL; BC056385; AAH56385.1; -; mRNA.
DR   EMBL; BC058708; AAH58708.1; -; mRNA.
DR   EMBL; BC059064; AAH59064.1; -; mRNA.
DR   IPI; IPI00381365; -.
DR   IPI; IPI00395178; -.
DR   IPI; IPI00515365; -.
DR   IPI; IPI00761596; -.
DR   RefSeq; NP_932135.1; NM_198018.1.
DR   RefSeq; NP_942597.1; NM_198894.1.
DR   RefSeq; NP_942598.1; NM_198895.1.
DR   UniGene; Mm.258939; -.
DR   HSSP; P52757; 1XA6.
DR   ProteinModelPortal; Q5SSL4; -.
DR   SMR; Q5SSL4; 504-600, 640-846.
DR   PhosphoSite; Q5SSL4; -.
DR   PRIDE; Q5SSL4; -.
DR   Ensembl; ENSMUST00000072740; ENSMUSP00000072522; ENSMUSG00000017631.
DR   GeneID; 109934; -.
DR   KEGG; mmu:109934; -.
DR   UCSC; uc007kft.1; mouse.
DR   CTD; 109934; -.
DR   MGI; MGI:107771; Abr.
DR   eggNOG; roNOG15048; -.
DR   GeneTree; ENSGT00600000084231; -.
DR   HOVERGEN; HBG004165; -.
DR   OMA; AEGHEEQ; -.
DR   OrthoDB; EOG476JZJ; -.
DR   PhylomeDB; Q5SSL4; -.
DR   NextBio; 363025; -.
DR   ArrayExpress; Q5SSL4; -.
DR   Bgee; Q5SSL4; -.
DR   Genevestigator; Q5SSL4; -.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0030675; F:Rac GTPase activator activity; IDA:MGI.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IGI:MGI.
DR   GO; GO:0007420; P:brain development; IGI:MGI.
DR   GO; GO:0042472; P:inner ear morphogenesis; IGI:MGI.
DR   GO; GO:0030336; P:negative regulation of cell migration; IGI:MGI.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
DR   GO; GO:0043314; P:negative regulation of neutrophil degranulation; IGI:MGI.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IGI:MGI.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; IGI:MGI.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; GTPase activation;
KW   Guanine-nucleotide releasing factor.
FT   CHAIN         1    859       Active breakpoint cluster region-related
FT                                protein.
FT                                /FTId=PRO_0000355539.
FT   DOMAIN       91    284       DH.
FT   DOMAIN      301    459       PH.
FT   DOMAIN      491    595       C2.
FT   DOMAIN      647    845       Rho-GAP.
FT   VAR_SEQ       1    218       Missing (in isoform 3).
FT                                /FTId=VSP_035903.
FT   VAR_SEQ       1     82       MEPLSHRGLPRLSWIDTLYSNFSYGAEDYDAEGHEEQKGPP
FT                                EGSETMPYIDESPTMSPQLSARSQGGGDSVSPTPPEGLAPG
FT                                -> MEEEEEAIGFLDKVLEDEDVFLLEECELGTPTSPGSGS
FT                                PFLVAVK (in isoform 4).
FT                                /FTId=VSP_035904.
FT   VAR_SEQ       1     21       MEPLSHRGLPRLSWIDTLYSN -> MAAGGRRRRPLRYQSL
FT                                AALVEDSQWPFLFLVSD (in isoform 2).
FT                                /FTId=VSP_035905.
FT   VAR_SEQ     219    233       GPKDSKDSHTSVTME -> MEILLIIRFCCNCTY (in
FT                                isoform 3).
FT                                /FTId=VSP_035906.
FT   CONFLICT    164    164       W -> R (in Ref. 1; BAE32119).
FT   CONFLICT    630    630       D -> E (in Ref. 1; BAE22375).
SQ   SEQUENCE   859 AA;  97667 MW;  79ED2F432899A1F9 CRC64;
     MEPLSHRGLP RLSWIDTLYS NFSYGAEDYD AEGHEEQKGP PEGSETMPYI DESPTMSPQL
     SARSQGGGDS VSPTPPEGLA PGVEAGKGLE MRKLVLSGFL ASEEIYINQL EALLLPMKPL
     KATATTSQPV LTIQQIETIF YKIQDIYEIH KEFYDNLCPK VQQWDSQVTM GHLFQKLASQ
     LGVYKAFVDN YKVALETAEK CSQSNNQFQK ISEELKVKGP KDSKDSHTSV TMEALLYKPI
     DRVTRSTLVL HDLLKHTPVD HPDYPLLQDA LRISQNFLSS INEDIDPRRT AVTTPKGETR
     QLVKDGFLVE MSESSRKLRH VFLFTDVLLC AKLKKTSAGK HQQYDCKWYI PLADLVFPSP
     EESEASPQVH PFPDHELEDM KTKISALKSE IQKEKANKGQ SRAIERLKKK MFENEFLLLL
     NSPTIPFRIH NRNGKSYLFL LSSDYERSEW REAIQKLQKK DLQAFVLSSV ELQVLTGSCF
     KLRTVHNIPV TSNKDDDESP GLYGFLHVIV HSAKGFKQSA NLYCTLEVDS FGYFVSKAKT
     RVFRDTTEPK WDEEFEIELE GSQSLRILCY EKCYDKTKVN KDNNEIVDKI MGKGQIQLDP
     QTVESKNWHT DVIEMNGIKV EFSMKFTSRD MSLKRTPSKK QTGVFGVKIS VVTKRERSKV
     PYIVRQCIEE VEKRGIEEVG IYRISGVATD IQALKAVFDA NNKDILLMLS DMDINAIAGT
     LKLYFRELPE PLLTDRLYPA FMEGIALSDP AAKENCMMHL LRSLPDPNLI TFLFLLEHLK
     RVAEKEPINK MSLHNLATVF GPTLLRPSEV ESKAHLTSAA DIWSHDVMAQ VQVLLYYLQH
     PPISFAELKR NTLYFSTDV
//
ID   RHG44_MOUSE             Reviewed;         814 AA.
AC   Q5SSM3; Q5SSM4; Q5SSM6; Q5SSM7; Q7TNB9; Q8BW90;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Rho GTPase-activating protein 44;
DE   AltName: Full=Rho-type GTPase-activating protein RICH2;
DE   AltName: Full=RhoGAP interacting with CIP4 homologs protein 2;
DE            Short=RICH-2;
GN   Name=Arhgap44; Synonyms=Rich2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting
CC       them to an inactive GDP-bound state. Acts as a GTPase activitor in
CC       vitro for CDC42 and RAC1 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q5SSM3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SSM3-2; Sequence=VSP_023740, VSP_023741;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q5SSM3-3; Sequence=VSP_023741;
CC       Name=4;
CC         IsoId=Q5SSM3-4; Sequence=VSP_023737, VSP_023738, VSP_023739;
CC         Note=No experimental confirmation available. Ref.1 (BAC35316)
CC         sequence differs from that shown due to a frameshift in position
CC         175;
CC   -!- SIMILARITY: Contains 1 BAR domain.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC35316.1; Type=Frameshift; Positions=19;
CC       Sequence=CAI24614.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK053220; BAC35316.1; ALT_FRAME; mRNA.
DR   EMBL; AL663045; CAI24613.2; -; Genomic_DNA.
DR   EMBL; AL663045; CAI24614.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL663045; CAI24616.1; -; Genomic_DNA.
DR   EMBL; AL663045; CAI24617.1; -; Genomic_DNA.
DR   EMBL; BC056366; AAH56366.1; -; mRNA.
DR   EMBL; BC059911; AAH59911.1; -; mRNA.
DR   IPI; IPI00128632; -.
DR   IPI; IPI00515397; -.
DR   IPI; IPI00648903; -.
DR   IPI; IPI00831188; -.
DR   RefSeq; NP_001092758.1; NM_001099288.1.
DR   RefSeq; NP_778168.2; NM_175003.3.
DR   UniGene; Mm.134338; -.
DR   HSSP; Q07960; 1RGP.
DR   ProteinModelPortal; Q5SSM3; -.
DR   SMR; Q5SSM3; 4-445.
DR   STRING; Q5SSM3; -.
DR   PhosphoSite; Q5SSM3; -.
DR   PRIDE; Q5SSM3; -.
DR   Ensembl; ENSMUST00000047463; ENSMUSP00000039139; ENSMUSG00000033389.
DR   Ensembl; ENSMUST00000093001; ENSMUSP00000090680; ENSMUSG00000033389.
DR   Ensembl; ENSMUST00000093002; ENSMUSP00000090681; ENSMUSG00000033389.
DR   Ensembl; ENSMUST00000093003; ENSMUSP00000090682; ENSMUSG00000033389.
DR   GeneID; 216831; -.
DR   KEGG; mmu:216831; -.
DR   CTD; 216831; -.
DR   MGI; MGI:2144423; AU040829.
DR   eggNOG; roNOG09803; -.
DR   GeneTree; ENSGT00600000084016; -.
DR   HOGENOM; HBG446214; -.
DR   HOVERGEN; HBG000015; -.
DR   InParanoid; Q5SSM3; -.
DR   OMA; PSPYGLS; -.
DR   OrthoDB; EOG4XD3QQ; -.
DR   NextBio; 375374; -.
DR   ArrayExpress; Q5SSM3; -.
DR   Bgee; Q5SSM3; -.
DR   CleanEx; MM_AU040829; -.
DR   Genevestigator; Q5SSM3; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR004148; BAR.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF03114; BAR; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00721; BAR; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS51021; BAR; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; GTPase activation; Phosphoprotein.
FT   CHAIN         1    814       Rho GTPase-activating protein 44.
FT                                /FTId=PRO_0000280481.
FT   DOMAIN       14    249       BAR.
FT   DOMAIN      255    445       Rho-GAP.
FT   COMPBIAS    540    740       Pro-rich.
FT   MOD_RES     514    514       Phosphoserine (By similarity).
FT   VAR_SEQ       1     18       MKKQFNRMRQLANQTVGR -> MELPGLELVRPSWVRAGRW
FT                                (in isoform 4).
FT                                /FTId=VSP_023737.
FT   VAR_SEQ     195    210       DQLSADMYSFVAKEID -> VPVPLALLSRDRLRSP (in
FT                                isoform 4).
FT                                /FTId=VSP_023738.
FT   VAR_SEQ     211    814       Missing (in isoform 4).
FT                                /FTId=VSP_023739.
FT   VAR_SEQ     509    514       Missing (in isoform 2).
FT                                /FTId=VSP_023740.
FT   VAR_SEQ     769    814       DLVHFDVPSIHIELGSTLRLSPLEHARRHSATDKRDSEEES
FT                                ESTAL -> AV (in isoform 2 and isoform 3).
FT                                /FTId=VSP_023741.
SQ   SEQUENCE   814 AA;  88994 MW;  466419A6D9471DDF CRC64;
     MKKQFNRMRQ LANQTVGRAE KTEVLSEDLL QVEKRLELVK QVSHSTHKKL TACLQGQQGA
     EADKRSKKLP LTTLAQCLVE GSAILGDDTL LGKMLKLCGE TEDKLAQELI HFELQVERDV
     IEPLFLLAEV EIPNIQKQRK HLAKLVLDMD SSRTRWQQTS KSSGLSSSLQ PAGAKADALR
     EEMEEAANRV EICRDQLSAD MYSFVAKEID YANYFQTLIE VQAEYHRKSL TLLQAVLPQI
     KAQQEAWVEK PSFGKPLEEH LMISGREIAF PIEACVTMLL ECGMQEEGLF RVAPSASKLK
     KLKAALDCCV VDVQEYSADP HAIAGALKSY LRELPEPLMT FELYDEWIQA SNIQEQDKRL
     QALWNACEKL PKANHNNIKY LIKFLSKLSE YQDVNKMTPS NMAIVLGPNL LWPQSEGNIT
     EMMTTVSLQI VGIIEPIIQH ADWFFPGEIE FNLTGSYGSP VHVNHNANYS SMPSPDMDPA
     DRRQPEQARR PLSVATDNMM LEFYKKDGLR KIQSMGVRVM DTSWVARRGS SAGRKASCAP
     PSMQPPAPPS ELAAPLPSPL PEQVPDSPAT PAPALSPSGA SLQPTPERPS VSKSKELSPG
     SGQKGSPGSI QGTPCPGTQL GPQPAASPSQ LPADQSPHTL RKVSKKVAPI PPKVPFVQPG
     TVSDQPVGQP SPVSLSPTPP STPSPYGLSY PPGYSMASGQ LSPASAPPLA SPSVFTSTLA
     KSRPTPKPRQ RPTLPPPQPP SVSLSASSPQ STEHPMLDGM SPGESMSTDL VHFDVPSIHI
     ELGSTLRLSP LEHARRHSAT DKRDSEEESE STAL
//
ID   Q5SUF5_MOUSE            Unreviewed;      2247 AA.
AC   Q5SUF5;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 47.
DE   SubName: Full=Calcium channel, voltage-dependent, T type, alpha 1G subunit;
GN   Name=Cacna1g; ORFNames=RP23-65I14.3-004;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Lad H.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL645965; CAI25957.1; -; Genomic_DNA.
DR   IPI; IPI00648377; -.
DR   UniGene; Mm.29585; -.
DR   ProteinModelPortal; Q5SUF5; -.
DR   STRING; Q5SUF5; -.
DR   PRIDE; Q5SUF5; -.
DR   Ensembl; ENSMUST00000107792; ENSMUSP00000103421; ENSMUSG00000020866.
DR   MGI; MGI:1201678; Cacna1g.
DR   GeneTree; ENSGT00560000076834; -.
DR   HOVERGEN; HBG050764; -.
DR   ArrayExpress; Q5SUF5; -.
DR   Bgee; Q5SUF5; -.
DR   Genevestigator; Q5SUF5; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0008332; F:low voltage-gated calcium channel activity; IDA:MGI.
DR   GO; GO:0060371; P:regulation of atrial cardiomyocyte membrane depolarization; IMP:MGI.
DR   GO; GO:0002027; P:regulation of heart rate; IMP:MGI.
DR   GO; GO:0010045; P:response to nickel ion; IMP:MGI.
DR   GO; GO:0007268; P:synaptic transmission; IGI:MGI.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR005445; VDCC_T_a1su.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR01629; TVDCCALPHA1.
PE   2: Evidence at transcript level;
KW   Ion transport; Ionic channel; Membrane; Transmembrane; Transport.
SQ   SEQUENCE   2247 AA;  249008 MW;  94FB25288CE91470 CRC64;
     MDEEEDGAGA EESGQPRSFT QLNDLSGAGG RQGPGSTEKD PGSADSEAEG LPYPALAPVV
     FFYLSQDSRP RSWCLRTVCN PWFERVSMLV ILLNCVTLGM FRPCEDIACD SQRCRILQAF
     DDFIFAFFAV EMVVKMVALG IFGKKCYLGD TWNRLDFFIV IAGMLEYSLD LQNVSFSAVR
     TVRVLRPLRA INRVPSMRIL VTLLLDTLPM LGNVLLLCFF VFFIFGIVGV QLWAGLLRNR
     CFLPENFSLP LSVDLEPYYQ TENEDESPFI CSQPRENGMR SCRSVPTLRG EGGGGPPCGL
     DYEAYNSSSN TTCVNWNQYY TNCSAGEHNP FKGAINFDNI GYAWIAIFQV ITLEGWVDIM
     YFVMDAHSFY NFIYFILLII VGSFFMINLC LVVIATQFSE TKQRESQLMR EQRVRFLSNA
     STLASFSEPG SCYEELLKYL VYILRKAARR LAQVSRAVGV RAGLLSSPVA RGGQEPQPSG
     SCSRSHRRLS VHHLVHHHHH HHHHYHLGNG TLRVPRASPE IQDRDANGSR WLMLPPPSTP
     TPSGGPPRGA ESVHSFYHAD CHLEPVRCQA PPPRSPSEAS GRTVGSGKVY PTVHTSPPPE
     MLKDKALVEV APSPGPPTLT SFNIPPGPFS SMHKLLETQS TGACHSSCKI SSPCSKADSG
     ACGPDSCPYC ARTGAGEPES ADHEMPDSDS EAVYEFTQDA QHSDLRDPHR RRRPSLGPDA
     EPSSVLAFWR LICDTFRKIV DSKYFGRGIM IAILVNTLSM GIEYHEQPEE LTNALEISNI
     VFTSLFALEM LLKLLVYGPF GYIKNPYNIF DGVIVVISVW EIVGQQGGGL SVLRTFRLMR
     VLKLVRFLPA LQRQLVVLMK TMDNVATFCM LLMLFIFIFS ILGMHLFGCK FASERDGDTL
     PDRKNFDSLL WAIVTVFQIL TQEDWNKVLY NGMASTSSWA ALYFIALMTF GNYVLFNLLV
     AILVEGFQAE GDATKSESEP DFFSPSVDGD GDRKKRLALV ALGEHSELRK SLLPPLIIHT
     AATPMSLPKS SSTGVGEALG SGSRRTSSSG SAEPGTAHHE MKSPPSARSS PHSPWSAASS
     WTSRRSSRNS LGRAPSLKRR SPSGERRSLL SGEGQESQDE EESSEEDRAS PAGSDHRHRG
     SLEREAKSSF DLPDTLQVPG LHRTASGRSS ASEHQDCNGK SASGRLARTL RADDPPLDGD
     DGDDEGNLSK GERLRAWVRA RLPACCRERD SWSAYIFPPQ SRFRLLCHRI ITHKMFDHVV
     LVIIFLNCIT IAMERPKIDP HSAERIFLTL SNYIFTAVFL AEMTVKVVAL GWCFGEQAYL
     RSSWNVLDGL LVLISVIDIL VSMVSDSGTK ILGMLRVLRL LRTLRPLRVI SRAQGLKLVV
     ETLMSSLKPI GNIVVICCAF FIIFGILGVQ LFKGKFFVCQ GEDTRNITNK SDCAEASYRW
     VRHKYNFDNL GQALMSLFVL ASKDGWVDIM YDGLDAVGVD QQPIMNHNPW MLLYFISFLL
     IVAFFVLNMF VGVVVENFHK CRQHQEEEEA RRREEKRLKR LEKKRRKAQC KPYYSDYSRF
     RLLVHHLCTS HYLDLFITGV IGLNVVTMAM EHYQQPQILD EALKICNYIF TVIFVLESVF
     KLVAFGFRRF FQDRWNQLDL AIVLLSIMGI TLEEIEVNAS LPINPTIIRI MRVLRIARVL
     KLLKMAVGMR ALLDTVMQAL PQVGNLGLLF MLLFFIFAAL GVELFGDLEC DETHPCEGLG
     RHATFRNFGM AFLTLFRVST GDNWNGIMKD TLRDCDQEST CYNTVISPIY FVSFVLTAQF
     VLVNVVIAVL MKHLEESNKE AKEEAELEAE LELEMKTLSP QPHSPLGSPF LWPGVEGVNS
     PDSPKPGAPH TTAHIGAASS GFSLEHPTMV PHTEEGPVPL GPDLLTVRKS GVSRTHSLPN
     DSYMCRNGST AERSLGHRGW GLPKAQSGSI LSVHSQPADT SCILQLPKDA HYLLQPHGAP
     TWGAIPKLPP PGRSPLAQRP LRRQAAIRTD SLDVQGLGSR EDLLSEVSGP SCPLTRSSSF
     WGGSSIQVQQ RSGSQSKVSK HIRLPAPCPG LEPSWAKDPQ ETRSSLELDT ELSWISGDLL
     PSSQEEPLSP RDLKKCYSVE AQSCRRRPGS WLDEQRRHSI AVSCLDSGSQ PRLCPSPSSL
     GGQPLGGPGS RPKKKLSPPS ISIDPPESQG PRPPCSPGVC LRRRAPASDS KDPSASSPLD
     STAASPSPKK DALSLSGLSS DPTDLDP
//
ID   Q5SUH6_MOUSE            Unreviewed;       641 AA.
AC   Q5SUH6;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 46.
DE   SubName: Full=Clathrin interactor 1;
DE   SubName: Full=MCG22297, isoform CRA_b;
GN   Name=Clint1; ORFNames=RP23-298M7.4-001, mCG_22297;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Phillimore B.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 ENTH (epsin N-terminal homology) domain.
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DR   EMBL; AL645948; CAI25021.1; -; Genomic_DNA.
DR   EMBL; CH466575; EDL33834.1; -; Genomic_DNA.
DR   IPI; IPI00648186; -.
DR   UniGene; Mm.169673; -.
DR   ProteinModelPortal; Q5SUH6; -.
DR   SMR; Q5SUH6; 17-152.
DR   STRING; Q5SUH6; -.
DR   PRIDE; Q5SUH6; -.
DR   Ensembl; ENSMUST00000109261; ENSMUSP00000104884; ENSMUSG00000006169.
DR   MGI; MGI:2144243; Clint1.
DR   eggNOG; roNOG07838; -.
DR   GeneTree; ENSGT00600000084490; -.
DR   HOGENOM; HBG714771; -.
DR   HOVERGEN; HBG048921; -.
DR   InParanoid; Q5SUH6; -.
DR   OMA; GMPNLAM; -.
DR   OrthoDB; EOG4BK53R; -.
DR   PhylomeDB; Q5SUH6; -.
DR   ArrayExpress; Q5SUH6; -.
DR   Bgee; Q5SUH6; -.
DR   Genevestigator; Q5SUH6; -.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR013809; Epsin-like_N.
DR   InterPro; IPR001026; Epsin_dom_N.
DR   Gene3D; G3DSA:1.25.40.90; ENTH_VHS; 1.
DR   Pfam; PF01417; ENTH; 1.
DR   SMART; SM00273; ENTH; 1.
DR   SUPFAM; SSF48464; ENTH_VHS; 1.
DR   PROSITE; PS50942; ENTH; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   641 AA;  69759 MW;  D55D5DE8445FAAEE CRC64;
     MLNMWKVREL VDKATNVVMN YSEIESKVRE ATNDDPWGPS GQLMGEIAKA TFMYEQFPEL
     MNMLWSRMLK DNKKNWRRVY KSLLLLAYLI RNGSERVVTS AREHIYDLRS LENYHFVDEH
     GKDQGINIRQ KVKELVEFAQ DDDRLREERK KAKKNKDKYV GVSSDSVGGF RYNERYDPEP
     KSKWDEEWDK NKSAFPFSDK LGELSDKIGS TIDDTISKFR RKDREDSPER CSDSDEEKKA
     RRGRSPKGEF KDEEETVTTK HIHITQATET TTTRHKRTAN PSKTIDLGAA AHYTGDKASP
     DQNASTHTPQ SSAKPSVPSS KSSGDLVDLF DGSSQSAGGS ADLFGGFADF GSAAASGNFP
     SQATSGNGDF GDWSAFNQAP SGPVASGGEL FGSAPQSAVE LISASQPALG PPPAASNSAD
     LFDLMGSSQA TMTSSQSMNF SLMSTNTVGL GLPMSRSQPL QNVSAVLQKP NPLYHQNTDM
     VQKSASKTLP STWSDPSVNI SLDNLLPGMQ PSKPQQPSLN TMIQQQNMQQ PLNVMTQSFG
     AVNLSSPSNM LPVRPQTNPL LGGPMPMNMP GVMTGTMGMA PLGNSAGMSQ GMVGMNMNMG
     MSASGMGLSG TMGMGMPSMA MPSGTVQPKQ DAFANFANFS K
//
ID   Q5SV64_MOUSE            Unreviewed;      2007 AA.
AC   Q5SV64;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 52.
DE   SubName: Full=Myosin, heavy polypeptide 10, non-muscle;
GN   Name=Myh10; ORFNames=RP23-396M19.2-002;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Pelan S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Pearce A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 IQ domain.
CC   -!- SIMILARITY: Contains 1 myosin head-like domain.
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DR   EMBL; AL603662; CAI25527.1; -; Genomic_DNA.
DR   EMBL; AL645644; CAI25527.1; JOINED; Genomic_DNA.
DR   EMBL; AL645644; CAI25575.1; -; Genomic_DNA.
DR   EMBL; AL603662; CAI25575.1; JOINED; Genomic_DNA.
DR   IPI; IPI00338604; -.
DR   UniGene; Mm.218233; -.
DR   ProteinModelPortal; Q5SV64; -.
DR   SMR; Q5SV64; 7-995.
DR   STRING; Q5SV64; -.
DR   PRIDE; Q5SV64; -.
DR   Ensembl; ENSMUST00000018887; ENSMUSP00000018887; ENSMUSG00000020900.
DR   MGI; MGI:1930780; Myh10.
DR   HOVERGEN; HBG004704; -.
DR   PhylomeDB; Q5SV64; -.
DR   ArrayExpress; Q5SV64; -.
DR   Bgee; Q5SV64; -.
DR   Genevestigator; Q5SV64; -.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0005938; C:cell cortex; IDA:MGI.
DR   GO; GO:0043197; C:dendritic spine; IDA:MGI.
DR   GO; GO:0030426; C:growth cone; IDA:MGI.
DR   GO; GO:0016459; C:myosin complex; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0001725; C:stress fiber; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:motor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007512; P:adult heart development; IMP:MGI.
DR   GO; GO:0007411; P:axon guidance; IMP:MGI.
DR   GO; GO:0055003; P:cardiac myofibril assembly; IMP:MGI.
DR   GO; GO:0008283; P:cell proliferation; IMP:MGI.
DR   GO; GO:0021680; P:cerebellar Purkinje cell layer development; IMP:MGI.
DR   GO; GO:0000281; P:cytokinesis after mitosis; IMP:MGI.
DR   GO; GO:0006887; P:exocytosis; IMP:MGI.
DR   GO; GO:0021592; P:fourth ventricle development; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0021670; P:lateral ventricle development; IMP:MGI.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0007097; P:nuclear migration; IMP:MGI.
DR   GO; GO:0001778; P:plasma membrane repair; IMP:MGI.
DR   GO; GO:0008360; P:regulation of cell shape; IMP:MGI.
DR   GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR   GO; GO:0006930; P:substrate-dependent cell migration, cell extension; IMP:MGI.
DR   GO; GO:0021678; P:third ventricle development; IMP:MGI.
DR   GO; GO:0055015; P:ventricular cardiac muscle cell development; IMP:MGI.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR002928; Myosin_tail.
DR   Pfam; PF00612; IQ; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   Pfam; PF01576; Myosin_tail_1; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 1.
DR   SMART; SM00242; MYSc; 1.
DR   PROSITE; PS50096; IQ; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; ATP-binding; Coiled coil; Motor protein; Myosin;
KW   Nucleotide-binding.
SQ   SEQUENCE   2007 AA;  232472 MW;  AEE288B572802E23 CRC64;
     MAQRTGLEDP ERYLFVDRAV IYNPATQADW TAKKLVWIPS ERHGFEAASI KEERGDEVMV
     ELAENGKKAM VNKDDIQKMN PPKFSKVEDM AELTCLNEAS VLHNLKDRYY SGLIYTYSGL
     FCVVINPYKN LPIYSENIIE MYRGKKRHEM PPHIYAISES AYRCMLQDRE DQSILCTGES
     GAGKTENTKK VIQYLAHVAS SHKGRKDHNI PQESPKPVKP QGELERQLLQ ANPILESFGN
     AKTVKNDNSS RFGKFIRINF DVTGYIVGAN IETYLLEKSR AVRQAKDERT FHIFYQLLSG
     AGEHLKSDLL LEGFNNYRFL SNGYIPIPGQ QDKDNFQETM EAMHIMGFSH EEILSMLKVV
     SSVLQFGNIS FKKERNTDQA SMPENTVAQK LCHLLGMNVM EFTRAILTPR IKVGRDYVQK
     AQTKEQADFA VEALAKATYE RLFRWLVHRI NKALDRTKRQ GASFIGILDI AGFEIFELNS
     FEQLCINYTN EKLQQLFNHT MFILEQEEYQ REGIEWNFID FGLDLQPCID LIERPANPPG
     VLALLDEECW FPKATDKTFV EKLVQEQGSH SKFQKPRQLK DKADFCIIHY AGKVDYKADE
     WLMKNMDPLN DNVATLLHQS SDRFVAELWK DEIQTIQRAS FYDSVSGLHE PPVDRIVGLD
     QVTGMTETAF GSAYKTKKGM FRTVGQLYKE SLTKLMATLR NTNPNFVRCI IPNHEKRAGK
     LDPHLVLDQL RCNGVLEGIR ICRQGFPNRI VFQEFRQRYE ILTPNAIPKG FMDGKQACER
     MIRALELDPN LYRIGQSKIF FRAGVLAHLE EERDLKITDI IIFFQAVCRG YLARKAFAKK
     QQQLSALKVL QRNCAAYLKL RHWQWWRVFT KVKPLLQVTR QEEELQAKDE ELLKVKEKQT
     KVEGELEEME RKHQQLLEEK NILAEQLQAE TELFAEAEEM RARLAAKKQE LEEILHDLES
     RVEEEEERNQ ILQNEKKKMQ AHIQDLEEQL DEEEGARQKL QLEKVTAEAK IKKMEEEVLL
     LEDQNSKFIK EKKLMEDRIA ECSSQLAEEE EKAKNLAKIR NKQEVMISDL EERLKKEEKT
     RQELEKAKRK LDGETTDLQD QIAELQAQVD ELKVQLTKKE EELQGALARG DDETLHKNNA
     LKVARELQAQ IAELQEDFES EKASRNKAEK QKRDLSEELE ALKTELEDTL DTTAAQQELR
     TKREQEVAEL KKALEDETKN HEAQIQDMRQ RHATALEELS EQLEQAKRFK ANLEKNKQGL
     ETDNKELACE VKVLQQVKAE SEHKRKKLDA QVQELHAKVS EGDRLRVELA EKANKLQNEL
     DNVSTLLEEA EKKGIKFAKD AAGLESQLQD TQELLQEETR QKLNLSSRIR QLEEEKNSLQ
     EQQEEEEEAR KNLEKQVLAL QSQLADTKKK VDDDLGTIES LEEAKKKLLK DVEALSQRLE
     EKVLAYDKLE KTKNRLQQEL DDLTVDLDHQ RQIVSNLEKK QKKFDQLLAE EKGISARYAE
     ERDRAEAEAR EKETKALSLA RALEEALEAK EEFERQNKQL RADMEDLMSS KDDVGKNVHE
     LEKSKRALEQ QVEEMRTQLE ELEDELQATE DAKLRLEVNM QAMKAQFERD LQTRDEQNEE
     KKRLLLKQVR ELEAELEDER KQRALAVASK KKMEIDLKDL EAQIEAANKA RDEVIKQLRK
     LQAQMKDYQR ELEEARASRD EIFAQSKESE KKLKSLEAEI LQLQEELASS ERARRHAEQE
     RDELADEIAN SASGKSALLD EKRRLEARIA QLEEELEEEQ SNMELLNDRF RKTTLQVDTL
     NTELAAERSA AQKSDNARQQ LERQNKELKA KLQELEGAVK SKFKATISAL EAKIGQLEEQ
     LEQEAKERAA ANKLVRRTEK KLKEIFMQVE DERRHADQYK EQMEKANARM KQLKRQLEEA
     EEEATRANAS RRKLQRELDD ATEANEGLSR EVSTLKNRLR RGGPISFSSS RSGRRQLHIE
     GASLELSDDD TESKTSDVND TQPPQSE
//
ID   SYNRG_MOUSE             Reviewed;        1306 AA.
AC   Q5SV85; Q5SV84; Q6PHT6;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Synergin gamma;
DE   AltName: Full=AP1 subunit gamma-binding protein 1;
DE   AltName: Full=Gamma-synergin;
GN   Name=Synrg; Synonyms=Ap1gbp1, Syng;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12808037; DOI=10.1091/mbc.E02-11-0735;
RA   Lui W.W.Y., Collins B.M., Hirst J., Motley A., Millar C., Schu P.,
RA   Owen D.J., Robinson M.S.;
RT   "Binding partners for the COOH-terminal appendage domains of the GGAs
RT   and gamma-adaptin.";
RL   Mol. Biol. Cell 14:2385-2398(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-974, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-744, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May play a role in endocytosis and/or membrane
CC       trafficking at the trans-Golgi network (TGN). May act by linking
CC       the adapter protein complex AP-1 to other proteins (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with SCAMP1 via its EH-domain. Interacts with
CC       GGA1, GGA2 and GGA3. Interacts with the AP1G1 and AP1G2 subunits
CC       of the adapter protein complexes AP-1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Golgi apparatus, trans-
CC       Golgi network membrane; Peripheral membrane protein.
CC       Note=Associated with membranes of the TGN, colocalizes with AP1G1
CC       (By similarity). Associates with membranes via the adapter protein
CC       complex AP-1.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5SV85-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SV85-2; Sequence=VSP_013251, VSP_013252, VSP_013253,
CC                                  VSP_013254;
CC   -!- DOMAIN: The DFXDF motifs mediate the interaction with gamma-
CC       appendage subunits AP1G1 and AP1G2 (By similarity).
CC   -!- SIMILARITY: Contains 1 EH domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI25511.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
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DR   EMBL; AL645615; CAI25509.1; -; Genomic_DNA.
DR   EMBL; AL645615; CAI25510.1; -; Genomic_DNA.
DR   EMBL; AL645615; CAI25511.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC056370; AAH56370.1; -; mRNA.
DR   IPI; IPI00380008; -.
DR   IPI; IPI00515622; -.
DR   RefSeq; NP_001108481.1; NM_001115009.1.
DR   RefSeq; NP_919322.1; NM_194341.1.
DR   UniGene; Mm.82680; -.
DR   ProteinModelPortal; Q5SV85; -.
DR   SMR; Q5SV85; 298-376.
DR   STRING; Q5SV85; -.
DR   PhosphoSite; Q5SV85; -.
DR   PRIDE; Q5SV85; -.
DR   Ensembl; ENSMUST00000049714; ENSMUSP00000059000; ENSMUSG00000034940.
DR   Ensembl; ENSMUST00000092834; ENSMUSP00000090510; ENSMUSG00000034940.
DR   GeneID; 217030; -.
DR   KEGG; mmu:217030; -.
DR   UCSC; uc007kqa.1; mouse.
DR   CTD; 217030; -.
DR   MGI; MGI:1354742; Synrg.
DR   GeneTree; ENSGT00390000010789; -.
DR   HOGENOM; HBG444264; -.
DR   HOVERGEN; HBG055053; -.
DR   InParanoid; Q5SV85; -.
DR   OMA; MFSSVNC; -.
DR   OrthoDB; EOG4P5K8D; -.
DR   PhylomeDB; Q5SV85; -.
DR   NextBio; 375518; -.
DR   ArrayExpress; Q5SV85; -.
DR   Bgee; Q5SV85; -.
DR   CleanEx; MM_AP1GBP1; -.
DR   Genevestigator; Q5SV85; -.
DR   GermOnline; ENSMUSG00000034940; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR000261; EPS15_homology.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   PROSITE; PS50031; EH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW   Endocytosis; Golgi apparatus; Membrane; Phosphoprotein;
KW   Protein transport; Repeat; Transport.
FT   CHAIN         1   1306       Synergin gamma.
FT                                /FTId=PRO_0000072388.
FT   DOMAIN      293    404       EH.
FT   REGION      514    778       Interaction with A1P1G1 and A1P1G2 (By
FT                                similarity).
FT   COILED      113    153       Potential.
FT   MOTIF       455    459       DFXDF motif 1.
FT   MOTIF       685    689       DFXDF motif 2.
FT   MOTIF       767    771       DFXDF motif 3.
FT   MOD_RES     471    471       Phosphoserine (By similarity).
FT   MOD_RES     509    509       N6-acetyllysine (By similarity).
FT   MOD_RES     736    736       N6-acetyllysine (By similarity).
FT   MOD_RES     744    744       Phosphoserine.
FT   MOD_RES     844    844       Phosphoserine (By similarity).
FT   MOD_RES     847    847       Phosphoserine (By similarity).
FT   MOD_RES     901    901       Phosphoserine (By similarity).
FT   MOD_RES     911    911       Phosphoserine (By similarity).
FT   MOD_RES     927    927       Phosphoserine (By similarity).
FT   MOD_RES     928    928       Phosphoserine (By similarity).
FT   MOD_RES     974    974       Phosphoserine.
FT   MOD_RES    1065   1065       Phosphoserine (By similarity).
FT   MOD_RES    1067   1067       Phosphoserine (By similarity).
FT   VAR_SEQ      38     38       Missing (in isoform 2).
FT                                /FTId=VSP_013251.
FT   VAR_SEQ     195    272       Missing (in isoform 2).
FT                                /FTId=VSP_013252.
FT   VAR_SEQ     862    938       Missing (in isoform 2).
FT                                /FTId=VSP_013253.
FT   VAR_SEQ    1252   1263       Missing (in isoform 2).
FT                                /FTId=VSP_013254.
SQ   SEQUENCE   1306 AA;  139616 MW;  EB149A0B7ADAE2D7 CRC64;
     MALRPGAGAS GAAGAGAGPG GAGSFMFPVA GGMRPPQAGL IPMQQQGFPM VSVMQPNMQG
     MMGMNYSSQM SQGPIAMQAG IPMGPMPAAG VPFLGQPPFL SMRPAGPQYT PDMQKQFAEE
     QQKRFEQQQK LLEEERKRRQ FEEQKQKLRL LSSVKPKTGE KNRDDALEAI KGNLDGFSRD
     AKMHPTPASH PKKQGPSLEE KLLVSCDVSA SGQEHIKLNT PDAGHKAIVP GSSKNCPGLM
     AHNRGAVDGC VSGPASAEAE KTSDQTLSKE ESGVGVFPSQ DPAQSRMPPW IYNESLVPDA
     YKKILETTMT PTGIDTAKLY PILMSSGLPR ETLGQIWALA NRTTPGRLTK EELYTVLAMV
     AVTQRGVPAM SPDALSQFPA APIPTLSGFP MTLPTPVSQP TAMPSGPTGS MPLTLGQPIM
     GINLVGPVGG AAAPTSSGFM PAYPSNQVGK TEEDDFQDFQ DASKSGSIDD SFTDFQEMPA
     SSKTSNSQHG NSAPSLLIPF PGTKASTDKY AVFKGISTDK PSENPASFGE SGDKYSAFRE
     LEQTTDSKPL GESFAEFRST GTDDGFTDFK TADSVSPLEP PTKDTFPSAF ASGAAQQTQT
     QVKTPLNLED LDMFSSVDCS GEKQVPFSAT FSTAKSVSTR PQPAGSAAAS AALASTKTSS
     LADDFGEFNL FGEYSNPASA GEQDDFADFM AFGNSSISSE PKASDKYEAL REEVSPSPLS
     SSTVEGAQHP PAAATKYDVF KQLSLEGAGL AMEEFKENTS STKSEDDFAD FHSSKFSSTS
     SDKSLGEKAV AFRHAKEDSS SVKSLDLPSI GGSSVGKEDS EDALSVQFDM KLADVGGDLK
     HVMSDSSLDL PTVSGQHPPA ADTEDLSCAA FGSCSSHFTV STLTSCEWSD RADALQGRKL
     SPFVLSAGSR SFSATSNLHT KEISFGSSEN ITMSSLSKGS ALASEDALPE TAFPAFASFK
     DMMPQTTEQK EFESGDFQDF TRQDMPTVDR SQETSCPSPA SSVASHETPK EGADDFGEFQ
     SEKSKISKFD FLVANSQSKM KSSEEMIKSE LATFDLSVQG SHKRSLSLGD KEISRSSPSP
     ALEQPFRDRS NTLSERAALP VIRDKYKDLT GEVEENERYA YEWQRCLGSA LDVIKKANDT
     LNGISSSAVC TEVIQSAQGM EYLLGVVEVY RVTKRVELGI KATAVCSEKL QQLLKDIDKV
     WNNLIGFMSL ATLTPDENSL DFSSCMLRPG IKNAQELACG VCLLNVDSRS RKEETPAEEQ
     PKKAFNSETD SFKLAYGGHQ YHASCANFWI NCVEPKPPGL LLPDLL
//
ID   Q5SVI1_MOUSE            Unreviewed;       589 AA.
AC   Q5SVI1;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   SubName: Full=Calcium/calmodulin-dependent protein kinase II, beta;
GN   Name=Camk2b; ORFNames=RP23-340E18.5-002;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Howden P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Collins J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AL611926; CAI24954.1; -; Genomic_DNA.
DR   EMBL; AL645469; CAI24954.1; JOINED; Genomic_DNA.
DR   EMBL; AL645469; CAI25256.1; -; Genomic_DNA.
DR   EMBL; AL611926; CAI25256.1; JOINED; Genomic_DNA.
DR   IPI; IPI00649296; -.
DR   UniGene; Mm.439733; -.
DR   ProteinModelPortal; Q5SVI1; -.
DR   SMR; Q5SVI1; 11-301, 457-583.
DR   STRING; Q5SVI1; -.
DR   PRIDE; Q5SVI1; -.
DR   Ensembl; ENSMUST00000093355; ENSMUSP00000091046; ENSMUSG00000057897.
DR   MGI; MGI:88257; Camk2b.
DR   HOVERGEN; HBG108055; -.
DR   OrthoDB; EOG42JNR7; -.
DR   PhylomeDB; Q5SVI1; -.
DR   ArrayExpress; Q5SVI1; -.
DR   Bgee; Q5SVI1; -.
DR   Genevestigator; Q5SVI1; -.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0051233; C:spindle midzone; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IDA:MGI.
DR   GO; GO:0060466; P:activation of meiosis involved in egg activation; IMP:MGI.
DR   GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI.
DR   GO; GO:0031558; P:induction of apoptosis in response to chemical stimulus; IDA:MGI.
DR   GO; GO:0002030; P:inhibitory G-protein coupled receptor phosphorylation; IDA:MGI.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; IMP:MGI.
DR   GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:MGI.
DR   GO; GO:0032222; P:regulation of synaptic transmission, cholinergic; IMP:MGI.
DR   GO; GO:0046686; P:response to cadmium ion; IDA:MGI.
DR   InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF08332; CaMKII_AD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Transferase.
SQ   SEQUENCE   589 AA;  65035 MW;  C108DE09A21A24CB CRC64;
     MATTVTCTRF TDEYQLYEDI GKGAFSVVRR CVKLCTGHEY AAKIINTKKL SARDHQKLER
     EARICRLLKH SNIVRLHDSI SEEGFHYLVF DLVTGGELFE DIVAREYYSE ADASHCIQQI
     LEAVLHCHQM GVVHRDLKPE NLLLASKCKG AAVKLADFGL AIEVQGDQQA WFGFAGTPGY
     LSPEVLRKEA YGKPVDIWAC GVILYILLVG YPPFWDEDQH KLYQQIKAGA YDFPSPEWDT
     VTPEAKNLIN QMLTINPAKR ITAHEALKHP WVCQRSTVAS MMHRQETVEC LKKFNARRKL
     KGAILTTMLA TRNFSAAKSL LNKKADGVKP QTNSTKNSSA ITSPKGSLPP AALESSDSTN
     TTIEDEDAKA PRISDILNSV RRGCGTPEAE GPLSVGPPPC LSPGLLGPLP TPSPRISDIL
     NSVRRGSGTP EAEGLPPVGP PPCPSPTLPG PLPTPSRKQE IIKTTEQLIE AVNNGDFEAY
     AKICDPGLTS FEPEALGNLV EGMDFHRFYF ENLLAKNSKP IHTTILNPHV HVIGEDAACI
     AYIRLTQYID GQGRPRTSQS EETRVWHRRD GKWQNVHFHC SGAPVAPLQ
//
ID   Q5SVJ0_MOUSE            Unreviewed;       666 AA.
AC   Q5SVJ0;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   SubName: Full=Calcium/calmodulin-dependent protein kinase II, beta;
DE   SubName: Full=Calcium/calmodulin-dependent protein kinase II, beta, isoform CRA_b;
GN   Name=Camk2b; ORFNames=RP23-340E18.5-009, mCG_122182;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Howden P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RA   Collins J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL611926; CAI24951.1; -; Genomic_DNA.
DR   EMBL; AL645469; CAI24951.1; JOINED; Genomic_DNA.
DR   EMBL; AL645469; CAI25261.1; -; Genomic_DNA.
DR   EMBL; AL611926; CAI25261.1; JOINED; Genomic_DNA.
DR   EMBL; CH466574; EDL40571.1; -; Genomic_DNA.
DR   IPI; IPI00649778; -.
DR   UniGene; Mm.439733; -.
DR   ProteinModelPortal; Q5SVJ0; -.
DR   SMR; Q5SVJ0; 11-301, 534-660.
DR   STRING; Q5SVJ0; -.
DR   PRIDE; Q5SVJ0; -.
DR   Ensembl; ENSMUST00000019133; ENSMUSP00000019133; ENSMUSG00000057897.
DR   MGI; MGI:88257; Camk2b.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108055; -.
DR   InParanoid; Q5SVJ0; -.
DR   OMA; VGPPPCL; -.
DR   PhylomeDB; Q5SVJ0; -.
DR   ArrayExpress; Q5SVJ0; -.
DR   Bgee; Q5SVJ0; -.
DR   Genevestigator; Q5SVJ0; -.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0051233; C:spindle midzone; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IDA:MGI.
DR   GO; GO:0060466; P:activation of meiosis involved in egg activation; IMP:MGI.
DR   GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI.
DR   GO; GO:0031558; P:induction of apoptosis in response to chemical stimulus; IDA:MGI.
DR   GO; GO:0002030; P:inhibitory G-protein coupled receptor phosphorylation; IDA:MGI.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; IMP:MGI.
DR   GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:MGI.
DR   GO; GO:0032222; P:regulation of synaptic transmission, cholinergic; IMP:MGI.
DR   GO; GO:0046686; P:response to cadmium ion; IDA:MGI.
DR   InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF08332; CaMKII_AD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Transferase.
SQ   SEQUENCE   666 AA;  72903 MW;  6A1F33857752D69E CRC64;
     MATTVTCTRF TDEYQLYEDI GKGAFSVVRR CVKLCTGHEY AAKIINTKKL SARDHQKLER
     EARICRLLKH SNIVRLHDSI SEEGFHYLVF DLVTGGELFE DIVAREYYSE ADASHCIQQI
     LEAVLHCHQM GVVHRDLKPE NLLLASKCKG AAVKLADFGL AIEVQGDQQA WFGFAGTPGY
     LSPEVLRKEA YGKPVDIWAC GVILYILLVG YPPFWDEDQH KLYQQIKAGA YDFPSPEWDT
     VTPEAKNLIN QMLTINPAKR ITAHEALKHP WVCQRSTVAS MMHRQETVEC LKKFNARRKL
     KGAILTTMLA TRNFSVGRQT TAPATMSTAA SGTTMGLVEQ AKSLLNKKAD GVKPQTNSTK
     NSSAITSPKG SLPPAALEPQ TTVIHNPVDG IKESSDSTNT TIEDEDAKAP RVPDVLSLVR
     RASGAPEAEG PLSCQSPVPI SPLPTPSPRI SDILNSVRRG CGTPEAEGPL SVGPPPCLSP
     GLLGPLPTPS PRISDILNSV RRGSGTPEAE GLPPVGPPPC PSPTLPGPLP TPSRKQEIIK
     TTEQLIEAVN NGDFEAYAKI CDPGLTSFEP EALGNLVEGM DFHRFYFENL LAKNSKPIHT
     TILNPHVHVI GEDAACIAYI RLTQYIDGQG RPRTSQSEET RVWHRRDGKW QNVHFHCSGA
     PVAPLQ
//
ID   RPGP2_MOUSE             Reviewed;         712 AA.
AC   Q5SVL6; Q3KNA3; Q3V3L0; Q80TL8;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=Rap1 GTPase-activating protein 2;
DE            Short=Rap1GAP2;
DE   AltName: Full=GTPase-activating Rap/Ran-GAP domain-like protein 4;
GN   Name=Rap1gap2; Synonyms=Garnl4, Kiaa1039, Rap1ga2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 243-712.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 382-712.
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: GTPase activator for the nuclear Ras-related regulatory
CC       protein RAP-1A (KREV-1), converting it to the putatively inactive
CC       GDP-bound state (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5SVL6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SVL6-2; Sequence=VSP_029890, VSP_029952;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 Rap-GAP domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65706.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC       Sequence=BAC65706.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL645971; CAI25407.1; -; Genomic_DNA.
DR   EMBL; AL604065; CAI25407.1; JOINED; Genomic_DNA.
DR   EMBL; AL627348; CAI25407.1; JOINED; Genomic_DNA.
DR   EMBL; AL604065; CAI24516.1; -; Genomic_DNA.
DR   EMBL; AL627348; CAI24516.1; JOINED; Genomic_DNA.
DR   EMBL; AL645971; CAI24516.1; JOINED; Genomic_DNA.
DR   EMBL; AL627348; CAI25645.1; -; Genomic_DNA.
DR   EMBL; AL604065; CAI25645.1; JOINED; Genomic_DNA.
DR   EMBL; AL645971; CAI25645.1; JOINED; Genomic_DNA.
DR   EMBL; BC107388; AAI07389.1; -; mRNA.
DR   EMBL; AK038834; BAE20542.1; -; mRNA.
DR   EMBL; AK122424; BAC65706.1; ALT_SEQ; mRNA.
DR   IPI; IPI00461277; -.
DR   IPI; IPI00875755; -.
DR   RefSeq; NP_001015046.1; NM_001015046.2.
DR   UniGene; Mm.425690; -.
DR   HSSP; P47736; 1SRQ.
DR   ProteinModelPortal; Q5SVL6; -.
DR   SMR; Q5SVL6; 128-460.
DR   PhosphoSite; Q5SVL6; -.
DR   PRIDE; Q5SVL6; -.
DR   Ensembl; ENSMUST00000047488; ENSMUSP00000040180; ENSMUSG00000038807.
DR   Ensembl; ENSMUST00000102521; ENSMUSP00000099580; ENSMUSG00000038807.
DR   Ensembl; ENSMUST00000108454; ENSMUSP00000104094; ENSMUSG00000038807.
DR   GeneID; 380711; -.
DR   KEGG; mmu:380711; -.
DR   UCSC; uc007kbx.1; mouse.
DR   CTD; 380711; -.
DR   MGI; MGI:3028623; Rap1gap2.
DR   GeneTree; ENSGT00550000074284; -.
DR   HOGENOM; HBG445308; -.
DR   HOVERGEN; HBG016371; -.
DR   InParanoid; Q5SVL6; -.
DR   OMA; IYQKARQ; -.
DR   OrthoDB; EOG42Z4PM; -.
DR   NextBio; 401143; -.
DR   ArrayExpress; Q5SVL6; -.
DR   Bgee; Q5SVL6; -.
DR   CleanEx; MM_GARNL4; -.
DR   Genevestigator; Q5SVL6; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR000331; Rap_GAP.
DR   Pfam; PF02145; Rap_GAP; 1.
DR   PROSITE; PS50085; RAPGAP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; GTPase activation; Phosphoprotein.
FT   CHAIN         1    712       Rap1 GTPase-activating protein 2.
FT                                /FTId=PRO_0000312717.
FT   DOMAIN      229    445       Rap-GAP.
FT   COMPBIAS    553    709       Ser-rich.
FT   MOD_RES      26     26       Phosphoserine (By similarity).
FT   MOD_RES      30     30       Phosphothreonine (By similarity).
FT   MOD_RES     525    525       Phosphoserine (By similarity).
FT   MOD_RES     590    590       Phosphoserine (By similarity).
FT   MOD_RES     594    594       Phosphoserine.
FT   VAR_SEQ       1    194       Missing (in isoform 2).
FT                                /FTId=VSP_029890.
FT   VAR_SEQ     195    206       LSKLPSVPQIAK -> MVLDLCVFLPSQ (in isoform
FT                                2).
FT                                /FTId=VSP_029952.
SQ   SEQUENCE   712 AA;  78254 MW;  49FD87D1AF030A57 CRC64;
     MLAGLKVKKQ ELANSSDVTL PDRPLSPPLT APPTMKSAEF FEMLEKMQGI KLEEQRPGPQ
     KNKDDYIPYP SIDEVVEKGG PYPLIILPQF GGYWIEDPEN VGTPTSLGSS VYEEEEEDSL
     SPNTFGYKLE CRGEARAYRR HFLGKDHLNF YCTGSSLGNL ILSIKCEEAE GMEYLRIILR
     SKLKTVHERI PLAGLSKLPS VPQIAKAFCD DAVGLKFNPV LYPKASQMIV SYDEHDVNNT
     FKFGVIYQKA RQTLEEELFG NNEESPAFKE FLDLLGDTIT LQDFKGFRGG LDVTHGQTGV
     ESVYTTFRDR EIMFHVSTKL PFTDGDTQQL QRKRHIGNDI VAIIFQEENT PFVPDMIASN
     FLHAYIVVQA DNPGTETPSY KVSVTAREDV PAFGPPLPSP PVFQKGAEFR EFLLTKLTNA
     ENACCKSDKF AKLEDRTRAA LLDNLHDELH THTQVMLGMG PEEDKFENGG HGGFLESFKR
     AIRVRSHSME TMVGSQRKLH GGNLPGSLSG GIVHNSMEVT KTTFSPPVAA ATAKNQSRSP
     IKRRSGLFPR LHSGSEGQGD SRTRCDSASS TPKTPDGGHS SQEIKSETSS NPSSPEICPN
     KEKPFIKLKE NGRANISRSS SSTSSFSSTA GEGEAMEECD SGSSQPSTTS PFKQEVFAYS
     PSPSSESPSL GAAATPIIMS RSPTDAKSRN SPRSNLKFRF DKLSHASSSA GH
//
ID   MYST2_MOUSE             Reviewed;         613 AA.
AC   Q5SVQ0; Q5SVQ1; Q5SVQ2; Q5SVQ3; Q5SVQ7; Q6PGC6; Q80Y65;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Histone acetyltransferase MYST2;
DE            Short=MYST-2;
DE            EC=2.3.1.48;
DE   AltName: Full=Histone acetyltransferase binding to ORC1;
DE   AltName: Full=MOZ, YBF2/SAS3, SAS2 and TIP60 protein 2;
GN   Name=Myst2; Synonyms=Hbo1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Component of the HBO1 complex which has a histone H4-
CC       specific acetyltransferase activity, a reduced activity toward
CC       histone H3 and is responsible for the bulk of histone H4
CC       acetylation in vivo. Through chromatin acetylation it may regulate
CC       DNA replication and act as a coactivator of TP53-dependent
CC       transcription. Specifically represses AR-mediated transcription
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + [histone] = CoA + acetyl-
CC       [histone].
CC   -!- SUBUNIT: Component of the HBO1 complex composed at least of ING4
CC       or ING5, MYST2/HBO1, MEAF6, and one of PHF15, PHF16 and PHF17.
CC       Interacts with MCM2 and ORC1L. Interacts with the androgen
CC       receptor (AR) in the presence of dihydrotestosterone (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q5SVQ0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SVQ0-2; Sequence=VSP_014584;
CC       Name=3;
CC         IsoId=Q5SVQ0-3; Sequence=VSP_014582;
CC       Name=4;
CC         IsoId=Q5SVQ0-4; Sequence=VSP_014582, VSP_014584;
CC       Name=5;
CC         IsoId=Q5SVQ0-5; Sequence=VSP_014582, VSP_014583, VSP_014584;
CC   -!- DOMAIN: The C2HC-type zinc finger is required for interaction with
CC       MCM2 and ORC1L (By similarity).
CC   -!- DOMAIN: The N-terminus is involved in transcriptional repression,
CC       while the C-terminus mediates AR-interaction (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC   -!- SIMILARITY: Contains 1 C2HC-type zinc finger.
CC   -----------------------------------------------------------------------
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DR   EMBL; AL627222; CAI24800.1; -; Genomic_DNA.
DR   EMBL; AL627222; CAI24801.1; -; Genomic_DNA.
DR   EMBL; AL627222; CAI24802.1; -; Genomic_DNA.
DR   EMBL; AL627222; CAI24803.1; -; Genomic_DNA.
DR   EMBL; AL627222; CAI24804.1; -; Genomic_DNA.
DR   EMBL; AL627222; CAI24805.1; -; Genomic_DNA.
DR   EMBL; BC057102; AAH57102.1; -; mRNA.
DR   EMBL; BC048904; AAH48904.1; -; mRNA.
DR   IPI; IPI00228457; -.
DR   IPI; IPI00403506; -.
DR   IPI; IPI00515403; -.
DR   IPI; IPI00607967; -.
DR   IPI; IPI00608043; -.
DR   RefSeq; NP_001181932.1; NM_001195003.1.
DR   RefSeq; NP_001181933.1; NM_001195004.1.
DR   RefSeq; NP_808287.1; NM_177619.3.
DR   UniGene; Mm.205400; -.
DR   ProteinModelPortal; Q5SVQ0; -.
DR   SMR; Q5SVQ0; 182-214, 342-609.
DR   STRING; Q5SVQ0; -.
DR   PhosphoSite; Q5SVQ0; -.
DR   PRIDE; Q5SVQ0; -.
DR   Ensembl; ENSMUST00000092766; ENSMUSP00000090441; ENSMUSG00000038909.
DR   Ensembl; ENSMUST00000103159; ENSMUSP00000099448; ENSMUSG00000038909.
DR   Ensembl; ENSMUST00000107733; ENSMUSP00000103361; ENSMUSG00000038909.
DR   Ensembl; ENSMUST00000107734; ENSMUSP00000103362; ENSMUSG00000038909.
DR   GeneID; 217127; -.
DR   KEGG; mmu:217127; -.
DR   UCSC; uc007lad.1; mouse.
DR   UCSC; uc007lae.1; mouse.
DR   UCSC; uc007laf.1; mouse.
DR   CTD; 217127; -.
DR   MGI; MGI:2182799; Myst2.
DR   GeneTree; ENSGT00550000074503; -.
DR   HOVERGEN; HBG053268; -.
DR   InParanoid; Q5SVQ0; -.
DR   OMA; VYSTRRV; -.
DR   OrthoDB; EOG4BCDMN; -.
DR   PhylomeDB; Q5SVQ0; -.
DR   BRENDA; 2.3.1.48; 244.
DR   NextBio; 375581; -.
DR   ArrayExpress; Q5SVQ0; -.
DR   Bgee; Q5SVQ0; -.
DR   CleanEx; MM_MYST2; -.
DR   Genevestigator; Q5SVQ0; -.
DR   GermOnline; ENSMUSG00000038909; Mus musculus.
DR   GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:EC.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR   GO; GO:0043966; P:histone H3 acetylation; ISS:UniProtKB.
DR   GO; GO:0043983; P:histone H4-K12 acetylation; ISS:UniProtKB.
DR   GO; GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
DR   GO; GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR002717; MOZ_SAS.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR002515; Znf_C2HC.
DR   Gene3D; G3DSA:3.40.630.30; Acyl_CoA_acyltransferase; 1.
DR   Pfam; PF01853; MOZ_SAS; 1.
DR   Pfam; PF01530; zf-C2HC; 1.
DR   SMART; SM00355; ZnF_C2H2; 1.
DR   SUPFAM; SSF55729; Acyl_CoA_acyltransferase; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Acyltransferase; Alternative splicing;
KW   Chromatin regulator; DNA replication; Metal-binding; Nucleus;
KW   Phosphoprotein; Transcription; Transcription regulation; Transferase;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    613       Histone acetyltransferase MYST2.
FT                                /FTId=PRO_0000051570.
FT   ZN_FING     368    390       C2HC-type.
FT   REGION      484    490       Acetyl-CoA binding (By similarity).
FT   COMPBIAS     12     59       Ser-rich.
FT   ACT_SITE    476    476       Nucleophile (By similarity).
FT   BINDING     479    479       Acetyl-CoA (By similarity).
FT   BINDING     514    514       Acetyl-CoA (By similarity).
FT   MOD_RES      52     52       Phosphoserine (By similarity).
FT   MOD_RES      54     54       Phosphoserine (By similarity).
FT   MOD_RES      55     55       Phosphoserine (By similarity).
FT   MOD_RES      58     58       Phosphoserine (By similarity).
FT   MOD_RES      59     59       Phosphoserine (By similarity).
FT   MOD_RES      87     87       Phosphothreonine (By similarity).
FT   MOD_RES      90     90       Phosphothreonine (By similarity).
FT   MOD_RES     101    101       Phosphoserine (By similarity).
FT   MOD_RES     102    102       Phosphoserine (By similarity).
FT   MOD_RES     104    104       Phosphoserine (By similarity).
FT   MOD_RES     106    106       Phosphothreonine (By similarity).
FT   MOD_RES     126    126       Phosphoserine (By similarity).
FT   MOD_RES     130    130       Phosphothreonine (By similarity).
FT   MOD_RES     201    201       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1      6       MAIGVV -> MPRR (in isoform 3, isoform 4
FT                                and isoform 5).
FT                                /FTId=VSP_014582.
FT   VAR_SEQ      57    115       Missing (in isoform 5).
FT                                /FTId=VSP_014583.
FT   VAR_SEQ     224    253       Missing (in isoform 2, isoform 4 and
FT                                isoform 5).
FT                                /FTId=VSP_014584.
FT   CONFLICT    429    429       L -> P (in Ref. 2; AAH57102).
FT   CONFLICT    545    548       EISQ -> GPDR (in Ref. 1; CAI24805).
SQ   SEQUENCE   613 AA;  70641 MW;  7D6F05EE90A7134E CRC64;
     MAIGVVKRNA GSSSDGTEDS DFSTDLEHTD SSESDGTSRR SARVTRSSAR LSQSSQDSSP
     VRNLPSFGTE EPAYSTRRVT RSQQQPTPVT PKKYPLRQTR SSGSETEQVV DFSDRETKNT
     ADHDESPPRT PTGNAPSSES DIDISSPNVS HDESIAKDMS LKDSGSDLSH RPKRRRFHES
     YNFNMKCPTP GCNSLGHLTG KHERHFSISG CPLYHNLSAD ECKVRAQSRD KQIEERMLSH
     RQDDNNRHAT RHQAPTERQL RYKEKVAELR KKRNSGLSKE QKEKYMEHRQ TYGNTREPLL
     ENLTSEYDLD LFRRAQARAS EDLEKLRLQG QITEGSNMIK TIAFGRYELD TWYHSPYPEE
     YARLGRLYMC EFCLKYMKSQ TILRRHMAKC VWKHPPGDEI YRKGSISVFE VDGKKNKIYC
     QNLCLLAKLF LDHKTLYYDV EPFLFYVMTE ADNTGCHLIG YFSKEKNSFL NYNVSCILTM
     PQYMRQGYGK MLIDFSYLLS KVEEKVGSPE RPLSDLGLIS YRSYWKEVLL RYLHNFQGKE
     ISIKEISQET AVNPVDIVST LQALQMLKYW KGKHLVLKRQ DLIDEWIAKE AKRSNSNKTM
     DPSCLKWTPP KGT
//
ID   TBC9B_MOUSE             Reviewed;        1263 AA.
AC   Q5SVR0; Q3UGF5; Q6A019; Q6P1G9; Q6PDP2; Q80ZU6; Q8C7K9; Q8CBR7;
AC   Q8CCW2; Q9CSQ2;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=TBC1 domain family member 9B;
GN   Name=Tbc1d9b; Synonyms=Kiaa0676;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryo, Hippocampus, Medulla oblongata, Melanocyte, and
RC   Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 797-1263 (ISOFORM 1).
RC   TISSUE=Brain, Eye, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May act as a GTPase-activating protein for Rab family
CC       protein(s).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5SVR0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SVR0-2; Sequence=VSP_025700;
CC   -!- SIMILARITY: Contains 1 EF-hand domain.
CC   -!- SIMILARITY: Contains 2 GRAM domains.
CC   -!- SIMILARITY: Contains 1 Rab-GAP TBC domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC27640.1; Type=Erroneous initiation;
CC       Sequence=BAD32277.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK172999; BAD32277.1; ALT_INIT; mRNA.
DR   EMBL; AK012224; BAB28107.1; -; mRNA.
DR   EMBL; AK031992; BAC27640.1; ALT_INIT; mRNA.
DR   EMBL; AK035457; BAC29068.1; -; mRNA.
DR   EMBL; AK049999; BAC34024.2; -; mRNA.
DR   EMBL; AK147964; BAE28254.1; -; mRNA.
DR   EMBL; AL627187; CAI25112.1; -; Genomic_DNA.
DR   EMBL; AL627187; CAI25113.1; -; Genomic_DNA.
DR   EMBL; BC048085; AAH48085.1; -; mRNA.
DR   EMBL; BC058596; AAH58596.1; -; mRNA.
DR   EMBL; BC062928; AAH62928.1; -; mRNA.
DR   EMBL; BC065080; AAH65080.1; -; mRNA.
DR   IPI; IPI00453611; -.
DR   IPI; IPI00649505; -.
DR   RefSeq; NP_084021.2; NM_029745.2.
DR   UniGene; Mm.290975; -.
DR   UniGene; Mm.413847; -.
DR   ProteinModelPortal; Q5SVR0; -.
DR   SMR; Q5SVR0; 482-792, 803-928.
DR   PhosphoSite; Q5SVR0; -.
DR   PRIDE; Q5SVR0; -.
DR   Ensembl; ENSMUST00000093138; ENSMUSP00000090825; ENSMUSG00000036644.
DR   Ensembl; ENSMUST00000101270; ENSMUSP00000098828; ENSMUSG00000036644.
DR   GeneID; 76795; -.
DR   KEGG; mmu:76795; -.
DR   UCSC; uc007irr.1; mouse.
DR   CTD; 76795; -.
DR   MGI; MGI:1924045; Tbc1d9b.
DR   eggNOG; roNOG10238; -.
DR   GeneTree; ENSGT00580000081243; -.
DR   HOVERGEN; HBG054142; -.
DR   InParanoid; Q5SVR0; -.
DR   OMA; GLKIKDQ; -.
DR   OrthoDB; EOG4JQ3WT; -.
DR   PhylomeDB; Q5SVR0; -.
DR   NextBio; 345829; -.
DR   ArrayExpress; Q5SVR0; -.
DR   Bgee; Q5SVR0; -.
DR   CleanEx; MM_TBC1D9B; -.
DR   Genevestigator; Q5SVR0; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005097; F:Rab GTPase activator activity; IEA:InterPro.
DR   GO; GO:0032313; P:regulation of Rab GTPase activity; IEA:InterPro.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR004182; GRAM.
DR   InterPro; IPR000195; RabGAP/TBC_dom.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF02893; GRAM; 2.
DR   Pfam; PF00566; TBC; 1.
DR   SMART; SM00568; GRAM; 2.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; RabGAP_TBC; 2.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; GTPase activation; Membrane; Phosphoprotein;
KW   Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN         1   1263       TBC1 domain family member 9B.
FT                                /FTId=PRO_0000288502.
FT   TRANSMEM    669    689       Helical; (Potential).
FT   DOMAIN      142    209       GRAM 1.
FT   DOMAIN      288    356       GRAM 2.
FT   DOMAIN      509    696       Rab-GAP TBC.
FT   DOMAIN      880    915       EF-hand.
FT   MOD_RES     412    412       Phosphoserine (By similarity).
FT   MOD_RES     433    433       Phosphoserine (By similarity).
FT   MOD_RES     436    436       Phosphoserine (By similarity).
FT   MOD_RES     464    464       Phosphoserine (By similarity).
FT   VAR_SEQ     957    973       Missing (in isoform 2).
FT                                /FTId=VSP_025700.
FT   CONFLICT     73     73       I -> T (in Ref. 1; BAD32277).
FT   CONFLICT    161    163       SCN -> PCT (in Ref. 1; BAD32277).
FT   CONFLICT    415    415       D -> A (in Ref. 1; BAD32277).
FT   CONFLICT    807    807       Missing (in Ref. 1; BAD32277).
FT   CONFLICT   1225   1225       V -> M (in Ref. 2; BAE28254).
SQ   SEQUENCE   1263 AA;  141779 MW;  2D12CE5E297D723E CRC64;
     MWLGPEEVLV ANALWVTERA NPFFVLQRRR GHGKGGGLTG LLVGTLDVVL DSSARVAPYR
     ILHQTQDSQV YWIVACGSSR KEITKHWEWL ENNLLQTLSI FDNEEDITTF VKGKIHGIIA
     EENKNLQPQG DEDPGKFKEA ELKMRKQFGM PEGEKLVNYY SCNFWKGRVP RQGWLYLTVN
     HLCFYSFLLG KEVSLVVQWV DVTRLEKNAT LLFPESIRVD TRDQELFFSM FLNIGETFKL
     MEQLANLAMR QLLDSEGFLE DKALPRPIRP HKNISALKRD LDARAKNECY RATFRLPKDE
     RLDGHTGCTL WTPFNKLHIP GQMFISNNYI CFASKEEDAC RLIIPLREVT IVEKADSSSV
     LPSPLSISTK SKMTFLFANL KDRDFLVQRI SDFLQKTPSK QTGSSIGGTK ASVSDPAPES
     LPTPQEASEP PASPSSPLSS PPSFSTQEIP TTSQGLLKVF QKNSPMEDLG AKGAKEKMKE
     ESWNIHFFEY GRGMCMYRTA KTRELVLKGI PESLRGELWL LFSGAWNEMV THPGYYAELV
     EKSLGKYSLA TEEIERDLHR SMPEHPAFQN ELGIAALRRV LTAYAFRNPT IGYCQAMNIV
     TSVLLLYGSE EEAFWLLVAL CERMLPDYYN TRVVGALVDQ GIFEELTRDV LPRLSEKMQE
     LGVISSISLS WFLTLFLSVM PFESAVVIVD CFFYEGIKVI LQVALAVLDA NVEQLLDCND
     EGEAMTVLGR YLDNVVNKQS ISPPIPHLHA LLTSGDDPPV EVDIFDLLRV SYEKFSNLRA
     DDIEQMRFKQ RLKVIQSLED TAKRSVVRAI PGDIGFSIEE LEDLYMVFKA KHLASQYWGG
     NRSAAVHRDP SLPYLEQYRI DASQFRELFA SLTPWACGSH TPVLAGRMFR LLDQNKDSLI
     NFKEFVTGMS GMYHGDLTEK LKALYKLHLP PALIPEEAES ALEAAHYFTE DSSSEASPLA
     SDLDLFLPWE AQALLQEQQE GSGNEDTPER REEKGTSPPD YRHYLRMWAK EKEAQKETIK
     DLPKMNQEQF IELCKTLYNM FSEDPMEQDL YHAIATVASL LLRIGEVGKK FSALTTKKPR
     DGAHSGDPNS ATEEDEPPTP KLHQDPTQEC QPPAAGDRQA KASGDMHLGK ALQDSHVIVE
     GGSGEGQGSP SLLLSDDETK DDMSMSSYSV VSTGSLQCED LTEDTVLVGG GACSPTATSR
     AGGTVDTDWC ISFEQILASI LTESVLVNFF EKRVDIGLKI KDQKKVERQF STSSDHEPPG
     VLG
//
ID   K0664_MOUSE             Reviewed;        1315 AA.
AC   Q5SW19; A8Y5E2; Q3U014; Q3U4M5; Q3V3Q8; Q505Q6; Q6GQX1; Q6PAT1;
AC   Q8CHD9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 2.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=Protein KIAA0664;
GN   Name=Kiaa0664;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone, Dendritic cell, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 226-1315 (ISOFORM 1).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 81-1315 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5SW19-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SW19-2; Sequence=VSP_036579, VSP_036580;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q5SW19-3; Sequence=VSP_036578;
CC         Note=No experimental confirmation available. Gene prediction
CC         based on EST data;
CC   -!- SIMILARITY: Belongs to the KIAA0664/TIF31 family.
CC   -!- SIMILARITY: Contains 4 TPR repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH72573.1; Type=Erroneous initiation;
CC       Sequence=BAE20503.1; Type=Erroneous initiation;
CC       Sequence=BAE32406.1; Type=Erroneous initiation;
CC       Sequence=BAE32929.1; Type=Erroneous initiation;
CC       Sequence=BAE34042.1; Type=Erroneous initiation;
CC       Sequence=CAI24374.1; Type=Erroneous gene model prediction;
CC       Sequence=CAP19360.1; Type=Erroneous gene model prediction;
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DR   EMBL; AK036540; BAE20503.1; ALT_INIT; mRNA.
DR   EMBL; AK154146; BAE32406.1; ALT_INIT; mRNA.
DR   EMBL; AK154925; BAE32929.1; ALT_INIT; mRNA.
DR   EMBL; AK157310; BAE34042.1; ALT_INIT; mRNA.
DR   EMBL; AL607024; CAI24374.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL607024; CAP19360.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC060069; AAH60069.1; -; mRNA.
DR   EMBL; BC072573; AAH72573.1; ALT_INIT; mRNA.
DR   EMBL; BC094446; AAH94446.1; -; mRNA.
DR   EMBL; AB093256; BAC41440.3; -; Transcribed_RNA.
DR   IPI; IPI00347394; -.
DR   IPI; IPI00880722; -.
DR   IPI; IPI00923637; -.
DR   RefSeq; NP_001074627.1; NM_001081158.2.
DR   UniGene; Mm.214574; -.
DR   ProteinModelPortal; Q5SW19; -.
DR   SMR; Q5SW19; 978-1217.
DR   Ensembl; ENSMUST00000092915; ENSMUSP00000090593; ENSMUSG00000020741.
DR   GeneID; 74148; -.
DR   KEGG; mmu:74148; -.
DR   UCSC; uc007kca.1; mouse.
DR   MGI; MGI:1921398; 1300001I01Rik.
DR   HOVERGEN; HBG108020; -.
DR   InParanoid; Q5SW19; -.
DR   OrthoDB; EOG4PNXG4; -.
DR   PhylomeDB; Q5SW19; -.
DR   NextBio; 339906; -.
DR   ArrayExpress; Q5SW19; -.
DR   Bgee; Q5SW19; -.
DR   Genevestigator; Q5SW19; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR023231; GSKIP/TIF31_domain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
DR   SUPFAM; SSF103107; GSKIP/TIF31_domain; 1.
DR   PROSITE; PS50005; TPR; FALSE_NEG.
DR   PROSITE; PS50293; TPR_REGION; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Phosphoprotein; Repeat; TPR repeat.
FT   CHAIN         1   1315       Protein KIAA0664.
FT                                /FTId=PRO_0000366373.
FT   REPEAT      980   1013       TPR 1.
FT   REPEAT     1022   1055       TPR 2.
FT   REPEAT     1106   1139       TPR 3.
FT   REPEAT     1148   1181       TPR 4.
FT   MOD_RES     279    279       Phosphoserine (By similarity).
FT   MOD_RES     281    281       Phosphoserine (By similarity).
FT   MOD_RES     655    655       Phosphoserine (By similarity).
FT   VAR_SEQ     761    811       Missing (in isoform 3).
FT                                /FTId=VSP_036578.
FT   VAR_SEQ     762    856       KDCTEYAVLPMDGATLAEVMRQRGINMRYLGKVLDLVLRSP
FT                                ARDQLDHIYKIGIGELITRSAKHIFKTYLQGVELSGLSAAI
FT                                SHFLNCFLSSYPN -> REGLKGWVGAAERGCCPLVPPVPW
FT                                FLDHIENLLVTSALASPSLAHWQCPISQRRRQI (in
FT                                isoform 2).
FT                                /FTId=VSP_036579.
FT   VAR_SEQ     857   1315       Missing (in isoform 2).
FT                                /FTId=VSP_036580.
FT   CONFLICT    412    412       E -> D (in Ref. 3; AAH72573).
FT   CONFLICT    817    817       E -> D (in Ref. 1; BAE32406).
FT   CONFLICT   1284   1284       A -> APE (in Ref. 1; BAE34042 and 4;
FT                                BAC41440).
SQ   SEQUENCE   1315 AA;  148068 MW;  868CC53BDA8E3A65 CRC64;
     MLLNGDCSEN LKKEEGTSEP PRENGLDEGE PGDETTGQEV IVIQDTGFSV KILAPGIEPF
     SLQVSPQEMV QEIHQVLMDR EDTCHRTCFS LHLDGNMLDH FSELRSVEGL QEGSVLRVVE
     EPYTVREARI HVRHVRDLLK SLDPSDAFNG VDCNSLSFLS VFTDGDLGDS GKRKKGLEMD
     PIDCTPPEYI LPGSRERPLC PLQPQNRDWK PLQCLKVLTM SGWNPPPGNR KMHGDLMYLF
     VITAEDRQVS ITASTRGFYL NQSTAYHFNP KPASPRFLSH SLVELLNQIS PTFKKNFAVL
     QKKRVQRHPF ERIATPFQVY SWTAPQAEHA MDCVRAEDAY TSRLGYEEHI PGQTRDWNEE
     LQTTRELPRK NLPERLLRER AIFKVHSDFT AAATRGAMAV IDGNVMAINP SEETKMQMFI
     WNNIFFSLGF DVRDHYKDFG GDVAAYVAPT NDLNGVRTYN AVDVEGLYTL GTVVVDYRGY
     RVTAQSIIPG ILERDQEQSV IYGSIDFGKT VVSHPRYLEL LERTSRPLKI LRHRVLNDRD
     EEVELCSSVE CKGIIGNDGR HYILDLLRTF PPDLNFLPVP GEELPEECSR AGFPRTHRHK
     LCCLRQELVD AFVEHRYLLF MKLAALQLMQ QKASKVETTT SLENGGLPSS AETKSEDSIG
     PEAGCEEEGS SVSGLAKVKE LAETIASDDG TVDPRSREVI RNACKAVGSI SSTAFDIRFN
     PDIFSPGVRF PESCQDEVRD QKQLLKDAAA FLLSCQIPGL VKDCTEYAVL PMDGATLAEV
     MRQRGINMRY LGKVLDLVLR SPARDQLDHI YKIGIGELIT RSAKHIFKTY LQGVELSGLS
     AAISHFLNCF LSSYPNPVAH LPADELLSKK RNKRRKNRPP GAADNTAWAV MTPQELWKNI
     CHEAKNYFDF TLECDSVDQA VETYGLQKIT LLREISLKTG IQILLKEYSF DSRHKPAFTE
     EDVLNIFPVV KHVNPKASDA FHFFQSGQAK VQQGFLKEGC ELINEALNLF NNVYGAMHVE
     ICACLRLLAR LHYIMGDYAE ALSNQQKAVL MSERVMGIEH PNTIQEYMHL ALYCFASSQL
     STALSLLYRA RYLMLLVFGE DHPEMALLDN NIGLVLHGVM EYDLSLRFLE NALAVTTKYH
     GPKALKVALS HHLVARVYES KAEFRSALQH EKEGYTIYKT QLGEDHEKTK ESSEYLKCLT
     QQAVALQRTM NEIYRNGSSA NIPPLKFTAP SMTSVLEQLN VINGILFIPL SQKDLENLKA
     EVARRHQLQE ANRNRDKAEE QPMAPEPEPE PERAVEDMGS PQTAKEGPSS LNLQG
//
ID   SSH2_MOUSE              Reviewed;        1423 AA.
AC   Q5SW75; B9EJ94; Q3TDK8; Q3TYP8; Q3U2K3; Q5F268; Q5SW74; Q69ZC3;
AC   Q76I78;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Protein phosphatase Slingshot homolog 2;
DE            EC=3.1.3.16;
DE            EC=3.1.3.48;
DE   AltName: Full=SSH-like protein 2;
DE            Short=SSH-2L;
DE            Short=mSSH-2L;
GN   Name=Ssh2; Synonyms=Kiaa1725, Ssh2l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
RP   ACTIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND MUTAGENESIS OF CYS-392.
RC   TISSUE=Kidney;
RX   MEDLINE=22894424; PubMed=14531860;
RX   DOI=10.1046/j.1365-2443.2003.00678.x;
RA   Ohta Y., Kousaka K., Nagata-Ohashi K., Ohashi K., Muramoto A.,
RA   Shima Y., Niwa R., Uemura T., Mizuno K.;
RT   "Differential activities, subcellular distribution and tissue
RT   expression patterns of three members of Slingshot family phosphatases
RT   that dephosphorylate cofilin.";
RL   Genes Cells 8:811-824(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 371-1423 (ISOFORMS 1/2).
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1422, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
CC   -!- FUNCTION: Protein phosphatase which regulates actin filament
CC       dynamics. Dephosphorylates and activates the actin
CC       binding/depolymerizing factor cofilin, which subsequently binds to
CC       actin filaments and stimulates their disassembly. Inhibitory
CC       phosphorylation of cofilin is mediated by LIMK1, which may also be
CC       dephosphorylated and inactivated by this protein.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- SUBUNIT: Interacts with filamentous actin.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction,
CC       focal adhesion. Note=Colocalizes with filamentous actin in the
CC       cytoplasm and the cell periphery. Also localizes to focal
CC       adhesions.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q5SW75-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SW75-2; Sequence=VSP_016326;
CC       Name=3;
CC         IsoId=Q5SW75-3; Sequence=VSP_016326, VSP_016328, VSP_016329;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q5SW75-4; Sequence=VSP_016327;
CC         Note=Gene prediction based on EST data. No experimental
CC         confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, heart, liver, skeletal
CC       muscle, testis and thymus. Also expressed at lower levels in
CC       kidney, small intestine and spleen.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the nervous system at E14.5.
CC   -!- MISCELLANEOUS: Tyrosine phosphatase activity has not been
CC       demonstrated for this protein to date.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE41593.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC       Sequence=CAI24907.1; Type=Erroneous gene model prediction;
CC       Sequence=CAI35940.1; Type=Erroneous gene model prediction;
CC       Sequence=CAI51882.1; Type=Erroneous gene model prediction;
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AB099288; BAC97811.1; -; mRNA.
DR   EMBL; AK155232; BAE33137.1; -; mRNA.
DR   EMBL; AK158449; BAE34514.1; -; mRNA.
DR   EMBL; AK170142; BAE41593.1; ALT_SEQ; mRNA.
DR   EMBL; AL606724; CAI24906.2; -; Genomic_DNA.
DR   EMBL; AL607072; CAI24906.2; JOINED; Genomic_DNA.
DR   EMBL; AL663066; CAI24906.2; JOINED; Genomic_DNA.
DR   EMBL; AL606724; CAI24907.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL663066; CAI24907.1; JOINED; Genomic_DNA.
DR   EMBL; AL663066; CAI35939.2; -; Genomic_DNA.
DR   EMBL; AL606724; CAI35939.2; JOINED; Genomic_DNA.
DR   EMBL; AL607072; CAI35939.2; JOINED; Genomic_DNA.
DR   EMBL; AL663066; CAI35940.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL606724; CAI35940.1; JOINED; Genomic_DNA.
DR   EMBL; AL606724; CAI51882.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL607072; CAI52040.1; -; Genomic_DNA.
DR   EMBL; AL606724; CAI52040.1; JOINED; Genomic_DNA.
DR   EMBL; AL663066; CAI52040.1; JOINED; Genomic_DNA.
DR   EMBL; BC141392; AAI41393.1; -; mRNA.
DR   EMBL; BC141393; AAI41394.1; -; mRNA.
DR   EMBL; AK173243; BAD32521.1; -; mRNA.
DR   IPI; IPI00223805; -.
DR   IPI; IPI00553668; -.
DR   IPI; IPI00649165; -.
DR   IPI; IPI00656233; -.
DR   RefSeq; NP_808378.2; NM_177710.3.
DR   UniGene; Mm.440381; -.
DR   UniGene; Mm.440666; -.
DR   ProteinModelPortal; Q5SW75; -.
DR   SMR; Q5SW75; 253-302, 307-448.
DR   STRING; Q5SW75; -.
DR   PhosphoSite; Q5SW75; -.
DR   PRIDE; Q5SW75; -.
DR   Ensembl; ENSMUST00000037912; ENSMUSP00000042625; ENSMUSG00000037926.
DR   Ensembl; ENSMUST00000108396; ENSMUSP00000104033; ENSMUSG00000037926.
DR   Ensembl; ENSMUST00000108397; ENSMUSP00000104034; ENSMUSG00000037926.
DR   GeneID; 237860; -.
DR   KEGG; mmu:237860; -.
DR   UCSC; uc007kgl.1; mouse.
DR   UCSC; uc007kgo.1; mouse.
DR   CTD; 237860; -.
DR   MGI; MGI:2679255; Ssh2.
DR   eggNOG; roNOG12364; -.
DR   GeneTree; ENSGT00590000082789; -.
DR   HOVERGEN; HBG094002; -.
DR   OMA; DFSTDRI; -.
DR   OrthoDB; EOG4ZGPBG; -.
DR   PhylomeDB; Q5SW75; -.
DR   BRENDA; 3.1.3.16; 244.
DR   BRENDA; 3.1.3.48; 244.
DR   NextBio; 383532; -.
DR   ArrayExpress; Q5SW75; -.
DR   Bgee; Q5SW75; -.
DR   CleanEx; MM_SSH2; -.
DR   Genevestigator; Q5SW75; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   InterPro; IPR014876; DEK_C.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR020422; Dual-sp_phosphatase_subgr_cat.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   Pfam; PF08766; DEK_C; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   SMART; SM00195; DSPc; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Cell junction; Cytoplasm;
KW   Cytoskeleton; Hydrolase; Phosphoprotein; Protein phosphatase.
FT   CHAIN         1   1423       Protein phosphatase Slingshot homolog 2.
FT                                /FTId=PRO_0000094844.
FT   DOMAIN      307    447       Tyrosine-protein phosphatase.
FT   ACT_SITE    392    392       Phosphocysteine intermediate (Probable).
FT   MOD_RES      36     36       Phosphoserine (By similarity).
FT   MOD_RES     461    461       Phosphoserine (By similarity).
FT   MOD_RES     487    487       Phosphoserine (By similarity).
FT   MOD_RES    1422   1422       Phosphothreonine.
FT   VAR_SEQ       1     36       MALVTVQRSPTPSTTSSPCASEADSGEEECRSQPRS -> M
FT                                TLSTLAGERKALPASTCSLGGPDMIPYFSANAVISQNAINQ
FT                                L (in isoform 2 and isoform 3).
FT                                /FTId=VSP_016326.
FT   VAR_SEQ      21     21       S -> SSSYLEDSESAALLCCEYGESEIFSDFN (in
FT                                isoform 4).
FT                                /FTId=VSP_016327.
FT   VAR_SEQ     133    133       S -> R (in isoform 3).
FT                                /FTId=VSP_016328.
FT   VAR_SEQ     134   1423       Missing (in isoform 3).
FT                                /FTId=VSP_016329.
FT   MUTAGEN     392    392       C->S: Abrogates phosphatase activity.
FT   CONFLICT    133    133       Missing (in Ref. 2; BAE33137).
FT   CONFLICT    325    325       N -> D (in Ref. 2; BAE41593).
SQ   SEQUENCE   1423 AA;  158230 MW;  7F2608E87A72BAFD CRC64;
     MALVTVQRSP TPSTTSSPCA SEADSGEEEC RSQPRSISES FLTVKGAALF LPRGNGSSTP
     RVSHRRNKHA GDLQQHLQAM FILLRPEDNI RLAVRLESTY QNRTRYMVVV STNGRQDTEE
     SIVLGMDFSS NDSSTCTMGL VLPLWSDTLI HLDGDGGFSV STDNRVHIFK PVSVQAMWSA
     LQSLHKACEV ARMHNYYPGS LFLTWVSYYE SHINSDQSSV NEWNAMQDVQ SHRPDSPALF
     TDIPTERERT ERLIKTKLRE IMMQKDLENI TSKEIRTELE MQMVCNLREF KEFIDNEMIV
     ILGQMDSPTQ IFEHVFLGSE WNASNLEDLQ NRGVRYILNV TREIDNFFPG VFEYHNIRVY
     DEEATDLLAY WNDTYKFISK AKKHGSKCLV HCKMGVSRSA STVIAYAMKE YGWNLDRAYD
     YVKERRTVTK PNPSFMRQLE EYQGILLASK QRHNKLWRSH SDSDLSDHHE PICKPGLELN
     KKEMTTSADQ IAEVKTVENL AAMPTVFMEH VVPQDANQKG LHTKERVICL EFSSQEFRAG
     QIEDELNLND INGCSSGCCL SESKLPLDNC HASKALLQPG QAPDIANKFP DLAVEDLETD
     ALKADMNVHL LPMEELTSRL KDLPMSPDLE SPSPQASCQA AISDFSTDRI DFFSALEKFV
     ELSQETRSRS FSHSRIEELG GGRSEGCRLS VIEVAASEMA ADDQRSSSLS NTPHASEESS
     VDEDQSKAIT ELVSPDIIMQ SHSENAISVK EIVTEIESIS QGVGQVQLKG DILSNPCHTP
     KKSTIHELPL ERVPAPESKP GHWEQDESFC SVQPELARDS GKCAPEEGCL TTHSSTADLE
     EEEPVEGEHD WGPGMHSGAK WCPGSVRRAT LEFEERLRQE QENHGTASAG PTLSNRKNSK
     NDSSVADLMP KWKSDETTPE HSFFLKEAEP SKGKGKCSGS EAGSLSHCER NPTMPDCELL
     EHHSLPAPQD CLGSDSRSKK QEGDLKKQRA VVPNQECDTQ AILLPLPKKI EIIEYTPTVT
     SLGHTEPGGE ATPSKEGEKQ GLRKVKMEQS ITMFCALDEN LNRTLEPSQV SLHPQVLPLP
     HSSSECDRPA DPNPMLSSPQ DKGDCPSTPF KTAAPFVSCS TQGASFSLDY LLPHSVVHLE
     GCTEQSSATD NELSPEQASW EDSRGHFLSS GSGMAHTSSP LTNEDLSLIN KLGDSVGVLQ
     KKLDPSPEAC RIPHSSSSEN IRDLSHSRGV VKEHAKEIES RVIFQAGFSK TSQMKRSASL
     AKLGYLDLCK DYLPDRELVS SESPHLKLLQ PFLRTDSGMH ALMAHEPSES AGAQQNPQPT
     KYSVEQLKTS ECIVQSKPVE RPSVQYAKEF GYSQQCLLPK ARPELTSSEG GLPLLQTQGL
     QYTGPSPGLA VAPRQQHGRT HPLRRLKRAN DKKRTTNPFY NTM
//
ID   NACAD_MOUSE             Reviewed;        1504 AA.
AC   Q5SWP3; Q6I6F5;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=NAC-alpha domain-containing protein 1;
GN   Name=Nacad; Synonyms=Kiaa0363;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 62-1504.
RC   TISSUE=Fetal brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-980, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May prevent inappropriate targeting of non-secretory
CC       polypeptides to the endoplasmic reticulum (ER). May bind to
CC       nascent polypeptide chains as they emerge from the ribosome and
CC       block their interaction with the signal recognition particle
CC       (SRP), which normally targets nascent secretory peptides to the
CC       ER. May also reduce the inherent affinity of ribosomes for protein
CC       translocation sites in the ER membrane (M sites) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the NAC-alpha family.
CC   -!- SIMILARITY: Contains 1 NAC-A/B (NAC-alpha/beta) domain.
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DR   EMBL; AL603787; CAI24213.1; -; Genomic_DNA.
DR   EMBL; BC072589; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AB182283; BAD23961.1; -; mRNA.
DR   IPI; IPI00112419; -.
DR   RefSeq; NP_001075121.1; NM_001081652.1.
DR   UniGene; Mm.337771; -.
DR   ProteinModelPortal; Q5SWP3; -.
DR   SMR; Q5SWP3; 1363-1502.
DR   PhosphoSite; Q5SWP3; -.
DR   PRIDE; Q5SWP3; -.
DR   Ensembl; ENSMUST00000045713; ENSMUSP00000049490; ENSMUSG00000041073.
DR   GeneID; 192950; -.
DR   KEGG; mmu:192950; -.
DR   UCSC; uc007hyy.1; mouse.
DR   CTD; 192950; -.
DR   MGI; MGI:3603030; Nacad.
DR   eggNOG; roNOG09734; -.
DR   GeneTree; ENSGT00440000033468; -.
DR   HOGENOM; HBG507016; -.
DR   HOVERGEN; HBG096144; -.
DR   InParanoid; Q5SWP3; -.
DR   OMA; RDNHSDI; -.
DR   OrthoDB; EOG4DJJXZ; -.
DR   PhylomeDB; Q5SWP3; -.
DR   NextBio; 371390; -.
DR   ArrayExpress; Q5SWP3; -.
DR   Bgee; Q5SWP3; -.
DR   Genevestigator; Q5SWP3; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002715; Nas_poly-pep-assoc_cplx.
DR   Pfam; PF01849; NAC; 1.
DR   PROSITE; PS51151; NAC_AB; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1   1504       NAC-alpha domain-containing protein 1.
FT                                /FTId=PRO_0000280749.
FT   DOMAIN     1354   1419       NAC-A/B.
FT   COMPBIAS    109    247       Pro-rich.
FT   COMPBIAS    278    356       Ser-rich.
FT   COMPBIAS    399    405       Poly-Glu.
FT   COMPBIAS    408    419       Poly-Ala.
FT   COMPBIAS   1175   1178       Poly-Glu.
FT   MOD_RES     980    980       Phosphoserine.
FT   CONFLICT    520    520       C -> R (in Ref. 3; BAD23961).
FT   CONFLICT    523    523       N -> S (in Ref. 3; BAD23961).
FT   CONFLICT    548    548       P -> S (in Ref. 3; BAD23961).
FT   CONFLICT    575    577       LVV -> SVA (in Ref. 3; BAD23961).
FT   CONFLICT    706    706       P -> S (in Ref. 3; BAD23961).
FT   CONFLICT    819    819       P -> L (in Ref. 3; BAD23961).
FT   CONFLICT    930    930       P -> S (in Ref. 3; BAD23961).
FT   CONFLICT   1090   1090       A -> T (in Ref. 3; BAD23961).
FT   CONFLICT   1142   1142       L -> LDP (in Ref. 3; BAD23961).
FT   CONFLICT   1175   1175       E -> V (in Ref. 3; BAD23961).
SQ   SEQUENCE   1504 AA;  156764 MW;  F6A2A7B272633B80 CRC64;
     MSALPLALRS ARRAGARSLG LIGGRGSADV IYAPPPPSRG AVAVLATPSA LTDRGTERQG
     YRQAHVQAMP GEAAGAELPL PEAGGPGSRT DHSCDAAIAT ILKGDQLEPH GLTPGPSPLA
     LTFLSSKPGA RPQPEGASWD AGPSGAASAW VDPAEGSPSL VVLPEGLPLR PVPAEGPLPT
     TLEPRIVMGE ETCQVIASPR AAWPVLRDRE GGHPALHPPP ELCSQGDPPV PSPPPDLESY
     FTPPSTPTKS THALLPDHGP HRDAWDLEAE LLDELLDSTP ASPSGSYITA DGDSWASSPS
     CSLSLLDPAE GLDFPSDWGL SPSGSVADDL EPHPAAPPEP PSSESSLSAD SSSSWSQEGH
     FFDPNFLAND PMIPAALLPF RGSLIFQVEA VEVTPLPQEE EEDEEDVAAT AAAAAPAAAT
     PDGDLAGEGE DDSTSASFLQ SLSDLSIIEG MDEAFAFRDD TSAASSDSDS ASYAGADDDR
     LYSGEPHAQP SAQNTEQAYR SRATFPGIES TPQTSEQEIC LTNSQESVAE IAEEILTLGL
     ESEAMRTPPD QQAAPGPQVE ETPTVTPWVG NKVDLVVEQV SKALPEPCQE GISTTLGCKP
     LTAEAIPDLQ EGASPSLCPV LPEKKEEGQG LPSTLEYVAV ALEGPWKAEG GVTIPQDPLM
     TLPPLLQSTV PTSGPESVAV VALEPQQNEG CVTVLPDVPV VLPPSPQSVD PSSGPEAMAV
     ATYEFQRAKE GTPGLQDSPV AASPALQGPD PTSEPEPEVV VTSRSQQDEG IVTVPQESPT
     ASSLTLQSSH PTSDQEREVA ATLGPQQAEE GVTIPQVAPV ASPSLLQGLE STSDLESVVV
     GTPESQQDEG IATATQDTPV MAPPPLRGTD STSDPELIAP DTSQALQREA GHTPGTKPSV
     SEAHQELGVA SGPRPVPKEG DAEPPPHSAP PASNQAQQNG SEPGYKSDSF GAPEESDSTL
     STKTSEPTSC MGEKVAANMS APKQGACLEA HDGVKTHSPQ REALRSKNKR GRGTKSPGQG
     NGPKSATSQG AVETCRAHSA ARSEVSQPQL RSNEDTSGPR LPVAVSVQAR LGSCPGSPAR
     ATCTLSRVYA EETSRCAPPF QHLEPMLGLG SAEQPKVTPG ILNLSPDNSA GDLLTTSQNR
     FLDPDPAPST LDRASQSSPG PPDPCLCPPP QKASEEEEKP PASRGPMPRA GAQGAAAITT
     SGSTKPPGAR QRVSLSPHST LNPKVAPTDT KDLACIISSP CQVPPPSGTQ NPSGPREFPA
     LEQKDEDSLE EDAQRAPGSG QRWESHGESS SELDEYLAPP PDAQRTPGSG QRSESHGESS
     SELGEQDLSP QKSQCPAQGP AGSNEETIAK AKQSRSEKKA RKAMSKLGLR QIQGVTRITI
     QKSKNILFVI AKPDVFKSPA SDTYVVFGEA KIEDLSQQVH KAAAEKFKVP SEPSALVPEL
     SPGPRVRPEC EEQEEEDEEV EEAGLEPRDI ELVMAQANVT RAKAVRALKD NHSDIVNAIM
     ELTM
//
ID   ACACA_MOUSE             Reviewed;        2345 AA.
AC   Q5SWU9; A2A6H4; Q5SWU6; Q5SWU7; Q5SWU8; Q6JIZ1; Q6PHL9; Q705X8;
AC   Q705X9; Q91VC8; Q925C4; Q925C5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Acetyl-CoA carboxylase 1;
DE            Short=ACC1;
DE            EC=6.4.1.2;
DE   AltName: Full=ACC-alpha;
DE   AltName: Full=Acetyl-CoA carboxylase 265;
DE   Includes:
DE     RecName: Full=Biotin carboxylase;
DE              EC=6.3.4.14;
GN   Name=Acaca; Synonyms=Acac, Gm738;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RA   Mao J., Wakil S.J.;
RT   "Characterization of the mouse acetyl-CoA carboxylase 1 (ACC1) gene
RT   and identification of an intronless pseudogene.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-119 (ISOFORM 2).
RC   STRAIN=Swiss; TISSUE=Brain;
RX   PubMed=15607423; DOI=10.1016/j.ygeno.2004.10.001;
RA   Travers M.T., Cambot M., Kennedy H.T., Lenoir G.M., Barber M.C.,
RA   Joulin V.;
RT   "Asymmetric expression of transcripts derived from the shared promoter
RT   between the divergently oriented ACACA and TADA2L genes.";
RL   Genomics 85:71-84(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-38; 1221-1348 AND 1681-1891.
RC   STRAIN=C57BL/6;
RX   MEDLINE=22554029; PubMed=12668174; DOI=10.1016/S1388-1981(03)00041-6;
RA   Salles J., Sargueil F., Knoll-Gellida A., Witters L.A., Cassagne C.,
RA   Garbay B.;
RT   "Acetyl-CoA carboxylase and SREBP expression during peripheral nervous
RT   system myelination.";
RL   Biochim. Biophys. Acta 1631:229-238(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1501-2345.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 298-306 AND 2267-2275, INTERACTION WITH BRCA1, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=12360400; DOI=10.1038/sj.onc.1205915;
RA   Magnard C., Bachelier R., Vincent A., Jaquinod M., Kieffer S.,
RA   Lenoir G.M., Venezia N.D.;
RT   "BRCA1 interacts with acetyl-CoA carboxylase through its tandem of
RT   BRCT domains.";
RL   Oncogene 21:6729-6739(2002).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25 AND SER-29,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-79, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-79, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [13]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ENZYME REGULATION, INTERACTION
RP   WITH MID1IP1, PHOSPHORYLATION AT SER-79, AND SUBCELLULAR LOCATION.
RX   PubMed=20952656; DOI=10.1073/pnas.1012736107;
RA   Colbert C.L., Kim C.W., Moon Y.A., Henry L., Palnitkar M.,
RA   McKean W.B., Fitzgerald K., Deisenhofer J., Horton J.D., Kwon H.J.;
RT   "Crystal structure of Spot 14, a modulator of fatty acid synthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:18820-18825(2010).
CC   -!- FUNCTION: Catalyzes the rate-limiting reaction in the biogenesis
CC       of long-chain fatty acids. Carries out three functions: biotin
CC       carboxyl carrier protein, biotin carboxylase and
CC       carboxyltransferase (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate
CC       + malonyl-CoA.
CC   -!- CATALYTIC ACTIVITY: ATP + biotin-carboxyl-carrier protein + CO(2)
CC       = ADP + phosphate + carboxybiotin-carboxyl-carrier protein.
CC   -!- COFACTOR: Biotin (By similarity).
CC   -!- COFACTOR: Binds 2 manganese ions per subunit (By similarity).
CC   -!- ENZYME REGULATION: By phosphorylation (By similarity). Activity is
CC       increased by oligomerization. Citrate and MID1IP1 promote
CC       oligomerization.
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from acetyl-CoA: step 1/1.
CC   -!- SUBUNIT: Monomer, homodimer, and homotetramer. Can form
CC       filamentous polymers. Interacts in its inactive phosphorylated
CC       form with the BRCT domains of BRCA1 which prevents ACACA
CC       dephosphorylation and inhibits lipid synthesis. Interacts with
CC       MID1IP1; interaction with MID1IP1 promotes oligomerization and
CC       increases its activity.
CC   -!- INTERACTION:
CC       Q923E4:Sirt1; NbExp=1; IntAct=EBI-773043, EBI-1802585;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5SWU9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SWU9-2; Sequence=VSP_026101;
CC   -!- PTM: Phosphorylation on Ser-1262 is required for interaction with
CC       BRCA1 (By similarity).
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain.
CC   -!- SIMILARITY: Contains 1 biotin carboxylation domain.
CC   -!- SIMILARITY: Contains 1 biotinyl-binding domain.
CC   -!- SIMILARITY: Contains 1 carboxyltransferase domain.
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DR   EMBL; AY451393; AAS13685.1; -; mRNA.
DR   EMBL; AL596252; CAI24019.1; -; Genomic_DNA.
DR   EMBL; AL596447; CAI24019.1; JOINED; Genomic_DNA.
DR   EMBL; AL596447; CAI25271.1; -; Genomic_DNA.
DR   EMBL; AL596252; CAI25271.1; JOINED; Genomic_DNA.
DR   EMBL; AL596447; CAI25272.1; -; Genomic_DNA.
DR   EMBL; AL596447; CAI25273.1; -; Genomic_DNA.
DR   EMBL; AL596447; CAI25274.1; -; Genomic_DNA.
DR   EMBL; AL596447; CAM21560.1; -; Genomic_DNA.
DR   EMBL; AJ619664; CAF02251.1; -; mRNA.
DR   EMBL; AJ619665; CAF02252.1; -; Genomic_DNA.
DR   EMBL; AF374167; AAK57389.1; -; mRNA.
DR   EMBL; AF374168; AAK57390.1; -; mRNA.
DR   EMBL; AF374169; AAK57391.1; -; mRNA.
DR   EMBL; AF374170; AAK57392.1; -; mRNA.
DR   EMBL; BC056500; AAH56500.1; -; mRNA.
DR   IPI; IPI00474783; -.
DR   IPI; IPI00848443; -.
DR   RefSeq; NP_579938.2; NM_133360.2.
DR   UniGene; Mm.31374; -.
DR   HSSP; Q00955; 1W96.
DR   ProteinModelPortal; Q5SWU9; -.
DR   SMR; Q5SWU9; 94-833, 1577-2333.
DR   IntAct; Q5SWU9; 2.
DR   PhosphoSite; Q5SWU9; -.
DR   PRIDE; Q5SWU9; -.
DR   Ensembl; ENSMUST00000020843; ENSMUSP00000020843; ENSMUSG00000020532.
DR   Ensembl; ENSMUST00000103201; ENSMUSP00000099490; ENSMUSG00000020532.
DR   GeneID; 107476; -.
DR   KEGG; mmu:107476; -.
DR   UCSC; uc007kql.1; mouse.
DR   CTD; 107476; -.
DR   MGI; MGI:108451; Acaca.
DR   HOVERGEN; HBG005371; -.
DR   InParanoid; Q5SWU9; -.
DR   OMA; FMEIMQP; -.
DR   OrthoDB; EOG4X0MRD; -.
DR   PhylomeDB; Q5SWU9; -.
DR   BRENDA; 6.3.4.14; 244.
DR   BRENDA; 6.4.1.2; 244.
DR   NextBio; 358872; -.
DR   ArrayExpress; Q5SWU9; -.
DR   Bgee; Q5SWU9; -.
DR   CleanEx; MM_ACACA; -.
DR   Genevestigator; Q5SWU9; -.
DR   GermOnline; ENSMUSG00000020532; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IMP:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055088; P:lipid homeostasis; IMP:MGI.
DR   GO; GO:0044268; P:multicellular organismal protein metabolic process; IMP:MGI.
DR   GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
DR   InterPro; IPR013537; AcCoA_COase_cen.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CarbamoylP_synth_lsu_ATP-bd.
DR   InterPro; IPR005481; CarbamoylP_synth_lsu_N.
DR   InterPro; IPR000022; Carboxyl_trans.
DR   InterPro; IPR011763; COA_CT_C.
DR   InterPro; IPR011762; COA_CT_N.
DR   InterPro; IPR013817; Pre-ATP_grasp.
DR   InterPro; IPR016185; PreATP-grasp-like.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Gene3D; G3DSA:3.30.1490.20; ATP_grasp_subdomain_1; 1.
DR   Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1.
DR   Gene3D; G3DSA:3.40.50.20; Pre-ATP_grasp; 1.
DR   Pfam; PF08326; ACC_central; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   Pfam; PF00289; CPSase_L_chain; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51230; Hybrid_motif; 1.
DR   SUPFAM; SSF52440; PreATP-grasp-like; 1.
DR   SUPFAM; SSF51246; Rudmnt_hyb_motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Allosteric enzyme; Alternative promoter usage;
KW   ATP-binding; Biotin; Cytoplasm; Direct protein sequencing;
KW   Fatty acid biosynthesis; Ligase; Lipid synthesis; Manganese;
KW   Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Phosphoprotein.
FT   CHAIN         1   2345       Acetyl-CoA carboxylase 1.
FT                                /FTId=PRO_0000258040.
FT   DOMAIN      116    617       Biotin carboxylation.
FT   DOMAIN      274    465       ATP-grasp.
FT   DOMAIN      751    817       Biotinyl-binding.
FT   DOMAIN     1697   2193       Carboxyltransferase.
FT   NP_BIND     300    357       ATP (Potential).
FT   ACT_SITE    440    440       By similarity.
FT   METAL       423    423       Manganese 1 (By similarity).
FT   METAL       436    436       Manganese 1 (By similarity).
FT   METAL       436    436       Manganese 2 (By similarity).
FT   METAL       438    438       Manganese 2 (By similarity).
FT   BINDING    1822   1822       Coenzyme A (By similarity).
FT   BINDING    2126   2126       Coenzyme A (By similarity).
FT   BINDING    2128   2128       Coenzyme A (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES       5      5       Phosphoserine (By similarity).
FT   MOD_RES      23     23       Phosphoserine.
FT   MOD_RES      25     25       Phosphoserine.
FT   MOD_RES      29     29       Phosphoserine.
FT   MOD_RES      47     47       Phosphoserine (By similarity).
FT   MOD_RES      49     49       Phosphoserine (By similarity).
FT   MOD_RES      52     52       Phosphoserine (By similarity).
FT   MOD_RES      55     55       Phosphoserine (By similarity).
FT   MOD_RES      57     57       Phosphothreonine (By similarity).
FT   MOD_RES      59     59       Phosphoserine (By similarity).
FT   MOD_RES      77     77       Phosphoserine (By similarity).
FT   MOD_RES      79     79       Phosphoserine.
FT   MOD_RES     785    785       N6-biotinyllysine (By similarity).
FT   MOD_RES    1041   1041       Phosphothreonine (By similarity).
FT   MOD_RES    1200   1200       Phosphoserine (By similarity).
FT   MOD_RES    1262   1262       Phosphoserine (By similarity).
FT   MOD_RES    1333   1333       N6-acetyllysine (By similarity).
FT   MOD_RES    1579   1579       N6-acetyllysine (By similarity).
FT   MOD_RES    1843   1843       Phosphoserine (By similarity).
FT   MOD_RES    2107   2107       Phosphotyrosine (By similarity).
FT   VAR_SEQ       1      1       M -> MMWWSTLMSLLRASSFWRRISAETIRIIRALRAYFE
FT                                RIM (in isoform 2).
FT                                /FTId=VSP_026101.
FT   CONFLICT    623    623       E -> G (in Ref. 1; AAS13685).
FT   CONFLICT    906    906       S -> P (in Ref. 1; AAS13685).
FT   CONFLICT    933    933       C -> Y (in Ref. 1; AAS13685).
FT   CONFLICT   1456   1456       L -> S (in Ref. 1; AAS13685).
FT   CONFLICT   1995   1995       S -> G (in Ref. 1; AAS13685).
FT   CONFLICT   2077   2077       V -> I (in Ref. 1; AAS13685).
FT   CONFLICT   2169   2169       E -> K (in Ref. 1; AAS13685).
FT   CONFLICT   2251   2251       F -> S (in Ref. 1; AAS13685).
FT   CONFLICT   2257   2257       T -> A (in Ref. 1; AAS13685).
SQ   SEQUENCE   2345 AA;  265257 MW;  6995C534B054FE02 CRC64;
     MDEPSPLAKT LELNQHSRFI IGSVSEDNSE DEISNLVKLD LEEKEGSLSP ASVSSDTLSD
     LGISGLQDGL AFHMRSSMSG LHLVKQGRDR KKIDSQRDFT VASPAEFVTR FGGNKVIEKV
     LIANNGIAAV KCMRSIRRWS YEMFRNERAI RFVVMVTPED LKANAEYIKM ADHYVPVPGG
     PNNNNYANVE LILDIAKRIP VQAVWAGWGH ASENPKLPEL LLKNGIAFMG PPSQAMWALG
     DKIASSIVAQ TAGIPTLPWS GSGLRVDWQE NDFSKRILNV PQDLYEKGYV KDVDDGLKAA
     EEVGYPVMIK ASEGGGGKGI RKVNNADDFP NLFRQVQAEV PGSPIFVMRL AKQSRHLEVQ
     ILADQYGNAI SLFGRDCSVQ RRHQKIIEEA PAAIATPAVF EHMEQCAVKL AKMVGYVSAG
     TVEYLYSQDG SFYFLELNPR LQVEHPCTEM VADVNLPAAQ LQIAMGIPLF RIKDIRMMYG
     VSPWGDAPID FENSAHVPCP RGHVIAARIT SENPDEGFKP SSGTVQELNF RSNKNVWGYF
     SVAAAGGLHE FADSQFGHCF SWGENREEAI SNMVVALKEL SIRGDFRTTV EYLIKLLETE
     SFQLNRIDTG WLDRLIAEKV QAERPDTMLG VVCGALHVAD VSLRNSISNF LHSLERGQVL
     PAHTLLNTVD VELIYEGIKY VLKVTRQSPN SYVVIMNGSC VEVDVHRLSD GGLLLSYDGS
     SYTTYMKEEV DRYRITIGNK TCVFEKENDP SVMRSPSAGK LIQYIVEDGG HVFAGQCYAE
     IEVMKMVMTL TAVESGCIHY VKRPGAALDP GCVIAKMQLD NPSKVQQAEL HTGSLPQIQS
     TALRGEKLHR VFHYVLDNLV NVMNGYCLPD PFFSSRVKDW VERLMKTLRD PSLPLLELQD
     IMTSVSGRIP LNVEKSIKKE MAQYASNITS VLCQFPSQQI ANILDSHAAT LNRKSEREVF
     FMNTQSIVQL VQRYRSGIRG HMKAVVMDLL RQYLRVETQF QNGHYDKCVF ALREENKSDM
     NTVLNYIFSH AQVTKKNLLV TMLIDQLCGR DPTLTDELLN ILTELTQLSK TTNAKVALRA
     RQVLIASHLP SYELRHNQVE SIFLSAIDMY GHQFCIENLQ KLILSETSIF DVLPNFFYHS
     NQVVRMAALE VYVRRAYIAY ELNSVQHRQL KDNTCVVEFQ FMLPTSHPNR GNIPTLNRMS
     FASNLNHYGM THVASVSDVL LDNAFTPPCQ RMGGMVSFRT FEDFVRIFDE IMGCFCDSPP
     QSPTFPESGH TSLYDEDKVP RDEPIHILNV AIKTDGDIED DRLAAMFREF TQQNKATLVE
     HGIRRLTFLV AQKDFRKQVN CEVDQRFHRE FPKFFTFRAR DKFEEDRIYR HLEPALAFQL
     ELNRMRNFDL TAIPCANHKM HLYLGAAKVE VGTEVTDYRF FVRAIIRHSD LVTKEASFEY
     LQNEGERLLL EAMDELEVAF NNTNVRTDCN HIFLNFVPTV IMDPSKIEES VRSMVMRYGS
     RLWKLRVLQA ELKINIRLTT TGKAIPIRLF LTNESGYYLD ISLYKEVTDS RTAQIMFQAY
     GDKQGPLHGM LINTPYVTKD LLQSKRFQAQ SLGTTYIYDI PEMFRQSLIK LWESMSTQAF
     LPSPPLPSDI LTYTELVLDD QGQLVHMNRL PGGNEIGMVA WKMSLKSPEY PDGRDIIVIG
     NDITYRIGSF GPQEDLLFLR ASELARAEGI PRIYVAANSG ARIGLAEEIR HMFHVAWVDP
     EDPYKGYKYL YLTPQDYKRV SALNSVHCEH VEDEGESRYK ITDIIGKEEG LGAENLRGSG
     MIAGESSLAY DEVITISLVT CRAIGIGAYL VRLGQRTIQV ENSHLILTGA GALNKVLGRE
     VYTSNNQLGG IQIMHNNGVT HSTVCDDFEG VFTVLHWLSY MPKSVHSSVP LLNSKDPIDR
     IIEFVPTKAP YDPRWMLAGR PHPTQKGQWL SGFFDYGSFS EIMQPWAQTV VVGRARLGGI
     PVGVVAVETR TVELSIPADP ANLDSEAKII QQAGQVWFPD SAFKTYQAIK DFNREGLPLM
     VFANWRGFSG GMKDMYDQVL KFGAYIVDGL RECSQPVMVY IPPQAELRGG SWVVIDPTIN
     PRHMEMYADR ESRGSVLEPE GTVEIKFRKK DLVKTMRRVD PVYIRLAERL GTPELSPTER
     KELESKLKER EEFLIPIYHQ VAVQFADLHD TPGRMQEKGV INDILDWKTS RTFFYWRLRR
     LLLEDLVKKK IHNANPELTD GQIQAMLRRW FVEVEGTVKA YVWDNNKDLV EWLEKQLTEE
     DGVRSVIEEN IKYISRDYVL KQIRSLVQAN PEVAMDSIVH MTQHISPTQR AEVVRILSTM
     DSPST
//
ID   Q5SWZ5_MOUSE            Unreviewed;      2269 AA.
AC   Q5SWZ5;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 44.
DE   SubName: Full=Myosin phosphatase Rho interacting protein;
GN   Name=Mprip; Synonyms=AA536749; ORFNames=RP23-180B18.4-002;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Griffiths C.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- SIMILARITY: Contains 2 PH domains.
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DR   EMBL; AL596204; CAI24302.1; -; Genomic_DNA.
DR   IPI; IPI00406030; -.
DR   UniGene; Mm.2402; -.
DR   ProteinModelPortal; Q5SWZ5; -.
DR   SMR; Q5SWZ5; 44-148.
DR   STRING; Q5SWZ5; -.
DR   PRIDE; Q5SWZ5; -.
DR   Ensembl; ENSMUST00000066330; ENSMUSP00000071081; ENSMUSG00000005417.
DR   UCSC; uc007jem.1; mouse.
DR   MGI; MGI:1349438; Mprip.
DR   HOGENOM; HBG445700; -.
DR   HOVERGEN; HBG058072; -.
DR   InParanoid; Q5SWZ5; -.
DR   OMA; QTEVATS; -.
DR   PhylomeDB; Q5SWZ5; -.
DR   ArrayExpress; Q5SWZ5; -.
DR   Bgee; Q5SWZ5; -.
DR   Genevestigator; Q5SWZ5; -.
DR   InterPro; IPR013326; ApoA/E_ApoLp.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:1.20.120.20; ApoA/E_ApoLp; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Pfam; PF00169; PH; 2.
DR   SMART; SM00233; PH; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
PE   1: Evidence at protein level;
SQ   SEQUENCE   2269 AA;  257286 MW;  7FE63CE606E4402C CRC64;
     MSAAKENPCR KFQANIFNKS KCQNCFKPRE SHLLNDEDLT QAKPIYGGWL LLAPDGTDFD
     NPVHRSRKWQ RRFFILYEHG LLRYALDEMP TTLPQGTINM NQCTDVVDGE ARTGQKFSLC
     ILTPDKEHFI RAETKEIISG WLEMLMVYPR TNKQNQKKKR KVEPPTPQEP GPAKMAVTSS
     SGGSSGSSSS IPSAEKVPTT KSTLWQEEMR AKDQPDGTSL SPAQSPSQSQ PPAACTPREP
     GLESKEDEST ISGDRVDGGR KVRVESGYFS LEKAKQDLRA EEQLPPLLSP PSPSTPHSRR
     SQVIEKFEAL DIEKAEHMET NMLILTTPSS DTRQGRSERR AIPRKRPDLL NFKKGWLTKQ
     YEDGQWKKHW FVLADQSLRY YRDSVAEEAA DLDGEINLST CYDVTEYPVQ RNYGFQIHTK
     EGEFTLSAMT SGIRRNWIQT IMKHVLPASA PDVTSSLPEG KNKSTSFETC SRSTEKQEAE
     PGEPDPEQKK SRARERRREG RSKTFDWAEF RPIQQALAQE RASAVGSSDS GDPGCLEAEP
     GELERERARR REERRKRFGM LDTIDGPGME DTALRMDIDR SPGLLGTPDL KTQNVHVEIE
     QRWHQVETTP LREEKQVPIA PLHLSLEDRS ERLSTHELTS LLEKELEQSQ KEASDLLEQN
     RLLQDQLRVA LGREQSAREG YVLQTEVATS PSGAWQRLHR VNQDLQSELE AQCRRQELIT
     QQIQTLKHSY GEAKDAIRHH EAEIQTLQTR LGNAAAELAI KEQALAKLKG ELKMEQGKVR
     EQLEEWQHSK AMLSGQLRAS EQKLRSTEAR LLEKTQELRD LETQQALQRD RQKEVQRLQE
     CIAELSQQLG TSEQAQRLME KKLKRNYTLL LESCEQEKQA LLQNLKEVED KASAYEDQLQ
     GHVQQVEALQ KEKLSETCKG SEQVHKLEEE LEAREASIRQ LAQHVQSLHD ERDLIKHQFQ
     ELMERVATSD GDVAELQEKL RGKEVDYQNL EHSHHRVSVQ LQSVRTLLRE KEEELKHIKE
     THERVLEKKD QDLNEALVKM IALGSSLEET EIKLQEKEEC LRRFVSDSPK DAKEPLSTTE
     PTEEGSGILP LGSVTRVFPG FPHSQPEDED PSAGLGEEGS SGSLSREENT ILPKSADMPE
     REGHLQSTSK SDPGAPIKRP RIRFSTIQCQ RYIHPEGCAK AWTSSTSSDT SQDQSPSEDS
     VSSEATPNTL PAAADAETYI SIIHSLETKL YVTEEKLKDV TVRLESQQGQ SQEALLALHQ
     QWAGTEAQLR EQLRASLLQA SALASQLEQE RQQKATNIEH HPGELEDFQA KNSQALTCLE
     NCWKKLRSLP WADQEEGQDA CAASLANIES MLVSAIKALQ PWASPAESRT QAEQEKEHPI
     ESGMAAPVQQ PCQPILNEQE HRKLLSAQIV LEASLINQIA DSLKNTTSDV YGVLCELTQS
     GEWPLKEESA APSAGAPVEI WAKKVLVNGE FWSQVESLSK HLGTLGEETA CTSGDRQQHT
     PQSLADATWI RAELSYATQS VRELFHHRLQ SIQETLQGTQ AALQQHKCML GEILGAYQTP
     DFERVIQQIL ETLRHPTGRE DQVQTSWDQN PLGEILRPGT DGSQEPLQAL HQSPEVLAAI
     QDELAQQLRE KASILEEISA ALPVLPPTEP LGGCQRLLRM SQHLSYESCL EGLGQYSSLL
     VQDAIIQAQV CYAACRIRLE YEKELRFYKK ACQEAKGASG QKRAQAVGAL KEEYEELLHK
     QKSEYQKVIT LIEKENTELK AKVSQMDHQQ RCLQEAENKH SESMFALQGR YEEEIRCMVE
     QLSHTENTLQ AERSRVLSQL DASVKDRQAM EQHHVQQMKM LEDRFQLKVR ELQAVHQEEL
     RALQEHYIWS LRGALSLYQP SHPDSSLAPG PSEPRAVPAA KDEAESMSGL RERIQELEAQ
     MGVMREELGH KELEGDVAAL QEKYQRDFES LKATCERGFA AMEETHQKKI EDLQRQHQRE
     LEKLREEKDR LLAEETAATI SAIEAMKNAH REEMERELEK SQRSQISSIN SDIEALRRQY
     LEELQSVQRE LEVLSEQYSQ KCLENAHLAQ ALEAERQALR QCQRENQELN AHNQELNNRL
     AAEITRLRTL LTGDGGGEST GLPLTQGKDA YELEVLLRVK ESEIQYLKQE ISSLKDELQT
     ALRDKKYASD KYKDIYTELS IAKAKADCDI SRLKEQLKAA TEALGEKSPE GTTVSGYDIM
     KSKSNPDFLK KDRSCVTRQL RNIRSKSLKE GLTVQERLKL FESRDLKKD
//
ID   Q5SX11_MOUSE            Unreviewed;      1563 AA.
AC   Q5SX11;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   08-MAR-2011, entry version 33.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase;
DE            EC=3.1.2.15;
GN   Name=Usp32; ORFNames=RP23-167D6.2-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Whitehead S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Dunn M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Ubiquitin C-terminal thioester + H(2)O =
CC       ubiquitin + a thiol.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
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DR   EMBL; AL669859; CAI24206.1; -; Genomic_DNA.
DR   EMBL; AL596183; CAI24206.1; JOINED; Genomic_DNA.
DR   EMBL; AL596183; CAI24915.1; -; Genomic_DNA.
DR   EMBL; AL669859; CAI24915.1; JOINED; Genomic_DNA.
DR   IPI; IPI00131330; -.
DR   UniGene; Mm.178524; -.
DR   ProteinModelPortal; Q5SX11; -.
DR   Ensembl; ENSMUST00000000821; ENSMUSP00000000821; ENSMUSG00000000804.
DR   Ensembl; ENSMUST00000108075; ENSMUSP00000103710; ENSMUSG00000000804.
DR   MGI; MGI:2144475; Usp32.
DR   HOGENOM; HBG357271; -.
DR   HOVERGEN; HBG057958; -.
DR   InParanoid; Q5SX11; -.
DR   PhylomeDB; Q5SX11; -.
DR   ArrayExpress; Q5SX11; -.
DR   Bgee; Q5SX11; -.
DR   Genevestigator; Q5SX11; -.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:EC.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR006615; Pept_C19_DUSP.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19.
DR   InterPro; IPR001125; Recoverin.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   Pfam; PF06337; DUF1055; 1.
DR   Pfam; PF00443; UCH; 1.
DR   PRINTS; PR00450; RECOVERIN.
DR   SMART; SM00695; DUSP; 1.
DR   SMART; SM00054; EFh; 2.
DR   PROSITE; PS51283; DUSP; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 3.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; 1.
DR   PROSITE; PS50235; UCH_2_3; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Hydrolase; Protease; Repeat; Thiol protease;
KW   Ubl conjugation pathway.
SQ   SEQUENCE   1563 AA;  176949 MW;  DE7CAC3E04DC3EEA CRC64;
     MSQHCFIREV LGDGVPPKVA EVIYCSFGGT SKGLHFNNLI VGLVLLTRGK DEEKAKYIFS
     LFSSESGSYV VREEMERMLH VVDGKVPDTL RKCFSEGEKV NYEKFRNWLL LNKDAFTFSR
     WLLSGGVYVT LTDDSDTPTF YQTLAGVTHL EESDIIDLEK RYWLLKAQSR TGRFDLETFG
     PLVSPPIRPS LSEGLFNAFD ENRDNHIDFK EISCGLSACC RGPLAERQKF CFKVFDVDRD
     GVLSRVELKD MVVALLEVWK DNRTDDIPEL HMDLSDIVER ILNAHDTTKV GHLTLEDYQI
     WSVKNVLANE FLNLLFQVCH IVLGLRPATP EEEGQIIRGW LERESRYGLQ PGHNWFIISM
     QWWQQWKEYV KYDASPVVIE PSSVLNGGKF SFGTAAHPIE HGEDRISNNL GYMNTTEEKY
     SDNISSASEA SESTGSGFLY SGTPGADMCF ARQHNTSDNN NQCLLGANGN ILLHLNPQKP
     GAIDNQPLVT QEPVKATSLT LEGGRLKRTP QLIHGRDYEM VPEPVWRALY HWYGSNLALP
     RPVIKNSKTD IPELELFPRY LLFLRQQPAT RTQQSNIWVN MGNVPSPNAP LKRVLAYTGC
     FSRMQTIKEI HEYLSQRLRI KEEDMRLWLY NSENYLTLLD DEDHRLEYLK IQDEQHLVIE
     VRNKDMSWPE EMSFIANSSK IDRHKVPTEK GATGLSNLGN TCFMNSSIQC VSNTQPLTQY
     FISGRHLYEL NRTNPIGMKG HMAKCYGDLV QELWSGTQKN VAPLKLRWTI AKYAPRFNGF
     QQQDSQELLA FLLDGLHEDL NRVHEKPYVE LKDSDGRPDW EVAAEAWDNH LRRNRSIVVD
     LFHGQLRSQV KCKTCGHISV RFDPFNFLSL PLPMDSYMHL EITVIKLDGT TPIRYGLRLN
     MDEKYTGLKK QLSDLCGLKS EQILFAEVHS SNIKNFPQDN QKVRLSVSGF LCAFEIPIPA
     SPVSACSPIQ TDCSSSPSTN GLFTLTTNGD LPRPIFIPNG MPNTVVPCGT EKNVTNGIVN
     GHMPPLPDDP FTGYIIAVHR KMMRTELYFL SSQKNRPSLF GMPLIVPCTV HTRKKDLYDA
     VWIQVSRLAS PLPPQEASNH AQDCDDSMGY QYPFTLRVVQ KDGNSCAWCP WYRFCRGCKI
     DCGEDRAFIG NACIAVDWDP TALHLRYQTS QERVVEEHES VEQSRRAQAE PINLDSCLRA
     FTSEEELGEN EMYYCSKCKT HCLATKKLDL WRLPPILIIH LKRFQFVNGR WIKSQKIVKF
     PRESFDPSAF LVPRDPTLCQ HKPLTPQGDD FSELRIPAGD VKKVDIQSSA GEEDVLLSKS
     PSSLSANVTS SPKGSPSSSR KSGASCPSSK NSSPNSSPRT LGRNKGRLRL PQIGSKNKLS
     NSKENLDTSK ENGAGQICEL ADTLNRRHVL GGSQPELVTP LDHEITLANG FLYEHEACGN
     GYSNGQLGNH SEEDSTDDQR EETHSKPIYN LYAISCHSGI LGGGHYVTYA KNPNCKWYCY
     NDSSCKELHP DEIDTDSAYI LFYEQQGIDC AQFLPKTDGK KMADTSSMDE DFESDYKKYC
     VLQ
//
ID   KIBRA_MOUSE             Reviewed;        1104 AA.
AC   Q5SXA9; Q571D0; Q8K1Y3; Q8VD17; Q922W3;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Protein KIBRA;
DE   AltName: Full=Kidney and brain protein;
DE            Short=KIBRA;
DE   AltName: Full=WW domain-containing protein 1;
GN   Name=Wwc1; Synonyms=Kiaa0869;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/SvEv;
RA   Kremerskothen J.;
RT   "Protein-coding sequence of KIBRA from Mus musculus.";
RL   Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 141-1104.
RC   TISSUE=Pancreatic islet;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Seino S., Nishimura M.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 146-1104.
RC   STRAIN=FVB/N; TISSUE=Mammary gland, Mammary tumor, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-887 AND SER-891, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=18190796; DOI=10.1016/j.bbamcr.2007.12.007;
RA   Hilton H.N., Stanford P.M., Harris J., Oakes S.R., Kaplan W.,
RA   Daly R.J., Ormandy C.J.;
RT   "KIBRA interacts with discoidin domain receptor 1 to modulate
RT   collagen-induced signalling.";
RL   Biochim. Biophys. Acta 1783:383-393(2008).
CC   -!- FUNCTION: Probable regulator of the Hippo/SWH (Sav/Wts/Hpo)
CC       signaling pathway, a signaling pathway that plays a pivotal role
CC       in tumor suppression by restricting proliferation and promoting
CC       apoptosis. Along with NF2 can synergistically induce the
CC       phosphorylation of LATS1 and LATS2 and can probably function in
CC       the regulation of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway.
CC       Acts as a transcriptional coactivator of ESR1 which plays an
CC       essential role in DYNLL1-mediated ESR1 transactivation. Regulates
CC       collagen-stimulated activation of the ERK/MAPK cascade. Modulates
CC       directional migration of podocytes. Acts as a substrate for PRKCZ
CC       and may be associated with memory performance (By similarity).
CC       Regulates collagen-stimulated activation of the ERK/MAPK cascade.
CC   -!- SUBUNIT: Homodimer. Interacts with DDN. Interacts with DYNLL1 and
CC       histone H3. The interaction with DYNLL1 is mandatory for the
CC       recruitment and transactivation functions of ESR1 or DYNLL1 to the
CC       target chromatin and the interaction with histone H3 ensures
CC       proper regulatory interaction of WWC1-DYNLL1-ESR1 complexes with
CC       target chromatin. Interacts (via WW domains) with DDR1 (via PPxY
CC       motif) in a collagen-regulated manner. Interacts with PRKCZ (via
CC       the protein kinase domain). Forms a tripartite complex with DDR1
CC       and PRKCZ, but predominantly in the absence of collagen. Interacts
CC       (via the ADDV motif) with INADL (via PDZ domain 8). Interacts (via
CC       WW domains) with SYNPO (via PPxY motifs). Interacts with NF2 and
CC       SNX4 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region (By
CC       similarity). Nucleus (By similarity). Cell projection, ruffle
CC       membrane (By similarity). Note=Co-localizes with PRKCZ in the
CC       perinuclear region (By similarity).
CC   -!- TISSUE SPECIFICITY: Mammary epithelium.
CC   -!- DEVELOPMENTAL STAGE: Expressed in mammary tissue throughout
CC       development (at protein level). Strongly up-regulated during
CC       pregnancy, falls during lactation and is again up-regulated during
CC       involution of the gland at weaning.
CC   -!- DOMAIN: The C2-domain mediates homodimerization (By similarity).
CC   -!- SIMILARITY: Belongs to the WWC family. KIBRA subfamily.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 2 WW domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH06733.1; Type=Erroneous initiation;
CC       Sequence=AAH37006.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; DQ256090; ABB51169.1; -; mRNA.
DR   EMBL; AL596084; CAI24387.1; -; Genomic_DNA.
DR   EMBL; AL645912; CAI24387.1; JOINED; Genomic_DNA.
DR   EMBL; AL645912; CAI35081.1; -; Genomic_DNA.
DR   EMBL; AL596084; CAI35081.1; JOINED; Genomic_DNA.
DR   EMBL; AK220259; BAD90184.1; -; mRNA.
DR   EMBL; BC006733; AAH06733.1; ALT_INIT; mRNA.
DR   EMBL; BC017638; AAH17638.1; -; mRNA.
DR   EMBL; BC037006; AAH37006.1; ALT_INIT; mRNA.
DR   IPI; IPI00123509; -.
DR   RefSeq; NP_740749.1; NM_170779.1.
DR   UniGene; Mm.31267; -.
DR   ProteinModelPortal; Q5SXA9; -.
DR   SMR; Q5SXA9; 7-38, 52-87, 659-786.
DR   STRING; Q5SXA9; -.
DR   PhosphoSite; Q5SXA9; -.
DR   PRIDE; Q5SXA9; -.
DR   Ensembl; ENSMUST00000018993; ENSMUSP00000018993; ENSMUSG00000018849.
DR   GeneID; 211652; -.
DR   KEGG; mmu:211652; -.
DR   UCSC; uc007ili.1; mouse.
DR   CTD; 211652; -.
DR   MGI; MGI:2388637; Wwc1.
DR   eggNOG; roNOG05269; -.
DR   GeneTree; ENSGT00410000025556; -.
DR   HOGENOM; HBG357360; -.
DR   HOVERGEN; HBG058082; -.
DR   InParanoid; Q5SXA9; -.
DR   OMA; IDPRDRY; -.
DR   OrthoDB; EOG4H4632; -.
DR   NextBio; 373320; -.
DR   ArrayExpress; Q5SXA9; -.
DR   Bgee; Q5SXA9; -.
DR   CleanEx; MM_WWC1; -.
DR   Genevestigator; Q5SXA9; -.
DR   GermOnline; ENSMUSG00000018849; Mus musculus.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR   GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR   GO; GO:0043410; P:positive regulation of MAPKKK cascade; ISS:UniProtKB.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Pfam; PF00397; WW; 2.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF51045; WW_Rsp5_WWP; 2.
DR   PROSITE; PS50004; C2; FALSE_NEG.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   1: Evidence at protein level;
KW   Activator; Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW   Membrane; Nucleus; Phosphoprotein; Repeat; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   1104       Protein KIBRA.
FT                                /FTId=PRO_0000242154.
FT   DOMAIN        6     39       WW 1.
FT   DOMAIN       53     86       WW 2.
FT   DOMAIN      656    784       C2.
FT   REGION      836   1104       Interaction with histone H3 (By
FT                                similarity).
FT   REGION      945    988       Interaction with PRKCZ (By similarity).
FT   COILED      107    193       Potential.
FT   COILED      994   1024       Potential.
FT   MOTIF      1102   1104       ADDV motif.
FT   COMPBIAS    255    294       Ser-rich.
FT   COMPBIAS    421    461       Ser-rich.
FT   COMPBIAS    816    873       Glu-rich.
FT   MOD_RES     887    887       Phosphoserine.
FT   MOD_RES     891    891       Phosphoserine.
FT   MOD_RES     915    915       Phosphothreonine (By similarity).
FT   MOD_RES     919    919       Phosphoserine (By similarity).
FT   MOD_RES     921    921       Phosphothreonine (By similarity).
FT   MOD_RES     923    923       Phosphoserine (By similarity).
FT   MOD_RES     967    967       Phosphoserine; by PKC/PRKCZ (By
FT                                similarity).
FT   MOD_RES     970    970       Phosphoserine; by PKC/PRKCZ (By
FT                                similarity).
FT   CONFLICT    141    145       SQVSL -> AGLPV (in Ref. 3; BAD90184).
FT   CONFLICT    348    348       E -> K (in Ref. 4; AAH06733).
SQ   SEQUENCE   1104 AA;  124110 MW;  D827EFD9AAB19FBA CRC64;
     MPRPELPLPE GWEEARDFDG KVYYIDHRNR TTSWIDPRDR YTKPLTFADC ISDELPLGWE
     EAYDPQVGDY FIDHNTKTTQ IEDPRVQWRR EQEHMLKDYL VVAQEALSAQ KEIYQVKQQR
     LELAQQEYQQ LHAVWEHKLG SQVSLVSGSS SSSKYDPEIL KAEIATAKSR VNKLKREMVH
     LQHELQFKER GFQTLKKIDE RMSDAQGGYK LDEAQAVLRE TKAIKKAITC GEKEKQDLIK
     SLAMLKDGFR TDRGSHSDLW SSSSSLESSS FPMPKQFLDV SSQTDISGSF STSSNNQLAE
     KVRLRLRYEE AKRRIANLKI QLAKLDSEAW PGVLDSERDR LILINEKEEL LKEMRFISPR
     KWTQGEVEQL EMARRRLEKD LQAARDTQSK ALTERLKLNS KRNQLVRELE EATRQVATLH
     SQLKSLSSSM QSLSSGSSPG SLTSSRGSLA ASSLDSSTSA SFTDLYYDPF EQLDSELQSK
     VELLFLEGAT GFRPSGCITT IHEDEVAKTQ KAEGGSRLQA LRSLSGTPRS MTSLSPRSSL
     SSPSPPCSPL ITDPLLTGDA FLAPLEFEDT ELSTTLCELN LGGSGTQERY RLEEPGPEGK
     PLGQAASVAP GCGLKVACVS AAVSDESVAG DSGVYEASAQ RPGTSEAAAF DSDESEAVGA
     TRVQIALKYD EKNKQFAILI IQLSHLSALS LQQDQKVNIR VAILPCSESS TCLFRTRPLD
     SANTLVFNEA FWVSISYPAL HQKTLRVDVC TTDRSHTEEC LGGAQISLAE VCRSGERSTR
     WYNLLSYKYL KKQCREPQPT EAPGPDHVDA VSALLEQTAV ELEKRQEGRS SSQTLEGSWT
     YEEEASENEA VAEEEEEGEE DVFTEKVSPE AEECPALKVD RETNTDSVAP SPTVVRPKDR
     RVGAPSTGPF LRGNTIIRSK TFSPGPQSQY VCRLNRSDSD SSTLSKKPPF VRNSLERRSV
     RMKRPSSVKS LRTERLIRTS LDLELDLQAT RTWHSQLTQE ISVLKELKEH LEQAKNHGEK
     ELPQWLREDE RFRLLLRMLE KKVDRGEHKS ELQADKMMRA AAKDVHRLRG QSCKEPPEVQ
     SFREKMAFFT RPRMNIPALS ADDV
//
ID   Q5SXG0_MOUSE            Unreviewed;      1300 AA.
AC   Q5SXG0;
DT   21-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   SubName: Full=Misshapen-like kinase 1 (Zebrafish);
DE   SubName: Full=Misshapen-like kinase 1 (Zebrafish), isoform CRA_c;
GN   Name=Mink1; ORFNames=DN-183N8.7-005, RP23-122P1.6-005, mCG_134369;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Lawlor S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Smith M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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CC   -----------------------------------------------------------------------
DR   EMBL; AL592547; CAI24008.1; -; Genomic_DNA.
DR   EMBL; CR933736; CAM28125.1; -; Genomic_DNA.
DR   EMBL; CH466596; EDL12581.1; -; Genomic_DNA.
DR   IPI; IPI00468997; -.
DR   RefSeq; NP_057922.2; NM_016713.2.
DR   UniGene; Mm.42967; -.
DR   ProteinModelPortal; Q5SXG0; -.
DR   SMR; Q5SXG0; 20-291.
DR   STRING; Q5SXG0; -.
DR   Ensembl; ENSMUST00000102558; ENSMUSP00000099618; ENSMUSG00000020827.
DR   GeneID; 50932; -.
DR   KEGG; mmu:50932; -.
DR   UCSC; uc007jvl.1; mouse.
DR   CTD; 50932; -.
DR   MGI; MGI:1355329; Mink1.
DR   HOVERGEN; HBG036506; -.
DR   PhylomeDB; Q5SXG0; -.
DR   NextBio; 307959; -.
DR   ArrayExpress; Q5SXG0; -.
DR   Bgee; Q5SXG0; -.
DR   Genevestigator; Q5SXG0; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0005083; F:small GTPase regulator activity; IEA:InterPro.
DR   GO; GO:0045060; P:negative thymic T cell selection; IMP:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR001180; Citron.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Transferase.
SQ   SEQUENCE   1300 AA;  146390 MW;  9DB699C6D1F39C54 CRC64;
     MGDPAPARSL DDIDLSALRD PAGIFELVEV VGNGTYGQVY KGRHVKTGQL AAIKVMDVTE
     DEEEEIKQEI NMLKKYSHHR NIATYYGAFI KKSPPGNDDQ LWLVMEFCGA GSVTDLVKNT
     KGNALKEDCI AYICREILRG LAHLHAHKVI HRDIKGQNVL LTENAEVKLV DFGVSAQLDR
     TVGRRNTFIG TPYWMAPEVI ACDENPDATY DYRSDIWSLG ITAIEMAEGA PPLCDMHPMR
     ALFLIPRNPP PRLKSKKWSK KFTDFIDTCL IKTYLSRPPT EQLLKFPFIR DQPTERQVRI
     QLKDHIDRSR KKRGEKEETE YEYSGSEEED DSHGEEGEPS SIMNVPGEST LRREFLRLQQ
     ENKSNSEALK QQQQLQQQQQ RDPEAHIKHL LHQRQRRIEE QKEERRRVEE QQRREREQRK
     LQEKEQQRRL EDMQALRREE ERRQAEREQE YKRKQLEEQR QSERLQRQLQ QEHAYLKSLQ
     QQQQQQQLQK QQQQQQQILP GDRKPLYHYG RGINPADKPA WAREVEERAR MNKQQNSPLA
     KAKPSSAGPE PPISQASPSP PGPLSQTPPM QRPVEPQEGP HKSLVAHRVP LKPYAAPVPR
     SQSLQDQPTR NLAAFPASHD PDPAAVPTPT ATPSARGAVI RQNSDPTSEG PGPSPNPPSW
     VRPDNEAPPK VPQRTSSIAT ALNTSGAGGS RPAQAVRASN PDLRRSDPGW ERSDSVLPAS
     HGHLPQAGSL ERNRNRVGAS TKLDSSPVLS PGNKAKPEDH RSRPGRPADF VLLKERTLDE
     APKPPKKAMD YSSSSEEVES SEEEEEEGDG EPSEGSRDTP GGRSDGDTDS VSTMVVHDVE
     EISGTQPSYG GGTMVVQRTP EEERSLLLAD SNGYTNLPDV VQPSHSPTEN SKGQSPPTKD
     GGSDYQSRGL VKAPGKSSFT MFVDLGIYQP GGSGDTIPIT ALVGGEGGRL DQLQFDVRKG
     SVVNVNPTNT RAHSETPEIR KYKKRFNSEI LCAALWGVNL LVGTENGLML LDRSGQGKVY
     GLIGRRRFQQ MDVLEGLNLL ITISGKRNKL RVYYLSWLRN KILHNDPEVE KKQGWTTVGD
     MEGCGHYRVV KYERIKFLVI ALKNSVEVYA WAPKPYHKFM AFKSFADLPH RPLLVDLTVE
     EGQRLKVIYG SSAGFHAVDV DSGNSYDIYI PVHIQSQITP HAIIFLPNTD GMEMLLCYED
     EGVYVNTYGR IIKDVVLQWG EMPTSVAYIC SNQIMGWGEK AIEIRSVETG HLDGVFMHKR
     AQRLKFLCER NDKVFFASVR SGGSSQVYFM TLNRNCIMNW
//
ID   CYTSB_MOUSE             Reviewed;        1067 AA.
AC   Q5SXY1; Q5DTQ5; Q5SXY0; Q8BKR3; Q8BL39;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Cytospin-B;
DE   AltName: Full=Sperm antigen with calponin homology and coiled-coil domains 1;
GN   Name=Specc1; Synonyms=Cytsb, Kiaa4061;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-656 (ISOFORMS 1 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-357, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111 AND SER-119, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5SXY1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SXY1-2; Sequence=VSP_021167, VSP_021168;
CC       Name=4;
CC         IsoId=Q5SXY1-3; Sequence=VSP_021166;
CC   -!- SIMILARITY: Belongs to the cytospin-A family.
CC   -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90492.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK220465; BAD90492.1; ALT_INIT; mRNA.
DR   EMBL; AL592080; CAI23916.1; -; Genomic_DNA.
DR   EMBL; AL592080; CAI23917.1; -; Genomic_DNA.
DR   EMBL; AL596110; CAI23917.1; JOINED; Genomic_DNA.
DR   EMBL; AL596110; CAI35329.1; -; Genomic_DNA.
DR   EMBL; AL592080; CAI35329.1; JOINED; Genomic_DNA.
DR   EMBL; AK046469; BAC32744.2; -; mRNA.
DR   EMBL; AK050982; BAC34484.2; -; mRNA.
DR   IPI; IPI00122577; -.
DR   IPI; IPI00381563; -.
DR   IPI; IPI00798550; -.
DR   UniGene; Mm.458025; -.
DR   HSSP; Q01082; 1BKR.
DR   ProteinModelPortal; Q5SXY1; -.
DR   SMR; Q5SXY1; 961-1066.
DR   PhosphoSite; Q5SXY1; -.
DR   PRIDE; Q5SXY1; -.
DR   Ensembl; ENSMUST00000049836; ENSMUSP00000063102; ENSMUSG00000042331.
DR   Ensembl; ENSMUST00000092415; ENSMUSP00000090071; ENSMUSG00000042331.
DR   Ensembl; ENSMUST00000108709; ENSMUSP00000104349; ENSMUSG00000042331.
DR   UCSC; uc007jin.1; mouse.
DR   MGI; MGI:2442356; Specc1.
DR   GeneTree; ENSGT00530000062761; -.
DR   InParanoid; Q5SXY1; -.
DR   OMA; AKDSEIN; -.
DR   OrthoDB; EOG4THVSB; -.
DR   PhylomeDB; Q5SXY1; -.
DR   ArrayExpress; Q5SXY1; -.
DR   Bgee; Q5SXY1; -.
DR   Genevestigator; Q5SXY1; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR001715; CH-domain.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 1.
DR   Pfam; PF00307; CH; 1.
DR   SMART; SM00033; CH; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS50021; CH; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Nucleus; Phosphoprotein.
FT   CHAIN         1   1067       Cytospin-B.
FT                                /FTId=PRO_0000254034.
FT   DOMAIN      961   1063       CH.
FT   COILED      574    773       Potential.
FT   COMPBIAS    259    371       Ser-rich.
FT   MOD_RES     111    111       Phosphoserine.
FT   MOD_RES     119    119       Phosphoserine.
FT   MOD_RES     133    133       Phosphoserine (By similarity).
FT   MOD_RES     135    135       Phosphothreonine (By similarity).
FT   MOD_RES     137    137       Phosphoserine (By similarity).
FT   MOD_RES     141    141       Phosphothreonine (By similarity).
FT   MOD_RES     357    357       Phosphothreonine.
FT   MOD_RES     359    359       Phosphoserine (By similarity).
FT   MOD_RES     360    360       Phosphoserine (By similarity).
FT   MOD_RES     365    365       Phosphoserine (By similarity).
FT   MOD_RES     810    810       Phosphoserine (By similarity).
FT   MOD_RES     847    847       Phosphoserine (By similarity).
FT   MOD_RES     863    863       Phosphoserine (By similarity).
FT   MOD_RES     912    912       Phosphoserine (By similarity).
FT   VAR_SEQ       1     92       MRSAAKPWSPVAKAGSHGPDRTRPLPGTPSGMKSSKSSTSL
FT                                AFESRLSKLKRASSEDTLNKPGSASSGVARLKKTSTSGAIS
FT                                ELTESRLRSN -> MGNHSAKLEEPE (in isoform
FT                                4).
FT                                /FTId=VSP_021166.
FT   VAR_SEQ     785    790       PVNEEP -> SMVSVS (in isoform 2).
FT                                /FTId=VSP_021167.
FT   VAR_SEQ     791   1067       Missing (in isoform 2).
FT                                /FTId=VSP_021168.
FT   CONFLICT    776    784       Missing (in Ref. 1; BAD90492).
SQ   SEQUENCE   1067 AA;  118101 MW;  B199047FB7DF1957 CRC64;
     MRSAAKPWSP VAKAGSHGPD RTRPLPGTPS GMKSSKSSTS LAFESRLSKL KRASSEDTLN
     KPGSASSGVA RLKKTSTSGA ISELTESRLR SNTGTIPTTK RTGIPAPREL SVTISRERSV
     PRGPSSSKKL GSSPTSSCNP TPTKHLRTTP AKPKQEHEGA EKAVLESQVR ELLAEAKTKD
     SEINRLRSEL KKCKERWALS TEDANASDPS AEGTASPESD AQPLIRTLEE KNKTFQKELA
     DLEEENRALK EKLTYLEQSP NSEGAASHTG DSSCPTSITH ESSFGSPVGN ELSSETDEYR
     RTTHGSALRT SGSSSSDVTK ASLSPDASDF EHITADTPSR PLSATSNPFK SSKGSPTGSS
     PNNASELSLA SLTEKIQKME ENQHSTAEEL QATLQELSDQ QQMVQELTAE NEKLVDEKTI
     LETSFHQHRE RAEQLSQENE KLINLLQERV KNEEPSAQGG KVLELEQKCT DILEKSRFER
     EKLLNIQQQL TCSLRKVEEE NQGAIDMIKH LKEENEKLNG FLEHERCNNS VMAKTLEECR
     VTLEGLKMEN GSLKALLEAD KQKAIEASST VGQTAENFEV QEMLKVARAE KDQLQLSCTE
     LRQELLKANG EIKHVSSLLA KMEKDYSYLK EVCDHQAEQL SRTSLKLQEK ASESDAEIKD
     MKETIFELED QVEQHRAVKL HNNQLISELE GSVIKLEEQK SDLERQLKTL TKQIKEETEE
     WRRFQADLQT AVVVANDIKC EAQQELRTVK RRLLEEEEKN ARLQKELGDI QGHSRWVTGR
     ATLLPVNEEP EPSEADAAGR WRGVYVNRTS PAPSDSATTV KSLIKSFDLG HSGGTGQSIS
     VHKTPRSPLS GIPVRTAPAA AVSPMQRHST YSSMKPASKG TSQRLDLPDL PLSDLLKGRA
     EDRKSDPYLR KSPSLESLSR PPSLGFGNTR LLSASTGGLK PSKLSVERRD PLAALAREYG
     GSKRNALLKW CQKKTEGYAN IDITNFSSSW SDGLALCALL HTYLPAHIPY QELNSQEKKR
     NLLLAFEAAQ SVGINPSLEL SEMLYTDRPD WQSVMQYVAQ IYKYFET
//
ID   MYO1D_MOUSE             Reviewed;        1006 AA.
AC   Q5SYD0; Q5SSK7; Q8BWY5;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Myosin-Id;
GN   Name=Myo1d;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-536, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Myosins are actin-based motor molecules with ATPase
CC       activity. Unconventional myosins serve in intracellular movements.
CC       Their highly divergent tails are presumed to bind to membranous
CC       compartments, which would be moved relative to actin filaments (By
CC       similarity).
CC   -!- SUBUNIT: Binds calmodulin through its IQ motifs (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5SYD0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SYD0-2; Sequence=VSP_051938, VSP_051939;
CC   -!- SIMILARITY: Contains 2 IQ domains.
CC   -!- SIMILARITY: Contains 1 myosin head-like domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC33719.1; Type=Frameshift; Positions=784;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK049374; BAC33719.1; ALT_FRAME; mRNA.
DR   EMBL; AL591146; CAI24746.1; -; Genomic_DNA.
DR   EMBL; AL591410; CAI24746.1; JOINED; Genomic_DNA.
DR   EMBL; AL663054; CAI24746.1; JOINED; Genomic_DNA.
DR   EMBL; AL591410; CAI26106.1; -; Genomic_DNA.
DR   EMBL; AL591146; CAI26106.1; JOINED; Genomic_DNA.
DR   EMBL; AL663054; CAI26106.1; JOINED; Genomic_DNA.
DR   EMBL; AL591410; CAI26107.1; -; Genomic_DNA.
DR   EMBL; AL663054; CAI26107.1; JOINED; Genomic_DNA.
DR   EMBL; AL663054; CAI25852.1; -; Genomic_DNA.
DR   EMBL; AL591146; CAI25852.1; JOINED; Genomic_DNA.
DR   EMBL; AL591410; CAI25852.1; JOINED; Genomic_DNA.
DR   EMBL; AL663054; CAI25853.1; -; Genomic_DNA.
DR   EMBL; AL591410; CAI25853.1; JOINED; Genomic_DNA.
DR   IPI; IPI00226551; -.
DR   IPI; IPI00408207; -.
DR   RefSeq; NP_796364.2; NM_177390.3.
DR   UniGene; Mm.151948; -.
DR   ProteinModelPortal; Q5SYD0; -.
DR   SMR; Q5SYD0; 9-722.
DR   STRING; Q5SYD0; -.
DR   PhosphoSite; Q5SYD0; -.
DR   PRIDE; Q5SYD0; -.
DR   Ensembl; ENSMUST00000041065; ENSMUSP00000037819; ENSMUSG00000035441.
DR   Ensembl; ENSMUST00000070997; ENSMUSP00000066948; ENSMUSG00000035441.
DR   GeneID; 338367; -.
DR   KEGG; mmu:338367; -.
DR   UCSC; uc007kmh.1; mouse.
DR   CTD; 338367; -.
DR   MGI; MGI:107728; Myo1d.
DR   eggNOG; roNOG06653; -.
DR   HOGENOM; HBG717149; -.
DR   HOVERGEN; HBG062373; -.
DR   InParanoid; Q5SYD0; -.
DR   OMA; HGVKTMR; -.
DR   OrthoDB; EOG4Z36CZ; -.
DR   PhylomeDB; Q5SYD0; -.
DR   NextBio; 400167; -.
DR   ArrayExpress; Q5SYD0; -.
DR   Bgee; Q5SYD0; -.
DR   CleanEx; MM_MYO1D; -.
DR   Genevestigator; Q5SYD0; -.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR010926; Myosin_tail_2.
DR   Pfam; PF00612; IQ; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF06017; Myosin_TH1; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 1.
DR   SMART; SM00242; MYSc; 1.
DR   PROSITE; PS50096; IQ; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Alternative splicing; ATP-binding;
KW   Calmodulin-binding; Motor protein; Myosin; Nucleotide-binding;
KW   Phosphoprotein; Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1006       Myosin-Id.
FT                                /FTId=PRO_0000123448.
FT   DOMAIN        2    682       Myosin head-like.
FT   DOMAIN      699    719       IQ 1.
FT   DOMAIN      721    741       IQ 2.
FT   NP_BIND     102    109       ATP (Potential).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     200    200       Phosphoserine (By similarity).
FT   MOD_RES     203    203       Phosphoserine (By similarity).
FT   MOD_RES     212    212       Phosphoserine (By similarity).
FT   MOD_RES     536    536       Phosphotyrosine.
FT   VAR_SEQ     904    944       LTGLSVSNGKDQLVVFHTKDNKDLIVCLFSKQPTHESRIGE
FT                                -> ISHAHSSALTLHLLLGRTNFRTMEWLPPLVRQTGYKGG
FT                                LQM (in isoform 2).
FT                                /FTId=VSP_051938.
FT   VAR_SEQ     945   1006       Missing (in isoform 2).
FT                                /FTId=VSP_051939.
SQ   SEQUENCE   1006 AA;  116081 MW;  547A7FDCA656E572 CRC64;
     MAEQESLEFG KADFVLMDTV SMPEFMANLR LRFEKGRIYT FIGEVVVSVN PYKVLNIYGR
     DTVEQYKGRE LYERPPHLFA IADAAYKAMK RRSKDTCIMI SGESGAGKTE ASKYIMQYIA
     AITNPSQRAE IERVKNMLLK SNCVLEAFGN AKTNRNDNSS RFGKYMDINF DFKGDPIGGH
     INNYLLEKSR VIVQQPGERS FHSFYQLLQG GSEQMLHSLH LQKSLSSYNY IRVGAQLKSS
     INDAAEFKVV ADAMKVIGFK PEEIQTVYKI LAVILHLGNL KFIVDGDTPL IENGKVVSVI
     AELLSTKADM VEKALLYRTV ATGRDIIDKQ HTEQEASYGR DAFAKAIYER LFCWIVTRIN
     DIIEVKNYDT TIHGKNTVIG VLDIYGFEIF DNNSFEQFCI NYCNEKLQQL FIQLVLKQEQ
     EEYQREGIPW KHIDYFNNQI IVDLVEQQHK GIIAILDDAC MNVGKVTDGM FLEALNSKLG
     KHGHFSSRKT CASDKILEFD RDFRIRHYAG DVVYSAIGFI DKNKDTLFQD FKRLMYNSSN
     PVLKNMWPEG KLSITEVTKR PLTAATLFKN SMIALVDNLA SKEPYYVRCI KPNDKKSPQI
     FDDERCRHQV EYLGLLENVR VRRAGFAFRQ TYEKFLHRYK MISEFTWPNH DLPSDKEAVK
     KLIERCGFQD DVAYGKSKIF IRTPRTLFTL EELRAQMLVR VVLFLQKVWR GTLARMRYKR
     TKAALTIIRY YRRYKVKSYI HEVARRFHGV KNMRDYGKHV KWPTPPKVLR RFEEALQSIF
     NRWRASQLIK TIPASDLPQV RAKVAAMEML KGQRADLGLQ RAWEGNYLAS KPDTPQTSGT
     FVPVANELKR KDKYMNVLFS CHVRKVNRFS KVEDRAIFVT DRHLYKMDPT KQYKVMKTIP
     LYNLTGLSVS NGKDQLVVFH TKDNKDLIVC LFSKQPTHES RIGELVGVLV NHFKSEKRHL
     QVNVTNPVQC SLHGKKCTVS VETRLNQPQP DFTKNRSGFI LSVPGN
//
ID   K0319_MOUSE             Reviewed;        1081 AA.
AC   Q5SZV5; Q14BF3; Q80U39;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=Dyslexia-associated protein KIAA0319 homolog;
DE   Flags: Precursor;
GN   Name=Kiaa0319;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16600991; DOI=10.1093/hmg/ddl089;
RA   Paracchini S., Thomas A., Castro S., Lai C., Paramasivam M., Wang Y.,
RA   Keating B.J., Taylor J.M., Hacking D.F., Scerri T., Francks C.,
RA   Richardson A.J., Wade-Martins R., Stein J.F., Knight J.C., Copp A.J.,
RA   Loturco J., Monaco A.P.;
RT   "The chromosome 6p22 haplotype associated with dyslexia reduces the
RT   expression of KIAA0319, a novel gene involved in neuronal migration.";
RL   Hum. Mol. Genet. 15:1659-1666(2006).
CC   -!- FUNCTION: Involved in neuronal migration during development of the
CC       cerebral neocortex. May function in a cell autonomous and a non-
CC       cell autonomous manner and play a role in appropriate adhesion
CC       between migrating neurons and radial glial fibers. May also
CC       regulate growth and differentiation of dendrites (By similarity).
CC   -!- SUBUNIT: Homodimer. Interacts with AP2M1; required for clathrin-
CC       mediated endocytosis (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein (By similarity). Early endosome membrane; Single-pass type
CC       I membrane protein (By similarity).
CC   -!- DEVELOPMENTAL STAGE: Expressed in the frontal neocortex,
CC       glanglionic eminence, mesencephalon and cerebellum at E13.5. More
CC       prominently expressed in the developing cerebral neocortex and
CC       mesencephalon at E15.5 and in the cortical plate and in the
CC       remnant of the ventricular zone at E18.5.
CC   -!- PTM: N-glycosylated (By similarity).
CC   -!- PTM: O-glycosylated (By similarity).
CC   -!- PTM: Shedding of the extracellular domain and intramembrane
CC       cleavage produce several proteolytic products. The intramembrane
CC       cleavage releases a soluble cytoplasmic polypeptide that
CC       translocates to the nucleolus (By similarity).
CC   -!- SIMILARITY: Contains 1 MANSC domain.
CC   -!- SIMILARITY: Contains 5 PKD domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65528.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK122246; BAC65528.1; ALT_INIT; mRNA.
DR   EMBL; AL589699; CAI26085.1; -; Genomic_DNA.
DR   EMBL; BC115723; AAI15724.1; -; mRNA.
DR   EMBL; BC115940; AAI15941.1; -; mRNA.
DR   IPI; IPI00124582; -.
DR   RefSeq; NP_001074520.1; NM_001081051.1.
DR   UniGene; Mm.261514; -.
DR   ProteinModelPortal; Q5SZV5; -.
DR   SMR; Q5SZV5; 336-436, 439-821.
DR   STRING; Q5SZV5; -.
DR   PhosphoSite; Q5SZV5; -.
DR   PRIDE; Q5SZV5; -.
DR   Ensembl; ENSMUST00000006893; ENSMUSP00000006893; ENSMUSG00000006711.
DR   GeneID; 210108; -.
DR   KEGG; mmu:210108; -.
DR   UCSC; uc007pwn.1; mouse.
DR   MGI; MGI:3036268; D130043K22Rik.
DR   GeneTree; ENSGT00390000006285; -.
DR   HOGENOM; HBG714850; -.
DR   HOVERGEN; HBG057130; -.
DR   InParanoid; Q5SZV5; -.
DR   OMA; SQSTDDT; -.
DR   OrthoDB; EOG49GKFT; -.
DR   NextBio; 372870; -.
DR   ArrayExpress; Q5SZV5; -.
DR   Bgee; Q5SZV5; -.
DR   CleanEx; MM_D130043K22RIK; -.
DR   Genevestigator; Q5SZV5; -.
DR   GermOnline; ENSMUSG00000006711; Mus musculus.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:2000171; P:negative regulation of dendrite development; ISS:UniProtKB.
DR   GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013980; MANSC.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR002859; PKD/REJ-like.
DR   InterPro; IPR000601; PKD_dom.
DR   Gene3D; G3DSA:2.60.40.670; PKD; 2.
DR   Pfam; PF02010; REJ; 1.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00089; PKD; 5.
DR   SUPFAM; SSF49299; PKD; 4.
DR   PROSITE; PS50986; MANSC; 1.
DR   PROSITE; PS50093; PKD; 2.
PE   2: Evidence at transcript level;
KW   Cell membrane; Developmental protein; Endosome; Glycoprotein;
KW   Membrane; Neurogenesis; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     22       Potential.
FT   CHAIN        23   1081       Dyslexia-associated protein KIAA0319
FT                                homolog.
FT                                /FTId=PRO_0000042947.
FT   TOPO_DOM     23    964       Extracellular (Potential).
FT   TRANSMEM    965    985       Helical; (Potential).
FT   TOPO_DOM    986   1081       Cytoplasmic (Potential).
FT   DOMAIN       23     99       MANSC.
FT   DOMAIN      345    436       PKD 1.
FT   DOMAIN      444    533       PKD 2.
FT   DOMAIN      539    629       PKD 3.
FT   DOMAIN      630    723       PKD 4.
FT   DOMAIN      729    820       PKD 5.
FT   MOTIF      1004   1007       Endocytosis signal.
FT   CARBOHYD    196    196       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    228    228       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    272    272       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    302    302       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    430    430       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    507    507       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    522    522       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    545    545       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    560    560       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    742    742       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   1081 AA;  117988 MW;  C142C9746D9AF4DA CRC64;
     MVSPPGVLSS LLLLAAMAGG SSQQCSEGRT YSDAIISPNP ETIRIMRVSQ TFSVGDCTAA
     CCDLLTCDLA WWFEGSCYLV KCMRSENCEP RTTGPIRSYL TFVRRPVQRP GQLLDYGDMM
     LSRGSPSGAW GDSLEDLRKD LPFLGKDGGP EETTEYSDEY KDLERGLLQP SNQQDPRGSA
     EYPDWSLLPS NEGGFNATAT GDNSAASMEK LQDPTPHPLD QEQLQALNES TWSPTPGHSS
     ISSVWPSSAS PLPTEEGLEG EETLQLQEQP SNSSGKEVPM PSHNPSPASL ESSPATTEKN
     SNFTVTPRSR KHSTPTFPTS TVLTGLTPPP WPLSPTASRT VKALAVSAGD NLVLTLPDRE
     AELKASVEPA PPADTTYSYE WSLMSHPVDF QGKIKQENKP TLHLSQLSVG LYAFRVAVSS
     ENAFGEGYVN VTVMPAARVN QPPVAVVSPQ TQELSVPLTS ALIDGSQSTD DTEIVSYHWE
     EVDGPFLGEE FPADTPILRL SNLVPGNYTF RLTITDSDGA TNSTTASLVI RDAVDYPPVA
     NAGPNQTITL PQNTIILNGN QSSDDHQIVL YEWFAGPGGE SKEMVMQGAQ TPYLHLSELQ
     EGEYTFQLMV TDSSGQQSTA LVAVTVQAEN NQAPVAVAGP DKELVFPVQS ATLDGSRSSD
     DHGIVCYHWE HIRGPSAVEM ENVDKAIATV TGLQVGIYHF RLTVRDQQGL SSTSTLTVAV
     KKENNSPPRA QAGGRHVLIL PNNSITLDGS RSTDDRGIVS YLWIRDGQSP AAGDVIGGSD
     HRAALQLTNL VEGVYTFHLL VTDSQGASDS DAATVEVLPD PKKDGLVELI LQVGVEQLTE
     QQKETLVRQL AVLLNVLDSD VKVLKIQAHT DVSTVIVFYV QSGSPFKVLR AAAVARNLHK
     RLSKEKEAFL LFKVLRVDTA GCLLKCSGHG HCDPITKRCI CSQLWMENLI QRYMWDGESN
     CEWSVFYVAA LALTLTLLTG AVSWLCICCC RRRKRTKIRK KTKYTILDSM DEQERMELRP
     KYGIKHRSTE HNSSLMVSES EFESDQDTLF SRERMERGVL KGSLNGCARN GVSFGYYSKD
     R
//
ID   PARF_MOUSE              Reviewed;         725 AA.
AC   Q5U3K5; A2AJB0; Q3TAT5; Q3TRU4; Q6PDP8; Q8BFS4; Q8CGJ9;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Putative GTP-binding protein Parf;
GN   Name=Parf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-658.
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Corpora quadrigemina, Embryo, Head, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480; SER-482 AND
RP   SER-483, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594 AND THR-597, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482 AND SER-483, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482 AND SER-483, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: May enhance cellular proliferation. May reduce growth
CC       inhibitory activity of CDKN2A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable). Cytoplasm.
CC       Note=Predominantly cytoplasmic. Proposed to shuttle between
CC       cytoplasm and nucleus (By similarity).
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DR   EMBL; AK045520; BAC32404.1; -; mRNA.
DR   EMBL; AK081440; BAC38220.1; -; mRNA.
DR   EMBL; AK171643; BAE42583.1; -; mRNA.
DR   EMBL; AK162461; BAE36932.1; -; mRNA.
DR   EMBL; AL732590; CAM25173.1; -; Genomic_DNA.
DR   EMBL; BC023692; AAH23692.1; -; mRNA.
DR   EMBL; BC058585; AAH58585.1; -; mRNA.
DR   EMBL; BC085507; AAH85507.2; -; mRNA.
DR   IPI; IPI00349069; -.
DR   RefSeq; NP_001019787.2; NM_001024616.1.
DR   UniGene; Mm.29600; -.
DR   UniGene; Mm.443064; -.
DR   ProteinModelPortal; Q5U3K5; -.
DR   SMR; Q5U3K5; 41-228.
DR   STRING; Q5U3K5; -.
DR   PhosphoSite; Q5U3K5; -.
DR   PRIDE; Q5U3K5; -.
DR   Ensembl; ENSMUST00000058137; ENSMUSP00000058746; ENSMUSG00000015087.
DR   GeneID; 227624; -.
DR   KEGG; mmu:227624; -.
DR   UCSC; uc008isr.1; mouse.
DR   MGI; MGI:2442633; B230208H17Rik.
DR   GeneTree; ENSGT00390000016002; -.
DR   HOGENOM; HBG507170; -.
DR   HOVERGEN; HBG080325; -.
DR   InParanoid; Q5U3K5; -.
DR   OMA; SIFLEMM; -.
DR   OrthoDB; EOG4K6G4S; -.
DR   PhylomeDB; Q5U3K5; -.
DR   NextBio; 378682; -.
DR   ArrayExpress; Q5U3K5; -.
DR   Bgee; Q5U3K5; -.
DR   CleanEx; MM_B230208H17RIK; -.
DR   Genevestigator; Q5U3K5; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR013684; MIRO-like.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF08477; Miro; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; GTP-binding; Nucleotide-binding; Nucleus; Phosphoprotein.
FT   CHAIN         1    725       Putative GTP-binding protein Parf.
FT                                /FTId=PRO_0000274224.
FT   NP_BIND      50     57       GTP (Potential).
FT   NP_BIND     100    104       GTP (Potential).
FT   NP_BIND     177    179       GTP (Potential).
FT   REGION       39    279       Small GTPase-like.
FT   REGION      652    690       Interaction with CDKN2A (By similarity).
FT   MOD_RES     414    414       Phosphoserine (By similarity).
FT   MOD_RES     436    436       Phosphoserine (By similarity).
FT   MOD_RES     438    438       Phosphoserine (By similarity).
FT   MOD_RES     476    476       Phosphoserine (By similarity).
FT   MOD_RES     480    480       Phosphoserine.
FT   MOD_RES     482    482       Phosphoserine.
FT   MOD_RES     483    483       Phosphoserine.
FT   MOD_RES     502    502       Phosphoserine (By similarity).
FT   MOD_RES     506    506       Phosphothreonine (By similarity).
FT   MOD_RES     575    575       Phosphoserine (By similarity).
FT   MOD_RES     578    578       Phosphoserine (By similarity).
FT   MOD_RES     594    594       Phosphoserine.
FT   MOD_RES     597    597       Phosphothreonine.
FT   MOD_RES     637    637       Phosphoserine (By similarity).
FT   MOD_RES     638    638       Phosphoserine (By similarity).
FT   MOD_RES     722    722       Phosphotyrosine (By similarity).
FT   CONFLICT    520    520       R -> G (in Ref. 1; BAE42583).
FT   CONFLICT    670    670       S -> K (in Ref. 3; AAH58585).
SQ   SEQUENCE   725 AA;  79831 MW;  B538A8420DC04964 CRC64;
     MFSALKKLVG SEQAPGRDKN IPAGLQSMNQ ALQRRFAKGV QYNMKIVIRG DRNTGKTALW
     HRLQGKKFVE EYIPTQEIQV TSIHWNYKTT DDVVKVEVWD VVDKGKCKKR GDGLKTENDP
     QEAESELALD AEFLDVYKNC NGVVMMFDIT KQWTFNYVLR ELPKVPTHVP VCVLGNYRDM
     GEHRVILPDD VRDFIEHLDR PPGSSYFRYA ESSMKNSFGL KYLHKFFNIP FLQLQRETLL
     RQLETNQLDI DATLEELSVQ QETEDQNYSI FLEMMEARSR GHASPLAANG QSPSSGSQSP
     VVPPSAVSTG SSSPSTPQPA PQLSLGVSST CPSAPSPVPS LEAMPSSVHS SAPAPTPAPA
     PAPAQRRSII SRLFGTSPAA EVTPSPPEPA PALEAPARVQ NVEDFVPEDG LDRSFLEDTS
     VPKDKKVGAK GPQQDSDSDD GEALGGNPMV AGFQDDVDIE DQTHGKSLLP SDPMPSKNIS
     LSSEEEAEGL AGHPRVAPQQ CSEPETKWSS TKVSHPQKKR APTRGTPPWS DGLTTDDSER
     PQEGKDKQVS SESDPEGPIA AQMLSFVMDD PDFESDESDT QRRMGRFPVR EDLSDVTDED
     TGPAQPPPPS KLPGAFRLKN DSDLFGLGLE EMGPKESSDE DRDSKLPSKE KKKKKKKSKE
     EEEKTTKKKS KHKKSKDKEE GKEDRKKKRK PPRSKEQKAA DELEAFLGGG APGSRHPGGG
     DYEEL
//
ID   DJC11_MOUSE             Reviewed;         559 AA.
AC   Q5U458; Q8BP83; Q8C1Z4; Q8C6U5;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=DnaJ homolog subfamily C member 11;
GN   Name=Dnajc11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Lung, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the DNAJC11 family.
CC   -!- SIMILARITY: Contains 1 J domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC41027.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK053156; BAC35287.1; -; mRNA.
DR   EMBL; AK077544; BAC36856.1; -; mRNA.
DR   EMBL; AK089983; BAC41027.1; ALT_SEQ; mRNA.
DR   EMBL; AK171781; BAE42661.1; -; mRNA.
DR   EMBL; AK172542; BAE43060.1; -; mRNA.
DR   EMBL; BC085257; AAH85257.1; -; mRNA.
DR   IPI; IPI00226466; -.
DR   RefSeq; NP_766292.2; NM_172704.3.
DR   UniGene; Mm.21353; -.
DR   ProteinModelPortal; Q5U458; -.
DR   SMR; Q5U458; 12-89.
DR   STRING; Q5U458; -.
DR   PRIDE; Q5U458; -.
DR   Ensembl; ENSMUST00000062904; ENSMUSP00000051643; ENSMUSG00000039768.
DR   Ensembl; ENSMUST00000103200; ENSMUSP00000099489; ENSMUSG00000089825.
DR   GeneID; 230935; -.
DR   KEGG; mmu:230935; -.
DR   UCSC; uc008vys.1; mouse.
DR   UCSC; uc008vyt.1; mouse.
DR   CTD; 230935; -.
DR   MGI; MGI:2443386; Dnajc11.
DR   GeneTree; ENSGT00540000072084; -.
DR   HOGENOM; HBG445537; -.
DR   HOVERGEN; HBG080125; -.
DR   InParanoid; Q5U458; -.
DR   OrthoDB; EOG45TCMW; -.
DR   NextBio; 380306; -.
DR   ArrayExpress; Q5U458; -.
DR   Bgee; Q5U458; -.
DR   CleanEx; MM_DNAJC11; -.
DR   Genevestigator; Q5U458; -.
DR   GermOnline; ENSMUSG00000039768; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   InterPro; IPR001623; DnaJ_N.
DR   InterPro; IPR018253; Heat_shock_DnaJ_CS.
DR   InterPro; IPR003095; Hsp_DnaJ.
DR   Gene3D; G3DSA:1.10.287.110; DnaJ_N; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; DnaJ_N; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Coiled coil.
FT   CHAIN         1    559       DnaJ homolog subfamily C member 11.
FT                                /FTId=PRO_0000247158.
FT   DOMAIN       14     82       J.
FT   COILED      415    457       Potential.
FT   CONFLICT    195    195       I -> V (in Ref. 1; BAC35287).
FT   CONFLICT    256    256       T -> S (in Ref. 1; BAC41027).
SQ   SEQUENCE   559 AA;  63247 MW;  8251D2AA456A6338 CRC64;
     MATALSEEEL DNEDYYSLLN VRREASSEEL KAAYRRLCML YHPDKHRDPE LKSQAERLFN
     LVHQAYEVLS DPQTRAIYDI YGKRGLEMEG WEVVERKRTP AEIREEFERL QREREERRLQ
     QRTNPKGTIS VGVDATDLFD RYDEEYEDVS GSGFPQIEIN KMHISQSIEA PLTATDTAIL
     SGSLSTQNGN GGGSINFALR RVTSAKGWGE LEFGAGDLQG PLFGLKLFRN LTPRCFVTTN
     CALQFSSRGI RPGLTTVLAR NLDKNTVGYL QWRWGIQSAM NTSIVRDTKT CHFTVALQLG
     IPHSFALISY QHKFQDDDQT RVKGSLKAGF FGTIVEYGAE RKISRHSVLG AAVSIGVPQG
     VSLKVKLNRA SQTYFFPIHL TDQLLPSAVF YATVGPLVVY LAVHRLIIRP YLRAQKEKEL
     EKQRENTASD ILQKKQEAEA AVRLMQESVR RIIEAEESRM GLIIVNAWYG KFVNDKSRKN
     EKVKVIDVTV PLQCLVKDSK LILTEASKAG LPGFYDPCVG EEKSLRVLYQ FRGVLHQVMV
     PDSEALRIPK QSHRIDTDG
//
ID   GASP1_MOUSE             Reviewed;        1347 AA.
AC   Q5U4C1; A2AGB6; Q8BKR8; Q8BUN4; Q8BYK9; Q8CHF4; Q8R095;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=G-protein coupled receptor-associated sorting protein 1;
DE            Short=GASP-1;
GN   Name=Gprasp1; Synonyms=Kiaa0443;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-379 AND 943-1347 (ISOFORM
RP   1).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Hippocampus, and Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=15086532; DOI=10.1111/j.1471-4159.2004.02411.x;
RA   Simonin F., Karcher P., Boeuf J.J.-M., Matifas A., Kieffer B.L.;
RT   "Identification of a novel family of G protein-coupled receptor
RT   associated sorting proteins.";
RL   J. Neurochem. 89:766-775(2004).
CC   -!- FUNCTION: May modulate lysosomal sorting and functional down-
CC       regulation of a variety of G-protein coupled receptors. Targets
CC       receptors for degradation in lysosomes (By similarity).
CC   -!- SUBUNIT: Interacts with cytoplasmic tails of a variety of G-
CC       protein coupled receptors such as delta opioid receptor/OPRD1,
CC       beta-2 adrenergic receptor/ADRB2 and D4 dopamine receptor/DRD4 as
CC       well as D2 dopamine receptor/DRD2. Interacts with PER1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5U4C1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5U4C1-2; Sequence=VSP_019080;
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, with higher expression
CC       in the hippocampus, hypothalamus and olfactory bulb.
CC   -!- SIMILARITY: Belongs to the GPRASP family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC41425.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB093241; BAC41425.1; ALT_INIT; mRNA.
DR   EMBL; AL683822; CAM27375.1; -; Genomic_DNA.
DR   EMBL; BC027187; AAH27187.1; -; mRNA.
DR   EMBL; BC085157; AAH85157.1; -; mRNA.
DR   EMBL; AK039156; BAC30259.1; -; mRNA.
DR   EMBL; AK050919; BAC34459.2; -; mRNA.
DR   EMBL; AK083192; BAC38803.1; -; mRNA.
DR   IPI; IPI00229642; -.
DR   IPI; IPI00759976; -.
DR   RefSeq; NP_001004359.1; NM_001004359.2.
DR   RefSeq; NP_001005385.1; NM_001005385.1.
DR   RefSeq; NP_080357.4; NM_026081.5.
DR   UniGene; Mm.271980; -.
DR   ProteinModelPortal; Q5U4C1; -.
DR   STRING; Q5U4C1; -.
DR   PRIDE; Q5U4C1; -.
DR   Ensembl; ENSMUST00000057164; ENSMUSP00000061873; ENSMUSG00000043384.
DR   Ensembl; ENSMUST00000070053; ENSMUSP00000065114; ENSMUSG00000043384.
DR   Ensembl; ENSMUST00000113144; ENSMUSP00000108769; ENSMUSG00000043384.
DR   Ensembl; ENSMUST00000113145; ENSMUSP00000108770; ENSMUSG00000043384.
DR   Ensembl; ENSMUST00000113147; ENSMUSP00000108772; ENSMUSG00000043384.
DR   GeneID; 67298; -.
DR   KEGG; mmu:67298; -.
DR   NMPDR; fig|10090.3.peg.22157; -.
DR   UCSC; uc009uhn.1; mouse.
DR   CTD; 67298; -.
DR   MGI; MGI:1917418; Gprasp1.
DR   HOGENOM; HBG283587; -.
DR   HOVERGEN; HBG057167; -.
DR   InParanoid; Q5U4C1; -.
DR   OrthoDB; EOG47PX56; -.
DR   PhylomeDB; Q5U4C1; -.
DR   NextBio; 324156; -.
DR   ArrayExpress; Q5U4C1; -.
DR   Bgee; Q5U4C1; -.
DR   Genevestigator; Q5U4C1; -.
DR   GermOnline; ENSMUSG00000043384; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR006911; DUF634.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF04826; DUF634; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm.
FT   CHAIN         1   1347       G-protein coupled receptor-associated
FT                                sorting protein 1.
FT                                /FTId=PRO_0000239051.
FT   COMPBIAS   1109   1112       Poly-Leu.
FT   VAR_SEQ       1    473       Missing (in isoform 2).
FT                                /FTId=VSP_019080.
FT   CONFLICT    942    942       V -> L (in Ref. 1; BAC41425).
FT   CONFLICT    943    943       I -> F (in Ref. 4; BAC30259).
SQ   SEQUENCE   1347 AA;  151745 MW;  1FD29E59CBF91B59 CRC64;
     MTRAEVEPGA QAKAENKPGD ENANAAEVEP EAPLVVRPKV RTQIMTGARP KVKPKGTPGA
     RPKGETSTPG GAYAKCKPKA IPIARSKHDA QVWAPNKFRG ESMSKMGKQC QISAADPPLL
     SNDSGMVAQA KCLPVDRELA NMDTESIPKK ANSPAGFQPS YGSEEGTNMG SWYRARPVPK
     GEAYENSDFK WADKPSGSPS FWNRDEASTR FRPRKSMKAN NRFRHMAKQE ANTMPRHKNK
     QEFYNISSSD SEDESGKTPW FWPKDKTKVW SKPKEEPNSR SWFRSKKEVR VESTSGSECE
     NPTKSLFWSG EEAKSRSKPR ARKGVNMRAR QQAKREACSD AMSGAIDTNK KESWFLPEEK
     ANVFSKSKTK KEPRTRAVPK EEVKTKARAS TKQEARPEEE VLVGAWFWDT QESTMADRIS
     IKTTFVEEEP IVGDWFWSEE EASVDSETCH TSRPRAKEEQ VSSFCLGSGK KSSMESGPKA
     TSKSMPVAKE DEVVIGSWFW ADDEEINLQA DDESIFGSWF WGTGENSLRS VGVNCEKMPK
     AGEKEVTDSW FWAGDVNTEA EVEEQARSAS TKATIFVPWF WSEKQPNMDL GSEPCSDIMA
     GAEEEPIIGP WFWAKVDNSV EAEVNSKSSL EDEEEPIRSP WFGAREQTDM KYAAGIRYKP
     MAEAEDANKK SCVWAKEPCL YPTNRECLKS TLGEKEDTVD PWLWSNNYPR TKTITGSWLW
     AAEEGNIDDE TGEKIKLPTL EDNAFNSWFW KENEESIVEA PKREEFRPEA EEEDIIGSWF
     WAGDEDRFEP AAKINEENKI ASEDEDTVGS WFWGNEEASL EAVRRGTFES APGIKEEKVT
     GSWFWTDKAK VGAGSQTVET GSETEEEAIF ESLIWAAKKD SIQAGVKRVS KPKDDGNIAV
     GSWLWSSDKA TKEAKTLIVS EASPENGKES VVKFGSRAKD EVINKTGSGD NCKHSTEAET
     IVGAWFWEGD EASFESNPVP VCKAVCEPES SAEHEPDPSR RPQSWDEVTV QFKAGPWGKA
     GFPPMNPFRF PKEAASLFAE MFGGKPKLVE VGPEREPEPQ FPFQYDPSYR SVREIREHLK
     ARESAQPENW SCNCIQCELR IGSEEFEELL LLMDRNRDPF IHEISKIAMG MRGASQFTRD
     FIRNSGVVSL IEALLNYPSS RVRTRFLENM VRMAPPYPDL NMIETYVCQI CEDTFDYDLD
     SPDQLSGLTM ITHLTATSDY HKVVVNYLAG FFYLLNSGNT KTRFHVLKLL LNLSENLVMT
     KRLLVTDSVS EFMDLINREE SDENIQIVLA IFETISKHIQ KEALFSDDDD DDEEEDAVNL
     EPFISAFREA EKIAKELKRK PGNQKAP
//
ID   SFR19_MOUSE             Reviewed;        1256 AA.
AC   Q5U4C3; Q3UR01;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Splicing factor, arginine/serine-rich 19;
DE   AltName: Full=SR-related and CTD-associated factor 1;
GN   Name=Scaf1; Synonyms=Sfrs19;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, Embryonic brain, and Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; SER-510; SER-518;
RP   SER-691; SER-695; SER-912 AND THR-936, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-328; SER-691; SER-695
RP   AND SER-821, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May function in pre-mRNA splicing (By similarity).
CC   -!- SUBUNIT: Interacts with POLR2A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5U4C3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5U4C3-2; Sequence=VSP_027636, VSP_027637;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the splicing factor SR family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK141920; BAE24887.1; -; mRNA.
DR   EMBL; BC042576; AAH42576.1; -; mRNA.
DR   EMBL; BC043138; AAH43138.1; -; mRNA.
DR   EMBL; BC085153; AAH85153.1; -; mRNA.
DR   IPI; IPI00344430; -.
DR   IPI; IPI00856501; -.
DR   RefSeq; NP_001008422.1; NM_001008422.1.
DR   UniGene; Mm.28298; -.
DR   ProteinModelPortal; Q5U4C3; -.
DR   STRING; Q5U4C3; -.
DR   PhosphoSite; Q5U4C3; -.
DR   PRIDE; Q5U4C3; -.
DR   Ensembl; ENSMUST00000085383; ENSMUSP00000082501; ENSMUSG00000038406.
DR   Ensembl; ENSMUST00000117282; ENSMUSP00000114117; ENSMUSG00000038406.
DR   GeneID; 233208; -.
DR   KEGG; mmu:233208; -.
DR   UCSC; uc009gso.1; mouse.
DR   CTD; 233208; -.
DR   MGI; MGI:2141980; Scaf1.
DR   eggNOG; roNOG15318; -.
DR   GeneTree; ENSGT00530000063661; -.
DR   HOGENOM; HBG269033; -.
DR   HOVERGEN; HBG097942; -.
DR   InParanoid; Q5U4C3; -.
DR   OMA; PKELAPS; -.
DR   OrthoDB; EOG4MSD0F; -.
DR   PhylomeDB; Q5U4C3; -.
DR   NextBio; 381613; -.
DR   ArrayExpress; Q5U4C3; -.
DR   Bgee; Q5U4C3; -.
DR   CleanEx; MM_SCAF1; -.
DR   Genevestigator; Q5U4C3; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Alternative splicing; mRNA processing; mRNA splicing; Nucleus;
KW   Phosphoprotein; Repeat; RNA-binding.
FT   CHAIN         1   1256       Splicing factor, arginine/serine-rich 19.
FT                                /FTId=PRO_0000299407.
FT   REGION     1131   1256       Necessary for interaction with the CTD
FT                                domain of POLR2A (By similarity).
FT   COMPBIAS    185    268       Pro-rich.
FT   COMPBIAS    192    208       Ser-rich.
FT   COMPBIAS    269    281       Glu-rich.
FT   COMPBIAS    476    640       Arg-rich.
FT   COMPBIAS    710    821       Ser-rich.
FT   COMPBIAS    843    873       Lys-rich.
FT   COMPBIAS    956    983       Glu-rich.
FT   COMPBIAS   1228   1255       Pro-rich.
FT   MOD_RES     240    240       Phosphoserine.
FT   MOD_RES     302    302       Phosphoserine (By similarity).
FT   MOD_RES     304    304       Phosphoserine (By similarity).
FT   MOD_RES     312    312       Phosphoserine (By similarity).
FT   MOD_RES     328    328       Phosphothreonine.
FT   MOD_RES     442    442       Phosphoserine (By similarity).
FT   MOD_RES     447    447       Phosphoserine (By similarity).
FT   MOD_RES     491    491       Phosphoserine (By similarity).
FT   MOD_RES     493    493       Phosphoserine (By similarity).
FT   MOD_RES     510    510       Phosphoserine.
FT   MOD_RES     518    518       Phosphoserine.
FT   MOD_RES     520    520       Phosphoserine (By similarity).
FT   MOD_RES     577    577       Phosphoserine (By similarity).
FT   MOD_RES     579    579       Phosphoserine (By similarity).
FT   MOD_RES     676    676       Phosphoserine (By similarity).
FT   MOD_RES     682    682       Phosphoserine (By similarity).
FT   MOD_RES     689    689       Phosphotyrosine (By similarity).
FT   MOD_RES     691    691       Phosphoserine.
FT   MOD_RES     695    695       Phosphoserine.
FT   MOD_RES     819    819       Phosphoserine (By similarity).
FT   MOD_RES     821    821       Phosphoserine.
FT   MOD_RES     880    880       Phosphoserine (By similarity).
FT   MOD_RES     888    888       Phosphoserine (By similarity).
FT   MOD_RES     912    912       Phosphoserine.
FT   MOD_RES     922    922       Phosphoserine (By similarity).
FT   MOD_RES     923    923       Phosphothreonine (By similarity).
FT   MOD_RES     936    936       Phosphothreonine.
FT   MOD_RES     939    939       Phosphoserine (By similarity).
FT   MOD_RES     941    941       Phosphothreonine (By similarity).
FT   VAR_SEQ     161    166       VSPQSH -> GSCPVA (in isoform 2).
FT                                /FTId=VSP_027636.
FT   VAR_SEQ     167   1256       Missing (in isoform 2).
FT                                /FTId=VSP_027637.
SQ   SEQUENCE   1256 AA;  133842 MW;  E3D3BFCF441FE554 CRC64;
     MEEEDESRGK TEESGEDRGD GPPDRDPALS PSAFILRAIQ QAVGSSLQGD LPNDKDGARC
     RGLRWRRCCR SPRSEPRSQE SGAADTATVL DTAADSFLVE LVSILDPPDT WVPSRLDLQP
     GESEDMLELV AEVRIGDRDP MPLPVPSLFP RLRAWRTGKT VSPQSHASRP ACSRHLTLGT
     GDGGPAPPPA PSSASSSPSP SPSSSSPSPP PPPPPPPPPA LPAPRFDIYD PFHPTDEAYS
     PPPAPEQKYD PFEPTGSNPS SSAGTPSPEE EEEEEEEEEE EGLSQSISRI SETLAGIYDD
     NSLSQDFPGD DSPRREPPPP QTLGAPGTPP QADSTRAEGA PRRRVFVLGP EAEACHEGKV
     SVEVVTAGAP ALSLPPLPPT DPEIEEGEIV QPEEEPRVAV SLFRAARPRQ PPASVATLAS
     VAAPAAPPAS APRAPEGDDF LSLHADSDGE GALQVDLGEP PAPPAADARW GGLDLRRKIL
     TQRRERYRQR SASPGPPPAR KKARRERQRS GDPAPPDSPS WEAKKHRSRE RKLGSHSTAR
     RRSRSRSRRR SRSRSADRRR GGHRSRSREK RRRRRRSASP PPAASSSSSS RRERHRGKRR
     EGGKKKKKRS RSRAEKRSGD LEKLPASVPP SGSDRDSRRR GAVPPSIQDL TDHDLFAIKR
     TITVGRPDKA EPRAPSPAPA VSPKREVLYD SEGLSADERG GKSDKDRRRS GAASSSSSSR
     EKGSRRKALD GDRGRDRDRS SKKTRPPKDS TPGSGPLPKA PPSSGSSSSS SSCSSRKVKL
     QSKVAVLIRE GVSSTTPAKD SSSSGLGSIG VKFSRDRESR SPFLKPDERA PAEVAKVAPG
     SNKPKKTKAK AKAGAKKAKG TKGKTKPSKT RKKVRSGGSS TASGGPGSLK KSKADSCSQA
     ASAKGTEETS WSGEERTTKA PSTPPPKVAP PPPALTPDSQ TVDSSCKTPE VSFLPEEASE
     DTGVRVGAEE EEEEEEEEEE EEEQQPATTT ATSTAAAAPS TAPSAGSTAG DSGAEDGPAA
     RISQLPTLPP PMPWNLPAGV DCTTSGVLAL TALLFKMEEA NLASRAKAQE LIQATNQILS
     HRKPSSTLGV TPAPVPTSLG LPPGPSSYLL PGSLPIGGCG STPPTPTGLA PASDKREGSS
     SSEGRGDTDK YLKKLHTQER AVEEVKLAIK PYYQKKDITK EEYKDILRKA VHKICHSKSG
     EINPVKVSNL VRAYVQRYRY FRKHGRKPGD PPGPPRPPKE PGPPDKGGPG LPLPPL
//
ID   DYRK2_MOUSE             Reviewed;         599 AA.
AC   Q5U4C9;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Dual specificity tyrosine-phosphorylation-regulated kinase 2;
DE            EC=2.7.12.1;
GN   Name=Dyrk2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Role in the regulation of cellular growth and/or
CC       development. Regulates TP53 by phosphorylation on Ser-46 to induce
CC       apoptosis in response to DNA damage, functioning downstream of
CC       ATM. Inactivates GYS1 by phosphorylation at Ser-641, and
CC       potentially also a second phosphorylation site, thus regulating
CC       glycogen synthesis. Phosphorylates EIF2B5 at Ser-544, enabling its
CC       subsequent phosphorylation and inhibition by GSK3, and may play a
CC       more general role in the priming of GSK3 substrates (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- COFACTOR: Manganese (By similarity).
CC   -!- ENZYME REGULATION: Autophosphorylates on tyrosine residues (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Translocates into the nucleus following DNA
CC       damage (By similarity).
CC   -!- PTM: Phosphorylated on serine/threonine residues (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. MNB/DYRK subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC085145; AAH85145.1; -; mRNA.
DR   IPI; IPI00468101; -.
DR   RefSeq; NP_001014412.1; NM_001014390.2.
DR   UniGene; Mm.45565; -.
DR   UniGene; Mm.458174; -.
DR   HSSP; Q00534; 1BI8.
DR   ProteinModelPortal; Q5U4C9; -.
DR   SMR; Q5U4C9; 144-541.
DR   STRING; Q5U4C9; -.
DR   PhosphoSite; Q5U4C9; -.
DR   PRIDE; Q5U4C9; -.
DR   Ensembl; ENSMUST00000004281; ENSMUSP00000004281; ENSMUSG00000028630.
DR   GeneID; 69181; -.
DR   KEGG; mmu:69181; -.
DR   UCSC; uc007hea.1; mouse.
DR   CTD; 69181; -.
DR   MGI; MGI:1330301; Dyrk2.
DR   eggNOG; roNOG07594; -.
DR   GeneTree; ENSGT00570000079111; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG051426; -.
DR   InParanoid; Q5U4C9; -.
DR   OMA; QVPHDHV; -.
DR   OrthoDB; EOG4QRH3Z; -.
DR   PhylomeDB; Q5U4C9; -.
DR   BRENDA; 2.7.12.1; 244.
DR   NextBio; 328782; -.
DR   ArrayExpress; Q5U4C9; -.
DR   Bgee; Q5U4C9; -.
DR   Genevestigator; Q5U4C9; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0042771; P:DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis; ISS:UniProtKB.
DR   GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; ATP-binding; Cytoplasm; Kinase; Magnesium; Manganese;
KW   Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT   CHAIN         1    599       Dual specificity tyrosine-
FT                                phosphorylation-regulated kinase 2.
FT                                /FTId=PRO_0000291265.
FT   DOMAIN      220    533       Protein kinase.
FT   NP_BIND     226    234       ATP (By similarity).
FT   ACT_SITE    346    346       Proton acceptor (By similarity).
FT   BINDING     249    249       ATP (By similarity).
FT   MOD_RES     380    380       Phosphotyrosine (By similarity).
SQ   SEQUENCE   599 AA;  66556 MW;  2378D39A5E1E8056 CRC64;
     MLTRKPSAAA PAAYPTGRGG DTAVRQLQAS PGIGAGAPRS GVGTGPPSPI ALPPLRASNA
     TTTAHTIGGS KHTMNDHLHL NSHGQIQVQQ LFEDNSNKRT VLTTQPNGLT TVGKTGLPGV
     PERQLESIHR RQGSSTSLKS MEGMGKVKAS PMTPEQAMKQ YMQKLTAFEH HEIFSYPEIY
     FLGPNAKKRQ GMTGGPNNGG YDDDQGSYVQ VPHDHVAYRY EVLKVIGKGS FGQVVKAYDH
     KVHQHVALKM VRNEKRFHRQ AAEEIRILEH LRKQDKDNTM NVIHMLENFT FRNHICMTFE
     LLSMNLYELI KKNKFQGFSL PLVRKFAHSI LQCLDALHKN RIIHCDLKPE NILLKQQGRS
     SIKVIDFGSS CYEHQRVYTY IQSRFYRAPE VILGARYGMP IDMWSLGCIL AELLTGYPLL
     PGEDEGDQLA CMIELLGMPS QKLLDASKRA KNFVSSKGYP RYCTVTTLSD GSVVLNGGRS
     RRGKLRGPPE SREWGNALKG CDDPLFLDFL KQCLEWDPAV RMTPGQALRH PWLRRRLPKP
     PTGEKTAVKR VTESTGAITS ISKLPPPSSS ASKLRTNLAQ MTDANGNIQQ RTVLPKLVS
//
ID   SC5A6_MOUSE             Reviewed;         634 AA.
AC   Q5U4D8;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Sodium-dependent multivitamin transporter;
DE            Short=Na(+)-dependent multivitamin transporter;
DE   AltName: Full=Solute carrier family 5 member 6;
GN   Name=Slc5a6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Transports pantothenate, biotin and lipoate in the
CC       presence of sodium.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF)
CC       (TC 2.A.21) family.
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DR   EMBL; BC085132; AAH85132.1; -; mRNA.
DR   IPI; IPI00225228; -.
DR   RefSeq; NP_001171092.1; NM_001177621.1.
DR   RefSeq; NP_001171093.1; NM_001177622.1.
DR   RefSeq; NP_808538.1; NM_177870.5.
DR   UniGene; Mm.205463; -.
DR   ProteinModelPortal; Q5U4D8; -.
DR   STRING; Q5U4D8; -.
DR   PRIDE; Q5U4D8; -.
DR   Ensembl; ENSMUST00000006817; ENSMUSP00000006817; ENSMUSG00000006641.
DR   Ensembl; ENSMUST00000080431; ENSMUSP00000079291; ENSMUSG00000006641.
DR   Ensembl; ENSMUST00000114665; ENSMUSP00000110313; ENSMUSG00000006641.
DR   Ensembl; ENSMUST00000114668; ENSMUSP00000110316; ENSMUSG00000006641.
DR   GeneID; 330064; -.
DR   KEGG; mmu:330064; -.
DR   CTD; 330064; -.
DR   MGI; MGI:2660847; Slc5a6.
DR   HOGENOM; HBG446891; -.
DR   HOVERGEN; HBG057280; -.
DR   InParanoid; Q5U4D8; -.
DR   OrthoDB; EOG4X6C80; -.
DR   ArrayExpress; Q5U4D8; -.
DR   Bgee; Q5U4D8; -.
DR   Genevestigator; Q5U4D8; -.
DR   GermOnline; ENSMUSG00000006641; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR001734; Na/solute_symporter.
DR   InterPro; IPR018212; Na/solute_symporter_CS.
DR   InterPro; IPR019900; Na/solute_symporter_subgr.
DR   PANTHER; PTHR11819; Na/solut_symport; 1.
DR   Pfam; PF00474; SSF; 1.
DR   TIGRFAMs; TIGR00813; sss; 1.
DR   PROSITE; PS00456; NA_SOLUT_SYMP_1; 1.
DR   PROSITE; PS00457; NA_SOLUT_SYMP_2; FALSE_NEG.
DR   PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
PE   2: Evidence at transcript level;
KW   Biotin; Glycoprotein; Ion transport; Membrane; Sodium;
KW   Sodium transport; Symport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    634       Sodium-dependent multivitamin
FT                                transporter.
FT                                /FTId=PRO_0000105387.
FT   TRANSMEM     23     43       Helical; (Potential).
FT   TRANSMEM     65     85       Helical; (Potential).
FT   TRANSMEM    100    120       Helical; (Potential).
FT   TRANSMEM    142    162       Helical; (Potential).
FT   TRANSMEM    175    195       Helical; (Potential).
FT   TRANSMEM    207    227       Helical; (Potential).
FT   TRANSMEM    255    275       Helical; (Potential).
FT   TRANSMEM    295    315       Helical; (Potential).
FT   TRANSMEM    350    370       Helical; (Potential).
FT   TRANSMEM    403    423       Helical; (Potential).
FT   TRANSMEM    427    447       Helical; (Potential).
FT   TRANSMEM    455    475       Helical; (Potential).
FT   TRANSMEM    526    546       Helical; (Potential).
FT   CARBOHYD    488    488       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    497    497       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   634 AA;  68527 MW;  13A9702228B6E7DB CRC64;
     MSVASTAAPF HTTSGSSGAI STFSDVDYVV FGLLLVLSLV IGLYHACRGW GHHTVGELLM
     ADRKMGCLPV ALSLLATFQS AVAILGAPAE IFRFGTQYWF LGCSYFLGLL IPAHIFIPVF
     YRLHLTSAYE YLELRFNKAV RICGTVTFIF QMVIYMGVAL YAPSLALNAV TGFDLWLSVL
     ALGIVCNIYT ALGGLKAVIW TDVFQTLVMF LGQLVVIIVG AARVGGLGHV WNVTSQHGLI
     SGINLDPDPF VRHTFWTLAF GGVFMMLSLY GVNQAQVQRY LSSHSERAAV LSCYAVFPCQ
     QVALCMSCLI GLVMFAYYNM YSMSPELKQA APDQLVLYFV MDLLKDMPGL PGLFVACLFS
     GSLSTISSAF NSLATVTMED LIQPWFPQLT ETRAIMLSRG LAFAYGLVCL GMAYISSHLG
     SVLQAALSIF GMVGGPLLGL FCLGLFFPCA NPLGAIVGLL TGLTMAFWIG IGSIVSRMSS
     AVAPPPLNGS SSFLPANVTV AAVTTVMPST LSKPTGLQHF YSLSYLWYSA HNSTTVIVVG
     LIVSLLTGGM RGRSLNPGTI YPVLPKLLAL LPLSCQKRLC WRSHSQDIPV IPNLFPEKMR
     NGVLQDSTDK ERMAEDGLVH QPCSPTYVVQ ETSL
//
ID   Q5UE59_MOUSE            Unreviewed;       542 AA.
AC   Q5UE59;
DT   07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT   07-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   SubName: Full=Kinesin light chain-1;
GN   Name=Klc1; Synonyms=Kns2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6;
RX   PubMed=17332754; DOI=10.1038/sj.emboj.7601609;
RA   Araki Y., Kawano T., Taru H., Saito Y., Wada S., Miyamoto K.,
RA   Kobayashi H., Ishikawa H.O., Ohsugi Y., Yamamoto T., Matsuno K.,
RA   Kinjo M., Suzuki T.;
RT   "The novel cargo Alcadein induces vesicle association of kinesin-1
RT   motor components and activates axonal transport.";
RL   EMBO J. 26:1475-1486(2007).
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DR   EMBL; AY753300; AAV30550.1; -; mRNA.
DR   IPI; IPI00874549; -.
DR   RefSeq; NP_032476.2; NM_008450.2.
DR   UniGene; Mm.278357; -.
DR   ProteinModelPortal; Q5UE59; -.
DR   SMR; Q5UE59; 187-494.
DR   STRING; Q5UE59; -.
DR   Ensembl; ENSMUST00000118471; ENSMUSP00000113171; ENSMUSG00000021288.
DR   GeneID; 16593; -.
DR   KEGG; mmu:16593; -.
DR   UCSC; uc007pdv.1; mouse.
DR   CTD; 16593; -.
DR   MGI; MGI:107978; Klc1.
DR   GeneTree; ENSGT00390000006393; -.
DR   HOVERGEN; HBG006217; -.
DR   NextBio; 290149; -.
DR   ArrayExpress; Q5UE59; -.
DR   Bgee; Q5UE59; -.
DR   Genevestigator; Q5UE59; -.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0035253; C:ciliary rootlet; IDA:MGI.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR   GO; GO:0005871; C:kinesin complex; IEA:InterPro.
DR   GO; GO:0043227; C:membrane-bounded organelle; IDA:MGI.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0008088; P:axon cargo transport; IMP:MGI.
DR   InterPro; IPR002151; Kinesin_light.
DR   InterPro; IPR015792; Kinesin_light_repeat.
DR   InterPro; IPR015390; Rabaptin_Rab5-bd.
DR   InterPro; IPR001440; TPR-1.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 2.
DR   Pfam; PF09311; Rab5-bind; 1.
DR   Pfam; PF00515; TPR_1; 3.
DR   PRINTS; PR00381; KINESINLIGHT.
DR   SMART; SM00028; TPR; 5.
DR   PROSITE; PS01160; KINESIN_LIGHT; 4.
DR   PROSITE; PS50005; TPR; 6.
DR   PROSITE; PS50293; TPR_REGION; 2.
PE   2: Evidence at transcript level;
KW   Repeat; TPR repeat.
SQ   SEQUENCE   542 AA;  61629 MW;  5A44688CEA0AB123 CRC64;
     MYDNMSTMVY IKEEKLEKLT QDEIISKTKQ VIQGLEALKN EHNSILQSLL ETLKCLKKDD
     ESNLVEEKSS MIRKSLEMLE LGLSEAQVMM ALSNHLNAVE SEKQKLRAQV RRLCQENQWL
     RDELANTQQK LQKSEQSVAQ LEEEKKHLEF MNQLKKYDDD ISPSEDKDSD SSKEPLDDLF
     PNDEDEPGQG IQQQHSSAAA AAQQGGYEIP ARLRTLHNLV IQYASQGRYE VAVPLCKQAL
     EDLEKTSGHD HPDVATMLNI LALVYRDQNK YKDAANLLND ALAIREKTLG RDHPAVAATL
     NNLAVLYGKR GKYKEAEPLC KRALEIREKV LGKDHPDVAK QLNNLALLCQ NQGKYEEVEY
     YYQRALGIYQ TKLGPDDPNV AKTKNNLASC YLKQGKFKQA ETLYKEILTR AHEREFGSVD
     DENKPIWMHA EEREECKGKQ KDGSAFGEYG GWYKACKVDS PTVTTTLKNL GALYRRQGKF
     EAAETLEEAA MRSRKQGLDN VHKQRVAEVL NDPESMEKRR SRESLNMDVV KYESGPDGGE
     EA
//
ID   F169A_MOUSE             Reviewed;         665 AA.
AC   Q5XG69; Q69ZW7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Protein FAM169A;
GN   Name=Fam169a; Synonyms=Kiaa0888;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic germ cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-630; SER-631 AND
RP   SER-632, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
CC   -!- SIMILARITY: Belongs to the FAM169 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH84589.1; Type=Erroneous initiation;
CC       Sequence=BAD32329.1; Type=Erroneous initiation;
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DR   EMBL; AK173051; BAD32329.1; ALT_INIT; mRNA.
DR   EMBL; BC084589; AAH84589.1; ALT_INIT; mRNA.
DR   IPI; IPI00808550; -.
DR   RefSeq; NP_001093928.1; NM_001100458.1.
DR   RefSeq; NP_001139517.1; NM_001146045.1.
DR   UniGene; Mm.458280; -.
DR   PhosphoSite; Q5XG69; -.
DR   PRIDE; Q5XG69; -.
DR   Ensembl; ENSMUST00000042517; ENSMUSP00000043738; ENSMUSG00000041817.
DR   GeneID; 320557; -.
DR   KEGG; mmu:320557; -.
DR   CTD; 320557; -.
DR   MGI; MGI:2444268; Fam169a.
DR   eggNOG; roNOG12478; -.
DR   GeneTree; ENSGT00510000048902; -.
DR   HOGENOM; HBG282332; -.
DR   HOVERGEN; HBG107873; -.
DR   InParanoid; Q5XG69; -.
DR   OrthoDB; EOG4W9J3J; -.
DR   NextBio; 396961; -.
DR   ArrayExpress; Q5XG69; -.
DR   Bgee; Q5XG69; -.
DR   Genevestigator; Q5XG69; -.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    665       Protein FAM169A.
FT                                /FTId=PRO_0000320588.
FT   COMPBIAS    375    453       Asp/Glu-rich.
FT   MOD_RES     445    445       Phosphoserine (By similarity).
FT   MOD_RES     447    447       Phosphoserine (By similarity).
FT   MOD_RES     614    614       Phosphoserine (By similarity).
FT   MOD_RES     630    630       Phosphoserine.
FT   MOD_RES     631    631       Phosphoserine.
FT   MOD_RES     632    632       Phosphoserine.
FT   CONFLICT    112    112       E -> G (in Ref. 2; AAH84589).
FT   CONFLICT    339    339       R -> H (in Ref. 2; AAH84589).
SQ   SEQUENCE   665 AA;  73259 MW;  1418A156EE8877C8 CRC64;
     MAFPVDLLDN CTHEELENSS EDYLSSLRCG DPEHPECFSS LNITIPVSLS NVGFVPLYGG
     NQTQKILALF APEDSLTAVA LYLVGQWWAI DDIVKTSEPS REGLKQVSTL GERVVLYVLN
     RIIYRKQEME RNEIPFLCHS STDYAKILWK KGEAVGFYSV KPTGSLCASF LTQNYQLPVL
     DTMFIRKKYR GKDLGLHMLE DFVDSFTEDA LGLRYPLSSL MYTASKQYFE KYPGDHELLW
     EVEGVGHWHQ RVPVTRALQR EAIKATDVSQ YEATRPVSGE YGLAAVPEHE PGLDDTQSSE
     LQIHSLKDAF ASTSEGPEKT PVSTRTRSSH LKRPKIGKRF QDSEFSSSQG EDENVAKTSP
     TASVNKIEYA ARTSESSEEF LEEEPEQGVI DFEDESGDKD AQPALETQPR LQKQDGDKDS
     ALEPVNGEVM DAALKPSLTT EDEDSTSEGL EEDLKVPPFN SSGEPGNPVP LVAESSKVPE
     ATLAKTSPDT DSEMLIDQSP SDDKGHTEEN LSPVSKKKTL LGSSDNVATV SNIEKSDGNF
     PNSVVPEFPE EPVSQNLSPN TTSSVEDQGE EGAPEAQEPS ATQSSLIEVE LEDAPFPQNA
     GQKSQSEEQS EASSEHLEQF TQSAEKAVDS SSEEIEVEVP VVDRRNLRRK AKGHKGPGKK
     KAKLT
//
ID   ACBD5_MOUSE             Reviewed;         508 AA.
AC   Q5XG73; A2AQX9; A2AQY0; Q6P7V7; Q7TSC2; Q8BKU6; Q8CI99; Q9CW41;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Acyl-CoA-binding domain-containing protein 5;
GN   Name=Acbd5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=FVB/N; TISSUE=Colon, Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-163; SER-184; SER-185;
RP   SER-187; SER-191 AND SER-418, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q5XG73-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5XG73-2; Sequence=VSP_025450;
CC       Name=3;
CC         IsoId=Q5XG73-3; Sequence=VSP_025450, VSP_025451;
CC   -!- SIMILARITY: Contains 1 ACB (acyl-CoA-binding) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH35202.1; Type=Erroneous initiation;
CC       Sequence=AAH53518.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK005001; BAB23735.2; -; mRNA.
DR   EMBL; AK050450; BAC34262.1; -; mRNA.
DR   EMBL; AK147839; BAE28174.1; -; mRNA.
DR   EMBL; AL845257; CAM19533.1; -; Genomic_DNA.
DR   EMBL; AL845257; CAM19534.1; -; Genomic_DNA.
DR   EMBL; AL845257; CAM19535.1; -; Genomic_DNA.
DR   EMBL; AL845257; CAM19536.1; -; Genomic_DNA.
DR   EMBL; BC035202; AAH35202.1; ALT_INIT; mRNA.
DR   EMBL; BC053518; AAH53518.1; ALT_INIT; mRNA.
DR   EMBL; BC061484; AAH61484.2; -; mRNA.
DR   EMBL; BC084584; AAH84584.1; -; mRNA.
DR   IPI; IPI00229804; -.
DR   IPI; IPI00754110; -.
DR   IPI; IPI00845729; -.
DR   RefSeq; NP_001095906.1; NM_001102436.1.
DR   RefSeq; NP_001095907.1; NM_001102437.1.
DR   RefSeq; NP_001095908.1; NM_001102438.1.
DR   RefSeq; NP_083069.1; NM_028793.3.
DR   UniGene; Mm.181973; -.
DR   UniGene; Mm.439111; -.
DR   HSSP; P07107; 1HB6.
DR   ProteinModelPortal; Q5XG73; -.
DR   SMR; Q5XG73; 42-133.
DR   PhosphoSite; Q5XG73; -.
DR   PRIDE; Q5XG73; -.
DR   Ensembl; ENSMUST00000114526; ENSMUSP00000110172; ENSMUSG00000026781.
DR   Ensembl; ENSMUST00000114529; ENSMUSP00000110175; ENSMUSG00000026781.
DR   GeneID; 74159; -.
DR   KEGG; mmu:74159; -.
DR   NMPDR; fig|10090.3.peg.5513; -.
DR   CTD; 74159; -.
DR   MGI; MGI:1921409; Acbd5.
DR   eggNOG; roNOG09629; -.
DR   GeneTree; ENSGT00530000063580; -.
DR   HOVERGEN; HBG106445; -.
DR   OrthoDB; EOG4J3WGS; -.
DR   PhylomeDB; Q5XG73; -.
DR   NextBio; 339946; -.
DR   ArrayExpress; Q5XG73; -.
DR   Bgee; Q5XG73; -.
DR   CleanEx; MM_ACBD5; -.
DR   Genevestigator; Q5XG73; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000062; F:fatty-acyl-CoA binding; IEA:InterPro.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR022408; Acyl-CoA-binding_prot_CS.
DR   InterPro; IPR000582; Acyl-CoA-binding_protein.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR016347; M-assoc_diazepam-bd-inh.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   PANTHER; PTHR23310; ACBP; 1.
DR   Pfam; PF00887; ACBP; 1.
DR   PIRSF; PIRSF002412; MA_DBI; 1.
DR   PRINTS; PR00689; ACOABINDINGP.
DR   SUPFAM; SSF47027; ACBP; 1.
DR   PROSITE; PS00880; ACB_1; 1.
DR   PROSITE; PS51228; ACB_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Lipid-binding; Membrane;
KW   Phosphoprotein; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    508       Acyl-CoA-binding domain-containing
FT                                protein 5.
FT                                /FTId=PRO_0000287378.
FT   TRANSMEM    480    500       Helical; (Potential).
FT   DOMAIN       44    133       ACB.
FT   COILED      181    214       Potential.
FT   COILED      428    453       Potential.
FT   COMPBIAS     15     19       Poly-Cys.
FT   COMPBIAS    502    505       Poly-Arg.
FT   MOD_RES     130    130       Phosphothreonine (By similarity).
FT   MOD_RES     134    134       Phosphothreonine (By similarity).
FT   MOD_RES     159    159       Phosphoserine (By similarity).
FT   MOD_RES     163    163       Phosphothreonine.
FT   MOD_RES     184    184       Phosphoserine.
FT   MOD_RES     185    185       Phosphoserine.
FT   MOD_RES     187    187       Phosphoserine.
FT   MOD_RES     191    191       Phosphoserine.
FT   MOD_RES     206    206       Phosphoserine (By similarity).
FT   MOD_RES     246    246       Phosphoserine (By similarity).
FT   MOD_RES     365    365       Phosphoserine (By similarity).
FT   MOD_RES     395    395       Phosphoserine (By similarity).
FT   MOD_RES     405    405       Phosphoserine (By similarity).
FT   MOD_RES     414    414       Phosphoserine (By similarity).
FT   MOD_RES     418    418       Phosphoserine.
FT   VAR_SEQ       1     36       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_025450.
FT   VAR_SEQ     387    387       R -> RV (in isoform 3).
FT                                /FTId=VSP_025451.
SQ   SEQUENCE   508 AA;  56614 MW;  B8345C43231DDAA8 CRC64;
     MLFLAFHAGS WGSWCCCCCV ITADRPWDRG RRWQLEMADT PSVYETRFEA AVKVIQSLPK
     NGSFQPTNEM MLKFYSFYKQ ATEGPCKLSR PGFWDPIGRY KWDAWSSLGD MTKEEAMIAY
     VEEMKKIIET MPMTEKVEEL LHVIGPFYEI VEDKKSSKSS DLTSDLGNVL TSSNAKAVNG
     KAESSDSGAE SEEEEAQEEL KGAEQSGSDD KKTLKKSADK NLEIIVTNGY KGSFVQDIQS
     DIHTDSSRST RSSEDEKPGD ESSQQTGHTI VCAHQDRNED PSEDASGIHH LTSDSDSEVY
     CDSMEQFGQE EYYLGGDPTQ HLESSGFCED AQQSPGNGSI GKMWMVAVKG KGEVKHGGED
     GRSSSGAPHR ETRGGESEDF SSVRRGRGNR IPHLSEGPKG RQVGSGGDGE RWGSDRGSRG
     SLNEQIALVL IRLQEDMQNV LQRLHKLETL TASQAKLSLQ TSNQPSSQRP AWWPFEMSPG
     ALAFAIIWPF IAQWLAHLYY QRRRRKLN
//
ID   LEO1_MOUSE              Reviewed;         667 AA.
AC   Q5XJE5; Q640R1;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=RNA polymerase-associated protein LEO1;
GN   Name=Leo1; Synonyms=Gm185;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-659, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278; SER-280; SER-608;
RP   SER-609; SER-611 AND SER-615, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247; SER-255; SER-295;
RP   SER-297 AND SER-631, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: The PAF1 complex is a multifunctional complex. The PAF1
CC       complex interacts with POLR2A. May be involved in both initiation
CC       and elongation, histone methylation and RNA processing.
CC   -!- SUBUNIT: Component of the PAF1 complex, which consists of at least
CC       of CDC73, PAF1, LEO1, CTR9. Interacts with CDC73 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5XJE5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5XJE5-2; Sequence=VSP_020054, VSP_020055;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the LEO1 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC082540; AAH82540.1; -; mRNA.
DR   EMBL; BC083358; AAH83358.1; -; mRNA.
DR   IPI; IPI00474486; -.
DR   IPI; IPI00776281; -.
DR   RefSeq; NP_001034611.1; NM_001039522.1.
DR   UniGene; Mm.41508; -.
DR   STRING; Q5XJE5; -.
DR   PhosphoSite; Q5XJE5; -.
DR   PRIDE; Q5XJE5; -.
DR   Ensembl; ENSMUST00000048937; ENSMUSP00000046905; ENSMUSG00000042487.
DR   GeneID; 235497; -.
DR   KEGG; mmu:235497; -.
DR   UCSC; uc009qsh.1; mouse.
DR   CTD; 235497; -.
DR   MGI; MGI:2685031; Leo1.
DR   eggNOG; roNOG15591; -.
DR   GeneTree; ENSGT00550000074952; -.
DR   HOGENOM; HBG715600; -.
DR   HOVERGEN; HBG081913; -.
DR   InParanoid; Q5XJE5; -.
DR   OrthoDB; EOG4HQDJC; -.
DR   NextBio; 382712; -.
DR   ArrayExpress; Q5XJE5; -.
DR   Bgee; Q5XJE5; -.
DR   Genevestigator; Q5XJE5; -.
DR   GermOnline; ENSMUSG00000042487; Mus musculus.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR007149; Leo1.
DR   Pfam; PF04004; Leo1; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Nucleus; Phosphoprotein;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    667       RNA polymerase-associated protein LEO1.
FT                                /FTId=PRO_0000247820.
FT   COMPBIAS     26    330       Asp-rich.
FT   MOD_RES      10     10       Phosphoserine (By similarity).
FT   MOD_RES      14     14       Phosphoserine (By similarity).
FT   MOD_RES     151    151       Phosphoserine (By similarity).
FT   MOD_RES     154    154       Phosphoserine (By similarity).
FT   MOD_RES     162    162       Phosphoserine (By similarity).
FT   MOD_RES     171    171       Phosphoserine (By similarity).
FT   MOD_RES     179    179       Phosphoserine (By similarity).
FT   MOD_RES     189    189       Phosphothreonine (By similarity).
FT   MOD_RES     198    198       Phosphoserine (By similarity).
FT   MOD_RES     206    206       Phosphoserine (By similarity).
FT   MOD_RES     213    213       Phosphoserine (By similarity).
FT   MOD_RES     221    221       Phosphoserine (By similarity).
FT   MOD_RES     230    230       Phosphoserine (By similarity).
FT   MOD_RES     239    239       Phosphoserine (By similarity).
FT   MOD_RES     247    247       Phosphoserine.
FT   MOD_RES     255    255       Phosphoserine.
FT   MOD_RES     272    272       Phosphoserine (By similarity).
FT   MOD_RES     278    278       Phosphoserine.
FT   MOD_RES     280    280       Phosphoserine.
FT   MOD_RES     295    295       Phosphoserine.
FT   MOD_RES     297    297       Phosphoserine.
FT   MOD_RES     301    301       Phosphoserine (By similarity).
FT   MOD_RES     303    303       Phosphothreonine (By similarity).
FT   MOD_RES     552    552       Phosphoserine (By similarity).
FT   MOD_RES     608    608       Phosphoserine.
FT   MOD_RES     609    609       Phosphoserine.
FT   MOD_RES     611    611       Phosphoserine.
FT   MOD_RES     615    615       Phosphoserine.
FT   MOD_RES     631    631       Phosphoserine.
FT   MOD_RES     659    659       Phosphoserine.
FT   VAR_SEQ     308    324       DNNGTMDLFGGADDISS -> GSPFTLYAGLLHSSLCL
FT                                (in isoform 2).
FT                                /FTId=VSP_020054.
FT   VAR_SEQ     325    667       Missing (in isoform 2).
FT                                /FTId=VSP_020055.
SQ   SEQUENCE   667 AA;  75641 MW;  07FA68ACF7A8EB89 CRC64;
     MADMEDLFGS EAESEAERKD SESESDSDSD QDNGASGSNA SGSESDQDDR GDSGQPSNKE
     LFGDDSEEEG ASHHSGSDNH SERSDNRSEA SERSDHEDNE PSDEDQHSGS EAHNDDDDEG
     HRSDEGSRHS EAEGSEKAQS DDEKWDGEDK SDQSDDEKLQ NSDDEDREQG SDEDKLQNSD
     DDEEKMQNTD DEDRAQISDD DRQQLSEEEK GNSDDEHPVA SDNDEEKQNS DDEDQPQVSD
     EEKMQNSDDE RPQVSDEDGR RSDGEEEQDQ KSESARGSDS EDEVLRLKRK NAIPSDSEAD
     SDTEVPKDNN GTMDLFGGAD DISSGSDGED KPPTPGQPVD ENGLPQDQQE EEPIPETRIE
     VEIPKVNTDL GNDLYFVKLP NFLSVEPRPF DPQYYEDEFE DEEMLDEEGR TRLKLKVENT
     IRWRIRRDEE GNEIKESNAR IVKWSDGSMS LHLGNEVFDV YKAPLQGDHN HLFIRQGTGL
     QGQAVFKTKL TFRPHSTDSD THRKMTLSLA DRCSKTQKIR ILPMAGRDPE CQRTEMIKKE
     EERLRASIRR ESQQRRMREK QHQRGLSASY LEPDRYDEEE EGEESVSLAA IKNRYKGGIR
     EERARIYSSD SDEGSEEDKA QRLLKAKKLN SDEEGESSGK RKAEDDDKAN KKHKKYVISD
     EEEEEDD
//
ID   LMTK3_MOUSE             Reviewed;        1424 AA.
AC   Q5XJV6; Q52KF1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Serine/threonine-protein kinase LMTK3;
DE            EC=2.7.11.1;
DE   AltName: Full=Lemur tyrosine kinase 3;
DE   Flags: Precursor;
GN   Name=Lmtk3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-947, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-962 AND SER-977, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; BC083185; AAH83185.1; -; mRNA.
DR   EMBL; BC094377; AAH94377.1; -; mRNA.
DR   IPI; IPI00471270; -.
DR   RefSeq; NP_001005511.2; NM_001005511.2.
DR   UniGene; Mm.44928; -.
DR   HSSP; P08069; 1JQH.
DR   ProteinModelPortal; Q5XJV6; -.
DR   SMR; Q5XJV6; 124-414.
DR   PhosphoSite; Q5XJV6; -.
DR   PRIDE; Q5XJV6; -.
DR   Ensembl; ENSMUST00000072580; ENSMUSP00000072388; ENSMUSG00000062044.
DR   Ensembl; ENSMUST00000118564; ENSMUSP00000113323; ENSMUSG00000062044.
DR   Ensembl; ENSMUST00000120005; ENSMUSP00000112592; ENSMUSG00000062044.
DR   GeneID; 381983; -.
DR   KEGG; mmu:381983; -.
DR   UCSC; uc009gxd.1; mouse.
DR   CTD; 381983; -.
DR   MGI; MGI:3039582; Lmtk3.
DR   eggNOG; roNOG07762; -.
DR   GeneTree; ENSGT00600000084075; -.
DR   HOGENOM; HBG506033; -.
DR   HOVERGEN; HBG081921; -.
DR   InParanoid; Q5XJV6; -.
DR   OrthoDB; EOG4B8JCT; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 402812; -.
DR   ArrayExpress; Q5XJV6; -.
DR   Bgee; Q5XJV6; -.
DR   CleanEx; MM_LMTK3; -.
DR   Genevestigator; Q5XJV6; -.
DR   GermOnline; ENSMUSG00000062044; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21   1424       Serine/threonine-protein kinase LMTK3.
FT                                /FTId=PRO_0000259461.
FT   TRANSMEM     40     60       Helical; (Potential).
FT   DOMAIN      133    411       Protein kinase.
FT   NP_BIND     139    147       ATP (By similarity).
FT   COMPBIAS    416    842       Pro-rich.
FT   COMPBIAS   1117   1223       Pro-rich.
FT   COMPBIAS   1347   1421       Pro-rich.
FT   ACT_SITE    266    266       Proton acceptor (By similarity).
FT   BINDING     164    164       ATP (By similarity).
FT   MOD_RES     947    947       Phosphoserine.
FT   MOD_RES     962    962       Phosphoserine.
FT   MOD_RES     977    977       Phosphoserine.
FT   CONFLICT    811    811       K -> E (in Ref. 1; AAH94377).
SQ   SEQUENCE   1424 AA;  150891 MW;  86A0BACC47909C91 CRC64;
     MPAPGALILL AAVSASGCLA SPAHPDGFAL SRAPLAPPYA VVLISCSGLL AFIFLLLTCL
     CCKRGDVRFK EFENPEGEDC SGEYTPPAEE TSSSQSLPDV YILPLAEVSL PMPAPQPPHS
     DISTPLGLSR QHLSYLQEIG SGWFGKVILG EVFSDYSPAQ VVVKELRASA GPLEQRKFIS
     EAQPYRSLQH PNVLQCLGVC VETLPFLLIM EFCQLGDLKR YLRAQRPPEG MSPELPPRDL
     RTLQRMGLEI ARGLAHLHSH NYVHSDLALR NCLLTSDLTV RIGDYGLAHS NYKEDYYLTP
     ERLWVPLRWA APELLGELHG SFVLVDQSRE SNVWSLGVTL WELFEFGAQP YRHLSDEEVL
     AFVVRQQHVK LARPRLKLPY ADYWYDILQS CWRPPAQRPS ASDLQLQLTY LLSERPPRPP
     PPPPPPRDGP FPWPWPPSHS APRPGTLSSQ FPLLDGFPGA DPDDVLTVTE SSRGLNLECL
     WEKARRGAGR GGGAPPWQPA SAPPAPHTNP SNPFYEALST PSVLPVISAR SPSVSSEYYI
     RLEEHGSPPE PLFPNDWDPL DPGVPGPQAP QTPSEVPQLV SETWASPLFP APRPFPAQSS
     GSGGFLLSGW DPEGRGAGET LAGDPAEVLG EQGTAPWAEE EEEESSPGED SSSLGGGPSR
     RGPLPCPLCS REGPCSCLPL ERGDAVAGWG DHPALGCPHP PEDDSSLRAE RGSLADLPLV
     PPTSAPLEFL DPLMGAAAPQ YPGRGPPPAP PPPPPPPRAS AEPAASPDPP SALASPGSGL
     SSPGPKPGDS GYETETPFSP EGAFPGGGAA KEEGVPRPRA PPEPPDPGAP RPPPDPGPLP
     LPGSQEKPTF VVQVSTEQLL MSLREDVTKN LLGDKGSTPG ETGPRKAGRS PANREKGPGP
     NRDLTSLVSR KKVPSRSLPV NGVTVLENGK PGVPDMKEKV AENGLESPEK EERALVNGEP
     MSPEAGEKVL ANGVLMSPKS EEKVAENGVL RLPRNTERPP EIGPRRVPGP WEKTPETGGL
     APETLLDRAP APCEAALPQN GLEMAPGQLG PAPKSGNPDP GTEWRVHESG GAPRAPGAGK
     LDLGSGGRAL GGVGTAPAGG PASAVDAKAG WVDNSRPLPP PPQPLGAQQR RPEPVPLKAR
     PEVAQEEEPG VPDNRLGGDM APSVDEDPLK PERKGPEMPR LFLDLGPPQG NSEQIKAKLS
     RLSLALPPLT LTPFPGPGPR RPPWEGADAG AAGGEAGGAG APGPAEEDGE DEDEDEEDEE
     AAGSRDPGRT REAPVPVVVS SADGDTVRPL RGLLKSPRAA DEPEDSELER KRKMVSFHGD
     VTVYLFDQET PTNELSVQGT PEGDTEPSTP PAPPTPPHPT TPGDGFPNSD SGFGGSFEWA
     EDFPLLPPPG PPLCFSRFSV SPALETPGPP ARAPDARPAG PVEN
//
ID   ZDH20_MOUSE             Reviewed;         380 AA.
AC   Q5Y5T1; Q3TDL1; Q8VCL6; Q9D3Q8;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Probable palmitoyltransferase ZDHHC20;
DE            EC=2.3.1.-;
DE   AltName: Full=Zinc finger DHHC domain-containing protein 20;
DE            Short=DHHC-20;
GN   Name=Zdhhc20;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15603741; DOI=10.1016/j.neuron.2004.12.005;
RA   Fukata M., Fukata Y., Adesnik H., Nicoll R.A., Bredt D.S.;
RT   "Identification of PSD-95 palmitoylating enzymes.";
RL   Neuron 44:987-996(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Corpora quadrigemina, Forelimb, Ovary, and Uterus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: Palmitoyl-CoA + protein-cysteine = S-palmitoyl
CC       protein + CoA.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5Y5T1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5Y5T1-2; Sequence=VSP_016278;
CC   -!- TISSUE SPECIFICITY: Highest levels in lung.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase
CC       activity (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC   -!- SIMILARITY: Contains 1 DHHC-type zinc finger.
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DR   EMBL; AY668951; AAU89705.1; -; mRNA.
DR   EMBL; AK017158; BAB30620.1; -; mRNA.
DR   EMBL; AK031184; BAC27294.1; -; mRNA.
DR   EMBL; AK049270; BAC33648.1; -; mRNA.
DR   EMBL; AK140182; BAE24268.1; -; mRNA.
DR   EMBL; AK163174; BAE37221.1; -; mRNA.
DR   EMBL; AK170139; BAE41590.1; -; mRNA.
DR   EMBL; BC019536; AAH19536.1; -; mRNA.
DR   IPI; IPI00311064; -.
DR   IPI; IPI00620467; -.
DR   RefSeq; NP_083768.4; NM_029492.4.
DR   UniGene; Mm.29044; -.
DR   PhosphoSite; Q5Y5T1; -.
DR   PRIDE; Q5Y5T1; -.
DR   Ensembl; ENSMUST00000022541; ENSMUSP00000022541; ENSMUSG00000021969.
DR   Ensembl; ENSMUST00000089473; ENSMUSP00000086900; ENSMUSG00000021969.
DR   GeneID; 75965; -.
DR   KEGG; mmu:75965; -.
DR   UCSC; uc007udr.1; mouse.
DR   UCSC; uc007uds.1; mouse.
DR   CTD; 75965; -.
DR   MGI; MGI:1923215; Zdhhc20.
DR   eggNOG; roNOG15411; -.
DR   GeneTree; ENSGT00570000078748; -.
DR   HOGENOM; HBG443608; -.
DR   HOVERGEN; HBG055108; -.
DR   InParanoid; Q5Y5T1; -.
DR   OMA; FITFVVV; -.
DR   OrthoDB; EOG45B1FN; -.
DR   PhylomeDB; Q5Y5T1; -.
DR   NextBio; 344351; -.
DR   ArrayExpress; Q5Y5T1; -.
DR   Bgee; Q5Y5T1; -.
DR   CleanEx; MM_ZDHHC20; -.
DR   Genevestigator; Q5Y5T1; -.
DR   GermOnline; ENSMUSG00000021969; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008415; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001594; Znf_DHHC_palmitoyltrfase.
DR   Pfam; PF01529; zf-DHHC; 1.
DR   PROSITE; PS50216; ZF_DHHC; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Alternative splicing; Membrane; Metal-binding;
KW   Phosphoprotein; Transferase; Transmembrane; Transmembrane helix; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    380       Probable palmitoyltransferase ZDHHC20.
FT                                /FTId=PRO_0000212907.
FT   TRANSMEM     13     33       Helical; (Potential).
FT   TRANSMEM     54     74       Helical; (Potential).
FT   TRANSMEM    170    190       Helical; (Potential).
FT   TRANSMEM    223    243       Helical; (Potential).
FT   ZN_FING     126    176       DHHC-type.
FT   MOD_RES     354    354       Phosphoserine (By similarity).
FT   VAR_SEQ     199    210       Missing (in isoform 2).
FT                                /FTId=VSP_016278.
FT   CONFLICT    130    130       K -> R (in Ref. 2; BAE41590).
FT   CONFLICT    243    243       F -> Y (in Ref. 2; BAB30620).
FT   CONFLICT    370    370       T -> I (in Ref. 2; BAE41590).
SQ   SEQUENCE   380 AA;  43976 MW;  3ECD9E424185BF01 CRC64;
     MAPWTLWRCC QRVVGWVPVL FITFVVVWSY YAYVVELCVS TISRTGEKGK TVVYLVAFHL
     FFVMFVWSYW MTIFTSPASP SKEFYLSNSE KERYEKEFSQ ERQQDILRRA ARDLPIYTTS
     ASKAIRYCEK CQLIKPDRAH HCSACDRCVL KMDHHCPWVN NCVGFTNYKF FMLFLLYSLL
     YCLFVAATVL EYFIKFWTLC RRKSTENCPK NEPTVLNFPS AKFHVLFLFF VSAMFFVSVL
     SLFSYHCWLV GKNRTTIESF RAPMFSYGID GNGFSLGCSK NWRQVFGDEK KYWLVPIFSS
     LGDGCSFPAR LVGMDPEQAS VANQSDYVRS IGSNQPFPIK PLSESKNRLL DSESQWLENG
     AEEGVTKSGT NNHVTVEIEN
//
ID   ZDH18_MOUSE             Reviewed;         380 AA.
AC   Q5Y5T2; A2A9F0;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 4.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Palmitoyltransferase ZDHHC18;
DE            EC=2.3.1.-;
DE   AltName: Full=Zinc finger DHHC domain-containing protein 18;
DE            Short=DHHC-18;
GN   Name=Zdhhc18;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 90-380.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 103-227.
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 128-380, FUNCTION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15603741; DOI=10.1016/j.neuron.2004.12.005;
RA   Fukata M., Fukata Y., Adesnik H., Nicoll R.A., Bredt D.S.;
RT   "Identification of PSD-95 palmitoylating enzymes.";
RL   Neuron 44:987-996(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Has palmitoyltransferase activity towards HRAS and LCK.
CC   -!- CATALYTIC ACTIVITY: Palmitoyl-CoA + protein-cysteine = S-palmitoyl
CC       protein + CoA.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase
CC       activity (By similarity).
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       ERF2/ZDHHC9 subfamily.
CC   -!- SIMILARITY: Contains 1 DHHC-type zinc finger.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AL627228; CAM14825.1; -; Genomic_DNA.
DR   EMBL; BX537327; CAM14825.1; JOINED; Genomic_DNA.
DR   EMBL; BX537327; CAM25149.1; -; Genomic_DNA.
DR   EMBL; AL627228; CAM25149.1; JOINED; Genomic_DNA.
DR   EMBL; BF582271; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; CJ065144; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AY668950; AAU89704.1; -; mRNA.
DR   IPI; IPI00275216; -.
DR   RefSeq; NP_001017968.2; NM_001017968.2.
DR   UniGene; Mm.331948; -.
DR   STRING; Q5Y5T2; -.
DR   PhosphoSite; Q5Y5T2; -.
DR   PRIDE; Q5Y5T2; -.
DR   Ensembl; ENSMUST00000084238; ENSMUSP00000081260; ENSMUSG00000037553.
DR   GeneID; 503610; -.
DR   KEGG; mmu:503610; -.
DR   UCSC; uc008vde.1; mouse.
DR   CTD; 503610; -.
DR   MGI; MGI:3527792; Zdhhc18.
DR   eggNOG; roNOG16564; -.
DR   GeneTree; ENSGT00550000074293; -.
DR   HOGENOM; HBG744542; -.
DR   HOVERGEN; HBG056239; -.
DR   InParanoid; Q5Y5T2; -.
DR   OMA; QQIDPRA; -.
DR   OrthoDB; EOG4G7BZ7; -.
DR   PhylomeDB; Q5Y5T2; -.
DR   NextBio; 411848; -.
DR   ArrayExpress; Q5Y5T2; -.
DR   Bgee; Q5Y5T2; -.
DR   CleanEx; MM_ZDHHC18; -.
DR   Genevestigator; Q5Y5T2; -.
DR   GermOnline; ENSMUSG00000037553; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016409; F:palmitoyltransferase activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0034613; P:cellular protein localization; IDA:MGI.
DR   InterPro; IPR001594; Znf_DHHC_palmitoyltrfase.
DR   Pfam; PF01529; zf-DHHC; 1.
DR   PROSITE; PS50216; ZF_DHHC; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Membrane; Metal-binding; Phosphoprotein; Transferase;
KW   Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT   CHAIN         1    380       Palmitoyltransferase ZDHHC18.
FT                                /FTId=PRO_0000212903.
FT   TRANSMEM     83    103       Helical; (Potential).
FT   TRANSMEM    112    132       Helical; (Potential).
FT   TRANSMEM    228    248       Helical; (Potential).
FT   TRANSMEM    270    290       Helical; (Potential).
FT   ZN_FING     184    234       DHHC-type.
FT   COMPBIAS     11     42       Pro-rich.
FT   ACT_SITE    214    214       S-palmitoyl cysteine intermediate (By
FT                                similarity).
FT   MOD_RES      19     19       Phosphoserine.
SQ   SEQUENCE   380 AA;  41148 MW;  91311320F4AE505C CRC64;
     MKDCEYQQIS PGAAPPPASP GARRPGPAAP PAPSPGPAPG APRWSGSGSG SGSLGRRPRR
     KWEVFPGRNR FYCGGRLMLA GHGGVFALTL LLILSTTILF FVFDCPYLAR TLTLAIPIIA
     AILFFFVMSC LLQTSFTDPG ILPRATICEA AALEKQIDNT GSSTYRPPPR TREVMINGQT
     VKLKYCFTCK MFRPPRTSHC SVCDNCVERF DHHCPWVGNC VGRRNYRFFY AFILSLSFLT
     AFIFACVVTH LTLLSQGSNF LSALKKTPAS VLELVICFFS IWSILGLSGF HTYLVASNLT
     TNEDIKGSWS SKRGGEASVN PYSHKSIITN CCAVLCGPLP PSLIDRRGFV QSDTALPSPI
     RSDDPACGAK PDASMVGGHP
//
ID   ZDHC8_MOUSE             Reviewed;         762 AA.
AC   Q5Y5T5; Q7TNF7;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Probable palmitoyltransferase ZDHHC8;
DE            EC=2.3.1.-;
DE   AltName: Full=Zinc finger DHHC domain-containing protein 8;
DE            Short=DHHC-8;
GN   Name=Zdhhc8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15603741; DOI=10.1016/j.neuron.2004.12.005;
RA   Fukata M., Fukata Y., Adesnik H., Nicoll R.A., Bredt D.S.;
RT   "Identification of PSD-95 palmitoylating enzymes.";
RL   Neuron 44:987-996(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 527-762.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=15184899; DOI=10.1038/ng1375;
RA   Mukai J., Liu H., Burt R.A., Swor D.E., Lai W.-S., Karayiorgou M.,
RA   Gogos J.A.;
RT   "Evidence that the gene encoding ZDHHC8 contributes to the risk of
RT   schizophrenia.";
RL   Nat. Genet. 36:725-731(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-672, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
CC   -!- FUNCTION: Palmitoyltransferase involved in glutamatergic
CC       transmission. Mediates palmitoylation of ABCA1.
CC   -!- CATALYTIC ACTIVITY: Palmitoyl-CoA + protein-cysteine = S-palmitoyl
CC       protein + CoA.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in brain cortex and hippocampus.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase
CC       activity (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice have normal brain morphology, but
CC       female have strong locomotor deficits in open field, due to a
CC       greater fear of new environments.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       ERF2/ZDHHC9 subfamily.
CC   -!- SIMILARITY: Contains 1 DHHC-type zinc finger.
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DR   EMBL; AY668947; AAU89701.1; -; mRNA.
DR   EMBL; BC055694; AAH55694.1; -; mRNA.
DR   IPI; IPI00377908; -.
DR   RefSeq; NP_742163.4; NM_172151.4.
DR   UniGene; Mm.326263; -.
DR   ProteinModelPortal; Q5Y5T5; -.
DR   STRING; Q5Y5T5; -.
DR   PhosphoSite; Q5Y5T5; -.
DR   PRIDE; Q5Y5T5; -.
DR   Ensembl; ENSMUST00000076957; ENSMUSP00000076224; ENSMUSG00000060166.
DR   GeneID; 27801; -.
DR   KEGG; mmu:27801; -.
DR   UCSC; uc007ymx.1; mouse.
DR   CTD; 27801; -.
DR   MGI; MGI:1338012; Zdhhc8.
DR   HOGENOM; HBG443552; -.
DR   HOVERGEN; HBG057186; -.
DR   InParanoid; Q5Y5T5; -.
DR   OMA; AHTTITM; -.
DR   OrthoDB; EOG466VKB; -.
DR   PhylomeDB; Q5Y5T5; -.
DR   NextBio; 306146; -.
DR   ArrayExpress; Q5Y5T5; -.
DR   Bgee; Q5Y5T5; -.
DR   CleanEx; MM_ZDHHC8; -.
DR   Genevestigator; Q5Y5T5; -.
DR   GermOnline; ENSMUSG00000060166; Mus musculus.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008415; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007610; P:behavior; IMP:MGI.
DR   InterPro; IPR001594; Znf_DHHC_palmitoyltrfase.
DR   Pfam; PF01529; zf-DHHC; 1.
DR   PROSITE; PS50216; ZF_DHHC; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Cytoplasmic vesicle; Membrane; Metal-binding;
KW   Phosphoprotein; Transferase; Transmembrane; Transmembrane helix; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    762       Probable palmitoyltransferase ZDHHC8.
FT                                /FTId=PRO_0000212878.
FT   TOPO_DOM      1     13       Cytoplasmic (Potential).
FT   TRANSMEM     14     34       Helical; (Potential).
FT   TOPO_DOM     35     52       Lumenal (Potential).
FT   TRANSMEM     53     73       Helical; (Potential).
FT   TOPO_DOM     74    148       Cytoplasmic (Potential).
FT   TRANSMEM    149    169       Helical; (Potential).
FT   TOPO_DOM    170    190       Lumenal (Potential).
FT   TRANSMEM    191    211       Helical; (Potential).
FT   TOPO_DOM    212    762       Cytoplasmic (Potential).
FT   ZN_FING     104    154       DHHC-type.
FT   ACT_SITE    134    134       S-palmitoyl cysteine intermediate (By
FT                                similarity).
FT   MOD_RES     335    335       Phosphoserine.
FT   MOD_RES     672    672       Phosphoserine.
FT   MOD_RES     740    740       Phosphoserine (By similarity).
SQ   SEQUENCE   762 AA;  82031 MW;  28FC98CACA74B2E8 CRC64;
     MPRSPGTRLK PAKYIPVATA AALLVGSSTL FFVFTCPWLT RAVSPAIPVY NGILFLFVLA
     NFSMATFMDP GVFPRADEDE DKEDDFRAPL YKNVDVRGIQ VRMKWCATCH FYRPPRCSHC
     SVCDNCVEDF DHHCPWVNNC IGRRNYRYFF LFLLSLSAHM VGVVAFGLLY VLNHSEGLGA
     AHTTITMAVM CVAGLFFIPV IGLTGFHVVL VTRGRTTNEQ VTGKFRGGVN PFTRGCYGNV
     EHVLCSPLAP RYVVEPPRMP LSVSLKPPFL RPELLERAVP LKVKLSDNGL KAGRSKSKGS
     LDQLDEKPLD LGPPLPPKIE AGTFGRDLKT PRPGSAESAL SVQRTSPPTP AMYKFRPAFS
     TGPKTPFCGP NEQVPGPDSL TLADDSTHSL DFVSEPSLDL PDHGPGGLRP PYPPSPPLNT
     TDAFSGALRS LSLKAASRRG GDHMTLQPLR SEGGPPTPHR SLFAPHALPN RNGSLSYDSL
     LNPGSPSGHA CPTHPSVGIA SYHSPYLHPG PSDPPRPPPR SFSPVLGPRP REPSPVRYDN
     LSRTIMASIQ ERKDREERER LLRSQTDSLF GDSGVYDTPS SYSLQQASVL TEGPRGSVLR
     YGSRDDLVAG PGFGGARNPA LQTSLSSLSS SMSRAPRTSS SSLQADQANN NAPGPRPGSG
     SHRSPARQGL PSPPGTPRSP SYTGSKAVAF IHTDLPDRQP SLAMQRDHPQ LKTPPSKLNG
     QSPGMARLGP AASPMGPNAS PARHTLVKKV SGVGGTTYEI SV
//
ID   KIF1B_MOUSE             Reviewed;        1816 AA.
AC   Q60575; Q9R0B4; Q9WVE5; Q9Z119;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 2.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Kinesin-like protein KIF1B;
GN   Name=Kif1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=95094296; PubMed=7528108; DOI=10.1016/0092-8674(94)90012-4;
RA   Nangaku M., Sato-Yoshitake R., Okada Y., Noda Y., Takemura R.,
RA   Yamazaki H., Hirokawa N.;
RT   "KIF1B, a novel microtubule plus end-directed monomeric motor protein
RT   for transport of mitochondria.";
RL   Cell 79:1209-1220(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=20035818; PubMed=10571041; DOI=10.1016/S0378-1119(99)00370-4;
RA   Gong T.L., Winnicki R.S., Kohrman D.C., Lomax M.I.;
RT   "A novel kinesin of the UNC-104/KIF1 subfamily encoded by the Kif1b
RT   gene.";
RL   Gene 239:117-127(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   MEDLINE=99272823; PubMed=10341097; DOI=10.1007/s003359901056;
RA   Conforti L., Buckmaster E.A., Tarlton A., Brown M.C., Lyon M.F.,
RA   Perry V.H., Coleman M.P.;
RT   "The major brain isoform of kif1b lacks the putative mitochondria-
RT   binding domain.";
RL   Mamm. Genome 10:617-622(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=ICR;
RA   Nakagawa T., Hirokawa N.;
RT   "Identification and characterization of a new kinesin superfamily
RT   KIF1B-beta.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1454, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1487, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Motor for anterograde transport of mitochondria. Has a
CC       microtubule plus end-directed motility.
CC   -!- SUBUNIT: Monomer. Interacts with KBP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle. Cytoplasm,
CC       cytoskeleton. Mitochondrion (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q60575-1; Sequence=Displayed;
CC       Name=2; Synonyms=Beta;
CC         IsoId=Q60575-2; Sequence=VSP_002862, VSP_002863;
CC       Name=3;
CC         IsoId=Q60575-3; Sequence=VSP_002862, VSP_002863, VSP_002864,
CC                                  VSP_002865;
CC   -!- TISSUE SPECIFICITY: Expressed almost exclusively in adult brain
CC       tissue (mainly in the cerebellum and cerebrum) within a single
CC       type of neuronal cell.
CC   -!- SIMILARITY: Belongs to the kinesin-like protein family. Unc-104
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 FHA domain.
CC   -!- SIMILARITY: Contains 1 kinesin-motor domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D17577; BAA04503.1; -; mRNA.
DR   EMBL; AF090190; AAF06718.1; -; mRNA.
DR   EMBL; AF131865; AAD39438.1; -; mRNA.
DR   EMBL; AB023656; BAA75243.1; -; mRNA.
DR   IPI; IPI00130390; -.
DR   IPI; IPI00407144; -.
DR   IPI; IPI00411082; -.
DR   PIR; A55289; A55289.
DR   RefSeq; NP_032467.2; NM_008441.2.
DR   UniGene; Mm.402393; -.
DR   UniGene; Mm.474289; -.
DR   ProteinModelPortal; Q60575; -.
DR   SMR; Q60575; 4-353, 531-647, 1700-1799.
DR   STRING; Q60575; -.
DR   PhosphoSite; Q60575; -.
DR   PRIDE; Q60575; -.
DR   Ensembl; ENSMUST00000030806; ENSMUSP00000030806; ENSMUSG00000063077.
DR   Ensembl; ENSMUST00000055647; ENSMUSP00000061472; ENSMUSG00000063077.
DR   Ensembl; ENSMUST00000060537; ENSMUSP00000056754; ENSMUSG00000063077.
DR   GeneID; 16561; -.
DR   KEGG; mmu:16561; -.
DR   UCSC; uc008vvy.1; mouse.
DR   UCSC; uc008vvz.1; mouse.
DR   UCSC; uc008vwa.1; mouse.
DR   CTD; 16561; -.
DR   MGI; MGI:108426; Kif1b.
DR   HOGENOM; HBG381254; -.
DR   HOVERGEN; HBG052251; -.
DR   InParanoid; Q60575; -.
DR   OMA; SEVITPP; -.
DR   OrthoDB; EOG447FSB; -.
DR   ArrayExpress; Q60575; -.
DR   Bgee; Q60575; -.
DR   CleanEx; MM_KIF1B; -.
DR   Genevestigator; Q60575; -.
DR   GermOnline; ENSMUSG00000063077; Mus musculus.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005875; C:microtubule associated complex; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; TAS:UniProtKB.
DR   GO; GO:0003777; F:microtubule motor activity; IDA:UniProtKB.
DR   GO; GO:0008089; P:anterograde axon cargo transport; IMP:UniProtKB.
DR   GO; GO:0009790; P:embryo development; NAS:UniProtKB.
DR   GO; GO:0047497; P:mitochondrion transport along microtubule; IDA:MGI.
DR   GO; GO:0007270; P:nerve-nerve synaptic transmission; IMP:UniProtKB.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:UniProtKB.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR022140; KIF1B.
DR   InterPro; IPR022164; Kinesin-like.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR008984; SMAD_FHA_domain.
DR   Gene3D; G3DSA:2.60.200.20; FHA; 1.
DR   Gene3D; G3DSA:3.40.850.10; kinesin_motor; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF12473; DUF3694; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF12423; KIF1B; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00240; FHA; 1.
DR   SMART; SM00129; KISc; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF49879; SMAD_FHA; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_DOMAIN1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_DOMAIN2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Coiled coil; Cytoplasm;
KW   Cytoplasmic vesicle; Cytoskeleton; Microtubule; Mitochondrion;
KW   Motor protein; Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1   1816       Kinesin-like protein KIF1B.
FT                                /FTId=PRO_0000125408.
FT   DOMAIN        1    361       Kinesin-motor.
FT   DOMAIN      556    612       FHA.
FT   DOMAIN     1702   1799       PH.
FT   NP_BIND      97    104       ATP (By similarity).
FT   REGION      270    350       Interaction with KBP (By similarity).
FT   COILED      365    386       Potential.
FT   COILED      470    502       Potential.
FT   COILED      668    737       Potential.
FT   COILED      841    869       Potential.
FT   MOD_RES    1057   1057       Phosphoserine (By similarity).
FT   MOD_RES    1454   1454       Phosphoserine.
FT   MOD_RES    1487   1487       Phosphoserine.
FT   VAR_SEQ     289    294       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_002862.
FT   VAR_SEQ     394    434       IDPLIDDYSGSGGKYLKDFQNNKHRYLLASENQRPGNFSTA
FT                                -> T (in isoform 2 and isoform 3).
FT                                /FTId=VSP_002863.
FT   VAR_SEQ     707   1196       YESKLQALQRQVETRSLAAETTEEEEEEEEVPWTQHEFELA
FT                                QWAFRKWKSHQFTSLRDLLWGNAVYLKEANAISVELKKKVQ
FT                                FQFVLLTDTLYSPVPPELLPSEMEKTHEDRPFPRTVVAVEV
FT                                QDLKNGATHYWSLDKLKQRLDLMREMYDRAGEVASSAQDDS
FT                                ETTMTGSDPFYDRFHWFKLVGSSPIFHGCVNERLADRTPSP
FT                                TFSTADSDITELADEQQDAMEDFDDEAFVDDTGSDAGTEEG
FT                                SELFSDGHDPFYDRSPWFILVGRAFVYLSNLLYPVPLIHRV
FT                                AIVSEKGEVRGFLRVAVQAIAADEEAPDYGSGIRQSGTAKI
FT                                SFDNEYFNQSDFSSAAMTRSGLSLEELRIVEGQGQSSEVIS
FT                                PPEEVNRMNDLDLKSGTLLDGKMVMEGFSEEIGNHLKLGSA
FT                                FTFRVTVLQASGILPEYADIFCQFNFLHRHDEAFSTEPLKN
FT                                NGRGSPLGFYHVQNIAVEVTESFVDYIKTKPIVFEVFGH
FT                                -> ADSDSGDDSDKRSCEESWKLITSLREKLPPSKLQTIVK
FT                                KCGLPSSGKKREPIKMYQIPQRRRLSKDSKWVTISDLKIQA
FT                                VKEICYEVALNDFRHSRQEIEALAIVKMKELCAMYGKKDPN
FT                                ERDSWRAVARDVWDTVGVGDEKIEDMMVTGKGGTDVDDLKV
FT                                HIDKLEDILQEVKKQNNMKDEEIKVLRNKMLKMEKVLPLIG
FT                                SQEQKSQGSHKTKEPLVAGANSVSDNGVSKGESGELGKEER
FT                                VSQLMNGDPAFRRGRLRWMRQEQIRFKNLQQQEITKQLRRQ
FT                                NVPHRFIPPENRKPRFPFKSNPKHRNSWSPGTHIIITEDEV
FT                                IELRIPKDEEGRKENKEESQEKVGRAASRDVQSAWGTRSQD
FT                                HIQVSKQHISNQQPPPQLRWRSNSLNNGQPKTTRCQATASS
FT                                ESLNSHSGHPTADLQTFQAKRHIHQHRQPYCNYNTGGQVEG
FT                                STASCCQKQTDKPSHCNQFVTPPRMRRQFSAPNLKAGRETT
FT                                V (in isoform 3).
FT                                /FTId=VSP_002864.
FT   VAR_SEQ    1197   1816       Missing (in isoform 3).
FT                                /FTId=VSP_002865.
FT   CONFLICT    117    117       G -> V (in Ref. 1 and 2).
FT   CONFLICT    520    523       GGTL -> RGDI (in Ref. 1; BAA04503).
FT   CONFLICT    909    909       P -> S (in Ref. 4; BAA75243).
FT   CONFLICT   1608   1609       KL -> TW (in Ref. 3; AAD39438).
FT   CONFLICT   1612   1612       I -> V (in Ref. 3; AAD39438).
FT   CONFLICT   1784   1784       D -> G (in Ref. 4; BAA75243).
SQ   SEQUENCE   1816 AA;  204081 MW;  E316EC295138E5DE CRC64;
     MSGASVKVAV RVRPFNSRET SKESKCIIQM QGNSTSIINP KNPKEAPKSF SFDYSYWSHT
     SPEDPCFASQ NRVYNDIGKE MLLHAFEGYN VCIFAYGQTG AGKSYTMMGK QEESQAGIIP
     QLCEELFEKI NDNCNEEMSY SVEVSYMEIY CERVRDLLNP KNKGNLRVRE HPLLGPYVED
     LSKLAVTSYT DIADLMDAGN KARTVAATNM NETSSRSHAV FTIVFTQKKQ DPETNLSTEK
     VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEVDN CTSKSKKKKK
     TDFIPYRDSV LTWLLRENLG GNSRTAMVAA LSPADINYDE TLSTLRYADR AKQIKCNAVI
     NEDPNAKLVR ELKEEVTRLK DLLRAQGLGD IIDIDPLIDD YSGSGGKYLK DFQNNKHRYL
     LASENQRPGN FSTASMGSLT SSPSSCSLNS QVGLTSVTSI QERIMSTPGG EEAIERLKES
     EKIIAELNET WEEKLRKTEA IRMEREALLA EMGVAIREDG GTLGVFSPKK TPHLVNLNED
     PLMSECLLYY IKDGITRVGQ ADAERRQDIV LSGAHIKEEH CLFRSERSNT GEVIVTLEPC
     ERSETYVNGK RVAHPVQLRS GNRIIMGKNH VFRFNHPEQA RAEREKTPSA ETPSEPVDWT
     FAQRELLEKQ GIDMKQEMEK RLQEMEILYK KEKEEADLLL EQQRLDYESK LQALQRQVET
     RSLAAETTEE EEEEEEVPWT QHEFELAQWA FRKWKSHQFT SLRDLLWGNA VYLKEANAIS
     VELKKKVQFQ FVLLTDTLYS PVPPELLPSE MEKTHEDRPF PRTVVAVEVQ DLKNGATHYW
     SLDKLKQRLD LMREMYDRAG EVASSAQDDS ETTMTGSDPF YDRFHWFKLV GSSPIFHGCV
     NERLADRTPS PTFSTADSDI TELADEQQDA MEDFDDEAFV DDTGSDAGTE EGSELFSDGH
     DPFYDRSPWF ILVGRAFVYL SNLLYPVPLI HRVAIVSEKG EVRGFLRVAV QAIAADEEAP
     DYGSGIRQSG TAKISFDNEY FNQSDFSSAA MTRSGLSLEE LRIVEGQGQS SEVISPPEEV
     NRMNDLDLKS GTLLDGKMVM EGFSEEIGNH LKLGSAFTFR VTVLQASGIL PEYADIFCQF
     NFLHRHDEAF STEPLKNNGR GSPLGFYHVQ NIAVEVTESF VDYIKTKPIV FEVFGHYQQH
     PLHLQGQDLN SPPQPSRRFF PPPMPLSKPV PATKLNTMNK TTLGQSMSKY DLLVWFEISE
     LEPTGEYIPA VVDHTAGLPC QGTFLLHQGI QRRITVTIIH EKGSELHWKD VRELVVGRIR
     NKPEVDEAAV DAVLSLNIIS AKSLKAAHSS SRTFYRFEAV WDSSLHNSLL LNRVTPYGEK
     IYMTLSAYLE LDHCIQPAVI TKDVCMVFYS RDAKISPPRS LRNLFGSGYS KSPDSNRVTG
     IYELSLCKMA DTGSPGMQRR RRKVLDTSVA YVRGEENLAG WRPRGDSLIL EHQWELEKLE
     LLHEVEKTRH FLLLRERLGD SVPKSLSDSL SPSLSSGTLS TSTSISSQIS TTTFESAITP
     SESSGYDSAD VESLVDREKE LATKCLQLLT HTFNREFSQV HGSISDCKLS DISPIGRDPS
     VSSFSSSTLT PSSTCPSLVD SRSSSMDQKT PEANSRASSP CQEFEQFQIV PTVETPYLAR
     AGKNEFLNLV PDIEEVRAGS VVSKKGYLHF KEPLSSNWAK HFVVVRRPYV FIYNSDKDPV
     ERGIINLSTA QVEYSEDQQA MVKTPNTFAV CTKHRGVLLQ ALNDKDMNDW LYAFNPLLAG
     TIRSKLSRRC PSQPKY
//
ID   MAST2_MOUSE             Reviewed;        1734 AA.
AC   Q60592; Q6P9M1; Q8CHD1;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Microtubule-associated serine/threonine-protein kinase 2;
DE            EC=2.7.11.1;
GN   Name=Mast2; Synonyms=Mast205;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=Swiss Webster; TISSUE=Testis;
RX   MEDLINE=94067123; PubMed=8246979;
RA   Walden P.D., Cowan N.J.;
RT   "A novel 205-kDa testis-specific serine/threonine protein kinase
RT   associated with microtubules of the spermatid manchette.";
RL   Mol. Cell. Biol. 13:7625-7635(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 302-1734.
RC   TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=8902215;
RA   Walden P.D., Millette C.F.;
RT   "Increased activity associated with the MAST205 protein kinase complex
RT   during mammalian spermiogenesis.";
RL   Biol. Reprod. 55:1039-1044(1996).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION
RP   WITH SNTB2.
RX   MEDLINE=99338326; PubMed=10404183; DOI=10.1038/10165;
RA   Lumeng C., Phelps S., Crawford G.E., Walden P.D., Barald K.,
RA   Chamberlain J.S.;
RT   "Interactions between beta 2-syntrophin and a family of microtubule-
RT   associated serine/threonine kinases.";
RL   Nat. Neurosci. 2:611-617(1999).
RN   [6]
RP   FUNCTION, UBIQUITINATION, AND MUTAGENESIS OF 482-LYS-LYS-483.
RX   PubMed=14764729;
RA   Zhou H., Xiong H., Li H., Plevy S.E., Walden P.D., Sassaroli M.,
RA   Prestwich G.D., Unkeless J.C.;
RT   "Microtubule-associated serine/threonine kinase-205 kDa and Fc gamma
RT   receptor control IL-12 p40 synthesis and NF-kappa B activation.";
RL   J. Immunol. 172:2559-2568(2004).
RN   [7]
RP   FUNCTION, UBIQUITINATION, PHOSPHORYLATION, AND INTERACTION WITH TRAF6.
RX   PubMed=15308666; DOI=10.1074/jbc.M404328200;
RA   Xiong H., Li H., Chen Y., Zhao J., Unkeless J.C.;
RT   "Interaction of TRAF6 with MAST205 regulates NF-kappaB activation and
RT   MAST205 stability.";
RL   J. Biol. Chem. 279:43675-43683(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-42 AND SER-1462,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Appears to link the dystrophin/utrophin network with
CC       microtubule filaments via the syntrophins. Phosphorylation of DMD
CC       or UTRN may modulate their affinities for associated proteins.
CC       Functions in a multi-protein complex in spermatid maturation.
CC       Regulates lipopolysaccharide-induced IL-12 synthesis in
CC       macrophages by forming a complex with TRAF6, resulting in the
CC       inhibition of TRAF6 NF-kappa-B activation.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium.
CC   -!- SUBUNIT: Interacts with CDHR2 (By similarity).
CC   -!- INTERACTION:
CC       P60484:PTEN (xeno); NbExp=2; IntAct=EBI-493888, EBI-696162;
CC       P0CG47:RPS27A (xeno); NbExp=2; IntAct=EBI-493888, EBI-413034;
CC       Q61235:Sntb2; NbExp=3; IntAct=EBI-493888, EBI-295974;
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Cytoplasm, cytoskeleton. Cell junction.
CC       Note=Colocalizes with beta 2-syntrophin and utrophin at
CC       neuromuscular junctions.
CC   -!- TISSUE SPECIFICITY: Detected in round spermatids and residual
CC       bodies but not epididymal spermatozoa (at protein level).
CC       Expressed in adult but not fetal testis with levels increasing in
CC       parallel with testicular development. Also expressed at high
CC       levels in heart, lower levels in all other tissues tested.
CC   -!- PTM: Phosphorylated and ubiquitinated. N-terminal ubiquitination
CC       leads to degradation of MAST2 by proteasome-mediated proteolysis.
CC       N-terminal phosphorylation appears to be a prerequisite for
CC       ubiquitination.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; U02313; AAC04312.1; -; mRNA.
DR   EMBL; BC060703; AAH60703.1; -; mRNA.
DR   EMBL; AB093264; BAC41448.1; -; mRNA.
DR   IPI; IPI00622008; -.
DR   PIR; A54602; A54602.
DR   RefSeq; NP_001036208.1; NM_001042743.1.
DR   RefSeq; NP_032667.2; NM_008641.2.
DR   UniGene; Mm.9287; -.
DR   ProteinModelPortal; Q60592; -.
DR   SMR; Q60592; 263-755, 1040-1136.
DR   IntAct; Q60592; 12.
DR   MINT; MINT-152278; -.
DR   STRING; Q60592; -.
DR   PhosphoSite; Q60592; -.
DR   PRIDE; Q60592; -.
DR   Ensembl; ENSMUST00000003908; ENSMUSP00000003908; ENSMUSG00000003810.
DR   Ensembl; ENSMUST00000106485; ENSMUSP00000102094; ENSMUSG00000003810.
DR   GeneID; 17776; -.
DR   KEGG; mmu:17776; -.
DR   UCSC; uc008ugn.1; mouse.
DR   CTD; 17776; -.
DR   MGI; MGI:894676; Mast2.
DR   eggNOG; roNOG08915; -.
DR   HOVERGEN; HBG052414; -.
DR   OrthoDB; EOG44F68B; -.
DR   PhylomeDB; Q60592; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 292503; -.
DR   ArrayExpress; Q60592; -.
DR   Bgee; Q60592; -.
DR   CleanEx; MM_MAST2; -.
DR   Genevestigator; Q60592; -.
DR   GermOnline; ENSMUSG00000003810; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0045075; P:regulation of interleukin-12 biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0048515; P:spermatid differentiation; IDA:UniProtKB.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR015022; MA_Ser/thr_Kinase_dom.
DR   InterPro; IPR023142; MAST_pre-PK_dom.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF08926; DUF1908; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell junction; Cytoplasm; Cytoskeleton; Kinase;
KW   Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase;
KW   Ubl conjugation.
FT   CHAIN         1   1734       Microtubule-associated serine/threonine-
FT                                protein kinase 2.
FT                                /FTId=PRO_0000086313.
FT   DOMAIN      453    726       Protein kinase.
FT   DOMAIN      727    795       AGC-kinase C-terminal.
FT   DOMAIN     1042   1130       PDZ.
FT   NP_BIND     459    467       ATP (By similarity).
FT   ACT_SITE    576    576       Proton acceptor (By similarity).
FT   BINDING     482    482       ATP (By similarity).
FT   MOD_RES      14     14       Phosphoserine.
FT   MOD_RES      42     42       Phosphoserine.
FT   MOD_RES      88     88       Phosphoserine (By similarity).
FT   MOD_RES      91     91       Phosphoserine.
FT   MOD_RES     841    841       Phosphoserine (By similarity).
FT   MOD_RES    1441   1441       Phosphoserine (By similarity).
FT   MOD_RES    1446   1446       Phosphothreonine (By similarity).
FT   MOD_RES    1462   1462       Phosphoserine.
FT   MUTAGEN     482    483       KK->RA: Abolishes LPS-stimulated IL12B
FT                                synthesis.
FT   CONFLICT    162    162       R -> RSHGHRTD (in Ref. 2; AAH60703).
FT   CONFLICT    232    232       R -> A (in Ref. 2; AAH60703).
FT   CONFLICT    275    278       PSLT -> LAD (in Ref. 2; AAH60703).
FT   CONFLICT    478    478       R -> C (in Ref. 3).
FT   CONFLICT   1228   1228       Missing (in Ref. 2 and 3).
FT   CONFLICT   1502   1502       T -> S (in Ref. 3).
FT   CONFLICT   1521   1521       V -> L (in Ref. 2 and 3).
SQ   SEQUENCE   1734 AA;  190534 MW;  97292FACD85F12E3 CRC64;
     MVTGLSPLLF RKLSNPDIFA PTGKVKLQRQ LSQDDCKLRR GSLASSLSGK QLLPLSSSVH
     SSVGQVTWQS TGEASNLVRM RNQSLGQSAP SLTAGLKELS LPRRGSFCRT SNRKSLIVTS
     STSPTLPRPH SPLHGHTGNS PLDSPRNFSP NAPAHFSFVP ARRTDGRRWS LASLPSSGYG
     TNTPSSTVSS SCSSQEKLHQ LPFQPTADEL HFLTKHFSTE NVPDEEGRRS PRMRPRSRSL
     SPGRSPVSFD SEIIMMNHVY KERFPKATAQ MEERPSLTFI SSNTPDSVLP LADGALSFIH
     HQVIEMARDC LDKSRSGLIT SHYFYELQEN LEKLLQDAHE RSESSDVAFV IQLVKKLMII
     IARPARLLEC LEFDPEEFYH LLEAAEGHAK EGHGIKCDIP RYIVSQLGLT RDPLEEMAQL
     SSYDSPDTPE TDDSVEGRGV SQPSQKTPSE EDFETIKLIS NGAYGAVFLV RHKSTRQRFA
     MKKINKQNLI LRNQIQQAFV ERDILTFAEN PFVVSMFCSF ETKRHLCMVM EYVEGGDCAT
     LLKNIGALPV DMVRLYFAET VLALEYLHNY GIVHRDLKPD NLLITSMGHI KLTDFGLSKI
     GLMSLTTNLY EGHIEKDARE FLDKQVCGTP EYIAPEVILR QGYGKPVDWW AMGIILYEFL
     VGCVPFFGDT PEELFGQVIS DEIVWPEGDD ALPPDAQDLT SKLLHQNPLE RLGTSSAYEV
     KQHPFFMGLD WTGLLRQKAE FIPQLESEDD TSYFDTRSER YHHVDSEDEE EVSEDGCLEI
     RQFSSCSPRF SKVYSSMERL SLLEERRTPP PTKRSLSEEK EDHSDGLAGL KGRDRSWVIG
     SPEILRKRLS VSESSHTESD SSPPMTVRHR CSGLPDGPHC PEETSSTPRK QQQEGIWVLI
     PPSGEGSSRP VPERPLERQL KLDEEPPGQS SRCCPALETR GRGTPQLAEE ATAKAISDLA
     VRRARHRLLS GDSIEKRTTR PVNKVIKSAS ATALSLLIPS EHHACSPLAS PMSPHSQSSN
     PSSRDSSPSR DFLPALGSLR PPIIIHRAGK KYGFTLRAIR VYMGDTDVYT VHHMVWHVED
     GGPASEAGLR QGDLITHVNG EPVHGLVHTE VVELVLKSGN KVSISTTPLE NTSIKVGPAR
     KGSYKAKMAR RSKRSKGKDG QESRKRSSLF RKITKQASLL HTSRSLSSLN RSLSSGESGP
     GSPTHSHSLS PRSPPQGYRV APDAVHSVGG NSSQSSSPSS SVPSSPAGSG HTRPSSLHGL
     APKLQRQYRS PRRKSAGSIP LSPLAHTPSP PATAASPQRS PSPLSGHGSQ SFPTKLHLSP
     PLGRQLSRPK SAEPPRSPLL KRVQSAEKLA AALAAAEKKL APSRKHSLDL PHGELKKELT
     PREASPLEVV GTRSVLSGKG PLPGKGVLQP APSRALGTLR QDRAERRESL QKQEAIREVD
     SSEDDTDEEP ENSQATQEPR LSPHPEASHN LLPKGSGEGT EEDTFLHRDL KKQGPVLSGL
     VTGATLGSPR VDVPGLSPRK VSRPQAFEEA TNPLQVPSLS RSGPTSPTPS EGCWKAQHLH
     TQALTALCPS FSELTPTGCS AATSTSGKPG TWSWKFLIEG PDRASTNKTI TRKGEPANSQ
     DTNTTVPNLL KNLSPEEEKP QPPSVPGLTH PLLEVPSQNW PWESECEQME KEEPSLSITE
     VPDSSGDRRQ DIPCRAHPLS PETRPSLLWK SQELGGQQDH QDLALTSDEL LKQT
//
ID   XRCC1_MOUSE             Reviewed;         631 AA.
AC   Q60596; Q3THC5; Q5U435; Q7TNQ5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 2.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=DNA repair protein XRCC1;
DE   AltName: Full=X-ray repair cross-complementing protein 1;
GN   Name=Xrcc1; Synonyms=Xrcc-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=95048367; PubMed=7959765; DOI=10.1006/geno.1994.1359;
RA   Brookman K.W., Tebbs R.S., Allen S.A., Tucker J.D., Swiger R.R.,
RA   Lamerdin J.E., Carrano A.V., Thompson L.H.;
RT   "Isolation and characterization of mouse Xrcc-1, a DNA repair gene
RT   affecting ligation.";
RL   Genomics 22:180-188(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=DBA/2;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Colon, and Egg;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-446 AND THR-452, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-452, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484 AND THR-487, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-446 AND THR-452, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Corrects defective DNA strand-break repair and sister
CC       chromatid exchange following treatment with ionizing radiation and
CC       alkylating agents.
CC   -!- SUBUNIT: Homodimer. Interacts with polynucleotide kinase (PNK),
CC       DNA polymerase-beta (POLB) and DNA ligase III (LIG3). Interacts
CC       with APTX and APLF. Interacts with APEX1; the interaction is
CC       induced by SIRT1 and increases with the acetylated form of APEX1
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- PTM: Phosphorylation of Ser-371 causes dimer dissociation.
CC       Phosphorylation by CK2 promotes interaction with APTX and APLF (By
CC       similarity).
CC   -!- PTM: Sumoylated.
CC   -!- SIMILARITY: Contains 2 BRCT domains.
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DR   EMBL; U02887; AAA93115.1; -; mRNA.
DR   EMBL; AK168334; BAE40272.1; -; mRNA.
DR   EMBL; BC055900; AAH55900.1; -; mRNA.
DR   EMBL; BC085281; AAH85281.1; -; mRNA.
DR   IPI; IPI00118139; -.
DR   PIR; A54659; A54659.
DR   RefSeq; NP_033558.3; NM_009532.4.
DR   UniGene; Mm.4347; -.
DR   ProteinModelPortal; Q60596; -.
DR   SMR; Q60596; 2-155, 301-413, 536-631.
DR   STRING; Q60596; -.
DR   PhosphoSite; Q60596; -.
DR   PRIDE; Q60596; -.
DR   Ensembl; ENSMUST00000063249; ENSMUSP00000070995; ENSMUSG00000051768.
DR   GeneID; 22594; -.
DR   KEGG; mmu:22594; -.
DR   UCSC; uc009fpx.1; mouse.
DR   CTD; 22594; -.
DR   MGI; MGI:99137; Xrcc1.
DR   GeneTree; ENSGT00390000004140; -.
DR   HOGENOM; HBG447214; -.
DR   HOVERGEN; HBG052992; -.
DR   InParanoid; Q60596; -.
DR   OMA; YAGSTDE; -.
DR   OrthoDB; EOG4C87SH; -.
DR   PhylomeDB; Q60596; -.
DR   NextBio; 302941; -.
DR   ArrayExpress; Q60596; -.
DR   Bgee; Q60596; -.
DR   Genevestigator; Q60596; -.
DR   GermOnline; ENSMUSG00000051768; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0000012; P:single strand break repair; IEA:InterPro.
DR   InterPro; IPR001357; BRCT.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR002706; Xrcc1_N.
DR   Pfam; PF00533; BRCT; 2.
DR   Pfam; PF01834; XRCC1_N; 1.
DR   SMART; SM00292; BRCT; 2.
DR   SUPFAM; SSF52113; BRCT; 2.
DR   SUPFAM; SSF49785; Gal_bind_like; 1.
DR   PROSITE; PS50172; BRCT; 2.
PE   1: Evidence at protein level;
KW   DNA damage; DNA repair; Nucleus; Phosphoprotein; Repeat;
KW   Ubl conjugation.
FT   CHAIN         1    631       DNA repair protein XRCC1.
FT                                /FTId=PRO_0000066045.
FT   DOMAIN      315    403       BRCT 1.
FT   DOMAIN      536    627       BRCT 2.
FT   MOD_RES     200    200       Phosphothreonine (By similarity).
FT   MOD_RES     201    201       Phosphoserine (By similarity).
FT   MOD_RES     213    213       Phosphotyrosine (By similarity).
FT   MOD_RES     228    228       Phosphoserine (By similarity).
FT   MOD_RES     261    261       Phosphoserine (By similarity).
FT   MOD_RES     371    371       Phosphoserine (By similarity).
FT   MOD_RES     408    408       Phosphoserine (By similarity).
FT   MOD_RES     409    409       Phosphoserine (By similarity).
FT   MOD_RES     410    410       Phosphoserine (By similarity).
FT   MOD_RES     416    416       Phosphoserine (By similarity).
FT   MOD_RES     418    418       Phosphoserine (By similarity).
FT   MOD_RES     445    445       Phosphoserine (By similarity).
FT   MOD_RES     446    446       Phosphoserine.
FT   MOD_RES     452    452       Phosphothreonine.
FT   MOD_RES     456    456       Phosphothreonine (By similarity).
FT   MOD_RES     460    460       Phosphoserine (By similarity).
FT   MOD_RES     484    484       Phosphoserine.
FT   MOD_RES     487    487       Phosphothreonine.
FT   CONFLICT     28     28       D -> G (in Ref. 3; AAH85281).
FT   CONFLICT     68     68       V -> L (in Ref. 2; BAE40272).
FT   CONFLICT    108    108       N -> S (in Ref. 3; AAH85281).
FT   CONFLICT    172    172       L -> F (in Ref. 3; AAH85281).
FT   CONFLICT    197    197       I -> V (in Ref. 3; AAH85281).
FT   CONFLICT    263    263       P -> H (in Ref. 2; BAE40272).
FT   CONFLICT    295    295       V -> I (in Ref. 1; AAA93115).
FT   CONFLICT    379    379       R -> G (in Ref. 2; BAE40272).
FT   CONFLICT    391    391       H -> R (in Ref. 1; AAA93115).
FT   CONFLICT    582    582       V -> A (in Ref. 3; AAH85281).
SQ   SEQUENCE   631 AA;  68971 MW;  1A730F206E5B8879 CRC64;
     MPEISLRHVV SCSSQDSTHC AENLLKADTY RKWRAAKAGE KTISVVLQLE KEEQIHSVDI
     GNDGSAFVEV LVGSSAGGAT AGEQDYEVLL VTSSFMSPSE SRSGSNPNRV RIFGPDKLVR
     AAAEKRWDRV KIVCSQPYSK DSPYGLSFVK FHSPPDKDEA EATSQKVTVT KLGQFRVKEE
     DDSANSLKPG ALFFSRINKT SSASTSDPAG PSYAAATLQA SSAASSASPV PKVVGSSSKP
     QEPPKGKRKL DLSLEDRKPP SKPSAGPSTL KRPKLSVPSR TPAAAPASTP AQRAVPGKPR
     GEGTEPRGAR TGPQELGKIL QGVVVVLSGF QNPFRSELRD KALELGAKYR PDWTPDSTHL
     ICAFANTPKY SQVLGLGGRI VRKEWVLDCH HMRRRLPSRR YLMAGLGSSS EDEGDSHSES
     GEDEAPKLPQ KRPQPKAKTQ AAGPSSPPRP PTPKETKAPS PGPQDNSDTE GEESEGRDNG
     AEDSGDTEDE LRRVAKQREQ RQPPAPEENG EDPYAGSTDE NTDSETPSEA DLPIPELPDF
     FEGKHFFLYG EFPGDERRRL IRYVTAFNGE LEDYMNERVQ FVITAQEWDP NFEEALMENP
     SLAFVRPRWI YSCNEKQKLL PHQLYGVVPQ A
//
ID   ODO1_MOUSE              Reviewed;        1023 AA.
AC   Q60597; Q3UDM7; Q5DTI4; Q5SVX7; Q5SVX9; Q6PFZ2; Q80Y57; Q8K0K7;
AC   Q8K2Z3; Q8R3M2; Q91WP2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 3.
DT   08-MAR-2011, entry version 105.
DE   RecName: Full=2-oxoglutarate dehydrogenase, mitochondrial;
DE            EC=1.2.4.2;
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E1;
DE            Short=OGDC-E1;
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase;
DE   Flags: Precursor;
GN   Name=Ogdh; Synonyms=Kiaa4192;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC   STRAIN=C57BL/6, and FVB/N;
RC   TISSUE=Brain, Colon, Mammary tumor, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 123-135; 185-204; 311-319; 561-568; 616-633 AND
RP   916-925, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 829-958 (ISOFORMS 1/2/3/4).
RC   STRAIN=BALB/c;
RX   MEDLINE=94068586; PubMed=8248240; DOI=10.1073/pnas.90.23.11272;
RA   Udaka K., Tsomides T.J., Walden P., Fukusen N., Eisen H.N.;
RT   "A ubiquitous protein is the source of naturally occurring peptides
RT   that are recognized by a CD8+ T-cell clone.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:11272-11276(1993).
RN   [7]
RP   PROTEIN SEQUENCE OF 933-939.
RX   MEDLINE=92298396; PubMed=1606619; DOI=10.1016/0092-8674(92)90617-L;
RA   Udaka K., Tsomides T.J., Eisen H.N.;
RT   "A naturally occurring peptide recognized by alloreactive CD8+
RT   cytotoxic T lymphocytes in association with a class I MHC protein.";
RL   Cell 69:989-998(1992).
CC   -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the
CC       overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
CC       contains multiple copies of three enzymatic components: 2-
CC       oxoglutarate dehydrogenase (E1), dihydrolipoamide
CC       succinyltransferase (E2) and lipoamide dehydrogenase (E3).
CC   -!- CATALYTIC ACTIVITY: 2-oxoglutarate + [dihydrolipoyllysine-residue
CC       succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       succinyltransferase] S-succinyldihydrolipoyllysine + CO(2).
CC   -!- COFACTOR: Thiamine pyrophosphate.
CC   -!- ENZYME REGULATION: Catabolite repressed.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q60597-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q60597-2; Sequence=VSP_024799;
CC       Name=3;
CC         IsoId=Q60597-3; Sequence=VSP_024801;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q60597-4; Sequence=VSP_024800;
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase
CC       family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH31165.1; Type=Erroneous initiation;
CC       Sequence=BAD90530.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK147289; BAE27824.1; -; mRNA.
DR   EMBL; AK150009; BAE29234.1; -; mRNA.
DR   EMBL; AK169286; BAE41044.1; -; mRNA.
DR   EMBL; AK220536; BAD90530.1; ALT_INIT; mRNA.
DR   EMBL; AL607152; CAI24404.1; -; Genomic_DNA.
DR   EMBL; AL607152; CAI24405.1; -; Genomic_DNA.
DR   EMBL; AL607152; CAI24406.1; -; Genomic_DNA.
DR   EMBL; BC025040; AAH25040.1; -; mRNA.
DR   EMBL; BC013670; AAH13670.1; -; mRNA.
DR   EMBL; BC029143; AAH29143.1; -; mRNA.
DR   EMBL; BC031165; AAH31165.1; ALT_INIT; mRNA.
DR   EMBL; BC049104; AAH49104.1; -; mRNA.
DR   EMBL; BC057354; AAH57354.1; -; mRNA.
DR   EMBL; U02971; AAC52130.1; -; mRNA.
DR   IPI; IPI00420882; -.
DR   IPI; IPI00626237; -.
DR   IPI; IPI00719841; -.
DR   IPI; IPI00845652; -.
DR   PIR; I48884; A41911.
DR   RefSeq; NP_035086.2; NM_010956.3.
DR   UniGene; Mm.276348; -.
DR   UniGene; Mm.472458; -.
DR   ProteinModelPortal; Q60597; -.
DR   STRING; Q60597; -.
DR   PhosphoSite; Q60597; -.
DR   REPRODUCTION-2DPAGE; Q60597; -.
DR   PRIDE; Q60597; -.
DR   Ensembl; ENSMUST00000003461; ENSMUSP00000003461; ENSMUSG00000020456.
DR   Ensembl; ENSMUST00000101554; ENSMUSP00000099090; ENSMUSG00000020456.
DR   Ensembl; ENSMUST00000109797; ENSMUSP00000105421; ENSMUSG00000020456.
DR   GeneID; 18293; -.
DR   KEGG; mmu:18293; -.
DR   NMPDR; fig|10090.3.peg.23245; -.
DR   CTD; 18293; -.
DR   MGI; MGI:1098267; Ogdh.
DR   eggNOG; roNOG15522; -.
DR   GeneTree; ENSGT00530000063092; -.
DR   HOVERGEN; HBG001892; -.
DR   OMA; WIRRRFE; -.
DR   OrthoDB; EOG4VQ9NH; -.
DR   PhylomeDB; Q60597; -.
DR   BRENDA; 1.2.4.2; 244.
DR   NextBio; 293740; -.
DR   ArrayExpress; Q60597; -.
DR   Bgee; Q60597; -.
DR   CleanEx; MM_OGDH; -.
DR   Genevestigator; Q60597; -.
DR   GermOnline; ENSMUSG00000020456; Mus musculus.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR   GO; GO:0034602; F:oxoglutarate dehydrogenase (NAD+) activity; IDA:MGI.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; ISS:UniProtKB.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0021695; P:cerebellar cortex development; IEP:UniProtKB.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0021766; P:hippocampus development; IEP:UniProtKB.
DR   GO; GO:0061034; P:olfactory bulb mitral cell layer development; IEP:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0021860; P:pyramidal neuron development; IEP:UniProtKB.
DR   GO; GO:0021756; P:striatum development; IEP:UniProtKB.
DR   GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; IEP:UniProtKB.
DR   GO; GO:0021794; P:thalamus development; IEP:UniProtKB.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   PANTHER; PTHR23152; 2oxoglutarate_DH_E1; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Direct protein sequencing;
KW   Glycolysis; Isopeptide bond; Mitochondrion; Oxidoreductase;
KW   Thiamine pyrophosphate; Transit peptide; Ubl conjugation.
FT   TRANSIT       1     40       Mitochondrion (By similarity).
FT   CHAIN        41   1023       2-oxoglutarate dehydrogenase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000020434.
FT   REGION      933    939       Recognized by alloreactive CD8 cytotoxic
FT                                T-lymphocytes in association with a class
FT                                I MHC protein.
FT   MOD_RES     970    970       N6-acetyllysine (By similarity).
FT   CROSSLNK    534    534       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   VAR_SEQ     139    172       IRGHHVAQLDPLGILDADLDSSVPADIISSTDKL -> VRG
FT                                HHIAKSCVNFDDAPVTVSSNV (in isoform 2).
FT                                /FTId=VSP_024799.
FT   VAR_SEQ     139    172       IRGHHVAQLDPLGILDADLDSSVPADIISSTDKL -> VRG
FT                                HHIAKLDPLGISCVNFDDAPVTVSSNVDLAVFKERLRMLTV
FT                                G (in isoform 4).
FT                                /FTId=VSP_024800.
FT   VAR_SEQ     172    172       L -> LDLAVFKERLRMLTVG (in isoform 3).
FT                                /FTId=VSP_024801.
FT   CONFLICT    416    416       G -> V (in Ref. 4; AAH49104).
FT   CONFLICT    549    549       V -> F (in Ref. 4; AAH49104).
FT   CONFLICT    552    552       Q -> E (in Ref. 4; AAH57354).
FT   CONFLICT    576    576       E -> K (in Ref. 1; BAE29234).
SQ   SEQUENCE   1023 AA;  116449 MW;  A0F3F8D36C7A76BC CRC64;
     MFHLRTCAAK LRPLTASQTV KTFSQNKPAA IRTFQQIRCY SAPVAAEPFL SGTSSNYVEE
     MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLSLS RSSLATMAHA QSLVEAQPNV
     DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL GILDADLDSS VPADIISSTD KLGFYGLHES
     DLDKVFHLPT TTFIGGQEPA LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET
     PGIMQFTNEE KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDMSSAN
     GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDMKYH LGMYHRRINR
     VTDRNITLSL VANPSHLEAA DPVVMGKTKA EQFYCGDTEG KKVMSILLHG DAAFAGQGIV
     YETFHLSDLP SYTTHGTVHV VVNNQIGFTT DPRMARSSPY PTDVARVVNA PIFHVNSDDP
     EAVMYVCKVA AEWRNTFHKD VVVDLVCYRR NGHNEMDEPM FTQPLMYKQI RKQKPVLQKY
     AELLVSQGVV NQPEYEEEIS KYDKICEEAF TRSKDEKILH IKHWLDSPWP GFFTLDGQPR
     SMTCPSTGLE EDVLFHIGKV ASSVPVENFT IHGGLSRILK TRRELVTNRT VDWALAEYMA
     FGSLLKEGIH VRLSGQDVER GTFSHRHHVL HDQNVDKRTC IPMNHLWPNQ APYTVCNSSL
     SEYGVLGFEL GFAMASPNAL VLWEAQFGDF NNMAQCIIDQ FICPGQAKWV RQNGIVLLLP
     HGMEGMGPEH SSARPERFLQ MCNDDPDVLP DLQEENFDIN QLYDCNWIVV NCSTPGNFFH
     VLRRQILLPF RKPLIVFTPK SLLRHPEART SFDEMLPGTH FQRVIPENGP AAQDPHKVKR
     LLFCTGKVYY DLTRERKARN MEEEVAITRI EQLSPFPFDL LLKEAQKYPN AELAWCQEEH
     KNQGYYDYVK PRLRTTIDRA KPVWYAGRDP AAAPATGNKK THLTELQRFL DTAFDLDAFK
     KFS
//
ID   SRC8_MOUSE              Reviewed;         546 AA.
AC   Q60598;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 103.
DE   RecName: Full=Src substrate cortactin;
GN   Name=Cttn; Synonyms=Ems1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=94268839; PubMed=7516062;
RA   Miglarese M.R., Mannion-Henderson J., Wu H., Parsons J.T.,
RA   Bender T.P.;
RT   "The protein tyrosine kinase substrate cortactin is differentially
RT   expressed in murine B lymphoid tumors.";
RL   Oncogene 9:1989-1997(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 125-138; 273-289
RP   AND 534-543.
RX   MEDLINE=94043284; PubMed=7693700;
RA   Zhan X., Hu X., Hampton B., Burgess W.H., Friesel R., Maciag T.;
RT   "Murine cortactin is phosphorylated in response to fibroblast growth
RT   factor-1 on tyrosine residues late in the G1 phase of the BALB/c 3T3
RT   cell cycle.";
RL   J. Biol. Chem. 268:24427-24431(1993).
RN   [3]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH FGD1.
RX   PubMed=12913069; DOI=10.1093/hmg/ddg209;
RA   Hou P., Estrada L., Kinley A.W., Parsons J.T., Vojtek A.B.,
RA   Gorski J.L.;
RT   "Fgd1, the Cdc42 GEF responsible for faciogenital dysplasia, directly
RT   interacts with cortactin and mAbp1 to modulate cell shape.";
RL   Hum. Mol. Genet. 12:1981-1993(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-418, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401; SER-405 AND
RP   SER-407, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-401, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May contribute to the organization of cell structure.
CC       The SH3 motif may function as a binding region to cytoskeleton.
CC       Tyrosine phosphorylation in transformed cells may contribute to
CC       cellular growth regulation and transformation.
CC   -!- SUBUNIT: Interacts with SHANK2 and SHANK3 via its SH3 domain, and
CC       with PLXDC2 and SRCIN1 (By similarity). Also interacts with FGD1.
CC   -!- INTERACTION:
CC       O43516:WIPF1 (xeno); NbExp=2; IntAct=EBI-397955, EBI-346356;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection,
CC       lamellipodium. Cell projection, ruffle. Note=Associated with
CC       membrane ruffles and lamellipodia.
CC   -!- TISSUE SPECIFICITY: Detected in most murine tissues, but not
CC       detected in B-lymphocytes or plasma cells.
CC   -!- SIMILARITY: Contains 7 cortactin repeats.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; U03184; AAA19689.1; -; mRNA.
DR   IPI; IPI00118143; -.
DR   PIR; I48899; I48899.
DR   UniGene; Mm.205601; -.
DR   PDB; 2F9X; Model; -; A=1-546.
DR   PDBsum; 2F9X; -.
DR   ProteinModelPortal; Q60598; -.
DR   SMR; Q60598; 488-546.
DR   DIP; DIP-31562N; -.
DR   IntAct; Q60598; 9.
DR   MINT; MINT-100616; -.
DR   STRING; Q60598; -.
DR   PhosphoSite; Q60598; -.
DR   PRIDE; Q60598; -.
DR   Ensembl; ENSMUST00000103079; ENSMUSP00000099368; ENSMUSG00000031078.
DR   MGI; MGI:99695; Cttn.
DR   GeneTree; ENSGT00530000062953; -.
DR   HOGENOM; HBG446303; -.
DR   HOVERGEN; HBG005994; -.
DR   InParanoid; Q60598; -.
DR   OrthoDB; EOG4RNB86; -.
DR   ArrayExpress; Q60598; -.
DR   Bgee; Q60598; -.
DR   CleanEx; MM_CTTN; -.
DR   Genevestigator; Q60598; -.
DR   GermOnline; ENSMUSG00000031078; Mus musculus.
DR   GO; GO:0005938; C:cell cortex; IDA:MGI.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR   GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   InterPro; IPR015503; Cortactin.
DR   InterPro; IPR003134; Hs1_Cortactin.
DR   InterPro; IPR000108; p67phox.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR10829:SF4; Cortactin; 1.
DR   Pfam; PF02218; HS1_rep; 7.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00499; P67PHOX.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS51090; CORTACTIN; 7.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell projection; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Phosphoprotein; Repeat; SH3 domain.
FT   CHAIN         1    546       Src substrate cortactin.
FT                                /FTId=PRO_0000072190.
FT   REPEAT       80    116       Cortactin 1.
FT   REPEAT      117    153       Cortactin 2.
FT   REPEAT      154    190       Cortactin 3.
FT   REPEAT      191    227       Cortactin 4.
FT   REPEAT      228    264       Cortactin 5.
FT   REPEAT      265    301       Cortactin 6.
FT   REPEAT      302    324       Cortactin 7; truncated.
FT   DOMAIN      488    546       SH3.
FT   MOD_RES      87     87       N6-acetyllysine (By similarity).
FT   MOD_RES     113    113       Phosphoserine (By similarity).
FT   MOD_RES     117    117       Phosphoserine (By similarity).
FT   MOD_RES     141    141       Phosphotyrosine (By similarity).
FT   MOD_RES     154    154       Phosphotyrosine (By similarity).
FT   MOD_RES     198    198       N6-acetyllysine (By similarity).
FT   MOD_RES     215    215       Phosphotyrosine (By similarity).
FT   MOD_RES     218    218       N6-acetyllysine (By similarity).
FT   MOD_RES     235    235       N6-acetyllysine (By similarity).
FT   MOD_RES     272    272       N6-acetyllysine (By similarity).
FT   MOD_RES     304    304       N6-acetyllysine (By similarity).
FT   MOD_RES     309    309       N6-acetyllysine (By similarity).
FT   MOD_RES     334    334       Phosphotyrosine (By similarity).
FT   MOD_RES     401    401       Phosphothreonine.
FT   MOD_RES     405    405       Phosphoserine.
FT   MOD_RES     407    407       Phosphoserine.
FT   MOD_RES     417    417       Phosphoserine (By similarity).
FT   MOD_RES     418    418       Phosphoserine.
FT   MOD_RES     421    421       Phosphotyrosine (By similarity).
FT   MOD_RES     442    442       Phosphotyrosine (By similarity).
FT   CONFLICT      9      9       A -> R (in Ref. 2; AA sequence).
SQ   SEQUENCE   546 AA;  61260 MW;  8F93A026AD1D6D4F CRC64;
     MWKASAGHAV SITQDDGGAD DWETDPDFVN DVSEKEQRWG AKTVQGSGHQ EHINIHKLRE
     NVFQEHQTLK EKELETGPKA SHGYGGKFGV EQDRMDRSAV GHEYQSKLSK HCSQVDSVRG
     FGGKFGVQMD RVDQSAVGFE YQGKTEKHAS QKDYSSGFGG KYGVQADRVD KSAVGFDYQG
     KTEKHESQKD YSKGFGGKYG IDKDKVDKSA VGFEYQGKTE KHESQKDYVK GFGGKFGVQT
     DRQDKCALGW DHQEKLQLHE SQKDYKTGFG GKFGVQSERQ DSSAVGFDYK ERLAKHEPQQ
     DYAKGFGGKY GVQKDRMDKN ASTFEEVVQV PSAYQKTVPI EAVTSKTSNI RANFENLAKE
     REQEDRRKAE AERAQRMAKE RQEQEEARRK LEEQARAKKQ TPPASPSPQP IEDRPPSSPI
     YEDAAPFKAE PSYRGSEPEP EYSIEAAGIP EAGSQQGLTY TSEPVYETTE APGHYQAEDD
     TYDGYESDLG ITAIALYDYQ AAGDDEISFD PDDIITNIEM IDDGWWRGVC KGRYGLFPAN
     YVELRQ
//
ID   KCNH1_MOUSE             Reviewed;         989 AA.
AC   Q60603;
DT   28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 101.
DE   RecName: Full=Potassium voltage-gated channel subfamily H member 1;
DE   AltName: Full=Ether-a-go-go potassium channel 1;
DE            Short=EAG channel 1;
DE            Short=EAG1;
DE            Short=m-eag;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv10.1;
GN   Name=Kcnh1; Synonyms=Eag;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=94211879; PubMed=8159766; DOI=10.1073/pnas.91.8.3438;
RA   Warmke J.W., Ganetzky B.;
RT   "A family of potassium channel genes related to eag in Drosophila and
RT   mammals.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:3438-3442(1994).
CC   -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated non-
CC       inactivating delayed rectifier potassium channel. Channel
CC       properties may be modulated by cAMP and subunit assembly. Mediates
CC       IK(NI) current in myoblasts (By similarity).
CC   -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC       heterotetrameric complex of pore-forming alpha subunits that can
CC       associate with modulating beta subunits. Heteromultimer with
CC       KCNH5/EAG2. Interacts with ALG10B (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position.
CC   -!- SIMILARITY: Belongs to the potassium channel family. H (Eag)
CC       (TC 1.A.1.20) subfamily. Kv10.1/KCNH1 sub-subfamily.
CC   -!- SIMILARITY: Contains 1 cyclic nucleotide-binding domain.
CC   -!- SIMILARITY: Contains 1 PAC (PAS-associated C-terminal) domain.
CC   -!- SIMILARITY: Contains 1 PAS (PER-ARNT-SIM) domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; U04294; AAA62474.1; -; mRNA.
DR   IPI; IPI00118979; -.
DR   PIR; I48912; I48912.
DR   RefSeq; NP_034730.1; NM_010600.2.
DR   UniGene; Mm.4489; -.
DR   ProteinModelPortal; Q60603; -.
DR   SMR; Q60603; 29-135, 450-503, 506-693.
DR   STRING; Q60603; -.
DR   PRIDE; Q60603; -.
DR   Ensembl; ENSMUST00000078470; ENSMUSP00000077563; ENSMUSG00000058248.
DR   GeneID; 16510; -.
DR   KEGG; mmu:16510; -.
DR   UCSC; uc007edo.1; mouse.
DR   CTD; 16510; -.
DR   MGI; MGI:1341721; Kcnh1.
DR   GeneTree; ENSGT00550000074394; -.
DR   HOGENOM; HBG717083; -.
DR   HOVERGEN; HBG101348; -.
DR   InParanoid; Q60603; -.
DR   OMA; ENARTEQ; -.
DR   OrthoDB; EOG47PX5C; -.
DR   PhylomeDB; Q60603; -.
DR   NextBio; 289847; -.
DR   ArrayExpress; Q60603; -.
DR   Bgee; Q60603; -.
DR   Genevestigator; Q60603; -.
DR   GermOnline; ENSMUSG00000058248; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:two-component sensor activity; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003949; K_chnl_volt-dep_EAG.
DR   InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PRINTS; PR01463; EAGCHANLFMLY.
DR   PRINTS; PR01464; EAGCHANNEL.
DR   SMART; SM00100; cNMP; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF51206; cNMP_binding; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; FALSE_NEG.
DR   PROSITE; PS00889; CNMP_BINDING_2; FALSE_NEG.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   2: Evidence at transcript level;
KW   Calmodulin-binding; Glycoprotein; Ion transport; Ionic channel;
KW   Membrane; Potassium; Potassium channel; Potassium transport;
KW   Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    989       Potassium voltage-gated channel subfamily
FT                                H member 1.
FT                                /FTId=PRO_0000053995.
FT   TOPO_DOM      1    220       Cytoplasmic (Potential).
FT   TRANSMEM    221    241       Helical; Name=Segment S1; (Potential).
FT   TOPO_DOM    242    248       Extracellular (Potential).
FT   TRANSMEM    249    269       Helical; Name=Segment S2; (Potential).
FT   TOPO_DOM    270    294       Cytoplasmic (Potential).
FT   TRANSMEM    295    315       Helical; Name=Segment S3; (Potential).
FT   TOPO_DOM    316    349       Extracellular (Potential).
FT   TRANSMEM    350    370       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TOPO_DOM    371    376       Cytoplasmic (Potential).
FT   TRANSMEM    377    397       Helical; Name=Segment S5; (Potential).
FT   TOPO_DOM    398    450       Extracellular (Potential).
FT   INTRAMEM    451    471       Pore-forming; Name=Segment H5;
FT                                (Potential).
FT   TOPO_DOM    472    477       Extracellular (Potential).
FT   TRANSMEM    478    498       Helical; Name=Segment S6; (Potential).
FT   TOPO_DOM    499    989       Cytoplasmic (Potential).
FT   DOMAIN       14     94       PAS.
FT   DOMAIN       93    145       PAC.
FT   NP_BIND     581    698       cNMP.
FT   REGION      673    770       Calmodulin-binding (By similarity).
FT   REGION      924    964       CAD (involved in subunit assembly) (By
FT                                similarity).
FT   MOTIF       463    468       Selectivity filter (By similarity).
FT   CARBOHYD    415    415       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    433    433       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   989 AA;  111314 MW;  BA9B8C30F958CDCA CRC64;
     MTMAGGRRGL VAPQNTFLEN IVRRSNDTNF VLGNAQIVDW PIVYSNDGFC KLSGYHRAEV
     MQKSSACSFM YGELTDKDTV EKVRQTFENY EMNSFEILMY KKNRTPVWFF VKIAPIRNEQ
     DKVVLFLCTF SDITAFKQPI EDDSCKGWGK FARLTRALTS SRGVLQQLAP SVQKGENVHK
     HSRLAEVLQL GSDILPQYKQ EAPKTPPHII LHYCVFKTTW DWIILILTFY TAILVPYNVS
     FKTRQNNVAW LVVDSIVDVI FLVDIVLNFH TTFVGPAGEV ISDPKLIRMN YLKTWFVIDL
     LSCLPYDVIN AFENVDEVSA FMGDPGKIGF ADQIPPPLEG RESQGISSLF SSLKVVRLLR
     LGRVARKLDH YIEYGAAVLV LLVCVFGLAA HWMACIWYSI GDYEIFDEDT KTIRNNSWLY
     QLALDIGTPY QFNGSGSGKW EGGPSKNSVY ISSLYFTMTS LTSVGFGNIA PSTDIEKIFA
     VAIMMIGSLL YATIFGNVTT IFQQMYANTN RYHEMLNSVR DFLKLYQVPK GLSERVMDYI
     VSTWSMSRGI DTEKVLQICP KDMRADICVH LNRKVFKEHP AFRLASDGCL RALAMEFQTV
     HCAPGDLIYH AGESVDSLCF VVSGSLEVIQ DDEVVAILGK GDVFGDVFWK EATLAQSCAN
     VRALTYCDLH VIKRDALQKV LEFYTAFSHS FSRNLILTYN LRKRIVFRKI SDVKREEEER
     MKRKNEAPLI LPPDHPVRRL FQRFRQQKEA RLAAERGGRD LDDLDVEKGN ALTDHTSANH
     SLVKASVVTV RESPATPVSF QAATTSTMSD HAKLHAPGSE CLGPKAVSCD PAKRKGWARF
     KDACGKGEDW NKVSKAESME TLPERTKAPG EATLKKTDSC DSGITKSDLR LDNVGETRSP
     QDRSPILAEV KHSFYPIPEQ TLQATVLEVK YELKEDIKAL NAKMTSIEKQ LSEILRILMS
     RGSAQSPQET GEISRPQSPE SDRDIFGAS
//
ID   TIAM1_MOUSE             Reviewed;        1591 AA.
AC   Q60610;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 104.
DE   RecName: Full=T-lymphoma invasion and metastasis-inducing protein 1;
DE            Short=TIAM-1;
GN   Name=Tiam1; Synonyms=Tiam-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=94243921; PubMed=7999144; DOI=10.1016/0092-8674(94)90216-X;
RA   Habets G.G.M., Scholtes E.H.M., Zuydgeest D., van der Kammen R.A.,
RA   Stam J.C., Berns A., Collard J.G.;
RT   "Identification of an invasion-inducing gene, Tiam-1, that encodes a
RT   protein with homology to GDP-GTP exchangers for Rho-like proteins.";
RL   Cell 77:537-549(1994).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1323, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1033-1406 IN COMPLEX WITH
RP   RAC1.
RX   MEDLINE=21012003; PubMed=11130063; DOI=10.1038/35047014;
RA   Worthylake D.K., Rossman K.L., Sondek J.;
RT   "Crystal structure of Rac1 in complex with the guanine nucleotide
RT   exchange region of Tiam1.";
RL   Nature 408:682-688(2000).
CC   -!- FUNCTION: Modulates the activity of RHO-like proteins and connects
CC       extracellular signals to cytoskeletal activities. Acts as a GDP-
CC       dissociation stimulator protein that stimulates the GDP-GTP
CC       exchange activity of RHO-like GTPases and activates them.
CC       Activates RAC1, CDC42, and to a lesser extent RHOA (By
CC       similarity). Affects invasiveness of T-lymphoma cells.
CC   -!- SUBUNIT: Interacts with BAIAP2 (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and testis and at
CC       low or moderate levels in almost all other normal tissues. Found
CC       in virtually all analyzed tumor cell lines including B- and T-
CC       lymphomas, neuroblastomas, melanomas and carcinomas.
CC   -!- SIMILARITY: Belongs to the TIAM family.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -!- SIMILARITY: Contains 1 RBD (Ras-binding) domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U05245; AAA18830.1; -; mRNA.
DR   IPI; IPI00119006; -.
DR   PIR; A54146; A54146.
DR   UniGene; Mm.310902; -.
DR   PDB; 1FOE; X-ray; 2.80 A; A/C/E/G=1033-1406.
DR   PDB; 3A8N; X-ray; 4.50 A; A=429-702.
DR   PDBsum; 1FOE; -.
DR   PDBsum; 3A8N; -.
DR   ProteinModelPortal; Q60610; -.
DR   SMR; Q60610; 433-670, 835-935, 1034-1401.
DR   STRING; Q60610; -.
DR   PhosphoSite; Q60610; -.
DR   SWISS-2DPAGE; Q60610; -.
DR   PRIDE; Q60610; -.
DR   Ensembl; ENSMUST00000002588; ENSMUSP00000002588; ENSMUSG00000002489.
DR   Ensembl; ENSMUST00000114124; ENSMUSP00000109759; ENSMUSG00000002489.
DR   UCSC; uc007zvu.1; mouse.
DR   MGI; MGI:103306; Tiam1.
DR   GeneTree; ENSGT00600000084055; -.
DR   HOGENOM; HBG506823; -.
DR   HOVERGEN; HBG059279; -.
DR   InParanoid; Q60610; -.
DR   OrthoDB; EOG49CQ6T; -.
DR   NextBio; 301314; -.
DR   PMAP-CutDB; Q60610; -.
DR   ArrayExpress; Q60610; -.
DR   Bgee; Q60610; -.
DR   CleanEx; MM_TIAM1; -.
DR   Genevestigator; Q60610; -.
DR   GermOnline; ENSMUSG00000002489; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0046875; F:ephrin receptor binding; IPI:MGI.
DR   GO; GO:0005543; F:phospholipid binding; IDA:MGI.
DR   GO; GO:0005057; F:receptor signaling protein activity; IEA:InterPro.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:MGI.
DR   GO; GO:0050772; P:positive regulation of axonogenesis; IMP:MGI.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:MGI.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR003116; Raf-like_ras-bd.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF02196; RBD; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00455; RBD; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50898; RBD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Guanine-nucleotide releasing factor; Lipoprotein;
KW   Myristate; Phosphoprotein; Repeat.
FT   INIT_MET      1      1       Removed (Potential).
FT   CHAIN         2   1591       T-lymphoma invasion and metastasis-
FT                                inducing protein 1.
FT                                /FTId=PRO_0000080977.
FT   DOMAIN      434    549       PH 1.
FT   DOMAIN      765    832       RBD.
FT   DOMAIN      845    908       PDZ.
FT   DOMAIN     1040   1234       DH.
FT   DOMAIN     1261   1397       PH 2.
FT   COMPBIAS    595    598       Poly-Lys.
FT   COMPBIAS   1445   1449       Poly-Arg.
FT   MOD_RES     231    231       Phosphoserine.
FT   MOD_RES     356    356       Phosphoserine (By similarity).
FT   MOD_RES     358    358       Phosphoserine (By similarity).
FT   MOD_RES    1323   1323       Phosphotyrosine.
FT   LIPID         2      2       N-myristoyl glycine (Potential).
FT   HELIX      1037   1065
FT   HELIX      1067   1071
FT   STRAND     1073   1076
FT   HELIX      1078   1085
FT   HELIX      1088   1106
FT   HELIX      1112   1114
FT   HELIX      1118   1121
FT   HELIX      1122   1135
FT   HELIX      1138   1141
FT   HELIX      1142   1148
FT   TURN       1149   1151
FT   HELIX      1152   1156
FT   TURN       1157   1161
FT   HELIX      1163   1172
FT   HELIX      1178   1180
FT   HELIX      1182   1185
FT   HELIX      1188   1193
FT   HELIX      1196   1205
FT   HELIX      1212   1249
FT   HELIX      1264   1266
FT   STRAND     1267   1277
FT   HELIX      1280   1283
FT   STRAND     1290   1296
FT   STRAND     1299   1304
FT   TURN       1318   1321
FT   STRAND     1332   1336
FT   HELIX      1337   1339
FT   STRAND     1340   1343
FT   TURN       1348   1351
FT   STRAND     1355   1360
FT   HELIX      1365   1367
FT   STRAND     1371   1379
FT   HELIX      1380   1400
SQ   SEQUENCE   1591 AA;  177533 MW;  ECC2BAB189A6F019 CRC64;
     MGNAESQNVD HEFYGEKHAS LGRKHTSRSL RLSHKTRRTR HASSGKAIHR NSEVSTRSSS
     TPSIPQSLAE NGLEPFSQEG ALDDFGDPIW VDRVDMGLRP VSYTDSSVTP SVDGSIVLTA
     ASVQSMPDSE ESRLYGDDAT YLAEGGRRQC PYTSNGPTFM ETASFKKKRS KSADIWREDS
     LEFSLSDLSQ EHLTSNEEIL GSAEEKDCEE ARGMETEASP RQLSTCQRAN SLGDLYAQKN
     SGVKANGGPR NRFSSYCRNL VSDIPDLAKH KMPPAAAEET PPYSNYNTLP CRKSHCLSEG
     ATNPQISLSK SMQGRRAKTT QDVNTGEGSE FADSGIEGAT TDTDLLSRRS NATNSSYSPP
     TGRAFVGSDS GSSSTGDRAR QGVYENFRRE LEMSTTNSES LEEAGSAHSD EQSSGTLSSP
     GQSDILLTAA QGTVRKAGAL AVKNFLVHKK NKKVESATRR KWKHYWVSLK GCTLFFYETD
     GRSGIDHNSV PKHAVWVENS IVQAVPEHPK KDFVFCLSNS LGDAFLFQTT SQTELENWIT
     AIHSACAAAV ARHHHKEDTL RLLKSEIKKL EQKIDMDEKM KKMGEMQLSS VTDSKKKKTI
     LDQIFVWEQN LEQFQMDLFR FRCYLASLQG GELPNPKRLL AFASRPTKVA MGRLGIFSVS
     SFHALVAART GEIGVRRRTQ AMSRSASKRR SRFSSLWGLD TTSKKKQGRP TINQVFGEGT
     DAVKRSLEGI FDDTVPDGKR EKEVVLPSVH QHNPDCDIWV HEYFTPSWFC LPNNQPALTV
     VRPGDTARDT LELICKTHQL DHSAHYLRLK FLMENRVQFY IPQPEEDIYE LLYKEIEICP
     KVTQNIHIEK SDAAADNYGF LLSSVDEDGI RRLYVNSVKE TGLASKKGLK AGDEILEINN
     RAAGTLNSSM LKDFLSQPSL GLLVRTYPEP EGGVELLENP PHRVDGPVDL GESPLAFLTS
     NPGHSLSSEQ GSSAETAPEE GEGPDLESSD ETDHSSKSTE QVAAFCRSLH EMSPSDSSPS
     PQDATSPQLA TTRQLSDADK LRKVICELLE TERTYVKDLN CLMERYLKPL QKETFLTQDE
     LDVLFGNLTE MVEFQVEFLK TLEDGVRLVP DLEKLEKVDQ FKKVLFSLGG SFLYYADRFK
     LYSAFCASHT KVPKVLVKAK TDTAFKAFLD AQNPRQQHSS TLESYLIKPI QRVLKYPLLL
     RELFALTDAE SEEHYHLDVA IKTMNKVASH INEMQKIHEE FGAVFDQLIA EQTGEKKEVA
     DLSMGDLLLH TSVIWLNPPA SLGKWKKEPE LAAFVFKTAV VLVYKDGSKQ KKKLVGSHRL
     SIYEEWDPFR FRHMIPTEAL QVRALPSADA EANAVCEIVH VKSESEGRPE RVFHLCCSSP
     ESRKDFLKSV HSILRDKHRR QLLKTESLPS AQQYVPFGGK RLCALKGARP AMSRAVSAPS
     KSLGRRRRRL ARNRFTIDSD AISASSPEKE PQQPAGGGDT DRWVEEQFDL AQYEEQDDIK
     ETDILSDDDE FCESLKGASV DRDLQEQLQA ASISQRARGR RTLDSHASRM TQLKKQAALS
     GINGGLESAS EEVIWVRRED FAPSRKLNTE I
//
ID   SATB1_MOUSE             Reviewed;         764 AA.
AC   Q60611;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-FEB-2011, entry version 99.
DE   RecName: Full=DNA-binding protein SATB1;
DE   AltName: Full=Special AT-rich sequence-binding protein 1;
GN   Name=Satb1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Thymus;
RX   MEDLINE=94158857; PubMed=8114718;
RA   Nakagomi K., Kohwi Y., Dickinson L.A., Kohwi-Shigematsu T.;
RT   "A novel DNA-binding motif in the nuclear matrix attachment DNA-
RT   binding protein SATB1.";
RL   Mol. Cell. Biol. 14:1852-1860(1994).
RN   [2]
RP   PROTEIN SEQUENCE OF 255-259, FUNCTION, DIMERIZATION, AND CLEAVAGE BY
RP   CASP6.
RX   PubMed=11463840; DOI=10.1128/MCB.21.16.5591-5604.2001;
RA   Galande S., Dickinson L.A., Mian I.S., Sikorska M.,
RA   Kohwi-Shigematsu T.;
RT   "SATB1 cleavage by caspase 6 disrupts PDZ domain-mediated
RT   dimerization, causing detachment from chromatin early in T-cell
RT   apoptosis.";
RL   Mol. Cell. Biol. 21:5591-5604(2001).
RN   [3]
RP   FUNCTION.
RX   PubMed=9271405;
RA   Liu J., Bramblett D., Zhu Q., Lozano M., Kobayashi R., Ross S.R.,
RA   Dudley J.P.;
RT   "The matrix attachment region-binding protein SATB1 participates in
RT   negative regulation of tissue-specific gene expression.";
RL   Mol. Cell. Biol. 17:5275-5287(1997).
RN   [4]
RP   INTERACTION WITH CUX1.
RX   PubMed=10373541;
RA   Liu J., Barnett A., Neufeld E.J., Dudley J.P.;
RT   "Homeoproteins CDP and SATB1 interact: potential for tissue-specific
RT   regulation.";
RL   Mol. Cell. Biol. 19:4918-4926(1999).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=10716941;
RA   Alvarez J.D., Yasui D.H., Niida H., Joh T., Loh D.Y.,
RA   Kohwi-Shigematsu T.;
RT   "The MAR-binding protein SATB1 orchestrates temporal and spatial
RT   expression of multiple genes during T-cell development.";
RL   Genes Dev. 14:521-535(2000).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12692553; DOI=10.1038/ng1146;
RA   Cai S., Han H.-J., Kohwi-Shigematsu T.;
RT   "Tissue-specific nuclear architecture and gene expression regulated by
RT   SATB1.";
RL   Nat. Genet. 34:42-51(2003).
RN   [7]
RP   SUBCELLULAR LOCATION, AND NUCLEAR MATRIX TARGETING SEQUENCE.
RX   PubMed=15851481; DOI=10.1074/jbc.M414076200;
RA   Seo J., Lozano M.M., Dudley J.P.;
RT   "Nuclear matrix binding regulates SATB1-mediated transcriptional
RT   repression.";
RL   J. Biol. Chem. 280:24600-24609(2005).
RN   [8]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=15814699;
RA   Nie H., Maika S.D., Tucker P.W., Gottlieb P.D.;
RT   "A role for SATB1, a nuclear matrix association region-binding
RT   protein, in the development of CD8SP thymocytes and peripheral T
RT   lymphocytes.";
RL   J. Immunol. 174:4745-4752(2005).
RN   [9]
RP   FUNCTION.
RX   PubMed=17057718; DOI=10.1038/ng1913;
RA   Cai S., Lee C.C., Kohwi-Shigematsu T.;
RT   "SATB1 packages densely looped, transcriptionally active chromatin for
RT   coordinated expression of cytokine genes.";
RL   Nat. Genet. 38:1278-1288(2006).
RN   [10]
RP   FUNCTION.
RX   PubMed=18722016; DOI=10.1016/j.molimm.2008.07.007;
RA   Nie H., Yao X., Maika S.D., Tucker P.W.;
RT   "SATB1 is required for CD8 coreceptor reversal.";
RL   Mol. Immunol. 46:207-211(2008).
RN   [11]
RP   FUNCTION.
RX   PubMed=19386260; DOI=10.1016/j.devcel.2009.03.006;
RA   Agrelo R., Souabni A., Novatchkova M., Haslinger C., Leeb M.,
RA   Komnenovic V., Kishimoto H., Gresh L., Kohwi-Shigematsu T., Kenner L.,
RA   Wutz A.;
RT   "SATB1 defines the developmental context for gene silencing by Xist in
RT   lymphoma and embryonic cells.";
RL   Dev. Cell 16:507-516(2009).
RN   [12]
RP   FUNCTION, AND INTERACTION WITH CTBP1.
RX   PubMed=19103759; DOI=10.1128/MCB.00822-08;
RA   Purbey P.K., Singh S., Notani D., Kumar P.P., Limaye A.S., Galande S.;
RT   "Acetylation-dependent interaction of SATB1 and CtBP1 mediates
RT   transcriptional repression by SATB1.";
RL   Mol. Cell. Biol. 29:1321-1337(2009).
CC   -!- FUNCTION: Required for the switching of fetal globin species, and
CC       beta- and gamma-globin genes regulation during erythroid
CC       differentiation. Plays a role in chromatin organization and
CC       nuclear architecture during apoptosis (By similarity). Crucial
CC       silencing factor contributing to the initiation of X inactivation
CC       mediated by Xist RNA that occurs during embryogenesis and in
CC       lymphoma. Binds to DNA at special AT-rich sequences, the consensus
CC       SATB1-binding sequence (CSBS), at nuclear matrix- or scaffold-
CC       associated regions. Thought to recognize the sugar-phosphate
CC       structure of double-stranded DNA. Transcriptional repressor
CC       controlling nuclear and viral gene expression in a phosphorylated
CC       and acetylated status-dependent manner, by binding to matrix
CC       attachment regions (MARs) of DNA and inducing a local chromatin-
CC       loop remodeling. Acts as a docking site for several chromatin
CC       remodeling enzymes and also by recruiting corepressors (HDACs) or
CC       coactivators (HATs) directly to promoters and enhancers. Modulates
CC       genes that are essential in the maturation of the immune T-cell
CC       CD8SP from thymocytes.
CC   -!- SUBUNIT: Interacts with PCAF. Interacts with sumoylated PML and
CC       HDAC1 Tat via the PDZ-like dimerization domain. Interacts also
CC       with DYNLT3 and POLR2J2. Binds to EP300 (By similarity).
CC       Homodimer. Part of the nuclear protein complex gamma-globin
CC       promoter and enhancer binding factor (gamma-PE) composed at least
CC       by SATB1 and HOXB2. Interaction with CtBP1 when not acetylated
CC       stabalizes attachment to DNA and promotes transcription
CC       repression. Interacts (via DNA-binding domains) with CUX1; leading
CC       to inhibit the attachment to DNA.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body. Note=Organized
CC       into a cage-like network anchoring loops of heterochromatin and
CC       tethering specialized DNA sequences. When sumoylated, localized in
CC       promyelocytic leukemia nuclear bodies (PML NBs) (By similarity).
CC   -!- TISSUE SPECIFICITY: Mainly expressed in thymus, spleen, and lymph
CC       nodes with a lower level observed in the brain.
CC   -!- PTM: Sumoylated (By similarity). Sumoylation promotes cleavage by
CC       caspases (By similarity).
CC   -!- PTM: Phosphorylated by PKC. Acetylated by PCAF. Phosphorylated
CC       form interacts with HDAC1, but unphosphorylated form interacts
CC       with PCAF. DNA binding properties are activated by phosphorylation
CC       and inactivated by acetylation. In opposition, gene expression is
CC       down-regulated by phosphorylation but up-regulated by acetylation
CC       (By similarity).
CC   -!- PTM: Cleaved at Asp-254 by caspase-3 and caspase-6 during T-cell
CC       apoptosis in thymus and during B-cell stimulation. The cleaved
CC       forms can not dimerize and lose transcription regulation function
CC       because of impaired DNA and chromatin association.
CC   -!- DISRUPTION PHENOTYPE: Mice are small in size, have
CC       disproportionately small thymi and spleens, and die at 3 weeks of
CC       age. Multiple defects in T-cell development are observed,
CC       including interrupted thymocytes differentiation and abnormal T-
CC       cell transcriptome.
CC   -!- SIMILARITY: Belongs to the CUT homeobox family.
CC   -!- SIMILARITY: Contains 2 CUT DNA-binding domains.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
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DR   EMBL; U05252; AAA17372.1; -; mRNA.
DR   IPI; IPI00928043; -.
DR   PIR; A56208; A56208.
DR   UniGene; Mm.311655; -.
DR   ProteinModelPortal; Q60611; -.
DR   SMR; Q60611; 179-246, 370-452, 486-573, 647-705.
DR   STRING; Q60611; -.
DR   PhosphoSite; Q60611; -.
DR   PRIDE; Q60611; -.
DR   Ensembl; ENSMUST00000024720; ENSMUSP00000024720; ENSMUSG00000023927.
DR   UCSC; uc008czf.1; mouse.
DR   MGI; MGI:105084; Satb1.
DR   eggNOG; roNOG07523; -.
DR   HOGENOM; HBG447119; -.
DR   HOVERGEN; HBG054240; -.
DR   InParanoid; Q60611; -.
DR   NextBio; 297861; -.
DR   ArrayExpress; Q60611; -.
DR   Bgee; Q60611; -.
DR   CleanEx; MM_SATB1; -.
DR   Genevestigator; Q60611; -.
DR   GermOnline; ENSMUSG00000023927; Mus musculus.
DR   GO; GO:0005720; C:nuclear heterochromatin; IDA:MGI.
DR   GO; GO:0016363; C:nuclear matrix; IDA:MGI.
DR   GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0016564; F:transcription repressor activity; IDA:MGI.
DR   GO; GO:0050798; P:activated T cell proliferation; IMP:MGI.
DR   GO; GO:0043367; P:CD4-positive, alpha beta T cell differentiation; IMP:MGI.
DR   GO; GO:0043374; P:CD8-positive, alpha-beta T cell differentiation; IMP:MGI.
DR   GO; GO:0016571; P:histone methylation; IDA:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0060004; P:reflex; IMP:MGI.
DR   InterPro; IPR003350; Hmoeo_CUT.
DR   InterPro; IPR001356; Homeobox.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR010982; Lambda_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Pfam; PF02376; CUT; 2.
DR   Pfam; PF00046; Homeobox; 1.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
DR   SUPFAM; SSF47413; Lambda_like_DNA; 2.
DR   PROSITE; PS51042; CUT; 2.
DR   PROSITE; PS00027; HOMEOBOX_1; FALSE_NEG.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromatin regulator; Chromosomal rearrangement;
KW   Direct protein sequencing; DNA-binding; Homeobox; Isopeptide bond;
KW   Nucleus; Phosphoprotein; Repeat; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN         1    764       DNA-binding protein SATB1.
FT                                /FTId=PRO_0000202399.
FT   DNA_BIND    361    448       CUT 1.
FT   DNA_BIND    484    571       CUT 2.
FT   DNA_BIND    646    705       Homeobox.
FT   REGION       90    204       PDZ-like dimerization domain.
FT   REGION      224    278       Nuclear matrix targeting sequence (NMTS)
FT                                (By similarity).
FT   REGION      400    410       Matrix attachment region (MAR) DNA-
FT                                binding (By similarity).
FT   MOTIF        20     40       Nuclear localization signal (By
FT                                similarity).
FT   MOTIF       139    143       Protein interaction (By similarity).
FT   MOTIF       224    278       Nuclear matrix targeting sequence (NMTS).
FT   COMPBIAS    591    607       Poly-Gln.
FT   COMPBIAS    608    617       Poly-Pro.
FT   BINDING     390    390       Matrix attachment region (MAR) DNA (By
FT                                similarity).
FT   BINDING     425    425       Matrix attachment region (MAR) DNA (By
FT                                similarity).
FT   SITE        254    255       Cleavage; by caspases.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     136    136       N6-acetyllysine (By similarity).
FT   MOD_RES     185    185       Phosphoserine (By similarity).
FT   CROSSLNK    745    745       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
SQ   SEQUENCE   764 AA;  85863 MW;  E86D22BB6E261F5C CRC64;
     MDHLNEATQG KEHSEMSNNV SDPKGPPAKI ARLEQNGSPL GRGRLGSTGG KMQGVPLKHS
     GHLMKTNLRK GTMLPVFCVV EHYENAIEYD CKEEHAEFVL VRKDMLFNQL IEMALLSLGY
     SHSSAAQAKG LIQVGKWNPV PLSYVTDAPD ATVANMLQDV YHVVTLKIQL HSCPKLEDLP
     PEQWSHTTVR NALKDLLKDM NQSSLAKECP LSQSMISSIV NSTYYANVSA AKCQEFGRWY
     KHFKKTKDMM VEMDSLSELS QQGANHVNFG QQPVPGNTAE QPPSPAQLSH GSQPSVRTPL
     PNLHPGLVST PISPQLVNQQ LVMAQLLNQQ YAVNRLLAQQ SLNQQYLNHP PPVSRSMNKP
     LEQQVSTNTE VSSEIYQWVR DELKRAGISQ AVFARVAFNR TQGLLSEILR KEEDPKTASQ
     SLLVNLRAMQ NFLQLPEAER DRIYQDERER SLNAASAMGP APLLSTPPSR PPQVKTATLA
     TERNGKPENN TMNINASIYD EIQQEMKRAK VSQAPFAKVA ATKSQGWLCE LLRWKEDPSP
     ENRTLWENLS MIRRFLSLPQ PERDAIYEQE SNAVHHHGDR PPHIIHVPAE QIQQQQQQQQ
     QQQQQQQPPP PPPQPQPQPQ AGPRLPPRQP TVASSAESDE ENRQKTRPRT KISVEALGIL
     QSFIQDVGLY PDEEAIQTLS AQLDLPKYTI IKFFQNQRYY LKHHGKLKDN SGLEVDVAEY
     KDEELLKDLE ESVQDKNANT LFSVKLEEEL SVEGSTDVNA DLKD
//
ID   HNRPD_MOUSE             Reviewed;         355 AA.
AC   Q60668; Q60667; Q80ZJ0; Q91X94;
DT   04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   04-AUG-2003, sequence version 2.
DT   08-MAR-2011, entry version 105.
DE   RecName: Full=Heterogeneous nuclear ribonucleoprotein D0;
DE            Short=hnRNP D0;
DE   AltName: Full=AU-rich element RNA-binding protein 1;
GN   Name=Hnrnpd; Synonyms=Auf1, Hnrpd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-228 (ISOFORMS 2/4), AND NUCLEOTIDE
RP   SEQUENCE [MRNA] OF 25-355 (ISOFORM 3).
RC   STRAIN=BALB/c; TISSUE=Embryo;
RX   MEDLINE=95047495; PubMed=7959009; DOI=10.1016/0378-1119(94)90168-6;
RA   Ehrenman K., Long L., Wagner B.J., Brewer G.;
RT   "Characterization of cDNAs encoding the murine A+U-rich RNA-binding
RT   protein AUF1.";
RL   Gene 149:315-319(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 5-355 (ISOFORM 1).
RC   TISSUE=Brain, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 184-197, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-83, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Binds with high affinity to RNA molecules that contain
CC       AU-rich elements (AREs) found within the 3'-UTR of many proto-
CC       oncogenes and cytokine mRNAs. Also binds to double- and single-
CC       stranded DNA sequences in a specific manner and functions a
CC       transcription factor. Each of the RNA-binding domains specifically
CC       can bind solely to a single-stranded non-monotonous 5'-UUAG-3'
CC       sequence and also weaker to the single-stranded 5'-TTAGGG-3'
CC       telomeric DNA repeat. Binds RNA oligonucleotides with 5'-UUAGGG-3'
CC       repeats more tightly than the telomeric single-stranded DNA 5'-
CC       TTAGGG-3' repeats. Binding of RRM1 to DNA inhibits the formation
CC       of DNA quadruplex structure which may play a role in telomere
CC       elongation. May be involved in translationally coupled mRNA
CC       turnover. Implicated with other RNA-binding proteins in the
CC       cytoplasmic deadenylation/translational and decay interplay of the
CC       FOS mRNA mediated by the major coding-region determinant of
CC       instability (mCRD) domain (By similarity).
CC   -!- SUBUNIT: Identified in a mRNP granule complex, at least composed
CC       of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD,
CC       HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1,
CC       NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8,
CC       RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Part of a
CC       complex associated with the FOS mCRD domain and consisting of
CC       PABPC1, PAIP1, CSDE1/UNR and SYNCRIP. Interacts with IGF2BP2 (By
CC       similarity).
CC   -!- INTERACTION:
CC       P06151:Ldha; NbExp=2; IntAct=EBI-299932, EBI-444940;
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity). Note=Localized in cytoplasmic mRNP granules
CC       containing untranslated mRNAs. Component of ribonucleosomes (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q60668-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q60668-2; Sequence=VSP_007940;
CC       Name=3; Synonyms=muAUF1-3;
CC         IsoId=Q60668-3; Sequence=VSP_007941;
CC       Name=4;
CC         IsoId=Q60668-4; Sequence=VSP_007940, VSP_007941;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Methylated by PRMT1, in an insulin dependent manner. The
CC       PRMT1-mediated methylation regulates its phosphorylation (By
CC       similarity).
CC   -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA64653.1; Type=Frameshift; Positions=Several;
CC       Sequence=AAA64653.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence;
CC       Sequence=AAA64654.1; Type=Frameshift; Positions=Several;
CC       Sequence=AAA64654.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence;
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DR   EMBL; U11273; AAA64653.1; ALT_SEQ; mRNA.
DR   EMBL; U11274; AAA64654.1; ALT_SEQ; mRNA.
DR   EMBL; BC011172; AAH11172.2; -; mRNA.
DR   EMBL; BC049098; AAH49098.1; -; mRNA.
DR   IPI; IPI00230086; -.
DR   IPI; IPI00330958; -.
DR   IPI; IPI00336873; -.
DR   IPI; IPI00336874; -.
DR   PIR; I49069; I49069.
DR   PIR; I49070; I49070.
DR   RefSeq; NP_001070733.1; NM_001077265.1.
DR   RefSeq; NP_001070734.1; NM_001077266.1.
DR   RefSeq; NP_001070735.1; NM_001077267.1.
DR   RefSeq; NP_031542.2; NM_007516.2.
DR   UniGene; Mm.150231; -.
DR   ProteinModelPortal; Q60668; -.
DR   SMR; Q60668; 95-260.
DR   IntAct; Q60668; 5.
DR   STRING; Q60668; -.
DR   PhosphoSite; Q60668; -.
DR   PRIDE; Q60668; -.
DR   Ensembl; ENSMUST00000019128; ENSMUSP00000019128; ENSMUSG00000000568.
DR   Ensembl; ENSMUST00000072750; ENSMUSP00000072533; ENSMUSG00000000568.
DR   Ensembl; ENSMUST00000112939; ENSMUSP00000108561; ENSMUSG00000000568.
DR   GeneID; 11991; -.
DR   KEGG; mmu:11991; -.
DR   UCSC; uc008ygt.1; mouse.
DR   UCSC; uc008ygu.1; mouse.
DR   UCSC; uc008ygv.1; mouse.
DR   UCSC; uc008ygw.1; mouse.
DR   CTD; 11991; -.
DR   MGI; MGI:101947; Hnrnpd.
DR   GeneTree; ENSGT00560000076532; -.
DR   HOGENOM; HBG756718; -.
DR   HOVERGEN; HBG002295; -.
DR   InParanoid; Q60668; -.
DR   OMA; NEEDEGX; -.
DR   OrthoDB; EOG49W2FZ; -.
DR   PhylomeDB; Q60668; -.
DR   NextBio; 280159; -.
DR   ArrayExpress; Q60668; -.
DR   Bgee; Q60668; -.
DR   Genevestigator; Q60668; -.
DR   GermOnline; ENSMUSG00000000568; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030529; C:ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0042162; F:telomeric DNA binding; ISS:UniProtKB.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR012956; CARG-binding_factor_N.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   Pfam; PF08143; CBFNT; 1.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm;
KW   Direct protein sequencing; DNA-binding; Methylation; Nucleus;
KW   Phosphoprotein; Repeat; Ribonucleoprotein; RNA-binding; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    355       Heterogeneous nuclear ribonucleoprotein
FT                                D0.
FT                                /FTId=PRO_0000081850.
FT   DOMAIN       97    179       RRM 1.
FT   DOMAIN      182    261       RRM 2.
FT   MOD_RES      80     80       Phosphoserine.
FT   MOD_RES      82     82       Phosphoserine (By similarity).
FT   MOD_RES      83     83       Phosphoserine.
FT   MOD_RES     119    119       N6-methyllysine (By similarity).
FT   MOD_RES     165    165       N6-acetyllysine (By similarity).
FT   MOD_RES     190    190       Phosphoserine (By similarity).
FT   MOD_RES     193    193       Phosphothreonine (By similarity).
FT   MOD_RES     251    251       N6-acetyllysine (By similarity).
FT   MOD_RES     341    341       N6-acetyllysine (By similarity).
FT   MOD_RES     345    345       Asymmetric dimethylarginine (By
FT                                similarity).
FT   MOD_RES     353    353       N6-acetyllysine (By similarity).
FT   VAR_SEQ      74     92       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_007940.
FT   VAR_SEQ     285    334       GPSQNWNQGYSNYWNQGYGNYGYNSQGYGGYGGYDYTGYNN
FT                                YYGYGDYSN -> D (in isoform 3 and isoform
FT                                4).
FT                                /FTId=VSP_007941.
FT   CONFLICT     22     23       SA -> G (in Ref. 1; AAA64653).
FT   CONFLICT     35     38       AQGP -> RRA (in Ref. 1; AAA64654).
FT   CONFLICT     35     37       AQG -> RR (in Ref. 1; AAA64653).
FT   CONFLICT     50     53       GSAA -> LCG (in Ref. 1; AAA64654).
FT   CONFLICT    217    217       N -> K (in Ref. 1; AAA64654).
FT   CONFLICT    227    228       FI -> ID (in Ref. 1; AAA64653).
SQ   SEQUENCE   355 AA;  38354 MW;  5941DFC6F65B88DF CRC64;
     MSEEQFGGDG AAAAATAAVG GSAGEQEGAM VAAAAQGPAA AAGSGSGGGG SAAGGTEGGS
     AEAEGAKIDA SKNEEDEGHS NSSPRHTEAA AAQREEWKMF IGGLSWDTTK KDLKDYFSKF
     GEVVDCTLKL DPITGRSRGF GFVLFKESES VDKVMDQKEH KLNGKVIDPK RAKAMKTKEP
     VKKIFVGGLS PDTPEEKIRE YFGGFGEVES IELPMDNKTN KRRGFCFITF KEEEPVKKIM
     EKKYHNVGLS KCEIKVAMSK EQYQQQQQWG SRGGFAGRAR GRGGGPSQNW NQGYSNYWNQ
     GYGNYGYNSQ GYGGYGGYDY TGYNNYYGYG DYSNQQSGYG KVSRRGGHQN SYKPY
//
ID   Q60669_MOUSE            Unreviewed;       938 AA.
AC   Q60669;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Ephrin receptor;
DE            EC=2.7.10.1;
DE   Flags: Fragment;
GN   Name=Ephb3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=95200798; PubMed=7893599; DOI=10.1016/0925-4773(94)90056-6;
RA   Ruiz J.C., Conlon F.L., Robertson E.J.;
RT   "Identification of novel protein kinases expressed in the myocardium
RT   of the developing mouse heart.";
RL   Mech. Dev. 48:153-164(1994).
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Ephrin receptor subfamily.
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; U11493; AAA67925.1; -; mRNA.
DR   IPI; IPI00387374; -.
DR   PIR; I49071; I49071.
DR   UniGene; Mm.6972; -.
DR   HSSP; P54763; 1JPA.
DR   ProteinModelPortal; Q60669; -.
DR   STRING; Q60669; -.
DR   Ensembl; ENSMUST00000006112; ENSMUSP00000006112; ENSMUSG00000005958.
DR   MGI; MGI:104770; Ephb3.
DR   HOVERGEN; HBG062180; -.
DR   InParanoid; Q60669; -.
DR   ArrayExpress; Q60669; -.
DR   Bgee; Q60669; -.
DR   Genevestigator; Q60669; -.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008046; F:axon guidance receptor activity; IDA:MGI.
DR   GO; GO:0005005; F:transmembrane-ephrin receptor activity; TAS:MGI.
DR   GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IDA:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0031290; P:retinal ganglion cell axon guidance; IDA:MGI.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   InterPro; IPR001090; Ephrin_rcpt_lig-bd.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   InterPro; IPR016257; Tyr_prot_kinase_ephrin_rcpt.
DR   InterPro; IPR001426; Tyr_prot_kinase_rcpt_V_CS.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF01404; Ephrin_lbd; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07699; GCC2_GCC3; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00615; EPH_lbd; 1.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; FN_III-like; 2.
DR   SUPFAM; SSF49785; Gal_bind_like; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
DR   PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Membrane; Nucleotide-binding; Receptor;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   NON_TER       1      1
SQ   SEQUENCE   938 AA;  103997 MW;  8D128CA46F19E73F CRC64;
     EVSGYDEAMN PIRTYQVCNV RESSQNNWLR TGFIWRREVQ RVYVELKFTV RDCNSIPNIP
     GSCKETFNLF YYEADSDVAS ASSPFWMENP YVKVDTISPD ESFSRSMPGR VNTKVRSFGP
     LSKAGFYLGF QDQGACMSLI SVRAFYKKCA STTAGFALFP ETLTGAEATS LVIAPRACIA
     NAVEVSVPLK LYCNGDGEWM VPVGACTCAT GHEPAAKESQ CRACPPGSYK AKQGEGPCLP
     CPPNSRTTSP AASICTCHNN FYRADSDSAD SACTTRRSPP RGVISNVNET SLILEWSEPR
     DLGGRDDLLY NVICKKCRGS SGAGGPATCS RCDDNVEFVP RQLGLTERRV HISHLLAHTR
     YTFEVQAVNG VSGKSPLPPR YAAVNITTNQ AAPSEVPTLH SHSTSGSSLT LSWAPPERPN
     GVILDYEMKY FEKSKAIAST VTSQKNSVQL DGLQPDARYV VQVRARTVAG YGQYTHPAEF
     ETTSERGSGA QQLQEQLPLI VGSNVAGFVF MVVVVVIALV CLRKQRHGPD AEYTEKLQQY
     IAPGMKVYID PFTYEDPNEA VREFAKEIDV SCVKIEEVIG AGEFGEVCRG RLKLPGRREV
     FVAIKTLKVG YTERQRRDFL SEASNMGQFD HPNIIRLEGV VTKSRPVMIL TEFMENCALD
     SFLRLNDGQF TVIQLVGMLR GIAAGMKYLS EMNYVHRDLA ARNILVNSNL VCKVSDFGLS
     RFLEDDPSDP TYTSSLGGKI PIRWTAPEPI AYRKFDSASD VWSYGIVMWE VMSYGEQPYW
     NMSNQDDINA VEQDYRLPPP MDCPTALHQL MASCWVRDRN LRPKFSQIVN TLDKLIRNAA
     SLKVTASAPS GMSQPLLDRT VPDYTTFTTG CDWLDAIKMR RYKESFVGAG FASFDLVAQM
     TAEDLLRIGV TLVGHQKKIL CSIQDMRLQM NQTLPVQV
//
ID   PTPRN_MOUSE             Reviewed;         979 AA.
AC   Q60673; Q62129;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Receptor-type tyrosine-protein phosphatase-like N;
DE            Short=R-PTP-N;
DE   AltName: Full=PTP IA-2;
DE   Flags: Precursor;
GN   Name=Ptprn; Synonyms=Ptp35;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=95071416; PubMed=7980563; DOI=10.1006/bbrc.1994.2549;
RA   Lu J., Notkins A.L., Lan M.S.;
RT   "Isolation, sequence and expression of a novel mouse brain cDNA, mIA-
RT   2, and its relatedness to members of the protein tyrosine phosphatase
RT   family.";
RL   Biochem. Biophys. Res. Commun. 204:930-936(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster; TISSUE=Fibroblast;
RX   MEDLINE=96095652; PubMed=8526904; DOI=10.1006/bbrc.1995.2758;
RA   Magistrelli G., Covini N., Mosca M., Lippoli G., Isacchi A.;
RT   "Expression of PTP35, the murine homologue of the protein tyrosine
RT   phosphatase-related sequence IA-2, is regulated during cell growth and
RT   stimulated by mitogens in 3T3 fibroblasts.";
RL   Biochem. Biophys. Res. Commun. 217:154-161(1995).
CC   -!- FUNCTION: Implicated in neuroendocrine secretory processes. May be
CC       involved in processes specific for neurosecretory granules, such
CC       as their biogenesis, trafficking or regulated exocytosis or may
CC       have a general role in neuroendocrine functions. Seems to lack
CC       intrinsic enzyme activity. May play a role in the regulation of
CC       secretory granules via its interaction with SNTB2 (By similarity).
CC   -!- SUBUNIT: Interacts with phosphorylated SNTB2, protecting it from
CC       protein cleavage by CAPN1. Dephosphorylation of SNTB2 upon insulin
CC       stimulation disrupts the interaction and results in its cleavage
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in the brain and
CC       fibroblasts. Weakly expressed in the colon, intestine, stomach and
CC       pancreas.
CC   -!- DEVELOPMENTAL STAGE: In fibroblasts, maximally expressed in
CC       exponentially growing cells (days 1 to 4).
CC   -!- INDUCTION: By mitogens such as basic fibroblast growth factor
CC       (BFGF) and platelet derived growth factor (PDGF).
CC   -!- PTM: Appears to undergo multiple proteolytic cleavage at
CC       consecutive basic residues (By similarity).
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 8 subfamily.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA52453.1; Type=Erroneous initiation;
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DR   EMBL; U11812; AAA52102.1; -; mRNA.
DR   EMBL; X74438; CAA52453.1; ALT_INIT; mRNA.
DR   IPI; IPI00313306; -.
DR   PIR; I48721; I48721.
DR   PIR; JC2349; JC2349.
DR   UniGene; Mm.2902; -.
DR   ProteinModelPortal; Q60673; -.
DR   SMR; Q60673; 468-558, 687-976.
DR   STRING; Q60673; -.
DR   PhosphoSite; Q60673; -.
DR   PRIDE; Q60673; -.
DR   Ensembl; ENSMUST00000027404; ENSMUSP00000027404; ENSMUSG00000026204.
DR   MGI; MGI:102765; Ptprn.
DR   HOVERGEN; HBG053762; -.
DR   InParanoid; Q60673; -.
DR   OrthoDB; EOG4WDDBX; -.
DR   ArrayExpress; Q60673; -.
DR   Bgee; Q60673; -.
DR   CleanEx; MM_PTPRN; -.
DR   Genevestigator; Q60673; -.
DR   GermOnline; ENSMUSG00000026204; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; TAS:MGI.
DR   GO; GO:0005886; C:plasma membrane; TAS:MGI.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; TAS:MGI.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   GO; GO:0000302; P:response to reactive oxygen species; ISS:UniProtKB.
DR   GO; GO:0007185; P:transmembrane receptor protein tyrosine phosphatase signaling pathway; TAS:MGI.
DR   InterPro; IPR021613; Receptor_IA-2.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Pfam; PF11548; Receptor_IA-2; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Receptor; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     37       By similarity.
FT   CHAIN        38    979       Receptor-type tyrosine-protein
FT                                phosphatase-like N.
FT                                /FTId=PRO_0000025452.
FT   TOPO_DOM     38    575       Extracellular (Potential).
FT   TRANSMEM    576    600       Helical; (Potential).
FT   TOPO_DOM    601    979       Cytoplasmic (Potential).
FT   DOMAIN      709    969       Tyrosine-protein phosphatase.
FT   REGION      909    915       Substrate binding (By similarity).
FT   ACT_SITE    909    909       Phosphocysteine intermediate (By
FT                                similarity).
FT   SITE        448    449       Cleavage (By similarity).
FT   CARBOHYD    506    506       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    524    524       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    166    169       RSWG -> GDGAGA (in Ref. 2; CAA52453).
FT   CONFLICT    363    363       M -> L (in Ref. 2; CAA52453).
FT   CONFLICT    615    615       L -> V (in Ref. 2; CAA52453).
FT   CONFLICT    675    675       S -> T (in Ref. 2; CAA52453).
FT   CONFLICT    859    859       L -> V (in Ref. 2; CAA52453).
SQ   SEQUENCE   979 AA;  106087 MW;  99921701B202B8C3 CRC64;
     MRRPRRPGGS GGSGGSGGLR LLVCLLLLSG RPGGCSAISA HGCLFDRRLC SHLEVCIQDG
     LFGQCQAGVG QARPLLQVTS PVLQRLQGVL RQLMSQGLSW HDDLTQHVIS QEMERIPRLR
     PPEPHPRDRS GLVPRKPGPA GELLTQGNPT GSSPAAQGFP RPAGGRSWGG SPLSSLQAEL
     LPPLLEHLLM PPQPPHPALT YEPALLQPYL FHQFGSRDGS RGSESSSGVV GVGHLSKAEG
     PALFSRSASK AILGTHSGHS FGDLTGPSPA QLFQDSGLLY MAQELPVPGR ARAPRLPENG
     GNRAEDSSEG HEEEVLGGRG EKSPPQAAQP ELSLQRLTAV LAGYGVELRQ LTPEQFSTLL
     TLMQLLPKGT GRNLEGAVNV GGADVKKTIQ QMQRGDPAEA LPPTPSLPGY LTASPASSEV
     QQVLSPGFPE PPHTPSPLGS SSVLLEKKSP LGQSQPTVVG RPSARPSAEE YGYIVTDQKP
     LSLVAGVRLL EILAEHVHMS SGSFINISVV GPAVTFRIRH NEQNLSLADV TQQAGLVKSE
     LEAQTGLQIL QTGVGQREEA AEVLPRQAHG ISPMRSVLLT LVALAGVAGL LVALAVALCM
     RHHSRQRDKE RLAALGPEGA HGDTTFEYQD LCRQHMATKS LFNRAEGQPE PSRVSSVSSQ
     FSDAAQASPS SHSSSPSWCE EPAQANMDIS TGHMILAYME DHLRNRDRLA KEWQALCAYQ
     AEPNTCAAAQ DESNIKKNRH PDFLPYDHAR IKLKVESSPS RSDYINASPI IEHDPRMPAY
     IATQGPLSHT IADFWQMVWE SGCTVIVMLT PLVEDGVKQC DRYWPDEGSS LYHVYEVNLV
     SEHIWCEDFL VRSFYLKNLQ TQETRTLTQF HFLSWPAEGT PASTRPLLDF RRKVNKCYRG
     RSCPIIVHCS DGAGRTGTYI LIDMVLNRMA KGVKEIDIAA TLEHVRDQRP GLVRSKDQFE
     FALTAVAEEV NAILKALPQ
//
ID   SKI_MOUSE               Reviewed;         725 AA.
AC   Q60698; Q8VIL5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Ski oncogene;
DE   AltName: Full=Proto-oncogene c-Ski;
GN   Name=Ski;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/Sv;
RA   Chen Y., Berk M., Chen H., Stavnezer E., Colmenares C.;
RT   "Mouse Ski proto-oncogene cDNA.";
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-324.
RC   STRAIN=129/J;
RX   MEDLINE=96127473; PubMed=8573720;
RA   Namciu S., Lyons G.E., Micales B.K., Heyman H.-C., Colmenares C.,
RA   Stavnezer E.;
RT   "Enhanced expression of mouse c-ski accompanies terminal skeletal
RT   muscle differentiation in vivo and in vitro.";
RL   Dev. Dyn. 204:291-300(1995).
CC   -!- FUNCTION: May play a role in terminal differentiation of skeletal
CC       muscle cells but not in the determination of cells to the myogenic
CC       lineage. Functions as a repressor of TGF-beta signaling.
CC   -!- SUBUNIT: Interacts with SMAD2, SMAD3 and SMAD4. Interacts with
CC       HIPK2. Part of a complex with HIPK2 and SMAD1/2/3. Interacts with
CC       PRDM16 and SMAD3; the interaction with PRDM16 promotes the
CC       recruitment SMAD3-HDAC1 complex on the promoter of TGF-beta target
CC       genes (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DEVELOPMENTAL STAGE: Is expressed in a uniform pattern in all
CC       embryonic cells prior to skeletal muscle cell formation in the
CC       myotomes of somites. Expression is first up-regulated in skeletal
CC       muscle at 12 dpc, this up-regulation is evident first in body wall
CC       muscle and one day later in limb muscles. At 13.5 dpc a most
CC       prominent expression is seen in all skeletal muscles. At this
CC       stage expression is seen in all other cells and tissues but at
CC       lower levels than in skeletal muscle.
CC   -!- SIMILARITY: Belongs to the SKI family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF435852; AAL30825.1; -; mRNA.
DR   EMBL; U14173; AAA99669.1; ALT_SEQ; Genomic_DNA.
DR   IPI; IPI00462772; -.
DR   UniGene; Mm.480566; -.
DR   ProteinModelPortal; Q60698; -.
DR   SMR; Q60698; 89-190, 216-310.
DR   STRING; Q60698; -.
DR   PhosphoSite; Q60698; -.
DR   PRIDE; Q60698; -.
DR   Ensembl; ENSMUST00000030917; ENSMUSP00000030917; ENSMUSG00000029050.
DR   UCSC; uc008wcz.1; mouse.
DR   MGI; MGI:98310; Ski.
DR   eggNOG; roNOG10432; -.
DR   HOVERGEN; HBG006599; -.
DR   InParanoid; Q60698; -.
DR   OrthoDB; EOG44QT1K; -.
DR   ArrayExpress; Q60698; -.
DR   Bgee; Q60698; -.
DR   CleanEx; MM_SKI; -.
DR   Genevestigator; Q60698; -.
DR   GermOnline; ENSMUSG00000029050; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005667; C:transcription factor complex; IPI:MGI.
DR   GO; GO:0017053; C:transcriptional repressor complex; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IGI:MGI.
DR   GO; GO:0046811; F:histone deacetylase inhibitor activity; IGI:MGI.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR   GO; GO:0030528; F:transcription regulator activity; IGI:MGI.
DR   GO; GO:0009948; P:anterior/posterior axis specification; IMP:MGI.
DR   GO; GO:0060349; P:bone morphogenesis; IMP:MGI.
DR   GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
DR   GO; GO:0060325; P:face morphogenesis; IMP:MGI.
DR   GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
DR   GO; GO:0022011; P:myelination in peripheral nervous system; IMP:MGI.
DR   GO; GO:0014902; P:myotube differentiation; IDA:MGI.
DR   GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR   GO; GO:0043585; P:nose morphogenesis; IMP:MGI.
DR   GO; GO:0021772; P:olfactory bulb development; IMP:MGI.
DR   GO; GO:0060021; P:palate development; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0042981; P:regulation of apoptosis; IMP:MGI.
DR   GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR   GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI.
DR   InterPro; IPR014890; c-SKI_SMAD-bd_dom.
DR   InterPro; IPR009061; DNA-bd_dom_put.
DR   InterPro; IPR010919; SAND_dom-like.
DR   InterPro; IPR003380; Transform_Ski.
DR   InterPro; IPR023216; Tscrpt_reg_SKI_SnoN.
DR   Gene3D; G3DSA:3.10.390.10; SAND; 1.
DR   Gene3D; G3DSA:3.10.260.20; Transform_Ski; 1.
DR   PANTHER; PTHR10005; Tscrpt_reg_SKI_SnoN; 1.
DR   Pfam; PF08782; c-SKI_SMAD_bind; 1.
DR   Pfam; PF02437; Ski_Sno; 1.
DR   SUPFAM; SSF46955; Putativ_DNA_bind; 1.
DR   SUPFAM; SSF63763; SAND_like; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Nucleus; Phosphoprotein; Proto-oncogene; Repeat.
FT   CHAIN         1    725       Ski oncogene.
FT                                /FTId=PRO_0000129383.
FT   COILED      534    708       Potential.
FT   MOD_RES     429    429       Phosphoserine (By similarity).
FT   MOD_RES     477    477       Phosphoserine (By similarity).
SQ   SEQUENCE   725 AA;  80119 MW;  1BFD05C38519505C CRC64;
     MEAAAAGRGG FQQPGLQKTL EQFHLSSMSS LGGPAVSRRA GQEAYKKESA KEAGAATVPA
     PVPTAAEPPP VLHLPAIQPP PPVLPGPFFM PSDRSTERCE TVLEGETISC FVVGGEKRLC
     LPQILNSVLR DFSLQQINSV CDELHIYCSR CTADQLEILK VMGILPFSAP SCGLITKTDA
     ERLCNALLYG GAYPPPCKKE LAASLALGLE LSERSVRVYH ECFGKCKGLL VPELYSSPSA
     ACIQCLDCRL MYPPHKFVVH SHKALENRTC HWGFDSANWR AYILLSQDYT GKEEQARLGR
     CLDDVKEKFD YANKYKRRVP RVSEPPASIR PKTDDTSSQS PASSEKDKQS TWLRTLAGSS
     NKSLGCTHPR QRLSAFRPWS PAVSASEKET SPHLPALIRD SFYSYKSFET AVAPNVALAP
     PTQQKVVNSP PCTTVVSRAP EPLTTCIQPR KRKLTLDTAG APDMLTPVAA AEEDKDSEAE
     VEVESREEFT SSLSSLSSPS FTSSSSAKDL SSPGMHAPPV VAPDAAAHVD APSGLEAELE
     HLRQALEGGL DTKEAKEKFL HEVVKMRVKQ EEKLTAALQA KRTLHQELEF LRVAKKEKLR
     EATEAKRNLR KEIERLRAEN EKKMKEANES RVRLKRELEQ ARQVRVCDKG CEAGRLRAKY
     SAQVEDLQAK LQHAEADREQ LRADLLRERE AREHLEKVVR ELQEQLRPRP RPEHPGGESN
     AELGP
//
ID   M3K12_MOUSE             Reviewed;         888 AA.
AC   Q60700; P70286; Q3TLL7; Q8C4N7; Q8CBX3; Q8CDL6;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 108.
DE   RecName: Full=Mitogen-activated protein kinase kinase kinase 12;
DE            EC=2.7.11.25;
DE   AltName: Full=Dual leucine zipper bearing kinase;
DE            Short=DLK;
DE   AltName: Full=Leucine-zipper protein kinase;
DE            Short=ZPK;
DE   AltName: Full=MAPK-upstream kinase;
DE            Short=MUK;
DE   AltName: Full=Mixed lineage kinase;
GN   Name=Map3k12; Synonyms=Zpk;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CD-1; TISSUE=Brain;
RX   MEDLINE=95074107; PubMed=7983011;
RA   Holzman L.B., Merritt S.E., Fan G.;
RT   "Identification, molecular cloning, and characterization of dual
RT   leucine zipper bearing kinase. A novel serine/threonine protein kinase
RT   that defines a second subfamily of mixed lineage kinases.";
RL   J. Biol. Chem. 269:30808-30817(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR X Swiss Webster; TISSUE=Brain;
RX   MEDLINE=96365388; PubMed=8769565; DOI=10.1089/dna.1996.15.631;
RA   Blouin R., Beaudoin J., Bergeron P., Nadeau A., Grondin G.;
RT   "Cell-specific expression of the ZPK gene in adult mouse tissues.";
RL   DNA Cell Biol. 15:631-642(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon, Embryonic head, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION, AND MUTAGENESIS OF LYS-185 AND GLU-192.
RX   MEDLINE=96279269; PubMed=8663324; DOI=10.1074/jbc.271.28.16888;
RA   Mata M., Merritt S.E., Fan G., Yu G.G., Holzman L.B.;
RT   "Characterization of dual leucine zipper-bearing kinase, a mixed
RT   lineage kinase present in synaptic terminals whose phosphorylation
RT   state is regulated by membrane depolarization via calcineurin.";
RL   J. Biol. Chem. 271:16888-16896(1996).
CC   -!- FUNCTION: May be an activator of the JNK/SAPK pathway.
CC       Phosphorylates beta-casein, histone 1 and myelin basic protein in
CC       vitro.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium.
CC   -!- SUBUNIT: Interacts with MBIP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, kidney, lung, heart,
CC       testis, gastrointestinal tract, stomach, liver and pancreas.
CC       Within the nervous system, predominantly expressed in neurons and
CC       enriched in synaptic terminals.
CC   -!- DOMAIN: Interacts with MBIP through the leucine-zipper motif (By
CC       similarity).
CC   -!- PTM: Autophosphorylated on Ser/Thr. Phosphorylated in cytosol
CC       under basal conditions and dephosphorylated when membrane-
CC       associated.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U14636; AAA57280.1; -; mRNA.
DR   EMBL; U23789; AAB17123.1; -; mRNA.
DR   EMBL; AK029882; BAC26658.1; -; mRNA.
DR   EMBL; AK034374; BAC28689.1; -; mRNA.
DR   EMBL; AK081623; BAC38274.1; -; mRNA.
DR   EMBL; AK166435; BAE38775.1; -; mRNA.
DR   EMBL; BC047158; AAH47158.1; -; mRNA.
DR   EMBL; BC057572; AAH57572.1; -; mRNA.
DR   IPI; IPI00120072; -.
DR   PIR; A55318; A55318.
DR   RefSeq; NP_001157115.1; NM_001163643.1.
DR   RefSeq; NP_033608.3; NM_009582.4.
DR   UniGene; Mm.172897; -.
DR   ProteinModelPortal; Q60700; -.
DR   SMR; Q60700; 151-398.
DR   MINT; MINT-126821; -.
DR   STRING; Q60700; -.
DR   PhosphoSite; Q60700; -.
DR   PRIDE; Q60700; -.
DR   Ensembl; ENSMUST00000023812; ENSMUSP00000023812; ENSMUSG00000023050.
DR   GeneID; 26404; -.
DR   KEGG; mmu:26404; -.
DR   UCSC; uc007xwc.1; mouse.
DR   CTD; 26404; -.
DR   MGI; MGI:1346881; Map3k12.
DR   eggNOG; roNOG11442; -.
DR   GeneTree; ENSGT00600000084040; -.
DR   HOGENOM; HBG447061; -.
DR   HOVERGEN; HBG052383; -.
DR   InParanoid; Q60700; -.
DR   OMA; TGREGTS; -.
DR   OrthoDB; EOG4G4GPV; -.
DR   PhylomeDB; Q60700; -.
DR   BRENDA; 2.7.11.25; 244.
DR   NextBio; 304373; -.
DR   ArrayExpress; Q60700; -.
DR   Bgee; Q60700; -.
DR   CleanEx; MM_MAP3K12; -.
DR   Genevestigator; Q60700; -.
DR   GermOnline; ENSMUSG00000023050; Mus musculus.
DR   GO; GO:0033267; C:axon part; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0030426; C:growth cone; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:EC.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0016572; P:histone phosphorylation; IDA:UniProtKB.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR017419; MAP3K12_MAP3K13.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PIRSF; PIRSF038165; MAPKKK12_MAPKKK13; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Kinase; Magnesium; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Repeat;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    888       Mitogen-activated protein kinase kinase
FT                                kinase 12.
FT                                /FTId=PRO_0000086262.
FT   DOMAIN      158    399       Protein kinase.
FT   DOMAIN      423    444       Leucine-zipper 1.
FT   DOMAIN      476    497       Leucine-zipper 2.
FT   NP_BIND     164    172       ATP (By similarity).
FT   COMPBIAS     56     62       Poly-Gly.
FT   COMPBIAS    668    671       Poly-Pro.
FT   COMPBIAS    698    701       Poly-Pro.
FT   COMPBIAS    753    764       Glu-rich (acidic).
FT   ACT_SITE    269    269       Proton acceptor (By similarity).
FT   BINDING     185    185       ATP.
FT   MOD_RES     667    667       Phosphoserine (By similarity).
FT   MOD_RES     790    790       Phosphoserine (By similarity).
FT   MUTAGEN     185    185       K->A: Loss of catalytic activity.
FT   MUTAGEN     192    192       E->A: No change.
FT   CONFLICT     18     18       V -> A (in Ref. 2; AAB17123).
FT   CONFLICT     28     29       KL -> NV (in Ref. 2; AAB17123).
FT   CONFLICT    218    218       C -> S (in Ref. 3; BAC26658).
FT   CONFLICT    382    382       S -> T (in Ref. 2; AAB17123).
FT   CONFLICT    392    392       Q -> K (in Ref. 3; BAC28689).
FT   CONFLICT    494    495       EQ -> DE (in Ref. 2; AAB17123).
FT   CONFLICT    517    517       N -> D (in Ref. 2; AAB17123).
FT   CONFLICT    794    794       E -> G (in Ref. 2; AAB17123).
SQ   SEQUENCE   888 AA;  96084 MW;  CFECF1D34F889ABB CRC64;
     MACLHETRTP SPSFGGFVST LSEASMRKLD PDTSDCTPEK DLTPTQCVLR DVVPLGGQGG
     GGPSPSPGGE PPPEPFANSV LQLHEQDTGG PGGATGSPES RASRVRADEV RLQCQSGSGF
     LEGLFGCLRP VWTMIGKAYS TEHKQQQEDL WEVPFEEILD LQWVGSGAQG AVFLGRFHGE
     EVAVKKVRDL KETDIKHLRK LKHPNIITFK GVCTQAPCYC ILMEFCAQGQ LYEVLRAGRP
     VTPSLLVDWS MGIAGGMNYL HLHKIIHRDL KSPNMLITYD DVVKISDFGT SKELSDKSTK
     MSFAGTVAWM APEVIRNEPV SEKVDIWSFG VVLWELLTGE IPYKDVDSSA IIWGVGSNSL
     HLPVPSSCPD GFKILLRQCW NSKPRNRPSF RQILLHLDIA SADVLSTPQE TYFKSQAEWR
     EEVKLHFEKI KSEGTCLHRL EEELVMRRRE ELRHALDIRE HYERKLERAN NLYMELNALM
     LQLELKEREL LRREQALERR CPGLLKSHPS RGLLHGNTME KLIKKRNVPQ KLSPHSKRPD
     ILKTESLLPK LDAALSGVGL PGCPKGPPSP GRSRRGKTRH RKASAKGSCG DLPGLRAALP
     PHEPGGLGSP GGLGVGPSAW DACPPALRGL HHDLLLRKMS SSSPDLLSAA LGARGRGATG
     GARDPGSPPP PQGDTPPSEG SAPGSTSPDS PGGAKGEPPP PVGPGEGVGL LGTGREGTAG
     RGGNRAGSQH LTPAALLYRA AVTRSQKRGI SSEEEEGEVD SEVELPPSQR WPQGPNMRQS
     LSTFSSENPS DVEEGTASEP SPSGTPEVGS TNTDERPDER SDDMCSQGSE IPLDLPTSEV
     VPEREASSLP MQHQDGQGPN PEDSDCDSTE LDNSNSIDAL RPPASLPP
//
ID   ZNT1_MOUSE              Reviewed;         503 AA.
AC   Q60738;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Zinc transporter 1;
DE            Short=ZnT-1;
DE   AltName: Full=Solute carrier family 30 member 1;
GN   Name=Slc30a1; Synonyms=Znt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Brain;
RX   MEDLINE=95188868; PubMed=7882967;
RA   Palmiter R.D., Findley S.D.;
RT   "Cloning and functional characterization of a mammalian zinc
RT   transporter that confers resistance to zinc.";
RL   EMBO J. 14:639-649(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in zinc transport out of the cell.
CC       Lethality of knockout early in gestation suggests a role of the
CC       protein in fetal zinc acquisition and retention.
CC   -!- SUBUNIT: Multimer (Probable).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Probable).
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC       transporter (TC 2.A.4) family. SLC30A subfamily.
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DR   EMBL; U17132; AAA79233.1; -; Genomic_DNA.
DR   EMBL; BC052166; AAH52166.1; -; mRNA.
DR   IPI; IPI00120166; -.
DR   PIR; S54302; S54302.
DR   RefSeq; NP_033605.1; NM_009579.3.
DR   UniGene; Mm.9024; -.
DR   ProteinModelPortal; Q60738; -.
DR   STRING; Q60738; -.
DR   PhosphoSite; Q60738; -.
DR   PRIDE; Q60738; -.
DR   Ensembl; ENSMUST00000044954; ENSMUSP00000042410; ENSMUSG00000037434.
DR   GeneID; 22782; -.
DR   KEGG; mmu:22782; -.
DR   UCSC; uc007edc.1; mouse.
DR   CTD; 22782; -.
DR   MGI; MGI:1345281; Slc30a1.
DR   GeneTree; ENSGT00550000074381; -.
DR   HOGENOM; HBG317426; -.
DR   HOVERGEN; HBG000588; -.
DR   InParanoid; Q60738; -.
DR   OMA; RARLLCM; -.
DR   OrthoDB; EOG4GF3F3; -.
DR   PhylomeDB; Q60738; -.
DR   NextBio; 303351; -.
DR   ArrayExpress; Q60738; -.
DR   Bgee; Q60738; -.
DR   Genevestigator; Q60738; -.
DR   GermOnline; ENSMUSG00000037434; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019855; F:calcium channel inhibitor activity; IDA:BHF-UCL.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:BHF-UCL.
DR   GO; GO:0006882; P:cellular zinc ion homeostasis; IDA:BHF-UCL.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0090281; P:negative regulation of calcium ion import; IDA:BHF-UCL.
DR   GO; GO:0071584; P:negative regulation of zinc ion import; IDA:BHF-UCL.
DR   InterPro; IPR002524; Cation_efflux.
DR   PANTHER; PTHR11562; Cation_efflux; 1.
DR   Pfam; PF01545; Cation_efflux; 1.
DR   TIGRFAMs; TIGR01297; CDF; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Ion transport; Membrane; Phosphoprotein;
KW   Repeat; Transmembrane; Transmembrane helix; Transport; Zinc;
KW   Zinc transport.
FT   CHAIN         1    503       Zinc transporter 1.
FT                                /FTId=PRO_0000206092.
FT   TOPO_DOM      1     10       Cytoplasmic (Potential).
FT   TRANSMEM     11     31       Helical; (Potential).
FT   TOPO_DOM     32     35       Extracellular (Potential).
FT   TRANSMEM     36     56       Helical; (Potential).
FT   TOPO_DOM     57     78       Cytoplasmic (Potential).
FT   TRANSMEM     79     99       Helical; (Potential).
FT   TOPO_DOM    100    113       Extracellular (Potential).
FT   TRANSMEM    114    134       Helical; (Potential).
FT   TOPO_DOM    135    243       Cytoplasmic (Potential).
FT   TRANSMEM    244    264       Helical; (Potential).
FT   TOPO_DOM    265    303       Extracellular (Potential).
FT   TRANSMEM    304    324       Helical; (Potential).
FT   TOPO_DOM    325    503       Cytoplasmic (Potential).
FT   REGION      145    156       6 X 2 AA approximate repeats of H-G.
FT   MOD_RES     502    502       Phosphoserine (By similarity).
FT   CARBOHYD    294    294       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   503 AA;  54716 MW;  7C4FF93FC13CDA22 CRC64;
     MGCWGRNRGR LLCMLLLTFM FMVLEVVVSR VTASLAMLSD SFHMLSDVLA LVVALVAERF
     ARRTHATQKN TFGWIRAEVM GALVNAIFLT GLCFAILLEA VERFIEPHEM QQPLVVLSVG
     VAGLLVNVLG LCLFHHHSGE GQGAGHGHSH GHGHGHLAKG ARKAGRAGVE AGAPPGRAPD
     QEETNTLVAN TSNSNGLKAD QAEPEKLRSD DPVDVQVNGN LIQESDNLEA EDNRAGQLNM
     RGVFLHVLGD ALGSVIVVVN ALVFYFNWKG CTEDDFCTNP CFPDPCKSSV EIINSTQAPM
     RDAGPCWVLY LDPTLCIIMV CILLYTTYPL LKESALILLQ TVPKQIDIKH LVKELRDVDG
     VEEVHELHVW QLAGSRIIAT AHIKCEDPAS YMQVAKTIKD VFHNHGIHAT TIQPEFASVG
     SKSSVLPCEL ACRTQCALKQ CCGTRPQVHS GKDAEKAPTV SISCLELSEN LEKKARRTKA
     EGSLPAVVIE IKNVPNKQPE SSL
//
ID   KHDR1_MOUSE             Reviewed;         443 AA.
AC   Q60749; A2ACH3; B2KG38; Q3U8T3; Q60735; Q7M4N5; Q99M33;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 2.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=KH domain-containing, RNA-binding, signal transduction-associated protein 1;
DE   AltName: Full=GAP-associated tyrosine phosphoprotein p62;
DE   AltName: Full=Src-associated in mitosis 68 kDa protein;
DE            Short=Sam68;
DE   AltName: Full=p21 Ras GTPase-activating protein-associated p62;
DE   AltName: Full=p68;
GN   Name=Khdrbs1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 103-120 AND
RP   139-150.
RC   STRAIN=BALB/c X DBA/2; TISSUE=Dendritic cell;
RX   MEDLINE=95331638; PubMed=7541765; DOI=10.1016/0378-1119(95)00040-D;
RA   Agger R., Freimuth P.;
RT   "Purification and cDNA sequence of a murine protein homologous to the
RT   human p62 tyrosine phosphoprotein that associates with the Ras GTPase-
RT   activating protein p120 GAP.";
RL   Gene 158:307-308(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH FYN; GRB2 AND PLCG1.
RC   TISSUE=Thymus;
RX   MEDLINE=95097990; PubMed=7799925;
RA   Richard S., Yu D., Blumer K.J., Hausladen D., Olszowy M.W.,
RA   Connelly P.A., Shaw A.S.;
RT   "Association of p62, a multifunctional SH2- and SH3-domain-binding
RT   protein, with src family tyrosine kinases, Grb2, and phospholipase C
RT   gamma-1.";
RL   Mol. Cell. Biol. 15:186-197(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 57-71; 103-131; 139-152; 158-165; 222-230; 273-282
RP   AND 433-443, FUNCTION, PHOSPHORYLATION AT SER-113, AND INTERACTION
RP   WITH SRC.
RX   PubMed=7512695; DOI=10.1038/368871a0;
RA   Fumagalli S., Totty N.F., Hsuan J.J., Courtneidge S.A.;
RT   "A target for Src in mitosis.";
RL   Nature 368:871-874(1994).
RN   [7]
RP   FUNCTION, RNA-BINDING, AND HOMOOLIGOMERIZATION.
RX   PubMed=9315629;
RA   Chen T., Damaj B.B., Herrera C., Lasko P., Richard S.;
RT   "Self-association of the single-KH-domain family members Sam68, GRP33,
RT   GLD-1, and Qk1: role of the KH domain.";
RL   Mol. Cell. Biol. 17:5707-5718(1997).
RN   [8]
RP   INTERACTION WITH RBMY1A1.
RX   PubMed=10823932; DOI=10.1073/pnas.97.11.5717;
RA   Elliott D.J., Bourgeois C.F., Klink A., Stevenin J., Cooke H.J.;
RT   "A mammalian germ cell-specific RNA-binding protein interacts with
RT   ubiquitously expressed proteins involved in splice site selection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:5717-5722(2000).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CBP.
RX   PubMed=12496368;
RA   Hong W., Resnick R.J., Rakowski C., Shalloway D., Taylor S.J.,
RA   Blobel G.A.;
RT   "Physical and functional interaction between the transcriptional
RT   cofactor CBP and the KH domain protein Sam68.";
RL   Mol. Cancer Res. 1:48-55(2002).
RN   [10]
RP   INTERACTION WITH PRMT1.
RX   PubMed=12529443; DOI=10.1091/mbc.E02-08-0484;
RA   Cote J., Boisvert F.-M., Boulanger M.-C., Bedford M.T., Richard S.;
RT   "Sam68 RNA binding protein is an in vivo substrate for protein
RT   arginine N-methyltransferase 1.";
RL   Mol. Biol. Cell 14:274-287(2003).
CC   -!- FUNCTION: Recruited and tyrosine phosphorylated by several
CC       receptor systems, for example the T-cell, leptin and insulin
CC       receptors. Once phosphorylated, functions as an adapter protein in
CC       signal transduction cascades by binding to SH2 and SH3 domain-
CC       containing proteins. Role in G2-M progression in the cell cycle.
CC       Represses CBP-dependent transcriptional activation apparently by
CC       competing with other nuclear factors for binding to CBP. Also acts
CC       as a putative regulator of mRNA stability and/or translation rates
CC       and mediates mRNA nuclear export.
CC   -!- SUBUNIT: Self-associates to form homooligomers when bound to RNA,
CC       oligomerization appears to be limited when binding to proteins.
CC       Interacts with CBL, KHDRBS3, LCK, GRB2, JAK3, PIK3R1, PLCG1,
CC       PTPN6, RASA1, RBMY1A1 and STAT3. Interacts with PRMT1. Binds the
CC       WW domains of WBP4/FBP21, FNBP4/FBP30 and the SH3 domain of FYN
CC       through the Arg/Gly-rich-flanked Pro-rich regions. Forms a complex
CC       with ILF2, ILF3, YLPM1, RBMX, NCOA5 and PPP1CA (By similarity).
CC   -!- INTERACTION:
CC       P45481:Crebbp; NbExp=3; IntAct=EBI-519077, EBI-296306;
CC       P39688:Fyn; NbExp=4; IntAct=EBI-519077, EBI-524514;
CC       Q9JIF0:Prmt1; NbExp=2; IntAct=EBI-519077, EBI-519055;
CC       P12931:SRC (xeno); NbExp=1; IntAct=EBI-519077, EBI-621482;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Membrane.
CC   -!- DOMAIN: The KH domain is required for binding to RNA.
CC   -!- DOMAIN: The Pro-rich domains are flanked by Arg/Gly-rich motifs
CC       which can be asymmetric dimethylated on arginine residues to give
CC       the DMA/Gly-rich regions. Selective methylation on these motifs
CC       can modulate protein-protein interactions (By similarity).
CC   -!- PTM: Tyrosine phosphorylated by several non-receptor tyrosine
CC       kinases, for example LCK, FYN and JAK3.
CC   -!- PTM: Acetylated. Positively correlates with ability to bind RNA
CC       (By similarity).
CC   -!- PTM: Arginine methylation is required for nuclear localization.
CC       Inhibits interaction with Src-like SH3 domains, but not
CC       interaction with WW domains of WBP4/FBP21 AND FNBP4/FBP30 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the KHDRBS family.
CC   -!- SIMILARITY: Contains 1 KH domain.
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DR   EMBL; U17961; AAA86693.1; -; mRNA.
DR   EMBL; U17046; AAA64997.1; -; mRNA.
DR   EMBL; AK050520; BAC34303.1; -; mRNA.
DR   EMBL; AK152084; BAE30934.1; -; mRNA.
DR   EMBL; AL669834; CAM13766.1; -; Genomic_DNA.
DR   EMBL; CU210913; CAQ51789.1; -; Genomic_DNA.
DR   EMBL; BC002051; AAH02051.1; -; mRNA.
DR   IPI; IPI00458765; -.
DR   PIR; I49140; I49140.
DR   PIR; S43974; S43974.
DR   RefSeq; NP_035447.3; NM_011317.3.
DR   UniGene; Mm.8256; -.
DR   ProteinModelPortal; Q60749; -.
DR   SMR; Q60749; 98-135, 155-285.
DR   DIP; DIP-2861N; -.
DR   IntAct; Q60749; 27.
DR   STRING; Q60749; -.
DR   PhosphoSite; Q60749; -.
DR   PRIDE; Q60749; -.
DR   Ensembl; ENSMUST00000066257; ENSMUSP00000066516; ENSMUSG00000028790.
DR   GeneID; 20218; -.
DR   KEGG; mmu:20218; -.
DR   UCSC; uc008uyd.1; mouse.
DR   CTD; 20218; -.
DR   MGI; MGI:893579; Khdrbs1.
DR   eggNOG; roNOG09046; -.
DR   GeneTree; ENSGT00550000074434; -.
DR   HOGENOM; HBG713086; -.
DR   HOVERGEN; HBG079164; -.
DR   InParanoid; Q60749; -.
DR   OMA; VRQAPSR; -.
DR   OrthoDB; EOG4JHCGB; -.
DR   PhylomeDB; Q60749; -.
DR   NextBio; 297827; -.
DR   ArrayExpress; Q60749; -.
DR   Bgee; Q60749; -.
DR   Genevestigator; Q60749; -.
DR   GermOnline; ENSMUSG00000028790; Mus musculus.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0005070; F:SH3/SH2 adaptor activity; IPI:UniProtKB.
DR   GO; GO:0016564; F:transcription repressor activity; IDA:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0007166; P:cell surface receptor linked signaling pathway; IDA:UniProtKB.
DR   GO; GO:0046831; P:regulation of RNA export from nucleus; IDA:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR004088; KH_type_1.
DR   InterPro; IPR018111; KH_type_1_subgr.
DR   Pfam; PF00013; KH_1; 1.
DR   SMART; SM00322; KH; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell cycle; Direct protein sequencing; Membrane;
KW   Methylation; Nucleus; Phosphoprotein; RNA-binding; SH3-binding;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    443       KH domain-containing, RNA-binding, signal
FT                                transduction-associated protein 1.
FT                                /FTId=PRO_0000050125.
FT   DOMAIN      171    197       KH.
FT   COMPBIAS     34     41       Pro-rich.
FT   COMPBIAS     44     55       Arg/Gly-rich.
FT   COMPBIAS     59     89       Pro-rich.
FT   COMPBIAS    282    292       Arg/Gly-rich.
FT   COMPBIAS    295    301       Pro-rich.
FT   COMPBIAS    302    332       Arg/Gly-rich.
FT   COMPBIAS    334    363       Pro-rich.
FT   MOD_RES      15     15       Phosphoserine (By similarity).
FT   MOD_RES      18     18       Phosphoserine (By similarity).
FT   MOD_RES      20     20       Phosphoserine (By similarity).
FT   MOD_RES      29     29       Phosphoserine (By similarity).
FT   MOD_RES      33     33       Phosphothreonine (By similarity).
FT   MOD_RES      45     45       Omega-N-methylated arginine; by PRMT1 (By
FT                                similarity).
FT   MOD_RES      52     52       Omega-N-methylated arginine; by PRMT1 (By
FT                                similarity).
FT   MOD_RES      58     58       Phosphoserine (By similarity).
FT   MOD_RES     113    113       Phosphoserine.
FT   MOD_RES     175    175       N6-acetyllysine (By similarity).
FT   MOD_RES     291    291       Omega-N-methylated arginine; by PRMT1 (By
FT                                similarity).
FT   MOD_RES     304    304       Omega-N-methylated arginine; by PRMT1 (By
FT                                similarity).
FT   MOD_RES     310    310       Omega-N-methylated arginine; by PRMT1 (By
FT                                similarity).
FT   MOD_RES     315    315       Omega-N-methylated arginine; by PRMT1 (By
FT                                similarity).
FT   MOD_RES     320    320       Omega-N-methylated arginine; by PRMT1 (By
FT                                similarity).
FT   MOD_RES     325    325       Omega-N-methylated arginine; by PRMT1 (By
FT                                similarity).
FT   MOD_RES     331    331       Omega-N-methylated arginine; by PRMT1 (By
FT                                similarity).
FT   MOD_RES     340    340       Omega-N-methylated arginine; by PRMT1 (By
FT                                similarity).
FT   MOD_RES     346    346       Omega-N-methylated arginine; by PRMT1 (By
FT                                similarity).
FT   CONFLICT    104    104       L -> P (in Ref. 2; AAA64997).
FT   CONFLICT    147    147       D -> N (in Ref. 6; AA sequence).
FT   CONFLICT    174    174       G -> R (in Ref. 1; AAA86693).
FT   CONFLICT    197    197       V -> VS (in Ref. 1; AAA86693).
FT   CONFLICT    225    230       MDLHVF -> LGENGL (in Ref. 6; AA
FT                                sequence).
FT   CONFLICT    327    327       A -> S (in Ref. 1; AAA86693).
SQ   SEQUENCE   443 AA;  48371 MW;  D33DE960BEA9E5AA CRC64;
     MQRRDDPASR LTRSSGRSCS KDPSGAHPSV RLTPSRPSPL PHRPRGGGGG PRGGARASPA
     TQPPPLLPPS TPGPDATVVG SAPTPLLPPS ATAAVKMEPE NKYLPELMAE KDSLDPSFTH
     AMQLLSVEIE KIQKGESKKD DEENYLDLFS HKNMKLKERV LIPVKQYPKF NFVGKILGPQ
     GNTIKRLQEE TGAKISVLGK GSMRDKAKEE ELRKGGDPKY AHLNMDLHVF IEVFGPPCEA
     YALMAHAMEE VKKFLVPDMM DDICQEQFLE LSYLNGVPEP SRGRGVSVRG RGAAPPPPPV
     PRGRGVGPPR GALVRGTPVR GSITRGATVT RGVPPPPTVR GAPTPRARTA GIQRIPLPPT
     PAPETYEDYG YDDTYAEQSY EGYEGYYSQS QGESEYYDYG HGELQDSYEA YGQDDWNGTR
     PSLKAPPARP VKGAYREHPY GRY
//
ID   TNAP3_MOUSE             Reviewed;         775 AA.
AC   Q60769;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Tumor necrosis factor alpha-induced protein 3;
DE            Short=TNF alpha-induced protein 3;
DE            EC=3.4.19.12;
DE            EC=6.3.2.-;
DE   AltName: Full=Putative DNA-binding protein A20;
DE   AltName: Full=Zinc finger protein A20;
GN   Name=Tnfaip3; Synonyms=Tnfip3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=95138513; PubMed=7836754;
RA   Tewari M., Wolf F.W., Seldin M.F., O'Shea K.S., Dixit V.M.,
RA   Turka L.A.;
RT   "Lymphoid expression and regulation of A20, an inhibitor of programmed
RT   cell death.";
RL   J. Immunol. 154:1699-1706(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   MEDLINE=99315915; PubMed=10385526; DOI=10.1083/jcb.145.7.1471;
RA   Heyninck K., De Valck D., Vanden Berghe W., Van Criekinge W.,
RA   Contreras R., Fiers W., Haegeman G., Beyaert R.;
RT   "The zinc finger protein A20 inhibits TNF-induced NF-B-dependent gene
RT   expression by interfering with an RIP- or TRAF2-mediated
RT   transactivation signal and directly binds to a novel NF-B-inhibiting
RT   protein ABIN.";
RL   J. Cell Biol. 145:1471-1482(1999).
RN   [3]
RP   INTERACTION WITH TAX1BP1; RNF11 AND RIPK1.
RX   PubMed=19131965; DOI=10.1038/emboj.2008.285;
RA   Shembade N., Parvatiyar K., Harhaj N.S., Harhaj E.W.;
RT   "The ubiquitin-editing enzyme A20 requires RNF11 to downregulate NF-
RT   kappaB signalling.";
RL   EMBO J. 28:513-522(2009).
CC   -!- FUNCTION: Ubiquitin-editing enzyme that contains both ubiquitin
CC       ligase and deubiquitinase activities. Essential component of a
CC       ubiquitin-editing protein complex, comprising also RNF11, ITCH and
CC       TAX1BP1, that ensures the transient nature of inflammatory
CC       signaling pathways. Upon TNF stimulation, deubiquitinates 'Lys-
CC       63'-polyubiquitin chains on RIPK1 and catalyzes the formation of
CC       'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteosomal
CC       degradation and consequently termination of the TNF- or LPS-
CC       mediated activation of NF-kappa-B. In vitro able to deubiquitinate
CC       both 'Lys-48'- and 'Lys-63' polyubiquitin chains. Inhibitor of
CC       programmed cell death. Has a role in the function of the lymphoid
CC       system.
CC   -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- SUBUNIT: Homodimer. Interacts with NAF1, TAX1BP1 and TRAF2.
CC       Interacts with RNF11, ITCH and TAX1BP1 only after TNF stimulation;
CC       these interaction are transient and they are lost after 1 hour of
CC       stimulation with TNF (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Found in most tissues during development.
CC       Strikingly high levels are found in lymphoid organs, including the
CC       thymus, spleen, and gut-associated lymphoid tissue. Constitutively
CC       expressed in immature and mature thymocyte subpopulations as well
CC       as in resting peripheral T-cells; activation of these leads to
CC       down-regulation.
CC   -!- INDUCTION: By cytokines. TNF-alpha may regulate expression in the
CC       thymus.
CC   -!- DOMAIN: The A20-type zinc fingers mediate the ubiquitin ligase
CC       activity (By similarity).
CC   -!- DOMAIN: The OTU domain mediates the deubiquitinase activity (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the peptidase C64 family.
CC   -!- SIMILARITY: Contains 7 A20-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 OTU domain.
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DR   EMBL; U19463; AAC52153.1; -; mRNA.
DR   IPI; IPI00120270; -.
DR   PIR; I49237; I49237.
DR   UniGene; Mm.116683; -.
DR   ProteinModelPortal; Q60769; -.
DR   SMR; Q60769; 3-362, 382-419, 588-620, 743-775.
DR   IntAct; Q60769; 2.
DR   STRING; Q60769; -.
DR   MEROPS; C64.003; -.
DR   PhosphoSite; Q60769; -.
DR   PRIDE; Q60769; -.
DR   Ensembl; ENSMUST00000019997; ENSMUSP00000019997; ENSMUSG00000019850.
DR   Ensembl; ENSMUST00000105527; ENSMUSP00000101167; ENSMUSG00000019850.
DR   MGI; MGI:1196377; Tnfaip3.
DR   HOGENOM; HBG444017; -.
DR   HOVERGEN; HBG059260; -.
DR   InParanoid; Q60769; -.
DR   OrthoDB; EOG4XD3QK; -.
DR   ArrayExpress; Q60769; -.
DR   Bgee; Q60769; -.
DR   CleanEx; MM_TNFAIP3; -.
DR   Genevestigator; Q60769; -.
DR   GermOnline; ENSMUSG00000019850; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; ISS:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0004843; F:ubiquitin-specific protease activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB cascade; ISS:UniProtKB.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
DR   InterPro; IPR003323; OTU.
DR   InterPro; IPR002653; Znf_A20.
DR   Pfam; PF02338; OTU; 1.
DR   Pfam; PF01754; zf-A20; 6.
DR   SMART; SM00259; ZnF_A20; 7.
DR   PROSITE; PS50802; OTU; 1.
DR   PROSITE; PS51036; ZF_A20; 7.
PE   1: Evidence at protein level;
KW   Apoptosis; Cytoplasm; DNA-binding; Hydrolase; Ligase; Metal-binding;
KW   Multifunctional enzyme; Nucleus; Phosphoprotein; Protease; Repeat;
KW   Thiol protease; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    775       Tumor necrosis factor alpha-induced
FT                                protein 3.
FT                                /FTId=PRO_0000188793.
FT   DOMAIN       92    263       OTU.
FT   REPEAT      286    317       1.
FT   REPEAT      324    356       2.
FT   ZN_FING     381    416       A20-type 1.
FT   ZN_FING     464    499       A20-type 2.
FT   ZN_FING     500    533       A20-type 3.
FT   ZN_FING     586    621       A20-type 4.
FT   ZN_FING     636    671       A20-type 5.
FT   ZN_FING     695    730       A20-type 6.
FT   ZN_FING     741    775       A20-type 7.
FT   REGION       58    300       TRAF-binding (By similarity).
FT   REGION      157    159       Interaction with ubiquitin (By
FT                                similarity).
FT   REGION      190    192       Interaction with ubiquitin (By
FT                                similarity).
FT   REGION      224    227       Interaction with ubiquitin (By
FT                                similarity).
FT   REGION      286    356       2 X approximate repeats.
FT   REGION      369    775       Interaction with NAF1.
FT   ACT_SITE    103    103       Nucleophile (By similarity).
FT   ACT_SITE    256    256       Proton acceptor (By similarity).
FT   MOD_RES     451    451       Phosphoserine (By similarity).
SQ   SEQUENCE   775 AA;  87596 MW;  86349D68D7A6B2E8 CRC64;
     MAEQLLPQAL YLSNMRKAVK IRERTPEDIF KPTNGIIYHF KTMHRYTLEM FRTCQFCPQF
     REIIHKALID RSVQASLESQ KKLNWCREVR KLVALKTNGD GNCLMHAACQ YMWGVQDTDL
     VLRKALCSTL KETDTRNFKF RWQLESLKSQ EFVETGLCYD TRNWNDEWDN LVKMASADTP
     AARSGLQYNS LEEIHIFVLS NILRRPIIVI SDKMLRSLES GSNFAPLKVG GIYLPLHWPA
     QECYRYPIVL GYDSQHFVPL VTLKDSGPEL RAVPLVNRDR GRFEDLKVHF LTDPENEMKE
     KLLKEYLIVM EIPVQGWDHG TTHLINAAKL DEANLPKEIN LVDDYFELVQ HEYKKWQENS
     DQARRAAHAQ NPLEPSTPQL SLMDIKCETP NCPFFMSVNT QPLCHECSER RQKNQSKLPK
     LNSKLGPEGL PGVGLGSSNW SPEETAGGPH SAPPTAPSLF LFSETTAMKC RSPGCPFTLN
     VQHNGFCERC HARQINASHT ADPGKCQACL QDVTRTFNGI CSTCFKRTTA EPSSSLTSSI
     PASCHQRSKS DPSQLIQSLT PHSCHRTGNV SPSGCLSQAA RTPGDRAGTS KCRKAGCMYF
     GTPENKGFCT LCFIEYRENK QSVTASAKAG SPAPRFQNNV PCLGRECGTL GSTMFEGYCQ
     KCFIEAQNQR FHEARRTEEQ LRSSQHRDMP RTTQVASRLK CARASCKNIL ACRSEELCME
     CQHLSQRVGS VAHRGEPTPE EPPKQRCRAP ACDHFGNAKC NGYCNECYQF KQMYG
//
ID   CLD11_MOUSE             Reviewed;         207 AA.
AC   Q60771; Q545N5; Q9DB65;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Claudin-11;
DE   AltName: Full=Oligodendrocyte transmembrane protein;
DE   AltName: Full=Oligodendrocyte-specific protein;
GN   Name=Cldn11; Synonyms=Osp, Otm;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96390492; PubMed=8797478;
RA   Bronstein J.M., Popper P., Micevych P.E., Farber D.B.;
RT   "Isolation and characterization of a novel oligodendrocyte-specific
RT   protein.";
RL   Neurology 47:772-778(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   MEDLINE=99242612; PubMed=10225958; DOI=10.1083/jcb.145.3.579;
RA   Morita K., Furuse M., Tsukita S.;
RT   "Claudin-11/OSP-based tight junctions of myelin sheaths in brain and
RT   Sertoli cells in testis.";
RL   J. Cell Biol. 145:579-588(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 190-203, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   INTERACTION WITH TSPAN3.
RX   MEDLINE=21206015; PubMed=11309411; DOI=10.1083/jcb.153.2.295;
RA   Tiwari-Woodruff S.K., Buznikov A.G., Vu T.Q., Micevych P.E., Chen K.,
RA   Kornblum H.I., Bronstein J.M.;
RT   "OSP/claudin-11 forms a complex with a novel member of the tetraspanin
RT   super family and beta1 integrin and regulates proliferation and
RT   migration of oligodendrocytes.";
RL   J. Cell Biol. 153:295-306(2001).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND SER-198, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Plays a major role in tight junction-specific
CC       obliteration of the intercellular space, through calcium-
CC       independent cell-adhesion activity (By similarity).
CC   -!- SUBUNIT: Interacts with tetraspanin-3/TSPAN3.
CC   -!- INTERACTION:
CC       P07141:Csf1; NbExp=1; IntAct=EBI-309095, EBI-777188;
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction. Cell
CC       membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the claudin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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DR   EMBL; U19582; AAB50270.1; -; mRNA.
DR   EMBL; AF124426; AAD17321.1; -; mRNA.
DR   EMBL; AK005088; BAB23810.1; -; mRNA.
DR   EMBL; AK005171; BAB23860.1; -; mRNA.
DR   EMBL; AK161698; BAE36538.1; -; mRNA.
DR   EMBL; BC021659; AAH21659.1; -; mRNA.
DR   IPI; IPI00120295; -.
DR   RefSeq; NP_032796.1; NM_008770.3.
DR   UniGene; Mm.4425; -.
DR   IntAct; Q60771; 3.
DR   MINT; MINT-217520; -.
DR   STRING; Q60771; -.
DR   PhosphoSite; Q60771; -.
DR   PRIDE; Q60771; -.
DR   Ensembl; ENSMUST00000046174; ENSMUSP00000042181; ENSMUSG00000037625.
DR   GeneID; 18417; -.
DR   KEGG; mmu:18417; -.
DR   UCSC; uc008ovw.1; mouse.
DR   CTD; 18417; -.
DR   MGI; MGI:106925; Cldn11.
DR   eggNOG; roNOG14387; -.
DR   GeneTree; ENSGT00560000077244; -.
DR   HOGENOM; HBG716859; -.
DR   HOVERGEN; HBG102313; -.
DR   InParanoid; Q60771; -.
DR   OMA; VILCCAG; -.
DR   OrthoDB; EOG46HGBS; -.
DR   PhylomeDB; Q60771; -.
DR   NextBio; 294056; -.
DR   ArrayExpress; Q60771; -.
DR   Bgee; Q60771; -.
DR   CleanEx; MM_CLDN11; -.
DR   Genevestigator; Q60771; -.
DR   GermOnline; ENSMUSG00000037625; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:MGI.
DR   GO; GO:0005923; C:tight junction; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0008366; P:axon ensheathment; IMP:MGI.
DR   GO; GO:0016338; P:calcium-independent cell-cell adhesion; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   InterPro; IPR006187; Claudin.
DR   InterPro; IPR003555; Claudin11.
DR   InterPro; IPR017974; Claudin_CS.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   PANTHER; PTHR12002; Claudin; 1.
DR   PANTHER; PTHR12002:SF6; Claudin11; 1.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01077; CLAUDIN.
DR   PRINTS; PR01384; CLAUDIN11.
DR   PROSITE; PS01346; CLAUDIN; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Direct protein sequencing; Membrane;
KW   Phosphoprotein; Tight junction; Transmembrane; Transmembrane helix.
FT   CHAIN         1    207       Claudin-11.
FT                                /FTId=PRO_0000144762.
FT   TOPO_DOM      1      1       Cytoplasmic (Potential).
FT   TRANSMEM      2     22       Helical; (Potential).
FT   TOPO_DOM     23     82       Extracellular (Potential).
FT   TRANSMEM     83    103       Helical; (Potential).
FT   TOPO_DOM    104    122       Cytoplasmic (Potential).
FT   TRANSMEM    123    143       Helical; (Potential).
FT   TOPO_DOM    144    157       Extracellular (Potential).
FT   TRANSMEM    158    178       Helical; (Potential).
FT   TOPO_DOM    179    207       Cytoplasmic (Potential).
FT   MOD_RES     197    197       Phosphoserine.
FT   MOD_RES     198    198       Phosphoserine.
FT   CONFLICT    196    196       S -> C (in Ref. 3; BAB23860).
SQ   SEQUENCE   207 AA;  22114 MW;  A3F936F15958F27B CRC64;
     MVATCLQVVG FVTSFVGWIG IIVTTSTNDW VVTCSYTIPT CRKMDELGSK GLWADCVMAT
     GLYHCKPLVD ILILPGYVQA CRALMIAASV LGLPAILLLL TVLPCIRMGH EPGVAKYRRA
     QLAGVLLILL ALCAIVATIW FPVCAHREIT IVSFGYSLYA GWIGAVMCLV GGCVIVCCSG
     DAQSFGENRF YYSSGSSSPT HAKSAHV
//
ID   RASA3_MOUSE             Reviewed;         834 AA.
AC   Q60790;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   11-JAN-2011, entry version 78.
DE   RecName: Full=Ras GTPase-activating protein 3;
DE   AltName: Full=GAP1(IP4BP);
DE   AltName: Full=GapIII;
DE   AltName: Full=Ins P4-binding protein;
GN   Name=Rasa3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=96058749; PubMed=7500386; DOI=10.1002/jnr.490410615;
RA   Baba H., Fuss B., Urano J., Poullet P., Watson J.B., Tamanoi F.,
RA   Macklin W.B.;
RT   "GapIII, a new brain-enriched member of the GTPase-activating protein
RT   family.";
RL   J. Neurosci. Res. 41:846-858(1995).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-66, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-809, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. May
CC       bind inositol tetrakisphosphate (IP4).
CC   -!- TISSUE SPECIFICITY: High levels in brain, lower in spleen and
CC       lung.
CC   -!- SIMILARITY: Contains 1 Btk-type zinc finger.
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 Ras-GAP domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U20238; AAA93008.1; -; mRNA.
DR   IPI; IPI00468396; -.
DR   UniGene; Mm.18517; -.
DR   ProteinModelPortal; Q60790; -.
DR   SMR; Q60790; 11-268, 274-568, 573-713.
DR   STRING; Q60790; -.
DR   PhosphoSite; Q60790; -.
DR   PRIDE; Q60790; -.
DR   Ensembl; ENSMUST00000033833; ENSMUSP00000033833; ENSMUSG00000031453.
DR   MGI; MGI:1197013; Rasa3.
DR   HOVERGEN; HBG055643; -.
DR   ArrayExpress; Q60790; -.
DR   Bgee; Q60790; -.
DR   CleanEx; MM_RASA3; -.
DR   Genevestigator; Q60790; -.
DR   GermOnline; ENSMUSG00000031453; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001936; RasGAP.
DR   InterPro; IPR023152; RasGAP_CS.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR001562; Znf_Btk_motif.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.10.506.10; RasGAP; 1.
DR   Pfam; PF00779; BTK; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00616; RasGAP; 1.
DR   SMART; SM00107; BTK; 1.
DR   SMART; SM00239; C2; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00323; RasGAP; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR   PROSITE; PS51113; ZF_BTK; 1.
PE   1: Evidence at protein level;
KW   GTPase activation; Metal-binding; Phosphoprotein; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    834       Ras GTPase-activating protein 3.
FT                                /FTId=PRO_0000056643.
FT   DOMAIN        1     96       C2 1.
FT   DOMAIN      132    247       C2 2.
FT   DOMAIN      330    524       Ras-GAP.
FT   DOMAIN      576    677       PH.
FT   ZN_FING     679    715       Btk-type.
FT   MOD_RES      66     66       Phosphotyrosine.
FT   MOD_RES      77     77       Phosphoserine (By similarity).
FT   MOD_RES     110    110       Phosphothreonine (By similarity).
FT   MOD_RES     765    765       Phosphotyrosine (By similarity).
FT   MOD_RES     809    809       Phosphoserine.
SQ   SEQUENCE   834 AA;  96009 MW;  8676B07CAB786018 CRC64;
     MAVEEEGLRV FQSVRIKIGE AKNLPSYPGP NKMRDCYCTV NLDQEEVFRT KIVEKSLCPF
     YGEDFYCEIP RSFRHLSFYI FDRDVFRRDS IIGKVAIQKE DLQRYHNRDT WFQLQHVDAD
     SEVQGKVHLE LRLSEVITHT GVVCHKLAAR IFECQGLPIV NGQCDPYATV TLAGPFRSEA
     KKTKVKKKTN NPQFDEVFYF EVTRPCSYSK KSHFDFEEED VDKLEIRVDL WNASNLKFGD
     EFLGELRLPL KILRHSSSYE AWYFLQPRDN GNKSLKPDDL GSLRLNVVYT EDHVFSSEYY
     SPLRDLLLKS ADVEPVSASA AHILGEVCRD KQEAAIPLVR LLLHYGRVVP FISAIASAEV
     KRTQDPNTIF RGNSLTSKCI DETMKLAGMH YLHVTLKPTI EEICQSHKSC EIDPVKLKDG
     ENLENNMESL RQYVDRIFTV ITKSGVSCPT VMCDIFFSLR EAAAKRFQDD LDVRYTAVSS
     FIFLRFFAPA ILSPNLFQLT PHHTDPQTSR TLTLISKTIQ TLGSLSKSKS ASFKESYMAT
     FYEFFNEQKY ADAVKNFLDL ISSSGRRDPK SIEQPILLKE GFMIKRAQGR KRFGMKNFKK
     RWFRLTNHEF TYQKSKGDQP LCNIPIENIL AVERLEEESF RMKNMFQVIQ PERALYIQAN
     NCVEAKDWID ILTKVSQCNQ KRLTVFHPSA YLNGHWLCCR ASSDTAAGCT PCTGGLPANI
     QLDIDGDRET ERIYSLFNLY MGKLEKMQEA CGSKSVYDGP EQEEYSTFVI DDPQETYKTL
     KQVIAGVGTL EQEHAQYRRD KFKKTRYGSQ EHPIGDKSFQ NYIRQQSEIS THSI
//
ID   TRAF3_MOUSE             Reviewed;         567 AA.
AC   Q60803; Q62380;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 105.
DE   RecName: Full=TNF receptor-associated factor 3;
DE   AltName: Full=CD40 receptor-associated factor 1;
DE            Short=CRAF1;
DE   AltName: Full=TRAFAMN;
GN   Name=Traf3; Synonyms=Craf1, Trafamn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH TNFRSF5.
RX   MEDLINE=95184010; PubMed=7533327; DOI=10.1126/science.7533327;
RA   Cheng G., Cleary A.M., Ye Z.S., Hong D.I., Lederman S., Baltimore D.;
RT   "Involvement of CRAF1, a relative of TRAF, in CD40 signaling.";
RL   Science 267:1494-1498(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   MEDLINE=96299439; PubMed=8660894; DOI=10.1006/dbio.1996.0162;
RA   Wang X., Bornslaeger E.A., Haub O., Tomihara-Newberger C., Lonberg N.,
RA   Dinulos M.B., Disteche C.M., Copeland N.G., Gilbert D.J.,
RA   Jenkins N.A., Lacy E.;
RT   "A candidate gene for the amnionless gastrulation stage mouse mutation
RT   encodes a TRAF-related protein.";
RL   Dev. Biol. 177:274-290(1996).
RN   [3]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=8934568; DOI=10.1016/S1074-7613(00)80497-5;
RA   Xu Y., Cheng G., Baltimore D.;
RT   "Targeted disruption of TRAF3 leads to postnatal lethality and
RT   defective T-dependent immune responses.";
RL   Immunity 5:407-415(1996).
RN   [4]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=17015635; DOI=10.1084/jem.20061166;
RA   He J.Q., Zarnegar B., Oganesyan G., Saha S.K., Yamazaki S.,
RA   Doyle S.E., Dempsey P.W., Cheng G.;
RT   "Rescue of TRAF3-null mice by p100 NF-kappa B deficiency.";
RL   J. Exp. Med. 203:2413-2418(2006).
RN   [5]
RP   FUNCTION, INTERACTION WITH MYD88, AND IDENTIFICATION IN A COMPLEX WITH
RP   TRAF6.
RX   PubMed=16306937; DOI=10.1038/nature04369;
RA   Hacker H., Redecke V., Blagoev B., Kratchmarova I., Hsu L.C.,
RA   Wang G.G., Kamps M.P., Raz E., Wagner H., Hacker G., Mann M.,
RA   Karin M.;
RT   "Specificity in Toll-like receptor signalling through distinct
RT   effector functions of TRAF3 and TRAF6.";
RL   Nature 439:204-207(2006).
RN   [6]
RP   INTERACTION WITH TICAM1, AND FUNCTION.
RX   PubMed=16306936; DOI=10.1038/nature04374;
RA   Oganesyan G., Saha S.K., Guo B., He J.Q., Shahangian A., Zarnegar B.,
RA   Perry A., Cheng G.;
RT   "Critical role of TRAF3 in the Toll-like receptor-dependent and
RT   -independent antiviral response.";
RL   Nature 439:208-211(2006).
RN   [7]
RP   FUNCTION, DOMAIN, INTERACTION WITH MAP3K14, AND MUTAGENESIS OF CYS-52;
RP   CYS-55; CYS-67 AND HIS-69.
RX   PubMed=17158868; DOI=10.1074/jbc.M610271200;
RA   He J.Q., Saha S.K., Kang J.R., Zarnegar B., Cheng G.;
RT   "Specificity of TRAF3 in its negative regulation of the noncanonical
RT   NF-kappa B pathway.";
RL   J. Biol. Chem. 282:3688-3694(2007).
RN   [8]
RP   FUNCTION.
RX   PubMed=18313334; DOI=10.1016/j.immuni.2008.01.009;
RA   Gardam S., Sierro F., Basten A., Mackay F., Brink R.;
RT   "TRAF2 and TRAF3 signal adapters act cooperatively to control the
RT   maturation and survival signals delivered to B cells by the BAFF
RT   receptor.";
RL   Immunity 28:391-401(2008).
RN   [9]
RP   INTERACTION WITH TRAFD1.
RX   PubMed=18849341; DOI=10.1074/jbc.M806923200;
RA   Sanada T., Takaesu G., Mashima R., Yoshida R., Kobayashi T.,
RA   Yoshimura A.;
RT   "FLN29 deficiency reveals its negative regulatory role in the Toll-
RT   like receptor (TLR) and retinoic acid-inducible gene I (RIG-I)-like
RT   helicase signaling pathway.";
RL   J. Biol. Chem. 283:33858-33864(2008).
RN   [10]
RP   FUNCTION, DISRUPTION PHENOTYPE, IDENTIFICATION IN A COMPLEX WITH
RP   TRAF2; BIRC3 AND MAP3K14, UBIQUITINATION, AND TISSUE SPECIFICITY.
RX   PubMed=18997792; DOI=10.1038/ni.1678;
RA   Vallabhapurapu S., Matsuzawa A., Zhang W., Tseng P.H., Keats J.J.,
RA   Wang H., Vignali D.A., Bergsagel P.L., Karin M.;
RT   "Nonredundant and complementary functions of TRAF2 and TRAF3 in a
RT   ubiquitination cascade that activates NIK-dependent alternative NF-
RT   kappaB signaling.";
RL   Nat. Immunol. 9:1364-1370(2008).
RN   [11]
RP   FUNCTION, AND INTERACTION WITH MAP3K14.
RX   PubMed=18997794; DOI=10.1038/ni.1676;
RA   Zarnegar B.J., Wang Y., Mahoney D.J., Dempsey P.W., Cheung H.H.,
RA   He J., Shiba T., Yang X., Yeh W.C., Mak T.W., Korneluk R.G., Cheng G.;
RT   "Noncanonical NF-kappaB activation requires coordinated assembly of a
RT   regulatory complex of the adaptors cIAP1, cIAP2, TRAF2 and TRAF3 and
RT   the kinase NIK.";
RL   Nat. Immunol. 9:1371-1378(2008).
RN   [12]
RP   FUNCTION.
RX   PubMed=19228877; DOI=10.1093/intimm/dxp013;
RA   Jabara H.H., Weng Y., Sannikova T., Geha R.S.;
RT   "TRAF2 and TRAF3 independently mediate Ig class switching driven by
RT   CD40.";
RL   Int. Immunol. 21:477-488(2009).
RN   [13]
RP   FUNCTION, E3 PROTEIN-UBIQUITIN LIGASE ACTIVITY, MUTAGENESIS OF CYS-67
RP   AND HIS-69, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH TLR4,
RP   IDENTIFICATION IN A COMPLEX WITH TLR4; TRAF6; MAP3K7; MYD88; IKBKG;
RP   TICAM1; BIRC2; BIRC3 AND UBE2N, UBIQUITINATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=19898473; DOI=10.1038/ni.1819;
RA   Tseng P.H., Matsuzawa A., Zhang W., Mino T., Vignali D.A., Karin M.;
RT   "Different modes of ubiquitination of the adaptor TRAF3 selectively
RT   activate the expression of type I interferons and proinflammatory
RT   cytokines.";
RL   Nat. Immunol. 11:70-75(2010).
CC   -!- FUNCTION: Regulates pathways leading to the activation of NF-
CC       kappa-B and MAP kinases, and plays a central role in the
CC       regulation of B cell survival. Part of signaling pathways leading
CC       to the production of cytokines and interferon. Required for normal
CC       antibody isotype switching from IgM to IgG. Plays a role T-cell
CC       dependent immune responses. Plays a role in the regulation of
CC       antiviral responses. Is an essential constituent of several E3
CC       ubiquitin-protein ligase complexes. May have E3 ubiquitin-protein
CC       ligase activity and promote 'Lys-63'-linked ubiquitination of
CC       target proteins. Inhibits activation of NF-kappa-B in response to
CC       LTBR stimulation. Inhibits TRAF2-mediated activation of NF-kappa-
CC       B. Down-regulates proteolytic processing of NFKB2, and thereby
CC       inhibits non-canonical activation of NF-kappa-B. Promotes
CC       ubiquitination and proteasomal degradation of MAP3K14.
CC   -!- SUBUNIT: Homotrimer. Heterotrimer with TRAF2 and TRAF5. Interacts
CC       with LTBR/TNFRSF3, TNFRSF4, TNFRSF5/CD40, TNFRSF8/CD30, TNFRSF13C
CC       TNFRSF17/BCMA, TLR4 and EDAR. Interacts with MAP3K5, MAP3K14,
CC       TRAIP/TRIP, TDP2/TTRAP, TANK/ITRAF and TRAF3IP1. Interaction with
CC       TNFRSF5/CD40 is modulated by TANK/ITRAF, which competes for the
CC       same binding site. Interacts with TICAM1. Interacts with TRAFD1.
CC       Interacts with OTUB1, OTUB2 and OTUD5. Interacts with RNF216,
CC       MAVS, OPTN and TBK1 (By similarity). Identified in a complex with
CC       TRAF2, MAP3K14 and BIRC3. Upon exposure to bacterial
CC       lipopolysaccharide (LPS), recruited to a transient complex
CC       containing TLR4, TRAF3, TRAF6, IKBKG, MAP3K7, MYD88, TICAM1,
CC       BIRC2, BIRC3 and UBE2N.
CC   -!- INTERACTION:
CC       P62991:Rps27a; NbExp=1; IntAct=EBI-520135, EBI-413074;
CC       O35305:Tnfrsf11a; NbExp=2; IntAct=EBI-520135, EBI-647362;
CC       P47741:Tnfrsf4; NbExp=2; IntAct=EBI-520135, EBI-520001;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome. Note=Undergoes
CC       endocytosis together with TLR4 upon LPS signaling.
CC   -!- TISSUE SPECIFICITY: Detected in bone marrow macrophages and spleen
CC       B cells (at protein level). In adult, highest in brain. Also found
CC       in kidney, heart, thymus, spleen, lung, muscle, testis and ovary.
CC       Not found in liver.
CC   -!- DEVELOPMENTAL STAGE: In the embryo, expressed from E6.5 with
CC       highest levels found between E11.5 and E13.5. At late stages of
CC       gestation, from E14.5, only low levels are detected.
CC   -!- DOMAIN: The MATH/TRAF domain binds to receptor cytoplasmic
CC       domains.
CC   -!- DOMAIN: The Ring-type zinc finger domain is required for its
CC       function in down-regulation of NFKB2 proteolytic processing.
CC   -!- PTM: Undergoes 'Lys-48'-linked polyubiquitination, leading to its
CC       proteasomal degradation in response to signaling by TNFSF13B, TLR4
CC       or through CD40. Undergoes 'Lys-63'-linked ubiquitination during
CC       early stages of virus infection, and 'Lys-48'-linked
CC       ubiquitination during later stages. Undergoes both 'Lys-48'-linked
CC       and 'Lys-63'-linked ubiquitination in response to TLR3 and TLR4
CC       signaling. Deubiquitinated by OTUB1, OTUB2 and OTUD5 (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Newborns appear normal, but do not thrive.
CC       Their blood glucose levels and leukocyte levels decrease steadily,
CC       the spleen size is dramatically reduced, and they become
CC       progressively runted. They die about ten days after birth. Mice
CC       exhibit abnormally high MAP3K14 protein levels and constitutive
CC       proteolytic processing of NFKB2/p100, leading to constitutive
CC       activation of NF-kappa-B.
CC   -!- SIMILARITY: Belongs to the TNF receptor-associated factor family.
CC       A subfamily.
CC   -!- SIMILARITY: Contains 1 MATH domain.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SIMILARITY: Contains 2 TRAF-type zinc fingers.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U21050; AAC52175.1; -; mRNA.
DR   EMBL; U33840; AAC52710.1; -; mRNA.
DR   IPI; IPI00310635; -.
DR   PIR; I49272; I49272.
DR   RefSeq; NP_035762.2; NM_011632.2.
DR   UniGene; Mm.27431; -.
DR   ProteinModelPortal; Q60803; -.
DR   SMR; Q60803; 36-229, 376-567.
DR   IntAct; Q60803; 8.
DR   MINT; MINT-1506326; -.
DR   STRING; Q60803; -.
DR   PRIDE; Q60803; -.
DR   Ensembl; ENSMUST00000021706; ENSMUSP00000021706; ENSMUSG00000021277.
DR   GeneID; 22031; -.
DR   KEGG; mmu:22031; -.
DR   UCSC; uc007pcl.1; mouse.
DR   CTD; 22031; -.
DR   MGI; MGI:108041; Traf3.
DR   eggNOG; roNOG10564; -.
DR   GeneTree; ENSGT00550000074359; -.
DR   HOGENOM; HBG506127; -.
DR   HOVERGEN; HBG058222; -.
DR   InParanoid; Q60803; -.
DR   OrthoDB; EOG4JWVD7; -.
DR   NextBio; 301784; -.
DR   ArrayExpress; Q60803; -.
DR   Bgee; Q60803; -.
DR   CleanEx; MM_TRAF3; -.
DR   Genevestigator; Q60803; -.
DR   GermOnline; ENSMUSG00000021277; Mus musculus.
DR   GO; GO:0035631; C:CD40 receptor complex; IDA:BHF-UCL.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0009898; C:internal side of plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR   GO; GO:0042981; P:regulation of apoptosis; IEA:InterPro.
DR   GO; GO:0050688; P:regulation of defense response to virus; IMP:UniProtKB.
DR   GO; GO:0032648; P:regulation of interferon-beta production; IMP:UniProtKB.
DR   GO; GO:0030162; P:regulation of proteolysis; IDA:UniProtKB.
DR   GO; GO:0002224; P:toll-like receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB.
DR   InterPro; IPR002083; MATH.
DR   InterPro; IPR013323; SIAH-type.
DR   InterPro; IPR012227; TNF_recpt_TRAF.
DR   InterPro; IPR008974; TRAF-like.
DR   InterPro; IPR013322; TRAF-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   InterPro; IPR001293; Znf_TRAF.
DR   Gene3D; G3DSA:3.90.890.10; SIAH-type; 1.
DR   Gene3D; G3DSA:2.60.210.10; TRAF-type; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00917; MATH; 1.
DR   PIRSF; PIRSF015614; TRAF; 1.
DR   SMART; SM00061; MATH; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF49599; Traf_like; 2.
DR   PROSITE; PS50144; MATH; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS50145; ZF_TRAF; 2.
PE   1: Evidence at protein level;
KW   Apoptosis; Coiled coil; Cytoplasm; Endosome; Immunity;
KW   Isopeptide bond; Ligase; Metal-binding; Repeat; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    567       TNF receptor-associated factor 3.
FT                                /FTId=PRO_0000056402.
FT   DOMAIN      414    559       MATH.
FT   ZN_FING      67     76       RING-type.
FT   ZN_FING     134    189       TRAF-type 1.
FT   ZN_FING     190    248       TRAF-type 2.
FT   COILED      266    337       Potential.
FT   CROSSLNK    106    106       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin)
FT                                (Probable).
FT   CROSSLNK    155    155       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin)
FT                                (Probable).
FT   MUTAGEN      52     52       C->A: Abolishes inhibition of NFKB2
FT                                processing; when associated with A-55.
FT   MUTAGEN      55     55       C->A: Abolishes inhibition of NFKB2
FT                                processing; when associated with A-52.
FT   MUTAGEN      67     67       C->A: Strongly reduces 'Lys-63'-linked
FT                                ubiquitination; when associated with A-
FT                                69. Abolishes inhibition of NFKB2
FT                                processing; when associated with A-69.
FT   MUTAGEN      69     69       H->A: Strongly reduces 'Lys-63'-linked
FT                                ubiquitination; when associated with A-
FT                                69. Abolishes inhibition of NFKB2
FT                                processing; when associated with A-67.
FT   MUTAGEN     106    106       K->R: Reduces 'Lys-48'-linked
FT                                polyubiquitination; when associated with
FT                                R-155.
FT   MUTAGEN     155    155       K->R: Reduces 'Lys-48'-linked
FT                                polyubiquitination; when associated with
FT                                R-106.
FT   CONFLICT     72     73       CE -> WQ (in Ref. 2; AAC52710).
FT   CONFLICT    390    390       T -> M (in Ref. 2; AAC52710).
SQ   SEQUENCE   567 AA;  64264 MW;  2522B343B41192DC CRC64;
     MESSKKMDAA GTLQPNPPLK LQPDRGAGSV LVPEQGGYKE KFVKTVEDKY KCEKCRLVLC
     NPKQTECGHR FCESCMAALL SSSSPKCTAC QESIIKDKVF KDNCCKREIL ALQVYCRNEG
     RGCAEQLTLG HLLVHLKNEC QFEELPCLRA DCKEKVLRKD LRDHVEKACK YREATCSHCK
     SQVPMIKLQK HEDTDCPCVV VSCPHKCSVQ TLLRSELSAH LSECVNAPST CSFKRYGCVF
     QGTNQQIKAH EASSAVQHVN LLKEWSNSLE KKVSLLQNES VEKNKSIQSL HNQICSFEIE
     IERQKEMLRN NESKILHLQR VIDSQAEKLK ELDKEIRPFR QNWEEADSMK SSVESLQNRV
     TELESVDKSA GQAARNTGLL ESQLSRHDQT LSVHDIRLAD MDLRFQVLET ASYNGVLIWK
     IRDYKRRKQE AVMGKTLSLY SQPFYTGYFG YKMCARVYLN GDGMGKGTHL SLFFVIMRGE
     YDALLPWPFK QKVTLMLMDQ GSSRRHLGDA FKPDPNSSSF KKPTGEMNIA SGCPVFVAQT
     VLENGTYIKD DTIFIKVIVD TSDLPDP
//
ID   AKT2_MOUSE              Reviewed;         481 AA.
AC   Q60823;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=RAC-beta serine/threonine-protein kinase;
DE            EC=2.7.11.1;
DE   AltName: Full=Protein kinase Akt-2;
DE   AltName: Full=Protein kinase B beta;
DE            Short=PKB beta;
DE   AltName: Full=RAC-PK-beta;
GN   Name=Akt2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X CBA; TISSUE=Thymus;
RX   MEDLINE=96032568; PubMed=7566964;
RA   Altomare D.A., Guo K., Cheng J.Q., Sonoda G., Walsh K., Testa J.R.;
RT   "Cloning, chromosomal localization and expression analysis of the
RT   mouse Akt2 oncogene.";
RL   Oncogene 11:1055-1060(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Retina, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: General protein kinase capable of phosphorylating
CC       several known proteins.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Two specific sites, one in the kinase domain
CC       (Thr-309) and the other in the C-terminal regulatory region (Ser-
CC       474), need to be phosphorylated for its full activation (By
CC       similarity).
CC   -!- SUBUNIT: Interacts (via PH domain) with MTCP1, TCL1A AND TCL1B.
CC       Interacts with TRAF6 (By similarity).
CC   -!- PTM: Phosphorylation on Thr-309 and Ser-474 is required for full
CC       activity (By similarity).
CC   -!- PTM: Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked
CC       polyubiquitination. TRAF6-induced 'Lys-63'-linked AKT2
CC       ubiquitination. When fully phosphorylated and translocated into
CC       the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed by
CC       TTC3, leading to its degradation by the proteasome (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. RAC subfamily.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U22445; AAA83557.1; -; mRNA.
DR   EMBL; BC026151; AAH26151.1; -; mRNA.
DR   EMBL; BC040377; AAH40377.1; -; mRNA.
DR   IPI; IPI00121335; -.
DR   RefSeq; NP_001103678.1; NM_001110208.1.
DR   RefSeq; NP_031460.1; NM_007434.3.
DR   UniGene; Mm.177194; -.
DR   ProteinModelPortal; Q60823; -.
DR   SMR; Q60823; 1-480.
DR   IntAct; Q60823; 5.
DR   STRING; Q60823; -.
DR   PhosphoSite; Q60823; -.
DR   PRIDE; Q60823; -.
DR   Ensembl; ENSMUST00000051356; ENSMUSP00000052103; ENSMUSG00000004056.
DR   Ensembl; ENSMUST00000108343; ENSMUSP00000103980; ENSMUSG00000004056.
DR   Ensembl; ENSMUST00000108344; ENSMUSP00000103981; ENSMUSG00000004056.
DR   GeneID; 11652; -.
DR   KEGG; mmu:11652; -.
DR   UCSC; uc009fwr.1; mouse.
DR   CTD; 11652; -.
DR   MGI; MGI:104874; Akt2.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108317; -.
DR   InParanoid; Q60823; -.
DR   OMA; EEIRFPK; -.
DR   OrthoDB; EOG40GCQP; -.
DR   PhylomeDB; Q60823; -.
DR   BRENDA; 2.7.11.1; 244.
DR   Reactome; REACT_13641; Regulation of Beta-Cell Development.
DR   NextBio; 461547; -.
DR   ArrayExpress; Q60823; -.
DR   Bgee; Q60823; -.
DR   CleanEx; MM_AKT2; -.
DR   Genevestigator; Q60823; -.
DR   GermOnline; ENSMUSG00000004056; Mus musculus.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046328; P:regulation of JNK cascade; IDA:MGI.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT   CHAIN         1    481       RAC-beta serine/threonine-protein kinase.
FT                                /FTId=PRO_0000085609.
FT   DOMAIN        5    108       PH.
FT   DOMAIN      152    409       Protein kinase.
FT   DOMAIN      410    481       AGC-kinase C-terminal.
FT   NP_BIND     158    166       ATP (By similarity).
FT   ACT_SITE    275    275       Proton acceptor (By similarity).
FT   BINDING     181    181       ATP (By similarity).
FT   MOD_RES     126    126       Phosphoserine (By similarity).
FT   MOD_RES     309    309       Phosphothreonine; by PDPK1 (By
FT                                similarity).
FT   MOD_RES     447    447       Phosphoserine (By similarity).
FT   MOD_RES     451    451       Phosphothreonine (By similarity).
FT   MOD_RES     474    474       Phosphoserine (By similarity).
FT   MOD_RES     478    478       Phosphoserine (By similarity).
SQ   SEQUENCE   481 AA;  55742 MW;  4AB4A9C4FB9CFA7D CRC64;
     MNEVSVIKEG WLHKRGEYIK TWRPRYFLLK SDGSFIGYKE RPEAPDQTLP PLNNFSVAEC
     QLMKTERPRP NTFVIRCLQW TTVIERTFHV DSPDEREEWM RAIQMVANSL KQRGPGEDAM
     DYKCGSPSDS STSEMMEVAV NKARAKVTMN DFDYLKLLGK GTFGKVILVR EKATGRYYAM
     KILRKEVIIA KDEVAHTVTE SRVLQNTRHP FLTALKYAFQ THDRLCFVME YANGGELFFH
     LSRERVFTED RARFYGAEIV SALEYLHSRD VVYRDIKLEN LMLDKDGHIK ITDFGLCKEG
     ISDGATMKTF CGTPEYLAPE VLEDNDYGRA VDWWGLGVVM YEMMCGRLPF YNQDHERLFE
     LILMEEIRFP RTLGPEAKSL LAGLLKKDPK QRLGGGPSDA KEVMEHRFFL SINWQDVVQK
     KLLPPFKPQV TSEVDTRYFD DEFTAQSITI TPPDRYDSLD PLELDQRTHF PQFSYSASIR
     E
//
ID   PPR1B_MOUSE             Reviewed;         194 AA.
AC   Q60829; A2A564; Q3URF2; Q6DV86; Q91XB5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 2.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 1B;
DE   AltName: Full=DARPP-32;
DE   AltName: Full=Dopamine- and cAMP-regulated neuronal phosphoprotein;
GN   Name=Ppp1r1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J;
RA   Liu Q.-R., Uhl G.R.;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RC   STRAIN=BALB/c;
RX   MEDLINE=96043524; PubMed=7485543;
RA   Blau S., Daly L., Fienberg A., Teitelman G., Ehrlich M.E.;
RT   "DARPP-32 promoter directs transgene expression to renal thick
RT   ascending limb of loop of Henle.";
RL   Am. J. Physiol. 269:F564-F570(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 48-194.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Inhibitor of protein-phosphatase 1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q60829-1; Sequence=Displayed;
CC       Name=2; Synonyms=DARPP-30;
CC         IsoId=Q60829-2; Sequence=VSP_025058;
CC   -!- PTM: Dopamine- and cyclic AMP-regulated neuronal phosphoprotein
CC       (By similarity).
CC   -!- PTM: Phosphorylation of Thr-34 is required for activity (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein phosphatase inhibitor 1 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY640620; AAT66920.1; -; mRNA.
DR   EMBL; AY640621; AAT66921.1; -; mRNA.
DR   EMBL; AL591390; CAM22017.1; -; Genomic_DNA.
DR   EMBL; BC011122; AAH11122.1; -; mRNA.
DR   EMBL; BC026568; AAH26568.1; -; mRNA.
DR   EMBL; BC031129; AAH31129.1; -; mRNA.
DR   EMBL; U23160; AAA93223.1; -; Genomic_DNA.
DR   EMBL; AK141563; BAE24736.1; -; mRNA.
DR   IPI; IPI00121349; -.
DR   IPI; IPI00845821; -.
DR   RefSeq; NP_659077.1; NM_144828.1.
DR   UniGene; Mm.45372; -.
DR   ProteinModelPortal; Q60829; -.
DR   STRING; Q60829; -.
DR   PhosphoSite; Q60829; -.
DR   PRIDE; Q60829; -.
DR   Ensembl; ENSMUST00000078694; ENSMUSP00000077760; ENSMUSG00000061718.
DR   GeneID; 19049; -.
DR   KEGG; mmu:19049; -.
DR   UCSC; uc007lfz.1; mouse.
DR   CTD; 19049; -.
DR   MGI; MGI:94860; Ppp1r1b.
DR   eggNOG; roNOG15961; -.
DR   HOGENOM; HBG127280; -.
DR   HOVERGEN; HBG099182; -.
DR   InParanoid; Q60829; -.
DR   OMA; GYPREEE; -.
DR   OrthoDB; EOG4P2Q3W; -.
DR   PhylomeDB; Q60829; -.
DR   NextBio; 295517; -.
DR   ArrayExpress; Q60829; -.
DR   Bgee; Q60829; -.
DR   Genevestigator; Q60829; -.
DR   GermOnline; ENSMUSG00000061718; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; TAS:MGI.
DR   GO; GO:0007621; P:negative regulation of female receptivity; IDA:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0006350; P:transcription; IMP:MGI.
DR   InterPro; IPR015670; Dopamine/cAMP_neuron_P-prot.
DR   InterPro; IPR008466; PPI_1DARPP-32.
DR   PANTHER; PTHR15417:SF2; DARP-32; 1.
DR   PANTHER; PTHR15417; PPI_1DARPP-32; 1.
DR   Pfam; PF05395; DARPP-32; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Phosphoprotein;
KW   Protein phosphatase inhibitor.
FT   CHAIN         1    194       Protein phosphatase 1 regulatory subunit
FT                                1B.
FT                                /FTId=PRO_0000071474.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      34     34       Phosphothreonine; by PKA (By similarity).
FT   MOD_RES      75     75       Phosphothreonine; by CDK5 (By
FT                                similarity).
FT   MOD_RES      97     97       Phosphoserine.
FT   MOD_RES     192    192       Phosphoserine.
FT   VAR_SEQ       1     36       Missing (in isoform 2).
FT                                /FTId=VSP_025058.
SQ   SEQUENCE   194 AA;  21781 MW;  E0509291E6615EA3 CRC64;
     MDPKDRKKIQ FSVPAPPSQL DPRQVEMIRR RRPTPAMLFR VSEHSSPEEE ASPHQRTSGE
     GHHPKSKRPN PCAYTPPSLK AVQHLQTISN LSENQASEEE DELGELRELG YPQEDDEEDE
     DEEEDEEEDS QAEVLKGSRG TVGQKPTCGR GLEGPWERPP PLDEPQRDGN SEDQVEGRAT
     LSEPGEEPQH PSPP
//
ID   RELN_MOUSE              Reviewed;        3461 AA.
AC   Q60841; Q9CUA6;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 2.
DT   08-MAR-2011, entry version 105.
DE   RecName: Full=Reelin;
DE            EC=3.4.21.-;
DE   AltName: Full=Reeler protein;
DE   Flags: Precursor;
GN   Name=Reln; Synonyms=Rl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Cerebellum;
RX   MEDLINE=95231649; PubMed=7715726; DOI=10.1038/374719a0;
RA   D'Arcangelo G., Miao G.G., Chen S.-C., Soares H.D., Morgan J.I.,
RA   Curran T.;
RT   "A protein related to extracellular matrix proteins deleted in the
RT   mouse mutant reeler.";
RL   Nature 374:719-723(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX   MEDLINE=98086481; PubMed=9417911; DOI=10.1006/geno.1997.4983;
RA   Royaux I., Lambert de Rouvroit C., D'Arcangelo G., Demirov D.,
RA   Goffinet A.M.;
RT   "Genomic organization of the mouse reelin gene.";
RL   Genomics 46:240-250(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2152-3461 (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=95375789; PubMed=7647795; DOI=10.1038/ng0595-77;
RA   Hirotsune S., Takahara T., Sasaki N., Hirose K., Yoshiki A.,
RA   Ohashi T., Kusakabe M., Murakami Y., Muramatsu M., Watanabe S.,
RA   Nakao K., Katsuki M., Hayashizaki Y.;
RT   "The reeler gene encodes a protein with an EGF-like motif expressed by
RT   pioneer neurons.";
RL   Nat. Genet. 10:77-83(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3044-3461 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   CHARACTERIZATION.
RX   MEDLINE=97141547; PubMed=8987733;
RA   D'Arcangelo G., Nakajima K., Miyata T., Ogawa M., Mikoshiba K.,
RA   Curran T.;
RT   "Reelin is a secreted glycoprotein recognized by the CR-50 monoclonal
RT   antibody.";
RL   J. Neurosci. 17:23-31(1997).
RN   [6]
RP   CHARACTERIZATION.
RX   MEDLINE=21634904; PubMed=11689558; DOI=10.1074/jbc.M106996200;
RA   Quattrocchi C.C., Wannenes F., Persico A.M., Ciafre S.A.,
RA   D'Arcangelo G., Farace M.G., Keller F.;
RT   "Reelin is a serine protease of the extracellular matrix.";
RL   J. Biol. Chem. 277:303-309(2002).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=97325946; PubMed=9182958;
RX   DOI=10.1111/j.1460-9568.1997.tb01456.x;
RA   Schiffmann S.N., Bernier B., Goffinet A.M.;
RT   "Reelin mRNA expression during mouse brain development.";
RL   Eur. J. Neurosci. 9:1055-1071(1997).
RN   [8]
RP   ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX   MEDLINE=99263436; PubMed=10328932; DOI=10.1006/exnr.1999.7019;
RA   Lambert de Rouvroit C., Bernier B., Royaux I., de Bergeyck V.,
RA   Goffinet A.M.;
RT   "Evolutionarily conserved, alternative splicing of reelin during brain
RT   development.";
RL   Exp. Neurol. 156:229-238(1999).
RN   [9]
RP   INTERACTION WITH VLDLR AND APOER2.
RX   MEDLINE=20036019; PubMed=10571241; DOI=10.1016/S0896-6273(00)80861-2;
RA   Hiesberger T., Trommsdorff M., Howell B.W., Goffinet A.M., Mumby M.C.,
RA   Cooper J.A., Herz J.;
RT   "Direct binding of Reelin to VLDL receptor and ApoE receptor 2 induces
RT   tyrosine phosphorylation of disabled-1 and modulates tau
RT   phosphorylation.";
RL   Neuron 24:481-489(1999).
RN   [10]
RP   FUNCTION.
RX   MEDLINE=20359755; PubMed=10880573; DOI=10.1073/pnas.150040497;
RA   Yip J.W., Yip Y.P.L., Nakajima K., Capriotti C.;
RT   "Reelin controls position of autonomic neurons in the spinal cord.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:8612-8616(2000).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1273, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1222-1597, DISULFIDE BONDS,
RP   AND CALCIUM-BINDING.
RX   PubMed=16858396; DOI=10.1038/sj.emboj.7601240;
RA   Nogi T., Yasui N., Hattori M., Iwasaki K., Takagi J.;
RT   "Structure of a signaling-competent reelin fragment revealed by X-ray
RT   crystallography and electron tomography.";
RL   EMBO J. 25:3675-3683(2006).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1948-2662, DISULFIDE BONDS,
RP   GLYCOSYLATION AT ASN-2145; ASN-2269; ASN-2317 AND ASN-2569,
RP   CALCIUM-BINDING, ZINC-BINDING SITES, AND MUTAGENESIS OF LYS-2360 AND
RP   LYS-2467.
RX   PubMed=17548821; DOI=10.1073/pnas.0700438104;
RA   Yasui N., Nogi T., Kitao T., Nakano Y., Hattori M., Takagi J.;
RT   "Structure of a receptor-binding fragment of reelin and mutational
RT   analysis reveal a recognition mechanism similar to endocytic
RT   receptors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:9988-9993(2007).
CC   -!- FUNCTION: Extracellular matrix serine protease that plays a role
CC       in layering of neurons in the cerebral cortex and cerebellum.
CC       Regulates microtubule function in neurons and neuronal migration.
CC       Affects migration of sympathetic preganglionic neurons in the
CC       spinal cord, where it seems to act as a barrier to neuronal
CC       migration. Enzymatic activity is important for the modulation of
CC       cell adhesion. Binding to the extracellular domains of lipoprotein
CC       receptors VLDLR and ApoER2 induces tyrosine phosphorylation of
CC       Dab1 and modulation of Tau phosphorylation.
CC   -!- SUBUNIT: Binds to the ectodomains of VLDLR and ApoER2.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q60841-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q60841-2; Sequence=VSP_005577;
CC       Name=3;
CC         IsoId=Q60841-3; Sequence=VSP_005578;
CC   -!- TISSUE SPECIFICITY: The major isoform 1 is neuron-specific. It is
CC       abundantly produced during brain ontogenesis by the Cajal-Retzius
CC       cells and other pioneer neurons located in the telencephalic
CC       marginal zone and by granule cells of the external granular layer
CC       of the cerebellum. Expression is located in deeper layers in the
CC       developing hippocampus and olfactory bulb, low levels of
CC       expression are also detected in the immature striatum. At early
CC       developmental stages, expressed also in hypothalamic
CC       differentiation fields, tectum and spinal cord. A moderate to low
CC       level of expression occurs in the septal area, striatal fields,
CC       habenular nuclei, some thalamic nuclei, particularly the lateral
CC       geniculate, the retina and some nuclei of the reticular formation
CC       in the central field of the medulla. Very low levels found in
CC       liver and kidney. No expression in radial glial cells, cortical
CC       plate, Purkinje cells and inferior olivary neurons. The minor
CC       isoform 2 is only expressed in non neuronal cells. The minor
CC       isoform 3 is found in the same cells as isoform 1, but is almost
CC       undetectable in retina and brain stem.
CC   -!- DEVELOPMENTAL STAGE: First detected at embryonic day 11.5.
CC       Expression increases up to birth and remains high from postnatal
CC       day 2 to 11 in both cerebellum and fore/midbrain. Expression
CC       declines thereafter and is largely brain specific in the adult.
CC   -!- DOMAIN: The basic C-terminal region is essential for secretion.
CC   -!- PTM: N-glycosylated and to a lesser extent also O-glycosylated.
CC   -!- DISEASE: Note=Defects in Reln are the cause of the autosomal
CC       recessive reeler (rl) phenotype which is characterized by impaired
CC       motor coordination, tremors and ataxia. Neurons in affected mice
CC       fail to reach their correct locations in the developing brain,
CC       disrupting the organization of the cerebellar and cerebral
CC       cortices and other laminated regions.
CC   -!- SIMILARITY: Belongs to the reelin family.
CC   -!- SIMILARITY: Contains 16 BNR repeats.
CC   -!- SIMILARITY: Contains 8 EGF-like domains.
CC   -!- SIMILARITY: Contains 1 reelin domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA09788.1; Type=Erroneous initiation;
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DR   EMBL; U24703; AAB91599.1; -; mRNA.
DR   EMBL; D63520; BAA09788.1; ALT_INIT; mRNA.
DR   EMBL; AK017094; BAB30592.1; -; mRNA.
DR   IPI; IPI00121421; -.
DR   IPI; IPI00230330; -.
DR   IPI; IPI00230331; -.
DR   PIR; S58870; S58870.
DR   RefSeq; NP_035391.2; NM_011261.2.
DR   UniGene; Mm.425236; -.
DR   PDB; 2DDU; X-ray; 2.05 A; A=1222-1597.
DR   PDB; 2E26; X-ray; 2.00 A; A=1948-2662.
DR   PDB; 3A7Q; X-ray; 2.60 A; A=1948-2662.
DR   PDBsum; 2DDU; -.
DR   PDBsum; 2E26; -.
DR   PDBsum; 3A7Q; -.
DR   ProteinModelPortal; Q60841; -.
DR   SMR; Q60841; 51-181, 569-863, 921-1220, 1294-1947, 1956-2662, 2749-3049.
DR   STRING; Q60841; -.
DR   PhosphoSite; Q60841; -.
DR   PRIDE; Q60841; -.
DR   Ensembl; ENSMUST00000062372; ENSMUSP00000058025; ENSMUSG00000042453.
DR   Ensembl; ENSMUST00000115152; ENSMUSP00000110805; ENSMUSG00000042453.
DR   GeneID; 19699; -.
DR   KEGG; mmu:19699; -.
DR   UCSC; uc008wpi.1; mouse.
DR   CTD; 19699; -.
DR   MGI; MGI:103022; Reln.
DR   HOGENOM; HBG358144; -.
DR   HOVERGEN; HBG023117; -.
DR   InParanoid; Q60841; -.
DR   OrthoDB; EOG4GB757; -.
DR   NextBio; 297056; -.
DR   ArrayExpress; Q60841; -.
DR   Bgee; Q60841; -.
DR   CleanEx; MM_RELN; -.
DR   Genevestigator; Q60841; -.
DR   GermOnline; ENSMUSG00000042453; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; TAS:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IDA:MGI.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007411; P:axon guidance; IMP:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0021800; P:cerebral cortex tangential migration; IMP:MGI.
DR   GO; GO:0010001; P:glial cell differentiation; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
DR   GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:MGI.
DR   GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; IDA:MGI.
DR   GO; GO:0048265; P:response to pain; IMP:MGI.
DR   GO; GO:0021511; P:spinal cord patterning; IMP:MGI.
DR   InterPro; IPR002860; BNR_rpt.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR011040; Neuraminidase.
DR   InterPro; IPR002861; Reeler_dom.
DR   Gene3D; G3DSA:2.120.10.10; Neuraminidase; 6.
DR   Pfam; PF02012; BNR; 11.
DR   Pfam; PF07974; EGF_2; 6.
DR   Pfam; PF02014; Reeler; 1.
DR   SMART; SM00181; EGF; 5.
DR   SUPFAM; SSF50939; Sialidase; 2.
DR   PROSITE; PS00022; EGF_1; 7.
DR   PROSITE; PS01186; EGF_2; 6.
DR   PROSITE; PS50026; EGF_3; 5.
DR   PROSITE; PS51019; REELIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Cell adhesion;
KW   Developmental protein; Disulfide bond; EGF-like domain;
KW   Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding;
KW   Phosphoprotein; Protease; Repeat; Secreted; Serine protease; Signal;
KW   Zinc.
FT   SIGNAL        1     26       Potential.
FT   CHAIN        27   3461       Reelin.
FT                                /FTId=PRO_0000030305.
FT   DOMAIN       27    191       Reelin.
FT   REPEAT      593    604       BNR 1.
FT   DOMAIN      671    702       EGF-like 1.
FT   REPEAT      799    810       BNR 2.
FT   REPEAT      952    963       BNR 3.
FT   DOMAIN     1030   1061       EGF-like 2.
FT   REPEAT     1157   1168       BNR 4.
FT   REPEAT     1323   1334       BNR 5.
FT   DOMAIN     1409   1442       EGF-like 3.
FT   REPEAT     1535   1546       BNR 6.
FT   REPEAT     1686   1697       BNR 7.
FT   DOMAIN     1765   1796       EGF-like 4.
FT   REPEAT     1884   1895       BNR 8.
FT   REPEAT     2043   2054       BNR 9.
FT   DOMAIN     2129   2161       EGF-like 5.
FT   REPEAT     2250   2261       BNR 10.
FT   REPEAT     2399   2410       BNR 11.
FT   DOMAIN     2478   2509       EGF-like 6.
FT   REPEAT     2598   2609       BNR 12.
FT   REPEAT     2778   2789       BNR 13.
FT   DOMAIN     2853   2884       EGF-like 7.
FT   REPEAT     2979   2990       BNR 14.
FT   REPEAT     3143   3155       BNR 15.
FT   DOMAIN     3228   3260       EGF-like 8.
FT   REPEAT     3363   3374       BNR 16.
FT   COMPBIAS   3432   3461       Arg-rich (basic).
FT   METAL      2061   2061       Zinc 1.
FT   METAL      2074   2074       Zinc 1.
FT   METAL      2179   2179       Zinc 1.
FT   METAL      2264   2264       Zinc 1.
FT   METAL      2397   2397       Zinc 2.
FT   METAL      2399   2399       Zinc 2.
FT   METAL      2460   2460       Zinc 2.
FT   MOD_RES    1273   1273       Phosphothreonine.
FT   CARBOHYD    141    141       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    258    258       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    290    290       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    306    306       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    629    629       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1267   1267       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1447   1447       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1503   1503       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1600   1600       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1750   1750       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1921   1921       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2145   2145       N-linked (GlcNAc...).
FT   CARBOHYD   2269   2269       N-linked (GlcNAc...).
FT   CARBOHYD   2317   2317       N-linked (GlcNAc...).
FT   CARBOHYD   2569   2569       N-linked (GlcNAc...).
FT   CARBOHYD   2962   2962       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3016   3016       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3073   3073       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3185   3185       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3412   3412       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3439   3439       N-linked (GlcNAc...) (Potential).
FT   DISULFID     41    127       By similarity.
FT   DISULFID    155    179       By similarity.
FT   DISULFID    540    581       By similarity.
FT   DISULFID    609    614       By similarity.
FT   DISULFID    675    685       By similarity.
FT   DISULFID    692    701       By similarity.
FT   DISULFID    895    937       By similarity.
FT   DISULFID    968    975       By similarity.
FT   DISULFID   1034   1044       By similarity.
FT   DISULFID   1051   1060       By similarity.
FT   DISULFID   1271   1310
FT   DISULFID   1339   1348
FT   DISULFID   1633   1673       By similarity.
FT   DISULFID   1702   1709       By similarity.
FT   DISULFID   1983   2030
FT   DISULFID   2059   2070
FT   DISULFID   2133   2143
FT   DISULFID   2137   2149
FT   DISULFID   2151   2160
FT   DISULFID   2195   2235
FT   DISULFID   2348   2387
FT   DISULFID   2393   2559
FT   DISULFID   2482   2492
FT   DISULFID   2486   2497
FT   DISULFID   2499   2508
FT   DISULFID   2544   2584
FT   DISULFID   2794   2801       By similarity.
FT   DISULFID   2919   2966       By similarity.
FT   DISULFID   3160   3170       By similarity.
FT   DISULFID   3232   3242       By similarity.
FT   DISULFID   3236   3248       By similarity.
FT   DISULFID   3250   3259       By similarity.
FT   DISULFID   3296   3346       By similarity.
FT   VAR_SEQ    3429   3461       Missing (in isoform 3).
FT                                /FTId=VSP_005578.
FT   VAR_SEQ    3429   3430       Missing (in isoform 2).
FT                                /FTId=VSP_005577.
FT   MUTAGEN    2360   2360       K->A: Abolishes ApoER2-binding.
FT   MUTAGEN    2467   2467       K->A: Abolishes ApoER2-binding.
FT   CONFLICT   3066   3066       Missing (in Ref. 4; BAB30592).
FT   STRAND     1958   1960
FT   STRAND     1963   1965
FT   HELIX      1968   1970
FT   STRAND     1971   1973
FT   STRAND     1978   1980
FT   STRAND     1996   1999
FT   STRAND     2005   2011
FT   STRAND     2014   2016
FT   STRAND     2020   2032
FT   STRAND     2040   2047
FT   STRAND     2053   2056
FT   STRAND     2059   2061
FT   STRAND     2078   2080
FT   STRAND     2089   2095
FT   TURN       2096   2099
FT   STRAND     2102   2113
FT   STRAND     2122   2131
FT   HELIX      2134   2139
FT   STRAND     2140   2144
FT   TURN       2145   2147
FT   STRAND     2148   2151
FT   STRAND     2155   2157
FT   STRAND     2170   2172
FT   STRAND     2174   2176
FT   STRAND     2178   2187
FT   STRAND     2189   2193
FT   STRAND     2197   2201
FT   STRAND     2203   2206
FT   STRAND     2212   2216
FT   STRAND     2226   2233
FT   STRAND     2236   2238
FT   STRAND     2247   2254
FT   STRAND     2260   2265
FT   TURN       2269   2272
FT   STRAND     2275   2280
FT   HELIX      2283   2285
FT   STRAND     2287   2296
FT   STRAND     2299   2301
FT   STRAND     2307   2315
FT   STRAND     2324   2326
FT   STRAND     2328   2330
FT   TURN       2333   2335
FT   STRAND     2336   2338
FT   STRAND     2343   2345
FT   STRAND     2354   2357
FT   STRAND     2364   2368
FT   STRAND     2371   2373
FT   STRAND     2378   2384
FT   STRAND     2395   2403
FT   STRAND     2409   2412
FT   STRAND     2419   2422
FT   TURN       2433   2436
FT   STRAND     2440   2445
FT   HELIX      2448   2450
FT   STRAND     2452   2461
FT   STRAND     2471   2480
FT   HELIX      2484   2488
FT   STRAND     2489   2493
FT   STRAND     2496   2499
FT   STRAND     2503   2505
FT   STRAND     2510   2513
FT   STRAND     2519   2521
FT   TURN       2529   2531
FT   STRAND     2532   2542
FT   STRAND     2547   2550
FT   STRAND     2552   2555
FT   STRAND     2562   2565
FT   STRAND     2575   2582
FT   STRAND     2584   2586
FT   HELIX      2591   2593
FT   STRAND     2594   2602
FT   STRAND     2608   2613
FT   STRAND     2622   2627
FT   HELIX      2630   2632
FT   STRAND     2634   2642
SQ   SEQUENCE   3461 AA;  387513 MW;  4131F3E84A9D4AE2 CRC64;
     MERGCWAPRA LVLAVLLLLA TLRARAATGY YPRFSPFFFL CTHHGELEGD GEQGEVLISL
     HIAGNPTYYV PGQEYHVTIS TSTFFDGLLV TGLYTSTSIQ SSQSIGGSSA FGFGIMSDHQ
     FGNQFMCSVV ASHVSHLPTT NLSFVWIAPP AGTGCVNFMA TATHRGQVIF KDALAQQLCE
     QGAPTEATAY SHLAEIHSDS VILRDDFDSY QQLELNPNIW VECSNCEMGE QCGTIMHGNA
     VTFCEPYGPR ELTTTCLNTT TASVLQFSIG SGSCRFSYSD PSITVSYAKN NTADWIQLEK
     IRAPSNVSTV IHILYLPEEA KGESVQFQWK QDSLRVGEVY EACWALDNIL VINSAHREVV
     LEDNLDPVDT GNWLFFPGAT VKHSCQSDGN SIYFHGNEGS EFNFATTRDV DLSTEDIQEQ
     WSEEFESQPT GWDILGAVVG ADCGTVESGL SLVFLKDGER KLCTPYMDTT GYGNLRFYFV
     MGGICDPGVS HENDIILYAK IEGRKEHIAL DTLTYSSYKV PSLVSVVINP ELQTPATKFC
     LRQKSHQGYN RNVWAVDFFH VLPVLPSTMS HMIQFSINLG CGTHQPGNSV SLEFSTNHGR
     SWSLLHTECL PEICAGPHLP HSTVYSSENY SGWNRITIPL PNAALTRDTR IRWRQTGPIL
     GNMWAIDNVY IGPSCLKFCS GRGQCTRHGC KCDPGFSGPA CEMASQTFPM FISESFGSAR
     LSSYHNFYSI RGAEVSFGCG VLASGKALVF NKDGRRQLIT SFLDSSQSRF LQFTLRLGSK
     SVLSTCRAPD QPGEGVLLHY SYDNGITWKL LEHYSYVNYH EPRIISVELP DDARQFGIQF
     RWWQPYHSSQ GEDVWAIDEI VMTSVLFNSI SLDFTNLVEV TQSLGFYLGN VQPYCGHDWT
     LCFTGDSKLA SSMRYVETQS MQIGASYMIQ FSLVMGCGQK YTPHMDNQVK LEYSANHGLT
     WHLVQEECLP SMPSCQEFTS ASIYHASEFT QWRRVTVVLP QKTWSGATRF RWSQSYYTAQ
     DEWALDNIYI GQQCPNMCSG HGSCDHGVCR CDQGYQGTEC HPEAALPSTI MSDFENPSSW
     ESDWQEVIGG EVVKPEQGCG VVSSGSSLYF SKAGKRQLVS WDLDTSWVDF VQFYIQIGGE
     SAACNKPDSR EEGILLQYSN NGGIQWHLLA EMYFSDFSKP RFVYLELPAA GKTPCTRFRW
     WKPVFSGEDY DQWAVDDIII LSEKQKQVIP VVNPTLPQNF YEKPAFDYPM NQMSVWLMLA
     NEGMAKNDSF CATTPSAMVF GKSDGDRFAV TRDLTLKPGY VLQFKLNIGC TSQFSSTAPV
     LLQYSHDAGM SWFLLKEGCF PASAAKGCEG NSRELSEPTV YYTGDFEEWT RITIAIPRSL
     ASSKTRFRWI QESSSQKNVP PFGLDGVYIS EPCPSYCSGH GDCISGVCFC DLGYTAAQGT
     CVSNTPNHSE MFDRFEGKLS PLWYKITGGQ VGTGCGTLND GRSLYFNGLG KREARTVPLD
     TRNISLVQFY IQIGSKTSGI TYITPRARYE GLVVQYSNDN GILWHLLREL DFMSFLEPQI
     ISIDLPREAK TPATAFRWWQ PQHGKHSAQW ALGDVLIGVN DSSQTGFQDK LDGSIDLQAN
     WYRIQGGQVD IDCLSMDTAL IFTENIGNPR YAETWDFHVS ESSFLQWEMN MGCSKPFSGA
     HGIQLQYSLN NGKDWQLVTE ECVPPTIGCV HYTESSTYTS ERFQNWRRVT VYLPLATNSP
     RTRFRWIQTN YTVGADSWAI DNVILASGCP WMCSGRGICD SGRCVCDRGF GGPFCVPVVP
     LPSILKDDFN GNLHPDLWPE VYGAERGNLN GETIKSGTCL IFKGEGLRML ISRDLDCTNT
     MYVQFSLRFI AKGTPERSHS ILLQFSVSGG VTWHLMDEFY FPQTTSILFI NVPLPYGAQT
     NATRFRLWQP YNNGKKEEIW IIDDFIIDGN NLNNPVLLLD TFDFGPREDN WFFYPGGNIG
     LYCPYSSKGA PEEDSAMVFV SNEVGEHSIT TRDLSVNENT IIQFEINVGC STDSSSADPV
     RLEFSRDFGA TWHLLLPLCY HSSSLVSSLC STEHHPSSTY YAGTTQGWRR EVVHFGKLHL
     CGSVRFRWYQ GFYPAGSQPV TWAIDNVYIG PQCEEMCYGH GSCINGTKCI CDPGYSGPTC
     KISTKNPDFL KDDFEGQLES DRFLLMSGGK PSRKCGILSS GNNLFFNEDG LRMLVTRDLD
     LSHARFVQFF MRLGCGKGVP DPRSQPVLLQ YSLNGGLSWS LLQEFLFSNS SNVGRYIALE
     MPLKARSGST RLRWWQPSEN GHFYSPWVID QILIGGNISG NTVLEDDFST LDSRKWLLHP
     GGTKMPVCGS TGDALVFIEK ASTRYVVTTD IAVNEDSFLQ IDFAASCSVT DSCYAIELEY
     SVDLGLSWHP LVRDCLPTNV ECSRYHLQRI LVSDTFNKWT RITLPLPSYT RSQATRFRWH
     QPAPFDKQQT WAIDNVYIGD GCLDMCSGHG RCVQGSCVCD EQWGGLYCDE PETSLPTQLK
     DNFNRAPSNQ NWLTVSGGKL STVCGAVASG LALHFSGGCS RLLVTVDLNL TNAEFIQFYF
     MYGCLITPSN RNQGVLLEYS VNGGITWNLL MEIFYDQYSK PGFVNILLPP DAKEIATRFR
     WWQPRHDGLD QNDWAIDNVL ISGSADQRTV MLDTFSSAPV PQHERSPADA GPVGRIAFEM
     FLEDKTSVNE NWLFHDDCTV ERFCDSPDGV MLCGSHDGRE VYAVTHDLTP TENWIMQFKI
     SVGCKVPEKI AQNQIHVQFS TDFGVSWSYL VPQCLPADPK CSGSVSQPSV FFPTEGWKRI
     TYPLPESLTG NPVRFRFYQK YSDVQWAIDN FYLGPGCLDN CGGHGDCLKE QCICDPGYSG
     PNCYLTHSLK TFLKERFDSE EIKPDLWMSL EGGSTCTECG VLAENTALYF GGSTVRQAIT
     QDLDLRGAKF LQYWGRIGSE NNMTSCHRPV CRKEGVLLDF STDGGITWTL LHEMDFQKYI
     SVRHDYILLP EGALTNTTRL RWWQPFVISN GLVVSGVERA QWALDNILIG GAEINPSQLV
     DTFDDEGSSH EENWSFYPNA VRTAGFCGNP SFHLYWPNKK KDKTHNALSS RELIIQPGYM
     MQFKIVVGCE ATSCGDLHSV MLEYTKDARS DSWQLVQTQC LPSSSNSIGC SPFQFHEATI
     YNAVNSSSWK RITIQLPDHV SSSATQFRWI QKGEETEKQS WAIDHVYIGE ACPKLCSGHG
     YCTTGAVCIC DESFQGDDCS VFSHELPSYI KDNFESARVT EANWETIQGG VIGSGCGQLA
     PYAHGDSLYF NGCQIRQAAT KPLDLTRASK IMFVLQIGSP AQTDSCNSDL SGPHTVDKAV
     LLQYSVNNGI TWHVIAQHQP KDFTQAQRVS YNVPLEARMK GVLLRWWQPR HNGTGHDQWA
     LDHVEVVLVS TRKQNYMMNF SRQHGLRHFY NRRRRSLRRY P
//
ID   STIP1_MOUSE             Reviewed;         543 AA.
AC   Q60864; Q3TT16; Q8BPH3; Q99L66;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Stress-induced-phosphoprotein 1;
DE            Short=STI1;
DE            Short=mSTI1;
DE   AltName: Full=Hsc70/Hsp90-organizing protein;
DE            Short=Hop;
GN   Name=Stip1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung carcinoma;
RX   MEDLINE=97417498; PubMed=9272871; DOI=10.1016/S0378-1119(97)00206-0;
RA   Blatch G.L., Laessle M., Zetter B.R., Kundra V.;
RT   "Isolation of a mouse cDNA encoding mSTI1, a stress-inducible protein
RT   containing the TPR motif.";
RL   Gene 194:277-282(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Liver, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-10; 94-109; 124-136; 145-169; 306-315; 352-364;
RP   435-446; 506-513 AND 534-543, ACETYLATION AT MET-1, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Kidney;
RA   Bienvenut W.V., Frezza C., Gottlieb E.;
RL   Submitted (MAY-2009) to UniProtKB.
RN   [5]
RP   PROTEIN SEQUENCE OF 14-44, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [6]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH HSC70; HSPCA AND HSPCB.
RX   MEDLINE=97153154; PubMed=8999875; DOI=10.1074/jbc.272.3.1876;
RA   Laessle M., Blatch G.L., Kundra V., Takatori T., Zetter B.R.;
RT   "Stress-inducible, murine protein mSTI1. Characterization of binding
RT   domains for heat shock proteins and in vitro phosphorylation by
RT   different kinases.";
RL   J. Biol. Chem. 272:1876-1884(1997).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Mediates the association of the molecular chaperones
CC       HSC70 and HSP90 (HSPCA and HSPCB).
CC   -!- SUBUNIT: Interacts with PACRG (By similarity). Forms a complex
CC       with HSC70 and HSPCA/HSP-86 and HSPCB/HSP-84.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- DOMAIN: The TPR 1 repeat interacts with the C-terminal of HSC70.
CC       The TPR 4, 5 and 6 repeats (also called TPR2A domain) and TPR 7, 8
CC       and 9 repeats (also called TPR2B domain) interact with HSP90 (By
CC       similarity).
CC   -!- PTM: In vitro kinase assay failed to detect phosphorylation by
CC       MAPKAPK2.
CC   -!- SIMILARITY: Contains 2 STI1 domains.
CC   -!- SIMILARITY: Contains 9 TPR repeats.
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DR   EMBL; U27830; AAC53267.1; -; mRNA.
DR   EMBL; AK075988; BAC36100.1; -; mRNA.
DR   EMBL; AK088494; BAC40389.1; -; mRNA.
DR   EMBL; AK149493; BAE28916.1; -; mRNA.
DR   EMBL; AK161645; BAE36509.1; -; mRNA.
DR   EMBL; AK167273; BAE39385.1; -; mRNA.
DR   EMBL; BC003794; AAH03794.1; -; mRNA.
DR   IPI; IPI00121514; -.
DR   RefSeq; NP_058017.1; NM_016737.2.
DR   UniGene; Mm.258633; -.
DR   ProteinModelPortal; Q60864; -.
DR   SMR; Q60864; 2-118, 223-499.
DR   STRING; Q60864; -.
DR   PhosphoSite; Q60864; -.
DR   REPRODUCTION-2DPAGE; IPI00121514; -.
DR   REPRODUCTION-2DPAGE; Q60864; -.
DR   UCD-2DPAGE; Q60864; -.
DR   PRIDE; Q60864; -.
DR   Ensembl; ENSMUST00000025918; ENSMUSP00000025918; ENSMUSG00000024966.
DR   GeneID; 20867; -.
DR   KEGG; mmu:20867; -.
DR   UCSC; uc008gke.1; mouse.
DR   CTD; 20867; -.
DR   MGI; MGI:109130; Stip1.
DR   GeneTree; ENSGT00600000084418; -.
DR   HOGENOM; HBG384096; -.
DR   HOVERGEN; HBG057820; -.
DR   InParanoid; Q60864; -.
DR   OMA; ENDPRTR; -.
DR   OrthoDB; EOG4FN4H9; -.
DR   PhylomeDB; Q60864; -.
DR   NextBio; 299693; -.
DR   ArrayExpress; Q60864; -.
DR   Bgee; Q60864; -.
DR   CleanEx; MM_STIP1; -.
DR   Genevestigator; Q60864; -.
DR   GermOnline; ENSMUSG00000024966; Mus musculus.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR006636; STI1_HS-bd.
DR   InterPro; IPR001440; TPR-1.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 3.
DR   Pfam; PF00515; TPR_1; 6.
DR   SMART; SM00727; STI1; 2.
DR   SMART; SM00028; TPR; 9.
DR   PROSITE; PS50005; TPR; 9.
DR   PROSITE; PS50293; TPR_REGION; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Nucleus;
KW   Phosphoprotein; Repeat; TPR repeat.
FT   CHAIN         1    543       Stress-induced-phosphoprotein 1.
FT                                /FTId=PRO_0000106373.
FT   REPEAT        4     37       TPR 1.
FT   REPEAT       39     71       TPR 2.
FT   REPEAT       73    105       TPR 3.
FT   DOMAIN      130    169       STI1 1.
FT   REPEAT      225    258       TPR 4.
FT   REPEAT      260    292       TPR 5.
FT   REPEAT      300    333       TPR 6.
FT   REPEAT      360    393       TPR 7.
FT   REPEAT      395    427       TPR 8.
FT   REPEAT      428    461       TPR 9.
FT   DOMAIN      492    531       STI1 2.
FT   MOTIF       222    239       Bipartite nuclear localization signal
FT                                (Potential).
FT   MOD_RES       1      1       N-acetylmethionine.
FT   MOD_RES       8      8       N6-acetyllysine (By similarity).
FT   MOD_RES      16     16       Phosphoserine (By similarity).
FT   MOD_RES      68     68       N6-acetyllysine (By similarity).
FT   MOD_RES      73     73       N6-acetyllysine (By similarity).
FT   MOD_RES     100    100       N6-acetyllysine (By similarity).
FT   MOD_RES     198    198       Phosphothreonine (By similarity).
FT   MOD_RES     246    246       N6-acetyllysine (By similarity).
FT   MOD_RES     301    301       N6-acetyllysine (By similarity).
FT   MOD_RES     312    312       N6-acetyllysine (By similarity).
FT   MOD_RES     325    325       N6-acetyllysine (By similarity).
FT   MOD_RES     344    344       N6-acetyllysine (By similarity).
FT   MOD_RES     354    354       Phosphotyrosine (By similarity).
FT   MOD_RES     388    388       N6-acetyllysine (By similarity).
FT   MOD_RES     446    446       N6-acetyllysine (By similarity).
FT   MOD_RES     481    481       Phosphoserine.
FT   CONFLICT     15     15       L -> P (in Ref. 2; BAC36100).
FT   CONFLICT    106    106       L -> V (in Ref. 3; AAH03794).
FT   CONFLICT    274    279       DYNKCR -> RLYKCT (in Ref. 2; BAC36100).
FT   CONFLICT    288    288       V -> S (in Ref. 2; BAC36100).
FT   CONFLICT    305    310       RIGNSY -> PNWQFL (in Ref. 2; BAC36100).
FT   CONFLICT    316    317       YK -> VQ (in Ref. 2; BAC36100).
FT   CONFLICT    333    347       PDVLKKCQQAEKILK -> QMCSRSASSQRNSE (in
FT                                Ref. 2; BAC36100).
SQ   SEQUENCE   543 AA;  62582 MW;  B737FBA92B198D6C CRC64;
     MEQVNELKEK GNKALSAGNI DDALQCYSEA IKLDPQNHVL YSNRSAAYAK KGDYQKAYED
     GCKTVDLKPD WGKGYSRKAA ALEFLNRFEE AKRTYEEGLK HEANNLQLKE GLQNMEARLA
     ERKFMNPFNL PNLYQKLEND PRTRSLLSDP TYRELIEQLQ NKPSDLGTKL QDPRVMTTLS
     VLLGVDLGSM DEEEEAATPP PPPPPKKEPK PEPMEEDLPE NKKQALKEKE LGNDAYKKKD
     FDKALKHYDR AKELDPTNMT YITNQAAVHF EKGDYNKCRE LCEKAIEVGR ENREDYRQIA
     KAYARIGNSY FKEEKYKDAI HFYNKSLAEH RTPDVLKKCQ QAEKILKEQE RLAYINPDLA
     LEEKNKGNEC FQKGDYPQAM KHYTEAIKRN PRDAKLYSNR AACYTKLLEF QLALKDCEEC
     IQLEPTFIKG YTRKAAALEA MKDYTKAMDV YQKALDLDSS CKEAADGYQR CMMAQYNRHD
     SPEDVKRRAM ADPEVQQIMS DPAMRLILEQ MQKDPQALSE HLKNPVIAQK IQKLMDVGLI
     AIR
//
ID   ARHG2_MOUSE             Reviewed;         985 AA.
AC   Q60875; O09115; Q3TBI4; Q3TJ16; Q8CHE1; Q923E0; Q9ESG7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 3.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Rho guanine nucleotide exchange factor 2;
DE   AltName: Full=Guanine nucleotide exchange factor H1;
DE            Short=GEF-H1;
DE   AltName: Full=LBC'S first cousin;
DE   AltName: Full=Lymphoid blast crisis-like 1;
DE   AltName: Full=Oncogene LFC;
DE   AltName: Full=Rhobin;
GN   Name=Arhgef2; Synonyms=Kiaa0651, Lbcl1, Lfc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Myeloid;
RX   MEDLINE=95355462; PubMed=7629163; DOI=10.1074/jbc.270.31.18388;
RA   Whitehead I., Kirk H., Tognon C., Trigo-Gonzalez G., Kay R.;
RT   "Expression cloning of lfc, a novel oncogene with structural
RT   similarities to guanine nucleotide exchange factors and to the
RT   regulatory region of protein kinase C.";
RL   J. Biol. Chem. 270:18388-18395(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   STRAIN=BALB/c;
RA   Olofsson B.;
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   De Sepulveda P., Rottapel R.;
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Brain;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=22502955; PubMed=12604587; DOI=10.1083/jcb.200211047;
RA   Benais-Pont G., Punn A., Flores-Maldonado C., Eckert J., Raposo G.,
RA   Fleming T.P., Cereijido M., Balda M.S., Matter K.;
RT   "Identification of a tight junction-associated guanine nucleotide
RT   exchange factor that activates Rho and regulates paracellular
RT   permeability.";
RL   J. Cell Biol. 160:729-740(2003).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-959, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   REVIEW ON FUNCTION.
RX   PubMed=18394899; DOI=10.1016/j.tcb.2008.02.006;
RA   Birkenfeld J., Nalbant P., Yoon S.-H., Bokoch G.M.;
RT   "Cellular functions of GEF-H1, a microtubule-regulated Rho-GEF: is
RT   altered GEF-H1 activity a crucial determinant of disease
RT   pathogenesis?";
RL   Trends Cell Biol. 18:210-219(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163; SER-646; SER-781;
RP   THR-795; SER-885; SER-931; SER-939; SER-940; THR-944; SER-955 AND
RP   SER-959, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Activates Rho-GTPases by promoting the exchange of GDP
CC       for GTP. May be involved in epithelial barrier permeability, cell
CC       motility and polarization, dendritic spine morphology, antigen
CC       presentation, leukemic cell differentiation, cell cycle
CC       regulation, and cancer. Binds Rac-GTPases, but does not seem to
CC       promote nucleotide exchange activity toward Rac-GTPases. May
CC       stimulate instead the cortical activity of Rac. Inactive toward
CC       CDC42, TC10, or Ras-GTPases. Forms an intracellular sensing system
CC       along with NOD1 for the detection of microbial effectors during
CC       cell invasion by pathogens (By similarity).
CC   -!- SUBUNIT: Interacts with 14-3-3 zeta; when phosphorylated at Ser-
CC       885. Interacts with the kinases PAK4, AURKA/STK6 and MAPK1.
CC       Interacts with RHOA and RAC1. Interacts with NOD1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell junction,
CC       tight junction. Golgi apparatus (By similarity). Cytoplasm,
CC       cytoskeleton, spindle (By similarity). Note=Localizes to the tips
CC       of cortical microtubules of the mitotic spindle during cell
CC       division, and is further released upon microtubule
CC       depolymerization (By similarity). Associated with apical
CC       intercellular junctions in the trophectoderm of the blastocyst.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q60875-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q60875-2; Sequence=VSP_022641;
CC       Name=3;
CC         IsoId=Q60875-3; Sequence=VSP_022640, VSP_022642, VSP_022643;
CC       Name=4;
CC         IsoId=Q60875-4; Sequence=VSP_034962;
CC       Name=5;
CC         IsoId=Q60875-5; Sequence=VSP_034962, VSP_034963;
CC   -!- TISSUE SPECIFICITY: Ubiquitous, with the exception of liver
CC       tissue. Levels are high in hemopoietic tissues (thymus, spleen,
CC       bone marrow) as well as in kidney and lung.
CC   -!- DOMAIN: The DH (DBL-homology) domain interacts with and promotes
CC       loading of GTP on RhoA.
CC   -!- DOMAIN: The PH (pleckstrin-homology) domain is involved in
CC       microtubule binding and targeting to tight junctions.
CC   -!- PTM: Phosphorylation of Ser-885 by PAK1 induces binding to protein
CC       14-3-3 zeta, promoting its relocation to microtubules and the
CC       inhibition of its activity. Phosphorylated by STK6 and CDK1 during
CC       mitosis, which negatively regulates its activity. Phosphorylation
CC       by MAPK1 or MAPK3 increases nucleotide exchange activity.
CC       Phosphorylation by PAK4 releases GEF-H1 from the microtubules (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC41438.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; U28495; AAC52234.1; -; mRNA.
DR   EMBL; X95761; CAA65067.1; -; mRNA.
DR   EMBL; AF177032; AAG09271.1; -; mRNA.
DR   EMBL; AB093254; BAC41438.1; ALT_INIT; mRNA.
DR   EMBL; AK167628; BAE39679.1; -; mRNA.
DR   EMBL; AK171223; BAE42325.1; -; mRNA.
DR   EMBL; BC006589; AAH06589.1; -; mRNA.
DR   IPI; IPI00310764; -.
DR   IPI; IPI00828540; -.
DR   IPI; IPI00828583; -.
DR   IPI; IPI00900401; -.
DR   IPI; IPI00900466; -.
DR   PIR; I49342; I49342.
DR   RefSeq; NP_001185841.1; NM_001198912.1.
DR   UniGene; Mm.239329; -.
DR   ProteinModelPortal; Q60875; -.
DR   SMR; Q60875; 36-87, 216-574.
DR   MINT; MINT-4115919; -.
DR   STRING; Q60875; -.
DR   PRIDE; Q60875; -.
DR   Ensembl; ENSMUST00000029694; ENSMUSP00000029694; ENSMUSG00000028059.
DR   Ensembl; ENSMUST00000107510; ENSMUSP00000103134; ENSMUSG00000028059.
DR   GeneID; 16800; -.
DR   UCSC; uc008pvw.1; mouse.
DR   MGI; MGI:103264; Arhgef2.
DR   eggNOG; roNOG14875; -.
DR   GeneTree; ENSGT00600000084265; -.
DR   HOVERGEN; HBG050566; -.
DR   InParanoid; Q60875; -.
DR   OrthoDB; EOG43FGW6; -.
DR   ArrayExpress; Q60875; -.
DR   Bgee; Q60875; -.
DR   Genevestigator; Q60875; -.
DR   GermOnline; ENSMUSG00000028059; Mus musculus.
DR   GO; GO:0043198; C:dendritic shaft; IDA:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0048365; F:Rac GTPase binding; ISS:UniProtKB.
DR   GO; GO:0030676; F:Rac guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000902; P:cell morphogenesis; ISS:UniProtKB.
DR   GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISS:UniProtKB.
DR   GO; GO:0050768; P:negative regulation of neurogenesis; IMP:UniProtKB.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IDA:MGI.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR015721; RhoGEF-like.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   PANTHER; PTHR22825; RhoGEF_like; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   PROSITE; PS00741; DH_1; FALSE_NEG.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell cycle; Cell division;
KW   Cell junction; Coiled coil; Cytoplasm; Cytoskeleton; Golgi apparatus;
KW   Guanine-nucleotide releasing factor; Metal-binding; Microtubule;
KW   Mitosis; Phosphoprotein; Proto-oncogene; Tight junction; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    985       Rho guanine nucleotide exchange factor 2.
FT                                /FTId=PRO_0000080910.
FT   DOMAIN      236    433       DH.
FT   DOMAIN      473    572       PH.
FT   ZN_FING      39     86       Phorbol-ester/DAG-type.
FT   COILED      591    619       Potential.
FT   COILED      797    866       Potential.
FT   COMPBIAS    493    496       Poly-Leu.
FT   MOD_RES     143    143       Phosphoserine; by PAK4 (By similarity).
FT   MOD_RES     149    149       Phosphoserine (By similarity).
FT   MOD_RES     151    151       Phosphoserine (By similarity).
FT   MOD_RES     152    152       Phosphothreonine (By similarity).
FT   MOD_RES     153    153       Phosphothreonine (By similarity).
FT   MOD_RES     163    163       Phosphoserine.
FT   MOD_RES     172    172       Phosphoserine (By similarity).
FT   MOD_RES     174    174       Phosphoserine (By similarity).
FT   MOD_RES     177    177       Phosphoserine (By similarity).
FT   MOD_RES     354    354       N6-acetyllysine (By similarity).
FT   MOD_RES     646    646       Phosphoserine.
FT   MOD_RES     649    649       Phosphoserine (By similarity).
FT   MOD_RES     680    680       Phosphothreonine; by MAPK1 or MAPK3 (By
FT                                similarity).
FT   MOD_RES     692    692       Phosphoserine (By similarity).
FT   MOD_RES     781    781       Phosphoserine.
FT   MOD_RES     795    795       Phosphothreonine.
FT   MOD_RES     885    885       Phosphoserine; by PAK1 and STK6 (By
FT                                similarity).
FT   MOD_RES     893    893       Phosphotyrosine (By similarity).
FT   MOD_RES     895    895       Phosphoserine; by PAK4 (By similarity).
FT   MOD_RES     931    931       Phosphoserine.
FT   MOD_RES     939    939       Phosphoserine.
FT   MOD_RES     940    940       Phosphoserine.
FT   MOD_RES     944    944       Phosphothreonine.
FT   MOD_RES     946    946       Phosphoserine (By similarity).
FT   MOD_RES     952    952       Phosphoserine (By similarity).
FT   MOD_RES     955    955       Phosphoserine.
FT   MOD_RES     959    959       Phosphoserine.
FT   VAR_SEQ       1     27       Missing (in isoform 4 and isoform 5).
FT                                /FTId=VSP_034962.
FT   VAR_SEQ       1     21       MSRIESLTRARIDRSKEQATK -> MSGNRRQPSRRGQ
FT                                (in isoform 3).
FT                                /FTId=VSP_022640.
FT   VAR_SEQ     112    113       Missing (in isoform 5).
FT                                /FTId=VSP_034963.
FT   VAR_SEQ     574    985       Missing (in isoform 2).
FT                                /FTId=VSP_022641.
FT   VAR_SEQ     596    596       T -> S (in isoform 3).
FT                                /FTId=VSP_022642.
FT   VAR_SEQ     597    985       Missing (in isoform 3).
FT                                /FTId=VSP_022643.
FT   CONFLICT    156    156       A -> V (in Ref. 2; CAA65067).
FT   CONFLICT    539    539       M -> V (in Ref. 3; AAG09271).
FT   CONFLICT    679    679       T -> M (in Ref. 5; BAE39679/BAE42325).
FT   CONFLICT    810    810       H -> Y (in Ref. 5; BAE42325).
FT   CONFLICT    941    941       D -> G (in Ref. 3; AAG09271).
SQ   SEQUENCE   985 AA;  111944 MW;  EA5091F97F8FD865 CRC64;
     MSRIESLTRA RIDRSKEQAT KTREKEKMKE AKDARYTNGH LFTTISVSGM TMCYACNKSI
     TAKEALICPT CNVTIHNRCK DTLANCTKVK QKQQKAALLR NNTALQSVSL RSKTTTRERP
     TSAIYPSDSF RQSLLGSRRG LSSLSLAKSV STTNIAGHFN DESPLGLRQI LSQSTDSLNM
     RNRTLSVESL IDEGVEVFYN ELMSDFEMDE KDFEADSWSL AVDSSFLQQH KKEVMKKQDV
     IYELIQTELH HVRTLKIMTR LFRTGMLEEL QMEPEVVQGL FPCVDELSDI HTRFLNQLLE
     RRRQALCPGS TRNFVIHRLG DLLISQFSGS NAEQMRKTYS EFCSRHTKAL KLYKELYARD
     KRFQQFIRKM TRSAVLKRHG VQECILLVTQ RITKYPVLIN RILQNSHGVE EEYQDLASAL
     GLVKELLSNV DQDVHELEKE ARLQEIYNRM DPRAQTPVPG KGPFGRDELL RRKLIHEGCL
     LWKTATGRFK DVLLLLMTDV LVFLQEKDQK YIFTSLDKPS VVSLQNLIVR DIANQAKGMF
     LISSGPPEMY EVHAASRDDR TTWIRVIQQS VRLCPSREDF PLIETEDKAY LRRIKTKLQQ
     KNQALVELLQ KNVELFAEMV HFQALKAGFV GMPPPALPRG LFRLESFESL RGERLLKDAL
     REVEGLKDLL LGPCVDLPTT SREPALPLDS DSGSCPGVTA NGEARTFNGS IELCRADSDS
     SQKDRNGNQL RSPQEEVLQP LINLYGLLHG LQAVVVQQER LMEALFPEGP ERWEKLSRAN
     SRDGEAGRAA VASVTPEKQA TELALLQRQH TLLQEELRRC QRLGEERATE AGSLEARLRE
     SEQARALLER EAEEIRRQLA ALGQNEPLPA EAPWARRPLD PRRRSLPAGD ALYLSFNPPQ
     PSRGHDRLDL PVTVRSLHRP FDDREAQELG SPEDRLQDSS DPDTGSEEEV SSRLSPPHSP
     RDFTRMQDIP EETESRDGEP TASES
//
ID   ELAV2_MOUSE             Reviewed;         360 AA.
AC   Q60899;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-FEB-2011, entry version 79.
DE   RecName: Full=ELAV-like protein 2;
DE   AltName: Full=ELAV-like neuronal protein 1;
DE   AltName: Full=Hu-antigen B;
DE            Short=HuB;
DE   AltName: Full=Nervous system-specific RNA-binding protein Mel-N1;
GN   Name=Elavl2; Synonyms=Hub;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   MEDLINE=96251080; PubMed=8668530; DOI=10.1093/nar/24.11.2011;
RA   Abe R., Yamamoto K., Sakamoto H.;
RT   "Target specificity of neuronal RNA-binding protein, Mel-N1: direct
RT   binding to the 3' untranslated region of its own mRNA.";
RL   Nucleic Acids Res. 24:2011-2016(1996).
CC   -!- FUNCTION: Binds RNA. Seems to recognize a GAAA motif. Can bind to
CC       its own 3'-UTR, the FOS 3'-UTR and the ID 3'-UTR.
CC   -!- SUBUNIT: Interacts with IGF2BP1 (By similarity).
CC   -!- TISSUE SPECIFICITY: Brain; neural-specific.
CC   -!- SIMILARITY: Belongs to the RRM elav family.
CC   -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.
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DR   EMBL; U29088; AAC52644.1; -; mRNA.
DR   IPI; IPI00121676; -.
DR   PIR; JC6057; JC6057.
DR   RefSeq; NP_034616.1; NM_010486.2.
DR   UniGene; Mm.318042; -.
DR   ProteinModelPortal; Q60899; -.
DR   SMR; Q60899; 37-359.
DR   STRING; Q60899; -.
DR   PhosphoSite; Q60899; -.
DR   PRIDE; Q60899; -.
DR   Ensembl; ENSMUST00000008633; ENSMUSP00000008633; ENSMUSG00000008489.
DR   Ensembl; ENSMUST00000107114; ENSMUSP00000102731; ENSMUSG00000008489.
DR   Ensembl; ENSMUST00000107116; ENSMUSP00000102733; ENSMUSG00000008489.
DR   Ensembl; ENSMUST00000107124; ENSMUSP00000102741; ENSMUSG00000008489.
DR   GeneID; 15569; -.
DR   KEGG; mmu:15569; -.
DR   NMPDR; fig|10090.3.peg.9895; -.
DR   UCSC; uc008ton.1; mouse.
DR   CTD; 15569; -.
DR   MGI; MGI:1100887; Elavl2.
DR   GeneTree; ENSGT00560000077064; -.
DR   HOVERGEN; HBG002295; -.
DR   InParanoid; Q60899; -.
DR   PhylomeDB; Q60899; -.
DR   NextBio; 288546; -.
DR   ArrayExpress; Q60899; -.
DR   Bgee; Q60899; -.
DR   Genevestigator; Q60899; -.
DR   GermOnline; ENSMUSG00000008489; Mus musculus.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR006548; ELAD_HUD_SF.
DR   InterPro; IPR002343; Hud_Sxl_RNA.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 3.
DR   Pfam; PF00076; RRM_1; 3.
DR   PRINTS; PR00961; HUDSXLRNA.
DR   SMART; SM00360; RRM; 3.
DR   TIGRFAMs; TIGR01661; ELAV_HUD_SF; 1.
DR   PROSITE; PS50102; RRM; 3.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Repeat; RNA-binding.
FT   CHAIN         1    360       ELAV-like protein 2.
FT                                /FTId=PRO_0000081580.
FT   DOMAIN       39    117       RRM 1.
FT   DOMAIN      125    205       RRM 2.
FT   DOMAIN      277    355       RRM 3.
FT   MOD_RES     221    221       Phosphoserine (By similarity).
SQ   SEQUENCE   360 AA;  39577 MW;  780CDD07F2E97D74 CRC64;
     METQLSNGPT CNNTANGPTT VNNNCSSPVD SGNTEDSKTN LIVNYLPQNM TQEELKSLFG
     SIGEIESCKL VRDKITGQSL GYGFVNYIDP KDAEKAINTL NGLRLQTKTI KVSYARPSSA
     SIRDANLYVS GLPKTMTQKE LEQLFSQYGR IITSRILVDQ VTGISRGVGF IRFDKRIEAE
     EAIKGLNGQK PPGATEPITV KFANNPSQKT NQAILSQLYQ SPNRRYPGPL AQQAQRFRLD
     NLLNMAYGVK SRFSPMTIDG MTSLAGINIP GHPGTGWCIF VYNLAPDADE SILWQMFGPF
     GAVTNVKVIR DFNTNKCKGF GFVTMTNYDE AAMAIASLNG YRLGDRVLQV SFKTNKTHKA
//
ID   MEF2A_MOUSE             Reviewed;         498 AA.
AC   Q60929; Q3V155; Q4VA09; Q6P8Q3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Myocyte-specific enhancer factor 2A;
GN   Name=Mef2a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   DEVEPOMENTAL STAGE.
RC   TISSUE=Cerebellum;
RX   MEDLINE=97165895; PubMed=9013788; DOI=10.1016/S0169-328X(96)00135-0;
RA   Lin X., Shah S., Bulleit R.F.;
RT   "The expression of MEF2 genes is implicated in CNS neuronal
RT   differentiation.";
RL   Brain Res. Mol. Brain Res. 42:307-316(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=NMRI; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH HDAC7.
RX   MEDLINE=21601647; PubMed=11585834; DOI=10.1074/jbc.M107631200;
RA   Kao H.-Y., Verdel A., Tsai C.-C., Simon C., Juguilon H., Khochbin S.;
RT   "Mechanism for nucleocytoplasmic shuttling of histone deacetylase 7.";
RL   J. Biol. Chem. 276:47496-47507(2001).
RN   [5]
RP   TISSUE SPECIFICITY OF ISOFORMS.
RX   PubMed=15834131; DOI=10.1074/jbc.M502491200;
RA   Zhu B., Ramachandran B., Gulick T.;
RT   "Alternative pre-mRNA splicing governs expression of a conserved
RT   acidic transactivation domain in myocyte enhancer factor 2 factors of
RT   striated muscle and brain.";
RL   J. Biol. Chem. 280:28749-28760(2005).
RN   [6]
RP   INTERACTION WITH NLK, AND PHOSPHORYLATION AT THR-310.
RX   PubMed=17785444; DOI=10.1128/MCB.01481-07;
RA   Satoh K., Ohnishi J., Sato A., Takeyama M., Iemura S., Natsume T.,
RA   Shibuya H.;
RT   "Nemo-like kinase-myocyte enhancer factor 2A signaling regulates
RT   anterior formation in Xenopus development.";
RL   Mol. Cell. Biol. 27:7623-7630(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 (ISOFORM 1),
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 AND THR-108 (ISOFORM
RP   3), AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Transcriptional activator which binds specifically to
CC       the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-
CC       specific genes. Also involved in the activation of numerous growth
CC       factor- and stress-induced genes. Mediates cellular functions not
CC       only in skeletal and cardiac muscle development, but also in
CC       neuronal differentiation and survival. Plays diverse roles in the
CC       control of cell growth, survival and apoptosis via p38 MAPK
CC       signaling in muscle-specific and/or growth factor-related
CC       transcription. In cerebellar granule neurons, phosphorylated and
CC       sumoylated MEF2A represses transcription of NUR77 promoting
CC       synaptic differentiation (By similarity).
CC   -!- SUBUNIT: Binds DNA as a homo- or heterodimer. Dimerizes with
CC       MEF2D. Interacts with HDAC7. Interacts with PIAS1; the interaction
CC       enhances sumoylation. Interacts with HDAC4, HDAC9 and SLC2A4RG.
CC       Interacts (via the N-terminal) with MAPK7; the interaction results
CC       in the phosphorylation and transcriptional activity of MEF2A (By
CC       similarity).
CC   -!- INTERACTION:
CC       P70257-2:Nfix; NbExp=1; IntAct=EBI-2639094, EBI-2639084;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q60929-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q60929-2; Sequence=VSP_026031;
CC       Name=3;
CC         IsoId=Q60929-3; Sequence=VSP_026060, VSP_026031;
CC         Note=Phosphorylated on Ser-98 and Thr-108;
CC   -!- TISSUE SPECIFICITY: Widely expressed though mainly restricted to
CC       skeletal and cardiac muscle, brain, neurons and lymphocytes.
CC       Differentially expressed depending on if isoforms contain the beta
CC       domain or not, with the total expression of the beta domain-
CC       lacking isoforms vastly exceding that of the beta domain-
CC       containing isoforms. Isoforms containing the beta domain are
CC       expressed primarily in skeletal and cardiac muscle and in brain.
CC       Also present in lung and testis. Splicing to include the beta
CC       domain is induced in differentiating myocytes. Isoforms lacking
CC       the beta domain are expressed less abundantly in skeletal muscle,
CC       brain and lymphocytes, and are uniquely found in ovary, liver,
CC       spleen and kidney. In embryos, the beta domain-containing and beta
CC       domain-lacking isoforms are equally expressed. Also expressed
CC       cerebellar granule neurons and other regions of the CNS. Highest
CC       levels in the olfactory bulb, cortex, hippocampus, thalamus and
CC       cerebellum.
CC   -!- DEVELOPMENTAL STAGE: In the developing cerebellum, increasing
CC       levels after birth. The majority of this increase occurs around
CC       postnataL day 9 reaching a peak at postnatal day 15-18 which is
CC       maintained in adults.
CC   -!- DOMAIN: The beta domain, missing in a number of isoforms, is
CC       required for enhancement of transcriptional activity (By
CC       similarity).
CC   -!- PTM: Constitutive phosphorylation on Ser-406 promotes Lys-401
CC       sumoylation thus preventing acetylation at this site.
CC       Dephosphorylation on Ser-406 by PPP3CA upon neuron depolarization
CC       promotes a switch from sumoylation to acetylation on residue Lys-
CC       403 leading to inhibition of dendrite claw differentiation.
CC       Phosphorylation on Thr-312 and Thr-319 are the main sites involved
CC       in p38 MAPK signaling and activate transcription. Phosphorylated
CC       on these sites by MAPK14/p38alpha and MAPK11/p38beta, but not by
CC       MAPK13/p38delta nor by MAPK12/p38gamma. Phosphorylation on Ser-408
CC       by CDK5 induced by neurotoxicity inhibits MEF2A transcriptional
CC       activation leading to apoptosis of cortical neurons.
CC       Phosphorylation on Thr-312, Thr-319 and Ser-355 can be induced by
CC       EGF (By similarity). Isoform 3 is phosphorylated on Ser-98 and
CC       Thr-108.
CC   -!- PTM: Sumoylation on Lys-401 is enhanced by PIAS1 and represses
CC       transcriptional activity. Phosphorylation on Ser-406 is required
CC       for sumoylation. Has no effect on nuclear location nor on DNA
CC       binding. Sumoylated by SUMO1 and, to a lesser extent by SUMO2 and
CC       SUMO3. PIASx facilitates sumoylation in postsynaptic dendrites in
CC       the cerebellar cortex and promotes their morphogenesis (By
CC       similarity).
CC   -!- PTM: Acetylation on Lys-401 activates transcriptional activity.
CC       Acetylated by p300 on several sites in diffentiating myocytes.
CC       Acetylation on Lys-4 increases DNA binding and transactivation.
CC       Hyperacetylation by p300 leads to enhanced cardiac myocyte growth
CC       and heart failure (By similarity).
CC   -!- PTM: Proteolytically cleaved in cerebellar granule neurons on
CC       several sites by caspase 3 and caspase 7 following neurotoxicity.
CC       Preferentially cleaves the CDK5-mediated hyperphosphorylated form
CC       which leads to neuron apoptosis and transcriptional inactivation
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the MEF2 family.
CC   -!- SIMILARITY: Contains 1 MADS-box domain.
CC   -!- SIMILARITY: Contains 1 Mef2-type DNA-binding domain.
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DR   EMBL; U30823; AAA74030.1; -; mRNA.
DR   EMBL; AK132678; BAE21297.1; -; mRNA.
DR   EMBL; BC061128; AAH61128.1; -; mRNA.
DR   EMBL; BC096598; AAH96598.1; -; mRNA.
DR   IPI; IPI00420437; -.
DR   IPI; IPI00465749; -.
DR   IPI; IPI00607917; -.
DR   RefSeq; NP_001028885.1; NM_001033713.1.
DR   UniGene; Mm.132788; -.
DR   UniGene; Mm.480401; -.
DR   ProteinModelPortal; Q60929; -.
DR   SMR; Q60929; 2-73.
DR   IntAct; Q60929; 4.
DR   MINT; MINT-3155471; -.
DR   STRING; Q60929; -.
DR   PhosphoSite; Q60929; -.
DR   PRIDE; Q60929; -.
DR   Ensembl; ENSMUST00000032776; ENSMUSP00000032776; ENSMUSG00000030557.
DR   GeneID; 17258; -.
DR   KEGG; mmu:17258; -.
DR   CTD; 17258; -.
DR   MGI; MGI:99532; Mef2a.
DR   eggNOG; roNOG06368; -.
DR   GeneTree; ENSGT00390000011828; -.
DR   HOGENOM; HBG443633; -.
DR   HOVERGEN; HBG053944; -.
DR   InParanoid; Q60929; -.
DR   OMA; RMDTWVT; -.
DR   OrthoDB; EOG4XWFXW; -.
DR   NextBio; 291742; -.
DR   ArrayExpress; Q60929; -.
DR   Bgee; Q60929; -.
DR   CleanEx; MM_MEF2A; -.
DR   Genevestigator; Q60929; -.
DR   GermOnline; ENSMUSG00000030557; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0016563; F:transcription activator activity; IDA:MGI.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IDA:MGI.
DR   InterPro; IPR022102; HJURP_C.
DR   InterPro; IPR002100; TF_MADSbox.
DR   Pfam; PF12347; HJURP_C; 1.
DR   Pfam; PF00319; SRF-TF; 1.
DR   PRINTS; PR00404; MADSDOMAIN.
DR   SMART; SM00432; MADS; 1.
DR   SUPFAM; SSF55455; TF_MADSbox; 1.
DR   PROSITE; PS00350; MADS_BOX_1; 1.
DR   PROSITE; PS50066; MADS_BOX_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Alternative splicing; Apoptosis;
KW   Developmental protein; Differentiation; DNA-binding; Isopeptide bond;
KW   Neurogenesis; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN         1    498       Myocyte-specific enhancer factor 2A.
FT                                /FTId=PRO_0000199429.
FT   DOMAIN        3     57       MADS-box.
FT   DNA_BIND     58     86       Mef2-type (Potential).
FT   REGION      264    281       Required for interaction with MAPKs (By
FT                                similarity).
FT   REGION      287    294       Beta domain (By similarity).
FT   COMPBIAS    254    257       Poly-Pro.
FT   COMPBIAS    288    293       Poly-Glu.
FT   COMPBIAS    418    439       Gln/Pro-rich.
FT   COMPBIAS    448    455       Poly-Ser.
FT   SITE        174    175       Cleavage (Probable).
FT   SITE        211    212       Cleavage (Probable).
FT   SITE        457    458       Cleavage (Probable).
FT   MOD_RES       4      4       N6-acetyllysine (By similarity).
FT   MOD_RES      59     59       Phosphoserine; by CK2 (By similarity).
FT   MOD_RES      98     98       Phosphoserine.
FT   MOD_RES     117    117       N6-acetyllysine (By similarity).
FT   MOD_RES     233    233       Phosphoserine (By similarity).
FT   MOD_RES     247    247       N6-acetyllysine (By similarity).
FT   MOD_RES     252    252       N6-acetyllysine (By similarity).
FT   MOD_RES     253    253       Phosphoserine (By similarity).
FT   MOD_RES     268    268       N6-acetyllysine (By similarity).
FT   MOD_RES     280    280       N6-acetyllysine (By similarity).
FT   MOD_RES     310    310       Phosphothreonine; by MAPK7 (By
FT                                similarity).
FT   MOD_RES     310    310       Phosphothreonine; by NLK.
FT   MOD_RES     317    317       Phosphothreonine; by MAPK7 (By
FT                                similarity).
FT   MOD_RES     353    353       Phosphoserine; by MAPK7 (By similarity).
FT   MOD_RES     401    401       N6-acetyllysine; alternate (By
FT                                similarity).
FT   MOD_RES     406    406       Phosphoserine (By similarity).
FT   CROSSLNK    401    401       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO);
FT                                alternate (By similarity).
FT   VAR_SEQ      87    130       TLRKKGLNGCESPDADDYFEHSPLSEDRFSKLNEDSDFIFK
FT                                RGP -> ALNKKEHRGCDSPDPDTSYVLTPHTEEKYKKINE
FT                                EFDNMMRNHKIA (in isoform 3).
FT                                /FTId=VSP_026060.
FT   VAR_SEQ     287    294       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_026031.
FT   CONFLICT     98     98       S -> N (in Ref. 1; AAA74030).
FT   CONFLICT    116    116       S -> I (in Ref. 1; AAA74030).
FT   CONFLICT    133    133       L -> F (in Ref. 1; AAA74030).
FT   CONFLICT    151    151       A -> P (in Ref. 1; AAA74030).
FT   CONFLICT    154    154       Y -> D (in Ref. 1; AAA74030).
FT   CONFLICT    174    175       DS -> ET (in Ref. 1; AAA74030).
FT   CONFLICT    201    201       G -> S (in Ref. 2; BAE21297).
FT   CONFLICT    274    274       V -> A (in Ref. 1; AAA74030).
FT   CONFLICT    367    367       Q -> E (in Ref. 1; AAA74030).
FT   CONFLICT    373    374       AA -> TT (in Ref. 1; AAA74030).
FT   CONFLICT    419    423       QQQQQ -> HHHHH (in Ref. 1; AAA74030).
FT   CONFLICT    478    478       P -> A (in Ref. 1; AAA74030).
SQ   SEQUENCE   498 AA;  53579 MW;  FE291C3E3E0A5E70 CRC64;
     MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS SNKLFQYAST
     DMDKVLLKYT EYNEPHESRT NSDIVETLRK KGLNGCESPD ADDYFEHSPL SEDRFSKLNE
     DSDFIFKRGP PGLPPQNFSM SVTVPVTSPN ALSYTNPGSS LVSPSLAASS TLADSSMLSP
     PPATLHRNVS PGAPQRPPST GSASGMLSTT DLTVPNGAGN SPVGNGFVNS RASPNLIGNT
     GANSLGKVMP TKSPPPPGGG SLGMNSRKPD LRVVIPPSSK GMMPPLSEEE ELELNAQRIS
     SSQATQPLAT PVVSVTTPSL PPQGLVYSAM PTAYNTDYSL TSADLSALQG FTSPGMLSLG
     QASAWQQHHL GQAALSSLVA GGQLSQGSNL SINTNQNINI KSEPISPPRD RMTPSGFQQQ
     QQQPQQQPPP QPPQPQPRQE MGRSPVDSLS SSSSSYDGSD REDPRGDFHS PIVLGRPPNT
     EDRESPSVKR MRMDTWVT
//
ID   VDAC2_MOUSE             Reviewed;         295 AA.
AC   Q60930; Q78MH6; Q99L98;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 2.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Voltage-dependent anion-selective channel protein 2;
DE            Short=VDAC-2;
DE            Short=mVDAC2;
DE   AltName: Full=Outer mitochondrial membrane protein porin 2;
DE   AltName: Full=Voltage-dependent anion-selective channel protein 6;
DE            Short=VDAC-6;
DE            Short=mVDAC6;
GN   Name=Vdac2; Synonyms=Vdac6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=96301405; PubMed=8660977; DOI=10.1006/geno.1996.0193;
RA   Sampson M.J., Lovell R.S., Craigen W.J.;
RT   "Isolation, characterization, and mapping of two mouse mitochondrial
RT   voltage-dependent anion channel isoforms.";
RL   Genomics 33:283-288(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, and C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RA   Brathwaite M.E., Waeltz P., Qian Y., Dudekula D., Schlessinger D.,
RA   Nagaraja R.;
RT   "Genomic sequence analysis in the mouse T-complex region.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 33-40; 47-65; 76-121; 179-230 AND 237-278, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-32 AND LYS-75, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-207, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Forms a channel through the mitochondrial outer membrane
CC       that allows diffusion of small hydrophilic molecules. The channel
CC       adopts an open conformation at low or zero membrane potential and
CC       a closed conformation at potentials above 30-40 mV. The open state
CC       has a weak anion selectivity whereas the closed state is cation-
CC       selective (By similarity).
CC   -!- SUBUNIT: Interacts with hexokinases (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane.
CC   -!- TISSUE SPECIFICITY: Highest levels of expression detected in
CC       testis, less but still abundant expression in heart, kidney,
CC       brain, and skeletal muscle.
CC   -!- DOMAIN: Consists mainly of a membrane-spanning beta-barrel formed
CC       by 19 beta-strands (By similarity).
CC   -!- SIMILARITY: Belongs to the eukaryotic mitochondrial porin family.
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DR   EMBL; U30838; AAC13321.1; -; mRNA.
DR   EMBL; AK168199; BAE40159.1; -; mRNA.
DR   EMBL; AK159561; BAE35185.1; -; mRNA.
DR   EMBL; AK152274; BAE31090.1; -; mRNA.
DR   EMBL; AK150940; BAE29975.1; -; mRNA.
DR   EMBL; AK150627; BAE29717.1; -; mRNA.
DR   EMBL; AK150504; BAE29617.1; -; mRNA.
DR   EMBL; AK012359; BAE43231.1; -; mRNA.
DR   EMBL; AY294423; AAQ01516.1; -; Genomic_DNA.
DR   EMBL; BC003731; AAH03731.2; -; mRNA.
DR   IPI; IPI00122547; -.
DR   RefSeq; NP_035825.1; NM_011695.2.
DR   UniGene; Mm.262327; -.
DR   ProteinModelPortal; Q60930; -.
DR   SMR; Q60930; 13-295.
DR   STRING; Q60930; -.
DR   PhosphoSite; Q60930; -.
DR   REPRODUCTION-2DPAGE; Q60930; -.
DR   PRIDE; Q60930; -.
DR   Ensembl; ENSMUST00000022293; ENSMUSP00000022293; ENSMUSG00000021771.
DR   GeneID; 22334; -.
DR   KEGG; mmu:22334; -.
DR   UCSC; uc007sls.1; mouse.
DR   CTD; 22334; -.
DR   MGI; MGI:106915; Vdac2.
DR   eggNOG; roNOG11568; -.
DR   GeneTree; ENSGT00390000011336; -.
DR   HOGENOM; HBG396026; -.
DR   HOVERGEN; HBG054036; -.
DR   InParanoid; Q60930; -.
DR   OMA; LETKYKR; -.
DR   OrthoDB; EOG4T4CVZ; -.
DR   PhylomeDB; Q60930; -.
DR   NextBio; 302579; -.
DR   ArrayExpress; Q60930; -.
DR   Bgee; Q60930; -.
DR   CleanEx; MM_VDAC2; -.
DR   Genevestigator; Q60930; -.
DR   GermOnline; ENSMUSG00000021771; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR   GO; GO:0008308; F:voltage-gated anion channel activity; IEA:InterPro.
DR   InterPro; IPR001925; Porin_Euk.
DR   Pfam; PF01459; Porin_3; 1.
DR   PRINTS; PR00185; EUKARYTPORIN.
DR   PROSITE; PS00558; EUKARYOTIC_PORIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Ion transport; Membrane;
KW   Mitochondrion; Mitochondrion outer membrane; NAD; Nucleotide-binding;
KW   Phosphoprotein; Porin; Transmembrane; Transmembrane beta strand;
KW   Transport.
FT   CHAIN         1    295       Voltage-dependent anion-selective channel
FT                                protein 2.
FT                                /FTId=PRO_0000050506.
FT   TRANSMEM     38     47       Beta stranded; (By similarity).
FT   TRANSMEM     51     59       Beta stranded; (By similarity).
FT   TRANSMEM     66     76       Beta stranded; (By similarity).
FT   TRANSMEM     81     88       Beta stranded; (By similarity).
FT   TRANSMEM     92    101       Beta stranded; (By similarity).
FT   TRANSMEM    107    116       Beta stranded; (By similarity).
FT   TRANSMEM    123    132       Beta stranded; (By similarity).
FT   TRANSMEM    135    142       Beta stranded; (By similarity).
FT   TRANSMEM    149    157       Beta stranded; (By similarity).
FT   TRANSMEM    162    170       Beta stranded; (By similarity).
FT   TRANSMEM    175    187       Beta stranded; (By similarity).
FT   TRANSMEM    190    197       Beta stranded; (By similarity).
FT   TRANSMEM    201    210       Beta stranded; (By similarity).
FT   TRANSMEM    214    223       Beta stranded; (By similarity).
FT   TRANSMEM    230    239       Beta stranded; (By similarity).
FT   TRANSMEM    243    250       Beta stranded; (By similarity).
FT   TRANSMEM    254    263       Beta stranded; (By similarity).
FT   TRANSMEM    266    275       Beta stranded; (By similarity).
FT   TRANSMEM    285    294       Beta stranded; (By similarity).
FT   NP_BIND     254    256       NAD (By similarity).
FT   NP_BIND     272    276       NAD (By similarity).
FT   SITE         85     85       Involved in hexokinase binding (By
FT                                similarity).
FT   MOD_RES      32     32       N6-acetyllysine.
FT   MOD_RES      40     40       N6-acetyllysine (By similarity).
FT   MOD_RES      73     73       N6-acetyllysine (By similarity).
FT   MOD_RES      75     75       N6-acetyllysine.
FT   MOD_RES     116    116       Phosphoserine (By similarity).
FT   MOD_RES     207    207       Phosphotyrosine.
FT   MOD_RES     237    237       Phosphotyrosine (By similarity).
FT   CONFLICT    260    260       T -> A (in Ref. 4; AAH03731).
SQ   SEQUENCE   295 AA;  31733 MW;  7BBCDC625AD013C7 CRC64;
     MAECCVPVCP RPMCIPPPYA DLGKAARDIF NKGFGFGLVK LDVKTKSCSG VEFSTSGSSN
     TDTGKVSGTL ETKYKWCEYG LTFTEKWNTD NTLGTEIAIE DQICQGLKLT FDTTFSPNTG
     KKSGKIKSAY KRECINLGCD VDFDFAGPAI HGSAVFGYEG WLAGYQMTFD SAKSKLTRSN
     FAVGYRTGDF QLHTNVNNGT EFGGSIYQKV CEDFDTSVNL AWTSGTNCTR FGIAAKYQLD
     PTASISAKVN NSSLIGVGYT QTLRPGVKLT LSALVDGKSF NAGGHKLGLA LELEA
//
ID   VDAC1_MOUSE             Reviewed;         296 AA.
AC   Q60932; B1ASZ9; Q5SVC6;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 3.
DT   08-FEB-2011, entry version 98.
DE   RecName: Full=Voltage-dependent anion-selective channel protein 1;
DE            Short=VDAC-1;
DE            Short=mVDAC1;
DE   AltName: Full=Outer mitochondrial membrane protein porin 1;
DE   AltName: Full=Plasmalemmal porin;
DE   AltName: Full=Voltage-dependent anion-selective channel protein 5;
DE            Short=VDAC-5;
DE            Short=mVDAC5;
GN   Name=Vdac1; Synonyms=Vdac5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MT-VDAC1), AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=96301405; PubMed=8660977; DOI=10.1006/geno.1996.0193;
RA   Sampson M.J., Lovell R.S., Craigen W.J.;
RT   "Isolation, characterization, and mapping of two mouse mitochondrial
RT   voltage-dependent anion channel isoforms.";
RL   Genomics 33:283-288(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS MT-VDAC1 AND
RP   PL-VDAC1), FUNCTION, AND SUBCELLULAR LOCATION.
RX   MEDLINE=20202612; PubMed=10716730; DOI=10.1073/pnas.060242297;
RA   Buettner R., Papoutsoglou G., Scemes E., Spray D.C., Dermietzel R.;
RT   "Evidence for secretory pathway localization of a voltage-dependent
RT   anion channel isoform.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:3201-3206(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MT-VDAC1).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Amnion, Embryonic kidney, Embryonic stomach, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MT-VDAC1).
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 34-41; 46-66; 77-106; 110-123; 134-174; 177-210;
RP   214-231; 238-279 AND 288-296, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   FUNCTION.
RX   PubMed=15477379; DOI=10.1085/jgp.200409154;
RA   Okada S.F., O'Neal W.K., Huang P., Nicholas R.A., Ostrowski L.E.,
RA   Craigen W.J., Lazarowski E.R., Boucher R.C.;
RT   "Voltage-dependent anion channel-1 (VDAC-1) contributes to ATP release
RT   and cell volume regulation in murine cells.";
RL   J. Gen. Physiol. 124:513-526(2004).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33; LYS-41; LYS-74 AND
RP   LYS-237, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-80 AND TYR-208, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 14-296, FUNCTION, AND
RP   TOPOLOGY.
RX   PubMed=18988731; DOI=10.1073/pnas.0809634105;
RA   Ujwal R., Cascio D., Colletier J.-P., Faham S., Zhang J., Toro L.,
RA   Ping P., Abramson J.;
RT   "The crystal structure of mouse VDAC1 at 2.3 A resolution reveals
RT   mechanistic insights into metabolite gating.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:17742-17747(2008).
CC   -!- FUNCTION: Forms a channel through the mitochondrial outer membrane
CC       and also the plasma membrane. The channel at the outer
CC       mitochondrial membrane allows diffusion of small hydrophilic
CC       molecules; in the plasma membrane it is involved in cell volume
CC       regulation and apoptosis. It adopts an open conformation at low or
CC       zero membrane potential and a closed conformation at potentials
CC       above 30-40 mV. The open state has a weak anion selectivity
CC       whereas the closed state is cation-selective. May participate in
CC       the formation of the permeability transition pore complex (PTPC)
CC       responsible for the release of mitochondrial products that
CC       triggers apoptosis.
CC   -!- SUBUNIT: Interacts with hexokinases (By similarity). Interacts
CC       with BCL2L1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform Mt-VDAC1: Mitochondrion outer
CC       membrane; Multi-pass membrane protein.
CC   -!- SUBCELLULAR LOCATION: Isoform Pl-VDAC1: Cell membrane; Multi-pass
CC       membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Pl-VDAC1;
CC         IsoId=Q60932-1; Sequence=Displayed;
CC       Name=Mt-VDAC1;
CC         IsoId=Q60932-2; Sequence=VSP_005075;
CC         Note=Initiator Met-1 is removed. Contains a N-acetylalanine at
CC         position 2 (By similarity);
CC   -!- TISSUE SPECIFICITY: High levels of expression detected in heart,
CC       kidney, brain, and skeletal muscle. Not expressed in testis.
CC   -!- DOMAIN: Consists mainly of a membrane-spanning beta-barrel formed
CC       by 19 beta-strands. The helical N-terminus folds back into the
CC       pore opening and plays a role in voltage-gated channel activity
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the eukaryotic mitochondrial porin family.
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DR   EMBL; U30840; AAB47777.1; -; mRNA.
DR   EMBL; AK168672; BAE40522.1; -; mRNA.
DR   EMBL; AK169671; BAE41292.1; -; mRNA.
DR   EMBL; AK169354; BAE41103.1; -; mRNA.
DR   EMBL; AK169282; BAE41040.1; -; mRNA.
DR   EMBL; AK169160; BAE40939.1; -; mRNA.
DR   EMBL; AL645589; CAI24939.1; -; Genomic_DNA.
DR   EMBL; AL645589; CAM19812.1; -; Genomic_DNA.
DR   EMBL; BC092257; AAH92257.1; -; mRNA.
DR   IPI; IPI00122549; -.
DR   IPI; IPI00230540; -.
DR   RefSeq; NP_035824.1; NM_011694.4.
DR   UniGene; Mm.3555; -.
DR   UniGene; Mm.470023; -.
DR   PDB; 3EMN; X-ray; 2.30 A; X=14-296.
DR   PDBsum; 3EMN; -.
DR   ProteinModelPortal; Q60932; -.
DR   SMR; Q60932; 14-296.
DR   STRING; Q60932; -.
DR   PhosphoSite; Q60932; -.
DR   SWISS-2DPAGE; Q60932; -.
DR   REPRODUCTION-2DPAGE; Q60932; -.
DR   PRIDE; Q60932; -.
DR   Ensembl; ENSMUST00000020673; ENSMUSP00000020673; ENSMUSG00000020402.
DR   Ensembl; ENSMUST00000109065; ENSMUSP00000104693; ENSMUSG00000020402.
DR   GeneID; 22333; -.
DR   KEGG; mmu:22333; -.
DR   UCSC; uc007ivm.1; mouse.
DR   CTD; 22333; -.
DR   MGI; MGI:106919; Vdac1.
DR   GeneTree; ENSGT00390000011336; -.
DR   HOGENOM; HBG396026; -.
DR   HOVERGEN; HBG054036; -.
DR   InParanoid; Q60932; -.
DR   OMA; GYQMTFE; -.
DR   PhylomeDB; Q60932; -.
DR   ArrayExpress; Q60932; -.
DR   Bgee; Q60932; -.
DR   CleanEx; MM_VDAC1; -.
DR   Genevestigator; Q60932; -.
DR   GermOnline; ENSMUSG00000020402; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR   GO; GO:0008308; F:voltage-gated anion channel activity; IDA:UniProtKB.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR   GO; GO:0007612; P:learning; IMP:MGI.
DR   GO; GO:0007270; P:nerve-nerve synaptic transmission; IMP:MGI.
DR   InterPro; IPR001925; Porin_Euk.
DR   Pfam; PF01459; Porin_3; 1.
DR   PRINTS; PR00185; EUKARYTPORIN.
DR   PROSITE; PS00558; EUKARYOTIC_PORIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Apoptosis;
KW   Cell membrane; Direct protein sequencing; Ion transport; Membrane;
KW   Mitochondrion; Mitochondrion outer membrane; NAD; Nucleotide-binding;
KW   Phosphoprotein; Porin; Transmembrane; Transmembrane beta strand;
KW   Transport.
FT   CHAIN         1    296       Voltage-dependent anion-selective channel
FT                                protein 1.
FT                                /FTId=PRO_0000050500.
FT   TRANSMEM     39     46       Beta stranded.
FT   TRANSMEM     52     61       Beta stranded.
FT   TRANSMEM     67     77       Beta stranded.
FT   TRANSMEM     82     89       Beta stranded.
FT   TRANSMEM     93    101       Beta stranded.
FT   TRANSMEM    108    117       Beta stranded.
FT   TRANSMEM    123    132       Beta stranded.
FT   TRANSMEM    136    145       Beta stranded.
FT   TRANSMEM    149    158       Beta stranded.
FT   TRANSMEM    162    171       Beta stranded.
FT   TRANSMEM    178    188       Beta stranded.
FT   TRANSMEM    191    198       Beta stranded.
FT   TRANSMEM    202    211       Beta stranded.
FT   TRANSMEM    215    223       Beta stranded.
FT   TRANSMEM    230    239       Beta stranded.
FT   TRANSMEM    244    251       Beta stranded.
FT   TRANSMEM    255    264       Beta stranded.
FT   TRANSMEM    268    276       Beta stranded.
FT   TRANSMEM    286    296       Beta stranded.
FT   NP_BIND     255    257       NAD (By similarity).
FT   NP_BIND     273    277       NAD (By similarity).
FT   SITE         86     86       Involved in hexokinase binding (By
FT                                similarity).
FT   MOD_RES      14     14       N-acetylmethionine; in isoform Mt-VDAC1
FT                                (By similarity).
FT   MOD_RES      26     26       Phosphoserine (By similarity).
FT   MOD_RES      33     33       N6-acetyllysine.
FT   MOD_RES      41     41       N6-acetyllysine.
FT   MOD_RES      74     74       N6-acetyllysine.
FT   MOD_RES      80     80       Phosphotyrosine.
FT   MOD_RES     114    114       Phosphoserine (By similarity).
FT   MOD_RES     117    117       Phosphoserine.
FT   MOD_RES     120    120       Phosphothreonine (By similarity).
FT   MOD_RES     150    150       Phosphoserine (By similarity).
FT   MOD_RES     208    208       Phosphotyrosine.
FT   MOD_RES     237    237       N6-acetyllysine.
FT   MOD_RES     279    279       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1     13       Missing (in isoform Mt-VDAC1).
FT                                /FTId=VSP_005075.
FT   HELIX        20     22
FT   HELIX        26     32
FT   STRAND       43     45
FT   STRAND       53     56
FT   TURN         62     64
FT   STRAND       71     76
FT   STRAND       83     88
FT   STRAND       96    104
FT   STRAND      109    116
FT   STRAND      123    128
FT   STRAND      141    144
FT   STRAND      150    152
FT   STRAND      167    171
FT   TURN        172    175
FT   STRAND      176    184
FT   STRAND      189    198
FT   STRAND      206    210
FT   STRAND      212    224
FT   STRAND      235    238
FT   STRAND      241    249
FT   STRAND      261    264
FT   STRAND      269    271
FT   STRAND      293    295
SQ   SEQUENCE   296 AA;  32351 MW;  C0710C1717063B32 CRC64;
     MCSFFLVLLL WQNMAVPPTY ADLGKSARDV FTKGYGFGLI KLDLKTKSEN GLEFTSSGSA
     NTETTKVNGS LETKYRWTEY GLTFTEKWNT DNTLGTEITV EDQLARGLKL TFDSSFSPNT
     GKKNAKIKTG YKREHINLGC DVDFDIAGPS IRGALVLGYE GWLAGYQMNF ETSKSRVTQS
     NFAVGYKTDE FQLHTNVNDG TEFGGSIYQK VNKKLETAVN LAWTAGNSNT RFGIAAKYQV
     DPDACFSAKV NNSSLIGLGY TQTLKPGIKL TLSALLDGKN VNAGGHKLGL GLEFQA
//
ID   TBCD1_MOUSE             Reviewed;        1255 AA.
AC   Q60949; Q80TJ9; Q923F8;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2003, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=TBC1 domain family member 1;
GN   Name=Tbc1d1; Synonyms=Kiaa1108, Tbc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RX   MEDLINE=96032578; PubMed=7566974;
RA   Richardson P.M., Zon L.I.;
RT   "Molecular cloning of a cDNA with a novel domain present in the tre-2
RT   oncogene and the yeast cell cycle regulators BUB2 and cdc16.";
RL   Oncogene 11:1139-1148(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 762-1255.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May act as a GTPase-activating protein for Rab family
CC       protein(s). May play a role in the cell cycle and differentiation
CC       of various tissues.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q60949-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q60949-2; Sequence=VSP_008473;
CC   -!- TISSUE SPECIFICITY: Expressed in highest levels in hematopoietic
CC       cells, testis and kidney.
CC   -!- SIMILARITY: Contains 1 PID domain.
CC   -!- SIMILARITY: Contains 1 Rab-GAP TBC domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA85223.1; Type=Frameshift; Positions=15, 30, 795, 822, 1224;
CC       Sequence=BAC65727.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U33005; AAA85223.1; ALT_FRAME; mRNA.
DR   EMBL; AK122445; BAC65727.1; ALT_INIT; mRNA.
DR   EMBL; BC004675; AAH04675.1; -; mRNA.
DR   IPI; IPI00379682; -.
DR   IPI; IPI00379683; -.
DR   PIR; T29104; T29104.
DR   UniGene; Mm.286353; -.
DR   ProteinModelPortal; Q60949; -.
DR   SMR; Q60949; 282-370, 860-1152.
DR   STRING; Q60949; -.
DR   PhosphoSite; Q60949; -.
DR   PRIDE; Q60949; -.
DR   Ensembl; ENSMUST00000043893; ENSMUSP00000044577; ENSMUSG00000029174.
DR   Ensembl; ENSMUST00000101195; ENSMUSP00000098756; ENSMUSG00000029174.
DR   UCSC; uc008xmj.1; mouse.
DR   UCSC; uc008xmm.1; mouse.
DR   MGI; MGI:1889508; Tbc1d1.
DR   GeneTree; ENSGT00550000074196; -.
DR   HOGENOM; HBG714321; -.
DR   HOVERGEN; HBG059376; -.
DR   InParanoid; Q60949; -.
DR   OrthoDB; EOG4NS39Q; -.
DR   PhylomeDB; Q60949; -.
DR   ArrayExpress; Q60949; -.
DR   Bgee; Q60949; -.
DR   CleanEx; MM_TBC1D1; -.
DR   Genevestigator; Q60949; -.
DR   GermOnline; ENSMUSG00000029174; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005097; F:Rab GTPase activator activity; IEA:InterPro.
DR   GO; GO:0032313; P:regulation of Rab GTPase activity; IEA:InterPro.
DR   InterPro; IPR021785; DUF3350.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   InterPro; IPR000195; RabGAP/TBC_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 3.
DR   Pfam; PF11830; DUF3350; 1.
DR   Pfam; PF00640; PID; 1.
DR   Pfam; PF00566; TBC; 1.
DR   SMART; SM00462; PTB; 2.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; RabGAP_TBC; 2.
DR   PROSITE; PS01179; PID; 1.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; GTPase activation; Nucleus; Phosphoprotein.
FT   CHAIN         1   1255       TBC1 domain family member 1.
FT                                /FTId=PRO_0000208023.
FT   DOMAIN      238    398       PID.
FT   DOMAIN      887   1081       Rab-GAP TBC.
FT   MOD_RES     113    113       Phosphotyrosine (By similarity).
FT   MOD_RES     501    501       Phosphoserine (By similarity).
FT   MOD_RES     559    559       Phosphoserine (By similarity).
FT   MOD_RES     564    564       Phosphoserine (By similarity).
FT   MOD_RES     579    579       Phosphoserine (By similarity).
FT   MOD_RES     621    621       Phosphoserine (By similarity).
FT   VAR_SEQ     631    724       NVDHLPGGESQGCPGQPSAPPPPRLNPSASSPNFFKYLKHN
FT                                SSGEQSGNAVPKSVSYRNALRKKLHSSSSVPNFLKFLAPVD
FT                                ENNTCDFKNTNR -> K (in isoform 2).
FT                                /FTId=VSP_008473.
FT   CONFLICT    174    174       K -> E (in Ref. 1).
FT   CONFLICT    289    289       Q -> P (in Ref. 1).
FT   CONFLICT    462    462       E -> A (in Ref. 1).
FT   CONFLICT    848    848       E -> D (in Ref. 3; AAH04675).
FT   CONFLICT   1047   1047       I -> T (in Ref. 1).
FT   CONFLICT   1050   1051       SL -> PT (in Ref. 1).
FT   CONFLICT   1143   1143       A -> P (in Ref. 3; AAH04675).
FT   CONFLICT   1151   1151       L -> V (in Ref. 1).
FT   CONFLICT   1176   1176       S -> T (in Ref. 1).
FT   CONFLICT   1215   1215       A -> R (in Ref. 1).
SQ   SEQUENCE   1255 AA;  142025 MW;  206BE7714AB07DBC CRC64;
     MEAITFTARK HPFPNEVSVD FGLQLVGSLP VHSLTTMPML PWVVAEVRRL SGQCSKKEPR
     TKQVRLWVSP SGLRCEPDLE KSQPWDPLIC SSIFECKPQR VHKLIHNSHD PSYFACLIKE
     DAAHRQSLCY VFKADDQTKV PEIISSIRQA GKIARQEELR CPSEFDDTFA KKFKVLFCGR
     VTVAHKKAPP ALIDECIEKF NHVSCGRRTD WEAPTGQPSA PGPRPMRKSF SQPGLRSLAF
     RKEFQDASLR SSTFSSFDND IENHLIGGHN VVQPTDMEEN RTMLFTIGQS EVYLISPDTK
     KIALEKNFKE ISFCSQGIRH VDHFGFICRE CSGGGSGGFH FVCYVFQCTN EALVDEIMMT
     LKQAFTVAAV QQTAKAPAQL CEGCPLQGLH KLCERIEGMN SSKTKLELQK HLTTLTNQEQ
     ATIFEEVQKL RPRNEQRENE LIISFLRCLY EEKQKEHSHT GEPKQTLQVA AENIGSDLPP
     SASRFRLDSL KNRAKRSLTE SLESILSRGN KARGLQDHSA SVDLDSSTSS TLSNTSKELS
     MGDKEAFPVS ETSFKLLGSS DDLSSDSEGH IAEESALLSP QQAFRRRANT LSHFPVECPA
     PPEPAQSSPG VSQRKLMRYH SVSTETPHER NVDHLPGGES QGCPGQPSAP PPPRLNPSAS
     SPNFFKYLKH NSSGEQSGNA VPKSVSYRNA LRKKLHSSSS VPNFLKFLAP VDENNTCDFK
     NTNRDFESKA NHLGDTDGTP VKTRRHSWRQ QIFLRVATPQ KACDSPSRYE DYSELGELPP
     RSPLEPVCED GPFGPVQEEK RKTSRELREL WKKAILQQIL LLRMEKENQK LQASENDLLN
     KRLKLDYEEI TPCLKEVTTV WEKMLSTPGR SKIKFDMEKV HSAVGQGVPR HHRGEIWKFL
     AEQFHLKHPF PSKQQPKDVP YKELLKKLTS QQHAILIDLG RTFPTHPYFS AQLGAGQLSL
     YNILKAYSLL DQEVGYCQGL SFVAGILLLH MSEEEAFKML KFLMFDMGLR KQYRPDMIIL
     QIQMYQLSRL LHDYHRDLYN HLEEHEIGPS LYAAPWFLTV FASQFPLGFV ARVFDMIFLQ
     GSEVIFKVAL SLLGSHKPLI LQHENLETIV DFIKNTLPNL GLVQMEKTIS QVFEMDIAKQ
     LQAYEVEYHV LQEELIESSP LSDNQRMEKL EKTNSSLRKQ NLDLLEQLQV ANARIQSLEA
     TVEKLLTSES KLKQAALTLE VERSALLQMV EELRRQSARP STPEPDCTQL EPTGD
//
ID   RBBP7_MOUSE             Reviewed;         425 AA.
AC   Q60973; A2AFJ0; Q3UX20;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   08-MAR-2011, entry version 109.
DE   RecName: Full=Histone-binding protein RBBP7;
DE   AltName: Full=Histone acetyltransferase type B subunit 2;
DE   AltName: Full=Nucleosome-remodeling factor subunit RBAP46;
DE   AltName: Full=Retinoblastoma-binding protein 7;
DE            Short=RBBP-7;
DE   AltName: Full=Retinoblastoma-binding protein p46;
GN   Name=Rbbp7; Synonyms=Rbap46;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 7-32 AND 133-155, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Embryo;
RX   MEDLINE=96029633; PubMed=7503932; DOI=10.1074/jbc.270.43.25507;
RA   Qian Y.-W., Lee E.Y.-H.P.;
RT   "Dual retinoblastoma-binding proteins with properties related to a
RT   negative regulator of ras in yeast.";
RL   J. Biol. Chem. 270:25507-25513(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Egg, Heart, Kidney, Liver, Placenta, Sympathetic ganglion, and
RC   Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH SUV39H1.
RX   MEDLINE=21648906; PubMed=11788710; DOI=10.1093/nar/30.2.475;
RA   Vaute O., Nicolas E., Vandel L., Trouche D.;
RT   "Functional and physical interaction between the histone methyl
RT   transferase Suv39H1 and histone deacetylases.";
RL   Nucleic Acids Res. 30:475-481(2002).
RN   [6]
RP   INTERACTION WITH HDAC7.
RX   MEDLINE=20442375; PubMed=10984530; DOI=10.1073/pnas.97.19.10330;
RA   Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M.;
RT   "Identification of a nuclear domain with deacetylase activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Core histone-binding subunit that may target chromatin
CC       remodeling factors, histone acetyltransferases and histone
CC       deacetylases to their histone substrates in a manner that is
CC       regulated by nucleosomal DNA. Component of several complexes which
CC       regulate chromatin metabolism. These include the type B histone
CC       acetyltransferase (HAT) complex, which is required for chromatin
CC       assembly following DNA replication; the core histone deacetylase
CC       (HDAC) complex, which promotes histone deacetylation and
CC       consequent transcriptional repression; the nucleosome remodeling
CC       and histone deacetylase complex (the NuRD complex), which promotes
CC       transcriptional repression by histone deacetylation and nucleosome
CC       remodeling; and the PRC2/EED-EZH2 complex, which promotes
CC       repression of homeotic genes during development; and the NURF
CC       (nucleosome remodeling factor) complex (By similarity).
CC   -!- SUBUNIT: Binds directly to helix 1 of the histone fold of histone
CC       H4, a region that is not accessible when H4 is in chromatin.
CC       Subunit of the type B histone acetyltransferase (HAT) complex,
CC       composed of RBBP7 and HAT1. Subunit of the core histone
CC       deacetylase (HDAC) complex, which is composed of HDAC1, HDAC2,
CC       RBBP4 and RBBP7. The core HDAC complex associates with SIN3A,
CC       ARID4B/SAP180, SAP18, SAP30, SAP130, SDS3/SAP45 and possibly
CC       ARID4A/RBP1 and ING1 to form the SIN3 HDAC complex. The core HDAC
CC       complex may also associate with MTA2, MBD3, CHD3 and CHD4 to form
CC       the nucleosome remodeling and histone deacetylase complex (the
CC       NuRD complex). The NuRD complex may also interact with MBD3L1 and
CC       MBD3L2. Interacts with MTA1. Subunit of the PRC2/EED-EZH2 complex,
CC       which is composed of at least EED, EZH2, RBBP4, RBBP7 and SUZ12.
CC       The PRC2/EED-EZH2 complex may also associate with HDAC1. Part of
CC       the nucleosome remodeling factor (NURF) complex which consists of
CC       SMARCA1; BPTF; RBBP4 and RBBP7. Interacts with the viral protein-
CC       binding domain of the retinoblastoma protein (RB1). Interacts with
CC       CREBBP, and this interaction may be enhanced by the binding of
CC       phosphorylated CREB1 to CREBBP. Interacts with BRCA1, HDAC7 and
CC       SUV39H1.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Higher levels in brain, thymus, lung, spleen,
CC       kidney, testis, and ovary/uterus; lower levels in heart, liver,
CC       and muscle.
CC   -!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
CC   -!- SIMILARITY: Contains 7 WD repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U35142; AAC52276.1; -; mRNA.
DR   EMBL; AK076016; BAC36122.1; -; mRNA.
DR   EMBL; AK135779; BAE22658.1; -; mRNA.
DR   EMBL; AK135956; BAE22743.1; -; mRNA.
DR   EMBL; AK136110; BAE22826.1; -; mRNA.
DR   EMBL; AK145531; BAE26487.1; -; mRNA.
DR   EMBL; AK145651; BAE26567.1; -; mRNA.
DR   EMBL; AK146014; BAE26833.1; -; mRNA.
DR   EMBL; AK146904; BAE27517.1; -; mRNA.
DR   EMBL; AK146967; BAE27573.1; -; mRNA.
DR   EMBL; AK147062; BAE27646.1; -; mRNA.
DR   EMBL; AK148852; BAE28678.1; -; mRNA.
DR   EMBL; AK153913; BAE32251.1; -; mRNA.
DR   EMBL; AK160023; BAE35566.1; -; mRNA.
DR   EMBL; AL672123; CAM24314.1; -; Genomic_DNA.
DR   EMBL; BC003785; AAH03785.1; -; mRNA.
DR   IPI; IPI00122698; -.
DR   PIR; I49367; I49367.
DR   RefSeq; NP_033057.3; NM_009031.3.
DR   UniGene; Mm.249161; -.
DR   UniGene; Mm.270186; -.
DR   UniGene; Mm.371732; -.
DR   ProteinModelPortal; Q60973; -.
DR   SMR; Q60973; 1-410.
DR   STRING; Q60973; -.
DR   PhosphoSite; Q60973; -.
DR   REPRODUCTION-2DPAGE; Q60973; -.
DR   PRIDE; Q60973; -.
DR   Ensembl; ENSMUST00000033720; ENSMUSP00000033720; ENSMUSG00000031353.
DR   GeneID; 245688; -.
DR   KEGG; mmu:245688; -.
DR   UCSC; uc009uuf.1; mouse.
DR   CTD; 245688; -.
DR   MGI; MGI:1194910; Rbbp7.
DR   HOGENOM; HBG435352; -.
DR   HOVERGEN; HBG053236; -.
DR   InParanoid; Q60973; -.
DR   OMA; NDEEPDI; -.
DR   OrthoDB; EOG4DBTDH; -.
DR   PhylomeDB; Q60973; -.
DR   NextBio; 386918; -.
DR   ArrayExpress; Q60973; -.
DR   Bgee; Q60973; -.
DR   CleanEx; MM_RBBP7; -.
DR   Genevestigator; Q60973; -.
DR   GermOnline; ENSMUSG00000031353; Mus musculus.
DR   GO; GO:0035098; C:ESC/E(Z) complex; ISS:UniProtKB.
DR   GO; GO:0016581; C:NuRD complex; ISS:UniProtKB.
DR   GO; GO:0016564; F:transcription repressor activity; IDA:MGI.
DR   GO; GO:0070370; P:cellular heat acclimation; ISS:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; TAS:MGI.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR022052; Histone-bd_RBBP4.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF12265; CAF1C_H4-bd; 1.
DR   Pfam; PF00400; WD40; 5.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 3.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chaperone; Chromatin regulator;
KW   Direct protein sequencing; DNA replication; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Repeat; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation; WD repeat.
FT   CHAIN         1    425       Histone-binding protein RBBP7.
FT                                /FTId=PRO_0000051196.
FT   REPEAT       47    122       WD 1.
FT   REPEAT      128    173       WD 2.
FT   REPEAT      181    217       WD 3.
FT   REPEAT      228    269       WD 4.
FT   REPEAT      275    312       WD 5.
FT   REPEAT      318    369       WD 6.
FT   REPEAT      376    403       WD 7.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       3      3       Phosphoserine (By similarity).
FT   MOD_RES       4      4       N6-acetyllysine (By similarity).
FT   MOD_RES      21     21       N6-acetyllysine (By similarity).
FT   MOD_RES      99     99       Phosphoserine.
FT   MOD_RES     119    119       N6-acetyllysine (By similarity).
FT   MOD_RES     354    354       Phosphoserine (By similarity).
FT   MOD_RES     413    413       Phosphoserine (By similarity).
FT   MOD_RES     416    416       Phosphothreonine (By similarity).
FT   CROSSLNK      4      4       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
SQ   SEQUENCE   425 AA;  47790 MW;  0A4A4CD1A8E96815 CRC64;
     MASKEMFEDT VEERVINEEY KIWKKNTPFL YDLVMTHALQ WPSLTVQWLP EVTKPEGKDY
     ALHWLVLGTH TSDEQNHLVV ARVHIPNDDA QFDASHCDSD KGEFGGFGSV TGKIECEIKI
     NHEGEVNRAR YMPQNPHIIA TKTPSSDVLV FDYTKHPAKP DPSGECNPDL RLRGHQKEGY
     GLSWNSNLSG HLLSASDDHT VCLWDINAGP KEGKIVDAKA IFTGHSAVVE DVAWHLLHES
     LFGSVADDQK LMIWDTRSNT TSKPSHLVDA HTAEVNCLSF NPYSEFILAT GSADKTVALW
     DLRNLKLKLH TFESHKDEIF QVHWSPHNET ILASSGTDRR LNVWDLSKIG EEQSAEDAED
     GPPELLFIHG GHTAKISDFS WNPNEPWVIC SVSEDNIMQI WQMAENIYND EESDVTASEL
     EGQGS
//
ID   KLF3_MOUSE              Reviewed;         344 AA.
AC   Q60980;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Krueppel-like factor 3;
DE   AltName: Full=Basic krueppel-like factor;
DE   AltName: Full=CACCC-box-binding protein BKLF;
DE   AltName: Full=TEF-2;
GN   Name=Klf3; Synonyms=Bklf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=DBA; TISSUE=Leukemia;
RX   MEDLINE=96239526; PubMed=8657145;
RA   Crossley M., Whitelaw E., Perkins A., Williams G., Fujiwara Y.,
RA   Orkin S.H.;
RT   "Isolation and characterization of the cDNA encoding BKLF/TEF-2, a
RT   major CACCC-box-binding protein in erythroid cells and selected other
RT   cells.";
RL   Mol. Cell. Biol. 16:1695-1705(1996).
RN   [2]
RP   SUMOYLATION AT LYS-10 AND LYS-197, FUNCTION, AND MUTAGENESIS OF
RP   LYS-10; GLU-12; LYS-197 AND GLU-199.
RX   PubMed=15684403; DOI=10.1128/MCB.25.4.1549-1559.2005;
RA   Perdomo J., Verger A., Turner J., Crossley M.;
RT   "Role for SUMO modification in facilitating transcriptional repression
RT   by BKLF.";
RL   Mol. Cell. Biol. 25:1549-1559(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71 AND SER-91, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   STRUCTURE BY NMR OF 314-344 OF WILD TYPE AND MUTANT FORMS, SUBUNIT,
RP   DNA-BINDING, AND MUTAGENESIS OF HIS-341.
RX   PubMed=12736264; DOI=10.1074/jbc.M211146200;
RA   Simpson R.J.Y., Cram E.D., Czolij R., Matthews J.M., Crossley M.,
RA   Mackay J.P.;
RT   "CCHX zinc finger derivatives retain the ability to bind Zn(II) and
RT   mediate protein-DNA interactions.";
RL   J. Biol. Chem. 278:28011-28018(2003).
CC   -!- FUNCTION: Binds to the CACCC box of erythroid cell-expressed
CC       genes. May play a role in hematopoiesis.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- TISSUE SPECIFICITY: In 8.5 day embryos, expressed in midbrain,
CC       anterior hindbrain and ventral forebrain. In 9 day embryos,
CC       expressed throughout ventral anterior half of embryo including
CC       midbrain-hindbrain junction, ventral midbrain, diencephalon and
CC       forebrain. At 10.5 days, distribution is more widespread with
CC       expression also found in developing limb buds. Widely expressed in
CC       the adult.
CC   -!- PTM: Sumoylated by SUMO1. Sumoylation is enhanced by PIAS1,
CC       PIAS2alpha and PIAS2beta, and PIAS4, but not by Pc2. Enhances
CC       transcriptional repression, but has no effect on DNA binding.
CC       Sumoylation on Lys-197 is the major site.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family.
CC   -!- SIMILARITY: Contains 3 C2H2-type zinc fingers.
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DR   EMBL; U36340; AAA93256.1; -; mRNA.
DR   IPI; IPI00122757; -.
DR   PIR; JC6100; JC6100.
DR   RefSeq; NP_032479.1; NM_008453.5.
DR   UniGene; Mm.392759; -.
DR   UniGene; Mm.439720; -.
DR   PDB; 1P7A; NMR; -; A=314-344.
DR   PDB; 1U85; NMR; -; A=314-344.
DR   PDB; 1U86; NMR; -; A=322-344.
DR   PDBsum; 1P7A; -.
DR   PDBsum; 1U85; -.
DR   PDBsum; 1U86; -.
DR   ProteinModelPortal; Q60980; -.
DR   SMR; Q60980; 214-344.
DR   STRING; Q60980; -.
DR   PhosphoSite; Q60980; -.
DR   PRIDE; Q60980; -.
DR   Ensembl; ENSMUST00000031074; ENSMUSP00000031074; ENSMUSG00000029178.
DR   GeneID; 16599; -.
DR   KEGG; mmu:16599; -.
DR   UCSC; uc008xms.1; mouse.
DR   CTD; 16599; -.
DR   MGI; MGI:1342773; Klf3.
DR   HOGENOM; HBG402881; -.
DR   HOVERGEN; HBG003941; -.
DR   InParanoid; Q60980; -.
DR   OMA; NSSMQVP; -.
DR   OrthoDB; EOG4JHCG4; -.
DR   PhylomeDB; Q60980; -.
DR   NextBio; 460295; -.
DR   ArrayExpress; Q60980; -.
DR   Bgee; Q60980; -.
DR   CleanEx; MM_KLF3; -.
DR   Genevestigator; Q60980; -.
DR   GermOnline; ENSMUSG00000029178; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 3.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; DNA-binding; Isopeptide bond;
KW   Metal-binding; Nucleus; Phosphoprotein; Repeat; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    344       Krueppel-like factor 3.
FT                                /FTId=PRO_0000047166.
FT   ZN_FING     259    283       C2H2-type 1.
FT   ZN_FING     289    313       C2H2-type 2.
FT   ZN_FING     319    341       C2H2-type 3.
FT   REGION        1     74       Repressor domain.
FT   MOTIF        61     65       CTBP-binding motif.
FT   COMPBIAS      1    250       Pro-rich.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      71     71       Phosphoserine.
FT   MOD_RES      91     91       Phosphoserine.
FT   MOD_RES     100    100       Phosphoserine (By similarity).
FT   MOD_RES     249    249       Phosphoserine (By similarity).
FT   CROSSLNK     10     10       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT   CROSSLNK    197    197       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT   MUTAGEN      10     10       K->A: Reduced sumoylation levels. No
FT                                effect on DNA-binding and slight
FT                                reduction of transcriptional repression.
FT                                Abolishes sumoylation. No effect on DNA-
FT                                binding but great reduction in
FT                                transcriptional repression; when
FT                                associated with A-197.
FT   MUTAGEN      12     12       E->A: Slight reduction of transcriptional
FT                                repression. Great reduction of
FT                                transcriptional repression; when
FT                                associated with A-199.
FT   MUTAGEN     197    197       K->A: Reduced sumoylation levels. No
FT                                effect on DNA-binding and slight
FT                                reduction of transcriptional repression.
FT                                Abolishes sumoylation. No effect on DNA-
FT                                binding but great reduction of
FT                                transcriptional repression; when
FT                                associated with A-10.
FT   MUTAGEN     199    199       E->A: Slight reduction of transcriptional
FT                                repression. Great reduction of
FT                                transcriptional repression; when
FT                                associated with A-199.
FT   MUTAGEN     341    341       H->A,D,E,N,Q,R: Little change in DNA-
FT                                binding ability.
FT   STRAND      316    319
FT   TURN        322    324
FT   STRAND      328    330
FT   HELIX       331    338
FT   HELIX       339    341
SQ   SEQUENCE   344 AA;  38561 MW;  2BB7E3B63A7C1D88 CRC64;
     MLMFDPVPVK QEAMDPVSVS FPSNYIESMK PNKYGVIYST PLPDKFFQTP EGLTHGIQVE
     PVDLTVNKRG SPPAAGGSPS SLKFPSHRRA SPGLSMPSSS PPIKKYSPPS PGVQPFGVPL
     SMPPVMAAAL SRHGIRSPGI LPVIQPVVVQ PVPFMYTSHL QQPLMVSLSE EMDNSNSGMP
     VPVIESYEKP LLQKKIKIEP GIEPQRTDYY PEEMSPPLMN PVSPPQALLQ ENHPSVIVQP
     GKRPLPVESP DTQRKRRIHR CDYDGCNKVY TKSSHLKAHR RTHTGEKPYK CTWEGCTWKF
     ARSDELTRHF RKHTGIKPFQ CPDCDRSFSR SDHLALHRKR HMLV
//
ID   GBG7_MOUSE              Reviewed;          68 AA.
AC   Q61016; Q8JZP6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-7;
DE   Flags: Precursor;
GN   Name=Gng7; Synonyms=Gngt7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RA   Xiong X., Han J.;
RT   "Mouse G-protein gamma 7 cDNA.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-51.
RC   STRAIN=CF-1 / Harlan;
RX   MEDLINE=97011591; PubMed=8858601;
RX   DOI=10.1002/(SICI)1098-2795(199607)44:3<315::AID-MRD5>3.3.CO;2-V;
RA   Williams C.J., Schultz R.M., Kopf G.S.;
RT   "G protein gene expression during mouse oocyte growth and maturation,
RT   and preimplantation embryo development.";
RL   Mol. Reprod. Dev. 44:315-323(1996).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=12488442; DOI=10.1074/jbc.M211132200;
RA   Schwindinger W.F., Betz K.S., Giger K.E., Sabol A., Bronson S.K.,
RA   Robishaw J.D.;
RT   "Loss of G protein gamma 7 alters behavior and reduces striatal
RT   alpha(olf) level and cAMP production.";
RL   J. Biol. Chem. 278:6575-6579(2003).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC       involved as a modulator or transducer in various transmembrane
CC       signaling systems. The beta and gamma chains are required for the
CC       GTPase activity, for replacement of GDP by GTP, and for G protein-
CC       effector interaction. Plays a role in the regulation of adenylyl
CC       cyclase signaling in certain regions of the brain. Plays a role in
CC       the formation or stabilzation of a G protein heterotrimer (G(olf)
CC       subunit alpha-beta-gamma-7) that is required for adenylyl cyclase
CC       activity in the striatum.
CC   -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and
CC       gamma.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- TISSUE SPECIFICITY: Brain. Found in the hippocampus, striatum,
CC       midbrain and cortex.
CC   -!- DISRUPTION PHENOTYPE: Mice display increased startle response but
CC       normal prepulse inhibition of the startle response. No effect on
CC       survival to weaning, fertility and mortality.
CC   -!- SIMILARITY: Belongs to the G protein gamma family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY035844; AAK61365.1; -; mRNA.
DR   EMBL; BC034108; AAH34108.1; -; mRNA.
DR   EMBL; U38499; AAB01730.1; -; mRNA.
DR   IPI; IPI00230566; -.
DR   RefSeq; NP_001033744.1; NM_001038655.1.
DR   RefSeq; NP_034449.2; NM_010319.3.
DR   UniGene; Mm.222496; -.
DR   ProteinModelPortal; Q61016; -.
DR   SMR; Q61016; 9-58.
DR   PRIDE; Q61016; -.
DR   Ensembl; ENSMUST00000092285; ENSMUSP00000089936; ENSMUSG00000048240.
DR   Ensembl; ENSMUST00000099462; ENSMUSP00000097061; ENSMUSG00000048240.
DR   Ensembl; ENSMUST00000117805; ENSMUSP00000112409; ENSMUSG00000048240.
DR   Ensembl; ENSMUST00000118233; ENSMUSP00000114003; ENSMUSG00000048240.
DR   Ensembl; ENSMUST00000118465; ENSMUSP00000113798; ENSMUSG00000048240.
DR   GeneID; 14708; -.
DR   KEGG; mmu:14708; -.
DR   CTD; 14708; -.
DR   MGI; MGI:95787; Gng7.
DR   GeneTree; ENSGT00550000074352; -.
DR   HOGENOM; HBG444905; -.
DR   HOVERGEN; HBG014983; -.
DR   InParanoid; Q61016; -.
DR   OMA; NNVAQAR; -.
DR   OrthoDB; EOG4ZGPF1; -.
DR   PhylomeDB; Q61016; -.
DR   NextBio; 286695; -.
DR   ArrayExpress; Q61016; -.
DR   Bgee; Q61016; -.
DR   Genevestigator; Q61016; -.
DR   GermOnline; ENSMUSG00000048240; Mus musculus.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro.
DR   GO; GO:0004871; F:signal transducer activity; IMP:MGI.
DR   GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; IEA:InterPro.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IMP:MGI.
DR   GO; GO:0045761; P:regulation of adenylate cyclase activity; IMP:UniProtKB.
DR   InterPro; IPR015898; G-protein_gamma_dom.
DR   InterPro; IPR001770; Gprotein-gamma.
DR   Gene3D; G3DSA:4.10.260.10; G-protein_gamma_dom; 1.
DR   PANTHER; PTHR13809; Gprotein-gamma; 1.
DR   Pfam; PF00631; G-gamma; 1.
DR   PRINTS; PR00321; GPROTEING.
DR   SMART; SM00224; GGL; 1.
DR   SUPFAM; SSF48670; G-protein_gamma-like; 1.
DR   PROSITE; PS50058; G_PROTEIN_GAMMA; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell membrane; Lipoprotein; Membrane; Methylation;
KW   Prenylation; Transducer.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2     65       Guanine nucleotide-binding protein
FT                                G(I)/G(S)/G(O) subunit gamma-7.
FT                                /FTId=PRO_0000012637.
FT   PROPEP       66     68       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000012638.
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES      65     65       Cysteine methyl ester (By similarity).
FT   LIPID        65     65       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   68 AA;  7480 MW;  0F07C667A29ADC07 CRC64;
     MSGTNNVAQA RKLVEQLRIE AGIERIKVSK ASSDLMGYCE QHARNDPLLV GVPASENPFK
     DKKPCIIL
//
ID   ASNS_MOUSE              Reviewed;         561 AA.
AC   Q61024; Q3TJA1; Q8BPC8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Asparagine synthetase [glutamine-hydrolyzing];
DE            EC=6.3.5.4;
DE   AltName: Full=Glutamine-dependent asparagine synthetase;
GN   Name=Asns;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Liver;
RA   Goodwin L., Sellati L., Millan C., Guzowski D., Leeds N., Broome J.,
RA   Pergolizzi R.;
RL   Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartate + L-glutamine + H(2)O = AMP
CC       + diphosphate + L-asparagine + L-glutamate.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-asparagine biosynthesis; L-
CC       asparagine from L-aspartate (L-Gln route): step 1/1.
CC   -!- SIMILARITY: Contains 1 asparagine synthetase domain.
CC   -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain.
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DR   EMBL; U38940; AAA85125.1; -; mRNA.
DR   EMBL; AK076207; BAC36254.1; -; mRNA.
DR   EMBL; AK167524; BAE39594.1; -; mRNA.
DR   EMBL; BC005552; AAH05552.1; -; mRNA.
DR   IPI; IPI00116966; -.
DR   RefSeq; NP_036185.1; NM_012055.3.
DR   UniGene; Mm.2942; -.
DR   ProteinModelPortal; Q61024; -.
DR   SMR; Q61024; 2-532.
DR   STRING; Q61024; -.
DR   MEROPS; C44.974; -.
DR   PhosphoSite; Q61024; -.
DR   PRIDE; Q61024; -.
DR   Ensembl; ENSMUST00000031766; ENSMUSP00000031766; ENSMUSG00000029752.
DR   Ensembl; ENSMUST00000115542; ENSMUSP00000111204; ENSMUSG00000029752.
DR   GeneID; 27053; -.
DR   KEGG; mmu:27053; -.
DR   NMPDR; fig|10090.3.peg.12931; -.
DR   UCSC; uc009axf.1; mouse.
DR   CTD; 27053; -.
DR   MGI; MGI:1350929; Asns.
DR   GeneTree; ENSGT00390000001994; -.
DR   HOGENOM; HBG752912; -.
DR   HOVERGEN; HBG003103; -.
DR   InParanoid; Q61024; -.
DR   OMA; KVTDQQM; -.
DR   OrthoDB; EOG4RV2R2; -.
DR   PhylomeDB; Q61024; -.
DR   BRENDA; 6.3.5.4; 244.
DR   NextBio; 304991; -.
DR   ArrayExpress; Q61024; -.
DR   Bgee; Q61024; -.
DR   CleanEx; MM_ASNS; -.
DR   Genevestigator; Q61024; -.
DR   GermOnline; ENSMUSG00000029752; Mus musculus.
DR   GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006529; P:asparagine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006426; Asn_synth_AEB.
DR   InterPro; IPR001962; Asn_synthase.
DR   InterPro; IPR000583; GATase_2.
DR   InterPro; IPR017932; GATase_II.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Pfam; PF00733; Asn_synthase; 1.
DR   Pfam; PF00310; GATase_2; 1.
DR   TIGRFAMs; TIGR01536; asn_synth_AEB; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Amino-acid biosynthesis; Asparagine biosynthesis;
KW   ATP-binding; Glutamine amidotransferase; Ligase; Nucleotide-binding;
KW   Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    561       Asparagine synthetase [glutamine-
FT                                hydrolyzing].
FT                                /FTId=PRO_0000056912.
FT   DOMAIN        2    191       Glutamine amidotransferase type-2.
FT   DOMAIN      213    536       Asparagine synthetase.
FT   ACT_SITE      2      2       For GATase activity (By similarity).
FT   MOD_RES     385    385       N6-acetyllysine (By similarity).
FT   MOD_RES     471    471       Phosphoserine (By similarity).
FT   CONFLICT      5      5       W -> G (in Ref. 2; BAC36254).
SQ   SEQUENCE   561 AA;  64283 MW;  1981956B69E1F9F1 CRC64;
     MCGIWALFGS DDCLSVQCLS AMKIAHRGPD AFRFENVNGY TNCCFGFHRL AVVDPLFGMQ
     PIRVRKYPYL WLCYNGEIYN HKALQQRFEF EYQTNVDGEI ILHLYDKGGI EKTICMLDGV
     FAFILLDTAN KKVFLGRDTY GVRPLFKAMT EDGFLAVCSE AKGLVSLKHS TTPFLKVEPF
     LPGHYEVLDL KPNGKVASVE MVKYHHCTDE PLHAIYDSVE KLFPGFDLET VKNNLRILFD
     NAIKKRLMTD RRIGCLLSGG LDSSLVAASL LKQLKEAQVQ YPLQTFAIGM EDSPDLLAAR
     KVANYIGSEH HEVLFNSEEG IQALDEVIFS LETYDITTVR ASVGMYLISK YIRKNTDSVV
     IFSGEGSDEL TQGYIYFHKA PSPEKAEEES ERLLKELYLF DVLRADRTTA AHGLELRVPF
     LDHRFSSYYL SLPPDMRIPK NGIEKHLLRE TFEDCNLLPK EILWRPKEAF SDGITSVKNS
     WFKILQDYVE HQVDDEMMSA ASQKFPFNTP KTKEGYFYRQ IFERHYPGRA DWLTHYWMPK
     WINATDPSAR TLTHYKSAAK A
//
ID   SYHC_MOUSE              Reviewed;         509 AA.
AC   Q61035;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Histidyl-tRNA synthetase, cytoplasmic;
DE            EC=6.1.1.21;
DE   AltName: Full=Histidine--tRNA ligase;
DE            Short=HisRS;
GN   Name=Hars;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=97080562; PubMed=8921907; DOI=10.1016/0378-1119(96)00358-7;
RA   Blechynden L.M., Lawson C.M., Garlepp M.J.;
RT   "Sequence and polymorphism analysis of the murine gene encoding
RT   histidyl-tRNA synthetase.";
RL   Gene 178:151-156(1996).
CC   -!- CATALYTIC ACTIVITY: ATP + L-histidine + tRNA(His) = AMP +
CC       diphosphate + L-histidyl-tRNA(His).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
CC   -!- SIMILARITY: Contains 1 WHEP-TRS domain.
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DR   EMBL; U39473; AAC52914.1; -; mRNA.
DR   IPI; IPI00116991; -.
DR   PIR; JC5223; JC5223.
DR   UniGene; Mm.10528; -.
DR   ProteinModelPortal; Q61035; -.
DR   SMR; Q61035; 1-502.
DR   STRING; Q61035; -.
DR   PhosphoSite; Q61035; -.
DR   PRIDE; Q61035; -.
DR   Ensembl; ENSMUST00000001416; ENSMUSP00000001416; ENSMUSG00000001380.
DR   MGI; MGI:108087; Hars.
DR   HOGENOM; HBG616575; -.
DR   HOVERGEN; HBG002731; -.
DR   InParanoid; Q61035; -.
DR   OrthoDB; EOG4D26PM; -.
DR   PhylomeDB; Q61035; -.
DR   BRENDA; 6.1.1.21; 244.
DR   ArrayExpress; Q61035; -.
DR   Bgee; Q61035; -.
DR   CleanEx; MM_HARS; -.
DR   Genevestigator; Q61035; -.
DR   GermOnline; ENSMUSG00000001380; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:EC.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:InterPro.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb_cons-dom.
DR   InterPro; IPR006195; Aminoacyl-tRNA-synth_II.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR015807; His-tRNA-synth_IIa_sub.
DR   InterPro; IPR004516; His-tRNA_synth_IIA.
DR   InterPro; IPR009068; S15_NS1_RNA-bd.
DR   InterPro; IPR000738; WHEP-TRS.
DR   Gene3D; G3DSA:3.40.50.800; Anticodon_bd; 1.
DR   Gene3D; G3DSA:1.10.287.10; S15_NS1_RNA_bd; 1.
DR   PANTHER; PTHR11476; His-tRNA_synth; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   Pfam; PF00458; WHEP-TRS; 1.
DR   PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR   SUPFAM; SSF52954; Anticodon_bd; 1.
DR   SUPFAM; SSF47060; S15/NS1_bind; 1.
DR   TIGRFAMs; TIGR00442; hisS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR   PROSITE; PS00762; WHEP_TRS_1; 1.
DR   PROSITE; PS51185; WHEP_TRS_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    509       Histidyl-tRNA synthetase, cytoplasmic.
FT                                /FTId=PRO_0000136334.
FT   DOMAIN        3     59       WHEP-TRS.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     443    443       N6-acetyllysine (By similarity).
SQ   SEQUENCE   509 AA;  57416 MW;  17BABAAA9771C6F6 CRC64;
     MADRAALEEL VRLQGAHVRG LKEQKASAEQ IEEEVTKLLK LKAQLGQDEG KQKFVLKTPK
     GTRDYSPRQM AVREKVFDVI IRCFKRHGAE VIDTPVFELK ETLTGKYGED SKLIYDLKDQ
     GGELLSLRYD LTVPFARYLA MNKLTNIKRY HIAKVYRRDN PAMTRGRYRE FYQCDFDIAG
     QFDPMIPDAE CLKIMCEILS SLQIGNFLVK VNDRRILDGM FAVCGVPDSK FRTICSSVDK
     LDKVSWEEVK NEMVGEKGLA PEVADRIGDY VQQHGGVSLV EQLLQDPKLS QNKQAVEGLG
     DLKLLFEYLI LFGIDDKISF DLSLARGLDY YTGVIYEAVL LQMPTQAGEE PLGVGSIAAG
     GRYDGLVGMF DPKGRKVPCV GLSIGVERIF SIVEQRLEAS EEKVRTTETQ VLVASAQKKL
     LEERLKLVSE LWDAGIKAEL LYKKNPKLLN QLQYCEEAGI PLVAIIGEQE LKDGVIKLRS
     VASREEVDVQ REDLVEEIRR RTNQPLSIC
//
ID   PAK3_MOUSE              Reviewed;         559 AA.
AC   Q61036; O88645; Q8K1R5; Q8K1R6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   08-MAR-2011, entry version 116.
DE   RecName: Full=Serine/threonine-protein kinase PAK 3;
DE            EC=2.7.11.1;
DE   AltName: Full=Beta-PAK;
DE   AltName: Full=CDC42/RAC effector kinase PAK-B;
DE   AltName: Full=p21-activated kinase 3;
DE            Short=PAK-3;
GN   Name=Pak3; Synonyms=Pak-3, Pakb, Stk4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Fibroblast;
RX   MEDLINE=96032693; PubMed=7559398; DOI=10.1074/jbc.270.39.22731;
RA   Bagrodia S., Taylor S.J., Creasy C.L., Chernoff J., Cerione R.A.;
RT   "Identification of a mouse p21Cdc42/Rac activated kinase.";
RL   J. Biol. Chem. 270:22731-22737(1995).
RN   [2]
RP   ERRATUM.
RA   Bagrodia S., Taylor S.J., Creasy C.L., Chernoff J., Cerione R.A.;
RL   J. Biol. Chem. 271:1250-1250(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   MEDLINE=99282526; PubMed=10352232; DOI=10.1016/S0378-1119(99)00110-9;
RA   Burbelo P.D., Kozak C.A., Finegold A.A., Hall A., Pirone D.M.;
RT   "Cloning, central nervous system expression and chromosomal mapping of
RT   the mouse PAK-1 and PAK-3 genes.";
RL   Gene 232:209-215(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain;
RX   MEDLINE=22450678; PubMed=12464619; DOI=10.1074/jbc.M207251200;
RA   Rousseau V., Goupille O., Morin N., Barnier J.V.;
RT   "A new constitutively active brain Pak3 isoform displays modified
RT   specificities towards Rac and Cdc42 GTPases.";
RL   J. Biol. Chem. 278:3912-3920(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C3H/He; TISSUE=Mesenchymal stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   FUNCTION, AND MUTAGENESIS OF LYS-312.
RX   PubMed=15574732; DOI=10.1523/JNEUROSCI.2931-04.2004;
RA   Boda B., Alberi S., Nikonenko I., Node-Langlois R., Jourdain P.,
RA   Moosmayer M., Parisi-Jourdain L., Muller D.;
RT   "The mental retardation protein PAK3 contributes to synapse formation
RT   and plasticity in hippocampus.";
RL   J. Neurosci. 24:10816-10825(2004).
RN   [8]
RP   STRUCTURE BY NMR OF 65-92 AND 108-123 IN COMPLEX WITH CDC42.
RX   PubMed=10747784; DOI=10.1021/bi992646d;
RA   Gizachew D., Guo W., Chohan K.K., Sutcliffe M.J., Oswald R.E.;
RT   "Structure of the complex of Cdc42Hs with a peptide derived from P-21
RT   activated kinase.";
RL   Biochemistry 39:3963-3971(2000).
CC   -!- FUNCTION: Key regulator of synapse formation and plasticity in the
CC       hippocampus.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activated by binding small G proteins. Binding
CC       of GTP-bound CDC42 or RAC1 to the autoregulatory region releases
CC       monomers from the autoinhibited dimer, enables phosphorylation of
CC       Thr-436 and allows the kinase domain to adopt an active structure
CC       (By similarity).
CC   -!- SUBUNIT: Interacts tightly with GTP-bound but not GDP-bound
CC       CDC42/p21 and RAC1. Shows highly specific binding to the SH3
CC       domains of phospholipase C-gamma and of adapter protein NCK.
CC   -!- INTERACTION:
CC       P60953:CDC42 (xeno); NbExp=1; IntAct=EBI-457317, EBI-81752;
CC       P63000:RAC1 (xeno); NbExp=1; IntAct=EBI-457317, EBI-413628;
CC       P18851:STE4 (xeno); NbExp=1; IntAct=EBI-457317, EBI-7390;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q61036-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q61036-2; Sequence=VSP_010243;
CC   -!- PTM: Autophosphorylated when activated by CDC42/p21.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC   -!- SIMILARITY: Contains 1 CRIB domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U39738; AAC52354.1; -; mRNA.
DR   EMBL; AF082297; AAC31969.1; -; mRNA.
DR   EMBL; AJ496262; CAD42790.1; -; mRNA.
DR   EMBL; AJ496263; CAD42791.1; -; mRNA.
DR   EMBL; AK031853; BAC27580.1; -; mRNA.
DR   EMBL; BC053403; AAH53403.1; -; mRNA.
DR   IPI; IPI00262114; -.
DR   IPI; IPI00411094; -.
DR   PIR; I49376; I49376.
DR   RefSeq; NP_001181977.1; NM_001195048.1.
DR   RefSeq; NP_001181978.1; NM_001195049.1.
DR   RefSeq; NP_032804.2; NM_008778.3.
DR   UniGene; Mm.40035; -.
DR   PDB; 1EES; NMR; -; B=65-123.
DR   PDBsum; 1EES; -.
DR   ProteinModelPortal; Q61036; -.
DR   SMR; Q61036; 65-156, 262-553.
DR   DIP; DIP-447N; -.
DR   IntAct; Q61036; 3.
DR   STRING; Q61036; -.
DR   PhosphoSite; Q61036; -.
DR   PRIDE; Q61036; -.
DR   Ensembl; ENSMUST00000033640; ENSMUSP00000033640; ENSMUSG00000031284.
DR   Ensembl; ENSMUST00000070348; ENSMUSP00000064224; ENSMUSG00000031284.
DR   Ensembl; ENSMUST00000112863; ENSMUSP00000108484; ENSMUSG00000031284.
DR   GeneID; 18481; -.
DR   KEGG; mmu:18481; -.
DR   UCSC; uc009umg.1; mouse.
DR   UCSC; uc009umh.1; mouse.
DR   CTD; 18481; -.
DR   MGI; MGI:1339656; Pak3.
DR   GeneTree; ENSGT00580000081260; -.
DR   HOVERGEN; HBG108518; -.
DR   InParanoid; Q61036; -.
DR   OMA; EFTPDLY; -.
DR   OrthoDB; EOG45DWP5; -.
DR   PhylomeDB; Q61036; -.
DR   BRENDA; 2.7.1.12; 244.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 294190; -.
DR   ArrayExpress; Q61036; -.
DR   Bgee; Q61036; -.
DR   CleanEx; MM_PAK3; -.
DR   CleanEx; MM_STK4; -.
DR   Genevestigator; Q61036; -.
DR   GermOnline; ENSMUSG00000031284; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017048; F:Rho GTPase binding; IPI:BHF-UCL.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000095; PAK_box_Rho-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00786; PBD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00285; PBD; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Allosteric enzyme; Alternative splicing;
KW   ATP-binding; Developmental protein; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase;
KW   SH3-binding; Transferase.
FT   CHAIN         1    559       Serine/threonine-protein kinase PAK 3.
FT                                /FTId=PRO_0000086470.
FT   DOMAIN       70     83       CRIB.
FT   DOMAIN      283    534       Protein kinase.
FT   NP_BIND     289    297       ATP (By similarity).
FT   REGION       65    150       Autoregulatory region (By similarity).
FT   REGION       65    123       GTPase-binding (By similarity).
FT   REGION       84    282       Linker.
FT   ACT_SITE    402    402       Proton acceptor (By similarity).
FT   BINDING     312    312       ATP (Probable).
FT   MOD_RES      50     50       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     154    154       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     436    436       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     535    535       N6-acetyllysine (By similarity).
FT   VAR_SEQ      93    107       Missing (in isoform 2).
FT                                /FTId=VSP_010243.
FT   MUTAGEN     312    312       K->A: Loss of kinase activity.
FT   CONFLICT    176    176       A -> G (in Ref. 1; AAC52354).
FT   CONFLICT    286    286       F -> L (in Ref. 1 and 3).
FT   CONFLICT    376    376       E -> V (in Ref. 1; AAC52354).
FT   CONFLICT    508    508       R -> H (in Ref. 1; AAC52354).
FT   CONFLICT    540    540       L -> M (in Ref. 3; AAC31969).
FT   TURN         88     89
SQ   SEQUENCE   559 AA;  62398 MW;  9AD07B0328F0B08C CRC64;
     MSDSLDNEEK PPAPPLRMNS NNRDSSALNH SSKPLPMAPE EKNKKARLRS IFPGGGDKTN
     KKKEKERPEI SLPSDFEHTI HVGFDAVTGE FTPDLYGSQM CPGKLPEGIP EQWARLLQTS
     NITKLEQKKN PQAVLDVLKF YDSKETVNNQ KYMSFTSGDK SAHGYIAAHQ SNTKTASEPP
     LAPPVSEEED EEEEEEEDDN EPPPVIAPRP EHTKSIYTRS VVESIASPAA PNKEDIPPSA
     ENANSTTLYR NTDRQRKKSK MTDEEILEKL RSIVSVGDPK KKYTRFEKIG QGASGTVYTA
     LDIATGQEVA IKQMNLQQQP KKELIINEIL VMRENKNPNI VNYLDSYLVG DELWVVMEYL
     AGGSLTDVVT ETCMDEGQIA AVCRECLQAL DFLHSNQVIH RDIKSDNILL GMDGSVKLTD
     FGFCAQITPE QSKRSTMVGT PYWMAPEVVT RKAYGPKVDI WSLGIMAIEM VEGEPPYLNE
     NPLRALYLIA TNGTPELQNP ERLSAVFRDF LNRCLEMDVD RRGSAKELLQ HPFLKLAKPL
     SSLTPLIIAA KEAIKNSSR
//
ID   Q61053_MOUSE            Unreviewed;       237 AA.
AC   Q61053;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   SubName: Full=FBP 17;
DE   Flags: Fragment;
GN   Name=Fnbp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FVB;
RX   MEDLINE=96183189; PubMed=8605874;
RA   Chan D.C., Bedford M.T., Leder P.;
RT   "Formin binding proteins bear WWP/WW domains that bind proline-rich
RT   peptides and functionally resemble SH3 domains.";
RL   EMBO J. 15:1045-1054(1996).
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; U40751; AAC52479.1; -; mRNA.
DR   IPI; IPI00466701; -.
DR   PIR; S64718; S64718.
DR   UniGene; Mm.440993; -.
DR   UniGene; Mm.52297; -.
DR   HSSP; P14598; 1OV3.
DR   ProteinModelPortal; Q61053; -.
DR   IntAct; Q61053; 2.
DR   STRING; Q61053; -.
DR   Ensembl; ENSMUST00000075326; ENSMUSP00000074796; ENSMUSG00000075415.
DR   Ensembl; ENSMUST00000100208; ENSMUSP00000097782; ENSMUSG00000075415.
DR   UCSC; uc008jdl.1; mouse.
DR   MGI; MGI:109606; Fnbp1.
DR   GeneTree; ENSGT00510000046403; -.
DR   HOVERGEN; HBG002489; -.
DR   ArrayExpress; Q61053; -.
DR   Bgee; Q61053; -.
DR   Genevestigator; Q61053; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR000861; HR1_rpt_rho-bd.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF02185; HR1; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   SH3 domain.
FT   NON_TER       1      1
SQ   SEQUENCE   237 AA;  27173 MW;  4E23794C8CC744D7 CRC64;
     KIHCFRSLKR GGVTPEDFSN FPPEQRRKKL QQKVDDLNRE IQKETDQRDA ITKMKDVYLK
     NPQMGDPASL DQKLTEVTQN IEKLRLEAQK FEAWLAEVEG RLPARSEQAR RQSGLYDGQT
     HQTVTNCAQD RESPDGSYTE EQSQESEHKV LAPDFDDEFD DEEPLPAIGT CKALYTFEGQ
     NEGTISVVEG ETLSVIEEDK GDGWTRIRRN EDEEGYFPTS YVEVYLDKNA KGAKTYI
//
ID   DVL3_MOUSE              Reviewed;         716 AA.
AC   Q61062;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Segment polarity protein dishevelled homolog DVL-3;
DE            Short=Dishevelled-3;
DE   AltName: Full=DSH homolog 3;
GN   Name=Dvl3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=97081279; PubMed=8922524;
RX   DOI=10.1002/(SICI)1097-0177(199611)207:3<253::AID-AJA2>3.0.CO;2-G;
RA   Tsang M., Lijam N., Yang Y., Beier D.R., Wynshaw-Boris A.,
RA   Sussman D.J.;
RT   "Isolation and characterization of mouse dishevelled-3.";
RL   Dev. Dyn. 207:253-262(1996).
RN   [2]
RP   INTERACTION WITH VANGL1 AND VANGL2.
RX   PubMed=15456783; DOI=10.1074/jbc.M408675200;
RA   Torban E., Wang H.-J., Groulx N., Gros P.;
RT   "Independent mutations in mouse Vangl2 that cause neural tube defects
RT   in looptail mice impair interaction with members of the Dishevelled
RT   family.";
RL   J. Biol. Chem. 279:52703-52713(2004).
CC   -!- FUNCTION: May play a role in the signal transduction pathway
CC       mediated by multiple Wnt genes.
CC   -!- SUBUNIT: Interacts (via the PDZ domain) with the C-terminal
CC       regions of VANGL1 and VANGL2. Interacts (via the region containing
CC       both the PDZ and DEP domains) with LRRFIP2; the DIX domain may
CC       inhibit this interaction. Interacts with CYLD (By similarity).
CC   -!- INTERACTION:
CC       Q80Z96:Vangl1; NbExp=1; IntAct=EBI-1538450, EBI-1750708;
CC       Q91ZD4:Vangl2; NbExp=1; IntAct=EBI-1538450, EBI-1750744;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- PTM: Ubiquitinated. Deubiquitinated by CYLD, which acts on 'Lys-
CC       63'-linked ubiquitin chains (By similarity).
CC   -!- SIMILARITY: Belongs to the DSH family.
CC   -!- SIMILARITY: Contains 1 DEP domain.
CC   -!- SIMILARITY: Contains 1 DIX domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; U41285; AAB01761.1; -; mRNA.
DR   IPI; IPI00117059; -.
DR   UniGene; Mm.247259; -.
DR   UniGene; Mm.272443; -.
DR   ProteinModelPortal; Q61062; -.
DR   SMR; Q61062; 2-82, 247-335, 411-499.
DR   IntAct; Q61062; 7.
DR   STRING; Q61062; -.
DR   PhosphoSite; Q61062; -.
DR   PRIDE; Q61062; -.
DR   Ensembl; ENSMUST00000003318; ENSMUSP00000003318; ENSMUSG00000003233.
DR   UCSC; uc007ypw.1; mouse.
DR   MGI; MGI:108100; Dvl3.
DR   eggNOG; roNOG10726; -.
DR   GeneTree; ENSGT00390000013552; -.
DR   HOGENOM; HBG717800; -.
DR   HOVERGEN; HBG005542; -.
DR   InParanoid; Q61062; -.
DR   OrthoDB; EOG4TQM8S; -.
DR   ArrayExpress; Q61062; -.
DR   Bgee; Q61062; -.
DR   CleanEx; MM_DVL3; -.
DR   Genevestigator; Q61062; -.
DR   GermOnline; ENSMUSG00000003233; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0090103; P:cochlea morphogenesis; IGI:MGI.
DR   GO; GO:0003148; P:outflow tract septum morphogenesis; IMP:MGI.
DR   GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IGI:MGI.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR008339; Dishevelled.
DR   InterPro; IPR008342; Dishevelled_3.
DR   InterPro; IPR003351; Dishevelled_protein.
DR   InterPro; IPR001158; DIX.
DR   InterPro; IPR015506; Dsh.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   PANTHER; PTHR10878; Dsh; 1.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF02377; Dishevelled; 1.
DR   Pfam; PF00778; DIX; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   PRINTS; PR01760; DISHEVELLED.
DR   PRINTS; PR01763; DISHEVELLED3.
DR   SMART; SM00021; DAX; 1.
DR   SMART; SM00049; DEP; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50186; DEP; 1.
DR   PROSITE; PS50841; DIX; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Developmental protein; Phosphoprotein; Ubl conjugation;
KW   Wnt signaling pathway.
FT   CHAIN         1    716       Segment polarity protein dishevelled
FT                                homolog DVL-3.
FT                                /FTId=PRO_0000145750.
FT   DOMAIN        1     82       DIX.
FT   DOMAIN      249    321       PDZ.
FT   DOMAIN      422    496       DEP.
FT   MOD_RES     346    346       Phosphothreonine (By similarity).
SQ   SEQUENCE   716 AA;  78123 MW;  55412C03202301F0 CRC64;
     MGETKIIYHL DGQETPYLVK LPLPAERVTL ADFKGVLQRP SYKFFFKSMD DDFGVVKEEI
     SDDNAKLPCF NGRVVSWLVS AEGSHPEPAP FCADNPSELP PSMERTGGIG DSRPPSFHPH
     ASGGSQENLD NDTETDSLVS AQRERPRRRD GPEHAARLNG TTKGERRREP GGYDSSSTLM
     SSELETTSFF DSDEDDSTSR FSSSTEQSSA SRLMRRHKRR RRKQKVSRIE RSSSFSSITD
     STMSLNIITV TLNMEKYNFL GISIVGQSNE RGDGGIYIGS IMKGGAVAAD GRIEPGDMLL
     QVNEINFENM SNDDAVRVLR EIVHKPGPIT LTVAKCWDPS PRGCFTLPRS EPIRPIDPAA
     WVSHTAAMTG TFPAYGMSPS LSTITSTSSS ITSSIPDTER LDDFHLSIHS DMAAIVKAMA
     SPESGLEVRD RMWLKITIPN AFIGSDVVDW LYHNVEGFTE RREARKYASN LLKAGFIRHT
     VNKITFSEQC YYIFGDLCGN MANLSLHDHD GSSGASDQDT LAPLPHPGAA PWPMAFPYQY
     PPPPHPYNPH PGFPELGYSY GGGSASSQHS EGSRSSGSNR SGSDRRKEKD PKAGDSKSGG
     SGSESDHTTR SSLRGPRERA PSERSGPAAS EHSHRSHHSL TSSLRSHHTH PSYGPPGVPP
     LYGPPMLMMT PPPGAMGPPG APPGRDLASV PPELTASRQS FRMAMGNPSE FFVDVM
//
ID   EI24_MOUSE              Reviewed;         340 AA.
AC   Q61070; Q3T9X1; Q3TVX9; Q3UGS7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 3.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Etoposide-induced protein 2.4;
DE   AltName: Full=p53-induced gene 8 protein;
GN   Name=Ei24; Synonyms=Pig8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fibroblast;
RX   MEDLINE=96226348; PubMed=8649819;
RA   Lehar S.M., Nacht M., Jacks T., Vater C.A., Chittenden T., Guild B.C.;
RT   "Identification and cloning of EI24, a gene induced by p53 in
RT   etoposide-treated cells.";
RL   Oncogene 12:1181-1187(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318 AND SER-326, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May play a role in the cellular response to DNA damage
CC       and/or p53-mediated apoptosis.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- TISSUE SPECIFICITY: Found in all the examined tissues. High
CC       expression was found in liver, skeletal muscle, pancreas, kidney
CC       heart and to a lesser extent in brain, placenta and lung.
CC   -!- INDUCTION: By etoposide treatment, induction requires p53.
CC       Etoposide induces DNA damage in cells by inhibiting DNA
CC       topoisomerase II, and ultimately causes apoptotic cell death.
CC   -!- SIMILARITY: Belongs to the EI24 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC52483.2; Type=Erroneous initiation;
CC       Sequence=BAE28130.1; Type=Erroneous initiation;
CC       Sequence=BAE35489.1; Type=Erroneous initiation;
CC       Sequence=BAE42899.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; U41751; AAC52483.2; ALT_INIT; mRNA.
DR   EMBL; AK147776; BAE28130.1; ALT_INIT; mRNA.
DR   EMBL; AK159927; BAE35489.1; ALT_INIT; mRNA.
DR   EMBL; AK172233; BAE42899.1; ALT_INIT; mRNA.
DR   IPI; IPI00117068; -.
DR   RefSeq; NP_001186423.1; NM_001199494.1.
DR   RefSeq; NP_031941.1; NM_007915.5.
DR   UniGene; Mm.4337; -.
DR   STRING; Q61070; -.
DR   PhosphoSite; Q61070; -.
DR   PRIDE; Q61070; -.
DR   Ensembl; ENSMUST00000115086; ENSMUSP00000110738; ENSMUSG00000062762.
DR   GeneID; 13663; -.
DR   KEGG; mmu:13663; -.
DR   NMPDR; fig|10090.3.peg.19881; -.
DR   UCSC; uc009oua.1; mouse.
DR   CTD; 13663; -.
DR   MGI; MGI:108090; Ei24.
DR   eggNOG; roNOG12248; -.
DR   HOGENOM; HBG445394; -.
DR   HOVERGEN; HBG001857; -.
DR   InParanoid; Q61070; -.
DR   OrthoDB; EOG4JM7QC; -.
DR   NextBio; 284408; -.
DR   ArrayExpress; Q61070; -.
DR   Bgee; Q61070; -.
DR   CleanEx; MM_EI24; -.
DR   Genevestigator; Q61070; -.
DR   GermOnline; ENSMUSG00000062762; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006917; P:induction of apoptosis; IDA:MGI.
DR   GO; GO:0042493; P:response to drug; IMP:MGI.
DR   InterPro; IPR009890; EI24.
DR   PANTHER; PTHR21389; EI24; 1.
DR   Pfam; PF07264; EI24; 1.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    340       Etoposide-induced protein 2.4.
FT                                /FTId=PRO_0000086946.
FT   TRANSMEM     77     97       Helical; (Potential).
FT   TRANSMEM    117    137       Helical; (Potential).
FT   TRANSMEM    179    199       Helical; (Potential).
FT   TRANSMEM    238    255       Helical; (Potential).
FT   TRANSMEM    257    277       Helical; (Potential).
FT   COMPBIAS     41     44       Poly-Arg.
FT   COMPBIAS    316    320       Poly-Ser.
FT   MOD_RES      56     56       Phosphoserine.
FT   MOD_RES     318    318       Phosphoserine.
FT   MOD_RES     326    326       Phosphoserine.
FT   MOD_RES     330    330       Phosphoserine (By similarity).
FT   CONFLICT     78     78       N -> D (in Ref. 2; BAE28130).
FT   CONFLICT    144    144       I -> F (in Ref. 2; BAE35489).
FT   CONFLICT    320    320       S -> P (in Ref. 2; BAE42899).
SQ   SEQUENCE   340 AA;  38933 MW;  AA3B824B2CE330BC CRC64;
     MADSVKTFLQ DLGRGIKDSI WGICTISKLD ARIQQKREEQ RRRRASSLLA QRRPQSVERK
     QESEPRIVSR IFQCCAWNGG VFWFSLLLFY RVFIPVLQSV TARIIGDPSL HGDVWSWLEF
     FLTSIFSALW VLPLFVLSKV VNAIWFQDIA DLAFEVSGRK PHPFPSVSKI IADMLFNLLL
     QALFLIQGMF VSLFPIHLVG QLVSLLHMSL LYSLYCFEYR WFNKGIEMHQ RLSNIERNWP
     YYFGFGLPLA FLTAMQSSYI ISGCLFSILF PLFIISANEA KTPGKAYLFQ LRLFSLVVFL
     SNRLFHKTVY LQSALSSSSS AEKFPSPHPS PAKLKAAAGH
//
ID   CDC37_MOUSE             Reviewed;         379 AA.
AC   Q61081; Q3TGP0;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Hsp90 co-chaperone Cdc37;
DE   AltName: Full=Hsp90 chaperone protein kinase-targeting subunit;
DE   AltName: Full=p50Cdc37;
GN   Name=Cdc37;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   MEDLINE=96258250; PubMed=8666233;
RA   Stepanova L., Leng X., Parker S.B., Harper J.W.;
RT   "Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90
RT   that binds and stabilizes Cdk4.";
RL   Genes Dev. 10:1491-1502(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Embryonic stem cell, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Co-chaperone that binds to numerous kinases and promotes
CC       their interaction with the Hsp90 complex, resulting in
CC       stabilization and promotion of their activity.
CC   -!- SUBUNIT: Forms a complex with Hsp90. Interacts with AR, CDK4,
CC       CDK6, EIF2AK1 and RB1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the CDC37 family.
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DR   EMBL; U43076; AAB18761.1; -; mRNA.
DR   EMBL; AK010494; BAB26984.1; -; mRNA.
DR   EMBL; AK013255; BAB28749.1; -; mRNA.
DR   EMBL; AK145671; BAE26580.1; -; mRNA.
DR   EMBL; AK168651; BAE40508.1; -; mRNA.
DR   EMBL; BC060079; AAH60079.1; -; mRNA.
DR   IPI; IPI00117087; -.
DR   RefSeq; NP_058022.1; NM_016742.4.
DR   UniGene; Mm.32331; -.
DR   ProteinModelPortal; Q61081; -.
DR   SMR; Q61081; 149-348.
DR   STRING; Q61081; -.
DR   PhosphoSite; Q61081; -.
DR   PRIDE; Q61081; -.
DR   Ensembl; ENSMUST00000019615; ENSMUSP00000019615; ENSMUSG00000019471.
DR   GeneID; 12539; -.
DR   KEGG; mmu:12539; -.
DR   UCSC; uc009okg.1; mouse.
DR   CTD; 12539; -.
DR   MGI; MGI:109531; Cdc37.
DR   eggNOG; roNOG14905; -.
DR   GeneTree; ENSGT00390000013443; -.
DR   HOGENOM; HBG715286; -.
DR   HOVERGEN; HBG056343; -.
DR   InParanoid; Q61081; -.
DR   OMA; GLWVPNA; -.
DR   OrthoDB; EOG4CVG75; -.
DR   NextBio; 281578; -.
DR   ArrayExpress; Q61081; -.
DR   Bgee; Q61081; -.
DR   CleanEx; MM_CDC37; -.
DR   Genevestigator; Q61081; -.
DR   GermOnline; ENSMUSG00000019471; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0051879; F:Hsp90 protein binding; IDA:MGI.
DR   InterPro; IPR004918; Cdc37.
DR   InterPro; IPR013873; Cdc37_C.
DR   InterPro; IPR013874; Cdc37_Hsp90-bd.
DR   InterPro; IPR013855; Cdc37_N.
DR   PANTHER; PTHR12800; Cdc37; 1.
DR   Pfam; PF08564; CDC37_C; 1.
DR   Pfam; PF08565; CDC37_M; 1.
DR   Pfam; PF03234; CDC37_N; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; Chaperone; Cytoplasm; Phosphoprotein.
FT   CHAIN         1    379       Hsp90 co-chaperone Cdc37.
FT                                /FTId=PRO_0000195058.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      13     13       Phosphoserine (By similarity).
FT   MOD_RES      45     45       N6-acetyllysine (By similarity).
FT   MOD_RES     155    155       N6-acetyllysine (By similarity).
FT   MOD_RES     241    241       N6-acetyllysine (By similarity).
FT   MOD_RES     299    299       Phosphotyrosine (By similarity).
FT   MOD_RES     331    331       N6-acetyllysine (By similarity).
FT   MOD_RES     378    378       Phosphoserine (By similarity).
SQ   SEQUENCE   379 AA;  44593 MW;  847C146B4FE3AAF1 CRC64;
     MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRGCRECKRK
     VAECQRKLKE LEVAESDGQV ELERLRAEAQ QLRKEERSWE QKLEDMRKKE KNMPWNVDTL
     SKDGFSKSMV NTKPEKAEED SEEAREQKHK TFVEKYEKQI KHFGMLHRWD DSQKYLSDNV
     HLVCEETANY LVIWCIDLEV EEKCALMEQV AHQTMVMQFI LELAKSLKVD PRACFRQFFT
     KIKTADHQYM EGFKYELEAF KERVRGRAKL RIEKAMKEYE EEERKKRLGP GGLDPVEVYE
     SLPEELQKCF DVKDVQMLQD AISKMDPTDA KYHMQRCIDS GLWVPNSKSG EAKEGEEAGP
     GDPLLEAVPK AGNEKDVSA
//
ID   KSR1_MOUSE              Reviewed;         873 AA.
AC   Q61097; Q61648; Q78DX8;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Kinase suppressor of Ras 1;
DE            Short=mKSR1;
DE   AltName: Full=Protein Hb;
GN   Name=Ksr1; Synonyms=Ksr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH HSPCA;
RP   YWHAB; CDC37 AND MAP2K.
RX   MEDLINE=96107327; PubMed=8521512; DOI=10.1016/0092-8674(95)90204-X;
RA   Therrien M., Chang H.C., Solomon N.M., Karim F.D., Wassarman D.A.,
RA   Rubin G.M.;
RT   "KSR, a novel protein kinase required for RAS signal transduction.";
RL   Cell 83:879-888(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2), INTERACTION WITH MAPK,
RP   MUTAGENESIS OF GLY-572; ARG-589; ARG-615; ASP-700 AND CYS-809, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=10891492; DOI=10.1128/MCB.20.15.5529-5539.2000;
RA   Mueller J., Cacace A.M., Lyons W.E., McGill C.B., Morrison D.K.;
RT   "Identification of B-KSR1, a novel brain-specific isoform of KSR1 that
RT   functions in neuronal signaling.";
RL   Mol. Cell. Biol. 20:5529-5539(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Pelan S.;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 49-474 (ISOFORMS 1/2).
RC   STRAIN=BALB/c;
RX   MEDLINE=95352957; PubMed=7626882; DOI=10.1007/BF00364794;
RA   Nehls M., Luno K., Schorpp M., Pfeifer D., Krause S.,
RA   Matysiak-Scholze U., Dierbach H., Boehm T.;
RT   "YAC/P1 contigs defining the location of 56 microsatellite markers and
RT   several genes across a 3.4cM interval on mouse chromosome 11.";
RL   Mamm. Genome 6:321-331(1995).
RN   [5]
RP   INTERACTION WITH MARK3, PHOSPHORYLATION AT SER-297 AND SER-392, AND
RP   MUTAGENESIS OF SER-297; SER-392; ILE-397 AND VAL-401.
RX   PubMed=11741534; DOI=10.1016/S1097-2765(01)00383-5;
RA   Mueller J., Ory S., Copeland T., Piwnica-Worms H., Morrison D.K.;
RT   "C-TAK1 regulates Ras signaling by phosphorylating the MAPK scaffold,
RT   KSR1.";
RL   Mol. Cell 8:983-993(2001).
RN   [6]
RP   INTERACTION WITH PPP2R1A AND PPP2CA, AND DEPHOSPHORYLATION BY PPP2CA.
RX   PubMed=12932319; DOI=10.1016/S0960-9822(03)00535-9;
RA   Ory S., Zhou M., Conrads T.P., Veenstra T.D., Morrison D.K.;
RT   "Protein phosphatase 2A positively regulates Ras signaling by
RT   dephosphorylating KSR1 and Raf-1 on critical 14-3-3 binding sites.";
RL   Curr. Biol. 13:1356-1364(2003).
RN   [7]
RP   REVIEW.
RX   PubMed=12007434; DOI=10.1016/S0960-9822(02)00831-X;
RA   Roy F., Therrien M.;
RT   "MAP kinase module: the Ksr connection.";
RL   Curr. Biol. 12:R325-R327(2002).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   STRUCTURE BY NMR OF 331-378 IN COMPLEX WITH ZINC.
RX   PubMed=11786023; DOI=10.1006/jmbi.2001.5263;
RA   Zhou M., Horita D.A., Waugh D.S., Byrd R.A., Morrison D.K.;
RT   "Solution structure and functional analysis of the cysteine-rich C1
RT   domain of kinase suppressor of Ras (KSR).";
RL   J. Mol. Biol. 315:435-446(2002).
CC   -!- FUNCTION: Location-regulated scaffolding protein connecting MEK to
CC       RAF. Promotes MEK and RAF phosphorylation and activity through
CC       assembly of an activated signaling complex. By itself, it has no
CC       demonstrated kinase activity.
CC   -!- SUBUNIT: Interacts with HSPCA/HSP90, YWHAB/14-3-3, CDC37,
CC       MAP2K/MEK, MARK3, PPP2R1A and PPP2CA. Also interacts with RAF and
CC       MAPK/ERK, in a Ras-dependent manner. The binding of 14-3-3
CC       proteins to phosphorylated KSR prevents the membrane localization.
CC   -!- INTERACTION:
CC       P15531:NME1 (xeno); NbExp=2; IntAct=EBI-1536336, EBI-741141;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC       protein. Note=In unstimulated cells, where the phosphorylated form
CC       is bound to a 14-3-3 protein, sequestration in the cytoplasm
CC       occurs. Following growth factor treatment, the protein is free for
CC       membrane translocation, and it moves from the cytoplasm to the
CC       cell periphery.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q61097-1; Sequence=Displayed;
CC       Name=2; Synonyms=B-KSR1;
CC         IsoId=Q61097-2; Sequence=VSP_012232, VSP_012233;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, spleen and testis. Isoform
CC       1 is highly expressed spleen and weakly in testis, and isoform 2
CC       is highly expressed in brain and weakly in testis.
CC   -!- PTM: Phosphorylated on Ser-297 and, to a higher extent, on Ser-392
CC       by MARK3. Dephosphorylated on Ser-392 by PPP2CA. Phosphorylated
CC       KSR is cytoplasmic and dephosphorylated KSR is membrane-
CC       associated.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family.
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; U43585; AAC52382.1; -; mRNA.
DR   EMBL; AL592551; CAI24047.1; -; Genomic_DNA.
DR   EMBL; X81634; CAA57288.1; -; mRNA.
DR   IPI; IPI00515699; -.
DR   IPI; IPI00623208; -.
DR   PIR; I48379; I48379.
DR   RefSeq; NP_038599.1; NM_013571.2.
DR   UniGene; Mm.4745; -.
DR   PDB; 1KBE; NMR; -; A=331-378.
DR   PDB; 1KBF; NMR; -; A=331-378.
DR   PDBsum; 1KBE; -.
DR   PDBsum; 1KBF; -.
DR   ProteinModelPortal; Q61097; -.
DR   SMR; Q61097; 331-378, 554-831.
DR   IntAct; Q61097; 8.
DR   MINT; MINT-99547; -.
DR   STRING; Q61097; -.
DR   PhosphoSite; Q61097; -.
DR   PRIDE; Q61097; -.
DR   Ensembl; ENSMUST00000018478; ENSMUSP00000018478; ENSMUSG00000018334.
DR   Ensembl; ENSMUST00000100745; ENSMUSP00000098310; ENSMUSG00000018334.
DR   GeneID; 16706; -.
DR   KEGG; mmu:16706; -.
DR   CTD; 16706; -.
DR   MGI; MGI:105051; Ksr1.
DR   GeneTree; ENSGT00600000084040; -.
DR   HOGENOM; HBG714131; -.
DR   HOVERGEN; HBG052293; -.
DR   InParanoid; Q61097; -.
DR   OMA; AQGPRSI; -.
DR   OrthoDB; EOG4TTGH8; -.
DR   NextBio; 290486; -.
DR   ArrayExpress; Q61097; -.
DR   Bgee; Q61097; -.
DR   CleanEx; MM_KSR1; -.
DR   Genevestigator; Q61097; -.
DR   GermOnline; ENSMUSG00000018334; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   SMART; SM00109; C1; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Membrane;
KW   Metal-binding; Phosphoprotein; Zinc; Zinc-finger.
FT   CHAIN         1    873       Kinase suppressor of Ras 1.
FT                                /FTId=PRO_0000086230.
FT   DOMAIN      563    833       Protein kinase.
FT   ZN_FING     333    377       Phorbol-ester/DAG-type.
FT   COMPBIAS     17     21       Poly-Gly.
FT   COMPBIAS    275    278       Poly-Pro.
FT   COMPBIAS    429    491       Ser-rich.
FT   METAL       334    334       Zinc 1.
FT   METAL       346    346       Zinc 2.
FT   METAL       349    349       Zinc 2.
FT   METAL       359    359       Zinc 1.
FT   METAL       362    362       Zinc 1.
FT   METAL       367    367       Zinc 2.
FT   METAL       370    370       Zinc 2.
FT   METAL       377    377       Zinc 1.
FT   MOD_RES     256    256       Phosphothreonine (By similarity).
FT   MOD_RES     260    260       Phosphothreonine (By similarity).
FT   MOD_RES     297    297       Phosphoserine; by MARK3.
FT   MOD_RES     320    320       Phosphoserine (By similarity).
FT   MOD_RES     392    392       Phosphoserine; by MARK3.
FT   MOD_RES     518    518       Phosphoserine (By similarity).
FT   VAR_SEQ     474    474       P -> PAAYFIHHRQQFIFP (in isoform 2).
FT                                /FTId=VSP_012232.
FT   VAR_SEQ     848    873       DINSSKVMPRFERFGLGTLESGNPKM -> EL (in
FT                                isoform 2).
FT                                /FTId=VSP_012233.
FT   MUTAGEN     297    297       S->A: Constitutive targeting to the
FT                                plasma membrane; when associated with A-
FT                                392.
FT   MUTAGEN     392    392       S->A: Constitutive targeting to the
FT                                plasma membrane; when associated with A-
FT                                297.
FT   MUTAGEN     397    397       I->A: Decrease in MARK3 binding; when
FT                                associated with A-401.
FT   MUTAGEN     401    401       V->A: Decrease in MARK3 binding; when
FT                                associated with A-397.
FT   MUTAGEN     572    572       G->E: Decrease in MEK binding.
FT   MUTAGEN     589    589       R->M: Almost no MEK binding.
FT   MUTAGEN     615    615       R->H: Decrease in MEK binding.
FT   MUTAGEN     700    700       D->V: Decrease in MEK binding.
FT   MUTAGEN     809    809       C->Y: No MEK binding.
FT   STRAND      336    339
FT   STRAND      347    349
FT   STRAND      356    359
FT   TURN        360    363
FT   STRAND      364    369
FT   TURN        371    373
SQ   SEQUENCE   873 AA;  96755 MW;  EAEEB23FAE715D94 CRC64;
     MDRAALRAAA MGEKKEGGGG GAAADGGAGA AVSRALQQCG QLQKLIDISI GSLRGLRTKC
     SVSNDLTQQE IRTLEAKLVK YICKQQQSKL SVTPSDRTAE LNSYPRFSDW LYIFNVRPEV
     VQEIPQELTL DALLEMDEAK AKEMLRRWGA STEECSRLQQ ALTCLRKVTG LGGEHKMDSG
     WSSTDARDSS LGPPMDMLSS LGRAGASTQG PRSISVSALP ASDSPVPGLS EGLSDSCIPL
     HTSGRLTPRA LHSFITPPTT PQLRRHAKLK PPRTPPPPSR KVFQLLPSFP TLTRSKSHES
     QLGNRIDDVT PMKFELPHGS PQLVRRDIGL SVTHRFSTKS WLSQVCNVCQ KSMIFGVKCK
     HCRLKCHNKC TKEAPACRIT FLPLARLRRT ESVPSDINNP VDRAAEPHFG TLPKALTKKE
     HPPAMNLDSS SNPSSTTSST PSSPAPFLTS SNPSSATTPP NPSPGQRDSR FSFPDISACS
     QAAPLSSTAD STRLDDQPKT DVLGVHEAEA EEPEAGKSEA EDDEEDEVDD LPSSRRPWRG
     PISRKASQTS VYLQEWDIPF EQVELGEPIG QGRWGRVHRG RWHGEVAIRL LEMDGHNQDH
     LKLFKKEVMN YRQTRHENVV LFMGACMNPP HLAIITSFCK GRTLHSFVRD PKTSLDINKT
     RQIAQEIIKG MGYLHAKGIV HKDLKSKNVF YDNGKVVITD FGLFGISGVV REERRENQLK
     LSHDWLCYLA PEIVREMIPG RDEDQLPFSK AADVYAFGTV WYELQARDWP FKHQPAEALI
     WQIGSGEGVR RVLASVSLGK EVGEILSACW AFDLQERPSF SLLMDMLERL PKLNRRLSHP
     GHFWKSADIN SSKVMPRFER FGLGTLESGN PKM
//
ID   SHC3_MOUSE              Reviewed;         474 AA.
AC   Q61120;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=SHC-transforming protein 3;
DE   AltName: Full=Neuronal Shc;
DE            Short=N-Shc;
DE   AltName: Full=SHC-transforming protein C;
DE   AltName: Full=Src homology 2 domain-containing-transforming protein C3;
DE            Short=SH2 domain protein C3;
GN   Name=Shc3; Synonyms=Nshc, ShcC;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96181475; PubMed=8610109; DOI=10.1073/pnas.93.7.2729;
RA   O'Bryan J.P., Songyang Z., Cantley L., Der C.J., Pawson T.;
RT   "A mammalian adaptor protein with conserved Src homology 2 and
RT   phosphotyrosine-binding domains is related to Shc and is specifically
RT   expressed in the brain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:2729-2734(1996).
CC   -!- FUNCTION: Signaling adapter that couples activated growth factor
CC       receptors to signaling pathway in neurons. Involved in the signal
CC       transduction pathways of neurotrophin-activated Trk receptors in
CC       cortical neurons (By similarity).
CC   -!- SUBUNIT: Interacts with the Trk receptors in a phosphotyrosine-
CC       dependent manner. Once activated, binds to GRB2. Interacts with
CC       activated EGF receptors (By similarity).
CC   -!- INTERACTION:
CC       P12023:App; NbExp=1; IntAct=EBI-79107, EBI-78814;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in the adult brain.
CC   -!- PTM: Tyrosine phosphorylated (By similarity).
CC   -!- SIMILARITY: Contains 1 PID domain.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; U46854; AAC52508.1; -; mRNA.
DR   IPI; IPI00117773; -.
DR   RefSeq; NP_033193.2; NM_009167.3.
DR   UniGene; Mm.131870; -.
DR   ProteinModelPortal; Q61120; -.
DR   SMR; Q61120; 16-190, 328-473.
DR   IntAct; Q61120; 2.
DR   MINT; MINT-258872; -.
DR   STRING; Q61120; -.
DR   PhosphoSite; Q61120; -.
DR   PRIDE; Q61120; -.
DR   Ensembl; ENSMUST00000021898; ENSMUSP00000021898; ENSMUSG00000021448.
DR   GeneID; 20418; -.
DR   KEGG; mmu:20418; -.
DR   UCSC; uc007qmg.1; mouse.
DR   CTD; 20418; -.
DR   MGI; MGI:106179; Shc3.
DR   GeneTree; ENSGT00390000018860; -.
DR   HOGENOM; HBG314352; -.
DR   HOVERGEN; HBG050121; -.
DR   InParanoid; Q61120; -.
DR   OrthoDB; EOG4SF960; -.
DR   NextBio; 298416; -.
DR   ArrayExpress; Q61120; -.
DR   Bgee; Q61120; -.
DR   Genevestigator; Q61120; -.
DR   GermOnline; ENSMUSG00000021448; Mus musculus.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0007611; P:learning or memory; IMP:MGI.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR006019; PID_domain.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   InterPro; IPR000980; SH2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF00640; PID; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00629; SHCPIDOMAIN.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM00252; SH2; 1.
DR   PROSITE; PS01179; PID; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; SH2 domain.
FT   CHAIN         1    474       SHC-transforming protein 3.
FT                                /FTId=PRO_0000097735.
FT   DOMAIN       29    214       PID.
FT   DOMAIN      379    470       SH2.
FT   REGION      215    378       CH1.
SQ   SEQUENCE   474 AA;  52206 MW;  DEE6CBA83A54A6C4 CRC64;
     MSATRKSRAG DEPLPRPPRG APHTSDQVLG PGVTYVVKYL GCIEVLRSMR SLDFSTRTQV
     TREAISRVCE RVPGAKGALK KRKPPSKMLS SILGKSNLQF AGMSISLTIS TASLNLRTPD
     SKQIIANHHM RSISFASGGD PDTTDYVAYV AKDPVNRRAC HILECCDGLA QDVIGSIGQA
     FELRFKQYLQ CPSKVPALQD RMQSLDEPWT EEEGDGPDHP YYNSVPTKMP PPGGFLDARL
     KGRPHAPEAA QFAGKEQTYY QGRHLGDTFG EDWQRAPTRQ GSLDIYSTAE GKTHMVPVGE
     TPTYVNTQPV PPQVWPAATS STESSPRKDL FDMKPFEDAL RNQPLGPMLS KAASVECISP
     VTPRAPDARM LEELNAEPWY QGEMSRKEAE ALLREDGDFL VRKSTTNPGS FVLTGMHNGQ
     AKHLLLVDPE GTIRTKDRVF DSISHLINYH LESSLPIVSA GSELCLQQPV ERKP
//
ID   ASTN1_MOUSE             Reviewed;        1302 AA.
AC   Q61137; Q505A0; Q7TQG3; Q8CHH2;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 3.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Astrotactin-1;
DE   AltName: Full=Neuronal migration protein GC14;
DE   Flags: Precursor;
GN   Name=Astn1; Synonyms=Astn, Kiaa0289;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 44-1302 (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   MEDLINE=96185502; PubMed=8602532; DOI=10.1126/science.272.5260.417;
RA   Zheng C., Heintz N., Hatten M.E.;
RT   "CNS gene encoding astrotactin, which supports neuronal migration
RT   along glial fibers.";
RL   Science 272:417-419(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 46-1302 (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [4]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54 AND SER-1088, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: Neuronal adhesion molecule that is required for glial-
CC       guided migration of young postmitotic neuroblasts in cortical
CC       regions of developing brain, including cerebrum, hippocampus,
CC       cerebellum and olfactory bulb.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q61137-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q61137-2; Sequence=VSP_014917;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed specifically in the brain. Expressed
CC       in the cerebellum, hippocampus, cerebrum and olfactory bulb.
CC   -!- SIMILARITY: Belongs to the astrotactin family.
CC   -!- SIMILARITY: Contains 3 EGF-like domains.
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC52516.1; Type=Frameshift; Positions=84, 92, 185, 274, 370, 439, 469, 488, 592, 595;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; BC054545; AAH54545.1; -; mRNA.
DR   EMBL; BC094666; AAH94666.1; -; mRNA.
DR   EMBL; U48797; AAC52516.1; ALT_FRAME; mRNA.
DR   EMBL; AB093222; BAC41406.2; -; mRNA.
DR   IPI; IPI00117803; -.
DR   IPI; IPI00620601; -.
DR   RefSeq; NP_031521.2; NM_007495.3.
DR   UniGene; Mm.329586; -.
DR   ProteinModelPortal; Q61137; -.
DR   SMR; Q61137; 660-715.
DR   STRING; Q61137; -.
DR   PhosphoSite; Q61137; -.
DR   PRIDE; Q61137; -.
DR   Ensembl; ENSMUST00000046110; ENSMUSP00000039711; ENSMUSG00000026587.
DR   GeneID; 11899; -.
DR   KEGG; mmu:11899; -.
DR   UCSC; uc007dds.1; mouse.
DR   UCSC; uc007ddu.1; mouse.
DR   CTD; 11899; -.
DR   MGI; MGI:1098567; Astn1.
DR   GeneTree; ENSGT00390000003140; -.
DR   HOGENOM; HBG507153; -.
DR   HOVERGEN; HBG050597; -.
DR   InParanoid; Q61137; -.
DR   OrthoDB; EOG4255RX; -.
DR   ArrayExpress; Q61137; -.
DR   Bgee; Q61137; -.
DR   CleanEx; MM_ASTN1; -.
DR   Genevestigator; Q61137; -.
DR   GermOnline; ENSMUSG00000026587; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016477; P:cell migration; IMP:MGI.
DR   GO; GO:0016337; P:cell-cell adhesion; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR020864; MACPF.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00457; MACPF; 1.
DR   SUPFAM; SSF49265; FN_III-like; 1.
DR   PROSITE; PS00022; EGF_1; FALSE_NEG.
DR   PROSITE; PS01186; EGF_2; FALSE_NEG.
DR   PROSITE; PS50026; EGF_3; FALSE_NEG.
DR   PROSITE; PS50853; FN3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Membrane; Phosphoprotein; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     21       Potential.
FT   CHAIN        22   1302       Astrotactin-1.
FT                                /FTId=PRO_0000007482.
FT   TRANSMEM    154    174       Helical; (Potential).
FT   TRANSMEM    389    409       Helical; (Potential).
FT   DOMAIN      459    507       EGF-like 1.
FT   DOMAIN      608    652       EGF-like 2.
FT   DOMAIN      656    708       EGF-like 3.
FT   DOMAIN     1030   1145       Fibronectin type-III 1.
FT   MOD_RES      54     54       Phosphoserine.
FT   MOD_RES    1088   1088       Phosphoserine.
FT   MOD_RES    1277   1277       Phosphoserine (By similarity).
FT   CARBOHYD    115    115       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    226    226       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    382    382       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    453    453       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    729    729       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    742    742       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    804    804       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    984    984       N-linked (GlcNAc...) (Potential).
FT   DISULFID    463    475       By similarity.
FT   DISULFID    471    490       By similarity.
FT   DISULFID    492    506       By similarity.
FT   DISULFID    612    625       By similarity.
FT   DISULFID    619    636       By similarity.
FT   DISULFID    638    651       By similarity.
FT   DISULFID    660    672       By similarity.
FT   DISULFID    668    692       By similarity.
FT   DISULFID    694    707       By similarity.
FT   VAR_SEQ     480    487       Missing (in isoform 2).
FT                                /FTId=VSP_014917.
FT   CONFLICT    216    216       S -> T (in Ref. 2; AAC52516).
FT   CONFLICT    369    369       R -> L (in Ref. 2; AAC52516).
FT   CONFLICT    396    396       I -> L (in Ref. 3; BAC41406).
FT   CONFLICT    421    421       I -> M (in Ref. 1; AAH94666).
FT   CONFLICT    437    437       A -> R (in Ref. 2; AAC52516).
FT   CONFLICT    681    681       E -> D (in Ref. 3; BAC41406).
FT   CONFLICT   1045   1045       N -> T (in Ref. 3; BAC41406).
FT   CONFLICT   1067   1067       I -> Y (in Ref. 2; AAC52516).
FT   CONFLICT   1214   1214       Missing (in Ref. 2; AAC52516).
FT   CONFLICT   1260   1261       GC -> AG (in Ref. 2; AAC52516).
SQ   SEQUENCE   1302 AA;  144928 MW;  D69332152F37E250 CRC64;
     MALAGLCALF ACCWGPAAVL ATAAGDVDPS KELECKLKSI TVSALPFLRE NDLSIMHSPS
     ASEPKLLFSV RNDFPGEMVV VDDLENTELP YFVLEISGNT EDIPLVRWRQ QWLENGTLLF
     HIHHQDGAPS LPGQDPTEEP QHESAEEELR ILHISVMGGM IALLLSILCL VMILYTRRRW
     CKRRRVPQPQ KSASAEAANE IHYIPSVLIG GHGRESLRNA RVQGHNSSGT LSIRETPILD
     GYEYDITDLR HHLQRECMNG GEDFASQVTR TLDSLQGCNE KSGMDLTPGS DNAKLSLMNK
     YKDNIIATSP VDSNHQQATL LSHTSSSQRK RINNKARAGS AFLNPEGDSS TEAENDPQLT
     FYTDPSRSRR RSRVGSPRSP VNKTTLTLIS VTSCVIGLVC SSHVSCPLVV KITLHVPEHL
     IADGSRFILL EGSQLDASDW LNPAQVVLFS QQNSSGPWAM DLCARRLLDP CEHQCDPETG
     RREHRADGEC LCYEGYMKDP VHKHLCIRNE WGTNQGPWPY TIFQRGFDLV LGEQPSDKIF
     RFTYTLGEGM WLPLSKSFVI PPAELAINPS AKCKTDMTVM EDAVEVREEL MTSSSFDSLE
     VLLDSFGPVR DCSKDNGGCS KNFRCISDRK LDSTGCVCPS GLSPMKDSSG CYDRHIGVDC
     SDGFNGGCEQ LCLQQMAPFP EDPTLYNILM FCGCIEDYKL GVDGRSCQLV TETCPEGGDC
     GESREVPMNQ TLFGEMFFGY NNQSKEVATG QVLKGTFRQN NFARGLDQQL PDGLVVASVP
     LENQCLEEIS EPTPDPDFLT GMVNFSEVSG YPVLQHWKVR SVMYHIKLNQ AAISQAFSNA
     LHSLDGATSR ADFVALLDQF GNHYIQEAVY GFEESCSIWY PNKQVQRRLW LEYEDISKGN
     SPSDESEERE RDPKVLTFPE YIASLSDSGT KRMAAGVRME CQSKGRCPSS CPLCHVTSSP
     ETPAEPVLLE VTRASPIYEL VTNNQTQRLL QEATMSSLWC SGTGDVIEDW CRCDSTAFGA
     DGLPTCAPLP QPVLRLSTVH EPSSNLVVLE WEHSEPPIGV QIVDYLIRQE KVTDRMDHSK
     VETETVLSFV DDIISGAKAP CAMPSQVPDK QLTTISLIIR CLEPDTIYMF TLWGVDNTGR
     RSRPSDVIVK TPCPVVDDVK AQEIADKIYN LFNGYTSGKE QQTAYNTLLD LGSPTLHRVL
     YHYNQHYESF GEFTWRCEDE LGPRKAGLIL SQLGDLSSWC NGLLQEPKIS LRRGSLKYLG
     CRYSEIKPYG LDWSELSRDL RKTCEEQTLS VPYNDYGDSK DI
//
ID   SPIN1_MOUSE             Reviewed;         262 AA.
AC   Q61142; Q3TLC3; Q3UT05; Q91VG8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Spindlin-1;
DE   AltName: Full=30000 Mr metaphase complex;
DE   AltName: Full=SSEC P;
GN   Name=Spin1; Synonyms=Spin;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION,
RP   DEVELOPMENTAL STAGE, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6 X DBA/2; TISSUE=Embryo;
RX   MEDLINE=97178984; PubMed=9053325;
RA   Oh B., Hwang S.Y., Solter D., Knowles B.B.;
RT   "Spindlin, a major maternal transcript expressed in the mouse during
RT   the transition from oocyte to embryo.";
RL   Development 124:493-503(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Embryo, Embryonic heart, Embryonic limb, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=NMRI; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in cell-cycle regulation during the
CC       transition from gamete to embryo.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle.
CC       Note=Associates with the meiotic spindle.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q61142-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q61142-2; Sequence=VSP_017942;
CC   -!- TISSUE SPECIFICITY: Oocyte, egg, and very early embryo; not in the
CC       8-, and 16-cell stage of the embryo.
CC   -!- DEVELOPMENTAL STAGE: Gametogenesis. Synthesized from maternal
CC       transcripts but not from the zygote genome.
CC   -!- PTM: Phosphorylated during oocyte meiotic maturation.
CC   -!- PTM: Post-translationally modified during the first mitotic cell
CC       cycle.
CC   -!- SIMILARITY: Belongs to the SPIN/STSY family.
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DR   EMBL; U48972; AAA91233.1; -; mRNA.
DR   EMBL; AK088127; BAC40162.1; -; mRNA.
DR   EMBL; AK134259; BAE22069.1; -; mRNA.
DR   EMBL; AK136251; BAE22897.1; -; mRNA.
DR   EMBL; AK139899; BAE24175.1; -; mRNA.
DR   EMBL; AK162171; BAE36769.1; -; mRNA.
DR   EMBL; AK162195; BAE36784.1; -; mRNA.
DR   EMBL; AK162258; BAE36820.1; -; mRNA.
DR   EMBL; AK163263; BAE37266.1; -; mRNA.
DR   EMBL; AK163293; BAE37280.1; -; mRNA.
DR   EMBL; AK163382; BAE37327.1; -; mRNA.
DR   EMBL; AK166528; BAE38832.1; -; mRNA.
DR   EMBL; AK166580; BAE38869.1; -; mRNA.
DR   EMBL; AK166677; BAE38937.1; -; mRNA.
DR   EMBL; AK168544; BAE40420.1; -; mRNA.
DR   EMBL; BC016517; AAH16517.1; -; mRNA.
DR   IPI; IPI00162994; -.
DR   IPI; IPI00620436; -.
DR   RefSeq; NP_035592.1; NM_011462.2.
DR   RefSeq; NP_666155.1; NM_146043.3.
DR   UniGene; Mm.188432; -.
DR   ProteinModelPortal; Q61142; -.
DR   SMR; Q61142; 50-260.
DR   PhosphoSite; Q61142; -.
DR   REPRODUCTION-2DPAGE; Q61142; -.
DR   PRIDE; Q61142; -.
DR   Ensembl; ENSMUST00000057478; ENSMUSP00000062273; ENSMUSG00000021395.
DR   Ensembl; ENSMUST00000095797; ENSMUSP00000093473; ENSMUSG00000021395.
DR   GeneID; 20729; -.
DR   KEGG; mmu:20729; -.
DR   UCSC; uc007qly.1; mouse.
DR   UCSC; uc007qma.1; mouse.
DR   CTD; 20729; -.
DR   MGI; MGI:109242; Spin1.
DR   eggNOG; roNOG12049; -.
DR   GeneTree; ENSGT00550000074439; -.
DR   HOGENOM; HBG713360; -.
DR   HOVERGEN; HBG000686; -.
DR   InParanoid; Q61142; -.
DR   OMA; HKDERVQ; -.
DR   OrthoDB; EOG4RV2S3; -.
DR   NextBio; 459529; -.
DR   ArrayExpress; Q61142; -.
DR   Bgee; Q61142; -.
DR   CleanEx; MM_SPIN1; -.
DR   Genevestigator; Q61142; -.
DR   GermOnline; ENSMUSG00000021395; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IDA:MGI.
DR   GO; GO:0007143; P:female meiosis; IC:MGI.
DR   GO; GO:0007276; P:gamete generation; IEA:InterPro.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   InterPro; IPR003671; Spin_Ssty.
DR   Pfam; PF02513; Spin-Ssty; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell cycle; Cytoplasm;
KW   Cytoskeleton; Developmental protein; Nucleus; Phosphoprotein.
FT   CHAIN         1    262       Spindlin-1.
FT                                /FTId=PRO_0000181368.
FT   MOD_RES       7      7       N6-acetyllysine (By similarity).
FT   MOD_RES      39     39       Phosphoserine (By similarity).
FT   MOD_RES      91     91       Phosphotyrosine (By similarity).
FT   MOD_RES      98     98       Phosphotyrosine (By similarity).
FT   MOD_RES     124    124       Phosphoserine (By similarity).
FT   MOD_RES     199    199       Phosphoserine (By similarity).
FT   VAR_SEQ       1     34       MKTPFGKTPGQRSRADAGHAGVSANMMKKRTSHK -> MAS
FT                                ASSPASCPR (in isoform 2).
FT                                /FTId=VSP_017942.
SQ   SEQUENCE   262 AA;  29643 MW;  33005229982E110E CRC64;
     MKTPFGKTPG QRSRADAGHA GVSANMMKKR TSHKKHRTSV GPSKPVSQPR RNIVGCRIQH
     GWREGNGPVT QWKGTVLDQV PVNPSLYLIK YDGFDCVYGL ELNKDERVSA LEVLPDRVAT
     SRISDAHLAD TMIGKAVEHM FETEDGSKDE WRGMVLARAP VMNTWFYITY EKDPVLYMYQ
     LLDDYKEGDL RIMPDSNDSP PAEREPGEVV DSLVGKQVEY AKEDGSKRTG MVIHQVEAKP
     SVYFIKFDDD FHIYVYDLVK TS
//
ID   TRPC6_MOUSE             Reviewed;         930 AA.
AC   Q61143; Q9Z2J1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 2.
DT   11-JAN-2011, entry version 99.
DE   RecName: Full=Short transient receptor potential channel 6;
DE            Short=TrpC6;
DE   AltName: Full=Calcium entry channel;
DE   AltName: Full=Transient receptor protein 6;
DE            Short=TRP-6;
GN   Name=Trpc6; Synonyms=Trp6, Trrp6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=98037793; PubMed=9368034; DOI=10.1074/jbc.272.47.29672;
RA   Boulay G., Zhu X., Peyton M., Jiang M., Hurst R., Stefani E.,
RA   Birnbaumer L.;
RT   "Cloning and expression of a novel mammalian homolog of Drosophila
RT   transient receptor potential (Trp) involved in calcium entry secondary
RT   to activation of receptors coupled by the Gq class of G protein.";
RL   J. Biol. Chem. 272:29672-29680(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=DBA/2;
RX   MEDLINE=99158172; PubMed=10050885; DOI=10.1038/sj.onc.1202445;
RA   Buess M., Engler O., Hirsch H.H., Moroni C.;
RT   "Search for oncogenic regulators in an autocrine tumor model using
RT   differential display PCR: identification of novel candidate genes
RT   including the calcium channel mtrp6.";
RL   Oncogene 18:1487-1494(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 631-739.
RC   TISSUE=Brain;
RX   MEDLINE=96234226; PubMed=8646775; DOI=10.1016/S0092-8674(00)81233-7;
RA   Zhu X., Jiang M., Peyton M., Boulay G., Hurst R., Stefani E.,
RA   Birnbaumer L.;
RT   "trp, a novel mammalian gene family essential for agonist-activated
RT   capacitative Ca2+ entry.";
RL   Cell 85:661-671(1996).
CC   -!- FUNCTION: Thought to form a receptor-activated non-selective
CC       calcium permeant cation channel. Probably is operated by a
CC       phosphatidylinositol second messenger system activated by receptor
CC       tyrosine kinases or G-protein coupled receptors. Activated by
CC       diacylglycerol (DAG) in a membrane-delimited fashion,
CC       independently of protein kinase C. Seems not to be activated by
CC       intracellular calcium store depletion.
CC   -!- SUBUNIT: Interacts with MX1 and RNF24 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Probable).
CC   -!- TISSUE SPECIFICITY: Lung and brain.
CC   -!- PTM: N-glycosylated.
CC   -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
CC       STrpC subfamily. TRPC6 sub-subfamily.
CC   -!- SIMILARITY: Contains 3 ANK repeats.
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DR   EMBL; U49069; AAC06146.1; -; mRNA.
DR   EMBL; AF057748; AAC64394.1; -; mRNA.
DR   IPI; IPI00117824; -.
DR   UniGene; Mm.325086; -.
DR   ProteinModelPortal; Q61143; -.
DR   SMR; Q61143; 100-245, 361-388.
DR   STRING; Q61143; -.
DR   PhosphoSite; Q61143; -.
DR   PRIDE; Q61143; -.
DR   Ensembl; ENSMUST00000050433; ENSMUSP00000057965; ENSMUSG00000031997.
DR   UCSC; uc009odl.1; mouse.
DR   MGI; MGI:109523; Trpc6.
DR   HOGENOM; HBG355804; -.
DR   HOVERGEN; HBG068337; -.
DR   InParanoid; Q61143; -.
DR   ArrayExpress; Q61143; -.
DR   Bgee; Q61143; -.
DR   Genevestigator; Q61143; -.
DR   GermOnline; ENSMUSG00000031997; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015279; F:store-operated calcium channel activity; IDA:MGI.
DR   GO; GO:0007204; P:elevation of cytosolic calcium ion concentration; IDA:MGI.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR013555; TRP_2.
DR   InterPro; IPR004729; TRP_channel.
DR   InterPro; IPR005462; TRPC6_channel.
DR   InterPro; IPR002153; TRPC_channel.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF08344; TRP_2; 1.
DR   PRINTS; PR01097; TRNSRECEPTRP.
DR   PRINTS; PR01647; TRPCHANNEL6.
DR   SMART; SM00248; ANK; 3.
DR   SUPFAM; SSF48403; ANK; 1.
DR   TIGRFAMs; TIGR00870; trp; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
PE   2: Evidence at transcript level;
KW   ANK repeat; Calcium; Calcium channel; Calcium transport; Glycoprotein;
KW   Ion transport; Ionic channel; Membrane; Phosphoprotein; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    930       Short transient receptor potential
FT                                channel 6.
FT                                /FTId=PRO_0000215323.
FT   TOPO_DOM      1    437       Cytoplasmic (Potential).
FT   TRANSMEM    438    458       Helical; (Potential).
FT   TOPO_DOM    459    486       Extracellular (Potential).
FT   TRANSMEM    487    507       Helical; (Potential).
FT   TOPO_DOM    508    520       Cytoplasmic (Potential).
FT   TRANSMEM    521    541       Helical; (Potential).
FT   TOPO_DOM    542    591       Extracellular (Potential).
FT   TRANSMEM    592    612       Helical; (Potential).
FT   TOPO_DOM    613    635       Cytoplasmic (Potential).
FT   TRANSMEM    636    656       Helical; (Potential).
FT   TOPO_DOM    657    705       Extracellular (Potential).
FT   TRANSMEM    706    726       Helical; (Potential).
FT   TOPO_DOM    727    930       Cytoplasmic (Potential).
FT   REPEAT      131    160       ANK 1.
FT   REPEAT      162    188       ANK 2.
FT   REPEAT      217    246       ANK 3.
FT   MOD_RES      69     69       Phosphothreonine (By similarity).
FT   MOD_RES     814    814       Phosphoserine (By similarity).
FT   MOD_RES     838    838       Phosphoserine (By similarity).
FT   CARBOHYD    560    560       N-linked (GlcNAc...) (Potential).
FT   CONFLICT      3     56       Missing (in Ref. 2).
FT   CONFLICT    105    105       V -> A (in Ref. 2; AAC64394).
FT   CONFLICT    114    114       W -> R (in Ref. 2; AAC64394).
FT   CONFLICT    134    134       N -> D (in Ref. 2; AAC64394).
FT   CONFLICT    184    184       S -> A (in Ref. 2; AAC64394).
FT   CONFLICT    371    371       D -> Y (in Ref. 2; AAC64394).
FT   CONFLICT    436    437       PR -> RG (in Ref. 2; AAC64394).
FT   CONFLICT    905    905       S -> T (in Ref. 2; AAC64394).
SQ   SEQUENCE   930 AA;  106733 MW;  CF21A426972732F3 CRC64;
     MSQSPRFVTR RGGSLKAAPG AGTRRNESQD YLLMDELGDD GYPQLPLPPY GYYPSFRGNE
     NRLTHRRQTI LREKGRRLAN RGPAYMFNDH STSLSIEEER FLDAVEYGNI PVVWKMLEEC
     HSLNVNCVDY MGQNALQLAV ANEHLEITEL LLKKENLSRV GDALLLAISK GYVRIVEAIL
     NHPSFAEGKR LATSPSQSEL QQDDFYAYDE DGTRFSHDVT PIILAAHCQE YEIVHTLLRK
     GARIERPHDY FCKCTECSQK QKHDSFSHSR SRINAYKGLA SPAYLSLSSE DPVMTALELS
     NELAVLANIE KEFKNDYRKL SMQCKDFVVG LLDLCRNTEE VEAILNGDAE TRQPGDFGRP
     NLSRLKLAIK DEVKKFVAHP NCQQQLLSIW YENLSGLRQQ TMAVKFLVVL AVAIGLPFLA
     LIYWCAPCSK MGKILPRPFM KFVAHAASFT IFLGLLVMNA ADRFEGTKLL PNETSTDNAR
     QLFRMKTSCF SWMEMLIISW VIGMIWAECK EIWTQGPKEY LFELWNMLDF GMLAIFAASF
     IARFMAFWHA SKAQSIIDAN DTLKDLTKVT LGDNVKYYNL ARIKWDPTDP QIISEGLYAI
     AVVLSFSRIA YILPANESFG PLQISLGRTV KDIFKFMVIF IMVFVAFMIG MFNLYSYYIG
     AKQNEAFTTV EESFKTLFWA IFGLSEVKSV VINYNHKFIE NIGYVLYGVY NVTMVIVLLN
     MLIAMINSSF QEIEDDADVE WKFARAKLWF SYFEEGRTLP VPFNLVPSPK SLLYLLLKFK
     KWMCELIQGQ KQGFQEDAEM NKRNEEKKFG ISGSHEDLSK FSLDKNQLAH NKQSSTRSSE
     DYHLNSFSNP PRQYQKIMKR LIKRYVLQAQ IDKESDEVNE GELKEIKQDI SSLRYELLEE
     KSQNSEDLAE LIRKLGERLS LEPKLEESRR
//
ID   PSN2_MOUSE              Reviewed;         448 AA.
AC   Q61144; O54977; P97934; P97935; Q91VS3; Q9D616;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2003, sequence version 3.
DT   08-MAR-2011, entry version 102.
DE   RecName: Full=Presenilin-2;
DE            Short=PS-2;
DE            EC=3.4.23.-;
DE   Contains:
DE     RecName: Full=Presenilin-2 NTF subunit;
DE   Contains:
DE     RecName: Full=Presenilin-2 CTF subunit;
GN   Name=Psen2; Synonyms=Ad4h, Alg3, Ps-2, Psnl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RX   MEDLINE=97094860; PubMed=8940094; DOI=10.1074/jbc.271.49.31025;
RA   Vito P., Wolozin B., Ganjei J.K., Iwasaki K., Lacana E., D'Adamio L.;
RT   "Requirement of the familial Alzheimer's disease gene PS2 for
RT   apoptosis. Opposing effect of ALG-3.";
RL   J. Biol. Chem. 271:31025-31028(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=NIH Swiss;
RA   Sahara N., Mori H., Shirasawa T.;
RT   "Molecular cloning of mouse presenilin 2 gene.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 340-448 (ISOFORM 1).
RC   TISSUE=Liver;
RX   MEDLINE=96152375; PubMed=8560270; DOI=10.1126/science.271.5248.521;
RA   Vito P., Lacana E., D'Adamio L.;
RT   "Interfering with apoptosis: Ca(2+)-binding protein ALG-2 and
RT   Alzheimer's disease gene ALG-3.";
RL   Science 271:521-525(1996).
RN   [6]
RP   INTERACTION WITH DOCK3.
RX   MEDLINE=22100008; PubMed=12093789; DOI=10.1083/jcb.200110151;
RA   Chen Q., Kimura H., Schubert D.;
RT   "A novel mechanism for the regulation of amyloid precursor protein
RT   metabolism.";
RL   J. Cell Biol. 158:79-89(2002).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Probable catalytic subunit of the gamma-secretase
CC       complex, an endoprotease complex that catalyzes the intramembrane
CC       cleavage of integral membrane proteins such as Notch receptors and
CC       APP (beta-amyloid precursor protein). Requires the other members
CC       of the gamma-secretase complex to have a protease activity. May
CC       play a role in intracellular signaling and gene expression or in
CC       linking chromatin to the nuclear membrane. May function in the
CC       cytoplasmic partitioning of proteins (By similarity).
CC   -!- SUBUNIT: Homodimer. Component of the gamma-secretase complex, a
CC       complex composed of a presenilin homodimer (PSEN1 or PSEN2),
CC       nicastrin (NCSTN), APH1 (APH1A or APH1B) and PEN2. Such minimal
CC       complex is sufficient for secretase activity, although other
CC       components may exist. Interacts with DOCK3. Interacts with
CC       HERPUD1, FLNA, FLNB and PARL (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity). Golgi apparatus membrane; Multi-
CC       pass membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q61144-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q61144-2; Sequence=VSP_008383, VSP_008384;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in
CC       the liver.
CC   -!- DOMAIN: The PAL motif is required for normal active site
CC       conformation (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase A22A family.
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DR   EMBL; U57324; AAC52937.1; -; mRNA.
DR   EMBL; U57325; AAC53311.1; -; mRNA.
DR   EMBL; AF038935; AAB92660.1; -; mRNA.
DR   EMBL; AK014706; BAB29514.1; -; mRNA.
DR   EMBL; BC010403; AAH10403.1; -; mRNA.
DR   EMBL; U49111; AAC52935.1; -; mRNA.
DR   IPI; IPI00357545; -.
DR   IPI; IPI00357546; -.
DR   RefSeq; NP_001122077.1; NM_001128605.1.
DR   RefSeq; NP_035313.2; NM_011183.2.
DR   UniGene; Mm.330850; -.
DR   STRING; Q61144; -.
DR   MEROPS; A22.002; -.
DR   PhosphoSite; Q61144; -.
DR   PRIDE; Q61144; -.
DR   Ensembl; ENSMUST00000010753; ENSMUSP00000010753; ENSMUSG00000010609.
DR   Ensembl; ENSMUST00000111105; ENSMUSP00000106734; ENSMUSG00000010609.
DR   Ensembl; ENSMUST00000111106; ENSMUSP00000106735; ENSMUSG00000010609.
DR   Ensembl; ENSMUST00000111108; ENSMUSP00000106737; ENSMUSG00000010609.
DR   GeneID; 19165; -.
DR   KEGG; mmu:19165; -.
DR   UCSC; uc007dwe.1; mouse.
DR   CTD; 19165; -.
DR   MGI; MGI:109284; Psen2.
DR   eggNOG; roNOG11148; -.
DR   GeneTree; ENSGT00390000016593; -.
DR   HOGENOM; HBG559840; -.
DR   HOVERGEN; HBG011375; -.
DR   InParanoid; Q61144; -.
DR   OrthoDB; EOG4RJG1V; -.
DR   ArrayExpress; Q61144; -.
DR   Bgee; Q61144; -.
DR   CleanEx; MM_PSEN2; -.
DR   Genevestigator; Q61144; -.
DR   GermOnline; ENSMUSG00000010609; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral to plasma membrane; ISS:HGNC.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0030018; C:Z disc; IDA:MGI.
DR   GO; GO:0004175; F:endopeptidase activity; IMP:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0042640; P:anagen; IGI:MGI.
DR   GO; GO:0006915; P:apoptosis; IDA:MGI.
DR   GO; GO:0050435; P:beta-amyloid metabolic process; IDA:MGI.
DR   GO; GO:0048854; P:brain morphogenesis; IGI:MGI.
DR   GO; GO:0006816; P:calcium ion transport; IPI:MGI.
DR   GO; GO:0060048; P:cardiac muscle contraction; IMP:MGI.
DR   GO; GO:0001708; P:cell fate specification; IGI:MGI.
DR   GO; GO:0044267; P:cellular protein metabolic process; IGI:MGI.
DR   GO; GO:0021904; P:dorsal/ventral neural tube patterning; IGI:MGI.
DR   GO; GO:0030326; P:embryonic limb morphogenesis; IGI:MGI.
DR   GO; GO:0030900; P:forebrain development; IGI:MGI.
DR   GO; GO:0002244; P:hemopoietic progenitor cell differentiation; IGI:MGI.
DR   GO; GO:0040011; P:locomotion; IGI:MGI.
DR   GO; GO:0048286; P:lung alveolus development; IMP:MGI.
DR   GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISS:HGNC.
DR   GO; GO:0007613; P:memory; IGI:MGI.
DR   GO; GO:0002573; P:myeloid leukocyte differentiation; IGI:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptosis; IDA:MGI.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IGI:MGI.
DR   GO; GO:0007219; P:Notch signaling pathway; IGI:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptosis; IGI:MGI.
DR   GO; GO:0043085; P:positive regulation of catalytic activity; ISS:HGNC.
DR   GO; GO:0050820; P:positive regulation of coagulation; IMP:MGI.
DR   GO; GO:0051605; P:protein maturation by peptide bond cleavage; IGI:MGI.
DR   GO; GO:0015031; P:protein transport; IGI:MGI.
DR   GO; GO:0007176; P:regulation of epidermal growth factor receptor activity; IGI:MGI.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; IGI:MGI.
DR   GO; GO:0001756; P:somitogenesis; IGI:MGI.
DR   GO; GO:0002286; P:T cell activation involved in immune response; IGI:MGI.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IGI:MGI.
DR   GO; GO:0048538; P:thymus development; IGI:MGI.
DR   InterPro; IPR001493; Pept_A22A_PS2.
DR   InterPro; IPR006639; Peptidase_A22.
DR   InterPro; IPR001108; Peptidase_A22A.
DR   PANTHER; PTHR10202; Peptidase_A22A; 1.
DR   Pfam; PF01080; Presenilin; 1.
DR   PRINTS; PR01072; PRESENILIN.
DR   PRINTS; PR01074; PRESENILIN2.
DR   SMART; SM00730; PSN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endoplasmic reticulum; Golgi apparatus;
KW   Hydrolase; Membrane; Notch signaling pathway; Phosphoprotein;
KW   Protease; Transmembrane; Transmembrane helix.
FT   CHAIN         1    297       Presenilin-2 NTF subunit (By similarity).
FT                                /FTId=PRO_0000025607.
FT   CHAIN       298    448       Presenilin-2 CTF subunit.
FT                                /FTId=PRO_0000025608.
FT   TOPO_DOM      1     87       Cytoplasmic (Potential).
FT   TRANSMEM     88    108       Helical; (Potential).
FT   TOPO_DOM    109    138       Lumenal (Potential).
FT   TRANSMEM    139    159       Helical; (Potential).
FT   TOPO_DOM    160    166       Cytoplasmic (Potential).
FT   TRANSMEM    167    187       Helical; (Potential).
FT   TOPO_DOM    188    200       Lumenal (Potential).
FT   TRANSMEM    201    221       Helical; (Potential).
FT   TOPO_DOM    222    223       Cytoplasmic (Potential).
FT   TRANSMEM    224    244       Helical; (Potential).
FT   TOPO_DOM    245    249       Lumenal (Potential).
FT   TRANSMEM    250    270       Helical; (Potential).
FT   TOPO_DOM    271    388       Cytoplasmic (Potential).
FT   TRANSMEM    389    409       Helical; (Potential).
FT   TRANSMEM    414    434       Helical; (Potential).
FT   MOTIF       414    416       PAL.
FT   ACT_SITE    263    263       By similarity.
FT   ACT_SITE    366    366       By similarity.
FT   MOD_RES      22     22       Phosphoserine (By similarity).
FT   MOD_RES      25     25       Phosphoserine (By similarity).
FT   MOD_RES      30     30       Phosphoserine.
FT   MOD_RES      52     52       Phosphoserine.
FT   VAR_SEQ     296    332       SAMVWTVGMAKLDPSSQGALQLPYDPEMEEDSYDSFG ->
FT                                CEWSHASARHWGVSRWPFVEAWKWAVVLISDRLYILS (in
FT                                isoform 2).
FT                                /FTId=VSP_008383.
FT   VAR_SEQ     333    448       Missing (in isoform 2).
FT                                /FTId=VSP_008384.
FT   CONFLICT     40     40       D -> G (in Ref. 3; BAB29514).
FT   CONFLICT     86     87       KR -> ND (in Ref. 3; BAB29514).
FT   CONFLICT     87     87       R -> H (in Ref. 2 and 4).
FT   CONFLICT    226    226       V -> A (in Ref. 1; AAC52937).
FT   CONFLICT    324    324       Missing (in Ref. 2; AAB92660).
SQ   SEQUENCE   448 AA;  49983 MW;  54787212DCBB2C78 CRC64;
     MLAFMASDSE EEVCDERTSL MSAESPTSRS CQEGRPGPED GESTAQWRTQ ESEEDCEEDP
     DRYACSGAPG RPSGLEEELT LKYGAKRVIM LFVPVTLCMI VVVATIKSVR FYTEKNGQLI
     YTPFTEDTPS VGQRLLNSVL NTLIMISVIV VMTIFLVVLY KYRCYKFIHG WLIMSSLMLL
     FLFTYIYLGE VLKTYNVAMD YPTLFLAVWN FGAVGMVCIH WKGPLVLQQA YLIVISALMA
     LVFIKYLPEW SAWVILGAIS VYDLVAVLCP KGPLRMLVET AQERNEPIFP ALIYSSAMVW
     TVGMAKLDPS SQGALQLPYD PEMEEDSYDS FGEPSYPEAF EAPLPGYPGE ELEEEEERGV
     KLGLGDFIFY SVLVGKAAAT GNGDWNTTLA CFIAILIGLC LTLLLLAVFK KALPALPISI
     TFGLIFYFST DNLVRPFMDT LASHQLYI
//
ID   2A5E_MOUSE              Reviewed;         467 AA.
AC   Q61151; Q3V1I5; Q571M6; Q8C2M2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 3.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform;
DE   AltName: Full=PP2A B subunit isoform B'-epsilon;
DE   AltName: Full=PP2A B subunit isoform B56-epsilon;
DE   AltName: Full=PP2A B subunit isoform PR61-epsilon;
DE   AltName: Full=PP2A B subunit isoform R5-epsilon;
GN   Name=Ppp2r5e; Synonyms=Kiaa4006;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Skin, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-436.
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 51-437.
RC   TISSUE=Embryonic fibroblast;
RX   MEDLINE=97042488; PubMed=8887688;
RA   Okamoto K., Kamibayashi C., Serrano M., Prives C., Mumby M.C.,
RA   Beach D.;
RT   "p53-dependent association between cyclin G and the B' subunit of
RT   protein phosphatase 2A.";
RL   Mol. Cell. Biol. 16:6593-6602(1996).
CC   -!- FUNCTION: The B regulatory subunit might modulate substrate
CC       selectivity and catalytic activity, and also might direct the
CC       localization of the catalytic enzyme to a particular subcellular
CC       compartment. Interacts with cyclin G in vitro.
CC   -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme,
CC       composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa
CC       constant regulatory subunit (PR65 or subunit A), that associates
CC       with a variety of regulatory subunits. Proteins that associate
CC       with the core dimer include three families of regulatory subunits
CC       B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56
CC       families), the 48 kDa variable regulatory subunit, viral proteins,
CC       and cell signaling molecules. Interacts with SGOL1. Found in a
CC       complex with at least ARL2, PPP2CB; PPP2R1A, PPP2R2A, PPP2R5E and
CC       TBCD (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B56
CC       family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB37234.1; Type=Frameshift; Positions=162, 180, 185;
CC       Sequence=BAD90335.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; AK088366; BAC40306.1; -; mRNA.
DR   EMBL; AK132432; BAE21166.1; -; mRNA.
DR   EMBL; BC085149; AAH85149.1; -; mRNA.
DR   EMBL; AK220163; BAD90335.1; ALT_INIT; mRNA.
DR   EMBL; U49728; AAB37234.1; ALT_FRAME; mRNA.
DR   IPI; IPI00224697; -.
DR   RefSeq; NP_036154.1; NM_012024.2.
DR   UniGene; Mm.259626; -.
DR   UniGene; Mm.440646; -.
DR   ProteinModelPortal; Q61151; -.
DR   SMR; Q61151; 51-423.
DR   PhosphoSite; Q61151; -.
DR   PRIDE; Q61151; -.
DR   Ensembl; ENSMUST00000021447; ENSMUSP00000021447; ENSMUSG00000021051.
DR   GeneID; 26932; -.
DR   KEGG; mmu:26932; -.
DR   UCSC; uc007nxe.1; mouse.
DR   CTD; 26932; -.
DR   MGI; MGI:1349473; Ppp2r5e.
DR   GeneTree; ENSGT00550000074525; -.
DR   HOGENOM; HBG602178; -.
DR   HOVERGEN; HBG000009; -.
DR   InParanoid; Q61151; -.
DR   OMA; TEQAYPE; -.
DR   PhylomeDB; Q61151; -.
DR   NextBio; 304835; -.
DR   ArrayExpress; Q61151; -.
DR   Bgee; Q61151; -.
DR   Genevestigator; Q61151; -.
DR   GermOnline; ENSMUSG00000021051; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; TAS:MGI.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:InterPro.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0008601; F:protein phosphatase type 2A regulator activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002554; PP2A_B56.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   PANTHER; PTHR10257; B56; 1.
DR   Pfam; PF01603; B56; 1.
DR   PIRSF; PIRSF028043; PP2A_B56; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Phosphoprotein.
FT   CHAIN         1    467       Serine/threonine-protein phosphatase 2A
FT                                56 kDa regulatory subunit epsilon
FT                                isoform.
FT                                /FTId=PRO_0000071455.
FT   MOD_RES       7      7       Phosphothreonine (By similarity).
FT   CONFLICT     74     74       F -> C (in Ref. 4; AAB37234).
FT   CONFLICT    162    162       L -> W (in Ref. 4; AAB37234).
FT   CONFLICT    388    388       F -> S (in Ref. 4; AAB37234).
FT   CONFLICT    409    409       N -> T (in Ref. 4; AAB37234).
SQ   SEQUENCE   467 AA;  54713 MW;  77DA129F9A4EC6AC CRC64;
     MSSAPTTPPS VDKVDGFSRK SVRKARQKRS QSSSQFRSQG KPIELTPLPL LKDVPTSEQP
     ELFLKKLQQC CVIFDFMDTL SDLKMKEYKR STLNELVDYI TISRGCLTEQ TYPEVVRMVS
     CNIFRTLPPS DSNEFDPEED EPTLEASWPH LQLVYEFFIR FLESQEFQPS IAKKYIDQKF
     VLQLLELFDS EDPRERDYLK TVLHRIYGKF LGLRAFIRKQ INNIFLRFVY ETEHFNGVAE
     LLEILGSIIN GFALPLKAEH KQFLVKVLIP LHTVRSLSLF HAQLAYCIVQ FLEKDPSLTE
     PVIRGLMKFW PKTCSQKEVM FLGELEEILD VIEPSQFVKI QEPLFKQIAK CVSSPHFQVA
     ERALYYWNNE YIMSLIEENS NVILPIMFSS LYRISKEHWN PAIVALVYNV LKAFMEMNST
     MFDELTATYK SDRQREKKKE KEREELWKKL EDLELKRGLR RDGIIPT
//
ID   M4K2_MOUSE              Reviewed;         821 AA.
AC   Q61161;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Mitogen-activated protein kinase kinase kinase kinase 2;
DE            EC=2.7.11.1;
DE   AltName: Full=Germinal center kinase;
DE            Short=GCK;
DE   AltName: Full=MAPK/ERK kinase kinase kinase 2;
DE            Short=MEK kinase kinase 2;
DE            Short=MEKKK 2;
DE   AltName: Full=Rab8-interacting protein;
GN   Name=Map4k2; Synonyms=Rab8ip;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RAB8, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=BALB/c;
RX   MEDLINE=96209873; PubMed=8643544; DOI=10.1073/pnas.93.10.5151;
RA   Ren M., Zeng J., De Lemos-Chiarandini C., Rosenfeld M., Adesnik M.,
RA   Sabatini D.D.;
RT   "In its active form, the GTP-binding protein rab8 interacts with a
RT   stress-activated protein kinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:5151-5155(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 42-821.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Enhances MAP3K1 oligomerization, which may relieve
CC       amino-terminal mediated MAP3K1 autoinhibition and lead to
CC       activation following autophosphorylation. May play a role in the
CC       regulation of vesicle targeting or fusion.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium.
CC   -!- SUBUNIT: Interacts with TRAF2, MAP3K1 and RAB8A.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Basolateral cell membrane;
CC       Peripheral membrane protein. Golgi apparatus membrane; Peripheral
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC   -!- SIMILARITY: Contains 1 CNH domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; U50595; AAC52571.1; -; mRNA.
DR   EMBL; AK051036; BAC34507.1; -; mRNA.
DR   IPI; IPI00117889; -.
DR   RefSeq; NP_033032.1; NM_009006.2.
DR   UniGene; Mm.25860; -.
DR   ProteinModelPortal; Q61161; -.
DR   SMR; Q61161; 9-278.
DR   STRING; Q61161; -.
DR   PhosphoSite; Q61161; -.
DR   PRIDE; Q61161; -.
DR   Ensembl; ENSMUST00000025897; ENSMUSP00000025897; ENSMUSG00000024948.
DR   GeneID; 26412; -.
DR   KEGG; mmu:26412; -.
DR   UCSC; uc008gie.1; mouse.
DR   CTD; 26412; -.
DR   MGI; MGI:1346883; Map4k2.
DR   GeneTree; ENSGT00600000084124; -.
DR   HOGENOM; HBG315791; -.
DR   HOVERGEN; HBG036702; -.
DR   InParanoid; Q61161; -.
DR   OMA; KFGAPRR; -.
DR   OrthoDB; EOG4V6ZG4; -.
DR   PhylomeDB; Q61161; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 304405; -.
DR   ArrayExpress; Q61161; -.
DR   Bgee; Q61161; -.
DR   Genevestigator; Q61161; -.
DR   GermOnline; ENSMUSG00000024948; Mus musculus.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005083; F:small GTPase regulator activity; IEA:InterPro.
DR   GO; GO:0007243; P:intracellular protein kinase cascade; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0006903; P:vesicle targeting; IDA:UniProtKB.
DR   InterPro; IPR001180; Citron.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR021160; MAPKKKK.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF038172; MAPKKKK; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Cytoplasm; Golgi apparatus; Kinase;
KW   Membrane; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    821       Mitogen-activated protein kinase kinase
FT                                kinase kinase 2.
FT                                /FTId=PRO_0000086276.
FT   DOMAIN       16    273       Protein kinase.
FT   DOMAIN      483    794       CNH.
FT   NP_BIND      22     30       ATP (By similarity).
FT   ACT_SITE    136    136       Proton acceptor (By similarity).
FT   BINDING      45     45       ATP (By similarity).
FT   MOD_RES       8      8       Phosphoserine (By similarity).
FT   MOD_RES     298    298       Phosphoserine (By similarity).
FT   MOD_RES     326    326       Phosphothreonine (By similarity).
FT   MOD_RES     328    328       Phosphoserine (By similarity).
FT   MOD_RES     394    394       Phosphoserine (By similarity).
FT   CONFLICT    223    223       L -> M (in Ref. 2; BAC34507).
SQ   SEQUENCE   821 AA;  91265 MW;  2CCF750E45A53B05 CRC64;
     MALLRDVSLQ DPRDRFELLQ RVGAGTYGDV YKARDTVTSE LAAVKIVKLD PGDDISSLQQ
     EITILRECRH PNVVAYIGSY LRNDRLWICM EFCGGGSLQE IYHATGPLEE RQIAYVCREA
     LKGLHHLHSQ GKIHRDIKGA NLLLTLQGDV KLADFGVSGE LTASVAKRRS FIGTPYWMAP
     EVAAVERKGG YNELCDVWAL GITAIELGEL QPPLFHLHPM RALMLMSKSS FQPPKLRDKT
     RWTQNFHHFL KLALTKNPKK RPTAERLLQH PFTTQHLPPA LLTQLLDKAS DPHLGTLSPE
     DSELETHDMF PDTIHSRSHH GPAERTPSEI QFHQVKFGAP RRKETDPLNE PWEEEWTLLG
     KEELSGSLLQ SVQEALEERS LTIRPALELQ ELDSPDDAIG TIKRAPFLGL PHTESTSGDN
     AQSCSPGTLS APPAGPGSPA LLPTAWATLK QQEDRERSSC HGLPPTPKVH MGACFSKVFN
     GCPLQIHAAV TWVHPVTRDQ FLVVGAEEGI YTLNLHELHE DTMEKLISQR CSWLYCVNNV
     LLSLSGKSTH IWAHDLPGLF EQRRLQHQAP LSIPTNRITQ RIIPRRFALS TKIPDTKGCL
     QCRVVRNPYT GSTFLLAALP ASLLLLQWYE PLQKFLLLKN FSSPLPSPAG MLEPLVLDGK
     ELPQVCVGAE GPEGPGCRVL FHVLPLEAGL TPDILIPPEG IPGSAQQVIQ VDRDTVLVSF
     ERCVRIVNLQ GEPTAALAPE LTFDFTIETV VCLQDSVLAF WSHGMQGRSL DTNEVTQEIT
     DETRIFRVLG AHRDIILESI PTDNPGAHSN LYILTGHQSS Y
//
ID   CTCF_MOUSE              Reviewed;         736 AA.
AC   Q61164;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 2.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Transcriptional repressor CTCF;
DE   AltName: Full=11-zinc finger protein;
DE   AltName: Full=CCCTC-binding factor;
DE   AltName: Full=CTCFL paralog;
GN   Name=Ctcf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=BDF1;
RX   MEDLINE=96220465; PubMed=8649389;
RA   Filippova G.N., Fagerlie S., Klenova E.M., Myers C., Dehner Y.,
RA   Goodwin G., Neiman P.E., Collins S.J., Lobanenkov V.V.;
RT   "An exceptionally conserved transcriptional repressor, CTCF, employs
RT   different combinations of zinc fingers to bind diverged promoter
RT   sequences of avian and mammalian c-myc oncogenes.";
RL   Mol. Cell. Biol. 16:2802-2813(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain, Mammary gland, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-201.
RC   STRAIN=C57BL/6J; TISSUE=Extraembryonic tissue, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   FUNCTION.
RX   PubMed=11743158; DOI=10.1126/science.1065982;
RA   Chao W., Huynh K.D., Spencer R.J., Davidow L.S., Lee J.T.;
RT   "CTCF, a candidate trans-acting factor for X-inactivation choice.";
RL   Science 295:345-347(2002).
RN   [5]
RP   FUNCTION.
RX   PubMed=15669143; DOI=10.1016/j.devcel.2004.10.018;
RA   Filippova G.N., Cheng M.K., Moore J.M., Truong J.-P., Hu Y.J.,
RA   Nguyen D.K., Tsuchiya K.D., Disteche C.M.;
RT   "Boundaries between chromosomal domains of X inactivation and escape
RT   bind CTCF and lack CpG methylation during early development.";
RL   Dev. Cell 8:31-42(2005).
RN   [6]
RP   FUNCTION.
RX   PubMed=16951251; DOI=10.1101/gad.399506;
RA   Splinter E., Heath H., Kooren J., Palstra R.-J., Klous P.,
RA   Grosveld F., Galjart N., de Laat W.;
RT   "CTCF mediates long-range chromatin looping and local histone
RT   modification in the beta-globin locus.";
RL   Genes Dev. 20:2349-2354(2006).
RN   [7]
RP   INTERACTION WITH CHD8.
RX   PubMed=16949368; DOI=10.1016/j.molcel.2006.08.008;
RA   Ishihara K., Oshimura M., Nakao M.;
RT   "CTCF-dependent chromatin insulator is linked to epigenetic
RT   remodeling.";
RL   Mol. Cell 23:733-742(2006).
RN   [8]
RP   FUNCTION.
RX   PubMed=16614224; DOI=10.1126/science.1123191;
RA   Ling J.Q., Li T., Hu J.F., Vu T.H., Chen H.L., Qiu X.W., Cherry A.M.,
RA   Hoffman A.R.;
RT   "CTCF mediates interchromosomal colocalization between Igf2/H19 and
RT   Wsb1/Nf1.";
RL   Science 312:269-272(2006).
RN   [9]
RP   FUNCTION.
RX   PubMed=17329968;
RA   Bergstroem R., Whitehead J., Kurukuti S., Ohlsson R.;
RT   "CTCF regulates asynchronous replication of the imprinted H19/Igf2
RT   domain.";
RL   Cell Cycle 6:450-454(2007).
RN   [10]
RP   FUNCTION.
RX   PubMed=17952071; DOI=10.1038/ng.2007.5;
RA   Xu N., Donohoe M.E., Silva S.S., Lee J.T.;
RT   "Evidence that homologous X-chromosome pairing requires transcription
RT   and Ctcf protein.";
RL   Nat. Genet. 39:1390-1396(2007).
RN   [11]
RP   FUNCTION.
RX   PubMed=18614575; DOI=10.1242/dev.024539;
RA   Wan L.-B., Pan H., Hannenhalli S., Cheng Y., Ma J., Fedoriw A.,
RA   Lobanenkov V., Latham K.E., Schultz R.M., Bartolomei M.S.;
RT   "Maternal depletion of CTCF reveals multiple functions during oocyte
RT   and preimplantation embryo development.";
RL   Development 135:2729-2738(2008).
RN   [12]
RP   SUMOYLATION AT LYS-74 AND LYS-698, AND MUTAGENESIS OF LYS-74 AND
RP   LYS-698.
RX   PubMed=19029252; DOI=10.1128/MCB.00825-08;
RA   MacPherson M.J., Beatty L.G., Zhou W., Du M., Sadowski P.D.;
RT   "The CTCF insulator protein is posttranslationally modified by SUMO.";
RL   Mol. Cell. Biol. 29:714-725(2009).
CC   -!- FUNCTION: Chromatin binding factor that binds to DNA sequence
CC       specific sites. Involved in transcriptional regulation by binding
CC       to chromatin insulators and preventing interaction between
CC       promoter and nearby enhancers and silencers. Acts as
CC       transcriptional repressor binding to promoters of vertebrate MYC
CC       gene and BAG1 gene. Also binds to the PLK and PIM1 promoters. Acts
CC       as a transcriptional activator of APP. Regulates APOA1/C3/A4/A5
CC       gene cluster and controls MHC class II gene expression. Plays an
CC       essential role in oocyte and preimplantation embryo development by
CC       activating or repressing transcription. Seems to act as tumor
CC       suppressor. Plays a critical role in the epigenetic regulation.
CC       Participates to the allele-specific gene expression at the
CC       imprinted IGF2/H19 gene locus. On the maternal allele, binding
CC       within the H19 imprinting control region (ICR) mediates maternally
CC       inherited higher-order chromatin conformation to restrict enhancer
CC       access to IGF2. Plays a critical role in gene silencing over
CC       considerable distances in the genome. Preferentially interacts
CC       with unmethylated DNA, preventing spreading of CpG methylation and
CC       maintaining methylation-free zones. Inversely, binding to target
CC       sites is prevented by CpG methylation. Plays a important role in
CC       chromatin remodeling. Can dimerize when it is bound to different
CC       DNA sequences, mediating long-range chromatin looping (By
CC       similarity). Mediates interchromosomal association between
CC       IGF2/H19 and WSB1/NF1 and may direct distant DNA segments to a
CC       common transcription factory. Causes local loss of histone
CC       acetylation and gain of histone methylation in the beta-globin
CC       locus, without affecting transcription. When bound to chromatin,
CC       it provides an anchor point for nucleosomes positioning. Seems to
CC       be essential for homologous X-chromosome pairing. May participate
CC       with Tsix in establishing a regulatable epigenetic switch for X
CC       chromosome inactivation. May play a role in preventing the
CC       propagation of stable methylation at the escape genes from X-
CC       inactivation. Involved in sister chromatid cohesion. Associates
CC       with both centromeres and chromosomal arms during metaphase and
CC       required for cohesin localization to CTCF sites. Regulates
CC       asynchronous replication of IGF2/H19.
CC   -!- SUBUNIT: Interacts with CHD8.
CC   -!- INTERACTION:
CC       Q09XV5:Chd8; NbExp=3; IntAct=EBI-932785, EBI-1169080;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm (Probable). Chromosome
CC       (By similarity). Chromosome, centromere (By similarity). Note=May
CC       translocate to the nucleolus upon cell differentiation. Associates
CC       with both centromeres and chromosomal arms during metaphase.
CC       Associates with the H19 ICR in mitotic chromosomes. May be
CC       preferentially excluded from heterochromatin during interphase (By
CC       similarity).
CC   -!- PTM: Sumoylated on Lys-74 and Lys-698; sumoylation of CTCF
CC       contributes to the repressive function of CTCF on the MYC P2
CC       promoter.
CC   -!- SIMILARITY: Belongs to the CTCF zinc-finger protein family.
CC   -!- SIMILARITY: Contains 11 C2H2-type zinc fingers.
CC   -----------------------------------------------------------------------
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DR   EMBL; U51037; AAC52928.1; -; mRNA.
DR   EMBL; BC037456; AAH37456.1; -; mRNA.
DR   EMBL; BC046398; AAH46398.1; -; mRNA.
DR   EMBL; BC049131; AAH49131.1; -; mRNA.
DR   EMBL; BC058240; AAH58240.1; -; mRNA.
DR   EMBL; AK076192; BAC36245.1; -; mRNA.
DR   IPI; IPI00320741; -.
DR   RefSeq; NP_851839.1; NM_181322.3.
DR   UniGene; Mm.269474; -.
DR   ProteinModelPortal; Q61164; -.
DR   SMR; Q61164; 262-602.
DR   IntAct; Q61164; 17.
DR   STRING; Q61164; -.
DR   PRIDE; Q61164; -.
DR   Ensembl; ENSMUST00000005841; ENSMUSP00000005841; ENSMUSG00000005698.
DR   GeneID; 13018; -.
DR   KEGG; mmu:13018; -.
DR   UCSC; uc009ndm.1; mouse.
DR   CTD; 13018; -.
DR   MGI; MGI:109447; Ctcf.
DR   GeneTree; ENSGT00530000063079; -.
DR   HOGENOM; HBG715698; -.
DR   HOVERGEN; HBG000350; -.
DR   InParanoid; Q61164; -.
DR   OMA; NQPKQTQ; -.
DR   OrthoDB; EOG4QJRN4; -.
DR   PhylomeDB; Q61164; -.
DR   NextBio; 282878; -.
DR   ArrayExpress; Q61164; -.
DR   Bgee; Q61164; -.
DR   CleanEx; MM_CTCF; -.
DR   Genevestigator; Q61164; -.
DR   GermOnline; ENSMUSG00000005698; Mus musculus.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR   GO; GO:0009048; P:dosage compensation, by inactivation of X chromosome; TAS:MGI.
DR   GO; GO:0010216; P:maintenance of DNA methylation; IMP:MGI.
DR   GO; GO:0006349; P:regulation of gene expression by genetic imprinting; IDA:MGI.
DR   GO; GO:0035065; P:regulation of histone acetylation; IMP:UniProtKB.
DR   GO; GO:0031060; P:regulation of histone methylation; IMP:UniProtKB.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 10.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 11.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE   1: Evidence at protein level;
KW   Activator; Centromere; Chromatin regulator; Chromosome;
KW   Chromosome partition; DNA-binding; Isopeptide bond; Metal-binding;
KW   Nucleus; Phosphoprotein; Repeat; Repressor; Transcription;
KW   Transcription regulation; Tumor suppressor; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    736       Transcriptional repressor CTCF.
FT                                /FTId=PRO_0000047229.
FT   ZN_FING     266    288       C2H2-type 1.
FT   ZN_FING     294    316       C2H2-type 2.
FT   ZN_FING     322    345       C2H2-type 3.
FT   ZN_FING     351    373       C2H2-type 4.
FT   ZN_FING     379    401       C2H2-type 5.
FT   ZN_FING     407    430       C2H2-type 6.
FT   ZN_FING     437    460       C2H2-type 7.
FT   ZN_FING     467    489       C2H2-type 8.
FT   ZN_FING     495    517       C2H2-type 9.
FT   ZN_FING     523    546       C2H2-type 10.
FT   ZN_FING     555    577       C2H2-type 11; atypical.
FT   COMPBIAS    635    676       Pro-rich.
FT   MOD_RES     374    374       Phosphothreonine (By similarity).
FT   MOD_RES     402    402       Phosphoserine (By similarity).
FT   MOD_RES     609    609       Phosphoserine (By similarity).
FT   MOD_RES     610    610       Phosphoserine (By similarity).
FT   MOD_RES     612    612       Phosphoserine (By similarity).
FT   CROSSLNK     74     74       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT   CROSSLNK    698    698       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT   MUTAGEN      74     74       K->R: No sumoylation.
FT   MUTAGEN     698    698       K->R: No sumoylation.
FT   CONFLICT     38     38       C -> S (in Ref. 1; AAC52928).
FT   CONFLICT    257    257       I -> K (in Ref. 2; AAH37456).
SQ   SEQUENCE   736 AA;  83745 MW;  7C49D4A7BDCFEFA1 CRC64;
     MEGEAVEAIV EESETFIKGK ERKTYQRRRE GGQEEDACHL PQNQTDGGEV VQDVNSSVQM
     VMMEQLDPTL LQMKTEVMEG TVAPEAEAAV DDTQIITLQV VNMEEQPINI GELQLVQVPV
     PVTVPVATTS VEELQGAYEN EVSKEGLAES EPMICHTLPL PEGFQVVKVG ANGEVETLEQ
     GELPPQEDSS WQKDPDYQPP AKKTKKTKKS KLRYTEEGKD VDVSVYDFEE EQQEGLLSEV
     NAEKVVGNMK PPKPTKIKKK GVKKTFQCEL CSYTCPRRSN LDRHMKSHTD ERPHKCHLCG
     RAFRTVTLLR NHLNTHTGTR PHKCPDCDMA FVTSGELVRH RRYKHTHEKP FKCSMCDYAS
     VEVSKLKRHI RSHTGERPFQ CSLCSYASRD TYKLKRHMRT HSGEKPYECY ICHARFTQSG
     TMKMHILQKH TENVAKFHCP HCDTVIARKS DLGVHLRKQH SYIEQGKKCR YCDAVFHERY
     ALIQHQKSHK NEKRFKCDQC DYACRQERHM IMHKRTHTGE KPYACSHCDK TFRQKQLLDM
     HFKRYHDPNF VPAAFVCSKC GKTFTRRNTM ARHADNCAGP DGVEGENGGE TKKSKRGRKR
     KMRSKKEDSS DSEENAEPDL DDNEEEEEPA VEIEPEPEPQ PQPPPPPQPV APAPPPAKKR
     RGRPPGRTNQ PKQNQPTAII QVEDQNTGAI ENIIVEVKKE PDAEPAEGEE EEAQAATTDA
     PNGDLTPEMI LSMMDR
//
ID   SL9A1_MOUSE             Reviewed;         820 AA.
AC   Q61165;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Sodium/hydrogen exchanger 1;
DE   AltName: Full=Na(+)/H(+) exchanger 1;
DE            Short=NHE-1;
DE   AltName: Full=Solute carrier family 9 member 1;
GN   Name=Slc9a1; Synonyms=Nhe1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=21928362; PubMed=11931388; DOI=10.1023/A:1017984311138;
RA   Dewey M.J., Ennis T.M., Bowman L.H.;
RT   "cDNA cloning and expression of the mouse Na/H antiporter (NHE-1) and
RT   a potential splice variant.";
RL   Mol. Biol. Rep. 28:111-117(2001).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-707, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-603; SER-606 AND
RP   SER-609, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-707 AND THR-755, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-697, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Involved in pH regulation to eliminate acids generated
CC       by active metabolism or to counter adverse environmental
CC       conditions. Major proton extruding system driven by the inward
CC       sodium ion chemical gradient. Plays an important role in signal
CC       transduction.
CC   -!- SUBUNIT: Interacts with CALMODULIN, CHP, CHP2 and TESC (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1
CC       (CPA1) transporter (TC 2.A.36) family.
CC   -!- CAUTION: The region between transmembrane regions M4 and M5 and
CC       between M6 and M7 (also termed intracellular loops IL2 and IL4,
CC       respectively) seem to be localized at least in part in the
CC       membrane. The hydrophobic region H10 is proposed to be located
CC       within the membrane.
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DR   EMBL; U51112; AAA92976.1; -; mRNA.
DR   IPI; IPI00380785; -.
DR   RefSeq; NP_058677.1; NM_016981.2.
DR   UniGene; Mm.4312; -.
DR   ProteinModelPortal; Q61165; -.
DR   SMR; Q61165; 159-184, 254-279, 342-369, 507-549.
DR   IntAct; Q61165; 1.
DR   STRING; Q61165; -.
DR   PhosphoSite; Q61165; -.
DR   PRIDE; Q61165; -.
DR   Ensembl; ENSMUST00000030669; ENSMUSP00000030669; ENSMUSG00000028854.
DR   GeneID; 20544; -.
DR   KEGG; mmu:20544; -.
DR   UCSC; uc008vcs.1; mouse.
DR   CTD; 20544; -.
DR   MGI; MGI:102462; Slc9a1.
DR   HOVERGEN; HBG052615; -.
DR   OrthoDB; EOG4FR0R9; -.
DR   PhylomeDB; Q61165; -.
DR   NextBio; 298831; -.
DR   ArrayExpress; Q61165; -.
DR   Bgee; Q61165; -.
DR   Genevestigator; Q61165; -.
DR   GermOnline; ENSMUSG00000028854; Mus musculus.
DR   GO; GO:0016323; C:basolateral plasma membrane; TAS:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0015385; F:sodium:hydrogen antiporter activity; IDA:MGI.
DR   GO; GO:0006885; P:regulation of pH; IDA:MGI.
DR   GO; GO:0001101; P:response to acid; IMP:MGI.
DR   GO; GO:0010447; P:response to acidity; IMP:MGI.
DR   InterPro; IPR006153; Cation/H_exchanger.
DR   InterPro; IPR018422; Cation/H_exchanger_CPA1.
DR   InterPro; IPR001970; Na/H_exchanger_1.
DR   InterPro; IPR004709; NaH_exchanger.
DR   PANTHER; PTHR10110; Cation/H_exchanger_cons-reg; 1.
DR   Pfam; PF00999; Na_H_Exchanger; 1.
DR   PRINTS; PR01084; NAHEXCHNGR.
DR   PRINTS; PR01085; NAHEXCHNGR1.
DR   TIGRFAMs; TIGR00840; b_cpa1; 1.
PE   1: Evidence at protein level;
KW   Antiport; Glycoprotein; Ion transport; Membrane; Phosphoprotein;
KW   Sodium; Sodium transport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    820       Sodium/hydrogen exchanger 1.
FT                                /FTId=PRO_0000052348.
FT   TOPO_DOM      1     12       Cytoplasmic (Potential).
FT   TRANSMEM     13     33       Helical; Name=M1; (Potential).
FT   TOPO_DOM     34    105       Extracellular (Potential).
FT   TRANSMEM    106    126       Helical; Name=M2; (Potential).
FT   TOPO_DOM    127    133       Cytoplasmic (Potential).
FT   TRANSMEM    134    153       Helical; Name=M3; (Potential).
FT   TOPO_DOM    154    158       Extracellular (Potential).
FT   TRANSMEM    159    178       Helical; Name=M4; (Potential).
FT   TOPO_DOM    179    195       Cytoplasmic (Potential).
FT   TRANSMEM    196    215       Helical; Name=M5; (Potential).
FT   TOPO_DOM    216    231       Extracellular (Potential).
FT   TRANSMEM    232    251       Helical; Name=M6; (Potential).
FT   TOPO_DOM    252    260       Cytoplasmic (Potential).
FT   TRANSMEM    261    280       Helical; Name=M7; (Potential).
FT   TOPO_DOM    281    298       Extracellular (Potential).
FT   TRANSMEM    299    319       Helical; Name=M8; (Potential).
FT   TOPO_DOM    320    342       Cytoplasmic (Potential).
FT   TRANSMEM    343    362       Helical; Name=M9; (Potential).
FT   TOPO_DOM    363    385       Extracellular (Potential).
FT   INTRAMEM    386    406       Name=H10; (By similarity).
FT   TOPO_DOM    407    414       Extracellular (Potential).
FT   TRANSMEM    415    434       Helical; Name=M10; (Potential).
FT   TOPO_DOM    435    452       Cytoplasmic (Potential).
FT   TRANSMEM    453    474       Helical; Name=M11; (Potential).
FT   TOPO_DOM    475    483       Extracellular (Potential).
FT   TRANSMEM    484    503       Helical; Name=M12; (Potential).
FT   TOPO_DOM    504    820       Cytoplasmic (Potential).
FT   REGION      520    543       Interaction with CHP2 (By similarity).
FT   SITE        165    165       Channel pore-lining (By similarity).
FT   MOD_RES     603    603       Phosphoserine.
FT   MOD_RES     606    606       Phosphoserine.
FT   MOD_RES     609    609       Phosphoserine.
FT   MOD_RES     697    697       Phosphoserine.
FT   MOD_RES     699    699       Phosphothreonine (By similarity).
FT   MOD_RES     701    701       Phosphoserine (By similarity).
FT   MOD_RES     707    707       Phosphoserine.
FT   MOD_RES     727    727       Phosphoserine (By similarity).
FT   MOD_RES     730    730       Phosphoserine (By similarity).
FT   MOD_RES     733    733       Phosphoserine (By similarity).
FT   MOD_RES     755    755       Phosphothreonine.
FT   MOD_RES     790    790       Phosphoserine (By similarity).
FT   MOD_RES     792    792       Phosphoserine (By similarity).
FT   MOD_RES     793    793       Phosphoserine (By similarity).
FT   CARBOHYD    374    374       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   820 AA;  91468 MW;  0589C4D08DD348BE CRC64;
     MMLRWSGVWG FHPPRIFPSL LVVVALVGLL PVLRSHGLQH SPTASTIRGS EPPRERSIGD
     VTTAPSEPLH RPDDHNLTNL IIEHGGKPSR KAFPVLDIDY PHVRTPFEIS LWILLACLMK
     IGFHVIPTIS SIVPESCLLI VVGLLVGGLI KGVGETPPFL QSDVFFLFLL PPIILDAGYF
     LPLRQFTENL GTILIFAVVG TLWNAFFLGG LLYAVCLVGG EQINNIGLLD TLLFGSIISA
     VDPVAVLAVF EEIHINELLH ILVFGESLLN DAVTVVLYHL FEEFASYDSV GISDIFLGFL
     SFFVVALGGV FVGVVYGVIA AFTSRFTSHI RVIEPLFVFL YSYMAYLSAE LFHLSGIMAL
     IASGVVMRPY VEANISHKSH TTIKYFLKMW SSVSETLIFI FLGVSTVAGS HQWNWTFVIS
     TLLFCLIARV LGVLVLTWFI NKFRIVKLTP KDQFIIAYGG LRGAIAFSLG YLLDKKHFPM
     CDLFLTAIIT VIFFTVFVQG MTIRPLVDLL AVKKKQETKR SINEEIHTQF LDHLLTGIED
     ICGHYGHHHW KDKLNRFNKK YVKKCLIAGE RSKEPQLIAF YHKMEMKQAI ELVESGGMGK
     IPSAVSTVSM QNIHPKAVTS DRILPALSKD KEEEIRKILR SNLQKTRQRL RSYNRHTLVA
     DPYEEAWNQM LLRRQKARQL EQKITNYLTV PAHKLDSPTL SRARIGSDPL AYEPKADLPV
     ITIDPASPQS PESVDLVNEE LKGKVLGLNR GPRVTPEEEE EDEDGIIMIR SKEPSSPGTD
     DVFTPGSSDS PSSQRIQRCL SDPGPHPEPG EGEPFIPKGQ
//
ID   HCFC1_MOUSE             Reviewed;        2045 AA.
AC   Q61191; Q684R1; Q7TSB0; Q8C2D0; Q9QWH2;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Host cell factor 1;
DE            Short=HCF;
DE            Short=HCF-1;
DE   AltName: Full=C1 factor;
DE   Contains:
DE     RecName: Full=HCF N-terminal chain 1;
DE   Contains:
DE     RecName: Full=HCF N-terminal chain 2;
DE   Contains:
DE     RecName: Full=HCF N-terminal chain 3;
DE   Contains:
DE     RecName: Full=HCF N-terminal chain 4;
DE   Contains:
DE     RecName: Full=HCF N-terminal chain 5;
DE   Contains:
DE     RecName: Full=HCF N-terminal chain 6;
DE   Contains:
DE     RecName: Full=HCF C-terminal chain 1;
DE   Contains:
DE     RecName: Full=HCF C-terminal chain 2;
DE   Contains:
DE     RecName: Full=HCF C-terminal chain 3;
DE   Contains:
DE     RecName: Full=HCF C-terminal chain 4;
DE   Contains:
DE     RecName: Full=HCF C-terminal chain 5;
DE   Contains:
DE     RecName: Full=HCF C-terminal chain 6;
GN   Name=Hcfc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Fetal liver;
RX   PubMed=9334261; DOI=10.1074/jbc.272.42.26749;
RA   Kristie T.M.;
RT   "The mouse homologue of the human transcription factor C1 (host cell
RT   factor). Conservation of forms and function.";
RL   J. Biol. Chem. 272:26749-26755(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Limb mesenchyme;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-209.
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 165-520.
RC   STRAIN=NMRI; TISSUE=Embryo;
RA   Kolb A.A., Mehrle A., Bechtel S., Wellenreuther R., Simpson J.,
RA   Pepperkok R., Wiemann S., Poustka A.;
RT   "Towards functional annotation of all Xq28 genes: expression and
RT   intracellular localization analyses reveal novel candidates for
RT   disease genes.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c;
RX   PubMed=9990006; DOI=10.1073/pnas.96.4.1229;
RA   Kristie T.M., Vogel J.L., Sears A.E.;
RT   "Nuclear localization of the C1 factor (host cell factor) in sensory
RT   neurons correlates with reactivation of herpes simplex virus from
RT   latency.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:1229-1233(1999).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452088; DOI=10.1074/mcp.T500040-MCP200;
RA   Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G.,
RA   Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F.,
RA   Maltby D.A., Schoepfer R., Burlingame A.L.;
RT   "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT   preparations using lectin weak affinity chromatography and mass
RT   spectrometry.";
RL   Mol. Cell. Proteomics 5:923-934(2006).
RN   [7]
RP   INTERACTION WITH THAP11.
RX   PubMed=18585351; DOI=10.1016/j.cell.2008.05.047;
RA   Dejosez M., Krumenacker J.S., Zitur L.J., Passeri M., Chu L.-F.,
RA   Songyang Z., Thomson J.A., Zwaka T.P.;
RT   "Ronin is essential for embryogenesis and the pluripotency of mouse
RT   embryonic stem cells.";
RL   Cell 133:1162-1174(2008).
RN   [8]
RP   ERRATUM.
RA   Dejosez M., Krumenacker J.S., Zitur L.J., Passeri M., Chu L.-F.,
RA   Songyang Z., Thomson J.A., Zwaka T.P.;
RL   Cell 134:692-692(2008).
CC   -!- FUNCTION: Involved in control of the cell cycle. Also antagonizes
CC       transactivation by ZBTB17 and GABP2; represses ZBTB17 activation
CC       of the p15(INK4b) promoter and inhibits its ability to recruit
CC       p300. Coactivator for EGR2 and GABP2. Tethers the chromatin
CC       modifying Set1/Ash2 histone H3 'Lys-4' methyltransferase (H3K4me)
CC       and Sin3 histone deacetylase (HDAC) complexes (involved in the
CC       activation and repression of transcription respectively) together.
CC   -!- SUBUNIT: Composed predominantly of six polypeptides ranging from
CC       110 to 150 kDa and a minor 300 kDa polypeptide. The majority of N-
CC       and C-terminal cleavage products remain tightly, albeit non-
CC       covalently, associated. Interacts with POU2F1, CREB3, ZBTB17,
CC       EGR2, E2F4, CREBZF, SP1, GABP2, Sin3 HDAC complex (SIN3A, HDAC1,
CC       HDAC2, SDS3), SAP30, SIN3B, OGT1 and FHL2. Component of some
CC       MLL1/MLL complex, at least composed of the core components MLL,
CC       ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative
CC       components C17orf49, CHD8, DPY30, E2F6, HCFC2, HSP70, IN80C,
CC       KIAA1267, LAS1L, MAX, MCRS1, MEN1, MGA, MYST1/MOF, PELP1, PHF20,
CC       PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6,
CC       TAF7, TAF9 and TEX10. Component of the MLL5-L complex, at least
CC       composed of MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and
CC       OGT (By similarity). Interacts with HCFC1R1 (By similarity).
CC       Interacts with THAP11. Component of the SET1 complex, at least
CC       composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82,
CC       RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30. Interacts (via HBM
CC       motif) with SETD1A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=HCFC1R1 modulates
CC       its subcellular localization and overexpression of HCFC1R1 leads
CC       to accumulation of HCFC1 in the cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in liver, pituitary gland, skeletal
CC       muscle, kidney, eye and brain (at protein level). Also observed at
CC       low level in heart, spleen and lung.
CC   -!- DOMAIN: The HCF repeat is a highly specific proteolytic cleavage
CC       signal (By similarity).
CC   -!- DOMAIN: The kelch repeats fold into a 6-bladed kelch beta-
CC       propeller called the beta-propeller domain which mediates
CC       interaction with HCFC1R1 (By similarity).
CC   -!- PTM: Proteolytically cleaved at one or several PPCE--THET sites
CC       within the HCF repeats (By similarity).
CC   -!- PTM: O-glycosylated.
CC   -!- PTM: Ubiquitinated. Lys-1817 and Lys-1818 are ubiquitinated both
CC       via 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. BAP1
CC       mediated deubiquitination of 'Lys-48'-linked polyubiquitin chains;
CC       deubiquitination by BAP1 does not seem to stabilize the protein
CC       (By similarity).
CC   -!- SIMILARITY: Contains 5 Kelch repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAF25305.1; Type=Frameshift; Positions=339;
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DR   EMBL; U53925; AAB01163.1; -; Genomic_DNA.
DR   EMBL; U80821; AAD09225.1; -; Genomic_DNA.
DR   EMBL; BC053742; AAH53742.1; -; mRNA.
DR   EMBL; AK088827; BAC40597.1; -; mRNA.
DR   EMBL; AJ627036; CAF25305.1; ALT_FRAME; mRNA.
DR   IPI; IPI00828490; -.
DR   RefSeq; NP_032250.2; NM_008224.3.
DR   UniGene; Mm.420572; -.
DR   UniGene; Mm.439140; -.
DR   UniGene; Mm.480587; -.
DR   ProteinModelPortal; Q61191; -.
DR   SMR; Q61191; 360-386, 1860-2018.
DR   STRING; Q61191; -.
DR   PhosphoSite; Q61191; -.
DR   PRIDE; Q61191; -.
DR   Ensembl; ENSMUST00000033761; ENSMUSP00000033761; ENSMUSG00000031386.
DR   GeneID; 15161; -.
DR   KEGG; mmu:15161; -.
DR   UCSC; uc009tnm.1; mouse.
DR   CTD; 15161; -.
DR   MGI; MGI:105942; Hcfc1.
DR   GeneTree; ENSGT00550000074193; -.
DR   HOVERGEN; HBG051888; -.
DR   OrthoDB; EOG49GKGP; -.
DR   ArrayExpress; Q61191; -.
DR   Bgee; Q61191; -.
DR   CleanEx; MM_HCFC1; -.
DR   Genevestigator; Q61191; -.
DR   GermOnline; ENSMUSG00000031386; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR   GO; GO:0048188; C:Set1C/COMPASS complex; ISS:UniProtKB.
DR   GO; GO:0003713; F:transcription coactivator activity; TAS:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0019046; P:reactivation of latent virus; IDA:UniProtKB.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR011498; Kelch_2.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Gene3D; G3DSA:2.120.10.80; Kelch-typ_b-propeller; 1.
DR   Pfam; PF01344; Kelch_1; 2.
DR   Pfam; PF07646; Kelch_2; 1.
DR   SMART; SM00060; FN3; 2.
DR   SUPFAM; SSF49265; FN_III-like; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Autocatalytic cleavage; Cell cycle; Cytoplasm;
KW   Glycoprotein; Isopeptide bond; Kelch repeat; Nucleus; Phosphoprotein;
KW   Repeat; Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1432       HCF N-terminal chain 6 (By similarity).
FT                                /FTId=PRO_0000016635.
FT   CHAIN         2   1332       HCF N-terminal chain 5 (By similarity).
FT                                /FTId=PRO_0000016636.
FT   CHAIN         2   1304       HCF N-terminal chain 4 (By similarity).
FT                                /FTId=PRO_0000016637.
FT   CHAIN         2   1110       HCF N-terminal chain 3 (By similarity).
FT                                /FTId=PRO_0000016638.
FT   CHAIN         2   1081       HCF N-terminal chain 2 (By similarity).
FT                                /FTId=PRO_0000016639.
FT   CHAIN         2   1019       HCF N-terminal chain 1 (By similarity).
FT                                /FTId=PRO_0000016640.
FT   CHAIN      1020   2045       HCF C-terminal chain 1 (By similarity).
FT                                /FTId=PRO_0000016641.
FT   CHAIN      1082   2045       HCF C-terminal chain 2 (By similarity).
FT                                /FTId=PRO_0000016642.
FT   CHAIN      1111   2045       HCF C-terminal chain 3 (By similarity).
FT                                /FTId=PRO_0000016643.
FT   CHAIN      1305   2045       HCF C-terminal chain 4 (By similarity).
FT                                /FTId=PRO_0000016644.
FT   CHAIN      1333   2045       HCF C-terminal chain 5 (By similarity).
FT                                /FTId=PRO_0000016645.
FT   CHAIN      1433   2045       HCF C-terminal chain 6 (By similarity).
FT                                /FTId=PRO_0000016646.
FT   REPEAT       44     89       Kelch 1.
FT   REPEAT       93    140       Kelch 2.
FT   REPEAT      148    194       Kelch 3.
FT   REPEAT      217    265       Kelch 4.
FT   REPEAT      266    313       Kelch 5.
FT   REPEAT     1010   1035       HCF repeat 1.
FT   REPEAT     1072   1097       HCF repeat 2.
FT   REPEAT     1101   1126       HCF repeat 3.
FT   REPEAT     1157   1182       HCF repeat 4; degenerate.
FT   REPEAT     1295   1320       HCF repeat 5.
FT   REPEAT     1323   1348       HCF repeat 6.
FT   REPEAT     1358   1383       HCF repeat 7; degenerate.
FT   REPEAT     1423   1448       HCF repeat 8.
FT   REGION      610    722       Interaction with SIN3A (By similarity).
FT   REGION      750    902       Interaction with ZBTB17 (By similarity).
FT   REGION      813    912       Interaction with GABP2 (By similarity).
FT   COMPBIAS    574   1500       Thr-rich.
FT   COMPBIAS   1622   1674       Ala-rich.
FT   COMPBIAS   1684   1720       Gln-rich.
FT   SITE       1019   1020       Cleavage; by autolysis (By similarity).
FT   SITE       1081   1082       Cleavage; by autolysis (By similarity).
FT   SITE       1110   1111       Cleavage; by autolysis (By similarity).
FT   SITE       1304   1305       Cleavage; by autolysis (By similarity).
FT   SITE       1332   1333       Cleavage; by autolysis (By similarity).
FT   SITE       1432   1433       Cleavage; by autolysis (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       6      6       Phosphoserine (By similarity).
FT   MOD_RES     288    288       N6-acetyllysine (By similarity).
FT   MOD_RES     411    411       Phosphoserine (By similarity).
FT   MOD_RES     598    598       Phosphoserine (By similarity).
FT   MOD_RES     666    666       Phosphoserine (By similarity).
FT   MOD_RES     733    733       Phosphothreonine (By similarity).
FT   MOD_RES     737    737       Phosphothreonine (By similarity).
FT   MOD_RES     738    738       Phosphothreonine (By similarity).
FT   MOD_RES     813    813       N6-acetyllysine (By similarity).
FT   MOD_RES     836    836       N6-acetyllysine (By similarity).
FT   MOD_RES    1204   1204       Phosphoserine (By similarity).
FT   MOD_RES    1500   1500       Phosphothreonine (By similarity).
FT   MOD_RES    1516   1516       Phosphoserine (By similarity).
FT   MOD_RES    2015   2015       N6-acetyllysine (By similarity).
FT   MOD_RES    2017   2017       Phosphoserine (By similarity).
FT   MOD_RES    2018   2018       Phosphoserine (By similarity).
FT   MOD_RES    2030   2030       Phosphoserine (By similarity).
FT   CROSSLNK    105    105       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK    163    163       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK    244    244       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK    363    363       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK   1817   1817       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK   1818   1818       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CONFLICT    483    483       R -> V (in Ref. 2 and 4).
FT   CONFLICT    520    520       P -> S (in Ref. 4; CAF25305).
FT   CONFLICT    567    568       AW -> VL (in Ref. 2; AAH53742).
FT   CONFLICT    711    711       Q -> H (in Ref. 1; AAD09225).
FT   CONFLICT   1104   1104       S -> C (in Ref. 2; AAH53742).
FT   CONFLICT   1230   1230       A -> G (in Ref. 2; AAH53742).
SQ   SEQUENCE   2045 AA;  210537 MW;  B89CC2FDA35B969F CRC64;
     MASAVSPANL PAVLLQPRWK RVVGWSGPVP RPRHGHRAVA IKELIVVFGG GNEGIVDELH
     VYNTATNQWF IPAVRGDIPP GCAAYGFVCD GTRLLVFGGM VEYGKYSNDL YELQASRWEW
     KRLKAKTPKN GPPPCPRLGH SFSLVGNKCY LFGGLANDSE DPKNNIPRYL NDLYILELRP
     GSGVVAWDIP ITYGVLPPPR ESHTAVVYTE KDNKKSKLVI YGGMSGCRLG DLWTLDIETL
     TWNKPSLSGV APLPRSLHSA TTIGNKMYVF GGWVPLVMDD VKVATHEKEW KCTNTLACLN
     LDTMAWETIL MDTLEDNIPR ARAGHCAVAI NTRLYIWSGR DGYRKAWNNQ VCCKDLWYLE
     TEKPPPPARV QLVRANTNSL EVSWGAVATA DSYLLQLQKY DIPATAATAT SPTPNPVPSV
     PANPPKSPAP AAAAPAVQPL TQVGITLVPQ AATAPPSTTT IQVLPTVPGS SISVPTAART
     QGRPAVLKVT GPQATTGTPL VTMRPASQAG KAPVTVTSLP ASVRMVVPTQ SAQGTVIGSN
     PQMSGMAALA AAAAATQKIP PSSAPTAWSV PAGTTIVKTV AVTPGTTTLP ATVKVASSPV
     MVSNPATRML KTAAAQVGTS VSSAANTSTR PIITVHKSGT VTVAQQAQVV TTVVGGVTKT
     ITLVKSPISV PGGSALISNL GKVMSVVQTK PVQTSAVTGQ ASTGPVTQII QTKGPLPAGT
     ILKLVTSADG KPTTIITTTQ ASGAGTKPTI LGISSVSPST TKPGTTTIIK TIPMSAIITQ
     AGATGVTSSP GIKSPITIIT TKVMTSGTGA PAKIITAVPK IATGHGQQGV TQVVLKGAPG
     QPGTILRTVP MGGVRLVTPV TVSAVKPAVT TLVVKGTTGV TTLGTVTGTV STSLAGAGAH
     STSASLATPI TTLGTIATLS SQVINPTAIT VSAAQTTLTA AGGLTTPTIT MQPVSQPTQV
     TLITAPSGVE AQPVHDLPVS ILASPTTEQP TATVTIADSG QGDVQPGTVT LVCSNPPCET
     HETGTTNTAT TTVVANLGGH PQPTQVQFVC DRQETAASLV TSAVGQQNGN VVRVCSNPPC
     ETHETGTTNT ATTATSNMAG QHGSSNPPCE THETGTTSTA TTAMSSMGTG QQRDTRRTTN
     TPTVVRITVA PGALERVQGT VKPQCQTQQT NMTTTTMTVQ ATGAPCSAGP LLRPSVALES
     GSHSPAFVQL ALPSVRVGLS GPSSKDMPTA RQPETYHTYT TNTPTTTRSI MVAGELGAAR
     VVPTSTYESL QASSPSSTMT MTALEALLCP SATVTQVCSN PPCETHETGT TNTATTSNAG
     SAQRVCSNPP CETHETGTTH TATTATSNGG AGQPEGGQQP ASGHPCETHQ TTSTGTTMSV
     SVGTLIPDAT SSHGTLESGL EVVAVPTVTS QAGSTLLASF PTQRVCSNPP CETHETGTTH
     TATTVTSNMS SNQDPPPAAS DQGEVASTQG DSTNITSASA ITTSVSSTLP RAVTTVTQST
     PVPGPSVPPP EELQVSPGPR QQLPPRQLLQ SASTPLMGES TEVLSASQTP ELQAAVDLSS
     TGDPSSGQEP TTSAVVATVV VQPPPPTQSE VDQLSLPQEL MAEAQAGTTT LMVTGLTPEE
     LAVTAAAEAA AQAAATEEAQ ALAIQAVLQA AQQAVMGTGE PMDTSEAAAA VTQAELGHLS
     AEGQEGQATT IPIVLTQQEL AALVQQQQQL QEAQAQAQQQ HHLPTEALAP ADSLNDPSIE
     SNCLNELASA VPSTVALLPS TATESLAPSN TFVAPQPVVA SPAKMQAAAT LTEVANGIES
     LGVKPDLPPP PSKAPVKKEN QWFDVGVIKG TSVMVTHYFL PPDDAVQSDD DSGTVPDYNQ
     LKKQELQPGT AYKFRVAGIN ACGRGPFSEI SAFKTCLPGF PGAPCAIKIS KSPDGAHLTW
     EPPSVTSGKI IEYSVYLAIQ SSQASGEPKS STPAQLAFMR VYCGPSPSCL VQSSSLSNAH
     IDYTTKPAII FRIAARNEKG YGPATQVRWL QETSKDSSGT KPASKRPMSS PEMKSAPKKS
     KADGQ
//
ID   PA1B2_MOUSE             Reviewed;         229 AA.
AC   Q61206; Q6PKE6; Q7TNP3;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Platelet-activating factor acetylhydrolase IB subunit beta;
DE            EC=3.1.1.47;
DE   AltName: Full=PAF acetylhydrolase 30 kDa subunit;
DE            Short=PAF-AH 30 kDa subunit;
DE   AltName: Full=PAF-AH subunit beta;
DE            Short=PAFAH subunit beta;
GN   Name=Pafah1b2; Synonyms=Pafahb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=97115706; PubMed=8954729; DOI=10.1006/dbio.1996.0330;
RA   Albrecht U., Abu-Issa R., Raetz B., Hattori M., Aoki J., Arai H.,
RA   Inoue K., Eichele G.;
RT   "Platelet-activating factor acetylhydrolase expression and activity
RT   suggest a link between neuronal migration and platelet-activating
RT   factor.";
RL   Dev. Biol. 180:579-593(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Embryo, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 61-79 AND 134-142, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
CC   -!- FUNCTION: Inactivates PAF by removing the acetyl group at the sn-2
CC       position. This is a catalytic subunit.
CC   -!- CATALYTIC ACTIVITY: 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine +
CC       H(2)O = 1-alkyl-sn-glycero-3-phosphocholine + acetate.
CC   -!- SUBUNIT: Cytosolic PAF-AH IB is formed of three subunits of 45 kDa
CC       (alpha), 30 kDa (beta) and 29 kDa (gamma). The catalytic activity
CC       of the enzyme resides in the beta and gamma subunits, whereas the
CC       alpha subunit has regulatory activity. Trimer formation is not
CC       essential for the catalytic activity.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DEVELOPMENTAL STAGE: Expressed already by the time of neurulation.
CC       By E10.5, expression is abundant in the developing central and
CC       peripheral nervous systems. Major sites include the
CC       neuroepithelium of the fore-, mid-, and hindbrain, the spinal
CC       cord, the dorsal root, and cranial ganglia.
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       Platelet-activating factor acetylhydrolase IB beta/gamma subunits
CC       subfamily.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; U57747; AAC52997.1; -; mRNA.
DR   EMBL; AK153424; BAE31983.1; -; mRNA.
DR   EMBL; BC002037; AAH02037.1; -; mRNA.
DR   EMBL; BC056211; AAH56211.1; -; mRNA.
DR   IPI; IPI00118821; -.
DR   RefSeq; NP_032801.2; NM_008775.3.
DR   UniGene; Mm.200859; -.
DR   ProteinModelPortal; Q61206; -.
DR   SMR; Q61206; 6-217.
DR   MINT; MINT-4106420; -.
DR   STRING; Q61206; -.
DR   PhosphoSite; Q61206; -.
DR   REPRODUCTION-2DPAGE; IPI00118821; -.
DR   REPRODUCTION-2DPAGE; Q61206; -.
DR   UCD-2DPAGE; Q61206; -.
DR   PRIDE; Q61206; -.
DR   Ensembl; ENSMUST00000003215; ENSMUSP00000003215; ENSMUSG00000003131.
DR   GeneID; 18475; -.
DR   KEGG; mmu:18475; -.
DR   CTD; 18475; -.
DR   MGI; MGI:108415; Pafah1b2.
DR   eggNOG; roNOG10533; -.
DR   HOGENOM; HBG715888; -.
DR   HOVERGEN; HBG053477; -.
DR   InParanoid; Q61206; -.
DR   OMA; SMVQLLQ; -.
DR   OrthoDB; EOG45QHF4; -.
DR   PhylomeDB; Q61206; -.
DR   BRENDA; 3.1.1.47; 244.
DR   NextBio; 294170; -.
DR   ArrayExpress; Q61206; -.
DR   Bgee; Q61206; -.
DR   Genevestigator; Q61206; -.
DR   GermOnline; ENSMUSG00000003131; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IEA:EC.
DR   GO; GO:0006928; P:cellular component movement; TAS:ProtInc.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0007283; P:spermatogenesis; IGI:MGI.
DR   InterPro; IPR013830; Esterase_SGNH_hydro-type.
DR   InterPro; IPR013831; Esterase_SGNH_hydro-type_subgr.
DR   InterPro; IPR001087; Lipase_GDSL.
DR   Gene3D; G3DSA:3.40.50.1110; Esterase_SGNH_hydro-type_subgr; 1.
DR   Pfam; PF00657; Lipase_GDSL; 1.
DR   SUPFAM; SSF52266; Esterase_SGNH_hydro-type; 1.
DR   PROSITE; PS01098; LIPASE_GDSL_SER; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Hydrolase; Lipid degradation;
KW   Phosphoprotein.
FT   CHAIN         1    229       Platelet-activating factor
FT                                acetylhydrolase IB subunit beta.
FT                                /FTId=PRO_0000058152.
FT   ACT_SITE     48     48       By similarity.
FT   ACT_SITE    193    193       By similarity.
FT   ACT_SITE    196    196       By similarity.
FT   MOD_RES       2      2       Phosphoserine (By similarity).
FT   CONFLICT    129    130       QP -> HA (in Ref. 1; AAC52997).
FT   CONFLICT    188    188       C -> W (in Ref. 3; AAH56211).
FT   CONFLICT    222    222       E -> G (in Ref. 1; AAC52997).
SQ   SEQUENCE   229 AA;  25581 MW;  B4D24048621AB182 CRC64;
     MSQGDSNPAA IPHAAEDIQG DDRWMSQHNR FVLDCKDKEP DVLFVGDSMV QLMQQYEIWR
     ELFSPLHALN FGIGGDTTRH VLWRLKNGEL ENIKPKVIVV WVGTNNHENT AEEVAGGIEA
     IVQLINTRQP QAKIIVLGLL PRGEKPNPLR QKNAKVNQLL KVSLPKLANV QLLDIDGGFV
     HSDGAISCHD MFDFLHLTGG GYAKICKPLH ELIMQLLEET PEEKQTTIA
//
ID   EIF2D_MOUSE             Reviewed;         570 AA.
AC   Q61211; Q3TDE0; Q3THV5; Q3TTP4; Q8C491; Q8CBF1; Q8CC17; Q8R1I9;
AC   Q8R3M5;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 3.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Eukaryotic translation initiation factor 2D;
DE            Short=eIF2D;
DE   AltName: Full=Ligatin;
GN   Name=Eif2d; Synonyms=Lgtn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=BALB/c, C57BL/6J, and NOD;
RC   TISSUE=Adrenal gland, Cerebellum, Diencephalon, Embryo, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-550.
RX   MEDLINE=97224508; PubMed=9070942; DOI=10.1006/geno.1996.4550;
RA   Malnar-Dragojevic D., Trachtulec Z., Vincek V.;
RT   "Assignment of the mouse ligatin gene (Lgtn) to chromosome 1F by in
RT   situ hybridization.";
RL   Genomics 40:192-193(1997).
CC   -!- FUNCTION: Translation initiation factor that is able to deliver
CC       tRNA to the P-site of the eukaryotic ribosome in a GTP-independent
CC       manner. The binding of Met-tRNA(I) occurs after the AUG codon
CC       finds its position in the P-site of 40S ribosomes, the situation
CC       that takes place during initiation complex formation on some
CC       specific RNAs. Its activity in tRNA binding with 40S subunits does
CC       not require the presence of the aminoacyl moiety. Possesses the
CC       unique ability to deliver non-Met (elongator) tRNAs into the P-
CC       site of the 40S subunit. In addition to its role in initiation,
CC       can promote release of deacylated tRNA and mRNA from recycled 40S
CC       subunits following ABCE1-mediated dissociation of post-termination
CC       ribosomal complexes into subunits (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q61211-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q61211-2; Sequence=VSP_016233;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the eIF2D family.
CC   -!- SIMILARITY: Contains 1 PUA domain.
CC   -!- SIMILARITY: Contains 1 SUI1 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC53056.1; Type=Frameshift; Positions=4;
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DR   EMBL; AK034115; BAC28591.1; -; mRNA.
DR   EMBL; AK036154; BAC29323.1; -; mRNA.
DR   EMBL; AK046539; BAC32777.1; -; mRNA.
DR   EMBL; AK082748; BAC38598.1; -; mRNA.
DR   EMBL; AK083638; BAC38976.1; -; mRNA.
DR   EMBL; AK139052; BAE23874.1; -; mRNA.
DR   EMBL; AK161269; BAE36281.1; -; mRNA.
DR   EMBL; AK167980; BAE39972.1; -; mRNA.
DR   EMBL; AK168120; BAE40091.1; -; mRNA.
DR   EMBL; AK170252; BAE41662.1; -; mRNA.
DR   EMBL; AK170448; BAE41806.1; -; mRNA.
DR   EMBL; AK171115; BAE42257.1; -; mRNA.
DR   EMBL; BC024501; AAH24501.1; -; mRNA.
DR   EMBL; BC025036; AAH25036.1; -; mRNA.
DR   EMBL; U58337; AAC53056.1; ALT_FRAME; mRNA.
DR   IPI; IPI00153773; -.
DR   IPI; IPI00348910; -.
DR   RefSeq; NP_001129542.1; NM_001136070.1.
DR   RefSeq; NP_034839.2; NM_010709.3.
DR   UniGene; Mm.276294; -.
DR   ProteinModelPortal; Q61211; -.
DR   SMR; Q61211; 93-175.
DR   PhosphoSite; Q61211; -.
DR   PRIDE; Q61211; -.
DR   Ensembl; ENSMUST00000068805; ENSMUSP00000063894; ENSMUSG00000026427.
DR   Ensembl; ENSMUST00000086578; ENSMUSP00000083770; ENSMUSG00000026427.
DR   GeneID; 16865; -.
DR   KEGG; mmu:16865; -.
DR   UCSC; uc007cmy.1; mouse.
DR   CTD; 16865; -.
DR   MGI; MGI:109342; Eif2d.
DR   eggNOG; roNOG14309; -.
DR   GeneTree; ENSGT00550000074865; -.
DR   HOVERGEN; HBG006268; -.
DR   PhylomeDB; Q61211; -.
DR   NextBio; 290818; -.
DR   PMAP-CutDB; Q61211; -.
DR   ArrayExpress; Q61211; -.
DR   Bgee; Q61211; -.
DR   CleanEx; MM_LGTN; -.
DR   Genevestigator; Q61211; -.
DR   GermOnline; ENSMUSG00000026427; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR   InterPro; IPR002478; PUA.
DR   InterPro; IPR015947; PUA-like.
DR   InterPro; IPR003121; SWIB_MDM2_domain.
DR   InterPro; IPR001950; TIF_SUI1.
DR   InterPro; IPR004521; Uncharacterised_dom_2.
DR   Pfam; PF01253; SUI1; 1.
DR   SMART; SM00359; PUA; 1.
DR   SUPFAM; SSF47592; MDM2; 1.
DR   SUPFAM; SSF88697; PUA-like; 1.
DR   SUPFAM; SSF55159; TIF_SUI1; 1.
DR   TIGRFAMs; TIGR00451; unchar_dom_2; 1.
DR   PROSITE; PS50890; PUA; 1.
DR   PROSITE; PS50296; SUI1; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Initiation factor; Phosphoprotein;
KW   Protein biosynthesis.
FT   CHAIN         1    570       Eukaryotic translation initiation factor
FT                                2D.
FT                                /FTId=PRO_0000130612.
FT   DOMAIN       93    173       PUA.
FT   DOMAIN      478    548       SUI1.
FT   MOD_RES     184    184       Phosphoserine (By similarity).
FT   VAR_SEQ     551    570       YRLPGKYIQGLEKAPKPGKK -> NTGTLHLPAQYPHPHVQ
FT                                NKPEIPHLSCCGLPASHDSI (in isoform 2).
FT                                /FTId=VSP_016233.
FT   CONFLICT    176    179       LWRS -> HASA (in Ref. 2; AAH24501).
FT   CONFLICT    177    177       W -> V (in Ref. 3; AAC53056).
FT   CONFLICT    249    249       E -> K (in Ref. 1; BAE36281).
FT   CONFLICT    268    268       K -> E (in Ref. 1; BAE41662).
FT   CONFLICT    289    289       P -> R (in Ref. 1; BAE40091).
FT   CONFLICT    341    341       S -> P (in Ref. 1; BAC28591).
FT   CONFLICT    549    549       E -> G (in Ref. 1; BAC29323/BAC38598 and
FT                                3).
FT   CONFLICT    550    552       EYR -> IMW (in Ref. 1; BAC28591).
SQ   SEQUENCE   570 AA;  62830 MW;  68DAA2768A595AC8 CRC64;
     MFAKAFRVKS NTAIKGSDRR KLRADVTAAF PALGTDQISE LIPGKEELNV VKLYVHKGDS
     VTVYTSGGNP ILFELEKNLY PTVYTLWAYP DILPTFITWP LVLEKLVGGA DLMLPGVVVP
     PTGLPQVQQG DLCAIALVGN RAPVAIGVAA MSTAQMLASG LKGKGVSVLH TYQDHLWRSG
     DKSSPPAIAP LDPTDSCEEK VHLGLQGNLK SLTLDGEEEN GQVPLREASE DTSSRAPSQD
     SLDGKPLQEQ MDDLLLRCFL HALKSRVKKA DLPLLTSTLL GSHMFSCCPE GQQLDIKKSS
     YKKLSKFLQH MQQEQIVQVK ELSKGVESIV AVDWRHPRIT SFVIPEPSLT SQTVQEVSRE
     QPYLPPDIKS LYCVPANMTQ LFLESGHKKG STLEGSEVRK IITDYAKRNR LVDADNRNLV
     KLDPILCDCI LEKNEQHLVT KLPWDCLLTR CLKNMQPAYQ VTFPGQEPIL KKGKLCPIDI
     TLALKTYNKK VTVVRNLETY GLDPCSVAAI LQQRCQASTI VSPAPGAKDS LQVQVQGNQI
     HHLGQLLLEE YRLPGKYIQG LEKAPKPGKK
//
ID   DYR1A_MOUSE             Reviewed;         763 AA.
AC   Q61214;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 102.
DE   RecName: Full=Dual specificity tyrosine-phosphorylation-regulated kinase 1A;
DE            EC=2.7.12.1;
DE   AltName: Full=Dual specificity YAK1-related kinase;
DE   AltName: Full=MP86;
DE   AltName: Full=Protein kinase minibrain homolog;
DE            Short=MNBH;
GN   Name=Dyrk1a; Synonyms=Dyrk;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Swiss Webster / NIH; TISSUE=Embryo;
RX   MEDLINE=97131512; PubMed=8975710; DOI=10.1006/geno.1996.0636;
RA   Song W.J., Sternberg L.R., Kasten-Sportes C., van Keuren M.L.,
RA   Chung S.H., Slack A.C., Miller D.E., Glover T.W., Chiang P.W., Lou L.,
RA   Kurnit D.W.;
RT   "Isolation of human and murine homologues of the Drosophila minibrain
RT   gene: human homologue maps to 21q22.2 in the Down syndrome 'critical
RT   region'.";
RL   Genomics 38:331-339(1996).
RN   [2]
RP   SUBCELLULAR LOCATION, AND SUBUNIT.
RX   MEDLINE=97224401; PubMed=9070862; DOI=10.1006/bbrc.1997.6154;
RA   Song W.J., Chung S.H., Kurnit D.M.;
RT   "The murine Dyrk protein maps to chromosome 16, localizes to the
RT   nucleus, and can form multimers.";
RL   Biochem. Biophys. Res. Commun. 231:640-644(1997).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321, AND MASS
RP   SPECTROMETRY.
RX   MEDLINE=22426906; PubMed=12522270; DOI=10.1073/pnas.2436191100;
RA   Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,
RA   Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.;
RT   "Profiling of tyrosine phosphorylation pathways in human cells using
RT   mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
RN   [4]
RP   INTERACTION WITH RAD54L2.
RX   PubMed=15199138; DOI=10.1128/MCB.24.13.5821-5834.2004;
RA   Sitz J.H., Tigges M., Baumgaertel K., Khaspekov L.G., Lutz B.;
RT   "Dyrk1A potentiates steroid hormone-induced transcription via the
RT   chromatin remodeling factor Arip4.";
RL   Mol. Cell. Biol. 24:5821-5834(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321, AND MASS
RP   SPECTROMETRY.
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-145, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: May play a role in a signaling pathway regulating
CC       nuclear functions of cell proliferation. Phosphorylates serine,
CC       threonine and tyrosine residues in its sequence and in exogenous
CC       substrates.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Inhibited by RANBP9 (By similarity).
CC   -!- SUBUNIT: Interacts with RANBP9 (By similarity). Interacts with
CC       RAD54L2/ARIP4. Interacts with WDR68 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle.
CC   -!- TISSUE SPECIFICITY: Expressed in a variety of embryonic and adult
CC       tissues. Expressed abundantly in neurons of the brain, spinal
CC       cord, and retina in developing embryos.
CC   -!- PTM: Autophosphorylated on tyrosine residues (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. MNB/DYRK subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; U58497; AAC52994.1; -; mRNA.
DR   IPI; IPI00118849; -.
DR   RefSeq; NP_001106860.1; NM_001113389.1.
DR   RefSeq; NP_031916.1; NM_007890.2.
DR   UniGene; Mm.310973; -.
DR   ProteinModelPortal; Q61214; -.
DR   SMR; Q61214; 148-481.
DR   IntAct; Q61214; 1.
DR   MINT; MINT-1205474; -.
DR   STRING; Q61214; -.
DR   PhosphoSite; Q61214; -.
DR   PRIDE; Q61214; -.
DR   Ensembl; ENSMUST00000023614; ENSMUSP00000023614; ENSMUSG00000022897.
DR   Ensembl; ENSMUST00000119878; ENSMUSP00000113660; ENSMUSG00000022897.
DR   GeneID; 13548; -.
DR   KEGG; mmu:13548; -.
DR   UCSC; uc008abg.1; mouse.
DR   CTD; 13548; -.
DR   MGI; MGI:1330299; Dyrk1a.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG051425; -.
DR   InParanoid; Q61214; -.
DR   OMA; HRHSGGH; -.
DR   OrthoDB; EOG4MW85K; -.
DR   PhylomeDB; Q61214; -.
DR   BRENDA; 2.7.12.1; 244.
DR   NextBio; 284158; -.
DR   ArrayExpress; Q61214; -.
DR   Bgee; Q61214; -.
DR   Genevestigator; Q61214; -.
DR   GermOnline; ENSMUSG00000022897; Mus musculus.
DR   GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043621; F:protein self-association; IPI:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT   CHAIN         1    763       Dual specificity tyrosine-
FT                                phosphorylation-regulated kinase 1A.
FT                                /FTId=PRO_0000085932.
FT   DOMAIN      159    479       Protein kinase.
FT   NP_BIND     165    173       ATP (By similarity).
FT   MOTIF       117    134       Bipartite nuclear localization signal
FT                                (Potential).
FT   COMPBIAS    509    515       Poly-Ser.
FT   COMPBIAS    599    602       Poly-His.
FT   COMPBIAS    607    619       Poly-His.
FT   COMPBIAS    656    672       Ser/Thr-rich.
FT   COMPBIAS    664    671       Poly-Ser.
FT   ACT_SITE    287    287       Proton acceptor (By similarity).
FT   BINDING     188    188       ATP (By similarity).
FT   MOD_RES     145    145       Phosphotyrosine.
FT   MOD_RES     219    219       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     319    319       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     321    321       Phosphotyrosine; by autocatalysis.
FT   MOD_RES     324    324       Phosphoserine (By similarity).
FT   MOD_RES     748    748       Phosphoserine (By similarity).
FT   MOD_RES     758    758       Phosphoserine (By similarity).
SQ   SEQUENCE   763 AA;  85494 MW;  E117DDD6C5E8C74F CRC64;
     MHTGGETSAC KPSSVRLAPS FSFHAAGLQM AAQMPHSHQY SDRRQPSISD QQVSALPYSD
     QIQQPLTNQV MPDIVMLQRR MPQTFRDPAT APLRKLSVDL IKTYKHINEV YYAKKKRRHQ
     QGQGDDSSHK KERKVYNDGY DDDNYDYIVK NGEKWMDRYE IDSLIGKGSF GQVVKAYDRV
     EQEWVAIKII KNKKAFLNQA QIEVRLLELM NKHDTEMKYY IVHLKRHFMF RNHLCLVFEM
     LSYNLYDLLR NTNFRGVSLN LTRKFAQQMC TALLFLATPE LSIIHCDLKP ENILLCNPKR
     SAIKIVDFGS SCQLGQRIYQ YIQSRFYRSP EVLLGMPYDL AIDMWSLGCI LVEMHTGEPL
     FSGANEVDQM NKIVEVLGIP PAHILDQAPK ARKFFEKLPD GTWSLKKTKD GKREYKPPGT
     RKLHNILGVE TGGPGGRRAG ESGHTVADYL KFKDLILRML DYDPKTRIQP YYALQHSFFK
     KTADEGTNTS NSVSTSPAME QSQSSGTTSS TSSSSGGSSG TSNSGRARSD PTHQHRHSGG
     HFAAAVQAMD CETHSPQVRQ QFPAPLGWSG TEAPTQVTVE THPVQETTFH VAPQQNALHH
     HHGNSSHHHH HHHHHHHHHG QQALGNRTRP RVYNSPTNSS STQDSMEVGH SHHSMTSLSS
     STTSSSTSSS STGNQGNQAY QNRPVAANTL DFGQNGAMDV NLTVYSNPRQ ETGIAGHPTY
     QFSANTGPAH YMTEGHLAMR QGADREESPM TGVCVQQSPV ASS
//
ID   MRE11_MOUSE             Reviewed;         706 AA.
AC   Q61216; Q62430;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Double-strand break repair protein MRE11A;
DE            Short=MmMRE11A;
DE   AltName: Full=Meiotic recombination 11 homolog 1;
DE            Short=MRE11 homolog 1;
DE   AltName: Full=Meiotic recombination 11 homolog A;
DE            Short=MRE11 homolog A;
GN   Name=Mre11a; Synonyms=Mre11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=CD-1; TISSUE=Testis;
RA   Oshiumi H., Shinohara A., Ogawa H.;
RL   Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Component of the MRN complex, which plays a central role
CC       in double-strand break (DSB) repair, DNA recombination,
CC       maintenance of telomere integrity and meiosis. The complex
CC       possesses single-strand endonuclease activity and double-strand-
CC       specific 3'-5' exonuclease activity, which are provided by MRE11A.
CC       RAD50 may be required to bind DNA ends and hold them in close
CC       proximity. This could facilitate searches for short or long
CC       regions of sequence homology in the recombining DNA templates, and
CC       may also stimulate the activity of DNA ligases and/or restrict the
CC       nuclease activity of MRE11A to prevent nucleolytic degradation
CC       past a given point. The complex may also be required for DNA
CC       damage signaling via activation of the ATM kinase. In telomeres
CC       the MRN complex may modulate t-loop formation (By similarity).
CC   -!- COFACTOR: Manganese (By similarity).
CC   -!- SUBUNIT: Component of the MRN complex composed of two heterodimers
CC       RAD50/MRE11A associated with a single NBN. Component of the BASC
CC       complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM,
CC       RAD50, MRE11A and NBN. Interacts with DCLRE1C/Artemis and
CC       DCLRE1B/Apollo (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Note=Localizes to
CC       discrete nuclear foci after treatment with genotoxic agents (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=A;
CC         IsoId=Q61216-1; Sequence=Displayed;
CC       Name=2; Synonyms=B;
CC         IsoId=Q61216-2; Sequence=VSP_003263;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the MRE11/RAD32 family.
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DR   EMBL; U58987; AAB04955.1; -; mRNA.
DR   EMBL; U60318; AAB03664.1; -; mRNA.
DR   EMBL; BC065144; AAH65144.1; -; mRNA.
DR   IPI; IPI00118853; -.
DR   IPI; IPI00283379; -.
DR   RefSeq; NP_061206.1; NM_018736.2.
DR   UniGene; Mm.149071; -.
DR   ProteinModelPortal; Q61216; -.
DR   IntAct; Q61216; 3.
DR   STRING; Q61216; -.
DR   PhosphoSite; Q61216; -.
DR   PRIDE; Q61216; -.
DR   Ensembl; ENSMUST00000034405; ENSMUSP00000034405; ENSMUSG00000031928.
DR   Ensembl; ENSMUST00000115632; ENSMUSP00000111295; ENSMUSG00000031928.
DR   GeneID; 17535; -.
DR   KEGG; mmu:17535; -.
DR   UCSC; uc009ofc.1; mouse.
DR   UCSC; uc009ofd.1; mouse.
DR   CTD; 17535; -.
DR   MGI; MGI:1100512; Mre11a.
DR   GeneTree; ENSGT00390000017288; -.
DR   HOGENOM; HBG596413; -.
DR   HOVERGEN; HBG052508; -.
DR   InParanoid; Q61216; -.
DR   OMA; GFEPFSV; -.
DR   OrthoDB; EOG46WZ82; -.
DR   PhylomeDB; Q61216; -.
DR   NextBio; 292160; -.
DR   PMAP-CutDB; Q61216; -.
DR   ArrayExpress; Q61216; -.
DR   Bgee; Q61216; -.
DR   Genevestigator; Q61216; -.
DR   GermOnline; ENSMUSG00000031928; Mus musculus.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR   GO; GO:0007126; P:meiosis; IEA:UniProtKB-KW.
DR   InterPro; IPR003701; DNA_repair.
DR   InterPro; IPR004843; Metallo-dependent_phosphatase.
DR   InterPro; IPR007281; Mre11_DNA-bd.
DR   PANTHER; PTHR10139; DNA_repair; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   Pfam; PF04152; Mre11_DNA_bind; 1.
DR   PIRSF; PIRSF000882; DSB_repair_MRE11; 1.
DR   TIGRFAMs; TIGR00583; mre11; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; DNA damage; DNA repair; Endonuclease;
KW   Exonuclease; Hydrolase; Manganese; Meiosis; Nuclease; Nucleus;
KW   Phosphoprotein.
FT   CHAIN         1    706       Double-strand break repair protein
FT                                MRE11A.
FT                                /FTId=PRO_0000138674.
FT   ACT_SITE    129    129       Proton donor (By similarity).
FT   MOD_RES      74     74       Phosphoserine (By similarity).
FT   MOD_RES     648    648       Phosphoserine (By similarity).
FT   MOD_RES     676    676       Phosphoserine (By similarity).
FT   MOD_RES     686    686       Phosphoserine (By similarity).
FT   VAR_SEQ     340    366       Missing (in isoform 2).
FT                                /FTId=VSP_003263.
SQ   SEQUENCE   706 AA;  80223 MW;  0F12F51902FC179A CRC64;
     MSPTDPLDDE DTFKILVATD IHLGFMEKDA VRGNDTFVTF DEILRLALEN EVDFILLGGD
     LFHENKPSRK TLHSCLELLR KYCMGDRPVQ FEVISDQSVN FGFSKFPWVN YQDGNLNISI
     PVFSIHGNHD DPTGADALCA LDVLSCAGFV NHFGRSMSVE KVDISPVLLQ KGSTKLALYG
     LGSIPDERLY RMFVNKKVTM LRPKEDENSW FNLFVIHQNR SKHGNTNFIP EQFLDDFIDL
     VIWGHEHECK IGPIKNEQQL FYVSQPGSSV VTSLSPGEAV KKHVGLLRIK GRKMNMQKLP
     LRTVRRFFIE DVVLANHPNL FNPDNPKVTQ AIQSFCLEKI EEMLDSAERE RLGNPQQPGK
     PLIRLRVDYS GGFEPFNVLR FSQKFVDRVA NPKDVIHFFR HREQKGKTGE EINFGMLITK
     PASEGATLRV EDLVKQYFQT AEKNVQLSLL TERGMGEAVQ EFVDKEEKDA IEELVKYQLE
     KTQRFLKERH IDALEDKIDE EVRRFRESRQ RNTNEEDDEV REAMSRARAL RSQSETSTSA
     FSAEDLSFDT SEQTANDSDD SLSAVPSRGR GRGRGRRGAR GQSSAPRGGS QRGRDTGLEI
     TTRGRSSKAT SSTSRNMSII DAFRSTRQQP SRNVAPKNYS ETIEVDDSDE DDIFPTNSRA
     DQRWSGTTSS KRMSQSQTAK GVDFESDEDD DDDPFMSSSC PRRNRR
//
ID   SNTA1_MOUSE             Reviewed;         503 AA.
AC   Q61234; Q8VEF3;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-FEB-2011, entry version 111.
DE   RecName: Full=Alpha-1-syntrophin;
DE   AltName: Full=59 kDa dystrophin-associated protein A1 acidic component 1;
DE   AltName: Full=Syntrophin-1;
GN   Name=Snta1; Synonyms=Snt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 155-161; 165-171;
RP   213-228; 247-261 AND 271-307.
RC   TISSUE=Muscle;
RX   MEDLINE=94000819; PubMed=7691103; DOI=10.1016/0896-6273(93)90157-M;
RA   Adams M.E., Butler M.H., Dwyer T.M., Peters M.F., Murnane A.A.,
RA   Froehner S.C.;
RT   "Two forms of mouse syntrophin, a 58 kDa dystrophin-associated
RT   protein, differ in primary structure and tissue distribution.";
RL   Neuron 11:531-540(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 7-16, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   INTERACTION WITH SNTB1; SNTB2; DMD; SGCA AND SGCG.
RX   MEDLINE=96032613; PubMed=7547961; DOI=10.1021/bi00038a014;
RA   Madhavan R., Jarrett H.W.;
RT   "Interactions between dystrophin glycoprotein complex proteins.";
RL   Biochemistry 34:12204-12209(1995).
RN   [5]
RP   INTERACTION WITH NOS1.
RX   MEDLINE=96193770; PubMed=8625413; DOI=10.1016/S0092-8674(00)81053-3;
RA   Brenman J.E., Chao D.S., Gee S.H., McGee A.W., Craven S.E.,
RA   Santillano D.R., Wu Z., Huang F., Xia H., Peters M.F., Froehner S.C.,
RA   Bredt D.S.;
RT   "Interaction of nitric oxide synthase with the postsynaptic density
RT   protein PSD-95 and alpha1-syntrophin mediated by PDZ domains.";
RL   Cell 84:757-767(1996).
RN   [6]
RP   INTERACTION WITH CALMODULIN.
RX   MEDLINE=97178814; PubMed=9063877; DOI=10.1021/bi962452n;
RA   Newbell B.J., Anderson J.T., Jarrett H.W.;
RT   "Ca2+-calmodulin binding to mouse alpha1 syntrophin: syntrophin is
RT   also a Ca2+-binding protein.";
RL   Biochemistry 36:1295-1305(1997).
RN   [7]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH DMD;
RP   DTNA AND UTRN.
RX   MEDLINE=97362062; PubMed=9214383; DOI=10.1083/jcb.138.1.81;
RA   Peters M.F., Adams M.E., Froehner S.C.;
RT   "Differential association of syntrophin pairs with the dystrophin
RT   complex.";
RL   J. Cell Biol. 138:81-93(1997).
RN   [8]
RP   INTERACTION WITH SCN4A AND SCN5A.
RX   MEDLINE=98075111; PubMed=9412493;
RA   Gee S.H., Madhavan R., Levinson S.R., Caldwell J.H., Sealock R.,
RA   Froehner S.C.;
RT   "Interaction of muscle and brain sodium channels with multiple members
RT   of the syntrophin family of dystrophin-associated proteins.";
RL   J. Neurosci. 18:128-137(1998).
RN   [9]
RP   ASSOCIATION WITH PHOSPHATIDYLINOSITOL 4,5-BIPHOSPHATE.
RX   MEDLINE=99238336; PubMed=10220348; DOI=10.1021/bi982564+;
RA   Chockalingam P.S., Gee S.H., Jarrett H.W.;
RT   "Pleckstrin homology domain 1 of mouse alpha 1-syntrophin binds
RT   phosphatidylinositol 4,5-bisphosphate.";
RL   Biochemistry 38:5596-5602(1999).
RN   [10]
RP   PHOSPHORYLATION BY CAM-KINASE II.
RX   MEDLINE=99454625; PubMed=10525145; DOI=10.1016/S0167-4838(99)00193-4;
RA   Madhavan R., Jarrett H.W.;
RT   "Phosphorylation of dystrophin and alpha-syntrophin by Ca(2+)-
RT   calmodulin dependent protein kinase II.";
RL   Biochim. Biophys. Acta 1434:260-274(1999).
RN   [11]
RP   OLIGOMERIZATION.
RX   MEDLINE=20374567; PubMed=10913299; DOI=10.1021/bi0000824;
RA   Oak S.A., Jarrett H.W.;
RT   "Oligomerization of mouse alpha 1-syntrophin and self-association of
RT   its pleckstrin homology domain 1 containing sequences.";
RL   Biochemistry 39:8870-8877(2000).
RN   [12]
RP   INTERACTION WITH GRB2.
RX   MEDLINE=21435681; PubMed=11551227; DOI=10.1021/bi010490n;
RA   Oak S.A., Russo K., Petrucci T.C., Jarrett H.W.;
RT   "Mouse alpha1-syntrophin binding to Grb2: further evidence of a role
RT   for syntrophin in cell signaling.";
RL   Biochemistry 40:11270-11278(2001).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183 AND SER-187, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Adapter protein that binds to and probably organizes the
CC       subcellular localization of a variety of membrane proteins. May
CC       link various receptors to the actin cytoskeleton and the
CC       extracellular matrix via the dystrophin glycoprotein complex.
CC       Plays an important role in synapse formation and in the
CC       organization of UTRN and acetylcholine receptors at the
CC       neuromuscular synapse. Binds to phosphatidylinositol 4,5-
CC       biphosphate.
CC   -!- SUBUNIT: Monomer and homodimer. Interacts with MAPK12, TGFA, GA
CC       and F-actin (By similarity). Interacts with the other members of
CC       the syntrophin family: SNTB1 and SNTB2; with dystrophin protein
CC       DMD and related proteins DTNA and UTRN; SGCG and SGCA of the
CC       dystrophin glycoprotein complex; NOS1; GRB2; calmodulin and the
CC       sodium channel proteins SCN4A and SCN5A.
CC   -!- INTERACTION:
CC       P11531:Dmd; NbExp=1; IntAct=EBI-295952, EBI-295928;
CC       P29476:Nos1 (xeno); NbExp=1; IntAct=EBI-295952, EBI-349460;
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Peripheral
CC       membrane protein; Cytoplasmic side. Cell junction. Cytoplasm,
CC       cytoskeleton. Note=In skeletal muscle, it localizes at the
CC       cytoplasmic side of the sarcolemmal membrane and at neuromuscular
CC       junctions.
CC   -!- TISSUE SPECIFICITY: High expression in skeletal muscle. Expressed
CC       at intermediate level in heart, kidney and brain, and at low level
CC       in intestine, liver, lung and testis.
CC   -!- DOMAIN: The PH 1 domain mediates the oligomerization in a calcium
CC       dependent manner, and the association with the
CC       phosphatidylinositol 4,5-biphosphate.
CC   -!- DOMAIN: The PDZ domain binds to the last three or four amino acids
CC       of ion channels and receptor proteins. The association with
CC       dystrophin or related proteins probably leaves the PDZ domain
CC       available to recruit proteins to the membrane.
CC   -!- DOMAIN: The SU domain binds calmodulin in a calcium-dependent
CC       manner.
CC   -!- PTM: Phosphorylated by CaM-kinase II. Phosphorylation may inhibit
CC       the interaction with DMD.
CC   -!- SIMILARITY: Belongs to the syntrophin family.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -!- SIMILARITY: Contains 1 SU (syntrophin unique) domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; U00677; AAC52119.1; -; mRNA.
DR   EMBL; BC018546; AAH18546.1; -; mRNA.
DR   IPI; IPI00267848; -.
DR   PIR; I84771; I84771.
DR   UniGene; Mm.1541; -.
DR   PDB; 1QAV; X-ray; 1.90 A; A=77-164.
DR   PDB; 1Z86; NMR; -; A=79-165.
DR   PDB; 1Z87; NMR; -; A=2-264.
DR   PDB; 2ADZ; NMR; -; A=2-264.
DR   PDB; 2PDZ; NMR; -; A=79-164.
DR   PDBsum; 1QAV; -.
DR   PDBsum; 1Z86; -.
DR   PDBsum; 1Z87; -.
DR   PDBsum; 2ADZ; -.
DR   PDBsum; 2PDZ; -.
DR   ProteinModelPortal; Q61234; -.
DR   SMR; Q61234; 2-264.
DR   DIP; DIP-32898N; -.
DR   IntAct; Q61234; 5.
DR   MINT; MINT-99385; -.
DR   STRING; Q61234; -.
DR   PhosphoSite; Q61234; -.
DR   PRIDE; Q61234; -.
DR   Ensembl; ENSMUST00000028991; ENSMUSP00000028991; ENSMUSG00000027488.
DR   UCSC; uc008njd.1; mouse.
DR   MGI; MGI:101772; Snta1.
DR   GeneTree; ENSGT00550000074581; -.
DR   HOGENOM; HBG314224; -.
DR   HOVERGEN; HBG054204; -.
DR   InParanoid; Q61234; -.
DR   OMA; MKEISPY; -.
DR   ArrayExpress; Q61234; -.
DR   Bgee; Q61234; -.
DR   CleanEx; MM_SNTA1; -.
DR   Genevestigator; Q61234; -.
DR   GermOnline; ENSMUSG00000027488; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR   GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR015482; Syntrophin.
DR   PANTHER; PTHR10554; Syntrophin; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00233; PH; 2.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Calcium; Calmodulin-binding;
KW   Cell junction; Cell membrane; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Membrane; Phosphoprotein; Repeat.
FT   CHAIN         1    503       Alpha-1-syntrophin.
FT                                /FTId=PRO_0000184007.
FT   DOMAIN        6    263       PH 1.
FT   DOMAIN       81    164       PDZ.
FT   DOMAIN      287    399       PH 2.
FT   DOMAIN      447    503       SU.
FT   REGION      481    503       Calmodulin-binding.
FT   MOD_RES     183    183       Phosphoserine.
FT   MOD_RES     187    187       Phosphoserine.
FT   CONFLICT     16     16       R -> C (in Ref. 2; AAH18546).
FT   CONFLICT    341    344       Missing (in Ref. 2; AAH18546).
FT   CONFLICT    405    405       I -> V (in Ref. 2; AAH18546).
FT   STRAND        9     16
FT   STRAND       28     35
FT   STRAND       37     43
FT   STRAND       63     67
FT   STRAND       80     85
FT   TURN         88     90
FT   STRAND       94     99
FT   HELIX       100    102
FT   STRAND      104    111
FT   HELIX       116    119
FT   STRAND      127    132
FT   HELIX       142    150
FT   STRAND      154    162
FT   STRAND      169    171
FT   STRAND      180    182
FT   STRAND      189    193
FT   STRAND      195    197
FT   STRAND      207    219
FT   STRAND      225    227
FT   STRAND      229    234
FT   TURN        235    238
FT   STRAND      239    244
FT   HELIX       248    262
SQ   SEQUENCE   503 AA;  53665 MW;  161BA76CAF50AE96 CRC64;
     MASGRRAPRT GLLELRCGAG SGAGGERWQR VLLSLAEDAL TVSPADGEPG PEPEPAQLNG
     AAEPGAAPPQ LPEALLLQRR RVTVRKADAG GLGISIKGGR ENKMPILISK IFKGLAADQT
     EALFVGDAIL SVNGEDLSSA THDEAVQALK KTGKEVVLEV KYMKEVSPYF KNSAGGTSVG
     WDSPPASPLQ RQPSSPGPQP RNLSEAKHVS LKMAYVSRRC TPTDPEPRYL EICAADGQDA
     VFLRAKDEAS ARSWAGAIQA QIGTFIPWVK DELQALLTAT GTAGSQDIKQ IGWLTEQLPS
     GGTAPTLALL TEKELLFYCS LPQSREALSR PTRTAPLIAT SSAHRLVHSG PSKGSVPYDA
     ELSFALRTGT RHGVDTHLFS VESPQELAAW TRQLVDGCHR AAEGIQEVST ACTWNGRPCS
     LSVHIDKGFT LWAAEPGAAR AMLLRQPFEK LQMSSDDGTS LLFLDFGGAE GEIQLDLHSC
     PKTMVFIIHS FLSAKVTRLG LLA
//
ID   SNTB2_MOUSE             Reviewed;         520 AA.
AC   Q61235;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 2.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Beta-2-syntrophin;
DE   AltName: Full=59 kDa dystrophin-associated protein A1 basic component 2;
DE   AltName: Full=Syntrophin-3;
DE            Short=SNT3;
DE   AltName: Full=Syntrophin-like;
DE            Short=SNTL;
GN   Name=Sntb2; Synonyms=Snt2b2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Diaphragm;
RX   MEDLINE=96029685; PubMed=7592771; DOI=10.1074/jbc.270.43.25859;
RA   Adams M.E., Dwyer T.M., Dowler L.L., White R.A., Froehner S.C.;
RT   "Mouse alpha 1- and beta 2-syntrophin gene structure, chromosome
RT   localization, and homology with a discs large domain.";
RL   J. Biol. Chem. 270:25859-25865(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 91-520.
RC   TISSUE=Diaphragm;
RX   MEDLINE=94000819; PubMed=7691103; DOI=10.1016/0896-6273(93)90157-M;
RA   Adams M.E., Butler M.H., Dwyer T.M., Peters M.F., Murnane A.A.,
RA   Froehner S.C.;
RT   "Two forms of mouse syntrophin, a 58 kDa dystrophin-associated
RT   protein, differ in primary structure and tissue distribution.";
RL   Neuron 11:531-540(1993).
RN   [3]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH UTRN.
RX   MEDLINE=97362062; PubMed=9214383; DOI=10.1083/jcb.138.1.81;
RA   Peters M.F., Adams M.E., Froehner S.C.;
RT   "Differential association of syntrophin pairs with the dystrophin
RT   complex.";
RL   J. Cell Biol. 138:81-93(1997).
RN   [4]
RP   INTERACTION WITH SCN4A AND SCN5A.
RX   MEDLINE=98075111; PubMed=9412493;
RA   Gee S.H., Madhavan R., Levinson S.R., Caldwell J.H., Sealock R.,
RA   Froehner S.C.;
RT   "Interaction of muscle and brain sodium channels with multiple members
RT   of the syntrophin family of dystrophin-associated proteins.";
RL   J. Neurosci. 18:128-137(1998).
RN   [5]
RP   INTERACTION WITH SAST; MAST205; MICROTUBULES AND
RP   MICROTUBULE-ASSOCIATED PROTEINS.
RX   MEDLINE=99338326; PubMed=10404183; DOI=10.1038/10165;
RA   Lumeng C., Phelps S., Crawford G.E., Walden P.D., Barald K.,
RA   Chamberlain J.S.;
RT   "Interactions between beta 2-syntrophin and a family of microtubule-
RT   associated serine/threonine kinases.";
RL   Nat. Neurosci. 2:611-617(1999).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-90, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Adapter protein that binds to and probably organizes the
CC       subcellular localization of a variety of membrane proteins. May
CC       link various receptors to the actin cytoskeleton and the
CC       dystrophin glycoprotein complex. May play a role in the regulation
CC       of secretory granules via its interaction with PTPRN (By
CC       similarity).
CC   -!- SUBUNIT: Monomer and homodimer (Probable). Interacts with the
CC       dystrophin protein DMD and related protein DTNA; and with the
CC       other members of the syntrophin family: SNTA1 and SNTB1. Interacts
CC       with the neuroregulin receptor ERBB4. Interacts with PTPRN when
CC       phosphorylated, protecting PTPRN from protein cleavage by CAPN1.
CC       Dephosphorylation upon insulin stimulation disrupts the
CC       interaction with PTPRN and results in the cleavage of PTPRN (By
CC       similarity). Interacts with the sodium channel proteins SCN4A and
CC       SCN5A. Interacts with SAST, MAST205, microtubules and microtubule-
CC       associated proteins. Interacts with the dystrophin related protein
CC       UTRN.
CC   -!- INTERACTION:
CC       Q9R1L5:Mast1; NbExp=3; IntAct=EBI-295974, EBI-491771;
CC       Q60592:Mast2; NbExp=3; IntAct=EBI-295974, EBI-493888;
CC   -!- SUBCELLULAR LOCATION: Membrane. Cytoplasmic vesicle, secretory
CC       vesicle membrane; Peripheral membrane protein. Cell junction (By
CC       similarity). Cytoplasm, cytoskeleton. Note=Membrane-associated. In
CC       insulinoma cell line, it is enriched in secretory granules (By
CC       similarity). In muscle, it is exclusively localized at the
CC       neuromuscular junction.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at high levels in the
CC       testis.
CC   -!- DOMAIN: The PH 1 domain mediates the oligomerization in a calcium
CC       dependent manner (By similarity).
CC   -!- DOMAIN: The PDZ domain binds to the last three or four amino acids
CC       of ion channels and receptor proteins. The association with
CC       dystrophin or related proteins probably leaves the PDZ domain
CC       available to recruit proteins to the membrane (By similarity).
CC   -!- DOMAIN: The SU domain binds calmodulin in a calcium-dependent
CC       manner (By similarity).
CC   -!- PTM: Phosphorylated. Partially dephosphorylated upon insulin
CC       stimulation (By similarity).
CC   -!- SIMILARITY: Belongs to the syntrophin family.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -!- SIMILARITY: Contains 1 SU (syntrophin unique) domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; U00678; AAC53060.1; -; mRNA.
DR   IPI; IPI00118895; -.
DR   RefSeq; NP_033255.1; NM_009229.4.
DR   UniGene; Mm.30228; -.
DR   ProteinModelPortal; Q61235; -.
DR   SMR; Q61235; 2-281.
DR   IntAct; Q61235; 12.
DR   MINT; MINT-99343; -.
DR   STRING; Q61235; -.
DR   PhosphoSite; Q61235; -.
DR   PRIDE; Q61235; -.
DR   Ensembl; ENSMUST00000047425; ENSMUSP00000037324; ENSMUSG00000041308.
DR   GeneID; 20650; -.
DR   KEGG; mmu:20650; -.
DR   UCSC; uc009ngt.1; mouse.
DR   CTD; 20650; -.
DR   MGI; MGI:101771; Sntb2.
DR   GeneTree; ENSGT00550000074581; -.
DR   HOGENOM; HBG314224; -.
DR   HOVERGEN; HBG054204; -.
DR   InParanoid; Q61235; -.
DR   OMA; SSWTRIL; -.
DR   OrthoDB; EOG4VX257; -.
DR   PhylomeDB; Q61235; -.
DR   NextBio; 299071; -.
DR   ArrayExpress; Q61235; -.
DR   Bgee; Q61235; -.
DR   CleanEx; MM_SNTB2; -.
DR   Genevestigator; Q61235; -.
DR   GermOnline; ENSMUSG00000041308; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR015482; Syntrophin.
DR   PANTHER; PTHR10554; Syntrophin; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00233; PH; 2.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Calcium; Calmodulin-binding; Cell junction; Cytoplasm;
KW   Cytoplasmic vesicle; Cytoskeleton; Membrane; Microtubule;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1    520       Beta-2-syntrophin.
FT                                /FTId=PRO_0000184012.
FT   DOMAIN       95    178       PDZ.
FT   DOMAIN      143    280       PH 1.
FT   DOMAIN      305    417       PH 2.
FT   DOMAIN      464    520       SU.
FT   REGION      498    520       Calmodulin-binding (By similarity).
FT   COMPBIAS     57     60       Poly-Gly.
FT   MOD_RES      75     75       Phosphoserine.
FT   MOD_RES      90     90       Phosphoserine.
FT   MOD_RES     181    181       Phosphothreonine (By similarity).
FT   MOD_RES     202    202       Phosphoserine (By similarity).
FT   MOD_RES     213    213       Phosphoserine (By similarity).
FT   MOD_RES     373    373       Phosphoserine (By similarity).
FT   MOD_RES     375    375       Phosphoserine (By similarity).
SQ   SEQUENCE   520 AA;  56382 MW;  9F6886837C1CDB20 CRC64;
     MAVWTRATKA GLVELLLRER WVRVVAELSG ESLSLTGDAA AVEPEPPAAA FNGLPNGGGG
     ESLPGSPNRG LGPPSPPAPP RGPAGEASAS PPVRRVRVVK QEAGGLGISI KGGRENRMPI
     LISKIFPGLA ADQSRALRLG DAILSVNGTD LRQATHDQAV QALKRAGKEV LLEVKFIREV
     TPYIKKPSLV SDLPWEGASP QSPSFSGSED SGSPKHQNTT KDRKVIPLKM CFAARNLSMP
     DLENRLIELH SPDSRNTLIL RCKDTATAHS WFVAIHTNIM ALLPQVLAEL NAMLGATSTA
     GGSKEVKHIA WLAEQAKLDG GRQQWRPVLM AVTEKDLLLY DCMPWTRDAW ASPCHSYPLV
     ATRLVHSGSG CRSPSLGSDL TFATRTGSRQ GIEMHLFRVE THRDLSTWTR ILVQGCHAAA
     ELIKEVSLGC TLSGQEVRFT VHYEHGFTIT RDNGGASSIL YRYPFERLKM SADDGIRNLY
     LDFGGPEGEL TMDLHSCPKP IVFVLHTFLS AKVTRMGLLV
//
ID   ACV1B_MOUSE             Reviewed;         505 AA.
AC   Q61271;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Activin receptor type-1B;
DE            EC=2.7.11.30;
DE   AltName: Full=Activin receptor type IB;
DE            Short=ACTR-IB;
DE   AltName: Full=Activin receptor-like kinase 4;
DE            Short=ALK-4;
DE   AltName: Full=Serine/threonine-protein kinase receptor R2;
DE            Short=SKR2;
DE   Flags: Precursor;
GN   Name=Acvr1b; Synonyms=Alk4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=NIH Swiss; TISSUE=Placenta;
RX   MEDLINE=96076132; PubMed=7577669; DOI=10.1016/0925-4773(95)00395-H;
RA   Verschuern K., Dewulf N., Goumans M.J., Lonnoy O., Freijen A.,
RA   Grimsby S., Vande Spiegle K., ten Dijke P., Moren A.,
RA   Vanscheeuwijck P., Heldin C.H., Miyazono K., Mummery C.,
RA   Van Den Eijnden-Van Raaij J., Huylebroeck D.;
RT   "Expression of type I and type IB receptors for activin in
RT   midgestation mouse embryos suggests distinct functions in
RT   organogensis.";
RL   Mech. Dev. 52:109-123(1995).
RN   [2]
RP   FUNCTION, AND INTERACTION WITH TDP2.
RX   PubMed=18039968; DOI=10.1242/dev.000026;
RA   Esguerra C.V., Nelles L., Vermeire L., Ibrahimi A., Crawford A.D.,
RA   Derua R., Janssens E., Waelkens E., Carmeliet P., Collen D.,
RA   Huylebroeck D.;
RT   "Ttrap is an essential modulator of Smad3-dependent Nodal signaling
RT   during zebrafish gastrulation and left-right axis determination.";
RL   Development 134:4381-4393(2007).
CC   -!- FUNCTION: On ligand binding, forms a receptor complex consisting
CC       of two type II and two type I transmembrane serine/threonine
CC       kinases. Type II receptors phosphorylate and activate type I
CC       receptors which autophosphorylate, then bind and activate SMAD
CC       transcriptional regulators. Phosphorylates TDP2.
CC   -!- CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-
CC       protein] phosphate.
CC   -!- COFACTOR: Magnesium or manganese (By similarity).
CC   -!- SUBUNIT: Interacts with AIP1. Part of a complex consisting of
CC       AIP1, ACVR2A, ACVR1B and SMAD3 (By similarity). Interacts with
CC       TDP2.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- PTM: Autophosphorylated (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily.
CC   -!- SIMILARITY: Contains 1 GS domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; Z31663; CAA83483.1; -; mRNA.
DR   IPI; IPI00119012; -.
DR   RefSeq; NP_031421.1; NM_007395.3.
DR   UniGene; Mm.308467; -.
DR   ProteinModelPortal; Q61271; -.
DR   SMR; Q61271; 31-106, 202-501.
DR   MINT; MINT-2842316; -.
DR   STRING; Q61271; -.
DR   PRIDE; Q61271; -.
DR   Ensembl; ENSMUST00000000544; ENSMUSP00000000544; ENSMUSG00000000532.
DR   GeneID; 11479; -.
DR   KEGG; mmu:11479; -.
DR   UCSC; uc007xsr.1; mouse.
DR   CTD; 11479; -.
DR   MGI; MGI:1338944; Acvr1b.
DR   GeneTree; ENSGT00560000076615; -.
DR   HOGENOM; HBG314718; -.
DR   HOVERGEN; HBG054502; -.
DR   InParanoid; Q61271; -.
DR   OMA; HHQRVYH; -.
DR   OrthoDB; EOG4FJ88P; -.
DR   PhylomeDB; Q61271; -.
DR   BRENDA; 2.7.11.30; 244.
DR   NextBio; 278824; -.
DR   ArrayExpress; Q61271; -.
DR   Bgee; Q61271; -.
DR   CleanEx; MM_ACVR1B; -.
DR   Genevestigator; Q61271; -.
DR   GermOnline; ENSMUSG00000000532; Mus musculus.
DR   GO; GO:0048185; F:activin binding; IPI:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007166; P:cell surface receptor linked signaling pathway; TAS:MGI.
DR   GO; GO:0001942; P:hair follicle development; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:UniProtKB.
DR   InterPro; IPR000472; Activin_rcpt.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR003605; TGF_beta_rcpt_GS.
DR   Pfam; PF01064; Activin_recp; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF08515; TGF_beta_GS; 1.
DR   SMART; SM00467; GS; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51256; GS; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Glycoprotein; Kinase; Magnesium; Manganese; Membrane;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Receptor;
KW   Serine/threonine-protein kinase; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     23       Potential.
FT   CHAIN        24    505       Activin receptor type-1B.
FT                                /FTId=PRO_0000024418.
FT   TOPO_DOM     24    126       Extracellular (Potential).
FT   TRANSMEM    127    149       Helical; (Potential).
FT   TOPO_DOM    150    505       Cytoplasmic (Potential).
FT   DOMAIN      177    206       GS.
FT   DOMAIN      207    497       Protein kinase.
FT   NP_BIND     213    221       ATP (By similarity).
FT   ACT_SITE    335    335       Proton acceptor (By similarity).
FT   BINDING     234    234       ATP (By similarity).
FT   MOD_RES     380    380       Phosphotyrosine (By similarity).
FT   CARBOHYD     43     43       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   505 AA;  56700 MW;  56E9EEF1607A2517 CRC64;
     MAESAGASSF FPLVVLLLAG SGGSGPRGIQ ALLCACTSCL QTNYTCETDG ACMVSIFNLD
     GVEHHVRTCI PKVELVPAGK PFYCLSSEDL RNTHCCYIDF CNKIDLRVPS GHLKEPAHPS
     MWGPVELVGI IAGPVFLLFL IIIIVFLVIN YHQRVYHNRQ RLDMEDPSCE MCLSKDKTLQ
     DLVYDLSTSG SGSGLPLFVQ RTVARTIVLQ EIIGKGRFGE VWRGRWRGGD VAVKIFSSRE
     ERSWFREAEI YQTVMLRHEN ILGFIAADNK DNGTWTQLWL VSDYHEHGSL FDYLNRYTVT
     IEGMIKLALS AASGLAHLHM EIVGTQGKPG IAHRDLKSKN ILVKKNGMCA IADLGLAVRH
     DAVTDTIDIA PNQRVGTKRY MAPEVLDETI NMKHFDSFKC ADIYALGLVY WEIARRCNSG
     GVHEDYQLPY YDLVPSDPSI EEMRKVVCDQ KLRPNVPNWW QSYEALRVMG KMMRECWYAN
     GAARLTALRI KKTLSQLSVQ EDVKI
//
ID   HTF4_MOUSE              Reviewed;         706 AA.
AC   Q61286;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Transcription factor 12;
DE            Short=TCF-12;
DE   AltName: Full=Class A helix-loop-helix transcription factor ME1;
DE   AltName: Full=DNA-binding protein HTF4;
DE   AltName: Full=E-box-binding protein;
DE   AltName: Full=Transcription factor HTF-4;
GN   Name=Tcf12; Synonyms=Alf1, Meb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALF1A AND ALF1B).
RX   MEDLINE=92334344; PubMed=1321336;
RA   Nielsen A.L., Pallisgaard N., Pedersen F.S., Joergensen P.;
RT   "Murine helix-loop-helix transcriptional activator proteins binding to
RT   the E-box motif of the Akv murine leukemia virus enhancer identified
RT   by cDNA cloning.";
RL   Mol. Cell. Biol. 12:3449-3459(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Cerebellum;
RX   MEDLINE=94084260; PubMed=8261111;
RX   DOI=10.1111/j.1460-9568.1993.tb00498.x;
RA   Neuman T., Keen A., Knapik E., Shain D., Ross M., Nornes H.O.,
RA   Zuber M.X.;
RT   "ME1 and GE1: basic helix-loop-helix transcription factors expressed
RT   at high levels in the developing nervous system and in
RT   morphogenetically active regions.";
RL   Eur. J. Neurosci. 5:311-318(1993).
RN   [3]
RP   INTERACTION WITH PTF1A.
RX   MEDLINE=21570228; PubMed=11562365; DOI=10.1074/jbc.M106264200;
RA   Rose S.D., Swift G.H., Peyton M.J., Hammer R.E., MacDonald R.J.;
RT   "The role of PTF1-P48 in pancreatic acinar gene expression.";
RL   J. Biol. Chem. 276:44018-44026(2001).
CC   -!- FUNCTION: Binds specifically to oligomers of E-box motifs. May
CC       play important roles during development of the nervous system as
CC       well as in other organ systems.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another
CC       bHLH protein. Forms homo- or heterooligomers with myogenin, E12
CC       and ITF2 proteins and RUNX1T1 (By similarity). Interacts with
CC       PTF1A.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=ALF1B; Synonyms=ME1A;
CC         IsoId=Q61286-1; Sequence=Displayed;
CC       Name=ALF1A; Synonyms=ME1B;
CC         IsoId=Q61286-2; Sequence=VSP_002105;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- DEVELOPMENTAL STAGE: Abundantly expressed during development of
CC       the central nervous system, in particular in proliferating
CC       neuroblasts and in cells at the initial stages of differentiation.
CC       Also expressed at high levels in morphogenetically active regions
CC       such as limb buds, somites and mesonephric tubules. Expression
CC       decreases once cellular differentiation is over.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 basic helix-loop-helix (bHLH) domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; X64840; CAA46052.1; -; mRNA.
DR   EMBL; M97635; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; M97636; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00119042; -.
DR   IPI; IPI00230668; -.
DR   PIR; C45020; C45020.
DR   PIR; S19958; S19958.
DR   RefSeq; NP_035674.2; NM_011544.3.
DR   UniGene; Mm.171615; -.
DR   UniGene; Mm.480117; -.
DR   ProteinModelPortal; Q61286; -.
DR   SMR; Q61286; 602-661.
DR   DIP; DIP-42840N; -.
DR   MINT; MINT-2567849; -.
DR   STRING; Q61286; -.
DR   PhosphoSite; Q61286; -.
DR   PRIDE; Q61286; -.
DR   Ensembl; ENSMUST00000034755; ENSMUSP00000034755; ENSMUSG00000032228.
DR   Ensembl; ENSMUST00000113549; ENSMUSP00000109178; ENSMUSG00000032228.
DR   GeneID; 21406; -.
DR   KEGG; mmu:21406; -.
DR   UCSC; uc009qpf.1; mouse.
DR   UCSC; uc009qpi.1; mouse.
DR   CTD; 21406; -.
DR   MGI; MGI:101877; Tcf12.
DR   GeneTree; ENSGT00510000046438; -.
DR   HOGENOM; HBG713543; -.
DR   HOVERGEN; HBG003854; -.
DR   InParanoid; Q61286; -.
DR   OrthoDB; EOG4K3KVX; -.
DR   ArrayExpress; Q61286; -.
DR   Bgee; Q61286; -.
DR   CleanEx; MM_TCF12; -.
DR   Genevestigator; Q61286; -.
DR   GermOnline; ENSMUSG00000032228; Mus musculus.
DR   GO; GO:0005667; C:transcription factor complex; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0016563; F:transcription activator activity; IDA:MGI.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR011598; HLH_DNA-bd.
DR   InterPro; IPR001092; HLH_DNA-bd_dom.
DR   Gene3D; G3DSA:4.10.280.10; HLH_DNA_bd; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; HLH_basic; 1.
DR   PROSITE; PS50888; HLH; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Developmental protein; DNA-binding; Nucleus;
KW   Phosphoprotein; Transcription; Transcription regulation.
FT   CHAIN         1    706       Transcription factor 12.
FT                                /FTId=PRO_0000127230.
FT   DOMAIN      119    140       Leucine-zipper.
FT   DOMAIN      614    655       Helix-loop-helix motif.
FT   DNA_BIND    601    613       Basic motif.
FT   REGION      656    679       Class A specific domain.
FT   MOTIF       181    188       Nuclear localization signal (Potential).
FT   MOD_RES      44     44       Phosphoserine (By similarity).
FT   MOD_RES      47     47       Phosphoserine (By similarity).
FT   MOD_RES      67     67       Phosphoserine (By similarity).
FT   MOD_RES     305    305       Phosphoserine (By similarity).
FT   MOD_RES     313    313       Phosphothreonine (By similarity).
FT   MOD_RES     333    333       Phosphoserine (By similarity).
FT   MOD_RES     581    581       Phosphothreonine (By similarity).
FT   VAR_SEQ     397    420       Missing (in isoform ALF1A).
FT                                /FTId=VSP_002105.
FT   CONFLICT    416    416       K -> E (in Ref. 2; M97635).
FT   CONFLICT    537    537       V -> F (in Ref. 2; M97635/M97636).
SQ   SEQUENCE   706 AA;  75784 MW;  4394FE8078A7F68C CRC64;
     MNPQQQRMAA IGTDKELSDL LDFSAMFSPP VNSGKTRPTT LGSSQFSGSG MDERGGTTSW
     GTSGQPSPSY DSSRGFTDSP HYSDHLNDSR LGTHEGLSPT PFMNSNLIGK TSERGSFSLY
     SRDSGLSGCQ SSLLRQDLGL GSPAQLSSSG KPGTPYYSFS ATSSRRRPLH DSVALDPLQA
     KKVRKVPPGL PSSVYAPSPN SDDFNRESPS YPSPKPPTSM FASTFFMQDG THSSSDLWSS
     SNGMSQPGFG GILGTSTSHM SQSSSYGSLH SHDRLSYPPH SVSPTDINTS LPPMSSFHRG
     STSSSPYVAA SHTPPINGSD SILGTRGNAA GSSQTGDALG KALASIYSPD HTSSSFPSNP
     STPVGSPSPL TGTSQWPRAG GQAPSSPSYE NSLHSLKNRV EQQLHEHLQD AMSFLKDVCE
     QSRMEDRLDR LDDAIHVLRN HAVGPSTSLP TSHSDIHSLL GPSHNASIGN LNSNYGGSSL
     VTNSRSASMV GTHREDSVSL NGNHSVLSST VAASNTELNH KTPENFRGGV QNQSGSVVPT
     EIKTENKEKD ENLHEPPSSD DMKSDDESSQ KDIKVSSRGR TSSTNEDEDL NPEQKIEREK
     ERRMANNARE RLRVRDINEA FKELGRMCQL HLKSEKPQTK LLILHQAVAV ILSLEQQVRE
     RNLNPKAACL KRREEEKVSA ASAEPPSTLP GAHPGLSEST NPMGHL
//
ID   CTNA2_MOUSE             Reviewed;         953 AA.
AC   Q61301; Q3TY37; Q61300; Q6AXD1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Catenin alpha-2;
DE   AltName: Full=Alpha N-catenin;
GN   Name=Ctnna2; Synonyms=Catna2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   MEDLINE=94229360; PubMed=8174789; DOI=10.1006/dbio.1994.1124;
RA   Uchida N., Shimamura K., Miyatani S., Copeland N.G., Gilbert D.J.,
RA   Jenkins N.A., Takeichi M.;
RT   "Mouse alpha N-catenin: two isoforms, specific expression in the
RT   nervous system, and chromosomal localization of the gene.";
RL   Dev. Biol. 163:75-85(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=12089526; DOI=10.1038/ng908;
RA   Park C., Falls W., Finger J.H., Longo-Guess C.M., Ackerman S.L.;
RT   "Deletion in Catna2, encoding alpha N-catenin, causes cerebellar and
RT   hippocampal lamination defects and impaired startle modulation.";
RL   Nat. Genet. 31:279-284(2002).
RN   [5]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=12123610; DOI=10.1016/S0896-6273(02)00748-1;
RA   Togashi H., Abe K., Mizoguchi A., Takaoka K., Chisaka O., Takeichi M.;
RT   "Cadherin regulates dendritic spine morphogenesis.";
RL   Neuron 35:77-89(2002).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262; SER-640 AND
RP   SER-901, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=15034585; DOI=10.1038/nn1212;
RA   Abe K., Chisaka O., Van Roy F., Takeichi M.;
RT   "Stability of dendritic spines and synaptic contacts is controlled by
RT   alpha N-catenin.";
RL   Nat. Neurosci. 7:357-363(2004).
RN   [8]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16185771; DOI=10.1016/j.devbrainres.2005.08.004;
RA   Ajioka I., Nakajima K.;
RT   "Switching of alpha-catenin from alphaE-catenin in the cortical
RT   ventricular zone to alphaN-catenin II in the intermediate zone.";
RL   Brain Res. Dev. Brain Res. 160:106-111(2005).
RN   [9]
RP   DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX   PubMed=16457793; DOI=10.1016/j.brainres.2005.12.057;
RA   Stocker A.M., Chenn A.;
RT   "Differential expression of alpha-E-catenin and alpha-N-catenin in the
RT   developing cerebral cortex.";
RL   Brain Res. 1073:151-158(2006).
RN   [10]
RP   DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX   PubMed=16691566; DOI=10.1002/dvdy.20841;
RA   Uemura M., Takeichi M.;
RT   "Alpha N-catenin deficiency causes defects in axon migration and
RT   nuclear organization in restricted regions of the mouse brain.";
RL   Dev. Dyn. 235:2559-2566(2006).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, PHOSPHORYLATION AT SER-6;
RP   SER-640; SER-654 AND THR-657, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-653 AND SER-654, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5; THR-261; SER-640 AND
RP   SER-901, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-654 AND THR-657, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-654, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: May function as a linker between cadherin adhesion
CC       receptors and the cytoskeleton to regulate cell-cell adhesion and
CC       differentiation in the nervous system. Regulates morphological
CC       plasticity of synapses and cerebellar and hippocampal lamination
CC       during development. Functions in the control of startle
CC       modulation.
CC   -!- SUBUNIT: Interacts with ZNF639 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity). Cell junction, adherens junction.
CC       Cell membrane; Peripheral membrane protein; Cytoplasmic side (By
CC       similarity). Cell projection, axon.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=alpha N-catenin II;
CC         IsoId=Q61301-1; Sequence=Displayed;
CC       Name=2; Synonyms=alpha N-catenin I;
CC         IsoId=Q61301-2; Sequence=VSP_006734;
CC       Name=3;
CC         IsoId=Q61301-3; Sequence=VSP_038010, VSP_006734;
CC   -!- TISSUE SPECIFICITY: Expressed almost exclusively in the nervous
CC       system.
CC   -!- DEVELOPMENTAL STAGE: The ratio of the two isoforms changes during
CC       development; isoform 1 is more abundant than isoform 2 in earlier
CC       embryonic stages, whereas isoform 2 is predominant in the adult
CC       stage. Expressed in the ventricular zone and in neurons of the
CC       developing cortical plate (at protein level). Expressed in
CC       migrating neurons of the external granule cell layer at E13.5
CC       while expression appears in the Purkinje cell layer at E17.5 (at
CC       protein level). Expressed postnatally in Purkinje cells and
CC       hippocampus (at protein level).
CC   -!- DISRUPTION PHENOTYPE: Mice generally die within 24 hours after
CC       birth. They display altered Purkinje cells migration, unstable
CC       synaptic junctions, defective ventricular architecture, impaired
CC       axon migration, reduced number of neurons in specific nuclei, and
CC       disordered laminar formation.
CC   -!- MISCELLANEOUS: The cdf (cerebellar deficient folia) mice are
CC       viable but are ataxic and have cerebellar hypoplasia associated
CC       with abnormal lobulation of the cerebellum. They also display
CC       defects in Purkinje cells positioning and in packing density and
CC       lamination. Fear conditioning and prepulse inhibition of the
CC       startle response are altered in cdf mice. Those phenotypes are
CC       associated with alteration of the Ctnna2 gene which results in the
CC       C-terminal truncation of the protein and are rescued by expression
CC       of a Ctnna2 transgene (isoform 2).
CC   -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC   -----------------------------------------------------------------------
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DR   EMBL; D25282; BAA04970.1; -; mRNA.
DR   EMBL; D25281; BAA04969.1; -; mRNA.
DR   EMBL; AK158916; BAE34726.1; -; mRNA.
DR   EMBL; BC079648; AAH79648.1; -; mRNA.
DR   IPI; IPI00119870; -.
DR   IPI; IPI00230751; -.
DR   IPI; IPI00944734; -.
DR   PIR; I49499; I49499.
DR   PIR; I49500; I49500.
DR   RefSeq; NP_001103234.1; NM_001109764.1.
DR   RefSeq; NP_033949.2; NM_009819.2.
DR   RefSeq; NP_663785.2; NM_145732.2.
DR   UniGene; Mm.34637; -.
DR   UniGene; Mm.476578; -.
DR   ProteinModelPortal; Q61301; -.
DR   SMR; Q61301; 56-260, 375-629.
DR   STRING; Q61301; -.
DR   PhosphoSite; Q61301; -.
DR   PRIDE; Q61301; -.
DR   Ensembl; ENSMUST00000075340; ENSMUSP00000074809; ENSMUSG00000063063.
DR   Ensembl; ENSMUST00000079296; ENSMUSP00000078277; ENSMUSG00000063063.
DR   GeneID; 12386; -.
DR   KEGG; mmu:12386; -.
DR   NMPDR; fig|10090.3.peg.14657; -.
DR   UCSC; uc009cjq.1; mouse.
DR   UCSC; uc009cjr.1; mouse.
DR   CTD; 12386; -.
DR   MGI; MGI:88275; Ctnna2.
DR   GeneTree; ENSGT00550000074411; -.
DR   HOGENOM; HBG356872; -.
DR   HOVERGEN; HBG000069; -.
DR   InParanoid; Q61301; -.
DR   OMA; XTGRKEK; -.
DR   OrthoDB; EOG49W2G4; -.
DR   PhylomeDB; Q61301; -.
DR   NextBio; 281100; -.
DR   ArrayExpress; Q61301; -.
DR   Bgee; Q61301; -.
DR   CleanEx; MM_CTNNA2; -.
DR   Genevestigator; Q61301; -.
DR   GermOnline; ENSMUSG00000063063; Mus musculus.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR   GO; GO:0030424; C:axon; IMP:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0005913; C:cell-cell adherens junction; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0045296; F:cadherin binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0007409; P:axonogenesis; IMP:UniProtKB.
DR   GO; GO:0048854; P:brain morphogenesis; IMP:UniProtKB.
DR   GO; GO:0016337; P:cell-cell adhesion; ISS:UniProtKB.
DR   GO; GO:0048813; P:dendrite morphogenesis; IMP:UniProtKB.
DR   GO; GO:0060134; P:prepulse inhibition; IMP:UniProtKB.
DR   GO; GO:0021942; P:radial glia guided migration of Purkinje cell; IMP:UniProtKB.
DR   GO; GO:0051823; P:regulation of synapse structural plasticity; IMP:UniProtKB.
DR   InterPro; IPR001033; Alpha_catenin.
DR   InterPro; IPR006077; Vinculin/catenin.
DR   InterPro; IPR000633; Vinculin_CS.
DR   Pfam; PF01044; Vinculin; 2.
DR   PRINTS; PR00805; ALPHACATENIN.
DR   SUPFAM; SSF47220; Vinculin/catenin; 4.
DR   PROSITE; PS00663; VINCULIN_1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell adhesion; Cell junction;
KW   Cell membrane; Cell projection; Cytoplasm; Cytoskeleton;
KW   Developmental protein; Differentiation; Membrane; Phosphoprotein.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    953       Catenin alpha-2.
FT                                /FTId=PRO_0000064264.
FT   MOD_RES       2      2       N-acetylthreonine.
FT   MOD_RES       5      5       Phosphothreonine.
FT   MOD_RES       6      6       Phosphoserine.
FT   MOD_RES     151    151       Phosphoserine (By similarity).
FT   MOD_RES     261    261       Phosphothreonine.
FT   MOD_RES     262    262       Phosphoserine.
FT   MOD_RES     640    640       Phosphoserine.
FT   MOD_RES     653    653       Phosphothreonine.
FT   MOD_RES     654    654       Phosphoserine.
FT   MOD_RES     657    657       Phosphothreonine.
FT   MOD_RES     889    889       N6-acetyllysine (By similarity).
FT   MOD_RES     901    901       Phosphoserine.
FT   VAR_SEQ       1      1       M -> MTDIHSSYTYTGSM (in isoform 3).
FT                                /FTId=VSP_038010.
FT   VAR_SEQ     811    858       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_006734.
FT   CONFLICT    103    103       M -> K (in Ref. 1; BAA04970/BAA04969).
FT   CONFLICT    331    331       I -> M (in Ref. 1; BAA04970/BAA04969).
FT   CONFLICT    349    349       Y -> D (in Ref. 1; BAA04970/BAA04969).
FT   CONFLICT    558    558       M -> I (in Ref. 3; AAH79648).
FT   CONFLICT    618    618       D -> Y (in Ref. 1; BAA04970/BAA04969).
FT   CONFLICT    648    648       Missing (in Ref. 3; AAH79648).
FT   CONFLICT    660    660       D -> R (in Ref. 1; BAA04970/BAA04969).
FT   CONFLICT    817    817       F -> S (in Ref. 1; BAA04970).
FT   CONFLICT    862    862       A -> S (in Ref. 1; BAA04970/BAA04969).
FT   CONFLICT    911    911       P -> S (in Ref. 2; BAE34726).
SQ   SEQUENCE   953 AA;  105286 MW;  52DC5230A4A4A159 CRC64;
     MTSATSPIIL KWDPKSLEIR TLTVERLLEP LVTQVTTLVN TSNKGPSGKK KGRSKKAHVL
     AASVEQATQN FLEKGEQIAK ESQDLKEELV AAVEDVRKQG ETMRIASSEF ADDPCSSVKR
     GTMVRAARAL LSAVTRLLIL ADMADVMRLL SHLKIVEEAL EAVKNATNEQ DLANRFKEFG
     KEMVKLNYVA ARRQQELKDP HCRDEMAAAR GALKKNATML YTASQAFLRH PDVAATRANR
     DYVFKQVQEA IAGISSAAQA TSPTDEAKGH TGIGELAAAL NEFDNKIILD PMTFSEARFR
     PSLEERLESI ISGAALMADS SCTRDDRRER IVAECNAVRQ ALQDLLSEYM NNTGRKEKGD
     PLNIAIDKMT KKTRDLRRQL RKAVMDHISD SFLETNVPLL VLIEAAKSGN EKEVKEYAQV
     FREHANKLVE VANLACSISN NEEGVKLVRM AATQIDSLCP QVINAALTLA ARPQSKVAQD
     NMDVFKDQWE KQVRVLTEAV DDITSVDDFL SVSENHILED VNKCVIALQE GDVDTLDRTA
     GAIRGRAARV IHIINAEMEN YEAGVYTEKV LEATKLLSET VMPRFAEQVE VAIEALSANV
     PQPFEENEFI DASRLVYDGV RDIRKAVLMI RTPEELEDDS DFEQEDYDVR SRTSVQTEDD
     QLIAGQSARA IMAQLPQEEK AKIAEQVEIF HQEKSKLDAE VAKWDDSGND IIVLAKQMCM
     IMMEMTDFTR GKGPLKNTSD VINAAKKIAE AGSRMDKLAR AVADQCPDSA CKQDLLAYLQ
     RIALYCHQLN ICSKVKAEVQ NLGGELIVSG TGVQSTFTTF YEVDCDVIDG GRASQLSTHL
     PTCAEGAPIG SGSSDSSMLD SATSLIQAAK NLMNAVVLTV KASYVASTKY QKVYGTAAVN
     SPVVSWKMKA PEKKPLVKRE KPEEFQTRVR RGSQKKHISP VQALSEFKAM DSF
//
ID   APC_MOUSE               Reviewed;        2845 AA.
AC   Q61315; Q62044;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 100.
DE   RecName: Full=Adenomatous polyposis coli protein;
DE            Short=Protein APC;
DE            Short=mAPC;
GN   Name=Apc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS.
RC   STRAIN=C57BL/6J, and CAST/Ei; TISSUE=Brain;
RX   MEDLINE=92263101; PubMed=1350108; DOI=10.1126/science.1350108;
RA   Su L.-K., Kinzler K.W., Vogelstein B., Preisinger A.C., Moser A.R.,
RA   Luongo C., Gould K.A., Dove W.F.;
RT   "Multiple intestinal neoplasia caused by a mutation in the murine
RT   homolog of the APC gene.";
RL   Science 256:668-670(1992).
RN   [2]
RP   ERRATUM.
RA   Su L.-K., Kinzler K.W., Vogelstein B., Preisinger A.C., Moser A.R.,
RA   Luongo C., Gould K.A., Dove W.F.;
RL   Science 256:1114-1114(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
RC   STRAIN=BALB/c; TISSUE=Liver;
RA   Dicker F., Lambertz S., Reitmair A., Ballhausen W.G.;
RT   "The murine APC gene: alternative splicing of 5' untranslated region
RT   segments.";
RL   Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 1795-1810, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   ALTERNATIVE SPLICING.
RX   MEDLINE=94061824; PubMed=8242607;
RA   Oshima M., Sugiyama H., Kitagawa K., Taketo M.;
RT   "APC gene messenger RNA: novel isoforms that lack exon 7.";
RL   Cancer Res. 53:5589-5591(1993).
RN   [6]
RP   INTERACTION WITH DIAPH1; DIAPH2 AND MAPRE1.
RX   PubMed=15311282; DOI=10.1038/ncb1160;
RA   Wen Y., Eng C.H., Schmoranzer J., Cabrera-Poch N., Morris E.J.S.,
RA   Chen M., Wallar B.J., Alberts A.S., Gundersen G.G.;
RT   "EB1 and APC bind to mDia to stabilize microtubules downstream of Rho
RT   and promote cell migration.";
RL   Nat. Cell Biol. 6:820-830(2004).
RN   [7]
RP   INTERACTION WITH SCRIB.
RX   PubMed=16611247; DOI=10.1111/j.1365-2443.2006.00954.x;
RA   Takizawa S., Nagasaka K., Nakagawa S., Yano T., Nakagawa K.,
RA   Yasugi T., Takeuchi T., Kanda T., Huibregtse J.M., Akiyama T.,
RA   Taketani Y.;
RT   "Human scribble, a novel tumor suppressor identified as a target of
RT   high-risk HPV E6 for ubiquitin-mediated degradation, interacts with
RT   adenomatous polyposis coli.";
RL   Genes Cells 11:453-464(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1370; SER-2674 AND
RP   SER-2713, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1036, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1557, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Tumor suppressor. Promotes rapid degradation of CTNNB1
CC       and participates in Wnt signaling as a negative regulator. APC
CC       activity is correlated with its phosphorylation state (By
CC       similarity).
CC   -!- SUBUNIT: Forms homooligomers and heterooligomers with APC2.
CC       Interacts with PDZ domains of DLG1 and DLG3. Associates with
CC       catenins. Binds axin. Interacts with MAPRE2 and MAPRE3 (via C-
CC       terminus). Found in a complex consisting of ARHGEF4, APC and
CC       CTNNB1. Interacts with ARHGEF4 (via N-terminus) (By similarity).
CC       Interacts with MAPRE1 (via C-terminus); probably required for APC
CC       targeting to the growing microtubule plus ends. Interacts with
CC       DIAPH1 and DIAPH2. Interacts with SCRIB; may mediate targeting to
CC       adherens junctions of epithelial cells.
CC   -!- SUBCELLULAR LOCATION: Cell junction, adherens junction (By
CC       similarity). Cytoplasm, cytoskeleton (By similarity).
CC       Note=Associated with the microtubule network at the growing distal
CC       tip of microtubules (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q61315-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q61315-2; Sequence=VSP_004116;
CC       Name=3;
CC         IsoId=Q61315-3; Sequence=VSP_004117;
CC       Name=4;
CC         IsoId=Q61315-4; Sequence=VSP_004116, VSP_004117;
CC   -!- TISSUE SPECIFICITY: Expressed in liver, spleen, kidney, heart,
CC       lung, brain, stomach, intestine, testis and ovary.
CC   -!- DOMAIN: The microtubule tip localization signal (MtLS) motif;
CC       mediates interaction with MAPRE1 and targeting to the growing
CC       microtubule plus ends (By similarity).
CC   -!- PTM: Phosphorylated by GSK3B (By similarity).
CC   -!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
CC       Ubiquitination is facilitated by Axin. Deubiquitinated by
CC       ZRANB1/TRABID (By similarity).
CC   -!- SIMILARITY: Belongs to the adenomatous polyposis coli (APC)
CC       family.
CC   -!- SIMILARITY: Contains 7 ARM repeats.
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DR   EMBL; M88127; AAB59632.1; -; mRNA.
DR   EMBL; U02937; AAA03443.1; -; Unassigned_DNA.
DR   IPI; IPI00119913; -.
DR   IPI; IPI00229891; -.
DR   IPI; IPI00229894; -.
DR   IPI; IPI00468234; -.
DR   PIR; I49505; I49505.
DR   UniGene; Mm.384171; -.
DR   PDB; 1VJ6; NMR; -; B=2834-2845.
DR   PDBsum; 1VJ6; -.
DR   ProteinModelPortal; Q61315; -.
DR   SMR; Q61315; 2-55, 128-237, 445-733, 1485-1527.
DR   STRING; Q61315; -.
DR   PhosphoSite; Q61315; -.
DR   PRIDE; Q61315; -.
DR   Ensembl; ENSMUST00000079362; ENSMUSP00000078337; ENSMUSG00000005871.
DR   Ensembl; ENSMUST00000115781; ENSMUSP00000111447; ENSMUSG00000005871.
DR   UCSC; uc008eke.1; mouse.
DR   MGI; MGI:88039; Apc.
DR   HOGENOM; HBG715475; -.
DR   HOVERGEN; HBG004264; -.
DR   InParanoid; Q61315; -.
DR   OrthoDB; EOG4D26NZ; -.
DR   ArrayExpress; Q61315; -.
DR   Bgee; Q61315; -.
DR   CleanEx; MM_APC; -.
DR   Genevestigator; Q61315; -.
DR   GermOnline; ENSMUSG00000005871; Mus musculus.
DR   GO; GO:0044295; C:axonal growth cone; IDA:MGI.
DR   GO; GO:0030877; C:beta-catenin destruction complex; ISS:UniProtKB.
DR   GO; GO:0031253; C:cell projection membrane; IDA:MGI.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IDA:MGI.
DR   GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR   GO; GO:0035371; C:microtubule plus end; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0034750; C:Scrib-APC-beta-catenin complex; IDA:BHF-UCL.
DR   GO; GO:0008013; F:beta-catenin binding; ISS:UniProtKB.
DR   GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
DR   GO; GO:0019887; F:protein kinase regulator activity; ISS:UniProtKB.
DR   GO; GO:0009952; P:anterior/posterior pattern formation; IMP:MGI.
DR   GO; GO:0009798; P:axis specification; IMP:MGI.
DR   GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR   GO; GO:0060070; P:canonical Wnt receptor signaling pathway; IMP:MGI.
DR   GO; GO:0007050; P:cell cycle arrest; ISS:UniProtKB.
DR   GO; GO:0016477; P:cell migration; IMP:MGI.
DR   GO; GO:0051276; P:chromosome organization; IGI:MGI.
DR   GO; GO:0000281; P:cytokinesis after mitosis; IMP:MGI.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IGI:MGI.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
DR   GO; GO:0001942; P:hair follicle development; IMP:MGI.
DR   GO; GO:0001822; P:kidney development; IMP:MGI.
DR   GO; GO:0007091; P:mitotic metaphase/anaphase transition; IMP:MGI.
DR   GO; GO:0046716; P:muscle cell homeostasis; IGI:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptosis; IMP:MGI.
DR   GO; GO:0045736; P:negative regulation of cyclin-dependent protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; IMP:MGI.
DR   GO; GO:0043409; P:negative regulation of MAPKKK cascade; IGI:MGI.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISS:UniProtKB.
DR   GO; GO:0042483; P:negative regulation of odontogenesis; IMP:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptosis; IMP:MGI.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; IMP:MGI.
DR   GO; GO:0051781; P:positive regulation of cell division; IMP:MGI.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:MGI.
DR   GO; GO:0030858; P:positive regulation of epithelial cell differentiation; IGI:MGI.
DR   GO; GO:0031116; P:positive regulation of microtubule polymerization; IMP:MGI.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:MGI.
DR   GO; GO:0006461; P:protein complex assembly; ISS:UniProtKB.
DR   GO; GO:0009954; P:proximal/distal pattern formation; IMP:MGI.
DR   GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; IMP:MGI.
DR   GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IMP:MGI.
DR   GO; GO:0045667; P:regulation of osteoblast differentiation; IMP:MGI.
DR   GO; GO:0045670; P:regulation of osteoclast differentiation; IMP:MGI.
DR   GO; GO:0006974; P:response to DNA damage stimulus; ISS:UniProtKB.
DR   GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR   GO; GO:0043588; P:skin development; IMP:MGI.
DR   GO; GO:0035019; P:somatic stem cell maintenance; IGI:MGI.
DR   GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR   GO; GO:0048538; P:thymus development; IMP:MGI.
DR   InterPro; IPR009240; APC_15aa.
DR   InterPro; IPR009234; APC_basic.
DR   InterPro; IPR009223; APC_crr.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR009232; EB1-bd.
DR   InterPro; IPR009224; SAMP.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 3.
DR   Pfam; PF05972; APC_15aa; 4.
DR   Pfam; PF05956; APC_basic; 1.
DR   Pfam; PF05923; APC_crr; 7.
DR   Pfam; PF00514; Arm; 3.
DR   Pfam; PF05937; EB1_binding; 1.
DR   Pfam; PF05924; SAMP; 3.
DR   SMART; SM00185; ARM; 6.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell junction; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; Microtubule;
KW   Phosphoprotein; Repeat; Tumor suppressor; Ubl conjugation;
KW   Wnt signaling pathway.
FT   CHAIN         1   2845       Adenomatous polyposis coli protein.
FT                                /FTId=PRO_0000064628.
FT   REPEAT      451    493       ARM 1.
FT   REPEAT      503    545       ARM 2.
FT   REPEAT      546    589       ARM 3.
FT   REPEAT      590    636       ARM 4.
FT   REPEAT      637    681       ARM 5.
FT   REPEAT      682    723       ARM 6.
FT   REPEAT      724    765       ARM 7.
FT   REGION     1864   1891       Highly charged.
FT   COILED        1     61       Potential.
FT   COILED      125    245       Potential.
FT   MOTIF      2805   2808       Microtubule tip localization signal.
FT   MOTIF      2843   2845       PDZ-binding (By similarity).
FT   COMPBIAS      1    728       Leu-rich.
FT   COMPBIAS    739   2834       Ser-rich.
FT   COMPBIAS   1130   1156       Asp/Glu-rich (acidic).
FT   COMPBIAS   1556   1575       Asp/Glu-rich (acidic).
FT   MOD_RES     778    778       Phosphoserine (By similarity).
FT   MOD_RES     985    985       Phosphoserine (By similarity).
FT   MOD_RES    1036   1036       Phosphoserine.
FT   MOD_RES    1040   1040       Phosphoserine (By similarity).
FT   MOD_RES    1179   1179       Phosphoserine (By similarity).
FT   MOD_RES    1359   1359       Phosphoserine (By similarity).
FT   MOD_RES    1370   1370       Phosphoserine.
FT   MOD_RES    1437   1437       Phosphothreonine (By similarity).
FT   MOD_RES    1557   1557       Phosphoserine.
FT   MOD_RES    1695   1695       Phosphothreonine (By similarity).
FT   MOD_RES    1859   1859       Phosphoserine (By similarity).
FT   MOD_RES    1861   1861       Phosphoserine (By similarity).
FT   MOD_RES    1862   1862       Phosphoserine (By similarity).
FT   MOD_RES    2087   2087       Phosphoserine (By similarity).
FT   MOD_RES    2092   2092       Phosphoserine (By similarity).
FT   MOD_RES    2095   2095       Phosphoserine (By similarity).
FT   MOD_RES    2125   2125       Phosphoserine (By similarity).
FT   MOD_RES    2143   2143       Phosphoserine (By similarity).
FT   MOD_RES    2151   2151       Phosphothreonine (By similarity).
FT   MOD_RES    2260   2260       Phosphoserine (By similarity).
FT   MOD_RES    2270   2270       Phosphoserine (By similarity).
FT   MOD_RES    2283   2283       Phosphoserine (By similarity).
FT   MOD_RES    2398   2398       Phosphoserine (By similarity).
FT   MOD_RES    2464   2464       Phosphoserine (By similarity).
FT   MOD_RES    2469   2469       Phosphoserine (By similarity).
FT   MOD_RES    2473   2473       Phosphoserine (By similarity).
FT   MOD_RES    2533   2533       Phosphoserine (By similarity).
FT   MOD_RES    2535   2535       Phosphoserine (By similarity).
FT   MOD_RES    2671   2671       Phosphoserine (By similarity).
FT   MOD_RES    2674   2674       Phosphoserine.
FT   MOD_RES    2676   2676       Phosphothreonine (By similarity).
FT   MOD_RES    2679   2679       Phosphothreonine (By similarity).
FT   MOD_RES    2713   2713       Phosphoserine.
FT   MOD_RES    2791   2791       Phosphoserine (By similarity).
FT   MOD_RES    2837   2837       Phosphoserine (By similarity).
FT   MOD_RES    2839   2839       Phosphoserine (By similarity).
FT   MOD_RES    2840   2840       Phosphotyrosine (By similarity).
FT   VAR_SEQ     243    276       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_004116.
FT   VAR_SEQ     310    410       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_004117.
FT   VARIANT     120    120       T -> A (in strain: CAST/Ei).
FT   VARIANT     493    493       V -> I (in strain: CAST/Ei).
FT   VARIANT     797    797       Y -> F (in strain: CAST/Ei).
FT   VARIANT    1330   1330       A -> T (in strain: CAST/Ei).
FT   VARIANT    1618   1618       A -> S (in strain: CAST/Ei).
FT   VARIANT    2294   2294       G -> A (in strain: CAST/Ei).
FT   VARIANT    2496   2496       H -> Q (in strain: CAST/Ei).
FT   VARIANT    2523   2523       T -> A (in strain: CAST/Ei).
FT   VARIANT    2813   2813       T -> S (in strain: CAST/Ei).
SQ   SEQUENCE   2845 AA;  311089 MW;  145CA73CF570A499 CRC64;
     MAAASYDQLL KQVEALKMEN SNLRQELEDN SNHLTKLETE ASNMKEVLKQ LQGSIEDETM
     TSGQIDLLER LKEFNLDSNF PGVKLRSKMS LRSYGSREGS VSSRSGECSP VPMGSFPRRT
     FVNGSRESTG YLEELEKERS LLLADLDKEE KEKDWYYAQL QNLTKRIDSL PLTENFSLQT
     DMTRRQLEYE ARQIRAAMEE QLGTCQDMEK RAQRRIARIQ QIEKDILRVR QLLQSQAAEA
     ERSSQSRHDA ASHEAGRQHE GHGVAESNTA ASSSGQSPAT RVDHETASVL SSSGTHSAPR
     RLTSHLGTKV EMVYSLLSML GTHDKDDMSR TLLAMSSSQD SCISMRQSGC LPLLIQLLHG
     NDKDSVLLGN SRGSKEARAR ASAALHNIIH SQPDDKRGRR EIRVLHLLEQ IRAYCETCWE
     WQEAHEQGMD QDKNPMPAPV EHQICPAVCV LMKLSFDEEH RHAMNELGGL QAIAELLQVD
     CEMYGLTNDH YSVTLRRYAG MALTNLTFGD VANKATLCSM KGCMRALVAQ LKSESEDLQQ
     VIASVLRNLS WRADVNSKKT LREVGSVKAL MECALEVKKE STLKSVLSAL WNLSAHCTEN
     KADICAVDGA LAFLVGTLTY RSQTNTLAII ESGGGILRNV SSLIATNEDH RQILRENNCL
     QTLLQHLKSH SLTIVSNACG TLWNLSARNP KDQEALWDMG AVSMLKNLIH SKHKMIAMGS
     AAALRNLMAN RPAKYKDANI MSPGSSLPSL HVRKQKALEA ELDAQHLSET FDNIDNLSPK
     ASHRSKQRHK QNLYGDYAFD ANRHDDSRSD NFNTGNMTVL SPYLNTTVLP SSSSSRGSLD
     SSRSEKDRSL ERERGIGLSA YHPTTENAGT SSKRGLQITT TAAQIAKVME EVSAIHTSQD
     DRSSASTTEF HCVADDRSAA RRSSASHTHS NTYNFTKSEN SNRTCSMPYA KVEYKRSSND
     SLNSVTSSDG YGKRGQMKPS VESYSEDDES KFCSYGQYPA DLAHKIHSAN HMDDNDGELD
     TPINYSLKYS DEQLNSGRQS PSQNERWARP KHVIEDEIKQ NEQRQARSQN TSYPVYSENT
     DDKHLKFQPH FGQQECVSPY RSRGTSGSET NRMGSSHAIN QNVNQSLCQE DDYEDDKPTN
     YSERYSEEEQ HEEEEERPTN YSIKYNEEKH HVDQPIDYSL KYATDISSSQ KPSFSFSKNS
     SAQSTKPEHL SPSSENTAVP PSNAKRQNQL RPSSAQRNGQ TQKGTTCKVP SINQETIQTY
     CVEDTPICFS RCSSLSSLSS ADDEIGCDQT TQEADSANTL QTAEVKENDV TRSAEDPATE
     VPAVSQNARA KPSRLQASGL SSESTRHNKA VEFSSGAKSP SKSGAQTPKS PPEHYVQETP
     LVFSRCTSVS SLDSFESRSI ASSVQSEPCS GMVSGIISPS DLPDSPGQTM PPSRSKTPPP
     PPQTVQAKRE VPKSKVPAAE KRESGPKQTA VNAAVQRVQV LPDVDTLLHF ATESTPDGFS
     CSSSLSALSL DEPFIQKDVE LRIMPPVQEN DNGNETESEQ PEESNENQDK EVEKPDSEKD
     LLDDSDDDDI EILEECIISA MPTKSSRKAK KLAQTASKLP PPVARKPSQL PVYKLLPAQN
     RLQAQKHVSF TPGDDVPRVY CVEGTPINFS TATSLSDLTI ESPPNELATG DGVRAGIQSG
     EFEKRDTIPT EGRSTDDAQR GKISSIVTPD LDDNKAEEGD ILAECINSAM PKGKSHKPFR
     VKKIMDQVQQ ASSTSSGANK NQVDTKKKKP TSPVKPMPQN TEYRTRVRKN TDSKVNVNTE
     ETFSDNKDSK KPSLQTNAKA FNEKLPNNED RVRGTFALDS PHHYTPIEGT PYCFSRNDSL
     SSLDFDDDDV DLSREKAELR KGKESKDSEA KVTCRPEPNS SQQAASKSQA SIKHPANRAQ
     SKPVLQKQPT FPQSSKDGPD RGAATDEKLQ NLAIENTPVC FSRNSSLSSL SDIDQENNNN
     KESEPIKEAE PANSQGEPSK PQASGYAPKS FHVEDTPVCF SRNSSLSSLS IDSEDDLLQE
     CISSAMPKKK RPSRLKSESE KQSPRKVGGI LAEDLTLDLK DLQRPDSEHA FSPGSENFDW
     KAIQEGANSI VSSLHQAAAA AACLSRQASS DSDSILSLKS GISLGSPFHL TPDQEEKPFT
     SNKGPRILKP GEKSTLEAKK IESENKGIKG GKKVYKSLIT GKIRSNSEIS SQMKQPLPTN
     MPSISRGRTM IHIPGLRNSS SSTSPVSKKG PPLKTPASKS PSEGPGATTS PRGTKPAGKS
     ELSPITRQTS QISGSNKGSS RSGSRDSTPS RPTQQPLSRP MQSPGRNSIS PGRNGISPPN
     KLSQLPRTSS PSTASTKSSG SGKMSYTSPG RQLSQQNLTK QASLSKNASS IPRSESASKG
     LNQMSNGNGS NKKVELSRMS STKSSGSESD SSERPALVRQ STFIKEAPSP TLRRKLEESA
     SFESLSPSSR PDSPTRSQAQ TPVLSPSLPD MSLSTHPSVQ AGGWRKLPPN LSPTIEYNDG
     RPTKRHDIAR SHSESPSRLP INRAGTWKRE HSKHSSSLPR VSTWRRTGSS SSILSASSES
     SEKAKSEDER HVSSMPAPRQ MKENQVPTKG TWRKIKESDI SPTGMASQSA SSGAASGAES
     KPLIYQMAPP VSKTEDVWVR IEDCPINNPR SGRSPTGNTP PVIDSVSEKG SSSIKDSKDS
     KDTHGKQSVG SGSPVQTVGL ETRLNSFVQV EAPEQKGTEA KPGQSNPVSI AETAETCIAE
     RTPFSSSSSS KHSSPSGTVA ARVTPFNYNP SPRKSSADST SARPSQIPTP VSTNTKKRDS
     KTDITESSGA QSPKRHSGSY LVTSV
//
ID   ZFHX3_MOUSE             Reviewed;        3726 AA.
AC   Q61329;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 100.
DE   RecName: Full=Zinc finger homeobox protein 3;
DE   AltName: Full=AT motif-binding factor;
DE   AltName: Full=AT-binding transcription factor 1;
DE   AltName: Full=Alpha-fetoprotein enhancer-binding protein;
DE   AltName: Full=Zinc finger homeodomain protein 3;
DE            Short=ZFH-3;
GN   Name=Zfhx3; Synonyms=Atbf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/MK X ICR; TISSUE=Brain;
RX   MEDLINE=96194902; PubMed=8654949; DOI=10.1016/0378-1119(95)00740-7;
RA   Ido A., Miura Y., Watanabe M., Sakai M., Inoue Y., Miki T.,
RA   Hashimoto T., Morinaga T., Nishi S., Tamaoki T.;
RT   "Cloning of the cDNA encoding the mouse ATBF1 transcription factor.";
RL   Gene 168:227-231(1996).
RN   [2]
RP   INTERACTION WITH FNBP3.
RX   MEDLINE=97315177; PubMed=9171351; DOI=10.1093/emboj/16.9.2376;
RA   Bedford M.T., Chan D.C., Leder P.;
RT   "FBP WW domains and the Abl SH3 domain bind to a specific class of
RT   proline-rich ligands.";
RL   EMBO J. 16:2376-2383(1997).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=11312261; DOI=10.1074/jbc.M010378200;
RA   Berry F.B., Miura Y., Mihara K., Kaspar P., Sakata N.,
RA   Hashimoto-Tamaoki T., Tamaoki T.;
RT   "Positive and negative regulation of myogenic differentiation of C2C12
RT   cells by isoforms of the multiple homeodomain zinc finger
RT   transcription factor ATBF1.";
RL   J. Biol. Chem. 276:25057-25065(2001).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Transcriptional repressor. It inhibits the enhancer
CC       element of the AFP gene by binding to its AT-rich core sequence.
CC       Regulator of myoblasts differentiation through the binding to the
CC       AT-rich sequence of MYF6 promoter and promoter repression (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with PIAS3 (By similarity). Interacts with
CC       FNBP3.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed in skeletal muscle. Levels of
CC       expression are high in myoblasts but low in differentiated muscle.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 22 C2H2-type zinc fingers.
CC   -!- SIMILARITY: Contains 4 homeobox DNA-binding domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D26046; BAA05046.1; -; mRNA.
DR   IPI; IPI00119958; -.
DR   UniGene; Mm.416972; -.
DR   UniGene; Mm.477670; -.
DR   ProteinModelPortal; Q61329; -.
DR   SMR; Q61329; 641-749, 795-823, 944-1013, 1040-1068, 1089-1117, 1224-1289, 1371-1470, 1545-1628, 2153-2214, 2254-2312, 2645-2707, 2954-3015, 3028-3073.
DR   STRING; Q61329; -.
DR   PhosphoSite; Q61329; -.
DR   PRIDE; Q61329; -.
DR   Ensembl; ENSMUST00000043896; ENSMUSP00000044612; ENSMUSG00000038872.
DR   UCSC; uc009nid.1; mouse.
DR   MGI; MGI:99948; Zfhx3.
DR   HOGENOM; HBG444826; -.
DR   HOVERGEN; HBG050606; -.
DR   InParanoid; Q61329; -.
DR   OrthoDB; EOG4Z0B4P; -.
DR   ArrayExpress; Q61329; -.
DR   Bgee; Q61329; -.
DR   CleanEx; MM_ZFHX3; -.
DR   Genevestigator; Q61329; -.
DR   GermOnline; ENSMUSG00000038872; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR   InterPro; IPR001356; Homeobox.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   InterPro; IPR003604; Znf_U1.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 4.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 4.
DR   Pfam; PF00046; Homeobox; 4.
DR   SMART; SM00389; HOX; 4.
DR   SMART; SM00355; ZnF_C2H2; 23.
DR   SMART; SM00451; ZnF_U1; 7.
DR   SUPFAM; SSF46689; Homeodomain_like; 4.
DR   PROSITE; PS00027; HOMEOBOX_1; 2.
DR   PROSITE; PS50071; HOMEOBOX_2; 4.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 15.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE   1: Evidence at protein level;
KW   Activator; DNA-binding; Homeobox; Metal-binding; Myogenesis; Nucleus;
KW   Phosphoprotein; Repeat; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   3726       Zinc finger homeobox protein 3.
FT                                /FTId=PRO_0000046931.
FT   ZN_FING      79    103       C2H2-type 1.
FT   ZN_FING     282    305       C2H2-type 2.
FT   ZN_FING     641    664       C2H2-type 3.
FT   ZN_FING     672    695       C2H2-type 4.
FT   ZN_FING     727    751       C2H2-type 5.
FT   ZN_FING     805    829       C2H2-type 6; atypical.
FT   ZN_FING     946    969       C2H2-type 7; degenerate.
FT   ZN_FING     985   1009       C2H2-type 8; atypical.
FT   ZN_FING    1041   1065       C2H2-type 9; atypical.
FT   ZN_FING    1089   1113       C2H2-type 10; atypical.
FT   ZN_FING    1233   1256       C2H2-type 11; atypical.
FT   ZN_FING    1262   1285       C2H2-type 12.
FT   ZN_FING    1370   1395       C2H2-type 13.
FT   ZN_FING    1411   1433       C2H2-type 14.
FT   ZN_FING    1439   1462       C2H2-type 15.
FT   ZN_FING    1555   1579       C2H2-type 16.
FT   ZN_FING    1606   1630       C2H2-type 17.
FT   ZN_FING    1990   2013       C2H2-type 18.
FT   DNA_BIND   2152   2211       Homeobox 1.
FT   DNA_BIND   2249   2308       Homeobox 2.
FT   ZN_FING    2335   2358       C2H2-type 19; atypical.
FT   ZN_FING    2539   2561       C2H2-type 20.
FT   DNA_BIND   2650   2709       Homeobox 3.
FT   ZN_FING    2720   2743       C2H2-type 21.
FT   DNA_BIND   2952   3011       Homeobox 4.
FT   ZN_FING    3032   3056       C2H2-type 22.
FT   ZN_FING    3552   3576       C2H2-type.
FT   COMPBIAS    461    491       Poly-Glu.
FT   COMPBIAS    771    785       Poly-Ala.
FT   COMPBIAS   1314   1317       Poly-Ala.
FT   COMPBIAS   1734   1748       Poly-Gln.
FT   COMPBIAS   1794   1799       Poly-Gln.
FT   COMPBIAS   1856   1863       Poly-Gln.
FT   COMPBIAS   2044   2059       Poly-Pro.
FT   COMPBIAS   2405   2408       Poly-Ala.
FT   COMPBIAS   3216   3220       Poly-Pro.
FT   COMPBIAS   3380   3409       Poly-Gln.
FT   COMPBIAS   3412   3420       Poly-Gln.
FT   COMPBIAS   3534   3550       Poly-Gly.
FT   COMPBIAS   3620   3623       Poly-Pro.
FT   COMPBIAS   3659   3662       Poly-Ser.
FT   MOD_RES     267    267       Phosphoserine (By similarity).
FT   MOD_RES     425    425       Phosphoserine (By similarity).
FT   MOD_RES     573    573       Phosphoserine (By similarity).
FT   MOD_RES    1190   1190       Phosphoserine (By similarity).
FT   MOD_RES    1207   1207       Phosphoserine (By similarity).
FT   MOD_RES    1600   1600       Phosphoserine.
SQ   SEQUENCE   3726 AA;  406570 MW;  915ACBE588A72C98 CRC64;
     MEGCDSPVVS GKDNGCGIPQ HRQWTELNSA HLPDKPSSME QPTGESHGPL DSLRAPFNER
     LADSSTSAGP PAEPASKEVS CNECSASFSS LQTYMEHHCP GTHPPPALRE ESASDTSEEG
     EEESDVENLA GEIVYQPDGS AYIVESLSQL AQSGAACGSS SGSGAVPSLF LNSLPGVGGK
     QGDPSCAAPV YPQIINTSHI ASSFGKWFEG SDPAFPNTSA LAGLSPVLHS FRVFDVRHKS
     NKDYLNSDGS AKSSCVSKDV PNNVDLSKFD GFVLYGKRKP ILMCFLCKLS FGYVRSFVTH
     AVHDHRMTLS EEERKLLSNK NISAIIQGIG KDKEPLVSFL EPKNKNFQHP LVSTGNLIGP
     GHSFYGKFSG IRMEGEEALP AVAAAGPEQP QAGLLTPSTL LNLGGLTSSV LKTPITSVPL
     GPLASSPTKS SEGKDSGAAE GDKQESGGHQ DCFSEKVEPA EEEEAEEEEE EEEEAEEEEE
     EEEEEEEEEE EASKGLFPND LEEELEDSPS EESGPPAGGT TKKDLALSNP SISNSPLMPN
     VLQTLSRGPA STTSNSASNF VVFDGANRRS RLSFNSEGVR ANVAEGRRLD FADESANKDS
     ATAPEPNEST EGDDGGFVPH HQHAGSLCEL GVGESPSGSG VECPKCDTVL GSSRSLGGHM
     TMMHSRNSCK TLKCPKCNWH YKYQQTLEAH MKEKHPEPGG SCVYCKSGQP HPRLARGESY
     TCGYKPFRCE VCNYSTTTKG NLSIHMQSDK HLNNMQNLQN GGGEQVFSHS AGAAAAAAAA
     AAAAANIGSS WGAPSPTKPK TKPTWRCEVC DYETNVARNL RIHMTSEKHM HNMMLLQQNM
     TQIQHNRHLG LGSLPSPAEA ELYQYYLAQN MNLPNLKMDS TASDAQFMMS GFQLDPTGPM
     AAMTPALVGG EIPLDMRLGG GQLVSEELMN LGESFIQTND PSLKLFQCAV CNKFTTDNLD
     MLGLHMNVER SLSEDEWKAV MGDSYQCKLC RYNTQLKANF QLHCKTDKHV QKYQLVAHIK
     EGGKANEWRL KCVAIGNPVH LKCNACDYYT NSLEKLRLHT VNSRHEASLK LYKHLQQHES
     GVEGESCYYH CVLCNYSTKA KLNLIQHVRS MKHQRSESLR KLQRLQKGLP EEDEDLGQIF
     TIRRCPSTDP EEPVEDAEGP SEASADPEEL AKDQGSGSEE GQSKRAASSS QAEKELTDSP
     ATTKRTSFPG SSETPLSSKR PKASEEIKPE QMYQCPYCKY SNADVNRLRV HAMTQHSVQP
     LLRCPLCQDM LNNKIHLQLH LTHLHSVAPD CVEKLIMTVT APEMVMPSSM FLPAAAADRD
     GNSTLEEVGK QPEASEDPGK NILPPASMEH GGDLKPTSAD PSCGREDSGF LCWKKGCNQV
     FKTSATLQTH FNEVHAKRPQ LPVSDRHVYK YRCNQCSLAF KTIEKLQLHS QYHVIRAATM
     CCLCQRSFRT FQALKKHLET SHLELSEADI QQLYGGLLAN GDLLAMGDPT LAEDHTIIVE
     EDKEEESDLE DKQSPTGSDS GSVQEDSGSE PKRALPFRKG PNFTMEKFLD PSRPYKCTVC
     KESFTQKNIL LVHYNSVSHL HKLKRALQES ATGQPEPTSS PDNKPFKCNT CNVAYSQSST
     LEIHMRSVLH QTKARAAKLE AASGNSNGTG NSGGVSLSSS TPSPVGSSGA NNTFTATNPS
     SAAMAPSVNA LSQVPPESVV MPPLGNPISA NIASPSEPKE ANRKKLADMI ASRQQQQQQQ
     QQQQQQAQTL AQAQAQVQAH LQQELQQQAA LIQSQLFNPT LLPHFPMTTE TLLQLQQQQH
     LLFPFYIPSA EFQLNPEVSL PVTSGALTLT GSGPGLLEDL KVQVQIPQQS HQQILQQQQQ
     QSQLSLSQSH SALLQPSQHP EKKNKVVIKE KDKESQRERE GPEGAEGNTG PQESLPDASK
     AKEKKDLAPG GGSEGTMLPP RIASDARGNA TKALLENFGF ELVIQYNENK QKAQKKNGKA
     EQGGESLEKL ECDSCGKLFS NILILKSHQE HVHQNYFPFK QLERFAKQYR EHYDKLYPLR
     PQTPEPPPPP PPPPPPPLPT APPQPASAPA IPASAPPITS PTIAPAQPSV PLTQLSMPME
     LPIFSPLMMQ TMPLQTLPAQ LPPQLGPVEP LPADLAQLYQ HQLNPTLLQQ QNKRPRTRIT
     DDQLRVLRQY FDINNSPSEE QIKEMADKSG LPQKVIKHWF RNTLFKERQR NKDSPYNFSN
     PPITSLEELK IDSRPPSPEP QKQEYWGSKR SSRTRFTDYQ LRVLQDFFDA NAYPKDDEFE
     QLSNLLNLPT RVIVVWFQNA RQKARKNYEN QGEGKDGERR ELTNDRYIRT SNLNYQCKKC
     SLVFQRIFDL IKHQKKLCYK DEDEEGQDDS QNEDSMDAME ILTPTSSSCS TPMPSQAYST
     PAPSAAAANT APSAFLQLTA ETDELATFNS KAEASDEKPK QADPPSAQPN QTQEKQGQPK
     PEMQQQLEQL EQKTNAPQPK LPQPAAPSLP QPPPQAPPPQ CPLPQSSPSP SQLSHLPLKP
     LHTSTPQQLA NLPPQLIPYQ CDQCKLAFPS FEHWQEHQQL HFLSAQNQFI HPQFLDRSLD
     MPFMLFDPSN PLLASQLLSG AIPQIPASSA TSPSTPTSTM NTLKRKLEEK ASASPGENDS
     GTGGEEPQRD KRLRTTITPE QLEILYQKYL LDSNPTRKML DHIAHEVGLK KRVVQVWFQN
     TRARERKGQF RAVGPAQAHR RCPFCRALFK AKTALEAHIR SRHWHEAKRA GYNLTLSAML
     LDCDGGLQMK GDIFDGTSFS HLPPSSSDGQ GVPLSPVSKT MELSPRTLLS PSSIKVEGIE
     DFESPSMSSV NLNFDQTKLD NDDCSSVNTA ITDTTTGDEG NADNDSATGI ATETKSSAPN
     EGLTKAAMMA MSEYEDRLSS GLVSPAPSFY SKEYDNEGTV DYSETSSLAD PCSPSPGASG
     SAGKSGDGGD RPGQKRFRTQ MTNLQLKVLK SCFNDYRTPT MLECEVLGND IGLPKRVVQV
     WFQNARAKEK KSKLSMAKHF GINQTSYEGP KTECTLCGIK YSARLSVRDH IFSQQHISKV
     KDTIGSQLDK EKEYFDPATV RQLMAQQELD RIKKANEVLG LAAQQQGMFD NAPLQALNLP
     TTYPALQGIP PVLLPGLNRP SLPGFTPANT ALTSPKPNLM GLPSTTVPSP GLPTSGLPNK
     PSSASLSSPT PAQATMAMAP QPPPQPQQPQ PPVQQPPPPP AAQQIPAPQL TPQQQRKDKD
     GEKGKEKEKA HKGKGEPLPV PKKEKGEAPP AGTGTISAPL PAMEYAVDPA QLQALQAALT
     SDPTALLTSQ FLPYFVPGFS PYYAPQIPGA LQSGYLQPMY GMEGLFPYSP ALSRPLMGLS
     PGSLLQQYQQ YQQSLQEAIQ QQQQQQQQQQ QQQQQQQRQL QQQQQQQQQK VQQQQQQQQQ
     PKASQTPVPQ GAASPDKDPA KESPKPEEQK NVPRELSPLL PKPPEEPEAE SKSASADSLC
     DPFIVPKVQY KLVCRKCQAG FGDEEAARSH LKSLCCFGQS VVNLQEMVLH VPTGSGGGGG
     GGGGSGGGGG SYHCLACESA LCGEEALSQH LESALHKHRT ITRAARNAKE HPSLLPHSAC
     FPDPSTASTS QSAAHSNDSP PPPSAAPSSS ASPHASRKSW PPVGSRASAA KPPSFPPLSS
     SSTVTSSSCS TSGVQPSMPT DDYSEESDTD LSQKSDGPAS PVEGPKDPSC PKDSGLTSVG
     TDTFRL
//
ID   BAD_MOUSE               Reviewed;         204 AA.
AC   Q61337;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Bcl2 antagonist of cell death;
DE            Short=BAD;
DE   AltName: Full=Bcl-2-binding component 6;
DE   AltName: Full=Bcl-xL/Bcl-2-associated death promoter;
GN   Name=Bad; Synonyms=Bbc6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain, and Thymus;
RX   MEDLINE=95136361; PubMed=7834748; DOI=10.1016/0092-8674(95)90411-5;
RA   Yang E., Zha J., Jockel J., Boise L.H., Thompson C.B., Korsmeyer S.J.;
RT   "Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and
RT   promotes cell death.";
RL   Cell 80:285-291(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NMRI; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION AT SER-112 AND SER-136, AND MUTAGENESIS OF SER-112 AND
RP   SER-136.
RX   MEDLINE=98022383; PubMed=9381178; DOI=10.1126/science.278.5338.687;
RA   Del Peso L., Gonzalez-Garcia M., Page C., Herrera R., Nunez G.;
RT   "Interleukin-3-induced phosphorylation of BAD through the protein
RT   kinase Akt.";
RL   Science 278:687-689(1997).
RN   [4]
RP   MUTAGENESIS OF SERINE RESIDUES.
RX   MEDLINE=20403302; PubMed=10949026; DOI=10.1016/S1097-2765(00)00006-X;
RA   Datta S.R., Katsov A., Hu L., Petros A., Fesik S.W., Yaffe M.B.,
RA   Greenberg M.E.;
RT   "14-3-3 proteins and survival kinases cooperate to inactivate BAD by
RT   BH3 domain phosphorylation.";
RL   Mol. Cell 6:41-51(2000).
RN   [5]
RP   PHOSPHORYLATION AT SER-170, MUTAGENESIS OF SER-112; SER-155 AND
RP   SER-170, AND MASS SPECTROMETRY.
RX   MEDLINE=21839005; PubMed=11717309; DOI=10.1074/jbc.M109990200;
RA   Dramsi S., Scheid M.P., Maiti A., Hojabrpour P., Chen X., Schubert K.,
RA   Goodlett D.R., Aebersold R., Duronio V.;
RT   "Identification of a novel phosphorylation site, Ser-170, as a
RT   regulator of bad pro-apoptotic activity.";
RL   J. Biol. Chem. 277:6399-6405(2002).
RN   [6]
RP   PHOSPHORYLATION AT SER-112 BY PIM2.
RX   PubMed=12954615; DOI=10.1074/jbc.M307933200;
RA   Yan B., Zemskova M., Holder S., Chin V., Kraft A., Koskinen P.J.,
RA   Lilly M.;
RT   "The PIM-2 kinase phosphorylates BAD on serine 112 and reverses BAD-
RT   induced cell death.";
RL   J. Biol. Chem. 278:45358-45367(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Promotes cell death. Successfully competes for the
CC       binding to Bcl-X(L), Bcl-2 and Bcl-W, thereby affecting the level
CC       of heterodimerization of these proteins with BAX. Can reverse the
CC       death repressor activity of Bcl-X(L), but not that of Bcl-2.
CC       Appears to act as a link between growth factor receptor signaling
CC       and the apoptotic pathways.
CC   -!- SUBUNIT: Forms heterodimers with the anti-apoptotic proteins, Bcl-
CC       X(L), Bcl-2 and Bcl-W. Also binds protein S100A10 (By similarity).
CC       The Ser-112/Ser-136 phosphorylated form binds 14-3-3 proteins.
CC       Interacts with PIM3 (By similarity).
CC   -!- INTERACTION:
CC       P10415:BCL2 (xeno); NbExp=3; IntAct=EBI-400328, EBI-77694;
CC       Q07817:BCL2L1 (xeno); NbExp=1; IntAct=EBI-400328, EBI-78035;
CC       Q07817-1:BCL2L1 (xeno); NbExp=2; IntAct=EBI-400328, EBI-287195;
CC       Q92843:BCL2L2 (xeno); NbExp=1; IntAct=EBI-400328, EBI-707714;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane. Cytoplasm.
CC       Note=Upon phosphorylation, locates to the cytoplasm.
CC   -!- DOMAIN: Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX
CC       for their pro-apoptotic activity and for their interaction with
CC       anti-apoptotic members of the Bcl-2 family.
CC   -!- PTM: Phosphorylated on one or more of Ser-112, Ser-136, Ser-155
CC       and Ser-170 in response to survival stimuli, which blocks its pro-
CC       apoptotic activity. Phosphorylation on Ser-136 or Ser-112 promotes
CC       heterodimerization with 14-3-3 proteins. This interaction then
CC       facilitates the phosphorylation at Ser-155, a site within the BH3
CC       motif, leading to the release of Bcl-X(L) and the promotion of
CC       cell survival. Ser-136 is the major site of AKT/PKB
CC       phosphorylation, Ser-155 the major site of protein kinase A (CAPK)
CC       phosphorylation. Ser-112 is phosphorylated by AKT/PKB, protein
CC       kinase A and PIM2.
CC   -!- SIMILARITY: Belongs to the Bcl-2 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; L37296; AAA64465.1; -; mRNA.
DR   EMBL; BC006762; AAH06762.1; -; mRNA.
DR   IPI; IPI00119986; -.
DR   PIR; A55671; A55671.
DR   RefSeq; NP_031548.1; NM_007522.2.
DR   UniGene; Mm.4387; -.
DR   PDB; 2BZW; X-ray; 2.30 A; B=137-163.
DR   PDBsum; 2BZW; -.
DR   ProteinModelPortal; Q61337; -.
DR   SMR; Q61337; 137-163.
DR   DIP; DIP-273N; -.
DR   IntAct; Q61337; 21.
DR   STRING; Q61337; -.
DR   PhosphoSite; Q61337; -.
DR   PRIDE; Q61337; -.
DR   Ensembl; ENSMUST00000025910; ENSMUSP00000025910; ENSMUSG00000024959.
DR   GeneID; 12015; -.
DR   KEGG; mmu:12015; -.
DR   UCSC; uc008gjn.1; mouse.
DR   CTD; 12015; -.
DR   MGI; MGI:1096330; Bad.
DR   GeneTree; ENSGT00390000010740; -.
DR   HOGENOM; HBG125823; -.
DR   HOVERGEN; HBG001653; -.
DR   InParanoid; Q61337; -.
DR   OMA; SFKGLPR; -.
DR   OrthoDB; EOG42RD8W; -.
DR   PhylomeDB; Q61337; -.
DR   NextBio; 280229; -.
DR   PMAP-CutDB; Q61337; -.
DR   ArrayExpress; Q61337; -.
DR   Bgee; Q61337; -.
DR   CleanEx; MM_BAD; -.
DR   Genevestigator; Q61337; -.
DR   GermOnline; ENSMUSG00000024959; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006915; P:apoptosis; IDA:MGI.
DR   GO; GO:0008283; P:cell proliferation; IDA:MGI.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
DR   GO; GO:0006007; P:glucose catabolic process; IMP:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0008624; P:induction of apoptosis by extracellular signals; IMP:MGI.
DR   GO; GO:0045579; P:positive regulation of B cell differentiation; IMP:MGI.
DR   GO; GO:0045582; P:positive regulation of T cell differentiation; IMP:MGI.
DR   GO; GO:0043281; P:regulation of caspase activity; IMP:MGI.
DR   InterPro; IPR018868; Bcl-2_BAD.
DR   Pfam; PF10514; Bcl-2_BAD; 1.
DR   PROSITE; PS01259; BH3; FALSE_NEG.
PE   1: Evidence at protein level;
KW   3D-structure; Apoptosis; Cytoplasm; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Phosphoprotein.
FT   CHAIN         1    204       Bcl2 antagonist of cell death.
FT                                /FTId=PRO_0000143104.
FT   MOTIF       147    161       BH3.
FT   MOD_RES      67     67       Phosphoserine (By similarity).
FT   MOD_RES     112    112       Phosphoserine; by PKA, PKB and PIM2.
FT   MOD_RES     128    128       Phosphoserine (By similarity).
FT   MOD_RES     136    136       Phosphoserine; by PKA and PKB.
FT   MOD_RES     155    155       Phosphoserine; by PKA and PKB.
FT   MOD_RES     170    170       Phosphoserine.
FT   MUTAGEN     112    112       S->A: Enhances pro-apoptotic activity; no
FT                                phosphorylation.
FT   MUTAGEN     136    136       S->A: No phosphorylation.
FT   MUTAGEN     155    155       S->A: Enhances pro-apoptotic activity; no
FT                                phosphorylation; interacts with Bcl-X(L).
FT   MUTAGEN     155    155       S->D: No pro-apoptotic activity, no
FT                                interaction with Bcl-X(L).
FT   MUTAGEN     170    170       S->A: Enhances pro-apoptotic activity.
FT   MUTAGEN     170    170       S->D: No pro-apoptotic activity; even
FT                                when associated with A-112.
FT   HELIX       139    141
FT   HELIX       142    160
SQ   SEQUENCE   204 AA;  22080 MW;  6C2BA910205053F7 CRC64;
     MGTPKQPSLA PAHALGLRKS DPGIRSLGSD AGGRRWRPAA QSMFQIPEFE PSEQEDASAT
     DRGLGPSLTE DQPGPYLAPG LLGSNIHQQG RAATNSHHGG AGAMETRSRH SSYPAGTEED
     EGMEEELSPF RGRSRSAPPN LWAAQRYGRE LRRMSDEFEG SFKGLPRPKS AGTATQMRQS
     AGWTRIIQSW WDRNLGKGGS TPSQ
//
ID   PGCB_MOUSE              Reviewed;         883 AA.
AC   Q61361;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Brevican core protein;
DE   Flags: Precursor;
GN   Name=Bcan;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=97432816; PubMed=9286696; DOI=10.1006/geno.1997.4853;
RA   Rauch U., Meyer H., Brakebusch C., Seidenbecher C., Gundelfinger E.D.,
RA   Beier D.R., Fassler R.;
RT   "Sequence and chromosomal localization of the mouse brevican gene.";
RL   Genomics 44:15-21(1997).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: May play a role in the terminally differentiating and
CC       the adult nervous system during postnatal development. Could
CC       stabilize interactions between hyaluronan (HA) and brain
CC       proteoglycans.
CC   -!- SUBUNIT: Interacts with TNR (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix (By similarity).
CC   -!- TISSUE SPECIFICITY: Brain (By similarity).
CC   -!- PTM: Contains mostly chondroitin sulfate (By similarity).
CC   -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC   -!- SIMILARITY: Contains 1 C-type lectin domain.
CC   -!- SIMILARITY: Contains 1 EGF-like domain.
CC   -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 2 Link domains.
CC   -!- SIMILARITY: Contains 1 Sushi (CCP/SCR) domain.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=Brevican;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_155";
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DR   EMBL; X87096; CAA60575.1; -; mRNA.
DR   IPI; IPI00623371; -.
DR   PIR; S57653; S57653.
DR   UniGene; Mm.4598; -.
DR   ProteinModelPortal; Q61361; -.
DR   SMR; Q61361; 41-154, 157-255, 258-356, 625-852.
DR   STRING; Q61361; -.
DR   PhosphoSite; Q61361; -.
DR   PRIDE; Q61361; -.
DR   Ensembl; ENSMUST00000090971; ENSMUSP00000088491; ENSMUSG00000004892.
DR   Ensembl; ENSMUST00000107573; ENSMUSP00000103199; ENSMUSG00000004892.
DR   UCSC; uc008pto.1; mouse.
DR   MGI; MGI:1096385; Bcan.
DR   HOGENOM; HBG716672; -.
DR   HOVERGEN; HBG008175; -.
DR   InParanoid; Q61361; -.
DR   OrthoDB; EOG4XGZZW; -.
DR   ArrayExpress; Q61361; -.
DR   Bgee; Q61361; -.
DR   CleanEx; MM_BCAN; -.
DR   Genevestigator; Q61361; -.
DR   GermOnline; ENSMUSG00000004892; Mus musculus.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:MGI.
DR   GO; GO:0005540; F:hyaluronic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0005529; F:sugar binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR   InterPro; IPR002353; AntifreezeII.
DR   InterPro; IPR001304; C-type_lectin.
DR   InterPro; IPR016186; C-type_lectin-like.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; C-type_lectin_fold.
DR   InterPro; IPR016060; Complement_control_module.
DR   InterPro; IPR006209; EGF.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003006; Ig/MHC_CS.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR003596; Ig_V-set_sub.
DR   InterPro; IPR000538; Link.
DR   InterPro; IPR000436; Sushi_SCR_CCP.
DR   Gene3D; G3DSA:3.10.100.10; C-type_lectin-like; 3.
DR   Gene3D; G3DSA:2.10.70.10; Complement_control_module; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF00084; Sushi; 1.
DR   Pfam; PF07686; V-set; 1.
DR   Pfam; PF00193; Xlink; 2.
DR   PRINTS; PR00356; ANTIFREEZEII.
DR   PRINTS; PR01265; LINKMODULE.
DR   SMART; SM00032; CCP; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00406; IGv; 1.
DR   SMART; SM00445; LINK; 2.
DR   SUPFAM; SSF56436; C-type_lectin_fold; 3.
DR   SUPFAM; SSF57535; Complement_control_module; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00290; IG_MHC; 1.
DR   PROSITE; PS01241; LINK_1; 2.
DR   PROSITE; PS50963; LINK_2; 2.
DR   PROSITE; PS50923; SUSHI; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW   Hyaluronic acid; Immunoglobulin domain; Lectin; Phosphoprotein;
KW   Proteoglycan; Repeat; Secreted; Signal; Sushi.
FT   SIGNAL        1     22       Potential.
FT   CHAIN        23    883       Brevican core protein.
FT                                /FTId=PRO_0000017512.
FT   DOMAIN       35    154       Ig-like V-type.
FT   DOMAIN      156    251       Link 1.
FT   DOMAIN      256    353       Link 2.
FT   DOMAIN      622    658       EGF-like.
FT   DOMAIN      658    786       C-type lectin.
FT   DOMAIN      789    849       Sushi.
FT   MOD_RES     546    546       Phosphoserine.
FT   CARBOHYD    129    129       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    336    336       N-linked (GlcNAc...) (Potential).
FT   DISULFID     56    136       By similarity.
FT   DISULFID    178    249       By similarity.
FT   DISULFID    202    223       By similarity.
FT   DISULFID    276    351       By similarity.
FT   DISULFID    300    321       By similarity.
FT   DISULFID    626    637       By similarity.
FT   DISULFID    631    646       By similarity.
FT   DISULFID    648    657       By similarity.
FT   DISULFID    664    675       By similarity.
FT   DISULFID    692    784       By similarity.
FT   DISULFID    760    776       By similarity.
FT   DISULFID    791    834       By similarity.
FT   DISULFID    820    847       By similarity.
SQ   SEQUENCE   883 AA;  96013 MW;  CC2C33C97B453E45 CRC64;
     MIPLLLSLLA ALVLTQAPAA LADDLKEDSS EDRAFRVRIG AAQLRGVLGG ALAIPCHVHH
     LRPPRSRRAA PGFPRVKWTF LSGDREVEVL VARGLRVKVN EAYRFRVALP AYPASLTDVS
     LVLSELRPND SGVYRCEVQH GIDDSSDAVE VKVKGVVFLY REGSARYAFS FAGAQEACAR
     IGARIATPEQ LYAAYLGGYE QCDAGWLSDQ TVRYPIQNPR EACSGDMDGY PGVRNYGVVG
     PDDLYDVYCY AEDLNGELFL GAPPSKLTWE EARDYCLERG AQIASTGQLY AAWNGGLDRC
     SPGWLADGSV RYPIITPSQR CGGGLPGVKT LFLFPNQTGF PSKQNRFNVY CFRDSAHPSA
     SSEASSPASD GLEAIVTVTE KLEELQLPQE AMESESRGAI YSIPISEDGG GGSSTPEDPA
     EAPRTPLESE TQSIAPPTES SEEEGVALEE EERFKDLEAL EEEKEQEDLW VWPRELSSPL
     PTGSETEHSL SQVSPPAQAV LQLDASPSPG PPRFRGPPAE TLLPPREWSA TSTPGGAREV
     GGETGSPELS GVPRESEEAG SSSLEDGPSL LPATWAPVGP RELETPSEEK SGRTVLAGTS
     VQAQPVLPTD SASHGGVAVA PSSGDCIPSP CHNGGTCLEE KEGFRCLCLP GYGGDLCDVG
     LHFCSPGWEA FQGACYKHFS TRRSWEEAES QCRALGAHLT SICTPEEQDF VNDRYREYQW
     IGLNDRTIEG DFLWSDGAPL LYENWNPGQP DSYFLSGENC VVMVWHDQGQ WSDVPCNYHL
     SYTCKMGLVS CGPPPQLPLA QIFGRPRLRY AVDTVLRYRC RDGLAQRNLP LIRCQENGLW
     EAPQISCVPR RPGRALRSMD APEGPRGQLS RHRKAPLTPP SSL
//
ID   KGP2_MOUSE              Reviewed;         762 AA.
AC   Q61410;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=cGMP-dependent protein kinase 2;
DE            Short=cGK 2;
DE            Short=cGK2;
DE            EC=2.7.11.12;
DE   AltName: Full=cGMP-dependent protein kinase II;
DE            Short=cGKII;
GN   Name=Prkg2; Synonyms=Prkgr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=93293885; PubMed=8514791;
RA   Uhler M.D.;
RT   "Cloning and expression of a novel cyclic GMP-dependent protein kinase
RT   from mouse brain.";
RL   J. Biol. Chem. 268:13586-13591(1993).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Binding of cGMP results in enzyme activation.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. cGMP subfamily.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 2 cyclic nucleotide-binding domains.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; L12460; AAA02572.1; -; mRNA.
DR   IPI; IPI00121070; -.
DR   PIR; A46590; A46590.
DR   UniGene; Mm.263002; -.
DR   ProteinModelPortal; Q61410; -.
DR   SMR; Q61410; 118-403, 447-762.
DR   STRING; Q61410; -.
DR   PhosphoSite; Q61410; -.
DR   PRIDE; Q61410; -.
DR   Ensembl; ENSMUST00000031277; ENSMUSP00000031277; ENSMUSG00000029334.
DR   MGI; MGI:108173; Prkg2.
DR   GeneTree; ENSGT00550000074358; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG006211; -.
DR   InParanoid; Q61410; -.
DR   OrthoDB; EOG4V6ZFZ; -.
DR   PhylomeDB; Q61410; -.
DR   BRENDA; 2.7.11.12; 244.
DR   ArrayExpress; Q61410; -.
DR   Bgee; Q61410; -.
DR   CleanEx; MM_PRKG2; -.
DR   Genevestigator; Q61410; -.
DR   GermOnline; ENSMUSG00000029334; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004692; F:cGMP-dependent protein kinase activity; IEA:EC.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR016232; cGMP-dependent_protein_kinase.
DR   InterPro; IPR002374; cGMP_dep__kinase.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 2.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF000559; cGMP-dep_kinase; 1.
DR   PRINTS; PR00104; CGMPKINASE.
DR   SMART; SM00100; cNMP; 2.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF51206; cNMP_binding; 2.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; 2.
DR   PROSITE; PS00889; CNMP_BINDING_2; 2.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; cGMP; cGMP-binding; Kinase; Nucleotide-binding;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    762       cGMP-dependent protein kinase 2.
FT                                /FTId=PRO_0000086124.
FT   DOMAIN      453    711       Protein kinase.
FT   DOMAIN      712    762       AGC-kinase C-terminal.
FT   NP_BIND     168    285       cGMP 1.
FT   NP_BIND     286    417       cGMP 2.
FT   NP_BIND     459    467       ATP (By similarity).
FT   ACT_SITE    576    576       Proton acceptor (By similarity).
FT   BINDING     482    482       ATP (By similarity).
SQ   SEQUENCE   762 AA;  87085 MW;  74F9D9A6835711A5 CRC64;
     MGNGSVKPKH AKHPDGHSGN LSNEALRSKV LELERELRRK DAELQEREYH LKELREQLAK
     QTVAIAELTE ELQSKCIQLN KLQDVIHVQG GSPLQASPDK VPLDVHRKTS GLVSLHSRRG
     AKAGVSAEPT TRTYDLNKPP EFSFEKARVR KDSSEKKLIT DALNKNQFLK RLDPQQIKDM
     VECMYGEKLS TGSYVIKQGE PGNHIFVLAE GRLEVFQGEK LLSSIPMWTT FGELAILYNC
     TRTASVKAIT NVKTWALDRE VFQNIMRRTA QARDEEYRNF LRSVSLLKNL PEDKLTKIID
     CLEVEYYDKG DYIIREGEEG STFFILAKGK VKVTQSTEGH DQPQLIKTLQ KGEYFGEKAL
     ISDDVRSANI IAEENDVACL VIDRETFNQT VGTFDELQKY LEGYVATLNR DDEKRHAKRS
     MSSWKLSKAL SLEMIQLKEK VARFSSTSPF QNLEIIATLG VGGFGRVELV KVKNENVAFA
     MKCIRKKHIV DTKQQEHVYS EKRILEELCS PFIVKLYRTF KDNKYVYMLL EACLGGELWS
     ILRDRGSFDE PTSKFCVACV TEAFDYLHLL GIIYRDLKPE NLILDADGYL KLVDFGFAKK
     IGSGQKTWTF CGTPEYVAPE VILNKGHDFS VDFWSLGILV YELLTGNPPF SGIDQMMTYN
     LILKGIEKMD FPRKITRRPE DLIRRLCRQN PTERLGNLKN GINDIKKHRW LNGFNWEGLK
     ARSLPSPLRR ELSGPIDHSY FDKYPPEKGV PPDEMSGWDK DF
//
ID   ZN638_MOUSE             Reviewed;        1960 AA.
AC   Q61464; Q6DFV9; Q8C941;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Zinc finger protein 638;
DE   AltName: Full=Nuclear protein 220;
DE   AltName: Full=Zinc finger matrin-like protein;
GN   Name=Znf638; Synonyms=Np220, Zfml;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5 AND 6).
RC   TISSUE=Heart;
RX   MEDLINE=96264657; PubMed=8670298; DOI=10.1006/bbrc.1996.0910;
RA   Matsushima Y., Ohshima M., Sonoda M., Kitagawa Y.;
RT   "A family of novel DNA-binding nuclear proteins having polypyrimidine
RT   tract-binding motif and arginine/serine-rich motif.";
RL   Biochem. Biophys. Res. Commun. 223:427-433(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Head;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 761-768; 873-891; 1395-1404; 1506-1513 AND
RP   1874-1881, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Binds to cytidine clusters in double-stranded DNA.
CC   -!- SUBUNIT: Interacts with FHL2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1; Synonyms=Alpha;
CC         IsoId=Q61464-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q61464-2; Sequence=VSP_014809, VSP_014812, VSP_014813,
CC                                  VSP_014814;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q61464-3; Sequence=VSP_014807, VSP_014808;
CC         Note=No experimental confirmation available;
CC       Name=4; Synonyms=Beta;
CC         IsoId=Q61464-4; Sequence=VSP_014814;
CC       Name=5; Synonyms=Gamma;
CC         IsoId=Q61464-5; Sequence=VSP_014811;
CC       Name=6; Synonyms=Delta;
CC         IsoId=Q61464-7; Sequence=VSP_014810;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 matrin-type zinc finger.
CC   -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
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DR   EMBL; D83033; BAA11749.1; -; mRNA.
DR   EMBL; AK043029; BAC31439.1; -; mRNA.
DR   EMBL; BC076615; AAH76615.1; -; mRNA.
DR   IPI; IPI00121264; -.
DR   IPI; IPI00607921; -.
DR   IPI; IPI00607987; -.
DR   IPI; IPI00608012; -.
DR   IPI; IPI00608089; -.
DR   IPI; IPI00608115; -.
DR   PIR; JC4842; JC4842.
DR   RefSeq; NP_001159843.1; NM_001166371.1.
DR   RefSeq; NP_032743.2; NM_008717.3.
DR   UniGene; Mm.132392; -.
DR   ProteinModelPortal; Q61464; -.
DR   SMR; Q61464; 668-754.
DR   STRING; Q61464; -.
DR   PhosphoSite; Q61464; -.
DR   PRIDE; Q61464; -.
DR   Ensembl; ENSMUST00000032088; ENSMUSP00000032088; ENSMUSG00000030016.
DR   Ensembl; ENSMUST00000089597; ENSMUSP00000087024; ENSMUSG00000030016.
DR   Ensembl; ENSMUST00000113834; ENSMUSP00000109465; ENSMUSG00000030016.
DR   Ensembl; ENSMUST00000113835; ENSMUSP00000109466; ENSMUSG00000030016.
DR   Ensembl; ENSMUST00000113836; ENSMUSP00000109467; ENSMUSG00000030016.
DR   GeneID; 18139; -.
DR   KEGG; mmu:18139; -.
DR   UCSC; uc009con.1; mouse.
DR   UCSC; uc009coo.1; mouse.
DR   UCSC; uc009coq.1; mouse.
DR   CTD; 18139; -.
DR   MGI; MGI:1203484; Zfml.
DR   GeneTree; ENSGT00590000083029; -.
DR   HOGENOM; HBG126722; -.
DR   HOVERGEN; HBG094186; -.
DR   InParanoid; Q61464; -.
DR   OrthoDB; EOG4GXFKV; -.
DR   NextBio; 293380; -.
DR   ArrayExpress; Q61464; -.
DR   Bgee; Q61464; -.
DR   CleanEx; MM_ZFML; -.
DR   Genevestigator; Q61464; -.
DR   GermOnline; ENSMUSG00000030016; Mus musculus.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR000690; Znf_C2H2_matrin.
DR   InterPro; IPR003604; Znf_U1.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   SMART; SM00360; RRM; 2.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SMART; SM00451; ZnF_U1; 2.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50171; ZF_MATRIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing; DNA-binding;
KW   Metal-binding; Nucleus; Phosphoprotein; Repeat; RNA-binding; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1960       Zinc finger protein 638.
FT                                /FTId=PRO_0000082012.
FT   DOMAIN      676    751       RRM 1.
FT   DOMAIN      902    976       RRM 2.
FT   ZN_FING    1876   1906       Matrin-type.
FT   COMPBIAS    470    575       Arg-rich.
FT   COMPBIAS   1577   1582       Poly-Lys.
FT   MOD_RES     125    125       Phosphothreonine (By similarity).
FT   MOD_RES     128    128       Phosphoserine (By similarity).
FT   MOD_RES     381    381       Phosphoserine (By similarity).
FT   MOD_RES     418    418       Phosphoserine (By similarity).
FT   MOD_RES     506    506       Phosphoserine (By similarity).
FT   MOD_RES     508    508       Phosphoserine (By similarity).
FT   MOD_RES     518    518       Phosphoserine (By similarity).
FT   MOD_RES     520    520       Phosphoserine (By similarity).
FT   MOD_RES     554    554       Phosphoserine (By similarity).
FT   MOD_RES     560    560       Phosphoserine (By similarity).
FT   MOD_RES     562    562       Phosphoserine (By similarity).
FT   MOD_RES     606    606       Phosphoserine (By similarity).
FT   MOD_RES     770    770       Phosphoserine (By similarity).
FT   MOD_RES     801    801       Phosphoserine (By similarity).
FT   MOD_RES    1099   1099       Phosphoserine (By similarity).
FT   MOD_RES    1400   1400       Phosphoserine (By similarity).
FT   MOD_RES    1809   1809       Phosphoserine (By similarity).
FT   MOD_RES    1864   1864       Phosphoserine (By similarity).
FT   VAR_SEQ     438    454       DWIQHQNTSTHIESCRQ -> VSVFKRLLYNDAQCPGF
FT                                (in isoform 3).
FT                                /FTId=VSP_014807.
FT   VAR_SEQ     456   1960       Missing (in isoform 3).
FT                                /FTId=VSP_014808.
FT   VAR_SEQ     810    832       Missing (in isoform 2).
FT                                /FTId=VSP_014809.
FT   VAR_SEQ    1147   1866       Missing (in isoform 6).
FT                                /FTId=VSP_014810.
FT   VAR_SEQ    1147   1832       Missing (in isoform 5).
FT                                /FTId=VSP_014811.
FT   VAR_SEQ    1147   1200       KEEPKQALCESDFAIQTLELEAQGAEVSIEIPLVASTPANI
FT                                ELFSENIDESALN -> PGSETVTQKDLKTMPERHLAAKTP
FT                                MKRVRIGKSSPSQKVAEPTKGEEAFQMSEG (in
FT                                isoform 2).
FT                                /FTId=VSP_014812.
FT   VAR_SEQ    1201   1832       Missing (in isoform 2).
FT                                /FTId=VSP_014813.
FT   VAR_SEQ    1833   1866       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_014814.
FT   CONFLICT     32     32       V -> L (in Ref. 3; AAH76615).
SQ   SEQUENCE   1960 AA;  218134 MW;  27DF6740BFE410ED CRC64;
     MSRPRFNPRG TFPLQRPRAP NPPGMRPPGP FVRPGSMGLP RFYPAGRARG IPHRFPGHGS
     YQNMGPQRMN VQVTQHRTDP RLTKEKLDFP EAQQKKGKPH GSRWDDESHI TPPVEVKQSS
     VTQVTEQSPK VQSRYTKESA SSILASFGLS NEDLEELSRY PDEQLTPENM PLILRDIRMR
     KMSRRLPNLP SHSRNKETLS NETVSSNVID YGHASKYGYT EDPLEVRIYD PEIPTDEVKN
     EFQPQQSISA TVSTPNVICN SVFPGGDMFR QMDFPGESSS QSFFPVESGT KMSGLHISGQ
     SVLEPVKSIS QSISQTVSQT TSQSLNPPSM NQVPFTFELD AVLRQQERIS QKSVISSADA
     HGGPTESKKD YQSEADLPIR SPFGIVKASW LPKFTQAGAQ KMKRLPTPSM MNDYYAASPR
     IFPHLCSLCN VECSHLKDWI QHQNTSTHIE SCRQLRQQYP DWNPEILPSR RNESNRKENE
     TPRRRSHSPS PRHSRRSSSG HRIRRSRSPV RYIYRPRSRS PRICHRFISK YRSRSRSRSR
     SRSPYRSRNL LRRSPKSYRS ASPERTSRKS VRSDRKKALE DGGQRSVHGT EVTKQKHTET
     VDKGLSPAQK PKLASGTKPS AKSLSSVKSD SHLGAYSAHK SENLEDDTLP EGKQESGKSA
     LAQRKPQKDQ SLSSNSILLV SELPEDGFTE EDIRKAFLPF GKISDVLLVP CRNEAYLEME
     LRKAVTSIMK YIETMPLVIK GKSVKVCVPG KKKPQNKEMK KKPSDIKKSS ASALKKETDA
     SKTMETVSSS SSAKSGQIKS STVKVNKCAG KSAGSVKSVV TVAAKGKASI KTAKSGKKSL
     EAKKSGNIKN KDSNKPVTVP ANSEIKASSE DKATGKSAEE SPSGTLEATE KEPVNKESEE
     MSVVFISNLP NKGYSTEEIY NLAKPFGALK DILVLSSHKK AYIEINKKSA DSMVKFYTCF
     PISMDGNQLS ISMAPEHVDL KDEEALFTTL IQENDPEANI DKIYNRFVHL DNLPEDGLQC
     VLCVGHQFGK VDRYMFMSNK NKVILQLESP ESALSMYNFL KQNPQNIGEH VLTCTLSPKT
     DSEVQRKNDL ELGKGSTFSP DLKNSPVDES EVQTAADSSS VKPSEVEEET TSNIGTETSV
     HQEELGKEEP KQALCESDFA IQTLELEAQG AEVSIEIPLV ASTPANIELF SENIDESALN
     QQMYTSDFEK EEAEVTNPET ELAVSDSVFI EERNIKGIIE DSPSETEDIF SGIVQPMVDA
     IAEVDKHETV SEVLPSACNV TQAPGSYIED EKVVSKKDIA EKVILDEKEE DEFNVKETRM
     DLQVKTEKAE KNEAIIFKEK LEKIIAAIRE KPIESSVIKA DPTKGLDQTS KPDETGKSSV
     LTVSNVYSSK SSIKATVVSS PKAKSTPSKT ESHSTFPKPV LREQIKADKK VSAKEFGLLK
     NTRSGLAESN SKSKPTQIGV NRGCSGRISA LQCKDSKVDY KDITKQSQET ETKPPIMKRD
     DSNNKALALQ NTKNSKSTTD RSSKSKEEPL FTFNLDEFVT VDEVIEEVNP SQAKQNPLKG
     KRKEALKISP SPELNLKKKK GKTSVPHSVE GELSFVTLDE IGEEEDATVQ ALVTVDEVID
     EEELNMEEMV KNSNSLLTLD ELIDQDDCIP HSGPKDVTVL SMAEEQDLQQ ERLVTVDEIG
     EVEESADITF ATLNAKRDKR DSIGFISSQM PEDPSTLVTV DEIQDDSSDF HLMTLDEVTE
     EDENSLADFN NLKEELNFVT VDEVGDEEDG DNDSKVELAR GKIEHHTDKK GNRKRRAVDP
     KKSKLDSFSQ VGPGSETVTQ KDLKTMPERH LAAKTPMKRV RLGKSSPSQK VAEPTKGEEA
     FQMSEGVDDA ELKDSEPDEK RRKTQDSSVG KSMTSDVPGD LDFLVPKAGF FCPICSLFYS
     GEKAMANHCK STRHKQNTEK FMAKQRKEKE QNETEERSSR
//
ID   LPP1_MOUSE              Reviewed;         283 AA.
AC   Q61469; Q61690; Q6GT30; Q8BPB8;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Lipid phosphate phosphohydrolase 1;
DE            EC=3.1.3.4;
DE   AltName: Full=35 kDa PAP;
DE            Short=mPAP;
DE   AltName: Full=Hydrogen peroxide-inducible protein 53;
DE            Short=Hic53;
DE   AltName: Full=PAP2-alpha;
DE   AltName: Full=Phosphatidate phosphohydrolase type 2a;
DE   AltName: Full=Phosphatidic acid phosphatase 2a;
DE            Short=PAP-2a;
DE            Short=PAP2a;
GN   Name=Ppap2a; Synonyms=Hpic53, Lpp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
RC   TISSUE=Calvaria;
RX   MEDLINE=96032549; PubMed=7556647; DOI=10.1016/0014-5793(95)00957-B;
RA   Egawa K., Yoshiwara M., Shibanuma M., Nose K.;
RT   "Isolation of a novel ras-recision gene that is induced by hydrogen
RT   peroxide from a mouse osteoblastic cell line, MC3T3-E1.";
RL   FEBS Lett. 372:74-77(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Kidney;
RX   MEDLINE=96324980; PubMed=8702556; DOI=10.1074/jbc.271.31.18931;
RA   Kai M., Wada I., Imai S., Sakane F., Kanoh H.;
RT   "Identification and cDNA cloning of 35-kDa phosphatidic acid
RT   phosphatase (type 2) bound to plasma membranes.";
RL   J. Biol. Chem. 271:18931-18938(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=FVB/N;
RA   Yokoyama K., Tigyi G.;
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   CHARACTERIZATION.
RC   TISSUE=Liver;
RX   MEDLINE=99289308; PubMed=10359651; DOI=10.1042/0264-6021:3400677;
RA   Jasinska R., Zhang Q.-X., Pilquil C., Singh I., Xu J., Dewald J.,
RA   Dillon D.A., Berthiaume L.G., Carman G.M., Waggoner D.W.,
RA   Brindley D.N.;
RT   "Lipid phosphate phosphohydrolase-1 degrades exogenous glycerolipid
RT   and sphingolipid phosphate esters.";
RL   Biochem. J. 340:677-686(1999).
RN   [7]
RP   SUBUNIT.
RX   PubMed=14725715; DOI=10.1186/1471-2091-5-2;
RA   Burnett C., Makridou P., Hewlett L., Howard K.;
RT   "Lipid phosphate phosphatases dimerise, but this interaction is not
RT   required for in vivo activity.";
RL   BMC Biochem. 5:2-2(2004).
RN   [8]
RP   OVEREXPRESSION.
RX   PubMed=14687668; DOI=10.1016/j.cellsig.2003.08.012;
RA   Yue J., Yokoyama K., Balazs L., Baker D.L., Smalley D., Pilquil C.,
RA   Brindley D.N., Tigyi G.;
RT   "Mice with transgenic overexpression of lipid phosphate phosphatase-1
RT   display multiple organotypic deficits without alteration in
RT   circulating lysophosphatidate level.";
RL   Cell. Signal. 16:385-399(2004).
CC   -!- FUNCTION: Broad-specificity phosphohydrolase that dephosphorylates
CC       exogenous bioactive glycerolipids and sphingolipids. Catalyzes the
CC       conversion of phosphatidic acid (PA) to diacylglycerol (DG). In
CC       addition it hydrolyzes lysophosphatidic acid (LPA), diacyl
CC       glycerol pyrophosphate (DGPP), ceramide-1-phosphate (C-1-P) and
CC       sphingosine-1-phosphate (S-1-P). The relative catalytic efficiency
CC       is LPA > PA > C-1-P > S-1-P.
CC   -!- CATALYTIC ACTIVITY: A 1,2-diacylglycerol 3-phosphate + H(2)O = a
CC       1,2-diacyl-sn-glycerol + phosphate.
CC   -!- SUBUNIT: Homodimer. This complex seems not to be involved in
CC       substrate recognition, it may confer only structural or functional
CC       stability.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Note=Found predominantly in plasma membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q61469-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q61469-2; Sequence=VSP_009652;
CC   -!- TISSUE SPECIFICITY: Highly expressed in kidney and lung. Almost
CC       undetectable in brain, heart, bone, muscle or spleen.
CC   -!- INDUCTION: Moderately, by hydrogen peroxide, calcium ionophore and
CC       dexamethasone.
CC   -!- PTM: N-glycosylated. Contains high-mannose oligosaccharide.
CC   -!- MISCELLANEOUS: Overexpression elicited a number of phenotypic
CC       alteration without affecting several aspects of LPA signaling.
CC       Phenotypic abnormalities affect primarily three organs: the liver,
CC       the skin, and the reproductive organs. There is a reduction on
CC       body size, birth weight, abnormalities in fur growth, and a
CC       severely impaired spermatogenesis.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA85353.1; Type=Frameshift; Positions=Several;
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DR   EMBL; L43371; AAA85353.1; ALT_SEQ; mRNA.
DR   EMBL; D84376; BAA12335.1; -; mRNA.
DR   EMBL; AY247795; AAP04434.1; -; mRNA.
DR   EMBL; AY247796; AAP04435.1; -; mRNA.
DR   EMBL; AK077275; BAC36724.1; -; mRNA.
DR   EMBL; BC061161; AAH61161.1; -; mRNA.
DR   IPI; IPI00223459; -.
DR   IPI; IPI00407419; -.
DR   PIR; S66668; S66668.
DR   RefSeq; NP_032273.1; NM_008247.2.
DR   RefSeq; NP_032929.1; NM_008903.1.
DR   UniGene; Mm.317186; -.
DR   ProteinModelPortal; Q61469; -.
DR   SMR; Q61469; 113-240.
DR   STRING; Q61469; -.
DR   PhosphoSite; Q61469; -.
DR   PRIDE; Q61469; -.
DR   Ensembl; ENSMUST00000016144; ENSMUSP00000016144; ENSMUSG00000021759.
DR   Ensembl; ENSMUST00000070951; ENSMUSP00000064423; ENSMUSG00000021759.
DR   GeneID; 19012; -.
DR   KEGG; mmu:19012; -.
DR   NMPDR; fig|10090.3.peg.28430; -.
DR   UCSC; uc007rwq.1; mouse.
DR   CTD; 19012; -.
DR   MGI; MGI:108412; Ppap2a.
DR   eggNOG; roNOG15797; -.
DR   HOVERGEN; HBG002048; -.
DR   OMA; PPYRRGF; -.
DR   OrthoDB; EOG4RR6J5; -.
DR   PhylomeDB; Q61469; -.
DR   BRENDA; 3.1.3.4; 244.
DR   NextBio; 295422; -.
DR   ArrayExpress; Q61469; -.
DR   Bgee; Q61469; -.
DR   CleanEx; MM_PPAP2A; -.
DR   Genevestigator; Q61469; -.
DR   GermOnline; ENSMUSG00000021759; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:MGI.
DR   GO; GO:0005624; C:membrane fraction; ISS:UniProtKB.
DR   GO; GO:0008195; F:phosphatidate phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0006672; P:ceramide metabolic process; TAS:MGI.
DR   GO; GO:0006651; P:diacylglycerol biosynthetic process; TAS:MGI.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
DR   GO; GO:0007165; P:signal transduction; TAS:MGI.
DR   GO; GO:0006670; P:sphingosine metabolic process; TAS:MGI.
DR   InterPro; IPR016118; P_Acid_Pase/Cl_peroxidase_N.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   Gene3D; G3DSA:1.20.144.10; P_Acid_Pase/Cl_peroxidase_N; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; AcPase_VanPerase; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Glycoprotein; Hydrolase;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    283       Lipid phosphate phosphohydrolase 1.
FT                                /FTId=PRO_0000220906.
FT   TOPO_DOM      1      6       Cytoplasmic (Potential).
FT   TRANSMEM      7     27       Helical; (Potential).
FT   TOPO_DOM     28     53       Extracellular (Potential).
FT   TRANSMEM     54     74       Helical; (Potential).
FT   TOPO_DOM     75     88       Cytoplasmic (Potential).
FT   TRANSMEM     89    109       Helical; (Potential).
FT   TOPO_DOM    110    164       Extracellular (Potential).
FT   TRANSMEM    165    185       Helical; (Potential).
FT   TOPO_DOM    186    199       Cytoplasmic (Potential).
FT   TRANSMEM    200    220       Helical; (Potential).
FT   TOPO_DOM    221    229       Extracellular (Potential).
FT   TRANSMEM    230    250       Helical; (Potential).
FT   TOPO_DOM    251    283       Cytoplasmic (Potential).
FT   CARBOHYD    142    142       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ      21     70       GLPFAILTSRHTPFQRGIFCNDDSIKYPYKEDTIPYALLGG
FT                                IVIPFCIIV -> AMPMTILKLGKVYPFQRGFFCTDNSVKY
FT                                PYHDSTIPSRILAILGLGLPIFS (in isoform 2).
FT                                /FTId=VSP_009652.
SQ   SEQUENCE   283 AA;  31892 MW;  669690568E549CC6 CRC64;
     MFDKTRLPYV ALDVICVLLA GLPFAILTSR HTPFQRGIFC NDDSIKYPYK EDTIPYALLG
     GIVIPFCIIV MSIGESLSVY FNVLHSNSFV GNPYIATIYK AVGAFLFGVS ASQSLTDIAK
     YTIGSLRPHF LAICNPDWSK INCSDGYIED YICQGNEEKV KEGRLSFYSG HSSFSMYCML
     FVALYLQARM KGDWARLLRP MLQFGLIAFS IYVGLSRVSD YKHHWSDVTV GLIQGAAMAI
     LVALYVSDFF KDTHSYKERK EEDPHTTLHE TASSRNYSTN HEP
//
ID   MSI1H_MOUSE             Reviewed;         362 AA.
AC   Q61474; Q8BNC7;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=RNA-binding protein Musashi homolog 1;
DE            Short=Musashi-1;
GN   Name=Msi1; Synonyms=Msi1h;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), RNA-BINDING, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=ICR; TISSUE=Cerebellum;
RX   MEDLINE=96239577; PubMed=8660864; DOI=10.1006/dbio.1996.0130;
RA   Sakakibara S., Imai T., Hamaguchi K., Okabe M., Aruga J., Nakajima K.,
RA   Yasutomi D., Nagata T., Kurihara Y., Uesugi S., Miyata T., Ogawa M.,
RA   Mikoshiba K., Okano H.;
RT   "Mouse-Musashi-1, a neural RNA-binding protein highly enriched in the
RT   mammalian CNS stem cell.";
RL   Dev. Biol. 176:230-242(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   FUNCTION, AND MUTAGENESIS OF PHE-63; PHE-65 AND PHE-68.
RX   PubMed=11359897; DOI=10.1128/MCB.21.12.3888-3900.2001;
RA   Imai T., Tokunaga A., Yoshida T., Hashimoto M., Mikoshiba K.,
RA   Weinmaster G., Nakafuku M., Okano H.;
RT   "The neural RNA-binding protein Musashi1 translationally regulates
RT   mammalian numb gene expression by interacting with its mRNA.";
RL   Mol. Cell. Biol. 21:3888-3900(2001).
RN   [4]
RP   FUNCTION.
RX   PubMed=12407178; DOI=10.1073/pnas.232087499;
RA   Sakakibara S., Nakamura Y., Yoshida T., Shibata S., Koike M.,
RA   Takano H., Ueda S., Uchiyama Y., Noda T., Okano H.;
RT   "RNA-binding protein Musashi family: roles for CNS stem cells and a
RT   subpopulation of ependymal cells revealed by targeted disruption and
RT   antisense ablation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:15194-15199(2002).
RN   [5]
RP   STRUCTURE BY NMR OF 110-184, AND INTERACTION WITH RNA.
RX   PubMed=10080895; DOI=10.1006/jmbi.1999.2596;
RA   Nagata T., Kanno R., Kurihara Y., Uesugi S., Imai T., Sakakibara S.,
RA   Okano H., Katahira M.;
RT   "Structure, backbone dynamics and interactions with RNA of the C-
RT   terminal RNA-binding domain of a mouse neural RNA-binding protein,
RT   Musashi1.";
RL   J. Mol. Biol. 287:315-330(1999).
RN   [6]
RP   STRUCTURE BY NMR OF 20-96, AND INTERACTION WITH RNA.
RX   PubMed=12907678; DOI=10.1074/jbc.M306210200;
RA   Miyanoiri Y., Kobayashi H., Imai T., Watanabe M., Nagata T.,
RA   Uesugi S., Okano H., Katahira M.;
RT   "Origin of higher affinity to RNA of the N-terminal RNA-binding domain
RT   than that of the C-terminal one of a mouse neural protein, musashi1,
RT   as revealed by comparison of their structures, modes of interaction,
RT   surface electrostatic potentials, and backbone dynamics.";
RL   J. Biol. Chem. 278:41309-41315(2003).
CC   -!- FUNCTION: RNA binding protein that regulates the expression of
CC       target mRNAs at the translation level. Regulates expression of the
CC       NOTCH1 antagonist NUMB. Binds RNA containing the sequence 5'-
CC       GUUAGUUAGUUAGUU-3' and other sequences containing the pattern 5'-
CC       [GA]U(1-3)AGU-3'. May play a role in the proliferation and
CC       maintenance of stem cells in the central nervous system.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q61474-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q61474-2; Sequence=VSP_011166, VSP_011167;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Detected in olfactory bulb, brain stem, small
CC       intestine, and at low levels in brain cortex, hippocampus and
CC       ovary. Detected in neural progenitor cells, including neural stem
CC       cells.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in embryonic brain at day
CC       12. Expressed at intermediate levels during the rest of embryonic
CC       development and in newborns up to day 3. After this expression
CC       decreases and stabilizes at low levels of expression around day
CC       13.
CC   -!- DOMAIN: The first RNA recognition motif binds more strongly to RNA
CC       compared to the second one.
CC   -!- SIMILARITY: Belongs to the Musashi family.
CC   -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; D49654; BAA08530.1; -; mRNA.
DR   EMBL; AK084019; BAC39099.1; -; mRNA.
DR   IPI; IPI00121300; -.
DR   IPI; IPI00462260; -.
DR   RefSeq; NP_032655.1; NM_008629.1.
DR   UniGene; Mm.5077; -.
DR   PDB; 1UAW; NMR; -; A=20-96.
DR   PDB; 2MSS; NMR; -; A=110-184.
DR   PDB; 2MST; NMR; -; A=110-184.
DR   PDBsum; 1UAW; -.
DR   PDBsum; 2MSS; -.
DR   PDBsum; 2MST; -.
DR   ProteinModelPortal; Q61474; -.
DR   SMR; Q61474; 18-187.
DR   STRING; Q61474; -.
DR   PhosphoSite; Q61474; -.
DR   PRIDE; Q61474; -.
DR   Ensembl; ENSMUST00000067168; ENSMUSP00000070415; ENSMUSG00000054256.
DR   GeneID; 17690; -.
DR   KEGG; mmu:17690; -.
DR   UCSC; uc008zdu.1; mouse.
DR   UCSC; uc008zdv.1; mouse.
DR   CTD; 17690; -.
DR   MGI; MGI:107376; Msi1.
DR   eggNOG; roNOG08785; -.
DR   GeneTree; ENSGT00560000076532; -.
DR   HOGENOM; HBG756718; -.
DR   HOVERGEN; HBG002295; -.
DR   InParanoid; Q61474; -.
DR   OMA; TTQEGLR; -.
DR   OrthoDB; EOG48GW3J; -.
DR   NextBio; 292270; -.
DR   ArrayExpress; Q61474; -.
DR   Bgee; Q61474; -.
DR   CleanEx; MM_MSI1; -.
DR   Genevestigator; Q61474; -.
DR   GermOnline; ENSMUSG00000054256; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005844; C:polysome; IDA:MGI.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0008266; F:poly(U) RNA binding; IDA:MGI.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm; Nucleus;
KW   Phosphoprotein; Repeat; RNA-binding.
FT   CHAIN         1    362       RNA-binding protein Musashi homolog 1.
FT                                /FTId=PRO_0000081650.
FT   DOMAIN       20    110       RRM 1.
FT   DOMAIN      109    186       RRM 2.
FT   COMPBIAS    274    281       Poly-Ala.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      12     12       Phosphoserine (By similarity).
FT   MOD_RES     191    191       Phosphoserine (By similarity).
FT   VAR_SEQ       1     21       Missing (in isoform 2).
FT                                /FTId=VSP_011166.
FT   VAR_SEQ     264    362       AIPLTAYGPMAAAAAAAAVVRGTGSHPWTMAPPPGSTPSRT
FT                                GGFLGTTSPGPMAELYGAANQDSGVSSYISAASPAPSTGFG
FT                                HSLGGPLIATAFTNGYH -> GQWLRFRASHRPRGEKGGER
FT                                DCPLPRGEAGRTTVPGHWPVSSATWPSRVGREAKPGRRR
FT                                (in isoform 2).
FT                                /FTId=VSP_011167.
FT   MUTAGEN      63     63       F->L: Abolishes RNA binding; when
FT                                associated with L-65 and L-68.
FT   MUTAGEN      65     65       F->L: Abolishes RNA binding; when
FT                                associated with L-63 and L-68.
FT   MUTAGEN      68     68       F->L: Abolishes RNA binding; when
FT                                associated with L-63 and L-65.
FT   STRAND       22     26
FT   HELIX        34     40
FT   TURN         41     43
FT   STRAND       49     52
FT   STRAND       57     59
FT   STRAND       61     66
FT   HELIX        73     79
FT   TURN         80     82
FT   STRAND       91     94
FT   STRAND      111    114
FT   HELIX       122    130
FT   STRAND      136    138
FT   STRAND      144    146
FT   STRAND      151    156
FT   HELIX       160    167
FT   STRAND      168    170
FT   STRAND      174    176
FT   STRAND      180    182
SQ   SEQUENCE   362 AA;  39119 MW;  75C316BB384AE211 CRC64;
     METDAPQPGL ASPDSPHDPC KMFIGGLSWQ TTQEGLREYF GQFGEVKECL VMRDPLTKRS
     RGFGFVTFMD QAGVDKVLAQ SRHELDSKTI DPKVAFPRRA QPKMVTRTKK IFVGGLSVNT
     TVEDVKHYFE QFGKVDDAML MFDKTTNRHR GFGFVTFESE DIVEKVCEIH FHEINNKMVE
     CKKAQPKEVM SPTGSARGRS RVMPYGMDAF MLGIGMLGYP GFQATTYASR SYTGLAPGYT
     YQFPEFRVER SPLPSAPVLP ELTAIPLTAY GPMAAAAAAA AVVRGTGSHP WTMAPPPGST
     PSRTGGFLGT TSPGPMAELY GAANQDSGVS SYISAASPAP STGFGHSLGG PLIATAFTNG
     YH
//
ID   DDX4_MOUSE              Reviewed;         702 AA.
AC   Q61496; Q9D5X7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Probable ATP-dependent RNA helicase DDX4;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 4;
DE   AltName: Full=Mvh;
DE   AltName: Full=Vasa homolog;
GN   Name=Ddx4; Synonyms=Vasa;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 60-702.
RC   STRAIN=BALB/c; TISSUE=Testis;
RX   MEDLINE=95083681; PubMed=7991615; DOI=10.1073/pnas.91.25.12258;
RA   Fujiwara Y., Komiya T., Kawabata H., Sato M., Fujimoto H.,
RA   Furusawa M., Noce T.;
RT   "Isolation of a DEAD-family protein gene that encodes a murine homolog
RT   of Drosophila vasa and its specific expression in germ cell lineage.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:12258-12262(1994).
RN   [3]
RP   INTERACTION WITH PIWIL2.
RX   PubMed=14736746; DOI=10.1242/dev.00973;
RA   Kuramochi-Miyagawa S., Kimura T., Ijiri T.W., Isobe T., Asada N.,
RA   Fujita Y., Ikawa M., Iwai N., Okabe M., Deng W., Lin H., Matsuda Y.,
RA   Nakano T.;
RT   "Mili, a mammalian member of piwi family gene, is essential for
RT   spermatogenesis.";
RL   Development 131:839-849(2004).
RN   [4]
RP   INTERACTION WITH RANBP9.
RC   TISSUE=Testis;
RX   PubMed=14648869; DOI=10.1002/mrd.20009;
RA   Shibata N., Tsunekawa N., Okamoto-Ito S., Akasu R., Tokumasu A.,
RA   Noce T.;
RT   "Mouse RanBPM is a partner gene to a germline specific RNA helicase,
RT   mouse vasa homolog protein.";
RL   Mol. Reprod. Dev. 67:1-7(2004).
RN   [5]
RP   INTERACTION WITH MAEL.
RX   PubMed=16787967; DOI=10.1093/hmg/ddl158;
RA   Costa Y., Speed R.M., Gautier P., Semple C.A., Maratou K.,
RA   Turner J.M.A., Cooke H.J.;
RT   "Mouse MAELSTROM: the link between meiotic silencing of unsynapsed
RT   chromatin and microRNA pathway?";
RL   Hum. Mol. Genet. 15:2324-2334(2006).
RN   [6]
RP   IDENTIFICATION IN A MRNP COMPLEX.
RX   PubMed=17141210; DOI=10.1016/j.ydbio.2006.10.046;
RA   Hosokawa M., Shoji M., Kitamura K., Tanaka T., Noce T., Chuma S.,
RA   Nakatsuji N.;
RT   "Tudor-related proteins TDRD1/MTR-1, TDRD6 and TDRD7/TRAP: domain
RT   composition, intracellular localization, and function in male germ
RT   cells in mice.";
RL   Dev. Biol. 301:38-52(2007).
CC   -!- FUNCTION: May play a role in germ cell development. May play a
CC       role in sperm motility (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Found in a mRNP complex, at least composed of TDRD1,
CC       TDRD6, TDRD7 and DDX4. N-terminus interacts with RANBP9. Interacts
CC       with PIWIL2 and MAEL.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
CC   -!- TISSUE SPECIFICITY: Testis.
CC   -!- DEVELOPMENTAL STAGE: Expressed in spermatogenic cells from the
CC       spermatocyte stage to the round spermatid stage.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX4/VASA
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK014844; BAB29578.1; -; mRNA.
DR   EMBL; D14859; BAA03584.1; -; mRNA.
DR   IPI; IPI00121394; -.
DR   RefSeq; NP_034159.1; NM_010029.2.
DR   UniGene; Mm.12818; -.
DR   ProteinModelPortal; Q61496; -.
DR   SMR; Q61496; 219-645.
DR   STRING; Q61496; -.
DR   PhosphoSite; Q61496; -.
DR   REPRODUCTION-2DPAGE; IPI00121394; -.
DR   REPRODUCTION-2DPAGE; Q61496; -.
DR   PRIDE; Q61496; -.
DR   Ensembl; ENSMUST00000075748; ENSMUSP00000075157; ENSMUSG00000021758.
DR   GeneID; 13206; -.
DR   KEGG; mmu:13206; -.
DR   UCSC; uc007rwm.1; mouse.
DR   CTD; 13206; -.
DR   MGI; MGI:102670; Ddx4.
DR   GeneTree; ENSGT00390000005849; -.
DR   HOVERGEN; HBG015893; -.
DR   PhylomeDB; Q61496; -.
DR   NextBio; 283368; -.
DR   ArrayExpress; Q61496; -.
DR   Bgee; Q61496; -.
DR   CleanEx; MM_DDX4; -.
DR   Genevestigator; Q61496; -.
DR   GermOnline; ENSMUSG00000021758; Mus musculus.
DR   GO; GO:0033391; C:chromatoid body; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR   GO; GO:0071546; C:pi-body; IDA:UniProtKB.
DR   GO; GO:0071547; C:piP-body; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0000237; P:leptotene; IMP:MGI.
DR   GO; GO:0007141; P:male meiosis I; IMP:MGI.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0032880; P:regulation of protein localization; IMP:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Developmental protein; Helicase; Hydrolase;
KW   Nucleotide-binding; Repeat.
FT   CHAIN         1    702       Probable ATP-dependent RNA helicase DDX4.
FT                                /FTId=PRO_0000054979.
FT   DOMAIN      292    475       Helicase ATP-binding.
FT   DOMAIN      503    648       Helicase C-terminal.
FT   NP_BIND     305    312       ATP (By similarity).
FT   MOTIF       261    289       Q motif.
FT   MOTIF       419    422       DEAD box.
FT   COMPBIAS     58    207       Gly-rich.
FT   CONFLICT    152    152       R -> C (in Ref. 2; BAA03584).
FT   CONFLICT    156    160       LFGSR -> FLVLG (in Ref. 2; BAA03584).
FT   CONFLICT    277    277       A -> R (in Ref. 2; BAA03584).
FT   CONFLICT    291    291       S -> T (in Ref. 2; BAA03584).
FT   CONFLICT    368    369       RA -> IS (in Ref. 2; BAA03584).
FT   CONFLICT    423    423       R -> S (in Ref. 2; BAA03584).
FT   CONFLICT    430    430       G -> A (in Ref. 2; BAA03584).
FT   CONFLICT    433    433       M -> I (in Ref. 2; BAA03584).
FT   CONFLICT    448    448       R -> H (in Ref. 2; BAA03584).
FT   CONFLICT    472    472       S -> N (in Ref. 2; BAA03584).
FT   CONFLICT    499    509       SKREKLVEILR -> QKEKSLLRFYE (in Ref. 2;
FT                                BAA03584).
FT   CONFLICT    540    540       T -> S (in Ref. 2; BAA03584).
FT   CONFLICT    680    702       HTLNTAGISSSQAPNPVDDESWD -> AHVEYSGDFFFTSS
FT                                QSS (in Ref. 2).
SQ   SEQUENCE   702 AA;  76470 MW;  5D1E4CC0BDF39748 CRC64;
     MGDEDWEAEI LKPHVSSYVP VFEKDKYSSG ANGDTFNRTS ASSDIGESSK KENTSTTGGF
     GRGKGFGNRG FLNNKFEEGD SSGFWKESNN DCEDNQTRSR GFSKRGGCQD GNDSEASGPF
     RRGGRGSFRG CRGGFGLGRP NSESDQDQGT QRGGGLFGSR KPAASDSGNG DTYQSRSGSG
     RGGYKGLNEE VVTGSGKNSW KSETEGGESS DSQGPKVTYI PPPPPEDEDS IFAHYQTGIN
     FDKYDTILVE VSGHDAPPAI LTFEEANLCQ TLNNNIAKAG YTKLTPVQKY SIPIVLAGRD
     LMACAQTGSG KTAAFLLPIL AHMMRDGITA SRFKELQEPE CIIVAPTREL INQIYLEARK
     FSFGTCVRAV VIYGGTQFGH SVRQIVQGCN ILCATPGRLM DIIGKEKIGL KQVKYLVLDE
     ADRMLDMGFG PEMKKLISCP GMPSKEQRQT LLFSATFPEE IQRLAGDFLK SSYLFVAVGQ
     VGGACRDVQQ TILQVGQYSK REKLVEILRN IGDERTMVFV ETKKKADFIA TFLCQEKIST
     TSIHGDREQR EREQALGDFR CGKCPVLVAT SVAARGLDIE NVQHVINFDL PSTIDEYVHR
     IGRTGRCGNT GRAISFFDTD SDNHLAQPLV KVLSDAQQDV PAWLEEIAFS TYVPPSFSSS
     TRGGAVFASV DTRKNYQGKH TLNTAGISSS QAPNPVDDES WD
//
ID   ERBB3_MOUSE             Reviewed;        1339 AA.
AC   Q61526; Q3KQR1; Q68J64; Q810U8; Q8K317;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 2.
DT   08-MAR-2011, entry version 101.
DE   RecName: Full=Receptor tyrosine-protein kinase erbB-3;
DE            EC=2.7.10.1;
DE   AltName: Full=Glial growth factor receptor;
DE   AltName: Full=Proto-oncogene-like protein c-ErbB-3;
DE   Flags: Precursor;
GN   Name=Erbb3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RA   Yamauchi J., Shooter E.M.;
RT   "Involvement of the ErbB3 signaling pathway in Schwann cell
RT   migration.";
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor, and Thyroid;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1061-1154.
RC   TISSUE=Muscle fibroblast;
RX   MEDLINE=96069911; PubMed=7589796; DOI=10.1006/dbio.1995.0012;
RA   Moscoso L.M., Chu G.C., Gautam M., Noakes P.G., Merlie J.P.,
RA   Sanes J.R.;
RT   "Synapse-associated expression of an acetylcholine receptor-inducing
RT   protein, ARIA/heregulin, and its putative receptors, ErbB2 and ErbB3,
RT   in developing mammalian muscle.";
RL   Dev. Biol. 172:158-169(1995).
CC   -!- FUNCTION: Binds and is activated by neuregulins and NTAK. May also
CC       be activated by CSPG5 (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBUNIT: Heterodimer with each of the other ERBB receptors
CC       (Potential). Interacts with CSPG5, PA2G4 and MUC1 (By similarity).
CC   -!- INTERACTION:
CC       Q9UQ80:PA2G4 (xeno); NbExp=1; IntAct=EBI-931878, EBI-924893;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- TISSUE SPECIFICITY: In the muscle, expression localizes to the
CC       synaptic sites of muscle fibers.
CC   -!- DOMAIN: The cytoplasmic part of the receptor may interact with the
CC       SH2 or SH3 domains of many signal-transducing proteins.
CC   -!- PTM: Ligand-binding increases phosphorylation on tyrosine residues
CC       and promotes its association with the p85 subunit of
CC       phosphatidylinositol 3-kinase (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. EGF receptor subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AY686636; AAT95433.1; -; mRNA.
DR   EMBL; BC029028; AAH29028.1; -; mRNA.
DR   EMBL; BC049279; AAH49279.1; -; mRNA.
DR   EMBL; BC106091; AAI06092.1; -; mRNA.
DR   EMBL; L47240; AAA93533.1; -; mRNA.
DR   IPI; IPI00468814; -.
DR   RefSeq; NP_034283.1; NM_010153.1.
DR   UniGene; Mm.373043; -.
DR   ProteinModelPortal; Q61526; -.
DR   SMR; Q61526; 25-630, 665-990.
DR   IntAct; Q61526; 1.
DR   STRING; Q61526; -.
DR   PhosphoSite; Q61526; -.
DR   PRIDE; Q61526; -.
DR   Ensembl; ENSMUST00000082059; ENSMUSP00000080716; ENSMUSG00000018166.
DR   GeneID; 13867; -.
DR   KEGG; mmu:13867; -.
DR   UCSC; uc007hnm.1; mouse.
DR   CTD; 13867; -.
DR   MGI; MGI:95411; Erbb3.
DR   GeneTree; ENSGT00600000084253; -.
DR   HOGENOM; HBG445128; -.
DR   HOVERGEN; HBG000490; -.
DR   InParanoid; Q61526; -.
DR   OMA; GTTPDED; -.
DR   OrthoDB; EOG42BX7Q; -.
DR   BRENDA; 2.7.10.1; 244.
DR   NextBio; 284768; -.
DR   ArrayExpress; Q61526; -.
DR   Bgee; Q61526; -.
DR   Genevestigator; Q61526; -.
DR   GermOnline; ENSMUSG00000018166; Mus musculus.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004716; F:receptor signaling protein tyrosine kinase activity; IEA:InterPro.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:EC.
DR   GO; GO:0021545; P:cranial nerve development; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptosis; IMP:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0014037; P:Schwann cell differentiation; IMP:MGI.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   InterPro; IPR000494; EGF_rcpt_L.
DR   InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR009030; Growth_fac_rcpt.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   Pfam; PF00757; Furin-like; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF01030; Recep_L_domain; 2.
DR   PIRSF; PIRSF000619; TyrPK_EGF-R; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00261; FU; 5.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF57184; Grow_fac_recept; 2.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Disulfide bond; Glycoprotein; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Receptor; Signal; Transferase;
KW   Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
FT   SIGNAL        1     19       Potential.
FT   CHAIN        20   1339       Receptor tyrosine-protein kinase erbB-3.
FT                                /FTId=PRO_0000042231.
FT   TOPO_DOM     20    641       Extracellular (Potential).
FT   TRANSMEM    642    662       Helical; (Potential).
FT   TOPO_DOM    663   1339       Cytoplasmic (Potential).
FT   DOMAIN      707    964       Protein kinase.
FT   NP_BIND     713    721       ATP (By similarity).
FT   ACT_SITE    832    832       Proton acceptor (By similarity).
FT   BINDING     740    740       ATP (By similarity).
FT   MOD_RES     678    678       Phosphotyrosine (By similarity).
FT   MOD_RES     684    684       Phosphoserine (By similarity).
FT   MOD_RES    1325   1325       Phosphotyrosine (By similarity).
FT   CARBOHYD    126    126       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    250    250       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    353    353       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    408    408       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    414    414       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    437    437       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    469    469       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    522    522       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    566    566       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    616    616       N-linked (GlcNAc...) (Potential).
FT   DISULFID    186    194       By similarity.
FT   DISULFID    190    202       By similarity.
FT   DISULFID    210    218       By similarity.
FT   DISULFID    214    226       By similarity.
FT   DISULFID    227    235       By similarity.
FT   DISULFID    231    243       By similarity.
FT   DISULFID    246    255       By similarity.
FT   DISULFID    259    286       By similarity.
FT   DISULFID    290    301       By similarity.
FT   DISULFID    305    320       By similarity.
FT   DISULFID    323    327       By similarity.
FT   DISULFID    500    509       By similarity.
FT   DISULFID    504    517       By similarity.
FT   DISULFID    520    529       By similarity.
FT   DISULFID    533    549       By similarity.
FT   DISULFID    552    565       By similarity.
FT   DISULFID    556    573       By similarity.
FT   DISULFID    576    585       By similarity.
FT   DISULFID    589    610       By similarity.
FT   DISULFID    613    621       By similarity.
FT   DISULFID    617    629       By similarity.
FT   CONFLICT   1067   1067       A -> V (in Ref. 3; AAA93533).
SQ   SEQUENCE   1339 AA;  147613 MW;  59D56FD9C9536FBE CRC64;
     MSAIGTLQVL GFLLSLARGS EMGNSQAVCP GTLNGLSVTG DADNQYQTLY KLYEKCEVVM
     GNLEIVLTGH NADLSFLQWI REVTGYVLVA MNEFSVLPLP NLRVVRGTQV YDGKFAIFVM
     LNYNTNSSHA LRQLRFTQLT EILLGGVYIE KNDKLCHMDT IDWRDIVRVP DAEIVVKNNG
     GNCPPCHEVC KGRCWGPGPE DCQILTKTIC APQCNGRCFG PNPNQCCHDE CAGGCSGPQD
     TDCFACRHFN DSGACVPRCP APLVYNKLTF QLEPNPHIKY QYGGVCVASC PHNFVVDQTF
     CVRACPADKM EVDKNGLKMC EPCRGLCPKA CEGTGSGSRY QTVDSSNIDG FVNCTKILGN
     LDFLITGLNG DPWHKIPALD PEKLNVFRTV REITGYLNIQ SWPPHMHNFS VFSNLTTIGG
     RSLYNRGFSL LIMKNLNVTS LGFRSLKEIS AGRVYISANQ QLCYHHSLNW TRLLRGPAEE
     RLDIKYNRPL GECVAEGKVC DPLCSSGGCW GPGPGQCLSC RNYSREGVCV THCNVLQGEP
     REFVHEAHCF SCHPECQPME GTSTCNGSGS DACARCAHFR DGPHCVNSCP HGILGAKGPI
     YKYPDAQNEC RPCHENCTQG CKGPELQDCL GQAEVLMSKP HLVIAVTVGL TVIFLILGGS
     FLYWRGRRIQ NKRAMRRYLE RGESIEPLDP SEKANKVLAR IFKETELRKL KVLGSGVFGT
     VHKGIWIPEG ESIKIPVCIK VIEDKSGRQS FQAVTDHMLA VGSLDHAHIV RLLGLCPGSS
     LQLVTQYLPL GSLLDHVRQH RETLGPQLLL NWGVQIAKGM YYLEEHSMVH RDLALRNVML
     KSPSQVQVAD FGVADLLPPD DKQLLHSEAK TPIKWMALES IHFGKYTHQS DVWSYGVTVW
     ELMTFGAEPY AGLRLAEIPD LLEKGERLAQ PQICTIDVYM VMVKCWMIDE NIRPTFKELA
     NEFTRMARDP PRYLVIKRAS GPGIPPAAEP SALSTKELQD AELEPDLDLD LDVEVEEEGL
     ATTLGSALSL PTGTLTRPRG SQSLLSPSSG YMPMNQSNLG EACLDSAVLG GREQFSRPIS
     LHPIPRGRQT SESSEGHVTG SEAELQERVS MCRSRSRSRS PRPRGDSAYH SQRHSLLTPV
     TPLSPPGLEE EDGNGYVMPD THLRGTSSSR EGTLSSVGLS SVLGTEEEDE DEEYEYMNRK
     RRGSPARPPR PGSLEELGYE YMDVGSDLSA SLGSTQSCPL HPMAIVPSAG TTPDEDYEYM
     NRRRGAGGSG GDYAAMGACP AAEQGYEEMR AFQGPGHQAP HVRYARLKTL RSLEATDSAF
     DNPDYWHSRL FPKANAQRI
//
ID   ERBB4_MOUSE             Reviewed;        1292 AA.
AC   Q61527; O88460; Q3UNS6;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 101.
DE   RecName: Full=Receptor tyrosine-protein kinase erbB-4;
DE            EC=2.7.10.1;
DE   AltName: Full=Proto-oncogene-like protein c-ErbB-4;
DE   Contains:
DE     RecName: Full=ERBB4 intracellular domain;
DE              Short=4ICD;
DE              Short=E4ICD;
DE     AltName: Full=s80HER4;
DE   Flags: Precursor;
GN   Name=Erbb4; Synonyms=Mer4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1247.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 624-650 (ISOFORMS JM-A CYT-2 AND JM-B
RP   CYT-2).
RC   TISSUE=Heart, and Kidney;
RX   MEDLINE=97476287; PubMed=9334263; DOI=10.1074/jbc.272.42.26761;
RA   Elenius K., Corfas G., Paul S., Choi C.J., Rio C., Plowman G.D.,
RA   Klagsbrun M.;
RT   "A novel juxtamembrane domain isoform of HER4/ErbB4. Isoform-specific
RT   tissue distribution and differential processing in response to phorbol
RT   ester.";
RL   J. Biol. Chem. 272:26761-26768(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1019-1086.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=96069911; PubMed=7589796; DOI=10.1006/dbio.1995.0012;
RA   Moscoso L.M., Chu G.C., Gautam M., Noakes P.G., Merlie J.P.,
RA   Sanes J.R.;
RT   "Synapse-associated expression of an acetylcholine receptor-inducing
RT   protein, ARIA/heregulin, and its putative receptors, ErbB2 and ErbB3,
RT   in developing mammalian muscle.";
RL   Dev. Biol. 172:158-169(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1019-1077 (ISOFORM JM-A CYT-1).
RC   STRAIN=CD-1; TISSUE=Uterus;
RA   Lim H., Das S.K., Dey S.K.;
RT   "Potential signaling network by EGF-like growth factors in the mouse
RT   uterus during early pregnancy.";
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   INTERACTION WITH CBFA2T3.
RX   PubMed=16815842; DOI=10.1074/jbc.M603998200;
RA   Linggi B., Carpenter G.;
RT   "ErbB-4 s80 intracellular domain abrogates ETO2-dependent
RT   transcriptional repression.";
RL   J. Biol. Chem. 281:25373-25380(2006).
RN   [7]
RP   PROTEOLYTIC PROCESSING, AND SUBCELLULAR LOCATION.
RX   PubMed=16837552; DOI=10.1091/mbc.E06-02-0101;
RA   Muraoka-Cook R.S., Sandahl M., Husted C., Hunter D., Miraglia L.,
RA   Feng S.M., Elenius K., Earp H.S. III;
RT   "The intracellular domain of ErbB4 induces differentiation of mammary
RT   epithelial cells.";
RL   Mol. Biol. Cell 17:4118-4129(2006).
RN   [8]
RP   FUNCTION OF E4ICD.
RX   PubMed=19596786; DOI=10.1128/MCB.01705-08;
RA   Muraoka-Cook R.S., Sandahl M.A., Strunk K.E., Miraglia L.C.,
RA   Husted C., Hunter D.M., Elenius K., Chodosh L.A., Earp H.S. III;
RT   "ErbB4 splice variants Cyt1 and Cyt2 differ by 16 amino acids and
RT   exert opposing effects on the mammary epithelium in vivo.";
RL   Mol. Cell. Biol. 29:4935-4948(2009).
CC   -!- FUNCTION: Specifically binds and is activated by neuregulins, NRG-
CC       2, NRG-3, heparin-binding EGF-like growth factor, betacellulin and
CC       NTAK. Interaction with these factors induces cell differentiation.
CC       Not activated by EGF, TGF-A, and amphiregulin. The C-terminal
CC       fragment (CTF) of isoform JMA-A CYT-2 (containing E4ICD2) can
CC       stimulate transcription in the presence of YAP1. ERBB4
CC       intracellular domain is involved in the regulation of cell growth.
CC       Conflicting reports are likely due at least in part to the
CC       opposing effects of the isoform-specific and nuclear-translocated
CC       ERBB4 intracellular domains (E4ICD1 and E4ICD2). Overexpression
CC       studies in epithelium show growth inhibition using E4ICD1 and
CC       increased proliferation using E4ICD2. E4ICD2 has greater in vitro
CC       kinase activity than E4ICD1. The kinase activity is required for
CC       the nuclear translocation of E4ICD2 (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBUNIT: Homodimer or heterodimer with each of the other ERBB
CC       receptors. Interacts with PDZ domains of DLG2, DLG3, DLG4 and the
CC       syntrophin SNTB2. Interacts (via PPxy motifs)with WWOX. Interacts
CC       with MUC1. Interacts (via PPxY motif 2) with YAP1 (via WW domain
CC       1) (By similarity). Interacts with CBFA2T3. Isoform JM-A CYT-1 and
CC       isoform JM-B CYT-1 interact with WWP1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- SUBCELLULAR LOCATION: ERBB4 intracellular domain: Nucleus.
CC       Note=Following proteolytical processing E4ICD (E4ICD1 or E4ICD2
CC       generated from the respective isoforms) is translocated to the
CC       nucleus. Significantly more E4ICD2 than E4ICD1 is found in the
CC       nucleus. E4ICD2 colocalizes with YAP1 in the nucleus (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Additional isoforms seem to exist;
CC       Name=JM-A CYT-2;
CC         IsoId=Q61527-1; Sequence=Displayed;
CC         Note=Proteolytical processing generates E4ICD2 (s80Cyt2);
CC       Name=JM-B CYT-2;
CC         IsoId=Q61527-2; Sequence=VSP_002896;
CC       Name=JM-A CYT-1;
CC         IsoId=Q61527-3; Sequence=VSP_022149;
CC         Note=Proteolytical processing generates E4ICD1 (s80Cyt1);
CC   -!- TISSUE SPECIFICITY: Isoform JM-A CYT-2 and isoform JM-B CYT-2 are
CC       expressed in cerebellum, cerebral cortex, spinal cord, medulla
CC       oblongata and eye, but the kidney expresses solely isoform JM-A
CC       CYT-2 and the heart solely isoform JM-B CYT-2.
CC   -!- PTM: Isoform JM-A CYT-2 and isoform JM-A CYT-1 but not isoform JM-
CC       B CYT-2 are processed by ADAM17. Proteolytic processing in
CC       response to ligand or 12-O-tetradecanoylphorbol-13-acetate
CC       stimulation results in the production of 120 kDa soluble receptor
CC       forms and intermediate membrane-anchored 80 kDa fragments, which
CC       are further processed by a presenilin-dependent gamma-secretase to
CC       release the respective cytoplasmic intracellular domain E4ICD
CC       (either E4ICD1/s80Cyt1 or E4ICD2/s80Cyt2) (By similarity).
CC   -!- PTM: Ligand-binding increases phosphorylation on tyrosine
CC       residues. Isoform JM-A CYT-2 is constitutively phosphorylated on
CC       tyrosine residues in a ligand-independent manner. E4ICD2 but not
CC       E4ICD1 is phosphorylated on tyrosine residues (By similarity).
CC   -!- PTM: Ubiquitinated. The ERBB4 intracellular domain is
CC       ubiquitinated and targeted to proteosomal degradation during
CC       mitosis mediated by the APC/C complex. Isoform JM-A CYT-1 and
CC       isoform JM-B CYT-1 are ubiquitinated by WWP1. ERBB4 intracellular
CC       domain (E4ICD1) is ubiquitinated, and this involves NEDD4 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. EGF receptor subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AC099604; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC107673; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC138110; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC138285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC139369; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CAAA01019932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CAAA01109085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK144050; BAE25671.1; -; mRNA.
DR   EMBL; L47241; AAA93534.1; -; mRNA.
DR   EMBL; AF059177; AAC28334.1; -; mRNA.
DR   IPI; IPI00122341; -.
DR   IPI; IPI00357770; -.
DR   IPI; IPI00896073; -.
DR   RefSeq; NP_034284.1; NM_010154.1.
DR   UniGene; Mm.442420; -.
DR   ProteinModelPortal; Q61527; -.
DR   SMR; Q61527; 26-639, 676-1009.
DR   DIP; DIP-29887N; -.
DR   STRING; Q61527; -.
DR   PRIDE; Q61527; -.
DR   Ensembl; ENSMUST00000082184; ENSMUSP00000080821; ENSMUSG00000062209.
DR   Ensembl; ENSMUST00000097703; ENSMUSP00000095310; ENSMUSG00000062209.
DR   Ensembl; ENSMUST00000121473; ENSMUSP00000114123; ENSMUSG00000062209.
DR   GeneID; 13869; -.
DR   KEGG; mmu:13869; -.
DR   UCSC; uc007bjb.1; mouse.
DR   CTD; 13869; -.
DR   MGI; MGI:104771; Erbb4.
DR   GeneTree; ENSGT00600000084253; -.
DR   HOVERGEN; HBG000490; -.
DR   OrthoDB; EOG4T4CTM; -.
DR   BRENDA; 2.7.10.1; 244.
DR   NextBio; 284772; -.
DR   ArrayExpress; Q61527; -.
DR   Bgee; Q61527; -.
DR   Genevestigator; Q61527; -.
DR   GermOnline; ENSMUSG00000062209; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004716; F:receptor signaling protein tyrosine kinase activity; IEA:InterPro.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:EC.
DR   GO; GO:0045165; P:cell fate commitment; IDA:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0007399; P:nervous system development; IMP:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   InterPro; IPR000494; EGF_rcpt_L.
DR   InterPro; IPR006211; Furin-like_Cys-rich_dom.
DR   InterPro; IPR006212; Furin_repeat.
DR   InterPro; IPR009030; Growth_fac_rcpt.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR016245; Tyr_kinase_EGF/ERB/XmrK_rcpt.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   Pfam; PF00757; Furin-like; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF01030; Recep_L_domain; 2.
DR   PIRSF; PIRSF000619; TyrPK_EGF-R; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00261; FU; 5.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF57184; Grow_fac_recept; 2.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; ATP-binding; Disulfide bond;
KW   Glycoprotein; Kinase; Membrane; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Receptor; Repeat; Signal; Transcription;
KW   Transcription regulation; Transferase; Transmembrane;
KW   Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
FT   SIGNAL        1     25       Potential.
FT   CHAIN        26   1292       Receptor tyrosine-protein kinase erbB-4.
FT                                /FTId=PRO_0000270146.
FT   CHAIN       676   1292       ERBB4 intracellular domain.
FT                                /FTId=PRO_0000396798.
FT   TOPO_DOM     26    652       Extracellular (Potential).
FT   TRANSMEM    653    673       Potential.
FT   TOPO_DOM    674   1292       Cytoplasmic (Potential).
FT   DOMAIN      718    985       Protein kinase.
FT   NP_BIND     724    732       ATP (By similarity).
FT   MOTIF      1032   1035       PPxy motif 1 (By similarity).
FT   MOTIF      1282   1285       PPxY motif 2 (By similarity).
FT   MOTIF      1290   1292       PDZ-binding (By similarity).
FT   COMPBIAS    186    262       Cys-rich.
FT   COMPBIAS    496    593       Cys-rich.
FT   COMPBIAS   1281   1284       Poly-Pro.
FT   ACT_SITE    843    843       Proton acceptor (By similarity).
FT   BINDING     751    751       ATP (By similarity).
FT   MOD_RES     733    733       Phosphotyrosine (By similarity).
FT   MOD_RES    1146   1146       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES    1172   1172       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES    1242   1242       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES    1268   1268       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   CARBOHYD    138    138       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    174    174       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    181    181       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    253    253       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    410    410       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    473    473       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    495    495       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    548    548       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    576    576       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    620    620       N-linked (GlcNAc...) (Potential).
FT   DISULFID     29     56       By similarity.
FT   DISULFID    156    186       By similarity.
FT   DISULFID    189    197       By similarity.
FT   DISULFID    193    205       By similarity.
FT   DISULFID    213    221       By similarity.
FT   DISULFID    217    229       By similarity.
FT   DISULFID    230    238       By similarity.
FT   DISULFID    234    246       By similarity.
FT   DISULFID    249    258       By similarity.
FT   DISULFID    262    289       By similarity.
FT   DISULFID    293    304       By similarity.
FT   DISULFID    308    323       By similarity.
FT   DISULFID    326    330       By similarity.
FT   DISULFID    503    512       By similarity.
FT   DISULFID    507    520       By similarity.
FT   DISULFID    523    532       By similarity.
FT   DISULFID    536    552       By similarity.
FT   DISULFID    555    569       By similarity.
FT   DISULFID    559    577       By similarity.
FT   DISULFID    580    589       By similarity.
FT   DISULFID    593    614       By similarity.
FT   DISULFID    617    625       By similarity.
FT   DISULFID    621    633       By similarity.
FT   VAR_SEQ     626    648       NGPTSHDCIYYPWTGHSTLPQHA -> IGSSIEDCIGLTD
FT                                (in isoform JM-B CYT-2).
FT                                /FTId=VSP_002896.
FT   VAR_SEQ    1045   1045       R -> RSEIGHSPPPAYTPMWG (in isoform JM-A
FT                                CYT-1).
FT                                /FTId=VSP_022149.
FT   CONFLICT   1019   1019       A -> V (in Ref. 5; AAC28334).
SQ   SEQUENCE   1292 AA;  145213 MW;  46FBDC6AE4CB2908 CRC64;
     MKLATGLWVW GSLLMAAGTV QPSASQSVCA GTENKLSSLS DLEQQYRALR KYYENCEVVM
     GNLEITSIEH NRDLSFLRSI REVTGYVLVA LNQFRYLPLE NLRIIRGTKL YEDRYALAIF
     LNYRKDGNFG LQELGLKNLT EILNGGVYVD QNKFLCYADT IHWQDIVRNP WPSNMTLVST
     NGSSGCGRCH KSCTGRCWGP TENHCQTLTR TVCAEQCDGR CYGPYVSDCC HRECAGGCSG
     PKDTDCFACM NFNDSGACVT QCPQTFVYNP TTFQLEHNFN AKYTYGAFCV KKCPHNFVVD
     SSSCVRACPS SKMEVEENGI KMCKPCTDIC PKACDGIGTG SLMSAQTVDS SNIDKFINCT
     KINGNLIFLV TGIHGDPYNA IDAIDPEKLN VFRTVREITG FLNIQSWPPN MTDFSVFSNL
     VTIGGRVLYS GLSLLILKQQ GITSLQFQSL KEISAGNIYI TDNSNLCYYH TINWTTLFST
     INQRIVIRDN RRAENCTAEG MVCNHLCSND GCWGPGPDQC LSCRRFSRGK ICIESCNLYD
     GEFREFENGS ICVECDSQCE KMEDGLLTCH GPGPDNCTKC SHFKDGPNCV EKCPDGLQGA
     NSFIFKYADQ DRECHPCHPN CTQGCNGPTS HDCIYYPWTG HSTLPQHART PLIAAGVIGG
     LFILVIMALT FAVYVRRKSI KKKRALRRFL ETELVEPLTP SGTAPNQAQL RILKETELKR
     VKVLGSGAFG TVYKGIWVPE GETVKIPVAI KILNETTGPK ANVEFMDEAL IMASMDHPHL
     VRLLGVCLSP TIQLVTQLMP HGCLLDYVHE HKDNIGSQLL LNWCVQIAKG MMYLEERRLV
     HRDLAARNVL VKSPNHVKIT DFGLARLLEG DEKEYNADGG KMPIKWMALE CIHYRKFTHQ
     SDVWSYGVTI WELMTFGGKP YDGIPTREIP DLLEKGERLP QPPICTIDVY MVMVKCWMID
     ADSRPKFKEL AAEFSRMARD PQRYLVIQGD DRMKLPSPND SKFFQNLLDE EDLEDMMDAE
     EYLVPQAFNI PPPIYTSRTR IDSNRNQFVY QDGGFATQQG MPMPYRATTS TIPEAPVAQG
     ATAEMFDDSC CNGTLRKPVA PHVQEDSSTQ RYSADPTVFA PERNPRGELD EEGYMTPMHD
     KPKQEYLNPV EENPFVSRRK NGDLQALDNP EYHSASSGPP KAEDEYVNEP LYLNTFANAL
     GSAEYMKNSV LSVPEKAKKA FDNPDYWNHS LPPRSTLQHP DYLQEYSTKY FYKQNGRIRP
     IVAENPEYLS EFSLKPGTVL PPPPYRHRNT VV
//
ID   GSLG1_MOUSE             Reviewed;        1175 AA.
AC   Q61543; Q9QZ40;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Golgi apparatus protein 1;
DE   AltName: Full=E-selectin ligand 1;
DE            Short=ESL-1;
DE            Short=Selel;
DE   AltName: Full=Golgi sialoglycoprotein MG-160;
DE   Flags: Precursor;
GN   Name=Glg1; Synonyms=Esl1, Mg160, Selel;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 255-266; 357-363;
RP   636-641 AND 744-750.
RC   TISSUE=Neutrophil;
RX   MEDLINE=95157635; PubMed=7531823; DOI=10.1038/373615a0;
RA   Steegmaier M., Levinovitz A., Isenmann S., Borges E., Lenter M.,
RA   Kocher H.P., Kleuser B., Vestweber D.;
RT   "The E-selectin-ligand ESL-1 is a variant of a receptor for fibroblast
RT   growth factor.";
RL   Nature 373:615-620(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE OF 1-138.
RC   STRAIN=129/Sv; TISSUE=Embryonic stem cell;
RX   MEDLINE=20028322; PubMed=10556428; DOI=10.1007/s003359901166;
RA   Willmroth F., Beaudet A.L.;
RT   "Structure of the murine E-selectin ligand 1 (ESL-1) gene and
RT   assignment to chromosome 8.";
RL   Mamm. Genome 10:1085-1088(1999).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=97254533; PubMed=9099943;
RA   Steegmaier M., Borges E., Berger J., Schwarz H., Vestweber D.;
RT   "The E-selectin-ligand ESL-1 is located in the Golgi as well as on
RT   microvilli on the cell surface.";
RL   J. Cell Sci. 110:687-694(1997).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-161 AND ASN-673, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Binds fibroblast growth factor (By similarity). Binds E-
CC       selectin (cell-adhesion lectin on endothelial cells mediating the
CC       binding of neutrophils).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Golgi apparatus membrane; Single-pass type I membrane
CC       protein. Note=Golgi and microvilli on the cell surface.
CC   -!- TISSUE SPECIFICITY: Widely expressed; found in myeloid cells,
CC       fibroblasts, colon carcinoma, endothelioma, teratocarcinoma,
CC       lymphoma, myeloma.
CC   -!- PTM: Fucosylation is essential for binding to E-selectin.
CC   -!- PTM: Contains sialic acid residues (By similarity).
CC   -!- SIMILARITY: Contains 16 Cys-rich GLG1 repeats.
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DR   EMBL; X84037; CAA58855.1; -; mRNA.
DR   EMBL; BC021306; AAH21306.1; -; mRNA.
DR   EMBL; Y12462; CAA73066.1; -; Genomic_DNA.
DR   IPI; IPI00122399; -.
DR   PIR; S52417; S52417.
DR   RefSeq; NP_033175.1; NM_009149.2.
DR   UniGene; Mm.276271; -.
DR   UniGene; Mm.440619; -.
DR   ProteinModelPortal; Q61543; -.
DR   STRING; Q61543; -.
DR   PhosphoSite; Q61543; -.
DR   PRIDE; Q61543; -.
DR   Ensembl; ENSMUST00000003404; ENSMUSP00000003404; ENSMUSG00000003316.
DR   GeneID; 20340; -.
DR   KEGG; mmu:20340; -.
DR   UCSC; uc009nma.1; mouse.
DR   CTD; 20340; -.
DR   MGI; MGI:104967; Glg1.
DR   HOGENOM; HBG358482; -.
DR   HOVERGEN; HBG051850; -.
DR   InParanoid; Q61543; -.
DR   OMA; EKDAHSQ; -.
DR   OrthoDB; EOG4JWVCP; -.
DR   PhylomeDB; Q61543; -.
DR   NextBio; 298161; -.
DR   ArrayExpress; Q61543; -.
DR   Bgee; Q61543; -.
DR   CleanEx; MM_GLG1; -.
DR   Genevestigator; Q61543; -.
DR   GermOnline; ENSMUSG00000003316; Mus musculus.
DR   GO; GO:0000139; C:Golgi membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR001893; Cys-rich_GLG1_repeat.
DR   InterPro; IPR017873; Cys-rich_GLG1_repeat_euk.
DR   Pfam; PF00839; Cys_rich_FGFR; 15.
DR   PROSITE; PS51289; GLG1_C_RICH; 16.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Glycoprotein;
KW   Golgi apparatus; Membrane; Repeat; Sialic acid; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     27       Potential.
FT   CHAIN        28   1175       Golgi apparatus protein 1.
FT                                /FTId=PRO_0000011121.
FT   TOPO_DOM     28   1141       Extracellular (Potential).
FT   TRANSMEM   1142   1162       Helical; (Potential).
FT   TOPO_DOM   1163   1175       Cytoplasmic (Potential).
FT   REPEAT      112    145       Cys-rich GLG1 1.
FT   REPEAT      146    208       Cys-rich GLG1 2.
FT   REPEAT      211    274       Cys-rich GLG1 3.
FT   REPEAT      282    342       Cys-rich GLG1 4.
FT   REPEAT      343    409       Cys-rich GLG1 5.
FT   REPEAT      410    469       Cys-rich GLG1 6.
FT   REPEAT      471    533       Cys-rich GLG1 7.
FT   REPEAT      534    600       Cys-rich GLG1 8.
FT   REPEAT      605    664       Cys-rich GLG1 9.
FT   REPEAT      666    724       Cys-rich GLG1 10.
FT   REPEAT      725    784       Cys-rich GLG1 11.
FT   REPEAT      792    852       Cys-rich GLG1 12.
FT   REPEAT      854    907       Cys-rich GLG1 13.
FT   REPEAT      908    975       Cys-rich GLG1 14.
FT   REPEAT      976   1031       Cys-rich GLG1 15.
FT   REPEAT     1037   1097       Cys-rich GLG1 16.
FT   COMPBIAS     46     51       Poly-Gly.
FT   COMPBIAS     66     70       Poly-Gln.
FT   COMPBIAS     74     82       Poly-Gln.
FT   CARBOHYD    161    161       N-linked (GlcNAc...).
FT   CARBOHYD    206    206       N-linked (GlcNAc...).
FT   CARBOHYD    577    577       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    673    673       N-linked (GlcNAc...).
FT   CARBOHYD    782    782       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   1175 AA;  133734 MW;  105835DD38C7338B CRC64;
     MAVCGRVRGM FRLSAALPLL LLAAAGAQNG HGQGQGPGTN FGPFPGQGGG GSPAGQQPPQ
     QPQLSQQQQQ PPPQQQQQQQ QQSLFAAGGL PARRGGAGPG GTGGGWKLAE EESCREDVTR
     VCPKHTWSNN LAVLECLQDV REPENEISSD CNHLLWNYKL NLTTDPKFES VAREVCKSTI
     SEIKECAEEP VGKGYMVSCL VDHRGNITEY QCHQYITKMT AIIFSDYRLI CGFMDDCKND
     INLLKCGSIR LGEKDAHSQG EVVSCLEKGL VKEAEEKEPK IQVSELCKKA ILRVAELSSD
     DFHLDRHLYF ACRDDRERFC ENTQAGEGRV YKCLFNHKFE ESMSEKCREA LTTRQKLIAQ
     DYKVSYSLAK SCKSDLKKYR CNVENLPRSR EARLSYLLMC LESAVHRGRQ VSSECQGEML
     DYRRMLMEDF SLSPEIILSC RGEIEHHCSG LHRKGRTLHC LMKVVRGEKG NLGMNCQQAL
     QTLIQETDPG ADYRIDRALN EACESVIQTA CKHIRSGDPM ILSCLMEHLY TEKMVEDCEH
     RLLELQYFIS RDWKLDPVLY RKCQGDASRL CHTHGWNETS ELMPPGAVFS CLYRHAYRTE
     EQGRRLSREC RAEVQRILHQ RAMDVKLDPA LQDKCLIDLG KWCSEKTETG QELECLQDHL
     DDLAVECRDI VGNLTELESE DIQIEALLMR ACEPIIQNFC HDVADNQIDS GDLMECLIQN
     KHQKDMNEKC AIGVTHFQLV QMKDFRFSYK FKMACKEDVL KLCPNIKKKV DVVICLSTTV
     RNDTLQEAKE HRVSLKCRKQ LRVEELEMTE DIRLEPDLYE ACKSDIKNYC STVQYGNAQI
     IECLKENKKQ LSTRCHQKVF KLQETEMMDP ELDYTLMRVC KQMIKRFCPE ADSKTMLQCL
     KQNKNSELMD PKCKQMITKR QITQNTDYRL NPVLRKACKA DIPKFCHGIL TKAKDDSELE
     GQVISCLKLR YADQRLSSDC EDQIRIIIQE SALDYRLDPQ LQLHCSDEIA NLCAEEAAAQ
     EQTGQVEECL KVNLLKIKTE LCKKEVLNML KESKADIFVD PVLHTACALD IKHHCAAITP
     GRGRQMSCLM EALEDKRVRL QPECKKRLND RIEMWSYAAK VAPADGFSDL AMQVMTSPSK
     NYILSVISGS ICILFLIGLM CGRITKRVTR ELKDR
//
ID   AP180_MOUSE             Reviewed;         901 AA.
AC   Q61548; Q61547; Q8K0D4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-FEB-2011, entry version 90.
DE   RecName: Full=Clathrin coat assembly protein AP180;
DE   AltName: Full=91 kDa synaptosomal-associated protein;
DE   AltName: Full=Clathrin coat-associated protein AP180;
DE   AltName: Full=Phosphoprotein F1-20;
GN   Name=Snap91;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RX   MEDLINE=92300439; PubMed=1607933;
RA   Zhou S., Sousa R., Tannery N.H., Lafer E.M.;
RT   "Characterization of a novel synapse-specific protein. II. cDNA
RT   cloning and sequence analysis of the F1-20 protein.";
RL   J. Neurosci. 12:2144-2155(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-312; SER-316 AND
RP   SER-600, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Adaptins are components of the adaptor complexes which
CC       link clathrin to receptors in coated vesicles. Clathrin-associated
CC       protein complexes are believed to interact with the cytoplasmic
CC       tails of membrane proteins, leading to their selection and
CC       concentration. Binding of AP180 to clathrin triskelia induces
CC       their assembly into 60-70 nm coats.
CC   -!- SUBUNIT: Binds AP2A2. Interacts with AP2B1; clathrin competes with
CC       SNAP91 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane. Membrane, coated pit;
CC       Peripheral membrane protein; Cytoplasmic side. Note=Component of
CC       the coat surrounding the cytoplasmic face of coated vesicles in
CC       the plasma membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=Long;
CC         IsoId=Q61548-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=Q61548-2; Sequence=VSP_000172;
CC       Name=3;
CC         IsoId=Q61548-3; Sequence=VSP_000172, VSP_022635;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Brain. Associated with the synapses.
CC   -!- DEVELOPMENTAL STAGE: Developmentally regulated in a pattern
CC       coincident with active synaptogenesis and synaptic maturation.
CC   -!- DOMAIN: Possesses a three domain structure: the N-terminal 300
CC       residues harbor a clathrin binding site, an acidic middle domain
CC       450 residues, interrupted by an Ala-rich segment, and the C-
CC       terminal domain (166 residues).
CC   -!- SIMILARITY: Contains 1 ENTH (epsin N-terminal homology) domain.
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DR   EMBL; M83985; AAA37587.1; -; mRNA.
DR   EMBL; M83985; AAA37586.1; -; mRNA.
DR   EMBL; BC031773; AAH31773.1; -; mRNA.
DR   IPI; IPI00122409; -.
DR   IPI; IPI00230165; -.
DR   IPI; IPI00408269; -.
DR   PIR; A44825; A44825.
DR   RefSeq; NP_038697.1; NM_013669.1.
DR   UniGene; Mm.281651; -.
DR   UniGene; Mm.472993; -.
DR   ProteinModelPortal; Q61548; -.
DR   SMR; Q61548; 19-281.
DR   STRING; Q61548; -.
DR   PhosphoSite; Q61548; -.
DR   PRIDE; Q61548; -.
DR   Ensembl; ENSMUST00000036347; ENSMUSP00000046189; ENSMUSG00000033419.
DR   Ensembl; ENSMUST00000074468; ENSMUSP00000074066; ENSMUSG00000033419.
DR   GeneID; 20616; -.
DR   KEGG; mmu:20616; -.
DR   CTD; 20616; -.
DR   MGI; MGI:109132; Snap91.
DR   GeneTree; ENSGT00390000008805; -.
DR   HOGENOM; HBG713838; -.
DR   HOVERGEN; HBG049391; -.
DR   InParanoid; Q61548; -.
DR   NextBio; 298991; -.
DR   ArrayExpress; Q61548; -.
DR   Bgee; Q61548; -.
DR   CleanEx; MM_SNAP91; -.
DR   Genevestigator; Q61548; -.
DR   GO; GO:0030122; C:AP-2 adaptor complex; IC:BHF-UCL.
DR   GO; GO:0032050; F:clathrin heavy chain binding; IPI:BHF-UCL.
DR   GO; GO:0005545; F:1-phosphatidylinositol binding; IDA:BHF-UCL.
DR   GO; GO:0048268; P:clathrin coat assembly; IDA:BHF-UCL.
DR   GO; GO:0007269; P:neurotransmitter secretion; IMP:BHF-UCL.
DR   InterPro; IPR011417; ANTH.
DR   InterPro; IPR014712; Clathrin_Pinositid-bd_GAT-like.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR013809; Epsin-like_N.
DR   Gene3D; G3DSA:1.25.40.90; ENTH_VHS; 1.
DR   Gene3D; G3DSA:1.20.58.150; Pinositid-bd_clathrin_GAT-like; 1.
DR   Pfam; PF07651; ANTH; 1.
DR   SMART; SM00273; ENTH; 1.
DR   SUPFAM; SSF48464; ENTH_VHS; 1.
DR   PROSITE; PS50942; ENTH; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Coated pit; Membrane;
KW   Phosphoprotein.
FT   CHAIN         1    901       Clathrin coat assembly protein AP180.
FT                                /FTId=PRO_0000193865.
FT   DOMAIN       14    145       ENTH.
FT   COMPBIAS    410    413       Poly-Thr.
FT   COMPBIAS    535    539       Poly-Ala.
FT   COMPBIAS    547    550       Poly-Ala.
FT   COMPBIAS    659    664       Poly-Ser.
FT   COMPBIAS    704    710       Poly-Ser.
FT   MOD_RES     312    312       Phosphothreonine.
FT   MOD_RES     313    313       Phosphoserine.
FT   MOD_RES     316    316       Phosphoserine.
FT   MOD_RES     600    600       Phosphoserine.
FT   VAR_SEQ     715    719       Missing (in isoform Short and isoform 3).
FT                                /FTId=VSP_000172.
FT   VAR_SEQ     809    836       Missing (in isoform 3).
FT                                /FTId=VSP_022635.
SQ   SEQUENCE   901 AA;  91851 MW;  24A98FBACE8DB8B1 CRC64;
     MSGQTLTDRI AAAQYSVTGS AVARAVCKAT THEVMGPKKK HLDYLIQATN ETNVNIPQMA
     DTLFERATNS SWVVVFKALV TTHHLMVHGN ERFIQYLASR NTLFNLSNFL DKSGSHGYDM
     STFIRRYSRY LNEKAFSYRQ MAFDFARVKK GADGVMRTMV PEKLLKSMPI LQGQIDALLE
     FDVHPNELTN GVINAAFMLL FKDLIKLFAC YNDGVINLLE KFFEMKKGQC KDALEIYKRF
     LTRMTRVSEF LKVAEQVGID KGDIPDLTQA PSSLMETLEQ HLNTLEGKKP GNNEGSGAPS
     PLSKSSPATT VTSPNSTPAK TIDTSPPVDI FATASAAAPV SSAKPSSDLL DLQPDFSGAA
     AGAAAPVVPP SGGATAWGDL LGEDSLAALS SVPCEAPISD PFAPEPSPPT TTTEPASASA
     STTTAVTAVT TEVDLFGDAF AASPGEAPAA SEGATAPATP APVAAALDAC SGNDPFAPSE
     GSAEAAPELD LFAMKPPETS APVVTPTAST APPVPATAPS PAPTAVAATA ATTTAAAAAT
     TTATTSAAAA TTAAAPPALD IFGDLFDSAP EVAAAPKPDA APSIDLFGTD AFSSPPRGAS
     PVPESSLTAD LLSVDAFAAP SPASTASPAK AESSGVIDLF GDAFGSGASE TQPAPQAVSS
     SSASADLLAG FGGSFMAPST TPVTPAQNNL LQPSFEAAFG TTPSTSSSSS FDPSVFDGLG
     DLLMPTMAPS GQPAPVSMVP PSPAMAASKG LGSDLDSSLA SLVGNLGISG TTSKKGDLQW
     NAGEKKLTGG ANWQPKVTPA TWSAGVPPQG TVPPTSSVPP GAGAPSVGQP GAGFGMPPSG
     TGMTMMSQQP VMFAQPMMRP PFGAAAVPGT QLSPSPTPAT QSPKKPPAKD PLADLNIKDF
     L
//
ID   FXR1_MOUSE              Reviewed;         677 AA.
AC   Q61584; Q8VCU4; Q9R1E2; Q9R1E3; Q9R1E4; Q9R1E5; Q9WUA7; Q9WUA8;
AC   Q9WUA9;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 2.
DT   08-MAR-2011, entry version 108.
DE   RecName: Full=Fragile X mental retardation syndrome-related protein 1;
DE            Short=mFxr1p;
GN   Name=Fxr1; Synonyms=Fxr1h;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC   TISSUE=Fetal brain;
RX   MEDLINE=96177651; PubMed=8634689; DOI=10.1093/hmg/4.12.2209;
RA   Coy J.F., Sedlacek Z., Baechner D., Hameister H., Joos S., Lichter P.,
RA   Delius H., Poustka A.;
RT   "Highly conserved 3' UTR and expression pattern of FXR1 points to a
RT   divergent gene regulation of FXR1 and FMR1.";
RL   Hum. Mol. Genet. 4:2209-2218(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A; B; C; D; E; F
RP   AND G), AND TISSUE SPECIFICITY.
RX   MEDLINE=99339984; PubMed=10409431; DOI=10.1006/geno.1999.5868;
RA   Kirkpatrick L.L., McIlwain K.A., Nelson D.L.;
RT   "Alternative splicing in the murine and human FXR1 genes.";
RL   Genomics 59:193-202(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH CYFIP2.
RX   MEDLINE=21352978; PubMed=11438699; DOI=10.1073/pnas.151231598;
RA   Schenck A., Bardoni B., Moro A., Bagni C., Mandel J.-L.;
RT   "A highly conserved protein family interacting with the fragile X
RT   mental retardation protein (FMRP) and displaying selective
RT   interactions with FMRP-related proteins FXR1P and FXR2P.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:8844-8849(2001).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15128702; DOI=10.1093/hmg/ddh150;
RA   Mientjes E.J., Willemsen R., Kirkpatrick L.L., Nieuwenhuizen I.M.,
RA   Hoogeveen-Westerveld M., Verweij M., Reis S., Bardoni B.,
RA   Hoogeveen A.T., Oostra B.A., Nelson D.L.;
RT   "Fxr1 knockout mice show a striated muscle phenotype: implications for
RT   Fxr1p function in vivo.";
RL   Hum. Mol. Genet. 13:1291-1302(2004).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=16000371; DOI=10.1091/mbc.E05-04-0304;
RA   Huot M.-E., Bisson N., Davidovic L., Mazroui R., Labelle Y., Moss T.,
RA   Khandjian E.W.;
RT   "The RNA-binding protein Fragile X-related 1 regulates somite
RT   formation in Xenopus laevis.";
RL   Mol. Biol. Cell 16:4350-4361(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-68, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: RNA-binding protein required for embryonic and postnatal
CC       development of muscle tissue. May regulate intracellular transport
CC       and local translation of certain mRNAs.
CC   -!- SUBUNIT: Interacts with FMR1 and FXR2. Interacts with TDRD3 (By
CC       similarity). Interacts with CYFIP2 but not with CYFIP1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=E;
CC         IsoId=Q61584-1; Sequence=Displayed;
CC       Name=A;
CC         IsoId=Q61584-2; Sequence=VSP_002836, VSP_002838, VSP_002840;
CC       Name=B;
CC         IsoId=Q61584-3; Sequence=VSP_002838;
CC       Name=C;
CC         IsoId=Q61584-4; Sequence=VSP_002839;
CC       Name=D;
CC         IsoId=Q61584-5; Sequence=VSP_002836, VSP_002839;
CC       Name=F;
CC         IsoId=Q61584-6; Sequence=VSP_002836;
CC       Name=G;
CC         IsoId=Q61584-7; Sequence=VSP_002837;
CC   -!- TISSUE SPECIFICITY: In early embryogenesis, highest expression in
CC       somites and central nervous system. Also expressed in spinal cord,
CC       surrounding mesenchymal tissue and undifferentiated gonad. In mid-
CC       embryogenesis, most prominent in gonad and muscle tissue. Also
CC       expressed in liver, retina, telencephalon and mesencephalon. In
CC       late embryogenesis, restricted to skeletal muscle and
CC       proliferative active layers of brain. After birth, highly
CC       expressed in postmeiotic spermatids. Intermediate levels are found
CC       in heart, liver and kidney with lower levels in brain and skeletal
CC       muscle. Isoform(s) containing the 27 amino acid pocket (residues
CC       564-590) are present in adult heart and muscle.
CC   -!- DISRUPTION PHENOTYPE: Death shortly after birth. Mice expressing
CC       low levels of Fxr1 show postnatal growth retardation with reduced
CC       increase in muscle mass and strength. They die within 3 weeks of
CC       birth.
CC   -!- SIMILARITY: Belongs to the FMR1 family.
CC   -!- SIMILARITY: Contains 2 KH domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X90875; CAA62383.1; -; mRNA.
DR   EMBL; AF124385; AAD30211.1; -; mRNA.
DR   EMBL; AF124394; AAD30212.1; -; Genomic_DNA.
DR   EMBL; AF124386; AAD30212.1; JOINED; Genomic_DNA.
DR   EMBL; AF124387; AAD30212.1; JOINED; Genomic_DNA.
DR   EMBL; AF124388; AAD30212.1; JOINED; Genomic_DNA.
DR   EMBL; AF124389; AAD30212.1; JOINED; Genomic_DNA.
DR   EMBL; AF124390; AAD30212.1; JOINED; Genomic_DNA.
DR   EMBL; AF124391; AAD30212.1; JOINED; Genomic_DNA.
DR   EMBL; AF124392; AAD30212.1; JOINED; Genomic_DNA.
DR   EMBL; AF124393; AAD30212.1; JOINED; Genomic_DNA.
DR   EMBL; AF124394; AAD30213.1; -; Genomic_DNA.
DR   EMBL; AF124386; AAD30213.1; JOINED; Genomic_DNA.
DR   EMBL; AF124387; AAD30213.1; JOINED; Genomic_DNA.
DR   EMBL; AF124388; AAD30213.1; JOINED; Genomic_DNA.
DR   EMBL; AF124389; AAD30213.1; JOINED; Genomic_DNA.
DR   EMBL; AF124390; AAD30213.1; JOINED; Genomic_DNA.
DR   EMBL; AF124391; AAD30213.1; JOINED; Genomic_DNA.
DR   EMBL; AF124392; AAD30213.1; JOINED; Genomic_DNA.
DR   EMBL; AF124393; AAD30213.1; JOINED; Genomic_DNA.
DR   EMBL; AF124394; AAD30214.1; -; Genomic_DNA.
DR   EMBL; AF124386; AAD30214.1; JOINED; Genomic_DNA.
DR   EMBL; AF124387; AAD30214.1; JOINED; Genomic_DNA.
DR   EMBL; AF124388; AAD30214.1; JOINED; Genomic_DNA.
DR   EMBL; AF124389; AAD30214.1; JOINED; Genomic_DNA.
DR   EMBL; AF124390; AAD30214.1; JOINED; Genomic_DNA.
DR   EMBL; AF124391; AAD30214.1; JOINED; Genomic_DNA.
DR   EMBL; AF124392; AAD30214.1; JOINED; Genomic_DNA.
DR   EMBL; AF124393; AAD30214.1; JOINED; Genomic_DNA.
DR   EMBL; AF124394; AAD30215.1; -; Genomic_DNA.
DR   EMBL; AF124386; AAD30215.1; JOINED; Genomic_DNA.
DR   EMBL; AF124387; AAD30215.1; JOINED; Genomic_DNA.
DR   EMBL; AF124388; AAD30215.1; JOINED; Genomic_DNA.
DR   EMBL; AF124389; AAD30215.1; JOINED; Genomic_DNA.
DR   EMBL; AF124390; AAD30215.1; JOINED; Genomic_DNA.
DR   EMBL; AF124391; AAD30215.1; JOINED; Genomic_DNA.
DR   EMBL; AF124392; AAD30215.1; JOINED; Genomic_DNA.
DR   EMBL; AF124393; AAD30215.1; JOINED; Genomic_DNA.
DR   EMBL; AF124394; AAD30216.1; -; Genomic_DNA.
DR   EMBL; AF124386; AAD30216.1; JOINED; Genomic_DNA.
DR   EMBL; AF124387; AAD30216.1; JOINED; Genomic_DNA.
DR   EMBL; AF124388; AAD30216.1; JOINED; Genomic_DNA.
DR   EMBL; AF124389; AAD30216.1; JOINED; Genomic_DNA.
DR   EMBL; AF124390; AAD30216.1; JOINED; Genomic_DNA.
DR   EMBL; AF124391; AAD30216.1; JOINED; Genomic_DNA.
DR   EMBL; AF124392; AAD30216.1; JOINED; Genomic_DNA.
DR   EMBL; AF124393; AAD30216.1; JOINED; Genomic_DNA.
DR   EMBL; AF124394; AAD30217.1; -; Genomic_DNA.
DR   EMBL; AF124386; AAD30217.1; JOINED; Genomic_DNA.
DR   EMBL; AF124387; AAD30217.1; JOINED; Genomic_DNA.
DR   EMBL; AF124388; AAD30217.1; JOINED; Genomic_DNA.
DR   EMBL; AF124389; AAD30217.1; JOINED; Genomic_DNA.
DR   EMBL; AF124390; AAD30217.1; JOINED; Genomic_DNA.
DR   EMBL; AF124391; AAD30217.1; JOINED; Genomic_DNA.
DR   EMBL; AF124392; AAD30217.1; JOINED; Genomic_DNA.
DR   EMBL; AF124393; AAD30217.1; JOINED; Genomic_DNA.
DR   EMBL; AF124394; AAD30218.1; -; Genomic_DNA.
DR   EMBL; AF124386; AAD30218.1; JOINED; Genomic_DNA.
DR   EMBL; AF124387; AAD30218.1; JOINED; Genomic_DNA.
DR   EMBL; AF124388; AAD30218.1; JOINED; Genomic_DNA.
DR   EMBL; AF124389; AAD30218.1; JOINED; Genomic_DNA.
DR   EMBL; AF124390; AAD30218.1; JOINED; Genomic_DNA.
DR   EMBL; AF124391; AAD30218.1; JOINED; Genomic_DNA.
DR   EMBL; AF124392; AAD30218.1; JOINED; Genomic_DNA.
DR   EMBL; AF124393; AAD30218.1; JOINED; Genomic_DNA.
DR   EMBL; BC019139; AAH19139.1; -; mRNA.
DR   IPI; IPI00122521; -.
DR   IPI; IPI00230597; -.
DR   IPI; IPI00230598; -.
DR   IPI; IPI00230599; -.
DR   IPI; IPI00230600; -.
DR   IPI; IPI00230601; -.
DR   IPI; IPI00230602; -.
DR   RefSeq; NP_001106659.1; NM_001113188.1.
DR   RefSeq; NP_001106660.1; NM_001113189.1.
DR   RefSeq; NP_032079.1; NM_008053.2.
DR   UniGene; Mm.259021; -.
DR   ProteinModelPortal; Q61584; -.
DR   SMR; Q61584; 3-121, 212-359.
DR   MINT; MINT-257148; -.
DR   STRING; Q61584; -.
DR   PhosphoSite; Q61584; -.
DR   PRIDE; Q61584; -.
DR   Ensembl; ENSMUST00000001620; ENSMUSP00000001620; ENSMUSG00000027680.
DR   Ensembl; ENSMUST00000091244; ENSMUSP00000088789; ENSMUSG00000027680.
DR   Ensembl; ENSMUST00000108197; ENSMUSP00000103832; ENSMUSG00000027680.
DR   Ensembl; ENSMUST00000108198; ENSMUSP00000103833; ENSMUSG00000027680.
DR   GeneID; 14359; -.
DR   KEGG; mmu:14359; -.
DR   UCSC; uc008oxk.1; mouse.
DR   UCSC; uc008oxl.1; mouse.
DR   CTD; 14359; -.
DR   MGI; MGI:104860; Fxr1.
DR   eggNOG; roNOG11735; -.
DR   GeneTree; ENSGT00390000017033; -.
DR   HOVERGEN; HBG005739; -.
DR   InParanoid; Q61584; -.
DR   OMA; QIGMGFR; -.
DR   OrthoDB; EOG49KFQB; -.
DR   PhylomeDB; Q61584; -.
DR   NextBio; 285817; -.
DR   ArrayExpress; Q61584; -.
DR   Bgee; Q61584; -.
DR   Genevestigator; Q61584; -.
DR   GermOnline; ENSMUSG00000027680; Mus musculus.
DR   GO; GO:0043034; C:costamere; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005844; C:polysome; IDA:MGI.
DR   GO; GO:0002151; F:G-quadruplex RNA binding; IDA:MGI.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR   GO; GO:0007517; P:muscle organ development; IMP:MGI.
DR   GO; GO:0017148; P:negative regulation of translation; IDA:MGI.
DR   InterPro; IPR008395; Agenet.
DR   InterPro; IPR022034; FXR1P_C.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR004088; KH_type_1.
DR   InterPro; IPR018111; KH_type_1_subgr.
DR   Pfam; PF05641; Agenet; 1.
DR   Pfam; PF12235; FXR1P_C; 1.
DR   Pfam; PF00013; KH_1; 2.
DR   SMART; SM00322; KH; 2.
DR   PROSITE; PS50084; KH_TYPE_1; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Developmental protein;
KW   Differentiation; Methylation; Myogenesis; Phosphoprotein; Repeat;
KW   RNA-binding.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    677       Fragile X mental retardation syndrome-
FT                                related protein 1.
FT                                /FTId=PRO_0000050107.
FT   DOMAIN      222    251       KH 1.
FT   DOMAIN      285    314       KH 2.
FT   REGION      471    486       RNA-binding RGG-box.
FT   COMPBIAS     50     53       Poly-Pro.
FT   COMPBIAS    531    539       Poly-Arg.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      68     68       Phosphotyrosine.
FT   MOD_RES     435    435       Phosphoserine.
FT   MOD_RES     438    438       Phosphoserine (By similarity).
FT   MOD_RES     474    474       Omega-N-methylated arginine (By
FT                                similarity).
FT   MOD_RES     506    506       Phosphotyrosine (By similarity).
FT   MOD_RES     553    553       Phosphoserine (By similarity).
FT   MOD_RES     557    557       Phosphoserine (By similarity).
FT   MOD_RES     641    641       Phosphoserine.
FT   MOD_RES     643    643       Phosphoserine (By similarity).
FT   VAR_SEQ     380    408       Missing (in isoform A, isoform D and
FT                                isoform F).
FT                                /FTId=VSP_002836.
FT   VAR_SEQ     430    455       Missing (in isoform G).
FT                                /FTId=VSP_002837.
FT   VAR_SEQ     564    590       Missing (in isoform C and isoform D).
FT                                /FTId=VSP_002839.
FT   VAR_SEQ     564    568       DDSEK -> GKRCD (in isoform A and isoform
FT                                B).
FT                                /FTId=VSP_002838.
FT   VAR_SEQ     569    677       Missing (in isoform A).
FT                                /FTId=VSP_002840.
FT   CONFLICT    136    136       D -> H (in Ref. 3; AAH19139).
SQ   SEQUENCE   677 AA;  76222 MW;  908104FC95431A11 CRC64;
     MAELTVEVRG SNGAFYKGFI KDVHEDSLTV VFENNWQPER QVPFNEVRLP PPPDIKKEIS
     EGDEVEVYSR ANDQEPCGWW LAKVRMMKGE FYVIEYAACD ATYNEIVTFE RLRPVNQNKT
     VKKNTFFKCT VDVPEDLREA CANENAHKDF KKAVGACRIF YHPETTQLMI LSASEATVKR
     VNILSDMHLR SIRTKLMLMS RNEEATKHLE CTKQLAAAFH EEFVVREDLM GLAIGTHGSN
     IQQARKVPGV TAIELDEDTG TFRIYGESAE AVKKARGFLE FVEDFIQVPR NLVGKVIGKN
     GKVIQEIVDK SGVVRVRIEG DNENKLPRED GMVPFVFVGT KESIGNVQVL LEYHIAYLKE
     VEQLRMERLQ IDEQLRQIGM GFRPSSTRGP EREKGYATDE STVSSVQGSR SYSGRGRGRR
     GPNYTSGYGT NSELSNPSET ESERKDELSD WSLAGEDDRE TRHQRDSRRR PGGRGRSVSG
     GRGRGGPRGG KSSISSVLKD PDSNPYSLLD NTESDQTADT DASESHHSTN RRRRSRRRRT
     DEDAVLMDGL TESDTASVNE NGLDDSEKKP QRRNRSRRRR FRGQAEDRQP VTVADYISRA
     ESQSRQRNLP RETLAKNKKE MAKDVIEEHG PSEKAINGPT SASGDEIPKL PRTLGEEKTK
     TLKEDSTQEA AVLNGVS
//
ID   KTN1_MOUSE              Reviewed;        1327 AA.
AC   Q61595; Q8BG49; Q8BHF4; Q8BHM8; Q8C9Y5; Q8CG51; Q8CG52; Q8CG53;
AC   Q8CG54; Q8CG55; Q8CG56; Q8CG57; Q8CG58; Q8CG59; Q8CG60; Q8CG61;
AC   Q8CG62; Q8CG63;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Kinectin;
GN   Name=Ktn1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, AND
RP   TISSUE SPECIFICITY.
RX   MEDLINE=97068817; PubMed=8912005; DOI=10.1038/icb.1996.72;
RA   Leung E., Print C.G., Parry D.A.D., Closey D.N., Lockhart P.J.,
RA   Skinner S.J.M., Batchelor D.C., Krissansen G.W.;
RT   "Cloning of novel kinectin splice variants with alternative C-termini:
RT   structure, distribution and evolution of mouse kinectin.";
RL   Immunol. Cell Biol. 74:421-433(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-527.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 803-1327 (ISOFORMS 2; 3; 4; 5; 6; 7; 8;
RP   9; 10; 11; 12; 13; 14; 15 AND 16), SUBCELLULAR LOCATION, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=Swiss Webster; TISSUE=Astrocyte, and Hippocampus;
RX   PubMed=15316074; DOI=10.1242/jcs.01326;
RA   Santama N., Er C.P.N., Ong L.-L., Yu H.;
RT   "Distribution and functions of kinectin isoforms.";
RL   J. Cell Sci. 117:4537-4549(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Receptor for kinesin thus involved in kinesin-driven
CC       vesicle motility. Accumulates in integrin-based adhesion complexes
CC       (IAC) upon integrin aggregation by fibronectin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       type II membrane protein. Note=Vesicle membrane protein anchored
CC       to the endoplasmic reticulum (By similarity). Some isoforms
CC       containing the inserts at residues 1007-1035 and 1154-1177 are
CC       detected in neurite processes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=16;
CC       Name=1;
CC         IsoId=Q61595-1; Sequence=Displayed;
CC       Name=2; Synonyms=KNT1;
CC         IsoId=Q61595-2; Sequence=VSP_052042, VSP_052043, VSP_052044,
CC                                  VSP_052045, VSP_052046;
CC       Name=3; Synonyms=KNT2;
CC         IsoId=Q61595-3; Sequence=VSP_052042, VSP_052043, VSP_052044,
CC                                  VSP_052046;
CC       Name=4; Synonyms=KNT3;
CC         IsoId=Q61595-4; Sequence=VSP_052042, VSP_052043, VSP_052045;
CC       Name=5; Synonyms=KNT4;
CC         IsoId=Q61595-5; Sequence=VSP_052043, VSP_052046;
CC       Name=6; Synonyms=KNT5;
CC         IsoId=Q61595-6; Sequence=VSP_052043, VSP_052045, VSP_052046;
CC       Name=7; Synonyms=KNT6;
CC         IsoId=Q61595-7; Sequence=VSP_052042, VSP_052044;
CC       Name=8; Synonyms=KNT7;
CC         IsoId=Q61595-8; Sequence=VSP_052042, VSP_052044, VSP_052045;
CC       Name=9; Synonyms=KNT8;
CC         IsoId=Q61595-9; Sequence=VSP_052044, VSP_052045, VSP_052046;
CC       Name=10; Synonyms=KNT9;
CC         IsoId=Q61595-10; Sequence=VSP_052042, VSP_052043;
CC       Name=11; Synonyms=KNT10;
CC         IsoId=Q61595-11; Sequence=VSP_052042;
CC       Name=12; Synonyms=KNT11;
CC         IsoId=Q61595-12; Sequence=VSP_052042, VSP_052043, VSP_052044,
CC                                   VSP_052045;
CC       Name=13; Synonyms=KNT12;
CC         IsoId=Q61595-13; Sequence=VSP_052042, VSP_052045, VSP_052046;
CC       Name=14; Synonyms=KNT13;
CC         IsoId=Q61595-14; Sequence=VSP_052042, VSP_052044, VSP_052045,
CC                                   VSP_052046;
CC       Name=15; Synonyms=KNT14;
CC         IsoId=Q61595-15; Sequence=VSP_052044, VSP_052045;
CC       Name=16; Synonyms=KNT15;
CC         IsoId=Q61595-16; Sequence=VSP_052042, VSP_052043, VSP_052045,
CC                                   VSP_052046;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined including
CC       12-day embryo, adult heart, brain, ovary, kidney, lung, small
CC       intestine, spleen, thymus and pancreas.
CC   -!- DEVELOPMENTAL STAGE: Isoform 6, isoform 7 and isoform 8 are
CC       detected in embryonic hippocampus but not in later developmental
CC       stages. Isoform 14, isoform 15 and isoform 16 are adult-specific.
CC   -!- SIMILARITY: Belongs to the kinectin family.
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DR   EMBL; L43326; AAB65839.1; -; mRNA.
DR   EMBL; AK040200; BAC30538.1; -; mRNA.
DR   EMBL; AJ517365; CAD56924.1; -; mRNA.
DR   EMBL; AJ517366; CAD56925.1; -; mRNA.
DR   EMBL; AJ517367; CAD56926.1; -; mRNA.
DR   EMBL; AJ517368; CAD56927.1; -; mRNA.
DR   EMBL; AJ517369; CAD56928.1; -; mRNA.
DR   EMBL; AJ517370; CAD56929.1; -; mRNA.
DR   EMBL; AJ517371; CAD56930.1; -; mRNA.
DR   EMBL; AJ517372; CAD56931.1; -; mRNA.
DR   EMBL; AJ517373; CAD56932.1; -; mRNA.
DR   EMBL; AJ517374; CAD56933.1; -; mRNA.
DR   EMBL; AJ517375; CAD56934.1; -; mRNA.
DR   EMBL; AJ517376; CAD56935.1; -; mRNA.
DR   EMBL; AJ517377; CAD56936.1; -; mRNA.
DR   EMBL; AJ517378; CAD56937.1; -; mRNA.
DR   EMBL; AJ517379; CAD56938.1; -; mRNA.
DR   EMBL; AJ517380; CAD56939.1; -; mRNA.
DR   EMBL; AJ517381; CAD56940.1; -; mRNA.
DR   EMBL; AJ517382; CAD56941.1; -; mRNA.
DR   EMBL; AJ517383; CAD56942.1; -; mRNA.
DR   EMBL; AJ517384; CAD56943.1; -; mRNA.
DR   IPI; IPI00122559; -.
DR   IPI; IPI00407517; -.
DR   IPI; IPI00473546; -.
DR   IPI; IPI00759851; -.
DR   IPI; IPI00759887; -.
DR   IPI; IPI00759913; -.
DR   IPI; IPI00759916; -.
DR   IPI; IPI00759936; -.
DR   IPI; IPI00759943; -.
DR   IPI; IPI00759952; -.
DR   IPI; IPI00759972; -.
DR   IPI; IPI00760003; -.
DR   IPI; IPI00760049; -.
DR   IPI; IPI00760053; -.
DR   IPI; IPI00760076; -.
DR   IPI; IPI00760078; -.
DR   RefSeq; NP_032503.2; NM_008477.2.
DR   UniGene; Mm.3110; -.
DR   ProteinModelPortal; Q61595; -.
DR   STRING; Q61595; -.
DR   PhosphoSite; Q61595; -.
DR   PRIDE; Q61595; -.
DR   Ensembl; ENSMUST00000022391; ENSMUSP00000022391; ENSMUSG00000021843.
DR   Ensembl; ENSMUST00000070762; ENSMUSP00000070771; ENSMUSG00000021843.
DR   Ensembl; ENSMUST00000089901; ENSMUSP00000087345; ENSMUSG00000021843.
DR   Ensembl; ENSMUST00000111743; ENSMUSP00000107372; ENSMUSG00000021843.
DR   Ensembl; ENSMUST00000111744; ENSMUSP00000107373; ENSMUSG00000021843.
DR   Ensembl; ENSMUST00000111745; ENSMUSP00000107374; ENSMUSG00000021843.
DR   GeneID; 16709; -.
DR   KEGG; mmu:16709; -.
DR   UCSC; uc007til.1; mouse.
DR   UCSC; uc007tim.1; mouse.
DR   UCSC; uc007tin.1; mouse.
DR   CTD; 16709; -.
DR   MGI; MGI:109153; Ktn1.
DR   eggNOG; roNOG07492; -.
DR   GeneTree; ENSGT00530000063895; -.
DR   HOVERGEN; HBG007851; -.
DR   InParanoid; Q61595; -.
DR   OrthoDB; EOG4Z62N5; -.
DR   NextBio; 290490; -.
DR   ArrayExpress; Q61595; -.
DR   Bgee; Q61595; -.
DR   CleanEx; MM_KTN1; -.
DR   Genevestigator; Q61595; -.
DR   GermOnline; ENSMUSG00000021843; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019894; F:kinesin binding; TAS:MGI.
DR   GO; GO:0007018; P:microtubule-based movement; TAS:MGI.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Endoplasmic reticulum;
KW   Glycoprotein; Isopeptide bond; Membrane; Phosphoprotein;
KW   Signal-anchor; Transmembrane; Transmembrane helix; Ubl conjugation.
FT   CHAIN         1   1327       Kinectin.
FT                                /FTId=PRO_0000238620.
FT   TOPO_DOM      1      8       Cytoplasmic (Potential).
FT   TRANSMEM      9     29       Helical; Signal-anchor for type II
FT                                membrane protein; (Potential).
FT   TOPO_DOM     30   1327       Lumenal (Potential).
FT   COILED      329   1327       Potential.
FT   COMPBIAS     40    219       Lys-rich.
FT   MOD_RES      75     75       Phosphoserine.
FT   MOD_RES      77     77       Phosphoserine (By similarity).
FT   CARBOHYD     69     69       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1031   1031       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1066   1066       N-linked (GlcNAc...) (Potential).
FT   CROSSLNK    312    312       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   VAR_SEQ     836    858       Missing (in isoform 2, isoform 3, isoform
FT                                4, isoform 7, isoform 8, isoform 10,
FT                                isoform 11, isoform 12, isoform 13,
FT                                isoform 14 and isoform 16).
FT                                /FTId=VSP_052042.
FT   VAR_SEQ    1007   1035       Missing (in isoform 2, isoform 3, isoform
FT                                4, isoform 5, isoform 6, isoform 10,
FT                                isoform 12 and isoform 16).
FT                                /FTId=VSP_052043.
FT   VAR_SEQ    1154   1177       Missing (in isoform 2, isoform 3, isoform
FT                                7, isoform 8, isoform 9, isoform 12,
FT                                isoform 14 and isoform 15).
FT                                /FTId=VSP_052044.
FT   VAR_SEQ    1208   1235       Missing (in isoform 2, isoform 4, isoform
FT                                6, isoform 8, isoform 9, isoform 12,
FT                                isoform 13, isoform 14, isoform 15 and
FT                                isoform 16).
FT                                /FTId=VSP_052045.
FT   VAR_SEQ    1294   1327       ESPEKETMSVSLNQTVTQLQQLLQEVNQQLTKET -> SEV
FT                                IGKLLVRS (in isoform 2, isoform 3,
FT                                isoform 5, isoform 6, isoform 9, isoform
FT                                13, isoform 14 and isoform 16).
FT                                /FTId=VSP_052046.
FT   CONFLICT     10     10       I -> V (in Ref. 2; BAC30538).
FT   CONFLICT    115    115       Q -> K (in Ref. 2; BAC30538).
FT   CONFLICT    178    178       Missing (in Ref. 2).
FT   CONFLICT    238    238       M -> I (in Ref. 2).
FT   CONFLICT    360    360       R -> Q (in Ref. 2).
FT   CONFLICT   1118   1118       V -> VS (in Ref. 3; CAD56927).
FT   CONFLICT   1183   1183       E -> G (in Ref. 3; CAD56935).
FT   CONFLICT   1238   1238       L -> F (in Ref. 3; CAD56936).
SQ   SEQUENCE   1327 AA;  152592 MW;  2B79EB332D2470E5 CRC64;
     MELYESTYFI VLIPSVVITV IFLFFWLFMK ETLYDEVLAK QKREQKLIST KTDKKKAEKK
     KNKKKEIQNG TLRESDSEHV PRDFKLSDAS PAEDEQFVPA PLNVAETSSS VRERQKKEKK
     QKPSLEEQVI KESDASKIPG KKVEPVLVTK QPAPPPPLEA AALKKKAGQK KSKNGSEEQD
     KKVEMLMAPS KEQDVLLSHQ DTKQEGGLGK KKGLSKKQKS ENVAVLVDEP LIHATTYMPL
     DNANSNLMMD KREIIDMIKP DHVEGIQKSG TKKLKIETDK ENAEVKFKDF LLSLKTMMFS
     EDEALCVVDL LKEKSGVIKE ALKKSNKGEL SGLLHQLQEK ERLLSAMKED AAASKERCKR
     LTQEMMTEKE RSSVVIARMK DRIGTLEKEH NIFQNKMHAS YQETQQMQMK FQQVQEQMEA
     EIAHLKQENG ILRDAVSNTT NQLESKQSAE LNKLRQDCGR LVSELNEKTG KLQQEGVQKK
     NAEQAATQLK VQLQEAERRW EEVQSYIRKR TAEHEAAQQD LQSKFVAKEN EVQSLHSKLT
     DTLVSKQQLE QRLMQLMESE QKRASKEESL QIQVQDILEQ NEALKAQIQQ FHSQIAAQTS
     ASVLAEELHK VIAEKDKQLK QTEDSLANEQ DHLASKEEEL KDVQNMNFLL KAEVQKWQAL
     ANEQAATAHE VEKMQKSIHV KEDEIRLLEE QLQHEVASKM EELKILSEQN KALQSEVRKL
     QTAVSQQPNK DVVEQMEKCI QEKDEKLRTV EELLETGLIQ VATREEELSA IRTENSTLTR
     EVQELKAKQS DQVSFVSLIE DLKRVIHEKD GQIKSVEELL EVELLKVANK EKTVQALKQE
     IEVLKEEIGN AQLEKAHQLS VTSQVQELQN LLRGKEEQVN SMKAALEDRD RGLTGRGTCA
     QVCSTPQFEE LESVLKEKDN EIKRIEVKLK DTESDVSKMS ELLKEVQEEN KFLKCQLSHQ
     KHQQASFPSQ EELQTVISEK EKEITDLCNE LESLKNAVEH QRKKNNDLRE KNWEAMEALA
     STEKMLQDRV NKTSKERRQH VEAIELESKD LLKRLFPTVS VPSNLNYSEW LRGFEKKAKA
     CVAGTSDAEA VKVLEHRLKE ASEMHTLLQL ECEKYKSVLA ETEGILQKLQ RSVEQEESKW
     KIKADESQRM IKQMQSSFTA SERELERLRQ ENKDMENLRR EREHLEMELE KAEMERSTYV
     MEVRELKDLL TELQKKLDDS YSEAVRQNEE LNLLKTQLNE THSKLQNEQT ERKKVADDLH
     KAQQSLNSIH SKISLKAAGD TVVIENSDIS PEMESPEKET MSVSLNQTVT QLQQLLQEVN
     QQLTKET
//
ID   GLI3_MOUSE              Reviewed;        1583 AA.
AC   Q61602;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=Zinc finger protein GLI3;
GN   Name=Gli3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=NIH Swiss;
RX   MEDLINE=96305347; PubMed=8688459; DOI=10.1016/0167-4781(96)00079-6;
RA   Thien H., Buescher D., Ruether U.;
RT   "Cloning and sequence analysis of the murine Gli3 cDNA.";
RL   Biochim. Biophys. Acta 1307:267-269(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- FUNCTION: Plays a role in limb and brain development. Implicated
CC       in the transduction of SHH signal.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- PTM: Phosphorylated in vitro by ULK3 (By similarity).
CC   -!- DISEASE: Note=Several mutations result in developmental defects of
CC       cranofacial and limb structures. In particular the add (anterior
CC       digit-pattern deformity) and pdn (polydactyly Nagoya) alleles.
CC   -!- SIMILARITY: Belongs to the GLI C2H2-type zinc-finger protein
CC       family.
CC   -!- SIMILARITY: Contains 5 C2H2-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA64543.1; Type=Frameshift; Positions=1552;
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DR   EMBL; X95255; CAA64543.1; ALT_FRAME; mRNA.
DR   EMBL; AC163610; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC173115; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC173210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00123429; -.
DR   RefSeq; NP_032156.2; NM_008130.2.
DR   UniGene; Mm.5098; -.
DR   ProteinModelPortal; Q61602; -.
DR   SMR; Q61602; 436-633.
DR   STRING; Q61602; -.
DR   PhosphoSite; Q61602; -.
DR   PRIDE; Q61602; -.
DR   Ensembl; ENSMUST00000110510; ENSMUSP00000106137; ENSMUSG00000021318.
DR   GeneID; 14634; -.
DR   KEGG; mmu:14634; -.
DR   CTD; 14634; -.
DR   MGI; MGI:95729; Gli3.
DR   GeneTree; ENSGT00600000084058; -.
DR   HOGENOM; HBG447235; -.
DR   HOVERGEN; HBG005844; -.
DR   InParanoid; Q61602; -.
DR   OrthoDB; EOG45HRWN; -.
DR   NextBio; 286490; -.
DR   ArrayExpress; Q61602; -.
DR   Bgee; Q61602; -.
DR   CleanEx; MM_GLI3; -.
DR   Genevestigator; Q61602; -.
DR   GermOnline; ENSMUSG00000021318; Mus musculus.
DR   GO; GO:0017053; C:transcriptional repressor complex; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IGI:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0060873; P:anterior semicircular canal development; IMP:MGI.
DR   GO; GO:0009952; P:anterior/posterior pattern formation; IMP:MGI.
DR   GO; GO:0060840; P:artery development; IGI:MGI.
DR   GO; GO:0007411; P:axon guidance; IMP:MGI.
DR   GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IGI:MGI.
DR   GO; GO:0048593; P:camera-type eye morphogenesis; IMP:MGI.
DR   GO; GO:0048589; P:developmental growth; IMP:MGI.
DR   GO; GO:0048557; P:embryonic digestive tract morphogenesis; IMP:MGI.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR   GO; GO:0048704; P:embryonic skeletal system morphogenesis; IGI:MGI.
DR   GO; GO:0021798; P:forebrain dorsal/ventral pattern formation; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IGI:MGI.
DR   GO; GO:0007442; P:hindgut morphogenesis; IGI:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0060875; P:lateral semicircular canal development; IMP:MGI.
DR   GO; GO:0030324; P:lung development; IMP:MGI.
DR   GO; GO:0060594; P:mammary gland specification; IGI:MGI.
DR   GO; GO:0001656; P:metanephros development; IGI:MGI.
DR   GO; GO:0046639; P:negative regulation of alpha-beta T cell differentiation; IMP:BHF-UCL.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0045060; P:negative thymic T cell selection; IMP:BHF-UCL.
DR   GO; GO:0042475; P:odontogenesis of dentine-containing tooth; IGI:MGI.
DR   GO; GO:0021631; P:optic nerve morphogenesis; IMP:MGI.
DR   GO; GO:0021543; P:pallium development; IMP:MGI.
DR   GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; IMP:BHF-UCL.
DR   GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IMP:MGI.
DR   GO; GO:0010552; P:positive regulation of gene-specific transcription from RNA polymerase II promoter; IMP:BHF-UCL.
DR   GO; GO:0042307; P:positive regulation of protein import into nucleus; IGI:MGI.
DR   GO; GO:0016485; P:protein processing; IDA:MGI.
DR   GO; GO:0009954; P:proximal/distal pattern formation; IGI:MGI.
DR   GO; GO:0042981; P:regulation of apoptosis; IMP:MGI.
DR   GO; GO:0060831; P:smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IGI:MGI.
DR   GO; GO:0021776; P:smoothened signaling pathway involved in spinal cord motor neuron cell fate specification; IGI:MGI.
DR   GO; GO:0021775; P:smoothened signaling pathway involved in ventral spinal cord interneuron specification; IGI:MGI.
DR   GO; GO:0070242; P:thymocyte apoptosis; IMP:BHF-UCL.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 4.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   2: Evidence at transcript level;
KW   Acetylation; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1   1583       Zinc finger protein GLI3.
FT                                /FTId=PRO_0000047203.
FT   ZN_FING     480    505       C2H2-type 1.
FT   ZN_FING     513    540       C2H2-type 2.
FT   ZN_FING     546    570       C2H2-type 3.
FT   ZN_FING     576    601       C2H2-type 4.
FT   ZN_FING     607    632       C2H2-type 5.
FT   COMPBIAS    120    199       Pro-rich.
FT   COMPBIAS    849    910       Ser-rich.
FT   COMPBIAS   1494   1514       Asp/Glu-rich (acidic).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      19     19       Phosphoserine (By similarity).
FT   CONFLICT    209    209       S -> C (in Ref. 1; CAA64543).
FT   CONFLICT    428    428       D -> G (in Ref. 1; CAA64543).
FT   CONFLICT    928    928       R -> A (in Ref. 1; CAA64543).
FT   CONFLICT    936    936       A -> P (in Ref. 1; CAA64543).
FT   CONFLICT   1005   1005       A -> D (in Ref. 1; CAA64543).
FT   CONFLICT   1185   1186       SA -> R (in Ref. 1; CAA64543).
FT   CONFLICT   1475   1476       NG -> TC (in Ref. 1; CAA64543).
SQ   SEQUENCE   1583 AA;  171655 MW;  37ECC0C3ACF26C24 CRC64;
     MEAQAHSSTA TERKKAENSI GKCPTRTDVS EKAVASSTTS NEDESPGQIY HRERRNAITM
     QPQSVQGLNK ISEEPSTSSD ERASLIKKEI HGSLPHLAEP SLPYRGTVFA MDPRNGYMEP
     HYHPPHLFPA FHPPVPIDAR HHEGRYHYDP SPIPPLHVPS ALSSSPTYPD LPFIRISPHR
     NPTAASESPF SPPHPYINPY MDYIRSLHSS PSLSMISAAR GLSPTDAPHA GVSPAEYYHQ
     MALLTGQRSP YADILPSAAT AGAGAIHMEY LHAMDSTRFP SPRLSARPSR KRTLSISPLS
     DHSFDLQTMI RTSPNSLVTI LNNSRSSSSA SGSYGHLSAS AISPALSFTY PSAPVSLHMH
     QQILSRQQSL GSAFGHSPPL IHPAPTFPTQ RPIPGIPTVL NPVQVSSGPS ESSQSKPTSE
     SAVSSTGDPM HNKRSKIKPD EDLPSPGSRG QQEQPEGTTL VKEEADKDES KQEPEVIYET
     NCHWEGCTRE FDTQDQLVHH INNDHIHGEK KEFVCRWLDC SREQKPFKAQ YMLVVHMRRH
     TGEKPHKCTF EGCTKAYSRL ENLKTHLRSH TGEKPYVCEH EGCNKAFSNA SDRAKHQNRT
     HSNEKPYVCK IPGCTKRYTD PSSLRKHVKT VHGPEAHVTK KQRGDMHPRP PPPRDSGSHS
     QSRSPGRPTQ GAFGEQKELS NTTSKREECL QVKTVKAEKP MTSQPSPGGQ SSCSSQQSPI
     SNYSNSGLEL PLTDGGSVAD LSAIDETPIM DSTISTATTA LALQARRNPA GTKWMEHIKL
     ERLKQVNGMF PRLNPILPSK APAVSPLIGN GTQSNNNYSS GGPGTLLPSR SDLSGVDFTV
     LNTLNRRDSN TSTISSAYLS SRRSSGISPC FSSRRSSEAS QAEGRPQNVS VADSYDPIST
     DASRRSSEAS QGDGLPSLLS LTPVQQYRLK AKYAAATGGP PPTPLPHMER LSLKTKMALL
     GEGRDSGVTL PPVHPPRRCS DGGGHTYRGR HLMPHDALAN SVRRASDPVR TVSENMSLAR
     VQRFSSLNSF NPPNLPPSVE KRSLVLQNYT RQESSQPRYF QASPCPPSIT ENVALEALTM
     DADANLNDED LLPDDVVQYL NSQNQTGYGQ QLQSGISEDS KVAHEPEDLD LAGLPDSHVG
     QEYPALEQPC SEGSKTDLPI QWNEVSSGTS DLSSSKLKCG QQRPSAQQPR GFGLYNNMVV
     HPHNLWKVGT GPAGGYQTLG ENSSTYNGPE HFAIHSGDGL GTNGNTFHEQ PFKTQQYGSQ
     LNRQPLTSSA LDHACGTGIQ GSKLKGNSLQ ENGGLLDFSL SVAPNELAGN TVNGMQTQDQ
     MGQGYIAHQL LSGSMQHQGP SRPGQQVLGQ VGATSHINIY QGTESCLPGT QDNSSQPSSM
     AAIRGYQPCA SYGGNRRQAM PRGNLTLQQG QLSDMSQSSR VNSIKMEAQG QSQQLCSTVQ
     NYSGQFYDQT MGFSQQDRKA GSFSLSDANC LLQGNGTENS ELLSPGANQV TSTVDSFESH
     DLEGVQIDFD AIIDDGDHTS LMSGALSPSI IQNLSHSSSR LTTPRASLPF PSLSMGTTNM
     AIGDMSSLLT SLAEESKFLA VMQ
//
ID   S20A1_MOUSE             Reviewed;         681 AA.
AC   Q61609; A2AKR9; Q3U244; Q8CBJ1; Q91YQ9; Q9QVW6;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Sodium-dependent phosphate transporter 1;
DE   AltName: Full=Gibbon ape leukemia virus receptor 1;
DE            Short=GLVR-1;
DE   AltName: Full=Leukemia virus receptor 1 homolog;
DE   AltName: Full=Phosphate transporter 1;
DE            Short=PiT-1;
DE   AltName: Full=Solute carrier family 20 member 1;
GN   Name=Slc20a1; Synonyms=Glvr1, Pit1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX   PubMed=1531369;
RA   Johann S.V., Gibbons J.J., O'Hara B.;
RT   "GLVR1, a receptor for gibbon ape leukemia virus, is homologous to a
RT   phosphate permease of Neurospora crassa and is expressed at high
RT   levels in the brain and thymus.";
RL   J. Virol. 66:1635-1640(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94321979; PubMed=8046392;
RA   Wilson C.A., Farrell K.B., Eiden M.V.;
RT   "Comparison of cDNAs encoding the gibbon ape leukaemia virus receptor
RT   from susceptible and non-susceptible murine cells.";
RL   J. Gen. Virol. 75:1901-1908(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   MEDLINE=20156390; PubMed=10689185; DOI=10.1016/S0378-1119(00)00010-X;
RA   Palmer G., Manen D., Bonjour J.-P., Caverzasio J.;
RT   "Structure of the murine Pit1 phosphate transporter/retrovirus
RT   receptor gene and functional characterization of its promoter
RT   region.";
RL   Gene 244:35-45(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   FUNCTION.
RX   PubMed=1309898;
RA   Takeuchi Y., Vile R.G., Simpson G., O'Hara B., Collins M.K.,
RA   Weiss R.A.;
RT   "Feline leukemia virus subgroup B uses the same cell surface receptor
RT   as gibbon ape leukemia virus.";
RL   J. Virol. 66:1219-1222(1992).
RN   [8]
RP   MUTAGENESIS OF 553-LYS--ALA-560; 553-LYS--GLU-555 AND LYS-553, AND
RP   REGION.
RX   PubMed=8411375;
RA   Johann S.V., van Zeijl M., Cekleniak J., O'Hara B.;
RT   "Definition of a domain of GLVR1 which is necessary for infection by
RT   gibbon ape leukemia virus and which is highly polymorphic between
RT   species.";
RL   J. Virol. 67:6733-6736(1993).
RN   [9]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=9755124;
RA   Tenenhouse H.S., Roy S., Martel J., Gauthier C.;
RT   "Differential expression, abundance, and regulation of Na+-phosphate
RT   cotransporter genes in murine kidney.";
RL   Am. J. Physiol. 275:F527-F534(1998).
RN   [10]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=99113815; PubMed=9916777; DOI=10.1016/S8756-3282(98)00151-3;
RA   Palmer G., Zhao J., Bonjour J.-P., Hofstetter W., Caverzasio J.;
RT   "In vivo expression of transcripts encoding the Glvr-1 phosphate
RT   transporter/retrovirus receptor during bone development.";
RL   Bone 24:1-7(1999).
RN   [11]
RP   FUNCTION, AND REGION.
RX   PubMed=12097582; DOI=10.1128/JVI.76.15.7683-7693.2002;
RA   Farrell K.B., Russ J.L., Murthy R.K., Eiden M.V.;
RT   "Reassessing the role of region A in Pit1-mediated viral entry.";
RL   J. Virol. 76:7683-7693(2002).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269 AND SER-273, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268; SER-269 AND
RP   SER-273, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Sodium-phosphate symporter which plays a fundamental
CC       housekeeping role in phosphate transport, such as absorbing
CC       phosphate from interstitial fluid for normal cellular functions
CC       such as cellular metabolism, signal transduction, and nucleic acid
CC       and lipid synthesis. May play a role in extracellular matrix and
CC       cartilage calcification as well as in vascular calcification. May
CC       function as a retroviral receptor but do not confer infection
CC       susceptibility to Gibbon Ape Leukemia Virus (GaLV), Simian
CC       sarcoma-associated virus (SSAV) and Feline leukemia virus subgroup
CC       B (FeLV-B).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- DEVELOPMENTAL STAGE: Detected at E17 of embryonic development in a
CC       subpopulation of early hypertrophic chondrocytes in bone, but not
CC       when fully differentiated.
CC   -!- INDUCTION: By growth hormone.
CC   -!- DOMAIN: Region A does not confer susceptibility to infection by
CC       Gibbon Ape Leukemia Virus (GaLV) and Feline leukemia virus
CC       subgroup B (FeLV-B). Substitution of Human SLC20A1 region A by
CC       region A of murine SLC20A1 prevents viral infection.
CC   -!- SIMILARITY: Belongs to the inorganic phosphate transporter (PiT)
CC       (TC 2.A.20) family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC29234.1; Type=Miscellaneous discrepancy; Note=Intron retention. The sequence differs at the 3'end due to intron retention;
CC   -----------------------------------------------------------------------
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DR   EMBL; M73696; AAA74887.1; -; mRNA.
DR   EMBL; AF172634; AAF45041.1; -; Genomic_DNA.
DR   EMBL; AF172628; AAF45041.1; JOINED; Genomic_DNA.
DR   EMBL; AF172629; AAF45041.1; JOINED; Genomic_DNA.
DR   EMBL; AF172630; AAF45041.1; JOINED; Genomic_DNA.
DR   EMBL; AF172631; AAF45041.1; JOINED; Genomic_DNA.
DR   EMBL; AF172632; AAF45041.1; JOINED; Genomic_DNA.
DR   EMBL; AF172633; AAF45041.1; JOINED; Genomic_DNA.
DR   EMBL; AK035898; BAC29234.1; ALT_SEQ; mRNA.
DR   EMBL; AK155506; BAE33298.1; -; mRNA.
DR   EMBL; AL772347; CAM15802.1; -; Genomic_DNA.
DR   EMBL; BC015085; AAH15085.1; -; mRNA.
DR   IPI; IPI00322626; -.
DR   PIR; S27868; S27868.
DR   RefSeq; NP_001153065.1; NM_001159593.1.
DR   RefSeq; NP_056562.1; NM_015747.2.
DR   UniGene; Mm.272675; -.
DR   UniGene; Mm.401622; -.
DR   ProteinModelPortal; Q61609; -.
DR   STRING; Q61609; -.
DR   PhosphoSite; Q61609; -.
DR   PRIDE; Q61609; -.
DR   Ensembl; ENSMUST00000028880; ENSMUSP00000028880; ENSMUSG00000027397.
DR   Ensembl; ENSMUST00000110315; ENSMUSP00000105944; ENSMUSG00000027397.
DR   GeneID; 20515; -.
DR   KEGG; mmu:20515; -.
DR   UCSC; uc008mhk.1; mouse.
DR   UCSC; uc008mhl.1; mouse.
DR   CTD; 20515; -.
DR   MGI; MGI:108392; Slc20a1.
DR   eggNOG; roNOG09188; -.
DR   GeneTree; ENSGT00390000014879; -.
DR   HOGENOM; HBG681698; -.
DR   HOVERGEN; HBG053358; -.
DR   InParanoid; Q61609; -.
DR   OMA; VEMYNST; -.
DR   OrthoDB; EOG428212; -.
DR   PhylomeDB; Q61609; -.
DR   NextBio; 298723; -.
DR   ArrayExpress; Q61609; -.
DR   Bgee; Q61609; -.
DR   CleanEx; MM_SLC20A1; -.
DR   Genevestigator; Q61609; -.
DR   GermOnline; ENSMUSG00000027397; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR001204; Phos_transporter.
DR   PANTHER; PTHR11101; Phos_transporter; 1.
DR   Pfam; PF01384; PHO4; 1.
PE   1: Evidence at protein level;
KW   Membrane; Phosphate transport; Phosphoprotein; Receptor; Symport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    681       Sodium-dependent phosphate transporter 1.
FT                                /FTId=PRO_0000080772.
FT   TOPO_DOM      1     24       Extracellular (Potential).
FT   TRANSMEM     25     45       Helical; (Potential).
FT   TOPO_DOM     46     65       Cytoplasmic (Potential).
FT   TRANSMEM     66     86       Helical; (Potential).
FT   TOPO_DOM     87    105       Extracellular (Potential).
FT   TRANSMEM    106    126       Helical; (Potential).
FT   TOPO_DOM    127    161       Cytoplasmic (Potential).
FT   TRANSMEM    162    182       Helical; (Potential).
FT   TOPO_DOM    183    200       Extracellular (Potential).
FT   TRANSMEM    201    221       Helical; (Potential).
FT   TOPO_DOM    222    233       Cytoplasmic (Potential).
FT   TRANSMEM    234    254       Helical; (Potential).
FT   TOPO_DOM    255    513       Extracellular (Potential).
FT   TRANSMEM    514    534       Helical; (Potential).
FT   TOPO_DOM    535    560       Cytoplasmic (Potential).
FT   TRANSMEM    561    581       Helical; (Potential).
FT   TOPO_DOM    582    601       Extracellular (Potential).
FT   TRANSMEM    602    622       Helical; (Potential).
FT   TOPO_DOM    623    651       Cytoplasmic (Potential).
FT   TRANSMEM    652    672       Helical; (Potential).
FT   TOPO_DOM    673    681       Extracellular (Potential).
FT   REGION      553    560       A.
FT   MOD_RES     268    268       Phosphoserine.
FT   MOD_RES     269    269       Phosphoserine.
FT   MOD_RES     271    271       Phosphoserine (By similarity).
FT   MOD_RES     273    273       Phosphoserine.
FT   MUTAGEN     553    560       KQEASTKA->DTGDVSSKV: Confers virus
FT                                infectibility.
FT   MUTAGEN     553    555       KQE->DTGD: Confers virus infectibility.
FT   MUTAGEN     553    553       K->DT: Confers virus infectibility.
FT   CONFLICT    190    190       R -> H (in Ref. 2).
FT   CONFLICT    368    368       T -> A (in Ref. 2).
FT   CONFLICT    446    446       D -> E (in Ref. 2).
FT   CONFLICT    490    490       E -> G (in Ref. 6; AAH15085).
FT   CONFLICT    568    568       L -> P (in Ref. 4; BAE33298).
FT   CONFLICT    569    569       Y -> T (in Ref. 2).
FT   CONFLICT    639    639       R -> I (in Ref. 2).
FT   CONFLICT    672    672       A -> AA (in Ref. 2).
SQ   SEQUENCE   681 AA;  74153 MW;  F337B0982B5A297D CRC64;
     MESTVATITS TLAAVTASAP PKYDNLWMLI LGFIIAFVLA FSVGANDVAN SFGTAVGSGV
     VTLKQACILA SIFETVGSAL LGAKVSETIR NGLIDVELYN ETQDLLMAGS VSAMFGSAVW
     QLVASFLKLP ISGTHCIVGA TIGFSLVANG QKGVKWSELI KIVMSWFVSP LLSGIMSGIL
     FFLVRAFILR KADPVPNGLR ALPIFYACTI GINLFSIMYT GAPLLGFDKL PLWGTILISV
     GCAVFCALIV WFFVCPRMKR KIEREVKSSP SESPLMEKKS NLKEDHEETK MAPGDVEHRN
     PVSEVVCATG PLRAVVEERT VSFKLGDLEE APERERLPMD LKEETSIDST INGAVQLPNG
     NLVQFSQTVS NQINSSGHYQ YHTVHKDSGL YKELLHKLHL AKVGDCMGDS GDKPLRRNNS
     YTSYTMAICG MPLDSFRAKE GEQKGDEMET LTWPNADTKK RIRMDSYTSY CNAVSDLHSE
     SEMDMSVKAE MGLGDRKGSS GSLEEWYDQD KPEVSLLFQF LQILTACFGS FAHGGNDVSN
     AIGPLVALYL VYKQEASTKA ATPIWLLLYG GVGICMGLWV WGRRVIQTMG KDLTPITPSS
     GFSIELASAL TVVIASNIGL PISTTHCKVG SVVSVGWLRS KKAVDWRLFR NIFMAWFVTV
     PISGVISAAI MAVFKYIILP V
//
ID   DRD1_MOUSE              Reviewed;         446 AA.
AC   Q61616; B2RPW8; Q8C8P8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2003, sequence version 2.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=D(1A) dopamine receptor;
DE   AltName: Full=Dopamine D1 receptor;
GN   Name=Drd1; Synonyms=Drd1a, Gpcr15;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 193-279.
RC   TISSUE=Testis;
RX   MEDLINE=94116980; PubMed=8288218; DOI=10.1006/geno.1993.1452;
RA   Wilkie T.M., Chen Y., Gilbert D.J., Moore K.J., Yu L., Simon M.I.,
RA   Copeland N.G., Jenkins N.A.;
RT   "Identification, chromosomal location, and genome organization of
RT   mammalian G-protein-coupled receptors.";
RL   Genomics 18:175-184(1993).
CC   -!- FUNCTION: This is one of the five types (D1 to D5) of receptors
CC       for dopamine. The activity of this receptor is mediated by G
CC       proteins which activate adenylyl cyclase.
CC   -!- SUBUNIT: Interacts with DNAJC14 via its C-terminus (By
CC       similarity). Interacts with DRD1IP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity). Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity). Note=Transport from the
CC       endoplasmic reticulum to the cell surface is regulated by
CC       interaction with DNAJC14 (By similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK044723; BAC32050.1; -; mRNA.
DR   EMBL; BC137641; AAI37642.1; -; mRNA.
DR   EMBL; BC137655; AAI37656.1; -; mRNA.
DR   EMBL; L20336; AAA16848.1; -; mRNA.
DR   IPI; IPI00123490; -.
DR   RefSeq; NP_034206.1; NM_010076.3.
DR   UniGene; Mm.54161; -.
DR   ProteinModelPortal; Q61616; -.
DR   SMR; Q61616; 22-346.
DR   STRING; Q61616; -.
DR   PhosphoSite; Q61616; -.
DR   PRIDE; Q61616; -.
DR   Ensembl; ENSMUST00000021932; ENSMUSP00000021932; ENSMUSG00000021478.
DR   GeneID; 13488; -.
DR   KEGG; mmu:13488; -.
DR   UCSC; uc007qnz.1; mouse.
DR   CTD; 13488; -.
DR   MGI; MGI:99578; Drd1a.
DR   eggNOG; roNOG04390; -.
DR   HOGENOM; HBG445348; -.
DR   HOVERGEN; HBG106962; -.
DR   InParanoid; Q61616; -.
DR   OMA; ITFDVFV; -.
DR   OrthoDB; EOG4BG8W3; -.
DR   PhylomeDB; Q61616; -.
DR   NextBio; 283997; -.
DR   ArrayExpress; Q61616; -.
DR   Bgee; Q61616; -.
DR   CleanEx; MM_DRD1A; -.
DR   Genevestigator; Q61616; -.
DR   GermOnline; ENSMUSG00000021478; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0001590; F:dopamine D1 receptor activity; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007191; P:activation of adenylate cyclase activity by dopamine receptor signaling pathway; IDA:MGI.
DR   GO; GO:0060158; P:activation of phospholipase C activity by dopamine receptor signaling pathway; IDA:MGI.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0014002; P:astrocyte development; IMP:MGI.
DR   GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR   GO; GO:0048148; P:behavioral response to cocaine; IMP:MGI.
DR   GO; GO:0021853; P:cerebral cortex GABAergic interneuron migration; IMP:MGI.
DR   GO; GO:0001661; P:conditioned taste aversion; IMP:MGI.
DR   GO; GO:0021542; P:dentate gyrus development; IMP:MGI.
DR   GO; GO:0015872; P:dopamine transport; IMP:MGI.
DR   GO; GO:0046323; P:glucose import; IMP:MGI.
DR   GO; GO:0007625; P:grooming behavior; IMP:MGI.
DR   GO; GO:0060292; P:long term synaptic depression; IMP:MGI.
DR   GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
DR   GO; GO:0007617; P:mating behavior; IDA:MGI.
DR   GO; GO:0007613; P:memory; IMP:MGI.
DR   GO; GO:0035106; P:operant conditioning; IMP:MGI.
DR   GO; GO:0030432; P:peristalsis; IGI:MGI.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:MGI.
DR   GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:MGI.
DR   GO; GO:0006606; P:protein import into nucleus; IMP:MGI.
DR   GO; GO:0019228; P:regulation of action potential in neuron; IMP:MGI.
DR   GO; GO:0042053; P:regulation of dopamine metabolic process; IMP:MGI.
DR   GO; GO:0001975; P:response to amphetamine; IMP:MGI.
DR   GO; GO:0042493; P:response to drug; IDA:MGI.
DR   GO; GO:0046960; P:sensitization; IGI:MGI.
DR   GO; GO:0021756; P:striatum development; IMP:MGI.
DR   GO; GO:0001963; P:synaptic transmission, dopaminergic; IMP:MGI.
DR   GO; GO:0001659; P:temperature homeostasis; IMP:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR001413; Dopa_1A_rcpt.
DR   InterPro; IPR000929; Dopamine_rcpt.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00565; DOPAMINED1AR.
DR   PRINTS; PR00242; DOPAMINER.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; Endoplasmic reticulum;
KW   G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
KW   Palmitate; Receptor; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN         1    446       D(1A) dopamine receptor.
FT                                /FTId=PRO_0000069375.
FT   TOPO_DOM      1     22       Extracellular (Potential).
FT   TRANSMEM     23     48       Helical; Name=1; (Potential).
FT   TOPO_DOM     49     59       Cytoplasmic (Potential).
FT   TRANSMEM     60     86       Helical; Name=2; (Potential).
FT   TOPO_DOM     87     95       Extracellular (Potential).
FT   TRANSMEM     96    118       Helical; Name=3; (Potential).
FT   TOPO_DOM    119    137       Cytoplasmic (Potential).
FT   TRANSMEM    138    162       Helical; Name=4; (Potential).
FT   TOPO_DOM    163    192       Extracellular (Potential).
FT   TRANSMEM    193    218       Helical; Name=5; (Potential).
FT   TOPO_DOM    219    272       Cytoplasmic (Potential).
FT   TRANSMEM    273    299       Helical; Name=6; (Potential).
FT   TOPO_DOM    300    312       Extracellular (Potential).
FT   TRANSMEM    313    337       Helical; Name=7; (Potential).
FT   TOPO_DOM    338    446       Cytoplasmic (Potential).
FT   LIPID       347    347       S-palmitoyl cysteine (By similarity).
FT   LIPID       351    351       S-palmitoyl cysteine (By similarity).
FT   CARBOHYD      4      4       N-linked (GlcNAc...) (Potential).
FT   DISULFID     95    186       By similarity.
FT   CONFLICT    193    196       TYAI -> DIRH (in Ref. 3).
FT   CONFLICT    240    240       N -> S (in Ref. 3; AAA16848).
SQ   SEQUENCE   446 AA;  49612 MW;  509BA66F9DF82A74 CRC64;
     MAPNTSTMDE TGLPVERDFS FRILTACFLS LLILSTLLGN TLVCAAVIRF RHLRSKVTNF
     FVISLAVSDL LVAVLVMPWK AVAEIAGFWP FGSFCNIWVA FDIMCSTASI LNLCVISVDR
     YWAISSPFQY ERKMTPKAAF ILISVAWTLS VLISFIPVQL SWHKAKPTWP LDGNFTSLED
     AEDDNCDTRL SRTYAISSSL ISFYIPVAIM IVTYTSIYRI AQKQIRRISA LERAAVHAKN
     CQTTTGNGNP VECSQSESSF KMSFKRETKV LKTLSVIMGV FVCCWLPFFI SNCMVPFCGS
     EETQPFCIDS ITFDVFVWFG WANSSLNPII YAFNADFQKA FSTLLGCYRL CPTTNNAIET
     VSINNNGAVM FSSHHEPRGS ISKDCNLVYL IPHAVGSSED LKREEAGGIP KPLEKLSPAL
     SVILDYDTDV SLEKIQPVTH SGQHST
//
ID   ZN148_MOUSE             Reviewed;         794 AA.
AC   Q61624; P97475;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 2.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Zinc finger protein 148;
DE   AltName: Full=Beta enolase repressor factor 1;
DE   AltName: Full=G-rich box-binding protein;
DE   AltName: Full=Transcription factor BFCOL1;
DE   AltName: Full=Transcription factor ZBP-89;
DE   AltName: Full=Zinc finger DNA-binding protein 89;
GN   Name=Znf148; Synonyms=Zbp89, Zfp148;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CD-1; TISSUE=Limb;
RX   MEDLINE=98079087; PubMed=9417107; DOI=10.1074/jbc.273.1.484;
RA   Passantino R., Antona V., Barbieri G., Rubino P., Melchionna R.,
RA   Cossu G., Feo S., Giallongo A.;
RT   "Negative regulation of beta enolase gene transcription in embryonic
RT   muscle is dependent upon a zinc finger factor that binds to the G-rich
RT   box within the muscle-specific enhancer.";
RL   J. Biol. Chem. 273:484-494(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 26-794.
RX   MEDLINE=97184139; PubMed=9030551; DOI=10.1074/jbc.272.8.4915;
RA   Hasegawa T., Takeuchi A., Miyaishi O., Isobe K., de Crombrugghe B.;
RT   "Cloning and characterization of a transcription factor that binds to
RT   the proximal promoters of the two mouse type I collagen genes.";
RL   J. Biol. Chem. 272:4915-4923(1997).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-305 AND SER-306, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Involved in transcriptional regulation. Represses the
CC       transcription of a number of genes including gastrin, stromelysin
CC       and enolase. Binds to the G-rich box in the enhancer region of
CC       these genes.
CC   -!- SUBUNIT: Interacts with HNRPDL (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family.
CC   -!- SIMILARITY: Contains 4 C2H2-type zinc fingers.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X98096; CAA66725.1; -; mRNA.
DR   EMBL; BC026144; AAH26144.1; -; mRNA.
DR   EMBL; U80078; AAB38507.1; -; mRNA.
DR   IPI; IPI00123531; -.
DR   RefSeq; NP_035879.1; NM_011749.4.
DR   UniGene; Mm.392667; -.
DR   ProteinModelPortal; Q61624; -.
DR   SMR; Q61624; 135-385.
DR   STRING; Q61624; -.
DR   PhosphoSite; Q61624; -.
DR   PRIDE; Q61624; -.
DR   Ensembl; ENSMUST00000089677; ENSMUSP00000087106; ENSMUSG00000022811.
DR   GeneID; 22661; -.
DR   KEGG; mmu:22661; -.
DR   UCSC; uc007zab.1; mouse.
DR   CTD; 22661; -.
DR   MGI; MGI:1332234; Zfp148.
DR   eggNOG; roNOG14306; -.
DR   HOGENOM; HBG717076; -.
DR   HOVERGEN; HBG054247; -.
DR   InParanoid; Q61624; -.
DR   OMA; RMCHENR; -.
DR   OrthoDB; EOG43N7C2; -.
DR   PhylomeDB; Q61624; -.
DR   NextBio; 303071; -.
DR   ArrayExpress; Q61624; -.
DR   Bgee; Q61624; -.
DR   CleanEx; MM_ZFP148; -.
DR   Genevestigator; Q61624; -.
DR   GermOnline; ENSMUSG00000022811; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007276; P:gamete generation; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 4.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   1: Evidence at protein level;
KW   Acetylation; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Repeat; Repressor; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    794       Zinc finger protein 148.
FT                                /FTId=PRO_0000047428.
FT   ZN_FING     171    193       C2H2-type 1.
FT   ZN_FING     199    221       C2H2-type 2.
FT   ZN_FING     227    249       C2H2-type 3.
FT   ZN_FING     255    278       C2H2-type 4.
FT   MOD_RES     194    194       Phosphothreonine (By similarity).
FT   MOD_RES     250    250       Phosphoserine (By similarity).
FT   MOD_RES     305    305       Phosphothreonine.
FT   MOD_RES     306    306       Phosphoserine.
FT   MOD_RES     412    412       Phosphoserine (By similarity).
FT   MOD_RES     607    607       N6-acetyllysine (By similarity).
FT   MOD_RES     784    784       Phosphoserine (By similarity).
FT   CONFLICT    283    283       K -> N (in Ref. 3; AAB38507).
FT   CONFLICT    314    314       K -> P (in Ref. 3; AAB38507).
FT   CONFLICT    319    319       K -> Q (in Ref. 3; AAB38507).
SQ   SEQUENCE   794 AA;  88751 MW;  4CB1C2A1822703FD CRC64;
     MNIDDKLEGL FLKCGGIDEM QSSRAMVVMG GVSGQSAVSG ELQESVLQDR SLPHQEILAA
     DEVLQESEMR QQDMISHDEL MVHEETVKND EEQMDTHERL PQGLQYALNV PISVKQEITF
     TDVSEQLMRD KKQVREPVDL QKKKKRKQRS PAKILTINED GSLGLKTPKS HVCEHCNAAF
     RTNYHLQRHV FIHTGEKPFQ CSQCDMRFIQ KYLLQRHEKI HTGEKPFRCD ECGMRFIQKY
     HMERHKRTHS GEKPYQCEYC LQYFSRTDRV LKHKRMCHEN HDKKLNRCAI KGGLLTSEED
     SGFSTSPKDN SLPKKKRQKT EKKSSGMDKE SVLDKSDLKK DKNDYLPLYS SSTKVKDEYM
     VAEYAVEMPH SSVGGSHLED ASGEIHPPKL VLKKINSKRS LKQPLEQSQT ISPLSSYEDS
     KVSKYAFELV DKQALLDSEG SADIDQVDNL QEGPSKPVHS STNYDDAMQF LKKKRYLQAA
     SNNSREYALN VGTIASQPSV TQAAVASVID ESTTASILDS QALNVEIKSN HDKNVIPDEV
     LQTLLDHYSH KPNGQHEISF SVADTEVTSS ISINSSDVPE VTQSENVGSS SQASSSDKAN
     MLQEYSKFLQ QALDRTSQND AYLNSPSLNF VTDNQTLPNP PAFSSIDKQV YAAMPINSFR
     SGMNSPLRTT PDKSHFGLIV GDSQHPFPFS GDETNHASAT STADFLDQVT SQKKAEAQPV
     HQAYQMSSFE QPFRAPYHGS RAGIATQFST ANGQVNLRGP GTSAEFSEFP LVNVNDNRAG
     MTSSPDATTG QTFG
//
ID   GRID2_MOUSE             Reviewed;        1007 AA.
AC   Q61625; A4QPG1;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 105.
DE   RecName: Full=Glutamate receptor delta-2 subunit;
DE            Short=GluR delta-2 subunit;
DE   Flags: Precursor;
GN   Name=Grid2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=94107327; PubMed=7506541; DOI=10.1006/bbrc.1993.2614;
RA   Araki K., Meguro H., Kushiya E., Takayama C., Inoue Y., Mishina M.;
RT   "Selective expression of the glutamate receptor channel delta 2
RT   subunit in cerebellar Purkinje cells.";
RL   Biochem. Biophys. Res. Commun. 197:1267-1276(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH GOPC AND BECN1, AND DOMAIN.
RX   MEDLINE=22260737; PubMed=12372286; DOI=10.1016/S0896-6273(02)00861-9;
RA   Yue Z., Horton A., Bravin M., DeJager P.L., Selimi F., Heintz N.;
RT   "A novel protein complex linking the delta 2 glutamate receptor and
RT   autophagy: implications for neurodegeneration in lurcher mice.";
RL   Neuron 35:921-933(2002).
RN   [4]
RP   INTERACTION WITH SHANK1 AND SHANK2, MUTAGENESIS OF SER-920, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=15207857; DOI=10.1016/j.mcn.2004.02.007;
RA   Uemura T., Mori H., Mishina M.;
RT   "Direct interaction of GluRdelta2 with Shank scaffold proteins in
RT   cerebellar Purkinje cells.";
RL   Mol. Cell. Neurosci. 26:330-341(2004).
RN   [5]
RP   INTERACTION WITH GRID2IP.
RX   PubMed=17027646; DOI=10.1016/j.bbrc.2006.09.109;
RA   Sonoda T., Mochizuki C., Yamashita T., Watanabe-Kaneko K., Miyagi Y.,
RA   Shigeri Y., Yazama F., Okuda K., Kawamoto S.;
RT   "Binding of glutamate receptor delta2 to its scaffold protein,
RT   Delphilin, is regulated by PKA.";
RL   Biochem. Biophys. Res. Commun. 350:748-752(2006).
RN   [6]
RP   VARIANT LURCHER THR-654.
RC   TISSUE=Purkinje cell;
RX   MEDLINE=97429950; PubMed=9285588; DOI=10.1038/42009;
RA   Zuo J., De Jager P.L., Takahashi K.A., Jiang W., Linden D.J.,
RA   Heintz N.;
RT   "Neurodegeneration in Lurcher mice caused by mutation in delta2
RT   glutamate receptor gene.";
RL   Nature 388:769-773(1997).
CC   -!- FUNCTION: Receptor for glutamate. L-glutamate acts as an
CC       excitatory neurotransmitter at many synapses in the central
CC       nervous system. The postsynaptic actions of Glu are mediated by a
CC       variety of receptors that are named according to their selective
CC       agonists.
CC   -!- SUBUNIT: Interacts with AIP1 and AP4M1 (By similarity). Interacts
CC       with BECN1, GOPC, GRID2IP, SHANK1 and SHANK2.
CC   -!- INTERACTION:
CC       Q9R171:Cbln1; NbExp=2; IntAct=EBI-2794106, EBI-2794140;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity). Cell junction, synapse, postsynaptic cell
CC       membrane; Multi-pass membrane protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed selectively in cerebellar Purkinje
CC       cells where it is localized in dendritic spines.
CC   -!- DOMAIN: The PDZ-binding motif mediates interaction with GOPC.
CC   -!- DISEASE: Note=Defects in Grid2 are the cause of the Lurcher
CC       phenotype. Heterozygous animals display a characteristic swaying
CC       of the hind quarters and jerky up and down movements following
CC       cerebellar Purkinje cell degeneration during postnatal
CC       development. Homozygous animals die shortly after birth because of
CC       a massive loss of midbrain and hindbrain neurons during late
CC       embryogenesis.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel
CC       (TC 1.A.10.1) family. GRID2 subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D13266; BAA02524.1; -; mRNA.
DR   EMBL; BC139823; AAI39824.1; -; mRNA.
DR   IPI; IPI00123534; -.
DR   PIR; PN0156; PN0156.
DR   RefSeq; NP_032193.1; NM_008167.2.
DR   UniGene; Mm.439651; -.
DR   UniGene; Mm.447390; -.
DR   ProteinModelPortal; Q61625; -.
DR   SMR; Q61625; 435-811.
DR   IntAct; Q61625; 43.
DR   MINT; MINT-126960; -.
DR   STRING; Q61625; -.
DR   TCDB; 1.A.10.1.8; glutamate-gated ion channel (GIC) family of neurotransmitter receptors.
DR   PhosphoSite; Q61625; -.
DR   PRIDE; Q61625; -.
DR   Ensembl; ENSMUST00000095852; ENSMUSP00000093536; ENSMUSG00000071424.
DR   GeneID; 14804; -.
DR   KEGG; mmu:14804; -.
DR   UCSC; uc009cdz.1; mouse.
DR   CTD; 14804; -.
DR   MGI; MGI:95813; Grid2.
DR   HOGENOM; HBG443816; -.
DR   HOVERGEN; HBG051840; -.
DR   InParanoid; Q61625; -.
DR   OMA; VWWSRTW; -.
DR   OrthoDB; EOG4SBDX4; -.
DR   NextBio; 286973; -.
DR   ArrayExpress; Q61625; -.
DR   Bgee; Q61625; -.
DR   CleanEx; MM_GRID2; -.
DR   Genevestigator; Q61625; -.
DR   GermOnline; ENSMUSG00000071424; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
DR   GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0004970; F:ionotropic glutamate receptor activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0060134; P:prepulse inhibition; IMP:MGI.
DR   GO; GO:0060079; P:regulation of excitatory postsynaptic membrane potential; IMP:MGI.
DR   GO; GO:0043523; P:regulation of neuron apoptosis; IGI:MGI.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR019594; Glu_rcpt_Glu/Gly-bd.
DR   InterPro; IPR001320; Iontro_glu_rcpt.
DR   InterPro; IPR001508; NMDA_rcpt.
DR   InterPro; IPR001638; SBP_bac_3.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   PRINTS; PR00177; NMDARECEPTOR.
DR   SMART; SM00918; Lig_chan-Glu_bd; 1.
DR   SMART; SM00079; PBPe; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Disease mutation; Glycoprotein;
KW   Ion transport; Ionic channel; Ligand-gated ion channel; Membrane;
KW   Postsynaptic cell membrane; Receptor; Signal; Synapse; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     23       Potential.
FT   CHAIN        24   1007       Glutamate receptor delta-2 subunit.
FT                                /FTId=PRO_0000011565.
FT   TOPO_DOM     24    566       Extracellular (Potential).
FT   TRANSMEM    567    587       Helical; (Potential).
FT   TOPO_DOM    588    635       Cytoplasmic (Potential).
FT   TRANSMEM    636    656       Helical; (Potential).
FT   TOPO_DOM    657    830       Extracellular (Potential).
FT   TRANSMEM    831    851       Helical; (Potential).
FT   TOPO_DOM    852   1007       Cytoplasmic (Potential).
FT   REGION      921    991       Interaction with AP4M1 (By similarity).
FT   MOTIF      1005   1007       PDZ-binding.
FT   CARBOHYD    293    293       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    426    426       N-linked (GlcNAc...) (Potential).
FT   VARIANT     654    654       A -> T (in Lurcher).
FT   MUTAGEN     920    920       S->A: Abolishes interaction with SHANK1
FT                                and SHANK2.
SQ   SEQUENCE   1007 AA;  113082 MW;  A456166CC782A44B CRC64;
     MEVFPLLLFL SFCWSRTWDL ATADSIIHIG AIFDESAKKD DEVFRTAVGD LNQNEEILQT
     EKITFSVTFV DGNNPFQAVQ EACELMNQGI LALVSSIGCT SAGSLQSLAD AMHIPHLFIQ
     RSTAGTPRSG CGLTRSNRND DYTLSVRPPV YLNEVILRVV TEYAWQKFII FYDSEYDIRG
     IQEFLDKVSQ QGMDVALQKV ENNINKMITT LFDTMRIEEL NRYRDTLRRA ILVMNPATAK
     SFISEVVETN LVAFDCHWII INEEINDVDV QELVRRSIGR LTIIRQTFPV PQNISQRCFR
     GNHRISSSLC DPKDPFAQNM EISNLYIYDT VLLLANAFHK KLEDRKWHSM ASLSCIRKNS
     KPWQGGRSML ETIKKGGVNG LTGDLEFGEN GGNPNVHFEI LGTNYGEELG RGVRKLGCWN
     PVTGLNGSLT DKKLENNMRG VVLRVVTVLE EPFVMVSENV LGKPKKYQGF SIDVLDALSN
     YLGFNYEIYV APDHKYGSPQ EDGTWNGLVG ELVFKRADIG ISALTITPDR ENVVDFTTRY
     MDYSVGVLLR RAEKTVDMFA CLAPFDLSLW ACIAGTVLLV GLLVYLLNWL NPPRLQMGSM
     TSTTLYNSMW FVYGSFVQQG GEVPYTTLAT RMMMGAWWLF ALIVISSYTA NLAAFLTITR
     IESSIQSLQD LSKQTDIPYG TVLDSAVYQH VRMKGLNPFE RDSMYSQMWR MINRSNGSEN
     NVLESQAGIQ KVKYGNYAFV WDAAVLEYVA INDPDCSFYT VGNTVADRGY GIALQHGSPY
     RDVFSQRILE LQQSGDMDIL KHKWWPKNGQ CDLYSSVDAK QKGGALDIKS LAGVFCILAA
     GIVLSCLIAV LETWWSRRKG SRVPSKEDDK EIDLEHLHRR VNSLCTDDDS PHKQFSTSSI
     DLTPLDIDTL PTRQALEQIS DFRNTHITTT TFIPEQIQTL SRTLSAKAAS GFAFGSVPEH
     RTGPFRHRAP NGGFFRSPIK TMSSIPYQPT PTLGLNLGND PDRGTSI
//
ID   GRIK5_MOUSE             Reviewed;         979 AA.
AC   Q61626;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Glutamate receptor, ionotropic kainate 5;
DE   AltName: Full=Glutamate receptor KA-2;
DE            Short=KA2;
DE   AltName: Full=Glutamate receptor gamma-2;
DE            Short=GluR gamma-2;
DE   Flags: Precursor;
GN   Name=Grik5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Forebrain;
RX   MEDLINE=92153418; PubMed=1310861; DOI=10.1016/0896-6273(92)90293-M;
RA   Sakimura K., Morita T., Kushiya E., Mishina M.;
RT   "Primary structure and expression of the gamma 2 subunit of the
RT   glutamate receptor channel selective for kainate.";
RL   Neuron 8:267-274(1992).
CC   -!- FUNCTION: Receptor for glutamate. L-glutamate acts as an
CC       excitatory neurotransmitter at many synapses in the central
CC       nervous system. The postsynaptic actions of Glu are mediated by a
CC       variety of receptors that are named according to their selective
CC       agonists. This receptor binds kainate > quisqualate = glutamate >>
CC       AMPA.
CC   -!- SUBUNIT: Associates with GRIK1 (both edited and unedited
CC       versions), GRIK2, or GRIK3 to form functional channels. Homomeric
CC       associations do not produce any channel activity (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Cell junction, synapse, postsynaptic cell membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel
CC       (TC 1.A.10.1) family. GRIK5 subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D10011; BAA00899.1; -; mRNA.
DR   IPI; IPI00123538; -.
DR   PIR; JH0589; JH0589.
DR   UniGene; Mm.2879; -.
DR   ProteinModelPortal; Q61626; -.
DR   SMR; Q61626; 22-829.
DR   STRING; Q61626; -.
DR   PRIDE; Q61626; -.
DR   Ensembl; ENSMUST00000003468; ENSMUSP00000003468; ENSMUSG00000003378.
DR   UCSC; uc009frh.1; mouse.
DR   MGI; MGI:95818; Grik5.
DR   HOGENOM; HBG381523; -.
DR   HOVERGEN; HBG051839; -.
DR   InParanoid; Q61626; -.
DR   OrthoDB; EOG4RV2QP; -.
DR   ArrayExpress; Q61626; -.
DR   Bgee; Q61626; -.
DR   Genevestigator; Q61626; -.
DR   GermOnline; ENSMUSG00000003378; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0032983; C:kainate selective glutamate receptor complex; IPI:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:MGI.
DR   GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0015277; F:kainate selective glutamate receptor activity; IGI:MGI.
DR   GO; GO:0060079; P:regulation of excitatory postsynaptic membrane potential; IMP:MGI.
DR   GO; GO:0031630; P:regulation of synaptic vesicle fusion to presynaptic membrane; IMP:MGI.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR019594; Glu_rcpt_Glu/Gly-bd.
DR   InterPro; IPR001320; Iontro_glu_rcpt.
DR   InterPro; IPR001508; NMDA_rcpt.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR   PRINTS; PR00177; NMDARECEPTOR.
DR   SMART; SM00918; Lig_chan-Glu_bd; 1.
DR   SMART; SM00079; PBPe; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Glycoprotein; Ion transport;
KW   Ionic channel; Ligand-gated ion channel; Membrane; Polymorphism;
KW   Postsynaptic cell membrane; Receptor; Signal; Synapse; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     14       Potential.
FT   CHAIN        15    979       Glutamate receptor, ionotropic kainate 5.
FT                                /FTId=PRO_0000011553.
FT   TOPO_DOM     15    544       Extracellular (Potential).
FT   TRANSMEM    545    565       Helical; (Potential).
FT   TOPO_DOM    566    622       Cytoplasmic (Potential).
FT   TRANSMEM    623    643       Helical; (Potential).
FT   TOPO_DOM    644    803       Extracellular (Potential).
FT   TRANSMEM    804    824       Helical; (Potential).
FT   TOPO_DOM    825    979       Cytoplasmic (Potential).
FT   COMPBIAS    860    866       Poly-Arg.
FT   CARBOHYD    219    219       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    271    271       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    285    285       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    322    322       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    372    372       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    394    394       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    400    400       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    407    407       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    414    414       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    478    478       N-linked (GlcNAc...) (Potential).
FT   VARIANT     610    610       V -> I.
SQ   SEQUENCE   979 AA;  109262 MW;  123C071BAF0C4E16 CRC64;
     MPAELLLLLI VAFANPSCQV LSSLRMAAIL DDQTVCGRGE RLALALAREQ INGIIEVPAK
     ARVEVDIFEL QRDSQYETTD TMCQILPKGV VSVLGPSSSP ASASTVSHIC GEKEIPHIKV
     GPEETPRLQY LRFASVSLYP SNEDVSLAVS RILKSFNYPS ASLICAKAEC LLRLEELVRG
     FLISKETLSV RMLDDSRDPT PLLKEIRDDK VSTIIIDANA SISHLVLRKA SELGMTSAFY
     KYILTTMDFP ILHLDGIVED SSNILGFSMF NTSHPFYPEF VRSLNMSWRE NCEASTYPGP
     ALSAALMFDA VHVVVSAVRE LNRSQEIGVK PLACTSANIW PHGTSLMNYL RMVEYDGLTG
     RVEFNSKGQR TNYTLRILEK SRQGHREIGV WYSNRTLAMN ATTLDINLSQ TLANKTLVVT
     TILENPYVMR RPNFQALSGN ERFEGFCVDM LRELAELLRF RYRLRLVEDG LYGAPEPNGS
     WTGMVGELIN RKADLAVAAF TITAEREKVI DFSKPFMTLG ISILYRVHMG RKPGYFSFLD
     PFSPAVWLFM LLAYLAVSCV LFLAARLSPY EWYNPHPCLR ARPHILENQY TLGNSLWFPV
     GGFMQQGSEV MPRALSTRCV SGVWWAFTLI IISSYTANLA AFLTVQRMEV PVESADDLAD
     QTNIEYGTIH AGSTMTFFQN SRYQTYQRMW NYMQSKQPSV FVKSTEEGIA RVLNSRYAFL
     LESTMNEYHR RLNCNLTQIG GLLDTKGYGI GMPLGSPFRD EITLAILQLQ ENNRLEILKR
     KWWEGGRCPK EEDHRAKGLG MENIGGIFVV LICGLIIAVF VAVMEFIWST RRSAESEEVS
     VCQEMLQELR HAVSCRKTSR SRRRRRPGGP SRALLSLRAV REMRLSNGKL YSAGAGGDAG
     AHGGPQRLLD DPGPPGGPRP QAPTPCTHVR VCQECRRIQA LRASGAGAPP RGLGTPAEAT
     SPPRPRPGPT GPRELTEHE
//
ID   GRID1_MOUSE             Reviewed;        1009 AA.
AC   Q61627;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Glutamate receptor delta-1 subunit;
DE            Short=GluR delta-1 subunit;
DE   Flags: Precursor;
GN   Name=Grid1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=ICR; TISSUE=Forebrain;
RX   MEDLINE=92198486; PubMed=1372507; DOI=10.1016/0006-291X(92)90566-4;
RA   Yamazaki M., Araki K., Shibata A., Mishina M.;
RT   "Molecular cloning of a cDNA encoding a novel member of the mouse
RT   glutamate receptor channel family.";
RL   Biochem. Biophys. Res. Commun. 183:886-892(1992).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518 AND THR-523, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
CC   -!- FUNCTION: Receptor for glutamate. L-glutamate acts as an
CC       excitatory neurotransmitter at many synapses in the central
CC       nervous system. The postsynaptic actions of Glu are mediated by a
CC       variety of receptors that are named according to their selective
CC       agonists.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity). Cell junction, synapse, postsynaptic cell
CC       membrane; Multi-pass membrane protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Equally in forebrain and cerebellum.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel
CC       (TC 1.A.10.1) family. GRID1 subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D10171; BAA01041.1; -; mRNA.
DR   IPI; IPI00123542; -.
DR   PIR; JH0266; JH0266.
DR   UniGene; Mm.121569; -.
DR   UniGene; Mm.413604; -.
DR   UniGene; Mm.477417; -.
DR   ProteinModelPortal; Q61627; -.
DR   SMR; Q61627; 22-856.
DR   MINT; MINT-1791814; -.
DR   STRING; Q61627; -.
DR   PhosphoSite; Q61627; -.
DR   PRIDE; Q61627; -.
DR   Ensembl; ENSMUST00000043349; ENSMUSP00000044009; ENSMUSG00000041078.
DR   MGI; MGI:95812; Grid1.
DR   GeneTree; ENSGT00590000083017; -.
DR   HOGENOM; HBG443816; -.
DR   HOVERGEN; HBG051840; -.
DR   InParanoid; Q61627; -.
DR   OrthoDB; EOG4ZCT3V; -.
DR   ArrayExpress; Q61627; -.
DR   Bgee; Q61627; -.
DR   CleanEx; MM_GRID1; -.
DR   Genevestigator; Q61627; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0004970; F:ionotropic glutamate receptor activity; IEA:InterPro.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR019594; Glu_rcpt_Glu/Gly-bd.
DR   InterPro; IPR001320; Iontro_glu_rcpt.
DR   InterPro; IPR001508; NMDA_rcpt.
DR   InterPro; IPR001638; SBP_bac_3.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   PRINTS; PR00177; NMDARECEPTOR.
DR   SMART; SM00918; Lig_chan-Glu_bd; 1.
DR   SMART; SM00079; PBPe; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Glycoprotein; Ion transport;
KW   Ionic channel; Ligand-gated ion channel; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Receptor; Signal; Synapse; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21   1009       Glutamate receptor delta-1 subunit.
FT                                /FTId=PRO_0000011562.
FT   TOPO_DOM     21    562       Extracellular (Potential).
FT   TRANSMEM    563    583       Helical; (Potential).
FT   TOPO_DOM    584    637       Cytoplasmic (Potential).
FT   TRANSMEM    638    658       Helical; (Potential).
FT   TOPO_DOM    659    830       Extracellular (Potential).
FT   TRANSMEM    831    851       Helical; (Potential).
FT   TOPO_DOM    852   1009       Cytoplasmic (Potential).
FT   MOD_RES     518    518       Phosphoserine.
FT   MOD_RES     523    523       Phosphothreonine.
FT   CARBOHYD    200    200       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    422    422       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    498    498       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   1009 AA;  112244 MW;  F6B3EECB7A108486 CRC64;
     MEALTLWLLP WICQCVTVRA DSIIHIGAIF EENAAKDDRV FQLAVSDLSL NDDILQSEKI
     TYSIKVIEAN NPFQAVQEAC DLMTQGILAL VTSTGCASAN ALQSLTDAMH IPHLFVQRNP
     GGSPRTACHL NPSPDGEAYT LASRPPVRLN DVMLRLVTEL RWQKFVMFYD SEYDIRGFQS
     FLDQASRLGL DVSLQKVDKN ISHVFTSLFT TMKTEELNRY RDTLRRAILL LSPQGAHSFI
     NEAVETNLAS KDSHWVFVNE EISDPEILDL VHSALGRMTV VRQIFPSAKD NQKCMRNNHR
     ISSLLCDPQE GYLQMLQISN LYLYDSVLML ANAFHRKLED RKWHSMASLN CIRKSTKPWN
     GGRSMLDTIK KGHITGLTGV MEFREDSSNP YVQFEILGTT YSETFGKDMR KLATWDSEKG
     LNGSLQERPM GSRLQGLTLK VVTVLEEPFV MVAENILGQP KRYKGFSIDV LDALAKALGF
     KYEIYQAPDG RYGHQLHNTS WNGMIGELIS KRADLAISAI TITPERESVV DFSKRYMDYS
     VGILIKKPEE KISIFSLFAP FDFAVWACIA AAIPVVGVLI FVLNRIQAVR SQSATQPRPS
     ASATLHSAIW IVYGAFVQQG GESSVNSVAM RIVMGSWWLF TLIVCSSYTA NLAAFLTVSR
     MDNPIRTFQD LSKQLEMSYG TVRDSAVYEY FRAKGTNPLE QDSTFAELWR TISKNGGADN
     CVSNPSEGIR KAKKGNYAFL WDVAVVEYAA LTDDDCSVTV IGNSISSKGY GIALQHGSPY
     RDLFSQRILE LQDTGDLDVL KQKWWPHTGR CDLTSHSSTQ TEGKSLKLHS FAGVFCILAI
     GLLLACLVAA LELWWNSNRC HQETPKEDKE VNLEQVHRRI NSLMDEDIAH KQISPASIEL
     SALEMGGLAP SQALEPTREY QNTQLSVSTF LPEQSSHGTS RTLSSGPSSN LPLPLSSSAT
     MPSIQCKHRS PNGGLFRQSP VKTPIPMSFQ PVPGGVLPEA LDTSHGTSI
//
ID   PACN1_MOUSE             Reviewed;         441 AA.
AC   Q61644;
DT   13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Protein kinase C and casein kinase substrate in neurons protein 1;
GN   Name=Pacsin1; Synonyms=Pacsin;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=98417447; PubMed=9746365;
RX   DOI=10.1046/j.1432-1327.1998.2560201.x;
RA   Plomann M., Lange R., Vopper G., Cremer H., Heinlein U.A.O.,
RA   Scheff S., Baldwin S.A., Leitges M., Cramer M., Paulsson M.,
RA   Barthels D.;
RT   "PACSIN, a brain protein that is upregulated upon differentiation into
RT   neuronal cells.";
RL   Eur. J. Biochem. 256:201-211(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 52-62; 71-79; 319-341 AND 425-441, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   FUNCTION.
RX   MEDLINE=20534871; PubMed=11082044;
RA   Modregger J., Ritter B., Witter B., Paulsson M., Plomann M.;
RT   "All three PACSIN isoforms bind to endocytic proteins and inhibit
RT   endocytosis.";
RL   J. Cell Sci. 113:4511-4521(2000).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-391, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: May play a role in vesicle formation and transport.
CC   -!- SUBUNIT: Homo- and hetero-aggregates with other PACSINs. Binds
CC       dynamin I, synaptojanin, synapsin I and the neural Wiskott-Aldrich
CC       syndrome protein (N-WASP) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=Colocalizes
CC       with dynamin I at vesicular structures in the cell body and
CC       neurites (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in CNS neurons, especially in
CC       the pyramidal cells of the hippocampus, Purkinje cells of the
CC       cerebellum and large neurons of the cortex and brain stem.
CC   -!- DEVELOPMENTAL STAGE: Expression is seen at embryonic day 17 and is
CC       up-regulated developmentally with a correlation to neuronal
CC       differentiation.
CC   -!- PTM: Phosphorylated by casein kinase 2 (CK2) and protein kinase C
CC       (PKC) (Probable).
CC   -!- SIMILARITY: Belongs to the PACSIN family.
CC   -!- SIMILARITY: Contains 1 FCH domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X85124; CAA59437.1; -; mRNA.
DR   EMBL; BC014698; AAH14698.1; -; mRNA.
DR   IPI; IPI00123613; -.
DR   RefSeq; NP_035991.1; NM_011861.2.
DR   RefSeq; NP_848142.1; NM_178365.3.
DR   UniGene; Mm.4926; -.
DR   PDB; 2X3V; X-ray; 2.45 A; A/B/C=1-337.
DR   PDB; 2X3W; X-ray; 2.64 A; A/B/C=1-337, D=382-441.
DR   PDB; 2X3X; X-ray; 3.35 A; A/B/C=1-337, D/E=382-441.
DR   PDBsum; 2X3V; -.
DR   PDBsum; 2X3W; -.
DR   PDBsum; 2X3X; -.
DR   ProteinModelPortal; Q61644; -.
DR   SMR; Q61644; 13-304, 385-440.
DR   STRING; Q61644; -.
DR   PhosphoSite; Q61644; -.
DR   UCD-2DPAGE; Q61644; -.
DR   PRIDE; Q61644; -.
DR   Ensembl; ENSMUST00000045896; ENSMUSP00000044168; ENSMUSG00000040276.
DR   Ensembl; ENSMUST00000097360; ENSMUSP00000094973; ENSMUSG00000040276.
DR   Ensembl; ENSMUST00000114872; ENSMUSP00000110522; ENSMUSG00000040276.
DR   Ensembl; ENSMUST00000114873; ENSMUSP00000110523; ENSMUSG00000040276.
DR   GeneID; 23969; -.
DR   KEGG; mmu:23969; -.
DR   UCSC; uc008bpj.1; mouse.
DR   CTD; 23969; -.
DR   MGI; MGI:1345181; Pacsin1.
DR   GeneTree; ENSGT00510000046376; -.
DR   HOGENOM; HBG446365; -.
DR   HOVERGEN; HBG053486; -.
DR   InParanoid; Q61644; -.
DR   OMA; NSSYIHV; -.
DR   OrthoDB; EOG4QVCC5; -.
DR   PhylomeDB; Q61644; -.
DR   NextBio; 303847; -.
DR   ArrayExpress; Q61644; -.
DR   Bgee; Q61644; -.
DR   Genevestigator; Q61644; -.
DR   GermOnline; ENSMUSG00000040276; Mus musculus.
DR   GO; GO:0030137; C:COPI-coated vesicle; IDA:MGI.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IDA:MGI.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0045806; P:negative regulation of endocytosis; IDA:MGI.
DR   GO; GO:0007165; P:signal transduction; TAS:MGI.
DR   InterPro; IPR001060; FCH.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50133; FCH; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Cytoplasm; Direct protein sequencing;
KW   Endocytosis; Phosphoprotein; SH3 domain.
FT   CHAIN         1    441       Protein kinase C and casein kinase
FT                                substrate in neurons protein 1.
FT                                /FTId=PRO_0000161793.
FT   DOMAIN       10     73       FCH.
FT   DOMAIN      382    441       SH3.
FT   COILED      144    165       Potential.
FT   COILED      183    217       Potential.
FT   MOD_RES     391    391       Phosphotyrosine.
FT   HELIX        23     30
FT   HELIX        34     69
FT   HELIX        77     80
FT   HELIX        84    104
FT   HELIX       106    117
FT   HELIX       127    133
FT   HELIX       137    175
FT   STRAND      176    178
FT   HELIX       182    212
FT   HELIX       217    221
FT   HELIX       225    253
FT   HELIX       255    257
FT   HELIX       260    272
FT   HELIX       277    287
SQ   SEQUENCE   441 AA;  50575 MW;  21BEB339A14A41F9 CRC64;
     MSGSYDEASE EITDSFWEVG NYKRTVKRID DGHRLCNDLM SCVQERAKIE KAYAQQLTDW
     AKRWRQLIEK GPQYGSLERA WGAMMTEADK VSELHQEVKN SLLNEDLEKV KNWQKDAYHK
     QIMGGFKETK EAEDGFRKAQ KPWAKKMKEL EAAKKAYHLA CKEERLAMTR EMNSKTEQSV
     TPEQQKKLVD KVDKCRQDVQ KTQEKYEKVL EDVGKTTPQY MEGMEQVFEQ CQQFEEKRLV
     FLKEVLLDIK RHLNLAENSS YMHVYRELEQ AIRGADAQED LRWFRSTSGP GMPMNWPQFE
     EWNPDLPHTT AKKEKQPKKA EGATLSNATG AVESTSQAGD RGSVSSYDRG QTYATEWSDD
     ESGNPFGGNE ANGGANPFED DAKGVRVRAL YDYDGQEQDE LSFKAGDELT KLGEEDEQGW
     CRGRLDSGQL GLYPANYVEA I
//
ID   CBX5_MOUSE              Reviewed;         191 AA.
AC   Q61686; Q9CS35; Q9CXD1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Chromobox protein homolog 5;
DE   AltName: Full=Heterochromatin protein 1 homolog alpha;
DE            Short=HP1 alpha;
GN   Name=Cbx5; Synonyms=Hp1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH HP1BP3.
RX   MEDLINE=97133299; PubMed=8978696;
RA   le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H.,
RA   Jeanmougin F., Losson R., Chambon P.;
RT   "A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic
RT   control of transcription by nuclear receptors.";
RL   EMBO J. 15:6701-6715(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20560699; PubMed=11107181;
RX   DOI=10.1002/1098-2264(2000)9999:9999<::AID-GCC1058>3.3.CO;2-1;
RA   Li Y.-J., Pak B.J., Higgins R.R., Lu S.-J., Ben-David Y.;
RT   "Contiguous arrangement of p45 NFE2, HnRNP A1, and HP1 alpha on mouse
RT   chromosome 15 and human chromosome 12: evidence for suppression of
RT   these genes due to retroviral integration within the Fli-2 locus.";
RL   Genes Chromosomes Cancer 30:91-95(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Ovary, and Pituitary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH TRIM28.
RX   PubMed=10562550; DOI=10.1093/emboj/18.22.6385;
RA   Nielsen A.L., Ortiz J.A., You J., Oulad-Abdelghani M., Khechumian R.,
RA   Gansmuller A., Chambon P., Losson R.;
RT   "Interaction with members of the heterochromatin protein 1 (HP1)
RT   family and histone deacetylation are differentially involved in
RT   transcriptional silencing by members of the TIF1 family.";
RL   EMBO J. 18:6385-6395(1999).
RN   [6]
RP   INTERACTION WITH SUV420H1 AND SUV420H2.
RX   PubMed=15145825; DOI=10.1101/gad.300704;
RA   Schotta G., Lachner M., Sarma K., Ebert A., Sengupta R., Reuter G.,
RA   Reinberg D., Jenuwein T.;
RT   "A silencing pathway to induce H3-K9 and H4-K20 trimethylation at
RT   constitutive heterochromatin.";
RL   Genes Dev. 18:1251-1262(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-93, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-12; SER-13 AND
RP   SER-14, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Component of heterochromatin that recognizes and binds
CC       histone H3 tails methylated at 'Lys-9' (H3K9me), leading to
CC       epigenetic repression. In contrast, it is excluded from chromatin
CC       when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph). Can
CC       interact with lamin-B receptor (LBR). This interaction can
CC       contribute to the association of the heterochromatin with the
CC       inner nuclear membrane. Involved in the formation of functional
CC       kinetochore through interaction with MIS12 complex proteins (By
CC       similarity).
CC   -!- SUBUNIT: Interacts directly with ATRX, CHAF1A, LBR, NIPBL, SP100
CC       and STAM2 via the chromoshadow domain. Can interact directly with
CC       CBX3 via the chromoshadow domain. Interacts with histone H3
CC       methylated at 'Lys-9'. Interacts with BAHD1, SETDB1, MIS12 and
CC       DSN1 (By similarity). Interacts directly with TRIM28 via the
CC       chromoshadow domain. Interacts with SUV420H1 and SUV420H2.
CC       Interacts with HP1BP3. Interacts with POGZ; POGZ and PXVXL motif-
CC       containing proteins such as INCENP and TRIM28 compete for
CC       interaction with CBX5. Interacts with INCENP and TRIM24 (By
CC       similarity).
CC   -!- INTERACTION:
CC       P68431:HIST1H3A (xeno); NbExp=1; IntAct=EBI-307973, EBI-79722;
CC       Q64127:Trim24; NbExp=1; IntAct=EBI-307973, EBI-307947;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere.
CC       Note=Component of centromeric and pericentromeric heterochromatin.
CC       Associates with chromosomes during mitosis. Associates
CC       specifically with chromatin during metaphase and anaphase.
CC   -!- PTM: Phosphorylation of HP1 and LBR may be responsible for some of
CC       the alterations in chromatin organization and nuclear structure
CC       which occur at various times during the cell cycle. Phosphorylated
CC       during interphase and possibly hyper-phosphorylated during mitosis
CC       (By similarity).
CC   -!- PTM: Ubiquitinated (By similarity).
CC   -!- SIMILARITY: Contains 2 chromo domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; X99641; CAA67960.1; -; mRNA.
DR   EMBL; AF216290; AAF80993.1; -; mRNA.
DR   EMBL; AK008792; BAB25897.1; -; mRNA.
DR   EMBL; AK018349; BAB31173.1; -; mRNA.
DR   EMBL; AK030366; BAC26923.1; -; mRNA.
DR   EMBL; AK030442; BAC26966.1; -; mRNA.
DR   EMBL; AK032975; BAC28107.1; -; mRNA.
DR   EMBL; AK019198; BAB31596.1; -; mRNA.
DR   EMBL; BC004707; AAH04707.1; -; mRNA.
DR   IPI; IPI00123755; -.
DR   RefSeq; NP_001070257.1; NM_001076789.1.
DR   RefSeq; NP_001103686.1; NM_001110216.1.
DR   RefSeq; NP_031652.1; NM_007626.3.
DR   UniGene; Mm.262059; -.
DR   ProteinModelPortal; Q61686; -.
DR   SMR; Q61686; 18-68, 112-170.
DR   DIP; DIP-28137N; -.
DR   IntAct; Q61686; 6.
DR   MINT; MINT-191222; -.
DR   STRING; Q61686; -.
DR   PhosphoSite; Q61686; -.
DR   PRIDE; Q61686; -.
DR   Ensembl; ENSMUST00000108813; ENSMUSP00000104441; ENSMUSG00000009575.
DR   Ensembl; ENSMUST00000118152; ENSMUSP00000113157; ENSMUSG00000009575.
DR   Ensembl; ENSMUST00000122182; ENSMUSP00000113158; ENSMUSG00000009575.
DR   GeneID; 12419; -.
DR   KEGG; mmu:12419; -.
DR   UCSC; uc007xxl.1; mouse.
DR   CTD; 12419; -.
DR   MGI; MGI:109372; Cbx5.
DR   eggNOG; roNOG12282; -.
DR   GeneTree; ENSGT00510000046310; -.
DR   HOGENOM; HBG314523; -.
DR   HOVERGEN; HBG000400; -.
DR   InParanoid; Q61686; -.
DR   OMA; TWHEEGD; -.
DR   OrthoDB; EOG4NVZMP; -.
DR   PhylomeDB; Q61686; -.
DR   NextBio; 281216; -.
DR   ArrayExpress; Q61686; -.
DR   Bgee; Q61686; -.
DR   CleanEx; MM_CBX5; -.
DR   Genevestigator; Q61686; -.
DR   GermOnline; ENSMUSG00000009575; Mus musculus.
DR   GO; GO:0010369; C:chromocenter; IDA:MGI.
DR   GO; GO:0000118; C:histone deacetylase complex; IDA:BHF-UCL.
DR   GO; GO:0035097; C:histone methyltransferase complex; IDA:BHF-UCL.
DR   GO; GO:0000776; C:kinetochore; IDA:MGI.
DR   GO; GO:0005720; C:nuclear heterochromatin; IDA:MGI.
DR   GO; GO:0005730; C:nucleolus; IDA:MGI.
DR   GO; GO:0017053; C:transcriptional repressor complex; IDA:BHF-UCL.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
DR   GO; GO:0035064; F:methylated histone residue binding; ISS:UniProtKB.
DR   GO; GO:0030674; F:protein binding, bridging; IPI:BHF-UCL.
DR   GO; GO:0070491; F:repressing transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0006333; P:chromatin assembly or disassembly; IEA:InterPro.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:MGI.
DR   InterPro; IPR017984; Chromo_dom_subgr.
DR   InterPro; IPR008251; Chromo_shadow.
DR   InterPro; IPR018125; Chromo_shadow_sbgrp.
DR   InterPro; IPR000953; Chromodomain.
DR   InterPro; IPR016197; Chromodomain-like.
DR   Pfam; PF00385; Chromo; 1.
DR   Pfam; PF01393; Chromo_shadow; 1.
DR   PRINTS; PR00504; CHROMODOMAIN.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00300; ChSh; 1.
DR   SUPFAM; SSF54160; Chromodomain-like; 2.
DR   PROSITE; PS00598; CHROMO_1; 1.
DR   PROSITE; PS50013; CHROMO_2; 2.
PE   1: Evidence at protein level;
KW   Centromere; Chromosome; Nucleus; Phosphoprotein; Repeat;
KW   Ubl conjugation.
FT   CHAIN         1    191       Chromobox protein homolog 5.
FT                                /FTId=PRO_0000080209.
FT   DOMAIN       20     78       Chromo 1.
FT   DOMAIN      121    179       Chromo 2; shadow subtype.
FT   COMPBIAS     11     14       Poly-Ser.
FT   MOD_RES       8      8       Phosphothreonine (By similarity).
FT   MOD_RES      11     11       Phosphoserine.
FT   MOD_RES      12     12       Phosphoserine.
FT   MOD_RES      13     13       Phosphoserine.
FT   MOD_RES      14     14       Phosphoserine.
FT   MOD_RES      92     92       Phosphoserine.
FT   MOD_RES      93     93       Phosphoserine.
FT   MOD_RES      97     97       Phosphoserine (By similarity).
FT   MOD_RES     110    110       Phosphoserine (By similarity).
FT   CONFLICT     68     68       K -> R (in Ref. 3; BAB31173).
FT   CONFLICT    165    165       I -> M (in Ref. 3; BAB31596).
SQ   SEQUENCE   191 AA;  22186 MW;  8AB87E2F00DB8C40 CRC64;
     MGKKTKRTAD SSSSEDEEEY VVEKVLDRRM VKGQVEYLLK WKGFSEEHNT WEPEKNLDCP
     ELISEFMKKY KKMKEGENNK PREKSEGNKR KSSFSNSADD IKSKKKREQS NDIARGFERG
     LEPEKIIGAT DSCGDLMFLM KWKDTDEADL VLAKEANVKC PQIVIAFYEE RLTWHAYPED
     AENKEKESAK S
//
ID   ATRX_MOUSE              Reviewed;        2476 AA.
AC   Q61687;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 2.
DT   08-MAR-2011, entry version 100.
DE   RecName: Full=Transcriptional regulator ATRX;
DE            EC=3.6.4.12;
DE   AltName: Full=ATP-dependent helicase ATRX;
DE   AltName: Full=HP1 alpha-interacting protein;
DE   AltName: Full=HP1-BP38 protein;
DE   AltName: Full=Heterochromatin protein 2;
DE   AltName: Full=X-linked nuclear protein;
GN   Name=Atrx; Synonyms=Hp1bp2, Xnp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98213653; PubMed=9545503; DOI=10.1007/s003359900781;
RA   Picketts D.J., Tastan A.O., Higgs D.R., Gibbons R.J.;
RT   "Comparison of the human and murine ATRX gene identifies highly
RT   conserved, functionally important domains.";
RL   Mamm. Genome 9:400-403(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 325-1176.
RX   MEDLINE=97133299; PubMed=8978696;
RA   le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H.,
RA   Jeanmougin F., Losson R., Chambon P.;
RT   "A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic
RT   control of transcription by nuclear receptors.";
RL   EMBO J. 15:6701-6715(1996).
RN   [3]
RP   SUBCELLULAR LOCATION, AND ASSOCIATION WITH PERICENTROMERIC
RP   HETEROCHROMATIN.
RX   MEDLINE=20040663; PubMed=10570185; DOI=10.1073/pnas.96.24.13983;
RA   McDowell T.L., Gibbons R.J., Sutherland H., O'Rourke D.M.,
RA   Bickmore W.A., Pombo A., Turley H., Gatter K., Picketts D.J.,
RA   Buckle V.J., Chapman L., Rhodes D., Higgs D.R.;
RT   "Localization of a putative transcriptional regulator (ATRX) at
RT   pericentromeric heterochromatin and the short arms of acrocentric
RT   chromosomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:13983-13988(1999).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588; SER-626; SER-1339
RP   AND SER-1512, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; SER-717; SER-719;
RP   SER-1041; SER-1290; SER-1335 AND SER-1339, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Could be a global transcriptional regulator. Modifies
CC       gene expression by affecting chromatin.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Probably binds EZH2. Binds annexin V in a calcium and
CC       phosphatidylcholine/phosphatidylserine-dependent manner. Interacts
CC       directly with CBX5 via the PxVxL motif (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Associated with
CC       pericentromeric heterochromatin during interphase and mitosis,
CC       probably by interacting with HP1.
CC   -!- DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is
CC       required for interaction with chromoshadow domains. This motif
CC       requires additional residues -7, -6, +4 and +5 of the central Val
CC       which contact the chromoshadow domain.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC   -!- SIMILARITY: Contains 1 GATA-type zinc finger.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 PHD-type zinc finger.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF026032; AAC08741.1; -; mRNA.
DR   EMBL; X99643; CAA67962.1; -; mRNA.
DR   IPI; IPI00322707; -.
DR   UniGene; Mm.10141; -.
DR   ProteinModelPortal; Q61687; -.
DR   SMR; Q61687; 157-295, 1533-2206.
DR   STRING; Q61687; -.
DR   PhosphoSite; Q61687; -.
DR   PRIDE; Q61687; -.
DR   Ensembl; ENSMUST00000113573; ENSMUSP00000109203; ENSMUSG00000031229.
DR   UCSC; uc009ubb.1; mouse.
DR   MGI; MGI:103067; Atrx.
DR   HOGENOM; HBG714755; -.
DR   HOVERGEN; HBG000104; -.
DR   InParanoid; Q61687; -.
DR   OrthoDB; EOG4PVNXQ; -.
DR   ArrayExpress; Q61687; -.
DR   Bgee; Q61687; -.
DR   Genevestigator; Q61687; -.
DR   GermOnline; ENSMUSG00000031229; Mus musculus.
DR   GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR   GO; GO:0000228; C:nuclear chromosome; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS00344; GATA_ZN_FINGER_1; FALSE_NEG.
DR   PROSITE; PS50114; GATA_ZN_FINGER_2; FALSE_NEG.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS01359; ZF_PHD_1; FALSE_NEG.
DR   PROSITE; PS50016; ZF_PHD_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW   Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   2476       Transcriptional regulator ATRX.
FT                                /FTId=PRO_0000074303.
FT   DOMAIN     1566   1753       Helicase ATP-binding.
FT   DOMAIN     2008   2188       Helicase C-terminal.
FT   ZN_FING     170    199       GATA-type; atypical.
FT   ZN_FING     219    267       PHD-type.
FT   NP_BIND    1579   1586       ATP (Potential).
FT   MOTIF       573    586       PxVxL motif.
FT   MOTIF      1704   1707       DEGH box.
FT   COMPBIAS    319    322       Poly-Ser.
FT   COMPBIAS    735    738       Poly-Ser.
FT   COMPBIAS   1001   1004       Poly-Glu.
FT   COMPBIAS   1130   1135       Poly-Ser.
FT   COMPBIAS   1182   1185       Poly-Ser.
FT   COMPBIAS   1238   1245       Poly-Asp.
FT   COMPBIAS   1484   1487       Poly-Glu.
FT   COMPBIAS   1924   1931       Poly-Ser.
FT   COMPBIAS   2205   2208       Poly-Lys.
FT   COMPBIAS   2245   2248       Poly-Glu.
FT   COMPBIAS   2403   2408       Poly-Gln.
FT   MOD_RES      71     71       Phosphoserine (By similarity).
FT   MOD_RES      74     74       Phosphoserine (By similarity).
FT   MOD_RES      87     87       Phosphothreonine (By similarity).
FT   MOD_RES      89     89       Phosphotyrosine (By similarity).
FT   MOD_RES      92     92       Phosphoserine.
FT   MOD_RES     111    111       Phosphoserine (By similarity).
FT   MOD_RES     586    586       Phosphoserine (By similarity).
FT   MOD_RES     588    588       Phosphoserine.
FT   MOD_RES     590    590       Phosphoserine (By similarity).
FT   MOD_RES     626    626       Phosphoserine.
FT   MOD_RES     663    663       Phosphoserine (By similarity).
FT   MOD_RES     665    665       Phosphoserine (By similarity).
FT   MOD_RES     717    717       Phosphoserine.
FT   MOD_RES     719    719       Phosphoserine.
FT   MOD_RES     828    828       Phosphoserine (By similarity).
FT   MOD_RES     829    829       Phosphoserine (By similarity).
FT   MOD_RES     854    854       Phosphoserine (By similarity).
FT   MOD_RES     855    855       Phosphoserine (By similarity).
FT   MOD_RES    1041   1041       Phosphoserine.
FT   MOD_RES    1290   1290       Phosphoserine.
FT   MOD_RES    1335   1335       Phosphoserine.
FT   MOD_RES    1339   1339       Phosphoserine.
FT   MOD_RES    1512   1512       Phosphoserine.
FT   MOD_RES    1975   1975       Phosphoserine (By similarity).
FT   MOD_RES    1979   1979       Phosphoserine (By similarity).
FT   MOD_RES    2203   2203       Phosphoserine (By similarity).
SQ   SEQUENCE   2476 AA;  278604 MW;  90A42B790FC4FF4C CRC64;
     MTAEPMSGNK LSTLVQKLHD FLAHSSEESE ETCSSPRLVM NQSTDKICGS GLNSDMMENN
     KEEGASTSEK SRSSGSSRSK RKPSIVTKYV ESDDEKPTDE NVNEKAATEN SENDITMQSL
     PKGTVIVQPE PVLNEDKDDF KGPEFRSRSK MKADNLIKRG EDGLHGIVSC TACGQQVNHF
     QKDSIYRHPS LKVLICKNCF KYYMSDDISR DSDGMDEQCR WCAEGGNLIC CDFCHNAFCK
     KCILRNLGRK ELSTIMDENN QWYCYICQPE PLLDLVTACN SVFENLEQLL QQNKKKIKVD
     SEKTSKVCDQ TSKFSPKKSS SSCNGEEKKL EESCSGSVSS TYSHSALSVP KEMIKKTTKL
     IETTSNMNSS YIKFLKQAAD NSEMTSAMKL CQLKSFKSVL DDIKKAHLAL EEDLNSEIQA
     LDDVHKEKNT KDLKSTDAKS ETKLGKGEKS YSTEKREFLK LDARSSVKAI DGEEQRAHKS
     TSGEHKGSGR KDGSQYEPTN TPEDLDMDIV SVPSSVPEDI FDSLESAMEV QSSADYQGDG
     NSGTEPELES SSVKLNVSSK DSRGNIKSKV TAKVRKELFV KLTPVSLSNS PIKGVDCQEV
     SQEKNGRKSS GVARSSEKCR PREEISDHEN NVTILLEDSD LRRSPRVKTT PLRRQTESNP
     AMSNSDEESN GTMKEKQKMS GPIRKKDKRN SADCATDNPK PHKVPKAKQP VIGDQNSDSD
     EMLAVLKEAS QMGHSSSSDT DINEPQMNHK GKTGKDDNGK RKRKNSTSGS DFDTKKGKST
     ETSIISKKKR QNYSESSNYD SELEREIKTM SRIGAARKSV PEKKEEDSSE DEKQGKKVVD
     NGGHERAKTT QEGSSADDTG DTEGRQGGSC SIAGGSIEKV RSGVEFREML CKPGVSSDGA
     EKPSVKEENV NSPEDKRVSK TKEKTKHLRS RQSRKGKGGS SDGTDRFPKK EQSDESSEGE
     KKQSRQRPGT KGKKAPDLKG ETLKREQEWD SSSDGTERLP EEEEIGPFSK GIKQSKTDTA
     GGEKKGKKWK DKSCEKKEEL SDSVDKLPGK GDSCDSSEDK KTRNRVSLRE KKRFSLPAKS
     PGKRPECSSS DTEKSLKGQC CDSTEKRPKR IDLRERRNSS SKRNTKEVKS ASSSSDAEGS
     SEDNKKQKKQ RTSAKKKTGN TKEKKRNSLR ATPKRKQVDI TSSSSDIGDD DQNSAGEESS
     DEQKIKPVTE NLVLPSHTGF CQSSGDEALS KSVPATVDDD DDDNDPENRI AKKMLLEEIK
     ANLSSDEDGS SDDEPDGGGK KRIGKQSEES PADDGELRRE QLAVNQVNSE SDSDSEESKK
     PRYRHRLLRH KLTLSDGESG EEKPTKPKEH KEAKGRNRRK VSSEDSEDTD FQESGVSEEV
     SESEDEQRPR TRSAKKAELE ENQRSYKQKK KRRRIKVQED SSSENKSHSE EDKKEGDEED
     EEDEDEDEED ENDDSKSPGK GRKKIRKILK DDKLRTETQN ALKEEEERRK RIAERERERE
     KLREVIEIED ASPTKCPITT KLVLDENEET KEPLVQVHRN MVIKLKPHQV DGVQFMWDCC
     CESVEKTKKS PGSGCILAHC MGLGKTLQVV SFLHTVLLCD KLDFSTALVV CPLNTALNWM
     NEFEKWQEGL NDNEKLEVSE LATVKRPQER SYMLQRWQED GGVMIIGYEM YRNLAQGRNV
     KSRKLKDIFN KALVDPGPDF VVCDEGHILK NEASAVSKAM NSIKSRRRII LTGTPLQNNL
     IEYHCMVNFI KENLLGSIKE FRNRFINPIQ NGQCADSTMV DVRVMKKRAH ILYEMLAGCV
     QRKDYTALTK FLPPKHEYVL AVRMTAIQCK LYQYYLDHLT GVGNSTEGGR GKAGAKLFQD
     FQMLSRIWTH PWCLQLDYIS KENKGYFDED SMDEFIASDS DETSKSLSSD EKKKPKGKKG
     KKDSSSSGSG SDNDVEVIKV WNSRSRGGGD GNMDDTGNNP SVSLKLDESK TTSTSNPSSP
     APDWYKDFVT DTDAEVLEHS GKMVLLFEIL RMAEEIGDKV LVFSQSLISL DLIEDFLELA
     SREKTEDKEK PLIYKGEGKW IRNIDYYRLD GSTNAQSRKK WAEEFNDETN VRGRLFIIST
     KAGSLGINLV AANRVIIFDA SWNPSYDIQS IFRVYRFGQT KPVYVYRFLA QGTMEDKIYD
     RQVTKQSLSF RVVDQQQVER HFTMNELTEL YTFEPDLLDD PNSEKKKKRD TPMLPKDTIL
     AELLQIHKEH IVGYHEHDSL LDHKEEEELT EEERKAAWAE YEAEKKGLTM RFNIPTGTNL
     PPVTFTSQTP YIPFNLGALS AMSNQQLEDL INQGREKVVE ATNSMTAVRI QPLEDIISTV
     WKENMNLSEA QVQALALSRQ ASQELDVKRR EAIYNDVLTK QQMLINCVQR ILMNRRLQQQ
     YTQQQQQQLT YQQATLSHLM MPKPPNLIMT PSNYQQIDMR GMYQSVAGGM QPPPLQRAPP
     PTVRSKNPGP SPGKSM
//
ID   HS105_MOUSE             Reviewed;         858 AA.
AC   Q61699; Q3TNS2; Q3UIY8; Q62578; Q62579; Q6A0A5; Q8C430; Q8VCW6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 109.
DE   RecName: Full=Heat shock protein 105 kDa;
DE   AltName: Full=42 degrees C-HSP;
DE   AltName: Full=Heat shock 110 kDa protein;
DE   AltName: Full=Heat shock-related 100 kDa protein E7I;
DE            Short=HSP-E7I;
GN   Name=Hsph1; Synonyms=Hsp105, Hsp110, Kiaa0201;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM HSP105-ALPHA).
RX   MEDLINE=96013135; PubMed=7556594; DOI=10.1016/0014-5793(95)00884-C;
RA   Morozov A., Subjeck J., Raychaudhuri P.;
RT   "HPV16 E7 oncoprotein induces expression of a 110 kDa heat shock
RT   protein.";
RL   FEBS Lett. 371:214-218(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS HSP105-ALPHA AND HSP105-BETA).
RX   MEDLINE=96102018; PubMed=8530361; DOI=10.1074/jbc.270.50.29718;
RA   Yasuda K., Nakai A., Hatayama T., Nagata K.;
RT   "Cloning and expression of murine high molecular mass heat shock
RT   proteins, HSP105.";
RL   J. Biol. Chem. 270:29718-29723(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
RP   HSP105-ALPHA).
RC   STRAIN=BALB/c;
RX   MEDLINE=99167340; PubMed=10066425; DOI=10.1006/bbrc.1999.0283;
RA   Yasuda K., Ishihara K., Nakashima K., Hatayama T.;
RT   "Genomic cloning and promoter analysis of the mouse 105-kDa heat shock
RT   protein (HSP105) gene.";
RL   Biochem. Biophys. Res. Commun. 256:75-80(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HSP105-ALPHA).
RC   STRAIN=C57BL/6J; TISSUE=Eye, Hippocampus, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM HSP105-ALPHA).
RC   STRAIN=NMRI; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 54-68; 74-82; 361-374 AND 462-471, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 289-858.
RC   TISSUE=Pancreatic islet;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [8]
RP   INTERACTION WITH HSPA8.
RX   PubMed=9675148; DOI=10.1006/bbrc.1998.8979;
RA   Hatayama T., Yasuda K., Yasuda K.;
RT   "Association of HSP105 with HSC70 in high molecular mass complexes in
RT   mouse FM3A cells.";
RL   Biochem. Biophys. Res. Commun. 248:395-401(1998).
RN   [9]
RP   PHOSPHORYLATION.
RX   PubMed=10772927; DOI=10.1006/bbrc.2000.2541;
RA   Ishihara K., Yasuda K., Hatayama T.;
RT   "Phosphorylation of the 105-kDa heat shock proteins, HSP105alpha and
RT   HSP105beta, by casein kinase II.";
RL   Biochem. Biophys. Res. Commun. 270:927-931(2000).
RN   [10]
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=10865058; DOI=10.1016/S0006-8993(00)02346-5;
RA   Hylander B.L., Chen X., Graf P.C.F., Subjeck J.R.;
RT   "The distribution and localization of hsp110 in brain.";
RL   Brain Res. 869:49-55(2000).
RN   [11]
RP   PHOSPHORYLATION AT SER-509.
RX   PubMed=12558502; DOI=10.1042/BJ20021331;
RA   Ishihara K., Yamagishi N., Hatayama T.;
RT   "Protein kinase CK2 phosphorylates Hsp105 alpha at Ser509 and
RT   modulates its function.";
RL   Biochem. J. 371:917-925(2003).
RN   [12]
RP   FUNCTION.
RX   PubMed=14644449; DOI=10.1016/S0014-5793(03)01292-4;
RA   Yamagishi N., Ishihara K., Saito Y., Hatayama T.;
RT   "Hsp105 but not Hsp70 family proteins suppress the aggregation of
RT   heat-denatured protein in the presence of ADP.";
RL   FEBS Lett. 555:390-396(2003).
RN   [13]
RP   INTERACTION WITH HSPA8, AND FUNCTION.
RX   PubMed=15292236; DOI=10.1074/jbc.M407947200;
RA   Yamagishi N., Ishihara K., Hatayama T.;
RT   "Hsp105alpha suppresses Hsc70 chaperone activity by inhibiting Hsc70
RT   ATPase activity.";
RL   J. Biol. Chem. 279:41727-41733(2004).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-558, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [15]
RP   TISSUE SPECIFICITY.
RX   PubMed=16232202; DOI=10.1111/j.1349-7006.2005.00093.x;
RA   Miyazaki M., Nakatsura T., Yokomine K., Senju S., Monji M., Hosaka S.,
RA   Komori H., Yoshitake Y., Motomura Y., Minohara M., Kubo T.,
RA   Ishihara K., Hatayama T., Ogawa M., Nishimura Y.;
RT   "DNA vaccination of HSP105 leads to tumor rejection of colorectal
RT   cancer and melanoma in mice through activation of both CD4 T cells and
RT   CD8 T cells.";
RL   Cancer Sci. 96:695-705(2005).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-810, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-810, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-810, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Prevents the aggregation of denatured proteins in cells
CC       under severe stress, on which the ATP levels decrease markedly.
CC       Inhibits HSPA8/HSC70 ATPase and chaperone activities.
CC   -!- SUBUNIT: Interacts with HSPA8/HSC70.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Strictly
CC       cytoplasmic in neurons.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=HSP105-alpha;
CC         IsoId=Q61699-1; Sequence=Displayed;
CC       Name=HSP105-beta;
CC         IsoId=Q61699-2; Sequence=VSP_002429;
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis. Present at lower
CC       levels in most brain regions, except cerebellum. Within the brain,
CC       expression is restricted to neurons (at protein level).
CC       Overexpressed in cancer cells.
CC   -!- INDUCTION: By heat shock. Hsp105-alpha also induced by other
CC       stresses.
CC   -!- PTM: Phosphorylation on Ser-509 may be important for regulation of
CC       the HSPA8/HSC70 chaperone activity.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; L40406; AAA99485.1; -; mRNA.
DR   EMBL; D67016; BAA11035.1; -; mRNA.
DR   EMBL; D67017; BAA11036.1; -; mRNA.
DR   EMBL; AB005282; BAA74540.1; -; Genomic_DNA.
DR   EMBL; AK083179; BAC38797.1; -; mRNA.
DR   EMBL; AK146697; BAE27367.1; -; mRNA.
DR   EMBL; AK165046; BAE38016.1; -; mRNA.
DR   EMBL; BC018378; AAH18378.1; -; mRNA.
DR   EMBL; AK172913; BAD32191.1; -; mRNA.
DR   IPI; IPI00123802; -.
DR   IPI; IPI00224109; -.
DR   PIR; S66666; S66666.
DR   RefSeq; NP_038587.2; NM_013559.2.
DR   UniGene; Mm.270681; -.
DR   ProteinModelPortal; Q61699; -.
DR   SMR; Q61699; 1-651.
DR   DIP; DIP-32354N; -.
DR   IntAct; Q61699; 3.
DR   STRING; Q61699; -.
DR   PhosphoSite; Q61699; -.
DR   PRIDE; Q61699; -.
DR   Ensembl; ENSMUST00000074846; ENSMUSP00000074392; ENSMUSG00000029657.
DR   Ensembl; ENSMUST00000076410; ENSMUSP00000075746; ENSMUSG00000029657.
DR   Ensembl; ENSMUST00000110499; ENSMUSP00000106125; ENSMUSG00000029657.
DR   GeneID; 15505; -.
DR   KEGG; mmu:15505; -.
DR   UCSC; uc009apx.1; mouse.
DR   UCSC; uc009apz.1; mouse.
DR   CTD; 15505; -.
DR   MGI; MGI:105053; Hsph1.
DR   eggNOG; roNOG05689; -.
DR   GeneTree; ENSGT00390000016919; -.
DR   HOVERGEN; HBG047955; -.
DR   InParanoid; Q61699; -.
DR   OMA; MEQTQLK; -.
DR   OrthoDB; EOG4KD6KC; -.
DR   PhylomeDB; Q61699; -.
DR   NextBio; 288408; -.
DR   ArrayExpress; Q61699; -.
DR   Bgee; Q61699; -.
DR   CleanEx; MM_HSPH1; -.
DR   Genevestigator; Q61699; -.
DR   GermOnline; ENSMUSG00000029657; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0051085; P:chaperone mediated protein folding requiring cofactor; IDA:MGI.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR001023; Hsp70.
DR   InterPro; IPR013126; Hsp_70.
DR   PANTHER; PTHR19375; Hsp70; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   PROSITE; PS00297; HSP70_1; FALSE_NEG.
DR   PROSITE; PS00329; HSP70_2; FALSE_NEG.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm;
KW   Direct protein sequencing; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Stress response.
FT   CHAIN         1    858       Heat shock protein 105 kDa.
FT                                /FTId=PRO_0000078285.
FT   MOD_RES      31     31       Phosphoserine (By similarity).
FT   MOD_RES     384    384       Phosphoserine (By similarity).
FT   MOD_RES     509    509       Phosphoserine.
FT   MOD_RES     558    558       Phosphoserine.
FT   MOD_RES     701    701       Phosphothreonine (By similarity).
FT   MOD_RES     810    810       Phosphoserine.
FT   MOD_RES     816    816       Phosphothreonine (By similarity).
FT   VAR_SEQ     530    573       Missing (in isoform HSP105-beta).
FT                                /FTId=VSP_002429.
FT   CONFLICT      2      2       S -> L (in Ref. 4; BAC38797).
FT   CONFLICT      7      8       DV -> EL (in Ref. 1; AAA99485).
FT   CONFLICT      7      7       D -> N (in Ref. 4; BAC38797).
FT   CONFLICT     12     12       S -> R (in Ref. 4; BAC38797).
FT   CONFLICT     16     19       AVAR -> VGEG (in Ref. 4; BAC38797).
FT   CONFLICT     24     24       E -> D (in Ref. 4; BAC38797).
FT   CONFLICT     28     29       NE -> KD (in Ref. 4; BAC38797).
FT   CONFLICT    159    159       A -> R (in Ref. 1; AAA99485 and 2;
FT                                BAA11036).
FT   CONFLICT    310    310       C -> S (in Ref. 4; BAE38016).
FT   CONFLICT    320    320       P -> L (in Ref. 2; BAA11036).
FT   CONFLICT    373    373       A -> R (in Ref. 1; AAA99485).
FT   CONFLICT    518    518       P -> FQ (in Ref. 1; AAA99485).
FT   CONFLICT    658    658       I -> R (in Ref. 4; BAE27367).
FT   CONFLICT    744    744       I -> N (in Ref. 1; AAA99485).
FT   CONFLICT    838    838       A -> R (in Ref. 1; AAA99485).
SQ   SEQUENCE   858 AA;  96407 MW;  0576A4C2C4715032 CRC64;
     MSVVGLDVGS QSCYIAVARA GGIETIANEF SDRCTPSVIS FGSKNRTIGV AAKNQQITHA
     NNTVSSFKRF HGRAFNDPFI QKEKENLSYD LVPMKNGGVG IKVMYMDEEH FFSVEQITAM
     LLTKLKETAE NNLKKPVTDC VISVPSFFTD AERRSVLDAA QIVGLNCLRL MNDMTAVALN
     YGIYKQDLPN AEEKPRVVVF VDMGHSSFQV SACAFNKGKL KVLGTAFDPF LGGKNFDEKL
     VEHFCAEFKT KYKLDAKSKI RALLRLHQEC EKLKKLMSSN STDLPLNIEC FMNDKDVSGK
     MNRSQFEELC AELLQKIEVP LHSLMAQTQL KAEDVSAIEI VGGATRIPAV KERIAKFFGK
     DVSTTLNADE AVARGCALQC AILSPAFKVR EFSVTDAVPF PISLVWNHDS EETEGVHEVF
     SRNHAAPFSK VLTFLRRGPF ELEAFYSDPQ GVPYPEAKIG RFVVQNVSAQ KDGEKSRVKV
     KVRVNTHGIF TISTASMVEK VPTEEEDGSS LEADMECPNQ RPTESSDVDK NIQQDNSEAG
     TQPQVQTDGQ QTSQSPPSPE LTSEESKTPD ADKANEKKVD QPPEAKKPKI KVVNVELPVE
     ANLVWQLGRD LLNMYIETEG KMIMQDKLEK ERNDAKNAVE ECVYEFRDKL CGPYEKFICE
     QEHEKFLRLL TETEDWLYEE GEDQAKQAYI DKLEELMKMG TPVKVRFQEA EERPKVLEEL
     GQRLQHYAKI AADFRGKDEK YNHIDESEMK KVEKSVNEVM EWMNNVMNAQ AKRSLDQDPV
     VRTHEIRAKV KELNNVCEPV VTQPKPKIES PKLERTPNGP NIDKKEDLEG KNNLGAEAPH
     QNGECHPNEK GSVNMDLD
//
ID   ELAV4_MOUSE             Reviewed;         385 AA.
AC   Q61701; A2A9R7; O55010;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=ELAV-like protein 4;
DE   AltName: Full=Hu-antigen D;
DE            Short=HuD;
DE   AltName: Full=Paraneoplastic encephalomyelitis antigen HuD;
GN   Name=Elavl4; Synonyms=Hud;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=96051991; PubMed=8535975; DOI=10.1093/dnares/1.4.175;
RA   Abe R., Uyeno Y., Yamamoto K., Sakamoto H.;
RT   "Tissue-specific expression of the gene encoding a mouse RNA binding
RT   protein homologous to human HuD antigen.";
RL   DNA Res. 1:175-180(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=ICR;
RX   MEDLINE=98201607; PubMed=9524251; DOI=10.1016/S0378-1119(97)00615-X;
RA   Inman M.V., Levy S., Mock B.A., Owens G.C.;
RT   "Gene organization and chromosome location of the neural-specific RNA
RT   binding protein Elavl4.";
RL   Gene 208:139-145(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   IDENTIFICATION IN A MRNP COMPLEX WITH IGF2BP1 AND G3BP, AND
RP   INTERACTION WITH IGF2BP1.
RX   PubMed=15086518; DOI=10.1111/j.1471-4159.2004.02371.x;
RA   Atlas R., Behar L., Elliott E., Ginzburg I.;
RT   "The insulin-like growth factor mRNA binding-protein IMP-1 and the
RT   Ras-regulatory protein G3BP associate with tau mRNA and HuD protein in
RT   differentiated P19 neuronal cells.";
RL   J. Neurochem. 89:613-626(2004).
CC   -!- FUNCTION: May play a role in neuron-specific RNA processing.
CC       Protects CDKN1A mRNA from decay by binding to its 3'-UTR. Binds to
CC       AU-rich sequences (AREs) of target mRNAs, including VEGF and FOS
CC       mRNA (By similarity).
CC   -!- SUBUNIT: Component of a TAU mRNP complex, at least composed of
CC       IGF2BP1, ELAVL4 and G3BP.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1; Synonyms=Long;
CC         IsoId=Q61701-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short;
CC         IsoId=Q61701-2; Sequence=VSP_005792;
CC       Name=3;
CC         IsoId=Q61701-3; Sequence=Not described;
CC   -!- TISSUE SPECIFICITY: Expressed in brain and testis.
CC   -!- PTM: Methylation at Arg-248 by CARM1 weakens protective binding to
CC       the 3'-UTR of CDKN1A mRNA and down-regulates CDKN1A protein
CC       expression, thereby maintaining cells in a proliferative state.
CC       Methylation is inhibited by NGF, which facilitates neurite
CC       outgrowth (By similarity).
CC   -!- SIMILARITY: Belongs to the RRM elav family.
CC   -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.
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DR   EMBL; D31953; BAA06723.1; -; mRNA.
DR   EMBL; AF041341; AAC40080.1; -; mRNA.
DR   EMBL; AL627425; CAM19662.1; -; Genomic_DNA.
DR   IPI; IPI00229977; -.
DR   IPI; IPI00466120; -.
DR   PIR; JC2298; JC2298.
DR   RefSeq; NP_034618.2; NM_010488.4.
DR   UniGene; Mm.3970; -.
DR   ProteinModelPortal; Q61701; -.
DR   SMR; Q61701; 49-384.
DR   STRING; Q61701; -.
DR   PhosphoSite; Q61701; -.
DR   PRIDE; Q61701; -.
DR   Ensembl; ENSMUST00000106597; ENSMUSP00000102207; ENSMUSG00000028546.
DR   Ensembl; ENSMUST00000106603; ENSMUSP00000102214; ENSMUSG00000028546.
DR   GeneID; 15572; -.
DR   KEGG; mmu:15572; -.
DR   UCSC; uc008ucw.1; mouse.
DR   UCSC; uc008ucz.1; mouse.
DR   CTD; 15572; -.
DR   MGI; MGI:107427; Elavl4.
DR   GeneTree; ENSGT00560000077064; -.
DR   HOVERGEN; HBG002295; -.
DR   InParanoid; Q61701; -.
DR   OMA; SNSRNCP; -.
DR   OrthoDB; EOG4JHCFV; -.
DR   PhylomeDB; Q61701; -.
DR   NextBio; 288560; -.
DR   ArrayExpress; Q61701; -.
DR   Bgee; Q61701; -.
DR   Genevestigator; Q61701; -.
DR   GermOnline; ENSMUSG00000028546; Mus musculus.
DR   GO; GO:0017091; F:AU-rich element binding; ISS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   InterPro; IPR006548; ELAD_HUD_SF.
DR   InterPro; IPR002343; Hud_Sxl_RNA.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 3.
DR   Pfam; PF00076; RRM_1; 3.
DR   PRINTS; PR00961; HUDSXLRNA.
DR   SMART; SM00360; RRM; 3.
DR   TIGRFAMs; TIGR01661; ELAV_HUD_SF; 1.
DR   PROSITE; PS50102; RRM; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Methylation; Repeat; RNA-binding.
FT   CHAIN         1    385       ELAV-like protein 4.
FT                                /FTId=PRO_0000081584.
FT   DOMAIN       51    129       RRM 1.
FT   DOMAIN      137    217       RRM 2.
FT   DOMAIN      302    380       RRM 3.
FT   MOD_RES     248    248       Omega-N-methylated arginine; by CARM1 (By
FT                                similarity).
FT   VAR_SEQ     251    277       Missing (in isoform 2).
FT                                /FTId=VSP_005792.
SQ   SEQUENCE   385 AA;  42368 MW;  1EA9CDAB7E9BC683 CRC64;
     MEWNGLKMII STMEPQVSNG PTSNTSNGPS SNNRNCPSPM QTGAATDDSK TNLIVNYLPQ
     NMTQEEFRSL FGSIGEIESC KLVRDKITGQ SLGYGFVNYI DPKDAEKAIN TLNGLRLQTK
     TIKVSYARPS SASIRDANLY VSGLPKTMTQ KELEQLFSQY GRIITSRILV DQVTGVSRGV
     GFIRFDKRIE AEEAIKGLNG QKPSGATEPI TVKFANNPSQ KSSQALLSQL YQSPNRRYPG
     PLHHQAQRFR LDNLLNMAYG VKRLMSGPVP PSACPPRFSP ITIDGMTSLV GMNIPGHTGT
     GWCIFVYNLS PDSDESVLWQ LFGPFGAVNN VKVIRDFNTN KCKGFGFVTM TNYDEAAMAI
     ASLNGYRLGD RVLQVSFKTN KAHKS
//
ID   IL1AP_MOUSE             Reviewed;         570 AA.
AC   Q61730; Q8VCB9;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Interleukin-1 receptor accessory protein;
DE            Short=IL-1 receptor accessory protein;
DE            Short=IL-1RAcP;
DE   Flags: Precursor;
GN   Name=Il1rap;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH IL1R1,
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   TISSUE=Fibroblast;
RX   MEDLINE=95293970; PubMed=7775431; DOI=10.1074/jbc.270.23.13757;
RA   Greenfeder S.A., Nunes P., Kwee L., Labow M., Chizzonite R.A., Ju G.;
RT   "Molecular cloning and characterization of a second subunit of the
RT   interleukin 1 receptor complex.";
RL   J. Biol. Chem. 270:13757-13765(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH TOLLIP.
RX   MEDLINE=20313076; PubMed=10854325; DOI=10.1038/35014038;
RA   Burns K., Clatworthy J., Martin L., Martinon F., Plumpton C.,
RA   Maschera B., Lewis A., Ray K., Tschopp J., Volpe F.;
RT   "Tollip, a new component of the IL-1R1 pathway, links IRAK to the IL-1
RT   receptor.";
RL   Nat. Cell Biol. 2:346-351(2000).
RN   [5]
RP   MUTAGENESIS OF 527-LYS--PRO-534, INTERACTION WITH MYD88, AND FUNCTION.
RX   MEDLINE=21988196; PubMed=11880380; DOI=10.1074/jbc.M201000200;
RA   Radons J., Gabler S., Wesche H., Korherr C., Hofmeister R., Falk W.;
RT   "Identification of essential regions in the cytoplasmic tail of
RT   interleukin-1 receptor accessory protein critical for interleukin-1
RT   signaling.";
RL   J. Biol. Chem. 277:16456-16463(2002).
RN   [6]
RP   INTERACTION WITH IRAK2.
RX   MEDLINE=22546438; PubMed=12659850; DOI=10.1016/S0006-291X(03)00385-1;
RA   Boch J.A., Yoshida Y., Koyama Y., Wara-Aswapati N., Peng H., Unlu S.,
RA   Auron P.E.;
RT   "Characterization of a cascade of protein interactions initiated at
RT   the IL-1 receptor.";
RL   Biochem. Biophys. Res. Commun. 303:525-531(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-395 AND THR-398, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
CC   -!- FUNCTION: Mediates interleukin-1-dependent activation of NF-kappa-
CC       B. Isoform 1 is part of the membrane-bound form of the IL-1
CC       receptor. Signaling involves formation of a ternary complex
CC       containing IL1R1, TOLLIP, MYD88, and IRAK1 or IRAK2. Isoform 2
CC       modulates the response to interleukins by associating with soluble
CC       IL1R1 and enhancing interleukin-binding to the decoy receptor.
CC   -!- SUBUNIT: The signaling-competent complex is a heterodimer of IL1R2
CC       and IL1RAP bound to IL1B (By similarity).
CC   -!- INTERACTION:
CC       Q9QZ06:Tollip; NbExp=1; IntAct=EBI-525035, EBI-74272;
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
CC       membrane protein.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=MuIL-1R AcP;
CC         IsoId=Q61730-1; Sequence=Displayed;
CC       Name=2; Synonyms=SmuIL-1R AcP;
CC         IsoId=Q61730-2; Sequence=VSP_008054, VSP_008055;
CC   -!- TISSUE SPECIFICITY: Detected in lung, brain, spleen, thymus and
CC       liver.
CC   -!- SIMILARITY: Belongs to the interleukin-1 receptor family.
CC   -!- SIMILARITY: Contains 3 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SIMILARITY: Contains 1 TIR domain.
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DR   EMBL; X85999; CAA59991.1; -; mRNA.
DR   EMBL; AK039582; BAC30392.1; -; mRNA.
DR   EMBL; AK045686; BAC32457.1; -; mRNA.
DR   EMBL; BC021159; AAH21159.1; -; mRNA.
DR   IPI; IPI00113879; -.
DR   IPI; IPI00124823; -.
DR   PIR; A57535; A57535.
DR   RefSeq; NP_032390.1; NM_008364.2.
DR   RefSeq; NP_598864.1; NM_134103.2.
DR   UniGene; Mm.253424; -.
DR   ProteinModelPortal; Q61730; -.
DR   SMR; Q61730; 24-346, 403-548.
DR   DIP; DIP-296N; -.
DR   IntAct; Q61730; 4.
DR   STRING; Q61730; -.
DR   PhosphoSite; Q61730; -.
DR   PRIDE; Q61730; -.
DR   Ensembl; ENSMUST00000023156; ENSMUSP00000023156; ENSMUSG00000022514.
DR   Ensembl; ENSMUST00000096129; ENSMUSP00000093843; ENSMUSG00000022514.
DR   GeneID; 16180; -.
DR   KEGG; mmu:16180; -.
DR   UCSC; uc007yvd.1; mouse.
DR   UCSC; uc007yve.1; mouse.
DR   CTD; 16180; -.
DR   MGI; MGI:104975; Il1rap.
DR   GeneTree; ENSGT00570000079082; -.
DR   HOVERGEN; HBG104298; -.
DR   OMA; FFPSSVK; -.
DR   OrthoDB; EOG46MBJ6; -.
DR   PhylomeDB; Q61730; -.
DR   NextBio; 289053; -.
DR   ArrayExpress; Q61730; -.
DR   Bgee; Q61730; -.
DR   CleanEx; MM_IL1RAP; -.
DR   Genevestigator; Q61730; -.
DR   GermOnline; ENSMUSG00000022514; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004908; F:interleukin-1 receptor activity; IDA:MGI.
DR   GO; GO:0045087; P:innate immune response; IEA:InterPro.
DR   GO; GO:0042094; P:interleukin-2 biosynthetic process; IDA:MGI.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR015621; IL1-receptor.
DR   InterPro; IPR004075; IL1_rcpt_1.
DR   InterPro; IPR004074; IL1_rcpt_I/II.
DR   InterPro; IPR000157; Toll-Interleukin_rcpt.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3.
DR   PANTHER; PTHR11890; IL1-receptor; 1.
DR   Pfam; PF01582; TIR; 1.
DR   PRINTS; PR01536; INTRLKN1R12F.
DR   PRINTS; PR01537; INTRLKN1R1F.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00255; TIR; 1.
DR   SUPFAM; SSF52200; TIR; 1.
DR   PROSITE; PS50835; IG_LIKE; 2.
DR   PROSITE; PS50104; TIR; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Phosphoprotein; Receptor; Repeat;
KW   Secreted; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21    570       Interleukin-1 receptor accessory protein.
FT                                /FTId=PRO_0000015452.
FT   TOPO_DOM     21    367       Extracellular (Potential).
FT   TRANSMEM    368    388       Helical; (Potential).
FT   TOPO_DOM    389    570       Cytoplasmic (Potential).
FT   DOMAIN       21    128       Ig-like C2-type 1.
FT   DOMAIN      139    230       Ig-like C2-type 2.
FT   DOMAIN      243    348       Ig-like C2-type 3.
FT   DOMAIN      403    549       TIR.
FT   MOD_RES     395    395       Phosphothreonine.
FT   MOD_RES     398    398       Phosphothreonine.
FT   MOD_RES     555    555       Phosphoserine (By similarity).
FT   MOD_RES     556    556       Phosphoserine (By similarity).
FT   CARBOHYD     57     57       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    107    107       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    111    111       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    118    118       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    196    196       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    209    209       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    299    299       N-linked (GlcNAc...) (Potential).
FT   DISULFID     24    122       By similarity.
FT   DISULFID     47    114       By similarity.
FT   DISULFID    137    181       By similarity.
FT   DISULFID    160    212       By similarity.
FT   DISULFID    266    332       By similarity.
FT   VAR_SEQ     351    359       VIPPRYTVE -> GNGCTEPMTL (in isoform 2).
FT                                /FTId=VSP_008054.
FT   VAR_SEQ     360    570       Missing (in isoform 2).
FT                                /FTId=VSP_008055.
FT   MUTAGEN     527    534       KGEKSKYP->AAAAAAAA: Abolishes interaction
FT                                with MYD88 and IL-1-dependent activation
FT                                of NF-kappa-B.
SQ   SEQUENCE   570 AA;  65741 MW;  4D4B07E0310AFDC5 CRC64;
     MGLLWYLMSL SFYGILQSHA SERCDDWGLD TMRQIQVFED EPARIKCPLF EHFLKYNYST
     AHSSGLTLIW YWTRQDRDLE EPINFRLPEN RISKEKDVLW FRPTLLNDTG NYTCMLRNTT
     YCSKVAFPLE VVQKDSCFNS AMRFPVHKMY IEHGIHKITC PNVDGYFPSS VKPSVTWYKG
     CTEIVDFHNV LPEGMNLSFF IPLVSNNGNY TCVVTYPENG RLFHLTRTVT VKVVGSPKDA
     LPPQIYSPND RVVYEKEPGE ELVIPCKVYF SFIMDSHNEV WWTIDGKKPD DVTVDITINE
     SVSYSSTEDE TRTQILSIKK VTPEDLRRNY VCHARNTKGE AEQAAKVKQK VIPPRYTVEL
     ACGFGATVFL VVVLIVVYHV YWLEMVLFYR AHFGTDETIL DGKEYDIYVS YARNVEEEEF
     VLLTLRGVLE NEFGYKLCIF DRDSLPGGIV TDETLSFIQK SRRLLVVLSP NYVLQGTQAL
     LELKAGLENM ASRGNINVIL VQYKAVKDMK VKELKRAKTV LTVIKWKGEK SKYPQGRFWK
     QLQVAMPVKK SPRWSSNDKQ GLSYSSLKNV
//
ID   ITA6_MOUSE              Reviewed;        1091 AA.
AC   Q61739;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Integrin alpha-6;
DE   AltName: Full=CD49 antigen-like family member F;
DE   AltName: Full=VLA-6;
DE   AltName: CD_antigen=CD49f;
DE   Contains:
DE     RecName: Full=Integrin alpha-6 heavy chain;
DE   Contains:
DE     RecName: Full=Integrin alpha-6 light chain;
DE   Flags: Precursor;
GN   Name=Itga6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-6X1A AND ALPHA-6X1B).
RC   STRAIN=BALB/c; TISSUE=Mammary gland;
RX   MEDLINE=94363376; PubMed=8081870;
RA   Hierck B.P., Thorsteinsdottir S., Niessen C.M., Freund E.,
RA   van Iperen L., Feyen A., Hogervorst F., Poelmann R.E., Mummery C.L.,
RA   Sonnenberg A.;
RT   "Variants of the alpha 6 beta 1 laminin receptor in early murine
RT   development: distribution, molecular cloning and chromosomal
RT   localization of the mouse integrin alpha 6 subunit.";
RL   Cell Adhes. Commun. 1:33-53(1993).
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-284; ASN-927 AND ASN-958,
RP   AND MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Integrin alpha-6/beta-1 is a receptor for laminin on
CC       platelets. Integrin alpha-6/beta-4 is a receptor for laminin in
CC       epithelial cells and it plays a critical structural role in the
CC       hemidesmosome. Mice expressing a null mutation of the alpha-6
CC       subunit gene die soon after birth and develop severe blistering.
CC       The blisters are due to separation of the basal epithelial cells
CC       from a normally formed basement membrane.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha
CC       subunit is composed of an heavy and a light chain linked by a
CC       disulfide bond. Alpha-6 associates with either beta-1 or beta-4.
CC       Interacts with RAB21 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Alpha-6X1B;
CC         IsoId=Q61739-1; Sequence=Displayed;
CC       Name=Alpha-6X1A;
CC         IsoId=Q61739-2; Sequence=VSP_002726;
CC   -!- PTM: Isoforms containing segment A, but not segment B, are the
CC       major targets for PMA-induced phosphorylation. Phosphorylation
CC       occurs on 'Ser-1064' of isoform alpha-6X1A. Phosphorylation is not
CC       required for the induction of integrin alpha-6A/beta-1 high
CC       affinity but may reduce the affinity for ligand (By similarity).
CC   -!- SIMILARITY: Belongs to the integrin alpha chain family.
CC   -!- SIMILARITY: Contains 7 FG-GAP repeats.
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DR   EMBL; X69902; CAA49527.1; -; mRNA.
DR   IPI; IPI00227969; -.
DR   IPI; IPI00420835; -.
DR   PIR; A40463; A40463.
DR   UniGene; Mm.225096; -.
DR   ProteinModelPortal; Q61739; -.
DR   SMR; Q61739; 190-466, 560-588, 1009-1047.
DR   STRING; Q61739; -.
DR   PhosphoSite; Q61739; -.
DR   PRIDE; Q61739; -.
DR   Ensembl; ENSMUST00000028522; ENSMUSP00000028522; ENSMUSG00000027111.
DR   Ensembl; ENSMUST00000036783; ENSMUSP00000040155; ENSMUSG00000027111.
DR   Ensembl; ENSMUST00000112101; ENSMUSP00000107729; ENSMUSG00000027111.
DR   MGI; MGI:96605; Itga6.
DR   HOVERGEN; HBG108011; -.
DR   InParanoid; Q61739; -.
DR   OrthoDB; EOG4G4GPM; -.
DR   ArrayExpress; Q61739; -.
DR   Bgee; Q61739; -.
DR   CleanEx; MM_ITGA6; -.
DR   Genevestigator; Q61739; -.
DR   GermOnline; ENSMUSG00000027111; Mus musculus.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0008305; C:integrin complex; IDA:MGI.
DR   GO; GO:0005178; F:integrin binding; IPI:MGI.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:MGI.
DR   GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
DR   GO; GO:0031668; P:cellular response to extracellular stimulus; IDA:MGI.
DR   GO; GO:0046847; P:filopodium assembly; IMP:MGI.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0050900; P:leukocyte migration; IMP:MGI.
DR   GO; GO:0042475; P:odontogenesis of dentine-containing tooth; IMP:MGI.
DR   GO; GO:0022409; P:positive regulation of cell-cell adhesion; IDA:MGI.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR013519; Int_alpha_beta-p.
DR   InterPro; IPR000413; Integrin_alpha.
DR   InterPro; IPR013649; Integrin_alpha-2.
DR   InterPro; IPR018184; Integrin_alpha_C_CS.
DR   Pfam; PF01839; FG-GAP; 2.
DR   Pfam; PF08441; Integrin_alpha2; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   SMART; SM00191; Int_alpha; 5.
DR   PROSITE; PS51470; FG_GAP; 7.
DR   PROSITE; PS00242; INTEGRIN_ALPHA; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell adhesion;
KW   Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW   Integrin; Membrane; Phosphoprotein; Receptor; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     23       By similarity.
FT   CHAIN        24   1091       Integrin alpha-6.
FT                                /FTId=PRO_0000016261.
FT   CHAIN        24    899       Integrin alpha-6 heavy chain (Potential).
FT                                /FTId=PRO_0000016262.
FT   CHAIN       903   1091       Integrin alpha-6 light chain (Potential).
FT                                /FTId=PRO_0000016263.
FT   TOPO_DOM     24   1011       Extracellular (Potential).
FT   TRANSMEM   1012   1037       Helical; (Potential).
FT   TOPO_DOM   1038   1091       Cytoplasmic (Potential).
FT   REPEAT       30     95       FG-GAP 1.
FT   REPEAT      101    166       FG-GAP 2.
FT   REPEAT      176    229       FG-GAP 3.
FT   REPEAT      244    301       FG-GAP 4.
FT   REPEAT      302    363       FG-GAP 5.
FT   REPEAT      364    419       FG-GAP 6.
FT   REPEAT      420    479       FG-GAP 7.
FT   CA_BIND     324    332       Potential.
FT   CA_BIND     386    394       Potential.
FT   CA_BIND     441    449       Potential.
FT   MOTIF      1040   1044       GFFKR motif.
FT   CARBOHYD     78     78       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    223    223       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    284    284       N-linked (GlcNAc...).
FT   CARBOHYD    370    370       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    731    731       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    746    746       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    927    927       N-linked (GlcNAc...).
FT   CARBOHYD    958    958       N-linked (GlcNAc...).
FT   DISULFID     86     94       By similarity.
FT   DISULFID    131    154       By similarity.
FT   DISULFID    175    188       By similarity.
FT   DISULFID    489    496       By similarity.
FT   DISULFID    502    562       By similarity.
FT   DISULFID    626    632       By similarity.
FT   DISULFID    726    737       By similarity.
FT   DISULFID    881    928       Interchain (between heavy and light
FT                                chains) (By similarity).
FT   DISULFID    934    939       By similarity.
FT   VAR_SEQ    1045   1091       SRYDDSIPRYHAVRIRKEEREIKDEKHMDNLEKKQWITKWN
FT                                ENESYS -> NKKDHYDATYHKAEIHTQPSDKERLTSDA
FT                                (in isoform Alpha-6X1A).
FT                                /FTId=VSP_002726.
SQ   SEQUENCE   1091 AA;  122148 MW;  D8C96C8BDB67140D CRC64;
     MAVAGQLCLL YLSAGLLARL GTAFNLDTRE DNVIRKSGDP GSLFGFSLAM HWQLQPEDKR
     LLLVGAPRAE ALPLQRANRT GGLYSCDITS RGPCTRIEFD NDADPMSESK EDQWMGVTVQ
     SQGPGGKVVT CAHRYEKRQH VNTKQESRDI FGRCYVLSQN LRIEDDMDGG DWSFCDGRLR
     GHEKFGSCQQ GVAATFTKDF HYIVFGAPGT YNWKGIVRVE QKNNTFFDMN IFEDGPYEVG
     GETDHDESLV PVPANSYLGF SLDSGKGIVS KDDITFVSGA PRANHSGAVV LLKRDMKSAH
     LLPEYIFDGE GLASSFGYDV AVVDLNADGW QDIVIGAPQY FDRDGEVGGA VYVYINQQGK
     WSNVKPIRLN GTKDSMFGIS VKNIGDINQD GYPDIAVGAP YDDLGKVFIY HGSPTGIITK
     PTQVLEGTSP YFGYSIAGNM DLDRNSYPDL AVGSLSDSVT IFRSRPVINI LKTITVTPNR
     IDLRQKSMCG SPSGICLKVK ACFEYTAKPS GYNPPISILG ILEAEKERRK SGLSSRVQFR
     NQGSEPKYTQ ELTLNRQKQR ACMEETLWLQ ENIRDKLRPI PITASVEIQE PTSRRRVNSL
     PEVLPILNSN EAKTVQTDVH FLKEGCGDDN VCNSNLKLEY KFGTREGNQD KFSYLPIQKG
     IPELVLKDQK DIALEITVTN SPSDPRNPRK DGDDAHEAKL IATFPDTLTY SAYRELRAFP
     EKQLSCVANQ NGSQADCELG NPFKRNSSVT FYLILSTTEV TFDTTDLDIN LKLETTSNQD
     KLAPITAKAK VVIELLLSLS GVAKPSQVYF GGTVVGEQAM KSEDEVGSLI EYEFRVINLG
     KPLKNLGTAT LNIQWPKEIS NGKWLLYLMK VESKGLEQIV CEPHNEINYL KLKESHNSRK
     KRELPEKQID DSRKFSLFPE RKYQTLNCSV NVRCVNIRCP LRGLDTKASL VLCSRLWNST
     FLEEYSKLNY LDILVRASID VTAAAQNIKL PHAGTQVRVT VFPSKTVAQY SGVAWWIILL
     AVLAGILMLA LLVFLLWKCG FFKRSRYDDS IPRYHAVRIR KEEREIKDEK HMDNLEKKQW
     ITKWNENESY S
//
ID   IRK11_MOUSE             Reviewed;         390 AA.
AC   Q61743; Q9QX21;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=ATP-sensitive inward rectifier potassium channel 11;
DE   AltName: Full=Inward rectifier K(+) channel Kir6.2;
DE   AltName: Full=Potassium channel, inwardly rectifying subfamily J member 11;
GN   Name=Kcnj11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Pancreatic islet;
RX   MEDLINE=96072967; PubMed=7502040; DOI=10.1126/science.270.5239.1166;
RA   Inagaki N., Gonoi T., Clement J.P. IV, Namba N., Inazawa J.,
RA   Gonzalez G., Aguilar-Bryan L., Seino S., Bryan J.;
RT   "Reconstitution of IKATP: an inward rectifier subunit plus the
RT   sulfonylurea receptor.";
RL   Science 270:1166-1170(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Pancreatic islet;
RX   MEDLINE=96140543; PubMed=8549751; DOI=10.1016/0014-5793(95)01369-5;
RA   Sakura H., Aemmaelae C., Smith P.A., Gribble F.M., Ashcroft F.M.;
RT   "Cloning and functional expression of the cDNA encoding a novel ATP-
RT   sensitive potassium channel subunit expressed in pancreatic beta-
RT   cells, brain, heart and skeletal muscle.";
RL   FEBS Lett. 377:338-344(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Ola;
RA   Kooptiwut S., Shelton K.D., Magnuson M.A.;
RT   "Structural characterization of the mouse sulfonylurea receptor-1 and
RT   potassium inward rectifier 6.2 genes.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: This receptor is controlled by G proteins. Inward
CC       rectifier potassium channels are characterized by a greater
CC       tendency to allow potassium to flow into the cell rather than out
CC       of it. Their voltage dependence is regulated by the concentration
CC       of extracellular potassium; as external potassium is raised, the
CC       voltage range of the channel opening shifts to more positive
CC       voltages. The inward rectification is mainly due to the blockage
CC       of outward current by internal magnesium. Can be blocked by
CC       extracellular barium (By similarity).
CC   -!- SUBUNIT: Interacts with ABCC8/SUR.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
CC       (TC 1.A.2.1) family. KCNJ11 subfamily.
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DR   EMBL; D50581; BAA09130.1; -; mRNA.
DR   EMBL; U73626; AAB17355.1; -; mRNA.
DR   EMBL; AF037313; AAD02096.1; -; Genomic_DNA.
DR   EMBL; BC052731; AAH52731.1; -; mRNA.
DR   EMBL; BC057006; AAH57006.1; -; mRNA.
DR   IPI; IPI00124866; -.
DR   PIR; S68403; S68403.
DR   RefSeq; NP_034732.1; NM_010602.2.
DR   UniGene; Mm.333863; -.
DR   ProteinModelPortal; Q61743; -.
DR   SMR; Q61743; 33-358.
DR   MINT; MINT-2982880; -.
DR   STRING; Q61743; -.
DR   PhosphoSite; Q61743; -.
DR   PRIDE; Q61743; -.
DR   Ensembl; ENSMUST00000094412; ENSMUSP00000091979; ENSMUSG00000070561.
DR   GeneID; 16514; -.
DR   KEGG; mmu:16514; -.
DR   UCSC; uc009gyc.1; mouse.
DR   CTD; 16514; -.
DR   MGI; MGI:107501; Kcnj11.
DR   eggNOG; roNOG11806; -.
DR   HOGENOM; HBG716702; -.
DR   HOVERGEN; HBG006178; -.
DR   InParanoid; Q61743; -.
DR   OMA; LIFTMSF; -.
DR   OrthoDB; EOG4DFPNM; -.
DR   NextBio; 289865; -.
DR   ArrayExpress; Q61743; -.
DR   Bgee; Q61743; -.
DR   Genevestigator; Q61743; -.
DR   GermOnline; ENSMUSG00000070561; Mus musculus.
DR   GO; GO:0008282; C:ATP-sensitive potassium channel complex; IDA:BHF-UCL.
DR   GO; GO:0005524; F:ATP binding; IDA:BHF-UCL.
DR   GO; GO:0015272; F:ATP-activated inward rectifier potassium channel activity; IDA:BHF-UCL.
DR   GO; GO:0030955; F:potassium ion binding; IC:BHF-UCL.
DR   GO; GO:0010107; P:potassium ion import; IDA:BHF-UCL.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR016449; K_chnl_inward-rec_Kir.
DR   InterPro; IPR001838; K_chnl_inward-rec_Kir-like.
DR   InterPro; IPR003279; K_chnl_inward-rec_Kir6.2.
DR   InterPro; IPR013521; K_chnl_inward-rec_Kir_Cr2.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   Gene3D; G3DSA:2.60.40.1400; IR_K+channel_cytopl; 1.
DR   PANTHER; PTHR11767; K+channel_IR; 1.
DR   Pfam; PF01007; IRK; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01332; KIR62CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; Ig_E-set; 1.
PE   2: Evidence at transcript level;
KW   Ion transport; Ionic channel; Membrane; Potassium;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN         1    390       ATP-sensitive inward rectifier potassium
FT                                channel 11.
FT                                /FTId=PRO_0000154958.
FT   TOPO_DOM      1     68       Cytoplasmic (By similarity).
FT   TRANSMEM     69     93       Helical; Name=M1; (By similarity).
FT   TOPO_DOM     94    116       Extracellular (By similarity).
FT   INTRAMEM    117    128       Helical; Pore-forming; Name=H5; (By
FT                                similarity).
FT   INTRAMEM    129    135       Pore-forming; (By similarity).
FT   TOPO_DOM    136    144       Extracellular (By similarity).
FT   TRANSMEM    145    166       Helical; Name=M2; (By similarity).
FT   TOPO_DOM    167    390       Cytoplasmic (By similarity).
FT   MOTIF       130    135       Selectivity filter (By similarity).
FT   SITE        160    160       Role in the control of polyamine-mediated
FT                                channel gating and in the blocking by
FT                                intracellular magnesium (By similarity).
FT   CONFLICT    248    248       G -> S (in Ref. 3; AAD02096).
SQ   SEQUENCE   390 AA;  43562 MW;  6AFBFFD284C92C3A CRC64;
     MLSRKGIIPE EYVLTRLAED PAEPRYRTRE RRARFVSKKG NCNVAHKNIR EQGRFLQDVF
     TTLVDLKWPH TLLIFTMSFL CSWLLFAMVW WLIAFAHGDL APGEGTNVPC VTSIHSFSSA
     FLFSIEVQVT IGFGGRMVTE ECPLAILILI VQNIVGLMIN AIMLGCIFMK TAQAHRRAET
     LIFSKHAVIT LRHGRLCFML RVGDLRKSMI ISATIHMQVV RKTTSPEGEV VPLHQVDIPM
     ENGVGGNGIF LVAPLIIYHV IDSNSPLYDL APSDLHHHQD LEIIVILEGV VETTGITTQA
     RTSYLADEIL WGQRFVPIVA EEDGRYSVDY SKFGNTIKVP TPLCTARQLD EDRSLLDALT
     LASSRGPLRK RSVAVAKAKP KFSISPDSLS
//
ID   KCNA5_MOUSE             Reviewed;         602 AA.
AC   Q61762;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Potassium voltage-gated channel subfamily A member 5;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv1.5;
DE            Short=KV1-5;
GN   Name=Kcna5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=Swiss; TISSUE=Heart;
RX   MEDLINE=94043264; PubMed=8226976;
RA   Attali B., Lesage F., Ziliani P., Guillemare E., Honore E.,
RA   Waldmann R., Hugnot J.-P., Mattei M.-G., Lazdunski M., Barhanin J.;
RT   "Multiple mRNA isoforms encoding the mouse cardiac Kv1-5 delayed
RT   rectifier K+ channel.";
RL   J. Biol. Chem. 268:24283-24289(1993).
CC   -!- FUNCTION: Mediates the voltage-dependent potassium ion
CC       permeability of excitable membranes. Assuming opened or closed
CC       conformations in response to the voltage difference across the
CC       membrane, the protein forms a potassium-selective channel through
CC       which potassium ions may pass in accordance with their
CC       electrochemical gradient. This channel displays rapid activation
CC       and slow inactivation.
CC   -!- SUBUNIT: Heterotetramer of potassium channel proteins. Interacts
CC       with DLG1, which enhances channel currents. Forms a ternary
CC       complex with DLG1 and CAV3 (By similarity). Interacts with UBE2I
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q61762-1; Sequence=Displayed;
CC       Name=2; Synonyms=5';
CC         IsoId=Q61762-2; Sequence=VSP_000961;
CC       Name=3; Synonyms=3';
CC         IsoId=Q61762-3; Sequence=VSP_000962;
CC         Note=Inactive. Inhibits expression of isoform 1 and isoform 2;
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart and moderately in
CC       brain. Low levels in thymus, skeletal muscle and spleen. Not
CC       expressed in liver, lung or kidney.
CC   -!- DOMAIN: The amino terminus may be important in determining the
CC       rate of inactivation of the channel while the C-terminal PDZ-
CC       binding motif may play a role in modulation of channel activity
CC       and/or targeting of the channel to specific subcellular
CC       compartments (By similarity).
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position.
CC   -!- SIMILARITY: Belongs to the potassium channel family. A (Shaker)
CC       (TC 1.A.1.2) subfamily. Kv1.5/KCNA5 sub-subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; L22218; AAA39365.1; -; mRNA.
DR   IPI; IPI00124939; -.
DR   IPI; IPI00222003; -.
DR   IPI; IPI00222004; -.
DR   PIR; A49507; A49507.
DR   UniGene; Mm.222831; -.
DR   ProteinModelPortal; Q61762; -.
DR   SMR; Q61762; 111-516.
DR   STRING; Q61762; -.
DR   PhosphoSite; Q61762; -.
DR   PRIDE; Q61762; -.
DR   Ensembl; ENSMUST00000060972; ENSMUSP00000055673; ENSMUSG00000045534.
DR   MGI; MGI:96662; Kcna5.
DR   eggNOG; roNOG13161; -.
DR   HOGENOM; HBG445693; -.
DR   HOVERGEN; HBG052230; -.
DR   InParanoid; Q61762; -.
DR   OrthoDB; EOG4R502V; -.
DR   ArrayExpress; Q61762; -.
DR   Bgee; Q61762; -.
DR   Genevestigator; Q61762; -.
DR   GermOnline; ENSMUSG00000045534; Mus musculus.
DR   GO; GO:0019870; F:potassium channel inhibitor activity; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0043267; P:negative regulation of potassium ion transport; IDA:MGI.
DR   GO; GO:0042391; P:regulation of membrane potential; IGI:MGI.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003972; K_chnl_volt-dep_Kv1.
DR   InterPro; IPR004052; K_chnl_volt-dep_Kv1.5.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   PANTHER; PTHR11537:SF25; KV15channel; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01512; KV15CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01496; SHAKERCHANEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Ion transport; Ionic channel;
KW   Isopeptide bond; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Potassium; Potassium channel; Potassium transport; Transmembrane;
KW   Transmembrane helix; Transport; Ubl conjugation;
KW   Voltage-gated channel.
FT   CHAIN         1    602       Potassium voltage-gated channel subfamily
FT                                A member 5.
FT                                /FTId=PRO_0000053986.
FT   TRANSMEM    242    260       Helical; Name=Segment S1; (Potential).
FT   TRANSMEM    316    336       Helical; Name=Segment S2; (Potential).
FT   TRANSMEM    347    368       Helical; Name=Segment S3; (Potential).
FT   TRANSMEM    387    408       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TRANSMEM    423    444       Helical; Name=Segment S5; (Potential).
FT   TRANSMEM    484    505       Helical; Name=Segment S6; (Potential).
FT   MOTIF       469    474       Selectivity filter (By similarity).
FT   MOTIF       600    602       PDZ-binding.
FT   COMPBIAS    373    376       Poly-Gly.
FT   MOD_RES      81     81       Phosphoserine; by CK2 and PKA
FT                                (Potential).
FT   MOD_RES     403    403       Phosphoserine (By similarity).
FT   MOD_RES     535    535       Phosphoserine; by PKA (Potential).
FT   MOD_RES     546    546       Phosphoserine; by PKA (Potential).
FT   MOD_RES     569    569       Phosphoserine; by PKA (Potential).
FT   LIPID       337    337       S-palmitoyl cysteine (Potential).
FT   CARBOHYD     10     10       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     44     44       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    116    116       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    181    181       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    290    290       N-linked (GlcNAc...) (Potential).
FT   CROSSLNK    212    212       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    525    525       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   VAR_SEQ       1    200       Missing (in isoform 2).
FT                                /FTId=VSP_000961.
FT   VAR_SEQ     515    602       Missing (in isoform 3).
FT                                /FTId=VSP_000962.
SQ   SEQUENCE   602 AA;  66645 MW;  FC2C92E8062FAC97 CRC64;
     MEISLVPTEN GSAMTLRGGG EAVASCVQSP RGECGCPPTA GLNNQSKETS PRRRATHEDA
     AQGGRPLPPM PQELPQPRRP SAEDEEGEGD PGLGTVEEDQ APQDSGSLHH QRVLINISGL
     RFETQLDTLV QFPNNLLGDP VKRLRYFDPL RNEYFFDRNR PSFDGILYYY QSGGRLRRPV
     NVSLDVFADE IRFYQLGDEA MERFREDEGF IKEEEKPLPR NEFQRQVWLI FEYPESSGSA
     RAIAIVSVSV ILISIITFCL ETLPEFRVDR ELLLHPPVPP QPPAPAPGTN ASGSGVLSSG
     TTVAPLLPRT LADPFFIVET TCVIWFTFEL LVRFFACPSK AEFSRNIMNI IDIVAIFPYF
     ITLGTELAEQ QPGGGGQNGQ QAMSLAILRV IRLVRVFRIF KLSRHSKGLQ ILGKTLQASM
     RELGLLIFFL FIGVILFSSA VYFAEADNQG SQLSSIPDAF WWAVVTMTTV GYGDMRPITV
     GGKIVGSLCA IAGVLTIALP VPVIVSNFNY FYHRETDHEE QAALKEEQGI QRRESGLDTG
     GQRKVSCSKA SFHKTGGPLE STDSIRRGSC PLEKCHLKAK SNVDLRRSLY ALCLDTSRET
     DL
//
ID   Q61764_MOUSE            Unreviewed;       270 AA.
AC   Q61764;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   SubName: Full=Keratin;
DE   Flags: Fragment;
GN   Name=Krt2; Synonyms=Krt2-17;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NMRI; TISSUE=Foot pad epidermis;
RX   MEDLINE=88112584; PubMed=2448177;
RX   DOI=10.1111/j.1432-0436.1987.tb00066.x;
RA   Rentrop M., Nischt R., Knapp B., Schweizer J., Winter H.;
RT   "An unusual type-II 70-kilodalton keratin protein of mouse epidermis
RT   exhibiting postnatal body-site specificity and sensitivity to
RT   hyperproliferation.";
RL   Differentiation 34:189-200(1987).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
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DR   EMBL; M24151; AAA39370.1; -; mRNA.
DR   IPI; IPI00463282; -.
DR   PIR; A60830; A60830.
DR   UniGene; Mm.358616; -.
DR   HSSP; P08670; 1GK4.
DR   ProteinModelPortal; Q61764; -.
DR   STRING; Q61764; -.
DR   PRIDE; Q61764; -.
DR   Ensembl; ENSMUST00000052664; ENSMUSP00000051114; ENSMUSG00000064201.
DR   MGI; MGI:96699; Krt2.
DR   GeneTree; ENSGT00550000074491; -.
DR   ArrayExpress; Q61764; -.
DR   Bgee; Q61764; -.
DR   Genevestigator; Q61764; -.
DR   GO; GO:0045095; C:keratin filament; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR016044; F.
DR   InterPro; IPR001664; IF.
DR   InterPro; IPR018039; Intermediate_filament_CS.
DR   InterPro; IPR003054; Keratin_II.
DR   PANTHER; PTHR23239; IF; 1.
DR   PANTHER; PTHR23239:SF18; Keratin_II; 1.
DR   Pfam; PF00038; Filament; 1.
DR   PROSITE; PS00226; IF; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Intermediate filament.
FT   NON_TER       1      1
SQ   SEQUENCE   270 AA;  25287 MW;  9605C698CF2CB8C1 CRC64;
     EVVKKQCIGV QDSIADAEQH GEHAIKDARG KLTDLEEALQ QCREDLARLL RDYQELMNTK
     LSLDVEIATY RKLLEGEECR MSGDFSDNVS VSITSSTISS SMASKTGFGS GGQSSGGRGS
     YGGRGGGGGG GSSYGSGGRS SGSRGSGSGS GGGGYSSGGG SRGGSGGGYG SGGGSRGGSG
     GGYGSGGGSG SGGGYSSGGG SRGGSGGGGA SSGGGSRGGS SSGGGSRGGS SSGGGGYSSG
     GGSRGGSSSG GQDLALKREV LGQGKVVAQV
//
ID   KIF3B_MOUSE             Reviewed;         747 AA.
AC   Q61771;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Kinesin-like protein KIF3B;
DE   AltName: Full=Microtubule plus end-directed kinesin motor 3B;
GN   Name=Kif3b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=96032268; PubMed=7559760; DOI=10.1083/jcb.130.6.1387;
RA   Yamazaki H., Nakata T., Okada Y., Hirokawa N.;
RT   "KIF3A/B: a heterodimeric kinesin superfamily protein that works as a
RT   microtubule plus end-directed motor for membrane organelle
RT   transport.";
RL   J. Cell Biol. 130:1387-1399(1995).
RN   [2]
RP   INTERACTION WITH IFT20.
RX   PubMed=12821668; DOI=10.1074/jbc.M300156200;
RA   Baker S.A., Freeman K., Luby-Phelps K., Pazour G.J., Besharse J.C.;
RT   "IFT20 links kinesin II with a mammalian intraflagellar transport
RT   complex that is conserved in motile flagella and sensory cilia.";
RL   J. Biol. Chem. 278:34211-34218(2003).
CC   -!- FUNCTION: Involved in tethering the chromosomes to the spindle
CC       pole and in chromosome movement. Microtubule-based anterograde
CC       translocator for membranous organelles. Plus end-directed
CC       microtubule sliding activity in vitro (By similarity).
CC   -!- SUBUNIT: Interacts with the SMC3 subunit of the cohesin complex
CC       (By similarity). Heterodimer of KIF3A and KIF3B. Interacts
CC       directly with IFT20.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (Probable).
CC   -!- SIMILARITY: Belongs to the kinesin-like protein family. Kinesin II
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 kinesin-motor domain.
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DR   EMBL; D26077; BAA05070.1; -; mRNA.
DR   IPI; IPI00465809; -.
DR   PIR; A57107; A57107.
DR   RefSeq; NP_032470.3; NM_008444.4.
DR   UniGene; Mm.315560; -.
DR   ProteinModelPortal; Q61771; -.
DR   SMR; Q61771; 7-358.
DR   STRING; Q61771; -.
DR   PhosphoSite; Q61771; -.
DR   PRIDE; Q61771; -.
DR   Ensembl; ENSMUST00000028977; ENSMUSP00000028977; ENSMUSG00000027475.
DR   GeneID; 16569; -.
DR   KEGG; mmu:16569; -.
DR   CTD; 16569; -.
DR   MGI; MGI:107688; Kif3b.
DR   HOVERGEN; HBG052255; -.
DR   InParanoid; Q61771; -.
DR   OMA; KDQSKRL; -.
DR   OrthoDB; EOG4J3WGM; -.
DR   PhylomeDB; Q61771; -.
DR   ArrayExpress; Q61771; -.
DR   Bgee; Q61771; -.
DR   CleanEx; MM_KIF3B; -.
DR   Genevestigator; Q61771; -.
DR   GermOnline; ENSMUSG00000027475; Mus musculus.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   Gene3D; G3DSA:3.40.850.10; kinesin_motor; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_DOMAIN1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_DOMAIN2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW   Motor protein; Nucleotide-binding.
FT   CHAIN         1    747       Kinesin-like protein KIF3B.
FT                                /FTId=PRO_0000125396.
FT   DOMAIN        1    345       Kinesin-motor.
FT   NP_BIND      96    103       ATP (By similarity).
FT   REGION      580    747       Globular.
FT   COILED      346    579       Potential.
FT   COMPBIAS    386    393       Poly-Gly.
FT   COMPBIAS    394    405       Poly-Glu.
FT   COMPBIAS    723    730       Poly-Ser.
SQ   SEQUENCE   747 AA;  85288 MW;  FA369A4190EC8B47 CRC64;
     MSKLKSSESV RVVVRCRPMN GKEKAASYDK VVDVDVKLGQ VSVKNPKGTS HEMPKTFTFD
     AVYDWNAKQF ELYDETFRPL VDSVLQGFNG TIFAYGQTGT GKTYTMEGVR GDPEKRGVIP
     NSFDHIFTHI SRSQNQQYLV RASYLEIYQE EIRDLLSKDQ TKRLELKERP DTGVYVKDLS
     SFVTKSVKEI EHVMNVGNQN RSVGATNMNE HSSRSHAIFV ITIECSEVGL DGENHIRVGK
     LNLVDLAGSE RQAKTGAQGE RLKEATKINL SLSALGNVIS ALVDGKSTHI PYRDSKLTRL
     LQDSLGGNAK TVMVANVGPA SYNVEETLTT LRYANRAKNI KNKPRVNEDP KDALLREFQE
     EIARLKAQLE KRSIGRRKRR EKRREGGGSG GGGEEEEEEG EEGEEDGDDK DDYWREQQEK
     LEIEKRAIVE DHSLVAEEKM RLLKEKEKKM EDLRREKDAA EMLGAKIKAM ESKLLVGGKN
     IVDHTNEQQK ILEQKRQEIA EQKRREREIQ QQMESRDEET LELKETYTSL QQEVDIKTKK
     LKKLFSKLQA VKAEIHDLQE EHIKERQELE QTQNELTREL KLKHLIIENF IPLEEKNKIM
     NRSFFDDEED HWKLHPITRL ENQQMMKRPV SAVGYKRPLS QHARMSMMIR PEPRYRAENI
     MLLELDMPSR TTRDYEGPAI SPKVQAALDA ALQDEDEIQV DASSFESTAS RKPKARPKSG
     RKSGSSSSSS GNPASQFYPQ SRGLVPK
//
ID   LASP1_MOUSE             Reviewed;         263 AA.
AC   Q61792; Q62416;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=LIM and SH3 domain protein 1;
DE            Short=LASP-1;
DE   AltName: Full=Metastatic lymph node gene 50 protein;
DE            Short=MLN 50;
GN   Name=Lasp1; Synonyms=Mln50;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98172750; PubMed=9511759; DOI=10.1016/S0378-1119(97)00622-7;
RA   Schreiber V., Masson R., Linares J.L., Mattei M.-G., Tomasetto C.,
RA   Rio M.-C.;
RT   "Chromosomal assignment and expression pattern of the murine Lasp-1
RT   gene.";
RL   Gene 207:171-175(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 59-263.
RX   MEDLINE=98294438; PubMed=9630982; DOI=10.1038/nbt0696-741;
RA   Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.;
RT   "Cloning of ligand targets: systematic isolation of SH3 domain-
RT   containing proteins.";
RL   Nat. Biotechnol. 14:741-744(1996).
RN   [5]
RP   PHOSPHORYLATION AT THR-156.
RX   PubMed=15465019; DOI=10.1016/j.bbrc.2004.08.235;
RA   Keicher C., Gambaryan S., Schulze E., Marcus K., Meyer H.E., Butt E.;
RT   "Phosphorylation of mouse LASP-1 on threonine 156 by cAMP- and cGMP-
RT   dependent protein kinase.";
RL   Biochem. Biophys. Res. Commun. 324:308-316(2004).
CC   -!- FUNCTION: Plays an important role in the regulation of dynamic
CC       actin-based, cytoskeletal activities. Agonist-dependent changes in
CC       LASP1 phosphorylation may also serve to regulate actin-associated
CC       ion transport activities, not only in the parietal cell but also
CC       in certain other F-actin-rich secretory epithelial cell types (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with F-actin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex (By similarity).
CC       Cytoplasm, cytoskeleton (By similarity). Note=Associated with the
CC       F-actin rich cortical cytoskeleton (By similarity).
CC   -!- SIMILARITY: Contains 1 LIM zinc-binding domain.
CC   -!- SIMILARITY: Contains 2 nebulin repeats.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; X96973; CAA65659.1; -; mRNA.
DR   EMBL; AK078445; BAC37278.1; -; mRNA.
DR   EMBL; BC010840; AAH10840.1; -; mRNA.
DR   EMBL; U58882; AAC52639.1; -; mRNA.
DR   IPI; IPI00125091; -.
DR   RefSeq; NP_034818.1; NM_010688.4.
DR   UniGene; Mm.271967; -.
DR   ProteinModelPortal; Q61792; -.
DR   SMR; Q61792; 1-59, 207-263.
DR   STRING; Q61792; -.
DR   PhosphoSite; Q61792; -.
DR   PRIDE; Q61792; -.
DR   Ensembl; ENSMUST00000043843; ENSMUSP00000042123; ENSMUSG00000038366.
DR   GeneID; 16796; -.
DR   KEGG; mmu:16796; -.
DR   UCSC; uc007lew.1; mouse.
DR   CTD; 16796; -.
DR   MGI; MGI:109656; Lasp1.
DR   GeneTree; ENSGT00530000062924; -.
DR   HOGENOM; HBG715149; -.
DR   HOVERGEN; HBG054636; -.
DR   InParanoid; Q61792; -.
DR   OMA; SIQRNAP; -.
DR   OrthoDB; EOG4PVP0H; -.
DR   PhylomeDB; Q61792; -.
DR   NextBio; 290666; -.
DR   ArrayExpress; Q61792; -.
DR   Bgee; Q61792; -.
DR   CleanEx; MM_LASP1; -.
DR   Genevestigator; Q61792; -.
DR   GermOnline; ENSMUSG00000038366; Mus musculus.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR   GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR   GO; GO:0015075; F:ion transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR013998; Nebulin.
DR   InterPro; IPR000900; Nebulin_35r-motif.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR001781; Znf_LIM.
DR   Gene3D; G3DSA:2.10.110.10; Znf_LIM; 1.
DR   PANTHER; PTHR11039; Nebulin; 1.
DR   Pfam; PF00412; LIM; 1.
DR   Pfam; PF00880; Nebulin; 2.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00132; LIM; 1.
DR   SMART; SM00227; NEBU; 2.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR   PROSITE; PS51216; NEBULIN; 2.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Cytoplasm; Cytoskeleton; Ion transport;
KW   LIM domain; Metal-binding; Phosphoprotein; Repeat; SH3 domain;
KW   Transport; Zinc.
FT   CHAIN         1    263       LIM and SH3 domain protein 1.
FT                                /FTId=PRO_0000075762.
FT   DOMAIN        5     56       LIM zinc-binding.
FT   REPEAT       61     95       Nebulin 1.
FT   REPEAT       97    131       Nebulin 2.
FT   DOMAIN      204    263       SH3.
FT   COMPBIAS    174    180       Poly-Gln.
FT   COMPBIAS    203    206       Poly-Gly.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      42     42       N6-acetyllysine (By similarity).
FT   MOD_RES      68     68       Phosphothreonine (By similarity).
FT   MOD_RES     104    104       Phosphothreonine (By similarity).
FT   MOD_RES     128    128       N6-acetyllysine (By similarity).
FT   MOD_RES     151    151       Phosphoserine (By similarity).
FT   MOD_RES     156    156       Phosphothreonine; by PKA.
FT   MOD_RES     173    173       Phosphotyrosine (By similarity).
SQ   SEQUENCE   263 AA;  29994 MW;  A6CA2FC2E451433E CRC64;
     MNPNCARCGK IVYPTEKVNC LDKYWHKACF HCETCKMTLN MKNYKGYEKK PYCNAHYPKQ
     SFTMVADTPE NLRLKQQSEL QSQVRYKEEF EKNKGKGFSV VADTPELQRI KKTQDQISNI
     KYHEEFEKSR MGPSGGEGVE PERREAQDSS SYRRPTEQQQ PQPHHIPTSA PVYQQPQQQQ
     MTSSYGGYKE PAAPVSIQRS APGGGGKRYR AVYDYSAADE DEVSFQDGDT IVNVQQIDDG
     WMYGTVERTG DTGMLPANYV EAI
//
ID   RAI1_MOUSE              Reviewed;        1889 AA.
AC   Q61818; Q6ZPH7; Q8CEV1;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Retinoic acid-induced protein 1;
GN   Name=Rai1; Synonyms=Kiaa1820;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 676-690,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=96078271; PubMed=7476016; DOI=10.1016/0169-328X(95)00020-S;
RA   Imai Y., Suzuki Y., Matsui T., Tohyama M., Wanaka A., Takagi T.;
RT   "Cloning of a retinoic acid-induced gene, GT1, in the embryonal
RT   carcinoma cell line P19: neuron-specific expression in the mouse
RT   brain.";
RL   Brain Res. Mol. Brain Res. 31:1-9(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 372-1889 (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1706-1840 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15746153; DOI=10.1093/hmg/ddi085;
RA   Bi W., Ohyama T., Nakamura H., Yan J., Visvanathan J., Justice M.J.,
RA   Lupski J.R.;
RT   "Inactivation of Rai1 in mice recapitulates phenotypes observed in
RT   chromosome engineered mouse models for Smith-Magenis syndrome.";
RL   Hum. Mol. Genet. 14:983-995(2005).
CC   -!- FUNCTION: May function as a transcriptional regulator. Regulates
CC       transcription through chromatin remodeling by interacting with
CC       other proteins in chromatin as well as proteins in the basic
CC       transcriptional machinery. May be important for embryonic and
CC       postnatal development. May be involved in neuronal
CC       differentiation.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=In neurons,
CC       localized to neurites.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q61818-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q61818-2; Sequence=VSP_011004, VSP_011005;
CC   -!- TISSUE SPECIFICITY: Detected in all tissues examined with strong
CC       expression in the thymus and brain. Expressed in epithelial cells
CC       involved in organogenesis. No expression was seen in the corpus
CC       callosum of the brain.
CC   -!- DISRUPTION PHENOTYPE: Haploinsufficiency cause obesity and
CC       craniofacial abnormalities. Homozygous mice die during
CC       gastrulation and organogenesis. The few surviving mice experienced
CC       postnatal growth retardation and most of them died before weaning.
CC   -!- SIMILARITY: Contains 1 PHD-type zinc finger.
CC   -----------------------------------------------------------------------
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DR   EMBL; D29801; BAA06184.1; -; mRNA.
DR   EMBL; AK129449; BAC98259.1; -; mRNA.
DR   EMBL; AK013909; BAC25417.1; -; mRNA.
DR   IPI; IPI00454207; -.
DR   IPI; IPI00890011; -.
DR   PIR; T30250; T30250.
DR   UniGene; Mm.296366; -.
DR   STRING; Q61818; -.
DR   PhosphoSite; Q61818; -.
DR   PRIDE; Q61818; -.
DR   Ensembl; ENSMUST00000064190; ENSMUSP00000070896; ENSMUSG00000062115.
DR   Ensembl; ENSMUST00000102688; ENSMUSP00000099749; ENSMUSG00000062115.
DR   MGI; MGI:103291; Rai1.
DR   GeneTree; ENSGT00530000063684; -.
DR   HOGENOM; HBG282250; -.
DR   HOVERGEN; HBG056862; -.
DR   InParanoid; Q61818; -.
DR   ArrayExpress; Q61818; -.
DR   Bgee; Q61818; -.
DR   CleanEx; MM_RAI1; -.
DR   Genevestigator; Q61818; -.
DR   GermOnline; ENSMUSG00000062115; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:MGI.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR   InterPro; IPR001965; Znf_PHD.
DR   SMART; SM00249; PHD; 1.
DR   PROSITE; PS01359; ZF_PHD_1; FALSE_NEG.
DR   PROSITE; PS50016; ZF_PHD_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm;
KW   Direct protein sequencing; Metal-binding; Nucleus; Phosphoprotein;
KW   Zinc; Zinc-finger.
FT   CHAIN         1   1889       Retinoic acid-induced protein 1.
FT                                /FTId=PRO_0000097160.
FT   ZN_FING    1838   1885       PHD-type.
FT   MOTIF      1143   1160       Nuclear localization signal (Potential).
FT   MOTIF      1206   1223       Nuclear localization signal (Potential).
FT   COMPBIAS    117    197       Pro-rich.
FT   COMPBIAS    117    128       Poly-Pro.
FT   COMPBIAS   1462   1465       Poly-Gly.
FT   COMPBIAS   1597   1609       Ser-rich.
FT   MOD_RES     328    328       Phosphoserine (By similarity).
FT   MOD_RES     551    551       Phosphoserine (By similarity).
FT   MOD_RES     554    554       Phosphoserine (By similarity).
FT   MOD_RES     557    557       Phosphoserine (By similarity).
FT   MOD_RES     666    666       Phosphoserine (By similarity).
FT   MOD_RES     679    679       Phosphothreonine (By similarity).
FT   MOD_RES     757    757       N6-acetyllysine (By similarity).
FT   MOD_RES     863    863       Phosphoserine (By similarity).
FT   MOD_RES     875    875       Phosphoserine (By similarity).
FT   MOD_RES    1047   1047       Phosphoserine (By similarity).
FT   MOD_RES    1051   1051       Phosphothreonine (By similarity).
FT   MOD_RES    1090   1090       Phosphoserine (By similarity).
FT   MOD_RES    1091   1091       Phosphoserine (By similarity).
FT   MOD_RES    1093   1093       Phosphoserine (By similarity).
FT   MOD_RES    1102   1102       Phosphoserine (By similarity).
FT   MOD_RES    1105   1105       Phosphoserine (By similarity).
FT   MOD_RES    1109   1109       Phosphoserine (By similarity).
FT   MOD_RES    1312   1312       Phosphoserine (By similarity).
FT   MOD_RES    1332   1332       Phosphoserine (By similarity).
FT   MOD_RES    1343   1343       Phosphoserine (By similarity).
FT   MOD_RES    1400   1400       Phosphoserine (By similarity).
FT   VAR_SEQ    1838   1840       PCT -> VRG (in isoform 2).
FT                                /FTId=VSP_011004.
FT   VAR_SEQ    1841   1889       Missing (in isoform 2).
FT                                /FTId=VSP_011005.
FT   CONFLICT    412    413       DL -> EV (in Ref. 1; BAA06184).
SQ   SEQUENCE   1889 AA;  201529 MW;  4B315415981EB7B6 CRC64;
     MQSFRERCGF HGKQQNYPQT SQETSRLENY RQPGQAGLSC DRQRLLAKDY YSPQPYTGYE
     GGTGTPSGTV ATAAADKYHR GSKSLQGRPA FPSYVQDSSP YPGRYSGEEG LQTWGGPQPP
     PPQPQPLPGA VSKYEENLMK KTVVPPPNRQ YPEQGPQLPF RTHSLHVPPP QPQQPLAYPK
     LQRQKPQNDL ASPLPFPQGS HFPQHSQSFP TSSTYAPTVQ GGGQGAHSYK SCTAPSAQPH
     DRPMSANANL APGQRVQNLH AYQPGRLGYE QQQQALQGRH HTQETLHYQN LAKYQHYGQQ
     GQGYCPPDTA VRTPEQYYQT FSPSSSHSPA RSVGRSPSYS STPSPLMPNL ENFPYSQQPL
     STGAFPTGIT DHSHFMPLLN PSPTDAASSV DPQAGNCKPL QKEKLPDNLL SDLSLQSLTA
     LTSQVENISN TVQQLLLSKA TMPQKKGVKN LVSRTPEQHK SQHCSPEGSG YSAEPAGTPL
     SEPPSSTPQS THAEPQDTDY LSGSEDPLER SFLYCSQARG SPARVNSNSK AKPESVSTCS
     VTSPDDMSTK SDDSFQSLHS TLPLDSFSKF VAGERDCPRL LLSALAQEDL ASEILGLQEA
     IVEKADKAWA EASSLPKDNG KPPFSLENHG ACLDTVAKTS WSQPGEPETL PEPLQLDKGG
     STKDFSPGLF EDPSVAFATT DPKKTSSPLS FGTKPLLGTA TPDPTTAAFD CFPDTPTASS
     VDGANPFAWP EENLGDACPR WGLHPGELTK GLEQGAKASD GVGKADAHEA SACMGFQEDH
     AIGKPAAALS GDFKQQEAEG VKEEVGGLLQ CPEVAKADQW LEESRHCCSS TDFGDLPLLP
     PPGRKEDLEA EEEYSSLCEL LGSPEQRPSL QDPLSPKAPL MCTKEEAEEA LDTKAGWVSP
     CHLSGEPAVL LGPSVGAQSK VQSWFESSLS HMKPGEEGPE MERAPGSSGT SQGSLAPKPN
     KPAVPEGPIA KKEPVPRGKS LRSRRVHRGL PEAEDSPCRV PALPKDLLLP ESCTGPPQGQ
     AEGAGAPGRG LSEGLPRMCT RSLTALSEPQ TPGPPGLTTT PTPPDKLGGK QRAAFKSGKR
     VGKPSPKAAS SPSNPAALPV ASDSSPMGSK TKEPDSPSMP GKDQRSMVLR SRTKPQQVFH
     AKRRRPSESR IPDCRATKKL PANNHLPTAF KVSSGPQKEG RMSQRVKVPK PGTGNKLSDR
     PLHTLKRKSA FMAPVPAKKR SLILRSNNGS GGDGREERAE SSPGLLRRMA SPQRARPRGS
     GEPPPPPPLE PPAACMGLST QSSLPSAVRT KVLPPRKGRG LKLEAIVQKI TSPGLKKLAC
     RVAGAPPGTP RSPALPERRP GGSPAGAEEG LGGMGQMLPA ASGADPLCRN PASRSLKGKL
     LNSKKLSSAA DCPKAEAFMS PETLPSLGTA RAPKKRSRKG RTGTLGPSKG PLEKRPCPGQ
     PLLLAPHDRA SSTQGGGEDN SSGGGKKPKT EELGPASQPP EGRPCQPQTR AQKQPGQASY
     SSYSKRKRLS RGRGKTAHAS PCKGRATRRR QQQVLPLDPA EPEIRLKYIS SCKRLRADSR
     TPAFSPFVRV EKRDAYTTIC TVVNSPGDEP KPHWKPSSSA ASSSTSSSSL EPAGASLTTF
     PGGSVLQQRP SLPLSSTMHL GPVVSKALST SCLVCCLCQN PANFKDLGDL CGPYYPEHCL
     PKKKPKLKEK ARLEGTLEEA SLPLERTLKG LECSASTTAA APTTATITTP TALGRLSRPD
     GPADPAKQGP LRTSARGLSR RLQSCYCCDG QGDGGEEVAQ ADKSRKHECS KEAPTEPGGD
     TQEHWVHEAC AVWTSGVYLV AGKLFGLQEA MKVAVDMPCT SCHEPGATIS CSYKGCIHTY
     HYPCANDTGC TFIEENFTLK CPKHKRLPL
//
ID   PDCD4_MOUSE             Reviewed;         469 AA.
AC   Q61823; P97296; Q3T9A9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Programmed cell death protein 4;
DE   AltName: Full=Protein MA-3;
DE   AltName: Full=Topoisomerase-inhibitor suppressed protein;
GN   Name=Pdcd4; Synonyms=Ma3, Tis;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=ICR; TISSUE=Thymus;
RX   MEDLINE=96125207; PubMed=8543179; DOI=10.1016/0378-1119(95)00607-9;
RA   Shibahara K., Asano M., Ishida Y., Aoki T., Koike T., Honjo T.;
RT   "Isolation of a novel mouse gene MA-3 that is induced upon programmed
RT   cell death.";
RL   Gene 166:297-301(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lymphoma;
RX   MEDLINE=97069646; PubMed=8912629; DOI=10.1006/bbrc.1996.1609;
RA   Onishi Y., Kizaki H.;
RT   "Molecular cloning of the genes suppressed in RVC lymphoma cells by
RT   topoisomerase inhibitors.";
RL   Biochem. Biophys. Res. Commun. 228:7-13(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=98382539; PubMed=9714845; DOI=10.1016/S0378-1119(98)00313-8;
RA   Onishi Y., Hashimoto S., Kizaki H.;
RT   "Cloning of the TIS gene suppressed by topoisomerase inhibitors.";
RL   Gene 215:453-459(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BTBR T+ tf/J;
RX   PubMed=16682971; DOI=10.1038/ng1796;
RA   Clee S.M., Yandell B.S., Schueler K.M., Rabaglia M.E., Richards O.C.,
RA   Raines S.M., Kabara E.A., Klass D.M., Mui E.T.-K., Stapleton D.S.,
RA   Gray-Keller M.P., Young M.B., Stoehr J.P., Lan H., Boronenkov I.,
RA   Raess P.W., Flowers M.T., Attie A.D.;
RT   "Positional cloning of Sorcs1, a type 2 diabetes quantitative trait
RT   locus.";
RL   Nat. Genet. 38:688-693(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E.,
RA   Mollenhauer J., Wiemann S., Schick M., Korn B.;
RT   "Cloning of mouse full open reading frames in Gateway(R) system entry
RT   vector (pDONR201).";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EIF4A1 AND
RP   EIF4A2.
RX   PubMed=12482958; DOI=10.1128/MCB.23.1.26-37.2003;
RA   Yang H.-S., Jansen A.P., Komar A.A., Zheng X., Merrick W.C.,
RA   Costes S., Lockett S.J., Sonenberg N., Colburn N.H.;
RT   "The transformation suppressor Pdcd4 is a novel eukaryotic translation
RT   initiation factor 4A binding protein that inhibits translation.";
RL   Mol. Cell. Biol. 23:26-37(2003).
RN   [9]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12894233; DOI=10.1038/sj.onc.1206710;
RA   Boehm M., Sawicka K., Siebrasse J.P., Brehmer-Fastnacht A., Peters R.,
RA   Klempnauer K.-H.;
RT   "The transformation suppressor protein Pdcd4 shuttles between nucleus
RT   and cytoplasm and binds RNA.";
RL   Oncogene 22:4905-4910(2003).
RN   [10]
RP   FUNCTION.
RX   PubMed=16024603; DOI=10.1158/0008-5472.CAN-04-2119;
RA   Jansen A.P., Camalier C.E., Colburn N.H.;
RT   "Epidermal expression of the translation inhibitor programmed cell
RT   death 4 suppresses tumorigenesis.";
RL   Cancer Res. 65:6034-6041(2005).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) OF 320-469, FUNCTION,
RP   INTERACTION WITH EIF4A AND EIF4G, SUBUNIT, AND MUTAGENESIS OF ASP-414;
RP   ASP-418 AND SER-457.
RX   PubMed=17060447; DOI=10.1128/MCB.00867-06;
RA   Laronde-Leblanc N., Santhanam A.N., Baker A.R., Wlodawer A.,
RA   Colburn N.H.;
RT   "Structural basis for inhibition of translation by the tumor
RT   suppressor pdcd4.";
RL   Mol. Cell. Biol. 27:147-156(2007).
RN   [13]
RP   STRUCTURE BY NMR OF 319-449, AND INTERACTION WITH EIF4A1.
RX   PubMed=17310995; DOI=10.1038/sj.onc.1210305;
RA   Waters L.C., Veverka V., Bohm M., Schmedt T., Choong P.T.,
RA   Muskett F.W., Klempnauer K.H., Carr M.D.;
RT   "Structure of the C-terminal MA-3 domain of the tumour suppressor
RT   protein Pdcd4 and characterization of its interaction with eIF4A.";
RL   Oncogene 26:4941-4950(2007).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 120-469 IN COMPLEX WITH
RP   EIF4A1, SUBUNIT, AND DOMAIN.
RX   PubMed=19153607; DOI=10.1038/emboj.2008.278;
RA   Loh P.G., Yang H.S., Walsh M.A., Wang Q., Wang X., Cheng Z., Liu D.,
RA   Song H.;
RT   "Structural basis for translational inhibition by the tumour
RT   suppressor Pdcd4.";
RL   EMBO J. 28:274-285(2009).
CC   -!- FUNCTION: Inhibits translation initiation and cap-dependent
CC       translation. May excert its function by hindering the interaction
CC       between EIF4A1 and EIF4G. Inhibits the helicase activity of EIF4A.
CC       Modulates the activation of JUN kinase. Down-regulates the
CC       expression of MAP4K1, thus inhibiting events important in driving
CC       invasion, namely, MAPK85 activation and consequent JUN-dependent
CC       transcription. May play a role in apoptosis. Tumor suppressor.
CC       Inhibits tumor promoter-induced neoplastic transformation. Binds
CC       RNA.
CC   -!- SUBUNIT: Interacts (via MI domains) with EIF4A1 and EIF4A2 (via N-
CC       terminal domain). Heterotrimer with EIF4A1; one molecule of PDCD4
CC       binds two molecules of EIF4A1. Interacts with EIF4G1. May form a
CC       complex with EIF4A1 and EIF4G1. The interaction between PDCD4 and
CC       EIF4A1 interferes with the interaction between EIF4A1 and EIF4G.
CC       When phosphorylated, interacts with BTRC and FBXW11 (By
CC       similarity).
CC   -!- INTERACTION:
CC       Q61655:Ddx19a; NbExp=1; IntAct=EBI-296473, EBI-296479;
CC       Q62448:Eif4g2; NbExp=1; IntAct=EBI-296473, EBI-296494;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between
CC       the nucleus and cytoplasm. Predominantly nuclear under normal
CC       growth conditions, and when phosphorylated at Ser-457 (By
CC       similarity). Exported from the nucleus in the absence of serum.
CC   -!- TISSUE SPECIFICITY: Expressed ubiquitously. Highyly expressed in
CC       thymus and liver. Moderately expressed in brain, kidney and
CC       spleen; weakly in lung and heart. Expression is up- or down-
CC       regulated in response to apoptosis inducers. Regulated by many
CC       programmed cell death-inducing stimuli.
CC   -!- DOMAIN: Binds EIF4A1 via both MI domains.
CC   -!- PTM: Polyubiquitinated, leading to its proteasomal degradation.
CC       Rapidly degraded in response to mitogens. Phosphorylation of the
CC       phosphodegron promotes interaction with BTRC and proteasomal
CC       degradation (By similarity).
CC   -!- DISEASE: Note=Decreases benign tumor development and malignant
CC       progression.
CC   -!- SIMILARITY: Belongs to the PDCD4 family.
CC   -!- SIMILARITY: Contains 2 MI domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; D50465; BAA09056.1; -; mRNA.
DR   EMBL; D86344; BAA13072.1; -; mRNA.
DR   EMBL; AB010139; BAA32356.1; -; Genomic_DNA.
DR   EMBL; DQ479921; ABF51670.1; -; Genomic_DNA.
DR   EMBL; CT010188; CAJ18396.1; -; mRNA.
DR   EMBL; AK134366; BAE22118.1; -; mRNA.
DR   EMBL; AK172654; BAE43115.1; -; mRNA.
DR   EMBL; BC055739; AAH55739.1; -; mRNA.
DR   IPI; IPI00323064; -.
DR   PIR; JC4523; JC4523.
DR   RefSeq; NP_001161963.1; NM_001168491.1.
DR   RefSeq; NP_001161964.1; NM_001168492.1.
DR   RefSeq; NP_035180.2; NM_011050.4.
DR   UniGene; Mm.1605; -.
DR   PDB; 2HM8; NMR; -; A=319-449.
DR   PDB; 2IOL; X-ray; 2.00 A; A/B=320-469.
DR   PDB; 2ION; X-ray; 1.57 A; A=320-469.
DR   PDB; 2IOS; X-ray; 1.76 A; A=320-469.
DR   PDB; 2NSZ; X-ray; 1.15 A; A=322-450.
DR   PDB; 3EIQ; X-ray; 3.50 A; C=120-469.
DR   PDBsum; 2HM8; -.
DR   PDBsum; 2IOL; -.
DR   PDBsum; 2ION; -.
DR   PDBsum; 2IOS; -.
DR   PDBsum; 2NSZ; -.
DR   PDBsum; 3EIQ; -.
DR   ProteinModelPortal; Q61823; -.
DR   SMR; Q61823; 157-450.
DR   IntAct; Q61823; 3.
DR   MINT; MINT-7012023; -.
DR   STRING; Q61823; -.
DR   PhosphoSite; Q61823; -.
DR   PRIDE; Q61823; -.
DR   Ensembl; ENSMUST00000025931; ENSMUSP00000025931; ENSMUSG00000024975.
DR   Ensembl; ENSMUST00000074371; ENSMUSP00000073975; ENSMUSG00000024975.
DR   GeneID; 18569; -.
DR   KEGG; mmu:18569; -.
DR   UCSC; uc008hxb.1; mouse.
DR   CTD; 18569; -.
DR   MGI; MGI:107490; Pdcd4.
DR   eggNOG; roNOG08674; -.
DR   GeneTree; ENSGT00390000015948; -.
DR   HOGENOM; HBG714347; -.
DR   HOVERGEN; HBG052841; -.
DR   InParanoid; Q61823; -.
DR   OMA; MSKGGKR; -.
DR   OrthoDB; EOG4GMTX3; -.
DR   PhylomeDB; Q61823; -.
DR   NextBio; 294400; -.
DR   ArrayExpress; Q61823; -.
DR   Bgee; Q61823; -.
DR   CleanEx; MM_PDCD4; -.
DR   Genevestigator; Q61823; -.
DR   GermOnline; ENSMUSG00000024975; Mus musculus.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0007569; P:cell aging; ISS:UniProtKB.
DR   GO; GO:0043508; P:negative regulation of JUN kinase activity; ISS:UniProtKB.
DR   GO; GO:0016481; P:negative regulation of transcription; ISS:UniProtKB.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR   Pfam; PF02847; MA3; 2.
DR   SMART; SM00544; MA3; 2.
DR   SUPFAM; SSF48371; ARM-type_fold; 2.
DR   PROSITE; PS51366; MI; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Apoptosis; Cytoplasm; Nucleus; Phosphoprotein; Repeat;
KW   RNA-binding; Tumor suppressor; Ubl conjugation.
FT   CHAIN         1    469       Programmed cell death protein 4.
FT                                /FTId=PRO_0000256520.
FT   DOMAIN      163    284       MI 1.
FT   DOMAIN      326    449       MI 2.
FT   MOTIF        58     64       Nuclear localization signal (Potential).
FT   MOTIF        70     76       Phosphodegron (By similarity).
FT   MOTIF       448    454       Nuclear localization signal (Potential).
FT   MOD_RES      67     67       Phosphoserine; by PKB and RPS6KB1 (By
FT                                similarity).
FT   MOD_RES      76     76       Phosphoserine.
FT   MOD_RES      78     78       Phosphoserine (By similarity).
FT   MOD_RES      93     93       Phosphothreonine (By similarity).
FT   MOD_RES      94     94       Phosphoserine (By similarity).
FT   MOD_RES     152    152       Phosphotyrosine (By similarity).
FT   MOD_RES     457    457       Phosphoserine; by PKB (By similarity).
FT   MUTAGEN     414    414       D->A: Strongly reduced interaction with
FT                                EIF4A1.
FT   MUTAGEN     418    418       D->A: Strongly reduced interaction with
FT                                EIF4A1.
FT   MUTAGEN     457    457       S->A,D: No effect on interaction with
FT                                EIF4A1.
FT   CONFLICT    232    232       S -> I (in Ref. 2; BAA32356 and 3;
FT                                BAA13072).
FT   CONFLICT    369    369       V -> I (in Ref. 2; BAA32356 and 3;
FT                                BAA13072).
FT   CONFLICT    414    414       D -> G (in Ref. 5; BAE43115).
FT   HELIX       326    341
FT   HELIX       344    354
FT   HELIX       357    359
FT   HELIX       360    373
FT   HELIX       378    392
FT   HELIX       398    418
FT   HELIX       422    435
FT   HELIX       441    445
SQ   SEQUENCE   469 AA;  51702 MW;  6883BCE5011692F1 CRC64;
     MDIENEQTLN VNPTDPDNLS DSLFSGDEEN AGTEEIKNEI NGNWISASTI NEARINAKAK
     RRLRKNSSRD SGRGDSVSDN GSEAVRSGVA VPTSPKGRLL DRRSRSGKGR GLPKKGGAGG
     KGVWGTPGQV YDVEEVDVKD PNYDDDQENC VYETVVLPLD ETAFEKTLTP IIQEYFEHGD
     TNEVAEMLRD LNLGEMKSGV PVLAVSLALE GKASHREMTS KLLSDLCGTV MSTNDVEKSF
     DKLLKDLPEL ALDTPRAPQL VGQFIARAVG DGILCNTYID SYKGTVDCVQ ARAALDKATV
     LLSMSKGGKR KDSVWGSGGG QQPVNHLVKE IDMLLKEYLL SGDISEAEHC LKELEVPHFH
     HELVYEAIVM VLESTGESAF KMILDLLKSL WKSSTITIDQ MKRGYERIYN EIPDINLDVP
     HSYSVLERFV EECFQAGIIS KQLRDLCPSR GRKRFVSEGD GGRLKPESY
//
ID   FGFR3_MOUSE             Reviewed;         801 AA.
AC   Q61851; Q61564; Q63834;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 109.
DE   RecName: Full=Fibroblast growth factor receptor 3;
DE            Short=FGFR-3;
DE            EC=2.7.10.1;
DE   AltName: Full=Heparin-binding growth factor receptor;
DE   AltName: CD_antigen=CD333;
DE   Flags: Precursor;
GN   Name=Fgfr3; Synonyms=Mfr3, Sam3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=92355591; PubMed=1379594;
RA   Ornitz D.M., Leder P.;
RT   "Ligand specificity and heparin dependence of fibroblast growth factor
RT   receptors 1 and 3.";
RL   J. Biol. Chem. 267:16305-16311(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=93177694; PubMed=8382556;
RA   Katoh O., Hattori Y., Sasaki H., Sakamoto H., Fujimoto K., Fujii T.,
RA   Sugimura T., Terada M.;
RT   "Isolation of the complementary DNA encoding a mouse heparin-binding
RT   growth factor receptor with the use of a unique kinase insert
RT   sequence.";
RL   Cancer Res. 53:1136-1141(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 242-364 (ISOFORM 2).
RX   MEDLINE=94209351; PubMed=7512569;
RA   Chellaiah A.T., McEwen D.G., Werner S., Xu J., Ornitz D.M.;
RT   "Fibroblast growth factor receptor (FGFR) 3. Alternative splicing in
RT   immunoglobulin-like domain III creates a receptor highly specific for
RT   acidic FGF/FGF-1.";
RL   J. Biol. Chem. 269:11620-11627(1994).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-641, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Receptor for acidic and basic fibroblast growth factors.
CC       Preferentially binds FGF1.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=IIIc;
CC         IsoId=Q61851-1; Sequence=Displayed;
CC       Name=2; Synonyms=IIIb;
CC         IsoId=Q61851-2; Sequence=VSP_002990;
CC   -!- TISSUE SPECIFICITY: In embryo, expressed in heart, lung, kidney,
CC       skin, head and liver but not in muscle. In adult, highest levels
CC       in brain. Also expressed in liver, lung, kidney, testis, ovary and
CC       uterus. Very low levels in heart, thymus, spleen and muscle.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryos from mid-gestation and
CC       in adult.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Fibroblast growth factor receptor subfamily.
CC   -!- SIMILARITY: Contains 3 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; M81342; AAA39535.1; -; mRNA.
DR   EMBL; S56291; AAB25535.1; -; mRNA.
DR   EMBL; L26492; AAA21490.2; -; Genomic_DNA.
DR   IPI; IPI00126264; -.
DR   IPI; IPI00223033; -.
DR   PIR; A48991; A48991.
DR   PIR; I55363; I55363.
DR   UniGene; Mm.6904; -.
DR   ProteinModelPortal; Q61851; -.
DR   SMR; Q61851; 6-356, 453-751.
DR   DIP; DIP-6031N; -.
DR   STRING; Q61851; -.
DR   PhosphoSite; Q61851; -.
DR   PRIDE; Q61851; -.
DR   Ensembl; ENSMUST00000067150; ENSMUSP00000070998; ENSMUSG00000054252.
DR   Ensembl; ENSMUST00000114411; ENSMUSP00000110053; ENSMUSG00000054252.
DR   MGI; MGI:95524; Fgfr3.
DR   GeneTree; ENSGT00600000084001; -.
DR   HOVERGEN; HBG000345; -.
DR   OrthoDB; EOG48WC1F; -.
DR   BRENDA; 2.7.10.1; 244.
DR   ArrayExpress; Q61851; -.
DR   Bgee; Q61851; -.
DR   CleanEx; MM_FGFR3; -.
DR   Genevestigator; Q61851; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009898; C:internal side of plasma membrane; IDA:MGI.
DR   GO; GO:0005764; C:lysosome; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005007; F:fibroblast growth factor receptor activity; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0070977; P:bone maturation; IMP:BHF-UCL.
DR   GO; GO:0051216; P:cartilage development; IMP:MGI.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0060113; P:inner ear receptor cell differentiation; IMP:MGI.
DR   GO; GO:0000165; P:MAPKKK cascade; IDA:MGI.
DR   GO; GO:0002009; P:morphogenesis of an epithelium; IMP:MGI.
DR   GO; GO:0048640; P:negative regulation of developmental growth; IMP:BHF-UCL.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IMP:MGI.
DR   GO; GO:0010553; P:negative regulation of gene-specific transcription from RNA polymerase II promoter; IMP:MGI.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptosis; IMP:MGI.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; IMP:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IGI:MGI.
DR   GO; GO:0090080; P:positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway; IGI:MGI.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:MGI.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0035121; P:tail morphogenesis; IMP:BHF-UCL.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013151; Immunoglobulin.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR016248; Tyr_kinase_fibroblast_GF_rcpt.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PIRSF; PIRSF000628; FGFR; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00408; IGc2; 3.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Receptor; Repeat; Signal; Transferase; Transmembrane;
KW   Transmembrane helix; Tyrosine-protein kinase.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21    801       Fibroblast growth factor receptor 3.
FT                                /FTId=PRO_0000016786.
FT   TOPO_DOM     21    369       Extracellular (Potential).
FT   TRANSMEM    370    390       Helical; (Potential).
FT   TOPO_DOM    391    801       Cytoplasmic (Potential).
FT   DOMAIN       22    124       Ig-like C2-type 1.
FT   DOMAIN      145    238       Ig-like C2-type 2.
FT   DOMAIN      247    349       Ig-like C2-type 3.
FT   DOMAIN      466    756       Protein kinase.
FT   NP_BIND     472    480       ATP (By similarity).
FT   ACT_SITE    611    611       Proton acceptor (By similarity).
FT   BINDING     502    502       ATP (By similarity).
FT   MOD_RES     641    641       Phosphotyrosine.
FT   MOD_RES     642    642       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   CARBOHYD     96     96       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    219    219       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    256    256       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    288    288       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    309    309       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    322    322       N-linked (GlcNAc...) (Potential).
FT   DISULFID     59    107       Potential.
FT   DISULFID    170    222       Potential.
FT   DISULFID    269    333       Potential.
FT   VAR_SEQ     305    352       TAGANTTDKELEVLSLHNVTFEDAGEYTCLAGNSIGFSHHS
FT                                AWLVVLP -> SWISENVEADARLRLANVSERDGGEYLCRA
FT                                TNFIGVAEKAFWLRVHGPQA (in isoform 2).
FT                                /FTId=VSP_002990.
FT   CONFLICT    684    684       P -> L (in Ref. 2; AAB25535).
FT   CONFLICT    687    687       Missing (in Ref. 2; AAB25535).
SQ   SEQUENCE   801 AA;  87758 MW;  68BC110212691705 CRC64;
     MVVPACVLVF CVAVVAGATS EPPGPEQRVV RRAAEVPGPE PSQQEQVAFG SGDTVELSCH
     PPGGAPTGPT VWAKDGTGLV ASHRILVGPQ RLQVLNASHE DAGVYSCQHR LTRRVLCHFS
     VRVTDAPSSG DDEDGEDVAE DTGAPYWTRP ERMDKKLLAV PAANTVRFRC PAAGNPTPSI
     SWLKNGKEFR GEHRIGGIKL RHQQWSLVME SVVPSDRGNY TCVVENKFGS IRQTYTLDVL
     ERSPHRPILQ AGLPANQTAI LGSDVEFHCK VYSDAQPHIQ WLKHVEVNGS KVGPDGTPYV
     TVLKTAGANT TDKELEVLSL HNVTFEDAGE YTCLAGNSIG FSHHSAWLVV LPAEEELMET
     DEAGSVYAGV LSYGVVFFLF ILVVAAVILC RLRSPPKKGL GSPTVHKVSR FPLKRQVSLE
     SNSSMNSNTP LVRIARLSSG EGPVLANVSE LELPADPKWE LSRTRLTLGK PLGEGCFGQV
     VMAEAIGIDK DRTAKPVTVA VKMLKDDATD KDLSDLVSEM EMMKMIGKHK NIINLLGACT
     QGGPLYVLVE YAAKGNLREF LRARRPPGMD YSFDACRLPE EQLTCKDLVS CAYQVARGME
     YLASQKCIHR DLAARNVLVT EDNVMKIADF GLARDVHNLD YYKKTTNGRL PVKWMAPEAL
     FDRVYTHQSD VWSFGVLLWE IFTPGGPSPY PGIPVEELFK LLKEGHRMDK PASCTHDLYM
     IMRECWHAVP SQRPTFKQLV EDLDRILTVT STDEYLDLSV PFEQYSPGGQ DTPSSSSSGD
     DSVFTHDLLP PGPPSNGGPR T
//
ID   KCNA6_MOUSE             Reviewed;         529 AA.
AC   Q61923;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Potassium voltage-gated channel subfamily A member 6;
DE   AltName: Full=MK1.6;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv1.6;
GN   Name=Kcna6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   PubMed=1285906;
RA   Migeon M.B., Street V.A., Demas V.P., Tempel B.L.;
RT   "Cloning, sequence and chromosomal localization of MK1.6, a murine
RT   potassium channel gene.";
RL   Epilepsy Res. Suppl. 9:173-180(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Mediates the voltage-dependent potassium ion
CC       permeability of excitable membranes. Assuming opened or closed
CC       conformations in response to the voltage difference across the
CC       membrane, the protein forms a potassium-selective channel through
CC       which potassium ions may pass in accordance with their
CC       electrochemical gradient.
CC   -!- SUBUNIT: Heterotetramer of potassium channel proteins (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- DOMAIN: The N-terminus may be important in determining the rate of
CC       inactivation of the channel while the tail may play a role in
CC       modulation of channel activity and/or targeting of the channel to
CC       specific subcellular compartments.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position.
CC   -!- SIMILARITY: Belongs to the potassium channel family. A (Shaker)
CC       (TC 1.A.1.2) subfamily. Kv1.6/KCNA6 sub-subfamily.
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DR   EMBL; M96688; AAA39772.1; -; mRNA.
DR   EMBL; BC048782; AAH48782.1; -; mRNA.
DR   EMBL; BC054804; AAH54804.1; -; mRNA.
DR   IPI; IPI00127368; -.
DR   PIR; S09043; S09043.
DR   RefSeq; NP_038596.1; NM_013568.6.
DR   UniGene; Mm.62535; -.
DR   ProteinModelPortal; Q61923; -.
DR   SMR; Q61923; 41-469.
DR   STRING; Q61923; -.
DR   PhosphoSite; Q61923; -.
DR   PRIDE; Q61923; -.
DR   Ensembl; ENSMUST00000040751; ENSMUSP00000036872; ENSMUSG00000038077.
DR   Ensembl; ENSMUST00000112242; ENSMUSP00000107861; ENSMUSG00000038077.
DR   GeneID; 16494; -.
DR   KEGG; mmu:16494; -.
DR   CTD; 16494; -.
DR   MGI; MGI:96663; Kcna6.
DR   eggNOG; maNOG11602; -.
DR   GeneTree; ENSGT00560000076957; -.
DR   HOGENOM; HBG445693; -.
DR   HOVERGEN; HBG052230; -.
DR   InParanoid; Q61923; -.
DR   OMA; KATDNGL; -.
DR   OrthoDB; EOG43JC4R; -.
DR   PhylomeDB; Q61923; -.
DR   NextBio; 289803; -.
DR   ArrayExpress; Q61923; -.
DR   Bgee; Q61923; -.
DR   Genevestigator; Q61923; -.
DR   GermOnline; ENSMUSG00000038077; Mus musculus.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003972; K_chnl_volt-dep_Kv1.
DR   InterPro; IPR004053; K_chnl_volt-dep_Kv1.6.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01513; KV16CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01496; SHAKERCHANEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Ion transport; Ionic channel; Lipoprotein; Membrane;
KW   Palmitate; Phosphoprotein; Potassium; Potassium channel;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN         1    529       Potassium voltage-gated channel subfamily
FT                                A member 6.
FT                                /FTId=PRO_0000053991.
FT   TRANSMEM    175    193       Helical; Name=Segment S1; (Potential).
FT   TRANSMEM    263    284       Helical; Name=Segment S2; (Potential).
FT   TRANSMEM    296    316       Helical; Name=Segment S3; (Potential).
FT   TRANSMEM    340    360       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TRANSMEM    376    396       Helical; Name=Segment S5; (Potential).
FT   TRANSMEM    437    457       Helical; Name=Segment S6; (Potential).
FT   MOTIF       422    427       Selectivity filter (By similarity).
FT   MOTIF       527    529       PDZ-binding (Potential).
FT   MOD_RES       8      8       Phosphothreonine.
FT   MOD_RES     511    511       Phosphoserine; by PKA (Probable).
FT   LIPID       285    285       S-palmitoyl cysteine (Potential).
FT   CARBOHYD     46     46       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   529 AA;  58674 MW;  336D78C069ABEADD CRC64;
     MRSEKSLTLA APGEVRGPEG EQQDAGEFQE AEGGGGCCSS ERLVINISGL RFETQLRTLS
     LFPDTLLGDP GRRVRFFDPL RNEYFFDRNR PSFDAILYYY QSGGRLRRPV NVPLDIFMEE
     IRFYQLGEEA LAAFREDEGC LPEGGEDEKP LPSQPFQRQV WLLFEYPESS GPARGIAIVS
     VLVILISIVI FCLETLPQFR ADGRGGSNEG SGTRLSPASR SHEEEDEDED SYAFPGSIPS
     GGLGTGGTSS LSTLGGSFFT DPFFLVETLC IVWFTFELLV RFSACPSKAA FFRNIMNIID
     LVAIFPYFIT LGTELVQRHE QQSVSGGSGQ NGQQAMSLAI LRVIRLVRVF RIFKLSRHSK
     GLQILGKTLQ ASMRELGLLI FFLFIGVILF SSAVYFAEAD DVDSLFPSIP DAFWWAVVTM
     TTVGYGDMYP MTVGGKIVGS LCAIAGVLTI ALPVPVIVSN FNYFYHRETE QEEQGQYTHV
     TCGQPTPDLK ATDNGLGKPD FAEASRERRP SYLPTPHRAY AEKRMLTEV
//
ID   NPM_MOUSE               Reviewed;         292 AA.
AC   Q61937;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=Nucleophosmin;
DE            Short=NPM;
DE   AltName: Full=Nucleolar phosphoprotein B23;
DE   AltName: Full=Nucleolar protein NO38;
DE   AltName: Full=Numatrin;
GN   Name=Npm1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=89120362; PubMed=3219912; DOI=10.1007/BF00303035;
RA   Schmidt-Zachmann M.S., Franke W.W.;
RT   "DNA cloning and amino acid sequence determination of a major
RT   constituent protein of mammalian nucleoli. Correspondence of the
RT   nucleoplasmin-related protein NO38 to mammalian protein B23.";
RL   Chromosoma 96:417-426(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 33-45.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [5]
RP   PROTEIN SEQUENCE OF 46-52 AND 266-271, SUBUNIT, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Spleen;
RX   MEDLINE=98307943; PubMed=9642267; DOI=10.1074/jbc.273.27.17025;
RA   Borggrefe T., Wabl M., Akhmedov A.T., Jessberger R.;
RT   "A B-cell-specific DNA recombination complex.";
RL   J. Biol. Chem. 273:17025-17035(1998).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252 AND SER-258, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-125, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Involved in diverse cellular processes such as ribosome
CC       biogenesis, centrosome duplication, protein chaperoning, histone
CC       assembly, cell proliferation, and regulation of tumor suppressors
CC       p53/TP53 and ARF. Binds ribosome presumably to drive ribosome
CC       nuclear export. Acts as a chaperonin for the core histones H3, H2B
CC       and H4. Stimulates APEX1 endonuclease activity on
CC       apurinic/apyrimidinic (AP) double-stranded DNA but inhibits APEX1
CC       endonuclease activity on AP single-stranded RNA. May exert a
CC       control of APEX1 endonuclease activity within nucleoli devoted to
CC       repair AP on rDNA and the removal of oxidized rRNA molecules (By
CC       similarity). Associated with nucleolar ribonucleoprotein
CC       structures and bind single-stranded nucleic acids.
CC   -!- SUBUNIT: Decamer formed by two pentameric rings associated in a
CC       head-to-head fashion. Disulfide-linked dimers under certain
CC       conditions. Interacts with NSUN2 and SENP3 (By similarity). The
CC       SWAP complex consists of NPM1, NCL, PARP1 and SWAP70. Interacts
CC       with the methylated form of RPS10. Interacts (via N-terminal
CC       domain) with APEX1; the interaction is RNA-dependent and decreases
CC       in hydrogen peroxide-damaged cells (By similarity).
CC   -!- INTERACTION:
CC       Q00987:MDM2 (xeno); NbExp=2; IntAct=EBI-626362, EBI-389668;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm (By
CC       similarity). Note=Generally nucleolar, but is translocated to the
CC       nucleoplasm in case of serum starvation or treatment with
CC       anticancer drugs. Co-localizes with the methylated form of RPS10
CC       in the granular component (GC) region of the nucleolus.
CC       Colocalized with nucleolin and APEX1 in nucleoli (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in B-cells that have been induced to
CC       switch to various Ig isotypes.
CC   -!- PTM: Acetylated at C-terminal lysine residues, thereby increasing
CC       affinity to histones (By similarity).
CC   -!- PTM: ADP-ribosylated (By similarity).
CC   -!- PTM: Phosphorylated at Ser-4 by PLK1. Phosphorylated by CDK2 at
CC       Ser-125 and Thr-198. Phosphorylation at Thr-198 may trigger
CC       initiation of centrosome duplication. Phosphorylated by CDK1 at
CC       Thr-198, Thr-217, Thr-232 and Thr-235 during cell mitosis. When
CC       these four sites are phosphorated, RNA-binding activity seem to be
CC       abolished. May be phosphorylated at Ser-70 by NEK2 (By
CC       similarity).
CC   -!- PTM: Sumoylated by ARF (By similarity).
CC   -!- SIMILARITY: Belongs to the nucleoplasmin family.
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DR   EMBL; M33212; AAA39801.1; -; mRNA.
DR   EMBL; AK028253; BAC25844.1; -; mRNA.
DR   EMBL; BC054755; AAH54755.1; -; mRNA.
DR   IPI; IPI00127415; -.
DR   PIR; I52858; I52858.
DR   RefSeq; NP_032748.1; NM_008722.2.
DR   UniGene; Mm.480560; -.
DR   ProteinModelPortal; Q61937; -.
DR   SMR; Q61937; 15-118, 241-292.
DR   IntAct; Q61937; 2.
DR   MINT; MINT-270928; -.
DR   STRING; Q61937; -.
DR   PhosphoSite; Q61937; -.
DR   PRIDE; Q61937; -.
DR   Ensembl; ENSMUST00000075641; ENSMUSP00000075067; ENSMUSG00000057113.
DR   GeneID; 18148; -.
DR   KEGG; mmu:18148; -.
DR   UCSC; uc007ikd.1; mouse.
DR   CTD; 18148; -.
DR   MGI; MGI:106184; Npm1.
DR   HOGENOM; HBG278094; -.
DR   HOVERGEN; HBG001860; -.
DR   InParanoid; Q61937; -.
DR   OMA; NCFRTED; -.
DR   OrthoDB; EOG4W3SNZ; -.
DR   PhylomeDB; Q61937; -.
DR   NextBio; 293410; -.
DR   ArrayExpress; Q61937; -.
DR   Bgee; Q61937; -.
DR   CleanEx; MM_NPM1; -.
DR   Genevestigator; Q61937; -.
DR   GermOnline; ENSMUSG00000057113; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0001652; C:granular component; IDA:MGI.
DR   GO; GO:0015934; C:large ribosomal subunit; IDA:MGI.
DR   GO; GO:0016607; C:nuclear speck; IDA:MGI.
DR   GO; GO:0015935; C:small ribosomal subunit; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0051059; F:NF-kappaB binding; ISS:UniProtKB.
DR   GO; GO:0019843; F:rRNA binding; IDA:MGI.
DR   GO; GO:0051082; F:unfolded protein binding; ISS:UniProtKB.
DR   GO; GO:0007569; P:cell aging; ISS:UniProtKB.
DR   GO; GO:0016049; P:cell growth; IDA:MGI.
DR   GO; GO:0006884; P:cell volume homeostasis; IDA:MGI.
DR   GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
DR   GO; GO:0048025; P:negative regulation of nuclear mRNA splicing, via spliceosome; IDA:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
DR   GO; GO:0010825; P:positive regulation of centrosome duplication; IGI:MGI.
DR   GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:MGI.
DR   GO; GO:0008104; P:protein localization; IMP:MGI.
DR   GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; IGI:MGI.
DR   GO; GO:0032071; P:regulation of endodeoxyribonuclease activity; ISS:UniProtKB.
DR   GO; GO:0060699; P:regulation of endoribonuclease activity; ISS:UniProtKB.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; IDA:MGI.
DR   GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:MGI.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IDA:MGI.
DR   GO; GO:0000056; P:ribosomal small subunit export from nucleus; IDA:MGI.
DR   GO; GO:0006407; P:rRNA export from nucleus; IDA:MGI.
DR   InterPro; IPR004301; Nucleoplasmin.
DR   PANTHER; PTHR22747; Nucleoplasmin; 1.
DR   Pfam; PF03066; Nucleoplasmin; 1.
DR   SUPFAM; SSF69203; Nucleoplasmin; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ADP-ribosylation; Chaperone; Direct protein sequencing;
KW   Disulfide bond; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
KW   RNA-binding; Ubl conjugation.
FT   CHAIN         1    292       Nucleophosmin.
FT                                /FTId=PRO_0000219482.
FT   REGION        1    185       Required for interaction with SENP3 (By
FT                                similarity).
FT   REGION        1    117       Necessary for interaction with APEX1 (By
FT                                similarity).
FT   REGION      241    292       Required for nucleolar localization (By
FT                                similarity).
FT   MOTIF       152    157       Nuclear localization signal (Potential).
FT   MOTIF       190    196       Nuclear localization signal (Potential).
FT   COMPBIAS      1      9       Met-rich.
FT   COMPBIAS    120    132       Asp/Glu-rich (acidic).
FT   COMPBIAS    158    187       Asp/Glu-rich (highly acidic).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES       4      4       Phosphoserine; by PLK1 (By similarity).
FT   MOD_RES      10     10       Phosphoserine (By similarity).
FT   MOD_RES      32     32       N6-acetyllysine (By similarity).
FT   MOD_RES      70     70       Phosphoserine.
FT   MOD_RES      75     75       Phosphothreonine (By similarity).
FT   MOD_RES      88     88       Phosphoserine (By similarity).
FT   MOD_RES      95     95       Phosphothreonine (By similarity).
FT   MOD_RES     106    106       Phosphoserine (By similarity).
FT   MOD_RES     125    125       Phosphoserine.
FT   MOD_RES     139    139       Phosphoserine (By similarity).
FT   MOD_RES     150    150       N6-acetyllysine (By similarity).
FT   MOD_RES     154    154       N6-acetyllysine (By similarity).
FT   MOD_RES     198    198       Phosphothreonine; by CDK1 and CDK2 (By
FT                                similarity).
FT   MOD_RES     211    211       N6-acetyllysine (By similarity).
FT   MOD_RES     217    217       Phosphothreonine; by CDK1 (By
FT                                similarity).
FT   MOD_RES     232    232       Phosphothreonine (By similarity).
FT   MOD_RES     232    232       Phosphothreonine; by CDK1 (By
FT                                similarity).
FT   MOD_RES     235    235       Phosphothreonine (By similarity).
FT   MOD_RES     235    235       Phosphothreonine; by CDK1 (By
FT                                similarity).
FT   MOD_RES     241    241       Phosphoserine (By similarity).
FT   MOD_RES     252    252       Phosphoserine.
FT   MOD_RES     255    255       N6-acetyllysine (By similarity).
FT   MOD_RES     258    258       Phosphoserine.
FT   MOD_RES     265    265       N6-acetyllysine (By similarity).
FT   MOD_RES     271    271       N6-acetyllysine (By similarity).
FT   MOD_RES     277    277       Phosphothreonine (By similarity).
FT   CROSSLNK    228    228       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    261    261       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
SQ   SEQUENCE   292 AA;  32560 MW;  E68750C549ED25E6 CRC64;
     MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG AGAKDELHIV
     EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL RLKCGSGPVH ISGQHLVAVE
     EDAESEDEDE EDVKLLGMSG KRSAPGGGNK VPQKKVKLDE DDEDDDEDDE DDEDDDDDDF
     DEEETEEKVP VKKSVRDTPA KNAQKSNQNG KDLKPSTPRS KGQESFKKQE KTPKTPKGPS
     SVEDIKAKMQ ASIEKGGSLP KVEAKFINYV KNCFRMTDQE AIQDLWQWRK SL
//
ID   PCBP2_MOUSE             Reviewed;         362 AA.
AC   Q61990; Q61383; Q62042;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Poly(rC)-binding protein 2;
DE   AltName: Full=Alpha-CP2;
DE   AltName: Full=CTBP;
DE            Short=CBP;
DE   AltName: Full=Putative heterogeneous nuclear ribonucleoprotein X;
DE            Short=hnRNP X;
GN   Name=Pcbp2; Synonyms=Cbp, Hnrnpx, Hnrpx;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX   MEDLINE=93376518; PubMed=8367306; DOI=10.1093/nar/21.16.3894;
RA   Hahm K.B., Kim G., Turch C., Smale S.T.;
RT   "Isolation of a murine gene encoding a nucleic acid-binding protein
RT   with homology to hnRNP K.";
RL   Nucleic Acids Res. 21:3894-3894(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE (ISOFORM 2).
RC   STRAIN=C57BL/6 X 129/Ola; TISSUE=Liver;
RX   MEDLINE=94268912; PubMed=8208614; DOI=10.1093/nar/22.10.1885;
RA   Goller M., Funke B., Gehe-Becker C., Kroeger B., Lottspeich F.,
RA   Horak I.;
RT   "Murine protein which binds preferentially to oligo-C-rich single-
RT   stranded nucleic acids.";
RL   Nucleic Acids Res. 22:1885-1889(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 3).
RC   STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RA   Horak I.;
RL   Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 1).
RX   MEDLINE=20396135; PubMed=10936052; DOI=10.1006/geno.2000.6244;
RA   Makeyev A.V., Liebhaber S.A.;
RT   "Identification of two novel mammalian genes establishes a subfamily
RT   of KH-domain RNA-binding proteins.";
RL   Genomics 67:301-316(2000).
CC   -!- FUNCTION: Single-stranded nucleic acid binding protein that binds
CC       preferentially to oligo dC. Major cellular poly(rC)-binding
CC       protein. Binds also poly(rU). Negatively regulates cellular
CC       antiviral responses mediated by MAVS signaling. It acts as an
CC       adapter between MAVS and the E3 ubiquitin ligase ITCH, therefore
CC       triggering MAVS ubiquitinationa and degradation (By similarity).
CC   -!- SUBUNIT: Identified in a mRNP complex, at least composed of DHX9,
CC       DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1,
CC       STAU2, SYNCRIP and YBX1. Interacts with IFIH1 and RNF135 (By
CC       similarity). Interacts with MAVS (via C-terminus) and ITCH (via WW
CC       domains) (By similarity).
CC   -!- INTERACTION:
CC       P97473:Tarbp2; NbExp=1; IntAct=EBI-644300, EBI-2644020;
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q61990-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q61990-2; Sequence=VSP_002820;
CC       Name=3;
CC         IsoId=Q61990-3; Sequence=VSP_002821;
CC   -!- SIMILARITY: Contains 3 KH domains.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; L19661; AAA03705.1; -; mRNA.
DR   EMBL; X75947; CAA53546.1; -; mRNA.
DR   EMBL; X97982; CAA66619.1; -; mRNA.
DR   EMBL; AF236845; AAK14059.1; -; Genomic_DNA.
DR   EMBL; AF236842; AAK14059.1; JOINED; Genomic_DNA.
DR   EMBL; AF236843; AAK14059.1; JOINED; Genomic_DNA.
DR   EMBL; AF236844; AAK14059.1; JOINED; Genomic_DNA.
DR   IPI; IPI00127707; -.
DR   IPI; IPI00221796; -.
DR   IPI; IPI00221799; -.
DR   PIR; S78515; S78515.
DR   RefSeq; NP_001096635.1; NM_001103165.1.
DR   RefSeq; NP_001096636.1; NM_001103166.1.
DR   RefSeq; NP_035172.2; NM_011042.2.
DR   UniGene; Mm.236513; -.
DR   ProteinModelPortal; Q61990; -.
DR   SMR; Q61990; 11-169, 283-355.
DR   IntAct; Q61990; 19.
DR   STRING; Q61990; -.
DR   PhosphoSite; Q61990; -.
DR   REPRODUCTION-2DPAGE; Q61990; -.
DR   PRIDE; Q61990; -.
DR   Ensembl; ENSMUST00000077037; ENSMUSP00000076294; ENSMUSG00000056851.
DR   Ensembl; ENSMUST00000078404; ENSMUSP00000077509; ENSMUSG00000056851.
DR   Ensembl; ENSMUST00000108838; ENSMUSP00000104466; ENSMUSG00000056851.
DR   GeneID; 18521; -.
DR   KEGG; mmu:18521; -.
DR   UCSC; uc007xvy.2; mouse.
DR   UCSC; uc007xvz.2; mouse.
DR   UCSC; uc009vat.1; mouse.
DR   CTD; 18521; -.
DR   MGI; MGI:108202; Pcbp2.
DR   GeneTree; ENSGT00550000074311; -.
DR   HOGENOM; HBG445439; -.
DR   HOVERGEN; HBG053520; -.
DR   InParanoid; Q61990; -.
DR   OMA; PRTLLDM; -.
DR   OrthoDB; EOG46WZ8K; -.
DR   PhylomeDB; Q61990; -.
DR   NextBio; 294276; -.
DR   ArrayExpress; Q61990; -.
DR   Bgee; Q61990; -.
DR   CleanEx; MM_PCBP2; -.
DR   Genevestigator; Q61990; -.
DR   GermOnline; ENSMUSG00000056851; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0050687; P:negative regulation of defense response to virus; ISS:UniProtKB.
DR   GO; GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0009615; P:response to virus; IEA:UniProtKB-KW.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR004088; KH_type_1.
DR   InterPro; IPR018111; KH_type_1_subgr.
DR   Pfam; PF00013; KH_1; 3.
DR   SMART; SM00322; KH; 3.
DR   PROSITE; PS50084; KH_TYPE_1; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Antiviral defense; Cytoplasm;
KW   Direct protein sequencing; DNA-binding; Immunity; Innate immunity;
KW   Nucleus; Phosphoprotein; Repeat; Ribonucleoprotein; RNA-binding.
FT   CHAIN         1    362       Poly(rC)-binding protein 2.
FT                                /FTId=PRO_0000050091.
FT   DOMAIN       13     75       KH 1.
FT   DOMAIN       97    162       KH 2.
FT   DOMAIN      284    348       KH 3.
FT   MOD_RES     169    169       Phosphoserine (By similarity).
FT   MOD_RES     183    183       Phosphoserine (By similarity).
FT   MOD_RES     185    185       Phosphoserine (By similarity).
FT   MOD_RES     232    232       Phosphotyrosine (By similarity).
FT   MOD_RES     268    268       Phosphoserine (By similarity).
FT   VAR_SEQ     194    224       Missing (in isoform 2).
FT                                /FTId=VSP_002820.
FT   VAR_SEQ     263    275       Missing (in isoform 3).
FT                                /FTId=VSP_002821.
SQ   SEQUENCE   362 AA;  38222 MW;  70C8AF710E3BF3C0 CRC64;
     MDTGVIEGGL NVTLTIRLLM HGKEVGSIIG KKGESVKKMR EESGARINIS EGNCPERIIT
     LAGPTNAIFK AFAMIIDKLE EDISSSMTNS TAASRPPVTL RLVVPASQCG SLIGKGGCKI
     KEIRESTGAQ VQVAGDMLPN STERAITIAG IPQSIIECVK QICVVMLESP PKGVTIPYRP
     KPSSSPVIFA GGQDRYSTGS DSASFPHTTP SMCLNPDLEG PPLEAYTIQG QYAIPQPDLT
     KLHQLAMQQS HFPMTHGNTG FSGIESSSPE VKGYWAGLDA SAQTTSHELT IPNDLIGCII
     GRQGAKINEI RQMSGAQIKI ANPVEGSTDR QVTITGSAAS ISLAQYLINV RLSSETGGMG
     SS
//
ID   CTR9_MOUSE              Reviewed;        1173 AA.
AC   Q62018; Q3UFF5; Q3UY40; Q66JX4; Q7TPS6; Q8BND9; Q8BRD1; Q8C9W7;
AC   Q8C9Y3; Q8CHI1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=RNA polymerase-associated protein CTR9 homolog;
DE   AltName: Full=SH2 domain-binding protein 1;
DE   AltName: Full=Tetratricopeptide repeat-containing, SH2-binding phosphoprotein of 150 kDa;
DE            Short=TPR-containing, SH2-binding phosphoprotein of 150 kDa;
DE            Short=p150TSP;
GN   Name=Ctr9; Synonyms=Kiaa0155, Sh2bp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP   PHOSPHORYLATION.
RC   TISSUE=Lymphoma;
RX   MEDLINE=96215125; PubMed=8636124; DOI=10.1074/jbc.271.12.6952;
RA   Malek S.N., Yang C.H., Earnshaw W.C., Kozak C.A., Desiderio S.;
RT   "p150TSP, a conserved nuclear phosphoprotein that contains multiple
RT   tetratricopeptide repeats and binds specifically to SH2 domains.";
RL   J. Biol. Chem. 271:6952-6962(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [LARGE
RP   SCALE MRNA] OF 1-955 (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Olfactory bulb, Pancreas, Spinal ganglion, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-936 (ISOFORM 1).
RC   STRAIN=129, and C3H/He; TISSUE=Mammary tumor, and Osteoblast;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 705-1173 (ISOFORM 3), AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925 AND SER-970, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1079; SER-1083 AND
RP   SER-1085, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925; SER-941; SER-943;
RP   SER-970; SER-1037; SER-1039 AND SER-1041, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q62018-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q62018-2; Sequence=VSP_017846, VSP_017847;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q62018-3; Sequence=VSP_017848, VSP_017849;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- SIMILARITY: Contains 16 TPR repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH53910.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 937;
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DR   EMBL; L49502; AAC42083.1; -; mRNA.
DR   EMBL; AK040205; BAC30540.1; -; mRNA.
DR   EMBL; AK040331; BAC30566.1; -; mRNA.
DR   EMBL; AK045101; BAC32223.1; -; mRNA.
DR   EMBL; AK083921; BAC39065.2; -; mRNA.
DR   EMBL; AK134990; BAE22373.1; -; mRNA.
DR   EMBL; AK148536; BAE28606.1; -; mRNA.
DR   EMBL; BC053910; AAH53910.1; ALT_SEQ; mRNA.
DR   EMBL; BC080719; AAH80719.1; -; mRNA.
DR   EMBL; AB093211; BAC41395.1; -; Transcribed_RNA.
DR   IPI; IPI00120919; -.
DR   IPI; IPI00461860; -.
DR   IPI; IPI00742373; -.
DR   PIR; T42719; T42719.
DR   RefSeq; NP_033457.2; NM_009431.2.
DR   UniGene; Mm.255858; -.
DR   ProteinModelPortal; Q62018; -.
DR   SMR; Q62018; 43-68, 117-268, 272-594, 629-760.
DR   IntAct; Q62018; 3.
DR   STRING; Q62018; -.
DR   PhosphoSite; Q62018; -.
DR   PRIDE; Q62018; -.
DR   Ensembl; ENSMUST00000005749; ENSMUSP00000005749; ENSMUSG00000005609.
DR   Ensembl; ENSMUST00000098103; ENSMUSP00000095707; ENSMUSG00000005609.
DR   GeneID; 22083; -.
DR   KEGG; mmu:22083; -.
DR   NMPDR; fig|10090.3.peg.17445; -.
DR   UCSC; uc009jfw.1; mouse.
DR   UCSC; uc009jfx.1; mouse.
DR   CTD; 22083; -.
DR   MGI; MGI:109345; Ctr9.
DR   GeneTree; ENSGT00390000005097; -.
DR   HOVERGEN; HBG081372; -.
DR   InParanoid; Q62018; -.
DR   OMA; QADAQFN; -.
DR   OrthoDB; EOG4NKBTV; -.
DR   PhylomeDB; Q62018; -.
DR   NextBio; 301916; -.
DR   ArrayExpress; Q62018; -.
DR   Bgee; Q62018; -.
DR   Genevestigator; Q62018; -.
DR   GermOnline; ENSMUSG00000005609; Mus musculus.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0042169; F:SH2 domain binding; IDA:MGI.
DR   InterPro; IPR001440; TPR-1.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 7.
DR   Pfam; PF00515; TPR_1; 4.
DR   SMART; SM00028; TPR; 9.
DR   PROSITE; PS50005; TPR; 10.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Nucleus; Phosphoprotein; Repeat; TPR repeat.
FT   CHAIN         1   1173       RNA polymerase-associated protein CTR9
FT                                homolog.
FT                                /FTId=PRO_0000231589.
FT   REPEAT       41     75       TPR 1.
FT   REPEAT      129    162       TPR 2.
FT   REPEAT      163    196       TPR 3.
FT   REPEAT      198    231       TPR 4.
FT   REPEAT      235    268       TPR 5.
FT   REPEAT      306    339       TPR 6.
FT   REPEAT      341    374       TPR 7.
FT   REPEAT      412    444       TPR 8.
FT   REPEAT      451    484       TPR 9.
FT   REPEAT      497    530       TPR 10.
FT   REPEAT      531    564       TPR 11.
FT   REPEAT      566    598       TPR 12.
FT   REPEAT      613    646       TPR 13.
FT   REPEAT      647    680       TPR 14.
FT   REPEAT      681    714       TPR 15.
FT   REPEAT      717    750       TPR 16.
FT   COMPBIAS    904    908       Poly-Gly.
FT   COMPBIAS    933    936       Poly-Lys.
FT   COMPBIAS    944    951       Poly-Glu.
FT   COMPBIAS    959    962       Poly-Arg.
FT   COMPBIAS    971    976       Poly-Glu.
FT   COMPBIAS   1015   1172       Ser-rich.
FT   MOD_RES     925    925       Phosphothreonine.
FT   MOD_RES     932    932       Phosphoserine (By similarity).
FT   MOD_RES     941    941       Phosphoserine.
FT   MOD_RES     943    943       Phosphoserine.
FT   MOD_RES     970    970       Phosphoserine.
FT   MOD_RES    1015   1015       Phosphoserine (By similarity).
FT   MOD_RES    1016   1016       Phosphoserine (By similarity).
FT   MOD_RES    1017   1017       Phosphoserine (By similarity).
FT   MOD_RES    1020   1020       Phosphoserine (By similarity).
FT   MOD_RES    1021   1021       Phosphoserine (By similarity).
FT   MOD_RES    1037   1037       Phosphoserine.
FT   MOD_RES    1039   1039       Phosphoserine.
FT   MOD_RES    1041   1041       Phosphoserine.
FT   MOD_RES    1079   1079       Phosphoserine.
FT   MOD_RES    1083   1083       Phosphoserine.
FT   MOD_RES    1085   1085       Phosphoserine.
FT   VAR_SEQ     704    721       YENCLRKFYKHQNTEVVL -> VTSLLLRIVACNVEPWLP
FT                                (in isoform 2).
FT                                /FTId=VSP_017846.
FT   VAR_SEQ     722   1173       Missing (in isoform 2).
FT                                /FTId=VSP_017847.
FT   VAR_SEQ     816    860       Missing (in isoform 3).
FT                                /FTId=VSP_017848.
FT   VAR_SEQ     995   1032       Missing (in isoform 3).
FT                                /FTId=VSP_017849.
FT   CONFLICT    144    144       K -> Q (in Ref. 1; AAC42083).
FT   CONFLICT    223    223       R -> S (in Ref. 3; AAH53910).
FT   CONFLICT    242    242       E -> Q (in Ref. 2; BAC32223).
FT   CONFLICT    390    390       D -> Y (in Ref. 3; AAH53910).
FT   CONFLICT    719    719       V -> I (in Ref. 2; BAE22373).
FT   CONFLICT    877    877       Q -> R (in Ref. 3; AAH80719).
FT   CONFLICT    900    900       E -> K (in Ref. 3; AAH80719).
SQ   SEQUENCE   1173 AA;  133408 MW;  2FB84564F1BEFD79 CRC64;
     MSRGSIEIPL RDTDEVIELD FDQLPEGDEV ISILKQEHTQ LHIWIALALE YYKQGKTEEF
     VKLLEAARID GNLDYRDHEK DQMTCLDTLA AYYVQQARKE KNKDNKKDLI TQATLLYTMA
     DKIIMYDQNH LLGRACFCLL EGDKMDQADA QFHFVLNQSP NNIPALLGKA CISFNKKDYR
     GALAYYKKAL RTNPGCPAEV RLGMGHCFVK LNKLEKARLA FSRALELNSK CVGALVGLAV
     LELNNKEADS IKNGVQLLSR AYTIDPSNPM VLNHLANHFF FKKDYSKVQH LALHAFHNTE
     VEAMQAESCY QLARSFHVQE DYDQAFQYYY QATQFASSSF VLPFFGLGQM YIYRGDKENA
     SQCFEKVLKA YPNNYETMKI LGSLYAASED QEKRDIAKGH LKKVTEQYPD DVEAWIELAQ
     ILEQTDIQGA LSAYGTATRI LQEKVQADVP PEILNNVGAL HFRLGNLGEA KKYFLASLDR
     AKAEAEHDEH YYNAISVTTS YNLARLYEAM CEFHEAEKLY KNILREHPNY VDCYLRLGAM
     ARDKGNFYEA SDWFKEALQI NQDHPDAWSL IGNLHLAKQE WGPGQKKFER ILKQPATQSD
     TYSMLALGNV WLQTLHQPTR DREKEKRHQD RALAIYKQVL RNDAKNLYAA NGIGAVLAHK
     GYFREARDVF AQVREATADI SDVWLNLAHI YVEQKQYISA VQMYENCLRK FYKHQNTEVV
     LYLARALFKC GKLQECKQTL LKARHVAPSD TVLMFNVALV LQRLATSVLK DEKSNLKEVL
     NAVKELELAH RYFSYLSKVG DKMRFDLALA ASEARQCSDL LSQAQYHVAR ARKQDEEERE
     LRAKQEQEKE LLRQKLLKEQ EEKRLREKEE QKKLLEQRAQ YVEKTKNILM FTGETEATKE
     KKRGGGGGRR SKKGGEFDEF VNDDTDDDLP VSKKKKRRKG SGSEQEGEEE EGGERKKKRR
     RRPPKGEEGS EEEETENGPK PKKRRPPRAE KKKAPKPERL PPSMKGKIKS KAIISSSDDS
     SDEDKLKIAD EGHPRNSNSD SDDDERPNRR ASSESDSDDN QNKSGSEAGS PRRSGRQESD
     EDSDSDQPSR KRRRSGSEQS DNESVQSGRS PSGASENEND SRPASPSAES DHESEQGSDN
     EGSGQGSGNE SEPEGSNNEA SDRGSEHGSD DSD
//
ID   AZI1_MOUSE              Reviewed;        1060 AA.
AC   Q62036;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-FEB-2011, entry version 70.
DE   RecName: Full=5-azacytidine-induced protein 1;
DE   AltName: Full=Pre-acrosome localization protein 1;
GN   Name=Azi1; Synonyms=Az1, Azi;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=96096715; PubMed=8529672;
RX   DOI=10.1111/j.1432-1033.1995.008_c.x;
RA   Aoto H., Tsuchida J., Nishina Y., Nishimune Y., Asano A., Tajima S.;
RT   "Isolation of a novel cDNA that encodes a protein localized to the
RT   pre-acrosome region of spermatids.";
RL   Eur. J. Biochem. 234:8-15(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=97224496; PubMed=9070930; DOI=10.1006/geno.1996.4546;
RA   Aoto H., Miyake Y., Nakamura M., Tajima S.;
RT   "Genomic organization of the mouse AZ1 gene that encodes the protein
RT   localized to preacrosomes of spermatids.";
RL   Genomics 40:138-141(1997).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-79, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May play a role in spermatogenesis.
CC   -!- TISSUE SPECIFICITY: Localized to the pre-acrosome region of round
CC       and elongated spermatids in testis but also present in ovary,
CC       brain and adipose tissue.
CC   -!- DEVELOPMENTAL STAGE: Significant amounts are found in the testis
CC       of 16 day old mice, at a late stage of pachytene spermatocytes
CC       when meiosis occurs. The level increases thereafter.
CC   -!- INDUCTION: By 5-azacytidine.
CC   -!- SIMILARITY: Contains 1 IQ domain.
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DR   EMBL; D43921; BAA07868.1; -; mRNA.
DR   EMBL; D88509; BAA19002.1; -; Genomic_DNA.
DR   IPI; IPI00226228; -.
DR   PIR; S63993; S63993.
DR   RefSeq; NP_033864.3; NM_009734.3.
DR   UniGene; Mm.2556; -.
DR   ProteinModelPortal; Q62036; -.
DR   STRING; Q62036; -.
DR   PhosphoSite; Q62036; -.
DR   PRIDE; Q62036; -.
DR   Ensembl; ENSMUST00000106229; ENSMUSP00000101836; ENSMUSG00000039781.
DR   GeneID; 12009; -.
DR   KEGG; mmu:12009; -.
DR   UCSC; uc007mrp.1; mouse.
DR   CTD; 12009; -.
DR   MGI; MGI:107440; Azi1.
DR   eggNOG; roNOG11305; -.
DR   GeneTree; ENSGT00390000001758; -.
DR   HOGENOM; HBG283708; -.
DR   HOVERGEN; HBG024371; -.
DR   InParanoid; Q62036; -.
DR   NextBio; 280207; -.
DR   ArrayExpress; Q62036; -.
DR   Bgee; Q62036; -.
DR   CleanEx; MM_AZI1; -.
DR   Genevestigator; Q62036; -.
DR   GermOnline; ENSMUSG00000039781; Mus musculus.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0007283; P:spermatogenesis; TAS:UniProtKB.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   SMART; SM00015; IQ; 1.
DR   PROSITE; PS50096; IQ; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Developmental protein; Differentiation; Phosphoprotein;
KW   Spermatogenesis.
FT   CHAIN         1   1060       5-azacytidine-induced protein 1.
FT                                /FTId=PRO_0000064782.
FT   DOMAIN      263    283       IQ.
FT   MOD_RES      47     47       Phosphoserine (By similarity).
FT   MOD_RES      52     52       Phosphoserine (By similarity).
FT   MOD_RES      76     76       Phosphoserine (By similarity).
FT   MOD_RES      78     78       Phosphoserine (By similarity).
FT   MOD_RES      79     79       Phosphothreonine.
FT   MOD_RES      89     89       Phosphoserine (By similarity).
FT   MOD_RES     105    105       Phosphoserine (By similarity).
FT   MOD_RES     114    114       Phosphoserine (By similarity).
FT   MOD_RES     150    150       Phosphoserine (By similarity).
SQ   SEQUENCE   1060 AA;  120343 MW;  470E2DE65DF0282A CRC64;
     MKGSRTITAT PEGSPEAVDL SLIGLPPPMS QRPGSASATR SIFRSMSVAT GSEPRKKALE
     ATGPGGPRAI NNLRRSNSTT QVNQSWTGSP RPAEPTDFLM LFEGSTSGRR RVASLSKASS
     EKEATWNVLD EQPRGLALPA SAQSPSTLDS ALGPRRKECP LAPSFTANNR SNKGAVGNCV
     TTMVHNHYAS SKMVSPPKSS NQTAPSLNNI VKAAAREGGE GSDLGKPRKN LSSASQSARG
     TTGLLRRREV TEEEAERFIH QVNQAAVTIQ RWYRCQVQRR RAGAAALEHL LASKREGQRQ
     RLGGGNLLEL HRQEEAARKK AREEKARQAR QAAIQELQQK RAQKASEAEH RRPKDRPETR
     APEQPRPMQE PGCVTHPKAN NAGASIYPTG PADPCPPASE SSPEQWQSPE DKPQDIHSQG
     EARQDLAVSG SSRGKARARA TLDDLLDTLK LLEEEPEPLP HPKAYHKDRY AWTDEEEDAN
     SLTADNLEKF GKLSAAPGPP DDGTLLSEAK LQSIMTFLDE MEKSGQERPA PWRESLVLEA
     GSGSEGSTSV MRLKLELEEK KQAMALLQRA LAQQRDLTVR RVKETEKELT RQLRQQKEQY
     EATIQRHLSF IDQLIEDKKV LSEKCEAVVA ELKHGDQRCR ERVAQMQEQH ELEIKKLKEL
     MSATEKIRRE KWINEKTKKI KEITVRGLEP EIQKLIAKHK QEVRRLRGLH EAELQQREEQ
     AAQRHLRQAE ELRQHLDRER EVLGQQERER AQQRFEQHLE QEQRALEQQR RRLYNEVAEE
     KERLGQQAAR QRAELEELRQ QLEESSAALT RALRAEFERS REEQERRHQM ELKALKDQLE
     AERQAWVASC AKKEEAWLLT RERELKEEIR KGRDQEIELV IHRLEADMTL AKEESERAAE
     SRVKRVRDKY ETELSELEQS ERKLQERCSE LKGRLGEAEG EKERLQSLVR QKEKELEDLR
     AVNTQMCSER ASLAQVVRQE FAEQLAASQE ETQRVKVELA ELQARQQVEL DEVHRRVKTA
     LARKEAAVNS LRKQHEAAVK RADHLEELLE QHKGSSLSSK
//
ID   Q62043_MOUSE            Unreviewed;       935 AA.
AC   Q62043;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   SubName: Full=Pyruvate carboxylase;
DE   Flags: Fragment;
GN   Name=Pcx;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c; TISSUE=Liver;
RA   Leiter E.H.;
RL   Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; M97957; AAA39897.1; -; mRNA.
DR   IPI; IPI00114710; -.
DR   UniGene; Mm.1845; -.
DR   HSSP; P24182; 1DV1.
DR   ProteinModelPortal; Q62043; -.
DR   STRING; Q62043; -.
DR   Ensembl; ENSMUST00000068004; ENSMUSP00000063825; ENSMUSG00000024892.
DR   Ensembl; ENSMUST00000113825; ENSMUSP00000109456; ENSMUSG00000024892.
DR   MGI; MGI:97520; Pcx.
DR   HOVERGEN; HBG008340; -.
DR   InParanoid; Q62043; -.
DR   ArrayExpress; Q62043; -.
DR   Bgee; Q62043; -.
DR   Genevestigator; Q62043; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CarbamoylP_synth_lsu_ATP-bd.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR005930; Pyruv_COase.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF02436; PYC_OADA; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51230; Hybrid_motif; 1.
DR   SUPFAM; SSF51246; Rudmnt_hyb_motif; 1.
DR   TIGRFAMs; TIGR01235; pyruv_carbox; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   2: Evidence at transcript level;
KW   Biotin; Pyruvate.
FT   NON_TER       1      1
SQ   SEQUENCE   935 AA;  103106 MW;  A335A36EA0AAEF6F CRC64;
     HIEVQILGDQ YGNILHLYER DCSIQRRHQK VVEIAPATHL DPQLRSRLTS DSVKLAKQVG
     YENAGTVEFL VDKHGKHYFI EVNSRLQVEH TVTEEITDVD LVHAQIHVSE GRSLPDLGLR
     QENIRINGCA IQCRVTTEDP ARSFQPDTGR IEVFRSGEGM GIRLDNASAF QGAVISPHYD
     SLLVKVIAHG KDHPTAATKM SRALAEFRVR GVKTNIPFLQ NVLNNQQFLA GTVDTQFIDE
     NPELFQLRPA QNRAQKLLHY LGHVMVNGPT TPIPVNVSPS PVDPAVPVVP IGPPPAGFRD
     ILLREGPEGF ARAVRNHQGL LLMDTTFRDA HQSLLATRVR THDLKKIAPY VAHNFNKLFS
     MENWGGATFD VAMRFLYECP WRRLQELREL IPNIPFQMLL RGANAVGYTN YPDNVVFKFC
     EVAKENGMDV FRVFDSLNYL PNMLLGMEAA GSAGGVVEAA ISYTGDLADP SRTKYSLEYY
     MGLAEELVRA GTHILCIKDM AGLLKPAACT MLVSSLRDRF PDLPLHIHTH DTSGAGVAAM
     LACAQAGADV VDVAVDSMSG MTSQPSMGAL VACTKGTPLD TEVPLERVFD YSEYWEGARG
     LYAAFDCTAT MKSGNSDVYE NEIPGGQYTN LHFQAHSMGL GSKFKEVKKA YVEANQMLGD
     LIKVTPSSKI VGDLAQFMVQ NGCSRAEARS SGRRAVLPPL CGGVPAGLHW HSPWGFPEPF
     RSKVLKDLPR IEGRPGASLP PLNLKELEKD LIDRHGEEVT PEDVLSAAMY PDVFAQFKDF
     TATFGPLDSL NTRLFLQGPK IAEEFEVELE RGKTLHIKAL AVSDLNRAGQ RQVFFELNGQ
     LRSILVKDTQ AMKEMHFHPK ALKDVKGQIG APMPGKVIDI KVAAGDKVAK GQPLCVLSAM
     KMETVVTSPM EGTIRKVHVT KDMTLEGDDL ILEIE
//
ID   PEA15_MOUSE             Reviewed;         130 AA.
AC   Q62048; Q3U5N7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Astrocytic phosphoprotein PEA-15;
DE   AltName: Full=15 kDa phosphoprotein enriched in astrocytes;
GN   Name=Pea15; Synonyms=Pea15a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND PARTIAL PROTEIN
RP   SEQUENCE.
RC   STRAIN=Swiss; TISSUE=Astrocyte;
RX   MEDLINE=96278966; PubMed=8662970; DOI=10.1074/jbc.271.25.14800;
RA   Estelles A., Yokoyama M., Nothias F., Vincent J.-D., Glowinski J.,
RA   Vernier P., Chneiweiss H.;
RT   "The major astrocytic phosphoprotein PEA-15 is encoded by two mRNAs
RT   conserved on their full length in mouse and human.";
RL   J. Biol. Chem. 271:14800-14806(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX   MEDLINE=21077541; PubMed=11210189; DOI=10.1007/s003350010243;
RA   Underhill D.A., Vogan K.J., Underhill T.M., Gros P.;
RT   "Identification of a novel, alternatively spliced isoform and single
RT   nucleotide polymorphisms in the murine Pea-15 gene.";
RL   Mamm. Genome 12:172-174(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Cerebellum, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 58-71, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [6]
RP   FUNCTION, PHOSPHORYLATION AT SER-104 AND SER-116, AND MUTAGENESIS OF
RP   SER-104 AND SER-116.
RX   MEDLINE=20057753; PubMed=10588860; DOI=10.1006/dbio.1999.9510;
RA   Estelles A., Charlton C.A., Blau H.M.;
RT   "The phosphoprotein protein PEA-15 inhibits Fas- but increases TNF-R1-
RT   mediated caspase-8 activity and apoptosis.";
RL   Dev. Biol. 216:16-28(1999).
RN   [7]
RP   INTERACTION WITH PLD1 AND PLD2, AND SUBCELLULAR LOCATION.
RX   PubMed=10926929; DOI=10.1074/jbc.M003329200;
RA   Zhang Y., Redina O., Altshuller Y.M., Yamazaki M., Ramos J.,
RA   Chneiweiss H., Kanaho Y., Frohman M.A.;
RT   "Regulation of expression of phospholipase D1 and D2 by PEA-15, a
RT   novel protein that interacts with them.";
RL   J. Biol. Chem. 275:35224-35232(2000).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 AND SER-116, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND SER-116, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Blocks Ras-mediated inhibition of integrin activation
CC       and modulates the ERK MAP kinase cascade. Inhibits RPS6KA3
CC       activities by retaining it in the cytoplasm. Inhibits both
CC       TNFRSF6- and TNFRSF1A-mediated CASP8 activity and apoptosis.
CC       Regulates glucose transport by controlling both the content of
CC       SLC2A1 glucose transporters on the plasma membrane and the
CC       insulin-dependent trafficking of SLC2A4 from the cell interior to
CC       the surface (By similarity).
CC   -!- SUBUNIT: Binds RPS6KA3, MAPK3 and MAPK1. Interacts with CASP8 and
CC       FADD (By similarity). Transient interaction with PLD1 and PLD2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Associated with
CC       microtubules.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q62048-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q62048-2; Sequence=VSP_007736, VSP_007737;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in the brain. Low
CC       levels in some peripheral organs.
CC   -!- PTM: Phosphorylated by protein kinase C and calcium-calmodulin-
CC       dependent protein kinase. These phosphorylation events are
CC       modulated by neurotransmitters or hormones.
CC   -!- MISCELLANEOUS: Increases PLD1 and PLD2 levels, possibly by
CC       stabilizing the protein.
CC   -!- SIMILARITY: Contains 1 DED (death effector) domain.
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DR   EMBL; X86694; CAA60387.1; -; Genomic_DNA.
DR   EMBL; AK089070; BAC40734.1; -; mRNA.
DR   EMBL; AK153141; BAE31752.1; -; mRNA.
DR   EMBL; AK153493; BAE32041.1; -; mRNA.
DR   EMBL; AK161635; BAE36504.1; -; mRNA.
DR   EMBL; AK161977; BAE36662.1; -; mRNA.
DR   EMBL; BC038282; AAH38282.1; -; mRNA.
DR   IPI; IPI00121013; -.
DR   IPI; IPI00336400; -.
DR   PIR; S55385; S55385.
DR   RefSeq; NP_035193.1; NM_011063.2.
DR   UniGene; Mm.544; -.
DR   ProteinModelPortal; Q62048; -.
DR   SMR; Q62048; 1-130.
DR   STRING; Q62048; -.
DR   PhosphoSite; Q62048; -.
DR   PRIDE; Q62048; -.
DR   Ensembl; ENSMUST00000013842; ENSMUSP00000013842; ENSMUSG00000013698.
DR   GeneID; 18611; -.
DR   KEGG; mmu:18611; -.
DR   UCSC; uc007dpy.1; mouse.
DR   CTD; 18611; -.
DR   MGI; MGI:104799; Pea15a.
DR   eggNOG; roNOG16274; -.
DR   GeneTree; ENSGT00390000000230; -.
DR   HOGENOM; HBG716590; -.
DR   HOVERGEN; HBG053557; -.
DR   InParanoid; Q62048; -.
DR   OMA; CKEDIPE; -.
DR   OrthoDB; EOG4229M2; -.
DR   PhylomeDB; Q62048; -.
DR   NextBio; 294542; -.
DR   ArrayExpress; Q62048; -.
DR   Bgee; Q62048; -.
DR   CleanEx; MM_PEA15A; -.
DR   Genevestigator; Q62048; -.
DR   GermOnline; ENSMUSG00000013698; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005624; C:membrane fraction; TAS:MGI.
DR   GO; GO:0005875; C:microtubule associated complex; NAS:UniProtKB.
DR   GO; GO:0005080; F:protein kinase C binding; TAS:MGI.
DR   GO; GO:0006915; P:apoptosis; IDA:UniProtKB.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   GO; GO:0046325; P:negative regulation of glucose import; ISS:UniProtKB.
DR   GO; GO:0042981; P:regulation of apoptosis; IDA:UniProtKB.
DR   InterPro; IPR011029; DEATH-like.
DR   InterPro; IPR001875; DED.
DR   Gene3D; G3DSA:1.10.533.10; DEATH_like; 1.
DR   Pfam; PF01335; DED; 1.
DR   SMART; SM00031; DED; 1.
DR   SUPFAM; SSF47986; DEATH_like; 1.
DR   PROSITE; PS50168; DED; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Cytoplasm; Direct protein sequencing;
KW   Phosphoprotein; Sugar transport; Transport.
FT   CHAIN         1    130       Astrocytic phosphoprotein PEA-15.
FT                                /FTId=PRO_0000191283.
FT   DOMAIN        3     81       DED.
FT   REGION       98    107       Microtubule-binding (Potential).
FT   REGION      122    129       Microtubule-binding (Potential).
FT   MOD_RES       6      6       Phosphothreonine (By similarity).
FT   MOD_RES      25     25       Phosphoserine (By similarity).
FT   MOD_RES      61     61       Phosphoserine.
FT   MOD_RES     104    104       Phosphoserine; by PKC.
FT   MOD_RES     108    108       Phosphotyrosine (By similarity).
FT   MOD_RES     116    116       Phosphoserine; by CaMK2.
FT   VAR_SEQ      36     57       Missing (in isoform 2).
FT                                /FTId=VSP_007736.
FT   VAR_SEQ      58     58       D -> N (in isoform 2).
FT                                /FTId=VSP_007737.
FT   MUTAGEN     104    104       S->A: Abolishes inhibitory effect on FAS-
FT                                mediated apoptosis. Does not change
FT                                effect on TNFRSF1A-mediated apoptosis.
FT   MUTAGEN     116    116       S->A: Abolishes inhibitory effect on FAS-
FT                                mediated apoptosis. Does not change
FT                                effect on TNFRSF1A-mediated apoptosis.
SQ   SEQUENCE   130 AA;  15054 MW;  780F93A40B2834A8 CRC64;
     MAEYGTLLQD LTNNITLEDL EQLKSACKED IPSEKSEEIT TGSAWFSFLE SHNKLDKDNL
     SYIEHIFEIS RRPDLLTMVV DYRTRVLKIS EEEELDTKLT RIPSAKKYKD IIRQPSEEEI
     IKLAPPPKKA
//
ID   CSPG2_MOUSE             Reviewed;        3357 AA.
AC   Q62059; Q62058; Q9CUU0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 2.
DT   08-MAR-2011, entry version 109.
DE   RecName: Full=Versican core protein;
DE   AltName: Full=Chondroitin sulfate proteoglycan core protein 2;
DE            Short=Chondroitin sulfate proteoglycan 2;
DE   AltName: Full=Large fibroblast proteoglycan;
DE   AltName: Full=PG-M;
DE   Flags: Precursor;
GN   Name=Vcan; Synonyms=Cspg2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS V0; V1 AND V2).
RC   STRAIN=C57BL/6, and Swiss Webster; TISSUE=Brain, and Endothelial cell;
RX   MEDLINE=95122551; PubMed=7822336; DOI=10.1074/jbc.270.2.958;
RA   Ito K., Shinomura T., Zako M., Ujita M., Kimata K.;
RT   "Multiple forms of mouse PG-M, a large chondroitin sulfate
RT   proteoglycan generated by alternative splicing.";
RL   J. Biol. Chem. 270:958-965(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM V3).
RC   STRAIN=C57BL/6; TISSUE=Endothelial cell;
RX   MEDLINE=95181355; PubMed=7876137; DOI=10.1074/jbc.270.8.3914;
RA   Zako M., Shinomura T., Ujita M., Ito K., Kimata K.;
RT   "Expression of PG-M(V3), an alternatively spliced form of PG-M without
RT   a chondroitin sulfate attachment in region in mouse and human
RT   tissues.";
RL   J. Biol. Chem. 270:3914-3918(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1691 (ISOFORM V1).
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PROTEIN SEQUENCE OF 277-288, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   INTERACTION WITH FBLN1.
RX   MEDLINE=99329059; PubMed=10400671; DOI=10.1074/jbc.274.29.20444;
RA   Aspberg A., Adam S., Kostka G., Timpl R., Heinegaard D.;
RT   "Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and
RT   versican.";
RL   J. Biol. Chem. 274:20444-20449(1999).
CC   -!- FUNCTION: May play a role in intercellular signaling and in
CC       connecting cells with the extracellular matrix. May take part in
CC       the regulation of cell motility, growth and differentiation. Binds
CC       hyaluronic acid.
CC   -!- SUBUNIT: Interacts with FBLN1.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Additional isoforms seem to exist;
CC       Name=V0;
CC         IsoId=Q62059-1; Sequence=Displayed;
CC       Name=V1;
CC         IsoId=Q62059-2; Sequence=VSP_003087, VSP_003088;
CC       Name=V2;
CC         IsoId=Q62059-3; Sequence=VSP_003089;
CC       Name=V3;
CC         IsoId=Q62059-4; Sequence=VSP_003087, VSP_003090;
CC   -!- TISSUE SPECIFICITY: Isoform V2 is found only in brain.
CC   -!- DEVELOPMENTAL STAGE: Disappears after the cartilage development.
CC   -!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
CC   -!- SIMILARITY: Contains 1 C-type lectin domain.
CC   -!- SIMILARITY: Contains 2 EGF-like domains.
CC   -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 2 Link domains.
CC   -!- SIMILARITY: Contains 1 Sushi (CCP/SCR) domain.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=Versican;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_157";
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DR   EMBL; D16263; BAA03796.1; -; mRNA.
DR   EMBL; D28599; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; D32040; BAA06802.1; -; mRNA.
DR   EMBL; AK014525; BAB29411.3; -; mRNA.
DR   IPI; IPI00121038; -.
DR   IPI; IPI00230441; -.
DR   IPI; IPI00469172; -.
DR   IPI; IPI00469565; -.
DR   PIR; A55535; A55535.
DR   UniGene; Mm.158700; -.
DR   UniGene; Mm.410783; -.
DR   ProteinModelPortal; Q62059; -.
DR   SMR; Q62059; 27-148, 151-248, 252-349, 3050-3319.
DR   STRING; Q62059; -.
DR   PhosphoSite; Q62059; -.
DR   PRIDE; Q62059; -.
DR   Ensembl; ENSMUST00000022114; ENSMUSP00000022114; ENSMUSG00000021614.
DR   Ensembl; ENSMUST00000109543; ENSMUSP00000105170; ENSMUSG00000021614.
DR   Ensembl; ENSMUST00000109544; ENSMUSP00000105171; ENSMUSG00000021614.
DR   Ensembl; ENSMUST00000109545; ENSMUSP00000105172; ENSMUSG00000021614.
DR   UCSC; uc007rjg.1; mouse.
DR   UCSC; uc007rjh.1; mouse.
DR   MGI; MGI:102889; Vcan.
DR   GeneTree; ENSGT00550000074236; -.
DR   HOVERGEN; HBG051140; -.
DR   OrthoDB; EOG4G4GPG; -.
DR   ArrayExpress; Q62059; -.
DR   Bgee; Q62059; -.
DR   CleanEx; MM_VCAN; -.
DR   Genevestigator; Q62059; -.
DR   GermOnline; ENSMUSG00000021614; Mus musculus.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005540; F:hyaluronic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0005529; F:sugar binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0001657; P:ureteric bud development; IEP:UniProtKB.
DR   InterPro; IPR001304; C-type_lectin.
DR   InterPro; IPR016186; C-type_lectin-like.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; C-type_lectin_fold.
DR   InterPro; IPR016060; Complement_control_module.
DR   InterPro; IPR006209; EGF.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR001881; EGF_Ca-bd.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR000538; Link.
DR   InterPro; IPR000436; Sushi_SCR_CCP.
DR   Gene3D; G3DSA:3.10.100.10; C-type_lectin-like; 3.
DR   Gene3D; G3DSA:2.10.70.10; Complement_control_module; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF00084; Sushi; 1.
DR   Pfam; PF07686; V-set; 1.
DR   Pfam; PF00193; Xlink; 2.
DR   PRINTS; PR01265; LINKMODULE.
DR   SMART; SM00032; CCP; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00445; LINK; 2.
DR   SUPFAM; SSF56436; C-type_lectin_fold; 3.
DR   SUPFAM; SSF57535; Complement_control_module; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS01241; LINK_1; 2.
DR   PROSITE; PS50963; LINK_2; 2.
DR   PROSITE; PS50923; SUSHI; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Direct protein sequencing;
KW   Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein;
KW   Hyaluronic acid; Immunoglobulin domain; Lectin; Proteoglycan; Repeat;
KW   Secreted; Signal; Sushi.
FT   SIGNAL        1     23       Potential.
FT   CHAIN        24   3357       Versican core protein.
FT                                /FTId=PRO_0000017523.
FT   DOMAIN       24    146       Ig-like V-type.
FT   DOMAIN      150    245       Link 1.
FT   DOMAIN      251    347       Link 2.
FT   DOMAIN     3051   3087       EGF-like 1.
FT   DOMAIN     3089   3125       EGF-like 2; calcium-binding (Potential).
FT   DOMAIN     3138   3252       C-type lectin.
FT   DOMAIN     3256   3316       Sushi.
FT   REGION      348   1308       GAG-alpha (glucosaminoglycan attachment
FT                                domain).
FT   REGION     1309   3051       GAG-beta.
FT   CARBOHYD     57     57       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    330    330       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    351    351       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    441    441       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    807    807       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    914    914       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    951    951       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1305   1305       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1371   1371       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1678   1678       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2053   2053       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2243   2243       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2361   2361       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2626   2626       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3029   3029       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3331   3331       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3341   3341       N-linked (GlcNAc...) (Potential).
FT   DISULFID     44    130       By similarity.
FT   DISULFID    172    243       By similarity.
FT   DISULFID    196    217       By similarity.
FT   DISULFID    270    333       By similarity.
FT   DISULFID    294    315       By similarity.
FT   DISULFID   3055   3066       By similarity.
FT   DISULFID   3060   3075       By similarity.
FT   DISULFID   3077   3086       By similarity.
FT   DISULFID   3093   3104       By similarity.
FT   DISULFID   3098   3113       By similarity.
FT   DISULFID   3115   3124       By similarity.
FT   DISULFID   3131   3142       By similarity.
FT   DISULFID   3159   3251       By similarity.
FT   DISULFID   3227   3243       By similarity.
FT   DISULFID   3258   3301       By similarity.
FT   DISULFID   3287   3314       By similarity.
FT   VAR_SEQ     348    348       P -> R (in isoform V1 and isoform V3).
FT                                /FTId=VSP_003087.
FT   VAR_SEQ     349   3051       Missing (in isoform V3).
FT                                /FTId=VSP_003090.
FT   VAR_SEQ     349   1308       Missing (in isoform V1).
FT                                /FTId=VSP_003088.
FT   VAR_SEQ    1309   3051       Missing (in isoform V2).
FT                                /FTId=VSP_003089.
FT   CONFLICT    126    126       A -> G (in Ref. 3).
FT   CONFLICT   1657   1657       I -> T (in Ref. 3).
FT   CONFLICT   1673   1679       TVWNSNS -> QFGIQTA (in Ref. 3).
SQ   SEQUENCE   3357 AA;  366787 MW;  AE82A0D942B8323A CRC64;
     MLINMKGILW MCSTLLLTHA LHQAKMETSP PVKGSLSGKV VLPCHFSTLP TLPPNYNTSE
     FLRIKWSKME VDKNGKDIKE TTVLVAQNGN IKIGQDYKGR VSVPTHPDDV GDASLTMVKL
     RASDAAVYRC DVMYGIEDTQ DTMSLAVDGV VFHYRAATSR YTLNFAAAQQ ACLDIGAVIA
     SPEQLFAAYE DGFEQCDAGW LSDQTVRYPI RAPREGCYGD MMGKEGVRTY GFRSPQETYD
     VYCYVDHLDG DVFHITAPSK FTFEEAEAEC TSRDARLATV GELQAAWRNG FDQCDYGWLS
     DASVRHPVTV ARAQCGGGLL GVRTLYRFEN QTCFPLPDSR FDAYCFKPKQ NISEATTIEM
     NILAETSSPS LSKEPHMVPD RATPVIPLAT ELPIFTTHFP PAGNIVNSEQ KSVVYSQAIT
     GRLATESPTT TRNTINSWDL NDSLASGSGP LGMPDISEIK EEELRSTTVI SQHATGSQAV
     ITEDTQTHES VSQIEQIEVG PLVTSMEITN HISLKELPEK NKTPYESTEV TLEHTTEMPT
     VSASPELATT SHYGFTLRED DREDRTLTVR SDQSTRVFSQ IPEVITVSKT SEDTTYSQLG
     DLESISTSTI TMLGTDRSLI DKEKEPKTNG KVTEDEFGQS QPTTTFPSQH LTEVELLPYS
     GDTTSVEGIS TVIYPSLQTD VTQGRERTET PRPELKKDPY TVDEIPEKVT KDPFIGKTEE
     VFSGMPLSTS SSESSVERTE SVSPALTIEK LTGKPTEARD VEEMTTLTRL ETDVTKSDKD
     VTRVHLTHST LNVEVVTVSK WPGDEDNSTS KPLPSTEHAG FTKLPPVPLS TIGINGKDKE
     IPSFTDGGGE YTLFPDGTPK PLEKVSEEDL ASGELTVTFH TSTSIGSAEK SASGEPTTGD
     RFLPTTSTED QVINATAEGS ALGEDTEASK PLFTGPPFVH TSDVEELAFV NYSSTQEPTT
     YVDISHTSPL SIIPKTEWSV LETSVPLEDE ILGKSDQDIL EQTHLEATMS PGALRTTGVS
     QGETQEEPQT PGSPFPTFSS TAVMAKETTA FEEGEGSTYT PSEGRLMTGS ERVPGLETTP
     VGTSYPPGAI TDQEVEMDTM VTLMSTIRPT VVSSTESEVI YEAEGSSPTE FASTLRPFQT
     HVTQLMEETT EEGKKASLDY TDLGSGLFEP RATELPKFPS TPSDISVFTA IDSLHRTPPL
     SPSSSFTEEQ RVFEEESSEK TTGDILPGES VTQHPVTTLI DIVAMKTESD IDHMTSKPPV
     TQPTRPSVVE RKTTSKTQEL STSTPAAGTK FHPDINVYII EVRENKTGRL SDMIVSGHPI
     DSESKEEEPC SEETDPLHDL FAEILPELPD SFEIDIYHSE EDEDGEEDCV NATDVTTTPS
     VQYINGKQLV TTVPKDPEAA EARRGQYESV APSQNFPDSS ATDTHQFILA ETESSTTMQF
     KKSKEGTELL EITWKPETYP ETPDHVSSGE PDVFPTLSSH DGKTTRWSES ITESSPNLEN
     PVHKQPKPVP LFPEESSGEG AIEQASQETI LSRATEVALG KETDQSPTLS TSSILSSSVS
     VNVLEEEPLT LTGISQTDES MSTIESWVEI TPSQTVKFSE SSSAPIIEGS GEVEENKNKI
     FNMVTDLPQR DPTDTLSPLD MSKIMITNHH IYIPATIAPL DSKLPSPDAR PTTVWNSNST
     SEWVSDKSFE GRKKKENEDE EGAVNAAHQG EVRAATERSD HLLLTPELES SNVDASSDLA
     TWEGFILETT PTESEKEMAN STPVFRETIG VANVEAQPFE HSSSSHPRVQ EELTTLSGNP
     PSLFTDLGSG DASTGMELIT ASLFTLDLES ETKVKKELPS TPSPSVEISS SFEPTGLTPS
     TVLDIEIAGV MSQTSQKTLI SEISGKPTSQ SGVRDLYTGF PMGEDFSGDF SEYPTVSYPT
     MKEETVGMGG SDDERVRDTQ TSSSIPTTSD NIYPVPDSKG PDSTVASTTA FPWEEVMSSA
     EGSGEQLASV RSSVGPVLPL AVDIFSGTES PYFDEEFEEV AAVTEANERP TVLPTAASGN
     TVDLTENGYI EVNSTMSLDF PQTMEPSKLW SKPEVNLDKQ EIGRETVTKE KAQGQKTFES
     LHSSFAPEQT ILETQSLIET EFQTSDYSML TTLKTYITNK EVEEEGMSIA HMSTPGPGIK
     DLESYTTHPE APGKSHSFSA TALVTESGAA RSVLMDSSTQ EEESIKLFQK GVKLTNKESN
     ADLSFSGLGS GGALPPLPTT SVNLTDMKQI ISTLYAETSH MESLGTSILG DKMEDHERME
     DVSSNEVRML ISKIGSISQD STEALDTTLS HTGTEEPTTS TLPFVKLMDL ERSPKQDPSG
     GKRKPKTHRP QTMSGLISNE NSSASEAEEG ATSPTAFLPQ TYSVEMTKHF APSESQPSDL
     FNVNSGEGSG EVDTLDLVYT SGTTQASSQG DSMLASHGFL EKHPEVSKTE AGATDVSPTA
     SAMFLHHSEY KSSLYPTSTL PSTEPYKSPS EGIEDGLQDN IQFEGSTLKP SRRKTTESII
     IDLDKEDSKD LGLTITESAI VKSLPELTSD KNIIIDIDHT KPVYEYIPGI QTDLDPEIKL
     ESHGSSEESL QVQEKYEGAV TLSPTEESFE GSGDALLAGY TQAIYNESVT PNDGKQAEDI
     SFSFATGIPV SSTETELHTF FPTASTLHIP SKLTTASPEI DKPNIEAISL DDIFESSTLS
     DGQAIADQSE VISTLGHLEK TQEEYEEKKY GGPSFQPEFF SGVGEVLTDP PAYVSIGSTY
     LIAQTLTELP NVVRPSDSTH YTEATPEVSS LAELSPQIPS SPFPVYVDNG VSKFPEVPHT
     SAQPVSTVTS SQKSIESPFK EVHANIEETI KPLGGNVHRT EPPSMSRDPA LDVSEDESKH
     KLLEELETSP TKPETSQDFP NKAKDHIPGE TVGMLAGIRT TESEPVITAD DMELGGATQQ
     PHSASAAFRV ETGMVPQPIQ QEPERPTFPS LEINHETHTS LFGESILATS EKQVSQKILD
     NSNQATVSST LDLHTAHALS PFSILDNSNE TAFLIGISEE SVEGTAVYLP GPDLCKTNPC
     LNGGTCYPTE TSYVCTCAPG YSGDQCELDF DECHSNPCRN GATCVDGFNT FRCLCLPSYV
     GALCEQDTET CDYGWHKFQG QCYKYFAHRR TWDAAERECR LQGAHLTSIL SHEEQMFVNR
     VGHDYQWIGL NDKMFEHDFR WTDGSALQYE NWRPNQPDSF FSAGEDCVVI IWHENGQWND
     VPCNYHLTYT CKKGTVACGQ PPVVENAKTF GKMKPRYEIN SLIRYHCKDG FIQRHLPTIR
     CLGNGRWAMP KITCMNPSAY QRTYSKKYLK NSSSAKDNSI NTSKHEHRWS RRQETRR
//
ID   KPCI_MOUSE              Reviewed;         595 AA.
AC   Q62074;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 3.
DT   08-MAR-2011, entry version 119.
DE   RecName: Full=Protein kinase C iota type;
DE            EC=2.7.11.13;
DE   AltName: Full=Atypical protein kinase C-lambda/iota;
DE            Short=aPKC-lambda/iota;
DE   AltName: Full=nPKC-iota;
GN   Name=Prkci; Synonyms=Pkcl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=94230340; PubMed=7513693;
RA   Akimoto K., Mizuno K., Osada S., Hirai S., Tanuma S., Suzuki K.,
RA   Ohno S.;
RT   "A new member of the third class in the protein kinase C family, PKC
RT   lambda, expressed dominantly in an undifferentiated mouse embryonal
RT   carcinoma cell line and also in many tissues and cells.";
RL   J. Biol. Chem. 269:12677-12683(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   SUBUNIT OF A COMPLEX CONTAINING PARD6B; PARD3 AND CDC42.
RX   MEDLINE=20394296; PubMed=10934474; DOI=10.1038/35019573;
RA   Joberty G., Petersen C., Gao L., Macara I.G.;
RT   "The cell-polarity protein Par6 links Par3 and atypical protein kinase
RT   C to Cdc42.";
RL   Nat. Cell Biol. 2:531-539(2000).
RN   [4]
RP   INTERACTION WITH SQSTM1 AND MAP2K5, AND MUTAGENESIS OF ARG-27; VAL-28;
RP   LYS-29; TRP-70; ASP-72; GLU-74; ASP-76; GLN-83 AND GLU-85.
RX   PubMed=12813044; DOI=10.1074/jbc.M303221200;
RA   Lamark T., Perander M., Outzen H., Kristiansen K., Oevervatn A.,
RA   Michaelsen E., Bjoerkoey G., Johansen T.;
RT   "Interaction codes within the family of mammalian Phox and Bem1p
RT   domain-containing proteins.";
RL   J. Biol. Chem. 278:34568-34581(2003).
CC   -!- FUNCTION: Calcium-independent, phospholipid-dependent, serine- and
CC       threonine-specific kinase. May play a role in the secretory
CC       response to nutrients. Involved in cell polarization processes and
CC       the formation of epithelial tight junctions. Implicated in the
CC       activation of several signaling pathways including Ras, c-Src and
CC       NF-kappa-B pathways. Functions in both pro- and anti-apoptotic
CC       pathways. Functions in the RAC1/ERK signaling required for
CC       transformed growth. Plays a role in microtubule dynamics through
CC       interaction with RAB2A and GAPDH and recruitment to vesicular
CC       tubular clusters (VTCs) (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Might be a target for novel lipid activators
CC       that are elevated during nutrient-stimulated insulin secretion.
CC       Two specific sites, Thr-411 (activation loop of the kinase domain)
CC       and Thr-563 (turn motif), need to be phosphorylated for its full
CC       activation (By similarity). Atypical PCKs are not regulated by
CC       diacylglycerol, phorbol esters nor calcium ions.
CC   -!- SUBUNIT: Forms a complex with SQSTM1 and MP2K5 (By similarity).
CC       Interacts directly with SQSTM1 (Probable). Interacts with IKBKB.
CC       Interacts with PARD6A, PARD6B and PARD6G. Part of a quaternary
CC       complex containing aPKC, PARD3, a PARD6 protein (PARD6A, PARD6B or
CC       PARD6G) and a GTPase protein (CDC42 or RAC1). Part of a complex
CC       with LLGL1 and PARD6B. Interacts with ADAP1/CENTA1. Interaction
CC       with SMG1, through the ZN-finger domain, activates the kinase
CC       activity. Interacts with CDK7. Forms a complex with RAB2A and
CC       GAPDH involved in recruitment onto the membrane of vesicular
CC       tubular clusters (VTCs) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane (By
CC       similarity). Endosome (By similarity). Nucleus (By similarity).
CC       Note=Transported into the endosome through interaction with
CC       SQSTM1/p62. After phosphorylation by cSrc, transported into the
CC       nucleus through interaction with KPNB1. Colocalizes with CDK7 in
CC       the cytoplasm and nucleus. Vesicular tubular clusters. Transported
CC       to VTCs through interaction with RAB2A (By similarity).
CC   -!- DOMAIN: The OPR domain mediates interaction with SQSTM1.
CC   -!- DOMAIN: The C1 domain does not bind diacylglycerol (DAG) (By
CC       similarity).
CC   -!- PTM: On neuronal growth factor (NGF) stimulation, phosphorylated
CC       on tyrosine residues by Src. Phosphorylation on Tyr-264
CC       facilitates binding to KPNB1/importin-beta regulating entry of
CC       PRKCI into the nucleus. Phosphorylation on Tyr-333 is important
CC       for NF-kappa-B stimulation (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. PKC subfamily.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 OPR domain.
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH21630.1; Type=Erroneous initiation;
CC       Sequence=BAA32499.1; Type=Erroneous initiation;
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DR   EMBL; D28577; BAA32499.1; ALT_INIT; mRNA.
DR   EMBL; BC021630; AAH21630.1; ALT_INIT; mRNA.
DR   IPI; IPI00121084; -.
DR   PIR; A53758; A53758.
DR   RefSeq; NP_032883.2; NM_008857.3.
DR   UniGene; Mm.291554; -.
DR   ProteinModelPortal; Q62074; -.
DR   SMR; Q62074; 25-107, 136-196, 248-587.
DR   STRING; Q62074; -.
DR   PhosphoSite; Q62074; -.
DR   PRIDE; Q62074; -.
DR   Ensembl; ENSMUST00000046401; ENSMUSP00000041030; ENSMUSG00000037643.
DR   Ensembl; ENSMUST00000108249; ENSMUSP00000103884; ENSMUSG00000037643.
DR   GeneID; 18759; -.
DR   KEGG; mmu:18759; -.
DR   CTD; 18759; -.
DR   MGI; MGI:99260; Prkci.
DR   GeneTree; ENSGT00590000082854; -.
DR   HOVERGEN; HBG108317; -.
DR   InParanoid; Q62074; -.
DR   OMA; KGDIMIT; -.
DR   OrthoDB; EOG4T782V; -.
DR   BRENDA; 2.7.11.13; 244.
DR   ArrayExpress; Q62074; -.
DR   Bgee; Q62074; -.
DR   CleanEx; MM_PRKCI; -.
DR   Genevestigator; Q62074; -.
DR   GermOnline; ENSMUSG00000037643; Mus musculus.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005543; F:phospholipid binding; ISS:UniProtKB.
DR   GO; GO:0004697; F:protein kinase C activity; IDA:BHF-UCL.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007015; P:actin filament organization; IMP:MGI.
DR   GO; GO:0045216; P:cell-cell junction organization; ISS:UniProtKB.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IMP:BHF-UCL.
DR   GO; GO:0035089; P:establishment of apical/basal cell polarity; IMP:MGI.
DR   GO; GO:0042462; P:eye photoreceptor cell development; IMP:MGI.
DR   GO; GO:0090004; P:positive regulation of establishment of protein localization in plasma membrane; IMP:BHF-UCL.
DR   GO; GO:0046326; P:positive regulation of glucose import; IMP:BHF-UCL.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:BHF-UCL.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000270; OPR_PB1.
DR   InterPro; IPR012233; PKC_zeta.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00564; PB1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   PIRSF; PIRSF000554; PKC_zeta; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00666; PB1; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Endosome; Kinase; Membrane; Metal-binding;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Proto-oncogene;
KW   Serine/threonine-protein kinase; Transferase; Tumor suppressor; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    595       Protein kinase C iota type.
FT                                /FTId=PRO_0000055711.
FT   DOMAIN       25    108       OPR.
FT   DOMAIN      253    521       Protein kinase.
FT   DOMAIN      522    595       AGC-kinase C-terminal.
FT   ZN_FING     140    190       Phorbol-ester/DAG-type.
FT   NP_BIND     259    267       ATP (By similarity).
FT   REGION        1    252       Regulatory domain (By similarity).
FT   REGION        1     28       Required for interaction with RAB2 (By
FT                                similarity).
FT   REGION       72     91       Interaction with PARD6A (By similarity).
FT   ACT_SITE    377    377       Proton acceptor (By similarity).
FT   BINDING     282    282       ATP (By similarity).
FT   MOD_RES     264    264       Phosphotyrosine; by Src (By similarity).
FT   MOD_RES     279    279       Phosphotyrosine; by Src (By similarity).
FT   MOD_RES     333    333       Phosphotyrosine; by Src (By similarity).
FT   MOD_RES     411    411       Phosphothreonine (Probable).
FT   MOD_RES     563    563       Phosphothreonine (Probable).
FT   MUTAGEN      27     27       R->A: No effect on interaction with
FT                                SQSTM1.
FT   MUTAGEN      28     28       V->A: No effect on interaction with
FT                                SQSTM1; when associated with A-29.
FT   MUTAGEN      29     29       K->A: No effect on interaction with
FT                                SQSTM1; when associated with A-118.
FT   MUTAGEN      70     70       W->A: Loss of interaction with SQSTM1.
FT   MUTAGEN      72     72       D->A: Loss of interaction with SQSTM1.
FT   MUTAGEN      74     74       E->A: Loss of interaction with SQSTM1.
FT   MUTAGEN      76     76       D->A: Loss of interaction with SQSTM1.
FT   MUTAGEN      83     83       Q->A: No effect on interaction with
FT                                SQSTM1.
FT   MUTAGEN      85     85       E->A: Loss of interaction with SQSTM1.
SQ   SEQUENCE   595 AA;  68203 MW;  6AC612D1E9264825 CRC64;
     MPTQRDSSTM SHTVACGGGG DHSHQVRVKA YYRGDIMITH FEPSISFEGL CSEVRDMCSF
     DNEQPFTMKW IDEEGDPCTV SSQLELEEAF RLYELNKDSE LLIHVFPCVP ERPGMPCPGE
     DKSIYRRGAR RWRKLYCANG HTFQAKRFNR RAHCAICTDR IWGLGRQGYK CINCKLLVHK
     KCHKLVTIEC GRHSLPPEPM MPMDQTMHPD HTQTVIPYNP SSHESLDQVG EEKEAMNTRE
     SGKASSSLGL QDFDLLRVIG RGSYAKVLLV RLKKTDRIYA MKVVKKELVN DDEDIDWVQT
     EKHVFEQASN HPFLVGLHSC FQTESRLFFV IEYVNGGDLM FHMQRQRKLP EEHARFYSAE
     ISLALNYLHE RGIIYRDLKL DNVLLDSEGH IKLTDYGMCK EGLRPGDTTS TFCGTPNYIA
     PEILRGEDYG FSVDWWALGV LMFEMMAGRS PFDIVGSSDN PDQNTEDYLF QVILEKQIRI
     PRSLSVKAAS VLKSFLNKDP KERLGCHPQT GFADIQGHPF FRNVDWDMME QKQVVPPFKP
     NISGEFGLDN FDSQFTNEPV QLTPDDDDIV RKIDQSEFEG FEYINPLLMS AEECV
//
ID   PLCG1_MOUSE             Reviewed;        1302 AA.
AC   Q62077; Q6P1G1;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 2.
DT   08-MAR-2011, entry version 109.
DE   RecName: Full=1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-1;
DE            EC=3.1.4.11;
DE   AltName: Full=Phosphoinositide phospholipase C-gamma-1;
DE   AltName: Full=Phospholipase C-gamma-1;
DE            Short=PLC-gamma-1;
GN   Name=Plcg1; Synonyms=Plcg-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 846-1052.
RC   TISSUE=Oocyte;
RX   MEDLINE=96257754; PubMed=8687404;
RA   Dupont G., McGuinness O.M., Johnson M.H., Berridge M.J., Borgese F.;
RT   "Phospholipase C in mouse oocytes: characterization of beta and gamma
RT   isoforms and their possible involvement in sperm-induced Ca2+
RT   spiking.";
RL   Biochem. J. 316:583-591(1996).
RN   [3]
RP   INTERACTION WITH KHDRBS1.
RX   PubMed=10748127; DOI=10.1074/jbc.M909368199;
RA   Bedford M.T., Frankel A., Yaffe M.B., Clarke S., Leder P., Richard S.;
RT   "Arginine methylation inhibits the binding of proline-rich ligands to
RT   Src homology 3, but not WW, domains.";
RL   J. Biol. Chem. 275:16030-16036(2000).
RN   [4]
RP   INTERACTION WITH CBLB.
RX   PubMed=10646608; DOI=10.1038/35003228;
RA   Bachmaier K., Krawczyk C., Kozieradzki I., Kong Y.-Y., Sasaki T.,
RA   Oliveira-dos-Santos A., Mariathasan S., Bouchard D., Wakeham A.,
RA   Itie A., Le J., Ohashi P.S., Sarosi I., Nishina H., Lipkowitz S.,
RA   Penninger J.M.;
RT   "Negative regulation of lymphocyte activation and autoimmunity by the
RT   molecular adaptor Cbl-b.";
RL   Nature 403:211-216(2000).
RN   [5]
RP   INTERACTION WITH CLNK, AND DOMAIN.
RX   PubMed=11463797; DOI=10.1074/jbc.M106390200;
RA   Goitsuka R., Tatsuno A., Ishiai M., Kurosaki T., Kitamura D.;
RT   "MIST functions through distinct domains in immunoreceptor signaling
RT   in the presence and absence of LAT.";
RL   J. Biol. Chem. 276:36043-36050(2001).
RN   [6]
RP   PHOSPHORYLATION, UBIQUITINATION, AND FUNCTION.
RX   PubMed=15308098; DOI=10.1016/j.immuni.2004.07.013;
RA   Jeon M.-S., Atfield A., Venuprasad K., Krawczyk C., Sarao R., Elly C.,
RA   Yang C., Arya S., Bachmaier K., Su L., Bouchard D., Jones R.,
RA   Gronski M., Ohashi P., Wada T., Bloom D., Fathman C.G., Liu Y.-C.,
RA   Penninger J.M.;
RT   "Essential role of the E3 ubiquitin ligase Cbl-b in T cell anergy
RT   induction.";
RL   Immunity 21:167-177(2004).
RN   [7]
RP   INTERACTION WITH INPP5D.
RX   PubMed=16000869;
RA   Song M., Kim M.J., Ha S., Park J.B., Ryu S.H., Suh P.-G.;
RT   "Inositol 5'-phosphatase, SHIP1 interacts with phospholipase C-gamma1
RT   and modulates EGF-induced PLC activity.";
RL   Exp. Mol. Med. 37:161-168(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-771 AND TYR-775, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-379; TYR-481; TYR-506
RP   AND TYR-977, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1248 AND SER-1263, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [11]
RP   INTERACTION WITH THEMIS.
RX   PubMed=19597499; DOI=10.1038/ni.1766;
RA   Fu G., Vallee S., Rybakin V., McGuire M.V., Ampudia J., Brockmeyer C.,
RA   Salek M., Fallen P.R., Hoerter J.A.H., Munshi A., Huang Y.H., Hu J.,
RA   Fox H.S., Sauer K., Acuto O., Gascoigne N.R.J.;
RT   "Themis controls thymocyte selection through regulation of T cell
RT   antigen receptor-mediated signaling.";
RL   Nat. Immunol. 10:848-856(2009).
CC   -!- FUNCTION: The production of the second messenger molecules
CC       diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is
CC       mediated by activated phosphatidylinositol-specific phospholipase
CC       C enzymes.
CC   -!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-
CC       bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate +
CC       diacylglycerol.
CC   -!- COFACTOR: Calcium.
CC   -!- SUBUNIT: Interacts with RALGPS1 (By similarity). Interacts with
CC       AGAP2 via its SH3 domain. Interacts with phosphorylated LAT upon
CC       TCR activation. Interacts with the Pro-rich domain of TNK1 via its
CC       SH3 domain. Associates with BLNK, VAV1, GRB2 and NCK1 in a B-cell
CC       antigen receptor-dependent fashion. Interacts with CBLB in
CC       activated T-cells; which inhibits phosphorylation. Interacts with
CC       SHB. Interacts via its SH3 domain with the Arg/Gly-rich-flanked
CC       Pro-rich domains of KHDRBS1/SAM68. This interaction is selectively
CC       regulated by arginine methylation of KHDRBS1/SAM68. Interacts with
CC       INPP5D/SHIP1, THEMIS and CLNK.
CC   -!- INTERACTION:
CC       P35329:Cd22; NbExp=1; IntAct=EBI-300133, EBI-300059;
CC       P14753:Epor; NbExp=4; IntAct=EBI-300133, EBI-617901;
CC       Q60631:Grb2; NbExp=1; IntAct=EBI-300133, EBI-1688;
CC       Q9ES52:Inpp5d; NbExp=1; IntAct=EBI-300133, EBI-300210;
CC       Q62245:Sos1; NbExp=1; IntAct=EBI-300133, EBI-1693;
CC   -!- DOMAIN: The SH3 domain mediates interaction with RALGPS1 (By
CC       similarity). The SH3 domain also mediates interaction with CLNK.
CC   -!- PTM: May be dephosphorylated by PTPRJ (By similarity). The
CC       receptor-mediated activation of PLC-gamma-1 and PLC-gamma-2
CC       involves their phosphorylation by tyrosine kinases in response to
CC       ligation of a variety of growth factor receptors and immune system
CC       receptors.
CC   -!- PTM: Ubiquitinated by CBLB in activated T-cells.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 EF-hand domain.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -!- SIMILARITY: Contains 1 PI-PLC X-box domain.
CC   -!- SIMILARITY: Contains 1 PI-PLC Y-box domain.
CC   -!- SIMILARITY: Contains 2 SH2 domains.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; BC065091; AAH65091.1; -; mRNA.
DR   EMBL; X95346; CAA64639.1; -; mRNA.
DR   IPI; IPI00121089; -.
DR   RefSeq; NP_067255.2; NM_021280.3.
DR   UniGene; Mm.44463; -.
DR   ProteinModelPortal; Q62077; -.
DR   SMR; Q62077; 157-220, 489-933, 1088-1195.
DR   IntAct; Q62077; 14.
DR   MINT; MINT-124146; -.
DR   STRING; Q62077; -.
DR   PhosphoSite; Q62077; -.
DR   PRIDE; Q62077; -.
DR   Ensembl; ENSMUST00000103115; ENSMUSP00000099404; ENSMUSG00000016933.
DR   GeneID; 18803; -.
DR   KEGG; mmu:18803; -.
DR   NMPDR; fig|10090.3.peg.7332; -.
DR   UCSC; uc008nra.1; mouse.
DR   CTD; 18803; -.
DR   MGI; MGI:97615; Plcg1.
DR   HOGENOM; HBG402919; -.
DR   HOVERGEN; HBG053611; -.
DR   InParanoid; Q62077; -.
DR   OMA; YRSLMYS; -.
DR   OrthoDB; EOG4320X7; -.
DR   PhylomeDB; Q62077; -.
DR   BRENDA; 3.1.4.11; 244.
DR   NextBio; 295106; -.
DR   ArrayExpress; Q62077; -.
DR   Bgee; Q62077; -.
DR   CleanEx; MM_PLCG1; -.
DR   Genevestigator; Q62077; -.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0035254; F:glutamate receptor binding; IPI:MGI.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:EC.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0009395; P:phospholipid catabolic process; IEA:InterPro.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IDA:MGI.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR015359; Phospholipase_C_EF-hand-like.
DR   InterPro; IPR001711; Phospholipase_C_Pinositol-sp_Y.
DR   InterPro; IPR001192; Pinositol_Phospholipase-C.
DR   InterPro; IPR016279; PLC-gamma.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 3.
DR   Gene3D; G3DSA:3.20.20.190; PLC-like_Pdiesterase_TIM-brl; 2.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 2.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF09279; efhand_like; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00388; PI-PLC-X; 1.
DR   Pfam; PF00387; PI-PLC-Y; 1.
DR   Pfam; PF00017; SH2; 2.
DR   Pfam; PF00018; SH3_1; 1.
DR   PIRSF; PIRSF000952; PLC-gamma; 1.
DR   PRINTS; PR00390; PHPHLIPASEC.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00233; PH; 3.
DR   SMART; SM00148; PLCXc; 1.
DR   SMART; SM00149; PLCYc; 1.
DR   SMART; SM00252; SH2; 2.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF51695; PLC-like_Pdiesterase_TIM-brl; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
DR   PROSITE; PS50001; SH2; 2.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Calcium; Hydrolase; Lipid degradation; Phosphoprotein;
KW   Repeat; SH2 domain; SH3 domain; Transducer; Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1302       1-phosphatidylinositol-4,5-bisphosphate
FT                                phosphodiesterase gamma-1.
FT                                /FTId=PRO_0000088499.
FT   DOMAIN       27    142       PH 1.
FT   DOMAIN      152    187       EF-hand.
FT   DOMAIN      320    464       PI-PLC X-box.
FT   DOMAIN      489    523       PH 2; first part.
FT   DOMAIN      550    657       SH2 1.
FT   DOMAIN      668    756       SH2 2.
FT   DOMAIN      791    851       SH3.
FT   DOMAIN      895    931       PH 2; second part.
FT   DOMAIN      953   1070       PI-PLC Y-box.
FT   DOMAIN     1075   1177       C2.
FT   CA_BIND     165    176       Potential.
FT   ACT_SITE    335    335       By similarity.
FT   ACT_SITE    380    380       By similarity.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     379    379       Phosphotyrosine.
FT   MOD_RES     481    481       Phosphotyrosine.
FT   MOD_RES     506    506       Phosphotyrosine.
FT   MOD_RES     525    525       Phosphoserine (By similarity).
FT   MOD_RES     771    771       Phosphotyrosine.
FT   MOD_RES     775    775       Phosphotyrosine.
FT   MOD_RES     783    783       Phosphotyrosine (By similarity).
FT   MOD_RES     977    977       Phosphotyrosine.
FT   MOD_RES    1221   1221       Phosphoserine (By similarity).
FT   MOD_RES    1248   1248       Phosphoserine.
FT   MOD_RES    1253   1253       Phosphotyrosine (By similarity).
FT   MOD_RES    1263   1263       Phosphoserine.
FT   CONFLICT    966    966       D -> A (in Ref. 2; CAA64639).
FT   CONFLICT    984    984       P -> R (in Ref. 2; CAA64639).
SQ   SEQUENCE   1302 AA;  149668 MW;  5D123C508D425EB2 CRC64;
     MAGVATPCAN GCGPGAPSEA EVLHLCRSLE VGTVMTLFYS KKSQRPERKT FQVKLETRQI
     TWSRGADKIE GSIDIREIKE IRPGKTSRDF DRYQEDPAFR PDQSHCFVIL YGMEFRLKTL
     SLQATSEDEV NMWIKGLTWL MEDTLQAATP LQIERWLRKQ FYSVDRNRED RISAKDLKNM
     LSQVNYRVPN MRFLRERLTD LEQRSGDITY GQFAQLYRSL MYSAQKTMDL PFLETNALRT
     GERPEHCQVS LSEFQQFLLE YQGELWAVDR LQVQEFMLSF LRDPLREIEE PYFFLDELVT
     FLFSKENSVW NSQLDAVCPD TMNNPLSHYW ISSSHNTYLT GDQFSSESSL EAYARCLRMG
     CRCIELDCWD GPDGMPVIYH GHTLTTKIKF SDVLHTIKEH AFVASEYPVI LSIEDHCSIA
     QQRNMAQHFR KVLGDTLLTK PVDIAADGLP SPNQLRRKIL IKHKKLAEGS AYEEVPTSVM
     YSENDISNSI KNGILYLEDP VNHEWYPHYF VLTSSKIYYS EETSSDQGNE DEEEPKEASS
     STELHSSEKW FHGKLGAGRD GRHIAERLLT EYCIETGAPD GSFLVRESET FVGDYTLSFW
     RNGKVQHCRI HSRQDAGTPK FFLTDNLVFD SLYDLITHYQ QVPLRCNEFE MRLSEPVPQT
     NAHESKEWYH ASLTRAQAEH MLMRVPRDGA FLVRKRNEPN SYAISFRAEG KIKHCRVQQE
     GQTVMLGNSE FDSLVDLISY YEKHPLYRKM KLRYPINEEA LEKIGTAEPD YGALYEGRNP
     GFYVEANPMP TFKCAVKALF DYKAQREDEL TFTKSAIIQN VEKQDGGWWR GDYGGKKQLW
     FPSNYVEEMI NPAVLEPERE HLDENSPLGD LLRGVLDVPA CQIAIRPEGK NNRLFVFSIS
     MPSVAQWSLD VAADSQEELQ DWVKKIREVA QTADARLTEG KMMERRKKIA LELSELVVYC
     RPVPFDEEKI GTERACYRDM SSFPETKAEK YVNKAKGKKF LQYNRLQLSR IYPKGQRLDS
     SNYDPLPMWI CGSQLVALNF QTPDKPMQMN QALFMAGGHC GYVLQPSTMR DEAFDPFDKS
     SLRGLEPCVI CIEVLGARHL PKNGRGIVCP FVEIEVAGAE YDSTKQKTEF VVDNGLNPVW
     PAKPFHFQIS NPEFAFLRFV VYEEDMFSDQ NFLAQATFPV KGLKTGYRAV PLKNNYSEDL
     ELASLLIKID IFPAKENGDL SPFSGISLRE RASDASSQLF HVRAREGSFE ARYQQPFEDF
     RISQEHLADH FDSRERSTSD GPSSATNLIE DPLHDKLWKC SL
//
ID   NSG1_MOUSE              Reviewed;         185 AA.
AC   Q62092; O54717; Q3UF63; Q922E5;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 3.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Neuron-specific protein family member 1;
DE   AltName: Full=Brain neuron cytoplasmic protein 1;
DE   AltName: Full=M234;
DE   AltName: Full=p21;
GN   Name=Nsg1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=97165882; PubMed=9013775; DOI=10.1016/S0169-328X(96)00115-5;
RA   Carlock L., Vo T., Lorincz M., Walker P.D., Bessert D., Wisniewski D.,
RA   Dunbar J.C.;
RT   "Variable subcellular localization of a neuron-specific protein during
RT   NTera 2 differentiation into post-mitotic human neurons.";
RL   Brain Res. Mol. Brain Res. 42:202-212(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=98129794; PubMed=9461575; DOI=10.1074/jbc.273.7.3909;
RA   Saberan-Djoneidi D., Picart R., Escalier D., Gelman M., Barret A.,
RA   Tougard C., Glowinski J., Levi-Strauss M.;
RT   "A 21-kDa polypeptide belonging to a new family of proteins is
RT   expressed in the Golgi apparatus of neural and germ cells.";
RL   J. Biol. Chem. 273:3909-3914(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex, Head, and Sympathetic ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type
CC       II membrane protein (Probable).
CC   -!- TISSUE SPECIFICITY: Pituitary and less in adrenal gland and
CC       testis.
CC   -!- SIMILARITY: Belongs to the NSG family.
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DR   EMBL; M98530; AAA39966.1; -; Genomic_DNA.
DR   EMBL; AF035683; AAB88210.1; -; mRNA.
DR   EMBL; AK076451; BAC36347.1; -; mRNA.
DR   EMBL; AK144503; BAE25919.1; -; mRNA.
DR   EMBL; AK148941; BAE28698.1; -; mRNA.
DR   EMBL; BC008272; AAH08272.1; -; mRNA.
DR   IPI; IPI00121131; -.
DR   RefSeq; NP_035072.2; NM_010942.3.
DR   UniGene; Mm.7414; -.
DR   STRING; Q62092; -.
DR   PRIDE; Q62092; -.
DR   Ensembl; ENSMUST00000031009; ENSMUSP00000031009; ENSMUSG00000029126.
DR   GeneID; 18196; -.
DR   KEGG; mmu:18196; -.
DR   UCSC; uc008xga.1; mouse.
DR   CTD; 18196; -.
DR   MGI; MGI:109149; Nsg1.
DR   eggNOG; roNOG17631; -.
DR   HOGENOM; HBG713191; -.
DR   HOVERGEN; HBG012403; -.
DR   InParanoid; Q62092; -.
DR   OMA; TIMSEEK; -.
DR   OrthoDB; EOG415GFN; -.
DR   PhylomeDB; Q62092; -.
DR   NextBio; 293552; -.
DR   ArrayExpress; Q62092; -.
DR   Bgee; Q62092; -.
DR   CleanEx; MM_NSG1; -.
DR   Genevestigator; Q62092; -.
DR   GermOnline; ENSMUSG00000029126; Mus musculus.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050780; F:dopamine receptor binding; IEA:InterPro.
DR   GO; GO:0007212; P:dopamine receptor signaling pathway; IEA:InterPro.
DR   InterPro; IPR009431; D1-dopamine_rcpt_interact.
DR   Pfam; PF06387; Calcyon; 1.
DR   PIRSF; PIRSF002383; Calcyon; 1.
PE   2: Evidence at transcript level;
KW   Golgi apparatus; Membrane; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    185       Neuron-specific protein family member 1.
FT                                /FTId=PRO_0000164364.
FT   TOPO_DOM      1     82       Cytoplasmic (Potential).
FT   TRANSMEM     83    103       Helical; Signal-anchor for type II
FT                                membrane protein; (Potential).
FT   TOPO_DOM    104    185       Lumenal (Potential).
FT   CONFLICT    112    112       C -> Y (in Ref. 1; AAA39966).
FT   CONFLICT    139    139       A -> D (in Ref. 1; AAA39966).
FT   CONFLICT    151    152       NV -> KL (in Ref. 1; AAA39966).
SQ   SEQUENCE   185 AA;  20929 MW;  B184238A71710C1F CRC64;
     MVKLGNNFAE KGTKQPLLED GFDTIPLMTP LDVNQLQFPP PDKVVVKTKT EYEPDRKKGK
     ARPPKIAEFT VSITEGVTER FKVSVLVLFA LAFLTCVVFL VVYKVYKYDR ACPDGFVLKN
     TQCIPEGLES YYTEQDSSAR EKFYTVINHY NVAKQSITRS VSPWMSVLSE EKLSEQETEA
     AEKSA
//
ID   SRSF2_MOUSE             Reviewed;         221 AA.
AC   Q62093; Q542L3; Q60701;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   08-MAR-2011, entry version 109.
DE   RecName: Full=Serine/arginine-rich splicing factor 2;
DE   AltName: Full=Protein PR264;
DE   AltName: Full=Putative myelin regulatory factor 1;
DE            Short=MRF-1;
DE   AltName: Full=Splicing component, 35 kDa;
DE   AltName: Full=Splicing factor SC35;
DE            Short=SC-35;
DE   AltName: Full=Splicing factor, arginine/serine-rich 2;
GN   Name=Srsf2; Synonyms=Pr264, Sfrs10, Sfrs2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN MBP REGULATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=95074156; PubMed=7527040;
RA   Haque N.S., Buchberg A.M., Khalili K.;
RT   "Isolation and characterization of MRF-1, a brain-derived DNA-binding
RT   protein with a capacity to regulate expression of myelin basic protein
RT   gene.";
RL   J. Biol. Chem. 269:31149-31156(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98447613; PubMed=9774382; DOI=10.1074/jbc.273.43.27761;
RA   Yang L., Embree L.J., Tsai S., Hickstein D.D.;
RT   "Oncoprotein TLS interacts with serine-arginine proteins involved in
RT   RNA splicing.";
RL   J. Biol. Chem. 273:27761-27764(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Bone marrow, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-121.
RC   STRAIN=129/Sv; TISSUE=Liver;
RA   Gaillard C., Perbal B.;
RL   Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-208 AND
RP   SER-212, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; SER-189; SER-191;
RP   SER-206 AND SER-208, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Necessary for the splicing of pre-mRNA. It is required
CC       for formation of the earliest ATP-dependent splicing complex and
CC       interacts with spliceosomal components bound to both the 5'- and
CC       3'-splice sites during spliceosome assembly. It also is required
CC       for ATP-dependent interactions of both U1 and U2 snRNPs with pre-
CC       mRNA (By similarity). Can bind to the myelin basic protein (MBP)
CC       gene MB3 regulatory region and increase transcription of the mbp
CC       promoter in cells derived from the CNS.
CC   -!- SUBUNIT: Interacts with CCNL1 and CCNL2. Interacts with SCAF11.
CC       Interacts with ZRSR2/U2AF1-RS2 (By similarity). In vitro, self-
CC       associates and binds SRSF1/SFRS1 (ASF/SF2), SNRNP70 and U2AF1 but
CC       not U2AF2. Binds SREK1/SFRS12.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed in all the tissues examined; liver,
CC       kidney, spleen, heart, lung and brain.
CC   -!- PTM: Extensively phosphorylated on serine residues in the RS
CC       domain (By similarity).
CC   -!- SIMILARITY: Belongs to the splicing factor SR family.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA64595.1; Type=Frameshift; Positions=56, 125, 141;
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DR   EMBL; U14648; AAA64595.1; ALT_FRAME; mRNA.
DR   EMBL; AF077858; AAC71000.1; -; mRNA.
DR   EMBL; AK086103; BAC39610.1; -; mRNA.
DR   EMBL; AK088042; BAC40111.1; -; mRNA.
DR   EMBL; AK165670; BAE38330.1; -; mRNA.
DR   EMBL; BC005493; AAH05493.1; -; mRNA.
DR   EMBL; X98511; CAA67134.1; -; Genomic_DNA.
DR   IPI; IPI00121135; -.
DR   PIR; A55335; A55335.
DR   RefSeq; NP_035488.1; NM_011358.2.
DR   UniGene; Mm.21841; -.
DR   UniGene; Mm.348004; -.
DR   ProteinModelPortal; Q62093; -.
DR   SMR; Q62093; 2-94.
DR   DIP; DIP-44831N; -.
DR   STRING; Q62093; -.
DR   PhosphoSite; Q62093; -.
DR   PRIDE; Q62093; -.
DR   Ensembl; ENSMUST00000092404; ENSMUSP00000090059; ENSMUSG00000034120.
DR   GeneID; 20382; -.
DR   KEGG; mmu:20382; -.
DR   UCSC; uc007mmn.1; mouse.
DR   CTD; 20382; -.
DR   MGI; MGI:98284; Srsf2.
DR   HOVERGEN; HBG107480; -.
DR   OrthoDB; EOG4D26RH; -.
DR   PhylomeDB; Q62093; -.
DR   NextBio; 298298; -.
DR   ArrayExpress; Q62093; -.
DR   Bgee; Q62093; -.
DR   CleanEx; MM_SFRS2; -.
DR   Genevestigator; Q62093; -.
DR   GermOnline; ENSMUSG00000034120; Mus musculus.
DR   GO; GO:0016607; C:nuclear speck; IDA:MGI.
DR   GO; GO:0005681; C:spliceosomal complex; IDA:MGI.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Acetylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   RNA-binding.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    221       Serine/arginine-rich splicing factor 2.
FT                                /FTId=PRO_0000081919.
FT   DOMAIN       14     92       RRM.
FT   COMPBIAS    111    116       Gly-rich (hinge region).
FT   COMPBIAS    117    221       Arg/Ser-rich (RS domain).
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES      23     23       Phosphotyrosine (By similarity).
FT   MOD_RES      26     26       Phosphoserine (By similarity).
FT   MOD_RES      36     36       N6-acetyllysine (By similarity).
FT   MOD_RES     187    187       Phosphoserine.
FT   MOD_RES     189    189       Phosphoserine.
FT   MOD_RES     191    191       Phosphoserine.
FT   MOD_RES     204    204       Phosphoserine (By similarity).
FT   MOD_RES     206    206       Phosphoserine.
FT   MOD_RES     208    208       Phosphoserine.
FT   MOD_RES     212    212       Phosphoserine.
FT   MOD_RES     220    220       Phosphoserine (By similarity).
FT   MOD_RES     221    221       Phosphoserine (By similarity).
FT   CONFLICT     66     67       RD -> PH (in Ref. 1; AAA64595).
FT   CONFLICT     89     89       M -> L (in Ref. 1; AAA64595).
FT   CONFLICT    120    120       Missing (in Ref. 1).
FT   CONFLICT    218    218       A -> E (in Ref. 1; AAA64595).
SQ   SEQUENCE   221 AA;  25476 MW;  68121AC4D35714FA CRC64;
     MSYGRPPPDV EGMTSLKVDN LTYRTSPDTL RRVFEKYGRV GDVYIPRDRY TKESRGFAFV
     RFHDKRDAED AMDAMDGAVL DGRELRVQMA RYGRPPDSHH SRRGPPPRRY GGGGYGRRSR
     SPRRRRRSRS RSRSRSRSRS RSRYSRSKSR SRTRSRSRST SKSRSARRSK SKSSSVSRSR
     SRSRSRSRSR SPPPVSKRES KSRSRSKSPP KSPEEEGAVS S
//
ID   DDX3Y_MOUSE             Reviewed;         658 AA.
AC   Q62095; Q9QWS9;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=ATP-dependent RNA helicase DDX3Y;
DE            EC=3.6.4.13;
DE   AltName: Full=D1Pas1-related sequence 1;
DE   AltName: Full=DEAD box protein 3, Y-chromosomal;
DE   AltName: Full=DEAD-box RNA helicase DEAD2;
DE            Short=mDEAD2;
GN   Name=Ddx3y; Synonyms=D1Pas1-rs1, Dead2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Testis;
RX   MEDLINE=98409500; PubMed=9736773; DOI=10.1093/hmg/7.11.1713;
RA   Mazeyrat S., Saut N., Sargent C.A., Grimmond S., Longepied G.,
RA   Ehrmann I.E., Ellis P.S., Greenfield A., Affara N.A., Mitchell M.J.;
RT   "The mouse Y chromosome interval necessary for spermatogonial
RT   proliferation is gene dense with syntenic homology to the human AZFa
RT   region.";
RL   Hum. Mol. Genet. 7:1713-1724(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 283-527, AND TISSUE SPECIFICITY.
RC   TISSUE=Erythroleukemia;
RX   MEDLINE=94192995; PubMed=8144024; DOI=10.1016/0378-1119(94)90541-X;
RA   Gee S.L., Conboy J.G.;
RT   "Mouse erythroid cells express multiple putative RNA helicase genes
RT   exhibiting high sequence conservation from yeast to mammals.";
RL   Gene 140:171-177(1994).
RN   [4]
RP   PROTEIN SEQUENCE OF 428-439.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [5]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15383328; DOI=10.1016/j.yexcr.2004.07.005;
RA   Sekiguchi T., Iida H., Fukumura J., Nishimoto T.;
RT   "Human DDX3Y, the Y-encoded isoform of RNA helicase DDX3, rescues a
RT   hamster temperature-sensitive ET24 mutant cell line with a DDX3X
RT   mutation.";
RL   Exp. Cell Res. 300:213-222(2004).
CC   -!- FUNCTION: Probable ATP-dependent RNA helicase. May play a role in
CC       spermatogenesis.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: May interact with TDRD3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between
CC       the nucleus and the cytoplasm in an XPO1-dependent manner.
CC   -!- TISSUE SPECIFICITY: Found in heart, brain, liver, skeletal muscle,
CC       kidney and testis. Low expression detected in lung. In testis,
CC       expressed in all types of spermatogenic cells including
CC       spermatogonia, spermatocytes, spermatids and somatic Sertoli cells
CC       within the seminiferous tubules. Also expressed in Leydig cells
CC       and other interstitial cells.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
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DR   EMBL; AJ007376; CAA07483.1; -; mRNA.
DR   EMBL; BC021453; AAH21453.1; -; mRNA.
DR   EMBL; L25337; AAA53631.1; -; mRNA.
DR   IPI; IPI00134371; -.
DR   RefSeq; NP_036138.1; NM_012008.2.
DR   UniGene; Mm.302938; -.
DR   ProteinModelPortal; Q62095; -.
DR   SMR; Q62095; 167-579.
DR   STRING; Q62095; -.
DR   PhosphoSite; Q62095; -.
DR   PRIDE; Q62095; -.
DR   Ensembl; ENSMUST00000091190; ENSMUSP00000088729; ENSMUSG00000069045.
DR   GeneID; 26900; -.
DR   KEGG; mmu:26900; -.
DR   UCSC; uc009uzm.1; mouse.
DR   CTD; 26900; -.
DR   MGI; MGI:1349406; Ddx3y.
DR   GeneTree; ENSGT00390000005849; -.
DR   HOGENOM; HBG737336; -.
DR   HOVERGEN; HBG015893; -.
DR   InParanoid; Q62095; -.
DR   OMA; MGNLGVA; -.
DR   OrthoDB; EOG47D9FV; -.
DR   PhylomeDB; Q62095; -.
DR   NextBio; 304749; -.
DR   ArrayExpress; Q62095; -.
DR   Bgee; Q62095; -.
DR   Genevestigator; Q62095; -.
DR   GermOnline; ENSMUSG00000069045; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Direct protein sequencing; Helicase;
KW   Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; RNA-binding.
FT   CHAIN         1    658       ATP-dependent RNA helicase DDX3Y.
FT                                /FTId=PRO_0000055012.
FT   DOMAIN      210    402       Helicase ATP-binding.
FT   DOMAIN      413    574       Helicase C-terminal.
FT   NP_BIND     199    206       ATP (By similarity).
FT   NP_BIND     223    230       ATP (By similarity).
FT   MOTIF       179    207       Q motif.
FT   MOTIF       346    349       DEAD box.
FT   MOD_RES      70     70       Phosphotyrosine (By similarity).
FT   MOD_RES     322    322       Phosphothreonine (By similarity).
FT   MOD_RES     592    592       Phosphoserine (By similarity).
FT   CONFLICT    527    527       R -> S (in Ref. 3; AAA53631).
SQ   SEQUENCE   658 AA;  73428 MW;  C64668326B2C3BB9 CRC64;
     MSQVAAESTA GLDQQFVGLD LKSSDNQNGG GNTESKGRYI PPHLRNRETS KGVCDKDSSG
     WSCSKDKDAY SSFGSRDSRG KPNYFSDRGS GSRGRFDDHG RNDYDGIGGR DRTGFGKFER
     SGHSRWSDRS DEDDWSKPLP PSERLEQELF SGGNTGINFE KYDDIPVEAT GNNCPPHIEN
     FSDIEMGEII MGNIELTRYT RPTPVQKHAI PIIKEKRDLM ACAQTGSGKT AAFLLPILSQ
     IYTDGPGEAL KAMKENGRYG RRKQYPISLV LAPTRELAVQ IYEEARKFSY RSRVRPCVVY
     GGADTVQQIR DLERGCHLLV ATPGRLVDMM ERGKIGLDFC KYLVLDEADR MLDMGFEPQI
     RRIVEQDTMP PKGVRHTMMF SATFPKEIQM LARDFLDEYI FLAVGRVGST SENITQKVVW
     VEELDKRSFL LDLLNATGKD SLTLVFVETK KGADSLENFL FQERYACTSI HGDRSQKDRE
     EALHQFRSGR KPILVATAVA ARGLDISNVK HVINFDLPSD IEEYVHRIGR TGRVGNLGLA
     TSFFNERNLN ITKDLLDLLV EAKQEVPSWL ESMAYEHHYK GSSRGRSKSR FSGGFGARDY
     RQSSGSANAG FNSNRANSSR SSGSSHNRGF GGGGYGGFYN NDGYGGNYNS QAVDWWGN
//
ID   KPCD1_MOUSE             Reviewed;         918 AA.
AC   Q62101;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 105.
DE   RecName: Full=Serine/threonine-protein kinase D1;
DE            EC=2.7.11.13;
DE   AltName: Full=Protein kinase C mu type;
DE   AltName: Full=Protein kinase D;
DE   AltName: Full=nPKC-D1;
DE   AltName: Full=nPKC-mu;
GN   Name=Prkd1; Synonyms=Pkcm, Pkd, Prkcm;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Lung;
RX   MEDLINE=94359973; PubMed=8078925; DOI=10.1073/pnas.91.18.8572;
RA   Valverde A.M., Sinnet-Smith J., Van Lint J., Rozengurt E.;
RT   "Molecular cloning and characterization of protein kinase D: a target
RT   for diacylglycerol and phorbol esters with a distinctive catalytic
RT   domain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:8572-8576(1994).
RN   [2]
RP   PHOSPHORYLATION AT SER-916.
RX   MEDLINE=99403106; PubMed=10473617; DOI=10.1074/jbc.274.37.26543;
RA   Matthews S.A., Rozengurt E., Cantrell D.;
RT   "Characterization of serine 916 as an in vivo autophosphorylation site
RT   for protein kinase D/protein kinase Cmu.";
RL   J. Biol. Chem. 274:26543-26549(1999).
RN   [3]
RP   PHOSPHORYLATION AT SER-744 AND SER-748.
RX   PubMed=11410586; DOI=10.1074/jbc.M101648200;
RA   Waldron R.T., Rey O., Iglesias T., Tugal T., Cantrell D.,
RA   Rozengurt E.;
RT   "Activation loop Ser744 and Ser748 in protein kinase D are
RT   transphosphorylated in vivo.";
RL   J. Biol. Chem. 276:32606-32615(2001).
RN   [4]
RP   FUNCTION, ENZYME REGULATION, MUTAGENESIS OF SER-744 AND SER-748, AND
RP   PHOSPHORYLATION AT SER-744 AND SER-748.
RX   PubMed=12407104; DOI=10.1074/jbc.M208075200;
RA   Waldron R.T., Rozengurt E.;
RT   "Protein kinase C phosphorylates protein kinase D activation loop
RT   Ser744 and Ser748 and releases autoinhibition by the pleckstrin
RT   homology domain.";
RL   J. Biol. Chem. 278:154-163(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND SER-253, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Converts transient diacylglycerol (DAG) signals into
CC       prolonged physiological effects, downstream of PKC. Involved in
CC       resistance to oxidative stress through activation of NF-kappa-B.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: Activated by DAG and phorbol esters. Phorbol-
CC       ester/DAG-type domain 1 binds DAG with high affinity and appears
CC       to play the dominant role in mediating translocation to the cell
CC       membrane and trans-Golgi network. Phorbol-ester/DAG-type domain 2
CC       binds phorbol ester with higher affinity. Autophosphorylation of
CC       Ser-748 and phosphorylation of Ser-744 by PKC relieves auto-
CC       inhibition by the PH domain. Phosphorylation on Tyr-469 by the
CC       Src/Abl pathway in response to oxidative stress, is also required
CC       for activation.
CC   -!- SUBUNIT: Interacts (via N-terminus) with ADAP1/CENTA1. Interacts
CC       with Src (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane (By
CC       similarity). Note=Translocation to the cell membrane is required
CC       for kinase activation (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. PKD subfamily.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 2 phorbol-ester/DAG-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; Z34524; CAA84283.1; -; mRNA.
DR   IPI; IPI00122084; -.
DR   PIR; I48719; I48719.
DR   UniGene; Mm.133719; -.
DR   ProteinModelPortal; Q62101; -.
DR   SMR; Q62101; 141-195, 272-329, 426-552, 585-849.
DR   STRING; Q62101; -.
DR   PhosphoSite; Q62101; -.
DR   PRIDE; Q62101; -.
DR   Ensembl; ENSMUST00000002765; ENSMUSP00000002765; ENSMUSG00000002688.
DR   UCSC; uc007nmj.1; mouse.
DR   MGI; MGI:99879; Prkd1.
DR   eggNOG; roNOG09017; -.
DR   GeneTree; ENSGT00600000084006; -.
DR   HOGENOM; HBG314865; -.
DR   HOVERGEN; HBG003564; -.
DR   InParanoid; Q62101; -.
DR   OrthoDB; EOG4548XW; -.
DR   BRENDA; 2.7.11.1; 244.
DR   BRENDA; 2.7.11.13; 244.
DR   ArrayExpress; Q62101; -.
DR   Bgee; Q62101; -.
DR   CleanEx; MM_PRKD1; -.
DR   Genevestigator; Q62101; -.
DR   GermOnline; ENSMUSG00000002688; Mus musculus.
DR   GO; GO:0005938; C:cell cortex; IDA:MGI.
DR   GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004697; F:protein kinase C activity; IEA:EC.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR015727; Protein_Kinase_C_mu-related.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   PANTHER; PTHR22968; PKC_mu_like; 1.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Kinase; Magnesium; Membrane; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Repeat;
KW   Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    918       Serine/threonine-protein kinase D1.
FT                                /FTId=PRO_0000055715.
FT   DOMAIN      428    547       PH.
FT   DOMAIN      589    845       Protein kinase.
FT   ZN_FING     144    194       Phorbol-ester/DAG-type 1.
FT   ZN_FING     276    326       Phorbol-ester/DAG-type 2.
FT   NP_BIND     595    603       ATP (By similarity).
FT   COMPBIAS     16     26       Poly-Ala.
FT   COMPBIAS    198    201       Poly-Arg.
FT   ACT_SITE    712    712       Proton acceptor (By similarity).
FT   BINDING     618    618       ATP (By similarity).
FT   MOD_RES      93     93       Phosphotyrosine (By similarity).
FT   MOD_RES     203    203       Phosphoserine.
FT   MOD_RES     206    206       Phosphoserine (By similarity).
FT   MOD_RES     208    208       Phosphothreonine (By similarity).
FT   MOD_RES     215    215       Phosphothreonine (By similarity).
FT   MOD_RES     241    241       Phosphoserine (By similarity).
FT   MOD_RES     243    243       Phosphoserine (By similarity).
FT   MOD_RES     253    253       Phosphoserine.
FT   MOD_RES     255    255       Phosphoserine (By similarity).
FT   MOD_RES     351    351       Phosphoserine (By similarity).
FT   MOD_RES     401    401       Phosphothreonine (By similarity).
FT   MOD_RES     403    403       Phosphoserine (By similarity).
FT   MOD_RES     405    405       Phosphoserine (By similarity).
FT   MOD_RES     406    406       Phosphothreonine (By similarity).
FT   MOD_RES     407    407       Phosphoserine (By similarity).
FT   MOD_RES     426    426       Phosphoserine (By similarity).
FT   MOD_RES     438    438       Phosphotyrosine (By similarity).
FT   MOD_RES     454    454       Phosphoserine (By similarity).
FT   MOD_RES     466    466       Phosphoserine (By similarity).
FT   MOD_RES     469    469       Phosphotyrosine (By similarity).
FT   MOD_RES     508    508       Phosphotyrosine (By similarity).
FT   MOD_RES     554    554       Phosphoserine (By similarity).
FT   MOD_RES     555    555       Phosphoserine (By similarity).
FT   MOD_RES     744    744       Phosphoserine; by PKC.
FT   MOD_RES     748    748       Phosphoserine; by autocatalysis.
FT   MOD_RES     894    894       Phosphoserine (By similarity).
FT   MOD_RES     896    896       Phosphoserine (By similarity).
FT   MOD_RES     916    916       Phosphoserine; by autocatalysis.
FT   MUTAGEN     744    744       S->A: Loss of basal kinase activity and
FT                                phorbol ester-stimulated kinase activity;
FT                                when associated with A-748.
FT   MUTAGEN     744    744       S->D: High basal kinase activity, loss of
FT                                phorbol ester-stimulated kinase activity;
FT                                when associated with D-748.
FT   MUTAGEN     748    748       S->A: Loss of basal kinase activity and
FT                                phorbol ester-stimulated kinase activity;
FT                                when associated with A-744.
FT   MUTAGEN     748    748       S->D: High basal kinase activity, loss of
FT                                phorbol ester-stimulated kinase activity;
FT                                when associated with D-744.
SQ   SEQUENCE   918 AA;  102067 MW;  234486180521BDDA CRC64;
     MSVPPLLRPP SPLLPAAAAV AAAAAALVPG SGPAPFPAPG AAPAGGISFH LQIGLSREPV
     LLLQDSSGDY SLAHVREMAC SIVDQKFPEC GFYGLYDKIL LFRHDPASDN ILQLVKIASD
     IQEGDLIEVV LSASATFEDF QIRPHALFVH SYRAPAFCDH CGEMLWGLVR QGLKCEGCGL
     NYHKRCAFKI PNNCSGVRRR RLSNVSLTGL GTVRTASAEF STSVPDEPLL SPVSPGFEQK
     SPSESFIGRE KRSNSQSYIG RPIQLDKLLM SKVKVPHTFV IHSYTRPTVC QFCKKLLKGL
     FRQGLQCKDC RFNCHKRCAP KVPNNCLGEV TINGELLSPG AESDVVMEEG SDDNDSERNS
     GLMDDMDEAM VQDTEMALAE GQSGGAEMQD PDADQEDSNR TISPSTSNNI PLMRVVQSVK
     HTKRRSSTVM KEGWMVHYTS KDTLRKRHYW RLDSKCITLF QNDTGSRYYK EIPLSEILCL
     EPAKPSALTP VGATPHCFEI TTANVVYYVG ENVVNPSSSP PNNSVLPSGI GPDVARMWEV
     AIQHALMPVI PKGSSVGSGS NSHKDISVSI SVSNCQIQEN VDISTVYQIF PDEVLGSGQF
     GIVYGGKHRK TGRDVAIKII DKLRFPTKQE SQLRNEVAIL QNLHHPGVVN LECMFETPER
     VFVVMEKLHG DMLEMILSSE KGWLPEHITK FLITQILVAL RHLHFKNIVH CDLKPENVLL
     ASADPFPQVK LCDFGFARII GEKSFRRSVV GTPAYLAPEV LRNKGYNRSL DMWSVGVIIY
     VSLSGTFPFN EDEDIHDQIQ NAAFMYPPNP WKEISHEAID LINNLLQVKM RKRYSVDKTL
     SHPWLQDYQT WLDLRELECR IGERYITHES DDSRWEQYAG EQGLQYPAHL ISLSASHSDS
     PEAEEREMKA LSERVSIL
//
ID   DLG4_MOUSE              Reviewed;         724 AA.
AC   Q62108; Q5NCV5; Q5NCV6; Q5NCV7; Q91WJ1;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   08-MAR-2011, entry version 115.
DE   RecName: Full=Disks large homolog 4;
DE   AltName: Full=Postsynaptic density protein 95;
DE            Short=PSD-95;
DE   AltName: Full=Synapse-associated protein 90;
DE            Short=SAP-90;
DE            Short=SAP90;
GN   Name=Dlg4; Synonyms=Dlgh4, Psd95;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=DBA/2; TISSUE=Brain;
RA   Kohmura N., Yagi T.;
RT   "Mouse homologue of rat PSD-95/SAP90A.";
RL   Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, AND NULL MUTANT.
RX   PubMed=9853749; DOI=10.1038/24790;
RA   Migaud M., Charlesworth P., Dempster M., Webster L.C., Watabe A.M.,
RA   Makhinson M., He Y., Ramsay M.F., Morris R.G.M., Morrison J.H.,
RA   O'Dell T.J., Grant S.G.N.;
RT   "Enhanced long-term potentiation and impaired learning in mice with
RT   mutant postsynaptic density-95 protein.";
RL   Nature 396:433-439(1998).
RN   [5]
RP   INTERACTION WITH SEMA4C.
RX   PubMed=11134026; DOI=10.1074/jbc.M009051200;
RA   Inagaki S., Ohoka Y., Sugimoto H., Fujioka S., Amazaki M.,
RA   Kurinami H., Miyazaki N., Tohyama M., Furuyama T.;
RT   "Sema4c, a transmembrane semaphorin, interacts with a post-synaptic
RT   density protein, PSD-95.";
RL   J. Biol. Chem. 276:9174-9181(2001).
RN   [6]
RP   INTERACTION WITH HTR2A.
RX   PubMed=14988405; DOI=10.1074/jbc.M312106200;
RA   Becamel C., Gavarini S., Chanrion B., Alonso G., Galeotti N.,
RA   Dumuis A., Bockaert J., Marin P.;
RT   "The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets
RT   of PDZ proteins.";
RL   J. Biol. Chem. 279:20257-20266(2004).
RN   [7]
RP   INTERACTION WITH ADR1B, DOMAIN, AND FUNCTION.
RX   PubMed=15358775; DOI=10.1074/jbc.M404876200;
RA   He J., Bellini M., Xu J., Castleberry A.M., Hall R.A.;
RT   "Interaction with cystic fibrosis transmembrane conductance regulator-
RT   associated ligand (CAL) inhibits beta1-adrenergic receptor surface
RT   expression.";
RL   J. Biol. Chem. 279:50190-50196(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415; SER-418 AND
RP   TYR-432, AND MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [9]
RP   INTERACTION WITH LRFN1; LRFN2 AND LRFN4.
RC   STRAIN=Swiss Webster;
RX   PubMed=16828986; DOI=10.1016/j.gene.2006.05.014;
RA   Morimura N., Inoue T., Katayama K., Aruga J.;
RT   "Comparative analysis of structure, expression and PSD95-binding
RT   capacity of Lrfn, a novel family of neuronal transmembrane proteins.";
RL   Gene 380:72-83(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; TYR-240 AND
RP   SER-295, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [11]
RP   INTERACTION WITH LRRC4B AND LRRC4.
RX   PubMed=16980967; DOI=10.1038/nn1763;
RA   Kim S., Burette A., Chung H.S., Kwon S.-K., Woo J., Lee H.W., Kim K.,
RA   Kim H., Weinberg R.J., Kim E.;
RT   "NGL family PSD-95-interacting adhesion molecules regulate excitatory
RT   synapse formation.";
RL   Nat. Neurosci. 9:1294-1301(2006).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240; TYR-397; TYR-580;
RP   TYR-604 AND TYR-715, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-240; SER-415 AND
RP   SER-418, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [14]
RP   INTERACTION WITH ANO2.
RC   STRAIN=C57BL/6; TISSUE=Retina;
RX   PubMed=19474308; DOI=10.1523/JNEUROSCI.5546-08.2009;
RA   Stoehr H., Heisig J.B., Benz P.M., Schoeberl S., Milenkovic V.M.,
RA   Strauss O., Aartsen W.M., Wijnholds J., Weber B.H.F., Schulz H.L.;
RT   "TMEM16B, a novel protein with calcium-dependent chloride channel
RT   activity, associates with a presynaptic protein complex in
RT   photoreceptor terminals.";
RL   J. Neurosci. 29:6809-6818(2009).
RN   [15]
RP   INTERACTION WITH NETO1.
RX   PubMed=19243221; DOI=10.1371/journal.pbio.1000041;
RA   Ng D., Pitcher G.M., Szilard R.K., Sertie A., Kanisek M.,
RA   Clapcote S.J., Lipina T., Kalia L.V., Joo D., McKerlie C., Cortez M.,
RA   Roder J.C., Salter M.W., McInnes R.R.;
RT   "Neto1 is a novel CUB-domain NMDA receptor-interacting protein
RT   required for synaptic plasticity and learning.";
RL   PLoS Biol. 7:E41-E41(2009).
CC   -!- FUNCTION: Interacts with the cytoplasmic tail of NMDA receptor
CC       subunits and shaker-type potassium channels. Required for synaptic
CC       plasticity associated with NMDA receptor signaling. Overexpression
CC       or depletion of DLG4 changes the ratio of excitatory to inhibitory
CC       synapses in hippocampal neurons. May reduce the amplitude of ACCN3
CC       acid-evoked currents by retaining the channel intracellularly. May
CC       regulate the intracellular trafficking of ADR1B.
CC   -!- SUBUNIT: Interacts through its PDZ domains with NETO1. Interacts
CC       through its first two PDZ domains with GRIN2A, GRIN2B, GRIN2C,
CC       GRIN2D, ACCN3, certain splice forms of GRIN1, KCND2, CXADR,
CC       SYNGAP1, KCNA1, KCNA2, KCNA3, KCNA4 and ERBB4. Interacts through
CC       its first PDZ domain with GRIK2, KCNA4 and CRIPT. Interacts
CC       through its second PDZ domain with the PDZ domain of NOS1 or the
CC       C-terminus of CAPON. Interacts through its third PDZ domain with
CC       NLGN1 and CRIPT, and probably with NLGN2 and NLGN3. Interacts
CC       through its guanylate kinase-like domain with DLGAP1/GKAP, DLGAP2,
CC       DLGAP3, DLGAP4, MAP1A, BEGAIN and KIF13B. Isoform 2 interacts
CC       through an L27 domain with HGS/HRS and the first L27 domain of
CC       CASK. Interacts with ANKS1B and PRR7 (By similarity). Interacts
CC       with ADR1B. May interact with HTR2A. Interacts with ADAM22, KLHL17
CC       and LGI1 (By similarity). Interacts with ANO2 through its PDZ
CC       domains. Interacts with FRMPD4 (via C-terminus). Interacts (via
CC       guanylate kinase-like domain) with SIPA1L1 (By similarity).
CC       Interacts (via PDZ1 and PDZ2 domains) with LRRC4; LRRC4B and
CC       SEMA4C. Interacts with LRFN1, LRFN2 and LRFN4, but not with LRFN3
CC       nor LRFN5.
CC   -!- INTERACTION:
CC       Q8K4G5:Ablim1; NbExp=1; IntAct=EBI-300895, EBI-2307994;
CC       Q9WV31:Arc; NbExp=1; IntAct=EBI-300895, EBI-397779;
CC       Q8BKX1:Baiap2; NbExp=1; IntAct=EBI-300895, EBI-771498;
CC       P11798:Camk2a; NbExp=1; IntAct=EBI-300895, EBI-400384;
CC       Q811D0:Dlg1; NbExp=1; IntAct=EBI-300895, EBI-514290;
CC       Q91XM9:Dlg2; NbExp=1; IntAct=EBI-300895, EBI-400138;
CC       P70175:Dlg3; NbExp=1; IntAct=EBI-300895, EBI-396969;
CC       Q9R111:Gda; NbExp=1; IntAct=EBI-300895, EBI-2308876;
CC       P35438:Grin1; NbExp=1; IntAct=EBI-300895, EBI-400084;
CC       P35436:Grin2a; NbExp=2; IntAct=EBI-300895, EBI-400115;
CC       Q01097:Grin2b; NbExp=2; IntAct=EBI-300895, EBI-400125;
CC       Q80TG9:Lrfn2; NbExp=2; IntAct=EBI-300895, EBI-877092;
CC       Q91ZX7:Lrp1; NbExp=1; IntAct=EBI-300895, EBI-300955;
CC       Q924X6:Lrp8; NbExp=1; IntAct=EBI-300895, EBI-432319;
CC       P63085:Mapk1; NbExp=1; IntAct=EBI-300895, EBI-397697;
CC       P46460:Nsf; NbExp=1; IntAct=EBI-300895, EBI-398006;
CC       P63001:Rac1; NbExp=1; IntAct=EBI-300895, EBI-413646;
CC       Q8IUH5:ZDHHC17 (xeno); NbExp=1; IntAct=EBI-300895, EBI-524753;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       (By similarity). Cell junction, synapse, postsynaptic cell
CC       membrane, postsynaptic density (By similarity). Cell junction,
CC       synapse (By similarity). Cell junction, synapse, synaptosome (By
CC       similarity). Note=Membrane-associated. High levels in postsynaptic
CC       density of neurons in the forebrain. Also in presynaptic region of
CC       inhibitory synapses formed by cerebellar basket cells on axon
CC       hillocks of Purkinje cells (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=PSD95-alpha;
CC         IsoId=Q62108-1; Sequence=Displayed;
CC       Name=2; Synonyms=PSD95-beta;
CC         IsoId=Q62108-2; Sequence=VSP_014930;
CC       Name=3;
CC         IsoId=Q62108-3; Sequence=VSP_014931;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The PDZ domain 3 mediates interaction with ADR1B.
CC   -!- DOMAIN: The L27 domain near the N-terminus of isoform 2 is
CC       required for HGS/HRS-dependent targeting to post-synaptic density
CC       (By similarity).
CC   -!- PTM: Palmitoylation of isoform 1 is required for targeting to
CC       postsynaptic density (By similarity).
CC   -!- MISCELLANEOUS: Mice with a stop codon in the third PDZ domain have
CC       impaired spatial learning. NMDA-mediated synaptic plasticity is
CC       lost even though receptor levels and localization are unchanged.
CC       Long-term potentiation of synaptic transmission is enhanced due to
CC       minimal long-term depression.
CC   -!- SIMILARITY: Belongs to the MAGUK family.
CC   -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC   -!- SIMILARITY: Contains 3 PDZ (DHR) domains.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; D50621; BAA09297.1; -; mRNA.
DR   EMBL; AL596185; CAI35168.1; -; Genomic_DNA.
DR   EMBL; AL596185; CAI35169.1; -; Genomic_DNA.
DR   EMBL; AL596185; CAI35170.1; -; Genomic_DNA.
DR   EMBL; BC014807; AAH14807.1; -; mRNA.
DR   IPI; IPI00122094; -.
DR   IPI; IPI00622720; -.
DR   IPI; IPI00626797; -.
DR   RefSeq; NP_001103222.1; NM_001109752.1.
DR   RefSeq; NP_031890.1; NM_007864.3.
DR   UniGene; Mm.27256; -.
DR   ProteinModelPortal; Q62108; -.
DR   SMR; Q62108; 61-402, 430-724.
DR   DIP; DIP-29888N; -.
DR   IntAct; Q62108; 437.
DR   MINT; MINT-136080; -.
DR   STRING; Q62108; -.
DR   PhosphoSite; Q62108; -.
DR   PRIDE; Q62108; -.
DR   Ensembl; ENSMUST00000018700; ENSMUSP00000018700; ENSMUSG00000020886.
DR   Ensembl; ENSMUST00000108589; ENSMUSP00000104230; ENSMUSG00000020886.
DR   GeneID; 13385; -.
DR   KEGG; mmu:13385; -.
DR   UCSC; uc007jtp.1; mouse.
DR   UCSC; uc007jtq.1; mouse.
DR   CTD; 13385; -.
DR   MGI; MGI:1277959; Dlg4.
DR   eggNOG; roNOG08565; -.
DR   HOVERGEN; HBG107814; -.
DR   OMA; WIPTRER; -.
DR   NextBio; 283740; -.
DR   ArrayExpress; Q62108; -.
DR   Bgee; Q62108; -.
DR   CleanEx; MM_DLG4; -.
DR   Genevestigator; Q62108; -.
DR   GermOnline; ENSMUSG00000020886; Mus musculus.
DR   GO; GO:0032281; C:alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex; IDA:MGI.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR   GO; GO:0031234; C:extrinsic to internal side of plasma membrane; IDA:MGI.
DR   GO; GO:0044224; C:juxtaparanode region of axon; IDA:MGI.
DR   GO; GO:0044306; C:neuron projection terminus; IDA:MGI.
DR   GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019717; C:synaptosome; ISS:UniProtKB.
DR   GO; GO:0042043; F:neurexin binding; NAS:UniProtKB.
DR   GO; GO:0008022; F:protein C-terminus binding; NAS:UniProtKB.
DR   GO; GO:0005198; F:structural molecule activity; NAS:UniProtKB.
DR   GO; GO:0007626; P:locomotory behavior; NAS:UniProtKB.
DR   GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IGI:MGI.
DR   GO; GO:0042220; P:response to cocaine; NAS:UniProtKB.
DR   GO; GO:0007416; P:synapse assembly; NAS:UniProtKB.
DR   GO; GO:0016188; P:synaptic vesicle maturation; IDA:MGI.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR016313; M-assoc_guanylate_kinase.
DR   InterPro; IPR019590; MAGUK_PEST_N.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR019583; PDZ_assoc.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF10608; MAGUK_N_PEST; 2.
DR   Pfam; PF00595; PDZ; 3.
DR   Pfam; PF10600; PDZ_assoc; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   PIRSF; PIRSF001741; MAGUK_DLGH; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 3.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50156; PDZ; 3.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 3.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Lipoprotein;
KW   Membrane; Palmitate; Phosphoprotein; Postsynaptic cell membrane;
KW   Repeat; SH3 domain; Synapse; Synaptosome.
FT   CHAIN         1    724       Disks large homolog 4.
FT                                /FTId=PRO_0000094561.
FT   DOMAIN       65    151       PDZ 1.
FT   DOMAIN      160    246       PDZ 2.
FT   DOMAIN      313    393       PDZ 3.
FT   DOMAIN      428    498       SH3.
FT   DOMAIN      534    709       Guanylate kinase-like.
FT   MOD_RES     142    142       Phosphoserine.
FT   MOD_RES     240    240       Phosphotyrosine.
FT   MOD_RES     295    295       Phosphoserine.
FT   MOD_RES     397    397       Phosphotyrosine.
FT   MOD_RES     415    415       Phosphoserine.
FT   MOD_RES     418    418       Phosphoserine.
FT   MOD_RES     432    432       Phosphotyrosine.
FT   MOD_RES     580    580       Phosphotyrosine.
FT   MOD_RES     604    604       Phosphotyrosine.
FT   MOD_RES     701    701       Phosphotyrosine (By similarity).
FT   MOD_RES     715    715       Phosphotyrosine.
FT   LIPID         3      3       S-palmitoyl cysteine (By similarity).
FT   LIPID         5      5       S-palmitoyl cysteine (By similarity).
FT   VAR_SEQ       1     10       MDCLCIVTTK -> MSQRPRAPRSALWLLAPPLLRWAPPLL
FT                                TVLHSDLFQALLDILDYYEACISESQ (in isoform
FT                                2).
FT                                /FTId=VSP_014930.
FT   VAR_SEQ      51     53       Missing (in isoform 3).
FT                                /FTId=VSP_014931.
FT   CONFLICT    203    203       D -> E (in Ref. 3; AAH14807).
SQ   SEQUENCE   724 AA;  80472 MW;  7EFFC99E1FFF90BA CRC64;
     MDCLCIVTTK KYRYQDEDTP PLEHSPAHLP NQANSPPVIV NTDTLEAPGY ELQVNGTEGE
     MEYEEITLER GNSGLGFSIA GGTDNPHIGD DPSIFITKII PGGAAAQDGR LRVNDSILFV
     NEVDVREVTH SAAVEALKEA GSIVRLYVMR RKPPAEKIIE IKLIKGPKGL GFSIAGGVGN
     QHIPGDNSIY VTKIIEGGAA HKDGRLQIGD KILAVNSVGL EDVMHEDAVA ALKNTYDVVY
     LKVAKPSNAY LSDSYAPPDI TTSYSQHLDN EISHSSYLGT DYPTAMTPTS PRRYSPVAKD
     LLGEEDIPRE PRRIVIHRGS TGLGFNIVGG EDGEGIFISF ILAGGPADLS GELRKGDQIL
     SVNGVDLRNA SHEQAAIALK NAGQTVTIIA QYKPEEYSRF EAKIHDLREQ LMNSSLGSGT
     ASLRSNPKRG FYIRALFDYD KTKDCGFLSQ ALSFHFGDVL HVIDASDEEW WQARRVHSDS
     ETDDIGFIPS KRRVERREWS RLKAKDWGSS SGSQGREDSV LSYETVTQME VHYARPIIIL
     GPTKDRANDD LLSEFPDKFG SCVPHTTRPK REYEIDGRDY HFVSSREKME KDIQAHKFIE
     AGQYNSHLYG TSVQSVREVA EQGKHCILDV SANAVRRLQA AHLHPIAIFI RPRSLENVLE
     INKRITEEQA RKAFDRATKL EQEFTECFSA IVEGDSFEEI YHKVKRVIED LSGPYIWVPA
     RERL
//
ID   PTN14_MOUSE             Reviewed;        1189 AA.
AC   Q62130;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type 14;
DE            EC=3.1.3.48;
DE   AltName: Full=Protein-tyrosine phosphatase PTP36;
GN   Name=Ptpn14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CB-17-SCID; TISSUE=Thymus;
RX   MEDLINE=94354845; PubMed=8074693; DOI=10.1006/bbrc.1994.2207;
RA   Sawada M., Ogata M., Fujino Y., Hamaoka T.;
RT   "cDNA cloning of a novel protein tyrosine phosphatase with homology to
RT   cytoskeletal protein 4.1 and its expression in T-lineage cells.";
RL   Biochem. Biophys. Res. Commun. 203:479-484(1994).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-593 AND SER-594, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May be involved in the regulation of T-cell development.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC   -!- TISSUE SPECIFICITY: Thymus; in cells of both hematopoietic and
CC       non-hematopoietic origins.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class subfamily.
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D31842; BAA06628.1; -; mRNA.
DR   IPI; IPI00122168; -.
DR   PIR; JC2366; JC2366.
DR   UniGene; Mm.4498; -.
DR   ProteinModelPortal; Q62130; -.
DR   SMR; Q62130; 21-305, 897-1186.
DR   STRING; Q62130; -.
DR   PhosphoSite; Q62130; -.
DR   PRIDE; Q62130; -.
DR   Ensembl; ENSMUST00000027898; ENSMUSP00000027898; ENSMUSG00000026604.
DR   Ensembl; ENSMUST00000097442; ENSMUSP00000095051; ENSMUSG00000026604.
DR   UCSC; uc007eau.1; mouse.
DR   MGI; MGI:102467; Ptpn14.
DR   eggNOG; roNOG14007; -.
DR   HOGENOM; HBG444644; -.
DR   HOVERGEN; HBG053757; -.
DR   InParanoid; Q62130; -.
DR   OrthoDB; EOG4320X9; -.
DR   BRENDA; 3.1.3.48; 244.
DR   ArrayExpress; Q62130; -.
DR   Bgee; Q62130; -.
DR   Genevestigator; Q62130; -.
DR   GermOnline; ENSMUSG00000026604; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR014392; Tyr_Pase_non-rcpt_typ-14/21.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PIRSF; PIRSF000934; Tyr-Ptase_nr14; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00194; PTPc; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Hydrolase; Phosphoprotein;
KW   Protein phosphatase.
FT   CHAIN         1   1189       Tyrosine-protein phosphatase non-receptor
FT                                type 14.
FT                                /FTId=PRO_0000219438.
FT   DOMAIN       21    306       FERM.
FT   DOMAIN      911   1182       Tyrosine-protein phosphatase.
FT   REGION     1123   1129       Substrate binding (By similarity).
FT   COMPBIAS    566    573       Poly-Pro.
FT   COMPBIAS    635    639       Poly-Gly.
FT   COMPBIAS    712    718       Poly-Glu.
FT   ACT_SITE   1123   1123       Phosphocysteine intermediate (By
FT                                similarity).
FT   BINDING    1167   1167       Substrate (By similarity).
FT   MOD_RES     486    486       Phosphoserine (By similarity).
FT   MOD_RES     512    512       Phosphoserine (By similarity).
FT   MOD_RES     584    584       Phosphoserine (By similarity).
FT   MOD_RES     593    593       Phosphoserine.
FT   MOD_RES     594    594       Phosphoserine.
SQ   SEQUENCE   1189 AA;  135031 MW;  2B85BE5F9C723303 CRC64;
     MPFGLKLRRT RRYNVLSKNC FVARIRLLDS NVIECTLSVE STGQECLEAV AQRLELRETH
     YFGLWFLSKS QQARWVELEK PLKKHLDKFA NEPLLFFGVM FYVPNVSRLQ QEATRYQYYL
     QVKKDVLEGR LRCSLEQVIR LAGLAVQADF GDYNQFDSQE FLREYVLFPM DLAMEEAALE
     ELTQKVAQEH KAHSGILPAE AELMYINEVE RLDGFGQEIF PVKDSHGNSV HLGIFFMGIF
     VRNRVGRQAV IYRWNDIGSV THSKAAILLE LIDKEETALF HTDDIENAKY ISRLFTTRHK
     FYKQNKICTE QSNSPPPIRR QPTWSRSSLP RQQPYILPPM HVQCSEHYSE THTSQDSIFP
     GNEEALYCRS HNSLDLNYLN GTVTNGSVCS VHSVNSLSCS QSFIQASPVS SNLSIPGSDI
     MRADYIPSHR HSTIIVPSYR PTPDYETVMR QMKRGLMHAD SQSRSLRNLN IINTHAYNQP
     EELVYSQPEM RERHPYTVPY AHQGCYGHKL VSPSDQMNPQ NCAMPIKPGA SSISHTVSTP
     ELANMQLQGA QHYSTAHMLK NYLFRPPPPY PRPRPATSTP DLASHRHKYV SGSSPDLVTR
     KVQLSVKTFQ EDSSPVVHQS LQEVSEPLTA TKHHGGGGGT VNKRHSLEVM NSMVRGMEAM
     TLKSLNIPMA RRNTLREQGP SEETGGHEVH GLPQYHHKKT FSDATMLIHS SESEEEEETL
     EAAPQVPVLR EKVEYSAQLQ AALARIPNRP PPEYPGPRKS VSNGALRQDQ GTPLPAMARC
     RVLRHGPSKA LSVSRAEQLA VNGASLGPSI SEPDLTSVKE RVKKEPVKER PVSEMFSLED
     SIIEREMMIR NLEKQKMTGP QAQKRPLMLA ALNGLSVARV SGREDGRHDA TRVPIDERLR
     ALKKKLEDGM VFTEYEQIPN KKANGVFSTA TLPENAERSR IREVVPYEEN RVELIPTKEN
     NTGYINASHI KVVVGGSEWH YIATQGPLPH TCHDFWQMVW EQGVNVIAMV TAEEEGGRTK
     SHRYWPKLGS KHSSATYGKF KVTTKFRTDS GCYATTGLKV KHLLSGQERT VWHLQYTDWP
     HHGCPEDVQG FLSYLEEIQS VRRHTNSVLE GIRTRHPPIV VHCSAGVGRT GVVILSELMI
     YCLEHNEKVE VPTMLRFLRE QRMFMIQTIA QYKFVYQVLV QFLQNSRLI
//
ID   PTPRR_MOUSE             Reviewed;         656 AA.
AC   Q62132; Q64491; Q64492; Q9QUH9;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 103.
DE   RecName: Full=Receptor-type tyrosine-protein phosphatase R;
DE            Short=R-PTP-R;
DE            EC=3.1.3.48;
DE   AltName: Full=Phosphotyrosine phosphatase 13;
DE   AltName: Full=Protein-tyrosine-phosphatase SL;
DE   Flags: Precursor;
GN   Name=Ptprr; Synonyms=Ptp13;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=95138207; PubMed=7836467; DOI=10.1074/jbc.270.25.15076;
RA   Ogata M., Sawada M., Fujino Y., Hamaoka T.;
RT   "cDNA cloning and characterization of a novel receptor-type protein
RT   tyrosine phosphatase expressed predominantly in the brain.";
RL   J. Biol. Chem. 270:2337-2343(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA), AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=95134232; PubMed=7832766;
RA   Hendriks W., Schepens J., Brugman C., Zeeuwen P., Wieringa B.;
RT   "A novel receptor-type protein tyrosine phosphatase with a single
RT   catalytic domain is specifically expressed in mouse brain.";
RL   Biochem. J. 305:499-504(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Colon;
RX   MEDLINE=20170777; PubMed=10705342;
RX   DOI=10.1002/(SICI)1097-0185(20000301)258:3<221::AID-AR1>3.0.CO;2-W;
RA   Augustine K.A., Silbiger S.M., Bucay N., Ulias L., Boynton A.,
RA   Trebasky L.D., Medlock E.S.;
RT   "Protein tyrosine phosphatase (PC12, Br7,Sl) family: expression
RT   characterization in the adult human and mouse.";
RL   Anat. Rec. 258:221-234(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GAMMA), FUNCTION, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=20403321; PubMed=10949045;
RA   Augustine K.A., Rossi R.M., Silbiger S.M., Bucay N., Duryea D.,
RA   Marshall W.S., Medlock E.S.;
RT   "Evidence that the protein tyrosine phosphatase (PC12,Br7,Sl) gamma
RT   (-) isoform modulates chondrogenic patterning and growth.";
RL   Int. J. Dev. Biol. 44:361-371(2000).
RN   [5]
RP   FUNCTION, INTERACTION WITH MAPK1; MAPK3 AND MAPK14, SUBCELLULAR
RP   LOCATION, AND MUTAGENESIS OF SER-338; CYS-587 AND ARG-593.
RC   TISSUE=Brain;
RX   MEDLINE=20069779; PubMed=10601328; DOI=10.1083/jcb.147.6.1129;
RA   Blanco-Aparicio C., Torres J., Pulido R.;
RT   "A novel regulatory mechanism of MAP kinases activation and nuclear
RT   translocation mediated by PKA and the PTP-SL tyrosine phosphatase.";
RL   J. Cell Biol. 147:1129-1136(1999).
CC   -!- FUNCTION: Sequesters mitogen-activated protein kinases (MAPKs)
CC       such as MAPK1, MAPK3 and MAPK14 in the cytoplasm in an inactive
CC       form. The MAPKs bind to a dephosphorylated kinase interacting
CC       motif, phosphorylation of which by the protein kinase A complex
CC       releases the MAPKs for activation and translocation into the
CC       nucleus. Isoform gamma may have a role in patterning and cellular
CC       proliferation of skeletal elements in the
CC       precartilaginous/cartilaginous skeleton.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- SUBUNIT: Interacts with MAPKs.
CC   -!- SUBCELLULAR LOCATION: Isoform Alpha: Cell membrane; Single-pass
CC       type I membrane protein.
CC   -!- SUBCELLULAR LOCATION: Isoform Beta: Cytoplasm. Note=Locates to the
CC       areas within the cytoplasm.
CC   -!- SUBCELLULAR LOCATION: Isoform Gamma: Cytoplasm. Note=Locates to
CC       the areas within the cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=Alpha; Synonyms=PTPBR7;
CC         IsoId=Q62132-1; Sequence=Displayed;
CC       Name=Beta; Synonyms=PTP-SL;
CC         IsoId=Q62132-2; Sequence=VSP_005159, VSP_005160;
CC       Name=Gamma;
CC         IsoId=Q62132-3; Sequence=VSP_005161;
CC   -!- TISSUE SPECIFICITY: Expressed in the heart, brain, spleen, lung,
CC       liver, skeletal muscle, kidney and testis. Isoform alpha is
CC       expressed throughout the granular layer of the cerebellar but not
CC       within the Purkinje cells, also in the villi of the ileum and
CC       jejunum and both the villi and crypts of the duodenum. Isoform
CC       beta is expressed only in the Purkinje cells. Isoform gamma is
CC       expressed throughout the brain, the villi and crypts of the
CC       duodenum, jejunum and ileum and expressed at low levels in the
CC       proximal colon.
CC   -!- DEVELOPMENTAL STAGE: Isoform gamma is the only family member
CC       developmentally expressed. Expressed throughout the brain in 15.5
CC       day embryos and in cranial nerve cells, skeletal tissues such as
CC       neural crest-derived face bones, and the periphery of
CC       cartiliginous skeletal elements including the rib and vertebrae
CC       anlage. On day 17.5, expression was observed throughout the brain,
CC       trigeminal ganglion, cranofacial bones, oral-facial structures,
CC       cervical vertebrae, axis and the ileum. Expression continued in
CC       the vertebral column throughout ossification.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 7 subfamily.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA82958.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; D31898; BAA06696.1; -; mRNA.
DR   EMBL; Z30313; CAA82957.1; -; mRNA.
DR   EMBL; Z30313; CAA82958.1; ALT_INIT; mRNA.
DR   EMBL; AF129509; AAD29673.1; -; mRNA.
DR   EMBL; AF041866; AAD09171.1; -; mRNA.
DR   IPI; IPI00122172; -.
DR   IPI; IPI00224149; -.
DR   IPI; IPI00349706; -.
DR   PIR; A55574; A55574.
DR   RefSeq; NP_001155310.1; NM_001161838.1.
DR   RefSeq; NP_001155311.1; NM_001161839.1.
DR   RefSeq; NP_001155312.1; NM_001161840.1.
DR   RefSeq; NP_035347.1; NM_011217.2.
DR   UniGene; Mm.336316; -.
DR   PDB; 1JLN; X-ray; 1.81 A; A=361-655.
DR   PDBsum; 1JLN; -.
DR   ProteinModelPortal; Q62132; -.
DR   SMR; Q62132; 360-655.
DR   STRING; Q62132; -.
DR   PhosphoSite; Q62132; -.
DR   PRIDE; Q62132; -.
DR   Ensembl; ENSMUST00000063470; ENSMUSP00000064392; ENSMUSG00000020151.
DR   Ensembl; ENSMUST00000105271; ENSMUSP00000100907; ENSMUSG00000020151.
DR   GeneID; 19279; -.
DR   KEGG; mmu:19279; -.
DR   UCSC; uc007hbp.1; mouse.
DR   UCSC; uc007hbs.1; mouse.
DR   CTD; 19279; -.
DR   MGI; MGI:109559; Ptprr.
DR   GeneTree; ENSGT00560000077216; -.
DR   HOGENOM; HBG716490; -.
DR   HOVERGEN; HBG001594; -.
DR   InParanoid; Q62132; -.
DR   OMA; PIGLQER; -.
DR   OrthoDB; EOG4B8JD5; -.
DR   PhylomeDB; Q62132; -.
DR   BRENDA; 3.1.3.48; 244.
DR   NextBio; 296188; -.
DR   ArrayExpress; Q62132; -.
DR   Bgee; Q62132; -.
DR   CleanEx; MM_PTPRR; -.
DR   Genevestigator; Q62132; -.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:MGI.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0001701; P:in utero embryonic development; ISS:UniProtKB.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR008356; Tyr_Pase_KIM-con.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   InterPro; IPR016334; Tyr_Pase_rcpt_R/non-rcpt_5.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PIRSF; PIRSF001997; PTPRR; 1.
DR   PRINTS; PR01778; KIMPTPASE.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Cytoplasm;
KW   Glycoprotein; Hydrolase; Membrane; Phosphoprotein;
KW   Protein phosphatase; Receptor; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     23       Potential.
FT   CHAIN        24    656       Receptor-type tyrosine-protein
FT                                phosphatase R.
FT                                /FTId=PRO_0000025460.
FT   TOPO_DOM     24    226       Extracellular (Potential).
FT   TRANSMEM    227    247       Helical; (Potential).
FT   TOPO_DOM    248    656       Cytoplasmic (Potential).
FT   DOMAIN      392    646       Tyrosine-protein phosphatase.
FT   REGION      587    593       Substrate binding (By similarity).
FT   ACT_SITE    587    587       Phosphocysteine intermediate (By
FT                                similarity).
FT   BINDING     553    553       Substrate (By similarity).
FT   BINDING     631    631       Substrate (By similarity).
FT   MOD_RES     338    338       Phosphoserine; by PKA.
FT   MOD_RES     369    369       Phosphotyrosine (By similarity).
FT   CARBOHYD    128    128       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1    244       Missing (in isoform Gamma).
FT                                /FTId=VSP_005161.
FT   VAR_SEQ       1    107       Missing (in isoform Beta).
FT                                /FTId=VSP_005159.
FT   VAR_SEQ     108    121       LPIPAANVIVVTLQ -> MHRNTRSVSTPTLQ (in
FT                                isoform Beta).
FT                                /FTId=VSP_005160.
FT   MUTAGEN     338    338       S->A: Loss of phosphorylation by PKA,
FT                                constitutive MAPK binding.
FT   MUTAGEN     338    338       S->E: Mimics phosphorylation by PKA,
FT                                prevents MAPK binding.
FT   MUTAGEN     587    587       C->S: Loss of phosphatase activity.
FT   MUTAGEN     593    593       R->M: Loss of phosphatase activity.
FT   HELIX       363    372
FT   HELIX       379    387
FT   TURN        388    390
FT   HELIX       391    398
FT   TURN        406    408
FT   HELIX       414    417
FT   HELIX       427    429
FT   HELIX       442    444
FT   STRAND      447    451
FT   HELIX       454    456
FT   STRAND      460    464
FT   HELIX       469    471
FT   HELIX       472    481
FT   STRAND      486    489
FT   STRAND      493    498
FT   STRAND      506    511
FT   STRAND      514    523
FT   STRAND      525    536
FT   STRAND      539    548
FT   HELIX       561    575
FT   STRAND      583    591
FT   HELIX       592    610
FT   STRAND      611    613
FT   HELIX       615    625
FT   HELIX       633    648
SQ   SEQUENCE   656 AA;  74036 MW;  31FA82F582992720 CRC64;
     MRRAVGFPAL CLLLNLHAAG CFSRNNDHFL AIRQKKSWKP VFIYDHSQDI KKSLDIAQEA
     YKHNYHSPSE VQISKHHQII NSAFPRPAYD PSLNLLAESD QDLEIENLPI PAANVIVVTL
     QMDITKLNIT LLRIFRQGVA AALGLLPQQV HINRLIEKKN QVELFVSPGN RKPGETQALQ
     AEEVLRSLNV DGLHQSLPQF GITDVAPEKN VLQGQHEADK IWSKEGFYAV VIFLSIFIII
     VTCLMIIYRL KERLQLSLRQ DKEKNQEIHL SPIARQQAQS EAKTTHSMVQ PDQAPKVLNV
     VVDPQGQCTP EIRNSTSTSV CPSPFRMKPI GLQERRGSNV SLTLDMSSLG SVEPFVAVST
     PREKVAMEYL QSASRVLTRS QLRDVVASSH LLQSEFMEIP MNFVDPKEID IPRHGTKNRY
     KTILPNPLSR VCLRPKNITD SLSTYINANY IRGYSGKEKA FIATQGPMIN TVNDFWQMVW
     QEDSPVIVMI TKLKEKNEKC VLYWPEKRGI YGKVEVLVTG VTECDNYTIR NLVLKQGSHT
     QHVKHYWYTS WPDHKTPDSA QPLLQLMLDV EEDRLASEGR GPVVVHCSAG IGRTGCFIAT
     SIGCQQLKEE GVVDALSIVC QLRVDRGGMV QTSEQYEFVH HALCLFESRL SPETVE
//
ID   DAG1_MOUSE              Reviewed;         893 AA.
AC   Q62165; Q61094; Q61141; Q61497;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2001, sequence version 4.
DT   08-MAR-2011, entry version 106.
DE   RecName: Full=Dystroglycan;
DE   AltName: Full=Dystrophin-associated glycoprotein 1;
DE   Contains:
DE     RecName: Full=Alpha-dystroglycan;
DE              Short=Alpha-DG;
DE   Contains:
DE     RecName: Full=Beta-dystroglycan;
DE              Short=Beta-DG;
DE   Flags: Precursor;
GN   Name=Dag1; Synonyms=Dag-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, FUNCTION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=129/SvJ;
RX   MEDLINE=97318791; PubMed=9175728; DOI=10.1093/hmg/6.6.831;
RA   Williamson R.A., Henry M.D., Daniels K.J., Hrstka R.F., Lee J.C.,
RA   Sunada Y., Ibraghimov-Beskrovnaya O., Campbell K.P.;
RT   "Dystroglycan is essential for early embryonic development: disruption
RT   of Reichert's membrane in Dag1-null mice.";
RL   Hum. Mol. Genet. 6:831-841(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-650.
RC   TISSUE=Skeletal muscle;
RX   MEDLINE=97210754; PubMed=9057818; DOI=10.1016/S0945-053X(05)80032-0;
RA   Brancaccio A., Ruegg M.A., Engel J.;
RT   "Cloning and sequencing of mouse skeletal muscle alpha-dystroglycan.";
RL   Matrix Biol. 14:681-685(1995).
RN   [4]
RP   SEQUENCE REVISION TO 142-143.
RA   Brancaccio A.;
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 352-650, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/10; TISSUE=Skeletal muscle;
RX   MEDLINE=95135414; PubMed=7833916; DOI=10.1093/hmg/3.9.1589;
RA   Gorecki D.C., Derry J.M.J., Barnard E.A.;
RT   "Dystroglycan: brain localisation and chromosome mapping in the
RT   mouse.";
RL   Hum. Mol. Genet. 3:1589-1597(1994).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 620-893.
RC   STRAIN=C57BL/6J; TISSUE=Decidua;
RX   MEDLINE=97026286; PubMed=8872465; DOI=10.1093/hmg/5.9.1259;
RA   Yotsumoto S., Fujiwara H., Horton J.H., Mosby T.A., Wang X., Cui Y.,
RA   Ko M.S.H.;
RT   "Cloning and expression analyses of mouse dystroglycan gene: specific
RT   expression in maternal decidua at the peri-implantation stage.";
RL   Hum. Mol. Genet. 5:1259-1267(1996).
RN   [7]
RP   DISULFIDE BOND.
RX   MEDLINE=99116369; PubMed=9917844;
RX   DOI=10.1111/j.1749-6632.1998.tb10119.x;
RA   Brancaccio A., Jeno P., Engel J.;
RT   "A single disulfide bridge (Cys182-Cys264) is crucial for alpha-
RT   dystroglycan N-terminal domain stability.";
RL   Ann. N. Y. Acad. Sci. 857:228-231(1998).
RN   [8]
RP   INTERACTION WITH SGCD.
RX   PubMed=9864373; DOI=10.1083/jcb.143.7.2033;
RA   Chan Y.-M., Boennemann C.G., Lidov H.G.W., Kunkel L.M.;
RT   "Molecular organization of sarcoglycan complex in mouse myotubes in
RT   culture.";
RL   J. Cell Biol. 143:2033-2044(1998).
RN   [9]
RP   PHOSPHORYLATION, AND INTERACTION WITH DMD.
RX   PubMed=11495720; DOI=10.1016/S0898-6568(01)00188-7;
RA   Ilsley J.L., Sudol M., Winder S.J.;
RT   "The interaction of dystrophin with beta-dystroglycan is regulated by
RT   tyrosine phosphorylation.";
RL   Cell. Signal. 13:625-632(2001).
RN   [10]
RP   DEVELOPMENTAL STAGE.
RX   MEDLINE=22557185; PubMed=12670716; DOI=10.1016/S0169-328X(03)00055-X;
RA   Henion T.R., Qu Q., Smith F.I.;
RT   "Expression of dystroglycan, fukutin and POMGnT1 during mouse
RT   cerebellar development.";
RL   Brain Res. Mol. Brain Res. 112:177-181(2003).
RN   [11]
RP   DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=12843252;
RA   Previtali S.C., Nodari A., Taveggia C., Pardini C., Dina G., Villa A.,
RA   Wrabetz L., Quattrini A., Feltri M.L.;
RT   "Expression of laminin receptors in schwann cell differentiation:
RT   evidence for distinct roles.";
RL   J. Neurosci. 23:5520-5530(2003).
RN   [12]
RP   FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND
RP   LIGAND-BINDING.
RX   PubMed=12797959; DOI=10.1016/S0896-6273(03)00301-5;
RA   Saito F., Moore S.A., Barresi R., Henry M.D., Messing A.,
RA   Ross-Barta S.E., Cohn R.D., Williamson R.A., Sluka K.A., Sherman D.L.,
RA   Brophy P.J., Schmelzer J.D., Low P.A., Wrabetz L., Feltri M.L.,
RA   Campbell K.P.;
RT   "Unique role of dystroglycan in peripheral nerve myelination, nodal
RT   structure, and sodium channel stabilization.";
RL   Neuron 38:747-758(2003).
RN   [13]
RP   STRUCTURE OF CARBOHYDRATES, LIGAND-BINDING, ADENOVIRUS BINDING, AND
RP   MASS SPECTROMETRY.
RX   PubMed=20044576; DOI=10.1126/science.1180512;
RA   Yoshida-Moriguchi T., Yu L., Stalnaker S.H., Davis S., Kunz S.,
RA   Madson M., Oldstone M.B., Schachter H., Wells L., Campbell K.P.;
RT   "O-mannosyl phosphorylation of alpha-dystroglycan is required for
RT   laminin binding.";
RL   Science 327:88-92(2010).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 58-303 IN COMPLEX WITH
RP   LIGAND.
RX   PubMed=15326183; DOI=10.1074/jbc.C400353200;
RA   Bozic D., Sciandra F., Lamba D., Brancaccio A.;
RT   "The structure of the N-terminal region of murine skeletal muscle
RT   alpha-dystroglycan discloses a modular architecture.";
RL   J. Biol. Chem. 279:44812-44816(2004).
CC   -!- FUNCTION: The dystroglycan complex is involved in a number of
CC       processes including laminin and basement membrane assembly,
CC       sacrolemmal stability, cell survival, peripheral nerve
CC       myelination, nodal structure, cell migration, and epithelial
CC       polarization.
CC   -!- FUNCTION: Alpha-dystroglycan is an extracellular peripheral
CC       glycoprotein that acts as a receptor for both extracellular matrix
CC       proteins containing laminin-G domains, and for certain
CC       adenoviruses. Receptor for laminin-2 (LAMA2) and agrin in
CC       peripheral nerve Schwann cells. Also receptor for lymphocytic
CC       choriomeningitis virus, Old World Lassa fever virus, and clade C
CC       New World arenaviruses.
CC   -!- FUNCTION: Beta-dystroglycan is a transmembrane protein that plays
CC       important roles in connecting the extracellular matrix to the
CC       cytoskeleton. Acts as a cell adhesion receptor in both muscle and
CC       non-muscle tissues. Receptor for both DMD and UTRN and, through
CC       these interactions, scaffolds axin to the cytoskeleton. Also
CC       functions in cell adhesion-mediated signaling and implicated in
CC       cell polarity (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity). Heterodimer of alpha- and beta-
CC       dystroglycan subunits which are the central components of the
CC       dystrophin-glycoprotein complex. This complex then can form a
CC       dystrophin-associated glycoprotein complex (DGC) which is composed
CC       of three subcomplexes: a cytoplasmic complex comprised of DMD (or
CC       UTRN), DTNA and a number of syntrophins, such as SNTB1, SNTB2,
CC       SNTG1 and SNTG2, the transmembrane dystroglycan complex, and the
CC       sarcoglycan-sarcospan complex. Interacts (via the N-terminal of
CC       alphaDAG1) with LARGE; the interaction enhances laminin binding
CC       (By similarity). Interacts with AGR2 and AGR3. Interacts
CC       (betaDAG1) with DMD; the interaction is inhibited by
CC       phosphorylaion on the PPXY motif. Interacts (betaDAG1, via its
CC       PPXY motif) with UTRN (via its WWW and ZZ domains); the
CC       interaction is inhibited by phosphorylation on the PPXY motif.
CC       Interacts (betaDAG1, via its phosphorylated PPXY motif) with the
CC       SH2 domain-containing proteins, FYN, CSK, NCK and SHC. Interacts
CC       (betaDAG1) with CAV3 (via a central WW-like domain); the
CC       interaction disrupts the binding of DMD (By similarity). Interacts
CC       with SGCD.
CC   -!- SUBCELLULAR LOCATION: Alpha-dystroglycan: Secreted, extracellular
CC       space (By similarity).
CC   -!- SUBCELLULAR LOCATION: Beta-dystroglycan: Cell membrane; Single-
CC       pass type I membrane protein (By similarity). Cytoplasm,
CC       cytoskeleton. Nucleus, nucleoplasm. Note=The monomeric form
CC       translocates to the nucleus via the action of importins and
CC       depends on RAN. Nuclear transport is inhibited by Tyr-892
CC       phosphorylation. In skeletal muscle, this phosphorylated form
CC       locates to a vesicular internal membrane compartment. In
CC       peripheral nerves, localizes to the Schwann cell membrane.
CC       Colocalizes with ERM proteins in Schwann-cell microvilli.
CC   -!- TISSUE SPECIFICITY: Expressed in a variety of tissues. In brain,
CC       expressed in the hippocampal formation, the olfactory bulb, the
CC       cerebellum and the thalamus. In the peripheral nerve system,
CC       expressed in Schwann cells.
CC   -!- DEVELOPMENTAL STAGE: Broadly expressed in late embryonic and early
CC       postnatal cerebellar neurons, including premigratory granule
CC       neurons of the external granule cell layer, but expression is
CC       largely down-regulated. Weak expression in Purkinje cells
CC       throughout development. Alpha- and beta-DG proteins are also
CC       present on the Bergmann glial scaffolds used by granule cells
CC       during early postnatal radial migration. In the peripheral nerve
CC       system, expression briefly precedes and parallels myelination.
CC       First expressed at E18.5 in spinal roots, dorsal root ganglions
CC       and nerve trunks. At P1, at the onset of myelination, expressed in
CC       motor roots. At P5 and P15, expression progressively increases in
CC       sensory roots and peripheral nerves. Between postnatal 2 weeks and
CC       18 months, localizes at the nodes of Ranvier as well as at the
CC       Schwann cell outer membrane.
CC   -!- PTM: O- and N-glycosylated (By similarity). Alpha-dystroglycan is
CC       heavily O-glycosylated comprising of up to two thirds of its mass
CC       and the carbohydrate composition differs depending on tissue type.
CC       Mucin-type O-glycosylation is important for ligand binding
CC       activity. O-mannosylation of alpha-DAG1 is found in high abundance
CC       in both brain and muscle where the most abundant glycan is Sia-
CC       alpha-2-3-Gal-beta-1-4-Glc-NAc-beta-1-2-Man. O-glycosylated in the
CC       N-terminal region with a core 1 or possibly core 8 glycan. The
CC       beta subunit is N-glycosylated (By similarity). In muscle,
CC       glycosylation on Thr-379 by a phosphorylated O-mannosyl glycan (N-
CC       acetylamido)-2-deoxyglucosyl-beta-1,4-6-phosphomannose is mediated
CC       by like-acetylglucosaminyltransferase (LARGE) protein amd is
CC       required for laminin binding. O-mannosylation is also required for
CC       binding lymphocytic choriomeningitis virus, Old World Lassa fever
CC       virus, and clade C New World arenaviruses.
CC   -!- PTM: Autolytic cleavage produces the alpha and beta subunits. In
CC       cutaneous cells, as well as in certain pathological conditions,
CC       shedding of beta-dystroglcan can occur releasing a peptide of
CC       about 30 kDa (By similarity).
CC   -!- PTM: SRC-mediated phosphorylation of the PPXY motif of the beta
CC       subunit recruits SH2 domain-containing proteins, but inhibits
CC       binding to WWW domain-containing proteins, DMD and UTRN. This
CC       phosphorylation also inhibits nuclear entry (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Homozygous null mice embryos exhibit gross
CC       developmental abonormalities, beginning around 6.5 days of
CC       gestation, in the Reichert's membrane, an extra-embryonic basement
CC       membrane. In peripheral nerves, ablation of DAG1 from 4 week-old
CC       mice causes abnormalities in nerve structure and function
CC       including mildly impaired sorting of axons, dysmyelination, axonal
CC       loss and aberrrant nerve conduction. Laminin-binding is lost and
CC       there is disruption of the Schwann cell dystroglycan complex.
CC   -!- SIMILARITY: Contains 1 peptidase S72 domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U48854; AAA99779.2; -; Genomic_DNA.
DR   EMBL; BC007150; AAH07150.1; -; mRNA.
DR   EMBL; X86073; CAA60031.1; -; mRNA.
DR   EMBL; Z34532; CAA84293.1; -; mRNA.
DR   EMBL; U43512; AAC52853.1; -; mRNA.
DR   IPI; IPI00122273; -.
DR   PIR; S59630; S59630.
DR   RefSeq; NP_034147.1; NM_010017.3.
DR   UniGene; Mm.477413; -.
DR   UniGene; Mm.7524; -.
DR   PDB; 1U2C; X-ray; 2.30 A; A=58-303.
DR   PDBsum; 1U2C; -.
DR   ProteinModelPortal; Q62165; -.
DR   SMR; Q62165; 58-303.
DR   DisProt; DP00491; -.
DR   MINT; MINT-145749; -.
DR   STRING; Q62165; -.
DR   MEROPS; S72.001; -.
DR   PhosphoSite; Q62165; -.
DR   PRIDE; Q62165; -.
DR   Ensembl; ENSMUST00000080435; ENSMUSP00000079294; ENSMUSG00000039952.
DR   GeneID; 13138; -.
DR   KEGG; mmu:13138; -.
DR   UCSC; uc009rox.1; mouse.
DR   CTD; 13138; -.
DR   MGI; MGI:101864; Dag1.
DR   HOGENOM; HBG716177; -.
DR   HOVERGEN; HBG000078; -.
DR   InParanoid; Q62165; -.
DR   OMA; TRRPTKK; -.
DR   OrthoDB; EOG49S65X; -.
DR   PhylomeDB; Q62165; -.
DR   NextBio; 283210; -.
DR   PMAP-CutDB; Q62165; -.
DR   ArrayExpress; Q62165; -.
DR   Bgee; Q62165; -.
DR   CleanEx; MM_DAG1; -.
DR   Genevestigator; Q62165; -.
DR   GermOnline; ENSMUSG00000039952; Mus musculus.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0016011; C:dystroglycan complex; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005626; C:insoluble fraction; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045121; C:membrane raft; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IMP:MGI.
DR   GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IMP:MGI.
DR   GO; GO:0044419; P:interspecies interaction between organisms; IEA:UniProtKB-KW.
DR   GO; GO:0002011; P:morphogenesis of an epithelial sheet; IMP:MGI.
DR   InterPro; IPR006644; Cadg.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR008465; DAG1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Pfam; PF05454; DAG1; 1.
DR   SMART; SM00736; CADG; 2.
DR   SUPFAM; SSF49313; Cadherin; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Cytoplasm; Cytoskeleton; Disulfide bond;
KW   Glycoprotein; Host-virus interaction; Membrane; Nucleus;
KW   Phosphoprotein; Secreted; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     27       Potential.
FT   CHAIN        28    651       Alpha-dystroglycan.
FT                                /FTId=PRO_0000021067.
FT   CHAIN       652    893       Beta-dystroglycan.
FT                                /FTId=PRO_0000021068.
FT   TOPO_DOM    652    751       Extracellular (Potential).
FT   TRANSMEM    752    772       Helical; (Potential).
FT   TOPO_DOM    773    893       Cytoplasmic (Potential).
FT   DOMAIN      498    731       Peptidase S72.
FT   REGION       28    406       Required for laminin recognition (By
FT                                similarity).
FT   REGION       47     69       O-glycosylated at one site (By
FT                                similarity).
FT   REGION      314    483       Mucin-like domain (By similarity).
FT   REGION      461    483       O-glycosylated at seven sites with GalNAc
FT                                (By similarity).
FT   REGION      817    893       Required for interaction with CAV3 (By
FT                                similarity).
FT   REGION      878    893       Required for binding DMD and UTRN (By
FT                                similarity).
FT   MOTIF       774    780       Nuclear localization signal (By
FT                                similarity).
FT   MOTIF       887    890       PPXY motif (By similarity).
FT   COMPBIAS    316    475       Pro-rich.
FT   COMPBIAS    807    893       Pro-rich.
FT   SITE        651    652       Cleavage; by autolysis (By similarity).
FT   SITE        713    714       Cleavage; by MMP9 (By similarity).
FT   MOD_RES     890    890       Phosphotyrosine; by SRC (By similarity).
FT   CARBOHYD    139    139       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    377    377       O-linked (Man6P...) (By similarity).
FT   CARBOHYD    639    639       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    647    647       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    659    659       N-linked (GlcNAc...) (Potential).
FT   DISULFID    180    262
FT   DISULFID    667    711       Potential.
FT   CONFLICT    448    450       TKK -> SKE (in Ref. 5; CAA84293).
FT   CONFLICT    599    600       GD -> PH (in Ref. 5; CAA84293).
FT   CONFLICT    643    643       I -> V (in Ref. 3; CAA60031 and 5;
FT                                AAC52853).
FT   STRAND       68     71
FT   STRAND       76     79
FT   HELIX        82     85
FT   STRAND       90     96
FT   STRAND       99    101
FT   STRAND      106    109
FT   TURN        110    113
FT   STRAND      114    117
FT   HELIX       121    123
FT   STRAND      125    136
FT   STRAND      142    157
FT   STRAND      186    194
FT   HELIX       197    199
FT   HELIX       202    216
FT   HELIX       220    222
FT   STRAND      224    227
FT   STRAND      239    243
FT   STRAND      254    263
FT   TURN        266    268
FT   HELIX       273    281
FT   HELIX       283    288
FT   STRAND      292    300
SQ   SEQUENCE   893 AA;  96905 MW;  59C081EA86AB0AC1 CRC64;
     MSVDNWLLHP LWGQTFLLLL SVAVAQAHWP SEPSEAVRDW KNQLEASMHS VLSDFQEAVP
     TVVGIPDGTA VVGRSFRVSI PTDLIASSGE IIKVSAAGKE ALPSWLHWDP HSHILEGLPL
     DTDKGVHYIS VSAARLGANG SHVPQTSSVF SIEVYPEDHN EPQSVRAASS DPGEVVPSAC
     AADEPVTVLT VILDADLTKM TPKQRIDLLN RMQSFSEVEL HNMKLVPVVN NRLFDMSAFM
     AGPGNAKKVV ENGALLSWKL GCSLNQNSVP DIRGVETPAR EGAMSAQLGY PVVGWHIANK
     KPTLPKRLRR QIHATPTPVT AIGPPTTAIQ EPPSRIVPTP TSPAIAPPTE TMAPPVRDPV
     PGKPTVTIRT RGAIIQTPTL GPIQPTRVSE AGTTVPGQIR PTLTIPGYVE PTAVITPPTT
     TTKKPRVSTP KPATPSTDSS TTTTRRPTKK PRTPRPVPRV TTKAPITRLE TASPPTRIRT
     TTSGVPRGGE PNQRPELKNH IDRVDAWVGT YFEVKIPSDT FYDNEDTTTD KLKLTLKLRE
     QQLVGEKSWV QFNSNSQLMY GLPDSSHVGK HEYFMHATDK GGLSAVDAFE IHVHKRPQGD
     KAPARFKARL AGDPAPVVND IHKKIALVKK LAFAFGDRNC SSITLQNITR GSIVVEWTNN
     TLPLEPCPKE QIIGLSRRIA DENGKPRPAF SNALEPDFKA LSIAVTGSGS CRHLQFIPVA
     PPSPGSSAAP ATEVPDRDPE KSSEDDVYLH TVIPAVVVAA ILLIAGIIAM ICYRKKRKGK
     LTLEDQATFI KKGVPIIFAD ELDDSKPPPS SSMPLILQEE KAPLPPPEYP NQSMPETTPL
     NQDTVGEYTP LRDEDPNAPP YQPPPPFTAP MEGKGSRPKN MTPYRSPPPY VPP
//
ID   DDX3X_MOUSE             Reviewed;         662 AA.
AC   Q62167; O09060; O09143;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 103.
DE   RecName: Full=ATP-dependent RNA helicase DDX3X;
DE            EC=3.6.4.13;
DE   AltName: Full=D1Pas1-related sequence 2;
DE   AltName: Full=DEAD box RNA helicase DEAD3;
DE            Short=mDEAD3;
DE   AltName: Full=DEAD box protein 3, X-chromosomal;
DE   AltName: Full=Embryonic RNA helicase;
GN   Name=Ddx3x; Synonyms=D1Pas1-rs2, Ddx3, Dead3, Erh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6, and DBA;
RX   MEDLINE=97104282; PubMed=8948440;
RA   Sowden J.C., Putt W., Morrison K., Beddington R., Edwards Y.;
RT   "The embryonic RNA helicase gene (ERH): a new member of the DEAD box
RT   family of RNA helicases.";
RL   Biochem. J. 308:839-846(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Erythroleukemia;
RX   MEDLINE=94192995; PubMed=8144024; DOI=10.1016/0378-1119(94)90541-X;
RA   Gee S.L., Conboy J.G.;
RT   "Mouse erythroid cells express multiple putative RNA helicase genes
RT   exhibiting high sequence conservation from yeast to mammals.";
RL   Gene 140:171-177(1994).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT SER-2.
RX   MEDLINE=20318637; PubMed=10859333; DOI=10.1084/jem.191.12.2083;
RA   Yaguee J., Alvarez I., Rognan D., Ramos M., Vazquez J.,
RA   Lopez de Castro J.A.;
RT   "An N-acetylated natural ligand of human histocompatibility leukocyte
RT   antigen (HLA)-B39. Classical major histocompatibility complex class I
RT   proteins bind peptides with a blocked NH(2) terminus in vivo.";
RL   J. Exp. Med. 191:2083-2092(2000).
RN   [4]
RP   PROTEIN SEQUENCE OF 535-548, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Putative ATP-dependent RNA helicase. It may play a role
CC       in translational activation of mRNA in the oocyte and early
CC       embryo.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Identified in a mRNP complex, at least composed of DHX9,
CC       DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1,
CC       STAU2, SYNCRIP and YBX1. Interacts with XPO1 and TDRD3 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle (By similarity). Cytoplasm
CC       (By similarity). Note=Located predominantly in nuclear speckles
CC       and, at low levels, throughout the cytoplasm. Located to the outer
CC       side of nuclear pore complexes (NPC). Shuttles between the nucleus
CC       and the cytoplasm in a XPO1-dependent manner (By similarity).
CC   -!- TISSUE SPECIFICITY: Developmentally regulated.
CC   -!- DEVELOPMENTAL STAGE: Expressed in oocytes. Ubiquitously found in 9
CC       days post-conception embryo, at later stages it is restricted to
CC       brain and kidney.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX3/DED1
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
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DR   EMBL; Z38117; CAA86261.1; -; mRNA.
DR   EMBL; L25126; AAA53630.1; -; mRNA.
DR   IPI; IPI00230035; -.
DR   PIR; I84741; I84741.
DR   RefSeq; NP_034158.1; NM_010028.3.
DR   UniGene; Mm.289662; -.
DR   UniGene; Mm.474912; -.
DR   UniGene; Mm.474961; -.
DR   ProteinModelPortal; Q62167; -.
DR   SMR; Q62167; 168-580.
DR   MINT; MINT-1870173; -.
DR   STRING; Q62167; -.
DR   PhosphoSite; Q62167; -.
DR   REPRODUCTION-2DPAGE; Q62167; -.
DR   PRIDE; Q62167; -.
DR   Ensembl; ENSMUST00000000804; ENSMUSP00000000804; ENSMUSG00000000787.
DR   GeneID; 13205; -.
DR   KEGG; mmu:13205; -.
DR   UCSC; uc009srl.1; mouse.
DR   CTD; 13205; -.
DR   MGI; MGI:103064; Ddx3x.
DR   eggNOG; roNOG09378; -.
DR   GeneTree; ENSGT00390000005849; -.
DR   HOGENOM; HBG737336; -.
DR   HOVERGEN; HBG015893; -.
DR   InParanoid; Q62167; -.
DR   OMA; KYERGGN; -.
DR   OrthoDB; EOG47D9FV; -.
DR   PhylomeDB; Q62167; -.
DR   NextBio; 283364; -.
DR   ArrayExpress; Q62167; -.
DR   Bgee; Q62167; -.
DR   CleanEx; MM_ERH; -.
DR   Genevestigator; Q62167; -.
DR   GermOnline; ENSMUSG00000000787; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing;
KW   DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; RNA-binding.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    662       ATP-dependent RNA helicase DDX3X.
FT                                /FTId=PRO_0000055010.
FT   DOMAIN      211    403       Helicase ATP-binding.
FT   DOMAIN      414    575       Helicase C-terminal.
FT   NP_BIND     200    207       ATP (By similarity).
FT   NP_BIND     224    231       ATP (By similarity).
FT   REGION      260    517       Necessary for interaction with XPO1 (By
FT                                similarity).
FT   MOTIF       180    208       Q motif.
FT   MOTIF       347    350       DEAD box.
FT   COMPBIAS    582    662       Gly/Ser-rich.
FT   COMPBIAS    609    616       Poly-Ser.
FT   COMPBIAS    624    630       Poly-Gly.
FT   COMPBIAS    633    641       Poly-Gly.
FT   MOD_RES       2      2       N-acetylserine.
FT   MOD_RES      69     69       Phosphotyrosine (By similarity).
FT   MOD_RES      74     74       Phosphoserine.
FT   MOD_RES      78     78       Phosphoserine (By similarity).
FT   MOD_RES     104    104       Phosphotyrosine (By similarity).
FT   MOD_RES     118    118       N6-acetyllysine (By similarity).
FT   MOD_RES     125    125       Phosphoserine (By similarity).
FT   MOD_RES     343    343       Phosphotyrosine (By similarity).
FT   MOD_RES     590    590       Phosphoserine (By similarity).
FT   MOD_RES     594    594       Phosphoserine.
FT   MOD_RES     612    612       Phosphoserine (By similarity).
SQ   SEQUENCE   662 AA;  73101 MW;  216515CB00324017 CRC64;
     MSHVAVENAL GLDQQFAGLD LNSSDNQSGG STASKGRYIP PHLRNREATK GFYDKDSSGW
     SSSKDKDAYS SFGSRGDSRG KSSFFGDRGS GSRGRFDDRG RGDYDGIGGR GDRSGFGKFE
     RGGNSRWCDK SDEDDWSKPL PPSERLEQEL FSGGNTGINF EKYDDIPVEA TGNNCPPHIE
     SFSDVEMGEI IMGNIELTRY TRPTPVQKHA IPIIKEKRDL MACAQTGSGK TAAFLLPILS
     QIYADGPGEA LRAMKENGRY GRRKQYPISL VLAPTRELAV QIYEEARKFS YRSRVRPCVV
     YGGAEIGQQI RDLERGCHLL VATPGRLVDM MERGKIGLDF CKYLVLDEAD RMLDMGFEPQ
     IRRIVEQDTM PPKGVRHTMM FSATFPKEIQ MLARDFLDEY IFLAVGRVGS TSENITQKVV
     WVEEIDKRSF LLDLLNATGK DSLTLVFVET KKGADSLEDF LYHEGYACTS IHGDRSQRDR
     EEALHQFRSG KSPILVATAV AARGLDISNV KHVINFDLPS DIEEYVHRIG RTGRVGNLGL
     ATSFFNERNI NITKDLLDLL VEAKQEVPSW LENMAFEHHY KGSSRGRSKS SRFSGGFGAR
     DYRQSSGASS SSFSSSRASS SRSGGGGHGG SRGFGGGGYG GFYNSDGYGG NYNSQGVDWW
     GN
//
ID   RBP1_MOUSE              Reviewed;         648 AA.
AC   Q62172; Q9CRE5;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=RalA-binding protein 1;
DE            Short=RalBP1;
DE   AltName: Full=Dinitrophenyl S-glutathione ATPase;
DE            Short=DNP-SG ATPase;
DE   AltName: Full=Ral-interacting protein 1;
GN   Name=Ralbp1; Synonyms=Rip1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   STRAIN=NIH Swiss; TISSUE=Embryo;
RX   MEDLINE=96112637; PubMed=8570186;
RA   Park S.-H., Weinberg R.A.;
RT   "A putative effector of Ral has homology to Rho/Rac GTPase activating
RT   proteins.";
RL   Oncogene 11:2349-2355(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-136.
RC   STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   INTERACTION WITH REPS1.
RC   TISSUE=Muscle;
RX   MEDLINE=98058900; PubMed=9395447; DOI=10.1074/jbc.272.50.31230;
RA   Yamaguchi A., Urano T., Goi T., Feig L.A.;
RT   "An eps homology (EH) domain protein that binds to the ral-GTPase
RT   target, RalBP1.";
RL   J. Biol. Chem. 272:31230-31234(1997).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-93, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-93, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Can activate specifically hydrolysis of GTP bound to
CC       RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of
CC       S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX)
CC       and is the major ATP-dependent transporter of glutathione
CC       conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can
CC       catalyze transport of glutathione conjugates and xenobiotics, and
CC       may contribute to the multidrug resistance phenomenon. Serves as a
CC       scaffold protein that brings together proteins forming an
CC       endocytotic complex during interphase and also with CDK1 to switch
CC       off endocytosis, One of its substrates would be EPN1/Epsin(By
CC       similarity).
CC   -!- SUBUNIT: Interacts with the GTP-bound form of RALA, RALB, CDC42
CC       and RAC1. Interacts with REPS1 and REPS2 and this does not affect
CC       the Ral-binding activity. Interacts with DAB2IP. Interacts with
CC       catalytically active CCNB1 and CDK1 during mitosis. Interacts with
CC       EPN1, NUMB and TFAP2A during interphase and mitosis (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitous. The highest level of expression
CC       was observed in ovaries and skeletal muscle, whereas the lowest
CC       was found in spleen, liver and peripheral blood leukocytes.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X80937; CAA56912.1; -; mRNA.
DR   EMBL; BC075732; AAH75732.1; -; mRNA.
DR   EMBL; AK019116; BAB31552.1; -; mRNA.
DR   IPI; IPI00421132; -.
DR   UniGene; Mm.17009; -.
DR   ProteinModelPortal; Q62172; -.
DR   SMR; Q62172; 187-353.
DR   DIP; DIP-29741N; -.
DR   MINT; MINT-4132030; -.
DR   STRING; Q62172; -.
DR   PhosphoSite; Q62172; -.
DR   PRIDE; Q62172; -.
DR   Ensembl; ENSMUST00000024905; ENSMUSP00000024905; ENSMUSG00000024096.
DR   MGI; MGI:108466; Ralbp1.
DR   HOGENOM; HBG713891; -.
DR   HOVERGEN; HBG044496; -.
DR   InParanoid; Q62172; -.
DR   OrthoDB; EOG41RPTW; -.
DR   ArrayExpress; Q62172; -.
DR   Bgee; Q62172; -.
DR   CleanEx; MM_RALBP1; -.
DR   Genevestigator; Q62172; -.
DR   GermOnline; ENSMUSG00000024096; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0030675; F:Rac GTPase activator activity; IDA:UniProtKB.
DR   GO; GO:0017160; F:Ral GTPase binding; IPI:UniProtKB.
DR   GO; GO:0043089; P:positive regulation of Cdc42 GTPase activity; IDA:UniProtKB.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
KW   GTPase activation; Membrane; Phosphoprotein; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    648       RalA-binding protein 1.
FT                                /FTId=PRO_0000056734.
FT   DOMAIN      192    380       Rho-GAP.
FT   REGION      391    446       Interacts with RalA.
FT   COMPBIAS    164    171       Poly-Lys.
FT   MOD_RES      11     11       Phosphoserine (By similarity).
FT   MOD_RES      27     27       Phosphothreonine (By similarity).
FT   MOD_RES      29     29       Phosphoserine.
FT   MOD_RES      30     30       Phosphoserine (By similarity).
FT   MOD_RES      34     34       Phosphoserine (By similarity).
FT   MOD_RES      62     62       Phosphoserine (By similarity).
FT   MOD_RES      92     92       Phosphoserine.
FT   MOD_RES      93     93       Phosphoserine.
FT   MOD_RES     270    270       Phosphotyrosine (By similarity).
FT   MOD_RES     280    280       Phosphothreonine (By similarity).
FT   MOD_RES     463    463       Phosphoserine (By similarity).
FT   MOD_RES     638    638       Phosphoserine (By similarity).
FT   CONFLICT     30     30       S -> F (in Ref. 3; BAB31552).
SQ   SEQUENCE   648 AA;  75031 MW;  E28DCCCA4E6FDBBA CRC64;
     MTECFLPPSS SPSEHRRAEH GSGLTRTPSS EEISPTKFPG LYRTGEPSPP HDVLHEPPDT
     VSDDDKDHGK KKGKFKKKEK RTEGYAAFQE DSSGDEAESP SKVKRSKGIH VFKKPSFSKK
     KEKDFKIKEK PKEEKHKEEK HKEEKHKEKK SKDLTAADVV KQWKEKKKKK KPIQEPEVPQ
     MDAPSVKPIF GVPLVDAVER TMMYDGVRLP AVFRECVDYM EKHGMKCEGV YRVSGIKSKV
     DELKAAYDRE ESPNLEEYEP NTVASLLKQY LRDLPENLLT KELMPRFEEA CGKTTEMEKV
     QEFQRLLREL PECNHLLLSW LIVHLDHVIA KELETKMNIQ NISIVLSPTV QISNRVLYVL
     FTHVQELFGT VVLKQVTRPL RWSNMATMPT LPETQAGIKE EIRRQEFLLN CLHRDLQGGI
     KDLSKEERLW EVQRILTALK RKLREAKRQE CETKIAQEIA SLSKEDVSKE EMNENEEVIN
     ILLAQENEIL TEQEELLAME QFLRRQIASE KEEIDRLRAE IAEIQSRQQH GRSETEEYSS
     DSESESEDEE ELQLILEDLQ RQNEELEIKN NHLNQAVHEE REAIIELRVQ LRLLQMQRAK
     SEQQPQEEEE PERRGGTGPP PCDGVLEVRV AKEQAKASPS KDRKETPI
//
ID   DPYL3_MOUSE             Reviewed;         570 AA.
AC   Q62188;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-FEB-2011, entry version 99.
DE   RecName: Full=Dihydropyrimidinase-related protein 3;
DE            Short=DRP-3;
DE   AltName: Full=Unc-33-like phosphoprotein 1;
DE            Short=ULIP-1;
GN   Name=Dpysl3; Synonyms=Drp3, Ulip;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=96133606; PubMed=8551352;
RA   Byk T., Dobransky T., Cifuentes-Diaz C., Sobel A.;
RT   "Identification and molecular characterization of Unc-33-like
RT   phosphoprotein (Ulip), a putative mammalian homolog of the axonal
RT   guidance-associated unc-33 gene product.";
RL   J. Neurosci. 16:688-701(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 468-480.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-499 AND THR-509, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-509, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   SUBUNIT.
RX   MEDLINE=20545548; PubMed=10956643; DOI=10.1074/jbc.M003277200;
RA   Fukada M., Watakabe I., Yuasa-Kawada J., Kawachi H., Kuroiwa A.,
RA   Matsuda Y., Noda M.;
RT   "Molecular characterization of CRMP5, a novel member of the collapsin
RT   response mediator protein family.";
RL   J. Biol. Chem. 275:37957-37965(2000).
RN   [8]
RP   INTERACTION WITH PLEXA1, AND SUBUNIT.
RX   PubMed=14685275; DOI=10.1038/sj.emboj.7600021;
RA   Deo R.C., Schmidt E.F., Elhabazi A., Togashi H., Burley S.K.,
RA   Strittmatter S.M.;
RT   "Structural bases for CRMP function in plexin-dependent semaphorin3A
RT   signaling.";
RL   EMBO J. 23:9-22(2004).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522 AND SER-541, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-514; SER-518 AND
RP   SER-522, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Necessary for signaling by class 3 semaphorins and
CC       subsequent remodeling of the cytoskeleton. Plays a role in axon
CC       guidance, neuronal growth cone collapse and cell migration (By
CC       similarity).
CC   -!- SUBUNIT: Homotetramer, and heterotetramer with CRMP1, DPYSL2,
CC       DPYSL4 or DPYSL5. Interacts with synaptic vesicle protein 2 and
CC       SH3A domain of intersectin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell projection,
CC       growth cone (By similarity). Note=Colocalizes with synaptic
CC       vesicle protein 2 in the central region of the growth cone (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the DHOase family.
CC       Hydantoinase/dihydropyrimidinase subfamily.
CC   -!- CAUTION: Lacks most of the conserved residues that are essential
CC       for binding the metal cofactor and hence for dihydropyrimidinase
CC       activity. Its enzyme activity is therefore unsure.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X87817; CAA61082.1; -; mRNA.
DR   EMBL; BC023003; AAH23003.1; -; mRNA.
DR   IPI; IPI00122349; -.
DR   PIR; S55525; S55525.
DR   RefSeq; NP_033494.1; NM_009468.4.
DR   UniGene; Mm.428551; -.
DR   UniGene; Mm.8180; -.
DR   ProteinModelPortal; Q62188; -.
DR   SMR; Q62188; 14-490.
DR   STRING; Q62188; -.
DR   MEROPS; M38.976; -.
DR   PhosphoSite; Q62188; -.
DR   REPRODUCTION-2DPAGE; IPI00122349; -.
DR   REPRODUCTION-2DPAGE; Q62188; -.
DR   PRIDE; Q62188; -.
DR   Ensembl; ENSMUST00000025379; ENSMUSP00000025379; ENSMUSG00000024501.
DR   GeneID; 22240; -.
DR   KEGG; mmu:22240; -.
DR   NMPDR; fig|10090.3.peg.3923; -.
DR   UCSC; uc008euh.1; mouse.
DR   CTD; 22240; -.
DR   MGI; MGI:1349762; Dpysl3.
DR   GeneTree; ENSGT00550000074371; -.
DR   HOVERGEN; HBG000806; -.
DR   OMA; KMADLHA; -.
DR   PhylomeDB; Q62188; -.
DR   NextBio; 302301; -.
DR   ArrayExpress; Q62188; -.
DR   Bgee; Q62188; -.
DR   CleanEx; MM_DPYSL3; -.
DR   Genevestigator; Q62188; -.
DR   GermOnline; ENSMUSG00000024501; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0007399; P:nervous system development; IDA:MGI.
DR   InterPro; IPR006680; Amidohydro_1.
DR   InterPro; IPR011778; D-hydantoinase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Metalo_hydrolase; 1.
DR   TIGRFAMs; TIGR02033; D-hydantoinase; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cytoplasm; Direct protein sequencing; Phosphoprotein.
FT   CHAIN         1    570       Dihydropyrimidinase-related protein 3.
FT                                /FTId=PRO_0000165918.
FT   MOD_RES     499    499       Phosphotyrosine.
FT   MOD_RES     509    509       Phosphothreonine.
FT   MOD_RES     514    514       Phosphothreonine.
FT   MOD_RES     518    518       Phosphoserine.
FT   MOD_RES     522    522       Phosphoserine.
FT   MOD_RES     541    541       Phosphoserine.
FT   MOD_RES     551    551       Phosphoserine (By similarity).
SQ   SEQUENCE   570 AA;  61936 MW;  14C339BF90015D96 CRC64;
     MSYQGKKNIP RITSDRLLIK GGRIVNDDQS FYADIYMEDG LIKQIGDNLI VPGGVKTIEA
     NGKMVIPGGI DVHTHFQMPY KGMTTVDDFF QGTKAALAGG TTMIIDHVVP EPESSLTEAY
     EKWREWADGK SCCDYALHVD ITHWNDSVKQ EVQSLSKEKG VNSFMVYMAY KDLYQVSNTE
     LYEIFTCLGE LGAIAQVHAE NGDIIAQEQA RMLEMGITGP EGHVLSRPEE LEAEAVFRAI
     TVASQTNCPL YVTKVMSKSA ADLISQARKK GNVVFGEPIT ASLGIDGTHY WSKNWAKAAA
     FVTSPPLSPD PTTPDYINSL LASGDLQLSG SAHCTFSTAQ KAIGKDNFTA IPEGTNGVEE
     RMSVIWDKAV ATGKMDENQF VAVTSTNAAK IFNLYPRKGR IAVGSDSDLV IWDPDALKIV
     SAKNHQSVAE YNIFEGMELR GAPLVVICQG KIMLEDGNLH VTQGAGRFIP CSPFSDYVYK
     RIKARRKMAD LHAVPRGMYD GPVFDLTTTP KGGTPAGSTR GSPTRPNPPV RNLHQSGFSL
     SGTQVDEGVR SASKRIVAPP GGRSNITSLS
//
ID   SIX3_MOUSE              Reviewed;         333 AA.
AC   Q62233; P70176; P70177; Q4QQQ3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Homeobox protein SIX3;
DE   AltName: Full=Sine oculis homeobox homolog 3;
GN   Name=Six3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Embryonic brain;
RX   MEDLINE=96125147; PubMed=8575305;
RA   Oliver G., Mailhos A., Wehr R., Copeland N.G., Jenkins N.A., Gruss P.;
RT   "Six3, a murine homologue of the sine oculis gene, demarcates the most
RT   anterior border of the developing neural plate and is expressed during
RT   eye development.";
RL   Development 121:4045-4055(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=96409319; PubMed=8814301; DOI=10.1016/0014-5793(96)00899-X;
RA   Kawakami K., Ohto H., Takizawa T., Saito T.;
RT   "Identification and expression of Six family genes in mouse retina.";
RL   FEBS Lett. 393:259-263(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SIX3B).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in visual system development.
CC   -!- INTERACTION:
CC       P63002:Aes; NbExp=3; IntAct=EBI-2297327, EBI-646888;
CC       P16371:gro (xeno); NbExp=2; IntAct=EBI-2297327, EBI-153866;
CC       Q62441:Tle4; NbExp=2; IntAct=EBI-2297327, EBI-2297871;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=SIX3B;
CC         IsoId=Q62233-1; Sequence=Displayed;
CC       Name=SIX3A;
CC         IsoId=Q62233-2; Sequence=VSP_002291, VSP_002292;
CC   -!- DEVELOPMENTAL STAGE: First expressed at E6.5 of embryo development
CC       around the anterior border. At E8.5, expression is found over the
CC       anterior neural plate. At E9.5, in the diencephalic part of the
CC       ventral forebrain, optic vesicles, olfactory placodes and Rathke
CC       pouch. In later stages, present in hypothalamus, eyes and
CC       pituitary.
CC   -!- SIMILARITY: Belongs to the SIX/Sine oculis homeobox family.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA62379.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; X90871; CAA62379.1; ALT_INIT; mRNA.
DR   EMBL; D83144; BAA11822.1; -; mRNA.
DR   EMBL; D83145; BAA11823.1; -; mRNA.
DR   EMBL; BC098096; AAH98096.1; -; mRNA.
DR   IPI; IPI00123350; -.
DR   IPI; IPI00230578; -.
DR   PIR; S74255; S74255.
DR   RefSeq; NP_035511.2; NM_011381.4.
DR   UniGene; Mm.370208; -.
DR   UniGene; Mm.391586; -.
DR   ProteinModelPortal; Q62233; -.
DR   SMR; Q62233; 154-269.
DR   DIP; DIP-46499N; -.
DR   IntAct; Q62233; 9.
DR   STRING; Q62233; -.
DR   PRIDE; Q62233; -.
DR   Ensembl; ENSMUST00000043819; ENSMUSP00000039867; ENSMUSG00000038805.
DR   GeneID; 20473; -.
DR   KEGG; mmu:20473; -.
DR   UCSC; uc008dub.1; mouse.
DR   CTD; 20473; -.
DR   MGI; MGI:102764; Six3.
DR   eggNOG; maNOG18260; -.
DR   GeneTree; ENSGT00540000070251; -.
DR   HOVERGEN; HBG003609; -.
DR   InParanoid; Q62233; -.
DR   OrthoDB; EOG4ZKJMW; -.
DR   NextBio; 298587; -.
DR   ArrayExpress; Q62233; -.
DR   Bgee; Q62233; -.
DR   Genevestigator; Q62233; -.
DR   GermOnline; ENSMUSG00000038805; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0003705; F:sequence-specific enhancer binding RNA polymerase II transcription factor activity; IDA:MGI.
DR   GO; GO:0016564; F:transcription repressor activity; IDA:MGI.
DR   GO; GO:0021536; P:diencephalon development; IGI:MGI.
DR   GO; GO:0021797; P:forebrain anterior/posterior pattern formation; IGI:MGI.
DR   GO; GO:0060235; P:lens induction in camera-type eye; IMP:MGI.
DR   GO; GO:0030178; P:negative regulation of Wnt receptor signaling pathway; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0006606; P:protein import into nucleus; IDA:MGI.
DR   GO; GO:0021537; P:telencephalon development; IMP:MGI.
DR   InterPro; IPR001356; Homeobox.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Pfam; PF00046; Homeobox; 1.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; FALSE_NEG.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Developmental protein; DNA-binding; Homeobox;
KW   Nucleus.
FT   CHAIN         1    333       Homeobox protein SIX3.
FT                                /FTId=PRO_0000049300.
FT   DNA_BIND    207    266       Homeobox.
FT   COMPBIAS     33     70       Gly-rich.
FT   COMPBIAS    264    267       Poly-Ala.
FT   VAR_SEQ     271    286       LQHQAIGPSGMRSLAE -> SVAGTAARPPQA (in
FT                                isoform SIX3A).
FT                                /FTId=VSP_002291.
FT   VAR_SEQ     287    333       Missing (in isoform SIX3A).
FT                                /FTId=VSP_002292.
FT   CONFLICT     44     44       G -> GG (in Ref. 1).
FT   CONFLICT    118    119       VA -> WP (in Ref. 1; CAA62379).
FT   CONFLICT    278    333       PSGMRSLAEPGCPTHGSAESPSTAASPTTSVSSLTERADTG
FT                                TSILSVTSSDSECDV -> ERDALPGRARLPHARLSRVTVH
FT                                GGQPDHQCVQPDGARGHRHFDPLGNLQRLGM (in Ref.
FT                                1).
SQ   SEQUENCE   333 AA;  35593 MW;  1AD7D3C4388043B9 CRC64;
     MVFRSPLDLY SSHFLLPNFA DSHHCSLLLA SSGGGSGASG GGGGAGGGGG GNRAGGGGAG
     GAGGGSGGGG SRAPPEELSM FQLPTLNFSP EQVASVCETL EETGDIERLG RFLWSLPVAP
     GACEAINKHE SILRARAVVA FHTGNFRDLY HILENHKFTK ESHGKLQAMW LEAHYQEAEK
     LRGRPLGPVD KYRVRKKFPL PRTIWDGEQK THCFKERTRS LLREWYLQDP YPNPSKKREL
     AQATGLTPTQ VGNWFKNRRQ RDRAAAAKNR LQHQAIGPSG MRSLAEPGCP THGSAESPST
     AASPTTSVSS LTERADTGTS ILSVTSSDSE CDV
//
ID   SALL3_MOUSE             Reviewed;        1320 AA.
AC   Q62255; Q08EB0; Q52KR5; Q6GQT8; Q8BRD9;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Sal-like protein 3;
DE   AltName: Full=MSal;
DE   AltName: Full=Spalt-like protein 3;
GN   Name=Sall3; Synonyms=Sal;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-1320 (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 30-1320 (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and Embryo;
RX   MEDLINE=96391179; PubMed=8798152; DOI=10.1016/0925-4773(96)00516-3;
RA   Ott T., Kaestner K.H., Monaghan A.P., Schuetz G.;
RT   "The mouse homolog of the region specific homeotic gene spalt of
RT   Drosophila is expressed in the developing nervous system and in
RT   mesoderm-derived structures.";
RL   Mech. Dev. 56:117-128(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 692-1320.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Probable transcription factor.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q62255-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q62255-2; Sequence=VSP_006834;
CC         Note=Lacks two zinc finger domains (6 and 7) and is the major
CC         isoform;
CC   -!- TISSUE SPECIFICITY: In adult brain, testis and kidney. In lower
CC       levels also in adult ovaries and embryonic stem cells. In embryo
CC       in developing neuroectoderm of brain, inner ear and spinal chord.
CC       Also weakly and transiently expressed in embryonic branchial
CC       arches, notochord, limb buds and heart.
CC   -!- DEVELOPMENTAL STAGE: During embryogenesis detected from 7 dpc
CC       onward in tissues derived from mesoderm and ectoderm.
CC   -!- SIMILARITY: Belongs to the sal C2H2-type zinc-finger protein
CC       family.
CC   -!- SIMILARITY: Contains 9 C2H2-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC32197.1; Type=Erroneous initiation;
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DR   EMBL; AC125210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC072631; AAH72631.1; -; mRNA.
DR   EMBL; AK045051; BAC32197.1; ALT_INIT; mRNA.
DR   EMBL; X97581; CAA66196.1; ALT_TERM; mRNA.
DR   IPI; IPI00123404; -.
DR   IPI; IPI00222002; -.
DR   PIR; T30253; T30253.
DR   RefSeq; NP_840064.2; NM_178280.3.
DR   UniGene; Mm.215917; -.
DR   ProteinModelPortal; Q62255; -.
DR   SMR; Q62255; 418-482, 660-808, 991-1184.
DR   STRING; Q62255; -.
DR   PhosphoSite; Q62255; -.
DR   PRIDE; Q62255; -.
DR   Ensembl; ENSMUST00000025457; ENSMUSP00000025457; ENSMUSG00000024565.
DR   Ensembl; ENSMUST00000057950; ENSMUSP00000056967; ENSMUSG00000024565.
DR   GeneID; 20689; -.
DR   KEGG; mmu:20689; -.
DR   UCSC; uc008ftl.1; mouse.
DR   UCSC; uc008ftm.1; mouse.
DR   UCSC; uc008ftn.1; mouse.
DR   CTD; 20689; -.
DR   MGI; MGI:109295; Sall3.
DR   eggNOG; roNOG08306; -.
DR   GeneTree; ENSGT00550000074555; -.
DR   HOGENOM; HBG716076; -.
DR   HOVERGEN; HBG058921; -.
DR   InParanoid; Q62255; -.
DR   OrthoDB; EOG495ZR2; -.
DR   PhylomeDB; Q62255; -.
DR   NextBio; 299221; -.
DR   ArrayExpress; Q62255; -.
DR   Bgee; Q62255; -.
DR   CleanEx; MM_SALL3; -.
DR   Genevestigator; Q62255; -.
DR   GermOnline; ENSMUSG00000024565; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0021891; P:olfactory bulb interneuron development; IMP:MGI.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 9.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE   2: Evidence at transcript level;
KW   Alternative splicing; DNA-binding; Metal-binding; Nucleus; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1   1320       Sal-like protein 3.
FT                                /FTId=PRO_0000047025.
FT   ZN_FING     427    449       C2H2-type 1.
FT   ZN_FING     455    477       C2H2-type 2.
FT   ZN_FING     692    714       C2H2-type 3.
FT   ZN_FING     720    742       C2H2-type 4.
FT   ZN_FING     752    774       C2H2-type 5.
FT   ZN_FING     997   1019       C2H2-type 6.
FT   ZN_FING    1025   1047       C2H2-type 7.
FT   ZN_FING    1133   1155       C2H2-type 8.
FT   ZN_FING    1161   1183       C2H2-type 9.
FT   COMPBIAS    142    160       Pro-rich.
FT   COMPBIAS    217    220       Poly-Gln.
FT   COMPBIAS    374    377       Poly-Ser.
FT   COMPBIAS    829    932       Ser-rich.
FT   VAR_SEQ     993   1064       Missing (in isoform 2).
FT                                /FTId=VSP_006834.
FT   CONFLICT    131    132       EP -> S (in Ref. 3; CAA66196).
FT   CONFLICT    236    236       A -> G (in Ref. 3; CAA66196).
FT   CONFLICT    255    256       TA -> NT (in Ref. 3; CAA66196).
FT   CONFLICT    307    307       C -> CC (in Ref. 3; CAA66196).
FT   CONFLICT    497    498       NV -> KC (in Ref. 3; CAA66196).
FT   CONFLICT    744    744       A -> G (in Ref. 3; CAA66196).
FT   CONFLICT    765    765       V -> I (in Ref. 4; BAC32197).
SQ   SEQUENCE   1320 AA;  138760 MW;  33A19F56C69D5EEB CRC64;
     MSRRKQAKPQ HLKSDEELPP QDGASEHGVP GDGAEDADSG SESRSGSEET SVCEKCCAEF
     FKWADFLQHK KTCTKNPLVL IVHDDEPAPP SEDFPEPSPA SSPSDRTESE VAEEVAPTEG
     SEVKAATKEA EPMDVEVSTD KGPPGPSVPP PPPALPPQPE PAAFSMPSTN VTLETLLSTK
     VAVAQFSQGA RAGGTTGAGG SVGAVAIPMI LEQLVALQQQ QIHQLQLIEQ IRSQVALMSR
     QPGPPLKPSA SAPGTASVQL QGLTPHAALQ LSAGPATASA GSGSTLPAAF DGPQHLSQPA
     SGTSTPCSTS AAPPDSGAHP ACSTGPAPGA VAAASSTVGN AVQPQNASTP PALGPGPLLS
     SASNLPNPLL PQTSSSSVIF PNPLVSIAAT ANALDPLSAL MKHRKGKPPN VSVFEPKASA
     EDPFFKHKCR FCAKVFGSDS ALQIHLRSHT GERPFKCNIC GNRFSTKGNL KVHFQRHKEK
     YPHIQMNPYP VPEYLDNVPT CSGIPYGMSL PPEKPVTTWL DSKPVLPTVP TSVGLQLPPT
     VPGTHNYTDS PSITPVSRSP QRPSPASSEC TSLSPGLNNT ESGITVRPES PQPLLGGPSL
     TKAEPVSLPC TSTRTGDAPV VGGQVSGLPT SAATAVTDSA CTSLGSPGLP AVSDQFKAQF
     PFGGLLDSMQ TSETSKLQQL VENIDKKMTD PNQCVICHRV LSCQSALKMH YRTHTGERPF
     KCKICGRAFT TKGNLKTHFG VHRAKPPLRV QHSCPICQKK FTNAVVLQQH IRMHMGGQIP
     NTPLPEGLQE AMDADLPFDE KNAETLSSFD DDIDENSMEE DSELKDTASD SSKPLLSYSG
     SCPPSPPSVI SSIAALENQM KMIDSVMNCQ QLANLKSVEN GSGESDRLSN DSSSAVGDLE
     SRSAGSPALS ESSSSQALSP AHSNGESFRS KSPGLGHQED PQEIPLKTER LDSPPPGPGN
     GGALDLTAGH PGRPLIKEEA PFSLLFLSRE RGKCASTVCG VCGKPFACKS ALEIHYRSHT
     KERRFVCTVC RRGCSTMGNL KQHLLTHKLK ELPSQVFDPN FTLGPSHSTP SLASSPAPTM
     IKMEVNGHSK AIALGEGPAL PAGVQVPTGP QTVMSPGLAP MLAPPPRRTP KQHNCQSCGK
     TFSSASALQI HERTHTGEKP FGCTICGRAF TTKGNLKVHM GTHMWNNAPA RRGRRLSVEN
     PMALLGGDAL KFSEMFQKDL AARAMNVDPS FWNQYAAAIT NGLAMKNNEI SVIQNGGIPQ
     LPVSLGGGAI PPLGAMASGV DKARTGSSPP IVSLDKASSE TGASRPFARF IEDNKEIGIN
//
ID   SPTB2_MOUSE             Reviewed;        2363 AA.
AC   Q62261; A2AFU1; Q3TEM7; Q5SQL8; Q5SQL9; Q9QWJ7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 111.
DE   RecName: Full=Spectrin beta chain, brain 1;
DE   AltName: Full=Beta-II spectrin;
DE   AltName: Full=Embryonic liver fodrin;
DE   AltName: Full=Fodrin beta chain;
DE   AltName: Full=Spectrin, non-erythroid beta chain 1;
GN   Name=Sptbn1; Synonyms=Elf, Spnb-2, Spnb2, Sptb2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c;
RX   MEDLINE=93240985; PubMed=8479293; DOI=10.1016/0169-328X(93)90176-P;
RA   Ma Y., Zimmer W.E., Riederer B.M., Goodman S.R.;
RT   "The complete amino acid sequence for brain beta spectrin (beta
RT   fodrin): relationship to globin sequences.";
RL   Brain Res. Mol. Brain Res. 18:87-99(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC   STRAIN=C57BL/6; TISSUE=Liver;
RX   PubMed=9927192; DOI=10.1038/sj.onc.1202313;
RA   Mishra L., Cai T., Yu P., Monga S.P., Mishra B.;
RT   "Elf3 encodes a novel 200-kD beta-spectrin: role in liver
RT   development.";
RL   Oncogene 18:353-364(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-399 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   INTERACTION WITH ANK2, AND TISSUE SPECIFICITY.
RX   PubMed=15262991; DOI=10.1074/jbc.M406018200;
RA   Mohler P.J., Yoon W., Bennett V.;
RT   "Ankyrin-B targets beta2-spectrin to an intracellular compartment in
RT   neonatal cardiomyocytes.";
RL   J. Biol. Chem. 279:40185-40193(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1918; SER-2115; SER-2137
RP   AND SER-2168, AND MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-999; SER-2102; SER-2164;
RP   SER-2168 AND THR-2194, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT SER-2323, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452088; DOI=10.1074/mcp.T500040-MCP200;
RA   Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G.,
RA   Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F.,
RA   Maltby D.A., Schoepfer R., Burlingame A.L.;
RT   "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT   preparations using lectin weak affinity chromatography and mass
RT   spectrometry.";
RL   Mol. Cell. Proteomics 5:923-934(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2102, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1805, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2127; SER-2137 AND
RP   THR-2194, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-10 (ISOFORM
RP   2), AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; SER-2102; SER-2137;
RP   THR-2327 AND SER-2357, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2164 AND SER-2168, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [15]
RP   STRUCTURE BY NMR OF 2199-2304.
RX   MEDLINE=94268558; PubMed=8208297; DOI=10.1038/369675a0;
RA   Macias M.J., Musacchio A., Ponstingl H., Nilges M., Saraste M.,
RA   Oschkinat H.;
RT   "Structure of the pleckstrin homology domain from beta-spectrin.";
RL   Nature 369:675-677(1994).
RN   [16]
RP   STRUCTURE BY NMR OF 2199-2304.
RX   MEDLINE=97342712; PubMed=9199409; DOI=10.1006/jmbi.1997.1044;
RA   Nilges M., Macias M.J., O'Donoghue S.I., Oschkinat H.;
RT   "Automated NOESY interpretation with ambiguous distance restraints:
RT   the refined NMR solution structure of the pleckstrin homology domain
RT   from beta-spectrin.";
RL   J. Mol. Biol. 269:408-422(1997).
RN   [17]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2199-2304.
RX   MEDLINE=96030773; PubMed=7588597;
RA   Hyvoenen M., Macias M.J., Nilges M., Oschkinat H., Saraste M.,
RA   Wilmanns M.;
RT   "Structure of the binding site for inositol phosphates in a PH
RT   domain.";
RL   EMBO J. 14:4676-4685(1995).
CC   -!- FUNCTION: Fodrin, which seems to be involved in secretion,
CC       interacts with calmodulin in a calcium-dependent manner and is
CC       thus candidate for the calcium-dependent movement of the
CC       cytoskeleton at the membrane.
CC   -!- SUBUNIT: Like erythrocyte spectrin, the spectrin-like proteins are
CC       capable to form dimers which can further associate to tetramers.
CC       Interacts with ANK2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
CC       myofibril, sarcomere, M-band. Note=Colocalizes with ANK2 in a
CC       distinct intracellular compartment of neonatal cardiomyocytes.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Peripheral
CC       membrane protein; Cytoplasmic side.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q62261-1; Sequence=Displayed;
CC       Name=2; Synonyms=Elf3;
CC         IsoId=Q62261-2; Sequence=VSP_026057, VSP_026058, VSP_026059;
CC         Note=Phosphorylated on Ser-14 (By similarity), Ser-8 and Ser-10;
CC   -!- TISSUE SPECIFICITY: Isoform 2 is present in brain, heart, kidney
CC       and liver (at protein level).
CC   -!- DEVELOPMENTAL STAGE: Isoform 2 is expressed in brain, heart and
CC       liver throughout embryonic development. Isoform 1 is mainly
CC       expressed in neonatal developing ventricular cardiomyocytes.
CC   -!- PTM: Isoform 2 is phosphorylated on Ser-8 and Ser-10.
CC   -!- SIMILARITY: Belongs to the spectrin family.
CC   -!- SIMILARITY: Contains 2 CH (calponin-homology) domains.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 17 spectrin repeats.
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DR   EMBL; M74773; AAC42040.1; -; mRNA.
DR   EMBL; AF017112; AAD01616.1; -; mRNA.
DR   EMBL; AL731792; CAI24366.1; -; Genomic_DNA.
DR   EMBL; AL672225; CAI24366.1; JOINED; Genomic_DNA.
DR   EMBL; AL731792; CAI24367.1; -; Genomic_DNA.
DR   EMBL; AL672225; CAI24367.1; JOINED; Genomic_DNA.
DR   EMBL; AL672225; CAI25429.1; -; Genomic_DNA.
DR   EMBL; AL731792; CAI25429.1; JOINED; Genomic_DNA.
DR   EMBL; AL672225; CAI25430.1; -; Genomic_DNA.
DR   EMBL; AL731792; CAI25430.1; JOINED; Genomic_DNA.
DR   EMBL; AL731792; CAM16973.1; -; Genomic_DNA.
DR   EMBL; AL672225; CAM16973.1; JOINED; Genomic_DNA.
DR   EMBL; AL672225; CAM22716.1; -; Genomic_DNA.
DR   EMBL; AL731792; CAM22716.1; JOINED; Genomic_DNA.
DR   EMBL; AK169544; BAE41221.1; -; mRNA.
DR   IPI; IPI00121892; -.
DR   IPI; IPI00319830; -.
DR   RefSeq; NP_033286.2; NM_009260.2.
DR   RefSeq; NP_787030.2; NM_175836.2.
DR   UniGene; Mm.123110; -.
DR   UniGene; Mm.466085; -.
DR   PDB; 1BTN; X-ray; 2.00 A; A=2199-2304.
DR   PDB; 1MPH; NMR; -; A=2199-2304.
DR   PDBsum; 1BTN; -.
DR   PDBsum; 1MPH; -.
DR   ProteinModelPortal; Q62261; -.
DR   SMR; Q62261; 49-283, 297-2086, 2197-2332.
DR   IntAct; Q62261; 12.
DR   STRING; Q62261; -.
DR   PhosphoSite; Q62261; -.
DR   PRIDE; Q62261; -.
DR   Ensembl; ENSMUST00000006629; ENSMUSP00000006629; ENSMUSG00000020315.
DR   Ensembl; ENSMUST00000011877; ENSMUSP00000011877; ENSMUSG00000020315.
DR   Ensembl; ENSMUST00000102838; ENSMUSP00000099902; ENSMUSG00000020315.
DR   GeneID; 20742; -.
DR   KEGG; mmu:20742; -.
DR   UCSC; uc007ihs.1; mouse.
DR   CTD; 20742; -.
DR   MGI; MGI:98388; Spnb2.
DR   eggNOG; roNOG06871; -.
DR   HOGENOM; HBG357452; -.
DR   HOVERGEN; HBG057912; -.
DR   InParanoid; Q62261; -.
DR   OMA; KEGEDMI; -.
DR   OrthoDB; EOG4WWRHM; -.
DR   NextBio; 299385; -.
DR   ArrayExpress; Q62261; -.
DR   Bgee; Q62261; -.
DR   CleanEx; MM_SPNB2; -.
DR   Genevestigator; Q62261; -.
DR   GermOnline; ENSMUSG00000020315; Mus musculus.
DR   GO; GO:0032437; C:cuticular plate; IDA:MGI.
DR   GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0008091; C:spectrin; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR   GO; GO:0007182; P:common-partner SMAD protein phosphorylation; IDA:MGI.
DR   GO; GO:0007184; P:SMAD protein import into nucleus; IDA:MGI.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR016343; Spectrin_bsu.
DR   InterPro; IPR001605; Spectrin_PH.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00435; Spectrin; 17.
DR   PIRSF; PIRSF002297; Spectrin_beta_subunit; 1.
DR   PRINTS; PR00683; SPECTRINPH.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00150; SPEC; 17.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Actin capping; Actin-binding;
KW   Alternative splicing; Calmodulin-binding; Cell membrane; Cytoplasm;
KW   Cytoskeleton; Glycoprotein; Membrane; Phosphoprotein; Repeat.
FT   CHAIN         1   2363       Spectrin beta chain, brain 1.
FT                                /FTId=PRO_0000073462.
FT   DOMAIN        1    275       Actin-binding.
FT   DOMAIN       54    158       CH 1.
FT   DOMAIN      173    275       CH 2.
FT   REPEAT      276    384       Spectrin 1.
FT   REPEAT      385    498       Spectrin 2.
FT   REPEAT      499    608       Spectrin 3.
FT   REPEAT      609    714       Spectrin 4.
FT   REPEAT      715    819       Spectrin 5.
FT   REPEAT      820    925       Spectrin 6.
FT   REPEAT      926   1032       Spectrin 7.
FT   REPEAT     1033   1139       Spectrin 8.
FT   REPEAT     1140   1245       Spectrin 9.
FT   REPEAT     1246   1350       Spectrin 10.
FT   REPEAT     1351   1462       Spectrin 11.
FT   REPEAT     1463   1562       Spectrin 12.
FT   REPEAT     1563   1668       Spectrin 13.
FT   REPEAT     1669   1775       Spectrin 14.
FT   REPEAT     1776   1881       Spectrin 15.
FT   REPEAT     1882   1987       Spectrin 16.
FT   REPEAT     1988   2132       Spectrin 17.
FT   DOMAIN     2196   2306       PH.
FT   REGION     1563   2093       Interaction with ANK2 (By similarity).
FT   MOD_RES      90     90       N6-acetyllysine (By similarity).
FT   MOD_RES     257    257       Phosphoserine.
FT   MOD_RES     999    999       Phosphothreonine.
FT   MOD_RES    1447   1447       Phosphoserine (By similarity).
FT   MOD_RES    1805   1805       Phosphotyrosine.
FT   MOD_RES    1815   1815       N6-acetyllysine (By similarity).
FT   MOD_RES    1913   1913       N6-acetyllysine (By similarity).
FT   MOD_RES    1918   1918       Phosphoserine.
FT   MOD_RES    1989   1989       N6-acetyllysine (By similarity).
FT   MOD_RES    2102   2102       Phosphoserine.
FT   MOD_RES    2115   2115       Phosphoserine.
FT   MOD_RES    2127   2127       Phosphoserine.
FT   MOD_RES    2137   2137       Phosphoserine.
FT   MOD_RES    2158   2158       Phosphothreonine (By similarity).
FT   MOD_RES    2159   2159       Phosphoserine (By similarity).
FT   MOD_RES    2163   2163       Phosphoserine (By similarity).
FT   MOD_RES    2164   2164       Phosphoserine.
FT   MOD_RES    2168   2168       Phosphoserine.
FT   MOD_RES    2186   2186       Phosphothreonine (By similarity).
FT   MOD_RES    2194   2194       Phosphothreonine.
FT   MOD_RES    2327   2327       Phosphothreonine.
FT   MOD_RES    2340   2340       Phosphoserine (By similarity).
FT   MOD_RES    2357   2357       Phosphoserine.
FT   CARBOHYD   2323   2323       O-linked (GlcNAc).
FT   VAR_SEQ       1     49       MTTTVATDYDNIEIQQQYSDVNNRWDVDDWDNENSSARLFE
FT                                RSRIKALA -> MELQRTSSISGPLSPAYTGQVPYNYNQLE
FT                                GRFKQLQ (in isoform 2).
FT                                /FTId=VSP_026057.
FT   VAR_SEQ    2140   2246       MAGTMETSEMVNGAAEQRTSSKESSPVPSPTLDRKAKSALP
FT                                AQSAATLPARTLETPAAQMEGFLNRKHEWEAHNKKASSRSW
FT                                HNVYCVINNQEMGFYKDAKSAASGI -> VSYRSQTYQNYK
FT                                NFNSRRTASDHSWSGM (in isoform 2).
FT                                /FTId=VSP_026058.
FT   VAR_SEQ    2247   2363       Missing (in isoform 2).
FT                                /FTId=VSP_026059.
FT   CONFLICT    252    252       D -> A (in Ref. 4; BAE41221).
FT   CONFLICT    309    309       S -> T (in Ref. 2; AAD01616).
FT   CONFLICT    368    368       T -> A (in Ref. 2; AAD01616).
FT   CONFLICT    737    737       K -> I (in Ref. 1; AAC42040).
FT   CONFLICT    796    796       Y -> C (in Ref. 2; AAD01616).
FT   CONFLICT    846    846       Q -> R (in Ref. 1; AAC42040).
FT   CONFLICT    970    970       W -> C (in Ref. 2; AAD01616).
FT   CONFLICT    996    996       R -> C (in Ref. 2; AAD01616).
FT   CONFLICT   1401   1403       SQI -> KPGF (in Ref. 1; AAC42040).
FT   CONFLICT   1414   1455       SVNILLKKQQMLENQMEVRKKEIEELQSQAQALSQEGKSTD
FT                                E -> QSQYSSEKGNRRRRIRWKFGRKRSRNCRPSPGSSRG
FT                                RAQMR (in Ref. 1; AAC42040).
FT   CONFLICT   1508   1508       A -> R (in Ref. 1; AAC42040).
FT   CONFLICT   1619   1624       EKAKDE -> KRPRMK (in Ref. 1; AAC42040).
FT   CONFLICT   1898   1898       D -> G (in Ref. 1; AAC42040).
FT   CONFLICT   2171   2171       L -> S (in Ref. 1; AAC42040).
FT   CONFLICT   2345   2346       EK -> AE (in Ref. 1; AAC42040).
FT   CONFLICT   2356   2358       FSL -> STV (in Ref. 1; AAC42040).
FT   STRAND     2200   2209
FT   STRAND     2222   2229
FT   STRAND     2232   2238
FT   HELIX      2239   2244
FT   STRAND     2248   2250
FT   STRAND     2260   2263
FT   STRAND     2269   2277
FT   STRAND     2283   2287
FT   HELIX      2291   2303
SQ   SEQUENCE   2363 AA;  274223 MW;  221362054E64BB8C CRC64;
     MTTTVATDYD NIEIQQQYSD VNNRWDVDDW DNENSSARLF ERSRIKALAD EREAVQKKTF
     TKWVNSHLAR VSCRITDLYT DLRDGRMLIK LLEVLSGERL PKPTKGRMRI HCLENVDKAL
     QFLKEQRVHL ENMGSHDIVD GNHRLTLGLI WTIILRFQIQ DISVETEDNK EKKSAKDALL
     LWCQMKTAGY PNVNIHNFTT SWRDGMAFNA LIHKHRPDLI DFDKLKKSNA HYNLQNAFNL
     AEQHLGLTKL LDPEDISVDH PDEKSIITYV VTYYHYFSKM KALAVEGKRI GKVLDNAIET
     EKMIEKYESL ASDLLEWIEQ TIIILNNRKF ANSLVGVQQQ LQAFNTYRTV EKPPKFTEKG
     NLEVLLFTIQ SKMRANNQKV YMPREGKLIS DINKAWERLE KAEHERELAL RNELIRQEKL
     EQLARRFDRK AAMRETWLSE NQRLVSQDNF GFDLPAVEAA TKKHEAIETD IAAYEERVQA
     VVAVARELEA ENYHDIKRIT ARKDNVIRLW EYLLELLRAR RQRLEMNLGL QKIFQEMLYI
     MDWMDEMKVL LLSQDYGKHL LGVEDLLQKH ALVEADIAIQ AERVRGVNAS AQKFATDGEG
     YKPCDPQVIR DRVAHMEFCY QELCQLAAER RARLEESRRL WKFFWEMAEE EGWIREKEKI
     LSSDDYGKDL TSVMRLLSKH RAFEDEMSGR SGHFEQAIKE GEDMIAEEHF GSEKIRERII
     YIREQWANLE QLSAIRKKRL EEASLLHQFQ ADADDIDAWM LDILKIVSSN DVGHDEYSTQ
     SLVKKHKDVA EEITNYRPTI DTLHEQASAL PQAHAESPDV KGRLAGIEER CKEMAELTRL
     RKQALQDTLA LYKMFSEADA CELWIDEKEQ WLNNMQIPEK LEDLEVIQHR FESLEPEMNN
     QASRVAVVNQ IARQLMHNGH PSEKEIRAQQ DKLNTRWSQF RELVDRKKDA LLSALSIQNY
     HLECNETKSW IREKTKVIES TQDLGNDLAG VMALQRKLTG MERDLVAIEA KLSDLQKEAE
     KLESEHPDQA QAILSRLAEI SDVWEEMKTT LKNREASLGE ASKLQQFLRD LDDFQSWLSR
     TQTAIASEDM PNTLTEAEKL LTQHENIKNE IDNYEEDYQK MRDMGEMVTQ GQTDAQYMFL
     RQRLQALDTG WNELHKMWEN RQNLLSQSHA YQQFLRDTKQ AEAFLNNQEY VLAHTEMPTT
     LEGAEAAIKK QEDFMTTMDA NEEKINAVVE TGRRLVSDGN INSDRIQEKV DSIDDRHRKN
     REAASELLMR LKDNRDLQKF LQDCQELSLW INEKMLTAQD MSYDEARNLH SKWLKHQAFM
     AELASNKEWL DKIEKEGMQL ISEKPETEAV VKEKLTGLHK MWEVLESTTQ TKAQRLFDAN
     KAELFTQSCA DLDKWLHGLE SQIQSDDYGK DLTSVNILLK KQQMLENQME VRKKEIEELQ
     SQAQALSQEG KSTDEVDSKR LTVQTKFMEL LEPLSERKHN LLASKEIHQF NRDVEDEILW
     VGERMPLATS TDHGHNLQTV QLLIKKNQTL QKEIQGHQPR IDDIFERSQN IITDSSSLNA
     EAIRQRLADL KQLWGLLIEE TEKRHRRLEE AHKAQQYYFD AAEAEAWMSE QELYMMSEEK
     AKDEQSAVSM LKKHQILEQA VEDYAETVHQ LSKTSRALVA DSHPESERIS MRQSKVDKLY
     AGLKDLAEER RGKLDERHRL FQLNREVDDL EQWIAEREVV AGSHELGQDY EHVTMLQERF
     REFARDTGNI GQERVDTVNN MADELINSGH SDAATIAEWK DGLNEAWADL LELIDTRTQI
     LAASYELHKF YHDAKEIFGR IQDKHKKLPE ELGRDQNTVE TLQRMHTTFE HDIQALGTQV
     RQLQEDAARL QAAYAGDKAD DIQKRENEVL EAWKSLLDAC EGRRVRLVDT GDKFRFFSMV
     RDLMLWMEDV IRQIEAQEKP RDVSSVELLM NNHQGIKAEI DARNDSFTAC IELGKSLLAR
     KHYASEEIKE KLLQLTEKRK EMIDKWEDRW EWLRLILEVH QFSRDASVAE AWLLGQEPYL
     SSREIGQSVD EVEKLIKRHE AFEKSAATWD ERFSALERLT TLELLEVRRQ QEEEERKRRP
     PSPDPNTKVS EEAESQQWDT SKGDQVSQNG LPAEQGSPRM AGTMETSEMV NGAAEQRTSS
     KESSPVPSPT LDRKAKSALP AQSAATLPAR TLETPAAQME GFLNRKHEWE AHNKKASSRS
     WHNVYCVINN QEMGFYKDAK SAASGIPYHS EVPVSLKEAI CEVALDYKKK KHVFKLRLSD
     GNEYLFQAKD DEEMNTWIQA ISSAISSDKH DTSASTQSTP ASSRAQTLPT SVVTITSESS
     PGKREKDKEK DKEKRFSLFG KKK
//
ID   SYPH_MOUSE              Reviewed;         314 AA.
AC   Q62277; Q8BRQ0; Q91WI8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2003, sequence version 2.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Synaptophysin;
DE   AltName: Full=BM89 antigen;
DE   AltName: Full=Major synaptic vesicle protein p38;
GN   Name=Syp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 7-314.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=97354226; PubMed=9210520;
RX   DOI=10.1002/(SICI)1097-4547(19970615)48:6<507::AID-JNR3>3.3.CO;2-2;
RA   Gaitanou M., Mamalaki A., Merkouri E., Matsas R.;
RT   "Purification and cDNA cloning of mouse BM89 antigen shows that it is
RT   identical with the synaptic vesicle protein synaptophysin.";
RL   J. Neurosci. Res. 48:507-514(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-314.
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 77-89; 170-179 AND 226-235, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=10595519; DOI=10.1016/S0896-6273(00)81122-8;
RA   Janz R., Suedhof T.C., Hammer R.E., Unni V., Siegelbaum S.A.,
RA   Bolshakov V.Y.;
RT   "Essential roles in synaptic plasticity for synaptogyrin I and
RT   synaptophysin I.";
RL   Neuron 24:687-700(1999).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-81, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Possibly involved in structural functions as organizing
CC       other membrane components or in targeting the vesicles to the
CC       plasma membrane (By similarity). Involved in the regulation of
CC       short-term and long-term synaptic plasticity.
CC   -!- SUBUNIT: Homohexamer or homotetramer. Interacts with SRCIN1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane; Multi-pass membrane protein (By
CC       similarity). Cell junction, synapse, synaptosome (By similarity).
CC   -!- DOMAIN: The calcium-binding activity is thought to be localized in
CC       the cytoplasmic tail of the protein.
CC   -!- PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its
CC       subsequent proteasomal degradation (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice lackin both SYNGR1 and SYP show normal
CC       brain structure and composition, but impaired short-term and long-
CC       term synaptic plasticity.
CC   -!- SIMILARITY: Belongs to the synaptophysin/synaptobrevin family.
CC   -!- SIMILARITY: Contains 1 MARVEL domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK043756; BAC31642.1; -; mRNA.
DR   EMBL; X95818; CAA65084.1; -; mRNA.
DR   EMBL; BC014823; AAH14823.1; -; mRNA.
DR   IPI; IPI00123505; -.
DR   RefSeq; NP_033331.2; NM_009305.2.
DR   UniGene; Mm.223674; -.
DR   ProteinModelPortal; Q62277; -.
DR   IntAct; Q62277; 3.
DR   STRING; Q62277; -.
DR   PhosphoSite; Q62277; -.
DR   PRIDE; Q62277; -.
DR   Ensembl; ENSMUST00000069520; ENSMUSP00000069429; ENSMUSG00000031144.
DR   Ensembl; ENSMUST00000116638; ENSMUSP00000112337; ENSMUSG00000031144.
DR   GeneID; 20977; -.
DR   KEGG; mmu:20977; -.
DR   UCSC; uc009sls.1; mouse.
DR   CTD; 20977; -.
DR   MGI; MGI:98467; Syp.
DR   GeneTree; ENSGT00390000010039; -.
DR   HOGENOM; HBG714484; -.
DR   HOVERGEN; HBG006681; -.
DR   InParanoid; Q62277; -.
DR   OMA; TGNTCKE; -.
DR   OrthoDB; EOG4JM7QJ; -.
DR   PhylomeDB; Q62277; -.
DR   NextBio; 299960; -.
DR   ArrayExpress; Q62277; -.
DR   Bgee; Q62277; -.
DR   CleanEx; MM_SYP; -.
DR   Genevestigator; Q62277; -.
DR   GermOnline; ENSMUSG00000031144; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0030285; C:integral to synaptic vesicle membrane; TAS:MGI.
DR   GO; GO:0044306; C:neuron projection terminus; IDA:MGI.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:MGI.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR   GO; GO:0042169; F:SH2 domain binding; IDA:MGI.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; TAS:MGI.
DR   GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:UniProtKB.
DR   GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IMP:UniProtKB.
DR   GO; GO:0007268; P:synaptic transmission; TAS:MGI.
DR   InterPro; IPR008253; Marvel.
DR   InterPro; IPR021128; MARVEL-like_dom.
DR   InterPro; IPR001285; Synaptophysin/porin.
DR   PANTHER; PTHR10306; Synaptophysin; 1.
DR   Pfam; PF01284; MARVEL; 1.
DR   PRINTS; PR00220; SYNAPTOPHYSN.
DR   PROSITE; PS51225; MARVEL; 1.
DR   PROSITE; PS00604; SYNAPTOP; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell junction; Cytoplasmic vesicle;
KW   Direct protein sequencing; Glycoprotein; Membrane; Phosphoprotein;
KW   Repeat; Synapse; Synaptosome; Transmembrane; Transmembrane helix;
KW   Ubl conjugation.
FT   CHAIN         1    314       Synaptophysin.
FT                                /FTId=PRO_0000179162.
FT   TOPO_DOM      1     25       Cytoplasmic (Potential).
FT   TRANSMEM     26     49       Helical; (Potential).
FT   TOPO_DOM     50    107       Vesicular (Potential).
FT   TRANSMEM    108    131       Helical; (Potential).
FT   TOPO_DOM    132    138       Cytoplasmic (Potential).
FT   TRANSMEM    139    162       Helical; (Potential).
FT   TOPO_DOM    163    200       Vesicular (Potential).
FT   TRANSMEM    201    224       Helical; (Potential).
FT   TOPO_DOM    225    314       Cytoplasmic (Potential).
FT   DOMAIN       21    228       MARVEL.
FT   REGION      255    305       Repeats, Gly-rich.
FT   MOD_RES      81     81       Phosphotyrosine.
FT   MOD_RES     227    227       Phosphothreonine (Potential).
FT   MOD_RES     279    279       Phosphotyrosine (Potential).
FT   MOD_RES     296    296       Phosphotyrosine (Potential).
FT   CARBOHYD     59     59       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    105    105       A -> G (in Ref. 2; CAA65084).
SQ   SEQUENCE   314 AA;  34025 MW;  F6AC6E30AECE10CE CRC64;
     MLLLADMDVV NQLVAGGQFR VVKEPLGFVK VLQWVFAIFA FATCGSYTGE LRLSVECANK
     TESALNIEVE FEYPFRLHQV YFDAPSCVKG GTTKIFLVGD YSSSAEFFVT VAVFAFLYSM
     GALATYIFLQ NKYRENNKGP MMDFLATAVF AFMWLVSSSA WAKGLSDVKM ATDPENIIKE
     MPMCRQTGNT CKELRDPVTS GLNTSVVFGF LNLVLWVGNL WFVFKETGWA APFMRAPPGA
     PEKQPAPGDA YGDAGYGQGP GGYGPQDSYG PQGGYQPDYG QPASGGGGGY GPQGDYGQQG
     YGQQGAPTSF SNQM
//
ID   TGON1_MOUSE             Reviewed;         353 AA.
AC   Q62313;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Trans-Golgi network integral membrane protein 1;
DE   AltName: Full=TGN38A;
DE   Flags: Precursor;
GN   Name=Tgoln1; Synonyms=Ttgn1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=95301533; PubMed=7540170; DOI=10.1074/jbc.270.24.14471;
RA   Kasai K., Takahashi S., Murakami K., Nakayama K.;
RT   "Strain-specific presence of two TGN38 isoforms and absence of TGN41
RT   in mouse.";
RL   J. Biol. Chem. 270:14471-14476(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Aorta, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230 AND SER-231, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-110, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: May be involved in regulating membrane traffic to and
CC       from trans-Golgi network.
CC   -!- INTERACTION:
CC       P00441:SOD1 (xeno); NbExp=1; IntAct=EBI-991369, EBI-990792;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein (By similarity). Golgi apparatus, trans-Golgi network
CC       membrane; Single-pass type I membrane protein (By similarity).
CC       Note=Primarily in trans-Golgi network. Cycles between the trans-
CC       Golgi network and the cell surface returning via endosomes (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- MISCELLANEOUS: Also found in strains BALB/c, C57BL/6 and DBA/2.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D50031; BAA08757.1; -; mRNA.
DR   EMBL; AK041302; BAC30896.1; -; mRNA.
DR   EMBL; AK076586; BAC36404.1; -; mRNA.
DR   EMBL; BC009143; AAH09143.1; -; mRNA.
DR   IPI; IPI00408895; -.
DR   PIR; B56940; B56940.
DR   RefSeq; NP_033469.1; NM_009443.3.
DR   UniGene; Mm.246563; -.
DR   IntAct; Q62313; 1.
DR   STRING; Q62313; -.
DR   PhosphoSite; Q62313; -.
DR   PRIDE; Q62313; -.
DR   Ensembl; ENSMUST00000070524; ENSMUSP00000068487; ENSMUSG00000056429.
DR   GeneID; 22134; -.
DR   KEGG; mmu:22134; -.
DR   NMPDR; fig|10090.3.peg.14645; -.
DR   CTD; 22134; -.
DR   MGI; MGI:105080; Tgoln1.
DR   HOVERGEN; HBG060160; -.
DR   InParanoid; Q62313; -.
DR   OrthoDB; EOG4J3WHP; -.
DR   PhylomeDB; Q62313; -.
DR   NextBio; 445169; -.
DR   ArrayExpress; Q62313; -.
DR   Bgee; Q62313; -.
DR   CleanEx; MM_TGOLN1; -.
DR   Genevestigator; Q62313; -.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Golgi apparatus; Membrane;
KW   Phosphoprotein; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     17       Potential.
FT   CHAIN        18    353       Trans-Golgi network integral membrane
FT                                protein 1.
FT                                /FTId=PRO_0000022485.
FT   TOPO_DOM     18    298       Extracellular (Potential).
FT   TRANSMEM    299    319       Helical; (Potential).
FT   TOPO_DOM    320    353       Cytoplasmic (Potential).
FT   REPEAT      131    138       1.
FT   REPEAT      139    146       2.
FT   REPEAT      147    154       3.
FT   REPEAT      155    162       4.
FT   REPEAT      163    170       5.
FT   REPEAT      171    178       6.
FT   REGION      131    178       6 X 8 AA tandem repeats.
FT   MOTIF       346    349       Endocytosis signal (By similarity).
FT   MOD_RES     230    230       Phosphoserine.
FT   MOD_RES     231    231       Phosphoserine.
FT   CARBOHYD    110    110       N-linked (GlcNAc...).
FT   CARBOHYD    293    293       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   353 AA;  37848 MW;  95C340C2F4A21EB3 CRC64;
     MRFQVALLLL SVAVARALPS VYKRDADSGD SQNPPNQPSK QSSTPLPSSN QVKTTRPTDG
     QGQKSDKKDQ DKTTLAAVSS KAESGPRTAA TDHSLGDSRR QPEKTDAELN ETARPLSPVN
     PKLEKSDQSS TEDSGKPTGG NSGKPTGGDS GKPTEAGSNK ATEDDSGKST KVDLDKPTSK
     ISPDTETSKT DKVQPTEKGQ KPTLTSKTES GETLAGDSDF SLKPEKGDKS SEPTEDVETK
     EIEEGDTEPE EGSPLEEENE KVPGPSSSEN QEGTLTDSMK NEKDDLYKDS SGNTSAESSH
     FFAYLVTAAV LVAVLYIAYH NKRKIIAFAL EGKRSKVTRR PKASDYQRLN LKL
//
ID   TGON2_MOUSE             Reviewed;         363 AA.
AC   Q62314;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-FEB-2011, entry version 70.
DE   RecName: Full=Trans-Golgi network integral membrane protein 2;
DE   AltName: Full=TGN38B;
DE   Flags: Precursor;
GN   Name=Tgoln2; Synonyms=Ttgn2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=95301533; PubMed=7540170; DOI=10.1074/jbc.270.24.14471;
RA   Kasai K., Takahashi S., Murakami K., Nakayama K.;
RT   "Strain-specific presence of two TGN38 isoforms and absence of TGN41
RT   in mouse.";
RL   J. Biol. Chem. 270:14471-14476(1995).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; SER-241; SER-288
RP   AND TYR-297, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; SER-240; SER-241
RP   AND SER-277, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May be involved in regulating membrane traffic to and
CC       from trans-Golgi network.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein (By similarity). Golgi apparatus, trans-Golgi network
CC       membrane; Single-pass type I membrane protein (By similarity).
CC       Note=Primarily in trans-Golgi network. Cycles between the trans-
CC       Golgi network and the cell surface returning via endosomes (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- MISCELLANEOUS: Not found in strains BALB/c, C57BL/6 and DBA/2.
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DR   EMBL; D50032; BAA08758.1; -; mRNA.
DR   IPI; IPI00124572; -.
DR   PIR; A56940; A56940.
DR   PIR; B56940; B56940.
DR   RefSeq; NP_033470.1; NM_009444.1.
DR   UniGene; Mm.246563; -.
DR   STRING; Q62314; -.
DR   PhosphoSite; Q62314; -.
DR   PRIDE; Q62314; -.
DR   Ensembl; ENSMUST00000070524; ENSMUSP00000068487; ENSMUSG00000056429.
DR   GeneID; 22135; -.
DR   KEGG; mmu:22135; -.
DR   CTD; 22135; -.
DR   MGI; MGI:105079; Tgoln2.
DR   GeneTree; ENSGT00530000064712; -.
DR   HOVERGEN; HBG060160; -.
DR   InParanoid; Q62314; -.
DR   NextBio; 302014; -.
DR   ArrayExpress; Q62314; -.
DR   Bgee; Q62314; -.
DR   Genevestigator; Q62314; -.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Golgi apparatus; Membrane;
KW   Phosphoprotein; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     17       Potential.
FT   CHAIN        18    363       Trans-Golgi network integral membrane
FT                                protein 2.
FT                                /FTId=PRO_0000022487.
FT   TOPO_DOM     18    308       Extracellular (Potential).
FT   TRANSMEM    309    329       Helical; (Potential).
FT   TOPO_DOM    330    363       Cytoplasmic (Potential).
FT   REPEAT      133    140       1.
FT   REPEAT      141    148       2.
FT   REPEAT      149    156       3.
FT   REPEAT      157    164       4.
FT   REPEAT      165    172       5.
FT   REPEAT      173    180       6.
FT   REPEAT      181    188       7.
FT   REGION      133    188       7 X 8 AA tandem repeats.
FT   MOTIF       356    359       Endocytosis signal (By similarity).
FT   MOD_RES      42     42       Phosphoserine (By similarity).
FT   MOD_RES     220    220       Phosphoserine.
FT   MOD_RES     240    240       Phosphoserine.
FT   MOD_RES     241    241       Phosphoserine.
FT   MOD_RES     277    277       Phosphoserine.
FT   MOD_RES     288    288       Phosphoserine.
FT   MOD_RES     297    297       Phosphotyrosine.
FT   CARBOHYD    303    303       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   363 AA;  38821 MW;  2826FA9E958C5C27 CRC64;
     MRFQVALLLL SVAVARALPP VYKRDADSGD SQNPPNQPSK QSSTPLPPES SNQVKTTRPT
     DGQGQKSDKK DQDKTTLAAV SSKAESGPPT AATDHSLGDS RRQPEKTDAE LKETARPLSP
     VNPKLEKSDQ SSTEDSGKPT GGNSGKPTGG DSGKPTGGDS DKPTEAGSNK ATEDDSGKST
     KVDLDKPTSK IFPDTETSKT DKVQPTEKGQ KATLTSKTES GETLAGDSDF SLKPEKGDKS
     SEPTEDVETK EIEEGDTEPE EGSPLEEENE KVSGPSSSEN QEGTLTDSMK NEKDDLYKDS
     SGNTSAESSH FFAYLVTAAV LVAVLYIAYH NKRKIIAFAL EGKRSKVTRR PKASDYQRLN
     LKL
//
ID   TIF1B_MOUSE             Reviewed;         834 AA.
AC   Q62318; P70391; Q8C283; Q99PN4;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 124.
DE   RecName: Full=Transcription intermediary factor 1-beta;
DE            Short=TIF1-beta;
DE   AltName: Full=KRAB-A-interacting protein;
DE   AltName: Full=KRIP-1;
DE   AltName: Full=Tripartite motif-containing protein 28;
GN   Name=Trim28; Synonyms=Krip1, Tif1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=97133299; PubMed=8978696;
RA   le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H.,
RA   Jeanmougin F., Losson R., Chambon P.;
RT   "A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic
RT   control of transcription by nuclear receptors.";
RL   EMBO J. 15:6701-6715(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Kidney;
RX   MEDLINE=97140325; PubMed=8986806; DOI=10.1073/pnas.93.26.15299;
RA   Kim S.-S., Chen Y.-M., O'Leary E., Witzgall R., Vidal M.,
RA   Bonventre J.V.;
RT   "A novel member of the RING finger family, KRIP-1, associates with the
RT   KRAB-A transcriptional repressor domain of zinc finger proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:15299-15304(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   MEDLINE=20400347; PubMed=10940561; DOI=10.1016/S0378-1119(00)00263-8;
RA   Cammas F., Garnier J.-M., Chambon P., Losson R.;
RT   "Correlation of the exon/intron organization to the conserved domains
RT   of the mouse transcriptional corepressor TIF1beta.";
RL   Gene 253:231-235(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2).
RX   MEDLINE=21231161; PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA   Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA   Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A.,
RA   Minucci S., Pelicci P.G., Ballabio A.;
RT   "The tripartite motif family identifies cell compartments.";
RL   EMBO J. 20:2140-2151(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 595-834 (ISOFORM 1).
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [7]
RP   INTERACTION WITH CEBPB AND NR3C1, AND FUNCTION.
RX   MEDLINE=98414604; PubMed=9742105;
RA   Chang C.J., Chen Y.L., Lee S.C.;
RT   "Coactivator TIF1beta interacts with transcription factor C/EBPbeta
RT   and glucocorticoid receptor to induce alpha1-acid glycoprotein gene
RT   expression.";
RL   Mol. Cell. Biol. 18:5880-5887(1998).
RN   [8]
RP   INTERACTION WITH HP1 PROTEINS.
RX   PubMed=10562550; DOI=10.1093/emboj/18.22.6385;
RA   Nielsen A.L., Ortiz J.A., You J., Oulad-Abdelghani M., Khechumian R.,
RA   Gansmuller A., Chambon P., Losson R.;
RT   "Interaction with members of the heterochromatin protein 1 (HP1)
RT   family and histone deacetylation are differentially involved in
RT   transcriptional silencing by members of the TIF1 family.";
RL   EMBO J. 18:6385-6395(1999).
RN   [9]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH HP1 PROTEINS.
RX   MEDLINE=99263008; PubMed=10330177;
RA   Ryan R.F., Schultz D.C., Ayyanathan K., Singh P.B., Friedman J.R.,
RA   Fredericks W.J., Rauscher F.J. III;
RT   "KAP-1 corepressor protein interacts and colocalizes with
RT   heterochromatic and euchromatic HP1 proteins: a potential role for
RT   Kruppel-associated box-zinc finger proteins in heterochromatin-
RT   mediated gene silencing.";
RL   Mol. Cell. Biol. 19:4366-4378(1999).
RN   [10]
RP   INTERACTION WITH ZNF382, AND SUBCELLULAR LOCATION.
RX   PubMed=11154279; DOI=10.1128/MCB.21.3.928-939.2001;
RA   Gebelein B., Urrutia R.;
RT   "Sequence-specific transcriptional repression by KS1, a multiple-zinc-
RT   finger-Kruppel-associated box protein.";
RL   Mol. Cell. Biol. 21:928-939(2001).
RN   [11]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12154074;
RA   Cammas F., Oulad-Abdelghani M., Vonesch J.-L., Huss-Garcia Y.,
RA   Chambon P., Losson R.;
RT   "Cell differentiation induces TIF1beta association with centromeric
RT   heterochromatin via an HP1 interaction.";
RL   J. Cell Sci. 115:3439-3448(2002).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-473, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-473 AND SER-501,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Forms a complex with a KRAB-domain transcription factor
CC       and increases the efficiency of KRAB-mediated repression. Silences
CC       transcription through an interaction with HP1 proteins. Acts as a
CC       corepressor of transcription for the KRAB zinc finger proteins and
CC       as a moderator of the repression activity (By similarity). May
CC       play a role as a coactivator for Cebpb and Nr3c1 in the
CC       transcriptional activation of the Alpha-1-acid glycoprotein gene.
CC   -!- SUBUNIT: Associated with HP1 alpha (CBX5), beta (CBX1) and gamma
CC       (CBX3) in interphase nuclei. Interacts with NCOR1 and CHD3.
CC       Interacts with CEBPB and NR3C1. Interacts with SETDB1, ZFP53 and
CC       ZFP68 (By similarity). Interacts directly with CBX5 via the PxVxL
CC       motif (By similarity). Interacts with ZNF382; enhances ZNF382
CC       transcriptional repressor activity. Interacts with ZNF256.
CC       Interacts with POGZ. Interacts with CBX5; POGZ and TRIM28 compete
CC       for interaction with CBX5 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Associated with centromeric
CC       heterochromatin during cell differentiation through CBX1.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q62318-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q62318-2; Sequence=VSP_010899, VSP_010900;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The HP1 box is both necessary and sufficient for HP1
CC       binding. The RING finger domain and th B-box domains mediate
CC       interaction with CEBPB. The PHD domain enhances the CEBPB
CC       transcriptional activity.
CC   -!- DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is
CC       required for interaction with chromoshadow domains. This motif
CC       requires additional residues -7, -6, +4 and +5 of the central Val
CC       which contact the chromoshadow domain.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC   -!- SIMILARITY: Contains 2 B box-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 bromo domain.
CC   -!- SIMILARITY: Contains 1 PHD-type zinc finger.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
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DR   EMBL; X99644; CAA67963.1; -; mRNA.
DR   EMBL; U67303; AAB17272.1; -; mRNA.
DR   EMBL; AF230878; AAG02638.1; -; Genomic_DNA.
DR   EMBL; AF230391; AAG50170.1; -; mRNA.
DR   EMBL; AF230392; AAG50171.1; -; mRNA.
DR   EMBL; BC058391; AAH58391.1; -; mRNA.
DR   EMBL; AK089084; BAC40742.1; -; mRNA.
DR   IPI; IPI00312128; -.
DR   IPI; IPI00453895; -.
DR   RefSeq; NP_035718.2; NM_011588.3.
DR   UniGene; Mm.15701; -.
DR   UniGene; Mm.398345; -.
DR   ProteinModelPortal; Q62318; -.
DR   SMR; Q62318; 64-141, 151-248, 624-812.
DR   IntAct; Q62318; 25.
DR   STRING; Q62318; -.
DR   PhosphoSite; Q62318; -.
DR   REPRODUCTION-2DPAGE; IPI00312128; -.
DR   REPRODUCTION-2DPAGE; Q62318; -.
DR   PRIDE; Q62318; -.
DR   Ensembl; ENSMUST00000005705; ENSMUSP00000005705; ENSMUSG00000005566.
DR   GeneID; 21849; -.
DR   KEGG; mmu:21849; -.
DR   CTD; 21849; -.
DR   MGI; MGI:109274; Trim28.
DR   eggNOG; roNOG13843; -.
DR   GeneTree; ENSGT00530000062982; -.
DR   HOGENOM; HBG268305; -.
DR   HOVERGEN; HBG055353; -.
DR   InParanoid; Q62318; -.
DR   OMA; PGMAIVK; -.
DR   OrthoDB; EOG4320XK; -.
DR   PhylomeDB; Q62318; -.
DR   NextBio; 301330; -.
DR   PMAP-CutDB; Q62318; -.
DR   ArrayExpress; Q62318; -.
DR   Bgee; Q62318; -.
DR   CleanEx; MM_TRIM28; -.
DR   Genevestigator; Q62318; -.
DR   GermOnline; ENSMUSG00000005566; Mus musculus.
DR   GO; GO:0005719; C:nuclear euchromatin; IDA:MGI.
DR   GO; GO:0005720; C:nuclear heterochromatin; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR   GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR   GO; GO:0016564; F:transcription repressor activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0001837; P:epithelial to mesenchymal transition; IDA:HGNC.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0043193; P:positive regulation of gene-specific transcription; IDA:HGNC.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:1.20.920.10; Bromodomain; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 2.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF00643; zf-B_box; 2.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 2.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00184; RING; 2.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; FALSE_NEG.
DR   PROSITE; PS50014; BROMODOMAIN_2; FALSE_NEG.
DR   PROSITE; PS50119; ZF_BBOX; 2.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Bromodomain; Isopeptide bond;
KW   Metal-binding; Nucleus; Phosphoprotein; Repeat; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    834       Transcription intermediary factor 1-beta.
FT                                /FTId=PRO_0000056393.
FT   DOMAIN      697    801       Bromo.
FT   ZN_FING      66    122       RING-type.
FT   ZN_FING     149    196       B box-type 1.
FT   ZN_FING     205    246       B box-type 2.
FT   ZN_FING     625    672       PHD-type.
FT   REGION      476    513       HP1 box.
FT   MOTIF       481    494       PxVxL motif.
FT   COMPBIAS      2     53       Ala-rich.
FT   COMPBIAS     54     57       Poly-Gly.
FT   COMPBIAS    526    531       Poly-Ala.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      18     18       Phosphoserine (By similarity).
FT   MOD_RES      21     21       Phosphoserine (By similarity).
FT   MOD_RES      23     23       Phosphoserine.
FT   MOD_RES      30     30       Phosphoserine (By similarity).
FT   MOD_RES      46     46       Phosphoserine (By similarity).
FT   MOD_RES      50     50       Phosphoserine (By similarity).
FT   MOD_RES      51     51       Phosphoserine (By similarity).
FT   MOD_RES     259    259       Phosphoserine (By similarity).
FT   MOD_RES     267    267       N6-acetyllysine (By similarity).
FT   MOD_RES     305    305       N6-acetyllysine (By similarity).
FT   MOD_RES     341    341       N6-acetyllysine (By similarity).
FT   MOD_RES     378    378       N6-acetyllysine (By similarity).
FT   MOD_RES     441    441       Phosphoserine (By similarity).
FT   MOD_RES     466    466       Phosphoserine (By similarity).
FT   MOD_RES     471    471       Phosphoserine (By similarity).
FT   MOD_RES     473    473       Phosphoserine.
FT   MOD_RES     479    479       Phosphoserine (By similarity).
FT   MOD_RES     489    489       Phosphoserine (By similarity).
FT   MOD_RES     501    501       Phosphoserine.
FT   MOD_RES     594    594       Phosphoserine (By similarity).
FT   MOD_RES     596    596       Phosphoserine (By similarity).
FT   MOD_RES     600    600       Phosphoserine (By similarity).
FT   MOD_RES     601    601       Phosphoserine (By similarity).
FT   MOD_RES     681    681       Phosphoserine (By similarity).
FT   MOD_RES     683    683       Phosphoserine (By similarity).
FT   MOD_RES     689    689       Phosphoserine (By similarity).
FT   MOD_RES     752    752       Phosphoserine (By similarity).
FT   MOD_RES     757    757       Phosphoserine (By similarity).
FT   MOD_RES     770    770       N6-acetyllysine (By similarity).
FT   MOD_RES     774    774       N6-acetyllysine (By similarity).
FT   MOD_RES     824    824       Phosphoserine (By similarity).
FT   CROSSLNK    676    676       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    750    750       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    779    779       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO-1) (By
FT                                similarity).
FT   CROSSLNK    804    804       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO-1) (By
FT                                similarity).
FT   VAR_SEQ     500    500       D -> L (in isoform 2).
FT                                /FTId=VSP_010899.
FT   VAR_SEQ     501    834       Missing (in isoform 2).
FT                                /FTId=VSP_010900.
FT   CONFLICT    530    530       A -> S (in Ref. 2; AAB17272).
FT   CONFLICT    821    821       G -> C (in Ref. 5; AAH58391).
SQ   SEQUENCE   834 AA;  88847 MW;  DE87AAA5DC67BB8B CRC64;
     MAASAAATAA ASAATAASAA SGSPGSGEGS AGGEKRPAAS SAAAASAAAS SPAGGGGEAQ
     ELLEHCGVCR ERLRPERDPR LLPCLHSACS ACLGPATPAA ANNSGDGGSA GDGAMVDCPV
     CKQQCYSKDI VENYFMRDSG SKASSDSQDA NQCCTSCEDN APATSYCVEC SEPLCETCVE
     AHQRVKYTKD HTVRSTGPAK TRDGERTVYC NVHKHEPLVL FCESCDTLTC RDCQLNAHKD
     HQYQFLEDAV RNQRKLLASL VKRLGDKHAT LQKNTKEVRS SIRQVSDVQK RVQVDVKMAI
     LQIMKELNKR GRVLVNDAQK VTEGQQERLE RQHWTMTKIQ KHQEHILRFA SWALESDNNT
     ALLLSKKLIY FQLHRALKMI VDPVEPHGEM KFQWDLNAWT KSAEAFGKIV AERPGTNSTG
     PGPMAPPRAP GPLSKQGSGS SQPMEVQEGY GFGSDDPYSS AEPHVSGMKR SRSGEGEVSG
     LLRKVPRVSL ERLDLDLTSD SQPPVFKVFP GSTTEDYNLI VIERGAAAAA AGQAGTVPPG
     APGAPPLPGM AIVKEEETEA AIGAPPAAPE GPETKPVLMP LTEGPGAEGP RLASPSGSTS
     SGLEVVAPEV TSAPVSGPGI LDDSATICRV CQKPGDLVMC NQCEFCFHLD CHLPALQDVP
     GEEWSCSLCH VLPDLKEEDG SLSLDGADST GVVAKLSPAN QRKCERVLLA LFCHEPCRPL
     HQLATDSTFS MEQPGGTLDL TLIRARLQEK LSPPYSSPQE FAQDVGRMFK QFNKLTEDKA
     DVQSIIGLQR FFETRMNDAF GDTKFSAVLV EPPPLNLPSA GLSSQELSGP GDGP
//
ID   RU17_MOUSE              Reviewed;         448 AA.
AC   Q62376; Q3UIW4;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=U1 small nuclear ribonucleoprotein 70 kDa;
DE            Short=U1 snRNP 70 kDa;
DE            Short=U1-70K;
DE            Short=snRNP70;
GN   Name=Snrnp70; Synonyms=Snrp70;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 71-448 (ISOFORMS 1 AND 2).
RC   STRAIN=BALB/c;
RX   MEDLINE=89276388; PubMed=2525092;
RX   DOI=10.1111/j.1432-1033.1989.tb14798.x;
RA   Hornig H., Fischer U., Costas M., Rauh A., Luehrmann R.;
RT   "Analysis of genomic clones of the murine U1RNA-associated 70-kDa
RT   protein reveals a high evolutionary conservation of the protein
RT   between human and mouse.";
RL   Eur. J. Biochem. 182:45-50(1989).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Mediates the splicing of pre-mRNA by binding to the loop
CC       I region of U1-snRNA. The truncated isoform cannot bind U1-snRNA
CC       (By similarity).
CC   -!- SUBUNIT: Found in a pre-mRNA splicing complex with SFRS4, SFRS5,
CC       SNRNP70, SNRPA1, SRRM1 and SRRM2. Found in a pre-mRNA exonic
CC       splicing enhancer (ESE) complex with SNRNP70, SNRPA1, SRRM1 and
CC       TRA2B/SFRS10. Interacts with dephosphorylated SFRS13A and SFPQ.
CC       Interacts with NUDT21/CPSF5, CPSF6, SCAF11 and ZRANB2 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q62376-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q62376-2; Sequence=VSP_005851, VSP_005852;
CC   -!- PTM: Extensively phosphorylated on serine residues in the C-
CC       terminal region (By similarity).
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK133115; BAE21515.1; -; mRNA.
DR   EMBL; AK146729; BAE27392.1; -; mRNA.
DR   EMBL; X15769; CAA33777.1; -; Genomic_DNA.
DR   EMBL; X15770; CAA33777.1; JOINED; Genomic_DNA.
DR   EMBL; X15771; CAA33777.1; JOINED; Genomic_DNA.
DR   EMBL; X15772; CAA33777.1; JOINED; Genomic_DNA.
DR   EMBL; X15774; CAA33777.1; JOINED; Genomic_DNA.
DR   EMBL; X15775; CAA33777.1; JOINED; Genomic_DNA.
DR   EMBL; X15776; CAA33777.1; JOINED; Genomic_DNA.
DR   IPI; IPI00230541; -.
DR   IPI; IPI00625105; -.
DR   PIR; S04336; S04336.
DR   PIR; S04824; S04824.
DR   RefSeq; NP_033250.3; NM_009224.4.
DR   UniGene; Mm.216386; -.
DR   ProteinModelPortal; Q62376; -.
DR   SMR; Q62376; 99-181.
DR   MINT; MINT-1868298; -.
DR   STRING; Q62376; -.
DR   PhosphoSite; Q62376; -.
DR   PRIDE; Q62376; -.
DR   Ensembl; ENSMUST00000063243; ENSMUSP00000065824; ENSMUSG00000063511.
DR   Ensembl; ENSMUST00000074575; ENSMUSP00000074160; ENSMUSG00000063511.
DR   GeneID; 20637; -.
DR   KEGG; mmu:20637; -.
DR   NMPDR; fig|10090.3.peg.16477; -.
DR   UCSC; uc009guw.1; mouse.
DR   CTD; 20637; -.
DR   MGI; MGI:98341; Snrnp70.
DR   HOVERGEN; HBG094947; -.
DR   InParanoid; Q62376; -.
DR   OMA; DGRDMYM; -.
DR   OrthoDB; EOG4CJVJ7; -.
DR   PhylomeDB; Q62376; -.
DR   NextBio; 299035; -.
DR   ArrayExpress; Q62376; -.
DR   Bgee; Q62376; -.
DR   Genevestigator; Q62376; -.
DR   GermOnline; ENSMUSG00000063511; Mus musculus.
DR   GO; GO:0005681; C:spliceosomal complex; ISS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0000398; P:nuclear mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR022023; U1snRNP70_N.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF12220; U1snRNP70_N; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Nucleus; Phosphoprotein;
KW   Ribonucleoprotein; RNA-binding.
FT   CHAIN         1    448       U1 small nuclear ribonucleoprotein 70
FT                                kDa.
FT                                /FTId=PRO_0000081881.
FT   DOMAIN      103    181       RRM.
FT   COMPBIAS    231    310       Arg/Glu-rich (mixed charge).
FT   COMPBIAS    311    326       Poly-Gly.
FT   COMPBIAS    356    403       Arg/Asp/Glu-rich (mixed charge).
FT   COMPBIAS    404    409       Poly-Gly.
FT   MOD_RES     118    118       N6-acetyllysine (By similarity).
FT   MOD_RES     126    126       Phosphotyrosine (By similarity).
FT   MOD_RES     162    162       N6-acetyllysine (By similarity).
FT   MOD_RES     226    226       Phosphoserine.
FT   MOD_RES     266    266       Phosphoserine (By similarity).
FT   MOD_RES     268    268       Phosphoserine (By similarity).
FT   MOD_RES     332    332       Phosphoserine (By similarity).
FT   MOD_RES     408    408       Phosphoserine.
FT   VAR_SEQ     160    166       AYKHADG -> TTQLACS (in isoform 2).
FT                                /FTId=VSP_005851.
FT   VAR_SEQ     167    448       Missing (in isoform 2).
FT                                /FTId=VSP_005852.
FT   CONFLICT    263    263       R -> Q (in Ref. 2; CAA33777).
FT   CONFLICT    281    281       S -> T (in Ref. 2; CAA33777).
SQ   SEQUENCE   448 AA;  51992 MW;  5B025A3B6992D0BD CRC64;
     MTQFLPPNLL ALFAPRDPIP YLPPLEKLPH EKHHNQPYCG IAPYIREFED PRDAPPPTRA
     ETREERMERK RREKIERRQQ EVETELKMWD PHNDPNAQGD AFKTLFVARV NYDTTESKLR
     REFEVYGPIK RIHMVYSKRS GKPRGYAFIE YEHERDMHSA YKHADGKKID GRRVLVDVER
     GRTVKGWRPR RLGGGLGGTR RGGADVNIRH SGRDDTSRYD ERPGPSPLPH RDRDRDRERE
     RRERSRERDK ERERRRSRSR DRRRRSRSRD KDERRRSRER SKDKDRDRKR RSSRSRERAR
     RERERKEELR GGGGGGGGGS GGGGGGDMAE PSEAGDGAPD DGPPGELGPE GPDGPEEKGR
     DRDRERRRSH RSERERRRDR DRDRDREHKR GERGSERGRD EARGGGGSGQ DNGLEGLGSD
     GRDMYMEAEG GDGYMAPENG YLMEAAPE
//
ID   SPT6H_MOUSE             Reviewed;        1726 AA.
AC   Q62383; Q5SYM0; Q6GQS3; Q6ZQI0; Q8BQY6;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 2.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Transcription elongation factor SPT6;
GN   Name=Supt6h; Synonyms=Kiaa0162;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster;
RX   MEDLINE=96374824; PubMed=8786132; DOI=10.1006/geno.1996.0294;
RA   Chiang P.-W., Wang S., Smithivas P., Song W.-J., Ramamoorthy S.,
RA   Hillman J., Puett S., Van Keuren M.L., Crombez E., Kumar A.,
RA   Glover T.W., Miller D.E., Tsai C.-H., Blackburn C.C., Chen X.-N.,
RA   Sun Z., Cheng J.-F., Korenberg J.R., Kurnit D.M.;
RT   "Identification and analysis of the human and murine putative
RT   chromatin structure regulator SUPT6H and Supt6h.";
RL   Genomics 34:328-333(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 498-1726.
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1359-1726.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Acts to stimulate transcriptional elongation by RNA
CC       polymerase II (By similarity).
CC   -!- SUBUNIT: Interacts with RNA polymerase II and the DRB sensitivity-
CC       inducing factor complex (DSIF complex), which is composed of
CC       SUPT5H and SUPT4H1 or SUPT4H2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- SIMILARITY: Belongs to the SPT6 family.
CC   -!- SIMILARITY: Contains 1 S1 motif domain.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
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DR   EMBL; U40375; AAB18950.1; -; mRNA.
DR   EMBL; AL591070; CAI24323.1; -; Genomic_DNA.
DR   EMBL; BC072657; AAH72657.1; -; mRNA.
DR   EMBL; AK129069; BAC97879.1; -; mRNA.
DR   EMBL; AK046156; BAC32616.1; -; mRNA.
DR   IPI; IPI00454050; -.
DR   PIR; T30810; T30810.
DR   RefSeq; NP_033323.2; NM_009297.2.
DR   UniGene; Mm.20755; -.
DR   ProteinModelPortal; Q62383; -.
DR   SMR; Q62383; 1324-1517.
DR   STRING; Q62383; -.
DR   PhosphoSite; Q62383; -.
DR   PRIDE; Q62383; -.
DR   Ensembl; ENSMUST00000002121; ENSMUSP00000002121; ENSMUSG00000002052.
DR   Ensembl; ENSMUST00000108314; ENSMUSP00000103950; ENSMUSG00000002052.
DR   GeneID; 20926; -.
DR   KEGG; mmu:20926; -.
DR   UCSC; uc007kip.1; mouse.
DR   CTD; 20926; -.
DR   MGI; MGI:107726; Supt6h.
DR   GeneTree; ENSGT00510000047446; -.
DR   HOGENOM; HBG381660; -.
DR   HOVERGEN; HBG093994; -.
DR   InParanoid; Q62383; -.
DR   OMA; VTIAGEN; -.
DR   OrthoDB; EOG44F687; -.
DR   PhylomeDB; Q62383; -.
DR   NextBio; 299837; -.
DR   ArrayExpress; Q62383; -.
DR   Bgee; Q62383; -.
DR   CleanEx; MM_SUPT6H; -.
DR   Genevestigator; Q62383; -.
DR   GermOnline; ENSMUSG00000002052; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003711; F:transcription elongation regulator activity; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEA:InterPro.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR016027; NA-bd_OB-fold-like.
DR   InterPro; IPR003029; Rbsml_prot_S1_RNA-bd_dom.
DR   InterPro; IPR022967; RNA-binding_domain_S1.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR023323; Tex-like_dom.
DR   InterPro; IPR023097; Tex_RuvX-like_dom.
DR   InterPro; IPR017072; TF_Spt6.
DR   InterPro; IPR006641; YqgF/RNaseH-like_dom.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   Gene3D; G3DSA:3.30.420.140; Resolv_Hlld_junc_YqgF-like; 1.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF00575; S1; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PIRSF; PIRSF036947; Spt6; 1.
DR   SMART; SM00316; S1; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00732; YqgFc; 1.
DR   SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR   PROSITE; PS50126; S1; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   1726       Transcription elongation factor SPT6.
FT                                /FTId=PRO_0000072172.
FT   DOMAIN     1213   1282       S1 motif.
FT   DOMAIN     1325   1431       SH2.
FT   COILED        3     51       Potential.
FT   COMPBIAS      6    250       Asp/Glu-rich.
FT   MOD_RES       7      7       Phosphoserine (By similarity).
FT   MOD_RES      12     12       Phosphoserine (By similarity).
FT   MOD_RES      73     73       Phosphoserine (By similarity).
FT   MOD_RES      75     75       Phosphoserine (By similarity).
FT   MOD_RES      78     78       Phosphoserine (By similarity).
FT   MOD_RES     125    125       Phosphoserine.
FT   MOD_RES     179    179       Phosphoserine (By similarity).
FT   MOD_RES     267    267       Phosphoserine (By similarity).
FT   MOD_RES     743    743       N6-acetyllysine (By similarity).
FT   MOD_RES    1523   1523       Phosphothreonine (By similarity).
FT   MOD_RES    1526   1526       Phosphoserine (By similarity).
FT   MOD_RES    1532   1532       Phosphothreonine (By similarity).
FT   MOD_RES    1535   1535       Phosphoserine (By similarity).
FT   MOD_RES    1539   1539       Phosphothreonine (By similarity).
FT   MOD_RES    1676   1676       N6-acetyllysine (By similarity).
FT   MOD_RES    1697   1697       Phosphothreonine (By similarity).
FT   MOD_RES    1701   1701       Phosphoserine (By similarity).
FT   MOD_RES    1703   1703       Phosphoserine (By similarity).
FT   MOD_RES    1718   1718       Phosphothreonine (By similarity).
FT   CONFLICT    609    609       T -> A (in Ref. 1; AAB18950).
FT   CONFLICT   1520   1520       P -> Q (in Ref. 5; BAC32616).
SQ   SEQUENCE   1726 AA;  199086 MW;  98BD891493372166 CRC64;
     MSDFVESEAE ESEEEYNHEG EVVPRVTKKF VEEEDDDEEE EEENLDDQDE RGNLKDFIND
     DDDEEEGEED EGSDSGDSED DVGHKKRKRP SFDDRLEDDD FDLIEENLGV KVKRGQKYRR
     VKKMSDDDED DEEEYGKEEH EKEAIAGEIF QDEEGEEGQE AVEAPMAPPD EEEEDDEESD
     IDDFIVDDDG QPLKKPKWRK KLPGYTDAAL QEAQEIFGVD FDYDEFEKYN EYDEELEEDY
     EYEDDETEGE IRVRPKKTTK KRVSRRSIFE MYEPSELESS HLTDQDNEIR ATDLPERFQL
     RSIPVKAAED DELEEEADWI YRNAFATPTI SLQDSCDYLD RGQPTSSFSR KGPSTVQKIK
     EALGFMRNQH FEVPFIAFYR KEYVEPELHI NDLWRVWQWD EKWTQLRIRK ENLTRLFEKM
     QAYQYEQISA DPDKPLADGI RALDTTDMER LKDVQSMDEL KDVYNHFLLY YGRDIPKMQN
     AAKASRKKLK RIKEDGDEEG EGEEAEDEEQ RGPELKQASR RDMYTICQSA GLDGLAKKFG
     LTPEQFGENL RDSYQRHETE QFPAEPLELA KDYVCSQFPT PEAVLEGARY MVALQIAREP
     LVRQVLRQTF QERAKLNITP TKKGRKDVDE AHYAYSFKYL KNKPVKELRD DQFLKIGLAE
     DEGLLTIDIS IDMKGVEGYG NDQTYFEEIK QFYYRDEFSH QVQEWNRQRT MAIERALQQF
     LYVQMAKELK NKLLAEARES VVKACSRKLY NWLRVAPYRP DQQVEEDDDF MDENQGKGIR
     VLGIAFSSAR DHPVFCALVN GEGEVTDFLR LPHFTKRRTA WREEEREKKA QDIETLKKFL
     VNKKPHVVTI AGENRDAQML TEDVKRIVHE LDQGQQLSSI GVELVDNELA ILYMNSKKSE
     AEFRDYPPVL RQAVSLARRI QDPLIEFAQV CSSDEDILCL KFHPLQEHVV KEELLNALYC
     EFINRVNEVG VDVNRAIAHP YSQALIQYVC GLGPRKGTHL LKILKQNNTR LESRTQLVTM
     CHMGPKVFMN CAGFLKIDTA SLGDSTDSYI EVLDGSRVHP ETYEWARKMA VDALEYDESA
     EDANPAGALE EILENPERLK DLDLDAFAEE LERQGYGDKH ITLYDIRAEL SCRYKDLRTA
     YRSPNTEEIF NMLTKETPET FYIGKLIICN VTGIAHRRPQ GESYDQAIRN DETGLWQCPF
     CQQDNFPELS EVWNHFDSGS CPGQAIGVKT RLDNGVTGFI PTKFLSDKVV KRPEERVKVG
     MTVHCRIMKI DIEKFSADLT CRTSDLMDRN NEWKLPKDTY YDFDAEAADH KQEEDMKRKQ
     QRTTYIKRVI AHPSFHNINF KQAEKMMETM DQGDVIIRPS SKGENHLTVT WKVSAGIYQH
     VDVREEGKEN AFSLGATLWI NSEEFEDLDE IVARYVQPMA SFARDLLNHK YYQDCSGGDR
     KKLEELLIKT KKEKPTFIPY FICACKELPG KFLLGYQPRG KPRIEYVTVT PEGFRYRGQI
     FPTVNGLFRW FKDHYQDPVP GITPSSSNRT RTPASINATP ANINLADLTR AVNALPQNMT
     SQMFSAIAAV TGQGQNPNAT PAQWASSQYG YGGSGGGSSA YHVFPTPAQQ PVATPLMTPS
     YSYTTPSQPI TTPQYHQLQA STTPQSTQAQ PQPSSSSRQR QQQPKSNSHA AIDWGKMAEQ
     WLQEKEAERR KQKQRLTPRP SPSPMIESTP MSIAGDATPL LDEMDR
//
ID   TPD52_MOUSE             Reviewed;         224 AA.
AC   Q62393; Q545M5; Q8CCU1; Q8K564; Q99KP8;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 2.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Tumor protein D52;
DE            Short=mD52;
GN   Name=Tpd52;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Mammary gland;
RX   MEDLINE=97001154; PubMed=8812487; DOI=10.1006/geno.1996.0393;
RA   Byrne J.A., Mattei M.-G., Basset P.;
RT   "Definition of the tumor protein D52 (TPD52) gene family through
RT   cloning of D52 homologues in human (hD53) and mouse (mD52).";
RL   Genomics 35:523-532(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Zhou J.-G., Huang C.-F.;
RT   "Cloning and characterization of PC-1 homolog in Mouse (mPC-1).";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Amnion, Bone marrow macrophage, Dendritic cell,
RC   Medulla oblongata, Placenta, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 110-123, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=96197754; PubMed=8632896;
RA   Chen S.-L., Maroulakou I.G., Green J.E., Romano-Spica V., Modi W.,
RA   Lautenberger J., Bhat N.K.;
RT   "Isolation and characterization of a novel gene expressed in multiple
RT   cancers.";
RL   Oncogene 12:741-751(1996).
CC   -!- SUBUNIT: Forms homodimer or heterodimer with other members of the
CC       family (By similarity).
CC   -!- INTERACTION:
CC       Self; NbExp=1; IntAct=EBI-782591, EBI-782591;
CC       P55327:TPD52 (xeno); NbExp=1; IntAct=EBI-782591, EBI-782581;
CC       O43399-2:TPD52L2 (xeno); NbExp=1; IntAct=EBI-782591, EBI-782616;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q62393-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q62393-2; Sequence=VSP_037379;
CC       Name=3;
CC         IsoId=Q62393-3; Sequence=VSP_037379, VSP_037380;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Isoform 2 is expressed at higher levels in
CC       kidney and brain than in liver, lung, testis and heart. Within the
CC       brain, isoform 2 is highly expressed in the granular layer of the
CC       cerebellum, the cortex and the hippocampus. In embryos, isoform 2
CC       is expressed in the epithelium of the developing intestine,
CC       stomach, olfactory epithelium, neuronal layers of the retina,
CC       salivary gland, kidney and dorsal root ganglion.
CC   -!- SIMILARITY: Belongs to the TPD52 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; U44426; AAB40897.1; -; mRNA.
DR   EMBL; AY048852; AAL05266.1; -; mRNA.
DR   EMBL; AK005456; BAB24048.1; -; mRNA.
DR   EMBL; AK032111; BAC27709.1; -; mRNA.
DR   EMBL; AK151471; BAE30428.1; -; mRNA.
DR   EMBL; AK151744; BAE30655.1; -; mRNA.
DR   EMBL; AK152543; BAE31298.1; -; mRNA.
DR   EMBL; AK153266; BAE31856.1; -; mRNA.
DR   EMBL; AK153292; BAE31875.1; -; mRNA.
DR   EMBL; AK161753; BAE36558.1; -; mRNA.
DR   EMBL; AK168379; BAE40308.1; -; mRNA.
DR   EMBL; AK168817; BAE40644.1; -; mRNA.
DR   EMBL; AK169751; BAE41345.1; -; mRNA.
DR   EMBL; AK170725; BAE41982.1; -; mRNA.
DR   EMBL; AK171050; BAE42212.1; -; mRNA.
DR   EMBL; CH466577; EDL05193.1; -; Genomic_DNA.
DR   EMBL; BC002036; AAH02036.1; -; mRNA.
DR   EMBL; BC004068; AAH04068.1; -; mRNA.
DR   EMBL; BC094018; AAH94018.1; -; mRNA.
DR   IPI; IPI00408626; -.
DR   IPI; IPI00473743; -.
DR   IPI; IPI00622833; -.
DR   RefSeq; NP_001020432.1; NM_001025261.1.
DR   RefSeq; NP_001020433.1; NM_001025262.1.
DR   RefSeq; NP_001020434.1; NM_001025263.1.
DR   RefSeq; NP_001020435.1; NM_001025264.1.
DR   RefSeq; NP_033438.1; NM_009412.2.
DR   UniGene; Mm.371590; -.
DR   IntAct; Q62393; 10.
DR   STRING; Q62393; -.
DR   PhosphoSite; Q62393; -.
DR   PRIDE; Q62393; -.
DR   Ensembl; ENSMUST00000094381; ENSMUSP00000091943; ENSMUSG00000027506.
DR   GeneID; 21985; -.
DR   KEGG; mmu:21985; -.
DR   UCSC; uc008oov.1; mouse.
DR   CTD; 21985; -.
DR   MGI; MGI:107749; Tpd52.
DR   eggNOG; roNOG16849; -.
DR   GeneTree; ENSGT00390000015988; -.
DR   HOVERGEN; HBG058643; -.
DR   PhylomeDB; Q62393; -.
DR   NextBio; 301708; -.
DR   ArrayExpress; Q62393; -.
DR   Bgee; Q62393; -.
DR   CleanEx; MM_TPD52; -.
DR   Genevestigator; Q62393; -.
DR   GermOnline; ENSMUSG00000027506; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0030183; P:B cell differentiation; ISS:UniProtKB.
DR   InterPro; IPR007327; TPD52.
DR   PANTHER; PTHR19307; TPD52; 1.
DR   Pfam; PF04201; TPD52; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Direct protein sequencing;
KW   Phosphoprotein.
FT   CHAIN         1    224       Tumor protein D52.
FT                                /FTId=PRO_0000185739.
FT   COILED       61    113       Potential.
FT   MOD_RES     170    170       Phosphoserine (By similarity).
FT   MOD_RES     172    172       Phosphothreonine (By similarity).
FT   MOD_RES     175    175       Phosphoserine (By similarity).
FT   MOD_RES     223    223       Phosphoserine (By similarity).
FT   VAR_SEQ       1     45       MECRDMELADDYQSPFDFDSGVNKNYLYLSPSGNTSPPGSP
FT                                TQNV -> MDRGEQ (in isoform 2 and isoform
FT                                3).
FT                                /FTId=VSP_037379.
FT   VAR_SEQ     168    168       K -> NIRSIQHSISMPAMR (in isoform 3).
FT                                /FTId=VSP_037380.
FT   CONFLICT    129    129       V -> L (in Ref. 5; AAH04068).
SQ   SEQUENCE   224 AA;  24313 MW;  C80D8AB9038B0D73 CRC64;
     MECRDMELAD DYQSPFDFDS GVNKNYLYLS PSGNTSPPGS PTQNVGLLKT EPVAEEGEDA
     VTMLSAPEAL TEEEQEELRR ELTKVEEEIQ TLSQVLAAKE KHLAELKRKL GISSLQEFKQ
     NIAKGWQDVT ATNAYKKTSE TLSQAGQKAS AAFSSVGSVI TKKLEDVKNS PTFKSFEEKV
     ENLKSKVGGA KPAGGDFGEV LNSTANATST MTTEPPPEQM TESP
//
ID   ZN185_MOUSE             Reviewed;         352 AA.
AC   Q62394;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   30-NOV-2010, entry version 63.
DE   RecName: Full=Zinc finger protein 185;
DE   AltName: Full=LIM domain protein Zfp185;
DE   AltName: Full=P1-A;
GN   Name=Znf185; Synonyms=Zfp185;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96425694; PubMed=8828036;
RA   Levin M.L., Chatterjee A., Pragliola A., Worley K.C., Wehnert M.,
RA   Zhuchenko O., Smith R.F., Lee C.C., Herman G.E.;
RT   "A comparative transcription map of the murine bare patches (Bpa) and
RT   striated (Str) critical regions and human Xq28.";
RL   Genome Res. 6:465-477(1996).
CC   -!- FUNCTION: May be involved in the regulation of cellular
CC       proliferation and/or differentiation (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Cell junction, focal adhesion (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in skin, kidney, ovary, testis. Also
CC       expressed in brain, cartilage, heart, lung, spleen and thymus.
CC   -!- DEVELOPMENTAL STAGE: At E14.5, only expressed in mesenchymal
CC       cells. At E16.5 expressed also in cells lining the vertebrae and
CC       tendons of the proximal tail. In late embryogenesis, expressed in
CC       mesenchymal cells adjacent to the distal limb bones (tibia and
CC       calcaneum), in tendons and in the connective tissue sheath
CC       (epimysium) surrounding the skeletal muscle. Also expressed in the
CC       epithelia of the epididymis of the testis.
CC   -!- SIMILARITY: Contains 1 LIM zinc-binding domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U46687; AAC52628.1; -; mRNA.
DR   IPI; IPI00387481; -.
DR   RefSeq; NP_001102513.1; NM_001109043.1.
DR   RefSeq; NP_033575.3; NM_009549.3.
DR   UniGene; Mm.1161; -.
DR   ProteinModelPortal; Q62394; -.
DR   SMR; Q62394; 290-352.
DR   STRING; Q62394; -.
DR   PhosphoSite; Q62394; -.
DR   PRIDE; Q62394; -.
DR   Ensembl; ENSMUST00000114543; ENSMUSP00000110190; ENSMUSG00000031351.
DR   GeneID; 22673; -.
DR   KEGG; mmu:22673; -.
DR   CTD; 22673; -.
DR   MGI; MGI:108095; Zfp185.
DR   eggNOG; roNOG17401; -.
DR   HOVERGEN; HBG071794; -.
DR   ArrayExpress; Q62394; -.
DR   Bgee; Q62394; -.
DR   CleanEx; MM_ZFP185; -.
DR   Genevestigator; Q62394; -.
DR   GermOnline; ENSMUSG00000031351; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001781; Znf_LIM.
DR   Gene3D; G3DSA:2.10.110.10; Znf_LIM; 1.
DR   SMART; SM00132; LIM; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cytoplasm; Cytoskeleton; LIM domain; Metal-binding;
KW   Phosphoprotein; Zinc.
FT   CHAIN         1    352       Zinc finger protein 185.
FT                                /FTId=PRO_0000075912.
FT   DOMAIN      292    347       LIM zinc-binding.
FT   COMPBIAS     23     26       Poly-Glu.
FT   MOD_RES     183    183       Phosphoserine (By similarity).
SQ   SEQUENCE   352 AA;  38322 MW;  2AB1F833D7AF1A5C CRC64;
     MTTEDYKKLA PYNIRRSSIS GTEEEEVPFT PDEQKRRSQA ALGVLRKTAP REHSYVLSAA
     KKTTSSPTQE LQSPFLAKRV DVVDEDVLPE KNQEPPALAR PDSGLSSSTT EKIAHRQITP
     PTAELHLVAP DLEALSTPDS CEENNAAPKI IKEIPGTLQD GQSDPTVASQ QLADLSILEP
     LGSPSGAEQQ IKAEDCTNML MSPSSCMVTV TVSDTSEQSQ LCVPGVSSKV DSSSTIKGIL
     FVKEYMNTSE VSSGKPVSSH CDSPSSIEDS LDLAKKPPHE GTPSERPTEG VCTYCSHEIQ
     DCPKITLEHL GICCHEYCFK CGICNKPMGD LLDQIFIHRD TIHCGKCYEK LF
//
ID   SPEG_MOUSE              Reviewed;        3262 AA.
AC   Q62407; Q3TPH8; Q6P5V1; Q80TF7; Q80ZN0; Q8BZF4; Q9EQJ5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 100.
DE   RecName: Full=Striated muscle-specific serine/threonine-protein kinase;
DE            EC=2.7.11.1;
DE   AltName: Full=Aortic preferentially expressed protein 1;
DE            Short=APEG-1;
GN   Name=Speg; Synonyms=Apeg1, Kiaa1297;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY,
RP   SUBCELLULAR LOCATION, AND INDUCTION.
RC   STRAIN=C57BL/6;
RX   MEDLINE=96291890; PubMed=8663449; DOI=10.1074/jbc.271.29.17354;
RA   Hsieh C.-M., Yoshizumi M., Endege W.O., Kho C.-J., Jain M.K.,
RA   Kashiki S., de Los Santos R., Lee W.-S., Perrella M.A., Lee M.-E.;
RT   "APEG-1, a novel gene preferentially expressed in aortic smooth muscle
RT   cells, is down-regulated by vascular injury.";
RL   J. Biol. Chem. 271:17354-17359(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), TISSUE
RP   SPECIFICITY, AND PHOSPHORYLATION.
RC   STRAIN=BALB/c;
RX   MEDLINE=20538441; PubMed=10973969; DOI=10.1074/jbc.M006028200;
RA   Hsieh C.-M., Fukumoto S., Layne M.D., Maemura K., Charles H.,
RA   Patel A., Perrella M.A., Lee M.-E.;
RT   "Striated muscle preferentially expressed genes alpha and beta are two
RT   serine/threonine protein kinases derived from the same gene as the
RT   aortic preferentially expressed gene-1.";
RL   J. Biol. Chem. 275:36966-36973(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 723-3262 (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Embryonic brain, and Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2092-3262.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481 AND SER-1177, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Isoform 3 may have a role in regulating the growth and
CC       differentiation of arterial smooth muscle cells.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Isoform 3 is found as a monomer or homodimer (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 3: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=SPEG-beta;
CC         IsoId=Q62407-1; Sequence=Displayed;
CC       Name=2; Synonyms=BPEG;
CC         IsoId=Q62407-2; Sequence=VSP_018265, VSP_018266, VSP_018267,
CC                                  VSP_018268;
CC       Name=3; Synonyms=APEG1;
CC         IsoId=Q62407-3; Sequence=VSP_018264, VSP_018267;
CC         Note=Produced by alternative promoter usage;
CC       Name=4; Synonyms=SPEG-alpha;
CC         IsoId=Q62407-4; Sequence=VSP_018264;
CC         Note=No experimental confirmation available. Produced by
CC         alternative promoter usage;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is preferentially expressed in
CC       striated muscle. Non-kinase form such as isoform 3 is
CC       predominantly expressed in the aorta. Isoform 3 appears to be
CC       expressed only in highly differentiated ASMC in normal vessel
CC       walls and down-regulated in dedifferentiated ASMC in vivo. In
CC       response to vascular injuries ASMC dedifferentiate and change from
CC       a quiescent and contractile phenotype to a proliferative and
CC       synthetic phenotype. This proliferation of vascular smooth muscle
CC       cells is one of the most prominent features of arteriosclerosis.
CC   -!- INDUCTION: Isoform 3 is quickly down-regulated in response to
CC       vascular injury, when ASMC cells change from a quiescent to a
CC       proliferative phenotype.
CC   -!- PTM: May be autophosphorylated. Phosphorylated upon DNA damage,
CC       probably by ATM or ATR (By similarity).
CC   -!- MISCELLANEOUS: Expression is under the tight control of the locus
CC       control region (LCRs).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family.
CC   -!- SIMILARITY: Contains 2 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 9 Ig-like (immunoglobulin-like) domains.
CC   -!- SIMILARITY: Contains 2 protein kinase domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG34791.1; Type=Frameshift; Positions=2957, 2992;
CC   -----------------------------------------------------------------------
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DR   EMBL; U57098; AAC52666.1; -; mRNA.
DR   EMBL; AF215896; AAG34791.1; ALT_FRAME; mRNA.
DR   EMBL; AK035543; BAC29098.1; -; mRNA.
DR   EMBL; AK164360; BAE37758.1; -; mRNA.
DR   EMBL; BC048698; AAH48698.3; -; mRNA.
DR   EMBL; BC062643; AAH62643.1; -; mRNA.
DR   EMBL; AK122488; BAC65770.1; -; mRNA.
DR   IPI; IPI00331223; -.
DR   IPI; IPI00752259; -.
DR   IPI; IPI00755319; -.
DR   IPI; IPI00762377; -.
DR   RefSeq; NP_001078839.1; NM_001085370.1.
DR   RefSeq; NP_001078840.1; NM_001085371.1.
DR   RefSeq; NP_001166948.1; NM_001173477.1.
DR   UniGene; Mm.275397; -.
DR   ProteinModelPortal; Q62407; -.
DR   SMR; Q62407; 43-199, 725-1385, 1393-1581, 1599-1862, 2555-2770, 2951-3238.
DR   STRING; Q62407; -.
DR   PhosphoSite; Q62407; -.
DR   PRIDE; Q62407; -.
DR   Ensembl; ENSMUST00000038230; ENSMUSP00000045263; ENSMUSG00000026207.
DR   Ensembl; ENSMUST00000087122; ENSMUSP00000084361; ENSMUSG00000026207.
DR   GeneID; 11790; -.
DR   KEGG; mmu:11790; -.
DR   UCSC; uc007boz.1; mouse.
DR   UCSC; uc007bpa.1; mouse.
DR   UCSC; uc007bpc.1; mouse.
DR   CTD; 11790; -.
DR   MGI; MGI:109282; Speg.
DR   eggNOG; roNOG09264; -.
DR   GeneTree; ENSGT00600000084221; -.
DR   HOVERGEN; HBG083339; -.
DR   InParanoid; Q62407; -.
DR   OrthoDB; EOG4J6RPZ; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 279613; -.
DR   ArrayExpress; Q62407; -.
DR   Bgee; Q62407; -.
DR   CleanEx; MM_SPEG; -.
DR   Genevestigator; Q62407; -.
DR   GermOnline; ENSMUSG00000026207; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR020675; Myosin_light_chain_kin-rel.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR015726; Ser/Thr_kin_striated_muscle-sp.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 11.
DR   PANTHER; PTHR22964; Myosin_light_chain_kin-rel; 1.
DR   PANTHER; PTHR22964:SF9; Ser/Thr_kinase_striated_musc; 1.
DR   Pfam; PF07679; I-set; 8.
DR   Pfam; PF00069; Pkinase; 2.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 5.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF49265; FN_III-like; 2.
DR   SUPFAM; SSF56112; Kinase_like; 2.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS50835; IG_LIKE; 8.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE   1: Evidence at protein level;
KW   Alternative promoter usage; Alternative splicing; ATP-binding;
KW   Differentiation; Disulfide bond; Immunoglobulin domain; Kinase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Repeat;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1   3262       Striated muscle-specific
FT                                serine/threonine-protein kinase.
FT                                /FTId=PRO_0000072667.
FT   DOMAIN       45    126       Ig-like 1.
FT   DOMAIN      727    815       Ig-like 2.
FT   DOMAIN      874    963       Ig-like 3.
FT   DOMAIN      968   1062       Ig-like 4.
FT   DOMAIN     1069   1157       Ig-like 5.
FT   DOMAIN     1193   1283       Ig-like 6.
FT   DOMAIN     1287   1382       Fibronectin type-III 1.
FT   DOMAIN     1389   1485       Ig-like 7.
FT   DOMAIN     1490   1578       Ig-like 8.
FT   DOMAIN     1606   1859       Protein kinase 1.
FT   DOMAIN     2586   2676       Ig-like 9.
FT   DOMAIN     2681   2772       Fibronectin type-III 2.
FT   DOMAIN     2946   3213       Protein kinase 2.
FT   NP_BIND    1612   1620       ATP (By similarity).
FT   COMPBIAS    277    348       Pro-rich.
FT   COMPBIAS    530    639       Pro-rich.
FT   COMPBIAS   1924   1929       Poly-Ser.
FT   COMPBIAS   1930   1936       Poly-Glu.
FT   COMPBIAS   2180   2320       Pro-rich.
FT   COMPBIAS   2775   2962       Pro-rich.
FT   COMPBIAS   3241   3244       Poly-Arg.
FT   ACT_SITE   1724   1724       Proton acceptor (By similarity).
FT   ACT_SITE   3080   3080       Proton acceptor (By similarity).
FT   BINDING    1635   1635       ATP (By similarity).
FT   MOD_RES     316    316       Phosphoserine.
FT   MOD_RES     439    439       Phosphoserine.
FT   MOD_RES     453    453       Phosphothreonine (By similarity).
FT   MOD_RES     457    457       Phosphoserine (By similarity).
FT   MOD_RES     481    481       Phosphoserine.
FT   MOD_RES     604    604       Phosphothreonine (By similarity).
FT   MOD_RES    1177   1177       Phosphoserine.
FT   DISULFID    994   1046       By similarity.
FT   DISULFID   1413   1469       By similarity.
FT   DISULFID   2608   2660       By similarity.
FT   VAR_SEQ       1    854       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_018264.
FT   VAR_SEQ       1    106       Missing (in isoform 2).
FT                                /FTId=VSP_018265.
FT   VAR_SEQ     107    131       VYSCSAQNERGQASCEAVLTVLEVR -> MKKLWVKKRFQK
FT                                TGHSRRAFGRLTH (in isoform 2).
FT                                /FTId=VSP_018266.
FT   VAR_SEQ     966    967       AH -> GE (in isoform 2 and isoform 3).
FT                                /FTId=VSP_018267.
FT   VAR_SEQ     968   3262       Missing (in isoform 2).
FT                                /FTId=VSP_018268.
FT   CONFLICT   3237   3237       L -> R (in Ref. 3; BAC65770).
SQ   SEQUENCE   3262 AA;  354343 MW;  0387BDD6518B7BB7 CRC64;
     MQKARGTRGE DAGTRAPPSP GVPPKRAKVG AGRGVLVTGD GAGAPVFLRP LKNAAVCAGS
     DVRLRVVVSG TPQPSLSWFR DGQLLPPPAP EPSCLWLRSC GAQDAGVYSC SAQNERGQAS
     CEAVLTVLEV RDSETAEDDI SDVPGTQRLE LRDDRAFSTP TGGSDTLVGT SLDTPPTSVT
     GTSEEQVSWW GSGQTVLEQE AGSGGGTRPL PGSPRQAQTT GAGPRHLGVE PLVRASRANL
     VGASWGSEDS LSVASDLYGS AFSLYRGRAL SIHVSIPPSG LHREEPDLQP QPASDALRPR
     PALPPPSKSA LLPPPSPRVG KRALPGPSTQ PPATPTSPHR RAQEPSLPED ITTTEEKRGK
     KPKSSGPSLA GTVESRPQTP LSEASGRLSA LGRSPRLVRA GSRILDKLQF FEERRRSLER
     SDSPPAPLRP WVPLRKARSL EQPKSEGGAA WGTPEASQEE LRSPRGSVAE RRRLFQQKAA
     SLDERTRQRS ATSDLELRFA QELGRIRRST SREELVRSHE SLRATLQRAP SPREPGEPPL
     FSRPSTPKTS RAVSPAATQP PPPSGAGKSG DEPGRPRSRG PVGRTEPGEG PQQEIKRRDQ
     FPLTRSRAIQ ECRSPVPPYT ADPPESRTKA PSGRKREPPA QAVRFLPWAT PGVEDSVLPQ
     TLEKNRAGPE AEKRLRRGPE EDGPWGPWDR RGTRSQGKGR RARPTSPELE SSDDSYVSAG
     EEPLEAPVFE IPLQNMVVAP GADVLLKCII TANPPPQVSW KKDGSMLHSE GRLLIRAEGE
     RHTLLLREAQ AADAGSYTAT ATNELGQATC ASSLAVRPGG STSPFSSPIT SDEEYLSPPE
     EFPEPGETWP RTPTMKLSPS QDHDSSDSSS KAPPTFKVSL MDQSVREGQD VIMSIRVQGE
     PKPVVSWLRN RQPVRPDQRR FAEEAEGGLC RLRILAAERG DAGFYTCKAV NEYGARQCEA
     RLEVRAHPES RSLAVLAPLQ DVDVGAGEMA LFECLVAGPA DVEVDWLCRG RLLQPALLKC
     KMHFDGRKCK LLLTSVHEDD SGVYTCKLST AKDELTCSAR LTVRPSLAPL FTRLLEDVEV
     LEGRAARLDC KISGTPPPSV TWTHFGHPVN EGDNLRLRQD GGLHSLHIAR VGSEDEGLYE
     VSATNTHGQA HCSAQLYVEE PRTAASGPSS KLEKMPSIPE EPEHGDLERL SIPDFLRPLQ
     DLEVGLAKEA MLECQVTGLP YPTISWFHNG HRIQSSDDRR MTQYRDIHRL VFPAVGPQHA
     GVYKSVIANK LGKAACYAHL YVTDVVPGPP DGAPEVVAVT GRMVTLSWNP PRSLDMAIDP
     DSLTYTVQHQ VLGSDQWTAL VTGLREPAWA ATGLKKGIQH IFRVLSSSGK SSSKPSAPSE
     PVQLLEHGPP LEEAPAVLDK QDIVYVVEGQ PACVTVTFNH VEAQVVWRSC RGALLEARTG
     VYELSQPDDD QYCLRICRVS RRDLGPLTCS ARNRHGTKAC SVTLELAEAP RFESIMEDVE
     VGPGETARFA VVVEGKPLPD IMWYKDEVLL AESNHVSFVY EENECSLVLL SAGSQDGGVY
     TCTARNLAGE VSCKAELSVL SAQTAMEVEG VGEDEEHRGR RLSDYYDIHQ EIGRGAFSYL
     RRVVERSSGL EFAAKFIPSQ AKPKASARRE ARLLARLQHG CVLYFHEAFE RRRGLVIVTE
     LCTEELLERM ARKPTVCESE TRTYMRQVLE GICYLHQSHV LHLDVKPENL LVWDGAGGEE
     QVRICDFGNA QELTPGEPQY CQYGTPEFVA PEIVNQSPVS GVTDIWPVGV VAFLCLTGIS
     PFVGENDRTT LMNIRNYNVA FEETTFLSLS REARGFLIKV LVQDRLRPTA EETLEHPWFK
     TEAKGAEVST DHLKLFLSRR RWQRSQISYK CHLVLRPIPE LLRAPPERVW VAMPRRQPPS
     GGLSSSSDSE EEELEELPSV PRPLQPEFSG SRVSLTDIPT EDEALGTPEA GAATPMDWQE
     QERTPSKDQE APSPEALPSP GQESPDGPSP RRPELRRGSS AESALPRVGS REPGRSLHKA
     ASVELPQRRS PSPGATRLTR GGLGEGEYAQ RLQALRQRLL RGGPEDGKVS GLRGPLLESL
     GGRARDPRMA RAASSEAAPH HQPPPESRGL QKSSSFSQGE AEPRGRHRRA GAPLEIPVAR
     LGARRLQESP SLSALSETQP PSPARPSVPK LSITKSPEPS AVTSRDSPQP PEPQPVPEKV
     PEPKPEPVRA AKPAQPPLAL QMPTQPLTPY AQIMQSLQLS SPTLSPQDPA VPPSEPKPHA
     AVFARVASPP PGVSEKRVPS ARTPPVLAEK ARVPTVPPRP GSSLSGSIEN LESEAVFEAK
     FKRSRESPLS RGLRLLSRSR SEERGPFRGA EDDGIYRPSP AGTPLELVRR PERSRSVQDL
     RVAGEPGLVR RLSLSLSQKL RRTPPGQRHP AWESRSGDGE SSEGGSSARA SPVLAVRRRL
     SSTLERLSSR LQRSGSSEDS GGASGRSTPL FGRLRRATSE GESLRRLGVP HNQLGSQTGA
     TTPSAESLGS EASGTSGSSA PGESRSRHRW GLSRLRKDKG LSQPNLSSSV QEDLGHQYVP
     SESDFPPVFH IKLKDQVLLE GEAATLLCLP AACPAPRISW MKDKQSLRSE PSVVIVSCKD
     GRQLLSIPRA GKRHAGLYEC SATNVLGSIT SSCTVAVARI PGKLAPPEVP QTYHDTALVV
     WKPGDGRAPC TYTLERRVDG ESVWHPVSSG IPDCYYNVTQ LPVGVTVRFR VACSNRAGQG
     PFSNPSEKVF IRGTPDSPAQ PAAAPRDAPV TSGPTRAPPP DSPTSLAPTP ALAPPASQAS
     TLSPSTSSMS ANQALSSLKA VGPPPATPPR KHRGLLATQQ AEPSPPSIVV TPSEPRSFVP
     DTGTLTPTSS PQGVKPAPSS TSLYMVTSFV SAPPAPQAPA PEPPPEPTKV TVRSLSPAKE
     VVSSPTPEST TLRQGPPQKP YTFLEEKARG RFGVVRSCRE NATGRTFVAK IVPYAAEGKR
     RVLQEYEVLR TLHHERLMSL HEAYITPRYL VLIAESCGNR ELLCGLSDRF RYSEDDVATY
     VVQLLQGLDY LHGHHVLHLD IKPDNLLLAA DNALKIVDFG SAQPYNPQAL KPLGHRTGTL
     EFMAPEMVKG DPIGSATDIW GAGVLTYIML SGYSPFYEPD PQETEARIVG GRFDAFQLYP
     NTSQSATLFL RKVLSVHPWS RPSLQDCLAH PWLQDAYLMK LRRQTLTFTT NRLKEFLGEQ
     RRRRAEAATR HKVLLRSYPG SP
//
ID   ASPP1_MOUSE             Reviewed;        1087 AA.
AC   Q62415;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-AUG-2003, sequence version 2.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Apoptosis-stimulating of p53 protein 1;
DE   AltName: Full=Protein phosphatase 1 regulatory subunit 13B;
GN   Name=Ppp1r13b; Synonyms=Aspp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 944-1087.
RX   MEDLINE=98294438; PubMed=9630982; DOI=10.1038/nbt0696-741;
RA   Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.;
RT   "Cloning of ligand targets: systematic isolation of SH3 domain-
RT   containing proteins.";
RL   Nat. Biotechnol. 14:741-744(1996).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-669, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332 AND SER-335, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Regulator that plays a central role in regulation of
CC       apoptosis via its interaction with p53/TP53. Regulates TP53 by
CC       enhancing the DNA binding and transactivation function of TP53 on
CC       the promoters of proapoptotic genes in vivo (By similarity).
CC   -!- SUBUNIT: Interacts with TP53 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Predominantly cytoplasmic (By similarity). Some
CC       fraction is nuclear.
CC   -!- DOMAIN: The ankyrin repeats and the SH3 domain are required for a
CC       specific interactions with TP53 (By similarity).
CC   -!- MISCELLANEOUS: In contrast to its official gene name, it is not a
CC       regulatory subunit of protein phosphatase 1. This name was given
CC       due to its similarity with a protein that binds to protein
CC       phosphatase 1.
CC   -!- SIMILARITY: Belongs to the ASPP family.
CC   -!- SIMILARITY: Contains 2 ANK repeats.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; BC054788; AAH54788.1; -; mRNA.
DR   EMBL; BC053092; AAH53092.1; -; mRNA.
DR   EMBL; U58881; AAC52638.1; -; mRNA.
DR   IPI; IPI00354665; -.
DR   RefSeq; NP_035755.1; NM_011625.1.
DR   UniGene; Mm.313076; -.
DR   ProteinModelPortal; Q62415; -.
DR   SMR; Q62415; 1-83, 885-1077.
DR   STRING; Q62415; -.
DR   PhosphoSite; Q62415; -.
DR   PRIDE; Q62415; -.
DR   Ensembl; ENSMUST00000054815; ENSMUSP00000062464; ENSMUSG00000021285.
DR   GeneID; 21981; -.
DR   KEGG; mmu:21981; -.
DR   UCSC; uc007ped.1; mouse.
DR   CTD; 21981; -.
DR   MGI; MGI:1336199; Ppp1r13b.
DR   GeneTree; ENSGT00600000084381; -.
DR   HOGENOM; HBG443981; -.
DR   HOVERGEN; HBG050596; -.
DR   InParanoid; Q62415; -.
DR   OrthoDB; EOG4RNB7N; -.
DR   NextBio; 301692; -.
DR   ArrayExpress; Q62415; -.
DR   Bgee; Q62415; -.
DR   Genevestigator; Q62415; -.
DR   GermOnline; ENSMUSG00000021285; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0006917; P:induction of apoptosis; ISS:UniProtKB.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 2.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Apoptosis; Cytoplasm; Nucleus; Phosphoprotein; Repeat;
KW   SH3 domain.
FT   CHAIN         1   1087       Apoptosis-stimulating of p53 protein 1.
FT                                /FTId=PRO_0000066963.
FT   REPEAT      917    949       ANK 1.
FT   REPEAT      950    982       ANK 2.
FT   DOMAIN     1016   1078       SH3.
FT   COMPBIAS    132    292       Gln-rich.
FT   COMPBIAS    446    857       Pro-rich.
FT   MOD_RES     332    332       Phosphoserine.
FT   MOD_RES     335    335       Phosphoserine.
FT   MOD_RES     669    669       Phosphoserine.
FT   MOD_RES     679    679       Phosphoserine (By similarity).
SQ   SEQUENCE   1087 AA;  119170 MW;  8B3E9CC4B2390F13 CRC64;
     MMPMILTVFL SNNEQILTEV PITPETTCRD VVEFCKEPGE GGCHLAEVWR GSERPIPYDH
     MMYEHLQKWG PRREEVKFFL RHEDSPTESS EQGARQTQEQ RTQRSVVNVP GEKRTENGVG
     NPRVELTLSE LQDMAARQQQ QIENQQQMLV AKEQRLHFLK QQERRQQQSV SENEKLQKLK
     ERVEAQENKL KKIRAMRGQV DYSKIMNGNL SAEIERFSAM FQEKKQEVQT AILRVDQLSQ
     QLEDLKKGKL NGFQSYNGRL TGPAAVELKR LYQELQIRNQ LNQEQNSKLQ QQKELLNKRN
     MEVAMMDKRI SELRERLYGK KIQLNRVNGT SSPQSPLSTS GRVAAVGPYI QVPSTGGFPL
     PGDPVKPQSL TIASSAAHGR SKSANDGNWP PLKQNSASVK STQMTGDWKD SGMEGTLKQG
     AISSQPLPLS ALGATEKLGI EIGKGPPPIP GVGKPLPPSY GTYPSSGPLG PGSTSSLERR
     KEGSLPRPGA GPPSRQKPAP LPPASNAPQP GSSQQIQQRI SVPPSPTYPP AGPPAFPTGD
     GKPELPLTVA IRPFLADKGS RPQSPRKGPQ TVNSSSIYSM YLQQATPPKN YQPPAHGTLN
     KSVKAVYGKP VLPSGSASPS PLPFLHGSLG TGTAQPQPPS DSAEKEPEQE GPSVPGEGST
     VESLPRPLSP TKLTPIVHSP LRYQSDADLE ALRRKLANAP RPLKKRSSIT EPEGPGGPNI
     QKLLYQRFNT LAGGMEGTPF YQPSPSQDFV GTLADMDNGN TNANGNLDEP FPPRPTAPLP
     EELAPSSDAN DNELPSPEPE ELICPQTTHQ TAEPTEDNNN NVAPVPSTEQ IPSPVAEAPS
     EEDQVPPAPL SPVIHPPAAS ASKRTNLKKP NSERTGHGLR VRFNPLALLL DASLEGEFDL
     VQRIIYEVED PSKPNDEGIT PLHNAVCAGH HHIVKFLLDF GVNVNAADSD GWTPLHCAAS
     CNSVHLCKQL VESGAAIFAS TISDIETAAD KCEEMEEGYI QCSQFLYGVQ EKLGVMNKGT
     VYALWDYEAQ NSDELSFHEG DAITILRRKD ENETEWWWAR LGDREGYVPK NLLGLYPRIK
     PRQRTLA
//
ID   SRBS1_MOUSE             Reviewed;        1290 AA.
AC   Q62417; Q80TF8; Q8BZI3; Q8K3Y2; Q921F8; Q9Z0Z8; Q9Z0Z9;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   08-FEB-2011, entry version 95.
DE   RecName: Full=Sorbin and SH3 domain-containing protein 1;
DE   AltName: Full=Ponsin;
DE   AltName: Full=SH3 domain protein 5;
DE   AltName: Full=SH3P12;
DE   AltName: Full=c-Cbl-associated protein;
DE            Short=CAP;
GN   Name=Sorbs1; Synonyms=Kiaa1296, Sh3d5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RC   TISSUE=Embryo;
RX   MEDLINE=98294438; PubMed=9630982; DOI=10.1038/nbt0696-741;
RA   Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.;
RT   "Cloning of ligand targets: systematic isolation of SH3 domain-
RT   containing proteins.";
RL   Nat. Biotechnol. 14:741-744(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, TISSUE SPECIFICITY,
RP   AND INTERACTION WITH CBL AND INSULIN RECEPTOR.
RX   MEDLINE=98107672; PubMed=9447983;
RA   Ribon V., Printen J.A., Hoffman N.G., Kay B.K., Saltiel A.R.;
RT   "A novel, multifunctional c-Cbl binding protein in insulin receptor
RT   signaling in 3T3-L1 adipocytes.";
RL   Mol. Cell. Biol. 18:872-879(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND INTERACTION WITH MLLT4 AND VCL.
RC   TISSUE=Brain;
RX   MEDLINE=99187134; PubMed=10085297; DOI=10.1083/jcb.144.5.1001;
RA   Mandai K., Nakanishi H., Satoh A., Takahashi K., Satoh K.,
RA   Nishioka H., Mizoguchi A., Takai Y.;
RT   "Ponsin/SH3P12: an l-afadin- and vinculin-binding protein localized at
RT   cell-cell and cell-matrix adherens junctions.";
RL   J. Cell Biol. 144:1001-1017(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=15047181; DOI=10.1016/j.bbrc.2004.03.038;
RA   Alcazar O., Ho R.C., Fujii N., Goodyear L.J.;
RT   "cDNA cloning and functional characterization of a novel splice
RT   variant of c-Cbl-associated protein from mouse skeletal muscle.";
RL   Biochem. Biophys. Res. Commun. 317:285-293(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [6]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC   STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PTK2.
RX   PubMed=9461600; DOI=10.1074/jbc.273.7.4073;
RA   Ribon V., Herrera R., Kay B.K., Saltiel A.R.;
RT   "A role for CAP, a novel, multifunctional Src homology 3 domain-
RT   containing protein in formation of actin stress fibers and focal
RT   adhesions.";
RL   J. Biol. Chem. 273:4073-4080(1998).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FLOTILLIN.
RX   PubMed=11001060; DOI=10.1038/35025089;
RA   Baumann C.A., Ribon V., Kanzaki M., Thurmond D.C., Mora S.,
RA   Shigematsu S., Bickel P.E., Pessin J.E., Saltiel A.R.;
RT   "CAP defines a second signalling pathway required for insulin-
RT   stimulated glucose transport.";
RL   Nature 407:202-207(2000).
RN   [11]
RP   INTERACTION WITH CBLB.
RX   PubMed=12842890; DOI=10.1074/jbc.M300664200;
RA   Liu J., DeYoung S.M., Hwang J.B., O'Leary E.E., Saltiel A.R.;
RT   "The roles of Cbl-b and c-Cbl in insulin-stimulated glucose
RT   transport.";
RL   J. Biol. Chem. 278:36754-36762(2003).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270; THR-286 AND
RP   SER-345, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [13]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452088; DOI=10.1074/mcp.T500040-MCP200;
RA   Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G.,
RA   Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F.,
RA   Maltby D.A., Schoepfer R., Burlingame A.L.;
RT   "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT   preparations using lectin weak affinity chromatography and mass
RT   spectrometry.";
RL   Mol. Cell. Proteomics 5:923-934(2006).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-89 AND TYR-103, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-184 AND SER-533, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-407, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-286 AND SER-432, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Plays a role in tyrosine phosphorylation of CBL by
CC       linking CBL to the insulin receptor. Required for insulin-
CC       stimulated glucose transport. Involved in formation of actin
CC       stress fibers and focal adhesions.
CC   -!- SUBUNIT: Interacts (via SH3 domain 2) with PXN (By similarity).
CC       Interacts with the long isoform of MLLT4/afadin and with VCL.
CC       MLLT4 and VCL bind to SORBS1 in a competitive manner and do not
CC       form a ternary complex. Interacts with ABL1, CBL, CBLB and
CC       INPPL1/SHIP2 through the third SH3 domain. Interaction with ABL1
CC       occurs only after insulin stimulation while this has no effect on
CC       the interaction with INPPL1. Interacts with the insulin receptor
CC       but dissociates from it following insulin stimulation. Also
CC       interacts with SCA7, PTK2/p125FAK and flotillin.
CC   -!- SUBCELLULAR LOCATION: Cell junction, adherens junction. Cell
CC       membrane. Cytoplasm, cytoskeleton. Cell junction, focal adhesion
CC       (By similarity). Note=Colocalized with PXN at focal adhesions
CC       during myogenic differentiation (By similarity). Colocalizes with
CC       actin stress fibers. Also detected at the plasma membrane and in
CC       neuronal intranuclear inclusions.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=1;
CC         IsoId=Q62417-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2; Synonyms=CAPsm;
CC         IsoId=Q62417-2; Sequence=VSP_050886, VSP_050889, VSP_050890,
CC                                  VSP_050892;
CC       Name=3; Synonyms=Ponsin-2;
CC         IsoId=Q62417-3; Sequence=VSP_050886, VSP_050891, VSP_050892,
CC                                  VSP_050893;
CC       Name=4; Synonyms=Ponsin-1;
CC         IsoId=Q62417-4; Sequence=VSP_050885, VSP_050886, VSP_050889,
CC                                  VSP_050890, VSP_050892, VSP_050893;
CC       Name=5;
CC         IsoId=Q62417-5; Sequence=VSP_050886, VSP_050889, VSP_050890,
CC                                  VSP_050892, VSP_050893;
CC       Name=6;
CC         IsoId=Q62417-6; Sequence=VSP_050886, VSP_050887, VSP_050889,
CC                                  VSP_050890, VSP_050892, VSP_050893;
CC         Note=No experimental confirmation available;
CC       Name=7;
CC         IsoId=Q62417-7; Sequence=VSP_050886, VSP_050888, VSP_050889,
CC                                  VSP_050890, VSP_050892, VSP_050894;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues tested: heart, brain,
CC       spleen, lung, liver, muscle, kidney and testis. Expressed in 3T3-
CC       L1 adipocytes but not in 3T3-L1 fibroblasts.
CC   -!- PTM: O-glycosylated.
CC   -!- SIMILARITY: Contains 3 SH3 domains.
CC   -!- SIMILARITY: Contains 1 SoHo domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65769.2; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; U58883; AAC71776.1; -; mRNA.
DR   EMBL; AF078666; AAD16007.1; -; mRNA.
DR   EMBL; AF078667; AAD16008.1; -; mRNA.
DR   EMBL; AF521593; AAM77354.1; -; mRNA.
DR   EMBL; AK122487; BAC65769.2; ALT_INIT; mRNA.
DR   EMBL; AK035212; BAC28980.1; -; mRNA.
DR   EMBL; BC012703; AAH12703.1; -; mRNA.
DR   IPI; IPI00125895; -.
DR   IPI; IPI00129707; -.
DR   IPI; IPI00129708; -.
DR   IPI; IPI00458043; -.
DR   IPI; IPI00458047; -.
DR   IPI; IPI00458048; -.
DR   IPI; IPI00468140; -.
DR   RefSeq; NP_001030134.1; NM_001034962.1.
DR   RefSeq; NP_001030135.1; NM_001034963.1.
DR   RefSeq; NP_001030136.1; NM_001034964.1.
DR   UniGene; Mm.210815; -.
DR   UniGene; Mm.417719; -.
DR   UniGene; Mm.440351; -.
DR   ProteinModelPortal; Q62417; -.
DR   SMR; Q62417; 1047-1289.
DR   IntAct; Q62417; 1.
DR   MINT; MINT-1342490; -.
DR   STRING; Q62417; -.
DR   PhosphoSite; Q62417; -.
DR   PRIDE; Q62417; -.
DR   Ensembl; ENSMUST00000025972; ENSMUSP00000025972; ENSMUSG00000025006.
DR   Ensembl; ENSMUST00000025973; ENSMUSP00000025973; ENSMUSG00000025006.
DR   Ensembl; ENSMUST00000099465; ENSMUSP00000097064; ENSMUSG00000025006.
DR   Ensembl; ENSMUST00000099466; ENSMUSP00000097065; ENSMUSG00000025006.
DR   GeneID; 20411; -.
DR   KEGG; mmu:20411; -.
DR   UCSC; uc008hkm.1; mouse.
DR   UCSC; uc008hkn.1; mouse.
DR   UCSC; uc008hko.1; mouse.
DR   UCSC; uc008hkp.1; mouse.
DR   UCSC; uc008hkq.1; mouse.
DR   UCSC; uc008hkr.1; mouse.
DR   UCSC; uc008hks.1; mouse.
DR   CTD; 20411; -.
DR   MGI; MGI:700014; Sorbs1.
DR   eggNOG; roNOG04222; -.
DR   GeneTree; ENSGT00550000074287; -.
DR   HOVERGEN; HBG053053; -.
DR   InParanoid; Q62417; -.
DR   NextBio; 298396; -.
DR   ArrayExpress; Q62417; -.
DR   Bgee; Q62417; -.
DR   CleanEx; MM_SORBS1; -.
DR   Genevestigator; Q62417; -.
DR   GermOnline; ENSMUSG00000025006; Mus musculus.
DR   GO; GO:0005913; C:cell-cell adherens junction; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR   GO; GO:0005158; F:insulin receptor binding; IDA:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; IDA:MGI.
DR   GO; GO:0005070; F:SH3/SH2 adaptor activity; IPI:BHF-UCL.
DR   GO; GO:0048041; P:focal adhesion assembly; IDA:UniProtKB.
DR   GO; GO:0015758; P:glucose transport; IDA:UniProtKB.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0090004; P:positive regulation of establishment of protein localization in plasma membrane; IMP:BHF-UCL.
DR   GO; GO:0046326; P:positive regulation of glucose import; IMP:BHF-UCL.
DR   GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IMP:BHF-UCL.
DR   GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IMP:BHF-UCL.
DR   GO; GO:0043149; P:stress fiber assembly; IDA:UniProtKB.
DR   InterPro; IPR000108; p67phox.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR003127; Sorb.
DR   Pfam; PF00018; SH3_1; 2.
DR   Pfam; PF07653; SH3_2; 1.
DR   Pfam; PF02208; Sorb; 1.
DR   PRINTS; PR00499; P67PHOX.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 3.
DR   SMART; SM00459; Sorb; 1.
DR   SUPFAM; SSF50044; SH3; 3.
DR   PROSITE; PS50002; SH3; 3.
DR   PROSITE; PS50831; SOHO; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Cytoplasm;
KW   Cytoskeleton; Glycoprotein; Membrane; Phosphoprotein; Repeat;
KW   SH3 domain; Transport.
FT   CHAIN         1   1290       Sorbin and SH3 domain-containing protein
FT                                1.
FT                                /FTId=PRO_0000072186.
FT   DOMAIN      202    247       SoHo.
FT   DOMAIN     1049   1108       SH3 1.
FT   DOMAIN     1123   1184       SH3 2.
FT   DOMAIN     1236   1290       SH3 3.
FT   MOD_RES      48     48       Phosphotyrosine (By similarity).
FT   MOD_RES      55     55       Phosphoserine (By similarity).
FT   MOD_RES      58     58       Phosphoserine.
FT   MOD_RES      89     89       Phosphothreonine.
FT   MOD_RES     103    103       Phosphotyrosine.
FT   MOD_RES     184    184       Phosphothreonine.
FT   MOD_RES     261    261       Phosphoserine (By similarity).
FT   MOD_RES     270    270       Phosphoserine.
FT   MOD_RES     286    286       Phosphothreonine.
FT   MOD_RES     345    345       Phosphoserine.
FT   MOD_RES     407    407       Phosphoserine.
FT   MOD_RES     432    432       Phosphoserine.
FT   MOD_RES     533    533       Phosphoserine.
FT   MOD_RES    1201   1201       Phosphoserine (By similarity).
FT   MOD_RES    1209   1209       Phosphoserine (By similarity).
FT   VAR_SEQ      26     26       K -> KADPFRARSISAVKIIPVKTVKSPSGLVLPP (in
FT                                isoform 4).
FT                                /FTId=VSP_050885.
FT   VAR_SEQ      70     78       Missing (in isoform 2, isoform 3, isoform
FT                                4, isoform 5, isoform 6 and isoform 7).
FT                                /FTId=VSP_050886.
FT   VAR_SEQ     117    117       G -> GATSSSSAPSEG (in isoform 6).
FT                                /FTId=VSP_050887.
FT   VAR_SEQ     117    117       G -> GATSSSSAPSEVIVVPLYLVNTDRGQGQEGTARTPA
FT                                SLGPLGCVHTVPATTPAASPLTFPTLDDFIPPHLQRRPHHS
FT                                QPASACGSLSPASQTSPPSPPPPLVPPVPEDLHRGLEPDLP
FT                                GAVSSTG (in isoform 7).
FT                                /FTId=VSP_050888.
FT   VAR_SEQ     163    163       R -> REQQKRLSSLS (in isoform 2, isoform
FT                                4, isoform 5, isoform 6 and isoform 7).
FT                                /FTId=VSP_050889.
FT   VAR_SEQ     341    402       Missing (in isoform 2, isoform 4, isoform
FT                                5, isoform 6 and isoform 7).
FT                                /FTId=VSP_050890.
FT   VAR_SEQ     369    402       TNLEKDLSFCQAELEADLEKVETVNKSPSANSPQ -> PPK
FT                                KIWDYTPGDCSILPREDRK (in isoform 3).
FT                                /FTId=VSP_050891.
FT   VAR_SEQ     477    965       Missing (in isoform 2, isoform 3, isoform
FT                                4, isoform 5, isoform 6 and isoform 7).
FT                                /FTId=VSP_050892.
FT   VAR_SEQ     994   1049       Missing (in isoform 3, isoform 4, isoform
FT                                5 and isoform 6).
FT                                /FTId=VSP_050893.
FT   VAR_SEQ    1212   1290       QPQAQQRRVTPDRSQPSLDLCSYQALYSYVPQNDDELELRD
FT                                GDIVDVMEKCDDGWFVGTSRRTRQFGTFPGNYVKPLYL ->
FT                                VSKLSNSACSFHPQLCQRHTALLGLLFHALIKSYLEQAGWE
FT                                FFSYMSVAFS (in isoform 7).
FT                                /FTId=VSP_050894.
FT   CONFLICT    205    205       A -> T (in Ref. 7; BAC28980).
FT   CONFLICT    308    308       L -> P (in Ref. 7; BAC28980).
FT   CONFLICT   1004   1004       K -> M (in Ref. 4; AAM77354).
SQ   SEQUENCE   1290 AA;  143070 MW;  07C9A74BD794E390 CRC64;
     MSSECDVGSS KAVVNGLASG NHGPDKDMDP TKICTGKGTV TLRASSSYRG TPSSSPVSPQ
     ESPKHESKSG LEPEDPSADE WKLSSSADTN GNAQPSPLAA KGYRSVHPSL SADKPQGSPL
     LNEVSSSHIE TDSQDFPPTS RPSSAYPSTT IVNPTIVLLQ HNRDPASERR AGEQDPVPTP
     AELTSPGRAS ERRAKDASRR VVRSAQDLSD VSTDEVGIPL RNTERSKDWY KTMFKQIHKL
     NRDDDSDVHS PRYSFSDDTK SPLSVPRSKS EMNYIEGEKV VKRSATLPLP ARSSSLKSSP
     ERNDWEPLDK KVDTRKYRAE PKSIYEYQPG KSSVLTNEKM SRDISPEEID LKNEPWYKFF
     SELEFGRPTN LEKDLSFCQA ELEADLEKVE TVNKSPSANS PQSSAVSPTP DITSEPPGYI
     YSSNFHAVKR ESDGTPGGLA SLENERQIYK SVLEGGDIPL QGLSGLKRPS SSASTKVDRK
     GGNAHMISSS SVHSRTFHTS NALGPGCKHK KPLSAAKACI SEILPSKFKP RLSAPSALLQ
     EQKSVLLPSE KAQSCENLCV SLNDSKRGLP LRVGGSIENL LMRSRRDYDS KSSSTMSLQE
     YGTSSRRPCP LSRKAGLHFS MFYRDMHQIN RAGLSLGSIS SSSVRDLASH FERSSLTLAR
     GELGASQEGS EHIPKHTVSS RITAFEQLIQ RSRSMPSLDF SGRLSKSPTP VLSRSGLTSA
     RSAESLLEST KLRPREMDGM DSGGVYASPT CSNMADHALS FRSLVPSEPL SICSDELDHC
     SNVSNDSREG SGGSVHGDFP KHRLNKCKGT CPASYTRFTT IRKHEQQSSR QSDWRSDSRG
     DKNSLLRNIH LMSPLPFRLK KPLQQHPRQP PPSDSSESPA GQKADLPCHD PQDQPHSAGK
     PQVPTRLSSR HTMARLSHNS EPPLDRPAGL EDCTRAINNG NPVPYSDHGL DRNNNPQSEL
     AAAHGDSESP RHFIPADYLE STEEFIRRRH DDKEKLLADQ RRLKREQEEA DIAARRHTGV
     IPTHHQFITN ERFGDLLNID DTAKRKSGLE MRPARAKFDF KAQTLKELPL QKGDVVYIYR
     QIDQNWYEGE HHGRVGIFPR TYIELLPPAE KAQPRKLAPV QVLEYGEAIA KFNFNGDTQV
     EMSFRKGERI TLLRQVDENW YEGRIPGTSR QGIFPITYVD VLKRPLVKTP VDYIDLPYSS
     SPSRSATVSP QQPQAQQRRV TPDRSQPSLD LCSYQALYSY VPQNDDELEL RDGDIVDVME
     KCDDGWFVGT SRRTRQFGTF PGNYVKPLYL
//
ID   DBNL_MOUSE              Reviewed;         436 AA.
AC   Q62418; Q3TG34; Q3U5X3; Q3U8I5; Q3UZ33; Q5NCI5; Q5NCI6; Q5NCI7;
AC   Q80WP1; Q8BH56;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   08-FEB-2011, entry version 95.
DE   RecName: Full=Drebrin-like protein;
DE   AltName: Full=Actin-binding protein 1;
DE   AltName: Full=SH3 domain-containing protein 7;
GN   Name=Dbnl; Synonyms=Abp1, Sh3p7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Embryo;
RX   MEDLINE=98294438; PubMed=9630982; DOI=10.1038/nbt0696-741;
RA   Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.;
RT   "Cloning of ligand targets: systematic isolation of SH3 domain-
RT   containing proteins.";
RL   Nat. Biotechnol. 14:741-744(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 79-94 AND
RP   135-144, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF
RP   TYR-340 AND TYR-350, AND PHOSPHORYLATION AT TYR-340 AND TYR-350.
RC   TISSUE=Myeloma;
RX   PubMed=9891087;
RA   Larbolette O., Wollscheid B., Schweikert J., Nielsen P.J.,
RA   Wienands J.;
RT   "SH3P7 is a cytoskeleton adapter protein and is coupled to signal
RT   transduction from lymphocyte antigen receptors.";
RL   Mol. Cell. Biol. 19:1539-1546(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH FGD1.
RC   STRAIN=C57BL/6J; TISSUE=Osteoblast;
RX   PubMed=12913069; DOI=10.1093/hmg/ddg209;
RA   Hou P., Estrada L., Kinley A.W., Parsons J.T., Vojtek A.B.,
RA   Gorski J.L.;
RT   "Fgd1, the Cdc42 GEF responsible for faciogenital dysplasia, directly
RT   interacts with cortactin and mAbp1 to modulate cell shape.";
RL   Hum. Mol. Genet. 12:1981-1993(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Amnion, Bone marrow, Corpora quadrigemina, Eye, Head, Kidney,
RC   Medulla oblongata, Spleen, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   INTERACTION WITH ACTIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=10637315;
RA   Kessels M.M., Engqvist-Goldstein A.E.Y., Drubin D.G.;
RT   "Association of mouse actin-binding protein 1 (mAbp1/SH3P7), an Src
RT   kinase target, with dynamic regions of the cortical actin cytoskeleton
RT   in response to Rac1 activation.";
RL   Mol. Biol. Cell 11:393-412(2000).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277 AND THR-278, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-299, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Actin-binding adapter protein. May act as a common
CC       effector of antigen receptor-signaling pathways in leukocytes. Its
CC       association with dynamin suggests that it may also connect the
CC       actin cytoskeleton to endocytic function. Acts as a key component
CC       of the immunological synapse that regulates T-cell activation by
CC       bridging TCRs and the actin cytoskeleton to gene activation and
CC       endocytic processes. Binds to F-actin but is not involved in actin
CC       polymerization, capping or bundling. Does not bind G-actin.
CC   -!- SUBUNIT: Interacts with SHANK2, SHANK3 and PRAM1 (By similarity).
CC       Interacts with FGD1, dynamin and MAP4K1.
CC   -!- INTERACTION:
CC       P68135:ACTA1 (xeno); NbExp=1; IntAct=EBI-1550322, EBI-367540;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection,
CC       lamellipodium. Cell projection, ruffle. Note=Cortical
CC       cytoskeleton. Associates with lamellipodial actin and membrane
CC       ruffles.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q62418-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q62418-2; Sequence=VSP_050790;
CC       Name=3;
CC         IsoId=Q62418-3; Sequence=VSP_050789;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in brain, thymus and
CC       spleen. Also found in testis, heart and lung. Little or no
CC       expression detected in ovary or muscle.
CC   -!- DEVELOPMENTAL STAGE: In the embryo, expression is high during
CC       early development but drops during later development.
CC   -!- DOMAIN: The SH3 domain mediates interaction with SHANK2, SHANK3
CC       and PRAM1 (By similarity).
CC   -!- SIMILARITY: Belongs to the ABP1 family.
CC   -!- SIMILARITY: Contains 1 ADF-H domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; U58884; AAC52640.1; -; mRNA.
DR   EMBL; AY098595; AAM28340.1; -; mRNA.
DR   EMBL; AK046073; BAC32592.1; -; mRNA.
DR   EMBL; AK053796; BAC35528.1; -; mRNA.
DR   EMBL; AK078082; BAC37118.1; -; mRNA.
DR   EMBL; AK134136; BAE22028.1; -; mRNA.
DR   EMBL; AK134487; BAE22160.1; -; mRNA.
DR   EMBL; AK140752; BAE24466.1; -; mRNA.
DR   EMBL; AK142818; BAE25201.1; -; mRNA.
DR   EMBL; AK146920; BAE27532.1; -; mRNA.
DR   EMBL; AK151096; BAE30108.1; -; mRNA.
DR   EMBL; AK152204; BAE31033.1; -; mRNA.
DR   EMBL; AK153389; BAE31953.1; -; mRNA.
DR   EMBL; AK159984; BAE35535.1; -; mRNA.
DR   EMBL; AK168898; BAE40714.1; -; mRNA.
DR   EMBL; AK172471; BAE43024.1; -; mRNA.
DR   EMBL; AL627069; CAI25434.1; -; Genomic_DNA.
DR   EMBL; AL627069; CAI25435.1; -; Genomic_DNA.
DR   EMBL; AL627069; CAI25436.1; -; Genomic_DNA.
DR   EMBL; BC046430; AAH46430.1; -; mRNA.
DR   IPI; IPI00308222; -.
DR   IPI; IPI00378015; -.
DR   IPI; IPI00458127; -.
DR   RefSeq; NP_001139780.1; NM_001146308.1.
DR   RefSeq; NP_001139781.1; NM_001146309.1.
DR   RefSeq; NP_038838.1; NM_013810.3.
DR   UniGene; Mm.256925; -.
DR   ProteinModelPortal; Q62418; -.
DR   SMR; Q62418; 1-133, 379-434.
DR   IntAct; Q62418; 2.
DR   MINT; MINT-100768; -.
DR   STRING; Q62418; -.
DR   PhosphoSite; Q62418; -.
DR   PRIDE; Q62418; -.
DR   Ensembl; ENSMUST00000020769; ENSMUSP00000020769; ENSMUSG00000020476.
DR   Ensembl; ENSMUST00000102928; ENSMUSP00000099992; ENSMUSG00000020476.
DR   GeneID; 13169; -.
DR   KEGG; mmu:13169; -.
DR   UCSC; uc007hxb.1; mouse.
DR   UCSC; uc007hxc.1; mouse.
DR   UCSC; uc007hxd.1; mouse.
DR   CTD; 13169; -.
DR   MGI; MGI:700006; Dbnl.
DR   eggNOG; roNOG16265; -.
DR   GeneTree; ENSGT00530000062953; -.
DR   HOVERGEN; HBG051316; -.
DR   InParanoid; Q62418; -.
DR   OMA; QRYQEQG; -.
DR   ArrayExpress; Q62418; -.
DR   Bgee; Q62418; -.
DR   CleanEx; MM_DBNL; -.
DR   Genevestigator; Q62418; -.
DR   GermOnline; ENSMUSG00000020476; Mus musculus.
DR   GO; GO:0005938; C:cell cortex; IDA:MGI.
DR   GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR   GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR   GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; IDA:MGI.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0016601; P:Rac protein signal transduction; IDA:MGI.
DR   InterPro; IPR002108; Actin-bd_cofilin/tropomyosin.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00241; Cofilin_ADF; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00102; ADF; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS51263; ADF_H; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Adaptive immunity; Alternative splicing;
KW   Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Endocytosis; Immunity; Phosphoprotein;
KW   SH3 domain.
FT   CHAIN         1    436       Drebrin-like protein.
FT                                /FTId=PRO_0000079794.
FT   DOMAIN        2    133       ADF-H.
FT   DOMAIN      377    436       SH3.
FT   COILED      179    233       Potential.
FT   SITE        367    368       Cleavage; by caspase-3 (By similarity).
FT   MOD_RES     162    162       Phosphotyrosine (By similarity).
FT   MOD_RES     176    176       N6-acetyllysine (By similarity).
FT   MOD_RES     277    277       Phosphoserine.
FT   MOD_RES     278    278       Phosphothreonine.
FT   MOD_RES     280    280       Phosphoserine (By similarity).
FT   MOD_RES     283    283       Phosphoserine (By similarity).
FT   MOD_RES     291    291       Phosphoserine (By similarity).
FT   MOD_RES     296    296       N6-acetyllysine (By similarity).
FT   MOD_RES     299    299       Phosphothreonine.
FT   MOD_RES     340    340       Phosphotyrosine.
FT   MOD_RES     350    350       Phosphotyrosine.
FT   VAR_SEQ     235    238       Missing (in isoform 3).
FT                                /FTId=VSP_050789.
FT   VAR_SEQ     236    238       Missing (in isoform 2).
FT                                /FTId=VSP_050790.
FT   MUTAGEN     340    340       Y->F: Reduces phosphorylation. Abolishes
FT                                phosphorylation; when associated with F-
FT                                350.
FT   MUTAGEN     350    350       Y->F: Reduces phosphorylation. Abolishes
FT                                phosphorylation; when associated with F-
FT                                340.
FT   CONFLICT     30     30       L -> F (in Ref. 4; BAE40714).
FT   CONFLICT    101    101       V -> D (in Ref. 4; BAE31953).
FT   CONFLICT    135    135       A -> V (in Ref. 4; BAE30108/BAE31033).
FT   CONFLICT    327    327       S -> C (in Ref. 4; BAE22028).
SQ   SEQUENCE   436 AA;  48700 MW;  85AEF9781C698A3F CRC64;
     MAVNLSRNGP ALQEAYVRVV TEKSPTDWAL FTYEGNSNDI RVAGTGEGGL EELVEELNSG
     KVMYAFCRVK DPNSGLPKFV LINWTGEGVN DVRKGACANH VSTMANFLKG AHVTINARAE
     EDVEPECIME KVAKASGANY SFHKESTSFQ DVGPQAPVGS VYQKTNAISE IKRVGKDNFW
     AKAEKEEENR RLEEKRRAEE ERQRLEEERR ERELQEAARR EQRYQEQHRS AGAPSPSSRT
     GEPEQEAVSR TRQEWESAGQ QAPHPREIFK QKERAMSTTS VTSSQPGKLR SPFLQKQLTQ
     PETSYGREPT APVSRPAAGV CEEPAPSTLS SAQTEEEPTY EVPPEQDTLY EEPPLVQQQG
     AGSEHIDNYM QSQGFSGQGL CARALYDYQA ADDTEISFDP ENLITGIEVI DEGWWRGYGP
     DGHFGMFPAN YVELIE
//
ID   SH3G3_MOUSE             Reviewed;         347 AA.
AC   Q62421; Q8R0B7;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Endophilin-A3;
DE   AltName: Full=Endophilin-3;
DE   AltName: Full=SH3 domain protein 2C;
DE   AltName: Full=SH3 domain-containing GRB2-like protein 3;
DE   AltName: Full=SH3p13;
GN   Name=Sh3gl3; Synonyms=Sh3d2c, Sh3d2c2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RX   MEDLINE=98294438; PubMed=9630982; DOI=10.1038/nbt0696-741;
RA   Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.;
RT   "Cloning of ligand targets: systematic isolation of SH3 domain-
RT   containing proteins.";
RL   Nat. Biotechnol. 14:741-744(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Implicated in endocytosis. May recruit other proteins to
CC       membranes with high curvature (By similarity).
CC   -!- SUBUNIT: Interacts with ARC, DNM1, SGIP1, SYNJ1 and DYDC1.
CC       Interacts with FASLG (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Early endosome
CC       membrane; Peripheral membrane protein (By similarity).
CC       Note=Associated with postsynaptic endosomes in hippocampal
CC       neurons. Associated with presynaptic endosomes in olfactory
CC       neurons (By similarity).
CC   -!- DOMAIN: An N-terminal amphipathic helix, the BAR domain and a
CC       second amphipathic helix inserted into helix 1 of the BAR domain
CC       (N-BAR domain) induce membrane curvature and bind curved membranes
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the endophilin family.
CC   -!- SIMILARITY: Contains 1 BAR domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; U58887; AAC72268.1; -; mRNA.
DR   EMBL; BC027096; AAH27096.1; -; mRNA.
DR   IPI; IPI00312771; -.
DR   RefSeq; NP_059096.3; NM_017400.4.
DR   UniGene; Mm.432002; -.
DR   UniGene; Mm.736; -.
DR   ProteinModelPortal; Q62421; -.
DR   SMR; Q62421; 30-252, 286-344.
DR   MINT; MINT-238811; -.
DR   STRING; Q62421; -.
DR   PRIDE; Q62421; -.
DR   Ensembl; ENSMUST00000032874; ENSMUSP00000032874; ENSMUSG00000030638.
DR   GeneID; 20408; -.
DR   KEGG; mmu:20408; -.
DR   CTD; 20408; -.
DR   MGI; MGI:700011; Sh3gl3.
DR   HOGENOM; HBG447412; -.
DR   HOVERGEN; HBG052866; -.
DR   InParanoid; Q62421; -.
DR   OrthoDB; EOG4C2H9V; -.
DR   ArrayExpress; Q62421; -.
DR   Bgee; Q62421; -.
DR   CleanEx; MM_SH3GL3; -.
DR   Genevestigator; Q62421; -.
DR   GermOnline; ENSMUSG00000030638; Mus musculus.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   InterPro; IPR004148; BAR.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF03114; BAR; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00721; BAR; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS51021; BAR; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Endocytosis; Endosome; Lipid-binding;
KW   Membrane; SH3 domain.
FT   CHAIN         1    347       Endophilin-A3.
FT                                /FTId=PRO_0000146751.
FT   DOMAIN       18    249       BAR.
FT   DOMAIN      285    344       SH3.
FT   REGION        1     21       Membrane-binding amphipathic helix (By
FT                                similarity).
FT   REGION       60     87       Required for dimerization upon membrane
FT                                association (By similarity).
FT   REGION      218    254       Interaction with ARC (By similarity).
FT   COILED      180    201       Potential.
FT   COMPBIAS    273    276       Poly-Ser.
FT   CONFLICT    285    285       A -> S (in Ref. 2; AAH27096).
SQ   SEQUENCE   347 AA;  38934 MW;  A2174642F853B5EB CRC64;
     MSVAGLKKQF HKASQLFSEK ISGAEGTKLD EEFLNMEKKI DITSKAVAEI LSKATEYLQP
     NPAYRAKLGM LNTVSKLRGQ VKATGYPQTE GLLGDCMLKY GKELGEDSAF GNSLVDVGEA
     LKLMAEVKDS LDINVKQTFI DPLQLLQDKD LKEIGHHLRK LEGRRLDYDY KKRRVGKIPE
     EEIRQAVEKF EESKELAERS MFNFLENDVE QVSQLAVFVE AALDYHRQST EILQELQSKL
     ELRISLASKV PKREFMPKPV NMSSTDANGV GPSSSSKTPG TDTPADQPCC RGLYDFEPEN
     EGELGFKEGD IITLTNQIDE NWYEGMLRGE SGFFPINYVE VIVPLPP
//
ID   OSTF1_MOUSE             Reviewed;         215 AA.
AC   Q62422; Q3UF05;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Osteoclast-stimulating factor 1;
DE   AltName: Full=SH3 domain protein 3;
GN   Name=Ostf1; Synonyms=Sh3d3, Sh3p2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=97381295; PubMed=9238627; DOI=10.1007/BF01718694;
RA   Hoffman N.G., Sparks A.B., Carter J.M., Kay B.K.;
RT   "Binding properties of SH3 peptide ligands identified from phage-
RT   displayed random peptide libraries.";
RL   Mol. Divers. 2:5-12(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RX   MEDLINE=98294438; PubMed=9630982; DOI=10.1038/nbt0696-741;
RA   Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.;
RT   "Cloning of ligand targets: systematic isolation of SH3 domain-
RT   containing proteins.";
RL   Nat. Biotechnol. 14:741-744(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Kidney, Placenta, Small intestine,
RC   Sympathetic ganglion, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart, and Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203 AND SER-214, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Induces bone resorption, acting probably through a
CC       signaling cascade which results in the secretion of factor(s)
CC       enhancing osteoclast formation and activity (By similarity).
CC   -!- SUBUNIT: Interacts with C-SRC and SMN1. Interacts with FASLG (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- DOMAIN: The SH3 domain mediates interaction with SMN1 (By
CC       similarity).
CC   -!- SIMILARITY: Contains 3 ANK repeats.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC52641.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U58888; AAC52641.1; ALT_INIT; mRNA.
DR   EMBL; AK002899; BAB22442.1; -; mRNA.
DR   EMBL; AK005525; BAB24098.1; -; mRNA.
DR   EMBL; AK008123; BAB25477.1; -; mRNA.
DR   EMBL; AK008467; BAB25685.1; -; mRNA.
DR   EMBL; AK010074; BAB26683.1; -; mRNA.
DR   EMBL; AK145949; BAE26777.1; -; mRNA.
DR   EMBL; AK149175; BAE28756.1; -; mRNA.
DR   EMBL; AK150145; BAE29340.1; -; mRNA.
DR   EMBL; AK155028; BAE33000.1; -; mRNA.
DR   EMBL; BC060986; AAH60986.1; -; mRNA.
DR   IPI; IPI00125923; -.
DR   RefSeq; NP_059071.1; NM_017375.3.
DR   UniGene; Mm.172222; -.
DR   ProteinModelPortal; Q62422; -.
DR   SMR; Q62422; 12-193.
DR   STRING; Q62422; -.
DR   PhosphoSite; Q62422; -.
DR   UCD-2DPAGE; Q62422; -.
DR   PRIDE; Q62422; -.
DR   Ensembl; ENSMUST00000025631; ENSMUSP00000025631; ENSMUSG00000024725.
DR   GeneID; 20409; -.
DR   KEGG; mmu:20409; -.
DR   UCSC; uc008gxs.1; mouse.
DR   CTD; 20409; -.
DR   MGI; MGI:700012; Ostf1.
DR   eggNOG; roNOG09147; -.
DR   GeneTree; ENSGT00530000063487; -.
DR   HOGENOM; HBG377860; -.
DR   HOVERGEN; HBG053379; -.
DR   InParanoid; Q62422; -.
DR   OMA; HGGHKDV; -.
DR   OrthoDB; EOG4Z62PH; -.
DR   PhylomeDB; Q62422; -.
DR   NextBio; 298388; -.
DR   ArrayExpress; Q62422; -.
DR   Bgee; Q62422; -.
DR   CleanEx; MM_OSTF1; -.
DR   Genevestigator; Q62422; -.
DR   GermOnline; ENSMUSG00000024725; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0017124; F:SH3 domain binding; IDA:MGI.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR000108; p67phox.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00499; P67PHOX.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Cytoplasm; Phosphoprotein; Repeat; SH3 domain.
FT   CHAIN         1    215       Osteoclast-stimulating factor 1.
FT                                /FTId=PRO_0000067036.
FT   DOMAIN       12     71       SH3.
FT   REPEAT       72    101       ANK 1.
FT   REPEAT      105    135       ANK 2.
FT   REPEAT      139    168       ANK 3.
FT   COMPBIAS      4     11       Pro-rich.
FT   MOD_RES     201    201       Phosphothreonine (By similarity).
FT   MOD_RES     203    203       Phosphoserine.
FT   MOD_RES     214    214       Phosphoserine.
SQ   SEQUENCE   215 AA;  23783 MW;  DAB682C371929B8A CRC64;
     MSKPPPKPVK PGQVKVFRAL YTFEPRTPDE LYFEEGDIIY ITDMSDTSWW KGTCKGRTGL
     IPSNYVAEQA ESIDNPLHEA AKRGNLSWLR ECLDNRVGVN GLDKAGSTAL YWACHGGHKD
     IVEVLFTQPN VELNQQNKLG DTALHAAAWK GYADIVQLLL AKGARTDLRN NEKKLALDMA
     TNAACASLLK KKQQGTDGAR TLSNAEDYLD DEDSD
//
ID   NDUA4_MOUSE             Reviewed;          82 AA.
AC   Q62425; Q9CQP6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2002, sequence version 2.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 4;
DE   AltName: Full=Complex I-MLRQ;
DE            Short=CI-MLRQ;
DE   AltName: Full=NADH-ubiquinone oxidoreductase MLRQ subunit;
GN   Name=Ndufa4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Small intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-82, AND PROTEIN SEQUENCE OF 61-68.
RC   STRAIN=C57BL/6;
RX   MEDLINE=97188917; PubMed=9064319; DOI=10.1084/jem.184.3.1017;
RA   Tallquist M.D., Yun T.J., Pease L.R.;
RT   "A single T cell receptor recognizes structurally distinct MHC/peptide
RT   complexes with high specificity.";
RL   J. Exp. Med. 184:1017-1026(1996).
RN   [4]
RP   PROTEIN SEQUENCE OF 36-74, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 61-68 IN COMPLEX WITH THE
RP   MAJOR HISTOCOMPATIBILITY COMPLEX.
RX   PubMed=11994422; DOI=10.1084/jem.20011644;
RA   Luz J.G., Huang M., Garcia K.C., Rudolph M.G., Apostolopoulos V.,
RA   Teyton L., Wilson I.A.;
RT   "Structural comparison of allogeneic and syngeneic T cell receptor-
RT   peptide-major histocompatibility complex complexes: a buried
RT   alloreactive mutation subtly alters peptide presentation substantially
RT   increasing V(beta) interactions.";
RL   J. Exp. Med. 195:1175-1186(2002).
CC   -!- FUNCTION: Accessory subunit of the mitochondrial membrane
CC       respiratory chain NADH dehydrogenase (Complex I), that is believed
CC       to be not involved in catalysis. Complex I functions in the
CC       transfer of electrons from NADH to the respiratory chain. The
CC       immediate electron acceptor for the enzyme is believed to be
CC       ubiquinone (By similarity).
CC   -!- SUBUNIT: Mammalian complex I is composed of 45 different subunits
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein; Matrix side (By similarity).
CC   -!- SIMILARITY: Belongs to the complex I NDUFA4 subunit family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK005084; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK008357; BAB25627.1; -; mRNA.
DR   EMBL; AK008506; BAB25706.1; -; mRNA.
DR   EMBL; AK076036; BAC36137.1; -; mRNA.
DR   EMBL; BC011114; AAH11114.1; -; mRNA.
DR   EMBL; U59509; AAB03395.1; -; mRNA.
DR   IPI; IPI00125929; -.
DR   RefSeq; NP_035016.1; NM_010886.2.
DR   UniGene; Mm.415865; -.
DR   UniGene; Mm.479528; -.
DR   PDB; 1LEG; X-ray; 1.75 A; P=61-68.
DR   PDBsum; 1LEG; -.
DR   STRING; Q62425; -.
DR   PhosphoSite; Q62425; -.
DR   PRIDE; Q62425; -.
DR   Ensembl; ENSMUST00000031637; ENSMUSP00000031637; ENSMUSG00000029632.
DR   GeneID; 17992; -.
DR   KEGG; mmu:17992; -.
DR   UCSC; uc009ayd.1; mouse.
DR   CTD; 17992; -.
DR   MGI; MGI:107686; Ndufa4.
DR   eggNOG; roNOG17426; -.
DR   GeneTree; ENSGT00390000010457; -.
DR   HOGENOM; HBG738659; -.
DR   HOVERGEN; HBG006548; -.
DR   InParanoid; Q62425; -.
DR   OMA; YKFFAVN; -.
DR   OrthoDB; EOG4TF0MX; -.
DR   PhylomeDB; Q62425; -.
DR   NextBio; 292971; -.
DR   ArrayExpress; Q62425; -.
DR   Bgee; Q62425; -.
DR   Genevestigator; Q62425; -.
DR   GermOnline; ENSMUSG00000029632; Mus musculus.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR019550; NADH_Ub_cplx-1_asub_su-4.
DR   Pfam; PF10526; NADH_ub_rd_NUML; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing;
KW   Electron transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Respiratory chain; Transport.
FT   CHAIN         1     82       NADH dehydrogenase [ubiquinone] 1 alpha
FT                                subcomplex subunit 4.
FT                                /FTId=PRO_0000118822.
FT   MOD_RES      56     56       N6-acetyllysine.
SQ   SEQUENCE   82 AA;  9327 MW;  6E29865845807C7B CRC64;
     MLRQILGQAK KHPSLIPLFV FIGAGGTGAA LYVMRLALFN PDVSWDRKNN PEPWNKLGPN
     EQYKFYSVNV DYSKLKKEGP DF
//
ID   NDRG1_MOUSE             Reviewed;         394 AA.
AC   Q62433; P97862;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Protein NDRG1;
DE   AltName: Full=N-myc downstream-regulated gene 1 protein;
DE            Short=Protein Ndr1;
GN   Name=Ndrg1; Synonyms=Ndr1, Ndrl, Tdd5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99310663; PubMed=10381566; DOI=10.1016/S0925-4773(99)00025-8;
RA   Shimono A., Okuda T., Kondoh H.;
RT   "N-myc-dependent repression of ndr1, a gene identified by direct
RT   subtraction of whole mouse embryo cDNAs between wild type and N-myc
RT   mutant.";
RL   Mech. Dev. 83:39-52(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Hybridoma;
RX   MEDLINE=97289706; PubMed=9144177; DOI=10.1073/pnas.94.10.4988;
RA   Lin T.-M., Chang C.;
RT   "Cloning and characterization of TDD5, an androgen target gene that is
RT   differentially repressed by testosterone and dihydrotestosterone.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:4988-4993(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-328; SER-330; THR-335
RP   AND SER-336, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-346 AND SER-362,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May have a growth inhibitory role (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Expressed most abundantly in kidney followed
CC       by nervous tissues (hypothalamus, cerebellum, and cerebrum) and
CC       preputial gland, and in much smaller quantities in other tissues,
CC       except duodenum and prostate.
CC   -!- DEVELOPMENTAL STAGE: Its expression increases after 13.5 dpc when
CC       n-Myc expression is largely down-regulated.
CC   -!- INDUCTION: Repressed by testosterone and also to a lesser extent
CC       by dihydrotestosterone.
CC   -!- SIMILARITY: Belongs to the NDRG family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U60593; AAB03484.1; -; mRNA.
DR   EMBL; U52073; AAB58249.1; -; mRNA.
DR   EMBL; BC015282; AAH15282.1; -; mRNA.
DR   EMBL; BC071235; AAH71235.1; -; mRNA.
DR   IPI; IPI00125960; -.
DR   RefSeq; NP_032707.2; NM_008681.2.
DR   UniGene; Mm.30837; -.
DR   ProteinModelPortal; Q62433; -.
DR   SMR; Q62433; 33-311.
DR   STRING; Q62433; -.
DR   MEROPS; S33.987; -.
DR   PhosphoSite; Q62433; -.
DR   PRIDE; Q62433; -.
DR   Ensembl; ENSMUST00000005256; ENSMUSP00000005256; ENSMUSG00000005125.
DR   GeneID; 17988; -.
DR   KEGG; mmu:17988; -.
DR   UCSC; uc007wax.1; mouse.
DR   CTD; 17988; -.
DR   MGI; MGI:1341799; Ndrg1.
DR   eggNOG; roNOG13272; -.
DR   GeneTree; ENSGT00390000001874; -.
DR   HOGENOM; HBG445737; -.
DR   HOVERGEN; HBG052591; -.
DR   InParanoid; Q62433; -.
DR   OMA; QEFDVQE; -.
DR   OrthoDB; EOG4QC15K; -.
DR   NextBio; 292963; -.
DR   ArrayExpress; Q62433; -.
DR   Bgee; Q62433; -.
DR   CleanEx; MM_NDRG1; -.
DR   Genevestigator; Q62433; -.
DR   GermOnline; ENSMUSG00000005125; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0045576; P:mast cell activation; IDA:MGI.
DR   InterPro; IPR004142; Ndr.
DR   PANTHER; PTHR11034; Ndr; 1.
DR   Pfam; PF03096; Ndr; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Phosphoprotein; Repeat.
FT   CHAIN         1    394       Protein NDRG1.
FT                                /FTId=PRO_0000159574.
FT   REPEAT      339    348       1.
FT   REPEAT      349    358       2.
FT   REPEAT      359    368       3.
FT   REGION      339    368       3 X 10 AA tandem repeats of G-[PST]-R-S-
FT                                R-S-H-T-S-E.
FT   MOD_RES       2      2       Phosphoserine.
FT   MOD_RES     319    319       Phosphoserine (By similarity).
FT   MOD_RES     326    326       Phosphoserine (By similarity).
FT   MOD_RES     328    328       Phosphothreonine.
FT   MOD_RES     330    330       Phosphoserine.
FT   MOD_RES     332    332       Phosphoserine (By similarity).
FT   MOD_RES     333    333       Phosphoserine (By similarity).
FT   MOD_RES     335    335       Phosphothreonine.
FT   MOD_RES     336    336       Phosphoserine.
FT   MOD_RES     346    346       Phosphothreonine.
FT   MOD_RES     362    362       Phosphoserine.
FT   MOD_RES     364    364       Phosphoserine (By similarity).
FT   MOD_RES     366    366       Phosphothreonine (By similarity).
FT   MOD_RES     375    375       Phosphothreonine (By similarity).
FT   CONFLICT     33     35       QEQ -> LEE (in Ref. 2; AAB58249).
FT   CONFLICT     89     89       F -> P (in Ref. 2; AAB58249).
FT   CONFLICT    103    109       APSFPVG -> PLPSQW (in Ref. 2; AAB58249).
FT   CONFLICT    141    148       AGAYILTR -> PWXLHPDP (in Ref. 2).
FT   CONFLICT    191    208       VVSHLFGKEEIHNNVEVV -> CVPPLRXGGDTQQRGGM
FT                                (in Ref. 2; AAB58249).
FT   CONFLICT    241    241       R -> A (in Ref. 2; AAB58249).
FT   CONFLICT    298    350       PAKLAEAFKYFVQGMGYMPSASMTRLMRSRTASGSSVTSLE
FT                                GTRSRSHTSEGP -> RPSLLRPSSTLCRHGIHAFCQHDSP
FT                                DRVPHPVWLQCHILEGT (in Ref. 2; AAB58249).
SQ   SEQUENCE   394 AA;  43009 MW;  905CA71ECF4C87C2 CRC64;
     MSRELHDVDL AEVKPLVEKG ESITGLLQEF DVQEQDIETL HGSLHVTLCG TPKGNRPVIL
     TYHDIGMNHK TCYNPLFNSE DMQEITQHFA VCHVDAPGQQ DGAPSFPVGY MYPSMDQLAE
     MLPGVLHQFG LKSVIGMGTG AGAYILTRFA LNNPEMVEGL VLMNVNPCAE GWMDWAASKI
     SGWTQALPDM VVSHLFGKEE IHNNVEVVHT YRQHILNDMN PSNLHLFISA YNSRRDLEIE
     RPMPGTHTVT LQCPALLVVG DNSPAVDAVV ECNSKLDPTK TTLLKMADCG GLPQISQPAK
     LAEAFKYFVQ GMGYMPSASM TRLMRSRTAS GSSVTSLEGT RSRSHTSEGP RSRSHTSEGS
     RSRSHTSEDA RLNITPNSGA TGNNAGPKSM EVSC
//
ID   VAMP1_MOUSE             Reviewed;         118 AA.
AC   Q62442; Q6PFF3; Q810K6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Vesicle-associated membrane protein 1;
DE            Short=VAMP-1;
DE   AltName: Full=Synaptobrevin-1;
GN   Name=Vamp1; Synonyms=Syb1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Martin S., Tellam J.T., Livington C., Slot J.W., Gould G.W.,
RA   James D.E.;
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Brain;
RA   Olken S.K., Doerre S., Corley R.B.;
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 34-49; 50-58 AND 62-85, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15648052; DOI=10.1002/pmic.200401066;
RA   Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA   Hart G.W., Burlingame A.L.;
RT   "Quantitative analysis of both protein expression and serine /
RT   threonine post-translational modifications through stable isotope
RT   labeling with dithiothreitol.";
RL   Proteomics 5:388-398(2005).
CC   -!- FUNCTION: Involved in the targeting and/or fusion of transport
CC       vesicles to their target membrane.
CC   -!- SUBUNIT: Interacts with VAPA and VAPB (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasmic vesicle, secretory
CC       vesicle, synaptic vesicle membrane; Single-pass type IV membrane
CC       protein (By similarity). Cell junction, synapse, synaptosome (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasmic vesicle membrane;
CC       Single-pass type IV membrane protein (By similarity). Cell
CC       junction, synapse, synaptosome (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q62442-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q62442-2; Sequence=VSP_029186;
CC   -!- SIMILARITY: Belongs to the synaptobrevin family.
CC   -!- SIMILARITY: Contains 1 v-SNARE coiled-coil homology domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; U61751; AAB03491.1; -; mRNA.
DR   EMBL; AF007167; AAB62930.1; -; mRNA.
DR   EMBL; AK018783; BAB31407.1; -; mRNA.
DR   EMBL; AK078156; BAC37151.1; -; mRNA.
DR   EMBL; BC049902; AAH49902.2; -; mRNA.
DR   EMBL; BC057587; AAH57587.1; -; mRNA.
DR   IPI; IPI00125990; -.
DR   IPI; IPI00761439; -.
DR   RefSeq; NP_001074026.1; NM_001080557.1.
DR   RefSeq; NP_033522.1; NM_009496.3.
DR   UniGene; Mm.32321; -.
DR   ProteinModelPortal; Q62442; -.
DR   SMR; Q62442; 30-94.
DR   STRING; Q62442; -.
DR   PhosphoSite; Q62442; -.
DR   PRIDE; Q62442; -.
DR   Ensembl; ENSMUST00000032487; ENSMUSP00000032487; ENSMUSG00000030337.
DR   GeneID; 22317; -.
DR   KEGG; mmu:22317; -.
DR   UCSC; uc009dtx.1; mouse.
DR   CTD; 22317; -.
DR   MGI; MGI:1313276; Vamp1.
DR   eggNOG; roNOG17295; -.
DR   GeneTree; ENSGT00550000074449; -.
DR   HOVERGEN; HBG006675; -.
DR   OrthoDB; EOG43JC6B; -.
DR   PhylomeDB; Q62442; -.
DR   NextBio; 302523; -.
DR   ArrayExpress; Q62442; -.
DR   Bgee; Q62442; -.
DR   CleanEx; MM_VAMP1; -.
DR   Genevestigator; Q62442; -.
DR   GermOnline; ENSMUSG00000030337; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019717; C:synaptosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR001388; Synaptobrevin.
DR   InterPro; IPR016444; Synaptobrevin_met/fun.
DR   Pfam; PF00957; Synaptobrevin; 1.
DR   PIRSF; PIRSF005409; Synaptobrevin_euk; 1.
DR   PRINTS; PR00219; SYNAPTOBREVN.
DR   PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR   PROSITE; PS50892; V_SNARE; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Coiled coil; Cytoplasmic vesicle;
KW   Direct protein sequencing; Membrane; Phosphoprotein; Synapse;
KW   Synaptosome; Transmembrane; Transmembrane helix.
FT   CHAIN         1    118       Vesicle-associated membrane protein 1.
FT                                /FTId=PRO_0000206720.
FT   TOPO_DOM      1     96       Cytoplasmic (Potential).
FT   TRANSMEM     97    116       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   TOPO_DOM    117    118       Vesicular (Potential).
FT   DOMAIN       33     93       v-SNARE coiled-coil homology.
FT   MOD_RES      63     63       Phosphoserine.
FT   VAR_SEQ     114    118       IYFFT -> SKYR (in isoform 2).
FT                                /FTId=VSP_029186.
SQ   SEQUENCE   118 AA;  12890 MW;  31CB8701446A7FB0 CRC64;
     MSAPAQPPAE GTEGAAPGGG PPGPPPNMTS NRRLQQTQAQ VEEVVDIMRV NVDKVLERDQ
     KLSELDDRAD ALQAGASQFE SSAAKLKRKY WWKNCKMMIM LGAICAIIVV VIVIYFFT
//
ID   IF4G2_MOUSE             Reviewed;         906 AA.
AC   Q62448; P97867; Q0VGZ3; Q3UNC1; Q5XKD8; Q6P1Z0; Q921U3;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-APR-2003, sequence version 2.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Eukaryotic translation initiation factor 4 gamma 2;
DE            Short=eIF-4-gamma 2;
DE            Short=eIF-4G 2;
DE            Short=eIF4G 2;
DE   AltName: Full=Novel APOBEC-1 target 1;
DE   AltName: Full=Translation repressor NAT1;
DE   AltName: Full=p97;
GN   Name=Eif4g2; Synonyms=Nat1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX   MEDLINE=97182546; PubMed=9030685;
RA   Yamanaka S., Poksay K.S., Arnold K.S., Innerarity T.L.;
RT   "A novel translational repressor mRNA is edited extensively in livers
RT   containing tumors caused by the transgene expression of the apoB mRNA-
RT   editing enzyme.";
RL   Genes Dev. 11:321-333(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=97179220; PubMed=9027506; DOI=10.1006/geno.1996.4502;
RA   Shaughnessy J.D. Jr., Jenkins N.A., Copeland N.G.;
RT   "cDNA cloning, expression analysis, and chromosomal localization of a
RT   gene with high homology to wheat eIF-(iso)4F and mammalian eIF-4G.";
RL   Genomics 39:192-197(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and Czech II;
RC   TISSUE=Embryonic brain, Eye, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-507, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-901, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Appears to play a role in the switch from cap-dependent
CC       to IRES-mediated translation during mitosis, apoptosis and viral
CC       infection. Cleaved by some caspases and viral proteases.
CC   -!- SUBUNIT: Interacts with the serine/threonine protein kinases MKNK1
CC       and MKNK2. Binds EIF4A and EIF3. Interacts with MIF4GD (By
CC       similarity).
CC   -!- INTERACTION:
CC       Q61823:Pdcd4; NbExp=1; IntAct=EBI-296494, EBI-296473;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q62448-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q62448-2; Sequence=VSP_021640;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues
CC       examined.
CC   -!- PTM: Phosphorylation; hyperphosphorylated during mitosis (By
CC       similarity).
CC   -!- MISCELLANEOUS: This gene has been shown to be extensively edited
CC       in the liver of APOBEC1 transgenic animals. Its aberrant editing
CC       could contribute to the potent oncogenesis induced by
CC       overexpression of APOBEC1. The aberrant edited sequence, called
CC       NAT1, is likely to be a fundamental translational repressor.
CC   -!- SIMILARITY: Belongs to the eIF4G family.
CC   -!- SIMILARITY: Contains 1 MI domain.
CC   -!- SIMILARITY: Contains 1 MIF4G domain.
CC   -!- SIMILARITY: Contains 1 W2 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE25826.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U76112; AAC53095.1; -; mRNA.
DR   EMBL; U63323; AAC53030.1; -; mRNA.
DR   EMBL; AK144309; BAE25826.1; ALT_INIT; mRNA.
DR   EMBL; BC040391; AAH40391.2; -; mRNA.
DR   EMBL; BC043034; AAH43034.2; -; mRNA.
DR   EMBL; BC056387; AAH56387.1; -; mRNA.
DR   EMBL; BC057673; AAH57673.2; -; mRNA.
DR   EMBL; BC064810; AAH64810.2; -; mRNA.
DR   EMBL; BC092521; AAH92521.1; -; mRNA.
DR   IPI; IPI00126006; -.
DR   IPI; IPI00776162; -.
DR   RefSeq; NP_001035221.1; NM_001040131.2.
DR   RefSeq; NP_038535.2; NM_013507.3.
DR   UniGene; Mm.185453; -.
DR   ProteinModelPortal; Q62448; -.
DR   SMR; Q62448; 70-311, 539-896.
DR   IntAct; Q62448; 6.
DR   STRING; Q62448; -.
DR   PhosphoSite; Q62448; -.
DR   PRIDE; Q62448; -.
DR   Ensembl; ENSMUST00000005750; ENSMUSP00000005750; ENSMUSG00000005610.
DR   Ensembl; ENSMUST00000106666; ENSMUSP00000102277; ENSMUSG00000005610.
DR   GeneID; 13690; -.
DR   KEGG; mmu:13690; -.
DR   UCSC; uc009jfz.1; mouse.
DR   CTD; 13690; -.
DR   MGI; MGI:109207; Eif4g2.
DR   GeneTree; ENSGT00530000063038; -.
DR   HOVERGEN; HBG052084; -.
DR   InParanoid; Q62448; -.
DR   OrthoDB; EOG4SBDXB; -.
DR   NextBio; 284458; -.
DR   ArrayExpress; Q62448; -.
DR   Bgee; Q62448; -.
DR   Genevestigator; Q62448; -.
DR   GermOnline; ENSMUSG00000005610; Mus musculus.
DR   GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
DR   GO; GO:0006446; P:regulation of translational initiation; IDA:UniProtKB.
DR   GO; GO:0016070; P:RNA metabolic process; IEA:InterPro.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003307; eIF5C.
DR   InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR   InterPro; IPR016021; MIF4-like_typ_1/2/3.
DR   InterPro; IPR003890; MIF4G-like_typ-3.
DR   Gene3D; G3DSA:1.25.40.180; MIF4-like_typ_1/2/3; 2.
DR   Pfam; PF02847; MA3; 1.
DR   Pfam; PF02854; MIF4G; 1.
DR   Pfam; PF02020; W2; 1.
DR   SMART; SM00515; eIF5C; 1.
DR   SMART; SM00544; MA3; 1.
DR   SMART; SM00543; MIF4G; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 3.
DR   PROSITE; PS51366; MI; 1.
DR   PROSITE; PS51363; W2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Initiation factor; Phosphoprotein;
KW   Protein biosynthesis; Repressor; Translation regulation.
FT   CHAIN         1    906       Eukaryotic translation initiation factor
FT                                4 gamma 2.
FT                                /FTId=PRO_0000213326.
FT   DOMAIN       78    308       MIF4G.
FT   DOMAIN      542    665       MI.
FT   DOMAIN      719    903       W2.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     394    394       Phosphoserine (By similarity).
FT   MOD_RES     507    507       Phosphothreonine.
FT   MOD_RES     513    513       Phosphothreonine (By similarity).
FT   MOD_RES     901    901       Phosphoserine.
FT   VAR_SEQ     433    470       Missing (in isoform 2).
FT                                /FTId=VSP_021640.
FT   CONFLICT      1      1       M -> V (in Ref. 3; BAE25826).
FT   CONFLICT     14     14       S -> T (in Ref. 2; AAC53030).
FT   CONFLICT    236    236       L -> G (in Ref. 2; AAC53030).
FT   CONFLICT    245    245       K -> Q (in Ref. 1; AAC53095).
FT   CONFLICT    346    347       RS -> MSR (in Ref. 2; AAC53030).
FT   CONFLICT    347    347       S -> N (in Ref. 3; BAE25826 and 4;
FT                                AAH40391/AAH43034/AAH56387/AAH57673/
FT                                AAH64810/AAH92521).
FT   CONFLICT    355    355       F -> L (in Ref. 2; AAC53030).
FT   CONFLICT    394    394       S -> P (in Ref. 2; AAC53030).
FT   CONFLICT    437    437       L -> F (in Ref. 2; AAC53030).
FT   CONFLICT    472    472       S -> R (in Ref. 2; AAC53030).
FT   CONFLICT    476    476       A -> D (in Ref. 2; AAC53030).
FT   CONFLICT    488    488       K -> M (in Ref. 2; AAC53030).
FT   CONFLICT    550    550       V -> G (in Ref. 2; AAC53030).
FT   CONFLICT    708    708       D -> N (in Ref. 2; AAC53030).
FT   CONFLICT    753    753       I -> S (in Ref. 2; AAC53030).
FT   CONFLICT    760    760       K -> T (in Ref. 2; AAC53030).
FT   CONFLICT    784    784       S -> N (in Ref. 2; AAC53030).
FT   CONFLICT    797    798       SK -> PT (in Ref. 2; AAC53030).
FT   CONFLICT    825    825       L -> V (in Ref. 2; AAC53030).
FT   CONFLICT    833    833       L -> F (in Ref. 1; AAC53095).
FT   CONFLICT    844    844       K -> Q (in Ref. 2; AAC53030).
SQ   SEQUENCE   906 AA;  102106 MW;  EA73E717671562E4 CRC64;
     MESAIAEGGA SRFSASSGGG GSRGAPQHYP KTAGNSEFLG KTPGQNAQKW IPARSTRRDD
     NSAANNSANE KERHDAIFRK VRGILNKLTP EKFDKLCLEL LNVGVESKLI LKGVILLIVD
     KALEEPKYSS LYAQLCLRLA EDAPNFDGPA AEGQPGQKQS TTFRRLLISK LQDEFENRTR
     NVDVYDKREN PLLPEEEEQR AIAKIKMLGN IKFIGELGKL DLIHESILHK CIKTLLEKKK
     RVQLKDMGED LECLCQIMRT VGPRLDHERA KSLMDQYFAR MCSLMLSKEL PARIRFLLQD
     TVELREHHWV PRKAFLDNGP KTINQIRQDA VKDLGVFIPA PMAQGRSDFF LEGPFMPPRM
     KMDRDPLGGL ADMFGQMPGS GIGTGPGVIQ DRFSPTMGRH RSNQLFNGHG GHIMPPTQSQ
     FGEMGGKFMK SQGLSQLYHN QSQGLLSQLQ GQSKDMPPRF SKKGQLNADE ISLRPAQSFL
     MNKNQVPKLQ PQITMIPPSA QPPRTQTPPL GQTPQLGLKT NPPLIQEKPA KTSKKPPPSK
     EELLKLTEAV VTDYLNSGNA NDAVSGVREM RAPKHFLPEM LSKVIILSLD RSDEDKEKAS
     SLISLLKQEG IATSDNFMQA FLNVLEQCPK LEVDIPLVKS YLAQFAARAI ISELVSISEL
     AQPLESGTHF PLFLLCLQQL AKLQDREWLT ELFQQSKVNM QKMLPEIDQN KDRMLEILEG
     KGLSFLFPLL KLEKELLKQI KLDPSPQTIY KWIKDNISPK LHVDKGFVNI LMTSFLQYIS
     SEVSPPSDET DSSSAPSKEQ LEQEKQLLLS FKPVMQKFLH DHVDLQVSAL YALQVHCYNS
     SFPKGMLLRF FVHFYDMEII EEEAFLAWKE DITQEFPGKG KALFQVNQWL TWLETAEEEE
     SEEEAD
//
ID   VAT1_MOUSE              Reviewed;         406 AA.
AC   Q62465; Q8R3G0; Q8R3T8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 3.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Synaptic vesicle membrane protein VAT-1 homolog;
DE            EC=1.-.-.-;
GN   Name=Vat1; Synonyms=Vat-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 105-209, PROTEIN SEQUENCE OF 239-258;
RP   264-308; 369-378; 386-390 AND 396-404, AND FUNCTION.
RX   MEDLINE=98241025; PubMed=9581869;
RX   DOI=10.1002/(SICI)1097-4644(19980601)69:3<304::AID-JCB8>3.3.CO;2-U;
RA   Hayess K., Kraft R., Sachsinger J., Janke J., Beckmann G., Rohde K.,
RA   Jandrig B., Benndorf R.;
RT   "Mammalian protein homologous to VAT-1 of Torpedo californica:
RT   isolation from Ehrlich ascites tumor cells, biochemical
RT   characterization, and organization of its gene.";
RL   J. Cell. Biochem. 69:304-315(1998).
CC   -!- FUNCTION: Plays a part in calcium-regulated keratinocyte
CC       activation in epidermal repair mechanisms. Has no effect on cell
CC       proliferation (By similarity). Possesses ATPase activity.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Quinone oxidoreductase subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA64807.1; Type=Erroneous initiation;
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DR   EMBL; AK034795; BAC28833.1; -; mRNA.
DR   EMBL; BC024586; AAH24586.1; -; mRNA.
DR   EMBL; BC025496; AAH25496.1; -; mRNA.
DR   EMBL; X95562; CAA64807.1; ALT_INIT; mRNA.
DR   IPI; IPI00126072; -.
DR   RefSeq; NP_036167.1; NM_012037.2.
DR   UniGene; Mm.29210; -.
DR   ProteinModelPortal; Q62465; -.
DR   SMR; Q62465; 59-400.
DR   STRING; Q62465; -.
DR   PhosphoSite; Q62465; -.
DR   PRIDE; Q62465; -.
DR   Ensembl; ENSMUST00000040430; ENSMUSP00000048350; ENSMUSG00000034993.
DR   GeneID; 26949; -.
DR   KEGG; mmu:26949; -.
DR   UCSC; uc007loz.1; mouse.
DR   CTD; 26949; -.
DR   MGI; MGI:1349450; Vat1.
DR   GeneTree; ENSGT00550000074483; -.
DR   HOGENOM; HBG753318; -.
DR   HOVERGEN; HBG002466; -.
DR   InParanoid; Q62465; -.
DR   OMA; LPVTPGM; -.
DR   OrthoDB; EOG4FXR7X; -.
DR   PhylomeDB; Q62465; -.
DR   NextBio; 304887; -.
DR   ArrayExpress; Q62465; -.
DR   Bgee; Q62465; -.
DR   Genevestigator; Q62465; -.
DR   GermOnline; ENSMUSG00000034993; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR013149; ADH_C.
DR   InterPro; IPR013154; ADH_GroES-like.
DR   InterPro; IPR002085; ADH_SF_Zn.
DR   InterPro; IPR011032; GroES-like.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR11695; ADH_Sf_Zn; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; GroES_like; 1.
DR   PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Oxidoreductase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    406       Synaptic vesicle membrane protein VAT-1
FT                                homolog.
FT                                /FTId=PRO_0000160919.
FT   MOD_RES       2      2       N-acetylserine (By similarity).
SQ   SEQUENCE   406 AA;  43097 MW;  3F704C3667C21E37 CRC64;
     MSAEREAAEA ATVAAATEAG AETGTGAGEG APSQPPTVEV ASDPQPPPAP EASASASAPP
     LRCLVLTGFG GYDKVKLQSR PAVPPAPGPG QLTLRVRACG LNFADLMGRQ GLYDRLPPLP
     VTPGMEGAGV VVAVGEGVGD RKAGDRVMVL NRSGMWQEEV TVPSAQTFLM PEAMTFEEAA
     ALLVNYITAY MVLFDFGNLR PGHSVLVHMA AGGVGMAALQ LCRTVENVTV FGTASASKHE
     VLKENGVTHP IDYHTTDYVD EIKKISPKGV DIVMDPLGGS DTAKGYHLLK PMGKVVTYGM
     ANLLTGPKRN LMAMARTWWN QFSVTALQLL QANRAVCGFH LGYLDGEVEL VNSVVTRLVA
     LYNQGHIKPR IDSVWPFEKV ADAMKQMQEK KNIGKVLLVP GPEKET
//
ID   MINT_MOUSE              Reviewed;        3644 AA.
AC   Q62504; Q80TN9; Q99PS4; Q9QZW2;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2003, sequence version 2.
DT   08-MAR-2011, entry version 106.
DE   RecName: Full=Msx2-interacting protein;
DE   AltName: Full=SMART/HDAC1-associated repressor protein;
DE   AltName: Full=SPEN homolog;
GN   Name=Spen; Synonyms=Kiaa0929, Mint, Sharp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-112.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 49-3644 (ISOFORM 1), FUNCTION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DNA-BINDING, AND INTERACTION
RP   WITH MSX2.
RC   TISSUE=Testis;
RX   MEDLINE=99379811; PubMed=10451362; DOI=10.1021/bi990967j;
RA   Newberry E.P., Latifi T., Towler D.A.;
RT   "The RRM domain of MINT, a novel msx2 binding protein, recognizes and
RT   regulates the rat osteocalcin promoter.";
RL   Biochemistry 38:10678-10690(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 69-3644 (ISOFORM 2), AND VARIANTS
RP   THR-348; PHE-762; PHE-773 AND LEU-933.
RC   STRAIN=ICR; TISSUE=Brain;
RA   Sakamoto T., Gotou T., Isagawa Y., Mimura H., Kimura K., Kawaichi M.;
RT   "MINT/spen negatively regulates Notch signaling by inhibiting RBP-
RT   J/Su(H) activity.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 318-578, AND VARIANT THR-348.
RC   TISSUE=Cochlea;
RX   MEDLINE=97237053; PubMed=9119401; DOI=10.1006/geno.1996.4526;
RA   Crozet F., El-Amraoui A., Blanchard S., Lenoir M., Ripoll C., Vago P.,
RA   Hamel C., Fizames C., Levi-Acobas F., Depetris D., Mattei M.-G.,
RA   Weil D., Pujol R., Petit C.;
RT   "Cloning of the genes encoding two murine and human cochlear
RT   unconventional type I myosins.";
RL   Genomics 40:332-341(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2600-3644 (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [6]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=22261914; PubMed=12374742; DOI=10.1093/emboj/cdf549;
RA   Oswald F., Kostezka U., Astrahantseff K., Bourteele S., Dillinger K.,
RA   Zechner U., Ludwig L., Wilda M., Hameister H., Knoechel W., Liptay S.,
RA   Schmid R.M.;
RT   "SHARP is a novel component of the Notch/RBP-Jkappa signalling
RT   pathway.";
RL   EMBO J. 21:5417-5426(2002).
RN   [8]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   MEDLINE=22483652; PubMed=12594956; DOI=10.1016/S1074-7613(03)00029-3;
RA   Kuroda K., Han H., Tani S., Tanigaki K., Tun T., Furukawa T.,
RA   Taniguchi Y., Kurooka H., Hamada Y., Toyokuni S., Honjo T.;
RT   "Regulation of marginal zone B cell development by MINT, a suppressor
RT   of Notch/RBP-J signaling pathway.";
RL   Immunity 18:301-312(2003).
RN   [9]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15131132; DOI=10.1074/jbc.M314098200;
RA   Sierra O.L., Cheng S.L., Loewy A.P., Charlton-Kachigian N.,
RA   Towler D.A.;
RT   "MINT, the Msx2 interacting nuclear matrix target, enhances Runx2-
RT   dependent activation of the osteocalcin fibroblast growth factor
RT   response element.";
RL   J. Biol. Chem. 279:32913-32923(2004).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-758; SER-762 AND
RP   SER-766, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May serve as a nuclear matrix platform that organizes
CC       and integrates transcriptional responses. In osteoblasts, supports
CC       transcription activation: synergizes with RUNX2 to enhance FGFR2-
CC       mediated activation of the osteocalcin FGF-responsive element
CC       (OCFRE). Has also been shown to be an essential corepressor
CC       protein, which probably regulates different key pathways, such as
CC       the Notch pathway. Negative regulator of the Notch pathway via its
CC       interaction with RBPSUH, which prevents the association between
CC       NOTCH1 and RBPSUH, and therefore suppresses the transactivation
CC       activity of Notch signaling. Blocks the differentiation of
CC       precursor B-cells into marginal zone B-cells. Probably represses
CC       transcription via the recruitment of large complexes containing
CC       histone deacetylase proteins. May bind both to DNA and RNA.
CC   -!- SUBUNIT: Interacts with NCOR2, HDAC1, HDAC2, RBBP4, MBD3 and
CC       MTA1L1. Interacts with the nuclear receptors RAR and PPARD.
CC       Interacts with RAR in absence of ligand. Binds to the steroid
CC       receptor RNA coactivator SRA (By similarity). Interacts with MSX2.
CC       Interacts with RBPSUH; this interaction may prevent the
CC       interaction between RBPSUH and NOTCH1.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Associates with chromatin.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q62504-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q62504-2; Sequence=VSP_008564;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q62504-3; Sequence=VSP_013802, VSP_013803, VSP_013804;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis. Expressed at lower
CC       level in brain, lung, spleen, liver and kidney. Weakly expressed
CC       in cardiac and skeletal muscles and ovary. In spleen, it is
CC       expressed in follicular B-cells, while it is weakly expressed in
CC       marginal zone B-cells.
CC   -!- DOMAIN: The RID domain mediates the interaction with nuclear
CC       receptors.
CC   -!- DOMAIN: The SPOC domain, which mediates the interaction with
CC       NCOR2, is essential for the repressive activity (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the RRM Spen family.
CC   -!- SIMILARITY: Contains 1 RID (receptor interacting) domain.
CC   -!- SIMILARITY: Contains 4 RRM (RNA recognition motif) domains.
CC   -!- SIMILARITY: Contains 1 SPOC domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD55931.1; Type=Erroneous initiation;
CC       Sequence=CAB01562.1; Type=Erroneous termination; Positions=394; Note=Translated as Leu;
CC       Sequence=CAB01562.1; Type=Frameshift; Positions=446, 561;
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DR   EMBL; BY726481; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AF156529; AAD55931.1; ALT_INIT; mRNA.
DR   EMBL; AB055980; BAB32786.1; -; mRNA.
DR   EMBL; Z78160; CAB01562.1; ALT_SEQ; mRNA.
DR   EMBL; AK122402; BAC65684.3; -; Transcribed_RNA.
DR   IPI; IPI00378158; -.
DR   IPI; IPI00378159; -.
DR   IPI; IPI00605780; -.
DR   RefSeq; NP_062737.2; NM_019763.2.
DR   UniGene; Mm.299906; -.
DR   ProteinModelPortal; Q62504; -.
DR   SMR; Q62504; 3-68, 337-590, 3475-3644.
DR   STRING; Q62504; -.
DR   PhosphoSite; Q62504; -.
DR   PRIDE; Q62504; -.
DR   Ensembl; ENSMUST00000078886; ENSMUSP00000077925; ENSMUSG00000040761.
DR   Ensembl; ENSMUST00000105786; ENSMUSP00000101412; ENSMUSG00000040761.
DR   Ensembl; ENSMUST00000105787; ENSMUSP00000101413; ENSMUSG00000040761.
DR   GeneID; 56381; -.
DR   KEGG; mmu:56381; -.
DR   UCSC; uc008vom.1; mouse.
DR   UCSC; uc008von.1; mouse.
DR   CTD; 56381; -.
DR   MGI; MGI:1891706; Spen.
DR   GeneTree; ENSGT00530000063730; -.
DR   HOVERGEN; HBG045583; -.
DR   OrthoDB; EOG4JM7NS; -.
DR   PhylomeDB; Q62504; -.
DR   ArrayExpress; Q62504; -.
DR   Bgee; Q62504; -.
DR   Genevestigator; Q62504; -.
DR   GermOnline; ENSMUSG00000040761; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0003697; F:single-stranded DNA binding; IDA:MGI.
DR   GO; GO:0016563; F:transcription activator activity; IDA:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR   GO; GO:0016564; F:transcription repressor activity; IDA:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:MGI.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR016194; SPOC-like.
DR   InterPro; IPR012921; SPOC_C.
DR   InterPro; IPR010912; SPOC_met.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 4.
DR   Gene3D; G3DSA:2.40.290.10; G3DSA:2.40.290.10; 1.
DR   Pfam; PF00076; RRM_1; 3.
DR   Pfam; PF07744; SPOC; 1.
DR   SMART; SM00360; RRM; 4.
DR   SUPFAM; SSF100939; SPOC-like; 1.
DR   PROSITE; PS50102; RRM; 4.
DR   PROSITE; PS50917; SPOC; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Coiled coil; DNA-binding;
KW   Notch signaling pathway; Nucleus; Phosphoprotein; Polymorphism;
KW   Repeat; Repressor; RNA-binding; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   3644       Msx2-interacting protein.
FT                                /FTId=PRO_0000081628.
FT   DOMAIN        6     81       RRM 1.
FT   DOMAIN      336    416       RRM 2.
FT   DOMAIN      439    514       RRM 3.
FT   DOMAIN      518    590       RRM 4.
FT   DOMAIN     2216   2704       RID.
FT   DOMAIN     3478   3644       SPOC.
FT   DNA_BIND      1    574
FT   REGION     2138   2462       Interaction with MSX2.
FT   REGION     2706   2845       Interaction with RBPSUH.
FT   COILED      559    575       Potential.
FT   COILED      822    850       Potential.
FT   COILED     1185   1206       Potential.
FT   COILED     1509   1544       Potential.
FT   COILED     1607   1627       Potential.
FT   COMPBIAS    125    277       Arg-rich.
FT   COMPBIAS    236    326       Ser-rich.
FT   COMPBIAS    648    721       Tyr-rich.
FT   COMPBIAS    702    832       Arg-rich.
FT   COMPBIAS   2101   2233       Ala-rich.
FT   COMPBIAS   2377   2518       Pro-rich.
FT   COMPBIAS   2950   3475       Pro-rich.
FT   MOD_RES      43     43       Phosphoserine (By similarity).
FT   MOD_RES     260    260       Phosphoserine (By similarity).
FT   MOD_RES     263    263       Phosphoserine (By similarity).
FT   MOD_RES     266    266       Phosphothreonine (By similarity).
FT   MOD_RES     747    747       Phosphoserine (By similarity).
FT   MOD_RES     749    749       Phosphoserine (By similarity).
FT   MOD_RES     758    758       Phosphoserine.
FT   MOD_RES     762    762       Phosphoserine.
FT   MOD_RES     766    766       Phosphoserine.
FT   MOD_RES     869    869       Phosphoserine (By similarity).
FT   MOD_RES    1209   1209       Phosphoserine (By similarity).
FT   MOD_RES    1237   1237       Phosphoserine (By similarity).
FT   MOD_RES    1276   1276       Phosphoserine (By similarity).
FT   MOD_RES    1283   1283       Phosphoserine (By similarity).
FT   MOD_RES    1293   1293       Phosphoserine (By similarity).
FT   MOD_RES    1298   1298       Phosphoserine (By similarity).
FT   MOD_RES    1302   1302       Phosphoserine (By similarity).
FT   MOD_RES    1348   1348       Phosphoserine (By similarity).
FT   MOD_RES    1395   1395       Phosphoserine (By similarity).
FT   MOD_RES    1397   1397       Phosphoserine (By similarity).
FT   MOD_RES    1405   1405       Phosphoserine (By similarity).
FT   MOD_RES    1407   1407       Phosphoserine (By similarity).
FT   MOD_RES    1454   1454       Phosphothreonine (By similarity).
FT   MOD_RES    1456   1456       Phosphothreonine (By similarity).
FT   MOD_RES    1634   1634       Phosphothreonine (By similarity).
FT   MOD_RES    1651   1651       Phosphoserine (By similarity).
FT   MOD_RES    1844   1844       Phosphothreonine (By similarity).
FT   MOD_RES    1875   1875       Phosphoserine (By similarity).
FT   MOD_RES    1915   1915       Phosphoserine (By similarity).
FT   MOD_RES    1936   1936       Phosphoserine (By similarity).
FT   MOD_RES    1965   1965       Phosphothreonine (By similarity).
FT   MOD_RES    2128   2128       Phosphoserine (By similarity).
FT   MOD_RES    2134   2134       Phosphoserine (By similarity).
FT   MOD_RES    2366   2366       Phosphoserine (By similarity).
FT   MOD_RES    2450   2450       Phosphoserine (By similarity).
FT   MOD_RES    2458   2458       Phosphothreonine (By similarity).
FT   MOD_RES    2491   2491       Phosphoserine (By similarity).
FT   MOD_RES    2682   2682       Phosphothreonine (By similarity).
FT   MOD_RES    2913   2913       Phosphothreonine (By similarity).
FT   MOD_RES    2925   2925       Phosphothreonine (By similarity).
FT   MOD_RES    3413   3413       Phosphoserine (By similarity).
FT   VAR_SEQ     618    640       Missing (in isoform 2).
FT                                /FTId=VSP_008564.
FT   VAR_SEQ    3318   3322       PPEGE -> RKPAFF (in isoform 3).
FT                                /FTId=VSP_013802.
FT   VAR_SEQ    3550   3552       ETD -> RLE (in isoform 3).
FT                                /FTId=VSP_013803.
FT   VAR_SEQ    3553   3644       Missing (in isoform 3).
FT                                /FTId=VSP_013804.
FT   VARIANT     348    348       I -> T.
FT   VARIANT     762    762       S -> F.
FT   VARIANT     773    773       S -> F.
FT   VARIANT     933    933       S -> L.
FT   CONFLICT    366    366       V -> E (in Ref. 4; CAB01562).
FT   CONFLICT    394    394       L -> B (in Ref. 4; CAB01562).
FT   CONFLICT    409    409       V -> E (in Ref. 4; CAB01562).
FT   CONFLICT    413    413       V -> E (in Ref. 4; CAB01562).
FT   CONFLICT    430    430       I -> K (in Ref. 4; CAB01562).
FT   CONFLICT    454    462       DLRNIFQRF -> EPSETSFSAL (in Ref. 4;
FT                                CAB01562).
FT   CONFLICT    511    511       F -> L (in Ref. 4; CAB01562).
FT   CONFLICT    527    527       S -> P (in Ref. 4; CAB01562).
FT   CONFLICT    537    537       H -> N (in Ref. 4; CAB01562).
FT   CONFLICT    566    566       A -> V (in Ref. 4; CAB01562).
FT   CONFLICT    569    569       A -> V (in Ref. 4; CAB01562).
FT   CONFLICT    573    577       TKGRK -> DQGQE (in Ref. 4; CAB01562).
FT   CONFLICT    754    754       R -> G (in Ref. 3; BAB32786).
FT   CONFLICT   1524   1524       D -> A (in Ref. 3; BAB32786).
FT   CONFLICT   1560   1560       H -> Y (in Ref. 3; BAB32786).
FT   CONFLICT   1570   1570       F -> L (in Ref. 3; BAB32786).
FT   CONFLICT   1574   1574       R -> G (in Ref. 3; BAB32786).
FT   CONFLICT   1609   1609       Q -> R (in Ref. 3; BAB32786).
FT   CONFLICT   1659   1659       I -> V (in Ref. 3; BAB32786).
FT   CONFLICT   1669   1669       S -> F (in Ref. 3; BAB32786).
FT   CONFLICT   1705   1705       V -> A (in Ref. 3; BAB32786).
FT   CONFLICT   1815   1815       A -> V (in Ref. 3; BAB32786).
FT   CONFLICT   2097   2097       G -> A (in Ref. 3; BAB32786).
FT   CONFLICT   2201   2202       Missing (in Ref. 3; BAB32786).
FT   CONFLICT   2322   2322       A -> V (in Ref. 3; BAB32786).
FT   CONFLICT   2385   2385       P -> Q (in Ref. 3; BAB32786).
FT   CONFLICT   2502   2502       R -> K (in Ref. 3; BAB32786).
FT   CONFLICT   2505   2505       E -> K (in Ref. 3; BAB32786).
FT   CONFLICT   2519   2519       D -> N (in Ref. 3; BAB32786).
FT   CONFLICT   2554   2554       T -> S (in Ref. 3; BAB32786).
FT   CONFLICT   2679   2688       LVSTPAGPVN -> VGEHPWWARD (in Ref. 3;
FT                                BAB32786).
FT   CONFLICT   3010   3010       L -> P (in Ref. 3; BAB32786 and 5;
FT                                BAC65684).
SQ   SEQUENCE   3644 AA;  398754 MW;  9C7EC49A81A7DA4A CRC64;
     MVRETRHLWV GNLPENVREE KIIEHFKRYG RVESVKILPK RGSEGGVAAF VDFVDIKSAQ
     KAHNSVNKMG DRDLRTDYNE PGTIPSAARG LDETVSIASR SREVSGFRGS AGGPAYGPPP
     SLHAREGRYE RRLDGASDNR ERAYEHSAYG HHERGTGAFD RTRHYDQDYY RDPRERTLQH
     GLYYTSRSRS PNRFDAHDPR YEPRAREQFT LPSVVHRDIY RDDITREVRG RRPERSYQHS
     RSRSPHSSQS RNQSPQRLAS QASRPTRSPS GSGSRSRSSS SDSISSSSSS SNTDSSDSSS
     TASDDSPARS VQSAAVPAPT SQLLSSLEKD EPRKSFGIKV QNLPVRSIDT SLKDGLFHEF
     KKFGKVTSVQ IHGASEERYG LVFFRQQEDQ EKALTASKGK LFFGMQIEVT AWVGPETESE
     NEFRPLDERI DEFHPKATRT LFIGNLEKTT TYHDLRNIFQ RFGEIVDIDI KKVNGVPQYA
     FLQYCDIASV CKAIKKMDGE YLGNNRLKLG FGKSMPTNCV WLDGLSSNVS DQYLTRHFCR
     YGPVVKVVFD RLKGMALVLY SEIEDAQAAV KETKGRKIGG NKIKVDFANR ESQLAFYHCM
     EKSGQDMRDF YEMLTERRAG QMAQSKHEDW SADAQSPHKC REERRGSYEY SQERTYYENV
     RTPGTYPEDS RRDYPARGRE FYSEWETYQG EYYDSRYYDE PREYREYRSD PYEQDIREYS
     YRQRERERER ERFESDRDHE RRPIERSQSP VHLRRPQSPG VSPAHSERLP SDSERRLYRR
     SSERSGSCSS VSPPRYDKLE KARLERYTKN EKADKERTFD PERVERERRI VRKEKGEKDK
     AERQKRKGKA HSPSSQPSET EQENDREQSP EKPRGSTKLS RDRADKEGPA KNRLELVPCV
     VLTRVKEKEG KVIEHPPPEK LKARLGRDTT KASALDQKPQ AAQGEPAKSD PARGKALREK
     VLPSHAEVGE KEGRTKLRKH LKAEQTPELS ALDLEKLEAR KRRFADSGLK IEKQKPEIKK
     TSPETEDTRI LLKKQPDTSR DGVLLREGES ERKPVRKEIL KRESKKTKLE RLNSALSPKD
     CQDPAAVSAG SGSRPSSDVH AGLGELTHGS VETQETQPKK AIPSKPQPKQ LQLLENQGPE
     KEEVRKNYCR PREEPAEHRA GQEKPHGGNA EEKLGIDIDH TQSYRKQMEQ SRRKQRMEME
     IAKAEKFGSP KKDVDDYERR SLVHEVGKPP QDVTDDSPPS KKRRTDHVDF DICTKRERNY
     RSSRQISEDS ERTSCSPSVR HGSFHDDDDP RGSPRLVSVK GSPKGDEKGL PYPNAAVRDD
     PLKCNPYDSG KREQTADTAK IKLSVLNSEG EPSRWDPPMK QDPSRFDVSF PNSVIKRDSL
     RKRSVRDLEP GEVPSDSDED AEHRSQSPRA SSFYDSPRLS FLLRDRDQKL RERDERLASS
     LERNKFYSFA LDKTITPDTK ALLERAKSLS SSREENWSFL DWDSRFANFR NNKDKEKVDS
     APRPIPSWYM KKKKIRTDSE GKLDDKKDER REEEQERQEL FASRFLHSSI FEQDSKRLQH
     LERKSEESDF PPGRLYGRQA SEGANSTSDS VQEPVVLFHS RFMELTRMQQ KEKEKDQKPK
     EAEKQEEPET HPKTPEPAAE TKEPEPKAPV SAGLPAVTIT VVTPEPASSA PEKAEEAAEA
     PSPAGEKPAE PAPVSEETKL VSEPVSVPVE QPRQSDVPPG EDSRDSQDSA ALAPSAPQES
     AATDAVPCVN AEPLTPGTTV SQVESSVDPK PSSPQPLSKL TQRSEEAEEG KVEKPDTTPS
     TEPDATQNAG VASEAQPPAS EDVEANPPVA AKDRKTNKSK RSKTSVQAAA ASVVEKPVTR
     KSERIDREKL KRSSSPRGEA QKLLELKMEA EKITRTASKS SGGDTEHPEP SLPLSRSRRR
     NVRSVYATMT DHESRSPAKE PVEQPRVTRK RLERELQEAV VPPTTPRRGR PPKTRRRAEE
     DGEHERKEPA ETPRPAEGWR SPRSQKSAAA AGPQGKRGRN EQKVEAAAEA GAQASTREGN
     PKSRGEREAA SEPKRDRRDP STDKSGPDTF PVEVLERKPP EKTYKSKRGR ARSTRSGMDR
     AAHQRSLEMA ARAAGQAADK EAGPAAASPQ ESESPQKGSG SSPQLANNPA DPDREAEEES
     ASASTAPPEG TQLARQIELE QAVQNIAKLP EPSAAAASKG TATATATAAS EEPAPEHGHK
     PAHQASETEL AAAIGSIISD ASGEPENFSA PPSVPPGSQT HPREGMEPGL HEAESGILET
     GTATESSAPQ VSALDPPEGS ADTKETRGNS GDSVQEAKGS KAEVTPPRKD KGRQKTTRRR
     KRNANKKVVA ITETRASEAE QTQSESPAAE EATAATPEAP QEEKPSEKPP SPPAECTFDP
     SKTPPAESLS QENSAAEKTP CKAPVLPALP PLSQPALMDD GPQARFKVHS IIESDPVTPP
     SDSGIPPPTI PLVTIAKLPP PVIPGGVPHQ SPPPKVTEWI TRQEEPRAQS TPSPALPPDT
     KASDMDTSSS TLRKILMDPK YVSATGVTST SVTTAIAEPV SAPCLQEAPA PPCDPKHPPL
     EGVSAAAVPN ADTQASEVPV AADKEKVAPV IAPKITSVIS RMPVSIDLEN SQKITLAKPA
     PQTLTGLVSA LTGLVNVSLV PVNALKGPVK GSVATLKGLV STPAGPVNLL KGPVNVLTGP
     VNVLTTPVSA TVGTVNAAPG PVTAACGVTA TTGTAAVTGA VTAPAAKGKQ RASSNENSRF
     HPGSMSVIDD RPADTGSGAG LRVNTSEGVV LLSYSGQKTE GPQRISAKIS QIPPASAMDI
     EFQQSVSKSQ VKADSITPTQ SAPKGPQTPS AFANVAAHST LVLTAQTYNA SPVISSVKTD
     RPSLEKPEPI HLSVSTPVTQ GGTVKVLTQG INTPPVLVHN QLVLTPSIVT TNKKLADPVT
     LKIETKVLQP ANLGPTLTPH HPPALPSKLP AEVNHVPSGP STPADRTIAH LATPKPDTHS
     PRPTGPTPGL FPRPCHPSST TSTALSTNAT VMLAAGIPVP QFISSIHPEQ SVIMPPHSIT
     QTVSLGHLSQ GEVRMSTPTL PSITYSIRPE TLHSPRAPLQ PQQIEARAPQ RVGTPQPATT
     GVPALATQHP PEEEVHYHLP VARAAAPVQS EVLVMQSEYR LHPYTVPRDV RIMVHPHVTA
     VSEQPRATEG VVKVPPANKA PQQLVKEAVK TSDAKAVPAP APVPVPVPVP TPAPPPHGEA
     RILTVTPSSQ LQGLPLTPPV VVTHGVQIVH SSGELFQEYR YGDVRTYHAP AQQLTHTQFP
     VASSISLASR TKTSAQVPPE GEPLQSTQSA QPAPSTQATQ PIPPAPPCQP SQLSQPAQPP
     SGKIPQVSQE AKGTQTGGVE QTRLPAIPTN RPSEPHAQLQ RAPVETAQPA HPSPVSVSMK
     PDLPSPLSSQ AAPKQPLFVP ANSGPSTPPG LALPHAEVQP APKQESSPHG TPQRPVDMVQ
     LLKKYPIVWQ GLLALKNDTA AVQLHFVSGN NVLAHRSLPL SEGGPPLRIA QRMRLEASQL
     EGVARRMTVE TDYCLLLALP CGRDQEDVVS QTESLKAAFI TYLQAKQAAG IINVPNPGSN
     QPAYVLQIFP PCEFSESHLS RLAPDLLASI SNISPHLMIV IASV
//
ID   ZFP91_MOUSE             Reviewed;         572 AA.
AC   Q62511; Q3TEQ3; Q3UH61; Q62509; Q6P219; Q6PG06; Q8BPY3; Q8C2B4;
AC   Q8CDZ3;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 3.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=E3 ubiquitin-protein ligase ZFP91;
DE            EC=6.3.2.-;
DE   AltName: Full=Penta Zf protein;
DE   AltName: Full=Zinc finger protein 91 homolog;
DE            Short=Zfp-91;
DE   AltName: Full=Zinc finger protein PZF;
GN   Name=Zfp91; Synonyms=Pzf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Brain, and Testis;
RX   MEDLINE=95137394; PubMed=7835706; DOI=10.1016/0378-1119(94)00717-7;
RA   Saotome Y., Winter C.G., Hirsh D.;
RT   "A widely expressed novel C2H2 zinc-finger protein with multiple
RT   consensus phosphorylation sites is conserved in mouse and man.";
RL   Gene 152:233-238(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Eye, Head, Placenta, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 252-572.
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Colon, and Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Atypical E3 ubiquitin-protein ligase that mediates 'Lys-
CC       63'-linked ubiquitination of MAP3K14/NIK, leading to stabilize and
CC       activate MAP3K14/NIK. It thereby acts as an activator of the non-
CC       canonical NF-kappa-B2/NFKB2 pathway. May also play an important
CC       role in cell proliferation and/or anti-apoptosis (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with MAP3K14/NIK (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q62511-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q62511-2; Sequence=VSP_025759, VSP_025760;
CC   -!- TISSUE SPECIFICITY: Found in all the examined tissues including
CC       brain, heart, kidney, lung, liver, spleen, thymus, skeletal
CC       muscle, ovary and testis.
CC   -!- MISCELLANEOUS: In contrast to other E3 ubiquitin-protein ligase,
CC       does not contain any domain (RING-type zinc finger or HECT domain)
CC       known to mediate E3 ligase activity.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family.
CC   -!- SIMILARITY: Contains 5 C2H2-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC26394.1; Type=Frameshift; Positions=341;
CC       Sequence=BAC34808.1; Type=Erroneous initiation;
CC       Sequence=BAC40660.1; Type=Frameshift; Positions=341;
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DR   EMBL; U05342; AAA81911.1; -; mRNA.
DR   EMBL; U05343; AAA81913.1; -; mRNA.
DR   EMBL; AK029319; BAC26394.1; ALT_FRAME; mRNA.
DR   EMBL; AK051904; BAC34808.1; ALT_INIT; mRNA.
DR   EMBL; AK088933; BAC40660.1; ALT_FRAME; mRNA.
DR   EMBL; AK147502; BAE27956.1; -; mRNA.
DR   EMBL; AK147560; BAE27996.1; -; mRNA.
DR   EMBL; AK169477; BAE41195.1; -; mRNA.
DR   EMBL; BC057323; AAH57323.1; -; mRNA.
DR   EMBL; BC064766; AAH64766.1; -; mRNA.
DR   EMBL; BC083000; AAH83000.1; -; mRNA.
DR   IPI; IPI00652969; -.
DR   IPI; IPI00849177; -.
DR   PIR; I48722; I48722.
DR   PIR; I48724; I48724.
DR   RefSeq; NP_443735.2; NM_053009.3.
DR   UniGene; Mm.290924; -.
DR   ProteinModelPortal; Q62511; -.
DR   SMR; Q62511; 309-461.
DR   STRING; Q62511; -.
DR   PhosphoSite; Q62511; -.
DR   PRIDE; Q62511; -.
DR   Ensembl; ENSMUST00000038627; ENSMUSP00000037971; ENSMUSG00000024695.
DR   GeneID; 109910; -.
DR   KEGG; mmu:109910; -.
DR   CTD; 109910; -.
DR   MGI; MGI:104854; Zfp91.
DR   GeneTree; ENSGT00530000063153; -.
DR   HOVERGEN; HBG055547; -.
DR   OrthoDB; EOG4Z8XXK; -.
DR   NextBio; 362995; -.
DR   ArrayExpress; Q62511; -.
DR   Bgee; Q62511; -.
DR   CleanEx; MM_ZFP91; -.
DR   Genevestigator; Q62511; -.
DR   GermOnline; ENSMUSG00000024695; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; ISS:UniProtKB.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 3.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; Ligase; Metal-binding; Nucleus; Phosphoprotein;
KW   Repeat; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    572       E3 ubiquitin-protein ligase ZFP91.
FT                                /FTId=PRO_0000047313.
FT   ZN_FING     313    338       C2H2-type 1.
FT   ZN_FING     344    368       C2H2-type 2.
FT   ZN_FING     374    396       C2H2-type 3.
FT   ZN_FING     402    424       C2H2-type 4.
FT   ZN_FING     432    455       C2H2-type 5.
FT   REGION      340    370       Interaction with MAP3K14/NIK (By
FT                                similarity).
FT   COMPBIAS    211    284       Glu-rich.
FT   MOD_RES      85     85       Phosphoserine (By similarity).
FT   MOD_RES      86     86       Phosphoserine (By similarity).
FT   MOD_RES     106    106       Phosphoserine.
FT   MOD_RES     397    397       Phosphothreonine (By similarity).
FT   VAR_SEQ       1    111       Missing (in isoform 2).
FT                                /FTId=VSP_025759.
FT   VAR_SEQ     112    128       KSPRLQCIEKLTTDKDP -> MKTKKECEEDD (in
FT                                isoform 2).
FT                                /FTId=VSP_025760.
FT   CONFLICT    104    104       P -> A (in Ref. 2; BAE41195).
FT   CONFLICT    218    218       E -> Q (in Ref. 2; BAC40660).
FT   CONFLICT    256    256       K -> T (in Ref. 1; AAA81911/AAA81913).
FT   CONFLICT    297    297       K -> R (in Ref. 2; BAC40660).
FT   CONFLICT    331    331       Q -> E (in Ref. 1; AAA81911).
FT   CONFLICT    466    466       A -> V (in Ref. 1; AAA81911/AAA81913).
FT   CONFLICT    498    498       P -> T (in Ref. 2; BAC26394).
FT   CONFLICT    528    529       VS -> LI (in Ref. 1; AAA81911).
SQ   SEQUENCE   572 AA;  63389 MW;  C57D976BA1DC07F4 CRC64;
     MPGETEEPRS PEQQDQEGGP AAAADAASEE LRPGAAAAPA APAETASSRV LRGGRDRGRT
     AAAAAAAAAA VSRRRKAEYP RRRRSSPSNR PPDGPGHQPA AAKPPSPAQG KKSPRLQCIE
     KLTTDKDPKE EKEDDSVLPQ EVSITTTRAS RSWRSSSRTS ISRLRDSENT RSSRSKTGSL
     QLVCKTEPIT DQLDYDVPEE HQSPGGISSD EEEEEEEEML ISEEEIPFKD DPRDETYKPH
     LERETPKPRR KSGKVKEEKE KKEIKVEVEV EVKEEENEIR EDEEPPRKRG RRRKDDKSPR
     LPKRRKKPPI QYVRCEMEGC GTVLAHPRYL QHHIKYQHLL KKKYVCPHPS CGRLFRLQKQ
     LLRHAKHHTD QRDYICEYCA RAFKSSHNLA VHRMIHTGEK PLQCEICGFT CRQKASLNWH
     MKKHDADSFY QFSCNICGKK FEKKDSVVAH KAKSHPEVLI AEALAANAGA LITSTDILGT
     NPEPLTQPAD GQGLPLLPEP LGNSTAGECL LLEAEGMSKS YCSGTERVSL MADGKIFVGS
     GSSGGTEGLV MNSDILGATT EVLIEDTDST GP
//
ID   ZYX_MOUSE               Reviewed;         564 AA.
AC   Q62523; P70461;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Zyxin;
GN   Name=Zyx;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR X Swiss Webster;
RX   MEDLINE=97094926; PubMed=8940160; DOI=10.1074/jbc.271.49.31470;
RA   Macalma T., Otte J., Hensler M.E., Bockholt S.M., Louis H.A.,
RA   Kalff-Suske M., Grzeschik K.H., von der Ahe D., Beckerle M.C.;
RT   "Molecular characterization of human zyxin.";
RL   J. Biol. Chem. 271:31470-31478(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Otte J., Heischmann A., Breier G., Beckerle M.C., von der Ahe D.;
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-160, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144 AND SER-336, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Adhesion plaque protein. Binds alpha-actinin and the CRP
CC       protein. Important for targeting TES and ENA/VASP family members
CC       to focal adhesions and for the formation of actin-rich structures.
CC       May be a component of a signal transduction pathway that mediates
CC       adhesion-stimulated changes in gene expression (By similarity).
CC   -!- SUBUNIT: Interacts, via the Pro-rich regions, with the EVH1
CC       domains of ENAH, EVL and VASP. Interacts with the first LIM domain
CC       of TES (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity). Cell junction, focal adhesion (By
CC       similarity). Nucleus (By similarity). Note=Associates with the
CC       actin cytoskeleton near the adhesion plaques. Enters the nucleus
CC       in the presence of HESX1 (By similarity).
CC   -!- SIMILARITY: Belongs to the zyxin/ajuba family.
CC   -!- SIMILARITY: Contains 3 LIM zinc-binding domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Y07711; CAA68984.1; -; mRNA.
DR   EMBL; X99063; CAA67510.1; -; mRNA.
DR   IPI; IPI00228360; -.
DR   RefSeq; NP_035907.1; NM_011777.2.
DR   UniGene; Mm.282303; -.
DR   ProteinModelPortal; Q62523; -.
DR   SMR; Q62523; 373-564.
DR   STRING; Q62523; -.
DR   PhosphoSite; Q62523; -.
DR   PRIDE; Q62523; -.
DR   Ensembl; ENSMUST00000070635; ENSMUSP00000070427; ENSMUSG00000029860.
DR   GeneID; 22793; -.
DR   KEGG; mmu:22793; -.
DR   CTD; 22793; -.
DR   MGI; MGI:103072; Zyx.
DR   eggNOG; maNOG14552; -.
DR   HOGENOM; HBG714563; -.
DR   HOVERGEN; HBG093602; -.
DR   InParanoid; Q62523; -.
DR   OrthoDB; EOG4MSCZN; -.
DR   ArrayExpress; Q62523; -.
DR   Bgee; Q62523; -.
DR   CleanEx; MM_ZYX; -.
DR   Genevestigator; Q62523; -.
DR   GermOnline; ENSMUSG00000029860; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   InterPro; IPR001781; Znf_LIM.
DR   Gene3D; G3DSA:2.10.110.10; Znf_LIM; 3.
DR   Pfam; PF00412; LIM; 3.
DR   SMART; SM00132; LIM; 3.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Cell adhesion; Cell junction; Cytoplasm; Cytoskeleton;
KW   LIM domain; Metal-binding; Nucleus; Phosphoprotein; Repeat; Zinc.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    564       Zyxin.
FT                                /FTId=PRO_0000075914.
FT   DOMAIN      376    435       LIM zinc-binding 1.
FT   DOMAIN      436    495       LIM zinc-binding 2.
FT   DOMAIN      496    562       LIM zinc-binding 3.
FT   COMPBIAS     64     77       Pro-rich.
FT   COMPBIAS     94    109       Pro-rich.
FT   COMPBIAS    116    121       Pro-rich.
FT   COMPBIAS    128    138       Pro-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     144    144       Phosphoserine.
FT   MOD_RES     160    160       Phosphothreonine.
FT   MOD_RES     170    170       Phosphoserine (By similarity).
FT   MOD_RES     180    180       Phosphothreonine (By similarity).
FT   MOD_RES     265    265       Phosphothreonine (By similarity).
FT   MOD_RES     270    270       N6-acetyllysine (By similarity).
FT   MOD_RES     272    272       Phosphoserine (By similarity).
FT   MOD_RES     300    300       Phosphoserine (By similarity).
FT   MOD_RES     305    305       Phosphoserine (By similarity).
FT   MOD_RES     336    336       Phosphoserine.
FT   CONFLICT    215    215       R -> A (in Ref. 1; CAA68984).
FT   CONFLICT    284    292       IKKWCLRMP -> NQKMVPPDA (in Ref. 1;
FT                                CAA68984).
FT   CONFLICT    484    484       S -> C (in Ref. 1; CAA68984).
SQ   SEQUENCE   564 AA;  60790 MW;  001E1B3C82ADA1EB CRC64;
     MAAPRPPPAI SVSVSAPAFY APQKKFAPVV APKPKVNPFR PGDSEPPVAA GAQRAQMGRV
     GEIPPPPPED FPLPPPPLIG EGDDSEGALG GAFPPPPPPM IEEPFPPAPL EEDIFPSPPP
     PLEEEGGPEA PTQLPPQPRE KVCSIDLEID SLSSLLDDMT KNDPFKARVS SGYVPPPVAT
     PFVPKPSTKP APGGTAPLPP WKTPSSSQPP PQPQRKPQVQ LHVQPQAKPH VQPQPVSSAN
     TQPRGPLSQA PTPAPKFAPV APKFTPVVSK FSPGAPSGPG PQPIKKWCLR MPPSSVSTGS
     PQPPSFTYAQ QKEKPLVQEK QHPQPPPAQN QNQVRSPGGP GPLTLKEVEE LEQLTQQLMQ
     DMEHPQRQSV AVNESCGKCN QPLARAQPAV RALGQLFHIT CFTCHQCQQQ LQGQQFYSLE
     GAPYCEGCYT DTLEKCNTCG QPITDRMLRA TGKAYHPQCF TCVVCACPLE GTSFIVDQAN
     QPHSVPDYHK QYAPRCSVCS EPIMPEPGRD ETVRVVALDK NFHMKCYKCE DCGKPLSIEA
     DDNGCFPLDG HVLCRKCHSA RAQT
//
ID   MK03_MOUSE              Reviewed;         380 AA.
AC   Q63844; Q61531; Q8K0X5; Q91YW5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 5.
DT   08-MAR-2011, entry version 117.
DE   RecName: Full=Mitogen-activated protein kinase 3;
DE            Short=MAP kinase 3;
DE            Short=MAPK 3;
DE            EC=2.7.11.24;
DE   AltName: Full=ERT2;
DE   AltName: Full=Extracellular signal-regulated kinase 1;
DE            Short=ERK-1;
DE   AltName: Full=Insulin-stimulated MAP2 kinase;
DE   AltName: Full=MAP kinase isoform p44;
DE            Short=p44-MAPK;
DE   AltName: Full=MNK1;
DE   AltName: Full=Microtubule-associated protein 2 kinase;
DE   AltName: Full=Mitogen-activated protein kinase 1;
DE            Short=MAP kinase 1;
DE            Short=MAPK 1;
DE   AltName: Full=p44-ERK1;
GN   Name=Mapk3; Synonyms=Erk1, Prkm3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-65; 89-105; 110-132; 157-209; 213-221; 280-288;
RP   304-319 AND 361-371, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP   ALA-2, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RA   Bienvenut W.V., Serrels B., Brunton V.G., Frame M.C.;
RL   Submitted (FEB-2008) to UniProtKB.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4-380.
RX   PubMed=8424957; DOI=10.1016/0167-4781(93)90074-N;
RA   Tanner B., Mueckler M.;
RT   "Molecular cloning of a mouse extracellular signal regulated kinase
RT   (erk-1).";
RL   Biochim. Biophys. Acta 1171:319-320(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-19.
RC   TISSUE=Pre-B cell;
RX   MEDLINE=92020947; PubMed=1717989; DOI=10.1073/pnas.88.19.8845;
RA   Crews C.M., Alessandrini A.A., Erikson R.L.;
RT   "Mouse Erk-1 gene product is a serine/threonine protein kinase that
RT   has the potential to phosphorylate tyrosine.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:8845-8849(1991).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 77-380.
RC   TISSUE=Fetal brain;
RX   MEDLINE=91369479; PubMed=1716439; DOI=10.1089/dna.1991.10.505;
RA   de Miguel C., Kligman D., Patel J., Detera-Wadleigh S.D.;
RT   "Molecular analysis of microtubule-associated protein-2 kinase cDNA
RT   from mouse and rat brain.";
RL   DNA Cell Biol. 10:505-514(1991).
RN   [6]
RP   PROTEIN SEQUENCE OF 136-153 AND 191-209, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 171-209.
RC   STRAIN=CBA; TISSUE=Bone marrow;
RX   MEDLINE=93185941; PubMed=8444355; DOI=10.1016/0378-1119(93)90411-U;
RA   Ershler M.A., Nagorskaya T.V., Visser J.W.M., Belyavsky A.V.;
RT   "Novel CDC2-related protein kinases produced in murine hematopoietic
RT   stem cells.";
RL   Gene 124:305-306(1993).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 171-205.
RX   MEDLINE=93092802; PubMed=1459009;
RA   Ershler M.A., Nagorskaya T.V., Visser J.W.M., Belyavsky A.V.;
RT   "Identification of new protein kinase genes, similar to kinases of the
RT   cdc2 family and expressed in murine hematopoietic stem cells.";
RL   Dokl. Akad. Nauk SSSR 324:893-897(1992).
RN   [9]
RP   INTERACTION WITH MORG1.
RX   PubMed=15118098; DOI=10.1073/pnas.0305894101;
RA   Vomastek T., Schaeffer H.-J., Tarcsafalvi A., Smolkin M.E.,
RA   Bissonette E.A., Weber M.J.;
RT   "Modular construction of a signaling scaffold: MORG1 interacts with
RT   components of the ERK cascade and links ERK signaling to specific
RT   agonists.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:6981-6986(2004).
RN   [10]
RP   PHOSPHORYLATION OF SPZ1.
RX   PubMed=15899793; DOI=10.1158/0008-5472.CAN-04-3658;
RA   Hsu S.-H., Hsieh-Li H.-M., Huang H.-Y., Huang P.-H., Li H.;
RT   "bHLH-zip transcription factor Spz1 mediates mitogen-activated protein
RT   kinase cell proliferation, transformation, and tumorigenesis.";
RL   Cancer Res. 65:4041-4050(2005).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND TYR-205, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND TYR-205, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND TYR-205, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND TYR-205, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Involved in both the initiation and regulation of
CC       meiosis, mitosis, and postmitotic functions in differentiated
CC       cells by phosphorylating a number of transcription factors such as
CC       ELK-1. Phosphorylates EIF4EBP1; required for initiation of
CC       translation. Phosphorylates microtubule-associated protein 2
CC       (MAP2) and heat shock factor protein 4 (HSF4) (By similarity).
CC       Phosphorylates SPZ1.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activated by tyrosine and threonine
CC       phosphorylation.
CC   -!- SUBUNIT: Interacts with HSF4 and NISCH (By similarity). Interacts
CC       with MORG1. Interacts with ARRB2 (By similarity). Interacts with
CC       ADAM15 (By similarity).
CC   -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC       whose phosphorylation activates the MAP kinases.
CC   -!- PTM: Dually phosphorylated on Thr-203 and Tyr-205, which activates
CC       the enzyme. Dephosphorylated by PTPRJ at Tyr-205 (By similarity).
CC       Autophosphorylates on threonine and tyrosine residues in vitro.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. MAP kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC013754; AAH13754.1; -; mRNA.
DR   EMBL; BC029712; AAH29712.1; -; mRNA.
DR   EMBL; S58470; AAB19973.1; -; mRNA.
DR   EMBL; X64605; CAA45889.1; -; mRNA.
DR   IPI; IPI00230277; -.
DR   PIR; S28184; S28184.
DR   RefSeq; NP_036082.1; NM_011952.2.
DR   UniGene; Mm.8385; -.
DR   ProteinModelPortal; Q63844; -.
DR   SMR; Q63844; 25-375.
DR   STRING; Q63844; -.
DR   PhosphoSite; Q63844; -.
DR   PRIDE; Q63844; -.
DR   Ensembl; ENSMUST00000057669; ENSMUSP00000051619; ENSMUSG00000063065.
DR   GeneID; 26417; -.
DR   KEGG; mmu:26417; -.
DR   NMPDR; fig|10090.3.peg.17639; -.
DR   UCSC; uc009jsm.1; mouse.
DR   CTD; 26417; -.
DR   MGI; MGI:1346859; Mapk3.
DR   eggNOG; roNOG04134; -.
DR   GeneTree; ENSGT00550000074298; -.
DR   HOVERGEN; HBG014652; -.
DR   OrthoDB; EOG45HRXM; -.
DR   PhylomeDB; Q63844; -.
DR   BRENDA; 2.7.11.24; 244.
DR   NextBio; 304429; -.
DR   ArrayExpress; Q63844; -.
DR   Bgee; Q63844; -.
DR   CleanEx; MM_MAPK3; -.
DR   Genevestigator; Q63844; -.
DR   GermOnline; ENSMUSG00000063065; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; EXP:Reactome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004707; F:MAP kinase activity; IDA:MGI.
DR   GO; GO:0001784; F:phosphotyrosine binding; IMP:MGI.
DR   GO; GO:0030528; F:transcription regulator activity; IMP:UniProtKB.
DR   GO; GO:0051216; P:cartilage development; IDA:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:MGI.
DR   GO; GO:0009887; P:organ morphogenesis; IDA:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR   GO; GO:0051090; P:regulation of transcription factor activity; IMP:UniProtKB.
DR   GO; GO:0006974; P:response to DNA damage stimulus; IDA:MGI.
DR   GO; GO:0043330; P:response to exogenous dsRNA; IDA:MGI.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:UniProtKB.
DR   InterPro; IPR008349; Erk_1_2_MAPK.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR003527; MAP_kinase_CS.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01770; ERK1ERK2MAPK.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS01351; MAPK; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cell cycle; Direct protein sequencing;
KW   Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    380       Mitogen-activated protein kinase 3.
FT                                /FTId=PRO_0000186252.
FT   DOMAIN       43    331       Protein kinase.
FT   NP_BIND      49     57       ATP (By similarity).
FT   MOTIF       203    205       TXY.
FT   ACT_SITE    167    167       Proton acceptor (By similarity).
FT   BINDING      72     72       ATP (By similarity).
FT   MOD_RES       2      2       N-acetylalanine.
FT   MOD_RES     171    171       Phosphoserine (By similarity).
FT   MOD_RES     199    199       Phosphothreonine (By similarity).
FT   MOD_RES     203    203       Phosphothreonine.
FT   MOD_RES     205    205       Phosphotyrosine.
FT   CONFLICT    178    178       T -> P (in Ref. 7; CAA45889 and 8; no
FT                                nucleotide entry).
SQ   SEQUENCE   380 AA;  43066 MW;  49C14A95B627237F CRC64;
     MAAAAAAPGG GGGEPRGTAG VVPVVPGEVE VVKGQPFDVG PRYTQLQYIG EGAYGMVSSA
     YDHVRKTRVA IKKISPFEHQ TYCQRTLREI QILLRFRHEN VIGIRDILRA PTLEAMRDVY
     IVQDLMETDL YKLLKSQQLS NDHICYFLYQ ILRGLKYIHS ANVLHRDLKP SNLLINTTCD
     LKICDFGLAR IADPEHDHTG FLTEYVATRW YRAPEIMLNS KGYTKSIDIW SVGCILAEML
     SNRPIFPGKH YLDQLNHILG ILGSPSQEDL NCIINMKARN YLQSLPSKTK VAWAKLFPKS
     DSKALDLLDR MLTFNPNKRI TVEEALAHPY LEQYYDPTDE PVAEEPFTFD MELDDLPKER
     LKELIFQETA RFQPGAPEGP
//
ID   NUP62_MOUSE             Reviewed;         526 AA.
AC   Q63850; Q99JN7;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Nuclear pore glycoprotein p62;
DE   AltName: Full=62 kDa nucleoporin;
DE   AltName: Full=Nucleoporin Nup62;
GN   Name=Nup62;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=92007945; PubMed=1915419;
RA   Cordes V., Waizenegger I., Krohne G.;
RT   "Nuclear pore complex glycoprotein p62 of Xenopus laevis and mouse:
RT   cDNA cloning and identification of its glycosylated region.";
RL   Eur. J. Cell Biol. 55:31-47(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Essential component of the nuclear pore complex. The N-
CC       terminal is probably involved in nucleocytoplasmic transport. The
CC       C-terminal is probably involved in protein-protein interaction via
CC       coiled-coil formation and may function in anchorage of p62 to the
CC       pore complex (By similarity).
CC   -!- SUBUNIT: Component of the p62 complex, a complex at least composed
CC       of NUP62, NUP54, and NUPL1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Cytoplasm,
CC       cytoskeleton, spindle pole (By similarity). Note=Central region of
CC       the nuclear pore, within the transporter. During mitotic cell
CC       division, it associates with the poles of the mitotic spindle (By
CC       similarity).
CC   -!- DOMAIN: Contains F-X-F-G repeats.
CC   -!- PTM: O-glycosylated.
CC   -!- SIMILARITY: Belongs to the nucleoporin NSP1/NUP62 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; S59342; AAB19953.1; -; mRNA.
DR   EMBL; BC005784; AAH05784.1; -; mRNA.
DR   IPI; IPI00139994; -.
DR   PIR; A56573; A56573.
DR   RefSeq; NP_444304.1; NM_053074.1.
DR   UniGene; Mm.2565; -.
DR   UniGene; Mm.440497; -.
DR   ProteinModelPortal; Q63850; -.
DR   STRING; Q63850; -.
DR   PhosphoSite; Q63850; -.
DR   PRIDE; Q63850; -.
DR   Ensembl; ENSMUST00000057195; ENSMUSP00000056785; ENSMUSG00000043858.
DR   Ensembl; ENSMUST00000107891; ENSMUSP00000103523; ENSMUSG00000043858.
DR   GeneID; 18226; -.
DR   KEGG; mmu:18226; -.
DR   UCSC; uc009gqw.1; mouse.
DR   CTD; 18226; -.
DR   MGI; MGI:1351500; Nup62.
DR   GeneTree; ENSGT00490000043409; -.
DR   HOGENOM; HBG281771; -.
DR   HOVERGEN; HBG052699; -.
DR   InParanoid; Q63850; -.
DR   OMA; DSLQWVD; -.
DR   OrthoDB; EOG4TXBT3; -.
DR   PhylomeDB; Q63850; -.
DR   NextBio; 293652; -.
DR   ArrayExpress; Q63850; -.
DR   Bgee; Q63850; -.
DR   CleanEx; MM_NUP62; -.
DR   Genevestigator; Q63850; -.
DR   GermOnline; ENSMUSG00000043858; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005643; C:nuclear pore; ISS:UniProtKB.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0051425; F:PTB domain binding; IPI:UniProtKB.
DR   GO; GO:0030159; F:receptor signaling complex scaffold activity; ISS:UniProtKB.
DR   GO; GO:0042169; F:SH2 domain binding; ISS:UniProtKB.
DR   GO; GO:0017056; F:structural constituent of nuclear pore; IEA:InterPro.
DR   GO; GO:0046966; F:thyroid hormone receptor binding; ISS:UniProtKB.
DR   GO; GO:0030528; F:transcription regulator activity; ISS:UniProtKB.
DR   GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR   GO; GO:0007569; P:cell aging; IDA:MGI.
DR   GO; GO:0008219; P:cell death; ISS:UniProtKB.
DR   GO; GO:0016477; P:cell migration; NAS:UniProtKB.
DR   GO; GO:0007166; P:cell surface receptor linked signaling pathway; ISS:UniProtKB.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0043066; P:negative regulation of apoptosis; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
DR   GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IMP:UniProtKB.
DR   GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:UniProtKB.
DR   GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IMP:UniProtKB.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; ISS:UniProtKB.
DR   GO; GO:0045941; P:positive regulation of transcription; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:UniProtKB-KW.
DR   InterPro; IPR007758; Nucleoporin_Nsp1_C.
DR   PANTHER; PTHR12084; Nsp1_C; 1.
DR   Pfam; PF05064; Nsp1_C; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Glycoprotein; mRNA transport;
KW   Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW   Repeat; Translocation; Transport.
FT   CHAIN         1    526       Nuclear pore glycoprotein p62.
FT                                /FTId=PRO_0000204881.
FT   COILED      332    462       Potential.
FT   COMPBIAS     17    295       Thr-rich.
FT   COMPBIAS    202    335       Ala-rich.
FT   COMPBIAS    271    284       Poly-Thr.
FT   COMPBIAS    292    295       Poly-Thr.
FT   MOD_RES     412    412       Phosphoserine.
FT   CARBOHYD    377    377       O-linked (GlcNAc) (By similarity).
FT   CARBOHYD    472    472       O-linked (GlcNAc) (By similarity).
FT   CONFLICT    113    113       G -> V (in Ref. 1; AAB19953).
FT   CONFLICT    319    319       A -> V (in Ref. 1; AAB19953).
SQ   SEQUENCE   526 AA;  53255 MW;  54AE74B211018FE4 CRC64;
     MSGFNFGGTG APAGGFTFGT AKTATTTPAT GFSFSASGTG TGGFNFGTPS QPAATTPSTS
     LFSLTTQTPT TQTPGFNFGT TPASGGTGFS LGISTPKLSL SNAAATPATA NTGSFGLGSS
     TLTNAISSGS TSNQGTAPTG FVFGSSTTSA PSTGSTGFSF TSGSASQPGA SGFSLGSVGS
     SAQPTALSGS PFTPATLVTT TAGATQPAAA APTAATTSAG STLFASIAAA PASSSATGLS
     LPAPVTTAAT PSAGTLGFSL KAPGAAPGAS TTSTTTTTTT TTTTAAAAAA STTTTGFALS
     LKPLVSAGPS SVAATALPAS STAAGTATGP AMTYAQLESL INKWSLELED QERHFLQQAT
     QVNAWDRTLI ENGEKITSLH REVEKVKLDQ KRLDQELDFI LSQQKELEDL LSPLEESVKE
     QSGTIYLQHA DEEREKTYKL AENIDAQLKR MAQDLKDIIE HLNMAGGPAD TSDPLQQICK
     ILNAHMDSLQ WVDQSSALLQ RRVEEASRVC EGRRKEQERS LRIAFD
//
ID   SDPR_MOUSE              Reviewed;         418 AA.
AC   Q63918; Q3V1P6; Q78EC3; Q8CBT4;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Serum deprivation-response protein;
DE   AltName: Full=Cavin-2;
DE   AltName: Full=Phosphatidylserine-binding protein;
GN   Name=Sdpr; Synonyms=Sdr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RX   MEDLINE=94059824; PubMed=8241023;
RA   Gustincich S., Schneider C.;
RT   "Serum deprivation response gene is induced by serum starvation but
RT   not by contact inhibition.";
RL   Cell Growth Differ. 4:753-760(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryonic head, Embryonic spinal ganglion, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Mammary gland, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293; SER-359; SER-363
RP   AND THR-368, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-204; SER-359
RP   AND SER-363, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INDUCTION.
RX   PubMed=18332105; DOI=10.1128/MCB.02186-07;
RA   Ogata T., Ueyama T., Isodono K., Tagawa M., Takehara N., Kawashima T.,
RA   Harada K., Takahashi T., Shioi T., Matsubara H., Oh H.;
RT   "MURC, a muscle-restricted coiled-coil protein that modulates the
RT   Rho/ROCK pathway, induces cardiac dysfunction and conduction
RT   disturbance.";
RL   Mol. Cell. Biol. 28:3424-3436(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; SER-293; SER-359
RP   AND SER-363, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: May play a role in targeting PRKCA to caveolae (By
CC       similarity).
CC   -!- SUBUNIT: Binds to PRKCA in the presence of phosphatidylserine.
CC       Interacts with MURC; this augments the transactivation of NPPA by
CC       MURC (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Membrane, caveola (By
CC       similarity). Note=Colocalizes with CAV1 to caveolae (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in kidney, lung and heart,
CC       and expressed at lower levels in liver, spleen, thymus, stomach,
CC       intestine and uterus.
CC   -!- DEVELOPMENTAL STAGE: Expression gradually increases during
CC       embryonic stages and reaches a maximum in neonates.
CC   -!- INDUCTION: Up-regulated in response to cardiac hypertrophy and in
CC       serum-starved but not in density-dependent growth-arrested NIH3T3
CC       cells. Down-regulated within 6 hours after the addition of serum
CC       or epidermal growth factor to serum-starved cells.
CC   -!- PTM: The N-terminus is blocked (By similarity).
CC   -!- MISCELLANEOUS: Binds phosphatidylserine (PS) in a calcium-
CC       independent manner. PS-binding is inhibited by phosphotidic acid
CC       and phosphatidylinositol. Does not bind phosphatidylcholine (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the PTRF/SDPR family.
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DR   EMBL; S67386; AAB28953.1; -; mRNA.
DR   EMBL; AK035324; BAC29033.1; -; mRNA.
DR   EMBL; AK084096; BAC39116.1; -; mRNA.
DR   EMBL; AK132324; BAE21104.1; -; mRNA.
DR   EMBL; BC020008; AAH20008.1; -; mRNA.
DR   EMBL; BC027005; AAH27005.1; -; mRNA.
DR   IPI; IPI00135660; -.
DR   RefSeq; NP_620080.1; NM_138741.1.
DR   UniGene; Mm.480575; -.
DR   ProteinModelPortal; Q63918; -.
DR   STRING; Q63918; -.
DR   PhosphoSite; Q63918; -.
DR   PRIDE; Q63918; -.
DR   Ensembl; ENSMUST00000051572; ENSMUSP00000055694; ENSMUSG00000045954.
DR   GeneID; 20324; -.
DR   KEGG; mmu:20324; -.
DR   UCSC; uc007axk.1; mouse.
DR   CTD; 20324; -.
DR   MGI; MGI:99513; Sdpr.
DR   eggNOG; roNOG09995; -.
DR   GeneTree; ENSGT00530000063058; -.
DR   HOGENOM; HBG715099; -.
DR   HOVERGEN; HBG056807; -.
DR   InParanoid; Q63918; -.
DR   OMA; QASTSNT; -.
DR   OrthoDB; EOG4S4PGT; -.
DR   PhylomeDB; Q63918; -.
DR   NextBio; 298127; -.
DR   ArrayExpress; Q63918; -.
DR   Bgee; Q63918; -.
DR   CleanEx; MM_SDPR; -.
DR   Genevestigator; Q63918; -.
DR   GermOnline; ENSMUSG00000045954; Mus musculus.
DR   GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Cytoplasm; Lipid-binding; Membrane;
KW   Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    418       Serum deprivation-response protein.
FT                                /FTId=PRO_0000238919.
FT   COILED       61     87       Potential.
FT   COILED      126    268       Potential.
FT   MOD_RES       2      2       N-acetylglycine (By similarity).
FT   MOD_RES     203    203       Phosphoserine.
FT   MOD_RES     204    204       Phosphoserine.
FT   MOD_RES     218    218       Phosphoserine.
FT   MOD_RES     287    287       Phosphoserine (By similarity).
FT   MOD_RES     288    288       Phosphoserine.
FT   MOD_RES     293    293       Phosphoserine.
FT   MOD_RES     359    359       Phosphoserine.
FT   MOD_RES     363    363       Phosphoserine.
FT   MOD_RES     368    368       Phosphothreonine.
FT   MOD_RES     388    388       Phosphotyrosine (By similarity).
FT   MOD_RES     392    392       Phosphotyrosine (By similarity).
FT   CONFLICT     14     14       P -> L (in Ref. 2; BAE21104).
FT   CONFLICT     76     76       Q -> L (in Ref. 2; BAC29033).
FT   CONFLICT    173    173       K -> R (in Ref. 2; BAC29033).
SQ   SEQUENCE   418 AA;  46764 MW;  EFD7B4E383785F41 CRC64;
     MGEDAAQAEK FQHPNTDMLQ EKPSSPSPMP SSTPSPSLNL GSTEEAIRDN SQVNAVTVHT
     LLDKLVNMLD AVRENQHNME QRQINLEGSV KGIQNDLTKL SKYQASTSNT VSKLLEKSRK
     VSAHTRAVRE RLERQCVQVK RLENNHAQLL RRNHFKVLIF QEESEIPASV FVKEPVPSAA
     EGKEELADEN KSLEETLHNV DLSSDDELPR DEEALEDSAE EKMEESRAEK IKRSSLKKVD
     SLKKAFSRQN IEKKMNKLGT KIVSVERREK IKKSLTPNHQ KASSGKSSPF KVSPLSFGRK
     KVREGESSVE NETKLEDQMQ EDREEGSFTE GLSEASLPSG LMEGSAEDAE KSARRGNNSA
     VGSNADLTIE EDEEEEPVAL QQAQQVRYES GYMLNSEEME EPSEKQVQPA VLHVDQTA
//
ID   MP2K2_MOUSE             Reviewed;         401 AA.
AC   Q63932;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=Dual specificity mitogen-activated protein kinase kinase 2;
DE            Short=MAP kinase kinase 2;
DE            Short=MAPKK 2;
DE            EC=2.7.12.2;
DE   AltName: Full=ERK activator kinase 2;
DE   AltName: Full=MAPK/ERK kinase 2;
DE            Short=MEK 2;
GN   Name=Map2k2; Synonyms=Mek2, Mkk2, Prkmk2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS.
RC   STRAIN=BALB/c; TISSUE=Neonatal brain;
RX   MEDLINE=94128609; PubMed=8297798;
RA   Brott B.K., Alessandrini A., Largaespada D.A., Copeland N.G.,
RA   Jenkins N.A., Crews C.M., Erikson R.L.;
RT   "MEK2 is a kinase related to MEK1 and is differentially expressed in
RT   murine tissues.";
RL   Cell Growth Differ. 4:921-929(1993).
RN   [2]
RP   PROTEIN SEQUENCE OF 118-140 AND 210-238.
RC   TISSUE=T-cell;
RX   MEDLINE=92390415; PubMed=1381507; DOI=10.1073/pnas.89.17.8205;
RA   Crews C.M., Erikson R.L.;
RT   "Purification of a murine protein-tyrosine/threonine kinase that
RT   phosphorylates and activates the Erk-1 gene product: relationship to
RT   the fission yeast byr1 gene product.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:8205-8209(1992).
RN   [3]
RP   INTERACTION WITH MORG1.
RX   PubMed=15118098; DOI=10.1073/pnas.0305894101;
RA   Vomastek T., Schaeffer H.-J., Tarcsafalvi A., Smolkin M.E.,
RA   Bissonette E.A., Weber M.J.;
RT   "Modular construction of a signaling scaffold: MORG1 interacts with
RT   components of the ERK cascade and links ERK signaling to specific
RT   agonists.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:6981-6986(2004).
CC   -!- FUNCTION: Catalyzes the concomitant phosphorylation of a threonine
CC       and a tyrosine residue in a Thr-Glu-Tyr sequence located in MAP
CC       kinases. Activates the ERK1 and ERK2 MAP kinases.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Inhibited by serine/threonine phosphatase 2A.
CC   -!- SUBUNIT: Interacts with MORG1.
CC   -!- TISSUE SPECIFICITY: Expressed in adult intestine, kidney, liver,
CC       lung, pancreas, spleen, thymus, and at high levels in the neonatal
CC       brain. Lower expression is found in adult brain and heart.
CC   -!- PTM: Phosphorylation on Ser/Thr by MAP kinase kinase kinases (RAF
CC       or MEKK1) regulates positively the kinase activity. Low levels of
CC       autophosphorylation have been observed.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; S68267; AAC60678.1; -; mRNA.
DR   IPI; IPI00135708; -.
DR   UniGene; Mm.275436; -.
DR   ProteinModelPortal; Q63932; -.
DR   SMR; Q63932; 60-393.
DR   DIP; DIP-454N; -.
DR   IntAct; Q63932; 6.
DR   MINT; MINT-1518275; -.
DR   STRING; Q63932; -.
DR   PhosphoSite; Q63932; -.
DR   PRIDE; Q63932; -.
DR   Ensembl; ENSMUST00000143517; ENSMUSP00000121111; ENSMUSG00000035027.
DR   MGI; MGI:1346867; Map2k2.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108518; -.
DR   InParanoid; Q63932; -.
DR   OrthoDB; EOG4SF965; -.
DR   PhylomeDB; Q63932; -.
DR   BRENDA; 2.7.12.2; 244.
DR   ArrayExpress; Q63932; -.
DR   Bgee; Q63932; -.
DR   CleanEx; MM_MAP2K2; -.
DR   Genevestigator; Q63932; -.
DR   GermOnline; ENSMUSG00000035027; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Direct protein sequencing; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase;
KW   Transferase; Tyrosine-protein kinase.
FT   CHAIN         1    401       Dual specificity mitogen-activated
FT                                protein kinase kinase 2.
FT                                /FTId=PRO_0000086373.
FT   DOMAIN       72    370       Protein kinase.
FT   NP_BIND      78     86       ATP (By similarity).
FT   COMPBIAS    266    316       Pro-rich.
FT   ACT_SITE    194    194       Proton acceptor (By similarity).
FT   BINDING     101    101       ATP.
FT   SITE         10     11       Cleavage; by anthrax lethal factor (By
FT                                similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      23     23       Phosphoserine (By similarity).
FT   MOD_RES     222    222       Phosphoserine; by RAF (By similarity).
FT   MOD_RES     226    226       Phosphoserine; by RAF (By similarity).
FT   MOD_RES     293    293       Phosphoserine (By similarity).
FT   MOD_RES     295    295       Phosphoserine (By similarity).
FT   MOD_RES     395    395       Phosphothreonine (By similarity).
FT   MOD_RES     397    397       Phosphothreonine (By similarity).
FT   MUTAGEN     101    101       K->M: Inactivation.
SQ   SEQUENCE   401 AA;  44436 MW;  04EB6D8A5DE60A4B CRC64;
     MLARRKPVLP ALTINPTIAE GPSPTSEGAS EANLVDLQKK LEELDLDEQQ RKRLEAFLTQ
     KAKVGELKDD DFERISELGA GNGGVVTKAR HRPSGFIMAR KLIHLEIKPA VRNQIIRELQ
     VLHECNSPYI VGFYGAFYSD GEISICMEHM DGGSLDQVLK EAKRIPEDIL GKVSIAVLRG
     LAYLREKHQI MHRDVKPSNI LVNSRGEIKL CDFGVSGQLI DSMANSFVGT RSYMSPERLQ
     GTHYSVQSDI WSMGLSLVEL AIGRYPIPPP DAKELEASFG RPVVDGADGE PHSVSPRPRP
     PGRPISVGHG MDSRPAMAIF ELLDYIVNEP PPKLPSGVFS SDFQEFVNKC LIKNPAERAD
     LKLLMNHAFI KRSEGEEVDF AGWLCRTLRL KQPSTPTRTA V
//
ID   MEF2D_MOUSE             Reviewed;         514 AA.
AC   Q63943; Q63944;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   08-FEB-2011, entry version 87.
DE   RecName: Full=Myocyte-specific enhancer factor 2D;
GN   Name=Mef2d;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS MUSCLE AND NON-MUSCLE).
RX   MEDLINE=94158837; PubMed=8114702;
RA   Martin J.F., Miano J.M., Hustad C.M., Copeland N.G., Jenkins N.A.,
RA   Olson E.N.;
RT   "A Mef2 gene that generates a muscle-specific isoform via alternative
RT   mRNA splicing.";
RL   Mol. Cell. Biol. 14:1647-1656(1994).
RN   [2]
RP   TISSUE SPECIFICITY, AND DEVEPOMENTAL STAGE.
RC   TISSUE=Cerebellum;
RX   MEDLINE=97165895; PubMed=9013788; DOI=10.1016/S0169-328X(96)00135-0;
RA   Lin X., Shah S., Bulleit R.F.;
RT   "The expression of MEF2 genes is implicated in CNS neuronal
RT   differentiation.";
RL   Brain Res. Mol. Brain Res. 42:307-316(1996).
RN   [3]
RP   TISSUE SPECIFICITY OF ISOFORMS.
RX   PubMed=15834131; DOI=10.1074/jbc.M502491200;
RA   Zhu B., Ramachandran B., Gulick T.;
RT   "Alternative pre-mRNA splicing governs expression of a conserved
RT   acidic transactivation domain in myocyte enhancer factor 2 factors of
RT   striated muscle and brain.";
RL   J. Biol. Chem. 280:28749-28760(2005).
RN   [4]
RP   SUMOYLATION.
RX   PubMed=16166628; DOI=10.1128/MCB.25.19.8456-8464.2005;
RA   Zhao X., Sternsdorf T., Bolger T.A., Evans R.M., Yao T.-P.;
RT   "Regulation of MEF2 by histone deacetylase 4- and SIRT1 deacetylase-
RT   mediated lysine modifications.";
RL   Mol. Cell. Biol. 25:8456-8464(2005).
RN   [5]
RP   PHOSPHORYLATION AT SER-437, FUNCTION, TISSUE SPECIFICITY, AND
RP   MUTAGENESIS OF SER-437.
RX   PubMed=16407541; DOI=10.1523/JNEUROSCI.2875-05.2006;
RA   Smith P.D., Mount M.P., Shree R., Callaghan S., Slack R.S.,
RA   Anisman H., Vincent I., Wang X., Mao Z., Park D.S.;
RT   "Calpain-regulated p35/cdk5 plays a central role in dopaminergic
RT   neuron death through modulation of the transcription factor myocyte
RT   enhancer factor 2.";
RL   J. Neurosci. 26:440-447(2006).
RN   [6]
RP   PHOSPHORYLATION AT SER-121 AND SER-190, INTERACTION WITH HDAC4,
RP   FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND MUTAGENESIS OF
RP   THR-20; SER-121 AND SER-190.
RX   PubMed=18299387; DOI=10.1128/MCB.00248-08;
RA   Du M., Perry R.L.S., Nowacki N.B., Gordon J.W., Salma J., Zhao J.,
RA   Aziz A., Chan J., Siu K.W.M., McDermott J.C.;
RT   "Protein kinase A represses skeletal myogenesis by targeting myocyte
RT   enhancer factor 2D.";
RL   Mol. Cell. Biol. 28:2952-2970(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Transcriptional activator which binds specifically to
CC       the MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-
CC       specific, growth factor- and stress-induced genes. Mediates
CC       cellular functions not only in skeletal and cardiac muscle
CC       development, but also in neuronal differentiation and survival.
CC       Plays diverse roles in the control of cell growth, survival and
CC       apoptosis via p38 MAPK signaling in muscle-specific and/or growth
CC       factor-related transcription. Plays a critical role in the
CC       regulation of neuronal apoptosis.
CC   -!- SUBUNIT: Forms a complex with class II HDACs in undifferentiating
CC       cells. On myogenic differentiation, HDACs are released into the
CC       cytoplasm allowing MEF2s to interact with other proteins for
CC       activation. Interacts with HDAC4 (in undifferentiating cells); the
CC       interaction translocates MEF2D to nuclear dots. Forms a
CC       heterodimer with MEF2A (By similarity). Interacts with MAPK7; the
CC       interaction phosphorylates but does not activate MEF2D.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Translocated by HDAC4 to
CC       nuclear dots (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Non-muscle;
CC         IsoId=Q63943-1; Sequence=Displayed;
CC       Name=Muscle;
CC         IsoId=Q63943-2; Sequence=VSP_006253, VSP_006254;
CC   -!- TISSUE SPECIFICITY: Widely expressed though mainly restricted to
CC       skeletal and cardiac muscle, brain, neurons and lymphocytes.
CC       Differentially expressed depending on if isoforms contain the beta
CC       domain or not, with the total expression of the beta domain-
CC       lacking isoforms vastly exceding that of the beta domain-
CC       containing isoforms. Isoforms containing the beta domain are
CC       expressed primarily in skeletal and cardiac muscle and in brain.
CC       Also present in lung and testis. Splicing to include the beta
CC       domain is induced in differentiating myocytes. Isoforms lacking
CC       the beta domain are expressed less abundantly in skeletal muscle,
CC       brain and lymphocytes, and are uniquely found in ovary, liver,
CC       spleen and kidney. In embryos, the beta domain-containing and beta
CC       domain-lacking isoforms are equally expressed. Also expressed
CC       cerebellar granule neurons and other regions of the CNS. Highest
CC       levels in the olfactory bulb, cortex, hippocampus, thalamus and
CC       cerebellum.
CC   -!- DEVELOPMENTAL STAGE: In the developing cerebellum, increasing
CC       levels after birth. The majority of this increase occurs around
CC       postnataL day 9 reaching a peak at postnatal day 15-18 which is
CC       maintained in adults.
CC   -!- PTM: Phosphorylated on Ser-437 is which is required for Lys-432
CC       sumoylation and inhibits transcriptional activity. Phosphorylation
CC       on this residue by CDK5 is dependent on p35 and calpains.
CC       Phosphorylated by PKA at Ser-121 and Ser-190 represses
CC       transcriptional activity in embryonic and postnatal skeletal
CC       muscle, and stabilizes protein levels. No in vitro phosphorylation
CC       by PKA on Thr-20.
CC   -!- PTM: Acetylated on Lys-432 by CREBBP. Deacetylated by SIRT1 (By
CC       similarity).
CC   -!- PTM: Sumoylated on Lys-432 by SUMO2 but not SUMO1; which inhibits
CC       transcriptional activity and myogenic activity. Desumoylated by
CC       SENP3 (By similarity).
CC   -!- PTM: Proteolytically cleaved in cerebellar granule neurons by
CC       caspase 7 following neurotoxicity. Preferentially cleaves the
CC       CDK5-mediated hyperphosphorylated form which leads to neuron
CC       apoptosis and transcriptional inactivation.
CC   -!- SIMILARITY: Belongs to the MEF2 family.
CC   -!- SIMILARITY: Contains 1 MADS-box domain.
CC   -!- SIMILARITY: Contains 1 Mef2-type DNA-binding domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; S68893; AAB29973.1; -; mRNA.
DR   EMBL; S68895; AAB29974.1; -; mRNA.
DR   IPI; IPI00230611; -.
DR   IPI; IPI00331135; -.
DR   PIR; B56201; B56201.
DR   UniGene; Mm.402786; -.
DR   ProteinModelPortal; Q63943; -.
DR   SMR; Q63943; 2-73.
DR   IntAct; Q63943; 3.
DR   STRING; Q63943; -.
DR   PhosphoSite; Q63943; -.
DR   PRIDE; Q63943; -.
DR   Ensembl; ENSMUST00000107558; ENSMUSP00000103183; ENSMUSG00000001419.
DR   Ensembl; ENSMUST00000107559; ENSMUSP00000103184; ENSMUSG00000001419.
DR   UCSC; uc008pua.1; mouse.
DR   UCSC; uc008pub.1; mouse.
DR   MGI; MGI:99533; Mef2d.
DR   GeneTree; ENSGT00390000011828; -.
DR   HOGENOM; HBG443633; -.
DR   HOVERGEN; HBG053944; -.
DR   InParanoid; Q63943; -.
DR   PhylomeDB; Q63943; -.
DR   PMAP-CutDB; Q63943; -.
DR   ArrayExpress; Q63943; -.
DR   Bgee; Q63943; -.
DR   CleanEx; MM_MEF2D; -.
DR   Genevestigator; Q63943; -.
DR   GermOnline; ENSMUSG00000001419; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0016563; F:transcription activator activity; IDA:MGI.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0002062; P:chondrocyte differentiation; IGI:MGI.
DR   GO; GO:0001958; P:endochondral ossification; IGI:MGI.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0001649; P:osteoblast differentiation; IGI:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IDA:MGI.
DR   InterPro; IPR022102; HJURP_C.
DR   InterPro; IPR002100; TF_MADSbox.
DR   Pfam; PF12347; HJURP_C; 1.
DR   Pfam; PF00319; SRF-TF; 1.
DR   PRINTS; PR00404; MADSDOMAIN.
DR   SMART; SM00432; MADS; 1.
DR   SUPFAM; SSF55455; TF_MADSbox; 1.
DR   PROSITE; PS00350; MADS_BOX_1; 1.
DR   PROSITE; PS50066; MADS_BOX_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Alternative splicing; Apoptosis;
KW   Developmental protein; Differentiation; DNA-binding; Isopeptide bond;
KW   Neurogenesis; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN         1    514       Myocyte-specific enhancer factor 2D.
FT                                /FTId=PRO_0000199436.
FT   DOMAIN        3     57       MADS-box.
FT   DNA_BIND     58     86       Mef2-type (Potential).
FT   REGION      286    292       Beta domain (By similarity).
FT   COMPBIAS      3     31       Arg/Lys-rich (basic).
FT   COMPBIAS    252    255       Poly-Pro.
FT   COMPBIAS    365    402       Gln/Pro-rich.
FT   COMPBIAS    444    449       Poly-Pro.
FT   SITE        288    289       Cleavage (Probable).
FT   MOD_RES       4      4       N6-acetyllysine (By similarity).
FT   MOD_RES      98     98       Phosphoserine (By similarity).
FT   MOD_RES     106    106       Phosphoserine (By similarity).
FT   MOD_RES     110    110       Phosphoserine (By similarity).
FT   MOD_RES     116    116       N6-acetyllysine (By similarity).
FT   MOD_RES     121    121       Phosphoserine; by PKA.
FT   MOD_RES     180    180       Phosphoserine; by MAPK7 (By similarity).
FT   MOD_RES     190    190       Phosphoserine; by PKA.
FT   MOD_RES     212    212       Phosphoserine (By similarity).
FT   MOD_RES     231    231       Phosphoserine (By similarity).
FT   MOD_RES     245    245       N6-acetyllysine (By similarity).
FT   MOD_RES     250    250       N6-acetyllysine (By similarity).
FT   MOD_RES     251    251       Phosphoserine.
FT   MOD_RES     267    267       N6-acetyllysine (By similarity).
FT   MOD_RES     279    279       N6-acetyllysine (By similarity).
FT   MOD_RES     432    432       N6-acetyllysine; alternate (By
FT                                similarity).
FT   MOD_RES     437    437       Phosphoserine.
FT   CROSSLNK    432    432       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO);
FT                                alternate (By similarity).
FT   VAR_SEQ      87    132       TLRKKGFNGCDSPEPDGEDSLEQSPLLEDKYRRASEELDGL
FT                                FRRYG -> ALHNNDRECESPEVDEAFALTPQTEEKYKKID
FT                                EEKYKKIDEEFDKMMQSYRLA (in isoform
FT                                Muscle).
FT                                /FTId=VSP_006253.
FT   VAR_SEQ     286    292       Missing (in isoform Muscle).
FT                                /FTId=VSP_006254.
FT   MUTAGEN      20     20       T->A: No change in DNA-binding activity.
FT   MUTAGEN      20     20       T->D: Dramatic decrease in DNA-binding.
FT   MUTAGEN     121    121       S->A: Abolishes phosphorylation by PKA.
FT                                No change in protein levels. Loss of
FT                                protein stability on PKA stimulation.
FT                                Loss of PKA-mediated repression. No
FT                                change in interaction with HDAC4 in
FT                                reponse to PKA; when associated with A-
FT                                190.
FT   MUTAGEN     190    190       S->A: Abolishes phosphorylation by PKA.
FT                                No change in protein levels. Loss of
FT                                protein stability on PKA stimulation
FT                                mediated repression. No change in
FT                                interaction with HDAC4 in response to
FT                                PKA; when associated with A-121.
FT   MUTAGEN     437    437       S->A: Loss of calpain/Cdk5-mediated
FT                                neuron apoptosis.
SQ   SEQUENCE   514 AA;  54993 MW;  1D25A80DB3E04F43 CRC64;
     MGRKKIQIQR ITDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNH SNKLFQYAST
     DMDKVLLKYT EYNEPHESRT NADIIETLRK KGFNGCDSPE PDGEDSLEQS PLLEDKYRRA
     SEELDGLFRR YGSSVPAPNF AMPVTVPVSN QSSMQFSNPS SSLVTPSLVT SSLTDPRLLS
     PQQPALQRNS VSPGLPQRPA SAGAMLGGDL NSANGACPSP VGNGYVSARA SPGLLPVANG
     NSLNKVIPAK SPPPPTHNTQ LGAPSRKPDL RVITSQGGKG LMHHLTGDHL DLNNAQRLGV
     SQSTHSLTTP VVSVATPSLL SQGLPFSSMP TAYNTDYQLP SAELSSLPAF SSPAGLALGN
     VTAWQQPQPP QQPQPPQPPQ SQPQPPQPQP QQPPQQQPHL VPVSLSNLIP GSPLPHVGAA
     LTVTTHPHIS IKSEPVSPSR ERSPAPPPPA VFPAARPEPG EGLSSPAGGS YETGDRDDGR
     GDFGPTLGLL RPAPEPEAEG SAVKRMRLDT WTLK
//
ID   KCNC3_MOUSE             Reviewed;         769 AA.
AC   Q63959; Q62088;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Potassium voltage-gated channel subfamily C member 3;
DE   AltName: Full=KSHIIID;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv3.3;
GN   Name=Kcnc3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ISOFORM KV3.3B).
RX   MEDLINE=94132879; PubMed=8301351;
RA   Goldman-Wohl D.S., Chan E., Baird D., Heintz N.;
RT   "Kv3.3b: a novel Shaw type potassium channel expressed in terminally
RT   differentiated cerebellar Purkinje cells and deep cerebellar nuclei.";
RL   J. Neurosci. 14:511-522(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 78-769 (ISOFORM KV3.3A).
RC   STRAIN=AKR/J;
RX   MEDLINE=92155707; PubMed=1740329; DOI=10.1016/0888-7543(92)90365-Y;
RA   Ghanshani S., Pak M., McPherson J.D., Strong M., Dethlefs B.,
RA   Wasmuth J.J., Salkoff L.A., Gutman G.A., Chandy G.K.;
RT   "Genomic organization, nucleotide sequence, and cellular distribution
RT   of a Shaw-related potassium channel gene, Kv3.3, and mapping of Kv3.3
RT   and Kv3.4 to human chromosomes 19 and 1.";
RL   Genomics 12:190-196(1992).
CC   -!- FUNCTION: This protein mediates the voltage-dependent potassium
CC       ion permeability of excitable membranes. Assuming opened or closed
CC       conformations in response to the voltage difference across the
CC       membrane, the protein forms a potassium-selective channel through
CC       which potassium ions may pass in accordance with their
CC       electrochemical gradient.
CC   -!- SUBUNIT: Heterotetramer of potassium channel proteins (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=KV3.3B;
CC         IsoId=Q63959-1; Sequence=Displayed;
CC       Name=KV3.3A;
CC         IsoId=Q63959-2; Sequence=VSP_001021;
CC   -!- TISSUE SPECIFICITY: The KV3.3B isoform is highly enriched in the
CC       brain, particularly in the cerebellum, where its expression is
CC       confined to Purkinje cells and deep cerebellar nuclei. Isoform
CC       KV3.3A is not expressed in cerebellum.
CC   -!- DEVELOPMENTAL STAGE: Expression of KV3.3B begins in cerebellar
CC       Purkinje cells between postnatal day 8 (P8) and P10 and continues
CC       through adulthood.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position.
CC   -!- DOMAIN: The tail may be important in modulation of channel
CC       activity and/or targeting of the channel to specific subcellular
CC       compartments.
CC   -!- SIMILARITY: Belongs to the potassium channel family. C (Shaw)
CC       (TC 1.A.1.2) subfamily. Kv3.3/KCNC3 sub-subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; S69381; AAC60679.1; -; mRNA.
DR   EMBL; X60796; CAA43209.1; -; Genomic_DNA.
DR   EMBL; X60797; CAA43209.1; JOINED; Genomic_DNA.
DR   IPI; IPI00229264; -.
DR   IPI; IPI00467430; -.
DR   PIR; A42073; A42073.
DR   UniGene; Mm.40312; -.
DR   ProteinModelPortal; Q63959; -.
DR   SMR; Q63959; 86-547.
DR   STRING; Q63959; -.
DR   PhosphoSite; Q63959; -.
DR   PRIDE; Q63959; -.
DR   Ensembl; ENSMUST00000107906; ENSMUSP00000103539; ENSMUSG00000062785.
DR   UCSC; uc009gqg.1; mouse.
DR   MGI; MGI:96669; Kcnc3.
DR   eggNOG; maNOG18894; -.
DR   GeneTree; ENSGT00580000081499; -.
DR   HOGENOM; HBG445693; -.
DR   HOVERGEN; HBG105862; -.
DR   InParanoid; Q63959; -.
DR   ArrayExpress; Q63959; -.
DR   Bgee; Q63959; -.
DR   Genevestigator; Q63959; -.
DR   GermOnline; ENSMUSG00000062785; Mus musculus.
DR   GO; GO:0030673; C:axolemma; IDA:MGI.
DR   GO; GO:0043679; C:axon terminus; IDA:MGI.
DR   GO; GO:0032590; C:dendrite membrane; IDA:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0032809; C:neuronal cell body membrane; IDA:MGI.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0046928; P:regulation of neurotransmitter secretion; IMP:MGI.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003974; K_chnl_volt-dep_Kv3.
DR   InterPro; IPR005404; K_chnl_volt-dep_Kv3.3.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01582; KV33CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01498; SHAWCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Ion transport; Ionic channel;
KW   Membrane; Phosphoprotein; Potassium; Potassium channel;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN         1    769       Potassium voltage-gated channel subfamily
FT                                C member 3.
FT                                /FTId=PRO_0000054056.
FT   TOPO_DOM      1    290       Cytoplasmic (Potential).
FT   TRANSMEM    291    309       Helical; Name=Segment S1; (Potential).
FT   TRANSMEM    351    370       Helical; Name=Segment S2; (Potential).
FT   TOPO_DOM    371    379       Cytoplasmic (Potential).
FT   TRANSMEM    380    398       Helical; Name=Segment S3; (Potential).
FT   TRANSMEM    412    434       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TOPO_DOM    435    447       Cytoplasmic (Potential).
FT   TRANSMEM    448    469       Helical; Name=Segment S5; (Potential).
FT   TRANSMEM    518    539       Helical; Name=Segment S6; (Potential).
FT   TOPO_DOM    540    769       Cytoplasmic (Potential).
FT   MOTIF       503    508       Selectivity filter (By similarity).
FT   COMPBIAS     41     44       Poly-Gln.
FT   COMPBIAS     82     86       Poly-Gly.
FT   COMPBIAS    229    234       Poly-Gly.
FT   COMPBIAS    577    587       Poly-Pro.
FT   COMPBIAS    596    599       Poly-Pro.
FT   COMPBIAS    669    674       Poly-Ala.
FT   CARBOHYD    320    320       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    336    336       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    483    483       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     660    769       VDPRPNGDPAAAALAHEDCPAIDQPAMSPEDKSPITPGSRG
FT                                RYSRDRACFLVTDYAPSPDGSIRKGYEKSRSLSSIVGLSGV
FT                                SLRLAPLATPPGSPRATRRAPPTLPSIL -> GEAGARTGG
FT                                VGRSGGKVAGLEGMQGQGFLGSGRVGWEATADRKDKWLEGW
FT                                TPGTKSHRNRIPRTRACEHGFQPGCSQRPLVRSSRVRIFGE
FT                                RDSETQV (in isoform KV3.3A).
FT                                /FTId=VSP_001021.
FT   CONFLICT    256    256       G -> D (in Ref. 2; CAA43209).
FT   CONFLICT    260    266       GAGGAGG -> ARAAGA (in Ref. 2; CAA43209).
SQ   SEQUENCE   769 AA;  82116 MW;  BCACD5AB2D66D9EC CRC64;
     MLSSVCVWSF RGCQGTGKQQ PQPVPTPQPP ESSPPPLPPP QQQQCSQPGT GPSPGVPAFL
     RPGGRRAEPC PGLPAVAMGR HGGGGGDSGK IVINVGGVRH ETYRSTLRTL PGTRLAGLTE
     PEAAARFDYD PGTDEFFFDR HPGVFAYVLN YYRTGKLHCP ADVCGPLFEE ELGFWGIDET
     DVEACCWMTY RQHRDAEEAL DSFEAPDSSA NANANAGGAH DAGLDDEAGA GGGGLDGAGG
     ELKRLCFQDA GGGAGGLPGG AGGAGGTWWR RWQPRVWALF EDPYSSRAAR YVAFASLFFI
     LISITTFCLE THEGFIHISN KTVTQASPIP GAPPENITNV EVETEPFLTY VEGVCVVWFT
     FEFLMRVTFC PDKVEFLKSS LNIIDCVAIL PFYLEVGLSG LSSKAAKDVL GFLRVVRFVR
     ILRIFKLTRH FVGLRVLGHT LRASTNEFLL LIIFLALGVL IFATMIYYAE RIGADPDDIL
     GSNHTYFKNI PIGFWWAVVT MTTLGYGDMY PKTWSGMLVG GLCALAGVLT IAMPVPVIVN
     NFGMYYSLAM AKQKLPKKKN KHIPRPPQPG SPNYCKPDPP PPPPPHPHHG SGGISPPPPI
     TPPSMGVNVA GAYPPGPHTH PGLLRGGAGG LGIMGLPPLP APGEPCPLAQ EEVIETNRAV
     DPRPNGDPAA AALAHEDCPA IDQPAMSPED KSPITPGSRG RYSRDRACFL VTDYAPSPDG
     SIRKGYEKSR SLSSIVGLSG VSLRLAPLAT PPGSPRATRR APPTLPSIL
//
ID   INADL_MOUSE             Reviewed;        1834 AA.
AC   Q63ZW7; A2ADS7; O70471; Q5PRG3; Q6P6J1; Q80YR8; Q8BPB9;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=InaD-like protein;
DE            Short=Inadl protein;
DE   AltName: Full=Channel-interacting PDZ domain-containing protein;
DE   AltName: Full=Pals1-associated tight junction protein;
DE   AltName: Full=Protein associated to tight junctions;
GN   Name=Inadl; Synonyms=Cipp, Patj;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY,
RP   INTERACTION WITH KCNJ10; KCNJ15; NRXN2; NLGN2; GRIN2A; GRIN2B; GRIN2C
RP   AND GRIN2D, AND DOMAINS.
RC   STRAIN=BALB/c; TISSUE=Cerebellum;
RX   MEDLINE=98313406; PubMed=9647694; DOI=10.1006/mcne.1998.0679;
RA   Kurschner C., Mermelstein P.G., Holden W.T., Surmeier D.J.;
RT   "CIPP, a novel multivalent PDZ domain protein, selectively interacts
RT   with Kir4.0 family members, NMDA receptor subunits, neurexins, and
RT   neuroligins.";
RL   Mol. Cell. Neurosci. 11:161-172(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 5),
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 493-1834 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 523-1834 (ISOFORM 6).
RC   STRAIN=C57BL/6, FVB/N, and NMRI;
RC   TISSUE=Brain, Embryo, Eye, Mammary tumor, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH ASIC3, DOMAIN, AND FUNCTION.
RX   PubMed=11872753; DOI=10.1074/jbc.M201087200;
RA   Anzai N., Deval E., Schaefer L., Friend V., Lazdunski M.,
RA   Lingueglia E.;
RT   "The multivalent PDZ domain-containing protein CIPP is a partner of
RT   acid-sensing ion channel 3 in sensory neurons.";
RL   J. Biol. Chem. 277:16655-16661(2002).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=22291956; PubMed=12403818; DOI=10.1083/jcb.200207050;
RA   Poliak S., Matlis S., Ullmer C., Scherer S.S., Peles E.;
RT   "Distinct claudins and associated PDZ proteins form different
RT   autotypic tight junctions in myelinating Schwann cells.";
RL   J. Cell Biol. 159:361-372(2002).
RN   [7]
RP   INTERACTION WITH HTR2A, AND SUBCELLULAR LOCATION.
RX   PubMed=14988405; DOI=10.1074/jbc.M312106200;
RA   Becamel C., Gavarini S., Chanrion B., Alonso G., Galeotti N.,
RA   Dumuis A., Bockaert J., Marin P.;
RT   "The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets
RT   of PDZ proteins.";
RL   J. Biol. Chem. 279:20257-20266(2004).
RN   [8]
RP   INTERACTION WITH HTR4.
RX   PubMed=15466885; DOI=10.1242/jcs.01379;
RA   Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W.,
RA   Marin P., Dumuis A., Bockaert J.;
RT   "New sorting nexin (SNX27) and NHERF specifically interact with the 5-
RT   HT4a receptor splice variant: roles in receptor targeting.";
RL   J. Cell Sci. 117:5367-5379(2004).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-647, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [11]
RP   INTERACTION WITH SLC6A4.
RX   PubMed=17452640; DOI=10.1073/pnas.0610964104;
RA   Chanrion B., Mannoury la Cour C., Bertaso F., Lerner-Natoli M.,
RA   Freissmuth M., Millan M.J., Bockaert J., Marin P.;
RT   "Physical interaction between the serotonin transporter and neuronal
RT   nitric oxide synthase underlies reciprocal modulation of their
RT   activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8119-8124(2007).
CC   -!- FUNCTION: Scaffolding protein that may bring different proteins
CC       into adjacent positions at the cell membrane. May regulate protein
CC       targeting, cell polarity and integrity of tight junctions. May
CC       regulate the surface expression and/or function of ASIC3 in
CC       sensory neurons.
CC   -!- SUBUNIT: Forms a ternary complex with MPP5 and CRB1. Interacts
CC       with TJP3/ZO-3 and CLDN1/claudin-1. Component of a complex whose
CC       core is composed of ARHGAP17, AMOT, MPP5/PALS1, INADL/PATJ and
CC       PARD3/PAR3 (By similarity). Interacts with ASIC3, KCNJ10, KCNJ15,
CC       GRIN2A, GRIN2B, GRIN2C, GRIN2D, NLGN2, MPP7 and HTR2A. Isoform 2
CC       interacts with NRXN2. Directly interacts with HTR4. Interacts (via
CC       PDZ domain 8) with WWC1 (via the ADDV motif) (By similarity).
CC       Interacts with SLC6A4.
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction. Cell
CC       membrane; Peripheral membrane protein. Apical cell membrane;
CC       Peripheral membrane protein (By similarity). Cytoplasm,
CC       perinuclear region (By similarity). Note=Localizes to tight
CC       junctions in epithelial cells. Also found at the apical plasma
CC       membrane (By similarity). Localized in the paranodal region of
CC       myelinating Schwann cells.
CC   -!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Cytoplasm, perinuclear
CC       region. Note=Concentrates around the nucleus upon HTR2A
CC       coexpression. Cytoplasm, perinuclear region.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q63ZW7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q63ZW7-2; Sequence=VSP_014211;
CC       Name=3;
CC         IsoId=Q63ZW7-3; Sequence=VSP_014210, VSP_014216;
CC       Name=4;
CC         IsoId=Q63ZW7-4; Sequence=VSP_014210, VSP_014216, VSP_014217,
CC                                  VSP_014218;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q63ZW7-5; Sequence=VSP_014212, VSP_014213;
CC         Note=No experimental confirmation available;
CC       Name=6;
CC         IsoId=Q63ZW7-6; Sequence=VSP_014214, VSP_014215;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed exclusively in brain and kidney.
CC       Isoform 3 might be brain-specific. In brain, high levels are
CC       detected in the cerebellum, inferior colliculus, vestibular
CC       nucleus, facial nucleus and thalamus. Also detected in deep
CC       cerebellar nuclei, superior colliculus, dorsal transition zone,
CC       brain stem, as well as the glomerular and mitral cell layers of
CC       the olfactory bulb. Within the cerebellum it is expressed in both
CC       Purkinje and granule cell layers.
CC   -!- DOMAIN: The L27 domain (also called Maguk recruitment domain) is
CC       required for interaction with MPP5 and CRB3, and MPP5 localization
CC       to tight junctions (By similarity).
CC   -!- DOMAIN: The PDZ domain 6 mediates interaction with the C-terminus
CC       of TJP3 and is crucial for localization to the tight junctions.
CC       The PDZ domain 8 interacts with CLDN1 but is not required for
CC       proper localization (By similarity). The PDZ domain 2 of isoform 3
CC       mediates interactions with KCNJ10, KCNJ15, GRIN2B and NLGN2. The
CC       PDZ domain 3 of isoform 3 mediates interactions with KCNJ15,
CC       GRIN2A, GRIN2B, GRIN2C, GRIN2D and NRXN2. The PDZ domain 4 of
CC       isoform 3 mediates interaction with ASIC3.
CC   -!- SIMILARITY: Contains 1 L27 domain.
CC   -!- SIMILARITY: Contains 10 PDZ (DHR) domains.
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DR   EMBL; AF060539; AAC40148.1; -; mRNA.
DR   EMBL; AK077268; BAC36720.1; -; mRNA.
DR   EMBL; AL671229; CAM27361.1; -; Genomic_DNA.
DR   EMBL; BC037607; AAH37607.1; -; mRNA.
DR   EMBL; BC050846; AAH50846.1; -; mRNA.
DR   EMBL; BC057124; AAH57124.1; -; mRNA.
DR   EMBL; BC062194; AAH62194.1; -; mRNA.
DR   EMBL; BC082787; AAH82787.1; -; mRNA.
DR   IPI; IPI00177061; -.
DR   IPI; IPI00403927; -.
DR   IPI; IPI00471243; -.
DR   IPI; IPI00480255; -.
DR   IPI; IPI00607955; -.
DR   IPI; IPI00608053; -.
DR   RefSeq; NP_001005784.1; NM_001005784.1.
DR   RefSeq; NP_001005787.1; NM_001005787.1.
DR   RefSeq; NP_031730.1; NM_007704.2.
DR   RefSeq; NP_766284.2; NM_172696.2.
DR   UniGene; Mm.90218; -.
DR   ProteinModelPortal; Q63ZW7; -.
DR   SMR; Q63ZW7; 4-65, 116-473, 579-777, 1060-1798.
DR   MINT; MINT-1777910; -.
DR   STRING; Q63ZW7; -.
DR   PhosphoSite; Q63ZW7; -.
DR   PRIDE; Q63ZW7; -.
DR   Ensembl; ENSMUST00000030290; ENSMUSP00000030290; ENSMUSG00000061859.
DR   Ensembl; ENSMUST00000041284; ENSMUSP00000049176; ENSMUSG00000061859.
DR   Ensembl; ENSMUST00000102792; ENSMUSP00000099854; ENSMUSG00000061859.
DR   Ensembl; ENSMUST00000107030; ENSMUSP00000102645; ENSMUSG00000061859.
DR   GeneID; 12695; -.
DR   KEGG; mmu:12695; -.
DR   UCSC; uc008tub.1; mouse.
DR   UCSC; uc008tuc.1; mouse.
DR   UCSC; uc008tug.1; mouse.
DR   UCSC; uc008tuh.1; mouse.
DR   CTD; 12695; -.
DR   MGI; MGI:1277960; Inadl.
DR   GeneTree; ENSGT00570000078792; -.
DR   HOGENOM; HBG445379; -.
DR   HOVERGEN; HBG080134; -.
DR   InParanoid; Q63ZW7; -.
DR   OMA; FQAPLSV; -.
DR   PhylomeDB; Q63ZW7; -.
DR   NextBio; 281940; -.
DR   ArrayExpress; Q63ZW7; -.
DR   Bgee; Q63ZW7; -.
DR   CleanEx; MM_INADL; -.
DR   Genevestigator; Q63ZW7; -.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   InterPro; IPR004172; L27.
DR   InterPro; IPR015132; L27_2.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF09045; L27_2; 1.
DR   Pfam; PF00595; PDZ; 10.
DR   SMART; SM00569; L27; 1.
DR   SMART; SM00228; PDZ; 10.
DR   SUPFAM; SSF50156; PDZ; 10.
DR   PROSITE; PS51022; L27; 1.
DR   PROSITE; PS50106; PDZ; 10.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Cytoplasm;
KW   Membrane; Phosphoprotein; Repeat; Tight junction.
FT   CHAIN         1   1834       InaD-like protein.
FT                                /FTId=PRO_0000094593.
FT   DOMAIN        1     65       L27.
FT   DOMAIN      134    221       PDZ 1.
FT   DOMAIN      248    328       PDZ 2.
FT   DOMAIN      365    453       PDZ 3.
FT   DOMAIN      555    641       PDZ 4.
FT   DOMAIN      688    774       PDZ 5.
FT   DOMAIN     1074   1166       PDZ 6.
FT   DOMAIN     1245   1328       PDZ 7.
FT   DOMAIN     1472   1555       PDZ 8.
FT   DOMAIN     1568   1650       PDZ 9.
FT   DOMAIN     1709   1795       PDZ 10.
FT   MOD_RES     455    455       Phosphoserine.
FT   MOD_RES     524    524       Phosphoserine (By similarity).
FT   MOD_RES     647    647       Phosphoserine.
FT   VAR_SEQ       1   1222       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_014210.
FT   VAR_SEQ       1    573       Missing (in isoform 2).
FT                                /FTId=VSP_014211.
FT   VAR_SEQ     564    598       LLPIHTLRLGMEVDSFDGHHYISSVAPGGPVDTLN -> WM
FT                                LVLKAKAVPPSALHVVGSRAHIRRYKMALTAVF (in
FT                                isoform 5).
FT                                /FTId=VSP_014212.
FT   VAR_SEQ     599   1834       Missing (in isoform 5).
FT                                /FTId=VSP_014213.
FT   VAR_SEQ     951    975       MEETFGLDSRAPIPSSEGNGQHGRF -> VRLCDTATTCSP
FT                                LCPHTPRSCYFHS (in isoform 6).
FT                                /FTId=VSP_014214.
FT   VAR_SEQ     976   1834       Missing (in isoform 6).
FT                                /FTId=VSP_014215.
FT   VAR_SEQ    1223   1230       EDCALTDK -> MVHGGFPE (in isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_014216.
FT   VAR_SEQ    1792   1804       VADTNISAIATQL -> FRSMENQLAEADK (in
FT                                isoform 4).
FT                                /FTId=VSP_014217.
FT   VAR_SEQ    1805   1834       Missing (in isoform 4).
FT                                /FTId=VSP_014218.
FT   CONFLICT    740    740       V -> L (in Ref. 2; BAC36720).
FT   CONFLICT    986    986       S -> R (in Ref. 2; BAC36720).
SQ   SEQUENCE   1834 AA;  198517 MW;  177ADF8E12B82A30 CRC64;
     MPENPAAEKM QVLQVLDRLR GKLQEKGDTT QNEKLSAFYE TLKSPLFNQI LTLQQSIKQL
     KGQLSHIPSD CSANFDFSRK GLLVFTDGSI TNGNAQRPCS NVTASELLPW TQKSASEDFN
     SVIQQMAQGR HVEYIDIERP STGGLGFSVV ALRSQSLGLI DIFVKEVHPG SVADRDHRLK
     ENDQILAIND TPLDQNISHQ QAIALLQQAT GSLRLVVARE VGHTQGRAST SSADTTLPET
     VCWGHTEEVE LINDGSGLGF GIVGGKSSGV VVRTIVPGGL ADRDGRLQTG DHILKIGGTN
     VQGMTSEQVA QVLRNCGNSV RMLVARDPVG EIAVTPPTPV SLPVALPAVA TRTLDSDRSP
     FETYSVELVK KDGQSLGIRI VGYVGTAHPG EASGIYVKSI IPGSAAYHNG QIQVNDKIVA
     VDGVNIQGFA NQDVVEVLRN AGQVVHLTLV RRKTSLSASP FEHSSSRETV AEPPKVPERA
     GSPKPEANLS VEAEEIGERL DNLKNNTVQA LEKPDVYPEK VPGSPENELK SRWENLLGPD
     YEVMVATLDA QIADDEELQK YSKLLPIHTL RLGMEVDSFD GHHYISSVAP GGPVDTLNLL
     QPEDELLEVN GMQLYGKSRR EAVSFLKEVP PPFTLVCCRR LFDDEASVDE PRTMEPALLE
     AEVDHSVDVN IEDDDDGELA LWSPEVKTVE LVKDCKGLGF SILDYQDPLD PTRSVIVIRS
     LVADGVAERS GELLPGDRLV SVNEFSLDNA TLAEAVEVLK AVPPGVVHLG ICKPLVEDEK
     EERFSLHSNN NGDSSEPADA VHEIHSSLIL EAPQGFRDEP YLEELVDEPF LDLGKSLQFQ
     QKDVDSSSEA WEMHEFLSPP LDGRGEEREM LVDEEYELYQ DHLRAMESNP PPPHIREAAP
     ASPVLELQAG TQWLHANLSG GERLECHDAE SMMSAYPQEM QQYSYSTADM MEETFGLDSR
     APIPSSEGNG QHGRFDDMGH LHSLTSSSLD LGMMIPSDLQ GPGVLVDLPA VAQRREQEDL
     PLYRLPSARV VTKPSSHMGL VSSRHANAAC ELPEREEGEG EETPNFSHWG PPRIVEIFRE
     PNVSLGISIV GGQTVIKRLK NGEELKGIFI KQVLEDSPAG KTNALKTGDK ILEVSGVDLQ
     NASHAEAVEA IKSAGNPVVF VVQSLSSTPR VIPTVNNKGK TPAPNQDQNT QERKAKRHGT
     APPPMKLPPP YRAPSADMEG SEEDCALTDK KIRQRYADLP GELHIIELEK DKNGLGLSLA
     GNKDRSRMSI FVVGINPEGP AAADGRMRIG DELLEINNQI LYGRSHQNAS AIIKTAPTRV
     KLVFIRNEDA VSQMAVAPFP ELSHSPSPVE DLGGTELVSS EEESSVDAKH LPEPESSKPE
     DLSQVVDDNM VAEQQKESES PDSAACQIKQ QTYSTQVSSS SQDSPSSPAP LCQSAHADVT
     GSGNFQAPLP VDPAPLSVDP ATCPIVPGQE MIIEISKGRS GLGLSIVGGK DTPLDAIVIH
     EVYEEGAAAR DGRLWAGDQI LEVNGVDLRS SSHEEAITAL RQTPQKVRLV VYRDEAQYRD
     EENLEVFLVD LQKKTGRGLG LSIVGKRSGS GVFISDIVKG GAADLDGRLI RGDQILSVNG
     EDMRHASQET VATILKCVQG LVQLEIGRLR AGSWAASRKT SQNSQGDQHS AHSSCRPSFA
     PVITSLQNLV GTKRSSDPPQ KCTEEEPRTV EIIRELSDAL GISIAGGKGS PLGDIPIFIA
     MIQANGVAAR TQKLKVGDRI VSINGQPLDG LSHTDAVNLL KNAFGRIILQ VVADTNISAI
     ATQLEIMSAG SQLGSPTADR HPEDTEEQMQ RTAD
//
ID   RAB34_MOUSE             Reviewed;         259 AA.
AC   Q64008; Q8BHJ0; Q99P59; Q99P90;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   31-JAN-2002, sequence version 2.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Ras-related protein Rab-34;
DE   AltName: Full=Ras-related homolog;
DE   AltName: Full=Ras-related protein Rab-39;
DE   AltName: Full=Ras-related protein Rah;
GN   Name=Rab34; Synonyms=Rab39, Rah, Rah1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Hong W.;
RT   "Mouse Rab39 coding region (cDNA).";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Neuron;
RA   Hari M., Morimoto B.H., Asai D.J.;
RT   "Full length sequence of Rah, a novel member of the Rab family of
RT   small GTPases.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Sun P., Yamamoto H., Endo T.;
RT   "Rah, a Rab family small GTPase.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 52-259.
RC   TISSUE=Neuron;
RX   MEDLINE=92090719; PubMed=1752434;
RA   Morimoto B.H., Chuang C.-C., Koshland D.E. Jr.;
RT   "Molecular cloning of a member of a new class of low-molecular-weight
RT   GTP-binding proteins.";
RL   Genes Dev. 5:2386-2391(1991).
RN   [6]
RP   FUNCTION IN LYSOSOME REDISTRIBUTION, INTERACTION WITH RILP,
RP   MUTAGENESIS OF LYS-82, AND SUBCELLULAR LOCATION.
RX   PubMed=12475955; DOI=10.1091/mbc.E02-05-0280;
RA   Wang T., Hong W.;
RT   "Interorganellar regulation of lysosome positioning by the Golgi
RT   apparatus through Rab34 interaction with Rab-interacting lysosomal
RT   protein.";
RL   Mol. Biol. Cell 13:4317-4332(2002).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Protein transport. Involved in the redistribution of
CC       lysosomes to the peri-Golgi region.
CC   -!- SUBUNIT: Interacts with RILP.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus. Note=Associates
CC       with the Golgi complex.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR   EMBL; AF322068; AAK09398.1; -; mRNA.
DR   EMBL; AF327929; AAK11241.1; -; mRNA.
DR   EMBL; AB082927; BAC16803.1; -; mRNA.
DR   EMBL; BC038638; AAH38638.1; -; mRNA.
DR   EMBL; S72304; AAB20669.1; -; mRNA.
DR   IPI; IPI00130112; -.
DR   PIR; A41636; A41636.
DR   RefSeq; NP_001152954.1; NM_001159482.1.
DR   RefSeq; NP_258436.2; NM_033475.3.
DR   UniGene; Mm.275864; -.
DR   ProteinModelPortal; Q64008; -.
DR   SMR; Q64008; 50-221.
DR   STRING; Q64008; -.
DR   PhosphoSite; Q64008; -.
DR   PRIDE; Q64008; -.
DR   Ensembl; ENSMUST00000002128; ENSMUSP00000002128; ENSMUSG00000002059.
DR   Ensembl; ENSMUST00000108322; ENSMUSP00000103958; ENSMUSG00000002059.
DR   GeneID; 19376; -.
DR   KEGG; mmu:19376; -.
DR   CTD; 19376; -.
DR   MGI; MGI:104606; Rab34.
DR   GeneTree; ENSGT00600000084435; -.
DR   HOVERGEN; HBG106693; -.
DR   OrthoDB; EOG41NTMP; -.
DR   PhylomeDB; Q64008; -.
DR   NextBio; 296471; -.
DR   ArrayExpress; Q64008; -.
DR   Bgee; Q64008; -.
DR   CleanEx; MM_RAB34; -.
DR   CleanEx; MM_RAB39; -.
DR   Genevestigator; Q64008; -.
DR   GermOnline; ENSMUSG00000002059; Mus musculus.
DR   GO; GO:0005769; C:early endosome; IDA:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0001726; C:ruffle; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IDA:MGI.
DR   GO; GO:0006897; P:endocytosis; IDA:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Golgi apparatus; GTP-binding; Lipoprotein;
KW   Nucleotide-binding; Phosphoprotein; Prenylation; Protein transport;
KW   Transport.
FT   CHAIN         1    259       Ras-related protein Rab-34.
FT                                /FTId=PRO_0000121244.
FT   NP_BIND      59     66       GTP (By similarity).
FT   NP_BIND     107    111       GTP (By similarity).
FT   NP_BIND     166    169       GTP (By similarity).
FT   MOTIF        81     89       Effector region (By similarity).
FT   MOD_RES     241    241       Phosphoserine.
FT   LIPID       257    257       S-geranylgeranyl cysteine (Potential).
FT   LIPID       258    258       S-geranylgeranyl cysteine (Potential).
FT   MUTAGEN      82     82       K->Q: Abolishes interaction with RILP and
FT                                localization to the peri-Golgi region.
FT   MUTAGEN      82     82       K->Y: Does not abolish interaction with
FT                                RILP and localization to the peri-Golgi
FT                                region.
FT   CONFLICT     52     52       I -> N (in Ref. 5; AAB20669).
FT   CONFLICT    224    225       DV -> EL (in Ref. 3 and 4).
SQ   SEQUENCE   259 AA;  29101 MW;  158F5132F0DDE808 CRC64;
     MNILAPVRRD RVLAELPQCL KKEAALHVRK DFHPRVTCAC QEHRTGTVGF KISKVIVVGD
     LSVGKTCLIN RFCKDTFDKN YKATIGVDFE MERFEVLGVP FSLQLWDTAG QERFKCIAST
     YYRGAQAIII VFNLNDVASL EHTKQWLTDA LKENDPSNVL LFLVGSKKDL STPAQYSLME
     KDALKVAQEI KAEYWAVSSL TGENVREFFF RVAALTFEAN VLADVEKSGA RHIADVVRIN
     SDDKNLYLTA SKKKATCCP
//
ID   CRK_MOUSE               Reviewed;         304 AA.
AC   Q64010;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 106.
DE   RecName: Full=Adapter molecule crk;
DE   AltName: Full=Proto-oncogene c-Crk;
DE   AltName: Full=p38;
GN   Name=Crk; Synonyms=Crko;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CRK-I AND CRK-II).
RC   TISSUE=Liver;
RX   MEDLINE=94239744; PubMed=8183562;
RA   Ogawa S., Toyoshima H., Kozutsumi H., Hagiwara K., Sakai R.,
RA   Tanaka T., Hirano N., Mano H., Yazaki Y., Hirai H.;
RT   "The C-terminal SH3 domain of the mouse c-Crk protein negatively
RT   regulates tyrosine-phosphorylation of Crk associated p130 in rat 3Y1
RT   cells.";
RL   Oncogene 9:1669-1678(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CRK-II).
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   INTERACTION WITH REPS1.
RC   TISSUE=Muscle;
RX   MEDLINE=98058900; PubMed=9395447; DOI=10.1074/jbc.272.50.31230;
RA   Yamaguchi A., Urano T., Goi T., Feig L.A.;
RT   "An eps homology (EH) domain protein that binds to the ral-GTPase
RT   target, RalBP1.";
RL   J. Biol. Chem. 272:31230-31234(1997).
RN   [4]
RP   INTERACTION WITH DDEF1/ASAP1.
RX   MEDLINE=99038209; PubMed=9819391;
RA   Brown M.T., Andrade J., Radhakrishna H., Donaldson J.G., Cooper J.A.,
RA   Randazzo P.A.;
RT   "ASAP1, a phospholipid-dependent arf GTPase-activating protein that
RT   associates with and is phosphorylated by Src.";
RL   Mol. Cell. Biol. 18:7038-7051(1998).
RN   [5]
RP   INTERACTION WITH DOCK3.
RC   TISSUE=Brain;
RX   MEDLINE=20312861; PubMed=10854253;
RX   DOI=10.1046/j.1471-4159.2000.0750109.x;
RA   Kashiwa A., Yoshida H., Lee S., Paladino T., Liu Y., Chen Q.,
RA   Dargusch R., Schubert D., Kimura H.;
RT   "Isolation and characterization of novel presenilin binding protein.";
RL   J. Neurochem. 75:109-116(2000).
RN   [6]
RP   INTERACTION WITH CBLB.
RX   PubMed=12842890; DOI=10.1074/jbc.M300664200;
RA   Liu J., DeYoung S.M., Hwang J.B., O'Leary E.E., Saltiel A.R.;
RT   "The roles of Cbl-b and c-Cbl in insulin-stimulated glucose
RT   transport.";
RL   J. Biol. Chem. 278:36754-36762(2003).
RN   [7]
RP   PHOSPHORYLATION AT TYR-221, AND INTERACTION WITH ABL1.
RX   PubMed=8194526;
RA   Feller S.M., Knudsen B., Hanafusa H.;
RT   "c-Abl kinase regulates the protein binding activity of c-Crk.";
RL   EMBO J. 13:2341-2351(1994).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-221, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 134-190.
RX   MEDLINE=95253821; PubMed=7735837; DOI=10.1016/S0969-2126(01)00151-4;
RA   Wu X., Knudsen B., Feller S.M., Zheng J., Sali A., Cowburn D.,
RA   Hanafusa H., Kuriyan J.;
RT   "Structural basis for the specific interaction of lysine-containing
RT   proline-rich peptides with the N-terminal SH3 domain of c-Crk.";
RL   Structure 3:215-226(1995).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 133-191.
RX   MEDLINE=99069628; PubMed=9851931; DOI=10.1126/science.282.5396.2088;
RA   Nguyen J.T., Turck C.W., Cohen F.E., Zuckermann R.N., Lim W.A.;
RT   "Exploiting the basis of proline recognition by SH3 and WW domains:
RT   design of N-substituted inhibitors.";
RL   Science 282:2088-2092(1998).
CC   -!- FUNCTION: The Crk-I and Crk-II forms differ in their biological
CC       activities. Crk-II has less transforming activity than Crk-I. Crk-
CC       II mediates attachment-induced MAPK8 activation, membrane ruffling
CC       and cell motility in a Rac-dependent manner.
CC   -!- SUBUNIT: Interacts with ABL1, C3G, SOS, MAP4K1 and MAPK8 via its
CC       first SH3 domain. Interacts with BCAR1, CBL, CBLB, PXN, IRS4 and
CC       GAB1 via its SH2 domain upon stimulus-induced tyrosine
CC       phosphorylation. Interacts with several tyrosine-phosphorylated
CC       growth factor receptors such as EGFR, PDGFR and INSR via its SH2
CC       domain. Interacts with DOCK1, DOCK4, C3G and EPS15 via its SH3
CC       domain. Interacts with SHB (By similarity). Interacts with PEAK1
CC       (By similarity). Interacts with DOCK3. Interacts with REPS1 and
CC       DDEF1/ASAP1 via its SH3 domain. Interacts with FASLG (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By
CC       similarity). Note=Translocated to the plasma membrane upon cell
CC       adhesion (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Crk-II;
CC         IsoId=Q64010-1; Sequence=Displayed;
CC       Name=Crk-I;
CC         IsoId=Q64010-2; Sequence=VSP_004174;
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- DOMAIN: The C-terminal SH3 domain function as a negative modulator
CC       for transformation and the N-terminal SH3 domain appears to
CC       function as a positive regulator for transformation (By
CC       similarity).
CC   -!- DOMAIN: The SH2 domain mediates interaction with SHB.
CC   -!- PTM: Phosphorylated on Tyr-221 upon cell adhesion. Results in the
CC       negative regulation of the association with SH2- and SH3-binding
CC       partners, possibly by the formation of an intramolecular
CC       interaction of phosphorylated Tyr-221 with the SH2 domain. This
CC       leads finally to the down-regulation of the Crk signaling pathway.
CC   -!- SIMILARITY: Belongs to the CRK family.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
CC   -!- SIMILARITY: Contains 2 SH3 domains.
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DR   EMBL; S72408; AAB30755.1; -; mRNA.
DR   EMBL; AK028488; BAC25976.1; -; mRNA.
DR   IPI; IPI00307991; -.
DR   IPI; IPI00345994; -.
DR   RefSeq; NP_598417.2; NM_133656.3.
DR   UniGene; Mm.280125; -.
DR   PDB; 1B07; X-ray; 2.50 A; A=134-190.
DR   PDB; 1CKA; X-ray; 1.50 A; A=134-190.
DR   PDB; 1CKB; X-ray; 1.90 A; A=134-190.
DR   PDB; 1JU5; NMR; -; B=217-228.
DR   PDB; 1M30; NMR; -; A=134-190.
DR   PDB; 1M3A; NMR; -; A=136-190.
DR   PDB; 1M3B; NMR; -; A=136-190.
DR   PDB; 1M3C; NMR; -; A=134-190.
DR   PDB; 2GGR; NMR; -; A=230-304.
DR   PDBsum; 1B07; -.
DR   PDBsum; 1CKA; -.
DR   PDBsum; 1CKB; -.
DR   PDBsum; 1JU5; -.
DR   PDBsum; 1M30; -.
DR   PDBsum; 1M3A; -.
DR   PDBsum; 1M3B; -.
DR   PDBsum; 1M3C; -.
DR   PDBsum; 2GGR; -.
DR   ProteinModelPortal; Q64010; -.
DR   SMR; Q64010; 1-304.
DR   STRING; Q64010; -.
DR   PhosphoSite; Q64010; -.
DR   PRIDE; Q64010; -.
DR   Ensembl; ENSMUST00000017920; ENSMUSP00000017920; ENSMUSG00000017776.
DR   GeneID; 12928; -.
DR   KEGG; mmu:12928; -.
DR   UCSC; uc007ker.1; mouse.
DR   CTD; 12928; -.
DR   MGI; MGI:88508; Crk.
DR   HOGENOM; HBG314739; -.
DR   HOVERGEN; HBG105616; -.
DR   InParanoid; Q64010; -.
DR   OrthoDB; EOG4WWRK5; -.
DR   PhylomeDB; Q64010; -.
DR   NextBio; 282592; -.
DR   ArrayExpress; Q64010; -.
DR   Bgee; Q64010; -.
DR   CleanEx; MM_CRK; -.
DR   Genevestigator; Q64010; -.
DR   GermOnline; ENSMUSG00000017776; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045309; F:protein phosphorylated amino acid binding; IDA:MGI.
DR   GO; GO:0005070; F:SH3/SH2 adaptor activity; IPI:BHF-UCL.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 2.
DR   SUPFAM; SSF50044; SH3; 2.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW   Cytoplasm; Membrane; Phosphoprotein; Proto-oncogene; Repeat;
KW   SH2 domain; SH3 domain.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    304       Adapter molecule crk.
FT                                /FTId=PRO_0000079352.
FT   DOMAIN       13    118       SH2.
FT   DOMAIN      132    192       SH3 1.
FT   DOMAIN      237    296       SH3 2.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      41     41       Phosphoserine.
FT   MOD_RES      42     42       Phosphothreonine.
FT   MOD_RES      74     74       Phosphoserine (By similarity).
FT   MOD_RES      83     83       Phosphoserine (By similarity).
FT   MOD_RES     136    136       Phosphotyrosine (By similarity).
FT   MOD_RES     221    221       Phosphotyrosine.
FT   MOD_RES     239    239       Phosphotyrosine (By similarity).
FT   MOD_RES     251    251       Phosphotyrosine (By similarity).
FT   VAR_SEQ     205    304       Missing (in isoform Crk-I).
FT                                /FTId=VSP_004174.
FT   STRAND      136    141
FT   STRAND      158    163
FT   STRAND      165    173
FT   STRAND      179    183
FT   HELIX       184    186
FT   STRAND      238    244
FT   STRAND      252    254
FT   STRAND      262    268
FT   STRAND      271    273
FT   STRAND      275    279
FT   STRAND      282    286
FT   HELIX       288    290
FT   STRAND      291    294
SQ   SEQUENCE   304 AA;  33815 MW;  5491896FC7A89065 CRC64;
     MAGNFDSEER SSWYWGRLSR QEAVALLQGQ RHGVFLVRDS STSPGDYVLS VSENSRVSHY
     IINSSGPRPP VPPSPAQPPP GVSPSRLRIG DQEFDSLPAL LEFYKIHYLD TTTLIEPVAR
     SRQGSGVILR QEEAEYVRAL FDFNGNDEED LPFKKGDILR IRDKPEEQWW NAEDSEGKRG
     MIPVPYVEKY RPASASVSAL IGGNQEGSHP QPLGGPEPGP YAQPSVNTPL PNLQNGPIYA
     RVIQKRVPNA YDKTALALEV GELVKVTKIN VSGQWEGECN GKRGHFPFTH VRLLDQQNPD
     EDFS
//
ID   GLRA1_MOUSE             Reviewed;         457 AA.
AC   Q64018; Q5NCT8; Q64019; Q9R0Y6; Q9R0Y7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 2.
DT   08-FEB-2011, entry version 105.
DE   RecName: Full=Glycine receptor subunit alpha-1;
DE   AltName: Full=Glycine receptor 48 kDa subunit;
DE   AltName: Full=Glycine receptor strychnine-binding subunit;
DE   Flags: Precursor;
GN   Name=Glra1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), AND VARIANT SPD SER-80.
RX   MEDLINE=95004575; PubMed=7920629; DOI=10.1038/ng0694-131;
RA   Ryan S.G., Buckwalter M.S., Lynch J.W., Handford C.A., Segura L.,
RA   Shiang R., Wasmuth J.J., Camper S.A., Schofield P., O'Connell P.;
RT   "A missense mutation in the gene encoding the alpha 1 subunit of the
RT   inhibitory glycine receptor in the spasmodic mouse.";
RL   Nat. Genet. 7:131-135(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=BALB/c;
RX   MEDLINE=94132024; PubMed=7507926;
RA   Matzenbach B., Maulet Y., Sefton L., Courtier B., Avner P.,
RA   Guenet J.-L., Betz H.;
RT   "Structural analysis of mouse glycine receptor alpha subunit genes.
RT   Identification and chromosomal localization of a novel variant.";
RL   J. Biol. Chem. 269:2607-2612(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- FUNCTION: The glycine receptor is a neurotransmitter-gated ion
CC       channel. Binding of glycine to its receptor increases the chloride
CC       conductance and thus produces hyperpolarization (inhibition of
CC       neuronal firing).
CC   -!- SUBUNIT: Pentamer composed of alpha and beta subunits.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane; Multi-pass membrane protein. Cell membrane; Multi-pass
CC       membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a; Synonyms=Long;
CC         IsoId=Q64018-1; Sequence=Displayed;
CC       Name=b; Synonyms=Short;
CC         IsoId=Q64018-2; Sequence=VSP_000080;
CC   -!- DISEASE: Note=Defects in Glra1 are the cause of the spasmodic
CC       (spd) phenotype, a mouse mutant which resembles to the human
CC       neurological disease, hyperekplexia (or startle disease (STHE)).
CC   -!- MISCELLANEOUS: The alpha subunit binds strychnine.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
CC       family. Glycine receptor (TC 1.A.9.3) subfamily. GLRA1 sub-
CC       subfamily.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; S73717; AAB32157.2; -; mRNA.
DR   EMBL; S73718; AAB32158.2; -; mRNA.
DR   EMBL; X75832; CAB52398.1; -; Genomic_DNA.
DR   EMBL; X75833; CAB52398.1; JOINED; Genomic_DNA.
DR   EMBL; X75834; CAB52398.1; JOINED; Genomic_DNA.
DR   EMBL; X75835; CAB52398.1; JOINED; Genomic_DNA.
DR   EMBL; X75836; CAB52398.1; JOINED; Genomic_DNA.
DR   EMBL; X75837; CAB52398.1; JOINED; Genomic_DNA.
DR   EMBL; X75838; CAB52398.1; JOINED; Genomic_DNA.
DR   EMBL; X75839; CAB52398.1; JOINED; Genomic_DNA.
DR   EMBL; X75840; CAB52398.1; JOINED; Genomic_DNA.
DR   EMBL; X75832; CAB52399.1; -; Genomic_DNA.
DR   EMBL; X75833; CAB52399.1; JOINED; Genomic_DNA.
DR   EMBL; X75834; CAB52399.1; JOINED; Genomic_DNA.
DR   EMBL; X75835; CAB52399.1; JOINED; Genomic_DNA.
DR   EMBL; X75836; CAB52399.1; JOINED; Genomic_DNA.
DR   EMBL; X75837; CAB52399.1; JOINED; Genomic_DNA.
DR   EMBL; X75838; CAB52399.1; JOINED; Genomic_DNA.
DR   EMBL; X75839; CAB52399.1; JOINED; Genomic_DNA.
DR   EMBL; X75840; CAB52399.1; JOINED; Genomic_DNA.
DR   EMBL; AL596207; CAI35359.1; -; Genomic_DNA.
DR   IPI; IPI00405549; -.
DR   IPI; IPI00466207; -.
DR   PIR; C49970; C49970.
DR   UniGene; Mm.89320; -.
DR   ProteinModelPortal; Q64018; -.
DR   SMR; Q64018; 277-337.
DR   STRING; Q64018; -.
DR   PhosphoSite; Q64018; -.
DR   PRIDE; Q64018; -.
DR   Ensembl; ENSMUST00000075603; ENSMUSP00000075032; ENSMUSG00000000263.
DR   Ensembl; ENSMUST00000102716; ENSMUSP00000099777; ENSMUSG00000000263.
DR   NMPDR; fig|10090.3.peg.23704; -.
DR   UCSC; uc007izn.1; mouse.
DR   UCSC; uc007izo.1; mouse.
DR   MGI; MGI:95747; Glra1.
DR   GeneTree; ENSGT00550000074453; -.
DR   HOGENOM; HBG506497; -.
DR   HOVERGEN; HBG051707; -.
DR   InParanoid; Q64018; -.
DR   OMA; KGANNSN; -.
DR   ArrayExpress; Q64018; -.
DR   Bgee; Q64018; -.
DR   CleanEx; MM_GLRA1; -.
DR   Genevestigator; Q64018; -.
DR   GermOnline; ENSMUSG00000000263; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005887; C:integral to plasma membrane; ISS:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR   GO; GO:0016934; F:extracellular-glycine-gated chloride channel activity; ISS:UniProtKB.
DR   GO; GO:0016594; F:glycine binding; ISS:UniProtKB.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0030977; F:taurine binding; ISS:UniProtKB.
DR   GO; GO:0007340; P:acrosome reaction; IMP:MGI.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0006936; P:muscle contraction; ISS:UniProtKB.
DR   GO; GO:0051970; P:negative regulation of transmission of nerve impulse; ISS:UniProtKB.
DR   GO; GO:0050884; P:neuromuscular process controlling posture; IMP:MGI.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; ISS:UniProtKB.
DR   GO; GO:0001508; P:regulation of action potential; IMP:MGI.
DR   GO; GO:0060080; P:regulation of inhibitory postsynaptic membrane potential; IMP:MGI.
DR   GO; GO:0002087; P:regulation of respiratory gaseous exchange by neurological system process; IMP:MGI.
DR   GO; GO:0060013; P:righting reflex; IMP:MGI.
DR   GO; GO:0001964; P:startle response; ISS:UniProtKB.
DR   GO; GO:0060012; P:synaptic transmission, glycinergic; IMP:MGI.
DR   GO; GO:0007601; P:visual perception; IMP:MGI.
DR   InterPro; IPR006028; GABAA_rcpt.
DR   InterPro; IPR008127; Glycine_rcpt_A.
DR   InterPro; IPR008128; Glycine_rcpt_A1.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   Gene3D; G3DSA:2.70.170.10; Neur_chan_lig_bd; 1.
DR   PANTHER; PTHR18945; Neur_channel; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 2.
DR   PRINTS; PR00253; GABAARECEPTR.
DR   PRINTS; PR01673; GLYRALPHA.
DR   PRINTS; PR01674; GLYRALPHA1.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF90112; Neu_channel_TM; 1.
DR   SUPFAM; SSF63712; Neur_chan_LBD; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Chloride;
KW   Chloride channel; Disease mutation; Disulfide bond; Glycoprotein;
KW   Ion transport; Ionic channel; Ligand-gated ion channel; Membrane;
KW   Postsynaptic cell membrane; Receptor; Signal; Synapse; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     28       By similarity.
FT   CHAIN        29    457       Glycine receptor subunit alpha-1.
FT                                /FTId=PRO_0000000413.
FT   TOPO_DOM     29    247       Extracellular (Probable).
FT   TRANSMEM    248    274       Helical; (Probable).
FT   TRANSMEM    281    298       Helical; (Probable).
FT   TRANSMEM    313    336       Helical; (Probable).
FT   TOPO_DOM    337    428       Cytoplasmic (Probable).
FT   TRANSMEM    429    446       Helical; (Probable).
FT   REGION      225    230       Strychnine-binding (By similarity).
FT   CARBOHYD     66     66       N-linked (GlcNAc...) (Probable).
FT   DISULFID    166    180       By similarity.
FT   DISULFID    226    237       By similarity.
FT   VAR_SEQ     354    361       Missing (in isoform b).
FT                                /FTId=VSP_000080.
FT   VARIANT      80     80       A -> S (in spd).
FT   CONFLICT     84     84       M -> I (in Ref. 2; CAB52398/CAB52399).
FT   CONFLICT    426    429       ISRI -> NISH (in Ref. 2; CAB52398/
FT                                CAB52399).
SQ   SEQUENCE   457 AA;  52657 MW;  29268DC4991A6E20 CRC64;
     MYSFNTLRFY LWETIVFFSL AASKEAEAAR SAPKPMSPSD FLDKLMGRTS GYDARIRPNF
     KGPPVNVSCN IFINSFGSIA ETTMDYRVNI FLRQQWNDPR LAYNEYPDDS LDLDPSMLDS
     IWKPDLFFAN EKGAHFHEIT TDNKLLRISR NGNVLYSIRI TLTLACPMDL KNFPMDVQTC
     IMQLESFGYT MNDLIFEWQE QGAVQVADGL TLPQFILKEE KDLRYCTKHY NTGKFTCIEA
     RFHLERQMGY YLIQMYIPSL LIVILSWISF WINMDAAPAR VGLGITTVLT MTTQSSGSRA
     SLPKVSYVKA IDIWMAVCLL FVFSALLEYA AVNFVSRQHK ELLRFRRKRR HHKSPMLNLF
     QDDEGGEGRF NFSAYGMGPA CLQAKDGISV KGANNNNTTN PPPAPSKSPE EMRKLFIQRA
     KKIDKISRIG FPMAFLIFNM FYWIIYKIVR REDVHNK
//
ID   TFE3_MOUSE              Reviewed;         572 AA.
AC   Q64092; A2AEW3; A2AEW4; Q3U8H0; Q3UMV4; Q3UT52; Q7TNC1; Q8BN29;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Transcription factor E3;
GN   Name=Tfe3; Synonyms=Tcfe3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Egg, Lung, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 127-572.
RX   MEDLINE=92123207; PubMed=1732746;
RA   Roman C., Matera A.G., Cooper C., Artandi S., Blain S., Ward D.C.,
RA   Calame K.;
RT   "mTFE3, an X-linked transcriptional activator containing basic helix-
RT   loop-helix and zipper domains, utilizes the zipper to stabilize both
RT   DNA binding and multimerization.";
RL   Mol. Cell. Biol. 12:817-827(1992).
RN   [5]
RP   FUNCTION, DNA-BINDING, AND TISSUE SPECIFICITY.
RX   PubMed=16936731; DOI=10.1038/ni1378;
RA   Huan C., Kelly M.L., Steele R., Shapira I., Gottesman S.R.S.,
RA   Roman C.A.J.;
RT   "Transcription factors TFE3 and TFEB are critical for CD40 ligand
RT   expression and thymus-dependent humoral immunity.";
RL   Nat. Immunol. 7:1082-1091(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-565, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Transcription factor that specifically recognizes and
CC       binds E-box sequences (3'-CANNTG-5'). Efficient DNA-binding
CC       requires dimerization with itself or with another MiT/TFE family
CC       member such as TFEB or MITF. In association with TFEB, activates
CC       the expression of CD40L in T-cells, thereby playing a role in T-
CC       cell-dependent antibody responses in activated CD4(+) T-cells and
CC       thymus-dependent humoral immunity. Specifically recognizes the
CC       MUE3 box, a subset of E-boxes, present in the immunoglobulin
CC       enhancer. It also binds very well to a USF/MLTF site.
CC   -!- SUBUNIT: Homodimer and heterodimer; with TFEB or MITF (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q64092-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q64092-2; Sequence=VSP_022143;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q64092-3; Sequence=VSP_022143, VSP_022144;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q64092-4; Sequence=VSP_022144;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- PTM: Sumoylated; does not affect dimerization with MITF (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the MiT/TFE family.
CC   -!- SIMILARITY: Contains 1 basic helix-loop-helix (bHLH) domain.
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DR   EMBL; AK089762; BAC40955.1; -; mRNA.
DR   EMBL; AK139756; BAE24128.1; -; mRNA.
DR   EMBL; AK144657; BAE25994.1; -; mRNA.
DR   EMBL; AK152221; BAE31048.1; -; mRNA.
DR   EMBL; AL671995; CAM13597.1; -; Genomic_DNA.
DR   EMBL; AL671995; CAM13598.1; -; Genomic_DNA.
DR   EMBL; BC056358; AAH56358.1; -; mRNA.
DR   EMBL; BC063047; AAH63047.1; -; mRNA.
DR   EMBL; S76673; AAB21130.1; -; mRNA.
DR   IPI; IPI00272774; -.
DR   IPI; IPI00380308; -.
DR   IPI; IPI00653132; -.
DR   IPI; IPI00761192; -.
DR   PIR; A42029; A42029.
DR   RefSeq; NP_001098666.1; NM_001105196.1.
DR   RefSeq; NP_766060.2; NM_172472.3.
DR   UniGene; Mm.249142; -.
DR   ProteinModelPortal; Q64092; -.
DR   SMR; Q64092; 343-422.
DR   STRING; Q64092; -.
DR   PhosphoSite; Q64092; -.
DR   PRIDE; Q64092; -.
DR   Ensembl; ENSMUST00000077680; ENSMUSP00000076864; ENSMUSG00000000134.
DR   Ensembl; ENSMUST00000079542; ENSMUSP00000078498; ENSMUSG00000000134.
DR   GeneID; 209446; -.
DR   KEGG; mmu:209446; -.
DR   UCSC; uc009smg.1; mouse.
DR   UCSC; uc009smh.1; mouse.
DR   UCSC; uc009smi.1; mouse.
DR   UCSC; uc009smk.1; mouse.
DR   CTD; 209446; -.
DR   MGI; MGI:98511; Tcfe3.
DR   HOGENOM; HBG716774; -.
DR   HOVERGEN; HBG006768; -.
DR   InParanoid; Q64092; -.
DR   OrthoDB; EOG4DV5MG; -.
DR   NextBio; 372667; -.
DR   ArrayExpress; Q64092; -.
DR   Bgee; Q64092; -.
DR   CleanEx; MM_TCFE3; -.
DR   Genevestigator; Q64092; -.
DR   GermOnline; ENSMUSG00000000134; Mus musculus.
DR   GO; GO:0005667; C:transcription factor complex; IC:MGI.
DR   GO; GO:0010843; F:promoter binding; IDA:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0030528; F:transcription regulator activity; IEA:InterPro.
DR   GO; GO:0006959; P:humoral immune response; IMP:UniProtKB.
DR   GO; GO:0010552; P:positive regulation of gene-specific transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   GO; GO:0045670; P:regulation of osteoclast differentiation; IGI:MGI.
DR   InterPro; IPR021802; DUF3371.
DR   InterPro; IPR011598; HLH_DNA-bd.
DR   InterPro; IPR001092; HLH_DNA-bd_dom.
DR   Gene3D; G3DSA:4.10.280.10; HLH_DNA_bd; 1.
DR   Pfam; PF11851; DUF3371; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; HLH_basic; 1.
DR   PROSITE; PS50888; HLH; 1.
PE   1: Evidence at protein level;
KW   Activator; Adaptive immunity; Alternative splicing; DNA-binding;
KW   Immunity; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN         1    572       Transcription factor E3.
FT                                /FTId=PRO_0000127472.
FT   DOMAIN      359    399       Helix-loop-helix motif.
FT   DOMAIN      408    429       Leucine-zipper.
FT   DNA_BIND    343    358       Basic motif.
FT   REGION      259    270       Strong transcription activation domain
FT                                (Potential).
FT   MOD_RES     553    553       Phosphoserine (By similarity).
FT   MOD_RES     565    565       Phosphoserine.
FT   VAR_SEQ       1    105       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_022143.
FT   VAR_SEQ     260    294       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_022144.
FT   CONFLICT     73     73       F -> S (in Ref. 1; BAE24128/BAE25994).
FT   CONFLICT    127    131       QERRE -> TSGTR (in Ref. 4; AAB21130).
FT   CONFLICT    143    143       S -> G (in Ref. 1; BAE25994).
FT   CONFLICT    558    558       K -> N (in Ref. 4; AAB21130).
FT   CONFLICT    568    568       M -> I (in Ref. 4; AAB21130).
SQ   SEQUENCE   572 AA;  61536 MW;  DAB0487EC0F6E92D CRC64;
     MSHAAEPARD AVEASAEGPR AVFLLLEERR PAESAQLLSL NSLLPESGIV ADIELENILD
     PDSFYELKSQ PLFLRSSLPI SLQATPTTPA TLSASSSAGG SRTPAMSSSS SRVLLRQQLM
     RAQAQEQERR ERREQAAAAP FPSPAPASPA ISVIGVSAGG HTLSRPPPAQ VPREVLKVQT
     HLENPTRYHL QQARRQQVKQ YLSTTLGPKL ASQALTPPPG PSSAQPLPAP ETAHATGPTG
     SAPNSPMALL TIGSSSEKEI DDVIDEIISL ESSYNDEMLS YLPGGTAGLQ LPSTLPVSGN
     LLDVYSSQGV ATPAITVSNS CPAELPNIKR EISETEAKAL LKERQKKDNH NLIERRRRFN
     INDRIKELGT LIPKSNDPEM RWNKGTILKA SVDYIRKLQK EQQRSKDLES RQRSLEQANR
     SLQLRIQELE LQAQIHGLPV PPNPGLLSLT TSSVSDSLKP EQLDIEEEGR PSTTFHVSGG
     PAQNAPPQQP PAPPSDALLD LHFPSDHLGD LGDPFHLGLE DILMEEEGMV GGLSGGALSP
     LRAASDPLLS SVSPAVSKAS SRRSSFSMEE ES
//
ID   Q640L6_MOUSE            Unreviewed;       389 AA.
AC   Q640L6;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   SubName: Full=Activating transcription factor 2;
DE   SubName: Full=Atf2 protein;
GN   Name=Atf2; ORFNames=RP23-290B1.2-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Head;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Dunn M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RA   Tracey A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the bZIP family.
CC   -!- SIMILARITY: Contains 1 bZIP domain.
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DR   EMBL; BC082596; AAH82596.1; -; mRNA.
DR   EMBL; AL844581; CAM15304.1; -; Genomic_DNA.
DR   EMBL; AL845523; CAM15304.1; JOINED; Genomic_DNA.
DR   EMBL; AL845523; CAM19860.1; -; Genomic_DNA.
DR   EMBL; AL844581; CAM19860.1; JOINED; Genomic_DNA.
DR   IPI; IPI00230233; -.
DR   RefSeq; NP_001020264.1; NM_001025093.1.
DR   UniGene; Mm.209903; -.
DR   UniGene; Mm.480355; -.
DR   ProteinModelPortal; Q640L6; -.
DR   SMR; Q640L6; 1-38, 238-298.
DR   STRING; Q640L6; -.
DR   PRIDE; Q640L6; -.
DR   Ensembl; ENSMUST00000112016; ENSMUSP00000107647; ENSMUSG00000027104.
DR   GeneID; 11909; -.
DR   KEGG; mmu:11909; -.
DR   NMPDR; fig|10090.3.peg.6156; -.
DR   UCSC; uc008kdh.1; mouse.
DR   CTD; 11909; -.
DR   MGI; MGI:109349; Atf2.
DR   HOVERGEN; HBG004300; -.
DR   NextBio; 461420; -.
DR   ArrayExpress; Q640L6; -.
DR   Bgee; Q640L6; -.
DR   Genevestigator; Q640L6; -.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0001077; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0060612; P:adipose tissue development; IGI:MGI.
DR   GO; GO:0045444; P:fat cell differentiation; IGI:MGI.
DR   GO; GO:0003151; P:outflow tract morphogenesis; IMP:MGI.
DR   GO; GO:0032915; P:positive regulation of transforming growth factor-beta2 production; IMP:MGI.
DR   InterPro; IPR011616; bZIP_1.
DR   InterPro; IPR004827; TF_bZIP.
DR   InterPro; IPR016378; TF_cAMP-dep.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 1.
DR   Pfam; PF00170; bZIP_1; 1.
DR   PIRSF; PIRSF003153; ATF2_CRE-BP1; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SMART; SM00355; ZnF_C2H2; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Nucleus.
SQ   SEQUENCE   389 AA;  42345 MW;  770AD65EA6114F10 CRC64;
     MSDDKPFLCT APGCGQRFTN EDHLAVHKHK HEMTLKFGPA RNDSVIVADQ TPTPTRFLKN
     CEEVGLFNEL ASPFENEFKK ASEDDIKKMP LDLSPLATPI IRSKIEEPSV VETTHQDSPL
     PHPESTTSDE KLVRPVTMVP SVPGIPGPSS PQPVQSEAKM RLKAALTQQH PPVTNGDTVK
     GHGSGLVRTQ SEESRPQSLQ QPATSTTETP ASPAHTTPQT QNTSGRRRRA ANEDPDEKRR
     KFLERNRAAA SRCRQKRKVW VQSLEKKAED LSSLNGQLQS EVTLLRNEVA QLKQLLLAHK
     DCPVTAMQKK SGYHTADKDD SSEDLSVPSS PHTEAIQHSS VSTSNGVSST SKAEAVATSV
     LTQMADQSTE PALSQIVMAP PSQAQPSGS
//
ID   AR13B_MOUSE             Reviewed;         427 AA.
AC   Q640N2;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=ADP-ribosylation factor-like protein 13B;
DE   AltName: Full=ADP-ribosylation factor-like protein 2-like 1;
DE            Short=ARL2-like protein 1;
GN   Name=Arl13b; Synonyms=Arl2l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
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DR   EMBL; BC082574; AAH82574.1; -; mRNA.
DR   IPI; IPI00137109; -.
DR   RefSeq; NP_080853.3; NM_026577.3.
DR   UniGene; Mm.96833; -.
DR   HSSP; Q9D0J4; 1KSH.
DR   ProteinModelPortal; Q640N2; -.
DR   SMR; Q640N2; 8-195.
DR   STRING; Q640N2; -.
DR   PhosphoSite; Q640N2; -.
DR   PRIDE; Q640N2; -.
DR   Ensembl; ENSMUST00000089289; ENSMUSP00000086703; ENSMUSG00000022911.
DR   Ensembl; ENSMUST00000114319; ENSMUSP00000109958; ENSMUSG00000022911.
DR   GeneID; 68146; -.
DR   KEGG; mmu:68146; -.
DR   UCSC; uc007zpu.1; mouse.
DR   CTD; 68146; -.
DR   MGI; MGI:1915396; Arl13b.
DR   eggNOG; roNOG05428; -.
DR   HOGENOM; HBG715396; -.
DR   HOVERGEN; HBG060221; -.
DR   InParanoid; Q640N2; -.
DR   OrthoDB; EOG441QBW; -.
DR   NextBio; 326526; -.
DR   ArrayExpress; Q640N2; -.
DR   Bgee; Q640N2; -.
DR   CleanEx; MM_ARL13B; -.
DR   Genevestigator; Q640N2; -.
DR   GermOnline; ENSMUSG00000022911; Mus musculus.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007368; P:determination of left/right symmetry; IMP:MGI.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
DR   InterPro; IPR006689; ARF/SAR.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   PANTHER; PTHR11711; ARF/SAR; 1.
DR   Pfam; PF00025; Arf; 1.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51417; ARF; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; GTP-binding; Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1    427       ADP-ribosylation factor-like protein 13B.
FT                                /FTId=PRO_0000251138.
FT   NP_BIND      28     35       GTP (By similarity).
FT   NP_BIND      71     75       GTP (By similarity).
FT   NP_BIND     130    133       GTP (By similarity).
FT   COILED      194    285       Potential.
FT   COMPBIAS    371    379       Poly-Pro.
FT   MOD_RES     328    328       Phosphoserine.
SQ   SEQUENCE   427 AA;  48135 MW;  9E2E021A56999AAC CRC64;
     MFSLMANCCN LFKRWREPVR KVTLVMVGLD NAGKTATAKG IQGEHPEDVA PTVGFSKIDL
     RQGKFQVTIF DLGGGKRIRG IWKNYYAESY GVIFVVDSSD EERMEETKET MSEVLRHPRI
     SGKPILVLAN KQDKEGALGE ADVIECLSLE KLVNEHKCLC QIEPCSAVLG YGKKIDKSIK
     KGLYWLLHII AKDFDALSER IQKDTTEQRA LEEQEKRERA ERVRKLREER EREQTELDGT
     SGLAEIDSGP VLANPFQPIA AVIIENEKKQ EKEKKKQTVE KDSDVGLLEH KVEPEQAAPQ
     SEADCCLQNP DERVVDSYRE ALSQQLDSED EQDQRGSESG ENSKKKTKKL RMKRSQRVEP
     VNTDESTPKS PTPPQPPPPV GWGTPKVTRL PKLEPLGETR HNDFYGKPLP PLAVRQRPNG
     DAQDTIS
//
ID   PAN3_MOUSE              Reviewed;         691 AA.
AC   Q640Q5; Q3U5F2; Q8CE75; Q9CZM6;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=PAB-dependent poly(A)-specific ribonuclease subunit 3;
GN   Name=Pan3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-147 (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 585-691 (ISOFORMS 1/2/3).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Skin, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Functions in cytoplasmic mRNA decay. As part of the Pan
CC       nuclease complex, recruits polyadenylate-binding protein which in
CC       turn stimulates PAN2 nuclease activity (By similarity).
CC   -!- SUBUNIT: Interacts with PAN2 to form the Pan nuclease complex.
CC       Mediates the interaction of the Pan nuclease complex with
CC       polyadenylate-binding protein (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q640Q5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q640Q5-2; Sequence=VSP_023758;
CC       Name=3;
CC         IsoId=Q640Q5-4; Sequence=VSP_023757;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH82547.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK012409; BAB28221.1; -; mRNA.
DR   EMBL; AK028869; BAC26161.1; -; mRNA.
DR   EMBL; AK153632; BAE32127.1; -; mRNA.
DR   EMBL; BC082547; AAH82547.1; ALT_INIT; mRNA.
DR   IPI; IPI00480343; -.
DR   IPI; IPI00623361; -.
DR   IPI; IPI00830682; -.
DR   RefSeq; NP_082567.3; NM_028291.4.
DR   UniGene; Mm.320469; -.
DR   UniGene; Mm.465343; -.
DR   ProteinModelPortal; Q640Q5; -.
DR   STRING; Q640Q5; -.
DR   PhosphoSite; Q640Q5; -.
DR   PRIDE; Q640Q5; -.
DR   Ensembl; ENSMUST00000031651; ENSMUSP00000031651; ENSMUSG00000029647.
DR   Ensembl; ENSMUST00000085571; ENSMUSP00000082708; ENSMUSG00000029647.
DR   Ensembl; ENSMUST00000110543; ENSMUSP00000106172; ENSMUSG00000029647.
DR   GeneID; 72587; -.
DR   KEGG; mmu:72587; -.
DR   UCSC; uc009aoe.1; mouse.
DR   CTD; 72587; -.
DR   MGI; MGI:1919837; Pan3.
DR   eggNOG; roNOG04006; -.
DR   GeneTree; ENSGT00390000001504; -.
DR   HOGENOM; HBG315011; -.
DR   HOVERGEN; HBG058849; -.
DR   InParanoid; Q640Q5; -.
DR   OMA; HTPNPAN; -.
DR   OrthoDB; EOG4K9BBK; -.
DR   PhylomeDB; Q640Q5; -.
DR   NextBio; 336551; -.
DR   ArrayExpress; Q640Q5; -.
DR   Bgee; Q640Q5; -.
DR   Genevestigator; Q640Q5; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Nonsense-mediated mRNA decay.
FT   CHAIN         1    691       PAB-dependent poly(A)-specific
FT                                ribonuclease subunit 3.
FT                                /FTId=PRO_0000280526.
FT   DOMAIN      292    554       Protein kinase.
FT   REGION        1    291       Interaction with polyadenylate-binding
FT                                protein (By similarity).
FT   REGION      292    687       Interaction with PAN2 (By similarity).
FT   VAR_SEQ       1    440       Missing (in isoform 3).
FT                                /FTId=VSP_023757.
FT   VAR_SEQ       1    133       MDGGALTDASLTESYFSTSFIGVNGFGSPVETKYPLMQRMT
FT                                SSSSSPSLLNDSAKPYTGHDLLTSSASSLFNDFGALNISQR
FT                                RKTPNPTASEFIPKGGSTSRLSNVSQSNMSAFSQVFSHPSM
FT                                GSPATAGLAP -> MKQTDSTKGWIVWAALDSSMR (in
FT                                isoform 2).
FT                                /FTId=VSP_023758.
SQ   SEQUENCE   691 AA;  76381 MW;  9A7385BB3ABD18BB CRC64;
     MDGGALTDAS LTESYFSTSF IGVNGFGSPV ETKYPLMQRM TSSSSSPSLL NDSAKPYTGH
     DLLTSSASSL FNDFGALNIS QRRKTPNPTA SEFIPKGGST SRLSNVSQSN MSAFSQVFSH
     PSMGSPATAG LAPGMSLSAG SSPLHSPKIT PHTSPAPRRR SHTPNPASFM VPPSASTPAN
     NPAPQPPSSG QVIQKETVGG TTYFYTDTTP APLTGMVFPN YHIYPPTAPH VAYMQPKANA
     PSFFMADELR QELINRHLIT MAQIDQADMP AVPTEVDSYH SLFPLEPLPP PNRIQKSSNF
     GYITSCYKAV NSKDDLPYCL RRIHGFRLVN TKCMVLVDMW KKIQHSNIVT LREVFTTKAF
     AEPSLVFAYD FHAGGETMMS RHFNDPNSDA YFTKRKWGQH DGPLPRQHAG LLPESLIWAY
     IVQLSSALRT IHTAGLACRV MDPTKILITS KTRLRVNCVG VFDVLTFDNS QNNNPLALMA
     QYQQADLISL GKVVLALACN SLAGIQRENL QKAMELVTIN YSSDLKNLIL YLLTDQNRMR
     SVNDIMPMIG ARFYTQLDAA QMRNDVIEED LAKEVQNGRL FRLLAKLGTI NERPEFQKDP
     TWSETGDRYL LKLFRDHLFH QVTEAGAPWI DLSHIISCLN KLDAGVPEKI SLISRDEKSV
     LVVTYSDLKR CFENTFQELI AAANGNDRNS N
//
ID   HECAM_MOUSE             Reviewed;         418 AA.
AC   Q640R3;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 2.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Hepatocyte cell adhesion molecule;
DE            Short=Protein hepaCAM;
DE   Flags: Precursor;
GN   Name=Hepacam;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-418.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-320 AND
RP   SER-352, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Involved in regulating cell motility and cell-matrix
CC       interactions. May inhibit cell growth through suppression of cell
CC       proliferation (By similarity).
CC   -!- SUBUNIT: Homodimer. Dimer formation occurs predominantly through
CC       cis interactions on the cell surface (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Single-pass type I
CC       membrane protein; Cytoplasmic side (By similarity).
CC       Note=Colocalizes with CDH1 (By similarity).
CC   -!- DOMAIN: The cytoplasmic domain plays an important role in
CC       regulation of cell-matrix adhesion and cell motility (By
CC       similarity).
CC   -!- PTM: N-glycosylated (By similarity).
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC       domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; AC138284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC082537; AAH82537.1; -; mRNA.
DR   IPI; IPI00471176; -.
DR   RefSeq; NP_780398.2; NM_175189.4.
DR   UniGene; Mm.266133; -.
DR   ProteinModelPortal; Q640R3; -.
DR   SMR; Q640R3; 36-236.
DR   STRING; Q640R3; -.
DR   PhosphoSite; Q640R3; -.
DR   PRIDE; Q640R3; -.
DR   Ensembl; ENSMUST00000051839; ENSMUSP00000054105; ENSMUSG00000046240.
DR   GeneID; 72927; -.
DR   KEGG; mmu:72927; -.
DR   UCSC; uc009our.1; mouse.
DR   CTD; 72927; -.
DR   MGI; MGI:1920177; Hepacam.
DR   eggNOG; roNOG08121; -.
DR   GeneTree; ENSGT00530000063550; -.
DR   HOGENOM; HBG445444; -.
DR   HOVERGEN; HBG107974; -.
DR   InParanoid; Q640R3; -.
DR   OMA; AGVHLIR; -.
DR   OrthoDB; EOG49W2FV; -.
DR   PhylomeDB; Q640R3; -.
DR   NextBio; 337151; -.
DR   ArrayExpress; Q640R3; -.
DR   Bgee; Q640R3; -.
DR   CleanEx; MM_HEPACAM; -.
DR   Genevestigator; Q640R3; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007050; P:cell cycle arrest; IEA:UniProtKB-KW.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion; Cell cycle; Cytoplasm; Disulfide bond; Glycoprotein;
KW   Growth arrest; Growth regulation; Immunoglobulin domain; Membrane;
KW   Phosphoprotein; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     33       Potential.
FT   CHAIN        34    418       Hepatocyte cell adhesion molecule.
FT                                /FTId=PRO_0000298778.
FT   TOPO_DOM     34    240       Extracellular (Potential).
FT   TRANSMEM    241    261       Helical; (Potential).
FT   TOPO_DOM    262    418       Cytoplasmic (Potential).
FT   DOMAIN       34    142       Ig-like V-type.
FT   DOMAIN      148    234       Ig-like C2-type.
FT   MOD_RES     280    280       Phosphoserine.
FT   MOD_RES     320    320       Phosphoserine.
FT   MOD_RES     352    352       Phosphoserine.
FT   CARBOHYD     35     35       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    138    138       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    167    167       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    189    189       N-linked (GlcNAc...) (Potential).
FT   DISULFID    168    217       By similarity.
SQ   SEQUENCE   418 AA;  46367 MW;  39D65EB953A5B933 CRC64;
     MKRERGALSR ASRALRLSPF VYLLLIQPVP LEGVNITSPV RLIHGTVGKS ALLSVQYSST
     SSDKPVVKWQ LKRDKPVTVV QSIGTEVIGT LRPDYRDRIR LFENGSLLLS DLQLADEGTY
     EVEISITDDT FTGEKTINLT VDVPISRPQV LVASTTVLEL SEAFTLNCSH ENGTKPSYTW
     LKDGKPLLND SRMLLSPDQK VLTITRVLME DDDLYSCVVE NPISQVRSLP VKITVYRRSS
     LYIILSTGGI FLLVTLVTVC ACWKPSKKSR KKRKLEKQNS LEYMDQNDDR LKSEADTLPR
     SGEQERKNPM ALYILKDKDS SEPDENPATE PRSTTEPGPP GYSVSPPVPG RSPGLPIRSA
     RRYPRSPARS PATGRTHTSP PRAPSSPGRS RSSSRSLRTA GVQRIREQDE SGQVEISA
//
ID   SPRE_MOUSE              Reviewed;         261 AA.
AC   Q64105; Q63996;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Sepiapterin reductase;
DE            Short=SPR;
DE            EC=1.1.1.153;
GN   Name=Spr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=95178553; PubMed=7873607; DOI=10.1016/0167-4781(94)00225-R;
RA   Ota A., Ichinose H., Nagatsu T.;
RT   "Mouse sepiapterin reductase: an enzyme involved in the final step of
RT   tetrahydrobiopterin biosynthesis. Primary structure deduced from the
RT   cDNA sequence.";
RL   Biochim. Biophys. Acta 1260:320-322(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129;
RX   MEDLINE=99227131; PubMed=10209270; DOI=10.1016/S0167-4781(99)00030-5;
RA   Lee S.W., Park I.Y., Hahn Y., Lee J.E., Seong C.S., Chung J.H.,
RA   Park Y.S.;
RT   "Cloning of mouse sepiapterin reductase gene and characterization of
RT   its promoter region.";
RL   Biochim. Biophys. Acta 1445:165-171(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 209-261.
RX   MEDLINE=94136218; PubMed=8304109;
RA   Maier J., Schott K., Werner T., Bacher A., Ziegler I.;
RT   "Northern blot analysis of sepiapterin reductase mRNA in mammalian
RT   cell lines and tissues.";
RL   Adv. Exp. Med. Biol. 338:195-198(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 209-255.
RX   MEDLINE=93178546; PubMed=8440319; DOI=10.1006/excr.1993.1027;
RA   Maier J., Schott K., Werner T., Bacher A., Ziegler I.;
RT   "Detection of a novel sepiapterin reductase mRNA: assay of mRNA in
RT   various cells and tissues of various species.";
RL   Exp. Cell Res. 204:217-222(1993).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) IN COMPLEXES WITH PTERIN;
RP   N-ACETYL SEROTONIN AND NADP, ACTIVE SITE, AND SUBUNIT.
RX   MEDLINE=98070299; PubMed=9405351; DOI=10.1093/emboj/16.24.7219;
RA   Auerbach G., Herrmann A., Gutlich M., Fischer M., Jacob U., Bacher A.,
RA   Huber R.;
RT   "The 1.25-A crystal structure of sepiapterin reductase reveals its
RT   binding mode to pterins and brain neurotransmitters.";
RL   EMBO J. 16:7219-7230(1997).
CC   -!- FUNCTION: Catalyzes the final one or two reductions in tetra-
CC       hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin.
CC   -!- CATALYTIC ACTIVITY: 7,8-dihydrobiopterin + NADP(+) = sepiapterin +
CC       NADPH.
CC   -!- CATALYTIC ACTIVITY: Tetrahydrobiopterin + 2 NADP(+) = 6-pyruvoyl-
CC       5,6,7,8-tetrahydropterin + 2 NADPH.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the sepiapterin reductase family.
CC   -----------------------------------------------------------------------
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DR   EMBL; S77493; AAB33611.1; -; mRNA.
DR   EMBL; U78077; AAC69364.1; -; Genomic_DNA.
DR   EMBL; U78076; AAC69364.1; JOINED; Genomic_DNA.
DR   EMBL; S71375; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00129164; -.
DR   PIR; S52110; S52110.
DR   UniGene; Mm.28393; -.
DR   PDB; 1NAS; X-ray; 2.10 A; A=3-261.
DR   PDB; 1OAA; X-ray; 1.25 A; A=3-261.
DR   PDB; 1SEP; X-ray; 1.95 A; A=1-261.
DR   PDBsum; 1NAS; -.
DR   PDBsum; 1OAA; -.
DR   PDBsum; 1SEP; -.
DR   ProteinModelPortal; Q64105; -.
DR   SMR; Q64105; 3-261.
DR   STRING; Q64105; -.
DR   PhosphoSite; Q64105; -.
DR   REPRODUCTION-2DPAGE; Q64105; -.
DR   PRIDE; Q64105; -.
DR   Ensembl; ENSMUST00000045986; ENSMUSP00000048111; ENSMUSG00000033735.
DR   MGI; MGI:103078; Spr.
DR   eggNOG; roNOG10314; -.
DR   HOVERGEN; HBG006973; -.
DR   InParanoid; Q64105; -.
DR   OrthoDB; EOG4HMJB9; -.
DR   BRENDA; 1.1.1.153; 244.
DR   ArrayExpress; Q64105; -.
DR   Bgee; Q64105; -.
DR   CleanEx; MM_SPR; -.
DR   Genevestigator; Q64105; -.
DR   GermOnline; ENSMUSG00000033735; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0004757; F:sepiapterin reductase activity; ISS:UniProtKB.
DR   GO; GO:0048667; P:cell morphogenesis involved in neuron differentiation; IMP:MGI.
DR   GO; GO:0016265; P:death; IMP:MGI.
DR   GO; GO:0042417; P:dopamine metabolic process; IMP:MGI.
DR   GO; GO:0006558; P:L-phenylalanine metabolic process; IMP:MGI.
DR   GO; GO:0042415; P:norepinephrine metabolic process; IMP:MGI.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0019889; P:pteridine metabolic process; IMP:MGI.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
DR   GO; GO:0042428; P:serotonin metabolic process; IMP:MGI.
DR   GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IEA:InterPro.
DR   GO; GO:0050882; P:voluntary musculoskeletal movement; IMP:MGI.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR006393; Sepiapterin_red.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   TIGRFAMs; TIGR01500; sepiapter_red; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; NADP; Oxidoreductase.
FT   CHAIN         1    261       Sepiapterin reductase.
FT                                /FTId=PRO_0000072150.
FT   NP_BIND      15     21       NADP.
FT   NP_BIND      43     44       NADP.
FT   NP_BIND      70     71       NADP.
FT   NP_BIND     202    207       NADP.
FT   REGION      158    159       Substrate binding.
FT   BINDING     171    171       Substrate.
FT   BINDING     175    175       NADP.
FT   BINDING     200    200       Substrate; via amide nitrogen.
FT   BINDING     222    222       Substrate.
FT   BINDING     258    258       Substrate.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   CONFLICT      4      4       D -> G (in Ref. 2; AAC69364).
FT   STRAND        7     15
FT   HELIX        19     29
FT   STRAND       37     43
FT   HELIX        45     58
FT   STRAND       62     68
FT   HELIX        74     86
FT   STRAND       95    100
FT   HELIX       112    114
FT   HELIX       118    128
FT   HELIX       130    141
FT   STRAND      150    156
FT   HELIX       159    161
FT   HELIX       169    188
FT   STRAND      192    198
FT   STRAND      201    204
FT   HELIX       205    213
FT   HELIX       217    228
FT   HELIX       235    248
FT   STRAND      255    258
SQ   SEQUENCE   261 AA;  27883 MW;  102294E439CB8AEC CRC64;
     MEADGLGCAV CVLTGASRGF GRALAPQLAR LLSPGSVMLV SARSESMLRQ LKEELGAQQP
     DLKVVLAAAD LGTEAGVQRL LSAVRELPRP EGLQRLLLIN NAATLGDVSK GFLNVNDLAE
     VNNYWALNLT SMLCLTSGTL NAFQDSPGLS KTVVNISSLC ALQPYKGWGL YCAGKAARDM
     LYQVLAAEEP SVRVLSYAPG PLDNDMQQLA RETSKDPELR SKLQKLKSDG ALVDCGTSAQ
     KLLGLLQKDT FQSGAHVDFY D
//
ID   TIF1A_MOUSE             Reviewed;        1051 AA.
AC   Q64127; Q64126;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 110.
DE   RecName: Full=Transcription intermediary factor 1-alpha;
DE            Short=TIF1-alpha;
DE            EC=6.3.2.-;
DE   AltName: Full=E3 ubiquitin-protein ligase Trim24;
DE   AltName: Full=Tripartite motif-containing protein 24;
GN   Name=Trim24; Synonyms=Tif1, Tif1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH ESTROGEN
RP   RECEPTOR, AND SUBCELLULAR LOCATION.
RC   TISSUE=Carcinoma;
RX   MEDLINE=95262642; PubMed=7744009;
RA   le Douarin B., Zechel C., Garnier J.-M., Lutz Y., Tora L., Pierrat B.,
RA   Heery D., Gronemeyer H., Chambon P., Losson R.;
RT   "The N-terminal part of TIF1, a putative mediator of the ligand-
RT   dependent activation function (AF-2) of nuclear receptors, is fused to
RT   B-raf in the oncogenic protein T18.";
RL   EMBO J. 14:2020-2033(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH CBX1 AND CBX3.
RX   MEDLINE=97133299; PubMed=8978696;
RA   le Douarin B., Nielsen A.L., Garnier J.-M., Ichinose H.,
RA   Jeanmougin F., Losson R., Chambon P.;
RT   "A possible involvement of TIF1 alpha and TIF1 beta in the epigenetic
RT   control of transcription by nuclear receptors.";
RL   EMBO J. 15:6701-6715(1996).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PML.
RX   PubMed=10610177; DOI=10.1038/15463;
RA   Zhong S., Delva L., Rachez C., Cenciarelli C., Gandini D., Zhang H.,
RA   Kalantry S., Freedman L.P., Pandolfi P.P.;
RT   "A RA-dependent, tumour-growth suppressive transcription complex is
RT   the target of the PML-RARalpha and T18 oncoproteins.";
RL   Nat. Genet. 23:287-295(1999).
RN   [5]
RP   SUMOYLATION, SUBCELLULAR LOCATION, INTERACTION WITH CBX5, AND
RP   MUTAGENESIS OF LYS-724 AND LYS-742.
RX   MEDLINE=21214370; PubMed=11313457;
RX   DOI=10.1128/MCB.21.10.3314-3324.2001;
RA   Seeler J.-S., Marchio A., Losson R., Desterro J.M.P., Hay R.T.,
RA   Chambon P., Dejean A.;
RT   "Common properties of nuclear protein SP100 and TIF1alpha chromatin
RT   factor: role of SUMO modification.";
RL   Mol. Cell. Biol. 21:3314-3324(2001).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16880268; DOI=10.1083/jcb.200603146;
RA   Torres-Padilla M.E., Zernicka-Goetz M.;
RT   "Role of TIF1alpha as a modulator of embryonic transcription in the
RT   mouse zygote.";
RL   J. Cell Biol. 174:329-338(2006).
RN   [7]
RP   FUNCTION, INTERACTION WITH CARM1, AND IDENTIFICATION IN A COACTIVATOR
RP   COMPLEX WITH CARM1 AND NCOA2/GRIP1.
RX   PubMed=16322096; DOI=10.1210/me.2005-0393;
RA   Teyssier C., Ou C.Y., Khetchoumian K., Losson R., Stallcup M.R.;
RT   "Transcriptional intermediary factor 1alpha mediates physical
RT   interaction and functional synergy between the coactivator-associated
RT   arginine methyltransferase 1 and glucocorticoid receptor-interacting
RT   protein 1 nuclear receptor coactivators.";
RL   Mol. Endocrinol. 20:1276-1286(2006).
RN   [8]
RP   INDUCTION, AND TISSUE SPECIFICITY.
RX   PubMed=17412818; DOI=10.1210/en.2006-1192;
RA   Laz E.V., Holloway M.G., Chen C.S., Waxman D.J.;
RT   "Characterization of three growth hormone-responsive transcription
RT   factors preferentially expressed in adult female liver.";
RL   Endocrinology 148:3327-3337(2007).
RN   [9]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=18026104; DOI=10.1038/ng.2007.15;
RA   Khetchoumian K., Teletin M., Tisserand J., Mark M., Herquel B.,
RA   Ignat M., Zucman-Rossi J., Cammas F., Lerouge T., Thibault C.,
RA   Metzger D., Chambon P., Losson R.;
RT   "Loss of Trim24 (Tif1alpha) gene function confers oncogenic activity
RT   to retinoic acid receptor alpha.";
RL   Nat. Genet. 39:1500-1506(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-812; SER-1026 AND
RP   SER-1029, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [11]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=18287084; DOI=10.1073/pnas.0712030105;
RA   Ignat M., Teletin M., Tisserand J., Khetchoumian K., Dennefeld C.,
RA   Chambon P., Losson R., Mark M.;
RT   "Arterial calcifications and increased expression of vitamin D
RT   receptor targets in mice lacking TIF1alpha.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2598-2603(2008).
RN   [12]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AR; KAT5/TIP60
RP   AND BRD7.
RX   PubMed=19909775; DOI=10.1016/j.bbamcr.2009.11.001;
RA   Kikuchi M., Okumura F., Tsukiyama T., Watanabe M., Miyajima N.,
RA   Tanaka J., Imamura M., Hatakeyama S.;
RT   "TRIM24 mediates ligand-dependent activation of androgen receptor and
RT   is repressed by a bromodomain-containing protein, BRD7, in prostate
RT   cancer cells.";
RL   Biochim. Biophys. Acta 1793:1828-1836(2009).
RN   [13]
RP   FUNCTION, INTERACTION WITH TP53, AND MASS SPECTROMETRY.
RX   PubMed=19556538; DOI=10.1073/pnas.0813177106;
RA   Allton K., Jain A.K., Herz H.M., Tsai W.W., Jung S.Y., Qin J.,
RA   Bergmann A., Johnson R.L., Barton M.C.;
RT   "Trim24 targets endogenous p53 for degradation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:11612-11616(2009).
CC   -!- FUNCTION: Transcriptional coactivator that interacts with numerous
CC       nuclear receptors and coactivators and modulates the transcription
CC       of target genes. Interacts with chromatin depending on histone H3
CC       modifications, having the highest affinity for histone H3 that is
CC       both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23'
CC       (H3K23ac) (By similarity). Has E3 protein-ubiquitin ligase
CC       activity. Promotes ubiquitination and proteasomal degradation of
CC       TP53. Plays a role in the regulation of cell proliferation and
CC       apoptosis via its effects on TP53 levels. Up-regulates ligand-
CC       dependent transcription activation by AR, GCR/NR3C1, thyroid
CC       hormone receptor (TR) and ESR1. Modulates transcription activation
CC       by retinoic acid (RA) receptors, such as RARA. Plays a role in
CC       regulating retinoic acid-dependent proliferation of hepatocytes.
CC       Required for normal transition from proliferating neonatal
CC       hepatocytes to quiescent adult hepatocytes.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts (via bromo domain) with histone H3 (via N-
CC       terminus), provided that it is not methylated at 'Lys-4'
CC       (H3K4me0). Does not interact with histone H3 that is methylated at
CC       'Lys-4' (H3K4me1, H3K4me2 or H3K4me3). Interacts (via bromo
CC       domain) with histone H3 (via N-terminus) that is acetylated at
CC       'Lys-23' (H3K23ac). Has the highest affinity for histone H3 that
CC       is both unmodified at 'Lys-4' (H3K4me0) and acetylated at 'Lys-23'
CC       (H3K23ac). Has very low affinity for histone H3 that is methylated
CC       at 'Lys-9' (H3K9me), or acetylated at both 'Lys-9' (H3K9ac) and
CC       'Lys-14' (H3K14ac), or acetylated at 'Lys-27' (H3K27ac) (in
CC       vitro). Interacts with NR3C2/MCR (By similarity). Interacts with
CC       the ligand-binding domain of estrogen receptors (in vitro).
CC       Interaction with DNA-bound estrogen receptors requires the
CC       presence of estradiol (By similarity). Interacts with AR, CARM1,
CC       KAT5/TIP60, NCOA2/GRIP1, BRD7, CBX1, CBX3 and CBX5. Part of a
CC       coactivator complex containing TRIM24, NCOA2/GRIP1 and CARM1.
CC       Interacts with TP53 and PML.
CC   -!- INTERACTION:
CC       P83917:Cbx1; NbExp=1; IntAct=EBI-307947, EBI-78119;
CC       Q61686:Cbx5; NbExp=1; IntAct=EBI-307947, EBI-307973;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Detected in the
CC       cytoplasm of the zygote. Translocates into the pronucleus at the
CC       time of genome activation. Colocalizes with sites of active
CC       transcription.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=Q64127-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=Q64127-2; Sequence=VSP_005773;
CC   -!- TISSUE SPECIFICITY: Detected in embryonic and adult liver.
CC       Detected in zygote and throughout embryogenesis (at protein
CC       level). Detected in all adult tissues, with the highest expression
CC       level in testis.
CC   -!- INDUCTION: Before puberty, highly expressed in liver from males
CC       and females. After puberty, expression is considerably higher in
CC       liver from females compared to males. Up-regulated in males by
CC       continuous exposure to growth hormone.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- PTM: Sumoylated.
CC   -!- DISEASE: Note=A chromosomal aberration involving TRIM24 produces a
CC       TRIM24-BRAF (T18) oncogene originally isolated from a furfural-
CC       induced hepatoma.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype during the first few
CC       months. Impaired transition from proliferating neonatal
CC       hepatocytes to quiescent adult hepatocytes. Hepatocytes continue
CC       to proliferate throughout adulthood. High incidence hypertrophic
CC       hepatocytes with enlarged nuclei after three months. After nine
CC       months, about half of the mice have hepatocellular adenomas. Very
CC       high incidence of hepatocarcinoma in 13 to 29 month old mice,
CC       increasing from 40% to 80%. When one copy of Rara is disrupted,
CC       mice do not develop liver tumors or liver dysplasia.
CC   -!- SIMILARITY: Contains 2 B box-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 bromo domain.
CC   -!- SIMILARITY: Contains 1 PHD-type zinc finger.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
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DR   EMBL; S78221; AAB34290.1; -; mRNA.
DR   EMBL; S78219; AAB34289.1; -; mRNA.
DR   EMBL; BC056959; AAH56959.1; -; mRNA.
DR   IPI; IPI00131130; -.
DR   IPI; IPI00227778; -.
DR   PIR; S55259; S55259.
DR   RefSeq; NP_659542.3; NM_145076.3.
DR   UniGene; Mm.41063; -.
DR   ProteinModelPortal; Q64127; -.
DR   SMR; Q64127; 46-150, 159-261, 825-1013.
DR   IntAct; Q64127; 14.
DR   STRING; Q64127; -.
DR   PhosphoSite; Q64127; -.
DR   PRIDE; Q64127; -.
DR   Ensembl; ENSMUST00000031859; ENSMUSP00000031859; ENSMUSG00000029833.
DR   GeneID; 21848; -.
DR   KEGG; mmu:21848; -.
DR   UCSC; uc009bjk.1; mouse.
DR   UCSC; uc009bjl.1; mouse.
DR   CTD; 21848; -.
DR   MGI; MGI:109275; Trim24.
DR   HOGENOM; HBG446888; -.
DR   HOVERGEN; HBG054599; -.
DR   InParanoid; Q64127; -.
DR   OMA; FWAQNIF; -.
DR   OrthoDB; EOG4P8FH9; -.
DR   PhylomeDB; Q64127; -.
DR   NextBio; 301326; -.
DR   ArrayExpress; Q64127; -.
DR   Bgee; Q64127; -.
DR   CleanEx; MM_TRIM24; -.
DR   Genevestigator; Q64127; -.
DR   GermOnline; ENSMUSG00000029833; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005719; C:nuclear euchromatin; IDA:MGI.
DR   GO; GO:0005726; C:perichromatin fibrils; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0034056; F:estrogen response element binding; ISS:UniProtKB.
DR   GO; GO:0070577; F:histone acetyl-lysine binding; ISS:UniProtKB.
DR   GO; GO:0016922; F:ligand-dependent nuclear receptor binding; IDA:MGI.
DR   GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
DR   GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR   GO; GO:0016564; F:transcription repressor activity; IDA:MGI.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0055074; P:calcium ion homeostasis; IMP:MGI.
DR   GO; GO:0071391; P:cellular response to estrogen stimulus; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IGI:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR   GO; GO:0030163; P:protein catabolic process; IMP:UniProtKB.
DR   GO; GO:0042981; P:regulation of apoptosis; IMP:UniProtKB.
DR   GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
DR   GO; GO:0070562; P:regulation of vitamin D receptor signaling pathway; IMP:MGI.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Gene3D; G3DSA:1.20.920.10; Bromodomain; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 3.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF00643; zf-B_box; 2.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 2.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS50119; ZF_BBOX; 2.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Bromodomain; Chromosomal rearrangement;
KW   Coiled coil; Cytoplasm; DNA-binding; Isopeptide bond; Ligase;
KW   Metal-binding; Nucleus; Phosphoprotein; Proto-oncogene; Repeat;
KW   Repressor; Transcription; Transcription regulation; Tumor suppressor;
KW   Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1   1051       Transcription intermediary factor 1-
FT                                alpha.
FT                                /FTId=PRO_0000056391.
FT   DOMAIN      933    988       Bromo.
FT   ZN_FING      52     77       RING-type.
FT   ZN_FING     158    211       B box-type 1.
FT   ZN_FING     218    259       B box-type 2.
FT   ZN_FING     827    874       PHD-type.
FT   REGION      755    780       Nuclear receptor binding site (NRBS).
FT   REGION      835    841       Interaction with histone H3 that is not
FT                                methylated at 'Lys-4' (H3K4me0) (By
FT                                similarity).
FT   COILED      289    359       Potential.
FT   MOTIF       892    908       Nuclear localization signal (Potential).
FT   COMPBIAS      8     15       Poly-Ala.
FT   COMPBIAS     19     22       Poly-Ala.
FT   COMPBIAS    344    347       Poly-Gln.
FT   COMPBIAS    583    587       Poly-Ser.
FT   SITE        332    333       Breakpoint for translocation to form
FT                                TRIM24-BRAF oncogene.
FT   SITE        828    828       Interaction with histone H3 that is not
FT                                methylated at 'Lys-4' (H3K4me0) (By
FT                                similarity).
FT   MOD_RES     661    661       Phosphoserine (By similarity).
FT   MOD_RES     668    668       Phosphoserine (By similarity).
FT   MOD_RES     688    688       Phosphoserine (By similarity).
FT   MOD_RES     769    769       Phosphoserine (By similarity).
FT   MOD_RES     809    809       Phosphoserine (By similarity).
FT   MOD_RES     812    812       Phosphoserine.
FT   MOD_RES    1026   1026       Phosphoserine.
FT   MOD_RES    1029   1029       Phosphoserine.
FT   CROSSLNK    724    724       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO)
FT                                (Probable).
FT   CROSSLNK    742    742       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO)
FT                                (Probable).
FT   VAR_SEQ     477    510       Missing (in isoform Short).
FT                                /FTId=VSP_005773.
FT   MUTAGEN     724    724       K->R: Loss of sumoylation; when
FT                                associated with R-742.
FT   MUTAGEN     742    742       K->R: Loss of sumoylation; when
FT                                associated with R-724.
SQ   SEQUENCE   1051 AA;  116657 MW;  610584C1C6885972 CRC64;
     MEVAVEKAAA AAAPAGGPAA AAPSGENEAE SRQGPDSESG GEASRLNLLD TCAVCHQNIQ
     SRVPKLLPCL HSFCQRCLPA PQRYLMLTAP ALGSAETPPP APAPAPAPGS PAGGPSPFAT
     QVGVIRCPVC SQECAERHII DNFFVKDTTE VPSSTVEKSN QVCTSCEDNA EANGFCVECV
     EWLCKTCIRA HQRVKFTKDH TVRQKEEVSP EAVGVTSQRP VFCPFHKKEQ LKLYCETCDK
     LTCRDCQLLE HKEHRYQFIE EAFQNQKVII DTLITKLMEK TKYIKYTGNQ IQNRIIEINQ
     NQKQVEQDIK VAIFTLMVEI NKKGKALLHQ LESLAKDHRM KLMQQQQEVA GLSKQLEHVM
     HFSKWAVSSG SSTALLYSKR LITYRLRHLL RARCDASPVT NTTIQFHCDP SFWAQNIINL
     GSLVIEDKES QPQMPKQNPV VEQSSQPPGG LPSNQLSKFP TQISLAQLRL QHIQQQVMAQ
     RQQVQRRPAP VGLPNPRMQG PIQQPSISHQ HPPPRLINFQ NHSPKPNGPV LPPYPQQLRY
     SPSQNVPRQT TIKPNPLQMA FLAQQAIKQW QISSVQAPPT TASSSSSTPS SPTITSAAGY
     DGKAFSSPMI DLSAPVGGSY NLPSLPDIDC SSTIMLDNIA RKDTGVDHAQ PRPPSNRTVQ
     SPNSSVPSPG LAGPVTMTSV HPPIRSPSAS SVGSRGSSGS SSKPAGADST HKVPVVMLEP
     IRIKQENSGP PENYDFPVVI VKQESDEESR PQNTNYPRSI LTSLLLNSSQ SSASEETVLR
     SDAPDSTGDQ PGLHQENSSN GKSEWSDASQ KSPVHVGETR KEDDPNEDWC AVCQNGGELL
     CCEKCPKVFH LTCHVPTLTN FPSGEWICTF CRDLSKPEVD YDCDVPSHHS EKRKSEGLTK
     LTPIDKRKCE RLLLFLYCHE MSLAFQDPVP LTVPDYYKII KNPMDLSTIK KRLQEDYCMY
     TKPEDFVADF RLIFQNCAEF NEPDSEVANA GIKLESYFEE LLKNLYPEKR FPKVEFRHEA
     EDCKFSDDSD DDFVQPRKKR LKSTEDRQLL K
//
ID   CBPC1_MOUSE             Reviewed;        1218 AA.
AC   Q641K1; Q3TDS0; Q3V147; Q6P9R9; Q8C1K8; Q9D962; Q9EQI4;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Cytosolic carboxypeptidase 1;
DE            EC=3.4.17.-;
DE   AltName: Full=ATP/GTP-binding protein 1;
DE   AltName: Full=Nervous system nuclear protein induced by axotomy protein 1;
GN   Name=Agtpbp1; Synonyms=Ccp1, Nna1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
RP   INDUCTION BY AXON REGENERATION, AND DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20538704; PubMed=11083920; DOI=10.1006/mcne.2000.0900;
RA   Harris A., Morgan J.I., Pecot M., Soumare A., Osborne A., Soares H.D.;
RT   "Regenerating motor neurons express Nna1, a novel ATP/GTP-binding
RT   protein related to zinc carboxypeptidases.";
RL   Mol. Cell. Neurosci. 16:578-596(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1115-1218 (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Hippocampus, Pancreas, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INVOLVEMENT IN PCD, INDUCTION BY AXONAL REGENERATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=11884758; DOI=10.1126/science.1068912;
RA   Fernandez-Gonzalez A., La Spada A.R., Treadaway J., Higdon J.C.,
RA   Harris B.S., Sidman R.L., Morgan J.I., Zuo J.;
RT   "Purkinje cell degeneration (pcd) phenotypes caused by mutations in
RT   the axotomy-induced gene, Nna1.";
RL   Science 295:1904-1906(2002).
RN   [5]
RP   VARIANT PCD ASP-832 INS.
RX   PubMed=16465590; DOI=10.1007/s00335-005-0096-x;
RA   Chakrabarti L., Neal J.T., Miles M., Martinez R.A., Smith A.C.,
RA   Sopher B.L., La Spada A.R.;
RT   "The Purkinje cell degeneration 5J mutation is a single amino acid
RT   insertion that destabilizes Nna1 protein.";
RL   Mamm. Genome 17:103-110(2006).
RN   [6]
RP   INVOLVEMENT IN PCD.
RX   PubMed=16942761; DOI=10.1016/j.brainres.2006.07.065;
RA   Wang T., Morgan J.I.;
RT   "The Purkinje cell degeneration (pcd) mouse: an unexpected molecular
RT   link between neuronal degeneration and regeneration.";
RL   Brain Res. 1140:26-40(2007).
RN   [7]
RP   INVOLVEMENT IN PCD, AND MUTAGENESIS OF 971-ASN-ARG-972.
RX   PubMed=16952463; DOI=10.1016/j.mcn.2006.07.009;
RA   Wang T., Parris J., Li L., Morgan J.I.;
RT   "The carboxypeptidase-like substrate-binding site in Nna1 is essential
RT   for the rescue of the Purkinje cell degeneration (pcd) phenotype.";
RL   Mol. Cell. Neurosci. 33:200-213(2006).
RN   [8]
RP   INVOLVEMENT IN PCD, AND MUTAGENESIS OF HIS-912 AND GLU-915.
RX   PubMed=18602413; DOI=10.1016/j.visres.2008.05.026;
RA   Chakrabarti L., Eng J., Martinez R.A., Jackson S., Huang J.,
RA   Possin D.E., Sopher B.L., La Spada A.R.;
RT   "The zinc-binding domain of Nna1 is required to prevent retinal
RT   photoreceptor loss and cerebellar ataxia in Purkinje cell degeneration
RT   (pcd) mice.";
RL   Vision Res. 48:1999-2005(2008).
RN   [9]
RP   FUNCTION, TISSUE SPECIFICITY, INVOLVEMENT IN PCD, INTERACTION WITH
RP   MYLK, AND MUTAGENESIS OF HIS-912 AND GLU-915.
RX   PubMed=21074048; DOI=10.1016/j.cell.2010.10.014;
RA   Rogowski K., van Dijk J., Magiera M.M., Bosc C., Deloulme J.C.,
RA   Bosson A., Peris L., Gold N.D., Lacroix B., Grau M.B., Bec N.,
RA   Larroque C., Desagher S., Holzer M., Andrieux A., Moutin M.J.,
RA   Janke C.;
RT   "A family of protein-deglutamylating enzymes associated with
RT   neurodegeneration.";
RL   Cell 143:564-578(2010).
RN   [10]
RP   INVOLVEMENT IN PCD, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-912
RP   AND GLU-915.
RX   PubMed=20620870; DOI=10.1016/j.neuron.2010.05.024;
RA   Chakrabarti L., Zahra R., Jackson S.M., Kazemi-Esfarjani P.,
RA   Sopher B.L., Mason A.G., Toneff T., Ryu S., Shaffer S., Kansy J.W.,
RA   Eng J., Merrihew G., MacCoss M.J., Murphy A., Goodlett D.R., Hook V.,
RA   Bennett C.L., Pallanck L.J., La Spada A.R.;
RT   "Mitochondrial dysfunction in NnaD mutant flies and Purkinje cell
RT   degeneration mice reveals a role for Nna proteins in neuronal
RT   bioenergetics.";
RL   Neuron 66:835-847(2010).
RN   [11]
RP   INVOLVEMENT IN PCD.
RX   PubMed=20920790; DOI=10.1016/j.neuron.2010.08.013;
RA   Li J., Gu X., Ma Y., Calicchio M.L., Kong D., Teng Y.D., Yu L.,
RA   Crain A.M., Vartanian T.K., Pasqualini R., Arap W., Libermann T.A.,
RA   Snyder E.Y., Sidman R.L.;
RT   "Nna1 mediates Purkinje cell dendritic development via lysyl oxidase
RT   propeptide and NF-kappaB signaling.";
RL   Neuron 68:45-60(2010).
CC   -!- FUNCTION: Metallocarboxypeptidase that mediates deglutamylation of
CC       target proteins. Catalyzes the deglutamylation of polyglutamate
CC       side chains generated by post-translational polyglutamylation in
CC       proteins such as tubulins. Also removes gene-encoded
CC       polyglutamates from the carboxy-terminus of target proteins such
CC       as MYLK. Acts as a long-chain deglutamylase and specifically
CC       shortens long polyglutamate chains, while it is not able to remove
CC       the branching point glutamate, a process catalyzed by AGBL5/CCP5.
CC       Deglutamylation plays a key role in cerebellar Purkinje cell
CC       differentiation, accumulation of tubulin polyglutamylation causing
CC       neurodegeneration.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Interacts with MYLK.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. Mitochondrion.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q641K1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q641K1-2; Sequence=VSP_029047, VSP_029048;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q641K1-3; Sequence=VSP_029045, VSP_029046;
CC         Note=No experimental confirmation available. Apparent retained
CC         intron. May be produced at very low levels due to a premature
CC         stop codon in the mRNA, leading to nonsense-mediated mRNA decay;
CC       Name=4;
CC         IsoId=Q641K1-4; Sequence=VSP_038803, VSP_038805;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q641K1-5; Sequence=VSP_038804;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in the cerebellum and cortex
CC       of adult mouse brain. Expressed at similar levels in both the
CC       cerebellum and the cortex throughout all developmental stages.
CC       Also expressed in sciatic nerve transection, spinal motor neurons
CC       undergoing axon regeneration, testis, heart and in developing
CC       brain. Expression in cranial motor nuclei is the same as that
CC       observed in uninjured primary motor neurons. Expression is
CC       prevalent in sensory neurons and hippocampal CA3 neurons in
CC       addition to regenerating motor neurons.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in differentiating neurons.
CC       From E16.5, expression is widespread in brain, spinal cord, and
CC       peripheral nervous tissue. Within the developing CNS, expression
CC       is restricted to regions of brain and spinal cord containing
CC       differentiating neurons.
CC   -!- INDUCTION: By axonal regeneration.
CC   -!- DISEASE: Note=Defects in Agtpbp1 are the cause of Purkinje cell
CC       degeneration (pcd). Pcd is a spontaneous mutation that causes
CC       adult-onset degeneration of cerebellar Purkinje neurons, retinal
CC       photoreceptors, olfactory bulb mitral neurons, and selected
CC       thalamic neurons, and has defective spermatogenesis. Defects in
CC       mitochondrial metabolic functions are also observed. The molecular
CC       causes of neurodegeneration are still unclear, but they are
CC       probably due to an accumulation of glutamylation, either tubulin
CC       hyperglutamylation or another hyperglutamylated target proteins.
CC       An increase of intranuclear localization of lysyl oxidase (Lox)
CC       propeptide, which interferes with NF-kappa-B Rela signaling and
CC       microtubule-associated protein regulation of microtubule stability
CC       is also observed, possibly leading to underdevelopment of Purkinje
CC       cell dendrites.
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG37102.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; AF219141; AAG37102.1; ALT_INIT; mRNA.
DR   EMBL; AK007328; BAB24963.2; -; mRNA.
DR   EMBL; AK013688; BAC25412.1; -; mRNA.
DR   EMBL; AK132695; BAE21306.1; -; mRNA.
DR   EMBL; AK170046; BAE41530.1; -; mRNA.
DR   EMBL; BC082335; AAH82335.1; -; mRNA.
DR   EMBL; BC060633; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00111209; -.
DR   IPI; IPI00471182; -.
DR   IPI; IPI00869451; -.
DR   IPI; IPI00955657; -.
DR   IPI; IPI00955759; -.
DR   RefSeq; NP_001041473.1; NM_001048008.1.
DR   RefSeq; NP_075817.2; NM_023328.2.
DR   UniGene; Mm.153008; -.
DR   UniGene; Mm.212923; -.
DR   ProteinModelPortal; Q641K1; -.
DR   STRING; Q641K1; -.
DR   MEROPS; M14.028; -.
DR   PhosphoSite; Q641K1; -.
DR   PRIDE; Q641K1; -.
DR   Ensembl; ENSMUST00000022040; ENSMUSP00000022040; ENSMUSG00000021557.
DR   Ensembl; ENSMUST00000091573; ENSMUSP00000089161; ENSMUSG00000021557.
DR   Ensembl; ENSMUST00000109830; ENSMUSP00000105456; ENSMUSG00000021557.
DR   GeneID; 67269; -.
DR   KEGG; mmu:67269; -.
DR   UCSC; uc007qun.1; mouse.
DR   CTD; 67269; -.
DR   MGI; MGI:2159437; Agtpbp1.
DR   HOVERGEN; HBG107587; -.
DR   InParanoid; Q641K1; -.
DR   OMA; HGLNNDI; -.
DR   OrthoDB; EOG4TMR17; -.
DR   NextBio; 324062; -.
DR   ArrayExpress; Q641K1; -.
DR   Bgee; Q641K1; -.
DR   CleanEx; MM_AGTPBP1; -.
DR   Genevestigator; Q641K1; -.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IDA:UniProtKB.
DR   GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0035609; P:C-terminal protein deglutamylation; IDA:UniProtKB.
DR   GO; GO:0008219; P:cell death; IEA:UniProtKB-KW.
DR   GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IMP:UniProtKB.
DR   GO; GO:0001754; P:eye photoreceptor cell differentiation; IMP:UniProtKB.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR   GO; GO:0050905; P:neuromuscular process; IMP:UniProtKB.
DR   GO; GO:0042133; P:neurotransmitter metabolic process; IMP:MGI.
DR   GO; GO:0021772; P:olfactory bulb development; IMP:UniProtKB.
DR   GO; GO:0035610; P:protein side chain deglutamylation; IDA:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000834; Peptidase_M14.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS00132; CARBOXYPEPT_ZN_1; FALSE_NEG.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Carboxypeptidase; Cytoplasm; Disease mutation;
KW   Hydrolase; Metal-binding; Metalloprotease; Mitochondrion;
KW   Neurodegeneration; Nucleus; Phosphoprotein; Protease; Zinc.
FT   CHAIN         1   1218       Cytosolic carboxypeptidase 1.
FT                                /FTId=PRO_0000308691.
FT   ACT_SITE    962    962       Nucleophile (By similarity).
FT   METAL       912    912       Zinc (Probable).
FT   METAL       915    915       Zinc (Probable).
FT   METAL      1009   1009       Zinc (By similarity).
FT   MOD_RES    1159   1159       Phosphothreonine (By similarity).
FT   MOD_RES    1160   1160       Phosphoserine (By similarity).
FT   VAR_SEQ     689   1218       Missing (in isoform 5).
FT                                /FTId=VSP_038804.
FT   VAR_SEQ     771    795       GMQPLMYSVQEALNARPWWIRMGTD -> EITSHEAQLPQA
FT                                DRRASPTTPSPSP (in isoform 3).
FT                                /FTId=VSP_029045.
FT   VAR_SEQ     771    789       GMQPLMYSVQEALNARPWW -> DGEETCYKMIVVSTICCK
FT                                D (in isoform 4).
FT                                /FTId=VSP_038803.
FT   VAR_SEQ     790   1218       Missing (in isoform 4).
FT                                /FTId=VSP_038805.
FT   VAR_SEQ     796   1218       Missing (in isoform 3).
FT                                /FTId=VSP_029046.
FT   VAR_SEQ    1160   1174       SPTTYVLDEDEPRFL -> RTRGSSELQLFPAVL (in
FT                                isoform 2).
FT                                /FTId=VSP_029047.
FT   VAR_SEQ    1175   1218       Missing (in isoform 2).
FT                                /FTId=VSP_029048.
FT   VARIANT     832    832       D -> DD (in pcd; pcd(5J) mutant).
FT   MUTAGEN     912    912       H->A: Abolishes ability to rescue
FT                                Purkinje cell degeneration in pcd mice
FT                                when expressed in a transgene.
FT   MUTAGEN     912    912       H->S: Abolishes deglutamylase activity;
FT                                when associated with Q-915.
FT   MUTAGEN     915    915       E->A: Abolishes ability to rescue
FT                                Purkinje cell degeneration in pcd mice
FT                                when expressed in a transgene.
FT   MUTAGEN     915    915       E->Q: Abolishes deglutamylase activity;
FT                                when associated with S-912.
FT   MUTAGEN     971    972       NR->AA: Abolishes ability to rescue
FT                                Purkinje cell degeneration in pcd mice
FT                                when expressed in a transgene.
FT   CONFLICT    237    237       A -> V (in Ref. 1; AAG37102).
FT   CONFLICT    274    274       Q -> R (in Ref. 1; AAG37102).
FT   CONFLICT    380    380       V -> A (in Ref. 3; BC060633).
FT   CONFLICT    542    548       NAGMRKD -> ERRNEEG (in Ref. 1; AAG37102).
FT   CONFLICT    644    644       F -> S (in Ref. 1; AAG37102).
FT   CONFLICT    969    969       D -> G (in Ref. 1; AAG37102).
FT   CONFLICT   1043   1043       D -> G (in Ref. 1; AAG37102).
FT   CONFLICT   1121   1121       K -> Q (in Ref. 1; AAG37102).
FT   CONFLICT   1126   1126       L -> I (in Ref. 2; BAC25412).
FT   CONFLICT   1167   1167       D -> G (in Ref. 2; BAB24963).
SQ   SEQUENCE   1218 AA;  137197 MW;  89917C6897AD9DD5 CRC64;
     MSKLKVVGEK SLTNSSRVVG LLAQLEKINT DSTESDTARY VTSKILHLAQ SQEKTRREMT
     TKGSTGMEVL LSTLENTKDL QTVLNILSIL IELVSSGGGR RASFLVAKGG SQILLQLLMN
     ASKDSPPHEE VMVQTHSILA KIGPKDKKFG VKARVNGALT VTLNLVKQHF QNYRLVLPCL
     QLLRVYSTNS VNSVSLGKNG VVELMFKIIG PFSKKNSGLM KVALDTLAAL LKSKTNARRA
     VDRGYVQVLL TIYVDWHRHD NRHRNMLIRK GILQSLKSVT NIKLGRKAFI DANGMKILYN
     TSQECLAVRT LDPLVNTSSL IMRKCFPKNR LPLPTIKSSF HFQLPIIPVT GPVAQLYSLP
     PEVDDVVDES DDNDDIDLEV ENELENEDDL DQSFKNDDIE TDINKLRPQQ VPGRTIEELK
     MYEHLFPELV DDFQDYELIS KEPKPFVFEG KARGPIVVPT AGEEVPGNSG SVKKGVVMKE
     RASPKGEEAK EDPKGHDRTL PQQLGGQSRV APSAHSFNND LVKALDRITL QNVPSQVASG
     LNAGMRKDFG LPLTVLSCTK ACPHVAKCGS TLFEGRTVHL GKLCCTGVET EDDEDTESHS
     STEQAPSVEA SDGPTLHDPD LYIEIVKNTK SVPEYSEVAY PDYFGHIPPP FKEPILERPY
     GVQRTKIAQD IERLIHQNDI IDRVVYDLDN PTYTTPEEGD TLKFNSKFES GNLRKVIQIR
     KSEYDLILNS DINSNHYHQW FYFEVSGMRP GVAYRFNIIN CEKSNSQFNY GMQPLMYSVQ
     EALNARPWWI RMGTDICYYK NHFSRSSVAA GGQKGKSYYT ITFTVNFPHK DDVCYFAYHY
     PYTYSTLQMH LQKLESAHNP QQIYFRKDVL CETLSGNICP LVTITAMPES NYYEHICQFR
     TRPYIFLSAR VHPGETNASW VMKGTLEYLM SNSPTAQSLR ESYIFKIVPM LNPDGVINGN
     HRCSLSGEDL NRQWQSPNPE LHPTIYHAKG LLQYLAAVKR LPLVYCDYHG HSRKKNVFMY
     GCSIKETVWH THDNSASCDI VEDMGYRTLP KILSHIAPAF CMSSCSFVVE KSKESTARVV
     VWREIGVQRS YTMESTLCGC DQGRYKGLQI GTRELEEMGA KFCVGLLRLK RLTSSLEYNL
     PSNLLDFEND LIESSCKVTS PTTYVLDEDE PRFLEEVDYS AESNDELDVE LAENTGDYEP
     SAQEEALSDS EVSRTHLI
//
ID   NUAK1_MOUSE             Reviewed;         658 AA.
AC   Q641K5; Q6I6D6; Q8CGE1;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=NUAK family SNF1-like kinase 1;
DE            EC=2.7.11.1;
GN   Name=Nuak1; Synonyms=Kiaa0537;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 84-658.
RC   TISSUE=Fetal brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
CC   -!- FUNCTION: Involved in tolerance to glucose starvation.
CC       Phosphorylates ATM. Suppresses Fas-induced apoptosis by
CC       phosphorylation of CASP6, thus suppressing the activation of the
CC       caspase and the subsequent cleavage of CFLAR (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activated by PKB/AKT1 during glucose
CC       starvation. Activated by phosphorylation on Thr-212 by STK11 in
CC       complex with STE20-related adapter-alpha (STRAD alpha) pseudo
CC       kinase and CAB39 (By similarity).
CC   -!- PTM: Ubiquitinated with 'Lys-29'- and 'Lys-33'-linked
CC       polyubiquitins which appear to impede LKB1-mediated
CC       phosphorylation. Deubiquitinated by USP9X (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. SNF1 subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; BC040467; AAH40467.1; -; mRNA.
DR   EMBL; BC082328; AAH82328.1; -; mRNA.
DR   EMBL; AB182364; BAD23995.1; -; mRNA.
DR   IPI; IPI00465504; -.
DR   RefSeq; NP_001004363.1; NM_001004363.1.
DR   UniGene; Mm.25874; -.
DR   ProteinModelPortal; Q641K5; -.
DR   SMR; Q641K5; 54-311.
DR   PhosphoSite; Q641K5; -.
DR   PRIDE; Q641K5; -.
DR   Ensembl; ENSMUST00000020220; ENSMUSP00000020220; ENSMUSG00000020032.
DR   GeneID; 77976; -.
DR   KEGG; mmu:77976; -.
DR   UCSC; uc007gko.1; mouse.
DR   CTD; 77976; -.
DR   MGI; MGI:1925226; Nuak1.
DR   eggNOG; roNOG11620; -.
DR   GeneTree; ENSGT00600000084026; -.
DR   HOGENOM; HBG445847; -.
DR   HOVERGEN; HBG007160; -.
DR   InParanoid; Q641K5; -.
DR   OMA; NRPRPQY; -.
DR   OrthoDB; EOG4KD6KP; -.
DR   PhylomeDB; Q641K5; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 347923; -.
DR   ArrayExpress; Q641K5; -.
DR   Bgee; Q641K5; -.
DR   CleanEx; MM_NUAK1; -.
DR   Genevestigator; Q641K5; -.
DR   GermOnline; ENSMUSG00000020032; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT   CHAIN         1    658       NUAK family SNF1-like kinase 1.
FT                                /FTId=PRO_0000086454.
FT   DOMAIN       56    307       Protein kinase.
FT   NP_BIND      62     70       ATP (By similarity).
FT   ACT_SITE    179    179       Proton acceptor (By similarity).
FT   BINDING      85     85       ATP (By similarity).
FT   MOD_RES      22     22       Phosphoserine (By similarity).
FT   MOD_RES     212    212       Phosphothreonine (By similarity).
FT   MOD_RES     216    216       Phosphoserine (By similarity).
FT   MOD_RES     372    372       Phosphoserine (By similarity).
FT   MOD_RES     381    381       Phosphoserine (By similarity).
FT   MOD_RES     389    389       Phosphoserine (By similarity).
FT   MOD_RES     445    445       Phosphoserine (By similarity).
FT   MOD_RES     446    446       Phosphoserine (By similarity).
FT   MOD_RES     456    456       Phosphoserine (By similarity).
FT   MOD_RES     601    601       Phosphoserine; by PKB/AKT1 (By
FT                                similarity).
SQ   SEQUENCE   658 AA;  73661 MW;  E7176F13B75B899F CRC64;
     MEGAAVSAAG DGPAVETGLP GSPLEAVAGA TAAPVEPRKP HGVKRHHHKH NLKHRYELQE
     TLGKGTYGKV KRATERFSGR VVAIKSIRKD KIKDELDMVH IRREIEIMSS LNHPHIISIY
     EVFENKDKIV IIMEYASKGE LYDYISERRR LSERETRHFF RQIVSAVHYC HKNGVVHRDL
     KLENILLDDN CNIKIADFGL SNLYQKDKFL QTFCGSPLYA SPEIVNGRPY RGPEVDSWAL
     GVLLYTLIYG TMPFDGFDHK NLIRQISSGE YREPTQPSDA RGLIRWMLMV NPDRRATIED
     IANHWWVNWG YKSSVCDCDA LPDSESPLLA RIIDWHHRST GLQAEAEAKM KGLAKPGASE
     VVLERQRSLK KSKKENDFPQ SGQDSVPESP SKLSSKRPKG ILKKRSNSEH RSHSTGFIEG
     IVSPALPSPF KMEQDLCRTA IPLPSSPEAD MSGKLSLKQS ATMPKKGILK KTQQRESGYY
     SSPERSESSE LLDSNDVVIS GGLSSPPPDP ARGTSHSLSC RRKGILKHSS RYSDGGTDPA
     LTRPEMPTLE SLSPPGVPSD GISRSYSRPS SIISDDSVLS SDSFDLLELQ ENRPARQRIR
     SCVSAENFLQ LQDFETPHNR PRPQYLKRLA DSSFSLLTDM DDVTQVYKKA LEICSKLN
//
ID   ARP3B_MOUSE             Reviewed;         418 AA.
AC   Q641P0; Q7TSH1;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   08-FEB-2011, entry version 42.
DE   RecName: Full=Actin-related protein 3B;
DE   AltName: Full=ARP3-beta;
DE   AltName: Full=Actin-like protein 3B;
GN   Name=Actr3b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Plays a role in the organization of the actin
CC       cytoskeleton. May function as ATP-binding component of the Arp2/3
CC       complex which is involved in regulation of actin polymerization
CC       and together with an activating nucleation-promoting factor (NPF)
CC       mediates the formation of branched actin networks. May decrease
CC       the metastatic potential of tumors (By similarity).
CC   -!- SUBUNIT: Interacts with the Arp2/3 complex composed of ARP2, ARP3,
CC       ARPC1B, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-
CC       ARC and ARPC5/p16-ARC (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Cell projection (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q641P0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q641P0-2; Sequence=VSP_034419;
CC   -!- SIMILARITY: Belongs to the actin family. ARP3 subfamily.
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DR   EMBL; BC053106; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC082279; AAH82279.1; -; mRNA.
DR   IPI; IPI00380734; -.
DR   IPI; IPI00620582; -.
DR   RefSeq; NP_001004365.1; NM_001004365.1.
DR   UniGene; Mm.150319; -.
DR   HSSP; P61157; 1U2V.
DR   ProteinModelPortal; Q641P0; -.
DR   SMR; Q641P0; 3-417.
DR   PhosphoSite; Q641P0; -.
DR   PRIDE; Q641P0; -.
DR   Ensembl; ENSMUST00000070431; ENSMUSP00000067564; ENSMUSG00000056367.
DR   Ensembl; ENSMUST00000088244; ENSMUSP00000085578; ENSMUSG00000056367.
DR   GeneID; 242894; -.
DR   KEGG; mmu:242894; -.
DR   UCSC; uc008wtc.1; mouse.
DR   CTD; 242894; -.
DR   MGI; MGI:2661120; Actr3b.
DR   eggNOG; roNOG14108; -.
DR   GeneTree; ENSGT00550000074695; -.
DR   HOVERGEN; HBG003771; -.
DR   PhylomeDB; Q641P0; -.
DR   NextBio; 385602; -.
DR   ArrayExpress; Q641P0; -.
DR   Bgee; Q641P0; -.
DR   Genevestigator; Q641P0; -.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR   InterPro; IPR004000; Actin-like.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR015623; Arp3.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   PANTHER; PTHR11937:SF31; Arp3; 1.
DR   Pfam; PF00022; Actin; 1.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Actin-binding; Alternative splicing; ATP-binding;
KW   Cell projection; Cytoplasm; Cytoskeleton; Nucleotide-binding;
KW   Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    418       Actin-related protein 3B.
FT                                /FTId=PRO_0000342359.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     231    231       Phosphotyrosine (By similarity).
FT   MOD_RES     418    418       Phosphoserine (By similarity).
FT   VAR_SEQ       1     88       Missing (in isoform 2).
FT                                /FTId=VSP_034419.
SQ   SEQUENCE   418 AA;  47580 MW;  3A9E34AF53F2345A CRC64;
     MAGSLPPCVV DCGTGYTKLG YAGNTEPQFI IPSCIAIRES AKVVDQAQRR VLRGVDDLDF
     FIGDEAIDKP TYATKWPIRH GIVEDWDLME RFMEQVVFKY LRAEPEDHYF LMTEPPLNTP
     ENREYLAEIM FESFNVPGLY IAVQAVLALA ASWTSRQVGE RTLTGIVIDS GDGVTHVIPV
     AEGYVIGSCI KHIPIAGRDI TYFIQQLLRE REVGIPPEQS LETAKAIKEK YCYICPDIVR
     EFAKYDVDPR KWIKQYTGIN AINQKKFIID VGYERFLGPE IFFHPEFANP DFMESISDVV
     DEVIQSCPID VRRPLYKNVV LSGGSTMFRD FGRRLQRDLK RVVDARLKLS QELSGGRIKP
     KPVEVQVVTH HMQRYAVWFG GSMLASTPEF FQVCHTKKDY EEYGPSICRH NPVFGVMS
//
ID   SF01_MOUSE              Reviewed;         653 AA.
AC   Q64213; O08817; P70167; Q61454; Q921Z4;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 5.
DT   08-FEB-2011, entry version 91.
DE   RecName: Full=Splicing factor 1;
DE   AltName: Full=CW17;
DE   AltName: Full=Mammalian branch point-binding protein;
DE            Short=BBP;
DE            Short=mBBP;
DE   AltName: Full=Transcription factor ZFM1;
DE            Short=mZFM;
DE   AltName: Full=Zinc finger gene in MEN1 locus;
DE   AltName: Full=Zinc finger protein 162;
GN   Name=Sf1; Synonyms=Zfm1, Zfp162;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS CW17 AND CW17E).
RC   STRAIN=C57BL/10; TISSUE=Spleen;
RX   MEDLINE=97355688; PubMed=9212169;
RA   Wrehlke C., Schmitt-Wrede H.-P., Qiao Z.D., Wunderlich F.;
RT   "Enhanced expression in spleen macrophages of the mouse homolog to the
RT   human putative tumor suppressor gene ZFM1.";
RL   DNA Cell Biol. 16:761-767(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C57B1/10;
RX   MEDLINE=99287587; PubMed=10360842; DOI=10.1089/104454999315303;
RA   Wrehlke C., Wiedemeyer W.-R., Schmitt-Wrede H.-P., Mincheva A.,
RA   Lichter P., Wunderlich F.;
RT   "Genomic organization of mouse gene zfp162 (mzfm).";
RL   DNA Cell Biol. 18:419-428(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS CW17E AND 3).
RC   STRAIN=C3H/He; TISSUE=Mammary tumor, and Osteoblast;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-82, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Necessary for the ATP-dependent first step of
CC       spliceosome assembly. Binds to the intron branch point sequence
CC       (BPS) 5'-UACUAAC-3' of the pre-mRNA. May act as transcription
CC       repressor (By similarity).
CC   -!- SUBUNIT: Binds U2AF2. Interacts with U1 snRNA. Binds EWSR1, FUS
CC       and TAF15 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=CW17;
CC         IsoId=Q64213-1; Sequence=Displayed;
CC       Name=CW17E;
CC         IsoId=Q64213-2; Sequence=VSP_050424;
CC       Name=3;
CC         IsoId=Q64213-3; Sequence=VSP_008840;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Detected at intermediate levels in spleen.
CC       Lower levels in heart, kidney, brain, liver, testis, bone marrow,
CC       adrenal gland, lymph nodes, pancreas and thymus.
CC   -!- PTM: Phosphorylation on Ser-20 interferes with U2AF2 binding and
CC       spliceosome assembly (By similarity).
CC   -!- SIMILARITY: Belongs to the BBP/SF1 family.
CC   -!- SIMILARITY: Contains 1 CCHC-type zinc finger.
CC   -!- SIMILARITY: Contains 1 KH domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; X80159; CAA56440.1; -; mRNA.
DR   EMBL; X85802; CAA59797.1; -; mRNA.
DR   EMBL; Y08907; CAA70113.1; -; Genomic_DNA.
DR   EMBL; Y12838; CAA73359.1; -; Genomic_DNA.
DR   EMBL; BC009091; AAH09091.1; -; mRNA.
DR   EMBL; BC055370; AAH55370.1; -; mRNA.
DR   IPI; IPI00116284; -.
DR   IPI; IPI00387376; -.
DR   IPI; IPI00830819; -.
DR   UniGene; Mm.256422; -.
DR   ProteinModelPortal; Q64213; -.
DR   SMR; Q64213; 134-255.
DR   STRING; Q64213; -.
DR   PhosphoSite; Q64213; -.
DR   PRIDE; Q64213; -.
DR   Ensembl; ENSMUST00000076351; ENSMUSP00000075689; ENSMUSG00000024949.
DR   Ensembl; ENSMUST00000113485; ENSMUSP00000109113; ENSMUSG00000024949.
DR   UCSC; uc008gik.1; mouse.
DR   MGI; MGI:1095403; Sf1.
DR   eggNOG; roNOG09707; -.
DR   GeneTree; ENSGT00550000074434; -.
DR   HOGENOM; HBG282680; -.
DR   HOVERGEN; HBG063318; -.
DR   InParanoid; Q64213; -.
DR   PhylomeDB; Q64213; -.
DR   ArrayExpress; Q64213; -.
DR   Bgee; Q64213; -.
DR   CleanEx; MM_SF1; -.
DR   Genevestigator; Q64213; -.
DR   GermOnline; ENSMUSG00000024949; Mus musculus.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0022402; P:cell cycle process; IGI:MGI.
DR   GO; GO:0033327; P:Leydig cell differentiation; IGI:MGI.
DR   GO; GO:0030238; P:male sex determination; IGI:MGI.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0050810; P:regulation of steroid biosynthetic process; IGI:MGI.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR004088; KH_type_1.
DR   InterPro; IPR018111; KH_type_1_subgr.
DR   InterPro; IPR013084; Znf_CCH_retrovir.
DR   InterPro; IPR001878; Znf_CCHC.
DR   Gene3D; G3DSA:4.10.60.10; Znf_CCH_retrovir; 1.
DR   Pfam; PF00013; KH_1; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   SMART; SM00322; KH; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Metal-binding; mRNA processing;
KW   mRNA splicing; Nucleus; Phosphoprotein; Repressor; RNA-binding;
KW   Spliceosome; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    653       Splicing factor 1.
FT                                /FTId=PRO_0000050130.
FT   DOMAIN      141    222       KH.
FT   ZN_FING     277    296       CCHC-type.
FT   MOTIF        15     19       Nuclear localization signal (Potential).
FT   COMPBIAS    324    585       Pro-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      20     20       Phosphoserine; by PKG (By similarity).
FT   MOD_RES      80     80       Phosphoserine.
FT   MOD_RES      82     82       Phosphoserine.
FT   MOD_RES      87     87       Phosphotyrosine (By similarity).
FT   MOD_RES      89     89       Phosphoserine (By similarity).
FT   VAR_SEQ     529    653       TTTTTTSAGTGSIPPWQQQQAAAAASPGTPQMQGNPTMVPL
FT                                PPGVQPPLPPGAPPPPTCSIECLLCLLSSPNSLCLSPNRAA
FT                                RIPPRGSDGPSHESEDFPRPLVTLPGRQPQQRPWWTGWFGK
FT                                AA -> SLPAAAMARAMRVRTFRAHW (in isoform
FT                                CW17E).
FT                                /FTId=VSP_050424.
FT   VAR_SEQ     586    653       TCSIECLLCLLSSPNSLCLSPNRAARIPPRGSDGPSHESED
FT                                FPRPLVTLPGRQPQQRPWWTGWFGKAA -> PPPPPGSAGM
FT                                MYAPPPPPPPPMDPSNFVTMMGMGVAGMPPFGMPPAPPPPP
FT                                PQN (in isoform 3).
FT                                /FTId=VSP_008840.
FT   CONFLICT    184    184       E -> K (in Ref. 3; AAH09091/AAH55370).
FT   CONFLICT    509    509       P -> S (in Ref. 3; AAH55370).
FT   CONFLICT    524    524       P -> L (in Ref. 3; AAH09091).
FT   CONFLICT    528    528       N -> R (in Ref. 1).
SQ   SEQUENCE   653 AA;  70408 MW;  8228DE3E79AB1BFC CRC64;
     MATGANATPL DFPSKKRKRS RWNQDTMEQK TVIPGMPTVI PPGLTREQER AYIVQLQIED
     LTRKLRTGDL GIPPNPEDRS PSPEPIYNSE GKRLNTREFR TRKKLEEERH TLITEMVALN
     PDFKPPADYK PPATRVSDKV MIPQDEYPEI NFVGLLIGPR GNTLKNIEKE CNAKIMIRGK
     GSVEEGKVGR KDGQMLPGED EPLHALVTAN TMENVKKAVE QIRNILKQGI ETPEDQNDLR
     KMQLRELARL NGTLREDDNR ILRPWQSSET RSITNTTVCT KCGGAGHIAS DCKFQRPGDP
     QSAQDKARMD KEYLSLMAEL GEAPVPASVG STSGPATTPL ASAPRPAAPA SNPPPPSLMS
     TTQSRPPWMN SGPSENRPYH GMHGGGPGGP GGGPHSFPHP LPSLTGGHGG HPMQHNPNGP
     PPPWMQPPPP PMNQGPHPPG HHGPPPMDQY LGSTPVGSGV YRLHQGKGMM PPPPMGMMPP
     PPPPPSGQPP PPPSGPLPPW QQQQQQPPPP PPPSSSMASS TPLPWQQNTT TTTTSAGTGS
     IPPWQQQQAA AAASPGTPQM QGNPTMVPLP PGVQPPLPPG APPPPTCSIE CLLCLLSSPN
     SLCLSPNRAA RIPPRGSDGP SHESEDFPRP LVTLPGRQPQ QRPWWTGWFG KAA
//
ID   Q642K0_MOUSE            Unreviewed;       151 AA.
AC   Q642K0;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   SubName: Full=MCG140959, isoform CRA_a;
DE   SubName: Full=Myl6 protein;
DE   SubName: Full=Myosin, light polypeptide 6, alkali, smooth muscle and non-muscle;
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Myl6; ORFNames=mCG_140959;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Testes;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Stomach;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Stomach;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Stomach;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Stomach;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Stomach;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Stomach;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Stomach;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [11]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Stomach;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC081470; AAH81470.1; -; mRNA.
DR   EMBL; BC089485; AAH89485.1; -; mRNA.
DR   EMBL; BC092214; AAH92214.1; -; mRNA.
DR   EMBL; AK167106; BAE39255.1; -; mRNA.
DR   EMBL; AK167191; BAE39321.1; -; mRNA.
DR   EMBL; AK168450; BAE40353.1; -; mRNA.
DR   EMBL; AK168869; BAE40688.1; -; mRNA.
DR   EMBL; CH466578; EDL24571.1; -; Genomic_DNA.
DR   IPI; IPI00354819; -.
DR   RefSeq; NP_034990.1; NM_010860.3.
DR   UniGene; Mm.337074; -.
DR   ProteinModelPortal; Q642K0; -.
DR   SMR; Q642K0; 4-151.
DR   STRING; Q642K0; -.
DR   PRIDE; Q642K0; -.
DR   Ensembl; ENSMUST00000074642; ENSMUSP00000074216; ENSMUSG00000060680.
DR   GeneID; 17904; -.
DR   KEGG; mmu:17904; -.
DR   UCSC; uc007hnc.1; mouse.
DR   CTD; 17904; -.
DR   GeneTree; ENSGT00590000082921; -.
DR   HOVERGEN; HBG012180; -.
DR   InParanoid; Q642K0; -.
DR   OrthoDB; EOG4JM7R0; -.
DR   NextBio; 292729; -.
DR   Genevestigator; Q642K0; -.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   SMART; SM00054; EFh; 3.
DR   PROSITE; PS50222; EF_HAND_2; 3.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   151 AA;  16961 MW;  25B244E686095233 CRC64;
     MCDFTEDQTA EFKEAFQLFD RTGDGKILYS QCGDVMRALG QNPTNAEVLK VLGNPKSDEM
     NVKVLDFEHF LPMLQTVAKN KDQGTYEDYV EGLRVFDKEG NGTVMGAEIR HVLVTLGEKM
     TEEEVEMLVA GHEDSNGCIN YEELVRMVLN G
//
ID   CD34_MOUSE              Reviewed;         382 AA.
AC   Q64314; Q62550; Q62551;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Hematopoietic progenitor cell antigen CD34;
DE   AltName: CD_antigen=CD34;
DE   Flags: Precursor;
GN   Name=Cd34;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ISOFORM LONG).
RC   STRAIN=129, and BALB/c; TISSUE=Bone marrow;
RX   MEDLINE=91223042; PubMed=1709048; DOI=10.1093/intimm/3.2.175;
RA   Brown J., Greaves M.F., Molgaard H.V.;
RT   "The gene encoding the stem cell antigen, CD34, is conserved in mouse
RT   and expressed in haemopoietic progenitor cell lines, brain, and
RT   embryonic fibroblasts.";
RL   Int. Immunol. 3:175-184(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ISOFORMS LONG AND SHORT).
RX   MEDLINE=92239883; PubMed=1373970;
RA   Suda J., Sudo T., Ito M., Ohno N., Yamaguchi Y., Suda T.;
RT   "Two types of murine CD34 mRNA generated by alternative splicing.";
RL   Blood 79:2288-2295(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-326 AND TYR-336, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-246, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
CC   -!- FUNCTION: Possible adhesion molecule with a role in early
CC       hematopoiesis by mediating the attachment of stem cells to the
CC       bone marrow extracellular matrix or directly to stromal cells.
CC       Could act as a scaffold for the attachment of lineage specific
CC       glycans, allowing stem cells to bind to lectins expressed by
CC       stromal cells or other marrow components. Presents carbohydrate
CC       ligands to selectins (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=Q64314-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=Q64314-2; Sequence=VSP_004161, VSP_004162;
CC   -!- TISSUE SPECIFICITY: Highly expressed in hematopoietic progenitor
CC       cell lines, brain and testis, and moderately in the thymus,
CC       spleen, and bone marrow, but not in adult liver.
CC   -!- PTM: Highly glycosylated (By similarity).
CC   -!- PTM: Phosphorylated on serine residues by PKC (By similarity).
CC   -!- SIMILARITY: Belongs to the CD34 family.
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DR   EMBL; S69293; AAB19246.1; -; mRNA.
DR   EMBL; S69302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; S69295; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; S69299; AAB22108.1; ALT_SEQ; mRNA.
DR   EMBL; S69301; AAB22109.1; -; mRNA.
DR   EMBL; BC006607; AAH06607.1; -; mRNA.
DR   IPI; IPI00133257; -.
DR   IPI; IPI00222348; -.
DR   PIR; I65354; I65354.
DR   RefSeq; NP_598415.1; NM_133654.3.
DR   UniGene; Mm.29798; -.
DR   ProteinModelPortal; Q64314; -.
DR   STRING; Q64314; -.
DR   PhosphoSite; Q64314; -.
DR   PRIDE; Q64314; -.
DR   Ensembl; ENSMUST00000016638; ENSMUSP00000016638; ENSMUSG00000016494.
DR   Ensembl; ENSMUST00000110815; ENSMUSP00000106439; ENSMUSG00000016494.
DR   GeneID; 12490; -.
DR   KEGG; mmu:12490; -.
DR   UCSC; uc007eep.1; mouse.
DR   UCSC; uc007eeq.1; mouse.
DR   CTD; 12490; -.
DR   MGI; MGI:88329; Cd34.
DR   GeneTree; ENSGT00390000008414; -.
DR   HOGENOM; HBG125903; -.
DR   HOVERGEN; HBG003461; -.
DR   InParanoid; Q64314; -.
DR   OMA; TVNFTST; -.
DR   OrthoDB; EOG4GF3G0; -.
DR   PhylomeDB; Q64314; -.
DR   NextBio; 281408; -.
DR   ArrayExpress; Q64314; -.
DR   Bgee; Q64314; -.
DR   CleanEx; MM_CD34; -.
DR   Genevestigator; Q64314; -.
DR   GermOnline; ENSMUSG00000016494; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043199; F:sulfate binding; IDA:MGI.
DR   GO; GO:0050900; P:leukocyte migration; IMP:MGI.
DR   InterPro; IPR008083; CD34.
DR   InterPro; IPR013836; CD34/Podocalyxin.
DR   PANTHER; PTHR16677; CD34; 1.
DR   Pfam; PF06365; CD34_antigen; 1.
DR   PRINTS; PR01700; CD34ANTIGEN.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Glycoprotein; Membrane;
KW   Phosphoprotein; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     34       Potential.
FT   CHAIN        35    382       Hematopoietic progenitor cell antigen
FT                                CD34.
FT                                /FTId=PRO_0000020901.
FT   TOPO_DOM     35    287       Extracellular (Potential).
FT   TRANSMEM    288    308       Helical; (Potential).
FT   TOPO_DOM    309    382       Cytoplasmic (Potential).
FT   MOD_RES     326    326       Phosphotyrosine.
FT   MOD_RES     336    336       Phosphotyrosine.
FT   CARBOHYD     50     50       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     56     56       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     87     87       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    137    137       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    144    144       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    145    145       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    246    246       N-linked (GlcNAc...).
FT   VAR_SEQ     322    325       GEDP -> ELEP (in isoform Short).
FT                                /FTId=VSP_004161.
FT   VAR_SEQ     326    382       Missing (in isoform Short).
FT                                /FTId=VSP_004162.
SQ   SEQUENCE   382 AA;  40983 MW;  EAE611ABE85C4957 CRC64;
     MQVHRDTRAG LLLPWRWVAL CLMSLLHLNN LTSATTETST QGISPSVPTN ESVEENITSS
     IPGSTSHYLI YQDSSKTTPA ISETMVNFTV TSGIPSGSGT PHTFSQPQTS PTGILPTTSD
     SISTSEMTWK SSLPSINVSD YSPNNSSFEM TSPTEPYAYT SSSAPSAIKG EIKCSGIREV
     RLAQGICLEL SEASSCEEFK KEKGEDLIQI LCEKEEAEAD AGASVCSLLL AQSEVRPECL
     LMVLANSTEL PSKLQLMEKH QSDLRKLGIQ SFNKQDIGSH QSYSRKTLIA LVTSGVLLAI
     LGTTGYFLMN RRSWSPTGER LGEDPYYTEN GGGQGYSSGP GASPETQGKA NVTRGAQENG
     TGQATSRNGH SARQHVVADT EL
//
ID   NPDC1_MOUSE             Reviewed;         332 AA.
AC   Q64322;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Neural proliferation differentiation and control protein 1;
DE            Short=NPDC-1;
DE   Flags: Precursor;
GN   Name=Npdc1; Synonyms=Npdc-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=94087786; PubMed=7903403; DOI=10.1002/jnr.490360204;
RA   Galiana E., Bernard R., Borde I., Rouget P., Evrard C.;
RT   "Proliferation and differentiation properties of bipotent glial
RT   progenitor cell lines immortalized with the adenovirus E1A gene.";
RL   J. Neurosci. Res. 36:133-146(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=95183505; PubMed=7878019; DOI=10.1073/pnas.92.5.1560;
RA   Galiana E., Vernier P., Dupont E., Evrard C., Rouget P.;
RT   "Identification of a neural-specific cDNA, NPDC-1, able to down-
RT   regulate cell proliferation and to suppress transformation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:1560-1564(1995).
CC   -!- FUNCTION: Suppresses oncogenic transformation in neural and non-
CC       neural cells and down-regulates neural cell proliferation. Might
CC       be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- TISSUE SPECIFICITY: Expressed in the brain and nervous system. Not
CC       detected in liver, heart, skeletal muscle, spleen, pancreas,
CC       pituitary and adrenal glands. Expression increases when cultured
CC       neural cells are growth-arrested and begin to differentiate.
CC   -!- SIMILARITY: Belongs to the NPDC1/cab-1 family.
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DR   EMBL; X67209; CAA47648.1; -; mRNA.
DR   EMBL; L03814; AAA39836.1; -; mRNA.
DR   IPI; IPI00331534; -.
DR   PIR; I48691; I48691.
DR   UniGene; Mm.1131; -.
DR   STRING; Q64322; -.
DR   PhosphoSite; Q64322; -.
DR   PRIDE; Q64322; -.
DR   Ensembl; ENSMUST00000071442; ENSMUSP00000071387; ENSMUSG00000015094.
DR   MGI; MGI:1099802; Npdc1.
DR   HOVERGEN; HBG052657; -.
DR   OrthoDB; EOG46DM3G; -.
DR   ArrayExpress; Q64322; -.
DR   Bgee; Q64322; -.
DR   Genevestigator; Q64322; -.
DR   GermOnline; ENSMUSG00000015094; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR009635; NPDC1.
DR   PANTHER; PTHR23352; NPDC1; 1.
DR   Pfam; PF06809; NPDC1; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Phosphoprotein; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     34       Potential.
FT   CHAIN        35    332       Neural proliferation differentiation and
FT                                control protein 1.
FT                                /FTId=PRO_0000021831.
FT   TRANSMEM    191    211       Helical; (Potential).
FT   COMPBIAS    151    173       Pro/Ser/Thr-rich.
FT   COMPBIAS    234    244       Pro/Ser/Thr-rich.
FT   MOD_RES     236    236       Phosphoserine (By similarity).
SQ   SEQUENCE   332 AA;  35805 MW;  26D459B9EA1D63B3 CRC64;
     MATPVPPPSP RHLRLLRLLL SGLILGAALN GATARRPDAT TCPGSLDCAL KRRAKCPPGA
     HACGPCLQSF QEDQRGFCVP RKHLSSGEGL PQPRLEEEID SLAQELALKE KEAGHSRLTA
     QPLLERAQKL LEPAATLGFS QWGQRLEPGL PSTHGTSSPI PHTSLSSRAS SGPVQMSPLE
     PQGRHGNGLT LVLILAFCLA SSAALAVAAL CWCRLQREIR LTQKADYAAT AKGPTSPSTP
     RISPGDQRLA HSAEMYHYQH QRQQMLCLER HKEPPKELES ASSDEENEDG DFTVYECPGL
     APTGEMEVRN PLFDHSTLSA PVPGPHSLPP LQ
//
ID   SYN2_MOUSE              Reviewed;         586 AA.
AC   Q64332; Q6NZR0; Q9QWV7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   30-NOV-2010, entry version 83.
DE   RecName: Full=Synapsin-2;
DE   AltName: Full=Synapsin II;
GN   Name=Syn2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IIB).
RC   STRAIN=H129; TISSUE=Brain;
RA   Han S.J.;
RT   "Identification of mouse synapsin IIb.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM IIA).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-126, AND TISSUE SPECIFICITY.
RC   STRAIN=129/Sv;
RX   MEDLINE=94308086; PubMed=8034599;
RA   Chin L.S., Li L., Greengard P.;
RT   "Neuron-specific expression of the synapsin II gene is directed by a
RT   specific core promoter and upstream regulatory elements.";
RL   J. Biol. Chem. 269:18507-18513(1994).
RN   [4]
RP   PROTEIN SEQUENCE OF 59-112; 116-129; 136-143; 178-213; 245-270;
RP   338-353 AND 405-414, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-422 AND SER-426, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Neuronal phosphoprotein that coats synaptic vesicles,
CC       binds to the cytoskeleton, and is believed to function in the
CC       regulation of neurotransmitter release (By similarity).
CC   -!- SUBUNIT: Interacts with CAPON (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=IIa;
CC         IsoId=Q64332-1; Sequence=Displayed;
CC       Name=IIb;
CC         IsoId=Q64332-2; Sequence=VSP_015203, VSP_015204;
CC   -!- TISSUE SPECIFICITY: Expressed exclusively in neuronal cells.
CC   -!- SIMILARITY: Belongs to the synapsin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH66004.1; Type=Erroneous initiation;
CC       Sequence=AAH85129.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF096867; AAC72966.1; -; mRNA.
DR   EMBL; BC066004; AAH66004.1; ALT_INIT; mRNA.
DR   EMBL; BC085129; AAH85129.1; ALT_INIT; mRNA.
DR   EMBL; L32026; AAA79964.1; -; Genomic_DNA.
DR   IPI; IPI00134492; -.
DR   IPI; IPI00469548; -.
DR   PIR; I61260; I61260.
DR   RefSeq; NP_001104485.1; NM_001111015.1.
DR   RefSeq; NP_038709.1; NM_013681.2.
DR   UniGene; Mm.441431; -.
DR   UniGene; Mm.466323; -.
DR   ProteinModelPortal; Q64332; -.
DR   SMR; Q64332; 113-420.
DR   STRING; Q64332; -.
DR   PhosphoSite; Q64332; -.
DR   PRIDE; Q64332; -.
DR   Ensembl; ENSMUST00000009538; ENSMUSP00000009538; ENSMUSG00000009394.
DR   GeneID; 20965; -.
DR   KEGG; mmu:20965; -.
DR   UCSC; uc009dim.1; mouse.
DR   UCSC; uc009din.1; mouse.
DR   CTD; 20965; -.
DR   MGI; MGI:103020; Syn2.
DR   eggNOG; roNOG09210; -.
DR   HOGENOM; HBG445598; -.
DR   HOVERGEN; HBG016354; -.
DR   InParanoid; Q64332; -.
DR   OMA; VDEPHAD; -.
DR   NextBio; 299926; -.
DR   ArrayExpress; Q64332; -.
DR   Bgee; Q64332; -.
DR   CleanEx; MM_SYN2; -.
DR   Genevestigator; Q64332; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; TAS:MGI.
DR   GO; GO:0007269; P:neurotransmitter secretion; IGI:MGI.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR013817; Pre-ATP_grasp.
DR   InterPro; IPR016185; PreATP-grasp-like.
DR   InterPro; IPR001359; Synapsin.
DR   InterPro; IPR020898; Synapsin_ATP-bd_dom.
DR   InterPro; IPR019735; Synapsin_CS.
DR   InterPro; IPR019736; Synapsin_P_site.
DR   InterPro; IPR020897; Synapsin_pre-ATP-grasp_dom.
DR   Gene3D; G3DSA:3.30.1490.20; ATP_grasp_subdomain_1; 1.
DR   Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 2.
DR   Gene3D; G3DSA:3.40.50.20; Pre-ATP_grasp; 1.
DR   Pfam; PF02078; Synapsin; 1.
DR   Pfam; PF02750; Synapsin_C; 1.
DR   Pfam; PF10581; Synapsin_N; 1.
DR   PRINTS; PR01368; SYNAPSIN.
DR   SUPFAM; SSF52440; PreATP-grasp-like; 1.
DR   PROSITE; PS00415; SYNAPSIN_1; 1.
DR   PROSITE; PS00416; SYNAPSIN_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Direct protein sequencing;
KW   Phosphoprotein; Synapse.
FT   CHAIN         1    586       Synapsin-2.
FT                                /FTId=PRO_0000183022.
FT   REGION        1     29       A.
FT   REGION       33    113       B; linker.
FT   REGION      114    421       C; actin-binding and synaptic-vesicle
FT                                binding.
FT   REGION      422    458       G; Pro-rich linker.
FT   REGION      459    537       H; Pro/Ser-rich linker.
FT   REGION      538    586       E.
FT   COMPBIAS    486    499       Poly-Ser.
FT   COMPBIAS    515    520       Poly-Ser.
FT   MOD_RES     422    422       Phosphothreonine.
FT   MOD_RES     426    426       Phosphoserine.
FT   VAR_SEQ     459    479       GPGQPQGMQPPGKVLPPRRLP -> CLQYILDCNGIAVGPK
FT                                QVQAS (in isoform IIb).
FT                                /FTId=VSP_015203.
FT   VAR_SEQ     480    586       Missing (in isoform IIb).
FT                                /FTId=VSP_015204.
SQ   SEQUENCE   586 AA;  63373 MW;  2B1B6A7453E286FC CRC64;
     MMNFLRRRLS DSSFIANLPN GYMTDLQRPE PQQPPPAPGP GAATASAATS AASPGPERRP
     PPAQAPAPQP APQPAPTPSV GSSFFSSLSQ AVKQTAASAG LVDAPAPSAA SRKAKVLLVV
     DEPHTDWAKC FRGKKILGDY DIKVEQAEFS ELNLVAHADG TYAVDMQVLR NGTKVVRSFR
     PDFVLIRQHA FGMAENEDFR HLVIGMQYAG LPSINSLESI YNFCDKPWVF AQMVAIFKTL
     GGEKFPLIEQ TYYPNHREML TLPTFPVVVK IGHAHSGMGK VKVENHYDFQ DIASVVALTQ
     TYATAEPFID AKYDIRVQKI GNNYKAYMRT SISGNWKTNT GSAMLEQIAM SDRYKLWVDA
     CSEMFGGLDI CAVKAVHGKD GKDYIFEVMD CSMPLIGEHQ VEDRQLITDL VISKMNQLLS
     RTPALSPQRP LTTQQPQSGT LKEPDSSKTP PQRPPPQGGP GQPQGMQPPG KVLPPRRLPS
     GPSLPSSSSS SSSSSSSSSA PQRPGGPTTT HGDASSSSNS LAEAQAPQAA PAQKPQPHPQ
     LNKSQSLTNA FSFSESSFFR SSANEDEAKA ETIRSLRKSF ASLFSD
//
ID   TBR1_MOUSE              Reviewed;         681 AA.
AC   Q64336;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=T-box brain protein 1;
DE            Short=T-brain-1;
DE            Short=TBR-1;
DE   AltName: Full=TES-56;
GN   Name=Tbr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Fetal brain;
RX   MEDLINE=95344783; PubMed=7619531; DOI=10.1016/0896-6273(95)90065-9;
RA   Bulfone A., Smiga S.M., Shimamura K., Peterson A., Puelles L.,
RA   Rubenstein J.L.R.;
RT   "T-brain-1: a homolog of Brachyury whose expression defines
RT   molecularly distinct domains within the cerebral cortex.";
RL   Neuron 15:63-78(1995).
CC   -!- FUNCTION: Probable transcriptional regulator involved in
CC       developmental processes. TBR1 is required for normal brain
CC       development.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- TISSUE SPECIFICITY: Expressed in specific lamina in the developing
CC       and adult brain.
CC   -!- DEVELOPMENTAL STAGE: First detected around day 10 of embryonic
CC       development in the preplate, at day 12.5, in the cortical plate
CC       and intermediate zone, and from day 16.5 to 18.5, in a rostro-
CC       caudal gradient in the subplate. In the thalamus, expression is
CC       first observed at postnatal stage, P7, and weak expression
CC       continues in later postnatal and adult stages.
CC   -!- SIMILARITY: Contains 1 T-box DNA-binding domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; U49251; AAA92011.1; -; mRNA.
DR   IPI; IPI00621143; -.
DR   UniGene; Mm.308525; -.
DR   UniGene; Mm.404741; -.
DR   ProteinModelPortal; Q64336; -.
DR   SMR; Q64336; 204-393.
DR   STRING; Q64336; -.
DR   PhosphoSite; Q64336; -.
DR   PRIDE; Q64336; -.
DR   Ensembl; ENSMUST00000048934; ENSMUSP00000046787; ENSMUSG00000035033.
DR   MGI; MGI:107404; Tbr1.
DR   HOGENOM; HBG443799; -.
DR   HOVERGEN; HBG000578; -.
DR   InParanoid; Q64336; -.
DR   OrthoDB; EOG45B1F1; -.
DR   ArrayExpress; Q64336; -.
DR   Bgee; Q64336; -.
DR   CleanEx; MM_TBR1; -.
DR   Genevestigator; Q64336; -.
DR   GermOnline; ENSMUSG00000035033; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0007411; P:axon guidance; IMP:MGI.
DR   GO; GO:0030902; P:hindbrain development; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd.
DR   InterPro; IPR001699; TF_T-box.
DR   InterPro; IPR018186; TF_T-box_CS.
DR   Gene3D; G3DSA:2.60.40.820; TF_T-box; 1.
DR   PANTHER; PTHR11267; TF_T-box; 1.
DR   Pfam; PF00907; T-box; 1.
DR   PRINTS; PR00937; TBOX.
DR   SMART; SM00425; TBOX; 1.
DR   SUPFAM; SSF49417; P53_like_DNA_bnd; 1.
DR   PROSITE; PS01283; TBOX_1; 1.
DR   PROSITE; PS01264; TBOX_2; 1.
DR   PROSITE; PS50252; TBOX_3; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Nucleus; Transcription; Transcription regulation.
FT   CHAIN         1    681       T-box brain protein 1.
FT                                /FTId=PRO_0000184458.
FT   DNA_BIND    213    393       T-box.
FT   COMPBIAS    569    573       Poly-Ala.
SQ   SEQUENCE   681 AA;  73941 MW;  8732EF250EF1D009 CRC64;
     MQLEHCLSPS IMLSKKFLNV SSSYPHSGGS ELVLHDHPII STTDNLERSS PLEKITRGMT
     NQSDTDNFPD SKDSPGDVQR SKLSPVLDGV SELRHSFDGS AADRYLLSQS SQPQSAATAP
     SAMFPYPSQH GPAHPAFSIG SPSRYMAHHP VITNGAYNSL LSNSSPQGYP TAGYPYPQQY
     GHSYQGAPFY QFSSTQPGLV PGKAQVYLCN RPLWLKFHRH QTEMIITKQG RRMFPFLSFN
     ISGLDPTAHY NIFVDVILAD PNHWRFQGGK WVPCGKADTN VQGNRVYMHP DSPNTGAHWM
     RQEISFGKLK LTNNKGASNN NGQMVVLQSL HKYQPRLHVV EVNEDGTEDT SQPGRVQTFT
     FPETQFIAVT AYQNTDITQL KIDHNPFAKG FRDNYDTIYT GCDMDRLTPS PNDSPRSQIV
     PGARYAMAGS FLQDQFVSNY AKARFHPGAG AGPGPGTDRS VPHTNGLLSP QQAEDPGAPS
     PQRWFVTPAN NRLDFAASAY DTATDFAGNA ATLLSYAAAG VKALPLQAAG CTGRPLGYYA
     DPSGWGARSP PQYCGAKSGS VLPCWPNSAA AAARMAGANP YLGEEAEGLA AERSPLAPAA
     EDAKPKDLSD SSWIETPSSI KSIDSSDSGI YEQAKRRRIS PADTPVSESS SPLKSEVLAQ
     RDCEKNCAKD IGGYYGFYSH S
//
ID   SQSTM_MOUSE             Reviewed;         442 AA.
AC   Q64337; Q99JM8;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-FEB-2011, entry version 94.
DE   RecName: Full=Sequestosome-1;
DE   AltName: Full=STONE14;
DE   AltName: Full=Ubiquitin-binding protein p62;
GN   Name=Sqstm1; Synonyms=A170, STAP;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION.
RC   STRAIN=ddY; TISSUE=Macrophage;
RX   MEDLINE=96400280; PubMed=8806656; DOI=10.1006/bbrc.1996.1377;
RA   Ishii T., Yanagawa T., Kawane T., Yuki K., Seita J., Yoshida H.,
RA   Bannai S.;
RT   "Murine peritoneal macrophages induce a novel 60-kDa protein with
RT   structural similarity to a tyrosine kinase p56lck-associated protein
RT   in reponse to oxidative stress.";
RL   Biochem. Biophys. Res. Commun. 226:456-460(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c;
RA   Morris J.C., Long A., Finnerty H., Fitz L., Towler P., Turner K.,
RA   Wood C.R.;
RT   "Murine cDNA similar to EBI3-associated protein p60 mRNA.";
RL   Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   INDUCTION.
RX   MEDLINE=97236275; PubMed=9125146; DOI=10.1006/bbrc.1997.6221;
RA   Ishii T., Yanagawa T., Yuki K., Kawane T., Yoshida H., Bannai S.;
RT   "Low micromolar levels of hydrogen peroxide and proteasome inhibitors
RT   induce the 60-kDa A170 stress protein in murine peritoneal
RT   macrophages.";
RL   Biochem. Biophys. Res. Commun. 232:33-37(1997).
RN   [7]
RP   PHOSPHORYLATION.
RX   MEDLINE=98070921; PubMed=9405250; DOI=10.1006/bbrc.1997.7783;
RA   Yanagawa T., Yuki K., Yoshida H., Bannai S., Ishii T.;
RT   "Phosphorylation of A170 stress protein by casein kinase II-like
RT   activity in macrophages.";
RL   Biochem. Biophys. Res. Commun. 241:157-163(1997).
RN   [8]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=10458914; DOI=10.1006/geno.1999.5902;
RA   Okazaki M., Ito S., Kawakita K., Takeshita S., Kawai S., Makishima F.,
RA   Oda H., Kakinuma A.;
RT   "Cloning, expression profile, and genomic organization of the mouse
RT   STAP/A170 gene.";
RL   Genomics 60:87-95(1999).
RN   [9]
RP   INDUCTION.
RX   PubMed=11162503; DOI=10.1006/bbrc.2000.4107;
RA   Kuusisto E., Suuronen T., Salminen A.;
RT   "Ubiquitin-binding protein p62 expression is induced during apoptosis
RT   and proteasomal inhibition in neuronal cells.";
RL   Biochem. Biophys. Res. Commun. 280:223-228(2001).
RN   [10]
RP   INDUCTION.
RX   MEDLINE=22630149; PubMed=12745069; DOI=10.1016/S0006-291X(03)00728-9;
RA   Aono J., Yanagawa T., Itoh K., Li B., Yoshida H., Kumagai Y.,
RA   Yamamoto M., Ishii T.;
RT   "Activation of Nrf2 and accumulation of ubiquitinated A170 by arsenic
RT   in osteoblasts.";
RL   Biochem. Biophys. Res. Commun. 305:271-277(2003).
RN   [11]
RP   FUNCTION, INDUCTION, INTERACTION WITH TRAF6, AND DISRUPTION PHENOTYPE.
RX   PubMed=14960283; DOI=10.1016/S1534-5807(03)00403-9;
RA   Duran A., Serrano M., Leitges M., Flores J.M., Picard S., Brown J.P.,
RA   Moscat J., Diaz-Meco M.T.;
RT   "The atypical PKC-interacting protein p62 is an important mediator of
RT   RANK-activated osteoclastogenesis.";
RL   Dev. Cell 6:303-309(2004).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [13]
RP   INDUCTION.
RX   PubMed=15890008; DOI=10.1089/ars.2005.7.639;
RA   Holtz W.A., Turetzky J.M., O'Malley K.L.;
RT   "Microarray expression profiling identifies early signaling
RT   transcripts associated with 6-OHDA-induced dopaminergic cell death.";
RL   Antioxid. Redox Signal. 7:639-648(2005).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [15]
RP   FUNCTION, INTERACTION WITH CYLD AND TRAF6, AND IDENTIFICATION IN A
RP   COMPLEX WITH CYLD AND TRAF6.
RX   PubMed=18382763; DOI=10.1172/JCI34257;
RA   Jin W., Chang M., Paul E.M., Babu G., Lee A.J., Reiley W., Wright A.,
RA   Zhang M., You J., Sun S.C.;
RT   "Deubiquitinating enzyme CYLD negatively regulates RANK signaling and
RT   osteoclastogenesis in mice.";
RL   J. Clin. Invest. 118:1858-1866(2008).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; THR-269 AND
RP   THR-272, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Adapter protein which binds ubiquitin and may regulate
CC       the activation of NFKB1 by TNF-alpha, nerve growth factor (NGF)
CC       and interleukin-1. May play a role in titin/TTN downstream
CC       signaling in muscle cells. May regulate signaling cascades through
CC       ubiquitination. May be involved in cell differentiation,
CC       apoptosis, immune response and regulation of K(+) channels.
CC       Adapter that mediates the interaction between TRAF6 and CYLD.
CC   -!- SUBUNIT: Homooligomer or heterooligomer; may form homotypic
CC       arrays. Interacts directly with PRKCI and PRKCZ (Probable).
CC       Interacts with EBI3, LCK, RASA1, PRKCZ, PRKCI, NR2F2, NTRK1,
CC       NTRK2, NTRK3, NBR1, MAP2K5, TRIM55 and MAPKAPK5. Interacts with
CC       the proteasome subunits PSMD4 and PSMC2. Interacts with K63-
CC       polyubiquitinated MAPT/TAU. Interacts with IKBKB through PRKCZ and
CC       PRKCI. Interacts with NGFR through TRAF6 and bridges that complex
CC       to NTRK1. Forms a complex with MAP2K5 and PRKCZ or PRKCI.
CC       Component of a ternary complex with PAWR and PRKCZ. Upon TNF-alpha
CC       stimulation, interacts with RIPK1 problably bridging IKBKB to the
CC       TNF-R1 complex composed of TNF-R1/TNFRSF1A, TRADD and RIPK1. Forms
CC       a complex with JUB/Ajuba, PRKCZ and TRAF6. Forms ternary complexes
CC       with PRKCZ and KCNAB2 or PRKCZ and GABBR3. Interacts with KCNAB1,
CC       GABRR1, GABRR2 and GABRR3. Forms an NGF-induced complex with
CC       IKBKB, PRKCI and TRAF6 (By similarity). Interacts with TRAF6 and
CC       CYLD. Identified in a complex with TRAF6 and CYLD.
CC   -!- INTERACTION:
CC       P60520:GABARAPL2 (xeno); NbExp=1; IntAct=EBI-645025, EBI-720116;
CC       Q9GZQ8:MAP1LC3B (xeno); NbExp=3; IntAct=EBI-645025, EBI-373144;
CC       Q9WVS7:Map2k5; NbExp=2; IntAct=EBI-645025, EBI-446144;
CC       P62991:Rps27a; NbExp=1; IntAct=EBI-645025, EBI-413074;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Late endosome. Nucleus.
CC       Note=Sarcomere. In cardiac muscles localizes to the sarcomeric
CC       band. Localizes to late endosomes. May also localize to the
CC       nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q64337-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q64337-2; Sequence=VSP_015842;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- INDUCTION: By diethylmaleate, paraquat, menadione, sodium arsenite
CC       and cadmium chloride, arsenite and arsenate. By MG132, MG115,
CC       lactacystin and proteasome inhibitor I (PSI). By serum starvation,
CC       okadaic acid and glucose oxidase. Also up-regulated by RANK-L (at
CC       protein level). By etoposide and trichostatin. By the parkinsonian
CC       mimetic 6-hydroxydopamine (6-OHDA). By TGF-beta.
CC   -!- DOMAIN: The UBA domain binds specifically 'Lys-63'-linked
CC       polyubiquitin chains of polyubiquitinated substrates. Mediates the
CC       interaction with TRIM55 (By similarity).
CC   -!- DOMAIN: The OPR domain mediates homooligomerization and
CC       interactions with PRKCZ, PRKCI, MAP2K5 and NBR1 (By similarity).
CC   -!- DOMAIN: The ZZ-type zinc finger mediates the interaction with
CC       RIPK1 (By similarity).
CC   -!- PTM: Phosphorylated. May be phosphorylated by PRKCZ.
CC       Phosphorylated in vitro by TTN (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Impaired induced osteoclastogenesis.
CC   -!- SIMILARITY: Contains 1 OPR domain.
CC   -!- SIMILARITY: Contains 1 UBA domain.
CC   -!- SIMILARITY: Contains 1 ZZ-type zinc finger.
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DR   EMBL; U40930; AAB17127.1; -; mRNA.
DR   EMBL; U57413; AAB02908.1; -; mRNA.
DR   EMBL; AK028898; BAC26183.1; -; mRNA.
DR   EMBL; AL627187; CAI25117.1; -; Genomic_DNA.
DR   EMBL; AL627187; CAI25118.1; -; Genomic_DNA.
DR   EMBL; BC006019; AAH06019.1; -; mRNA.
DR   IPI; IPI00133374; -.
DR   IPI; IPI00474373; -.
DR   PIR; JC4978; JC4978.
DR   RefSeq; NP_035148.1; NM_011018.2.
DR   UniGene; Mm.40828; -.
DR   PDB; 2ZJD; X-ray; 1.56 A; B/D=334-344.
DR   PDB; 3ADE; X-ray; 2.80 A; B=346-359.
DR   PDBsum; 2ZJD; -.
DR   PDBsum; 3ADE; -.
DR   ProteinModelPortal; Q64337; -.
DR   SMR; Q64337; 3-101, 126-171, 389-438.
DR   IntAct; Q64337; 14.
DR   STRING; Q64337; -.
DR   PhosphoSite; Q64337; -.
DR   PRIDE; Q64337; -.
DR   Ensembl; ENSMUST00000102774; ENSMUSP00000099835; ENSMUSG00000015837.
DR   GeneID; 18412; -.
DR   KEGG; mmu:18412; -.
DR   UCSC; uc007irw.1; mouse.
DR   UCSC; uc007irx.1; mouse.
DR   CTD; 18412; -.
DR   MGI; MGI:107931; Sqstm1.
DR   eggNOG; roNOG04229; -.
DR   GeneTree; ENSGT00390000002781; -.
DR   HOGENOM; HBG402810; -.
DR   HOVERGEN; HBG052750; -.
DR   InParanoid; Q64337; -.
DR   OMA; SPFGHLS; -.
DR   NextBio; 294036; -.
DR   ArrayExpress; Q64337; -.
DR   Bgee; Q64337; -.
DR   CleanEx; MM_SQSTM1; -.
DR   Genevestigator; Q64337; -.
DR   GermOnline; ENSMUSG00000015837; Mus musculus.
DR   GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005080; F:protein kinase C binding; ISS:UniProtKB.
DR   GO; GO:0042169; F:SH2 domain binding; ISS:UniProtKB.
DR   GO; GO:0003712; F:transcription cofactor activity; TAS:MGI.
DR   GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0016236; P:macroautophagy; ISS:UniProtKB.
DR   GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB cascade; ISS:UniProtKB.
DR   InterPro; IPR000270; OPR_PB1.
DR   InterPro; IPR009060; UBA-like.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   InterPro; IPR000433; Znf_ZZ.
DR   Pfam; PF00564; PB1; 1.
DR   Pfam; PF00569; ZZ; 1.
DR   SMART; SM00666; PB1; 1.
DR   SMART; SM00165; UBA; 1.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF46934; UBA_like; 1.
DR   PROSITE; PS50030; UBA; 1.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Apoptosis; Cytoplasm;
KW   Differentiation; Endosome; Immunity; Metal-binding; Nucleus;
KW   Phosphoprotein; Zinc; Zinc-finger.
FT   CHAIN         1    442       Sequestosome-1.
FT                                /FTId=PRO_0000072177.
FT   DOMAIN       20    102       OPR.
FT   DOMAIN      391    436       UBA.
FT   ZN_FING     122    167       ZZ-type.
FT   REGION        1     50       Interaction with LCK (By similarity).
FT   REGION       43    107       Interaction with PRKCZ and dimerization
FT                                (By similarity).
FT   REGION       50     80       Interaction with PAWR (By similarity).
FT   REGION      122    224       Interaction with GABRR3 (By similarity).
FT   REGION      170    220       LIM protein-binding (LB).**interaction
FT                                with ajuba and probably limd1 (By
FT                                similarity).
FT   REGION      269    442       Interaction with NTRK1 (By similarity).
FT   MOTIF       228    233       TRAF6-binding (By similarity).
FT   COMPBIAS    272    296       Ser-rich.
FT   MOD_RES      24     24       Phosphoserine.
FT   MOD_RES     148    148       Phosphotyrosine (By similarity).
FT   MOD_RES     176    176       Phosphoserine (By similarity).
FT   MOD_RES     178    178       Phosphoserine.
FT   MOD_RES     207    207       Phosphoserine (By similarity).
FT   MOD_RES     266    266       Phosphoserine (By similarity).
FT   MOD_RES     269    269       Phosphothreonine.
FT   MOD_RES     272    272       Phosphothreonine.
FT   MOD_RES     276    276       Phosphoserine (By similarity).
FT   MOD_RES     277    277       Phosphoserine (By similarity).
FT   MOD_RES     330    330       Phosphoserine (By similarity).
FT   MOD_RES     334    334       Phosphoserine.
FT   MOD_RES     357    357       Phosphoserine (By similarity).
FT   MOD_RES     363    363       Phosphoserine (By similarity).
FT   MOD_RES     367    367       Phosphoserine.
FT   MOD_RES     368    368       Phosphoserine (By similarity).
FT   MOD_RES     372    372       Phosphoserine (By similarity).
FT   VAR_SEQ     353    390       Missing (in isoform 2).
FT                                /FTId=VSP_015842.
SQ   SEQUENCE   442 AA;  48163 MW;  ED4CCCA7741D35CA CRC64;
     MASFTVKAYL LGKEEATREI RRFSFCFSPE PEAEAQAAAG PGPCERLLSR VAVLFPTLRP
     GGFQAHYRDE DGDLVAFSSD EELTMAMSYV KDDIFRIYIK EKKECRREHR PPCAQEAPRN
     MVHPNVICDG CNGPVVGTRY KCSVCPDYDL CSVCEGKGLH REHSKLIFPN PFGHLSDSFS
     HSRWLRKLKH GHFGWPGWEM GPPGNWSPRP PRAGDGRPCP TAESASAPPE DPNVNFLKNV
     GESVAAALSP LGIEVDIDVE HGGKRSRLTP TTPESSSTGT EDKSNTQPSS CSSEVSKPDG
     AGEGPAQSLT EQMKKIALES VGQPEEQMES GNCSGGDDDW THLSSKEVDP STGELQSLQM
     PESEGPSSLD PSQEGPTGLK EAALYPHLPP EADPRLIESL SQMLSMGFSD EGGWLTRLLQ
     TKNYDIGAAL DTIQYSKHPP PL
//
ID   PDE1C_MOUSE             Reviewed;         706 AA.
AC   Q64338; Q62045; Q8BSV6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C;
DE            Short=Cam-PDE 1C;
DE            EC=3.1.4.17;
GN   Name=Pde1c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=96411795; PubMed=8810348; DOI=10.1074/jbc.271.41.25699;
RA   Yan C., Zhao A.Z., Bentley J.K., Beavo J.A.;
RT   "The calmodulin-dependent phosphodiesterase gene PDE1C encodes several
RT   functionally different splice variants in a tissue-specific manner.";
RL   J. Biol. Chem. 271:25699-25706(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Pituitary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Cyclic nucleotide phosphodiesterase with a dual-
CC       specificity for the second messengers cAMP and cGMP, which are key
CC       regulators of many important physiological processes. Has a high
CC       affinity for both cAMP and cGMP.
CC   -!- CATALYTIC ACTIVITY: Nucleoside 3',5'-cyclic phosphate + H(2)O =
CC       nucleoside 5'-phosphate.
CC   -!- COFACTOR: Binds 2 divalent metal cations per subunit. Site 1 may
CC       preferentially bind zinc ions, while site 2 has a preference for
CC       magnesium and/or manganese ions (By similarity).
CC   -!- ENZYME REGULATION: Type I PDE are activated by the binding of
CC       calmodulin in the presence of Ca(2+).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Additional isoforms seem to exist;
CC       Name=3;
CC         IsoId=Q64338-3; Sequence=Displayed;
CC       Name=1; Synonyms=PDE1C4, PDE1C5;
CC         IsoId=Q64338-1; Sequence=VSP_012381, VSP_012382;
CC       Name=2; Synonyms=PDE1C1;
CC         IsoId=Q64338-2; Sequence=VSP_004554, VSP_012380;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is highly expressed in testis.
CC       Isoform 2 is highly expressed in heart and testis, and detected at
CC       lower levels in olfactory epithelium and cerebellum.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
CC       family. PDE1 subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; L76947; AAC37702.1; -; mRNA.
DR   EMBL; L76946; AAC37703.1; -; mRNA.
DR   EMBL; L76944; AAC37701.1; -; mRNA.
DR   EMBL; AK030423; BAC26956.1; -; mRNA.
DR   IPI; IPI00133376; -.
DR   IPI; IPI00225618; -.
DR   IPI; IPI00466650; -.
DR   RefSeq; NP_001020739.1; NM_001025568.2.
DR   RefSeq; NP_001153424.1; NM_001159952.1.
DR   RefSeq; NP_001153425.1; NM_001159953.1.
DR   RefSeq; NP_001153427.1; NM_001159955.1.
DR   RefSeq; NP_001153432.1; NM_001159960.1.
DR   RefSeq; NP_035184.1; NM_011054.4.
DR   UniGene; Mm.5145; -.
DR   ProteinModelPortal; Q64338; -.
DR   SMR; Q64338; 78-525.
DR   STRING; Q64338; -.
DR   PhosphoSite; Q64338; -.
DR   PRIDE; Q64338; -.
DR   Ensembl; ENSMUST00000044505; ENSMUSP00000046601; ENSMUSG00000004347.
DR   Ensembl; ENSMUST00000101372; ENSMUSP00000098923; ENSMUSG00000004347.
DR   Ensembl; ENSMUST00000114327; ENSMUSP00000109966; ENSMUSG00000004347.
DR   GeneID; 18575; -.
DR   KEGG; mmu:18575; -.
DR   UCSC; uc009caz.1; mouse.
DR   UCSC; uc009cbb.1; mouse.
DR   UCSC; uc009cbe.1; mouse.
DR   CTD; 18575; -.
DR   MGI; MGI:108413; Pde1c.
DR   GeneTree; ENSGT00550000074309; -.
DR   HOGENOM; HBG315720; -.
DR   HOVERGEN; HBG056120; -.
DR   InParanoid; Q64338; -.
DR   OMA; KTDKKDH; -.
DR   OrthoDB; EOG4NZTSR; -.
DR   PhylomeDB; Q64338; -.
DR   BRENDA; 3.1.4.17; 244.
DR   ArrayExpress; Q64338; -.
DR   Bgee; Q64338; -.
DR   CleanEx; MM_PDE1C; -.
DR   Genevestigator; Q64338; -.
DR   GermOnline; ENSMUSG00000004347; Mus musculus.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR003607; Metal-dep_PHydrolase_HD_dom.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR023174; PDEase_CS.
DR   InterPro; IPR013706; PDEase_N.
DR   Gene3D; G3DSA:1.10.1300.10; PDEase_catalytic_dom; 2.
DR   Pfam; PF00233; PDEase_I; 1.
DR   Pfam; PF08499; PDEase_I_N; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00471; HDc; 1.
DR   PROSITE; PS00126; PDEASE_I; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Calmodulin-binding; cAMP; cGMP; Hydrolase;
KW   Metal-binding; Phosphoprotein.
FT   CHAIN         1    706       Calcium/calmodulin-dependent 3',5'-cyclic
FT                                nucleotide phosphodiesterase 1C.
FT                                /FTId=PRO_0000198793.
FT   REGION      202    521       Catalytic (By similarity).
FT   ACT_SITE    228    228       Proton donor (By similarity).
FT   METAL       232    232       Divalent metal cation 1 (By similarity).
FT   METAL       268    268       Divalent metal cation 1 (By similarity).
FT   METAL       269    269       Divalent metal cation 1 (By similarity).
FT   METAL       269    269       Divalent metal cation 2 (By similarity).
FT   METAL       376    376       Divalent metal cation 1 (By similarity).
FT   MOD_RES       3      3       Phosphoserine (By similarity).
FT   MOD_RES     469    469       Phosphoserine (By similarity).
FT   VAR_SEQ     628    631       GTKK -> DPEE (in isoform 2).
FT                                /FTId=VSP_004554.
FT   VAR_SEQ     632    706       Missing (in isoform 2).
FT                                /FTId=VSP_012380.
FT   VAR_SEQ     651    654       VIKP -> GDYG (in isoform 1).
FT                                /FTId=VSP_012381.
FT   VAR_SEQ     655    706       Missing (in isoform 1).
FT                                /FTId=VSP_012382.
SQ   SEQUENCE   706 AA;  80290 MW;  1F58533E1259801F CRC64;
     MESPTKEIEE FESNSLKHLQ PEQIEKIWLR LRGLRKYKKT SQRLRSLVKQ LERGEASVVD
     LKKNLEYAAT VLESVYIDET RRLLDTEDEL SDIQSDAVPS EVRDWLASTF TRQMGMMLRR
     SDEKPRFKSI VHAVQAGIFV ERMYRRTSNM VGLSYPPAVI DALKDVDTWS FDVFSLNEAS
     GDHALKFIFY ELLTRYDLIS RFKIPISALV SFVEALEVGY SKHKNPYHNL MHAADVTQTV
     HYLLYKTGVA NWLTELEIFA IIFSAAIHDY EHTGTTNNFH IQTRSDPAIL YNDRSVLENH
     HLSAAYRLLQ EDEEMNILVN LSKDDWREFR TLVIEMVMAT DMSCHFQQIK AMKTALQQPE
     AIEKPKALSL MLHTADISHP AKAWDLHHRW TMSLLEEFFR QGDREAELGL PFSPLCDRKS
     TMVAQSQVGF IDFIVEPTFT VLTDMTEKIV SPLIDESSQT GGTGQRRSSL NSINSSDAKR
     SGVKSSGSDG SAPINNSVIP VDYKSFKATW TEVVQINRER WRAKVPKEEK AKKEAEEKAR
     LAAEEKQKEM EAKSQAEQGT TSKGEKKTSG EAKSQVNGTR KGDNPRGKNS KGEKAGEKQQ
     NGDLKDGKNK ADKKDHSNTG NESKKTDGTK KRSHGSPAPS TSSTSRITLP VIKPPLRHFK
     RPAYASSSYA PSVPKKTDDH PVRYKMLDQR IKMKKIQNIS HHWNKK
//
ID   ATP4A_MOUSE             Reviewed;        1033 AA.
AC   Q64436; Q9CV46;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Potassium-transporting ATPase alpha chain 1;
DE            EC=3.6.3.10;
DE   AltName: Full=Gastric H(+)/K(+) ATPase subunit alpha;
DE   AltName: Full=Proton pump;
GN   Name=Atp4a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Gastric mucosa;
RX   MEDLINE=95282844; PubMed=7762614;
RA   Mathews P.M., Claeys D., Jaisser F., Geering K., Horisberger J.-D.,
RA   Kraehenbuhl J.-P., Rossier B.C.;
RT   "Primary structure and functional expression of the mouse and frog
RT   alpha-subunit of the gastric H(+)-K(+)-ATPase.";
RL   Am. J. Physiol. 268:C1207-C1214(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 222-249; 369-386; 486-496; 622-634; 659-667 AND
RP   776-783, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 822-1033.
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the
CC       exchange of H(+) and K(+) ions across the plasma membrane.
CC       Responsible for acid production in the stomach.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) + K(+)(Out) = ADP +
CC       phosphate + H(+)(Out) + K(+)(In).
CC   -!- SUBUNIT: Composed of two subunits: alpha (catalytic) and beta.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       (TC 3.A.3) family. Type IIC subfamily.
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DR   EMBL; U17282; AAA79514.1; -; mRNA.
DR   EMBL; AK009676; BAB26432.1; -; mRNA.
DR   IPI; IPI00230680; -.
DR   PIR; I49143; I49143.
DR   UniGene; Mm.12821; -.
DR   ProteinModelPortal; Q64436; -.
DR   SMR; Q64436; 1-33, 41-1033.
DR   STRING; Q64436; -.
DR   PhosphoSite; Q64436; -.
DR   PRIDE; Q64436; -.
DR   Ensembl; ENSMUST00000005692; ENSMUSP00000005692; ENSMUSG00000005553.
DR   UCSC; uc009gfz.1; mouse.
DR   MGI; MGI:88113; Atp4a.
DR   eggNOG; maNOG17678; -.
DR   HOGENOM; HBG456486; -.
DR   HOVERGEN; HBG004298; -.
DR   InParanoid; Q64436; -.
DR   OrthoDB; EOG41C6VF; -.
DR   BRENDA; 3.6.3.10; 244.
DR   ArrayExpress; Q64436; -.
DR   Bgee; Q64436; -.
DR   Genevestigator; Q64436; -.
DR   GermOnline; ENSMUSG00000005553; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008900; F:hydrogen:potassium-exchanging ATPase activity; IDA:MGI.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
DR   GO; GO:0045851; P:pH reduction; IDA:MGI.
DR   GO; GO:0010155; P:regulation of proton transport; IDA:MGI.
DR   GO; GO:0042493; P:response to drug; IDA:MGI.
DR   InterPro; IPR023306; ATPase_cation_domN.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR005775; ATPase_P-typ_cation-ex_asu_euk.
DR   InterPro; IPR006069; ATPase_P-typ_cation-exchng_asu.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023300; ATPase_P-typ_cyto_domA.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR015127; ATPase_P-typ_H/K-transp_N.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Gene3D; G3DSA:2.70.150.10; ATPase_P-typ_cyto_domA; 1.
DR   Gene3D; G3DSA:3.40.1110.10; ATPase_P-typ_cyto_domN; 1.
DR   Gene3D; G3DSA:1.20.1110.10; ATPase_P-typ_TM_dom; 2.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF09040; H-K_ATPase_N; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00121; NAKATPASE.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81660; ATPase_cation_domN; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01106; ATPase-IIC_X-K; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 4.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Hydrogen ion transport;
KW   Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Potassium; Potassium transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1033       Potassium-transporting ATPase alpha chain
FT                                1.
FT                                /FTId=PRO_0000046254.
FT   TOPO_DOM      2     96       Cytoplasmic (Potential).
FT   TRANSMEM     97    117       Helical; (Potential).
FT   TOPO_DOM    118    140       Lumenal (Potential).
FT   TRANSMEM    141    161       Helical; (Potential).
FT   TOPO_DOM    162    297       Cytoplasmic (Potential).
FT   TRANSMEM    298    317       Helical; (Potential).
FT   TOPO_DOM    318    329       Lumenal (Potential).
FT   TRANSMEM    330    347       Helical; (Potential).
FT   TOPO_DOM    348    781       Cytoplasmic (Potential).
FT   TRANSMEM    782    801       Helical; (Potential).
FT   TOPO_DOM    802    811       Lumenal (Potential).
FT   TRANSMEM    812    832       Helical; (Potential).
FT   TOPO_DOM    833    852       Cytoplasmic (Potential).
FT   TRANSMEM    853    875       Helical; (Potential).
FT   TOPO_DOM    876    927       Lumenal (Potential).
FT   TRANSMEM    928    947       Helical; (Potential).
FT   TOPO_DOM    948    961       Cytoplasmic (Potential).
FT   TRANSMEM    962    980       Helical; (Potential).
FT   TOPO_DOM    981    995       Lumenal (Potential).
FT   TRANSMEM    996   1016       Helical; (Potential).
FT   TOPO_DOM   1017   1033       Cytoplasmic (Potential).
FT   ACT_SITE    385    385       4-aspartylphosphate intermediate (By
FT                                similarity).
FT   METAL       726    726       Magnesium (By similarity).
FT   METAL       730    730       Magnesium (By similarity).
FT   MOD_RES     952    952       Phosphoserine; by PKA (By similarity).
FT   CONFLICT    828    828       S -> F (in Ref. 3; BAB26432).
FT   CONFLICT   1030   1031       DF -> EL (in Ref. 3; BAB26432).
SQ   SEQUENCE   1033 AA;  114016 MW;  C2A812256439766D CRC64;
     MGKEKYELYS VELGSGPGGD MTAKMSKKKA GGGGGKKKEK LENMKKEMEI NDHQLSVSEL
     EQKYQTSATK GLKASLAAEL LLRDGPNALR PPRGTPEYVK FARQLAGGLQ CLMWVAAAIC
     LIAFAIQASE GDLTTDDNLY LAVALIAVVV VTGCFGYYQE FKSTNIIASF KNLVPQQATV
     IRDGDKFQIN ADQLVVGDLV EMKGGDRVPA DIRILSAQGC KVDNSSLTGE SEPQTRSPEC
     THESPLETRN IAFFSTMCLE GTAQGLVVST GDRTIIGRIA SLASGVENEK TPIAIEIEHF
     VDIIAGLAIL FGATFFVVAM CIGYTFLRAM VFFMAIVVAY VPEGLLATVT VCLSLTAKRL
     ASKNCVVKNL EAVETLGSTS VICSDKTGTL TQNRMTVSHL WFDNHIHTAD TTEDQSGQTF
     DQSSETWRAL CRVLTLCNRA AFKSGQDAVP VPKRIVIGDA SETALLKFSE LTLGNAMGYR
     DRFPKVCEIP FNSTNKFQLS IHTLEDPRDS RHLLVMKGAP ERVLERCSSI LIKGQELPLD
     EQWREAFQTA YLSLGGLGER VLGFCQLYLN EKDYPPGYAF DVEAMNFPSS GLCFAGLVSM
     IDPPRATVPD AVLKCRTAGI RVIMVTGDHP ITAKAIAASV GIISEGSETV EDIAARLRMP
     VDQVNRKDAR ACVINGMQLK DMDPSELVEA LRTHPEMVFA RTSPQQKLVI VESCQRLGAI
     VAVTGDGVND SPALKKADIG VAMGIAGSDA AKNAADMILL DDNFASIVTG VEQGRLIFDN
     LKKSIAYTLT KNIPELTPYL IYITVSVPLP LGCITILFIE LCTDIFPSVS LAYEKAESDI
     MHLRPRNPKR DRLVNEPLAA YSYFQIGAIQ SFAGFADYFT AMAQEGWFPL LCVGLRPQWE
     DHHLQDLQDS YGQEWTFGQR LYQQYTCYTV FFISIEMCQI ADVLIRKTRR LSVFQQGFFR
     NKILVIAIVF QVCIGCFLCY CPGMPNIFNF MPIRFQWWLV PMPFGLLIFV YDEIRKLGVR
     CCPGSWWDQD FYY
//
ID   ATP7B_MOUSE             Reviewed;        1462 AA.
AC   Q64446;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 106.
DE   RecName: Full=Copper-transporting ATPase 2;
DE            EC=3.6.3.4;
DE   AltName: Full=Copper pump 2;
DE   AltName: Full=Wilson disease-associated protein homolog;
GN   Name=Atp7b; Synonyms=Wnd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=DAT; TISSUE=Liver;
RX   MEDLINE=97049969; PubMed=8894697; DOI=10.1093/hmg/5.10.1619;
RA   Theophilos M.B., Cox D.W., Mercer J.F.B.;
RT   "The toxic milk mouse is a murine model of Wilson disease.";
RL   Hum. Mol. Genet. 5:1619-1624(1996).
CC   -!- FUNCTION: Involved in the export of copper out of the cells, such
CC       as the efflux of hepatic copper into the bile (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + Cu(2+)(In) = ADP + phosphate +
CC       Cu(2+)(Out).
CC   -!- SUBUNIT: Monomer. Interacts with COMMD1/MURR1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC       membrane; Multi-pass membrane protein (By similarity).
CC       Note=Predominantly found in the trans-Golgi network (TGN). Not
CC       redistributed to the plasma membrane in response to elevated
CC       copper levels (By similarity).
CC   -!- TISSUE SPECIFICITY: Detected in liver and kidney.
CC   -!- DISEASE: Note=Defects in Atp7b are the cause of the toxic milk
CC       mouse mutant (tx) phenotype, characterized by accumulation of
CC       copper in the liver in a manner similar to that observed in
CC       patients with Wilson disease.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       (TC 3.A.3) family. Type IB subfamily.
CC   -!- SIMILARITY: Contains 6 HMA domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; U38477; AAC52852.1; -; mRNA.
DR   IPI; IPI00134479; -.
DR   UniGene; Mm.87854; -.
DR   ProteinModelPortal; Q64446; -.
DR   SMR; Q64446; 69-635, 792-910, 1005-1318.
DR   STRING; Q64446; -.
DR   PhosphoSite; Q64446; -.
DR   PRIDE; Q64446; -.
DR   Ensembl; ENSMUST00000006742; ENSMUSP00000006742; ENSMUSG00000006567.
DR   UCSC; uc009lck.1; mouse.
DR   MGI; MGI:103297; Atp7b.
DR   eggNOG; roNOG09411; -.
DR   GeneTree; ENSGT00530000063773; -.
DR   HOGENOM; HBG507745; -.
DR   HOVERGEN; HBG050616; -.
DR   InParanoid; Q64446; -.
DR   OrthoDB; EOG43N7BZ; -.
DR   PhylomeDB; Q64446; -.
DR   ArrayExpress; Q64446; -.
DR   Bgee; Q64446; -.
DR   CleanEx; MM_ATP7B; -.
DR   Genevestigator; Q64446; -.
DR   GermOnline; ENSMUSG00000006567; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; ISS:HGNC.
DR   GO; GO:0005507; F:copper ion binding; ISS:HGNC.
DR   GO; GO:0004008; F:copper-exporting ATPase activity; IDA:MGI.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006878; P:cellular copper ion homeostasis; IMP:MGI.
DR   GO; GO:0006882; P:cellular zinc ion homeostasis; IMP:MGI.
DR   GO; GO:0015680; P:intracellular copper ion transport; IMP:MGI.
DR   GO; GO:0007595; P:lactation; IMP:MGI.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR006403; ATPase_P-typ_cat/Cu-transptr.
DR   InterPro; IPR023300; ATPase_P-typ_cyto_domA.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR006416; ATPase_P-typ_heavy-metal.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR006122; Cu_ion-bd.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   InterPro; IPR017969; Heavy-metal-associated_CS.
DR   InterPro; IPR006121; HeavyMe_transpt.
DR   Gene3D; G3DSA:2.70.150.10; ATPase_P-typ_cyto_domA; 1.
DR   Gene3D; G3DSA:3.40.1110.10; ATPase_P-typ_cyto_domN; 1.
DR   Gene3D; G3DSA:3.40.50.1000; HAD-like_dom; 2.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00403; HMA; 6.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00942; CUATPASEI.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   SUPFAM; SSF55008; HeavyMe_transpt; 6.
DR   TIGRFAMs; TIGR01511; ATPase-IB1_Cu; 1.
DR   TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR   TIGRFAMs; TIGR00003; Cu_ion_bd; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 5.
DR   PROSITE; PS50846; HMA_2; 6.
PE   1: Evidence at protein level;
KW   ATP-binding; Copper; Copper transport; Disease mutation;
KW   Golgi apparatus; Hydrolase; Ion transport; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1   1462       Copper-transporting ATPase 2.
FT                                /FTId=PRO_0000046315.
FT   TOPO_DOM      1    655       Cytoplasmic (Potential).
FT   TRANSMEM    656    677       Helical; (Potential).
FT   TOPO_DOM    678    699       Extracellular (Potential).
FT   TRANSMEM    700    719       Helical; (Potential).
FT   TOPO_DOM    720    726       Cytoplasmic (Potential).
FT   TRANSMEM    727    747       Helical; (Potential).
FT   TOPO_DOM    748    766       Extracellular (Potential).
FT   TRANSMEM    767    787       Helical; (Potential).
FT   TOPO_DOM    788    921       Cytoplasmic (Potential).
FT   TRANSMEM    922    944       Helical; (Potential).
FT   TOPO_DOM    945    974       Extracellular (Potential).
FT   TRANSMEM    975    996       Helical; (Potential).
FT   TOPO_DOM    997   1319       Cytoplasmic (Potential).
FT   TRANSMEM   1320   1337       Helical; (Potential).
FT   TOPO_DOM   1338   1348       Extracellular (Potential).
FT   TRANSMEM   1349   1368       Helical; (Potential).
FT   TOPO_DOM   1369   1462       Cytoplasmic (Potential).
FT   DOMAIN       69    135       HMA 1.
FT   DOMAIN      154    220       HMA 2.
FT   DOMAIN      268    334       HMA 3.
FT   DOMAIN      362    428       HMA 4.
FT   DOMAIN      491    557       HMA 5.
FT   DOMAIN      567    633       HMA 6.
FT   ACT_SITE   1029   1029       4-aspartylphosphate intermediate (By
FT                                similarity).
FT   METAL      1264   1264       Magnesium (By similarity).
FT   METAL      1268   1268       Magnesium (By similarity).
FT   VARIANT    1356   1356       M -> V (in tx mice).
SQ   SEQUENCE   1462 AA;  157298 MW;  67F5C659CE9A54CD CRC64;
     MDPRKNLASV GTMPEQERQV TAKEASRKIL SKLALPGRPW EQSMKQSFAF DNVGYEGGLD
     STSSSPAATD VVNILGMTCH SCVKSIEDRI SSLKGIVNIK VSLEQGKHTV RYVPSVMNLQ
     QICLQIEDMG FEASAAEGKA ASWPSRSSPA QEAVVKLRVE GMTCQSCVSS IEGKIRKLQG
     VVRIKVSLSN QEAVITYQPY LIQPEDLRDH ICDMGFEAAI KNRTAPLRLG PIDVNKLEST
     NLKKETVSPV QISNHFETLG HQGSYLATLP LRIDGMHCKS CVLNIEGNIG QLPGVQNIHV
     SLENKTAQIQ YDPSCVTPMF LQTAIEALPP GHFKVSLPDG VEENEPQSGS SQRHQEQGPG
     RTAVLTISGI TCASSVQPIE DMLSQRKGVQ QTSISLAEGT GAVLYDPSIV SLDELRTAVE
     DMGFEVSVNS ETFTINPVRN FKSGNSVPQT MGDIAGSVQK MAPDTRGLPT HQGPGHSSET
     PSSPGATASQ KCFVQIKGMT CASCVSNIER SLQRHAGILS VLVALMSGKA EVKYDPEIIQ
     SPRIAQLIQD LGFEASVMED NTVSEGDIEL IITGMTCASC VHNIESKLTR TNGITYASVA
     LATSKAHVKF DPEIVGPRDI IKIIEEIGFH ASLAQRNPNA HHLDHKTEIK QWKKSFLCSL
     VFGIPVMGLM VYMLIPSSTP QETMVLDHNI IPGLSVLNLI FFILCTFVQF LGGWYFYVQA
     YKSLRHRSAN MDVLIVLATT IAYAYSLVIL VVAVAEKAEK SPVTFFDTPP MLFVFIALGR
     WLEHVAKSKT SEALAKLMSL QATEATVVTL GEDNLILREE QVPMELVQRG DVIKVVPGGK
     FPVDGKVLEG NTMADESLIT GEAMPVTKKP GSIVIAGSIN AHGSVLLKAT HVGNDTTLAQ
     IVKLVEEAQM SKAPIQQLAD RFSGYFVPFI IIISTLTLVV WIVIGFVDFG VVQKYFPSPS
     KHISQTEVII RFAFQTSITV LCIACPCSLG LATPTAVMVG TGVAAQNGVL IKGGKPLEMA
     HKIKTVMFDK TGTITHGVPR VMRFLLLADV ATLPLRKVLA VVGTAEASSE HPLGVAVTKY
     CKEELGTETL GYSTDFQAVP GCGISCKVSN VEGILARSDL TAHPVGVGNP PTGEGAGPQT
     FSVLIGNREW MRRNGLTISS DISDAMTDHE MKGQTAILVA IDGVLCGMIA IADAVKPEAA
     LAIYTLKSMG VDVALITGDN RKTARAIATQ VGINKVFAEV LPSHKVAKVQ ELQNEGKKVA
     MVGDGVNDSP ALAQADVGIA IGTGTDVAIE AADVVLIRND LLDVVASIHL SKRTVRRIRV
     NLVLALIYNM VGIPIAAGVF MPIGIVLQPW MGSAAMAASS VSVVLSSLQL KCYRKPDLER
     YEAQAHGRMK PLSASQVSVH IGMDDRRRDS PRATAWDQVS YVSQVSLSSL TSDRLSRHGG
     AAEDGGDKWS LLLSDRDEEQ CI
//
ID   MRC2_MOUSE              Reviewed;        1479 AA.
AC   Q64449; Q6ZQ64; Q8C6P0;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=C-type mannose receptor 2;
DE   AltName: Full=Lectin lambda;
DE   AltName: Full=Macrophage mannose receptor 2;
DE   AltName: CD_antigen=CD280;
DE   Flags: Precursor;
GN   Name=Mrc2; Synonyms=Kiaa0709;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   MEDLINE=96355501; PubMed=8702911; DOI=10.1074/jbc.271.35.21323;
RA   Wu K., Yuan J., Lasky L.A.;
RT   "Characterization of a novel member of the macrophage mannose receptor
RT   type C lectin family.";
RL   J. Biol. Chem. 271:21323-21330(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Oviduct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 479-1479 (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=12835757; DOI=10.1038/sj.embor.embor882;
RA   East L., McCarthy A., Wienke D., Sturge J., Ashworth A., Isacke C.M.;
RT   "A targeted deletion in the endocytic receptor gene Endo180 results in
RT   a defect in collagen uptake.";
RL   EMBO Rep. 4:710-716(2003).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12668656; DOI=10.1083/jcb.200211091;
RA   Engelholm L.H., List K., Netzel-Arnett S., Cukierman E., Mitola D.J.,
RA   Aaronson H., Kjoller L., Larsen J.K., Yamada K.M., Strickland D.K.,
RA   Holmbeck K., Danoe K., Birkedal-Hansen H., Behrendt N., Bugge T.H.;
RT   "uPARAP/Endo180 is essential for cellular uptake of collagen and
RT   promotes fibroblast collagen adhesion.";
RL   J. Cell Biol. 160:1009-1015(2003).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=14729061; DOI=10.1016/j.yexcr.2003.10.008;
RA   Kjoller L., Engelholm L.H., Hoyer-Hansen M., Danoe K., Bugge T.H.,
RA   Behrendt N.;
RT   "uPARAP/endo180 directs lysosomal delivery and degradation of collagen
RT   IV.";
RL   Exp. Cell Res. 293:106-116(2004).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15967816; DOI=10.1083/jcb.200411153;
RA   Curino A.C., Engelholm L.H., Yamada S.S., Holmbeck K., Lund L.R.,
RA   Molinolo A.A., Behrendt N., Nielsen B.S., Bugge T.H.;
RT   "Intracellular collagen degradation mediated by uPARAP/Endo180 is a
RT   major pathway of extracellular matrix turnover during malignancy.";
RL   J. Cell Biol. 169:977-985(2005).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-139 AND ASN-363, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [9]
RP   STRUCTURE BY ELECTRON MICROSCOPY (18 ANGSTROMS).
RX   PubMed=12856000; DOI=10.1038/sj.embor.embor898;
RA   Rivera-Calzada A., Robertson D., MacFadyen J.R., Boskovic J.,
RA   Isacke C.M., Llorca O.;
RT   "Three-dimensional interplay among the ligand-binding domains of the
RT   urokinase-plasminogen-activator-receptor-associated protein,
RT   Endo180.";
RL   EMBO Rep. 4:807-812(2003).
CC   -!- FUNCTION: May play a role as endocytotic lectin receptor
CC       displaying calcium-dependent lectin activity. Internalizes
CC       glycosylated ligands from the extracellular space for release in
CC       an endosomal compartment via clathrin-mediated endocytosis. May be
CC       involved in plasminogen activation system controlling the
CC       extracellular level of PLAUR/PLAU, and thus may regulate protease
CC       activity at the cell surface. May contribute to cellular uptake,
CC       remodeling and degradation of extracellular collagen matrices. May
CC       participate in remodeling of extracellular matrix co-operating
CC       with the matrix metalloproteinases (MMPs).
CC   -!- SUBUNIT: Interacts directly with PLAUR/UPAR and PLAU/pro-UPA to
CC       form a tri-molecular complex. Interacts with collagen V and with
CC       C-terminal region of type I collagen/COL1A1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q64449-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q64449-2; Sequence=VSP_017223, VSP_017224;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart, lung and kidney,
CC       but little or no expression in brain, thymus or adult liver.
CC       Expressed at highly endothelialized sites such as those in choroid
CC       plexus and kidney glomerulai as well as in chondrocytes in
CC       cartilaginous regions of the embryo.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed at day 7 of embryonic
CC       development and detected throughout the later stages of embryonic
CC       development.
CC   -!- DOMAIN: C-type lectin domains 3 to 8 are not required for calcium-
CC       dependent binding of mannose, fucose and N-acetylglucosamine. C-
CC       type lectin domain 2 is responsible for sugar-binding in a
CC       calcium-dependent manner (By similarity).
CC   -!- DOMAIN: Fibronectin type-II domain mediates collagen-binding (By
CC       similarity).
CC   -!- DOMAIN: Ricin B-type lectin domain contacts with the second C-type
CC       lectin domain.
CC   -!- PTM: Phosphorylated (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice show impaired mammary tumor growth.
CC       Tumors from mice lacking Mrc2 display an abrogation of cellular
CC       collagen uptake, a fibrotic state characterized by the
CC       accumulation of both basement membrane and interstitial collagens,
CC       and an overall tumor size reduction, despite the collagen
CC       accumulation. Fibroblasts from mice lacking Mrc2 display a severe
CC       impairment of internalization of collagen IV and V and thus,
CC       exhibit a general deficiency in uptake and delivery of collagens
CC       to vesicular compartments. Fibroblasts also have diminished
CC       initial adhesion to collagen as well as impaired migration on
CC       fibrillar collagen. Mice with a targeted deletion of Mrc2 exon 2-6
CC       are phenotypically normal, healthy and fertile. This deletion
CC       resulted in expression of a protein that lacks the ricin B-type
CC       lectin domain, the fibronectin type-II domain and the first C-type
CC       lectin domain. Fibroblasts from these mice display C-type lectin
CC       activity, but have a defect in collagen-binding and
CC       internalization, and an impaired migratory phenotype.
CC   -!- SIMILARITY: Contains 8 C-type lectin domains.
CC   -!- SIMILARITY: Contains 1 fibronectin type-II domain.
CC   -!- SIMILARITY: Contains 1 ricin B-type lectin domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC52729.1; Type=Frameshift; Positions=120, 145;
CC       Sequence=BAC35672.1; Type=Erroneous initiation;
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=Endo180;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_252";
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DR   EMBL; U56734; AAC52729.1; ALT_FRAME; mRNA.
DR   EMBL; AK054150; BAC35672.1; ALT_INIT; mRNA.
DR   EMBL; AK129195; BAC98005.1; -; mRNA.
DR   IPI; IPI00649313; -.
DR   IPI; IPI00762091; -.
DR   PIR; T42710; T42710.
DR   UniGene; Mm.235616; -.
DR   ProteinModelPortal; Q64449; -.
DR   SMR; Q64449; 39-645, 667-808, 823-952, 970-1111, 1123-1245, 1258-1398.
DR   PRIDE; Q64449; -.
DR   Ensembl; ENSMUST00000100335; ENSMUSP00000097909; ENSMUSG00000020695.
DR   MGI; MGI:107818; Mrc2.
DR   GeneTree; ENSGT00540000069746; -.
DR   HOGENOM; HBG715588; -.
DR   HOVERGEN; HBG053606; -.
DR   InParanoid; Q64449; -.
DR   OrthoDB; EOG415GCH; -.
DR   ArrayExpress; Q64449; -.
DR   Bgee; Q64449; -.
DR   CleanEx; MM_MRC2; -.
DR   Genevestigator; Q64449; -.
DR   GermOnline; ENSMUSG00000020695; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005529; F:sugar binding; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   InterPro; IPR002353; AntifreezeII.
DR   InterPro; IPR001304; C-type_lectin.
DR   InterPro; IPR016186; C-type_lectin-like.
DR   InterPro; IPR018378; C-type_lectin_CS.
DR   InterPro; IPR016187; C-type_lectin_fold.
DR   InterPro; IPR000562; FN_type2_col-bd.
DR   InterPro; IPR013806; Kringle-like.
DR   InterPro; IPR008997; Ricin_B-rel_lectin.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   Gene3D; G3DSA:3.10.100.10; C-type_lectin-like; 8.
DR   Gene3D; G3DSA:2.10.10.10; FN2; 1.
DR   Pfam; PF00040; fn2; 1.
DR   Pfam; PF00059; Lectin_C; 8.
DR   PRINTS; PR00356; ANTIFREEZEII.
DR   SMART; SM00034; CLECT; 8.
DR   SMART; SM00059; FN2; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF56436; C-type_lectin_fold; 8.
DR   SUPFAM; SSF57440; Kringle-like; 1.
DR   SUPFAM; SSF50370; RicinB_like; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 3.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 8.
DR   PROSITE; PS00023; FN2_1; 1.
DR   PROSITE; PS51092; FN2_2; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Disulfide bond; Endocytosis;
KW   Glycoprotein; Isopeptide bond; Lectin; Membrane; Phosphoprotein;
KW   Receptor; Repeat; Signal; Transmembrane; Transmembrane helix;
KW   Ubl conjugation.
FT   SIGNAL        1     30       Potential.
FT   CHAIN        31   1479       C-type mannose receptor 2.
FT                                /FTId=PRO_0000046079.
FT   TOPO_DOM     31   1413       Extracellular (Potential).
FT   TRANSMEM   1414   1434       Helical; (Potential).
FT   TOPO_DOM   1435   1479       Cytoplasmic (Potential).
FT   DOMAIN       37    190       Ricin B-type lectin.
FT   DOMAIN      181    229       Fibronectin type-II.
FT   DOMAIN      243    359       C-type lectin 1.
FT   DOMAIN      388    504       C-type lectin 2.
FT   DOMAIN      527    643       C-type lectin 3.
FT   DOMAIN      677    808       C-type lectin 4.
FT   DOMAIN      831    950       C-type lectin 5.
FT   DOMAIN      978   1106       C-type lectin 6.
FT   DOMAIN     1131   1242       C-type lectin 7.
FT   DOMAIN     1271   1391       C-type lectin 8.
FT   CARBOHYD    101    101       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    139    139       N-linked (GlcNAc...).
FT   CARBOHYD    363    363       N-linked (GlcNAc...).
FT   CARBOHYD   1028   1028       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1348   1348       N-linked (GlcNAc...) (Potential).
FT   DISULFID     92    111       By similarity.
FT   DISULFID    186    212       By similarity.
FT   DISULFID    200    227       By similarity.
FT   DISULFID    265    358       By similarity.
FT   DISULFID    334    350       By similarity.
FT   DISULFID    409    503       By similarity.
FT   DISULFID    480    495       By similarity.
FT   DISULFID    617    634       By similarity.
FT   DISULFID    703    807       By similarity.
FT   DISULFID    784    799       By similarity.
FT   DISULFID    852    949       By similarity.
FT   DISULFID    926    941       By similarity.
FT   DISULFID   1077   1097       By similarity.
FT   DISULFID   1219   1233       By similarity.
FT   DISULFID   1367   1382       By similarity.
FT   CROSSLNK   1141   1141       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO-1) (By
FT                                similarity).
FT   VAR_SEQ     173    180       EVYTIQGN -> GEGSIAKS (in isoform 2).
FT                                /FTId=VSP_017223.
FT   VAR_SEQ     181   1479       Missing (in isoform 2).
FT                                /FTId=VSP_017224.
FT   CONFLICT     66     66       F -> V (in Ref. 2; BAC35672).
FT   CONFLICT    519    519       G -> D (in Ref. 1; AAC52729).
FT   CONFLICT    869    869       D -> G (in Ref. 1; AAC52729).
FT   CONFLICT    984    984       Q -> R (in Ref. 1; AAC52729).
SQ   SEQUENCE   1479 AA;  167094 MW;  662459738ABD3709 CRC64;
     MVPIRPALAP WPRHLLRCVL LLGGLRLGHP ADSAAALLEP DVFLIFSQGM QGCLEAQGVQ
     VRVTPFCNAS LPAQRWKWVS RNRLFNLGAT QCLGTGWPVT NTTVSLGMYE CDREALSLRW
     QCRTLGDQLS LLLGARASNA SKPGTLERGD QTRSGHWNIY GSEEDLCARP YYEVYTIQGN
     SHGKPCTIPF KYDNQWFHGC TSTGREDGHL WCATTQDYGK DERWGFCPIK SNDCETFWDK
     DQLTDSCYQF NFQSTLSWRE AWASCEQQGA DLLSITEIHE QTYINGLLTG YSSTLWIGLN
     DLDTSGGWQW SDNSPLKYLN WESDQPDNPG EENCGVIRTE SSGGWQNHDC SIALPYVCKK
     KPNATVEPIQ PDRWTNVKVE CDPSWQPFQG HCYRLQAEKR SWQESKRACL RGGGDLLSIH
     SMAELEFITK QIKQEVEELW IGLNDLKLQM NFEWSDGSLV SFTHWHPFEP NNFRDSLEDC
     VTIWGPEGRW NDSPCNQSLP SICKKAGRLS QGAAEEDHGC RKGWTWHSPS CYWLGEDQVI
     YSDARRLCTD HGSQLVTITN RFEQAFVSSL IYNWEGEYFW TALQDLNSTG SFRWLSGDEV
     IYTHWNRDQP GYRRGGCVAL ATGSAMGLWE VKNCTSFRAR YICRQSLGTP VTPELPGPDP
     TPSLTGSCPQ GWVSDPKLRH CYKVFSSERL QEKKSWIQAL GVCRELGAQL LSLASYEEEH
     FVAHMLNKIF GESEPESHEQ HWFWIGLNRR DPREGHSWRW SDGLGFSYHN FARSRHDDDD
     IRGCAVLDLA SLQWVPMQCQ TQLDWICKIP RGVDVREPDI GRQGRLEWVR FQEAEYKFFE
     HHSSWAQAQR ICTWFQADLT SVHSQAELDF LGQNLQKLSS DQEQHWWIGL HTLESDGRFR
     WTDGSIINFI SWAPGKPRPI GKDKKCVYMT ARQEDWGDQR CHTALPYICK RSNSSGETQP
     QDLPPSALGG CPSGWNQFLN KCFQIQGQDP QDRVKWSEAQ FSCEQQEAQL VTIANPLEQA
     FITASLPNVT FDLWIGLHAS QRDFQWIEQE PLLYTNWAPG EPSGPSPAPS GTKPTSCAVI
     LHSPSAHFTG RWDDRSCTEE THGFICQKGT DPSLSPSPAA TPPAPGAELS YLNHTFRLLQ
     KPLRWKDALL LCESRNASLA HVPDPYTQAF LTQAARGLQT PLWIGLASEE GSRRYSWLSE
     EPLNYVSWQD EEPQHSGGCA YVDVDGTWRT TSCDTKLQGA VCGVSRGPPP RRINYRGSCP
     QGLADSSWIP FREHCYSFHM EVLLGHKEAL QRCQKAGGTV LSILDEMENV FVWEHLQTAE
     AQSRGAWLGM NFNPKGGTLV WQDNTAVNYS NWGPPGLGPS MLSHNSCYWI QSSSGLWRPG
     ACTNITMGVV CKLPRVEENS FLPSAALPES PVALVVVLTA VLLLLALMTA ALILYRRRQS
     AERGSFEGAR YSRSSHSGPA EATEKNILVS DMEMNEQQE
//
ID   PTPRJ_MOUSE             Reviewed;        1238 AA.
AC   Q64455; Q3UH64; Q3UHL5; Q541R5; Q8CIW9; Q8K3Q2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 2.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Receptor-type tyrosine-protein phosphatase eta;
DE            Short=Protein-tyrosine phosphatase eta;
DE            Short=R-PTP-eta;
DE            EC=3.1.3.48;
DE   AltName: Full=HPTP beta-like tyrosine phosphatase;
DE   AltName: Full=Protein-tyrosine phosphatase receptor type J;
DE            Short=R-PTP-J;
DE   AltName: Full=Susceptibility to colon cancer 1;
DE   AltName: CD_antigen=CD148;
DE   Flags: Precursor;
GN   Name=Ptprj; Synonyms=Byp, Scc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=MRL-LPR/LPR; TISSUE=Lymph node;
RX   MEDLINE=96140699; PubMed=8549806; DOI=10.1016/0014-5793(95)01415-2;
RA   Kuramochi S., Matsuda S., Matsuda Y., Saitoh T., Ohsugi M.,
RA   Yamamoto T.;
RT   "Molecular cloning and characterization of Byp, a murine receptor-type
RT   tyrosine phosphatase similar to human DEP-1.";
RL   FEBS Lett. 378:7-14(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=129/SvSl, and BALB/c;
RX   MEDLINE=22084388; PubMed=12089527; DOI=10.1038/ng903;
RA   Ruivenkamp C.A.L., van Wezel T., Zanon C., Stassen A.P.M., Vlcek C.,
RA   Csikos T., Klous A.M., Tripodis N., Perrakis A., Boerrigter L.,
RA   Groot P.C., Lindeman J., Mooi W.J., Meijjer G.A., Scholten G.,
RA   Dauwerse H., Paces V., van Zandwijk N., van Ommen G.J.B., Demant P.;
RT   "Ptprj is a candidate for the mouse colon-cancer susceptibility locus
RT   Scc1 and is frequently deleted in human cancers.";
RL   Nat. Genet. 31:295-300(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129P2;
RA   Csikos T., Snoek M., de Boer T., Drenth T., Krimpenfort P.,
RA   van Amerongen R., Zevenhoven J., van der Valk M., Hellberg C.,
RA   Ostman A., Demant P., Berns A.;
RT   "Phenotypic consequences of the germ-line loss of the putative tumor
RT   suppressor Ptprj (Scc1).";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=93247293; PubMed=8483328;
RA   Honda H., Shibuya M., Chiba S., Yazaki Y., Hirai H.;
RT   "Identification of novel protein-tyrosine phosphatases in a human
RT   leukemia cell line, F-36P.";
RL   Leukemia 7:742-746(1993).
RN   [6]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=9823776;
RA   Osborne J.M., den Elzen N., Lichanska A.M., Costelloe E.O., Yamada T.,
RA   Cassady A.I., Hume D.A.;
RT   "Murine DEP-1, a receptor protein tyrosine phosphatase, is expressed
RT   in macrophages and is regulated by CSF-1 and LPS.";
RL   J. Leukoc. Biol. 64:692-701(1998).
RN   [7]
RP   FUNCTION, AND MUTAGENESIS OF ASP-1106 AND CYS-1140.
RX   PubMed=12771128; DOI=10.1083/jcb.200209019;
RA   Grazia Lampugnani M., Zanetti A., Corada M., Takahashi T., Balconi G.,
RA   Breviario F., Orsenigo F., Cattelino A., Kemler R., Daniel T.O.,
RA   Dejana E.;
RT   "Contact inhibition of VEGF-induced proliferation requires vascular
RT   endothelial cadherin, beta-catenin, and the phosphatase DEP-1/CD148.";
RL   J. Cell Biol. 161:793-804(2003).
RN   [8]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12913111; DOI=10.1083/jcb.200303040;
RA   Lin J., Weiss A.;
RT   "The tyrosine phosphatase CD148 is excluded from the immunologic
RT   synapse and down-regulates prolonged T cell signaling.";
RL   J. Cell Biol. 162:673-682(2003).
RN   [9]
RP   FUNCTION.
RX   PubMed=12588999;
RA   Takahashi T., Takahashi K., St John P.L., Fleming P.A., Tomemori T.,
RA   Watanabe T., Abrahamson D.R., Drake C.J., Shirasawa T., Daniel T.O.;
RT   "A mutant receptor tyrosine phosphatase, CD148, causes defects in
RT   vascular development.";
RL   Mol. Cell. Biol. 23:1817-1831(2003).
RN   [10]
RP   FUNCTION, AND MUTAGENESIS OF CYS-1140.
RX   PubMed=12833140; DOI=10.1038/sj.onc.1206652;
RA   Jandt E., Denner K., Kovalenko M., Ostman A., Bohmer F.D.;
RT   "The protein-tyrosine phosphatase DEP-1 modulates growth factor-
RT   stimulated cell migration and cell-matrix adhesion.";
RL   Oncogene 22:4175-4185(2003).
RN   [11]
RP   FUNCTION.
RX   PubMed=18249142; DOI=10.1016/j.immuni.2007.11.024;
RA   Zhu J.W., Brdicka T., Katsumoto T.R., Lin J., Weiss A.;
RT   "Structurally distinct phosphatases CD45 and CD148 both regulate B
RT   cell and macrophage immunoreceptor signaling.";
RL   Immunity 28:183-196(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-912, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [13]
RP   FUNCTION.
RX   PubMed=19246339; DOI=10.1182/blood-2008-08-174318;
RA   Senis Y.A., Tomlinson M.G., Ellison S., Mazharian A., Lim J., Zhao Y.,
RA   Kornerup K.N., Auger J.M., Thomas S.G., Dhanjal T., Kalia N.,
RA   Zhu J.W., Weiss A., Watson S.P.;
RT   "The tyrosine phosphatase CD148 is an essential positive regulator of
RT   platelet activation and thrombosis.";
RL   Blood 113:4942-4954(2009).
RN   [14]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=19268662; DOI=10.1016/j.yexcr.2009.02.023;
RA   Dave R.K., Hume D.A., Elsegood C., Kellie S.;
RT   "CD148/DEP-1 association with areas of cytoskeletal organisation in
RT   macrophages.";
RL   Exp. Cell Res. 315:1734-1744(2009).
RN   [15]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145; ASN-313; ASN-317 AND
RP   ASN-538, AND MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Tyrosine phosphatase which dephosphorylates or
CC       contributes to the dephosphorylation of CTNND1, PDGFRB, MET, RET,
CC       KDR, LYN, SRC, MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and PIK3R2.
CC       Plays a role in cell adhesion, migration, proliferation and
CC       differentiation. Involved in vascular development. May be involved
CC       in the mechanism of contact inhibition of cell growth. Regulator
CC       of macrophage adhesion and spreading. Positively affects cell-
CC       matrix adhesion. Positive regulator of platelet activation and
CC       thrombosis. Negative regulator of cell proliferation. Negative
CC       regulator of PDGF-stimulated cell migration; through
CC       dephosphorylation of PDGFR. Positive regulator of endothelial cell
CC       survival, as well as of VEGF-induced SRC and AKT activation;
CC       through KDR dephosphorylation. Negative regulator of EGFR
CC       signaling pathway; through EGFR dephosphorylation. Enhances the
CC       barrier function of epithelial junctions during reassembly.
CC       Negatively regulates T-cell receptor (TCR) signaling. Upon T-cell
CC       TCR activation, it is up-regulated and excluded from the
CC       immunological synapses, while upon T-cell-antigen presenting cells
CC       (APC) disengagement, it is no longer excluded and can
CC       dephosphorylate PLCG1 and LAT to down-regulate prolongation of
CC       signaling.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- SUBUNIT: Monomer. Interacts with CTNNB1 (phosphorylated) and JUP
CC       (phosphorylated). Interacts with GAB1 and GRB2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Cell projection, ruffle membrane. Cell junction.
CC       Note=After T cell stimulation, it is temporarily excluded from
CC       immunological synapses. Found at cell borders.
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in brain, kidney,
CC       spleen and intestine, and at lower levels in liver, lung, thymus
CC       and heart. Expressed at a high level in the myeloid cell line FDC-
CC       P2, and at a lower level in the pre-B lymphoid cell line WEHI-231
CC       and the T hybridoma cell line HB21.7.31. Not expressed in the
CC       fibroblast cell line NIH3T3 or the erythroid cell line F5-5.
CC       Expressed in macrophages.
CC   -!- DEVELOPMENTAL STAGE: Expressed at 11.5 dpc in presumptive
CC       macrophages concentrated in the liver and scattered throughout the
CC       embryonic mesenchyme. Expressed at 11.5 and 12.5 dpc in the
CC       developing eye and in the ganglia and processes of cranial and
CC       spinal nerves constituting the PNS.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 3 subfamily.
CC   -!- SIMILARITY: Contains 8 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
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DR   EMBL; D45212; BAA08146.1; -; mRNA.
DR   EMBL; AY038877; AAN11409.1; -; Genomic_DNA.
DR   EMBL; AY038861; AAN11409.1; JOINED; Genomic_DNA.
DR   EMBL; AY038891; AAK96030.1; -; mRNA.
DR   EMBL; AY039232; AAK98640.1; -; mRNA.
DR   EMBL; DQ133576; ABA07808.1; -; mRNA.
DR   EMBL; AK147318; BAE27842.1; -; mRNA.
DR   EMBL; AK147556; BAE27993.1; -; mRNA.
DR   IPI; IPI00469426; -.
DR   PIR; S68700; S68700.
DR   RefSeq; NP_033008.3; NM_008982.5.
DR   UniGene; Mm.330393; -.
DR   ProteinModelPortal; Q64455; -.
DR   SMR; Q64455; 38-154, 228-607, 919-1204.
DR   STRING; Q64455; -.
DR   PhosphoSite; Q64455; -.
DR   PRIDE; Q64455; -.
DR   Ensembl; ENSMUST00000026352; ENSMUSP00000026352; ENSMUSG00000025314.
DR   Ensembl; ENSMUST00000111493; ENSMUSP00000107119; ENSMUSG00000025314.
DR   Ensembl; ENSMUST00000111495; ENSMUSP00000107121; ENSMUSG00000025314.
DR   GeneID; 19271; -.
DR   KEGG; mmu:19271; -.
DR   CTD; 19271; -.
DR   MGI; MGI:104574; Ptprj.
DR   GeneTree; ENSGT00600000084280; -.
DR   HOGENOM; HBG282919; -.
DR   HOVERGEN; HBG053761; -.
DR   InParanoid; Q64455; -.
DR   OrthoDB; EOG43BMN7; -.
DR   BRENDA; 3.1.3.48; 244.
DR   ArrayExpress; Q64455; -.
DR   Bgee; Q64455; -.
DR   CleanEx; MM_PTPRJ; -.
DR   Genevestigator; Q64455; -.
DR   GermOnline; ENSMUSG00000025314; Mus musculus.
DR   GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 8.
DR   Pfam; PF00041; fn3; 4.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 8.
DR   SMART; SM00194; PTPc; 1.
DR   SUPFAM; SSF49265; FN_III-like; 6.
DR   PROSITE; PS50853; FN3; 7.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Cell projection; Glycoprotein;
KW   Hydrolase; Membrane; Phosphoprotein; Protein phosphatase; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     28       Potential.
FT   CHAIN        29   1238       Receptor-type tyrosine-protein
FT                                phosphatase eta.
FT                                /FTId=PRO_0000025445.
FT   TOPO_DOM     29    876       Extracellular (Potential).
FT   TRANSMEM    877    897       Helical; (Potential).
FT   TOPO_DOM    898   1238       Cytoplasmic (Potential).
FT   DOMAIN       40    130       Fibronectin type-III 1.
FT   DOMAIN      170    266       Fibronectin type-III 2.
FT   DOMAIN      267    354       Fibronectin type-III 3.
FT   DOMAIN      356    440       Fibronectin type-III 4.
FT   DOMAIN      442    527       Fibronectin type-III 5.
FT   DOMAIN      529    618       Fibronectin type-III 6.
FT   DOMAIN      620    712       Fibronectin type-III 7.
FT   DOMAIN      717    803       Fibronectin type-III 8.
FT   DOMAIN      942   1199       Tyrosine-protein phosphatase.
FT   REGION     1140   1146       Substrate binding (By similarity).
FT   ACT_SITE   1140   1140       Phosphocysteine intermediate (By
FT                                similarity).
FT   BINDING    1106   1106       Substrate (By similarity).
FT   BINDING    1184   1184       Substrate (By similarity).
FT   MOD_RES     912    912       Phosphoserine.
FT   CARBOHYD     62     62       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     78     78       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     85     85       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     90     90       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    110    110       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    114    114       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    145    145       N-linked (GlcNAc...).
FT   CARBOHYD    164    164       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    173    173       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    182    182       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    198    198       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    207    207       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    244    244       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    253    253       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    267    267       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    278    278       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    313    313       N-linked (GlcNAc...).
FT   CARBOHYD    317    317       N-linked (GlcNAc...).
FT   CARBOHYD    333    333       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    366    366       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    379    379       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    398    398       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    403    403       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    437    437       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    452    452       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    488    488       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    506    506       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    538    538       N-linked (GlcNAc...).
FT   CARBOHYD    572    572       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    576    576       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    662    662       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    668    668       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    685    685       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    691    691       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    725    725       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    811    811       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    838    838       N-linked (GlcNAc...) (Potential).
FT   MUTAGEN    1106   1106       D->A: Substrate trapping with much higher
FT                                affinity for substrate.
FT   MUTAGEN    1140   1140       C->S: Catalytically inactive and
FT                                substrate trapping with higher affinity
FT                                for substrate.
FT   CONFLICT    175    175       S -> T (in Ref. 1; BAA08146 and 2;
FT                                AAK96030/AAK98640).
FT   CONFLICT    211    211       L -> P (in Ref. 2; AAK98640).
FT   CONFLICT    217    217       V -> A (in Ref. 2; AAK98640).
FT   CONFLICT    463    463       Q -> H (in Ref. 4; BAE27842).
FT   CONFLICT    553    553       A -> T (in Ref. 2; AAK98640).
FT   CONFLICT    622    622       P -> S (in Ref. 2; AAK98640).
FT   CONFLICT   1061   1061       D -> E (in Ref. 2; AAK98640).
FT   CONFLICT   1126   1126       Y -> D (in Ref. 2; AAN11409).
FT   CONFLICT   1133   1133       E -> K (in Ref. 2; AAN11409).
SQ   SEQUENCE   1238 AA;  136769 MW;  E525D346A2C60335 CRC64;
     MKPAARETRT PPRSPGLRWA LLPLLLLLRQ GQVLCAGAAP NPIFDIEAVV SPTSVLLTWK
     HNDSGASECR IENKMESNLT FPVKNQTSCN ITGLSPGTSY TFSIISVTTN ETLNKTITTE
     PWPVSDLHVT SVGVTQARLT WSNANGTASY RMLIEELTTH SSVNISGLKP GTNNSFAFPE
     SNETQADFAV AEEVPDANGT KRIPVTNLSQ LHKNSLVSVD PPSGQDPSLT EILLTDLKPD
     TQYNATIYSQ AANGTEGQPR NKVFKTNSTQ VSDVRAMNIS ASSMTLTWKS NYDGSRTSIV
     YKIHVAGGTH SVNQTVNKTE AIILGLSSST LYNITVHPFL GQTEGTPGFL QVYTSPDQVS
     DFRVTNVSTR AIGLAWRSND SKSFEIFIKQ DGGEKHRNAS TGNQSYMVED LKPGTSYHFE
     IIPRGPDGTE GLSSTVNGST DPSAVTDIRV VNISTTEMQL EWQNTDDASG YTYHLVLESK
     SGSIIRTNSS QKWITVGSLT PGTLYNVTIF PEVDQIQGIS NSITQYTRPS SVSHIEVNTT
     TTTAAIRWKN EDAASASYAY SVLILKTGDG SNVTSNFTKD PSILIPELIP GVSYTVKILT
     QVGDGTTSLV PGWNLFCTEP EPVTSFHCEV VPKEPALVLK WACPFGMYTG FELGVRSDSW
     DNMTRLENCT SDDDTECRTE VAYLNFSTSY NISIATLSCG KMALPAQNIC TTGITDPPTP
     DGSPNITSVS HNSVKVKFSG FEASHGPIKA YAVILTTGEA AQPSADVLKY TYEDFKRGAS
     DTYVTYLIRI EEKGQSQGLS EVLNYEIDVG NQSTTLGYYN GRLEPLGSYR ACVAGFTNIT
     YNLQNDGLIN GDESYVSFSP YSEAVFLPQD PGVICGAVFG CIFGALAITA VGGFIFWRKK
     RTDAKNNEVS FSQIKPKKSK LIRVENFEAY FKKQQADSNC GFAEEYEDLK LIGISLPKYT
     AEIAENRGKN RYNNVLPYDI SRVKLSVQTH STDDYINANY MPGYHSKKDF IATQGPLPNT
     LKDFWRMVWE KNVYAIVMLT KCVEQGRTKC EEYWPSKQAQ DYGDITVAMT SEVVLPEWTI
     RDFVVKNMQN SESHPLRQFH FTSWPDHGVP DTTDLLINFR YLVRDYMKQI PPESPILVHC
     SAGVGRTGTF IAIDRLIYQI ENENTVDVYG IVYDLRMHRP LMVQTEDQYV FLNQCVLDII
     RAQKDSKVDL IYQNTTAMTI YENLEPVSMF GKTNGYIA
//
ID   TOP2B_MOUSE             Reviewed;        1612 AA.
AC   Q64511; Q7TQG4;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   08-MAR-2011, entry version 101.
DE   RecName: Full=DNA topoisomerase 2-beta;
DE            EC=5.99.1.3;
DE   AltName: Full=DNA topoisomerase II, beta isozyme;
GN   Name=Top2b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RA   Miyaike M., Adachi N., Kikuchi A.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419; THR-627; SER-1387;
RP   SER-1400; SER-1453 AND THR-1458, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1387; SER-1453;
RP   SER-1509; SER-1511; SER-1513; SER-1537 AND SER-1539, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1324; SER-1328;
RP   SER-1330; SER-1332; SER-1387; SER-1509; SER-1511; SER-1537 AND
RP   SER-1539, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1509, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1453; SER-1509 AND
RP   SER-1511, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Control of topological states of DNA by transient
CC       breakage and subsequent rejoining of DNA strands. Topoisomerase II
CC       makes double-strand breaks. Indirectly ivolved in vitamin D-
CC       coupled transcription regulation via its association with the
CC       WINAC complex, a chromatin-remodeling complex recruited by vitamin
CC       D receptor (VDR), which is required for the ligand-bound VDR-
CC       mediated transrepression of the CYP27B1 gene (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
CC       of double-stranded DNA.
CC   -!- SUBUNIT: Homodimer. Component of the WINAC complex, at least
CC       composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1,
CC       SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- MISCELLANEOUS: Eukaryotic topoisomerase I and II can relax both
CC       negative and positive supercoils, whereas prokaryotic enzymes
CC       relax only negative supercoils.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family.
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DR   EMBL; D38046; BAA07236.1; -; mRNA.
DR   EMBL; BC041106; AAH41106.1; -; mRNA.
DR   EMBL; BC054541; AAH54541.1; -; mRNA.
DR   IPI; IPI00135443; -.
DR   RefSeq; NP_033435.2; NM_009409.2.
DR   UniGene; Mm.130362; -.
DR   ProteinModelPortal; Q64511; -.
DR   SMR; Q64511; 38-414, 440-1193.
DR   STRING; Q64511; -.
DR   PhosphoSite; Q64511; -.
DR   PRIDE; Q64511; -.
DR   Ensembl; ENSMUST00000017629; ENSMUSP00000017629; ENSMUSG00000017485.
DR   GeneID; 21974; -.
DR   KEGG; mmu:21974; -.
DR   NMPDR; fig|10090.3.peg.28582; -.
DR   UCSC; uc007shc.1; mouse.
DR   CTD; 21974; -.
DR   MGI; MGI:98791; Top2b.
DR   HOGENOM; HBG521093; -.
DR   HOVERGEN; HBG052998; -.
DR   InParanoid; Q64511; -.
DR   OMA; IPKKTTT; -.
DR   OrthoDB; EOG4640B2; -.
DR   PhylomeDB; Q64511; -.
DR   BRENDA; 5.99.1.3; 244.
DR   NextBio; 301674; -.
DR   ArrayExpress; Q64511; -.
DR   Bgee; Q64511; -.
DR   CleanEx; MM_TOP2B; -.
DR   Genevestigator; Q64511; -.
DR   GermOnline; ENSMUSG00000017485; Mus musculus.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase (ATP-hydrolyzing) activity; IEA:EC.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR020899; Arg_repress_C.
DR   InterPro; IPR003594; ATPase-like_ATP-bd.
DR   InterPro; IPR012542; DTHCT.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR002205; Topo_IIA_A/C.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a.
DR   InterPro; IPR001241; Topo_IIA_B/N.
DR   InterPro; IPR013759; Topo_IIA_B/N_ab.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR   InterPro; IPR013760; Topo_IIA_cen.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   Gene3D; G3DSA:3.30.1360.40; Arg_repress; 1.
DR   Gene3D; G3DSA:3.30.565.10; ATP_bd_ATPase; 1.
DR   Gene3D; G3DSA:3.30.230.10; Ribosomal_S5_D2-type_fold; 1.
DR   Gene3D; G3DSA:3.90.199.10; Topo_IIA_A/C_ab; 1.
DR   Gene3D; G3DSA:1.10.268.10; Topo_IIA_A_a; 1.
DR   Gene3D; G3DSA:3.40.50.670; Topo_IIA_B/N_ab; 1.
DR   Pfam; PF00204; DNA_gyraseB; 1.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   Pfam; PF08070; DTHCT; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   PRINTS; PR00418; TPI2FAMILY.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00433; TOP2c; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF55874; ATP_bd_ATPase; 1.
DR   SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR   SUPFAM; SSF56719; Topo_IIA_cen; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; DNA-binding; Isomerase; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Topoisomerase.
FT   CHAIN         1   1612       DNA topoisomerase 2-beta.
FT                                /FTId=PRO_0000145370.
FT   NP_BIND     170    175       ATP (Potential).
FT   ACT_SITE    814    814       O-(5'-phospho-DNA)-tyrosine intermediate
FT                                (By similarity).
FT   MOD_RES     353    353       N6-acetyllysine (By similarity).
FT   MOD_RES     355    355       N6-acetyllysine (By similarity).
FT   MOD_RES     361    361       N6-acetyllysine (By similarity).
FT   MOD_RES     419    419       Phosphoserine.
FT   MOD_RES     627    627       Phosphothreonine.
FT   MOD_RES     628    628       Phosphoserine (By similarity).
FT   MOD_RES     980    980       N6-acetyllysine (By similarity).
FT   MOD_RES    1224   1224       Phosphoserine (By similarity).
FT   MOD_RES    1280   1280       Phosphothreonine (By similarity).
FT   MOD_RES    1324   1324       Phosphoserine.
FT   MOD_RES    1328   1328       Phosphoserine.
FT   MOD_RES    1330   1330       Phosphoserine.
FT   MOD_RES    1332   1332       Phosphoserine.
FT   MOD_RES    1363   1363       Phosphoserine (By similarity).
FT   MOD_RES    1387   1387       Phosphoserine.
FT   MOD_RES    1390   1390       Phosphothreonine (By similarity).
FT   MOD_RES    1400   1400       Phosphoserine.
FT   MOD_RES    1408   1408       Phosphotyrosine (By similarity).
FT   MOD_RES    1411   1411       Phosphoserine (By similarity).
FT   MOD_RES    1441   1441       Phosphoserine (By similarity).
FT   MOD_RES    1448   1448       Phosphoserine (By similarity).
FT   MOD_RES    1453   1453       Phosphoserine.
FT   MOD_RES    1458   1458       Phosphothreonine.
FT   MOD_RES    1460   1460       Phosphoserine (By similarity).
FT   MOD_RES    1509   1509       Phosphoserine.
FT   MOD_RES    1511   1511       Phosphoserine.
FT   MOD_RES    1513   1513       Phosphoserine.
FT   MOD_RES    1537   1537       Phosphoserine.
FT   MOD_RES    1539   1539       Phosphoserine.
FT   MOD_RES    1562   1562       Phosphothreonine (By similarity).
FT   MOD_RES    1563   1563       Phosphoserine (By similarity).
FT   MOD_RES    1568   1568       Phosphoserine (By similarity).
FT   MOD_RES    1596   1596       Phosphotyrosine (By similarity).
FT   MOD_RES    1600   1600       Phosphoserine (By similarity).
FT   CONFLICT     16     16       V -> A (in Ref. 1; BAA07236).
FT   CONFLICT   1434   1434       L -> P (in Ref. 1; BAA07236).
SQ   SEQUENCE   1612 AA;  181909 MW;  974D9D5DAD0DB96A CRC64;
     MAKSSLAGSD GALTWVNNAT KKEELETANK NDSTKKLSVE RVYQKKTQLE HILLRPDTYI
     GSVEPLTQLM WVYDEDVGMN CREVTFVPGL YKIFDEILVN AADNKQRDKN MTCIKVSIDP
     ESNIISIWNN GKGIPVVEHK VEKVYVPALI FGQLLTSSNY DDDEKKVTGG RNGYGAKLCN
     IFSTKFTVET ACKEYKHSFK QTWMNNMMKT SEAKIKHFDG EDYTCITFQP DLSKFKMEKL
     DKDIVALMTR RAYDLAGSCK GVKVMFNGKK LPVNGFRSYV DLYVKDKLDE TGVALKVIHE
     LANERWDVCL TLSEKGFQQI SFVNSIATTK GGRHVDYVVD QVVSKLIEVV KKKNKAGVSV
     KPFQVKNHIW VFINCLIENP TFDSQTKENM TLQPKSFGSK CQLSEKFFKA ASNCGIVESI
     LNWVKFKAQT QLNKKCSSVK YSKIKGIPKL DDANDAGGKH SLECTLILTE GDSAKSLAVS
     GLGVIGRDRY GVFPLRGKIL NVREASHKQI MENAEINNII KIVGLQYKKS YDDAESLKTL
     RYGKIMIMTD QDQDGSHIKG LLINFIHHNW PSLLKHGFLE EFITPIVKAS KNKQELSFYS
     IPEFDEWKKH IENQKAWKIK YYKGLGTSTA KEAKEYFADM ERHRILFRYA GPEDDAAITL
     AFSKKKIDDR KEWLTNFMED RRQRRLHGLP EQFLYGTATK HLTYNDFINK ELILFSNSDN
     ERSIPSLVDG FKPGQRKVLF TCFKRNDKRE VKVAQLAGSV AEMSAYHHGE QALMMTIVNL
     AQNFVGSNNI NLLQPIGQFG TRLHGGKDAA SPRYIFTMLS SLARLLFPAV DDNLLKFLYD
     DNQRVEPEWY IPIIPMVLIN GAEGIGTGWA CKLPNYDARE IVNNVRRMLE GLDPHPMLPN
     YKNFKGTIQE LGQNQYAVSG EIFVVDRNTV EITELPVRTW TQVYKEQVLE PMLNGTDKTP
     ALISDYKEYH TDTTVKFVVK MTEEKLAQAE AAGLHKVFKL QTTLTCNSMV LFDHMGCLKK
     YETVQDILKE FFDLRLSYYG LRKEWLVGML GAESTKLNNQ ARFILEKIQG KITIENRSKK
     DLIQMLVQRG YESDPVKAWK EAQEKAAEEE DSQNQHDDSS SDSGTPSGPD FNYILNMSLW
     SLTKEKVEEL IKQRDTKGRE VNDLKRKSPS DLWKEDLAAF VEELDKVEAQ EREDILAGMS
     GKAIKGKVGK PKVKKLQLEE TMPSPYGRRI VPEITAMKAD ASRKLLKKKK GDPDTTVVKV
     EFDEEFSGTP AEGTGEETLT PSAPVNKGPK PKREKKEPGT RVRKTPTSTG KTNAKKVKKR
     NPWSDDESKS ESDLEEAEPV VIPRDSLLRR AAAERPKYTF DFSEEEDDDA AAADDSNDLE
     ELKVKASPIT NDGEDEFVPS DGLDKDEYAF SSGKSKATPE KSSNDKKSQD FGNLFSFPSY
     SQKSEDDSAK FDSNEEDTAS VFAPSFGLKQ TDKLPSKTVA AKKGKPPSDT APKAKRAPKQ
     KKIVETINSD SDSEFGIPKK TTTPKGKGRG AKKRKASGSE NEGDYNPGRK PSKTASKKPK
     KTSFDQDSDV DIFPSDFTSE PPALPRTGRA RKEVKYFAES DEEEDVDFAM FN
//
ID   GLPK_MOUSE              Reviewed;         559 AA.
AC   Q64516; B1ASZ1; Q8C2M1; Q8C8X0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Glycerol kinase;
DE            Short=GK;
DE            Short=Glycerokinase;
DE            EC=2.7.1.30;
DE   AltName: Full=ATP:glycerol 3-phosphotransferase;
GN   Name=Gk; Synonyms=Gyk;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c;
RX   MEDLINE=97038697; PubMed=8884278; DOI=10.1006/geno.1996.0500;
RA   Huq A.H., Lovell R.S., Sampson M.J., Decker W.K., Dinulos M.B.,
RA   Disteche C.M., Craigen W.J.;
RT   "Isolation, mapping, and functional expression of the mouse X
RT   chromosome glycerol kinase gene.";
RL   Genomics 36:530-534(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Retina, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Key enzyme in the regulation of glycerol uptake and
CC       metabolism (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + glycerol = ADP + sn-glycerol 3-
CC       phosphate.
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol
CC       kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Peripheral
CC       membrane protein; Cytoplasmic side (By similarity). Cytoplasm (By
CC       similarity). Note=Bound to the mitochondrial surface or
CC       cytoplasmic (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=3;
CC         IsoId=Q64516-3; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q64516-2; Sequence=VSP_034650;
CC       Name=1;
CC         IsoId=Q64516-1; Sequence=VSP_034650, VSP_034651;
CC   -!- SIMILARITY: Belongs to the FGGY kinase family.
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DR   EMBL; U48403; AAC52824.1; -; mRNA.
DR   EMBL; AK044308; BAC31861.1; -; mRNA.
DR   EMBL; AK088373; BAC40312.1; -; mRNA.
DR   EMBL; AL645567; CAM16667.1; -; Genomic_DNA.
DR   EMBL; AL672056; CAM16667.1; JOINED; Genomic_DNA.
DR   EMBL; AL645567; CAM16668.1; -; Genomic_DNA.
DR   EMBL; AL672056; CAM16668.1; JOINED; Genomic_DNA.
DR   EMBL; AL672056; CAM25261.1; -; Genomic_DNA.
DR   EMBL; AL645567; CAM25261.1; JOINED; Genomic_DNA.
DR   EMBL; AL672056; CAM25262.1; -; Genomic_DNA.
DR   EMBL; AL645567; CAM25262.1; JOINED; Genomic_DNA.
DR   EMBL; BC003767; AAH03767.1; -; mRNA.
DR   IPI; IPI00135446; -.
DR   IPI; IPI00224993; -.
DR   IPI; IPI00404687; -.
DR   RefSeq; NP_032220.1; NM_008194.3.
DR   RefSeq; NP_997609.1; NM_212444.2.
DR   UniGene; Mm.246682; -.
DR   ProteinModelPortal; Q64516; -.
DR   SMR; Q64516; 10-523.
DR   STRING; Q64516; -.
DR   PRIDE; Q64516; -.
DR   Ensembl; ENSMUST00000026039; ENSMUSP00000026039; ENSMUSG00000025059.
DR   Ensembl; ENSMUST00000113978; ENSMUSP00000109611; ENSMUSG00000025059.
DR   GeneID; 14933; -.
DR   KEGG; mmu:14933; -.
DR   NMPDR; fig|10090.3.peg.21824; -.
DR   UCSC; uc009trw.1; mouse.
DR   CTD; 14933; -.
DR   MGI; MGI:106594; Gyk.
DR   eggNOG; roNOG10665; -.
DR   HOGENOM; HBG511469; -.
DR   HOVERGEN; HBG002451; -.
DR   InParanoid; Q64516; -.
DR   OMA; KILPNVR; -.
DR   OrthoDB; EOG41G33T; -.
DR   BRENDA; 2.7.1.30; 244.
DR   ArrayExpress; Q64516; -.
DR   Bgee; Q64516; -.
DR   CleanEx; MM_GYK; -.
DR   Genevestigator; Q64516; -.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004370; F:glycerol kinase activity; IDA:MGI.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:InterPro.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
DR   InterPro; IPR018485; Carb_kinase_FGGY_C.
DR   InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR   InterPro; IPR018484; Carb_kinase_FGGY_N.
DR   InterPro; IPR005999; Glycerol_kin.
DR   PANTHER; PTHR10196; FGGY_kin; 1.
DR   PANTHER; PTHR10196:SF9; Glycerol_kin; 1.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   TIGRFAMs; TIGR01311; glycerol_kin; 1.
DR   PROSITE; PS00933; FGGY_KINASES_1; 1.
DR   PROSITE; PS00445; FGGY_KINASES_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Glycerol metabolism;
KW   Kinase; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   Nucleotide-binding; Transferase.
FT   CHAIN         1    559       Glycerol kinase.
FT                                /FTId=PRO_0000059538.
FT   NP_BIND     433    437       ATP (By similarity).
FT   BINDING      20     20       Substrate (By similarity).
FT   BINDING      24     24       ATP (By similarity).
FT   BINDING      94     94       Substrate (By similarity).
FT   BINDING     148    148       Substrate (By similarity).
FT   BINDING     265    265       Substrate (By similarity).
FT   BINDING     287    287       ATP (By similarity).
FT   BINDING     332    332       ATP; via carbonyl oxygen (By similarity).
FT   VAR_SEQ     245    250       Missing (in isoform 1 and isoform 2).
FT                                /FTId=VSP_034650.
FT   VAR_SEQ     528    556       Missing (in isoform 1).
FT                                /FTId=VSP_034651.
FT   CONFLICT     55     55       Q -> R (in Ref. 2; BAC31861).
SQ   SEQUENCE   559 AA;  61227 MW;  09A58CB47AB5CD41 CRC64;
     MAAAKKAVLG PLVGAVDQGT SSTRFLVFNS KTAELLSHHQ VEIKQEFPRE GWVEQDPKEI
     LQSVYECIEK TCEKLGQLNI DISNIKAIGV SNQRETTVVW DKVTGEPLYN AVVWLDLRTQ
     STVENLSKRI PGNNNFVKSK TGLPLSTYFS AVKLRWLLDN VKKVQEAVEE NRALFGTIDS
     WLIWSLTGGI HGGVHCTDVT NASRTMLFNI HSLEWDKELC EFFGIPMEIL PNVRSSSEIY
     GLMKISHSLK AGALEGVPIS GCLGDQSAAL VGQMCFQDGQ AKNTYGTGCF LLCNTGHKCV
     FSEHGLLTTV AYKLGRDKPV YYALEGSVAI AGAVIRWLRD NLGIIKSSEE IEKLAKEVGT
     SYGCYFVPAF SGLYAPYWEP SARGIICGLT QFTNKCHIAF AALEAVCFQT REILDAMNRD
     CGIPLSHLQV DGGMTSNKIL MQLQADILYI PVVKPSMPET TALGAAMAAG AAEGVGVWSL
     EPEDLSAVTM ERFEPQINAE ESEIRYSTWK KAVMKSIGWV TTQSPESGDP SIFCSLPLGF
     FIVSSMVMLI GARYISGIP
//
ID   AT2A3_MOUSE             Reviewed;        1038 AA.
AC   Q64518; O70625; Q64517;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   18-OCT-2001, sequence version 2.
DT   08-MAR-2011, entry version 100.
DE   RecName: Full=Sarcoplasmic/endoplasmic reticulum calcium ATPase 3;
DE            Short=SERCA3;
DE            Short=SR Ca(2+)-ATPase 3;
DE            EC=3.6.3.8;
DE   AltName: Full=Calcium pump 3;
GN   Name=Atp2a3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SERCA3A AND SERCA3B).
RC   STRAIN=C57BL/6;
RA   Tokuyama Y., Chen X., Roe M.W., Bell G.I.;
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM SERCA3A), AND
RP   ALTERNATIVE SPLICING.
RX   MEDLINE=98256332; PubMed=9593748; DOI=10.1074/jbc.273.22.13982;
RA   Dode L., De Greef C., Mountian I., Attard M., Town M.M., Casteels R.,
RA   Wuytack F.;
RT   "Structure of the human sarco/endoplasmic reticulum Ca2+-ATPase 3
RT   gene. Promoter analysis and alternative splicing of the SERCA3 pre-
RT   mRNA.";
RL   J. Biol. Chem. 273:13982-13994(1998).
CC   -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis
CC       of ATP coupled with the transport of the calcium. Transports
CC       calcium ions from the cytosol into the sarcoplasmic/endoplasmic
CC       reticulum lumen. Contributes to calcium sequestration involved in
CC       muscular excitation/contraction.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + Ca(2+)(Cis) = ADP + phosphate +
CC       Ca(2+)(Trans).
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane; Multi-pass membrane
CC       protein (By similarity). Endoplasmic reticulum membrane; Multi-
CC       pass membrane protein (By similarity). Sarcoplasmic reticulum
CC       membrane; Multi-pass membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=SERCA3B;
CC         IsoId=Q64518-1; Sequence=Displayed;
CC       Name=SERCA3A;
CC         IsoId=Q64518-2; Sequence=VSP_000369;
CC       Name=SERCA3C;
CC         IsoId=Q64518-3; Sequence=VSP_000370;
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       (TC 3.A.3) family. Type IIA subfamily.
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DR   EMBL; U49394; AAB04099.1; -; mRNA.
DR   EMBL; U49393; AAB04098.1; -; mRNA.
DR   EMBL; Y15734; CAA75744.1; -; Genomic_DNA.
DR   EMBL; Y15735; CAA75744.1; JOINED; Genomic_DNA.
DR   EMBL; Y15734; CAA75745.1; -; Genomic_DNA.
DR   EMBL; Y15735; CAA75745.1; JOINED; Genomic_DNA.
DR   EMBL; Y15734; CAA75743.1; -; Genomic_DNA.
DR   EMBL; Y15735; CAA75743.1; JOINED; Genomic_DNA.
DR   EMBL; Y15736; CAA75746.1; -; Genomic_DNA.
DR   IPI; IPI00311200; -.
DR   IPI; IPI00336889; -.
DR   IPI; IPI00944111; -.
DR   RefSeq; NP_001156809.1; NM_001163337.1.
DR   RefSeq; NP_058025.2; NM_016745.3.
DR   UniGene; Mm.6306; -.
DR   ProteinModelPortal; Q64518; -.
DR   SMR; Q64518; 1-994.
DR   STRING; Q64518; -.
DR   PRIDE; Q64518; -.
DR   Ensembl; ENSMUST00000021142; ENSMUSP00000021142; ENSMUSG00000020788.
DR   Ensembl; ENSMUST00000108485; ENSMUSP00000104125; ENSMUSG00000020788.
DR   GeneID; 53313; -.
DR   KEGG; mmu:53313; -.
DR   CTD; 53313; -.
DR   MGI; MGI:1194503; Atp2a3.
DR   eggNOG; maNOG16465; -.
DR   HOGENOM; HBG456486; -.
DR   HOVERGEN; HBG105648; -.
DR   InParanoid; Q64518; -.
DR   PhylomeDB; Q64518; -.
DR   BRENDA; 3.6.3.8; 244.
DR   ArrayExpress; Q64518; -.
DR   Bgee; Q64518; -.
DR   CleanEx; MM_ATP2A3; -.
DR   Genevestigator; Q64518; -.
DR   GermOnline; ENSMUSG00000020788; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005388; F:calcium-transporting ATPase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   InterPro; IPR023306; ATPase_cation_domN.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR005782; ATPase_P-typ_Ca-transp.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023300; ATPase_P-typ_cyto_domA.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Gene3D; G3DSA:2.70.150.10; ATPase_P-typ_cyto_domA; 2.
DR   Gene3D; G3DSA:3.40.1110.10; ATPase_P-typ_cyto_domN; 1.
DR   Gene3D; G3DSA:1.20.1110.10; ATPase_P-typ_TM_dom; 2.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81660; ATPase_cation_domN; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01116; ATPase-IIA1_Ca; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 4.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; ATP-binding; Calcium;
KW   Calcium transport; Endoplasmic reticulum; Hydrolase; Ion transport;
KW   Magnesium; Membrane; Metal-binding; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Sarcoplasmic reticulum; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1   1038       Sarcoplasmic/endoplasmic reticulum
FT                                calcium ATPase 3.
FT                                /FTId=PRO_0000046203.
FT   TOPO_DOM      1     48       Cytoplasmic (By similarity).
FT   TRANSMEM     49     69       Helical; Name=1; (By similarity).
FT   TOPO_DOM     70     89       Lumenal (By similarity).
FT   TRANSMEM     90    110       Helical; Name=2; (By similarity).
FT   TOPO_DOM    111    253       Cytoplasmic (By similarity).
FT   TRANSMEM    254    273       Helical; Name=3; (By similarity).
FT   TOPO_DOM    274    295       Lumenal (By similarity).
FT   TRANSMEM    296    313       Helical; Name=4; (By similarity).
FT   TOPO_DOM    314    757       Cytoplasmic (By similarity).
FT   TRANSMEM    758    777       Helical; Name=5; (By similarity).
FT   TOPO_DOM    778    787       Lumenal (By similarity).
FT   TRANSMEM    788    808       Helical; Name=6; (By similarity).
FT   TOPO_DOM    809    828       Cytoplasmic (By similarity).
FT   TRANSMEM    829    851       Helical; Name=7; (By similarity).
FT   TOPO_DOM    852    897       Lumenal (By similarity).
FT   TRANSMEM    898    917       Helical; Name=8; (By similarity).
FT   TOPO_DOM    918    930       Cytoplasmic (By similarity).
FT   TRANSMEM    931    949       Helical; Name=9; (By similarity).
FT   TOPO_DOM    950    964       Lumenal (By similarity).
FT   TRANSMEM    965    985       Helical; Name=10; (By similarity).
FT   TOPO_DOM    986   1038       Cytoplasmic (By similarity).
FT   ACT_SITE    351    351       4-aspartylphosphate intermediate (By
FT                                similarity).
FT   METAL       304    304       Calcium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       305    305       Calcium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       307    307       Calcium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       309    309       Calcium 2 (By similarity).
FT   METAL       703    703       Magnesium (By similarity).
FT   METAL       707    707       Magnesium (By similarity).
FT   METAL       768    768       Calcium 1 (By similarity).
FT   METAL       771    771       Calcium 1 (By similarity).
FT   METAL       796    796       Calcium 2 (By similarity).
FT   METAL       799    799       Calcium 1 (By similarity).
FT   METAL       800    800       Calcium 1 (By similarity).
FT   METAL       800    800       Calcium 2 (By similarity).
FT   METAL       908    908       Calcium 1 (By similarity).
FT   BINDING     515    515       ATP (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   VAR_SEQ     994   1038       GVLGTFMQARSRQLPTTSRTPYHTGKKGPEVNPGSRGESPV
FT                                WPSD -> EKKDLK (in isoform SERCA3A).
FT                                /FTId=VSP_000369.
FT   VAR_SEQ    1019   1038       KKGPEVNPGSRGESPVWPSD -> LACKKKT (in
FT                                isoform SERCA3C).
FT                                /FTId=VSP_000370.
SQ   SEQUENCE   1038 AA;  113608 MW;  47C3763E843EEA8E CRC64;
     MEEAHLLSAA DVLRRFSVTA EGGLSLEQVT DARERYGPNE LPTEEGKSLW ELVVEQFEDL
     LVRILLLAAL VSFVLAWFEE GEETTTAFVE PLVIMLILVA NAIVGVWQER NAESAIEALK
     EYEPEMGKVI RSDRKGVQRI RARDIVPGDI VEVAVGDKVP ADLRLIEIKS TTLRVDQSIL
     TGESVSVTKH TDAIPDPRAV NQDKKNMLFS GTNIASGKAL GVAVATGLQT ELGKIRSQMA
     AVEPERTPLQ RKLDEFGRQL SHAISVICVA VWVINIGHFA DPAHGGSWLR GAVYYFKIAV
     ALAVAAIPEG LPAVITTCLA LGTRRMARKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ
     MSVCRMFVVA EAEAGTCRLH EFTISGTTYT PEGEVRQGEQ PVRCGQFDGL VELATICALC
     NDSALDYNEA KGVYEKVGEA TETALTCLVE KMNVFDTDLK GLSRVERAGA CNSVIKQLMR
     KEFTLEFSRD RKSMSVYCTP TRADPKVQGS KMFVKGAPES VIERCSSVRV GSRTAPLSTT
     SREHILAKIR DWGSGSDTLR CLALATRDTP PRKEDMHLDD CSRFVQYETD LTFVGCVGML
     DPPRPEVAAC ITRCSRAGIR VVMITGDNKG TAVAICRRLG IFGDTEDVLG KAYTGREFDD
     LSPEQQRQAC RTARCFARVE PAHKSRIVEN LQSFNEITAM TGDGVNDAPA LKKAEIGIAM
     GSGTAVAKSA AEMVLSDDNF ASIVAAVEEG RAIYNNMKQF IRYLISSNVG EVVCIFLTAI
     LGLPEALIPV QLLWVNLVTD GLPATALGFN PPDLDIMEKP PRNPREALIS GWLFFRYLAI
     GVYVGLATVA AATWWFLYDA EGPQVTFYQL RNFLKCSEDN PLFAGIDCKV FESRFPTTMA
     LSVLVTIEMC NALNSVSENQ SLLRMPPWLN PWLLGAVVMS MALHFLILLV PPLPLIFQVT
     PLSGRQWGVV LQMSLPVILL DEALKYLSRN HMDGVLGTFM QARSRQLPTT SRTPYHTGKK
     GPEVNPGSRG ESPVWPSD
//
ID   SDC3_MOUSE              Reviewed;         442 AA.
AC   Q64519; Q3UDD9; Q6ZQA4; Q7TQD4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Syndecan-3;
DE            Short=SYND3;
DE   Flags: Precursor;
GN   Name=Sdc3; Synonyms=Kiaa0468;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X CBA;
RA   Kung C.E., Deuel T.F.;
RT   "Cloning of rat and mouse syndecan-3 cDNAs.";
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Cell surface proteoglycan that may bear heparan sulfate.
CC       May have a role in the organization of cell shape by affecting the
CC       actin cytoskeleton, possibly by transferring signals from the cell
CC       surface in a sugar-dependent mechanism (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- PTM: O-glycosylated within the Thr/Ser-rich region which could
CC       interact with lectin domains on other molecules (Probable).
CC   -!- SIMILARITY: Belongs to the syndecan proteoglycan family.
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DR   EMBL; U52826; AAB03283.1; -; mRNA.
DR   EMBL; AK129153; BAC97963.1; -; mRNA.
DR   EMBL; AK150120; BAE29322.1; -; mRNA.
DR   EMBL; AK155127; BAE33064.1; -; mRNA.
DR   EMBL; BC054795; AAH54795.1; -; mRNA.
DR   EMBL; BC062093; AAH62093.1; -; mRNA.
DR   IPI; IPI00135452; -.
DR   RefSeq; NP_035650.2; NM_011520.3.
DR   UniGene; Mm.206536; -.
DR   ProteinModelPortal; Q64519; -.
DR   SMR; Q64519; 410-442.
DR   IntAct; Q64519; 1.
DR   STRING; Q64519; -.
DR   PhosphoSite; Q64519; -.
DR   PRIDE; Q64519; -.
DR   Ensembl; ENSMUST00000070478; ENSMUSP00000065877; ENSMUSG00000025743.
DR   GeneID; 20970; -.
DR   KEGG; mmu:20970; -.
DR   UCSC; uc008uzr.1; mouse.
DR   CTD; 20970; -.
DR   MGI; MGI:1349163; Sdc3.
DR   eggNOG; maNOG18190; -.
DR   GeneTree; ENSGT00530000063116; -.
DR   HOGENOM; HBG268654; -.
DR   HOVERGEN; HBG004144; -.
DR   InParanoid; Q64519; -.
DR   OMA; EETTQPD; -.
DR   OrthoDB; EOG4N30Q5; -.
DR   NextBio; 299934; -.
DR   ArrayExpress; Q64519; -.
DR   Bgee; Q64519; -.
DR   CleanEx; MM_SDC3; -.
DR   Genevestigator; Q64519; -.
DR   GermOnline; ENSMUSG00000025743; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR   InterPro; IPR003585; Neurexin-like.
DR   InterPro; IPR001050; Syndecan.
DR   PANTHER; PTHR10915; Syndecan; 1.
DR   Pfam; PF01034; Syndecan; 1.
DR   SMART; SM00294; 4.1m; 1.
DR   PROSITE; PS00964; SYNDECAN; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Heparan sulfate; Membrane; Phosphoprotein; Proteoglycan;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     44       Potential.
FT   CHAIN        45    442       Syndecan-3.
FT                                /FTId=PRO_0000033508.
FT   TOPO_DOM     45    387       Extracellular (Potential).
FT   TRANSMEM    388    408       Helical; (Potential).
FT   TOPO_DOM    409    442       Cytoplasmic (Potential).
FT   COMPBIAS    114    302       Ser/Thr-rich (mucin-like).
FT   SITE        383    384       Cleavage of ectodomain (Potential).
FT   MOD_RES     441    441       Phosphotyrosine (By similarity).
FT   CARBOHYD     78     78       O-linked (Xyl...) (glycosaminoglycan)
FT                                (Potential).
FT   CARBOHYD     80     80       O-linked (Xyl...) (glycosaminoglycan)
FT                                (Potential).
FT   CARBOHYD     82     82       O-linked (Xyl...) (glycosaminoglycan)
FT                                (Potential).
FT   CARBOHYD     89     89       O-linked (Xyl...) (glycosaminoglycan)
FT                                (Potential).
FT   CARBOHYD    315    315       O-linked (Xyl...) (glycosaminoglycan)
FT                                (Potential).
FT   CARBOHYD    367    367       O-linked (Xyl...) (glycosaminoglycan)
FT                                (Potential).
FT   CONFLICT    133    133       S -> R (in Ref. 1; AAB03283).
FT   CONFLICT    147    147       T -> K (in Ref. 1; AAB03283).
FT   CONFLICT    258    259       RA -> QS (in Ref. 1; AAB03283).
FT   CONFLICT    264    264       V -> I (in Ref. 1; AAB03283).
FT   CONFLICT    270    270       D -> E (in Ref. 1; AAB03283).
FT   CONFLICT    289    289       M -> V (in Ref. 1; AAB03283).
FT   CONFLICT    302    302       I -> T (in Ref. 1; AAB03283).
FT   CONFLICT    358    358       P -> L (in Ref. 1; AAB03283).
FT   CONFLICT    375    375       P -> L (in Ref. 1; AAB03283).
FT   CONFLICT    429    429       V -> D (in Ref. 4; BAE29322).
SQ   SEQUENCE   442 AA;  46002 MW;  E8FF8B90C5F0706B CRC64;
     MKPGPPRRGT AQGQRVDTAT HAPGARGLLL PPLLLLLLAG RAAGAQRWRN ENFERPVDLE
     GSGDDDSFPD DELDDLYSGS GSGYFEQESG LETAMRFIPD MALAAPTAPA MLPTTVIQPV
     DTPFEELLSE HPSPEPVTSP PLVTEVTEVV EESSQKATTI STTTSTTAAT TTGAPTMATA
     PATAATTAPS TPEAPPATAT VADVRTTGIQ GMLPLPLTTA ATAKITTPAA PSPPTTVATL
     DTEAPTPRLV NTATSRPRAL PRPVTTQEPD VAERSTLPLG TTAPGPTEMA QTPTPESLLT
     TIQDEPEVPV SGGPSGDFEL QEETTQPDTA NEVVAVEGAA AKPSPPLGTL PKGARPGPGL
     HDNAIDSGSS AAQLPQKSIL ERKEVLVAVI VGGVVGALFA AFLVTLLIYR MKKKDEGSYT
     LEEPKQASVT YQKPDKQEEF YA
//
ID   RBL2_MOUSE              Reviewed;        1135 AA.
AC   Q64700;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Retinoblastoma-like protein 2;
DE   AltName: Full=130 kDa retinoblastoma-associated protein;
DE            Short=p130;
DE   AltName: Full=Retinoblastoma-related protein 2;
DE            Short=RBR-2;
DE   AltName: Full=pRb2;
GN   Name=Rbl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96199216; PubMed=8621630; DOI=10.1074/jbc.271.16.9785;
RA   Chen G., Guy C.T., Chen H.W., Hu N., Lee E.Y.H.P., Lee W.H.;
RT   "Molecular cloning and developmental expression of mouse p130, a
RT   member of the retinoblastoma gene family.";
RL   J. Biol. Chem. 271:9567-9572(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96192345; PubMed=9019172;
RA   Pertile P., Baldi A., de Luca A., Virgilio L., Pisano M.M.,
RA   Giordano A.;
RT   "Molecular cloning, expression, and developmental characterization of
RT   the murine retinoblastoma-related gene Rb2/p130.";
RL   Cell Growth Differ. 6:1659-1664(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96203998; PubMed=8622859;
RA   Lecouter J.E., Whyte P.F.M., Rudnicki M.A.;
RT   "Cloning and expression of the Rb-related mouse p130 mRNA.";
RL   Oncogene 12:1433-1440(1996).
RN   [4]
RP   INTERACTION WITH USP4.
RX   PubMed=11571651; DOI=10.1038/sj.onc.1204823;
RA   Blanchette P., Gilchrist C.A., Baker R.T., Gray D.A.;
RT   "Association of UNP, a ubiquitin-specific protease, with the pocket
RT   proteins pRb, p107 and p130.";
RL   Oncogene 20:5533-5537(2001).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH SUV420H1 AND SUV420H2.
RX   PubMed=15750587; DOI=10.1038/ncb1235;
RA   Gonzalo S., Garcia-Cao M., Fraga M.F., Schotta G., Peters A.H.F.M.,
RA   Cotter S.E., Eguia R., Dean D.C., Esteller M., Jenuwein T.,
RA   Blasco M.A.;
RT   "Role of the RB1 family in stabilizing histone methylation at
RT   constitutive heterochromatin.";
RL   Nat. Cell Biol. 7:420-428(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410; THR-414; SER-636;
RP   THR-639; SER-942 AND THR-1027, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Key regulator of entry into cell division. Directly
CC       involved in heterochromatin formation by maintaining overall
CC       chromatin structure and, in particular, that of constitutive
CC       heterochromatin by stabilizing histone methylation. Recruits and
CC       targets histone methyltransferases SUV420H1 and SUV420H2, leading
CC       to epigenetic transcriptional repression. Controls histone H4
CC       'Lys-20' trimethylation. Probably acts as a transcription
CC       repressor by recruiting chromatin-modifying enzymes to promoters.
CC       Potent inhibitor of E2F-mediated trans-activation, associates
CC       preferentially with E2F5. Binds to cyclins A and E. Binds to and
CC       may be involved in the transforming capacity of the adenovirus E1A
CC       protein. May act as a tumor suppressor.
CC   -!- SUBUNIT: Interacts with AATF and RINT1. Component of the DREAM
CC       complex (also named LINC complex) at least composed of E2F4, E2F5,
CC       LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, RBL1, RBL2, RBBP4, TFDP1
CC       and TFDP2. The complex exists in quiescent cells where it
CC       represses cell cycle-dependent genes. It dissociates in S phase
CC       when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds to
CC       MYBL2. Interacts with USP4 (By similarity). Interacts with
CC       SUV420H1, SUV420H2 and USP4.
CC   -!- INTERACTION:
CC       Q155P7:Cenpf; NbExp=2; IntAct=EBI-2271232, EBI-2211248;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- PTM: During G0 and early G1 phase of the cell cycle,
CC       phosphorylated on Ser-636 and on 5 sites within the domain B.
CC       Phosphorylation on Ser-669 in G1 leads to its ubiquitin-dependent
CC       proteolysis (By similarity).
CC   -!- SIMILARITY: Belongs to the retinoblastoma protein (RB) family.
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DR   EMBL; U36799; AAB48991.1; -; mRNA.
DR   EMBL; U50850; AAC52598.1; -; mRNA.
DR   EMBL; U47333; AAC52555.1; -; mRNA.
DR   IPI; IPI00317271; -.
DR   RefSeq; NP_035380.3; NM_011250.3.
DR   UniGene; Mm.235580; -.
DR   ProteinModelPortal; Q64700; -.
DR   IntAct; Q64700; 3.
DR   MINT; MINT-5181879; -.
DR   STRING; Q64700; -.
DR   PhosphoSite; Q64700; -.
DR   PRIDE; Q64700; -.
DR   Ensembl; ENSMUST00000034091; ENSMUSP00000034091; ENSMUSG00000031666.
DR   GeneID; 19651; -.
DR   KEGG; mmu:19651; -.
DR   CTD; 19651; -.
DR   MGI; MGI:105085; Rbl2.
DR   HOGENOM; HBG358205; -.
DR   HOVERGEN; HBG017710; -.
DR   InParanoid; Q64700; -.
DR   OrthoDB; EOG4PNXG9; -.
DR   ArrayExpress; Q64700; -.
DR   Bgee; Q64700; -.
DR   CleanEx; MM_RBL2; -.
DR   Genevestigator; Q64700; -.
DR   GermOnline; ENSMUSG00000031666; Mus musculus.
DR   GO; GO:0005667; C:transcription factor complex; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR006670; Cyclin.
DR   InterPro; IPR011028; Cyclin-like.
DR   InterPro; IPR013763; Cyclin-related.
DR   InterPro; IPR002720; RB_A.
DR   InterPro; IPR002719; RB_B.
DR   Gene3D; G3DSA:1.10.472.10; Cyclin_related; 4.
DR   Pfam; PF01858; RB_A; 1.
DR   Pfam; PF01857; RB_B; 1.
DR   SMART; SM00385; CYCLIN; 2.
DR   SUPFAM; SSF47954; Cyclin_like; 2.
PE   1: Evidence at protein level;
KW   Cell cycle; Chromatin regulator; DNA-binding; Nucleus; Phosphoprotein;
KW   Repressor; Transcription; Transcription regulation; Tumor suppressor.
FT   CHAIN         1   1135       Retinoblastoma-like protein 2.
FT                                /FTId=PRO_0000167842.
FT   REGION      414   1021       Pocket; binds E1A.
FT   REGION      414    613       Domain A.
FT   REGION      614    824       Spacer.
FT   REGION      825   1021       Domain B.
FT   COMPBIAS      9     13       Poly-Pro.
FT   COMPBIAS     14     17       Poly-Ala.
FT   COMPBIAS     20     24       Poly-Glu.
FT   COMPBIAS    992    995       Poly-Glu.
FT   MOD_RES     398    398       Phosphothreonine (By similarity).
FT   MOD_RES     410    410       Phosphoserine.
FT   MOD_RES     414    414       Phosphothreonine.
FT   MOD_RES     636    636       Phosphoserine.
FT   MOD_RES     639    639       Phosphothreonine.
FT   MOD_RES     659    659       Phosphoserine (By similarity).
FT   MOD_RES     668    668       Phosphoserine (By similarity).
FT   MOD_RES     669    669       Phosphoserine (By similarity).
FT   MOD_RES     684    684       Phosphoserine (By similarity).
FT   MOD_RES     942    942       Phosphoserine.
FT   MOD_RES     946    946       Phosphoserine (By similarity).
FT   MOD_RES     960    960       Phosphoserine (By similarity).
FT   MOD_RES     965    965       Phosphoserine (By similarity).
FT   MOD_RES     967    967       Phosphoserine (By similarity).
FT   MOD_RES     968    968       Phosphothreonine (By similarity).
FT   MOD_RES     975    975       Phosphoserine (By similarity).
FT   MOD_RES     976    976       Phosphoserine (By similarity).
FT   MOD_RES     980    980       Phosphothreonine (By similarity).
FT   MOD_RES    1027   1027       Phosphothreonine.
FT   MOD_RES    1031   1031       Phosphoserine (By similarity).
FT   MOD_RES    1106   1106       Phosphoserine (By similarity).
FT   MOD_RES    1108   1108       Phosphoserine (By similarity).
FT   CONFLICT    211    253       Missing (in Ref. 3).
FT   CONFLICT    341    341       A -> P (in Ref. 2; AAB48991).
FT   CONFLICT    342    342       A -> P (in Ref. 3; AAC52555).
FT   CONFLICT    381    381       R -> T (in Ref. 1; AAC52598).
FT   CONFLICT    428    428       T -> S (in Ref. 1; AAC52598).
FT   CONFLICT    431    431       S -> T (in Ref. 1; AAC52598).
FT   CONFLICT    443    443       Q -> R (in Ref. 2 and 3).
FT   CONFLICT    484    493       Missing (in Ref. 2).
FT   CONFLICT    768    768       A -> R (in Ref. 1; AAC52598).
FT   CONFLICT    826    826       P -> A (in Ref. 3; AAC52555).
FT   CONFLICT    947    948       PT -> RA (in Ref. 3; AAC52555).
FT   CONFLICT   1023   1023       S -> A (in Ref. 2 and 3).
FT   CONFLICT   1044   1044       V -> I (in Ref. 1; AAC52598).
SQ   SEQUENCE   1135 AA;  127473 MW;  0565E4F998ACCA0D CRC64;
     MASGGNQSPP PPPAAAASSE EEEEDGDAAD RAQPAGSPSH QIQQRFEELC SRLNMDEAAR
     AEAWSSYRSM SESYTLEGND LHWLACALYV ACRKSVPTVS KGTAEGNYVS LTRILRCSEQ
     SLIEFFNKMK KWEDMANLPP HFRERTERLE RNFTVSAVIF KKYEPIFQDI FKYPQEEQPR
     QQRGRKQRRQ PCTTSEIFHF CWVLFIYAKG NFPMISDDLV NSYHLLLCAL DLVYGNALQC
     SNRKELVNPN FKGLSEDCHP KDSKASSDPP CVIEKLCSLH DGLVLEAKGI KEHFWKPYIR
     KLFEKKLLKG KEENLTGFLE PGNFGESFKA VNKAYEEYVL AAGNLDERVF LGEDAEEEVG
     TLSRCLSAAS GTESAERTQM RDILQQHLDK SKALRVCTPL TGVRYVQENS PCVTPVSTAA
     HSLSRLHTML SGLRNAPSEK LEQILRSCSR DPTQAIADRL KEMYEIYSQH FQPDENFSNC
     AKEIANKHFR FAEMLYYKVL ESVIEQEQKR LGDMDLSGVL EHDAFHRSLL ACCLEVVAFS
     HKPPGNFPFI AEIFDVPHYH FYKVIEVFIR AEDGLCREVV KHLNQIEEQI LDHLAWKTKS
     PLWDRIRDNE NRVPTCEEVM PPQNLERTDE IYIAGSPLTP RRVGEVRADA GGLGRSITSP
     TTLYDRYSSP TVSTTRRRLF ENDSPSEGST SGRIPPQPLV NAVPVQNVPG ETVSVTPVPG
     QTLVTMATAT VTANNGQTVT IPVQGIANEN GGITFFPVQV NVGGQAQAVA GSIQPLSAQA
     LAGSLSSQQV TGTTLQVPGP VAIQQISPGG QQQNPGQPLT SSSIRPRKTS SLALFFRKVY
     YLAGVRLRDL CIKLDISDEL RKKIWTCFEF SIIQCTELMM DRHLDQLLMC AIYVMAKVTK
     EDRSFQNIMR CYRTQPQARS QVYRSVLIKG KRRNSGSSES RSHQNSPTEL NTDRASRDSS
     PVMRSNSTLP VPQPSSAPPT PTRLTGASSD VEEEERGDLI QFYNNIYRKQ IQAFAMKYSQ
     ANSQTDTPPL SPYPFVRTGS PRRVQLSQSH PIYISPHNNE AMPSPREKIF YYFSNSPSKR
     LREINSMIRT GETPTKKRGI LLDDGSESPA KRICPENHSA LLRRLQDVAN DRGSQ
//
ID   VINC_MOUSE              Reviewed;        1066 AA.
AC   Q64727; Q8BP32; Q8BS46; Q922C5; Q922D9;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   08-MAR-2011, entry version 104.
DE   RecName: Full=Vinculin;
DE   AltName: Full=Metavinculin;
GN   Name=Vcl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=129/SvJ; TISSUE=Embryo;
RX   PubMed=7568093; DOI=10.1073/pnas.92.20.9161;
RA   Coll J.-L., Ben-Ze'ev A., Ezzell R.M., Rodriguez Fernandez J.L.,
RA   Baribault H., Oshima R.G., Adamson E.D.;
RT   "Targeted disruption of vinculin genes in F9 and embryonic stem cells
RT   changes cell morphology, adhesion, and locomotion.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:9161-9165(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=97424359; PubMed=9280281; DOI=10.1016/S0014-5793(97)00901-0;
RA   Alatortsev V.E., Kramerova I.A., Frolov M.V., Lavrov S.A.,
RA   Westphal E.D.;
RT   "Vinculin gene is non-essential in Drosophila melanogaster.";
RL   FEBS Lett. 413:197-201(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Forelimb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 286-300; 656-666 AND 916-924, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   INTERACTION WITH SORBS1.
RX   MEDLINE=99187134; PubMed=10085297; DOI=10.1083/jcb.144.5.1001;
RA   Mandai K., Nakanishi H., Satoh A., Takahashi K., Satoh K.,
RA   Nishioka H., Mizoguchi A., Takai Y.;
RT   "Ponsin/SH3P12: an l-afadin- and vinculin-binding protein localized at
RT   cell-cell and cell-matrix adherens junctions.";
RL   J. Cell Biol. 144:1001-1017(1999).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-822, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-324 AND SER-774, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290 AND SER-721, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290 AND SER-721, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [12]
RP   REGION INVOLVED IN PHOSPHOLIPID MEMBRANE INSERTION.
RX   PubMed=20599708; DOI=10.1016/j.bbrc.2010.06.094;
RA   Wirth V.F., List F., Diez G., Goldmann W.H.;
RT   "Vinculin's C-terminal region facilitates phospholipid membrane
RT   insertion.";
RL   Biochem. Biophys. Res. Commun. 398:433-437(2010).
CC   -!- FUNCTION: Actin filament (F-actin)-binding protein involved in
CC       cell-matrix adhesion and cell-cell adhesion. Regulates cell-
CC       surface E-cadherin expression and potentiates mechanosensing by
CC       the E-cadherin complex. May also play important roles in cell
CC       morphology and locomotion (By similarity).
CC   -!- SUBUNIT: Exhibits self-association properties. Interacts with
CC       NRAP, SORBS1 and TLN1. Interacts with SYNM. Interacts with CTNNB1
CC       and this interaction is necessary for its localization to the
CC       cell-cell junctions and for its function in regulating cell
CC       surface expression of E-cadherin (By similarity).
CC   -!- INTERACTION:
CC       Q61210:Arhgef1; NbExp=2; IntAct=EBI-432047, EBI-641821;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Cell junction, adherens junction (By similarity). Cell membrane;
CC       Peripheral membrane protein; Cytoplasmic side (By similarity).
CC       Cell junction (By similarity). Note=Cytoplasmic face of adhesion
CC       plaques. Recruitment to cell-cell junctions occurs in a myosin II-
CC       dependent manner. Interaction with CTNNB1 is necessary for its
CC       localization to the cell-cell junctions (By similarity).
CC   -!- DOMAIN: Exists in at least two conformations. When in the closed,
CC       'inactive' conformation, extensive interactions between the head
CC       and tail domains prevent detectable binding to most of its
CC       ligands. It takes on an 'active' conformation after cooperative
CC       and simultaneous binding of two different ligands. This activation
CC       involves displacement of the head-tail interactions and leads to a
CC       significant accumulation of ternary complexes. The active form
CC       then binds a number of proteins that have both signaling and
CC       structural roles that are essential for cell adhesion (By
CC       similarity).
CC   -!- DOMAIN: The N-terminal globular head (Vh) comprises of subdomains
CC       D1-D4. The C-terminal tail (Vt) binds F-actin and cross-links
CC       actin filaments into bundles. An intramolecular interaction
CC       between Vh and Vt masks the F-actin-binding domain located in Vt.
CC       The binding of talin and alpha-actinin to the D1 subdomain of
CC       vinculin induces a helical bundle conversion of this subdomain,
CC       leading to the disruption of the intramolecular interaction and
CC       the exposure of the cryptic F-actin-binding domain of Vt. Vt
CC       inhibits actin filament barbed end elongation without affecting
CC       the critical concentration of actin assembly (By similarity).
CC   -!- PTM: Phosphorylated; on serines, threonines and tyrosines.
CC       Phosphorylation on Tyr-1065 in activated platelets affects head-
CC       tail interactions and cell spreading but has no effect on actin
CC       binding nor on localization to focal adhesion plaques (By
CC       similarity).
CC   -!- PTM: Aceylated; mainly by myristic acid but also small amount of
CC       palmitic acid (By similarity).
CC   -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; L13300; AAA40557.1; -; Genomic_DNA.
DR   EMBL; L13299; AAA40557.1; JOINED; Genomic_DNA.
DR   EMBL; L18880; AAB96843.1; -; mRNA.
DR   EMBL; AK035184; BAC28973.1; -; mRNA.
DR   EMBL; AK077850; BAC37033.1; -; mRNA.
DR   EMBL; BC008520; AAH08520.1; -; mRNA.
DR   EMBL; BC008554; AAH08554.1; -; mRNA.
DR   IPI; IPI00405227; -.
DR   PIR; A60965; A60965.
DR   PIR; T10108; T10108.
DR   RefSeq; NP_033528.3; NM_009502.4.
DR   UniGene; Mm.279361; -.
DR   ProteinModelPortal; Q64727; -.
DR   SMR; Q64727; 1-258, 882-1063.
DR   IntAct; Q64727; 4.
DR   MINT; MINT-1634466; -.
DR   STRING; Q64727; -.
DR   PhosphoSite; Q64727; -.
DR   REPRODUCTION-2DPAGE; Q64727; -.
DR   PRIDE; Q64727; -.
DR   Ensembl; ENSMUST00000022369; ENSMUSP00000022369; ENSMUSG00000021823.
DR   GeneID; 22330; -.
DR   KEGG; mmu:22330; -.
DR   UCSC; uc007skz.1; mouse.
DR   CTD; 22330; -.
DR   MGI; MGI:98927; Vcl.
DR   eggNOG; roNOG04310; -.
DR   GeneTree; ENSGT00550000074411; -.
DR   HOGENOM; HBG358349; -.
DR   HOVERGEN; HBG079758; -.
DR   InParanoid; Q64727; -.
DR   OMA; VILHEEA; -.
DR   OrthoDB; EOG4P5K8C; -.
DR   NextBio; 302571; -.
DR   PMAP-CutDB; Q64727; -.
DR   ArrayExpress; Q64727; -.
DR   Bgee; Q64727; -.
DR   CleanEx; MM_VCL; -.
DR   Genevestigator; Q64727; -.
DR   GermOnline; ENSMUSG00000021823; Mus musculus.
DR   GO; GO:0043034; C:costamere; IDA:MGI.
DR   GO; GO:0005916; C:fascia adherens; IDA:MGI.
DR   GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0030032; P:lamellipodium assembly; IDA:MGI.
DR   GO; GO:0030334; P:regulation of cell migration; IDA:MGI.
DR   InterPro; IPR017997; Vinculin.
DR   InterPro; IPR006077; Vinculin/catenin.
DR   InterPro; IPR000633; Vinculin_CS.
DR   Pfam; PF01044; Vinculin; 2.
DR   PRINTS; PR00806; VINCULIN.
DR   SUPFAM; SSF47220; Vinculin/catenin; 7.
DR   PROSITE; PS00663; VINCULIN_1; 1.
DR   PROSITE; PS00664; VINCULIN_2; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Cell adhesion; Cell junction;
KW   Cell membrane; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Lipoprotein; Membrane; Myristate; Palmitate; Phosphoprotein; Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1066       Vinculin.
FT                                /FTId=PRO_0000064253.
FT   REPEAT      259    369       1.
FT   REPEAT      370    479       2.
FT   REPEAT      480    589       3.
FT   REGION        2    835       N-terminal globular head (By similarity).
FT   REGION      168    208       Talin-interaction (By similarity).
FT   REGION      259    589       3 X 112 AA tandem repeats.
FT   REGION      836    878       Linker (Pro-rich) (By similarity).
FT   REGION      879   1066       C-terminal tail (By similarity).
FT   REGION      935    978       Facilitates phospholipid membrane
FT                                insertion.
FT   REGION     1052   1066       Facilitates phospholipid membrane
FT                                insertion.
FT   COMPBIAS    837    878       Pro-rich.
FT   MOD_RES     100    100       Phosphotyrosine (By similarity).
FT   MOD_RES     173    173       N6-acetyllysine (By similarity).
FT   MOD_RES     290    290       Phosphoserine.
FT   MOD_RES     324    324       Phosphothreonine.
FT   MOD_RES     496    496       N6-acetyllysine (By similarity).
FT   MOD_RES     508    508       Phosphothreonine (By similarity).
FT   MOD_RES     537    537       Phosphotyrosine (Potential).
FT   MOD_RES     604    604       Phosphothreonine (By similarity).
FT   MOD_RES     692    692       Phosphotyrosine (By similarity).
FT   MOD_RES     721    721       Phosphoserine.
FT   MOD_RES     774    774       Phosphoserine.
FT   MOD_RES     822    822       Phosphotyrosine.
FT   MOD_RES    1065   1065       Phosphotyrosine; by SRC-type Tyr-kinases
FT                                (By similarity).
FT   CONFLICT     16     16       V -> E (in Ref. 1; AAB96843).
FT   CONFLICT    215    215       T -> S (in Ref. 1; AAB96843).
FT   CONFLICT    363    363       L -> V (in Ref. 1; AAB96843).
FT   CONFLICT    499    499       Q -> K (in Ref. 3; BAC37033).
FT   CONFLICT    501    501       Q -> R (in Ref. 1; AAB96843).
FT   CONFLICT    799    799       M -> K (in Ref. 3; BAC37033).
FT   CONFLICT    812    812       G -> D (in Ref. 1; AAB96843).
FT   CONFLICT   1044   1044       A -> T (in Ref. 3; BAC37033).
SQ   SEQUENCE   1066 AA;  116717 MW;  067F1B16A5285859 CRC64;
     MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVAAVQAA VSNLVRVGKE
     TVQTTEDQIL KRDMPPAFIK VENACTKLVQ AAQMLQSDPY SVPARDYLID GSRGILSGTS
     DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV VETMEDLVTY TKNLGPGMTK MAKMIDERQQ
     ELTHQEHRVM LVNSMNTVKE LLPVLISAMK IFVTTKNSKN QGIEEALKNR NFTVEKMSAE
     INEIIRVLQL TSWDEDAWAS KDTEAMKRAL ASIDSKLNQA KGWLRDPNAS PGDAGEQAIR
     QILDEAGKVG ELCAGKERRE ILGTCKMLGQ MTDQVADLRA RGQGASPVAM QKAQQVSQGL
     DVLTAKVENA ARKLEAMTNS KQSIAKKIDA AQNWLADPNG GPEGEEQIRG ALAEARKIAE
     LCDDPKERDD ILRSLGEIAA LTSKLGDLRR QGKGDSPEAR ALAKQVATAL QNLQTKTNRA
     VANSRPAKAA VHLEGKIEQA QRWIDNPTVD DRGVGQAAIR GLVAEGHRLA NVMMGPYRQD
     LLAKCDRVDQ LTAQLADLAA RGEGESPQAR ALASQLQDSL KDLKAQMQEA MTQEVSDVFS
     DTTTPIKLLA VAATAPPDAP NREEVFDERA ANFENHSGRL GATAEKAAAV GTANKSTVEG
     IQASVKTARE LTPQVISAAR ILLRNPGNQA AYEHFETMKN QWIDNVEKMT GLVDEAIDTK
     SLLDASEEAI KKDLDKCKVA MANIQPQMLV AGATSIARRA NRILLVAKRE VENSEDPKFR
     EAVKAASDEL SKTISPMVMD AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP
     DFPPPPPDLE QLRLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEVINQPMMM
     AARQLHDEAR KWSSKGNDII AAAKRMALLM AEMSRLVRGG SGTKRALIQC AKDIAKASDE
     VTRLAKEVAK QCTDKRIRTN LLQVCERIPT ISTQLKILST VKATMLGRTN ISDEESEQAT
     EMLVHNAQNL MQSVKETVRE AEAASIKIRT DAGFTLRWVR KTPWYQ
//
ID   Q64730_MOUSE            Unreviewed;      1343 AA.
AC   Q64730;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   SubName: Full=Leucocyte common antigen (L-CA);
DE   Flags: Fragment;
GN   Name=Ptprc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=87260986; PubMed=2955416; DOI=10.1073/pnas.84.15.5360;
RA   Thomas M.L., Reynolds P.J., Chain A., Ben-Neriah Y., Trowbridge I.S.;
RT   "B-cell variant of mouse T200 (Ly-5): evidence for alternative mRNA
RT   splicing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 84:5360-5363(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=89197920; PubMed=2522930;
RA   Johnson N.A., Meyer C.M., Pingel J.T., Thomas M.L.;
RT   "Sequence conservation in potential regulatory regions of the mouse
RT   and human leukocyte common antigen gene.";
RL   J. Biol. Chem. 264:6220-6229(1989).
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; M23158; AAA39418.1; -; Genomic_DNA.
DR   EMBL; M23127; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23128; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23129; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23130; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23131; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23132; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23133; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23134; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23135; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23136; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23137; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23138; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23139; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23140; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23141; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23142; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23143; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23144; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23145; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23146; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23147; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23148; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23149; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23150; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23151; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23152; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23153; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23154; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23155; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23156; AAA39418.1; JOINED; Genomic_DNA.
DR   EMBL; M23157; AAA39418.1; JOINED; Genomic_DNA.
DR   IPI; IPI00323053; -.
DR   UniGene; Mm.391573; -.
DR   HSSP; P18052; 1YFO.
DR   ProteinModelPortal; Q64730; -.
DR   STRING; Q64730; -.
DR   Ensembl; ENSMUST00000074797; ENSMUSP00000074352; ENSMUSG00000026395.
DR   MGI; MGI:97810; Ptprc.
DR   GeneTree; ENSGT00590000082937; -.
DR   HOGENOM; HBG717275; -.
DR   HOVERGEN; HBG000066; -.
DR   InParanoid; Q64730; -.
DR   ArrayExpress; Q64730; -.
DR   Bgee; Q64730; -.
DR   Genevestigator; Q64730; -.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0043395; F:heparan sulfate proteoglycan binding; IDA:MGI.
DR   GO; GO:0008201; F:heparin binding; IDA:MGI.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:MGI.
DR   GO; GO:0000187; P:activation of MAPK activity; IMP:MGI.
DR   GO; GO:0030183; P:B cell differentiation; IMP:MGI.
DR   GO; GO:0050853; P:B cell receptor signaling pathway; IMP:MGI.
DR   GO; GO:0034113; P:heterotypic cell-cell adhesion; IMP:MGI.
DR   GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:MGI.
DR   GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
DR   GO; GO:0031953; P:negative regulation of protein autophosphorylation; IMP:MGI.
DR   GO; GO:0045060; P:negative thymic T cell selection; IMP:MGI.
DR   GO; GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IMP:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptosis; IMP:MGI.
DR   GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:MGI.
DR   GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; IMP:MGI.
DR   GO; GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; IMP:MGI.
DR   GO; GO:0048304; P:positive regulation of isotype switching to IgG isotypes; IMP:MGI.
DR   GO; GO:0043410; P:positive regulation of MAPKKK cascade; IMP:MGI.
DR   GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IMP:MGI.
DR   GO; GO:0045059; P:positive thymic T cell selection; IMP:MGI.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   GO; GO:0045577; P:regulation of B cell differentiation; IMP:MGI.
DR   GO; GO:0050855; P:regulation of B cell receptor signaling pathway; IMP:MGI.
DR   GO; GO:0042098; P:T cell proliferation; IMP:MGI.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR016335; Leukocyte_common_Ag.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PIRSF; PIRSF002004; Leukocyte_common_antigen; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00194; PTPc; 2.
DR   SUPFAM; SSF49265; FN_III-like; 2.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   2: Evidence at transcript level;
KW   Hydrolase; Protein phosphatase.
FT   NON_TER       1      1
SQ   SEQUENCE   1343 AA;  150680 MW;  0DEBDEC97FC4C6A9 CRC64;
     MGLWLKLLAF GFALLDTEVF VTGQTPTPSD ELSTTENALL LPQSDPLPAR TTESTPPSIS
     ERGNGSSETT YHPGVLSTLL PHLSPQPDSQ TPSAGGADTQ TFSSQADNPT LTPAPGGGTD
     PPGVPGERTV PGTIPADTAF PVDTPSLARN SSAASPTHTS NVSTTDISSG ASLTTLTPST
     LGLASTDPPS TTIATTTKQT CAAMFGNITV NYTYESSNQT FKADLKDVQN AKCGNEDCEN
     VLNNLEECSQ IKNISVSNDS CAPATTIDLY VPPGTDKFSL HDCTPKEKAN TSICLEWKTK
     NLDFRKCNSD NISYVLHCEP ENNTKCIRRN TFIPERCQLD NLRAQTNYTC VAEILYRGVK
     LVKNVINVQT DLGIPETPKP SCGDPAARKT LVSWPEPVSK PESASKPHGY VLCYKNNSEK
     CKSLPNNVTS FEVESLKPYK YYEVSLLAYV NGKIQRNGTA EKCNFHTKAD RPDKVNGMKT
     SRPTDNSINV TCGPPYETNG PKTFYILVVR SGGSFVTKYN KTNCQFYVDN LYYSTDYEFL
     VSFHNGVYEG DSVIRNESTN FNAKALIIFL VFLIIVTSIA LLVVLYKIYD LRKKRSSNLD
     EQQELVERDD EKQLMDVEPI HSDILLETYK RKIADEGRLF LAEFQSIPRV FSKFPIKDAR
     KPHNQNKNRY VDILPYDYNR VELSEINGDA GSTYINASYI DGFGFKEPRK YIAAQGTRAP
     GPRDETVDDF WRMIWEQKAT VIVMVTRCEE GNRNRNKCNK CAEYWPSMEE GTRAFKDIVV
     TINDHKRCPD YIIQKLNVAH AHKKKKEKAT GREVTHIQFT SWPDHGVPED PHLLLKLRRR
     VNAFSNFFSG PIVVHCSTAV LVAGVGRTGT YIGIDAMLEG LEAEGKVDVY GYVVKLRRQR
     CLMVQVEVEA QYAQYILIHQ ALVEYNQFGE TEVNLSELHS CLHNMKKRDP PSDPSPLEAE
     YQYQRLRLPS YRSWRTQHIG NQEENKKKNR NSNVVPYDFN RVPLKHELEM SKESEPESDE
     SSDDDSDSEE TSKYINASFV MSYWSYWKPE MMIAAQGPLK ETIGDFWQMI FQRKVKVIVM
     LTELVNGDQD QEVCEVCAQY WGEGKQTYGD MEVEMKDTNR ASAYTLRTFE LRHSKSKRKR
     KEPRTVYQYQ CTTWKGEELP AEPKDLVSMI QDLKQKLPKA SPEGMKYHKH ASILVHCSTA
     EMEDGSQQTG LFCALFNLLE SAETEDVVDV FQVVKSLRKA RPGVVCSYSY EQYEQYQFLY
     DIIASIYPAQ NGQVKKTNSQ DKIEFHNEVD GGKQDANCVR PDGPLNKAQE DSRGVGTPEP
     TNSAEEPEHA ANGSASPAPT QSS
//
ID   CRRY_MOUSE              Reviewed;         483 AA.
AC   Q64735; Q3TV30; Q58E68; Q61447; Q61449; Q8CF59; Q8K328;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Complement regulatory protein Crry;
DE   AltName: Full=Protein p65;
DE   Flags: Precursor;
GN   Name=Crry; Synonyms=Cry;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS
RP   1 AND 2).
RC   STRAIN=BALB/c;
RX   MEDLINE=90171600; PubMed=2307848;
RA   Paul M.S., Aegerter-Shaw M., Cepek K., Miller M.D., Weis J.H.;
RT   "The murine complement receptor gene family: III. The genomic and
RT   transcriptional complexity of the Crry and Crry-ps genes.";
RL   J. Immunol. 144:1988-1996(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 64-437 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-477 (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP   [MRNA] OF 12-167 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Liver, and Spleen;
RX   MEDLINE=89093944; PubMed=2911011;
RA   Paul M.S., Aegerter-Shaw M., O'Brien S.E., Kurtz C.B., Weis J.H.;
RT   "The murine complement receptor gene family analysis of mCRY gene
RT   products and their homology to human CR1.";
RL   J. Immunol. 142:582-589(1989).
RN   [5]
RP   FUNCTION.
RX   PubMed=1730912; DOI=10.1084/jem.175.1.121;
RA   Molina H., Wong W., Kinoshita T., Brenner C., Foley S., Holers V.M.;
RT   "Distinct receptor and regulatory properties of recombinant mouse
RT   complement receptor 1 (CR1) and Crry, the two genetic homologues of
RT   human CR1.";
RL   J. Exp. Med. 175:121-129(1992).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=7691944;
RA   Li B., Sallee C., Dehoff M., Foley S., Molina H., Holers V.M.;
RT   "Mouse Crry/p65. Characterization of monoclonal antibodies and the
RT   tissue distribution of a functional homologue of human MCP and DAF.";
RL   J. Immunol. 151:4295-4305(1993).
RN   [7]
RP   FUNCTION.
RX   MEDLINE=95105691; PubMed=7528766; DOI=10.1084/jem.181.1.151;
RA   Kim Y.-U., Kinoshita T., Molina H., Hourcade D., Seya T., Wagner L.M.,
RA   Holers V.M.;
RT   "Mouse complement regulatory protein Crry/p65 uses the specific
RT   mechanisms of both human decay-accelerating factor and membrane
RT   cofactor protein.";
RL   J. Exp. Med. 181:151-159(1995).
RN   [8]
RP   FUNCTION.
RX   PubMed=10779754;
RA   Fernandez-Centeno E., de Ojeda G., Rojo J.M., Portoles P.;
RT   "Crry/p65, a membrane complement regulatory protein, has costimulatory
RT   properties on mouse T cells.";
RL   J. Immunol. 164:4533-4542(2000).
RN   [9]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=10642554; DOI=10.1126/science.287.5452.498;
RA   Xu C., Mao D., Holers V.M., Palanca B., Cheng A.M., Molina H.;
RT   "A critical role for murine complement regulator crry in fetomaternal
RT   tolerance.";
RL   Science 287:498-501(2000).
RN   [10]
RP   FUNCTION.
RX   PubMed=11986227; DOI=10.1182/blood.V99.10.3707;
RA   Miwa T., Zhou L., Hilliard B., Molina H., Song W.-C.;
RT   "Crry, but not CD59 and DAF, is indispensable for murine erythrocyte
RT   protection in vivo from spontaneous complement attack.";
RL   Blood 99:3707-3716(2002).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [13]
RP   3D-STRUCTURE MODELING OF 84-401.
RX   PubMed=12767833; DOI=10.1016/S0022-2836(03)00492-3;
RA   Aslam M., Guthridge J.M., Hack B.K., Quigg R.J., Holers V.M.,
RA   Perkins S.J.;
RT   "The extended multidomain solution structures of the complement
RT   protein Crry and its chimeric conjugate Crry-Ig by scattering,
RT   analytical ultracentrifugation and constrained modelling: implications
RT   for function and therapy.";
RL   J. Mol. Biol. 329:525-550(2003).
CC   -!- FUNCTION: Acts as a cofactor for complement factor I, a serine
CC       protease which protects autologous cells against complement-
CC       mediated injury by cleaving C3b and C4b deposited on host tissue.
CC       Also acts as a decay-accelerating factor, preventing the formation
CC       of C4b2a and C3bBb, the amplification convertases of the
CC       complement cascade. Plays a crucial role in early embryonic
CC       development by maintaining fetomaternal tolerance. Also acts as a
CC       costimulatory factor for T-cells which favors IL-4 secretion.
CC   -!- SUBUNIT: Interacts with C3b (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q64735-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q64735-2; Sequence=VSP_019050;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed (at protein level).
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in trophoblasts at 7.5 dpc,
CC       and in the maternally derived decidual tissues until 16 dpc.
CC       Expressed only at low levels in the embryo itself.
CC   -!- DISRUPTION PHENOTYPE: Death between 9.5 and 13.5 dpc from
CC       developmental arrest.
CC   -!- SIMILARITY: Contains 5 Sushi (CCP/SCR) domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA37477.1; Type=Frameshift; Positions=200;
CC       Sequence=BAC25098.1; Type=Frameshift; Positions=152;
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DR   EMBL; M34173; AAA37467.1; -; Genomic_DNA.
DR   EMBL; M34164; AAA37467.1; JOINED; Genomic_DNA.
DR   EMBL; M34165; AAA37467.1; JOINED; Genomic_DNA.
DR   EMBL; M34166; AAA37467.1; JOINED; Genomic_DNA.
DR   EMBL; M34167; AAA37467.1; JOINED; Genomic_DNA.
DR   EMBL; M34168; AAA37467.1; JOINED; Genomic_DNA.
DR   EMBL; M34169; AAA37467.1; JOINED; Genomic_DNA.
DR   EMBL; M34170; AAA37467.1; JOINED; Genomic_DNA.
DR   EMBL; M34171; AAA37467.1; JOINED; Genomic_DNA.
DR   EMBL; M34172; AAA37467.1; JOINED; Genomic_DNA.
DR   EMBL; M34173; AAA37468.1; -; Genomic_DNA.
DR   EMBL; M34164; AAA37468.1; JOINED; Genomic_DNA.
DR   EMBL; M34165; AAA37468.1; JOINED; Genomic_DNA.
DR   EMBL; M34166; AAA37468.1; JOINED; Genomic_DNA.
DR   EMBL; M34167; AAA37468.1; JOINED; Genomic_DNA.
DR   EMBL; M34168; AAA37468.1; JOINED; Genomic_DNA.
DR   EMBL; M34169; AAA37468.1; JOINED; Genomic_DNA.
DR   EMBL; M34170; AAA37468.1; JOINED; Genomic_DNA.
DR   EMBL; M34171; AAA37468.1; JOINED; Genomic_DNA.
DR   EMBL; M34172; AAA37468.1; JOINED; Genomic_DNA.
DR   EMBL; AK004825; BAC25098.1; ALT_FRAME; mRNA.
DR   EMBL; AK160440; BAE35790.1; -; mRNA.
DR   EMBL; BC028945; AAH28945.1; -; mRNA.
DR   EMBL; BC092048; AAH92048.1; -; mRNA.
DR   EMBL; M23529; AAA37477.1; ALT_FRAME; mRNA.
DR   EMBL; M23446; AAA37478.1; -; mRNA.
DR   IPI; IPI00138061; -.
DR   IPI; IPI00169975; -.
DR   PIR; A43519; A43519.
DR   PIR; B30550; B30550.
DR   PIR; I55975; I55975.
DR   RefSeq; NP_038527.2; NM_013499.2.
DR   UniGene; Mm.301652; -.
DR   PDB; 1NTL; X-ray; -; A/B=84-401.
DR   PDBsum; 1NTL; -.
DR   ProteinModelPortal; Q64735; -.
DR   SMR; Q64735; 37-464.
DR   STRING; Q64735; -.
DR   PhosphoSite; Q64735; -.
DR   PRIDE; Q64735; -.
DR   Ensembl; ENSMUST00000027918; ENSMUSP00000027918; ENSMUSG00000016481.
DR   Ensembl; ENSMUST00000075451; ENSMUSP00000074902; ENSMUSG00000016481.
DR   GeneID; 12946; -.
DR   KEGG; mmu:12946; -.
DR   UCSC; uc007eev.1; mouse.
DR   CTD; 12946; -.
DR   MGI; MGI:88513; Crry.
DR   eggNOG; maNOG10884; -.
DR   GeneTree; ENSGT00600000084351; -.
DR   HOVERGEN; HBG081346; -.
DR   InParanoid; Q64735; -.
DR   OrthoDB; EOG45QHDS; -.
DR   NextBio; 282646; -.
DR   ArrayExpress; Q64735; -.
DR   Bgee; Q64735; -.
DR   CleanEx; MM_CR1L; -.
DR   Genevestigator; Q64735; -.
DR   GermOnline; ENSMUSG00000016481; Mus musculus.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR   GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR   GO; GO:0007565; P:female pregnancy; IEA:UniProtKB-KW.
DR   GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0045916; P:negative regulation of complement activation; IMP:MGI.
DR   InterPro; IPR016060; Complement_control_module.
DR   InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR   InterPro; IPR000436; Sushi_SCR_CCP.
DR   Gene3D; G3DSA:2.10.70.10; Complement_control_module; 5.
DR   Gene3D; G3DSA:1.10.287.90; COX2_TM; 1.
DR   Pfam; PF00084; Sushi; 5.
DR   SMART; SM00032; CCP; 5.
DR   SUPFAM; SSF57535; Complement_control_module; 5.
DR   PROSITE; PS50923; SUSHI; 5.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Complement pathway;
KW   Developmental protein; Disulfide bond; Glycoprotein; Immunity;
KW   Innate immunity; Membrane; Phosphoprotein; Pregnancy; Receptor;
KW   Repeat; Signal; Sushi; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     40       Potential.
FT   CHAIN        41    483       Complement regulatory protein Crry.
FT                                /FTId=PRO_0000238978.
FT   TOPO_DOM     41    405       Extracellular (Potential).
FT   TRANSMEM    406    426       Helical; (Potential).
FT   TOPO_DOM    427    483       Cytoplasmic (Potential).
FT   DOMAIN       83    143       Sushi 1.
FT   DOMAIN      144    205       Sushi 2.
FT   DOMAIN      206    276       Sushi 3.
FT   DOMAIN      278    338       Sushi 4.
FT   DOMAIN      340    400       Sushi 5.
FT   MOD_RES     460    460       Phosphoserine.
FT   MOD_RES     477    477       Phosphoserine.
FT   CARBOHYD     98     98       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    366    366       N-linked (GlcNAc...) (Potential).
FT   DISULFID     85    128       By similarity.
FT   DISULFID    115    141       By similarity.
FT   DISULFID    146    187       By similarity.
FT   DISULFID    173    203       By similarity.
FT   DISULFID    208    257       By similarity.
FT   DISULFID    237    274       By similarity.
FT   DISULFID    280    323       By similarity.
FT   DISULFID    309    336       By similarity.
FT   DISULFID    342    385       By similarity.
FT   DISULFID    371    398       By similarity.
FT   VAR_SEQ      40     82       Missing (in isoform 2).
FT                                /FTId=VSP_019050.
FT   CONFLICT     21     21       G -> A (in Ref. 4; AAA37477).
FT   CONFLICT     28     28       E -> A (in Ref. 3; AAH92048).
FT   CONFLICT     64     67       ADSK -> GRLQ (in Ref. 2; BAE35790).
FT   CONFLICT    112    112       L -> M (in Ref. 3; AAH92048).
FT   CONFLICT    164    164       Q -> E (in Ref. 4; AAA37477).
FT   CONFLICT    182    182       S -> P (in Ref. 3; AAH92048).
FT   CONFLICT    240    240       D -> N (in Ref. 3; AAH92048).
FT   CONFLICT    435    437       NTT -> TRF (in Ref. 2; BAE35790).
SQ   SEQUENCE   483 AA;  53763 MW;  259BFFED4CE547C1 CRC64;
     MEVSSRSSEP LDPVWLLVAF GRGGVKLEVL LLFLLPFTLG ELRGGLGKHG HTVHREPAVN
     RLCADSKRWS GLPVSAQRPF PMGHCPAPSQ LPSAKPINLT DESMFPIGTY LLYECLPGYI
     KRQFSITCKQ DSTWTSAEDK CIRKQCKTPS DPENGLVHVH TGIQFGSRIN YTCNQGYRLI
     GSSSAVCVIT DQSVDWDTEA PICEWIPCEI PPGIPNGDFF SSTREDFHYG MVVTYRCNTD
     ARGKALFNLV GEPSLYCTSN DGEIGVWSGP PPQCIELNKC TPPPYVENAV MLSENRSLFS
     LRDIVEFRCH PGFIMKGASS VHCQSLNKWE PELPSCFKGV ICRLPQEMSG FQKGLGMKKE
     YYYGENVTLE CEDGYTLEGS SQSQCQSDGS WNPLLAKCVS RSISGLIVGI FIGIIVFILV
     IIVFIWMILK YKKRNTTDEK YKEVGIHLNY KEDSCVRLQS LLTSQENSST TSPARNSLTQ
     EVS
//
ID   CTNA3_MOUSE             Reviewed;         895 AA.
AC   Q65CL1; Q3UQ61; Q8C0N3;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 2.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Catenin alpha-3;
DE   AltName: Full=Alpha T-catenin;
DE   AltName: Full=Cadherin-associated protein;
GN   Name=Ctnna3; Synonyms=Catna3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RX   MEDLINE=22483630; PubMed=12596047; DOI=10.1007/s00439-002-0857-5;
RA   Janssens B., Mohapatra B., Vatta M., Goossens S., Vanpoucke G.,
RA   Kools P., Montoye T., van Hengel J., Bowles N.E., van Roy F.,
RA   Towbin J.A.;
RT   "Assessment of the CTNNA3 gene encoding human alpha T-catenin
RT   regarding its involvement in dilated cardiomyopathy.";
RL   Hum. Genet. 112:227-236(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   INTERACTION WITH CTNNB1.
RX   MEDLINE=21474377; PubMed=11590244;
RA   Janssens B., Goossens S., Staes K., Gilbert B., van Hengel J.,
RA   Colpaert C., Bruyneel E., Mareel M., van Roy F.;
RT   "AlphaT-catenin: a novel tissue-specific beta-catenin-binding protein
RT   mediating strong cell-cell adhesion.";
RL   J. Cell Sci. 114:3177-3188(2001).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
CC   -!- FUNCTION: May be involved in formation of stretch-resistant cell-
CC       cell adhesion complexes (By similarity).
CC   -!- SUBUNIT: Interacts with CTNNB1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Note=Localizes to intercalated disks of cardiomyocytes and in
CC       peritubular myoid cells of testis, and colocalizes with CTNNA1 and
CC       CTNNA2 (By similarity).
CC   -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
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DR   EMBL; AF344871; AAQ14965.1; -; mRNA.
DR   EMBL; AK030166; BAC26817.1; -; mRNA.
DR   EMBL; AK142745; BAE25182.1; -; mRNA.
DR   IPI; IPI00223882; -.
DR   RefSeq; NP_001157848.1; NM_001164376.1.
DR   RefSeq; NP_808280.2; NM_177612.3.
DR   UniGene; Mm.444682; -.
DR   UniGene; Mm.444692; -.
DR   ProteinModelPortal; Q65CL1; -.
DR   SMR; Q65CL1; 54-258, 372-626.
DR   STRING; Q65CL1; -.
DR   PhosphoSite; Q65CL1; -.
DR   PRIDE; Q65CL1; -.
DR   Ensembl; ENSMUST00000075099; ENSMUSP00000074606; ENSMUSG00000060843.
DR   Ensembl; ENSMUST00000105440; ENSMUSP00000101080; ENSMUSG00000060843.
DR   Ensembl; ENSMUST00000105441; ENSMUSP00000101081; ENSMUSG00000060843.
DR   GeneID; 216033; -.
DR   KEGG; mmu:216033; -.
DR   UCSC; uc007fkh.1; mouse.
DR   CTD; 216033; -.
DR   MGI; MGI:2661445; Ctnna3.
DR   GeneTree; ENSGT00550000074411; -.
DR   HOGENOM; HBG356872; -.
DR   HOVERGEN; HBG000069; -.
DR   InParanoid; Q65CL1; -.
DR   OMA; NAGKKER; -.
DR   OrthoDB; EOG4P8FHC; -.
DR   PhylomeDB; Q65CL1; -.
DR   NextBio; 374961; -.
DR   ArrayExpress; Q65CL1; -.
DR   Bgee; Q65CL1; -.
DR   CleanEx; MM_CTNNA3; -.
DR   Genevestigator; Q65CL1; -.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005916; C:fascia adherens; ISS:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0045296; F:cadherin binding; TAS:UniProtKB.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0016337; P:cell-cell adhesion; IPI:UniProtKB.
DR   InterPro; IPR001033; Alpha_catenin.
DR   InterPro; IPR006077; Vinculin/catenin.
DR   Pfam; PF01044; Vinculin; 2.
DR   PRINTS; PR00805; ALPHACATENIN.
DR   SUPFAM; SSF47220; Vinculin/catenin; 4.
DR   PROSITE; PS00663; VINCULIN_1; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Cell adhesion; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein.
FT   CHAIN         1    895       Catenin alpha-3.
FT                                /FTId=PRO_0000064267.
FT   COILED       74    107       Potential.
FT   COILED      325    379       Potential.
FT   MOD_RES     637    637       Phosphoserine.
FT   MOD_RES     867    867       Phosphothreonine (By similarity).
FT   CONFLICT    439    439       E -> K (in Ref. 2; BAC26817).
FT   CONFLICT    838    838       S -> C (in Ref. 2; BAC26817).
FT   CONFLICT    869    869       A -> V (in Ref. 2; BAC26817).
FT   CONFLICT    871    871       V -> A (in Ref. 1; AAQ14965).
SQ   SEQUENCE   895 AA;  99803 MW;  82355DA239D17A6A CRC64;
     MSAETPITLN MDTQDLQIQT FTVEKLLEPL IIQVTTLVNC PQNPSNRKKG RSKRARVLLA
     SVEEATWNLL DKGEMIAKEA TVLKEELAAA LQEVRKESKA LKVSAERFTD DPCYLPKREA
     VVQAARALLA AVTRLLVLAD MIDVMCLLQH VSSFQRTFES LKNVSNKSDL QRTYQKLGKE
     LESLDYLAFK RQQDLKSPSQ RDEIAGARAT LKENSPLLHS ICSACLEHSD VASLKASKDT
     VCEEIQNALD VISNASQGIQ NAPAPPEPQA ATLGSAFDEL ENLIVLNPLT VTEEDVRPSL
     EKRLEAIISG AALLADSSCT RDLHRERIIA ECNAIRQALQ DLLTEYMSNT GKTERSNTLN
     TAIVNMSKKT RDLRRQLRKA IIDHISDSFL DTTVPLLVLI EAAKNGRVKE IKDYAAIFHE
     HTGRLVEVAN LACSMSTNED GIKIVRIAAN HLETLCPQII NAALALASRP KSQVVKNTME
     MYKRTWEHYI HVLTEAVDDI TSIDDFLAVS ESHILEDVNK CIIALRDQDA DNLDRAAGAI
     RGRAARVAHI VAGEMDSYEP GAYTEGVMRN VNFLTSTVIP EFVTQVNVAL DALSKNSLTA
     LDDNQFVDIS KKIYDTIHDI RCSVMMIRTP EELEDVSDLE DDHEVRSHTS IQTEGKTDRA
     KMTQLPEAEK EKIAEQVADF KKVKSKLDAE IEIWDDTSND IIVLAKKMCM IMMEMTDFTR
     GKGPLKHTTD VIYAAKMISE SGSRMDVLAR QIANQCPDPP CKQDLLAYLE QIKFYSHQLK
     ICSQVKAEIQ NLGGELIVSA LDSVTSLIQA AKNLMNAVVQ TVKMSYIAST KIIRIQSSAG
     PRHPVVMWRM KAPAKKPLIK REKPEETWAA VRRGSAKKKI HPVQVMSEFR GRQVY
//
ID   WAPL_MOUSE              Reviewed;        1200 AA.
AC   Q65Z40; Q6ZQE9;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Wings apart-like protein homolog;
DE   AltName: Full=Dioxin-inducible factor 2;
DE            Short=DIF-2;
GN   Name=Wapal; Synonyms=Kiaa0261, Wapl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=15620708; DOI=10.1016/j.febslet.2004.11.070;
RA   Kuroda M., Oikawa K., Ohbayashi T., Yoshida K., Yamada K., Mimura J.,
RA   Matsuda Y., Fujii-Kuriyama Y., Mukai K.;
RT   "A dioxin sensitive gene, mammalian WAPL, is implicated in
RT   spermatogenesis.";
RL   FEBS Lett. 579:167-172(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   INTERACTION WITH THE COHESIN COMPLEX.
RX   PubMed=17113138; DOI=10.1016/j.cell.2006.09.040;
RA   Kueng S., Hegemann B., Peters B.H., Lipp J.J., Schleiffer A.,
RA   Mechtler K., Peters J.M.;
RT   "Wapl controls the dynamic association of cohesin with chromatin.";
RL   Cell 127:955-967(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468 AND SER-470, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468 AND SER-470, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Regulator of sister chromatid cohesion in mitosis which
CC       negatively regulates cohesin association with chromatin. Involved
CC       in both sister chromatid cohesion during interphase and sister-
CC       chromatid resolution during early stages of mitosis. Couples DNA
CC       replication to sister chromatid cohesion. Cohesion ensures that
CC       chromosome partitioning is accurate in both meiotic and mitotic
CC       cells and plays an important role in DNA repair (By similarity).
CC   -!- SUBUNIT: Interacts with the cohesin complex throughout the cell
CC       cycle; interacts with both chromatin-bound and soluble pools of
CC       the complex. Interacts with RAD21; the interaction is direct (By
CC       similarity). Interacts with PDS5A; the interaction is direct,
CC       cohesin-dependent and competitive with SORORIN (By similarity).
CC       Interacts (via FGF motifs) with PDS5B; the interaction is direct
CC       (By similarity). Interacts with SMC3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Chromosome (By
CC       similarity). Cytoplasm (By similarity). Note=Associates with
CC       chromatin through the cohesin complex during interphase. Released
CC       in the cytoplasm from nuclear envelope breakdown until anaphase,
CC       it reaccumulates in nucleus at telophase (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in large pachytene
CC       spermatocytes of testis. Down-regulated by dioxin in testis.
CC   -!- SIMILARITY: Contains 1 WAPL domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97915.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; AB167349; BAD44717.1; -; mRNA.
DR   EMBL; AK129105; BAC97915.1; ALT_INIT; mRNA.
DR   IPI; IPI00420597; -.
DR   UniGene; Mm.27957; -.
DR   ProteinModelPortal; Q65Z40; -.
DR   STRING; Q65Z40; -.
DR   PhosphoSite; Q65Z40; -.
DR   PRIDE; Q65Z40; -.
DR   Ensembl; ENSMUST00000048263; ENSMUSP00000040232; ENSMUSG00000041408.
DR   UCSC; uc007tbi.1; mouse.
DR   MGI; MGI:2675859; Wapal.
DR   eggNOG; roNOG07039; -.
DR   GeneTree; ENSGT00390000015768; -.
DR   HOGENOM; HBG715168; -.
DR   HOVERGEN; HBG088338; -.
DR   InParanoid; Q65Z40; -.
DR   OrthoDB; EOG4TXBR6; -.
DR   ArrayExpress; Q65Z40; -.
DR   Bgee; Q65Z40; -.
DR   CleanEx; MM_WAPAL; -.
DR   Genevestigator; Q65Z40; -.
DR   GermOnline; ENSMUSG00000041408; Mus musculus.
DR   GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR   GO; GO:0008278; C:cohesin complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0000795; C:synaptonemal complex; IDA:MGI.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0035562; P:negative regulation of chromatin binding; ISS:UniProtKB.
DR   GO; GO:0008156; P:negative regulation of DNA replication; ISS:UniProtKB.
DR   GO; GO:0045875; P:negative regulation of sister chromatid cohesion; ISS:UniProtKB.
DR   GO; GO:0071168; P:protein localization to chromatin; ISS:UniProtKB.
DR   GO; GO:0071922; P:regulation of cohesin localization to chromatin; ISS:UniProtKB.
DR   GO; GO:0009636; P:response to toxin; IDA:MGI.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR012502; WAPL_metazoan_plants.
DR   InterPro; IPR022771; WAPL_prot.
DR   Pfam; PF07814; WAPL; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS51271; WAPL; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell cycle; Cell division; Chromosome; Coiled coil;
KW   Cytoplasm; Mitosis; Nucleus; Phosphoprotein.
FT   CHAIN         1   1200       Wings apart-like protein homolog.
FT                                /FTId=PRO_0000245233.
FT   DOMAIN      635   1179       WAPL.
FT   REGION        1    668       Mediates interaction with the cohesin
FT                                complex (By similarity).
FT   COILED      266    293       Potential.
FT   COILED      751    791       Potential.
FT   MOTIF        73     75       FGF motif 1.
FT   MOTIF       437    439       FGF motif 2.
FT   MOTIF       462    464       FGF motif 3.
FT   MOD_RES      77     77       Phosphoserine.
FT   MOD_RES     168    168       N6-acetyllysine (By similarity).
FT   MOD_RES     226    226       Phosphoserine.
FT   MOD_RES     228    228       Phosphoserine (By similarity).
FT   MOD_RES     388    388       Phosphoserine (By similarity).
FT   MOD_RES     468    468       Phosphoserine.
FT   MOD_RES     470    470       Phosphoserine.
FT   MOD_RES     914    914       Phosphoserine (By similarity).
FT   CONFLICT    757    757       V -> L (in Ref. 2; BAC97915).
SQ   SEQUENCE   1200 AA;  134056 MW;  0300A9455758013E CRC64;
     MTSRFGKTYS RKGGNGSSKF DEVFSNKRTT LSTKWGETTF MAKLGQKRPN FKPDIQEIPK
     KPKVEEEDTG DPFGFDSDDE SLPVSSKNLA QGKGSSYSES SEAAQLEEVT SVFEANSKCS
     HVVGEDSFAS DRCLLVEDTL IGKEKSISRI PEDNANKSSC TKLLTSDKVE NFSEEHEKNS
     HHFHKNAEDS TKKPNAETAV ASEYKADETK ETNDTWNSQS GKRTESPSES CPVKGSVRTG
     LYEWDNDFED IRSEDCILSL DNESLLEMKD EDLKNRIGGL ENLNETFEED IIQSVLRPSN
     CRTYCRANKA RSSQGASNFD KLMDGTSQSL AKANSESSKD GLNQAKKGSA SCGTSFRGTV
     GRTRDYTVLH PSCLSVCNVT IQDTMERSMD EFTASTPADL GEAGRLRKKA DIATSKTTTR
     FRPSNTKSKK DVKLEFFGFE DHDETGGDEG GSGSSNYKIK YFGFDDLSES EDDDDDDCQV
     ERKKDKKRTK TAPSPSQQPP PESSDNSQDS QSSTNNAENL DFTEDLPGVP ESVKKPISKQ
     GDKSKENTRK IFSGPKRSPT KAVYNARHWN HPDSEELPGP PIAKPQRVTV RLSSKEPNQK
     DDGVFKAPAP PLKVIKTVTI PTQPYQEIVT ALKCRKEDKE LYTVVQHVKH FNDVVEFGEN
     QEFTDDIEYL LSGLKSTQPL NTRCLSVISL ATKCAMPSFR MHLRAHGMVA MVFKTLDDSQ
     HHQNLSLCTA ALMYILSRDR LNMDLDRASL DLMIRLVELE QDASSAKLLN EKDMNKIKEK
     IRRLCETVHN KHLDLENITT GHLAMETLLS LTSKRAGDWF KEELRLLGGL DHIVDKVKEC
     VDHLSRDDED EEKLVASLWG AERCLRVLES VTVHNPENQS YLIAYKDSQL IISSAKALQH
     CEDLIQQYNR AENSICVADS NPLPYQNVTN HVGKAVEDCM RAIIGVLLNL TNDNEWGSTK
     TGEQEGLIGT AMNCVLQVPK YLPQEQRFDI RVLGLGLLIN LVEYSARNRH CLVNMQTSCS
     FDSSFSSGEG DHSLRLAGQV HAVQALVQLF LERERAAQLA ESKTDELIKD APTTQHDKSG
     EWQETSGEIQ WVSTEKTDGA EEKQKKEEED EELDLNKALQ HAGKHMEDCI VASYTALLLG
     CLCQESPINV TTVREYLPEG DFSIMTEMLK KFLSFMNLTC AVGTTGQKSI SRVIEYLEHC
//
ID   Q66JR8_MOUSE            Unreviewed;       211 AA.
AC   Q66JR8;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   08-FEB-2011, entry version 52.
DE   SubName: Full=Ptms protein;
GN   Name=Ptms;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor. C3;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC080800; AAH80800.1; -; mRNA.
DR   IPI; IPI00471441; -.
DR   UniGene; Mm.142187; -.
DR   ProteinModelPortal; Q66JR8; -.
DR   SMR; Q66JR8; 15-77.
DR   STRING; Q66JR8; -.
DR   PRIDE; Q66JR8; -.
DR   Ensembl; ENSMUST00000112444; ENSMUSP00000108063; ENSMUSG00000030122.
DR   MGI; MGI:1916452; Ptms.
DR   eggNOG; maNOG21688; -.
DR   GeneTree; ENSGT00410000025588; -.
DR   InParanoid; Q66JR8; -.
DR   ArrayExpress; Q66JR8; -.
DR   Bgee; Q66JR8; -.
DR   Genevestigator; Q66JR8; -.
DR   GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro.
DR   GO; GO:0008612; P:peptidyl-lysine modification to hypusine; IEA:InterPro.
DR   GO; GO:0045901; P:positive regulation of translational elongation; IEA:InterPro.
DR   GO; GO:0045905; P:positive regulation of translational termination; IEA:InterPro.
DR   GO; GO:0006452; P:translational frameshifting; IEA:InterPro.
DR   InterPro; IPR005824; KOW.
DR   InterPro; IPR004931; Pro/parathymosin.
DR   InterPro; IPR019769; Trans_elong_IF5A_hypusine_site.
DR   InterPro; IPR001884; Transl_elong_IF5A.
DR   InterPro; IPR014722; Transl_SH3-like_sub.
DR   InterPro; IPR008991; Translation_prot_SH3-like.
DR   Gene3D; G3DSA:2.30.30.30; Ribosomal_L2; 1.
DR   PANTHER; PTHR11673; EIF5A_hypusine; 1.
DR   Pfam; PF00467; KOW; 1.
DR   Pfam; PF03247; Prothymosin; 1.
DR   SUPFAM; SSF50104; Transl_SH3_like; 1.
DR   TIGRFAMs; TIGR00037; eIF_5A; 1.
DR   PROSITE; PS00302; IF5A_HYPUSINE; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   211 AA;  23158 MW;  3578A577F4667ECC CRC64;
     MADDLDFETG DAGASATFPM QCSALRKNGF VVLKGRPCKI VEMSTSKTGK HGHAKVHLVG
     IDIFTGKKYE DICRRRHRAK FRPRPPSAVQ GSSASAPGPR LPASPGPGTM SEKSVEAAAE
     LSAKDLKEKK DKVEEKAGRK ERKKEVVEEE ENGAEEEEEE TAEDGEDDDE GDEEDEEEEE
     EEDEGPVRKR TAEEEDEADP KRQKTENGAS A
//
ID   EIF3J_MOUSE             Reviewed;         263 AA.
AC   Q66JS6; Q8BUW6;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit J;
DE            Short=eIF3j;
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 1;
DE   AltName: Full=eIF-3-alpha;
DE   AltName: Full=eIF3 p35;
GN   Name=Eif3j; Synonyms=Eif3s1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 42-263.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Component of the eukaryotic translation initiation
CC       factor 3 (eIF-3) complex, which is required for several steps in
CC       the initiation of protein synthesis. The eIF-3 complex associates
CC       with the 40S ribosome and facilitates the recruitment of eIF-1,
CC       eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S
CC       preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA
CC       recruitment to the 43S PIC and scanning of the mRNA for AUG
CC       recognition. The eIF-3 complex is also required for disassembly
CC       and recycling of posttermination ribosomal complexes and
CC       subsequently prevents premature joining of the 40S and 60S
CC       ribosomal subunits prior to initiation. This subunit binds
CC       directly within the mRNA entry channel of the 40S ribosome to the
CC       aminoacyl (A) site. It may regulate the interaction between the
CC       43S PIC and mRNA (By similarity).
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor
CC       3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B,
CC       EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K,
CC       EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable
CC       modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I;
CC       module B is composed of EIF3F, EIF3H, and EIF3M; and module C is
CC       composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module
CC       C binds EIF3B of module A and EIF3H of module B, thereby linking
CC       the three modules. EIF3J is a labile subunit that binds to the
CC       eIF-3 complex via EIF3B. The eIF-3 complex interacts with RPS6KB1
CC       under conditions of nutrient depletion. Mitogenic stimulation
CC       leads to binding and activation of a complex composed of MTOR and
CC       RPTOR, leading to phosphorylation and release of RPS6KB1 and
CC       binding of EIF4B to eIF-3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
CC       stimulation (By similarity).
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit J family.
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DR   EMBL; BC080788; AAH80788.1; -; mRNA.
DR   EMBL; AK082048; BAC38399.1; -; mRNA.
DR   IPI; IPI00471443; -.
DR   RefSeq; XP_001479331.1; XM_001479281.2.
DR   RefSeq; XP_003086318.1; XM_003086270.1.
DR   UniGene; Mm.458184; -.
DR   ProteinModelPortal; Q66JS6; -.
DR   SMR; Q66JS6; 147-216.
DR   STRING; Q66JS6; -.
DR   PhosphoSite; Q66JS6; -.
DR   PRIDE; Q66JS6; -.
DR   Ensembl; ENSMUST00000057110; ENSMUSP00000054421; ENSMUSG00000043424.
DR   GeneID; 100042807; -.
DR   KEGG; mmu:100042807; -.
DR   MGI; MGI:1925905; Eif3j.
DR   HOGENOM; HBG282796; -.
DR   HOVERGEN; HBG066230; -.
DR   InParanoid; Q66JS6; -.
DR   OMA; RWESEDE; -.
DR   OrthoDB; EOG4ZPDWV; -.
DR   NextBio; 454728; -.
DR   ArrayExpress; Q66JS6; -.
DR   Genevestigator; Q66JS6; -.
DR   GermOnline; ENSMUSG00000043424; Mus musculus.
DR   GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; ISS:UniProtKB.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR023194; eIF3-like_dom.
DR   InterPro; IPR013906; eIF3_subunit.
DR   PANTHER; PTHR21681; eIF3_subunit; 1.
DR   Pfam; PF08597; eIF3_subunit; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Coiled coil; Cytoplasm; Initiation factor;
KW   Phosphoprotein; Protein biosynthesis.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    263       Eukaryotic translation initiation factor
FT                                3 subunit J.
FT                                /FTId=PRO_0000123507.
FT   REGION        6     74       Sufficient for interaction with EIF3B (By
FT                                similarity).
FT   REGION      248    263       Promotes stable association with the 40S
FT                                ribosome (By similarity).
FT   COILED       75    140       Potential.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      16     16       Phosphoserine (By similarity).
FT   MOD_RES      18     18       Phosphoserine (By similarity).
FT   MOD_RES      25     25       Phosphoserine (By similarity).
FT   MOD_RES     114    114       Phosphothreonine (By similarity).
FT   MOD_RES     132    132       Phosphoserine (By similarity).
FT   MOD_RES     259    259       Phosphotyrosine (By similarity).
FT   CONFLICT    191    191       D -> N (in Ref. 2; BAC38399).
SQ   SEQUENCE   263 AA;  29486 MW;  7040416E40650960 CRC64;
     MAAAAAAAAA AAAGDSDSWD ADTFSMEDPV RKVAGGGTAG GDRWEGEDED EDVKDNWDDD
     DDENKEEAEV KPEVKISEKK KIAEKIKEKE RQQKKRQEEI KKRLEEPEES KVLTPEEQLA
     DKLRLKKLQE ESDLELAKET FGVNNTVYGI DAMNPSSRDD FTEFGKLLKD KITQYEKSLY
     YASFLEALVR DVCISLEIDD LKKITNSLTV LCSEKQKQEK QSKAKKKKKG VVPGGGLKAT
     MKDDLADYGG YEGGYVQDYE DFM
//
ID   M3K10_MOUSE             Reviewed;         940 AA.
AC   Q66L42; Q80UW4;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Mitogen-activated protein kinase kinase kinase 10;
DE            EC=2.7.11.25;
GN   Name=Map3k10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-940.
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Activates the JUN N-terminal pathway (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Homodimerization via the leucine zipper domains
CC       is required for autophosphorylation and subsequent activation (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- PTM: Autophosphorylation on serine and threonine residues within
CC       the activation loop plays a role in enzyme activation (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AC074312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC046514; AAH46514.1; -; mRNA.
DR   EMBL; BC078445; AAH78445.1; -; mRNA.
DR   IPI; IPI00672525; -.
DR   UniGene; Mm.389883; -.
DR   HSSP; O43318; 2EVA.
DR   ProteinModelPortal; Q66L42; -.
DR   SMR; Q66L42; 13-361, 415-473.
DR   STRING; Q66L42; -.
DR   PhosphoSite; Q66L42; -.
DR   PRIDE; Q66L42; -.
DR   Ensembl; ENSMUST00000036453; ENSMUSP00000037725; ENSMUSG00000040390.
DR   MGI; MGI:1346879; Map3k10.
DR   eggNOG; roNOG10743; -.
DR   GeneTree; ENSGT00600000084346; -.
DR   HOVERGEN; HBG067662; -.
DR   OrthoDB; EOG4NCMC3; -.
DR   PhylomeDB; Q66L42; -.
DR   BRENDA; 2.7.11.25; 244.
DR   ArrayExpress; Q66L42; -.
DR   Bgee; Q66L42; -.
DR   CleanEx; MM_MAP3K10; -.
DR   Genevestigator; Q66L42; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:EC.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR015785; MAPKKK-like.
DR   InterPro; IPR016231; MAPKKK9/10/11.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR23257:SF87; MAPKKK-like; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   PIRSF; PIRSF000556; MAPKKK9_11; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; Repeat;
KW   Serine/threonine-protein kinase; SH3 domain; Transferase.
FT   CHAIN         1    940       Mitogen-activated protein kinase kinase
FT                                kinase 10.
FT                                /FTId=PRO_0000277826.
FT   DOMAIN       16     81       SH3.
FT   DOMAIN       98    360       Protein kinase.
FT   DOMAIN      384    405       Leucine-zipper 1.
FT   DOMAIN      419    440       Leucine-zipper 2.
FT   NP_BIND     104    112       ATP (By similarity).
FT   COMPBIAS    763    915       Pro-rich.
FT   ACT_SITE    222    222       Proton acceptor (By similarity).
FT   BINDING     125    125       ATP (By similarity).
FT   MOD_RES     258    258       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     262    262       Phosphoserine; by autocatalysis and
FT                                MAP4K1 (By similarity).
FT   MOD_RES     489    489       Phosphoserine (By similarity).
FT   MOD_RES     498    498       Phosphoserine (By similarity).
FT   MOD_RES     502    502       Phosphoserine (By similarity).
FT   MOD_RES     506    506       Phosphoserine (By similarity).
FT   MOD_RES     508    508       Phosphoserine (By similarity).
FT   MOD_RES     552    552       Phosphothreonine (By similarity).
FT   MOD_RES     582    582       Phosphoserine (By similarity).
FT   MOD_RES     583    583       Phosphoserine (By similarity).
FT   MOD_RES     816    816       Phosphothreonine (By similarity).
FT   MOD_RES     818    818       Phosphoserine (By similarity).
FT   CONFLICT    350    353       FGSI -> PTRP (in Ref. 2; AAH46514).
SQ   SEQUENCE   940 AA;  103187 MW;  BE27F39679DC63D0 CRC64;
     MEEEEGAAAR EWGATPAGPV WTAVFDYEAV GDEELTLRRG DRVQVLSQDC AVSGDEGWWT
     GQLPSGRVGV FPSNYVAPAA PAAPSDLQLP QEIPFHELQL EEIIGVGGFG KVYRAVWRGE
     EVAVKAARLD PERDPAVTAE QVRQEARLFG ALQHPNIIAL RGACLSPPNL CLVMEYARGG
     ALSRVLAGRR VPPHVLVNWA VQVARGMNYL HNDAPVPIIH RDLKSINILI LEAIENHNLA
     DTVLKITDFG LAREWHKTTK MSAAGTYAWM APEVIRLSLF SKSSDVWSFG VLLWELLTGE
     VPYREIDALA VAYGVAMNKL TLPIPSTCPE PFARLLEECW DPDPHGRPDF GSILKQLEVI
     EQSALFQMPL ESFHSLQEDW KLEIQHMFDD LRTKEKELRS REEELLRAAQ EQRFQEEQLR
     RREQELAERE MDIVERELHL LMSQLSQEKP RVRKRKGNFK RSRLLKLREG SSHISLPSGF
     EHKITVQASP TLDKRKGSDG ASPPASPSII PRLRAIRLTP MDCGGSSGSG TWSRSGPPKK
     EELVGGKKKG RTWGPSSTLQ KERAGGEERL KALGEGSKQW SSSAPNLGKS PKHTPMAPGF
     ASLNEMEEFA EADEGNNVPP SPYSTPSYLK VPLPAEPSPC VQAPWEPPAV TPSRPGHGAR
     RRCDLALLSC ATLLSAVGLG ADVAEARAGD GEEQRRWLDS LFFPRPGRFP RGLSPTGRPG
     GRREDTAPGL GLAPSATLVS LSSVSDCNST RSLLRSDSDE AAPAAPSPPP SPLAPSPSTN
     PLVDVELESF KKDPRQSLTP THVTAAHAVS RGHRRTPSDG ALRQREPLEL TNHGPRDPLD
     FPRLPDPQAL FPTRRRPLEF PGRPTTLTFA PRPRPAASRP RLDPWKLVSF GRTLSISPPS
     RPDTPESPGP PSVQPTLLDM DMEGQSQDNT VPLCGVYGSH
//
ID   DOS_MOUSE               Reviewed;         705 AA.
AC   Q66L44; Q497H6; Q8CBL1;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 3.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Protein Dos;
DE   AltName: Full=Downstream of Stk11 protein;
GN   Name=Dos;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 289-705.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297; SER-485 AND
RP   SER-527, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI00553.1; Type=Frameshift; Positions=256;
CC       Sequence=BC052075; Type=Miscellaneous discrepancy; Note=Contains sequencing errors;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC052075; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC078442; AAH78442.1; -; mRNA.
DR   EMBL; BC100552; AAI00553.1; ALT_FRAME; mRNA.
DR   EMBL; AK035824; BAC29200.1; -; mRNA.
DR   IPI; IPI00828271; -.
DR   RefSeq; NP_001182197.1; NM_001195268.1.
DR   RefSeq; XP_003084915.1; XM_003084867.1.
DR   RefSeq; XP_003084916.1; XM_003084868.1.
DR   RefSeq; XP_003084917.1; XM_003084869.1.
DR   RefSeq; XP_003084918.1; XM_003084870.1.
DR   RefSeq; XP_003084920.1; XM_003084872.1.
DR   RefSeq; XP_003085753.1; XM_003085705.1.
DR   RefSeq; XP_003085754.1; XM_003085706.1.
DR   RefSeq; XP_003085755.1; XM_003085707.1.
DR   RefSeq; XP_003085756.1; XM_003085708.1.
DR   RefSeq; XP_003085758.1; XM_003085710.1.
DR   UniGene; Mm.44231; -.
DR   STRING; Q66L44; -.
DR   PhosphoSite; Q66L44; -.
DR   PRIDE; Q66L44; -.
DR   Ensembl; ENSMUST00000105368; ENSMUSP00000101007; ENSMUSG00000090156.
DR   Ensembl; ENSMUST00000105369; ENSMUSP00000101008; ENSMUSG00000035640.
DR   GeneID; 100503659; -.
DR   GeneID; 216164; -.
DR   KEGG; mmu:100503659; -.
DR   KEGG; mmu:216164; -.
DR   UCSC; uc007gbw.1; mouse.
DR   CTD; 216164; -.
DR   MGI; MGI:1354170; Dos.
DR   eggNOG; roNOG05672; -.
DR   GeneTree; ENSGT00390000009230; -.
DR   HOGENOM; HBG713984; -.
DR   HOVERGEN; HBG081461; -.
DR   InParanoid; Q66L44; -.
DR   OrthoDB; EOG4X97H8; -.
DR   NextBio; 375036; -.
DR   ArrayExpress; Q66L44; -.
DR   Bgee; Q66L44; -.
DR   CleanEx; MM_DOS; -.
DR   Genevestigator; Q66L44; -.
DR   GermOnline; ENSMUSG00000035640; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    705       Protein Dos.
FT                                /FTId=PRO_0000079984.
FT   TRANSMEM     36     56       Helical; (Potential).
FT   COMPBIAS     80     83       Poly-Thr.
FT   COMPBIAS    467    474       Poly-Gly.
FT   COMPBIAS    480    483       Poly-Pro.
FT   COMPBIAS    644    649       Poly-Gly.
FT   COMPBIAS    693    696       Poly-Ala.
FT   MOD_RES     297    297       Phosphoserine.
FT   MOD_RES     302    302       Phosphoserine (By similarity).
FT   MOD_RES     485    485       Phosphoserine.
FT   MOD_RES     527    527       Phosphoserine.
FT   MOD_RES     531    531       Phosphoserine (By similarity).
FT   MOD_RES     699    699       Phosphoserine (By similarity).
FT   MOD_RES     703    703       Phosphoserine (By similarity).
FT   CONFLICT    562    562       H -> Y (in Ref. 2; BAC29200).
FT   CONFLICT    641    641       E -> K (in Ref. 2; BAC29200).
FT   CONFLICT    644    644       G -> A (in Ref. 2; BAC29200).
SQ   SEQUENCE   705 AA;  75012 MW;  FE66275E8AFF1B5E CRC64;
     MATAAATTAT VALTTSWDNA TSRPTAEPDP ILDNYVLLVV VMSLFVGGTL VVLSGVLLLC
     KRCWEVHQRF NRAMEEAEKT TTTYLDNGTH PIQDWAQFES DSSLFPDPDC RGEDPEGQDT
     ETERFLATSS TGRRVSFNEA ALFEQSRKAQ DKGRRYTLTE GDFHHLKNAR LTHLHLPPLK
     IATIHECDSG EASAAATPHP ATTSKDSLAI FQPPGKTLTG HSVGPSSALP GGPYNSVDFS
     EISPSTSSDS GEGISLDAGT RGAKAAGPET VPGEMGTGSS GSGTVLQFFT RLRRHASLDG
     ASPYFKVKKW KLEPSQRASS LDTRGSPKRH HFQRQRAASE SMEQEGDVPH ADFIQYIASA
     GDSVAFPPPR PFLASPTSPP PTLGRLEAAE AAGGASPETP PEHGISLGPE HAQQQDPQQE
     QDAEHAQCSY RDLWSLRASL ELHAATASDH SSSGNDRDSV RSGDSSGSGS GGGGAAPAFP
     PPPESPPALR PKDGEARRLL QMDSGYASIE GRGAGDEVSE LPAPARSPPR SPRAWPRRPR
     RDYSIDEKTD ALFHEFLRHD PHFDDAPRHR TRAHPHTHAR KQWQQRGRQH SDPGGARAAT
     PPGVARPTRA PLRRGDSVDC PPEGRALPIT GDDPSIPVIE EEPGGGGGGC PGSGLCVEPA
     GALLDKLAAS LDERLFSPRL AEPVASSQVL IVAAAAPTSP DHSPA
//
ID   PKHG5_MOUSE             Reviewed;        1073 AA.
AC   Q66T02; A2A8B6; A2A8B7; Q66T00; Q6P3B1; Q6ZQ62; Q8R571;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Pleckstrin homology domain-containing family G member 5;
DE            Short=PH domain-containing family G member 5;
DE   AltName: Full=Synectin-binding RhoA exchange factor;
DE            Short=SYX;
GN   Name=Plekhg5; Synonyms=Kiaa0720, Syx;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
RP   AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J;
RX   PubMed=16467373; DOI=10.1091/mbc.E06-01-0002;
RA   Liu M., Horowitz A.;
RT   "A PDZ-binding motif as a critical determinant of Rho guanine exchange
RT   factor function and cell phenotype.";
RL   Mol. Biol. Cell 17:1880-1887(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 576-1073.
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 596-1073 (ISOFORM 1).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary gland, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-936; SER-938 AND
RP   SER-964, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Activates the NF-kappa-B signaling pathway and RHOA.
CC       Appears to be involved in the control of neuronal cell
CC       differentiation (By similarity).
CC   -!- SUBUNIT: Interacts with GIPC1/synectin and RHOA (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
CC       Note=Predominantly cytoplasmic, however when cells are stimulated
CC       found in perinuclear regions.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=SYX1;
CC         IsoId=Q66T02-1; Sequence=Displayed;
CC       Name=2; Synonyms=SYX2;
CC         IsoId=Q66T02-2; Sequence=VSP_028587;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Isoform 2 is expressed at detectable levels
CC       only in malignant cells.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM24581.1; Type=Erroneous gene model prediction;
CC       Sequence=CAM24582.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY605057; AAU04953.1; -; mRNA.
DR   EMBL; AY605058; AAU04954.1; -; mRNA.
DR   EMBL; AL772240; CAM19697.1; -; Genomic_DNA.
DR   EMBL; AL611927; CAM19697.1; JOINED; Genomic_DNA.
DR   EMBL; AL772240; CAM19699.1; -; Genomic_DNA.
DR   EMBL; AL611927; CAM19699.1; JOINED; Genomic_DNA.
DR   EMBL; AL611927; CAM24581.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL772240; CAM24581.1; JOINED; Genomic_DNA.
DR   EMBL; AL611927; CAM24582.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL772240; CAM24582.1; JOINED; Genomic_DNA.
DR   EMBL; AK129198; BAC98008.1; -; mRNA.
DR   EMBL; BC023181; AAH23181.1; -; mRNA.
DR   EMBL; BC064091; AAH64091.1; -; mRNA.
DR   IPI; IPI00471031; -.
DR   IPI; IPI00621873; -.
DR   RefSeq; NP_001004156.1; NM_001004156.2.
DR   UniGene; Mm.332102; -.
DR   HSSP; O15085; 1XCG.
DR   ProteinModelPortal; Q66T02; -.
DR   SMR; Q66T02; 388-755.
DR   STRING; Q66T02; -.
DR   PhosphoSite; Q66T02; -.
DR   PRIDE; Q66T02; -.
DR   Ensembl; ENSMUST00000105661; ENSMUSP00000101286; ENSMUSG00000039713.
DR   GeneID; 269608; -.
DR   KEGG; mmu:269608; -.
DR   UCSC; uc008vzh.1; mouse.
DR   CTD; 269608; -.
DR   MGI; MGI:2652860; Plekhg5.
DR   eggNOG; roNOG07998; -.
DR   GeneTree; ENSGT00510000046843; -.
DR   HOVERGEN; HBG058106; -.
DR   InParanoid; Q66T02; -.
DR   OMA; CMEYMRG; -.
DR   OrthoDB; EOG4P8FHB; -.
DR   PhylomeDB; Q66T02; -.
DR   ArrayExpress; Q66T02; -.
DR   Bgee; Q66T02; -.
DR   Genevestigator; Q66T02; -.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IDA:MGI.
DR   GO; GO:0043542; P:endothelial cell migration; IDA:MGI.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Phosphoprotein.
FT   CHAIN         1   1073       Pleckstrin homology domain-containing
FT                                family G member 5.
FT                                /FTId=PRO_0000307135.
FT   DOMAIN      406    598       DH.
FT   DOMAIN      654    754       PH.
FT   COMPBIAS    107    111       Poly-Glu.
FT   COMPBIAS    369    373       Poly-Glu.
FT   COMPBIAS    778    790       Poly-Glu.
FT   MOD_RES     259    259       Phosphoserine.
FT   MOD_RES     936    936       Phosphoserine.
FT   MOD_RES     938    938       Phosphoserine.
FT   MOD_RES     964    964       Phosphoserine.
FT   VAR_SEQ    1072   1073       Missing (in isoform 2).
FT                                /FTId=VSP_028587.
SQ   SEQUENCE   1073 AA;  118924 MW;  E34A0B88D61CEE2B CRC64;
     MGTGPGVSGR RAAARPSSEL PSPDSQLLWV GGHAHSSDSQ VCHHADCQQL HHRGPLNLCE
     TCDSKFHSTL HYDGHVRFDL PPQGSVLARN VSTRSCPPRT SPAADLEEEE EGCTDGKGDR
     KSAGLKISKK KARRRHTDDP SKECFTLKFD LNVDIETEIV PAMKKKSLGE VLLPVFERKG
     IALGKVDIYL DQSNTPLSLT FEAYRFGGHY LRVKAKPGDE GKVEQGVKDS KSLSLPALRP
     SGAGPPVSER VDPQSRRESS LDILAPGRRR KNMSEFLGEA GIPGHEPPAP SSCSLPVGSS
     GGTSSGINES WKNRAASRFS GFFSSSPSTS AFSREVDKME QLESKLHAYS LFGLPRMPRR
     LRFDHDSWEE EEEDDEEDEE SSGLRLEDSW RELTDGHEKL TRRQCHQQEA VWELLHTEVS
     YIRKLRVITN LFLCCLLNLQ ESGLLCEVEA ERLFSNIPEI AKLHRGLWGS VMVPVLEKAR
     RTRALLQPSD FLKGFKMFGS LFKPYIRYCM EEEGCMEYMR GLLRDNDLFR AYVTWAEKHQ
     QCQRLKLSDM LAKPHQRLTK YPLLLKSVLR KTDDPRTKEA IVTMISSVER FIHHVNTCMR
     QRQERQRLAG VVSRIDAYEV VEGSNDEVDK LLKEFLHLDL TAPMPGTSPE ETRQLLLEGS
     LRMKEGKDSK MDVYCFLFTD LLLVTKAVKK AERTKVIRPP LLVDKIVCRE LRDPGSFLLI
     YLNEFHSAVG AYTFQASSQA LCRSWVDTIY NAQNQLQQLR AQLSAQEHPG SQHLQSLEEE
     EDEQEEEGEE SGTSAASSPT ILRKSSNSLD SEHCTSDGST ETLAMVVVEP GATLSSPEFE
     GGPVSSQSDE SSLSNTASSV TPTSELLPLG PVDGRSCSMD SAYGTLSPTS LQDFVAPHPV
     VEPAPVPQTP SPQPSPRLRR RTPVQLLPRP PRLLKSKSEA SLLQLLSGTP AARGVPPAPS
     RSLSELCLIS VAPGVRTQRP LQEGGPGWNG PGMCDPCHGP QLSESENRPS HMTGGPADSA
     RRRCREMPSG TMSRVQSEPP SGVSAQHRKL TLAQLYRIRT TLLLNSTLTA SEV
//
ID   GRM7_MOUSE              Reviewed;         915 AA.
AC   Q68ED2;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Metabotropic glutamate receptor 7;
DE            Short=mGluR7;
DE   Flags: Precursor;
GN   Name=Grm7; Synonyms=Gprc1g, Mglur7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-900, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Receptor for glutamate. The activity of this receptor is
CC       mediated by a G-protein that inhibits adenylate cyclase activity
CC       (By similarity).
CC   -!- SUBUNIT: Interacts with PICK1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC080315; AAH80315.1; -; mRNA.
DR   IPI; IPI00470956; -.
DR   RefSeq; NP_796302.2; NM_177328.3.
DR   UniGene; Mm.240881; -.
DR   ProteinModelPortal; Q68ED2; -.
DR   SMR; Q68ED2; 40-580.
DR   DIP; DIP-32216N; -.
DR   STRING; Q68ED2; -.
DR   PhosphoSite; Q68ED2; -.
DR   PRIDE; Q68ED2; -.
DR   Ensembl; ENSMUST00000071076; ENSMUSP00000064404; ENSMUSG00000056755.
DR   GeneID; 108073; -.
DR   KEGG; mmu:108073; -.
DR   UCSC; uc009ddt.1; mouse.
DR   CTD; 108073; -.
DR   MGI; MGI:1351344; Grm7.
DR   HOGENOM; HBG445787; -.
DR   HOVERGEN; HBG107965; -.
DR   InParanoid; Q68ED2; -.
DR   OMA; PNIIVDY; -.
DR   OrthoDB; EOG4ZW59D; -.
DR   NextBio; 359996; -.
DR   ArrayExpress; Q68ED2; -.
DR   Bgee; Q68ED2; -.
DR   CleanEx; MM_GRM7; -.
DR   Genevestigator; Q68ED2; -.
DR   GermOnline; ENSMUSG00000056755; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048787; C:presynaptic active zone membrane; TAS:UniProtKB.
DR   GO; GO:0005246; F:calcium channel regulator activity; IDA:MGI.
DR   GO; GO:0001642; F:group III metabotropic glutamate receptor activity; TAS:MGI.
DR   GO; GO:0030165; F:PDZ domain binding; TAS:UniProtKB.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:UniProtKB.
DR   GO; GO:0030534; P:adult behavior; IMP:MGI.
DR   GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR   GO; GO:0001661; P:conditioned taste aversion; IMP:MGI.
DR   GO; GO:0043526; P:neuroprotection; TAS:UniProtKB.
DR   GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
DR   GO; GO:0007614; P:short-term memory; IMP:MGI.
DR   GO; GO:0007268; P:synaptic transmission; IDA:UniProtKB.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR000337; GPCR_3.
DR   InterPro; IPR011500; GPCR_3_9-Cys_dom.
DR   InterPro; IPR017978; GPCR_3_C.
DR   InterPro; IPR017979; GPCR_3_CS.
DR   InterPro; IPR000162; GPCR_3_mtglu_rcpt.
DR   InterPro; IPR001883; GPCR_3_mtglu_rcpt_7.
DR   Pfam; PF00003; 7tm_3; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF07562; NCD3G; 1.
DR   PRINTS; PR00248; GPCRMGR.
DR   PRINTS; PR01057; MTABOTROPC7R.
DR   PRINTS; PR00593; MTABOTROPICR.
DR   PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; 1.
DR   PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; 1.
DR   PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
DR   PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Olfaction; Phosphoprotein; Receptor; Sensory transduction; Signal;
KW   Transducer; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     34       Potential.
FT   CHAIN        35    915       Metabotropic glutamate receptor 7.
FT                                /FTId=PRO_0000012939.
FT   TOPO_DOM     35    590       Extracellular (Potential).
FT   TRANSMEM    591    615       Helical; Name=1; (Potential).
FT   TOPO_DOM    616    627       Cytoplasmic (Potential).
FT   TRANSMEM    628    648       Helical; Name=2; (Potential).
FT   TOPO_DOM    649    654       Extracellular (Potential).
FT   TRANSMEM    655    675       Helical; Name=3; (Potential).
FT   TOPO_DOM    676    702       Cytoplasmic (Potential).
FT   TRANSMEM    703    723       Helical; Name=4; (Potential).
FT   TOPO_DOM    724    753       Extracellular (Potential).
FT   TRANSMEM    754    775       Helical; Name=5; (Potential).
FT   TOPO_DOM    776    788       Cytoplasmic (Potential).
FT   TRANSMEM    789    810       Helical; Name=6; (Potential).
FT   TOPO_DOM    811    825       Extracellular (Potential).
FT   TRANSMEM    826    850       Helical; Name=7; (Potential).
FT   TOPO_DOM    851    915       Cytoplasmic (Potential).
FT   MOD_RES     900    900       Phosphoserine.
FT   CARBOHYD     98     98       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    458    458       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    486    486       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    572    572       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   915 AA;  102219 MW;  F0AF7AEDBFBCCF71 CRC64;
     MVQLGKLLRV LTLMKFPCCV LEVLLCVLAA AARGQEMYAP HSIRIEGDVT LGGLFPVHAK
     GPSGVPCGDI KRENGIHRLE AMLYALDQIN SDPNLLPNVT LGARILDTCS RDTYALEQSL
     TFVQALIQKD TSDVRCTNGE PPVFVKPEKV VGVIGASGSS VSIMVANILR LFQIPQISYA
     STAPELSDDR RYDFFSRVVP PDSFQAQAMV DIVKALGWNY VSTLASEGSY GEKGVESFTQ
     ISKEAGGLCI AQSVRIPQER KDRTIDFDRI IKQLLDTPNS RAVVIFANDE DIKQILAAAK
     RADQVGHFLW VGSDSWGSKI NPLHQHEDIA EGAITIQPKR ATVEGFDAYF TSRTLENNRR
     NVWFAEYWEE NFNCKLTISG SKKEDTDRKC TGQERIGKDS NYEQEGKVQF VIDAVYAMAH
     ALHHMNKDLC ADYRGVCPEM EQAGGKKLLK YIRNVNFNGS AGTPVMFNKN GDAPGRYDIF
     QYQTTNTTNP GYRLIGQWTD ELQLNIEDMQ WGKGVREIPP SVCTLPCKPG QRKKTQKGTP
     CCWTCEPCDG YQYQFDEMTC QHCPYDQRPN ENRTGCQNIP IIKLEWHSPW AVIPVFLAML
     GIIATIFVMA TFIRYNDTPI VRASGRELSY VLLTGIFLCY IITFLMIAKP DVAVCSFRRV
     FLGLGMCISY AALLTKTNRI YRIFEQGKKS VTAPRLISPT SQLAITSSLI SVQLLGVFIW
     FGVDPPNIII DYDEHKTMNP EQARGVLKCD ITDLQIICSL GYSILLMVTC TVYAIKTRGV
     PENFNEAKPI GFTMYTTCIV WLAFIPIFFG TAQSAEKLYI QTTTLTISMN LSASVALGML
     YMPKVYIIIF HPELNVQKRK RSFKAVVTAA TMSSRLSHKP SDRPNGEAKT ELCENVDPNS
     PAAKKKYVSY NNLVI
//
ID   RAB3I_MOUSE             Reviewed;         428 AA.
AC   Q68EF0;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Rab-3A-interacting protein;
DE            Short=Rab3A-interacting protein;
DE   AltName: Full=Rabin-3;
DE   AltName: Full=SSX2-interacting protein;
GN   Name=Rab3ip;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-217, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240 AND SER-242, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBUNIT: Interacts with the N-terminal region of SSX2. Interacts
CC       with RAB3A and RAB3D (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Predominantly cytoplasmic but a small proportion
CC       colocalizes with SSX2 in the nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the SEC2 family.
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DR   EMBL; BC080289; AAH80289.1; -; mRNA.
DR   IPI; IPI00461479; -.
DR   RefSeq; NP_001003950.1; NM_001003950.2.
DR   UniGene; Mm.336394; -.
DR   ProteinModelPortal; Q68EF0; -.
DR   SMR; Q68EF0; 152-207.
DR   STRING; Q68EF0; -.
DR   PhosphoSite; Q68EF0; -.
DR   PRIDE; Q68EF0; -.
DR   Ensembl; ENSMUST00000020375; ENSMUSP00000020375; ENSMUSG00000064181.
DR   GeneID; 216363; -.
DR   KEGG; mmu:216363; -.
DR   UCSC; uc007hcj.1; mouse.
DR   CTD; 216363; -.
DR   MGI; MGI:105933; Rab3ip.
DR   eggNOG; roNOG09985; -.
DR   HOGENOM; HBG315948; -.
DR   HOVERGEN; HBG057034; -.
DR   InParanoid; Q68EF0; -.
DR   OMA; APIQANA; -.
DR   OrthoDB; EOG4X6C8J; -.
DR   PhylomeDB; Q68EF0; -.
DR   NextBio; 375123; -.
DR   ArrayExpress; Q68EF0; -.
DR   Bgee; Q68EF0; -.
DR   CleanEx; MM_RAB3IP; -.
DR   Genevestigator; Q68EF0; -.
DR   GermOnline; ENSMUSG00000064181; Mus musculus.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR009449; Sec2p.
DR   Pfam; PF06428; Sec2p; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Guanine-nucleotide releasing factor; Nucleus;
KW   Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1    428       Rab-3A-interacting protein.
FT                                /FTId=PRO_0000097145.
FT   COILED      149    212       Potential.
FT   MOD_RES     147    147       Phosphoserine (By similarity).
FT   MOD_RES     217    217       Phosphothreonine.
FT   MOD_RES     218    218       Phosphoserine (By similarity).
FT   MOD_RES     220    220       Phosphothreonine (By similarity).
FT   MOD_RES     240    240       Phosphoserine.
FT   MOD_RES     242    242       Phosphoserine.
SQ   SEQUENCE   428 AA;  47133 MW;  443F79CDDACD9D3F CRC64;
     MANDPLEGFH EVNLASPTSP DLLGVCDPGT QEQTTSPSVI YRPHPSTLCA APLQANALDL
     SDLPTQPVYS SPRHFNCAEV SNISAHAPDP ASSVPSAVAS GLTKLTSRKD SCNAEREFLQ
     GATITEASAG NDDIFGLSTD SLSRLRSPSV LEVREKGYER LKEELAKAQR EAHKMVREAN
     VKQATAEKQL KEAQGKIDVL QAEVAALKTL VLSSSPTSPT QEPLAAAKTP FKRGHTRNKS
     TSSAMGGSHQ DLSVIQPIVK DCKEADLSLY NEFRSWKDEP TMDRTCPFLD KIYQEDIFPC
     LTFAKSELAS AVLEAVENNT LSIEPVGLQP IRFVKASAVE CGGPKKCALT GQSKPCRHRI
     RLGDSSCCYY ISPFCRYRIT SVCNFFTYIR YIQQGLVKQQ DVDQMFWEVM QLRKEMSLAK
     LGYFKEEL
//
ID   BEGIN_MOUSE             Reviewed;         600 AA.
AC   Q68EF6;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Brain-enriched guanylate kinase-associated protein;
GN   Name=Begain;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-600.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 AND SER-246, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-137, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265; SER-357 AND
RP   SER-473, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: May sustain the structure of the postsynaptic density
CC       (PSD).
CC   -!- SUBUNIT: Interacts with DLG4 and DLGAP1 and forms a ternary
CC       complex (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane;
CC       Peripheral membrane protein (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
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DR   EMBL; AC140111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC080282; AAH80282.1; -; mRNA.
DR   IPI; IPI00380950; -.
DR   RefSeq; NP_001156647.1; NM_001163175.1.
DR   UniGene; Mm.342085; -.
DR   ProteinModelPortal; Q68EF6; -.
DR   STRING; Q68EF6; -.
DR   PhosphoSite; Q68EF6; -.
DR   PRIDE; Q68EF6; -.
DR   Ensembl; ENSMUST00000073156; ENSMUSP00000072899; ENSMUSG00000040867.
DR   GeneID; 380785; -.
DR   KEGG; mmu:380785; -.
DR   UCSC; uc007pal.1; mouse.
DR   CTD; 380785; -.
DR   MGI; MGI:3044626; Begain.
DR   eggNOG; roNOG11365; -.
DR   GeneTree; ENSGT00530000063778; -.
DR   HOGENOM; HBG505527; -.
DR   HOVERGEN; HBG050683; -.
DR   InParanoid; Q68EF6; -.
DR   OMA; QNNYLAL; -.
DR   OrthoDB; EOG4WQ12D; -.
DR   ArrayExpress; Q68EF6; -.
DR   Bgee; Q68EF6; -.
DR   CleanEx; MM_BEGAIN; -.
DR   Genevestigator; Q68EF6; -.
DR   GermOnline; ENSMUSG00000040867; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Cytoplasm; Membrane; Phosphoprotein.
FT   CHAIN         1    600       Brain-enriched guanylate kinase-
FT                                associated protein.
FT                                /FTId=PRO_0000064905.
FT   MOD_RES     137    137       Phosphotyrosine.
FT   MOD_RES     194    194       Phosphoserine.
FT   MOD_RES     246    246       Phosphoserine.
FT   MOD_RES     265    265       Phosphoserine.
FT   MOD_RES     357    357       Phosphoserine.
FT   MOD_RES     473    473       Phosphoserine.
FT   MOD_RES     491    491       Phosphoserine (By similarity).
FT   MOD_RES     510    510       Phosphoserine (By similarity).
FT   MOD_RES     570    570       Phosphoserine (By similarity).
SQ   SEQUENCE   600 AA;  65309 MW;  0BECA620CF2971D0 CRC64;
     MEKLSALQEQ KGELRKRLSY TTHKLEKLET EFDSTRHYLE IELRRAQEEL DKVTEKLRRI
     QSNYMALQRI NQELEDKLYR MGQHYEEEKR AMSHEIVALN SHLLEAKVTI DKLSEDNELY
     RKDCNLAAQL LQCSQTYGRV HKVSELPSDF QQRVSLHMEK HGCSLPSALC HPAYADSVPT
     CVIAKVLEKP DPGSLSSRMS DASARDLGYR DGVEKSGPRP PYKGDIYCSD PALYCPDERE
     HARRPSVDTP VTDVGFLRAQ NSTDSAAEEE EEAEAAAFPE AYRREAYQGY AASLPTSSSY
     SSFSATSEEK EHAQAGTLTA SQQAIYLSSR DEFFNRKPSA TYGSGPRFAK AASTLGSPLE
     AQVAPGFART VSPYPAEPYR YPASPGPQQA LMPPNLWSLR AKPSGNRLAG EDIRGQWRPV
     SVEDVGAYSY QAGAAAGRAA SPCNYSERYY GGGGGGGAAG GGSPGDKAEG RASPLYATYK
     ADSFSEGDDL SQGHLAEPCF LRAGGDLSLS PSRSADALAG YAASDGDGDR LRVQLCGAGS
     SPEPEHGSRE SLEPSSMEAS PEMHPPTRLS PQQAFPRTGG SGLSRKDSLT KAQLYGTLLN
//
ID   CLH_MOUSE               Reviewed;        1675 AA.
AC   Q68FD5;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Clathrin heavy chain 1;
GN   Name=Cltc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 44-63; 87-96; 101-112; 145-157; 164-188; 190-205;
RP   228-245; 270-278; 298-320; 355-366; 377-382; 430-444; 446-453;
RP   457-481; 626-637; 768-780; 799-806; 838-852 AND 857-881.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-184; TYR-634; TYR-899;
RP   TYR-1206; TYR-1477 AND TYR-1487, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   INTERACTION WITH OCRL.
RX   PubMed=20133602; DOI=10.1073/pnas.0914658107;
RA   Swan L.E., Tomasini L., Pirruccello M., Lunardi J., De Camilli P.;
RT   "Two closely related endocytic proteins that share a common OCRL-
RT   binding motif with APPL1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:3511-3516(2010).
CC   -!- FUNCTION: Clathrin is the major protein of the polyhedral coat of
CC       coated pits and vesicles. Two different adapter protein complexes
CC       link the clathrin lattice either to the plasma membrane or to the
CC       trans-Golgi network (By similarity).
CC   -!- SUBUNIT: Clathrin triskelions, composed of 3 heavy chains and 3
CC       light chains, are the basic subunits of the clathrin coat. In the
CC       presence of light chains, hub assembly is influenced by both the
CC       pH and the concentration of calcium. Interacts with HIP1 (By
CC       similarity). Interacts with DENND1A, DENND1B and DENND1C (By
CC       similarity). Interacts with OCRL.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral
CC       membrane protein; Cytoplasmic side (By similarity). Membrane,
CC       coated pit; Peripheral membrane protein; Cytoplasmic side (By
CC       similarity). Melanosome (By similarity). Note=Cytoplasmic face of
CC       coated pits and vesicles (By similarity).
CC   -!- SIMILARITY: Belongs to the clathrin heavy chain family.
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DR   EMBL; AL592222; CAI25362.1; -; Genomic_DNA.
DR   EMBL; BC079897; AAH79897.1; -; mRNA.
DR   IPI; IPI00169916; -.
DR   RefSeq; NP_001003908.1; NM_001003908.1.
DR   UniGene; Mm.479526; -.
DR   ProteinModelPortal; Q68FD5; -.
DR   SMR; Q68FD5; 1-493, 1077-1630.
DR   STRING; Q68FD5; -.
DR   PRIDE; Q68FD5; -.
DR   Ensembl; ENSMUST00000103186; ENSMUSP00000099475; ENSMUSG00000047126.
DR   GeneID; 67300; -.
DR   KEGG; mmu:67300; -.
DR   UCSC; uc007kta.1; mouse.
DR   CTD; 67300; -.
DR   MGI; MGI:2388633; Cltc.
DR   HOVERGEN; HBG005344; -.
DR   OrthoDB; EOG4TXBR0; -.
DR   PhylomeDB; Q68FD5; -.
DR   NextBio; 324168; -.
DR   ArrayExpress; Q68FD5; -.
DR   Bgee; Q68FD5; -.
DR   CleanEx; MM_CLTC; -.
DR   Genevestigator; Q68FD5; -.
DR   GermOnline; ENSMUSG00000047126; Mus musculus.
DR   GO; GO:0030132; C:clathrin coat of coated pit; IEA:InterPro.
DR   GO; GO:0030130; C:clathrin coat of trans-Golgi network vesicle; IEA:InterPro.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR   InterPro; IPR016025; Clathrin_H-chain_link/propller.
DR   InterPro; IPR015348; Clathrin_H-chain_linker_core.
DR   InterPro; IPR001473; Clathrin_H-chain_propeller_N.
DR   InterPro; IPR022365; Clathrin_H-chain_propeller_rpt.
DR   InterPro; IPR016341; Clathrin_heavy_chain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   Gene3D; G3DSA:2.130.10.110; Clathrin_H-chain_link/propller; 1.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 3.
DR   Pfam; PF09268; Clathrin-link; 1.
DR   Pfam; PF01394; Clathrin_propel; 3.
DR   PIRSF; PIRSF002290; Clathrin_H_chain; 1.
DR   SMART; SM00299; CLH; 7.
DR   SUPFAM; SSF48371; ARM-type_fold; 5.
DR   SUPFAM; SSF50989; Clathrin_H-chain_propeller_N; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coated pit; Cytoplasmic vesicle;
KW   Direct protein sequencing; Membrane; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1675       Clathrin heavy chain 1.
FT                                /FTId=PRO_0000205779.
FT   REGION        2    479       Globular terminal domain.
FT   REGION      449    465       Binding site for the uncoating ATPase,
FT                                involved in lattice disassembly
FT                                (Potential).
FT   REGION      480    523       Flexible linker.
FT   REGION      524   1675       Heavy chain arm.
FT   REGION      524    634       Distal segment.
FT   REGION      639   1675       Proximal segment.
FT   REGION     1213   1522       Involved in binding clathrin light chain
FT                                (By similarity).
FT   REGION     1550   1675       Trimerization (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     184    184       Phosphotyrosine.
FT   MOD_RES     394    394       Phosphothreonine (By similarity).
FT   MOD_RES     634    634       Phosphotyrosine.
FT   MOD_RES     899    899       Phosphotyrosine.
FT   MOD_RES    1206   1206       Phosphotyrosine.
FT   MOD_RES    1477   1477       Phosphotyrosine.
FT   MOD_RES    1487   1487       Phosphotyrosine.
FT   MOD_RES    1494   1494       Phosphoserine (By similarity).
SQ   SEQUENCE   1675 AA;  191557 MW;  6C41EBD89EB7D56B CRC64;
     MAQILPIRFQ EHLQLQNLGI NPANIGFSTL TMESDKFICI REKVGEQAQV VIIDMNDPSN
     PIRRPISADS AIMNPASKVI ALKAGKTLQI FNIEMKSKMK AHTMTDDVTF WKWISLNTVA
     LVTDNAVYHW SMEGESQPVK MFDRHSSLAG CQIINYRTDA KQKWLLLTGI SAQQNRVVGA
     MQLYSVDRKV SQPIEGHAAS FAQFKMEGNA EESTLFCFAV RGQAGGKLHI IEVGTPPTGN
     QPFPKKAVDV FFPPEAQNDF PVAMQISEKH DVVFLITKYG YIHLYDLETG TCIYMNRISG
     ETIFVTAPHE ATAGIIGVNR KGQVLSVCVE EENIIPYITN VLQNPDLALR MAVRNNLAGA
     EELFARKFNA LFAQGNYSEA AKVAANAPKG ILRTPDTIRR FQSVPAQPGQ TSPLLQYFGI
     LLDQGQLNKY ESLELCRPVL QQGRKQLLEK WLKEDKLECS EELGDLVKSV DPTLALSVYL
     RANVPNKVIQ CFAETGQVQK IVLYAKKVGY TPDWIFLLRN VMRISPDQGQ QFAQMLVQDE
     EPLADITQIV DVFMEYNLIQ QCTAFLLDAL KNNRPSEGPL QTRLLEMNLM HAPQVADAIL
     GNQMFTHYDR AHIAQLCEKA GLLQRALEHF TDLYDIKRAV VHTHLLNPEW LVNYFGSLSV
     EDSLECLRAM LSANIRQNLQ ICVQVASKYH EQLSTQSLIE LFESFKSFEG LFYFLGSIVN
     FSQDPDVHFK YIQAACKTGQ IKEVERICRE SNCYDPERVK NFLKEAKLTD QLPLIIVCDR
     FDFVHDLVLY LYRNNLQKYI EIYVQKVNPS RLPVVIGGLL DVDCSEDVIK NLILVVRGQF
     STDELVAEVE KRNRLKLLLP WLEARIHEGC EEPATHNALA KIYIDSNNNP ERFLRENPYY
     DSRVVGKYCE KRDPHLACVA YERGQCDLEL INVCNENSLF KSLSRYLVRR KDPELWGSVL
     LESNPYRRPL IDQVVQTALS ETQDPEEVSV TVKAFMTADL PNELIELLEK IVLDNSVFSE
     HRNLQNLLIL TAIKADRTRV MEYINRLDNY DAPDIANIAI SNELFEEAFA IFRKFDVNTS
     AVQVLIEHIG NLDRAYEFAE RCNEPAVWSQ LAKAQLQKGM VKEAIDSYIK ADDPSSYMEV
     VQAANASGNW EELVKYLQMA RKKARESYVE TELIFALAKT NRLAELEEFI NGPNNAHIQQ
     VGDRCYDEKM YDAAKLLYNN VSNFGRLAST LVHLGEYQAA VDGARKANST RTWKEVCFAC
     VDGKEFRLAQ MCGLHIVVHA DELEELINYY QDRGYFEELI TMLEAALGLE RAHMGMFTEL
     AILYSKFKPQ KMREHLELFW SRVNIPKVLR AAEQAHLWAE LVFLYDKYEE YDNAIITMMN
     HPTDAWKEGQ FKDIITKVAN VELYYKAIQF YLEFKPLLLN DLLMVLSPRL DHTRAVNYFS
     KVKQLPLVKP YLRSVQNHNN KSVNESLNNL FITEEDYQAL RTSIDAYDNF DNISLAQRLE
     KHELIEFRRI AAYLFKGNNR WKQSVELCKK DSLYKDAMQY ASESKDTELA EELLQWFLQE
     EKRECFGACL FTCYDLLRPD VVLETAWRHN IMDFAMPYFI QVMKEYLTKV DKLDASESLR
     KEEEQATETQ PIVYGQPQLM LTAGPSVAVP PQAPFGYGYT APPYGQPQPG FGYSM
//
ID   K1549_MOUSE             Reviewed;        1799 AA.
AC   Q68FD9; Q6ZPN1;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   08-FEB-2011, entry version 37.
DE   RecName: Full=UPF0606 protein KIAA1549;
GN   Name=Kiaa1549;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-467 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 797-1799 (ISOFORM 2).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1432, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q68FD9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q68FD9-2; Sequence=VSP_034449, VSP_034450;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the UPF0606 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC125530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC157667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC054075; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC079889; AAH79889.1; -; mRNA.
DR   EMBL; AK129390; BAC98200.1; -; mRNA.
DR   IPI; IPI00623897; -.
DR   IPI; IPI00886009; -.
DR   RefSeq; NP_918950.2; NM_194061.2.
DR   UniGene; Mm.277163; -.
DR   PhosphoSite; Q68FD9; -.
DR   Ensembl; ENSMUST00000117556; ENSMUSP00000112939; ENSMUSG00000063455.
DR   GeneID; 330286; -.
DR   KEGG; mmu:330286; -.
DR   UCSC; uc009bjt.1; mouse.
DR   MGI; MGI:2669829; D630045J12Rik.
DR   GeneTree; ENSGT00530000063472; -.
DR   HOGENOM; HBG506931; -.
DR   HOVERGEN; HBG108038; -.
DR   InParanoid; Q68FD9; -.
DR   ArrayExpress; Q68FD9; -.
DR   Bgee; Q68FD9; -.
DR   Genevestigator; Q68FD9; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Alternative splicing; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   1799       UPF0606 protein KIAA1549.
FT                                /FTId=PRO_0000342406.
FT   TRANSMEM    847    867       Helical; (Potential).
FT   TRANSMEM   1147   1167       Helical; (Potential).
FT   COMPBIAS    198    738       Ser-rich.
FT   MOD_RES    1243   1243       Phosphoserine (By similarity).
FT   MOD_RES    1432   1432       Phosphoserine.
FT   VAR_SEQ    1613   1613       S -> R (in isoform 2).
FT                                /FTId=VSP_034449.
FT   VAR_SEQ    1614   1799       Missing (in isoform 2).
FT                                /FTId=VSP_034450.
FT   CONFLICT     20     20       R -> W (in Ref. 2; BC054075).
SQ   SEQUENCE   1799 AA;  193995 MW;  5DBF92C077575BCC CRC64;
     MDNFLPDAHW TSSRGVSPMR YITPSPPEPP QEMLEPGTTP SLPTISLPDE VLSGCQNTVQ
     QATVYVEPST YFGTSWSAFL TSEGIIPTPS RNSVLHPIEI HSQLSSKALP ETVASVTEGA
     ENLLFSSRIS VSQPSGNGMT QQPSVPLWEV SQPLVGVLAT SSDRYPNETT AWIEHPEEAI
     ALRAHPGITT SPTDPTFSSQ PSALFSTPLS SVSFATQLPG VSEDSFLSSE ARGALESWHS
     SPVPSFTDHP YVLSPESSLR PHTGCVSCVV SSFQQELARS LTEKDMGSGD RLETLSTASV
     EASHVSPLSS VGTDLSELEE PQEFNTLFPS RPVFSFSSRP VGLWKASMDV SPEVDVSGIA
     ITQVYPSHGR LSTPSSLDST FGFSVTSDLV MSSSMIHLLS SVIPSTHFDS SFSLTANQNS
     PSFPAGKPSL LTSPSLVPSA QSSAFSHGAP TSSLELQSGS RLDFTSGFYS TPPLDFSTPA
     PSRSDELAFP SLMSSDPSTF FSQTFSTMAE TFSLSNSMNL QSPQLSVLNP TSLEPSQPQS
     SADLLLNTVT VLPSPPERPP LSSSPSDSLE FTEVSRVSLR ESHVHLTSAF SETTSAFEFS
     PIPHESTIST LVPSSSEPSL GIYAAGTHLT SLPTTVFHLT PILTESSPFS TLTPSDGSVR
     VTDHHTPVLP TPSSVIPSST ESISDPYLSA SSSLVSEVSP SPPPTKPVMG SSLTSTDFPP
     STSPELSTSL ELSMPSASTA PGDTVDSALN SEPMSQNPQG NSVPPPQPSL GPATTSTLEA
     TVGTPALATA KPPYVCDITV PDVYLITTVL ARRAVQEYII TSIKEVLRIH FNRAVELKVY
     ELFTDFTFLV TSGPFVYTAI SVINVLINSK LVRGQTPLIL SVKPSFLVPD PRFQVQTVLQ
     FVPPSVDTGF CNFTQSIEKG LVTALFEVRK HQGTYNLTVQ IVNVTIASSR VAPRRGPVNI
     IFAVKGSQGF LNGSEVSDLL RNLTVVEFSF YLGYPVLQIA EPFQYPQLNL SQLLKSSWVR
     TVLLGVVEKQ LHNEVFPAEM ERKLAQLLSE VPTRRRVWRR ATVAAGNSVV QVVNVSRLEG
     DDNPVQLIYF VENQDGERLS AVKSSDLINK VDLQRAAIIL GYRIQGVIAQ PVDRVKRPSP
     ESQSNNLWVV VGVVIPVLVV TVIVVILYWK LCRTDKLDFQ PDTVANIQQR QKLQIPSVKG
     FDFAKQHLGQ HNKDDILIIH EPAPLPGPVK DHTTPSENGD VPSPKSKLPS KNIRLRGRVS
     PSDADSTVSE ESSERDAGEK APAAAPENKA LRAPQSGAPL PSSGNEQHSS ASIFEHVDRV
     SRTSEASRRV PSKIQLIAMQ PIPAPPAQHP VLADRVAETN KINKEIQSAL RHKSEIEHHR
     NKIRLRAKRR GHYEFPVVDD LSSGDTKERH RVYRRAQMQI DKILDPAASV PSVFIEPRKS
     SRMKRSPKPR RKHQVNGCPA DAEKDRLITT DSDGTYKRPP GVHNSAYIGC PSDPDLPADV
     QTPSSTELGR YPGLPFSASQ YIPPQPSIEE ARQTMHSLLD DAFALVAPSS QPTNAMGAGT
     GVPASLPVNS TPSREERRAT QWGSFYSPAQ TANNPCSRYE DYGMTPPSGP LPSRPSFGPG
     LLPSSELVPP EPPQPQSSTD APYAARGIYS EEMPSVARPR PVGGTTGSQI QHLTQVGIAS
     RIGAQPVEIP AGRGSQYGGP GWPVYGEEEA GRREATHMLG HQEYSSSPLF QVPRTSGREP
     SAPPGNLAHR GLQGPGLGYP TSSTEDLQPG HSSASLIKAI REELLRLSQK QGSVQNFHS
//
ID   FA65A_MOUSE             Reviewed;        1223 AA.
AC   Q68FE6; Q80T73; Q8K0T1; Q9D6R4;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Protein FAM65A;
GN   Name=Fam65a; Synonyms=Kiaa1930;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1091-1223.
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-351, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SIMILARITY: Belongs to the FAM65 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH06820.1; Type=Erroneous initiation;
CC       Sequence=AAH30451.1; Type=Erroneous initiation;
CC       Sequence=BAB26677.1; Type=Erroneous initiation;
CC       Sequence=BAC65855.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK122573; BAC65855.1; ALT_INIT; mRNA.
DR   EMBL; BC006820; AAH06820.1; ALT_INIT; mRNA.
DR   EMBL; BC030451; AAH30451.1; ALT_INIT; mRNA.
DR   EMBL; BC079880; AAH79880.1; -; mRNA.
DR   EMBL; AK010063; BAB26677.1; ALT_INIT; mRNA.
DR   IPI; IPI00808485; -.
DR   RefSeq; NP_001074710.2; NM_001081241.2.
DR   UniGene; Mm.41261; -.
DR   ProteinModelPortal; Q68FE6; -.
DR   SMR; Q68FE6; 1096-1190.
DR   STRING; Q68FE6; -.
DR   PhosphoSite; Q68FE6; -.
DR   PRIDE; Q68FE6; -.
DR   Ensembl; ENSMUST00000043531; ENSMUSP00000039966; ENSMUSG00000038604.
DR   Ensembl; ENSMUST00000109346; ENSMUSP00000104970; ENSMUSG00000038604.
DR   GeneID; 75687; -.
DR   KEGG; mmu:75687; -.
DR   CTD; 75687; -.
DR   MGI; MGI:1922937; Fam65a.
DR   eggNOG; roNOG09816; -.
DR   GeneTree; ENSGT00490000043360; -.
DR   HOGENOM; HBG716350; -.
DR   HOVERGEN; HBG053834; -.
DR   InParanoid; Q68FE6; -.
DR   OrthoDB; EOG4D7Z4X; -.
DR   NextBio; 343700; -.
DR   ArrayExpress; Q68FE6; -.
DR   Bgee; Q68FE6; -.
DR   CleanEx; MM_2310066E14RIK; -.
DR   Genevestigator; Q68FE6; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Phosphoprotein.
FT   CHAIN         1   1223       Protein FAM65A.
FT                                /FTId=PRO_0000289111.
FT   COILED       83    112       Potential.
FT   COMPBIAS    534    763       Ser-rich.
FT   MOD_RES     345    345       Phosphoserine (By similarity).
FT   MOD_RES     347    347       Phosphoserine (By similarity).
FT   MOD_RES     351    351       Phosphothreonine.
FT   CONFLICT    580    580       I -> T (in Ref. 1; BAC65855 and 2;
FT                                AAH30451).
FT   CONFLICT   1060   1060       Y -> C (in Ref. 2; AAH30451).
SQ   SEQUENCE   1223 AA;  132364 MW;  423063D502548577 CRC64;
     MMSLSVRPQR RLLSARVSRS QSFAGVLGSH ERGPRSFTVF SPPGPPRKPL VLSRVSRMFS
     VAHPAPKVPQ PERLDLVYTA LKRGLTAYLE VHQQEQEKLQ RQIKESKRNS RLGFLYDLDK
     QVKSIERFLR RLEFHASKID ELYEAYCVQR RLRDGAYNMV RAYSTGSPGS REARDSLAEA
     TRGHREYTES MCLLENELEA QLGEFHLRMK GLAGFARLCV GDQYEICMKY GRQRWKLRGR
     IESSGKQVWD SEETVFLPLL TEFLSIKVTE LKGLANHVVV GSVSCETKDL FAALPQVVAV
     DINDLGTIKL SLEVIWSPFD KDDQPSAAST VNKASTVTKR FSTYSQSPPD TPSLREQAFY
     NMLRRQEELE NGTAWSLSSE SSDDSSSPQL SGTARHSTPK PLVQQPEPLP VQVAFRRPES
     LTSGSMDEEP AMTPSLVNGH APYSRTLSHI SEASVDAALT EAVEAVDSQS PIPGPSPLVY
     PDSTHVERVS SVLPVLNNGH SATSPALSTT GPAPTFIDPA PTTQLDLVHK TTDSAPSELP
     SITHTTTSSA YSAVSLVNSV PSLTSTTIGS AHTTTPSPLI STGSVPNATD STQATPSPTH
     STPSPTHTTI RLTHTTVSPT HSSPSPIHTT PSPTHTTVSP TCTTPSSGHS TTSPTQEAKM
     STHTTGAVGP VQTTTSPIST TESPSPSTDV AIISSSSAES TGPGTEPLPC SHPASPPYTK
     ADPTASCTSY QSLASSGSKP LTSPAPDSPE QIPKSPSSSP SSSAPEPQHS EHNLAAVAQA
     PVPEATGGAG DRRLEEALGT LMSALDDYRG QFPELQGLEQ EVTRLESLLM QRQGLTRSRA
     SSLSITVEHA LESFSFLNDD EDEDNDGPGD RHTSSPEVVA EDRLDSSNGQ SLSTGCSALD
     ATLVQHLYHC SRLLLKLGTF GPLRCQEAWA LERLLREARV FQEVCERSKL WGNSATSAQE
     VVQFSASRPG FLTFWDQCTE GLSPFICSVE RVLLTFCSQY GARLSLRQPG LAEAVCVKFL
     EDALGQKLPR RPQPGPGEQF TIFQFWSYVE ALDSPSMDAY VTETAEEVLL VQNLNSDDQA
     VVLKALRLAP EGRLRKDGLR ALSSLLVHGN NKVMAAVSTQ LRSLSLGPVF RERALLCFLD
     QLEDGDVQTR VAGCLALGCI KAPEGIEPLV YLCQTDTEAV REAARQSLQQ CGEEGQSAHR
     QLEESLDALP CIFGPSSMAS TAF
//
ID   T151B_MOUSE             Reviewed;         561 AA.
AC   Q68FE7; Q5XJV8;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=Transmembrane protein 151B;
GN   Name=Tmem151b; Synonyms=Gm323;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the TMEM151 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC079879; AAH79879.1; -; mRNA.
DR   EMBL; BC083182; AAH83182.1; -; mRNA.
DR   IPI; IPI00470983; -.
DR   RefSeq; NP_001013771.1; NM_001013749.2.
DR   UniGene; Mm.329064; -.
DR   UniGene; Mm.480666; -.
DR   ProteinModelPortal; Q68FE7; -.
DR   PRIDE; Q68FE7; -.
DR   Ensembl; ENSMUST00000052694; ENSMUSP00000059332; ENSMUSG00000050405.
DR   GeneID; 210573; -.
DR   KEGG; mmu:210573; -.
DR   CTD; 210573; -.
DR   MGI; MGI:2685169; Tmem151b.
DR   GeneTree; ENSGT00390000013762; -.
DR   HOGENOM; HBG444651; -.
DR   HOVERGEN; HBG108535; -.
DR   InParanoid; Q68FE7; -.
DR   OMA; APSCRYG; -.
DR   OrthoDB; EOG45756K; -.
DR   NextBio; 373002; -.
DR   ArrayExpress; Q68FE7; -.
DR   Bgee; Q68FE7; -.
DR   CleanEx; MM_TMEM151B; -.
DR   Genevestigator; Q68FE7; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    561       Transmembrane protein 151B.
FT                                /FTId=PRO_0000307221.
FT   TRANSMEM     59     79       Helical; (Potential).
FT   TRANSMEM    106    126       Helical; (Potential).
FT   COMPBIAS     13     22       Poly-Gly.
FT   COMPBIAS    435    438       Poly-Ser.
FT   COMPBIAS    521    524       Poly-Pro.
SQ   SEQUENCE   561 AA;  61706 MW;  0F92F03E661ECF1D CRC64;
     MSPPGSAAGE SAGGGGGGGG SGVPEEPMAS ADEGPAREEQ RPIQPSFTKS LCRESHWKCL
     LLSLLMYGCL GAVAWCHVTT VTRLTFSSAY QGNSLMYHDS PCSNGYVYIP LAFLLMLYAV
     YLVECWHCQA RHELQHRVDV SSVQERVGRM QQATPCIWWK AISYHYVRRT RQVTRYRNGD
     AYTTTQVYHE RVNTHVAEAE FDYARCGVRD VSKTLVGLEG APATRLRFTK CFSFASVEAE
     NAYLCQRARF FAENEGLDDY MEAREGMHLK NVDFREFMVA FPDPARPPWY ACSSAFWAAA
     LLTLSWPLRV LAEYRTAYAH YHVEKLFGLE GPGSASSVGG GLSPSDELLP PLTHRLPRVN
     TVDSTELEWH IRSNQQLVPS YSEVLLMDLV ELGSRCGGPG GSYVPRCRYG GVGGPGAAGV
     TPHWRSCEHC QRAVSSSSIF SRSALSICAS PRAAQGPGAS AGCGGSRFSL SRLYGSRRSC
     LWRSRSGSVN EASCPTEQTR LSSQASMRDN EEDEDEEEAG PPPPYQDALC FPVLIVHRQE
     GCLGHSHRSL HRHGSCVETS L
//
ID   GIT1_MOUSE              Reviewed;         770 AA.
AC   Q68FF6;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=ARF GTPase-activating protein GIT1;
DE            Short=ARF GAP GIT1;
DE   AltName: Full=G protein-coupled receptor kinase-interactor 1;
DE   AltName: Full=GRK-interacting protein 1;
GN   Name=Git1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH TGFB1I1.
RX   PubMed=12153727;
RA   Nishiya N., Shirai T., Suzuki W., Nose K.;
RT   "Hic-5 interacts with GIT1 with a different binding mode from
RT   paxillin.";
RL   J. Biochem. 132:279-289(2002).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-224, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-371 AND
RP   SER-394, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397; SER-517 AND
RP   SER-601, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-554, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: GTPase-activating protein for the ADP ribosylation
CC       factor family. May serve as a scaffold to bring together molecules
CC       to form signaling modules controlling vesicle trafficking,
CC       adhesion and cytoskeletal organization. Increases the speed of
CC       cell migration, as well as the size and rate of formation of
CC       protrusions, possibly by targeting PAK1 to adhesions and the
CC       leading edge of lamellipodia. Sequesters inactive non-tyrosine-
CC       phosphorylated paxillin in cytoplasmic complexes (By similarity).
CC   -!- SUBUNIT: Interacts with G protein-coupled receptor kinases:
CC       ADRBK1/GRK2, PPFIA1 and PPFIA4, with ARHGEF6/alpha-PIX, with
CC       ARHGEF7/beta-PIX, with PXN/paxillin and with PTK2/FAK. Component
CC       of cytoplasmic complexes, which also contain PXN, ARHGEF6 and
CC       PAK1. Interacts with SCRIB (By similarity). Interacts with
CC       TGFB1I1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=Cycles
CC       between at least 3 distinct intracellular compartments, including
CC       focal adhesions, cytoplasmic complexes and membrane protrusions.
CC       During cell migration, when cells detach, moves from the adhesions
CC       into the cytoplasmic complexes towards the leading edge, while,
CC       when cells adhere, it is found in vinculin-containing adhesions.
CC       Recruitment to adhesions may be mediated by active tyrosine-
CC       phosphorylated paxillin (By similarity).
CC   -!- PTM: Phosphorylated on tyrosine residues by PTK2 and SRC in
CC       growing fibroblasts. Tyrosine-phosphorylation is increased
CC       following cell spreading on fibronectin, decreased in cells
CC       arrested in mitosis and increased in the ensuing G1 phase (By
CC       similarity).
CC   -!- SIMILARITY: Contains 3 ANK repeats.
CC   -!- SIMILARITY: Contains 1 Arf-GAP domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AL607072; CAI52039.1; -; Genomic_DNA.
DR   EMBL; BC079870; AAH79870.1; -; mRNA.
DR   IPI; IPI00470095; -.
DR   RefSeq; NP_001004144.1; NM_001004144.1.
DR   UniGene; Mm.290182; -.
DR   ProteinModelPortal; Q68FF6; -.
DR   SMR; Q68FF6; 3-227, 427-482, 640-770.
DR   IntAct; Q68FF6; 3.
DR   STRING; Q68FF6; -.
DR   PRIDE; Q68FF6; -.
DR   Ensembl; ENSMUST00000037285; ENSMUSP00000037210; ENSMUSG00000011877.
DR   GeneID; 216963; -.
DR   KEGG; mmu:216963; -.
DR   UCSC; uc007kgy.1; mouse.
DR   CTD; 216963; -.
DR   MGI; MGI:1927140; Git1.
DR   GeneTree; ENSGT00600000084201; -.
DR   HOGENOM; HBG358249; -.
DR   HOVERGEN; HBG012506; -.
DR   InParanoid; Q68FF6; -.
DR   OMA; QSGDPLL; -.
DR   OrthoDB; EOG4GTKCB; -.
DR   PhylomeDB; Q68FF6; -.
DR   NextBio; 375468; -.
DR   ArrayExpress; Q68FF6; -.
DR   Bgee; Q68FF6; -.
DR   CleanEx; MM_GIT1; -.
DR   Genevestigator; Q68FF6; -.
DR   GermOnline; ENSMUSG00000011877; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR001164; ArfGAP.
DR   InterPro; IPR022018; GIT1_C.
DR   InterPro; IPR013724; GIT_SHD.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 2.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF12205; GIT1_C; 1.
DR   Pfam; PF08518; GIT_SHD; 2.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00555; GIT; 2.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF57863; ArfGAP; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Cytoplasm; GTPase activation; Metal-binding;
KW   Phosphoprotein; Repeat; Zinc; Zinc-finger.
FT   CHAIN         1    770       ARF GTPase-activating protein GIT1.
FT                                /FTId=PRO_0000074201.
FT   DOMAIN        1    124       Arf-GAP.
FT   REPEAT      132    161       ANK 1.
FT   REPEAT      166    195       ANK 2.
FT   REPEAT      199    228       ANK 3.
FT   ZN_FING      11     34       C4-type.
FT   REGION      253    424       PTK2-binding (By similarity).
FT   REGION      254    376       ARHGEF6-binding (By similarity).
FT   REGION      646    770       Interaction with PXN and TGFB1I1 (By
FT                                similarity).
FT   MOD_RES     134    134       Phosphoserine (By similarity).
FT   MOD_RES     224    224       Phosphotyrosine.
FT   MOD_RES     370    370       Phosphoserine.
FT   MOD_RES     371    371       Phosphoserine.
FT   MOD_RES     373    373       Phosphothreonine (By similarity).
FT   MOD_RES     382    382       Phosphoserine (By similarity).
FT   MOD_RES     384    384       Phosphoserine (By similarity).
FT   MOD_RES     392    392       Phosphotyrosine (By similarity).
FT   MOD_RES     394    394       Phosphoserine.
FT   MOD_RES     397    397       Phosphoserine.
FT   MOD_RES     401    401       Phosphothreonine (By similarity).
FT   MOD_RES     419    419       Phosphoserine (By similarity).
FT   MOD_RES     517    517       Phosphoserine.
FT   MOD_RES     554    554       Phosphotyrosine.
FT   MOD_RES     563    563       Phosphotyrosine (By similarity).
FT   MOD_RES     570    570       Phosphoserine (By similarity).
FT   MOD_RES     601    601       Phosphoserine.
FT   MOD_RES     605    605       Phosphoserine (By similarity).
FT   MOD_RES     607    607       Phosphotyrosine (By similarity).
FT   MOD_RES     610    610       Phosphothreonine (By similarity).
SQ   SEQUENCE   770 AA;  85300 MW;  C516E7A49578D0B4 CRC64;
     MSRKGPRAEV CADCSAPDPG WASISRGVLV CDECCSVHRS LGRHISIVKH LRHSAWPPTL
     LQMVHTLASN GANSIWEHSL LDPAQVQSGR RKANPQDKVH PIKSEFIRAK YQMLAFVHKL
     PCRDDDGVTA KDLSKQLHSS VRTGNLETCL RLLSLGAQAN FFHPEKGTTP LHVAAKAGQT
     LQAELLVVYG ADPGSPDVNG RTPIDYARQA GHHELAERLV ECQYELTDRL AFYLCGRKPD
     HKNGHYIIPQ MADRSRQKCM SQSLDLSELA KAAKKKLQAL SNRLFEELAM DVYDEVDRRE
     NDAVWLATQN HSTLVTERSA VPFLPVNPEY SATRNQGRQK LARFNAREFA TLIIDILSEA
     KRRQQGKSLS SPTDNLELSA RSQSELDDQH DYDSVASDED TDQEPLPSAG ATRNNRARSM
     DSSDLSDGAV TLQEYLELKK ALATSEAKVQ QLMKVNSSLS DELRRLQREI HKLQAENLQL
     RQPPGPVPPP SLPSERAEHT LMGPGGSTHR RDRQAFSMYE PGSALKPFGG TPGDELATRL
     QPFHSTELED DAIYSVHVPA GLYRIRKGVS ASSVPFTPSS PLLSCSQEGS RHASKLSRHG
     SGADSDYENT QSGDPLLGLE GKRFLELSKE DELHPELESL DGDLDPGLPS TEDVILKTEQ
     VTKNIQELLR AAQEFKHDSF VPCSEKIHLA VTEMASLFPK RPALEPVRSS LRLLNASAYR
     LQSECRKTVP PEPGAPVDFQ LLTQQVIQCA YDIAKAAKQL VTITTREKKQ
//
ID   SLAI1_MOUSE             Reviewed;         579 AA.
AC   Q68FF7; Q8R3I6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=SLAIN motif-containing protein 1;
GN   Name=Slain1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and FVB/N-3; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   IDENTIFICATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=16546155; DOI=10.1016/j.ydbio.2006.01.023;
RA   Hirst C.E., Ng E.S., Azzola L., Voss A.K., Thomas T., Stanley E.G.,
RA   Elefanty A.G.;
RT   "Transcriptional profiling of mouse and human ES cells identifies
RT   SLAIN1, a novel stem cell gene.";
RL   Dev. Biol. 293:90-103(2006).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q68FF7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q68FF7-2; Sequence=VSP_030833;
CC   -!- TISSUE SPECIFICITY: Expressed in embryonic stem cells. Expressed
CC       in adult bone marrow, brain, kidney, lung, testis and thymus.
CC   -!- DEVELOPMENTAL STAGE: During embryonic stem cell differentiation,
CC       expression peaks at d2 and d3 (epiblast stage). In
CC       postimplantation embryos widely expressed throughout E6.5-E7.0,
CC       followed by higher levels of expression in the headfold
CC       neurectoderm at E7.5. Observed in the neural tube and optic
CC       vesicles at E8.5 and at sites of imminent neural tube closure in
CC       the midbrain, hindbrain, and tailbud at E9.0-E9.5 and in the
CC       dorsal aspects of the somites.
CC   -!- SIMILARITY: Belongs to the SLAIN motif-containing family.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC025223; AAH25223.1; -; mRNA.
DR   EMBL; BC079866; AAH79866.1; -; mRNA.
DR   IPI; IPI00153764; -.
DR   IPI; IPI00885674; -.
DR   RefSeq; NP_932131.2; NM_198014.2.
DR   UniGene; Mm.27548; -.
DR   ProteinModelPortal; Q68FF7; -.
DR   STRING; Q68FF7; -.
DR   PhosphoSite; Q68FF7; -.
DR   PRIDE; Q68FF7; -.
DR   Ensembl; ENSMUST00000069443; ENSMUSP00000070592; ENSMUSG00000055717.
DR   GeneID; 105439; -.
DR   KEGG; mmu:105439; -.
DR   UCSC; uc007uws.1; mouse.
DR   CTD; 105439; -.
DR   MGI; MGI:2145578; Slain1.
DR   eggNOG; roNOG05715; -.
DR   GeneTree; ENSGT00390000017860; -.
DR   HOGENOM; HBG506689; -.
DR   HOVERGEN; HBG072961; -.
DR   InParanoid; Q68FF7; -.
DR   OMA; EDDYTWL; -.
DR   OrthoDB; EOG4933JK; -.
DR   PhylomeDB; Q68FF7; -.
DR   NextBio; 357702; -.
DR   ArrayExpress; Q68FF7; -.
DR   Bgee; Q68FF7; -.
DR   CleanEx; MM_SLAIN1; -.
DR   Genevestigator; Q68FF7; -.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil.
FT   CHAIN         1    579       SLAIN motif-containing protein 1.
FT                                /FTId=PRO_0000316963.
FT   COILED       21     56       Potential.
FT   COMPBIAS     64    160       Pro-rich.
FT   VAR_SEQ       1    261       Missing (in isoform 2).
FT                                /FTId=VSP_030833.
SQ   SEQUENCE   579 AA;  61307 MW;  41D009ADAA1C6439 CRC64;
     MMAEQVKCAS PVAASGAGPG PVVNAELEVK KLQELVRKLE KQNEQLRSRA ASAAAAPHLL
     LLQPPPPSAP PPAGACSPLA THRAPASTTS PGPGALGPAF PGTYCLPSPA PSLLCSLQPA
     DAPFVYSKPA AGFFGGGGSP EPGTAGTPPG EAATPPLPPP TLLDEVEPLD LESLAAWSEE
     DDYTWLYVGS SKTFTSPEKS PSPLQWCRHV LDNPTPEMEA ARRSLRFRLE QGYTSRGSPL
     SPQSSIDSEL STSELEDDSI SMGYKLQDLT DVQIMARLQE ESLRQDYAST SASVSRNSSS
     VSLSSGKKGT CSDQEYDRYS LEDEEEFDHL PPPQPRLPRC SPFQRGIPHS QTFSSIRDCR
     RSPSTQYFPS NNFQQPQYYP PQAQTADQQP NRTNGDKLRR SMPNLARMPS TAAASSNLSS
     PVTVRSSQSF DSSLHGAGSG VSRVPSCIPS PGQIQHRVHS VGHFPVPIRQ PLKATAYVSP
     TVQGSSSSGS SGSSGGSGSG MPLSNGTQLY STTGIPTPNK AAASGILGRS ALPRPSLAIN
     GSNLPRSKIA QPVRSFLQPP KPLSSLSTLR DGNWRDGCY
//
ID   PKP4_MOUSE              Reviewed;        1190 AA.
AC   Q68FH0; A2AS46; Q640N0; Q68G56; Q8BK47; Q8BVH1; Q9CRE3;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Plakophilin-4;
DE   AltName: Full=Armadillo-related protein;
GN   Name=Pkp4; Synonyms=Armrp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and Czech II; TISSUE=Brain, Eye, and Mammary cancer;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 747-1190 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb, Ovary, and Uterus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509; SER-511; SER-514;
RP   SER-1047 AND SER-1048, AND MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289; SER-313; SER-405;
RP   SER-421 AND SER-1133, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-371 AND TYR-477, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; THR-225; SER-230;
RP   SER-232; SER-313; SER-335; SER-336; SER-405 AND SER-1136, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-272; TYR-274;
RP   SER-280 AND SER-446, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May play a role in junctional plaques.
CC   -!- SUBUNIT: Interacts (via the C-terminus) with FRMPD2 (via the PDZ 2
CC       domain). Interacts with PDZD2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, desmosome (By similarity).
CC       Note=Colocalized with desmoplakin at desmosomal junctional plaques
CC       in cultured epithelial cells (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q68FH0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q68FH0-2; Sequence=VSP_012377;
CC       Name=3;
CC         IsoId=Q68FH0-3; Sequence=VSP_012374, VSP_012375, VSP_012376;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the beta-catenin family.
CC   -!- SIMILARITY: Contains 4 ARM repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC37187.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC   -----------------------------------------------------------------------
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DR   EMBL; AL845536; CAM20481.1; -; Genomic_DNA.
DR   EMBL; BC078638; AAH78638.1; -; mRNA.
DR   EMBL; BC079848; AAH79848.1; -; mRNA.
DR   EMBL; BC082578; AAH82578.1; -; mRNA.
DR   EMBL; AK021168; BAB32313.1; -; mRNA.
DR   EMBL; AK077250; BAC36708.1; -; mRNA.
DR   EMBL; AK078240; BAC37187.1; ALT_INIT; mRNA.
DR   IPI; IPI00473693; -.
DR   IPI; IPI00515280; -.
DR   IPI; IPI00757327; -.
DR   RefSeq; NP_080637.1; NM_026361.2.
DR   RefSeq; NP_780673.2; NM_175464.2.
DR   UniGene; Mm.260938; -.
DR   ProteinModelPortal; Q68FH0; -.
DR   SMR; Q68FH0; 519-1012.
DR   STRING; Q68FH0; -.
DR   PhosphoSite; Q68FH0; -.
DR   PRIDE; Q68FH0; -.
DR   Ensembl; ENSMUST00000037903; ENSMUSP00000042249; ENSMUSG00000026991.
DR   Ensembl; ENSMUST00000102754; ENSMUSP00000099815; ENSMUSG00000026991.
DR   GeneID; 227937; -.
DR   KEGG; mmu:227937; -.
DR   UCSC; uc008jtc.1; mouse.
DR   UCSC; uc008jtd.1; mouse.
DR   UCSC; uc008jtg.1; mouse.
DR   CTD; 227937; -.
DR   MGI; MGI:109281; Pkp4.
DR   GeneTree; ENSGT00550000074290; -.
DR   HOGENOM; HBG446569; -.
DR   HOVERGEN; HBG004284; -.
DR   InParanoid; Q68FH0; -.
DR   OMA; HFITPVS; -.
DR   OrthoDB; EOG46WZ7J; -.
DR   NextBio; 378870; -.
DR   ArrayExpress; Q68FH0; -.
DR   Bgee; Q68FH0; -.
DR   CleanEx; MM_PKP4; -.
DR   Genevestigator; Q68FH0; -.
DR   GermOnline; ENSMUSG00000026991; Mus musculus.
DR   GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF00514; Arm; 3.
DR   SMART; SM00185; ARM; 6.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell adhesion; Cell junction;
KW   Coiled coil; Isopeptide bond; Phosphoprotein; Repeat; Ubl conjugation.
FT   CHAIN         1   1190       Plakophilin-4.
FT                                /FTId=PRO_0000064290.
FT   REPEAT      517    556       ARM 1.
FT   REPEAT      559    598       ARM 2.
FT   REPEAT      603    643       ARM 3.
FT   REPEAT      861    900       ARM 4.
FT   COILED       36     63       Potential.
FT   COMPBIAS    787    793       Poly-Lys.
FT   MOD_RES      75     75       Phosphoserine (By similarity).
FT   MOD_RES     132    132       Phosphoserine.
FT   MOD_RES     220    220       Phosphoserine.
FT   MOD_RES     225    225       Phosphothreonine.
FT   MOD_RES     230    230       Phosphoserine.
FT   MOD_RES     232    232       Phosphoserine.
FT   MOD_RES     272    272       Phosphoserine.
FT   MOD_RES     274    274       Phosphotyrosine.
FT   MOD_RES     280    280       Phosphoserine.
FT   MOD_RES     289    289       Phosphoserine.
FT   MOD_RES     313    313       Phosphoserine.
FT   MOD_RES     326    326       Phosphoserine (By similarity).
FT   MOD_RES     335    335       Phosphoserine.
FT   MOD_RES     336    336       Phosphoserine.
FT   MOD_RES     371    371       Phosphotyrosine.
FT   MOD_RES     389    389       Phosphotyrosine (By similarity).
FT   MOD_RES     391    391       Phosphoserine (By similarity).
FT   MOD_RES     402    402       Phosphoserine (By similarity).
FT   MOD_RES     405    405       Phosphoserine.
FT   MOD_RES     414    414       Phosphotyrosine (By similarity).
FT   MOD_RES     419    419       Phosphotyrosine (By similarity).
FT   MOD_RES     421    421       Phosphoserine.
FT   MOD_RES     437    437       Phosphoserine (By similarity).
FT   MOD_RES     446    446       Phosphoserine.
FT   MOD_RES     469    469       Phosphotyrosine (By similarity).
FT   MOD_RES     477    477       Phosphotyrosine.
FT   MOD_RES     481    481       Phosphotyrosine (By similarity).
FT   MOD_RES     509    509       Phosphoserine.
FT   MOD_RES     511    511       Phosphoserine.
FT   MOD_RES     514    514       Phosphoserine.
FT   MOD_RES     624    624       N6-acetyllysine (By similarity).
FT   MOD_RES     775    775       Phosphoserine (By similarity).
FT   MOD_RES    1016   1016       Phosphothreonine (By similarity).
FT   MOD_RES    1047   1047       Phosphoserine.
FT   MOD_RES    1048   1048       Phosphoserine.
FT   MOD_RES    1133   1133       Phosphoserine.
FT   MOD_RES    1136   1136       Phosphoserine.
FT   MOD_RES    1166   1166       Phosphotyrosine (By similarity).
FT   CROSSLNK    610    610       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   VAR_SEQ       1    341       Missing (in isoform 3).
FT                                /FTId=VSP_012374.
FT   VAR_SEQ     637    637       V -> G (in isoform 3).
FT                                /FTId=VSP_012375.
FT   VAR_SEQ     638   1190       Missing (in isoform 3).
FT                                /FTId=VSP_012376.
FT   VAR_SEQ    1042   1084       Missing (in isoform 2).
FT                                /FTId=VSP_012377.
FT   CONFLICT    328    328       S -> F (in Ref. 2; AAH78638).
FT   CONFLICT    877    877       V -> A (in Ref. 3; BAC36708).
FT   CONFLICT   1118   1118       D -> G (in Ref. 3; BAC36708).
FT   CONFLICT   1161   1161       K -> R (in Ref. 3; BAB32313).
SQ   SEQUENCE   1190 AA;  131551 MW;  DB6548B5EBE72CFE CRC64;
     MPAPEQGSLV EEGQPQTHQE AVSTGPGMEP ETTATTILAS VKEQELQFQR LTRELEVERQ
     IVASQLERCR LGAESPSIAS TSSTEKSFPW RSTDVPNPGV SKPRVSDTIH PNNYLIRTEP
     EQGTLYSPEQ TSLHESEGSL GNSRSSTQMN SYSDSGYQEA GSFHNSQTVN KADSRQHPFT
     GSTSNHVVRT SRAEGQTLVQ PSVANRAMRR VSSVPSRAQS PSYVTSTGVS PSRGSLRTSL
     GSGFGSPSVT DSRPLNPSAY SSSTLPAQRA ASPYSQRPAS PTAVRRVGSV TSRQTSNPNG
     PVPQYQTTTR VGSPLTLTDA QTRVASPSQG QVGSSSPKRS GMTAVPQHLG PSLQRTVHDM
     DQFGQQQYDI YERMVPPRPD SLTGLRSSYA SQHSQLGQEL RSAVSPDLHI TPIYEGRTYY
     SPVYRSPNHG TVELQGSQTA LYRTGSVGIG NLQRTSSQRS TLTYQRNNYA LNTAATYAEP
     YRPVQYRVQE CSYNRLQHTG PADDGATRSP SIDSIQKDPR EFAWRDPELP EVIHMLQHQF
     PSVQANAAAY LQHLCFGDNK VKMEVYRLGG IKHLVDLLDH RVLEVQKNAC GALRNLVFGK
     STDENKIAMK NVGGIPALLR LLRKSIDAEV RELVTGVLWN LSSCDAVKMT IIRDALSTLT
     NTVIVPHSGW NNSSFDDDHK IKFQTSLVLR NTTGCLRNLS SAGEEARKQM RSCEGLVDSL
     LYVIHTCVNT SDYDSKTVEN CVCTLRNLSY RLELEVPQAR LLGLNELDDL LGKESPSKDS
     EPSCWGKKKK KKKRTPQEDQ WDGVGPIPGL SKSPKGVEML WHPSVVKPYL TLLAESSNPA
     TLEGSAGSLQ NLSAGNWKFA AYIRAAVRKE KGLPILVELL RMDNDRVVSS VATALRNMAL
     DVRNKELIGK YAMRDLVNRL PGGNGPSILS DETVAAICCA LHEVTSKNME NAKALADSGG
     IEKLVNITKG RGDRSSLKVV KAAAQVLNTL WQYRDLRSIY KKDGWNQNHF ITPVSTLERD
     RFKSHPSLST TNQQMSPIIQ SVGSTSSSPA LLGIREPRSE YDRTQPPMQY YNSQGDTTHK
     GLYPGSSKPS PIYISSYSSP AREQNRRLQH QQLYYQDDST RKTLDAYRLY LQSPRSYEDP
     YCDDRVHFPA STDYSTQYGL KSTTNYVDFY STKRPSYRAE QYPGSPDSWV
//
ID   SAHH3_MOUSE             Reviewed;         613 AA.
AC   Q68FL4; Q8BIH1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Putative adenosylhomocysteinase 3;
DE            Short=AdoHcyase 3;
DE            EC=3.3.1.1;
DE   AltName: Full=S-adenosyl-L-homocysteine hydrolase 3;
DE   AltName: Full=S-adenosylhomocysteine hydrolase-like protein 2;
GN   Name=Ahcyl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-homocysteine + H(2)O = L-
CC       homocysteine + adenosine.
CC   -!- COFACTOR: Binds 1 NAD per subunit (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC       homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q68FL4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q68FL4-2; Sequence=VSP_017821;
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
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DR   EMBL; AK053527; BAC35415.1; -; mRNA.
DR   EMBL; BC079660; AAH79660.1; -; mRNA.
DR   IPI; IPI00308446; -.
DR   IPI; IPI00742293; -.
DR   RefSeq; NP_001164471.1; NM_001171000.1.
DR   RefSeq; NP_001164472.1; NM_001171001.1.
DR   RefSeq; NP_067389.4; NM_021414.5.
DR   UniGene; Mm.210899; -.
DR   UniGene; Mm.446883; -.
DR   ProteinModelPortal; Q68FL4; -.
DR   SMR; Q68FL4; 178-609.
DR   STRING; Q68FL4; -.
DR   PhosphoSite; Q68FL4; -.
DR   PRIDE; Q68FL4; -.
DR   Ensembl; ENSMUST00000115238; ENSMUSP00000110893; ENSMUSG00000029772.
DR   Ensembl; ENSMUST00000115242; ENSMUSP00000110897; ENSMUSG00000029772.
DR   GeneID; 74340; -.
DR   KEGG; mmu:74340; -.
DR   UCSC; uc009bei.1; mouse.
DR   UCSC; uc009bek.1; mouse.
DR   CTD; 74340; -.
DR   MGI; MGI:1921590; Ahcyl2.
DR   HOGENOM; HBG352029; -.
DR   HOVERGEN; HBG005041; -.
DR   InParanoid; Q68FL4; -.
DR   OMA; NTEIDVN; -.
DR   OrthoDB; EOG4GMTWR; -.
DR   PhylomeDB; Q68FL4; -.
DR   BRENDA; 3.3.1.1; 244.
DR   NextBio; 340487; -.
DR   ArrayExpress; Q68FL4; -.
DR   Bgee; Q68FL4; -.
DR   CleanEx; MM_AHCYL2; -.
DR   Genevestigator; Q68FL4; -.
DR   GermOnline; ENSMUSG00000029772; Mus musculus.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:EC.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000043; Adenosylhomocysteinase.
DR   InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR   InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
DR   PANTHER; PTHR23420; Ad_hcy_hydrolase; 1.
DR   Pfam; PF05221; AdoHcyase; 1.
DR   Pfam; PF00670; AdoHcyase_NAD; 1.
DR   TIGRFAMs; TIGR00936; ahcY; 1.
DR   PROSITE; PS00738; ADOHCYASE_1; 1.
DR   PROSITE; PS00739; ADOHCYASE_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; NAD; One-carbon metabolism;
KW   Phosphoprotein.
FT   CHAIN         1    613       Putative adenosylhomocysteinase 3.
FT                                /FTId=PRO_0000230301.
FT   NP_BIND     338    340       NAD (By similarity).
FT   NP_BIND     403    408       NAD (By similarity).
FT   NP_BIND     480    482       NAD (By similarity).
FT   BINDING     238    238       Substrate (By similarity).
FT   BINDING     312    312       Substrate (By similarity).
FT   BINDING     337    337       Substrate (By similarity).
FT   BINDING     367    367       Substrate (By similarity).
FT   BINDING     371    371       Substrate (By similarity).
FT   BINDING     372    372       NAD (By similarity).
FT   BINDING     424    424       NAD (By similarity).
FT   BINDING     459    459       NAD (By similarity).
FT   BINDING     527    527       NAD (By similarity).
FT   MOD_RES     109    109       Phosphoserine.
FT   VAR_SEQ       1    123       MSVQVVSAAAAAKVPEVELKDLSPSEAEPQLGLSAAAVGAM
FT                                VPPAGGGDPEAPAPAPAAERPPAPGPGSGPTAALSPAAGKV
FT                                PQASAMKRSDPHHQHQRHRDGGEALVSPDGTVTEAPRTVKK
FT                                -> MLSSKKKYIVNSNSGIKA (in isoform 2).
FT                                /FTId=VSP_017821.
FT   CONFLICT    440    440       L -> V (in Ref. 1; BAC35415).
SQ   SEQUENCE   613 AA;  66899 MW;  4413DBF1F4825860 CRC64;
     MSVQVVSAAA AAKVPEVELK DLSPSEAEPQ LGLSAAAVGA MVPPAGGGDP EAPAPAPAAE
     RPPAPGPGSG PTAALSPAAG KVPQASAMKR SDPHHQHQRH RDGGEALVSP DGTVTEAPRT
     VKKQIQFADQ KQEFNKRPTK IGRRSLSRSI SQSSTDSYSS AASYTDSSDD ETSPRDKQQK
     NSKGSSDFCV KNIKQAEFGR REIEIAEQEM PALMALRKRA QGEKPLAGAK IVGCTHITAQ
     TAVLMETLGA LGAQCRWAAC NIYSTLNEVA AALAESGFPV FAWKGESEDD FWWCIDRCVN
     VEGWQPNMIL DDGGDLTHWI YKKYPNMFKK IKGIVEESVT GVHRLYQLSK AGKLCVPAMN
     VNDSVTKQKF DNLYCCRESI LDGLKRTTDM MFGGKQVVVC GYGEVGKGCC AALKAMGSIV
     YVTEIDPICA LQACMDGFRL VKLNEVIRQV DIVITCTGNK NVVTREHLDR MKNSCIVCNM
     GHSNTEIDVA SLRTPELTWE RVRSQVDHVI WPDGKRIVLL AEGRLLNLSC STVPTFVLSI
     TATTQALALI ELYNAPEGRY KQDVYLLPKK MDEYVASLHL PTFDAHLTEL TDEQAKYLGL
     NKNGPFKPNY YRY
//
ID   LRFN6_MOUSE             Reviewed;         823 AA.
AC   Q68FM6; Q69Z72; Q8CCW8;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Leucine-rich repeat and fibronectin type-III domain-containing protein 6;
DE   AltName: Full=Extracellular leucine-rich repeat and fibronectin type III domain-containing protein 2;
DE   AltName: Full=Leucine-rich repeat-containing protein 62;
DE   Flags: Precursor;
GN   Name=Elfn2; Synonyms=Kiaa1904, Lrrc62;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 339-823.
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-622, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-622, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC   -!- SIMILARITY: Contains 5 LRR (leucine-rich) repeats.
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DR   EMBL; AK031970; BAC27630.1; -; mRNA.
DR   EMBL; BC079588; AAH79588.1; -; mRNA.
DR   EMBL; BC094219; AAH94219.1; -; mRNA.
DR   EMBL; AK173294; BAD32572.1; -; mRNA.
DR   IPI; IPI00471006; -.
DR   RefSeq; NP_898964.2; NM_183141.2.
DR   UniGene; Mm.323188; -.
DR   HSSP; P24014; 1W8A.
DR   ProteinModelPortal; Q68FM6; -.
DR   SMR; Q68FM6; 11-232.
DR   PhosphoSite; Q68FM6; -.
DR   PRIDE; Q68FM6; -.
DR   Ensembl; ENSMUST00000088592; ENSMUSP00000085960; ENSMUSG00000043460.
DR   GeneID; 207393; -.
DR   KEGG; mmu:207393; -.
DR   NMPDR; fig|10090.3.peg.30222; -.
DR   UCSC; uc007wrf.1; mouse.
DR   CTD; 207393; -.
DR   MGI; MGI:3608416; Elfn2.
DR   eggNOG; roNOG04739; -.
DR   GeneTree; ENSGT00550000074348; -.
DR   HOGENOM; HBG446203; -.
DR   HOVERGEN; HBG056941; -.
DR   InParanoid; Q68FM6; -.
DR   OMA; AFSECPS; -.
DR   OrthoDB; EOG4SXNC1; -.
DR   PhylomeDB; Q68FM6; -.
DR   NextBio; 371941; -.
DR   ArrayExpress; Q68FM6; -.
DR   Bgee; Q68FM6; -.
DR   Genevestigator; Q68FM6; -.
DR   GermOnline; ENSMUSG00000043460; Mus musculus.
DR   GO; GO:0009986; C:cell surface; IEA:InterPro.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR001899; Surface_protein_Gram_pos_cocci.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00082; LRRCT; 1.
DR   PROSITE; PS50853; FN3; FALSE_NEG.
DR   PROSITE; PS51450; LRR; 4.
PE   1: Evidence at protein level;
KW   Glycoprotein; Leucine-rich repeat; Membrane; Phosphoprotein; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     22       Potential.
FT   CHAIN        23    823       Leucine-rich repeat and fibronectin type-
FT                                III domain-containing protein 6.
FT                                /FTId=PRO_0000256139.
FT   TOPO_DOM     23    397       Extracellular (Potential).
FT   TRANSMEM    398    418       Helical; (Potential).
FT   TOPO_DOM    419    823       Cytoplasmic (Potential).
FT   REPEAT       54     77       LRR 1.
FT   REPEAT       78    101       LRR 2.
FT   REPEAT      103    125       LRR 3.
FT   REPEAT      127    149       LRR 4.
FT   REPEAT      150    173       LRR 5.
FT   DOMAIN      292    379       Fibronectin type-III.
FT   COMPBIAS    564    573       Poly-Gly.
FT   COMPBIAS    692    696       Poly-Gly.
FT   MOD_RES     475    475       Phosphoserine.
FT   MOD_RES     622    622       Phosphoserine.
FT   CARBOHYD     54     54       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     80     80       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     85     85       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    117    117       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    205    205       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    247    247       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    749    749       L -> P (in Ref. 1; BAC27630).
SQ   SEQUENCE   823 AA;  90029 MW;  B8CC92E32D1AC4D7 CRC64;
     MLRLGLCAAA LLCVCQPGAV RADCWLIEGD KGYVWLAICS QNQPPYETIP QHINSTVHDL
     RLNENKLKAV LYSSLNRFGN LTDLNLTKNE ISYIEDGAFL GQTSLQVLQL GYNRLSNLTE
     GMLRGMSRLQ FLFVQHNLIE VVTPTAFSEC PSLISIDLSS NRLSRLDGAT FASLASLMVC
     ELAGNPFNCE CDLFGFLAWL VVFNNVTKNY DRLQCESPRE FAGYPLLVPR PYHSLNAITV
     LQAKCRNGSM PARPVSHPTP YSTDAQREPD ENSGFNPDEI LSVEPPASST TDASAGPAIK
     LHQVTFTSAT LVVIIPHPYS KMYVLVQYNN SYFSDVMTLK NKKEIVTLDK LRAHTEYTFC
     VTSLRNSRRF NHTCLTFTTR DLVPGDLAPS TSTTTHYIMT ILGCLFGMVI VLGAVYYCLR
     KRRMQEEKQK SVNVKKTILE MRYGADVDAG SIVHAAQKLG EPPVLPVARM SSIPSMVGEK
     LPASKGLEAG LDTPKVATKG NYIEVRTGAA GDSLARPEEE LPEIENGQGS AAEISTIAKE
     VDKVNQIINN CIDALKLDSA SFLGGGGGGG GGGDSDLAFE CQSLPAAPAA SSAATPGALE
     RPSFLSPPYK ESSHHPLQRQ LSADAAVSRK TCSVSSSGSI KSAKVFSLDV PDHPTPTGLA
     KSDSKYIEKG SPLNSPLDRL PLVPTGSSGS SGGGGGIHHL EVKPAYHCSE HRHSFPALYY
     EEGADSLSQR VSFLKPLTRS KRDSTYSQLS PRHYYSGYSS SPEYSSESTH KIWERFRPYK
     KHHREEVYMA AGHALRKKVQ FAKDEDLHDI LDYWKGVSAQ QKL
//
ID   Q68FM7_MOUSE            Unreviewed;      1552 AA.
AC   Q68FM7;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   SubName: Full=Rho guanine nucleotide exchange factor (GEF) 11;
GN   Name=Arhgef11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
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DR   EMBL; BC079565; AAH79565.1; -; mRNA.
DR   IPI; IPI00471007; -.
DR   RefSeq; NP_001003912.1; NM_001003912.1.
DR   UniGene; Mm.287267; -.
DR   ProteinModelPortal; Q68FM7; -.
DR   SMR; Q68FM7; 37-120, 346-527, 744-1111.
DR   IntAct; Q68FM7; 1.
DR   MINT; MINT-1791186; -.
DR   STRING; Q68FM7; -.
DR   PhosphoSite; Q68FM7; -.
DR   PRIDE; Q68FM7; -.
DR   Ensembl; ENSMUST00000039476; ENSMUSP00000039900; ENSMUSG00000041977.
DR   GeneID; 213498; -.
DR   KEGG; mmu:213498; -.
DR   UCSC; uc008psm.1; mouse.
DR   CTD; 213498; -.
DR   MGI; MGI:2441869; Arhgef11.
DR   GeneTree; ENSGT00600000084190; -.
DR   HOGENOM; HBG716584; -.
DR   HOVERGEN; HBG101340; -.
DR   InParanoid; Q68FM7; -.
DR   OMA; GNCFYVS; -.
DR   NextBio; 374013; -.
DR   ArrayExpress; Q68FM7; -.
DR   Bgee; Q68FM7; -.
DR   Genevestigator; Q68FM7; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000342; Regulat_G_prot_signal.
DR   InterPro; IPR015212; Regulat_G_prot_signal-like.
DR   InterPro; IPR016137; Regulat_G_prot_signal_superfam.
DR   InterPro; IPR015721; RhoGEF-like.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   PANTHER; PTHR22825; RhoGEF_like; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF09128; RGS-like; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00315; RGS; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF48097; Regulat_G_prot_signal_superfam; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   1: Evidence at protein level;
SQ   SEQUENCE   1552 AA;  171803 MW;  8FF6AFC41AD63258 CRC64;
     MSIRLPHSID RLSSLSSLGD STPERTSPSH HRQPSDTSET TGLVQRCVII QKDQHGFGFT
     VSGDRIVLVQ SVRPGGAAMR AGVKEGDRII KVNGTMVTNS SHLEVVKLIK SGAYVALTLL
     GSSPSSIGVS GLQQNPSLSG GPRVNPMIPP PPPPPPLPPP QHITGPKPLQ DPEVQKHATQ
     ILRNMLRQEE KELQRICEVY SRNPASLLEE QIEGARRRVT QLQLKIQQET GGLVDVLPLC
     GETSQRTCEG RLSVDSQEAD SGLDSGTERF PSISESLVNR NSVLSDPGLD SPQTSPVILA
     RVGQHHRRQG SDAAVHPLNH QGIDQSPKPL IIGPEEDYDP GYFNNESDII FQDLEKLKSH
     PAYLVVFLRY IFSQADPGPL LFYLCSEVYQ QTNPKDSRNL GKDIWNIFLE KNAPLRVKIP
     EMLQAEIDLR LRNSEDPRSA LYEAQEAVMP EIQEQINDYR SKRTLGLGSL YGENDLLDLD
     GDPLRERQMA EKQLAALGDI LSKYEEDRSA PMDFAVNTYM SHTGIRLRES RPSSTAEKTQ
     SAPDKDKWLP FFPKTKKSSN SKKEKDALED KKRNPILRYI GKPKSSSQSI KPGNVRNIIQ
     HFENSHQYDV PEPGTQRLST GSFPEDLLES DSSRSEIRLG RSESLKGREE MKRSRKAENV
     PRSRSDVDMD AAAEATRLHQ SASSSASSLS TRSLENPTPP FTPKMGRRSI ESPNLGFCTD
     VILPHLLEDD LGQLSDLEPE PEVQNWQHTV GKDVVANLTQ REIDRQEVIN ELFVTEASHL
     RTLRVLDLIF YQRMKKENLM PREELSRLFP NLPELIEIHN SWCEAMKKLR EEGPIIRDIS
     DLMLARFDGP AREELQQVAA QFCSYQSVAL ELIRTKQRKE SRFQLFMQEA ESHPQCRRLQ
     LRDLIISEMQ RLTKYPLLLE NIIKHTAGGT SEYEKLCRAR DQCREILKFV NEAVKQTENR
     HRLEGYQKRL DATALERASN PLAAEFKSLD LTTRKMIHEG PLTWRISKDK TLDLQVLLLE
     DLVVLLQRQE EKLLLKCHSK TAVGSSDSKQ TFSPVLKLNA VLIRSVATDK RAFFIICTSE
     LGPPQIYELV ALTSSDKNIW MELLEEAVQN ATKHPGDAPV LNHPSPPGSQ EPAYQGSTSS
     RVEVNDSEVY PTEREPKKPS EGPGPEQRGQ DKQLLAQEGP EQEEDAEELR ALPCPPPSLD
     GENRGIRTRD PVLLALTGPL LMEGLADAAL EDVENLRHLI LWSLLPGHTV KTQAAGEPED
     DLTPTPSVVS ITSHPWDPGS PGQAPAISDN TQFPRPEGSQ PEGEDVALCS LAHLPPRTRN
     SGIWDSPELD RNPAEEASSS EPAGSYKVVR KVSLLPGGGV GAAKVAGSNV TPALPESGQS
     ESELSEVEGG AQATGNCFYV SMPAEPLDSS TEPPGTPPSL SQCHSLPAWP TEPPQHRGVT
     GGQRSSLVLR DMGVIFHTIE QLTVKLHRLK DMELAHRELL NSLGGESSGG TTPVGSFHTE
     AARWTDYSLS PPAKEALTSD PQNNQEQGSY PEEGSDTPLE DSATDTASSP GP
//
ID   Q68G59_MOUSE            Unreviewed;      1209 AA.
AC   Q68G59;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   08-FEB-2011, entry version 34.
DE   SubName: Full=Nup98 protein;
DE   Flags: Fragment;
GN   Name=Nup98;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic Germ Cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC078630; AAH78630.1; -; mRNA.
DR   IPI; IPI00474558; -.
DR   UniGene; Mm.439800; -.
DR   ProteinModelPortal; Q68G59; -.
DR   STRING; Q68G59; -.
DR   MEROPS; S59.001; -.
DR   PRIDE; Q68G59; -.
DR   Ensembl; ENSMUST00000096648; ENSMUSP00000094405; ENSMUSG00000063550.
DR   UCSC; uc009iqx.1; mouse.
DR   MGI; MGI:109404; Nup98.
DR   GeneTree; ENSGT00550000074799; -.
DR   HOGENOM; HBG356898; -.
DR   HOVERGEN; HBG052702; -.
DR   InParanoid; Q68G59; -.
DR   ArrayExpress; Q68G59; -.
DR   Bgee; Q68G59; -.
DR   Genevestigator; Q68G59; -.
DR   GO; GO:0005643; C:nuclear pore; IEA:InterPro.
DR   GO; GO:0006810; P:transport; IEA:InterPro.
DR   InterPro; IPR021967; Nup96.
DR   InterPro; IPR007230; Peptidase_S59.
DR   Gene3D; G3DSA:3.30.1610.10; Peptidase_S59; 1.
DR   Pfam; PF04096; Nucleoporin2; 1.
DR   Pfam; PF12110; Nup96; 1.
DR   SUPFAM; SSF82215; Peptidase_S59; 1.
DR   PROSITE; PS51434; NUP_C; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   1209 AA;  136360 MW;  F8C93646CB05728A CRC64;
     SNLFSPVNHD SEDLASPSEY PENGERFSFL SKPVDENNQQ DGEDDSLVSR FYTNPIAKPI
     PQTPESVGNK NNSSSNVEDT IVALNMRAAL RNGLEGSSEE TSFHDESLQD DREEIENNAY
     HIHPAGIVLT KVGYYTIPSM DDLAKITNEK GECIVFDFTI GRKGYGSIYF EGDVNLTNLN
     LDDIVHIRRK EVIVYVDDNQ KPPVGEGLNR KAEVTLDGVW PTDKTSRCLI KSPDRLADIN
     YEGRLEAVSR KQGAQFKEYR PETGSWVFKV SHFSKYGLQD SDEEEEEHPP KTTSKKLKTA
     PLPPAGQATT FQMTLNGKPA PPPQSQSPEV EQLGRVVELD SDMVDITQEP VPDSVLEESV
     PEDQEPVSAS THIASSLGIN PHVLQIMKAS LLVDEEDVDA MDQRFGHIPS KGETVQEICS
     PRLPISASHS SKSRSIVGGL LQSKFASETF LSPSASVQEC RTPRTSSRMN IPSTSPWSVP
     LPLATVFTVP SPAPEVQLKT VGIRRQPGLV PLEKSITYGK GKLLMDMALF MGRSFRVGWG
     PNWTLANSGE QLHGSHELEN HQVADSMEYG FLPNPVAVKS LSESPFKVHL EKLGLRQRKL
     DEDLQLYQTP LELKLKHSTV HVDELCPLIV PNPGVSVIHD YADWVKDSPG DFLELPIVKH
     WSLTWTLCEA LWGHLKELDG QLDEPSEYIQ TLERRRAFSR WLSHTAAPQI EEEVSLTRRD
     SPVEAVFSYL TGSRISGACC LAQQSGDHRL ALLLSQLVGS QSVRELLTMQ LADWHQLQAD
     SFIHDERLRI FALLAGKPVW QLSEQKQINV CSQLDWKRTL AIHLWYLLPP TASISRALSM
     YEEAFQNTPE GDKYACSPLP SYLEGCGCMV EEEKDSRRPL QDVCFHLLKL YSDRHYELNQ
     LLEPRSITAD PLDYRLSWHL WEVLRALNYT HLSEQCEGVL QASYAGQLES EGLWEWAIFV
     FLHIDNSGMR EKAVRELLTR HCQLSETPES WAKEAFLTQK LCVPAEWIHE AKAVRAHMES
     NKHLEALYLF KAGHWNRCHK LVIRHLASDA IINENYDYLK GFLEDLAPPE RSSLIQDWET
     SGLVYLDYIR VIEMLHRIQQ VDCSGYELEH LHTKVTSLCN RIEQIPCYNA KDRLAQSDMA
     KRVANLLRVV LSLQHAPDAT SNSTPDPQRV PLRLLAPHIG RLPMPEDYAL EELRGLTQSY
     LRELTVGSQ
//
ID   Q692V2_MOUSE            Unreviewed;       417 AA.
AC   Q692V2;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   08-MAR-2011, entry version 40.
DE   SubName: Full=Grp94 neighboring nucleotidase variant 4;
DE   Flags: Fragment;
GN   Name=Nt5dc3; Synonyms=BC030307, Gnn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NIH Swiss;
RX   PubMed=15827139; DOI=10.1128/JVI.79.9.5249-5258.2005;
RA   van den Akker E., Vankan-Berkhoudt Y., Valk P.J.M., Loewenberg B.,
RA   Delwel R.;
RT   "The common viral insertion site Evi12 is located in the 5'-noncoding
RT   region of Gnn, a novel gene with enhanced expression in two subclasses
RT   of human acute myeloid leukemia.";
RL   J. Virol. 79:5249-5258(2005).
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DR   EMBL; AY651022; AAT81234.1; -; mRNA.
DR   IPI; IPI00648312; -.
DR   UniGene; Mm.200446; -.
DR   ProteinModelPortal; Q692V2; -.
DR   STRING; Q692V2; -.
DR   Ensembl; ENSMUST00000099396; ENSMUSP00000096994; ENSMUSG00000054027.
DR   MGI; MGI:3513266; Nt5dc3.
DR   eggNOG; roNOG04271; -.
DR   GeneTree; ENSGT00550000074539; -.
DR   HOVERGEN; HBG053334; -.
DR   InParanoid; Q692V2; -.
DR   ArrayExpress; Q692V2; -.
DR   Bgee; Q692V2; -.
DR   Genevestigator; Q692V2; -.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR023214; HAD-like_dom.
DR   InterPro; IPR008380; HAD-SF_hydro_IG_5-nucl.
DR   InterPro; IPR016695; Pur_nucleotidase.
DR   Gene3D; G3DSA:3.40.50.1000; HAD-like_dom; 3.
DR   PANTHER; PTHR12103; HAD-SF_hydro_IG_5-nucl; 1.
DR   Pfam; PF05761; 5_nucleotid; 1.
DR   PIRSF; PIRSF017434; Purine_5'-nucleotidase; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR02244; HAD-IG-Ncltidse; 1.
PE   2: Evidence at transcript level;
KW   Magnesium; Metal-binding.
FT   ACT_SITE     41     41       Nucleophile (By similarity).
FT   ACT_SITE     43     43       Proton donor (By similarity).
FT   METAL        41     41       Magnesium (By similarity).
FT   METAL        43     43       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       328    328       Magnesium (By similarity).
FT   NON_TER       1      1
FT   NON_TER     417    417
SQ   SEQUENCE   417 AA;  48849 MW;  1BB844B1F5249F5B CRC64;
     LSDTLCKLEL VPSIMNNLLN PDAIFSNNEM SLSDIEIYGF DYDYTLVFYS KHLHTLIFNA
     ARDLLINEHR YPVEIRKYEY DPSFAIRGLH YDVQRAVLMK IDAFHYIQMG TVYKGLSVVP
     DEEVIDMYEG SHVPLEQMSD FYGKSSHGNT MEQFMDIFSL PEMTLLSCVN EHFLKNNIDY
     EPVHLYKDVK DSIRDVHIKG IMYRAIEADI EKYICYADQT RAVSAKLAAH GKKMFLITNS
     PSSFVDKGMR YIVGKDWRDL FDVVIVQAEK PNFFNDKRRP FRKVNEKGVL LWDKIHKLQK
     GQIYKQGNLY EFLKLTGWRG SKVLYFGDHI YSDLADLTLK HGRRTGAIIP ELRSELRIMN
     TEQYIQTMTR LQTLTGLLEQ MQVHRDAESQ LVLQEWKKER KEMREMTKSF FNAQFGS
//
ID   PEAK1_MOUSE             Reviewed;        1735 AA.
AC   Q69Z38; Q8BX56; Q8R365;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 3.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Pseudopodium-enriched atypical kinase 1;
DE            EC=2.7.10.2;
DE   AltName: Full=Sugen kinase 269;
DE   AltName: Full=Tyrosine-protein kinase SgK269;
GN   Name=Peak1; Synonyms=Kiaa2002, Sgk269;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-991.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1026-1735.
RC   TISSUE=Embryonic intestine;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1534-1735.
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-632, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   SUBCELLULAR LOCATION, AND PHOSPHORYLATION BY CSK.
RX   PubMed=20534451; DOI=10.1073/pnas.0914776107;
RA   Wang Y., Kelber J.A., Tran Cao H.S., Cantin G.T., Lin R., Wang W.,
RA   Kaushal S., Bristow J.M., Edgington T.S., Hoffman R.M., Bouvet M.,
RA   Yates J.R. III, Klemke R.L.;
RT   "Pseudopodium-enriched atypical kinase 1 regulates the cytoskeleton
RT   and cancer progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:10920-10925(2010).
RN   [9]
RP   ERRATUM.
RA   Wang Y., Kelber J.A., Tran Cao H.S., Cantin G.T., Lin R., Wang W.,
RA   Kaushal S., Bristow J.M., Edgington T.S., Hoffman R.M., Bouvet M.,
RA   Yates J.R. III, Klemke R.L.;
RL   Proc. Natl. Acad. Sci. U.S.A. 107:13556-13556(2010).
CC   -!- FUNCTION: Tyrosine kinase that may play a role in cell spreading
CC       and migration on fibronectin. May directly or indirectly affect
CC       phosphorylation levels of cytoskeleton-associated proteins
CC       MAPK1/ERK and PXN (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBUNIT: Interacts with BCAR1 and CRK (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction,
CC       focal adhesion. Note=Colocalizes with actin.
CC   -!- PTM: Autophosphorylated in vitro (By similarity). Phosphorylated
CC       on tyrosine in a CSK-dependent manner in response to adhesion to
CC       fibronectin and to EGF stimulation.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AC160935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK048912; BAC33490.1; -; mRNA.
DR   EMBL; AK173328; BAD32606.1; -; mRNA.
DR   EMBL; BC026466; AAH26466.1; -; mRNA.
DR   IPI; IPI00136917; -.
DR   RefSeq; NP_766512.2; NM_172924.3.
DR   UniGene; Mm.473654; -.
DR   ProteinModelPortal; Q69Z38; -.
DR   PhosphoSite; Q69Z38; -.
DR   PRIDE; Q69Z38; -.
DR   Ensembl; ENSMUST00000061552; ENSMUSP00000109901; ENSMUSG00000074305.
DR   GeneID; 244895; -.
DR   KEGG; mmu:244895; -.
DR   UCSC; uc009psz.1; mouse.
DR   MGI; MGI:2442366; C230081A13Rik.
DR   eggNOG; roNOG10877; -.
DR   GeneTree; ENSGT00460000041554; -.
DR   HOGENOM; HBG445852; -.
DR   HOVERGEN; HBG093946; -.
DR   InParanoid; Q69Z38; -.
DR   OrthoDB; EOG4PVNXS; -.
DR   BRENDA; 2.7.10.2; 244.
DR   NextBio; 386480; -.
DR   ArrayExpress; Q69Z38; -.
DR   Bgee; Q69Z38; -.
DR   CleanEx; MM_C230081A13RIK; -.
DR   Genevestigator; Q69Z38; -.
DR   GermOnline; ENSMUSG00000066635; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:EC.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell junction; Cytoplasm; Cytoskeleton; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Transferase;
KW   Tyrosine-protein kinase.
FT   CHAIN         1   1735       Pseudopodium-enriched atypical kinase 1.
FT                                /FTId=PRO_0000250590.
FT   DOMAIN     1302   1664       Protein kinase.
FT   NP_BIND    1308   1316       ATP (By similarity).
FT   COMPBIAS    145    148       Poly-Asn.
FT   COMPBIAS    775    872       Pro-rich.
FT   COMPBIAS    938    947       Poly-Glu.
FT   COMPBIAS    963    966       Poly-Pro.
FT   ACT_SITE   1505   1505       Proton acceptor (By similarity).
FT   BINDING    1348   1348       ATP (By similarity).
FT   MOD_RES     282    282       Phosphoserine.
FT   MOD_RES     371    371       Phosphoserine (By similarity).
FT   MOD_RES     537    537       Phosphoserine (By similarity).
FT   MOD_RES     568    568       Phosphothreonine (By similarity).
FT   MOD_RES     569    569       Phosphoserine (By similarity).
FT   MOD_RES     571    571       Phosphothreonine (By similarity).
FT   MOD_RES     584    584       Phosphoserine (By similarity).
FT   MOD_RES     632    632       Phosphotyrosine.
FT   MOD_RES     638    638       Phosphotyrosine (By similarity).
FT   MOD_RES     836    836       Phosphoserine (By similarity).
FT   MOD_RES     879    879       Phosphotyrosine (By similarity).
FT   MOD_RES    1097   1097       Phosphotyrosine (By similarity).
FT   MOD_RES    1141   1141       Phosphothreonine (By similarity).
FT   MOD_RES    1206   1206       Phosphoserine (By similarity).
FT   CONFLICT    965    991       PPVQRHHWFTEAKGEASEKPAIVFMYR -> SSPAPSLVHR
FT                                GQRRGQREACYSLHVQV (in Ref. 2; BAC33490).
FT   CONFLICT   1026   1039       SSYLPSQIPDKACS -> GDPVKMSLNGELCD (in Ref.
FT                                3; BAD32606).
FT   CONFLICT   1085   1085       L -> S (in Ref. 3; BAD32606).
FT   CONFLICT   1534   1536       LAC -> PTR (in Ref. 4; AAH26466).
SQ   SEQUENCE   1735 AA;  191125 MW;  1AB58647119DEBE9 CRC64;
     MSACNTFTEH VWKPGECKNC FKPKSLHQLP PDSEKTPITH GSGKTNANHS NNHRVRSTGN
     FRPPVAKKPT IAVKPTMMVA DGQSVCGELS IQEHCENKPV ILGWNQNKTS LSQKPLNNNS
     EGDAEGFGSD PQQCANNDSA QKISNNNNGL TEVLKEIAGL EATPPVRGNE TNARETFLGR
     INDCYKRSLE RKIPPSCMTG SMKDSQGKHV ILSGSAEVIS NEGGRFCYPE FSSGEESEED
     VLFSNMEEEH ESWDESDEEL LAMEIRMRGQ PRFANFRANT LSPVRFFVSK KWNTIPLRNK
     SLQRICAVDY DDSYDEILNG YEENSGVSYG QGSVQSTISS DCTSPGSSFT EESRSETASS
     LSQKVCNGGI SPGNPGNSKD IAETESNFES PPGNNEEKDE SLTSKSSVKV PETHKAVLAL
     RLQEKDGKIA VHTEKPESKA STDIAGQAVT ISLVPVEEQT KPYRVVNLEQ PLCKPYTVVD
     VSAAMASEHL GRPKIKGSSS TPNSPVTSPA LTPGQINAHL KKSSAIRYQE VWTSSTSPRQ
     KIPKIELSTG GPGPNVPPRR NCHKSAPTSP TATNISSKTI PVKSPNLSEI KFNSYNNAGM
     PPFPIIIHDE PSYARSSKNA IKVPIVINPN AYDNLAIYKS FLGTSGELSV KEKTTSVISH
     TYEEIETESK VSDSTPSKLT DCPQAKGFSN STERKRGSVA QKVQEFNNCL NRGQSSPQRS
     YSSTHSSPAK IQRPTQEPAG KTEGAQGSQV PGSSSNSTRE KASAVLCQIV ASIQPPQTPP
     EAPQSSPKAC SVEELYAVPP DADTTKSIPK NPPVRPKSLF TSQSSGEGEA HQTTESPTAK
     IQKDPSTKPV TSPPSKLVTS AQSEPPPPFP PPRSTSSPYH ASNLLQRHFT NWTKPTSPTR
     STEAESILHS EGSRRAADAK PKRWISFKSF FRRRKTDEEE EKEKEREKGK LVGLDGTVIH
     MLPPPPVQRH HWFTEAKGEA SEKPAIVFMY RCDPDQGHLS VDQSKAGAEK GRAEEVLLRN
     SEEKKSSYLP SQIPDKACSR VTHEVAGELS PRDPRTPAGK QDGTSVTPTL PPPDLEREEE
     KDDTLDPTDV SPCSATYSNL GQSRAAMIPP KHPRHPKGAV DDAIAFGEKT DQEGLNASQP
     TPPPLPKKMI RANTEPISKD LQKAMESSLC VMANPTYDID PNWDASSAGS SISYELKGLD
     VESYESLERP LHKERPVPSA ANSISSLATL SVKDRFSNSM ESLSSRRGLS YRQTRSIQKP
     QRQALYRGLD NREEVVGKLR SLHTDALKRL AVKCEDLFMA GQKDQLRFGV DSWSDFRLTS
     DKPCCEAGDA VYYTASYAKD PLSNYAVKIC KSKAKESQQY YHSLAVRQSL PVHFNIQQDC
     GHFLAEVPSR LLPWEDPDAP EKAEDGTEDS EEEGKAETLG GNPEPCSETE PSQKENQRVT
     NRKQRSHVVV ITREVPHLTV ADFVRDSLAH HGNSPDLYER QVCLLLLQLC SGLEHLKPYH
     VTHCDLRLEN LLLVQHQPGG AAQGPSPADP CPTLACPTRL IVSNFSQAKQ KSHLVDPQIL
     RDQSRLAPEI ITATQYKKCD EFQTGILIYE MLHLPNPFDE NPELKEKEYT RTDLPRIPLR
     SPYSWGLQQL ASCLLNPNPS ERILISDAKG ILQCLLWGPR EDLFQIFTTS ATLAQKNALL
     QNWLDIKRTL LMIKFAEKSL DREGGISLED WLCAQYLAFA TTDSLSYIVK ILQYR
//
ID   Q69Z47_MOUSE            Unreviewed;       536 AA.
AC   Q69Z47;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   08-MAR-2011, entry version 32.
DE   SubName: Full=MKIAA1991 protein;
DE   Flags: Fragment;
GN   Name=Rnf169; Synonyms=mKIAA1991;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
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DR   EMBL; AK173319; BAD32597.1; -; mRNA.
DR   IPI; IPI00464107; -.
DR   UniGene; Mm.323087; -.
DR   ProteinModelPortal; Q69Z47; -.
DR   PhosphoSite; Q69Z47; -.
DR   PRIDE; Q69Z47; -.
DR   Ensembl; ENSMUST00000080817; ENSMUSP00000079631; ENSMUSG00000058761.
DR   UCSC; uc009img.1; mouse.
DR   MGI; MGI:1920257; Rnf169.
DR   eggNOG; roNOG05793; -.
DR   GeneTree; ENSGT00390000000968; -.
DR   HOGENOM; HBG281571; -.
DR   HOVERGEN; HBG093905; -.
DR   InParanoid; Q69Z47; -.
DR   OMA; RCKTKHL; -.
DR   OrthoDB; EOG4GQQ4V; -.
DR   PhylomeDB; Q69Z47; -.
DR   ArrayExpress; Q69Z47; -.
DR   Bgee; Q69Z47; -.
DR   Genevestigator; Q69Z47; -.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   536 AA;  59572 MW;  2ED788C0EE0B9687 CRC64;
     RTPIKLSKPG ELSEEYGCLR KLRGEKLQEE KDCDDQIHKL LQEDSEMGKR KADEQKKRDE
     AVVLKTSLEQ CPARLSDSEN EEPSRGQMMQ THRSAFVSKN SSCSLAFLAG KLNTKVQRSQ
     SCSDTVQDRV RSRLRTAPPN RAKITTITPG STPIIGVLLS TQNNRCLSAP DLTIEKRLPF
     GSLSSLASLH KPERSISPES NDSISEELNH FKPIVCSPCT PPKRLPDGRV LSPLIIKSTP
     RNLTRSLQKQ TSYEASPRIL KKWEQIFQER QIKKTLSKAT LTSLAPEAGE EFPGSDTIHS
     SKERPSLAFN TRLSRVQVLS ECAGPTSTAL ECFPSVNQTK VEQDCVRKRS REFSLETCHS
     SEHGGASSGP SLEREQCEES GSTVDATLVK TCISTVMKTA AVNSLLPKND VLGGVLKTKQ
     QLKTLNHFDL GNGILVNSLG EEPIPSLRRG RKRRCKTKHL EQNGVKKLRP PSSDMDLAPK
     DPGLLEVGRK LQQEEEDQQL ALQSHRMFDS ERRTMSRRKG SVDQYLLRSS SLAGAK
//
ID   RADIL_MOUSE             Reviewed;        1099 AA.
AC   Q69Z89; Q8BNL0; Q8C549; Q8C6X2; Q8CAL1;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 2.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Ras-associating and dilute domain-containing protein;
GN   Name=Radil; Synonyms=Kiaa1849;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Pancreatic islet;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Head, and Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION.
RX   PubMed=17704304; DOI=10.1101/gad.1561507;
RA   Smolen G.A., Schott B.J., Stewart R.A., Diederichs S., Muir B.,
RA   Provencher H.L., Look A.T., Sgroi D.C., Peterson R.T., Haber D.A.;
RT   "A Rap GTPase interactor, RADIL, mediates migration of neural crest
RT   precursors.";
RL   Genes Dev. 21:2131-2136(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Downstream effector of Rap required for cell adhesion
CC       and migration of neural crest precursors during development.
CC   -!- SUBUNIT: Interacts with RAP1A; in a GTP-dependent manner. Does not
CC       interact with members of the Ras family (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q69Z89-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q69Z89-2; Sequence=VSP_016101, VSP_016103;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q69Z89-3; Sequence=VSP_016100;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q69Z89-4; Sequence=VSP_016101, VSP_016102;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q69Z89-5; Sequence=VSP_016101;
CC   -!- SIMILARITY: Belongs to the RADIL family.
CC   -!- SIMILARITY: Contains 1 dilute domain.
CC   -!- SIMILARITY: Contains 1 FHA domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 Ras-associating domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC38904.1; Type=Frameshift; Positions=985;
CC       Sequence=BAD32555.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK173277; BAD32555.1; ALT_INIT; mRNA.
DR   EMBL; AK038570; BAC30049.1; -; mRNA.
DR   EMBL; AK052964; BAC35223.1; -; mRNA.
DR   EMBL; AK079539; BAC37675.1; -; mRNA.
DR   EMBL; AK083410; BAC38904.1; ALT_FRAME; mRNA.
DR   EMBL; BC056483; AAH56483.1; -; mRNA.
DR   IPI; IPI00309138; -.
DR   IPI; IPI00623969; -.
DR   IPI; IPI00654933; -.
DR   IPI; IPI00655067; -.
DR   IPI; IPI00828941; -.
DR   RefSeq; NP_848817.2; NM_178702.3.
DR   UniGene; Mm.33766; -.
DR   ProteinModelPortal; Q69Z89; -.
DR   SMR; Q69Z89; 78-218, 276-393, 997-1092.
DR   PhosphoSite; Q69Z89; -.
DR   PRIDE; Q69Z89; -.
DR   Ensembl; ENSMUST00000063635; ENSMUSP00000064539; ENSMUSG00000029576.
DR   Ensembl; ENSMUST00000085758; ENSMUSP00000082910; ENSMUSG00000029576.
DR   Ensembl; ENSMUST00000110787; ENSMUSP00000106414; ENSMUSG00000029576.
DR   GeneID; 231858; -.
DR   KEGG; mmu:231858; -.
DR   UCSC; uc009ais.1; mouse.
DR   UCSC; uc009aiu.1; mouse.
DR   CTD; 231858; -.
DR   MGI; MGI:2443088; Radil.
DR   eggNOG; roNOG13028; -.
DR   GeneTree; ENSGT00530000063674; -.
DR   HOGENOM; HBG716049; -.
DR   HOVERGEN; HBG079536; -.
DR   InParanoid; Q69Z89; -.
DR   OMA; IMTLIEP; -.
DR   OrthoDB; EOG4RJG0X; -.
DR   NextBio; 380807; -.
DR   ArrayExpress; Q69Z89; -.
DR   Bgee; Q69Z89; -.
DR   CleanEx; MM_D930005D10RIK; -.
DR   Genevestigator; Q69Z89; -.
DR   GermOnline; ENSMUSG00000029576; Mus musculus.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR018444; Dil_domain.
DR   InterPro; IPR002710; Dilute.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR000159; Ras-assoc.
DR   InterPro; IPR008984; SMAD_FHA_domain.
DR   Gene3D; G3DSA:2.60.200.20; FHA; 1.
DR   Pfam; PF01843; DIL; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00788; RA; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00314; RA; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF49879; SMAD_FHA; 1.
DR   PROSITE; PS51126; DILUTE; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; FALSE_NEG.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50200; RA; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Developmental protein;
KW   Phosphoprotein.
FT   CHAIN         1   1099       Ras-associating and dilute domain-
FT                                containing protein.
FT                                /FTId=PRO_0000050804.
FT   DOMAIN       90    193       Ras-associating.
FT   DOMAIN      302    377       FHA.
FT   DOMAIN      525    792       Dilute.
FT   DOMAIN     1000   1085       PDZ.
FT   MOD_RES     235    235       Phosphoserine.
FT   VAR_SEQ       1    269       Missing (in isoform 3).
FT                                /FTId=VSP_016100.
FT   VAR_SEQ       1     29       Missing (in isoform 2, isoform 4 and
FT                                isoform 5).
FT                                /FTId=VSP_016101.
FT   VAR_SEQ     485   1079       Missing (in isoform 4).
FT                                /FTId=VSP_016102.
FT   VAR_SEQ    1019   1099       HTPLGAQGLYIQTLLPGSPAASDGRLSLGDQILEVNGSSLR
FT                                GVSYMRAVDLIRHGGKKMRFLVAKSDMETAKKIRFRNPPS
FT                                -> VRTLGPQPSTPPTPTPCFCRLILYSVSTVEASERCPDC
FT                                LMGLPLGALMEPSAFPWNIPGSG (in isoform 2).
FT                                /FTId=VSP_016103.
FT   CONFLICT    575    575       C -> S (in Ref. 2; BAC37675).
FT   CONFLICT    909    909       R -> Q (in Ref. 2; BAC38904).
SQ   SEQUENCE   1099 AA;  120355 MW;  CB1940EFFD10BC0D CRC64;
     MGSSIFLGLQ PSPSHWLKSS VVIHEDAPTM FYGTQLIMSP PTKNKLKRQS QLLSTMLSRT
     LSYKYRDLDS TFCSLGASDD PSELSTQLSA PGVLKVFGDS VCTGTHYKSV LATGSSSAQE
     LVKEALERYA LDPECAGQYV LCDVVGQAGD SGQRWQAQCF RVFGDNEKPL LIQELWKPRE
     GLSRRFELRK KSDVEELASR DVDTTTAGIN AQARRLQRIR AKGTPALTSE AAQSSPPTRL
     RRTVSETSLS PAPSLPEAAQ RPEEPVPEAM RYSLYQCPHL LLLQGYSQQH DSLVYVLSKE
     RHTVGQRTPS SKPSISLSAP DILPLHCTIR RHQSPEGGPA GTRLVLEPIT GASVSVNFSE
     VGRNPVVLQH GDLLSLGLYY LLLFKDPGQA QPLPACALAR LGAAPQSCRM CGAVLRARGA
     PSLPAAVVRR RSLLLEFEPD VEDTLLQRIM TLIEPGGDDH KLTPAFLLCL CIQHSAMHFQ
     PGTFRHLLLK ISKRVRDTVW EKTKELAEKQ AQLQEPISWA SFPMADLVPD LQHILFWMSN
     SIELLYFIQQ KSPLYVQSME EELDVTGSKE SLFSCTLTAS EEAMAALEEV VLYAFQQCVY
     YLSKCLYVCL PALLECPPFQ TERRESWRSG PALPEELRRV VSVFQATLDL LQQLQMHPEV
     ASQMLAYLFF FSGTLLLNQV LDKGPSLSCF HWPRGVQVCA RLQQFLEWAR SAGLGAPAER
     FFRKLSCTLH LLATPRAQLI QMSWATLRVT FPALNPAQLH RLLTQYQLAS AMGPVSAWEP
     GAPDGPEAFQ SEDILESYEN PPPIVLPSQG FQVDLEADCV EDSIYQHLLY IRHFLWGLRG
     QASPDSGPAQ PESIEGLYHT IPEGHLEGHG CPLANRDPGR VAVETAPPHS LPVTGAPRAQ
     GPPGRQPTRG DRRGSQAGSL HTDSSCMLTP PSTPLGLEPA GPSWPEPSGL CGRAVLDGQR
     NGPGGLPGAV LEGDAIQDAE PPAEASSPSS SAEDFCYVFM VELERGPSGL GMGLIDGMHT
     PLGAQGLYIQ TLLPGSPAAS DGRLSLGDQI LEVNGSSLRG VSYMRAVDLI RHGGKKMRFL
     VAKSDMETAK KIRFRNPPS
//
ID   BRSK2_MOUSE             Reviewed;         735 AA.
AC   Q69Z98; Q699J3; Q699J4; Q6DMN7; Q6PHM0;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=BR serine/threonine-protein kinase 2;
DE            EC=2.7.11.1;
GN   Name=Brsk2; Synonyms=Kiaa4256;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), FUNCTION, AND
RP   MUTAGENESIS OF LYS-49.
RX   PubMed=15705853; DOI=10.1126/science.1107403;
RA   Kishi M., Pan Y.A., Crump J.G., Sanes J.R.;
RT   "Mammalian SAD kinases are required for neuronal polarization.";
RL   Science 307:929-932(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RA   Tang W.W., Shan Y.X.;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 31-735 (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 131-653 (ISOFORM 4).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-423, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Required for the polarization of forebrain neurons which
CC       endows axons and dendrites with distinct properties, possibly by
CC       locally regulating phosphorylation of microtubule-associated
CC       proteins.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activated by phosphorylation on Thr-175 by
CC       STK11 in complex with STE20-related adapter-alpha (STRAD alpha)
CC       pseudo kinase and CAB39 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q69Z98-1; Sequence=Displayed;
CC       Name=2; Synonyms=SADA-beta;
CC         IsoId=Q69Z98-2; Sequence=VSP_022605;
CC         Note=No experimental confirmation available;
CC       Name=3; Synonyms=SADA-gamma;
CC         IsoId=Q69Z98-3; Sequence=VSP_022606;
CC         Note=No experimental confirmation available;
CC       Name=4; Synonyms=SADA-alpha;
CC         IsoId=Q69Z98-4; Sequence=VSP_022607, VSP_022608;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. AMPK subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY533672; AAT08447.1; -; mRNA.
DR   EMBL; AY533673; AAT08448.1; -; mRNA.
DR   EMBL; AY533674; AAT08449.1; -; mRNA.
DR   EMBL; AY660739; AAT74618.1; -; mRNA.
DR   EMBL; AL603836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL772165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK173268; BAD32546.1; -; mRNA.
DR   EMBL; BC056498; AAH56498.1; -; mRNA.
DR   IPI; IPI00466901; -.
DR   IPI; IPI00551400; -.
DR   IPI; IPI00551443; -.
DR   IPI; IPI00828329; -.
DR   RefSeq; NP_001009929.1; NM_001009929.2.
DR   RefSeq; NP_001009930.1; NM_001009930.2.
DR   RefSeq; NP_083702.1; NM_029426.2.
DR   UniGene; Mm.274868; -.
DR   UniGene; Mm.481638; -.
DR   HSSP; P06782; 2FH9.
DR   ProteinModelPortal; Q69Z98; -.
DR   SMR; Q69Z98; 10-338.
DR   STRING; Q69Z98; -.
DR   PhosphoSite; Q69Z98; -.
DR   PRIDE; Q69Z98; -.
DR   Ensembl; ENSMUST00000018971; ENSMUSP00000018971; ENSMUSG00000053046.
DR   Ensembl; ENSMUST00000075528; ENSMUSP00000074969; ENSMUSG00000053046.
DR   Ensembl; ENSMUST00000078200; ENSMUSP00000077330; ENSMUSG00000053046.
DR   Ensembl; ENSMUST00000105989; ENSMUSP00000101610; ENSMUSG00000053046.
DR   GeneID; 75770; -.
DR   KEGG; mmu:75770; -.
DR   UCSC; uc009kme.1; mouse.
DR   UCSC; uc009kmf.1; mouse.
DR   UCSC; uc009kmg.1; mouse.
DR   UCSC; uc009kmi.1; mouse.
DR   CTD; 75770; -.
DR   MGI; MGI:1923020; Brsk2.
DR   eggNOG; roNOG10787; -.
DR   GeneTree; ENSGT00570000078909; -.
DR   HOGENOM; HBG715635; -.
DR   HOVERGEN; HBG007240; -.
DR   InParanoid; Q69Z98; -.
DR   OMA; STNSYHY; -.
DR   OrthoDB; EOG479F6K; -.
DR   PhylomeDB; Q69Z98; -.
DR   BRENDA; 2.7.11.1; 244.
DR   ArrayExpress; Q69Z98; -.
DR   Bgee; Q69Z98; -.
DR   CleanEx; MM_BRSK2; -.
DR   Genevestigator; Q69Z98; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IC:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0030010; P:establishment of cell polarity; IGI:UniProtKB.
DR   GO; GO:0030182; P:neuron differentiation; IGI:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN         1    735       BR serine/threonine-protein kinase 2.
FT                                /FTId=PRO_0000274036.
FT   DOMAIN       20    271       Protein kinase.
FT   NP_BIND      26     34       ATP (By similarity).
FT   COMPBIAS    425    469       Pro-rich.
FT   ACT_SITE    142    142       Proton acceptor (By similarity).
FT   BINDING      49     49       ATP (By similarity).
FT   MOD_RES     175    175       Phosphothreonine (By similarity).
FT   MOD_RES     179    179       Phosphoserine (By similarity).
FT   MOD_RES     295    295       Phosphoserine (By similarity).
FT   MOD_RES     368    368       Phosphoserine (By similarity).
FT   MOD_RES     383    383       Phosphoserine (By similarity).
FT   MOD_RES     390    390       Phosphothreonine (By similarity).
FT   MOD_RES     394    394       Phosphoserine (By similarity).
FT   MOD_RES     413    413       Phosphoserine (By similarity).
FT   MOD_RES     423    423       Phosphothreonine.
FT   MOD_RES     424    424       Phosphoserine (By similarity).
FT   MOD_RES     428    428       Phosphoserine (By similarity).
FT   MOD_RES     436    436       Phosphoserine (By similarity).
FT   MOD_RES     467    467       Phosphoserine (By similarity).
FT   MOD_RES     490    490       Phosphoserine (By similarity).
FT   MOD_RES     510    510       Phosphothreonine (By similarity).
FT   VAR_SEQ     648    735       DTTNCMEVMTGRLSKCGTPLSNFFDVIKQLFSDEKNGQAAQ
FT                                APSTPAKRSAHGPLGDSAAAGPGGDTEYPMGKDMAKMGPPA
FT                                ARREQP -> EPPPPAPGLSWGAGLKGQKVATSYESSL
FT                                (in isoform 2).
FT                                /FTId=VSP_022605.
FT   VAR_SEQ     648    653       DTTNCM -> GIIPKS (in isoform 4).
FT                                /FTId=VSP_022607.
FT   VAR_SEQ     654    735       Missing (in isoform 4).
FT                                /FTId=VSP_022608.
FT   VAR_SEQ     664    679       Missing (in isoform 3).
FT                                /FTId=VSP_022606.
FT   MUTAGEN      49     49       K->A: Loss of kinase activity.
FT   CONFLICT     31     43       TGLVKLGIHCVTC -> VDGDLLASDTVDS (in Ref.
FT                                4; BAD32546).
SQ   SEQUENCE   735 AA;  81733 MW;  A37FCC6CC7253F11 CRC64;
     MTSTGKDGGG AQHAQYVGPY RLEKTLGKGQ TGLVKLGIHC VTCQKVAIKI VNREKLSESV
     LMKVEREIAI LKLIEHPHVL KLHDVYENKK YLYLVLEHVS GGELFDYLVK KGRLTPKEAR
     KFFRQIISAL DFCHSHSICH RDLKPENLLL DERNNIRIAD FGMASLQVGD SLLETSCGSP
     HYACPEVIRG EKYDGRKADV WSCGVILFAL LVGALPFDDD NLRQLLEKVK RGVFHMPHFI
     PPDCQSLLRG MIEVDAARRL TLEHIQKHIW YIGGKNEPEP EQPIPRKVQI RSLPSLEDID
     PDVLDSMHSL GCFRDRNKLL QDLLSEEENQ EKMIYFLLLD RKERYPSHED EDLPPRNEID
     PPRKRVDSPM LNRHGKRRPE RKSMEVLSVT DGGSPVPARR AIEMAQHGQR SRSISGASSG
     LSTSPLSSPR VTPHPSPRGS PLPTPKGTPV HTPKESPAGT PNPTPPSSPS VGGVPWRTRL
     NSIKNSFLGS PRFHRRKLQV PTPEEMSNLT PESSPELAKK SWFGNFINLE KEEQIFVVIK
     DKPLSSIKAD IVHAFLSIPS LSHSVISQTS FRAEYKATGG PAVFQKPVKF QVDITYTEGG
     EAQKENGIYS VTFTLLSGPS RRFKRVVETI QAQLLSTHDQ PSAQHLSDTT NCMEVMTGRL
     SKCGTPLSNF FDVIKQLFSD EKNGQAAQAP STPAKRSAHG PLGDSAAAGP GGDTEYPMGK
     DMAKMGPPAA RREQP
//
ID   ZN512_MOUSE             Reviewed;         562 AA.
AC   Q69Z99; Q3U365; Q3UDU3; Q3UJQ0; Q5FWY0; Q8BJF3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Zinc finger protein 512;
GN   Name=Znf512; Synonyms=Kiaa1805, Zfp512;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic intestine;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, C57BL/6J, and NOD; TISSUE=Bone marrow, and Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in transcriptional regulation (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family.
CC   -!- SIMILARITY: Contains 3 C2H2-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32545.1; Type=Erroneous initiation;
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DR   EMBL; AK173267; BAD32545.1; ALT_INIT; mRNA.
DR   EMBL; AK084205; BAC39137.1; -; mRNA.
DR   EMBL; AK146353; BAE27105.1; -; mRNA.
DR   EMBL; AK149921; BAE29168.1; -; mRNA.
DR   EMBL; AK154918; BAE32924.1; -; mRNA.
DR   EMBL; BC089160; AAH89160.1; -; mRNA.
DR   IPI; IPI00222382; -.
DR   RefSeq; NP_766581.2; NM_172993.3.
DR   UniGene; Mm.259127; -.
DR   HSSP; Q96ME7; 2CTD.
DR   ProteinModelPortal; Q69Z99; -.
DR   SMR; Q69Z99; 145-227, 243-365, 396-469.
DR   PhosphoSite; Q69Z99; -.
DR   PRIDE; Q69Z99; -.
DR   Ensembl; ENSMUST00000076264; ENSMUSP00000075613; ENSMUSG00000062761.
DR   GeneID; 269639; -.
DR   KEGG; mmu:269639; -.
DR   CTD; 269639; -.
DR   MGI; MGI:1917345; Zfp512.
DR   eggNOG; roNOG13700; -.
DR   GeneTree; ENSGT00490000043365; -.
DR   HOGENOM; HBG281888; -.
DR   HOVERGEN; HBG054123; -.
DR   InParanoid; Q69Z99; -.
DR   OMA; VKKYHRI; -.
DR   OrthoDB; EOG4J6RQV; -.
DR   NextBio; 392955; -.
DR   ArrayExpress; Q69Z99; -.
DR   Bgee; Q69Z99; -.
DR   Genevestigator; Q69Z99; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    562       Zinc finger protein 512.
FT                                /FTId=PRO_0000333737.
FT   ZN_FING     200    223       C2H2-type 1.
FT   ZN_FING     290    313       C2H2-type 2.
FT   ZN_FING     442    465       C2H2-type 3.
FT   CONFLICT     81     81       R -> G (in Ref. 2; BAE32924).
FT   CONFLICT    117    117       R -> G (in Ref. 2; BAC39137).
FT   CONFLICT    196    196       K -> E (in Ref. 2; BAE29168).
FT   CONFLICT    310    310       R -> G (in Ref. 2; BAE32924).
FT   CONFLICT    347    347       I -> M (in Ref. 2; BAC39137).
FT   CONFLICT    454    454       E -> K (in Ref. 2; BAE27105).
SQ   SEQUENCE   562 AA;  63908 MW;  DB522267A7113189 CRC64;
     MSSRLGAVTA TPGPTSLKQQ RSTRIVGAKN NRAQCSIKDN SFQYTIPHED SLSGSSSASS
     CEPVSDFTAT LRKSTYWMKM RRIKPAATSQ VEGAGEKEKE RAKGKRNVKQ EEDEDYRELP
     QKKHKLYGRK QRPKAQPHPK PQARRVRKEP PVYAAGSMEE KWYLEIMDKG SVSCPTCQAV
     GRKTIEGLKK HMENCKQEMF TCHHCGKQLH SLAGMKYHVM ANHNSLPILK AGDEVDEPSE
     RERLRTVLKR MGKLRCMRES CSSTFTSIMG YLYHVRKCGK EASELEKLAL KCHHCGKPYR
     SKAGLAYHMR SEHGPVFFPE SEQPDCLKEM SLEAKGGGRV QRRSAKIAVY HLQELASAEL
     TKEWPKRKVL QDLVPDDRKL KYTRPGLPTF SQEVLHKWKT DIKKYHRIQC PNQGCEAVYS
     SVSGLKAHLG SCTLGTFVAG KYKCLLCEKE FVSESGVKYH INSVHAEDWF VVNPTTTKSF
     EKLMKIKQRQ QEEEKQRQQH GRRRSLRRQQ QPCMEPPESQ LEPKAGKEQG GNEELVGPDP
     EPVPAQPQKA EPAKTTHKRG RK
//
ID   CDK13_MOUSE             Reviewed;        1511 AA.
AC   Q69ZA1; Q80V11; Q8BZG1; Q8K0A4;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Cyclin-dependent kinase 13;
DE            EC=2.7.11.22;
DE   AltName: Full=CDC2-related protein kinase 5;
DE   AltName: Full=Cell division cycle 2-like protein kinase 5;
DE   AltName: Full=Cell division protein kinase 13;
GN   Name=Cdk13; Synonyms=Cdc2l5, Kiaa1791;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryonic tail;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 295-1511 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 891-1511 (ISOFORMS 1 AND 2).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384; SER-396; SER-398;
RP   SER-401; SER-437 AND SER-438, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; SER-396; SER-398;
RP   SER-401; SER-410; SER-438 AND THR-871, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May be a controller of the mitotic cell cycle. Involved
CC       in the blood cell development (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q69ZA1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q69ZA1-2; Sequence=VSP_013580;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. CDC2/CDKX subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH32179.1; Type=Erroneous initiation;
CC       Sequence=BAC29077.1; Type=Frameshift; Positions=633, 666;
CC       Sequence=BAD32543.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK173265; BAD32543.1; ALT_INIT; mRNA.
DR   EMBL; AK035493; BAC29077.1; ALT_SEQ; mRNA.
DR   EMBL; BC032179; AAH32179.1; ALT_INIT; mRNA.
DR   EMBL; BC051093; AAH51093.1; -; mRNA.
DR   IPI; IPI00464128; -.
DR   IPI; IPI00556693; -.
DR   UniGene; Mm.193924; -.
DR   ProteinModelPortal; Q69ZA1; -.
DR   SMR; Q69ZA1; 701-1001.
DR   PhosphoSite; Q69ZA1; -.
DR   PRIDE; Q69ZA1; -.
DR   Ensembl; ENSMUST00000042365; ENSMUSP00000036013; ENSMUSG00000041297.
DR   UCSC; uc007poc.1; mouse.
DR   UCSC; uc007pod.1; mouse.
DR   MGI; MGI:1916812; Cdk13.
DR   HOGENOM; HBG279497; -.
DR   HOVERGEN; HBG050851; -.
DR   InParanoid; Q69ZA1; -.
DR   OrthoDB; EOG4TTGH6; -.
DR   PhylomeDB; Q69ZA1; -.
DR   BRENDA; 2.7.11.22; 244.
DR   ArrayExpress; Q69ZA1; -.
DR   Bgee; Q69ZA1; -.
DR   Genevestigator; Q69ZA1; -.
DR   GermOnline; ENSMUSG00000041297; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004693; F:cyclin-dependent protein kinase activity; IEA:EC.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN         1   1511       Cyclin-dependent kinase 13.
FT                                /FTId=PRO_0000085712.
FT   DOMAIN      705    998       Protein kinase.
FT   NP_BIND     711    719       ATP (By similarity).
FT   ACT_SITE    837    837       Proton acceptor (By similarity).
FT   BINDING     734    734       ATP (By similarity).
FT   MOD_RES       3      3       Phosphoserine (By similarity).
FT   MOD_RES     238    238       Phosphoserine (By similarity).
FT   MOD_RES     316    316       Phosphoserine (By similarity).
FT   MOD_RES     318    318       Phosphoserine (By similarity).
FT   MOD_RES     326    326       Phosphoserine.
FT   MOD_RES     341    341       Phosphoserine (By similarity).
FT   MOD_RES     343    343       Phosphoserine (By similarity).
FT   MOD_RES     349    349       Phosphoserine (By similarity).
FT   MOD_RES     350    350       Phosphoserine (By similarity).
FT   MOD_RES     359    359       Phosphoserine (By similarity).
FT   MOD_RES     361    361       Phosphoserine (By similarity).
FT   MOD_RES     368    368       Phosphoserine (By similarity).
FT   MOD_RES     384    384       Phosphoserine.
FT   MOD_RES     386    386       Phosphoserine (By similarity).
FT   MOD_RES     396    396       Phosphoserine.
FT   MOD_RES     398    398       Phosphoserine.
FT   MOD_RES     401    401       Phosphoserine.
FT   MOD_RES     410    410       Phosphoserine.
FT   MOD_RES     414    414       Phosphoserine (By similarity).
FT   MOD_RES     437    437       Phosphoserine.
FT   MOD_RES     438    438       Phosphoserine.
FT   MOD_RES     440    440       Phosphoserine (By similarity).
FT   MOD_RES     442    442       Phosphoserine (By similarity).
FT   MOD_RES     443    443       Phosphothreonine (By similarity).
FT   MOD_RES     491    491       Phosphoserine (By similarity).
FT   MOD_RES     495    495       Phosphothreonine (By similarity).
FT   MOD_RES     526    526       Phosphoserine (By similarity).
FT   MOD_RES     528    528       Phosphoserine (By similarity).
FT   MOD_RES     557    557       N6-acetyllysine (By similarity).
FT   MOD_RES     662    662       Phosphoserine (By similarity).
FT   MOD_RES     664    664       Phosphoserine (By similarity).
FT   MOD_RES     863    863       Phosphoserine (By similarity).
FT   MOD_RES     870    870       Phosphotyrosine (By similarity).
FT   MOD_RES     871    871       Phosphothreonine.
FT   MOD_RES    1048   1048       Phosphoserine (By similarity).
FT   MOD_RES    1054   1054       Phosphoserine (By similarity).
FT   MOD_RES    1056   1056       Phosphothreonine (By similarity).
FT   MOD_RES    1058   1058       Phosphothreonine (By similarity).
FT   MOD_RES    1143   1143       Phosphothreonine (By similarity).
FT   MOD_RES    1146   1146       Phosphoserine (By similarity).
FT   MOD_RES    1147   1147       Phosphothreonine (By similarity).
FT   MOD_RES    1245   1245       Phosphothreonine (By similarity).
FT   VAR_SEQ    1079   1138       Missing (in isoform 2).
FT                                /FTId=VSP_013580.
FT   CONFLICT    637    637       E -> K (in Ref. 2; BAC29077).
FT   CONFLICT   1009   1009       P -> L (in Ref. 1; BAD32543).
FT   CONFLICT   1206   1206       E -> K (in Ref. 3; AAH32179).
FT   CONFLICT   1400   1400       A -> P (in Ref. 3; AAH51093).
FT   CONFLICT   1464   1464       N -> D (in Ref. 2; BAC29077).
SQ   SEQUENCE   1511 AA;  164609 MW;  F945976C6CF54CB8 CRC64;
     MPSSSDTALG GGGGLSWAEK KLEERRKRRR FLSPQQPPLL LPLLQPQLLQ PPPPPPPLLF
     LAAPGAAAAA AAVAAASSSC FSPGPPLEVK RLARGKRRPG GRRKRRRGPR AGQEAEKRRV
     FSLPQPQQDG GGGASSGGGV TPLVEYEDVS SQSEQGLLLG GASAATAATA AGGTGGNGGS
     PASSSGTQRR AEGSERRPRR DRRSSSGRSK ERHREHRRRD GTRSGSEASK ARSRHGHSGE
     ERAEAAKSGS SSSSGGRRKS ASATSSSSSS RKDRDLKAHR SRTKSSKEPP SAYKEPPKAY
     REDKSEPKAY RRRQRSLSPL GGRDESPVSH RASQSLRSRK SPSPAGGGSS PYSRRLPRSP
     SPYSRRRSPS YSRHSSYERG GDVSPSPYSS SSWRRSRSPY SPVLRRSAKS RSRSPYSSRH
     SRSRSRHRLS RSRSRHSSIS PSTLTLKSSL AAELNKNKKA RAAEAARAAE AAKAAEAAKA
     AEAAAKAAKA SNASTPTKGN TETGASVSQT NHVKEVKKLK TEHAPSPSSG GTVKSDKAKT
     KPPLQVTKVD NNLTVEKATK KTVVGKESKP AATKEEPVST KEKSKPLTPS TGAKEKEQHV
     ALVTSTLPPL PLPPMLPEDK DADSLRGNIS VKAVKKEVEK KLRCLLADLP LPPELPGGDD
     LSKSPEEKKT AAQLHSKRRP KICGPRYGEI KEKDIDWGKR CVDKFDIIGI IGEGTYGQVY
     KARDKDTGEM VALKKVRLDN EKEGFPITAI REIKILRQLT HQSIINMKEI VTDKEDALDF
     KKDKGAFYLV FEYMDHDLMG LLESGLVHFN ENHIKSFMRQ LMEGLDYCHK KNFLHRDIKC
     SNILLNNRGQ IKLADFGLAR LYSSEESRPY TNKVITLWYR PPELLLGEER YTPAIDVWSC
     GCILGELFTK KPIFQANQEL AQLELISRIC GSPCPAVWPD VIKLPYFNTM KPKKQYRRKL
     REEFVFIPAA ALDLFDYMLA LDPSKRCTAE QALQCEFLRD VEPSKMPPPD LPLWQDCHEL
     WSKKRRRQKQ MGMTDDLSTI KAPRKDLSLG LDDSRTNTPQ GVLPPAQLKS QSNSNVAPVI
     TGPGQPLNHS ELAILLNLLQ SKSSVNMADF VQVLNIKVNS ETQQQLNKIN LPAGILATGE
     KQTDPSTPQQ ESSKSLGGVQ PSQTIQPKVE TDAAQAAVQS AFAVLLTQLI KAQQSKQKDA
     MLEERENGSG HEAPLQLRPP LEPSTPGSGQ DDLIQHQDRR ILELTPEPDR PRILPPDQRP
     PEPPEPPPVT EEDLDYRTEN QHVPTTSSSL TDPHAGVKAA LLQLLAQHQP QDDPKREGGI
     DYPTGDTYVP SSDYKDNFGS SFSAAPYVSS DGLGSSSAAA PLEARSFIGN SDIQSLDNYS
     TASSHTGGPP QTSAFTESFA SSVAGYGDIY LNAGPMLFSG DKDHRFEYSH GPITVLTNSN
     DPSTGPESTH PLPAKMHNYN YGGNLQENPG GPSLMHGQTW TSPAQGPGYS QGYRGHISTS
     AGRGRGRGLP Y
//
ID   TSYL5_MOUSE             Reviewed;         406 AA.
AC   Q69ZB3;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   08-MAR-2011, entry version 37.
DE   RecName: Full=Testis-specific Y-encoded-like protein 5;
DE            Short=TSPY-like protein 5;
GN   Name=Tspyl5; Synonyms=Kiaa1750;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
CC   -!- FUNCTION: Involved in modulation of cell growth and cellular
CC       response to gamma radiation probably via regulation of the Akt
CC       signaling pathway. Involved in regulation of p53/TP53. Suppresses
CC       p53/TP53 protein levels and promotes its ubiquitination; the
CC       function is dependent on USP7 and independent on MDM2. Proposed to
CC       displace p53/TP53 from interaction with USP7 (By similarity).
CC   -!- SUBUNIT: Interacts with USP7 (By similarity).
CC   -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP)
CC       family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32531.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK173253; BAD32531.1; ALT_INIT; mRNA.
DR   IPI; IPI00351345; -.
DR   RefSeq; NP_001078890.1; NM_001085421.1.
DR   UniGene; Mm.60794; -.
DR   HSSP; P25293; 2AYU.
DR   ProteinModelPortal; Q69ZB3; -.
DR   SMR; Q69ZB3; 183-377.
DR   PhosphoSite; Q69ZB3; -.
DR   PRIDE; Q69ZB3; -.
DR   Ensembl; ENSMUST00000042021; ENSMUSP00000045542; ENSMUSG00000038984.
DR   GeneID; 239364; -.
DR   KEGG; mmu:239364; -.
DR   UCSC; uc007vld.1; mouse.
DR   CTD; 239364; -.
DR   MGI; MGI:2442458; Tspyl5.
DR   eggNOG; roNOG08535; -.
DR   GeneTree; ENSGT00530000062882; -.
DR   HOGENOM; HBG126049; -.
DR   HOVERGEN; HBG014779; -.
DR   InParanoid; Q69ZB3; -.
DR   OrthoDB; EOG41RPV7; -.
DR   PhylomeDB; Q69ZB3; -.
DR   NextBio; 384087; -.
DR   Bgee; Q69ZB3; -.
DR   CleanEx; MM_TSPYL5; -.
DR   Genevestigator; Q69ZB3; -.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0071480; P:cellular response to gamma radiation; ISS:UniProtKB.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling cascade; ISS:UniProtKB.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:UniProtKB.
DR   InterPro; IPR002164; NAP_family.
DR   PANTHER; PTHR11875; NAP_family; 1.
DR   Pfam; PF00956; NAP; 1.
PE   2: Evidence at transcript level;
KW   Growth regulation.
FT   CHAIN         1    406       Testis-specific Y-encoded-like protein 5.
FT                                /FTId=PRO_0000307278.
SQ   SEQUENCE   406 AA;  44303 MW;  E272155AC2F9D213 CRC64;
     MSGRSRGRKS SRAKGRGKGR ARARVRAAAE DAWHDEKPPQ SPRLGEDSAA AQVQAGAAQG
     GAEPAELREE AACRLPLDCG LALRARAADE RGLAAPDPDL ERARSLAERL TSDTSFVGTV
     GALAKLRRGS RIGNRRVPGR KAPDTRSATG RGPQATVSGK PKMASAGLCA AAPVGEEKKM
     TEKHAGAGSP ATVGSMDTLE TVQLKLETMN AQADRAYLRL SRKFGQLRLH HLERRNLLIQ
     SIPGFWGQAF QNHPQLSAFL NTKDKEVLSY LNRLEVEELG LARLGYKIKF YFGRNPYFQN
     KVLIKEYGCG PSGQVVSRSA PIQWLPGHDL QSLSKENPEN NGSFFGWFSN HSSIESDKIV
     EIINEDLWPN PLQYYLISEE ARGEKGKEER PGPAKLSPAP AVRQPN
//
ID   GBA2_MOUSE              Reviewed;         918 AA.
AC   Q69ZF3; Q6PGM3; Q8BTN9;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Non-lysosomal glucosylceramidase;
DE            Short=NLGase;
DE            EC=3.2.1.45;
DE   AltName: Full=Beta-glucocerebrosidase 2;
DE            Short=Beta-glucosidase 2;
DE   AltName: Full=Glucosylceramidase 2;
GN   Name=Gba2; Synonyms=Kiaa1605;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=17080196; DOI=10.1172/JCI29224;
RA   Yildiz Y., Matern H., Thompson B., Allegood J.C., Warren R.L.,
RA   Ramirez D.M.O., Hammer R.E., Hamra F.K., Matern S., Russell D.W.;
RT   "Mutation of beta-glucosidase 2 causes glycolipid storage disease and
RT   impaired male fertility.";
RL   J. Clin. Invest. 116:2985-2994(2006).
CC   -!- FUNCTION: Non-lysosomal glucosylceramidase that catalyzes the
CC       conversion of glucosylceramide to free glucose and ceramide.
CC       Involved in sphingomyelin generation and prevention of glycolipid
CC       accumulation. May also catalyze the hydrolysis of bile acid 3-O-
CC       glucosides, however, the relevance of such activity is unclear in
CC       vivo.
CC   -!- CATALYTIC ACTIVITY: D-glucosyl-N-acylsphingosine + H(2)O = D-
CC       glucose + N-acylsphingosine.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein
CC       (By similarity). Note=Not localized to lipid rafts (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed at low level. Highly
CC       expressed in testis and brain.
CC   -!- DISRUPTION PHENOTYPE: Mice have a normal bile acid metabolism but
CC       males exhibit impaired fertility due to glucosylceramides
CC       accumulation.
CC   -!- SIMILARITY: Belongs to the non-lysosomal glucosylceramidase
CC       family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32491.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK173213; BAD32491.1; ALT_INIT; mRNA.
DR   EMBL; AK089192; BAC40785.1; -; mRNA.
DR   EMBL; AL732626; CAM17042.1; -; Genomic_DNA.
DR   EMBL; BC056935; AAH56935.1; -; mRNA.
DR   IPI; IPI00225123; -.
DR   RefSeq; NP_766280.2; NM_172692.3.
DR   UniGene; Mm.229444; -.
DR   ProteinModelPortal; Q69ZF3; -.
DR   STRING; Q69ZF3; -.
DR   CAZy; GH116; Glycoside Hydrolase Family 116.
DR   PRIDE; Q69ZF3; -.
DR   Ensembl; ENSMUST00000030189; ENSMUSP00000030189; ENSMUSG00000028467.
DR   GeneID; 230101; -.
DR   KEGG; mmu:230101; -.
DR   CTD; 230101; -.
DR   MGI; MGI:2654325; Gba2.
DR   eggNOG; roNOG07190; -.
DR   GeneTree; ENSGT00390000010998; -.
DR   HOGENOM; HBG403192; -.
DR   HOVERGEN; HBG105975; -.
DR   InParanoid; Q69ZF3; -.
DR   OMA; PHDLGAP; -.
DR   OrthoDB; EOG4BG8VC; -.
DR   PhylomeDB; Q69ZF3; -.
DR   BRENDA; 3.2.1.45; 244.
DR   NextBio; 379792; -.
DR   ArrayExpress; Q69ZF3; -.
DR   Bgee; Q69ZF3; -.
DR   CleanEx; MM_GBA2; -.
DR   Genevestigator; Q69ZF3; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008422; F:beta-glucosidase activity; ISS:UniProtKB.
DR   GO; GO:0004348; F:glucosylceramidase activity; IEA:EC.
DR   GO; GO:0006680; P:glucosylceramide catabolic process; IEA:InterPro.
DR   InterPro; IPR008928; 6-hairpin_glycosidase-like.
DR   InterPro; IPR014551; Beta_glucosidase_GBA2-type.
DR   InterPro; IPR006775; Glucosylceramidase.
DR   Pfam; PF04685; DUF608; 1.
DR   PIRSF; PIRSF028944; Beta_gluc_GBA2; 1.
DR   SUPFAM; SSF48208; Glyco_trans_6hp; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Glycosidase; Hydrolase; Lipid metabolism;
KW   Membrane; Sphingolipid metabolism; Transmembrane; Transmembrane helix.
FT   CHAIN         1    918       Non-lysosomal glucosylceramidase.
FT                                /FTId=PRO_0000283759.
FT   TOPO_DOM      1    678       Extracellular (Potential).
FT   TRANSMEM    679    699       Helical; (Potential).
FT   TOPO_DOM    700    918       Cytoplasmic (Potential).
FT   CARBOHYD     96     96       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    236    236       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    347    347       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    385    385       V -> I (in Ref. 2; BAC40785).
SQ   SEQUENCE   918 AA;  103294 MW;  EABE7B50B96B0B59 CRC64;
     MVTCVPASEQ VGCAERDSQV YCEDTGGTEA VRVTDCGSPE DSGPQDEPSY CNSEDSGQLM
     ASYEGKARGY QVPPFGWRIC LAHEFAEKRR PFQANNISLS NLVKHLGMGL RYLKWWYRKT
     HVEKKTPFID MLNSLPLRQI YGCPLGGIGG GTITRGWRGQ FCRWQLNPGM YQHQTVIADQ
     FIVCLRRDGR TVYQQVLSLE LPNVLRSWNW GLCGYFAFYH ALYPRAWTVY QLPGQNVTLT
     CRQVTPILPH DYQDSSLPVG VFVWDVENEG DETLDVSITF SMRNGLGGED DAAGSLWNEP
     FRLEQGGTTV QGLLLHHPTP PNPYTMAVAA RCTADTTVTH TTAFDPNGTG QQVWQDLLQD
     GQLDSPAGQS TPTQKGEGIA GAVCVSSKLL PRSRCCLEFS LAWDMPKIMF GAKSQVHYRR
     YTRFFGSDGD VAPALSHYAL CHYADWEDRI SAWQNPVLDD RTLPAWYKSA LFNELYFLAD
     GGTVWLEVPA DSLPEGLGGS MRQLRSTLQD YGRFGYLEGQ EYRMYNTYDV HFYASFALVM
     LWPKLELSLQ YDMALATLKE DLTRRRYLMS GVVAPVKRRN VIPHDIGDPD DEPWLRVNAY
     LIHDTADWKD LNLKFVLQIY RDYYLTGDQG FLEDMWPVCL AVMESEMKFD KDQDGLIENG
     GYADQTYDAW VTTGPSAYCG GLWLAAVAVM VQMAVLCGAQ DVQERFASIL CRGREAYERL
     LWNGRYYNYD SSSHPQSRSI MSDQCAGQWF LRACGLGEGD TEVFPTLHVV RALQTIFELN
     VQAFAGGAMG AVNGMHPHGV PDRSSVQSDE VWVGVVYGLA ATMIQEGLTW EGFRTAEGCY
     RTVWERLGLA FQTPEAYCQQ QVFRSLAYMR PLSIWAMQLA LQQQQHKKSR RPSVTQGTGL
     STQPECGPKR SLANLNSE
//
ID   CNNM4_MOUSE             Reviewed;         771 AA.
AC   Q69ZF7; Q9JIM7;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Metal transporter CNNM4;
DE   AltName: Full=Ancient conserved domain-containing protein 4;
DE            Short=mACDP4;
DE   AltName: Full=Cyclin-M4;
GN   Name=Cnnm4; Synonyms=Acdp4, Kiaa1592;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 99-771, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=14723793; DOI=10.1186/1471-2164-5-7;
RA   Wang C.-Y., Yang P., Shi J.-D., Purohit S., Guo D., An H., Gu J.-G.,
RA   Ling J., Dong Z., She J.-X.;
RT   "Molecular cloning and characterization of the mouse Acdp gene
RT   family.";
RL   BMC Genomics 5:7-7(2004).
RN   [3]
RP   TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=19200527; DOI=10.1016/j.ajhg.2009.01.006;
RA   Polok B., Escher P., Ambresin A., Chouery E., Bolay S., Meunier I.,
RA   Nan F., Hamel C., Munier F.L., Thilo B., Megarbane A.,
RA   Schorderet D.F.;
RT   "Mutations in CNNM4 cause recessive cone-rod dystrophy with
RT   amelogenesis imperfecta.";
RL   Am. J. Hum. Genet. 84:259-265(2009).
RN   [4]
RP   TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=19200525; DOI=10.1016/j.ajhg.2009.01.009;
RA   Parry D.A., Mighell A.J., El-Sayed W., Shore R.C., Jalili I.K.,
RA   Dollfus H., Bloch-Zupan A., Carlos R., Carr I.M., Downey L.M.,
RA   Blain K.M., Mansfield D.C., Shahrabi M., Heidari M., Aref P.,
RA   Abbasi M., Michaelides M., Moore A.T., Kirkham J., Inglehearn C.F.;
RT   "Mutations in CNNM4 cause Jalili syndrome, consisting of autosomal-
RT   recessive cone-rod dystrophy and amelogenesis imperfecta.";
RL   Am. J. Hum. Genet. 84:266-273(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-766, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Probable metal transporter. The interaction with the
CC       metal ion chaperone COX11 suggests that it may play a role in
CC       sensory neuron functions (By similarity). May play a role in
CC       biomineralization and retinal function.
CC   -!- SUBUNIT: Interacts with COX11 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- TISSUE SPECIFICITY: Cornea, retina, teeth (at protein level). In
CC       the retina it is predominantly localized to the outer plexiform
CC       layer, inner plexiform layer and ganglion cell layer. In the tooth
CC       strongest expression is observed in the cell body of the
CC       ameloblasts. Expressed at high level in kidney, small intestine
CC       and testis.
CC   -!- MISCELLANEOUS: Shares weak sequence similarity with the cyclin
CC       family, explaining its name. However it has no cyclin-like
CC       function in vivo.
CC   -!- SIMILARITY: Belongs to the ACDP family.
CC   -!- SIMILARITY: Contains 2 CBS domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF86375.1; Type=Erroneous initiation;
CC       Sequence=BAD32487.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK173209; BAD32487.1; ALT_INIT; mRNA.
DR   EMBL; AF216963; AAF86375.1; ALT_INIT; mRNA.
DR   IPI; IPI00120783; -.
DR   RefSeq; NP_291048.2; NM_033570.2.
DR   UniGene; Mm.422638; -.
DR   UniGene; Mm.472875; -.
DR   ProteinModelPortal; Q69ZF7; -.
DR   SMR; Q69ZF7; 332-505.
DR   PhosphoSite; Q69ZF7; -.
DR   PRIDE; Q69ZF7; -.
DR   Ensembl; ENSMUST00000045383; ENSMUSP00000048049; ENSMUSG00000037408.
DR   GeneID; 94220; -.
DR   KEGG; mmu:94220; -.
DR   CTD; 94220; -.
DR   MGI; MGI:2151060; Cnnm4.
DR   eggNOG; roNOG15282; -.
DR   GeneTree; ENSGT00390000002383; -.
DR   HOGENOM; HBG715526; -.
DR   HOVERGEN; HBG074775; -.
DR   InParanoid; Q69ZF7; -.
DR   OrthoDB; EOG405S0M; -.
DR   NextBio; 352207; -.
DR   ArrayExpress; Q69ZF7; -.
DR   Bgee; Q69ZF7; -.
DR   CleanEx; MM_CNNM4; -.
DR   Genevestigator; Q69ZF7; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000644; Cysta_beta_synth_core.
DR   InterPro; IPR002550; DUF21.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 2.
DR   Pfam; PF00571; CBS; 1.
DR   Pfam; PF01595; DUF21; 1.
DR   SUPFAM; SSF51206; cNMP_binding; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   1: Evidence at protein level;
KW   Biomineralization; CBS domain; Cell membrane; Glycoprotein;
KW   Ion transport; Membrane; Phosphoprotein; Repeat; Sensory transduction;
KW   Transmembrane; Transmembrane helix; Transport; Vision.
FT   CHAIN         1    771       Metal transporter CNNM4.
FT                                /FTId=PRO_0000295766.
FT   TRANSMEM     19     35       Helical; (Potential).
FT   TRANSMEM    176    196       Helical; (Potential).
FT   TRANSMEM    238    258       Helical; (Potential).
FT   TRANSMEM    262    282       Helical; (Potential).
FT   TRANSMEM    291    313       Helical; (Potential).
FT   DOMAIN      374    435       CBS 1.
FT   DOMAIN      442    508       CBS 2.
FT   MOD_RES     661    661       Phosphoserine (By similarity).
FT   MOD_RES     766    766       Phosphoserine.
FT   CARBOHYD    119    119       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   771 AA;  86626 MW;  C4207E51992D1DA2 CRC64;
     MAPGGGGGRR DGWPARGRLL LAALLLLWTR AASGQSSPQQ SVILGMRLAS CNKSCGMNPD
     GIIFVSEGST VNLRLYGHSL GDISSNLISF TEVDDAEAVH NSTNCLELTK DLVVQRLVNV
     SRGNTSGMLV VITKFLRRSE NMKLYALCTR PRADGPWTRW TDKDSLLFMV EEHGRFLPLW
     LHILLVMVLL VLSGIFSGLN LGLMALDPME LRIVQNCGTE KERKYARKIE PIRRKGNYLL
     CSLLLGNVLV NTSLTILLDN LIGSGIMAVA SSTIGIVIFG EILPQALCSR HGLAVGANTI
     VLTKVFMLLT FPLSFPISKL LDFVLGQEIR TVYNREKLME MLKVTEPYND LVKEELNMIQ
     GALELRTKTV EDIMTQLHDC FMIRSDAILD FNTMSEIMES GYTRIPVFED EQSNIVDILY
     VKDLAFVDPD DCTPLKTITR FYNHPVHFVF HDTKLDAMLE EFKKGKSHLA IVQKVNNEGE
     GDPFYEVLGL VTLEDVIEEI IKSEILDESD MYTDNRTRKR VSVKNKRDFS AFKDTDNELK
     VKISPQLLLA AHRFLATEVP QFSPSLMSEK ILLRLLKYPD VIQELRFNEH NRYCVRHYLY
     TRNKPADCFV LILQGKVEVE AGKENMKFET GAFSYYGTMA LSVAPPDRSP ALPTPLSRSA
     SLSYPDRNTD LTSTSLAGSN QFGSCILGQY VSDFSVRALT DLQYIKITRQ QYQNGLMASR
     MDNSPQPTFD GCATCSENFM ERPELPPVDE TTTLLNERNS LLHRASEEET I
//
ID   MSL2_MOUSE              Reviewed;         577 AA.
AC   Q69ZF8; Q497U7; Q8CBI7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   08-MAR-2011, entry version 47.
DE   RecName: Full=Male-specific lethal 2 homolog;
DE            Short=MSL-2;
DE   AltName: Full=Male-specific lethal 2-like 1;
DE            Short=MSL2-like 1;
DE   AltName: Full=Male-specific lethal-2 homolog 1;
DE   AltName: Full=RING finger protein 184;
GN   Name=Msl2; Synonyms=Kiaa1585, Msl2l1, Rnf184;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 111-577.
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 422-577.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Component of histone acetyltransferase complex
CC       responsible for the majority of histone H4 acetylation at lysine
CC       16 which is implicated in the formation of higher-order chromatin
CC       structure (By similarity).
CC   -!- SUBUNIT: Component of a multisubunit histone acetyltransferase
CC       complex (MSL) at least composed of the MOF/MYST1, MSL1/hampin,
CC       MSL2 and MSL3.
CC   -!- SIMILARITY: Belongs to the MSL2 family.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32486.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK173208; BAD32486.1; ALT_INIT; mRNA.
DR   EMBL; BC100371; AAI00372.1; -; mRNA.
DR   EMBL; AK035934; BAC29248.1; -; mRNA.
DR   IPI; IPI00658858; -.
DR   RefSeq; NP_001093921.1; NM_001100451.1.
DR   UniGene; Mm.326206; -.
DR   UniGene; Mm.436586; -.
DR   UniGene; Mm.480732; -.
DR   ProteinModelPortal; Q69ZF8; -.
DR   SMR; Q69ZF8; 36-86.
DR   STRING; Q69ZF8; -.
DR   PhosphoSite; Q69ZF8; -.
DR   PRIDE; Q69ZF8; -.
DR   Ensembl; ENSMUST00000085177; ENSMUSP00000082270; ENSMUSG00000066415.
DR   GeneID; 77853; -.
DR   KEGG; mmu:77853; -.
DR   UCSC; uc009rff.1; mouse.
DR   CTD; 77853; -.
DR   MGI; MGI:1925103; Msl2.
DR   eggNOG; roNOG08894; -.
DR   GeneTree; ENSGT00390000016814; -.
DR   HOGENOM; HBG712979; -.
DR   HOVERGEN; HBG108149; -.
DR   InParanoid; Q69ZF8; -.
DR   OrthoDB; EOG4JQ3XD; -.
DR   NextBio; 347671; -.
DR   ArrayExpress; Q69ZF8; -.
DR   Bgee; Q69ZF8; -.
DR   Genevestigator; Q69ZF8; -.
DR   GO; GO:0072487; C:MSL complex; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001841; Znf_RING.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Phosphoprotein; Zinc; Zinc-finger.
FT   CHAIN         1    577       Male-specific lethal 2 homolog.
FT                                /FTId=PRO_0000299537.
FT   ZN_FING      44     85       RING-type.
FT   COMPBIAS    396    463       Lys-rich.
FT   MOD_RES     453    453       Phosphotyrosine (By similarity).
SQ   SEQUENCE   577 AA;  62538 MW;  5B76E902299191C1 CRC64;
     MNPVNATALY ISASRLVLNY DPGDPKAFTE INRLLPYFRQ SLSCCVCGHL LQDPIAPTNS
     TCQHYVCKTC KGKKMMMKPS CSWCKDYEQF EENKQLSILV NCYKKLCEYI TQTTLARDII
     EAVDCSSDIL ALLNDGSLFC EETEKPSDSS FTLCLTHSPL PSTSEPTADP QASLSPMSES
     TLSIAIGSSV INGLPTYNGL SIDRFGINIP SPEHPNTIDV CNTVDIKTED LSDNLPPVCD
     TVATDLCSTG IDICSFSEDI KPGDSLLLSV EEVLRSLETV SNTEVCCPNL QPNLEATVSN
     GPFLQLSSQS LSHNVFMSTS PALHGLSCTA ATPKVAKLNR KRSRSESDSE KVQPLPISTI
     IRGPTLGASA PVTVKRESKI SLQPIATVPN GGTTPKISKT VLLSTKSMKK SHEHGSKKSH
     SKSKPGILKK DKAVKEKMPS HHFMPGSPTK TVYKKPQEKK GCKCGRATQN PSVLTCRGQR
     CPCYSNRKAC LDCICRGCQN SYMANGEKKL EAFAVPEKAL EQTRLTLGIN VTSIAVRNAS
     TSTSVINVTG SPVTTFLAAS THDDKSLDEA IDMRFDC
//
ID   Q69ZG5_MOUSE            Unreviewed;      1161 AA.
AC   Q69ZG5;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   SubName: Full=MKIAA1557 protein;
DE   Flags: Fragment;
GN   Name=Arid2; Synonyms=mKIAA1557;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Embryonic tail;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
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DR   EMBL; AK173201; BAD32479.1; -; mRNA.
DR   IPI; IPI00876196; -.
DR   UniGene; Mm.17166; -.
DR   ProteinModelPortal; Q69ZG5; -.
DR   STRING; Q69ZG5; -.
DR   PhosphoSite; Q69ZG5; -.
DR   PRIDE; Q69ZG5; -.
DR   Ensembl; ENSMUST00000058749; ENSMUSP00000052204; ENSMUSG00000033237.
DR   Ensembl; ENSMUST00000096250; ENSMUSP00000093969; ENSMUSG00000033237.
DR   Ensembl; ENSMUST00000109233; ENSMUSP00000104856; ENSMUSG00000033237.
DR   MGI; MGI:1924294; Arid2.
DR   eggNOG; roNOG11532; -.
DR   HOGENOM; HBG446325; -.
DR   HOVERGEN; HBG068777; -.
DR   InParanoid; Q69ZG5; -.
DR   OrthoDB; EOG49KFPP; -.
DR   PhylomeDB; Q69ZG5; -.
DR   ArrayExpress; Q69ZG5; -.
DR   Bgee; Q69ZG5; -.
DR   Genevestigator; Q69ZG5; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   1161 AA;  121475 MW;  5BEC3636CD4E76B8 CRC64;
     SFPVQGIHTV AQTVSRIPPN PSVHTHQQQN SPVTVIQNKA PIPCEVVKAT VIQNSVPQTA
     VPVSISVGGA PAQNSVGQNH SAGPQPVTVV NSQTLLHHPS VMPQPSPLHT VVPGQVPSGT
     PVTVIQQTVP QSRMFGRVQS IPACTSTVSQ GQQLITTSPQ PMHTSSQQTA AGSQPQDTVI
     IAPPQYVTTS ASNIVSATSV QNFQVATGQV VTIAGVPSPQ PSRVGFQNIA PKPLPSQQVS
     PSVVQQPIQQ PQQPAQQSVV IVSQPAQQGQ AYAPAIHQIV LANPAALPAG QTVQLTGQPN
     ITPSSSPSPV PPTNNQVPTA MSSSSTLQSQ GPPPTVSQML SVKRQQQQQH SPAAPAQQVQ
     VQVQQPQQVQ VQVQPQQPSA GVGQPAPNES SLIKQLLLPK RGPSTPGGKL ILPAPQIPPP
     NNARAPSPQV VYQVANNQAA GFGVQGQTPA QQLLVGQQNV QLVQSAMPPA GGVQTVPISN
     LQILPGPLIS NSPATIFQGT SGNQVTITVV PNTSFATATV SQGNAAQLIA PAGLSMSGAQ
     ASAGLQVQTL PAGQSACTTA PLPFKGDKII CQKEEEAKEA TGLHVHERKI EVMENPSCRR
     GTTNTSNGDT SESELQVGSL LNGRKYSDSS LPPSNSGKLQ SETSQCSLIS NGPSLELGEN
     GAPGKQNSEP VDMQDVKGDL KKALVNGICD FDKGDGSHLS KNIPNHKTSN HVGNGEISPV
     EPQGTSGATQ QDTAKGDQLE RVSNGPVLTL GGSPSTSSMQ EAPSVATPPL SGTDLPNGPL
     ASSLNSDVPQ QRPSVVVSPH STAPVIQGHQ VIAVPHSGPR VTPSALSSDA RSTNGTAECK
     TVKRPAEDND RDTVPGIPNK VGVRIVTISD PNNAGCSATM VAVPAGADPS TVAKVAIESA
     AQQKQQHPPT YMQSVAPQNT PMPPSPAVQV QGQPSSSQPS PVSASSQHAD PVRKPGQNFM
     CLWQSCKKWF QTPSQVFYHA ATEHGGKDVY PGQCLWEGCE PFQRQRFSFI THLQDKHCSK
     DALLAGLKQD EPGQVANQKS STKQPTVGGT GSAPRAQKAI ASHPSAALMA LRRGSRNLVF
     RDFTDEKEGP ITKHIRLTAA LILKNIGKYS ECGRRLLKRH ENNLSVLAIS NMEASSTLAK
     CLYELNFTVQ SKEQEKDSEM L
//
ID   RHG23_MOUSE             Reviewed;        1483 AA.
AC   Q69ZH9; Q8BNY7; Q9JJD6;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Rho GTPase-activating protein 23;
DE   AltName: Full=Rho-type GTPase-activating protein 23;
GN   Name=Arhgap23; Synonyms=Kiaa1501; ORFNames=MNCb-1301;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S.,
RA   Hashimoto K.;
RT   "Isolation of full-length cDNA clones from mouse brain cDNA library
RT   made by oligo-capping method.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 878-1483 (ISOFORM 1).
RC   TISSUE=Natural killer cell;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1107-1483.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351 AND SER-594, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting
CC       them to an inactive GDP-bound state (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q69ZH9-1; Sequence=Displayed;
CC         Note=No experimental confirmation available. Gene prediction
CC         based on EST data;
CC       Name=2;
CC         IsoId=Q69ZH9-2; Sequence=VSP_023710;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC37556.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB041572; BAA95056.1; -; mRNA.
DR   EMBL; AL596088; CAM15705.1; -; Genomic_DNA.
DR   EMBL; AK173187; BAD32465.1; -; mRNA.
DR   EMBL; AK079135; BAC37556.1; ALT_INIT; mRNA.
DR   IPI; IPI00458086; -.
DR   IPI; IPI00648449; -.
DR   RefSeq; NP_067468.2; NM_021493.2.
DR   UniGene; Mm.394118; -.
DR   HSSP; P52757; 1XA6.
DR   ProteinModelPortal; Q69ZH9; -.
DR   SMR; Q69ZH9; 41-155, 680-828, 897-1093.
DR   PhosphoSite; Q69ZH9; -.
DR   PRIDE; Q69ZH9; -.
DR   Ensembl; ENSMUST00000107601; ENSMUSP00000103227; ENSMUSG00000049807.
DR   Ensembl; ENSMUST00000107602; ENSMUSP00000103228; ENSMUSG00000049807.
DR   Ensembl; ENSMUST00000121799; ENSMUSP00000112999; ENSMUSG00000049807.
DR   GeneID; 58996; -.
DR   KEGG; mmu:58996; -.
DR   CTD; 58996; -.
DR   MGI; MGI:3697726; Arhgap23.
DR   eggNOG; maNOG22373; -.
DR   GeneTree; ENSGT00600000084250; -.
DR   HOVERGEN; HBG093896; -.
DR   InParanoid; Q69ZH9; -.
DR   OrthoDB; EOG48KR9S; -.
DR   PhylomeDB; Q69ZH9; -.
DR   NextBio; 314502; -.
DR   ArrayExpress; Q69ZH9; -.
DR   Bgee; Q69ZH9; -.
DR   Genevestigator; Q69ZH9; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; GTPase activation; Phosphoprotein.
FT   CHAIN         1   1483       Rho GTPase-activating protein 23.
FT                                /FTId=PRO_0000280472.
FT   DOMAIN       71    155       PDZ.
FT   DOMAIN      684    804       PH.
FT   DOMAIN      901   1093       Rho-GAP.
FT   COMPBIAS    183    273       Pro-rich.
FT   COMPBIAS   1421   1424       Poly-Gly.
FT   MOD_RES     351    351       Phosphoserine.
FT   MOD_RES     361    361       Phosphoserine (By similarity).
FT   MOD_RES     372    372       Phosphoserine (By similarity).
FT   MOD_RES     421    421       Phosphoserine (By similarity).
FT   MOD_RES     594    594       Phosphoserine.
FT   VAR_SEQ       1   1158       Missing (in isoform 2).
FT                                /FTId=VSP_023710.
FT   CONFLICT   1462   1464       DLG -> EPR (in Ref. 4; BAC37556).
SQ   SEQUENCE   1483 AA;  161832 MW;  652088C6725EC9BE CRC64;
     MNGVAFCLVG IPPRPEPRPP QLPLGPRDGC SSGRPLPWPG PRTLLLRKSL QDGFGFTLRH
     FIVYPPESAV HCILKEEENG GRGGGPSPRH RLEPMDTIFV KNVKDGGPAH RAGLRTGDRL
     VKVNGESIIG KTYSQVIGLI QNSDDTLELS IMPKDEDILQ LAYSQDAYLK GNEPYSGEAR
     SIPEPPPLCY PRKTYAPPTR APAWATMVPE PISALPPDPR SPAAWSDPGS RVPSATRAHL
     DNSSLGMSQP RPSPGAFPHL PSESRTPRAF PEPGSRVLPS RLECQQALSH WLSNQIPRRA
     GERRCPAMPP RARSASQDRL EDVTTHHPWP CSTSQDALSQ LGQEGWHRAR SDDYLSRATR
     SAEALGPGAL VSPRLERCGW ASQRPSARTS ACPSRDLTQA PPPSGLQGLD DIGYIGYRSY
     SPSFQRRTGL LHALSFRDSP FGGLPTFSLA QSPASFPPEA SEPPRVVRPD PSTRALEPPA
     EDHRDEVVLR QKPPTGRKVQ LTPARQMNLG FGDESPEPEA RGERLGRKVA PLATTEDSLA
     SIPFIDEPTS PSIDLQAKHV PASAVVSSAM NSAPVLGTSP SSPTFTFALS RHYSQDCSSI
     KAGRRSSYLL AITTERSKSC DDGLNTFRDE GRVLRRLPSR VPSLRVLRSF FTDGSLDSWG
     TSEDADAPSK RHSTSDLSDA TFSDIRREGW LYYKQILTKK GKKAGGGLRQ WKRVYAVLRA
     RSLSLSKERR EPGPAAAGAA AAGAGEDEAA PVCIGSCLVD ISYSETKRRH VFRLTTADFC
     EYLFQAEDRD DMLGWIRAIR ENSRAEGEDP GCANQALISK KLNDYRKVSH SSGPKADSSP
     KGSRGLGGLK SEFLKQTAVR GLRTQEQPPG SKEDSVAAPK TPWGINIIKK NKKAAPRAFG
     IRLEECQPAT ENQRVPLIVA ACCRIVEARG LESTGIYRVP GNNAVVSSLQ EQLNRGPSDI
     NLQDERWQDL NVISSLLKAF FRKLPEPLFT DDKYNDFIEA NRIEDSRERM KTLRKLIRDL
     PGHYYETLKF LVGHLKTIAD HSEKNKMEPR NLALVFGPTL VRTSEDNMTD MVTHMPDRYK
     IVETLIQHSD WFFSDDEDKG ERTPVDDKEP QSVPNIEYLL PNIGRTVPPS DPGSDSTTCS
     SAKSKGSWVP KKEPYAREML AISFISAVNR KRKKRREARG LGSSTDDDSE QEAHKAAVGT
     QEPPEGQLPG PAAEEAPGRL SPPTAPDERP AADTRSIVSG YSTLSTMDRS VCSGTGGRRA
     GAGDEADDER SELSHVETDT EGGAGPGGRL SRRPSFSSHH LMPCDTLARR RLSRSRAEAE
     GPGAGTARAC PRGPEPPGSA SSSSQESLRP PAAAPALGSR PSRVEALRLR LRGTADDMLA
     VRLRRPLSPE TRRRRSSWRR HTVVVQSPLT DLNFNEWKEL GGGGPQESVG VRPHSDNKDS
     GLSSLESTKA RASSAASLPS GDLGALQGLP QRRSAAARLH QCL
//
ID   SH3R1_MOUSE             Reviewed;         892 AA.
AC   Q69ZI1; O70254; Q3UG42; Q6P9M8; Q8BR66; Q8C2T5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Putative E3 ubiquitin-protein ligase SH3RF1;
DE            EC=6.3.2.-;
DE   AltName: Full=Plenty of SH3s;
DE            Short=Protein POSH;
DE   AltName: Full=SH3 domain-containing RING finger protein 1;
DE   AltName: Full=SH3 multiple domains protein 2;
GN   Name=Sh3rf1; Synonyms=Kiaa1494, Posh, Sh3md2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP   AND INTERACTION WITH RAC.
RX   MEDLINE=98151363; PubMed=9482736; DOI=10.1093/emboj/17.5.1395;
RA   Tapon N., Nagata K., Lamarche N., Hall A.;
RT   "A new rac target POSH is an SH3-containing scaffold protein involved
RT   in the JNK and NF-kappaB signalling pathways.";
RL   EMBO J. 17:1395-1404(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 200-892 (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Corpora quadrigemina, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH MAP3K10; MAP3K11; DLK1; MAP2K4; MAP2K7; MAPK8 AND
RP   MAPK9.
RX   PubMed=12514131; DOI=10.1093/emboj/cdg021;
RA   Xu Z., Kukekov N.V., Greene L.A.;
RT   "POSH acts as a scaffold for a multiprotein complex that mediates JNK
RT   activation in apoptosis.";
RL   EMBO J. 22:252-261(2003).
RN   [6]
RP   INTERACTION WITH AKT2, MUTAGENESIS OF GLU-470 AND TRP-489, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=14504284; DOI=10.1074/jbc.M307357200;
RA   Figueroa C., Tarras S., Taylor J., Vojtek A.B.;
RT   "Akt2 negatively regulates assembly of the POSH-MLK-JNK signaling
RT   complex.";
RL   J. Biol. Chem. 278:47922-47927(2003).
RN   [7]
RP   INTERACTION WITH SIAH1.
RX   PubMed=16230351; DOI=10.1074/jbc.M509060200;
RA   Xu Z., Sproul A., Wang W., Kukekov N., Greene L.A.;
RT   "Siah1 interacts with the scaffold protein POSH to promote JNK
RT   activation and apoptosis.";
RL   J. Biol. Chem. 281:303-312(2006).
RN   [8]
RP   INTERACTION WITH MAPK8IP.
RX   PubMed=16571722; DOI=10.1074/jbc.M601056200;
RA   Kukekov N.V., Xu Z., Greene L.A.;
RT   "Direct interaction of the molecular scaffolds POSH and JIP is
RT   required for apoptotic activation of JNKs.";
RL   J. Biol. Chem. 281:15517-15524(2006).
CC   -!- FUNCTION: Acts as a scaffold protein, contributes to Rac-induced
CC       signal transduction such as JNKs (MAPK8 and MAPK9) activation and
CC       induces apoptosis. Within a signaling complex, it probably
CC       recruits protein kinases such as MAP3K10 or MAP3K11 which are in
CC       turn activated leading to the sequential activation of MAP2K4,
CC       MAP2K7 and JNKs (MAPK8 and MAPK9) (By similarity). In fibroblasts,
CC       induces apoptosis.
CC   -!- FUNCTION: Might act as an E3 ubiquitin-protein ligase, or as part
CC       of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-
CC       conjugating enzymes such as UBE2D1 or UBE2N and then transfers it
CC       to substrates. In the absence of an external substrate, it can
CC       catalyZe self-ubiquitination (By similarity).
CC   -!- SUBUNIT: Interacts with HERP1 (By similarity). Interacts with Rac;
CC       in a GTP-dependent manner. Interacts with MAP3K10 and MAP3K11.
CC       Interacts with MAPK8IP; this interaction leads to the PJAC complex
CC       (POSH-JIP or SH3RF1/MAPK8IP apoptotic complex) with a 1:1 ratio.
CC       Interacts with SIAH1. Probably part of a signaling complex that
CC       may contain SH3RF1, MAPK8IP, DLK1, MAP2K4, MAP2K7, MAPK8, MAPK9,
CC       AKT1 and AKT2.
CC   -!- INTERACTION:
CC       Q9Z2F7:Bnip3l; NbExp=2; IntAct=EBI-957380, EBI-1774669;
CC       Q8IUQ4:SIAH1 (xeno); NbExp=2; IntAct=EBI-957380, EBI-747107;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region (By
CC       similarity). Cell projection, lamellipodium. Golgi apparatus,
CC       trans-Golgi network. Note=Co-localizes, with AKT2, in lamellipodia
CC       (By similarity). Co-localizes, with HERP1, in trans-Golgi network
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q69ZI1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q69ZI1-2; Sequence=VSP_033624;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q69ZI1-3; Sequence=VSP_033627, VSP_033628;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q69ZI1-4; Sequence=VSP_033625, VSP_033626;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- DOMAIN: The RING finger domain is responsible of ubiquitination
CC       and proteasomal degradation.
CC   -!- PTM: Phosphorylated at Ser-304 by AKT1 and AKT2. When
CC       phosphorylated, it has reduced ability to bind Rac (By
CC       similarity).
CC   -!- PTM: Subject to ubiquitination and proteasomal degradation (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the SH3RF family.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SIMILARITY: Contains 4 SH3 domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32463.1; Type=Erroneous initiation;
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DR   EMBL; AF030131; AAC40070.1; -; mRNA.
DR   EMBL; AK173185; BAD32463.1; ALT_INIT; mRNA.
DR   EMBL; BC060113; AAH60113.1; -; mRNA.
DR   EMBL; BC060696; AAH60696.1; -; mRNA.
DR   EMBL; AK088003; BAC40088.1; -; mRNA.
DR   EMBL; AK045470; BAC32385.1; -; mRNA.
DR   EMBL; AK148137; BAE28367.1; -; mRNA.
DR   IPI; IPI00399469; -.
DR   IPI; IPI00458726; -.
DR   IPI; IPI00894976; -.
DR   IPI; IPI00895133; -.
DR   PIR; T09071; T09071.
DR   RefSeq; NP_067481.2; NM_021506.2.
DR   UniGene; Mm.27949; -.
DR   HSSP; Q8R551; 1WI7.
DR   ProteinModelPortal; Q69ZI1; -.
DR   SMR; Q69ZI1; 5-56, 137-257, 455-512, 835-892.
DR   IntAct; Q69ZI1; 12.
DR   STRING; Q69ZI1; -.
DR   PhosphoSite; Q69ZI1; -.
DR   Ensembl; ENSMUST00000034060; ENSMUSP00000034060; ENSMUSG00000031642.
DR   Ensembl; ENSMUST00000093488; ENSMUSP00000091200; ENSMUSG00000031642.
DR   Ensembl; ENSMUST00000110291; ENSMUSP00000105920; ENSMUSG00000031642.
DR   GeneID; 59009; -.
DR   KEGG; mmu:59009; -.
DR   UCSC; uc009ltw.1; mouse.
DR   CTD; 59009; -.
DR   MGI; MGI:1913066; Sh3rf1.
DR   eggNOG; roNOG09333; -.
DR   GeneTree; ENSGT00550000074287; -.
DR   HOGENOM; HBG506330; -.
DR   HOVERGEN; HBG069552; -.
DR   InParanoid; Q69ZI1; -.
DR   OrthoDB; EOG4PG61S; -.
DR   NextBio; 314548; -.
DR   ArrayExpress; Q69ZI1; -.
DR   Bgee; Q69ZI1; -.
DR   Genevestigator; Q69ZI1; -.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005078; F:MAP-kinase scaffold activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0046328; P:regulation of JNK cascade; IDA:MGI.
DR   InterPro; IPR000108; p67phox.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00018; SH3_1; 4.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   PRINTS; PR00499; P67PHOX.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00326; SH3; 4.
DR   SUPFAM; SSF50044; SH3; 4.
DR   PROSITE; PS50002; SH3; 4.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell projection; Cytoplasm; Golgi apparatus;
KW   Ligase; Metal-binding; Phosphoprotein; Repeat; SH3 domain;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1    892       Putative E3 ubiquitin-protein ligase
FT                                SH3RF1.
FT                                /FTId=PRO_0000334152.
FT   DOMAIN      134    193       SH3 1.
FT   DOMAIN      196    259       SH3 2.
FT   DOMAIN      452    513       SH3 3.
FT   DOMAIN      833    892       SH3 4.
FT   ZN_FING      12     53       RING-type.
FT   REGION      447    550       Interaction with AKT2.
FT   COMPBIAS     84     90       Poly-Gly.
FT   COMPBIAS    397    403       Poly-Pro.
FT   COMPBIAS    406    431       Ala-rich.
FT   MOD_RES     304    304       Phosphoserine (By similarity).
FT   VAR_SEQ     160    189       Missing (in isoform 2).
FT                                /FTId=VSP_033624.
FT   VAR_SEQ     345    381       ELSGLSCSAPSQVHISTTGLIVTPPPSSPVTTGPAFT ->
FT                                APSQVQGRGQLPKRGLLTSGKILAASFIFALVTSSLL (in
FT                                isoform 4).
FT                                /FTId=VSP_033625.
FT   VAR_SEQ     382    892       Missing (in isoform 4).
FT                                /FTId=VSP_033626.
FT   VAR_SEQ     788    828       AAGTAALAQDAFHRKTSSLDSAVPIAPPPRQACSSLGPVMN
FT                                -> DRWNSSPSPGCLPPQDKLPGLRSAHCSTTSPGLLLPGP
FT                                SHE (in isoform 3).
FT                                /FTId=VSP_033627.
FT   VAR_SEQ     829    892       Missing (in isoform 3).
FT                                /FTId=VSP_033628.
FT   MUTAGEN     470    470       E->Q: Loss of binding to AKT2.
FT   MUTAGEN     489    489       W->A: Loss of binding to AKT2 and
FT                                enhanced binding to MAP3K11.
FT   CONFLICT    160    160       I -> T (in Ref. 1; AAC40070).
FT   CONFLICT    321    321       R -> S (in Ref. 3; BAE28367).
FT   CONFLICT    342    342       R -> G (in Ref. 3; BAE28367).
FT   CONFLICT    431    431       Missing (in Ref. 3; BAC32385 and 4;
FT                                AAH60113/AAH60696).
FT   CONFLICT    630    630       L -> M (in Ref. 3; BAE28367).
FT   CONFLICT    679    679       M -> V (in Ref. 3; BAC32385 and 4;
FT                                AAH60113/AAH60696).
SQ   SEQUENCE   892 AA;  93447 MW;  D92071116F4D6EBE CRC64;
     MDESALLDLL ECPVCLERLD ASAKVLPCQH TFCKRCLLGI VGSRNELRCP ECRTLVGSGV
     DELPSNILLV RLLDGIKQRP WKPGPGGGGG TTCTNTLRAQ GSTVVNCGSK DLQSSQCGQQ
     PRVQAWSPPV RGIPQLPCAK ALYNYEGKEP GDLKFSKGDI IILRRQVDEN WYHGEVSGVH
     GFFPTNFVQI IKPLPQPPPQ CKALYDFEVK DKEADKDCLP FAKDDVLTVI RRVDENWAEG
     MLADKIGIFP ISYVEFNSAA KQLIEWDKPP VPGVDTAECP SATAQSTSAS KHPDTKKNTR
     KRHSFTSLTM ANKSSQGSQN RHSMEISPPV LISSSNPTAA ARISELSGLS CSAPSQVHIS
     TTGLIVTPPP SSPVTTGPAF TFPSDVPYQA ALGSMNPPLP PPPLLAATVL ASTPSGATAA
     VAAAAAAAAA AGMGPRPVMG SSEQIAHLRP QTRPSVYVAI YPYTPRKEDE LELRKGEMFL
     VFERCQDGWY KGTSMHTSKI GVFPGNYVAP VTRAVTNASQ AKVSMSTAGQ ASRGVTMVSP
     STAGGPTQKP QGNGVAGNPS VVPTAVVSAA HIQTSPQAKV LLHMSGQMTV NQARNAVRTV
     AAHSQERPTA AVTPIQVQNA ACLGPASVGL PHHSLASQPL PPMAGPAAHG AAVSISRTNA
     PMACAAGASL ASPNMTSAML ETEPSGRTVT ILPGLPTSPE SAASACGNSS AGKPDKDSKK
     EKKGLLKLLS GASTKRKPRV SPPASPTLDV ELGAGEAPLQ GAVGPELPLG GSHGRVGSCP
     TDGDGPVAAG TAALAQDAFH RKTSSLDSAV PIAPPPRQAC SSLGPVMNEA RPVVCERHRV
     VVSYPPQSEA ELELKEGDIV FVHKKREDGW FKGTLQRNGK TGLFPGSFVE NI
//
ID   PREX1_MOUSE             Reviewed;        1650 AA.
AC   Q69ZK0; A2A5U1; Q6PFD4; Q8BN08;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein;
DE            Short=P-Rex1;
DE            Short=PtdIns(3,4,5)-dependent Rac exchanger 1;
GN   Name=Prex1; Synonyms=Kiaa1415;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Pancreatic islet;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1144-1650 (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Fetal brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH RAC1 AND RAC2.
RX   PubMed=16243036; DOI=10.1016/j.cub.2005.09.014;
RA   Dong X., Mo Z., Bokoch G., Guo C., Li Z., Wu D.;
RT   "P-Rex1 is a primary Rac2 guanine nucleotide exchange factor in mouse
RT   neutrophils.";
RL   Curr. Biol. 15:1874-1879(2005).
CC   -!- FUNCTION: Functions as a RAC guanine nucleotide exchange factor
CC       (GEF), which activates the Rac proteins by exchanging bound GDP
CC       for free GTP. Its activity is synergistically activated by
CC       phosphatidylinositol-3,4,5-triphosphate and the beta gamma
CC       subunits of heterotrimeric G protein. May function downstream of
CC       heterotrimeric G proteins in neutrophils (By similarity).
CC   -!- SUBUNIT: Interacts preferentially with RAC2. Interacts with RAC1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane.
CC       Note=Mainly cytosolic. Some amount is apparently associated to the
CC       plasma membrane (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q69ZK0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q69ZK0-2; Sequence=VSP_026436;
CC   -!- SIMILARITY: Contains 2 DEP domains.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32446.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK173168; BAD32446.1; ALT_INIT; mRNA.
DR   EMBL; AL591884; CAM16778.1; -; Genomic_DNA.
DR   EMBL; AL591884; CAM16779.1; -; Genomic_DNA.
DR   EMBL; AL732357; CAM16779.1; JOINED; Genomic_DNA.
DR   EMBL; AL732357; CAM22699.1; -; Genomic_DNA.
DR   EMBL; AL591884; CAM22699.1; JOINED; Genomic_DNA.
DR   EMBL; AK090301; BAC41161.1; -; mRNA.
DR   EMBL; BC057617; AAH57617.1; -; mRNA.
DR   IPI; IPI00464181; -.
DR   IPI; IPI00675236; -.
DR   RefSeq; NP_808450.2; NM_177782.3.
DR   UniGene; Mm.34420; -.
DR   UniGene; Mm.478314; -.
DR   HSSP; Q9ER22; 2DFK.
DR   ProteinModelPortal; Q69ZK0; -.
DR   SMR; Q69ZK0; 39-493, 504-597, 639-768.
DR   IntAct; Q69ZK0; 1.
DR   STRING; Q69ZK0; -.
DR   PhosphoSite; Q69ZK0; -.
DR   PRIDE; Q69ZK0; -.
DR   Ensembl; ENSMUST00000036719; ENSMUSP00000037180; ENSMUSG00000039621.
DR   GeneID; 277360; -.
DR   KEGG; mmu:277360; -.
DR   UCSC; uc008nyn.1; mouse.
DR   CTD; 277360; -.
DR   MGI; MGI:3040696; Prex1.
DR   eggNOG; roNOG11413; -.
DR   GeneTree; ENSGT00600000084023; -.
DR   HOGENOM; HBG445637; -.
DR   HOVERGEN; HBG053677; -.
DR   InParanoid; Q69ZK0; -.
DR   OMA; FKNEQVM; -.
DR   OrthoDB; EOG479F66; -.
DR   PhylomeDB; Q69ZK0; -.
DR   NextBio; 393758; -.
DR   ArrayExpress; Q69ZK0; -.
DR   Bgee; Q69ZK0; -.
DR   CleanEx; MM_BC067047; -.
DR   Genevestigator; Q69ZK0; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2.
DR   Pfam; PF00610; DEP; 2.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00049; DEP; 2.
DR   SMART; SM00228; PDZ; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   SUPFAM; SSF50156; PDZ; 2.
DR   PROSITE; PS50186; DEP; 2.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasm;
KW   Guanine-nucleotide releasing factor; Membrane; Phosphoprotein; Repeat.
FT   CHAIN         1   1650       Phosphatidylinositol 3,4,5-trisphosphate-
FT                                dependent Rac exchanger 1 protein.
FT                                /FTId=PRO_0000292674.
FT   DOMAIN       44    235       DH.
FT   DOMAIN      266    387       PH.
FT   DOMAIN      416    491       DEP 1.
FT   DOMAIN      518    592       DEP 2.
FT   DOMAIN      620    698       PDZ 1.
FT   COMPBIAS   1469   1472       Poly-Pro.
FT   MOD_RES     431    431       Phosphoserine (By similarity).
FT   VAR_SEQ       1   1188       Missing (in isoform 2).
FT                                /FTId=VSP_026436.
FT   CONFLICT   1575   1575       G -> V (in Ref. 4; AAH57617).
SQ   SEQUENCE   1650 AA;  184935 MW;  EB1C0140126209FC CRC64;
     MEAPGSGGGD GGGDPGGDGA HPDARGPVSG PCAAARDSER QLRLRLCVLN EILGTERDYV
     GTLRFLQSAF LQRIRQNVAD SVEKGLTEEN VKVLFSNIED ILEVHKDFLA ALEYCLHPEP
     QSQHELGNVF LKFKDKFCVY EEYCSNHEKA LRLLVELNKV PAVRAFLLSC MLLGGRKTTD
     IPLEGYLLSP IQRICKYPLL LKELAKRTPG KHPDHTAVQS ALQAMKTVCS NINETKRQME
     KLEALEQLQS HIEGWEGSNL TDICTELLLQ GNLLKISAGN IQERAFFLFD NLLVYCKRKS
     RVTGSKKSTK RTKSINGSLY IFRGRINTEV MEVENVEDGT ADYHSNGYTV TNGWKIHNTA
     KNKWFVCMAK TAEEKQKWLD ALIREREQRE SLKLGMERDA YVMIAEKGEK LYHMMMSKKV
     NLIKDRRRKL STVPKCFLGN EFVAWLLEIG EISKTEEGVN LGQALLENGI IHHVSDKHQF
     KNEQVMYRFR YDDGTYKARS ELEDIMSKGV RLYCRLHSLY APVIKDRDYH LKTYKSVVPG
     SKLVDWLLAQ GDCQTREEAV ALGVGLCNNG FMHHVLEKSE FKDESQYFRF HADEEMEGTS
     SKNKQLRNDF KLVENILAKR LLIPPQEDDY GFDLEEKNKA VVVKSVQRGS LAEMAGLQAG
     RKIYSINEDL VFLRPFSEVE TILNQFFCSR RPLRLLVATK AKETIKVPDH PEALSFQIRG
     TAPPCVFAVG RGSEAVAAGL CAGQCILKVN GTSVANDGAL EVLEHFQAFR NHREEALGLY
     QWVYHSHEDA QLARASQGAP DEDPQEDDQP DSALPLLSLG PQLSLHEDSA VVSLTLDNVH
     LEHGVVYEYM STAGAKCHVL EKIVEPRGCF RLAAKILEAF AVDDSIFVQN CGRLMAMSSA
     IVTMSHYEFH NICDTKLESI GQRIACYQEF AAQLKSRVSP PFKQASLEPH PLCGLDFCPT
     NCHVNLMEVS YPKTTPSVGR SFSIRFGRKP SLIGLDPEQG LNPMAYTQHC ITTMAAPSWK
     CSPAVDEDSQ GQGLNDSSYG SASGAPSQQD RGLSFLLKQE DREIQDAYLQ LFTKLDVALK
     EMKQYVTQIN RLLSTITEPT SAAPAPCDPS LVEETSSSPP VSEESEVDRT DHSGIKKVCF
     KVSEDEQEDS GHDTMSYRDS YSECNSNRDS VLSYTSVRSN SSYLGSDEMG SGDELPCDMR
     IPSDKQDKLH GCLEHLFNQV DSIHALLKGP VMSRAFEETR HFPMKHSWQE FKQKEECTVR
     GRNLIQISIQ EDPWNLPSSI RTLVDNIQQY VEDGKNQLLL ALLKCTDTEL QLRRDAVFCQ
     ALVAAVCTFS EQLLAALDYR YNNNGEYEES SRDASRKWLE QVAATGVLLH WQSLLAPASV
     KEERTMLEDI WVTLSELDNV TFSFKQLDEN SVANTNVFYH IEGSRQALKV VFYLDGFHFS
     RLPSRLEGGA SLRLHTVLFT KALESVEGPP PPGNQAAEEL QQEINAQSLE KVQQYYRKLR
     AFYLERSNLP TDAGATAVKI DQLIRPINAL DELYRLMKTF VHPKAGAAGS LGAGLIPVSS
     ELCYRLGACQ ITMCGTGMQR STLSVSLEQA AILARSHGLL PKCVMQATDI MRKQGPRVEI
     LAKNLRIKDP MPQGAPRLYQ LCQPPVDGDL
//
ID   NLGN2_MOUSE             Reviewed;         836 AA.
AC   Q69ZK9; Q5F288;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 2.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Neuroligin-2;
DE   Flags: Precursor;
GN   Name=Nlgn2; Synonyms=Kiaa1366;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-714, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 42-612, DISULFIDE BONDS, AND
RP   GLYCOSYLATION AT ASN-98.
RX   PubMed=18250328; DOI=10.1073/pnas.0711701105;
RA   Koehnke J., Jin X., Budreck E.C., Posy S., Scheiffele P., Honig B.,
RA   Shapiro L.;
RT   "Crystal structure of the extracellular cholinesterase-like domain
RT   from neuroligin-2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:1873-1878(2008).
CC   -!- FUNCTION: Neuronal cell surface protein thought to be involved in
CC       cell-cell-interactions by forming intercellular junctions through
CC       binding to beta-neurexins. Seems to play role in formation or
CC       maintenance of synaptic junctions. In vitro, triggers the de novo
CC       formation of presynaptic structures (By similarity).
CC   -!- SUBUNIT: Interacts with neurexin 1-beta, neurexin 2-beta and
CC       neurexin 3-beta. Interacts with INADL. Probably interacts through
CC       its C-terminus with DLG4 third PDZ domain (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32437.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK173159; BAD32437.1; ALT_INIT; mRNA.
DR   EMBL; AL603707; CAI51964.1; -; Genomic_DNA.
DR   IPI; IPI00468605; -.
DR   RefSeq; NP_942562.2; NM_198862.2.
DR   UniGene; Mm.151293; -.
DR   PDB; 3BL8; X-ray; 3.30 A; A/B/C/D=42-612.
DR   PDBsum; 3BL8; -.
DR   ProteinModelPortal; Q69ZK9; -.
DR   SMR; Q69ZK9; 42-609.
DR   DIP; DIP-29702N; -.
DR   STRING; Q69ZK9; -.
DR   PhosphoSite; Q69ZK9; -.
DR   PRIDE; Q69ZK9; -.
DR   Ensembl; ENSMUST00000056484; ENSMUSP00000053097; ENSMUSG00000051790.
DR   Ensembl; ENSMUST00000108634; ENSMUSP00000104274; ENSMUSG00000051790.
DR   GeneID; 216856; -.
DR   KEGG; mmu:216856; -.
DR   UCSC; uc007jrw.1; mouse.
DR   CTD; 216856; -.
DR   MGI; MGI:2681835; Nlgn2.
DR   HOGENOM; HBG716688; -.
DR   HOVERGEN; HBG008839; -.
DR   InParanoid; Q69ZK9; -.
DR   OMA; DIRDPGK; -.
DR   OrthoDB; EOG4ZPDTP; -.
DR   NextBio; 375400; -.
DR   ArrayExpress; Q69ZK9; -.
DR   Bgee; Q69ZK9; -.
DR   CleanEx; MM_NLGN2; -.
DR   Genevestigator; Q69ZK9; -.
DR   GermOnline; ENSMUSG00000051790; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0002087; P:regulation of respiratory gaseous exchange by neurological system process; IGI:MGI.
DR   GO; GO:0050804; P:regulation of synaptic transmission; IGI:MGI.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   InterPro; IPR000460; Neuroligin.
DR   PANTHER; PTHR11559; CarbesteraseB; 1.
DR   Pfam; PF00135; COesterase; 1.
DR   PRINTS; PR01090; NEUROLIGIN.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell adhesion; Disulfide bond; Glycoprotein; Membrane;
KW   Phosphoprotein; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     14       By similarity.
FT   CHAIN        15    836       Neuroligin-2.
FT                                /FTId=PRO_0000041879.
FT   TOPO_DOM     15    678       Extracellular (Potential).
FT   TRANSMEM    679    699       Helical; (Potential).
FT   TOPO_DOM    700    836       Cytoplasmic (Potential).
FT   MOD_RES     714    714       Phosphoserine.
FT   CARBOHYD     98     98       N-linked (GlcNAc...).
FT   CARBOHYD    136    136       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    522    522       N-linked (GlcNAc...) (Potential).
FT   DISULFID    106    141
FT   DISULFID    317    328
FT   DISULFID    487    521
FT   CONFLICT    210    210       V -> A (in Ref. 1; BAD32437).
FT   STRAND       59     63
FT   STRAND       66     73
FT   TURN         81     84
FT   STRAND       94     97
FT   STRAND      110    112
FT   TURN        116    118
FT   HELIX       121    125
FT   HELIX       127    131
FT   HELIX       132    134
FT   STRAND      135    137
FT   STRAND      143    149
FT   STRAND      151    154
FT   STRAND      177    183
FT   STRAND      186    190
FT   HELIX       193    195
FT   HELIX       199    205
FT   STRAND      207    212
FT   HELIX       217    221
FT   HELIX       233    248
FT   HELIX       249    252
FT   STRAND      254    264
FT   HELIX       266    276
FT   STRAND      281    283
FT   STRAND      286    291
FT   STRAND      294    296
FT   TURN        297    299
FT   HELIX       304    315
FT   HELIX       322    329
FT   HELIX       334    338
FT   STRAND      350    352
FT   STRAND      357    360
FT   HELIX       364    370
FT   STRAND      377    383
FT   HELIX       390    394
FT   STRAND      396    400
FT   HELIX       403    416
FT   HELIX       424    435
FT   HELIX       444    459
FT   HELIX       461    473
FT   STRAND      478    484
FT   TURN        500    503
FT   HELIX       504    508
FT   HELIX       510    513
FT   STRAND      517    519
FT   HELIX       525    544
FT   STRAND      549    551
FT   HELIX       564    566
FT   STRAND      575    577
FT   STRAND      579    586
FT   STRAND      589    592
FT   HELIX       595    602
FT   TURN        603    605
FT   HELIX       606    608
SQ   SEQUENCE   836 AA;  90989 MW;  4C03297F4F1A1F14 CRC64;
     MWLLALCLVG LAGAQRGGGG PGGGAPGGPG LGLGSLGEER FPVVNTAYGR VRGVRRELNN
     EILGPVVQFL GVPYATPPLG ARRFQPPEAP ASWPGVRNAT TLPPACPQNL HGALPAIMLP
     VWFTDNLEAA ATYVQNQSED CLYLNLYVPT EDGPLTKKRD EATLNPPDTD IRDSGKKPVM
     LFLHGGSYME GTGNMFDGSV LAAYGNVIVV TLNYRLGVLG FLSTGDQAAK GNYGLLDQIQ
     ALRWLSENIA HFGGDPERIT IFGSGAGASC VNLLILSHHS EGLFQKAIAQ SGTAISSWSV
     NYQPLKYTRL LAAKVGCDRE DSTEAVECLR RKSSRELVDQ DVQPARYHIA FGPVVDGDVV
     PDDPEILMQQ GEFLNYDMLI GVNQGEGLKF VEDSAESEDG VSASAFDFTV SNFVDNLYGY
     PEGKDVLRET IKFMYTDWAD RDNGEMRRKT LLALFTDHQW VAPAVATAKL HADYQSPVYF
     YTFYHHCQAE GRPEWADAAH GDELPYVFGV PMVGATDLFP CNFSKNDVML SAVVMTYWTN
     FAKTGDPNQP VPQDTKFIHT KPNRFEEVVW SKFNSKEKQY LHIGLKPRVR DNYRANKVAF
     WLELVPHLHN LHTELFTTTT RLPPYATRWP PRTPGPGTSG TRRPPPPATL PPESDIDLGP
     RAYDRFPGDS RDYSTELSVT VAVGASLLFL NILAFAALYY KRDRRQELRC RRLSPPGGSG
     SGVPGGGPLL PTAGRELPPE EELVSLQLKR GGGVGADPAE ALRPACPPDY TLALRRAPDD
     VPLLAPGALT LLPSGLGPPP PPPPPSLHPF GPFPPPPPTA TSHNNTLPHP HSTTRV
//
ID   FGD6_MOUSE              Reviewed;        1399 AA.
AC   Q69ZL1; Q8C8W5; Q8K3B0; Q9D3Y7;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=FYVE, RhoGEF and PH domain-containing protein 6;
GN   Name=Fgd6; Synonyms=Kiaa1362;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Pancreatic islet;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-1156 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Retina, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 457-1399 (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [5]
RP   STRUCTURE BY NMR OF 1303-1398.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the pleckstrin homology domain of mouse ethanol
RT   decreased 4 protein.";
RL   Submitted (NOV-2004) to the PDB data bank.
CC   -!- FUNCTION: May activate CDC42, a member of the Ras-like family of
CC       Rho- and Rac proteins, by exchanging bound GDP for free GTP. May
CC       play a role in regulating the actin cytoskeleton and cell shape
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). Cytoplasm,
CC       cytoskeleton (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q69ZL1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q69ZL1-2; Sequence=VSP_013093;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32435.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK173157; BAD32435.1; ALT_INIT; mRNA.
DR   EMBL; AK016940; BAB30510.2; -; mRNA.
DR   EMBL; AK044341; BAC31876.1; -; mRNA.
DR   EMBL; BC026860; AAH26860.2; -; mRNA.
DR   IPI; IPI00464194; -.
DR   IPI; IPI00553469; -.
DR   RefSeq; NP_444302.4; NM_053072.3.
DR   UniGene; Mm.269596; -.
DR   PDB; 1WGQ; NMR; -; A=1303-1397.
DR   PDBsum; 1WGQ; -.
DR   ProteinModelPortal; Q69ZL1; -.
DR   SMR; Q69ZL1; 839-1151, 1188-1251, 1308-1398.
DR   PhosphoSite; Q69ZL1; -.
DR   PRIDE; Q69ZL1; -.
DR   Ensembl; ENSMUST00000020208; ENSMUSP00000020208; ENSMUSG00000020021.
DR   GeneID; 13998; -.
DR   KEGG; mmu:13998; -.
DR   UCSC; uc007gvm.1; mouse.
DR   CTD; 13998; -.
DR   MGI; MGI:1261419; Fgd6.
DR   eggNOG; roNOG09010; -.
DR   GeneTree; ENSGT00550000074235; -.
DR   HOGENOM; HBG278690; -.
DR   HOVERGEN; HBG051610; -.
DR   InParanoid; Q69ZL1; -.
DR   OMA; SAQKWIE; -.
DR   OrthoDB; EOG4HQDHG; -.
DR   PhylomeDB; Q69ZL1; -.
DR   NextBio; 284882; -.
DR   ArrayExpress; Q69ZL1; -.
DR   Bgee; Q69ZL1; -.
DR   CleanEx; MM_FGD6; -.
DR   Genevestigator; Q69ZL1; -.
DR   GermOnline; ENSMUSG00000020021; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF00169; PH; 2.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton;
KW   Guanine-nucleotide releasing factor; Metal-binding; Phosphoprotein;
KW   Repeat; Zinc; Zinc-finger.
FT   CHAIN         1   1399       FYVE, RhoGEF and PH domain-containing
FT                                protein 6.
FT                                /FTId=PRO_0000080953.
FT   DOMAIN      841   1030       DH.
FT   DOMAIN     1059   1153       PH 1.
FT   DOMAIN     1302   1398       PH 2.
FT   ZN_FING    1191   1250       FYVE-type.
FT   COMPBIAS     10     75       Lys/Pro-rich.
FT   MOD_RES     494    494       Phosphoserine.
FT   MOD_RES     697    697       Phosphoserine (By similarity).
FT   VAR_SEQ       1    934       Missing (in isoform 2).
FT                                /FTId=VSP_013093.
FT   CONFLICT    126    126       Q -> L (in Ref. 2; BAC31876).
FT   CONFLICT    262    262       R -> H (in Ref. 2; BAC31876).
FT   CONFLICT    286    286       V -> D (in Ref. 2; BAC31876).
FT   CONFLICT    347    348       YC -> S (in Ref. 2; BAC31876).
FT   CONFLICT    368    368       V -> A (in Ref. 2; BAC31876).
FT   CONFLICT    517    517       Y -> H (in Ref. 2; BAC31876 and 3;
FT                                AAH26860).
FT   CONFLICT    637    637       A -> T (in Ref. 2; BAC31876 and 3;
FT                                AAH26860).
FT   CONFLICT    791    791       K -> Q (in Ref. 2; BAC31876 and 3;
FT                                AAH26860).
FT   STRAND     1306   1314
FT   STRAND     1320   1327
FT   STRAND     1330   1335
FT   STRAND     1343   1347
FT   STRAND     1349   1355
FT   STRAND     1362   1370
FT   STRAND     1373   1379
FT   HELIX      1383   1397
SQ   SEQUENCE   1399 AA;  155169 MW;  CB91142F176E5A2F CRC64;
     MTSAAELKKP PLAPKPKLVG TNNKPPPPPI APKPDIGSAS VPRLTKKTKP AIAPKPKVPT
     NSVVQDIKHP PSKKPTLNLE EREPELPEST GKSNCKDVRD PHSDYILPTC SCSSGCIHEP
     RTRETQCVEQ LVLEPLGMKE NLENSKNGES SKRGSSWDSS SEKCRGQSGV VLKASILEEK
     LKEVLTQQRS PCGSPGRHRA PKKPEMNGDH SCTRQIRIEF ADVSSSLTGF EKVPAHHNCH
     PQLPRDESQT LKTCQDGSAE SRGHTDSCEP ENKRVASDGI SQKTEVKGLG PLEIHLLPYT
     SKFPTPKPRK THAAARLRRQ KHVDTPGEST EEPGNSNNGS SCLLEDYCLK NNKVSVLRQN
     ALYNQGPVDE VRPANQRALT GDSNSGGQDS VGSQKAVQQQ TPSLDTDSSL TSDSSGSGVS
     PAVDKETTYT QCSTQPLSLP KQVTSACTDQ PPATCNPEVS APPIQKESSS SRIIPKKPQR
     HSLPAAGVLK KAASEELVEK SSSGKETNVE KGLHRNYLHH PGPPNHGASA SPFDMPNPTS
     EKPVWKLPHP ILPFSGSPEA LKRVTLSLNN EPSVSLTKPR AKSLSAVDAD RCNKPCKDPP
     KKTSFKKLIN VKLSIGFIKS DFQKIRSKSC QHGDVSAGHP LAREPKGLES DWQGLATGEE
     KRSKPTKAHS AENCSLESQK VKSWGQSSAV NGQRAESLDD RILSRHTSCT GDFGPEYENV
     RHYEEIPEYE NLPFVMAGRN TPDLGWQNSS SVEDTDASLY EVEEPYNAPD GQLQLDPRHQ
     PCSSGTSQEG KDALHLGLSD LPSDEEVINS SDEDDVSSES SKGEPDPLED KQDEDAGMKS
     KVHHIAKEIM SSEKVFVDVL KLLHIDFRGA VAHASRQLGK PVIEDRILNQ ILYYLPQLYE
     LNRDLLKELE ERMLTWTEQQ RIADIFVKKG PYLKMYSTYI KEFDKNVALL DEQCKKNPGF
     AAVVREFEMS PRCANLALKH YLLKPVQRIP QYRLLLTDYL KNLLEDSVDH RDTQDALAVV
     IEVANHANDT MKQGDNFQKL MQIQYSLSGH HEIVQPGRVF LKEGTLMKLS RKVMQPRMFF
     LFNDALLYTT PMQSGMYKLN NMLSLAGMKV RKPTQEAYQN ELKIESVERS FILSASSAAE
     RDDWLEAISS SIEEYAKKRI TFCPSRSLDE DSERKEEVSP LGAKAPIWIP DTRATMCMIC
     TSEFTLTWRR HHCRACGKIV CQACSSNKYG LDYLKGQLAR VCEHCFQELQ KLDHQLSPRV
     GSPGNHKSPS SALSSVLHSI PSGRKQKKIP AALKEVSANT EDSTMSGYLY RSKGSKKPWK
     HLWFVIKNKV LYTYAASEDV AALESQPLLG FTVTLVKDEN SESKVFQLLH KGMVFYVFKA
     DDAHSTQRWI DAFQEGTVL
//
ID   Q69ZN8_MOUSE            Unreviewed;      1848 AA.
AC   Q69ZN8;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   08-MAR-2011, entry version 42.
DE   SubName: Full=MKIAA1205 protein;
DE   Flags: Fragment;
GN   Name=Prr12; Synonyms=BC058674, mKIAA1205;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Embryonic tail;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK173130; BAD32408.1; -; mRNA.
DR   IPI; IPI00153715; -.
DR   RefSeq; NP_778187.2; NM_175022.2.
DR   UniGene; Mm.219137; -.
DR   ProteinModelPortal; Q69ZN8; -.
DR   PhosphoSite; Q69ZN8; -.
DR   Ensembl; ENSMUST00000057293; ENSMUSP00000054702; ENSMUSG00000046574.
DR   GeneID; 233210; -.
DR   KEGG; mmu:233210; -.
DR   UCSC; uc009gsu.1; mouse.
DR   CTD; 233210; -.
DR   MGI; MGI:2679002; Prr12.
DR   eggNOG; roNOG16206; -.
DR   HOGENOM; HBG269030; -.
DR   HOVERGEN; HBG082198; -.
DR   InParanoid; Q69ZN8; -.
DR   OrthoDB; EOG4RR6H3; -.
DR   PhylomeDB; Q69ZN8; -.
DR   NextBio; 381617; -.
DR   ArrayExpress; Q69ZN8; -.
DR   Bgee; Q69ZN8; -.
DR   Genevestigator; Q69ZN8; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR   SMART; SM00384; AT_hook; 2.
PE   1: Evidence at protein level;
FT   NON_TER       1      1
SQ   SEQUENCE   1848 AA;  192479 MW;  51696D30321FF565 CRC64;
     VLHLKPSQAP TVPSSLGFER LAGGGVLGPA GLGPAQTPPY RPGPPDPPPP PRHLPTQFNL
     LASSSAATAA EPSSPQLYNF SGAAPGPPPE RALPRQDTVI KHYQRPASAQ PPPPPPPAHS
     LQHYLSCGGS YPSMGHRASL ACSPLGGGEP SPGAGEPSKG GPSGATAGAA GRATGPETAG
     GGAAGGGGGY RPIIQSPGYK TSKGGYGPAT GGATRPPPPR STATPKCQSL GGPAAAYAAG
     KASGAGGAGS QAYSPGQPQG LLGPQAYGQG FGGGQAQDLS KGPSYSGGPP QPPSGPPPPG
     LATCQSYSPD QLQGQLYGVQ SEPYPGPAAH SQGLPTASPS LSYSTGHSPA LSGHGGGWGP
     SSLGGGGEAS PSHIIRPLQS PPATGRPPGV GSPGAPGKYL SSVLASAPFL APPGASSYAA
     GAGGYKGKGD GSELLAGPGG SAAERTEDEE FLIQHLLQAP SPPRTSGADG LVGEDGPADA
     AKGLGGSGGA GGAPGTPYEL AKEDPQRYHL QSVIRTSASL DEGATAALEL GLGRMKDKKK
     GPERGGETPE GLATSVVHYG AGAKELGAFL QKSPPPPPPS AQATQPAPHG LLLEAGGPDL
     PMVLPPPPPQ LLPSVLSHAP SPSPSAPKVG VHLLEPATRD GAPQPPPPPP PPMPLQLEAH
     LRGHGLEPTA PSPRLRPEES LEPPGAMQEL LGALEPLPSG PGDPGVGPPN SEGKDPAGAY
     RSPSPQGTKA PRFVPLTSIC FPDSLLQDEE RSFFPTMEEM FGGGAADDYG KAGQTEDDGD
     PKTGAGPPPG PTAYDPYGPY CGGRASGTGP ETPGLGLDHN KPPELPSTVN AEPLGLIQSG
     PHQSAPPPPP PPPPPPPVSE PKGGLTSPIF CSTKPKKLLK TSSFHLLRRR DPPFQTPKKL
     YAQEYEFEAD EDKADVPADI RLNPRRLPDL VSSCRSRPAL SPLGDIDFCP PNPGPDGPRR
     RGRKPTKAKR DGPPRPRGRP RIRPLEGPAM AGPASITTDG AKKPRGRGRG RGRKAEEMGG
     TRLEPLKPLK IKLSVPKAGE GLGAPSNDVI SGVDHNSLDS NLTREKIEAK IKEVEEKQPE
     MKSGFMASFL DFLKSGKRHP PLYQAGLTPP LSPPKSVPAS VPTRGLQPPP PTVPTVPHPA
     PSGPFGLGGA LEAAESEGLG LGCPSPCKRL DEELKRNLET LPSFSSDEED SVAKNRDLQE
     SISSAISALD DPPLTGPKDT STPEEPPLDT GPTASGPPPL PSLPSSNSSG TPEPPLLEEK
     PPPTPPPAPT PQPAPPPPPP PPPVPALPSP TPLVTPVASS PPPPPPPPPP PPALPSPPPP
     PPPAPTTVPP VAPPEEPPAP SPEDPEPPDA RPLHLAKKQE TAAVCGETDE EAGESGGEGI
     FRERDEFVIR AEDIPSLKLA LQTGREPPPI WRVQKALLQK FTPEIKDGQR QFCATSNYLG
     YFGDAKNRYQ RLYVKFLENV NKKDYVRVCA RKPWHRPPLP VRRSGQTKGP TPVGGNSAPP
     SKVQAPPPKP ETPEKMTSEK PPEPAPEPAV PEPPAPEKPS PPRPVEKEKE KEKEKEKEKE
     RVTRPLRSER ATSGRQMRTD RSLATGQSTT SRLPKARPSK VKAEPPPKKR KKWLKEAVGN
     ASAGDGPGGS SSDSESSPGA PSEDERAVPG RLLKTRAMRE MYRSYVEMLV STALDPDMIQ
     ALEDTHDELY LPPMRKIDGL LNEHKKKVLK RLSLSPALQD ALHTFPQLQV EQTGEGSPEE
     GAVRLRPAGE PYNRKTLSKL KRSVVRAQEF KVELEKSGYY TLYHSLHHYK YHTFLRCRDQ
     TLAIEGGAED LGQEEVVQQC MRNQPWLEQL FDSFSDLLAQ AQAHSRCG
//
ID   PNKD_MOUSE              Reviewed;         385 AA.
AC   Q69ZP3; Q3TLE6; Q6PD45; Q8BRV8; Q920D4; Q9CSF5; Q9D765; Q9JJA3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Probable hydrolase PNKD;
DE            EC=3.-.-.-;
DE   AltName: Full=Myofibrillogenesis regulator 1;
DE            Short=MR-1;
DE   AltName: Full=Paroxysmal nonkinesiogenic dyskinesia protein;
GN   Name=Pnkd; Synonyms=Brp17, Kiaa1184, Mr1, Tahccp2;
GN   ORFNames=Fksg19, MNCb-5687;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2), AND INDUCTION.
RX   PubMed=15188498;
RA   Liu M., Liu Y., Cheng J., Zhang S.-L., Wang L., Shao Q., Zhang J.,
RA   Yang Q.;
RT   "Transactivating effect of hepatitis C virus core protein: a
RT   suppression subtractive hybridization study.";
RL   World J. Gastroenterol. 10:1746-1749(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S.,
RA   Hashimoto K.;
RT   "Isolation of full-length cDNA clones from mouse brain cDNA library
RT   made by oligo-capping method.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Wang Y.-G., Gong L.;
RT   "Cloning of FKSG19, a novel gene expressed in ovarian tumour tissue.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RA   Hu Y., Li T., Wang Y.;
RT   "Cloning and functional analysis of Mus musculus myofibrillogenesis
RT   regulator 1 (MR-1).";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Pancreatic islet;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] (PARTIAL ISOFORM 4).
RC   STRAIN=C57BL/6J; TISSUE=Aorta, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=15496428; DOI=10.1093/hmg/ddh330;
RA   Lee H.-Y., Xu Y., Huang Y., Ahn A.H., Auburger G.W., Pandolfo M.,
RA   Kwiecinski H., Grimes D.A., Lang A.E., Nielsen J.E., Averyanov Y.,
RA   Servidei S., Friedman A., Van Bogaert P., Abramowicz M.J., Bruno M.K.,
RA   Sorensen B.F., Tang L., Fu Y.-H., Ptacek L.J.;
RT   "The gene for paroxysmal non-kinesigenic dyskinesia encodes an enzyme
RT   in a stress response pathway.";
RL   Hum. Mol. Genet. 13:3161-3170(2004).
RN   [9]
RP   TRANSGENIC MICE, AND FUNCTION.
RX   PubMed=17420335; DOI=10.1161/HYPERTENSIONAHA.106.085399;
RA   Li H.-L., She Z.-G., Li T.-B., Wang A.-B., Yang Q., Wei Y.-S.,
RA   Wang Y.-G., Liu D.-P.;
RT   "Overexpression of myofibrillogenesis regulator-1 aggravates cardiac
RT   hypertrophy induced by angiotensin II in mice.";
RL   Hypertension 49:1399-1408(2007).
CC   -!- FUNCTION: Probable hydrolase that plays an aggravative role in the
CC       development of cardiac hypertrophy via activation of the NF-kappa-
CC       B signaling pathway.
CC   -!- SUBUNIT: Isoform 2 interacts with the sarcomeric proteins, MRLC2,
CC       MYOM1 and ENO3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Membrane; Peripheral membrane
CC       protein.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus.
CC   -!- SUBCELLULAR LOCATION: Isoform 4: Mitochondrion (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q69ZP3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q69ZP3-2; Sequence=VSP_027743, VSP_027744;
CC         Note=Contains a phosphoserine at position 121 (By similarity);
CC       Name=3;
CC         IsoId=Q69ZP3-3; Sequence=VSP_027742;
CC       Name=4;
CC         IsoId=Q69ZP3-4; Sequence=VSP_027741;
CC   -!- TISSUE SPECIFICITY: Expressed in many discrete areas of the brain.
CC   -!- INDUCTION: By Hepatitis C virus core protein.
CC   -!- PTM: Isoform 2 is phosphorylated at Ser-121 upon DNA damage,
CC       probably by ATM or ATR (By similarity).
CC   -!- MISCELLANEOUS: Mice overexpressing Pnkd infused with angiotensin
CC       II develop greater cardiac hypertrophy as well as increased
CC       cardiac inflammation and fibrosis, compared with angiotensin II-
CC       infused normal mice. In these mice, Pnkd overexpression promote
CC       nuclear factor kappa B activation.
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC       Glyoxalase II family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC30873.1; Type=Erroneous initiation;
CC       Sequence=BAD32403.1; Type=Erroneous initiation;
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DR   EMBL; AY039041; AAK83447.1; -; mRNA.
DR   EMBL; AY039042; AAK83448.1; -; Genomic_DNA.
DR   EMBL; AB041609; BAA95092.1; -; mRNA.
DR   EMBL; AF318058; AAL25717.1; -; mRNA.
DR   EMBL; AY299972; AAP58373.1; -; mRNA.
DR   EMBL; AK173125; BAD32403.1; ALT_INIT; mRNA.
DR   EMBL; AK009545; BAB26351.1; -; mRNA.
DR   EMBL; AK012976; BAB28577.2; -; mRNA.
DR   EMBL; AK041238; BAC30873.1; ALT_INIT; mRNA.
DR   EMBL; AK166548; BAE38846.1; -; mRNA.
DR   EMBL; BC008274; AAH08274.1; -; mRNA.
DR   EMBL; BC058945; AAH58945.1; -; mRNA.
DR   EMBL; BC116236; AAI16237.1; -; mRNA.
DR   EMBL; BC116237; AAI16238.1; -; mRNA.
DR   IPI; IPI00121559; -.
DR   IPI; IPI00187405; -.
DR   IPI; IPI00453946; -.
DR   IPI; IPI00464245; -.
DR   RefSeq; NP_001034598.1; NM_001039509.1.
DR   RefSeq; NP_064383.1; NM_019999.2.
DR   RefSeq; NP_079856.2; NM_025580.2.
DR   UniGene; Mm.384726; -.
DR   HSSP; Q16775; 1QH5.
DR   ProteinModelPortal; Q69ZP3; -.
DR   SMR; Q69ZP3; 119-384.
DR   STRING; Q69ZP3; -.
DR   PhosphoSite; Q69ZP3; -.
DR   Ensembl; ENSMUST00000027370; ENSMUSP00000027370; ENSMUSG00000026179.
DR   Ensembl; ENSMUST00000087225; ENSMUSP00000084477; ENSMUSG00000026179.
DR   Ensembl; ENSMUST00000087226; ENSMUSP00000084478; ENSMUSG00000026179.
DR   GeneID; 56695; -.
DR   KEGG; mmu:56695; -.
DR   UCSC; uc007blt.1; mouse.
DR   CTD; 56695; -.
DR   MGI; MGI:1930773; Pnkd.
DR   eggNOG; maNOG16824; -.
DR   GeneTree; ENSGT00530000063033; -.
DR   HOVERGEN; HBG001152; -.
DR   OMA; GHEYAED; -.
DR   OrthoDB; EOG412M5W; -.
DR   PhylomeDB; Q69ZP3; -.
DR   NextBio; 313119; -.
DR   ArrayExpress; Q69ZP3; -.
DR   Bgee; Q69ZP3; -.
DR   CleanEx; MM_MR1; -.
DR   CleanEx; MM_PNKD; -.
DR   Genevestigator; Q69ZP3; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004416; F:hydroxyacylglutathione hydrolase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001279; Blactmase-like.
DR   InterPro; IPR017782; Hydroxyacylglutathione_Hdrlase.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   SMART; SM00849; Lactamase_B; 1.
DR   TIGRFAMs; TIGR03413; GSH_gloB; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Hydrolase; Membrane; Metal-binding;
KW   Mitochondrion; Nucleus; Phosphoprotein; Zinc.
FT   CHAIN         1    385       Probable hydrolase PNKD.
FT                                /FTId=PRO_0000299550.
FT   REGION      291    293       Substrate (By similarity).
FT   REGION      376    379       Substrate (By similarity).
FT   METAL       172    172       Zinc 1 (By similarity).
FT   METAL       174    174       Zinc 1 (By similarity).
FT   METAL       176    176       Zinc 2 (By similarity).
FT   METAL       177    177       Zinc 2 (By similarity).
FT   METAL       229    229       Zinc 1 (By similarity).
FT   METAL       253    253       Zinc 1 (By similarity).
FT   METAL       253    253       Zinc 2 (By similarity).
FT   METAL       291    291       Zinc 2 (By similarity).
FT   VAR_SEQ       1     79       MAAVVAATALKGRGARNARVLRGILSGATANKASQNRTRAL
FT                                QSHSSPECKEEPEPLSPELEYIPRKRGKNPMKAVGLAW ->
FT                                MAWQGWLAPWLWVSGCWLLFFAFVLLLSPRSCQEQRGFRGL
FT                                LMTRSQRLLFRIG (in isoform 4).
FT                                /FTId=VSP_027741.
FT   VAR_SEQ      79     79       W -> WAIGFPCGILFFVLTKQEVDKDRLKQMKARQNMRVS
FT                                NTGE (in isoform 3).
FT                                /FTId=VSP_027742.
FT   VAR_SEQ      80    142       YSLYTRTWLGYLFYRQQLRRARNRYPKGHSKTQPRLFNGVK
FT                                VLPIPVLSDNYSYLIIDTQAGL -> AIGFPCGILFFVLTK
FT                                QEVDKDRLKQMKARQNMRVSNTGEYESQRYRASPQQAQFPE
FT                                VGSGAQT (in isoform 2).
FT                                /FTId=VSP_027743.
FT   VAR_SEQ     143    385       Missing (in isoform 2).
FT                                /FTId=VSP_027744.
FT   CONFLICT     17     17       N -> H (in Ref. 3; AAL25717).
SQ   SEQUENCE   385 AA;  43017 MW;  2327D63BFDDA849A CRC64;
     MAAVVAATAL KGRGARNARV LRGILSGATA NKASQNRTRA LQSHSSPECK EEPEPLSPEL
     EYIPRKRGKN PMKAVGLAWY SLYTRTWLGY LFYRQQLRRA RNRYPKGHSK TQPRLFNGVK
     VLPIPVLSDN YSYLIIDTQA GLAVAVDPSD PRAVQASIEK ERVNLVAILC THKHWDHSGG
     NRDLSRRHRD CRVYGSPQDG IPYLTHPLCH QDVVSVGRLQ IRALATPGHT QGHLVYLLDG
     EPYKGPSCLF SGDLLFLSGC GRTFEGTAET MLSSLDTVLD LGDDTLLWPG HEYAEENLGF
     AGVVEPENLA RERKMQWVQR QRMERKSTCP STLGEERAYN PFLRTHCLEL QEALGPGPGP
     TSDDGCSRAQ LLEELRRLKD MHKSK
//
ID   Q69ZP8_MOUSE            Unreviewed;      1200 AA.
AC   Q69ZP8;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   08-MAR-2011, entry version 35.
DE   SubName: Full=MKIAA1172 protein;
DE   Flags: Fragment;
GN   Name=Scaf4; Synonyms=Sfrs15, Srsf15, mKIAA1172;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
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DR   EMBL; AK173120; BAD32398.1; -; mRNA.
DR   IPI; IPI00380738; -.
DR   UniGene; Mm.439811; -.
DR   ProteinModelPortal; Q69ZP8; -.
DR   Ensembl; ENSMUST00000039280; ENSMUSP00000044472; ENSMUSG00000022983.
DR   MGI; MGI:2146350; Scaf4.
DR   eggNOG; roNOG06735; -.
DR   InParanoid; Q69ZP8; -.
DR   OrthoDB; EOG498V17; -.
DR   ArrayExpress; Q69ZP8; -.
DR   Bgee; Q69ZP8; -.
DR   Genevestigator; Q69ZP8; -.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   InterPro; IPR006903; DUF618.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR006569; RNA_polymerase_II_lsu_CTD.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Gene3D; G3DSA:1.25.40.90; ENTH_VHS; 1.
DR   Pfam; PF04818; DUF618; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00582; RPR; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF48464; ENTH_VHS; 1.
DR   PROSITE; PS51391; CID; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   1200 AA;  130347 MW;  AD8BBC1093A58ADD CRC64;
     VTGGPGAAAA AAATRANMDA VNAFNQELFS LMDMKPPISR AKMILITKAA IKAIKLYKHV
     VQIVEKFIKK CKPEYKVPGL YVIDSIVRQS RHQFGTDKDV FGPRFSKNIT ATFQYLYLCP
     SEDKSKIVRV LNLWQKNGVF KIEIIQPLLD MAAGTSNAAP VAENVTNNEG SPPPPVKISS
     ELAQAPTNSM PTVAQLPSSD AFAAVAQLFQ TTQGQQLQQI LQTFQQPPQP QSPALDSAVM
     AQVQAITAQL KTAPTQPPEQ KTAFDKKLLD RFDYDDEPEA VEDSKKEDAA AISTAALATA
     APPAPTAATP AVATAVPVPS ATSPPPPQTP FGYPGDGVQQ PACTQHQSMD QFQPRMMPIQ
     QDTMHHQVPL PPNGQMPGFG LLSAPPPFPP MPQPGMPQPG MAQPGLAQPG MAQPTMPQPG
     MPQPGMPQPG MAQPGLAQPG MAQPGMPQPA MPQPAMPQPG MAQPGVSPAP PVQPTFQSTF
     QPQNEPHSQK PHQQVEMEVE QPCVTEVKRH VPESRKSRSR SPKRRRSRSG SRSRRSRHRR
     SRSRSRDRRR HSPRSRSQER RDREKERERR QKGLPQIKSE TASVCSTTLW VGQLDKRTTQ
     QDVASLLEEF GPIESINMIP PRGCAYIVMV HRQDAYRALQ KLSRGNYKVN QKSIKIAWAL
     NKGIKADYKQ YWDVELGVTY IPWDKVKAEE LESFCEGGML DSDTLNPDWK GIPKKPDNEV
     AQNGGAETSH TEPVSPIPKP VPVPVPPIPV PAPITVPPPQ VPPHQPGPPV VGALQPPAFT
     PPLGMPPPGF GPGVPPPPPP PPFLRPGFNP MHLPPGFLPP GPPPPITPPV SIPPPHTPPI
     SIPNLVSGAR GNAESGDSAK MYGSAGPPAA PTSLPTPPVT QPVSLLGTQG VAPGPVIGLQ
     APSTGLLGAR PGLIPLQRPP GMPPPHLQRF PMMPPRPMPP HMMHRGPPPG PGGFAMPPPH
     GMKGPFPPHG PFVRPGGMPG LGGPGPGPGA SEDRDGRQQQ PQQQPPPQQQ QQQQQPQQPP
     QQSPSQQPAP AQQQPPQFRN DSRQQFNSGR DQERFGRRSF GSRVENDRER YGSRNDDRDN
     SNRERREWGR RSPDRDRHRD LEERSRRSSG HRDRDRDSRD RESRREKEEN RKEKHEVADR
     AGGNKAVEPP LSQVGTIDTV SELNKGEAMA TVVKPEESPA EATSPVGPEK DPGSAAEPPR
//
ID   HECD1_MOUSE             Reviewed;        2618 AA.
AC   Q69ZR2;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=E3 ubiquitin-protein ligase HECTD1;
DE            EC=6.3.2.-;
DE   AltName: Full=HECT domain-containing protein 1;
DE   AltName: Full=Protein open mind;
GN   Name=Hectd1; Synonyms=Kiaa1131, Opm;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1045-2618.
RC   TISSUE=Thymus;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1395, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=17442300; DOI=10.1016/j.ydbio.2007.03.018;
RA   Zohn I.E., Anderson K.V., Niswander L.;
RT   "The Hectd1 ubiquitin ligase is required for development of the head
RT   mesenchyme and neural tube closure.";
RL   Dev. Biol. 306:208-221(2007).
CC   -!- FUNCTION: Probable E3 ubiquitin-protein ligase which accepts
CC       ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a
CC       thioester and then directly transfers the ubiquitin to targeted
CC       substrates. Involved in development of the head mesenchyme and
CC       neural tube closure.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with IGSF1 (By similarity).
CC   -!- DEVELOPMENTAL STAGE: Ubiquitously expressed throughout early
CC       development of the embryo.
CC   -!- DISRUPTION PHENOTYPE: Perinatal lethality, exencephaly, impaired
CC       neural fold elevation, abnormal head mesenchyme morhology and
CC       defects in eye and cranial vault morphology.
CC   -!- SIMILARITY: Contains 4 ANK repeats.
CC   -!- SIMILARITY: Contains 1 HECT (E6AP-type E3 ubiquitin-protein
CC       ligase) domain.
CC   -!- SIMILARITY: Contains 1 MIB/HERC2 domain.
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DR   EMBL; AC159644; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC157213; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK173106; BAD32384.1; -; mRNA.
DR   IPI; IPI00762434; -.
DR   UniGene; Mm.249391; -.
DR   ProteinModelPortal; Q69ZR2; -.
DR   SMR; Q69ZR2; 366-486, 1271-1343, 2134-2613.
DR   STRING; Q69ZR2; -.
DR   Ensembl; ENSMUST00000042052; ENSMUSP00000046766; ENSMUSG00000035247.
DR   UCSC; uc007nmx.1; mouse.
DR   MGI; MGI:2384768; Hectd1.
DR   HOGENOM; HBG315444; -.
DR   HOVERGEN; HBG067533; -.
DR   InParanoid; Q69ZR2; -.
DR   OrthoDB; EOG4R501T; -.
DR   ArrayExpress; Q69ZR2; -.
DR   Bgee; Q69ZR2; -.
DR   Genevestigator; Q69ZR2; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:InterPro.
DR   GO; GO:0001843; P:neural tube closure; IMP:UniProtKB.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR000569; HECT.
DR   InterPro; IPR010606; Mib_Herc2.
DR   InterPro; IPR012919; Sad1_UNC_C.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 2.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF06701; MIB_HERC2; 1.
DR   Pfam; PF07738; Sad1_UNC; 1.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF49785; Gal_bind_like; 1.
DR   SUPFAM; SSF56204; HECT; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS51416; MIB_HERC2; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Ligase; Phosphoprotein; Repeat; Ubl conjugation pathway.
FT   CHAIN         1   2618       E3 ubiquitin-protein ligase HECTD1.
FT                                /FTId=PRO_0000396127.
FT   REPEAT      396    425       ANK 1.
FT   REPEAT      427    456       ANK 2.
FT   REPEAT      460    492       ANK 3.
FT   REPEAT      580    613       ANK 4.
FT   DOMAIN     1271   1343       MIB/HERC2.
FT   DOMAIN     2156   2618       HECT.
FT   REGION     2034   2108       K-box (By similarity).
FT   COMPBIAS    496    499       Poly-Lys.
FT   COMPBIAS   1355   1654       Ser-rich.
FT   COMPBIAS   1750   1757       Poly-Glu.
FT   ACT_SITE   2587   2587       Glycyl thioester intermediate (By
FT                                similarity).
FT   MOD_RES     633    633       Phosphoserine (By similarity).
FT   MOD_RES    1395   1395       Phosphoserine.
FT   MOD_RES    1493   1493       Phosphoserine (By similarity).
FT   MOD_RES    1777   1777       Phosphoserine (By similarity).
FT   CONFLICT   1070   1070       F -> S (in Ref. 2; BAD32384).
FT   CONFLICT   2472   2474       Missing (in Ref. 2; BAD32384).
SQ   SEQUENCE   2618 AA;  290086 MW;  8A06C9F973B11AFA CRC64;
     MADVDPDTLL EWLQMGQGDE RDMQLIALEQ LCMLLLMSDN VDRCFETCPP RTFLPALCKI
     FLDESAPDNV LEVTARAITY YLDVSAECTR RIVGVDGAIK ALCNRLVVVE LNNRTSRDLA
     EQCVKVLELI CTRESGAVFE AGGLNCVLTF IRDSGHLVHK DTLHSAMAVV SRLCGKMEPQ
     DSSLEICVES LSSLLKHEDH QVSDGALRCF ASLADRFTRR GVDPAPLAKH GLTEELLSRM
     AAAGGTVSGP SSACKPGRST TGAPSAAADS KLSNQVSTIV SLLSTLCRGS PLVTHDLLRS
     ELPDSIESAL QGDERCVLDT MRLVDLLLVL LFEGRKALPK SSAGSTGRIP GLRRLDSSGE
     RSHRQLIDCI RSKDTDALID AIDTGAAFEV NFMDDVGQTL LNWASAFGTQ EMVEFLCERG
     ADVNRGQRSS SLHYAACFGR PQVAKTLLRH GANPDLRDED GKTPLDKARE RGHSEVVAIL
     QSPGDWMCPV NKGDDKKKKD TNKDEEECNE PRGDPEMAPL YLKRLLPVFA QTFQHTMLPS
     IRKASLALIR KMIHFCSEAL LKEVCDSDVG HNLPTTLVEI TATVLDQEDD DDGHLLALQI
     IRDLVDKGGD IFLDQLARLG VISKVSALAG PSSDDENEEE SKPEKEDEPQ EDAKELQQGK
     PYHWRDWSII RGRDCLYIWS DAAALELSNG SNGWFRFILD GKLATMYSSG SPEGGSDSSE
     SRSEFLEKLQ RARGQVKPST SSQPILSAPG PTKLTVGNWS LTCLKEGEIA IHNSDGQQAT
     ILKEDLPGFV FESNRGTKHS FTAETSLGSE FVTGWTGKRG RKLKSKLEKT KQKVRTMARD
     LYDDHFKAVE SMPRGVVVTL RNIATQLESS WELHTNRQCI EGENTWRDLM KTALENLIVL
     LKDENTISPY EMCSSGLVQA LLTVLNNVSI FRATKQKQNE VLVERINVFK TAFSESEDDE
     SYSRPAVALI RKLIAVLESI ERLPLHLYDT PGSTYNLQIL TRRLRFRLER APGETSLIDR
     TGRMLKMEPL ATVESLEQYL LKMVAKQWYD FDRSSFVFVR KLREGQNFIF RHQHDFDENG
     IIYWIGTNAK TAYEWVNPAA YGLVVVTSSE GRNLPYGRLE DILSRDNSAL NCHSNDDKNA
     WFAIDLGVWV IPSAYTLRHA RGYGRSALRN WVFQVSKDGQ NWTSLYTHVD DCSLNEPGST
     ATWPLDPAKD EKQGWRHVRL KQMGKNASGQ THYLSLSGFE LYGTVNGVCE DQLGKAAKEA
     EANLRRQRRL VRSQVLKYMV PGARVIRGLD WKWRDQDGSP QGEGTVTGEL HNGWIDVTWD
     AGGSNSYRMG AEGKFDLKLA PGYDPDTVAS PKPVSSTVSG TTQSWSSLVK NNCPDKTSAA
     AGSSSRKGSS SSVCSVASSS DISLASTKTE RRSEIVMEHS IVSGADVHEP IVVLSSAENV
     PQTEVGSSSS ASTSTLTAET GSENAERKLG PDSSVRAPGE SSAISMGIVS VSSPDVSSVS
     ELTNKEAASQ RPLSSSASNR LSVSSLLAAG APMSSSASVP NLSSRETSSL ESFVRRVANI
     ARTNATNNMN LSRSSSDNNT NTLGRNVMST ATSPLMGAQS FPNLTTPGTT STVTMSTSSV
     TSSSNVATAT TVLSVGQSLS NTLTTSLTST SSESDTGQEA EYSLYDFLDS CRASTLLAEL
     DDDEDLPEPD EEDDENEDDN QEDQEYEEVM ILRRPSLQRR AGSRSDVTHH VVTSQLPQVP
     SGAGSRPVGE QEEEEYETKG GRRRAWDDDY VLKRQFSALV PAFDPRPGRT NVQQTTDLEI
     PPPGTPHSEL LEEVECTPSP RLALTLKVTG LGTTREVELP LTNFRSTIFY YVQKLLQLSC
     NGNVKSDKLR RIWEPTYTIM YREMKDSDKE KENGKMGCWS IEHVEQYLGT DELPKNDLIT
     YLQKNADAAF LRHWKLTGTN KSIRKNRNCS QLIAAYKDFC EHGTKSGLNQ GAISSLQSSD
     ILNLTKEQPQ AKAGNGQSPC GVEDVLQLLR ILYIVASDPY SRISQEDGDE QPQFTFPPDE
     FTSKKITTKI LQQIEEPLAL ASGALPDWCE QLTSKCPFLI PFETRQLYFT CTAFGASRAI
     VWLQNRREAT VERTRTTSSV RRDDPGEFRV GRLKHERVKV PRGESLMEWA ENVMQIHADR
     KSVLEVEFLG EEGTGLGPTL EFYALVAAEF QRTDLGTWLC DDNFPDDESR HVDLGGGLKP
     PGYYVQRSCG LFTAPFPQDS DELERITKLF HFLGIFLAKC IQDNRLVDLP ISKPFFKLMC
     MGDIKSNMSK LIYESRGDRD LHCTESQSEA STEEGHDSLS VGSFEEDSKS EFILDPPKPK
     PPAWFNGILT WEDFELVNPH RARFLKEIKD LAIKRRQILG NKSLSEDEKN TKLQELVLRN
     PSGSGPPLSI EDLGLNFQFC PSSRIYGFTA VDLKPSGEDE MITMDNAEEY VDLMFDFCMH
     TGIQKQMEAF RGNVDGFNKV FPMEKLSSFS HEEVQMILCG NQSPSWAAED IINYTEPKLG
     YTRDSPGFLR FVRVLCGMSS DERKAFLQFT TGCSTLPPGG LANLHPRLTV VRKVDATDAS
     YPSVNTCVHY LKLPEYSSEE IMRERLLAAT MEKGFHLN
//
ID   CC063_MOUSE             Reviewed;        1610 AA.
AC   Q69ZR9; Q9CUD3;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   08-FEB-2011, entry version 36.
DE   RecName: Full=Uncharacterized protein C3orf63 homolog;
GN   Name=D14Abb1e; Synonyms=Kiaa1105;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-545.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1319-1610.
RC   TISSUE=Embryonic intestine;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
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DR   EMBL; AC154327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CAAA01054285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK016751; BAB30409.2; -; mRNA.
DR   EMBL; AK173099; BAD32377.1; -; mRNA.
DR   IPI; IPI00669506; -.
DR   RefSeq; NP_001108351.1; NM_001114879.1.
DR   RefSeq; NP_083221.1; NM_028945.1.
DR   UniGene; Mm.247767; -.
DR   ProteinModelPortal; Q69ZR9; -.
DR   PhosphoSite; Q69ZR9; -.
DR   PRIDE; Q69ZR9; -.
DR   Ensembl; ENSMUST00000059031; ENSMUSP00000050618; ENSMUSG00000040651.
DR   GeneID; 218850; -.
DR   KEGG; mmu:218850; -.
DR   UCSC; uc007stv.1; mouse.
DR   CTD; 218850; -.
DR   MGI; MGI:1921694; D14Abb1e.
DR   eggNOG; roNOG10640; -.
DR   GeneTree; ENSGT00530000063735; -.
DR   HOGENOM; HBG506605; -.
DR   HOVERGEN; HBG061247; -.
DR   InParanoid; Q69ZR9; -.
DR   NextBio; 376431; -.
DR   ArrayExpress; Q69ZR9; -.
DR   Bgee; Q69ZR9; -.
DR   CleanEx; MM_D14ABB1E; -.
DR   Genevestigator; Q69ZR9; -.
DR   InterPro; IPR022188; DUF3715.
DR   Pfam; PF12509; DUF3715; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1610       Uncharacterized protein C3orf63 homolog.
FT                                /FTId=PRO_0000295729.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      94     94       Phosphoserine (By similarity).
FT   MOD_RES     628    628       Phosphoserine (By similarity).
FT   MOD_RES     631    631       Phosphoserine (By similarity).
FT   MOD_RES     812    812       Phosphothreonine (By similarity).
FT   MOD_RES     921    921       Phosphoserine (By similarity).
FT   MOD_RES    1059   1059       Phosphoserine (By similarity).
FT   MOD_RES    1508   1508       Phosphoserine (By similarity).
SQ   SEQUENCE   1610 AA;  181396 MW;  B8DDF5E02905CE9F CRC64;
     MATAAETEAP STDASWKSRG GGGGDDGMKP ALPELESSLQ NGGGDGGGGA GPEETAAAEA
     ARSYGHEQPQ QTSEAAAAAL PKGAEEPERP FRRSFQIPRK SREKKALFQP LTPGSREFED
     VLNILHSSYL EPSSVTYFNY RRACLIHNEL LEKEFTEKRR ELKFDGRLDK ELSESYAFLM
     VDRYQVQSIC EKGLQVGQSK ITVLGSPSMG IYLCRYADLL QANPLEAGAV GDVVIFKIMK
     GKIKSIYDPL SVKSLESMLS KNALDPTPKH ECHVSKNASR ITSLLAYRAY ELTQYYFYEY
     GFDEVRRRPR HVCPYAVVSF TYKDDVQTPK FLSPLRSNSF NADRNIDKFN YTLWKGQLLN
     KGKLLCYISL RSANRAFLPV KLPEKLDVET VMSIDCLKQK IPPSFFYKDT YVGPNEVLKN
     GMYCSLYEVV EKTRIGSNME CLLQKLEKEK LVLVKPLGDR GYLFLLSPFQ MVSPYEHQTV
     KSRILHALFL FQEPRCLIIT QKGIMNTTPL EKPENLADIL KITQFLQFSL IQCRKEFKTI
     NTINFHSVVE KYVSEFFKRG FGSGKREFFM FSYDSRLDDR KFLYSAPRNK SHIDDCLHTY
     IYQPEMYQLS IFKLKELFEE NWRRQQFSPL SDYEGQEEEL NGSKMKFGKR NNSRDETTEP
     EQQKSSHSLD YDKDRVKELI NLIQCTKKNV GGDPDPEDTK SKNVLKRKLE DLPENMRKFA
     KTSNSTESCH LYEESPQSIG LLGQDPNLRV QQEDSGNTGD IHKLYNWLSE ALANARHSDG
     FLTETVNKAL GLSSSGAYEE LKQKCDYELN STLDKKESEQ PACTKIENVH FKDAQSPLLE
     VDAASVKYPP LLSSSEVGIN HKLHCKEDPN LINVNNFEGC SLCPTVSIEH GFLRQHSKSN
     DDEETEIHWK LIPITGGNAG SPEDQHGKHG EKQTPDTLKG TTEEDTVTAG QAMAVEEQCV
     PAAELPRVSE ITENTVLGEF HLFSRKVEEI LKEKNVSYVS AISTPIFSAQ EKMNRLSEFI
     HSNTSKAGVE EFVDGLHEKL NTVVITASAK GVSLPPAVSA NHSHAAAALA SLGRRVVSIS
     SSDFSAKELF EPLCSEHLKD NNSNEQYSSS VEVEMNRPHH CKELMLTSDH TVPGDTVLEP
     TEKEITKSPS DITISAQPAL SNFISQLEPE VFNSLVKIMK DVQKNTVKFY IHEEEESVLC
     KEIKEYLTKL GNTECHPDQF LERRSNLDKL LIIIQNEDIA GFIHKVPGLV TLKKLPCVSF
     AGVDSLDDVK NHTYNELFVS GGFIVSDESI LNLEVVTIES LKIFLTFLEE LSTPEGKWQW
     KIHCKFQKKL KELGRMNTKA LSLLTLLNVY QKKHLVEILS YHSCDSQTRN APEMDCLIRL
     QAQNIQQRHI VFLTEKNIKM VSSYTDNGIV VATTEDFMQN FTSLVGYHNS VTEESLPPLL
     GANENLESQS ALLENDEKDE EDMSLDSGDE ISHIEVFSNV HSEILAGETK GSSGTDQKKN
     IQIELQSSLD VQNSLLEDKT YLIDCEASAP IDRVCSEGES SNSAEQDAYS DFQADQNQLQ
     MSHQCSHFNV LTHQTFLGTP YALSSTRSQE NENYFLSAYK NSGTEKSPLS
//
ID   PZRN3_MOUSE             Reviewed;        1063 AA.
AC   Q69ZS0; Q91Z03; Q9QY54; Q9QY55;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 3.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=E3 ubiquitin-protein ligase PDZRN3;
DE            EC=6.3.2.-;
DE   AltName: Full=PDZ domain-containing RING finger protein 3;
DE   AltName: Full=Semaphorin cytoplasmic domain-associated protein 3;
DE            Short=Protein SEMACAP3;
GN   Name=Pdzrn3; Synonyms=Kiaa1095, Semcap3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH
RP   MUSK AND UBE2D2, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AUTOUBIQUITINATION, AND MUTAGENESIS OF CYS-18 AND CYS-38.
RX   PubMed=17576800; DOI=10.1083/jcb.200610060;
RA   Lu Z., Je H.S., Young P., Gross J., Lu B., Feng G.;
RT   "Regulation of synaptic growth and maturation by a synapse-associated
RT   E3 ubiquitin ligase at the neuromuscular junction.";
RL   J. Cell Biol. 177:1077-1089(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA   Wang L.-H., Strittmatter S.M.;
RT   "Cloning and characterization of a novel PDZ domain containing protein
RT   interacting with the transmembrane semaphorin, M-semF.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-1063 (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 392-1063.
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=17118964; DOI=10.1242/jcs.03290;
RA   Ko J.A., Kimura Y., Matsuura K., Yamamoto H., Gondo T., Inui M.;
RT   "PDZRN3 (LNX3, SEMCAP3) is required for the differentiation of C2C12
RT   myoblasts into myotubes.";
RL   J. Cell Sci. 119:5106-5113(2006).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase. Plays an important role in
CC       regulating the surface level of MUSK on myotubes. Mediates the
CC       ubiquitination of MUSK, promoting its endocytosis and lysosomal
CC       degradation. Might contribute to terminal myogenic
CC       differentiation.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with NLGN1 and EFNB2 (By similarity). Interacts
CC       with UBE2D2 and with MUSK via the first PDZ domain. In myotubes,
CC       the interaction between PDZRN3 and MUSK is enhanced upon agrin
CC       stimulation.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=SEMCAP-3A, PDZRN3B;
CC         IsoId=Q69ZS0-1; Sequence=Displayed;
CC       Name=2; Synonyms=SEMCAP-3B;
CC         IsoId=Q69ZS0-2; Sequence=VSP_012610;
CC       Name=3; Synonyms=PDZRN3A;
CC         IsoId=Q69ZS0-3; Sequence=VSP_039769;
CC   -!- TISSUE SPECIFICITY: Highly expressed in skeletal and cardiac
CC       muscle and at lower levels in spinal cord and brain (at protein
CC       level). Also expressed in kidney and lung. In muscles,
CC       concentrated at the neuromuscular junction (NMJ).
CC   -!- DEVELOPMENTAL STAGE: First detected at the NMJ at approximately
CC       16.5 dpc, when NMJs have just formed. As the NMJ grows and
CC       matures, expression levels increase in concert with that of
CC       acetylcholine receptors. Levels stay relatively high until 14 days
CC       after birth, but decrease significantly by 21 days. Up-regulated
CC       during myogenic differentiation in C2C12 cells and during injury-
CC       induced muscle regeneration.
CC   -!- DOMAIN: The RING-type zinc finger domain is required for E3 ligase
CC       activity.
CC   -!- PTM: Auto-ubiquitinated.
CC   -!- SIMILARITY: Contains 2 PDZ (DHR) domains.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SIMILARITY: Contains 1 TRAF-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH10329.1; Type=Erroneous termination; Positions=408; Note=Translated as Gln;
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DR   EMBL; HM560981; ADK56111.1; -; mRNA.
DR   EMBL; AF127084; AAF22131.1; -; mRNA.
DR   EMBL; AF127085; AAF22132.1; -; mRNA.
DR   EMBL; AK173098; BAD32376.1; -; mRNA.
DR   EMBL; BC010329; AAH10329.1; ALT_SEQ; mRNA.
DR   IPI; IPI00135609; -.
DR   IPI; IPI00551426; -.
DR   IPI; IPI00970713; -.
DR   RefSeq; NP_061372.2; NM_018884.2.
DR   UniGene; Mm.321654; -.
DR   ProteinModelPortal; Q69ZS0; -.
DR   SMR; Q69ZS0; 2-153, 245-515.
DR   STRING; Q69ZS0; -.
DR   PhosphoSite; Q69ZS0; -.
DR   PRIDE; Q69ZS0; -.
DR   Ensembl; ENSMUST00000075994; ENSMUSP00000075376; ENSMUSG00000035357.
DR   Ensembl; ENSMUST00000101117; ENSMUSP00000098676; ENSMUSG00000035357.
DR   GeneID; 55983; -.
DR   KEGG; mmu:55983; -.
DR   UCSC; uc009dcd.1; mouse.
DR   CTD; 55983; -.
DR   MGI; MGI:1933157; Pdzrn3.
DR   GeneTree; ENSGT00510000046421; -.
DR   HOGENOM; HBG445469; -.
DR   HOVERGEN; HBG053554; -.
DR   InParanoid; Q69ZS0; -.
DR   OrthoDB; EOG4T1HM7; -.
DR   NextBio; 311690; -.
DR   ArrayExpress; Q69ZS0; -.
DR   Bgee; Q69ZS0; -.
DR   CleanEx; MM_PDZRN3; -.
DR   Genevestigator; Q69ZS0; -.
DR   GermOnline; ENSMUSG00000035357; Mus musculus.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007528; P:neuromuscular junction development; IMP:UniProtKB.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR013323; SIAH-type.
DR   InterPro; IPR008974; TRAF-like.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   InterPro; IPR001293; Znf_TRAF.
DR   Gene3D; G3DSA:3.90.890.10; SIAH-type; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00595; PDZ; 2.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00228; PDZ; 2.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF50156; PDZ; 2.
DR   SUPFAM; SSF49599; Traf_like; 1.
DR   PROSITE; PS50106; PDZ; 2.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS50145; ZF_TRAF; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Ligase; Metal-binding; Repeat;
KW   Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1   1063       E3 ubiquitin-protein ligase PDZRN3.
FT                                /FTId=PRO_0000055918.
FT   DOMAIN      249    339       PDZ 1.
FT   DOMAIN      419    503       PDZ 2.
FT   ZN_FING      18     56       RING-type; degenerate.
FT   ZN_FING     100    158       TRAF-type.
FT   COILED      680    705       Potential.
FT   COMPBIAS    986    989       Poly-Arg.
FT   VAR_SEQ      82    133       Missing (in isoform 2).
FT                                /FTId=VSP_012610.
FT   VAR_SEQ     419    451       Missing (in isoform 3).
FT                                /FTId=VSP_039769.
FT   MUTAGEN      18     18       C->A: Loss of E3 ligase activity.
FT   MUTAGEN      38     38       C->A: Loss of E3 ligase activity.
FT   CONFLICT     82     82       C -> R (in Ref. 3; BAD32376).
FT   CONFLICT    199    199       V -> L (in Ref. 2; AAF22131/AAF22132).
FT   CONFLICT    596    596       S -> Y (in Ref. 2; AAF22131/AAF22132).
FT   CONFLICT    731    731       N -> Y (in Ref. 2; AAF22131/AAF22132).
FT   CONFLICT    823    823       A -> S (in Ref. 4; AAH10329).
FT   CONFLICT    912    912       V -> A (in Ref. 4; AAH10329).
FT   CONFLICT    938    938       R -> K (in Ref. 2; AAF22131/AAF22132).
SQ   SEQUENCE   1063 AA;  119401 MW;  AC87470326242BED CRC64;
     MGFELDRFDG DVDPDLKCAL CHKVLEDPLT TPCGHVFCAG CVLPWVVQEG SCPARCRGRL
     SAKELNHVLP LKRLILKLDI KCAHAARGCG RVVKLQDLPE HLERCDFAPA RCRHAGCGQL
     LLRRDVEAHM RDACDARPVG RCQEGCGLPL THGEQRAGGH CCARALRAHN GALQARLGAL
     HKALKKEALR AGKREKSLVA QLAAAQLELQ MTALRYQKKF TEYSARLDSL SRCVAAPPGG
     KGEETKSLTL VLHRDSGSLG FNIIGGRPCV DNQDGSSSEG IFVSKIVDSG PAAKEGGLQI
     HDRIIEVNGK DLSRATHDQA VEAFKTAKEP IVVQVLRRTP RTKMFTPASE SQLVDTGTQT
     DITFEHIMAL TKMSSPSPPV LDPYLLPEEH PASHDYYDPN DYMGDIHQDM DREELELEEV
     GLYRMNSQDK LGLTVCYRTD DEDDIGIYIS EIDPNSIAAK DGRIREGDRI IQINGIEVQN
     REEAVALLTS EENKNFSLLI ARPELQLDEG WMDDDRNDFL DDLHMDMLEE QHHQAMQFTA
     SVLQQKKHEE DGGTTDTATI LSNQHEKDSG VGRTDESTRN DESSEQENNG EDATASANPL
     AGQRKLTCSQ DTLGSGDLPF SNESFISADC TDVDYLGIPE DECERFRELL ELKCQVQSAS
     PYSLYYPSSP LDAAGKSDPE SVDKELELLN EELRSIELEC LSIVRAHKMQ QLKEQYRESW
     MLHHSGFRNY NTSVDVRRHE LSDITELPEK SDKDSSSAYN TGESCRSTPL TLEISPDNSL
     RRVAEGSSEG ATANIEAYRP SPKNLLAITE DPEVSTPSYN PSAKELDPSQ ALEIKERRGS
     DGSRSPTASP KLGNAYLPSY HHSPYKHAHI PAHAQHYQSY MHLIQQKSAV EYAQSQMSLV
     SMCKDLNSSN SVEPRMEWKV KIRSDGTRYI TKRPVRDRLL RERALKIREE RSGLTTDDDA
     MSEMKMGRYW SKEERKQHLV KAKEQRRRRE FMMQSRLDCL KEQQASDDRK EMNILELSHK
     KMMKKRNKKI FDNWMTIQEL LTHGTKSPDG TRVYNSFLSV TTV
//
ID   KAZRN_MOUSE             Reviewed;         779 AA.
AC   Q69ZS8; A2AC34; B1B0N1; Q8BIY2; Q8R1X4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   08-FEB-2011, entry version 52.
DE   RecName: Full=Kazrin;
GN   Name=Kaz; Synonyms=Kiaa1026;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=15337775; DOI=10.1083/jcb.200312123;
RA   Groot K.R., Sevilla L.M., Nishi K., DiColandrea T., Watt F.M.;
RT   "Kazrin, a novel periplakin-interacting protein associated with
RT   desmosomes and the keratinocyte plasma membrane.";
RL   J. Cell Biol. 166:653-659(2004).
RN   [6]
RP   SUBCELLULAR LOCATION, AND DEVELEOPMENTAL STAGE.
RX   PubMed=16086310; DOI=10.1002/dvdy.20519;
RA   Gallicano G.I., Foshay K., Pengetnze Y., Zhou X.;
RT   "Dynamics and unexpected localization of the plakin binding protein,
RT   kazrin, in mouse eggs and early embryos.";
RL   Dev. Dyn. 234:201-214(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350 AND SER-371, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Component of the cornified envelope of keratinocytes.
CC       May be involved in the interplay between adherens junctions and
CC       desmosomes. The function in the nucleus is not known.
CC   -!- SUBCELLULAR LOCATION: Cell junction. Nucleus. Cytoplasm,
CC       cytoskeleton. Note=In (PubMed:16086310) an antibody regognizing
CC       isoform 2 and isoform 3 has been used.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1;
CC         IsoId=Q69ZS8-1; Sequence=Displayed;
CC       Name=2; Synonyms=B;
CC         IsoId=Q69ZS8-2; Sequence=VSP_031905, VSP_031906, VSP_031907;
CC       Name=3; Synonyms=C;
CC         IsoId=Q69ZS8-3; Sequence=VSP_031904, VSP_031906, VSP_031907;
CC   -!- TISSUE SPECIFICITY: Expressed in skin interfollicular epidermis
CC       and hair follicles. Expressed in tongue epithelium basal
CC       suprabasal layers.
CC   -!- DEVELOPMENTAL STAGE: Expressed in eggs and early embryos. Detected
CC       in unfertilized eggs associated with the spindle apparatus and
CC       cytoskeletal sheets. As quickly as 5 min after egg activation,
CC       relocates to a diffuse peri-spindle position, followed 20-30 min
CC       later by localization to the presumptive cytokinetic ring. Before
CC       the blastocyst stage of development, associates with the nuclear
CC       matrix in a cell cycle-dependent manner, and also associates with
CC       the cytoplasmic actin cytoskeleton. After blastocyst formation, is
CC       found associating with cell-cell junctions, the cytoskeleton and
CC       nucleus.
CC   -!- SIMILARITY: Belongs to the kazrin family.
CC   -!- SIMILARITY: Contains 3 SAM (sterile alpha motif) domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32368.1; Type=Erroneous initiation;
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DR   EMBL; AK173090; BAD32368.1; ALT_INIT; mRNA.
DR   EMBL; AK052809; BAC35155.1; -; mRNA.
DR   EMBL; AL663037; CAM13390.1; -; Genomic_DNA.
DR   EMBL; BX537122; CAM13390.1; JOINED; Genomic_DNA.
DR   EMBL; BX537122; CAM27950.1; -; Genomic_DNA.
DR   EMBL; AL663037; CAM27950.1; JOINED; Genomic_DNA.
DR   EMBL; BC022941; AAH22941.1; -; mRNA.
DR   IPI; IPI00222264; -.
DR   IPI; IPI00403258; -.
DR   IPI; IPI00885597; -.
DR   RefSeq; NP_001103154.1; NM_001109684.1.
DR   RefSeq; NP_001103155.1; NM_001109685.1.
DR   RefSeq; NP_653114.3; NM_144531.3.
DR   UniGene; Mm.255986; -.
DR   UniGene; Mm.477412; -.
DR   ProteinModelPortal; Q69ZS8; -.
DR   SMR; Q69ZS8; 207-244, 453-513, 524-591.
DR   STRING; Q69ZS8; -.
DR   PhosphoSite; Q69ZS8; -.
DR   PRIDE; Q69ZS8; -.
DR   Ensembl; ENSMUST00000036476; ENSMUSP00000038835; ENSMUSG00000040606.
DR   Ensembl; ENSMUST00000070792; ENSMUSP00000069287; ENSMUSG00000040606.
DR   GeneID; 71529; -.
DR   KEGG; mmu:71529; -.
DR   UCSC; uc008vpv.1; mouse.
DR   MGI; MGI:1918779; 9030409G11Rik.
DR   GeneTree; ENSGT00550000074230; -.
DR   HOGENOM; HBG446942; -.
DR   HOVERGEN; HBG058718; -.
DR   InParanoid; Q69ZS8; -.
DR   NextBio; 333959; -.
DR   ArrayExpress; Q69ZS8; -.
DR   Bgee; Q69ZS8; -.
DR   CleanEx; MM_9030409G11RIK; -.
DR   Genevestigator; Q69ZS8; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR011510; SAM_2.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 3.
DR   Pfam; PF00536; SAM_1; 2.
DR   Pfam; PF07647; SAM_2; 1.
DR   SMART; SM00454; SAM; 3.
DR   SUPFAM; SSF47769; SAM_homology; 3.
DR   PROSITE; PS50105; SAM_DOMAIN; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Keratinization; Nucleus; Phosphoprotein; Repeat.
FT   CHAIN         1    779       Kazrin.
FT                                /FTId=PRO_0000322454.
FT   DOMAIN      450    515       SAM 1.
FT   DOMAIN      528    592       SAM 2.
FT   DOMAIN      616    683       SAM 3.
FT   COILED       79    261       Potential.
FT   MOD_RES     350    350       Phosphoserine.
FT   MOD_RES     371    371       Phosphoserine.
FT   VAR_SEQ       1     99       Missing (in isoform 3).
FT                                /FTId=VSP_031904.
FT   VAR_SEQ       1     80       MMEDNKQLALRIDGAVQSASQEVTNLRAELTATNRRLAELS
FT                                GGGGGPGSGPGAATSASAAAVTVADSAVATMENHQHGAQ
FT                                -> MRAADSGSWERVRQLAAYGQPTPSCGRDTGSARVPEPG
FT                                ACKLCADTTGLREQQGAGAVPDAADGFGIQP (in
FT                                isoform 2).
FT                                /FTId=VSP_031905.
FT   VAR_SEQ     412    425       DSDSQCSPTRHSLS -> GTAPDYYIEEDADW (in
FT                                isoform 2 and isoform 3).
FT                                /FTId=VSP_031906.
FT   VAR_SEQ     426    779       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_031907.
FT   CONFLICT     84     84       R -> Q (in Ref. 1; BAC35155).
SQ   SEQUENCE   779 AA;  86717 MW;  7A8FBD9D840E4126 CRC64;
     MMEDNKQLAL RIDGAVQSAS QEVTNLRAEL TATNRRLAEL SGGGGGPGSG PGAATSASAA
     AVTVADSAVA TMENHQHGAQ VLLREEVVQL QEEVHLLRQM KEMLAKDLEE SQGGKCSEVL
     SATELRVQLV QKEQELARAK EALQAMKADR KRLKGEKTDL VSQMQQLYAT LESREEQLRD
     FIRNYEQHRK ESEDAVKALA KEKDLLEREK WELRRQAKEA TDHAAALRSQ LDLKDNRMKE
     LEAELAMAKQ SLATLTKDVP KRHSLAMPGE TVLNGNQEWV VQADLPLTAA IRQSQQTLYH
     SHPPHPADRQ VRVSPCHSRQ PSVISDASAA EGDRSSTPSD INSPRHRTHS LCNGDSPGPV
     QKSLHNPIVQ SLEDLEDQKR KKKKEKMGFG SISRVFARGK QRKSLDPGLF DDSDSQCSPT
     RHSLSLSEGE EQMDRLQHVE LVRTTPMSHW KAGTVQAWLE VVMAMPMYVK ACAENVKSGK
     VLLSLSDEDL ELGLGVCSSL HRRKLRLAIE DYRDAEAGRS LSKAADLDHH WVAKAWLNDI
     GLSQYSQAFQ NHLVDGRMLN SLMKRDLEKH LNVSKKFHQV SILLGIELLY QVNFSREALQ
     ERRARCETQN TDPVVWTNQR VLKWVRDIDL KEYADNLTNS GVHGAVLVLE PTFNAEAMAT
     ALGIPSGKHI LRRHLAEEMS TIFHPSNSTG IRESERFGTP PGRASSITRA GREDSGGNSK
     HRAGRLPLGK IGRGFSSKEP DFHDDYGSLE NEDCGDEDLQ GRPEQCRLEG YGSLEVTNV
//
ID   Q69ZT3_MOUSE            Unreviewed;      1033 AA.
AC   Q69ZT3;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   08-MAR-2011, entry version 38.
DE   SubName: Full=MKIAA1012 protein;
DE   Flags: Fragment;
GN   Name=Trappc8; Synonyms=mKIAA1012;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Adult thymus;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK173085; BAD32363.1; -; mRNA.
DR   IPI; IPI00761429; -.
DR   RefSeq; NP_796012.2; NM_177038.3.
DR   UniGene; Mm.273769; -.
DR   ProteinModelPortal; Q69ZT3; -.
DR   PRIDE; Q69ZT3; -.
DR   Ensembl; ENSMUST00000025177; ENSMUSP00000025177; ENSMUSG00000033382.
DR   GeneID; 75964; -.
DR   KEGG; mmu:75964; -.
DR   UCSC; uc008eev.1; mouse.
DR   CTD; 75964; -.
DR   MGI; MGI:2443008; Trappc8.
DR   eggNOG; roNOG04908; -.
DR   HOGENOM; HBG402975; -.
DR   HOVERGEN; HBG036226; -.
DR   InParanoid; Q69ZT3; -.
DR   OMA; LGVVYNL; -.
DR   OrthoDB; EOG4RXXZB; -.
DR   ArrayExpress; Q69ZT3; -.
DR   Bgee; Q69ZT3; -.
DR   Genevestigator; Q69ZT3; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR011990; TPR-like_helical.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   1033 AA;  115518 MW;  D0140587ED34F595 CRC64;
     ELKNTSGLLY PPEAPELQIR KMADLCFLVQ HYDLAYSCYH TAKKDFLNDQ AMLYAAGALE
     MAAVSAFLQP GAPRPYPAHY MDTAIQTYRD ICKNMVLAER CVLLSAEILK SQSKYSEAAA
     LLIRLTSEDS DLRSALLLEQ AAHCFINMKS PMVRKYAFHM ILAGHRFSKA GQKKHALRCY
     CQAMQVYKGK GWSLAEDHIN FTIGRQSYTL RQLDNAVSAF RHILINESKQ SAAQQGAFLR
     EYLYVYKNVN QLSPDGPLPQ LPLPYINSSA TRVFFGHDRR PADGEKQAAT HISLDQEYDS
     ESSQQWRELE EHVVAVANKG VIPSSFYPTQ YCLNSYSDNS RFPLAVVEEP ITVEVAFRNP
     LKVPLLLSDL SLLWKFQPKD ASGKDIEKVK ERVTGEPEMI GTEVISEFLI NSEESKVARL
     KLFPHHIGEL HILGVVYNLG TIQGSGTVDG IGALPGCHTG KHSLSMSVRG RQDLEIQGPR
     LNNTKEEKTS VKYGPDRRLD PIVTEEMPLL EVFFIHFPTG LLCGEIRKAY VEFVNVSKCP
     LTGLKVVSKR PEFFTFGGNT AALTPLSPST SENCSAYKTV VTASPSLGTA LVSTASSMDF
     GTGTGQQLEA IPVPLPDSVL LPGASIQLPM WLRGPDEEGV HEINFLFYYE SVKKQPKKRH
     RILRHTAVIC TSRSLNVRAT VCRSNSLEDE EGRGGNMLVF VDVENTNTSE AGVKEFHMVQ
     VSSSSKHWQL HKSVNISENK DAKLASREKG KFCFKAVRCK QKEGGIQSSE KYTFADIIFG
     NEQIISSASP CADFFYRSLS SELKKTQDQL SAYPEKHREA TEGAVRLVEK CSEVDLSIVI
     LWKAYVVEDN KQLILEGQHH VVVRTVGKEA FSHSQKEEPP EMELLKFFRP ENTTVSTRPS
     VEQLSNLIKT SLHYPESFHH PFHQKSLCLV PVTLLLSNCS KADVDVIVDL RHKTTSPEAL
     ETHGSFTWLG QTQYKLQLKS QEMHSLQLKA CFVHTGVYNL GTPRVFAKLS DHVTVFETSQ
     QNSMPALIII NNA
//
ID   EHBP1_MOUSE             Reviewed;        1231 AA.
AC   Q69ZW3; Q5SQK3; Q91ZJ6;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   08-FEB-2011, entry version 50.
DE   RecName: Full=EH domain-binding protein 1;
GN   Name=Ehbp1; Synonyms=Kiaa0903;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J;
RX   MEDLINE=22325413; PubMed=12174196; DOI=10.1186/1471-2156-3-14;
RA   Fuchs S., Resch K., Thiel C., Ulbrich M., Platzer M., Jockusch H.,
RA   Schmitt-John T.;
RT   "Comparative transcription map of the wobbler critical region on mouse
RT   chromosome 11 and the homologous region on human chromosome 2p13-14.";
RL   BMC Genet. 3:14-14(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171; SER-174; SER-177;
RP   SER-442; SER-446 AND SER-1022, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May play a role in actin reorganization. Links clathrin-
CC       mediated endocytosis to the actin cytoskeleton (By similarity).
CC   -!- SUBUNIT: Interacts with EHD2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane. Note=Mostly found in
CC       cytosol and plasma membrane (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q69ZW3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q69ZW3-2; Sequence=VSP_024836;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32333.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF424697; AAL24806.1; -; mRNA.
DR   EMBL; AK173055; BAD32333.1; ALT_INIT; mRNA.
DR   EMBL; AL731860; CAI25363.1; -; Genomic_DNA.
DR   EMBL; AL669858; CAI25363.1; JOINED; Genomic_DNA.
DR   EMBL; AL669858; CAI25873.1; -; Genomic_DNA.
DR   EMBL; AL731860; CAI25873.1; JOINED; Genomic_DNA.
DR   IPI; IPI00515576; -.
DR   IPI; IPI00845795; -.
DR   RefSeq; NP_694718.2; NM_153078.2.
DR   UniGene; Mm.281732; -.
DR   HSSP; Q01082; 1BKR.
DR   ProteinModelPortal; Q69ZW3; -.
DR   SMR; Q69ZW3; 453-558.
DR   STRING; Q69ZW3; -.
DR   PhosphoSite; Q69ZW3; -.
DR   PRIDE; Q69ZW3; -.
DR   Ensembl; ENSMUST00000109563; ENSMUSP00000105191; ENSMUSG00000042302.
DR   GeneID; 216565; -.
DR   KEGG; mmu:216565; -.
DR   UCSC; uc007ieb.1; mouse.
DR   CTD; 216565; -.
DR   MGI; MGI:2667252; Ehbp1.
DR   eggNOG; roNOG09575; -.
DR   GeneTree; ENSGT00600000084275; -.
DR   HOGENOM; HBG356648; -.
DR   HOVERGEN; HBG057909; -.
DR   InParanoid; Q69ZW3; -.
DR   ArrayExpress; Q69ZW3; -.
DR   Bgee; Q69ZW3; -.
DR   CleanEx; MM_EHBP1; -.
DR   Genevestigator; Q69ZW3; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR022735; DUF3585.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF12130; DUF3585; 1.
DR   SMART; SM00033; CH; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS50021; CH; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Membrane;
KW   Phosphoprotein.
FT   CHAIN         1   1231       EH domain-binding protein 1.
FT                                /FTId=PRO_0000285203.
FT   DOMAIN      453    555       CH.
FT   COILED      185    219       Potential.
FT   COILED      812    882       Potential.
FT   COILED     1032   1100       Potential.
FT   COILED     1136   1230       Potential.
FT   COMPBIAS    400    447       Pro-rich.
FT   COMPBIAS   1110   1113       Poly-Glu.
FT   MOD_RES     171    171       Phosphoserine.
FT   MOD_RES     174    174       Phosphoserine.
FT   MOD_RES     177    177       Phosphoserine.
FT   MOD_RES     436    436       Phosphoserine (By similarity).
FT   MOD_RES     437    437       Phosphothreonine (By similarity).
FT   MOD_RES     438    438       Phosphoserine (By similarity).
FT   MOD_RES     442    442       Phosphoserine.
FT   MOD_RES     446    446       Phosphoserine.
FT   MOD_RES     719    719       Phosphoserine (By similarity).
FT   MOD_RES    1022   1022       Phosphoserine.
FT   MOD_RES    1061   1061       Phosphoserine (By similarity).
FT   VAR_SEQ     288    312       Missing (in isoform 2).
FT                                /FTId=VSP_024836.
FT   CONFLICT     46     47       RR -> KE (in Ref. 1; AAL24806).
FT   CONFLICT     51     51       K -> R (in Ref. 1; AAL24806).
FT   CONFLICT    797    797       N -> S (in Ref. 1; AAL24806 and 3;
FT                                CAI25363/CAI25873).
FT   CONFLICT    993    993       T -> A (in Ref. 1; AAL24806).
FT   CONFLICT    999    999       A -> G (in Ref. 1; AAL24806).
FT   CONFLICT   1089   1089       D -> G (in Ref. 1; AAL24806).
FT   CONFLICT   1155   1155       E -> A (in Ref. 1; AAL24806).
SQ   SEQUENCE   1231 AA;  139131 MW;  EC16F2888F0C8678 CRC64;
     MASVWKRLQR VGKHASKFQF VASYQELMVE CTKKWQPDKL VVVWTRRSRR KSSKAHSWQP
     GIKNPYRGVV VWPVPENIEI TVTLFKDPHA EEFEDKEWTF VIENESPSGR RKALATSSIN
     MKQYASPMPT QTDVKLKFKP LSKKVVSATL QFSLSCIFLR EGKATDEDMQ SLASLMSMKQ
     ADIGNLDDFE EDNEDDDENR VNQEEKAAKI TEIVNQLNAL SSLDEDQDDC IKQANVPSAK
     SASSSEELIN TLNFLDEAQK DLATVNTNPF DEPDVTELNP FGDPDSEEPI TETTSPKKPE
     ESFYNNSCNP FKGVQTPQYL NPFDEPETFV MIKDSPPQST RRKNLRPVDM SKYLYADSSK
     SEEELDESNP FYEPKPTSPN NLVNTVQEGE TERRVKRRAP APPAPLAPPA PPAPPALTPK
     TGVNENTVVS AGKDLSTSPK PSPIPSPVLG QKPNASQSLL AWCREVTKNY RGVKITNFTT
     SWRNGLSFCA ILHHFRPDLI DYKSLNPQDI KENNKKAYDG FASIGISRLL EPSDMVLLAI
     PDKLTVMTYL YQIRAHFSGQ ELNVVQIEEN SSKSTYKVGN YETDTNSSVD QEKFYAELSD
     LKREPEPHQP ARGAVDLLSQ DDSVFVTDSG VGESESEHQT PDDHLSPSTA SPYYRRTKSD
     TEPQKSQQSS ARTSGSDDPG LSSSTDSAQA LASLGKKRLK AENLELSDLC VSDKKKDVSP
     LSAYEQKLQT VHASSDMEQG KMEKSRSLEC RLDGELAITK PNVSSPSKLG YNRDTDFTKK
     PCASLRQIES DPDADKNTLN HADHPNKAVQ HRMLSRQEEL KERARVLLEQ ARRDAAFKVG
     SKHGGSAAPA LCSRQLNDQQ DEERRRQLRE RARQLIAEAR CGVKMSELPS YGEMAAEKLK
     ERSKASGDEN DNIEIDTNEE IPEGFVVGGG DELTNIESDL DNPEQNSKVV DLRLKKLLEA
     QPQVANLLPS AAQKAVTEAS EQGEKSGVED LRTERLQKAT ERFRNPVVFN KDSTVRKTQL
     QSFSQYVENR PEMKRQRSIQ EDTKRGTEEK AEITETQRKP SEDEKGFKDT SQYVVGELAA
     LENEQKQIDT RAALVEKRLR YLMDTGRNTE EEEAMMQEWF MLVNKKNALI RRMNQLSLLE
     KEHDLERRYE LLNRELRAML AIEDWQKTEA QKRREQLLLD ELVALVDKRD ALVRDLDAQE
     KQAEEEDEHL ERTLEQNKGK MAKKEEKCAL Q
//
ID   Q69ZX3_MOUSE            Unreviewed;      1984 AA.
AC   Q69ZX3;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   05-OCT-2010, entry version 48.
DE   SubName: Full=MKIAA0866 protein;
DE   Flags: Fragment;
GN   Name=Myh11; Synonyms=mKIAA0866;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Adult thymus;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
CC   -!- SIMILARITY: Contains 1 IQ domain.
CC   -!- SIMILARITY: Contains 1 myosin head-like domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK173045; BAD32323.1; -; mRNA.
DR   IPI; IPI00227865; -.
DR   UniGene; Mm.250705; -.
DR   ProteinModelPortal; Q69ZX3; -.
DR   STRING; Q69ZX3; -.
DR   PRIDE; Q69ZX3; -.
DR   Ensembl; ENSMUST00000090287; ENSMUSP00000087756; ENSMUSG00000018830.
DR   UCSC; uc007yhd.1; mouse.
DR   MGI; MGI:102643; Myh11.
DR   HOGENOM; HBG717149; -.
DR   HOVERGEN; HBG004704; -.
DR   InParanoid; Q69ZX3; -.
DR   ArrayExpress; Q69ZX3; -.
DR   Bgee; Q69ZX3; -.
DR   Genevestigator; Q69ZX3; -.
DR   GO; GO:0005859; C:muscle myosin complex; IDA:MGI.
DR   GO; GO:0030485; C:smooth muscle contractile fiber; IDA:MGI.
DR   GO; GO:0001725; C:stress fiber; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:motor activity; IMP:MGI.
DR   GO; GO:0006939; P:smooth muscle contraction; IDA:MGI.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR002928; Myosin_tail.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   Pfam; PF01576; Myosin_tail_1; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 1.
DR   SMART; SM00242; MYSc; 1.
DR   PROSITE; PS50096; IQ; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; ATP-binding; Coiled coil; Motor protein; Myosin;
KW   Nucleotide-binding.
FT   NON_TER       1      1
SQ   SEQUENCE   1984 AA;  228269 MW;  ED3399B5B4CBE6D7 CRC64;
     STPGVDLGPP DIMAQKGQLS DDEKFLFVDK NFMNSPMAQA DWVAKKLVWV PSEKQGFEAA
     SIKEEKGDEV VVELVENGKK VTVGKDDIQK MNPPKFSKVE DMAELTCLNE ASVLHNLRER
     YFSGLIYTYS GLFCVVVNPY KYLPIYSEKI VDMYKGKKRH EMPPHIYAIA DTAYRSMLQD
     REDQSILCTG ESGAGKTENT KKVIQYLAVV ASSHKGKKDS SITGELEKQL LQANPILEAF
     GNAKTVKNDN SSRFGKFIRI NFDVTGYIVG ANIETYLLEK SRAIRQARDE RTFHIFYYLL
     AGAKEKMKSD LLLESFNSYT FLSNGFVPIP AAQDDEMFQE TLEAMSIMGF NEEEQLAILK
     VVSSVLQLGN IVFKKERNTD QASMPDNTAA QKVCHLVGIN VTDFTRAILT PRIKVGRDVV
     QKAQTKEQAD FAIEALAKAT YERLFRWILS RVNKALDKTH RQGASFLGIL DIAGFEIFEV
     NSFEQLCINY TNEKLQQLFN HTMFILEQEE YQREGIEWNF IDFGLDLQPC IELIERPNNP
     PGVLALLDEE CWFPKATDKS FVEKLCSEQG NHPKFQKPKQ LKDKTEFSII HYAGKVDYNA
     SAWLTKNMDP LNDNVTSLLN ASSDKFVADL WKDVDRIVGL DQMAKMTESS LPSASKTKKG
     MFRTVGQLYK EQLGKLMTTL RNTTPNFVRC IIPNHEKRSG KLDAFLVLEQ LRCNGVLEGI
     RICRQGFPNR IVFQEFRQRY EILAANAIPK GFMDGKQACI LMIKALELDP NLYRIGQSKI
     FFRTGVLAHL EEERDLKITD VIMAFQAMCR GYLARKAFTK RQQQLTAMKV IQRNCAAYLK
     LRNWQWWRLF TKVKPLLQVT RQEEEMQAKE EEMQKIKERQ QKAETELKEL EQKHTQLAEE
     KTLLQEQLQA ETELYAEAEE MRVRLAAKKQ ELEEILHEME ARLEEEEDRG QQLQAERKKM
     AQQMLDLEEQ LEEEEAARQK LQLEKVTAEA KIKKLEDDIL VMDDQNSKLS KERKLLEERV
     SDLTTNLAEE EEKAKNLTKL KSKHESMISE LEVRLKKEEK SRQELEKLKR KLEGDASDFH
     EQIADLQAQI AELKMQLAKK EEELQAALAR LDEEIAQKNN ALKKIRELEG HISDLQEDLD
     SERAARNKAE KQKRDLGEEL EALKTELEDT LDSTATQQEL RAKREQEVTV LKKALDEETR
     SHEAQVQEMR QKHTQAVEEL TEQLEQFKRA KANLDKSKQT LEKENADLAG ELRVLGQAKQ
     EVEHKKKKLE VQLQDLQSKC SDGERARAEL SDKVHKLQNE VESVTGMLNE AEGKAIKLAK
     DVASLGSQLQ DTQELLQEET RQKLNVSTKL RQLEDERNSL QDQLDEEMEA KQNLERHVST
     LNIQLSDSKK KLQDFASTIE VMEEGKKRLQ KEMEGLSQQY EEKAAAYDKL EKTKNRLQQE
     LDDLVVDLDN QRQLVSNLEK KQKKFDQLLA EEKNISSKYA DERDRAEAEA REKETKALSL
     ARALEEALEA KEELERTNKM LKAEMEDLVS SKDDVGKNVH ELEKSKRALE TQMEEMKTQL
     EELEDELQAT EDAKLRLEVN MQALKGQFER DLQARDEQNE EKRRQLQRQL HEYETELEDE
     RKQRALAAAA KKKLEGDLKD LELQADSAIK GREEAIKQLR KLQAQMKDFQ RELDDARASR
     DEIFATSKEN EKKAKSLEAD LMQLQEDLAA AERARKQADL EKEELAEELA SSLSGRNTLQ
     DEKRRLEARI AQLEEELEEE QGNMEAMSDR VRKATLQAEQ LSNELATERS TAQKNESARQ
     QLERQNKELR SKLQEVEGAV KAKLKSTVAA LEAKIAQLEE QVEQEAREKQ AATKSLKQKD
     KKLKEVLLQV EDERKMAEQY KEQAEKGNTK VKQLKRQLEE AEEESQRINA NRRKLQRELD
     EATESNEAMG REVNALKSKL RRGNEASFVP SRRAGGRRVI ENTDGSEEEM DARDSDFNGT
     KASE
//
ID   MOR2A_MOUSE             Reviewed;        1030 AA.
AC   Q69ZX6; Q5QNQ7; Q6P547;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=MORC family CW-type zinc finger protein 2A;
DE   AltName: Full=Zinc finger CW-type coiled-coil domain protein 1;
GN   Name=Morc2a; Synonyms=Kiaa0852, Zcwcc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic intestine;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-1030.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-741, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-854, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- SIMILARITY: Contains 1 CW-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32320.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK173042; BAD32320.1; ALT_INIT; mRNA.
DR   EMBL; AL691413; CAI25064.1; -; Genomic_DNA.
DR   EMBL; BC063082; AAH63082.1; -; mRNA.
DR   IPI; IPI00623382; -.
DR   RefSeq; NP_001152760.1; NM_001159288.1.
DR   UniGene; Mm.139127; -.
DR   ProteinModelPortal; Q69ZX6; -.
DR   SMR; Q69ZX6; 27-124, 492-542.
DR   PRIDE; Q69ZX6; -.
DR   Ensembl; ENSMUST00000093389; ENSMUSP00000091087; ENSMUSG00000034543.
DR   Ensembl; ENSMUST00000096441; ENSMUSP00000094176; ENSMUSG00000034543.
DR   GeneID; 74522; -.
DR   KEGG; mmu:74522; -.
DR   UCSC; uc007htm.1; mouse.
DR   CTD; 74522; -.
DR   MGI; MGI:1921772; Morc2a.
DR   eggNOG; roNOG14804; -.
DR   HOGENOM; HBG713455; -.
DR   HOVERGEN; HBG056877; -.
DR   InParanoid; Q69ZX6; -.
DR   OMA; LRNCLRY; -.
DR   OrthoDB; EOG473PQP; -.
DR   ArrayExpress; Q69ZX6; -.
DR   Bgee; Q69ZX6; -.
DR   CleanEx; MM_MORC2A; -.
DR   Genevestigator; Q69ZX6; -.
DR   GermOnline; ENSMUSG00000034543; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR003594; ATPase-like_ATP-bd.
DR   InterPro; IPR011124; Znf_CW.
DR   Gene3D; G3DSA:3.30.565.10; ATP_bd_ATPase; 2.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF07496; zf-CW; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATP_bd_ATPase; 1.
DR   PROSITE; PS51050; ZF_CW; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Metal-binding; Phosphoprotein; Zinc; Zinc-finger.
FT   CHAIN         1   1030       MORC family CW-type zinc finger protein
FT                                2A.
FT                                /FTId=PRO_0000248243.
FT   ZN_FING     490    544       CW-type.
FT   COILED      285    362       Potential.
FT   COILED      555    583       Potential.
FT   COILED      738    775       Potential.
FT   COILED      966   1011       Potential.
FT   COMPBIAS    601    724       Pro-rich.
FT   MOD_RES     741    741       Phosphoserine.
FT   MOD_RES     854    854       Phosphoserine.
SQ   SEQUENCE   1030 AA;  117330 MW;  0EDD2D09F11C80A2 CRC64;
     MAFTNYSSLN RAQLTFEYLH TNSTTHEFLF GALAELVDNA RDADATRIDI YAERREDLRG
     GFMLCFLDDG AGMDPSDAAS VIQFGKSAKR TPESTQIGQY GNGLKSGSMR IGKDFILFTK
     KEDTMTCLFL SRTFHEEEGI DEVIVPLPTW NARTREPITD NVEKFAIETE LVYKYSPFHT
     EEQVMNQFMK IPGNSGTLVI IFNLKLMDNG EPELDIISNP KDIQMAETSP EGTKPERRSF
     RAYAAVLYID PRMRIFIHGH KVQTKRLSCC LYKPRMYKYT SSRFKTRAEQ EVKKAEHVAR
     IAEEKAREAE SKARTLEVRM GGDLTRDSRV MLRQVQNTAI TLRREADVKK RIKDAKQRAL
     KEPKELNFVF GVNIEHRDLD GMFIYNCSRL IKMYEKVGPQ LEGGMACGGV VGVVDVPYLV
     LEPTHNKQDF ADAKEYRHLL RAMGEHLAQY WKDIAIAQRG IIKFWDEFGY LSANWNQPPS
     SELRFKRRRA MEIPTTIQCD LCLKWRTLPF QLSSVETDYP DTWVCSMNPD PEQDRCEASE
     QKQKVPLGTL KKDPKTQEEK QKQLTEKIRQ QQEKLEALQK TTPIRSQADL KKLPLEVTTR
     PIEEPVRRPQ RPRSPPLPAV IKNAPSRPPS IQTPRPSTQL RKTSVISLPK PPTTAARGET
     STSRLLQPTE APRKPANPPI KTVPRPTPPV HTPPLSLIPS SKSLREVPAQ KAIKTPVVKK
     PEPPVKQSVA TSGRKRSLAV SDEEEAEEEA EKRRERCKRG KLAVKEEKKE ANELSDSAGE
     DHPAELRKAQ KDKGLHVEVR VNREWYTGRV TAVEVGKNAV RWKVKFDYVP TDTTPRDRWV
     EKGSEDVRLM KPPSPEHQSP DTQQEGGEEE EAMVARQAVA LPEPSTSDGL PIEPDTTATS
     PSHETIDLLV QILRNCLRYF LPPSFPISKK ELSVMNSEEL ISFPLKEYFK QYEVGLQNLC
     HSYQSRADSR AKASEESLRT SEKKLRETEE KLQKLRTNIV ALLQKVQEDI DINTDDELDA
     YIEDLITKGD
//
ID   ABLM3_MOUSE             Reviewed;         682 AA.
AC   Q69ZX8; Q52KR1; Q6PAI7;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 2.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Actin-binding LIM protein 3;
DE            Short=abLIM-3;
DE   AltName: Full=Actin-binding LIM protein family member 3;
GN   Name=Ablim3; Synonyms=Kiaa0843;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=17194709; DOI=10.1074/jbc.M607549200;
RA   Barrientos T., Frank D., Kuwahara K., Bezprozvannaya S., Pipes G.C.T.,
RA   Bassel-Duby R., Richardson J.A., Katus H.A., Olson E.N., Frey N.;
RT   "Two novel members of the ABLIM protein family, ABLIM-2 and -3,
RT   associate with STARS and directly bind F-actin.";
RL   J. Biol. Chem. 282:8393-8403(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277; SER-280; SER-373
RP   AND SER-502, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May act as scaffold protein. May stimulate ABRA activity
CC       and ABRA-dependent SRF transcriptional activity.
CC   -!- SUBUNIT: Directly interacts with F-actin and ABRA (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in heart, brain, lung and liver. In
CC       the brain, highly expressed in the olfactory bulb. In the
CC       hippocampus, expressed selectively in the CA2 and CA3 fields. In
CC       the cerebellum, expressed in internal granular cells.
CC   -!- DEVELOPMENTAL STAGE: At 15.5 dpc, expressed in skeletal muscle.
CC       Down-regulated in adult skeletal muscle.
CC   -!- SIMILARITY: Contains 1 HP (headpiece) domain.
CC   -!- SIMILARITY: Contains 4 LIM zinc-binding domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32318.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK173040; BAD32318.1; ALT_INIT; mRNA.
DR   EMBL; BC060275; AAH60275.1; -; mRNA.
DR   EMBL; BC094229; AAH94229.1; -; mRNA.
DR   IPI; IPI00464316; -.
DR   RefSeq; NP_001157963.1; NM_001164491.1.
DR   RefSeq; NP_941051.2; NM_198649.3.
DR   UniGene; Mm.329478; -.
DR   ProteinModelPortal; Q69ZX8; -.
DR   SMR; Q69ZX8; 21-268, 606-682.
DR   STRING; Q69ZX8; -.
DR   PhosphoSite; Q69ZX8; -.
DR   PRIDE; Q69ZX8; -.
DR   Ensembl; ENSMUST00000049378; ENSMUSP00000041243; ENSMUSG00000032735.
DR   GeneID; 319713; -.
DR   KEGG; mmu:319713; -.
DR   UCSC; uc008fcs.1; mouse.
DR   CTD; 319713; -.
DR   MGI; MGI:2442582; Ablim3.
DR   eggNOG; roNOG11941; -.
DR   GeneTree; ENSGT00570000079028; -.
DR   HOGENOM; HBG443863; -.
DR   HOVERGEN; HBG031499; -.
DR   InParanoid; Q69ZX8; -.
DR   OMA; KIRGPSH; -.
DR   OrthoDB; EOG4PNXGH; -.
DR   PhylomeDB; Q69ZX8; -.
DR   NextBio; 395258; -.
DR   ArrayExpress; Q69ZX8; -.
DR   Bgee; Q69ZX8; -.
DR   CleanEx; MM_ABLIM3; -.
DR   Genevestigator; Q69ZX8; -.
DR   GermOnline; ENSMUSG00000032735; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:MGI.
DR   InterPro; IPR003128; Villin_headpiece.
DR   InterPro; IPR001781; Znf_LIM.
DR   Gene3D; G3DSA:1.10.950.10; VHP; 1.
DR   Gene3D; G3DSA:2.10.110.10; Znf_LIM; 4.
DR   Pfam; PF00412; LIM; 4.
DR   Pfam; PF02209; VHP; 1.
DR   SMART; SM00132; LIM; 4.
DR   SMART; SM00153; VHP; 1.
DR   SUPFAM; SSF47050; VHP; 1.
DR   PROSITE; PS51089; HP; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 4.
PE   1: Evidence at protein level;
KW   Cytoplasm; LIM domain; Metal-binding; Phosphoprotein; Repeat; Zinc.
FT   CHAIN         1    682       Actin-binding LIM protein 3.
FT                                /FTId=PRO_0000075703.
FT   DOMAIN       21     80       LIM zinc-binding 1.
FT   DOMAIN       80    140       LIM zinc-binding 2.
FT   DOMAIN      149    208       LIM zinc-binding 3.
FT   DOMAIN      208    268       LIM zinc-binding 4.
FT   DOMAIN      614    682       HP.
FT   MOD_RES     277    277       Phosphoserine.
FT   MOD_RES     280    280       Phosphoserine.
FT   MOD_RES     282    282       Phosphoserine.
FT   MOD_RES     372    372       Phosphoserine (By similarity).
FT   MOD_RES     373    373       Phosphoserine.
FT   MOD_RES     388    388       Phosphoserine (By similarity).
FT   MOD_RES     394    394       Phosphoserine (By similarity).
FT   MOD_RES     502    502       Phosphoserine.
FT   MOD_RES     503    503       Phosphoserine (By similarity).
FT   CONFLICT    381    381       T -> I (in Ref. 2; AAH60275).
SQ   SEQUENCE   682 AA;  77630 MW;  44E7E59BD850F9CE CRC64;
     MNTSIPYQQS PYSPRGGSNV IQCYRCGDTC KGEVVRVHNN HFHIRCFTCQ VCGCGLAQSG
     FFFKNQEYIC TQDYQQLYGT RCDSCRDFIT GEVISALGRT YHPKCFVCSL CRKPFPIGDK
     VTFSGKECVC QTCSQSMTSS KPIKIRGPSH CAGCKEEIKH GQSLLALDKQ WHVSCFKCQT
     CSVILTGEYI SKDGVPYCES DYHSQFGIKC ETCDRYISGR VLEAGGKHYH PTCARCVRCH
     QMFTEGEEMY LTGSEVWHPI CKQAARAEKK LKHRRTSETS ISPPGSSIGS PNRVICAKVD
     NEILNYKDLA ALPKVKSIYE VQRPDLISYE PHSRYTSDEM LERCGYGESL GTLSPYSQDI
     YENLDLRQRR ASSPGYIDSP TYSRQGMSPT FSRSPHYYRS GPESGRSSPY HSQLDVRSST
     PTSYQAPKHF HIPAGESNIY RKPPIYKRHG DLSTATKSKT SEDISQASKY SPAYSPDPYY
     ASESEYWTYH GSPKVPRARR FSSGGEEEDF DRSMHKLQSG IGRLILKEEM KARSSSYADP
     WTPPRSSTSS REALHTTGYE MSFNGSPRSH YLADSDPLIS KSASLPAYRR NGLHRTPSAD
     LFHYDSMNAV NWGMREYKIY PYELLLVTTR GRNRLPKDVD RTRLERHLSQ EEFYQVFGMT
     ISEFERLALW KRNELKKQAR LF
//
ID   TMCC1_MOUSE             Reviewed;         649 AA.
AC   Q69ZZ6; Q8CEF4;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   08-MAR-2011, entry version 47.
DE   RecName: Full=Transmembrane and coiled-coil domains protein 1;
GN   Name=Tmcc1; Synonyms=Kiaa0779;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q69ZZ6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q69ZZ6-2; Sequence=VSP_019590, VSP_019591;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q69ZZ6-3; Sequence=VSP_019589;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the TEX28 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32300.1; Type=Erroneous initiation;
CC       Sequence=BAE32665.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK173022; BAD32300.1; ALT_INIT; mRNA.
DR   EMBL; AK028322; BAC25880.1; -; mRNA.
DR   EMBL; AK154540; BAE32665.1; ALT_INIT; mRNA.
DR   IPI; IPI00464322; -.
DR   IPI; IPI00671412; -.
DR   IPI; IPI00761258; -.
DR   RefSeq; NP_803131.1; NM_177412.1.
DR   UniGene; Mm.425352; -.
DR   UniGene; Mm.477923; -.
DR   ProteinModelPortal; Q69ZZ6; -.
DR   PRIDE; Q69ZZ6; -.
DR   Ensembl; ENSMUST00000032222; ENSMUSP00000032222; ENSMUSG00000030126.
DR   Ensembl; ENSMUST00000088896; ENSMUSP00000086285; ENSMUSG00000030126.
DR   GeneID; 330401; -.
DR   KEGG; mmu:330401; -.
DR   UCSC; uc009djo.1; mouse.
DR   UCSC; uc009djp.1; mouse.
DR   UCSC; uc009djq.1; mouse.
DR   CTD; 330401; -.
DR   MGI; MGI:2442368; Tmcc1.
DR   HOGENOM; HBG443696; -.
DR   HOVERGEN; HBG057342; -.
DR   InParanoid; Q69ZZ6; -.
DR   OMA; SGQEMAA; -.
DR   OrthoDB; EOG4SBDZ1; -.
DR   ArrayExpress; Q69ZZ6; -.
DR   Bgee; Q69ZZ6; -.
DR   CleanEx; MM_TMCC1; -.
DR   Genevestigator; Q69ZZ6; -.
DR   GermOnline; ENSMUSG00000030126; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR019394; Predicted_TM_coiled-coil_2.
DR   Pfam; PF10267; Tmemb_cc2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    649       Transmembrane and coiled-coil domains
FT                                protein 1.
FT                                /FTId=PRO_0000184596.
FT   TRANSMEM    588    608       Helical; (Potential).
FT   TRANSMEM    621    641       Helical; (Potential).
FT   COILED      224    310       Potential.
FT   COILED      457    566       Potential.
FT   MOD_RES     378    378       Phosphoserine (By similarity).
FT   MOD_RES     410    410       Phosphoserine.
FT   VAR_SEQ       1    320       Missing (in isoform 3).
FT                                /FTId=VSP_019589.
FT   VAR_SEQ       1    175       Missing (in isoform 2).
FT                                /FTId=VSP_019590.
FT   VAR_SEQ     176    188       GVCVPGEEATAER -> MVQRFSLRRQLSK (in
FT                                isoform 2).
FT                                /FTId=VSP_019591.
SQ   SEQUENCE   649 AA;  71642 MW;  6A7E07076CD3BF08 CRC64;
     MEPSGSEQLY EDPDPGGKSQ DAEARRQTES EQKLSKMTHN ALENINVIGQ GLKHLFQHQR
     RRSSVSPHDV QQIQTDPEPE VDLDSQNACA EIDGVSTHPT ALNRVLQQIR VPPKMKRGTS
     LHSRRGKSEA PKGSPQINRK SGQEVAAVIQ SGRPRSSSTT DAPTSSSVME IACAAGVCVP
     GEEATAERIE RLEVSSLAQT SSAVASSTDG SIHTESVDGI PDPQRTKAAI AHLQQKILKL
     TEQIKIAQTA RDDNVAEYLK LANSADKQQA ARIKQVFEKK NQKSAQTILQ LQKKLEHYHR
     KLREVEQNGI PRQPKDVFRD MHQGLKDVGA KVTGFSEGVV DSVKGGFSSF SQATHSAAGA
     VVSKPREIAS LIRNKFGSAD NIPNLKDSLE EGQVDDGGKA LGVISNFQSS PKYGSEEDCS
     SATSGSVGAN STTGGIAVGA SSSKTNTLDM QSSGFDALLH EVQEIRETQA RLEDSFETLK
     EHYQRDYSLI MQTLQEERYR CERLEEQLND LTELHQNEIL NLKQELASME EKIAYQSYER
     ARDIQEALEA CQTRISKMEL QQQQQQVVQL EGLENATARN LLGKLINILL AVMAVLLVFV
     STVANCVVPL MKTRNRTFST LFLVAFIAFL WKHWDALFSY VDRLFSPPR
//
ID   K0754_MOUSE             Reviewed;         979 AA.
AC   Q69ZZ9;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   05-OCT-2010, entry version 28.
DE   RecName: Full=Uncharacterized protein KIAA0754;
GN   Name=Kiaa0754;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-979.
RC   TISSUE=Embryonic tail;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
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DR   EMBL; AL606918; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK173019; BAD32297.1; -; mRNA.
DR   IPI; IPI00954629; -.
DR   UniGene; Mm.402299; -.
DR   PhosphoSite; Q69ZZ9; -.
DR   PRIDE; Q69ZZ9; -.
DR   MGI; MGI:3045367; D830031N03Rik.
DR   HOVERGEN; HBG108023; -.
DR   CleanEx; MM_D830031N03RIK; -.
DR   Genevestigator; Q69ZZ9; -.
PE   2: Evidence at transcript level;
KW   Phosphoprotein.
FT   CHAIN         1    979       Uncharacterized protein KIAA0754.
FT                                /FTId=PRO_0000295723.
FT   COMPBIAS    159    225       Glu-rich.
FT   COMPBIAS    803    858       Pro-rich.
FT   MOD_RES      25     25       Phosphoserine (By similarity).
FT   MOD_RES      28     28       Phosphoserine (By similarity).
FT   MOD_RES     605    605       Phosphoserine (By similarity).
SQ   SEQUENCE   979 AA;  104640 MW;  B007588379DFE03A CRC64;
     MPPNFPEFAE RMEASLSEVS EAGASNPSLQ EKKESSSALT ESSGHFDHRE PQSESVTLEH
     MSKSVDIPEV QNVKNLRDCQ DFKFQQHSES SPHEFQPLGS EAAAASGNTD EMQEHRFSSA
     TWPRAMKSSS KGGFSEKQYP LGDTACAVEL PPLSPCLSEE LLDPELHMLI TPSLREKTES
     ELKFEEDERW IMMEAEEEWE EEKLSEERKS LVTNEETSLA DPLEESDQAN SVPAVEDGSD
     RVAVSGTSDH LALHQMCCSV DLQPTRDQLA SVPRGSPPDC TCVPAGDTVI SEVKNRPDQG
     LEGLTSGLQC PVEAEQLSDT DSVQMFLELE KECLCEEGVT SSAELLSQAS SEGLAPTQDA
     EDSLLISHFP GAALEQEQHV GFLSVRIKDP DTGLDGEYCN ALDSSQVPKA VELCAQPDSG
     RDASTISKEC EKVPFSPKIG GEFKLLADLE PHSELDTGGL LNSNLRASCE ENLPVFIASE
     LAKENGNLSQ VDCSQTEGNV EEYMERIPLS FAFNYEQDVT SGPEVEVFSS DSNLLTDEIH
     LESGKGALIS QEDSNLASLG NVDLCELSME KVCDKDGETK EPGCQGKLLG NGAPAQFPTD
     FQRRSSESEV LSLHLLAGEL RLNKAGAETM SDREPQLSMA LSQEGELEMR DLDSTLNIFP
     EEQISKASNT VPGLEEWISS QQRPVPAAVV PMVENALDAV TPMPGEDIPA VALTASEGPA
     ANASASDGTA AATPIVPIPE EDIPGASVVI LVEDVMTAAI SAPEQAAASS GAVPPVETVT
     VPIIDEDVTS EEPDTQAAEM FLPEEPAIPT PAGPTAEEPD TPTVPVSTAE EPSMPPPAGP
     TPEESAAPTL KEPTPEKPDT QVVSSSIPEW SATPATAVPA KEIFSPDGPF LEGTTHTDSV
     PISEETPVLE NASSPGMGIK ECLDSSAFGI KEVPGTMIHG KVPLAATDGL NSHEVIVDHF
     IGRKGLEHKV RIASSLTWC
//
ID   PDS5A_MOUSE             Reviewed;        1332 AA.
AC   Q6A026;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Sister chromatid cohesion protein PDS5 homolog A;
GN   Name=Pds5a; Synonyms=Kiaa0648;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1112.
RC   TISSUE=Embryonic intestine;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
CC   -!- FUNCTION: Probable regulator of sister chromatid cohesion in
CC       mitosis which may stabilize cohesin complex association with
CC       chromatin. May couple sister chromatid cohesion during mitosis to
CC       DNA replication. Cohesion ensures that chromosome partitioning is
CC       accurate in both meiotic and mitotic cells and plays an important
CC       role in DNA repair (By similarity).
CC   -!- SUBUNIT: Interacts with the cohesin complex. Interacts with WAPAL
CC       (via FGF motifs) or CDCA5 (via the FGF motif); the interaction is
CC       direct, cohesin-dependent and competitive. Interacts with SMC3.
CC       Interacts with TP63 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Note=Associated
CC       with chromatin through most of the cell cycle. Dissociates from
CC       chromatin in late prophase, reassociates during late telophase (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the PDS5 family.
CC   -!- SIMILARITY: Contains 1 HEAT repeat.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32270.1; Type=Erroneous initiation;
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DR   EMBL; AC156034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK172992; BAD32270.1; ALT_INIT; Transcribed_RNA.
DR   IPI; IPI00669709; -.
DR   UniGene; Mm.278974; -.
DR   ProteinModelPortal; Q6A026; -.
DR   SMR; Q6A026; 283-350.
DR   STRING; Q6A026; -.
DR   PhosphoSite; Q6A026; -.
DR   PRIDE; Q6A026; -.
DR   Ensembl; ENSMUST00000031104; ENSMUSP00000031104; ENSMUSG00000029202.
DR   MGI; MGI:1918771; Pds5a.
DR   HOGENOM; HBG355580; -.
DR   HOVERGEN; HBG108241; -.
DR   InParanoid; Q6A026; -.
DR   OrthoDB; EOG46T30N; -.
DR   ArrayExpress; Q6A026; -.
DR   Bgee; Q6A026; -.
DR   Genevestigator; Q6A026; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0008156; P:negative regulation of DNA replication; ISS:UniProtKB.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 5.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell cycle; Cell division; Mitosis; Nucleus;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1   1332       Sister chromatid cohesion protein PDS5
FT                                homolog A.
FT                                /FTId=PRO_0000296342.
FT   REPEAT      392    428       HEAT.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     973    973       N6-acetyllysine (By similarity).
FT   MOD_RES    1145   1145       N6-acetyllysine (By similarity).
FT   MOD_RES    1194   1194       Phosphoserine (By similarity).
FT   MOD_RES    1207   1207       Phosphothreonine (By similarity).
FT   MOD_RES    1210   1210       N6-acetyllysine (By similarity).
FT   MOD_RES    1231   1231       Phosphoserine (By similarity).
FT   MOD_RES    1288   1288       N6-acetyllysine (By similarity).
FT   MOD_RES    1303   1303       Phosphoserine (By similarity).
FT   CONFLICT     45     45       Q -> L (in Ref. 1; BAD32270).
SQ   SEQUENCE   1332 AA;  150328 MW;  15AEC86AB82E71F0 CRC64;
     MDFTQPKPAT ALCGVVSADG KIAYPPGVKE ITDKITTDEM IKRLQMVVKT FMDMDQDSED
     EKQQYLPLAL HLASEFFLRN PNKDVRLLVA CCLADIFRIY APEAPYTSHD KLKDIFLFIT
     RQLKGLEDTK SPQFNRYFYL LENLAWVKSY NICFELEDCN EIFIQLFRTL FSVINNSHNT
     KVQMHMLDLM SSIIMEGDGV TQELLDSILI NLIPAHKNLN KQSFDLAKVL LKRTVQTIEA
     CIANFFNQVL VLGRSSVSDL SEHVFDLIQE LFAIDPQLLL SVMPQLEFKL KSNDGEERLA
     VVRLLAKLFG SKDSDLATQN RPLWQCFLGR FNDIHVPVRL ESVKFASHCL MNHPDLAKDL
     TEYLKVRSHD PEEAIRHDVI VTIITAAKRD LALVNDQLLG FVRERTLDKR WRVRKEAMMG
     LAQLYKKYCL HGEAGKEAAE KVSWIKDKLL HIYYQNSIDD KLLVEKIFAQ YLVPHNLETE
     ERMKCLYYLY ASLDPNAVKA LNEMWKCQNM LRSHVRELLD LHKQPTSEAN CSAMFGKLMT
     IAKNLPDPGK AQDFVKEFNQ VLGDDEKLRS QLELLISPTC SCKQADVCVR EIARKLANPK
     QPTNPFLEMV KFLLERIAPV HIDSEAISAL VKLMNKSIEG TADDEEEGVS PDSAIRSGLE
     LLKVLSFTHP TSFHSAETYE SLLQCLRMED DKVAEAAIQI FRNTGHKIET DLPQIRSTLI
     PILHQKAKRG TPHQAKQAVH CIHAIFSNKE VQLAQIFEPL SRSLNADVPE QLITPLVSLG
     HISMLAPDQF ASPMKSVVAN FIVKDLLMND RSTGEKNGKL WSPDEEVSPE VLAKVYLLRL
     LVRWLLGMKN NQSKSANSTL RLLSAMLVSE GDLTEQKRIS KSDMSRLRLA AGSAIMKLAQ
     EPCYHEIITP EQFQLCALVI NDECYQVRQI FAQKLHKALV KLLLPLEYMA IFALCAKDPV
     KERRAHARQC LLKNISIRRE YIKQNPMATE KLLSLLPEYV VPYMIHLLAH DPDFTRSQDV
     DQLRDIKECL WFMLEVLMTK NENNSHAFMK KMAENIKLTR DAQSPDESKT NEKLYTVCDV
     ALCVINSKSA LCNADSPKDP VLPMKFFTQP EKDFCNDKSY ISEETRVLLL TGKPKPTGVL
     GTVNKPLSAT GRKPYVRSAG TETGSNINAN SELSPSAGSR SREQSSEASE TGVSENEENP
     VRIISVTPVK NIDTVKNKEI NSDQSTQGNI SSDRGKKRIV TAAGAENIQK PDEKVDESGP
     PAPSKPRRGR RPKSESQGNA TKNDDLNKPV SKGRKRAAGS QESLEAGNAK APKLQDGAKK
     AVPAERQIDL QR
//
ID   Q6A029_MOUSE            Unreviewed;       810 AA.
AC   Q6A029;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   08-FEB-2011, entry version 37.
DE   SubName: Full=MKIAA0639 protein;
DE   Flags: Fragment;
GN   Name=Kif13b; Synonyms=mKIAA0639;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
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DR   EMBL; AK172989; BAD32267.1; -; mRNA.
DR   IPI; IPI00761751; -.
DR   UniGene; Mm.23611; -.
DR   ProteinModelPortal; Q6A029; -.
DR   STRING; Q6A029; -.
DR   PhosphoSite; Q6A029; -.
DR   Ensembl; ENSMUST00000100473; ENSMUSP00000098041; ENSMUSG00000060012.
DR   UCSC; uc007uin.1; mouse.
DR   MGI; MGI:1098265; Kif13b.
DR   GeneTree; ENSGT00570000078823; -.
DR   HOGENOM; HBG387786; -.
DR   InParanoid; Q6A029; -.
DR   ArrayExpress; Q6A029; -.
DR   Bgee; Q6A029; -.
DR   Genevestigator; Q6A029; -.
DR   InterPro; IPR023092; CAP-Gly_CS.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   InterPro; IPR022164; Kinesin-like.
DR   Gene3D; G3DSA:2.30.30.190; CAP-Gly_domain; 1.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   Pfam; PF12473; DUF3694; 1.
DR   SUPFAM; SSF74924; CAP-Gly_domain; 1.
DR   PROSITE; PS00845; CAP_GLY_1; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 1.
PE   1: Evidence at protein level;
FT   NON_TER       1      1
SQ   SEQUENCE   810 AA;  87633 MW;  C575E8D2942141DF CRC64;
     VQESGTLPLM EECILSVGIG CVKVRPLRSP KIHENVHEEE EDMDSYQDRD LERLRRKWLN
     ALTKRQEYLD QQLQKLVSKH DKTEDDADRE AQLLEMRLTL TEERNAVMVP SAGSGIPGAP
     AEWTPVPGME THIPVIFLDL NADDFSSQDN LDDPEAGWDA TLTGEEEEEF FELQIVKQHD
     GEVKAEASWD SAVHSCPQLS KGTPADERVF LILRVTVQLS HPADMQLVLR KRICVHVHGR
     QGFAQSLLKK MSHRSSIPGC GVTFEIVSNI PEDAQGVEER EALARMAANV ENPASADSEA
     YIEKYLRSVL AVENLLTLDR LRQEVAVKEQ LTGKGKLSRR SISSPSMNRL SGSRQELSPS
     HSLGSNKGRW ESQQDVSQTL VSRGIAPGPP ALSVSPQNNQ SSDPGLGGVA ASYLNPVKSL
     VPQMPKLLKS LFPVRDDRRG RHSSPLAHQP VPRILVQPTF SDTWATRTEE AQQGSPGPSG
     ALESMVKMAA PAVKICDKPV KVSSPPSPMV VTQPPEGQDG PPSPLSEASS GYFSHSVSSA
     TLSETLTLGL DTTGLGSQTP GSPPALCQVT PEPELAFLSC TLSHPPAPEE AHVPAAPTQS
     TELEVPRAPL LSEPASAVPT SPFRIRKVRT SELKSFTGML GGASSGAEED PLASEDPSNA
     RGQTLGRLEV TSDSEDASEV PEWLREGEYV VVGTNKTGIV RYIGPTDFQE GTWIGVELDL
     PAGKNDGSIG GKQYFRCNPG YGLLVRPSRV RRAVGTGRRR SSGLQPQGAP EVRRSATISG
     SATNLASLTA ALAKGDRSYK NPENRKSWAS
//
ID   N4BP1_MOUSE             Reviewed;         893 AA.
AC   Q6A037; Q3TCI4; Q3UH87; Q3UY69;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=NEDD4-binding protein 1;
DE            Short=N4BP1;
GN   Name=N4bp1; Synonyms=Kiaa0615;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreatic islet;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   SUBCELLULAR LOCATION, UBIQUITINATION, AND INTERACTION WITH NEDD4.
RX   MEDLINE=21659763; PubMed=11717310; DOI=10.1074/jbc.M110047200;
RA   Murillas R., Simms K.S., Hatakeyama S., Weissman A.M., Kuehn M.R.;
RT   "Identification of developmentally expressed proteins that
RT   functionally interact with Nedd4 ubiquitin ligase.";
RL   J. Biol. Chem. 277:2897-2907(2002).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH ITCH.
RX   PubMed=17592138; DOI=10.1073/pnas.0701773104;
RA   Oberst A., Malatesta M., Aqeilan R.I., Rossi M., Salomoni P.,
RA   Murillas R., Sharma P., Kuehn M.R., Oren M., Croce C.M.,
RA   Bernassola F., Melino G.;
RT   "The Nedd4-binding partner 1 (N4BP1) protein is an inhibitor of the E3
RT   ligase Itch.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:11280-11285(2007).
RN   [5]
RP   SUBCELLULAR LOCATION, UBIQUITINATION, SUMOYLATION, AND DESUMOYLATION
RP   BY SENP1.
RX   PubMed=20233849; DOI=10.1242/jcs.060160;
RA   Sharma P., Murillas R., Zhang H., Kuehn M.R.;
RT   "N4BP1 is a newly identified nucleolar protein that undergoes SUMO-
RT   regulated polyubiquitylation and proteasomal turnover at promyelocytic
RT   leukemia nuclear bodies.";
RL   J. Cell Sci. 123:1227-1234(2010).
CC   -!- FUNCTION: Inhibitor of the E3 ubiquitin-protein ligase ITCH. Acts
CC       by interacting with the second WW domain of ITCH, leading to
CC       compete with ITCH's substrates and impairing ubiquitination of
CC       substrates.
CC   -!- SUBUNIT: Interacts with NEDD4. Interacts with ITCH (via WW domain
CC       2).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, PML body.
CC       Note=Primarily localizes to the nucleolus. Also localizes to the
CC       PML nuclear bodies, when desumoylated.
CC   -!- PTM: Monoubiquitinated by NEDD4. Polyubiquitinated, leading to its
CC       degradation by the proteasome. Sumoylated by SUMO1, abrogating
CC       polyubiquitination and subsequent degradation. Desumoylated by
CC       SENP1, leading to accumulation in PML nuclear bodies.
CC   -!- SIMILARITY: Belongs to the N4BP1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32259.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK172981; BAD32259.1; ALT_INIT; mRNA.
DR   EMBL; AK134934; BAE22344.1; -; mRNA.
DR   EMBL; AK147522; BAE27970.1; -; mRNA.
DR   EMBL; AK170714; BAE41972.1; -; mRNA.
DR   IPI; IPI00938499; -.
DR   RefSeq; NP_085040.2; NM_030563.2.
DR   UniGene; Mm.25117; -.
DR   UniGene; Mm.428374; -.
DR   ProteinModelPortal; Q6A037; -.
DR   STRING; Q6A037; -.
DR   PhosphoSite; Q6A037; -.
DR   PRIDE; Q6A037; -.
DR   Ensembl; ENSMUST00000080846; ENSMUSP00000079657; ENSMUSG00000031652.
DR   GeneID; 80750; -.
DR   KEGG; mmu:80750; -.
DR   UCSC; uc009mqo.1; mouse.
DR   CTD; 80750; -.
DR   MGI; MGI:2136825; N4bp1.
DR   GeneTree; ENSGT00550000074448; -.
DR   HOGENOM; HBG505731; -.
DR   HOVERGEN; HBG059944; -.
DR   InParanoid; Q6A037; -.
DR   OMA; NYTMDLL; -.
DR   OrthoDB; EOG4K3KVJ; -.
DR   PhylomeDB; Q6A037; -.
DR   ArrayExpress; Q6A037; -.
DR   Bgee; Q6A037; -.
DR   CleanEx; MM_N4BP1; -.
DR   Genevestigator; Q6A037; -.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:UniProtKB.
DR   InterPro; IPR021869; RNase_Zc3h12.
DR   Pfam; PF11977; RNase_Zc3h12a; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Ubl conjugation.
FT   CHAIN         1    893       NEDD4-binding protein 1.
FT                                /FTId=PRO_0000301985.
FT   MOD_RES     241    241       Phosphothreonine (By similarity).
FT   MOD_RES     257    257       Phosphoserine (By similarity).
FT   CONFLICT     93     93       G -> E (in Ref. 2; BAE27970).
FT   CONFLICT    671    671       T -> P (in Ref. 2; BAE27970).
FT   CONFLICT    724    724       R -> T (in Ref. 2; BAE27970).
FT   CONFLICT    733    733       W -> C (in Ref. 2; BAE27970).
SQ   SEQUENCE   893 AA;  99147 MW;  AC6010E1F339B97A CRC64;
     MAARVVLDEF TAPAEKAALL ERSRGRIEAL FGVGLAVLGA LGAEEPLPAR IWLQLRGAQE
     AVHSAKEYIK GICEPELEEK ECYPKAMHCI FVGAQSLFLK SLIQDTCADL CVLDTGLLGI
     RGSAEAVVMA RSHIQQFVKL FESNENLPSN QRESEIKREF RQFVEAHADS YTMDLLILPT
     SLKKELLSLT QGEESLFETD DDVITVGDVR PPEYTQSAAT GPSSARDEVV VQEDSRNKAR
     TPVSELTKHM DTVFSSSPDV LFVPVNGLSP DEDALSKDRV CHKRRSSDTE ERHTKKQFSL
     ENVPEGELLP DGKGSAGNEV IDLSDPASNS TNLSPDGKDT TEEMEYNILV NFFKTMGYSQ
     EIVEKVIREY GPSTEPLLLL EEIEKENKRL QEDRDFPPCT VYPDASQSRN AGVGSTTNEL
     TADSTPKKAQ SHTEQSMVER FSQLPFKDSK HCTSNCKVNS FRTVPVGQKQ EIWGSKQNSS
     CTVDLETDGH SASAASASPK DISFVSRGAS GHQQRNPAFP ENGFQQQTEP LLPNNTKPAC
     EKRSGSCSSP QPKPNYPPLS PPLPLPQLLP SVTEARLGGS SDHIDSSVTG VQRFRDTLKI
     PYKLELKNEP GRADLKHIVI DGSNVAITHG LKKFFSCRGI AIAVEYFWKL GNRNITVFVP
     QWRTRRDPNI TEQHFLTQLQ ELGILSLTPA RMVFGERIAS HDDRFLLHLA DKTGGIIVTN
     DNFREFVTES VSWREIITKR LLQYTFVGDI FMVPDDPLGR NGPRLEEFLR KEAFLRHMQP
     LLNALPSVGT FDPGFRSPST QVANNSHQPP PRIQTSSSPW LPQQSHFTAL ATLPSMQQNP
     PLPAQRSSAE TSELREALLK IFPDSEQKLK IDQILAAHPY MKDLNALSAL VLD
//
ID   Q6A050_MOUSE            Unreviewed;       886 AA.
AC   Q6A050;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   08-MAR-2011, entry version 33.
DE   SubName: Full=MKIAA0545 protein;
DE   Flags: Fragment;
GN   Name=Sipa1l3; Synonyms=mKIAA0545;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Embryonic tail;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
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DR   EMBL; AK172968; BAD32246.1; -; mRNA.
DR   IPI; IPI00667750; -.
DR   UniGene; Mm.375176; -.
DR   UniGene; Mm.447042; -.
DR   ProteinModelPortal; Q6A050; -.
DR   PRIDE; Q6A050; -.
DR   Ensembl; ENSMUST00000085811; ENSMUSP00000082968; ENSMUSG00000030583.
DR   MGI; MGI:1921456; Sipa1l3.
DR   GeneTree; ENSGT00550000074284; -.
DR   HOVERGEN; HBG054989; -.
DR   OrthoDB; EOG4PZJ5R; -.
DR   ArrayExpress; Q6A050; -.
DR   Bgee; Q6A050; -.
DR   Genevestigator; Q6A050; -.
DR   InterPro; IPR021818; DUF3401.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF11881; DUF3401; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   886 AA;  97240 MW;  F14C04074685734E CRC64;
     DLQRCTRIQH GWEDVSTTHS PWPAASALSA PLSHRIWTPD SSTIKIFYGR GDHIFLQAAE
     GSVEDIRDIV QRLKVMTNGW ETVDMTLRRN GLGQLGFHVK YDGTVAEVED YGFAWQAGLR
     QGSRLVEICK VAVVTLSHDQ MIDLLRTSVT VKVVIIPPFE DGTPRRGWPE TYDMNASEPK
     TESETTTPGG RPPYRSNAPW QWSGPASHNS LPATKWTTPA TPGHAQSLSR LPKQTPVVPF
     RESQPLHSKR YAAAPHPLLS FDPHFMHDGM SSGDSSSGGL TSQESTMERP KPEPLWHVPA
     QARLSAMTGS IGSKHPSRQD AAGKDSPNRH SKGEPQYSSH SSSNTLSSNA SSSHSDDRWF
     DPLDPLEPEQ DPFSKGGSSD SGIDTTLYTS SPSCMSLAKA PRPTKPHKPP GNIGLCGGGR
     ESAGRPHPVD RRREVSPAPV VAGQNKGYRP KLYSSGSCTP PGLVGGSRDP PRQPSDMGSR
     AGYPTQVYKT ASAETPRPSQ LSQCSPFQLS TSVPKSFFSK QPAHNKHSTG WKRTDEPPPR
     PLPFTDSKKQ VDTNAKNVFG QPRLRASLRD LRSPRKNYKS TIEDDLKKLI VMDNLGPEQE
     RDTGSPKRKW SYPLFRSQPQ AERAPRNYLG SHSPKTQSPQ KSLQRTLSDE SLCSGRREPS
     FASPASLEPG LPSDVLFTST CTFPSSTLPA RRQHQHAHPP SGAPSTTPAT GNGFPEKKSA
     ISASELSLAD GRDRPLRRLD PGMMPLPDTA AGLEWSSLVN AAKAYEVQRA VSLFSLNDPA
     LSPEIPPAHS PVHSHLSLER GPQTPRATPT MSEESPLDLT GKVYQLEVML KQLHTDLQKE
     KQDKVVLQSE VASLRQNNQR LQEESQAASE QLRKFAELFS REKKEL
//
ID   Q6A062_MOUSE            Unreviewed;      1937 AA.
AC   Q6A062;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   SubName: Full=MKIAA0480 protein;
DE   Flags: Fragment;
GN   Name=Cep350; Synonyms=mKIAA0480;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Embryonic intestinal tract;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
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DR   EMBL; AK172956; BAD32234.1; -; mRNA.
DR   IPI; IPI00928565; -.
DR   UniGene; Mm.260247; -.
DR   ProteinModelPortal; Q6A062; -.
DR   PhosphoSite; Q6A062; -.
DR   PRIDE; Q6A062; -.
DR   Ensembl; ENSMUST00000138762; ENSMUSP00000120085; ENSMUSG00000033671.
DR   UCSC; uc007dbs.1; mouse.
DR   MGI; MGI:1921331; Cep350.
DR   eggNOG; roNOG14335; -.
DR   HOGENOM; HBG280472; -.
DR   HOVERGEN; HBG095435; -.
DR   InParanoid; Q6A062; -.
DR   OrthoDB; EOG4M0F0T; -.
DR   ArrayExpress; Q6A062; -.
DR   Bgee; Q6A062; -.
DR   Genevestigator; Q6A062; -.
DR   InterPro; IPR023092; CAP-Gly_CS.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   Gene3D; G3DSA:2.30.30.190; CAP-Gly_domain; 1.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   SUPFAM; SSF74924; CAP-Gly_domain; 1.
DR   PROSITE; PS00845; CAP_GLY_1; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 1.
PE   1: Evidence at protein level;
FT   NON_TER       1      1
SQ   SEQUENCE   1937 AA;  217275 MW;  B3DF1934209E67CE CRC64;
     AGSTRSSSAS KGKKGKKDKM DWLDSLTGSA QNPLIDEEKV QSDSERGSHP SRKLGTGSKL
     AVGDSEQTLD AESTLEDLSG HSVSGSSDKG RSQKTPTSPL SPSSQKLLQF DLPGTSLERS
     KSSVIVPPTT TGFKPTAAFT DVNKTEMASA PGPQRFSPAG LQHRMAAELS YLSALEESVR
     QLSDVERVRG IALAQQESVS LAQIIKAQQQ RHERDLALLK LKAEQEALEC QRQLEETRNK
     TAQVHAESLQ QVVKSQREVT EVLQEATCKI AAQQSETARL TTDAARQICE MAELTRTHLA
     DAITTSGVPL ATLYDHQRQH FPDFMRKLRT KAETDRISHS ASHSQSKEGA VDSKRQKFSP
     SRDSYSESSR YKSHDYRSSG SSRQDSPSVP PSKENEKPFH GEKMESSVDE QLQTAADDSL
     RSDSIPSLPD EKDSTSIATE YSLKFDESMT EDEIEEKSFR SLLPSESHRR FNMEKKRGHH
     DDSDEDASPD KTALSSTKEL SMPFSGGQDS FSKFTMEMVR QYMKEEEVRA AHQSSLLRLR
     EKALKEKTKA ELAWLEHQKK HLRDKGEDDK MPPLRKKQRG LLLRLQQEKA EIKRLQEANK
     AARKERQLIL KQQEEIERIR QTTIKLQEKL KSAGEKKLGS LADDDEAEDN KAASPGPPGL
     ETRSPSPISI SSSETSSIMQ KLKSMRSRMD EKFLTKREQK LMQRRQHAEE LLEWKRRLDA
     EEAEIQQMEK QALAAWDKEL VKPRTPKKEQ ESQRTEQKGI ASEEGSPMPS YSPRNSESCI
     PEDLGSPSDL CVPSEARVQA QPGSPEHSTL TEEMVFSQEL ESTSPSKHSP PKSCLSMSKQ
     ESSKASHRTE GHCHLPVKSH QPCYSWSDES LSMTQSETTS DQSDIEGRIR APKDELRKRK
     SVVEQLKREQ RKRQKERLKA QEASLLRQLE TYDEFIKKTE GELSQDLDIS PTSKFQMKTL
     SSVSEKPKIK PHPLHRSETA KTWKSVTESE RSRGSLASIA EHVDSSLSCS ERAISERSLS
     AYAKRGVELD SRIEHLQASS PDLSSRKAQT ESRDSLESAP SLSPVKELNA PDRIYDVSEA
     KAEDTSQKSE IQEIESMKLE SSEVEDACCK QSGGSEVLLK LDLASETLSS KELPSDSANV
     QQDLDKPATE TSHEKEEALK EDQSNHSTDD RSPDIQSAGG IPEQGCRESG DSTCSGQLSV
     PKESSYSEDF EVSSFRKGIS ADEISKDDSE GSSPSSLRKD SQSHRDRSQL TRSSRSRATG
     SGSDEEISEC LGEKSLSVHS GVHSERLLEL RSPTELMKSK ERSDVGHEQG GTEPLPLAAT
     EELLDFHIGD RVLIGSVQPG TLRFKGETDF AKGFWAGVEL DKPEGNNNGT YDGIVYFVCK
     DKHGIFAPPQ KISHLLENFD DTDINEDEES YSDEQYQPYN QEQKDIKCLK DRENNIAEYF
     CEKSLPSMHN TDASVDKDRS LNIETDTSEV LEVHGHQQPS VDPLISYKEN KVLVSDATES
     VPAAAGAATS DNTFSGESKQ QQLAEKEENF YSQVLEKPST PLLDLLTREK NQLEAQLKSS
     ISEEKKSKQQ LETVSLLTDS LLQVFVKDTV SQLQQVKKAR NEKIQLSNQE FLDQKKVPPQ
     DLPQNTEEQS PSVPSCFLRS ELEDEKEEIS SPDMCPRPES PVFGASGQEE LAKRLAELEI
     SREFLSALDD QDWFDEDFGL SSSHKIQKNK AEETIVPLMA EPKRAPQKPC ETLLAVPHTA
     EEVESLVHNA AEELWKWKEL GQDLHGLSLP TTFLGGASKG LDIGSTSRRV YKQAVFDLTK
     EIFEEIFAED PNVNQPVWMK PCRINSSYFR RVKNPNNLDE IKHFITTEVL KLLSLKKEPN
     HKTDWQKMMK FGRKKRDRVD HILVQELHEE EAQWVNYDED ELCVKMQLAD GIFETLIKDT
     IDVLNQISEK QGRMLLV
//
ID   CE170_MOUSE             Reviewed;        1588 AA.
AC   Q6A065; Q7TQD9; Q8BJW2; Q9D3Z0;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=Centrosomal protein of 170 kDa;
DE            Short=Cep170;
GN   Name=Cep170; Synonyms=Kiaa0470;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1462-1588 (ISOFORMS 1/3).
RC   STRAIN=C57BL/6J; TISSUE=Muellerian duct, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 786-1588 (ISOFORM 1).
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355 AND SER-358, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; SER-1102; SER-1155
RP   AND SER-1188, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443 AND SER-829, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Plays a role in microtubule organization (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with PLK1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome,
CC       centriole (By similarity). Cytoplasm, cytoskeleton, spindle (By
CC       similarity). Note=Associated with the mature mother centriole (By
CC       similarity). Associated with spindle microtubules during mitosis
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6A065-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6A065-2; Sequence=VSP_024244, VSP_024245;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q6A065-3; Sequence=VSP_024243, VSP_024246;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated; probably by PLK1. Phosphorylated upon DNA
CC       damage, probably by ATM or ATR (By similarity).
CC   -!- SIMILARITY: Belongs to the CEP170 family.
CC   -!- SIMILARITY: Contains 1 FHA domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK016937; BAB30507.2; -; mRNA.
DR   EMBL; AK078541; BAC37328.1; -; mRNA.
DR   EMBL; AC113311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC054781; AAH54781.1; -; mRNA.
DR   EMBL; BC057019; AAH57019.1; -; mRNA.
DR   EMBL; AK172953; BAD32231.1; -; mRNA.
DR   IPI; IPI00407623; -.
DR   IPI; IPI00620148; -.
DR   IPI; IPI00667973; -.
DR   UniGene; Mm.269991; -.
DR   ProteinModelPortal; Q6A065; -.
DR   SMR; Q6A065; 10-103.
DR   STRING; Q6A065; -.
DR   PhosphoSite; Q6A065; -.
DR   PRIDE; Q6A065; -.
DR   Ensembl; ENSMUST00000057037; ENSMUSP00000059562; ENSMUSG00000057335.
DR   Ensembl; ENSMUST00000070119; ENSMUSP00000064653; ENSMUSG00000057335.
DR   MGI; MGI:1918348; Cep170.
DR   eggNOG; roNOG05869; -.
DR   GeneTree; ENSGT00510000046748; -.
DR   HOGENOM; HBG714398; -.
DR   HOVERGEN; HBG058059; -.
DR   InParanoid; Q6A065; -.
DR   OMA; MSSDQET; -.
DR   OrthoDB; EOG4BCDMF; -.
DR   ArrayExpress; Q6A065; -.
DR   Bgee; Q6A065; -.
DR   CleanEx; MM_CEP170; -.
DR   Genevestigator; Q6A065; -.
DR   GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR008984; SMAD_FHA_domain.
DR   Gene3D; G3DSA:2.60.200.20; FHA; 1.
DR   Pfam; PF00498; FHA; 1.
DR   SMART; SM00240; FHA; 1.
DR   SUPFAM; SSF49879; SMAD_FHA; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Microtubule; Phosphoprotein.
FT   CHAIN         1   1588       Centrosomal protein of 170 kDa.
FT                                /FTId=PRO_0000282888.
FT   DOMAIN       23     73       FHA.
FT   REGION      844   1588       Targeting to microtubules (By
FT                                similarity).
FT   REGION     1103   1588       Targeting to centrosomes (By similarity).
FT   COILED     1467   1495       Potential.
FT   MOD_RES     167    167       Phosphoserine (By similarity).
FT   MOD_RES     353    353       Phosphoserine (By similarity).
FT   MOD_RES     355    355       Phosphoserine.
FT   MOD_RES     358    358       Phosphoserine.
FT   MOD_RES     376    376       Phosphothreonine (By similarity).
FT   MOD_RES     443    443       Phosphoserine.
FT   MOD_RES     498    498       Phosphothreonine (By similarity).
FT   MOD_RES     499    499       Phosphotyrosine (By similarity).
FT   MOD_RES     577    577       Phosphoserine (By similarity).
FT   MOD_RES     623    623       Phosphothreonine (By similarity).
FT   MOD_RES     628    628       Phosphoserine (By similarity).
FT   MOD_RES     631    631       Phosphoserine (By similarity).
FT   MOD_RES     662    662       Phosphoserine (By similarity).
FT   MOD_RES     829    829       Phosphoserine.
FT   MOD_RES     870    870       Phosphoserine (By similarity).
FT   MOD_RES     922    922       Phosphoserine (By similarity).
FT   MOD_RES     929    929       Phosphothreonine (By similarity).
FT   MOD_RES     950    950       Phosphoserine (By similarity).
FT   MOD_RES    1069   1069       Phosphoserine (By similarity).
FT   MOD_RES    1102   1102       Phosphoserine.
FT   MOD_RES    1150   1150       Phosphoserine (By similarity).
FT   MOD_RES    1155   1155       Phosphoserine.
FT   MOD_RES    1188   1188       Phosphoserine.
FT   MOD_RES    1241   1241       Phosphoserine (By similarity).
FT   MOD_RES    1250   1250       Phosphoserine (By similarity).
FT   MOD_RES    1260   1260       Phosphoserine (By similarity).
FT   MOD_RES    1521   1521       Phosphoserine (By similarity).
FT   MOD_RES    1522   1522       Phosphoserine (By similarity).
FT   MOD_RES    1529   1529       Phosphoserine (By similarity).
FT   MOD_RES    1533   1533       Phosphothreonine (By similarity).
FT   VAR_SEQ       1   1257       Missing (in isoform 3).
FT                                /FTId=VSP_024243.
FT   VAR_SEQ     211    236       CSTEAKHVEGQSAAASEEALFPFCRE -> KNTSVAVASNS
FT                                YWASIYSLNKSHSTL (in isoform 2).
FT                                /FTId=VSP_024244.
FT   VAR_SEQ     237   1588       Missing (in isoform 2).
FT                                /FTId=VSP_024245.
FT   VAR_SEQ    1344   1353       Missing (in isoform 3).
FT                                /FTId=VSP_024246.
SQ   SEQUENCE   1588 AA;  175050 MW;  B7140E6F82AF93A7 CRC64;
     MSLTSWFLVS SGGTRHRLPR EMIFVGRDDC ELMLQSRSVD KQHAVINYDA SMDEHLVKDL
     GSLNGTFVND VRIPEQTYIT LKLEDKLRFG YDTNLFTVVR GEMRVPEEAL KHEKFTIQLQ
     LSQKSSESEL PKSASAKGTD SKVEAAAEVQ PRATEALKSE EKPMDVSAMP RGTPLYGQPS
     WWGDAEEDEQ RAFKANGKPE GKSQEAGASG CSTEAKHVEG QSAAASEEAL FPFCREPSYF
     EIPTKEFQQP SQIAESTIHE IPTKDTPSSH TAGAGHASFT IEFDDSTPGK VTIRDHVTKF
     TSDQRHKSKK ASPGTQDLPG IQTGMMAPEN KVADWLAQNN PPQMVWERTE EDSKSIKSDV
     PVYLKRLKGN KHDDGTQSDS ENAGAHRRCS KRATLEEHLR RHHSEQKKKA QSTEKHQEQA
     ATSSTHHRGG HGVPHGKLLK QKSEEPSVSL PFLQTALLRS SGSLGHRPSQ EMDVMLKNQA
     TSASSEKDND DDQSDKGTYT IELENPNSEE VEARKMIDKV FGVDDNQDYN RPIINEKHKG
     LIKDWALNSA AVVMEERKPL STPGFHNSEE AISSSGSKRW VSQWASLAAN HTRHDPEERL
     MELSATVENE TDTGDAGVSL RSTSCTTSLA SQGERKRRTL PQLPNEEKLL ESSRAKVVPQ
     RSEIGEKQDT ELQEKEAQVY QSEKHDADRG LSKMSRAVNG ESPKTGGDGK ALLHSGSSSS
     KEKSETEKET SLVKQTLAKM QQQEQKEQAQ WTPTKFPSKN ALGHIDKCRE ESSKQESQLL
     EKVSGHSTSK GDRVIQNESK RRKAEEIPKC QASKGDKKES SKSLVRQGSF TIDKPSSNIP
     IELIPHINKQ NSSVPTALAL TSASRLRERS DSLDTDSSMD TTLILKDTEA VMAFLEAKLR
     EDNNKTDEGP DTPSYNRDNS ISPESDVDTA STISLVTGET ERKSTQKRKS FTSLYKDRCS
     TSSPSKDVTK SGSREKIEKK AKSRSADIGA RADGRKFVQS SGRIRQPSID LTDDDQTSSV
     PHSAISDIMS SDQETYSCKS HGRTPLTSAD EHNIHSKLEG GKATKSKTSP VASGSTSKST
     TLPRPRPTRT SLLRRARLGE ASDSELADAD KASVASEVST TSSTSKPPTG RRTISRIDLL
     AQPRRTRLGS LSARSDSEAT ISRSSASART AEAVIRSGAR LVPSDKLSPR TRANSISRLS
     DSKVKSMSST HGSPSVNSRW RRFPTDYAST SEDEFGSNRN SPKHTRLRTS PALKTTRMQS
     TGSAMPASSS FKHRIKEQED YIRDWTAHRE EIARISQDLA LIAREINDVA GEIDSVTSSG
     TAPSTTVSTA ATTPGSAIDT REEVGDLHGE MHKLVDRVFD ESLNFRKIPP LVHSKTPEGN
     NGRSVDSRPQ PAEHPDHLTI TRRRTWSRDE VMGDNLLLSS VFQFSRKIRQ SIDKTAGKIR
     ILFKDKDRNW DDIENKLRAE SEVPIVKTSS MEISSILQEL KRVEKQLQVI NAMIDPDGTL
     EALNNMGFPN AILPSPPKQK SSPVNNHSSP SQTPALCPPE TRALHPAAAG VAAAASTEFE
     NAESEADFSI HFNRFNPDGE EEDVTVHE
//
ID   F179B_MOUSE             Reviewed;        1759 AA.
AC   Q6A070;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Protein FAM179B;
GN   Name=Fam179b; Synonyms=Kiaa0423;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
CC   -!- SIMILARITY: Belongs to the FAM179 family.
CC   -!- SIMILARITY: Contains 7 HEAT repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK172948; BAD32226.1; -; Transcribed_RNA.
DR   IPI; IPI00944098; -.
DR   UniGene; Mm.138465; -.
DR   UniGene; Mm.421292; -.
DR   ProteinModelPortal; Q6A070; -.
DR   SMR; Q6A070; 181-210, 1276-1355.
DR   STRING; Q6A070; -.
DR   PhosphoSite; Q6A070; -.
DR   PRIDE; Q6A070; -.
DR   Ensembl; ENSMUST00000066296; ENSMUSP00000070382; ENSMUSG00000035614.
DR   MGI; MGI:2684313; Fam179b.
DR   HOVERGEN; HBG106757; -.
DR   InParanoid; Q6A070; -.
DR   OMA; PPIPRGI; -.
DR   OrthoDB; EOG4PVNXR; -.
DR   PhylomeDB; Q6A070; -.
DR   ArrayExpress; Q6A070; -.
DR   Bgee; Q6A070; -.
DR   Genevestigator; Q6A070; -.
DR   GermOnline; ENSMUSG00000035614; Mus musculus.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 5.
DR   SUPFAM; SSF48371; ARM-type_fold; 2.
DR   PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1   1759       Protein FAM179B.
FT                                /FTId=PRO_0000251953.
FT   REPEAT      175    212       HEAT 1.
FT   REPEAT      214    246       HEAT 2.
FT   REPEAT      389    426       HEAT 3.
FT   REPEAT      465    503       HEAT 4.
FT   REPEAT      505    542       HEAT 5.
FT   REPEAT     1582   1619       HEAT 6.
FT   REPEAT     1623   1661       HEAT 7.
FT   COMPBIAS    971   1106       Ser-rich.
FT   MOD_RES    1057   1057       Phosphoserine (By similarity).
SQ   SEQUENCE   1759 AA;  192915 MW;  BA78654DF0B771A3 CRC64;
     MAAAPSELLP LPPPATPGSY RLLSRCRPYA PGTDGRRSGG TMRGEKNYYC RGAAGDHGSC
     PATPSPLAST LLLPAEAVST SWSGPGSGLS GGDEEETRLL QLLRTAPDPS EAFQALQAAL
     PRRGGRLGFP RRKEALYRAL GRVLVEGGSE EKRLCLQLLS DVLRGQGEAG QLEEAFSLAL
     LPQLVVSLRE DNPALRKDAL QILHICLRRS SGQVLRTLIQ GLESPDARLR ASTALLLPIL
     FTPEDLLQGL DLTEVIISLA RKLGDQEMEE ESETAFSSLQ QIGERLGQER FHSYISRLPS
     ALRRHYNRRL ESQYGSQVPY YLELEASGFS EDAAPCVVNL SSSNLKFEII PQELHARLLD
     QEDYKNRTQA VEELKQLLGK FNPSSTPHAS LVGFISLLYN LLDDSNFKVV HGTLQVLHLL
     VIRLGEQVQQ FLGPVIAASV KVLADNKLVI KQEYMKIFLK LMKEVGPQRV LSLLLENLKH
     KHSRVREEVV NICICSLLTY PSEDFDLPKL SFDLAPALVD SKRRVRQAAL EAFAVLASSM
     GSGKTNVLFK AVDTVELQDN GDGVMNAVQA RLARKTLPRL TEQGFVEYAI LMPSSAQGRS
     SHLAHGADTD WLMSGNRTQS AHCYCGDHTR DSMQLYGSYS PTICTRRVLS AGKGKNKLPW
     ENEQPGVMGE NQTSNSKDIK DTEQFSAHDL IPSPKLKPSQ GMPASDDLCF SKKRSSRNLF
     QSSRDFNSES VPTCGAGNTA DLQTNLPGKC GQLGLSQIGC RTGSVGSDLQ FLGTANGHQD
     KVYASIDFGS KTQQTFGSQS ERTSSYSGSN ASPGSFILPS YPLASPRTSP KHTSPLSVAP
     KKSQDNSISF SNSWPLKSFE GLSKPSPQKK LANQKSSDPT GENFQEKTTA VQLTPALVRS
     PSSRRGLNGT KPVPPIPRGI NLLPDKADLS TMGHMKKQPD DIWKSEKDNL TIDLSELNFR
     DKDLDQEEMH SSLRSLRNSA AKKRAKLSGS SSTSDVDSPD SAMKLELTID SPSRASSPNI
     SSYSESGVYS QESLTSSLST TPQGKRIMSD IFPTFGSKPC STRLSSAKKT SHAAEQSPSA
     GFTRSSNLQQ ISSFDFTSTN TLSEDSVVIV GKGVFGNPNS APTTCSQPVI SSVESEDTFP
     VKPSIEPPSG VYGRAVQHNA PLYPEVENDK DTKVSIAKST YEKMRQKRKE EKELLDAKDC
     ERKETNPWER IKHLGSEKMT SENEPSSGVI PQYKERMSSV THSPEIMDSL ELRPFSKPDI
     ALTEALRLLA DEDWEKKMEG LNFVRCLAAF HSDLLNTKLH ETTFAVVQEV KNLRSGVSRA
     AVVCLGDLFT YLKKSMDQEL DSAVRALLHK AGESNTFIRE DVDKALKAMV NNVTPARAVT
     SLINGGQSHL HIAVRRCTAQ HLADVVECMD PERISSGTKD MADRLLPAAA KFAQDSSQET
     RYYGRKMLFL MMGHPNFEKL LEKYIPSKDL PYIKESVKNL RLKGLGEIPL DTASAKGRRS
     HPGSVGNTRS SSVSRDAFSS SEREVTEVRE VPRKSAPRNS LESAEYIKVI TGLLNAKDFR
     DRINGIKQLL SDTENNQELV VGNIVKIFDA FKSRLHDSNS KVNLVALETM HKMIPLLRDN
     LSPIINMLIP AIVDNNLNSK NPGIYAAATN VVHALSQHNG KAKQDMTEKL ADIVTELYQR
     KPHATEQKVL VVLWHLLGNM THSGSLPGAG GNIRTATAKL SKALFTQMGQ NLLNQAASQP
     PHIKKSLEEL LDVTVLSEL
//
ID   Q6A088_MOUSE            Unreviewed;       333 AA.
AC   Q6A088;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   05-OCT-2010, entry version 34.
DE   SubName: Full=MKIAA0299 protein;
DE   Flags: Fragment;
GN   Name=Dock3; Synonyms=mKIAA0299;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK172930; BAD32208.1; -; mRNA.
DR   IPI; IPI00624328; -.
DR   UniGene; Mm.150259; -.
DR   ProteinModelPortal; Q6A088; -.
DR   PRIDE; Q6A088; -.
DR   UCSC; uc009rkw.1; mouse.
DR   Genevestigator; Q6A088; -.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   333 AA;  37318 MW;  CCA77B530FDB4C48 CRC64;
     ALARVARGSS AARGVSRSVR TWHPAVAVAS RTACEGCAAY CPAPPDRPRL ASRCATAGPA
     AAPAAVPCEL SPSRRARGAA PGPAMWTPTE EEKYGVVICS FRGSVPQGLV LEIGETVQIL
     EKCEGWYRGV STKKPNVKGL FPANYIHLKK AIVSNRGQYE TVVPLEDSIV TEVTTTLQEW
     ASLWKQLYVK HKVDLFYKLR HVMNELIDLR RQLLSGHLTQ DQVREVKRHI TVRLDWGNEH
     LGLDLVPRKD FEVVDSDQIS VSDLYKMHLS SRQSVQQSTS QVDTMRPRHG ETCRMPVPHH
     FFFSLKSFTY NTIGEDSDVF FSLYDMREGK QIR
//
ID   SBP2L_MOUSE             Reviewed;        1086 AA.
AC   Q6A098;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   08-MAR-2011, entry version 44.
DE   RecName: Full=Selenocysteine insertion sequence-binding protein 2-like;
DE            Short=SECIS-binding protein 2-like;
GN   Name=Secisbp2l; Synonyms=Kiaa0256;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreatic islet;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264 AND SER-276, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32198.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK172920; BAD32198.1; ALT_INIT; Transcribed_RNA.
DR   IPI; IPI00553429; -.
DR   UniGene; Mm.138091; -.
DR   ProteinModelPortal; Q6A098; -.
DR   SMR; Q6A098; 706-811.
DR   PhosphoSite; Q6A098; -.
DR   PRIDE; Q6A098; -.
DR   Ensembl; ENSMUST00000053699; ENSMUSP00000055772; ENSMUSG00000035093.
DR   MGI; MGI:1917604; Secisbp2l.
DR   InParanoid; Q6A098; -.
DR   OrthoDB; EOG4933H6; -.
DR   ArrayExpress; Q6A098; -.
DR   Bgee; Q6A098; -.
DR   CleanEx; MM_3110001I20RIK; -.
DR   Genevestigator; Q6A098; -.
DR   GermOnline; ENSMUSG00000035093; Mus musculus.
DR   InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45.
DR   Pfam; PF01248; Ribosomal_L7Ae; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1   1086       Selenocysteine insertion sequence-binding
FT                                protein 2-like.
FT                                /FTId=PRO_0000050740.
FT   MOD_RES     264    264       Phosphoserine.
FT   MOD_RES     276    276       Phosphoserine.
SQ   SEQUENCE   1086 AA;  119641 MW;  E016F2E4E207DF52 CRC64;
     MDRAPAEQNV KLSAEVEPFV PQKKNLDAFV LPMALPSDNG SVSGVEPTPI PSYLITCYPF
     VQENQSNRQF PLYNNDIRWQ QPSPSPTGPY LAYPIISAQP PVSTEYTYYQ LMPAPCAQVM
     GFYHPFPTPY SSTFQAANTV NAISTECTER PNQLGQAFPL SSHRSRNGNR GPVVPKPQLL
     QQHIKNKRPQ VKNVATQKET SATGPDSRSK IVLLVDASQQ TDFPSDIANK SLSESTATML
     WKAKGRRRRA SHPAVESSSE QGASEADIDS DSGYCSPKHN NQSAPGALRD PASGTMNRLE
     SSGCSGGVNW PKVTCQATQK RPWMEKNQAF SRGGRQTEQR NNLQVGFRCR GHSTSSERRQ
     NLQKRQDNKH LNSTQSHRSD PNSESLYFED EDGFQELSEN GNSKDENIQQ KLSSKVLDDL
     PENSPINIVQ TPIPITTSVP KRAKSQKKKA LAAALATAQE YSEISKKSCR KLYQKQLEKT
     KTPVQLDLGD MLAALEKQQQ AMKARQITNT RPLAHPVVTT ATFHTKDSNR KTLAKSQPCV
     TSFNSLDITS SKAKKGKEKE IAKLKRPTAL KKVILKEREE KKGRLIVEHS VLGAEEPTET
     HLDLTNDLPQ ETVSQEDAGL SMPSDASLSP ASQNSPYCMT PVSQGSPASS GIGSPMASST
     ITKIHSKRFR EYCNQVLSKE IDECVTLLLQ ELVSFQERIY QKDPVRAKAR RRLVMGLREV
     TKHMKLNKIK CVIISPNCEK IQSKGGLDEA LYNVIAMARE QEIPFVFALG RKALGRCVNK
     LVPVSVVGIF NYFGAESLFN RLVELTEEAR KAYKDMVAAT EQEQAEEALR SVKTVPHHMG
     HSRNPSAASA ISFCSVISEP ISEVNEKEYE TNWRSMVETS DGLEPSEMEK AAPCTHSPPE
     KPSRLALDTS LVGKQLPLAA GSITSAPSQG KPTGDKDELK PDDLEWASQQ STETGSLDGS
     CRDLLNSSIT STTSTLVPGM LEEEEDEEEE EEDYSHEPTA EEVQLNSRIE SWVSETQRTM
     ETLQLGKALP GSEEDSAEQS GEEAAEVPEG LESGADSETW TPDQPPKPSS NMGKEHPDSS
     SPPQST
//
ID   Q6A099_MOUSE            Unreviewed;      1803 AA.
AC   Q6A099;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   08-MAR-2011, entry version 32.
DE   SubName: Full=MKIAA0248 protein;
DE   Flags: Fragment;
GN   Name=Gbf1; Synonyms=mKIAA0248;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
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DR   EMBL; AK172919; BAD32197.1; -; mRNA.
DR   IPI; IPI00463493; -.
DR   UniGene; Mm.271620; -.
DR   ProteinModelPortal; Q6A099; -.
DR   STRING; Q6A099; -.
DR   Ensembl; ENSMUST00000026254; ENSMUSP00000026254; ENSMUSG00000025224.
DR   UCSC; uc008hsq.1; mouse.
DR   MGI; MGI:1861607; Gbf1.
DR   HOVERGEN; HBG005810; -.
DR   InParanoid; Q6A099; -.
DR   ArrayExpress; Q6A099; -.
DR   Bgee; Q6A099; -.
DR   Genevestigator; Q6A099; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000904; Sec7.
DR   InterPro; IPR023394; SEC7_alpha_orthog.
DR   Gene3D; G3DSA:1.10.1000.11; G3DSA:1.10.1000.11; 1.
DR   Pfam; PF01369; Sec7; 1.
DR   SMART; SM00222; Sec7; 1.
DR   SUPFAM; SSF48425; Sec7; 1.
DR   PROSITE; PS50190; SEC7; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   1803 AA;  200183 MW;  DEF62DA28ED408D6 CRC64;
     ELSEIEPNVF LRPFLEVIRS EDTTGPITGL ALTSVNKFLS YALIDPTHEG TAEGMENMAD
     AVTHARFVGT DPASDEVVLM KILQVLRTLL LTPVGTHLTN ESVCEIMQSC FRICFEMRLS
     ELLRKSAEHT LVDMVQLLFT RLPQFKEEPK SYVGTNMKKL KMRAGGMSDS SKWKKQKRSP
     RPPRHTTKVT PGSELPTPNG ATLPSNLTGG VPFIDAPTSI SSASSEAAST VVSPCTDSGL
     ELSSQTTSKE DLTDLEQAGS PREITTSEPG SSEMGASDQL DPQEGAHVEK AQSASVESIP
     EVLEECTSPA DHSDSASVHD MDYVNPRGVR FTQSSQKEGT ALVPYGLPCI RELFRFLISL
     TNPHDRHNSE VMIHMGLHLL TVALESAPVA QCQTLLGLIK DEMCRHLFQL LSVERLNLYA
     ASLRVCFLLF ESMREHLKFQ LEMYIKKLME IITVENPKMP YEMKEMALEA VVQLWRIPSF
     VTELYINYDC DYYCSNLFED LTKLLSKNAF PVSGQLYTTH LLSLDALLTV IDSTESHCQA
     KVLNTLNQQE KKETARPGFE AVDGNPETNK SERATSDGKS TGVALDARGL HFPSGGWLST
     EHGKPGCRDL EEAGDSGADK KFTRKPPRFS CLLPDPRELI EIKNKKKLLI TGTEQFNQKP
     KKGIQFLQEK GLLTIPMDNT EVAQWLRENP RLDKKMIGEF VSDRKNMDLL ESFVSTFSFQ
     GLRLDEALRL YLEAFRLPGE APVIHRLLEV FTEHWRSCNG SPFANSDACF ALAYAVIMLN
     TDQHNHNVRK QNAPMTLEEF RKNLKGVNGG KDFEQDILED MYHAIKNEEI VMPEEQTGLV
     RENYVWSVLL HRGASPEGVF LRVPPGSYDL DLFTMTWGPT IAALSYVFDK SLEETIIQKA
     ISGFRKCAMI SAHYGLSDVF DNLIISLCKF TALSSESIEN LPSVFGSNPK AHIAAKTVFH
     LAHRHGDILR EGWKNIMEAM LQLFRAQLLP KAMVEVEDFV DPNGKISLQR EETPSNRGES
     TVLSFVSWLT LSGPEQSSVR GPSTENQEAK RVALDCIKQC DPEKMITESK FLQLESLQEL
     MKALVSVTPD EETYDEEDAA FCLEMLLRIV LENRDRVGCV WQTVRDHLYH LCVQAQDFCF
     LVERAVVGLL RLAIRLLRRE EISGQVLLSL RILLLMKPSV LSRVSHQVAY GLHELLKTNA
     ANIHSGDDWA TLFTLLECIG SGVKPPDALQ ATARADAPDA GAQSDSELPS YHQNDVSLDR
     GYTSDSEVYT DHGRPGKIHR SATDADMVNS GWLVVGKDDI DNSKPGAGLS RPGPSPLVNQ
     YSLTVGLDLG PHDTKSLLKC VESLSFIVRD AAHITPDNFE LCVKTLRIFV EASLNGGCKS
     QDKRSKSHKY DSKGNRFKKK PKEGSMLRRP RGSNQHATRG GHSDEEEDEG VPASYHTVSL
     QLLDLMHTLH TRAASIYSSW AEEQRHLEGG GQKIEADSRT LWAHCWCPLL QGIACLCCDA
     RRQVRMQALT YLQRALLVHD LQKLDALEWE SCFNKVLFPL LTKLLENISP ADVGGMEETR
     MRASTLLSKV FLQHLSPLLS LSTFAALWLT ILDFMDKYMH AGSSDLLSEA IPESLKNMLL
     VMDTAEIFHS ADARGGGPSA LWEITWERID CFLPHLRDEL FKQTVIQDPM PAEPHSQKPL
     ASTHLTSAAG DPRMPGHPPL PEIPSEMGVC DSEKPESTRA PSSSSPGSPM ASSPSKLSPA
     QEGPPPLTQP PLILQPLTSP LQVGVPPMTL PIILNPALIE ATSPVPLLAT PRPTDPIPTS
     EVN
//
ID   LAR4B_MOUSE             Reviewed;         741 AA.
AC   Q6A0A2; Q3TUH7; Q6AZA8; Q8BJP3; Q8BY17;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=La-related protein 4B;
DE   AltName: Full=La ribonucleoprotein domain family member 4B;
DE   AltName: Full=La ribonucleoprotein domain family member 5;
DE   AltName: Full=La-related protein 5;
GN   Name=Larp4b; Synonyms=D13Wsu64e, Kiaa0217, Larp5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-672 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Adipose tissue, Head, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-721, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500 AND SER-721, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6A0A2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6A0A2-2; Sequence=VSP_023987;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q6A0A2-3; Sequence=VSP_023988;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 HTH La-type RNA-binding domain.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32194.1; Type=Erroneous initiation;
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DR   EMBL; AK172916; BAD32194.1; ALT_INIT; mRNA.
DR   EMBL; AK042491; BAC31273.2; -; mRNA.
DR   EMBL; AK080953; BAC38091.1; -; mRNA.
DR   EMBL; AK160759; BAE35994.1; -; mRNA.
DR   EMBL; BC078640; AAH78640.1; -; mRNA.
DR   IPI; IPI00469235; -.
DR   IPI; IPI00620564; -.
DR   IPI; IPI00831428; -.
DR   RefSeq; NP_766173.1; NM_172585.2.
DR   UniGene; Mm.392515; -.
DR   UniGene; Mm.479947; -.
DR   HSSP; Q71RC2; 2CQK.
DR   ProteinModelPortal; Q6A0A2; -.
DR   SMR; Q6A0A2; 154-239.
DR   PhosphoSite; Q6A0A2; -.
DR   PRIDE; Q6A0A2; -.
DR   Ensembl; ENSMUST00000038260; ENSMUSP00000046477; ENSMUSG00000033499.
DR   Ensembl; ENSMUST00000091828; ENSMUSP00000089436; ENSMUSG00000033499.
DR   Ensembl; ENSMUST00000091829; ENSMUSP00000089437; ENSMUSG00000033499.
DR   GeneID; 217980; -.
DR   KEGG; mmu:217980; -.
DR   CTD; 217980; -.
DR   MGI; MGI:106330; Larp4b.
DR   eggNOG; roNOG13174; -.
DR   GeneTree; ENSGT00530000063417; -.
DR   InParanoid; Q6A0A2; -.
DR   OMA; AKVWGNH; -.
DR   OrthoDB; EOG4FN4HK; -.
DR   NextBio; 376122; -.
DR   ArrayExpress; Q6A0A2; -.
DR   Bgee; Q6A0A2; -.
DR   CleanEx; MM_LARP5; -.
DR   Genevestigator; Q6A0A2; -.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR006630; Lupus_La_RNA-bd.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF05383; La; 1.
DR   SMART; SM00715; LA; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50961; HTH_LA; 1.
DR   PROSITE; PS50102; RRM; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Phosphoprotein; RNA-binding.
FT   CHAIN         1    741       La-related protein 4B.
FT                                /FTId=PRO_0000281140.
FT   DOMAIN      152    241       HTH La-type RNA-binding.
FT   DOMAIN      242    309       RRM.
FT   MOD_RES     426    426       Phosphoserine (By similarity).
FT   MOD_RES     436    436       Phosphoserine (By similarity).
FT   MOD_RES     453    453       Phosphoserine (By similarity).
FT   MOD_RES     500    500       Phosphoserine.
FT   MOD_RES     518    518       Phosphoserine (By similarity).
FT   MOD_RES     520    520       Phosphothreonine (By similarity).
FT   MOD_RES     526    526       Phosphoserine (By similarity).
FT   MOD_RES     570    570       Phosphoserine (By similarity).
FT   MOD_RES     603    603       Phosphoserine (By similarity).
FT   MOD_RES     666    666       Phosphoserine (By similarity).
FT   MOD_RES     667    667       Phosphoserine (By similarity).
FT   MOD_RES     721    721       Phosphoserine.
FT   MOD_RES     727    727       N6-acetyllysine (By similarity).
FT   MOD_RES     730    730       Phosphoserine (By similarity).
FT   MOD_RES     735    735       Phosphothreonine (By similarity).
FT   MOD_RES     739    739       Phosphoserine (By similarity).
FT   VAR_SEQ     414    497       Missing (in isoform 2).
FT                                /FTId=VSP_023987.
FT   VAR_SEQ     568    645       Missing (in isoform 3).
FT                                /FTId=VSP_023988.
FT   CONFLICT    102    102       A -> D (in Ref. 1; BAD32194).
FT   CONFLICT    345    345       L -> S (in Ref. 1; BAD32194).
FT   CONFLICT    688    688       Q -> R (in Ref. 1; BAD32194).
SQ   SEQUENCE   741 AA;  81627 MW;  EE7DCECD17343C48 CRC64;
     MTSDQDAKVV AEPQAQRVQE GKDSSHLMNG PISQTTSQTR SLPALTQVPT TKVSELNPNA
     KVWGTHMLHL EASSAAVGVN AAWEEAPGHP TDCDQQVLGL DANGDGDKSR ENAALPDAQE
     AEQTDMSTLA LDHSEYEPLP ENNDTGGNES QPESQEDPRE VLKKTLEFCL SRENLASDMY
     LISQMDSDQY VPITTVANLD HIKKLSTDVD LIVEVLRSLP LVQVDEKGEK VRPNQNRCIV
     ILREISESTP VEEVEALFKG DNLPKFINCE FAYNDNWFIT FETEADAQQA YKYLREEVRT
     FQGKPIKARI KAKAIAINTF LPKNGFRPLD MNLYTQQRYA TSFYLPPVYS PQQQFPLYSL
     ITPQTWSTTH SYLDPPLVTP FPSTGFINGF TSPTFKPATS PLTSLRQYPP RSRNPSKSHL
     RHAIPSTERG PGLLESPSIF NFTADRLING VRSPQTRQAG QTRTRIQNPS AYAKREIGTG
     RVEPSSLESS PGLGRGRKNS FGYRKKREEK FTSSQTQSPT PPKPPSPSFE LGLSNFPPLP
     GAAGNLKTED LFENRLSSLI IGSSKERNLS TDASTNTVPV VGPREPSVPA PCAVSAAFER
     SPSPVHLPED PKVAEKQRET QSVDRLPSTP TTTACKSVQV NGAATELRKP SYAEICQRTS
     KDPSSSSPLQ PPKEQKPSTV ACGKEEKQLS EPVERHREPP ALKSTPGVPK DQRRQPGRRA
     SPPAAGKRLS KEQNTPPKSP Q
//
ID   RFTN1_MOUSE             Reviewed;         554 AA.
AC   Q6A0D4; Q3U654; Q3U8P6; Q80US1;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   08-MAR-2011, entry version 47.
DE   RecName: Full=Raftlin;
DE   AltName: Full=Raft-linking protein;
GN   Name=Rftn1; Synonyms=Kiaa0084;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=22688952; PubMed=12805216; DOI=10.1093/emboj/cdg293;
RA   Saeki K., Miura Y., Aki D., Kurosaki T., Yoshimura A.;
RT   "The B cell-specific major raft protein, Raftlin, is necessary for the
RT   integrity of lipid raft and BCR signal transduction.";
RL   EMBO J. 22:3015-3026(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-536, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-530 AND
RP   SER-536, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May play a pivotal role in the formation and/or
CC       maintenance of lipid rafts. May regulate B-cell antigen receptor-
CC       mediated signaling.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor (By similarity).
CC       Note=Associates with lipid rafts (By similarity).
CC   -!- TISSUE SPECIFICITY: Specifically expressed by lymphocytes.
CC   -!- SIMILARITY: Belongs to the raftlin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32162.1; Type=Erroneous initiation;
CC       Sequence=BAE31871.1; Type=Erroneous initiation;
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DR   EMBL; AK172884; BAD32162.1; ALT_INIT; mRNA.
DR   EMBL; AK152130; BAE30971.1; -; mRNA.
DR   EMBL; AK153288; BAE31871.1; ALT_INIT; mRNA.
DR   EMBL; AK155870; BAE33473.1; -; mRNA.
DR   EMBL; BC052074; AAH52074.1; -; mRNA.
DR   IPI; IPI00469253; -.
DR   RefSeq; NP_852062.1; NM_181397.2.
DR   UniGene; Mm.41854; -.
DR   ProteinModelPortal; Q6A0D4; -.
DR   PRIDE; Q6A0D4; -.
DR   Ensembl; ENSMUST00000044503; ENSMUSP00000046524; ENSMUSG00000039316.
DR   GeneID; 76438; -.
DR   KEGG; mmu:76438; -.
DR   UCSC; uc008cyr.1; mouse.
DR   CTD; 76438; -.
DR   MGI; MGI:1923688; Rftn1.
DR   eggNOG; roNOG10102; -.
DR   HOGENOM; HBG714935; -.
DR   HOVERGEN; HBG093894; -.
DR   InParanoid; Q6A0D4; -.
DR   OMA; EDSKTIQ; -.
DR   OrthoDB; EOG40P46F; -.
DR   PhylomeDB; Q6A0D4; -.
DR   NextBio; 345158; -.
DR   ArrayExpress; Q6A0D4; -.
DR   Bgee; Q6A0D4; -.
DR   CleanEx; MM_RFTN1; -.
DR   Genevestigator; Q6A0D4; -.
DR   GermOnline; ENSMUSG00000039316; Mus musculus.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Cell membrane; Lipoprotein; Membrane; Myristate; Palmitate;
KW   Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    554       Raftlin.
FT                                /FTId=PRO_0000251954.
FT   MOD_RES     183    183       Phosphoserine.
FT   MOD_RES     199    199       Phosphoserine (By similarity).
FT   MOD_RES     530    530       Phosphoserine.
FT   MOD_RES     536    536       Phosphoserine.
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
FT   LIPID         3      3       S-palmitoyl cysteine (By similarity).
FT   CONFLICT    236    236       Q -> R (in Ref. 2; BAE30971/BAE31871).
FT   CONFLICT    472    472       N -> D (in Ref. 1; BAD32162).
SQ   SEQUENCE   554 AA;  61537 MW;  34AFE53D91861A2C CRC64;
     MGCSLNKLEK REEKRPGNIY STLKRPQVET KVDVTYEYCF LEFTTLTAAE LPRSSATRLA
     SLRDLPDQLL ELYQQGFSLA ALHPFVQPTR RQEKILLEHI FRAILVKKTN RSQKAELHDE
     GYTLELDYCS SLEHLADQKL IPEFIKKVQE AASQGLKFVS VVPQYQPSVS SAGSRRLKPV
     ANSVEDARDV KCTLGDRSSL ENDTPKAAET DAATAGVNRR PETKPGSTGD VPSAQQPGIP
     SPSAENEAGE FPLRGLQPAL DRSEGDPSNG PEELPSRKME IFAFFNRPKS QQKCRQYYPV
     TIPLQVSKNG QTVSSLDASW LEHMSDHFRK GGVLVNAVFQ LGMANDSFYG LTDGVFIFEA
     VSTEDNRTTQ GYDAIVVEQW TVLEGTEVQT DYMPLLNSLA AYGWQLTCVL PTPILKTTRE
     GNVSTKQIVF LQRPCLPQKT KKRESKFQWR FSRNEIHGRQ TRKSKGKLSA SNKQQAEENE
     KNLEDQFSKA GDVGNCVLGA PQWGRASEVR EQRQGSAAVQ NGPAGHNRDS VALRHSNPRA
     EAELAAGPTP TEAN
//
ID   UBP7_MOUSE              Reviewed;        1103 AA.
AC   Q6A4J8; Q3UX92; Q496Y5; Q8BW01;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 7;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 7;
DE   AltName: Full=Herpesvirus-associated ubiquitin-specific protease;
DE            Short=mHAUSP;
DE   AltName: Full=Ubiquitin thioesterase 7;
DE   AltName: Full=Ubiquitin-specific-processing protease 7;
GN   Name=Usp7; Synonyms=Hausp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP   INTERACTION WITH TP53, AND MUTAGENESIS OF CYS-224.
RX   PubMed=14719112;
RA   Lim S.-K., Shin J.-M., Kim Y.-S., Baek K.-H.;
RT   "Identification and characterization of murine mHAUSP encoding a
RT   deubiquitinating enzyme that regulates the status of p53
RT   ubiquitination.";
RL   Int. J. Oncol. 24:357-364(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-545 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 832-1103.
RC   STRAIN=C57BL/6J; TISSUE=Egg, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 214-1103 (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19946331; DOI=10.1038/onc.2009.427;
RA   Kon N., Kobayashi Y., Li M., Brooks C.L., Ludwig T., Gu W.;
RT   "Inactivation of HAUSP in vivo modulates p53 function.";
RL   Oncogene 29:1270-1279(2010).
CC   -!- FUNCTION: Hydrolase that deubiquitinates target proteins such as
CC       FOXO4, p53/TP53, MDM2, PTEN and DAXX. Together with DAXX, prevents
CC       MDM2 self-ubiquitination and enhances the E3 ligase activity of
CC       MDM2 towards p53/TP53, thereby promoting p53/TP53 ubiquitination
CC       and proteasomal degradation. Deubiquitinates p53/TP53 and MDM2 and
CC       strongly stabilizes p53/TP53 even in the presence of excess MDM2,
CC       and also induces p53/TP53-dependent cell growth repression and
CC       apoptosis. Deubiquitination of FOXO4 in presence of hydrogen
CC       peroxide is not dependent on p53/TP53 and inhibits FOXO4-induced
CC       transcriptional activity. In association with DAXX, is involved in
CC       the deubiquitination and translocation of PTEN from the nucleus to
CC       the cytoplasm, both processes that are counteracted by PML.
CC       Involved in cell proliferation during early embryonic development.
CC   -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- SUBUNIT: Monomer. Homodimer. Part of a complex with DAXX, MDM2,
CC       RASSF1 and USP7. Part of a complex with DAXX, MDM2 and USP7.
CC       Interacts with MDM2; the interaction is independent of p53/TP53.
CC       Interacts with DAXX; the interaction is direct and independent of
CC       MDM2 and p53/TP53. Interacts with FOXO4; the interaction is
CC       enhanced in presence of hydrogen peroxide and occurs independently
CC       of p53/TP53. Interacts with p53/TP53; the interaction is enhanced
CC       in response to DNA damage; the interaction is impaired by TSPYL5.
CC       Interacts with PTEN; the interaction is direct. Interacts with
CC       UBXN6. Interacts with ATXN1 and the strength of interaction is
CC       influenced by the length of the poly-Gln region in ATXN1. A weaker
CC       interaction seen with mutants having longer poly-Gln regions (By
CC       similarity). Interacts with p53/TP53.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm (By similarity). Nucleus,
CC       PML body (By similarity). Note=Present in a minority of ND10
CC       nuclear bodies. Colocalizes with ATXN1 in the nucleus. Colocalized
CC       with DAXX in speckled structures. Colocalized with PML and PTEN in
CC       promyelocytic leukemia protein (PML) nuclear bodies (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6A4J8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6A4J8-2; Sequence=VSP_021952;
CC       Name=3;
CC         IsoId=Q6A4J8-3; Sequence=VSP_021953, VSP_021954;
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in brain, lung,
CC       thymus and testis. Expressed at low levels in the liver.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryo at 3.5 and from 7.5 to
CC       10.5 dpc (at protein level).
CC   -!- DOMAIN: The C-terminus plays a role in its oligomerization (By
CC       similarity).
CC   -!- PTM: Phosphorylated at positions Ser-19 and Ser-964 (By
CC       similarity).
CC   -!- PTM: Polyneddylated (By similarity).
CC   -!- PTM: Not sumoylated (By similarity).
CC   -!- PTM: Polyubiquitinated. Ubiquitinated at Lys-870 (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Led to early embryonic lethality. Show
CC       desorganized germinal layers without the formation of a
CC       proamniotic cavity. Many of the surviving cells were trophoblastic
CC       giant cells with large nuclei.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC   -!- SIMILARITY: Contains 1 MATH domain.
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DR   EMBL; AF548565; AAQ12339.1; -; mRNA.
DR   EMBL; AK075830; BAC35992.1; -; mRNA.
DR   EMBL; AK135814; BAE22671.1; -; mRNA.
DR   EMBL; BC100666; AAI00667.1; -; mRNA.
DR   IPI; IPI00463367; -.
DR   IPI; IPI00817018; -.
DR   IPI; IPI00969838; -.
DR   RefSeq; NP_001003918.2; NM_001003918.2.
DR   UniGene; Mm.295330; -.
DR   HSSP; Q93009; 1NBF.
DR   ProteinModelPortal; Q6A4J8; -.
DR   SMR; Q6A4J8; 64-555.
DR   STRING; Q6A4J8; -.
DR   MEROPS; C19.016; -.
DR   PhosphoSite; Q6A4J8; -.
DR   PRIDE; Q6A4J8; -.
DR   Ensembl; ENSMUST00000090399; ENSMUSP00000087880; ENSMUSG00000022710.
DR   Ensembl; ENSMUST00000115836; ENSMUSP00000111502; ENSMUSG00000022710.
DR   GeneID; 252870; -.
DR   KEGG; mmu:252870; -.
DR   UCSC; uc007ycw.1; mouse.
DR   CTD; 252870; -.
DR   MGI; MGI:2182061; Usp7.
DR   eggNOG; roNOG10276; -.
DR   GeneTree; ENSGT00600000084170; -.
DR   HOVERGEN; HBG018029; -.
DR   OrthoDB; EOG4640B4; -.
DR   PhylomeDB; Q6A4J8; -.
DR   BRENDA; 3.1.2.15; 244.
DR   NextBio; 387363; -.
DR   ArrayExpress; Q6A4J8; -.
DR   Bgee; Q6A4J8; -.
DR   CleanEx; MM_USP7; -.
DR   Genevestigator; Q6A4J8; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; ISS:UniProtKB.
DR   GO; GO:0004843; F:ubiquitin-specific protease activity; ISS:UniProtKB.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR   GO; GO:0051090; P:regulation of transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR002083; MATH.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19.
DR   InterPro; IPR008974; TRAF-like.
DR   Pfam; PF00917; MATH; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00061; MATH; 1.
DR   SUPFAM; SSF49599; Traf_like; 1.
DR   PROSITE; PS50144; MATH; 1.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; 1.
DR   PROSITE; PS50235; UCH_2_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Developmental protein;
KW   Hydrolase; Isopeptide bond; Nucleus; Phosphoprotein; Protease;
KW   Thiol protease; Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN         1   1103       Ubiquitin carboxyl-terminal hydrolase 7.
FT                                /FTId=PRO_0000268006.
FT   DOMAIN       69    196       MATH.
FT   REGION        1    209       Interaction with TSPYL5 (By similarity).
FT   REGION       54    209       Interaction with p53/TP53 and MDM2 (By
FT                                similarity).
FT   REGION       71    206       Necessary for nuclear localization (By
FT                                similarity).
FT   COMPBIAS      4     17       Gln-rich.
FT   ACT_SITE    224    224       Nucleophile (By similarity).
FT   ACT_SITE    465    465       Proton acceptor (By similarity).
FT   MOD_RES      19     19       Phosphoserine.
FT   MOD_RES      50     50       Phosphoserine (By similarity).
FT   MOD_RES     596    596       N6-acetyllysine (By similarity).
FT   MOD_RES     870    870       N6-acetyllysine (By similarity).
FT   MOD_RES     964    964       Phosphoserine (By similarity).
FT   MOD_RES    1085   1085       N6-acetyllysine (By similarity).
FT   MOD_RES    1097   1097       N6-acetyllysine (By similarity).
FT   CROSSLNK    870    870       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   VAR_SEQ       1     27       MNHQQQQQQQQKAGEQQLSEPEDMEME -> MASSTSPPRS
FT                                PSGGILTQDTIYFPQSNIISELLPWYLRYTPPEVPSTSVIT
FT                                KFILVNCPWNEGIEYQ (in isoform 2).
FT                                /FTId=VSP_021952.
FT   VAR_SEQ     974    974       E -> ECLQ (in isoform 3).
FT                                /FTId=VSP_021953.
FT   VAR_SEQ    1094   1103       YLEKAIKIHN -> LGLC (in isoform 3).
FT                                /FTId=VSP_021954.
FT   MUTAGEN     224    224       C->S: Loss of p53/TP53-deubiquitinating
FT                                activity.
FT   CONFLICT    162    162       E -> K (in Ref. 2; BAE22671).
SQ   SEQUENCE   1103 AA;  128475 MW;  989DFE733F0D961E CRC64;
     MNHQQQQQQQ QKAGEQQLSE PEDMEMEAGD TDDPPRITQN PVINGNVTLS DGHSNAEEDM
     EDDTSWRSEA TFQFTVERFS RLSESVLSPP CFVRNLPWKI MVMPRFYPDR PHQKSVGFFL
     QCNAESDSTS WSCHAQAVLK IINYRDDDKS FSRRISHLFF HEENDWGFSN FMAWSEVTDP
     EKGFIDDDKV TFEVFVQADA PHGVAWDSKK HTGYVGLKNQ GATCYMNSLL QTLFFTNQLR
     KAVYMMPTEG DDSSKSVPLA LQRVFYELQH SDKPVGTKKL TKSFGWETLD SFMQHDVQEL
     CRVLLDNVEN KMKGTCVEGT IPKLFRGKMV SYIQCKDVDY RSDRREDYYD IQLSIKGKKN
     IFESFVDYVA VEQLDGDNKY DAGEHGLQEA EKGVKFLTLP PVLHLQLMRF MYDPQTDQNI
     KINDRFEFPE QLPLDEFLQK TDPKDPANYI LHAVLVHSGD NHGGHYVVYL NPKGDGKWCK
     FDDDVVSRCT KEEAIEHNYG GHDDDLSVRH CTNAYMLVYI RESKLSEVLQ AVTDHDIPQQ
     LVERLQEEKR IEAQKRKERQ EAHLYMQVQI VAEDQFCGHQ GNDMYDEEKV RYTVFKVLKN
     SSLAEFVQSL SQTMGFPQDQ IRLWPMQARS NGTKRPAMLD NEADGNKTMI ELSDNENPWT
     IFLETVDPEL AASGATLPKF DKDHDVMLFL KMYDPKTRSL NYCGHIYTPI SCKIRDLLPV
     MCDRAGFIQD TSLILYEEVK PNLTERIQDY DVSLDKALDE LMDGDIIVFQ KDDPENDNSE
     LPTAKEYFRD LYHRVDVIFC DKTIPNDPGF VVTLSNRMNY FQVAKTVAQR LNTDPMLLQF
     FKSQGYRDGP GNPLRHNYEG TLRDLLQFFK PRQPKKLYYQ QLKMKITDFE NRRSFKCIWL
     NSQFREEEIT LYPDKHGCVR DLLEECKKAV ELGDKASGRL RLLEIVSYKI IGVHQEDELL
     ECLSPATSRT FRIEEIPLDQ VDIDKENEML ITVAHFHKEV FGTFGIPFLL RIHQGEHFRE
     VMKRIQSLLD IQEKEFEKFK FAIVMMGRHQ YINEDEYEVN LKDFEPQPGN MSHPRPWLGL
     DHFNKAPKRS RYTYLEKAIK IHN
//
ID   CGNL1_MOUSE             Reviewed;        1298 AA.
AC   Q6AW69; Q5U5U0; Q69ZB4; Q8BLZ5; Q8BZ26; Q9D2T3;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Cingulin-like protein 1;
DE   AltName: Full=Junction-associated coiled-coil protein;
GN   Name=Cgnl1; Synonyms=Jacop, Kiaa1749;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND DOMAIN.
RX   PubMed=15292197; DOI=10.1074/jbc.M402616200;
RA   Ohnishi H., Nakahara T., Furuse K., Sasaki H., Tsukita S., Furuse M.;
RT   "JACOP, a novel plaque protein localizing at the apical junctional
RT   complex with sequence similarity to cingulin.";
RL   J. Biol. Chem. 279:46014-46022(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-640 (ISOFORM 5), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-641 (ISOFORM 4).
RC   STRAIN=C57BL/6J; TISSUE=Aorta, Testis, Vagina, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 804-1298 (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 305-1298 (ISOFORM 3).
RC   TISSUE=Embryonic intestine;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205; SER-298; SER-299;
RP   SER-389 AND SER-392, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May be involved in anchoring the apical junctional
CC       complex, especially tight junctions, to actin-based cytoskeletons.
CC   -!- SUBUNIT: Homodimer or oligomer (Potential).
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction.
CC       Note=Localizes to the apical junction complex composed of tight
CC       and adherens junctions. In the liver and kidney, it is also found
CC       along non-junctional actin filament bundles in addition to the
CC       apical junction.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q6AW69-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6AW69-2; Sequence=VSP_029947;
CC       Name=3;
CC         IsoId=Q6AW69-3; Sequence=VSP_029948, VSP_029950;
CC       Name=4;
CC         IsoId=Q6AW69-4; Sequence=VSP_029948;
CC       Name=5;
CC         IsoId=Q6AW69-5; Sequence=VSP_029948, VSP_029949;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in the
CC       kidney and lung.
CC   -!- DOMAIN: The head region is responsible for both junction and actin
CC       filament-based distribution.
CC   -!- SIMILARITY: Belongs to the cingulin family.
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DR   EMBL; AB186125; BAD34967.1; -; mRNA.
DR   EMBL; AK018850; BAB31463.1; -; mRNA.
DR   EMBL; AK036871; BAC29612.1; -; mRNA.
DR   EMBL; AK040774; BAC30701.2; -; mRNA.
DR   EMBL; BC031499; AAH31499.1; -; mRNA.
DR   EMBL; BC039211; AAH39211.1; -; mRNA.
DR   EMBL; AK173252; BAD32530.1; -; mRNA.
DR   IPI; IPI00876281; -.
DR   IPI; IPI00877180; -.
DR   IPI; IPI00877235; -.
DR   IPI; IPI00877265; -.
DR   IPI; IPI00956893; -.
DR   RefSeq; NP_080875.3; NM_026599.4.
DR   UniGene; Mm.99961; -.
DR   HSSP; P13848; 1NO4.
DR   ProteinModelPortal; Q6AW69; -.
DR   SMR; Q6AW69; 1211-1252.
DR   STRING; Q6AW69; -.
DR   PhosphoSite; Q6AW69; -.
DR   PRIDE; Q6AW69; -.
DR   Ensembl; ENSMUST00000072899; ENSMUSP00000072672; ENSMUSG00000032232.
DR   Ensembl; ENSMUST00000122065; ENSMUSP00000112479; ENSMUSG00000032232.
DR   GeneID; 68178; -.
DR   KEGG; mmu:68178; -.
DR   UCSC; uc009qpc.1; mouse.
DR   CTD; 68178; -.
DR   MGI; MGI:1915428; Cgnl1.
DR   eggNOG; roNOG13074; -.
DR   GeneTree; ENSGT00530000063409; -.
DR   HOGENOM; HBG277893; -.
DR   HOVERGEN; HBG107670; -.
DR   InParanoid; Q6AW69; -.
DR   OrthoDB; EOG4Q84WW; -.
DR   NextBio; 326616; -.
DR   ArrayExpress; Q6AW69; -.
DR   Bgee; Q6AW69; -.
DR   CleanEx; MM_CGNL1; -.
DR   Genevestigator; Q6AW69; -.
DR   GO; GO:0016459; C:myosin complex; IEA:InterPro.
DR   GO; GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0003774; F:motor activity; IEA:InterPro.
DR   InterPro; IPR002928; Myosin_tail.
DR   Pfam; PF01576; Myosin_tail_1; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Coiled coil; Phosphoprotein;
KW   Tight junction.
FT   CHAIN         1   1298       Cingulin-like protein 1.
FT                                /FTId=PRO_0000312876.
FT   REGION        1    551       Head.
FT   REGION     1260   1298       Tail.
FT   COILED      605   1252       Potential.
FT   MOTIF        37     51       ZIM (By similarity).
FT   COMPBIAS    297    301       Poly-Ser.
FT   COMPBIAS   1265   1271       Poly-Asp.
FT   MOD_RES     205    205       Phosphothreonine.
FT   MOD_RES     284    284       Phosphoserine.
FT   MOD_RES     298    298       Phosphoserine.
FT   MOD_RES     299    299       Phosphoserine.
FT   MOD_RES     389    389       Phosphoserine.
FT   MOD_RES     392    392       Phosphoserine.
FT   VAR_SEQ       1   1184       Missing (in isoform 2).
FT                                /FTId=VSP_029947.
FT   VAR_SEQ     450    450       Missing (in isoform 3, isoform 4 and
FT                                isoform 5).
FT                                /FTId=VSP_029948.
FT   VAR_SEQ     633    635       Missing (in isoform 5).
FT                                /FTId=VSP_029949.
FT   VAR_SEQ     728    798       Missing (in isoform 3).
FT                                /FTId=VSP_029950.
FT   CONFLICT    464    464       K -> I (in Ref. 2; BAC29612).
FT   CONFLICT    529    529       S -> G (in Ref. 1; BAD34967).
FT   CONFLICT    902    902       Q -> R (in Ref. 4; BAD32530).
FT   CONFLICT    948    948       Q -> E (in Ref. 4; BAD32530).
SQ   SEQUENCE   1298 AA;  148231 MW;  535EDD1B752B3752 CRC64;
     MELYFGEYQH VQQEYGVHLR LASGDTPKPR NSQPSKAGSY GVSIRVQGID GHPYIVLNNT
     ERCLAGTPFP ENAPSFPSSV INNLSLHPSN GTVLKENTPE ELQLPENPYL QTSPLRGQKQ
     FSLHEGRNGV LERKDGPTKL PHVLNFQRHP ELLQPYDPEK NEVNAKKHHP PESPWLRNAT
     EDGTNCKKSR NCFPKSYGSQ PNSPTSEDLA KTNMTAIRLC SSVVIEDPQK QTSVCVNVQR
     CAKEGVGEET LSPRRKSPTA PSPQAYSETK KNRPDVLPFR RQDSAGPILD GARSRRSSSS
     STTPTSATSL YKFLLDDQEC AIHADSVNRH ENRRYIPFLP GTGRDIDTCS IPGVDQLIEK
     FDQKPGLQRR GRSGKRNRIN PDDRKRSRSV DSAFPFGLQG NTEYLTEFSR NLGKSSEHLL
     RPSQVFPQRS VAQEHRGKHS PSSPPAKLQG GAQGAHPKPP LQNKDGKVLN KGRQESTGAC
     APSLPAPNKK EEEIKIATAT LMLQNRAVAA TSDSGAKKIS VKTFPSDSST QATPDLLKGQ
     QELTQQTNEE TAKQILYNYL KEGGTDNEDA TKRKVNLVFE KIQTLKSRAA GSAQGSNQAP
     NSPSEGNSLL DQKNKLILEV SELQQQLQLE MKNQQNIKEE RERMREDLEE LRVRHQSQVE
     ETATLQRRLE ESEGELRKSL EELFQVKMER EQHQTEIRDL QDQLSEMHDE LDSTKRSEDR
     EKGALIEELL QAKQDLQDLL IAKEEQEDLL RKRERELTAL KGALKEEVSS HDQEMDKLKE
     QYDAELQAFR ESVEEATKNV EVLASRSNSS EQSQAEADLR EKVLKEENEK LQGRIAELER
     RAAQLQRQME DVKGDEAQAK ETLRKCESEV QQLEEALVHA RKEEKEATCA RRALEKELEQ
     AQRELSQVSQ EQKELLEKLR DEAEQKEQLR KLKNEMESER WHLDKTIQKL QKEMADIAEA
     SRTSSLELQK QLGEYKEKNR RELAEMQTQL KEKCLEVEKA RLAASKMQDE LRLKEEELQD
     YQRAEEEALT KRQLLEQSLK DLEYELEAKS HLKDDRSRLI KQMEDKVSQL EIELEEERTN
     ADLLSERITW SREQMEQMRS ELLQEKAAKQ DLECDKISLE RQNKDLKSRI IHLEGSYRSS
     KEGLVVQMEA RIAELEDRLE NEERDRANLQ LSNRRLERKV KELVMQVDDE HLSLTDQKDQ
     LSLRLKAMKR QVEEAEEEID RLESSKKKLQ RELEEQMGVN EQLQGQLNSL KKGLRLKTLS
     SKVLDDSDDD DLSSDAGSLY EAPLSYAFPK DSTIASQI
//
ID   Q6AXG6_MOUSE            Unreviewed;      1202 AA.
AC   Q6AXG6;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   08-MAR-2011, entry version 47.
DE   SubName: Full=Kank1 protein;
GN   Name=Kank1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; BC079563; AAH79563.1; -; mRNA.
DR   IPI; IPI00460667; -.
DR   RefSeq; NP_852069.4; NM_181404.5.
DR   UniGene; Mm.260722; -.
DR   ProteinModelPortal; Q6AXG6; -.
DR   SMR; Q6AXG6; 1005-1174.
DR   Ensembl; ENSMUST00000049400; ENSMUSP00000042177; ENSMUSG00000032702.
DR   GeneID; 107351; -.
DR   KEGG; mmu:107351; -.
DR   UCSC; uc008hbg.1; mouse.
DR   CTD; 107351; -.
DR   MGI; MGI:2147707; Kank1.
DR   eggNOG; roNOG05941; -.
DR   HOGENOM; HBG446458; -.
DR   HOVERGEN; HBG050511; -.
DR   InParanoid; Q6AXG6; -.
DR   ArrayExpress; Q6AXG6; -.
DR   Bgee; Q6AXG6; -.
DR   Genevestigator; Q6AXG6; -.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 3.
DR   SMART; SM00248; ANK; 5.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
PE   2: Evidence at transcript level;
KW   ANK repeat; Repeat.
SQ   SEQUENCE   1202 AA;  130796 MW;  85A877DC7A9487B7 CRC64;
     METRRRLEQE RVTMQMAPGD FRRPRLASFG GMGSTSSLPS FVGSANHSSV IHQLQNGYQG
     NGDYNSYVPA APTTSSMGSS VRHSPLSSGI STPVTNVSPM HLQHIREQMA IALKRLKELE
     EQVRTIPVLQ VKISVLQEEK RQLASQLKSQ RASSQNEACG VRKRSYSAGN ASQLELLARA
     RRGGGELYID YEEEEMESVE QSTQRIQEFR QLTADMQALE RKIQDSSCEV ASELRENGQC
     PSRECKSVAV GSDENMNDVV VYHRDLRPCK DTAVGTVTET RNVGISVTEA MLGVITEADK
     EIELQQQTIE ALKEKIYRLE VQLKETTHDR EMTKLKQELQ AAGSRKKVDK ATMAQPLVFS
     KLVEALVPTR DQMVGSHVDT RESCVGTSVQ TSSVGTSCHP DCKNQVVGSE LPMNWWVVKE
     RVAMHDQCVG RSVETCDRSV GVEVSVCETG SNTEASGSDL TLLKTNLNLK DVRSIGCGDC
     SVDVIVCFPK ECTSRSMNTE AVGQEEAAVM AVPHTTDQHT STNLERVDQC TNTEAATLVE
     SCTNTLLSTM DKQTSTQTVE MRTVAIGEGR VRDINPSTKT RSVGVGTVLS GNSEFDRPCA
     VKTKESGVGQ INIQDNYLVG LKMRTIACGP PQLTVGLMGS RRSVGVGNEP VGELPEESPQ
     PRVASGMVTG LDHYIERVQR LLAEQQTLLA ENYSELAEAF GEPHSQIGSL NSQLISTLSS
     INSVMKSAST EELRNSDFQK ASLGKTTGNH LEYTCKCGGL RSGGLLNVQP SQPEVEAETA
     EGKHSRGHEQ FPMQGSTLPP VNLTDDQIAT GLYVCPNNEN TLKSIMKKSD GNKDSNGAKK
     NLQFIGINGG YETTSSDESS SDGSSSSESD DECDTIGYPP EEEEEEEEKD HDTRGMAEGH
     HAVNIEGFKS ARVEDEVQVP ECEPEKEEIR ERYELSEKML SACNLLKYNI KDPKALASKD
     MRICLNTLQH DWFRVSSQKS AVPAMVGDYI AAFEAVSPDV LRYIINMADG NGNTALHYSV
     SHSNFQIVKL LLDADVCNVD HQNKAGYTPI MLAALAAVEA EKDMQVVEEL FSCGDVNAKA
     SQAGQTALML AVSHGRIDMV KGLLACGADV NIQDDEGSTA LMCASEHGHV EIVKLLLAQP
     GCNGHLEDND GSTALSIALE AGHKDIAVLL YAHLNFSKAQ SPSTPRLGRK TSPGPTHRGS
     FD
//
ID   Q6BCW5_MOUSE            Unreviewed;       204 AA.
AC   Q6BCW5;
DT   13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2004, sequence version 1.
DT   30-NOV-2010, entry version 46.
DE   SubName: Full=Rim1delta83-105;
DE   Flags: Fragment;
GN   Name=Rims1; Synonyms=rim1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c;
RX   PubMed=15330860; DOI=10.1111/j.1365-2443.2004.00767.x;
RA   Fukuda M.;
RT   "Alternative splicing in the first alpha-helical region of the Rab-
RT   binding domain of Rim regulates Rab3A binding activity: is Rim a Rab3
RT   effector protein during evolution?";
RL   Genes Cells 9:831-842(2004).
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DR   EMBL; AB162897; BAD32693.1; -; Genomic_DNA.
DR   IPI; IPI00462052; -.
DR   UniGene; Mm.380549; -.
DR   UniGene; Mm.461684; -.
DR   UniGene; Mm.60061; -.
DR   ProteinModelPortal; Q6BCW5; -.
DR   STRING; Q6BCW5; -.
DR   PRIDE; Q6BCW5; -.
DR   eggNOG; roNOG07027; -.
DR   Genevestigator; Q6BCW5; -.
DR   GO; GO:0017137; F:Rab GTPase binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   InterPro; IPR010911; Rab-bd_domain.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS50916; RABBD; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   4: Predicted;
KW   Metal-binding; Zinc.
FT   NON_TER     204    204
SQ   SEQUENCE   204 AA;  22803 MW;  ABF1B8132F21E58B CRC64;
     MSSAVGPRGP RPPTVPPPMQ ELPDLSHLTE EERNIIMAVM DRQKEEEEKE EAMLKCVVRD
     MAKPAACKTP RNAESQPHQP PLRLHQQFES YKEQVRKIGE EARRYQGEHK DDAPTCGICH
     KTKFADGCGH LCSYCRTKFC ARCGGRVSLR SNNEDKVVMW VCNLCRKQQE ILTKSGAWFF
     GSGPQQPSQD GTLSDTATGA GSEV
//
ID   CI072_MOUSE             Reviewed;         420 AA.
AC   Q6DFW0; A6PWW3;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 35.
DE   RecName: Full=Uncharacterized protein C9orf72 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and Czech II; TISSUE=Head;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; AL831776; CAO77739.1; -; Genomic_DNA.
DR   EMBL; BC076612; AAH76612.1; -; mRNA.
DR   IPI; IPI00857476; -.
DR   UniGene; Mm.331544; -.
DR   Ensembl; ENSMUST00000084724; ENSMUSP00000081775; ENSMUSG00000028300.
DR   Ensembl; ENSMUST00000108127; ENSMUSP00000103762; ENSMUSG00000028300.
DR   UCSC; uc008sgw.1; mouse.
DR   MGI; MGI:1920455; 3110043O21Rik.
DR   GeneTree; ENSGT00390000005644; -.
DR   HOVERGEN; HBG060354; -.
DR   InParanoid; Q6DFW0; -.
DR   OrthoDB; EOG42V8G6; -.
DR   ArrayExpress; Q6DFW0; -.
DR   Bgee; Q6DFW0; -.
DR   CleanEx; MM_3110043O21RIK; -.
DR   Genevestigator; Q6DFW0; -.
DR   GermOnline; ENSMUSG00000028300; Mus musculus.
PE   2: Evidence at transcript level;
FT   CHAIN         1    420       Uncharacterized protein C9orf72 homolog.
FT                                /FTId=PRO_0000089712.
SQ   SEQUENCE   420 AA;  47314 MW;  F366D54199127E0C CRC64;
     MSTICPPPSP AVAKTEIALS GESPLLAATF AYWDNILGPR VRHIWAPKTD QVLLSDGEIT
     FLANHTLNGE ILRNAESGAI DVKFFVLSEK GVIIVSLIFD GNWNGDRSTY GLSIILPQTE
     LSFYLPLHRV CVDRLTHIIR KGRIWMHKER QENVQKIVLE GTERMEDQGQ SIIPMLTGEV
     IPVMELLASM KSHSVPEDID IADTVLNDDD IGDSCHEGFL LNAISSHLQT CGCSVVVGSS
     AEKVNKIVRT LCLFLTPAER KCSRLCEAES SFKYESGLFV QGLLKDATGS FVLPFRQVMY
     APYPTTHIDV DVNTVKQMPP CHEHIYNQRR YMRSELTAFW RATSEEDMAQ DTIIYTDESF
     TPDLNIFQDV LHRDTLVKAF LDQVFHLKPG LSLRSTFLAQ FLLILHRKAL TLIKYIEDDT
//
ID   NOP58_MOUSE             Reviewed;         536 AA.
AC   Q6DFW4; O70396; Q3UYX9; Q3UZA3; Q8C8Y7;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Nucleolar protein 58;
DE   AltName: Full=MSSP;
DE   AltName: Full=Nucleolar protein 5;
DE   AltName: Full=SIK-similar protein;
GN   Name=Nop58; Synonyms=Nol5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C3H/HeJ;
RA   Zierke M., Martin M.U.;
RT   "cDNA for mouse SIK similar protein (MSSP).";
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Forelimb, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509 AND SER-521, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509 AND SER-521, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509 AND SER-521, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-509, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Required for 60S ribosomal subunit biogenesis (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with NOLC1/Nopp140. Component of box C/D small
CC       nucleolar ribonucleoprotein (snoRNP) particles (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity).
CC   -!- PTM: Sumoylation is essential for high-affinity binding to snoRNAs
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the NOP5/NOP56 family.
CC   -!- SIMILARITY: Contains 1 Nop domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC08435.1; Type=Frameshift; Positions=12;
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DR   EMBL; AF053232; AAC08435.1; ALT_FRAME; mRNA.
DR   EMBL; AK044216; BAC31822.1; -; mRNA.
DR   EMBL; AK133959; BAE21954.1; -; mRNA.
DR   EMBL; AK134286; BAE22082.1; -; mRNA.
DR   EMBL; BC076604; AAH76604.1; -; mRNA.
DR   EMBL; BC085135; AAH85135.1; -; mRNA.
DR   IPI; IPI00463468; -.
DR   RefSeq; NP_061356.2; NM_018868.2.
DR   UniGene; Mm.220367; -.
DR   ProteinModelPortal; Q6DFW4; -.
DR   SMR; Q6DFW4; 2-401.
DR   STRING; Q6DFW4; -.
DR   PhosphoSite; Q6DFW4; -.
DR   PRIDE; Q6DFW4; -.
DR   Ensembl; ENSMUST00000027174; ENSMUSP00000027174; ENSMUSG00000026020.
DR   GeneID; 55989; -.
DR   KEGG; mmu:55989; -.
DR   NMPDR; fig|10090.3.peg.407; -.
DR   UCSC; uc007bdy.1; mouse.
DR   CTD; 55989; -.
DR   MGI; MGI:1933184; Nop58.
DR   eggNOG; roNOG13018; -.
DR   GeneTree; ENSGT00550000074998; -.
DR   HOGENOM; HBG611715; -.
DR   InParanoid; Q6DFW4; -.
DR   OMA; DAHEQLA; -.
DR   OrthoDB; EOG451DQQ; -.
DR   PhylomeDB; Q6DFW4; -.
DR   NextBio; 311710; -.
DR   ArrayExpress; Q6DFW4; -.
DR   Bgee; Q6DFW4; -.
DR   CleanEx; MM_NOL5; -.
DR   Genevestigator; Q6DFW4; -.
DR   GO; GO:0005730; C:nucleolus; IC:MGI.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR012974; NOP5_N.
DR   InterPro; IPR012976; NOSIC.
DR   InterPro; IPR002687; SnoRNA-bd_dom.
DR   Pfam; PF01798; Nop; 1.
DR   Pfam; PF08156; NOP5NT; 1.
DR   Pfam; PF08060; NOSIC; 1.
DR   SMART; SM00931; NOSIC; 1.
PE   1: Evidence at protein level;
KW   Isopeptide bond; Nucleus; Phosphoprotein; Ribosome biogenesis;
KW   Ubl conjugation.
FT   CHAIN         1    536       Nucleolar protein 58.
FT                                /FTId=PRO_0000287350.
FT   DOMAIN      253    401       Nop.
FT   COMPBIAS    441    532       Lys-rich.
FT   MOD_RES     109    109       Phosphoserine (By similarity).
FT   MOD_RES     351    351       Phosphoserine (By similarity).
FT   MOD_RES     490    490       Phosphothreonine (By similarity).
FT   MOD_RES     509    509       Phosphoserine.
FT   MOD_RES     521    521       Phosphoserine.
FT   CROSSLNK    467    467       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    504    504       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CONFLICT     78     78       K -> R (in Ref. 1; AAC08435).
FT   CONFLICT    385    385       I -> V (in Ref. 2; BAC31822).
FT   CONFLICT    499    499       K -> P (in Ref. 2; BAE22082).
SQ   SEQUENCE   536 AA;  60343 MW;  D5FE1819F092D701 CRC64;
     MLVLFETSVG YAIFKVLNEK KLQEVDSLWK EFETPEKANK IVKLKHFEKF QDTAEALAAF
     TALMEGKINK QLKKVLKKIV KEAHEPLAVA DAKLGGVIKE KLNLSCIHSP VVNELMRGIR
     SQMDGLIPGV EPREMAAMCL GLAHSLSRYR LKFSADKVDT MIVQAISLLD DLDKELNNYI
     MRCREWYGWH FPELGKIISD NLTYCKCLQK VGDRKNYASA SLSEFLSEEV EAEVKAAAEI
     SMGTEVSEED ICNILHLCTQ VIEISEYRTQ LYEYLQNRMM AIAPNVTVMV GELVGARLIA
     HAGSLLNLAK HAASTVQILG AEKALFRALK SRRDTPKYGL IYHASLVGQS SPKHKGKISR
     MLAAKTVLAI RYDAFGEDSS SAMGIENRAK LEARLRILED RGIRKISGTG KALAKAEKYE
     HKSEVKTYDP SGDSTLPTCS KKRKIEEVDK EDEITEKKAK KAKIKIKAEV EEEMEEEEAE
     EEQVVEEEPT VKKKKKKDKK KHIKEEPLSE EEPCTSTAVP SPEKKKKKKK KKDAED
//
ID   Q6DFX1_MOUSE            Unreviewed;       754 AA.
AC   Q6DFX1;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   SubName: Full=HEG homolog 1 (Zebrafish);
GN   Name=Heg1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC076596; AAH76596.1; -; mRNA.
DR   IPI; IPI00406450; -.
DR   RefSeq; NP_780465.4; NM_175256.5.
DR   UniGene; Mm.245741; -.
DR   UniGene; Mm.37138; -.
DR   ProteinModelPortal; Q6DFX1; -.
DR   SMR; Q6DFX1; 357-432.
DR   PhosphoSite; Q6DFX1; -.
DR   Ensembl; ENSMUST00000038392; ENSMUSP00000039438; ENSMUSG00000075254.
DR   Ensembl; ENSMUST00000126532; ENSMUSP00000119790; ENSMUSG00000075254.
DR   Ensembl; ENSMUST00000152782; ENSMUSP00000123686; ENSMUSG00000075254.
DR   GeneID; 77446; -.
DR   KEGG; mmu:77446; -.
DR   CTD; 77446; -.
DR   MGI; MGI:1924696; Heg1.
DR   eggNOG; roNOG12238; -.
DR   HOGENOM; HBG280363; -.
DR   InParanoid; Q6DFX1; -.
DR   OMA; NTTAENH; -.
DR   OrthoDB; EOG4FR0SB; -.
DR   PhylomeDB; Q6DFX1; -.
DR   NextBio; 346948; -.
DR   ArrayExpress; Q6DFX1; -.
DR   Bgee; Q6DFX1; -.
DR   Genevestigator; Q6DFX1; -.
DR   GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0003209; P:cardiac atrium morphogenesis; IMP:MGI.
DR   GO; GO:0045216; P:cell-cell junction organization; IMP:MGI.
DR   GO; GO:0001886; P:endothelial cell morphogenesis; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR   GO; GO:0030324; P:lung development; IMP:MGI.
DR   GO; GO:0003017; P:lymph circulation; IMP:MGI.
DR   GO; GO:0001945; P:lymph vessel development; IMP:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IGI:MGI.
DR   GO; GO:0060039; P:pericardium development; IGI:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0050878; P:regulation of body fluid levels; IMP:MGI.
DR   GO; GO:0001570; P:vasculogenesis; IGI:MGI.
DR   GO; GO:0048845; P:venous blood vessel morphogenesis; IGI:MGI.
DR   GO; GO:0003281; P:ventricular septum development; IMP:MGI.
DR   InterPro; IPR006209; EGF.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR001881; EGF_Ca-bd.
DR   InterPro; IPR013091; EGF_Ca-bd_2.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00179; EGF_CA; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 1.
PE   2: Evidence at transcript level;
KW   EGF-like domain; Repeat.
SQ   SEQUENCE   754 AA;  81066 MW;  F90FEE2CED74F2A0 CRC64;
     MSSDDDEPAQ SSTESPVLHT SNLPTYTSTV NMPNTLVLDT GTKPVEDPSD SRVPSTQPSP
     SQPQPFSSAL PSTRSPGSTS ETTTSSPSPS PISLLVSTLA PYSVSQTTFP HPSSTLVPHR
     PREPRVTSVQ MSTAISAIAL IPSNQTANPK NQSTPQQEKP ITEAKSPSLV SPPTDSTKAV
     TVSLPPGAPW SPALTGFSTG PALPATSTSL AQMSPALTSA MPQTTHSPVT SPSTLSHVEA
     LTSGAVVVHT TPKKPHLPTN PEILVPHIST EGAITTEGNR EHTDPTTQPI PLTTSTTSAG
     ERTTELGRAE ESSPSHFLTP SSPQTTDVST AEMLTSRYIT FAAQSTSQSP TALPPLTPVN
     SCTVNPCLHD GKCIVDLTGR GYRCVCPPAW QGENCSVDVN ECLSSPCPPL ATCNNTQGSF
     TCRCPVGYQL EKGICNLVRT FVTEFKLKKT FLNTTAENHS NTQELENEIA QTLNVCFSTL
     PGYIRTTAHV SREPSTVFIS LKTTFALASN VTLFDLADRI QKYVNSCRSS AEVCQLLGSQ
     RRVFRAGSLC KRKSPECDKE TSICTDLDGV ALCQCKSGYF QFNKMDHSCR ACEDGYRLEN
     ETCMSCPFGL GGLNCGNPYQ LITVVIAAAG GGLLLILGVA LIVTCCRKSK NDISKLIFKS
     GDFQMSPYTD VPKNPRSQEW GREAIEMHEN GSTKNLLQMT DVYYSPTNVR NPELERNGLY
     PAYTGLPGSR HSCIFPGQYN PSFISDESRR RDYF
//
ID   FBX27_MOUSE             Reviewed;         280 AA.
AC   Q6DIA9; Q3TYP0; Q8BKF7;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=F-box only protein 27;
GN   Name=Fbxo27;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, Eye, and Inner ear;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=18203720; DOI=10.1074/jbc.M709508200;
RA   Glenn K.A., Nelson R.F., Wen H.M., Mallinger A.J., Paulson H.L.;
RT   "Diversity in tissue expression, substrate binding, and SCF complex
RT   formation for a lectin family of ubiquitin ligases.";
RL   J. Biol. Chem. 283:12717-12729(2008).
CC   -!- FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-
CC       box protein)-type E3 ubiquitin ligase complex (By similarity).
CC       Able to recognize and bind complex-type oligosaccharides (By
CC       similarity).
CC   -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex.
CC       Interacts with SKP1 and CUL1 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6DIA9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6DIA9-2; Sequence=VSP_013054;
CC         Note=May be due to a competing acceptor splice site;
CC   -!- TISSUE SPECIFICITY: Detected in brain, heart and muscle.
CC   -!- SIMILARITY: Contains 1 F-box domain.
CC   -!- SIMILARITY: Contains 1 FBA (F-box associated) domain.
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DR   EMBL; AK053292; BAC35334.1; -; mRNA.
DR   EMBL; AK140275; BAE24311.1; -; mRNA.
DR   EMBL; AK158463; BAE34522.1; -; mRNA.
DR   EMBL; BC075656; AAH75656.1; -; mRNA.
DR   IPI; IPI00411105; -.
DR   IPI; IPI00553412; -.
DR   RefSeq; NP_001157174.1; NM_001163702.1.
DR   RefSeq; NP_997121.1; NM_207238.3.
DR   UniGene; Mm.116116; -.
DR   ProteinModelPortal; Q6DIA9; -.
DR   SMR; Q6DIA9; 21-276.
DR   STRING; Q6DIA9; -.
DR   PRIDE; Q6DIA9; -.
DR   Ensembl; ENSMUST00000039998; ENSMUSP00000038432; ENSMUSG00000037463.
DR   Ensembl; ENSMUST00000108281; ENSMUSP00000103916; ENSMUSG00000037463.
DR   Ensembl; ENSMUST00000108282; ENSMUSP00000103917; ENSMUSG00000037463.
DR   GeneID; 233040; -.
DR   KEGG; mmu:233040; -.
DR   NMPDR; fig|10090.3.peg.16047; -.
DR   UCSC; uc009fzj.1; mouse.
DR   UCSC; uc009fzk.1; mouse.
DR   CTD; 233040; -.
DR   MGI; MGI:2685007; Fbxo27.
DR   GeneTree; ENSGT00390000003865; -.
DR   HOGENOM; HBG716440; -.
DR   HOVERGEN; HBG003593; -.
DR   InParanoid; Q6DIA9; -.
DR   OMA; IEICVSD; -.
DR   OrthoDB; EOG4W9J4K; -.
DR   PhylomeDB; Q6DIA9; -.
DR   NextBio; 381486; -.
DR   ArrayExpress; Q6DIA9; -.
DR   Bgee; Q6DIA9; -.
DR   CleanEx; MM_FBXO27; -.
DR   Genevestigator; Q6DIA9; -.
DR   GermOnline; ENSMUSG00000037463; Mus musculus.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0001948; F:glycoprotein binding; ISS:UniProtKB.
DR   GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR   InterPro; IPR007397; F-box-assoc_dom.
DR   InterPro; IPR001810; F-box_dom_cyclin-like.
DR   InterPro; IPR022364; F-box_dom_Skp2-like.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   Pfam; PF00646; F-box; 1.
DR   Pfam; PF04300; FBA; 1.
DR   SMART; SM00256; FBOX; 1.
DR   SUPFAM; SSF81383; F-box_dom_Skp2-like; 1.
DR   SUPFAM; SSF49785; Gal_bind_like; 1.
DR   PROSITE; PS51114; FBA; 1.
DR   PROSITE; PS50181; FBOX; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Ubl conjugation pathway.
FT   CHAIN         1    280       F-box only protein 27.
FT                                /FTId=PRO_0000119916.
FT   DOMAIN       20     67       F-box.
FT   DOMAIN      101    277       FBA.
FT   VAR_SEQ     119    119       Missing (in isoform 2).
FT                                /FTId=VSP_013054.
SQ   SEQUENCE   280 AA;  31633 MW;  36FF90947DFAE86B CRC64;
     MGAWISRTRV PTPEPDPQEV LDLSRLPPEL LLLVLSHVPP RTLLMHCRRV CRAWRALVDG
     QALWLLLLAR DHSAAGRALL TLARRCLPPA HEDTPCPLGQ FCALRPLGRN LISNPCGQEG
     LRKWMVRHGG DGWVVEKNRK PVPGAPSQTC FVTSFSWCRK KQVVDLVEKG LWPELLDSGG
     VEIAVSDWWG ARHDSGCKYR LFVTLLDAHQ NVIDKFSAVP DPIEQWNNDI YLQVTHVFSG
     IRRGIRFVSF EHWGQDTQFW AGHYGARVTN SSVIIRVCQS
//
ID   CT112_MOUSE             Reviewed;         494 AA.
AC   Q6DIB4;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 40.
DE   RecName: Full=Uncharacterized protein C20orf112 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; BC075648; AAH75648.1; -; mRNA.
DR   IPI; IPI00453784; -.
DR   UniGene; Mm.50600; -.
DR   PhosphoSite; Q6DIB4; -.
DR   PRIDE; Q6DIB4; -.
DR   Ensembl; ENSMUST00000035346; ENSMUSP00000036571; ENSMUSG00000061411.
DR   UCSC; uc008nhu.1; mouse.
DR   MGI; MGI:1918765; 8430427H17Rik.
DR   GeneTree; ENSGT00390000017363; -.
DR   HOVERGEN; HBG031438; -.
DR   InParanoid; Q6DIB4; -.
DR   OrthoDB; EOG4J117Q; -.
DR   NextBio; 398824; -.
DR   ArrayExpress; Q6DIB4; -.
DR   Bgee; Q6DIB4; -.
DR   CleanEx; MM_8430427H17RIK; -.
DR   Genevestigator; Q6DIB4; -.
DR   GermOnline; ENSMUSG00000061411; Mus musculus.
PE   2: Evidence at transcript level;
KW   Phosphoprotein.
FT   CHAIN         1    494       Uncharacterized protein C20orf112
FT                                homolog.
FT                                /FTId=PRO_0000079457.
FT   COMPBIAS    220    228       Poly-Asp.
FT   MOD_RES     189    189       Phosphoserine (By similarity).
SQ   SEQUENCE   494 AA;  53912 MW;  4B8C0AEF7235E61F CRC64;
     MHFNSSGPEP KENEPPSPLV SGIIDYNMPL TSTYLKQMKL RVMNSQEQDE TSVSSEDFDM
     NDSAWMSADP HLASSLSPSQ EERMRSPQNL HSQEDDDSSS ESGSGNGSST LNPSTSSSTQ
     GDPAFPEMNG NGAAAPMDFT ATAEDQPINL CEKLPPGTAL GTPSYPSDGC GTDGLRSRVK
     YGVKNTPESP PYSSGSYDSI KTEVSGCPED LTVGRAPAAD DDDDDHDDHE DNDKMNDSEG
     MDPERLKAFN MFVRLFVDEN LDRMVPISKQ PKEKIQAIIE SCSRQFPEFQ ERARKRIRTY
     LKSCRRMKKN GMEMTRPTPP HLTSAMAENI LAAACESETR KAAKRMRLEI YQSSQEEPIA
     LDKQHSRDST AITHSTYSLP ASAYSQDPVY VNGGLNYSYR GYGSLSSNLQ PSASLQTGNH
     SNGPTDLSMK GGASTPTPPT PTPSSNSTSR TMPTAQLSPT EISAVRQLIA GYRESAAFLL
     RSADELENLI LQQN
//
ID   MEG10_MOUSE             Reviewed;        1147 AA.
AC   Q6DIB5; Q3TLU3; Q3UG73;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Multiple epidermal growth factor-like domains protein 10;
DE            Short=Multiple EGF-like domains protein 10;
DE   Flags: Precursor;
GN   Name=Megf10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=17205124; DOI=10.1371/journal.pone.0000120;
RA   Hamon Y., Trompier D., Ma Z., Venegas V., Pophillat M., Mignotte V.,
RA   Zhou Z., Chimini G.;
RT   "Cooperation between engulfment receptors: the case of ABCA1 and
RT   MEGF10.";
RL   PLoS ONE 1:E120-E120(2006).
RN   [4]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=17643423; DOI=10.1016/j.yexcr.2007.06.015;
RA   Suzuki E., Nakayama M.;
RT   "MEGF10 is a mammalian ortholog of CED-1 that interacts with clathrin
RT   assembly protein complex 2 medium chain and induces large vacuole
RT   formation.";
RL   Exp. Cell Res. 313:3729-3742(2007).
CC   -!- FUNCTION: Involved in phagocytosis by macrophages of apoptotic
CC       cells. Cooperates with ABCA1 during engulfment. Destabilizes the
CC       oligomeric assemblies of the ABCA1 transporter. Plays a role in
CC       cell adhesion. Inhibits cell motility and cell proliferation in
CC       vitro. Promotes formation of large intracellular vacuoles (By
CC       similarity).
CC   -!- SUBUNIT: Homopolymer (Probable). Interacts with GULP1 and ABCA1.
CC       Interacts with AP2M1. Does not interact with MEGF11 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Basolateral cell membrane; Single-pass type I membrane
CC       protein (By similarity). Cell projection, phagocytic cup (By
CC       similarity). Note=Forms an irregular, mosaic-like adhesion pattern
CC       in region of the cell surface that becomes firmely fixed to the
CC       substrat. Expressed at the cell surface in clusters around cell
CC       corpses during engulfment. During the engulfment of apoptotic
CC       thymocytes, recruited at the bottom of the forming phagocytic cup.
CC       Colocalizes with ABCA1 in absence of any phagocytic challenge.
CC       Does not localize within lamellipodia. Does not localize with
CC       MEGF11 (By similarity). Enriched at the sites of contact with
CC       apoptotic thymocyte cells.
CC   -!- TISSUE SPECIFICITY: Expressed in cerebellum (at protein level).
CC       Expressed in kidney, stellate cells of the cerebellum and
CC       macrophage cell lines.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryo at 15 dpc (at protein
CC       level). Expressed in embryo at 8, 10, 11, 13, 14 and 15 dpc.
CC   -!- DOMAIN: The EMI and EGF-like domains work in concert to promote
CC       self-assembly.
CC   -!- PTM: Phosphorylated on tyrosine residues (By similarity).
CC   -!- PTM: Ubiquinated; mono- and polyubiquitinated forms are detected
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the MEGF family.
CC   -!- SIMILARITY: Contains 15 EGF-like domains.
CC   -!- SIMILARITY: Contains 1 EMI domain.
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DR   EMBL; AK147238; BAE27788.1; -; mRNA.
DR   EMBL; AK148084; BAE28336.1; -; mRNA.
DR   EMBL; AK166316; BAE38699.1; -; mRNA.
DR   EMBL; BC075647; AAH75647.1; -; mRNA.
DR   IPI; IPI00453778; -.
DR   RefSeq; NP_001001979.1; NM_001001979.2.
DR   UniGene; Mm.297863; -.
DR   HSSP; P01132; 1EGF.
DR   ProteinModelPortal; Q6DIB5; -.
DR   SMR; Q6DIB5; 90-353, 572-832.
DR   STRING; Q6DIB5; -.
DR   PhosphoSite; Q6DIB5; -.
DR   PRIDE; Q6DIB5; -.
DR   Ensembl; ENSMUST00000075770; ENSMUSP00000075174; ENSMUSG00000024593.
DR   Ensembl; ENSMUST00000115370; ENSMUSP00000111027; ENSMUSG00000024593.
DR   GeneID; 70417; -.
DR   KEGG; mmu:70417; -.
DR   UCSC; uc008eyz.1; mouse.
DR   CTD; 70417; -.
DR   MGI; MGI:2685177; Megf10.
DR   eggNOG; roNOG14574; -.
DR   GeneTree; ENSGT00550000074173; -.
DR   HOGENOM; HBG444481; -.
DR   HOVERGEN; HBG108333; -.
DR   InParanoid; Q6DIB5; -.
DR   OMA; NCSSACD; -.
DR   OrthoDB; EOG42JNQJ; -.
DR   NextBio; 331567; -.
DR   ArrayExpress; Q6DIB5; -.
DR   Bgee; Q6DIB5; -.
DR   CleanEx; MM_MEGF10; -.
DR   Genevestigator; Q6DIB5; -.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR002049; EGF_laminin.
DR   InterPro; IPR011489; EMI_domain.
DR   Pfam; PF07974; EGF_2; 2.
DR   Pfam; PF00053; Laminin_EGF; 5.
DR   SMART; SM00181; EGF; 12.
DR   SMART; SM00180; EGF_Lam; 5.
DR   PROSITE; PS00022; EGF_1; 17.
DR   PROSITE; PS01186; EGF_2; 17.
DR   PROSITE; PS50026; EGF_3; 15.
DR   PROSITE; PS51041; EMI; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion; Cell membrane; Cell projection; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Phagocytosis; Repeat; Signal;
KW   Transmembrane; Transmembrane helix; Ubl conjugation.
FT   SIGNAL        1     25       Potential.
FT   CHAIN        26   1147       Multiple epidermal growth factor-like
FT                                domains protein 10.
FT                                /FTId=PRO_0000309733.
FT   TOPO_DOM     26    857       Extracellular (Potential).
FT   TRANSMEM    858    878       Helical; (Potential).
FT   TOPO_DOM    879   1147       Cytoplasmic (Potential).
FT   DOMAIN       30    107       EMI.
FT   DOMAIN      101    136       EGF-like 1.
FT   DOMAIN      144    179       EGF-like 2.
FT   DOMAIN      187    222       EGF-like 3.
FT   DOMAIN      230    265       EGF-like 4.
FT   DOMAIN      278    308       EGF-like 5.
FT   DOMAIN      316    351       EGF-like 6.
FT   DOMAIN      405    440       EGF-like 7.
FT   DOMAIN      453    483       EGF-like 8.
FT   DOMAIN      491    526       EGF-like 9.
FT   DOMAIN      539    569       EGF-like 10.
FT   DOMAIN      577    612       EGF-like 11.
FT   DOMAIN      665    700       EGF-like 12.
FT   DOMAIN      713    743       EGF-like 13.
FT   DOMAIN      751    786       EGF-like 14.
FT   DOMAIN      799    829       EGF-like 15.
FT   REGION        1    857       Necessary for interaction with AP2M1,
FT                                self-assembly and formation of the
FT                                irregular, mosaic-like adhesion pattern
FT                                (By similarity).
FT   REGION      945   1147       Necessary for formation of large
FT                                intracellular vacuoles (By similarity).
FT   COMPBIAS   1119   1146       Ser-rich.
FT   CARBOHYD    134    134       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    496    496       N-linked (GlcNAc...) (Potential).
FT   DISULFID     34     95       Potential.
FT   DISULFID     60     69       Potential.
FT   DISULFID     94    105       Potential.
FT   DISULFID    109    124       By similarity.
FT   DISULFID    126    135       By similarity.
FT   DISULFID    148    160       By similarity.
FT   DISULFID    154    167       By similarity.
FT   DISULFID    169    178       By similarity.
FT   DISULFID    191    203       By similarity.
FT   DISULFID    197    210       By similarity.
FT   DISULFID    212    221       By similarity.
FT   DISULFID    234    246       By similarity.
FT   DISULFID    240    253       By similarity.
FT   DISULFID    255    264       By similarity.
FT   DISULFID    281    289       By similarity.
FT   DISULFID    283    296       By similarity.
FT   DISULFID    298    307       By similarity.
FT   DISULFID    320    332       By similarity.
FT   DISULFID    326    339       By similarity.
FT   DISULFID    341    350       By similarity.
FT   DISULFID    409    421       By similarity.
FT   DISULFID    415    428       By similarity.
FT   DISULFID    430    439       By similarity.
FT   DISULFID    456    464       By similarity.
FT   DISULFID    458    471       By similarity.
FT   DISULFID    473    482       By similarity.
FT   DISULFID    495    507       By similarity.
FT   DISULFID    501    514       By similarity.
FT   DISULFID    516    525       By similarity.
FT   DISULFID    542    550       By similarity.
FT   DISULFID    544    557       By similarity.
FT   DISULFID    559    568       By similarity.
FT   DISULFID    581    593       By similarity.
FT   DISULFID    587    600       By similarity.
FT   DISULFID    602    611       By similarity.
FT   DISULFID    669    681       By similarity.
FT   DISULFID    675    688       By similarity.
FT   DISULFID    690    699       By similarity.
FT   DISULFID    716    724       By similarity.
FT   DISULFID    718    731       By similarity.
FT   DISULFID    733    742       By similarity.
FT   DISULFID    755    767       By similarity.
FT   DISULFID    761    774       By similarity.
FT   DISULFID    776    785       By similarity.
FT   DISULFID    802    810       By similarity.
FT   DISULFID    804    817       By similarity.
FT   DISULFID    819    828       By similarity.
FT   CONFLICT    323    323       A -> T (in Ref. 1; BAE38699).
FT   CONFLICT   1092   1092       G -> S (in Ref. 1; BAE38699).
FT   CONFLICT   1137   1137       N -> S (in Ref. 1; BAE38699).
FT   CONFLICT   1140   1140       S -> T (in Ref. 1; BAE38699).
SQ   SEQUENCE   1147 AA;  122972 MW;  FBC50896096181CC CRC64;
     MAISSSSCLG LICSLLCHWV GTASSLNLED PNVCSHWESY SVTVQESYPH PFDQIYYTSC
     TDILNWFKCT RHRISYRTAY RHGEKTMYRR KSQCCPGFYE SRDMCVPHCA DKCVHGRCIA
     PNTCQCEPGW GGTNCSSACD GDHWGPHCSS RCQCKNRALC NPITGACHCA AGYRGWRCED
     RCEQGTYGND CHQRCQCQNG ATCDHITGEC RCSPGYTGAF CEDLCPPGKH GPHCEQRCPC
     QNGGVCHHVT GECSCPSGWM GTVCGQPCPE GRFGKNCSQE CQCHNGGTCD AATGQCHCSP
     GYTGERCQDE CPVGSYGVRC AEACRCVNGG KCYHVSGTCL CEAGFSGELC EARLCPEGLY
     GIKCDKRCPC HLDNTHSCHP MSGECGCKPG WSGLYCNETC SPGFYGEACQ QICSCQNGAD
     CDSVTGRCAC APGFKGTDCS TPCPLGRYGI NCSSRCGCKN DAVCSPVDGS CICKAGWHGV
     DCSIRCPSGT WGFGCNLTCQ CLNGGACNTL DGTCTCAPGW RGAKCEFPCQ DGTYGLNCAE
     RCDCSHADGC HPTTGHCRCL PGWSGVHCDS VCAEGRWGPN CSLPCYCKNG ASCSPDDGIC
     ECAPGFRGTT CQRICSPGFY GHRCSQTCPQ CVHSSGPCHH ITGLCDCLPG FTGALCNEVC
     PSGRFGKNCA GVCTCTNNGT CNPIDRSCQC YPGWIGSDCS QPCPPAHWGP NCIHTCNCHN
     GAFCSAYDGE CKCTPGWTGL YCTQRCPLGF YGKDCALICQ CQNGADCDHI SGQCTCRTGF
     MGRHCEQKCP AGTYGYGCRQ ICDCLNNSTC DHITGTCYCS PGWKGARCDQ AGVIIVGNLN
     SLSRTSTALP ADSYQIGAIA GIVVLVLVVL FLLALFIIYR HKQKRKESSM PAVTYTPAMR
     VINADYTIAE TLPHSNGGNA NSHYFTNPSY HTLSQCATSP HVNNRDRMTI AKSKNNQLFV
     NLKNVNPGKR GTLVDCTGTL PADWKQGGYL NELGAFGLDR SYMGKSLKDL GKNSEYNSST
     CSLSSSENPY ATIKDPPALL PKSSECGYVE MKSPARRDSP YAEINNSTPA NRNVYEVEPT
     VSVVQGVFSN SGHVTQDPYD LPKNSHIPCH YDLLPVRDSS SSPKREDGGG SNSTSSNSTS
     SSSSSSE
//
ID   SMCA2_MOUSE             Reviewed;        1577 AA.
AC   Q6DIC0;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Probable global transcription activator SNF2L2;
DE            EC=3.6.4.-;
DE   AltName: Full=ATP-dependent helicase SMARCA2;
DE   AltName: Full=BRG1-associated factor 190B;
DE            Short=BAF190B;
DE   AltName: Full=Protein brahma homolog;
DE   AltName: Full=SNF2-alpha;
DE   AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2;
GN   Name=Smarca2; Synonyms=Baf190b, Brm, Snf2a, Snf2l2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION BY MASS
RP   SPECTROMETRY, IDENTIFICATION IN THE NBAF AND NPBAF COMPLEXES, AND
RP   INTERACTION WITH PHF10.
RX   PubMed=17640523; DOI=10.1016/j.neuron.2007.06.019;
RA   Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T.,
RA   Wu H., Aebersold R., Graef I.A., Crabtree G.R.;
RT   "An essential switch in subunit composition of a chromatin remodeling
RT   complex during neural development.";
RL   Neuron 55:201-215(2007).
CC   -!- FUNCTION: Transcriptional coactivator cooperating with nuclear
CC       hormone receptors to potentiate transcriptional activation. Also
CC       involved in vitamin D-coupled transcription regulation via its
CC       association with the WINAC complex, a chromatin-remodeling complex
CC       recruited by vitamin D receptor (VDR), which is required for the
CC       ligand-bound VDR-mediated transrepression of the CYP27B1 gene (By
CC       similarity). Belongs to the neural progenitors-specific chromatin
CC       remodeling complex (npBAF complex) and the neuron-specific
CC       chromatin remodeling complex (nBAF complex). During neural
CC       development a switch from a stem/progenitor to a post-mitotic
CC       chromatin remodeling mechanism occurs as neurons exit the cell
CC       cycle and become committed to their adult state. The transition
CC       from proliferating neural stem/progenitor cells to post-mitotic
CC       neurons requires a switch in subunit composition of the npBAF and
CC       nBAF complexes. As neural progenitors exit mitosis and
CC       differentiate into neurons, npBAF complexes which contain
CC       ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous
CC       alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits
CC       in neuron-specific complexes (nBAF). The npBAF complex is
CC       essential for the self-renewal/proliferative capacity of the
CC       multipotent neural stem cells. The nBAF complex along with CREST
CC       plays a role regulating the activity of genes essential for
CC       dendrite growth.
CC   -!- SUBUNIT: Component of the BAF complex, which includes at least
CC       actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2,
CC       SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57,
CC       SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more
CC       of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle
CC       cells, the BAF complex also contains DPF3. Component of the WINAC
CC       complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1,
CC       SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H,
CC       CHAF1A and TOP2B. Binds TOPBP1 (By similarity). Component of
CC       neural progenitors-specific chromatin remodeling complex (npBAF
CC       complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B,
CC       SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B,
CC       SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155,
CC       SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and
CC       actin. Component of neuron-specific chromatin remodeling complex
CC       (nBAF complex) composed of at least, ARID1A/BAF250A or
CC       ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
CC       SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
CC       SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B,
CC       DPF3/BAF45C, ACTL6B/BAF53B and actin. Interacts with PHF10/BAF45A.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC   -!- SIMILARITY: Contains 1 bromo domain.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 HSA domain.
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DR   EMBL; BC075641; AAH75641.1; -; mRNA.
DR   IPI; IPI00469712; -.
DR   RefSeq; NP_035546.2; NM_011416.2.
DR   UniGene; Mm.313303; -.
DR   ProteinModelPortal; Q6DIC0; -.
DR   SMR; Q6DIC0; 713-1253, 1383-1491.
DR   DIP; DIP-48888N; -.
DR   STRING; Q6DIC0; -.
DR   PhosphoSite; Q6DIC0; -.
DR   PRIDE; Q6DIC0; -.
DR   Ensembl; ENSMUST00000025862; ENSMUSP00000025862; ENSMUSG00000024921.
DR   GeneID; 67155; -.
DR   KEGG; mmu:67155; -.
DR   UCSC; uc008hbn.1; mouse.
DR   CTD; 67155; -.
DR   MGI; MGI:99603; Smarca2.
DR   HOGENOM; HBG720361; -.
DR   HOVERGEN; HBG056636; -.
DR   InParanoid; Q6DIC0; -.
DR   OrthoDB; EOG418BMJ; -.
DR   PhylomeDB; Q6DIC0; -.
DR   NextBio; 323746; -.
DR   ArrayExpress; Q6DIC0; -.
DR   Bgee; Q6DIC0; -.
DR   Genevestigator; Q6DIC0; -.
DR   GO; GO:0071565; C:nBAF complex; IDA:UniProtKB.
DR   GO; GO:0071564; C:npBAF complex; IDA:UniProtKB.
DR   GO; GO:0016514; C:SWI/SNF complex; TAS:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0006334; P:nucleosome assembly; TAS:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR006576; BRK_domain.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR   InterPro; IPR013999; HAS_subgroup.
DR   InterPro; IPR014012; Helicase/SANT-assoc_DNA-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR006562; HSA.
DR   InterPro; IPR000330; SNF2_N.
DR   Gene3D; G3DSA:1.20.920.10; Bromodomain; 1.
DR   Pfam; PF07533; BRK; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07529; HSA; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00592; BRK; 1.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00573; HSA; 1.
DR   SMART; SM00951; QLQ; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51204; HSA; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; ATP-binding; Bromodomain; DNA-binding;
KW   Helicase; Hydrolase; Neurogenesis; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Transcription; Transcription regulation.
FT   CHAIN         1   1577       Probable global transcription activator
FT                                SNF2L2.
FT                                /FTId=PRO_0000391618.
FT   DOMAIN      441    513       HSA.
FT   DOMAIN      741    906       Helicase ATP-binding.
FT   DOMAIN     1059   1221       Helicase C-terminal.
FT   DOMAIN     1406   1476       Bromo.
FT   NP_BIND     754    761       ATP (By similarity).
FT   MOTIF       856    859       DEGH box.
FT   COMPBIAS      4    170       Pro-rich.
FT   COMPBIAS    172    340       Gln-rich.
FT   COMPBIAS    648    655       Poly-Glu.
FT   COMPBIAS   1302   1306       Poly-Glu.
FT   COMPBIAS   1496   1518       Glu-rich.
FT   MOD_RES     169    169       Phosphoserine (By similarity).
FT   MOD_RES     334    334       Phosphoserine (By similarity).
FT   MOD_RES     596    596       Phosphoserine (By similarity).
FT   MOD_RES     609    609       N6-acetyllysine (By similarity).
FT   MOD_RES     961    961       Phosphoserine (By similarity).
FT   MOD_RES    1002   1002       N6-acetyllysine (By similarity).
FT   MOD_RES    1004   1004       N6-acetyllysine (By similarity).
FT   MOD_RES    1382   1382       Phosphoserine (By similarity).
FT   MOD_RES    1405   1405       Phosphoserine (By similarity).
FT   MOD_RES    1406   1406       Phosphoserine (By similarity).
FT   MOD_RES    1499   1499       Phosphoserine (By similarity).
FT   MOD_RES    1503   1503       Phosphoserine (By similarity).
FT   MOD_RES    1515   1515       Phosphoserine (By similarity).
FT   MOD_RES    1540   1540       N6-acetyllysine (By similarity).
FT   MOD_RES    1542   1542       N6-acetyllysine (By similarity).
FT   MOD_RES    1555   1555       Phosphoserine (By similarity).
FT   MOD_RES    1559   1559       Phosphoserine (By similarity).
FT   MOD_RES    1569   1569       Phosphoserine (By similarity).
FT   MOD_RES    1572   1572       Phosphoserine (By similarity).
FT   MOD_RES    1574   1574       Phosphothreonine (By similarity).
SQ   SEQUENCE   1577 AA;  180253 MW;  5D79E8FFC66085BE CRC64;
     MSTPTDPAAM PHPGPSPGPG PSPGPILGPS PGPGPSPGSV HSMMGPSPGP PSVSHPLSTM
     GSADFPQEGM HQLHKPMDGI HDKGIVEDVH CGSMKGTSMR PPHPGMGPPQ SPMDQHSQGY
     MSPHPSPLGA PEHVSSPTPP QMPPSQPGAL IPGDPQAMNQ PNRGPSPFSP VQLHQLRAQI
     LAYKMLARGQ PLPETLQLAV QGKRTLPGMQ QQQQQQQQQQ QQQQQQQQQQ QQQQQPQQPQ
     QQAQAQPQQQ QQQQQQPALV SYNRPSGPGQ ELLLSGQSAP QKLSAPAPSG RPSPAPQAAV
     QPTATAVPGP SVQQPAPGQP SPVLQLQQKQ SRISPIQKPQ GLDPVEILQE REYRLQARIA
     HRIQELESLP GSLPPDLRTK ATVELKALRL LNFQRQLRQE VVACMRRDTT LETALNSKAY
     KRSKRQTLRE ARMTEKLEKQ QKIEQERKRR QKHQEYLNSI LQHAKDFKEY HRSVAGKIQK
     LSKAVATWHA NTEREQKKET ERIEKERMRR LMAEDEEGYR KLIDQKKDRR LAYLLQQTDE
     YVANLTNLVW EHKQAQAAKE KKKRRRRKKK AEENAEGGEP ALGPDGEPID ESSQMSDLPV
     KVTHTETGKV LFGPEAPKAS QLDAWLEMNP GYEVAPRSDS EESESDYEEE DEEEESSRQE
     TEEKILLDPN SEEVSEKDAK QIIETAKQDV DDEYSMQYSA RGSQSYYTVA HAISERVEKQ
     SALLINGTLK HYQLQGLEWM VSLYNNNLNG ILADEMGLGK TIQTIALITY LMEHKRLNGP
     YLIIVPLSTL SNWTYEFDKW APSVVKISYK GTPAMRRSLV PQLRSGKFNV LLTTYEYIIK
     DKHILAKIRW KYMIVDEGHR MKNHHCKLTQ VLNTHYVAPR RILLTGTPLQ NKLPELWALL
     NFLLPTIFKS CSTFEQWFNA PFAMTGERVD LNEEETILII RRLHKVLRPF LLRRLKKEVE
     SQLPEKVEYV IKCDMSALQK ILYRHMQAKG ILLTDGSEKD KKGKGGAKTL MNTIMQLRKI
     CNHPYMFQHI EESFAEHLGY SNGVINGAEL YRASGKFELL DRILPKLRAT NHRVLLFCQM
     TSLMTIMEDY FAFRNFLYLR LDGTTKSEDR AALLKKFNEP GSQYFIFLLS TRAGGLGLNL
     QAADTVVIFD SDWNPHQDLQ AQDRAHRIGQ QNEVRVLRLC TVNSVEEKIL AAAKYKLNVD
     QKVIQAGMFD QKSSSHERRA FLQAILEHEE ENEEEDEVPD DETLNQMIAR REEEFDLFMR
     MDMDRRREDA RNPKRKPRLM EEDELPSWII KDDAEVERLT CEEEEEKIFG RGSRQRRDVD
     YSDALTEKQW LRAIEDGNLE EMEEEVRLKK RKRRRNVDKD PVKEDVEKAK KRRGRPPAEK
     LSPNPPKLTK QMNAIIDTVI NYKDSSGRQL SEVFIQLPSR KDLPEYYELI RKPVDFKKIK
     ERIRNHKYRS LGDLEKDVML LCHNAQTFNL EGSQIYEDSI VLQSVFKSAR QKIAKEEESE
     EESNEEEEED DEEESESEAK SVKVKIKLNK KEEKGRDTGK GKKRPNRGKA KPVVSDFDSD
     EEQEENEQSE ASGTDNE
//
ID   Q6DIC6_MOUSE            Unreviewed;      2087 AA.
AC   Q6DIC6;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   SubName: Full=Tro protein;
DE   SubName: Full=Trophinin;
GN   Name=Tro; ORFNames=RP23-338A17.3-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Humphries M.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC075630; AAH75630.1; -; mRNA.
DR   EMBL; AL672150; CAM21430.1; -; Genomic_DNA.
DR   IPI; IPI00454175; -.
DR   RefSeq; NP_001002272.1; NM_001002272.2.
DR   UniGene; Mm.3597; -.
DR   ProteinModelPortal; Q6DIC6; -.
DR   STRING; Q6DIC6; -.
DR   PRIDE; Q6DIC6; -.
DR   Ensembl; ENSMUST00000087258; ENSMUSP00000084513; ENSMUSG00000025272.
DR   Ensembl; ENSMUST00000087259; ENSMUSP00000084514; ENSMUSG00000025272.
DR   Ensembl; ENSMUST00000112709; ENSMUSP00000108329; ENSMUSG00000025272.
DR   GeneID; 56191; -.
DR   KEGG; mmu:56191; -.
DR   UCSC; uc009uoq.1; mouse.
DR   CTD; 56191; -.
DR   MGI; MGI:1928994; Tro.
DR   HOGENOM; HBG282076; -.
DR   HOVERGEN; HBG003714; -.
DR   InParanoid; Q6DIC6; -.
DR   OMA; RQTEASS; -.
DR   PhylomeDB; Q6DIC6; -.
DR   NextBio; 311996; -.
DR   ArrayExpress; Q6DIC6; -.
DR   Bgee; Q6DIC6; -.
DR   Genevestigator; Q6DIC6; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0030308; P:negative regulation of cell growth; IDA:MGI.
DR   InterPro; IPR002190; MAGE.
DR   PANTHER; PTHR11736; MAGE; 1.
DR   Pfam; PF01454; MAGE; 1.
DR   PROSITE; PS50838; MAGE; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   2087 AA;  206008 MW;  971EFA7017AF44AC CRC64;
     MDRRNDHGHR VPTFQGPLPP AGSLGLPFSP DVQSETTEKD PPIASRSKKN KNKKNSIKPM
     DKTTPAPPPV PSANDNASNK PKVTLQALNL PMFTQISQAS ATTEAPNIQA SVTSQTQKAK
     TMRVTPKVSL TGSEDATTQL KPPLQALNLP VTTPTIQTPV ANESANSLAS TAVNKSKKAS
     TANNAANKTV PSAAEISLAS AATHTVTTQG QAAKETGSIQ TIAATARSKK NSKGKRTPAK
     TTNTDNEYVE ASNAIEASSR QIGASGRQTE ASNRQIEASS RQTEASNRQT EASSRQTEAS
     SRQTETSNRQ IGASNRQIMA SNRQIGASNR QIEASNRQIG ASNRQTEVSS RQIEASNRQI
     GASNRQTEAS NRQIGASNRQ TEASNRQIGA SNRQTDASNR QTDASNRQTE ASSRQTEASS
     RQTEASSRQT EASSRQIEAS AAAVRPKKPR GKKGNNKGSN SASEPSEAPP AIQTVTNHAL
     SVTVRIRRGS RARKAANKNR ATESQAQIAE QGAQASEASI SALETQVAAA VQALADDYLA
     QLSLEPTTRT RGKRNRKSKH PNGEERTGNN YRRIPWGRRL PPPRDVAILQ ERANKLVKYL
     LVKDQTKIPI KRSDMLKDVI QEYEDYFPEI IERASYALEK MFRVNLKEID KQNNLYILIS
     TQESSAGIMG TTKDTPKLGL LMVILSVIFM NGNKASEAVI WEVLRKLGLH PGVKHSLFGE
     VKKLITDEFV KQKYLEYKRV PNSRPPEYEF FWGLRSYHET SKMKVLKFAC KVQKKDPKDW
     AAQYREAVEM DIQAAAVAVA EAKARAEARA QMGIGEEAVA GPWNWDDMDI NCLTREELGD
     DAQAWSRFSF EIEPRAQENA DPTTNVLFNQ GATTRNSFSD GAGISFGGIT NPSGGFGGIS
     NPSGGFGGIS NPSGGFGGIS NPSGGFGGIS NPSGGFGGIS NPSGGFGGIS NPSGGFGGIS
     NPSGGFGGIS NPSGGFGGIS NPSGGFGGIS NPSGGFGGIS NPSGGFGGIS NPSGGFGGIS
     NPSGGFGGRN SITFGSVPNT SANFSSAPSI SFGDTPNTST SFSGGANSSF SGTPSTSAPF
     CNTASISFGG APSTSTSFST ASISFGGAPS TSTSLSTASI SFGGAPSTST SFSTASISFG
     GAPSTSTSLS TASISFGGAP SINSSSGGSS VSFGGAPTTS TSFSGGPCIS FGGAPCTTAS
     ISGGASSGFG STLCSTNPGF SALSTNTSFG SAPTTSTVFS GAVSTTTGFG GTLSTSVCFG
     SSPYSGAGFG GTLSTSISFG GSPSTNTGFG GTLSTSVSFG ASSSTSSDFG GTLSTSVSFG
     GSSGANAGFG GTLNSSTSFG GAISTSTGFG SALNNSANFG GAISTSFSGV LNSSASFGGA
     INTSAGFGST LNSSASFGSA LSTSASFGGV LNGSAGFGGA LNTNATFGGV LNGSAGFGGA
     MNTNATFGGA LNSNAGFGGA ISTSTNFGGA LNNSAGFGGA MNTSASFGGA LNNSAGFGGA
     ISTNATFGGA LNNSAGFGGA ISTNATFGGA LNNSAGFGGA ISTSASFGGT LNNSASFGGA
     INTSASFGGV LNNSAGFGGA INTSANFGGA LTNSAGFGGA ISTSASFGGA LNNSAGFGGA
     ISTSASFGGA LNNSAGFGGA ISTNASFGGA ISNSPDFGGA FSTSVGFGGT LNTTDFGSTH
     SNSISFGSAP TTSVSFGGSH STNLCFGGAP STSLCFGSAS NTNLCFGGSN STNCFSGATS
     ANFNEGHSIS FGNGLSTSAG FGNGLGTSAG FGSSLGTSTG FGGSLGPSAS FNGGLGTSTG
     FGGGLGTSTD FSGGLNHNAD FNGGLGNSAG FNGGLNTNTD FGGELGTSAG FGDGLGSSTS
     FGAGLVTSDG FAGNLGTNTG FGGTLGTGAG FSVSLNNGNG FGNGPNASFN RGLNTIIGFG
     SGSNTSNGFT GEPNTGSSFS NGPSSIVGFS GGPSTGAGFC SGPSTGGFGG GPSTGPGFGG
     PSTGPGFGGP STGGGFGGPN TGGGFGGPST GGGFGGPSTG GGFGGPSTGG GFGGPSTAAG
     FGSGLSTSTG FGGGLNTSAG FSGGPPSTGT GFGGGASSHG GCGFPYG
//
ID   Q6DIC7_MOUSE            Unreviewed;      2044 AA.
AC   Q6DIC7;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   SubName: Full=Phosphatidylinositol 4-kinase, catalytic, alpha polypeptide;
GN   Name=Pi4ka; Synonyms=Pik4ca;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SIMILARITY: Contains 1 PI3K/PI4K domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; BC075629; AAH75629.1; -; mRNA.
DR   IPI; IPI00115875; -.
DR   RefSeq; NP_001001983.2; NM_001001983.2.
DR   UniGene; Mm.5718; -.
DR   ProteinModelPortal; Q6DIC7; -.
DR   SMR; Q6DIC7; 1553-2036.
DR   STRING; Q6DIC7; -.
DR   PhosphoSite; Q6DIC7; -.
DR   PRIDE; Q6DIC7; -.
DR   Ensembl; ENSMUST00000036161; ENSMUSP00000036162; ENSMUSG00000041720.
DR   Ensembl; ENSMUST00000154364; ENSMUSP00000122550; ENSMUSG00000041720.
DR   GeneID; 224020; -.
DR   KEGG; mmu:224020; -.
DR   UCSC; uc007ykr.1; mouse.
DR   CTD; 224020; -.
DR   MGI; MGI:2448506; Pi4ka.
DR   HOGENOM; HBG315940; -.
DR   HOVERGEN; HBG052742; -.
DR   InParanoid; Q6DIC7; -.
DR   PhylomeDB; Q6DIC7; -.
DR   NextBio; 377009; -.
DR   ArrayExpress; Q6DIC7; -.
DR   Bgee; Q6DIC7; -.
DR   Genevestigator; Q6DIC7; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004428; F:inositol or phosphatidylinositol kinase activity; IEA:InterPro.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR   GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000403; PI3/4_kinase_cat.
DR   InterPro; IPR018936; PI3/4_kinase_CS.
DR   InterPro; IPR015433; PI_Kinase.
DR   InterPro; IPR001263; PInositide-3_kin_accessory_dom.
DR   Gene3D; G3DSA:1.10.1070.11; PI3/4_kinase_cat; 1.
DR   Gene3D; G3DSA:1.25.40.70; PI3Ka; 1.
DR   PANTHER; PTHR10048; PI_Kinase; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF00613; PI3Ka; 1.
DR   SMART; SM00145; PI3Ka; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   1: Evidence at protein level;
KW   Kinase; Transferase.
SQ   SEQUENCE   2044 AA;  231371 MW;  BD490DC93964A9F9 CRC64;
     MCPVDFHGIF QLDERRRDAV IALGIFLIES DLQHKDCVVP YLLRLLRGLP KVYWVEESTA
     RKGRGNLPVA ESFSFCLVTL LSDVACRDPS LRDEILEAIL QVLHVLLGMC QALEIQEKEY
     LCKYAIPCLI GISRSFGRYS NSEESLLSKL FPKVSPHSLR IPEELEGVRR RSFNDFRSIL
     PSNLLTVCQE GTLKRKTSSV SSISQVSPER GIPPPSSPGG SAFHYFEASC LPDGTALEPE
     YYFSTISSSF SISPLFNGIT YKEFCIPLEM LRELLNLVKK IVEEPVLKSL DAIVAGVMEA
     NPSADLYYTT FSDPLYLTMF KMLRDTLYYM KDLPTSFVKE IHDFVLEQFN MSQGELQKIL
     HDADRIHSEM SPLKLRCQAN AACVDLMVWA VKDEQGAENL CIKLSEKLQS KTSSKVIIAH
     LPLLICCLQG LGRLCERFPV VVHSVTPSLR DFLVIPSPVL VKLYKYHSQY HTVAGSDIKI
     SVTNEHSEST LNVLPGKKNQ PSMYEQLRDI AIDNICRCLK AGLTVDPVIV EAFLASLSNR
     LYISQESDKD AHLIPDHTIR ALGHIAVALR DTPKVMEPIL QILQQKFCQP PSPLDVLIID
     QLGCLVITGN QYIYQEVWNL FQQISVKASS VVYSATKDYK DHGYRHCSLA VINALANIAA
     NIQEEHLVDE LLMNLLELFV QLGLEGKRAS ERASEKGPAL KASSSAGNLG VLIPVIAVLT
     RRLPPIKEAK PRLQKLFRDF WLYSVLMGFA VEGSGLWPEE WYEGVCEIAT KSPLLTFPSK
     EPLRSVLQYN SAMKNDTVTL AELSELRSTI INLLDPPPEV SALINKLDFA MSTYLLSVYR
     LEYMRVLRST DPDRFQVMFC YFEDKAIQKD KSGMMQCVIA VADKVFDAFL NMMAEKAKTK
     ENEEELERHA QFLLVNFNHI HKRIRRVADK YLSGLVDKFP HLLWSGTVLK TMLDILQTLS
     LSLSADIHKD QPYYDIPDAP YRITVPDTYE ARESIVKDFA ARCGMILQEA MKWAPTVTKS
     HLQEYLNKHQ NWVSGLSQHT GLAMATESIL HFAGYNKQNT TLGATQLTER PACVKKDYSN
     FMASLNLRNR YAGEVHGMIR FSGATGQMSD LNKMMVQDLI TALDHSHPQH YTQAMFKLTA
     MLISSKDCDP QLLHHLCWGP LRMFNEHGME TALACWEWLL AGKNGVEVPF MREMAGAWHM
     TVEQKFGLFS VETKEADPLA ASEASQPRPC PPEVTPHYIW IDFLVQRFEI AKYCSSDQVE
     IFSSLLQRSM SLNIGGARGS MNRHVAAIGP RFKLLTLGLS LLHADVVPNA TIRNVLREKI
     YSTAFDYFSC PPKFPTQGEK RLREDISIMI KFWTAMFSDK KYLTASQLVP PDNQDTRSNL
     DITVGSRQQA TQGWINTYPL SSGMSTISKK SGMSKKTNRG SQLHKYYMKR RTLLLSLLAT
     EIERLITWYN PLSAPELELD QAGENSVANW RSKYISLSEK QWKDNVNLAW SISPYLAVQL
     PARFKNTEAI GNEVTRLVRL DPGAVSDVPE AIKFLVTWHT IDADAPELSH VLCWAPTDPP
     TGLSYFSSMY PPHPLTAQYG VKVLRSFPPD AILFYIPQIV QALRYDKMGY VREYILWAAA
     KSQLLAHQFI WNMKTNIYLD EEGHQKDPDI GDLLEQLVEE ITGSLSGPAK DFYQREFDFF
     NKITNVSAII KPYPKGDERK KACLSALSEV KVQPGCYLPS NPEAIVLDID YKSGTPMQSA
     AKAPYLAKFK VKRCGVSELE KEGLQCRSDA EDECFSQEAD GKKICWQAAI FKVGDDCRQD
     MLALQIIDLF KNIFQLVGLD LFVFPYRVVA TAPGCGVIEC IPDCTSRDQL GRQTDFGMYD
     YFTRQYGDES TLAFQQARYN FIRSMAAYSL LLFLLQIKDR HNGNIMLDKK GHIIHIDFGF
     MFESSPGGNL GWEPDIKLTD EMVMIMGGKM EATPFKWFME MCVRGYLAVR PYMDAVVSLV
     TLMLDTGLPC FRGQTIKLLK HRFSPNMTER EAANFIMKVI QNCFLSNRSR TYDMIQYYQN
     DIPY
//
ID   Q6DIC8_MOUSE            Unreviewed;      1118 AA.
AC   Q6DIC8;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   SubName: Full=Diacylglycerol kinase kappa;
GN   Name=Dgkk;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC075627; AAH75627.1; -; mRNA.
DR   IPI; IPI00453953; -.
DR   RefSeq; NP_808582.3; NM_177914.3.
DR   UniGene; Mm.392752; -.
DR   UniGene; Mm.464416; -.
DR   ProteinModelPortal; Q6DIC8; -.
DR   SMR; Q6DIC8; 60-151, 169-222, 224-293, 334-432.
DR   PhosphoSite; Q6DIC8; -.
DR   PRIDE; Q6DIC8; -.
DR   Ensembl; ENSMUST00000067410; ENSMUSP00000067591; ENSMUSG00000062393.
DR   GeneID; 331374; -.
DR   KEGG; mmu:331374; -.
DR   UCSC; uc009sla.1; mouse.
DR   CTD; 331374; -.
DR   MGI; MGI:3580254; Dgkk.
DR   GeneTree; ENSGT00600000084245; -.
DR   HOGENOM; HBG717797; -.
DR   HOVERGEN; HBG051346; -.
DR   InParanoid; Q6DIC8; -.
DR   ArrayExpress; Q6DIC8; -.
DR   Bgee; Q6DIC8; -.
DR   Genevestigator; Q6DIC8; -.
DR   GO; GO:0005886; C:plasma membrane; ISS:HGNC.
DR   GO; GO:0004143; F:diacylglycerol kinase activity; ISS:HGNC.
DR   GO; GO:0007205; P:activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway; IEA:InterPro.
DR   GO; GO:0046339; P:diacylglycerol metabolic process; ISS:HGNC.
DR   GO; GO:0035556; P:intracellular signal transduction; ISS:HGNC.
DR   GO; GO:0006979; P:response to oxidative stress; ISS:HGNC.
DR   InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00609; DAGK_acc; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00045; DAGKa; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS50146; DAGK; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   2: Evidence at transcript level;
KW   Kinase; Transferase.
SQ   SEQUENCE   1118 AA;  125963 MW;  DC853E8CFB9B84B6 CRC64;
     MERAPESWPE PTPESCLRMS PALHLLQVVP GEKSGTASPV LLPLPSPKPP ITWSRIKKIL
     KEGPLLKNCN SFRRWKLRYC LVQGQKLHFA HHPSFAHFET IDLSQVVLAE SSCRNLCHGF
     CVITPHRKVS LVAPTRQDME EWINIIKTVQ QGEIRQIPAA ENNPFLVGMH YWYSSSNPRS
     HFCNVCRENI PALSRDAVTC EVCQVKSHKF CALRANKDCK WNTLSVTDDL LLPADEIQTM
     PHQWVEGNIP AGSQCVVCHK SCGSHHRLQD FRCLWCGSTV HGACQKRFSK ECSFGSRRSS
     IVPPTALSDP RGDGQLVVSP DFWNLDWPLT CSCPLLIFIN SKSGDHQGII FLRKFKQYLN
     PSQVFDLAKG GPEAGIAMFK NFARFRVLVC GGDGSVSWVL STIDAYGLHD RCQLAIIPLG
     TGNDLARVLG WGAVWSKGTS PLDILSRVEQ AHVRILDRWS VMIRETPRQA PLLKGQVAMD
     IPRFEAAAIK NVESATTELN KILKAKYPTE MVIATRFLCS AVEDFVEDIV KAWHQIKQNS
     TAVESVILKS DLMYDKLSVL IDLLAEDAVA ASAERTATAY GSRSQADGKP FVPQLDHIAR
     AKLELAERAQ KLQQSLKLII FQVEQVLDEE SRQSLSVKNF TSSLFLGDGD DDDSDDYDQS
     PRHRSRCDIL CSIPSLRNED LDNLDLEHLH IAPETIRFKK KCVMNNYFGI GLDAKISLEF
     NSRREEHPEQ YNSRLKNKIW YGLLGSKELL QRSYRKLEER IHLECDGEAV SLPNLQGIVV
     LNITSYAGGV NFWGRNRATT EYDVPAINDG KLEVVAIFGS VQMAMSRIVN LQQHRIAQCH
     EVVITIDGED GVPVQVDGEA WIQKPGLIKI KYKNVAQMLM RDRDFENSMK TWESKHTEIQ
     AVQPPHLDFQ ESQDSLSDGE YAQMQHLARL AENLISRLTD LSKVHQHVSV LMDSVNASAN
     ILNDVFYSQD SGNEAGAASC IPIETLSRTD AVDVTFSLKG LYDDTKAFLD ENLLRDAEDR
     AMLQTALDAM NTELRRILAI GWLSQIFFPE EQASDTRSLS RRFRIKFPKL GKKKQREEGE
     KPKSSQRFPG FLGKFWRRRN RSNRAKADDP PTPSSSQL
//
ID   SCAF8_MOUSE             Reviewed;        1268 AA.
AC   Q6DID3; Q3TTX6; Q5U5V8; Q80TJ3; Q8C037;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=Protein SCAF8;
DE   AltName: Full=RNA-binding motif protein 16;
DE   AltName: Full=SR-related and CTD-associated factor 8;
GN   Name=Scaf8; Synonyms=Kiaa1116, Rbm16;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N-3; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 462-1268.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   INTERACTION WITH POLR2A.
RX   MEDLINE=96293459; PubMed=8692929; DOI=10.1073/pnas.93.14.6975;
RA   Yuryev A., Patturajan M., Litingtung Y., Joshi R.V., Gentile C.,
RA   Gebara M., Corden J.L.;
RT   "The C-terminal domain of the largest subunit of RNA polymerase II
RT   interacts with a novel set of serine/arginine-rich proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:6975-6980(1996).
RN   [5]
RP   INTERACTION WITH POLR2A, AND SUBCELLULAR LOCATION.
RX   PubMed=9528809;
RA   Patturajan M., Wei X., Berezney R., Corden J.L.;
RT   "A nuclear matrix protein interacts with the phosphorylated C-terminal
RT   domain of RNA polymerase II.";
RL   Mol. Cell. Biol. 18:2406-2415(1998).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May play a role in mRNA processing (By similarity).
CC   -!- SUBUNIT: Interacts with phosphorylated POLR2A (via C-terminus).
CC       Identified in a complex with CDC5L and other spliceosomal
CC       proteins. May associate with the spliceosome (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Nucleus matrix. Note=Detected in
CC       granular nuclear foci which correspond to sites of active
CC       transcription.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 CID domain.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65733.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK122451; BAC65733.1; ALT_INIT; mRNA.
DR   EMBL; BC038363; AAH38363.1; -; mRNA.
DR   EMBL; BC075621; AAH75621.1; -; mRNA.
DR   EMBL; AK032418; BAC27860.1; -; mRNA.
DR   EMBL; AK161113; BAE36197.1; -; mRNA.
DR   IPI; IPI00938443; -.
DR   RefSeq; NP_598884.2; NM_134123.3.
DR   UniGene; Mm.124373; -.
DR   ProteinModelPortal; Q6DID3; -.
DR   SMR; Q6DID3; 1-138, 476-586.
DR   Ensembl; ENSMUST00000076734; ENSMUSP00000076024; ENSMUSG00000046201.
DR   GeneID; 106583; -.
DR   KEGG; mmu:106583; -.
DR   UCSC; uc008aej.1; mouse.
DR   CTD; 106583; -.
DR   MGI; MGI:1925212; Scaf8.
DR   HOVERGEN; HBG055796; -.
DR   InParanoid; Q6DID3; -.
DR   OMA; PHARVFD; -.
DR   OrthoDB; EOG45MN4V; -.
DR   ArrayExpress; Q6DID3; -.
DR   Bgee; Q6DID3; -.
DR   Genevestigator; Q6DID3; -.
DR   GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR006903; DUF618.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR006569; RNA_polymerase_II_lsu_CTD.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Gene3D; G3DSA:1.25.40.90; ENTH_VHS; 1.
DR   Pfam; PF04818; DUF618; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00582; RPR; 1.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF48464; ENTH_VHS; 1.
DR   PROSITE; PS51391; CID; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
KW   Phosphoprotein; RNA-binding; Spliceosome; Ubl conjugation.
FT   CHAIN         1   1268       Protein SCAF8.
FT                                /FTId=PRO_0000394194.
FT   DOMAIN        1    139       CID.
FT   DOMAIN      477    551       RRM.
FT   COMPBIAS    193    371       Gln-rich.
FT   COMPBIAS    397    459       Arg-rich.
FT   COMPBIAS    635   1000       Pro-rich.
FT   COMPBIAS   1012   1179       Arg-rich.
FT   MOD_RES     617    617       Phosphoserine.
FT   CROSSLNK     18     18       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO-1) (By
FT                                similarity).
FT   CONFLICT    938    938       P -> T (in Ref. 3; BAC27860).
FT   CONFLICT   1171   1171       N -> I (in Ref. 2; AAH38363).
SQ   SEQUENCE   1268 AA;  139572 MW;  8FDFB70FCB2791FC CRC64;
     MEAVKTFNSE LYSLNDYKPP ISKAKMTQIT KAAIKAIKFY KHVVQSVEKF IQKCKPEYKV
     PGLYVIDSIV RQSRHQFGQE KDVFAPRFSN NIISTFQNLY RCPGDDKSKI VRVLNLWQKN
     NVFKSEIIQP LLDMAAGIPP PVVTPVLAST TAAMSNTPGT PVTPVTPANV VQGLPDPWVS
     QIANTDTLAA VAQILQSPQG QQLQQLIQTL QIQQQKPQPS ILQALDAGLV VQLQALTAQL
     TAAAAAANTL TPLDQGVSFN KKLMDRFDFG EDSEHSEESK KEMPTPQLSH VSESVNNSIF
     HQIAEQLQQQ NLEQLRQQLL EQQQPQKVTP QDSQEGTFGS EHSASPSQGS SQQHFLEPEA
     NLDDSIDIQQ QDMDIDEGQD VVEEEIFEPE AKKVAVRSRS RTHSRSRSRS PRKRRSRSRS
     GSRKRKHRKR SRSHSREKKR KASRSYSSER RAREREKERQ KKGLPPVRSK TLSVCSTTLW
     VGQVDKKATQ QDLTNLFEEF GQIESINMIP PRGCAYVCMV HRQDSFRALQ KLSSGSYKIG
     SKVIKIAWAL NKGVKTEYKQ FWDVDLGVTY IPWEKVKVDD LDGFAEGGMI DQETVNAEWE
     TVKASEPVKE PVQTAQSPAP VEKESVVTTQ AEVFPPPVAM LQIPVAPAVP AVSLVPPAFP
     VSMPVPPPGF NPIPPPPFLR ASFNPSQPPP GFMPPPVPPP VVPPPAIPPV VPTSLVQPPL
     SMTPEAVKDV GFGSLVLPSG SVAGSLAPST LPAGNVFNPP SKAEPEEKVP HLIEHQIPSG
     ENTRPVIPSD IPSSAAMLAQ PPGASSTSGI LCVQRPNVSS NSEILGVRPA NVSNSAAIMG
     AQPPNILNNS GILAIQPPNV SSGSGLLGVL PPNLPNNSGL VGLQPPNVTS PAGLLGTQPP
     IGPQNLPPLA IPAQRMPALP MLDIRPGLIA QAPGPRFPLL QPGIPPQRGI PPPSVLDAAL
     HPPPRGPFPP GDLFSQPERP FLAPGRPSID NVPNPDKRIP LGNDNIQQEG DRDYRFPPIE
     TREGITRPPQ VDVRDVVGRR LDPREGPGRP PLDARDHFGR PPVDMRENLV RPSLDHLGRR
     DHFGFPPEKP WGPRDFDERE HRVLPVFGGP KGLHEERGRF RAGNYRFDPR SGPWNRGFGQ
     EVHRDFDDRR RPWERQRDRD DRDFDFCREI NGNRLGRDRI QNTWVPPPHA RVFDYFEGAT
     SQRKGDNVPQ VNGENTERHA QPPPLPVQKD PELYEKLASS GDVDKEESGT VAGVESEAVV
     ESTETEGT
//
ID   LEMD2_MOUSE             Reviewed;         511 AA.
AC   Q6DVA0; Q8C4H8; Q8R0N2;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=LEM domain-containing protein 2;
GN   Name=Lemd2; Synonyms=Lem2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, FUNCTION, TISSUE
RP   SPECIFICITY, INTERACTION WITH LAMIN, AND DEVELOPMENTAL STAGE.
RC   STRAIN=FVB/N;
RX   PubMed=16339967; DOI=10.1242/jcs.02701;
RA   Brachner A., Reipert S., Foisner R., Gotzmann J.;
RT   "LEM2 is a novel MAN1-related inner nuclear membrane protein
RT   associated with A-type lamins.";
RL   J. Cell Sci. 118:5797-5810(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 225-511.
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507 AND SER-509, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Involved in nuclear structure organization.
CC   -!- SUBUNIT: Binds to the lamin tail, in vitro.
CC   -!- SUBCELLULAR LOCATION: Nucleus inner membrane; Multi-pass membrane
CC       protein. Note=Lamina-associated protein residing in the inner
CC       nuclear membrane (INM). Localized exclusively to the nuclear
CC       envelope, giving rise to a typical rim-like staining of the
CC       nuclear periphery.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- DEVELOPMENTAL STAGE: Expressed at detectable levels throughout
CC       later stages of mouse development such as E12, E14, E16 and E18.
CC   -!- SIMILARITY: Contains 1 LEM domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH26588.1; Type=Erroneous initiation;
CC       Sequence=BAC38419.1; Type=Frameshift; Positions=446;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY640307; AAT71319.1; -; mRNA.
DR   EMBL; AK082131; BAC38419.1; ALT_SEQ; mRNA.
DR   EMBL; AK143224; BAE25316.1; -; mRNA.
DR   EMBL; BC026588; AAH26588.1; ALT_INIT; mRNA.
DR   IPI; IPI00465876; -.
DR   RefSeq; NP_666187.2; NM_146075.2.
DR   UniGene; Mm.29689; -.
DR   HSSP; Q9Y2U8; 2CH0.
DR   ProteinModelPortal; Q6DVA0; -.
DR   SMR; Q6DVA0; 2-42, 404-510.
DR   STRING; Q6DVA0; -.
DR   PhosphoSite; Q6DVA0; -.
DR   PRIDE; Q6DVA0; -.
DR   Ensembl; ENSMUST00000055117; ENSMUSP00000058221; ENSMUSG00000044857.
DR   GeneID; 224640; -.
DR   KEGG; mmu:224640; -.
DR   CTD; 224640; -.
DR   MGI; MGI:2385045; Lemd2.
DR   eggNOG; roNOG08483; -.
DR   GeneTree; ENSGT00530000063791; -.
DR   HOGENOM; HBG125588; -.
DR   HOVERGEN; HBG099961; -.
DR   InParanoid; Q6DVA0; -.
DR   OMA; DTTRDVY; -.
DR   OrthoDB; EOG49CQ7W; -.
DR   PhylomeDB; Q6DVA0; -.
DR   NextBio; 377269; -.
DR   ArrayExpress; Q6DVA0; -.
DR   Bgee; Q6DVA0; -.
DR   CleanEx; MM_LEMD2; -.
DR   Genevestigator; Q6DVA0; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR018996; Inner-Nucl-membr_MAN1.
DR   InterPro; IPR003887; LEM.
DR   InterPro; IPR011015; LEM-like_dom.
DR   Gene3D; G3DSA:1.10.720.40; LEM; 1.
DR   Pfam; PF03020; LEM; 1.
DR   Pfam; PF09402; MAN1_C; 1.
DR   SMART; SM00540; LEM; 1.
DR   SUPFAM; SSF63451; LEM_like; 1.
DR   PROSITE; PS50954; LEM; 1.
PE   1: Evidence at protein level;
KW   Membrane; Nucleus; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    511       LEM domain-containing protein 2.
FT                                /FTId=PRO_0000285250.
FT   TRANSMEM    221    241       Helical; (Potential).
FT   TRANSMEM    385    405       Helical; (Potential).
FT   DOMAIN        1     42       LEM.
FT   REGION       80    112       Interaction with lamin A/C complexes (By
FT                                similarity).
FT   COMPBIAS    413    416       Poly-Glu.
FT   MOD_RES     145    145       Phosphoserine (By similarity).
FT   MOD_RES     149    149       Phosphoserine (By similarity).
FT   MOD_RES     150    150       Phosphoserine (By similarity).
FT   MOD_RES     507    507       Phosphoserine.
FT   MOD_RES     509    509       Phosphoserine.
FT   CONFLICT    357    357       T -> A (in Ref. 2; BAC38419).
SQ   SEQUENCE   511 AA;  57507 MW;  190BEA7724BF7EDB CRC64;
     MAGLSDLELR RELQALGFQP GPITDTTRNV YRNKLRRLRG EARLRDDERL REDAGPREDA
     GPRGPERQRE EARLREEAPL RARPAASVLR SEPWPLSPSP PAPSAASDAS GPYGNFGASA
     SPWAASRGLS YPPHAGPGPL RRRASVRGSS EDDEDTRTPD RHAPGRGRHW WAPPSASARP
     HSALLGADAR PGLKGSRTGS AGAGRTRPEV GRWLERCLSR LLLWASLGLL LGFLAILWVK
     MGKPSAPQEA EDNMKLLPVD CERKTDEFCQ AKQKAALLEL LHELYNFLAI QAGNFECGNP
     EKLKSKCIPV LEAQEYIANV TSSPSSRFKA ALTWILSSNK DVGIWLKGED PSELATTVDK
     VVCLESARPR MGIGCRLSRA LLTAVTHVLI FFWCLAFLWG LLILLKYRWR KLEEEEQAMY
     EMVKKIIDVV QDHYVDWEQD MERYPYVGIL HVRDSLIPPQ SRRRMKRVWD RAVEFLASNE
     SRIQTESHRV AGEDMLVWRW TKPSSFSDSE R
//
ID   LR16A_MOUSE             Reviewed;        1374 AA.
AC   Q6EDY6; Q5NCM0; Q8BQ45; Q8BRS5; Q91YZ6;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Leucine-rich repeat-containing protein 16A;
DE   AltName: Full=CARMIL homolog;
GN   Name=Lrrc16a; Synonyms=Carmil, Lrrc16;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP   LOCATION, INTERACTION WITH CAPZA2, AND MUTAGENESIS OF LYS-991 AND
RP   ARG-993.
RC   STRAIN=C57BL/6J;
RX   PubMed=16054028; DOI=10.1016/j.devcel.2005.06.008;
RA   Yang C., Pring M., Wear M.A., Huang M., Cooper J.A., Svitkina T.M.,
RA   Zigmond S.H.;
RT   "Mammalian CARMIL inhibits actin filament capping by capping
RT   protein.";
RL   Dev. Cell 9:209-221(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 410-1374 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 595-1374 (ISOFORM 1).
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-972, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Binds CAPZA2 with high affinity and significantly
CC       decreases CAPZA2 affinity for actin barbed ends. Increases the
CC       rate of elongation from seeds in the presence of CAPZA2, however,
CC       seems unable to nucleate filaments. Rapidly uncaps barbed ends
CC       capped by CAPZA2 and enhances barbed-end actin polymerization.
CC   -!- SUBUNIT: Interacts via its C-terminus with CAPZA2 in cytoplasm;
CC       interaction is essential for lamellipodial protrusion and cell
CC       translocation.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Colocalized with F-actin in
CC       lamellipodia but not with F-actin in stress fibers.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6EDY6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6EDY6-2; Sequence=VSP_032421, VSP_032422;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q6EDY6-3; Sequence=VSP_032423, VSP_032424;
CC         Note=No experimental confirmation available. May be produced at
CC         very low levels due to a premature stop codon in the mRNA,
CC         leading to nonsense-mediated mRNA decay;
CC   -!- SIMILARITY: Belongs to the CARMIL family.
CC   -!- SIMILARITY: Contains 11 LRR (leucine-rich) repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH12229.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAC31591.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC   -----------------------------------------------------------------------
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DR   EMBL; AY437876; AAR96060.1; -; mRNA.
DR   EMBL; AK051570; BAC34678.1; -; mRNA.
DR   EMBL; AK043591; BAC31591.1; ALT_INIT; mRNA.
DR   EMBL; AL606464; CAI35972.2; -; Genomic_DNA.
DR   EMBL; AL590864; CAI35972.2; JOINED; Genomic_DNA.
DR   EMBL; AL683873; CAI35972.2; JOINED; Genomic_DNA.
DR   EMBL; BC012229; AAH12229.1; ALT_INIT; mRNA.
DR   IPI; IPI00460032; -.
DR   IPI; IPI00474873; -.
DR   IPI; IPI00889303; -.
DR   RefSeq; NP_081101.3; NM_026825.3.
DR   UniGene; Mm.211047; -.
DR   PDB; 2KZ7; NMR; -; C=965-1039.
DR   PDB; 3AA0; X-ray; 1.70 A; C=985-1005.
DR   PDB; 3AAE; X-ray; 3.30 A; V/W/X/Y/Z=971-1002.
DR   PDBsum; 2KZ7; -.
DR   PDBsum; 3AA0; -.
DR   PDBsum; 3AAE; -.
DR   ProteinModelPortal; Q6EDY6; -.
DR   SMR; Q6EDY6; 192-638, 974-1039.
DR   STRING; Q6EDY6; -.
DR   Ensembl; ENSMUST00000072889; ENSMUSP00000072662; ENSMUSG00000021338.
DR   GeneID; 68732; -.
DR   KEGG; mmu:68732; -.
DR   UCSC; uc007pvn.1; mouse.
DR   CTD; 68732; -.
DR   MGI; MGI:1915982; Lrrc16a.
DR   GeneTree; ENSGT00390000014487; -.
DR   HOGENOM; HBG715980; -.
DR   HOVERGEN; HBG108094; -.
DR   InParanoid; Q6EDY6; -.
DR   OMA; VDEFFTK; -.
DR   OrthoDB; EOG4GTKC4; -.
DR   NextBio; 327798; -.
DR   ArrayExpress; Q6EDY6; -.
DR   Bgee; Q6EDY6; -.
DR   CleanEx; MM_LRRC16A; -.
DR   Genevestigator; Q6EDY6; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil; Cytoplasm;
KW   Isopeptide bond; Leucine-rich repeat; Phosphoprotein; Repeat;
KW   Ubl conjugation.
FT   CHAIN         1   1374       Leucine-rich repeat-containing protein
FT                                16A.
FT                                /FTId=PRO_0000325816.
FT   REPEAT      245    269       LRR 1.
FT   REPEAT      275    298       LRR 2.
FT   REPEAT      304    327       LRR 3.
FT   REPEAT      336    363       LRR 4.
FT   REPEAT      391    418       LRR 5.
FT   REPEAT      423    447       LRR 6.
FT   REPEAT      485    510       LRR 7.
FT   REPEAT      547    570       LRR 8.
FT   REPEAT      574    597       LRR 9.
FT   REPEAT      658    682       LRR 10.
FT   REPEAT      962    985       LRR 11.
FT   REGION      962   1084       Inhibits capping activity of CAPZA2.
FT   COILED      714    738       Potential.
FT   COMPBIAS   1246   1251       Poly-Ser.
FT   COMPBIAS   1253   1303       Pro-rich.
FT   MOD_RES     920    920       Phosphothreonine (By similarity).
FT   MOD_RES     972    972       Phosphoserine.
FT   MOD_RES    1229   1229       Phosphothreonine (By similarity).
FT   MOD_RES    1281   1281       Phosphoserine (By similarity).
FT   MOD_RES    1289   1289       Phosphoserine (By similarity).
FT   MOD_RES    1295   1295       Phosphoserine (By similarity).
FT   MOD_RES    1335   1335       Phosphoserine (By similarity).
FT   CROSSLNK    597    597       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   VAR_SEQ     260    260       I -> M (in isoform 2).
FT                                /FTId=VSP_032421.
FT   VAR_SEQ     261   1374       Missing (in isoform 2).
FT                                /FTId=VSP_032422.
FT   VAR_SEQ     918    918       M -> MTLCCTS (in isoform 3).
FT                                /FTId=VSP_032423.
FT   VAR_SEQ    1332   1374       SRRSWGPAQEYQEQKQRSSGKDGHQGSKCSDSGEEAEKEFI
FT                                FV -> CPTNF (in isoform 3).
FT                                /FTId=VSP_032424.
FT   MUTAGEN     991    991       K->A: Decreased binding affinity.
FT   MUTAGEN     993    993       R->A: Loss of binding affinity.
FT   MUTAGEN     993    993       R->E: Greatly decreased binding affinity.
FT   CONFLICT      8      8       V -> A (in Ref. 1; AAR96060).
FT   CONFLICT    782    782       L -> W (in Ref. 1; AAR96060 and 4;
FT                                AAH12229).
FT   CONFLICT    796    796       N -> S (in Ref. 4; AAH12229).
FT   CONFLICT   1309   1309       S -> P (in Ref. 1; AAR96060 and 4;
FT                                AAH12229).
SQ   SEQUENCE   1374 AA;  151860 MW;  A7BE0350B3770101 CRC64;
     MTDESSDVPR ELMESIKDVI GRKIKISVKK KVKLEVKGDR VENKVLVLTS CRAFLLSARI
     PSKLELTFSY LEIHGVICHK PAQMVVETEK CNMSMKMVSP EDVSEVLAHI GTCLRRIFPG
     LSPLRIMKKV SMEPSERLAS LQALWDSQTL AEPGPCGGFS QMYACVCDWL GFSYKEEVQW
     DVDTIYLTQD TRELNLQDFS HLEHRDLIPI IAALEYNQWF TKLSSKDLKL STDVCEQILR
     VVSRSNRLEE LVLENAGLRI DFAQKLAGAL AHNPNSGLHT INLAGNSLED RGVSSLSIQF
     AKLPKGLKHL NLSKTSLSPK GVNSLCQSLS ANPLTASTLT HLDLSGNALR GDDLSHMYNF
     LAQPNTIVHL DLSNTECSLE MVCSALLRGC LQCLAVLNLS RSVFSHRKGK EVPPSFKQFF
     SSSLALIQIN LSGTKLSPEP LKALLLGLAC NHSLKGVSLD LSNCELGHCL RSGGAQVLEG
     CIAEIHNITS LDISDNGLES DLSTLIVWLS KNRSIQHLAL GKNFNNMKSK NLTPVLDNLV
     QMIQDEDSPL QSLSLADSKL KAEVTIIINA LGSNTSLTKV DISGNGMGDM GAKMLAKALQ
     INTKLRTVIW DKNNITAQGF QDIAVAMEKN YTLRFMPIPM YDAAQALKTN PEKTEEALQK
     IENYLLRNHE TRKYLQEQAY RLQQGIVTST TQQMIDRICV KVQDHLNSLR ACGGDAIQED
     LKAAERLMRD AKNSKTLLPN LYHVGGASWA GASGLSSSPI QETLESMAGE VTRVVDEQLK
     DLLESMVDAA ETLCPNVMRK AHIRQDLIHA STEKISIPRT FVKNVLLEQS GIDILNKISE
     VKLTVASFLS DRIVDEILDS LSSSHRKLAN HFSRLNKSLP QREDLEVELV EEKPVKRAIL
     TVEDLTEVER LEDLDTCMMT PKSKRKSIHS RMLRPVSRAF EMEFDLDKAL EEVPIHIEDP
     PFPSVRQEKR SSGLISELPS EEGRRLEHFT KLRPKRNKKQ QPTQAAVCTI SILPQDGEQN
     GLMGRVDEGV DEFFTKKVTK MDCKRSSSRS SDAHELGEGD EKKKRDSRRS GFLNLIKSRS
     RSERPPTVLM TEELSSPKGA MRSPPVDTTR KEIKAAEHNG APDRTEEIKT PEPLEEGPAE
     EAGRAERSDS RGSPQGGRRY VQVMGSGLLA EMKAKQERRA ACAQKKLGND VISQDPSSPV
     SCNTERLEGG ATVPKLQPGL PEARFGSGTP EKNAKAEPRV DGGCRSRSSS SMPTSPKPLL
     QSPKPSPSAR PSIPQKPRTA SRPEDTPDSP SGPSSPKVAL LPPILKKVSS DKERDGQNSS
     QSSPRSFSQE ASRRSWGPAQ EYQEQKQRSS GKDGHQGSKC SDSGEEAEKE FIFV
//
ID   SCMC3_MOUSE             Reviewed;         467 AA.
AC   Q6GQS1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Calcium-binding mitochondrial carrier protein SCaMC-3;
DE   AltName: Full=Small calcium-binding mitochondrial carrier protein 3;
DE   AltName: Full=Solute carrier family 25 member 23;
GN   Name=Slc25a23; Synonyms=Scamc3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Calcium-dependent mitochondrial solute carrier.
CC       Mitochondrial solute carriers shuttle metabolites, nucleotides,
CC       and cofactors through the mitochondrial inner membrane. May act as
CC       a ATP-Mg/Pi exchanger that mediates the transport of Mg-ATP in
CC       exchange for phosphate, catalyzing the net uptake or efflux of
CC       adenine nucleotides into or from the mitochondria (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier family.
CC   -!- SIMILARITY: Contains 3 EF-hand domains.
CC   -!- SIMILARITY: Contains 3 Solcar repeats.
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DR   EMBL; BC072660; AAH72660.1; -; mRNA.
DR   IPI; IPI00283600; -.
DR   RefSeq; NP_080153.2; NM_025877.4.
DR   UniGene; Mm.23720; -.
DR   HSSP; P62166; 1G8I.
DR   ProteinModelPortal; Q6GQS1; -.
DR   SMR; Q6GQS1; 10-146, 183-464.
DR   PRIDE; Q6GQS1; -.
DR   Ensembl; ENSMUST00000040280; ENSMUSP00000040198; ENSMUSG00000046329.
DR   GeneID; 66972; -.
DR   KEGG; mmu:66972; -.
DR   NMPDR; fig|10090.3.peg.3211; -.
DR   UCSC; uc008ddu.1; mouse.
DR   CTD; 66972; -.
DR   MGI; MGI:1914222; Slc25a23.
DR   eggNOG; roNOG04467; -.
DR   GeneTree; ENSGT00390000010947; -.
DR   HOGENOM; HBG735918; -.
DR   HOVERGEN; HBG108464; -.
DR   InParanoid; Q6GQS1; -.
DR   OMA; NMEEIVH; -.
DR   OrthoDB; EOG4B2SX4; -.
DR   PhylomeDB; Q6GQS1; -.
DR   NextBio; 323175; -.
DR   ArrayExpress; Q6GQS1; -.
DR   Bgee; Q6GQS1; -.
DR   Genevestigator; Q6GQS1; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR002067; Mit_carrier.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00926; MITOCARRIER.
DR   SMART; SM00054; EFh; 3.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 3.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   2: Evidence at transcript level;
KW   Calcium; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    467       Calcium-binding mitochondrial carrier
FT                                protein SCaMC-3.
FT                                /FTId=PRO_0000317610.
FT   TOPO_DOM      1    187       Mitochondrial intermembrane (Potential).
FT   TRANSMEM    188    205       Helical; Name=1; (Potential).
FT   TOPO_DOM    206    242       Mitochondrial matrix (Potential).
FT   TRANSMEM    243    262       Helical; Name=2; (Potential).
FT   TOPO_DOM    263    285       Mitochondrial intermembrane (Potential).
FT   TRANSMEM    286    299       Helical; Name=3; (Potential).
FT   TOPO_DOM    300    335       Mitochondrial matrix (Potential).
FT   TRANSMEM    336    355       Helical; Name=4; (Potential).
FT   TOPO_DOM    356    378       Mitochondrial intermembrane (Potential).
FT   TRANSMEM    379    396       Helical; Name=5; (Potential).
FT   TOPO_DOM    397    435       Mitochondrial matrix (Potential).
FT   TRANSMEM    436    455       Helical; Name=6; (Potential).
FT   TOPO_DOM    456    467       Mitochondrial intermembrane (Potential).
FT   DOMAIN        9     44       EF-hand 1.
FT   DOMAIN       76    111       EF-hand 2.
FT   DOMAIN      112    147       EF-hand 3.
FT   REPEAT      182    268       Solcar 1.
FT   REPEAT      276    361       Solcar 2.
FT   REPEAT      373    461       Solcar 3.
FT   CA_BIND      22     33       1 (Potential).
FT   CA_BIND      89    100       2 (Potential).
SQ   SEQUENCE   467 AA;  52497 MW;  6C17CB6C03CDD8B6 CRC64;
     MRGGSSDAER RQRWGRLFEE LDSNKDGRVD VHELRQGLAR LGRGDPDRAQ QGVSSDWDAD
     PDGGLSLEEF TRYLQEREQR LLLMFHSLDR NQDGHIDVSE IQQSFRALGI SISLEQAEKI
     LHSMDRDGTM TIDWQEWRDH FLLHSLENVE DVLYFWKHST VLDIGECLTV PDEFSQEEKL
     TGMWWKQLVA GAVAGAVSRT GTAPLDRLKV FMQVHASKSN RLNILGGLRN MIQEGGVLSL
     WRGNGINVLK IAPESAIKFM AYEQIKRAIR GQQETLHVQE RFVAGSLAGA TAQTIIYPME
     VLKTRLTLRR TGQYKGLLDC AKRILEREGP RAFYRGYLPN VLGIIPYAGI DLAVYETLKN
     RWLQQYSHES ANPGILVLLG CGTISSTCGQ IASYPLALVR TRMQAQASIE GGPQVSMVGL
     LRHILSQEGV WGLYRGIAPN FMKVIPAVSI SYVVYENMKQ ALGVTSR
//
ID   Q6GQT3_MOUSE            Unreviewed;       835 AA.
AC   Q6GQT3;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 36.
DE   SubName: Full=2010300C02Rik protein;
GN   Name=2010300C02Rik;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
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DR   EMBL; BC072639; AAH72639.1; -; mRNA.
DR   IPI; IPI00454053; -.
DR   RefSeq; NP_082372.1; NM_028096.1.
DR   UniGene; Mm.142607; -.
DR   PhosphoSite; Q6GQT3; -.
DR   PRIDE; Q6GQT3; -.
DR   Ensembl; ENSMUST00000061505; ENSMUSP00000060549; ENSMUSG00000026090.
DR   Ensembl; ENSMUST00000162875; ENSMUSP00000123803; ENSMUSG00000026090.
DR   GeneID; 72097; -.
DR   KEGG; mmu:72097; -.
DR   MGI; MGI:1919347; 2010300C02Rik.
DR   eggNOG; roNOG14562; -.
DR   GeneTree; ENSGT00530000064039; -.
DR   InParanoid; Q6GQT3; -.
DR   OrthoDB; EOG4V4378; -.
DR   ArrayExpress; Q6GQT3; -.
DR   Bgee; Q6GQT3; -.
DR   Genevestigator; Q6GQT3; -.
PE   1: Evidence at protein level;
SQ   SEQUENCE   835 AA;  89378 MW;  84AB40A5785393A7 CRC64;
     MDIKLREAAE GLGEDGAGKK KSKFKTFKKL FGKKKRKESP SPTGNSAWKQ NPAKSEVIAV
     EESGPVYDSE DELEESRGTM GSRALSHDSI FFPESGQDPA RPVRVFSQEN ACDRIKALQL
     KIQCNVKMGP PPPGGLPIKR AEETGMSSED DGLPRSPPEM SLLHDVGPGT TIKILVSSSR
     PQSPDHMSDA SISSRTLDGS LAPVVDFSHP PEFSSCLDNS AAKHKLLVKP RNQRSSKLRR
     LSSRAQSECL SDLSWTLDEE DYEEKPLLHV SMEETPDARQ RDLIPGRRPE FGGPATFLSP
     GGACARRARL QHSMAVSASM EEGGCPRDEP SSLPATPEVT EPMVVSVPSL ESPSLPESSP
     NHILHSKSQK EELSPGGLCP LVESTSEEAP CGSGVAETPL STDVPERDMG PSKEGSAPPE
     GDPAFSERHM AFPGGGSIPP EGNTTPHKGV MEPPERDMSP SKDNMAPPKR IIAPPERDML
     PSEGDVAPPK RIMAPPERDM SPPEGDVAPP KKIMAPPERD MSPPEGDVAP PKKIMAPPER
     DMSPPEGDVA PPKKIMAPPE RDMSPSEGDV APPKKIMAPP ERDMSPPEGD VAPPKKIMAP
     PERDLSPSEG DVAPPKRIMA PPERDMSPFK GDMAPPKGIM EPPNRDTSLP KGDTPPPETI
     TDTNLETPSD TERQDQSVQK EEELTLVVVP RPEGVGTESS TAPAPSPPVP KSCLKHKALV
     TSGSPAESPL KEPGPAVQDK AVVPPARPRP TQAATSGGPE RTALGRKNER SAEPQRSSVK
     RFSVTSSRAR ARVSGSRLPE YSAHVPAGGR APLLRSGLAW KSEAALDDLQ VLPKP
//
ID   T151A_MOUSE             Reviewed;         468 AA.
AC   Q6GQT5;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Transmembrane protein 151A;
GN   Name=Tmem151a; Synonyms=Gm961, Tmem151;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 404-413, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the TMEM151 family.
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DR   EMBL; AK163651; BAE37438.1; -; mRNA.
DR   EMBL; BC072634; AAH72634.1; -; mRNA.
DR   IPI; IPI00378361; -.
DR   RefSeq; NP_001001885.1; NM_001001885.1.
DR   UniGene; Mm.329663; -.
DR   ProteinModelPortal; Q6GQT5; -.
DR   PRIDE; Q6GQT5; -.
DR   Ensembl; ENSMUST00000077066; ENSMUSP00000076321; ENSMUSG00000061451.
DR   GeneID; 381199; -.
DR   KEGG; mmu:381199; -.
DR   UCSC; uc008gcc.1; mouse.
DR   CTD; 381199; -.
DR   MGI; MGI:2147713; Tmem151a.
DR   eggNOG; maNOG16089; -.
DR   GeneTree; ENSGT00390000013762; -.
DR   HOGENOM; HBG444651; -.
DR   HOVERGEN; HBG108535; -.
DR   InParanoid; Q6GQT5; -.
DR   OMA; PRTDANT; -.
DR   OrthoDB; EOG45756K; -.
DR   PhylomeDB; Q6GQT5; -.
DR   NextBio; 401706; -.
DR   ArrayExpress; Q6GQT5; -.
DR   Bgee; Q6GQT5; -.
DR   CleanEx; MM_TMEM151A; -.
DR   Genevestigator; Q6GQT5; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    468       Transmembrane protein 151A.
FT                                /FTId=PRO_0000282987.
FT   TRANSMEM     45     65       Helical; (Potential).
FT   TRANSMEM     98    118       Helical; (Potential).
SQ   SEQUENCE   468 AA;  51312 MW;  0067ED7B07FAAF65 CRC64;
     MPEGEGGDCG EVPALVPDGE PLREEQRPLK QSLGGSLCRE SHWKCLLLTL LIHACGAVVA
     WCRLATVPRL VLGPEAALAR GAGGPPPTYP ASPCSDGYLY IPLAFVSLLY LLYLAECWHC
     HVRSCQAPRT DANTVLALIH RLQQAPPCVW WKATSYHYVR RTRQITRYRN GDAYTTTQVY
     HERADSRTAR GEFDYSAHGV RDVSKELVGL ADHAATRLRF TKCFSFGSAE AEASYLTQRA
     RFFSANEGLD DYLEAREGMH LKDVDFRESL MVFADPRSPP WYARAWVFWL VSAATLSWPL
     RVVAAYGTAH VHYQVEKLFG ASSPPPGAVP SGPPLSRVAT VDFTELEWHI CSNRQLVPSY
     SEAVVMGASS GAYLRGCQRC RRSVSSNSLP PARPSGPRLP FSRSRLSLGA GGRTTPGVFR
     SLSGGPLGRR GEDTEPLESP PCYEDALYFP VLIVHGDSGC RGDGQGAL
//
ID   SCAP_MOUSE              Reviewed;        1276 AA.
AC   Q6GQT6; Q6A0A6; Q6NS67; Q7TNG7; Q80UI6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Sterol regulatory element-binding protein cleavage-activating protein;
DE            Short=SCAP;
DE            Short=SREBP cleavage-activating protein;
GN   Name=Scap; Synonyms=Kiaa0199;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic heart, and Macrophage;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, Colon, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, AND MUTAGENESIS OF ASP-443.
RX   PubMed=9854040; DOI=10.1172/JCI5341;
RA   Korn B.S., Shimomura I., Bashmakov Y., Hammer R.E., Horton J.D.,
RA   Goldstein J.L., Brown M.S.;
RT   "Blunted feedback suppression of SREBP processing by dietary
RT   cholesterol in transgenic mice expressing sterol-resistant
RT   SCAP(D443N).";
RL   J. Clin. Invest. 102:2050-2060(1998).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11358865; DOI=10.1101/gad.891301;
RA   Matsuda M., Korn B.S., Hammer R.E., Moon Y.-A., Komuro R.,
RA   Horton J.D., Goldstein J.L., Brown M.S., Shimomura I.;
RT   "SREBP cleavage-activating protein (SCAP) is required for increased
RT   lipid synthesis in liver induced by cholesterol deprivation and
RT   insulin elevation.";
RL   Genes Dev. 15:1206-1216(2001).
CC   -!- FUNCTION: Escort protein required for cholesterol as well as lipid
CC       homeostasis. Regulates export of the SCAP/SREBF complex from the
CC       ER upon low cholesterol. Formation of a ternary complex with INSIG
CC       at high sterol concentrations leads to masking of an ER-export
CC       signal in SCAP and retention of the complex in the ER. Low sterol
CC       concentrations trigger release of INSIG, a conformational change
CC       in the SSC domain of SCAP, unmasking of the ER export signal,
CC       recruitment into COPII-coated vesicles, transport to the Golgi
CC       complex, proteolytic cleavage of SREBF in the Golgi, release of
CC       the transcription factor fragment of SREBF from the membrane, its
CC       import into the nucleus and up-regulation of LDLR, INSIG1 and the
CC       mevalonate pathway.
CC   -!- SUBUNIT: Membrane region forms a homotetramer. Forms a stable
CC       complex with SREBF1/SREBP1 or SREBF2/SREBP2 through its C-terminal
CC       cytoplasmic domain. Forms a ternary complex with INSIG1 or INSIG2
CC       through its transmembrane domains at high sterol concentrations.
CC       Interacts with the SEC23/SEC24 complex in a SAR1-GTP-dependent
CC       manner through an ER export signal in its third cytoplasmic loop.
CC       Binds cholesterol through its SSC domain. Component of SCAP/SREBP
CC       complex composed of SREBF2, SCAP and RNF139; the complex hampers
CC       the interaction between SCAP and SEC24B, thereby reducing SREBF2
CC       proteolytic processing. Interacts with RNF139; the interaction
CC       inhibits the interaction of SCAP with SEC24B and hampering the ER
CC       to Golgi transport of the SCAP/SREBP complex (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity). Golgi apparatus membrane; Multi-
CC       pass membrane protein (By similarity). Cytoplasmic vesicle, COPII-
CC       coated vesicle membrane; Multi-pass membrane protein (By
CC       similarity). Note=Moves from the endoplasmic reticulum to the
CC       Golgi in the absence of sterols (By similarity).
CC   -!- DOMAIN: Cholesterol bound to SSC domain of SCAP or oxysterol bound
CC       to INSIG1/2 leads to masking of an ER export signal on SCAP
CC       possibly by moving the signal further away from the ER membrane
CC       (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice lacking Scap in their liver show an 80%
CC       reduction in cholesterol and fatty acid synthesis in the liver as
CC       well as a lack of regulation of target gene expression in response
CC       to cholesterol deprivation or insulin elevation. Mice expressing
CC       dominant negative mutant Scap in their liver show higher levels of
CC       mature Srebf1 and Srebf2 as well as transcripts encoding proteins
CC       involved in uptake and synthesis of cholesterol and fatty acids.
CC       They show an 1.6-fold increase in liver size as well as a six-fold
CC       increase in cholesterol and a nine-fold increase in triglyceride
CC       content of the liver. Their plasma levels of cholesterol and
CC       triglycerides are reduced by 50%. They show reduced down-
CC       regulation of mature Srebf1/2 when fed a high cholesterol diet.
CC   -!- SIMILARITY: Belongs to the WD repeat SCAP family.
CC   -!- SIMILARITY: Contains 1 SSD (sterol-sensing) domain.
CC   -!- SIMILARITY: Contains 7 WD repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32190.1; Type=Erroneous initiation;
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DR   EMBL; AK172912; BAD32190.1; ALT_INIT; Transcribed_RNA.
DR   EMBL; AK146658; BAE27338.1; -; mRNA.
DR   EMBL; AK150275; BAE29431.1; -; mRNA.
DR   EMBL; AK152478; BAE31252.1; -; mRNA.
DR   EMBL; AK153330; BAE31909.1; -; mRNA.
DR   EMBL; BC051066; AAH51066.1; -; mRNA.
DR   EMBL; BC055472; AAH55472.1; -; mRNA.
DR   EMBL; BC069955; AAH69955.1; -; mRNA.
DR   EMBL; BC070437; AAH70437.1; -; mRNA.
DR   EMBL; BC072633; AAH72633.1; -; mRNA.
DR   IPI; IPI00856221; -.
DR   RefSeq; NP_001001144.2; NM_001001144.2.
DR   RefSeq; NP_001096632.1; NM_001103162.1.
DR   UniGene; Mm.288741; -.
DR   ProteinModelPortal; Q6GQT6; -.
DR   SMR; Q6GQT6; 771-812, 960-1269.
DR   STRING; Q6GQT6; -.
DR   PhosphoSite; Q6GQT6; -.
DR   PRIDE; Q6GQT6; -.
DR   Ensembl; ENSMUST00000098350; ENSMUSP00000095953; ENSMUSG00000032485.
DR   GeneID; 235623; -.
DR   KEGG; mmu:235623; -.
DR   NMPDR; fig|10090.3.peg.20923; -.
DR   CTD; 235623; -.
DR   MGI; MGI:2135958; Scap.
DR   eggNOG; roNOG04757; -.
DR   GeneTree; ENSGT00390000000003; -.
DR   HOGENOM; HBG402990; -.
DR   HOVERGEN; HBG019538; -.
DR   InParanoid; Q6GQT6; -.
DR   OMA; RLPPEAC; -.
DR   OrthoDB; EOG42Z4PB; -.
DR   PhylomeDB; Q6GQT6; -.
DR   NextBio; 382797; -.
DR   ArrayExpress; Q6GQT6; -.
DR   Bgee; Q6GQT6; -.
DR   CleanEx; MM_SCAP; -.
DR   Genevestigator; Q6GQT6; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR   GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015485; F:cholesterol binding; TAS:MGI.
DR   GO; GO:0008203; P:cholesterol metabolic process; IDA:MGI.
DR   GO; GO:0045540; P:regulation of cholesterol biosynthetic process; IMP:MGI.
DR   GO; GO:0042304; P:regulation of fatty acid biosynthetic process; IMP:MGI.
DR   GO; GO:0001666; P:response to hypoxia; IMP:MGI.
DR   GO; GO:0032868; P:response to insulin stimulus; IMP:MGI.
DR   InterPro; IPR000731; SSD.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 3.
DR   Pfam; PF00400; WD40; 4.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40_like; 2.
DR   PROSITE; PS50156; SSD; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Cholesterol metabolism; Cytoplasmic vesicle; Endoplasmic reticulum;
KW   Glycoprotein; Golgi apparatus; Lipid metabolism; Membrane;
KW   Phosphoprotein; Repeat; Steroid metabolism; Transmembrane;
KW   Transmembrane helix; WD repeat.
FT   CHAIN         1   1276       Sterol regulatory element-binding protein
FT                                cleavage-activating protein.
FT                                /FTId=PRO_0000315870.
FT   TOPO_DOM      1     18       Cytoplasmic (By similarity).
FT   TRANSMEM     19     39       Helical; Name=1; (Potential).
FT   TOPO_DOM     40    279       Lumenal (By similarity).
FT   TRANSMEM    280    300       Helical; Name=2; (Potential).
FT   TOPO_DOM    301    312       Cytoplasmic (By similarity).
FT   TRANSMEM    313    333       Helical; Name=3; (Potential).
FT   TOPO_DOM    334    344       Lumenal (By similarity).
FT   TRANSMEM    345    365       Helical; Name=4; (Potential).
FT   TOPO_DOM    366    401       Cytoplasmic (By similarity).
FT   TRANSMEM    402    422       Helical; Name=5; (Potential).
FT   TOPO_DOM    423    423       Lumenal (By similarity).
FT   TRANSMEM    424    444       Helical; Name=6; (Potential).
FT   TOPO_DOM    445    518       Cytoplasmic (By similarity).
FT   TRANSMEM    519    539       Helical; Name=7; (Potential).
FT   TOPO_DOM    540    707       Lumenal (By similarity).
FT   TRANSMEM    708    728       Helical; Name=8; (Potential).
FT   TOPO_DOM    729   1276       Cytoplasmic (By similarity).
FT   DOMAIN      284    442       SSD.
FT   REPEAT      771    811       WD 1.
FT   REPEAT      949    999       WD 2.
FT   REPEAT     1002   1039       WD 3.
FT   REPEAT     1074   1111       WD 4.
FT   REPEAT     1114   1152       WD 5.
FT   REPEAT     1155   1192       WD 6.
FT   REPEAT     1194   1232       WD 7.
FT   REGION      447    452       ER export signal (By similarity).
FT   REGION      731   1276       Interaction with SREBF2 (By similarity).
FT   MOD_RES     243    243       Phosphotyrosine (By similarity).
FT   MOD_RES     850    850       Phosphoserine (By similarity).
FT   MOD_RES     905    905       Phosphoserine (By similarity).
FT   CARBOHYD    263    263       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    590    590       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    641    641       N-linked (GlcNAc...) (Potential).
FT   MUTAGEN     443    443       D->N: Higher level of processed SREBF1
FT                                and SREBF2 when expressed in liver.
FT   CONFLICT    247    247       Missing (in Ref. 1; BAD32190).
FT   CONFLICT    619    619       P -> L (in Ref. 3; AAH70437).
SQ   SEQUENCE   1276 AA;  139611 MW;  4EE7DDCEEB6F3331 CRC64;
     MTLTERLREK ISQAFYNHGL LCASYPIPII LFTGLCILAC CYPLLKLPLP GTGPVEFSTP
     VKGYSPPPAD SDHKQGEPSE QPEWYVGAPV AYIQQIFVKS SVSPWHRNLL AVDVFRSPLS
     RAFQLVEEIR NHVLRDSSGT KSLEEVCLQV TDLLPGLRKL RSLLPEHGCL LLSPGNFWQN
     DWERFHADPD IIGTIHQHEP KTLQTSATLK DLLFGVPGKY SGVSLYTRKR MVSYTITLVF
     QRYHAKFLSS LRARLMLLHP SPNCSLRAEN LVHVHFKEEI GIAELIPLVT TYIILFAYIY
     FSTRKIDMVK SKWGLALAAV VTVLSSLLMS VGLCTLFGLT PTLNGGEIFP YLVVVIGLEN
     VLVLTKSVVS TPVDLEVKLR IAQGLSSESW SIMKNAATEL GIILIGYFTL VPAIQEFCLF
     AVVGLVSDFF LQMLFFTTVL SIDIRRMELA DLNKRLPPES CLPSAKPVGR PARYERQQAV
     RPSTPHTITL QPSSFRNLRL PKRLRVIYFL ARTRLAQRLI MAGTVVWIGI LVYTDPAGLR
     TYLAAQVTEQ SPLGEGSLGP MPVPSGVLPA SHPDPAFSIF PPDAPKLPEN QTLPGELPEH
     AGPAEGVHDS RAPEVTWGPE DEELWRKLSF RHWPTLFNYY NITLAKRYIS LLPVIPVTLH
     LNPREALEGR HPQDGRSAWA PQEPLPAGLW ESGPKGPGGT QTHGDITLYK VAALGLAAGI
     VLVLLLLCLY RVLCPRNYGQ PGGGPGRRRR GELPCDDYGY APPETEIVPL VLRGHLMDIE
     CLASDGMLLV SCCLAGQVCV WDAQTGDCLT RIPRPGPRRD SCGGGAFETQ ENWERLSDGG
     KASPEEPGDS PPLRRRPRGP PPPSLFGDQP DLTCLIDTNF SVQLPPEPTQ PEPRHRVGCG
     RSRDSGYDFS RLVQRVYQEE GLAAMRMPAL RPPSPGPPLP QASQEEGTAP EKGSPPLAWT
     PSTAGSIWSL ELQGNLIVVG RSSGRLEVWD AIEGVLCCSN EEISSGITAL VFLDRRIVAA
     RLNGSLDFFS LETHTSLSPL QFRGTPGRGS SPSSSVYSSS NTVTCHRTHT VPCAHQKPIT
     ALRAAAGRLV TGSQDHTLRV FRLDDSCCLF TLKGHSGAIT AVYIDQTMVL ASGGQDGAIC
     LWDVLTGSRV SQTFAHRGDV TSLTCTASCV ISSGLDDFIS IWDRSTGIKL YSIQQDLGCG
     ASLGVISDNL LVTGGQGCVS FWDLNYGDLL QTVYLGKNSE AQPARQILVL DNAAIVCNFG
     SELSLVYVPS VLEKLD
//
ID   BTBDB_MOUSE             Reviewed;        1109 AA.
AC   Q6GQW0; Q6PCZ7; Q8CAD2; Q8CDA2; Q9D3B9;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 2.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Ankyrin repeat and BTB/POZ domain-containing protein BTBD11;
DE   AltName: Full=BTB/POZ domain-containing protein 11;
GN   Name=Btbd11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 515-1109 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus, Medulla oblongata, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q6GQW0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6GQW0-2; Sequence=VSP_032805, VSP_032807;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q6GQW0-3; Sequence=VSP_032804;
CC       Name=4;
CC         IsoId=Q6GQW0-4; Sequence=VSP_032806, VSP_032808;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 5 ANK repeats.
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK018115; BAB31077.1; -; mRNA.
DR   EMBL; AK039038; BAC30216.1; -; mRNA.
DR   EMBL; AK030864; BAC27162.1; -; mRNA.
DR   EMBL; BC059036; AAH59036.1; -; mRNA.
DR   EMBL; BC072592; AAH72592.1; -; mRNA.
DR   EMBL; BC096535; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00224296; -.
DR   IPI; IPI00474324; -.
DR   IPI; IPI00556801; -.
DR   IPI; IPI00875861; -.
DR   RefSeq; NP_001017525.1; NM_001017525.1.
DR   RefSeq; NP_082985.2; NM_028709.2.
DR   UniGene; Mm.36544; -.
DR   ProteinModelPortal; Q6GQW0; -.
DR   SMR; Q6GQW0; 199-252, 584-759, 921-1071.
DR   PhosphoSite; Q6GQW0; -.
DR   PRIDE; Q6GQW0; -.
DR   Ensembl; ENSMUST00000020231; ENSMUSP00000020231; ENSMUSG00000020042.
DR   Ensembl; ENSMUST00000038045; ENSMUSP00000035917; ENSMUSG00000020042.
DR   Ensembl; ENSMUST00000105306; ENSMUSP00000100943; ENSMUSG00000020042.
DR   Ensembl; ENSMUST00000105307; ENSMUSP00000100944; ENSMUSG00000020042.
DR   GeneID; 74007; -.
DR   KEGG; mmu:74007; -.
DR   CTD; 74007; -.
DR   MGI; MGI:1921257; Btbd11.
DR   GeneTree; ENSGT00550000074669; -.
DR   HOGENOM; HBG444734; -.
DR   HOVERGEN; HBG050447; -.
DR   InParanoid; Q6GQW0; -.
DR   OMA; EDEYTEE; -.
DR   OrthoDB; EOG4NS39X; -.
DR   NextBio; 339514; -.
DR   ArrayExpress; Q6GQW0; -.
DR   Bgee; Q6GQW0; -.
DR   Genevestigator; Q6GQW0; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR013069; BTB_POZ.
DR   InterPro; IPR009072; Histone-fold.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 2.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Gene3D; G3DSA:1.10.20.10; Histone-fold; 3.
DR   Pfam; PF00023; Ank; 3.
DR   Pfam; PF00651; BTB; 1.
DR   SMART; SM00248; ANK; 4.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   SUPFAM; SSF47113; Histone-fold; 2.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
DR   PROSITE; PS50097; BTB; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ANK repeat; Membrane; Repeat; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   1109       Ankyrin repeat and BTB/POZ domain-
FT                                containing protein BTBD11.
FT                                /FTId=PRO_0000328828.
FT   TRANSMEM    168    188       Helical; (Potential).
FT   REPEAT      608    637       ANK 1.
FT   REPEAT      654    683       ANK 2.
FT   REPEAT      692    721       ANK 3.
FT   REPEAT      735    764       ANK 4.
FT   REPEAT      830    859       ANK 5.
FT   DOMAIN      928    994       BTB.
FT   COMPBIAS    338    346       His-rich.
FT   VAR_SEQ       1    926       Missing (in isoform 3).
FT                                /FTId=VSP_032804.
FT   VAR_SEQ       1    862       Missing (in isoform 2).
FT                                /FTId=VSP_032805.
FT   VAR_SEQ       1    723       Missing (in isoform 4).
FT                                /FTId=VSP_032806.
FT   VAR_SEQ     863    882       TEELVTQGLPLMFEILKASK -> MVRTKDLLPEFENIDKG
FT                                GWR (in isoform 2).
FT                                /FTId=VSP_032807.
FT   VAR_SEQ     918   1109       DPHFLNNKEMSDVTFLVEGRPFYAHKVLLFTASPRFKALLS
FT                                SKPTNDNTCIEIGYVKYPIFQLVMQYLYYGGPESLLIKNNE
FT                                IMELLSAAKFFQLEALQRHCEIICAKSINTDNCVDIYSHAK
FT                                FLGVTELSAYCEGYFLKNMMVLIENEAFKQLLYDKNGEGAG
FT                                QDVLQDLQRTLAIRIQSIHLSSSKGSVV -> GEQWSGYTQ
FT                                AMAVGSGDGKEANMWNRYRM (in isoform 4).
FT                                /FTId=VSP_032808.
FT   CONFLICT    515    515       R -> G (in Ref. 1; BAC30216).
SQ   SEQUENCE   1109 AA;  121561 MW;  8BDB3F0A03E670AD CRC64;
     MARRGKKPVV RTLEDLTLDS GYGGAADSVR SSNLSLCCSD SHPASPYGGS CWPPLADSMH
     SRHNSFDTVN TALVEDSEGL DCAGQHCSRL LPDLDEVPWT LQELELLLLR SRDPRAGPAV
     PGSLPKDALA KLSMLVSRAL VRIAKEAQRL SLRFAKCTKY EIQSAMEIVL SWGLAAHCTA
     AALAALSLYN MSSAGGDRLG RGKSARCGLT FSVGRVYRWM VDSRVALRIH EHAAIYLTAC
     MESLFRDIYS RVLASGLPRS CSGPGPGSSS GSGPGPGSGP GAPAADKERE TPGGGAASGG
     PCSAASSASG GSSCCAPPAT AATAVPPTTA TAAVAANHHH HHHTLHEAPK FTVETLEHTV
     NNDSEIWGLL QPYQHLICGK NASGVLSLPE SLNLHRDPQR PSKPGELPMF SQSELRTIEQ
     SLLATRVGSI AELSDLVSRA MHHLQPLNAK HHGNGTPMHH KQGALYWEPE ALYTLCYFMH
     CPQMEWENPN VEPSKVNLQV ERPFLVLPPL MEWIRVAVAH AGHRRSFSMD SDDVRQAARL
     LLPGVDCEPR QLKADDCFCA SRKLDAVAIE AKFKQDLGFR MLNCGRTDLV KQAVSLLGPD
     GINTMSEQGM TPLMYACVRG DEAMVQMLLD AGADLNVEVV STPHKYPSVH PETRHWTALT
     FAVLHGHIPV VQLLLDAGAK VEGSVEHGEE NYSETPLQLA AAVGNFELVS LLLERGADPL
     IGTMYRNGIS TTPQGDMNSF SQAAAHGHRN VFRKLLAQPE KEKSDILSLE EILAEGTDLA
     ETAPPPLCAS RNSKAKLRAL REAMYHSAEH GYVDVTIDIR SIGVPWTLHT WLESLRIAFQ
     QHRRPLIQCL LKEFKTIQEE EYTEELVTQG LPLMFEILKA SKNEVISQQL CVIFTHCYGP
     YPIPKLTEIK RKQTSRLDPH FLNNKEMSDV TFLVEGRPFY AHKVLLFTAS PRFKALLSSK
     PTNDNTCIEI GYVKYPIFQL VMQYLYYGGP ESLLIKNNEI MELLSAAKFF QLEALQRHCE
     IICAKSINTD NCVDIYSHAK FLGVTELSAY CEGYFLKNMM VLIENEAFKQ LLYDKNGEGA
     GQDVLQDLQR TLAIRIQSIH LSSSKGSVV
//
ID   NCK5L_MOUSE             Reviewed;        1323 AA.
AC   Q6GQX2; Q8BX75; Q8R364;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 44.
DE   RecName: Full=Nck-associated protein 5-like;
GN   Name=Nckap5l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 752-1323.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC026468; AAH26468.1; -; mRNA.
DR   EMBL; BC072572; AAH72572.1; -; mRNA.
DR   EMBL; AK048721; BAC33433.1; -; mRNA.
DR   IPI; IPI00381148; -.
DR   RefSeq; NP_001001884.1; NM_001001884.1.
DR   UniGene; Mm.22915; -.
DR   ProteinModelPortal; Q6GQX2; -.
DR   PhosphoSite; Q6GQX2; -.
DR   PRIDE; Q6GQX2; -.
DR   Ensembl; ENSMUST00000023747; ENSMUSP00000023747; ENSMUSG00000023009.
DR   GeneID; 380969; -.
DR   KEGG; mmu:380969; -.
DR   UCSC; uc007xpn.1; mouse.
DR   CTD; 380969; -.
DR   MGI; MGI:3609653; Nckap5l.
DR   eggNOG; roNOG09665; -.
DR   GeneTree; ENSGT00530000063607; -.
DR   HOGENOM; HBG755250; -.
DR   HOVERGEN; HBG080689; -.
DR   InParanoid; Q6GQX2; -.
DR   OMA; VSPCYEN; -.
DR   OrthoDB; EOG412M4N; -.
DR   PhylomeDB; Q6GQX2; -.
DR   NextBio; 401437; -.
DR   ArrayExpress; Q6GQX2; -.
DR   Bgee; Q6GQX2; -.
DR   CleanEx; MM_C230021P08RIK; -.
DR   Genevestigator; Q6GQX2; -.
PE   2: Evidence at transcript level;
KW   Coiled coil; Phosphoprotein.
FT   CHAIN         1   1323       Nck-associated protein 5-like.
FT                                /FTId=PRO_0000288448.
FT   COILED       22    109       Potential.
FT   COILED      942    985       Potential.
FT   COMPBIAS    112    613       Pro-rich.
FT   COMPBIAS    781    871       Pro-rich.
FT   COMPBIAS   1120   1257       Pro-rich.
FT   MOD_RES     436    436       Phosphoserine (By similarity).
FT   MOD_RES     447    447       Phosphoserine (By similarity).
FT   MOD_RES     473    473       Phosphoserine (By similarity).
FT   MOD_RES     489    489       Phosphoserine (By similarity).
FT   MOD_RES     492    492       Phosphoserine (By similarity).
FT   MOD_RES     494    494       Phosphoserine (By similarity).
FT   MOD_RES     573    573       Phosphoserine (By similarity).
FT   MOD_RES     760    760       Phosphoserine (By similarity).
FT   CONFLICT    752    752       A -> S (in Ref. 2; BAC33433).
FT   CONFLICT   1100   1100       T -> A (in Ref. 1; AAH26468).
SQ   SEQUENCE   1323 AA;  138170 MW;  944DCC62EB77EEF7 CRC64;
     MDQPAGGTGK LRASAGEDDS MELSTCQELL HRLRELEAEN SALAQANENQ RETYERCLDE
     VANHVVQALL NQKDLREECI KLKKRVFDLE RQNQVLSALL QQKLQLTANS LPQIPLTPLQ
     PPSERPTSPA PNVSEGPATS LPSGLCAGQR EVCWEQQLRP GGPGPPATPP PALDALSPFL
     RKKAQILEVL RALEETDPLL LCSPATPWRP TGQGPGSPEP INGEPCGPPQ PEPSPWAPYL
     LLGPGSLGAL LHWERVLGGP GEEEGIRQPW ASSRAPPSAQ GPSSGPHCAP GSSSSSSSDE
     AGDPNEAPSP DTLLGALARK QLNLGQLLGD TETYLQAFLA GATGPLSGDQ PGPGKPNSPD
     PGPPQVSKSK GLPKSAWGAS TPEATRLGFG ATSEGQGPLP FLSMFMGAGD APLGSRPGHP
     HSSSQVKSKL QIGPPSPGDA QGPLLPSPAR GLKFLKLPPA SEKVPSPGGP QLSPQLPRSS
     RIPCRNSGSD GSPSPLLARR GLGGGELSPE GAQGLPGSPL PCSAMPDSAQ LRPSQSTVST
     ALSPGPVVSP CFENILDLSR STFRGSPPEP PPSPLQVPTY PQLTLEVPQT PEVLRSPGAP
     SPGLPESCPY SGPQEKSMDR AGSESPHASR RTPGGSSKKP GQGSGRRPGD PSHTPLRDRL
     AALGKLKTGP EGPLGPEKNG VPARSSAEKA RALVRSGECA GDVPPSARPL EQPEAKGIFR
     GAVALGTSSL KQQEPGLTDP GARVYSSHSM GARVDLEPIS PRSCLTKVEL AKSRLAGALC
     PQMPRTPAKV PTSAPSLGKP KSPHSSPTKL PSKSPTKVVP RPVVPLGTKE PPKPDKVKGP
     PWADCGSTVG QPTSPVAGPA DPSQGSEGPA PHSAIEEKVM KGIEENVLRL QGQERTPGSE
     AKHRNTSSIA SWFGLKKSKL PALNRRTEAT KNKDGAGGGS PLRKEVKTEA RKLEAESLNI
     SKLMAKAEDL RRALEEEKAY LSRARPRPGG PATVPSPGLG QAQGQLAGMY QGADTFMQQL
     LNRVDGKELP PKSWREPKPE YGDFQPVSTD PKSPWPACGP RNGLVGPLQG CGKPGKPSSE
     PGRREEMPSE DSLAEPVSTT HFTACGSLTR TLDSGIGTFP PPDHSSSGTP SKNLPKTKSL
     RLDPPPGAPP ARPPGLTKVP RRAHTLEREV PGIEELLVSG RHPSMPAFPG LLTAPPGHRS
     HQTCPDDPCE DPGPPPPVQL AKNWTFPNTR TAGSSSDPFL CPPRQLEGLP RTPMALPVDR
     KQSVDPSRTS TPQGPAFGGS RTPSTSDMGE EGRVASGGAP GLETSESLSD SLYDSLSSCG
     SQG
//
ID   Q6GQX8_MOUSE            Unreviewed;      1014 AA.
AC   Q6GQX8;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   08-FEB-2011, entry version 35.
DE   SubName: Full=AU042671 protein;
DE   Flags: Fragment;
GN   Name=Gm15800; Synonyms=AU042671;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC072559; AAH72559.1; -; mRNA.
DR   IPI; IPI00881027; -.
DR   UniGene; Mm.184589; -.
DR   UniGene; Mm.481359; -.
DR   ProteinModelPortal; Q6GQX8; -.
DR   PRIDE; Q6GQX8; -.
DR   Ensembl; ENSMUST00000100769; ENSMUSP00000098332; ENSMUSG00000042744.
DR   UCSC; uc008zis.1; mouse.
DR   MGI; MGI:3647820; Gm15800.
DR   eggNOG; maNOG06444; -.
DR   GeneTree; ENSGT00600000084546; -.
DR   OMA; KINAMER; -.
DR   ArrayExpress; Q6GQX8; -.
DR   Bgee; Q6GQX8; -.
DR   Genevestigator; Q6GQX8; -.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   1014 AA;  110198 MW;  D7C92097E471B946 CRC64;
     LNLVDALQSL INFQYQEEHA EEYDLLCKIM GETFKKLNAM ERQLQSVAEL EQKWQSEAED
     AMQGKLENNM PFFYDYHFNE NKMKELELLC SMKEVSFDGN DLENMVLSLR EKFLQEVNSL
     AQKPSHPLAK TKTLVRSLMN RAELLLHVTI AAQAGLTRSI SGTPAETPAC KSASETKVAS
     HAVRQPVFLR SMSAPSDLEM IGNEDLEFTR ANQRRRHVTS HRSSSFTLLQ SLAIEDSRDK
     PTYSVLLGQL FAFIGTNPDQ AVSSSSFLLA AQTRWRRGNT RKQALVHMRE LLTAAVRVGG
     VTHLVGPVTM VLQGGPRIEE LTCGGMVEQV QEAFGETMTS VVSLCARYPI ACANSIGLLC
     TIPYTRSEEK CLVRSGLVQL MDRLCSLSSQ TESSSSEKQT KKQKVATMAW AAFQVLANRC
     VEWEKEEGGS TEAVHSGLAR QVSSLLTNHL ARATECCGNQ AAGNDALQDV LSLLNDLSRS
     HIGKAILSQP ACVSKLLSLL LDQRPSPKLV LIILQLCRAA LPLMSVEDCG NVELPPWSYS
     VPSLNSEQED PSDPASKIAS LLLAKLADYV VPGCQTVLSP TASEPDTTLT KTSPKNSLKG
     DKDPGEESEA VDGKLSIFIH KREDQSSHEV LQPLLSSSEG RPFRLGTGAN MEKVVKMDRD
     MTKGGCCEVI TEEASAALRK ATKWAQSGLI VSVGPPVESI NPETVSGLST GDKKKTAQTS
     ICRERNSELA RTDPVRPFIS GHVANSMAAE VIALLHSLLM APESNAAQIW TTTAEKVLSR
     ALMYIPQLGK YAESILENGS SSGRKLAKLQ RIARQAVAAL CALGGFKETI KIGSEVQVLG
     RGISGSIGVV ASINEQEGIA TVRFPPVDCR RTSQAADTLT IPLSRLCVPR SEALPLHKLS
     ITEKVVQAVQ SMLLPQEGSL SIHTSLPATG DGSAPVMAVV RLLAEIRTRA CLVMAQLLED
     SLFCEEFIQQ CPAAVEVLNL VAQECSAGSE FKSQQPHGGS QPSVMRSDAL FWCV
//
ID   Q6GT24_MOUSE            Unreviewed;       224 AA.
AC   Q6GT24;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   08-FEB-2011, entry version 61.
DE   SubName: Full=Peroxiredoxin 6;
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Prdx6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body, and Parthenogenote;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body, and Parthenogenote;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body, and Parthenogenote;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body, and Parthenogenote;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body, and Parthenogenote;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body, and Parthenogenote;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body, and Parthenogenote;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Parthenogenote;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC061181; AAH61181.1; -; mRNA.
DR   EMBL; AK157820; BAE34210.1; -; mRNA.
DR   EMBL; AK161710; BAE36544.1; -; mRNA.
DR   IPI; IPI00758024; -.
DR   RefSeq; NP_031479.1; NM_007453.3.
DR   UniGene; Mm.186185; -.
DR   ProteinModelPortal; Q6GT24; -.
DR   SMR; Q6GT24; 5-224.
DR   STRING; Q6GT24; -.
DR   PeroxiBase; 4425; Mm1CysPrx.
DR   PRIDE; Q6GT24; -.
DR   Ensembl; ENSMUST00000071718; ENSMUSP00000071636; ENSMUSG00000026701.
DR   GeneID; 11758; -.
DR   KEGG; mmu:11758; -.
DR   UCSC; uc007dfl.1; mouse.
DR   CTD; 11758; -.
DR   MGI; MGI:894320; Prdx6.
DR   GeneTree; ENSGT00550000074794; -.
DR   HOVERGEN; HBG105234; -.
DR   InParanoid; Q6GT24; -.
DR   OMA; HPNANDT; -.
DR   PhylomeDB; Q6GT24; -.
DR   NextBio; 279511; -.
DR   ArrayExpress; Q6GT24; -.
DR   Bgee; Q6GT24; -.
DR   Genevestigator; Q6GT24; -.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0004601; F:peroxidase activity; IMP:MGI.
DR   GO; GO:0032060; P:bleb assembly; IMP:MGI.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0000302; P:response to reactive oxygen species; IMP:MGI.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR019479; Peroxiredoxin_C.
DR   InterPro; IPR017936; Thioredoxin-like.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Pfam; PF10417; 1-cysPrx_C; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   224 AA;  24827 MW;  EF88FD923585FC88 CRC64;
     MPGGLLLGDE APNFEANTTI GRIRFHDFLG DSWGILFSHP RDFTPVCTTE LGRAAKLAPE
     FAKRNVKLIA LSIDSVEDHL AWSKDINAYN GETPTEKLPF PIIDDKGRDL AILLGMLDPV
     EKDANNMPVT ARVVFIFGPD KKLKLSILYP ATTGRNFDEI LRVVDSLQLT GTKPVATPVD
     WKKGESVMVV PTLSEEEAKQ CFPKGVFTKE LPSGKKYLRY TPQP
//
ID   Q6GTD3_MOUSE            Unreviewed;       377 AA.
AC   Q6GTD3;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   08-MAR-2011, entry version 34.
DE   SubName: Full=NADH dehydrogenase (Ubiquinone) 1 alpha subcomplex, 9;
GN   Name=Ndufa9; ORFNames=mCG_129735;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC058378; AAH58378.1; -; mRNA.
DR   EMBL; CH466523; EDK99844.1; -; Genomic_DNA.
DR   IPI; IPI00944067; -.
DR   RefSeq; NP_079634.2; NM_025358.3.
DR   UniGene; Mm.29939; -.
DR   ProteinModelPortal; Q6GTD3; -.
DR   STRING; Q6GTD3; -.
DR   Ensembl; ENSMUST00000088194; ENSMUSP00000085523; ENSMUSG00000000399.
DR   GeneID; 66108; -.
DR   KEGG; mmu:66108; -.
DR   CTD; 66108; -.
DR   MGI; MGI:1913358; Ndufa9.
DR   eggNOG; roNOG12817; -.
DR   HOVERGEN; HBG006546; -.
DR   InParanoid; Q6GTD3; -.
DR   OMA; NFDFEDV; -.
DR   ArrayExpress; Q6GTD3; -.
DR   Bgee; Q6GTD3; -.
DR   Genevestigator; Q6GTD3; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR008030; NmrA.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF05368; NmrA; 1.
PE   2: Evidence at transcript level;
KW   Ubiquinone.
SQ   SEQUENCE   377 AA;  42525 MW;  473FA5F2F018AC78 CRC64;
     MAAAVRFRVV RALPMSRPAI TAAATSVFCG SSHRQLHHAV IPHGKGGRSS VSGVVATVFG
     ATGFLGRYVV NHLGRMGSQV IIPYRCDVYD IMHLRLMGDL GQLTFLEWDA RDKDSIRKAV
     QHSNVVINLI GREWETRNFD FEDVFVNIPR AIAQASKEAG VERFIHVSHL NASMKSSSKS
     LRSKAVGEKE VRSVFPEAII IRPSDIFGRE DRFLNHFANY RWFLAVPLVS LGFKTVKQPV
     YVADVSKGIV NATKDPDAVG KTFAFTGPNR YLLFHLVKYI FGMTHRTFIP YPLPLFVYSW
     IGKLFGLSPF EPWTTKDKVE RIHISDVMPT DLPGLEDLGV QPTPLELKSI EVLRRHRTYR
     WLSSEIEETK PAKTVNY
//
ID   Q6GTK8_MOUSE            Unreviewed;      1358 AA.
AC   Q6GTK8;
DT   10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2005, sequence version 1.
DT   08-MAR-2011, entry version 46.
DE   SubName: Full=MutS homolog 6 (E. coli);
GN   Name=Msh6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Limb, and Mammary tumor. C3;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the DNA mismatch repair mutS family.
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DR   EMBL; BC051160; AAH51160.1; -; mRNA.
DR   EMBL; BC051634; AAH51634.1; -; mRNA.
DR   IPI; IPI00310173; -.
DR   RefSeq; NP_034960.1; NM_010830.2.
DR   UniGene; Mm.18210; -.
DR   ProteinModelPortal; Q6GTK8; -.
DR   SMR; Q6GTK8; 65-201, 361-1333.
DR   STRING; Q6GTK8; -.
DR   PRIDE; Q6GTK8; -.
DR   Ensembl; ENSMUST00000005503; ENSMUSP00000005503; ENSMUSG00000005370.
DR   GeneID; 17688; -.
DR   KEGG; mmu:17688; -.
DR   CTD; 17688; -.
DR   MGI; MGI:1343961; Msh6.
DR   HOVERGEN; HBG000101; -.
DR   InParanoid; Q6GTK8; -.
DR   OMA; QTYSVLD; -.
DR   PhylomeDB; Q6GTK8; -.
DR   NextBio; 292264; -.
DR   ArrayExpress; Q6GTK8; -.
DR   Bgee; Q6GTK8; -.
DR   Genevestigator; Q6GTK8; -.
DR   GO; GO:0032301; C:MutSalpha complex; IDA:MGI.
DR   GO; GO:0000790; C:nuclear chromatin; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0032137; F:guanine/thymine mispair binding; IDA:MGI.
DR   GO; GO:0008340; P:determination of adult lifespan; IMP:MGI.
DR   GO; GO:0008630; P:DNA damage response, signal transduction resulting in induction of apoptosis; IMP:MGI.
DR   GO; GO:0045190; P:isotype switching; IMP:MGI.
DR   GO; GO:0006298; P:mismatch repair; IMP:MGI.
DR   GO; GO:0045910; P:negative regulation of DNA recombination; IMP:MGI.
DR   GO; GO:0009411; P:response to UV; IMP:MGI.
DR   GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; IMP:MGI.
DR   InterPro; IPR017261; DNA_mismatch_repair_Msh6.
DR   InterPro; IPR015536; DNA_mismatch_repair_MSH6_C.
DR   InterPro; IPR007695; DNA_mismatch_repair_MutS-lik_N.
DR   InterPro; IPR000432; DNA_mismatch_repair_MutS_C.
DR   InterPro; IPR007861; DNA_mismatch_repair_MutS_clamp.
DR   InterPro; IPR007860; DNA_mismatch_repair_MutS_connt.
DR   InterPro; IPR007696; DNA_mismatch_repair_MutS_core.
DR   InterPro; IPR016151; DNA_mismatch_repair_MutS_N.
DR   InterPro; IPR000313; PWWP.
DR   Gene3D; G3DSA:3.40.1170.10; DNA_mismatch_repair_MutS_N; 1.
DR   PANTHER; PTHR11361; MutS_C; 1.
DR   PANTHER; PTHR11361:SF31; MutS_Hmlg_MSH6; 1.
DR   Pfam; PF01624; MutS_I; 1.
DR   Pfam; PF05188; MutS_II; 1.
DR   Pfam; PF05192; MutS_III; 1.
DR   Pfam; PF05190; MutS_IV; 1.
DR   Pfam; PF00488; MutS_V; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   PIRSF; PIRSF037677; DNA_mis_repair_Msh6; 1.
DR   SMART; SM00534; MUTSac; 1.
DR   SMART; SM00533; MUTSd; 1.
DR   SMART; SM00293; PWWP; 1.
DR   SUPFAM; SSF55271; DNA_mismatch_repair_MutS_N; 1.
DR   SUPFAM; SSF48334; DNA_repair_MutS_domIII; 1.
DR   PROSITE; PS00486; DNA_MISMATCH_REPAIR_2; 1.
DR   PROSITE; PS50812; PWWP; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding.
SQ   SEQUENCE   1358 AA;  151084 MW;  979D289BC69E6047 CRC64;
     MSRQSTLYSF FPKSPALGDT KKAAAEASRQ GAAASGASAS RGGDAAWSEA EPGSRSAAVS
     ASSPEAKDLN GGLRRASSSA QAVPPSSCDF SPGDLVWAKM EGYPWWPCLV YNHPFDGTFI
     RKKGKSVRVH VQFFDDSPTR GWVSKRMLKP YTGSKSKEAQ KGGHFYSSKS EILRAMQRAD
     EALSKDTAER LQLAVCDEPS EPEEEEETEV HEAYLSDKSE EDNYNESEEE AQPSVQGPRR
     SSRQVKKRRV ISDSESDIGG SDVEFKPDTK QEGSSDDASS GVGDSDSEDL GTFGKGAPKR
     KRAMVAQGGL RRKSLKKETG SAKRATPILS ETKSTLSAFS APQNSESQTH VSGGGNDSSG
     PTVWYHETLE WLKPEKRRDE HRRRPDHPEF NPTTLYVPEE FLNSCTPGMR KWWQLKSQNF
     DLVIFYKVGK FYELYHMDAV IGVSELGLIF MKGNWAHSGF PEIAFGRFSD SLVQKGYKVA
     RVEQTETPEM MEARCRKMAH VSKFDRVVRR EICRIITKGT QTYSVLDGDP SENYSRYLLS
     LKEKEEETSG HTRVYGVCFV DTSLGKFFIG QFSDDRHCSR FRTLVAHYPP VQILFEKGNL
     STETKTVLKG SLSSCLQEGL IPGSQFWDAT KTLRTLLEGG YFTGNGDSST VLPLVLKGMT
     SESDSVGLTP GEESELALSA LGGIVFYLKK CLIDQELLSM ANFEEYFPLD SDTVSTVKPG
     AVFTKASQRM VLDAVTLNNL EIFLNGTNGS TEGTLLERLD TCHTPFGKRL LKQWLCAPLC
     SPSAISDRLD AVEDLMAVPD KVTEVADLLK KLPDLERLLS KIHNVGSPLK SQNHPDSRAI
     MYEETTYSKK KIIDFLSALE GFKVMCKVSG LLEEVAGGFT SKTLKQVVTL QSKSPKGRFP
     DLTAELQRWD TAFDHEKARK TGLITPKAGF DSDYDQALAD IRENEQSLLE YLDKQRSRLG
     CKSIVYWGIG RNRYQLEIPE NFATRNLPEE YELKSTKKGC KRYWTKTIEK KLANLINAEE
     RRDTSLKDCM RRLFCNFDKN HKDWQSAVEC IAVLDVLLCL ANYSQGGDGP MCRPEIVLPG
     EDTHPFLEFK GSRHPCITKT FFGDDFIPND ILIGCEEEAE EHGKAYCVLV TGPNMGGKST
     LIRQAGLLAV MAQLGCYVPA EKCRLTPVDR VFTRLGASDR IMSGESTFFV ELSETASILR
     HATAHSLVLV DELGRGTATF DGTAIANAVV KELAETIKCR TLFSTHYHSL VEDYSKSVCV
     RLGHMACMVE NECEDPSQET ITFLYKFIKG ACPKSYGFNA ARLANLPEEV IQKGHRKARE
     FERMNQSLQL FREVCLATEK PTINGEAIHR LLALINGL
//
ID   HECW2_MOUSE             Reviewed;        1578 AA.
AC   Q6I6G8; Q3KNL8; Q6ZPU4; Q8C956;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=E3 ubiquitin-protein ligase HECW2;
DE            EC=6.3.2.-;
DE   AltName: Full=HECT, C2 and WW domain-containing protein 2;
DE   AltName: Full=NEDD4-like E3 ubiquitin-protein ligase 2;
GN   Name=Hecw2; Synonyms=Kiaa1301, Nedl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Miyazaki K., Takeda M., Aiyama Y., Nakagawara A.;
RT   "Mus musculus NEDL2 mRNA for NEDD4-like ubiquitin ligase 2.";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 124-1578 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination
CC       of TP73. Acts to stabilize TP73 and enhance activation of
CC       transcription by TP73 (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with TP73 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6I6G8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6I6G8-2; Sequence=VSP_023078;
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 HECT (E6AP-type E3 ubiquitin-protein
CC       ligase) domain.
CC   -!- SIMILARITY: Contains 2 WW domains.
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DR   EMBL; AB182244; BAD23960.1; -; mRNA.
DR   EMBL; AK042922; BAC31406.1; -; mRNA.
DR   EMBL; BC107219; AAI07220.1; -; mRNA.
DR   EMBL; AK129325; BAC98135.1; -; mRNA.
DR   IPI; IPI00453742; -.
DR   IPI; IPI00762336; -.
DR   RefSeq; NP_001001883.1; NM_001001883.3.
DR   RefSeq; NP_766243.2; NM_172655.3.
DR   UniGene; Mm.132150; -.
DR   UniGene; Mm.447527; -.
DR   HSSP; Q8CFI0; 1WR4.
DR   ProteinModelPortal; Q6I6G8; -.
DR   SMR; Q6I6G8; 190-321, 812-845, 921-1028, 1198-1573.
DR   PhosphoSite; Q6I6G8; -.
DR   PRIDE; Q6I6G8; -.
DR   Ensembl; ENSMUST00000087659; ENSMUSP00000084942; ENSMUSG00000042807.
DR   Ensembl; ENSMUST00000097741; ENSMUSP00000095348; ENSMUSG00000042807.
DR   Ensembl; ENSMUST00000120904; ENSMUSP00000113283; ENSMUSG00000042807.
DR   GeneID; 329152; -.
DR   KEGG; mmu:329152; -.
DR   CTD; 329152; -.
DR   MGI; MGI:2685817; Hecw2.
DR   GeneTree; ENSGT00570000078981; -.
DR   HOGENOM; HBG445632; -.
DR   HOVERGEN; HBG057414; -.
DR   InParanoid; Q6I6G8; -.
DR   OMA; LHSRKLV; -.
DR   OrthoDB; EOG405S06; -.
DR   PhylomeDB; Q6I6G8; -.
DR   NextBio; 398591; -.
DR   ArrayExpress; Q6I6G8; -.
DR   Bgee; Q6I6G8; -.
DR   Genevestigator; Q6I6G8; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0006464; P:protein modification process; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR000569; HECT.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00397; WW; 2.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF56204; HECT; 1.
DR   SUPFAM; SSF51045; WW_Rsp5_WWP; 2.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 2.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Ligase; Phosphoprotein;
KW   Repeat; Ubl conjugation pathway.
FT   CHAIN         1   1578       E3 ubiquitin-protein ligase HECW2.
FT                                /FTId=PRO_0000277668.
FT   DOMAIN      172    282       C2.
FT   DOMAIN      813    846       WW 1.
FT   DOMAIN      991   1024       WW 2.
FT   DOMAIN     1243   1578       HECT.
FT   REGION      737   1074       Interaction with TP73 (By similarity).
FT   COILED      853    880       Potential.
FT   ACT_SITE   1546   1546       Glycyl thioester intermediate (By
FT                                similarity).
FT   MOD_RES      48     48       Phosphoserine (By similarity).
FT   MOD_RES     858    858       Phosphoserine (By similarity).
FT   VAR_SEQ     295   1578       Missing (in isoform 2).
FT                                /FTId=VSP_023078.
FT   CONFLICT    226    226       H -> R (in Ref. 2; BAC31406).
SQ   SEQUENCE   1578 AA;  176235 MW;  6711C52EA0AF9CBF CRC64;
     MASSAREHLL FVRRRNPQMR YTLSPENLQS LAAQNSMPEN MALQRANSDT DLVTSESRSS
     LTASMYEYTL GQAQNLIIFW DIKEEVDPSD WIGLYHIDEN SPANFWDSKN RGVTGTQKGQ
     IVWRIEPGPY FMEPEIKICF KYYHGISGAL RATTPCITVK NPAVMMGAEG MEGGASGSLH
     SRKLVSFTLS DLRAVGLKKG MFFNPDPYLK MSIQPGKKSS FPTCAHHGQE RRSTIISNTT
     NPIWHREKYS FFALLTDVLE IEIKDKFAKS RPIIKRFLGK LTIPVQRLLE RQAGDQMLSY
     NLGRRLPADH VSGYLQFKVE VTSSAHEDAS PEAVGTILGV HTVNGDLGSP SDEEDMPGSH
     HDSTICANGP VSEDSVADGT PKHSFRTSST LEIDTEDLIS TSSRNSPPRG RQDSLNDYLD
     AIEHNGPARP GAASSSERSM GASPKLRSSF PTDTRLNAML HIDSDEEDHE FQQDLGYPSS
     LEEEGGLIMC SRASRIDDGS LTSQTKPEDD NPVENEDASI HETASLEERL ENLPEVADGS
     LPSSTAPDEN EANLEPQPSA DQGSTELCSS QEVDQPTSGA DAGASDTSGG SRRAASETES
     LDQGSEPSQV SSETEPSDPA RTESVSEAST RPEGESDPEG ADSSCNESVT TQLSSVETRC
     SSLESARFPE TPAFSSQEEE DGACAAEPTS SGPAEGSQES VCTPSSLPAV QVPSREEEGS
     AAEAAALSEQ GELGEVWQRR GSLEGAAAAA PAAAATDSQP QEDGDAGDAQ GACEGATAQE
     EGATGGSQTN GHQPLRSLPS VRQDVSRYQR VDEALPPNWE ARIDSHGRIF YVDHVNRTTT
     WQRPTAPPAP QVLQRSNSIQ QMEQLNRRYQ SIRRTMTNER PEENTSAIDG AGEEADFHQA
     SADFRRENVL PHSTSRSRLT LLLQSPPVKF LISPEFFTVL HSNPSAYRMF TNNTCLKHMI
     TKVRRDTHHF ERYQHNRDLV GFLNMFANKQ LELPRGWEMK HDHQGKAFFV DHNSRTTTFI
     DPRLPLQSSR PTSALVHRQH LTRQRSHSAG EVGEDSRHAG PPVLPRPSST FNTVSRPQYQ
     DMVPVAYNDK IVAFLRQPNI LEILQERQPD LARNHSLREK IQFIRTEGTP GLVRLSSDAD
     LVMLLSLFEE EIMSYVPPHA LLHPSYCQSP RGSPVSSPQN SPGTQRANAR APAPYKRDFE
     AKLRNFYRKL ETKGYGQGPG KLKLIIRRDH LLEDAFNQIM GYSRKDLQRN KLYVTFVGEE
     GLDYSGPSRE FFFLVSRELF NPYYGLFEYS ANDTYTVQIS PMSAFVDNHH EWFRFSGRIL
     GLALIHQYLL DAFFTRPFYK ALLRILCDLS DLEYLDEEFH QSLQWMKDND IHDILDLTFT
     VNEEVFGQIT ERELKPGGAN IPVTEKNKKE YIERMVKWRI ERGVVQQTES LVRGFYEVVD
     ARLVSVFDAR ELELVIAGTA EIDLNDWRNN TEYRGGYHDN HIVIRWFWAA VERFNNEQRL
     RLLQFVTGTS SIPYEGFASL RGSNGPRRFC VEKWGKITAL PRAHTCFNRL DLPPYPSFSM
     LYEKLLTAVE ETSTFGLE
//
ID   RHG20_MOUSE             Reviewed;        1182 AA.
AC   Q6IFT4; Q6ZPS4; Q8BLZ7; Q8BXI4;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Rho GTPase-activating protein 20;
DE   AltName: Full=RA and RhoGAP domain-containing protein;
DE            Short=RARhoGAP;
DE   AltName: Full=Rho-type GTPase-activating protein 20;
GN   Name=Arhgap20; Synonyms=Kiaa1391;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-388 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Aorta, Cerebellum, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 120-1182 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   IDENTIFICATION.
RX   PubMed=15234003; DOI=10.1016/j.ygeno.2004.03.004;
RA   Curry B.J., Su H., Law E.G., McLaughlin E.A., Nixon B., Aitken R.J.;
RT   "Identification of RARhoGAP, a novel putative RhoGAP gene expressed in
RT   male germ cells.";
RL   Genomics 84:406-418(2004).
RN   [4]
RP   IDENTIFICATION.
RX   PubMed=14532992;
RA   Katoh M., Katoh M.;
RT   "Identification and characterization of human KIAA1391 and mouse
RT   Kiaa1391 genes encoding novel RhoGAP family proteins with RA domain
RT   and ANXL repeats.";
RL   Int. J. Oncol. 23:1471-1476(2003).
CC   -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting
CC       them to an inactive GDP-bound state (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6IFT4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6IFT4-2; Sequence=VSP_024300, VSP_024301;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 Ras-associating domain.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK040756; BAC30694.1; -; mRNA.
DR   EMBL; AK046916; BAC32919.1; -; mRNA.
DR   EMBL; AK129345; BAC98155.1; -; mRNA.
DR   EMBL; BK004077; DAA04568.1; -; mRNA.
DR   IPI; IPI00222963; -.
DR   IPI; IPI00844725; -.
DR   RefSeq; NP_780744.2; NM_175535.3.
DR   UniGene; Mm.400352; -.
DR   UniGene; Mm.443529; -.
DR   HSSP; Q07960; 1RGP.
DR   ProteinModelPortal; Q6IFT4; -.
DR   SMR; Q6IFT4; 81-187, 354-551.
DR   STRING; Q6IFT4; -.
DR   PRIDE; Q6IFT4; -.
DR   Ensembl; ENSMUST00000065496; ENSMUSP00000065633; ENSMUSG00000053199.
DR   GeneID; 244867; -.
DR   KEGG; mmu:244867; -.
DR   UCSC; uc009plj.1; mouse.
DR   CTD; 244867; -.
DR   MGI; MGI:2445175; Arhgap20.
DR   eggNOG; roNOG06275; -.
DR   GeneTree; ENSGT00530000063299; -.
DR   HOGENOM; HBG268393; -.
DR   HOVERGEN; HBG061748; -.
DR   InParanoid; Q6IFT4; -.
DR   OMA; QISEHSV; -.
DR   NextBio; 386450; -.
DR   ArrayExpress; Q6IFT4; -.
DR   Bgee; Q6IFT4; -.
DR   CleanEx; MM_ARHGAP20; -.
DR   Genevestigator; Q6IFT4; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000159; Ras-assoc.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; GTPase activation.
FT   CHAIN         1   1182       Rho GTPase-activating protein 20.
FT                                /FTId=PRO_0000283087.
FT   DOMAIN       85    185       PH.
FT   DOMAIN      194    283       Ras-associating.
FT   DOMAIN      365    551       Rho-GAP.
FT   COMPBIAS    913   1012       Ser-rich.
FT   VAR_SEQ     184    217       IALEKEKDYPKSIPLKIFAKDIGNCAYFKTITVM -> VPV
FT                                HTVLMLSLTCLNQTCYCQICPRGAPFFLNGN (in
FT                                isoform 2).
FT                                /FTId=VSP_024300.
FT   VAR_SEQ     218   1182       Missing (in isoform 2).
FT                                /FTId=VSP_024301.
SQ   SEQUENCE   1182 AA;  131374 MW;  39B0BC5CC944D50B CRC64;
     MEAMSPQQDA LGAQPGRSSS LTGMSRIAGG PGTKKKMKTL AERRRSAPSL ILDKALQKRP
     STRDSHSASI DTCAFLSSFM CSSRTLLIDG PVELKRGLQR QERHLFLFND LFVSAKIKYN
     NNFKIKNKIR LTDMWTASCV EEVGEGNMNA QKSFVLGWPT VNFVATFSSP EQKDKWLSLL
     QRYIALEKEK DYPKSIPLKI FAKDIGNCAY FKTITVMNSD TASEVINMSL QMLGITGSER
     DYQLWVNSGK EAAPYPLIGH EYPYGIKMSH LRDTALLTQG SRDSASPSQL QEPFLMEQLP
     REMQCQFILK PTRLATAQQL SDSSQKTFKR RRSIINWAFW RGSSTHLDNL PMSPTSPMPG
     QLFGVSLPDL CENDNLPKPI LDMLSFLNQK GPLTKGIFRQ SANMKSCREL KEKLNSGIEV
     HLDCESIFVI ASVLKDFLRN IPESIFSSDL YDHWVCVMDQ GNDEEKINII QRLLDQLPRA
     NVVFLRYLFG VLHNIEQHSL SNQMTAFNLA VCIAPSILWP PASSSPELEN EFTKKVSLLI
     QFLIENCCRV FGEEIASLLG ELSERSDREH TPDITCFQMN DSSYDSLENE LNEEADAPCS
     DLVKKLGQGS RSMDSVLTLS DYDLEQPEVE GLLTLSNFDL DQSKEEHIPI KPPLEPKPVN
     VFVGYRKVSL GEHARAPAGP GTLSCLPVAA ADAPKVLRRH RRSSEPSIDY LDTKLSYLRE
     FYQKKLRKSS CDAVLSRKDE DYLKQTQPQK KGDKVCLKQS SVTGTDVSKR NTANENIKKK
     SLSGHEGTQV TLFTKSKPVP ISVASYSHGS SQDHPRKQAF DADPCRFSPP HLTDAQKSSR
     VQHRRCSEPS IDDQNYKLSY LRGIYSMKQN KASCEAGLLH GEDDYLRRHK SLQIEGQKLI
     NQSLVMGIEV GKSSSSHQST EKVLPPRLNL CPRASYSSLS SPGSSPSGSS VSSQDSAFSQ
     ISEHSVFTPT ETSSPIDCTF QTQRKQEELS SDFDSPSRLS GMPGPSMGQA SSHLAYLRKG
     TTEQPSQMHS VTLHPSAWLR SGLVTLKNWS LKKKTKAARP EDRKVCSLKE PLELPSCASG
     TPEADSLQES QDDLQGDEGP GQTACGFSSY ACQDSEQHAG SPFHLAESRL KPCMKLYKGE
     ESGGQYPCDN PWEGASSSLE TTEDTANPGA EPTTFAMTGT DI
//
ID   PANX2_MOUSE             Reviewed;         677 AA.
AC   Q6IMP4; B1PL20; Q4JGM2;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=Pannexin-2;
GN   Name=Panx2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Skoblov M., Baranova A.;
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 11-677 (ISOFORM 1).
RC   STRAIN=C57BL/6;
RA   Dvoriantchikova G., Ivanov D., Pestova A., Shestopalov V.;
RT   "Molecular characterization of pannexins in the lens.";
RL   Mol. Vis. 12:1417-1426(2006).
RN   [4]
RP   IDENTIFICATION.
RX   PubMed=15028292; DOI=10.1016/j.ygeno.2003.09.025;
RA   Baranova A., Ivanov D., Petrash N., Pestova A., Skoblov M.,
RA   Kelmanson I., Shagin D., Nazarenko S., Geraymovych E., Litvin O.,
RA   Tiunova A., Born T.L., Usman N., Staroverov D., Lukyanov S.,
RA   Panchin Y.;
RT   "The mammalian pannexin family is homologous to the invertebrate
RT   innexin gap junction proteins.";
RL   Genomics 83:706-716(2004).
CC   -!- FUNCTION: Structural component of the gap junctions and the
CC       hemichannels.
CC   -!- SUBUNIT: Forms PANX1/PANX2-heteromeric intercellular channels on
CC       coexpression in paired Xenopus oocytes. Does not form homomeric
CC       channels (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Potential). Cell junction, gap junction.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6IMP4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6IMP4-2; Sequence=VSP_039093, VSP_039094;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the pannexin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=DAA00307.1; Type=Frameshift; Positions=563, 584, 589;
CC   -----------------------------------------------------------------------
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DR   EMBL; EU446266; ACA30452.1; -; mRNA.
DR   EMBL; AC113069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DQ093579; AAY98749.1; -; mRNA.
DR   EMBL; BK000624; DAA00307.1; ALT_FRAME; mRNA.
DR   IPI; IPI00622936; -.
DR   IPI; IPI00918887; -.
DR   RefSeq; NP_001002005.2; NM_001002005.2.
DR   UniGene; Mm.40547; -.
DR   STRING; Q6IMP4; -.
DR   PRIDE; Q6IMP4; -.
DR   Ensembl; ENSMUST00000096304; ENSMUSP00000094027; ENSMUSG00000058441.
DR   GeneID; 406218; -.
DR   KEGG; mmu:406218; -.
DR   CTD; 406218; -.
DR   MGI; MGI:1890615; Panx2.
DR   GeneTree; ENSGT00390000009703; -.
DR   HOVERGEN; HBG053498; -.
DR   PhylomeDB; Q6IMP4; -.
DR   ArrayExpress; Q6IMP4; -.
DR   Bgee; Q6IMP4; -.
DR   CleanEx; MM_PANX2; -.
DR   Genevestigator; Q6IMP4; -.
DR   GermOnline; ENSMUSG00000058441; Mus musculus.
DR   GO; GO:0005921; C:gap junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000990; Innexin.
DR   Pfam; PF00876; Innexin; 1.
DR   PROSITE; PS51013; PANNEXIN; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell junction; Cell membrane; Gap junction;
KW   Glycoprotein; Ion transport; Ionic channel; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    677       Pannexin-2.
FT                                /FTId=PRO_0000208489.
FT   TOPO_DOM     11     53       Cytoplasmic (Potential).
FT   TRANSMEM     54     74       Helical; (Potential).
FT   TOPO_DOM     75    125       Extracellular (Potential).
FT   TRANSMEM    126    146       Helical; (Potential).
FT   TOPO_DOM    147    230       Cytoplasmic (Potential).
FT   TRANSMEM    231    251       Helical; (Potential).
FT   TOPO_DOM    252    295       Extracellular (Potential).
FT   TRANSMEM    296    316       Helical; (Potential).
FT   TOPO_DOM    317    617       Cytoplasmic (Potential).
FT   CARBOHYD     86     86       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ      75     75       A -> AARVSSLPS (in isoform 2).
FT                                /FTId=VSP_039093.
FT   VAR_SEQ     632    677       YEAREEEEGGPCAPSDMGDLLSIPPPQQILIATFEEPRTVV
FT                                STVEF -> SSSPPSRSREQL (in isoform 2).
FT                                /FTId=VSP_039094.
FT   CONFLICT     47     47       E -> G (in Ref. 1; ACA30452).
FT   CONFLICT     57     57       G -> D (in Ref. 1; ACA30452).
FT   CONFLICT    526    526       K -> E (in Ref. 1; ACA30452).
SQ   SEQUENCE   677 AA;  74614 MW;  38B0BE8B5771FD35 CRC64;
     MHHLLEQSAD MATALLAGEK LRELILPGSQ DDKAGALAAL LLQLKLELPF DRVVTIGTVL
     VPILLVTLVF TKNFAEEPIY CYTPHNFTRD QALYARGYCW TELRDALPGV DASLWPSLFE
     HKFLPYALLA FAAIMYVPAL GWEFLASTRL TSELNFLLQE IDNCYHRAAE GRAPKIEKQI
     QSKGPGITER EKREIIENAE KEKSPEQNLF EKYLERRGRS NFLAKLYLAR HVLILLLSVV
     PISYLCTYYA TQKQNEFTCA LGASPDGPVG SAGPTVRVSC KLPSVQLQRI IAGVDIVLLC
     FMNLIILVNL IHLFIFRKSN FIFDKLNKVG IKTRRQWRRS QFCDINILAM FCNENRDHIK
     SLNRLDFITN ESDLMYDNVV RQLLAALAQS NHDTTPTVRD SGIQTVDPSI NPAEPDGSAE
     PPVVKRPRKK MKWIPTSNPL PQPFKEQLAI MRVENSKTEK PKPVRRKTAT DTLIAPLLDA
     GARAAHHYKG SGGDSGPSSA PPAASEKKHT RHFSLDVHPY ILGTKKAKTE AVPPALPASR
     SQEGGFLSQT EECGLGLAAA PTKDAPLPEK EIPYPTEPAL PGLPSGGSFH VCSPPAAPAA
     ASLSPGSLGK ADPLTILSRN ATHPLLHIST LYEAREEEEG GPCAPSDMGD LLSIPPPQQI
     LIATFEEPRT VVSTVEF
//
ID   GPSM1_MOUSE             Reviewed;         673 AA.
AC   Q6IR34; A2AIX7; A2AIX8; A2AIX9; Q61366; Q8BUK4; Q8BX78; Q8R0R9;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 3.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=G-protein-signaling modulator 1;
DE   AltName: Full=Activator of G-protein signaling 3;
GN   Name=Gpsm1; Synonyms=Ags3; ORFNames=C10a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryonic heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC   STRAIN=C57BL/6; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 46-63, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 419-673.
RC   TISSUE=Erythroleukemia;
RA   Miller I.J., Bieker J.J.;
RT   "Subtractive cloning of murine erythroleukemia mRNAs.";
RL   Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   INTERACTION WITH STK11 AND MACF1, AND PHOSPHORYLATION.
RX   PubMed=12719437; DOI=10.1074/jbc.C200686200;
RA   Blumer J.B., Bernard M.L., Peterson Y.K., Nezu J., Chung P.,
RA   Dunican D.J., Knoblich J.A., Lanier S.M.;
RT   "Interaction of activator of G-protein signaling 3 (AGS3) with LKB1, a
RT   serine/threonine kinase involved in cell polarity and cell cycle
RT   progression: phosphorylation of the G-protein regulatory (GPR) motif
RT   as a regulatory mechanism for the interaction of GPR motifs with Gi
RT   alpha.";
RL   J. Biol. Chem. 278:23217-23220(2003).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-653, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [9]
RP   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION
RP   WITH GNAI3.
RX   PubMed=16009138; DOI=10.1016/j.cell.2005.05.009;
RA   Sanada K., Tsai L.-H.;
RT   "G protein betagamma subunits and AGS3 control spindle orientation and
RT   asymmetric cell fate of cerebral cortical progenitors.";
RL   Cell 122:119-131(2005).
CC   -!- FUNCTION: Guanine nucleotide dissociation inhibitor (GDI) which
CC       functions as a receptor-independent activator of heterotrimeric G-
CC       protein signaling. Keeps G(i/o) alpha subunit in its GDP-bound
CC       form thus uncoupling heterotrimeric G-proteins signaling from G
CC       protein-coupled receptors. Controls spindle orientation and
CC       asymmetric cell fate of cerebral cortical progenitors. May also be
CC       involved in macroautophagy in intestinal cells. May play a role in
CC       drug addiction.
CC   -!- SUBUNIT: Interacts with GNAI1 and GNAI2 preferentially in their
CC       GDP-bound state. May also interact with GNAO1. Interacts with
CC       INSC/inscuteable and FRMPD1 (By similarity). Interacts with GNAI3.
CC       Interacts with STK11 and MACF1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Endoplasmic reticulum
CC       membrane; Peripheral membrane protein; Cytoplasmic side. Golgi
CC       apparatus membrane; Peripheral membrane protein; Cytoplasmic side
CC       (By similarity). Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q6IR34-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6IR34-2; Sequence=VSP_039033;
CC       Name=3;
CC         IsoId=Q6IR34-3; Sequence=VSP_039029;
CC       Name=4;
CC         IsoId=Q6IR34-4; Sequence=VSP_039030, VSP_039031, VSP_039032;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q6IR34-5; Sequence=VSP_039030;
CC   -!- TISSUE SPECIFICITY: Expressed in neural progenitor cells (at
CC       protein level).
CC   -!- DEVELOPMENTAL STAGE: Expressed in brain at E14.
CC   -!- DOMAIN: The GoLoco domains are essential for the GDI activity
CC       toward G(i/o) alpha. The GoLoco domains mediate interaction with
CC       G(i/o) alpha (By similarity).
CC   -!- PTM: Phosphorylation regulates interaction with G(i/o) alpha.
CC   -!- SIMILARITY: Belongs to the GPSM family.
CC   -!- SIMILARITY: Contains 4 GoLoco domains.
CC   -!- SIMILARITY: Contains 9 TPR repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH26486.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=AAH71197.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK048691; BAC33422.1; -; mRNA.
DR   EMBL; AK084631; BAC39236.1; -; mRNA.
DR   EMBL; AL732541; CAM20327.1; -; Genomic_DNA.
DR   EMBL; AL732541; CAM20328.1; -; Genomic_DNA.
DR   EMBL; AL732541; CAM20329.1; -; Genomic_DNA.
DR   EMBL; CH466542; EDL08301.1; -; Genomic_DNA.
DR   EMBL; CH466542; EDL08300.1; -; Genomic_DNA.
DR   EMBL; BC026486; AAH26486.1; ALT_INIT; mRNA.
DR   EMBL; BC071197; AAH71197.1; ALT_INIT; mRNA.
DR   EMBL; L23316; AAB00119.1; -; mRNA.
DR   IPI; IPI00153257; -.
DR   IPI; IPI00226536; -.
DR   IPI; IPI00405083; -.
DR   IPI; IPI00751129; -.
DR   IPI; IPI00798498; -.
DR   RefSeq; NP_001186075.1; NM_001199146.1.
DR   RefSeq; NP_001186076.1; NM_001199147.1.
DR   RefSeq; NP_700459.2; NM_153410.5.
DR   UniGene; Mm.266611; -.
DR   ProteinModelPortal; Q6IR34; -.
DR   SMR; Q6IR34; 36-395.
DR   STRING; Q6IR34; -.
DR   PhosphoSite; Q6IR34; -.
DR   PRIDE; Q6IR34; -.
DR   Ensembl; ENSMUST00000066889; ENSMUSP00000067964; ENSMUSG00000026930.
DR   Ensembl; ENSMUST00000066914; ENSMUSP00000063200; ENSMUSG00000026930.
DR   Ensembl; ENSMUST00000066936; ENSMUSP00000065000; ENSMUSG00000026930.
DR   Ensembl; ENSMUST00000078616; ENSMUSP00000077686; ENSMUSG00000026930.
DR   GeneID; 67839; -.
DR   KEGG; mmu:67839; -.
DR   UCSC; uc008iun.1; mouse.
DR   UCSC; uc008iuo.1; mouse.
DR   CTD; 67839; -.
DR   MGI; MGI:1915089; Gpsm1.
DR   GeneTree; ENSGT00530000063126; -.
DR   HOVERGEN; HBG051823; -.
DR   InParanoid; Q6IR34; -.
DR   OMA; HIFLGRF; -.
DR   OrthoDB; EOG4SXNC5; -.
DR   ArrayExpress; Q6IR34; -.
DR   Bgee; Q6IR34; -.
DR   Genevestigator; Q6IR34; -.
DR   GermOnline; ENSMUSG00000026930; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR003109; GoLoco_motif.
DR   InterPro; IPR001440; TPR-1.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 2.
DR   Pfam; PF02188; GoLoco; 4.
DR   Pfam; PF00515; TPR_1; 2.
DR   SMART; SM00390; GoLoco; 4.
DR   SMART; SM00028; TPR; 6.
DR   PROSITE; PS50877; GOLOCO; 4.
DR   PROSITE; PS50005; TPR; 6.
DR   PROSITE; PS50293; TPR_REGION; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasm; Developmental protein;
KW   Differentiation; Direct protein sequencing; Endoplasmic reticulum;
KW   Golgi apparatus; Membrane; Neurogenesis; Phosphoprotein; Repeat;
KW   TPR repeat.
FT   CHAIN         1    673       G-protein-signaling modulator 1.
FT                                /FTId=PRO_0000252403.
FT   REPEAT       28     61       TPR 1.
FT   REPEAT       66     99       TPR 2.
FT   REPEAT      106    139       TPR 3.
FT   REPEAT      146    178       TPR 4.
FT   REPEAT      180    199       TPR 5.
FT   REPEAT      206    239       TPR 6.
FT   REPEAT      246    279       TPR 7.
FT   REPEAT      286    319       TPR 8.
FT   REPEAT      326    359       TPR 9.
FT   DOMAIN      493    515       GoLoco 1.
FT   DOMAIN      546    568       GoLoco 2.
FT   DOMAIN      594    616       GoLoco 3.
FT   DOMAIN      628    650       GoLoco 4.
FT   REGION        1    507       Mediates association with membranes (By
FT                                similarity).
FT   REGION      361    485       Interaction with STK11 (By similarity).
FT   MOD_RES     410    410       Phosphoserine (By similarity).
FT   MOD_RES     469    469       Phosphoserine (By similarity).
FT   MOD_RES     490    490       Phosphoserine (By similarity).
FT   MOD_RES     491    491       Phosphoserine (By similarity).
FT   MOD_RES     653    653       Phosphoserine.
FT   VAR_SEQ       1     23       Missing (in isoform 3).
FT                                /FTId=VSP_039029.
FT   VAR_SEQ       1     22       MASPAPPVAEELPGPASRRLYS -> MLASAMEGQPLALSL
FT                                AEKAVCKVVYGAPRPRPLLLPVGLELWLYVQKMRNLQRK
FT                                (in isoform 4 and isoform 5).
FT                                /FTId=VSP_039030.
FT   VAR_SEQ     251    271       NLGNAHIFLGRFDVAAEHYKK -> QPYPTLDSVGSRLSTV
FT                                AMIPQ (in isoform 4).
FT                                /FTId=VSP_039031.
FT   VAR_SEQ     272    673       Missing (in isoform 4).
FT                                /FTId=VSP_039032.
FT   VAR_SEQ     424    483       Missing (in isoform 2).
FT                                /FTId=VSP_039033.
FT   CONFLICT    668    668       C -> Y (in Ref. 6; AAB00119).
SQ   SEQUENCE   673 AA;  74362 MW;  60D284A5340604E7 CRC64;
     MASPAPPVAE ELPGPASRRL YSRMEASCLE LALEGERLCK AGDFKAGVAF FEAAVQVGTE
     DLKTLSAIYS QLGNAYFYLK EYARALQFHK HDLLLARTIG DRMGEAKASG NLGNTLKVLG
     RFDEAIVCCQ RHLDIAQEQG DKVGEARALY NIGNVYHAKG KQLSWNAAQD PGHLPPDVRE
     TLHRASEFYE RNLSLVKELG DRAAQGRAYG NLGNTHYLLG NFTEATTFHK ERLAIAKEFG
     DKAAERRAYS NLGNAHIFLG RFDVAAEHYK KTLQLSRQLR DQAVEAQACY SLGNTYTLLQ
     DYERAAEYHL RHLVIAQELA DRVGEGRACW SLGNAYVSMG SPAQALTFAK KHLQISQEIG
     DRNGELTARM NIAHLQLALG RLTSPAAAEK PDLAGYEAQG ARPKRTQRLS AETWDLLRLP
     LDREQNGETH HTGDWRGPGR DSLPLPMRSR KYQEGPDAIE RRPREGSHSP LDSADVRVQV
     PRTGIPRAPS SDEECFFDLL SKFQSSRMDD QRCPLEEGQA GAAEATAAPS VEDRAAQSSV
     TASPQTEEFF DLIASSQSRR LDDQRASVGS LPGLRITLNN VGHLRGDGDA QEPGDEFFNM
     LIKYQSSRID DQRCPPPDVL PRGPTMPDED FFSLIQRVQA KRMDEQRVDL AGSPEQEASG
     LPDPQQQCPP GAS
//
ID   ZN521_MOUSE             Reviewed;        1311 AA.
AC   Q6KAS7; Q8BIF5; Q8BV21; Q8CIQ2; Q8VDS6;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=Zinc finger protein 521;
DE   AltName: Full=Ecotropic viral integration site 3 protein;
GN   Name=Znf521; Synonyms=Evi3, Zfp521;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
RP   INVOLVEMENT IN B-CELL LEUKEMIA, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c;
RX   PubMed=12393497; DOI=10.1182/blood-2002-08-2652;
RA   Warming S., Liu P., Suzuki T., Akagi K., Lindtner S., Pavlakis G.N.,
RA   Jenkins N.A., Copeland N.G.;
RT   "Evi3, a common retroviral integration site in murine B-cell lymphoma,
RT   encodes an EBFAZ-related Kruppel-like zinc finger protein.";
RL   Blood 101:1934-1940(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of FLJ genes:
RT   the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:127-135(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 771-1311 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 983-1311 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   INVOLVEMENT IN B-CELL LEUKEMIA.
RX   PubMed=15580294; DOI=10.1038/sj.onc.1208243;
RA   Hentges K.E., Weiser K.C., Schountz T., Woodward L.S., Morse H.C.,
RA   Justice M.J.;
RT   "Evi3, a zinc-finger protein related to EBFAZ, regulates EBF activity
RT   in B-cell leukemia.";
RL   Oncogene 24:1220-1230(2005).
CC   -!- FUNCTION: Transcription factor that can both act as an activator
CC       or a repressor depending on the context. Involved in BMP signaling
CC       and in the regulation of the immature compartment of the
CC       hematopoietic system. Associates with SMADs in response to BMP2
CC       leading to activate transcription of BMP target genes. Acts as a
CC       transcriptional repressor via its interaction with EBF1, a
CC       transcription factor involved specification of B-cell lineage;
CC       this interaction preventing EBF1 to bind DNA and activate target
CC       genes.
CC   -!- SUBUNIT: Interacts with EBF1. Interacts with SMAD1 and SMAD4 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6KAS7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6KAS7-2; Sequence=VSP_028553;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed in all B-cell
CC       stages.
CC   -!- DOMAIN: Uses different DNA- and protein-binding zinc fingers to
CC       regulate the distinct BMP-Smad and hematopoietic system (By
CC       similarity).
CC   -!- DISEASE: Note=Defects in Znf521 are a cause of B-cell lymphomas.
CC       Znf521 gene is a frequent target of retroviral integration in
CC       murine B-cell lymphomas. Involved in most B-cell tumors in the
CC       AKXD-27 strain. Viral insertion causes overexpression resulting in
CC       the up-regulation of EBF1-target gene expression. Misexpression
CC       initiates tumorigenesis by perturbing B-cell development via an
CC       interaction with EBF1.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family.
CC   -!- SIMILARITY: Contains 30 C2H2-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC36964.1; Type=Erroneous initiation;
CC       Sequence=BAD21380.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AY147406; AAN39839.1; -; mRNA.
DR   EMBL; AK131130; BAD21380.1; ALT_INIT; mRNA.
DR   EMBL; BC021376; AAH21376.1; -; mRNA.
DR   EMBL; AK077697; BAC36964.1; ALT_INIT; mRNA.
DR   EMBL; AK081096; BAC38132.1; -; mRNA.
DR   IPI; IPI00421031; -.
DR   IPI; IPI00867882; -.
DR   RefSeq; NP_663467.1; NM_145492.4.
DR   UniGene; Mm.40325; -.
DR   HSSP; Q60980; 1U85.
DR   ProteinModelPortal; Q6KAS7; -.
DR   SMR; Q6KAS7; 44-332, 689-804, 847-913, 1055-1081, 1128-1310.
DR   STRING; Q6KAS7; -.
DR   PhosphoSite; Q6KAS7; -.
DR   PRIDE; Q6KAS7; -.
DR   Ensembl; ENSMUST00000025288; ENSMUSP00000025288; ENSMUSG00000024420.
DR   GeneID; 225207; -.
DR   KEGG; mmu:225207; -.
DR   CTD; 225207; -.
DR   MGI; MGI:95459; Zfp521.
DR   eggNOG; roNOG12716; -.
DR   GeneTree; ENSGT00530000063655; -.
DR   HOGENOM; HBG444784; -.
DR   HOVERGEN; HBG052773; -.
DR   InParanoid; Q6KAS7; -.
DR   OMA; DKPEQAH; -.
DR   OrthoDB; EOG4V9TPS; -.
DR   NextBio; 377576; -.
DR   ArrayExpress; Q6KAS7; -.
DR   Bgee; Q6KAS7; -.
DR   CleanEx; MM_ZFP521; -.
DR   Genevestigator; Q6KAS7; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 7.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 30.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 27.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 24.
PE   2: Evidence at transcript level;
KW   Activator; Alternative splicing; Developmental protein;
KW   Differentiation; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Proto-oncogene; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1   1311       Zinc finger protein 521.
FT                                /FTId=PRO_0000306872.
FT   ZN_FING      47     67       C2H2-type 1; degenerate.
FT   ZN_FING     118    140       C2H2-type 2.
FT   ZN_FING     146    168       C2H2-type 3.
FT   ZN_FING     174    196       C2H2-type 4.
FT   ZN_FING     202    224       C2H2-type 5.
FT   ZN_FING     246    269       C2H2-type 6.
FT   ZN_FING     281    304       C2H2-type 7.
FT   ZN_FING     310    332       C2H2-type 8.
FT   ZN_FING     405    429       C2H2-type 9; degenerate.
FT   ZN_FING     437    460       C2H2-type 10.
FT   ZN_FING     477    500       C2H2-type 11.
FT   ZN_FING     513    536       C2H2-type 12.
FT   ZN_FING     560    585       C2H2-type 13; atypical.
FT   ZN_FING     634    656       C2H2-type 14.
FT   ZN_FING     664    686       C2H2-type 15.
FT   ZN_FING     694    717       C2H2-type 16.
FT   ZN_FING     722    745       C2H2-type 17.
FT   ZN_FING     752    775       C2H2-type 18.
FT   ZN_FING     783    805       C2H2-type 19.
FT   ZN_FING     809    832       C2H2-type 20.
FT   ZN_FING     886    908       C2H2-type 21; degenerate.
FT   ZN_FING     930    952       C2H2-type 22.
FT   ZN_FING     959    981       C2H2-type 23.
FT   ZN_FING    1020   1042       C2H2-type 24.
FT   ZN_FING    1065   1083       C2H2-type 25; degenerate.
FT   ZN_FING    1138   1161       C2H2-type 26.
FT   ZN_FING    1195   1217       C2H2-type 27.
FT   ZN_FING    1225   1247       C2H2-type 28.
FT   ZN_FING    1256   1279       C2H2-type 29.
FT   ZN_FING    1286   1309       C2H2-type 30.
FT   MOD_RES     605    605       Phosphoserine (By similarity).
FT   MOD_RES     608    608       Phosphoserine (By similarity).
FT   VAR_SEQ    1191   1192       EK -> G (in isoform 2).
FT                                /FTId=VSP_028553.
FT   CONFLICT    595    595       I -> T (in Ref. 1; AAN39839).
FT   CONFLICT    771    771       V -> L (in Ref. 4; BAC38132).
FT   CONFLICT    897    897       M -> T (in Ref. 1; AAN39839).
SQ   SEQUENCE   1311 AA;  147666 MW;  C8D922B5335C099A CRC64;
     MSRRKQAKPR SLKDPNCKLE DKIEDGEAVD CKKRPEDGEE LEEDAVHSCD SCLQVFESLS
     DITEHKIHQC QLTDGVDVED DPSCSWPASS PSSKDQTSPS HGEGCDFGEE EGGPGLPYPC
     QFCDKSFSRL SYLKHHEQSH SDKLPFKCTY CSRLFKHKRS RDRHIKLHTG DKKYHCSECD
     AAFSRSDHLK IHLKTHTSNK PYKCAVCRRG FLSSSSLHGH MQVHERNKDG SQSGSRMEDW
     KMKDTQKCSQ CEEGFDFPED LQKHIAECHP ECSPNEDRAA LQCMYCHELF VEETSLMNHI
     EQVHGGEKKN SCSICSESFL TVEELYSHMD SHQQPESCNH SNSPSLVTVG YTSVSSTTPD
     SNLSVDSSTM VEAAPPIPKS RGRKRAAQQT SDMTGPSSKQ AKVTYSCIYC NKQLFSSLAV
     LQIHLKTMHL DKPEQAHICQ YCLEVLPSLY NLNEHLKQVH EAQDPGLIVS AMPAIVYQCN
     FCSEVVNDLN TLQEHIRCSH GFANPAAKDS NAFFCPHCYM GFLTDSSLEE HIRQVHCDLS
     GSRFGSPVLG TPKEPVVEVY SCSYCTNSPI FNSVLKLNKH IKENHKNIPL ALNYIHNGKK
     SRALSPLSPV AIEQTTLKMM QTVGGGPARA SGEYICNQCG AKYTSLDSFQ THLKTHLDTV
     LPKLTCPQCN KEFPNQESLL KHVTIHFMIT STYYICESCD KQFTSVDDLQ KHLLDMHTFV
     FFRCTLCQEV FDSKVSIQLH LAVKHSNEKK VYRCTSCNWD FRNETDLQLH VKHNHLENQG
     KVHKCIFCGE SFGTEVELQC HITTHSKKYN CRFCSKAFHA VILLEKHLRE KHCVFETKTP
     NCGTNGASEQ VQKEEAELQT LLTNSQESHN SHDGSEEDVD SSEPMYGCDI CGAAYTMETL
     LQNHQLRDHN IRPGESAIVK KKAELIKGNY KCNVCSRTFF SENGLREHMQ THLGPVKHYM
     CPICGERFPS LLTLTEHKVT HSKSLDTGNC RICKMPLQSE EEFLEHCQMH PDLRNSLTGF
     RCVVCMQTVT STLELKIHGT FHMQKTGNGS SVQTTGRGQH VQKLYKCASC LKEFRSKQDL
     VKLDINGLPY GLCAGCVNLS KSSSPGLSLP PGASRPGLGQ NESLSAMEGK GKAGGLKTRC
     SSCNVKFESE SELQNHIQTV HRELVPDANS TQLKTPQVSP MPRISPSQSD EKKTYQCIKC
     QMVFYNEWDI QVHVANHMID EGLNHECKLC SQTFDSPAKL QCHLIEHSFE GMGGTFKCPV
     CFTVFVQANK LQQHIFSAHG QEDKIYDCTQ CPQKFFFQTE LQNHTMTQHS S
//
ID   F125B_MOUSE             Reviewed;         317 AA.
AC   Q6KAU4; A2ARF1; Q6PB42;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=Multivesicular body subunit 12B;
DE   AltName: Full=ESCRT-I complex subunit MVB12B;
DE   AltName: Full=Protein FAM125B;
GN   Name=Fam125b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal brain;
RX   PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of FLJ genes:
RT   the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:127-135(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Component of the ESCRT-I complex, a regulator of
CC       vesicular trafficking process. Required for the sorting of
CC       endocytic ubiquitinated cargos into multivesicular bodies (By
CC       similarity).
CC   -!- SUBUNIT: Component of the ESCRT-I complex (endosomal sorting
CC       complex required for transport I) which consists of TSG101, VPS28,
CC       a VPS37 protein (VPS37A to -D) and a FAM125/MVB12 protein (FAM125A
CC       or -B) in a 1:1:1:1 stoechiometry. Interacts with TSG101; the
CC       association appears to be mediated by the TSG101-VPS37 binary
CC       subcomplex. Interacts with VPS28. Interacts with VPS37B; the
CC       association appears to be mediated by the TSG101-VPS37 binary
CC       subcomplex. Interacts with VPS37C; the association appears to be
CC       mediated by the TSG101-VPS37 binary subcomplex (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endosome (By similarity). Late endosome
CC       membrane; Peripheral membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the FAM125 family.
CC   -!- SIMILARITY: Contains 1 MABP domain.
CC   -!- SIMILARITY: Contains 1 UMA domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD21363.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK131113; BAD21363.1; ALT_INIT; mRNA.
DR   EMBL; AL845360; CAM23908.1; -; Genomic_DNA.
DR   EMBL; BX649361; CAM23908.1; JOINED; Genomic_DNA.
DR   EMBL; BX649361; CAM27811.1; -; Genomic_DNA.
DR   EMBL; AL845360; CAM27811.1; JOINED; Genomic_DNA.
DR   EMBL; BC049129; AAH49129.2; -; mRNA.
DR   EMBL; BC059907; AAH59907.1; -; mRNA.
DR   IPI; IPI00454035; -.
DR   RefSeq; NP_780393.2; NM_175184.4.
DR   UniGene; Mm.254914; -.
DR   ProteinModelPortal; Q6KAU4; -.
DR   PhosphoSite; Q6KAU4; -.
DR   PRIDE; Q6KAU4; -.
DR   Ensembl; ENSMUST00000041555; ENSMUSP00000048901; ENSMUSG00000038740.
DR   GeneID; 72543; -.
DR   KEGG; mmu:72543; -.
DR   UCSC; uc008jib.1; mouse.
DR   CTD; 72543; -.
DR   MGI; MGI:1919793; Fam125b.
DR   HOGENOM; HBG717190; -.
DR   HOVERGEN; HBG105828; -.
DR   InParanoid; Q6KAU4; -.
DR   OMA; PMDPITG; -.
DR   OrthoDB; EOG48GW3Z; -.
DR   NextBio; 336455; -.
DR   ArrayExpress; Q6KAU4; -.
DR   Bgee; Q6KAU4; -.
DR   Genevestigator; Q6KAU4; -.
DR   GermOnline; ENSMUSG00000038740; Mus musculus.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR018798; FAM125.
DR   InterPro; IPR023341; MABP.
DR   InterPro; IPR023340; UMA.
DR   Pfam; PF10240; DUF2464; 1.
DR   PROSITE; PS51498; MABP; 1.
DR   PROSITE; PS51497; UMA; 1.
PE   2: Evidence at transcript level;
KW   Endosome; Membrane; Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1    317       Multivesicular body subunit 12B.
FT                                /FTId=PRO_0000249075.
FT   DOMAIN       45    191       MABP.
FT   DOMAIN      252    301       UMA.
FT   MOD_RES      99     99       Phosphoserine (By similarity).
FT   MOD_RES     120    120       Phosphothreonine (By similarity).
FT   MOD_RES     202    202       Phosphothreonine (By similarity).
FT   MOD_RES     203    203       Phosphothreonine (By similarity).
FT   MOD_RES     307    307       Phosphoserine (By similarity).
SQ   SEQUENCE   317 AA;  35411 MW;  0FF01346C82C7998 CRC64;
     MRSCFCVRRS RDPPPPQPPP PQRGTDQATM PEVKELSEAL PETPMDPITG VGVVASRNRA
     PTGYDVVAQT ADGVDADLWK DGLFKSKVTR YLCFTRSFSK ENSHLGNVLV DMKLIDVKDT
     LPVGFIPIQE TVDTQEVVFR KKRLCIKFIP RDSTEAAICD IRIMGRTKQA PPQYTFIGEL
     NSMGIWYRMG RVPRNHDSSQ PTTPSQSSAS STPAPNLPRH ISLTLPATFR GRNNTSTDYE
     YQLSNLYAIS AMDGVPFMIS EKFSCIPESM QPFDLLGITI KSLAEIEKEY EYSFRTEQSA
     AARLPPSPTR CQQIPQS
//
ID   NIPBL_MOUSE             Reviewed;        2798 AA.
AC   Q6KCD5; Q6KC78; Q7TNS4; Q8BKV4; Q8CES9; Q9CUC6;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Nipped-B-like protein;
DE   AltName: Full=Delangin homolog;
DE   AltName: Full=SCC2 homolog;
GN   Name=Nipbl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RX   PubMed=15146185; DOI=10.1038/ng1363;
RA   Tonkin E.T., Wang T.-J., Lisgo S., Bamshad M.J., Strachan T.;
RT   "NIPBL, encoding a homolog of fungal Scc2-type sister chromatid
RT   cohesion proteins and fly Nipped-B, is mutated in Cornelia de Lange
RT   syndrome.";
RL   Nat. Genet. 36:636-641(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-325, AND NUCLEOTIDE SEQUENCE [LARGE
RP   SCALE MRNA] OF 2575-2798 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=15146186; DOI=10.1038/ng1364;
RA   Krantz I.D., McCallum J., DeScipio C., Kaur M., Gillis L.A.,
RA   Yaeger D., Jukofsky L., Wasserman N., Bottani A., Morris C.A.,
RA   Nowaczyk M.J.M., Toriello H., Bamshad M.J., Carey J.C., Rappaport E.,
RA   Kawauchi S., Lander A.D., Calof A.L., Li H.-H., Devoto M.,
RA   Jackson L.G.;
RT   "Cornelia de Lange syndrome is caused by mutations in NIPBL, the human
RT   homolog of Drosophila melanogaster Nipped-B.";
RL   Nat. Genet. 36:631-635(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2666, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; THR-2661 AND
RP   SER-2666, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553 AND THR-558, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1452; SER-1453 AND
RP   SER-2652, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Probably plays a structural role in chromatin. Involved
CC       in sister chromatid cohesion, possibly by interacting with the
CC       cohesin complex (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q6KCD5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6KCD5-2; Sequence=VSP_011098, VSP_011099;
CC       Name=3;
CC         IsoId=Q6KCD5-3; Sequence=VSP_011094;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q6KCD5-4; Sequence=VSP_011095, VSP_011096, VSP_011097;
CC         Note=No experimental confirmation available;
CC   -!- DEVELOPMENTAL STAGE: Widely expressed at E9.5 and E10.5, with
CC       notable accumulations in limb bud, branchial arch and craniofacial
CC       mesenchyme. These regions are involved in patterning of the
CC       skeleton and soft tissues of the limbs, jaw and face.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Belongs to the SCC2/Nipped-B family.
CC   -!- SIMILARITY: Contains 5 HEAT repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AJ627033; CAF25291.1; -; mRNA.
DR   EMBL; AJ640138; CAG26692.1; -; mRNA.
DR   EMBL; AK014915; BAC25453.1; -; mRNA.
DR   EMBL; AK016861; BAB30471.1; -; mRNA.
DR   EMBL; AK049588; BAC33829.1; -; mRNA.
DR   EMBL; BC055787; AAH55787.1; -; mRNA.
DR   IPI; IPI00357096; -.
DR   IPI; IPI00377849; -.
DR   IPI; IPI00380342; -.
DR   IPI; IPI00421052; -.
DR   RefSeq; NP_081983.2; NM_027707.2.
DR   RefSeq; NP_957684.1; NM_201232.1.
DR   UniGene; Mm.240329; -.
DR   UniGene; Mm.440537; -.
DR   ProteinModelPortal; Q6KCD5; -.
DR   STRING; Q6KCD5; -.
DR   PhosphoSite; Q6KCD5; -.
DR   PRIDE; Q6KCD5; -.
DR   Ensembl; ENSMUST00000052965; ENSMUSP00000059385; ENSMUSG00000022141.
DR   GeneID; 71175; -.
DR   KEGG; mmu:71175; -.
DR   UCSC; uc007veq.1; mouse.
DR   UCSC; uc007ver.1; mouse.
DR   UCSC; uc007vev.1; mouse.
DR   CTD; 71175; -.
DR   MGI; MGI:1913976; Nipbl.
DR   GeneTree; ENSGT00390000010427; -.
DR   HOGENOM; HBG282478; -.
DR   HOVERGEN; HBG052626; -.
DR   InParanoid; Q6KCD5; -.
DR   OMA; MMSQYKL; -.
DR   OrthoDB; EOG4001HC; -.
DR   PhylomeDB; Q6KCD5; -.
DR   NextBio; 333221; -.
DR   ArrayExpress; Q6KCD5; -.
DR   Bgee; Q6KCD5; -.
DR   CleanEx; MM_NIPBL; -.
DR   Genevestigator; Q6KCD5; -.
DR   GermOnline; ENSMUSG00000022141; Mus musculus.
DR   GO; GO:0032116; C:SMC loading complex; ISS:UniProtKB.
DR   GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IMP:MGI.
DR   GO; GO:0045444; P:fat cell differentiation; IMP:MGI.
DR   GO; GO:0034088; P:maintenance of mitotic sister chromatid cohesion; ISS:UniProtKB.
DR   GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
DR   GO; GO:0045778; P:positive regulation of ossification; IMP:MGI.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 4.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Nucleus; Phosphoprotein; Repeat.
FT   CHAIN         1   2798       Nipped-B-like protein.
FT                                /FTId=PRO_0000218597.
FT   REPEAT     1761   1799       HEAT 1.
FT   REPEAT     1837   1875       HEAT 2.
FT   REPEAT     1939   1978       HEAT 3.
FT   REPEAT     2221   2261       HEAT 4.
FT   REPEAT     2307   2345       HEAT 5.
FT   COMPBIAS    418    462       Gln-rich.
FT   MOD_RES     139    139       Phosphoserine (By similarity).
FT   MOD_RES     150    150       Phosphoserine (By similarity).
FT   MOD_RES     162    162       Phosphoserine (By similarity).
FT   MOD_RES     274    274       Phosphoserine (By similarity).
FT   MOD_RES     280    280       Phosphoserine.
FT   MOD_RES     284    284       Phosphoserine (By similarity).
FT   MOD_RES     306    306       Phosphoserine (By similarity).
FT   MOD_RES     350    350       Phosphoserine (By similarity).
FT   MOD_RES     553    553       Phosphoserine.
FT   MOD_RES     558    558       Phosphothreonine.
FT   MOD_RES     646    646       Phosphothreonine (By similarity).
FT   MOD_RES     906    906       Phosphoserine (By similarity).
FT   MOD_RES    1154   1154       Phosphoserine (By similarity).
FT   MOD_RES    1452   1452       Phosphothreonine.
FT   MOD_RES    1453   1453       Phosphoserine.
FT   MOD_RES    2503   2503       Phosphoserine (By similarity).
FT   MOD_RES    2505   2505       Phosphoserine (By similarity).
FT   MOD_RES    2507   2507       Phosphoserine (By similarity).
FT   MOD_RES    2509   2509       Phosphoserine (By similarity).
FT   MOD_RES    2652   2652       Phosphoserine.
FT   MOD_RES    2661   2661       Phosphothreonine.
FT   MOD_RES    2666   2666       Phosphoserine.
FT   VAR_SEQ       1   2694       Missing (in isoform 3).
FT                                /FTId=VSP_011094.
FT   VAR_SEQ       1    263       Missing (in isoform 4).
FT                                /FTId=VSP_011095.
FT   VAR_SEQ     499    556       DKPLKKRKQDSYPQEAGGATGGNRPASQETGSTGNGSRPAL
FT                                MVSIDLHQAGRVDSQAS -> GKGPLSLLLQHLATCVLIPT
FT                                SLLRYEFHSLAEASISDLIIQYHRLSNLNYITLFELLY
FT                                (in isoform 4).
FT                                /FTId=VSP_011096.
FT   VAR_SEQ     557   2798       Missing (in isoform 4).
FT                                /FTId=VSP_011097.
FT   VAR_SEQ    2678   2691       SLRRSKRNSDSTEL -> VRRRRSQRISQRIT (in
FT                                isoform 2).
FT                                /FTId=VSP_011098.
FT   VAR_SEQ    2692   2798       Missing (in isoform 2).
FT                                /FTId=VSP_011099.
FT   CONFLICT   2577   2577       K -> I (in Ref. 2; BAC25453).
SQ   SEQUENCE   2798 AA;  315450 MW;  BC23B6E2C949C9B3 CRC64;
     MNGDMPHVPI TTLAGIASLT DLLNQLPLPS PLPATTTKSL LFNSRIAEEV NCLLACRDDN
     LVSQLVHSLN QVSTDHIELK DNLGSDDPEG DIPVLLQAVL ARSPNVFREK SMQNRYVQSG
     MMMSQYKLSQ NSMHSSPASS NYQQTTISHS PSSRFVPPQT SSGNRFMPQQ NSPVPSPYAP
     QSPAGYMPYS HPSSYTTHPQ MQQASVSSPI VAGGLRNIHD NKVSGPLSGN SANHHADNPR
     HGSSDDYLHM VHRLSSDDGD SSTMRNAASF PLRSPQPVCS PAGSDGTPKG SRPPLILQSQ
     SLPCSSPRDV PPDILLDSPE RKQKKQKKIK LGKDEKDQNE KAAMYDIISS PTKDSTKLTL
     RLSRVRSSDM DQQDDMLSGM ENSNVSENDI PFNVQYPGQT SKTPITPQDV NRPLNAAQCL
     SQQEQTAFLP ANQVPVLQQN TSVATKQPQT SVVQNQQQVS QQGPIYDEVE LDALAEIERI
     ERESAIERER FSKEVQDKDK PLKKRKQDSY PQEAGGATGG NRPASQETGS TGNGSRPALM
     VSIDLHQAGR VDSQASITQD SDSIKKPEET KQCNDAPISV LQEDIVGSLK SIPENHPETP
     KKKSDPELSK SEMKQNESRL SESKPNENQL GESKSNESKL ETKTETPTEE LKQNENKTTE
     SKQSESAVVE PKQNENRPCD TKPNDNKQNN TRSENTKARP ETPKQKAESR PETPKQKSEG
     RPETPKQKGD GRPETPKQKS EGRPETPKQK GEGRPETPKH RHENRRDSGK PSTEKKPDVS
     KHKQDIKSDS PRLKSERAEA LKQRPDGRWE SLRRDHDSKQ KSDDRGESER HRGDQSRVRR
     PETLRSSSRN DHSTKSDGSK TEKLERKHRH ESGDSRDRPS GEQKSRPDSP RVKQGDTNKS
     RPGFKSPNSK DDKRTEGNRS KVDSNKAHTD NKAEFPSYLL GGRSGALKNF VIPKIKRDKD
     GNITQETKKM DMKGEQKDKV EKMGLVEDLN KGAKPVVVLQ KLSLDDVQKL IKDREEKSRS
     SLKSIKNKPS KSNKGSIDQS VLKELPPELL AEIESTMPLC ERVKMNKRKR STVNEKPKYA
     EISSDEDNDS DEAFESSRKR HKKDDDKAWE YEERDRRSSG DHRRSGHSHD GRRSSGGGRY
     RNRSPSDSDM EDYSPPPSLS EVARKMKKKE KQKKRKAYEP KLTPEEMMDS STFKRFTASI
     ENILDNLEDM DFTAFGDDDE IPQELLLGKH QLNELGSESA KIKAMGIMDK LSTDKTVKVL
     NILEKNIQDG SKLSTLLNHN NDTEEEERLW RDLIMERVTK SADACLTTIN IMTSPNMPKA
     VYIEDVIERV IQYTKFHLQN TLYPQYDPVY RVDPHGGGLL SSKAKRAKCS THKQRVIVML
     YNKVCDIVSS LSELLEIQLL TDTTILQVSS MGITPFFVEN VSELQLCAIK LVTAVFSRYE
     KHRQLILEEI FTSLARLPTS KRSLRNFRLN SSDVDGEPMY IQMVTALVLQ LIQCVVHLPS
     SEKDPNSEED SNKKVDQDVV ITNSYETAMR TAQNFLSIFL KKCGSKQGEE DYRPLFENFV
     QDLLSTVNKP EWPAAELLLS LLGRLLVHQF SNKSTEMALR VASLDYLGTV AARLRKDAVT
     SKMDQGSIER ILKQVSGGED EIQQLQKALL DYLDENTETD PSLVFSRKFY IAQWFRDTTL
     ETEKAMKSQK DEESSDATHH AKELETTGQI MHRAENRKKF LRSIIKTTPS QFSTLKMNSD
     TVDYDDACLI VRYLASMRPF AQSFDIYLTQ ILRVLGENAI AVRTKAMKCL SEVVAVDPSI
     LARLDMQRGV HGRLMDNSTS VREAAVELLG RFVLCRPQLA EQYYDMLIER ILDTGISVRK
     RVIKILRDIC IEQPTFPKIT EMCVKMIRRV NDEEGIKKLV NETFQKLWFT PTPHNDKEAM
     TRKILNITDV VAACRDTGYD WFEQLLQNLL KSEEDSSYKP VKKACTQLVD NLVEHILKYE
     ESLADSDNKG VNSGRLVACI TTLFLFSKIR PQLMVKHAMT MQPYLTTKCS TQNDFMVICN
     VAKILELVVP LMEHPSETFL ATIEEDLMKL IIKYGMTVVQ HCVSCLGAVV NKVTQNFKFV
     WACFNRYYGA ISKLKSQHQE DPNNTSLLTN KPALLRSLFT VGALCRHFDF DLEDFKGNSK
     VNIKDKVLEL LMYFTKHSDE EVQTKAIIGL GFAFIQHPSL MFEQEVKNLY NSILSDKNSS
     VNLKIQVLKN LQTYLQEEDT RMQQADRDWK KVAKQEDLKE MGDVSSGMSS SIMQLYLKQV
     LEAFFHTQSS VRHFALNVIA LTLNQGLIHP VQCVPYLIAM GTDPEPAMRN KADQQLVEID
     KKYAGFIHMK AVAGMKMSYQ VQQAINTCLK DPVRGFRQDE SSSALCSHLY SMIRGNRQHR
     RAFLISLLNL FDDTAKTEVT MLLYIADNLA CFPYQTQEEP LFIMHHIDIT LSVSGSNLLQ
     SFKESMVKDK RKERKTSPAK ENESSESEEE VSRPRKSRKR VDSESDSDSE DDINSVMKCL
     PENSAPLIEF ANVSQGILLL LMLKQHLKNL CGFSDSKIQK YSPSESAKVY DKAINRKTGV
     HFHPKQTLDF LRSDMANSKL TEDVKRSIVR QYLDFKLLME HLDPDEEEEE GEVSASTNAR
     NKAITSLLGG GSPKNNTAAD TEDEESDGED RGGGTSGSLR RSKRNSDSTE LAAQMNESVD
     VMDVIAICCP KYKDRPQIAR VVQRTSSGVS VQWMAGSYSG SWTEAKRRDG RKLVPWVDTI
     KESDIIYKKI ALTSANKLTN KVVQTLRSLY AAKDGTSS
//
ID   DGKB_MOUSE              Reviewed;         802 AA.
AC   Q6NS52; Q80TT5;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Diacylglycerol kinase beta;
DE            Short=DAG kinase beta;
DE            EC=2.7.1.107;
DE   AltName: Full=Diglyceride kinase beta;
DE            Short=DGK-beta;
GN   Name=Dgkb; Synonyms=Kiaa0718;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 34-802 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
CC   -!- FUNCTION: Exhibits high phosphorylation activity for long-chain
CC       diacylglycerols (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-
CC       sn-glycerol 3-phosphate.
CC   -!- ENZYME REGULATION: Stimulated by phosphatidylserine (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6NS52-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NS52-2; Sequence=VSP_021900;
CC   -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase
CC       family.
CC   -!- SIMILARITY: Contains 1 DAGKc domain.
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
CC   -!- SIMILARITY: Contains 2 phorbol-ester/DAG-type zinc fingers.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK139408; BAE23997.1; -; mRNA.
DR   EMBL; BC070461; AAH70461.1; -; mRNA.
DR   EMBL; AK122355; BAC65637.1; -; mRNA.
DR   IPI; IPI00421000; -.
DR   IPI; IPI00816974; -.
DR   RefSeq; NP_848796.2; NM_178681.4.
DR   UniGene; Mm.126525; -.
DR   ProteinModelPortal; Q6NS52; -.
DR   SMR; Q6NS52; 5-296, 305-359.
DR   STRING; Q6NS52; -.
DR   PhosphoSite; Q6NS52; -.
DR   PRIDE; Q6NS52; -.
DR   Ensembl; ENSMUST00000040500; ENSMUSP00000037900; ENSMUSG00000036095.
DR   Ensembl; ENSMUST00000072865; ENSMUSP00000072642; ENSMUSG00000036095.
DR   GeneID; 217480; -.
DR   KEGG; mmu:217480; -.
DR   UCSC; uc007nkj.1; mouse.
DR   UCSC; uc007nkn.1; mouse.
DR   CTD; 217480; -.
DR   MGI; MGI:2442474; Dgkb.
DR   HOGENOM; HBG315056; -.
DR   HOVERGEN; HBG051345; -.
DR   InParanoid; Q6NS52; -.
DR   OMA; SCVVIRT; -.
DR   OrthoDB; EOG4GHZNH; -.
DR   BRENDA; 2.7.1.107; 244.
DR   NextBio; 375875; -.
DR   ArrayExpress; Q6NS52; -.
DR   Bgee; Q6NS52; -.
DR   CleanEx; MM_DGKB; -.
DR   Genevestigator; Q6NS52; -.
DR   GermOnline; ENSMUSG00000036095; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004143; F:diacylglycerol kinase activity; IDA:MGI.
DR   GO; GO:0007205; P:activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway; IEA:InterPro.
DR   InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00609; DAGK_acc; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00045; DAGKa; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SMART; SM00054; EFh; 2.
DR   PROSITE; PS50146; DAGK; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Calcium; Cytoplasm; Kinase;
KW   Metal-binding; Nucleotide-binding; Repeat; Transferase; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    802       Diacylglycerol kinase beta.
FT                                /FTId=PRO_0000264623.
FT   DOMAIN      148    183       EF-hand 1.
FT   DOMAIN      193    228       EF-hand 2.
FT   DOMAIN      432    566       DAGKc.
FT   CA_BIND     161    172       1 (Potential).
FT   CA_BIND     206    217       2 (Potential).
FT   ZN_FING     243    293       Phorbol-ester/DAG-type 1.
FT   ZN_FING     308    357       Phorbol-ester/DAG-type 2.
FT   VAR_SEQ      50     56       Missing (in isoform 2).
FT                                /FTId=VSP_021900.
SQ   SEQUENCE   802 AA;  90272 MW;  2995ECF41057DEF3 CRC64;
     MTNQEKWAHL SPSEFSQLQK YAEYSTKKLK DVLEEFHGNG VLAKYNPEGK QDILNQTIDF
     EGFKLFMKTF LEAELPDDFT AHLFMSFSNK FPHSSPNVKS KPALLSGGLR MNKGAITPPR
     SSPANTCSPE VIHLKDIVCY LSLLERGRPE DKLEFMFRLY DTDGNGFLDS SELENIIGQM
     MHVAEYLEWD VTELNPILHE MMEEIDYDRD GTVSLEEWIQ GGMTTIPLLV LLGLENNVKD
     DGQHVWRLKH FNKPAYCNLC LNMLIGVGKQ GLCCSFCKYT VHERCVARAP PSCIKTYVKS
     KKNTDVMHHY WVEGNCPTKC DKCHKTVKCY QGLTGLHCVW CQTTLHNKCA SHLKPECDCG
     PLKDHILPPT TICPVVLTMP SAGASVPEER QSTAKKEKSS SQQPNKATDK NKMQRANSVT
     MDGQGLQITP VPGTHPLLVF VNPKSGGKQG ERIYRKFQYL LNPRQVYSLS GNGPMPGLHF
     FRDVPDFRVL ACGGDGTVGW ILDCIEKANV VKHPPVAILP LGTGNDLARC LRWGGGYEGE
     NLMKILKDIE SSTEIMLDRW KFEVTPNDKD EKGDPVPYSI INNYFSIGVD ASIAHRFHIM
     REKHPEKFNS RMKNKFWYFE FGTSETFSAT CKKLHESVEI ECDGVQIDLI NISLEGIAIL
     NIPSMHGGSN LWGESKKKRS HRRIEKKGSD KRPTLTDAKE LKFASQDLSD QLLEVVGLEG
     AMEMGQIYTG LKSAGRRLAQ CSSVVIRTSK SLPMQIDGEP WMQTPCTIKI THKNQAPMLM
     GPPPKTGLFC SLIKRTRNRS KE
//
ID   F135A_MOUSE             Reviewed;        1506 AA.
AC   Q6NS59; Q3UEW1; Q5XK31; Q8BXS8; Q8BZL9; Q8K2K2; Q9D2J6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Protein FAM135A;
GN   Name=Fam135a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-479 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon, Retina, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, Embryo, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6NS59-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NS59-2; Sequence=VSP_030231;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the FAM135 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH83093.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK019549; BAB31792.2; -; mRNA.
DR   EMBL; AK034175; BAC28616.1; -; mRNA.
DR   EMBL; AK044359; BAC31883.1; -; mRNA.
DR   EMBL; AK149303; BAE28800.1; -; mRNA.
DR   EMBL; BC031160; AAH31160.1; -; mRNA.
DR   EMBL; BC070446; AAH70446.1; -; mRNA.
DR   EMBL; BC083093; AAH83093.1; ALT_INIT; mRNA.
DR   IPI; IPI00227596; -.
DR   IPI; IPI00882309; -.
DR   RefSeq; NP_080880.4; NM_026604.4.
DR   UniGene; Mm.87130; -.
DR   ProteinModelPortal; Q6NS59; -.
DR   SMR; Q6NS59; 1240-1325.
DR   PhosphoSite; Q6NS59; -.
DR   PRIDE; Q6NS59; -.
DR   Ensembl; ENSMUST00000027337; ENSMUSP00000027337; ENSMUSG00000026153.
DR   GeneID; 68187; -.
DR   KEGG; mmu:68187; -.
DR   UCSC; uc007aml.1; mouse.
DR   CTD; 68187; -.
DR   MGI; MGI:1915437; Fam135a.
DR   GeneTree; ENSGT00390000007885; -.
DR   HOVERGEN; HBG106788; -.
DR   InParanoid; Q6NS59; -.
DR   OMA; YIQIYSL; -.
DR   OrthoDB; EOG4STS3R; -.
DR   PhylomeDB; Q6NS59; -.
DR   NextBio; 326642; -.
DR   ArrayExpress; Q6NS59; -.
DR   Bgee; Q6NS59; -.
DR   Genevestigator; Q6NS59; -.
DR   InterPro; IPR022122; DUF3657.
DR   InterPro; IPR007751; DUF676_hydro-like.
DR   Pfam; PF12394; DUF3657; 2.
DR   Pfam; PF05057; DUF676; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1   1506       Protein FAM135A.
FT                                /FTId=PRO_0000314169.
FT   MOD_RES     454    454       Phosphoserine (By similarity).
FT   VAR_SEQ       1    425       Missing (in isoform 2).
FT                                /FTId=VSP_030231.
FT   CONFLICT    486    486       E -> D (in Ref. 1; BAC31883).
FT   CONFLICT    703    703       D -> Y (in Ref. 2; AAH70446).
FT   CONFLICT    754    754       K -> N (in Ref. 1; BAB31792).
FT   CONFLICT    813    813       H -> R (in Ref. 1; BAB31792).
FT   CONFLICT    994    994       D -> E (in Ref. 1; BAC28616).
FT   CONFLICT   1044   1044       T -> A (in Ref. 2; AAH83093).
FT   CONFLICT   1162   1162       R -> K (in Ref. 1; BAB31792).
SQ   SEQUENCE   1506 AA;  166857 MW;  5428467DDF228796 CRC64;
     MTEVQAMVEF SVELNKFYNV DLFQRGFYQI RASMKIPARI PHRVEASLLH ATGMTLAFPA
     SVHDALVCSK TFQILYKNEE VVLNDVMIFK VKMLLDERKI EETLEEISFL LSLGLHFTDG
     DYSADDLNAL QLISSRTLKL HYSICRGLHH HANVMFDYFH LSVVSVTVHA SLVALHQPLI
     SFPRPVKTTW LNRNAPAQSK DSAIPTLESV VFGINYTKQL SPDGCSFLIA ESFLHHAYHF
     HYTLCATLLL AFKGLHSYFI TVTEEIPSCQ KLDLEEMDVE ARLTELCEEV KKVENPDELA
     ELINMNLAQL CSLLMALWGQ FLEAITLHED LRVLLAQEHH TLRVRRFSEA FFCFEHPREA
     AIAYQELHAQ SHLQMCTAIK NTSFCSSLPP LPIECSELDG DLNSLPIIFE DRYLDSVIED
     LDAPWMGIQS LQISEASKTD KHETEESSVV GLSSPELKVR PAVASSNCYT EGEKQLTKSL
     KGKNEESNKS KVKVTKLMKT MKPENTKKLI KQNSKDSVVL VSYKCLKTTA SSDFTKCLEG
     SPSHSQKEGL DPTLCAGNFD PKTYTRQPSQ KEASSLSANT DRSEHKSPDT ENMQPDQFEL
     LNSGSLNLCA NLSISGKLAI SQDNSDIPDT EHNLASTSSS NDCHDYQTTP SSGVRTLEVK
     SSSKESFNGE KITVKIGPWT ELQEAELFVD NLLPDFEALD SNDKPKSIDI PLERDALQET
     KCHSTEESLT KFRSNLPAPS TKEYHVAVSS DTIKLPDTNA TYASSRFSDS GVESEPSSFA
     THPNPEIAFE TLQGPGPCNN ERLFPQLLMK PDHNVKFSLG SHCTESTSAL SEIQSSLTSI
     NSLPSDDELS PDDNCKKSAV PDCHLSDSKT VFNLGTMDLP KCDDTKKSSI ILQQQSVVFS
     GHLDNDTLAM HSLDLSTEDP LRLVFLDEDA SSGVRSSWGS KPHLDAPFTG PQSQGTSSNN
     STESVPTLNS KLICLGSPCV VSGSVCTDAG LSADRTVEGK SGEPLNHKQV CSAAPVVESD
     PLSSSTDVVK QGLVENYFGS QSTTDVSDAC AITCHSPVSS QETCDKGISD LQQEQGKEEE
     EEDQEMVQNG YHEETDFSAT DGTVSVHYIS GNELGEGRHE QSEKLSSNYL SAGVTVPAVC
     TSGCLSFPSA LRESPCVKYS SRSKVDAITK QPSSISYNFS SSTSWYENSP KPQIHAFLQA
     KEELKQLRLP GFMYSDVPLL ASSAPYFSMD EEDGSEDGVH LIVCVHGLDG NSADLRLVKT
     YIELGLPGGR VDFLMSERNQ NDTFADFDCM TDRLLDEIIQ YIQIYSLTVS KISFIGHSLG
     NLIIRSVLTR PRFKYYLSKL HTFLSLSGPH LGTLYNSSAL VNTGLWFMQK WKKSGSLLQL
     TCRDHSDPRQ TFLYKLSNKA GLHYFKNVVL VGSLQDRYVP YHSARIEMCK TALKDKQSGQ
     IYSEMIHNLL RPVLQSKGCN LVRYNVINAL PNTADSLIGR AAHIAVLDSE IFLEKFFLVA
     ALKYFQ
//
ID   FBX41_MOUSE             Reviewed;         873 AA.
AC   Q6NS60; Q6P7W4; Q6ZPG1;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=F-box only protein 41;
GN   Name=Fbxo41; Synonyms=D6Ertd538e, Kiaa1940;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-873.
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION AT SER-3;
RP   SER-21; SER-476 AND THR-477, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-
CC       box protein)-type E3 ubiquitin ligase complex (By similarity).
CC   -!- SUBUNIT: Directly interacts with SKP1A and CUL1 (By similarity).
CC   -!- SIMILARITY: Contains 1 F-box domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC061475; AAH61475.1; -; mRNA.
DR   EMBL; BC070445; AAH70445.1; -; mRNA.
DR   EMBL; AK129466; BAC98276.1; -; mRNA.
DR   IPI; IPI00415914; -.
DR   RefSeq; NP_001001160.1; NM_001001160.2.
DR   UniGene; Mm.38777; -.
DR   ProteinModelPortal; Q6NS60; -.
DR   SMR; Q6NS60; 554-590, 741-813.
DR   PhosphoSite; Q6NS60; -.
DR   PRIDE; Q6NS60; -.
DR   Ensembl; ENSMUST00000054506; ENSMUSP00000058653; ENSMUSG00000047013.
DR   GeneID; 330369; -.
DR   KEGG; mmu:330369; -.
DR   NMPDR; fig|10090.3.peg.14752; -.
DR   UCSC; uc009cpw.1; mouse.
DR   CTD; 330369; -.
DR   MGI; MGI:1261912; Fbxo41.
DR   GeneTree; ENSGT00530000063713; -.
DR   HOGENOM; HBG445589; -.
DR   HOVERGEN; HBG051581; -.
DR   InParanoid; Q6NS60; -.
DR   OMA; RKQQEVV; -.
DR   OrthoDB; EOG444KJT; -.
DR   PhylomeDB; Q6NS60; -.
DR   NextBio; 399317; -.
DR   ArrayExpress; Q6NS60; -.
DR   Bgee; Q6NS60; -.
DR   CleanEx; MM_FBXO41; -.
DR   Genevestigator; Q6NS60; -.
DR   GermOnline; ENSMUSG00000047013; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR022364; F-box_dom_Skp2-like.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   SMART; SM00355; ZnF_C2H2; 1.
DR   SUPFAM; SSF81383; F-box_dom_Skp2-like; 1.
DR   PROSITE; PS50181; FBOX; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Phosphoprotein; Ubl conjugation pathway.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    873       F-box only protein 41.
FT                                /FTId=PRO_0000119941.
FT   DOMAIN      548    592       F-box.
FT   COILED      207    349       Potential.
FT   COMPBIAS     51     61       Poly-Ala.
FT   COMPBIAS    107    112       Poly-His.
FT   COMPBIAS    357    362       Poly-Gly.
FT   MOD_RES       2      2       N-acetylalanine.
FT   MOD_RES       3      3       Phosphoserine.
FT   MOD_RES      21     21       Phosphoserine.
FT   MOD_RES     476    476       Phosphoserine.
FT   MOD_RES     477    477       Phosphothreonine.
FT   MOD_RES     545    545       Phosphoserine.
SQ   SEQUENCE   873 AA;  94331 MW;  2B1BA501527F9700 CRC64;
     MASLDLPYRC PRCGEHKRFR SLSSLRAHLE YSHTYETLYI LSKTNSICDG AAAAAAAAAA
     ASGFPLAPEP AALLAVPGAR REVFESTSFQ GKEQATGPSP AGPHLLHHHH HHAPLAHFPA
     DLVPASLPCE ELAEPGLVPA ARYALREIEI PLGELFARKS VASSACSTPP PGPGPGPCSG
     PSSASPASPS PADVAYEEGL ARLKIRALEK LEVDRRLERL SEEVEQKIAG QVGRLQAELE
     RKAAELETAR QESARLGREK EELEERASEL SRQVDVSVEL LASLKQDLVH KEQELSRKQQ
     EVVQIDQFLK ETAAREASAK LRLQQFIEEL LERADRAERQ LQVISSSCGS TPSASLGRGG
     GGSASGPGVR GPGRMREHHA GSAVPSTYAV SRHGSSPSTG ASSRVPAASQ SSGCYDSDSL
     ELPRPEEGPS EDSGPGGLGS RAQATNGGSE RSQAPRSSGL RRQAIQNWQR RPRRHSTEGE
     EGDVSDVGSR TTESEAEGPS DVPRPGPAVA GPLNSCRLSA RPEGGSGRGR RVERGSPSRS
     NEVISPEILK MRAALFCIFT YLDTRTLLHA AEVCRDWRFV ARHPAVWTRV LLENARVCSK
     FLAMLAQWCT QAHSLTLQNL KPRQRGKKES KEEYARSTRG CLEAGLESLL KAAGGNLLIL
     RISHCPNILT DRSLWLASCY CRALQAVTYR SATDPVGHEV IWALGAGCRD IVSLQVAPLH
     PCQQPTRFSN RCLQMIGRCW PHLRALGVGG AGCGVQGLAS LARNCMRLQV LELDHVSEIT
     QEVAAEVCRE GLKGLEMLVL TATPVTPKAL LHFNSICRNL KSIVVQIGIA DYFKEPSSPE
     AQKLFEDMVT KLQALRRRPG FSKILHIKVE GGC
//
ID   GPR17_MOUSE             Reviewed;         339 AA.
AC   Q6NS65; Q80UD2;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Uracil nucleotide/cysteinyl leukotriene receptor;
DE            Short=UDP/CysLT receptor;
DE   AltName: Full=G-protein coupled receptor 17;
GN   Name=Gpr17;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 132-308.
RX   MEDLINE=22584407; PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA   Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA   Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA   Bergmann J.E., Gaitanaris G.A.;
RT   "The G protein-coupled receptor repertoires of human and mouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
CC   -!- FUNCTION: Dual specificity receptor for uracil nucleotides and
CC       cysteinyl leukotrienes (CysLTs). Signals through G(i) and
CC       inhibition of adenylyl cyclase. May mediate brain damage by
CC       nucleotides and CysLTs following ischemia (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
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CC   -----------------------------------------------------------------------
DR   EMBL; BC070439; AAH70439.1; -; mRNA.
DR   EMBL; AY255543; AAO85055.1; -; mRNA.
DR   IPI; IPI00125491; -.
DR   RefSeq; NP_001020552.1; NM_001025381.2.
DR   UniGene; Mm.391108; -.
DR   ProteinModelPortal; Q6NS65; -.
DR   SMR; Q6NS65; 1-324.
DR   DIP; DIP-48915N; -.
DR   STRING; Q6NS65; -.
DR   PRIDE; Q6NS65; -.
DR   Ensembl; ENSMUST00000064016; ENSMUSP00000063670; ENSMUSG00000052229.
DR   GeneID; 574402; -.
DR   KEGG; mmu:574402; -.
DR   UCSC; uc008eiw.1; mouse.
DR   CTD; 574402; -.
DR   MGI; MGI:3584514; Gpr17.
DR   eggNOG; roNOG07677; -.
DR   GeneTree; ENSGT00590000082782; -.
DR   HOGENOM; HBG714985; -.
DR   HOVERGEN; HBG102010; -.
DR   InParanoid; Q6NS65; -.
DR   OMA; SMNGLEV; -.
DR   OrthoDB; EOG44BB2S; -.
DR   PhylomeDB; Q6NS65; -.
DR   NextBio; 414384; -.
DR   ArrayExpress; Q6NS65; -.
DR   Bgee; Q6NS65; -.
DR   CleanEx; MM_GPR17; -.
DR   Genevestigator; Q6NS65; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045028; F:purinergic nucleotide receptor activity, G-protein coupled; IEA:InterPro.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR002286; P2_purnocptor.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01157; P2YPURNOCPTR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Receptor; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    339       Uracil nucleotide/cysteinyl leukotriene
FT                                receptor.
FT                                /FTId=PRO_0000278171.
FT   TOPO_DOM      1     36       Extracellular (Potential).
FT   TRANSMEM     37     57       Helical; Name=1; (Potential).
FT   TOPO_DOM     58     64       Cytoplasmic (Potential).
FT   TRANSMEM     65     85       Helical; Name=2; (Potential).
FT   TOPO_DOM     86    105       Extracellular (Potential).
FT   TRANSMEM    106    126       Helical; Name=3; (Potential).
FT   TOPO_DOM    127    147       Cytoplasmic (Potential).
FT   TRANSMEM    148    168       Helical; Name=4; (Potential).
FT   TOPO_DOM    169    195       Extracellular (Potential).
FT   TRANSMEM    196    216       Helical; Name=5; (Potential).
FT   TOPO_DOM    217    232       Cytoplasmic (Potential).
FT   TRANSMEM    233    253       Helical; Name=6; (Potential).
FT   TOPO_DOM    254    280       Extracellular (Potential).
FT   TRANSMEM    281    301       Helical; Name=7; (Potential).
FT   TOPO_DOM    302    339       Cytoplasmic (Potential).
FT   CARBOHYD     14     14       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    176    176       N-linked (GlcNAc...) (Potential).
FT   DISULFID    104    181       By similarity.
SQ   SEQUENCE   339 AA;  37839 MW;  087248DC3294D0D6 CRC64;
     MNGLEAALPS LTDNSSLAYS EQCGQETPLE NMLFACFYLL DFILAFVGNA LALWLFIWDH
     KSGTPANVFL MHLAVADLSC VLVLPTRLVY HFSGNHWPFG EIPCRLTGFL FYLNMYASIY
     FLTCISADRF LAIVHPVKSL KLRRPLYAHL ACAFLWIVVA VAMAPLLVSP QTVQTNHTVV
     CLQLYREKAS HHALASLAVA FTFPFITTVT CYLLIIRSLR QGPRIEKHLK NKAVRMIAMV
     LAIFLICFVP YHIHRSVYVL HYRGGGTSCA AQRALALGNR ITSCLTSLNG ALDPVMYFFV
     AEKFRHALCN LLCSKRLTGP PPSFEGKTNE SSLSARSEL
//
ID   F123C_MOUSE             Reviewed;         780 AA.
AC   Q6NS69; Q8BS82;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Protein FAM123C;
GN   Name=Fam123c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-780.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SIMILARITY: Belongs to the FAM123 family.
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DR   EMBL; BC070435; AAH70435.1; -; mRNA.
DR   EMBL; AK034979; BAC28901.1; -; mRNA.
DR   IPI; IPI00339467; -.
DR   RefSeq; NP_998892.1; NM_213727.2.
DR   UniGene; Mm.330696; -.
DR   ProteinModelPortal; Q6NS69; -.
DR   PRIDE; Q6NS69; -.
DR   Ensembl; ENSMUST00000052670; ENSMUSP00000054748; ENSMUSG00000045174.
DR   GeneID; 211383; -.
DR   KEGG; mmu:211383; -.
DR   CTD; 211383; -.
DR   MGI; MGI:3026939; Fam123c.
DR   eggNOG; roNOG04188; -.
DR   GeneTree; ENSGT00530000063529; -.
DR   HOGENOM; HBG125915; -.
DR   HOVERGEN; HBG098193; -.
DR   InParanoid; Q6NS69; -.
DR   OMA; TELAITM; -.
DR   OrthoDB; EOG4Z36D6; -.
DR   PhylomeDB; Q6NS69; -.
DR   NextBio; 373218; -.
DR   ArrayExpress; Q6NS69; -.
DR   Bgee; Q6NS69; -.
DR   Genevestigator; Q6NS69; -.
DR   InterPro; IPR019003; Uncharacterised_FAM123.
DR   Pfam; PF09422; WTX; 2.
PE   2: Evidence at transcript level;
FT   CHAIN         1    780       Protein FAM123C.
FT                                /FTId=PRO_0000320595.
SQ   SEQUENCE   780 AA;  83159 MW;  5A625E87A32EAD1D CRC64;
     MELRRGKTFI KSSVQISHEK LIDSPAKEDP DKWPLSLGEQ QRAYGEKSSQ TSPCSQGYGR
     CPNKEVLSDP EGGPVPLCGT TFKLVRKSKT HDSVPGAVKA AAPTGQMVGS TSFSETPGGQ
     RMIDYRHFVP QMPFVPAVAK SIPRKRISLK RSKKCFRNLF HMRRSKTENL ASLSAKGKNL
     SPSGVPAQQG TAFLSMGEGL GLDSLCQDLS DSEFLHDSPF DLCSALCEDV ASLKSFDSLT
     GCGEIFADGS SVPSVELKDG PESPAHSPQA LDCKTPCGPA QGGMEQLMSP AQNEASDFNK
     FWDSVNRSVQ QQQRALMGPW LTSPEGTETD QTRLDTSGLA ELPLFPCRGP PSGSKASSID
     TGTPKSEQPE SVSTSDEGYY DSFSPGLEEE KKEAASPGTP AATFPRDSYS GDALYELFYD
     PSEAPVGPIL DDDCVSESLS GPALGTPLSM CSFRVGAEEN LAPAPGPDLL SQGFLQSTWK
     GKECLLKLCD TELAITMGIV NWLRRTPPAT SPTPASTPAP TPALVLREPA APPDPHRVLR
     GASVGVKGRE DQATTCFPPS RQEPWAHSGT KNLLVRECEV LGEPARGSKT PSKDDSLEEG
     TQDFSEGQSS SEATMTSISG NNKAVTSATC LSSQKELGTP GNLRYSQGPL RPGHRGSALD
     PGPMLVGCVT HVAALQIYPD SNSPRQDKGN GLFWKPQAWG PNILQKNPIS SKPNEAAGCG
     LSSSASPQDQ KCRDLFLDLN QLKLEPSRLG PQACSSVDSQ PQQLCPRAPE QVPHRGSVGS
//
ID   F134A_MOUSE             Reviewed;         541 AA.
AC   Q6NS82; Q3TA48; Q3TMF7; Q8BSD3; Q8CHY1; Q8R0Q3;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 2.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Protein FAM134A;
GN   Name=Fam134a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, Embryo, Lung, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, Kidney, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-274; SER-276 AND
RP   SER-278, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=19838196; DOI=10.1038/ng.464;
RA   Kurth I., Pamminger T., Hennings J.C., Soehendra D., Huebner A.K.,
RA   Rotthier A., Baets J., Senderek J., Topaloglu H., Farrell S.A.,
RA   Nuernberg G., Nurnberg P., De Jonghe P., Gal A., Kaether C.,
RA   Timmerman V., Huebner C.A.;
RT   "Mutations in FAM134B, encoding a newly identified Golgi protein,
RT   cause severe sensory and autonomic neuropathy.";
RL   Nat. Genet. 41:1179-1181(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6NS82-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q6NS82-2; Sequence=VSP_014550, VSP_014551;
CC       Name=3;
CC         IsoId=Q6NS82-3; Sequence=VSP_014551;
CC   -!- TISSUE SPECIFICITY: Mainly expressed in the central nervous system
CC       and in parenchymatous organs including liver, lung and kidney.
CC   -!- SIMILARITY: Belongs to the FAM134 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC28789.1; Type=Frameshift; Positions=249, 340;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK034667; BAC28789.1; ALT_FRAME; mRNA.
DR   EMBL; AK160400; BAE35769.1; -; mRNA.
DR   EMBL; AK165957; BAE38485.1; -; mRNA.
DR   EMBL; AK172093; BAE42822.1; -; mRNA.
DR   EMBL; BC026519; AAH26519.1; -; mRNA.
DR   EMBL; BC038286; AAH38286.1; -; mRNA.
DR   EMBL; BC070406; AAH70406.1; -; mRNA.
DR   IPI; IPI00421012; -.
DR   IPI; IPI00607924; -.
DR   IPI; IPI00607951; -.
DR   RefSeq; NP_739561.2; NM_170755.2.
DR   UniGene; Mm.273062; -.
DR   ProteinModelPortal; Q6NS82; -.
DR   PhosphoSite; Q6NS82; -.
DR   PRIDE; Q6NS82; -.
DR   Ensembl; ENSMUST00000060113; ENSMUSP00000056972; ENSMUSG00000049339.
DR   Ensembl; ENSMUST00000097694; ENSMUSP00000095300; ENSMUSG00000049339.
DR   GeneID; 227298; -.
DR   KEGG; mmu:227298; -.
DR   UCSC; uc007bnt.1; mouse.
DR   UCSC; uc007bnu.1; mouse.
DR   CTD; 227298; -.
DR   MGI; MGI:2388278; Fam134a.
DR   eggNOG; roNOG15187; -.
DR   GeneTree; ENSGT00530000063240; -.
DR   HOGENOM; HBG715424; -.
DR   HOVERGEN; HBG093247; -.
DR   InParanoid; Q6NS82; -.
DR   OMA; CSPGGPV; -.
DR   OrthoDB; EOG4KH2VK; -.
DR   NextBio; 378544; -.
DR   ArrayExpress; Q6NS82; -.
DR   Bgee; Q6NS82; -.
DR   Genevestigator; Q6NS82; -.
DR   GermOnline; ENSMUSG00000049339; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Alternative splicing; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    541       Protein FAM134A.
FT                                /FTId=PRO_0000089347.
FT   TRANSMEM     10     30       Helical; (Potential).
FT   TRANSMEM     87    107       Helical; (Potential).
FT   TRANSMEM    199    219       Helical; (Potential).
FT   COMPBIAS     38     43       Poly-Ala.
FT   COMPBIAS     92     95       Poly-Ser.
FT   COMPBIAS    477    480       Poly-Glu.
FT   COMPBIAS    517    520       Poly-Pro.
FT   MOD_RES     274    274       Phosphothreonine.
FT   MOD_RES     276    276       Phosphoserine.
FT   MOD_RES     278    278       Phosphoserine.
FT   MOD_RES     301    301       Phosphothreonine (By similarity).
FT   MOD_RES     303    303       Phosphoserine (By similarity).
FT   MOD_RES     306    306       Phosphoserine (By similarity).
FT   MOD_RES     339    339       Phosphoserine (By similarity).
FT   MOD_RES     342    342       Phosphoserine (By similarity).
FT   VAR_SEQ       1    226       Missing (in isoform 2).
FT                                /FTId=VSP_014550.
FT   VAR_SEQ     431    467       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_014551.
FT   CONFLICT    139    139       G -> R (in Ref. 1; BAC28789).
FT   CONFLICT    515    515       V -> L (in Ref. 1; BAC28789).
FT   CONFLICT    525    525       S -> C (in Ref. 1; BAE38485).
SQ   SEQUENCE   541 AA;  57542 MW;  88C99862C92BAF10 CRC64;
     MASSGGGNTG AGGTSGLGLG LGLSLGMGEA TGDAEEEAAA AEAVGRLATS LWLRLRGWEA
     VLAAAQRLLV WEKPLHSLVT AATLNGLFWL LSSSSLRPFF LLSISLLTYF LLDLWHPRFL
     PDVSAPPPEE PHSDSEGAGS GAQPHLLSVP ELCRYLAESW LTFQIHLQEL LQYKRQNPAQ
     FCARGCAACA VLAVLGHYVP GVMISYIVLL SILLWPLVVY HELIQRMYTR LEPLLMQLDY
     SMKAEADALH HKHDKRKRQG KSAPPAGDEP LAETESESEA ELAGFSPVVD VKKTALALAI
     TDSELSDEEA SILESGGFSV SRATTPQLTD VSEDLDQQSL PSEPEEALNR ELGEGEETEL
     ASPEDLLSAP PALSKQALDT EEEGAADKEA LLQLSSPLHF VNTHFNGAGS PQDGVKCPPG
     APVKTLSPEA VSGDLMAPSS TLSPQLCLAE SGPVTPLSPS VLPSLPQDSP QPLAAPEEEE
     ALTTEDFELL DQGELEQLNA ELGLGPEMPP KPPDVLPPPP LGADSHSLVQ SDQEAHAEVE
     P
//
ID   SPKAP_MOUSE             Reviewed;        1687 AA.
AC   Q6NSW3; Q6PAM6; Q6PAP7; Q80TA7; Q80XT3; Q8BYQ9; Q8BZL6; Q8C1G7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   08-MAR-2011, entry version 43.
DE   RecName: Full=A-kinase anchor protein SPHKAP;
DE   AltName: Full=SPHK1-interactor and AKAP domain-containing protein;
GN   Name=Sphkap; Synonyms=Kiaa1678;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-868 (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 899-1687 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon, Hypothalamus, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain, Embryo, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 288-1687 (ISOFORM 1).
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
CC   -!- FUNCTION: Anchoring protein that mediates the subcellular
CC       compartmentation of cAMP-dependent protein kinase (PKA type II).
CC       May act as a converging factor linking cAMP and sphingosine
CC       signaling pathways. Plays a regulatory role in the modulation of
CC       SPHK1 (By similarity).
CC   -!- SUBUNIT: Interacts with RII subunit of PKA. Interacts with SPHK1
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q6NSW3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NSW3-2; Sequence=VSP_031714;
CC       Name=3;
CC         IsoId=Q6NSW3-3; Sequence=VSP_031713;
CC       Name=4;
CC         IsoId=Q6NSW3-4; Sequence=VSP_031713, VSP_031715, VSP_031716;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: RII-binding site, predicted to form an amphipathic helix,
CC       could participate in protein-protein interactions with a
CC       complementary surface on the R-subunit dimer (By similarity).
CC   -!- SIMILARITY: Belongs to the AKAP110 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC25605.1; Type=Frameshift; Positions=975;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK034183; BAC28620.1; -; mRNA.
DR   EMBL; AK038638; BAC30075.1; -; mRNA.
DR   EMBL; AK019735; BAC25605.1; ALT_FRAME; mRNA.
DR   EMBL; BC042654; AAH42654.1; -; mRNA.
DR   EMBL; BC060165; AAH60165.1; -; mRNA.
DR   EMBL; BC060217; AAH60217.1; -; mRNA.
DR   EMBL; BC069832; AAH69832.1; -; mRNA.
DR   EMBL; AK122538; BAC65820.1; -; mRNA.
DR   IPI; IPI00276671; -.
DR   IPI; IPI00454045; -.
DR   IPI; IPI00624796; -.
DR   IPI; IPI00886265; -.
DR   RefSeq; NP_766018.3; NM_172430.3.
DR   UniGene; Mm.154303; -.
DR   PhosphoSite; Q6NSW3; -.
DR   PRIDE; Q6NSW3; -.
DR   Ensembl; ENSMUST00000056934; ENSMUSP00000052336; ENSMUSG00000026163.
DR   GeneID; 77629; -.
DR   KEGG; mmu:77629; -.
DR   UCSC; uc007bsq.1; mouse.
DR   CTD; 77629; -.
DR   MGI; MGI:1924879; Sphkap.
DR   GeneTree; ENSGT00530000063606; -.
DR   HOVERGEN; HBG108508; -.
DR   OrthoDB; EOG4CRKZ6; -.
DR   NextBio; 347260; -.
DR   ArrayExpress; Q6NSW3; -.
DR   Bgee; Q6NSW3; -.
DR   CleanEx; MM_SPHKAP; -.
DR   Genevestigator; Q6NSW3; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR018292; AKAP_110_C.
DR   InterPro; IPR008382; SPHK1-interactor_AKAP_110.
DR   PANTHER; PTHR10226; AKAP_110; 1.
DR   Pfam; PF05716; AKAP_110; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm.
FT   CHAIN         1   1687       A-kinase anchor protein SPHKAP.
FT                                /FTId=PRO_0000320667.
FT   REGION      914    931       PKA-RII subunit binding domain (By
FT                                similarity).
FT   VAR_SEQ       1     10       MDVNSRLSVQ -> MSTPGFLCKAMWVVEPNSATCLSAALP
FT                                VKRHCQES (in isoform 3 and isoform 4).
FT                                /FTId=VSP_031713.
FT   VAR_SEQ    1533   1561       Missing (in isoform 2).
FT                                /FTId=VSP_031714.
FT   VAR_SEQ    1561   1561       N -> K (in isoform 4).
FT                                /FTId=VSP_031715.
FT   VAR_SEQ    1562   1687       Missing (in isoform 4).
FT                                /FTId=VSP_031716.
FT   CONFLICT     22     22       P -> S (in Ref. 1; BAC28620/BAC30075).
FT   CONFLICT    104    104       N -> S (in Ref. 1; BAC28620).
FT   CONFLICT    137    137       P -> L (in Ref. 1; BAC28620/BAC30075).
FT   CONFLICT    574    574       K -> R (in Ref. 2; AAH69832).
FT   CONFLICT    585    585       D -> G (in Ref. 1; BAC28620).
FT   CONFLICT    807    807       A -> G (in Ref. 1; BAC28620).
FT   CONFLICT    838    838       R -> Q (in Ref. 1; BAC28620).
FT   CONFLICT    884    884       V -> A (in Ref. 2; AAH69832).
FT   CONFLICT    957    957       P -> L (in Ref. 2; AAH69832).
FT   CONFLICT    974    974       G -> A (in Ref. 1; BAC25605).
FT   CONFLICT   1010   1010       S -> F (in Ref. 2; AAH69832).
FT   CONFLICT   1167   1167       S -> C (in Ref. 1; BAC30075).
FT   CONFLICT   1203   1203       D -> G (in Ref. 2; AAH69832).
FT   CONFLICT   1212   1212       S -> C (in Ref. 1; BAC30075).
SQ   SEQUENCE   1687 AA;  185095 MW;  DB2E129AB9036F6E CRC64;
     MDVNSRLSVQ SNVESPLMHE GPEPQQITSS AAGNLAGSIT ACKKVLRSNS LLESTDYWLQ
     NQRTPCQIGF VEDESENCAS VCFVNLDVNK DACITENLQQ KLVNVSPDLP NLISSMNVQQ
     PKENEIVLLS GLASGNPQAD FDVSQCPWLP DICLVQCARG NRPNSTNCII FEINKFLIGL
     EVVQERQLHL ETNVLKLEDD TNCSLSSIEE DFLTASEHLE EEIEVDDCRS GLENTNVSAN
     VLESKKPKET TQEGWDYHKE KLHCALGEKH IRKHRTPSTK TEGSKENTEE NTSLKSLNRL
     VRPSHLKSEV AGNKQLATNY SYPENIKGEL ETSQMLFIPR DAYLSMVKKD VLSPCSVLSE
     QGGSHRDHDV TPNPLPPVQN GEASTGEYAT NLAESVMQDA FIRLSQSQPT LPQESAVSFS
     MRSALLPSGC CTKDMVVPRS WNELPKIVIV QSPDGSDTVP EPNVSSWPDM EFVETSGIFS
     ADSSSRPTQS ALEVALACAA TVIGTISSPQ ATERFAMEQE SLVSTYAQRG TGVQQTQVPQ
     AFMAPSTTEY SFPSALCGMT QVASAVAVCG LCEKEEATCP VAPTDLLPTS GASEEISSIG
     SLVMERSTEL GKEAIAEALL REATLILARP DAYSSLGELL ESVNQRIIET TSKTQTLCTE
     SVQRNELAHT LSNVILKHSV DELHQKTTMA HPTDERHPCG TLDTLMESVN QLLHNVICFT
     FKKMNHIVTL SEHPSFDQAA GQAWVKAFAC PSSQPLSNAH GTGLVIRNLV EDASPKSNKG
     GARPELVNNP RLQSEFSCSH RMFDSTAKSF PKEIYLKGIM GEDTRNPHHT LNYDSNERRA
     STDLGKLTTA SEGCSGFQET EDSIVPNTQE KYICATPLNN EAQVNLSLLG DDLSVPAQST
     LEAKQSEVYG ITDFAEELAE TVVSMATEIA AICLDNSNGK QPWFCAWKRG NEFLTAPNGS
     CRSLKRKKEN SSAGSTVRKH KPPRLSEIKR KADEHPELKE KLMNRVMDES MNLEDIPDSV
     STFANEVAAK IMNLTEFSMV DGVWQGQSCS RTRLLGGDRW NRLKASSCES IPEEDSEARV
     FVNSLGLMST LSQPVSRASS VSKQSSCESI TDEFSRFMVK QMENEGRGFE LLLDYYAGKN
     ASSIMSSAMQ QACQKNDHLN VRPSCPSKQS STESITEEFY RYMLRDIAKE SKDGASSRRS
     SHDWTTGLLS PSTRSPLCYR QSSMPDSRSP CSRLTVNAPV KANSLDGFAQ NCPQDSVNVQ
     PVSRASSSGL CKSDSCLYRR SGTDQITNML IHETWASSIE ALMRKNKIIA DDSEAANASP
     GPVSSGSPLQ VEKNANRLAT SKGHRGPTLL VQESVDYQRK DAVTEGNHSP VSSPGKTAPV
     KKPSDFDPRR ETSACHNAAG LNSPRRSLCS RDVPLIQIET DQKEECIGEP GPFLSQSGSL
     EETEGHQPEE TIPDVARNED TAPSTCQSSR DSLETSGEVE VEVLKEDIPR DESRNPPSSS
     EESTGSWSQL ANEEDIPDDT SSFLQLSERS MSNGNSSGTS SLGIMDLDIY QESIPSSPMI
     NELVEEKEIL KEQSESIKEH ASGLPGRAAS PQRSLLVINF DLEPECPDAE LRATLQWIAA
     SELGIPTIYF KKSQESRIEK FLDVVKLVQQ KSWKVGDIFH AVVQYCKLHA EQKERTPSLF
     DWLLELG
//
ID   Q6NV66_MOUSE            Unreviewed;      1788 AA.
AC   Q6NV66;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   SubName: Full=Zinc finger protein 646;
GN   Name=Zfp646;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and C57BL/6; TISSUE=Embryonic Germ Cell, and Head;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC068300; AAH68300.1; -; mRNA.
DR   EMBL; BC079907; AAH79907.1; -; mRNA.
DR   IPI; IPI00221926; -.
DR   RefSeq; NP_766337.2; NM_172749.4.
DR   UniGene; Mm.425491; -.
DR   ProteinModelPortal; Q6NV66; -.
DR   SMR; Q6NV66; 1636-1745.
DR   PhosphoSite; Q6NV66; -.
DR   PRIDE; Q6NV66; -.
DR   Ensembl; ENSMUST00000050383; ENSMUSP00000052641; ENSMUSG00000049739.
DR   GeneID; 233905; -.
DR   KEGG; mmu:233905; -.
DR   UCSC; uc009jxb.1; mouse.
DR   CTD; 233905; -.
DR   MGI; MGI:3665412; Zfp646.
DR   eggNOG; roNOG14032; -.
DR   HOGENOM; HBG126795; -.
DR   HOVERGEN; HBG067847; -.
DR   InParanoid; Q6NV66; -.
DR   OMA; TLDHRPY; -.
DR   OrthoDB; EOG4X97GW; -.
DR   PhylomeDB; Q6NV66; -.
DR   NextBio; 381947; -.
DR   ArrayExpress; Q6NV66; -.
DR   Bgee; Q6NV66; -.
DR   Genevestigator; Q6NV66; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 16.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 29.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 27.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 27.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1788 AA;  196805 MW;  E6CB9191590E09F3 CRC64;
     MEDMPLSFSC SDCQRHFPNL PELARHRELR HSSAKQDGEE ADGIPHPYGS HPENLANHQR
     NHETLFFPCT TCGKDFSNRL ALQSHMRTHA PESHRRHGPP HAMETAPHLG SETMATDSWG
     QRLGSGEGWE NQTKLVRETH DWESGADPRA ASGTWEDPPT KQRQGLEMQP DSKGGTADWV
     PAVSSEGASP LPTPASNLLS NLEQYLAESV VNFTEAQEPT EPLPTEGERK YRCSECGKTY
     KHAGSLTNHR QSHTLGIYPC SICFKEFSNL MALKNHSRLH AQYRPYHCPH CPRAFRLPRD
     LLEHQQSHEG LKQEQPWEDK EMPTTNGHAD ERSWGQLSKT GMLNGSGELS SSGQLEDGGS
     EEYRPFCCGD CGRTYRHAGS LINHRKSHQT GIYPCSICSK QLFNAAALKN HIRAHHRPRQ
     GAGEGGQSSV SSTALTSAEN TPKVDEVPTA SLDHRPYKCN ECGRAYRHRG SLVNHRHSHR
     TGEYQCSLCP RKYPNLMALR NHVRVHCKAT RRSTDPGTEG SPSPVKKEQH DPVGMEAAFH
     GDEEHACKRE EEATSNPSMA DRTVPQVCSI CGMLFEDLKS LEHHSVTHRE GEKSRTDSTV
     SPTRTFACQD CGKSYRHSGS LINHRQTHQT GDFSCGACAK HFHTMAAMKS HLRRHSRQWN
     RRRQKQDSGT GEVATLPPGG AWTLKLENDE DPDSSQDPLG ESPCETEDNL ERDGDCLQAG
     SRGNECVLKR EEACFLGDKE GTEEGLEERE ACFLDDLGTP GDECNETGFC GGLPGMDSDR
     KRGICHSDSS SHPADADTVW KAAATHTCSD CGDSFSHAAG LLSHRSCHPP GIYQCSLCPK
     EFDSLPALRS HFQTHRPGEV ASAQPFLCCL CGMIFPGRTG YRRHLRQAHG ASAMTEGSEE
     EEEGTAETAS THSPPLQLSE AELLNQLQRE VEALDGAGYG HICGCCGQTY DDLGSLERHH
     QSQSSSNRTE NVPSHLEGAG DATEMVADHG FEGTVTSVSE EGGDIKSEEG VGGTVADSLC
     MQAGESFLES HPRPFQCNQC GKTYRHGGSL VNHRKIHQTG DFICPVCSRC YPNLAAYRNH
     LRNHPRCKGS EPQMGPISEA GGCSEPQNAA EAGQEQAVIG QLQEELKVEP LEELAGVKEE
     VWEGTAVKEE ELEQELETGC QTEVTSERPF SCEVCGRTYK HAGSLINHRQ SHQTGHFGCQ
     ACSKGFSNLM SLKNHRRIHA DPRQFRCSEC GKAFRLRKQL ANHQRVHAER RRSRGTQKLT
     REDRPFRCGQ CGRTYRHAGS LMNHQCNPEA SRYSCPFCFK TYSNRTALKD HQRVHSDSQQ
     RRQSGCPQRA AAVRCTLCGC GFSGQGSLEQ HLQEHEDTKL EVASGQGGQH ATEGSEENLD
     DWGLEGRSDG TEVLQVEHET KRPGGHSQSP SSPACSGGTE STQQVGKVDG SQGDRGQMNH
     NGAWVLQDQL TKPEGKLEDT VSRNPCHLSE SQSNGPTLRY RDSWKGADSG SQLQPESHCC
     SQCGKAYCQP DGLLNPSING KDCHICLLCS KEFLNPVTTE IHNHTTAQRF ACSNCSKVCE
     SHSELATHMK THAVEHSQMS GQMEKTRGPQ AGMAEVGPPG PGKAQEAPSE LPGDPEENGV
     PANGGQGIHF PAAEDKERPF CCAQCGRSYR HAGSLLNHQK AHTIGLYPCS LCPKLLPNLL
     SLKNHSRTHT DPKRYSCNIC GKAFRTAARL QGHGRVHAPQ EGPFTCSHCP RRFRHRISFL
     RHQQQHQEEW PVSSSGASVA PAASREDSST ASLPNPSPQW PADLSLSL
//
ID   CB044_MOUSE             Reviewed;         663 AA.
AC   Q6NV72; Q3U2S5; Q8C9V8;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=WD repeat-containing protein C2orf44 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=129/Sv X 129SvCp; TISSUE=Embryonic stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6NV72-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NV72-2; Sequence=VSP_027716;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 2 WD repeats.
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DR   EMBL; AK040407; BAC30587.1; -; mRNA.
DR   EMBL; AK155130; BAE33065.1; -; mRNA.
DR   EMBL; BC068281; AAH68281.1; -; mRNA.
DR   IPI; IPI00227722; -.
DR   IPI; IPI00454099; -.
DR   RefSeq; NP_001164329.1; NM_001170858.1.
DR   RefSeq; NP_775592.2; NM_173416.3.
DR   UniGene; Mm.146087; -.
DR   ProteinModelPortal; Q6NV72; -.
DR   PhosphoSite; Q6NV72; -.
DR   PRIDE; Q6NV72; -.
DR   Ensembl; ENSMUST00000053034; ENSMUSP00000054102; ENSMUSG00000051721.
DR   Ensembl; ENSMUST00000085793; ENSMUSP00000082948; ENSMUSG00000051721.
DR   GeneID; 238037; -.
DR   KEGG; mmu:238037; -.
DR   MGI; MGI:3040699; BC068281.
DR   eggNOG; roNOG08832; -.
DR   GeneTree; ENSGT00390000001660; -.
DR   HOGENOM; HBG713863; -.
DR   HOVERGEN; HBG055062; -.
DR   InParanoid; Q6NV72; -.
DR   OMA; HSYIWDS; -.
DR   OrthoDB; EOG4JT050; -.
DR   PhylomeDB; Q6NV72; -.
DR   NextBio; 383648; -.
DR   ArrayExpress; Q6NV72; -.
DR   Bgee; Q6NV72; -.
DR   CleanEx; MM_BC068281; -.
DR   Genevestigator; Q6NV72; -.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR   PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Phosphoprotein; Repeat; WD repeat.
FT   CHAIN         1    663       WD repeat-containing protein C2orf44
FT                                homolog.
FT                                /FTId=PRO_0000299502.
FT   REPEAT       55     98       WD 1.
FT   REPEAT      154    194       WD 2.
FT   COILED      549    577       Potential.
FT   MOD_RES     291    291       Phosphoserine (By similarity).
FT   MOD_RES     460    460       Phosphoserine (By similarity).
FT   MOD_RES     493    493       Phosphoserine (By similarity).
FT   MOD_RES     502    502       Phosphoserine (By similarity).
FT   MOD_RES     524    524       Phosphothreonine (By similarity).
FT   VAR_SEQ     600    663       NPCSVGPTERRAVLLCDGKLRLSTVQQMFGLHLVEMLHEVL
FT                                SSIPSNHMVTHNLHGPGGLFWSV -> VQSFLRNFHYTGSS
FT                                GIQSVLPATLWGRWGGRESEAQ (in isoform 2).
FT                                /FTId=VSP_027716.
FT   CONFLICT    150    150       K -> T (in Ref. 2; AAH68281).
FT   CONFLICT    269    269       S -> F (in Ref. 1; BAC30587).
FT   CONFLICT    485    485       R -> G (in Ref. 2; AAH68281).
FT   CONFLICT    567    567       Y -> H (in Ref. 2; AAH68281).
SQ   SEQUENCE   663 AA;  72268 MW;  62F299D3325A4D42 CRC64;
     MELGNGKLPR TGLNSLNQAV HPTWGLAWTD GNRVVLTDLQ LHSGEAKFGD SRVIGRFESV
     CGVCWAPVRT VRSPALLAIQ HRKLVSVWQL CPSTAGASKW QASQTSEVRE SLPILPRGCV
     WHPKDAVLTV LTAQGVSIFP NVHQDGSRVK VDVNTKGRVY CACWTLDGQR LVVAIDSNLH
     SYIWDSSQKS LHSCSFCPVF PVNCSIRSIE ATGNSQVAIA TELPLHKLCS LNASEALDGP
     PNGDDGSVHT RPVDEQVATM DMNSGVTVSP FSVPLDLTHI HFNPSQAEQS SLICLRKKDY
     LTGTGQDSSH LILVTFKKAI TITKKVAIPG ILVPDLIAFN LTAELVAVAS NTCNVILIYS
     AAPSSMPNIQ QIQLESNERP KGICFLTDRL LLIAVGKQKP SEAAFLPSSE YGQYTVRLIV
     REMAQGSESS GTSAESQGAY SDFTALLSKA DREKFTDSLS PGSSPLSQGL LLTPNSSTQS
     GRSGRALIQE IKSPLSPLSS DSVVHETLHR PPWLCPALPR PSRTPEHTST PELNSPQREN
     LQKEKETCPL SRELEILSRH LVAMQQYLSE LTGFLHKEKR VAPAYPPSQD APYVHLIYQN
     PCSVGPTERR AVLLCDGKLR LSTVQQMFGL HLVEMLHEVL SSIPSNHMVT HNLHGPGGLF
     WSV
//
ID   Q6NVE5_MOUSE            Unreviewed;      1067 AA.
AC   Q6NVE5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   SubName: Full=cDNA sequence BC068157;
GN   Name=BC068157;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
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DR   EMBL; BC068157; AAH68157.1; -; mRNA.
DR   IPI; IPI00410994; -.
DR   RefSeq; NP_997086.2; NM_207203.2.
DR   UniGene; Mm.193272; -.
DR   PhosphoSite; Q6NVE5; -.
DR   PRIDE; Q6NVE5; -.
DR   Ensembl; ENSMUST00000070717; ENSMUSP00000065481; ENSMUSG00000064125.
DR   GeneID; 73072; -.
DR   KEGG; mmu:73072; -.
DR   UCSC; uc009ktg.1; mouse.
DR   MGI; MGI:3605626; BC068157.
DR   eggNOG; roNOG16015; -.
DR   InParanoid; Q6NVE5; -.
DR   OrthoDB; EOG4DZ1V8; -.
DR   NextBio; 337413; -.
DR   ArrayExpress; Q6NVE5; -.
DR   Bgee; Q6NVE5; -.
DR   Genevestigator; Q6NVE5; -.
PE   1: Evidence at protein level;
SQ   SEQUENCE   1067 AA;  107617 MW;  561B9289E89FE824 CRC64;
     MDKRDSVKSG TAPRMPSSRP PGLLTPRPPS GSARPPPPVT TAALRVLEAN GAMGRRSLVE
     RAPGVCKAAL PQTSKAALPQ TSKAALPQTS KAALPQTSKA ALPQTTIHGA PARSAGAGPR
     SPANRPPASG KGERAPMKTP GQGSISSPGR ASSGIARPGP VVQKRLQPPT KEPSARGKTP
     ETPKRNTLNS GTRRVLSADS LGPTSGAPSP AITRRSRAPA TEVGLPQPAP SARQRPLTTE
     AARKPGSSAS EPSATELSPA FRRRSVAGGS LQKPVSRSLI PSATPQLSPS RSGVSPRVTP
     RAPAHTSQLK SKGQQALHPT QTTVPRKNKP SVQSLIPASS LVTPTPPGAS SVQGPDDPSQ
     TTLPPSPPTT PPLSLQNLPS TPATPPLLAP PTSLDTEEAS DSPPPRAVIS SSPPPLIQNM
     PPNQASSATL PQETLSAMPF SPAPLSLASS PPQLLPSPPI SPQNLPTSLV TSSQLPLSTP
     FRANFSESPP LPRATLANRT TPSLQDPLFL AISPPVSSST SISPPLPTSS VVTPPLRLPL
     SQTLPTSQAS LLTLPPSLAS SPQPATPPPL ALSPLSTQLS TGSPSLQASP SFLPTPPMQP
     RALPSPSLQA PPVTYPLPLS SPPASPPLPA LLSPPASPPL ESPLSPSASP SSPLATPPPE
     APPSLGSPTL SPLATPPPQT PPLAFPPLPA STSSLDTATC FPQGPLLALP PLQTSPSPLT
     IPCPQTPPSL ALPSLQSPSS PLATATPPLQ IPLVVLPTLQ TPPSPLTTFP PGVPPGLTSP
     VVQPPSPPAS PPLQAPRRPP TPGPDVPITG PRLTLALAPA PPPPPSRSPS STLSGPDLAG
     HSSSATSTPE ELRGYDSGPE GCPTISPAPD ADLAACHPAS WSRSSAPQLA VRSTPGVPLP
     WPPTAGPGSS DGLCTIYESE GPESVAPTPG SLDVEPEPMP GSGSAKVTAA DCAGASSRSP
     KSARLGELPL GALQASVVQH LLSRTLLLAA AEGAAVGCEG SSGGSGVGGV SGGSRAPLSD
     AELGRWAELL SPLDESRASI TSVTSFSPDD VASPQGDWTV VEVETFH
//
ID   WDR44_MOUSE             Reviewed;         915 AA.
AC   Q6NVE8; Q3UT13; Q8BTS1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=WD repeat-containing protein 44;
DE   AltName: Full=Rabphilin-11;
GN   Name=Wdr44;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-259 (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Egg, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346; THR-351; SER-472;
RP   SER-473 AND SER-474, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264; SER-472; SER-473
RP   AND SER-474, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Downstream effector for RAB11. May be involved in
CC       vesicle recycling (By similarity).
CC   -!- SUBUNIT: Interacts with the GTP-bound form of RAB11 when membrane-
CC       associated. Does not bind to other Rab and Rho small G proteins
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, perinuclear
CC       region. Endosome membrane. Golgi apparatus, trans-Golgi network.
CC       Note=Colocalized with RAB11 along microtubules oriented toward
CC       lamellipodia (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6NVE8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NVE8-2; Sequence=VSP_021811;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 8 WD repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK088885; BAC40631.2; -; mRNA.
DR   EMBL; AK139877; BAE24167.1; -; mRNA.
DR   EMBL; BC068151; AAH68151.1; -; mRNA.
DR   EMBL; BC049191; AAH49191.1; -; mRNA.
DR   IPI; IPI00308560; -.
DR   IPI; IPI00676517; -.
DR   RefSeq; NP_780389.2; NM_175180.2.
DR   UniGene; Mm.423; -.
DR   HSSP; P38262; 1R5M.
DR   ProteinModelPortal; Q6NVE8; -.
DR   SMR; Q6NVE8; 496-816.
DR   PhosphoSite; Q6NVE8; -.
DR   PRIDE; Q6NVE8; -.
DR   Ensembl; ENSMUST00000035766; ENSMUSP00000044616; ENSMUSG00000036769.
DR   Ensembl; ENSMUST00000101670; ENSMUSP00000099193; ENSMUSG00000036769.
DR   GeneID; 72404; -.
DR   KEGG; mmu:72404; -.
DR   UCSC; uc009suw.1; mouse.
DR   UCSC; uc009suy.1; mouse.
DR   CTD; 72404; -.
DR   MGI; MGI:1919654; Wdr44.
DR   eggNOG; roNOG12004; -.
DR   HOGENOM; HBG446429; -.
DR   HOVERGEN; HBG080376; -.
DR   InParanoid; Q6NVE8; -.
DR   OMA; DHTEVLL; -.
DR   OrthoDB; EOG4K6G3H; -.
DR   NextBio; 336206; -.
DR   ArrayExpress; Q6NVE8; -.
DR   Bgee; Q6NVE8; -.
DR   CleanEx; MM_WDR44; -.
DR   Genevestigator; Q6NVE8; -.
DR   GermOnline; ENSMUSG00000036769; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 3.
DR   Pfam; PF00400; WD40; 4.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Endosome;
KW   Golgi apparatus; Membrane; Phosphoprotein; Repeat; WD repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    915       WD repeat-containing protein 44.
FT                                /FTId=PRO_0000262770.
FT   REPEAT      511    550       WD 1.
FT   REPEAT      607    645       WD 2.
FT   REPEAT      647    687       WD 3.
FT   REPEAT      692    731       WD 4.
FT   REPEAT      742    781       WD 5.
FT   REPEAT      786    825       WD 6.
FT   REPEAT      840    880       WD 7.
FT   REPEAT      882    915       WD 8.
FT   REGION        2    173       Binding activity.
FT   COILED      114    139       Potential.
FT   COMPBIAS    213    259       Pro-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       5      5       Phosphoserine (By similarity).
FT   MOD_RES      27     27       Phosphoserine (By similarity).
FT   MOD_RES      50     50       Phosphoserine (By similarity).
FT   MOD_RES      90     90       Phosphoserine (By similarity).
FT   MOD_RES     161    161       Phosphothreonine (By similarity).
FT   MOD_RES     164    164       Phosphoserine (By similarity).
FT   MOD_RES     165    165       Phosphoserine (By similarity).
FT   MOD_RES     221    221       Phosphothreonine (By similarity).
FT   MOD_RES     264    264       Phosphoserine.
FT   MOD_RES     273    273       Phosphothreonine (By similarity).
FT   MOD_RES     346    346       Phosphoserine.
FT   MOD_RES     351    351       Phosphothreonine.
FT   MOD_RES     405    405       Phosphoserine.
FT   MOD_RES     472    472       Phosphoserine.
FT   MOD_RES     473    473       Phosphoserine.
FT   MOD_RES     474    474       Phosphoserine.
FT   MOD_RES     563    563       Phosphoserine (By similarity).
FT   MOD_RES     565    565       Phosphoserine (By similarity).
FT   MOD_RES     567    567       Phosphoserine (By similarity).
FT   MOD_RES     570    570       Phosphoserine (By similarity).
FT   MOD_RES     785    785       Phosphotyrosine (By similarity).
FT   MOD_RES     801    801       Phosphothreonine (By similarity).
FT   MOD_RES     802    802       Phosphotyrosine (By similarity).
FT   VAR_SEQ       1    478       Missing (in isoform 2).
FT                                /FTId=VSP_021811.
FT   CONFLICT    629    629       D -> E (in Ref. 1; BAE24167).
SQ   SEQUENCE   915 AA;  101555 MW;  B5FDF8A4C87295DC CRC64;
     MASESDTEEF YDAPEDVHLG TGYPVGSPGK VGLLSFKEAE NTANQAGNES PVQELRQDVS
     KKIIESIIEE SQKVLQLEDD SLDSKGKGLS DEATAGPSVA GTEFSNIPGL LAIEHELQQD
     SEKAESQNVA EESELETQKC FPSDETCEKS EKTVDETDNL TEVSSGEQLD ASGLEAETLN
     KEALEVKEGD VLDPASLDTL STTDFAAVEE VAPAKPPRHL TPEPDIVAST KKPVPARPPP
     PTNFPPPRPP PPSRPAPPPR KKKSELEFEA LKTPDLDVPK ENITSDSLLT TNMASENTVR
     DSLPSLDLAS ATSGDKIVTA QENGKAPDVQ TVAGEVMGPQ RPRSNSGREL TDEEILASVM
     IKNLDTGEEI PLSLAEEKLP TGINPLTLHI MRRTKEYVSN DATQSDDEEK LQSQQTDTDG
     GRLKQKTTQL KKFLGKSVKR AKHLAEEYGE RAINKVKSVR DEVFHTDQDD PSSSDDEGMP
     YTRPVKFKAA HGFKGPYDFD QIKVVQDLSG EHMGAVWTMK FSHCGRLLAS AGQDNIVRIW
     ALKNAFDYFN NMRMKYNTEG RVSPSPSQES LSSSKSDTDM GVCSGTDEDP DDKNAPFRQR
     PFCKYKGHTA DLLDLSWSKN YFLLSSSMDK TVRLWHISRR ECLCCFQHID FVTAIAFHPR
     DDRYFLSGSL DGKLRLWNIP DKKVALWNEV DGQTKLITAA NFCQNGKYAV IGTYDGRCIF
     YDTEHLKYHT QIHVRSTRGR NKVGRKITGI EPLPGENKIL VTSNDSRIRL YDLRDLSLSM
     KYKGYVNSSS QIKASFSHDF TYLVSGSEDK YVYIWSTYHD LSKFTSVRRD RNDFWEGIKA
     HNAVVTSAIF APNPSLMLSL DVQSEKLEGI DKYEDAEVLD STSTGIVKTD NTEVLLSADF
     TGAIKVFINK RKTVS
//
ID   HELB_MOUSE              Reviewed;        1074 AA.
AC   Q6NVF4; Q6KAT5; Q8C930; Q9EQT8;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 40.
DE   RecName: Full=DNA helicase B;
DE            EC=3.6.4.12;
GN   Name=Helb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 69-82; 632-648 AND
RP   797-814, AND FUNCTION.
RC   TISSUE=Fetal brain;
RX   MEDLINE=21441958; PubMed=11557815; DOI=10.1093/nar/29.18.3835;
RA   Tada S., Kobayashi T., Omori A., Kusa Y., Okumura N., Kodaira H.,
RA   Ishimi Y., Seki M., Enomoto T.;
RT   "Molecular cloning of a cDNA encoding mouse DNA helicase B, which has
RT   homology to Escherichia coli RecD protein, and identification of a
RT   mutation in the DNA helicase B from tsFT848 temperature-sensitive DNA
RT   replication mutant cells.";
RL   Nucleic Acids Res. 29:3835-3840(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of FLJ genes:
RT   the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:127-135(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-168.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-942 AND SER-946, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   FUNCTION.
RX   PubMed=7794903; DOI=10.1021/bi00024a016;
RA   Matsumoto K., Seki M., Masutani C., Tada S., Enomoto T., Ishimi Y.;
RT   "Stimulation of DNA synthesis by mouse DNA helicase B in a DNA
RT   replication system containing eukaryotic replication origins.";
RL   Biochemistry 34:7913-7922(1995).
RN   [7]
RP   FUNCTION.
RX   PubMed=7596831; DOI=10.1093/nar/23.11.2014;
RA   Saitoh A., Tada S., Katada T., Enomoto T.;
RT   "Stimulation of mouse DNA primase-catalyzed oligoribonucleotide
RT   synthesis by mouse DNA helicase B.";
RL   Nucleic Acids Res. 23:2014-2018(1995).
CC   -!- FUNCTION: Unwinds duplex DNA with 5'-3' polarity. Has single-
CC       strand DNA-dependent ATPase and DNA helicase activities. Prefers
CC       ATP and dATP as substrates.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- ENZYME REGULATION: Inhibited by salt concentration greater than
CC       100 mM. Uses either magnesium or manganese ions to support
CC       helicase activity. Binds strongly to single-stranded DNA in the
CC       absence of ATP but dissociates readily in the presence of 1 mM ATP
CC       (By similarity).
CC   -!- SUBUNIT: Binds to RPA1 and at least two subunits of pol-prim (By
CC       similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD21372.1; Type=Erroneous initiation;
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DR   EMBL; AB048542; BAB20809.1; -; mRNA.
DR   EMBL; AK131122; BAD21372.1; ALT_INIT; mRNA.
DR   EMBL; BC068140; AAH68140.1; -; mRNA.
DR   EMBL; AK043127; BAC31468.1; -; mRNA.
DR   IPI; IPI00111523; -.
DR   RefSeq; NP_536694.2; NM_080446.2.
DR   UniGene; Mm.214703; -.
DR   ProteinModelPortal; Q6NVF4; -.
DR   SMR; Q6NVF4; 446-474, 563-590.
DR   STRING; Q6NVF4; -.
DR   PhosphoSite; Q6NVF4; -.
DR   PRIDE; Q6NVF4; -.
DR   Ensembl; ENSMUST00000020449; ENSMUSP00000020449; ENSMUSG00000020228.
DR   GeneID; 117599; -.
DR   KEGG; mmu:117599; -.
DR   CTD; 117599; -.
DR   MGI; MGI:2152895; Helb.
DR   eggNOG; roNOG09409; -.
DR   GeneTree; ENSGT00390000006913; -.
DR   HOGENOM; HBG281397; -.
DR   HOVERGEN; HBG097647; -.
DR   InParanoid; Q6NVF4; -.
DR   OrthoDB; EOG4868BT; -.
DR   NextBio; 369702; -.
DR   ArrayExpress; Q6NVF4; -.
DR   Bgee; Q6NVF4; -.
DR   Genevestigator; Q6NVF4; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006269; P:DNA replication, synthesis of RNA primer; TAS:MGI.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Helicase; Hydrolase;
KW   Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1   1074       DNA helicase B.
FT                                /FTId=PRO_0000338993.
FT   COMPBIAS    223    226       Poly-Ser.
FT   MOD_RES     689    689       Phosphoserine (By similarity).
FT   MOD_RES     942    942       Phosphoserine.
FT   MOD_RES     946    946       Phosphoserine.
FT   MOD_RES     992    992       Phosphothreonine (By similarity).
FT   MOD_RES    1015   1015       Phosphoserine (By similarity).
FT   CONFLICT    805    805       I -> T (in Ref. 1; BAB20809 and 2;
FT                                BAD21372).
FT   CONFLICT    933    933       S -> T (in Ref. 1; BAB20809).
SQ   SEQUENCE   1074 AA;  121483 MW;  0D1ECB90429D5505 CRC64;
     MARQDRLREL LGPLHPYKSD DEEEDCAQEE EGEQEEEFVD AEELCSGGIK AGSLPGRARV
     SIPDEYTKEK CTVYGRFPLK GPWWRVKVQV LKPQRSRSYQ VQGFPAYFLQ VDMSPPDQKQ
     ICSLFLKECN LASERIQEFL KWVEKVSSFE NLHFENLWET LRLFYRETEK KDKKLSTPRE
     QQGEEMRVEK SFAFISAMVA LQFPKVMEFL PSLFPRHFKR LISSSSDWVL GCIEDVLGTQ
     PWKLGFRRIT YREMKLVRCE ASWTAFSQCP SLLQLMTPLQ KNALVIYSKL RQTCREDGHT
     YIEVKDLTSG LSEHMSFEEA CQSLAFLKDI DVVIYEKDYV FLSELYEAEQ DIASSICELM
     SRPPWHLKVD VKNVLASIRG AKPNDPGSAE AVEGSKPEEV GSEQGDSVLD AQDGDDHVRS
     NGEHVANAEI NDVPLDQDQV VALETICANA VTVLSGKGGC GKTTIVSRLF KHMEHLEETE
     VQQACEDFEQ DQEASEEWLD CPKQSPAGVD KAVEVLLTAP TGKAAGLLRQ RTDLPAYTLC
     QVNYSFYMWK TKNEVDKPWK FSTVRVLVVD EGSLVSVGIF KSVLQLLCKH SKLSKLIILG
     DVRQLPSIEP GNMLQDVFET LKSRQCAIEL KTNHRTESQL IVDNATRISR RQFPKFDAEL
     NICGNPTLPL SIQDKTFIFV RLPEEDSRSQ SSKGEHRSNL YTAVKTLLQG KDFCSFESSK
     TSQFIAFRRQ DCDLINDCCC KHYTGHLIKD HEKKLIFAVG DKICCTRNAY LSDLLPDKDQ
     EAEGKGYGDA PDDDAKIKQD FESSIRLCNG EIFFITRDVT DVTFKRKRLL TINNEAGLEV
     TVDFSKLMAN CQIKHAWART IHTFQGSEEN TVVYVVGKAG RQHWQHVYTA VTRGRSRVYI
     IAQESELRSA TRKRGFPRQT RLKHFLQKKL SGSCAPSTGF ASQPSSPRVG GRPDTQPPAS
     HLCRTPDNKA TADSARGDER WLSASVNDDV DTDEESAQLR GSKRIGDGFP FDEESPSKFR
     MVEAPSPQVS SVFQNMRLNT LTPRQLFKPT DNQDTGTAGV ADDANDPSNQ EMEM
//
ID   CPSF6_MOUSE             Reviewed;         551 AA.
AC   Q6NVF9; Q8BX86; Q8BXI8;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Cleavage and polyadenylation specificity factor subunit 6;
GN   Name=Cpsf6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, Kidney, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-404, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-404, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Component of the cleavage factor Im complex (CFIm) that
CC       plays a key role in pre-mRNA 3'-processing. Involved in
CC       association with NUDT21/CPSF5 in pre-MRNA 3'-end poly(A) site
CC       cleavage and poly(A) addition. CPSF6 binds to cleavage and
CC       polyadenylation RNA substrates (By similarity).
CC   -!- SUBUNIT: Component of the cleavage factor Im (CFIm) complex,
CC       composed at least of NUDT21/CPSF5 and CPSF6 or CPSF7. Interacts
CC       with NUDT21/CPSF5, SFRS3, SFRS7, SNRNP70 and TRA2B/SFRS10 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Note=In punctate
CC       subnuclear structures localized adjacent to nuclear speckles,
CC       called paraspeckles (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the RRM CPSF6/7 family.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR   EMBL; AK046856; BAC32898.1; -; mRNA.
DR   EMBL; AK048615; BAC33392.1; -; mRNA.
DR   EMBL; AK168764; BAE40600.1; -; mRNA.
DR   EMBL; BC068133; AAH68133.1; -; mRNA.
DR   IPI; IPI00421085; -.
DR   RefSeq; NP_001013409.1; NM_001013391.2.
DR   UniGene; Mm.478881; -.
DR   UniGene; Mm.478884; -.
DR   UniGene; Mm.479892; -.
DR   ProteinModelPortal; Q6NVF9; -.
DR   SMR; Q6NVF9; 80-158.
DR   IntAct; Q6NVF9; 2.
DR   STRING; Q6NVF9; -.
DR   PhosphoSite; Q6NVF9; -.
DR   PRIDE; Q6NVF9; -.
DR   Ensembl; ENSMUST00000069168; ENSMUSP00000068408; ENSMUSG00000055531.
DR   GeneID; 432508; -.
DR   KEGG; mmu:432508; -.
DR   UCSC; uc007hde.1; mouse.
DR   CTD; 432508; -.
DR   MGI; MGI:1913948; Cpsf6.
DR   eggNOG; roNOG10746; -.
DR   GeneTree; ENSGT00600000084083; -.
DR   InParanoid; Q6NVF9; -.
DR   OMA; EMQSRKS; -.
DR   OrthoDB; EOG432101; -.
DR   PhylomeDB; Q6NVF9; -.
DR   NextBio; 407730; -.
DR   ArrayExpress; Q6NVF9; -.
DR   Bgee; Q6NVF9; -.
DR   CleanEx; MM_CPSF6; -.
DR   Genevestigator; Q6NVF9; -.
DR   GermOnline; ENSMUSG00000055531; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   mRNA processing; Nucleus; Phosphoprotein; RNA-binding.
FT   CHAIN         1    551       Cleavage and polyadenylation specificity
FT                                factor subunit 6.
FT                                /FTId=PRO_0000081522.
FT   DOMAIN       81    161       RRM.
FT   REGION       81    161       Necessary for interaction with
FT                                NUDT21/CPSF5 (By similarity).
FT   REGION      510    551       Sufficient for nuclear targeting (By
FT                                similarity).
FT   COMPBIAS    208    398       Pro-rich.
FT   COMPBIAS    490    551       Arg-rich.
FT   MOD_RES     165    165       Phosphoserine (By similarity).
FT   MOD_RES     404    404       Phosphothreonine.
FT   MOD_RES     407    407       Phosphothreonine (By similarity).
FT   CONFLICT     95     95       E -> K (in Ref. 1; BAC32898).
FT   CONFLICT    266    266       P -> L (in Ref. 1; BAC32898).
FT   CONFLICT    289    289       L -> V (in Ref. 1; BAC33392).
SQ   SEQUENCE   551 AA;  59153 MW;  FCE1420FBE7589C8 CRC64;
     MADGVDHIDI YADVGEEFNQ EAEYGGHDQI DLYDDVISPS ANNGDAPEDR DYMDTLPPTV
     GDDVGKGAAP NVVYTYTGKR IALYIGNLTW WTTDEDLTEA VHSLGVNDIL EIKFFENRAN
     GQSKGFALVG VGSEASSKKL MDLLPKRELH GQSPVVTPCN KQFLSQFEMQ SRKTTQSGQM
     SGEGKAGPPG GGSRAAFPQG GRGRGRFPGA VPGGDRFPGP AGPGGPPPPF PAGQTPPRPP
     LGPPGPPGPP GPPPPGQVLP PPLAGPPNRG DRPPPPVLFP GQPFGQPPLG PLPPGPPPPV
     PGYGPPPGPP PPQQGPPPPP GPFPPRPPGP LGPPLTLAPP PHLPGPPPGA PPPAPHVNPA
     FFPPPTNSGM PTSDSRGPPP TDPYGRPPPY DRGDYGPPGR EMDTARTPLS EAEFEEIMNR
     NRAISSSAIS RAVSDASAGD YGSAIETLVT AISLIKQSKV SADDRCKVLI SSLQDCLHGI
     ESKSYGSGSR RERSRERDHS RSREKSRRHK SRSRDRHDDY YRERSRERER HRDRDRDRDR
     ERDREREYRH R
//
ID   GPBP1_MOUSE             Reviewed;         473 AA.
AC   Q6NXH3; Q3TQR2; Q3TSN7; Q6TYE7; Q8C498; Q8R252;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Vasculin;
DE   AltName: Full=GC-rich promoter-binding protein 1;
DE            Short=mGPBP;
GN   Name=Gpbp1; Synonyms=Gpbp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR
RP   LOCATION, INTERACTION WITH GTF2B; GTF2F2; RNA POLYMERASE II AND TBP,
RP   AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=22974702; PubMed=14612417;
RX   DOI=10.1128/MCB.23.23.8773-8785.2003;
RA   Hsu L.-C., Liu S., Abedinpour F., Beech R.D., Lahti J.M., Kidd V.J.,
RA   Greenspan J.A., Yeung C.-Y.;
RT   "The murine G+C-rich promoter binding protein mGPBP is required for
RT   promoter-specific transcription.";
RL   Mol. Cell. Biol. 23:8773-8785(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Egg, Embryo, Olfactory bulb, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6; TISSUE=Brain, Eye, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Functions as a GC-rich promoter-specific transactivating
CC       transcription factor.
CC   -!- SUBUNIT: Interacts with GTF2B, GTF2F2, RNA polymerase II and TBP.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6NXH3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NXH3-2; Sequence=VSP_032139;
CC       Name=3;
CC         IsoId=Q6NXH3-3; Sequence=VSP_032138, VSP_032139;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed (at protein level).
CC   -!- SIMILARITY: Belongs to the vasculin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH16083.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY382529; AAQ88446.1; -; mRNA.
DR   EMBL; AK082704; BAC38578.1; -; mRNA.
DR   EMBL; AK135728; BAE22631.1; -; mRNA.
DR   EMBL; AK145318; BAE26364.1; -; mRNA.
DR   EMBL; AK161928; BAE36638.1; -; mRNA.
DR   EMBL; AK163370; BAE37320.1; -; mRNA.
DR   EMBL; AK163390; BAE37330.1; -; mRNA.
DR   EMBL; AK169406; BAE41152.1; -; mRNA.
DR   EMBL; BC016083; AAH16083.1; ALT_INIT; mRNA.
DR   EMBL; BC067075; AAH67075.1; -; mRNA.
DR   EMBL; BC094888; AAH94888.1; -; mRNA.
DR   IPI; IPI00135932; -.
DR   IPI; IPI00272160; -.
DR   IPI; IPI00889259; -.
DR   RefSeq; NP_001116435.1; NM_001122963.1.
DR   RefSeq; NP_082763.3; NM_028487.4.
DR   UniGene; Mm.441830; -.
DR   UniGene; Mm.57286; -.
DR   IntAct; Q6NXH3; 1.
DR   STRING; Q6NXH3; -.
DR   PhosphoSite; Q6NXH3; -.
DR   PRIDE; Q6NXH3; -.
DR   Ensembl; ENSMUST00000047627; ENSMUSP00000048240; ENSMUSG00000032745.
DR   Ensembl; ENSMUST00000091236; ENSMUSP00000088777; ENSMUSG00000032745.
DR   Ensembl; ENSMUST00000109274; ENSMUSP00000104897; ENSMUSG00000032745.
DR   Ensembl; ENSMUST00000116379; ENSMUSP00000112080; ENSMUSG00000032745.
DR   GeneID; 73274; -.
DR   KEGG; mmu:73274; -.
DR   UCSC; uc007rvx.1; mouse.
DR   CTD; 73274; -.
DR   MGI; MGI:1920524; Gpbp1.
DR   eggNOG; roNOG05321; -.
DR   GeneTree; ENSGT00420000029753; -.
DR   HOVERGEN; HBG056980; -.
DR   OMA; LNQQPRL; -.
DR   OrthoDB; EOG4GHZP1; -.
DR   NextBio; 337827; -.
DR   ArrayExpress; Q6NXH3; -.
DR   Bgee; Q6NXH3; -.
DR   CleanEx; MM_GPBP1; -.
DR   Genevestigator; Q6NXH3; -.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:MGI.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; DNA-binding; Nucleus; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    473       Vasculin.
FT                                /FTId=PRO_0000324111.
FT   VAR_SEQ       3    137       QHDFAPAWLNFPTPPSSTKSSLNFEKHSENFSWTENRYDVS
FT                                RRRHNSSDGFDSGIGRPNGGNFGRKEKNGWRTHGRNGTENI
FT                                NHRGGYHGGNSRSRSSIFHSGKSQGLHENSIPDNETGRKED
FT                                KRERRQFEAEDF -> LILVLDVLME (in isoform
FT                                3).
FT                                /FTId=VSP_032138.
FT   VAR_SEQ     159    159       W -> WGLHAQTHTYPTKKISQAPLL (in isoform 2
FT                                and isoform 3).
FT                                /FTId=VSP_032139.
FT   CONFLICT    204    204       G -> S (in Ref. 1; AAQ88446).
FT   CONFLICT    361    361       M -> I (in Ref. 1; AAQ88446).
SQ   SEQUENCE   473 AA;  53423 MW;  ADE2CF4F36D81E1C CRC64;
     MAQHDFAPAW LNFPTPPSST KSSLNFEKHS ENFSWTENRY DVSRRRHNSS DGFDSGIGRP
     NGGNFGRKEK NGWRTHGRNG TENINHRGGY HGGNSRSRSS IFHSGKSQGL HENSIPDNET
     GRKEDKRERR QFEAEDFPSL NPEYEREPNQ NKSLAAGVWD YPPNPKSRTP RMLVIKKGNT
     KDLQLSGFPV AGNLQSQPVK NGTGPSVYKG LVPKPAVPPT KPTQWKSQTK ENKVGTSFSH
     ESTYGVGNFN TFKSTAKNIS PSTNSVKECN RSNSSSPVDK LNQQPRLTKL TRMRSDKKSE
     FLKALKRDRV EEEHEDESHA GSEKDDDSFN LHNSNTTHQE RDINRNFDEN EIPQENGNAS
     MISQQIIRSS TFPQTDVLSS SLEAEHRLLK EMGWQEDSEN DETCAPLTED EMREFQVISE
     QLQKNGLRKN GILKNGLICD FKFGPWKNST FKPTIENDDT ETSSSDTSDD DDV
//
ID   RPRD2_MOUSE             Reviewed;        1469 AA.
AC   Q6NXI6; Q3U3L8; Q6ZQA7;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Regulation of nuclear pre-mRNA domain-containing protein 2;
GN   Name=Rprd2; Synonyms=Kiaa0460;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-491 (ISOFORM 2).
RC   STRAIN=NOD; TISSUE=Dendritic cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-1469 (ISOFORM 2).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392; SER-738; THR-742
RP   AND SER-749, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374 AND THR-376, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392; SER-633; THR-742;
RP   SER-1040 AND SER-1117, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6NXI6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NXI6-2; Sequence=VSP_019548;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 CID domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC067054; AAH67054.1; -; mRNA.
DR   EMBL; AK129150; BAC97960.1; -; mRNA.
DR   EMBL; AK154692; BAE32767.1; -; mRNA.
DR   IPI; IPI00454123; -.
DR   IPI; IPI00762512; -.
DR   RefSeq; NP_001074762.1; NM_001081293.1.
DR   UniGene; Mm.196275; -.
DR   ProteinModelPortal; Q6NXI6; -.
DR   PhosphoSite; Q6NXI6; -.
DR   PRIDE; Q6NXI6; -.
DR   Ensembl; ENSMUST00000090791; ENSMUSP00000088297; ENSMUSG00000028106.
DR   Ensembl; ENSMUST00000098855; ENSMUSP00000096454; ENSMUSG00000028106.
DR   GeneID; 75137; -.
DR   KEGG; mmu:75137; -.
DR   UCSC; uc008qkx.1; mouse.
DR   UCSC; uc008qkz.1; mouse.
DR   CTD; 75137; -.
DR   MGI; MGI:1922387; Rprd2.
DR   GeneTree; ENSGT00400000022016; -.
DR   HOGENOM; HBG279151; -.
DR   HOVERGEN; HBG104176; -.
DR   InParanoid; Q6NXI6; -.
DR   OMA; PPPGEHS; -.
DR   OrthoDB; EOG4XSKQN; -.
DR   PhylomeDB; Q6NXI6; -.
DR   NextBio; 342303; -.
DR   ArrayExpress; Q6NXI6; -.
DR   Bgee; Q6NXI6; -.
DR   Genevestigator; Q6NXI6; -.
DR   GermOnline; ENSMUSG00000028106; Mus musculus.
DR   InterPro; IPR006903; DUF618.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR006569; RNA_polymerase_II_lsu_CTD.
DR   Gene3D; G3DSA:1.25.40.90; ENTH_VHS; 1.
DR   Pfam; PF04818; DUF618; 1.
DR   SMART; SM00582; RPR; 1.
DR   SUPFAM; SSF48464; ENTH_VHS; 1.
DR   PROSITE; PS51391; CID; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1   1469       Regulation of nuclear pre-mRNA domain-
FT                                containing protein 2.
FT                                /FTId=PRO_0000244356.
FT   DOMAIN       19    149       CID.
FT   COMPBIAS      4     19       Gly/Ser-rich.
FT   COMPBIAS    476    836       Ser-rich.
FT   COMPBIAS   1170   1176       Poly-Gly.
FT   COMPBIAS   1213   1330       Pro-rich.
FT   COMPBIAS   1393   1398       Poly-Gly.
FT   MOD_RES     374    374       Phosphoserine.
FT   MOD_RES     376    376       Phosphothreonine.
FT   MOD_RES     392    392       Phosphoserine.
FT   MOD_RES     492    492       Phosphoserine (By similarity).
FT   MOD_RES     495    495       Phosphoserine (By similarity).
FT   MOD_RES     498    498       Phosphoserine (By similarity).
FT   MOD_RES     504    504       Phosphoserine (By similarity).
FT   MOD_RES     506    506       Phosphoserine (By similarity).
FT   MOD_RES     536    536       Phosphothreonine (By similarity).
FT   MOD_RES     612    612       Phosphoserine (By similarity).
FT   MOD_RES     617    617       Phosphothreonine (By similarity).
FT   MOD_RES     633    633       Phosphoserine.
FT   MOD_RES     684    684       Phosphoserine (By similarity).
FT   MOD_RES     738    738       Phosphoserine.
FT   MOD_RES     742    742       Phosphothreonine.
FT   MOD_RES     749    749       Phosphoserine.
FT   MOD_RES     751    751       Phosphothreonine (By similarity).
FT   MOD_RES     753    753       Phosphothreonine (By similarity).
FT   MOD_RES     777    777       Phosphoserine (By similarity).
FT   MOD_RES     781    781       Phosphoserine (By similarity).
FT   MOD_RES     782    782       Phosphothreonine (By similarity).
FT   MOD_RES     788    788       Phosphoserine (By similarity).
FT   MOD_RES     836    836       Phosphoserine (By similarity).
FT   MOD_RES     845    845       Phosphoserine (By similarity).
FT   MOD_RES     919    919       Phosphoserine (By similarity).
FT   MOD_RES     926    926       Phosphoserine (By similarity).
FT   MOD_RES     947    947       Phosphoserine (By similarity).
FT   MOD_RES     951    951       Phosphoserine (By similarity).
FT   MOD_RES     995    995       Phosphoserine (By similarity).
FT   MOD_RES    1040   1040       Phosphoserine.
FT   MOD_RES    1117   1117       Phosphoserine.
FT   VAR_SEQ     146    189       Missing (in isoform 2).
FT                                /FTId=VSP_019548.
FT   CONFLICT    491    491       V -> K (in Ref. 2; BAC97960).
FT   CONFLICT    646    646       S -> N (in Ref. 3; BAE32767).
SQ   SEQUENCE   1469 AA;  156586 MW;  1EF4A65F32873748 CRC64;
     MAAGGGGGSS KASSSSASSA GALESSLDRK FQSVTNTMES IQGLSSWCIE NKKHHSTIVY
     HWMKWLRRST YPHRLNLFYL ANDVIQNCKR KNAIIFRESF ADVLPEAAAL VKDPSVSKSI
     ERIFKIWEDR NVYPEDMIVA LREALMDRAA SHNARLQKLQ CFPGTTFKTQ KQLKENLNKQ
     PNKQWKKSQT STNPKAALKS KIVAEFRSQA LIEELLMYKR SEDQIELKEK QLSTMRVDVC
     STETLKCLKD KTGGKKFSKE FEEASSKLEE FVNGLDKQVK NGPSLTEALE NAGIFYEAQY
     KEVKVVANAY KTFANRVNNL KKKLDQLKST LPDPEESPVP SPSMDAPSPT GSESPFQGMG
     GEEPQSPAME SDKSATPEPV TDNRDVEDME LSDVEDDGSK IIVEDRKEKP VEKPAVSTGV
     PTKSTESVSK ASPCAPPSVP TTAAPPLPKP LSTALLSPSP TLVLPNLANV DLAKISSILS
     SLTSVMKNTG VSSASRPSPG IPTSPSNLSS GLKTPAPATT PSHNPLANIL SKVEITPESI
     LSALSKTQTQ SAPALQGLSS LLQSVTANPV PASEVTSQST TASPASTTGS AVKGRNLLSS
     TQSFIPKSFN YSPSSSTSEV SSTSASKASV GQSPVLPSTT FKLPSSSLGF TGTHNPSPAA
     PPTEVAVCQS SEVSKPKPES ESTSPSLEMK IHNFLKGNPG FSGLNLNIPI LSSLGSSAPS
     EGHASDFQRG PTSTSVDSID GTPVRDERSG TPTQDEMMDK PTSSSVDTMS LLSKIISPGS
     STPSSTRSPP PGRDESYPQE LPNSVSTYRP FGLGSDSPYK QPSGGVERPS SLMDSSQEKL
     FPDTSFQEDE DYRDFEYSGP PPSAMMNLEK KPAKSILKSS KLSDATEYQP ILSSYNHRAQ
     EFGVKSAFPP SVRALLDSSE NCDRLSSPPG LFGAFNIRGN EPGSERSPSP SKNDAFFTPD
     SNHSGLSQST AGHLTLPQTQ YPDSPHSVPH RSIFSSQSTL AAPAGHPPTS GVEKVLASTI
     STTSTIEFKN MLKNASRKPS DDKHFGQTPN KGTSSDGVSL SNLTQPSLPT TDQQQEEHYR
     IETRVSSSCL DLPDSTEEKG APIETLGYHN AANRRMSGEP IKTVESIRVP GKGNRGHGRE
     VSRVGWFDLS TPGSSFDNGP SSASELASLG GGGSGGLTGF KTTPYKERAP QFQESVTSFR
     SNSFNSTFEH HLPPSPLEHG APFQREPVGP SSAPPAPPKD HGGIFSREAP THLPSVDLSN
     PFTKEASLAH AGPPPPPGEH SGVPFPPPPP PPPPGELSSG GTGVPFATPA PPPPPVDHSG
     VVPFPTPPLP EHGVTGAVSV FPKDHSSLLQ GTMAEHFGVL TGPRDLNGPG LNRSRESLSL
     PSHPLEHLGP ALGGGGGGNT SSSGLPLSPA HRDAIGRSGM ILRSPRPDFR PREAFLGRDP
     FHSLKRPRPP FVRGPPFFAP KRPFFPPRY
//
ID   Q6NXI9_MOUSE            Unreviewed;       956 AA.
AC   Q6NXI9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   SubName: Full=Kinesin family member 5C;
GN   Name=Kif5c; ORFNames=RP23-466O21.2-001, mCG_9692;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Tracey A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RA   Griffiths C.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the kinesin-like protein family.
CC   -!- SIMILARITY: Contains 1 kinesin-motor domain.
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CC   -----------------------------------------------------------------------
DR   EMBL; BC067051; AAH67051.1; -; mRNA.
DR   EMBL; AL845332; CAM20914.1; -; Genomic_DNA.
DR   EMBL; AL929069; CAM20914.1; JOINED; Genomic_DNA.
DR   EMBL; AL929069; CAM25239.1; -; Genomic_DNA.
DR   EMBL; AL845332; CAM25239.1; JOINED; Genomic_DNA.
DR   EMBL; CH466519; EDL26880.1; -; Genomic_DNA.
DR   IPI; IPI00753326; -.
DR   RefSeq; NP_032475.2; NM_008449.2.
DR   UniGene; Mm.256342; -.
DR   ProteinModelPortal; Q6NXI9; -.
DR   SMR; Q6NXI9; 2-372.
DR   STRING; Q6NXI9; -.
DR   PRIDE; Q6NXI9; -.
DR   Ensembl; ENSMUST00000028102; ENSMUSP00000028102; ENSMUSG00000026764.
DR   GeneID; 16574; -.
DR   KEGG; mmu:16574; -.
DR   UCSC; uc008jpy.1; mouse.
DR   CTD; 16574; -.
DR   MGI; MGI:1098269; Kif5c.
DR   HOVERGEN; HBG006210; -.
DR   InParanoid; Q6NXI9; -.
DR   OMA; RWRNGEA; -.
DR   NextBio; 290099; -.
DR   ArrayExpress; Q6NXI9; -.
DR   Bgee; Q6NXI9; -.
DR   Genevestigator; Q6NXI9; -.
DR   GO; GO:0035253; C:ciliary rootlet; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005871; C:kinesin complex; TAS:MGI.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003777; F:microtubule motor activity; TAS:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0008045; P:motor axon guidance; IMP:MGI.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   Gene3D; G3DSA:3.40.850.10; kinesin_motor; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_DOMAIN1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_DOMAIN2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Microtubule; Motor protein; Nucleotide-binding.
SQ   SEQUENCE   956 AA;  109275 MW;  A36BC903603D8748 CRC64;
     MADPAECSIK VMCRFRPLNE AEILRGDKFI PKFKGEETVV IGQGKPYVFD RVLPPNTTQE
     QVYNACAKQI VKDVLEGYNG TIFAYGQTSS GKTHTMEGKL HDPQLMGIIP RIAHDIFDHI
     YSMDENLEFH IKVSYFEIYL DKIRDLLDVS KTNLAVHEDK NRVPYVKGCT ERFVSSPEEV
     MDVIDEGKAN RHVAVTNMNE HSSRSHSIFL INIKQENVET EKKLSGKLYL VDLAGSEKVS
     KTGAEGAVLD EAKNINKSLS ALGNVISALA EGTKTHVPYR DSKMTRILQD SLGGNCRTTI
     VICCSPSVFN EAETKSTLMF GQRAKTIKNT VSVNLELTAE EWKKKYEKEK EKNKALKSVL
     QHLEMELNRW RNGEAVPEDE QISAKDQKSL EPCDNTPIID NITPVVDGIS AEKEKYDEEI
     TSLYRQLDDK DDEINQQSQL AEKLKQQMLD QDELLASTRR DYEKIQEELT RLQIENEAAK
     DEVKEVLQAL EELAVNYDQK SQEVEDKTRA NEQLTDELAQ KTTTLTTTQR ELSQLQELSN
     HQKKRATEIL NLLLKDLGEI GGIIGTNDVK TLADVNGVIE EEFTMARLYI SKMKSEVKSL
     VNRSKQLESA QMDSNRKMNA SERELAACQL LISQHEAKIK SLTDYMQNME QKRRQLEESQ
     DSLSEELAKL RAQEKMHEVS FQDKEKEHLT RLQDAEEVKK ALEQQMESHR EAHQKQLSRL
     RDEIEEKQRI IDEIRDLNQK LQLEQERLSS DYNKLKIEDQ EREVKLEKLL LLNDKREQAR
     EDLKGLEETV SRELQTLHNL RKLFVQDLTT RVKKSVELDS DDGGGSAAQK QKISFLENNL
     EQLTKVHKQL VRDNADLRCE LPKLEKRLRA TAERVKALES ALKEAKENAM RDRKRYQQEV
     DRIKEAVRAK NMARRAHSAQ IAKPIRPGHY PASSPTAVHA VRGGGGGSSN STHYQK
//
ID   WWC2_MOUSE              Reviewed;        1187 AA.
AC   Q6NXJ0; Q3UGG4; Q3UH10; Q7TMY1; Q8CE61; Q9JJ63;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Protein WWC2;
DE   AltName: Full=WW domain-containing protein 2;
GN   Name=Wwc2; Synonyms=D8Ertd594e; ORFNames=MNCb-4173;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S.,
RA   Hashimoto K.;
RT   "Isolation of full-length cDNA clones from mouse brain cDNA library
RT   made by oligo-capping method.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Placenta, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N-3; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the WWC family.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 2 WW domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA97983.1; Type=Frameshift; Positions=59, 61, 424, 578, 580;
CC       Sequence=BAE28244.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB045323; BAA97983.1; ALT_FRAME; mRNA.
DR   EMBL; AK028956; BAC26212.1; -; mRNA.
DR   EMBL; AK147648; BAE28047.1; -; mRNA.
DR   EMBL; AK147944; BAE28244.1; ALT_INIT; mRNA.
DR   EMBL; BC054434; AAH54434.1; -; mRNA.
DR   EMBL; BC067050; AAH67050.1; -; mRNA.
DR   IPI; IPI00121100; -.
DR   RefSeq; NP_598552.2; NM_133791.4.
DR   UniGene; Mm.235074; -.
DR   UniGene; Mm.390033; -.
DR   HSSP; Q62940; 1I5H.
DR   ProteinModelPortal; Q6NXJ0; -.
DR   SMR; Q6NXJ0; 7-98, 697-824.
DR   PhosphoSite; Q6NXJ0; -.
DR   PRIDE; Q6NXJ0; -.
DR   Ensembl; ENSMUST00000057561; ENSMUSP00000056121; ENSMUSG00000031563.
DR   GeneID; 52357; -.
DR   KEGG; mmu:52357; -.
DR   NMPDR; fig|10090.3.peg.18501; -.
DR   UCSC; uc009lrm.1; mouse.
DR   CTD; 52357; -.
DR   MGI; MGI:1261872; Wwc2.
DR   eggNOG; roNOG10725; -.
DR   GeneTree; ENSGT00410000025556; -.
DR   HOGENOM; HBG357360; -.
DR   HOVERGEN; HBG058082; -.
DR   InParanoid; Q6NXJ0; -.
DR   OMA; LAGTQIS; -.
DR   OrthoDB; EOG4GXFKZ; -.
DR   PhylomeDB; Q6NXJ0; -.
DR   NextBio; 308834; -.
DR   ArrayExpress; Q6NXJ0; -.
DR   Bgee; Q6NXJ0; -.
DR   CleanEx; MM_WWC2; -.
DR   Genevestigator; Q6NXJ0; -.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF51045; WW_Rsp5_WWP; 2.
DR   PROSITE; PS50004; C2; FALSE_NEG.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   2: Evidence at transcript level;
KW   Coiled coil; Phosphoprotein; Repeat.
FT   CHAIN         1   1187       Protein WWC2.
FT                                /FTId=PRO_0000309491.
FT   DOMAIN       10     43       WW 1.
FT   DOMAIN       57     90       WW 2.
FT   DOMAIN      714    803       C2.
FT   COILED      121    194       Potential.
FT   COILED      224    256       Potential.
FT   COILED      302    423       Potential.
FT   COILED      859    885       Potential.
FT   COILED     1063   1143       Potential.
FT   MOD_RES    1017   1017       Phosphoserine (By similarity).
FT   CONFLICT    352    352       E -> G (in Ref. 2; BAE28244).
FT   CONFLICT    361    361       I -> V (in Ref. 2; BAE28047).
FT   CONFLICT    572    572       S -> F (in Ref. 1; BAA97983).
FT   CONFLICT    576    577       SP -> FS (in Ref. 1; BAA97983).
FT   CONFLICT    683    683       M -> V (in Ref. 1; BAA97983).
FT   CONFLICT    699    699       A -> T (in Ref. 2; BAE28047).
FT   CONFLICT    773    773       V -> A (in Ref. 1; BAA97983).
FT   CONFLICT    864    864       T -> I (in Ref. 1; BAA97983).
FT   CONFLICT   1174   1174       R -> I (in Ref. 1; BAA97983).
SQ   SEQUENCE   1187 AA;  132620 MW;  40FB67C9D1D3B296 CRC64;
     MPRRAGSGQL PLPRGWEEAR DYDGKVFYID HNTRRTSWID PRDRLTKPLS FADCVGDELP
     WGWEAGFDPQ IGAYYIDHIN KTTQIEDPRK QWRGEQEKML KDYLSVAQDA LRTQKELYHV
     KEQRLALALD EYVRLNDAYK EKSSSHTSLF SGSSSSTKYD PDILKAEIST TQLRVKKLKR
     ELSHMKQELL YKQQGFETLQ QIDEKMSGGQ SGYELNEAKA ILTELKSIRK AISSGEKEKQ
     DLMQSLAKLQ ERFHLDQNMG SSEPDLRSSP VNSHLSLSRQ TLDAGSQTSI SGDIGVRSRS
     NLAEKVRLSL QYEEAKRSMA NLKIELSKLD GEAWPGALDI EKEKLMLINE KEELLKELQF
     ITPQKRSQEE LERLEAERQH LEEELMAARG SPSRALTERL KLEEKRKELL QKLEETTKLT
     TSLYSQLQSL SSSTLSMSSG SSLGSLASSR GSLNTSSRGS LNSLSSSELY YSSQGDQMDT
     DYQYKLDFLL QEKGGYIPSG PITTIHENEV VKSPSQPGQS GLCGVGVTAS SHTTPLTEAS
     KSVASLSSRS SLSSLSPPGS PLVLDSVFPG SSHDTSPHQF PTDFEDCELS RRFADVGLGE
     NQALLDSDSG GASQPLLEDK GLSDCPGELL CEGATDVEKS LPKRRGLHLR GDKTTRVSAA
     ASDESVAGDS GVYEASMKQP GEMEDVPYSE EDVTIVETAQ VQIGLRYDTK SSSFMVIIAQ
     LRNLHAFSIP HSSKVYFRVA LLPSSADVSC LFRTKVHPPT ESVLYNDVFR VAVSQAALQQ
     KTLRVDLCSA SKHRREECLA GTQISLADLP FSNEIFMLWY NLLPSKQMPC KKNEDGNEEP
     GARSQQPMLD PIDLDAVSAL LARTSAELLA VEQELAQEEE EEELRPERRG PGRDCLTMLR
     EASDEPAALR ESGVPLAEGS RCTEDPKPCP RGPETSQCRK EPAEDPGQLP SGLPTLVDKE
     TNTDEVVDSN MAVRPKDRSS LSSRQHPFVR NSVIVRSQTF SPGERSQYIC RLNRSDSDSS
     TLAKKSLFVR NSTERRSLRV KRAVCQPTLR RTAQECPVRT SLDLELDLQA SLTRQSRLND
     ELQALRGLRQ KLEELKAQGE TDLPPGVLED ERFQKLLKQA EKQAEQTKEE QKQDLNAERL
     MRQVSKDVCR LREQSQKEPR QVQSFREKIA YFTRAKISIP SLPADDV
//
ID   ZN532_MOUSE             Reviewed;        1036 AA.
AC   Q6NXK2; Q504Z6; Q6ZPL1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Zinc finger protein 532;
GN   Name=Znf532; Synonyms=Kiaa1629, Zfp532;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-643.
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6NXK2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NXK2-2; Sequence=VSP_027745;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family.
CC   -!- SIMILARITY: Contains 6 C2H2-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98220.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC067032; AAH67032.1; -; mRNA.
DR   EMBL; BC094671; AAH94671.1; -; mRNA.
DR   EMBL; AK129410; BAC98220.1; ALT_INIT; mRNA.
DR   IPI; IPI00411014; -.
DR   IPI; IPI00856136; -.
DR   RefSeq; NP_997138.1; NM_207255.2.
DR   UniGene; Mm.286232; -.
DR   UniGene; Mm.419081; -.
DR   ProteinModelPortal; Q6NXK2; -.
DR   SMR; Q6NXK2; 607-670, 750-1022.
DR   PhosphoSite; Q6NXK2; -.
DR   PRIDE; Q6NXK2; -.
DR   Ensembl; ENSMUST00000049016; ENSMUSP00000036582; ENSMUSG00000042439.
DR   GeneID; 328977; -.
DR   KEGG; mmu:328977; -.
DR   UCSC; uc008ffc.1; mouse.
DR   CTD; 328977; -.
DR   MGI; MGI:3036282; Zfp532.
DR   HOGENOM; HBG713613; -.
DR   HOVERGEN; HBG062228; -.
DR   InParanoid; Q6NXK2; -.
DR   OMA; KGDVPTS; -.
DR   OrthoDB; EOG4W9J39; -.
DR   PhylomeDB; Q6NXK2; -.
DR   NextBio; 398524; -.
DR   ArrayExpress; Q6NXK2; -.
DR   Bgee; Q6NXK2; -.
DR   CleanEx; MM_ZFP532; -.
DR   Genevestigator; Q6NXK2; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 2.
DR   SMART; SM00355; ZnF_C2H2; 8.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   2: Evidence at transcript level;
KW   Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW   Phosphoprotein; Repeat; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1036       Zinc finger protein 532.
FT                                /FTId=PRO_0000299553.
FT   ZN_FING     615    634       C2H2-type 1; degenerate.
FT   ZN_FING     751    775       C2H2-type 2; degenerate.
FT   ZN_FING     784    807       C2H2-type 3.
FT   ZN_FING     814    840       C2H2-type 4; degenerate.
FT   ZN_FING     938    961       C2H2-type 5.
FT   ZN_FING     999   1021       C2H2-type 6.
FT   COMPBIAS    861    866       Poly-Glu.
FT   VAR_SEQ     780   1036       QMKKHPCRQCDKSFSSSHSLCRHNRIKHKGIRKVYACSHCP
FT                                DSRRTFTKRLMLERHIQLMHGIKDPDVKELSDDAGDVTNDE
FT                                EEEAEIKEDAKVPSPKRKLEEPVLEFRPPRGAITQPLKKLK
FT                                INVFKVHKCAVCGFTTENLLQFHEHIPQHRSDGSSHQCREC
FT                                GLCYTSHGSLARHLFIVHKLKEPQPVSKQNGAGEDSQQENK
FT                                PSPEDEAAEGAASDRKCKVCAKTFETEAALNTHMRTHGMAF
FT                                IKSKRMSSAEK -> KTCTVCQMLLPNQCSYASHQRIHQHK
FT                                SPYTCPECGAICRSVHFQNHITKNCLHYTRRVGFRCVHCNV
FT                                VYSDVAALKSHIQGSHCEVFYKCPICPMAFKSAPSTHSHAY
FT                                TQHPGVKIGEPNK (in isoform 2).
FT                                /FTId=VSP_027745.
SQ   SEQUENCE   1036 AA;  110949 MW;  9A3B6E1F7803627B CRC64;
     MTMGDMKTPD FDDLLAAFDI PDMVDPKAAI ESGHDDHESH IKQNAHVDDD SHTPSSSDVG
     VSVIVKNVRN IDSSEGVEKD GHNPTGNGLH NGFLTASSLD SYGKDGAKSL KGDTPASEVT
     LKDPAFSQFS PISSAEEFED DEKIEVDDPP DKEEARAGFR SNVLTGSAPQ QDFDKLKALG
     GENSSKTGVS TSGHTDKNKV KREAESNSIT LSVYEPFKVR KAEDKLKENS EKMLESRVLD
     GKPSSEKSDS GIAAAASSKT KPSSKLSSCI AAIAALSAKK AASDSCKEPV ANSREASPLP
     KEVNDSPKAA DKSPESQNLI DGTKKASLKP SDSPRSVSSE NSSKGSPSSP VGSTPAIPKV
     RIKTIKTSSG EIKRTVTRVL PEVDLDSGKK PSEQAASVMA SVTSLLSSSA SATVLSSPPR
     APLQTAMVTS AVSSAELTPK QVTIKPVATA FLPVSAVKTA GSQVINLKLA NNTTVKATVI
     SAASVQSASS AIIKAANAIQ QQTVVVPASS LANAKLVPKT VHLANLNLLP QGAQATSELR
     QVLTKPQQQI KQAIINAAAS QPPKKVSRVQ VVSSLQSSVV EAFNKVLSSV NPVPVYTPNL
     SPPANAGITL PMRGYKCLEC GDAFALEKSL SQHYDRRSVR IEVTCNHCTK NLVFYNKCSL
     LSHARGHKEK GVVMQCSHLI LKPVPADQMI VPPSSNTAAS TLQSSVGAAT HTVPKVQPGI
     AGAVISAPAS TPMSPAMPLD EDPSKLCRHS LKCLECNEVF QDEPSLATHF QHAADTSGQQ
     MKKHPCRQCD KSFSSSHSLC RHNRIKHKGI RKVYACSHCP DSRRTFTKRL MLERHIQLMH
     GIKDPDVKEL SDDAGDVTND EEEEAEIKED AKVPSPKRKL EEPVLEFRPP RGAITQPLKK
     LKINVFKVHK CAVCGFTTEN LLQFHEHIPQ HRSDGSSHQC RECGLCYTSH GSLARHLFIV
     HKLKEPQPVS KQNGAGEDSQ QENKPSPEDE AAEGAASDRK CKVCAKTFET EAALNTHMRT
     HGMAFIKSKR MSSAEK
//
ID   ACCN2_MOUSE             Reviewed;         526 AA.
AC   Q6NXK8; Q50K97;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Amiloride-sensitive cation channel 2, neuronal;
DE   AltName: Full=Acid-sensing ion channel;
DE   AltName: Full=Acid-sensing ion channel 1;
DE   AltName: Full=Brain sodium channel 2;
DE            Short=BNaC2;
GN   Name=Accn2; Synonyms=Asic, Asic1, Bnac2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Ugawa S., Shimada S.;
RT   "Mus musculus mRNA for ASIC1b.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=11988176; DOI=10.1016/S0896-6273(02)00661-X;
RA   Wemmie J.A., Chen J., Askwith C.C., Hruska-Hageman A.M., Price M.P.,
RA   Nolan B.C., Yoder P.G., Lamani E., Hoshi T., Freeman J.H. Jr.,
RA   Welsh M.J.;
RT   "The acid-activated ion channel ASIC contributes to synaptic
RT   plasticity, learning, and memory.";
RL   Neuron 34:463-477(2002).
RN   [4]
RP   TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=12843249;
RA   Wemmie J.A., Askwith C.C., Lamani E., Cassell M.D., Freeman J.H. Jr.,
RA   Welsh M.J.;
RT   "Acid-sensing ion channel 1 is localized in brain regions with high
RT   synaptic density and contributes to fear conditioning.";
RL   J. Neurosci. 23:5496-5502(2003).
RN   [5]
RP   FUNCTION.
RX   PubMed=15369669; DOI=10.1016/j.cell.2004.08.026;
RA   Xiong Z.-G., Zhu X.-M., Chu X.-P., Minami M., Hey J., Wei W.-L.,
RA   MacDonald J.F., Wemmie J.A., Price M.P., Welsh M.J., Simon R.P.;
RT   "Neuroprotection in ischemia: blocking calcium-permeable acid-sensing
RT   ion channels.";
RL   Cell 118:687-698(2004).
RN   [6]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=15578512; DOI=10.1053/j.gastro.2004.08.061;
RA   Page A.J., Brierley S.M., Martin C.M., Martinez-Salgado C.,
RA   Wemmie J.A., Brennan T.J., Symonds E., Omari T., Lewin G.R.,
RA   Welsh M.J., Blackshaw L.A.;
RT   "The ion channel ASIC1 contributes to visceral but not cutaneous
RT   mechanoreceptor function.";
RL   Gastroenterology 127:1739-1747(2004).
RN   [7]
RP   INTERACTION WITH STOM.
RX   PubMed=15471860; DOI=10.1074/jbc.M407708200;
RA   Price M.P., Thompson R.J., Eshcol J.O., Wemmie J.A., Benson C.J.;
RT   "Stomatin modulates gating of acid-sensing ion channels.";
RL   J. Biol. Chem. 279:53886-53891(2004).
RN   [8]
RP   FUNCTION.
RX   PubMed=17060608; DOI=10.1073/pnas.0608018103;
RA   Zha X.-M., Wemmie J.A., Green S.H., Welsh M.J.;
RT   "Acid-sensing ion channel 1a is a postsynaptic proton receptor that
RT   affects the density of dendritic spines.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:16556-16561(2006).
RN   [9]
RP   FUNCTION IN CONTROL OF FEAR, AND DISRUPTION PHENOTYPE.
RX   PubMed=17662962; DOI=10.1016/j.biopsych.2007.05.008;
RA   Coryell M.W., Ziemann A.E., Westmoreland P.J., Haenfler J.M.,
RA   Kurjakovic Z., Zha X.-M., Price M., Schnizler M.K., Wemmie J.A.;
RT   "Targeting ASIC1a reduces innate fear and alters neuronal activity in
RT   the fear circuit.";
RL   Biol. Psychiatry 62:1140-1148(2007).
CC   -!- FUNCTION: Cation channel with high affinity for sodium, which is
CC       gated by extracellular protons and inhibited by the diuretic
CC       amiloride. Also permeable for Ca(2+), Li(+) and K(+). Generates a
CC       biphasic current with a fast inactivating and a slow sustained
CC       phase. Mediates glutamate-independent Ca(2+) entry into neurons
CC       upon acidosis. This Ca(2+) overloading is toxic for cortical
CC       neurons and may be in part responsible for ischemic brain injury.
CC       Heteromeric channel assembly seems to modulate channel properties.
CC       Functions as a postsynaptic proton receptor that influences
CC       intracellular Ca(2+) concentration and calmodulin-dependent
CC       protein kinase II phosphorylation and thereby the density of
CC       dendritic spines. Modulates activity in the circuits underlying
CC       innate fear.
CC   -!- SUBUNIT: Homotrimer or heterotrimer with other ASIC proteins (By
CC       similarity). Interacts with PRKCABP and ACCN1 (By similarity).
CC       Interacts with STOM.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity). Note=Localizes in synaptosomes at dendritic
CC       synapses of neurons. Colocalizes with DLG4.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Asic1a, Asic alpha;
CC         IsoId=Q6NXK8-1; Sequence=Displayed;
CC       Name=2; Synonyms=Asic1b, Asic beta;
CC         IsoId=Q6NXK8-2; Sequence=VSP_015614, VSP_015615;
CC   -!- TISSUE SPECIFICITY: Expressed in brain areas receiving strong
CC       excitatory corticofugal input. In hippocampus, expressed in the
CC       hilus of the dentate gyrus. In the cerebral cortex expressed in
CC       anterior and posterior cingulate cortex, sensory and motor
CC       cortices. In the sensory cortex strongest expression is detected
CC       in the whisker barrel field. In sensorimotor and cingulate cortex
CC       expression is elevated in layer III. Also expressed in basal
CC       ganglia, striatum, ventral pallidum, olfactory tubercle, and
CC       nucleus accumbens. Weakly expressed in thalamus with the exception
CC       of the habenula and the medial septal nuclei. In olfactory bulb,
CC       preferentially expressed in the glomerular layer, within
CC       glomeruli. Expressed in cerebellum in the molecular and granule
CC       cell layers. Strongly expressed in amygdala complex, particularly
CC       in the lateral and basolateral nuclei. Isoform 1 is more abundant
CC       in brain compared to isoform 2 (at protein level). Expressed in
CC       the nodose ganglion and dorsal root ganglion. Expressed in
CC       dendritic spine cells.
CC   -!- PTM: Phosphorylation by PKA regulates interaction with PRKCABP and
CC       subcellular location. Phosphorylation by PKC may regulate the
CC       channel (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice display reduced spatial learning and
CC       memory capability, associated with absence of proton-gated
CC       currents in hippocampal neurons and impairment of hippocampal long
CC       term potentiation (LTP). They also show an increased
CC       mechanosensitivity of colonic and gastroesophageal
CC       mechanoreceptors and prolonged gastric emptying and an altered
CC       fear conditioning.
CC   -!- MISCELLANEOUS: Potentiated by Ca(2+), Mg(2+), Ba(2+), multivalent
CC       cations and potentiated by FMRFamide-related neuropeptides. PH
CC       dependence may be regulated by serine proteases. Inhibited by
CC       anti-inflammatory drugs like salicylic acid (By similarity).
CC   -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel
CC       (TC 1.A.6) family. ACCN2 subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB208022; BAD97849.1; -; mRNA.
DR   EMBL; BC067025; AAH67025.1; -; mRNA.
DR   IPI; IPI00346778; -.
DR   IPI; IPI00607080; -.
DR   RefSeq; NP_033727.1; NM_009597.1.
DR   UniGene; Mm.440107; -.
DR   ProteinModelPortal; Q6NXK8; -.
DR   SMR; Q6NXK8; 40-460.
DR   DIP; DIP-29728N; -.
DR   STRING; Q6NXK8; -.
DR   PhosphoSite; Q6NXK8; -.
DR   PRIDE; Q6NXK8; -.
DR   Ensembl; ENSMUST00000023758; ENSMUSP00000023758; ENSMUSG00000023017.
DR   Ensembl; ENSMUST00000109052; ENSMUSP00000104680; ENSMUSG00000023017.
DR   GeneID; 11419; -.
DR   KEGG; mmu:11419; -.
DR   UCSC; uc007xqa.1; mouse.
DR   CTD; 11419; -.
DR   MGI; MGI:1194915; Accn2.
DR   GeneTree; ENSGT00550000074208; -.
DR   HOVERGEN; HBG004150; -.
DR   OMA; PVPFPCH; -.
DR   OrthoDB; EOG48GW36; -.
DR   PhylomeDB; Q6NXK8; -.
DR   NextBio; 278664; -.
DR   ArrayExpress; Q6NXK8; -.
DR   Bgee; Q6NXK8; -.
DR   CleanEx; MM_ACCN2; -.
DR   Genevestigator; Q6NXK8; -.
DR   GermOnline; ENSMUSG00000023017; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; IDA:MGI.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
DR   GO; GO:0022839; F:ion gated channel activity; IDA:MGI.
DR   GO; GO:0015280; F:ligand-gated sodium channel activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0008306; P:associative learning; IMP:MGI.
DR   GO; GO:0070588; P:calcium ion transmembrane transport; IMP:MGI.
DR   GO; GO:0007613; P:memory; IMP:MGI.
DR   GO; GO:0046929; P:negative regulation of neurotransmitter secretion; IMP:MGI.
DR   GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR   GO; GO:0001101; P:response to acid; IDA:MGI.
DR   InterPro; IPR004724; EnaC.
DR   InterPro; IPR001873; Na+channel_ASC.
DR   InterPro; IPR020903; Na+channel_ASC_CS.
DR   PANTHER; PTHR11690; Na+channel_ASC; 1.
DR   Pfam; PF00858; ASC; 1.
DR   PRINTS; PR01078; AMINACHANNEL.
DR   TIGRFAMs; TIGR00859; ENaC; 1.
DR   PROSITE; PS01206; ASC; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Calcium transport; Cell membrane;
KW   Disulfide bond; Glycoprotein; Ion transport; Ionic channel; Membrane;
KW   Phosphoprotein; Sodium; Sodium channel; Sodium transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    526       Amiloride-sensitive cation channel 2,
FT                                neuronal.
FT                                /FTId=PRO_0000181295.
FT   TOPO_DOM      1     45       Cytoplasmic (By similarity).
FT   TRANSMEM     46     69       Helical; (By similarity).
FT   TOPO_DOM     70    425       Extracellular (By similarity).
FT   TRANSMEM    426    452       Helical; (By similarity).
FT   TOPO_DOM    453    526       Cytoplasmic (By similarity).
FT   MOD_RES     477    477       Phosphoserine; by PKA (By similarity).
FT   CARBOHYD    366    366       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    393    393       N-linked (GlcNAc...) (Potential).
FT   DISULFID     93    194       By similarity.
FT   DISULFID    172    179       By similarity.
FT   DISULFID    290    365       By similarity.
FT   DISULFID    308    361       By similarity.
FT   DISULFID    312    359       By similarity.
FT   DISULFID    321    343       By similarity.
FT   DISULFID    323    335       By similarity.
FT   VAR_SEQ       1    184       Missing (in isoform 2).
FT                                /FTId=VSP_015614.
FT   VAR_SEQ     185    185       K -> MPIQIFCSVSFSSGEEAPGSMGDIWGPHHHHRQQQD
FT                                SSESEEEEEKEKESGMELDEGDSPRDLVAFANSCTLHGASH
FT                                VFVEGGPGPRQALWAVAFVIALGAFLCQVGDRVAYYLSYPH
FT                                VTLLDEVATTELVFPAVTFCNTNAVRLSQLSYPDLLYLAPM
FT                                LGLDESDDPGVPLAPPGPEAFSGEPFNLHRFYNRSCHRLED
FT                                MLLYCSYCGGPCGPHNFS (in isoform 2).
FT                                /FTId=VSP_015615.
SQ   SEQUENCE   526 AA;  59668 MW;  5462B3FEB5532726 CRC64;
     MELKTEEEEV GGVQPVSIQA FASSSTLHGL AHIFSYERLS LKRALWALCF LGSLAVLLCV
     CTERVQYYFC YHHVTKLDEV AASQLTFPAV TLCNLNEFRF SQVSKNDLYH AGELLALLNN
     RYEIPDTQMA DEKQLEILQD KANFRSFKPK PFNMREFYDR AGHDIRDMLL SCHFRGEACS
     AEDFKVVFTR YGKCYTFNSG QDGRPRLKTM KGGTGNGLEI MLDIQQDEYL PVWGETDETS
     FEAGIKVQIH SQDEPPFIDQ LGFGVAPGFQ TFVSCQEQRL IYLPSPWGTC NAVTMDSDFF
     DSYSITACRI DCETRYLVEN CNCRMVHMPG DAPYCTPEQY KECADPALDF LVEKDQEYCV
     CEMPCNLTRY GKELSMVKIP SKASAKYLAK KFNKSEQYIG ENILVLDIFF EVLNYETIEQ
     KKAYEIAGLL GDIGGQMGLF IGASILTVLE LFDYAYEVIK HRLCRRGKCQ KEAKRNSADK
     GVALSLDDVK RHNPCESLRG HPAGMTYAAN ILPHHPARGT FEDFTC
//
ID   CA144_MOUSE             Reviewed;         152 AA.
AC   Q6NXN1; Q3TB72; Q8BT36;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   RecName: Full=UPF0485 protein C1orf144 homolog;
GN   Name=D4Ertd22e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Dendritic cell, Embryo, Placenta, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6NXN1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NXN1-2; Sequence=VSP_027998;
CC   -!- SIMILARITY: Belongs to the UPF0485 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK027934; BAC25672.1; -; mRNA.
DR   EMBL; AK145912; BAE26745.1; -; mRNA.
DR   EMBL; AK171420; BAE42442.1; -; mRNA.
DR   EMBL; AK171702; BAE42618.1; -; mRNA.
DR   EMBL; AL645625; CAM16764.1; -; Genomic_DNA.
DR   EMBL; AL645625; CAM16765.1; -; Genomic_DNA.
DR   EMBL; BC066992; AAH66992.1; -; mRNA.
DR   IPI; IPI00224792; -.
DR   IPI; IPI00463086; -.
DR   RefSeq; NP_001020779.1; NM_001025608.1.
DR   RefSeq; NP_778161.1; NM_174996.2.
DR   UniGene; Mm.332006; -.
DR   PhosphoSite; Q6NXN1; -.
DR   PRIDE; Q6NXN1; -.
DR   Ensembl; ENSMUST00000094549; ENSMUSP00000092128; ENSMUSG00000040842.
DR   Ensembl; ENSMUST00000102487; ENSMUSP00000099545; ENSMUSG00000040842.
DR   GeneID; 213491; -.
DR   KEGG; mmu:213491; -.
DR   UCSC; uc008vnw.1; mouse.
DR   CTD; 213491; -.
DR   MGI; MGI:1098672; D4Ertd22e.
DR   GeneTree; ENSGT00390000005532; -.
DR   HOGENOM; HBG713273; -.
DR   HOVERGEN; HBG057301; -.
DR   InParanoid; Q6NXN1; -.
DR   OMA; TAIVIQD; -.
DR   OrthoDB; EOG4M91T1; -.
DR   NextBio; 374007; -.
DR   ArrayExpress; Q6NXN1; -.
DR   Bgee; Q6NXN1; -.
DR   CleanEx; MM_D4ERTD22E; -.
DR   Genevestigator; Q6NXN1; -.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Phosphoprotein.
FT   CHAIN         1    152       UPF0485 protein C1orf144 homolog.
FT                                /FTId=PRO_0000303069.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      37     37       Phosphoserine (By similarity).
FT   MOD_RES      39     39       Phosphoserine.
FT   MOD_RES      68     68       Phosphoserine (By similarity).
FT   MOD_RES      74     74       Phosphoserine (By similarity).
FT   MOD_RES     105    105       Phosphoserine (By similarity).
FT   MOD_RES     107    107       Phosphoserine.
FT   VAR_SEQ       1     34       MEDEEVAESWEEAADSGEIDRRLEKKLKITQKES -> MRR
FT                                SLRAGRRRQTAG (in isoform 2).
FT                                /FTId=VSP_027998.
FT   CONFLICT    124    124       S -> P (in Ref. 1; BAE42442).
SQ   SEQUENCE   152 AA;  16998 MW;  3EF639D6A97DE6B1 CRC64;
     MEDEEVAESW EEAADSGEID RRLEKKLKIT QKESRKSKSP PKVPIVIQDD SLPTGPPPQI
     RILKRPTSNG VVSSPNSTSR PALPVKSLAQ REAEYAEARR RILGSASPEE EQEKPILDRP
     TRISQPEDSR QPSNVIRQPL GPDGSQGFKQ RR
//
ID   TAF9B_MOUSE             Reviewed;         249 AA.
AC   Q6NZA9; A2AP80; Q3UXZ3; Q3V2M4; Q80WW6;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 2.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Transcription initiation factor TFIID subunit 9B;
DE   AltName: Full=Transcription initiation factor TFIID subunit 9-like;
DE   AltName: Full=Transcription-associated factor TAFII31L;
GN   Name=Taf9b; Synonyms=Taf9l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and C57BL/6J; TISSUE=Embryo, and Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-154, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Essential for cell viability. TAF9 and TAF9B are
CC       involved in transcriptional activation as well as repression of
CC       distinct but overlapping sets of genes. May have a role in gene
CC       regulation associated with apoptosis. TAFs are components of the
CC       transcription factor IID (TFIID) complex, the TBP-free TAFII
CC       complex (TFTC), the PCAF histone acetylase complex and the STAGA
CC       transcription coactivator-HAT complex. TFIID or TFTC are essential
CC       for the regulation of RNA polymerase II-mediated transcription (By
CC       similarity).
CC   -!- SUBUNIT: Binds TAF5 and TAF6. Component of TFIID and the TATA-
CC       binding protein-free TAF complex (TFTC). TFIID is composed of TATA
CC       binding protein (TBP) and a number of TBP-associated factors
CC       (TAFs). Binds N-terminal domain of p53/TP53 which is essential for
CC       transcription (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the TAF9 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH51635.1; Type=Erroneous initiation;
CC       Sequence=BAE20773.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK131710; BAE20773.1; ALT_INIT; mRNA.
DR   EMBL; AK135097; BAE22420.1; -; mRNA.
DR   EMBL; AL833778; CAM23480.1; -; Genomic_DNA.
DR   EMBL; BC051635; AAH51635.1; ALT_INIT; mRNA.
DR   EMBL; BC066223; AAH66223.1; -; mRNA.
DR   IPI; IPI00330677; -.
DR   RefSeq; NP_001001176.2; NM_001001176.2.
DR   RefSeq; NP_001161460.1; NM_001167988.1.
DR   UniGene; Mm.19440; -.
DR   ProteinModelPortal; Q6NZA9; -.
DR   SMR; Q6NZA9; 13-76.
DR   STRING; Q6NZA9; -.
DR   PRIDE; Q6NZA9; -.
DR   Ensembl; ENSMUST00000055497; ENSMUSP00000059751; ENSMUSG00000047242.
DR   Ensembl; ENSMUST00000113495; ENSMUSP00000109123; ENSMUSG00000047242.
DR   GeneID; 407786; -.
DR   KEGG; mmu:407786; -.
DR   UCSC; uc009ubp.1; mouse.
DR   CTD; 407786; -.
DR   MGI; MGI:3039562; Taf9b.
DR   GeneTree; ENSGT00390000001626; -.
DR   HOVERGEN; HBG002304; -.
DR   InParanoid; Q6NZA9; -.
DR   OrthoDB; EOG45757B; -.
DR   PhylomeDB; Q6NZA9; -.
DR   NextBio; 407183; -.
DR   ArrayExpress; Q6NZA9; -.
DR   Bgee; Q6NZA9; -.
DR   Genevestigator; Q6NZA9; -.
DR   GermOnline; ENSMUSG00000047242; Mus musculus.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0006352; P:transcription initiation, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR003162; TFIID-31.
DR   Gene3D; G3DSA:1.10.20.10; Histone-fold; 1.
DR   PANTHER; PTHR12075; TFIID-31; 1.
DR   Pfam; PF02291; TFIID-31kDa; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Transcription; Transcription regulation.
FT   CHAIN         1    249       Transcription initiation factor TFIID
FT                                subunit 9B.
FT                                /FTId=PRO_0000118892.
FT   COMPBIAS    241    247       Poly-Asp.
FT   MOD_RES     154    154       Phosphothreonine.
FT   MOD_RES     155    155       Phosphothreonine (By similarity).
FT   CONFLICT     28     28       I -> T (in Ref. 3; AAH66223).
FT   CONFLICT    193    193       A -> T (in Ref. 1; BAE22420).
SQ   SEQUENCE   249 AA;  27172 MW;  5615C356885322FD CRC64;
     MEPAKMAPIK NAPRDALVMA QILKDMGITE YEPRVINQML EFAFRYVTTI LDDAKIYSSH
     AKKPTVDADD VRLAIQCRAD QSFTSPPPRD FLLDIARQKN QTPLPLIKPY AGPRLPPDRY
     CLTAPNYRLK SLVKKGPNQG RLVPRLSAVS SRPTTPPVAP PQAVSGPNKA ATPVSVTSQR
     FAVQIPPSQS TPAKPAPAAT AVQNVLINPS MIGPKNILIT TSMVSSQNTA TDSNPLKRKH
     DDDDDNDTM
//
ID   IF4G1_MOUSE             Reviewed;        1600 AA.
AC   Q6NZJ6; Q6NZN8; Q8BW99;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Eukaryotic translation initiation factor 4 gamma 1;
DE            Short=eIF-4-gamma 1;
DE            Short=eIF-4G 1;
DE            Short=eIF-4G1;
GN   Name=Eif4g1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Fetal brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-520 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   INTERACTION WITH EIF4E3.
RX   PubMed=15153109; DOI=10.1111/j.1432-1033.2004.04149.x;
RA   Joshi B., Cameron A., Jagus R.;
RT   "Characterization of mammalian eIF4E-family members.";
RL   Eur. J. Biochem. 271:2189-2203(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-212; THR-214 AND
RP   SER-1211, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1211, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231 AND SER-1597, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1231 AND SER-1597, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Component of the protein complex eIF4F, which is
CC       involved in the recognition of the mRNA cap, ATP-dependent
CC       unwinding of 5'-terminal secondary structure and recruitment of
CC       mRNA to the ribosome (By similarity).
CC   -!- SUBUNIT: eIF4F is a multi-subunit complex, the composition of
CC       which varies with external and internal environmental conditions.
CC       It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3.
CC       Interacts with eIF3, mutually exclusive with EIF4A1 or EIFA2,
CC       EIF4E and through its N-terminus with PAPBC1. Interacts through
CC       its C-terminus with the serine/threonine kinases MKNK1, and with
CC       MKNK2. Appears to act as a scaffold protein, holding these enzymes
CC       in place to phosphorylate EIF4E. Non-phosphorylated EIF4EBP1
CC       competes with EIF4G1/EIF4G3 to interact with EIF4E; insulin
CC       stimulated MAP-kinase (MAPK1 and MAPK3) phosphorylation of
CC       EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3
CC       to bind and consequent initiation of translation. Interacts with
CC       CIRBP and MIF4GD (By similarity). Interacts with EIF4E3.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6NZJ6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NZJ6-2; Sequence=VSP_013974, VSP_013975;
CC   -!- SIMILARITY: Belongs to the eIF4G family.
CC   -!- SIMILARITY: Contains 1 MI domain.
CC   -!- SIMILARITY: Contains 1 MIF4G domain.
CC   -!- SIMILARITY: Contains 1 W2 domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC066038; AAH66038.1; -; mRNA.
DR   EMBL; BC066103; AAH66103.1; -; mRNA.
DR   EMBL; BC079675; AAH79675.1; -; mRNA.
DR   EMBL; AK053144; BAC35282.1; -; mRNA.
DR   IPI; IPI00421179; -.
DR   IPI; IPI00515195; -.
DR   RefSeq; NP_001005331.1; NM_001005331.1.
DR   RefSeq; NP_666053.2; NM_145941.2.
DR   UniGene; Mm.260256; -.
DR   ProteinModelPortal; Q6NZJ6; -.
DR   SMR; Q6NZJ6; 180-206, 755-995, 1234-1592.
DR   MINT; MINT-1856450; -.
DR   STRING; Q6NZJ6; -.
DR   PhosphoSite; Q6NZJ6; -.
DR   PRIDE; Q6NZJ6; -.
DR   Ensembl; ENSMUST00000044783; ENSMUSP00000047678; ENSMUSG00000045983.
DR   Ensembl; ENSMUST00000115460; ENSMUSP00000111120; ENSMUSG00000045983.
DR   GeneID; 208643; -.
DR   KEGG; mmu:208643; -.
DR   UCSC; uc007yqv.1; mouse.
DR   CTD; 208643; -.
DR   MGI; MGI:2384784; Eif4g1.
DR   HOGENOM; HBG445871; -.
DR   HOVERGEN; HBG052083; -.
DR   InParanoid; Q6NZJ6; -.
DR   OMA; HLSTAQY; -.
DR   OrthoDB; EOG4HX50F; -.
DR   PhylomeDB; Q6NZJ6; -.
DR   NextBio; 372353; -.
DR   ArrayExpress; Q6NZJ6; -.
DR   Bgee; Q6NZJ6; -.
DR   Genevestigator; Q6NZJ6; -.
DR   GermOnline; ENSMUSG00000045983; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0016070; P:RNA metabolic process; IEA:InterPro.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003307; eIF5C.
DR   InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR   InterPro; IPR016021; MIF4-like_typ_1/2/3.
DR   InterPro; IPR003890; MIF4G-like_typ-3.
DR   Gene3D; G3DSA:1.25.40.180; MIF4-like_typ_1/2/3; 2.
DR   Pfam; PF02847; MA3; 1.
DR   Pfam; PF02854; MIF4G; 1.
DR   Pfam; PF02020; W2; 1.
DR   SMART; SM00515; eIF5C; 1.
DR   SMART; SM00544; MA3; 1.
DR   SMART; SM00543; MIF4G; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 3.
DR   PROSITE; PS51366; MI; 1.
DR   PROSITE; PS51363; W2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Initiation factor; Phosphoprotein;
KW   Protein biosynthesis; RNA-binding; Translation regulation.
FT   CHAIN         1   1600       Eukaryotic translation initiation factor
FT                                4 gamma 1.
FT                                /FTId=PRO_0000213322.
FT   DOMAIN      765    993       MIF4G.
FT   DOMAIN     1241   1363       MI.
FT   DOMAIN     1429   1599       W2.
FT   REGION      179    207       PABPC1-binding (By similarity).
FT   REGION      611    622       EIF4E-binding (By similarity).
FT   REGION      686   1089       eIF3/EIF4A-binding (By similarity).
FT   REGION     1450   1600       EIF4A-binding (By similarity).
FT   REGION     1585   1600       Necessary but not sufficient for MKNK1-
FT                                binding (By similarity).
FT   COMPBIAS    464    487       Asp/Glu-rich.
FT   MOD_RES     212    212       Phosphothreonine.
FT   MOD_RES     214    214       Phosphothreonine.
FT   MOD_RES     460    460       Phosphoserine (By similarity).
FT   MOD_RES     598    598       Phosphotyrosine (By similarity).
FT   MOD_RES     651    651       Phosphothreonine (By similarity).
FT   MOD_RES    1096   1096       Phosphoserine (By similarity).
FT   MOD_RES    1099   1099       N6-acetyllysine (By similarity).
FT   MOD_RES    1147   1147       Phosphoserine (By similarity).
FT   MOD_RES    1149   1149       Phosphoserine (By similarity).
FT   MOD_RES    1187   1187       Phosphoserine (By similarity).
FT   MOD_RES    1189   1189       Phosphoserine (By similarity).
FT   MOD_RES    1190   1190       N6-acetyllysine (By similarity).
FT   MOD_RES    1211   1211       Phosphoserine.
FT   MOD_RES    1231   1231       Phosphoserine.
FT   MOD_RES    1238   1238       Phosphoserine (By similarity).
FT   MOD_RES    1597   1597       Phosphoserine.
FT   VAR_SEQ      49     55       Missing (in isoform 2).
FT                                /FTId=VSP_013974.
FT   VAR_SEQ    1046   1052       Missing (in isoform 2).
FT                                /FTId=VSP_013975.
SQ   SEQUENCE   1600 AA;  176077 MW;  8664A8B449C7A128 CRC64;
     MNKAPQPTGP PPARSPGLPQ PAFPPGQTAP VVFSTPQATQ MNTPSQPRQG GFRSLQHFYP
     SRAQPPSSAA SRVQSAAPAR PGPAPHVYPA GSQVMMIPSQ ISYSASQGAY YIPGQGRSTY
     VVPTQQYPVQ PGAPGFYPGA SPTEFGTYAG AYYPAQGVQQ FPASVAPAPV LMNQPPQIAP
     KRERKTIRIR DPNQGGKDIT EEIMSGARTA STPTPPQTGG SLEPQPNGES PQVAVIIRPD
     DRSQGAAIGG RPGLPGPEHS PGTESQPSSP SPTPSPPPIL EPGSESNLGV LSIPGDTMTT
     GMIPMSVEES TPISCETGEP YCLSPEPTLA EPILEVEVTL SKPIPESEFS SSPLQVSTAL
     VPHKVETHEP NGVIPSEDLE PEVESSTEPA PPPLSPCASE SLVPIAPTAQ PEELLNGAPS
     PPAVDLSPVS EPEEQAKKVS SAALASILSP APPVAPSDTS PAQEEEMEED DDDEEGGEAE
     SEKGGEDVPL DSTPVPAQLS QNLEVAAATQ VAVSVPKRRR KIKELNKKEA VGDLLDAFKE
     VDPAVPEVEN QPPTGSNPSP ESEGSMVPTQ PEETEETWDS KEDKIHNAEN IQPGEQKYEY
     KSDQWKPLNL EEKKRYDREF LLGFQFIFAS MQKPEGLPHI TDVVLDKANK TPLRQLDPSR
     LPGINCGPDF TPSFANLGRP ALSNRGPPRG GPGGELPRGP AGLGPRRSQQ GPRKETRKII
     SSVIMTEDIK LNKAEKAWKP SSKRTAADKD RGEEDADGSK TQDLFRRVRS ILNKLTPQMF
     QQLMKQVTQL AIDTEERLKG VIDLIFEKAI SEPNFSVAYA NMCRCLMALK VPTTEKPTVT
     VNFRKLLLNR CQKEFEKDKD DDEVFEKKQK EMDEAATAEE RGRLKEELEE ARDIARRRSL
     GNIKFIGELF KLKMLTEAIM HDCVVKLLKN HDEESLECLC RLLTTIGKDL DFAKAKPRMD
     QYFNQMEKII KEKKTSSRIR FMLQDVLDLR QSNWVPRRGD QGPKTIDQIH KEAEMEEHRE
     HIKVQQLMAK GSDKRRGGPP GPPINRGLPL VDDGGWNTVP ISKGSRPIDT SRLTKITKPG
     SIDSNNQLFA PGGRLSWGKG SSGGSGAKPS DTASEATRPA TLNRFSALQQ TLPAENTDNR
     RVVQRSSLSR ERGEKAGDRG DRLERSERGG DRGDRLDRAR TPATKRSFSK EVEERSRERP
     SQPEGLRKAA SLTEDRGRDP VKREATLPPV SPPKAALSVD EVEKKSKAII EEYLHLNDMK
     EAVQCVQELA SPSLLFIFVR LGIESTLERS TIAREHMGRL LHQLLCAGHL STAQYYQGLY
     ETLELAEDME IDIPHVWLYL AELITPILQE DGVPMGELFR EITKPLRPMG KATSLLLEIL
     GLLCKSMGPK KVGMLWREAG LSWREFLAEG QDVGSFVAEK KVEYTLGEES EAPGQRTLAF
     EELRRQLEKL LKDGGSNQRV FDWIDANLNE QQIASNTLVR ALMTTVCYSA IIFETPLRVD
     VQVLKVRARL LQKYLCDEQK ELQALYALQA LVVTLEQPAN LLRMFFDALY DEDVVKEDAF
     YSWESSKDPA EQQGKGVALK SVTAFFNWLR EAEDEESDHN
//
ID   PTPC1_MOUSE             Reviewed;         747 AA.
AC   Q6NZK8; Q3V0Z6; Q3V3K9; Q3V3Y0; Q6NV81; Q8BKD9;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Protein tyrosine phosphatase domain-containing protein 1;
DE            EC=3.1.3.-;
GN   Name=Ptpdc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-600 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Eye, Hypothalamus, Pituitary, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6NZK8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NZK8-2; Sequence=VSP_029737, VSP_029739;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q6NZK8-3; Sequence=VSP_029738;
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class PTPDC1 subfamily.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE20451.1; Type=Erroneous initiation;
CC       Sequence=BAE21357.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK030415; BAE20451.1; ALT_INIT; mRNA.
DR   EMBL; AK038922; BAE20543.1; -; mRNA.
DR   EMBL; AK053480; BAC35397.1; -; mRNA.
DR   EMBL; AK132781; BAE21357.1; ALT_INIT; mRNA.
DR   EMBL; BC066081; AAH66081.1; -; mRNA.
DR   EMBL; BC068267; AAH68267.1; -; mRNA.
DR   IPI; IPI00411006; -.
DR   IPI; IPI00877321; -.
DR   IPI; IPI00877330; -.
DR   RefSeq; NP_997115.1; NM_207232.1.
DR   UniGene; Mm.315089; -.
DR   HSSP; P29350; 1GWZ.
DR   ProteinModelPortal; Q6NZK8; -.
DR   SMR; Q6NZK8; 80-244.
DR   PRIDE; Q6NZK8; -.
DR   Ensembl; ENSMUST00000035824; ENSMUSP00000047374; ENSMUSG00000038042.
DR   GeneID; 218232; -.
DR   KEGG; mmu:218232; -.
DR   UCSC; uc007qii.1; mouse.
DR   CTD; 218232; -.
DR   MGI; MGI:2145430; Ptpdc1.
DR   eggNOG; roNOG13263; -.
DR   GeneTree; ENSGT00390000004113; -.
DR   HOGENOM; HBG445599; -.
DR   HOVERGEN; HBG058281; -.
DR   InParanoid; Q6NZK8; -.
DR   OMA; EFDPLWK; -.
DR   OrthoDB; EOG4M3987; -.
DR   PhylomeDB; Q6NZK8; -.
DR   NextBio; 376204; -.
DR   ArrayExpress; Q6NZK8; -.
DR   Bgee; Q6NZK8; -.
DR   CleanEx; MM_PTPDC1; -.
DR   Genevestigator; Q6NZK8; -.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   Pfam; PF00782; DSPc; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Hydrolase; Protein phosphatase.
FT   CHAIN         1    747       Protein tyrosine phosphatase domain-
FT                                containing protein 1.
FT                                /FTId=PRO_0000312213.
FT   DOMAIN      168    235       Tyrosine-protein phosphatase.
FT   ACT_SITE    190    190       Phosphocysteine intermediate (By
FT                                similarity).
FT   VAR_SEQ       1     75       Missing (in isoform 2).
FT                                /FTId=VSP_029737.
FT   VAR_SEQ      27     27       D -> DGEEKMLILRHLTDPVWMWSRVFCRLELAEPLRESI
FT                                LLVTASAMLKLRFLTRLSSGLSCCIL (in isoform
FT                                3).
FT                                /FTId=VSP_029738.
FT   VAR_SEQ      76     85       QAIKGVYSSW -> MFHGVWWESV (in isoform 2).
FT                                /FTId=VSP_029739.
FT   CONFLICT      8      8       Q -> H (in Ref. 1; BAE20543).
SQ   SEQUENCE   747 AA;  83934 MW;  7370D3AF44033D32 CRC64;
     MAAGVLPQNE DPYSTLVNSS GHAAHMDENS GRPAPKYTKV GERLRHVIPG HMACSMACGG
     RACKYENPAR WSEQEQAIKG VYSSWVTDNI LAMARPSSEL LEKYRIIEQF LGQGIKTIIN
     LQRPGEHASC GSALEQESGF TYLPEAFMEA GIYFYNFGWK DYGVASLTAI LDMVKVMTFA
     LQEGKVAVHC HAGLGRTGVL IACYLVFATR MTADQAIIFV RAKRPNSIQT RGQLLCVREF
     TQFLAPLRNI FSCCDPKAHA VTLAQYLIRQ RHLLHGYEAR LLKYVPKIIH LVCKLLLDLA
     ENRPVVMKSM LEGPVLSAEI EKTVSEMVTL QLDQELLRQN SDVPDPFNPT AEVAEFENQD
     VILSTEQEFD PLWKRRDIEC LQPLTHLKRQ LSYSDSDLKR AKAILEQGET PWTVPAQELL
     DHSLQHQKPT SHCYMPPTPE LGFNKEALVQ NTFSFWTPSK CGGLEGLKDE GSLLLCRKDI
     PKEVQRSRTF SVGVSCSHNP GEPVPPNFTS IHKDPEQVTH CRCEAPGGWV PGPVHEMVRS
     PCSPLNCGSS PKAQFPHGQE TQDSTDLSEA VPHAGLQPEL SAEARRILAA KALANLNEFV
     EKEEVKRKVE MWQKELNSRE EAWERICGER DPFILCSLMW SWVEQLKEPV ITKEDVDMLV
     DRQADAAEAL FLLEKGQYQT ILCVLHCIVS LQTLPMEVEE ACLLHAIKAF TKVNFDSENG
     PIVYDTLKKI FKHTLEEKRK MAKDSLS
//
ID   CF174_MOUSE             Reviewed;         945 AA.
AC   Q6NZL0; Q8BLM2; Q9CSN3; Q9CU45;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=Uncharacterized protein C6orf174 homolog;
DE   Flags: Precursor;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-912.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 205-945.
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex, Embryo, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC31794.2; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC092095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC153912; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC066079; AAH66079.1; ALT_TERM; mRNA.
DR   EMBL; AK012378; BAB28200.1; -; mRNA.
DR   EMBL; AK018139; BAB31090.1; -; mRNA.
DR   EMBL; AK044134; BAC31794.2; ALT_INIT; mRNA.
DR   IPI; IPI00403618; -.
DR   RefSeq; NP_080414.2; NM_026138.2.
DR   UniGene; Mm.390264; -.
DR   ProteinModelPortal; Q6NZL0; -.
DR   SMR; Q6NZL0; 450-484.
DR   PhosphoSite; Q6NZL0; -.
DR   PRIDE; Q6NZL0; -.
DR   Ensembl; ENSMUST00000092629; ENSMUSP00000090293; ENSMUSG00000038916.
DR   GeneID; 67412; -.
DR   KEGG; mmu:67412; -.
DR   UCSC; uc007est.1; mouse.
DR   MGI; MGI:1914662; 6330407J23Rik.
DR   eggNOG; roNOG07136; -.
DR   GeneTree; ENSGT00530000063889; -.
DR   HOGENOM; HBG444545; -.
DR   HOVERGEN; HBG081115; -.
DR   InParanoid; Q6NZL0; -.
DR   OMA; GKGVRAQ; -.
DR   OrthoDB; EOG402WRV; -.
DR   NextBio; 324494; -.
DR   ArrayExpress; Q6NZL0; -.
DR   Bgee; Q6NZL0; -.
DR   CleanEx; MM_6330407J23RIK; -.
DR   Genevestigator; Q6NZL0; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR021507; DUF3166.
DR   Pfam; PF11365; DUF3166; 2.
PE   2: Evidence at transcript level;
KW   Coiled coil; Membrane; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     25       Potential.
FT   CHAIN        26    945       Uncharacterized protein C6orf174 homolog.
FT                                /FTId=PRO_0000271353.
FT   TRANSMEM    913    933       Helical; (Potential).
FT   COILED      340    724       Potential.
FT   COILED      809    833       Potential.
FT   COMPBIAS     72     81       Poly-Gln.
FT   COMPBIAS     82    246       Gly-rich.
FT   COMPBIAS    268    275       Poly-Ala.
FT   CONFLICT    719    719       Q -> K (in Ref. 2; BAB31090).
SQ   SEQUENCE   945 AA;  103480 MW;  DBF08203CDAA4182 CRC64;
     MSQPPSGGAA PAATSASAAA AATEARMHPE GCSRKQQRAQ SPARPRDNSL RQTAGATRSP
     LGVGPKLNSV RQQQLQQQQQ QGNKITGRST SGTGSRGLGG GAEKAVPSIP KGAVPGAVQP
     APGAEGSPAA ILASVSFRRS GQPEEAPREI ESGPSKVGEP PPLGGVGGGG EGGGAGGGPG
     DREGGAPQPP PPRGWRGKGV RATQRGSSVA EGVSPSPPTA ATSKTPGPGS RNSGSGSTGS
     GSGGGGSYWK EGCLQSELIQ FHLKKERAAA AAAAAQMHTK NGGGGSRSSP VAGAPAICEP
     LVVPSSSPMA AAAEGPQQSA EGNGSGGAMQ AAAPPSSQPH SQQLQEQEDM QEEMEKLREE
     NETLKNEIDE LRTEMDEMRD TFFEEDACQL QEMRHELERA NKNCRILQYR LRKAERKRLR
     YAQTGEIDGE LLRSLEQDLK VAKDVSVRLH HELENVEEKR TTTEDENEKL RQQLIEVEIA
     KQALQNELEK MKELSLKRRG SKDLPKSEKK AQQTPTEDDN EDLKCQLQFV KEEAALMRKK
     MAKIDKEKDR FEHELQKYRS FYGDLDSPLP KGEAGGPPST REAELKLRLR LVEEEANILG
     RKIVELEVEN RGLKAELDDL RGEDFNGSSN PLMREQSESL SELRQHLQLV EDETELLRRN
     VADLEEQNKR ITAELNKYKY KSSGHDSSRH HDNAKTEALQ EELKAARLQI NELSGKVMQL
     QYENRVLMSN MQRYDLASHL GIRGSPRDSD AESDAGKKES DDDSRPPHRK REGPIGGESD
     SEEVRNIRSL TPTRSFYPTP GPWPKSFSDR QQMKDIRSEA ERLGKTIDRL IADTSTIITE
     ARIYVANGDL FGLMDEEDDG SRIREHELLY RINAQMKAFR KELQTFIDRL EVPKSADDRG
     AEEPISVSQM FQPIILLILI LVLFSSLSYT TIFKLVFLFT LFFVL
//
ID   Q6NZM5_MOUSE            Unreviewed;       980 AA.
AC   Q6NZM5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   SubName: Full=Putative uncharacterized protein;
DE   SubName: Full=SLIT and NTRK-like family, member 3;
GN   Name=Slitrk3; ORFNames=mCG_52101;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [11]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC066059; AAH66059.1; -; mRNA.
DR   EMBL; AK158856; BAE34696.1; -; mRNA.
DR   EMBL; CH466547; EDL15486.1; -; Genomic_DNA.
DR   IPI; IPI00421185; -.
DR   RefSeq; NP_942564.2; NM_198864.2.
DR   UniGene; Mm.331076; -.
DR   ProteinModelPortal; Q6NZM5; -.
DR   PRIDE; Q6NZM5; -.
DR   Ensembl; ENSMUST00000059407; ENSMUSP00000088561; ENSMUSG00000048304.
DR   GeneID; 386750; -.
DR   KEGG; mmu:386750; -.
DR   UCSC; uc008pms.1; mouse.
DR   CTD; 386750; -.
DR   MGI; MGI:2679447; Slitrk3.
DR   HOVERGEN; HBG056407; -.
DR   InParanoid; Q6NZM5; -.
DR   OMA; IAPYQTR; -.
DR   PhylomeDB; Q6NZM5; -.
DR   NextBio; 405558; -.
DR   ArrayExpress; Q6NZM5; -.
DR   Bgee; Q6NZM5; -.
DR   Genevestigator; Q6NZM5; -.
DR   GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR000372; LRR-contain_N.
DR   Pfam; PF00560; LRR_1; 1.
DR   SMART; SM00369; LRR_TYP; 3.
DR   SMART; SM00082; LRRCT; 2.
DR   SMART; SM00013; LRRNT; 1.
PE   2: Evidence at transcript level;
KW   Leucine-rich repeat; Repeat.
SQ   SEQUENCE   980 AA;  109406 MW;  C7671B133C601314 CRC64;
     MMKPSIAEML HRGRMLWIIL LSTIALGWTT PIPLIEDSEE IDEPCFDPCY CEVKESLFHI
     HCDSKGFTNI SQITEFWSRP FKLYLQRNSM RRLYTNSFLH LNNAVSINLG NNALQDIQTG
     AFNGLKILKR LYLHENKLDV FRNDTFLGLE SLEYLQADYN VIKRIESGAF RNLSKLRVLI
     LNDNLIPVLP TNLFKAVSLT HLDLRGNRLK VLFYRGMLDH IGRSLMELQL EENPWNCTCE
     IVQLKSWLER IPYTALVGDI TCETPFHFHG KDLREIKKTE LCPLLSDSEV EASLGIPHLS
     SSKENAWPTK PSSMLSSVHF TASSVEYKSS NKQPKPTKQP RTPRPPSTSQ ALYPGPNQPP
     IAPYQTRPPI PIICPTGCTC NLHINDLGLT VNCKERGFNN ISELLPRPLN AKKLYLSSNL
     IQKIYRSDFW NFSSLDLLHL GNNRISYVQD GAFINLPNLK SLFLNGNDIE KLTPGMFRGL
     QSLHYLYFEF NVIREIQPAA FSLMPNLKLL FLNNNLLRTL PTDAFAGTSL ARLNLRKNYF
     LYLPVAGVLE HLNAIVQIDL NENPWDCTCD LVPFKQWIET ISSVSVVGDV LCRTPENLTH
     RDVRTIELEV LCPEMLHIAQ PGPSPPQPGD YHPNGGPTSA SPYEFSPPGG PVPLSVLILS
     LLVLFFSAVF VAAGLFAYVL RRRRKKLPFR SKRQEGVDLT GIQMQCHRLF EDSGGNSGGS
     GGGGRPTLSS PEKAPPVGHV YEYIPHPVTQ MCNNPIYKPR EEEEVAASAA QDTGATDRGG
     PGTQPTGMAE VLLGSEQFAE TPKENHSNYR TLLEKEKEWA LAVSNSQLNT IVTVNHHHPH
     PHHSAVGGVS GVGGGTGGDL AGFRHHEKNG GVVLFPPGGG CGGGSLLLDR ERPQPAPCTV
     GFVDCLYGTV PKLKELHVHP PGMQYPDLQQ DARLKETLLF SAGKGFTDHQ TPKSDYLDLR
     AKLQTKPDYL EVLEKTAYRF
//
ID   HDAC4_MOUSE             Reviewed;        1076 AA.
AC   Q6NZM9; Q3TRZ9; Q3U2J3; Q3V3Y4;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Histone deacetylase 4;
DE            Short=HD4;
DE            EC=3.5.1.98;
GN   Name=Hdac4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Dendritic cell, Epididymis, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH AHRR.
RX   PubMed=17949687; DOI=10.1016/j.bbrc.2007.09.131;
RA   Oshima M., Mimura J., Yamamoto M., Fujii-Kuriyama Y.;
RT   "Molecular mechanism of transcriptional repression of AhR repressor
RT   involving ANKRA2, HDAC4, and HDAC5.";
RL   Biochem. Biophys. Res. Commun. 364:276-282(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on
CC       the N-terminal part of the core histones (H2A, H2B, H3 and H4).
CC       Histone deacetylation gives a tag for epigenetic repression and
CC       plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events. Histone deacetylases act via
CC       the formation of large multiprotein complexes. Involved in muscle
CC       maturation via its interaction with the myocyte enhancer factors
CC       such as MEF2A, MEF2C and MEF2D (By similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC   -!- SUBUNIT: Interacts with HDAC7. Homodimer. Homodimerization via its
CC       N-terminal domain. Interacts with MEF2C and NR2C1. Interacts with
CC       a 14-3-3 chaperone protein in a phosphorylation dependent manner.
CC       Interacts with BTBD14B. Interacts with KDM5B (By similarity).
CC       Interacts with AHRR.
CC   -!- INTERACTION:
CC       Q08775:Runx2; NbExp=1; IntAct=EBI-646397, EBI-903354;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between
CC       the nucleus and the cytoplasm. Upon muscle cells differentiation,
CC       it accumulates in the nuclei of myotubes, suggesting a positive
CC       role of nuclear HDAC4 in muscle differentiation. The export to
CC       cytoplasm depends on the interaction with a 14-3-3 chaperone
CC       protein and is due to its phosphorylation at Ser-245, Ser-465 and
CC       Ser-629 by CaMK4. The nuclear localization probably depends on
CC       sumoylation (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6NZM9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NZM9-2; Sequence=VSP_023952, VSP_023953;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The nuclear export sequence mediates the shuttling between
CC       the nucleus and the cytoplasm (By similarity).
CC   -!- PTM: Phosphorylated by CaMK4 at Ser-245, Ser-465 and Ser-629.
CC       Phosphorylation at other residues is required for the interaction
CC       with 14-3-3 (By similarity).
CC   -!- PTM: Sumoylation on Lys-556 is promoted by the E3 SUMO-protein
CC       ligase RANBP2, and prevented by phosphorylation by CaMK4.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK029933; BAE43272.1; -; mRNA.
DR   EMBL; AK155250; BAE33147.1; -; mRNA.
DR   EMBL; AK162369; BAE36877.1; -; mRNA.
DR   EMBL; BC066052; AAH66052.1; -; mRNA.
DR   IPI; IPI00411004; -.
DR   IPI; IPI00466540; -.
DR   RefSeq; NP_997108.1; NM_207225.1.
DR   UniGene; Mm.318567; -.
DR   HSSP; Q70I53; 1ZZ0.
DR   ProteinModelPortal; Q6NZM9; -.
DR   SMR; Q6NZM9; 62-128, 647-1043.
DR   IntAct; Q6NZM9; 6.
DR   STRING; Q6NZM9; -.
DR   PhosphoSite; Q6NZM9; -.
DR   PRIDE; Q6NZM9; -.
DR   Ensembl; ENSMUST00000008995; ENSMUSP00000008995; ENSMUSG00000026313.
DR   GeneID; 208727; -.
DR   KEGG; mmu:208727; -.
DR   NMPDR; fig|10090.3.peg.788; -.
DR   UCSC; uc007cbf.1; mouse.
DR   CTD; 208727; -.
DR   MGI; MGI:3036234; Hdac4.
DR   eggNOG; roNOG05360; -.
DR   GeneTree; ENSGT00530000062809; -.
DR   HOGENOM; HBG716007; -.
DR   HOVERGEN; HBG057100; -.
DR   InParanoid; Q6NZM9; -.
DR   OMA; RVNHMPS; -.
DR   OrthoDB; EOG44MXRC; -.
DR   PhylomeDB; Q6NZM9; -.
DR   NextBio; 372399; -.
DR   ArrayExpress; Q6NZM9; -.
DR   Bgee; Q6NZM9; -.
DR   CleanEx; MM_HDAC4; -.
DR   Genevestigator; Q6NZM9; -.
DR   GO; GO:0042641; C:actomyosin; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0016563; F:transcription activator activity; IMP:BHF-UCL.
DR   GO; GO:0003714; F:transcription corepressor activity; IGI:MGI.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IDA:MGI.
DR   GO; GO:0045820; P:negative regulation of glycolysis; IMP:BHF-UCL.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:MGI.
DR   GO; GO:0002076; P:osteoblast development; IMP:MGI.
DR   GO; GO:0010552; P:positive regulation of gene-specific transcription from RNA polymerase II promoter; IMP:BHF-UCL.
DR   GO; GO:0033235; P:positive regulation of protein sumoylation; ISS:UniProtKB.
DR   GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; IMP:MGI.
DR   GO; GO:0014894; P:response to denervation involved in regulation of muscle adaptation; IMP:BHF-UCL.
DR   GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR017320; Histone_deAcase_II_euk.
DR   Gene3D; G3DSA:3.40.800.20; His_deacetylse; 1.
DR   PANTHER; PTHR10625; His_deacetylse; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037911; HDAC_II_euk; 1.
DR   PRINTS; PR01270; HDASUPER.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromatin regulator; Coiled coil; Cytoplasm;
KW   Hydrolase; Isopeptide bond; Nucleus; Phosphoprotein; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN         1   1076       Histone deacetylase 4.
FT                                /FTId=PRO_0000281033.
FT   REGION      117    312       Interaction with MEF2A (By similarity).
FT   REGION      652   1076       Histone deacetylase (By similarity).
FT   COILED       66    169       Potential.
FT   MOTIF      1043   1076       Nuclear export signal (By similarity).
FT   COMPBIAS    464    499       Gln-rich.
FT   COMPBIAS    561    568       Poly-Glu.
FT   ACT_SITE    795    795       By similarity.
FT   MOD_RES     245    245       Phosphoserine; by CaMK4 (By similarity).
FT   MOD_RES     349    349       Phosphoserine (By similarity).
FT   MOD_RES     465    465       Phosphoserine.
FT   MOD_RES     562    562       Phosphoserine (By similarity).
FT   MOD_RES     629    629       Phosphoserine; by CaMK4 (By similarity).
FT   MOD_RES     630    630       Phosphoserine (By similarity).
FT   CROSSLNK    556    556       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   VAR_SEQ       1    171       Missing (in isoform 2).
FT                                /FTId=VSP_023952.
FT   VAR_SEQ     732    732       S -> SKKLLG (in isoform 2).
FT                                /FTId=VSP_023953.
FT   CONFLICT    569    569       A -> S (in Ref. 1; BAE33147).
FT   CONFLICT    904    904       R -> K (in Ref. 1; BAE33147).
SQ   SEQUENCE   1076 AA;  118562 MW;  A3CCC3CCCBB903A0 CRC64;
     MSSQSHPDGL SGRDQPVELL NPARVNHMPS TVDVATALPL QVAPTAVPMD LRLDHQFSLP
     LEPALREQQL QQELLALKQK QQIQRQILIA EFQRQHEQLS RQHEAQLHEH IKQQQEMLAM
     KHQQELLEHQ RKLERHRQEQ ELEKQHREQK LQQLKNKEKG KESAVASTEV KMKLQEFVLN
     KKKALAHRNL NHCISSDPRY WYGKTQHSSL DQSSPPQSGV SASYNHPVLG MYDAKDDFPL
     RKTASEPNLK LRSRLKQKVA ERRSSPLLRR KDGPVATALK KRPLDVTDSA CSSAPGSGPS
     SPNSSSGNVS TENGIAPTVP SAPAETSLAH RLVTREGSVA PLPLYTSPSL PNITLGLPAT
     GPAAGAAGQQ DAERLALPAL QQRILFPGTH LTPYLSTSPL ERDGAAAHNP LLQHMVLLEQ
     PPTQTPLVTG LGALPLHSQS LVGADRVSPS IHKLRQHRPL GRTQSAPLPQ NAQALQHLVI
     QQQHQQFLEK HKQQFQQQQL HLSKIISKPS EPPRQPESHP EETEEELREH QALLDEPYLD
     RLPGQKEPSL AGVQVKQEPI ESEEEEAEAT RETEPGQRPA TEQELLFRQQ ALLLEQQRIH
     QLRNYQASME AAGIPVSFGS HRPLSRAQSS PASATFPMSV QEPPTKPRFT TGLVYDTLML
     KHQCTCGNTN SHPEHAGRIQ SIWSRLQETG LRGKCECIRG RKATLEELQT VHSEAHTLLY
     GTNPLNRQKL DSSLTSVFVR LPCGGVGVDS DTIWNEVHSS GAARLAVGCV VELVFKVATG
     ELKNGFAVVR PPGHHAEEST PMGFCYFNSV AVAAKLLQQR LNVSKILIVD WDVHHGNGTQ
     QAFYNDPNVL YMSLHRYDDG NFFPGSGAPD EVGTGPGVGF NVNMAFTGGL EPPMGDAEYL
     AAFRTVVMPI ANEFAPDVVL VSSGFDAVEG HPTPLGGYNL SAKCFGYLTK QLMGLAGGRL
     VLALEGGHDL TAICDASEAC VSALLGNELE PLPEKVLHQR PNANAVHSME KVMDIHSKYW
     RCLQRLSSTV GHSLIEAQKC EKEEAETVTA MASLSVGVKP AEKRSEEEPM EEEPPL
//
ID   RBM26_MOUSE             Reviewed;        1012 AA.
AC   Q6NZN0; Q3TA77; Q3UTU9; Q8BQ22; Q8C7W9; Q8K101; Q921K4;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=RNA-binding protein 26;
DE   AltName: Full=Protein expressed in male leptotene and zygotene spermatocytes 393;
DE            Short=MLZ-393;
DE   AltName: Full=RNA-binding motif protein 26;
GN   Name=Rbm26;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 723-1012 (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 780-1012 (ISOFORM 5).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-746 (ISOFORM 4), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-999 (ISOFORM 3).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Cerebellum, Spinal ganglion, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF 692-701, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=20339383; DOI=10.1038/jhg.2010.26;
RA   Kogo H., Kowa-Sugiyama H., Yamada K., Bolor H., Tsutsumi M., Ohye T.,
RA   Inagaki H., Taniguchi M., Toda T., Kurahashi H.;
RT   "Screening of genes involved in chromosome segregation during meiosis
RT   I: toward the identification of genes responsible for infertility in
RT   humans.";
RL   J. Hum. Genet. 55:293-299(2010).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q6NZN0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NZN0-2; Sequence=VSP_022535;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q6NZN0-3; Sequence=VSP_022533, VSP_022535;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q6NZN0-4; Sequence=VSP_022533;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q6NZN0-5; Sequence=VSP_022534;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in testis and ovary.
CC   -!- DEVELOPMENTAL STAGE: Expressed in testis and ovary at E15.5.
CC   -!- SIMILARITY: Contains 1 C3H1-type zinc finger.
CC   -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH29079.1; Type=Erroneous initiation;
CC       Sequence=BAC33537.1; Type=Frameshift; Positions=442;
CC       Sequence=BAC34721.1; Type=Frameshift; Positions=40;
CC       Sequence=BAE23881.1; Type=Erroneous initiation;
CC       Sequence=BAE42792.1; Type=Erroneous initiation;
CC       Sequence=BC066051; Type=Frameshift; Positions=990;
CC   -----------------------------------------------------------------------
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DR   EMBL; BC011531; AAH11531.1; -; mRNA.
DR   EMBL; BC029079; AAH29079.1; ALT_INIT; mRNA.
DR   EMBL; BC066051; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK049083; BAC33537.1; ALT_FRAME; mRNA.
DR   EMBL; AK051686; BAC34721.1; ALT_FRAME; mRNA.
DR   EMBL; AK139077; BAE23881.1; ALT_INIT; mRNA.
DR   EMBL; AK172039; BAE42792.1; ALT_INIT; mRNA.
DR   IPI; IPI00223561; -.
DR   IPI; IPI00466369; -.
DR   IPI; IPI00828361; -.
DR   IPI; IPI00828405; -.
DR   IPI; IPI00828462; -.
DR   RefSeq; NP_598838.3; NM_134077.4.
DR   UniGene; Mm.291542; -.
DR   UniGene; Mm.474531; -.
DR   UniGene; Mm.474826; -.
DR   ProteinModelPortal; Q6NZN0; -.
DR   SMR; Q6NZN0; 533-610, 894-964.
DR   PhosphoSite; Q6NZN0; -.
DR   PRIDE; Q6NZN0; -.
DR   Ensembl; ENSMUST00000022715; ENSMUSP00000022715; ENSMUSG00000022119.
DR   Ensembl; ENSMUST00000077531; ENSMUSP00000076736; ENSMUSG00000022119.
DR   GeneID; 74213; -.
DR   KEGG; mmu:74213; -.
DR   UCSC; uc007uxk.1; mouse.
DR   UCSC; uc007uxm.1; mouse.
DR   UCSC; uc007uxn.1; mouse.
DR   CTD; 74213; -.
DR   MGI; MGI:1921463; Rbm26.
DR   eggNOG; roNOG08927; -.
DR   GeneTree; ENSGT00510000046929; -.
DR   HOVERGEN; HBG057372; -.
DR   InParanoid; Q6NZN0; -.
DR   OMA; IKTKTQM; -.
DR   OrthoDB; EOG498V06; -.
DR   NextBio; 340120; -.
DR   ArrayExpress; Q6NZN0; -.
DR   Bgee; Q6NZN0; -.
DR   CleanEx; MM_RBM26; -.
DR   Genevestigator; Q6NZN0; -.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR002483; PWI.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR000571; Znf_CCCH.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   Gene3D; G3DSA:1.20.1390.10; PWI; 1.
DR   Pfam; PF01480; PWI; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   PROSITE; PS50102; RRM; 2.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil;
KW   Direct protein sequencing; Metal-binding; Phosphoprotein; Repeat;
KW   RNA-binding; Zinc; Zinc-finger.
FT   CHAIN         1   1012       RNA-binding protein 26.
FT                                /FTId=PRO_0000273377.
FT   DOMAIN      537    611       RRM 1.
FT   DOMAIN      896    965       RRM 2.
FT   ZN_FING     288    316       C3H1-type.
FT   COILED       98    127       Potential.
FT   COILED      724    800       Potential.
FT   COILED      828    852       Potential.
FT   COMPBIAS    134    213       Arg-rich.
FT   COMPBIAS    326    420       Pro-rich.
FT   MOD_RES     127    127       Phosphoserine (By similarity).
FT   MOD_RES     515    515       N6-acetyllysine (By similarity).
FT   MOD_RES     523    523       Phosphoserine (By similarity).
FT   MOD_RES     621    621       Phosphoserine (By similarity).
FT   VAR_SEQ     426    430       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_022533.
FT   VAR_SEQ     984   1012       FQEESLVDDSLLQDDDEEEEDNESRSWRR -> RENITA
FT                                (in isoform 5).
FT                                /FTId=VSP_022534.
FT   VAR_SEQ     991   1012       DDSLLQDDDEEEEDNESRSWRR -> VGFFFFSLVFPSLFI
FT                                VLL (in isoform 2 and isoform 3).
FT                                /FTId=VSP_022535.
FT   CONFLICT    324    324       N -> K (in Ref. 2; BAC33537).
FT   CONFLICT    494    494       S -> Y (in Ref. 2; BAC33537).
FT   CONFLICT    550    550       N -> S (in Ref. 2; BAE42792).
FT   CONFLICT    777    777       E -> G (in Ref. 2; BAC33537).
FT   CONFLICT    786    786       T -> S (in Ref. 2; BAC33537).
SQ   SEQUENCE   1012 AA;  114143 MW;  EBD1FD8C14BE106F CRC64;
     MVSKMIIENF EALKSWLSKT LEPICDADPS ALAKYVLALV KKDKSEKELK ALCIDQLDVF
     LQKETQIFVE KLFDAVNTKS YLPPPEQPSS GSLKVDFLQH QEKDIKKEEL TKEEEREKKF
     SRRLNHSPPQ SSSRYRDNRS RDERKKDDRS RKRDYDRNPP RRDSYRDRYN RRRGRSRSYS
     RSRSRSWSKE RLRDRDRDRS RTRSRSRTRS RERDLVKPKY DLDRTDPLEN NYTPVSSVSN
     ISSGHYPVPT LSSTITVIAP THHGNNTTES WSEFHEDQVD HNSYVRPPMP KKRCRDYDEK
     GFCMRGDMCP FDHGSDPVVV EDVNLPGMLP FPAQPPVVEG PPPPGLPPPP PILTPPPVNL
     RPPVPPPGPL PPSLPPVTGP PPPLPPLQPS GMDAPPNSAT SSVPTVVTTG IHHQPPPAPP
     SLFTAVFVLP DTYDTDGYNP EAPSITNTSR PMYRHRVHAQ RPNLIGLTSG DMDLPPREKP
     PNKSSMRIVV DSESRKRTIG SGEPGVSTKK TWFDKPNFNR TNSPGFQKKV QFGNENTKLE
     LRKVPPELNN ISKLNEHFSR FGTLVNLQVA YNGDPEGALI QFATYEEAKK AISSTEAVLN
     NRFIKVYWHR EGTTQQLQTT SPKVIQPLVQ QPILPVVKQS VKERLGPVPS ATTEPAEAQS
     ATSELPQNVT KLSVKDRLGF VSKPSVSATE KVLSTSTGLT KTVYNPAALK AAQKTLSVST
     PAVDNNEAQK KKQEALKLQQ DVRKRKQEIL EKHIETQKML ISKLEKNKTM KSEDKAEIMK
     TLEILTKNIT KLKDEVKSTS PGRCLPKSIK TKTQMQKELL DTELDLYKKM QAGEEVTELR
     RKYTELQLEA AKRGILSSGR GRGIHTRGRG TAHGRGRGRG RGRGVPGHAV VDHRPRALEI
     SAFTESDRED LLPHFAQYGE IEDCQIDDAS LHAIITFKTR AEAEAAAIHG ARFKGQDLKL
     AWNKPIANMS AVDTEEAEPD EEEFQEESLV DDSLLQDDDE EEEDNESRSW RR
//
ID   MARH1_MOUSE             Reviewed;         289 AA.
AC   Q6NZQ8; Q3U7M8; Q3UVF8; Q8C294; Q8CBA1;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=E3 ubiquitin-protein ligase MARCH1;
DE            EC=6.3.2.-;
DE   AltName: Full=Membrane-associated RING finger protein 1;
DE   AltName: Full=Membrane-associated RING-CH protein I;
DE            Short=MARCH-I;
GN   Name=March1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Aorta, Bone, Bone marrow, Cerebellum, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION AS AN E3 UBIQUITIN LIGASE FOR HLA-DRB.
RX   PubMed=17051151; DOI=10.1038/nature05261;
RA   Shin J.S., Ebersold M., Pypaert M., Delamarre L., Hartley A.,
RA   Mellman I.;
RT   "Surface expression of MHC class II in dendritic cells is controlled
RT   by regulated ubiquitination.";
RL   Nature 444:115-118(2006).
RN   [4]
RP   FUNCTION AS AN E3 UBIQUITIN LIGASE FOR HLA-DRB, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=17255932; DOI=10.1038/sj.emboj.7601556;
RA   Matsuki Y., Ohmura-Hoshino M., Goto E., Aoki M., Mito-Yoshida M.,
RA   Uematsu M., Hasegawa T., Koseki H., Ohara O., Nakayama M., Toyooka K.,
RA   Matsuoka K., Hotta H., Yamamoto A., Ishido S.;
RT   "Novel regulation of MHC class II function in B cells.";
RL   EMBO J. 26:846-854(2007).
RN   [5]
RP   FUNCTION AS REGULATOR OF ANTIGEN PRESENTATION, PTM, MUTAGENESIS OF
RP   TRP-114; LEU-225 AND TYR-232, AND SUBCELLULAR LOCATION.
RX   PubMed=19880452; DOI=10.4049/jimmunol.0901521;
RA   Jabbour M., Campbell E.M., Fares H., Lybarger L.;
RT   "Discrete domains of MARCH1 mediate its localization, functional
RT   interactions, and posttranscriptional control of expression.";
RL   J. Immunol. 183:6500-6512(2009).
RN   [6]
RP   FUNCTION AS AN E3 UBIQUITIN LIGASE FOR HLA-DR AND REGULATOR OF ANTIGEN
RP   PRESENTATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19917682; DOI=10.4049/jimmunol.0902178;
RA   Ohmura-Hoshino M., Matsuki Y., Mito-Yoshida M., Goto E.,
RA   Aoki-Kawasumi M., Nakayama M., Ohara O., Ishido S.;
RT   "Requirement of MARCH-I-mediated MHC II ubiquitination for the
RT   maintenance of conventional dendritic cells.";
RL   J. Immunol. 183:6893-6897(2009).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination
CC       of TFRC, CD86, FAS and MHC class II proteins, such as HLA-DR alpha
CC       and beta, and promotes their subsequent endocytosis and sorting to
CC       lysosomes via multivesicular bodies. By constitutively
CC       ubiquitinating MHC class II proteins in immature dendritic cells,
CC       downregulates their cell surface localization thus sequestering
CC       them in the intracellular endosomal system.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Multi-pass
CC       membrane protein (By similarity). Late endosome membrane. Early
CC       endosome membrane. Golgi apparatus, trans-Golgi network membrane.
CC       Lysosome membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q6NZQ8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NZQ8-2; Sequence=VSP_022726;
CC       Name=3;
CC         IsoId=Q6NZQ8-3; Sequence=VSP_022727;
CC       Name=4;
CC         IsoId=Q6NZQ8-4; Sequence=VSP_022726, VSP_022728;
CC       Name=5;
CC         IsoId=Q6NZQ8-5; Sequence=VSP_022728;
CC   -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3
CC       ligase activity (By similarity).
CC   -!- PTM: Has a short half-life. Instability/short half-life permits
CC       rapid changes that allow efficient induction of antigen
CC       presentation once antigen presenting cells, APCs, receive
CC       maturation signals. Small changes in protein levels significantly
CC       alter the cell surface display of MHC class II proteins.
CC   -!- DISRUPTION PHENOTYPE: Shows increase in the cell surface
CC       expression or half-life of MHC class II. Null cells have
CC       accumulated MHC class II and CD86 at the cell surface and a low
CC       antigen-presenting ability for exogenous antigens, in conventional
CC       dendritic cells (PubMed:19917682). Null cells have high antigen-
CC       presenting ability for exogenous antigens in B-cells
CC       (PubMed:17255932).
CC   -!- SIMILARITY: Contains 1 RING-CH-type zinc finger.
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DR   EMBL; AK036489; BAC29449.1; -; mRNA.
DR   EMBL; AK089040; BAC40715.1; -; mRNA.
DR   EMBL; AK137337; BAE23311.1; -; mRNA.
DR   EMBL; AK152592; BAE31341.1; -; mRNA.
DR   EMBL; AK163081; BAE37183.1; -; mRNA.
DR   EMBL; BC066008; AAH66008.1; -; mRNA.
DR   IPI; IPI00421198; -.
DR   IPI; IPI00467707; -.
DR   IPI; IPI00652150; -.
DR   IPI; IPI00751349; -.
DR   IPI; IPI00756223; -.
DR   RefSeq; NP_001159844.1; NM_001166372.1.
DR   RefSeq; NP_001159847.1; NM_001166375.1.
DR   RefSeq; NP_780397.2; NM_175188.4.
DR   UniGene; Mm.380457; -.
DR   UniGene; Mm.479228; -.
DR   ProteinModelPortal; Q6NZQ8; -.
DR   SMR; Q6NZQ8; 72-136.
DR   PRIDE; Q6NZQ8; -.
DR   Ensembl; ENSMUST00000072482; ENSMUSP00000072302; ENSMUSG00000036469.
DR   Ensembl; ENSMUST00000098708; ENSMUSP00000096305; ENSMUSG00000036469.
DR   Ensembl; ENSMUST00000110253; ENSMUSP00000105882; ENSMUSG00000036469.
DR   Ensembl; ENSMUST00000110258; ENSMUSP00000105887; ENSMUSG00000036469.
DR   GeneID; 72925; -.
DR   KEGG; mmu:72925; -.
DR   UCSC; uc009lvl.1; mouse.
DR   CTD; 72925; -.
DR   MGI; MGI:1920175; March1.
DR   eggNOG; roNOG04100; -.
DR   GeneTree; ENSGT00570000078779; -.
DR   HOVERGEN; HBG081957; -.
DR   OMA; KXVLEWP; -.
DR   NextBio; 337147; -.
DR   ArrayExpress; Q6NZQ8; -.
DR   Bgee; Q6NZQ8; -.
DR   CleanEx; MM_MARCH1; -.
DR   Genevestigator; Q6NZQ8; -.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0002495; P:antigen processing and presentation of peptide antigen via MHC class II; IMP:UniProtKB.
DR   GO; GO:0006955; P:immune response; IDA:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR011016; Znf_RING-CH.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00744; RINGv; 1.
DR   PROSITE; PS51292; ZF_RING_CH; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasmic vesicle; Endosome; Golgi apparatus;
KW   Immunity; Ligase; Lysosome; Membrane; Metal-binding; Transmembrane;
KW   Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    289       E3 ubiquitin-protein ligase MARCH1.
FT                                /FTId=PRO_0000274366.
FT   TRANSMEM    155    175       Helical; (Potential).
FT   TRANSMEM    197    217       Helical; (Potential).
FT   ZN_FING      72    133       RING-CH-type.
FT   REGION        1     66       Responsible for low stability.
FT   REGION      222    279       Responsible for down-regulation of CD86
FT                                and MHC class II cell surface expression.
FT   VAR_SEQ       1     54       MLGWCEAIARNPHRIPNTTRTPETSGDVADASQTSTLNEKS
FT                                PGRSASRSSNISK -> MNLTMSNMTSSHICCNFLNMWKKS
FT                                KISTMYYLNQDAKLSNLFLQ (in isoform 2 and
FT                                isoform 4).
FT                                /FTId=VSP_022726.
FT   VAR_SEQ       1     37       MLGWCEAIARNPHRIPNTTRTPETSGDVADASQTSTL ->
FT                                MPLHQISVIPARETASNGRSSMGRNKEKNKEVE (in
FT                                isoform 3).
FT                                /FTId=VSP_022727.
FT   VAR_SEQ     187    190       Missing (in isoform 4 and isoform 5).
FT                                /FTId=VSP_022728.
FT   MUTAGEN     114    114       W->A: Loss of ubiquitin ligase activity
FT                                and loss of down-regulation of CD86 cell
FT                                surface expression.
FT   MUTAGEN     225    225       L->S: Partial loss of down-regulation of
FT                                CD86 cell surface expression. Almost
FT                                complete loss of down-regulation of CD86
FT                                cell surface expression; when associated
FT                                with F-232.
FT   MUTAGEN     232    232       Y->F: Almost complete loss of down-
FT                                regulation of CD86 cell surface
FT                                expression; when associated with S-225.
FT   CONFLICT     85     85       C -> Y (in Ref. 1; BAE31341).
SQ   SEQUENCE   289 AA;  32347 MW;  0DBE9A308D5ED0CE CRC64;
     MLGWCEAIAR NPHRIPNTTR TPETSGDVAD ASQTSTLNEK SPGRSASRSS NISKASSPTT
     GTAPRSQSRL SVCPSTQDIC RICHCEGDEE SPLITPCRCT GTLRFVHQSC LHQWIKSSDT
     RCCELCKYDF IMETKLKPLR KWEKLQMTTS ERRKIFCSVT FHVIAVTCVV WSLYVLIDRT
     AEEIKQGNDN GVLEWPFWTK LVVVAIGFTG GLVFMYVQCK VYVQLWRRLK AYNRVIFVQN
     CPDTANKLEK NFPCNVNTEI KDAVVVPVPQ TGSNTLPTAE GAPPEVIPV
//
ID   SLX4_MOUSE              Reviewed;        1565 AA.
AC   Q6P1D7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 44.
DE   RecName: Full=Structure-specific endonuclease subunit SLX4;
DE   AltName: Full=BTB/POZ domain-containing protein 12;
GN   Name=Slx4; Synonyms=Btbd12;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1117, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
CC   -!- FUNCTION: Regulatory subunit that interacts with and increases the
CC       activity of different structure-specific endonucleases. Has
CC       several distinct roles in protecting genome stability by resolving
CC       diverse forms of deleterious DNA structures originating from
CC       replication and recombination intermediates and from DNA damage.
CC       Component of the SLX1-SLX4 structure-specific endonuclease that
CC       resolves DNA secondary structures generated during DNA repair and
CC       recombination. Has endonuclease activity towards branched DNA
CC       substrates, introducing single-strand cuts in duplex DNA close to
CC       junctions with ss-DNA. Has a preference for 5'-flap structures,
CC       and promotes symmetrical cleavage of static and migrating Holliday
CC       junctions (HJs). Resolves HJs by generating two pairs of
CC       ligatable, nicked duplex products. Interacts with the structure-
CC       specific ERCC4-ERCC1 endonuclease and promotes the cleavage of
CC       bubble structures. Interacts with the structure-specific MUS81-
CC       EME1 endonuclease and promotes the cleavage of 3'-flap and
CC       replication fork-like structures. SLX4 is required for recovery
CC       from alkylation-induced DNA damage and is involved in the
CC       resolution of DNA double-strand breaks (By similarity).
CC   -!- SUBUNIT: Forms a heterodimer with SLX1A/GIYD1. Interacts with
CC       ERCC4; catalytic subunit of the ERCC4-ERCC1 endonuclease.
CC       Interacts with MUS81; catalytic subunit of the MUS81-EME1
CC       endonuclease. Interacts with MSH2; component of the MSH2-MSH3
CC       mismatch repair complex. Interacts with TERF2-TERF2IP. Interacts
CC       with PLK1 and C20ORF94 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Note=Localizes to
CC       sites of DNA dammage (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Belongs to the SLX4 family.
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
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DR   EMBL; BC065125; AAH65125.1; -; mRNA.
DR   IPI; IPI00408258; -.
DR   RefSeq; NP_803423.2; NM_177472.4.
DR   UniGene; Mm.29935; -.
DR   ProteinModelPortal; Q6P1D7; -.
DR   SMR; Q6P1D7; 498-604.
DR   STRING; Q6P1D7; -.
DR   PhosphoSite; Q6P1D7; -.
DR   PRIDE; Q6P1D7; -.
DR   Ensembl; ENSMUST00000040790; ENSMUSP00000038871; ENSMUSG00000039738.
DR   GeneID; 52864; -.
DR   KEGG; mmu:52864; -.
DR   UCSC; uc007xzg.1; mouse.
DR   CTD; 52864; -.
DR   MGI; MGI:106299; Btbd12.
DR   HOGENOM; HBG402812; -.
DR   InParanoid; Q6P1D7; -.
DR   OMA; EHQALQD; -.
DR   OrthoDB; EOG4S1T8J; -.
DR   PhylomeDB; Q6P1D7; -.
DR   NextBio; 309663; -.
DR   ArrayExpress; Q6P1D7; -.
DR   Bgee; Q6P1D7; -.
DR   Genevestigator; Q6P1D7; -.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR013069; BTB_POZ.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF00651; BTB; 1.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   1: Evidence at protein level;
KW   DNA damage; DNA recombination; DNA repair; Nucleus; Phosphoprotein.
FT   CHAIN         1   1565       Structure-specific endonuclease subunit
FT                                SLX4.
FT                                /FTId=PRO_0000383567.
FT   DOMAIN      506    579       BTB.
FT   REGION      499   1565       Interaction with PLK1 and TERF2-TERF2IP
FT                                (By similarity).
FT   REGION     1120   1413       Interaction with MUS81 (By similarity).
FT   REGION     1406   1565       Interaction with SLX1 (By similarity).
FT   MOD_RES     111    111       Phosphoserine (By similarity).
FT   MOD_RES     845    845       Phosphoserine (By similarity).
FT   MOD_RES    1117   1117       Phosphothreonine.
FT   MOD_RES    1237   1237       Phosphoserine (By similarity).
FT   MOD_RES    1254   1254       Phosphoserine (By similarity).
SQ   SEQUENCE   1565 AA;  172412 MW;  AB4CB4EB57CA6394 CRC64;
     MVPESAPNGN SQPLPSCFTT TGVPSPSKPR VSELVLQRMK QFKRADPERL RHASEESPQK
     TALGDDVPRS PPEETVGENE YKLDATDSDA AMALALQQEF RREEASSHHD SLEEKGLFFC
     QMCQKNLSAM NVTRREQHVN RCLDEAEKAQ RPASPRIPDC PICGKPFLTT KSRISHLKQC
     AVRMEVGPQL LLQAVRLQTA QPEVDGSPQV PSFSNNVGGL KRKGVTTKRE PRRRKVNKPE
     APSEDLLVAM ALSRSEVEHC PVVPPLRLEN AFSEKIRLGA EKKSRKKRPP VCPPQLVTQD
     SETTGRQIED RVAQLLSEEA ELSCTPPLLA SKISKEELEP AGWRARLPEG KRNFLWELSA
     LTGAWAEESF YTVGLFPPIV SQCPSKEPQL PLELPKQGEP SPRRPPASQS SLPVSHSPKI
     RLLSSSQRER QALQDLVDLA VEGLSSSPQP GSRGVPTGLD LVPSSLPLTG FVLPCKKTLK
     KDDSASLSLG LLVTDFGAMV NNPHLSDVQF QLDSGEVLYA HKFVLYARCP LLIQYVSTES
     FSSEEDGDLT QRALLSDVSS EAAHAFLNYL YMADTDMPPS LVPDLRSLAL RFGVSDLVQL
     CEQVPAVVDL EGEQPEETSE DCESRAETFL ELLRSVWVDN EEEVETLLKP ELCEEERERV
     NEAEMEEIYE FAATQRKLLQ WGRAADPDGS TNPHGEDGAV SEPSLAGVQS NRQLENTEHM
     ESSGLEKEEA LASWEQEGHS TPLQDQCPDW AGKAEAQDAL GEATDDPSFC SRHRRGKECL
     PLHPNKAHGC KQPLPSNPRV SSELSQITVD HEEQSDHVRE TQADMAQAPT PHSCSLVSQS
     SVDGSPSQSW LHLYHTSHLS PSVSQSHSSI SRVASPRSLS PTTPTKQRRG SNIVTLRKDA
     GHHRGQQSSP IAGHRNRGIL ISPAKSPPID LTQSVPEPLS PRAQDPLHFV KKEDEVILLL
     DSDEELEHTK TESVSKDSPE GRKVPEFSPR SSELFSVIDV EEDHEHFQSP LKREAGLQHG
     EEGQLGNQSA LGCRDIPWLL CSQKTSLDED SATDTSWLVP ATPGVSRSRD CSSQTQIKSL
     KTRIPSDETA QQTPRPNLER RTMLETAQQF SVIMPHTQPI TLGAFDSGRQ AYRSPSHPYP
     RHHRLSSSQP SCPGPDFTRW SQKSSAPRPC LPNLPAADDV VEVGDSDDEV ASHQGNSSPV
     LDGDPPGPMG DYCWNEPLSP IPIDHLNLER TGPLTTSSPS SQVLEALHSD DCHSPGLGTT
     PIRGSCGTLR ESQERSSLAG SPEALWDDWN EEEGQSPEAP PVAQMLSTRT RKPDRPETPK
     GANQKKNLPP KVPITPMPRY SIMETPVLKK ELDRFGVRAL PKRQMVLKLK EIFQYTHQTL
     ESDSEDEVQS PQIPAELPCR QASTTETCNP SRLPTGEPSH PDGDAQLPAS QESMATSVDG
     SDNSFSSKSS SAEFGAAFEY SDEDKDEEVG VTASQAAIQA ADTEEAVRRY IRSKPALHRQ
     VLRYQPVELA ELQAELKQNG IPVAMGKLSD ILDAQCITFT TAAARKEKLK HKRRQPSGRK
     KKDQK
//
ID   2ABA_MOUSE              Reviewed;         447 AA.
AC   Q6P1F6;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform;
DE   AltName: Full=PP2A subunit B isoform B55-alpha;
DE   AltName: Full=PP2A subunit B isoform PR55-alpha;
DE   AltName: Full=PP2A subunit B isoform R2-alpha;
DE   AltName: Full=PP2A subunit B isoform alpha;
GN   Name=Ppp2r2a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and C57BL/6J; TISSUE=Brain, and Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 200-210, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
CC   -!- FUNCTION: The B regulatory subunit might modulate substrate
CC       selectivity and catalytic activity, and also might direct the
CC       localization of the catalytic enzyme to a particular subcellular
CC       compartment (By similarity).
CC   -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme,
CC       composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa
CC       constant regulatory subunit (PR65 or subunit A), that associates
CC       with a variety of regulatory subunits. Proteins that associate
CC       with the core dimer include three families of regulatory subunits
CC       B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56
CC       families), the 48 kDa variable regulatory subunit, viral proteins,
CC       and cell signaling molecules. Interacts with TP53. Found in a
CC       complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and
CC       TBCD (By similarity).
CC   -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B
CC       family.
CC   -!- SIMILARITY: Contains 7 WD repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC065100; AAH65100.1; -; mRNA.
DR   EMBL; BC080692; AAH80692.1; -; mRNA.
DR   IPI; IPI00667471; -.
DR   RefSeq; NP_082308.1; NM_028032.2.
DR   UniGene; Mm.273997; -.
DR   ProteinModelPortal; Q6P1F6; -.
DR   SMR; Q6P1F6; 8-446.
DR   PRIDE; Q6P1F6; -.
DR   Ensembl; ENSMUST00000089230; ENSMUSP00000086640; ENSMUSG00000022052.
DR   GeneID; 71978; -.
DR   KEGG; mmu:71978; -.
DR   UCSC; uc007uku.1; mouse.
DR   CTD; 71978; -.
DR   MGI; MGI:1919228; Ppp2r2a.
DR   HOVERGEN; HBG000012; -.
DR   InParanoid; Q6P1F6; -.
DR   OrthoDB; EOG4M0F1K; -.
DR   PhylomeDB; Q6P1F6; -.
DR   NextBio; 335106; -.
DR   ArrayExpress; Q6P1F6; -.
DR   Bgee; Q6P1F6; -.
DR   Genevestigator; Q6P1F6; -.
DR   GermOnline; ENSMUSG00000022052; Mus musculus.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:InterPro.
DR   GO; GO:0008601; F:protein phosphatase type 2A regulator activity; IEA:InterPro.
DR   GO; GO:0043278; P:response to morphine; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR000009; PP2A_PR55.
DR   InterPro; IPR018067; PP2A_PR55_CS.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 3.
DR   PANTHER; PTHR11871; Pp2A_PR55; 1.
DR   Pfam; PF00400; WD40; 2.
DR   PIRSF; PIRSF037309; PP2A_PR55; 1.
DR   PRINTS; PR00600; PP2APR55.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS01024; PR55_1; 1.
DR   PROSITE; PS01025; PR55_2; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR   PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Repeat; WD repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    447       Serine/threonine-protein phosphatase 2A
FT                                55 kDa regulatory subunit B alpha
FT                                isoform.
FT                                /FTId=PRO_0000071417.
FT   REPEAT       26     65       WD 1.
FT   REPEAT       91    132       WD 2.
FT   REPEAT      175    213       WD 3.
FT   REPEAT      224    264       WD 4.
FT   REPEAT      283    321       WD 5.
FT   REPEAT      338    379       WD 6.
FT   REPEAT      414    446       WD 7.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
SQ   SEQUENCE   447 AA;  51692 MW;  F4D407FF7ADA4ED6 CRC64;
     MAGAGGGNDI QWCFSQVKGA VDDDVAEADI ISTVEFNHSG ELLATGDKGG RVVIFQQEQE
     NKIQSHSRGE YNVYSTFQSH EPEFDYLKSL EIEEKINKIR WLPQKNAAQF LLSTNDKTIK
     LWKISERDKR PEGYNLKEED GRYRDPTTVT TLRVPVFRPM DLMVEASPRR IFANAHTYHI
     NSISINSDYE TYLSADDLRI NLWHLEITDR SFNIVDIKPA NMEELTEVIT AAEFHPNSCN
     TFVYSSSKGT IRLCDMRASA LCDRHSKLFE EPEDPSNRSF FSEIISSISD VKFSHSGRYM
     MTRDYLSVKI WDLNMENRPV ETYQVHEYLR SKLCSLYEND CIFDKFECCW NGSDSVVMTG
     SYNNFFRMFD RNTKRDITLE ASRENNKPRT VLKPRKVCAS GKRKKDEISV DSLDFNKKIL
     HTAWHPKENI IAVATTNNLY IFQDKVN
//
ID   Q6P1F7_MOUSE            Unreviewed;       523 AA.
AC   Q6P1F7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   SubName: Full=Solute carrier family 1 (Neuronal/epithelial high affinity glutamate transporter, system Xag), member 1;
DE   SubName: Full=Solute carrier family 1 (Neuronal/epithelial high affinity glutamate transporter, system Xag), member 1, isoform CRA_a;
GN   Name=Slc1a1; ORFNames=mCG_13331;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC065099; AAH65099.1; -; mRNA.
DR   EMBL; CH466534; EDL41660.1; -; Genomic_DNA.
DR   IPI; IPI00420244; -.
DR   RefSeq; NP_033225.1; NM_009199.2.
DR   UniGene; Mm.246670; -.
DR   ProteinModelPortal; Q6P1F7; -.
DR   STRING; Q6P1F7; -.
DR   Ensembl; ENSMUST00000025875; ENSMUSP00000025875; ENSMUSG00000024935.
DR   GeneID; 20510; -.
DR   KEGG; mmu:20510; -.
DR   UCSC; uc008hcl.1; mouse.
DR   CTD; 20510; -.
DR   MGI; MGI:105083; Slc1a1.
DR   HOVERGEN; HBG000080; -.
DR   InParanoid; Q6P1F7; -.
DR   OMA; INPGRAG; -.
DR   PhylomeDB; Q6P1F7; -.
DR   NextBio; 298699; -.
DR   ArrayExpress; Q6P1F7; -.
DR   Bgee; Q6P1F7; -.
DR   Genevestigator; Q6P1F7; -.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0015501; F:glutamate:sodium symporter activity; IDA:MGI.
DR   GO; GO:0017153; F:sodium:dicarboxylate symporter activity; IEA:InterPro.
DR   InterPro; IPR001991; Na-dicarboxylate_symporter.
DR   InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR   PANTHER; PTHR11958; Na/diCO_symport; 1.
DR   Pfam; PF00375; SDF; 1.
DR   PRINTS; PR00173; EDTRNSPORT.
DR   PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
DR   PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   523 AA;  56694 MW;  46F35480465E5A82 CRC64;
     MGKPTSSGCD WRRFLRNHWL LLSTVAAVVL GIVLGVVVRG HSELSNLDKF YFAFPGEILM
     RMLKLVILPL IVSSMITGVA ALDSNVSGKI GLRAVVYYFS TTVIAVILGI VLVVSIKPGV
     TQKVNDINRT GKTPEVSTMD AMLDLIRNMF PENLVQACFQ QYKTKREEVK PVGDPGGNAT
     EVSVTTAMTT MSENKTKEYK IVGLYSDGIN VLGLIIFCLV FGLVIGKMGE KGQILVDFFN
     ALSDATMKIV QIIMCYMPIG ILFLIAGKII EVEDWEIFRK LGLYMATVLS GLAIHSLIVL
     PLLYFIVVRK NPFRFALGMA QALLTALMIS SSSATLPVTF RCAEEKNQVD KRITRFVLPV
     GATINMDGTA LYEAVAAVFI AQLNGLDLSI GQIVTISITA TAASIGAAGV PQAGLVTMVI
     VLSAVGLPAE DVTLIIAVDW LLDRFRTMVN VLGDAFGTGI VEKLSKKELE QMDVSSEVNI
     VNPFALEPTT LDNEDSDTKK SYVNGGFAVD KSDTISFTQT SQF
//
ID   KDM2B_MOUSE             Reviewed;        1309 AA.
AC   Q6P1G2; Q3V396; Q6PFD0; Q6ZPE8; Q9CSF7; Q9QZN6;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Lysine-specific demethylase 2B;
DE            EC=1.14.11.27;
DE   AltName: Full=F-box and leucine-rich repeat protein 10;
DE   AltName: Full=F-box protein FBL10;
DE   AltName: Full=F-box/LRR-repeat protein 10;
DE   AltName: Full=JmjC domain-containing histone demethylation protein 1B;
DE   AltName: Full=[Histone-H3]-lysine-36 demethylase 1B;
GN   Name=Kdm2b; Synonyms=Fbl10, Fbxl10, Jhdm1b, Kiaa3014;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-1309 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1011-1309 (ISOFORMS 1/2).
RX   MEDLINE=20003061; PubMed=10531037; DOI=10.1016/S0960-9822(00)80021-4;
RA   Winston J.T., Koepp D.M., Zhu C., Elledge S.J., Harper J.W.;
RT   "A family of mammalian F-box proteins.";
RL   Curr. Biol. 9:1180-1182(1999).
CC   -!- FUNCTION: Histone demethylase that demethylates 'Lys-4' and 'Lys-
CC       36' of histone H3, thereby playing a central role in histone code.
CC       Preferentially demethylates trimethylated H3 'Lys-4' and
CC       dimethylated H3 'Lys-36' residue while it has weak or no activity
CC       for mono- and tri-methylated H3 'Lys-36'. Preferentially binds the
CC       transcribed region of ribosomal RNA and represses the
CC       transcription of ribosomal RNA genes which inhibits cell growth
CC       and proliferation. May also serve as a substrate-recognition
CC       component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin
CC       ligase complex (By similarity).
CC   -!- CATALYTIC ACTIVITY: Protein N(6),N(6)-dimethyl-L-lysine + 2-
CC       oxoglutarate + O(2) = protein N(6)-methyl-L-lysine + succinate +
CC       formaldehyde + CO(2).
CC   -!- CATALYTIC ACTIVITY: Protein N(6)-methyl-L-lysine + 2-oxoglutarate
CC       + O(2) = protein L-lysine + succinate + formaldehyde + CO(2).
CC   -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity).
CC   -!- SUBUNIT: Directly interacts with SKP1A and CUL1 (By similarity).
CC   -!- INTERACTION:
CC       Q9CQJ4:Rnf2; NbExp=1; IntAct=EBI-1216214, EBI-927321;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q6P1G2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6P1G2-2; Sequence=VSP_011342, VSP_011343;
CC       Name=3;
CC         IsoId=Q6P1G2-3; Sequence=VSP_017477, VSP_017478;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q6P1G2-4; Sequence=VSP_019003;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The JmjC domain mediates demethylation activity. It is
CC       also required for repression of ribosomal RNA genes (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family.
CC   -!- SIMILARITY: Contains 1 CXXC-type zinc finger.
CC   -!- SIMILARITY: Contains 1 F-box domain.
CC   -!- SIMILARITY: Contains 1 JmjC domain.
CC   -!- SIMILARITY: Contains 4 LRR (leucine-rich) repeats.
CC   -!- SIMILARITY: Contains 1 PHD-type zinc finger.
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DR   EMBL; AK012952; BAB28568.2; -; mRNA.
DR   EMBL; AK043352; BAE20639.1; -; mRNA.
DR   EMBL; BC057622; AAH57622.1; -; mRNA.
DR   EMBL; BC065090; AAH65090.1; -; mRNA.
DR   EMBL; AK129479; BAC98289.1; -; mRNA.
DR   EMBL; AF176524; AAF09133.1; -; mRNA.
DR   IPI; IPI00420248; -.
DR   IPI; IPI00457832; -.
DR   IPI; IPI00853681; -.
DR   IPI; IPI00880832; -.
DR   RefSeq; NP_001003953.1; NM_001003953.1.
DR   RefSeq; NP_001005866.1; NM_001005866.1.
DR   RefSeq; NP_038938.1; NM_013910.2.
DR   UniGene; Mm.86406; -.
DR   ProteinModelPortal; Q6P1G2; -.
DR   SMR; Q6P1G2; 33-546, 579-628, 1039-1278.
DR   DIP; DIP-46351N; -.
DR   IntAct; Q6P1G2; 22.
DR   STRING; Q6P1G2; -.
DR   PhosphoSite; Q6P1G2; -.
DR   PRIDE; Q6P1G2; -.
DR   Ensembl; ENSMUST00000031435; ENSMUSP00000031435; ENSMUSG00000029475.
DR   Ensembl; ENSMUST00000046073; ENSMUSP00000038229; ENSMUSG00000029475.
DR   Ensembl; ENSMUST00000086200; ENSMUSP00000083376; ENSMUSG00000029475.
DR   GeneID; 30841; -.
DR   KEGG; mmu:30841; -.
DR   UCSC; uc008zmq.1; mouse.
DR   UCSC; uc008zmr.1; mouse.
DR   UCSC; uc008zmu.1; mouse.
DR   CTD; 30841; -.
DR   MGI; MGI:1354737; Kdm2b.
DR   eggNOG; roNOG07768; -.
DR   GeneTree; ENSGT00550000074396; -.
DR   HOGENOM; HBG444156; -.
DR   InParanoid; Q6P1G2; -.
DR   OMA; KNRAVGR; -.
DR   OrthoDB; EOG48WC1P; -.
DR   PhylomeDB; Q6P1G2; -.
DR   BRENDA; 1.14.11.27; 244.
DR   NextBio; 307252; -.
DR   Bgee; Q6P1G2; -.
DR   CleanEx; MM_FBXL10; -.
DR   Genevestigator; Q6P1G2; -.
DR   GermOnline; ENSMUSG00000029475; Mus musculus.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0051864; F:histone demethylase activity (H3-K36 specific); IEA:EC.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR001810; F-box_dom_cyclin-like.
DR   InterPro; IPR013129; TF_JmjC.
DR   InterPro; IPR003347; TF_JmjC_AAH.
DR   InterPro; IPR002857; Znf_CXXC.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00646; F-box; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF02008; zf-CXXC; 1.
DR   SMART; SM00256; FBOX; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS50181; FBOX; FALSE_NEG.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS51058; ZF_CXXC; 1.
DR   PROSITE; PS01359; ZF_PHD_1; FALSE_NEG.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromatin regulator; Coiled coil; Dioxygenase;
KW   Iron; Leucine-rich repeat; Metal-binding; Nucleus; Oxidoreductase;
KW   Phosphoprotein; Repeat; Repressor; RNA-binding; rRNA-binding;
KW   Transcription; Transcription regulation; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   CHAIN         1   1309       Lysine-specific demethylase 2B.
FT                                /FTId=PRO_0000119854.
FT   DOMAIN      147    315       JmjC.
FT   DOMAIN     1032   1078       F-box.
FT   REPEAT     1121   1144       LRR 1.
FT   REPEAT     1185   1208       LRR 2.
FT   REPEAT     1242   1266       LRR 3.
FT   REPEAT     1267   1309       LRR 4.
FT   ZN_FING     579    625       CXXC-type.
FT   ZN_FING     632    698       PHD-type.
FT   COILED      916    944       Potential.
FT   COMPBIAS    378    403       Glu-rich.
FT   METAL       211    211       Iron; catalytic (By similarity).
FT   METAL       213    213       Iron; catalytic (By similarity).
FT   METAL       283    283       Iron; catalytic (By similarity).
FT   BINDING     208    208       Substrate (By similarity).
FT   BINDING     228    228       Substrate (By similarity).
FT   MOD_RES     192    192       Phosphotyrosine (By similarity).
FT   MOD_RES     447    447       Phosphoserine (By similarity).
FT   MOD_RES     466    466       Phosphothreonine (By similarity).
FT   MOD_RES     470    470       Phosphoserine (By similarity).
FT   MOD_RES     948    948       Phosphoserine (By similarity).
FT   MOD_RES     952    952       Phosphoserine (By similarity).
FT   VAR_SEQ       1    533       Missing (in isoform 2).
FT                                /FTId=VSP_011342.
FT   VAR_SEQ       2   1196       Missing (in isoform 4).
FT                                /FTId=VSP_019003.
FT   VAR_SEQ     534    551       TLAITGVPVVSWPKKTAK -> MAMSVSAEDDDYESEPDQ
FT                                (in isoform 2).
FT                                /FTId=VSP_011343.
FT   VAR_SEQ     627    656       PVLPHTAVCLVCGEAGKEDTVEEEEGKFNL -> VSAQKAQ
FT                                AGLMQGLPAICPALGLLCGMGEV (in isoform 3).
FT                                /FTId=VSP_017477.
FT   VAR_SEQ     657   1309       Missing (in isoform 3).
FT                                /FTId=VSP_017478.
FT   CONFLICT    461    461       T -> M (in Ref. 3; BAC98289).
SQ   SEQUENCE   1309 AA;  149733 MW;  5BD203C3535C4D88 CRC64;
     MEAEKDSGRR LRAIDRQRYD ENEDLSDVEE IVSVRGFSLE EKLRSQLYQG DFVHAMEGKD
     FNYEYVQREA LRVPLVFRDK DGLGIKMPDP DFTVRDVKLL VGSRRLVDVM DVNTQKGTEM
     SMSQFVRYYE TPEAQRDKLY NVISLEFSHT KLEHLVKRPT VVDLVDWVDN MWPQHLKEKQ
     TEATNALAEM KYPKVKKYCL MSVKGCFTDF HIDFGGTSVW YHVFRGGKIF WLIPPTLHNL
     ALYEEWVLSG KQSDIFLGDR VERCQRIELK QGYTFFIPSG WIHAVYTPVD SLVFGGNILH
     SFNVPMQLRI YEIEDRTRVQ PKFRYPFYYE MCWYVLERYV YCVTQRSYLT QEYQRELMLI
     DAPRKTSVDG FSSDSWLDME EESCEQQPQE EEEEEEDKEE EGDGADKTPK PPTDDPTSPT
     STPPEDQDST GKKPKAPAIR FLKRTLSNES EESVKSTSMP TDDPKTPTGS PATEVSTKWT
     HLTEFELKGL KALVEKLESL PENKKCVPEG IEDPQALLEG VKNVLKEHVD DDPTLAITGV
     PVVSWPKKTA KNRVVGRPKG KLGPASAVKL AANRTTAGAR RRRTRCRKCE ACLRTECGEC
     HFCKDMKKFG GPGRMKQSCI MRQCIAPVLP HTAVCLVCGE AGKEDTVEEE EGKFNLMLME
     CSICNEIIHP GCLKIKESEG VVNDELPNCW ECPKCNHAGK TGKQKRGPGF KYASNLPGSL
     LKEQKMNRDN KEGQEPAKRR SECEEAPRRR SDEHPKKVPA DGILRRKSDD VHLRRKRKYE
     KPQELSGRKR ASSLQTSPGS SSHLSPRPPL GSSLSPWWRS SLTYFQQQLK PGKEDKLFRK
     KRRSWKNAED RLSLANKPLR RFKQEPEDDL PEAPPKTRES DQSRSSSPTA GPSTEGAEGP
     EEKKKVKMRR KRRLVNKELS KELSKELNHE IQKTESTLAH ESQQPIKSEP ESENDEPKRP
     LSHCERPHRF SKGLNGTPRE LRHSLGPGLR SPPRVMSRPP PSASPPKCIQ MERHVIRPPP
     ISPPPDSLPL DDGAAHVMHR EVWMAVFSYL SHRDLCVCMR VCRTWNRWCC DKRLWTRIDL
     NRCKSITPLM LSGIIRRQPV SLDLSWTNIS KKQLSWLINR LPGLRDLVLS GCSWIAVSAL
     CSSSCPLLRT LDVQWVEGLK DAQMRDLLSP PTDNRPGQMD NRSKLRNIVE LRLAGLDITD
     VSLRLIIRHM PLLSKLQLSY CNHINDQSIN LLTAVGTTTR DSLTEVNLSD CNKVTDLCLS
     FFKRCGNICH IDLRYCKQVT KEGCEQFIAE MSVSVQFGQV EEKLLQKLS
//
ID   PSD2_MOUSE              Reviewed;         770 AA.
AC   Q6P1I6; Q6NZP0; Q6PHQ7; Q8BHR9; Q9D3B8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=PH and SEC7 domain-containing protein 2;
DE   AltName: Full=Pleckstrin homology and SEC7 domain-containing protein 2;
GN   Name=Psd2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 373-770 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6P1I6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6P1I6-2; Sequence=VSP_033640;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q6P1I6-3; Sequence=VSP_033639;
CC   -!- SIMILARITY: Belongs to the PSD family.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 SEC7 domain.
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DR   EMBL; AK018116; BAB31078.2; -; mRNA.
DR   EMBL; AK045529; BAC32407.1; -; mRNA.
DR   EMBL; BC056437; AAH56437.1; -; mRNA.
DR   EMBL; BC062930; AAH62930.1; -; mRNA.
DR   EMBL; BC065053; AAH65053.1; -; mRNA.
DR   EMBL; BC065055; AAH65055.1; -; mRNA.
DR   EMBL; BC066026; AAH66026.1; -; mRNA.
DR   EMBL; BC066036; AAH66036.1; -; mRNA.
DR   IPI; IPI00221945; -.
DR   IPI; IPI00875813; -.
DR   IPI; IPI00895068; -.
DR   RefSeq; NP_082983.3; NM_028707.3.
DR   UniGene; Mm.196944; -.
DR   HSSP; Q15438; 1BC9.
DR   ProteinModelPortal; Q6P1I6; -.
DR   SMR; Q6P1I6; 309-723.
DR   PhosphoSite; Q6P1I6; -.
DR   Ensembl; ENSMUST00000025205; ENSMUSP00000025205; ENSMUSG00000024347.
DR   Ensembl; ENSMUST00000115716; ENSMUSP00000111381; ENSMUSG00000024347.
DR   GeneID; 74002; -.
DR   KEGG; mmu:74002; -.
DR   UCSC; uc008ena.1; mouse.
DR   CTD; 74002; -.
DR   MGI; MGI:1921252; Psd2.
DR   eggNOG; roNOG05955; -.
DR   GeneTree; ENSGT00570000079011; -.
DR   HOVERGEN; HBG108298; -.
DR   OMA; ARDSPEP; -.
DR   OrthoDB; EOG42RD7G; -.
DR   PhylomeDB; Q6P1I6; -.
DR   NextBio; 339498; -.
DR   ArrayExpress; Q6P1I6; -.
DR   Bgee; Q6P1I6; -.
DR   Genevestigator; Q6P1I6; -.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000904; Sec7.
DR   InterPro; IPR023394; SEC7_alpha_orthog.
DR   InterPro; IPR001605; Spectrin_PH.
DR   Gene3D; G3DSA:1.10.1000.11; G3DSA:1.10.1000.11; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF01369; Sec7; 1.
DR   PRINTS; PR00683; SPECTRINPH.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00222; Sec7; 1.
DR   SUPFAM; SSF48425; Sec7; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50190; SEC7; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    770       PH and SEC7 domain-containing protein 2.
FT                                /FTId=PRO_0000334163.
FT   TRANSMEM    619    636       Helical; (Potential).
FT   DOMAIN      256    459       SEC7.
FT   DOMAIN      509    622       PH.
FT   COILED      650    677       Potential.
FT   VAR_SEQ     420    420       H -> HV (in isoform 3).
FT                                /FTId=VSP_033639.
FT   VAR_SEQ     526    529       GKRT -> A (in isoform 2).
FT                                /FTId=VSP_033640.
SQ   SEQUENCE   770 AA;  84299 MW;  A64A9D0EA9F783F0 CRC64;
     MDEEKLPCEL HKEGSATQED HGLEPEEEPG LQNGTAASEG LSSHISGPGG EKTLEGTMEP
     VRGPDVALPG LNLSLTNGLA LGQDGNILED SIEFKTWRSG PAEEEDVPGS PCPDAGDPQL
     GLDCPGEPDV RDGFSATFEK ILESELLRGT QYSSLDSLDV LSLTDESDSC VSFEAPLTPL
     IQQRARDSPE AGAGLGNGDM GPEGDLGATG GCDGELGSPL RRSISSSRSE NVLSHLSLTS
     VPNGFHEDGP GGSGGDDEDD EDTDKLLNSA SDTSLKDGLS DSDSELSSSE GLEPGSTDPL
     ANGCQGVSEA ARRLARRLYH LEGFQRCDVA RQLGKNNEFS RLVAGEYLSF FDFSGLTLDR
     ALRTFLKAFP LMGETQERER VLTHFSRRYC QCNPDDSTSE DGIHTLTCAL MLLNTDLHGH
     NIGKKMSCQQ FIANLDQLND GQDFAKDLLK TLYNSIKNEK LEWAIDEDEL RKSLSELVDD
     KFGTGTKKVT RILDGGNPFL DVPQALNATT YKHGVLTRKT HADMDGKRTP RGRRGWKKFY
     AVLKGTILYL QKDEYRLDKA LSEGDLKNAI RVHHALATRA SDYSKKSNVL KLKTADWRVF
     LFQAPSKEEM LSWILRINLV AAIFSAPAFP AAVSSMKKFC RPLLPSCTTR LCQEEQLRSH
     ENKLRQVTAE LAEHRCHPLE RGLKSKEAEE YRLKEHYLTF EKSRYETYIH LLAVKIKVGS
     DDLERIEARL ATIEGDDPAL RKTHSSPALS LGHGPVTGSK ATKDTSASDT
//
ID   INP4B_MOUSE             Reviewed;         924 AA.
AC   Q6P1Y8;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Type II inositol-3,4-bisphosphate 4-phosphatase;
DE            EC=3.1.3.66;
DE   AltName: Full=Inositol polyphosphate 4-phosphatase type II;
GN   Name=Inpp4b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of
CC       phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4-
CC       trisphosphate and inositol 1,4-bisphosphate (By similarity).
CC   -!- CATALYTIC ACTIVITY: 1-phosphatidyl-myo-inositol 3,4-bisphosphate +
CC       H(2)O = 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate.
CC   -!- ENZYME REGULATION: Strongly inhibited by inositol hexakisphosphate
CC       (By similarity).
CC   -!- PATHWAY: Signal transduction; phosphatidylinositol signaling
CC       pathway.
CC   -!- SIMILARITY: Belongs to the inositol-3,4-bisphosphate 4-phosphatase
CC       family.
CC   -!- SIMILARITY: Contains 1 C2 domain.
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DR   EMBL; BC064813; AAH64813.1; -; mRNA.
DR   IPI; IPI00875164; -.
DR   RefSeq; NP_001019788.1; NM_001024617.2.
DR   UniGene; Mm.324468; -.
DR   ProteinModelPortal; Q6P1Y8; -.
DR   SMR; Q6P1Y8; 23-166.
DR   STRING; Q6P1Y8; -.
DR   PhosphoSite; Q6P1Y8; -.
DR   PRIDE; Q6P1Y8; -.
DR   Ensembl; ENSMUST00000042529; ENSMUSP00000044466; ENSMUSG00000037940.
DR   Ensembl; ENSMUST00000109851; ENSMUSP00000105477; ENSMUSG00000037940.
DR   GeneID; 234515; -.
DR   KEGG; mmu:234515; -.
DR   UCSC; uc009mjh.1; mouse.
DR   CTD; 234515; -.
DR   MGI; MGI:2158925; Inpp4b.
DR   eggNOG; roNOG06016; -.
DR   GeneTree; ENSGT00390000002033; -.
DR   HOVERGEN; HBG081796; -.
DR   PhylomeDB; Q6P1Y8; -.
DR   BRENDA; 3.1.3.66; 244.
DR   NextBio; 382201; -.
DR   ArrayExpress; Q6P1Y8; -.
DR   Bgee; Q6P1Y8; -.
DR   CleanEx; MM_INPP4B; -.
DR   Genevestigator; Q6P1Y8; -.
DR   GermOnline; ENSMUSG00000037940; Mus musculus.
DR   GO; GO:0016316; F:phosphatidylinositol-3,4-bisphosphate 4-phosphatase activity; IEA:EC.
DR   GO; GO:0034597; F:phosphatidylinositol-4,5-bisphosphate 4-phosphatase activity; IEA:EC.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   SMART; SM00239; C2; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   PROSITE; PS50004; C2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Hydrolase; Phosphoprotein.
FT   CHAIN         1    924       Type II inositol-3,4-bisphosphate 4-
FT                                phosphatase.
FT                                /FTId=PRO_0000190237.
FT   DOMAIN       25    132       C2.
FT   MOD_RES     470    470       Phosphoserine.
SQ   SEQUENCE   924 AA;  104531 MW;  09DF35368F4C1695 CRC64;
     MEIKEEGTSE EGQHFLPAAQ ANDPEDIQFT SIQKIPNEPQ LEFILACRDL VAPVSDRKLN
     TVVQISVIHP VEQTLTRYSS TEIVEGTKDP LFLTGVTFPP DYPIYEETRI KLTVYDVKDK
     SHDTRSFLGC ASFKVGELLK SKEQLLSLSL RTSDGGKVVG TIEVSLVKMG EIEDGDTDHI
     TTDVQGQKCA LMYESTAPES LSGKENLPFM NAVLRNPVCK LYRFPTSDNK WMRIREQMSE
     SILSFHIPKE LISLHIKEDL CRNQELKELG DLSPHWDNLR KNVLSHCDQM VTMYQDILTE
     LSKETGSSFK SSSSKGEKTL EFVPVNLHLQ RMQVHSPHLK DALYDVITVG APAAHFQGFK
     NGGLRKLLHR FETERRNTGY QFIYYSPENT AKAKEVLSSI NQLQPLIATH ADLLLTSASQ
     RSPDSLKSSL KLLSEKTELF VHAFKDQLVR SALLALYTAR PGGILKKPPS PNVSTEEKST
     QHDTPQLRRQ DSIPHHSDYD EEEWDRVWAN VGKSLNCIIA KVDKLIERDS HNEEGAGGSS
     SKDGEADHTL EDSITSHPRE DWYEQLHPLI LTLKECMGEV VNRAKQSLTF VLLQELAYSL
     PQCLMLTLRR DIVFSQALAG LVCGFIIKLH TSLHDPGFLQ QLHTVGLIVQ YEGLLSTYSD
     EIGMLEDMAV GISDLRKVAF KITEATSNDV LPVLTGRREH YVVEVKLPAT VFESLPLQIK
     EGQLLHVYPV LFNVGINEQQ TLAERFGDVS LQESINQENF ELVQEYYSIF MEKMPPDYIS
     HFQEQTDLKG LLDNLHQNIQ AKKRKNVEIM WLAATICRKL NGIRFTCCKS AKDRTSMSVT
     LEQCSILRDE HQLHKDFFIR ALDCMRSRQT QGALNESDDP ETGCLTDNKP TSRHFYPVAL
     LLVSSHLLVV WLILSLALLL AKYQ
//
ID   Q6P1Y9_MOUSE            Unreviewed;       901 AA.
AC   Q6P1Y9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   SubName: Full=Exocyst complex component 1;
GN   Name=Exoc1; Synonyms=Sec3l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC064811; AAH64811.1; -; mRNA.
DR   IPI; IPI00153813; -.
DR   RefSeq; NP_081546.1; NM_027270.1.
DR   UniGene; Mm.480388; -.
DR   STRING; Q6P1Y9; -.
DR   PRIDE; Q6P1Y9; -.
DR   Ensembl; ENSMUST00000113493; ENSMUSP00000109121; ENSMUSG00000036435.
DR   GeneID; 69940; -.
DR   KEGG; mmu:69940; -.
DR   UCSC; uc008xuz.1; mouse.
DR   CTD; 69940; -.
DR   MGI; MGI:2445020; Exoc1.
DR   GeneTree; ENSGT00530000063494; -.
DR   HOGENOM; HBG387773; -.
DR   HOVERGEN; HBG056730; -.
DR   InParanoid; Q6P1Y9; -.
DR   OMA; GHDMLLA; -.
DR   NextBio; 330647; -.
DR   ArrayExpress; Q6P1Y9; -.
DR   Bgee; Q6P1Y9; -.
DR   Genevestigator; Q6P1Y9; -.
DR   InterPro; IPR019160; Exocyst_Exoc1.
DR   Pfam; PF09763; Sec3; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   901 AA;  102686 MW;  C53B7048A45BFD4F CRC64;
     MTAIKHALQR DIFTPNDERL LSIVNVCKAG KKKKNCFLCA TVTTERPVQV KVVKVKKSDK
     GDFYKRQIAW ALRDLAVVDA KDAIKENPEF DLHFEKVYKW VASSTAEKNA FISCIWKLNQ
     RYLRKKIDFV NVSSQLLEEL PKVTEESVPS GENQSVAGGD EEAVDEYQEL NAREEQDIEI
     MMEGCECAIS NAEAFAEKLS RELQVLDGAN IQSIMASEKQ VNTLMQLLDE ALTEVDQIEL
     KLSSYEEMLQ SVKEQMDQIS ESNHLIHLSN TNNVKLLSEI EFLVNHMDLA KGHIKALQEG
     DLVSSRGIEA CTNAADALLQ CMNVALRPGH DMLLAVKQQQ QRFSDLREHF ARRLASHLNN
     VFVQQGHDQS STLAQHSVEL TLPNHHPFHR DLLRYAKLME WLKSTDYGKY EGLTKNYMDY
     LSRLYEREIK DFFEVAKMKM TGTSKESKKF ATLPRKESAV KQETESLHGS SGKLTGSTSS
     LNKLSVQSSG SRRSQSSSLL DMGNMSASDL DVADRTKFDK IFEQVLSELE PLCLAEQDFI
     SKFFKLQQHQ NMSASMTEAE DLDGGSLLRQ HSSGTLLPVS SEKDMIRQMM IKIFRCIEPE
     LNNLIALGDK VDSFNSLYML VKMSHHVWTA QNVDPASFLS TTLGNVLVTV KRNFDKCISN
     QIRQMEEVKI SKKSKVGILP FVAEFEEFAG LAESIFKNAE RRGDLDKAYT KLIRGVFINV
     EKVANESQKT PRDVVMMENF HHIFATLSRL KISCLEAEKK EAKQKYTDHL QSYVIYSLGQ
     PLEKLNHFFE GVEARVAQGI REEEVSYQLA FNKQELRKVI KEYPGKEVKK GLDNLYKKVD
     KHLCEEENLL QVVWHSMQDE FIRQYKHFEG LIARCYPGSG VTMEFTIQDI LDYCSSIAQS
     H
//
ID   Q6P247_MOUSE            Unreviewed;       235 AA.
AC   Q6P247;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-FEB-2011, entry version 34.
DE   SubName: Full=Fmnl2 protein;
DE   Flags: Fragment;
GN   Name=Fmnl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CD1; TISSUE=Neural Stem Cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC064731; AAH64731.1; -; mRNA.
DR   IPI; IPI00345373; -.
DR   UniGene; Mm.394427; -.
DR   ProteinModelPortal; Q6P247; -.
DR   STRING; Q6P247; -.
DR   Ensembl; ENSMUST00000090952; ENSMUSP00000088472; ENSMUSG00000036053.
DR   MGI; MGI:1918659; Fmnl2.
DR   GeneTree; ENSGT00570000078740; -.
DR   HOGENOM; HBG445684; -.
DR   HOVERGEN; HBG031551; -.
DR   InParanoid; Q6P247; -.
DR   ArrayExpress; Q6P247; -.
DR   Bgee; Q6P247; -.
DR   Genevestigator; Q6P247; -.
DR   InterPro; IPR014767; Diaphanous_autoregulatory.
DR   InterPro; IPR015425; FH2_actin-bd.
DR   Pfam; PF02181; FH2; 1.
DR   SUPFAM; SSF101447; FH2_actin_bd; 1.
DR   PROSITE; PS51231; DAD; 1.
DR   PROSITE; PS51444; FH2; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   235 AA;  27806 MW;  410D33F01B2BAB0A CRC64;
     DRKQTLLHYI SNVVKEKYQQ VTLFYNELHY VEKAAAVSLE NVLLDVKELQ RGMDLTKREY
     TMHDHNTLLK EFLLHNEGKL KKLQEDAKIA QDAFDDVVKY FGENPKTTPP SVFFPVFVRF
     VKAYKQAEEE NELRKKQEQA LMEKLLEQEA LMEQQDAKSP SHKSKRQQQE LIAELRRRQV
     KDNRHVYEGK DGAIEDIITD LRNQPYRRAD AVRRSVRRRF DDQNLRSVNG AEITM
//
ID   NSD3_MOUSE              Reviewed;        1439 AA.
AC   Q6P2L6; Q3TDS4; Q3U0L8; Q3V131; Q8BJT3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Histone-lysine N-methyltransferase NSD3;
DE            EC=2.1.1.43;
DE   AltName: Full=Nuclear SET domain-containing protein 3;
DE   AltName: Full=Wolf-Hirschhorn syndrome candidate 1-like protein 1 homolog;
DE            Short=WHSC1-like protein 1;
GN   Name=Whsc1l1; Synonyms=Nsd3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Aorta, Spleen, Testis, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 899-914, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: Histone methyltransferase. Preferentially methylates
CC       'Lys-4' and 'Lys-27' of histone H3. H3 'Lys-4' methylation
CC       represents a specific tag for epigenetic transcriptional
CC       activation, while 'Lys-27' is a mark for transcriptional
CC       repression (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Chromosome (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q6P2L6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6P2L6-2; Sequence=VSP_021432, VSP_021435, VSP_021436;
CC       Name=3;
CC         IsoId=Q6P2L6-3; Sequence=VSP_021431, VSP_021437, VSP_021438;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q6P2L6-4; Sequence=VSP_021432, VSP_021433, VSP_021434;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the histone-lysine methyltransferase
CC       family. SET2 subfamily.
CC   -!- SIMILARITY: Contains 1 AWS domain.
CC   -!- SIMILARITY: Contains 4 PHD-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 post-SET domain.
CC   -!- SIMILARITY: Contains 2 PWWP domains.
CC   -!- SIMILARITY: Contains 1 SET domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK079952; BAC37792.1; -; mRNA.
DR   EMBL; AK132725; BAE21322.1; -; mRNA.
DR   EMBL; AK156746; BAE33834.1; -; mRNA.
DR   EMBL; AK170040; BAE41526.1; -; mRNA.
DR   EMBL; AC156990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC162367; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC064447; AAH64447.1; -; mRNA.
DR   IPI; IPI00353681; -.
DR   IPI; IPI00625887; -.
DR   IPI; IPI00660619; -.
DR   IPI; IPI00663331; -.
DR   RefSeq; NP_001001735.1; NM_001001735.1.
DR   UniGene; Mm.217337; -.
DR   ProteinModelPortal; Q6P2L6; -.
DR   SMR; Q6P2L6; 263-389, 698-802, 919-1060, 1067-1289, 1322-1365.
DR   STRING; Q6P2L6; -.
DR   PhosphoSite; Q6P2L6; -.
DR   PRIDE; Q6P2L6; -.
DR   Ensembl; ENSMUST00000033974; ENSMUSP00000033974; ENSMUSG00000054823.
DR   Ensembl; ENSMUST00000084026; ENSMUSP00000081040; ENSMUSG00000054823.
DR   GeneID; 234135; -.
DR   KEGG; mmu:234135; -.
DR   UCSC; uc009lgk.1; mouse.
DR   UCSC; uc009lgm.1; mouse.
DR   UCSC; uc009lgn.1; mouse.
DR   UCSC; uc009lgp.1; mouse.
DR   CTD; 234135; -.
DR   MGI; MGI:2142581; Whsc1l1.
DR   eggNOG; roNOG07740; -.
DR   GeneTree; ENSGT00600000084164; -.
DR   HOGENOM; HBG443969; -.
DR   HOVERGEN; HBG079979; -.
DR   InParanoid; Q6P2L6; -.
DR   OMA; FSPTDYY; -.
DR   BRENDA; 2.1.1.43; 244.
DR   NextBio; 382034; -.
DR   ArrayExpress; Q6P2L6; -.
DR   Bgee; Q6P2L6; -.
DR   Genevestigator; Q6P2L6; -.
DR   GermOnline; ENSMUSG00000054823; Mus musculus.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR006560; AWS.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR000313; PWWP.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 3.
DR   Pfam; PF00855; PWWP; 2.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00570; AWS; 1.
DR   SMART; SM00249; PHD; 5.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00293; PWWP; 2.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 3.
DR   PROSITE; PS51215; AWS; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50812; PWWP; 2.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Chromatin regulator; Chromosome;
KW   Coiled coil; Direct protein sequencing; Metal-binding;
KW   Methyltransferase; Nucleus; Repeat; Transcription;
KW   Transcription regulation; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1   1439       Histone-lysine N-methyltransferase NSD3.
FT                                /FTId=PRO_0000259522.
FT   DOMAIN      270    333       PWWP 1.
FT   DOMAIN      960   1025       PWWP 2.
FT   DOMAIN     1096   1146       AWS.
FT   DOMAIN     1147   1269       SET.
FT   DOMAIN     1272   1288       Post-SET.
FT   ZN_FING     701    748       PHD-type 1.
FT   ZN_FING     749    805       PHD-type 2.
FT   ZN_FING     862    955       PHD-type 3.
FT   ZN_FING    1323   1370       PHD-type 4; atypical.
FT   COILED     1036   1065       Potential.
FT   MOD_RES     790    790       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1    941       Missing (in isoform 3).
FT                                /FTId=VSP_021431.
FT   VAR_SEQ     135    135       P -> PLPPPPPPPPP (in isoform 2 and
FT                                isoform 4).
FT                                /FTId=VSP_021432.
FT   VAR_SEQ     603    611       QVETAPQAS -> QVGFLHVES (in isoform 4).
FT                                /FTId=VSP_021433.
FT   VAR_SEQ     612   1439       Missing (in isoform 4).
FT                                /FTId=VSP_021434.
FT   VAR_SEQ     620    645       ASEISDSCKPLKKRSRASTDVETASC -> SADRGAQGSVR
FT                                FSDSSVSAAKEETVD (in isoform 2).
FT                                /FTId=VSP_021435.
FT   VAR_SEQ     646   1439       Missing (in isoform 2).
FT                                /FTId=VSP_021436.
FT   VAR_SEQ     973    975       Missing (in isoform 3).
FT                                /FTId=VSP_021437.
FT   VAR_SEQ    1199   1209       Missing (in isoform 3).
FT                                /FTId=VSP_021438.
FT   CONFLICT    122    122       H -> R (in Ref. 1; BAE33834).
FT   CONFLICT    950    950       N -> K (in Ref. 1; BAE21322).
FT   CONFLICT   1149   1149       D -> N (in Ref. 1; BAE21322).
SQ   SEQUENCE   1439 AA;  161002 MW;  917C7ADCD1248525 CRC64;
     MDFSFSFMQG IMGNTIQQPP QLIDSANIRQ EDAFDNHSDI VEDGGPTPFE ATLQQGFQYP
     PTTEDLPPLT NGYPPSISLY ETQTKYPPYN QYPNGSANGF GAVRNFSPTD YYHSEIPNTR
     PHEILEKPSP PQPPPPPSVP QTVIPKKTGS PEIKLKITKT IQNGRELFES SLCGDLLNEV
     QASEHTKSKH ESRKEKRKKS NRHESSRSEE RRSHKIPKLE PEGQNRPNER VDTAPEKPRE
     EPVLKEAIPV QPILSSVPTT ETSTGVKFQV GDLVWSKVGT YPWWPCMVSS DPQLEVHSKI
     NTRGAREYHV QFFSNQPERA WVHEKRVREY KGHEQYEELL AEAAKQASNH SEKQKIRKPR
     PQRERAQWDI GIAHAEKALK MTREERVEQY TFIYIDKQPE EASSQAKKNV TSKTEVKKPR
     RPRSVLNSQP EQTNAGEVAS SQSSTDLRRQ SQRRHTSLEE EEPPPVKIAW KTAAARKSLP
     ASITMHKGSL DLQKCNMSPV VKIEQVFALQ NATGDGKFID QFVYSTKGIG NKTEISVRGQ
     DRLIISSPSQ RSEKPAQSAS SPEATSGSAG PVEKKQQRRS IRTRSESEKS AEVVPKKKIK
     KEQVETAPQA SLKTGLQKGA SEISDSCKPL KKRSRASTDV ETASCTYRDT SDSDSRGLSD
     GQVGFGKQVD SPSATADADA SDAQSVDSSL SRRGVGTSKK DTVCQVCEKA GDCLVACEGE
     CCRHFHVECL GLTAVPEGHF TCEECETGQH PCFSCKVSGK DVKRCSVSVC GKFYHEACVR
     KFPTAIFESK GFRCPQHCCS SCSMEKDIHK ASKGRMMRCL RCPVAYHVGD ACVAAGSVSV
     SSHILICSNH SKRSSQSAAI NVGFCFVCAR GLIVQDHSDP MFSSYAYKSH YLLSESNRAE
     LMKLPMIPSS SASKKRCEKG GRLLCCESCP ASFHPECLSI DMPEGCWNCN DCKAGKKLHY
     KQIVWVKLGN YRQVLWWPAE ICSPRSVPLN IQGLKHDLGD FPVFFFGSHD YYWVHQGRVF
     PYVEGDKHFA EGQTSINKTF KKALEEAAKR FQELKAQRES KEALEMERTS RKPPPYKHIK
     ANKVIGKVQV QVADLSEIPR CNCKPGDENP CGLESQCLNR MSQYECHPQV CPAGDRCQNQ
     CFTKRLYPDA EVIKTERRGW GLRTKRSIKK GEFVNEYVGE LIDEEECRLR IKRAHENSVT
     NFYMLTVTKD RIIDAGPKGN YSRFMNHSCN PNCETQKWTV NGDVRVGLFA LCDIPAGMEL
     TFNYNLDCLG NGRTVCHCGA DNCSGFLGVR PKSACTSAVD EKTKNAKLKK RRKVKAEAKP
     IHEDYCFQCG DGGELVMCDK KDCPKAYHLL CLNLTQPPHG KWECPWHRCD ECGSVAVSFC
     EFCPHSFCKA HGKGALVPSA LEGRLCCSSH DPASPVSPEY WSKIRCKWES QDSGEEVKE
//
ID   CASC4_MOUSE             Reviewed;         435 AA.
AC   Q6P2L7; A2AR57; Q6RZW5; Q6RZW6; Q8C4Z2;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Protein CASC4;
DE   AltName: Full=Cancer susceptibility candidate gene 4 protein homolog;
GN   Name=Casc4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J;
RA   Zhou G., Liu X., Li H.;
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-176 (ISOFORMS 1/2/3).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane
CC       protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6P2L7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6P2L7-2; Sequence=VSP_026263;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q6P2L7-3; Sequence=VSP_026263, VSP_026264, VSP_026265;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the GOLM1/CASC4 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAR26705.1; Type=Frameshift; Positions=Several;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY484583; AAR26704.1; -; mRNA.
DR   EMBL; AY484585; AAR26705.1; ALT_FRAME; mRNA.
DR   EMBL; AL845286; CAM20995.1; -; Genomic_DNA.
DR   EMBL; AL845286; CAM20996.1; -; Genomic_DNA.
DR   EMBL; AL845286; CAM20997.1; -; Genomic_DNA.
DR   EMBL; BC064446; AAH64446.1; -; mRNA.
DR   EMBL; AK080364; BAC37891.1; -; mRNA.
DR   IPI; IPI00311324; -.
DR   IPI; IPI00453632; -.
DR   IPI; IPI00848768; -.
DR   RefSeq; NP_796028.2; NM_177054.5.
DR   RefSeq; NP_950239.2; NM_199038.3.
DR   UniGene; Mm.292109; -.
DR   ProteinModelPortal; Q6P2L7; -.
DR   PhosphoSite; Q6P2L7; -.
DR   PRIDE; Q6P2L7; -.
DR   Ensembl; ENSMUST00000078752; ENSMUSP00000077811; ENSMUSG00000060227.
DR   Ensembl; ENSMUST00000089912; ENSMUSP00000087357; ENSMUSG00000060227.
DR   GeneID; 319996; -.
DR   KEGG; mmu:319996; -.
DR   UCSC; uc008lzr.1; mouse.
DR   CTD; 319996; -.
DR   MGI; MGI:2443129; Casc4.
DR   eggNOG; roNOG06062; -.
DR   GeneTree; ENSGT00530000063675; -.
DR   HOGENOM; HBG446781; -.
DR   HOVERGEN; HBG057061; -.
DR   InParanoid; Q6P2L7; -.
DR   OMA; IPHGKEQ; -.
DR   OrthoDB; EOG4FR0RP; -.
DR   PhylomeDB; Q6P2L7; -.
DR   NextBio; 395807; -.
DR   ArrayExpress; Q6P2L7; -.
DR   Bgee; Q6P2L7; -.
DR   CleanEx; MM_CASC4; -.
DR   Genevestigator; Q6P2L7; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Membrane; Phosphoprotein;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN         1    435       Protein CASC4.
FT                                /FTId=PRO_0000291844.
FT   TOPO_DOM      1     14       Cytoplasmic (Potential).
FT   TRANSMEM     15     35       Helical; Signal-anchor for type II
FT                                membrane protein; (Potential).
FT   TOPO_DOM     36    435       Lumenal (Potential).
FT   COILED       35    194       Potential.
FT   MOD_RES     365    365       Phosphoserine.
FT   VAR_SEQ     267    299       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_026263.
FT   VAR_SEQ     357    357       S -> N (in isoform 3).
FT                                /FTId=VSP_026264.
FT   VAR_SEQ     358    413       Missing (in isoform 3).
FT                                /FTId=VSP_026265.
SQ   SEQUENCE   435 AA;  49409 MW;  C62F71B6B2FA7598 CRC64;
     MVGFGANRRA GRLPSFVLVV LLVVIVVLAF NYWSISSRHV LLQEEVAELQ GQVQRTEVAR
     GRLEKRNSDL LLLVDTHKKQ IDQKEADYGR LSSRLQAKEG LGKRCEDDKV KLQNNISYQM
     ADIHHLKEQL AELRQEFLRQ EDQLQDYRKN NTYLVKRLEY ESFQCGQQIK ELRAQHEENI
     KKLADQFLQE QKETHKIQSN DGKELGRNDH GAPKNIPNVP ENDANKNEDP SSNHLPHGKE
     QLKRVGDAGM PGVEENDLAK VDELPAALKK PPVLASQHES HQTISHLPTG QPLSPNMAPG
     SHLNQNENPS TSKQNPSNPL QHIIPGPNLD REPRIQTDTL KQATRDRAND FHKLKQSRFF
     DENESPVDPQ HGSKLADYNG DDGNVGEYEA DKQAELAYNE EEDGDGGEED VQDDEERELQ
     MDPADYGKQR FSDVL
//
ID   Z280C_MOUSE             Reviewed;         742 AA.
AC   Q6P3Y5; B1AU28; B1AU29; Q6ZPM2; Q8K145;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Zinc finger protein 280C;
DE   AltName: Full=Suppressor of hairy wing homolog 3;
GN   Name=Znf280c; Synonyms=Kiaa1584, Suhw3, Zfp280c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May function as a transcription factor.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6P3Y5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6P3Y5-2; Sequence=VSP_017620, VSP_017621;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q6P3Y5-3; Sequence=VSP_017619;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 5 C2H2-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98209.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK129399; BAC98209.1; ALT_INIT; mRNA.
DR   EMBL; AK141491; BAE24700.1; -; mRNA.
DR   EMBL; AL669901; CAM22224.1; -; Genomic_DNA.
DR   EMBL; AL669901; CAM22225.1; -; Genomic_DNA.
DR   EMBL; BC028839; AAH28839.1; -; mRNA.
DR   EMBL; BC051397; AAH51397.1; -; mRNA.
DR   EMBL; BC063775; AAH63775.1; -; mRNA.
DR   IPI; IPI00169658; -.
DR   IPI; IPI00469164; -.
DR   IPI; IPI00622268; -.
DR   RefSeq; NP_001160120.1; NM_001166648.1.
DR   RefSeq; NP_001160121.1; NM_001166649.1.
DR   RefSeq; NP_001160122.1; NM_001166650.1.
DR   RefSeq; NP_705760.2; NM_153532.3.
DR   UniGene; Mm.293819; -.
DR   ProteinModelPortal; Q6P3Y5; -.
DR   SMR; Q6P3Y5; 231-504, 599-624, 636-669.
DR   PhosphoSite; Q6P3Y5; -.
DR   PRIDE; Q6P3Y5; -.
DR   Ensembl; ENSMUST00000076635; ENSMUSP00000075933; ENSMUSG00000036916.
DR   Ensembl; ENSMUST00000088898; ENSMUSP00000086288; ENSMUSG00000036916.
DR   Ensembl; ENSMUST00000114940; ENSMUSP00000110590; ENSMUSG00000036916.
DR   GeneID; 208968; -.
DR   KEGG; mmu:208968; -.
DR   UCSC; uc009tcj.1; mouse.
DR   UCSC; uc009tck.1; mouse.
DR   UCSC; uc009tcm.1; mouse.
DR   CTD; 208968; -.
DR   MGI; MGI:2387585; Zfp280c.
DR   eggNOG; roNOG04576; -.
DR   GeneTree; ENSGT00530000063300; -.
DR   HOGENOM; HBG283620; -.
DR   HOVERGEN; HBG060885; -.
DR   InParanoid; Q6P3Y5; -.
DR   OMA; HMKRCCP; -.
DR   OrthoDB; EOG4J9MZM; -.
DR   NextBio; 372488; -.
DR   ArrayExpress; Q6P3Y5; -.
DR   Bgee; Q6P3Y5; -.
DR   CleanEx; MM_ZFP280C; -.
DR   Genevestigator; Q6P3Y5; -.
DR   GermOnline; ENSMUSG00000036916; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   SMART; SM00355; ZnF_C2H2; 10.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW   Phosphoprotein; Repeat; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    742       Zinc finger protein 280C.
FT                                /FTId=PRO_0000227976.
FT   ZN_FING     323    345       C2H2-type 1.
FT   ZN_FING     360    383       C2H2-type 2.
FT   ZN_FING     390    413       C2H2-type 3.
FT   ZN_FING     420    443       C2H2-type 4.
FT   ZN_FING     477    499       C2H2-type 5.
FT   COMPBIAS     30     37       Poly-Glu.
FT   COMPBIAS     62    244       Ser-rich.
FT   MOD_RES     125    125       Phosphoserine (By similarity).
FT   MOD_RES     128    128       Phosphoserine (By similarity).
FT   MOD_RES     232    232       Phosphoserine (By similarity).
FT   VAR_SEQ      11     19       Missing (in isoform 3).
FT                                /FTId=VSP_017619.
FT   VAR_SEQ     686    693       RGITLVCL -> SYRKSRNF (in isoform 2).
FT                                /FTId=VSP_017620.
FT   VAR_SEQ     694    742       Missing (in isoform 2).
FT                                /FTId=VSP_017621.
SQ   SEQUENCE   742 AA;  83146 MW;  04A82F753CAD6C10 CRC64;
     MDKDNSVQEK GLFLSSWKLD NSKMAELFME CEEEELEPWQ QKVEESQSKD DDDELIFVGE
     ISSSKPAISN ILNRCSPGSS SKGLKNGSFN PAISNIFKPT SQHYRNPSSN ALVALPSFHP
     ALKSSESSDG QTVSKLDFTK TSPQEDSGAC SVSQSDSTQD IPSSNILQPR TGVDQTLGLK
     HPSTSKVNSV NPKKPKTSAS ISETRPCSSS SSQTAPSGAS SQTVLSNVNT SSVQSAPGSS
     SLRSCPKCNV KFRLLDPLKC HMKRCCPDMI NKFLETLKSE NSKAVSKATT DSDKEKLIML
     VSDFYYGRHE GTIEESQKTH TTFKCFSCTK VLKNNIRFMN HMKHHLELEK QNNETWESHT
     TCQHCYRQYP NPFQLQCHIE STHTPHDFST ICKICELSFE TEHMLLQHMK DTHKPGEMPY
     ICQVCQFRSS IFSDVETHFR SSHENTKNLL CPFCLKVSRM ATPYMNHYMR HQKKGIYRCP
     KCRLQFLTSK EKTEHKLEHR TFIKPKELEG LPPGTKVIIR ASLGSSQSRA SSPPSSTIPS
     TSLQLSVPKS KSTTTKNNSK VSANKATTTS PQTVATTTGK PSASKPGTGT TKSKAKPSYK
     QKRQRTRKNK FSIDLKNLRC HQGSHMCIEC RSKIKDFSSH FSTHINCDFC KYTTNCNKAF
     TNHMSSHNDH PSKQLYIFKK QSRARRGITL VCLKCDFLAD TSGLDRMAKH LNQRKTHTCQ
     VVIENVTERA VTSESASDGL FK
//
ID   Q6P3Z4_MOUSE            Unreviewed;       590 AA.
AC   Q6P3Z4;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   SubName: Full=Zinc finger protein 37;
GN   Name=Zfp37;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC063757; AAH63757.1; -; mRNA.
DR   IPI; IPI00330912; -.
DR   RefSeq; NP_033580.3; NM_009554.3.
DR   UniGene; Mm.5011; -.
DR   HSSP; P08046; 1A1H.
DR   ProteinModelPortal; Q6P3Z4; -.
DR   SMR; Q6P3Z4; 9-59, 249-581.
DR   STRING; Q6P3Z4; -.
DR   Ensembl; ENSMUST00000068822; ENSMUSP00000070463; ENSMUSG00000028389.
DR   GeneID; 22696; -.
DR   KEGG; mmu:22696; -.
DR   UCSC; uc008tbx.1; mouse.
DR   CTD; 22696; -.
DR   MGI; MGI:99181; Zfp37.
DR   HOVERGEN; HBG018163; -.
DR   InParanoid; Q6P3Z4; -.
DR   PhylomeDB; Q6P3Z4; -.
DR   NextBio; 303155; -.
DR   ArrayExpress; Q6P3Z4; -.
DR   Bgee; Q6P3Z4; -.
DR   Genevestigator; Q6P3Z4; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; TAS:MGI.
DR   GO; GO:0007281; P:germ cell development; TAS:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR001909; Krueppel-associated_box.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 12.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF00096; zf-C2H2; 8.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 12.
DR   SUPFAM; SSF109640; Krueppel-associated_box; 1.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 11.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 12.
PE   2: Evidence at transcript level;
KW   Metal-binding; Zinc.
SQ   SEQUENCE   590 AA;  66772 MW;  7C7D82A4B2000287 CRC64;
     MATSEPAESD AEWEQLEPVQ RDVYKDTKLE NCSNPASMGN QDPKQDIVSV LEEEEPSSGK
     GKKASPSSLK KIARPKTAGT SAKLQQDDEH REEKQKSQSK LTKEVTLRKK SSNSKKSSEY
     GLLENKSLHS KHTPSEKKLL KSSSRGKNSN QNSDSLKKKP DTANDHRKSL SHSASDVNKD
     EIPTRKKCDK LPNNKLSDKG DKNQTSKKCE KVCRHSASHT KEDKIQTGEK RKSHCRTPSK
     PEKAPGSGKP YECNHCGKVL SHKQGLLDHQ RTHTGEKPYE CNECGIAFSQ KSHLVVHQRT
     HTGEKPYECE QCGKAHGHKH ALTDHLRIHT GEKPYKCNEC GKTFRHSSNL MQHLRSHTGE
     KPYECKECGK SFRYNSSLTE HVRTHTGEIP YECNECGKAF KYGSSLTKHM RIHTGEKPFE
     CNECGKTFSK KSHLVIHQRT HTKEKPYKCD ECGKAFGHSS SLTYHMRTHT GDCPFECNQC
     GKAFKQIEGL TQHQRVHTGE KPYECVECGK AFSQKSHLIV HQRTHTGEKP FECYECGKAF
     NAKSQLVIHQ RSHTGEKPYE CIECGKAFKQ NASLTKHMKI HSEEQSEEED
//
ID   SIK3_MOUSE              Reviewed;        1311 AA.
AC   Q6P4S6; Q641L5; Q66JZ5; Q6ZQ09; Q8K075; Q9CYD5;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 3.
DT   08-FEB-2011, entry version 67.
DE   RecName: Full=Serine/threonine-protein kinase SIK3;
DE            EC=2.7.11.1;
DE   AltName: Full=Salt-inducible kinase 3;
DE            Short=SIK-3;
DE   AltName: Full=Serine/threonine-protein kinase QSK;
GN   Name=Sik3; Synonyms=Kiaa0999, Qsk;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, C57BL/6J, and FVB/N;
RC   TISSUE=Brain, Limb, Salivary gland, and Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 260-1311 (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533 AND SER-534, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493 AND SER-616, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activated by phosphorylation on Thr-163 by
CC       STK11 in complex with STE20-related adapter-alpha (STRAD alpha)
CC       pseudo kinase and CAB39 (By similarity).
CC   -!- SUBUNIT: Binds to and is activated by YWHAZ when phosphorylated on
CC       Thr-163 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Locates to punctate
CC       structures within the cytoplasm on binding to YWHAZ (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6P4S6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6P4S6-2; Sequence=VSP_020894, VSP_020895;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. AMPK subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 UBA domain.
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DR   EMBL; AK017789; BAB30934.1; -; mRNA.
DR   EMBL; BC033915; AAH33915.1; -; mRNA.
DR   EMBL; BC063268; AAH63268.2; -; mRNA.
DR   EMBL; BC080688; AAH80688.1; -; mRNA.
DR   EMBL; BC082313; AAH82313.1; -; mRNA.
DR   EMBL; AK129257; BAC98067.1; -; mRNA.
DR   IPI; IPI00453673; -.
DR   IPI; IPI00788421; -.
DR   RefSeq; NP_081774.3; NM_027498.3.
DR   UniGene; Mm.219459; -.
DR   HSSP; O08679; 1ZMW.
DR   ProteinModelPortal; Q6P4S6; -.
DR   SMR; Q6P4S6; 3-326.
DR   PhosphoSite; Q6P4S6; -.
DR   PRIDE; Q6P4S6; -.
DR   Ensembl; ENSMUST00000078669; ENSMUSP00000077737; ENSMUSG00000034135.
DR   GeneID; 70661; -.
DR   KEGG; mmu:70661; -.
DR   UCSC; uc009pgz.1; mouse.
DR   UCSC; uc009pha.1; mouse.
DR   CTD; 70661; -.
DR   MGI; MGI:2446296; Sik3.
DR   eggNOG; roNOG08031; -.
DR   GeneTree; ENSGT00600000084026; -.
DR   HOGENOM; HBG716438; -.
DR   HOVERGEN; HBG079682; -.
DR   InParanoid; Q6P4S6; -.
DR   PhylomeDB; Q6P4S6; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 332051; -.
DR   ArrayExpress; Q6P4S6; -.
DR   Bgee; Q6P4S6; -.
DR   CleanEx; MM_BC033915; -.
DR   Genevestigator; Q6P4S6; -.
DR   GermOnline; ENSMUSG00000034135; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Cytoplasm; Kinase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1   1311       Serine/threonine-protein kinase SIK3.
FT                                /FTId=PRO_0000252258.
FT   DOMAIN        8    259       Protein kinase.
FT   DOMAIN      286    326       UBA.
FT   NP_BIND      14     22       ATP (By similarity).
FT   COMPBIAS    640   1003       Gln-rich.
FT   ACT_SITE    130    130       Proton acceptor (By similarity).
FT   BINDING      37     37       ATP (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      13     13       Phosphothreonine (By similarity).
FT   MOD_RES     156    156       Phosphothreonine (By similarity).
FT   MOD_RES     163    163       Phosphothreonine (By similarity).
FT   MOD_RES     167    167       Phosphoserine (By similarity).
FT   MOD_RES     493    493       Phosphoserine.
FT   MOD_RES     527    527       Phosphothreonine (By similarity).
FT   MOD_RES     533    533       Phosphoserine.
FT   MOD_RES     534    534       Phosphoserine.
FT   MOD_RES     616    616       Phosphoserine.
FT   MOD_RES     720    720       Phosphoserine (By similarity).
FT   MOD_RES     856    856       Phosphoserine (By similarity).
FT   VAR_SEQ       1     58       Missing (in isoform 2).
FT                                /FTId=VSP_020894.
FT   VAR_SEQ     546   1311       Missing (in isoform 2).
FT                                /FTId=VSP_020895.
FT   CONFLICT   1032   1032       H -> Q (in Ref. 2; AAH82313 and 3;
FT                                BAC98067).
FT   CONFLICT   1277   1277       S -> N (in Ref. 2; AAH63268/AAH80688).
SQ   SEQUENCE   1311 AA;  145784 MW;  CF110B679B4C3F2B CRC64;
     MAARIGYYEI DRTIGKGNFA VVKRATHLVT KAKVAIKIID KSQLDEENLK KIFREVQIMK
     MLCHPHIIRL YQVMETERMI YLVTEYASGG EIFDHLVAHG RMAEKEARRK FKQIVTAVYF
     CHCRNIVHRD LKAENLLLDA NLNIKIADFG FSNLFTPGQL LKTWCGSPPY AAPELFEGKE
     YDGPKVDIWS LGVVLYVLVC GALPFDGSTL QNLRARVLSG KFRIPFFMST ECEHLIRHML
     VLDPNKRLSM EQICRHKWMK LGDADPNFDR LIAECQQLKE ERQSDPLNDD VLLAMEDMGL
     DKERTLQSLR SDAYDHYSAI YSLLCDRHKK HKTLRPGALP SMPQAMTFQA PVNLQAEQTG
     TAMNLSVPQV QLINPENQII EPDGAVNLDS DEGEEPSPEA LVRYLSMRRH TVGVADPRTE
     VMEDLQKLLP GFPGVNPQGP FLQVAPNMNF THNLLPMQSL QPTGQLEYKE QSLLQPPTLQ
     LLNGMGPLGR RASDGGANIQ LHAQQLLKRP RGPSPLVTMT PAVPAVTPVD EESSDGEPDQ
     EAVQRYLANR SKRHTLAMTS PTAEIPPDLQ RQLGQQSFRS RVWPPHLVPD QHRSTYKDSN
     TLHLPTERFS PVRRFSDGAA SIQAFKAHLE KMGNSSSIKQ LQQECEQLQK MYGGQVDERT
     LEKTQQQHML YQQEQHHQIL QQQIQDSICP PQPSPPLQVA CENQPALLTH QLQRLRIQPS
     SPPPNHPSNH LFRQPSNSPP PVSSAMITSH GATSPSQFQG LPSHGAIFQQ QPENCSPPPS
     VALTCLGLQQ ASQSQPVTIQ LQEPVDMLSN MAGTAAGSAG RSIPISPSAS QIQIQHRASL
     MAPFSYGHRP LSKQLSADSA EAHSLNMNRF SPANYDQAHL HPHLFSDQSR GSPSSYSPST
     GVGFPPTQAL KVPPLDQFPT FPPSAQQQPP HYTTSALQQA LLSPTPPDYP RHQQVPHILQ
     GLLSPRHSLT GHSDIRLPPA EFAQLIKRQQ QHRQQQQQQQ QQQEYHELFR HMNQGDAVSL
     APSLGGQNMT EHQALSYQNA DSYHRHHTSP QHILQIRAQD CISQGPSPTP THGYAHQPPL
     MHSESMEEDC LCEGLKEGFP DKSSSTLTKG CHNSPLLLCT SGPGDPEPLL GTVSQARELG
     IHPYGHQPTA TTFSRNKVPS RESVLGNCLE RSSPGQAMEL PDHNGLGYPV RPLVSEHLRS
     RTLQRHHTIQ NSDDAYVQLD TLPGMSLVAG KALSSARMSD AVLSQSSLMG SQQFQDEEDE
     ECGVSLGHEH PGLGDGSQHL NSSRYPATCV TDIMLSHKHP EVSFSMEQAG V
//
ID   INT1_MOUSE              Reviewed;        2195 AA.
AC   Q6P4S8; Q0KK58; Q80UQ7; Q91Z01; Q9CTF7;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Integrator complex subunit 1;
DE            Short=Int1;
GN   Name=Ints1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RG   The German cDNA consortium;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2034-2195.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1328 AND SER-1329, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Component of the Integrator complex, a complex involved
CC       in the small nuclear RNAs (snRNA) U1 and U2 transcription and in
CC       their 3'-box-dependent processing. The Integrator complex is
CC       associated with the C-terminal domain (CTD) of RNA polymerase II
CC       largest subunit (POLR2A) and is recruited to the U1 and U2 snRNAs
CC       genes (By similarity).
CC   -!- SUBUNIT: Belongs to the multiprotein complex Integrator, at least
CC       composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7,
CC       INTS8, INTS9/RC74, INTS10, CPSF3L/INTS11 and INTS12 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane; Single-pass membrane
CC       protein (Potential).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH63266.1; Type=Miscellaneous discrepancy; Note=Could be due to alternative splicing but with non canonical splice junction;
CC       Sequence=BAF03197.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AB257854; BAF03197.1; ALT_INIT; mRNA.
DR   EMBL; BC010333; AAH10333.1; -; mRNA.
DR   EMBL; BC063266; AAH63266.1; ALT_SEQ; mRNA.
DR   EMBL; AK003728; BAB22963.1; -; mRNA.
DR   IPI; IPI00877221; -.
DR   RefSeq; NP_081024.3; NM_026748.2.
DR   UniGene; Mm.292942; -.
DR   STRING; Q6P4S8; -.
DR   PhosphoSite; Q6P4S8; -.
DR   PRIDE; Q6P4S8; -.
DR   Ensembl; ENSMUST00000072607; ENSMUSP00000072406; ENSMUSG00000029547.
DR   GeneID; 68510; -.
DR   KEGG; mmu:68510; -.
DR   UCSC; uc009agz.1; mouse.
DR   UCSC; uc009aha.1; mouse.
DR   CTD; 68510; -.
DR   MGI; MGI:1915760; Ints1.
DR   eggNOG; roNOG10970; -.
DR   GeneTree; ENSGT00390000015743; -.
DR   HOGENOM; HBG356920; -.
DR   HOVERGEN; HBG081799; -.
DR   InParanoid; Q6P4S8; -.
DR   OrthoDB; EOG4STS3P; -.
DR   NextBio; 327330; -.
DR   ArrayExpress; Q6P4S8; -.
DR   Bgee; Q6P4S8; -.
DR   CleanEx; MM_INTS1; -.
DR   Genevestigator; Q6P4S8; -.
DR   GermOnline; ENSMUSG00000029547; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001833; P:inner cell mass cell proliferation; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptosis; IMP:MGI.
DR   GO; GO:0043154; P:negative regulation of caspase activity; IMP:MGI.
DR   GO; GO:0034474; P:U2 snRNA 3'-end processing; IMP:MGI.
DR   InterPro; IPR022145; DUF3677.
DR   Pfam; PF12432; DUF3677; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Membrane; Nucleus; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   2195       Integrator complex subunit 1.
FT                                /FTId=PRO_0000236045.
FT   TRANSMEM   1165   1185       Helical; (Potential).
FT   MOD_RES      47     47       N6-acetyllysine (By similarity).
FT   MOD_RES      83     83       Phosphothreonine (By similarity).
FT   MOD_RES    1328   1328       Phosphoserine.
FT   MOD_RES    1329   1329       Phosphoserine.
FT   CONFLICT   1680   1680       C -> R (in Ref. 1; BAF03197 and 2;
FT                                AAH10333).
SQ   SEQUENCE   2195 AA;  245168 MW;  47C1DEA4609197BE CRC64;
     MNRAKPTTVR RPSAAAKPSG HPPPGDFIAL GSKGQASESK TTSTLLKPAP SGLPSERKRD
     ASASLSGTSA LTGLTKRPKL SSTPPLSALG RLAEAAVAEK RAISPSIKEP SVVPIEVLPT
     VLLDEIEAAE LEGNDDRIEG VLCGAVKQLK VTRAKPDSTL YLSLMYLAKI KPNIFATEGV
     IEALCSLLRR DASVNFKAKG NSLVSVLACN LLMAAYEEDE NWPEIFVKVY IEDSLGERIW
     VDSPHCRTFV DNIQTAFNTK MPPKSVLLQG EGARSGGELG AGSSPHPSLT EEEDSQTELL
     IAEEKLSPEQ EGQLMPRPRY DELTESVEEY VLDMLRDQLN RRQPIDNVSR NLLRLLTATC
     GYKEVRLLAV QRLEMWLQNP KLTRPAQDLL MSVCMNCNSH GSEDMDVISH LIKIRLKPKV
     LLNHYMLCIR ELLNAHKDNL GTTIKFVIFN ELSNARNPNN MQILYTVLQH SSELAPKFLA
     MVFQDLLTNK DDYLRASRAL LREIIKQTKH EINFQAFCLG LMQERKEPQY LEMEFKERFV
     VHITDVLAVS MMLGITAQVK EAGVAWDKGE KRNLEVLRTF QNQIAAIQRD AVWWLHTVVP
     SVSKLAPKDY VHCLHKVLFT EQPETYYKWD NWPPESDRNF FLRLCSEVPI LEDTLMRVLV
     IGLSRELPLG PADAMELADH LVKRAAAVQA DDVEVLKVER IQLIDAVLNL CTYHHPENIQ
     LPPGYQPPNL AISTLYWKAW PLLLVVAAFN PENIGLAAWE EYPTLKMLME MVMTNNYSYP
     PCTLTDEETR TEMINRELQI SQREKQEILA FEGHLAAAST KQTITESSSL LLSQLTSLDP
     QGPPRRPPPH ILDQVKALNQ SLRLGHLLCR SRNPDFLLHI IQRQASSQSM PWLADLVQSS
     EGSLDVLPVQ CLCEFLLHDA ADSTASGEED DEGESREQKA KKRQRQQKQR QLLGRLQDLL
     LGPKADEQTT CEVLDYFLRR LGSSQVASRV LAMKGLSLVL SEGGLRDKEE KEPPMEEDIG
     ETDALQGYQW LLRDLPRLPL FDSVRTTTAL ALQQAIHMET DPQTISAYLI YLSQHTPVEE
     QGPHSDLALD VARLVVERST IMAHLFSKPS CSTASDAVLS ALLSVFSRYV RRMRKSKEGE
     EVYSWSESQD QVFLRWSSGE TATMHILVVH AMVILLTLGP PRSGDSEFSE LLDIWFPEKK
     PLPTAFLVDT SEEALLLPDW LKLRMIRSEV PRLVDAALQD LEPQQLLLFV QSFGIPVSSM
     SKLLQYLDQA VAQDPQTLEQ NIMDKNYMAH LVEVQHERGA SGGQTFHSLL TASLPPRRDS
     TEAPKPESSP EPPPGQGRTR AGTQVPVLGP EDDLAGIFLQ IFPLSPDPRW QSSSPRPLAL
     ALQQALGQEL ARVRQGNPEV PGITVRLLQA MTTLLSSPHG GTLALAMHHS HFLSCPLMRQ
     LYQYQRAVPQ DTGFSSLFLK VLMQILQWLD SPAVEDGPLQ AQLKLFATRY SARHRISDVR
     SGLLHLADAL SFHGDLEVAN STARAVIATL RSGEKCPVEP ELISKVLRGL IEVRSPHLEE
     LLTALFSATT ETSCPSPASG PIVVVSSLLL QEKEELLGPS KQEVEGASTE AMRLGPASGL
     LVDWLETLDP EVVCSCPDLQ WKLLFSRRKG KGHISAQVLS FRPYLLALLT HQASWSTLHC
     CIRVLLGKSR EQRLDPSASL DFLWACIHVP RIWQGRDQRT PQKRREELVL HVQGPELLSL
     VELILSEAET RSQDGDSAAR TLIQTRLPLL LSCCRSNDES IGKVTEHLTS CIQQWGDSVL
     GQRCRDLLLQ LYLQRPEVRV PVPEVLLQSE GATSSSICKL DGLVHRFITL LADTSDSRSS
     ESRVADANMA CRKLAVAHPV LLLRHLPMIA ALLHGRTHLN FQEFRQQNHL AFFLHVLGIL
     ELLQPRVFQS EHQGALWDCL RSFIRLLLNY RKSSRHLAPF ISKFVQFIHK YVGCSAPAAV
     AFLQKHAEPL HDLSFDNSDL VMLKSLLAGL SLPSRDGRTD QGLDEEGEDE RSAGSLPLVS
     VSLSTPLTVA DVAPHMKRLS RGRAVEDVLE TLSDIDEMSR RRPEVLGFFS TNLQRLMSSA
     EESCRNLAFS LALRSIQNNP SIAADFLPTF MYCLGSRDFE VVQTALRNLP EYTLLCQEHA
     AVLLHRAFLV GVYGQIDTSA QISEALKILH MEAVM
//
ID   ATG2A_MOUSE             Reviewed;        1914 AA.
AC   Q6P4T0; Q3U9I1; Q6PHN0; Q6ZQC4; Q8R213;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Autophagy-related protein 2 homolog A;
GN   Name=Atg2a; Synonyms=Kiaa0404;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1696-1914.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-875 AND SER-877, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SIMILARITY: Belongs to the ATG2 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97942.1; Type=Erroneous initiation;
CC       Sequence=BAE30685.1; Type=Frameshift; Positions=1765;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK129132; BAC97942.1; ALT_INIT; mRNA.
DR   EMBL; BC022657; AAH22657.1; -; mRNA.
DR   EMBL; BC056482; AAH56482.2; -; mRNA.
DR   EMBL; BC063264; AAH63264.2; -; mRNA.
DR   EMBL; AK151782; BAE30685.1; ALT_FRAME; mRNA.
DR   IPI; IPI00830210; -.
DR   RefSeq; NP_919329.2; NM_194348.3.
DR   UniGene; Mm.277384; -.
DR   PhosphoSite; Q6P4T0; -.
DR   PRIDE; Q6P4T0; -.
DR   Ensembl; ENSMUST00000045351; ENSMUSP00000046412; ENSMUSG00000024773.
DR   GeneID; 329015; -.
DR   KEGG; mmu:329015; -.
DR   UCSC; uc008ghv.1; mouse.
DR   CTD; 329015; -.
DR   MGI; MGI:1916291; Atg2a.
DR   eggNOG; roNOG06723; -.
DR   GeneTree; ENSGT00580000081561; -.
DR   HOGENOM; HBG315549; -.
DR   HOVERGEN; HBG079553; -.
DR   InParanoid; Q6P4T0; -.
DR   OMA; CPPVETA; -.
DR   OrthoDB; EOG4C5CHH; -.
DR   PhylomeDB; Q6P4T0; -.
DR   NextBio; 398540; -.
DR   ArrayExpress; Q6P4T0; -.
DR   Bgee; Q6P4T0; -.
DR   Genevestigator; Q6P4T0; -.
DR   InterPro; IPR015412; Autophagy-rel_C.
DR   Pfam; PF09333; ATG_C; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1   1914       Autophagy-related protein 2 homolog A.
FT                                /FTId=PRO_0000315235.
FT   MOD_RES     258    258       Phosphotyrosine (By similarity).
FT   MOD_RES     875    875       Phosphoserine.
FT   MOD_RES     877    877       Phosphoserine.
FT   MOD_RES    1282   1282       Phosphoserine (By similarity).
FT   CONFLICT    285    285       L -> M (in Ref. 1; BAC97942).
FT   CONFLICT   1738   1738       R -> G (in Ref. 3; BAE30685).
FT   CONFLICT   1865   1865       V -> M (in Ref. 3; BAE30685).
SQ   SEQUENCE   1914 AA;  210939 MW;  16742111A5534572 CRC64;
     MSRWLWPWSN CVKERVCRYL LQHYLGHFFQ EHLSLDQLSL DLYKGSVALR DIHLETWSVN
     EFLRSMESPL ELVEGFVSSI EVAVPWAALL TDHCTVCVSG LQLTLQPRQG SGPGAADSQS
     WASCMTTSLQ LAQECLREGL PEPSEPPQPL EGLEMFAQTI ETVLRRIKVT FLNTVVRVEH
     SLGDEDRSVA VEVRVQRLEY CDEAVRDPSQ APPVDVHQPP AFLHKLLQLS GVCLYFEELP
     SQADPPQPPL QIGSCTGYVE LMVRLKQNEA FPGPKLEVSG QLGSLHLLLT PRQLQQLQRL
     LSAVNLADPA GLADKLNKSR PLGAEDLWLI EQDLNQQLQA GAVAESLSLY PITNPLNLDS
     TDLFFSMAGL TSSVTSAVSE LSVYSVDLGS SVHSNMAFHR PSTPPHSGGK MAPTPLLDTT
     RPDSLVKMTL GGVSLTLLQT ASPSSGPSDL PTHFFAEFDA AKDGPFGSRD FSHLRPRFQR
     ACPCSHVRLT GTAVQLSWEL RTGSHSRRTS STEVHFGQLE VLECLWPRAA TEPEYTEILS
     FPSHSGSEAS ARPCAHLRHT QTIRRVLKSR SRRSTACHCH SELSLDLADF QSDVELGSLD
     RLAALFRQVT TPSEPPAGLL TEPPQATELQ TVFRLSAPRA TLRLRFPIPD LRPDRDPWAG
     QAVRAEQLRL ELSEPQFRSE LNSGPGPPAP TRLELTCSDL QGIYEDGEKP PVPCLRVSKA
     LNPRSTEAKY FLPQVVVTLN PQSSGTQWET AYEKGRDLEL STESPCELQQ PEPSPFSSKR
     TMYETEEMVI PGDPEEMRTF QSRTLALSRC TLDVIMPSAH IFLPSKEVYE SIYNRINNDL
     LMWEPADLLP TSSAAARPPG SSGFKMCKSA FKLDSDSDEE DAQFFSMASG VPQTPAPEPS
     RRQSQSTFST LVTVLKGRIT ALCEAKDETG KRLDVTHGEL VLDVEQGTIF SVAQYRGQPG
     LGYFCLEAEK AKLYHRAAIE DYLLPTHLEV PSFAPPAQLA PTIYPSEEGV TERGTLGRKG
     QGPPMLSAAV RIHLDPHKNV KEFLVTVRLH KATLRHYMAP PEQSWHSQLL DFLDVLDDPV
     LGYLPPTVIT VLHTHLFSCA VDYRPLYLPV RVLVTAETFT LSSNIVMDTS TFLLRFILDD
     SALYLSDKCE VESLDLRRDY VCVLDIDLLE LVIKTWKGST EGRLSQPLFE LRCSNNVVHV
     HSCADSCALL VNLLQYLTSS GDLHPPPRPP SPTEIAGQKL SESPASLPSC LPVETALINQ
     RDLTDALLDT ERRGLQELAQ SSGGPLPQAS PVSVYLFPGE RSGAQAPLPP PGASSHTLGS
     KAKEHENEEE GDGDTLDSDE FCILDAPGLG IAPRDGEPIV TQLHPGPIIV HDGHFSQPLG
     STDLLRAPAH FPVPSSRVVL REVSFIWHLY GGRDFGLHPT YRARVGLTGP RVSPSRSSGP
     NRPQNSWRTQ GGIGRQHQVL MEIQLSKVSF QHEVYPEESA IAGGLGQELD ERPLSRQVLI
     VQELEIRDRL ATSKINKFLH LHTSERLPRR THSNMLTIKA LHVAPTSSVG GPECCLRVSM
     MPLRLNVDQD ALFFLKDFFT SLAASINPMV PGDTSEAPRE THSRPGSPQE GQSEDTETAS
     NPPEAPGSSH SSSDQQPIYF REFRFTSEVP ICLDYHGKHV TVDQVGTFMG LLIGLAQLNC
     SELKLKRLCC RHGLLGVDKV LCYALNEWLQ DIRKNQLPGL LGGVGPMHSV VQLFQGFRDL
     LWLPIEQYRK DGRLIRGLQR GAASFGSSTA SAALELSNRL VQAIQATAET VYDILSPASP
     VSRSLQDKRS SRKLRRGQQP ADLREGMAKA YDAVREGILD TAQTICDVAS RGHEQKGLTG
     AVGGVIRQLP PTVVKPIIVA TEATSNVLGG MRNQILPDAH KDHALKWRLE EAQD
//
ID   Q6P4T1_MOUSE            Unreviewed;       997 AA.
AC   Q6P4T1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   SubName: Full=Sorting nexin 19;
GN   Name=Snx19;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC063262; AAH63262.1; -; mRNA.
DR   IPI; IPI00337929; -.
DR   RefSeq; NP_083150.1; NM_028874.2.
DR   UniGene; Mm.35084; -.
DR   ProteinModelPortal; Q6P4T1; -.
DR   SMR; Q6P4T1; 540-663.
DR   STRING; Q6P4T1; -.
DR   PRIDE; Q6P4T1; -.
DR   Ensembl; ENSMUST00000034475; ENSMUSP00000034475; ENSMUSG00000031993.
DR   GeneID; 102607; -.
DR   KEGG; mmu:102607; -.
DR   UCSC; uc009oqy.1; mouse.
DR   CTD; 102607; -.
DR   MGI; MGI:1921581; Snx19.
DR   HOVERGEN; HBG062485; -.
DR   InParanoid; Q6P4T1; -.
DR   OMA; FLCEDSE; -.
DR   NextBio; 355556; -.
DR   ArrayExpress; Q6P4T1; -.
DR   Bgee; Q6P4T1; -.
DR   Genevestigator; Q6P4T1; -.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   InterPro; IPR001683; Phox.
DR   InterPro; IPR003114; Phox_assoc.
DR   InterPro; IPR013937; Sorting_nexin_C.
DR   Gene3D; G3DSA:3.30.1520.10; PX; 1.
DR   Pfam; PF08628; Nexin_C; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF02194; PXA; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; PX; 1.
DR   PROSITE; PS50195; PX; 1.
DR   PROSITE; PS51207; PXA; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   997 AA;  109808 MW;  AA8241D6F7BCCC71 CRC64;
     MKAQTVSPTQ GTISESSYVH SNLWSSRKLM IVGVLVGWLL VIHLLVNMWL LILLCASLVA
     LGGWLGSTAI LGASGQLHLE RFITITTCPP CPEAERQLEQ EINRTIQMII RDFVLSWYRS
     VSHEPAFEAE MEAAMKGLVQ ELRRRMSIVD SHALTQRVLT LCGCHLQSYI QAKEATAKEQ
     SCPVQPSQLW DAYCQVTAPH PAMSCPTTEV TYARGIVNLI LKELVPKPHL ETRTGRHVVV
     EVITCNVILP LISKLSDPDW IHLILVSIFS KYRHDAAQGT KPPCSSSVLE QPSVPTSLPL
     IVEVESLPVG KASSPATAPV HLTSSEPAPS PEIEEGHEAV EGDLPGMLEE KKVGNSSSHF
     LQPDIRGPLF LCEDSELESP LSELSKETIL LMTPGNFLSD RIQDALCALD DSGALEPKDG
     EGSECMEGAE AEEAPGTDTE TGMLVSVLNC PEIQIDTADK EVEQGDDTSL TALLEEPEKP
     CPLRPSCLDK DLASGVCSLE PAMPPVPLSS SPPGPLSSAT FSFESLSSPD GPVVIQNLRI
     TGTITAREHS GTGFHPYTLY TVKYETVLNG ENSSGLQQLA YHTVNRRYRE FLNLQTRLEE
     KPDLRKFIKN VKGPKKLFPD LPFGNMDSDR VEARKSLLES FLKQLCAIPE IGNSEEVQEF
     LALNTDARIA FVKKPFMVSR IDKMVVSAIV DTLKTAFPRS EPQSPTEELS EAENESKPQT
     EGKKASKSRL RFSSSKIAPA LSIAEAQDKI LYCLQEGNSE SEVLSMSGME SFIEKQTKLL
     RIQPAEVPDK DPQQVPKEYV DSGLLDKAVV AQELNKSGPG TETELADTAF DLILLLLMEQ
     WKWLCTESMQ KFLHIIFGTL VQRWLEVQVA NLTCPQRWAQ YLHLLRESIW PGGVLPKFPR
     PGRTQAQKAA TEKQALQSLM DLLPDFLVEI LGVNKCRLSW SLVLESFQQP LINRHLIYCL
     GDIILELLDL SASVEECAPA TSASDSPGSL KKMAVST
//
ID   Q6P4T2_MOUSE            Unreviewed;      2136 AA.
AC   Q6P4T2;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   SubName: Full=Activating signal cointegrator 1 complex subunit 3-like 1;
DE   SubName: Full=Small nuclear ribonucleoprotein 200 (U5);
GN   Name=Snrnp200; Synonyms=Ascc3l1; ORFNames=RP23-206D14.2-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RA   Wood J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC063261; AAH63261.1; -; mRNA.
DR   EMBL; AL845368; CAM17440.1; -; Genomic_DNA.
DR   IPI; IPI00420329; -.
DR   RefSeq; NP_796188.2; NM_177214.4.
DR   UniGene; Mm.215860; -.
DR   ProteinModelPortal; Q6P4T2; -.
DR   SMR; Q6P4T2; 464-1287, 1325-2129.
DR   STRING; Q6P4T2; -.
DR   PhosphoSite; Q6P4T2; -.
DR   PRIDE; Q6P4T2; -.
DR   Ensembl; ENSMUST00000103220; ENSMUSP00000099509; ENSMUSG00000003660.
DR   GeneID; 320632; -.
DR   KEGG; mmu:320632; -.
DR   UCSC; uc008mez.1; mouse.
DR   CTD; 320632; -.
DR   MGI; MGI:2444401; Snrnp200.
DR   HOGENOM; HBG736699; -.
DR   HOVERGEN; HBG051896; -.
DR   InParanoid; Q6P4T2; -.
DR   OMA; TQFYNGK; -.
DR   PhylomeDB; Q6P4T2; -.
DR   NextBio; 397101; -.
DR   ArrayExpress; Q6P4T2; -.
DR   Bgee; Q6P4T2; -.
DR   Genevestigator; Q6P4T2; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-KW.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR004179; Sec63-dom.
DR   InterPro; IPR023290; Sec63-domain.
DR   Pfam; PF00270; DEAD; 2.
DR   Pfam; PF00271; Helicase_C; 2.
DR   Pfam; PF02889; Sec63; 2.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM00487; DEXDc; 2.
DR   SMART; SM00490; HELICc; 2.
DR   SMART; SM00611; SEC63; 2.
DR   SMART; SM00973; Sec63; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR   PROSITE; PS51194; HELICASE_CTER; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW   Ribonucleoprotein; Viral nucleoprotein; Virion.
SQ   SEQUENCE   2136 AA;  244547 MW;  BBDD6058CA635519 CRC64;
     MADVTARSLQ YEYKANSNLV LQADRSLIDR TRRDEPTGEV LSLVGKLEGT RMGDKAQRTK
     PQMQEERRAK RRKRDEDRHD MNKMKGYTLL SEGIDEMVGI IYKPKTKETR ETYEVLLSFI
     QAALGDQPRD ILCGAADEVL AVLKNEKLRD KERRREIDLL LGQTDDTRYH VLVNLGKKIT
     DYGGDKEIQN MDDNIDETYG VNVQFESDEE EGDEDVYGEV REEASDDDME GDEAVVRCTL
     SANLVASGEL MSSKKKDLHP RDIDAFWLQR QLSRFYDDAI VSQKKADEVL EILKTASDDR
     ECENQLVLLL GFNTFDFIKV LRQHRMMILY CTLLASAQSE PEKERIVGKM EADPELSKFL
     YQLHETEKED LIREERSRRE RVRQSRMDTD LETMDLDQGG EALAPRQVLD LEDLVFTQGS
     HFMANKRCQL PDGSFRRQRK GYEEVHVPAL KPKPFGSEEQ LLPVEKLPKY AQAGFEGFKT
     LNRIQSKLYR AALETDENLL LCAPTGAGKT NVALMCMLRE IGKHINMDGT INVDDFKIIY
     IAPMRSLVQE MVGSFGKRLA TYGITVAELT GDHQLCKEEI SATQIIVCTP EKWDIITRKG
     GERTYTQLVR LIVLDEIHLL HDDRGPVLEA LVARAIRNIE MTQEDVRLIG LSATLPNYED
     VATFLRVDPA KGLFYFDNSF RPVPLEQTYV GITEKKAIKR FQIMNEIVYE KIMEHAGKNQ
     VLVFVHSRKE TGKTARAIRD MCLEKDTLGL FLREGSASTE VLRTEAEQCK NLELKDLLPY
     GFAIHHAGMT RVDRTLVEDL FADKHIQVLV STATLAWGVN LPAHTVIIKG TQVYSPEKGR
     WTELGALDIL QMLGRAGRPQ YDTKGEGILI TSHGELQYYL SLLNQQLPIE SQMVSKLPDM
     LNAEIVLGNV QNAKDAVNWL GYAYLYIRML RSPTLYGISH DDLKGDPLLD QRRLDLVHTA
     ALMLDKNNLV KYDKKTGNFQ VTELGRIASH YYITNDTVQT YNQLLKPTLS EIELFRVFSL
     SSEFKNITVR EEEKLELQKL LERVPIPVKE SIEEPSAKIN VLLQAFISQL KLEGFALMAD
     MVYVTQSAGR LMRAIFEIVL NRGWAQLTDK TLNLCKMIDK RMWQSMCPLR QFRKLPEEVV
     KKIEKKNFPF ERLYDLNHNE IGELIRMPKM GKTIHKYVHL FPKLELSVHL QPITRSTLKV
     ELTITPDFQW DEKVHGSSEA FWILVEDVDS EVILHHEYFL LKAKYAQDEH LITFFVPVFE
     PLPPQYFIRV VSDRWLSCET QLPVSFRHLI LPEKYPPPTE LLDLQPLPVS ALRNSAFESL
     YQDKFPFFNP IQTQVFNTVY NSDDNVFVGA PTGSGKTICA EFAILRMLLQ NSEGRCVYIT
     PMEALAEQVY MDWYEKFQDR LNKKVVLLTG ETSTDLKLLG KGNIIISTPE KWDILSRRWK
     QRKNVQNINL FVVDEVHLIG GENGPVLEVI CSRMRYISSQ IERPIRIVAL SSSLSNAKDV
     AHWLGCSATS TFNFHPNVRP VPLELHIQGF NISHTQTRLL SMAKPVYHAI TKHSPKKPVI
     VFVPSRKQTR LTAIDILTTC AADIQRQRFL HCTEKDLIPY LEKLSDSTLK ETLLNGVGYL
     HEGLSPMERR LVEQLFSSGA IQVVVASRSL CWGMNVAAHL VIIMDTQYYN GKIHAYVDYP
     IYDVLQMVGH ANRPLQDDEG RCVIMCQGSK KDFFKKFLYE PLPVESHLDH CMHDHFNAEI
     VTKTIENKQD AVDYLTWTFL YRRMTQNPNY YNLQGISHRH LSDHLSELVE QTLSDLEQSK
     CISIEDEMDV APLNLGMIAA YYYINYTTIE LFSMSLNAKT KVRGLIEIIS NAAEYENIPI
     RHHEDNLLRQ LAQKVPHKLN NPKFNDPHVK TNLLLQAHLS RMQLSAELQS DTEEILSKAI
     RLIQACVDVL SSNGWLSPAL AAMELAQMVT QAMWSKDSYL KQLPHFTSEH IKRCTDKGVE
     SVFDIMEMED EERNALLQLT DSQIADVARF CNRYPNIELS YEVVDKDSIR SGGPVVVLVQ
     LEREEEVTGP VIAPLFPQKR EEGWWVVIGD AKSNSLISIK RLTLQQKAKV KLDFVAPATG
     GHNYTLYFMS DAYMGCDQEY KFSVDVKEAE TDSDSD
//
ID   SHIP2_MOUSE             Reviewed;        1257 AA.
AC   Q6P549; O08611; Q0VDX5; Q80YB9; Q9JLL7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2;
DE            EC=3.1.3.n1;
DE   AltName: Full=AblSH3-binding protein;
DE   AltName: Full=Inositol polyphosphate phosphatase-like protein 1;
DE            Short=INPPL-1;
DE   AltName: Full=SH2 domain-containing inositol-5'-phosphatase 2;
DE            Short=SH2 domain-containing inositol phosphatase 2;
DE            Short=SHIP-2;
GN   Name=Inppl1; Synonyms=Ship2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   MEDLINE=20079159; PubMed=10610720; DOI=10.1006/geno.1999.5995;
RA   Schurmans S., Carrio R., Behrends J., Pouillon V., Merino J.,
RA   Clement S.;
RT   "The mouse SHIP2 (Inppl1) gene: complementary DNA, genomic structure,
RT   promoter analysis, and gene expression in the embryo and adult
RT   mouse.";
RL   Genomics 62:260-271(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 705-1183.
RX   MEDLINE=97271433; PubMed=9126384; DOI=10.1006/abio.1997.2040;
RA   Yamabhai M., Kay B.K.;
RT   "Examining the specificity of Src homology 3 domain -- ligand
RT   interactions with alkaline phosphatase fusion proteins.";
RL   Anal. Biochem. 247:143-151(1997).
RN   [4]
RP   INTERACTION WITH FCGR2B, AND PHOSPHORYLATION.
RX   PubMed=10789675; DOI=10.1016/S0165-2478(00)00162-0;
RA   Muraille E., Bruhns P., Pesesse X., Daeeron M., Erneux C.;
RT   "The SH2 domain containing inositol 5-phosphatase SHIP2 associates to
RT   the immunoreceptor tyrosine-based inhibition motif of Fc gammaRIIB in
RT   B cells under negative signaling.";
RL   Immunol. Lett. 72:7-15(2000).
RN   [5]
RP   FUNCTION, ENZYME ACTIVITY, AND MUTAGENESIS OF ARG-47; ASP-608;
RP   CYS-690; ARG-692 AND TYR-987.
RX   PubMed=10958682; DOI=10.1128/MCB.20.18.6860-6871.2000;
RA   Taylor V., Wong M., Brandts C., Reilly L., Dean N.M., Cowsert L.M.,
RA   Moodie S., Stokoe D.;
RT   "5' phospholipid phosphatase SHIP-2 causes protein kinase B
RT   inactivation and cell cycle arrest in glioblastoma cells.";
RL   Mol. Cell. Biol. 20:6860-6871(2000).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11343120; DOI=10.1038/35051094;
RA   Clement S., Krause U., Desmedt F., Tanti J.-F., Behrends J.,
RA   Pesesse X., Sasaki T., Penninger J., Doherty M., Malaisse W.,
RA   Dumont J.E., Le Marchand-Brustel Y., Erneux C., Hue L., Schurmans S.;
RT   "The lipid phosphatase SHIP2 controls insulin sensitivity.";
RL   Nature 409:92-97(2001).
RN   [7]
RP   ERRATUM.
RA   Clement S., Krause U., Desmedt F., Tanti J.-F., Behrends J.,
RA   Pesesse X., Sasaki T., Penninger J., Doherty M., Malaisse W.,
RA   Dumont J.E., Le Marchand-Brustel Y., Erneux C., Hue L., Schurmans S.;
RL   Nature 431:878-878(2004).
RN   [8]
RP   INDUCTION.
RX   PubMed=12145149;
RA   Hori H., Sasaoka T., Ishihara H., Wada T., Murakami S., Ishiki M.,
RA   Kobayashi M.;
RT   "Association of SH2-containing inositol phosphatase 2 with the insulin
RT   resistance of diabetic db/db mice.";
RL   Diabetes 51:2387-2394(2002).
RN   [9]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=14744864; DOI=10.1074/jbc.M311534200;
RA   Sasaoka T., Wada T., Fukui K., Murakami S., Ishihara H., Suzuki R.,
RA   Tobe K., Kadowaki T., Kobayashi M.;
RT   "SH2-containing inositol phosphatase 2 predominantly regulates Akt2,
RT   and not Akt1, phosphorylation at the plasma membrane in response to
RT   insulin in 3T3-L1 adipocytes.";
RL   J. Biol. Chem. 279:14835-14843(2004).
RN   [10]
RP   INTERACTION WITH FCGR2B.
RX   PubMed=15456754; DOI=10.1074/jbc.M410261200;
RA   Isnardi I., Lesourne R., Bruhns P., Fridman W.H., Cambier J.C.,
RA   Daeeron M.;
RT   "Two distinct tyrosine-based motifs enable the inhibitory receptor
RT   FcgammaRIIB to cooperatively recruit the inositol phosphatases SHIP1/2
RT   and the adapters Grb2/Grap.";
RL   J. Biol. Chem. 279:51931-51938(2004).
RN   [11]
RP   INTERACTION WITH TEC.
RX   PubMed=15492005; DOI=10.1074/jbc.M408141200;
RA   Tomlinson M.G., Heath V.L., Turck C.W., Watson S.P., Weiss A.;
RT   "SHIP family inositol phosphatases interact with and negatively
RT   regulate the Tec tyrosine kinase.";
RL   J. Biol. Chem. 279:55089-55096(2004).
RN   [12]
RP   FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH
RP   CSF1R.
RX   PubMed=15557176;
RA   Wang Y., Keogh R.J., Hunter M.G., Mitchell C.A., Frey R.S., Javaid K.,
RA   Malik A.B., Schurmans S., Tridandapani S., Marsh C.B.;
RT   "SHIP2 is recruited to the cell membrane upon macrophage colony-
RT   stimulating factor (M-CSF) stimulation and regulates M-CSF-induced
RT   signaling.";
RL   J. Immunol. 173:6820-6830(2004).
RN   [13]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15654325; DOI=10.1038/nm1178;
RA   Sleeman M.W., Wortley K.E., Lai K.-M.V., Gowen L.C., Kintner J.,
RA   Kline W.O., Garcia K., Stitt T.N., Yancopoulos G.D., Wiegand S.J.,
RA   Glass D.J.;
RT   "Absence of the lipid phosphatase SHIP2 confers resistance to dietary
RT   obesity.";
RL   Nat. Med. 11:199-205(2005).
RN   [14]
RP   FUNCTION.
RX   PubMed=16179375; DOI=10.1182/blood-2005-05-1841;
RA   Ai J., Maturu A., Johnson W., Wang Y., Marsh C.B., Tridandapani S.;
RT   "The inositol phosphatase SHIP-2 down-regulates FcgammaR-mediated
RT   phagocytosis in murine macrophages independently of SHIP-1.";
RL   Blood 107:813-820(2006).
CC   -!- FUNCTION: Phosphatidylinositol (PtdIns) phosphatase that
CC       specifically hydrolyzes the 5-phosphate of phosphatidylinositol-
CC       3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2,
CC       thereby negatively regulating the PI3K (phosphoinositide 3-kinase)
CC       pathways. Plays a central role in regulation of PI3K-dependent
CC       insulin signaling, although the precise molecular mechanisms and
CC       signaling pathways remain unclear. While overexpression reduces
CC       both insulin-stimulated MAP kinase and Akt activation, its absence
CC       does not affect insulin signaling or GLUT4 trafficking. Confers
CC       resistance to dietary obesity. May act by regulating AKT2, but not
CC       AKT1, phosphorylation at the plasma membrane. Part of a signaling
CC       pathway that regulates actin cytoskeleton remodeling. Required for
CC       the maintenance and dynamic remodeling of actin structures as well
CC       as in endocytosis, having a major impact on ligand-induced EGFR
CC       internalization and degradation. Participates in regulation of
CC       cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3
CC       thereby regulating membrane ruffling. Regulates cell adhesion and
CC       cell spreading. Required for HGF-mediated lamellipodium formation,
CC       cell scattering and spreading. Acts as a negative regulator of
CC       EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1
CC       activation. Acts as a regulator of neuritogenesis by regulating
CC       PtdIns(3,4,5)P3 level and is required to form an initial
CC       protrusive pattern, and later, maintain proper neurite outgrowth.
CC       Acts as a negative regulator of the FC-gamma-RIIA receptor
CC       (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor
CC       (FCGR2B), playing a central role in terminating signal
CC       transduction from activating immune/hematopoietic cell receptor
CC       systems. Involved in EGF signaling pathway. Upon stimulation by
CC       EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3.
CC       Plays a negative role in regulating the PI3K-PKB pathway, possibly
CC       by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated
CC       phagocytosis in macrophages independently of INPP5D/SHIP1. In
CC       macrophages, down-regulates NF-kappa-B-dependent gene
CC       transcription by regulating macrophage colony-stimulating factor
CC       (M-CSF)-induced signaling. May also hydrolyze PtdIns(1,3,4,5)P4,
CC       and could thus affect the levels of the higher inositol
CC       polyphosphates like InsP6.
CC   -!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 3,4,5-
CC       triphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 3,4-
CC       diphosphate + phosphate.
CC   -!- ENZYME REGULATION: Activated upon translocation to the sites of
CC       synthesis of PtdIns(3,4,5)P3 in the membrane. Enzymatic activity
CC       is enhanced in the presence of phosphatidylserine (By similarity).
CC   -!- SUBUNIT: Interacts with tyrosine phosphorylated form of SHC1,
CC       Interacts with EGFR. Upon stimulation by the EGF signaling
CC       pathway, it forms a complex with SHC1 and EGFR. Interacts with
CC       cytoskeletal protein SORBS3/vinexin, promoting its localization to
CC       the periphery of cells. Forms a complex with filamin (FLNA or
CC       FLNB), actin, GPIb (GP1BA or GP1BB) that regulates cortical and
CC       submembraneous actin. Interacts with c-Met/MET, when c-Met/MET is
CC       phosphorylated on 'Tyr-1356'. Interacts with p130Cas/BCAR1.
CC       Interacts with CENTD3/ARAP3 via its SAM domain. Interacts with c-
CC       Cbl/CBL and CAP/SORBS1. Interacts with activated EPHA2 receptor.
CC       Interacts with receptors FCGR2A and FCGR2B. Interacts with
CC       tyrosine kinases ABL1 and TEC. Interacts with CSF1R.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton,
CC       actin patch. Membrane; Peripheral membrane protein.
CC       Note=Translocates to membrane ruffles when activated,
CC       translocation is probably due to different mechanisms depending on
CC       the stimulus and cell type. Partly translocated via its SH2 domain
CC       which mediates interaction with tyrosine phosphorylated receptors
CC       such as the FC-gamma-RIIB receptor (FCGR2B). Tyrosine
CC       phosphorylation may also participate to membrane localization.
CC       Insulin specifically stimulates its redistribution from the
CC       cytosol to the plasma membrane. Recruited to the membrane
CC       following M-CSF stimulation.
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- DEVELOPMENTAL STAGE: In E15.5 embryos, it is strongly expressed in
CC       the liver, specific regions of the central nervous system, the
CC       thymus, the lung, and the cartilage perichondrium. In adult it is
CC       markedly present in the brain and the thymus and at different
CC       stages of spermatozoa maturation in the seminiferous tubules.
CC   -!- INDUCTION: Overexpressed in diabetic db/db mice.
CC   -!- DOMAIN: The SH2 domain interacts with tyrosine phosphorylated
CC       forms of proteins such as SHC1 or FCGR2A. It also mediates the
CC       interaction with p130Cas/BCAR1 (By similarity).
CC   -!- DOMAIN: The NPXY sequence motif found in many tyrosine-
CC       phosphorylated proteins is required for the specific binding of
CC       the PID domain (By similarity).
CC   -!- PTM: Tyrosine phosphorylated by the members of the SRC family
CC       after exposure to a diverse array of extracellular stimuli such as
CC       insulin, growth factors such as EGF or PDGF, chemokines, integrin
CC       ligands and hypertonic and oxidative stress. May be phosphorylated
CC       upon IgG receptor FCGR2B-binding. Phosphorylated at Tyr-987
CC       following cell attachment and spreading. Phosphorylated at Tyr-
CC       1161 following EGF signaling pathway stimulation (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice are viable, have normal glucose and
CC       insulin levels, and normal insulin and glucose tolerances. They
CC       are however highly resistant to weight gain when placed on a high-
CC       fat diet, suggesting that inhibition of Inppl1 would be useful in
CC       the effort to ameliorate diet-induced obesity. According to
CC       preliminary results from PubMed:11343120, mice display increased
CC       sensitivity to insulin, characterized by severe neonatal
CC       hypoglycaemia, deregulated expression of the genes involved in
CC       gluconeogenesis, and perinatal death. They display increased
CC       glucose tolerance and insulin sensitivity associated with an
CC       increased recruitment of the Slc2a4/Glut4 glucose transporter and
CC       increased glycogen synthesis in skeletal muscles. However, these
CC       knockout mice also contain a deletion of the last exon of Phox2a
CC       gene. It is therefore unknown whether the insulin sensitivity
CC       observed in these mice result from inactivation of either Inppl1
CC       or Phox2a.
CC   -!- SIMILARITY: Belongs to the inositol-1,4,5-trisphosphate 5-
CC       phosphatase family.
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI19454.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF162781; AAF28187.1; -; mRNA.
DR   EMBL; BC049961; AAH49961.1; -; mRNA.
DR   EMBL; BC063080; AAH63080.1; -; mRNA.
DR   EMBL; BC119453; AAI19454.1; ALT_INIT; mRNA.
DR   EMBL; U92477; AAB82337.1; -; mRNA.
DR   IPI; IPI00312067; -.
DR   RefSeq; NP_001116211.1; NM_001122739.1.
DR   RefSeq; NP_034697.2; NM_010567.2.
DR   UniGene; Mm.476000; -.
DR   HSSP; O60880; 1D1Z.
DR   ProteinModelPortal; Q6P549; -.
DR   SMR; Q6P549; 17-127, 423-732, 1193-1257.
DR   STRING; Q6P549; -.
DR   PhosphoSite; Q6P549; -.
DR   PRIDE; Q6P549; -.
DR   Ensembl; ENSMUST00000035836; ENSMUSP00000048057; ENSMUSG00000032737.
DR   GeneID; 16332; -.
DR   KEGG; mmu:16332; -.
DR   UCSC; uc009ipg.1; mouse.
DR   CTD; 16332; -.
DR   MGI; MGI:1333787; Inppl1.
DR   eggNOG; roNOG13415; -.
DR   GeneTree; ENSGT00590000082823; -.
DR   HOGENOM; HBG444184; -.
DR   HOVERGEN; HBG106726; -.
DR   InParanoid; Q6P549; -.
DR   OMA; YEEGLVH; -.
DR   OrthoDB; EOG4GMTW4; -.
DR   NextBio; 289422; -.
DR   ArrayExpress; Q6P549; -.
DR   Bgee; Q6P549; -.
DR   CleanEx; MM_INPPL1; -.
DR   Genevestigator; Q6P549; -.
DR   GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0044255; P:cellular lipid metabolic process; IMP:MGI.
DR   GO; GO:0006006; P:glucose metabolic process; IMP:MGI.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IDA:MGI.
DR   GO; GO:0010629; P:negative regulation of gene expression; IMP:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0032868; P:response to insulin stimulus; IMP:MGI.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   InterPro; IPR000300; IPPc.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR011510; SAM_2.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   SMART; SM00128; IPPc; 1.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00252; SH2; 1.
DR   SUPFAM; SSF56219; Exo_endo_phos; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Cell adhesion; Cytoplasm; Cytoskeleton; Hydrolase;
KW   Immunity; Membrane; Phosphoprotein; SH2 domain; SH3-binding.
FT   CHAIN         1   1257       Phosphatidylinositol-3,4,5-trisphosphate
FT                                5-phosphatase 2.
FT                                /FTId=PRO_0000302871.
FT   DOMAIN       21    117       SH2.
FT   DOMAIN     1195   1257       SAM.
FT   MOTIF       945    950       SH3-binding.
FT   MOTIF       984    987       NPXY motif.
FT   COMPBIAS    936   1170       Pro-rich.
FT   MOD_RES     132    132       Phosphoserine (By similarity).
FT   MOD_RES     158    158       Phosphoserine (By similarity).
FT   MOD_RES     165    165       Phosphothreonine (By similarity).
FT   MOD_RES     241    241       Phosphoserine (By similarity).
FT   MOD_RES     672    672       Phosphotyrosine (By similarity).
FT   MOD_RES     887    887       Phosphotyrosine (By similarity).
FT   MOD_RES     987    987       Phosphotyrosine (By similarity).
FT   MOD_RES     988    988       Phosphotyrosine (By similarity).
FT   MOD_RES    1004   1004       Phosphoserine (By similarity).
FT   MOD_RES    1136   1136       Phosphotyrosine (By similarity).
FT   MOD_RES    1161   1161       Phosphotyrosine (By similarity).
FT   MUTAGEN      47     47       R->A: Does not affect the ability to
FT                                inhibit PKB activity.
FT   MUTAGEN     608    608       D->A: Abolishes both enzyme activity and
FT                                ability to inhibit PKB activity.
FT   MUTAGEN     690    690       C->A: Induces little effect.
FT   MUTAGEN     692    692       R->A: Still partially active.
FT   MUTAGEN     987    987       Y->F: Does not affect the ability to
FT                                inhibit PKB activity.
FT   CONFLICT    412    412       M -> I (in Ref. 1; AAF28187).
FT   CONFLICT    506    506       L -> I (in Ref. 1; AAF28187).
FT   CONFLICT    705    705       C -> S (in Ref. 3; AAB82337).
FT   CONFLICT    972    972       G -> V (in Ref. 1; AAF28187).
SQ   SEQUENCE   1257 AA;  138973 MW;  B66DF96BEF22F01E CRC64;
     MASVCGTPSP GGALGSPAPA WYHRDLSRAA AEELLARAGR DGSFLVRDSE SVAGAFALCV
     LYQKHVHTYR ILPDGEDFLA VQTSQGVPVR RFQTLGELIG LYAQPNQGLV CALLLPVEGE
     REPDPPDDRD ASDVEDEKPP LPPRSGSTSI SAPVGPSSPL PTPETPTTPA AESTPNGLST
     VSHEYLKGSY GLDLEAVRGG ASNLPHLTRT LVTSCRRLHS EVDKVLSGLE ILSKVFDQQS
     SPMVTRLLQQ QSLPQTGEQE LESLVLKLSV LKDFLSGIQK KALKALQDMS STAPPAPLQP
     SIRKAKTIPV QAFEVKLDVT LGDLTKIGKS QKFTLSVDVE GGRLVLLRRQ RDSQEDWTTF
     THDRIRQLIK SQRVQNKLGV VFEKEKDRTQ RKDFIFVSAR KREAFCQLLQ LMKNRHSKQD
     EPDMISVFIG TWNMGSVPPP KNVTSWFTSK GLGKALDEVT VTIPHDIYVF GTQENSVGDR
     EWLDLLRGGL KELTDLDYRP IAMQSLWNIK VAVLVKPEHE NRISHVSTSS VKTGIANTLG
     NKGAVGVSFM FNGTSFGFVN CHLTSGNEKT TRRNQNYLDI LRLLSLGDRQ LSAFDISLRF
     THLFWFGDLN YRLDMDIQEI LNYISRREFE PLLRVDQLNL EREKHKVFLR FSEEEISFPP
     TYRYERGSRD TYAWHKQKPT GVRTNVPSWC DRILWKSYPE THIICNSYGC TDDIVTSDHS
     PVFGTFEVGV TSQFISKKGL SKTSDQAYIE FESIEAIVKT ASRTKFFIEF YSTCLEEYKK
     SFENDAQSSD NINFLKVQWS SRQLPTLKPI LADIEYLQDQ HLLLTVKSMD GYESYGECVV
     ALKSMIGSTA QQFLTFLSHR GEETGNIRGS MKVRVPTERL GTRERLYEWI SIDKDDTGAK
     SKVPSVSRGS QEHRSGSRKP ASTETSCPLS KLFEEPEKPP PTGRPPAPPR AVPREEPLNP
     RLKSEGTSEQ EGVAAPPPKN SFNNPAYYVL EGVPHQLLPL EPPSLARAPL PPATKNKVAI
     TVPAPQLGRH RTPRVGEGSS SDEDSGGTLP PPDFPPPPLP DSAIFLPPNL DPLSMPVVRG
     RSGGEARGPP PPKAHPRPPL PPGTSPASTF LGEVASGDDR SCSVLQMAKT LSEVDYAPGP
     GRSALLPNPL ELQPPRGPSD YGRPLSFPPP RIRESIQEDL AEEAPCPQGG RASGLGEAGM
     GAWLRAIGLE RYEEGLVHNG WDDLEFLSDI TEEDLEEAGV QDPAHKRLLL DTLQLSK
//
ID   RRP12_MOUSE             Reviewed;        1295 AA.
AC   Q6P5B0; Q7TMI5; Q80TU2;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=RRP12-like protein;
GN   Name=Rrp12; Synonyms=Kiaa0690;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mesenchymal stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1081, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1081, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity). Nucleus
CC       membrane; Single-pass membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the RRP12 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65628.3; Type=Miscellaneous discrepancy; Note=Intron retention;
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DR   EMBL; AK122346; BAC65628.3; ALT_SEQ; mRNA.
DR   EMBL; BC056232; AAH56232.1; -; mRNA.
DR   EMBL; BC062977; AAH62977.1; -; mRNA.
DR   IPI; IPI00420344; -.
DR   RefSeq; NP_955518.1; NM_199447.2.
DR   UniGene; Mm.276044; -.
DR   ProteinModelPortal; Q6P5B0; -.
DR   SMR; Q6P5B0; 237-265, 327-353, 417-444.
DR   PhosphoSite; Q6P5B0; -.
DR   PRIDE; Q6P5B0; -.
DR   Ensembl; ENSMUST00000038677; ENSMUSP00000039853; ENSMUSG00000035049.
DR   GeneID; 107094; -.
DR   KEGG; mmu:107094; -.
DR   UCSC; uc008hmk.1; mouse.
DR   CTD; 107094; -.
DR   MGI; MGI:2147437; Rrp12.
DR   GeneTree; ENSGT00390000013106; -.
DR   HOGENOM; HBG357519; -.
DR   HOVERGEN; HBG080767; -.
DR   InParanoid; Q6P5B0; -.
DR   OMA; LLCVFFE; -.
DR   OrthoDB; EOG4VMFDK; -.
DR   PhylomeDB; Q6P5B0; -.
DR   NextBio; 358574; -.
DR   ArrayExpress; Q6P5B0; -.
DR   Bgee; Q6P5B0; -.
DR   Genevestigator; Q6P5B0; -.
DR   GermOnline; ENSMUSG00000035049; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR012978; Uncharacterised_NUC173.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 2.
DR   Pfam; PF08161; NUC173; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
PE   1: Evidence at protein level;
KW   Membrane; Nucleus; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1   1295       RRP12-like protein.
FT                                /FTId=PRO_0000050769.
FT   TRANSMEM    904    924       Helical; (Potential).
FT   COMPBIAS   1055   1089       Glu-rich.
FT   MOD_RES      49     49       Phosphoserine (By similarity).
FT   MOD_RES      52     52       Phosphothreonine (By similarity).
FT   MOD_RES      72     72       Phosphoserine (By similarity).
FT   MOD_RES      77     77       Phosphothreonine (By similarity).
FT   MOD_RES    1050   1050       Phosphoserine (By similarity).
FT   MOD_RES    1073   1073       Phosphoserine (By similarity).
FT   MOD_RES    1081   1081       Phosphoserine.
FT   CONFLICT    706    706       E -> G (in Ref. 2; AAH56232).
FT   CONFLICT    732    732       S -> G (in Ref. 1; BAC65628 and 2;
FT                                AAH56232).
FT   CONFLICT   1050   1050       S -> N (in Ref. 2; AAH56232).
SQ   SEQUENCE   1295 AA;  143131 MW;  E662BD4432B43C50 CRC64;
     MGRSGKLPSG VSAKLKRWKK GHSSDSNPAT CRHRQAARSR FFSRPSGKSD LTVDAVKLHN
     ELQSGTLSLG KSQAPETTMD QDPEVAFTEK SSGTFLSGLS DCTNVTFSKV QRFWESNSAA
     HKEICAVLAA VTEVIRSQGG KETETEYFAA LMTTMEAVES PESLAAVAYL LNLVLKRVPS
     PVLMKKFSDT SKAFMDIMSA QASSGSTSAL RWVLSCLAIL LRKQDLEAWG YPITLQVYHG
     LLSFTVHAKP KIRKAAQHGV CSVLKGSDFM FGEKAPAHHP AAVSTAKFCI QEIEKSGGSK
     EATTTLHMLT LLKDMLPCFP EGLVKSCSET LLRVMTLNHV LVTACAMQAF HNLFHAKPSP
     STLSAELNAQ IVTALYDYVP SENDLQPLLA WLKVMEKAHI NLVRLQRDLG LGHLARFFGT
     AVTCLLSPHS QVAAAATQTL KEILKECVAP HIADIGSVTS SASGPPQYIT KMFRAVEEGL
     TYKFHAAWSS VLQLLGVFFE ACGKQAHPVM KKCLQSLCDL RLSPHFPHTA ALDQAVGAAV
     TSMGPEVVLQ AVPLEIDGSE ETLDFPRSWL LPVIRDHVRE TRLGFFTTYF LPLATTLKRK
     AMDLAQAGST VESKIYDTLQ WQIWTLLPGF CTRPTDVAAS FKGLARTLGT AINERPDLRV
     TVCQALRTLI TKGCEAEADR AEVSRFAKNF LPILFNLYGQ PVAAGEAAAP RRAVLETIKT
     YLTITEAQLV NSFLEKATEK VLDPASSDFT RLSVLDLVVA LAPYSDEAAI SKLYSTIRPY
     LESKVHGVQK KAYRVLEEVC ASSQGPAARF VQSHLDDLKK TLLDSLRTTS SPAKRPRLKC
     LIHIVKTLSA EHEEFIAALI PEVILCTKEV SVGARKSAFT LLVEMGHAFL RFGSNQEDAL
     QRYLVLIYPG LLGAVTTVSC SILALTHLLF EFKGLMGTST VEQLLENVCL LLASRTRDVV
     KSALGFIKVA VVVMDVVHLA KHVQLVMEAI GKLSDDMRRH FRMKLRNLFI KFTRKFGFEL
     VKGLLPAEYH KVLINIRKAE TRAKKHRALS QAAVEEEEEE EEEEEPVQSK GDSIEEILAD
     SEDEDEEEER GRGKEQRKLA RQRSRAWLKE GGGDEPLNFL DPKVAHRVLA TQPGPGRGKK
     RDHGFKLSAD GRLIIREEED GNKVEEEDGT KGEDEDMTDA MEDASVRSKK KLKRQREDEE
     DELEIPPRYQ AGGSGIHRPV AKKAAPGAEY KAKKAKGDVK KKGRLDPYAY VPLNRSKLNR
     RKKVKLQGQF KGLVKATQRG SQAGHKLRRK DRRRP
//
ID   Q6P5B5_MOUSE            Unreviewed;       674 AA.
AC   Q6P5B5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   SubName: Full=Fragile X mental retardation, autosomal homolog 2;
GN   Name=Fxr2; Synonyms=Fxr2h; ORFNames=RP23-422L16.5-006;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RA   Pearce A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 2 KH domains.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC057007; AAH57007.1; -; mRNA.
DR   EMBL; BC062971; AAH62971.1; -; mRNA.
DR   EMBL; AK154243; BAE32459.1; -; mRNA.
DR   EMBL; AL603707; CAI51937.1; -; Genomic_DNA.
DR   IPI; IPI00126389; -.
DR   RefSeq; NP_035944.2; NM_011814.2.
DR   UniGene; Mm.41930; -.
DR   ProteinModelPortal; Q6P5B5; -.
DR   SMR; Q6P5B5; 14-144, 229-369.
DR   STRING; Q6P5B5; -.
DR   PRIDE; Q6P5B5; -.
DR   Ensembl; ENSMUST00000018909; ENSMUSP00000018909; ENSMUSG00000018765.
DR   GeneID; 23879; -.
DR   KEGG; mmu:23879; -.
DR   UCSC; uc007jqt.1; mouse.
DR   CTD; 23879; -.
DR   MGI; MGI:1346074; Fxr2.
DR   eggNOG; roNOG11735; -.
DR   HOGENOM; HBG717761; -.
DR   HOVERGEN; HBG005739; -.
DR   InParanoid; Q6P5B5; -.
DR   OMA; DPPTRGE; -.
DR   PhylomeDB; Q6P5B5; -.
DR   NextBio; 303603; -.
DR   ArrayExpress; Q6P5B5; -.
DR   Bgee; Q6P5B5; -.
DR   Genevestigator; Q6P5B5; -.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   InterPro; IPR008395; Agenet.
DR   InterPro; IPR022034; FXR1P_C.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR004088; KH_type_1.
DR   InterPro; IPR018111; KH_type_1_subgr.
DR   Pfam; PF05641; Agenet; 1.
DR   Pfam; PF12235; FXR1P_C; 1.
DR   Pfam; PF00013; KH_1; 2.
DR   SMART; SM00322; KH; 2.
DR   PROSITE; PS50084; KH_TYPE_1; 2.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   674 AA;  74253 MW;  55ECC13AD09EFB34 CRC64;
     MGGLASGGDV EPGLPVEVRG SNGAFYKGFV KDVHEDSVTI FFENNWQSER QIPFGDVRLP
     PPADYNKEIT EGDEVEVYSR ANEQEPCGWW LARVRMMKGD FYVIEYAACD ATYNEIVTLE
     RLRPVNPSPL ATKGSFFKVT MAVPEDLREA CSNENVHKEF KKALGANCIF LNITNSELFI
     LSTTEAPVKR ASLLGDMHFR SLRTKLLLMS RNEEATKHLE TSKQLAAAFQ EEFTVREDLM
     GLAIGTHGAN IQQARKVPGV TAIELGEETC TFRIYGETPE ACRQARSYLE FSEDSVQVPR
     NLVGKVIGKN GKVIQEIVDK SGVVRVRVEG DNDKKNPREE GMVPFIFVGT RENISNAQAL
     LEYHLSYLQE VEQLRLERLQ IDEQLRQIGL GFRPPGSGRG GSGGGSDKAG YTTDESSSSS
     LHTTRTYGGS YGGRGRGRRT GGPAYGPSSD PSTASETESE KREESNRAGP GDRDPPSRGE
     ESRRRPIGGR GRGPPPVPRP TSRYNSSSIS SVLKDPDSNP YSLLDTSEPE PPVDSEPGEP
     PPASARRRRS RRRRTDEDRT VMDGGLESDG PNMTENGLED ESRPQRRNRS RRRRNRGNRT
     DGSISGDRQP VTVADYISRA ESQSRQRPLE RTKPSEDSLS GQKGDSVSKL PKGPSENGEL
     SAPLELGSLV NGVS
//
ID   UGGG1_MOUSE             Reviewed;        1551 AA.
AC   Q6P5E4; Q6NV70;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 3.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=UDP-glucose:glycoprotein glucosyltransferase 1;
DE            Short=UGT1;
DE            EC=2.4.1.-;
DE   AltName: Full=UDP--Glc:glycoprotein glucosyltransferase;
DE   AltName: Full=UDP-glucose ceramide glucosyltransferase-like 1;
DE   Flags: Precursor;
GN   Name=Uggt1; Synonyms=Gt, Ugcgl1, Uggt, Ugt1, Ugtr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and ICR; TISSUE=Brain, and Trophoblast stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   INTERACTION WITH SEP15.
RX   PubMed=11278576; DOI=10.1074/jbc.M009861200;
RA   Korotkov K.V., Kumaraswamy E., Zhou Y., Hatfield D.L., Gladyshev V.N.;
RT   "Association between the 15-kDa selenoprotein and UDP-
RT   glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum
RT   of mammalian cells.";
RL   J. Biol. Chem. 276:15330-15336(2001).
CC   -!- FUNCTION: Recognizes glycoproteins with minor folding defects.
CC       Reglucosylates single N-glycans near the misfolded part of the
CC       protein, thus providing quality control for protein folding in the
CC       endoplasmic reticulum. Reglucosylated proteins are recognized by
CC       calreticulin for recycling to the endoplasmic reticulum and
CC       refolding or degradation (By similarity).
CC   -!- COFACTOR: Calcium (By similarity).
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBUNIT: Monomer as well as in a tight complex with SEP15.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (By similarity).
CC       Endoplasmic reticulum-Golgi intermediate compartment (By
CC       similarity).
CC   -!- DOMAIN: The N-terminal non-catalytic domain is assumed to mediate
CC       recognition of proteins with partial folding defects (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 8 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC062936; AAH62936.1; -; mRNA.
DR   EMBL; BC068283; AAH68283.1; -; mRNA.
DR   IPI; IPI00762897; -.
DR   RefSeq; NP_942602.2; NM_198899.2.
DR   UniGene; Mm.261022; -.
DR   ProteinModelPortal; Q6P5E4; -.
DR   STRING; Q6P5E4; -.
DR   CAZy; GT24; Glycosyltransferase Family 24.
DR   PhosphoSite; Q6P5E4; -.
DR   PRIDE; Q6P5E4; -.
DR   Ensembl; ENSMUST00000046875; ENSMUSP00000037930; ENSMUSG00000037470.
DR   GeneID; 320011; -.
DR   KEGG; mmu:320011; -.
DR   UCSC; uc007app.1; mouse.
DR   CTD; 320011; -.
DR   MGI; MGI:2443162; Uggt1.
DR   eggNOG; roNOG07773; -.
DR   HOGENOM; HBG396631; -.
DR   HOVERGEN; HBG079469; -.
DR   InParanoid; Q6P5E4; -.
DR   OrthoDB; EOG46WZ7H; -.
DR   NextBio; 395857; -.
DR   ArrayExpress; Q6P5E4; -.
DR   Bgee; Q6P5E4; -.
DR   CleanEx; MM_UGCGL1; -.
DR   Genevestigator; Q6P5E4; -.
DR   GermOnline; ENSMUSG00000037470; Mus musculus.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR   GO; GO:0005793; C:ER-Golgi intermediate compartment; ISS:UniProtKB.
DR   GO; GO:0003980; F:UDP-glucose:glycoprotein glucosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0051082; F:unfolded protein binding; ISS:UniProtKB.
DR   GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR   InterPro; IPR009448; UDP-g_GGtrans.
DR   PANTHER; PTHR11226; UDP-g_GGtrans; 1.
DR   Pfam; PF06427; UDP-g_GGTase; 1.
DR   PROSITE; PS00014; ER_TARGET; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW   Phosphoprotein; Signal; Transferase.
FT   SIGNAL        1     42       By similarity.
FT   CHAIN        43   1551       UDP-glucose:glycoprotein
FT                                glucosyltransferase 1.
FT                                /FTId=PRO_0000012272.
FT   REGION     1244   1551       Glucosyltransferase (By similarity).
FT   MOTIF      1548   1551       Prevents secretion from ER (Potential).
FT   MOD_RES     738    738       Phosphoserine (By similarity).
FT   MOD_RES     741    741       Phosphotyrosine (By similarity).
FT   MOD_RES     748    748       Phosphoserine (By similarity).
FT   CARBOHYD    269    269       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    536    536       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1228   1228       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    319    319       K -> E (in Ref. 1; AAH68283).
FT   CONFLICT    445    445       S -> F (in Ref. 1; AAH68283).
FT   CONFLICT    824    824       S -> N (in Ref. 1; AAH68283).
FT   CONFLICT    935    935       Q -> R (in Ref. 1; AAH68283).
FT   CONFLICT   1015   1015       N -> T (in Ref. 1; AAH68283).
FT   CONFLICT   1058   1058       I -> T (in Ref. 1; AAH68283).
FT   CONFLICT   1083   1083       Q -> E (in Ref. 1; AAH68283).
FT   CONFLICT   1212   1212       K -> R (in Ref. 1; AAH68283).
SQ   SEQUENCE   1551 AA;  176433 MW;  6B7D3327ED851396 CRC64;
     MCSRGDANTA DAAAARRVTG LRYNMRLLIA LALPCLFSLA EANSKAITTS LTTKWFSAPL
     LLEASEFLAE DSQEKFWSFV EATQNIGSSD HHDTDHSYYD AVLEAAFRFL SPLQQNLLKF
     CLSLRSYSAS IQAFQQIAVD EPPPEGCKSF LSVHGKQTCD LDTLESLLLT AADRPKPLLF
     KGDHRYPSSN PESPVVILYS EIGHEEFSNI HHQLISKSNE GKINYVFRHY ISNPSKEPVY
     LSGYGVELAI KSTEYKAKDD TQVKGTEVNA TVIGESDPID EVQGFLFGKL RELYPALEGQ
     LKEFRKHLVE STNEMAPLKV WQLQDLSFQT AARILAASGA LSLVVMKDIS QNFPTKARAI
     TKTAVSAQLR AEVEENQKYF KGTIGLQPGD SALFINGLHI DLDTQDIFSL FDTLRNEARV
     MEGLHRLGIE GLSLHNILKL NIQPSETDYA VDIRSPAISW VNNLEVDSRY NSWPSSLQEL
     LRPTFPGVIR QIRKNLHNMV FIIDPVHETT AELISIAEMF LSNHIPLRIG FIFVVNDSED
     VDGMQDAGVA VLRAYNYVAQ EVDGYHAFQT LTQIYNKVRT GETVKVEHVV SVLEKKYPYV
     EVNSILGIDS AYDQNRKEAR GYYEQTGVGP LPVVLFNGMP FEKEQLDPDE LETITMHKIL
     ETTTFFQRAV YLGELSHDQD VVEYIMNQPN VVPRINSRIL TAKREYLDLT ASNNFYVDDF
     ARFSALDSRG KTAAIANSMN YLTKKGMSSK EIYDDSFIRP VTFWIVGDFD SPSGRQLLYD
     AIKHQKTSNN VRISMINNPS QEISDSSTPI FRAIWAALQT QASSSAKNFI TKMAKEETAE
     ALAAGVDIAE FSVGGMDVSL FKEVFESSRM DFILSHALYC RDVLKLKKGQ RVVISNGRII
     GPLEDNELFN QDDFHLLENI ILKTSGQKIK SHIQQLRVEE DVASDLVMKV DALLSAQPKG
     EARIEYQFFE DKHSAIKLKP KEGETYYDVV AVVDPVTREA QRLAPLLLVL TQLINMNLRV
     FMNCQSKLSD MPLKSFYRYV LEPEISFTAD SSFAKGPIAK FLDMPQSPLF TLNLNTPESW
     MVQSVRTPYD LDNIYLEEVD SIVAAEYELE YLLLEGHCYD ITTGQPPRGL QFTLGTSANP
     TIVDTIVMAN LGYFQLKANP GAWILRLRKG RSDDIYRIYS HDGTDSPPDA NDVVVILNNF
     KSKIIKVKVQ KKADMANEDL LSDGTNENES GFWDSFKWGF SGQKAEEVKQ DKDDIINIFS
     VASGHLYERF LRIMMLSVLK NTKTPVKFWF LKNYLSPTFK EFIPYMAKKY NFQYELVQYK
     WPRWLHQQTE KQRIIWGYKI LFLDVLFPLV VDKFLFVDAD QIVRTDLKEL RDFNLDGAPY
     GYTPFCDSRR EMDGYRFWKS GYWASHLAGR KYHISALYVV DLKKFRKIAA GDRLRGQYQG
     LSQDPNSLSN LDQDLPNNMI HQVPIKSLPQ EWLWCETWCD DASKKRAKTI DLCNNPMTKE
     PKLEAAVRIV PEWQDYDQEI KQLQTLFQEE KELGTLHTEE TQEGSQKHEE L
//
ID   DGKQ_MOUSE              Reviewed;         934 AA.
AC   Q6P5E8; Q3UYE8;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Diacylglycerol kinase theta;
DE            Short=DAG kinase theta;
DE            EC=2.7.1.107;
DE   AltName: Full=Diglyceride kinase theta;
DE            Short=DGK-theta;
GN   Name=Dgkq;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-26, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Phosphorylates diacylglycerol (DAG) to generate
CC       phosphatidic acid (PA). May regulate the activity of protein
CC       kinase C by controlling the balance between these two signaling
CC       lipids. Activated in the nucleus in response to alpha-thrombin and
CC       nerve growth factor (By similarity). May be involved in cAMP-
CC       induced activation of NR5A1 and subsequent steroidogenic gene
CC       transcription by delivering PA as ligand for NR5A1. Acts
CC       synergistically with NR5A1 on CYP17 transcriptional activity (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-
CC       sn-glycerol 3-phosphate.
CC   -!- ENZYME REGULATION: Inactivated by binding to RHOA. Not inhibited
CC       by phosphatidylserine (By similarity).
CC   -!- SUBUNIT: Interacts with RHOA (constitutively activated, GTP-
CC       bound); the interaction inhibits DGKQ. Interacts with PRKCE.
CC       Interacts with PRKCH. Interacts with PLCB1. Interacts with NR5A1
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By
CC       similarity). Cytoplasm, cytoskeleton (By similarity). Nucleus (By
CC       similarity). Nucleus speckle (By similarity). Note=Translocates to
CC       the nucleus in response to thrombin stimulation (By similarity).
CC       Translocates to the plasma membrane in response to steroid hormone
CC       receptor stimulation (By similarity). Translocation to the plasma
CC       membrane is dependent on G-protein coupled receptor stimulation
CC       and subsequent activation of PRKCE and probably PRKCH (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6P5E8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6P5E8-2; Sequence=VSP_037832;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated by PRKCE and PRKCH in vitro (By similarity).
CC   -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase
CC       family.
CC   -!- SIMILARITY: Contains 1 DAGKc domain.
CC   -!- SIMILARITY: Contains 3 phorbol-ester/DAG-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 Ras-associating domain.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK134745; BAE22264.1; -; mRNA.
DR   EMBL; BC062929; AAH62929.1; -; mRNA.
DR   IPI; IPI00396685; -.
DR   IPI; IPI00944172; -.
DR   RefSeq; NP_950176.1; NM_199011.1.
DR   UniGene; Mm.260921; -.
DR   HSSP; Q16760; 1R79.
DR   ProteinModelPortal; Q6P5E8; -.
DR   SMR; Q6P5E8; 49-106, 114-163, 176-229.
DR   STRING; Q6P5E8; -.
DR   PhosphoSite; Q6P5E8; -.
DR   PRIDE; Q6P5E8; -.
DR   Ensembl; ENSMUST00000053913; ENSMUSP00000057859; ENSMUSG00000004815.
DR   GeneID; 110524; -.
DR   KEGG; mmu:110524; -.
DR   UCSC; uc008yot.1; mouse.
DR   CTD; 110524; -.
DR   MGI; MGI:102918; Dgkq.
DR   HOGENOM; HBG315413; -.
DR   InParanoid; Q6P5E8; -.
DR   OMA; VCELHVH; -.
DR   OrthoDB; EOG49KFPV; -.
DR   PhylomeDB; Q6P5E8; -.
DR   NextBio; 364149; -.
DR   ArrayExpress; Q6P5E8; -.
DR   Bgee; Q6P5E8; -.
DR   Genevestigator; Q6P5E8; -.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004143; F:diacylglycerol kinase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007205; P:activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway; IEA:InterPro.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000159; Ras-assoc.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00609; DAGK_acc; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   Pfam; PF00788; RA; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 3.
DR   SMART; SM00045; DAGKa; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SMART; SM00314; RA; 1.
DR   PROSITE; PS50146; DAGK; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 3.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell membrane; Cytoplasm;
KW   Cytoskeleton; Kinase; Membrane; Metal-binding; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Repeat; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    934       Diacylglycerol kinase theta.
FT                                /FTId=PRO_0000381763.
FT   DOMAIN      387    486       Ras-associating.
FT   DOMAIN      576    713       DAGKc.
FT   ZN_FING      54    102       Phorbol-ester/DAG-type 1.
FT   ZN_FING     115    162       Phorbol-ester/DAG-type 2.
FT   ZN_FING     177    228       Phorbol-ester/DAG-type 3.
FT   MOD_RES      22     22       Phosphoserine.
FT   MOD_RES      26     26       Phosphoserine.
FT   VAR_SEQ       1    548       Missing (in isoform 2).
FT                                /FTId=VSP_037832.
SQ   SEQUENCE   934 AA;  102254 MW;  C7FA90936443818E CRC64;
     MAAAAEPGAR TWPGSGSPRL GSPAGSPVLG ISGRTRPGSG PERTSRAIGS AAPGHSFRKV
     TLTKPTFCHL CSDFIWGLAG FLCDVCNFMS HEKCLKQVKT PCTSIAPSLV RVPVAHCFGS
     LGLYKRKFCV VCRKSLEVPA FRCEVCELHV HPDCVPFACS DCRQCHQDGQ QDYDTYHHHW
     REGNLPSGAR CEVCRKTCGS SDVLAGVRCE WCGVQAHSVC STALAPECTF GRLRSMVLPP
     SCVRLLSRNF SKMHCFRIPE TMVLELGDGD DGVDGSAAIG TGREVLTATE STKQTLKIFD
     GNDSMRKNQF RLVTVSRLAR NEEVMEAALR AYYISEDPKD FQLQALPLSG NAQALGKAGT
     TEEEASKGSC PRDSVPEAWV IRSLPRTQEI LKIYPGWLKV GVAYVSIRVN SQSTARSVVQ
     EVLPLFGQQV EDKERFQLIE VLMSSRQVQR TVLADEEPLL DRLWDIRQTS VRQVSQTRFY
     VAETRATAPR VSLFVGGLPP GLSPQDYSNL LHEAMATKAA VVSVSHVYSL QGAVILDVTC
     FAEAERLYML ARDTAVHGRP LTALVLPDVL HTKLPPDCCP LLVFVNPKSG GLKGRELLCS
     FRKLLNPHQV FELTNGGPLP GFHLFSQVPS FRVLVCGGDG TVGWVLAALE ETRRHLACPE
     PSVAILPLGT GNDLGRVLRW GAGYSGEDPF SVLVSVDEAD AVLMDRWTIL LDAHEIDSTE
     NNVVETEPPK IVQMNNYCGI GIDAELSLDF HQAREEEPGK FTSRFHNKGV YVRVGLQKIS
     HSRSLHKEIR LQVEQQEVEL PSIEGLIFIN IPSWGSGADL WGSDNDSRFE KPRIDDGLLE
     VVGVTGVVHM GQVQGGLRSG IRIAQGSYFR VTLLKATPVQ VDGEPWVQAP GHMIISATAP
     KVHMLRKAKQ KPRKAGANRD TRVDTLPAPE GNPL
//
ID   S39AA_MOUSE             Reviewed;         833 AA.
AC   Q6P5F6; Q80TG2; Q8BX42; Q8C0L2;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Zinc transporter ZIP10;
DE   AltName: Full=Solute carrier family 39 member 10;
DE   AltName: Full=Zrt- and Irt-like protein 10;
DE            Short=ZIP-10;
DE   Flags: Precursor;
GN   Name=Slc39a10; Synonyms=Kiaa1265, Zip10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Egg;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 173-833.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 403-833.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-593, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-198 AND ASN-218, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-198; ASN-218 AND ASN-341,
RP   AND MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: May act as a zinc-influx transporter (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH59214.1; Type=Erroneous initiation;
CC       Sequence=BAC33542.1; Type=Erroneous initiation;
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DR   EMBL; BC052880; AAH52880.1; -; mRNA.
DR   EMBL; BC059214; AAH59214.1; ALT_INIT; mRNA.
DR   EMBL; BC062918; AAH62918.1; -; mRNA.
DR   EMBL; AK122483; BAC65765.1; -; mRNA.
DR   EMBL; AK030685; BAC27077.1; -; mRNA.
DR   EMBL; AK049099; BAC33542.1; ALT_INIT; mRNA.
DR   IPI; IPI00273801; -.
DR   RefSeq; NP_766241.2; NM_172653.2.
DR   UniGene; Mm.233889; -.
DR   ProteinModelPortal; Q6P5F6; -.
DR   STRING; Q6P5F6; -.
DR   PhosphoSite; Q6P5F6; -.
DR   PRIDE; Q6P5F6; -.
DR   Ensembl; ENSMUST00000027131; ENSMUSP00000027131; ENSMUSG00000025986.
DR   GeneID; 227059; -.
DR   KEGG; mmu:227059; -.
DR   UCSC; uc007axc.1; mouse.
DR   CTD; 227059; -.
DR   MGI; MGI:1914515; Slc39a10.
DR   eggNOG; roNOG05260; -.
DR   GeneTree; ENSGT00550000074174; -.
DR   HOGENOM; HBG443965; -.
DR   HOVERGEN; HBG055748; -.
DR   InParanoid; Q6P5F6; -.
DR   OMA; IKVVEIN; -.
DR   OrthoDB; EOG47SSD5; -.
DR   PhylomeDB; Q6P5F6; -.
DR   NextBio; 378450; -.
DR   ArrayExpress; Q6P5F6; -.
DR   Bgee; Q6P5F6; -.
DR   Genevestigator; Q6P5F6; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046873; F:metal ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0006829; P:zinc ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR003689; ZIP.
DR   Pfam; PF02535; Zip; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Ion transport; Membrane; Phosphoprotein; Signal;
KW   Transmembrane; Transmembrane helix; Transport; Zinc; Zinc transport.
FT   SIGNAL        1     25       Potential.
FT   CHAIN        26    833       Zinc transporter ZIP10.
FT                                /FTId=PRO_0000297633.
FT   TRANSMEM    413    433       Helical; (Potential).
FT   TRANSMEM    440    460       Helical; (Potential).
FT   TRANSMEM    497    517       Helical; (Potential).
FT   TRANSMEM    689    709       Helical; (Potential).
FT   TRANSMEM    734    754       Helical; (Potential).
FT   TRANSMEM    761    781       Helical; (Potential).
FT   TRANSMEM    803    823       Helical; (Potential).
FT   COMPBIAS     26     40       His-rich.
FT   COMPBIAS    101    294       His-rich.
FT   COMPBIAS    460    485       His-rich.
FT   COMPBIAS    609    658       His-rich.
FT   MOD_RES     548    548       Phosphoserine (By similarity).
FT   MOD_RES     555    555       Phosphothreonine (By similarity).
FT   MOD_RES     593    593       Phosphoserine.
FT   CARBOHYD    191    191       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    198    198       N-linked (GlcNAc...).
FT   CARBOHYD    218    218       N-linked (GlcNAc...).
FT   CARBOHYD    341    341       N-linked (GlcNAc...).
FT   CONFLICT    346    346       L -> S (in Ref. 2; BAC65765).
FT   CONFLICT    676    676       I -> F (in Ref. 3; BAC27077).
FT   CONFLICT    829    829       F -> Y (in Ref. 2; BAC65765).
SQ   SEQUENCE   833 AA;  94394 MW;  BA51B66A2296AFC2 CRC64;
     MKVHIHTKFC LICLLTFIFH HCNHCHEDHD HGPEELHRHH RGMTESESSK FSVQDAENEK
     KYYIEKLFDR YGENGRLSFF GLEKLLTNLG LGEIKVVEIN HEDLGHDHVS HLDILAVQEG
     KHFHSHTHQH FHNHLNAENH TTTSVTSKRN HKCDPEKEAA ELPIKADDKH LHDRNHRFHH
     RHRLHHHLDH NTTRHVHNDS VAHSEHGEPG HSPSPETNKT QEQSEVKSVK VRRKEKGKRK
     KENSEVNTPG FLPNHDHSEQ YEHNRVHKLD RVHSPGHPHA HLPEHSGHEL GHGHQELDPD
     NEGELRHTRK REAPHVRKSA IYSTPSHKDQ SEDDRQHECL NVTQLLKHFG LGPNSPISPD
     LFTYLCPALL YQIDSRLCIE HFDKLLVEDL NKDKTLVPED KTNIGASAWI CGIISITVIS
     LLSLLGVILV PIINQGCFKF LLTFLVALAV GTMSGDALLH LLPHSQGGHD HSHQHTHGHG
     HSHGHESKEF LEEYDAVLKG LVALGGIYLL FIIEHCIRMF KHYKQQRGKQ KWFMKQSTEE
     STIGRKLSDH KLNSTPDADW LQLKPLAGTD DSVVSEDRLN ETELTDLEAQ QESPPKNYLG
     VEEEKIMDHS HSDGLHTIHE HEVHVTSHNH HDEDKAVLRK HSHQWHHRHA HHSHGPCHSG
     SDLKETGIAN IAWMVIMGDG IHNFSDGLAI GAAFSAGLTG GISTSIAVFC HELPHELGDF
     AVLLKAGMTV KQAIVYNLLS AMMAYIGMLI GTAVGQYANN ITLWIFAITA GMFLYVALVD
     MLPEMLHGDG DHEEHGFCPV GQFILQNLGL LFGFAIMLVI ALYEDKIVFD IQF
//
ID   TTYH3_MOUSE             Reviewed;         524 AA.
AC   Q6P5F7; Q69ZD3; Q6PCX0; Q8C789;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Protein tweety homolog 3;
DE            Short=mTTY3;
GN   Name=Ttyh3; Synonyms=Kiaa1691;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 139-524 (ISOFORM 1).
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=15010458; DOI=10.1074/jbc.M313813200;
RA   Suzuki M., Mizuno A.;
RT   "A novel human Cl(-) channel family related to Drosophila flightless
RT   locus.";
RL   J. Biol. Chem. 279:22461-22468(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-504, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Probable large-conductance Ca(2+)-activated chloride
CC       channel. May play a role in Ca(2+) signal transduction (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6P5F7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6P5F7-2; Sequence=VSP_029771, VSP_029772;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in excitable tissues. Expressed in
CC       the brain, heart, skeletal muscle, colon, spleen, kidney and
CC       peripheral blood leukocytes. Also expressed in fat, the pancreas,
CC       thymus, and uterus.
CC   -!- PTM: N-glycosylated (By similarity).
CC   -!- SIMILARITY: Belongs to the tweety family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH59083.1; Type=Erroneous termination; Positions=294; Note=Translated as Gln;
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DR   EMBL; AK052340; BAC34944.1; -; mRNA.
DR   EMBL; BC059083; AAH59083.1; ALT_SEQ; mRNA.
DR   EMBL; BC062917; AAH62917.1; -; mRNA.
DR   EMBL; AK173233; BAD32511.1; -; mRNA.
DR   IPI; IPI00226563; -.
DR   IPI; IPI00877256; -.
DR   RefSeq; NP_780483.2; NM_175274.4.
DR   UniGene; Mm.28947; -.
DR   PhosphoSite; Q6P5F7; -.
DR   PRIDE; Q6P5F7; -.
DR   Ensembl; ENSMUST00000042661; ENSMUSP00000037447; ENSMUSG00000036565.
DR   GeneID; 78339; -.
DR   KEGG; mmu:78339; -.
DR   UCSC; uc009ahw.1; mouse.
DR   CTD; 78339; -.
DR   MGI; MGI:1925589; Ttyh3.
DR   eggNOG; roNOG06043; -.
DR   GeneTree; ENSGT00390000010182; -.
DR   HOGENOM; HBG446200; -.
DR   HOVERGEN; HBG108621; -.
DR   InParanoid; Q6P5F7; -.
DR   OMA; PEDTDYQ; -.
DR   OrthoDB; EOG4DJJWC; -.
DR   PhylomeDB; Q6P5F7; -.
DR   NextBio; 348727; -.
DR   ArrayExpress; Q6P5F7; -.
DR   Bgee; Q6P5F7; -.
DR   CleanEx; MM_TTYH3; -.
DR   Genevestigator; Q6P5F7; -.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   InterPro; IPR006990; Tweety.
DR   PANTHER; PTHR12424; Tweety; 1.
DR   Pfam; PF04906; Tweety; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell membrane; Chloride;
KW   Chloride channel; Glycoprotein; Ion transport; Ionic channel;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    524       Protein tweety homolog 3.
FT                                /FTId=PRO_0000312252.
FT   TOPO_DOM      1     42       Extracellular (Potential).
FT   TRANSMEM     43     63       Helical; Name=1; (Potential).
FT   TOPO_DOM     64     86       Cytoplasmic (Potential).
FT   TRANSMEM     87    107       Helical; Name=2; (Potential).
FT   TOPO_DOM    108    211       Extracellular (Potential).
FT   TRANSMEM    212    232       Helical; Name=3; (Potential).
FT   TOPO_DOM    233    236       Cytoplasmic (Potential).
FT   TRANSMEM    237    257       Helical; Name=4; (Potential).
FT   TOPO_DOM    258    386       Extracellular (Potential).
FT   TRANSMEM    387    407       Helical; Name=5; (Potential).
FT   TOPO_DOM    408    524       Cytoplasmic (Potential).
FT   MOD_RES     504    504       Phosphoserine.
FT   MOD_RES     519    519       Phosphoserine (By similarity).
FT   MOD_RES     522    522       Phosphoserine (By similarity).
FT   CARBOHYD    126    126       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    144    144       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    351    351       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     475    479       MSQNA -> ITPPA (in isoform 2).
FT                                /FTId=VSP_029771.
FT   VAR_SEQ     480    524       Missing (in isoform 2).
FT                                /FTId=VSP_029772.
FT   CONFLICT     60     60       F -> L (in Ref. 1; BAC34944).
SQ   SEQUENCE   524 AA;  57714 MW;  95B499209DBC6D51 CRC64;
     MAGVSYAAPW WVSLLHRLPH FDLRWEATSS QFRPEDADYQ QALLLLGATA LACLALDLLF
     LLFYSFWLCC RRRKTDEHLD ADCCCTAWCV IITTLVCSAG IAVGFYGNGE TSDGIHRATY
     SLRHANRTVA GVQDRVWDTA AALNRTAEPN LQSLERQLAG RQEPLRAVQR LQTLLGTLLG
     YTAAIPFWRN PGVSLEVLAE QVDLYDWYRW LGYLGLLLLD VIICLLVLVG LIRSSKGILV
     GVCLLGVLAL VISWGALGLE LAVSVGSSDF CVDPDTFVTK MVEEHSVLSG DILQYYLACS
     PRATNPFQQK LSGSHKALVE MQDVVAELLR NVPREHPATK DPLLRVQEVL NGTEVNLQHL
     TALVDCRSLH LDYVQALTGF CYDGVEGLIY LALFSFVTAL MFSSIVCSIP HTWQQKRGPD
     DDGEEETAPG PRQAHDSLYR VHMPSLYSCG SSYGSEASIP AAAHTVSNAP VTEYMSQNAN
     FQNPRCENTP LIGRESPPPS YTSSMRAKYL ATSQPRPDSS GSGH
//
ID   MK04_MOUSE              Reviewed;         583 AA.
AC   Q6P5G0;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Mitogen-activated protein kinase 4;
DE            Short=MAP kinase 4;
DE            Short=MAPK 4;
DE            EC=2.7.11.24;
DE   AltName: Full=Extracellular signal-regulated kinase 4;
DE            Short=ERK-4;
GN   Name=Mapk4; Synonyms=Erk4, Prkm4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Phosphorylates microtubule-associated protein 2 (MAP2).
CC       May promote entry in the cell cycle (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. MAP kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; BC058942; AAH58942.1; -; mRNA.
DR   EMBL; BC062911; AAH62911.1; -; mRNA.
DR   IPI; IPI00453690; -.
DR   RefSeq; NP_766220.2; NM_172632.2.
DR   UniGene; Mm.254517; -.
DR   ProteinModelPortal; Q6P5G0; -.
DR   SMR; Q6P5G0; 13-316.
DR   PhosphoSite; Q6P5G0; -.
DR   PRIDE; Q6P5G0; -.
DR   Ensembl; ENSMUST00000091851; ENSMUSP00000089462; ENSMUSG00000024558.
DR   GeneID; 225724; -.
DR   KEGG; mmu:225724; -.
DR   UCSC; uc008fpb.1; mouse.
DR   CTD; 225724; -.
DR   MGI; MGI:2444559; Mapk4.
DR   GeneTree; ENSGT00550000074298; -.
DR   HOGENOM; HBG507122; -.
DR   HOVERGEN; HBG104376; -.
DR   InParanoid; Q6P5G0; -.
DR   OMA; EKGDCIA; -.
DR   OrthoDB; EOG4PG60R; -.
DR   PhylomeDB; Q6P5G0; -.
DR   BRENDA; 2.7.11.24; 244.
DR   NextBio; 377772; -.
DR   ArrayExpress; Q6P5G0; -.
DR   Bgee; Q6P5G0; -.
DR   CleanEx; MM_MAPK4; -.
DR   Genevestigator; Q6P5G0; -.
DR   GermOnline; ENSMUSG00000024558; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004707; F:MAP kinase activity; IEA:EC.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR008350; Erk_3_4_MAPK.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01771; ERK3ERK4MAPK.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    583       Mitogen-activated protein kinase 4.
FT                                /FTId=PRO_0000186255.
FT   DOMAIN       20    312       Protein kinase.
FT   NP_BIND      26     34       ATP (By similarity).
FT   ACT_SITE    149    149       Proton acceptor (By similarity).
FT   BINDING      49     49       ATP (By similarity).
FT   MOD_RES     186    186       Phosphoserine (By similarity).
SQ   SEQUENCE   583 AA;  65574 MW;  7CE7B2D5359CB52A CRC64;
     MAEKGDCIAS VYGYDLGGRF IDFQPLGFGV NGLVLSATDS RACRKVAVKK IVLSDARSMK
     HALREIKIIR RLDHDNIVKV YEVLGPKGSD LQGELFKFSV AYIVQEYMET DLACLLEQGT
     LTEDHAKLFM YQLLRGLKYI HSANVLHRDL KPANIFISTE DLVLKIGDFG LARIVDQHYS
     HKGYLSEGLV TKWYRSPRLL LSPNNYTKAI DMWAAGCILA EMLTGKMLFA GAHELEQMQL
     ILDTIPVVRE EDKEELLRVM PSFVSSTWEV KRPLRKLLPD VNSEAIDFLE KILTFNPMDR
     LTAEMGLQHP YMSPYSCPED EPTSQHPFRI EDEIDDIVLM AASQSQLSNW DRYPVSLSSD
     LEWRPDRCQD ASEVQRDPRA GSTPLAEDVQ VDPRKDSQSS SERFLEQSHS SMERAFEADY
     GRSCDYKVGS PSYLDKLLWR DNKPHHYSEP KLILDLSHWK QAASAPPRAA VAADPVSRED
     EPASLFLEIA QWVKSTQSGS ERASPPPDAP EPRLSASPPG HPTPIDGGAS PQFDLDVFIS
     RALKLCTKPE DLPENKLGDL NGACISEHPG DLVQTEAFSK ERW
//
ID   NEST_MOUSE              Reviewed;        1864 AA.
AC   Q6P5H2; A1E2I2; Q80X00; Q8BPH7; Q9CV43; Q9R0C4;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Nestin;
GN   Name=Nes;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=BALB/c;
RX   MEDLINE=20302580; PubMed=10842089; DOI=10.1016/S0925-4773(00)00301-4;
RA   Yang J., Bian W., Gao X., Chen L., Jing N.;
RT   "Nestin expression during mouse eye and lens development.";
RL   Mech. Dev. 94:287-291(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-764 AND 1510-1864.
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 33-57.
RC   TISSUE=Heart;
RX   MEDLINE=95348496; PubMed=7542682;
RA   Kachinsky A.M., Dominov J.A., Miller J.B.;
RT   "Intermediate filaments in cardiac myogenesis: nestin in the
RT   developing mouse heart.";
RL   J. Histochem. Cytochem. 43:843-847(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1358-1514.
RC   STRAIN=VM;
RA   Huysentruyt L.C., Banerjee D., Seyfried T.N.;
RT   "Novel metastatic mouse tumor cells express multiple properties of
RT   macrophages.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1541, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20963821; DOI=10.1002/stem.541;
RA   Park D., Xiang A.P., Mao F.F., Zhang L., Di C.G., Liu X.M., Shao Y.,
RA   Ma B.F., Lee J.H., Ha K.S., Walton N., Lahn B.T.;
RT   "Nestin is required for the proper self-renewal of neural stem
RT   cells.";
RL   Stem Cells 28:2162-2171(2010).
CC   -!- FUNCTION: Required for brain and eye development. Promotes the
CC       disassembly of phosphorylated vimentin intermediate filaments (IF)
CC       during mitosis and may play a role in the trafficking and
CC       distribution of IF proteins and other cellular factors to daughter
CC       cells during progenitor cell division (By similarity). Required
CC       for survival, renewal and mitogen-stimulated proliferation of
CC       neural progenitor cells.
CC   -!- SUBUNIT: Forms homodimers and homotetramers in vitro. In mixtures
CC       with other intermediate filament proteins such as vimentin and
CC       alpha-internexin, this protein preferentially forms heterodimers
CC       which can assemble to form intermediate filaments if nestin does
CC       not exceed 25%. Interacts with FHOD3 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6P5H2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6P5H2-2; Sequence=VSP_024923;
CC   -!- PTM: Phosphorylated at Thr-316. This increases during mitosis when
CC       the cytoplasmic intermediate filament network is reorganized (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Embryonic lethality with the neuroepithelium
CC       of developing neural tube exhibiting low numbers of neural stem
CC       cells and high levels of apoptosis. No effect on cytoskeletal
CC       integrity.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF076623; AAF04456.2; -; mRNA.
DR   EMBL; BC060693; AAH60693.1; -; mRNA.
DR   EMBL; BC062893; AAH62893.1; -; mRNA.
DR   EMBL; AK009706; BAB26451.1; -; mRNA.
DR   EMBL; AK075690; BAC35892.1; -; mRNA.
DR   EMBL; S78708; AAP32014.1; -; mRNA.
DR   EMBL; EF101559; ABK96808.1; -; mRNA.
DR   IPI; IPI00453692; -.
DR   IPI; IPI00845608; -.
DR   RefSeq; NP_057910.3; NM_016701.3.
DR   UniGene; Mm.331129; -.
DR   ProteinModelPortal; Q6P5H2; -.
DR   SMR; Q6P5H2; 6-43, 47-154, 232-311.
DR   STRING; Q6P5H2; -.
DR   PhosphoSite; Q6P5H2; -.
DR   PRIDE; Q6P5H2; -.
DR   Ensembl; ENSMUST00000090973; ENSMUSP00000088493; ENSMUSG00000004891.
DR   GeneID; 18008; -.
DR   KEGG; mmu:18008; -.
DR   UCSC; uc008ptn.1; mouse.
DR   CTD; 18008; -.
DR   MGI; MGI:101784; Nes.
DR   eggNOG; roNOG13430; -.
DR   HOGENOM; HBG126246; -.
DR   HOVERGEN; HBG006463; -.
DR   InParanoid; Q6P5H2; -.
DR   OMA; EDQKELD; -.
DR   OrthoDB; EOG49GKHK; -.
DR   NextBio; 293025; -.
DR   ArrayExpress; Q6P5H2; -.
DR   Bgee; Q6P5H2; -.
DR   CleanEx; MM_NES; -.
DR   Genevestigator; Q6P5H2; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005882; C:intermediate filament; IDA:MGI.
DR   GO; GO:0019215; F:intermediate filament binding; ISS:UniProtKB.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR   GO; GO:0048858; P:cell projection morphogenesis; IMP:MGI.
DR   GO; GO:0031076; P:embryonic camera-type eye development; ISS:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptosis; IMP:UniProtKB.
DR   GO; GO:0030844; P:positive regulation of intermediate filament depolymerization; ISS:UniProtKB.
DR   GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISS:UniProtKB.
DR   InterPro; IPR016044; F.
DR   InterPro; IPR001664; IF.
DR   InterPro; IPR018039; Intermediate_filament_CS.
DR   PANTHER; PTHR23239; IF; 1.
DR   Pfam; PF00038; Filament; 1.
DR   PROSITE; PS00226; IF; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Developmental protein;
KW   Intermediate filament; Neurogenesis; Phosphoprotein.
FT   CHAIN         1   1864       Nestin.
FT                                /FTId=PRO_0000285856.
FT   REGION        1      7       Head.
FT   REGION        8    314       Rod.
FT   REGION        8     43       Coil 1A.
FT   REGION       44     55       Linker 1.
FT   REGION       56    151       Coil 1B.
FT   REGION      152    174       Linker 12.
FT   REGION      175    193       Coil 2A.
FT   REGION      194    196       Linker 2.
FT   REGION      197    314       Coil 2B.
FT   REGION      315   1864       Tail.
FT   MOD_RES     312    312       Phosphoserine (By similarity).
FT   MOD_RES     316    316       Phosphothreonine (By similarity).
FT   MOD_RES     321    321       Phosphoserine (By similarity).
FT   MOD_RES     355    355       Phosphothreonine (By similarity).
FT   MOD_RES     385    385       Phosphothreonine (By similarity).
FT   MOD_RES     389    389       Phosphothreonine (By similarity).
FT   MOD_RES     565    565       Phosphoserine (By similarity).
FT   MOD_RES     575    575       Phosphoserine (By similarity).
FT   MOD_RES     688    688       Phosphoserine.
FT   MOD_RES     862    862       Phosphoserine (By similarity).
FT   MOD_RES    1010   1010       Phosphoserine (By similarity).
FT   MOD_RES    1032   1032       Phosphoserine (By similarity).
FT   MOD_RES    1127   1127       Phosphoserine (By similarity).
FT   MOD_RES    1188   1188       Phosphoserine (By similarity).
FT   MOD_RES    1541   1541       Phosphoserine.
FT   MOD_RES    1656   1656       Phosphoserine (By similarity).
FT   MOD_RES    1665   1665       Phosphoserine (By similarity).
FT   MOD_RES    1858   1858       Phosphoserine (By similarity).
FT   MOD_RES    1860   1860       Phosphoserine (By similarity).
FT   MOD_RES    1861   1861       Phosphoserine (By similarity).
FT   VAR_SEQ     750    793       Missing (in isoform 2).
FT                                /FTId=VSP_024923.
FT   CONFLICT    184    184       G -> C (in Ref. 1; AAF04456).
FT   CONFLICT    257    257       A -> P (in Ref. 1; AAF04456).
FT   CONFLICT    265    265       V -> L (in Ref. 1; AAF04456).
FT   CONFLICT    319    319       R -> G (in Ref. 1; AAF04456).
FT   CONFLICT    458    458       T -> S (in Ref. 1; AAF04456).
FT   CONFLICT    535    535       M -> K (in Ref. 1; AAF04456).
FT   CONFLICT    544    544       E -> K (in Ref. 1; AAF04456).
FT   CONFLICT    558    558       G -> R (in Ref. 1; AAF04456).
FT   CONFLICT    570    570       S -> L (in Ref. 1; AAF04456).
FT   CONFLICT    587    587       L -> S (in Ref. 1; AAF04456).
FT   CONFLICT    673    673       M -> I (in Ref. 1; AAF04456).
FT   CONFLICT    704    704       Q -> L (in Ref. 1; AAF04456).
FT   CONFLICT    734    734       E -> D (in Ref. 1; AAF04456).
FT   CONFLICT    851    851       L -> P (in Ref. 1; AAF04456).
FT   CONFLICT    855    855       K -> R (in Ref. 1; AAF04456).
FT   CONFLICT    900    900       E -> D (in Ref. 1; AAF04456).
FT   CONFLICT   1008   1011       RKSL -> GKFF (in Ref. 1; AAF04456).
FT   CONFLICT   1021   1021       S -> F (in Ref. 1; AAF04456).
FT   CONFLICT   1157   1157       C -> S (in Ref. 1; AAF04456).
FT   CONFLICT   1241   1241       E -> EV (in Ref. 1; AAF04456).
FT   CONFLICT   1382   1382       G -> A (in Ref. 5; ABK96808).
FT   CONFLICT   1404   1404       A -> T (in Ref. 1; AAF04456).
FT   CONFLICT   1410   1410       G -> S (in Ref. 1; AAF04456).
FT   CONFLICT   1577   1577       F -> S (in Ref. 1; AAF04456).
FT   CONFLICT   1586   1591       GWSPAA -> DWGPAV (in Ref. 1; AAF04456).
FT   CONFLICT   1684   1684       T -> A (in Ref. 1; AAF04456).
FT   CONFLICT   1821   1821       G -> D (in Ref. 1; AAF04456).
SQ   SEQUENCE   1864 AA;  207124 MW;  B9DF21005D977983 CRC64;
     MEGCVGEESF QMWELNRRLE AYLTRVKTLE EQNQLLSAEL GGLRAQSGDA SWRARADDEL
     AALRVLVDQR WREKHEAEVQ RDNLAEELES VAGRCQQVRL ARERTIEEAA CSRRALEAEK
     NARGWLSTQA AELERELEAL RASHEEERAH LNAQAACTPR RPPAPAHASP IRAPEVEELA
     RRLGEVWRGA VRDYQERVAH MESSLGQARE RLGQAVRGAR ESRLEVQQLQ ADRDSLQERR
     EALEQRLEGR WQDRLQATEK FQLAVEALEQ EKQGLQSQIA QILEGGQQLA HLKMSLSLEV
     ATYRTLLEAE NSRLQTPGRS SQASLGFPDP KLKLHFLGIP EDQHLGSVLP VLSPTSFSSP
     LPNTLETPVT AFLKTQEFLK ARTPTLASTP IPPMSEAPYP KNAEVRAQDV PHSLLQGGRQ
     QAPEPLWAEA TVPSSTGVLP ELEEPGGEQP DHFPDDPTSL APPLNPHHSI LEAKDRESSE
     SRVSSIFQEE EGQIWELVKK EAATEVKVEN SLAQEIQESG LDTEEIQDSQ GPLQMETLEA
     LGDEPLMSLK TQNHETPGKE NCNSSIEENS GTVKSPEKEK QTPLKSLEEK NVEAEKTLEN
     GVLELSKPLG EEEPRMEDQE LMSPEHTLET VSFLGKENQE VVRSSEEQNL ESLITFKEES
     QYPLGGPEAE DQMLERLVEK EDQRFPRSPE EDQQAFRPLE KENQEPLRFE EAEDQVLERL
     IEKERQESLK SPEEEDQQAF RLLEKENQEP LRFEDAEDQV LERLIEKERQ ESLKSPEEED
     QQAFRLLEKE NQEPLRFEEA EDQVLERLVE KESQESLKSP EEEDQRTGKP LEKENQESLR
     SLDENQETIV LLESKNQRPL RSLEVEEEEQ RIVKPLEKVS QVSLESLEKE NVQSPRYLEE
     DDHMIKSLLE DKTHEILGSL EDRNGENFIP PENETQGSLR PPEEEDQRIV NHLEKESQEF
     LRSPEAEEEE EQVMVRSLEG ENHDPLSSVV KEEQMAESKL ENESQDSRKS LEDESQETFG
     SLEKENLESL RSLAGQDQEE QKLEQETQQP LRAVEDEQMT VNPPEKVDPE LPKPLRNDQE
     VVRSLDKENQ ESLVSLNEGG METVKSSETE NIESLETVGE CLGRRKSVDT QEPLWSTEVT
     SETIEPLEDE TQEPLGCVDE NQEVLTPLER ESQELRSLGK WNPETVESPG GVEDSQQCLE
     VEEGPEREQH QESLRSLGEV EWELPGSGSQ QRWEDVVEDG EGQEASLGAT GVETEDKAEL
     HLRGQGGEEK AVEEGELLQD AVGEAWSLGS SEPKEQRVPA EPLDDLEGQP EQTGTLEVPV
     AQGMPEATEQ DEDRAQAGEQ DSVEVTLGLE AARAGLELEQ EVVGLEDPRH FAREEAIHPS
     LGEESVKAKI DQGLEEPGKE PKEAGALDSG IPELPKTSSE TLECKGWEES GEGWGEEEAS
     LETSDHEGSH APQPRPPKTE EDEGLQAALT VPGPKLLEPC SPIPILTDAH ELQPQAEGIQ
     EAGWQPEAGT EALGRVEDEP EFGRGEIPEG LQDWEEGRED SEADELGETL PDSTPLGLYL
     KSPASPKWEQ AGEQRLFPQG EARKEGWSPA ALAAQGLSDP PEEEQQGHDS DLSSEEFEDL
     GTEASLLPGV PKEVSDHLGQ EPPVLQPACW DQGGESDGFA DEEESGEEGE EEDADEEEGA
     ESGTQWWGPG PSGGGVKVQD VTQRGDLEHE SVGDSGLWDD GLSGAAANVL VTALETVSQD
     SAEPSGSEGS ESASLEGEEG QAIDHLDAPQ EVTSVVPGAG DTFDISGQGP NLESEQVNGR
     MENGLEQAEG QVVLHGDEDQ GIPLQEQGTL KAPLVGSPVH LGPSQPLKFT LSGVDGDSWS
     SGED
//
ID   FRMD5_MOUSE             Reviewed;         517 AA.
AC   Q6P5H6; B0R0I9; Q6PFH6; Q8C0K0;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-FEB-2011, entry version 55.
DE   RecName: Full=FERM domain-containing protein 5;
GN   Name=Frmd5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q6P5H6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6P5H6-2; Sequence=VSP_019983, VSP_019984;
CC       Name=3;
CC         IsoId=Q6P5H6-3; Sequence=VSP_019983, VSP_019985;
CC       Name=4;
CC         IsoId=Q6P5H6-4; Sequence=VSP_019983, VSP_019986;
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK030883; BAC27170.1; -; mRNA.
DR   EMBL; AL928678; CAQ12956.1; -; Genomic_DNA.
DR   EMBL; BC057549; AAH57549.1; -; mRNA.
DR   EMBL; BC062889; AAH62889.1; -; mRNA.
DR   IPI; IPI00223843; -.
DR   IPI; IPI00466728; -.
DR   IPI; IPI00755067; -.
DR   IPI; IPI00885573; -.
DR   RefSeq; NP_766261.2; NM_172673.3.
DR   UniGene; Mm.121514; -.
DR   UniGene; Mm.428057; -.
DR   ProteinModelPortal; Q6P5H6; -.
DR   SMR; Q6P5H6; 15-327.
DR   PhosphoSite; Q6P5H6; -.
DR   PRIDE; Q6P5H6; -.
DR   Ensembl; ENSMUST00000110590; ENSMUSP00000106220; ENSMUSG00000027238.
DR   Ensembl; ENSMUST00000110591; ENSMUSP00000106221; ENSMUSG00000027238.
DR   Ensembl; ENSMUST00000110593; ENSMUSP00000106223; ENSMUSG00000027238.
DR   GeneID; 228564; -.
DR   KEGG; mmu:228564; -.
DR   UCSC; uc008lzl.1; mouse.
DR   UCSC; uc008lzm.1; mouse.
DR   CTD; 228564; -.
DR   MGI; MGI:2442557; Frmd5.
DR   GeneTree; ENSGT00600000084066; -.
DR   HOVERGEN; HBG057180; -.
DR   PhylomeDB; Q6P5H6; -.
DR   NextBio; 379036; -.
DR   ArrayExpress; Q6P5H6; -.
DR   Bgee; Q6P5H6; -.
DR   CleanEx; MM_FRMD5; -.
DR   Genevestigator; Q6P5H6; -.
DR   GermOnline; ENSMUSG00000027238; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0019898; C:extrinsic to membrane; IEA:InterPro.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR000798; Ez/rad/moesin.
DR   InterPro; IPR014847; FERM-adjacent.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH_type.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; FALSE_NEG.
DR   PROSITE; PS50057; FERM_3; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing.
FT   CHAIN         1    517       FERM domain-containing protein 5.
FT                                /FTId=PRO_0000247447.
FT   DOMAIN       17    298       FERM.
FT   VAR_SEQ       1     89       Missing (in isoform 2, isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_019983.
FT   VAR_SEQ     494    517       RVHLKGPQLQQQQWKGWGKSVPLD -> VNKFVLSVLRLLL
FT                                VTMGLLFVLLLLLIILTESDLDVAFFRDIRQTPEFEQFHYQ
FT                                YFCPLRRWFACKIRSVVSLLIDT (in isoform 2).
FT                                /FTId=VSP_019984.
FT   VAR_SEQ     494    517       RVHLKGPQLQQQQWKGWGKSVPLD -> MQERDRSEEGIEK
FT                                EQRPWKGPGSTKQDL (in isoform 3).
FT                                /FTId=VSP_019985.
FT   VAR_SEQ     494    517       RVHLKGPQLQQQQWKGWGKSVPLD -> AMVCLQNPLSGEP
FT                                AN (in isoform 4).
FT                                /FTId=VSP_019986.
SQ   SEQUENCE   517 AA;  58583 MW;  064722C4016B4BD5 CRC64;
     MLSRLMSGSS RSLEREYSCT VRLLDDSEYT CTIQRDAKGQ YLFDLLCHHL NLLEKDYFGI
     RFVDPDKQRH WLEFTKSVVK QLRSQPPFTM CFRVKFYPAD PAALKEEITR YLVFLQIKRD
     LYHGRLLCKT SDAALLAAYI LQAEIGDYDP GKHPEGYSSK FQFFPKHSEK LEKKIAEIHK
     TELSGQTPAT SELNFLRKAQ TLETYGVDPH PCKDVSGNAA FLAFTPFGFV VLQGNKRVHF
     IKWNEVTKLK FEGKTFYLYV SQKEEKKIIL TYFAPTPEAC KHLWKCGIEN QAFYKLEKSS
     QVRTVSSSNL FFKGSRFRYS GRVAKEVMES SAKIKREPPE IHRAGMVPSR SCPSITHGPR
     LSSVPRTRRR AVHISIMEGL ESLRDSAHST PVRSSSHGDT FLPHVRSSRA DSNERVAVIA
     DEAYSPADSV LPTPVAEHSL ELMLLSRQIN GATCSIEEEK ESEASTPTAT EAEALGGELR
     ALCQGHGGSE QEQRVHLKGP QLQQQQWKGW GKSVPLD
//
ID   K1239_MOUSE             Reviewed;        1742 AA.
AC   Q6P5U7; Q3UVW7; Q8CHA7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   08-FEB-2011, entry version 54.
DE   RecName: Full=Leucine-rich repeat and WD repeat-containing protein KIAA1239;
GN   Name=Kiaa1239;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 482-1742.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 541-1742.
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1046-1742.
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SIMILARITY: Contains 5 LRR (leucine-rich) repeats.
CC   -!- SIMILARITY: Contains 11 WD repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC41474.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC114408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC122744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC062655; AAH62655.1; -; mRNA.
DR   EMBL; AB093290; BAC41474.1; ALT_INIT; mRNA.
DR   EMBL; AK136869; BAE23152.1; -; mRNA.
DR   IPI; IPI00885399; -.
DR   RefSeq; NP_795980.2; NM_177006.3.
DR   UniGene; Mm.319487; -.
DR   ProteinModelPortal; Q6P5U7; -.
DR   SMR; Q6P5U7; 393-435, 965-1038, 1275-1338.
DR   PhosphoSite; Q6P5U7; -.
DR   PRIDE; Q6P5U7; -.
DR   Ensembl; ENSMUST00000053436; ENSMUSP00000055129; ENSMUSG00000090061.
DR   GeneID; 319807; -.
DR   KEGG; mmu:319807; -.
DR   MGI; MGI:1920464; 3110047P20Rik.
DR   GeneTree; ENSGT00530000063450; -.
DR   HOGENOM; HBG446858; -.
DR   HOVERGEN; HBG108031; -.
DR   InParanoid; Q6P5U7; -.
DR   PhylomeDB; Q6P5U7; -.
DR   NextBio; 395436; -.
DR   ArrayExpress; Q6P5U7; -.
DR   Bgee; Q6P5U7; -.
DR   CleanEx; MM_3110047P20RIK; -.
DR   Genevestigator; Q6P5U7; -.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 3.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; WD40_like; 2.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   2: Evidence at transcript level;
KW   Leucine-rich repeat; Repeat; WD repeat.
FT   CHAIN         1   1742       Leucine-rich repeat and WD repeat-
FT                                containing protein KIAA1239.
FT                                /FTId=PRO_0000320921.
FT   REPEAT      386    410       LRR 1.
FT   REPEAT      677    698       LRR 2.
FT   REPEAT      724    747       LRR 3.
FT   REPEAT      883    906       LRR 4.
FT   REPEAT      925    953       LRR 5.
FT   REPEAT      963   1004       WD 1.
FT   REPEAT     1007   1046       WD 2.
FT   REPEAT     1140   1179       WD 3.
FT   REPEAT     1229   1271       WD 4.
FT   REPEAT     1272   1311       WD 5.
FT   REPEAT     1314   1353       WD 6.
FT   REPEAT     1355   1394       WD 7.
FT   REPEAT     1396   1434       WD 8.
FT   REPEAT     1476   1516       WD 9.
FT   REPEAT     1522   1561       WD 10.
FT   REPEAT     1614   1653       WD 11.
FT   CONFLICT   1218   1218       G -> S (in Ref. 3; BAC41474).
SQ   SEQUENCE   1742 AA;  197414 MW;  630DA9B992EBB2D2 CRC64;
     MWPAGAGTKL PCPRDSALRR AAFSGNLTAL PSHLVPAGRS VRVFISANPE DTGAERQALR
     ETVYPKLREF CRENYGLEFQ VIDLYWGIEE DEWDSPELQK MRMKLLEECL KTSAGPCFVG
     LLGEKYGNIR IPGEVEASEF EMILDAAVEA KLETKLLEDW YCRDENSVPA AYYLRPRLEV
     PRSNKNSTQP SASSEQERPW QEISDEIKTI FKAAVKLLHE QGKMKQSQAK RYLFSAIEDE
     FDFALGKQTP AFLKKCVCYI RKIANIERFV KIPEMGKYMD ITGTDPRIVR DPEAQEKLIK
     LRDEFIPTIV ASSNLRVYTS VTHCDMKLGY SQEIENHYIE GLGKQFYEDM IDIIQATVQQ
     NFDTETDTLY DEILQHSSLC KTYASFYEYK CESLNILHKY ILPSKTGHIN PLVVYGGPCT
     GKTLLLAEVA KKAYGWLHED TGPDSDPVVI VRFLGTTDMS IDLRTLLLSV CEQLAVNYRC
     LVQSFPKKIH DLRDLFINLL NESSLQRPLV IILDALEQLS EADEARKLWW LPAHLPRFVR
     IILSTLPNKH GILQKLRCLI HEEDNYIELI PRDRKMCSQV LKHQLLRVKR KVTSGQQIYV
     NNAFSKCTLP MFVNLTFREV RHWRSHKDVD ESSLCVTVHE SIEQLFWSLE KKCGQKLVSR
     ALGYITMAKM GLSEMELEDV LALDNSVMNE LNENTRPSNP LRVPYLYIAR LKEGLNGYLI
     ERHVKNVTLL VWANRHLQLI AQKLYLQEDS NLREMHTILA DYFLGVWSGG RRKAFCLEDP
     YLNGCLDLEN RSLLEEEKHF MEQASFDRQA PDQPWVFQCN PLEPDIFFVN HRKMSELLYH
     LTRCGKTDDL LYGIIMNFSW LYTMIKIGQF DKVLADIELA YNYSQEKELK FLASTLRSIR
     NKVIAFPGSL SAELQQRLLP VVSSLPKLRH LLLECDKDGP KYCSIVPLHS SMDVTYSPER
     LPLASSHLHV TEILPTCNPS TVLTALENGS ISTWDVETRQ LLRQITTAQS VILGMKLSSD
     EKYLVVATTN NTLLIYDNVN SCLLSEVEIK GTKHGSGSTY INGFTLSVNH ALAWLEASKD
     VTVIDLLYGW PLYQFHCWYE VTCVQCSLDG VYAFCGQYLN NTTIFHLGSG EKICTVTSEF
     SGGFVKFLLI LDTAQEMVMV DSEGSLSVWN TEDISNPQLT EDFDCRKEDS EVVSIELSED
     QSAILICKAL SIELLDTGMW KVAEKFRARH NERFVSAVLS KNGDCIIATM ENTPAVFFWR
     RDTGQCLASL QESSGTIVKL VKSSHHNMLL SLSTSGVLSI WDIDIITAMS NIDKTGKPIQ
     SLVLPARGEI IYSLDGSDCV HKWNFSSGFI EAVFKHEGIV EHCVLTSTGD LMVTSDDKSS
     QYVWHTSSGE NLFRINGQRI SQLLITHNDQ FVVSLCEENA SRVWRLATGH RVCNILTTLQ
     NAFITSANTF VVGMTKSKVL AVSLWTGSIT KKFCCEDGIT IVNFKLIPDC PDVIVFITSA
     ETVNLWSLTD EVICRRVQLP SNFLKNLEDF EISPNGKLGI ISRGDENINV LDLHSGKLRV
     VHASGVIWRQ RLSRDGRYLV YICFRNGEEE EENDAISSLI VMRLADGKNI GACSLYKTPT
     FLALSQRHLN IIVGFDDGSI GIYTVVDRVD AALKIKIATS NSRQIFNNAT QTSRPKSNSY
     SFKVSVDCLW RESTEVFARD SPITVSDSSE SNEATPSKKH NSCYDRVCAA LESRSHSYTP
     DN
//
ID   GRL1A_MOUSE             Reviewed;         366 AA.
AC   Q6P6I6; Q8CG13; Q9CXJ7; Q9DCQ9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   08-MAR-2011, entry version 44.
DE   RecName: Full=Protein GRINL1A;
DE   AltName: Full=Glutamate receptor-like protein 1A;
GN   Name=Grinl1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryo, Embryonic eye, Embryonic head, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=129, and Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-45, AND IDENTIFICATION.
RC   STRAIN=C57BL/6J;
RX   PubMed=12063408;
RA   Wydner K.S., Mohan Raj B.K., Sciorra L.J., Roginski R.S.;
RT   "The mouse orthologue of the human ionotropic glutamate receptor-like
RT   gene (GRINL1A) maps to mouse chromosome 9.";
RL   Cytogenet. Cell Genet. 95:240-241(2001).
CC   -!- FUNCTION: Isoform 1 appears to be stable component of the Pol
CC       II(G) complex form of RNA polymerase II. Pol II synthesizes mRNA
CC       precursors and many functional non-coding RNAs and is the central
CC       component of the basal RNA polymerase II transcription machinery.
CC       Isoform 1 may play a role in Mediator-dependent regulation of
CC       transcription activation. Isoform 1 acts in vitro as negative
CC       regulator of transcriptional activation; this repression is
CC       relieved by the Mediator complex, which restores Pol II(G)
CC       activator-dependent transcription to a level equivalent to that of
CC       Pol II (By similarity).
CC   -!- SUBUNIT: Isoform 1 is a component of the Pol II(G) complex, which
CC       contains the RNA polymerase II (Pol II) core complex subunits and
CC       Grinl1a isoform 1 and appears to be an abundant form of Pol II.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6P6I6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6P6I6-2; Sequence=VSP_032623;
CC   -!- SIMILARITY: Belongs to the GRINL1 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK002571; BAB22196.1; -; mRNA.
DR   EMBL; AK014316; BAB29267.1; -; mRNA.
DR   EMBL; AK051868; BAC34793.1; -; mRNA.
DR   EMBL; AK052037; BAC34836.1; -; mRNA.
DR   EMBL; AK079119; BAC37548.1; -; mRNA.
DR   EMBL; AK159924; BAE35486.1; -; mRNA.
DR   EMBL; AK166738; BAE38981.1; -; mRNA.
DR   EMBL; BC018502; AAH18502.1; -; mRNA.
DR   EMBL; BC062199; AAH62199.1; -; mRNA.
DR   EMBL; AF462417; AAO15648.1; -; Genomic_DNA.
DR   EMBL; AF462416; AAO15648.1; JOINED; Genomic_DNA.
DR   IPI; IPI00466976; -.
DR   IPI; IPI00889304; -.
DR   RefSeq; NP_001158265.1; NM_001164793.1.
DR   RefSeq; NP_848717.1; NM_178602.3.
DR   UniGene; Mm.21094; -.
DR   ProteinModelPortal; Q6P6I6; -.
DR   STRING; Q6P6I6; -.
DR   PhosphoSite; Q6P6I6; -.
DR   PRIDE; Q6P6I6; -.
DR   Ensembl; ENSMUST00000034720; ENSMUSP00000034720; ENSMUSG00000032199.
DR   GeneID; 28015; -.
DR   KEGG; mmu:28015; -.
DR   CTD; 28015; -.
DR   MGI; MGI:107282; Grinl1a.
DR   eggNOG; roNOG17475; -.
DR   GeneTree; ENSGT00570000079401; -.
DR   HOVERGEN; HBG098324; -.
DR   InParanoid; Q6P6I6; -.
DR   OMA; AQSSDEC; -.
DR   OrthoDB; EOG4BCDN8; -.
DR   PhylomeDB; Q6P6I6; -.
DR   NextBio; 306524; -.
DR   ArrayExpress; Q6P6I6; -.
DR   Bgee; Q6P6I6; -.
DR   Genevestigator; Q6P6I6; -.
DR   GO; GO:0043025; C:neuronal cell body; IMP:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051685; P:maintenance of ER location; IMP:UniProtKB.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; DNA-directed RNA polymerase;
KW   Nucleus; Phosphoprotein; Transcription.
FT   CHAIN         1    366       Protein GRINL1A.
FT                                /FTId=PRO_0000326230.
FT   COILED       15     39       Potential.
FT   COILED      299    333       Potential.
FT   MOD_RES     362    362       Phosphoserine (By similarity).
FT   MOD_RES     363    363       Phosphoserine (By similarity).
FT   VAR_SEQ       1    104       Missing (in isoform 2).
FT                                /FTId=VSP_032623.
FT   CONFLICT    112    112       D -> V (in Ref. 2; AAH62199).
FT   CONFLICT    275    275       Q -> R (in Ref. 2; AAH62199).
SQ   SEQUENCE   366 AA;  41237 MW;  1115E39921CF3561 CRC64;
     MFSLPRGFEP PAPEDLGRQS SAELRERLRR QERLLRNEKF ICKLPDKGKK ISDTVAKLKA
     AISEREEVRG RSELFHPVSV DCKLRQKATT RADTDVDKAQ SSDLMLDTSS LDPDCSSIDI
     KSSKSTSETQ GPTHLTHRGN EETLEAGYTV NSSPAAHIRA RAPSSEVKEH LPQHSVSSQE
     EEISSSIDSL FITKLQKITI ADQSEPSEEN TSTENFPELQ SETPKKPHYM KVLEMRARNP
     VPPPHKFKTN VLPTQQSDSP SHCQRGQSPA SSEEQRRRAR QHLDDITAAR LLPLHHLPAQ
     LLSIEESLAL QREQKQNYEE MQAKLAAQKL AERLNIKMQS YNPEGESSGR YREVRDEADA
     QSSDEC
//
ID   ORAI3_MOUSE             Reviewed;         290 AA.
AC   Q6P8G8;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=Protein orai-3;
DE   AltName: Full=Transmembrane protein 142C;
GN   Name=Orai3; Synonyms=Tmem142c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Key regulator or component of store-operated Ca(2+)
CC       channel and transcription factor NFAT nuclear import (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with EFCAB4B/CRACR2A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the Orai family.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK136955; BAE23186.1; -; mRNA.
DR   EMBL; BC061259; AAH61259.1; -; mRNA.
DR   IPI; IPI00387460; -.
DR   RefSeq; NP_940816.1; NM_198424.3.
DR   UniGene; Mm.36852; -.
DR   ProteinModelPortal; Q6P8G8; -.
DR   STRING; Q6P8G8; -.
DR   PhosphoSite; Q6P8G8; -.
DR   PRIDE; Q6P8G8; -.
DR   Ensembl; ENSMUST00000061587; ENSMUSP00000050279; ENSMUSG00000043964.
DR   GeneID; 269999; -.
DR   KEGG; mmu:269999; -.
DR   UCSC; uc009jwr.1; mouse.
DR   CTD; 269999; -.
DR   MGI; MGI:3039586; Orai3.
DR   GeneTree; ENSGT00390000015354; -.
DR   HOGENOM; HBG715505; -.
DR   HOVERGEN; HBG081343; -.
DR   InParanoid; Q6P8G8; -.
DR   OMA; MASTVIM; -.
DR   OrthoDB; EOG4DV5MR; -.
DR   PhylomeDB; Q6P8G8; -.
DR   NextBio; 393150; -.
DR   ArrayExpress; Q6P8G8; -.
DR   Bgee; Q6P8G8; -.
DR   Genevestigator; Q6P8G8; -.
DR   GermOnline; ENSMUSG00000043964; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR012446; DUF1650.
DR   Pfam; PF07856; DUF1650; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    290       Protein orai-3.
FT                                /FTId=PRO_0000234396.
FT   TRANSMEM     63     82       Helical; (Potential).
FT   TRANSMEM     95    115       Helical; (Potential).
FT   TRANSMEM    157    177       Helical; (Potential).
FT   TRANSMEM    239    259       Helical; (Potential).
SQ   SEQUENCE   290 AA;  31358 MW;  F702164F9F1EB44B CRC64;
     MKGGEGDTGE QAPLNPEVDS PAGSATYREF VHRGYLDLMG ASQHSLRALS WRRLYLSRAK
     LKASSRTSAL LSGFAMVAMV EVQLENDHEY PPGLLVAFSA CTTVLVAVHL FALMVSTCLL
     PHIEAVSNIH NLNSVHQSPH QRLHRYVELA WGFSTALGTF LFLAEVVLVG WVKFVPIGAP
     MGKPAPVVPM SQVPPVTVSL SLASNLTPSS ASITTSQQPS KACPPRQVCD SAHGPGWQAA
     MASTAIMVPV GLVFMAFALH FYRSLVAHKT DRHKQELEEL SRLQGELQAV
//
ID   KCRS_MOUSE              Reviewed;         419 AA.
AC   Q6P8J7;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Creatine kinase S-type, mitochondrial;
DE            EC=2.7.3.2;
DE   AltName: Full=Basic-type mitochondrial creatine kinase;
DE            Short=Mib-CK;
DE   AltName: Full=Sarcomeric mitochondrial creatine kinase;
DE            Short=S-MtCK;
DE   Flags: Precursor;
GN   Name=Ckmt2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart, and Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 311-326, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: Reversibly catalyzes the transfer of phosphate between
CC       ATP and various phosphogens (e.g. creatine phosphate). Creatine
CC       kinase isoenzymes play a central role in energy transduction in
CC       tissues with large, fluctuating energy demands, such as skeletal
CC       muscle, heart, brain and spermatozoa (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + creatine = ADP + phosphocreatine.
CC   -!- SUBUNIT: Exists as an octamer composed of four CKMT2 homodimers
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein; Intermembrane side (By similarity).
CC   -!- MISCELLANEOUS: Mitochondrial creatine kinase binds cardiolipin.
CC   -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC   -!- SIMILARITY: Contains 1 phosphagen kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 phosphagen kinase N-terminal domain.
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DR   EMBL; BC061221; AAH61221.1; -; mRNA.
DR   IPI; IPI00120076; -.
DR   RefSeq; NP_940807.1; NM_198415.2.
DR   UniGene; Mm.316438; -.
DR   ProteinModelPortal; Q6P8J7; -.
DR   SMR; Q6P8J7; 47-413.
DR   STRING; Q6P8J7; -.
DR   PhosphoSite; Q6P8J7; -.
DR   PRIDE; Q6P8J7; -.
DR   Ensembl; ENSMUST00000022122; ENSMUSP00000022122; ENSMUSG00000021622.
DR   GeneID; 76722; -.
DR   KEGG; mmu:76722; -.
DR   UCSC; uc007rkc.1; mouse.
DR   CTD; 76722; -.
DR   MGI; MGI:1923972; Ckmt2.
DR   eggNOG; roNOG05439; -.
DR   GeneTree; ENSGT00550000074561; -.
DR   HOGENOM; HBG445448; -.
DR   HOVERGEN; HBG001339; -.
DR   InParanoid; Q6P8J7; -.
DR   OMA; LPQFGRK; -.
DR   OrthoDB; EOG40VVPN; -.
DR   PhylomeDB; Q6P8J7; -.
DR   BRENDA; 2.7.3.2; 244.
DR   NextBio; 345699; -.
DR   ArrayExpress; Q6P8J7; -.
DR   Bgee; Q6P8J7; -.
DR   CleanEx; MM_CKMT2; -.
DR   Genevestigator; Q6P8J7; -.
DR   GermOnline; ENSMUSG00000021622; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004111; F:creatine kinase activity; TAS:MGI.
DR   GO; GO:0006603; P:phosphocreatine metabolic process; TAS:MGI.
DR   InterPro; IPR000749; ATP-guanido_PTrfase.
DR   InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR   InterPro; IPR022415; ATP-guanido_PTrfase_cat_AS.
DR   InterPro; IPR022413; ATP-guanido_PTrfase_N.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   Gene3D; G3DSA:1.10.135.10; ATP-gua_Ptrans; 1.
DR   Gene3D; G3DSA:3.30.590.10; ATP-gua_Ptrans; 1.
DR   PANTHER; PTHR11547; ATP-gua_Ptrans; 1.
DR   Pfam; PF00217; ATP-gua_Ptrans; 1.
DR   Pfam; PF02807; ATP-gua_PtransN; 1.
DR   SUPFAM; SSF48034; ATP-gua_Ptrans; 1.
DR   PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR   PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
DR   PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Kinase; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW   Transferase; Transit peptide.
FT   TRANSIT       1     39       Mitochondrion.
FT   CHAIN        40    419       Creatine kinase S-type, mitochondrial.
FT                                /FTId=PRO_0000016595.
FT   DOMAIN       46    132       Phosphagen kinase N-terminal.
FT   DOMAIN      159    401       Phosphagen kinase C-terminal.
FT   NP_BIND     162    166       ATP (By similarity).
FT   NP_BIND     354    359       ATP (By similarity).
FT   REGION       40     64       Cardiolipin-binding (By similarity).
FT   BINDING     225    225       ATP (By similarity).
FT   BINDING     270    270       ATP (By similarity).
FT   BINDING     326    326       ATP (By similarity).
FT   BINDING     369    369       ATP (By similarity).
SQ   SEQUENCE   419 AA;  47473 MW;  E9083E4F689903EF CRC64;
     MASAFSKLLT GRNASLLFTT LGTSALTTGY LLNRQKVSAD AREQHKLFPP SADYPDLRKH
     NNCMAECLTP TIYAKLRNKM TPSGYTLDQC IQTGVDNPGH PFIKTVGMVA GDEESYEVFA
     DLFDPVIKLR HNGYDPRVMK HPTDLDASKI THGQFDERYV LSSRVRTGRS IRGLSLPPAC
     SRAERREVEN VAITALEGLK GDLAGRYYKL SEMTEQDQQR LIDDHFLFDK PVSPLLTCAG
     MARDWPDARG IWHNYDKTFL IWINEEDHTR VISMEKGGNM KRVFERFCRG LKEVERLIQE
     RGWEFMWNER LGYILTCPSN LGTGLRAGVH VRIPKLSKDP RFSKILENLR LQKRGTGGVD
     TAAVADVYDI SNIDRIGRSE VELVQIVIDG VNYLVDCEKK LERGQDIKVP PPLPQFGRK
//
ID   Q6P8K5_MOUSE            Unreviewed;       411 AA.
AC   Q6P8K5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   SubName: Full=5730601F06Rik protein;
DE   Flags: Fragment;
GN   Name=Zfp266;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC061209; AAH61209.1; -; mRNA.
DR   IPI; IPI00462339; -.
DR   UniGene; Mm.396415; -.
DR   UniGene; Mm.480973; -.
DR   ProteinModelPortal; Q6P8K5; -.
DR   Ensembl; ENSMUST00000068296; ENSMUSP00000066012; ENSMUSG00000060510.
DR   UCSC; uc009oiu.1; mouse.
DR   MGI; MGI:1924769; Zfp266.
DR   eggNOG; maNOG17891; -.
DR   GeneTree; ENSGT00530000063830; -.
DR   HOGENOM; HBG717200; -.
DR   HOVERGEN; HBG018163; -.
DR   InParanoid; Q6P8K5; -.
DR   OrthoDB; EOG4SBDXS; -.
DR   ArrayExpress; Q6P8K5; -.
DR   Bgee; Q6P8K5; -.
DR   Genevestigator; Q6P8K5; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR001909; Krueppel-associated_box.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 4.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF109640; Krueppel-associated_box; 1.
DR   PROSITE; PS50805; KRAB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   2: Evidence at transcript level;
KW   Metal-binding; Zinc.
FT   NON_TER     411    411
SQ   SEQUENCE   411 AA;  46695 MW;  372EB7DEC44307C7 CRC64;
     MAAIDLSHGL LSREPIYVYE ANIEVDGTVT DNQANCYQDS VTFDDVAVEF TPDEWTLLDL
     TQKNLYREVM LENYENLTSV GCQLFIPSLT PWLKQEESEV AESAVPQQLE LQPTIDDSEL
     ENYFRMQSSS ATEMVGDSSL HEQSGNHNEE DLCDSKPCGN VLGEQLCLNT EVSMQSQGYS
     SECNWYGKDI LSLLKETSTG QTVSELNQCG KLFSLTPNIM YPSTSTNEKP FECTDCETAF
     FNQSYFQPDM RPHNGGEPFD WSKYGNGFIH PTGLAMHLPI LNARNPYKFE ECGKDFQYFA
     CLNNPMGMCT GEKFCDCKEC WKAFTVSSHL TQYVSIHTEE KSKVCKICGK SFANYSRLSA
     HVKTHNEEKP FVCKECGKAF KNMSYLNDHV RIHTGIKSYK CEKKKKKKKK K
//
ID   Q6P8W7_MOUSE            Unreviewed;       181 AA.
AC   Q6P8W7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-FEB-2011, entry version 52.
DE   SubName: Full=Putative uncharacterized protein;
DE   SubName: Full=Zfp655 protein;
GN   Name=Zfp655;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung and heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory brain;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC061032; AAH61032.1; -; mRNA.
DR   EMBL; AK161949; BAE36650.1; -; mRNA.
DR   IPI; IPI00460180; -.
DR   RefSeq; NP_001077427.1; NM_001083958.1.
DR   UniGene; Mm.206555; -.
DR   ProteinModelPortal; Q6P8W7; -.
DR   SMR; Q6P8W7; 71-121.
DR   PRIDE; Q6P8W7; -.
DR   Ensembl; ENSMUST00000085661; ENSMUSP00000082803; ENSMUSG00000007812.
DR   GeneID; 72611; -.
DR   KEGG; mmu:72611; -.
DR   UCSC; uc009amp.1; mouse.
DR   CTD; 72611; -.
DR   MGI; MGI:1919861; Zfp655.
DR   GeneTree; ENSGT00390000021552; -.
DR   HOVERGEN; HBG062639; -.
DR   NextBio; 336593; -.
DR   ArrayExpress; Q6P8W7; -.
DR   Bgee; Q6P8W7; -.
DR   Genevestigator; Q6P8W7; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR001909; Krueppel-associated_box.
DR   Pfam; PF01352; KRAB; 1.
DR   SMART; SM00349; KRAB; 1.
DR   SUPFAM; SSF109640; Krueppel-associated_box; 1.
DR   PROSITE; PS50805; KRAB; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   181 AA;  19980 MW;  4E4E764E8B7F14DA CRC64;
     MEEVTSQEAA ESPRGHFQPL ENQSECLSPE LRFLQDTDME QGFSGAPPVP QVPALPHEGS
     PGDQAAALLT ARYQEFVTFE DVAVHLTREE WGCLDPVQRE LYREVMLENY GNVVSLGILL
     RLPTTRIHCV NSCPALSHTQ ASAFSGETLA VLTAGITKRW PRDRLSIGSA HPSTETPFPR
     L
//
ID   KANK4_MOUSE             Reviewed;        1016 AA.
AC   Q6P9J5; Q8BV03;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=KN motif and ankyrin repeat domain-containing protein 4;
DE   AltName: Full=Ankyrin repeat domain-containing protein 38;
GN   Name=Kank4; Synonyms=Ankrd38;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 5 ANK repeats.
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DR   EMBL; AK081525; BAC38246.1; -; mRNA.
DR   EMBL; BC060737; AAH60737.1; -; mRNA.
DR   IPI; IPI00311120; -.
DR   RefSeq; NP_766460.2; NM_172872.3.
DR   UniGene; Mm.440211; -.
DR   ProteinModelPortal; Q6P9J5; -.
DR   SMR; Q6P9J5; 826-1002.
DR   PhosphoSite; Q6P9J5; -.
DR   PRIDE; Q6P9J5; -.
DR   Ensembl; ENSMUST00000102790; ENSMUSP00000099851; ENSMUSG00000035407.
DR   GeneID; 242553; -.
DR   KEGG; mmu:242553; -.
DR   NMPDR; fig|10090.3.peg.9944; -.
DR   UCSC; uc008tuk.1; mouse.
DR   CTD; 242553; -.
DR   MGI; MGI:3043381; Kank4.
DR   GeneTree; ENSGT00530000063448; -.
DR   HOGENOM; HBG282993; -.
DR   HOVERGEN; HBG080220; -.
DR   InParanoid; Q6P9J5; -.
DR   OMA; LLTRESC; -.
DR   OrthoDB; EOG451DQG; -.
DR   PhylomeDB; Q6P9J5; -.
DR   NextBio; 385408; -.
DR   ArrayExpress; Q6P9J5; -.
DR   Bgee; Q6P9J5; -.
DR   CleanEx; MM_KANK4; -.
DR   Genevestigator; Q6P9J5; -.
DR   GermOnline; ENSMUSG00000035407; Mus musculus.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR021939; KN_motif.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 2.
DR   Pfam; PF12075; KN_motif; 1.
DR   SMART; SM00248; ANK; 5.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
PE   2: Evidence at transcript level;
KW   ANK repeat; Coiled coil; Phosphoprotein; Repeat.
FT   CHAIN         1   1016       KN motif and ankyrin repeat domain-
FT                                containing protein 4.
FT                                /FTId=PRO_0000244365.
FT   REPEAT      838    868       ANK 1.
FT   REPEAT      877    905       ANK 2.
FT   REPEAT      910    939       ANK 3.
FT   REPEAT      943    973       ANK 4.
FT   REPEAT      977   1007       ANK 5.
FT   COILED      346    409       Potential.
FT   COMPBIAS    314    318       Poly-Pro.
FT   COMPBIAS    625    652       Pro-rich.
FT   MOD_RES     160    160       Phosphoserine (By similarity).
FT   CONFLICT    282    282       P -> A (in Ref. 1; BAC38246).
SQ   SEQUENCE   1016 AA;  110404 MW;  522174CCE563D154 CRC64;
     MEKIDGKDQS SQGDEEKEPP KSYPYSVETP YGFHLDLDFL KYVDDIEKGH TIKRIPIHRR
     AKQAKFSTLP RNFSLPNSGD RTYAVPPQQN WSPVVPRKIS LGTQEPSQPL PLGDLPQASV
     QGSELNYHRK ALLAKDARQA EAGSLEDVGS GRPQLLRASS MPATLLQNQV PEEPSLTSGP
     STLLALPLLQ DEGSVCDGAF DPAEGLMGFQ ASAQSVDREL GELEPAIPEQ VWEGAEPEEG
     DLKASSHLSQ PGPSSAVQSV PMDLEEVEIE HHMREAELVL TPGSATPSPP PLPSPILEND
     LSLDEIELSI SEIPPPPPIE VDVRSIGIRV TEESLGLLET DTSSISSLKN QVLALEDKLS
     GRTEELARVR AALEQQEEET KAREQRIQEL ECTVAHLEEK LSQERASEAP DRTDATVNTD
     PLQELTPRES HDKNIGVNLL NTPDPECRAP RAEKNGFPWV QNNHKQSYPS PEEPVLPPQL
     SLPRGPEQIL ASSLCSCLSM ELRIEEEGSE QEGGQEEGAG GLSRAAGESS WSTRESAPVI
     REEATSELPG AERPGRPASS PQDATIGQYV KKIQELLHEQ WNCLEHGYPE LASAIKQPAS
     KLSSIQNQLL SSLNLLLSAY SAQAPEPEPK ETPAPPPSTP PPPPPPPPEI SPSTSLKSIM
     KKKDYGFRAG GNGTKKNLQF VGVNGGYETT SSEETSGEDS SPEDLSDSET EKKQDCSESR
     EDRDLHPSCE AGQGVPEGTR NSGHTSDRGE EVSHLRAERY KPSEEFLNAC QTLSQHLPET
     GDTTKQLLRQ SLNTISQEWF RVSSRKLSSP EAVAAYLLEV QPHSPYLLKL LVNLADRSGN
     TALHYSVSHS NFAIVKLLLD TGVCNVDHQN KAGYTAVMIT PLASAETKED MAVVWKLLRE
     GNVNIQATQG GQTALMLGVS HDREDMVQAL LSCQADVNLQ DNDGSSALML ACHQGNADLV
     RLLLAHPACN SSLTDKAGRT ALSLVLNSPA HVEIAELLRA HSEPGRSLGP KELQKN
//
ID   Q6P9K2_MOUSE            Unreviewed;      1707 AA.
AC   Q6P9K2;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   SubName: Full=Zfhx3 protein;
DE   Flags: Fragment;
GN   Name=Zfhx3; Synonyms=Atbf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
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DR   EMBL; BC060729; AAH60729.1; -; mRNA.
DR   IPI; IPI00475055; -.
DR   UniGene; Mm.416972; -.
DR   UniGene; Mm.477670; -.
DR   ProteinModelPortal; Q6P9K2; -.
DR   STRING; Q6P9K2; -.
DR   Ensembl; ENSMUST00000043896; ENSMUSP00000044612; ENSMUSG00000038872.
DR   MGI; MGI:99948; Zfhx3.
DR   GeneTree; ENSGT00530000063717; -.
DR   InParanoid; Q6P9K2; -.
DR   ArrayExpress; Q6P9K2; -.
DR   Bgee; Q6P9K2; -.
DR   Genevestigator; Q6P9K2; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001356; Homeobox.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 4.
DR   Pfam; PF00046; Homeobox; 4.
DR   SMART; SM00389; HOX; 4.
DR   SMART; SM00355; ZnF_C2H2; 6.
DR   SUPFAM; SSF46689; Homeodomain_like; 4.
DR   PROSITE; PS00027; HOMEOBOX_1; 2.
DR   PROSITE; PS50071; HOMEOBOX_2; 4.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE   2: Evidence at transcript level;
KW   DNA-binding; Homeobox; Nucleus.
FT   NON_TER       1      1
SQ   SEQUENCE   1707 AA;  186439 MW;  DC34F64C60FBA5DA CRC64;
     LPLQQLERFA KQYREHYDKL YPLRPQTPEP PPPPPPPPPP PLPTAPPQPA SAPAIPASAP
     PITSPTIAPA QPSVPLTQLS MPMELPIFSP LMMQTMPLQT LPAQLPPQLG PVEPLPADLA
     QLYQHQLNPT LLQQQNKRPR TRITDDQLRV LRQYFDINNS PSEEQIKEMA DKSGLPQKVI
     KHWFRNTLFK ERQRNKDSPY NFSNPPITSL EELKIDSRPP SPEPQKQEYW GSKRSSRTRF
     TDYQLRVLQD FFDANAYPKD DEFEQLSNLL NLPTRVIVVW FQNARQKARK NYENQGEGKD
     GERRELTNDR YIRTSNLNYQ CKKCSLVFQR IFDLIKHQKK LCYKDEDEEG QDDSQNEDSM
     DAMEILTPTS SSCSTPMPSQ AYSTPAPSAA AANTAPSAFL QLTAETDELA TFNSKAEASD
     EKPKQADPPS AQPNQTQEKQ GQPKPEMQQQ LEQLEQKTNA PQPKLPQPAA PSLPQPPPQA
     PPPQCPLPQS SPSPSQLSHL PLKPLHTSTP QQLANLPPQL IPYQCDQCKL AFPSFEHWQE
     HQQLHFLSAQ NQFIHPQFLD RSLDMPFMLF DPSNPLLASQ LLSGAIPQIP ASSATSPSTP
     TSTMNTLKRK LEEKASASPG ENDSGTGGEE PQRDKRLRTT ITPEQLEILY QKYLLDSNPT
     RKMLDHIAHE VGLKKRVVQV WFQNTRARER KGQFRAVGPA QAHRRCPFCR ALFKAKTALE
     AHIRSRHWHE AKRAGYNLTL SAMLLDCDGG LQMKGDIFDG TSFSHLPPSS SDGQGVPLSP
     VSKTMELSPR TLLSPSSIKV EGIEDFESPS MSSVNLNFDQ TKLDNDDCSS VNTAITDTTT
     GDEGNADNDS ATGIATETKS SAPNEGLTKA AMMAMSEYED RLSSGLVSPA PSFYSKEYDN
     EGTVDYSETS SLADPCSPSP GASGSAGKSG DGGDRPGQKR FRTQMTNLQL KVLKSCFNDY
     RTPTMLECEV LGNDIGLPKR VVQVWFQNAR AKEKKSKLSM AKHFGINQTS YEGPKTECTL
     CGIKYSARLS VRDHIFSQQH ISKVKDTIGS QLDKEKEYFD PATVRQLMAQ QELDRIKKAN
     EVLGLAAQQQ GMFDNAPLQA LNLPTTYPAL QGIPPVLLPG LNSPSLPGFT PANTALTSPK
     PNLMGLPSTT VPSPGLPTSG LPNKPSSASL SSPTPAQATM AMAPQPPPQP QQPQPPVQQP
     PPPPAAQQIP APQLTPQQQR KDKDGEKGKE KEKAHKGKGE PLPVPKKEKG EAPPAATATI
     SAPLPAMEYA VDPAQLQALQ AALTSDPTAL LTSQFLPYFV PGFSPYYAPQ IPGALQSGYL
     QPMYGMEGLF PYSPALSQAL MGLSPGSLLQ QYQQYQQSLQ EAIQQQQQQQ QQQQQQQQRQ
     LQQQQQQQQQ KVQQQQQQQQ QPKASQTPVP QGPASPDKDP AKESPKPEEQ KNVPREVSPL
     LPKPPEEPEA ESKSASADSL CDPFIVPKVQ YKLVCRKCQA GFGDEEAARS HLKSLCCFGQ
     SVVNLQEMVL HVPTGSGGSG GGGGGSGGGG GSYHCLACES ALCGEEALSQ HLESALHKHR
     TITRAARNAK EHPSLLPHSA CFPDPSTAST SQSAAHSNDS PPPPSAAPSS SASPHASRKS
     WPPVGSRASA AKPPSFPPLS SSSTVTSSSC STSGVQPSMP TDDYSEESDT DLSQKSDGPA
     SPVEGPKDPS CPKDSGLTSV GTDTFRL
//
ID   Q6P9K9_MOUSE            Unreviewed;      1587 AA.
AC   Q6P9K9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   SubName: Full=Nrxn3 protein;
GN   Name=Nrxn3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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CC   -----------------------------------------------------------------------
DR   EMBL; BC060719; AAH60719.1; -; mRNA.
DR   IPI; IPI00228680; -.
DR   UniGene; Mm.425766; -.
DR   UniGene; Mm.477211; -.
DR   ProteinModelPortal; Q6P9K9; -.
DR   SMR; Q6P9K9; 269-656, 699-881, 1105-1314.
DR   STRING; Q6P9K9; -.
DR   Ensembl; ENSMUST00000085138; ENSMUSP00000082225; ENSMUSG00000066392.
DR   UCSC; uc007okb.1; mouse.
DR   MGI; MGI:1096389; Nrxn3.
DR   HOGENOM; HBG358378; -.
DR   HOVERGEN; HBG052670; -.
DR   InParanoid; Q6P9K9; -.
DR   ArrayExpress; Q6P9K9; -.
DR   Bgee; Q6P9K9; -.
DR   Genevestigator; Q6P9K9; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005246; F:calcium channel regulator activity; IGI:MGI.
DR   GO; GO:0007269; P:neurotransmitter secretion; IGI:MGI.
DR   GO; GO:0007416; P:synapse assembly; IGI:MGI.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR012680; Laminin_G_2.
DR   InterPro; IPR003585; Neurexin-like.
DR   Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 6.
DR   Pfam; PF02210; Laminin_G_2; 6.
DR   SMART; SM00294; 4.1m; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00282; LamG; 6.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 6.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 6.
PE   2: Evidence at transcript level;
KW   EGF-like domain; Membrane; Repeat; Transmembrane; Transmembrane helix.
SQ   SEQUENCE   1587 AA;  175126 MW;  A5D7181B7824D0A0 CRC64;
     MSFTLHSVFF TLKVSIFLGS LVGLCLGLEF MGLPNQWARY LRWDASTRSD LSFQFKTNVS
     TGLLLYLDDG GVCDFLCLSL VDGRVQLRFS MDCAETTVLS NKQVNDSSWH FLMVSRDRVR
     TGLVIDGEGQ SGELRPQRPY MDVVSDLFLG GVPADIRPSA LTLDGVQSMP GFKGLMLDLK
     YGNSEPRLLG SQSVQLEAEG PCGERPCENG GICFLLDGHP TCDCSTTGYG GTLCSEDVSQ
     GPGLSHLMMS EQDVSQGPGL SHLMMSEQAR EENVATFRGS EYLCYDLSQN PIQSSSDEIT
     LSFKTWQRNG LILHTGKSAD YVNLALKDGA VSLVINLGSG AFEAIVEPVN GKFNDNAWHD
     VKVTRNLRQV TISVDGILTT TGYTQEDYTM LGSDDFFYVG GSPSTADLPG SPVSNNFMGC
     LKEVVYKNND IRLELSRLAR IGDTKMKIYG EVVFKCENVA TLDPINFETP EAYISLPKWN
     TKRMGSISFD FRTTEPNGLI LFTHGKPQER KDVRSQKNTK VDFFAVELLD GNLYLLLDMG
     SGTIKVKATQ KKANDGEWYH VDIQRDGRSG TISVNSRRTP FTASGESEIL DLEGDMYLGG
     LPENRAGLIL PTELWTAMLN YGYVGCIRDL FIDGRSKNIR QLAEMQNAAG VKSSCSRMSA
     KQCDSYPCKN NAVCKDGWNR FICDCTGTGY WGRTCEREAS ILSYDGSMYM KVIMPMVMHT
     EAEDVSFRFM SQRAYGLLVA TTSRDSADTL RLELDGGRVK LMVNLDCIRI NCNSSKGPET
     LYAGQKLNDN EWHTVRVVRR GKSLKLTVDD DVAEGTMVGD HTRLEFHNIE TGIMTEKRYI
     SVVPSSFIGH LQSLMFNGLL YIDLCKNGDI DYCELKARFG LRNIIADPVT FKTKSSYLTL
     ATLQAYTSMH LFFQFKTTSA DGFILFNSGD GNDFIAVELV KGYIHYVFDL GNGPNVIKGN
     SDRPLNDNQW HNVVITRDSS NTHSLKVDTK VVTQVINGAK NLDLKGDLYM AGLAQGMYSN
     LPKLVASRDG FQGCLASVDL NGRLPDLIND ALHRSGQIER GCEGPSTTCQ EDSCANQGVC
     MQQWEGFTCD CSMTSYSGNQ CNDPGATYIF GKSGGLILYT WPANDRPSTR SDRLAVGFST
     TVKDGILVRI DSAPGLGDFL QLHIEQGKIG VVFNIGTVDI SIKEERTPVN DGKYHVVRFT
     RNGGNATLQV DNWPVNEHYP TGNTDNERLQ MVKQKIPFKY NRPVEEWLQE KGRQLTIFNT
     QAQIAIGGKD KGRLFQGQLS GLYYDGLKVL NMAAENNPNI KINGSVRLVG EVPSVSGTTQ
     TTSMPPEMST TVMETTTTMA TTTTRKNRST ASIQPTSDDL VSSAECSSDD EDFVECEPST
     DKSLSTSIFE GGYKAHAPKW ESKDFRPNKV SETSRTTTTS LSPELIRFTA SSSSGMVPKL
     PAGKMNNRDL KPQPDIVLLP LPTAYELDST KLKSPLITSP MFRNVPTANP TEPGIRRVPG
     ASEVIRESSS TTGMVVGIVA AAALCILILL YAMYKYRNRD EGSYQVDETR NYISNSAQSN
     GTLMKEKQAS SKSGHKKQKN KDKEYYV
//
ID   Q6P9M9_MOUSE            Unreviewed;       515 AA.
AC   Q6P9M9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   SubName: Full=Poliovirus receptor-related 1;
GN   Name=Pvrl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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CC   -----------------------------------------------------------------------
DR   EMBL; BC060694; AAH60694.1; -; mRNA.
DR   IPI; IPI00420467; -.
DR   RefSeq; NP_067399.2; NM_021424.2.
DR   UniGene; Mm.335096; -.
DR   ProteinModelPortal; Q6P9M9; -.
DR   STRING; Q6P9M9; -.
DR   Ensembl; ENSMUST00000034510; ENSMUSP00000034510; ENSMUSG00000032012.
DR   GeneID; 58235; -.
DR   KEGG; mmu:58235; -.
DR   UCSC; uc009pbj.1; mouse.
DR   CTD; 58235; -.
DR   MGI; MGI:1926483; Pvrl1.
DR   eggNOG; roNOG09599; -.
DR   HOVERGEN; HBG100542; -.
DR   InParanoid; Q6P9M9; -.
DR   OMA; VISKKEW; -.
DR   NextBio; 314269; -.
DR   ArrayExpress; Q6P9M9; -.
DR   Bgee; Q6P9M9; -.
DR   Genevestigator; Q6P9M9; -.
DR   GO; GO:0005913; C:cell-cell adherens junction; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004872; F:receptor activity; IDA:MGI.
DR   GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
DR   GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR   InterPro; IPR013162; CD80_C2-set.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3.
DR   Pfam; PF08205; C2-set_2; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   2: Evidence at transcript level;
KW   Membrane; Receptor; Transmembrane; Transmembrane helix.
SQ   SEQUENCE   515 AA;  57035 MW;  A56FA2C7F8B25AFB CRC64;
     MARMGLAGAA GRWWGLALGL TAFFLPGTHT QVVQVNDSMY GFIGTDVVLH CSFANPLPSV
     KITQVTWQKA SNGSKQNMAI YNPTMGVSVL PPYEKRVEFL RPSFIDGTIR LSGLELEDEG
     MYICEFATFP TGNRESQLNL TVMAKPTNWI EGTRAVLRAR KGQDDKVLVA TCTSANGKPP
     SAVSWETRLK GEAEYQEIRN PNGTVTVISR YRLVPSREAH RQSLACIVNY HLDRFRESLT
     LNVQYEPEVT IEGFDGNWYL QRTDVKLTCK ADANPPATEY HWTTLNGSLP KGVEAQNRTL
     FFRGPITYSL AGTYICEATN PIGTRSGQVE VNITEFPYTP TPEHGRRAGQ MPTAIIGGVA
     GSVLLVLIVV GGIIVALRRR RHTFKGDYST KKHVYGNGYS KAGIPQHHPP MAQNLQYPDD
     SDDEKKAGPL GGSSYEEEEE EEGGGGGERK VGGPHPKYDE DAKRPYFTVD EAEARQDGYG
     DRTLGYQYDP EQLDLAENMV SQNDGSFISK KEWYV
//
ID   HYCCI_MOUSE             Reviewed;         521 AA.
AC   Q6P9N1; Q99NC4;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Hyccin;
DE   AltName: Full=Down-regulated by CTNNB1 protein A;
DE   AltName: Full=Protein FAM126A;
GN   Name=Fam126a; Synonyms=Drctnnb1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC   TISSUE=Spleen;
RX   MEDLINE=20365392; PubMed=10910037;
RA   Kawasoe T., Furukawa Y., Daigo Y., Nishiwaki T., Ishiguro H.,
RA   Fujita M., Satoh S., Miwa N., Nagasawa Y., Miyoshi Y., Ogawa M.,
RA   Nakamura Y.;
RT   "Isolation and characterization of a novel human gene, DRCTNNB1A, the
RT   expression of which is down-regulated by beta-catenin.";
RL   Cancer Res. 60:3354-3358(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May have a role in the beta-catenin/Lef signaling
CC       pathway. May have a role in the process of myelination of the
CC       central and peripheral nervous system (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane (By
CC       similarity).
CC   -!- INDUCTION: Down-regulated by beta-catenin.
CC   -!- SIMILARITY: Belongs to the FAM126 family.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB030242; BAB39850.1; -; mRNA.
DR   EMBL; BC056381; AAH56381.1; -; mRNA.
DR   EMBL; BC060692; AAH60692.1; -; mRNA.
DR   IPI; IPI00118616; -.
DR   RefSeq; NP_444320.2; NM_053090.2.
DR   UniGene; Mm.304976; -.
DR   PhosphoSite; Q6P9N1; -.
DR   PRIDE; Q6P9N1; -.
DR   Ensembl; ENSMUST00000030849; ENSMUSP00000030849; ENSMUSG00000028995.
DR   GeneID; 84652; -.
DR   KEGG; mmu:84652; -.
DR   UCSC; uc008wqv.1; mouse.
DR   CTD; 84652; -.
DR   MGI; MGI:2149839; Fam126a.
DR   GeneTree; ENSGT00390000011295; -.
DR   HOGENOM; HBG715056; -.
DR   HOVERGEN; HBG057270; -.
DR   InParanoid; Q6P9N1; -.
DR   OrthoDB; EOG47D9FZ; -.
DR   NextBio; 350924; -.
DR   ArrayExpress; Q6P9N1; -.
DR   Bgee; Q6P9N1; -.
DR   Genevestigator; Q6P9N1; -.
DR   GermOnline; ENSMUSG00000028995; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR018619; Hyccin.
DR   Pfam; PF09790; Hyccin; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Membrane; Phosphoprotein.
FT   CHAIN         1    521       Hyccin.
FT                                /FTId=PRO_0000080006.
FT   MOD_RES     208    208       Phosphoserine (By similarity).
FT   MOD_RES     306    306       Phosphothreonine (By similarity).
FT   MOD_RES     453    453       Phosphoserine.
FT   CONFLICT     39     39       S -> T (in Ref. 2; AAH56381/AAH60692).
SQ   SEQUENCE   521 AA;  57307 MW;  ABFF9D3156B85229 CRC64;
     MFTSEIGVVE EWLSEFKTLP ETSLPNYATN LKDKSSLVSS LYKVIQEPQS ELLEPVCHQL
     FEFYRSGEEQ LLRFTLQFLP ELMWCYLAVS ASRDVHSSGC IEALLLGVYN LEIVDKHGHS
     KVLSFTIPSL SKPSVYHEPS SIGSMALTES ALSQHGLSKV VYSGPHPQRE MLTAQNRFEV
     LTFLLLCYNA ALTYMPSVSL QSLCQICSRI CVCGYPRQHV RKYRGVSSRI PISSGFMVQM
     LTGVYFAIYN GEWDLAQKAL DDIIYRAQLE LYPEPLLVAN AIKASLPHGA MKSSKEGTRC
     IQVEITPTSS RISRNAVTSM SIRGHRWKRH GDTELTGQEE LMDITEVDEG FYSRAASSTS
     QSGLSNSSHN CSNKTSVGKN QRRSGGSKAG AKERETAGES CRDHFARKQT QRAQSENLEL
     LSLKRLTLTS SQSLPKPSSQ GLAKTAATVF SKSFEQVSGA PVPRSPSPAI GCVAGADANR
     FSACSLQEEK LIYVSERTEL AVKCQAGQQG PPSISVTLSA E
//
ID   Q6P9N8_MOUSE            Unreviewed;       913 AA.
AC   Q6P9N8;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 44.
DE   SubName: Full=Trafficking protein, kinesin binding 2;
GN   Name=Trak2; Synonyms=Als2cr3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC060681; AAH60681.1; -; mRNA.
DR   IPI; IPI00420468; -.
DR   RefSeq; NP_765994.2; NM_172406.3.
DR   UniGene; Mm.222887; -.
DR   ProteinModelPortal; Q6P9N8; -.
DR   PhosphoSite; Q6P9N8; -.
DR   PRIDE; Q6P9N8; -.
DR   Ensembl; ENSMUST00000027186; ENSMUSP00000027186; ENSMUSG00000026028.
DR   Ensembl; ENSMUST00000057069; ENSMUSP00000050118; ENSMUSG00000026028.
DR   GeneID; 70827; -.
DR   KEGG; mmu:70827; -.
DR   UCSC; uc007bcu.1; mouse.
DR   CTD; 70827; -.
DR   MGI; MGI:1918077; Trak2.
DR   eggNOG; roNOG06340; -.
DR   HOGENOM; HBG402997; -.
DR   HOVERGEN; HBG069248; -.
DR   InParanoid; Q6P9N8; -.
DR   OMA; LAEETFR; -.
DR   OrthoDB; EOG48KR9V; -.
DR   PhylomeDB; Q6P9N8; -.
DR   NextBio; 332346; -.
DR   ArrayExpress; Q6P9N8; -.
DR   Bgee; Q6P9N8; -.
DR   Genevestigator; Q6P9N8; -.
DR   InterPro; IPR006933; HAP1_N.
DR   InterPro; IPR022154; Milton.
DR   Pfam; PF04849; HAP1_N; 1.
DR   Pfam; PF12448; Milton; 2.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   913 AA;  101308 MW;  C41DEB19BE516144 CRC64;
     MSQSQNAIFK SRTGEANLMS SNHRDSESIT DVCSNEDLPE VELVNLLEEQ LPQYKLRVDS
     LFLYENQDWA QSSHQQQDAP ETLSPVLAEE TFRYMILGTD RVEQMTKTYN DIDMVTHLLA
     ERDRDLELAA RIGQALLKRN HVLSEQNEAL EEQLGQAFDQ VNQLQHELSK KDELLRIVSI
     ASEESETDSS CSTPLRFNES FSLSQGLLQL DMLHEKLREL EEENMALRSK ACHIKTETFT
     YEEKEQQLVN DCVKELRETN AQMSRMTEEL SGKSDELLRY QEEISSLLSQ IVDLQHKLKE
     HVIEKEELRL HLQASKDAQR QLTMELHELQ DRNMECLGML HESQEEIKEL RSKSGPSAHL
     CFSQSYGVFT GESLAAEIEG TMRKKLSLDE ESVSKQKAQQ KRVFDTVKVA NDTRGRSVTF
     PVLLPIPGSN RSSVIMTAKP FESGVQPAED KTLLSPGGST EVPGNSQPTN PPGSPEDSDL
     ATALHRLSLR RQNYLSEKQF FAEEWERKIQ ILAEQEEEVS SCDAPTENLA SVCTDQSETT
     DLGSASCLRG FMPEKLQIVK PLEGSQTLHH WQQLAQPNLG TILDPRPGVI TKGFTQVPKD
     VVYHISDLEE DEEEGITFQV QQPLQLEQKP ALPTPVTGIF LPPMTSAGGP GTVATSNPGK
     CLSFTNSTFT FTTCRILHPS DITQVTPSSG FPSLACGSSA SSSSNTAVNS PAASYRLSIG
     ESITNRRDST ITFSSTRSLA KLLQERGISA KVYHSPASEN PLLQPCPKAL ATPSTPPNSP
     AQSPCSSPLP FEPRVHVSEN FLASRPAETF LQEMYGLRPS RAPPDVGQLK MNLVDRLKRL
     GIARVVKTPD PQENGKSREA EMGLQKPDPA VYLNSGGSLL CGLRRNQSLP VMMGSFGAPV
     CTTSPKMGIL KED
//
ID   FKB15_MOUSE             Reviewed;        1216 AA.
AC   Q6P9Q6; Q3TSY4; Q5SQG3; Q80TU5;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=FK506-binding protein 15;
DE            Short=FKBP-15;
DE   AltName: Full=133 kDa FK506-binding protein;
DE            Short=133 kDa FKBP;
DE            Short=FKBP-133;
DE   AltName: Full=WASP and FKBP-like;
DE            Short=WAFL;
GN   Name=Fkbp15; Synonyms=Fkbp133, Kiaa0674;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-704.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 213-1216 (ISOFORM B).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   IDENTIFICATION, ALTERNATIVE SPLICING (ISOFORMS A AND B), FUNCTION,
RP   DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=16756961; DOI=10.1016/j.bbrc.2006.05.113;
RA   Nakajima O., Nakamura F., Yamashita N., Tomita Y., Suto F., Okada T.,
RA   Iwamatsu A., Kondo E., Fujisawa H., Takei K., Goshima Y.;
RT   "FKBP133: a novel mouse FK506-binding protein homolog alters growth
RT   cone morphology.";
RL   Biochem. Biophys. Res. Commun. 346:140-149(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1190, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1091; THR-1093; SER-1157
RP   AND SER-1159, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1091; THR-1093; SER-1157
RP   AND SER-1159, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306 AND SER-340, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Involved in the transport of early endosomes at the
CC       level of transition between microfilament-based and microtubule-
CC       based movement (By similarity). May be involved in the
CC       cytoskeletal organization of neuronal growth cones. Seems to be
CC       inactive as a PPIase.
CC   -!- SUBUNIT: Interacts with WIP and actin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell projection, axon. Early
CC       endosome. Note=Present in axons and neuronal growth cones.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=Q6P9Q6-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=Q6P9Q6-2; Sequence=VSP_027759;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, with highest levels in the
CC       granular cell layer of cerebellum and in the granule cell layer of
CC       dentate gyrus.
CC   -!- DEVELOPMENTAL STAGE: Strongly expressed in the developing nervous
CC       system at E18.5. Present in brain, heart, lung, kidney and thymus
CC       at E18.5 (at protein level).
CC   -!- DOMAIN: The PPIase FKBP-type domain seems to be inactive both for
CC       FK506-binding and enzymatic activity.
CC   -!- DOMAIN: The central coiled-coil region is responsible for
CC       association with early endosomes (By similarity).
CC   -!- SIMILARITY: Belongs to the FKBP-type PPIase family.
CC   -!- SIMILARITY: Contains 1 PPIase FKBP-type domain.
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DR   EMBL; AL683829; CAI25942.1; -; Genomic_DNA.
DR   EMBL; AL732548; CAI25942.1; JOINED; Genomic_DNA.
DR   EMBL; AL732548; CAI26145.1; -; Genomic_DNA.
DR   EMBL; AL683829; CAI26145.1; JOINED; Genomic_DNA.
DR   EMBL; BC060651; AAH60651.1; -; mRNA.
DR   EMBL; AK161705; BAE36541.1; -; mRNA.
DR   EMBL; AK122343; BAC65625.1; -; mRNA.
DR   IPI; IPI00458068; -.
DR   IPI; IPI00929847; -.
DR   RefSeq; NP_001038993.1; NM_001045528.1.
DR   UniGene; Mm.357792; -.
DR   HSSP; Q02790; 1N1A.
DR   ProteinModelPortal; Q6P9Q6; -.
DR   SMR; Q6P9Q6; 188-289.
DR   STRING; Q6P9Q6; -.
DR   PhosphoSite; Q6P9Q6; -.
DR   PRIDE; Q6P9Q6; -.
DR   Ensembl; ENSMUST00000084527; ENSMUSP00000081575; ENSMUSG00000066151.
DR   GeneID; 338355; -.
DR   KEGG; mmu:338355; -.
DR   CTD; 338355; -.
DR   MGI; MGI:2444782; Fkbp15.
DR   GeneTree; ENSGT00530000064286; -.
DR   HOGENOM; HBG447023; -.
DR   HOVERGEN; HBG067251; -.
DR   InParanoid; Q6P9Q6; -.
DR   OMA; ASAKDEH; -.
DR   ArrayExpress; Q6P9Q6; -.
DR   Bgee; Q6P9Q6; -.
DR   CleanEx; MM_FKBP15; -.
DR   Genevestigator; Q6P9Q6; -.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0030426; C:growth cone; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   Pfam; PF00254; FKBP_C; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Alternative splicing; Cell projection;
KW   Coiled coil; Cytoplasm; Endocytosis; Endosome; Phosphoprotein;
KW   Transport.
FT   CHAIN         1   1216       FK506-binding protein 15.
FT                                /FTId=PRO_0000299557.
FT   DOMAIN      196    289       PPIase FKBP-type.
FT   REGION       71    168       Important for function in growth cone
FT                                organization.
FT   COILED      519    790       Potential.
FT   COILED      820    865       Potential.
FT   COMPBIAS    929    941       Glu-rich.
FT   COMPBIAS    944   1045       Pro-rich.
FT   COMPBIAS   1203   1211       Poly-Asp.
FT   MOD_RES      91     91       N6-acetyllysine (By similarity).
FT   MOD_RES     306    306       Phosphoserine.
FT   MOD_RES     310    310       Phosphoserine (By similarity).
FT   MOD_RES     340    340       Phosphoserine.
FT   MOD_RES     342    342       Phosphoserine (By similarity).
FT   MOD_RES     344    344       Phosphoserine (By similarity).
FT   MOD_RES     948    948       Phosphoserine (By similarity).
FT   MOD_RES    1091   1091       Phosphoserine.
FT   MOD_RES    1093   1093       Phosphothreonine.
FT   MOD_RES    1108   1108       Phosphoserine (By similarity).
FT   MOD_RES    1157   1157       Phosphoserine.
FT   MOD_RES    1159   1159       Phosphoserine.
FT   MOD_RES    1190   1190       Phosphoserine.
FT   VAR_SEQ    1190   1216       SMKGRPPPTPLFGDDDDDDDDDIGWLG -> VRRPQALLSP
FT                                HTTTWGLFPAGSETRKGVCWWLVSWTLCTGPCGSKLGAQSG
FT                                QLCKHDGDGQLPLYS (in isoform B).
FT                                /FTId=VSP_027759.
FT   CONFLICT    652    652       H -> R (in Ref. 3; BAE36541).
SQ   SEQUENCE   1216 AA;  132961 MW;  8F8130D5038122FF CRC64;
     MFGAGDEDDT DFLSPSGGAK LASLFGLDQA TMGHGNEFFQ YTAPKQPKKG QGTAAGNQTA
     PKPAPATTGT SSVLFATAVH AYRYINGQYA KQGKFGAAVL GNHTSREYRI LLYISQQQPV
     TVATIHLNFE LMVRPNNYST FYDDQRQNWS IMFESEKAAV SFNKQVCVAK CNSISSLDAV
     LCQDLVAAEG PAVETGDSLE VAYTGWLLQN HVLGQVFDST ANKDKPLRLK LGSGKVVKGL
     EDGLLGMKKG GKRLIITPSA CAAGSEGVIG WTQPTDSILV FEVEVRRVKF ARDSGSDGHS
     VSSRDSAAPS PIPASDSLSA DPVVTPLPLP LKPGEPGLRS KSNSLSEQLT VNSNPDTVKA
     KLISRMAKMG QPMLPILPPQ LDSNDSETED ATVLRGAGQS LVTPSIQPSL QPAHPVLPQM
     ASQAPQPSGS GLQTPSAALM QAVSLDSHSA VSGNAQNFQP YAGVQAYAYP QTPSVTSQLQ
     PVRPLYPAPL SQAPHFQGSG DMMSFLMTEA RQHNTEIRMA VNKVADKMDH LMTKVEELQK
     HSSGNSMLLP SMSVTMETSM IMSNIQRIIQ ENERLKQELL EKSSRIEEQN DKISDLIERN
     QRYVEQSNLM MEKRNNSLQT ATENTQARIL HAEQEKAKVT EELAAATAQV SHLQLKMTAH
     QKKETELQLQ LTDNLKETDL LRGHVTRLQA DLSELREASE QTQTKFKSEK QSRRQLELKV
     TSLEEELTDL RAEKTSLEKN LSERKKKSAQ ERCQAEAEMD EIRKSHQEEL DRLRQLLKKA
     RVSTDQAAAE QLTLAQAELQ SQWEAKCEQL LASARDEHLQ QYREVCAQRD AHQQKLALLQ
     DECLALQAQI AAFTEQKEHM QRLEKTKSQA PAGRAAADPS EKVKKIMNQV FQSLRGEFEL
     EESYDGGTIL RTIMHTIKMV TLQLLNHQEE EEEEEEEEEE EKKPLRPSLE QPGPATPGMP
     PAPPSGETQE APEVLPEQVV GETTPLPLQA LPTPENGAQT RKGEPAEAEV PSEIKDSSLP
     PQPAGIPAHR VLGPPTSIPP KPPGPVTMDS ESEEMLAADQ RTVQPNGLLG EEHVREVATD
     GLLQGNSRRL SLTPDPEKGE PPALDPESQG GEAQPPECKQ AEDVSSSGPR ETLLDTELAS
     AAAGTSLRHN QDSQHCSLSG DEEDELFKGA TLKVPRPTAQ PEEEDEDEVS MKGRPPPTPL
     FGDDDDDDDD DIGWLG
//
ID   OXSR1_MOUSE             Reviewed;         527 AA.
AC   Q6P9R2; Q8BVZ9; Q8C0B9;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Serine/threonine-protein kinase OSR1;
DE            EC=2.7.11.1;
DE   AltName: Full=Oxidative stress-responsive 1 protein;
GN   Name=Oxsr1; Synonyms=Osr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 48-527.
RC   STRAIN=C57BL/6J; TISSUE=Head, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH SLA12A1; SLC12A2 AND SLC12A6.
RX   MEDLINE=22384319; PubMed=12386165; DOI=10.1074/jbc.M208108200;
RA   Piechotta K., Lu J., Delpire E.;
RT   "Cation chloride cotransporters interact with the stress-related
RT   kinases Ste20-related proline-alanine-rich kinase (SPAK) and oxidative
RT   stress response 1 (OSR1).";
RL   J. Biol. Chem. 277:50812-50819(2002).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=14707132; DOI=10.1074/jbc.M313562200;
RA   Chen W., Yazicioglu M., Cobb M.H.;
RT   "Characterization of OSR1, a member of the mammalian Ste20p/germinal
RT   center kinase subfamily.";
RL   J. Biol. Chem. 279:11129-11136(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Regulates downstream kinases in response to
CC       environmental stress. May also have a function in regulating the
CC       actin cytoskeleton.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: By autophosphorylation on threonine (By
CC       similarity).
CC   -!- SUBUNIT: Binds to and phosphorylates PAK1. Interacts with chloride
CC       channel proteins SLC12A6 isoform 2, SLC12A1 and SLC12A2 but not
CC       with SLC12A4 and SLC12A7, possibly establishing sensor/signaling
CC       modules that initiate the cellular response to environmental
CC       stress. Binds to and phosphorylates RELL1, RELL2 AND RELT (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues
CC       examined, except thymus.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC27551.1; Type=Erroneous initiation;
CC       Sequence=BAC35996.1; Type=Erroneous initiation;
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DR   EMBL; BC060645; AAH60645.1; -; mRNA.
DR   EMBL; AK031790; BAC27551.1; ALT_INIT; mRNA.
DR   EMBL; AK075837; BAC35996.1; ALT_INIT; mRNA.
DR   IPI; IPI00223738; -.
DR   RefSeq; NP_598746.1; NM_133985.1.
DR   UniGene; Mm.293565; -.
DR   ProteinModelPortal; Q6P9R2; -.
DR   SMR; Q6P9R2; 7-295, 433-527.
DR   IntAct; Q6P9R2; 5.
DR   STRING; Q6P9R2; -.
DR   PhosphoSite; Q6P9R2; -.
DR   PRIDE; Q6P9R2; -.
DR   Ensembl; ENSMUST00000040853; ENSMUSP00000042155; ENSMUSG00000036737.
DR   GeneID; 108737; -.
DR   KEGG; mmu:108737; -.
DR   UCSC; uc009sao.1; mouse.
DR   CTD; 108737; -.
DR   MGI; MGI:1917378; Oxsr1.
DR   eggNOG; roNOG10799; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108518; -.
DR   InParanoid; Q6P9R2; -.
DR   OMA; KMLQRAP; -.
DR   OrthoDB; EOG4KH2VM; -.
DR   PhylomeDB; Q6P9R2; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 361275; -.
DR   ArrayExpress; Q6P9R2; -.
DR   Bgee; Q6P9R2; -.
DR   CleanEx; MM_OSR1; -.
DR   CleanEx; MM_OXSR1; -.
DR   Genevestigator; Q6P9R2; -.
DR   GermOnline; ENSMUSG00000036737; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0007243; P:intracellular protein kinase cascade; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    527       Serine/threonine-protein kinase OSR1.
FT                                /FTId=PRO_0000086457.
FT   DOMAIN       17    291       Protein kinase.
FT   NP_BIND      23     31       ATP (By similarity).
FT   ACT_SITE    146    146       Proton acceptor (By similarity).
FT   BINDING      46     46       ATP (By similarity).
FT   MOD_RES     339    339       Phosphoserine.
FT   MOD_RES     347    347       Phosphoserine (By similarity).
FT   MOD_RES     427    427       Phosphoserine (By similarity).
FT   CONFLICT    201    201       V -> F (in Ref. 2; BAC27551).
SQ   SEQUENCE   527 AA;  58214 MW;  72A09F0D732375E1 CRC64;
     MSEDSSALPW SINRDDYELQ EVIGSGATAV VQAAYCAPKK ERVAIKRINL EKCQTSMDEL
     LKEIQAMSQC HHPNIVSYYT SFVVKDELWL VMKLLSGGSV LDIIKHIVAK GEHKSGVLDE
     PTIATILREV LEGLEYLHKN GQIHRDVKAG NILLGEDGSV QIADFGVSAF LATGGDITRN
     KVRKTFVGTP CWMAPEVMEQ VRGYDFKADI WSFGITAIEL ATGAAPYHKY PPMKVLMLTL
     QNDPPSLETG VQDKEMLKKY GKSFRKMISL CLQKDPEKRP TAAELLRHKF FQKAKNKEFL
     QEKILQRAPT ISERSKKVRR VPGSSGRLHK TEDGGWEWSD DEFDEESEEG RAAISQLRSP
     RVKDSLSSSE LFAAAEPMGT LLQVPEQISA HLPQPAGQMP TQPAQVSLLP PAEPAKPAQA
     QSSGERSQET KIPISLVLRL RNSKKELNDI RFEFTPGRDT AEGVSQELIS AGLVDGRDLV
     IVAANLQKIV EEPQSNRSVT FKLASGVEGS DIPDDGKLIG FAQLSIS
//
ID   ARHGI_MOUSE             Reviewed;        1021 AA.
AC   Q6P9R4; Q6A055; Q8BYA4; Q8K227;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Rho guanine nucleotide exchange factor 18;
GN   Name=Arhgef18; Synonyms=Kiaa0521;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, and Czech II; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 244-1021 (ISOFORM 2).
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
CC   -!- FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for
CC       RhoA GTPases. May play a role in actin cytoskeleton reorganization
CC       in different tissues since its activation induces formation of
CC       actin stress fibers. Also act as a GEF for RAC1, inducing
CC       production of reactive oxygen species (ROS). Does not act as a GEF
CC       for CDC42. The G protein beta-gamma (Gbetagamma) subunits of
CC       heterotrimeric G proteins act as activators, explaining the
CC       integrated effects of LPA and other G-protein coupled receptor
CC       agonists on actin stress fiber formation, cell shape change and
CC       ROS production (By similarity).
CC   -!- SUBUNIT: Interacts with SEPT9; interaction may inhibit GEF
CC       activity. Interacts with Gbetagamma subunits GNB1 and GNG2 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Colocalizes with actin
CC       stress fibers (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6P9R4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6P9R4-2; Sequence=VSP_034319;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q6P9R4-3; Sequence=VSP_034317, VSP_034318;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
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DR   EMBL; AK041423; BAC30940.1; -; mRNA.
DR   EMBL; BC034512; AAH34512.1; -; mRNA.
DR   EMBL; BC060639; AAH60639.1; -; mRNA.
DR   EMBL; AK172963; BAD32241.1; -; mRNA.
DR   IPI; IPI00420477; -.
DR   IPI; IPI00466979; -.
DR   IPI; IPI00896050; -.
DR   RefSeq; NP_598723.3; NM_133962.3.
DR   UniGene; Mm.170461; -.
DR   HSSP; O15085; 1XCG.
DR   ProteinModelPortal; Q6P9R4; -.
DR   SMR; Q6P9R4; 80-446.
DR   PhosphoSite; Q6P9R4; -.
DR   PRIDE; Q6P9R4; -.
DR   Ensembl; ENSMUST00000004684; ENSMUSP00000004684; ENSMUSG00000004568.
DR   GeneID; 102098; -.
DR   KEGG; mmu:102098; -.
DR   UCSC; uc009krj.1; mouse.
DR   CTD; 102098; -.
DR   MGI; MGI:2142567; Arhgef18.
DR   eggNOG; roNOG13550; -.
DR   GeneTree; ENSGT00600000084265; -.
DR   HOGENOM; HBG444567; -.
DR   HOVERGEN; HBG104846; -.
DR   InParanoid; Q6P9R4; -.
DR   OrthoDB; EOG466VKM; -.
DR   NextBio; 355276; -.
DR   ArrayExpress; Q6P9R4; -.
DR   Bgee; Q6P9R4; -.
DR   Genevestigator; Q6P9R4; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR015721; RhoGEF-like.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   PANTHER; PTHR22825; RhoGEF_like; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   PROSITE; PS00741; DH_1; FALSE_NEG.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Cytoplasm;
KW   Guanine-nucleotide releasing factor; Phosphoprotein.
FT   CHAIN         1   1021       Rho guanine nucleotide exchange factor
FT                                18.
FT                                /FTId=PRO_0000341416.
FT   DOMAIN      101    298       DH.
FT   DOMAIN      339    441       PH.
FT   COILED      700    800       Potential.
FT   MOD_RES      51     51       Phosphoserine (By similarity).
FT   MOD_RES     577    577       Phosphoserine (By similarity).
FT   MOD_RES     952    952       Phosphoserine (By similarity).
FT   MOD_RES     954    954       Phosphoserine (By similarity).
FT   MOD_RES     975    975       Phosphoserine (By similarity).
FT   VAR_SEQ     534    618       IEGIQSLICQRHLGSTSSQVEEGSVSAGLPRRAETFGGYDS
FT                                VGSPSKGGSFKRKVSNSDLRPQDWQGPASSPDSRPCDNSAP
FT                                SGC -> SKLASPLSYAMIFQGGLPGGPKPGSVLYCSPRTT
FT                                VILLFFIIQGMESSMCNGSTAELYPNPLSTYSTNAPWVTLC
FT                                SGVGGGGDKA (in isoform 3).
FT                                /FTId=VSP_034317.
FT   VAR_SEQ     619   1021       Missing (in isoform 3).
FT                                /FTId=VSP_034318.
FT   VAR_SEQ     926   1021       ASFDLKQQLLLSKFIGKDESASRNRRSLSPVLPAAHGSAPA
FT                                SDPCFPAPSPAPAATPPEAFKFGGTSLPPVSPASSLPTTPL
FT                                ATTDEVSKEDVIFF -> GELHPTPTTQRSCTPLPVDLSQQ
FT                                HIWNADREADRQAPVCARRQRGSLFQLHFCCDKIP (in
FT                                isoform 2).
FT                                /FTId=VSP_034319.
FT   CONFLICT     53     53       N -> S (in Ref. 1; BAC30940).
FT   CONFLICT    217    217       H -> Q (in Ref. 1; BAC30940).
FT   CONFLICT    967    967       S -> P (in Ref. 2; AAH34512).
SQ   SEQUENCE   1021 AA;  114345 MW;  B31A0786C526AE76 CRC64;
     MTISQKGGLQ PTPSPAGSGV RLGPIAGDMD EADSVFLKLK QTADDSLSLT SSNAESVFIE
     DPYIASLRCE IESDAHEFEA ESWSLSVDLA YAKKQKKEVV KRQDVLYELM QTEAHHVRTL
     KIMLKVYSRA LQEELQFSGQ AVSRLFPCAD DLLDMHSHFL ARLKERRQEF LEEGSDRNYV
     IQKIGDVLVQ QFSGETGERM KEKYAVFCSG HNDAVGHYKL LLQQSKKFQN LIKKIGNFSI
     VRRLGVQECI LLVTQRITKY PVLVERIIQN TEAGTEDYKD LSQALSLIKD IISQVDAKVS
     EYEKDQRLKE IAAKTDQKSS GKLKNGLTFR KEDMLQQRQL HLEGALCWKS TSGRLKDVLA
     VLLTDVLLLL QEKDQKYVFA SVDSKPPVIS LQKLIVREVA NEEKAMFLIS ASMQGPEMYE
     MYTSSKEDRN IWMAHIRRAV ESCPDEEEDV FSEAEEKKIA EARTMKLQEF QERLSLKDQL
     IAQSLLEKQQ IYLEMAQLSG LEESAQNRGL FRGGGDPSET LRGEQILRSA MSEIEGIQSL
     ICQRHLGSTS SQVEEGSVSA GLPRRAETFG GYDSVGSPSK GGSFKRKVSN SDLRPQDWQG
     PASSPDSRPC DNSAPSGCCE ESPQAVEMPS TESLPTVLEL ELVHRVQTLS QLLLSLQAVI
     AQQDSYVEMQ RTAIQEREKQ FRLQSTRGNL LLEQERQRNF EKQREERAGV EKLQSQLRQE
     QQRWERERAR QQQELELAGA RLQEREGEAR QMRQRLDQER TELERQRQAY QHDLERLREA
     QRAVDRERER LELLRRFKKQ NTVPGALPPE VLAEAQPASH PPSFNGDGLE GHSAPAKAPG
     TQGSAMLHGT GPDNVERPEV ARWDSAPPES RPAKSDVPIQ LLSATNQIQR QTAVQQQIPT
     KLAASTKGGK EKGSKSRGSQ RWESSASFDL KQQLLLSKFI GKDESASRNR RSLSPVLPAA
     HGSAPASDPC FPAPSPAPAA TPPEAFKFGG TSLPPVSPAS SLPTTPLATT DEVSKEDVIF
     F
//
ID   MTSSL_MOUSE             Reviewed;         715 AA.
AC   Q6P9S0; Q8C7B7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=MTSS1-like protein;
GN   Name=Mtss1l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 315-715.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257 AND SER-261, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May function in actin bundling.
CC   -!- SIMILARITY: Belongs to the MTSS1 family.
CC   -!- SIMILARITY: Contains 1 IMD (IRSp53/MIM homology) domain.
CC   -!- SIMILARITY: Contains 1 WH2 domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC060632; AAH60632.1; -; mRNA.
DR   EMBL; AK052172; BAC34868.1; -; mRNA.
DR   IPI; IPI00387602; -.
DR   RefSeq; NP_941027.1; NM_198625.1.
DR   UniGene; Mm.334807; -.
DR   ProteinModelPortal; Q6P9S0; -.
DR   SMR; Q6P9S0; 5-241, 685-713.
DR   PhosphoSite; Q6P9S0; -.
DR   PRIDE; Q6P9S0; -.
DR   Ensembl; ENSMUST00000052457; ENSMUSP00000050211; ENSMUSG00000033763.
DR   GeneID; 244654; -.
DR   KEGG; mmu:244654; -.
DR   NMPDR; fig|10090.3.peg.19247; -.
DR   UCSC; uc009nkx.1; mouse.
DR   CTD; 244654; -.
DR   MGI; MGI:3039591; Mtss1l.
DR   eggNOG; roNOG10381; -.
DR   GeneTree; ENSGT00390000002637; -.
DR   HOGENOM; HBG715988; -.
DR   HOVERGEN; HBG052530; -.
DR   InParanoid; Q6P9S0; -.
DR   OMA; WGSPSPE; -.
DR   OrthoDB; EOG4JHCFB; -.
DR   PhylomeDB; Q6P9S0; -.
DR   NextBio; 386361; -.
DR   ArrayExpress; Q6P9S0; -.
DR   Bgee; Q6P9S0; -.
DR   CleanEx; MM_BC060632; -.
DR   Genevestigator; Q6P9S0; -.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0008093; F:cytoskeletal adaptor activity; IEA:InterPro.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:InterPro.
DR   GO; GO:0046847; P:filopodium assembly; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR013606; IRSp53/MIM_homology_IMD.
DR   Gene3D; G3DSA:1.20.1270.80; IRSp53/MIM_homology_IMD; 1.
DR   Pfam; PF08397; IMD; 1.
DR   PROSITE; PS51338; IMD; 1.
DR   PROSITE; PS51082; WH2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Actin-binding; Coiled coil; Phosphoprotein.
FT   CHAIN         1    715       MTSS1-like protein.
FT                                /FTId=PRO_0000319611.
FT   DOMAIN        1    249       IMD.
FT   DOMAIN      687    704       WH2.
FT   COILED      134    156       Potential.
FT   COMPBIAS    249    339       Ser-rich.
FT   MOD_RES     257    257       Phosphothreonine.
FT   MOD_RES     260    260       Phosphoserine (By similarity).
FT   MOD_RES     261    261       Phosphoserine.
FT   MOD_RES     351    351       Phosphoserine (By similarity).
FT   MOD_RES     404    404       Phosphoserine (By similarity).
FT   MOD_RES     419    419       Phosphoserine.
FT   MOD_RES     542    542       Phosphoserine (By similarity).
FT   MOD_RES     564    564       Phosphoserine (By similarity).
FT   MOD_RES     575    575       Phosphoserine.
FT   MOD_RES     587    587       Phosphoserine (By similarity).
FT   MOD_RES     597    597       Phosphoserine (By similarity).
FT   MOD_RES     602    602       Phosphoserine (By similarity).
FT   MOD_RES     606    606       Phosphothreonine (By similarity).
FT   MOD_RES     610    610       Phosphoserine (By similarity).
SQ   SEQUENCE   715 AA;  76844 MW;  04AE3F9004A3561C CRC64;
     METAEKECGA LGGLFQAIVN DMKSSYPIWE DFNSKAAKLH SQLRTTVLAA VAFLDAFQKV
     ADMATNTRGA TRDIGSALTR MCMRHRSIET KLRQFTNALL ESLINPLQER IEDWKKSANQ
     LDKDHAKEYK RARHEIKKKS SDTLKLQKKA RKGKGDLQPQ LDSALQDVND MYLLLEETEK
     QAVRRALIEE RGRFCTFITF LQPVVNGELT MLGEITHLQG IIDDLVVLTA DPHKLPPASE
     QVIKDLKGSD YSWSYQTPPS SPSSSNSRKS SMCSLAQPAT TRLSSVSSHD SGFVSQDPTY
     SKPPSPMPSD ITSQKSSSSA SSEASETCQS VSECSSPTSD WTKAGPHEQP SATTLQRRKD
     RVEHLRDTEP GPTGGGTVGS SGEEVPRTRM SPATIAAKHG EEVSPAASDL AMVLTRGLSL
     EHQKSSRDSL QYSSGYSTQT TTPSCSEDTI PSQGSDYDCY SVNGDADSEG PPEFDKSSTI
     PRNSNIAQNY RRLIQTKRPA STAGLPTAGL PTAMGLPSGA PPGVATIRRT PSTKPTVRRA
     LSSAGPIPIR PPIVPVKTPT VPDSPGYVGP TRAGSEECVF YTDEVASPLA PDLAKASPKR
     LSLPNTAWGS QSPEVASYGG GAAVGLATED EEQQLAANRH SLVEKLGELV AGAHALGEGQ
     FPFPTALSAT PSEETPTPPP AATSDPPAED MLVAIRRGVR LRRTVTNDRS APRIL
//
ID   ATLA2_MOUSE             Reviewed;         583 AA.
AC   Q6PA06; Q3UX01; Q7TMM3;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Atlastin-2;
DE            EC=3.6.5.-;
DE   AltName: Full=ADP-ribosylation factor-like protein 6-interacting protein 2;
DE            Short=ARL-6-interacting protein 2;
DE            Short=Aip-2;
GN   Name=Atl2; Synonyms=Arl6ip2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Oocyte;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH REEP5 AND RTN3.
RX   PubMed=19665976; DOI=10.1016/j.cell.2009.05.025;
RA   Hu J., Shibata Y., Zhu P.-P., Voss C., Rismanchi N., Prinz W.A.,
RA   Rapoport T.A., Blackstone C.;
RT   "A class of dynamin-like GTPases involved in the generation of the
RT   tubular ER network.";
RL   Cell 138:549-561(2009).
CC   -!- FUNCTION: GTPase tethering membranes through formation of trans-
CC       homooligomer and mediating homotypic fusion of endoplasmic
CC       reticulum membranes. Functions in endoplasmic reticulum tubular
CC       network biogenesis (By similarity).
CC   -!- SUBUNIT: Interacts with REEP5 and RTN3.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6PA06-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PA06-2; Sequence=VSP_025311;
CC   -!- SIMILARITY: Belongs to the GBP family. Atlastin subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK135988; BAE22763.1; -; mRNA.
DR   EMBL; BC060501; AAH60501.1; -; mRNA.
DR   IPI; IPI00461142; -.
DR   IPI; IPI00474125; -.
DR   RefSeq; NP_062691.3; NM_019717.2.
DR   RefSeq; NP_835151.2; NM_178050.3.
DR   UniGene; Mm.175403; -.
DR   ProteinModelPortal; Q6PA06; -.
DR   SMR; Q6PA06; 57-470.
DR   STRING; Q6PA06; -.
DR   PhosphoSite; Q6PA06; -.
DR   PRIDE; Q6PA06; -.
DR   Ensembl; ENSMUST00000068282; ENSMUSP00000064758; ENSMUSG00000059811.
DR   Ensembl; ENSMUST00000112437; ENSMUSP00000108056; ENSMUSG00000059811.
DR   GeneID; 56298; -.
DR   KEGG; mmu:56298; -.
DR   UCSC; uc008dqe.1; mouse.
DR   CTD; 56298; -.
DR   MGI; MGI:1929492; Atl2.
DR   eggNOG; roNOG09496; -.
DR   HOGENOM; HBG443778; -.
DR   HOVERGEN; HBG062891; -.
DR   InParanoid; Q6PA06; -.
DR   OMA; CKSMEQV; -.
DR   OrthoDB; EOG4255SJ; -.
DR   PhylomeDB; Q6PA06; -.
DR   NextBio; 312226; -.
DR   ArrayExpress; Q6PA06; -.
DR   Bgee; Q6PA06; -.
DR   Genevestigator; Q6PA06; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; ISS:UniProtKB.
DR   GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR   InterPro; IPR003191; Guanylate-bd_C.
DR   InterPro; IPR015894; Guanylate-bd_N.
DR   Gene3D; G3DSA:1.20.1000.10; Guanylate-bd_C; 1.
DR   Pfam; PF02263; GBP; 1.
DR   Pfam; PF02841; GBP_C; 1.
DR   SUPFAM; SSF48340; GBP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Endoplasmic reticulum;
KW   GTP-binding; Hydrolase; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    583       Atlastin-2.
FT                                /FTId=PRO_0000287107.
FT   TOPO_DOM      1    476       Cytoplasmic (By similarity).
FT   TRANSMEM    477    497       Helical; (Potential).
FT   TOPO_DOM    498    499       Lumenal (Potential).
FT   TRANSMEM    500    520       Helical; (Potential).
FT   TOPO_DOM    521    583       Cytoplasmic (By similarity).
FT   NP_BIND     101    108       GTP (Potential).
FT   NP_BIND     173    177       GTP (Potential).
FT   COILED      256    284       Potential.
FT   COMPBIAS     18     21       Poly-Arg.
FT   MOD_RES      24     24       Phosphoserine (By similarity).
FT   MOD_RES     314    314       N6-acetyllysine (By similarity).
FT   MOD_RES     321    321       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1    195       Missing (in isoform 2).
FT                                /FTId=VSP_025311.
FT   CONFLICT    466    466       K -> R (in Ref. 1; BAE22763).
SQ   SEQUENCE   583 AA;  66224 MW;  9530B0F2077FE2D3 CRC64;
     MAEGDEAARR QQPQQGLRRR RQTSDSSVGV NHVSSTTSLG EDYEDDDLVN SDEVMKKPCP
     VQIVLAHEDD HNFELDEEAL EQILLQEHIR DLNIVVVSVA GAFRKGKSFL LDFMLRYMYN
     KDSQSWIGGN NEPLTGFTWR GGCERETTGI QVWNEVFVID RPNGTKVAVL LMDTQGAFDS
     QSTIKDCATV FALSTMTSSV QVYNLSQNIQ EDDLQHLQLF TEYGRLAMEE IYQKPFQTLM
     FLIRDWSYPY EHSYGLEGGK QFLEKRLQVK QNQHEELQNV RKHIHNCFSN LGCFLLPHPG
     LKVATNPSFD GRLKDIDEDF KRELRNLVPL LLAPENLVEK EISGSKVTCR DLVEYFKAYI
     KIYQGEELPH PKSMLQATAE ANNLAAVAGA RDVYCKSMEQ VCGGDKPYIA PSDLERKHLD
     LKEVALKQFR SVKKMGGDEF CRRYQDQLEA EIEETYANFI KHNDGKNIFY AARTPATLFA
     VMFAMYIISG LTGFIGLNSI AVLCNLVMGL ALTSLCTWAY VKYSGEFREI GTMIDQIAET
     LWEQVLKPLG DNLMEENIRQ SVTNSIKAGL TDQVSHHARL KTD
//
ID   BCR_MOUSE               Reviewed;        1270 AA.
AC   Q6PAJ1; Q61339; Q6ZPE5; Q99LW5;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Breakpoint cluster region protein;
DE            EC=2.7.11.1;
GN   Name=Bcr; Synonyms=Kiaa3017;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 212-1270.
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 276-428.
RX   MEDLINE=91088292; PubMed=2263470; DOI=10.1093/nar/18.23.7119;
RA   Zhu Q.S., Heisterkamp N., Groffen J.;
RT   "Unique organization of the human BCR gene promoter.";
RL   Nucleic Acids Res. 18:7119-7125(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 561-1270.
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [5]
RP   POSSIBLE INTERACTION WITH CCPG1.
RX   PubMed=17000758; DOI=10.1128/MCB.00670-06;
RA   Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P.;
RT   "Ccpg1, a novel scaffold protein that regulates the activity of the
RT   Rho guanine nucleotide exchange factor Dbs.";
RL   Mol. Cell. Biol. 26:8964-8975(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 AND TYR-247, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: GTPase-activating protein for RAC1 and CDC42. Promotes
CC       the exchange of RAC or CDC42-bound GDP by GTP, thereby activating
CC       them. Displays serine/threonine kinase activity (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Homotetramer. Interacts with PDZK1 (By similarity). May
CC       interact with CCPG1.
CC   -!- DOMAIN: The region involved in binding to ABL1 SH2-domain is rich
CC       in serine residues and needs to be Ser/Thr phosphorylated prior to
CC       SH2 binding. This region is essential for the activation of the
CC       ABL1 tyrosine kinase (By similarity).
CC   -!- DOMAIN: The DH domain is involved in interaction with CCPG1.
CC   -!- PTM: Autophosphorylated (By similarity).
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC160402; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC002193; AAH02193.1; -; mRNA.
DR   EMBL; BC060270; AAH60270.1; -; mRNA.
DR   EMBL; X52831; CAA37013.1; -; Genomic_DNA.
DR   EMBL; AK129482; BAC98292.1; -; mRNA.
DR   IPI; IPI00380817; -.
DR   PIR; S14194; S14193.
DR   UniGene; Mm.478843; -.
DR   ProteinModelPortal; Q6PAJ1; -.
DR   SMR; Q6PAJ1; 5-66, 495-695, 705-764, 909-1008, 1047-1253.
DR   STRING; Q6PAJ1; -.
DR   PhosphoSite; Q6PAJ1; -.
DR   PRIDE; Q6PAJ1; -.
DR   Ensembl; ENSMUST00000041070; ENSMUSP00000039247; ENSMUSG00000009681.
DR   UCSC; uc007fqb.1; mouse.
DR   MGI; MGI:88141; Bcr.
DR   HOGENOM; HBG446960; -.
DR   HOVERGEN; HBG004165; -.
DR   InParanoid; Q6PAJ1; -.
DR   OrthoDB; EOG4FFD11; -.
DR   BRENDA; 2.7.11.1; 244.
DR   ArrayExpress; Q6PAJ1; -.
DR   Bgee; Q6PAJ1; -.
DR   CleanEx; MM_BCR; -.
DR   Genevestigator; Q6PAJ1; -.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030675; F:Rac GTPase activator activity; IGI:MGI.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IGI:MGI.
DR   GO; GO:0007420; P:brain development; IGI:MGI.
DR   GO; GO:0042472; P:inner ear morphogenesis; IGI:MGI.
DR   GO; GO:0030336; P:negative regulation of cell migration; IGI:MGI.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
DR   GO; GO:0043314; P:negative regulation of neutrophil degranulation; IGI:MGI.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IGI:MGI.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; IGI:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR015123; Bcr-Abl_oncoprot_oligo.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Pfam; PF09036; Bcr-Abl_Oligo; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF69036; Bcr-Abl_oncoprot_oligo; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; GTPase activation; Guanine-nucleotide releasing factor;
KW   Kinase; Nucleotide-binding; Phosphoprotein; Proto-oncogene;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1   1270       Breakpoint cluster region protein.
FT                                /FTId=PRO_0000273731.
FT   DOMAIN      497    690       DH.
FT   DOMAIN      707    865       PH.
FT   DOMAIN      869   1001       C2.
FT   DOMAIN     1053   1247       Rho-GAP.
FT   REGION      198    387       Binding to ABL SH2-domain (By
FT                                similarity).
FT   COMPBIAS    135    140       Poly-Ala.
FT   COMPBIAS    317    384       Ser-rich.
FT   MOD_RES     122    122       Phosphoserine (By similarity).
FT   MOD_RES     178    178       Phosphotyrosine (By similarity).
FT   MOD_RES     237    237       Phosphoserine.
FT   MOD_RES     247    247       Phosphotyrosine.
FT   MOD_RES     312    312       Phosphothreonine (By similarity).
FT   MOD_RES     461    461       Phosphoserine.
FT   MOD_RES     465    465       Phosphoserine (By similarity).
FT   MOD_RES     590    590       Phosphotyrosine (By similarity).
FT   MOD_RES     643    643       Phosphotyrosine (By similarity).
FT   MOD_RES    1263   1263       Phosphoserine (By similarity).
FT   CONFLICT    418    418       S -> H (in Ref. 3; CAA37013).
FT   CONFLICT   1213   1213       S -> P (in Ref. 2; AAH02193 and 4;
FT                                BAC98292).
SQ   SEQUENCE   1270 AA;  143062 MW;  2F3D6E8486DD6717 CRC64;
     MVDSVGFAEA WRAQFPDSEP PRMELRSVGD IEQELERCKA SIRRLEQEVN QERFRMIYLQ
     TLLAKEKKSY DRQRWGFRRA AQPPDGAAEP RASAPRPPPA PADGADPAPV EESEARPDGE
     GSPSKGRSAS ARRPAAAASA DRDDRGPPTS VAALRSNFEK IRKGPAQPGS ADAEKPFYVN
     VEFHHERGLV KVNDKEVSDR ISSLGSQAMQ MERKKSQQSA GQGLGEAPRP HYRGRSSESS
     CGLDGDYEDA ELNPRFLKDN LINANGGNRP PWPPLEYQPY QSIYVGGMMV EGEGKSPLLR
     SQSTSEQEKR LTWPRRSYSP RSFEDSGGGY TPDCSSNENL TSSEEDFSSG QSSRVSPSPT
     TYRMFRDKSR SPSQNSQQSF DSSSPPTPQC QKRHRQCQVV VSEATIVGVR KTGQIWPSDG
     DSTFQGEADS SFGTPPGYGC AADQAEEQRR HQDGLPYIDD SPSSSPHLSS KGRGSLASGA
     LDPTKVSELD LEKGLEMRKW VLSGILASEE TYLSHLEALL LPMKPLKAAA TTSQPVLTSQ
     QIETIFFKVP ELYEIHKEFY DGLFPRVQQW SHQQRVGDLF QKLASQLGVY RAFVDNYGVA
     METAEKCCQA NAQFAEISEN LRARSNKDVK DSTTKNSLET LLYKPVDRVT RSTLVLHDLL
     KHTPSSHPDH SLLQDALRIS QNFLSSINEE ITPRRQSMTV KKGEHRQLLK DSFMVELVEG
     ARKLRHIFLF TDLLLCTKLK KQSGGKTQQY DCKWYIPLTD LSFQMVDELE ALPNIPLVPD
     EELDALKIKI SQIKSDIQRE KRANKGSKVM ERLRKKLSEQ ESLLLLMSPS MAFRVHSRNG
     KSYTFLISSD YERAEWRESI REQQKKCFKS FSLTSVELQM LTNSCVKLQT VHHIPLTINK
     EDDESPGLYG FLHVIVHSAT GFKQSSNLYC TLEVDSFGYF VNKAKTRVYR DTTEPNWNEE
     FEIELEGSQT LRILCYEKCY NKMKMTKEDG ESADKLMGKG QVQLDPQTLQ DRDWQRTVID
     MNGIEVKLSV KFTSREFSLK RMPSRKQTGV FGVKIAVVTK RERSKVPYIV RQCVEEIERR
     GMEEVGIYRV SGVATDIQAL KAAFDVNNKD VSVMMSEMDV NAIAGTLKLY FRELPEPLFT
     DEFYPNFAEG IALSDPVAKE SCMLNLLLSL PEANLLTFLF LLDHLKRVAE KETVNKMSLH
     NLATVFGPTL LRSSEKESKL PANPSQPITM TDSWSLEVMS QVQVLLYFLQ LEAIPAPDSK
     RQSILFSTEV
//
ID   ANM8_MOUSE              Reviewed;         394 AA.
AC   Q6PAK3; Q7M6Z2;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Protein arginine N-methyltransferase 8;
DE            EC=2.1.1.-;
DE   AltName: Full=Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 4;
GN   Name=Prmt8; Synonyms=Hrmt1l4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-394.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION.
RX   MEDLINE=22882817; PubMed=12923295; DOI=10.1073/pnas.1734197100;
RA   Aubert J., Stavridis M.P., Tweedie S., O'Reilly M., Vierlinger K.,
RA   Li M., Ghazal P., Pratt T., Mason J.O., Roy D., Smith A.;
RT   "Screening for mammalian neural genes via fluorescence-activated cell
RT   sorter purification of neural precursors from Sox1-gfp knock-in
RT   mice.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11836-11841(2003).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=17512914; DOI=10.1016/j.brainres.2007.03.086;
RA   Taneda T., Miyata S., Kousaka A., Inoue K., Koyama Y., Mori Y.,
RA   Tohyama M.;
RT   "Specific regional distribution of protein arginine methyltransferase
RT   8 (PRMT8) in the mouse brain.";
RL   Brain Res. 1155:1-9(2007).
CC   -!- FUNCTION: Membrane-associated arginine methyltransferase that can
CC       both catalyze the formation of omega-N monomethylarginine (MMA)
CC       and asymmetrical dimethylarginine (aDMA). Able to mono- and
CC       dimethylate EWS protein; however its precise role toward EWS
CC       remains unclear as it still interacts with fully methylated EWS
CC       (By similarity).
CC   -!- SUBUNIT: Homodimers and heterodimers with PRMT1 or PRMT2,
CC       recruiting PRMT1 to the cell membrane. Interacts with PRMT2 and
CC       FYN (via the SH3 domain). Interacts with EWS; independently of EWS
CC       methylation status (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (By similarity).
CC   -!- TISSUE SPECIFICITY: Brain-specific. Only expressed in neurons,
CC       especially in the somatosensory and limbic systems, and a part of
CC       motor system. Highly expressed in all of the regions related to
CC       general somatosensory system. Expressed in most of the relay
CC       nuclei intervening the special somatosensory system, such as the
CC       auditory, visual and vestibular systems. Also present in forebrain
CC       limbic areas and thalamic nuclei relevant to limbic areas and in
CC       areas related to the motor system, such as the caudate putamen,
CC       Purkinje cells, inferior olivary nucleus and cerebellar nuclei.
CC   -!- DOMAIN: The SH3-binding motifs mediate the interaction with SH3
CC       domain-containing proteins such as PRMT2 and FYN, possibly leading
CC       to displace the N-terminal domain and activate the protein (By
CC       similarity).
CC   -!- DOMAIN: The N-terminal region (1-60) inhibits the enzymatic
CC       activity (By similarity).
CC   -!- SIMILARITY: Belongs to the protein arginine N-methyltransferase
CC       family. PRMT8 subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH60250.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC127373; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC060250; AAH60250.1; ALT_INIT; mRNA.
DR   EMBL; BK001349; DAA01382.1; -; mRNA.
DR   IPI; IPI00420678; -.
DR   RefSeq; NP_958759.1; NM_201371.1.
DR   UniGene; Mm.39750; -.
DR   ProteinModelPortal; Q6PAK3; -.
DR   SMR; Q6PAK3; 82-394.
DR   STRING; Q6PAK3; -.
DR   PhosphoSite; Q6PAK3; -.
DR   PRIDE; Q6PAK3; -.
DR   Ensembl; ENSMUST00000032500; ENSMUSP00000032500; ENSMUSG00000030350.
DR   GeneID; 381813; -.
DR   KEGG; mmu:381813; -.
DR   UCSC; uc009dwb.1; mouse.
DR   CTD; 381813; -.
DR   MGI; MGI:3043083; Prmt8.
DR   eggNOG; roNOG14427; -.
DR   GeneTree; ENSGT00550000074406; -.
DR   HOGENOM; HBG715060; -.
DR   HOVERGEN; HBG001793; -.
DR   InParanoid; Q6PAK3; -.
DR   OMA; AMMEPLV; -.
DR   OrthoDB; EOG434W66; -.
DR   PhylomeDB; Q6PAK3; -.
DR   NextBio; 402600; -.
DR   ArrayExpress; Q6PAK3; -.
DR   Bgee; Q6PAK3; -.
DR   CleanEx; MM_PRMT8; -.
DR   Genevestigator; Q6PAK3; -.
DR   GermOnline; ENSMUSG00000030350; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0008469; F:histone-arginine N-methyltransferase activity; ISS:HGNC.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:HGNC.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:HGNC.
DR   GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0035241; F:protein-arginine omega-N monomethyltransferase activity; ISS:HGNC.
DR   InterPro; IPR010456; Ribosomal-L11_MeTrfase_PrmA.
DR   Pfam; PF06325; PrmA; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Lipoprotein; Membrane; Methylation; Methyltransferase;
KW   Myristate; Repeat; S-adenosyl-L-methionine; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    394       Protein arginine N-methyltransferase 8.
FT                                /FTId=PRO_0000212330.
FT   MOTIF        29     42       SH3-binding 1 (By similarity).
FT   MOTIF        53     58       SH3-binding 2 (By similarity).
FT   BINDING      86     86       S-adenosyl-L-methionine (By similarity).
FT   BINDING      95     95       S-adenosyl-L-methionine (By similarity).
FT   BINDING     119    119       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING     141    141       S-adenosyl-L-methionine (By similarity).
FT   BINDING     170    170       S-adenosyl-L-methionine (By similarity).
FT   MOD_RES      58     58       Omega-N-methylarginine; by PRMT8 (By
FT                                similarity).
FT   MOD_RES      73     73       Asymmetric dimethylarginine; by PRMT8 (By
FT                                similarity).
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
SQ   SEQUENCE   394 AA;  45276 MW;  A3A8B337C376D970 CRC64;
     MGMKHSSRCL LLRRKMAENA VESTEVSSAP PQPPQPVIPA KPVQCVHHVS TQPSCPGRGK
     MSKLLNPEEM TSRDYYFDSY AHFGIHEEML KDEVRTLTYR NSMYHNKHVF KDKVVLDVGS
     GTGILSMFAA KAGAKKVFGI ECSSISDYSE KIIKANHLDN VITIFKGKVE EVELPVEKVD
     IIISEWMGYC LFYESMLNTV IFARDKWLKP GGLMFPDRAA LYVVAIEDRQ YKDFKIHWWE
     NVYGFDMTCI RDVAMKEPLV DIVDPKQVVT NACLIKEVDI YTVKTEELSF TSAFCLQIQR
     NDYVHALVTY FNIEFTKCHK KMGFSTAPDA PYTHWKQTVF YLEDYLTVRR GEEIYGTISM
     KPNAKNVRDL DFTVDLDFKG QLCETSVSND YKMR
//
ID   AHDC1_MOUSE             Reviewed;        1594 AA.
AC   Q6PAL7; Q5U5N7; Q8C4Y6; Q8VCU7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=AT-hook DNA-binding motif-containing protein 1;
GN   Name=Ahdc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N;
RC   TISSUE=Brain, Mammary tumor, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1457-1594.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Contains 2 A.T hook DNA-binding domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH19130.1; Type=Erroneous initiation;
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DR   EMBL; AL627184; CAM14379.1; -; Genomic_DNA.
DR   EMBL; BC019130; AAH19130.1; ALT_INIT; mRNA.
DR   EMBL; BC042621; AAH42621.1; -; mRNA.
DR   EMBL; BC060231; AAH60231.1; -; mRNA.
DR   EMBL; AK080410; BAC37907.1; -; mRNA.
DR   IPI; IPI00420683; -.
DR   RefSeq; NP_666267.3; NM_146155.3.
DR   UniGene; Mm.31816; -.
DR   UniGene; Mm.421391; -.
DR   STRING; Q6PAL7; -.
DR   PhosphoSite; Q6PAL7; -.
DR   PRIDE; Q6PAL7; -.
DR   Ensembl; ENSMUST00000044521; ENSMUSP00000047113; ENSMUSG00000037692.
DR   Ensembl; ENSMUST00000105914; ENSMUSP00000101534; ENSMUSG00000037692.
DR   Ensembl; ENSMUST00000105915; ENSMUSP00000101535; ENSMUSG00000037692.
DR   Ensembl; ENSMUST00000105916; ENSMUSP00000101536; ENSMUSG00000037692.
DR   GeneID; 230793; -.
DR   KEGG; mmu:230793; -.
DR   NMPDR; fig|10090.3.peg.10513; -.
DR   UCSC; uc008vcc.1; mouse.
DR   CTD; 230793; -.
DR   MGI; MGI:2444218; Ahdc1.
DR   eggNOG; maNOG08163; -.
DR   GeneTree; ENSGT00390000018883; -.
DR   HOGENOM; HBG126343; -.
DR   HOVERGEN; HBG094919; -.
DR   InParanoid; Q6PAL7; -.
DR   OMA; FPEQVPS; -.
DR   OrthoDB; EOG41JZD1; -.
DR   PhylomeDB; Q6PAL7; -.
DR   NextBio; 380164; -.
DR   ArrayExpress; Q6PAL7; -.
DR   Bgee; Q6PAL7; -.
DR   CleanEx; MM_AHDC1; -.
DR   Genevestigator; Q6PAL7; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR   SMART; SM00384; AT_hook; 2.
PE   1: Evidence at protein level;
KW   DNA-binding; Phosphoprotein; Repeat.
FT   CHAIN         1   1594       AT-hook DNA-binding motif-containing
FT                                protein 1.
FT                                /FTId=PRO_0000313825.
FT   DNA_BIND    395    407       A.T hook 1.
FT   DNA_BIND    541    553       A.T hook 2.
FT   COMPBIAS     25    459       Pro-rich.
FT   COMPBIAS    661    820       Gly-rich.
FT   MOD_RES      70     70       Phosphoserine (By similarity).
FT   MOD_RES     825    825       Phosphoserine.
FT   MOD_RES     842    842       Phosphoserine (By similarity).
FT   MOD_RES    1392   1392       Phosphoserine (By similarity).
FT   MOD_RES    1396   1396       Phosphoserine (By similarity).
FT   MOD_RES    1540   1540       Phosphoserine (By similarity).
FT   CONFLICT    431    431       L -> LP (in Ref. 2; AAH42621).
SQ   SEQUENCE   1594 AA;  168081 MW;  2DC06E3D70D75DC4 CRC64;
     MRVKPQGLVV TSSAVCSSPD YLREPKYYPG GPPTPRPLLP TRPPASPPDK AFSTHTFSEN
     PRPPPRRDPS SRRPPVLAKG DDLLPPRAAR PVSQAHCPSP APDNSSLRHW DNGRVNLRPV
     VQLIDIMKDL TRLSQDLQHS GVHLDCGGLR LSRPPAPPPG DLQYSFFSSP SLANSIRSPE
     ERANPHTKSE RPSHPLYEPE PEPRDSPQPG QGHGPGAAAT ATGLPPEPEP DGPDYSELAD
     ADILSELASL TCPEAQLLEA QALEPPSPQP EPQLLDPQPR FLDPQALEPL GEGLELPPLQ
     PLADPLGLPS LTLQALDTLP DSLESQLLDP QALDPLPKLL DVPGRRLEPQ QSLGHCQLAE
     PLRLDLCSPH GPPGPEGHPK YALRRTDRPK ILCRRRKAGR GRKADSGPEG RLLPLPMPTG
     LAAALAEPPP LPPPPPPTLS GPGPVPELEP ESSQTPMVPT RKGKCRGVRR MVVKMAKIPV
     SLGRRNKTTY KVSSLSSSLS VEGKELGLRV SSEPTPLLKM KNNGRNVVVV FPPGEMPIIL
     KRKRGRPPKN LLLGPGKPKE PTVVAAEAAT VTAATMAMPE VKKRRRRKQK LASPQPSYAA
     DANDSKAEYS DVLAKLAFLN RQSQCAGRCS PPRCWTPSEP ESVHQAPDTQ SISQFLHRVQ
     GFRRRGGKTG GFGGRGGGHA AKAARCSFSD FFEGIGKKKK VVAVAAPGLV GPGLTELGHP
     RKRGRGEVDA VTGKPKRKRR SRKNGTLFPE QVPSGPGFGE AGAEWVGDKG GGWAPHHGHP
     GGQAGRNCGF QGTEARAFAS TGLESGASGR GSYYAGAPSG QTELSQERQN LFTGYFRSLL
     DSDDSSDLLD FALSASRPES RKASGTYAGP PSSALPAQRG LATFPSRGAK ASPVAVGSSG
     AGADPSFQPV LPSRQTFPPG RATSYGITPA TSDCRAAETF PKLAPPPSAV ARSPTTHPPA
     NTYPPQYGGY GAGQSVFASA KPFSGQDCAN SKDCSFAYGS GNSLPASPSS AHSAGYAPPP
     TGGPCLPPSK ASFFNSSEGG PFSGSAPTPL RCDSRASTVS PGGYMVPKGT TASAASVASS
     SSSSFQPSPE NCRQFVGASQ WPFRQGYGGL DWASEAFSQL YNPNFDCHGS EPNVILDISN
     YTPQKVKQQT AVSETFSESS SDSTQFSQPV GGGGFRRANS EASSSEGQSS LSSLEKLMMD
     WNEASSAPGY NWNQSVLFQS SSKPGRGRRK KVDLFEASHL GFSTSTSATA SGYPSKRSTG
     PRQPRGGRGS GACSAKKERG GTAAKAKFIP KPQPVNPLFQ DSPDLGLDYY SGDSSMSPLP
     SQSRAFGVGE RDPCDFMGPY SMNPSTPSDG TFGQGFHCDS PSLGAAELDG KHFPPLAHPP
     TVFDAGLQKA YSPTCSPTLG FKEELRPPPS KLTACEPLKH GLQGASLSHA AQAHLSCRDL
     PLGQPHYDSP SCKGTAYWYP PGSAARSPPY EGKVGSGLLA DFLGRTEAVC LSAPHLASPP
     ATPKADKEPL EMARPPGPPR GPAAATAGYG CPLLSDLTLS PVPRDSLLPL QDTAYRYPGF
     MPQAHPGLGG GPKSGFLGPM AEPHPEDTFT VTSL
//
ID   DEN5A_MOUSE             Reviewed;        1287 AA.
AC   Q6PAL8; Q62146; Q8C829; Q8VDF6; Q9QYZ2;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=DENN domain-containing protein 5A;
DE   AltName: Full=Rab6-interacting protein 1;
DE            Short=Rab6IP1;
GN   Name=Dennd5a; Synonyms=Rab6ip1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR;
RA   Goud B.;
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 703-1287.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 705-890, AND INTERACTION WITH RAB6A.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=95301579; PubMed=7782346; DOI=10.1074/jbc.270.24.14801;
RA   Janoueix-Lerosey I., Jollivet F., Camonis J., Marche P.N., Goud B.;
RT   "Two-hybrid system screen with the small GTP-binding protein Rab6.
RT   Identification of a novel mouse GDP dissociation inhibitor isoform and
RT   two other potential partners of Rab6.";
RL   J. Biol. Chem. 270:14801-14808(1995).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 707-1090 IN COMPLEX WITH
RP   RAB6A, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-763; TYR-932 AND
RP   LEU-935.
RX   PubMed=19141279; DOI=10.1016/j.str.2008.10.014;
RA   Recacha R., Boulet A., Jollivet F., Monier S., Houdusse A., Goud B.,
RA   Khan A.R.;
RT   "Structural basis for recruitment of Rab6-interacting protein 1 to
RT   Golgi via a RUN domain.";
RL   Structure 17:21-30(2009).
CC   -!- FUNCTION: May be involved in Rab6-mediated GTPase signaling.
CC   -!- SUBUNIT: Interacts with RAB6A bound to GTP.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane.
CC   -!- SIMILARITY: Belongs to the RAB6IP1 family.
CC   -!- SIMILARITY: Contains 1 dDENN domain.
CC   -!- SIMILARITY: Contains 1 DENN domain.
CC   -!- SIMILARITY: Contains 1 PLAT domain.
CC   -!- SIMILARITY: Contains 2 RUN domains.
CC   -!- SIMILARITY: Contains 1 uDENN domain.
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DR   EMBL; AJ245569; CAB55599.1; -; mRNA.
DR   EMBL; BC022119; AAH22119.1; -; mRNA.
DR   EMBL; BC060230; AAH60230.1; -; mRNA.
DR   EMBL; AK048609; BAC33389.1; -; mRNA.
DR   EMBL; L40894; AAA78787.1; -; mRNA.
DR   IPI; IPI00396735; -.
DR   PIR; A56956; A56956.
DR   RefSeq; NP_067469.1; NM_021494.1.
DR   UniGene; Mm.21904; -.
DR   PDB; 3CWZ; X-ray; 3.20 A; B=707-1090.
DR   PDBsum; 3CWZ; -.
DR   ProteinModelPortal; Q6PAL8; -.
DR   SMR; Q6PAL8; 737-1072.
DR   DIP; DIP-287N; -.
DR   STRING; Q6PAL8; -.
DR   PhosphoSite; Q6PAL8; -.
DR   PRIDE; Q6PAL8; -.
DR   Ensembl; ENSMUST00000080437; ENSMUSP00000079295; ENSMUSG00000035901.
DR   GeneID; 19347; -.
DR   KEGG; mmu:19347; -.
DR   UCSC; uc009jek.1; mouse.
DR   CTD; 19347; -.
DR   MGI; MGI:1201681; Dennd5a.
DR   eggNOG; roNOG07671; -.
DR   GeneTree; ENSGT00550000074509; -.
DR   HOGENOM; HBG381256; -.
DR   HOVERGEN; HBG059906; -.
DR   InParanoid; Q6PAL8; -.
DR   OMA; IQEARTM; -.
DR   OrthoDB; EOG4M397P; -.
DR   PhylomeDB; Q6PAL8; -.
DR   NextBio; 296369; -.
DR   ArrayExpress; Q6PAL8; -.
DR   Bgee; Q6PAL8; -.
DR   Genevestigator; Q6PAL8; -.
DR   GermOnline; ENSMUSG00000035901; Mus musculus.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0017137; F:Rab GTPase binding; IDA:MGI.
DR   InterPro; IPR005112; dDENN.
DR   InterPro; IPR001194; DENN.
DR   InterPro; IPR008976; Lipase_LipOase.
DR   InterPro; IPR001024; LipOase_LH2.
DR   InterPro; IPR004012; Run.
DR   InterPro; IPR005113; uDENN.
DR   Gene3D; G3DSA:2.60.60.20; Lipase_LipOase; 1.
DR   Pfam; PF03455; dDENN; 1.
DR   Pfam; PF02141; DENN; 1.
DR   Pfam; PF01477; PLAT; 1.
DR   Pfam; PF02759; RUN; 2.
DR   Pfam; PF03456; uDENN; 1.
DR   SMART; SM00801; dDENN; 1.
DR   SMART; SM00799; DENN; 1.
DR   SMART; SM00593; RUN; 2.
DR   SMART; SM00800; uDENN; 1.
DR   SUPFAM; SSF49723; Lipase_LipOase; 1.
DR   PROSITE; PS50947; DDENN; 1.
DR   PROSITE; PS50211; DENN; 1.
DR   PROSITE; PS50095; PLAT; 1.
DR   PROSITE; PS50826; RUN; 2.
DR   PROSITE; PS50946; UDENN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Golgi apparatus; Membrane; Phosphoprotein; Repeat.
FT   CHAIN         1   1287       DENN domain-containing protein 5A.
FT                                /FTId=PRO_0000097143.
FT   DOMAIN       68    138       UDENN.
FT   DOMAIN      202    390       DENN.
FT   DOMAIN      512    588       dDENN.
FT   DOMAIN      787    950       RUN 1.
FT   DOMAIN      954   1062       PLAT.
FT   DOMAIN     1134   1280       RUN 2.
FT   COMPBIAS      3      9       Poly-Gly.
FT   COMPBIAS    593    598       Poly-Asp.
FT   MOD_RES     193    193       Phosphoserine (By similarity).
FT   MUTAGEN     763    763       K->E: Abolishes the interaction with
FT                                RAP6A and localization to Golgi membrane.
FT   MUTAGEN     932    932       Y->S: Abolishes the interaction with
FT                                RAP6A and localization to Golgi membrane;
FT                                when associated with Ala-935.
FT   MUTAGEN     935    935       L->A: Abolishes the interaction with
FT                                RAP6A and localization to Golgi membrane;
FT                                when associated with Ser-932.
FT   CONFLICT     37     60       Missing (in Ref. 1; CAB55599).
FT   CONFLICT    706    706       T -> E (in Ref. 4; AAA78787).
FT   CONFLICT    761    761       K -> E (in Ref. 3; BAC33389).
FT   CONFLICT    871    872       IQ -> ME (in Ref. 4; AAA78787).
FT   CONFLICT    888    890       VRL -> GAT (in Ref. 4; AAA78787).
FT   HELIX       742    751
FT   HELIX       755    769
FT   HELIX       788    805
FT   HELIX       816    830
FT   HELIX       864    872
FT   HELIX       884    894
FT   HELIX       897    904
FT   HELIX       908    914
FT   TURN        920    922
FT   HELIX       924    934
FT   HELIX       935    938
FT   TURN        944    948
FT   STRAND      952    962
FT   STRAND      976    980
FT   STRAND      997   1003
FT   STRAND     1010   1013
FT   STRAND     1024   1034
FT   STRAND     1039   1043
FT   STRAND     1058   1061
SQ   SEQUENCE   1287 AA;  146653 MW;  9A48FE3DDC6A2BF1 CRC64;
     MSGGGGGGGS APSRFADYFV ICGLDTETGL EPDELSALCQ YIQASKARDG ASPFISSTTE
     GENFEQTPLR RTFKSKVLAR YPENVDWNPF DQDAVGMLCM PKGLAFKTQA DPREPQFHAF
     IITREDGSRT FGFALTFYEE VTSKQICSAM QTLYHMHNAE YDVLHAPLAD GGDQSGMEDG
     EGIPGTKLQR FNSYDISRDT LYVSKCICLI TPMSFMKACR SVLQQLHQAV TSPQPPPLPL
     ESYIYNVLYE VPLPPPGRSL KFSGVYGPII CQRPSTNELP LFDFPVKEVF ELLGVENVFQ
     LFTCALLEFQ ILLYSQHYQR LMTVAETITA LMFPFQWQHV YVPILPASLL HFLDAPVPYL
     MGLHSNGLDD RSKLELPQEA NLCFVDVDNH FIELPEDLPQ FPNKLEFVQE VSEILMAFGV
     PPEGNLHCSE SASKLKRIRA SELVSDKRNG NIAGSPLHSY ELLKENETIA RLQALVKRTG
     VSLEKLEVRE DPSSNKDFKV QCDEEELRIY QLNIQIREVF ANRFTQMFAD YEVFVIQPSQ
     DKESWFTNRE QMQNFDKASF LSDQPEPYLP FLSRFLETQM FASFIDNKIM CHDDDDKDPV
     LRVFDSRVDK IRLLNVRTPT LRTSMYQKCT TVDEAEKAIE LRLAKIDHTA VHPHLLDMKI
     GQGKYEPGFF PKLQSDVLCT GPASNKWTKR NAPAQWRRKD RQKQHTEHLR LDNDQREKYI
     QEARNMGSTI RQPKLSNLSP SVIAQTNWKF VEGLLKECRN KTKRMLVEKM GREAVELGHG
     EVNITGVEEN TLIASLCDLL ERIWSHGLQV KQGKSALWSH LLHYQENRQR KLTSGSLSTS
     GILLDSERRK SDASAVMSPL RISLIQDMRH IQNIGEIKTD VGKARAWVRL SMEKKLLSRH
     LKQLLSDHEL TKKLYKRYAF LRCDDEKEQF LYHLLSFNAV DYFCFTNVFT TILIPYHILI
     VPSKKLGGSM FTANPWICIS GELGETQILQ IPRNVLEMTF ECQNLGKLTT VQIGHDNSGL
     YAKWLVECVM VRNEVTGHTY KFPCGRWLGK GMDDGSLERV LVGELLTSLP EVDERPCRTP
     PLQQSPSVIR RLVTISPNNK PKLNTGQIQE SIGEAVNGIV KHFHKPEKER GSLTLLLCGE
     CGLVSALEQA FQHGFKSPRL FKNVFIWDFL EKAQTYYETL EQNDVVPEEN WHTRARNFCR
     FVTAVNNTPR NIGKDGKFQM LVCLGARDHL LHHWIALLAD CPITAHMYED VALIKDHTLV
     NSLIRVLQTL QEFNITLDTS LVKGIDI
//
ID   AAKB2_MOUSE             Reviewed;         271 AA.
AC   Q6PAM0;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=5'-AMP-activated protein kinase subunit beta-2;
DE            Short=AMPK subunit beta-2;
GN   Name=Prkab2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: AMPK is responsible for the regulation of fatty acid
CC       synthesis by phosphorylation of acetyl-CoA carboxylase. Also
CC       regulates cholesterol synthesis via phosphorylation and
CC       inactivation of hydroxymethylglutaryl-CoA reductase and hormone-
CC       sensitive lipase. This is a regulatory subunit, may be a positive
CC       regulator of AMPK activity. It may also serve as an adapter
CC       molecule for the catalytic alpha-subunit (By similarity).
CC   -!- SUBUNIT: Heterotrimer of an alpha catalytic subunit, a beta and a
CC       gamma non-catalytic regulatory subunits (By similarity).
CC   -!- PTM: Phosphorylated when associated with the catalytic subunit (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta
CC       subunit family.
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DR   EMBL; BC060228; AAH60228.1; -; mRNA.
DR   IPI; IPI00340519; -.
DR   RefSeq; NP_892042.2; NM_182997.2.
DR   UniGene; Mm.31175; -.
DR   ProteinModelPortal; Q6PAM0; -.
DR   SMR; Q6PAM0; 74-271.
DR   STRING; Q6PAM0; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   PhosphoSite; Q6PAM0; -.
DR   PRIDE; Q6PAM0; -.
DR   Ensembl; ENSMUST00000045743; ENSMUSP00000036410; ENSMUSG00000038205.
DR   GeneID; 108097; -.
DR   KEGG; mmu:108097; -.
DR   UCSC; uc008qpb.1; mouse.
DR   CTD; 108097; -.
DR   MGI; MGI:1336185; Prkab2.
DR   eggNOG; roNOG05515; -.
DR   HOGENOM; HBG623595; -.
DR   HOVERGEN; HBG050430; -.
DR   InParanoid; Q6PAM0; -.
DR   OMA; PGLYGQE; -.
DR   OrthoDB; EOG4W9J4H; -.
DR   PhylomeDB; Q6PAM0; -.
DR   NextBio; 360054; -.
DR   ArrayExpress; Q6PAM0; -.
DR   Bgee; Q6PAM0; -.
DR   Genevestigator; Q6PAM0; -.
DR   GermOnline; ENSMUSG00000038205; Mus musculus.
DR   GO; GO:0004679; F:AMP-activated protein kinase activity; TAS:MGI.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006950; P:response to stress; TAS:MGI.
DR   InterPro; IPR006828; AMP_prot_kin_bsu_interact-dom.
DR   Pfam; PF04739; AMPKBI; 1.
PE   2: Evidence at transcript level;
KW   Fatty acid biosynthesis; Lipid synthesis; Phosphoprotein.
FT   CHAIN         1    271       5'-AMP-activated protein kinase subunit
FT                                beta-2.
FT                                /FTId=PRO_0000204369.
FT   MOD_RES      39     39       Phosphothreonine (By similarity).
FT   MOD_RES     107    107       Phosphoserine (By similarity).
FT   MOD_RES     181    181       Phosphoserine (By similarity).
FT   MOD_RES     182    182       Phosphoserine (By similarity).
SQ   SEQUENCE   271 AA;  30209 MW;  883B42716E996BE7 CRC64;
     MGNTTSERVS GERHGAKAAR AEGGGHGPGK EHKIMVGSTD DPSVFSLPDS KLPGDKEFVP
     WQQDLDDSVK PAQQARPTVI RWSEGGKEVF ISGSFNNWST KIPLIKSHND FVAILDLPEG
     EHQYKFFVDG QWVHDPSEPV VTSQLGTINN LIHVKKSDFE VFDALKLDSM ESSETSCRDL
     SSSPPGPYGQ EMYVFRSEER FKSPPILPPH LLQVILNKDT NISCDPALLP EPNHVMLNHL
     YALSIKDSVM VLSATHRYKK KYVTTLLYKP I
//
ID   GAPD1_MOUSE             Reviewed;        1458 AA.
AC   Q6PAR5; A0PJI8; A2AR09; A2AR10; A2AR17; A2AR18; Q3TNS1; Q3UDL0;
AC   Q3UYD5; Q6ZPP0; Q80V37; Q80ZK4; Q8BTS5; Q9CRS2; Q9CTI1;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=GTPase-activating protein and VPS9 domain-containing protein 1;
DE   AltName: Full=GAPex-5;
DE   AltName: Full=Rab5-activating protein 6;
GN   Name=Gapvd1; Synonyms=Gapex5, Kiaa1521;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH TRIP10.
RC   STRAIN=Swiss albino;
RX   PubMed=17189207; DOI=10.1016/j.cmet.2006.12.006;
RA   Lodhi I.J., Chiang S.-H., Chang L., Vollenweider D., Watson R.T.,
RA   Inoue M., Pessin J.E., Saltiel A.R.;
RT   "Gapex-5, a Rab31 guanine nucleotide exchange factor that regulates
RT   Glut4 trafficking in adipocytes.";
RL   Cell Metab. 5:59-72(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 973-1458 (ISOFORM 6).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Eye, Liver, Medulla oblongata, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6, FVB/N, and FVB/N-3;
RC   TISSUE=Brain, Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   FUNCTION.
RX   PubMed=16880210; DOI=10.1074/jbc.M602873200;
RA   Su X., Lodhi I.J., Saltiel A.R., Stahl P.D.;
RT   "Insulin-stimulated Interaction between insulin receptor substrate 1
RT   and p85alpha and activation of protein kinase B/Akt require Rab5.";
RL   J. Biol. Chem. 281:27982-27990(2006).
RN   [7]
RP   FUNCTION.
RX   PubMed=17545148; DOI=10.1074/jbc.M703725200;
RA   Su X., Kong C., Stahl P.D.;
RT   "GAPex-5 mediates ubiquitination, trafficking, and degradation of
RT   epidermal growth factor receptor.";
RL   J. Biol. Chem. 282:21278-21284(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-903 AND 1085, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-902, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Acts both as a GTPase-activating protein (GAP) and a
CC       guanine nucleotide exchange factor (GEF), and participates in
CC       various processes such as endocytosis, insulin receptor
CC       internalization or LC2A4/GLUT4 trafficking. Acts as a GEF for the
CC       Ras-related protein RAB31 by exchanging bound GDP for free GTP,
CC       leading to regulate LC2A4/GLUT4 trafficking. In the absence of
CC       insulin, it maintains RAB31 in an active state and promotes a
CC       futile cycle between LC2A4/GLUT4 storage vesicles and early
CC       endosomes, retaining LC2A4/GLUT4 inside the cells. Upon insulin
CC       stimulation, it is translocated to the plasma membrane, releasing
CC       LC2A4/GLUT4 from intracellular storage vesicles. Also involved in
CC       EGFR trafficking and degradation, possibly by promoting EGFR
CC       ubiquitination and subsequent degradation by the proteasome. Has
CC       GEF activity for Rab5 and GAP activity for Ras.
CC   -!- SUBUNIT: Interacts with RAB5A (By similarity). Interacts with
CC       TRIP10/CIP4.
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC       Endosome (By similarity). Note=Recruited to the plasma membrane by
CC       TRIP10/CIP4 in response to insulin.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q6PAR5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PAR5-2; Sequence=VSP_032366;
CC       Name=3;
CC         IsoId=Q6PAR5-3; Sequence=VSP_032363, VSP_032364;
CC       Name=4;
CC         IsoId=Q6PAR5-4; Sequence=VSP_032365, VSP_032366;
CC       Name=5;
CC         IsoId=Q6PAR5-5; Sequence=VSP_032366, VSP_032368;
CC       Name=6;
CC         IsoId=Q6PAR5-6; Sequence=VSP_032367;
CC   -!- TISSUE SPECIFICITY: Present in adipocytes and fibroblasts (at
CC       protein level). Ubiquitously expressed.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the GAPVD1 family.
CC   -!- SIMILARITY: Contains 1 Ras-GAP domain.
CC   -!- SIMILARITY: Contains 1 VPS9 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH31478.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAH43715.1; Type=Erroneous initiation;
CC       Sequence=AAH48847.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAH57164.1; Type=Erroneous initiation;
CC       Sequence=BAB29377.2; Type=Erroneous initiation;
CC       Sequence=BAC98191.1; Type=Erroneous initiation;
CC       Sequence=BAE22277.1; Type=Erroneous initiation;
CC       Sequence=BAE29251.1; Type=Frameshift; Positions=811;
CC       Sequence=CAM15445.1; Type=Erroneous gene model prediction;
CC       Sequence=CAM15446.1; Type=Erroneous gene model prediction;
CC       Sequence=CAM15455.1; Type=Erroneous gene model prediction;
CC       Sequence=CAM15456.1; Type=Erroneous gene model prediction;
CC       Sequence=CAM24604.1; Type=Erroneous gene model prediction;
CC       Sequence=CAM24605.1; Type=Erroneous gene model prediction;
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DR   EMBL; EF155419; ABM68541.1; -; mRNA.
DR   EMBL; AK129381; BAC98191.1; ALT_INIT; Transcribed_RNA.
DR   EMBL; AK014474; BAB29377.2; ALT_INIT; mRNA.
DR   EMBL; AK088851; BAC40613.1; -; mRNA.
DR   EMBL; AK003521; BAB22834.1; -; mRNA.
DR   EMBL; AK134776; BAE22277.1; ALT_INIT; mRNA.
DR   EMBL; AK150026; BAE29251.1; ALT_FRAME; mRNA.
DR   EMBL; AK165047; BAE38017.1; -; mRNA.
DR   EMBL; AL845262; CAM15445.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL929106; CAM15445.1; JOINED; Genomic_DNA.
DR   EMBL; AL845262; CAM15446.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL929106; CAM15446.1; JOINED; Genomic_DNA.
DR   EMBL; AL845262; CAM15447.1; -; Genomic_DNA.
DR   EMBL; AL929106; CAM15447.1; JOINED; Genomic_DNA.
DR   EMBL; AL845262; CAM15455.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL845262; CAM15456.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL929106; CAM24604.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL845262; CAM24604.1; JOINED; Genomic_DNA.
DR   EMBL; AL929106; CAM24605.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL845262; CAM24605.1; JOINED; Genomic_DNA.
DR   EMBL; AL929106; CAM24606.1; -; Genomic_DNA.
DR   EMBL; AL845262; CAM24606.1; JOINED; Genomic_DNA.
DR   EMBL; BC031478; AAH31478.1; ALT_SEQ; mRNA.
DR   EMBL; BC043715; AAH43715.1; ALT_INIT; mRNA.
DR   EMBL; BC048847; AAH48847.1; ALT_SEQ; mRNA.
DR   EMBL; BC057164; AAH57164.1; ALT_INIT; mRNA.
DR   EMBL; BC060123; AAH60123.1; -; mRNA.
DR   IPI; IPI00406596; -.
DR   IPI; IPI00889216; -.
DR   IPI; IPI00889225; -.
DR   IPI; IPI00889231; -.
DR   IPI; IPI00889244; -.
DR   IPI; IPI00889253; -.
DR   RefSeq; NP_079985.2; NM_025709.2.
DR   UniGene; Mm.156452; -.
DR   UniGene; Mm.393397; -.
DR   ProteinModelPortal; Q6PAR5; -.
DR   SMR; Q6PAR5; 1240-1456.
DR   PhosphoSite; Q6PAR5; -.
DR   Ensembl; ENSMUST00000028224; ENSMUSP00000028224; ENSMUSG00000026867.
DR   Ensembl; ENSMUST00000102800; ENSMUSP00000099864; ENSMUSG00000026867.
DR   GeneID; 66691; -.
DR   KEGG; mmu:66691; -.
DR   UCSC; uc008jiq.1; mouse.
DR   CTD; 66691; -.
DR   MGI; MGI:1913941; Gapvd1.
DR   eggNOG; roNOG05259; -.
DR   GeneTree; ENSGT00530000063341; -.
DR   HOVERGEN; HBG107936; -.
DR   InParanoid; Q6PAR5; -.
DR   OMA; EMVDSNE; -.
DR   OrthoDB; EOG4548XR; -.
DR   NextBio; 322389; -.
DR   ArrayExpress; Q6PAR5; -.
DR   Bgee; Q6PAR5; -.
DR   CleanEx; MM_GAPVD1; -.
DR   Genevestigator; Q6PAR5; -.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032794; F:GTPase activating protein binding; IMP:UniProtKB.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IMP:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0051223; P:regulation of protein transport; IMP:UniProtKB.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR001936; RasGAP.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR003123; VPS9.
DR   InterPro; IPR013995; VPS9_sub.
DR   Gene3D; G3DSA:1.10.506.10; RasGAP; 1.
DR   Pfam; PF00616; RasGAP; 1.
DR   Pfam; PF02204; VPS9; 1.
DR   SMART; SM00167; VPS9; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS00509; RAS_GTPASE_ACTIV_1; FALSE_NEG.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR   PROSITE; PS51205; VPS9; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Endocytosis; Endosome;
KW   GTPase activation; Guanine-nucleotide releasing factor; Membrane;
KW   Phosphoprotein.
FT   CHAIN         1   1458       GTPase-activating protein and VPS9
FT                                domain-containing protein 1.
FT                                /FTId=PRO_0000324772.
FT   DOMAIN      131    353       Ras-GAP.
FT   DOMAIN     1318   1458       VPS9.
FT   MOD_RES     238    238       N6-acetyllysine (By similarity).
FT   MOD_RES     390    390       Phosphothreonine (By similarity).
FT   MOD_RES     458    458       Phosphothreonine (By similarity).
FT   MOD_RES     466    466       Phosphoserine (By similarity).
FT   MOD_RES     469    469       Phosphothreonine (By similarity).
FT   MOD_RES     470    470       Phosphothreonine (By similarity).
FT   MOD_RES     566    566       Phosphoserine (By similarity).
FT   MOD_RES     569    569       Phosphoserine (By similarity).
FT   MOD_RES     742    742       Phosphoserine (By similarity).
FT   MOD_RES     746    746       Phosphoserine (By similarity).
FT   MOD_RES     747    747       Phosphothreonine (By similarity).
FT   MOD_RES     748    748       Phosphoserine (By similarity).
FT   MOD_RES     766    766       Phosphoserine (By similarity).
FT   MOD_RES     900    900       Phosphoserine (By similarity).
FT   MOD_RES     902    902       Phosphoserine.
FT   MOD_RES     903    903       Phosphoserine.
FT   MOD_RES     964    964       Phosphoserine (By similarity).
FT   MOD_RES    1017   1017       Phosphoserine (By similarity).
FT   MOD_RES    1076   1076       Phosphoserine (By similarity).
FT   MOD_RES    1085   1085       Phosphoserine.
FT   VAR_SEQ     373    379       GCVAAFL -> VGMSVVS (in isoform 3).
FT                                /FTId=VSP_032363.
FT   VAR_SEQ     380   1458       Missing (in isoform 3).
FT                                /FTId=VSP_032364.
FT   VAR_SEQ     480    480       I -> IGQQLAAITAWDSSATNLTAHIPLVTPF (in
FT                                isoform 4).
FT                                /FTId=VSP_032365.
FT   VAR_SEQ     557    577       Missing (in isoform 2, isoform 4 and
FT                                isoform 5).
FT                                /FTId=VSP_032366.
FT   VAR_SEQ    1055   1055       Missing (in isoform 6).
FT                                /FTId=VSP_032367.
FT   VAR_SEQ    1202   1202       Missing (in isoform 5).
FT                                /FTId=VSP_032368.
FT   CONFLICT    581    581       N -> D (in Ref. 3; BAE29251).
FT   CONFLICT    661    661       G -> E (in Ref. 5; AAH31478).
FT   CONFLICT    893    893       Y -> H (in Ref. 3; BAE22277).
FT   CONFLICT   1257   1257       A -> V (in Ref. 2; BAC98191).
SQ   SEQUENCE   1458 AA;  162402 MW;  CA3D2EAF22051FD7 CRC64;
     MVKLDIHTLA HHLKQERLYV SSEKQLIQRL NADVLKTAEK LYRTAWIAKQ QRINLDRLII
     TSAEASPAEC CQHAKILEDT QFVDGYKQLG FQETAYGEFL SRLRENPRLI ASSLVAGEKL
     NQENTQSVIY TVFTSLYGNC IMQEDESYLL QVLRYLIEFE LKESDNPRRL LRRGTCAFSI
     LFKLFSEGLF SAKLFLTATL HEPIMQLLVE DEDHLETDPN KLIERFSPAQ QEKLFGEKGS
     DRFRQKVQEM VDSNEAKLVA LVNKFIGYLK QNTYCFPHSL RWIVSQMYKT LSCVDRLEVG
     EVRAMCTDLL LACFICPAVV NPEQYGIISD APINEVARFN LMQVGRLLQQ LAMTGTEEGD
     PRTKNSLGKF DKGCVAAFLD VVIGGRAVET PPMSSVNLLE GLSRTVVYIS YSQLITLVNF
     MKSVMSGDQL KEDRMALDNL LANLPQAKPG KSSSLDMTPY STPQMSPATT PANKKNRLPI
     ATRSRSRSNM LMDLHMDHEG SSQETIQEVQ PEEVLVISLG TGPQLTPGMM SENEVLNMQL
     SDGGQGDVPV DENKLHGKPD KTLRFSLCSD NLEGISEGPS NRSNSVSSLD LEGESVSELG
     AGPSGSNGVE ALQLLEHEQA TTQDNLDDKL RKFEIRDMMG LTDDRDISET VSETWSTDVL
     GSDFDPNVDE DRLQEIAGAA AENVLGSLLC LPGSGSVLLD PCTGSTISET TSEAWSVEVL
     PSDSEAPDLK QEERLQELES CSGLGSTSDD TDVREVSSRP STPGLSVVSG ISATSEDIPN
     KIEDLRSECS SDFGGKDSVT SPDMDDIAHG AHQLTSPPSQ SESLLAMFDP LSSHEGASAV
     VRPKVHYARP SHPPPDPPIL EGAVGGNEAR LPNFGSHVLT AAEMEAFKQR HSYPERLVRS
     RSSDIVSSVR RPMSDPSWNR RPGNEELPPA AATGATSLVA APHSSSSSPS KDSSRGETEE
     RKDSDDERSD RSRPWWRKRF VSAMPKAPIP FRKKEKQEKD KDDLGPDRFS TLTDEPSPRL
     SAQAQVAEDI LDKYRNAIKR TSPSEGAMAN DESAEVMGDG ESAHDSPREE ALQNISADDL
     PDSASQAAHP QDSAFSYRDV KKKLRLALCS ADSVAFPVLT HSTRNGLPDH TDPEDNEIVC
     FLKVQIAEAI NLQDKSLMAQ LQETMRCVCR FDNRTCRKLL ASIAEDYRKR APYIAYLTRC
     RQGLQTTQAH LERLLQRVLR DKEVANRYFT TVCVRLLLES KEKKIREFIQ DFQKLTAADD
     KTAQVEDFLQ FLYGVMAQDV IWQNASEEQL QDAQLAIERS VMNRIFKLAF YPNQDGDILR
     DQVLHEHIQR LSKVVTANHR ALQIPEVYLR EAPWPSAQSE IRTISAYKTP RDKVQCILRM
     CSTIMNLLSL ANEDSVPGAD DFVPVLVFVL IKANPPCLLS TVQYISSFYA SCLSGEESYW
     WMQFTAAVEF IKTIDDRK
//
ID   Q6PAS4_MOUSE            Unreviewed;       893 AA.
AC   Q6PAS4;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 46.
DE   SubName: Full=Dchs1 protein;
DE   Flags: Fragment;
GN   Name=Dchs1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC060096; AAH60096.1; -; mRNA.
DR   IPI; IPI00469095; -.
DR   UniGene; Mm.334108; -.
DR   UniGene; Mm.479808; -.
DR   ProteinModelPortal; Q6PAS4; -.
DR   Ensembl; ENSMUST00000078482; ENSMUSP00000077574; ENSMUSG00000036862.
DR   UCSC; uc009izh.1; mouse.
DR   MGI; MGI:2685011; Dchs1.
DR   eggNOG; roNOG15271; -.
DR   GeneTree; ENSGT00580000081266; -.
DR   InParanoid; Q6PAS4; -.
DR   OMA; TSANHEL; -.
DR   ArrayExpress; Q6PAS4; -.
DR   Bgee; Q6PAS4; -.
DR   Genevestigator; Q6PAS4; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 5.
DR   Pfam; PF00028; Cadherin; 4.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 5.
DR   SUPFAM; SSF49313; Cadherin; 5.
DR   PROSITE; PS00232; CADHERIN_1; 3.
DR   PROSITE; PS50268; CADHERIN_2; 5.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Membrane; Repeat; Transmembrane.
FT   NON_TER       1      1
SQ   SEQUENCE   893 AA;  92397 MW;  F01F4C6DB6324ED1 CRC64;
     GANGHISYHL ASPAEGFRVD PNNGTLFTTV GAMALGHEGP GVVDVVLEAR DHGAPGRTAQ
     ATVHVQLKDQ NDHAPSFTLP HYRVAVSEDL PPGSTLLTLE ATDADGSRTH ATVDYSIISG
     NRGRVFQLEP RLAEVGDGVG PGPQALGCLV LLEPLDFESL TQYNLTVAAA DRGQPPRSSA
     VPVTVTVLDV NDNPPVFTRA SYRVTVPEDM PVGAELLHVE ASDADPGPHG LVHFTLSSGD
     PLGLFELDEN SGALRLSRPL DCETQAQHQL VVQAADPAGT HFSLVPVTVE VQDVNDHGPA
     FPLSLLSTSL AENQPPGTLV TTLHAIDGDA GTFGRLRYSL LEAVPGPEGR EAFSLNSSTG
     ELRARVPFDY EHTGSFRLLV GAADAGNLSA SVTVSVLITG EDEYDPVFLA PSFHFQVPEG
     AQRGHSLGHV QATDEDGGAD GLVLYSLATS SPYFGINQTT GALYLRVDSR APGSGTTTSG
     GGGRTRREAP RELRLEVVAR GPLPGSRSAT VPVTVDITHT ALGLAPDLNL LLVGAVAASL
     GVVVVLALAA LVLGLVRARS RKAEAAPGPM SQTAPIASSS LQKLGREPPS PPPSEHLYHQ
     TLPSYGGPGA GGPYPRGGSL DPSHSSGRGS AEAAEDDEIR MINEFPRVAS VASSLAARGP
     DSGIQQDADG LSDTSCEPPA PDTWYKGRKA GLLLPGAGAT LYREEGPPAT ATAFLGGCGL
     SPAPAGDYGF PADGKPCVAG ALTAIVAGEE ELRGSYNWDY LLSWCPQFQP LASVFTEIAR
     LKDEARPCPP APRIDPPPLI TAVAHPGAKS VPPKPASTAV ARAIFPPASH RSPISHEGSL
     SSAAMSPSFS PSLSPLAARS PVVSPFGVAQ GPSASALSTE SGLEPPDDTE LRI
//
ID   PTN23_MOUSE             Reviewed;        1692 AA.
AC   Q6PB44; Q69ZJ0; Q8R1Z5; Q923E6;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type 23;
DE            EC=3.1.3.48;
GN   Name=Ptpn23; Synonyms=Kiaa1471;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-193.
RC   TISSUE=Dendritic cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 137-438.
RC   TISSUE=Fetal brain, and Fetal eye;
RG   The MGC Project Team;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 394-1692 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1183-1692 (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 712-1439.
RC   TISSUE=Thymus;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1182, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May act as a negative regulator of Ras-mediated
CC       mitogenic activity.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6PB44-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PB44-2; Sequence=VSP_014195;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class subfamily.
CC   -!- SIMILARITY: Contains 1 BRO1 domain.
CC   -!- SIMILARITY: Contains 2 TPR repeats.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32456.1; Type=Erroneous initiation;
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DR   EMBL; BY750106; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; CF734421; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; CB248963; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC006582; AAH06582.1; -; mRNA.
DR   EMBL; BC022721; AAH22721.1; -; mRNA.
DR   EMBL; BC059902; AAH59902.1; -; mRNA.
DR   EMBL; AK173178; BAD32456.1; ALT_INIT; mRNA.
DR   IPI; IPI00464166; -.
DR   IPI; IPI00606716; -.
DR   RefSeq; NP_001074512.1; NM_001081043.1.
DR   UniGene; Mm.335477; -.
DR   PDB; 2W10; X-ray; 1.90 A; C/D=719-730.
DR   PDBsum; 2W10; -.
DR   ProteinModelPortal; Q6PB44; -.
DR   SMR; Q6PB44; 1251-1511.
DR   DIP; DIP-48351N; -.
DR   STRING; Q6PB44; -.
DR   PhosphoSite; Q6PB44; -.
DR   PRIDE; Q6PB44; -.
DR   Ensembl; ENSMUST00000040021; ENSMUSP00000039580; ENSMUSG00000036057.
DR   GeneID; 104831; -.
DR   KEGG; mmu:104831; -.
DR   UCSC; uc009rty.1; mouse.
DR   CTD; 104831; -.
DR   MGI; MGI:2144837; Ptpn23.
DR   eggNOG; roNOG11313; -.
DR   GeneTree; ENSGT00550000074733; -.
DR   HOGENOM; HBG444522; -.
DR   HOVERGEN; HBG082231; -.
DR   InParanoid; Q6PB44; -.
DR   OMA; GPGPHYL; -.
DR   OrthoDB; EOG4NCMBX; -.
DR   PhylomeDB; Q6PB44; -.
DR   BRENDA; 3.1.3.48; 244.
DR   NextBio; 357310; -.
DR   ArrayExpress; Q6PB44; -.
DR   Bgee; Q6PB44; -.
DR   Genevestigator; Q6PB44; -.
DR   GermOnline; ENSMUSG00000036057; Mus musculus.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   InterPro; IPR004328; BRO1.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Gene3D; G3DSA:1.25.40.280; BRO1; 1.
DR   Pfam; PF03097; BRO1; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   PROSITE; PS51180; BRO1; 1.
DR   PROSITE; PS50005; TPR; FALSE_NEG.
DR   PROSITE; PS50293; TPR_REGION; FALSE_NEG.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil; Cytoplasmic vesicle;
KW   Hydrolase; Phosphoprotein; Protein phosphatase; Repeat; TPR repeat.
FT   CHAIN         1   1692       Tyrosine-protein phosphatase non-receptor
FT                                type 23.
FT                                /FTId=PRO_0000094778.
FT   DOMAIN        8    394       BRO1.
FT   REPEAT      250    283       TPR 1.
FT   REPEAT      374    407       TPR 2.
FT   REPEAT      977    978       1.
FT   REPEAT      979    980       2.
FT   REPEAT      981    982       3.
FT   REPEAT      983    984       4.
FT   REPEAT      985    986       5.
FT   REPEAT      987    988       6.
FT   REPEAT      989    990       7.
FT   REPEAT      991    992       8.
FT   REPEAT      993    994       9.
FT   REPEAT      995    996       10.
FT   REPEAT      997    998       11.
FT   REPEAT      999   1000       12.
FT   REPEAT     1001   1002       13.
FT   REPEAT     1003   1004       14.
FT   REPEAT     1005   1006       15.
FT   REPEAT     1007   1008       16.
FT   REPEAT     1009   1010       17.
FT   REPEAT     1011   1012       18.
FT   REPEAT     1013   1014       19.
FT   REPEAT     1015   1016       20.
FT   REPEAT     1017   1018       21.
FT   DOMAIN     1248   1508       Tyrosine-protein phosphatase.
FT   REGION      773   1186       His.
FT   REGION      977   1018       21 X 2 AA approximate tandem repeats of
FT                                P-Q.
FT   COILED      552    639       Potential.
FT   COMPBIAS    719   1164       Pro-rich.
FT   COMPBIAS   1572   1629       Pro-rich.
FT   ACT_SITE   1448   1448       Phosphocysteine intermediate (By
FT                                similarity).
FT   MOD_RES    1179   1179       Phosphoserine (By similarity).
FT   MOD_RES    1182   1182       Phosphoserine.
FT   MOD_RES    1187   1187       Phosphothreonine (By similarity).
FT   VAR_SEQ    1352   1353       Missing (in isoform 2).
FT                                /FTId=VSP_014195.
FT   CONFLICT   1353   1354       Missing (in Ref. 3; AAH06582).
FT   STRAND      724    726
SQ   SEQUENCE   1692 AA;  185216 MW;  331363C917E9C4D2 CRC64;
     MEAVPRMPMI WLDLKEAGDF HFQSAVKKFV LKNYGENPEA YNEELKKLEL LRQNAIRVAR
     DFEGCSVLRK YLGQLHYLQS RVPMGSGQEA AVAVTWTEIF SGKSVSHEDI KYEQACILYN
     LGALHSMLGA MDKRVSEEGM KVSCTHFQCA AGAFAYLREH FPQAFSVDMS RQILTLNVNL
     MLGQAQECLL EKSMLDNRKS FLVARISAQV VDYYKEACRA LENPDTASLL GRIQKDWKKL
     VQMKIYYFAA VAHLHMGKQA EEQQKFGERV AYFQSALDKL NEAIKLAKGQ PDTVQDALRF
     AMDVIGGKYN SAKKDNDFIY HEAVPALDTL QPVKGAPLVK PLPVNPTDPA VTGPDIFAKL
     VPMAAHEASS LYSEEKAKLL REMLAKIEDK NEVLDQFMDS MQLDPETVDN LDAYNHIPPQ
     LMEKCAALSV RPDTVKNLVQ SMQVLSGVFT DVEASLKDIR DLLEEDELQE QKLQETLGQA
     GAGPGPSVAK AELAEVRREW AKYMEVHEKA SFTNSELHRA MNLHVGNLRL LSGPLDQVRA
     ALPTPALTPE DKAVLQNLKR ILAKVQEMRD QRVSLEQQLR ELIQKDDITA SLVTTDHSEM
     KKLFEEQLKK YDQLKVYLEQ NLAAQDNVLR ALTEANVQYA AVRRVLSELD QKWNSTLQTL
     VASYEAYEDL MKKSQEGKDF YADLESKVAT LLERAQSICR AQEAARQQLL DRELKKKAPP
     PRPTAPKPLL SRREEGEAVE AGDTPEELRS LPPDMMVGPR LPDPFLGTTA PLHFSPGPFP
     SSTGPATHYL SGPLPPGTYS GPTQLMQPRA AVPMAPATVL YPAPAYTSEL GLVPRSSPQH
     GIVSSPYAGV GPPQPVVGLP SAPPPQLSGP ELAMTVRPAT TTVDSVQAPI SSHTAPRPNP
     TPALPQPCFP VPQPVPQSVP QPQPLPVPYT YSIGTKQPLP APYTYSIGTK QHLTGPLPQH
     QFPPGIPTGF PVPRTGPQAQ AQPQPQPQPQ PQPQPQPQPQ PQPQSQSQPQ PQPQPQPQRP
     AFGPQPTQQP LPFQHPHLFP SQAPGILPPP PPTPYHFTPQ PGVLGQPPPT LHTQLYPGPS
     QDPLPPHSGA LPFPSPGPPH PHPTLAYGPA PSPRPLGPQA TPVSIRGPPP ASQPTPSPHL
     VPSPAPSPGP GPVPSRPPTA EPPPCLRRGA AAADLLSSSP ESQHGGTQPP GGGQPLLQPT
     KVDAAEGRRP QALRLIEQDP YEHPERLQQL QQELEAFRGQ LGDAGALDAI WRELQEAQEH
     DARGRSIAIA RCYSLKNRHQ DVMPYDSNRV VLRSGKDDYI NASCVEGLSP YCPPLVATQA
     PLPGTAADFW LMVHEQKVSV IVMLVSEAEM EKQKVARYFP TERGQPMVHG ALSVALSSIR
     TTETHVERVL SLQFRDQSLK RSLVHLHFPT WPELGLPDSP GNLLRFIQEV HAHYLHQRPL
     HTPIVVHCSS GVGRTGAFAL LYAAVQEVEA GNGIPELPQL VRRMRQQRKH MLQEKLHLKF
     CHEALVRHVE QVLQRHGVPP PGKPVASVNI SQKNHLPQDS QDLVLGGDVP ISSIQATIAK
     LSIRPLGGLD SPAASLPGLV EPPGLPPASL PESTPVPSSS PPPLSSPLPE APQPEEEPSV
     PEAPSLGPPS SSLELLASLT PEAFSLDSSL RGKQRMSKQN FLQAHNGQGL RAAQPTDDPL
     SLLDPLWTLN KT
//
ID   ANO8_MOUSE              Reviewed;        1060 AA.
AC   Q6PB70; Q05CB5; Q69ZE4;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 3.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Anoctamin-8;
DE   AltName: Full=Transmembrane protein 16H;
GN   Name=Ano8; Synonyms=Kiaa1623, Tmem16h;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1057.
RC   TISSUE=Embryonic tail;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   IDENTIFICATION.
RX   PubMed=15647853;
RA   Katoh M., Katoh M.;
RT   "Identification and characterization of TMEM16H gene in silico.";
RL   Int. J. Mol. Med. 15:353-358(2005).
RN   [4]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=18729231; DOI=10.1002/dvdy.21676;
RA   Rock J.R., Harfe B.D.;
RT   "Expression of TMEM16 paralogs during murine embryogenesis.";
RL   Dev. Dyn. 237:2566-2574(2008).
CC   -!- FUNCTION: May act as a calcium-activated chloride channel (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- DEVELOPMENTAL STAGE: Detected in the mantle layer of the neural
CC       tube and in the dorsal root ganglia at E14.5.
CC   -!- SIMILARITY: Belongs to the anoctamin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32500.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; BC027735; AAH27735.1; -; mRNA.
DR   EMBL; BC059855; AAH59855.1; -; mRNA.
DR   EMBL; AK173222; BAD32500.1; ALT_INIT; Transcribed_RNA.
DR   IPI; IPI00464145; -.
DR   RefSeq; NP_001158151.1; NM_001164679.1.
DR   UniGene; Mm.475713; -.
DR   STRING; Q6PB70; -.
DR   PhosphoSite; Q6PB70; -.
DR   PRIDE; Q6PB70; -.
DR   Ensembl; ENSMUST00000093450; ENSMUSP00000091157; ENSMUSG00000034863.
DR   GeneID; 382014; -.
DR   KEGG; mmu:382014; -.
DR   CTD; 382014; -.
DR   MGI; MGI:2687327; Ano8.
DR   GeneTree; ENSGT00600000084125; -.
DR   HOGENOM; HBG713950; -.
DR   HOVERGEN; HBG100443; -.
DR   InParanoid; Q6PB70; -.
DR   OrthoDB; EOG41JZBJ; -.
DR   ArrayExpress; Q6PB70; -.
DR   Bgee; Q6PB70; -.
DR   Genevestigator; Q6PB70; -.
DR   GermOnline; ENSMUSG00000034863; Mus musculus.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   InterPro; IPR007632; Anoctamin.
DR   PANTHER; PTHR12308; DUF590; 1.
DR   Pfam; PF04547; DUF590; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Chloride; Chloride channel; Glycoprotein; Ion transport;
KW   Ionic channel; Membrane; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1   1060       Anoctamin-8.
FT                                /FTId=PRO_0000249004.
FT   TOPO_DOM      1    244       Cytoplasmic (Potential).
FT   TRANSMEM    245    265       Helical; (Potential).
FT   TOPO_DOM    266    281       Extracellular (Potential).
FT   TRANSMEM    282    302       Helical; (Potential).
FT   TOPO_DOM    303    356       Cytoplasmic (Potential).
FT   TRANSMEM    357    377       Helical; (Potential).
FT   TOPO_DOM    378    400       Extracellular (Potential).
FT   TRANSMEM    401    421       Helical; (Potential).
FT   TOPO_DOM    422    437       Cytoplasmic (Potential).
FT   TRANSMEM    438    458       Helical; (Potential).
FT   TOPO_DOM    459    745       Extracellular (Potential).
FT   TRANSMEM    746    766       Helical; (Potential).
FT   TOPO_DOM    767    802       Cytoplasmic (Potential).
FT   TRANSMEM    803    823       Helical; (Potential).
FT   TOPO_DOM    824    836       Extracellular (Potential).
FT   TRANSMEM    837    857       Helical; (Potential).
FT   TOPO_DOM    858   1060       Cytoplasmic (Potential).
FT   COMPBIAS    353    519       Leu-rich.
FT   COMPBIAS    550    600       Glu-rich.
FT   COMPBIAS    877    926       Arg-rich.
FT   COMPBIAS    949   1013       Pro-rich.
FT   CARBOHYD    708    708       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    196    196       I -> AV (in Ref. 2; BAD32500).
SQ   SEQUENCE   1060 AA;  119101 MW;  B10687A73CD65802 CRC64;
     MAEAASGAGD VTLEGERGKR PPPEGEPAAP ASGVLDKLFG KRLLQAGRYL VSHKAWMKTV
     PTEDCDVLMT FPDTTDDHTL LWLLNHIRVG IPELIVQVRH HRHTRAYAFF VTATYESLLR
     GADELGLRKA VKAEFGGGTR SFSCEEDFIY ENVESELRFF TSQERQSIIR FWLQNLRAKQ
     GEALHNVRFL EDQPIIPELA ARGIIQQVFP VHEQRILNRL MKSWVQAVCE NQPLDDICDY
     FGVKIAMYFA WLGFYTSAMV YPAVFGSVLY TFTEADQTSR DVSCVVFALF NVIWSTLFLE
     EWKRRGAELA YKWGTLDSPG EAVEEPRPQF RGIRRISPIT RAEEFYYPPW KRLLFQLLVS
     LPLCLACLIC VFILMLGCFQ LQELVLSVKG LPRLVRFLPK VMLALLVSVS AEGYKKLAVW
     LNDMENYRLE STYERHLIIK VVLFQFVNSY LSLFYIGFYL KDMDRLKEML ATLLITRQLL
     QNVREVLQPH LYRRLGSGEL GLRTILELAR ALLGLLNPLR PDPRRHLEAQ ADEGGAGSRR
     CLGGGCGAPE EENEEEEEAA VERRPAGEGG EVPEGPRGGK EEDEEEDDDE DEDEEYEGEE
     GSLLDCGLRL KKVSFAERGA GRRRPGPSPD GLLEEGSPTM VEKGLEPGVF TLAEEDDEPE
     GPPGSPGPEP QTVLLRRARG EGRDQGPDGD RDTETGSGDA AGRQKRHNRS SWIDPPEEEH
     SPQLTQAELE SCMKKYEDTF QDYQEMFVQF GYVVLFSSAF PLAALCALVN NLIEIRSDAF
     KLCTGLQRPF GRRVESIGQW QKVMEAMGVL AIVVNCYLIG QCGQLQRLFP WLSPEAAIVS
     VVVLEHLALL VKYLIHVAIP DIPGWVAEEM AKLEYQRREA FKRHERQAQQ RFQQQQRRRR
     EEEERQRHAE QQARRERDTG GREEARAEAP GPDPVAERGA AKAKGSERPR RPGALLPPGP
     VLRLKQIIPL QTRPPAPTGC APPPRSPADT RLPAFLSLRF LKAPERGPSP PRPGKLFAFS
     AREPSANGAP GGGARAHRSA GDEPAAAEPE PRPEDAGHRP
//
ID   TTBK1_MOUSE             Reviewed;        1308 AA.
AC   Q6PCN3;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 3.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Tau-tubulin kinase 1;
DE            EC=2.7.11.1;
GN   Name=Ttbk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 832-1308.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=16923168; DOI=10.1111/j.1471-4159.2006.04059.x;
RA   Sato S., Cerny R.L., Buescher J.L., Ikezu T.;
RT   "Tau-tubulin kinase 1 (TTBK1), a neuron-specific tau kinase candidate,
RT   is involved in tau phosphorylation and aggregation.";
RL   J. Neurochem. 98:1573-1584(2006).
CC   -!- FUNCTION: Serine/threonine kinase which is able to phosphorylate
CC       TAU on serine, threonine and tyrosine residues. Induces
CC       aggregation of TAU (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Divalent cations. Magnesium or, to a lesser extent,
CC       manganese, but not calcium or zinc (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in the brain. Strong expression in
CC       the cortical layers, the CA1 layers of the hippocampus and the
CC       granular layer of the cerebellum. Also expressed in the large
CC       cortical pyramidal cells in the temporal cortex, the CA1 pyramidal
CC       neurons and the cerebellum granular neurons.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC       protein kinase family.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AC165445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CAAA01116144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC059249; AAH59249.3; -; mRNA.
DR   IPI; IPI00938523; -.
DR   RefSeq; NP_001156336.1; NM_001162864.1.
DR   UniGene; Mm.297613; -.
DR   UniGene; Mm.460339; -.
DR   ProteinModelPortal; Q6PCN3; -.
DR   SMR; Q6PCN3; 27-313.
DR   STRING; Q6PCN3; -.
DR   PhosphoSite; Q6PCN3; -.
DR   PRIDE; Q6PCN3; -.
DR   Ensembl; ENSMUST00000047034; ENSMUSP00000044580; ENSMUSG00000015599.
DR   GeneID; 106763; -.
DR   KEGG; mmu:106763; -.
DR   UCSC; uc008csx.1; mouse.
DR   CTD; 106763; -.
DR   MGI; MGI:2147036; Ttbk1.
DR   GeneTree; ENSGT00600000084076; -.
DR   HOGENOM; HBG716715; -.
DR   HOVERGEN; HBG094095; -.
DR   InParanoid; Q6PCN3; -.
DR   OMA; PFEVNGL; -.
DR   OrthoDB; EOG4BVRSW; -.
DR   PhylomeDB; Q6PCN3; -.
DR   BRENDA; 2.7.11.1; 244.
DR   ArrayExpress; Q6PCN3; -.
DR   Bgee; Q6PCN3; -.
DR   CleanEx; MM_TTBK1; -.
DR   Genevestigator; Q6PCN3; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1   1308       Tau-tubulin kinase 1.
FT                                /FTId=PRO_0000278542.
FT   DOMAIN       34    297       Protein kinase.
FT   NP_BIND      40     48       ATP (By similarity).
FT   COMPBIAS    734    796       Glu-rich.
FT   COMPBIAS   1103   1107       Poly-Ser.
FT   ACT_SITE    154    154       Proton acceptor (By similarity).
FT   BINDING      63     63       ATP (By similarity).
SQ   SEQUENCE   1308 AA;  141613 MW;  8940FE7A58889736 CRC64;
     MQCLAAALKD ETNMSGGGEQ ADILPANYVV KDRWKVLKKI GGGGFGEIYE AMDLLTRENV
     ALKVESAQQP KQVLKMEVAV LKKLQGKDHV CRFIGCGRNE KFNYVVMQLQ GRNLADLRRS
     QPRGTFTLST TLRLGKQILE SIEAIHSVGF LHRDIKPSNF AMGRLPSTYR KCYMLDFGLA
     RQYTNTTGDV RPPRNVAGFR GTVRYASVNA HKNREMGRHD DLWSLFYMLV EFAVGQLPWR
     KIKDKEQVGM IKEKYEHRML LKHMPSEFHL FLDHIASLDY FTKPDYQLIM SVFENSMKER
     GIAENEAFDW EKAGTDALLS TSTSTPPQQN TRQTAAMFGV VNVTPVPGDL LRENTEDVLQ
     GEHLSDQENA PPILPGRPPE GLGPGPHLVP HPGGPEAEVW EETDVNRNKL RINIGKTPCV
     EEEQSRGVGV PSSPVRAPPD SPTTPVRSLC YRRVNSPESE RLSTAADGRV ELQERRSRMD
     LPGSPSRQAC SSQPAQMLSV DTGHADRQAS GRMDVSASVE QEALSNAFRS VPLAEEEDFD
     SKEWVIIDKE TELKDFPPGA EPSTSGTTDE EPEELRPLPE EGEERRRLGT EPTVRPRGRG
     MHTLTEEDPR QMLPQPAPPQ LSQADGRSET SQPPTPGSPS HSPLHSGPRP RRRESDPTGP
     QRQVFSVAPP FEVNGLPRAV PLALPYQDFK RDLSDYRERA RLLNRVRRVG FSHMLLTAPQ
     VPLAPFQPQA NGKEGEEEEE EEEEEEEEEE EEEEEEEEEE EEEEEEEEAG ALGEVLGPRS
     GSSSEGSERS TERSQEGAPS TLLADDQKEA RGRASMADGD LEPEEGSKTL VLVSPGDMKK
     SPVTAELAPD PDLGTLAALT PQHERPQPTG SQLDVSEPGT LSSILKSEPK PSGPGAGGGV
     GLVAPGAGVT AVTSPFTKVE RTFVHIAEKS HLNVMSSGGQ ASRPEELSTG GELGLEVLSE
     GGIAEEGAPA PLENGMALAG LDGTEMESCA LSGPPGETPS EVVTDSLPNG PALADGPAPA
     SQQEPVTKKG TTISPSRHAM PGSRPRSRIP VLLSEEDTGS EPSGSLSAKE RWSKRARPQQ
     DLARLVMEKR QGRLLLRLAS GASSSSSEEQ RRASETLSGT GSEEDTPASE PTTALPRKAV
     RAATTRSRIP RPISVSMPVE GQQLPGRPHG AASATDLAIT SRLQLQKPSG LAPAADLRPK
     QSASRGPGPG RAQVSKPAAP RSPGLPASTA RHPSGSPRSQ SLSRKESSSP SHQARPGVPP
     SRGVLQVRSQ PEASPVAPKK GPKGKQLQTQ RAATKGRAVV SEGRPGAR
//
ID   HLTF_MOUSE              Reviewed;        1003 AA.
AC   Q6PCN7; O35596; O35597; Q80VT6;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Helicase-like transcription factor;
DE            EC=3.6.4.-;
DE            EC=6.3.2.-;
DE   AltName: Full=P113;
DE   AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3;
DE   AltName: Full=Sucrose nonfermenting protein 2-like 3;
DE   AltName: Full=TNF-response element-binding protein;
GN   Name=Hltf; Synonyms=Smarca3, Snf2l3, Zbu1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, AND
RP   FUNCTION.
RC   TISSUE=Liver;
RX   PubMed=9427542; DOI=10.1016/S0378-1119(97)00446-0;
RA   Zhang Q., Ekhterae D., Kim K.-H.;
RT   "Molecular cloning and characterization of P113, a mouse SNF2/SWI2-
RT   related transcription factor.";
RL   Gene 202:31-37(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=9126292; DOI=10.1006/dbio.1996.8486;
RA   Gong X., Kaushal S., Ceccarelli E., Bogdanova N., Neville C.,
RA   Nguyen T., Clark H., Khatib Z.A., Valentine M., Look A.T.,
RA   Rosenthal N.;
RT   "Developmental regulation of Zbu1, a DNA-binding member of the
RT   SWI2/SNF2 family.";
RL   Dev. Biol. 183:166-182(1997).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
CC   -!- FUNCTION: Has both helicasee and E3 ubiquitin ligase activities.
CC       Possesses intrinsic ATP-dependent nucleosome-remodeling activity.
CC       This activity may be required for transcriptional activation or
CC       repression of specific target promoters (By similarity). These may
CC       include the SERPINE1, to which this protein can bind directly.
CC       Plays a role in error-free postreplication repair (PRR) of damaged
CC       DNA and maintains genomic stability through acting as a ubiquitin
CC       ligase for 'Lys-63'-linked polyubiquitination of chromatin-bound
CC       PCNA (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Binds to SP1 and SP3 independent of DNA; the interaction
CC       with these transcriptional factors may be required for basal
CC       transcription of target genes. Interacts with PCNA; the
CC       interaction promotes polyubiquitination of PCNA through
CC       association with the UBE2B-RAD18 and UBE2V2-UBE2N ubiquitin ligase
CC       complexes. Interacts with RAD18, SHPRH, UBE2V2 and UBE2N (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver,
CC       lung, pancreas, placenta and skeletal muscle.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the heart from E11.5. Gradually
CC       increases in skeletal muscle to E18.5.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RAD16
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB63915.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF010138; AAB64175.1; -; Genomic_DNA.
DR   EMBL; AF010600; AAB63915.1; ALT_SEQ; mRNA.
DR   EMBL; BC039796; AAH39796.1; -; mRNA.
DR   EMBL; BC057116; AAH57116.1; -; mRNA.
DR   EMBL; BC059240; AAH59240.1; -; mRNA.
DR   IPI; IPI00315178; -.
DR   RefSeq; NP_033236.2; NM_009210.2.
DR   RefSeq; NP_659208.2; NM_144959.2.
DR   UniGene; Mm.209650; -.
DR   ProteinModelPortal; Q6PCN7; -.
DR   SMR; Q6PCN7; 62-150, 470-981.
DR   STRING; Q6PCN7; -.
DR   PhosphoSite; Q6PCN7; -.
DR   PRIDE; Q6PCN7; -.
DR   Ensembl; ENSMUST00000002502; ENSMUSP00000002502; ENSMUSG00000002428.
DR   GeneID; 20585; -.
DR   KEGG; mmu:20585; -.
DR   NMPDR; fig|10090.3.peg.7817; -.
DR   UCSC; uc008osk.1; mouse.
DR   CTD; 20585; -.
DR   MGI; MGI:1196437; Hltf.
DR   eggNOG; roNOG07324; -.
DR   HOGENOM; HBG750276; -.
DR   HOVERGEN; HBG079192; -.
DR   InParanoid; Q6PCN7; -.
DR   OMA; HAKCPLC; -.
DR   OrthoDB; EOG47SSD6; -.
DR   PhylomeDB; Q6PCN7; -.
DR   NextBio; 298877; -.
DR   ArrayExpress; Q6PCN7; -.
DR   Bgee; Q6PCN7; -.
DR   CleanEx; MM_HLTF; -.
DR   Genevestigator; Q6PCN7; -.
DR   GermOnline; ENSMUSG00000002428; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003702; F:RNA polymerase II transcription factor activity; IDA:MGI.
DR   GO; GO:0016563; F:transcription activator activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR014905; HIP116_Rad5p_N.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF08797; HIRAN; 1.
DR   Pfam; PF00176; SNF2_N; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00910; HIRAN; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Activator; ATP-binding; Chromatin regulator; DNA-binding; Helicase;
KW   Hydrolase; Ligase; Metal-binding; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Transcription;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1   1003       Helicase-like transcription factor.
FT                                /FTId=PRO_0000056185.
FT   DOMAIN      433    600       Helicase ATP-binding.
FT   DOMAIN      831    990       Helicase C-terminal.
FT   NP_BIND     294    301       ATP (By similarity).
FT   ZN_FING     754    795       RING-type.
FT   REGION       38    287       DNA binding (By similarity).
FT   REGION      919   1003       Interaction with SP1 and SP3 (By
FT                                similarity).
FT   MOTIF       551    554       DEGH box.
FT   MOD_RES     391    391       Phosphotyrosine (By similarity).
FT   MOD_RES     394    394       Phosphoserine (By similarity).
FT   MOD_RES     395    395       Phosphoserine (By similarity).
FT   MOD_RES     397    397       Phosphoserine (By similarity).
FT   MOD_RES     629    629       Phosphoserine.
FT   MOD_RES     730    730       Phosphothreonine (By similarity).
FT   CONFLICT    150    150       F -> Y (in Ref. 1; AAB64175/AAB63915).
FT   CONFLICT    191    191       A -> R (in Ref. 1; AAB64175/AAB63915).
FT   CONFLICT    394    394       S -> N (in Ref. 1; AAB64175/AAB63915).
FT   CONFLICT    648    648       P -> S (in Ref. 1; AAB64175/AAB63915).
FT   CONFLICT    902    905       MLLS -> STV (in Ref. 1; AAB64175).
FT   CONFLICT    918    918       A -> R (in Ref. 1; AAB64175).
FT   CONFLICT    980    980       G -> A (in Ref. 1; AAB64175).
SQ   SEQUENCE   1003 AA;  113317 MW;  91F08509ACEA5513 CRC64;
     MSYTFTRGPV WKYSQSVQYG SHENIPRLSY STFLPHFEFQ DIIPPDDFLT SDEEQDLVLF
     GTMRGQVVGL RYYTGVVNNN EMVALQREPN NPYDKNAIKV NNVNGNQVGH IKREIAAAVA
     YIMDNKLAQV EGVVPFGASN TFTMPLYMTF WGKEENRNVV LEQLKKHGFK LGPTPKTLGS
     SLENAWGSGR AGPSYSRPAH VAVQMTTDQL KTEFDKLFED LKEDDRTVEM EPAEAIETPL
     LPHQKQALAW MIARENSKEL PPFWEQRNDL YYNTITNFSV KERPENVHGG ILADDMGLGK
     TLTAIAVILT NFDDGRPLLS KRGKKNHPGK EYKDETIKRR GSNMDKKEDG HSESSTCGEE
     PSISGTPEKS SCTLSQLSSV CPKRRKISVQ YIESSDSEEI ETSELPQKMK GKLKNVQLNT
     KSRVKGSSKV KEDSKFALTF FASATQRKML KKGMSMMECS EACDTGERTR ATLIICPLSV
     LSNWIDQFGQ HVKSEVHLNF YVYYGPDRIR DSAWLSKQDI ILTTYNILTH DYGTKDDSPL
     HSIKWLRVIL DEGHAIRNPN AQQTKAVLEL EAERRWVLTG TPIQNSLKDL WSLLSFLKLK
     PFIDREWWYR IIQRPVTTGD EGGLRRLQSL IKNITLRRTK TSKIKGKPVL ELPERKVFIQ
     HITLSEEERK IYQSVKNEGK AAIGRYFTEG TVLAHYADVL GLLLRLRQIC CHTHLLTNGM
     SSSGPSRSDT PEELRKMLIE KMKIILSSGS DEECAICLDS LTFPVITHCA HVFCKPCICQ
     VIHSEQPHAK CPLCRNEIHG DNLLECPPEE LACDSDKESS MEWKSSSKIN ALMHALIELR
     TKDPNIKSLV VSQFTTFLSL IETPLKASGF VFTRLDGSMA QKKRVESIQR FQNTEAGSPT
     IMLLSLKAGG VGLNLCAASR VFLMDPAWNP AAEDQCFDRC HRLGQKQEVI ITKFIVKDSV
     EENMLKIQNT KRDLAAGAFG TKKTDANDMK QAKINEIRTL IDL
//
ID   MFF_MOUSE               Reviewed;         291 AA.
AC   Q6PCP5; Q3UT87; Q91VG0; Q9D3P5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Mitochondrial fission factor;
GN   Name=Mff;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Egg, and Xiphoid cartilage;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146 AND SER-151, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129 AND SER-131, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Plays a role in mitochondrial and peroxisomal fission
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC       type IV membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q6PCP5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PCP5-2; Sequence=VSP_025959, VSP_025961;
CC       Name=3;
CC         IsoId=Q6PCP5-3; Sequence=VSP_025961;
CC       Name=4;
CC         IsoId=Q6PCP5-4; Sequence=VSP_025960;
CC   -!- SIMILARITY: Belongs to the tango11 family.
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DR   EMBL; AK017226; BAB30643.1; -; mRNA.
DR   EMBL; AK139649; BAE24093.1; -; mRNA.
DR   EMBL; BC016597; AAH16597.1; -; mRNA.
DR   EMBL; BC059229; AAH59229.1; -; mRNA.
DR   IPI; IPI00126855; -.
DR   IPI; IPI00420734; -.
DR   IPI; IPI00467571; -.
DR   IPI; IPI00850543; -.
DR   RefSeq; NP_083685.2; NM_029409.2.
DR   UniGene; Mm.479553; -.
DR   ProteinModelPortal; Q6PCP5; -.
DR   STRING; Q6PCP5; -.
DR   PhosphoSite; Q6PCP5; -.
DR   PRIDE; Q6PCP5; -.
DR   Ensembl; ENSMUST00000073025; ENSMUSP00000072784; ENSMUSG00000026150.
DR   Ensembl; ENSMUST00000076837; ENSMUSP00000076112; ENSMUSG00000026150.
DR   Ensembl; ENSMUST00000078332; ENSMUSP00000077446; ENSMUSG00000026150.
DR   GeneID; 75734; -.
DR   KEGG; mmu:75734; -.
DR   UCSC; uc007brx.1; mouse.
DR   CTD; 75734; -.
DR   MGI; MGI:1922984; Mff.
DR   eggNOG; roNOG10227; -.
DR   GeneTree; ENSGT00390000009776; -.
DR   HOGENOM; HBG713948; -.
DR   HOVERGEN; HBG105704; -.
DR   InParanoid; Q6PCP5; -.
DR   OMA; SVIMQVP; -.
DR   OrthoDB; EOG441QBV; -.
DR   PhylomeDB; Q6PCP5; -.
DR   NextBio; 343810; -.
DR   ArrayExpress; Q6PCP5; -.
DR   Bgee; Q6PCP5; -.
DR   Genevestigator; Q6PCP5; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR008518; DUF800.
DR   PANTHER; PTHR16501; DUF800; 1.
DR   Pfam; PF05644; DUF800; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    291       Mitochondrial fission factor.
FT                                /FTId=PRO_0000289185.
FT   TOPO_DOM      1    271       Cytoplasmic (Potential).
FT   TRANSMEM    272    289       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   TOPO_DOM    290    291       Mitochondrial intermembrane (Potential).
FT   COILED      240    271       Potential.
FT   MOD_RES     129    129       Phosphoserine.
FT   MOD_RES     131    131       Phosphoserine.
FT   MOD_RES     146    146       Phosphoserine.
FT   MOD_RES     149    149       Phosphothreonine (By similarity).
FT   MOD_RES     151    151       Phosphoserine.
FT   VAR_SEQ     117    117       E -> EQ (in isoform 2).
FT                                /FTId=VSP_025959.
FT   VAR_SEQ     147    220       IVTPSPPQARVCPPHMLPEDGANLSSARGILSLIQSSTRRA
FT                                YQQILDVLDENRRPVLRGGSAAATSNPHHDNVR -> M
FT                                (in isoform 4).
FT                                /FTId=VSP_025960.
FT   VAR_SEQ     148    200       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_025961.
SQ   SEQUENCE   291 AA;  32931 MW;  658884A1EF8EBCFD CRC64;
     MAEISRIQYE MEYTEGISQR MRVPEKLKVA PPNADLEQEF QDGVPNASVI MQVPERIVVT
     GNNEDISFSR PADLDLIQST PFKPLALKTP PRVLTLSERP LDFLDLERPL PTPQSEESRA
     VGRLKRERSM SENAVRQNGQ LVRNDSIVTP SPPQARVCPP HMLPEDGANL SSARGILSLI
     QSSTRRAYQQ ILDVLDENRR PVLRGGSAAA TSNPHHDNVR YGISNLDAAI EGASDDMTVV
     DAASLRRQII KLNRRLQLLE EENKERAKRE MVMYSITVAF WLLNSWLWFR R
//
ID   Q6PCW9_MOUSE            Unreviewed;       170 AA.
AC   Q6PCW9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-FEB-2011, entry version 52.
DE   SubName: Full=Myl1 protein;
DE   SubName: Full=Myosin, light polypeptide 1;
GN   Name=Myl1; ORFNames=AC124389.4-004;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Jaw and Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Kerry G.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC059087; AAH59087.1; -; mRNA.
DR   EMBL; CU407305; CAQ51715.1; -; Genomic_DNA.
DR   IPI; IPI00895557; -.
DR   UniGene; Mm.1000; -.
DR   HSSP; P62158; 1K90.
DR   ProteinModelPortal; Q6PCW9; -.
DR   SMR; Q6PCW9; 3-141.
DR   STRING; Q6PCW9; -.
DR   PRIDE; Q6PCW9; -.
DR   Ensembl; ENSMUST00000120415; ENSMUSP00000112880; ENSMUSG00000061816.
DR   MGI; MGI:97269; Myl1.
DR   GeneTree; ENSGT00590000082921; -.
DR   HOVERGEN; HBG012180; -.
DR   PhylomeDB; Q6PCW9; -.
DR   ArrayExpress; Q6PCW9; -.
DR   Bgee; Q6PCW9; -.
DR   Genevestigator; Q6PCW9; -.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   SMART; SM00054; EFh; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   170 AA;  18866 MW;  9D8FF0B0A81067C4 CRC64;
     MSFSADQIAD FKEAFLLFDR TGECKITLSQ VGDVLRALGT NPTNAEVKKV LGNPSNEEMN
     AKKIEFEQFL PMMQAISNNK DQGGYEDFVE GLRVFDKEGN GTVMGAELRH VLATLGEKMK
     EEEVEALLAG QEDSNGCINY EGTASLTSLR RDSFSTLFSS SLLTYMTYYK
//
ID   TRI37_MOUSE             Reviewed;         961 AA.
AC   Q6PCX9; Q8CHC5;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=E3 ubiquitin-protein ligase TRIM37;
DE            EC=6.3.2.-;
DE   AltName: Full=Tripartite motif-containing protein 37;
GN   Name=Trim37; Synonyms=Kiaa0898;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region (By
CC       similarity). Peroxisome (By similarity). Note=Found in vesicles of
CC       the peroxisome (By similarity). Aggregates as aggresomes, a
CC       perinuclear region where certain misfolded or aggregated proteins
CC       are sequestered for proteosomal degradation (By similarity).
CC   -!- PTM: Auto-ubiquitinated (By similarity).
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC   -!- SIMILARITY: Contains 1 B box-type zinc finger.
CC   -!- SIMILARITY: Contains 1 MATH domain.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC41455.1; Type=Erroneous initiation;
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DR   EMBL; AB093271; BAC41455.1; ALT_INIT; Transcribed_RNA.
DR   EMBL; BC058678; AAH58678.1; -; mRNA.
DR   EMBL; BC059070; AAH59070.1; -; mRNA.
DR   IPI; IPI00381355; -.
DR   RefSeq; NP_932104.1; NM_197987.1.
DR   UniGene; Mm.17436; -.
DR   ProteinModelPortal; Q6PCX9; -.
DR   SMR; Q6PCX9; 1-84, 90-136, 278-404.
DR   STRING; Q6PCX9; -.
DR   PhosphoSite; Q6PCX9; -.
DR   PRIDE; Q6PCX9; -.
DR   Ensembl; ENSMUST00000041282; ENSMUSP00000049057; ENSMUSG00000018548.
DR   GeneID; 68729; -.
DR   KEGG; mmu:68729; -.
DR   NMPDR; fig|10090.3.peg.24983; -.
DR   UCSC; uc007ktm.1; mouse.
DR   CTD; 68729; -.
DR   MGI; MGI:2153072; Trim37.
DR   GeneTree; ENSGT00410000025800; -.
DR   HOGENOM; HBG443598; -.
DR   HOVERGEN; HBG057591; -.
DR   InParanoid; Q6PCX9; -.
DR   OMA; RKMVTLG; -.
DR   OrthoDB; EOG42NHZP; -.
DR   PhylomeDB; Q6PCX9; -.
DR   NextBio; 327786; -.
DR   ArrayExpress; Q6PCX9; -.
DR   Bgee; Q6PCX9; -.
DR   CleanEx; MM_TRIM37; -.
DR   Genevestigator; Q6PCX9; -.
DR   GermOnline; ENSMUSG00000018548; Mus musculus.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR002083; MATH.
DR   InterPro; IPR008974; TRAF-like.
DR   InterPro; IPR013322; TRAF-type.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:2.60.210.10; TRAF-type; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00917; MATH; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00061; MATH; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF49599; Traf_like; 1.
DR   PROSITE; PS50144; MATH; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Ligase; Metal-binding; Peroxisome;
KW   Phosphoprotein; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    961       E3 ubiquitin-protein ligase TRIM37.
FT                                /FTId=PRO_0000056255.
FT   DOMAIN      276    403       MATH.
FT   ZN_FING      15     55       RING-type; degenerate.
FT   ZN_FING      90    132       B box-type.
FT   COILED      132    234       Potential.
FT   COILED      419    450       Potential.
FT   COMPBIAS    535    541       Poly-Ser.
FT   COMPBIAS    579    582       Poly-Ala.
FT   MOD_RES     770    770       Phosphoserine (By similarity).
FT   MOD_RES     772    772       Phosphoserine (By similarity).
FT   CONFLICT    227    232       Missing (in Ref. 1; BAC41455).
SQ   SEQUENCE   961 AA;  107660 MW;  85629CEFE0A1D6EA CRC64;
     MDEQSVESIA EVFRCFICME KLRDARLCPH CSKLCCFSCI RRWLTEQRAQ CPHCRAPLQL
     RELVNCRWAE EVTQQLDTLQ LCSLTKHEEN EKDKCENHHE KLSVFCWTCK KCICHQCALW
     GGMHGGHTFK PLAEIYEQHV TKVNEEVAKL RRRLMELISL VQEVERNVEA VRNAKDERVR
     EIRNAVEMMI ARLDTQLKNK LITLMGQKTS LTQETELLES LLQEVEHQLR SCSKSELISK
     SSEILMMFQQ VHRKPMASFV TTPVPPDFTS ELVPSYDSAT FVLENFSTLR QRADPVYSPP
     LQVSGLCWRL KVYPDGNGVV RGYYLSVFLE LSAGLPETSK YEYRVEMVHQ SCNDPTKNII
     REFASDFEVG ECWGYNRFFR LDLLANEGYL NRQNDTVILR FQVRSPTFFQ KCRDQHWYIT
     QLEAAQTGYI QQINNLKERL TIELSRTQKS RDLSPPDNHL SPQNDDSPET RTKKAGSCSD
     MLLEGGPTCA SVRETKEDED EEEKIQNEDY HHELSDGDLD LDLVGEDEVN HLDGSSSSAS
     STATSNTEEN DIDEETMSGE NDVEYNSMEL EEGELMEDAA AAGPPGSSHS YVGASSRMSR
     RTHLCSAATS SLLDIDPLIL IHLLDLKDRS SMENLWGLQP RPSASLLQPT ASYSRKDKDQ
     RKQQAMWRVP SDLKMLKRLK TQMAEVRCMK TDVKTTLSDI KGSSVASTDM QTNLFCADQA
     ALTTCGPENS GRLQDLGMEL LAKSSVAGCY IRNPTNKKNS PKSARAIAGS LSLRRAVDSG
     ENSRSKGDCQ VLAEGSSGSS QSGSRHSSPR ALTHGIIGDL LPKSEDRQCK ALDSDAVVVA
     VFNGLPTVEK RRKMVTLGTN AKGGRLEGMQ MADLESHSEA GEVQPTLPEG ASAAPEEGMS
     SDSDIECDTE NEEQEEHTSM GAFNDPFLAQ PPDEDSHSSF PDGEQIDPEN LHFNPDEGGG
     R
//
ID   SHB_MOUSE               Reviewed;         503 AA.
AC   Q6PD21; A2AKW3; Q3ULM3;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=SH2 domain-containing adapter protein B;
GN   Name=Shb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Fetal brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=94134414; PubMed=8302579;
RA   Welsh M., Mares J., Karlsson T., Lavergne C., Breant B.,
RA   Claesson-Welsh L.;
RT   "Shb is a ubiquitously expressed Src homology 2 protein.";
RL   Oncogene 9:19-27(1994).
RN   [5]
RP   INDUCTION BY OKADAIC ACID AND GENISTEIN.
RX   PubMed=8777141; DOI=10.1016/0898-6568(95)02019-5;
RA   Lavergne C., Mares J., Karlsson T., Breant B., Welsh M.;
RT   "Control of SHB gene expression by protein phosphorylation.";
RL   Cell. Signal. 8:55-58(1996).
RN   [6]
RP   INTERACTION WITH PTPN11.
RX   PubMed=12181353; DOI=10.1091/mbc.E02-02-0103;
RA   Cross M.J., Lu L., Magnusson P., Nyqvist D., Holmqvist K., Welsh M.,
RA   Claesson-Welsh L.;
RT   "The Shb adaptor protein binds to tyrosine 766 in the FGFR-1 and
RT   regulates the Ras/MEK/MAPK pathway via FRS2 phosphorylation in
RT   endothelial cells.";
RL   Mol. Biol. Cell 13:2881-2893(2002).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-113, AND MASS
RP   SPECTROMETRY.
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Adapter protein which regulates several signal
CC       transduction cascades by linking activated receptors to downstream
CC       signaling components. May play a role in angiogenesis by
CC       regulating FGFR1, VEGFR2 and PDGFR signaling. May also play a role
CC       in T-cell antigen receptor/TCR signaling, interleukin-2 signaling,
CC       apoptosis and neuronal cells differentiation by mediating basic-
CC       FGF and NGF-induced signaling cascades. May also regulate IRS1 and
CC       IRS2 signaling in insulin-producing cells (By similarity).
CC   -!- SUBUNIT: Interacts with phosphorylated 'Tyr-720' of the ligand-
CC       activated receptor PDGFRA via its SH2 domain. Interacts with the
CC       ligand-activated receptors PDGFRB, FGFR1, KDR/VEGFR2, IL2RB and
CC       IL2RG. Interacts with EPS8 and V-SRC. Interacts with GRB2 and
CC       GRAP. Interacts with CD3Z. Interacts with tyrosine-phosphorylated
CC       LAT upon T-cell antigen receptor activation. Interacts with PLCG1.
CC       Interacts with ZAP70, LCP2/SLP-76, VAV1 and GRAP2. Interacts with
CC       JAK1 and JAK3. Interacts with PTK2/FAK1. Interacts with CRK/CrKII.
CC       Interacts with IRS2 (By similarity). Interacts with PTPN11.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane;
CC       Peripheral membrane protein; Cytoplasmic side (By similarity).
CC       Note=Associates with membrane lipid rafts upon TCR stimulation (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6PD21-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PD21-2; Sequence=VSP_019848, VSP_019849, VSP_019850;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in heart, liver, brain and kidney
CC       (at protein level).
CC   -!- INDUCTION: Up-regulated by okadaic acid and genistein.
CC   -!- DOMAIN: The SH2 domain preferentially binds phosphopeptides with
CC       the consensus sequence Y-[TVI]-X-L and mediates interaction with
CC       PDGFRA, PDGFRB, FGRFR1, IL2RB, IL2RG, CD3Z and CRK/CrKII (By
CC       similarity).
CC   -!- PTM: Phosphorylated upon PDGFRA, PDGFRB, TCR, IL2 receptor, FGFR1
CC       or VEGFR2 activation (By similarity).
CC   -!- SIMILARITY: Contains 1 SH2 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH58986.1; Type=Erroneous initiation;
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DR   EMBL; AK145414; BAE26425.1; -; mRNA.
DR   EMBL; AL772376; CAM20448.1; -; Genomic_DNA.
DR   EMBL; BC058986; AAH58986.1; ALT_INIT; mRNA.
DR   IPI; IPI00652485; -.
DR   IPI; IPI00938488; -.
DR   RefSeq; NP_001028478.1; NM_001033306.1.
DR   UniGene; Mm.251716; -.
DR   ProteinModelPortal; Q6PD21; -.
DR   SMR; Q6PD21; 397-501.
DR   STRING; Q6PD21; -.
DR   PhosphoSite; Q6PD21; -.
DR   PRIDE; Q6PD21; -.
DR   Ensembl; ENSMUST00000061986; ENSMUSP00000060433; ENSMUSG00000044813.
DR   Ensembl; ENSMUST00000098095; ENSMUSP00000095699; ENSMUSG00000044813.
DR   GeneID; 230126; -.
DR   KEGG; mmu:230126; -.
DR   UCSC; uc008sss.1; mouse.
DR   UCSC; uc008sst.1; mouse.
DR   CTD; 230126; -.
DR   MGI; MGI:98294; Shb.
DR   eggNOG; roNOG12084; -.
DR   GeneTree; ENSGT00390000015203; -.
DR   HOGENOM; HBG716018; -.
DR   HOVERGEN; HBG066172; -.
DR   InParanoid; Q6PD21; -.
DR   OMA; DPLGGAC; -.
DR   OrthoDB; EOG45756M; -.
DR   ArrayExpress; Q6PD21; -.
DR   Bgee; Q6PD21; -.
DR   Genevestigator; Q6PD21; -.
DR   GermOnline; ENSMUSG00000044813; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001948; F:glycoprotein binding; IDA:MGI.
DR   GO; GO:0005070; F:SH3/SH2 adaptor activity; TAS:MGI.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0042100; P:B cell proliferation; IDA:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   InterPro; IPR000980; SH2.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   SMART; SM00252; SH2; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Angiogenesis; Apoptosis; Cell membrane;
KW   Cytoplasm; Developmental protein; Differentiation; Membrane;
KW   Phosphoprotein; SH2 domain.
FT   CHAIN         1    503       SH2 domain-containing adapter protein B.
FT                                /FTId=PRO_0000246325.
FT   DOMAIN      404    498       SH2.
FT   MOD_RES     113    113       Phosphotyrosine.
FT   MOD_RES     155    155       Phosphoserine.
FT   MOD_RES     240    240       Phosphotyrosine (By similarity).
FT   MOD_RES     262    262       Phosphotyrosine (By similarity).
FT   MOD_RES     304    304       Phosphoserine (By similarity).
FT   MOD_RES     308    308       Phosphoserine (By similarity).
FT   MOD_RES     311    311       Phosphoserine (By similarity).
FT   MOD_RES     330    330       Phosphotyrosine (By similarity).
FT   MOD_RES     382    382       Phosphoserine.
FT   VAR_SEQ       1    262       Missing (in isoform 2).
FT                                /FTId=VSP_019848.
FT   VAR_SEQ     443    479       KSNQGFMHMKLAKTKEKYVLGQNSPPFDSVPEVIHYY ->
FT                                NYADPEAVCAMPILPRTARPSVRPSVHPSVRKICARR (in
FT                                isoform 2).
FT                                /FTId=VSP_019849.
FT   VAR_SEQ     480    503       Missing (in isoform 2).
FT                                /FTId=VSP_019850.
SQ   SEQUENCE   503 AA;  54708 MW;  9A668DFC429F41E3 CRC64;
     MAKWLNKYFS LGNSKTKSPP QPPRPDYREQ RRRGERREQP PQAVPQACSA SSASCGSAAA
     CFSASSGSLP DDSGSTSDLI RAYRAQKERD FEDPYNGPGS SLRKLRAMCR LDYCGGGGGG
     DPGGGQRAFT AAAGAAGCCC AAAGAGAAAS SSSSSGSPHL YRSSSERRPT TPAEVRYISP
     KHRLIKVESA SAAGDPPGGV CSGGRTWSPT TCGGKKLLNK CSAEETGAGQ KDKVTIADDY
     SDPFDAKSDL KSKAGKGESA GYMEPYEAQR IMTEFQRQES VRSQHKGIQL YDTPYEPEGQ
     SVDSDSESTV SLRLRESKLP QDDDRPADEY DQPWEWNRVT IPALAAQFNG NEKRQSSPSP
     SRDRRRQLRA PGGGFKPIKH GSPEFCGILG ERVDPTIPLE KQIWYHGAIS RSDAENLLRL
     CKECSYLVRN SQTSKHDYSL SLKSNQGFMH MKLAKTKEKY VLGQNSPPFD SVPEVIHYYT
     TRKLPIKGAE HLSLLYPVAV RTL
//
ID   AN13D_MOUSE             Reviewed;         518 AA.
AC   Q6PD24;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Ankyrin repeat domain-containing protein 13D;
GN   Name=Ankrd13d;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 4 UIM (ubiquitin-interacting motif) repeats.
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DR   EMBL; BC058982; AAH58982.1; -; mRNA.
DR   IPI; IPI00396830; -.
DR   RefSeq; NP_080996.2; NM_026720.2.
DR   UniGene; Mm.23642; -.
DR   ProteinModelPortal; Q6PD24; -.
DR   SMR; Q6PD24; 440-517.
DR   PhosphoSite; Q6PD24; -.
DR   PRIDE; Q6PD24; -.
DR   Ensembl; ENSMUST00000056888; ENSMUSP00000053783; ENSMUSG00000005986.
DR   GeneID; 68423; -.
DR   KEGG; mmu:68423; -.
DR   UCSC; uc008fzs.1; mouse.
DR   CTD; 68423; -.
DR   MGI; MGI:1915673; Ankrd13d.
DR   eggNOG; roNOG11947; -.
DR   GeneTree; ENSGT00410000025381; -.
DR   HOGENOM; HBG444157; -.
DR   HOVERGEN; HBG059287; -.
DR   InParanoid; Q6PD24; -.
DR   OMA; PTVFEVP; -.
DR   OrthoDB; EOG4K0QN1; -.
DR   NextBio; 327150; -.
DR   ArrayExpress; Q6PD24; -.
DR   Bgee; Q6PD24; -.
DR   CleanEx; MM_ANKRD13D; -.
DR   Genevestigator; Q6PD24; -.
DR   GermOnline; ENSMUSG00000005986; Mus musculus.
DR   InterPro; IPR021832; DUF3424.
DR   InterPro; IPR003903; Ubiquitin-int_motif.
DR   Pfam; PF11904; DUF3424; 1.
DR   SMART; SM00726; UIM; 4.
DR   PROSITE; PS50330; UIM; 2.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1    518       Ankyrin repeat domain-containing protein
FT                                13D.
FT                                /FTId=PRO_0000240652.
FT   REPEAT      395    414       UIM 1.
FT   REPEAT      441    460       UIM 2.
FT   REPEAT      477    496       UIM 3.
FT   REPEAT      502    518       UIM 4.
FT   MOD_RES     465    465       Phosphoserine (By similarity).
FT   MOD_RES     469    469       Phosphothreonine (By similarity).
SQ   SEQUENCE   518 AA;  58405 MW;  181DFD88A5B098B8 CRC64;
     MVQLVLQYRD FQRATQRLAG IPELLNKLRQ APDFYVEMKW EFTSWVPLVS KMCPSDVYRV
     WKRGESLRVD TSLLGFEHMT WQRGRRSFIF RGQEAGALVM EVDHDRQVVH TETLAPALHE
     PEALLAAMRP SEEHVASRLT SPIVSTHLDT RNVAFERNKC GIWGWRSEKM ESVSGYEAKV
     YSATNVELVT RTRTEHLSDQ DKLRNKGGKT PFQSFLGMAQ QHSSHTLAPV QQAASPTNPT
     AISAEEYFDP SFSLESRNIG RPIEMSSKVQ RFKATLWLSE EHPLSLGDQV TPIIDLMAIS
     NAHFAKLRDF ITLRLPPGFP VKIEIPLFHV LNARITFSNL CGCDEPVSSV CVPNSSSAIS
     ASGSPFPCEV DPTVFEVPEG YSVLGAERSE PLRDEDDDLL QFAIQQSLLE AGTEAEQVTV
     WEALTNTRPG IHPPPRVTVF EEQLQLEQAL QESLQLSTES RGPESPQKTP PSPAPPSFEE
     QLRLALELSS REQEELERRG QQEEDDLQRI LQLSLTEH
//
ID   ZN513_MOUSE             Reviewed;         541 AA.
AC   Q6PD29; Q3U4K1; Q8BWH6;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 2.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Zinc finger protein 513;
GN   Name=Znf513; Synonyms=Zfp513;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6PD29-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PD29-2; Sequence=VSP_035626;
CC       Name=3;
CC         IsoId=Q6PD29-3; Sequence=VSP_035626, VSP_035627;
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family.
CC   -!- SIMILARITY: Contains 8 C2H2-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH58976.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK052459; BAC35001.1; -; mRNA.
DR   EMBL; AK154195; BAE32430.1; -; mRNA.
DR   EMBL; BC058976; AAH58976.1; ALT_INIT; mRNA.
DR   IPI; IPI00396769; -.
DR   IPI; IPI00830836; -.
DR   IPI; IPI00914683; -.
DR   RefSeq; NP_001171372.1; NM_001177901.1.
DR   RefSeq; NP_780520.3; NM_175311.4.
DR   UniGene; Mm.45033; -.
DR   HSSP; Q9NPA5; 1X5W.
DR   ProteinModelPortal; Q6PD29; -.
DR   SMR; Q6PD29; 117-495.
DR   Ensembl; ENSMUST00000114590; ENSMUSP00000110238; ENSMUSG00000043059.
DR   GeneID; 101023; -.
DR   KEGG; mmu:101023; -.
DR   UCSC; uc008wxo.1; mouse.
DR   CTD; 101023; -.
DR   MGI; MGI:2141255; Zfp513.
DR   eggNOG; roNOG14462; -.
DR   GeneTree; ENSGT00580000081649; -.
DR   HOGENOM; HBG713824; -.
DR   HOVERGEN; HBG097012; -.
DR   InParanoid; Q6PD29; -.
DR   OMA; GFERDSE; -.
DR   OrthoDB; EOG4CJVH5; -.
DR   NextBio; 354730; -.
DR   ArrayExpress; Q6PD29; -.
DR   Bgee; Q6PD29; -.
DR   Genevestigator; Q6PD29; -.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0010843; F:promoter binding; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0060041; P:retina development in camera-type eye; ISS:UniProtKB.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 8.
DR   SMART; SM00355; ZnF_C2H2; 8.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Metal-binding; Nucleus; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    541       Zinc finger protein 513.
FT                                /FTId=PRO_0000353093.
FT   ZN_FING     150    172       C2H2-type 1.
FT   ZN_FING     178    200       C2H2-type 2.
FT   ZN_FING     206    228       C2H2-type 3.
FT   ZN_FING     360    382       C2H2-type 4.
FT   ZN_FING     388    410       C2H2-type 5.
FT   ZN_FING     416    438       C2H2-type 6.
FT   ZN_FING     444    466       C2H2-type 7.
FT   ZN_FING     472    494       C2H2-type 8.
FT   COMPBIAS     55    141       Gly-rich.
FT   VAR_SEQ       1     18       MPRRKQSHPQPVKCEGVK -> MGTAWEGDSTSTLPSL
FT                                (in isoform 2 and isoform 3).
FT                                /FTId=VSP_035626.
FT   VAR_SEQ     112    382       Missing (in isoform 3).
FT                                /FTId=VSP_035627.
FT   CONFLICT    504    504       L -> R (in Ref. 1; BAC35001).
SQ   SEQUENCE   541 AA;  58067 MW;  4F284BE3EBCABB7F CRC64;
     MPRRKQSHPQ PVKCEGVKVD TEDSFDEGPG ALVLESDLLL GQDLEFEEEE EEDEGDGHND
     QLMGFERDSE GDSQGARPGL PYGLSDDESG GGRALSAESE VEEPARGPGE ARGERPGPAC
     QLCGGPTGEG PCCGAGGPGG GPPLPPRLLY SCRLCAFVSH YSSHLKRHMQ THSGEKPFRC
     GRCPYASAQL VNLTRHTRTH TGEKPYRCPH CPFACSSLGN LRRHQRTHTG PPTPPCPTCG
     FRCCAPRPTR PPSPTEQEGT MPRRSEDALI LPDLSLHVPP GGASFLPDCG QLRGEGESLC
     GTGSEPLPEL LFPWTCRGCG QELEEGEGSR LGAAMCGRCM RGEAGGVATG GPQGPGDKGF
     ACSLCPFATH YPNHLARHMK THSGEKPFRC ARCPYASAHL DNLKRHQRVH TGEKPYKCPL
     CPYACGNLAN LKRHGRIHSG DKPFRCSLCN YSCNQSMNLK RHMLRHTGEK PFRCATCAYT
     TGHWDNYKRH QKVHGHGGAG GPGLSAPEGW APPHSPPSVL STRGPAALGA TGSRALHSDS
     P
//
ID   TRAK1_MOUSE             Reviewed;         939 AA.
AC   Q6PD31; Q8BYA3;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Trafficking kinesin-binding protein 1;
GN   Name=Trak1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, TISSSUE SPECIFICITY, AND INTERACTION WITH GABRA1.
RX   PubMed=16380713; DOI=10.1038/ng1715;
RA   Gilbert S.L., Zhang L., Forster M.L., Anderson J.R., Iwase T.,
RA   Soliven B., Donahue L.R., Sweet H.O., Bronson R.T., Davisson M.T.,
RA   Wollmann R.L., Lahn B.T.;
RT   "Trak1 mutation disrupts GABA(A) receptor homeostasis in hypertonic
RT   mice.";
RL   Nat. Genet. 38:245-250(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Involved in the regulation of endosome-to-lysosome
CC       trafficking, including endocytic of EGF-EGFR complexes and GABA-A
CC       receptors (By similarity).
CC   -!- SUBUNIT: Interacts with O-GlcNAc transferase (By similarity).
CC       Interacts with RHOT1/Miro-1 and RHOT2/Miro-2 (By similarity).
CC       Interacts with HGS (By similarity). Interacts with GABRA1.
CC       Interacts with KIF5C (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Mitochondrion (By similarity). Early endosome (By
CC       similarity). Endosome (By similarity). Note=Predominantly
CC       associated with early endosome (By similarity). The localization
CC       to early endosomes depends on its interaction with HRS.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6PD31-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PD31-2; Sequence=VSP_039277, VSP_039278, VSP_039279;
CC   -!- TISSUE SPECIFICITY: Widely expressed with the greatest expression
CC       in brain, liver and kidney. Detected throughout the CNS, including
CC       the cortex, hippocamps, thalamus and various subcortical nuclei of
CC       the forebrain and midbrain, the granule of Purkinje layers of the
CC       cerebellum and the gray matter of the spinal cord. High level
CC       detected in lower moter neurons (at protein level).
CC   -!- PTM: O-glycosylated (By similarity).
CC   -!- DISEASE: A spontaneous mutation (hyrt mice) causes a recessively
CC       transmitted form of hypertonia neurological dysfunction
CC       characterized by postural abnormalities, jerky movements and
CC       tremormutant. Hyrt mice have much lower levels of GABA(A)
CC       receptors in the CNS, particularly the lower motor neurons, than
CC       do wild-type mice, indicating that the hypertonicity of the
CC       mutants is likely to be caused by deficits in GABA-mediated motor
CC       neuron inhibition.
CC   -!- SIMILARITY: Contains 1 HAP1 N-terminal domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK041436; BAC30946.1; -; mRNA.
DR   EMBL; BC058971; AAH58971.1; -; mRNA.
DR   EMBL; CH466587; EDL09157.1; -; Genomic_DNA.
DR   IPI; IPI00762231; -.
DR   IPI; IPI00968350; -.
DR   RefSeq; NP_780323.2; NM_175114.3.
DR   UniGene; Mm.480320; -.
DR   ProteinModelPortal; Q6PD31; -.
DR   SMR; Q6PD31; 320-350.
DR   STRING; Q6PD31; -.
DR   PhosphoSite; Q6PD31; -.
DR   PRIDE; Q6PD31; -.
DR   Ensembl; ENSMUST00000045903; ENSMUSP00000044482; ENSMUSG00000032536.
DR   GeneID; 67095; -.
DR   KEGG; mmu:67095; -.
DR   UCSC; uc009sdf.1; mouse.
DR   CTD; 67095; -.
DR   MGI; MGI:1914345; Trak1.
DR   HOVERGEN; HBG069248; -.
DR   InParanoid; Q6PD31; -.
DR   OMA; MALVFQF; -.
DR   OrthoDB; EOG4NGGM8; -.
DR   NextBio; 323558; -.
DR   ArrayExpress; Q6PD31; -.
DR   Bgee; Q6PD31; -.
DR   Genevestigator; Q6PD31; -.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0050811; F:GABA receptor binding; IDA:MGI.
DR   InterPro; IPR006933; HAP1_N.
DR   InterPro; IPR022154; Milton.
DR   Pfam; PF04849; HAP1_N; 1.
DR   Pfam; PF12448; Milton; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Endosome; Glycoprotein;
KW   Mitochondrion; Nucleus; Phosphoprotein.
FT   CHAIN         1    939       Trafficking kinesin-binding protein 1.
FT                                /FTId=PRO_0000394506.
FT   DOMAIN       46    353       HAP1 N-terminal.
FT   REGION      359    509       Interaction with HGS (By similarity).
FT   COILED      106    354       Potential.
FT   COILED      490    524       Potential.
FT   MOD_RES     199    199       Phosphoserine.
FT   VAR_SEQ       1     35       MALAIQLRQPSRAQPLPGLSHTLAGTDSCDVCNST -> ML
FT                                PATESTGMPAPSPTCATAP (in isoform 2).
FT                                /FTId=VSP_039277.
FT   VAR_SEQ     580    627       SATLHHWQQLAQPHLGGILDPRPGVVTKGFRTLDVDLDEVY
FT                                CLNDFEE -> DHQGLSVLLCDSLWALIHHRKASHQCHTYS
FT                                FFFRDSHPRCWFEFL (in isoform 2).
FT                                /FTId=VSP_039278.
FT   VAR_SEQ     628    939       Missing (in isoform 2).
FT                                /FTId=VSP_039279.
SQ   SEQUENCE   939 AA;  104467 MW;  64B1D5D34DF36FCB CRC64;
     MALAIQLRQP SRAQPLPGLS HTLAGTDSCD VCNSTNLPEV EIISLLEEQL PHYKLRADTI
     YGYDHDDWLH TPLISPDANI DLTTEQIEET LKYFLLCAER VGQMTKTYND IDAVTRLLEE
     KERDLELAAR IGQSLLKKNK TLTERNELLE EQVEHIREEV SQLRHELSMK DELLQFYTSA
     AEESEPESVC STPLKRNESS SSVQNYFHLD SLQKKLKDLE EENVVLRSEA CQLKTETITY
     EEKEQQLVND CVKELRDANV QIASISEELA KKTEDAARQQ EEITHLLSQI VDLQKKAKSC
     AVENEELVQH LGAAKDAQRQ LTAELRELED KYAECMEMLH EAQEELKNLR NKTMPTSRRY
     HSLGLFPMDS LAAEIEGTMR KELQLEELES PDITHQKRVF ETVRNVNQVV KQRSLTPSPM
     NIPGSNQSSA MNSLLSSCVS TPRSSFYGSD VSNVVLDNKT NSILLETEAA DLGNEDHNKK
     PGTPGTPGSH DLETALRRLS LRRENYLSER RFFEEEQERK LRELAEKGEL HSGSLTPTES
     IMSLGTHSRF SEFTGFSGMS FSSRSYLPEK LQIVKPLEGS ATLHHWQQLA QPHLGGILDP
     RPGVVTKGFR TLDVDLDEVY CLNDFEEDDT GDHISLAGLA TSTPIQHPET SAHHPGKCMS
     QTNSTFTFTT CRILHPSDEL TRVTPSLNSA PAPACSSTSH LKSTPVATPC TPRRLSLAES
     FTNVRESTTT MSTSLGLVWL LKERGISAAV YDPQSWDRAG RGSLLHSYTP RMAVIPSTPP
     NSPMQTPSAS PPSFEFKCTS PPYNNFLASK PASSILREVR EKRPVRSSES QTDVSVSNLN
     LVDKVRRFGV ARVVNSGRAR IPTLTEEQGP LLCGPTGPAQ ALVPGGLVPE GLPLGCPSGI
     RRNRSFPTMV GSSVQMRAPV ILTSGILMGA KLPKQTSLR
//
ID   RUN3B_MOUSE             Reviewed;         408 AA.
AC   Q6PDC0; Q6PFX5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   RecName: Full=RUN domain-containing protein 3B;
GN   Name=Rundc3b; Synonyms=Gm440;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBUNIT: Interacts with RAP2A (By similarity).
CC   -!- SIMILARITY: Belongs to the RUNDC3 family.
CC   -!- SIMILARITY: Contains 1 RUN domain.
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DR   EMBL; BC057375; AAH57375.1; -; mRNA.
DR   EMBL; BC058808; AAH58808.1; -; mRNA.
DR   IPI; IPI00396847; -.
DR   RefSeq; NP_941022.1; NM_198620.1.
DR   UniGene; Mm.332192; -.
DR   HSSP; Q9D394; 1WUS.
DR   ProteinModelPortal; Q6PDC0; -.
DR   SMR; Q6PDC0; 30-194.
DR   PRIDE; Q6PDC0; -.
DR   Ensembl; ENSMUST00000047485; ENSMUSP00000040108; ENSMUSG00000040570.
DR   GeneID; 242819; -.
DR   KEGG; mmu:242819; -.
DR   UCSC; uc008wkk.1; mouse.
DR   CTD; 242819; -.
DR   MGI; MGI:2685286; Rundc3b.
DR   eggNOG; roNOG16391; -.
DR   GeneTree; ENSGT00550000074558; -.
DR   HOVERGEN; HBG052747; -.
DR   OrthoDB; EOG4V9TQV; -.
DR   PhylomeDB; Q6PDC0; -.
DR   NextBio; 385575; -.
DR   ArrayExpress; Q6PDC0; -.
DR   Bgee; Q6PDC0; -.
DR   Genevestigator; Q6PDC0; -.
DR   InterPro; IPR004012; Run.
DR   Pfam; PF02759; RUN; 1.
DR   SMART; SM00593; RUN; 1.
DR   PROSITE; PS50826; RUN; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Phosphoprotein.
FT   CHAIN         1    408       RUN domain-containing protein 3B.
FT                                /FTId=PRO_0000336051.
FT   DOMAIN       58    190       RUN.
FT   COILED      301    326       Potential.
FT   COMPBIAS     14     21       Poly-Gly.
FT   MOD_RES     395    395       Phosphoserine (By similarity).
SQ   SEQUENCE   408 AA;  45138 MW;  035E82D9EACDCD8E CRC64;
     MASRSLGGLS GSRGGGGGGG GKKSLSARNA AVERRNLITV CRFSVKTLID RSCFETIDDS
     SPEFNNFAAV LEQILSHRLK GQVTWFGYES PRSFWDYIRV ACRKVSQNCI CSIENMENVS
     SSRAKGRAWI RVALMEKHLS EYISTALRDF KTTRRFYEDG AIVLGEEANM LAGMLLGLNA
     IDFSFCLKGE GLDGTFPAVI DYTPYLKFEQ SSDSISSDEE ELRTFGSSDS ESSTPENVGP
     PLILDENTWF NKCKRVRQKY QLTLEQKGYL EELLRLRENQ LSESVSQNKI LLQRIEDSDL
     AHKLEKEQLE YIIVELQDQL KSYQSLDQLS AEVSLSQASL DPSHSQEGDG KQDSLNFIGE
     GKEDTPSLLG LCGSLTSVAS YKSLTSLKSN DCLASPTTEL TSPGLTPS
//
ID   MON1A_MOUSE             Reviewed;         556 AA.
AC   Q6PDG8; Q80UP6; Q9CYS2;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 3.
DT   08-MAR-2011, entry version 44.
DE   RecName: Full=Vacuolar fusion protein MON1 homolog A;
GN   Name=Mon1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Embryonic brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, VARIANT SER-374, AND TISSUE SPECIFICITY.
RX   PubMed=17632513; DOI=10.1038/ng2059;
RA   Wang F., Paradkar P.N., Custodio A.O., McVey Ward D., Fleming M.D.,
RA   Campagna D., Roberts K.A., Boyartchuk V., Dietrich W.F., Kaplan J.,
RA   Andrews N.C.;
RT   "Genetic variation in Mon1a affects protein trafficking and modifies
RT   macrophage iron loading in mice.";
RL   Nat. Genet. 39:1025-1032(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; TYR-57; SER-69 AND
RP   SER-72, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 AND SER-91, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Plays an important in membrane trafficking through the
CC       secretory apparatus. Not involved in endocytic trafficking to
CC       lysosomes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6PDG8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PDG8-2; Sequence=VSP_024913, VSP_024914;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Widely expressed (at protein level).
CC   -!- POLYMORPHISM: The variant ser-374 is unique to C57BL strains. It
CC       may confer the low iron phenotype observed in these strains.
CC   -!- SIMILARITY: Belongs to the MON1/SAND family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK013387; BAB28823.1; -; mRNA.
DR   EMBL; AK172624; BAE43102.1; -; mRNA.
DR   EMBL; BC048852; AAH48852.1; -; mRNA.
DR   EMBL; BC058717; AAH58717.1; -; mRNA.
DR   IPI; IPI00457680; -.
DR   IPI; IPI00850149; -.
DR   RefSeq; NP_082645.1; NM_028369.3.
DR   UniGene; Mm.38037; -.
DR   PhosphoSite; Q6PDG8; -.
DR   PRIDE; Q6PDG8; -.
DR   Ensembl; ENSMUST00000035202; ENSMUSP00000035202; ENSMUSG00000032583.
DR   GeneID; 72825; -.
DR   KEGG; mmu:72825; -.
DR   UCSC; uc009rnh.1; mouse.
DR   CTD; 72825; -.
DR   MGI; MGI:1920075; Mon1a.
DR   eggNOG; roNOG13323; -.
DR   GeneTree; ENSGT00390000006665; -.
DR   HOGENOM; HBG447437; -.
DR   HOVERGEN; HBG064381; -.
DR   InParanoid; Q6PDG8; -.
DR   OrthoDB; EOG4CZBFS; -.
DR   NextBio; 336995; -.
DR   ArrayExpress; Q6PDG8; -.
DR   Bgee; Q6PDG8; -.
DR   CleanEx; MM_MON1A; -.
DR   Genevestigator; Q6PDG8; -.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IMP:MGI.
DR   GO; GO:0009306; P:protein secretion; IMP:MGI.
DR   InterPro; IPR004353; Vacuolar_fusion_protein_MON1.
DR   PANTHER; PTHR13027; DUF254_SAND; 1.
DR   Pfam; PF03164; Mon1; 1.
DR   PRINTS; PR01546; YEAST73DUF.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein; Polymorphism.
FT   CHAIN         1    556       Vacuolar fusion protein MON1 homolog A.
FT                                /FTId=PRO_0000285763.
FT   MOD_RES      31     31       Phosphoserine (By similarity).
FT   MOD_RES      56     56       Phosphoserine.
FT   MOD_RES      57     57       Phosphotyrosine.
FT   MOD_RES      69     69       Phosphoserine.
FT   MOD_RES      72     72       Phosphoserine.
FT   MOD_RES      79     79       Phosphoserine.
FT   MOD_RES      91     91       Phosphoserine.
FT   VAR_SEQ     461    461       S -> R (in isoform 2).
FT                                /FTId=VSP_024913.
FT   VAR_SEQ     462    556       Missing (in isoform 2).
FT                                /FTId=VSP_024914.
FT   VARIANT     374    374       N -> S (in strain: C57BL).
SQ   SEQUENCE   556 AA;  62131 MW;  78E1EA166530540F CRC64;
     MAADMQRKRS SECPEGTLAP SNGQSVERAE SPTPGLTQGT EPGAGQEGAM FVHTRSYEDL
     TELEDREASG DSPKECVGSP PPLATDMRQI SQDFSELSTQ LTGVARDLQE EMLPGSSEDW
     PEPQGAAGRG AATEPSQEGS TEGEEEDATE AWRLHQKHVF VLSEAGKPVY SRYGSEEALS
     STMGVMVALV SFLEADKNAI RSIHADGYKV VFVRRSPLVL VAVARTRQSA QELAQELLYI
     YYQILSLLTG AQLSHIFQQK QNYDLRRLLS GSERITDNLL QLMARDPSFL MGAARCLPLA
     AAVRDTVSAS LQQARARSLV FSILLAHNQL VALVRRKDQF LHPIDLHLLF NLISSSSSFR
     EGEAWTPVCL PKFNAAGFFH AHISYLEPDT DLCLLLISTD REDFFAVSDC RRRFQERLRK
     RGTHLALREA LRTPYYSVAQ VGIPDLRHFL YKSKSSGLFT SPEIEAPYSS EEEQERLLGL
     YQYLHSRAHN ASRPLKTIYY TGPNENLLAW VTGAFELYMC YSPLGTKASA VSAIHKLMRW
     IRKEEDRLFI LTPLTY
//
ID   PHLB1_MOUSE             Reviewed;        1371 AA.
AC   Q6PDH0; Q80TV2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Pleckstrin homology-like domain family B member 1;
DE   AltName: Full=Protein LL5-alpha;
GN   Name=Phldb1; Synonyms=Kiaa0638, Ll5a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 64-1371 (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   IDENTIFICATION OF THE GENE.
RX   PubMed=14532993;
RA   Katoh M., Katoh M.;
RT   "Identification and characterization of human LL5A gene and mouse Ll5a
RT   gene in silico.";
RL   Int. J. Oncol. 23:1477-1483(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-565, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6PDH0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PDH0-2; Sequence=VSP_016741, VSP_016742, VSP_016743;
CC   -!- DOMAIN: The PH domain mediates the binding to phosphoinositides
CC       (By similarity).
CC   -!- SIMILARITY: Contains 1 FHA domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC058712; AAH58712.1; -; mRNA.
DR   EMBL; AK122336; BAC65618.1; -; mRNA.
DR   IPI; IPI00330246; -.
DR   IPI; IPI00468120; -.
DR   RefSeq; NP_705765.3; NM_153537.3.
DR   UniGene; Mm.28639; -.
DR   ProteinModelPortal; Q6PDH0; -.
DR   SMR; Q6PDH0; 41-135, 1260-1360.
DR   STRING; Q6PDH0; -.
DR   PhosphoSite; Q6PDH0; -.
DR   PRIDE; Q6PDH0; -.
DR   Ensembl; ENSMUST00000034611; ENSMUSP00000034611; ENSMUSG00000048537.
DR   Ensembl; ENSMUST00000045838; ENSMUSP00000041534; ENSMUSG00000048537.
DR   GeneID; 102693; -.
DR   KEGG; mmu:102693; -.
DR   UCSC; uc009peg.1; mouse.
DR   UCSC; uc009peh.1; mouse.
DR   CTD; 102693; -.
DR   MGI; MGI:2143230; Phldb1.
DR   GeneTree; ENSGT00530000063148; -.
DR   HOVERGEN; HBG080571; -.
DR   OrthoDB; EOG4M0F15; -.
DR   NextBio; 355627; -.
DR   ArrayExpress; Q6PDH0; -.
DR   Bgee; Q6PDH0; -.
DR   Genevestigator; Q6PDH0; -.
DR   GermOnline; ENSMUSG00000048537; Mus musculus.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR008984; SMAD_FHA_domain.
DR   Gene3D; G3DSA:2.60.200.20; FHA; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF49879; SMAD_FHA; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; FALSE_NEG.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Phosphoprotein.
FT   CHAIN         1   1371       Pleckstrin homology-like domain family B
FT                                member 1.
FT                                /FTId=PRO_0000053892.
FT   DOMAIN       64    125       FHA.
FT   DOMAIN     1261   1364       PH.
FT   COILED      688    798       Potential.
FT   COILED     1150   1216       Potential.
FT   MOD_RES     220    220       Phosphoserine (By similarity).
FT   MOD_RES     223    223       Phosphoserine (By similarity).
FT   MOD_RES     325    325       Phosphoserine (By similarity).
FT   MOD_RES     431    431       Phosphoserine (By similarity).
FT   MOD_RES     445    445       Phosphoserine (By similarity).
FT   MOD_RES     503    503       Phosphoserine (By similarity).
FT   MOD_RES     518    518       Phosphothreonine (By similarity).
FT   MOD_RES     520    520       Phosphoserine.
FT   MOD_RES     522    522       Phosphoserine (By similarity).
FT   MOD_RES     541    541       Phosphoserine (By similarity).
FT   MOD_RES     553    553       Phosphoserine (By similarity).
FT   MOD_RES     557    557       Phosphoserine (By similarity).
FT   MOD_RES     565    565       Phosphoserine.
FT   MOD_RES     585    585       Phosphoserine (By similarity).
FT   VAR_SEQ     917    917       E -> EYVTLEQLRVVWGTPPMPPSPSPGLPSWASASQDLA
FT                                PITCLPPMLPSSFASITRSSK (in isoform 2).
FT                                /FTId=VSP_016741.
FT   VAR_SEQ    1174   1174       R -> RVRLTGARRQQV (in isoform 2).
FT                                /FTId=VSP_016742.
FT   VAR_SEQ    1325   1325       K -> KKRFFHFTMVTE (in isoform 2).
FT                                /FTId=VSP_016743.
FT   CONFLICT    402    402       R -> H (in Ref. 2; BAC65618).
SQ   SEQUENCE   1371 AA;  150070 MW;  E0E5204FF8C3C8C5 CRC64;
     MDPLNRSQLG PGCKTQAVVQ KGPLDLIETG QGLKVQTDKP HLVSLGSGRL STAITLLPLE
     EGRTVIGSAA RDISLQGPGL APEHCYIENL RGTLTLYPCG NACTIDGLPV RQPTRLTQGC
     MLCLGQSTFL RFNHPAEAKW MKSMIPAGVR APGPTYNPGS AESESLVNGN HTAQPATRAP
     SACASHSSLV SSIEKDLQEI MDSLVLEEPG AAGKKPAATS PLSPMANGGR YLLSPPTSPG
     AMSVGSSYEN TSPAFSPLSS PASSGSCASH SPSGQEPGPS VPPLVPARSS SYHLALQPPQ
     SRPSGSRSSD SPRLGRKGGH ERPPSPGLRG LLTDSPAATV LAEARRTTES PRLGGQLPVV
     AISLSEYPSS GARSQPASIP GSPKFQSPVP APRNKIGTLQ DRPPSPFREP PGTERVLTSS
     PSRQLVGRTF SDGLAATRTL QPPESPRLGR RGLDSMRELP PLSPSLSRRA LSPLPARTAP
     DPKLSREVAE SPRPRRWAAH GTSPEDFSLT LGARGRRTRS PSPTLGESLA PRKGSFSGRL
     SPAYSLGSLT GASPRQSPRA QRKLSSGDLR VPIPRERKNS ITEISDNEDE LLEYHRRQRQ
     ERLREQEMER LERQRLETIL NLCAEYSRAD GGPETGELPS IGEATAALAL AGRRPSRGLA
     GAIVVSGRCG EESGGASQRL WESMERSDEE NLKEECSSTE STQQEHEDAP GAKHQGEVLA
     VEEERAQVLG RVEQLKIRVK ELEQQLQEAA REAEMERALL QGEREAERAS LQKEQRAVDQ
     LQEKLVALET GIQKDRDKEA DALETETKLF EDLEFQQLER ESRVEEEREL AGQGLLRSKA
     ELLRSVSKRK ERLAVLDSQA GQIRAQAVQE SERLAREKNA ALQLLQKEKE KLNVLERRYH
     SLTGGRPFPK TTSTLKEMEK LLLPAVDLEQ WYQELMSGLG TGLAAASPRS SPPPLPAKAS
     RQLQVYRSKM DSDAASPLPR TRSGPLPSSS GSSSSSSQLS VATLGRSPSP KSALLAQNGT
     SSLPRNLAAT LQDIETKRQL ALQQKGHQVI EEQRRRLAEL KQKAAAEAQC QWDALHGAGP
     FSAGPSGFPA LMHHSILHHL PAGRERGEEG EHAYDTLSLE SSDSMETSIS TGGNSACSPD
     NMSSASGLDM GKIEEMEKML KEAHAEKSRL MESREREMEL RRQALEEERR RREQVERRLQ
     SESARRQQLV EKEVKLREKQ FSQARPLTRY LPNRKEDFDL KTHIESSGHG VDTCLHVVLS
     SKVCRGYLIK MGGKIKSWKK RWFVFDRLKR TLSYYVDKHE TKLKGVIYFQ AIEEVYYDHL
     RSAAKSPNPA LTFCVKTHDR LYYMVAPSAE AMRIWMDVIV TGAEGYTQFM N
//
ID   Q6PDH1_MOUSE            Unreviewed;      1216 AA.
AC   Q6PDH1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   SubName: Full=Phospholipase C, beta 1;
DE   SubName: Full=Plcb1 protein;
GN   Name=Plcb1; ORFNames=RP23-418D21.3-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Phillimore B.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RA   Tracey A.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RA   Griffiths C.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RA   Leongamornlert D.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 PI-PLC X-box domain.
CC   -!- SIMILARITY: Contains 1 PI-PLC Y-box domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC058710; AAH58710.1; -; mRNA.
DR   EMBL; AL928635; CAM23602.1; -; Genomic_DNA.
DR   EMBL; AL840635; CAM23602.1; JOINED; Genomic_DNA.
DR   EMBL; AL928956; CAM23602.1; JOINED; Genomic_DNA.
DR   EMBL; AL935278; CAM23602.1; JOINED; Genomic_DNA.
DR   EMBL; AL840635; CAM23766.1; -; Genomic_DNA.
DR   EMBL; AL928635; CAM23766.1; JOINED; Genomic_DNA.
DR   EMBL; AL928956; CAM23766.1; JOINED; Genomic_DNA.
DR   EMBL; AL935278; CAM23766.1; JOINED; Genomic_DNA.
DR   EMBL; AL928956; CAM26804.1; -; Genomic_DNA.
DR   EMBL; AL840635; CAM26804.1; JOINED; Genomic_DNA.
DR   EMBL; AL928635; CAM26804.1; JOINED; Genomic_DNA.
DR   EMBL; AL935278; CAM26804.1; JOINED; Genomic_DNA.
DR   EMBL; AL935278; CAM27130.1; -; Genomic_DNA.
DR   EMBL; AL840635; CAM27130.1; JOINED; Genomic_DNA.
DR   EMBL; AL928635; CAM27130.1; JOINED; Genomic_DNA.
DR   EMBL; AL928956; CAM27130.1; JOINED; Genomic_DNA.
DR   IPI; IPI00468121; -.
DR   RefSeq; NP_001139302.1; NM_001145830.1.
DR   RefSeq; NP_062651.2; NM_019677.2.
DR   UniGene; Mm.330607; -.
DR   ProteinModelPortal; Q6PDH1; -.
DR   SMR; Q6PDH1; 18-797, 900-1171.
DR   STRING; Q6PDH1; -.
DR   PRIDE; Q6PDH1; -.
DR   Ensembl; ENSMUST00000110116; ENSMUSP00000105743; ENSMUSG00000051177.
DR   GeneID; 18795; -.
DR   KEGG; mmu:18795; -.
DR   UCSC; uc008mny.1; mouse.
DR   CTD; 18795; -.
DR   MGI; MGI:97613; Plcb1.
DR   HOVERGEN; HBG053609; -.
DR   InParanoid; Q6PDH1; -.
DR   OMA; YEYNGKS; -.
DR   PhylomeDB; Q6PDH1; -.
DR   ArrayExpress; Q6PDH1; -.
DR   Bgee; Q6PDH1; -.
DR   Genevestigator; Q6PDH1; -.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR015359; Phospholipase_C_EF-hand-like.
DR   InterPro; IPR001711; Phospholipase_C_Pinositol-sp_Y.
DR   InterPro; IPR001192; Pinositol_Phospholipase-C.
DR   InterPro; IPR016280; PLC-beta.
DR   InterPro; IPR014815; PLC-beta_C.
DR   InterPro; IPR009535; PLC-beta_CS.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Gene3D; G3DSA:3.20.20.190; PLC-like_Pdiesterase_TIM-brl; 2.
DR   Pfam; PF06631; DUF1154; 1.
DR   Pfam; PF09279; efhand_like; 1.
DR   Pfam; PF00388; PI-PLC-X; 1.
DR   Pfam; PF00387; PI-PLC-Y; 1.
DR   Pfam; PF08703; PLC-beta_C; 1.
DR   PIRSF; PIRSF000956; PLC-beta; 1.
DR   PRINTS; PR00390; PHPHLIPASEC.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00148; PLCXc; 1.
DR   SMART; SM00149; PLCYc; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF51695; PLC-like_Pdiesterase_TIM-brl; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Transducer.
SQ   SEQUENCE   1216 AA;  138396 MW;  CC751D49895A47D0 CRC64;
     MAGAQPGVHA LQLKPVCVSD SLKKGTKFVK WDDDSTIVTP IILRTDPQGF FFYWTDQNKE
     TELLDLSLVK DARCGKHAKA PKDPKLRELL DVGNIGHLEQ RMITVVYGPD LVNISHLNLV
     AFQEEVAKEW TNEVFSLATN LLAQNMSRDA FLEKAYTKLK LQVTPEGRIP LKNIYRLFSA
     DRKRVETALE ACSLPSSRND SIPQEDFTPD VYRVFLNNLC PRPEIDNIFS EFGAKSKPYL
     TVDQMMDFIN LKQRDPRLNE ILYPPLKQEQ VQVLIEKYEP NSSLAKKGQM SVDGFMRYLS
     GEENGVVSPE KLDLNEDMSQ PLSHYFINSS HNTYLTAGQL AGNSSVEMYR QVLLSGCRCV
     ELDCWKGRTA EEEPVITHGF TMTTEISFKE VIEAIAECAF KTSPFPILLS FENHVDSPKQ
     QAKMAEYCRL IFGDALLMEP LEKYPLESGV PLPSPMDLMY KILVKNKKKS HKSSEGSGKK
     KLSEQASNTY SDSSSVFEPS SPGAGEADTE SDDDDDDDDC KKSSMDEGTA GSEAMATEEM
     SNLVNYIQPV KFESFEISKK RNKSFEMSSF VETKGLEQLT KSPVEFVEYN KMQLSRIYPK
     GTRVDSSNYM PQLFWNAGCQ MVALNFQTVD LAMQINMGMY EYNGKSGYRL KPEFMRRPDK
     HFDPFTEGIV DGIVANTLSV KIISGQFLSD KKVGTYVEVD MFGLPVDTRR KAFKTKTSQG
     NAVNPVWEEE PIVFKKVVLP SLACLRIAAY EEGGKFIGHR ILPVQAIRPG YHYICLRNER
     NQPLTLPAVF VYIEVKDYVP DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK
     EADPGETSSE APSETRTTPA ENGVNHTASL APKPPSQAPH SQPAPGSVKA PAKTEDLIQS
     VLTEVEAQTI EELKQQKSFV KLQKKHYKEM KDLVKRHHKK TTELIKEHTT KYNEIQNDYL
     RRRAALEKSA KKDSKKKSEP SSPDHGSSAI EQDLAALDAE MTQKLIDLKD KQQQQLLNLR
     QEQYYSEKYQ KREHIKLLIQ KLTDVAEECQ NNQLKKLKEI CEKEKKELKK KMDKKRQEKI
     TEAKSKDKSQ MEEEKTEMIR SYIQEVVQYI KRLEEAQSKR QEKLVEKHNE IRQQILDEKP
     KLQTELEQEY QDKFKRLPLE ILEFVQEAMK GKISEDSNHG SAPPSLASDA AKVNLKSPSS
     EEIERENPGR EFDTPL
//
ID   FA63B_MOUSE             Reviewed;         601 AA.
AC   Q6PDI6; Q571N1; Q6NSV8; Q7TML6; Q8BK25; Q8BL22; Q8BL47; Q8BZC1;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Protein FAM63B;
GN   Name=Fam63b; Synonyms=Kiaa1164;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-589 (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Adipose tissue, Cerebellum, and Corpora quadrigemina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, Czech II, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-590 (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6PDI6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PDI6-2; Sequence=VSP_034720;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q6PDI6-3; Sequence=VSP_034721, VSP_034722;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the FAM63 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH69845.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=BAC32709.1; Type=Frameshift; Positions=148;
CC       Sequence=BAD90344.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK035930; BAC29246.1; -; mRNA.
DR   EMBL; AK046403; BAC32709.1; ALT_FRAME; mRNA.
DR   EMBL; AK046623; BAC32810.1; -; mRNA.
DR   EMBL; AK077470; BAC36815.1; -; mRNA.
DR   EMBL; BC055816; AAH55816.1; -; mRNA.
DR   EMBL; BC058683; AAH58683.1; -; mRNA.
DR   EMBL; BC069845; AAH69845.1; ALT_SEQ; mRNA.
DR   EMBL; AK220158; BAD90344.1; ALT_INIT; mRNA.
DR   IPI; IPI00222705; -.
DR   IPI; IPI00420796; -.
DR   IPI; IPI00900427; -.
DR   RefSeq; NP_766360.2; NM_172772.2.
DR   UniGene; Mm.170855; -.
DR   ProteinModelPortal; Q6PDI6; -.
DR   PRIDE; Q6PDI6; -.
DR   Ensembl; ENSMUST00000049031; ENSMUSP00000037035; ENSMUSG00000042444.
DR   Ensembl; ENSMUST00000064901; ENSMUSP00000069104; ENSMUSG00000042444.
DR   GeneID; 235461; -.
DR   KEGG; mmu:235461; -.
DR   UCSC; uc009qon.1; mouse.
DR   CTD; 235461; -.
DR   MGI; MGI:2443086; Fam63b.
DR   eggNOG; roNOG09352; -.
DR   GeneTree; ENSGT00390000016607; -.
DR   HOVERGEN; HBG102840; -.
DR   InParanoid; Q6PDI6; -.
DR   OMA; STQAQQG; -.
DR   OrthoDB; EOG408N8C; -.
DR   PhylomeDB; Q6PDI6; -.
DR   NextBio; 382694; -.
DR   ArrayExpress; Q6PDI6; -.
DR   Bgee; Q6PDI6; -.
DR   Genevestigator; Q6PDI6; -.
DR   InterPro; IPR007518; DUF544.
DR   PANTHER; PTHR18063; DUF544; 1.
DR   Pfam; PF04424; DUF544; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    601       Protein FAM63B.
FT                                /FTId=PRO_0000344043.
FT   COMPBIAS    486    565       Gln-rich.
FT   MOD_RES      82     82       Phosphoserine (By similarity).
FT   MOD_RES     211    211       Phosphoserine.
FT   VAR_SEQ       1    263       Missing (in isoform 2).
FT                                /FTId=VSP_034720.
FT   VAR_SEQ     388    388       F -> R (in isoform 3).
FT                                /FTId=VSP_034721.
FT   VAR_SEQ     389    601       Missing (in isoform 3).
FT                                /FTId=VSP_034722.
FT   CONFLICT     78     78       G -> S (in Ref. 2; AAH55816).
FT   CONFLICT    107    107       A -> T (in Ref. 2; AAH55816).
FT   CONFLICT    261    261       L -> F (in Ref. 2; AAH69845 and 3;
FT                                BAD90344).
FT   CONFLICT    522    522       E -> G (in Ref. 1; BAC29246).
SQ   SEQUENCE   601 AA;  65637 MW;  D1094C08F6DFB10B CRC64;
     MENSPDSPQP LELGVAAGRV SPPEGRRRGG REAEDGPAGR AVDSGGQGAA AAAARSSLGD
     PTSPSQLGCG AGSDLKDGAS SSPAASEVPS RGQHKVTASP ELAEAAAGRG SGPVGDTGTC
     RVEQAAEEPS STGAPSSSCS EPSPPGDSPS LDSLESFSNL HSFPSSSEFN SEEGAETRVP
     EDVEEGAAGP PRAAPLCKEE EEDPAQVLAA SKERFPGQSV YHIKWIQWKE ENTPIITQNE
     NGPCPLLAIL NVLLLAWKVK LPPMMEIITA EQLMEYLGDY MLEAKPKEIS EIQRVNYEQN
     MSDAMAILHK LQTGLDVNVR FTGVRVFEYT PECIVFDLLD IPLYHGWLVD PQIDDIVKAV
     GNCSYNQLVE KIISCKQSDN SQLVSEGFVA EQFLNNTATQ LTYHGLCELT STVQEGELCV
     FFRNNHFSTM TKYKGQLYLL VTDQGFLTEE KIVWESLHNV DGDGNFCDSE FHLRPPSDPE
     TVYKGQQDQI DQDYLMALSL QQEQQSQEIN WEQIPEGISD LELAKKLQEE EDRRASQYYQ
     EQEQAQAVVT TTTPSTQAQQ GQPAQASPSS IKQPGNSERK RKEPREKDKE KEKEKNSCVI
     L
//
ID   MLL2_MOUSE              Reviewed;        5588 AA.
AC   Q6PDK2;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Histone-lysine N-methyltransferase MLL2;
DE            EC=2.1.1.43;
DE   AltName: Full=Lysine N-methyltransferase 2B;
DE            Short=KMT2B;
GN   Name=Mll2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4339-5588.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4789, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20808952; DOI=10.1371/journal.pbio.1000453;
RA   Andreu-Vieyra C.V., Chen R., Agno J.E., Glaser S., Anastassiadis K.,
RA   Stewart A.F., Matzuk M.M.;
RT   "MLL2 is required in oocytes for bulk histone 3 lysine 4
RT   trimethylation and transcriptional silencing.";
RL   PLoS Biol. 8:0-0(2010).
CC   -!- FUNCTION: Histone methyltransferase. Methylates 'Lys-4' of histone
CC       H3 (H3K4me). H3K4me represents a specific tag for epigenetic
CC       transcriptional activation. Plays a central role in beta-globin
CC       locus transcription regulation by being recruited by NFE2. Acts as
CC       a coactivator for estrogen receptor by being recruited by ESR1,
CC       thereby activating transcription (By similarity). Plays an
CC       important role in controlling bulk H3K4me during oocyte growth and
CC       preimplantation development. Required during the transcriptionally
CC       active period of oocyte growth for the establishment and/or
CC       maintenance of bulk H3K4 trimethylation (H3K4me3), global
CC       transcriptional silencing that preceeds resumption of meiosis,
CC       oocyte survival and normal zygotic genome activation.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC   -!- SUBUNIT: Component of the MLL2/MLL3 complex (also named ASCOM
CC       complex), at least composed of MLL2, MLL3, ASH2L, RBBP5, DPY30,
CC       NCOA6, WDR5, MEN1, KDM6A and PAXIP1/PTIP. Interacts with NFE2.
CC       Interacts with ESR1; interaction is direct (By similarity).
CC   -!- INTERACTION:
CC       Q9UBL3:ASH2L (xeno); NbExp=1; IntAct=EBI-996317, EBI-540797;
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- DOMAIN: LXXLL motifs 5 and 6 are essential for the association
CC       with ESR1 nuclear receptor (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Females are infertile due to anovulation and
CC       follicle loss. Oocytes show reduced H3K4me3 but not H3K4me1,
CC       abnormal expression of pro-apoptotic genes and Iap elements (which
CC       may contribute to oocyte death and, ultimately, follicle loss) and
CC       fail to establish transcriptional repression.
CC   -!- SIMILARITY: Belongs to the histone-lysine methyltransferase
CC       family. TRX/MLL subfamily.
CC   -!- SIMILARITY: Contains 1 FY-rich C-terminal domain.
CC   -!- SIMILARITY: Contains 1 FY-rich N-terminal domain.
CC   -!- SIMILARITY: Contains 5 PHD-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 post-SET domain.
CC   -!- SIMILARITY: Contains 4 RING-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 SET domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AC161165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC058659; AAH58659.1; -; mRNA.
DR   IPI; IPI00381244; -.
DR   RefSeq; NP_001028448.2; NM_001033276.2.
DR   UniGene; Mm.264889; -.
DR   IntAct; Q6PDK2; 1.
DR   PhosphoSite; Q6PDK2; -.
DR   Ensembl; ENSMUST00000023741; ENSMUSP00000023741; ENSMUSG00000048154.
DR   GeneID; 381022; -.
DR   KEGG; mmu:381022; -.
DR   UCSC; uc007xoc.1; mouse.
DR   MGI; MGI:2682319; Mll2.
DR   eggNOG; roNOG06941; -.
DR   GeneTree; ENSGT00580000081416; -.
DR   InParanoid; Q6PDK2; -.
DR   OrthoDB; EOG4T4CTJ; -.
DR   ArrayExpress; Q6PDK2; -.
DR   Bgee; Q6PDK2; -.
DR   Genevestigator; Q6PDK2; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006342; P:chromatin silencing; IMP:UniProtKB.
DR   GO; GO:0051568; P:histone H3-K4 methylation; IMP:UniProtKB.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0001555; P:oocyte growth; IMP:UniProtKB.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR003889; FYrich_C.
DR   InterPro; IPR018516; FYrich_C_sg.
DR   InterPro; IPR003888; FYrich_N.
DR   InterPro; IPR018518; FYrich_N_sg.
DR   InterPro; IPR000910; HMG_HMG1/HMG2.
DR   InterPro; IPR009071; HMG_superfamily.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Gene3D; G3DSA:1.10.30.10; HMG-box; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 5.
DR   Pfam; PF05965; FYRC; 1.
DR   Pfam; PF05964; FYRN; 1.
DR   Pfam; PF00628; PHD; 2.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00542; FYRC; 1.
DR   SMART; SM00541; FYRN; 1.
DR   SMART; SM00398; HMG; 1.
DR   SMART; SM00249; PHD; 7.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00184; RING; 6.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 5.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 5.
DR   PROSITE; PS50016; ZF_PHD_2; 4.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromatin regulator; Coiled coil; Metal-binding;
KW   Methyltransferase; Nucleus; Phosphoprotein; Repeat;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN         1   5588       Histone-lysine N-methyltransferase MLL2.
FT                                /FTId=PRO_0000401938.
FT   REPEAT      442    446       1.
FT   REPEAT      460    464       2.
FT   REPEAT      469    473       4.
FT   REPEAT      477    481       5.
FT   REPEAT      520    524       7.
FT   REPEAT      529    533       8.
FT   REPEAT      538    542       9.
FT   REPEAT      547    551       10.
FT   REPEAT      574    578       11.
FT   REPEAT      583    587       12.
FT   REPEAT      592    596       13.
FT   REPEAT      610    614       14.
FT   REPEAT      637    641       15.
FT   DOMAIN     4917   4969       FY-rich N-terminal.
FT   DOMAIN     4974   5060       FY-rich C-terminal.
FT   DOMAIN     5133   5254       SET.
FT   DOMAIN     5258   5274       Post-SET.
FT   ZN_FING     226    276       PHD-type 1; degenerate.
FT   ZN_FING     229    274       RING-type 1; atypical.
FT   ZN_FING     270    323       PHD-type 2.
FT   ZN_FING     276    321       RING-type 2; degenerate.
FT   ZN_FING    1071   1124       PHD-type 3.
FT   ZN_FING    1121   1171       PHD-type 4.
FT   ZN_FING    1198   1253       PHD-type 5.
FT   ZN_FING    1201   1251       RING-type 3; atypical.
FT   ZN_FING    4829   4874       RING-type 4; degenerate.
FT   REGION      439    642       15 X 5 AA repeats of S/P-P-P-E/P-E/A.
FT   REGION     5525   5526       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   COILED     2627   2665       Potential.
FT   COILED     2768   2813       Potential.
FT   COILED     3559   3613       Potential.
FT   COILED     3712   3747       Potential.
FT   COILED     3854   3883       Potential.
FT   COILED     3912   4052       Potential.
FT   MOTIF      2644   2648       LXXLL motif 1.
FT   MOTIF      3030   3034       LXXLL motif 2.
FT   MOTIF      4279   4293       LXXLL motif 3.
FT   MOTIF      4310   4314       LXXLL motif 4.
FT   MOTIF      4514   4518       LXXLL motif 5.
FT   MOTIF      5041   5045       LXXLL motif 6.
FT   COMPBIAS   1307   1311       Poly-Glu.
FT   COMPBIAS   2064   2583       Pro-rich.
FT   COMPBIAS   2610   2613       Poly-Ser.
FT   COMPBIAS   2769   2812       Gln-rich.
FT   COMPBIAS   2813   2819       Poly-Ala.
FT   COMPBIAS   3255   4332       Gln-rich.
FT   COMPBIAS   4841   4844       Poly-Ala.
FT   COMPBIAS   4960   5028       Pro-rich.
FT   METAL      5528   5528       Zinc (By similarity).
FT   METAL      5576   5576       Zinc (By similarity).
FT   METAL      5578   5578       Zinc (By similarity).
FT   METAL      5583   5583       Zinc (By similarity).
FT   BINDING    5502   5502       S-adenosyl-L-methionine (By similarity).
FT   MOD_RES    1627   1627       Phosphoserine (By similarity).
FT   MOD_RES    1822   1822       Phosphothreonine (By similarity).
FT   MOD_RES    2112   2112       Phosphoserine (By similarity).
FT   MOD_RES    2203   2203       N6-acetyllysine (By similarity).
FT   MOD_RES    2231   2231       Phosphoserine (By similarity).
FT   MOD_RES    2253   2253       Phosphoserine (By similarity).
FT   MOD_RES    2266   2266       Phosphoserine (By similarity).
FT   MOD_RES    2268   2268       Phosphoserine (By similarity).
FT   MOD_RES    2425   2425       N6-acetyllysine (By similarity).
FT   MOD_RES    3122   3122       Phosphoserine (By similarity).
FT   MOD_RES    3147   3147       N6-acetyllysine (By similarity).
FT   MOD_RES    3193   3193       Phosphoserine (By similarity).
FT   MOD_RES    3430   3430       N6-acetyllysine (By similarity).
FT   MOD_RES    4272   4272       Phosphoserine (By similarity).
FT   MOD_RES    4516   4516       N6-acetyllysine (By similarity).
FT   MOD_RES    4567   4567       N6-acetyllysine (By similarity).
FT   MOD_RES    4789   4789       Phosphoserine.
FT   MOD_RES    4827   4827       N6-acetyllysine (By similarity).
FT   MOD_RES    5327   5327       N6-acetyllysine (By similarity).
SQ   SEQUENCE   5588 AA;  600245 MW;  37A0E5D319A5F1A6 CRC64;
     MDSQKPPAED KDSDPAADGL AAPEKPGATE PDLPILCIGE VSVPGSGGSR PQKPPHDCSR
     GPARRCALCN CGEPGLHGQR ELQRFELPSD WPGFPVVPSG GNSGPCEAVL PKEDASQIGF
     PEGLTPAHLG EPGGHCWAHH WCAAWSAGVW GQEGPELCGV DKAIFSGISQ RCSHCARFGA
     SVPCRSPGCS RLYHFPCATA SGSFLSMKTL QLLCPEHSDG AAHLEEARCA VCEGPGQLCD
     LLFCTSCGHH YHGACLDTAL TARKRASWQC PECKVCQSCR KPGNDSKMLV CETCDKGYHT
     FCLKPPMEDL PAHSWKCKTC RLCRACGAGS AELNPNSEWF ENYSLCHRCH KAQGSQPVTS
     VAEQHPAVCS RLSPPEPGEI PIDAPDALYV ACQGQPKGGH VTSMQPKELA PLQCEAKPLG
     RAGTQLEAQL EAPLHEEMPL LPPPEESPLS PPPEESPTSP PPEASRLSPP TEESPLSPPP
     ESSPFSPLEG CPPSPALDTP LSPPPEASPL SPPFEESPLS PPPEELPSSP PPEASRLSPP
     PEESPMSPPP EESPMSPPPE ASRLFPPFEE SPLSPPPEDS PLSPPPEASR LSPPPEDSPM
     SPPPEDSPMS PPPEVSRFLP LPVLSHLSPL PEVSRLSPPP EESPLSPPPE DSPASPPPEA
     SRLSPPPEDS PASPPPEASR LSRPREDSPA SPPPEDSLVS LPMEESPLSP LPEELRLCPQ
     PEEPYLSPQP EEPRLCPQPE ELPLSPQSEE PCLSPVLVEP GPSSQPEEPH LSPVPQEPHL
     SPQPEEPHLS PQPQQLHLSP HSEEPCLSPM PEEPCLSPQP EELNGPPQPA EPPEEPSQSS
     APKELSLFSP SGEPPLPPML GEPALSEPGE PPLSPLPEEL PLSLSGEPVL SPQLMPPDPL
     PPPLSPIIPA AAPPALSPLG ELEYPFGAKG DSDPESPLAA PILETPISPP PEANCTDPEP
     VPPMILPPSP GSPLGPASPI LMERLPPPCS PLLPHSLPPP TPPPSHCSPP ALPLSVPSPL
     SPVQKAVDVS DEAELHEMET DKGPEPECPA LEPRATSPLP SPLGDLSCPA PSPAPALDDF
     SGLGEDTAPL DGTGQMSGSL AGELKGSPVL LDPEELTPVT PMEVYGPECK QAGQGSPCEE
     QEEPGAPMAP MPPTLIKSDI VNEISNLSQG DASASFPGSE PLLGSPDPEG GGSLSMELGV
     STDVSPARDE GSLRLCTDSL PETDDSLLCD TGTATSGGKA EGDKGRRRSS PARSRIKQGR
     SSSFPGRRRP RGGAAHGGRG RGRARLKSTT SSVETLVADI DSSPSKEEEE EDDDTMQNTV
     VLFSNTDKFV LMQDMCVVCG SFGRGAEGHL LACSQCSQCY HPYCVNSKIT KVMLLKGWRC
     VECIVCEVCG QASDPSRLLL CDDCDISYHT YCLDPPLLTV PKGGWKCKWC VSCMQCGAAS
     PGFHCEWQNS YTHCGPCASL VTCPVCHAPY VEEDLLIQCR HCERWMHAGC ESLFTEDEVE
     QAADEGFDCV SCQPYVVKPV VPVAPPELVP VKVKEPEPQF FRFEGVWLTE TGMAVLRNLT
     MSPLHKRRQR RGRLGLPGEA GLEGSEPSDA LGPDDKKDGD LDTDDLLKGE GGVEQMECEI
     KLEGPASPDV ELGKEETEES KKRKRKPYRP GIGGFMVRQR KSHTRVKRGP AAQAEVLSGD
     GQPDEVMPAD LPAEGSVEQS LAEGDEKKKQ QRRARKKSKL EDMFPAYLQA AFFGKDLLDL
     SRKALFAVGV GRPGFGLGAS KPRADGGSDR KELMTAMHKG DDGPDVADEE SHGPEGTADL
     PGLEDGGVKA SPVPSDPEKP GTPGEGVLSS DLDRIPTEEL PKMESKDLQQ LFKDVLGSER
     EQHLGCGTPG LEGGRTSLQR PFLQGGLALG SLPSSSPMDS YPGLCQSPFL DSRERGGFFS
     PEPGEPDSPW TGSGGTTPST PTTPTTEGEG DGLSYNQRSL QRWEKDEELG QLSTISPVLY
     ANINFPNLKQ DYPDWSSRCK QIMKLWRKVP AADKAPYLQK AKDNRAAHRI SKVQKQAESQ
     ISKQAKMGDI ARKTDRPALH LRIPSQPGAL GSPPPAAAPT IFLGSPTTPA GLSTSADGFL
     KPPAGTVPGP DSPGELFLKL PPQVPAQVPS QDPFGLAPAY APEPRFSAAP PTYPPYPSPT
     GAPAQPPMLG TTTRPGTGQP GEFHTTPPGT PRHQPSTPDP FLKPRCPSLD NLAVPESPGV
     AGGKASEPLL SPPPFGESRK SLEVKKEELG ASSPGYGPPN LGCVDSPSAG PHLGGLELKA
     PDVFKAPLTP RASQVEPQSP GLGLRAQEPP PAQALAPSPP SHPDVFRSGP YPDPYAQPPL
     TPRPQPPPPE SCCAPPPRSL PSDPFSRVPA SPQSQSSSQS PLTPRPLSAE AFCPSPVTPR
     FQSPDPYSRP PSRPQSRDPF APLHKPPRPQ PPEVAFKAGP LAHTPLGAGG FPAALPSGPA
     GELHAKVPSG QPTNFARSPG TGTFVGTPSP MRFTFPQGVG EPSLKPPVPQ PGLPSPHGIN
     SHFGPGPTLG KPQSTNYAVA TGNFHPSGSP LGPNSGPTGE GYGLSPLRPA SVLPPPAPDG
     SLPYLTHGAS QRVGITSPVE KREDPGATMS SSSLATPELS SAQDAGISSL SQTELEKQRQ
     RQRLRELLIR QQIQRNTLRQ EKETAAAAAG AVGPPGNWGA EPSSPAFEQL SRGQTPFTGS
     QDRSSIVGLP ASKLGGPTLG PGAFSSDDRL ARPLPPATPS SMDMNSRQLV GGSQAFYQRT
     PYPGSLPLQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQLWQ QQQQQQQQQQ QQAAAAAAAT
     SMRLAMSARF PSTPGPELGR QALGSPLAGI PTRLPGPAEP VPGPAGPAQF IELRHNVQKG
     LGPGVSPFPG QGPPQRPRFY PVSEELHRLA PEGLRGLAVP GLPSQKPSAL PAPELNNSLH
     QTPHAKGPAL ASGLELVSRP PSNTELSRPP LALEAGKLPC EDPELDDDFD AHKALEDDEE
     LAHLGLGVDV AKGDDELGTL ENLETNDPHL DDLLNGDEFD LLAYTDPELD TGDKKDIFNE
     HLRLVESANE KAEREALLRG VEPVSLGPEE RPPPAPDNSE PRLTSVLPEV KPKVEEGGRH
     PSPCQFTINT PKVEPAPPAT SLSLGLKPGQ TVMGTRDTRG GVGTGSFPSS GHTAEKGPFG
     ATGGTPAHLL NPSSLSGPAA SSLLEKFELE SGALTLPSGH AAAGDELDKM ESSLVASELP
     LLIEDLLEHE KKELQKKQQL SAQTVLPAQQ QQQQQQQQQQ QQQQHTLLPT PGPAQALPLP
     HEPGPPQQLA LGIGSTRQPG LGQSMVPIQP PAHALQQRLA PSVAMVSNQG HMLSGQQAGQ
     TGLVPQQSSQ PVLAQKPMSA MPASMCMKPQ QLAMQQQQLA NSFFPDTDLD KFAAEDIIDP
     IAKAKMVALK GIKKVMAQGS IGVAPGMNRQ QVSLLAQRLS GGSGSDLQNH VAPGSGQERN
     AGDPAQPRPN PPTFAQGVIN EADQRQYEEW LFHTQQLLQM QLKVLEEQIG VHRKSRKALC
     AKQRTAKKAG REFPEADAEK LKLVTEQQSK IQKQLDQVRK QQKEHTNLMA EYRNKQQQQQ
     QQQQQQQQQQ HSAVLAVSPS QNPRVLTKLP GQLLPAHGLQ PPQAPPGGQA GGLRLPPGGM
     VLPGQSGGPF LNTTLAQQQQ QQHSGVAGSL TGPPGSFFPG NLALRSLGPD SRLLQERQLQ
     LQQQRMQLAQ KLQQQQQQQQ QQQQQQHLLG QVAIQQQQGP GVQNQALGPK PQGLLPPSNH
     QGLLVQQLSP QQSQGSQGLL GPAQVTVLQQ QQQQQQHSGA LGPQGPHRQV LMTQSRVLSS
     PQLAQQGHSL MGHRLLTAQQ QQQQQQQQQQ QQQQQQQQQQ QQQGSMTGLS QLQQGMMSHG
     GQPKMSAQAL GSLQQQQQQL QQQQMLQQQQ LQQQQQQLQQ QQQQQQLQQQ QQQQLQLQQQ
     QQQQQQHLQH QQQQQQQLQQ QQQLQQQQQQ QLHLQQQLHQ QQQLQLQQQQ MGLLNQNRTL
     LSPQQQQQQQ QQQQQQQQQQ QQQQQQQQQV TLGPGLPVKP LQHFSSSGAL GPTLLLTGKE
     QNNAETALPS EVTEGPSTHQ GGPPAVGTAP EPMSVEPGEV KPSISGDSQL LLVQSQAQSQ
     ATSVQLQPPL RLPGQPQPQV NLLHTAGGGS HGQQLGSGSS SESPAVPHLL AQPSVSLGEQ
     PGPMAQNLLG SQQPLGLDRP IQNNTGSQPP KSGPAPQSGQ GPPGAGVMPT VGQLRAQLQG
     VLAKNPQLRH LSPQQQQQLQ ALLMQRQLQQ SQAVRQTPPF QEPGTQPSPL QGLLGCQPQP
     GGFSVSQTGP LQELGAGSRP QGPPRLPVPQ GALSTGPVLG PAHPTPPPSS PQEPKRPSQL
     PSPSAQLTPT HPGTPKPQGP ALELPPGRVS PAAAQLADTF FGKGLGPWDP SDNLTEAQKP
     EQSSLVPGHL DQVNGQVVHE PSQLSIKQEP REEPCALGAQ TVKREANGEP AGAPGTSNHL
     LLAGSRSEAG HLLLQKLLRA KNVQLGAGRG PEGLRAEING HIDSKLSGLE QKLQGTSSNK
     EDAATRKPLP AKPKRVQKTS DRLPSSRKKL RKEDGVRANE ALLKQLKQEL SQLPLTEPTI
     TANFSLFAPF GSGCLVSGQS QLRGAFGSGA LHTGPDYYSQ LLTKNNLSNP PTPPSSLPPT
     PPPSVQQKMV NGVTPSDELG ERPKDTASAQ DSEGALRDAA EVKSLDLLAA LPTPPHNQTE
     DVRMESDEDS DSPDSIVPAS SPESILGEEA PRFPQLGSGR WEQDNRALSP VIPIIPRTGI
     PVFPDTKPYG VLDLEVPGKL PATAWEKGKG SEVSVMLTVS AAAAKNLNGV MVAVAELLSM
     KIPNSYEVLF PDGPARAGLE PKKGEAEGPG GKEKGLSGKG PDTGPDWLKQ FDAVLPGYTL
     KSQLDILSLL KQESPAPEPS IQHSYTYNVS NLDVRQLSAP PPEEPSPPPS PLAPSPASPP
     AEPMVELQAE RPAEPPIPSP LPLASSPESA RPKPRARPPE ESEDSRPPRL KKWKGVRWKR
     LRLLLTIQKG SGHQEDEREV AEFMEQFGTA LRPSKVPRDN RRCCFCHEEG DGATDGPARL
     LNLDLDLWVH LNCALWSTEV YETQGGALMN VEVALHRGLL TKCSLCQRTG ATSSCNRMRC
     PNVYHFACAI RAKCMFFKDK TMLCPVHKIK GPCEQELSSF AVFRRVYIER DEVKQIASII
     QRGERLHMFR VGGLVFHAIG QLLPHQMADF HSATALYPVG YEATRIYWSL RTNNRRCCYR
     CSISENNGRP EFVIKVIEQG LEDLVFTDAS PQAVWNRIIE PVAAMRKEAD MLRLFPEYLK
     GEELFGLTVH AVLRIAESLP GVESCQNYLF RYGRHPLMEL PLMINPTGCA RSEPKILTHY
     KRPHTLNSTS MSKAYQSTFT GETNTPYSKQ FVHSKSSQYR RLRTEWKNNV YLARSRIQGL
     GLYAAKDLEK HTMVIEYIGT IIRNEVANRR EKIYEEQNRG IYMFRINNEH VIDATLTGGP
     ARYINHSCAP NCVAEVVTFD KEDKIIIISS RRIPKGEELT YDYQFDFEDD QHKIPCHCGA
     WNCRKWMN
//
ID   DC1L2_MOUSE             Reviewed;         492 AA.
AC   Q6PDL0;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Cytoplasmic dynein 1 light intermediate chain 2;
DE   AltName: Full=Dynein light intermediate chain 2, cytosolic;
GN   Name=Dync1li2; Synonyms=Dncli2, Dnclic2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Acts as one of several non-catalytic accessory
CC       components of the cytoplasmic dynein 1 complex that are thought to
CC       be involved in linking dynein to cargos and to adapter proteins
CC       that regulate dynein function. Cytoplasmic dynein 1 acts as a
CC       motor for the intracellular retrograde motility of vesicles and
CC       organelles along microtubules. May play a role in binding dynein
CC       to membranous organelles or chromosomes (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity). The cytoplasmic dynein 1
CC       complex consists of two catalytic heavy chains (HCs) and a number
CC       of non-catalytic subunits presented by intermediate chains (ICs),
CC       light intermediate chains (LICs) and light chains (LCs); the
CC       composition seems to vary in respect to the IC, LIC and LC
CC       composition. The heavy chain homodimer serves as a scaffold for
CC       the probable homodimeric assembly of the respective non-catalytic
CC       subunits. The ICs and LICs bind directly to the HC dimer and the
CC       LCs assemble on the IC dimer. Self-associates. Interacts with
CC       DYNC1H1; DYNC1LI1 and DYNC1LI2 bind mutually exclusive to DYNC1H1
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC   -!- SIMILARITY: Belongs to the dynein light intermediate chain family.
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DR   EMBL; BC058645; AAH58645.1; -; mRNA.
DR   IPI; IPI00420806; -.
DR   UniGene; Mm.289583; -.
DR   ProteinModelPortal; Q6PDL0; -.
DR   SMR; Q6PDL0; 55-87, 224-291.
DR   PhosphoSite; Q6PDL0; -.
DR   PRIDE; Q6PDL0; -.
DR   Ensembl; ENSMUST00000041769; ENSMUSP00000045480; ENSMUSG00000035770.
DR   UCSC; uc009nao.1; mouse.
DR   MGI; MGI:107738; Dync1li2.
DR   GeneTree; ENSGT00390000008295; -.
DR   HOGENOM; HBG314876; -.
DR   HOVERGEN; HBG005546; -.
DR   InParanoid; Q6PDL0; -.
DR   OrthoDB; EOG4PNXGQ; -.
DR   NextBio; 382249; -.
DR   ArrayExpress; Q6PDL0; -.
DR   Bgee; Q6PDL0; -.
DR   CleanEx; MM_DYNC1LI2; -.
DR   Genevestigator; Q6PDL0; -.
DR   GermOnline; ENSMUSG00000035770; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:motor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008467; Dynein1_light_intermed_chain.
DR   InterPro; IPR022780; Dynein_light_int_chain.
DR   PANTHER; PTHR12688; DLIC; 1.
DR   Pfam; PF05783; DLIC; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Dynein; Microtubule;
KW   Motor protein; Nucleotide-binding; Phosphoprotein; Transport.
FT   CHAIN         1    492       Cytoplasmic dynein 1 light intermediate
FT                                chain 2.
FT                                /FTId=PRO_0000114672.
FT   NP_BIND      61     68       ATP (Potential).
FT   MOD_RES     194    194       Phosphoserine.
FT   MOD_RES     383    383       Phosphoserine (By similarity).
FT   MOD_RES     391    391       Phosphoserine (By similarity).
FT   MOD_RES     407    407       Phosphoserine (By similarity).
FT   MOD_RES     441    441       Phosphothreonine (By similarity).
FT   MOD_RES     443    443       Phosphoserine (By similarity).
FT   MOD_RES     446    446       Phosphoserine (By similarity).
FT   MOD_RES     487    487       Phosphoserine (By similarity).
SQ   SEQUENCE   492 AA;  54218 MW;  6412DFD3497AA15E CRC64;
     MAPVGVEKKL LLGPNGPAVA AAGDLTSEEE EGQSLWSSIL SEVSTRARSK LPSGKNILVF
     GEDGSGKTTL MTKLQGAEHG KKGRGLEYLY LSVHDEDRDD HTRCNVWILD GDLYHKGLLK
     FAVSAESLRE TLVIFVADMS RPWTIMESLQ KWASVLREHI DKMKIPPEEM RDLERKFMKE
     FQDYIEPEEG CQGSPQRRGP LTSGSDEDSV ALPLGDNVLT HNLGIPVLVV CTKCDAMSVL
     EKEHDYRDEH LDFIQAHLRR FCLQYGAALI YTSVKEEKNL DLLYKYIVHK TYGFHFTIPA
     LVVEKDAVFI PAGWDNEKKI AILHENFTTV KPEDAYEDFI VKPPVRKLVH DKKLAAEDEQ
     VFLMKQQSLL AKQPATPTRT SESPARGPSG SPRTQGRGGP ASVPSASPGT SVKKPDPNIK
     NNAASEGVLA SFFNSLLSKK TGSPGSPSAG GVQSTAKKSG QKTVLSNVQE ELDRMTRKPD
     SMVTNSSTEN EA
//
ID   SRSF1_MOUSE             Reviewed;         248 AA.
AC   Q6PDM2; B2KGJ5; Q3UCH2; Q5SXC5; Q8BJV3; Q8C1H9;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-FEB-2011, entry version 86.
DE   RecName: Full=Serine/arginine-rich splicing factor 1;
DE   AltName: Full=ASF/SF2;
DE   AltName: Full=Splicing factor, arginine/serine-rich 1;
GN   Name=Srsf1; Synonyms=Sfrs1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow macrophage, Eye, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Embryonic brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 18-28.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [5]
RP   FUNCTION.
RX   PubMed=15652482; DOI=10.1016/j.cell.2004.11.036;
RA   Xu X., Yang D., Ding J.-H., Wang W., Chu P.-H., Dalton N.D.,
RA   Wang H.-Y., Bermingham J.R. Jr., Ye Z., Liu F., Rosenfeld M.G.,
RA   Manley J.L., Ross J. Jr., Chen J., Xiao R.-P., Cheng H., Fu X.-D.;
RT   "ASF/SF2-regulated CaMKIIdelta alternative splicing temporally
RT   reprograms excitation-contraction coupling in cardiac muscle.";
RL   Cell 120:59-72(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-238, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-201, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [8]
RP   STRUCTURE BY NMR OF 113-207.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of RRM domain in splicing factor 2.";
RL   Submitted (NOV-2005) to the PDB data bank.
CC   -!- FUNCTION: Plays a role in preventing exon skipping, ensuring the
CC       accuracy of splicing and regulating alternative splicing.
CC       Interacts with other spliceosomal components, via the RS domains,
CC       to form a bridge between the 5'- and 3'-splice site binding
CC       components, U1 snRNP and U2AF. Can stimulate binding of U1 snRNP
CC       to a 5'-splice site-containing pre-mRNA. Binds to purine-rich RNA
CC       sequences, either the octamer, 5'-RGAAGAAC-3' (r=A or G) or the
CC       decamers, AGGACAGAGC/AGGACGAAGC. Three copies of the octamer
CC       constitute a powerful splicing enhancer in vitro, the ASF/SF2
CC       splicing enhancer (ASE) which can specifically activate ASE-
CC       dependent splicing (By similarity). Specifically regulates
CC       alternative splicing of cardiac isoforms of CAMK2D, LDB3/CYPHER
CC       and TNNT2/CTNT during heart remodeling at the juvenile to adult
CC       transition. The inappropriate accumulation of a neonatal and
CC       neuronal isoform of CAMKD2 in the adult heart results in aberrant
CC       calcium handling and defective excitation-contraction coupling in
CC       cardiomyocytes.
CC   -!- SUBUNIT: Consists of two polypeptides of p32 and p33. In vitro,
CC       self-associates and binds SRSF2, SNRNP70 and U2AF1 but not U2AF2.
CC       Binds SREK1/SFRS12. Interacts with SAFB/SAFB1. Interacts with
CC       SRPK1. Interacts with PSIP1/LEDGF. Identified in the spliceosome C
CC       complex, at least composed of AQR, ASCC3L1, C19orf29, CDC40,
CC       CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38,
CC       DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC,
CC       HNRPF, HNRPH1, HNRPK, HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604,
CC       LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3,
CC       PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX,
CC       SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SRSF1/SFRS1,
CC       SKIV2L2, SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE,
CC       SNRPF, SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4,
CC       U2AF1, WDR57, XAB2 and ZCCHC8. Interacts with RSRC1 (via Arg/Ser-
CC       rich domain). Interacts with ZRSR2/U2AF1-RS2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Nucleus speckle (By similarity). Note=Shuttles
CC       between the nucleus and the cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6PDM2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PDM2-2; Sequence=VSP_013770, VSP_013773;
CC         Note=May be due to intron retention;
CC       Name=3;
CC         IsoId=Q6PDM2-3; Sequence=VSP_013771, VSP_013772;
CC         Note=No experimental confirmation. Gene prediction based on EST
CC         data. May be produced at very low levels due to a premature stop
CC         codon in the mRNA, leading to nonsense-mediated mRNA decay;
CC   -!- DOMAIN: Both the RS domain and an RRM domain are required for
CC       nucleocytoplasmic shuttling (By similarity).
CC   -!- PTM: Extensively phosphorylated on serine residues in the RS
CC       domain. This may regulate nucleocytoplasmic shuttling (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the splicing factor SR family.
CC   -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
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DR   EMBL; AK018176; BAC25546.1; -; mRNA.
DR   EMBL; AK078715; BAC37367.1; -; mRNA.
DR   EMBL; AK150535; BAE29641.1; -; mRNA.
DR   EMBL; AL593853; CAI24416.1; -; Genomic_DNA.
DR   EMBL; CU406964; CAQ51705.1; -; Genomic_DNA.
DR   EMBL; BC046773; AAH46773.1; -; mRNA.
DR   EMBL; BC058627; AAH58627.1; -; mRNA.
DR   IPI; IPI00420807; -.
DR   IPI; IPI00457656; -.
DR   IPI; IPI00515505; -.
DR   PIR; S26404; S26404.
DR   RefSeq; NP_001071635.1; NM_001078167.1.
DR   RefSeq; NP_775550.2; NM_173374.3.
DR   UniGene; Mm.391719; -.
DR   UniGene; Mm.478968; -.
DR   PDB; 1X4C; NMR; -; A=113-207.
DR   PDBsum; 1X4C; -.
DR   ProteinModelPortal; Q6PDM2; -.
DR   SMR; Q6PDM2; 6-102, 107-197.
DR   DIP; DIP-48723N; -.
DR   STRING; Q6PDM2; -.
DR   PhosphoSite; Q6PDM2; -.
DR   PRIDE; Q6PDM2; -.
DR   Ensembl; ENSMUST00000107920; ENSMUSP00000103553; ENSMUSG00000090049.
DR   GeneID; 110809; -.
DR   KEGG; mmu:110809; -.
DR   UCSC; uc007kvc.1; mouse.
DR   UCSC; uc007kvd.1; mouse.
DR   CTD; 110809; -.
DR   MGI; MGI:98283; Srsf1.
DR   eggNOG; roNOG04175; -.
DR   GeneTree; ENSGT00560000076885; -.
DR   HOGENOM; HBG756718; -.
DR   HOVERGEN; HBG002295; -.
DR   InParanoid; Q6PDM2; -.
DR   OMA; RSHEVCA; -.
DR   PhylomeDB; Q6PDM2; -.
DR   NextBio; 461971; -.
DR   ArrayExpress; Q6PDM2; -.
DR   Bgee; Q6PDM2; -.
DR   CleanEx; MM_SFRS1; -.
DR   Genevestigator; Q6PDM2; -.
DR   GermOnline; ENSMUSG00000018379; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0050733; F:RS domain binding; IPI:MGI.
DR   GO; GO:0060048; P:cardiac muscle contraction; IGI:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IDA:MGI.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW   Direct protein sequencing; Methylation; mRNA processing;
KW   mRNA splicing; Nucleus; Phosphoprotein; Repeat; RNA-binding;
KW   Spliceosome.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    248       Serine/arginine-rich splicing factor 1.
FT                                /FTId=PRO_0000081912.
FT   DOMAIN       16     91       RRM 1.
FT   DOMAIN      121    195       RRM 2.
FT   REGION      198    247       Interacts with SAFB1 (By similarity).
FT   COMPBIAS     94    113       Gly-rich (hinge region).
FT   COMPBIAS    198    247       Arg/Ser-rich (RS domain).
FT   MOD_RES       2      2       N-acetylserine (Potential).
FT   MOD_RES       2      2       Phosphoserine (By similarity).
FT   MOD_RES      38     38       N6-acetyllysine (By similarity).
FT   MOD_RES      93     93       Omega-N-methylated arginine (By
FT                                similarity).
FT   MOD_RES      97     97       Omega-N-methylated arginine (By
FT                                similarity).
FT   MOD_RES     109    109       Omega-N-methylated arginine (By
FT                                similarity).
FT   MOD_RES     179    179       N6-acetyllysine (By similarity).
FT   MOD_RES     189    189       Phosphotyrosine (By similarity).
FT   MOD_RES     199    199       Phosphoserine.
FT   MOD_RES     201    201       Phosphoserine.
FT   MOD_RES     202    202       Phosphotyrosine (By similarity).
FT   MOD_RES     205    205       Phosphoserine (By similarity).
FT   MOD_RES     231    231       Phosphoserine.
FT   MOD_RES     234    234       Phosphoserine (By similarity).
FT   MOD_RES     237    237       Phosphotyrosine (By similarity).
FT   MOD_RES     238    238       Phosphoserine.
FT   VAR_SEQ     185    203       GETAYIRVKVDGPRSPSYG -> VGYTLILFFGQNWIQFS
FT                                (in isoform 2).
FT                                /FTId=VSP_013770.
FT   VAR_SEQ     185    199       GETAYIRVKVDGPRS -> TYLKRWIKNALD (in
FT                                isoform 3).
FT                                /FTId=VSP_013771.
FT   VAR_SEQ     200    248       Missing (in isoform 3).
FT                                /FTId=VSP_013772.
FT   VAR_SEQ     204    248       Missing (in isoform 2).
FT                                /FTId=VSP_013773.
FT   CONFLICT    119    119       S -> A (in Ref. 1; BAC25546).
FT   CONFLICT    162    164       FVR -> CVP (in Ref. 1; BAC25546).
FT   CONFLICT    185    185       G -> W (in Ref. 1; BAC25546).
FT   CONFLICT    191    196       RVKVDG -> PRIVDR (in Ref. 1; BAC25546).
FT   CONFLICT    209    210       SR -> VC (in Ref. 1; BAC25546).
FT   CONFLICT    226    228       YSP -> DSR (in Ref. 1; BAC25546).
FT   STRAND      121    126
FT   HELIX       133    140
FT   HELIX       141    143
FT   STRAND      146    151
FT   STRAND      155    163
FT   HELIX       164    173
FT   STRAND      174    180
FT   STRAND      186    195
SQ   SEQUENCE   248 AA;  27745 MW;  C28A0B2F112EA713 CRC64;
     MSGGGVIRGP AGNNDCRIYV GNLPPDIRTK DIEDVFYKYG AIRDIDLKNR RGGPPFAFVE
     FEDPRDAEDA VYGRDGYDYD GYRLRVEFPR SGRGTGRGGG GGGGGGAPRG RYGPPSRRSE
     NRVVVSGLPP SGSWQDLKDH MREAGDVCYA DVYRDGTGVV EFVRKEDMTY AVRKLDNTKF
     RSHEGETAYI RVKVDGPRSP SYGRSRSRSR SRSRSRSRSN SRSRSYSPRR SRGSPRYSPR
     HSRSRSRT
//
ID   Q6PDM6_MOUSE            Unreviewed;      1166 AA.
AC   Q6PDM6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   SubName: Full=Mcf.2 transforming sequence-like;
GN   Name=Mcf2l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 584-929.
RX   PubMed=15274927; DOI=10.1016/j.str.2004.03.021;
RA   Worthylake D.K., Rossman K.L., Sondek J.;
RT   "Crystal structure of the DH/PH fragment of Dbs without bound
RT   GTPase.";
RL   Structure 12:1078-1086(2004).
CC   -!- INTERACTION:
CC       P61586:RHOA (xeno); NbExp=3; IntAct=EBI-602149, EBI-446668;
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
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DR   EMBL; BC058622; AAH58622.1; -; mRNA.
DR   IPI; IPI00466436; -.
DR   RefSeq; NP_001152957.1; NM_001159485.1.
DR   RefSeq; NP_001152958.1; NM_001159486.1.
DR   RefSeq; NP_835177.2; NM_178076.3.
DR   UniGene; Mm.334413; -.
DR   ProteinModelPortal; Q6PDM6; -.
DR   SMR; Q6PDM6; 585-926.
DR   IntAct; Q6PDM6; 3.
DR   STRING; Q6PDM6; -.
DR   Ensembl; ENSMUST00000033819; ENSMUSP00000033819; ENSMUSG00000031442.
DR   Ensembl; ENSMUST00000110876; ENSMUSP00000106500; ENSMUSG00000031442.
DR   GeneID; 17207; -.
DR   KEGG; mmu:17207; -.
DR   UCSC; uc009kwl.1; mouse.
DR   CTD; 17207; -.
DR   MGI; MGI:103263; Mcf2l.
DR   HOGENOM; HBG443572; -.
DR   HOVERGEN; HBG062385; -.
DR   InParanoid; Q6PDM6; -.
DR   OrthoDB; EOG4K0QMP; -.
DR   PhylomeDB; Q6PDM6; -.
DR   NextBio; 291594; -.
DR   ArrayExpress; Q6PDM6; -.
DR   Bgee; Q6PDM6; -.
DR   Genevestigator; Q6PDM6; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0005545; F:1-phosphatidylinositol binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IDA:MGI.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   GO; GO:0007266; P:Rho protein signal transduction; IDA:MGI.
DR   InterPro; IPR001251; CRAL-bd_TRIO_C.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:3.40.525.10; CRAL_bd_TRIO_C; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF00435; Spectrin; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00150; SPEC; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure.
SQ   SEQUENCE   1166 AA;  131131 MW;  D969135E4592F851 CRC64;
     MALEEMVQRL NAVSKNTDEI MHQDIVPLCA ADIQEQLKKR FAYLSGGRGQ DGSPVITFPD
     YPAFSEIPDK EFQNVMTYLT SIPSLQDAGI GFILVIDRRQ DKWTSVKASV LRIAASFPAN
     LQLVLVLRPT GFFQRTLSDI AFKFNRDEFK MKVPVMMLSS VPELHGYIDK SQLTEDLGGT
     LDYCHSRWLC HRTAIESFAL MVKQTAQMLQ AFGTELAETE LPNDVQSTSL VLSAHTEKKA
     KVKEDLQLAL KEGNSILESL REPLAESAAH SVNQDQLDNQ ATVQRLLAQL NETEAAFDEF
     WAKHQQKLEQ CLQLRHFEQG FREVKTTLDS MSQKIAAFTD VGNSLAHVQH LLKDLTAFEE
     KSSVAVDKAR ALSLEGQQLI ENRHYAVDSI HPKCEELQHL CDHFASEVTR RRGLLSKSLE
     LHSLLETSMK WSDEGIFLLA SQPVDKCQSQ DGAEAALQEI EKFLETGAEN KIQELNEIYK
     EYECILNQDL LEHVQKVFQK QESTEEMFHR RQASLKKLAA KQTRPVQPVA PRPEALTKSP
     SPSPGSWRSS ENSSSEGNAL RRGPYRRAKS EMSEPRQGRT SSTGEEEESL AILRRHVMNE
     LLDTERAYVE ELLCVLEGYA AEMDNPLMAH LISTGLQNKK NILFGNMEEI YHFHNRIFLR
     ELESCIDCPE LVGRCFLERM EEFQIYEKYC QNKPRSESLW RQCSDCPFFQ ECQKKLDHKL
     SLDSYLLKPV QRITKYQLLL KEMLKYSKHC EGAEDLQEAL SSILGILKAV NDSMHLIAIT
     GYDGNLGDLG KLLMQGSFSV WTDHKKGHTK VKELARFKPM QRHLFLHEKA VLFCKKREEN
     GEGYEKAPSY SYKQSLNMTA VGITENVKGD TKKFEIWYNA REEVYIIQAP TPEIKAAWVN
     EIRKVLTSQL QACREASQHR ALEQSHSLPL PTPSSTSPTK GNTRNVKKLE DRKTDPLSLE
     GYVSSSLPKP PEKGKDDAVP SSTSESSALS RKRFTLQGLA NLKGQKASPT SPDKKAKRHE
     VKSDPTPFGL RGWSKTSHSL EAPEEDGGWS SAEELINSSD AEEDGGVGPK KLVPGKYTVV
     MDDEKGGPDT LAMRSGDMVE VVEEGAEGLW YVRDLTSSKE GWVPASSLST LLGKSSSAQC
     LSSSGKIHCA RQLCPEPAEI LSPEPV
//
ID   CHD4_MOUSE              Reviewed;        1915 AA.
AC   Q6PDQ2;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Chromodomain-helicase-DNA-binding protein 4;
DE            Short=CHD-4;
DE            EC=3.6.4.12;
GN   Name=Chd4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   INTERACTION WITH IKFZ1 IN THE NURD COMPLEX.
RX   PubMed=11003653; DOI=10.1128/MCB.20.20.7572-7582.2000;
RA   O'Neill D.W., Schoetz S.S., Lopez R.A., Castle M., Rabinowitz L.,
RA   Shor E., Krawchuk D., Goll M.G., Renz M., Seelig H.P., Han S.,
RA   Seong R.H., Park S.D., Agalioti T., Munshi N., Thanos D.,
RA   Erdjument-Bromage H., Tempst P., Bank A.;
RT   "An ikaros-containing chromatin-remodeling complex in adult-type
RT   erythroid cells.";
RL   Mol. Cell. Biol. 20:7572-7582(2000).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1301, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   INTERACTION WITH CHD4, AND FUNCTION.
RX   PubMed=17938210; DOI=10.1128/MCB.00589-07;
RA   Siatecka M., Xue L., Bieker J.J.;
RT   "Sumoylation of EKLF promotes transcriptional repression and is
RT   involved in inhibition of megakaryopoiesis.";
RL   Mol. Cell. Biol. 27:8547-8560(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1533; THR-1538 AND
RP   THR-1542, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Probable transcription regulator (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Central component of the nucleosome remodeling and
CC       histone deacetylase (NuRD) repressor complex. Interacts with
CC       TRIM27. Interacts with ZGPAT; the interaction is direct. Part of a
CC       complex containing ATR and HDAC2 (By similarity). Interacts with
CC       KLF1; the interaction depends on sumoylation of KLF1, and leads to
CC       its transcriptional repression. Interacts directly with IKFZ1 in
CC       the NuRD complex.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC   -!- SIMILARITY: Contains 2 chromo domains.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SIMILARITY: Contains 2 PHD-type zinc fingers.
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DR   EMBL; BC058578; AAH58578.1; -; mRNA.
DR   IPI; IPI00396802; -.
DR   RefSeq; NP_666091.1; NM_145979.2.
DR   UniGene; Mm.333388; -.
DR   ProteinModelPortal; Q6PDQ2; -.
DR   SMR; Q6PDQ2; 361-1274.
DR   STRING; Q6PDQ2; -.
DR   PhosphoSite; Q6PDQ2; -.
DR   PRIDE; Q6PDQ2; -.
DR   Ensembl; ENSMUST00000056889; ENSMUSP00000060054; ENSMUSG00000063870.
DR   GeneID; 107932; -.
DR   KEGG; mmu:107932; -.
DR   UCSC; uc009dtk.1; mouse.
DR   CTD; 107932; -.
DR   MGI; MGI:1344380; Chd4.
DR   HOVERGEN; HBG005326; -.
DR   OrthoDB; EOG4WH8JX; -.
DR   PhylomeDB; Q6PDQ2; -.
DR   NextBio; 359735; -.
DR   PMAP-CutDB; Q6PDQ2; -.
DR   ArrayExpress; Q6PDQ2; -.
DR   Bgee; Q6PDQ2; -.
DR   CleanEx; MM_CHD4; -.
DR   Genevestigator; Q6PDQ2; -.
DR   GermOnline; ENSMUSG00000063870; Mus musculus.
DR   GO; GO:0000785; C:chromatin; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008134; F:transcription factor binding; IPI:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006333; P:chromatin assembly or disassembly; IEA:InterPro.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR012957; CHD_C2.
DR   InterPro; IPR012958; CHD_N.
DR   InterPro; IPR000953; Chromodomain.
DR   InterPro; IPR016197; Chromodomain-like.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR009462; DUF1086.
DR   InterPro; IPR009463; DUF1087.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 2.
DR   Pfam; PF08074; CHDCT2; 1.
DR   Pfam; PF08073; CHDNT; 1.
DR   Pfam; PF00385; Chromo; 2.
DR   Pfam; PF06461; DUF1086; 1.
DR   Pfam; PF06465; DUF1087; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00628; PHD; 2.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00249; PHD; 2.
DR   SMART; SM00184; RING; 2.
DR   SUPFAM; SSF54160; Chromodomain-like; 2.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 2.
DR   PROSITE; PS00598; CHROMO_1; 2.
DR   PROSITE; PS50013; CHROMO_2; 2.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 2.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Chromatin regulator; DNA-binding; Helicase;
KW   Hydrolase; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1   1915       Chromodomain-helicase-DNA-binding protein
FT                                4.
FT                                /FTId=PRO_0000080229.
FT   DOMAIN      522    579       Chromo 1.
FT   DOMAIN      615    676       Chromo 2.
FT   DOMAIN      731    915       Helicase ATP-binding.
FT   DOMAIN     1047   1196       Helicase C-terminal.
FT   ZN_FING     363    410       PHD-type 1.
FT   ZN_FING     442    489       PHD-type 2.
FT   NP_BIND     744    751       ATP (Potential).
FT   MOTIF       866    869       DEAH box.
FT   COMPBIAS     50    126       Lys-rich.
FT   COMPBIAS    471    532       Pro-rich.
FT   COMPBIAS   1560   1671       Glu-rich.
FT   MOD_RES      96     96       Phosphoserine (By similarity).
FT   MOD_RES     421    421       Phosphoserine.
FT   MOD_RES     508    508       Phosphoserine (By similarity).
FT   MOD_RES     510    510       Phosphothreonine (By similarity).
FT   MOD_RES     522    522       Phosphothreonine (By similarity).
FT   MOD_RES     524    524       Phosphoserine (By similarity).
FT   MOD_RES     980    980       N6-acetyllysine (By similarity).
FT   MOD_RES    1301   1301       Phosphoserine.
FT   MOD_RES    1342   1342       Phosphoserine (By similarity).
FT   MOD_RES    1363   1363       Phosphoserine (By similarity).
FT   MOD_RES    1524   1524       Phosphoserine (By similarity).
FT   MOD_RES    1528   1528       Phosphoserine (By similarity).
FT   MOD_RES    1530   1530       Phosphoserine (By similarity).
FT   MOD_RES    1533   1533       Phosphothreonine.
FT   MOD_RES    1535   1535       Phosphothreonine (By similarity).
FT   MOD_RES    1538   1538       Phosphothreonine.
FT   MOD_RES    1542   1542       Phosphothreonine.
FT   MOD_RES    1546   1546       Phosphothreonine (By similarity).
FT   MOD_RES    1563   1563       Phosphoserine (By similarity).
FT   MOD_RES    1569   1569       Phosphoserine (By similarity).
FT   MOD_RES    1646   1646       N6-acetyllysine (By similarity).
SQ   SEQUENCE   1915 AA;  217751 MW;  CFCB83B419AE6B5A CRC64;
     MASGLGSPSP CSAGSEEEDM DALLNNSLPP PHPENEEDPD EDLSEAETPK LKKKKKPKKP
     RDPKIPKSKR QKKELGDSSG EGPEFVEEEE EVALRSDSEG SDYTPGKKKK KKLGPKKEKK
     SKSKRKEEEE EEDEDDDSKE PKSSAQLLED WGMEDIDHVF SEEDYRTLTN YKAFSQFVRP
     LIAAKNPKIA VSKMMMVLGA KWREFSTNNP FKGSSGASVA AAAAAAVAVV ESMVTATEVA
     PPPPPVEVPI RKAKTKEGKG PNARRKPKGS PRVPDAKKPK PKKVAPLKIK LGGFGSKRKR
     SSSEDDDLDV ESDFDDASIN SYSVSDGSTS RSSRSRKKLR TAKKKKKGEE EVTAVDGYET
     DHQDYCEVCQ QGGEIILCDT CPRAYHMVCL DPDMEKAPEG KWSCPHCEKE GIQWEAKEDN
     SEGEEILEEV GGDPEEEDDH HMEFCRVCKD GGELLCCDTC PSSYHIHCLN PPLPEIPNGE
     WLCPRCTCPA LKGKVQKILI WKWGQPPSPT PVPRPPDADP NTPSPKPLEG RPERQFFVKW
     QGMSYWHCSW VSELQLELHC QVMFRNYQRK NDMDEPPSGD FGGDEEKSRK RKNKDPKFAE
     MEERFYRYGI KPEWMMIHRI LNHSVDKKGH VHYLIKWRDL PYDQASWESE DVEIQDYDLF
     KQSYWNHREL MRGEEGRPGK KLKKVKLRKL ERPPETPTVD PTVKYERQPE YLDATGGTLH
     PYQMEGLNWL RFSWAQGTDT ILADEMGLGK TVQTAVFLYS LYKEGHSKGP FLVSAPLSTI
     INWEREFEMW APDMYVVTYV GDKDSRAIIR ENEFSFEDNA IRGGKKASRM KKEASVKFHV
     LLTSYELITI DMAILGSIDW ACLIVDEAHR LKNNQSKFFR VLNGYSLQHK LLLTGTPLQN
     NLEELFHLLN FLTPERFHNL EGFLEEFADI AKEDQIKKLH DMLGPHMLRR LKADVFKNMP
     SKTELIVRVE LSPMQKKYYK YILTRNFEAL NARGGGNQVS LLNVVMDLKK CCNHPYLFPV
     AAMEAPKMPN GMYDGSALIR ASGKLLLLQK MLKNLKEGGH RVLIFSQMTK MLDLLEDFLE
     HEGYKYERID GGITGNMRQE AIDRFNAPGA QQFCFLLSTR AGGLGINLAT ADTVIIYDSD
     WNPHNDIQAF SRAHRIGQNK KVMIYRFVTR ASVEERITQV AKKKMMLTHL VVRPGLGSKT
     GSMSKQELDD ILKFGTEELF KDEATDGGGD NKEGEDSSVI HYDDKAIERL LDRNQDETED
     TELQGMNEYL SSFKVAQYVV REEEMGEEEE VEREIIKQEE SVDPDYWEKL LRHHYEQQQE
     DLARNLGKGK RIRKQVNYND GSQEDRDWQD DQSDNQSDYS VASEEGDEDF DERSEAPRRP
     SRKGLRNDKD KPLPPLLARV GGNIEVLGFN ARQRKAFLNA IMRYGMPPQD AFTTQWLVRD
     LRGKSEKEFK AYVSLFMRHL CEPGADGAET FADGVPREGL SRQHVLTRIG VMSLIRKKVQ
     EFEHVNGRWS MPELAEVEEN KKMSQPGSPS PKTPTPSTPG DTQPNTPAPV PPAEDGIKIE
     ENSLKEEEST EGEKEVKSTA PEATVECAQP PAPAPATAPA TATAPEDDKA PAEPPEGEEK
     VEKAEVKERT EEPMETEAKG TTEVEKVEEK SAVDLTPIVV EDKEEKKEEE EKKDVMLQNG
     ETPKDLSDEK QKKNSKQRFM FNIADGGFTE LHSLWQNEER AATVTKKTYE IWHRRHDYWL
     LAGIINHGYA RWQDIQNDPR YAILNEPFKG EMNRGNFLEI KNKFLARRFK LLEQALVIEE
     QLRRAAYLNM SEDPSHPSMA LNTRFAEVEC LAESHQHLSK ESMAGNKPAN AVLHKVLKQL
     EELLSDMKAD VTRLPATIAR IPPVAVRLQM SERNILSRLA NRAPEPPPQQ VAQQQ
//
ID   SARM1_MOUSE             Reviewed;         724 AA.
AC   Q6PDS3; Q5SYG5; Q5SYG6; Q6A054; Q6SZW0; Q8BRI9;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Sterile alpha and TIR motif-containing protein 1;
DE   AltName: Full=Tir-1 homolog;
GN   Name=Sarm1; Synonyms=Kiaa0524;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA   Bousson J.-C., Casteran C., Tiraby G.;
RT   "SARM1 isoforms nucleotide sequence.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Pancreatic islet;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Involved in innate immnune response. Acts as a negative
CC       regulator of TICAM1/TRIF-dependent Toll-like receptor signaling by
CC       inhibiting induction of TLR3- and TLR4-dependent genes.
CC       Specifically blocks TICAM1/TRIF-dependent transcription-factor
CC       activation and gene induction, without affecting the MYD88-
CC       dependent pathway or non-TLR signaling. Negative regulator of NF-
CC       kappa-B and IRF activation (By similarity).
CC   -!- SUBUNIT: Interacts with TICAM1/TRIF and thereby interferes with
CC       TICAM1/TRIF function (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q6PDS3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PDS3-2; Sequence=VSP_013604;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q6PDS3-3; Sequence=VSP_013605;
CC       Name=4;
CC         IsoId=Q6PDS3-4; Sequence=VSP_013606, VSP_013607;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 2 SAM (sterile alpha motif) domains.
CC   -!- SIMILARITY: Contains 1 TIR domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32242.1; Type=Erroneous initiation;
CC       Sequence=CAI25546.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
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DR   EMBL; AY444167; AAR17521.1; -; mRNA.
DR   EMBL; AK172964; BAD32242.1; ALT_INIT; Transcribed_RNA.
DR   EMBL; AK044113; BAC31784.1; -; mRNA.
DR   EMBL; AL591177; CAI25544.1; -; Genomic_DNA.
DR   EMBL; AL591177; CAI25545.1; -; Genomic_DNA.
DR   EMBL; AL591177; CAI25546.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC058534; AAH58534.1; -; mRNA.
DR   EMBL; BC080850; AAH80850.1; -; mRNA.
DR   IPI; IPI00454001; -.
DR   IPI; IPI00469207; -.
DR   IPI; IPI00515675; -.
DR   IPI; IPI00556903; -.
DR   RefSeq; NP_001161993.1; NM_001168521.1.
DR   RefSeq; NP_766383.2; NM_172795.3.
DR   UniGene; Mm.210332; -.
DR   ProteinModelPortal; Q6PDS3; -.
DR   SMR; Q6PDS3; 119-152, 406-476, 484-549, 561-659.
DR   STRING; Q6PDS3; -.
DR   PRIDE; Q6PDS3; -.
DR   Ensembl; ENSMUST00000061174; ENSMUSP00000051059; ENSMUSG00000050132.
DR   Ensembl; ENSMUST00000108287; ENSMUSP00000103922; ENSMUSG00000050132.
DR   GeneID; 237868; -.
DR   KEGG; mmu:237868; -.
DR   UCSC; uc007kjh.1; mouse.
DR   UCSC; uc007kji.1; mouse.
DR   UCSC; uc007kjj.1; mouse.
DR   CTD; 237868; -.
DR   MGI; MGI:2136419; Sarm1.
DR   GeneTree; ENSGT00390000004155; -.
DR   HOVERGEN; HBG079166; -.
DR   OMA; AFYLCVE; -.
DR   OrthoDB; EOG46WZ7W; -.
DR   NextBio; 383536; -.
DR   ArrayExpress; Q6PDS3; -.
DR   Bgee; Q6PDS3; -.
DR   Genevestigator; Q6PDS3; -.
DR   GermOnline; ENSMUSG00000050132; Mus musculus.
DR   GO; GO:0031315; C:extrinsic to mitochondrial outer membrane; IDA:MGI.
DR   GO; GO:0031224; C:intrinsic to membrane; IEA:InterPro.
DR   GO; GO:0005874; C:microtubule; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004888; F:transmembrane receptor activity; IEA:InterPro.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0042981; P:regulation of apoptosis; IMP:MGI.
DR   GO; GO:0009749; P:response to glucose stimulus; IMP:MGI.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR011510; SAM_2.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   InterPro; IPR000157; Toll-Interleukin_rcpt.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 2.
DR   Pfam; PF07647; SAM_2; 2.
DR   SMART; SM00454; SAM; 2.
DR   SMART; SM00255; TIR; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   SUPFAM; SSF52200; TIR; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 2.
DR   PROSITE; PS50104; TIR; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Immunity; Innate immunity; Repeat.
FT   CHAIN         1    724       Sterile alpha and TIR motif-containing
FT                                protein 1.
FT                                /FTId=PRO_0000097590.
FT   DOMAIN      412    476       SAM 1.
FT   DOMAIN      486    548       SAM 2.
FT   DOMAIN      559    657       TIR.
FT   VAR_SEQ       1    536       Missing (in isoform 4).
FT                                /FTId=VSP_013606.
FT   VAR_SEQ     435    439       Missing (in isoform 2).
FT                                /FTId=VSP_013604.
FT   VAR_SEQ     537    543       RILSAAR -> MSLSLAP (in isoform 4).
FT                                /FTId=VSP_013607.
FT   VAR_SEQ     543    543       R -> RGHFAQTGLRSLRRPSLHDDGPRDKQWGRATLTSMS
FT                                LSLAP (in isoform 3).
FT                                /FTId=VSP_013605.
FT   CONFLICT     61     61       V -> A (in Ref. 1; AAR17521).
SQ   SEQUENCE   724 AA;  79606 MW;  9A5BF03ED22E6102 CRC64;
     MVLTLLFSAY KLCRFFTMSG PRPGADRLTV PGPDRSGGAS PWWAAGGRGS REVSPGVGTE
     VQGALERSLP ELQQALSELK QASAARAVGA GLAEVFQLVE EAWLLPAVGR EVAQGLCDAI
     RLDGGLDLLL RLLQAPELET RVQAARLLEQ ILVAENRDRV ARIGLGVILN LAKEREPVEL
     ARSVAGILEH MFKHSEETCQ RLVAAGGLDA VLYWCRRTDP ALLRHCALAL ANCALHGGQT
     VQRCMVEKRA AEWLFPLAFS KEDELLRLHA CLAVAVLATN KEVEREVEHS GTLALVEPLV
     ASLDPGRFAR CLVDASDTSQ GRGPDDLQSL VLLLDSSRLE AQCIGAFYLC AEAAIKSLQG
     KTKVFSDIGA IQSLKRLVSY STNGTTSALA KRALRLLGEE VPRRILPCVA SWKEAEVQTW
     LQQIGFSQYC ENFREQQVDG DLLLRLTDEE LQTDLGMKSS ITRKRFFREL TELKTFASYA
     TCDRSNLADW LGSLDPRFRQ YTYGLVSCGL DRSLLHRVSE QQLLEDCGIR LGVHRTRILS
     AAREMLHSPL PCTGGKLSGD TPDVFISYRR NSGSQLASLL KVHLQLHGFS VFIDVEKLEA
     GKFEDKLIQS VIAARNFVLV LSAGALDKCM QDHDCKDWVH KEIVTALSCG KNIVPIIDGF
     EWPEPQALPE DMQAVLTFNG IKWSHEYQEA TIEKIIRFLQ GRPSQDSSAG SDTSLEGATP
     MGLP
//
ID   Q6PDY6_MOUSE            Unreviewed;       471 AA.
AC   Q6PDY6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Protein Wnt;
DE   Flags: Fragment;
GN   Name=Wnt7b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Ligand for members of the frizzled family of seven
CC       transmembrane receptors (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix (By similarity).
CC   -!- SIMILARITY: Belongs to the Wnt family.
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DR   EMBL; BC058398; AAH58398.1; -; mRNA.
DR   IPI; IPI00875309; -.
DR   RefSeq; NP_033554.3; NM_009528.3.
DR   UniGene; Mm.306946; -.
DR   STRING; Q6PDY6; -.
DR   PRIDE; Q6PDY6; -.
DR   GeneID; 22422; -.
DR   KEGG; mmu:22422; -.
DR   UCSC; uc007xdg.1; mouse.
DR   CTD; 22422; -.
DR   MGI; MGI:98962; Wnt7b.
DR   eggNOG; maNOG22330; -.
DR   Genevestigator; Q6PDY6; -.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-KW.
DR   GO; GO:0005109; F:frizzled binding; IPI:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0060033; P:anatomical structure regression; IMP:MGI.
DR   GO; GO:0060070; P:canonical Wnt receptor signaling pathway; IDA:MGI.
DR   GO; GO:0007267; P:cell-cell signaling; TAS:MGI.
DR   GO; GO:0044237; P:cellular metabolic process; IMP:MGI.
DR   GO; GO:0022009; P:central nervous system vasculogenesis; IGI:MGI.
DR   GO; GO:0060710; P:chorio-allantoic fusion; IMP:MGI.
DR   GO; GO:0060560; P:developmental growth involved in morphogenesis; IMP:MGI.
DR   GO; GO:0060669; P:embryonic placenta morphogenesis; IMP:MGI.
DR   GO; GO:0016332; P:establishment or maintenance of polarity of embryonic epithelium; IMP:MGI.
DR   GO; GO:0006917; P:induction of apoptosis; IMP:MGI.
DR   GO; GO:0072061; P:inner medullary collecting duct development; IMP:MGI.
DR   GO; GO:0060482; P:lobar bronchus development; IMP:MGI.
DR   GO; GO:0060428; P:lung epithelium development; IMP:MGI.
DR   GO; GO:0060425; P:lung morphogenesis; IMP:MGI.
DR   GO; GO:0060484; P:lung-associated mesenchyme development; IMP:MGI.
DR   GO; GO:0072205; P:metanephric collecting duct development; IMP:MGI.
DR   GO; GO:0072236; P:metanephric loop of Henle development; IMP:MGI.
DR   GO; GO:0003338; P:metanephros morphogenesis; IMP:MGI.
DR   GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:MGI.
DR   GO; GO:0042475; P:odontogenesis of dentine-containing tooth; IMP:MGI.
DR   GO; GO:0072060; P:outer medullary collecting duct development; IMP:MGI.
DR   GO; GO:0032364; P:oxygen homeostasis; IMP:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:MGI.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:MGI.
DR   GO; GO:0072053; P:renal inner medulla development; IMP:MGI.
DR   GO; GO:0072054; P:renal outer medulla development; IMP:MGI.
DR   GO; GO:0051145; P:smooth muscle cell differentiation; IMP:MGI.
DR   GO; GO:0050808; P:synapse organization; IGI:MGI.
DR   GO; GO:0060535; P:trachea cartilage morphogenesis; IMP:MGI.
DR   GO; GO:0007223; P:Wnt receptor signaling pathway, calcium modulating pathway; IEA:InterPro.
DR   InterPro; IPR013300; Wnt7.
DR   InterPro; IPR005816; Wnt_grthfactor.
DR   InterPro; IPR018161; Wnt_grthfactor_CS.
DR   InterPro; IPR005817; Wnt_SF.
DR   PANTHER; PTHR12027; Wnt; 1.
DR   Pfam; PF00110; wnt; 1.
DR   PRINTS; PR01891; WNT7PROTEIN.
DR   PRINTS; PR01349; WNTPROTEIN.
DR   SMART; SM00097; WNT1; 1.
DR   PROSITE; PS00246; WNT1; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Extracellular matrix; Secreted;
KW   Wnt signaling pathway.
FT   NON_TER       1      1
SQ   SEQUENCE   471 AA;  52395 MW;  95B9DFA895B1E792 CRC64;
     RTHWPPRRTA RRARPQAAKP SGGSARPLLL APACARRVPR SLRWAPRSRF PARVTPPGAR
     GGCGALGSPW WQRVPGAHAS PASRAEAPAE RGPTAAPWLL PGPCPPARPL RPQLSMAQPP
     SLDHAQKLSK VDLLRVSLLW RPLREARSIV IRGGPGSQHH LQQDSWPGPT AACHLPEPTR
     CHHCDRGGGA DGHRRVPAPV PIRPLELLRP GREDRLRART PRSREAAFTY AITAAGVAHA
     VTAACSQGNL SNCGCDREKQ GYYNQAEGWK WGGCSADVRY GIDFSRRFVD AREIKKNARR
     LMNLHNNEAG RKVLEDRMKL ECKCHGVSGS CTTKTCWTTL PKFREVGHLL KEKYNAAVQV
     EVVRASRLRQ PTFLRIKQLR SYQKPMETDL VYIEKSPNYC EEDAATGSVG TQGRLCNRTS
     PGADGCDTMC CGRVYNTHQY TKVWQCNCKF HWCCFVKCNT CSERTEVFTC K
//
ID   PRRT3_MOUSE             Reviewed;         971 AA.
AC   Q6PE13;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Proline-rich transmembrane protein 3;
DE   Flags: Precursor;
GN   Name=Prrt3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-845, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-799; SER-804; SER-806
RP   AND SER-865, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
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DR   EMBL; BC058349; AAH58349.1; -; mRNA.
DR   IPI; IPI00461626; -.
DR   RefSeq; NP_766075.2; NM_172487.3.
DR   UniGene; Mm.133060; -.
DR   ProteinModelPortal; Q6PE13; -.
DR   PhosphoSite; Q6PE13; -.
DR   PRIDE; Q6PE13; -.
DR   Ensembl; ENSMUST00000057429; ENSMUSP00000050657; ENSMUSG00000045009.
DR   Ensembl; ENSMUST00000101059; ENSMUSP00000098620; ENSMUSG00000045009.
DR   GeneID; 210673; -.
DR   KEGG; mmu:210673; -.
DR   UCSC; uc009dgp.1; mouse.
DR   CTD; 210673; -.
DR   MGI; MGI:2444810; Prrt3.
DR   eggNOG; roNOG11816; -.
DR   HOGENOM; HBG126606; -.
DR   HOVERGEN; HBG063615; -.
DR   InParanoid; Q6PE13; -.
DR   OMA; DGPRGWD; -.
DR   OrthoDB; EOG48D0TT; -.
DR   PhylomeDB; Q6PE13; -.
DR   NextBio; 373018; -.
DR   ArrayExpress; Q6PE13; -.
DR   Bgee; Q6PE13; -.
DR   CleanEx; MM_PRRT3; -.
DR   Genevestigator; Q6PE13; -.
DR   GermOnline; ENSMUSG00000045009; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Phosphoprotein; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     27       Potential.
FT   CHAIN        28    971       Proline-rich transmembrane protein 3.
FT                                /FTId=PRO_0000251979.
FT   TOPO_DOM     28    467       Extracellular (Potential).
FT   TRANSMEM    468    488       Helical; (Potential).
FT   TOPO_DOM    489    491       Cytoplasmic (Potential).
FT   TRANSMEM    492    512       Helical; (Potential).
FT   TOPO_DOM    513    532       Extracellular (Potential).
FT   TRANSMEM    533    553       Helical; (Potential).
FT   TOPO_DOM    554    560       Cytoplasmic (Potential).
FT   TRANSMEM    561    581       Helical; (Potential).
FT   TOPO_DOM    582    588       Extracellular (Potential).
FT   TRANSMEM    589    609       Helical; (Potential).
FT   TOPO_DOM    610    628       Cytoplasmic (Potential).
FT   TRANSMEM    629    649       Helical; (Potential).
FT   TOPO_DOM    650    669       Extracellular (Potential).
FT   TRANSMEM    670    690       Helical; (Potential).
FT   TOPO_DOM    691    971       Cytoplasmic (Potential).
FT   COMPBIAS    239    452       Pro-rich.
FT   MOD_RES     799    799       Phosphoserine.
FT   MOD_RES     804    804       Phosphoserine.
FT   MOD_RES     806    806       Phosphoserine.
FT   MOD_RES     845    845       Phosphoserine.
FT   MOD_RES     865    865       Phosphoserine.
FT   CARBOHYD     58     58       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    369    369       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   971 AA;  101224 MW;  3ED4E0DB57A01590 CRC64;
     MAPSPQACTS PLLLLLLPCL GAGPALGRGL PRPLENSEPH MIPSESQTFD LFWEKLRNES
     SWHSGDPQAR AEGPKKPADP YLGPALHGPK AAPGVQGERL LRADDLQLAR AFTSQGWTGP
     PDSQELLEPE APEPHPVRAP RLTLVTTTPS SLLSAAILST ASQKPGGTAG QQPARNEELI
     MVKAETHITQ ASPWDFQGSS HTPVPETDAV RTLVLGKQGG HEQGFQEAVQ GPLLTQQDPV
     VPGVGSTPPV KVESTPEPGA QLDLALVRSL PLPEGLPAEP PKTGAGDTWE VSSLGPQPEQ
     TDLLGGQDSP APQPIPPSAS DTSDGHLRPV SSLNGADPIS PQRVRGAMEA PGTPKSFIPD
     LPNSAQAANG TESPVRALQP DEAEDWPGRP QSHPPAPPVQ APSTSRRGLV RVTTQRALGQ
     PLPPEPSASS IVPIPASSPP ANATAPPLRW GPLRRVLSFS WELHVYGVGV LFLLPALLAL
     VTVAAALAGP RLALVAAALV LVASGLRSAY MLTDPYGSQA RLGVRAGLVL YNLPFPLLLT
     ALAALTLLGL GAGLPQPLQK PLLLGIVAPV HGTCLLATDL FSTSPVLNLL TQGLSCAWGA
     SVALGTLCLC RRRLLEGPRG WDASPGPRLL AVAGSLGLLA SGLQLAASLW LYPGPGREGR
     FSWAWWGVHF WLRLLELTWA LALALAALAA TRPRPPTEHA CWAKLLRLAC PAPTGKSEVP
     ERPNNCYAGP SGLGTGGLDI SKSLIRNAAG EAGLPVTPGS GPWGSAASLG RGRPGGQRMS
     RGSVGPAPSL SELDLRPPSP INLSRSIDAA LFREHLVRES VFQRCGLRGL ASSPTGGALR
     PRRGSQPDAE LDGAGTSLLR GRCRSLTEVC LRTSLPQHVM EPPVGAAAAG TSGSSLDSFS
     KGSLKISWNP WRHGLSSVDS LPLDELPSTV QLLPPPTPVP APARAGEPQG EGQSRCKSSE
     SHSASSDTIE L
//
ID   CTIF_MOUSE              Reviewed;         600 AA.
AC   Q6PEE2; Q6A069;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=CBP80/20-dependent translation initiation factor;
GN   Name=Ctif; Synonyms=Gm672, Kiaa0427;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 334-600 (ISOFORM 1).
RC   TISSUE=Pancreatic islet;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=19648179; DOI=10.1101/gad.1823409;
RA   Kim K.M., Cho H., Choi K., Kim J., Kim B.-W., Ko Y.-G., Jang S.K.,
RA   Kim Y.K.;
RT   "A new MIF4G domain-containing protein, CTIF, directs nuclear cap-
RT   binding protein CBP80/20-dependent translation.";
RL   Genes Dev. 23:2033-2045(2009).
CC   -!- FUNCTION: Specifically required for the pioneer round of mRNA
CC       translation mediated by the cap-binding complex (CBC), that takes
CC       place during or right after mRNA export via the nuclear pore
CC       complex (NPC). Acts via its interaction with the NCBP1/CBP80
CC       component of the CBC complex and recruits the 40S small subunit of
CC       the ribosome via eIF3. In contrast, it is not involved in steady
CC       state translation, that takes place when the CBC complex is
CC       replaced by cytoplasmic cap-binding protein eIF4E. Also required
CC       for nonsense-mediated mRNA decay (NMD), the pioneer round of mRNA
CC       translation mediated by the cap-binding complex playing a central
CC       role in nonsense-mediated mRNA decay (NMD) (By similarity).
CC   -!- SUBUNIT: Interacts with NCBP1/CBP80; the interaction is direct.
CC       Associates with the eukaryotic translation initiation factor 3
CC       (eIF-3) complex (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6PEE2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PEE2-2; Sequence=VSP_038120;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- SIMILARITY: Belongs to the CTIF family.
CC   -!- SIMILARITY: Contains 1 MIF4G domain.
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DR   EMBL; BC058104; AAH58104.1; -; mRNA.
DR   EMBL; AK172949; BAD32227.1; -; mRNA.
DR   IPI; IPI00400197; -.
DR   IPI; IPI00944727; -.
DR   RefSeq; NP_958742.2; NM_201354.2.
DR   UniGene; Mm.36745; -.
DR   ProteinModelPortal; Q6PEE2; -.
DR   SMR; Q6PEE2; 389-592.
DR   PhosphoSite; Q6PEE2; -.
DR   PRIDE; Q6PEE2; -.
DR   Ensembl; ENSMUST00000065082; ENSMUSP00000065041; ENSMUSG00000052928.
DR   GeneID; 269037; -.
DR   KEGG; mmu:269037; -.
DR   UCSC; uc008fqg.1; mouse.
DR   MGI; MGI:2685518; Gm672.
DR   GeneTree; ENSGT00530000063785; -.
DR   HOGENOM; HBG505924; -.
DR   InParanoid; Q6PEE2; -.
DR   OrthoDB; EOG4CVG6J; -.
DR   NextBio; 392656; -.
DR   ArrayExpress; Q6PEE2; -.
DR   Bgee; Q6PEE2; -.
DR   CleanEx; MM_GM672; -.
DR   Genevestigator; Q6PEE2; -.
DR   GermOnline; ENSMUSG00000052928; Mus musculus.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; ISS:UniProtKB.
DR   GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR016021; MIF4-like_typ_1/2/3.
DR   InterPro; IPR003890; MIF4G-like_typ-3.
DR   Gene3D; G3DSA:1.25.40.180; MIF4-like_typ_1/2/3; 1.
DR   Pfam; PF02854; MIF4G; 1.
DR   SMART; SM00543; MIF4G; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm;
KW   Nonsense-mediated mRNA decay; Phosphoprotein; Translation regulation.
FT   CHAIN         1    600       CBP80/20-dependent translation initiation
FT                                factor.
FT                                /FTId=PRO_0000050755.
FT   DOMAIN      378    579       MIF4G.
FT   REGION        1    305       Interaction with NCBP1/CBP80 (By
FT                                similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      16     16       Phosphoserine (By similarity).
FT   MOD_RES      18     18       Phosphoserine.
FT   MOD_RES     299    299       Phosphoserine (By similarity).
FT   VAR_SEQ     359    359       R -> RDIPNPTETSAPLRCVLCVPHVPQ (in isoform
FT                                2).
FT                                /FTId=VSP_038120.
FT   CONFLICT    383    383       I -> S (in Ref. 2; BAD32227).
SQ   SEQUENCE   600 AA;  67831 MW;  C648CFDEBC94D8AD CRC64;
     MENSSAASAS SEAGSSRSQE IEELERFIDS YVLEYQVQGL LTDKTEGDGE SQRTQSHISQ
     WTADCREQLD GSCSFSRGRA PPQQNGNKDN SLDMLGTDIW AANTFDSFSG ATWDLQPEKL
     DFTQFHRKVR HTPKQPLPHI DREGCGKGKL EDGDGISLND IEKVLPTWQG YHPMPHEAEI
     AHTKKLFRRR RNDRRRQQRP PGGNKPQQHG DHQPGSAKHN RDHQKSYQGG SGPHPSGRPT
     HHGYSQNRRW HHGNMKHPPG DKGEAGSHRN AKETVTVENP KLEDGPGDTG HSGLEPPCSP
     DTLTPAASER PTPQLPGGPE AEIKHKDTVL PERLRERPKI TLLQSSKDRL RRRLKEKDRD
     EVAVETSSPQ PSKMDRLMEI LNIMRNNSSD VDAKLTSFME EAQNSTNSEE MLGEIVRTIY
     QKAVSDRSFA FTAAKLCDKM ALFMVEGTKF RSLLLNMLQK DFTVREELQQ QDVERWLGFI
     TFLCEVFGTM RSSTGEPFRV LVCPIYTCLR ELLQSQDVKE DAVLCCSMEL QSTGRLLEEQ
     LPEMMTELLA SARDKMLCPS ESMLTRSLLL EVIELHANSW NPLTPPITQY YNRTIQKLTA
//
ID   GRAM3_MOUSE             Reviewed;         445 AA.
AC   Q6PEM6;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   RecName: Full=GRAM domain-containing protein 3;
GN   Name=Gramd3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SIMILARITY: Contains 1 GRAM domain.
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DR   EMBL; BC057978; AAH57978.1; -; mRNA.
DR   IPI; IPI00461745; -.
DR   UniGene; Mm.24356; -.
DR   PhosphoSite; Q6PEM6; -.
DR   PRIDE; Q6PEM6; -.
DR   Ensembl; ENSMUST00000070166; ENSMUSP00000068453; ENSMUSG00000001700.
DR   Ensembl; ENSMUST00000116636; ENSMUSP00000112335; ENSMUSG00000001700.
DR   UCSC; uc008eyk.1; mouse.
DR   MGI; MGI:1914815; Gramd3.
DR   HOVERGEN; HBG055715; -.
DR   InParanoid; Q6PEM6; -.
DR   OrthoDB; EOG4548ZJ; -.
DR   ArrayExpress; Q6PEM6; -.
DR   Bgee; Q6PEM6; -.
DR   CleanEx; MM_GRAMD3; -.
DR   Genevestigator; Q6PEM6; -.
DR   GermOnline; ENSMUSG00000001700; Mus musculus.
DR   InterPro; IPR004182; GRAM.
DR   Pfam; PF02893; GRAM; 1.
DR   SMART; SM00568; GRAM; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    445       GRAM domain-containing protein 3.
FT                                /FTId=PRO_0000087578.
FT   DOMAIN      123    190       GRAM.
FT   MOD_RES     234    234       Phosphoserine.
FT   MOD_RES     265    265       Phosphoserine.
SQ   SEQUENCE   445 AA;  49287 MW;  C54E0599805AEB5A CRC64;
     MVKKRLSSSD NVFKFEIPSN SKTSAEAPHS STDSPSSVFL SSEAENGAED RRRVSKSPTA
     QSPTSSVEAE SPDQKRSLGL WSKSSFDGSS LLSDKNDCKT ESKTDSKTER KKSSSSSQYK
     ANMHFHKLFL DVPTEEPLRQ SFTCALQKEI LYQGKLFVSE NWICFHSKVF GKDTKISIPA
     FSVTLIKKTK TALLVPNALI IATVTDRYIF VSLLSRDSTY KLIKSVCGHL EKTSVGNSPN
     PSSAENSFRA DRPSSLPLDF NDEFSDLDGV VRQRRQDLEG YSSSGSQTPE SENSRDFHVT
     ESQTVLNVTK GETKPPRTDA HGSRAPDGKA KILPAHGQSE TIGILHKMES RKCPTLHHIL
     IVYAIIVCAL IISTFYMRYR INTLEERLGT LTSIMDPHST EQTAPSGLGS QMQLNVEVLC
     QELTANIVKL EKIQNNLQKL LENGD
//
ID   MARE3_MOUSE             Reviewed;         281 AA.
AC   Q6PER3; Q61167;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Microtubule-associated protein RP/EB family member 3;
DE   AltName: Full=EB1 protein family member 3;
DE            Short=EBF3;
DE   AltName: Full=End-binding protein 3;
DE            Short=EB3;
DE   AltName: Full=RP3;
GN   Name=Mapre3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 57-281.
RA   Hoffman N.G., Kay B.K.;
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   INTERACTION WITH APC2.
RX   PubMed=17310996; DOI=10.1038/sj.onc.1210304;
RA   Hsieh P.-C., Chang J.-C., Sun W.-T., Hsieh S.-C., Wang M.-C.,
RA   Wang F.-F.;
RT   "p53 downstream target DDA3 is a novel microtubule-associated protein
RT   that interacts with end-binding protein EB3 and activates beta-catenin
RT   pathway.";
RL   Oncogene 26:4928-4940(2007).
CC   -!- FUNCTION: May be involved in microtubule polymerization, and
CC       spindle function by stabilizing microtubules and anchoring them at
CC       centrosomes. May play a role in cell migration (By similarity).
CC   -!- SUBUNIT: Interacts with DCTN1 and SRCIN1. Binds to the C-terminal
CC       domain of APC. Binds monomeric and polymerized tubulin (By
CC       similarity). Interacts with APC2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity). Note=Associated with the microtubule
CC       network (By similarity).
CC   -!- DOMAIN: Composed of two functionally independent domains. The N-
CC       terminal domain forms an hydrophobic cleft involved in microtubule
CC       binding and the C-terminal is involved in the formation of
CC       mutually exclusive complexes with APC and DCTN1 (By similarity).
CC   -!- SIMILARITY: Belongs to the MAPRE family.
CC   -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC   -!- SIMILARITY: Contains 1 EB1 C-terminal domain.
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DR   EMBL; BC057918; AAH57918.1; -; mRNA.
DR   EMBL; U51204; AAA96321.1; -; mRNA.
DR   IPI; IPI00343557; -.
DR   RefSeq; NP_579928.1; NM_133350.1.
DR   UniGene; Mm.332295; -.
DR   UniGene; Mm.471154; -.
DR   ProteinModelPortal; Q6PER3; -.
DR   SMR; Q6PER3; 1-130, 204-262.
DR   STRING; Q6PER3; -.
DR   PhosphoSite; Q6PER3; -.
DR   PRIDE; Q6PER3; -.
DR   Ensembl; ENSMUST00000031058; ENSMUSP00000031058; ENSMUSG00000029166.
DR   GeneID; 100732; -.
DR   KEGG; mmu:100732; -.
DR   UCSC; uc008wvz.1; mouse.
DR   CTD; 100732; -.
DR   MGI; MGI:2140967; Mapre3.
DR   GeneTree; ENSGT00490000043329; -.
DR   HOGENOM; HBG622485; -.
DR   HOVERGEN; HBG052410; -.
DR   InParanoid; Q6PER3; -.
DR   OMA; HESDNSP; -.
DR   OrthoDB; EOG41ZFBH; -.
DR   PhylomeDB; Q6PER3; -.
DR   NextBio; 354616; -.
DR   ArrayExpress; Q6PER3; -.
DR   Bgee; Q6PER3; -.
DR   Genevestigator; Q6PER3; -.
DR   GermOnline; ENSMUSG00000029166; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005874; C:microtubule; IDA:BHF-UCL.
DR   GO; GO:0030496; C:midbody; IDA:BHF-UCL.
DR   GO; GO:0008017; F:microtubule binding; IDA:BHF-UCL.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0043193; P:positive regulation of gene-specific transcription; IMP:BHF-UCL.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR004953; EB1_C.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF03271; EB1; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS51230; EB1_C; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Microtubule;
KW   Mitosis; Phosphoprotein.
FT   CHAIN         1    281       Microtubule-associated protein RP/EB
FT                                family member 3.
FT                                /FTId=PRO_0000213429.
FT   DOMAIN       14    116       CH.
FT   DOMAIN      194    264       EB1 C-terminal.
FT   REGION      217    281       DCTN1-binding (By similarity).
FT   REGION      217    260       APC-binding (By similarity).
FT   MOD_RES     161    161       Phosphothreonine.
SQ   SEQUENCE   281 AA;  31966 MW;  6713427C480838DC CRC64;
     MAVNVYSTSV TSENLSRHDM LAWVNDSLHL NYTKIEQLCS GAAYCQFMDM LFPGCVHLRK
     VKFQAKLEHE YIHNFKVLQA AFKKMGVDKI IPVEKLVKGK FQDNFEFIQW FKKFFDANYD
     GKDYNPLLAR QGQDVAPPPN PGDQIFNKSK KLIGTAVPQR TSPTGPKNMQ TSGRLSNVAP
     PCILRKNPPS ARNGGHEADA QILELNQQLL DLKLTVDGLE KERDFYFSKL RDIELICQEH
     ESENSPVISG IIGILYATEE GFAPPEDDEI EEHQQEDQDE Y
//
ID   WIPF2_MOUSE             Reviewed;         440 AA.
AC   Q6PEV3;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=WAS/WASL-interacting protein family member 2;
DE   AltName: Full=WASP-interacting protein-related protein;
DE   AltName: Full=WIP-related protein;
GN   Name=Wipf2; Synonyms=Wire;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Plays an active role in the formation of cell surface
CC       protrusions downstream of activated PDGFB receptors. Plays an
CC       important role in actin-microspike formation through cooperation
CC       with WASL. May cooperate with WASP and WASL to induce mobilization
CC       and reorganization of the actin filament system (By similarity).
CC   -!- SUBUNIT: Interacts with WASL and WASP, and this interaction
CC       results in cytoplasmic relocation of these two proteins along
CC       actin filaments. Interacts with NCK2 resulting in the localization
CC       to sites of focal adhesions (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Note=Localized to stress fibers and bundles of actin filaments (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the verprolin family.
CC   -!- SIMILARITY: Contains 1 WH2 domain.
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DR   EMBL; BC057854; AAH57854.1; -; mRNA.
DR   IPI; IPI00378728; -.
DR   RefSeq; NP_922922.1; NM_197940.2.
DR   UniGene; Mm.28661; -.
DR   UniGene; Mm.473466; -.
DR   ProteinModelPortal; Q6PEV3; -.
DR   SMR; Q6PEV3; 33-65.
DR   STRING; Q6PEV3; -.
DR   PhosphoSite; Q6PEV3; -.
DR   PRIDE; Q6PEV3; -.
DR   Ensembl; ENSMUST00000037480; ENSMUSP00000046991; ENSMUSG00000038013.
DR   GeneID; 68524; -.
DR   KEGG; mmu:68524; -.
DR   UCSC; uc007lht.1; mouse.
DR   CTD; 68524; -.
DR   MGI; MGI:1924462; Wipf2.
DR   eggNOG; roNOG07885; -.
DR   GeneTree; ENSGT00580000081291; -.
DR   HOGENOM; HBG714313; -.
DR   HOVERGEN; HBG060210; -.
DR   InParanoid; Q6PEV3; -.
DR   OMA; REGHPAP; -.
DR   OrthoDB; EOG40P482; -.
DR   PhylomeDB; Q6PEV3; -.
DR   NextBio; 327382; -.
DR   ArrayExpress; Q6PEV3; -.
DR   Bgee; Q6PEV3; -.
DR   CleanEx; MM_WIPF2; -.
DR   Genevestigator; Q6PEV3; -.
DR   GermOnline; ENSMUSG00000038013; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR003124; WH2_actin-bd.
DR   SMART; SM00246; WH2; 1.
DR   PROSITE; PS51082; WH2; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Cytoplasm; Cytoskeleton.
FT   CHAIN         1    440       WAS/WASL-interacting protein family
FT                                member 2.
FT                                /FTId=PRO_0000065976.
FT   DOMAIN       36     53       WH2.
FT   REGION       49     52       Binds actin (Potential).
FT   COMPBIAS      2     17       Poly-Pro.
FT   COMPBIAS    177    182       Poly-Pro.
FT   COMPBIAS    250    254       Poly-Pro.
FT   COMPBIAS    296    299       Poly-Pro.
FT   COMPBIAS    311    314       Poly-Pro.
FT   COMPBIAS    325    330       Poly-Pro.
FT   COMPBIAS    340    345       Poly-Pro.
FT   COMPBIAS    359    363       Poly-Pro.
FT   COMPBIAS    370    377       Poly-Pro.
SQ   SEQUENCE   440 AA;  46297 MW;  8DBE6864CABD52B4 CRC64;
     MPIPPPPPPP PGPPPPPTFN QANTEQPKLS RDEQRNRGAL LQDICKGTKL KKVTNVNDRS
     APVIEKPRGS SGGYGPGAAA LQPKGGLFQG GVPKLRPVGA KDASEAPAGK PALQVPSSRA
     AAPRPPGSAA SGRPHDDTDS NRASLPELPR MQRPSLPDLS RPNTASGTGM KHSSSAPPPP
     PPGRRANAPP TPLPLHSNKA QAYNREKPLP PTPGQRLHPG REGHPAPPPV KPPPSPVNIR
     TGPSGQSLAP PPPPYRQPPG VPNGPSSPTN ESAPELPQRH NSLHRKTPGP VRGLAPPPPT
     SATPSLLSNR PPPPAREPPS RGAAPPPPPP MIRNGARDAP PPPPPYRMHG SEPPSRGKPP
     PPPSRTPAGP PPPPPPPLRN GHRDSITTVR SFLDDFESKY SFHPVEDFPA PEEYKHLQRV
     YPSKTNRAAR GAPPLPPILR
//
ID   PK3C3_MOUSE             Reviewed;         887 AA.
AC   Q6PF93; Q8R3S8;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Phosphatidylinositol 3-kinase catalytic subunit type 3;
DE            Short=PI3-kinase type 3;
DE            Short=PI3K type 3;
DE            Short=PtdIns-3-kinase type 3;
DE            EC=2.7.1.137;
DE   AltName: Full=Phosphoinositide-3-kinase class 3;
GN   Name=Pik3c3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-525, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [3]
RP   INTERACTION WITH BECN1 AND AMBRA1.
RX   PubMed=17589504; DOI=10.1038/nature05925;
RA   Maria Fimia G., Stoykova A., Romagnoli A., Giunta L.,
RA   Di Bartolomeo S., Nardacci R., Corazzari M., Fuoco C., Ucar A.,
RA   Schwartz P., Gruss P., Piacentini M., Chowdhury K., Cecconi F.;
RT   "Ambra1 regulates autophagy and development of the nervous system.";
RL   Nature 447:1121-1125(2007).
CC   -!- FUNCTION: Catalytic subunit of the PI3K complex. Involved in the
CC       transport of lysosomal enzyme precursors to lysosomes (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol = ADP +
CC       1-phosphatidyl-1D-myo-inositol 3-phosphate.
CC   -!- COFACTOR: Manganese (By similarity).
CC   -!- SUBUNIT: Heterodimer. This subunit, part of a complex composed of
CC       regulatory and catalytic subunits, associates with regulatory
CC       subunit PIK3R4 (By similarity). Interacts with AMBRA1. Forms a
CC       complex with BECN1, PIK3R4 and either UVRAG and KIAA0226/Rubicon,
CC       or with ATG14. In this complex, presence of UVRAG and ATG14 are
CC       mutually exclusive (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6PF93-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PF93-2; Sequence=VSP_016459, VSP_016460;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC   -!- SIMILARITY: Contains 1 PI3K/PI4K domain.
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DR   EMBL; BC024675; AAH24675.1; -; mRNA.
DR   EMBL; BC057678; AAH57678.1; -; mRNA.
DR   IPI; IPI00113918; -.
DR   IPI; IPI00621925; -.
DR   RefSeq; NP_852079.2; NM_181414.5.
DR   UniGene; Mm.194127; -.
DR   ProteinModelPortal; Q6PF93; -.
DR   SMR; Q6PF93; 12-881.
DR   STRING; Q6PF93; -.
DR   PhosphoSite; Q6PF93; -.
DR   PRIDE; Q6PF93; -.
DR   Ensembl; ENSMUST00000091978; ENSMUSP00000089601; ENSMUSG00000033628.
DR   Ensembl; ENSMUST00000115812; ENSMUSP00000111479; ENSMUSG00000033628.
DR   GeneID; 225326; -.
DR   KEGG; mmu:225326; -.
DR   UCSC; uc008ehw.1; mouse.
DR   CTD; 225326; -.
DR   MGI; MGI:2445019; Pik3c3.
DR   eggNOG; roNOG12974; -.
DR   GeneTree; ENSGT00550000074176; -.
DR   HOGENOM; HBG320338; -.
DR   HOVERGEN; HBG082145; -.
DR   InParanoid; Q6PF93; -.
DR   OMA; YLMVEFP; -.
DR   OrthoDB; EOG46T30T; -.
DR   PhylomeDB; Q6PF93; -.
DR   BRENDA; 2.7.1.137; 244.
DR   NextBio; 377617; -.
DR   ArrayExpress; Q6PF93; -.
DR   Bgee; Q6PF93; -.
DR   CleanEx; MM_PIK3C3; -.
DR   Genevestigator; Q6PF93; -.
DR   GermOnline; ENSMUSG00000033628; Mus musculus.
DR   GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IEA:InterPro.
DR   GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IMP:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IMP:MGI.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000403; PI3/4_kinase_cat.
DR   InterPro; IPR018936; PI3/4_kinase_CS.
DR   InterPro; IPR002420; PI3K_C2.
DR   InterPro; IPR008290; PI3K_Vps34.
DR   InterPro; IPR015433; PI_Kinase.
DR   InterPro; IPR001263; PInositide-3_kin_accessory_dom.
DR   Gene3D; G3DSA:1.10.1070.11; PI3/4_kinase_cat; 1.
DR   Gene3D; G3DSA:1.25.40.70; PI3Ka; 2.
DR   PANTHER; PTHR10048; PI_Kinase; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF00792; PI3K_C2; 1.
DR   Pfam; PF00613; PI3Ka; 1.
DR   PIRSF; PIRSF000587; PI3K_Vps34; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00142; PI3K_C2; 1.
DR   SMART; SM00145; PI3Ka; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Kinase; Manganese;
KW   Nucleotide-binding; Phosphoprotein; Transferase.
FT   CHAIN         1    887       Phosphatidylinositol 3-kinase catalytic
FT                                subunit type 3.
FT                                /FTId=PRO_0000088803.
FT   DOMAIN      631    885       PI3K/PI4K.
FT   MOD_RES      25     25       Phosphoserine (By similarity).
FT   MOD_RES     163    163       Phosphothreonine (By similarity).
FT   MOD_RES     165    165       Phosphoserine (By similarity).
FT   MOD_RES     244    244       Phosphoserine (By similarity).
FT   MOD_RES     261    261       Phosphoserine (By similarity).
FT   MOD_RES     455    455       Phosphoserine (By similarity).
FT   MOD_RES     525    525       Phosphoserine.
FT   MOD_RES     625    625       Phosphothreonine (By similarity).
FT   VAR_SEQ     842    848       VQDKFRL -> ISCHRKM (in isoform 2).
FT                                /FTId=VSP_016459.
FT   VAR_SEQ     849    887       Missing (in isoform 2).
FT                                /FTId=VSP_016460.
FT   CONFLICT    455    455       Missing (in Ref. 1; AAH57678).
FT   CONFLICT    470    470       N -> S (in Ref. 1; AAH57678).
SQ   SEQUENCE   887 AA;  101487 MW;  80E8EF9EF3AF74D7 CRC64;
     MGEAEKFHYI YSCDLDINVQ LKIGSLEGKR EQKSYKAVLE DPMLKFSGLY QETCSDLYVT
     CQVFAEGKPL ALPVRTSYKA FSTRWNWNEW LKLPVKYPDL PRNAQVALTI WDVYGPGSAV
     PVGGTTVSLF GKYGMFRQGM HDLKVWPNVE ADGSEPTRTP GRTSSTLSED QMSRLAKLTK
     AHRQGHMVKV DWLDRLTFRE IEMINESEKR SSNFMYLMVE FRCVKCDDKE YGIVYYEKDG
     DESSPILTSF ELVKVPDPQM SMENLVESKH HKLARSLRSG PSDHDLKPNA TTRDQLNIIV
     SYPPTKQLTY EEQDLVWKFR YYLTNQEKAL TKFLKCVNWD LPQEAKQALE LLGKWKPMDV
     EDSLELLSSH YTNPTVRRYA VARLRQADDE DLLMYLLQLV QALKYENFDD IKNGLEPTKK
     DSQTSASESL SNSGVSSGDI DSSQIITNPL PPVASPPPAS KAKEVSDGEN LEQDLCTFLI
     SRACKNSTLA NYLYWYVIVE CEDQDTQQRD PKTHEMYLNV MRRFSQALLK GDKSVRVMRS
     LLAAQQTFVD RLVHLMKAVQ RESGNRKKKN ERLQALLGDN EKMNLSDVEL IPLPLEPQVK
     IRGIIPETAT LFKSALMPAQ LFFKTEDGGK YPVIFKHGDD LRQDQLILQI ISLMDKLLRK
     ENLDLKLTPY KVLATSTKHG FMQFIQSVPV AEVLDTEGSI QNFFRKYAPS ETGPYGISAE
     VMDTYVKSCA GYCVITYILG VGDRHLDNLL LTKTGKLFHI DFGYILGRDP KPLPPPMKLN
     KEMVEGMGGT QSEQYQEFRK QCYTAFLHLR RYSNLILNLF SLMVDANIPD IALEPDKTVK
     KVQDKFRLDL SDEEAVHYMQ SLIDESVHAL FAAVVEQIHK FAQYWRK
//
ID   DLGP3_MOUSE             Reviewed;         977 AA.
AC   Q6PFD5; Q6PDX0; Q6XBF2;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Disks large-associated protein 3;
DE            Short=DAP-3;
DE   AltName: Full=PSD-95/SAP90-binding protein 3;
DE   AltName: Full=SAP90/PSD-95-associated protein 3;
DE            Short=SAPAP3;
GN   Name=Dlgap3; Synonyms=Dap3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ICR;
RX   PubMed=15024750; DOI=10.1002/cne.20060;
RA   Welch J.M., Wang D., Feng G.;
RT   "Differential mRNA expression and protein localization of the
RT   SAP90/PSD-95-associated proteins (SAPAPs) in the nervous system of the
RT   mouse.";
RL   J. Comp. Neurol. 472:24-39(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-394; SER-404;
RP   SER-407; SER-410 AND SER-414, AND MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58; SER-500; SER-930 AND
RP   SER-965, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
CC   -!- FUNCTION: May play a role in the molecular organization of
CC       synapses and neuronal cell signaling. Could be an adapter protein
CC       linking ion channel to the subsynaptic cytoskeleton. May induce
CC       enrichment of PSD-95/SAP90 at the plasma membrane.
CC   -!- SUBUNIT: Interacts with DLG4/PSD-95 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC       Cell junction, synapse, postsynaptic cell membrane, postsynaptic
CC       density. Cell junction, synapse. Note=Postsynaptic density of
CC       neuronal cells.
CC   -!- TISSUE SPECIFICITY: Highly expressed in central and peripherical
CC       nervous system (at protein level).
CC   -!- SIMILARITY: Belongs to the SAPAP family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AY243848; AAO89219.2; -; mRNA.
DR   EMBL; BC057615; AAH57615.1; -; mRNA.
DR   EMBL; BC058433; AAH58433.1; -; mRNA.
DR   IPI; IPI00134997; -.
DR   RefSeq; NP_941020.1; NM_198618.4.
DR   UniGene; Mm.331885; -.
DR   ProteinModelPortal; Q6PFD5; -.
DR   MINT; MINT-4789697; -.
DR   STRING; Q6PFD5; -.
DR   PhosphoSite; Q6PFD5; -.
DR   PRIDE; Q6PFD5; -.
DR   Ensembl; ENSMUST00000046659; ENSMUSP00000039724; ENSMUSG00000042388.
DR   Ensembl; ENSMUST00000106094; ENSMUSP00000101700; ENSMUSG00000042388.
DR   GeneID; 242667; -.
DR   KEGG; mmu:242667; -.
DR   UCSC; uc008uuo.1; mouse.
DR   CTD; 242667; -.
DR   MGI; MGI:3039563; Dlgap3.
DR   GeneTree; ENSGT00550000074473; -.
DR   HOGENOM; HBG444624; -.
DR   HOVERGEN; HBG018957; -.
DR   InParanoid; Q6PFD5; -.
DR   OMA; GFHTLPY; -.
DR   OrthoDB; EOG4STS3Z; -.
DR   PhylomeDB; Q6PFD5; -.
DR   NextBio; 385480; -.
DR   ArrayExpress; Q6PFD5; -.
DR   Bgee; Q6PFD5; -.
DR   CleanEx; MM_DAP3; -.
DR   Genevestigator; Q6PFD5; -.
DR   GermOnline; ENSMUSG00000042388; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0001540; F:beta-amyloid binding; IDA:MGI.
DR   GO; GO:0007267; P:cell-cell signaling; IEA:InterPro.
DR   InterPro; IPR005026; GKAP.
DR   Pfam; PF03359; GKAP; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Synapse.
FT   CHAIN         1    977       Disks large-associated protein 3.
FT                                /FTId=PRO_0000174295.
FT   COMPBIAS    222    233       Poly-His.
FT   MOD_RES      58     58       Phosphoserine.
FT   MOD_RES     394    394       Phosphoserine.
FT   MOD_RES     404    404       Phosphoserine.
FT   MOD_RES     407    407       Phosphoserine.
FT   MOD_RES     410    410       Phosphoserine.
FT   MOD_RES     414    414       Phosphoserine.
FT   MOD_RES     500    500       Phosphoserine.
FT   MOD_RES     930    930       Phosphoserine.
FT   MOD_RES     965    965       Phosphoserine.
FT   CONFLICT    436    436       N -> S (in Ref. 1; AAO89219).
SQ   SEQUENCE   977 AA;  105873 MW;  26665D623D49E4C3 CRC64;
     MRGYHGDRGS HPRPARFADQ QHMDVGPAAR APYLLGSREA FSTEPRFCAP RAGLGHLSPE
     GPLSLSEGPS SVGPEGGPGG VGAGGGSSTF PRMYPGQGPF DTCEDCVGHP QGKGATRLPP
     TLLDQFEKQL PVQQDGFHTL PYQRGPAGPG PGPGSGAAPE ARSESPSRIR HLVHSVQKLF
     AKSHSLEAPG KRDYNGPKAD GRGSSGGDSY SGPGSGGTPT SHHHHHHHHH HHHQSRHGKR
     SKSKDRKGDG RHQTKATGWW SSDDNLDSDS GFLGGRPPGE PGGPFCLDAP DGSYRDLSFK
     GRSGGSEGRC LACTGMSMSL DGQSVKRSAW HTMMVSQGRD GYPGAGPGKG LLGPETKAKA
     RTYHYLQVPQ DDWGGYPTGG KDGEIPCRRM RSGSYIKAMG DEESGDSDGS PKTSPKALAR
     RFASRRSSSV DTARINCCVP PRIHPRSSIP GYSRSLTTGQ LSEEFNQQLE AVCGSVFGEL
     ESQAVDALDL PGCFRMRSHS YLRAIQAGCS QDDDCLPLLA APASVSGRPG SSFNFRKAPP
     PIPPGSQAPP RISITAQSST DSAHESFTAA EGPARRCSSA DGLDGPTMGA RTLELAPVPP
     RASPKPPTLI IKTIPGREEL RSLARQRKWR PSIGVQVETI SDSDTENRSR REFHSIGVQV
     EEDKRRARFK RSNSVTAGVQ ADLELEGLAG LATVATEDKA LQFGRSFQRH ASEPQPGPRA
     PTYSVFRTVH TQGQWAYREG YPLPYEPPAT DGSPGPTPVP APGPGSGRRD SWMERGSRSL
     PDSGRTSPCP RDGEWFIKML RAEVEKLEHW CQQMEREAED YELPEEILEK IRSAVGSTQL
     LLSQKVQQFF RLCQQSLDPT AFPVPTFQDL AGFWDLLQLS IEDVTLKFLE LQQLKANSWK
     LLEPKEEKKV PPPIPKKPSR GRGVPVKERS LDSVDRQRQE ARKRLLAAKR AASFRHSSAT
     ESADSIEIYI PEAQTRL
//
ID   TEFF1_MOUSE             Reviewed;         372 AA.
AC   Q6PFE7; A2AJN3; Q8BRP7; Q8C536; Q9JJS1;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Tomoregulin-1;
DE            Short=TR-1;
DE   AltName: Full=M7365;
DE   AltName: Full=Transmembrane protein with EGF-like and one follistatin-like domain;
DE   Flags: Precursor;
GN   Name=Tmeff1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 28-372 (ISOFORM 2), TISSUE SPECIFICITY,
RP   AND DEVELOPMENTAL STAGE.
RC   TISSUE=Brain;
RX   MEDLINE=20480371; PubMed=11025219; DOI=10.1016/S0925-4773(00)00426-3;
RA   Eib D.W., Holling T.M., Zwijsen A., Dewulf N., de Groot E.,
RA   van den Eijnden-van Raaij A.J.M., Huylebroeck D., Martens G.J.M.;
RT   "Expression of the follistatin/EGF-containing transmembrane protein
RT   M7365 (tomoregulin-1) during mouse development.";
RL   Mech. Dev. 97:167-171(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 118-372 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 125-372 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=11165370; DOI=10.1016/S0169-328X(00)00257-6;
RA   Kanemoto N., Horie M., Omori K., Nishino N., Kondo M., Noguchi K.,
RA   Tanigami A.;
RT   "Expression of TMEFF1 mRNA in the mouse central nervous system:
RT   precise examination and comparative studies of TMEFF1 and TMEFF2.";
RL   Brain Res. Mol. Brain Res. 86:48-55(2001).
RN   [6]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=11404089; DOI=10.1016/S0925-4773(01)00362-8;
RA   Morais da Silva S., Gates P.B., Eib D.W., Martens G.J.M.,
RA   Brockes J.P.;
RT   "The expression pattern of tomoregulin-1 in urodele limb regeneration
RT   and mouse limb development.";
RL   Mech. Dev. 104:125-128(2001).
CC   -!- FUNCTION: May inhibit NODAL and BMP signaling during neural
CC       patterning (By similarity).
CC   -!- SUBUNIT: May interact with ST14 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6PFE7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PFE7-2; Sequence=VSP_024960;
CC       Name=3;
CC         IsoId=Q6PFE7-3; Sequence=VSP_024960, VSP_024961;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, neurointermediate lobe,
CC       pars distalis, pancreas, ovary and testis.
CC   -!- DEVELOPMENTAL STAGE: At E8.5, highly expressed in the first
CC       branchial arch, somites, splanchnic mesoderm and ventral foregut
CC       epithelium. At E9.5, highly expressed in motor neurons and
CC       superficial neurons from the neural tube, and in the dorsal part
CC       of diencephalon and mesencephalon. At E11.5 and E12.5, expressed
CC       in limbs. At E15.5, highly expressed in brain and spinal cord.
CC   -!- SIMILARITY: Belongs to the tomoregulin family.
CC   -!- SIMILARITY: Contains 1 EGF-like domain.
CC   -!- SIMILARITY: Contains 2 Kazal-like domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB90827.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL807771; CAM15043.1; -; Genomic_DNA.
DR   EMBL; AL772151; CAM15043.1; JOINED; Genomic_DNA.
DR   EMBL; AL807771; CAM15044.1; -; Genomic_DNA.
DR   EMBL; AL772151; CAM15044.1; JOINED; Genomic_DNA.
DR   EMBL; AL772151; CAM20710.1; -; Genomic_DNA.
DR   EMBL; AL807771; CAM20710.1; JOINED; Genomic_DNA.
DR   EMBL; AL772151; CAM20711.1; -; Genomic_DNA.
DR   EMBL; AL807771; CAM20711.1; JOINED; Genomic_DNA.
DR   EMBL; BC057598; AAH57598.1; -; mRNA.
DR   EMBL; AJ400622; CAB90827.1; ALT_INIT; mRNA.
DR   EMBL; AK043792; BAC31655.1; -; mRNA.
DR   EMBL; AK079633; BAC37709.1; -; mRNA.
DR   IPI; IPI00420857; -.
DR   IPI; IPI00648679; -.
DR   IPI; IPI00845529; -.
DR   RefSeq; NP_067411.1; NM_021436.2.
DR   UniGene; Mm.422686; -.
DR   HSSP; P00995; 1HPT.
DR   ProteinModelPortal; Q6PFE7; -.
DR   SMR; Q6PFE7; 50-228, 265-307.
DR   STRING; Q6PFE7; -.
DR   MEROPS; I01.978; -.
DR   PRIDE; Q6PFE7; -.
DR   Ensembl; ENSMUST00000030032; ENSMUSP00000030032; ENSMUSG00000028347.
DR   Ensembl; ENSMUST00000107703; ENSMUSP00000103331; ENSMUSG00000028347.
DR   GeneID; 230157; -.
DR   KEGG; mmu:230157; -.
DR   UCSC; uc008svk.1; mouse.
DR   CTD; 230157; -.
DR   MGI; MGI:1926810; Tmeff1.
DR   eggNOG; roNOG15275; -.
DR   GeneTree; ENSGT00530000062996; -.
DR   HOVERGEN; HBG053816; -.
DR   OMA; RCESGYT; -.
DR   OrthoDB; EOG41NTMT; -.
DR   PhylomeDB; Q6PFE7; -.
DR   NextBio; 458689; -.
DR   ArrayExpress; Q6PFE7; -.
DR   Bgee; Q6PFE7; -.
DR   Genevestigator; Q6PFE7; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR002350; Prot_inh_Kazal.
DR   InterPro; IPR011497; Prot_Inh_Kazal_2.
DR   Pfam; PF07648; Kazal_2; 2.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00280; KAZAL; 2.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS51465; KAZAL_2; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Developmental protein;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     35       Potential.
FT   CHAIN        36    372       Tomoregulin-1.
FT                                /FTId=PRO_0000286057.
FT   TOPO_DOM     36    322       Extracellular (Potential).
FT   TRANSMEM    323    343       Helical; (Potential).
FT   TOPO_DOM    344    372       Cytoplasmic (Potential).
FT   DOMAIN       85    137       Kazal-like 1.
FT   DOMAIN      176    229       Kazal-like 2.
FT   DOMAIN      263    303       EGF-like.
FT   COMPBIAS     42     45       Poly-Gly.
FT   CARBOHYD     55     55       N-linked (GlcNAc...) (Potential).
FT   DISULFID    267    280       By similarity.
FT   DISULFID    275    291       By similarity.
FT   DISULFID    293    302       By similarity.
FT   VAR_SEQ     146    146       G -> GA (in isoform 2 and isoform 3).
FT                                /FTId=VSP_024960.
FT   VAR_SEQ     251    252       Missing (in isoform 3).
FT                                /FTId=VSP_024961.
FT   CONFLICT    235    235       L -> S (in Ref. 4; CAB90827).
FT   CONFLICT    241    241       D -> P (in Ref. 4; CAB90827).
FT   CONFLICT    244    244       Q -> L (in Ref. 4; CAB90827).
FT   CONFLICT    370    370       R -> K (in Ref. 4; CAB90827).
SQ   SEQUENCE   372 AA;  40114 MW;  BB3DA6710B78A530 CRC64;
     MGAQAPLRLP AAPPLAVCGY TSVLLLFAFC LPGSRASNQP AGGGGDCPGG RGKSNCSELN
     LRESDIRVCD ESSCKYGGVC KEDGDGLKCA CQFQCHTNYI PVCGSNGDTY QNECFLRRAA
     CKHQKDITVV ARGPCYSDNG SGSGEGEEEG SGAGAHRKHS KCGPCKYKAE CDEDAENVGC
     VCNIDCSGYS FNPVCASDGS SYNNPCFVRE ASCIKQEQID IRHLGHCTDT DDVSLLGKKD
     DGLQYRPDVK DAGDEREDVY IGSHMPCPEN LNGYCIHGKC EFIYSTQKAS CRCESGYTGQ
     HCEKTDFSIL YVVPSRQKLT HVLIAAIIGA VQIAIIVAIV MCITRKCPKN NRGRRQKQNL
     GHFTSDTSSR MV
//
ID   CG051_MOUSE             Reviewed;         833 AA.
AC   Q6PFX7; Q3UF51; Q8BNR4; Q8CCL6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 40.
DE   RecName: Full=Uncharacterized protein C7orf51 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Corpora quadrigemina, Olfactory bulb, and Sympathetic ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6PFX7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PFX7-2; Sequence=VSP_031748;
CC       Name=3;
CC         IsoId=Q6PFX7-3; Sequence=VSP_031747, VSP_031748;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC38036.1; Type=Frameshift; Positions=70, 102, 253, 276;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK032567; BAC27928.1; -; mRNA.
DR   EMBL; AK080821; BAC38036.1; ALT_FRAME; mRNA.
DR   EMBL; AK148980; BAE28710.1; -; mRNA.
DR   EMBL; BC057372; AAH57372.1; -; mRNA.
DR   IPI; IPI00341975; -.
DR   IPI; IPI00886276; -.
DR   IPI; IPI00886348; -.
DR   RefSeq; NP_780730.2; NM_175521.3.
DR   UniGene; Mm.74750; -.
DR   ProteinModelPortal; Q6PFX7; -.
DR   PhosphoSite; Q6PFX7; -.
DR   PRIDE; Q6PFX7; -.
DR   Ensembl; ENSMUST00000061789; ENSMUSP00000058217; ENSMUSG00000045348.
DR   Ensembl; ENSMUST00000118326; ENSMUSP00000113397; ENSMUSG00000045348.
DR   Ensembl; ENSMUST00000119498; ENSMUSP00000112894; ENSMUSG00000045348.
DR   GeneID; 243300; -.
DR   KEGG; mmu:243300; -.
DR   UCSC; uc009adq.1; mouse.
DR   MGI; MGI:2443880; 6430598A04Rik.
DR   GeneTree; ENSGT00450000040316; -.
DR   HOGENOM; HBG506885; -.
DR   HOVERGEN; HBG062871; -.
DR   InParanoid; Q6PFX7; -.
DR   OMA; RSPNTQL; -.
DR   OrthoDB; EOG483D49; -.
DR   PhylomeDB; Q6PFX7; -.
DR   NextBio; 385701; -.
DR   ArrayExpress; Q6PFX7; -.
DR   Bgee; Q6PFX7; -.
DR   CleanEx; MM_6430598A04RIK; -.
DR   Genevestigator; Q6PFX7; -.
PE   2: Evidence at transcript level;
KW   Alternative splicing.
FT   CHAIN         1    833       Uncharacterized protein C7orf51 homolog.
FT                                /FTId=PRO_0000320930.
FT   COMPBIAS    276    451       Pro-rich.
FT   COMPBIAS    613    617       Poly-Glu.
FT   VAR_SEQ       1    259       Missing (in isoform 3).
FT                                /FTId=VSP_031747.
FT   VAR_SEQ     644    645       TE -> K (in isoform 2 and isoform 3).
FT                                /FTId=VSP_031748.
SQ   SEQUENCE   833 AA;  87668 MW;  3BC67410155550AA CRC64;
     MNLLYRKTKL EWRQHKEEEA KRSSSKEAAP TGPVGPGAVP GPGVRVRDIA SLRRSLRMGF
     MTMPASQEHT PHPCRSTMAP RSLSCHSVGS MDSVGGGPGG GLTEDSSTRR PPAKPRRHPS
     TKLSMAGPGA ETPPSKKAGS QKPAPECRES SRKVPPQKPR RSPNTQLSVS FDESCAPAPS
     PRGANLPLQR LSRASRITGD LDAGAQEEEP VYIEMVGDVF RGGGRSGGGL AGPPLGSGGP
     TPPAAADSDS EDSEAIYEEM KYPLPEEAGD GRANGPPPLT APSPPQQTHI LQPHPHPHRR
     PASALPSRRD GTPTKTTPCE IPPPFPNLLQ HRPPLLAFPQ AKSASRAPGD GVSRLPVLCH
     SKEPAGSTPA PQVPARERET PPLPPPPPAA NLLLLGPSGR ARSHSTPLPP QGSGQTRGER
     ELPNSHSMIC PKAAGVPAAH PAPAALLPGP PKDKAVSYTM VYSAVKVTTH SVLPAGPPLG
     VGEPKTEEIS VLHGMLCASS RPPVPGKSSP HSGAMGSAAG VLHHRSCLAS PHSLPDPTGG
     SLTPLWTYPA TAAGLKRPPA YDSLKAGGVL NKGCGMGAPS PMVKIQLQEQ GTDGGAFASI
     SCAHVIASAG TPEEEEEMGA AFGAGWALQR KVLYGGRKAK EVDTEEDGAR AWNGSTEGPG
     KVEHEDRGPV PSGIPVRSQG AEGLLARIHH DRGGSRTALP VPCQTFPACH RNGDFTGGYR
     LGRSASTSGV RQAALHTPRP CSQPRDALSQ THPVLPLPLP PQPARERDGK LLEVIERKRC
     VCKEIKARHR PDRGLCKQES MPILPSWRRV PEPRKSGTPP CRRQHTVLWD TAI
//
ID   Q6PG01_MOUSE            Unreviewed;      1472 AA.
AC   Q6PG01;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-FEB-2011, entry version 29.
DE   SubName: Full=Pcnx protein;
DE   Flags: Fragment;
GN   Name=Pcnx;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC057333; AAH57333.1; -; mRNA.
DR   IPI; IPI00625314; -.
DR   UniGene; Mm.86584; -.
DR   ProteinModelPortal; Q6PG01; -.
DR   Ensembl; ENSMUST00000095565; ENSMUSP00000093221; ENSMUSG00000021140.
DR   UCSC; uc007ocs.1; mouse.
DR   MGI; MGI:1891924; Pcnx.
DR   GeneTree; ENSGT00390000013164; -.
DR   HOVERGEN; HBG045627; -.
DR   ArrayExpress; Q6PG01; -.
DR   Bgee; Q6PG01; -.
DR   Genevestigator; Q6PG01; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   InterPro; IPR007735; Pecanex.
DR   Pfam; PF05041; Pecanex_C; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   1472 AA;  164545 MW;  C24CE072B1F74D0F CRC64;
     DSRVCKDDGG KQKEGDVRPK SSSLIHRTTS AHKPGRRRTG KKRASSFDSS RHRDYVSFRG
     VSGTKPHSAV FGHDEDSSDQ SDLSRAPSIH SAHQFSSDSS SSATSHSCQS PEGKYGALKT
     KHGHRDRGTD SDHTHRAHPG PEGTTKKRAS RRTSSTSSAK TRARVLSLDS GTVACLNDSN
     RLLAPDSMKP LTTSKSDLEA KEGEVLDELS LLGRASQLET VTRSRNSLPS QVAFPEGEEQ
     DAATGGKFSS TLYETGGCDM SLVNFEPAAR RASNICDTDS HVSSSTSVRF YPHDMIRLNR
     LLTIDTDLLE QQDIDLSPDL AATYGPTEEA AQKVKHYYRF WVLPQLWIGI NFDRLTLLAL
     FDRNREILEN ILAVVLAILV AFLGSILLIQ GFFRDIWVFQ FCLVIASCQY SLLKSVQPDS
     SSPRHGHNRI IAYSRPVYFC LCCGLIWLLD YGSRNLTTSK FKLYGVTFTN PLVLLSARDL
     VIVFTLCFPI VFFIGLLPQV NTFVMYLCEQ LDIHIFGGNA TTSLLAALYS FLCSIVAVAL
     LYGLCYGALR DSWDGQHVPV LFSVFCGLLV AVSYHLSRQS SDPSVLFSLM QSKIFPKADE
     KNPEDPLSEV KDPLPEKLSN SVSERLQSDL VVCVIIGVLY FAIHVSTVFT ALQPALKYVL
     YALVGVVGLV THYVLPQVRK QLPWHCFSRP LLRTAEHSQY EVRNAATMMW FEKLHVWLLF
     VEKNIIYPLI VLNELSSSAE TIASPKKLDT ELGALMITIA GLKLLRSSFS SPTYQYITVI
     FTVLFFKFDY EAFSETMLLD LFFMSILFSK LWELLYKLQF VYTYVAPWQI TWGSAFHAFA
     QPFAVPHSAM LFVQAIVSAF FSTPLNPFLG SAIFITSYVR PVKFWERDYN TKRVDHSNTR
     LASQLDRNPG SDDNNLNSIF YEHLTRSLQH SLCGDLLLGR WGNYSTGDCF ILASDYLNAL
     VHLIEIGNGL VTFQLRGLEF RGTYCQQREV EAITEGVEED EGFCCCEPGH VPHVLSFNAA
     FGQRWLAWEV VVTKYILEGY SITDNSAASM LQVFDLRRVL TTYYVKGIIY YVTTSSKLEE
     WLANETMQEG LRLCADRNYV DVDPTFNPNI DEDYDHRLAG ISRESFCVIY LSWIEYCSSR
     RAKPLDVDKD SSLVTLCYGL CVLGRRALGT ASHHMSSNLE SFLYGLHALF KGDFRISSVR
     DEWIFADMEL LRKVVVPGIR MSIKLHQDHF TSPDEYDDPT VLYEAIVSHE KNLVIAHEGD
     PAWRSAVLAN SPSLLALRHV MDDGTNEYKI IMLNRRYLSF RVIKVNKECV RGLWAGQQQE
     LVFLRNRNPE RGSIQNAKQA LRNMINSSCD QPIGYPIFVS PLTTSYSDSH DQLKEILGGP
     ISLGNIRNFI VSTWHRLRKG CGAGCNSGGN IEDSDTGGGT SCPGNSAVTA SDPHNNVSQG
     STGHPGQGAG SGLHPPTTSY PPTLGNWRQN SV
//
ID   DHX29_MOUSE             Reviewed;        1365 AA.
AC   Q6PGC1; Q8BQJ4; Q8BT01; Q8C9B7; Q8C9H9;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=ATP-dependent RNA helicase Dhx29;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAH box protein 29;
GN   Name=Dhx29;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-469 AND 745-1365.
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: ATP-binding RNA helicase involved in translation
CC       initiation. Required for efficient initiation on mammalian mRNAs
CC       with structured 5'-UTRs by promoting efficient NTPase-dependent
CC       48S complex formation. Specifically binds to the 40S ribosome near
CC       the mRNA entrance. Does not possess a processive helicase activity
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC057112; AAH57112.1; -; mRNA.
DR   EMBL; BC082319; AAH82319.1; -; mRNA.
DR   EMBL; AK028342; BAC25894.1; -; mRNA.
DR   EMBL; AK042066; BAC31148.2; -; mRNA.
DR   EMBL; AK042497; BAC31274.2; -; mRNA.
DR   EMBL; AK049530; BAC33796.1; -; mRNA.
DR   IPI; IPI00410936; -.
DR   RefSeq; NP_766182.2; NM_172594.2.
DR   UniGene; Mm.35094; -.
DR   ProteinModelPortal; Q6PGC1; -.
DR   SMR; Q6PGC1; 550-1339.
DR   STRING; Q6PGC1; -.
DR   PhosphoSite; Q6PGC1; -.
DR   PRIDE; Q6PGC1; -.
DR   Ensembl; ENSMUST00000038574; ENSMUSP00000035244; ENSMUSG00000042426.
DR   GeneID; 218629; -.
DR   KEGG; mmu:218629; -.
DR   UCSC; uc007rwx.1; mouse.
DR   CTD; 218629; -.
DR   MGI; MGI:2145374; Dhx29.
DR   eggNOG; roNOG10837; -.
DR   HOGENOM; HBG715568; -.
DR   HOVERGEN; HBG081436; -.
DR   InParanoid; Q6PGC1; -.
DR   OMA; YWKCRVR; -.
DR   OrthoDB; EOG43FGW2; -.
DR   PhylomeDB; Q6PGC1; -.
DR   NextBio; 376359; -.
DR   ArrayExpress; Q6PGC1; -.
DR   Bgee; Q6PGC1; -.
DR   CleanEx; MM_DHX29; -.
DR   Genevestigator; Q6PGC1; -.
DR   GermOnline; ENSMUSG00000042426; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR011709; DUF1605.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF07717; DUF1605; 1.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Coiled coil; Cytoplasm; Helicase; Hydrolase;
KW   Initiation factor; Nucleotide-binding; Phosphoprotein;
KW   Protein biosynthesis.
FT   CHAIN         1   1365       ATP-dependent RNA helicase Dhx29.
FT                                /FTId=PRO_0000245536.
FT   DOMAIN      581    754       Helicase ATP-binding.
FT   DOMAIN      848   1025       Helicase C-terminal.
FT   NP_BIND     594    601       ATP (By similarity).
FT   COILED      264    309       Potential.
FT   MOTIF       701    704       DEAH box.
FT   COMPBIAS     10     53       Ala-rich.
FT   COMPBIAS    499    507       Poly-Gln.
FT   COMPBIAS    788    792       Poly-Glu.
FT   MOD_RES     190    190       Phosphoserine (By similarity).
FT   MOD_RES     198    198       Phosphoserine (By similarity).
SQ   SEQUENCE   1365 AA;  153975 MW;  4143A705CB092280 CRC64;
     MGGKNKKHKA PGAAAMRAAV SASRARSAEA GAVGEAQSKK PVARPAPAVP TGAREPRVKQ
     GPKIYSFNSA NDSGGSANLD KSILKVVINN KLEQRIIGVI NEHKKQNSDR GAISGRLSAK
     KLQDLYMALQ AFSFKTKDIE DAMTNTLLHG GDLHSALDWL CLNLSDDALP EGFSQEFEEQ
     QPKSRPKFQS VQIQATLSPP QQTKTKRQEE DPKIKPKKEE TTVEVNMKEW ILRYAEQQDE
     EEKGEGSKGL EEEEKFDPNQ RYLNLAARLL DAKEQAAAFK LEKNKQGQKE AQEKIRKFQR
     EMETLEDHPI FNPAIKISHQ QNEKKKPAPA TEAESALNLN LFEKSAAATE EEKGKKKEPH
     DVRNFDYTAR SWTGKSPKQF LIDWVRKNLP KSPNPSFEKV AVGRYWKCRV RVVRSEDDVL
     VVCPTILTED GMQAQHLGAT LALYRLVKGQ SVHQLLPPTY RDVWLEWSDE EKKREELNKM
     ETNKPRDLFI AKLLNKLKQQ QQQQQQQRPE SEKGGSEDPE ESWENLVSDE DLAALSLEPT
     SAEDLAPVRS LFRRLQSTPK YQRLLKERQQ LPVFKHRDSI VETLKRHRVV VVAGETGSGK
     STQVPHFLLE DLLLDECGAR KCNIVCTQPR RISAVSLATR VCEELGCESG PGGRNSLCGY
     QIRMESRASE STRLLYCTTG VLLRKLQEDG LLADVSHVIV DEVHERSVQS DFLLVILKEI
     LQKRSDLHLI LMSATVDSDK FSTYFTHCPI LRISGRSYPV EVFHLEDIVE ETGFVLEKDS
     EYCQKFLEEE EEITINVTSK AGGVKKYQEY IPVQSGASPE LNPFYQKYSS RTQHAILYMN
     PHKINLDLIL ELLVYLDKSP QFRNIEGAVL IFLPGLAHIQ QLYDLLSSDR RFYSERYQVI
     ALHSVLSTQD QAAAFMFPPP GVRKIVLATN IAETGITIPD VVFVIDTGRT KENKYHESSQ
     MSSLVETFVS KASALQRQGR AGRVRDGFCF RLYTRERFEG FLDYSVPEIL RVPLEELCLH
     IMKCDLGSPE DFLSKALDPP QLQVISNAMN LLRKIGACEP NEPKLTPLGQ HLAALPVNVK
     IGKMLIFGAI FGCLEPVATL AAVMTEKSPF ITPIGRKDEA DLAKSSLAVA DSDHLTIYNA
     YLGWKKAQQE GGFRSEISYC QRNFLNRTSL LTLEDVKQEL MKLVKAAGFS SSPSWEGRKG
     PQTLSFQDIA LLKAVLAAGL YDSVGKIMCT KSVDVTEKLA CMVETAQGKA QVHPSSVNRD
     LQTYGWLLYQ EKVRYTRVYL RETTLITPFP VLLFGGDIEV QHRERLLSVD GWIYFQAPVK
     IAVIFKQLRV LIDSVLRKKL ENPKMSLEND KILQIITELI KTENN
//
ID   SC6A7_MOUSE             Reviewed;         637 AA.
AC   Q6PGE7; Q80UM1;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Sodium-dependent proline transporter;
DE   AltName: Full=Solute carrier family 6 member 7;
GN   Name=Slc6a7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and ICR; TISSUE=Brain, and Trophoblast stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Terminates the action of proline by its high affinity
CC       sodium-dependent reuptake into presynaptic terminals (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF)
CC       (TC 2.A.22) family. SLC6A7 subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC050103; AAH50103.1; -; mRNA.
DR   EMBL; BC057070; AAH57070.1; -; mRNA.
DR   IPI; IPI00420909; -.
DR   RefSeq; NP_958741.1; NM_201353.1.
DR   UniGene; Mm.39846; -.
DR   ProteinModelPortal; Q6PGE7; -.
DR   SMR; Q6PGE7; 36-558.
DR   STRING; Q6PGE7; -.
DR   PhosphoSite; Q6PGE7; -.
DR   PRIDE; Q6PGE7; -.
DR   Ensembl; ENSMUST00000025520; ENSMUSP00000025520; ENSMUSG00000052026.
DR   GeneID; 240332; -.
DR   KEGG; mmu:240332; -.
DR   NMPDR; fig|10090.3.peg.4063; -.
DR   UCSC; uc008fbi.1; mouse.
DR   CTD; 240332; -.
DR   MGI; MGI:2147363; Slc6a7.
DR   eggNOG; maNOG05150; -.
DR   GeneTree; ENSGT00600000084044; -.
DR   HOGENOM; HBG702834; -.
DR   HOVERGEN; HBG071421; -.
DR   InParanoid; Q6PGE7; -.
DR   OMA; WNTELCL; -.
DR   OrthoDB; EOG46HG99; -.
DR   PhylomeDB; Q6PGE7; -.
DR   NextBio; 384558; -.
DR   ArrayExpress; Q6PGE7; -.
DR   Bgee; Q6PGE7; -.
DR   Genevestigator; Q6PGE7; -.
DR   GermOnline; ENSMUSG00000052026; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; IEA:InterPro.
DR   GO; GO:0005328; F:neurotransmitter:sodium symporter activity; IEA:InterPro.
DR   InterPro; IPR000175; Na/ntran_symport.
DR   PANTHER; PTHR11616; Na/ntran_symport; 1.
DR   Pfam; PF00209; SNF; 1.
DR   PRINTS; PR00176; NANEUSMPORT.
DR   PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR   PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
DR   PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid transport; Glycoprotein; Membrane;
KW   Neurotransmitter transport; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    637       Sodium-dependent proline transporter.
FT                                /FTId=PRO_0000214771.
FT   TOPO_DOM      1     45       Cytoplasmic (Potential).
FT   TRANSMEM     46     66       Helical; Name=1; (Potential).
FT   TRANSMEM     74     93       Helical; Name=2; (Potential).
FT   TRANSMEM    117    137       Helical; Name=3; (Potential).
FT   TOPO_DOM    138    214       Extracellular (Potential).
FT   TRANSMEM    215    233       Helical; Name=4; (Potential).
FT   TRANSMEM    242    259       Helical; Name=5; (Potential).
FT   TRANSMEM    295    312       Helical; Name=6; (Potential).
FT   TRANSMEM    324    345       Helical; Name=7; (Potential).
FT   TRANSMEM    378    397       Helical; Name=8; (Potential).
FT   TRANSMEM    425    443       Helical; Name=9; (Potential).
FT   TRANSMEM    459    479       Helical; Name=10; (Potential).
FT   TRANSMEM    500    519       Helical; Name=11; (Potential).
FT   TRANSMEM    538    556       Helical; Name=12; (Potential).
FT   TOPO_DOM    557    637       Cytoplasmic (Potential).
FT   CARBOHYD    182    182       N-linked (GlcNAc...) (Potential).
FT   CONFLICT     21     21       P -> S (in Ref. 1; AAH50103).
FT   CONFLICT    202    202       Q -> R (in Ref. 1; AAH50103).
SQ   SEQUENCE   637 AA;  71066 MW;  A122D5A6ED074680 CRC64;
     MKKLQEAHLR KPITPDLLMT PSDQGDVDLD VDFAADRGNW TGKLDFLLSC IGYCVGLGNV
     WRFPYRAYTN GGGAFLVPYF LMLAICGIPL FFLELSLGQF SSLGPLAVWK ISPLFKGAGA
     AMLLIVGLVA IYYNMIIAYV LFYLFASLTS NLPWEHCGNW WNTELCLEHR GPKSGNGVLP
     LNLSSTVSPS EEYWSRYVLH IQGSQGIGRP GEIRWNLCLC LLLAWVIVFL CILKGVKSSG
     KVVYFTATFP YLILLMLLVR GVTLPGAWKG IQFYLTPQFH HLLSSKVWIE AALQIFYSLG
     VGFGGLLTFA SYNTFHQNIY RDTFIVTLGN AITSILAGFA IFSVLGYMSQ ELGVPVDQVA
     KAGPGLAFVV YPQAMTMLPL SPFWSFLFFF MLLTLGLDSQ FAFLETIVTA VTDEFPYYLR
     PKKAVFSGLI CVAMYLMGLI LTTDGGMYWL VLLDDYSASF GLMVVVITTC LAVTRVYGIQ
     RFCRDIHMML GFKPGLYFRA CWLFLSPATL LALLVYSIVK YQPSEYGSYR FPAWAELLGI
     LMGLLSCLMI PAGMLVAVLR EEGSLWERLQ QASRPAMDWG PSLEENRTGM YVATLAGSQS
     PKPLMVHMRK YGGITSFENT AIEVDREIAE EEEESMM
//
ID   MED16_MOUSE             Reviewed;         828 AA.
AC   Q6PGF3;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 16;
DE   AltName: Full=Mediator complex subunit 16;
DE   AltName: Full=Thyroid hormone receptor-associated protein 5;
DE   AltName: Full=Thyroid hormone receptor-associated protein complex 95 kDa component;
DE            Short=Trap95;
DE   AltName: Full=Vitamin D3 receptor-interacting protein complex 92 kDa component;
DE            Short=DRIP92;
GN   Name=Med16; Synonyms=Thrap5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Component of the Mediator complex, a coactivator
CC       involved in the regulated transcription of nearly all RNA
CC       polymerase II-dependent genes. Mediator functions as a bridge to
CC       convey information from gene-specific regulatory proteins to the
CC       basal RNA polymerase II transcription machinery. Mediator is
CC       recruited to promoters by direct interactions with regulatory
CC       proteins and serves as a scaffold for the assembly of a functional
CC       preinitiation complex with RNA polymerase II and the general
CC       transcription factors (By similarity).
CC   -!- SUBUNIT: Component of the Mediator complex, which is composed of
CC       MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13,
CC       MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21,
CC       MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31,
CC       CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8
CC       subunits form a distinct module termed the CDK8 module. Mediator
CC       containing the CDK8 module is less active than Mediator lacking
CC       this module in supporting transcriptional activation. Individual
CC       preparations of the Mediator complex lacking one or more distinct
CC       subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and
CC       TRAP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 16 family.
CC   -!- SIMILARITY: Contains 5 WD repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC057056; AAH57056.1; -; mRNA.
DR   IPI; IPI00944127; -.
DR   UniGene; Mm.260089; -.
DR   UniGene; Mm.478651; -.
DR   ProteinModelPortal; Q6PGF3; -.
DR   SMR; Q6PGF3; 23-132.
DR   DIP; DIP-48408N; -.
DR   STRING; Q6PGF3; -.
DR   PRIDE; Q6PGF3; -.
DR   Ensembl; ENSMUST00000045844; ENSMUSP00000041768; ENSMUSG00000013833.
DR   Ensembl; ENSMUST00000105378; ENSMUSP00000101017; ENSMUSG00000013833.
DR   UCSC; uc007gak.1; mouse.
DR   MGI; MGI:2158394; Med16.
DR   GeneTree; ENSGT00390000003821; -.
DR   HOVERGEN; HBG054317; -.
DR   InParanoid; Q6PGF3; -.
DR   OrthoDB; EOG4HDSSV; -.
DR   NextBio; 375020; -.
DR   ArrayExpress; Q6PGF3; -.
DR   Bgee; Q6PGF3; -.
DR   CleanEx; MM_MED16; -.
DR   Genevestigator; Q6PGF3; -.
DR   GermOnline; ENSMUSG00000013833; Mus musculus.
DR   GO; GO:0016592; C:mediator complex; ISS:UniProtKB.
DR   GO; GO:0004872; F:receptor activity; ISS:UniProtKB.
DR   GO; GO:0046966; F:thyroid hormone receptor binding; ISS:UniProtKB.
DR   GO; GO:0030375; F:thyroid hormone receptor coactivator activity; ISS:UniProtKB.
DR   GO; GO:0016563; F:transcription activator activity; ISS:UniProtKB.
DR   GO; GO:0030521; P:androgen receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISS:UniProtKB.
DR   InterPro; IPR021665; Mediator_Med16.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
DR   Pfam; PF11635; Med16; 1.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00320; WD40; 2.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Activator; Nucleus; Repeat; Transcription; Transcription regulation;
KW   WD repeat.
FT   CHAIN         1    828       Mediator of RNA polymerase II
FT                                transcription subunit 16.
FT                                /FTId=PRO_0000051293.
FT   REPEAT       67    106       WD 1.
FT   REPEAT      198    240       WD 2.
FT   REPEAT      263    307       WD 3.
FT   REPEAT      621    662       WD 4.
FT   REPEAT      777    816       WD 5.
SQ   SEQUENCE   828 AA;  91772 MW;  C84E22E2782C0DE6 CRC64;
     MDLAYVCEWE KWAKSTYCPS LPLACAWSCR NLTAFTTDLR NDDQDLTHMI HILDTEHPWE
     VHSVSSGHSE AITCLEWDQS GSRLLSADAD GQIKCWSMAD HLANSWESSV GSQVEGDPIV
     ALSWLHNGVK LALHVEKSGA SSFGEKFSRV KFSPSLTLFG GKPMEGWIAV TVSGLVTVSL
     LKPSGQVLTS TESLCRLRGR VALADIAFTG GGNIVVAAAD GSSASPVKFY KVCVSVVSEK
     CRIDTEILPS LFMRCTTDPN RKDRFPAITH LKFLARDMSE QVLLCASSQT SSLVECWSLR
     KEGLPVNNIF QQISPVVGDK QPMILKWRIL SATNDLDRVS AVALPKLPIS LTNTDLKVAS
     DTQFYPGLGL ALAFQDGSVH MVHRLSLQTL AVFYSSAPRS LDEPALKRLR TTCPAVHFKA
     MQLSWTSLAL VGIDNHGKLS MLRISPSLGH PLEPKLALQH LLFLLEYCMV TGYDWWDILL
     HVQPGMVQSL VERLHEEYTR QKPALQQVLS TRILAMKASL CKLSPCTVAR VCDYHTKLFL
     MAITSTLKSL LRPHFLNTPD KSPGDRLAEI CAKITDVDID KVMINLKTEE FVLDMNTLQA
     LQQLLQWVGD FVLYLLVSLP NQGSPLRPGH SFLRDGTSLG MLRELMVVIR IWGLLKPSCL
     PVYTATSDTQ DSMSLLFRLL TKLWICCRDE GAASEPDEGL VDECCLLPSQ LLVPNLDWLP
     ASDGLVSRLQ PKQPLRLRFG RAPTLPSSTS TLQLDGLTRA PGQPKIDHLR RLHLGAYPTE
     ECKACTRCGC VTMLKSPNKT TAVTQWEQRW IKNCLCGGLW RRVPLSCS
//
ID   EXOC8_MOUSE             Reviewed;         716 AA.
AC   Q6PGF7;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Exocyst complex component 8;
DE   AltName: Full=Exocyst complex 84 kDa subunit;
GN   Name=Exoc8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-313, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
CC   -!- FUNCTION: Component of the exocyst complex involved in the docking
CC       of exocystic vesicles with fusion sites on the plasma membrane (By
CC       similarity).
CC   -!- SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3,
CC       EXOC4, EXOC5, EXOC6, EXOC7 and EXOC8. Interacts with the GTP-bound
CC       forms of RALA and RALB via its PH domain (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell projection, growth cone (By
CC       similarity). Note=Redistributes to growing neurites and growth
CC       cones during cell differentiation. Binds lipids with
CC       phosphatidylinositol-3,4,5-trisphosphate groups (By similarity).
CC   -!- SIMILARITY: Belongs to the EXO84 family.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC057052; AAH57052.1; -; mRNA.
DR   IPI; IPI00377299; -.
DR   RefSeq; NP_932771.1; NM_198103.2.
DR   UniGene; Mm.347360; -.
DR   UniGene; Mm.392449; -.
DR   ProteinModelPortal; Q6PGF7; -.
DR   SMR; Q6PGF7; 171-283.
DR   STRING; Q6PGF7; -.
DR   PhosphoSite; Q6PGF7; -.
DR   PRIDE; Q6PGF7; -.
DR   Ensembl; ENSMUST00000098312; ENSMUSP00000095915; ENSMUSG00000074030.
DR   GeneID; 102058; -.
DR   KEGG; mmu:102058; -.
DR   UCSC; uc009nxw.1; mouse.
DR   CTD; 102058; -.
DR   MGI; MGI:2142527; Exoc8.
DR   eggNOG; maNOG11263; -.
DR   GeneTree; ENSGT00390000015936; -.
DR   HOGENOM; HBG713746; -.
DR   HOVERGEN; HBG081489; -.
DR   InParanoid; Q6PGF7; -.
DR   OMA; EMKSCGV; -.
DR   OrthoDB; EOG4F4S9J; -.
DR   PhylomeDB; Q6PGF7; -.
DR   NextBio; 355252; -.
DR   ArrayExpress; Q6PGF7; -.
DR   Bgee; Q6PGF7; -.
DR   CleanEx; MM_EXOC8; -.
DR   Genevestigator; Q6PGF7; -.
DR   GermOnline; ENSMUSG00000074030; Mus musculus.
DR   GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR016159; Cullin_repeat-like_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR014812; Vps51.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF08700; Vps51; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF74788; Cullin_repeat-like; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cytoplasm; Exocytosis; Phosphoprotein;
KW   Protein transport; Transport.
FT   CHAIN         1    716       Exocyst complex component 8.
FT                                /FTId=PRO_0000227551.
FT   DOMAIN      173    273       PH.
FT   MOD_RES      15     15       Phosphoserine (By similarity).
FT   MOD_RES     313    313       Phosphothreonine.
SQ   SEQUENCE   716 AA;  81035 MW;  E512707F1DEF36E1 CRC64;
     MSDSGASRLR RQLESGGFEA RLYVKQLSQQ SDGDRDLQEH RQRVQALAEE TAQNLKRNVY
     QNYRQFIETA REISYLESEM YQLSHLLTEQ KSSLESIPLA LLPAAAAGAS AGEDTAGAGP
     RERGAVQAGF LPGPAGVPRE GSGTGEEGKQ RTLTTLLEKV EGCRDLLETP GQYLVYNGDL
     VEYDADHMAQ LQRVHGFLMN DCLLVATWLP QRRGMYRYNA LYPLDRLAVV NVKDNPPMKD
     MFKLLMFPES RIFQAENAKI KREWLEVLEE TKRALSDKRR REQEEAAAPR APPPVTSKGS
     NPFEDEDDEE LATPEAEEEK VDLSMEWIQE LPEDLDVCIA QRDFEGAVDL LDKLNHYLED
     KPSPPPVKEL RAKVDERVRQ LTEVLVFELS PDRSLRGGPK ATRRAVSQLI RLGQCTKACE
     LFLRNRAAAV HTAIRQLRIE GATLLYIHKL CHVFFTSLLE TAREFETDFA GTDSGCYSAF
     VVWARSAMGM FVDAFSKQVF DSKESLSTAA ECVKVAKEHC QQLGEIGLDL TFIIHALLVK
     DIQGALHSYK EIIIEATKHR NSEEMWRRMN LMTPEALGKL KEEMKSCGVS NFEQYTGDDC
     WVNLSYTVVA FTKQTMGFLE EALKLYFPEL HMVLLESLVE IILVAVQHVD YSLRCEQDPE
     KKAFIRQNAS FLYETVLPVV ERRFEEGVGK PAKQLQDLRN ASRLLRVNPE STTSVV
//
ID   GMIP_MOUSE              Reviewed;         971 AA.
AC   Q6PGG2; Q6P9S3;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=GEM-interacting protein;
DE            Short=GMIP;
GN   Name=Gmip;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-436, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Stimulates, in vitro and in vivo, the GTPase activity of
CC       RhoA (By similarity).
CC   -!- SUBUNIT: Interacts with GEM through its N-terminal (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6PGG2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PGG2-2; Sequence=VSP_013190, VSP_013191;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; BC057037; AAH57037.1; -; mRNA.
DR   EMBL; BC060628; AAH60628.1; -; mRNA.
DR   IPI; IPI00377290; -.
DR   IPI; IPI00554841; -.
DR   RefSeq; NP_932769.1; NM_198101.1.
DR   UniGene; Mm.324305; -.
DR   ProteinModelPortal; Q6PGG2; -.
DR   SMR; Q6PGG2; 491-756.
DR   STRING; Q6PGG2; -.
DR   PhosphoSite; Q6PGG2; -.
DR   PRIDE; Q6PGG2; -.
DR   Ensembl; ENSMUST00000036074; ENSMUSP00000045676; ENSMUSG00000036246.
DR   GeneID; 78816; -.
DR   KEGG; mmu:78816; -.
DR   UCSC; uc009lxs.1; mouse.
DR   UCSC; uc009lxt.1; mouse.
DR   CTD; 78816; -.
DR   MGI; MGI:1926066; Gmip.
DR   eggNOG; roNOG09582; -.
DR   GeneTree; ENSGT00600000084287; -.
DR   HOGENOM; HBG446219; -.
DR   HOVERGEN; HBG052839; -.
DR   InParanoid; Q6PGG2; -.
DR   OMA; EQKRMNE; -.
DR   OrthoDB; EOG4BK534; -.
DR   NextBio; 349584; -.
DR   ArrayExpress; Q6PGG2; -.
DR   Bgee; Q6PGG2; -.
DR   CleanEx; MM_GMIP; -.
DR   Genevestigator; Q6PGG2; -.
DR   GermOnline; ENSMUSG00000036246; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; GTPase activation; Metal-binding;
KW   Phosphoprotein; Zinc; Zinc-finger.
FT   CHAIN         1    971       GEM-interacting protein.
FT                                /FTId=PRO_0000056726.
FT   DOMAIN      553    756       Rho-GAP.
FT   ZN_FING     492    536       Phorbol-ester/DAG-type.
FT   COMPBIAS    256    261       Poly-Arg.
FT   COMPBIAS    361    366       Poly-Pro.
FT   MOD_RES      75     75       Phosphoserine.
FT   MOD_RES     235    235       Phosphoserine (By similarity).
FT   MOD_RES     238    238       Phosphoserine (By similarity).
FT   MOD_RES     247    247       Phosphoserine (By similarity).
FT   MOD_RES     433    433       Phosphoserine (By similarity).
FT   MOD_RES     436    436       Phosphoserine.
FT   MOD_RES     440    440       Phosphoserine (By similarity).
FT   MOD_RES     924    924       Phosphoserine (By similarity).
FT   VAR_SEQ     824    839       LATLQRDQREEEVEDT -> VGISLPCRCGEGPVCV (in
FT                                isoform 2).
FT                                /FTId=VSP_013190.
FT   VAR_SEQ     840    971       Missing (in isoform 2).
FT                                /FTId=VSP_013191.
SQ   SEQUENCE   971 AA;  107545 MW;  0ACA8B6048BD97F2 CRC64;
     MDSAETELTP APEGRKRYSD IFQSLDNLEI SLGNVTFDPL AGDPVRREDL EPDKADTATV
     VTEENSEASS WRDLSPEGPA PLTEEELDLR LIRTKGGVDA ALEYAKAWSR YAKELLAWTD
     KRANYELEFA KSIMKLAEAG KVSILQQSQM PLQYIYTLFL EHDLSLGALA LETVAQQKRD
     YYQPLAAKRM EIEKWRKEFK EQWLKEQKRM NEAVQALRRS ELQYIQRRED LRARSQGSPE
     DPPSQASPGS NKQQERRRRS REEAQAKAHE AEALYQACVR EANSRQQDLE TTKRRIVSHV
     RKLVLQGDEV LRRVTLGLFE LRGAQAERGP RSFSALAECC VPFEPGQRYQ EFVRTLQPGA
     PPPPSPAFCF QEFTAVVHSF PQDTKKKFSG PLPPRLEEEG SPEPGPWEVA SLGSQGIPGS
     DVDSVGGGSE SRSLDSPTSS PGAGARRLVK ASSTGTESSD DFEERDPDLG DGIENGVGSP
     FRKWTLSTAA QTHRLRRLRG PAKCRECEAF MVSGTECEEC FLTCHKRCLE TLLILCGHRR
     LPARMSLFGV DFLQLPRDFP EEVPFVITRC TAEIEHRALG LQGIYRVSGS RVRVERLCQA
     FENGRALVEL SGNSPHDITS VLKRFLQELT DPVVPFHLYD AFISLAKTLH ADPGDDPGTP
     NPSPEIIRSL KTLLVQLPDS NYSTLRHLVA HLFRVAARFE ENKMSANNLG IVFGPTLLRP
     PDGPRATGAS PVACLLDSGH QAQLVEFLIV HYEQIFGMDE LPLASEPLTQ DPGLAPACLE
     SSPQHPASLL AQDTQPLTIA LDSSPDPKHH SALEKCPEVT PPELATLQRD QREEEVEDTR
     DGAGDGSSHC PEDLALGAQS RGHFSRQPVK YSRGGVRPVT HQLSSLALVA SKLCEETPVT
     VSAVHRGSLR VRGLGPAAAC PEGSPLRRNP LPKHFEITQE TARLLSKLNS DAVSRTTCCA
     DPEPEESEEH L
//
ID   Q6PGG8_MOUSE            Unreviewed;       560 AA.
AC   Q6PGG8;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 44.
DE   SubName: Full=Tdrkh protein;
GN   Name=Tdrkh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 2 KH domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC057030; AAH57030.1; -; mRNA.
DR   IPI; IPI00330464; -.
DR   UniGene; Mm.331198; -.
DR   UniGene; Mm.470795; -.
DR   ProteinModelPortal; Q6PGG8; -.
DR   SMR; Q6PGG8; 54-208, 331-425.
DR   Ensembl; ENSMUST00000045245; ENSMUSP00000041002; ENSMUSG00000041912.
DR   MGI; MGI:1919884; Tdrkh.
DR   eggNOG; roNOG05603; -.
DR   HOVERGEN; HBG055309; -.
DR   InParanoid; Q6PGG8; -.
DR   ArrayExpress; Q6PGG8; -.
DR   Bgee; Q6PGG8; -.
DR   Genevestigator; Q6PGG8; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR004088; KH_type_1.
DR   InterPro; IPR018111; KH_type_1_subgr.
DR   InterPro; IPR008191; Maternal_tudor.
DR   InterPro; IPR002999; Tudor.
DR   InterPro; IPR018351; Tudor_subgroup.
DR   Pfam; PF00013; KH_1; 2.
DR   Pfam; PF00567; TUDOR; 1.
DR   SMART; SM00322; KH; 2.
DR   SMART; SM00333; TUDOR; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 2.
DR   PROSITE; PS50304; TUDOR; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   560 AA;  62150 MW;  C7AB710F56D336B7 CRC64;
     MSTERTSWTN LSTIQKIALG LGIPASATVA YILYRRYRES REERLTFVGE DDIEIEMRVP
     QEAVKLIIGR QGANIKQLRK QTGARIDVDT EDVGDERVLL ISGFPVQVCK AKAAIHQILT
     ENTPVFEQLS VPQRSVGRII GRGGETIRSI CKASGAKITC DKESEGTLLL SRLIKISGTQ
     KEVAAAKHLI LEKVSEDEEL RKRIAHSAET RVPRKQPISV RREEVTEPGG AGEAALWKNT
     NSSMGPATPL EVPLRKGGGD MVVVGPKEGS WEKPNDDSFQ NSGAQSSPET SMFEIPSPDF
     SFHADEYLEV YVSSSEHPNH FWIQIIGSRS LQLDKLVSEM TQHYENSLPE DLTVHVGDIV
     AAPLSTNGSW YRARVLGTLE NGNLDLYFVD FGDNGDCALK DLRALRSDFL SLPFQAIECS
     LARIAPTGEE WEEEALDEFD RLTHCADWKP LVAKISSYVQ TGISTWPKIY LYDTSDEKKL
     DIGLELVRKG YAVELPEDME ENRTVPNMLK DMATETDDSL ASILTETKKS PEEMPHTLSC
     LSLSEAASMS GDDNLEDDLF
//
ID   Q6PGJ3_MOUSE            Unreviewed;      1259 AA.
AC   Q6PGJ3;
DT   25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2004, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   SubName: Full=L1 cell adhesion molecule;
GN   Name=L1cam; ORFNames=RP23-373N8.1-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Holt K.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC056988; AAH56988.1; -; mRNA.
DR   EMBL; AL672094; CAM22467.1; -; Genomic_DNA.
DR   IPI; IPI00785371; -.
DR   RefSeq; NP_032504.3; NM_008478.3.
DR   UniGene; Mm.260568; -.
DR   HSSP; P11362; 1EVT.
DR   ProteinModelPortal; Q6PGJ3; -.
DR   SMR; Q6PGJ3; 34-1003.
DR   STRING; Q6PGJ3; -.
DR   Ensembl; ENSMUST00000102871; ENSMUSP00000099935; ENSMUSG00000031391.
DR   GeneID; 16728; -.
DR   KEGG; mmu:16728; -.
DR   UCSC; uc009tmv.1; mouse.
DR   CTD; 16728; -.
DR   MGI; MGI:96721; L1cam.
DR   HOVERGEN; HBG000144; -.
DR   InParanoid; Q6PGJ3; -.
DR   OMA; YRVQWRP; -.
DR   NextBio; 290518; -.
DR   PMAP-CutDB; Q6PGJ3; -.
DR   ArrayExpress; Q6PGJ3; -.
DR   Bgee; Q6PGJ3; -.
DR   Genevestigator; Q6PGJ3; -.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:MGI.
DR   GO; GO:0043195; C:terminal button; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR   GO; GO:0005178; F:integrin binding; IDA:MGI.
DR   GO; GO:0043621; F:protein self-association; IPI:MGI.
DR   GO; GO:0033691; F:sialic acid binding; IDA:MGI.
DR   GO; GO:0007411; P:axon guidance; IDA:MGI.
DR   GO; GO:0007166; P:cell surface receptor linked signaling pathway; IDA:MGI.
DR   GO; GO:0033631; P:cell-cell adhesion mediated by integrin; IMP:MGI.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion; IMP:MGI.
DR   GO; GO:0007156; P:homophilic cell adhesion; IMP:MGI.
DR   GO; GO:0034109; P:homotypic cell-cell adhesion; IMP:MGI.
DR   GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:MGI.
DR   GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IDA:MGI.
DR   GO; GO:0022409; P:positive regulation of cell-cell adhesion; IMP:MGI.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 11.
DR   Pfam; PF00041; fn3; 4.
DR   Pfam; PF07679; I-set; 5.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 5.
DR   SUPFAM; SSF49265; FN_III-like; 4.
DR   PROSITE; PS50853; FN3; 5.
DR   PROSITE; PS50835; IG_LIKE; 6.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   1259 AA;  140917 MW;  25743C039892A22F CRC64;
     MVVMLRYVWP LLLCSPCLLI QIPDEYKGHH VLEPPVITEQ SPRRLVVFPT DDISLKCEAR
     GRPQVEFRWT KDGIHFKPKE ELGVVVHEAP YSGSFTIEGN NSFAQRFQGI YRCYASNKLG
     TAMSHEIQLV AEGAPKWPKE TVKPVEVEEG ESVVLPCNPP PSAAPLRIYW MNSKILHIKQ
     DERVSMGQNG DLYFANVLTS DNHSDYICNA HFPGTRTIIQ KEPIDLRVKP TNSMIDRKPR
     LLFPTNSSSR LVALQGQSLI LECIAEGFPT PTIKWLHPSD PMPTDRVIYQ NHNKTLQLLN
     VGEEDDGEYT CLAENSLGSA RHAYYVTVEA APYWLQKPQS HLYGPGETAR LDCQVQGRPQ
     PEITWRINGM SMETVNKDQK YRIEQGSLIL SNVQPSDTMV TQCEARNQHG LLLANAYIYV
     VQLPARILTK DNQTYMAVEG STAYLLCKAF GAPVPSVQWL DEEGTTVLQD ERFFPYANGT
     LSIRDLQAND TGRYFCQAAN DQNNVTILAN LQVKEATQIT QGPRSAIEKK GARVTFTCQA
     SFDPSLQASI TWRGDGRDLQ ERGDSDKYFI EDGKLVIQSL DYSDQGNYSC VASTELDEVE
     SRAQLLVVGS PGPVPHLELS DRHLLKQSQV HLSWSPAEDH NSPIEKYDIE FEDKEMAPEK
     WFSLGKVPGN QTSTTLKLSP YVHYTFRVTA INKYGPGEPS PVSETVVTPE AAPEKNPVDV
     RGEGNETNNM VITWKPLRWM DWNAPQIQYR VQWRPQGKQE TWREQTVSDP FLVVSNTSTF
     VPYEIKVQAV NNQGKGPEPQ VTIGYSGEDY PQVSPELEDI TIFNSSTVLV RWRPVDLAQV
     KGHLKGYNVT YWWKGSQRKH SKRHIHKSHI VVPANTTSAI LSGLRPYSSY HVEVQAFNGR
     GLGPASEWTF STPEGVPGHP EALHLECQSD TSLLLHWQPP LSHNGVLTGY LLSYHPVEGE
     SKEQLFFNLS DPELRTHNLT NLNPDLQYRF QLQATTQQGP GEAIVREGGT MALFGKPDFG
     NISATAGENY SVVSWVPRKG QCNFRFHILF KALPEGKVSP DHQPQPQYVS YNQSSYTQWN
     LQPDTKYEIH LIKEKVLLHH LDVKTNGTGP VRVSTTGSFA SEGWFIAFVS AIILLLLILL
     ILCFIKRSKG GKYSVKDKED TQVDSEARPM KDETFGEYRS LESDNEEKAF GSSQPSLNGD
     IKPLGSDDSL ADYGGSVDVQ FNEDGSFIGQ YSGKKEKEAA GGNDSSGATS PINPAVALE
//
ID   FAM21_MOUSE             Reviewed;        1334 AA.
AC   Q6PGL7; Q3TQ99; Q80TW8; Q80UQ4; Q8CAP0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   RecName: Full=WASH complex subunit FAM21;
GN   Name=Fam21; Synonyms=D6Wsu116e, Kiaa0592;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, and FVB/N-3; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-793; THR-795 AND
RP   SER-1049, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-747, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614; SER-747; SER-798;
RP   SER-870 AND SER-1067, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-159; SER-533;
RP   SER-723 AND SER-747, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-159; SER-388;
RP   SER-533; SER-613; SER-614; SER-723; SER-747; SER-1172; SER-1173;
RP   SER-1222 AND SER-1333, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614 AND SER-747, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Component of the WASH complex, a complex present at the
CC       surface of endosomes that recruits and activates the Arp2/3
CC       complex to induce actin polymerization. The WASH complex plays a
CC       key role in the fission of tubules that serve as transport
CC       intermediates during endosome sorting. In the complex, it probably
CC       mediates the recruitment of the complex to endosome membranes (By
CC       similarity).
CC   -!- SUBUNIT: Component of the WASH complex, composed of F-actin-
CC       capping protein subunit alpha (CAPZA1, CAPZA2 or CAPZA3), F-actin-
CC       capping protein subunit beta (CAPZB), WASH1, FAM21, KIAA1033,
CC       KIAA0196 and CCDC53 (By similarity). Interacts (via WHD1 region)
CC       with WASH1; the interaction is direct (By similarity).
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6PGL7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PGL7-2; Sequence=VSP_030949;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the FAM21 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH49979.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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DR   EMBL; AK122320; BAC65602.2; -; Transcribed_RNA.
DR   EMBL; AK163765; BAE37485.1; -; mRNA.
DR   EMBL; AK038318; BAC29966.1; -; mRNA.
DR   EMBL; BC049979; AAH49979.1; ALT_SEQ; mRNA.
DR   EMBL; BC056942; AAH56942.1; -; mRNA.
DR   IPI; IPI00468516; -.
DR   IPI; IPI00886310; -.
DR   RefSeq; NP_080861.2; NM_026585.3.
DR   UniGene; Mm.28524; -.
DR   ProteinModelPortal; Q6PGL7; -.
DR   PhosphoSite; Q6PGL7; -.
DR   PRIDE; Q6PGL7; -.
DR   Ensembl; ENSMUST00000036759; ENSMUSP00000038983; ENSMUSG00000024104.
DR   GeneID; 28006; -.
DR   KEGG; mmu:28006; -.
DR   CTD; 28006; -.
DR   MGI; MGI:106463; D6Wsu116e.
DR   HOGENOM; HBG505241; -.
DR   HOVERGEN; HBG055529; -.
DR   InParanoid; Q6PGL7; -.
DR   OMA; VRGKRRP; -.
DR   OrthoDB; EOG4NVZJX; -.
DR   PhylomeDB; Q6PGL7; -.
DR   NextBio; 306510; -.
DR   ArrayExpress; Q6PGL7; -.
DR   Bgee; Q6PGL7; -.
DR   Genevestigator; Q6PGL7; -.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0071203; C:WASH complex; ISS:UniProtKB.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endosome; Membrane; Phosphoprotein; Transport.
FT   CHAIN         1   1334       WASH complex subunit FAM21.
FT                                /FTId=PRO_0000317433.
FT   COMPBIAS    221    228       Poly-Glu.
FT   COMPBIAS    443    453       Poly-Asp.
FT   COMPBIAS    661    665       Poly-Asp.
FT   COMPBIAS    780    783       Poly-Ser.
FT   MOD_RES     157    157       Phosphoserine.
FT   MOD_RES     159    159       Phosphoserine.
FT   MOD_RES     388    388       Phosphoserine.
FT   MOD_RES     533    533       Phosphoserine.
FT   MOD_RES     613    613       Phosphoserine.
FT   MOD_RES     614    614       Phosphoserine.
FT   MOD_RES     723    723       Phosphoserine.
FT   MOD_RES     747    747       Phosphoserine.
FT   MOD_RES     793    793       Phosphothreonine.
FT   MOD_RES     795    795       Phosphothreonine.
FT   MOD_RES     798    798       Phosphoserine.
FT   MOD_RES     870    870       Phosphoserine.
FT   MOD_RES    1049   1049       Phosphoserine.
FT   MOD_RES    1067   1067       Phosphoserine.
FT   MOD_RES    1172   1172       Phosphoserine.
FT   MOD_RES    1173   1173       Phosphoserine.
FT   MOD_RES    1222   1222       Phosphoserine.
FT   MOD_RES    1333   1333       Phosphoserine.
FT   VAR_SEQ     866    952       SSVPSGGSLFGDDEDDDLFSSAKTQPVVPEKKGTLKKDHPV
FT                                SLKNQDPLDSTQGSKEKSTWKTEPAQDSSGLTPFKSREPSS
FT                                RIGKI -> V (in isoform 2).
FT                                /FTId=VSP_030949.
FT   CONFLICT    385    385       L -> S (in Ref. 3; AAH49979).
FT   CONFLICT    556    556       P -> S (in Ref. 3; AAH49979).
FT   CONFLICT    630    630       A -> V (in Ref. 1; BAC65602).
FT   CONFLICT    910    910       N -> S (in Ref. 2; BAC29966).
SQ   SEQUENCE   1334 AA;  145311 MW;  AD35C3FFAC27C159 CRC64;
     MNRTSPDSER PPASEPVWER PWSVEEIRRS SQNWSLAADA GLLQFLQEFS QQTISRTHEI
     KKQVDGLIQE TKATHCRLHN VFNDFLMLSN TQFIENRVYD EEVEEQVLKA EAEKAEQEKT
     REQKEIDLIP KVQEAVNYGL QVLDSAFEQL DIKAGNSDSE EDDANERVDL ILEPKDLYID
     RPLPYLIGSK LFMEQEDVGL GELSSEEGSV GSDRGSIVDS EDEKEEEESD EDFASHSDND
     QNQHTTQISD EEEDDDGDLF ADSEKEGDDI EDIEESAKSK RPTSFADELA ARIKGDISNQ
     RKEGQTDGKP QKTVKEKKER RTPADDEEDI LFPPPTLTDE DFSPFGSRGG LFSNGQGLFD
     DEDESDLFKE APRARPAQAP VSEELPPSPK PGKKIPAGAV SVLLGHPDVS GSTSAPSLKE
     LQKHGQPTPG KSSHLPTPAG LFDDDDNDND EDDNNFFMPS SSKPSKTDKV KSTAIIFDDD
     EGDLFKEKAE ALPAASVSQT HESKTRADKT IALPSSKNLK LVSETKTQKG LFSDEEDSED
     LFSSQSSSKP KSASLPSSQP PTSVSLFGDE DEEDSLFGSA AAKKQTSSLQ PQSQEKAKPS
     EQPSKKTSAL LFSSDEEDQW NIADSHTKLA SDNKSKGELW DSGATQGQEA KAVKKTNLFE
     DDDDDEVDLF AIAKDSQKKT QRTSLLFEDD AESGSSLFGL PPTSVPSATT KKESVPKVPL
     LFSDEEDSEV PSGVKPEDLK VDNARVSPEV GSADVASIAQ KEGLLPASDQ EAGGPSDIFS
     SSSPLDKGAK GRTRTVLSLF DEDEDKVEDE SSTCAPQDGR EKGLKTDSRP KSTGVFQDEE
     LLFSHKLQKD NDPDVDLFAG TKKIRSSVPS GGSLFGDDED DDLFSSAKTQ PVVPEKKGTL
     KKDHPVSLKN QDPLDSTQGS KEKSTWKTEP AQDSSGLTPF KSREPSSRIG KIQANLAINP
     AALLPTVALQ IPGTKPVSSE LAFPSSEPGR SHILESVPTL PGSVEAGVSF DLPAQADTLH
     SANKSRVKVR GKRRPQTRAA RRLAAQESSE AEDVTVDRGP VAQLSSSPVL PNGHQPLLQP
     RMASGQTSSE TATAPPWEGG PVLSAADRSF FVKSRPQTGN EADLFDSGDI FPKSRGSQSV
     EGAGVMAGEP PSHSSGGRKE KSLAFPDLSE GSSTEDLFQS VKPRAAKNRN PFPLLEDEED
     LFADPRGKKN ERKPDSHQDS VSKTHDIFED DIFATEAIKP FPKKREKGRT LEPNLFDDNI
     DIFADLTVKP KEKSKKKVAA KSMFDDDTDD IFSSGLQAKA SKPKSQSAEA ASEQRSEHKV
     ASIFDDPLNA FGSQ
//
ID   DCLK2_MOUSE             Reviewed;         756 AA.
AC   Q6PGN3; Q1EDG7; Q1EDG8; Q4H483; Q4W8V1; Q8BUU0; Q8BX25;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Serine/threonine-protein kinase DCLK2;
DE            EC=2.7.11.1;
DE   AltName: Full=CaMK-like CREB regulatory kinase 2;
DE            Short=CL2;
DE            Short=CLICK-II;
DE            Short=CLICK2;
DE   AltName: Full=Doublecortin-like and CAM kinase-like 2;
DE   AltName: Full=Doublecortin-like kinase 2;
GN   Name=Dclk2; Synonyms=Dcamkl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4 AND 5), FUNCTION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   MUTAGENESIS OF LYS-422.
RC   STRAIN=ICR; TISSUE=Brain;
RX   PubMed=16684769; DOI=10.1074/jbc.M513212200;
RA   Ohmae S., Takemoto-Kimura S., Okamura M., Adachi-Morishima A.,
RA   Nonaka M., Fuse T., Kida S., Tanji M., Furuyashiki T., Arakawa Y.,
RA   Narumiya S., Okuno H., Bito H.;
RT   "Molecular identification and characterization of a family of kinases
RT   with homology to Ca2+/calmodulin-dependent protein kinases I/IV.";
RL   J. Biol. Chem. 281:20427-20439(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RA   Shimomura S., Nagamine T., Sueyoshi N., Kameshita I.;
RT   "Molecular cloning and expression of mouse doublecortin like protein
RT   kinase.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 6).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryonic stem cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Protein kinase with a significantly reduced Ca2+/CAM
CC       affinity and dependence compared to other members of the CaMK
CC       family. May play a role in the down-regulation of CRE-dependent
CC       gene activation probably by phosphorylation of the CREB
CC       coactivator CRTC2/TORC2 and the resulting retention of TORC2 in
CC       the cytoplasm.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Binds to and stabilizes microtubules (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Colocalizes
CC       with microtubules.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q6PGN3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PGN3-2; Sequence=VSP_012797;
CC       Name=3; Synonyms=alpha;
CC         IsoId=Q6PGN3-3; Sequence=VSP_038892, VSP_012797;
CC       Name=4; Synonyms=beta1;
CC         IsoId=Q6PGN3-4; Sequence=VSP_038892, VSP_038895, VSP_038896;
CC         Note=No experimental confirmation available;
CC       Name=5; Synonyms=beta2;
CC         IsoId=Q6PGN3-5; Sequence=VSP_038892, VSP_012797, VSP_038895,
CC                                  VSP_038896;
CC         Note=No experimental confirmation available;
CC       Name=6;
CC         IsoId=Q6PGN3-6; Sequence=VSP_038893, VSP_038894;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Brain-specific. Expressed in neurons, but not
CC       in glial cells, in most forebrain areas. Strong expression in the
CC       hippocampal CA1 pyramidal cell layer.
CC   -!- DEVELOPMENTAL STAGE: At 17.5 dpc, predominantly expressed in the
CC       central nervous system, throughout the forebrain, midbrain,
CC       hindbrain, and the spinal cord.
CC   -!- DOMAIN: The doublecortin domains are involved in the
CC       colocalization with microtubules.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. CaMK subfamily.
CC   -!- SIMILARITY: Contains 2 doublecortin domains.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AY968049; AAY40243.1; -; mRNA.
DR   EMBL; AY968050; AAY40244.1; -; mRNA.
DR   EMBL; AY968051; AAY40245.1; -; mRNA.
DR   EMBL; AB198721; BAE06836.1; -; mRNA.
DR   EMBL; AK049179; BAC33590.1; -; mRNA.
DR   EMBL; AK082633; BAC38555.1; -; mRNA.
DR   EMBL; BC056921; AAH56921.1; -; mRNA.
DR   IPI; IPI00226417; -.
DR   IPI; IPI00405162; -.
DR   IPI; IPI00553827; -.
DR   IPI; IPI00761924; -.
DR   IPI; IPI00955659; -.
DR   IPI; IPI00955667; -.
DR   RefSeq; NP_001182425.1; NM_001195496.1.
DR   RefSeq; NP_001182426.1; NM_001195497.1.
DR   RefSeq; NP_001182427.1; NM_001195498.1.
DR   RefSeq; NP_001182428.1; NM_001195499.1.
DR   RefSeq; NP_081815.3; NM_027539.5.
DR   UniGene; Mm.44490; -.
DR   ProteinModelPortal; Q6PGN3; -.
DR   SMR; Q6PGN3; 69-169, 191-289, 388-660.
DR   STRING; Q6PGN3; -.
DR   PhosphoSite; Q6PGN3; -.
DR   PRIDE; Q6PGN3; -.
DR   Ensembl; ENSMUST00000029719; ENSMUSP00000029719; ENSMUSG00000028078.
DR   GeneID; 70762; -.
DR   KEGG; mmu:70762; -.
DR   UCSC; uc008prl.2; mouse.
DR   UCSC; uc008prp.2; mouse.
DR   CTD; 70762; -.
DR   MGI; MGI:1918012; Dclk2.
DR   GeneTree; ENSGT00600000084006; -.
DR   HOVERGEN; HBG003790; -.
DR   OMA; VIMNTAL; -.
DR   PhylomeDB; Q6PGN3; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 332205; -.
DR   ArrayExpress; Q6PGN3; -.
DR   Bgee; Q6PGN3; -.
DR   CleanEx; MM_DCLK2; -.
DR   Genevestigator; Q6PGN3; -.
DR   GermOnline; ENSMUSG00000028078; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR003533; Doublecortin_dom.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Gene3D; G3DSA:3.10.20.230; Doublecortin_dom; 2.
DR   Pfam; PF03607; DCX; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00537; DCX; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF89837; Doublecortin_dom; 2.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50309; DC; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Cytoskeleton; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Repeat;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    756       Serine/threonine-protein kinase DCLK2.
FT                                /FTId=PRO_0000085923.
FT   DOMAIN       72    158       Doublecortin 1.
FT   DOMAIN      196    279       Doublecortin 2.
FT   DOMAIN      393    650       Protein kinase.
FT   NP_BIND     399    407       ATP (By similarity).
FT   COMPBIAS    292    361       Ser-rich.
FT   COMPBIAS    719    740       Pro-rich.
FT   ACT_SITE    514    514       Proton acceptor (By similarity).
FT   BINDING     422    422       ATP (By similarity).
FT   MOD_RES       6      6       Phosphoserine.
FT   VAR_SEQ     320    320       V -> VKRAGHSSAYSTAKSPV (in isoform 3,
FT                                isoform 4 and isoform 5).
FT                                /FTId=VSP_038892.
FT   VAR_SEQ     352    352       Missing (in isoform 2, isoform 3 and
FT                                isoform 5).
FT                                /FTId=VSP_012797.
FT   VAR_SEQ     625    651       Missing (in isoform 6).
FT                                /FTId=VSP_038893.
FT   VAR_SEQ     691    756       NTALDKEGQIFCSKLCQDSSRPSREQTSPVPPSAQEAPPPL
FT                                ESPRPPGPPATSGCDLAGTWRRHRD -> VSGTQSSASESR
FT                                GWPSWSCCLDSQGSAHGSWCLPCSCLHGGLPGM (in
FT                                isoform 6).
FT                                /FTId=VSP_038894.
FT   VAR_SEQ     691    699       NTALDKEGQ -> VQGHEHGSR (in isoform 4 and
FT                                isoform 5).
FT                                /FTId=VSP_038895.
FT   VAR_SEQ     700    756       Missing (in isoform 4 and isoform 5).
FT                                /FTId=VSP_038896.
FT   MUTAGEN     422    422       K->A: Loss of kinase activity. No effect
FT                                on colocalization with microtubules.
FT   CONFLICT     33     33       G -> D (in Ref. 1; AAY40245).
SQ   SEQUENCE   756 AA;  82979 MW;  C658F0999547B779 CRC64;
     MASTRSIELE HFEERDKRPR PGSRRGAPSS SGGSSISGPK GNGLIPSPAH SAHCSFYRTR
     TLQALSSEKK AKKARFYRNG DRYFKGLVFA ISNDRFRSFD ALLIELTRSL SDNVNLPQGV
     RTIYTIDGSR KVTSLDELLE GESYVCASNE PFRKVDYTKN VNPNWSVNIK GGTTRTLAVA
     SAKSEVKESK DFIKPKLVTV IRSGVKPRKA VRILLNKKTA HSFEQVLTDI TEAIKLDSGV
     VKRLCTLDGK QVTCLQDFFG DDDVFIACGP EKYRYAQDDF VLDHSECRVL KSSYSRASAA
     KYSGSRSPGF SRRSKSPASV NGTPSSQLST PKSTKSSSSS PTSPGSFRGL KQISAQGRSS
     SNVNGGPELD RCLSPEGVNG NRCSESFPLL EKYRIGKVIG DGNFAVVKEC VDRYTGKEFA
     LKIIDKAKCC GKEHLIENEV SILRRVKHPN IIMLVEEMET ATDLFLVMEL VKGGDLFDAI
     TSSTKYTERD GSAMVYNLAN ALRYLHSLSI VHRDIKPENL LVCEYPDGTK SLKLGDFGLA
     TVVEGPLYTV CGTPTYVAPE IIAETGYGLK VDVWAAGVIT YILLCGFPPF RSENNLQEDL
     FDQILAGKLE FPAPYWDNIT DSAKELISQM LQVNVEARCT AGEILSHPWV SDDASQENNM
     QAEVTGKLKQ HFNNALPKQN STTTGVSVIM NTALDKEGQI FCSKLCQDSS RPSREQTSPV
     PPSAQEAPPP LESPRPPGPP ATSGCDLAGT WRRHRD
//
ID   SORT_MOUSE              Reviewed;         825 AA.
AC   Q6PHU5; A2AEE8; Q3UHE2; Q8K043; Q9QXW6;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Sortilin;
DE   AltName: Full=Neurotensin receptor 3;
DE            Short=NTR3;
DE            Short=mNTR3;
DE   Flags: Precursor;
GN   Name=Sort1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION AS A
RP   NEUROTENSIN RECEPTOR, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=21223051; PubMed=11322955; DOI=10.1016/S0014-5793(01)02367-5;
RA   Navarro V., Martin S., Sarret P., Nielsen M.S., Petersen C.M.,
RA   Vincent J.-P., Mazella J.;
RT   "Pharmacological properties of the mouse neurotensin receptor 3.
RT   Maintenance of cell surface receptor during internalization of
RT   neurotensin.";
RL   FEBS Lett. 495:100-105(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   SUBCELLULAR LOCATION, AND INDUCTION.
RX   MEDLINE=98123136; PubMed=9452485; DOI=10.1074/jbc.273.6.3582;
RA   Morris N.J., Ross S.A., Lane W.S., Moestrup S.K., Petersen C.M.,
RA   Keller S.R., Lienhard G.E.;
RT   "Sortilin is the major 110-kDa protein in GLUT4 vesicles from
RT   adipocytes.";
RL   J. Biol. Chem. 273:3582-3587(1998).
RN   [6]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=99165852; PubMed=10064893; DOI=10.1016/S0169-328X(99)00022-4;
RA   Hermans-Borgmeyer I., Hermey G., Nykjaer A., Schaller C.;
RT   "Expression of the 100-kDa neurotensin receptor sortilin during mouse
RT   embryonal development.";
RL   Brain Res. Mol. Brain Res. 65:216-219(1999).
RN   [7]
RP   INTERACTION WITH LPL.
RX   MEDLINE=99185109; PubMed=10085125; DOI=10.1074/jbc.274.13.8832;
RA   Nielsen M.S., Jacobsen C., Olivecrona G., Gliemann J., Petersen C.M.;
RT   "Sortilin/neurotensin receptor-3 binds and mediates degradation of
RT   lipoprotein lipase.";
RL   J. Biol. Chem. 274:8832-8836(1999).
RN   [8]
RP   FUNCTION.
RX   PubMed=10594043; DOI=10.1128/MCB.20.1.416-427.2000;
RA   Hashiramoto M., James D.E.;
RT   "Characterization of insulin-responsive GLUT4 storage vesicles
RT   isolated from 3T3-L1 adipocytes.";
RL   Mol. Cell. Biol. 20:416-427(2000).
RN   [9]
RP   FUNCTION, INTERACTION WITH PSAP, AND SUBCELLULAR LOCATION.
RX   PubMed=15236332; DOI=10.1002/mrd.20097;
RA   Zeng J., Hassan A.J., Morales C.R.;
RT   "Study of the mouse sortilin gene: effects of its transient silencing
RT   by RNA interference in TM4 Sertoli cells.";
RL   Mol. Reprod. Dev. 68:469-475(2004).
RN   [10]
RP   FUNCTION.
RX   PubMed=15236333; DOI=10.1002/mrd.20096;
RA   Hassan A.J., Zeng J., Ni X., Morales C.R.;
RT   "The trafficking of prosaposin (SGP-1) and GM2AP to the lysosomes of
RT   TM4 Sertoli cells is mediated by sortilin and monomeric adaptor
RT   proteins.";
RL   Mol. Reprod. Dev. 68:476-483(2004).
RN   [11]
RP   FUNCTION.
RX   PubMed=15372498; DOI=10.1002/jnr.20231;
RA   Dicou E., Vincent J.-P., Mazella J.;
RT   "Neurotensin receptor-3/sortilin mediates neurotensin-induced
RT   cytokine/chemokine expression in a murine microglial cell line.";
RL   J. Neurosci. Res. 78:92-99(2004).
RN   [12]
RP   FUNCTION, INTERACTION WITH SLC2A4, SUBCELLULAR LOCATION, AND
RP   INDUCTION.
RX   PubMed=15992544; DOI=10.1016/j.devcel.2005.04.004;
RA   Shi J., Kandror K.V.;
RT   "Sortilin is essential and sufficient for the formation of Glut4
RT   storage vesicles in 3T3-L1 adipocytes.";
RL   Dev. Cell 9:99-108(2005).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-819, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: Functions as a sorting receptor in the Golgi compartment
CC       and as a clearance receptor on the cell surface. Required for
CC       protein transport from the Golgi apparatus to the lysosomes by a
CC       pathway that is independent of the mannose-6-phosphate receptor
CC       (M6PR). Also required for protein transport from the Golgi
CC       apparatus to the endosomes. Promotes neuronal apoptosis by
CC       mediating endocytosis of the proapoptotic precursor forms of BDNF
CC       (proBDNF) and NGFB (proNGFB). Also acts as a receptor for
CC       neurotensin. May promote mineralization of the extracellular
CC       matrix during osteogenic differentiation by scavenging
CC       extracellular LPL. Probably required in adipocytes for the
CC       formation of specialized storage vesicles containing the glucose
CC       transporter SLC2A4/GLUT4 (GLUT4 storage vesicles, or GSVs). These
CC       vesicles provide a stable pool of SLC2A4 and confer increased
CC       responsiveness to insulin. May also mediate transport from the
CC       endoplasmic reticulum to the Golgi.
CC   -!- SUBUNIT: Interacts with the cytosolic adapter proteins GGA1 and
CC       GGA2. Interacts with numerous ligands including the receptor-
CC       associated protein LRPAP1/RAP, NTS and GM2A. Forms a complex with
CC       NGFR which binds specifically to the precursor forms of NGFB
CC       (proNGFB) and BDNF (proBDNF) (By similarity). Interacts with LPL,
CC       PSAP and SLC2A4.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential). Endoplasmic reticulum membrane; Single-pass
CC       type I membrane protein (Potential). Endosome membrane; Single-
CC       pass type I membrane protein (Potential). Golgi apparatus, Golgi
CC       stack membrane; Single-pass type I membrane protein (Potential).
CC       Lysosome membrane; Single-pass type I membrane protein
CC       (Potential). Nucleus membrane; Single-pass type I membrane protein
CC       (Potential). Cell membrane; Single-pass type I membrane protein;
CC       Extracellular side. Lysosome membrane; Single-pass type I membrane
CC       protein (Potential). Note=Localized to membranes of the
CC       endoplasmic reticulum, endosomes, Golgi stack, lysosomes and
CC       nucleus. A small fraction of the protein is also localized to the
CC       plasma membrane. Also found in SLC2A4/GLUT4 storage vesicles
CC       (GSVs) in adipocytes. Localization to the plasma membrane in
CC       adipocytes is enhanced by insulin.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6PHU5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PHU5-2; Sequence=VSP_016650;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, particularly the
CC       piriform cortex, the cerebral cortex and the hippocampus.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the ectoderm at E7.5 and within
CC       the germ cell layers at E8.5. Expressed within the neural
CC       epithelium and the neural tube at E9.5 and subsequently expressed
CC       in the nervous system throughout development. Expression in the
CC       proliferative zones of the central nervous system declines between
CC       E14.5 and E16.5, while expression remains high in the cerebral
CC       cortex and the neural retina. Expressed in the pituitary and the
CC       sensory epithelia throughout development.
CC   -!- INDUCTION: During adipocyte differentiation.
CC   -!- DOMAIN: The N-terminal propeptide may facilitate precursor
CC       transport within the Golgi stack. Intrachain binding of the N-
CC       terminal propeptide and the extracellular domain may also inhibit
CC       premature ligand binding (By similarity).
CC   -!- DOMAIN: The extracellular domain may be shed following protease
CC       cleavage in some cell types (By similarity).
CC   -!- PTM: The N-terminal propeptide is cleaved by furin and possibly
CC       other homologous proteases (By similarity).
CC   -!- SIMILARITY: Belongs to the SORT1 family.
CC   -!- SIMILARITY: Contains 9 BNR repeats.
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DR   EMBL; AF175279; AAF22639.1; -; mRNA.
DR   EMBL; AK147442; BAE27915.1; -; mRNA.
DR   EMBL; AL671899; CAM19473.1; -; Genomic_DNA.
DR   EMBL; BC034129; AAH34129.1; -; mRNA.
DR   EMBL; BC056343; AAH56343.1; -; mRNA.
DR   IPI; IPI00420955; -.
DR   IPI; IPI00650038; -.
DR   RefSeq; NP_064356.2; NM_019972.2.
DR   UniGene; Mm.157119; -.
DR   ProteinModelPortal; Q6PHU5; -.
DR   SMR; Q6PHU5; 86-747.
DR   DIP; DIP-46095N; -.
DR   STRING; Q6PHU5; -.
DR   PhosphoSite; Q6PHU5; -.
DR   PRIDE; Q6PHU5; -.
DR   Ensembl; ENSMUST00000090564; ENSMUSP00000088052; ENSMUSG00000068747.
DR   Ensembl; ENSMUST00000102632; ENSMUSP00000099692; ENSMUSG00000068747.
DR   GeneID; 20661; -.
DR   KEGG; mmu:20661; -.
DR   UCSC; uc008qyr.1; mouse.
DR   UCSC; uc008qys.1; mouse.
DR   CTD; 20661; -.
DR   MGI; MGI:1338015; Sort1.
DR   GeneTree; ENSGT00510000046443; -.
DR   HOVERGEN; HBG080235; -.
DR   OMA; LTQMMYS; -.
DR   OrthoDB; EOG4QVCBD; -.
DR   PhylomeDB; Q6PHU5; -.
DR   NextBio; 299105; -.
DR   ArrayExpress; Q6PHU5; -.
DR   Bgee; Q6PHU5; -.
DR   CleanEx; MM_SORT1; -.
DR   Genevestigator; Q6PHU5; -.
DR   GermOnline; ENSMUSG00000068747; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005792; C:microsome; IDA:BHF-UCL.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0030140; C:trans-Golgi network transport vesicle; IDA:MGI.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0046323; P:glucose import; IMP:BHF-UCL.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0014902; P:myotube differentiation; IMP:BHF-UCL.
DR   GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR   GO; GO:0032868; P:response to insulin stimulus; IMP:BHF-UCL.
DR   GO; GO:0016050; P:vesicle organization; IMP:BHF-UCL.
DR   InterPro; IPR002860; BNR_rpt.
DR   InterPro; IPR006581; VPS10.
DR   Pfam; PF02012; BNR; 5.
DR   SMART; SM00602; VPS10; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane;
KW   Cleavage on pair of basic residues; Developmental protein;
KW   Differentiation; Disulfide bond; Endocytosis; Endoplasmic reticulum;
KW   Endosome; Glycoprotein; Golgi apparatus; Lysosome; Membrane; Nucleus;
KW   Osteogenesis; Phosphoprotein; Receptor; Repeat; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     31       Potential.
FT   PROPEP       32     75       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000045155.
FT   CHAIN        76    825       Sortilin.
FT                                /FTId=PRO_0000045156.
FT   TOPO_DOM     32    754       Extracellular (Potential).
FT   TRANSMEM    755    775       Helical; (Potential).
FT   TOPO_DOM    776    825       Cytoplasmic (Potential).
FT   REPEAT      143    154       BNR 1.
FT   REPEAT      196    207       BNR 2.
FT   REPEAT      238    249       BNR 3.
FT   REPEAT      285    296       BNR 4.
FT   REPEAT      326    337       BNR 5.
FT   REPEAT      375    386       BNR 6.
FT   REPEAT      426    437       BNR 7.
FT   REPEAT      504    515       BNR 8.
FT   REPEAT      546    557       BNR 9.
FT   REGION       48     59       Intrachain binding of the propeptide and
FT                                the extracellular domain (By similarity).
FT   REGION      610    754       Interactions with LRPAP1 and NGFB (By
FT                                similarity).
FT   REGION      777    825       Golgi to endosome transport and
FT                                interactions with GGA1 and GGA2 (By
FT                                similarity).
FT   MOTIF       785    790       Endocytosis signal (Potential).
FT   COMPBIAS     38     44       Poly-Pro.
FT   MOD_RES     819    819       Phosphoserine.
FT   CARBOHYD     96     96       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    160    160       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    272    272       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    404    404       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    580    580       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    682    682       N-linked (GlcNAc...) (Potential).
FT   DISULFID     84    554       By similarity.
FT   DISULFID    255    275       By similarity.
FT   DISULFID    446    456       By similarity.
FT   DISULFID    610    649       By similarity.
FT   DISULFID    632    664       By similarity.
FT   DISULFID    666    721       By similarity.
FT   DISULFID    673    686       By similarity.
FT   DISULFID    700    738       By similarity.
FT   VAR_SEQ     748    748       Q -> QDSRPQGHSLSQNPAPPPLGYTENTHFLSPTQKQ
FT                                (in isoform 2).
FT                                /FTId=VSP_016650.
FT   CONFLICT    315    315       V -> E (in Ref. 1; AAF22639).
SQ   SEQUENCE   825 AA;  91200 MW;  9A7A73C6FE1C8201 CRC64;
     MERPRGAADG LLRWPLGLLL LLQLLPPAAV GQDRLDAPPP PAPPLLRWAG PVGVSWGLRA
     AAPGGPVPRA GRWRRGAPAE DQDCGRLPDF IAKLTNNTHQ HVFDDLSGSV SLSWVGDSTG
     VILVLTTFQV PLVIVSFGQS KLYRSEDYGK NFKDITNLIN NTFIRTEFGM AIGPENSGKV
     ILTAEVSGGS RGGRVFRSSD FAKNFVQTDL PFHPLTQMMY SPQNSDYLLA LSTENGLWVS
     KNFGEKWEEI HKAVCLAKWG PNNIIFFTTH VNGSCKADLG ALELWRTSDL GKTFKTIGVK
     IYSFGLGGRF LFASVMADKD TTRRIHVSTD QGDTWSMAQL PSVGQEQFYS ILAANEDMVF
     MHVDEPGDTG FGTIFTSDDR GIVYSKSLDR HLYTTTGGET DFTNVTSLRG VYITSTLSED
     NSIQSMITFD QGGRWEHLRK PENSKCDATA KNKNECSLHI HASYSISQKL NVPMAPLSEP
     NAVGIVIAHG SVGDAISVMV PDVYISDDGG YSWAKMLEGP HYYTILDSGG IIVAIEHSNR
     PINVIKFSTD EGQCWQSYVF TQEPIYFTGL ASEPGARSMN ISIWGFTESF ITRQWVSYTV
     DFKDILERNC EEDDYTTWLA HSTDPGDYKD GCILGYKEQF LRLRKSSVCQ NGRDYVVAKQ
     PSVCPCSLED FLCDFGYFRP ENASECVEQP ELKGHELEFC LYGKEEHLTT NGYRKIPGDK
     CQGGMNPARE VKDLKKKCTS NFLNPTKQNS KSNSVPIILA IVGLMLVTVV AGVLIVKKYV
     CGGRFLVHRY SVLQQHAEAD GVEALDSTSH AKSGYHDDSD EDLLE
//
ID   KCC2D_MOUSE             Reviewed;         499 AA.
AC   Q6PHZ2; Q3UF87; Q3UQH9; Q5DTK4; Q8CAC5; Q9CZE2;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Calcium/calmodulin-dependent protein kinase type II subunit delta;
DE            Short=CaM kinase II subunit delta;
DE            Short=CaMK-II subunit delta;
DE            EC=2.7.11.17;
GN   Name=Camk2d; Synonyms=Kiaa4163;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Hypothalamus, Stomach, and Sympathetic ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C3H/He; TISSUE=Osteoblast;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-231, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-337, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330 AND THR-337, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: CaM-kinase II (CAMK2) is a prominent kinase in the
CC       central nervous system that may function in long-term potentiation
CC       and neurotransmitter release (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Autophosphorylation of CAMK2 plays an important
CC       role in the regulation of the kinase activity (By similarity).
CC   -!- SUBUNIT: CAMK2 is composed of four different chains: alpha, beta,
CC       gamma, and delta. The different isoforms assemble into homo- or
CC       heteromultimeric holoenzymes composed of 8 to 12 subunits.
CC       Interacts with RRAD (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=Delta 2;
CC         IsoId=Q6PHZ2-1; Sequence=Displayed;
CC       Name=2; Synonyms=Delta 6;
CC         IsoId=Q6PHZ2-2; Sequence=VSP_023103, VSP_023102;
CC         Note=Ref.1 (BAE25062) sequence is in conflict in position:
CC         478:N->K;
CC       Name=3; Synonyms=Delta 10;
CC         IsoId=Q6PHZ2-4; Sequence=VSP_023101, VSP_023103, VSP_023102;
CC       Name=4; Synonyms=Delta 5;
CC         IsoId=Q6PHZ2-5; Sequence=VSP_023100, VSP_023103, VSP_023102;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. CaMK subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90304.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK039076; BAC30232.1; -; mRNA.
DR   EMBL; AK012702; BAB28422.1; -; mRNA.
DR   EMBL; AK142435; BAE25062.1; -; mRNA.
DR   EMBL; AK148840; BAE28674.1; -; mRNA.
DR   EMBL; AK220516; BAD90304.1; ALT_INIT; mRNA.
DR   EMBL; BC052894; AAH52894.1; -; mRNA.
DR   IPI; IPI00112584; -.
DR   IPI; IPI00406790; -.
DR   IPI; IPI00475044; -.
DR   IPI; IPI00828919; -.
DR   RefSeq; NP_001020609.1; NM_001025438.1.
DR   RefSeq; NP_001020610.1; NM_001025439.1.
DR   RefSeq; NP_076302.1; NM_023813.3.
DR   UniGene; Mm.255822; -.
DR   HSSP; Q9NG91; 2BDW.
DR   ProteinModelPortal; Q6PHZ2; -.
DR   SMR; Q6PHZ2; 11-309, 339-471.
DR   MINT; MINT-4391081; -.
DR   STRING; Q6PHZ2; -.
DR   PhosphoSite; Q6PHZ2; -.
DR   PRIDE; Q6PHZ2; -.
DR   Ensembl; ENSMUST00000066466; ENSMUSP00000063359; ENSMUSG00000053819.
DR   Ensembl; ENSMUST00000106396; ENSMUSP00000102004; ENSMUSG00000053819.
DR   GeneID; 108058; -.
DR   KEGG; mmu:108058; -.
DR   UCSC; uc008rgk.1; mouse.
DR   CTD; 108058; -.
DR   MGI; MGI:1341265; Camk2d.
DR   GeneTree; ENSGT00550000074354; -.
DR   HOVERGEN; HBG108055; -.
DR   OrthoDB; EOG42JNR7; -.
DR   PhylomeDB; Q6PHZ2; -.
DR   BRENDA; 2.7.11.17; 244.
DR   NextBio; 359953; -.
DR   ArrayExpress; Q6PHZ2; -.
DR   Bgee; Q6PHZ2; -.
DR   Genevestigator; Q6PHZ2; -.
DR   GO; GO:0005954; C:calcium- and calmodulin-dependent protein kinase complex; TAS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0030315; C:T-tubule; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:EC.
DR   GO; GO:0006816; P:calcium ion transport; IDA:MGI.
DR   GO; GO:0060048; P:cardiac muscle contraction; IDA:MGI.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; IMP:MGI.
DR   InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF08332; CaMKII_AD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Calmodulin-binding;
KW   Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    499       Calcium/calmodulin-dependent protein
FT                                kinase type II subunit delta.
FT                                /FTId=PRO_0000277817.
FT   DOMAIN       14    272       Protein kinase.
FT   NP_BIND      20     28       ATP (By similarity).
FT   ACT_SITE    136    136       Proton acceptor (By similarity).
FT   BINDING      43     43       ATP (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       3      3       Phosphoserine (By similarity).
FT   MOD_RES     231    231       Phosphotyrosine.
FT   MOD_RES     287    287       Phosphothreonine.
FT   MOD_RES     306    306       Phosphothreonine (By similarity).
FT   MOD_RES     307    307       Phosphothreonine (By similarity).
FT   MOD_RES     315    315       Phosphoserine (By similarity).
FT   MOD_RES     319    319       Phosphoserine (By similarity).
FT   MOD_RES     330    330       Phosphoserine.
FT   MOD_RES     331    331       Phosphothreonine (By similarity).
FT   MOD_RES     333    333       Phosphoserine (By similarity).
FT   MOD_RES     334    334       Phosphoserine (By similarity).
FT   MOD_RES     336    336       Phosphothreonine (By similarity).
FT   MOD_RES     337    337       Phosphothreonine.
FT   MOD_RES     404    404       Phosphoserine (By similarity).
FT   MOD_RES     441    441       Phosphoserine (By similarity).
FT   MOD_RES     470    470       Phosphoserine (By similarity).
FT   MOD_RES     472    472       Phosphoserine (By similarity).
FT   MOD_RES     490    490       Phosphoserine (By similarity).
FT   VAR_SEQ     328    328       K -> KINNKANVVTSPKENIPTPALEPQTTVIHNPDGNK
FT                                (in isoform 4).
FT                                /FTId=VSP_023100.
FT   VAR_SEQ     329    329       E -> EPQTTVIHNPDGNKE (in isoform 3).
FT                                /FTId=VSP_023101.
FT   VAR_SEQ     478    478       K -> N (in isoform 2, isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_023103.
FT   VAR_SEQ     479    499       Missing (in isoform 2, isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_023102.
FT   CONFLICT    123    125       SVN -> AVL (in Ref. 1; BAC30232).
FT   CONFLICT    129    132       LNGI -> QMGV (in Ref. 1; BAC30232).
FT   CONFLICT    199    199       A -> V (in Ref. 1; BAC30232).
SQ   SEQUENCE   499 AA;  56369 MW;  62999FBAB98120CE CRC64;
     MASTTTCTRF TDEYQLFEEL GKGAFSVVRR CMKIPTGQEY AAKIINTKKL SARDHQKLER
     EARICRLLKH PNIVRLHDSI SEEGFHYLVF DLVTGGELFE DIVAREYYSE ADASHCIQQI
     LESVNHCHLN GIVHRDLKPE NLLLASKSKG AAVKLADFGL AIEVQGDQQA WFGFAGTPGY
     LSPEVLRKDP YGKPVDMWAC GVILYILLVG YPPFWDEDQH RLYQQIKAGA YDFPSPEWDT
     VTPEAKDLIN KMLTINPAKR ITASEALKHP WICQRSTVAS MMHRQETVDC LKKFNARRKL
     KGAILTTMLA TRNFSAAKSL LKKPDGVKES TESSNTTIED EDVKARKQEI IKVTEQLIEA
     INNGDFEAYT KICDPGLTAF EPEALGNLVE GMDFHRFYFE NALSKSNKPI HTIILNPHVH
     LVGDDAACIA YIRLTQYMDG SGMPKTMQSE ETRVWHRRDG KWQNVHFHRS GSPTVPIKPP
     CIPNGKENFS GGTSLWQNI
//
ID   RB15B_MOUSE             Reviewed;         887 AA.
AC   Q6PHZ5; Q8C6G2;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Putative RNA-binding protein 15B;
DE   AltName: Full=RNA-binding motif protein 15B;
GN   Name=Rbm15b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 311-887.
RC   TISSUE=Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 343-887.
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   STRUCTURE BY NMR OF 404-487.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the RNA recognition motif from hypothetical RNA
RT   binding protein BC052180.";
RL   Submitted (NOV-2004) to the PDB data bank.
CC   -!- FUNCTION: May function in the regulation of alternative or illicit
CC       splicing (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Note=Localized in the
CC       nucleoplasm with a granular staining pattern and excluded from the
CC       nucleoli.
CC   -!- SIMILARITY: Belongs to the RRM Spen family.
CC   -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.
CC   -!- SIMILARITY: Contains 1 SPOC domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH52180.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing;
CC       Sequence=BAC35951.1; Type=Erroneous initiation;
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DR   EMBL; AC147636; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC052180; AAH52180.1; ALT_SEQ; mRNA.
DR   EMBL; AK075777; BAC35951.1; ALT_INIT; mRNA.
DR   IPI; IPI00278942; -.
DR   RefSeq; NP_780611.3; NM_175402.4.
DR   UniGene; Mm.480580; -.
DR   PDB; 1WHY; NMR; -; A=404-487.
DR   PDBsum; 1WHY; -.
DR   ProteinModelPortal; Q6PHZ5; -.
DR   SMR; Q6PHZ5; 135-216, 331-488, 707-884.
DR   PhosphoSite; Q6PHZ5; -.
DR   PRIDE; Q6PHZ5; -.
DR   Ensembl; ENSMUST00000055843; ENSMUSP00000059330; ENSMUSG00000045365.
DR   GeneID; 109095; -.
DR   KEGG; mmu:109095; -.
DR   UCSC; uc009rks.1; mouse.
DR   CTD; 109095; -.
DR   MGI; MGI:1923598; Rbm15b.
DR   eggNOG; roNOG14285; -.
DR   GeneTree; ENSGT00530000063730; -.
DR   HOGENOM; HBG717522; -.
DR   HOVERGEN; HBG058366; -.
DR   InParanoid; Q6PHZ5; -.
DR   OrthoDB; EOG42RD6Z; -.
DR   ArrayExpress; Q6PHZ5; -.
DR   Bgee; Q6PHZ5; -.
DR   CleanEx; MM_RBM15B; -.
DR   Genevestigator; Q6PHZ5; -.
DR   GermOnline; ENSMUSG00000045365; Mus musculus.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0000381; P:regulation of alternative nuclear mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR016194; SPOC-like.
DR   InterPro; IPR012921; SPOC_C.
DR   InterPro; IPR010912; SPOC_met.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 3.
DR   Gene3D; G3DSA:2.40.290.10; G3DSA:2.40.290.10; 1.
DR   Pfam; PF00076; RRM_1; 2.
DR   Pfam; PF07744; SPOC; 1.
DR   SMART; SM00360; RRM; 3.
DR   SUPFAM; SSF100939; SPOC-like; 1.
DR   PROSITE; PS50102; RRM; 3.
DR   PROSITE; PS50917; SPOC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Repeat; RNA-binding; Transcription; Transcription regulation.
FT   CHAIN         1    887       Putative RNA-binding protein 15B.
FT                                /FTId=PRO_0000081779.
FT   DOMAIN      136    216       RRM 1.
FT   DOMAIN      333    410       RRM 2.
FT   DOMAIN      414    488       RRM 3.
FT   DOMAIN      708    886       SPOC.
FT   REGION      719    887       Interaction with Epstein-Barr virus BMLF1
FT                                (By similarity).
FT   MOTIF       590    594       Nuclear localization signal (Potential).
FT   COMPBIAS    655    674       His-rich.
FT   MOD_RES     263    263       Phosphoserine (By similarity).
FT   MOD_RES     529    529       Phosphothreonine (By similarity).
FT   MOD_RES     549    549       Phosphoserine (By similarity).
FT   MOD_RES     559    559       Phosphoserine.
FT   MOD_RES     595    595       Phosphoserine (By similarity).
FT   MOD_RES     597    597       Phosphoserine (By similarity).
FT   MOD_RES     598    598       Phosphoserine (By similarity).
FT   MOD_RES     606    606       Phosphoserine (By similarity).
FT   STRAND      416    419
FT   HELIX       427    435
FT   STRAND      440    445
FT   STRAND      447    449
FT   STRAND      452    458
FT   HELIX       459    469
FT   STRAND      475    478
FT   STRAND      482    485
SQ   SEQUENCE   887 AA;  97076 MW;  F9DFCA06595C5DCC CRC64;
     MKRQSERDSS PSGRGSSSSA KRPREREREA EAGGRRAAHK ASGGTKHPVP ARARDKPRGS
     GGGGGHRDGR AAGDANHRAS GGRSSGAPGG GGRTGKASGD PGAGGASPRA SPLPPPPPPP
     GAEPAGPGST AAPEYKTLLI SSLSPALPAE HLEDRLFHQF KRFGEISLRL SHTPELGRVA
     YVNFRHPQDA REARQHALAR QLLLYDRPLK VEPVYLRGGG SSRRSSSSSA AASTPPPGPP
     APADPLGYLP LHGGYQYKQR SLSPVAAPPL REPRARHAAA AFALDAAAAA AVGLSRERAL
     DYYGLYDDRG RPYGYQAVCE EDLMPEDDQR ATRNLFIGNL DHSVSEVELR RAFEKYGIIE
     EVVIKRPARG QGGAYAFLKF QNLDMAHRAK VAMSGRVIGR NPIKIGYGKA NPTTRLWVGG
     LGPNTSLAAL AREFDRFGSI RTIDHVKGDS FAYIQYESLD AAQAACAKMR GFPLGGPDRR
     LRVDFAKAEE TRYPQQYQPS PLPVHYELLT DGYTRHRNLD ADLRVRDRTP PHLLYSDRDR
     TFLEGDWTSL SKSSDRRNSL EGYSRSVRSR SGERWGGDGD RSIAKPWEER RKRRSLSSDR
     GRTTHSPYEE RSRTKGGGQQ SERGSDRTPE RSRKENHSSE GTKESGSNSL SNSRHGAEER
     SHHHHHHEAP DSSHGKKTRE SERNHRTTEA EPKTLEEPKH ETKKLKTLSE YAQTLQLGWN
     GLLVLKNSCF PTSMHILEGD QGVISGLLKD HPSGSKLTQL KIAQRLRLDQ PKLDEVTRRI
     KQGSPNGYAV LLAIQSTPSG PGAEGMPVVE PGLQRRLLRN LVSYLKQKQA AGVISLPVGG
     SKGRDNTGML YAFPPCDFSQ QYLQSALRTL GKLEEEHMVI VIVRDTA
//
ID   KCIP4_MOUSE             Reviewed;         250 AA.
AC   Q6PHZ8; Q6DTJ3; Q8CAD0; Q8R4I2; Q9EQ01;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Kv channel-interacting protein 4;
DE            Short=KChIP4;
DE   AltName: Full=A-type potassium channel modulatory protein 4;
DE   AltName: Full=Calsenilin-like protein;
DE   AltName: Full=Potassium channel-interacting protein 4;
GN   Name=Kcnip4; Synonyms=Calp, Kchip4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=21964093; PubMed=11847232; DOI=10.1074/jbc.M200897200;
RA   Morohashi Y., Hatano N., Ohya S., Takikawa R., Watabiki T.,
RA   Takasugi N., Imaizumi Y., Tomita T., Iwatsubo T.;
RT   "Molecular cloning and characterization of CALP/KChIP4, a novel EF-
RT   hand protein interacting with presenilin 2 and voltage-gated potassium
RT   channel subunit Kv4.";
RL   J. Biol. Chem. 277:14965-14975(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, TISSUE SPECIFICITY,
RP   DOMAIN, AND INTERACTION WITH KCND2.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=21664433; PubMed=11805342; DOI=10.1073/pnas.022509299;
RA   Holmqvist M.H., Cao J., Hernandez-Pineda R., Jacobson M.D.,
RA   Carroll K.I., Sung M.A., Betty M., Ge P., Gilbride K.J., Brown M.E.,
RA   Jurman M.E., Lawson D., Silos-Santiago I., Xie Y., Covarrubias M.,
RA   Rhodes K.J., Distefano P.S., An W.F.;
RT   "Elimination of fast inactivation in Kv4 A-type potassium channels by
RT   an auxiliary subunit domain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:1035-1040(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA   Xia K.U., Fang H.Y., Zhong X.Y., Xia J.H., Zhang Z.H.;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-192 (ISOFORM 2).
RC   TISSUE=Retina;
RA   Ida H., Boylan S., Weigel A., Smit-McBride Z., Chao A., Gao J.,
RA   Buchoff P., Wistow G., Hjelmeland L.;
RT   "Expressed sequence tag analysis of mouse retina.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=15363885; DOI=10.1016/j.molbrainres.2004.06.024;
RA   Xiong H., Kovacs I., Zhang Z.;
RT   "Differential distribution of KChIPs mRNAs in adult mouse brain.";
RL   Brain Res. Mol. Brain Res. 128:103-111(2004).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 56-250, INTERACTION WITH
RP   KCND3/KV4.3, AND FUNCTION.
RX   PubMed=19109250; DOI=10.1074/jbc.M807704200;
RA   Liang P., Wang H., Chen H., Cui Y., Gu L., Chai J., Wang K.;
RT   "Structural insights into KChIP4a modulation of Kv4.3 inactivation.";
RL   J. Biol. Chem. 284:4960-4967(2009).
CC   -!- FUNCTION: Regulatory subunit of Kv4/D (Shal)-type voltage-gated
CC       rapidly inactivating A-type potassium channels. Probably modulates
CC       channels density, inactivation kinetics and rate of recovery from
CC       inactivation in a calcium-dependent and isoform-specific manner.
CC       In vitro, modulates KCND3/Kv4.3 and KCND2/Kv4.2 currents (By
CC       similarity).
CC   -!- SUBUNIT: Component of heteromultimeric potassium channels.
CC       Interacts with the C-terminus of PSEN2 and probably PSEN1 (By
CC       similarity). Interacts with KCND2 and KCND3.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q6PHZ8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PHZ8-2; Sequence=VSP_015071;
CC         Note=Derived from EST data. No experimental confirmation
CC         available;
CC       Name=3;
CC         IsoId=Q6PHZ8-3; Sequence=VSP_015069;
CC       Name=4; Synonyms=KChIPa;
CC         IsoId=Q6PHZ8-4; Sequence=VSP_015070;
CC   -!- TISSUE SPECIFICITY: Expressed in brain. Highly expressed by
CC       neurons in layers II-IV of cortex and in hippocampus, thalamus and
CC       the Purkinje cell layer of the cerebellum.
CC   -!- DOMAIN: The KIS (K-channel inactivation suppressor) domain is
CC       required for converting A-type Kv4 current to a slowly
CC       inactivating delayed rectifier potassium current.
CC   -!- SIMILARITY: Belongs to the recoverin family.
CC   -!- SIMILARITY: Contains 4 EF-hand domains.
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DR   EMBL; AF305071; AAG36976.1; -; mRNA.
DR   EMBL; AF453243; AAL86766.1; -; mRNA.
DR   EMBL; AY647240; AAT68466.1; -; mRNA.
DR   EMBL; AK039048; BAC30218.1; -; mRNA.
DR   EMBL; BC051130; AAH51130.1; -; mRNA.
DR   EMBL; CK618709; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00454000; -.
DR   IPI; IPI00621710; -.
DR   IPI; IPI00648557; -.
DR   IPI; IPI00875649; -.
DR   RefSeq; NP_001186171.1; NM_001199242.1.
DR   RefSeq; NP_084541.3; NM_030265.3.
DR   UniGene; Mm.160172; -.
DR   PDB; 3DD4; X-ray; 3.00 A; A=56-250.
DR   PDBsum; 3DD4; -.
DR   ProteinModelPortal; Q6PHZ8; -.
DR   SMR; Q6PHZ8; 53-250.
DR   STRING; Q6PHZ8; -.
DR   PRIDE; Q6PHZ8; -.
DR   Ensembl; ENSMUST00000087395; ENSMUSP00000084656; ENSMUSG00000029088.
DR   Ensembl; ENSMUST00000101214; ENSMUSP00000098775; ENSMUSG00000029088.
DR   Ensembl; ENSMUST00000101215; ENSMUSP00000098776; ENSMUSG00000029088.
DR   Ensembl; ENSMUST00000113950; ENSMUSP00000109583; ENSMUSG00000029088.
DR   GeneID; 80334; -.
DR   KEGG; mmu:80334; -.
DR   UCSC; uc008xjw.1; mouse.
DR   CTD; 80334; -.
DR   MGI; MGI:1933131; Kcnip4.
DR   GeneTree; ENSGT00560000076973; -.
DR   HOGENOM; HBG746798; -.
DR   HOVERGEN; HBG108179; -.
DR   InParanoid; Q6PHZ8; -.
DR   OrthoDB; EOG4K6G52; -.
DR   PhylomeDB; Q6PHZ8; -.
DR   NextBio; 350021; -.
DR   ArrayExpress; Q6PHZ8; -.
DR   Bgee; Q6PHZ8; -.
DR   CleanEx; MM_KCNIP4; -.
DR   Genevestigator; Q6PHZ8; -.
DR   GermOnline; ENSMUSG00000029088; Mus musculus.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR   InterPro; IPR018248; EF-hand.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR001125; Recoverin.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF00036; efhand; 1.
DR   PRINTS; PR00450; RECOVERIN.
DR   SMART; SM00054; EFh; 3.
DR   PROSITE; PS00018; EF_HAND_1; 3.
DR   PROSITE; PS50222; EF_HAND_2; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Cell membrane;
KW   Ion transport; Ionic channel; Membrane; Potassium; Potassium channel;
KW   Potassium transport; Repeat; Transport; Voltage-gated channel.
FT   CHAIN         1    250       Kv channel-interacting protein 4.
FT                                /FTId=PRO_0000073827.
FT   DOMAIN       61    117       EF-hand 1; degenerate.
FT   DOMAIN      120    155       EF-hand 2.
FT   DOMAIN      156    191       EF-hand 3.
FT   DOMAIN      204    239       EF-hand 4.
FT   CA_BIND     133    144       1 (Potential).
FT   CA_BIND     169    180       2 (By similarity).
FT   CA_BIND     217    228       3 (By similarity).
FT   REGION        2     44       KIS.
FT   REGION      237    250       Interaction with KCND2 (By similarity).
FT   VAR_SEQ       1     62       Missing (in isoform 3).
FT                                /FTId=VSP_015069.
FT   VAR_SEQ       1     55       MNVRRVESISAQLEEASSTGGFLYAQNNTKRSIKERLMKLL
FT                                PCSAAKTSSPAIQN -> MNLEGLEMIAVLIVIVLFVKLLE
FT                                QFGLIEAGLED (in isoform 4).
FT                                /FTId=VSP_015070.
FT   VAR_SEQ      21     55       GFLYAQNNTKRSIKERLMKLLPCSAAKTSSPAIQN -> D
FT                                (in isoform 2).
FT                                /FTId=VSP_015071.
FT   CONFLICT     32     32       S -> T (in Ref. 1; AAG36976).
FT   CONFLICT     67     67       R -> K (in Ref. 4; BAC30218).
FT   HELIX        57     61
FT   HELIX        69     91
FT   HELIX        95     97
FT   HELIX       105    115
FT   HELIX       121    130
FT   HELIX       143    146
FT   HELIX       150    153
FT   HELIX       157    168
FT   HELIX       178    191
FT   HELIX       208    216
FT   HELIX       226    234
FT   HELIX       237    246
SQ   SEQUENCE   250 AA;  28756 MW;  56542298021192BF CRC64;
     MNVRRVESIS AQLEEASSTG GFLYAQNNTK RSIKERLMKL LPCSAAKTSS PAIQNSVEDE
     LEMATVRHRP EALELLEAQS KFTKKELQIL YRGFKNECPS GVVNEETFKE IYSQFFPQGD
     STTYAHFLFN AFDTDHNGAV SFEDFIKGLS ILLRGTVQEK LNWAFNLYDI NKDGYITKEE
     MLDIMKAIYD MMGKCTYPVL KEDAPRQHVE TFFQKMDKNK DGVVTIDEFI ESCQKDENIM
     RSMQLFENVI
//
ID   Q6PI88_MOUSE            Unreviewed;       483 AA.
AC   Q6PI88;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 47.
DE   SubName: Full=Zinc finger protein 358;
GN   Name=Zfp358;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II;
RC   TISSUE=Mammary tumor metastatized to lung. MMTV-LTR/Wnt1 model.
RC   Expression driven by an MMTV-LTR enhancer.;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC040067; AAH40067.1; -; mRNA.
DR   IPI; IPI00124688; -.
DR   UniGene; Mm.299073; -.
DR   HSSP; P08046; 1A1G.
DR   ProteinModelPortal; Q6PI88; -.
DR   SMR; Q6PI88; 80-313.
DR   Ensembl; ENSMUST00000061508; ENSMUSP00000060344; ENSMUSG00000047264.
DR   MGI; MGI:2153740; Zfp358.
DR   eggNOG; roNOG05157; -.
DR   HOVERGEN; HBG018163; -.
DR   InParanoid; Q6PI88; -.
DR   OrthoDB; EOG483D4J; -.
DR   ArrayExpress; Q6PI88; -.
DR   Bgee; Q6PI88; -.
DR   Genevestigator; Q6PI88; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 9.
DR   Pfam; PF00096; zf-C2H2; 5.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   483 AA;  50164 MW;  E732A2675F5D32BD CRC64;
     MSSSFDLDPD PDVIGPVPLV LDPSNDTPSP AAPDVDSLPS GLTATPEILA TSPAVLPAPA
     SPPRPFSCPD CGRAFRRSSG LSQHRRTHSG EKPYRCPDCG KSFSHGATLA QHRGIHTGAR
     PYQCAACGKA FGWRSTLLKH RSSHSGEKPH HCPVCGKAFG HGSLLAQHLR THGGPRPHKC
     PVCAKGFGQG SALLKHLRTH TGERPYPCPQ CGKAFGQSSA LLQHQRTHTA ERPYRCPHCG
     KAFGQSSNLQ HHLRIHTGER PYACPHCSKA FGQSSALLQH LHVHSGERPY RCQLCGKAFG
     QASSLTKHKR VHEGAAAAAA AAAAAAAAAA TAAGLGLGSG LSPVSMMRPG QISFLGPDAV
     SVLESGLGLS SGASSARSSA PTSVLGSLQN PILQTHSGSI SSPDLVLSSD PKPGHVADPD
     VVPSPDQESD PSPNPDLVPS PDPKPKSQTD PCSPTHDSSS PALPTGESPK WVKEEGALLG
     PDG
//
ID   AT1A3_MOUSE             Reviewed;        1013 AA.
AC   Q6PIC6;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-3;
DE            Short=Na(+)/K(+) ATPase alpha-3 subunit;
DE            EC=3.6.3.9;
DE   AltName: Full=Na(+)/K(+) ATPase alpha(III) subunit;
DE   AltName: Full=Sodium pump subunit alpha-3;
GN   Name=Atp1a3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 21-27; 36-81; 153-163; 168-184; 203-254; 260-271;
RP   350-367; 404-420; 425-434; 436-458; 466-492; 517-557; 587-595;
RP   603-615; 620-648; 652-682; 689-764; 878-901; 931-940; 943-969 AND
RP   1001-1009.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15648052; DOI=10.1002/pmic.200401066;
RA   Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA   Hart G.W., Burlingame A.L.;
RT   "Quantitative analysis of both protein expression and serine /
RT   threonine post-translational modifications through stable isotope
RT   labeling with dithiothreitol.";
RL   Proteomics 5:388-398(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-493; TYR-548 AND
RP   TYR-549, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-368, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: This is the catalytic component of the active enzyme,
CC       which catalyzes the hydrolysis of ATP coupled with the exchange of
CC       sodium and potassium ions across the plasma membrane. This action
CC       creates the electrochemical gradient of sodium and potassium ions,
CC       providing the energy for active transport of various nutrients (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + Na(+)(In) + K(+)(Out) = ADP +
CC       phosphate + Na(+)(Out) + K(+)(In).
CC   -!- SUBUNIT: Composed of three subunits: alpha (catalytic), beta and
CC       gamma (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       (TC 3.A.3) family. Type IIC subfamily.
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DR   EMBL; BC034645; AAH34645.1; -; mRNA.
DR   EMBL; BC037206; AAH37206.1; -; mRNA.
DR   EMBL; BC042894; AAH42894.1; -; mRNA.
DR   IPI; IPI00122048; -.
DR   UniGene; Mm.44101; -.
DR   ProteinModelPortal; Q6PIC6; -.
DR   SMR; Q6PIC6; 16-1013.
DR   STRING; Q6PIC6; -.
DR   PhosphoSite; Q6PIC6; -.
DR   PRIDE; Q6PIC6; -.
DR   Ensembl; ENSMUST00000080882; ENSMUSP00000079691; ENSMUSG00000040907.
DR   UCSC; uc009frf.1; mouse.
DR   MGI; MGI:88107; Atp1a3.
DR   eggNOG; roNOG12622; -.
DR   HOVERGEN; HBG004298; -.
DR   OrthoDB; EOG46MBHS; -.
DR   PhylomeDB; Q6PIC6; -.
DR   BRENDA; 3.6.3.9; 244.
DR   ArrayExpress; Q6PIC6; -.
DR   Bgee; Q6PIC6; -.
DR   CleanEx; MM_ATP1A3; -.
DR   Genevestigator; Q6PIC6; -.
DR   GermOnline; ENSMUSG00000040907; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005391; F:sodium:potassium-exchanging ATPase activity; ISS:UniProtKB.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IMP:MGI.
DR   GO; GO:0007613; P:memory; IMP:MGI.
DR   GO; GO:0042493; P:response to drug; IMP:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   InterPro; IPR023306; ATPase_cation_domN.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR005775; ATPase_P-typ_cation-ex_asu_euk.
DR   InterPro; IPR006069; ATPase_P-typ_cation-exchng_asu.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023300; ATPase_P-typ_cyto_domA.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Gene3D; G3DSA:2.70.150.10; ATPase_P-typ_cyto_domA; 1.
DR   Gene3D; G3DSA:3.40.1110.10; ATPase_P-typ_cyto_domN; 1.
DR   Gene3D; G3DSA:1.20.1110.10; ATPase_P-typ_TM_dom; 2.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00121; NAKATPASE.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81660; ATPase_cation_domN; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01106; ATPase-IIC_X-K; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 4.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Direct protein sequencing; Hydrolase;
KW   Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Potassium; Potassium transport; Sodium;
KW   Sodium transport; Sodium/potassium transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1   1013       Sodium/potassium-transporting ATPase
FT                                subunit alpha-3.
FT                                /FTId=PRO_0000046299.
FT   TOPO_DOM      1     77       Cytoplasmic (Potential).
FT   TRANSMEM     78     98       Helical; (Potential).
FT   TOPO_DOM     99    121       Extracellular (Potential).
FT   TRANSMEM    122    142       Helical; (Potential).
FT   TOPO_DOM    143    278       Cytoplasmic (Potential).
FT   TRANSMEM    279    298       Helical; (Potential).
FT   TOPO_DOM    299    310       Extracellular (Potential).
FT   TRANSMEM    311    328       Helical; (Potential).
FT   TOPO_DOM    329    762       Cytoplasmic (Potential).
FT   TRANSMEM    763    782       Helical; (Potential).
FT   TOPO_DOM    783    792       Extracellular (Potential).
FT   TRANSMEM    793    813       Helical; (Potential).
FT   TOPO_DOM    814    833       Cytoplasmic (Potential).
FT   TRANSMEM    834    856       Helical; (Potential).
FT   TOPO_DOM    857    908       Extracellular (Potential).
FT   TRANSMEM    909    928       Helical; (Potential).
FT   TOPO_DOM    929    941       Cytoplasmic (Potential).
FT   TRANSMEM    942    960       Helical; (Potential).
FT   TOPO_DOM    961    975       Extracellular (Potential).
FT   TRANSMEM    976    996       Helical; (Potential).
FT   TOPO_DOM    997   1013       Cytoplasmic (Potential).
FT   REGION       72     74       Interaction with phosphoinositide-3
FT                                kinase (By similarity).
FT   ACT_SITE    366    366       4-aspartylphosphate intermediate (By
FT                                similarity).
FT   METAL       707    707       Magnesium (By similarity).
FT   METAL       711    711       Magnesium (By similarity).
FT   MOD_RES     265    265       Phosphoserine.
FT   MOD_RES     368    368       Phosphothreonine.
FT   MOD_RES     493    493       Phosphotyrosine.
FT   MOD_RES     548    548       Phosphotyrosine.
FT   MOD_RES     549    549       Phosphotyrosine.
FT   MOD_RES     933    933       Phosphoserine; by PKA (By similarity).
SQ   SEQUENCE   1013 AA;  111692 MW;  72F051406284EA8A CRC64;
     MGDKKDDKSS PKKSKAKERR DLDDLKKEVA MTEHKMSVEE VCRKYNTDCV QGLTHSKAQE
     ILARDGPNAL TPPPTTPEWV KFCRQLFGGF SILLWIGAIL CFLAYGIQAG TEDDPSGDNL
     YLGIVLAAVV IITGCFSYYQ EAKSSKIMES FKNMVPQQAL VIREGEKMQV NAEEVVVGDL
     VEIKGGDRVP ADLRIISAHG CKVDNSSLTG ESEPQTRSPD CTHDNPLETR NITFFSTNCV
     EGTARGVVVA TGDRTVMGRI ATLASGLEVG KTPIAIEIEH FIQLITGVAV FLGVSFFILS
     LILGYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN LEAVETLGST
     STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTEDQSGTS FDKSSHTWVA LSHIAGLCNR
     AVFKGGQDNI PVLKRDVAGD ASESALLKCI ELSSGSVKLM RERNKKVAEI PFNSTNKYQL
     SIHETEDPND NRYLLVMKGA PERILDRCAT ILLQGKEQPL DEEMKEAFQN AYLELGGLGE
     RVLGFCHYYL PEEQFPKGFA FDCDDVNFTT DNLCFVGLMS MIDPPRAAVP DAVGKCRSAG
     IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVSQVNPRDA KACVIHGTDL
     KDFTSEQIDE ILQNHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN DSPALKKADI
     GVAMGIAGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL TSNIPEITPF
     LLFIMANIPL PLGTITILCI DLGTDMVPAI SLAYEAAESD IMKRQPRNPR TDKLVNERLI
     SMAYGQIGMI QALGGFFSYF VILAENGFLP GNLVGIRLNW DDRTVNDLED SYGQQWTYEQ
     RKVVEFTCHT AFFVSIVVVQ WADLIICKTR RNSVFQQGMK NKILIFGLFE ETALAAFLSY
     CPGMDVALRM YPLKPSWWFC AFPYSFLIFV YDEIRKLILR RNPGGWVEKE TYY
//
ID   AT1A2_MOUSE             Reviewed;        1020 AA.
AC   Q6PIE5; Q80UZ8;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-2;
DE            Short=Na(+)/K(+) ATPase alpha-2 subunit;
DE            EC=3.6.3.9;
DE   AltName: Full=Na(+)/K(+) ATPase alpha(+) subunit;
DE   AltName: Full=Sodium pump subunit alpha-2;
DE   Flags: Precursor;
GN   Name=Atp1a2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 44-59; 73-89; 161-171; 176-192; 211-238; 254-262;
RP   358-375; 413-428; 433-442; 444-456; 475-485; 494-505; 524-561;
RP   565-602; 610-622; 627-655; 659-680; 696-771; 891-908; 938-947 AND
RP   1008-1016.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-650, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: This is the catalytic component of the active enzyme,
CC       which catalyzes the hydrolysis of ATP coupled with the exchange of
CC       sodium and potassium ions across the plasma membrane. This action
CC       creates the electrochemical gradient of sodium and potassium ions,
CC       providing the energy for active transport of various nutrients (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + Na(+)(In) + K(+)(Out) = ADP +
CC       phosphate + Na(+)(Out) + K(+)(In).
CC   -!- SUBUNIT: Composed of three subunits: alpha (catalytic), beta and
CC       gamma (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity). Cell membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       (TC 3.A.3) family. Type IIC subfamily.
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DR   EMBL; BC036127; AAH36127.1; -; mRNA.
DR   EMBL; BC041774; AAH41774.1; -; mRNA.
DR   IPI; IPI00420569; -.
DR   RefSeq; NP_848492.1; NM_178405.3.
DR   UniGene; Mm.207432; -.
DR   ProteinModelPortal; Q6PIE5; -.
DR   SMR; Q6PIE5; 25-1020.
DR   DIP; DIP-48355N; -.
DR   STRING; Q6PIE5; -.
DR   PhosphoSite; Q6PIE5; -.
DR   PRIDE; Q6PIE5; -.
DR   Ensembl; ENSMUST00000085913; ENSMUSP00000083077; ENSMUSG00000007097.
DR   GeneID; 98660; -.
DR   KEGG; mmu:98660; -.
DR   UCSC; uc007dqc.1; mouse.
DR   CTD; 98660; -.
DR   MGI; MGI:88106; Atp1a2.
DR   HOVERGEN; HBG004298; -.
DR   InParanoid; Q6PIE5; -.
DR   OMA; KIQINAE; -.
DR   OrthoDB; EOG46MBHS; -.
DR   BRENDA; 3.6.3.9; 244.
DR   NextBio; 353565; -.
DR   ArrayExpress; Q6PIE5; -.
DR   Bgee; Q6PIE5; -.
DR   CleanEx; MM_ATP1A2; -.
DR   Genevestigator; Q6PIE5; -.
DR   GermOnline; ENSMUSG00000007097; Mus musculus.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0005391; F:sodium:potassium-exchanging ATPase activity; ISS:UniProtKB.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   GO; GO:0040011; P:locomotion; IMP:MGI.
DR   GO; GO:0045822; P:negative regulation of heart contraction; IMP:MGI.
DR   GO; GO:0045988; P:negative regulation of striated muscle contraction; IMP:MGI.
DR   GO; GO:0001504; P:neurotransmitter uptake; IMP:MGI.
DR   GO; GO:0051481; P:reduction of cytosolic calcium ion concentration; IMP:MGI.
DR   GO; GO:0008217; P:regulation of blood pressure; IGI:MGI.
DR   GO; GO:0002087; P:regulation of respiratory gaseous exchange by neurological system process; IMP:MGI.
DR   GO; GO:0006940; P:regulation of smooth muscle contraction; IMP:MGI.
DR   GO; GO:0002026; P:regulation of the force of heart contraction; IMP:MGI.
DR   GO; GO:0019229; P:regulation of vasoconstriction; IGI:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   InterPro; IPR023306; ATPase_cation_domN.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR005775; ATPase_P-typ_cation-ex_asu_euk.
DR   InterPro; IPR006069; ATPase_P-typ_cation-exchng_asu.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023300; ATPase_P-typ_cyto_domA.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Gene3D; G3DSA:2.70.150.10; ATPase_P-typ_cyto_domA; 1.
DR   Gene3D; G3DSA:3.40.1110.10; ATPase_P-typ_cyto_domN; 1.
DR   Gene3D; G3DSA:1.20.1110.10; ATPase_P-typ_TM_dom; 2.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00121; NAKATPASE.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81660; ATPase_cation_domN; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01106; ATPase-IIC_X-K; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 4.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Direct protein sequencing; Hydrolase;
KW   Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Potassium; Potassium transport; Sodium;
KW   Sodium transport; Sodium/potassium transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   PROPEP        1      5       By similarity.
FT                                /FTId=PRO_0000002505.
FT   CHAIN         6   1020       Sodium/potassium-transporting ATPase
FT                                subunit alpha-2.
FT                                /FTId=PRO_0000002506.
FT   TOPO_DOM      6     85       Cytoplasmic (Potential).
FT   TRANSMEM     86    106       Helical; (Potential).
FT   TOPO_DOM    107    129       Extracellular (Potential).
FT   TRANSMEM    130    150       Helical; (Potential).
FT   TOPO_DOM    151    286       Cytoplasmic (Potential).
FT   TRANSMEM    287    306       Helical; (Potential).
FT   TOPO_DOM    307    318       Extracellular (Potential).
FT   TRANSMEM    319    336       Helical; (Potential).
FT   TOPO_DOM    337    769       Cytoplasmic (Potential).
FT   TRANSMEM    770    789       Helical; (Potential).
FT   TOPO_DOM    790    799       Extracellular (Potential).
FT   TRANSMEM    800    820       Helical; (Potential).
FT   TOPO_DOM    821    840       Cytoplasmic (Potential).
FT   TRANSMEM    841    863       Helical; (Potential).
FT   TOPO_DOM    864    915       Extracellular (Potential).
FT   TRANSMEM    916    935       Helical; (Potential).
FT   TOPO_DOM    936    948       Cytoplasmic (Potential).
FT   TRANSMEM    949    967       Helical; (Potential).
FT   TOPO_DOM    968    982       Extracellular (Potential).
FT   TRANSMEM    983   1003       Helical; (Potential).
FT   TOPO_DOM   1004   1020       Cytoplasmic (Potential).
FT   REGION       80     82       Interaction with phosphoinositide-3
FT                                kinase (By similarity).
FT   ACT_SITE    374    374       4-aspartylphosphate intermediate (By
FT                                similarity).
FT   METAL       714    714       Magnesium (By similarity).
FT   METAL       718    718       Magnesium (By similarity).
FT   MOD_RES     570    570       Phosphothreonine (By similarity).
FT   MOD_RES     587    587       Phosphoserine (By similarity).
FT   MOD_RES     650    650       Phosphoserine.
FT   MOD_RES     940    940       Phosphoserine; by PKA (By similarity).
SQ   SEQUENCE   1020 AA;  112217 MW;  5436E795BD5B4CFA CRC64;
     MGRGAGREYS PAATTAENGG GKKKQKEKEL DELKKEVAMD DHKLSLDELG RKYQVDLSKG
     LTNQRAQDIL ARDGPNALTP PPTTPEWVKF CRQLFGGFSI LLWIGALLCF LAYGILAAME
     DEPSNDNLYL GIVLAAVVIV TGCFSYYQEA KSSKIMDSFK NMVPQQALVI REGEKMQINA
     EEVVVGDLVE VKGGDRVPAD LRIISSHGCK VDNSSLTGES EPQTRSPEFT HENPLETRNI
     CFFSTNCVEG TARGIVIATG DRTVMGRIAT LASGLEVGQT PIAMEIEHFI QLITGVAVFL
     GVSFFVLSLI LGYSWLEAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA RKNCLVKNLE
     AVETLGSTST ICSDKTGTLT QNRMTVAHMW FDNQIHEADT TEDQSGATFD KRSPTWTALS
     RIAGLCNRAV FKAGQENISV SKRDTAGDAS ESALLKCIEL SCGSVRKMRD RNPKVAEIPF
     NSTNKYQLSI HEREDSPQSH VLVMKGAPER ILDRCSTILV QGKEIPLDKE MQDAFQNAYM
     ELGGLGERVL GFCQLNLPSG KFPRGFKFDT DELNFPTEKL CFVGLMSMID PPRAAVPDAV
     GKCRSAGIKV IMVTGDHPIT AKAIAKGVGI ISEGNETVED IAARLNIPVS QVNPREAKAC
     VVHGSDLKDM TSEQLDEILR DHTEIVFART SPQQKLIIVE GCQRQGAIVA VTGDGVNDSP
     ALKKADIGIA MGISGSDVSK QAADMILLDD NFASIVTGVE EGRLIFDNLK KSIAYTLTSN
     IPEITPFLLF IIANIPLPLG TVTILCIDLG TDMVPAISLA YEAAESDIMK RQPRNSQTDK
     LVNERLISMA YGQIGMIQAL GGFFTYFVIL AENGFLPSRL LGIRLDWDDR TTNDLEDSYG
     QEWTYEQRKV VEFTCHTAFF ASIVVVQWAD LIICKTRRNS VFQQGMKNKI LIFGLLEETA
     LAAFLSYCPG MGVALRMYPL KVTWWFCAFP YSLLIFIYDE VRKLILRRYP GGWVEKETYY
//
ID   YJ005_MOUSE             Reviewed;         354 AA.
AC   Q6PIU9; Q8BPJ9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   08-MAR-2011, entry version 39.
DE   RecName: Full=Uncharacterized protein FLJ45252 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 197-354.
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 200-354.
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-291, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-291 AND SER-292, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- CAUTION: Found in the 3'-UTR of AAK1 but there is evidence for the
CC       existence of the protein from a number of proteomics studies.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH28270.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC       Sequence=BAC35570.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; AC159712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK053876; BAC35570.1; ALT_INIT; mRNA.
DR   EMBL; BC028270; AAH28270.2; ALT_INIT; mRNA.
DR   IPI; IPI00874995; -.
DR   UniGene; Mm.221038; -.
DR   PRIDE; Q6PIU9; -.
DR   Ensembl; ENSMUST00000116070; ENSMUSP00000111752; ENSMUSG00000079954.
DR   eggNOG; roNOG16453; -.
DR   GeneTree; ENSGT00390000008255; -.
DR   HOVERGEN; HBG108721; -.
DR   InParanoid; Q6PIU9; -.
DR   OrthoDB; EOG408N93; -.
DR   NextBio; 456554; -.
DR   ArrayExpress; Q6PIU9; -.
DR   Bgee; Q6PIU9; -.
DR   Genevestigator; Q6PIU9; -.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    354       Uncharacterized protein FLJ45252 homolog.
FT                                /FTId=PRO_0000325933.
FT   MOD_RES      66     66       Phosphoserine (By similarity).
FT   MOD_RES     115    115       Phosphoserine.
FT   MOD_RES     156    156       Phosphoserine (By similarity).
FT   MOD_RES     174    174       Phosphoserine (By similarity).
FT   MOD_RES     285    285       Phosphoserine (By similarity).
FT   MOD_RES     291    291       Phosphotyrosine.
FT   MOD_RES     292    292       Phosphoserine.
FT   MOD_RES     298    298       Phosphoserine (By similarity).
SQ   SEQUENCE   354 AA;  37705 MW;  7F25C49F1522CAA0 CRC64;
     MGTKGLPLYP DPCRAPGTKT QNTLASDSLA REGPSSNSSF HSSEEEGTDL EGDMLDCSGS
     RPLLESEEED ENCRPLQEKL GEAALFSESG VCTEPEERGQ GGKKSQFLPI NQRASDDLGE
     PDVFATAPFR SSLVPADDVD IFSKAPFVSK GSVAPSQMDE VDVFSRAPFT KKRSMEEFLA
     VQGSSQDLPM QANLSQSNEG PLLAGRDRAI YTPAQAQYPM TGFAPQAGLP SHSVQVADHF
     DGNSPRGSPM SSGGHPVDRN RGLQPQKEAF SGPAAGKPFH PQALSKYSRH YSPEDELSAE
     AQPIAAYKIV SQSNKQLLAG SVSVTSLSSR TTELATADPF ALAPFPSKAG KQKP
//
ID   DMXL1_MOUSE             Reviewed;        3013 AA.
AC   Q6PNC0; Q3TLG8; Q6PHM6; Q8BQF2;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=DmX-like protein 1;
DE            Short=X-like 1 protein;
GN   Name=Dmxl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/Sv; TISSUE=Embryonic stem cell;
RA   Bikar S.E., Kraemer C., Schmidt E.R.;
RT   "Mus musculus mRNA for Dmx-like 1 protein.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1916-3013.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2719-3013.
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-915, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SIMILARITY: Contains 15 WD repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE38824.1; Type=Erroneous initiation;
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DR   EMBL; AY590892; AAT01618.1; -; mRNA.
DR   EMBL; BC056490; AAH56490.1; -; mRNA.
DR   EMBL; AK050888; BAC34446.1; -; mRNA.
DR   EMBL; AK166520; BAE38824.1; ALT_INIT; mRNA.
DR   IPI; IPI00674554; -.
DR   UniGene; Mm.257790; -.
DR   ProteinModelPortal; Q6PNC0; -.
DR   SMR; Q6PNC0; 110-135, 168-194, 227-267, 1135-1163, 2744-2994.
DR   STRING; Q6PNC0; -.
DR   PhosphoSite; Q6PNC0; -.
DR   PRIDE; Q6PNC0; -.
DR   Ensembl; ENSMUST00000041772; ENSMUSP00000045559; ENSMUSG00000037416.
DR   UCSC; uc008ewn.1; mouse.
DR   MGI; MGI:2443926; Dmxl1.
DR   eggNOG; roNOG04652; -.
DR   GeneTree; ENSGT00390000000096; -.
DR   HOGENOM; HBG403190; -.
DR   HOVERGEN; HBG079593; -.
DR   InParanoid; Q6PNC0; -.
DR   OrthoDB; EOG44J2H3; -.
DR   PhylomeDB; Q6PNC0; -.
DR   ArrayExpress; Q6PNC0; -.
DR   Bgee; Q6PNC0; -.
DR   CleanEx; MM_DMXL1; -.
DR   Genevestigator; Q6PNC0; -.
DR   GermOnline; ENSMUSG00000037416; Mus musculus.
DR   InterPro; IPR022033; Rav1p_C.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 5.
DR   Pfam; PF12234; Rav1p_C; 1.
DR   Pfam; PF00400; WD40; 4.
DR   SMART; SM00320; WD40; 10.
DR   SUPFAM; SSF50978; WD40_like; 2.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Repeat; WD repeat.
FT   CHAIN         1   3013       DmX-like protein 1.
FT                                /FTId=PRO_0000223323.
FT   REPEAT      108    145       WD 1.
FT   REPEAT      164    204       WD 2.
FT   REPEAT      227    275       WD 3.
FT   REPEAT      474    514       WD 4.
FT   REPEAT      578    619       WD 5.
FT   REPEAT      842    893       WD 6.
FT   REPEAT      970   1008       WD 7.
FT   REPEAT     1145   1193       WD 8.
FT   REPEAT     1208   1248       WD 9.
FT   REPEAT     2728   2769       WD 10.
FT   REPEAT     2771   2810       WD 11.
FT   REPEAT     2822   2864       WD 12.
FT   REPEAT     2870   2909       WD 13.
FT   REPEAT     2912   2951       WD 14.
FT   REPEAT     2964   3002       WD 15.
FT   MOD_RES     434    434       Phosphoserine.
FT   MOD_RES     913    913       Phosphotyrosine (By similarity).
FT   MOD_RES     915    915       Phosphoserine.
FT   MOD_RES     922    922       Phosphoserine (By similarity).
FT   MOD_RES    1899   1899       Phosphothreonine (By similarity).
FT   MOD_RES    1965   1965       Phosphoserine (By similarity).
FT   CONFLICT   2812   2812       S -> N (in Ref. 3; BAE38824).
FT   CONFLICT   2944   2944       S -> L (in Ref. 3; BAE38824).
SQ   SEQUENCE   3013 AA;  336008 MW;  3C57BD3218EE748D CRC64;
     MNLHQVLTGA VNPGDHCFAV GSVGEQRFTA YASGCDIVIL GSNFERLQII PGAKHGNIQV
     GCVDCSMQQG KIAASYGNVI SVFEPVSLPK KRKNLEFYSQ WQKSGQFFLD SIAHNITWDP
     AGNRLLTGSS CLQLWCNSRK QTEDENPDKT DLNFGNWMCI WHCKTASQVH LMKFSPDGEF
     FATAGKDDCL LKVWYNVENW RPAVTSPDKN SEKQSQGEID FSFVYLAHPR AVNGFSWRKT
     SKYMPRASVC NVLLTCCKDN VCRLWVETFL PNDCFLYGSD CNHWCEPVSL TNNLKRNASS
     KDRVQSALEV NLRPFRRGRS RSLALVAHTG YLPHQQDPHH AHRNTPLHAN ALCHFHIAAS
     INPATDIPLL PSITSLSLNE NEEKCGPFVV HWLNNKELHF TLSMEVFLQQ LRKSFEQPSS
     EASVEDSIQA DLKSDEELDD GVDDLKINHE KKELDEDKML PSSSFTPLSS AAVDHQIEVL
     LSEWSKNADM LFSIHPMDGS LLVWHVDWLD EYQPGMFRQV QVSFVSRIPV AFPTGDANSL
     CKSIVMYACT KNVDLAIQQG KQRPTGLTRS TSMLISSAHS KSSNNLKLSI FTPNVMMISK
     HADGSLNQWL VSFAEESAFS TVLSISHKSR YCGHRFHLND LACHSVLPLL LTTSHHNALR
     TPNVGNQKQA HDAVNTEECS LAQQNKSNVD MAFQDPNAIY SELILWRVDP VGPLSFSGGV
     SELARINSLH VSAFSNVAWL PTLIPSYCLG AYCNSPSACF VASDGQYLRL YEAVIDAKKL
     LYELSNPEIS KYVGEVFNIV SQQSTARPGC IIALDSITKL HGRKTQLLHV FQEDFILNNL
     EKKRLGVDNI LLDSDSSCNG FSEKFYLVVI ECTEDNRSLL RMWDLHLRST PVSLDERIDT
     KISEASWLPE EHYSSSPEKI LSPFSQKFQA CRANLQSTSK LSLFSEMVYS KELDLPEGVE
     IISVKPSAGH LSSSSIYPVC SAPYLLATSC SDDKVRFWRC RVTNGESATS KNGKLDVVYV
     WEEWPLLIED GLENNSSVTV PGRPVEVSCA HTSRLAVAYK QPTGNSRSQE FVMHVSIFEC
     ESTGGSCWIL EQTIHLDELS TVLDSGISID SNLVAYNKQE TYLVSKESIT SNTKHLVHLD
     WMSREDGSHI LTVGIGSKLF MYGPMAGKVQ DQTGKENQAF PLWDSTKIVP LSKFVLLRSV
     DLVSSVEGAP PFPVSLSWVR DGILVVGMDC EMHVYSQWQP SNKQEPVISE SYNGSTPSIL
     SLIKQSNSSS SGLHPPKKTL TRSMTSLAQK ICGKKSIFDP SVDMEDSGLF EAAHVLSPTL
     PQYHPLQLLE LMDLGKVRRA KAILSHLVKC IAGEVVALNE AESNHERRLR SLTISASGST
     TRDPQAFNKA DSRDYTEIDS VPPLPLYALL AADDDSYCSS LEKTGSESSL KKSKQLSKES
     YDELFQTSVL MSDNHMLETD EENTQPRVID LSQYSPTYFG PEHAQVLSGH LLHSSLPGLT
     RMEQMSLMAL ADTIATTSTD IGESRDRNQG GETLDECGLK FLLAVRLHTF LTTSLPAYRA
     QLLHQGLSTG HFAWAFHSVA EEELLNMLPA MQKDDPTWSE LRAMGVGWWV RNARILRRCI
     EKVAKAAFHR NNDPLDAAIF YLAMKKKAVI WGLYRSQKDT KMTQFFGHNF EEERWRKAAL
     KNAFSLLGKQ RFEHSAAFFL LGGCLKDAIE VCLEKLNDIQ LALVIARLFE SEFDKSATYK
     SILRKKVLGI GSPASELSSS SINAHHDPFL RSMAHWILED YSAALETLIK QPVTEDEDQV
     MMSACNPIVF NFYNYLRTHP LLLRRHFGSS SETFSTHMTL AGKSGLAGTI NLSERRLFFT
     TASAHLKAGC PMLALEVLSK MPKVSKKAKP CCRGSSFLTS KDSSLKLDVR EDKCCAADWS
     PSLTNGLESS SEGSSERHSH STLSFDWSQP SVVFQDDSLE LKWDSDNDEE NEDPPISMKE
     IRPLQRKTVK EIDELSSYTD SLSTLDENDI LNPSEDIIAV QLKFRACLKI LTVELRTLST
     GYEIDGGKLR YQLYHWLEKE VVALQRTCDF CSDADQLQTT FSQSADESGS TEDADDLHHQ
     TKVKQLRESF QEKRQWLLKY QSLLRMFLSY CVLHGSHGGG LASVRMELIL LLQESQQETA
     EPIFSNPLSE QTSVPLLFAC TASAKTVVAN PLLHLSNLTH DILHAIINFD SPPHPDSQTN
     KVYVMHTLAA SLSACIYQCL CGSHNYSSFQ TNQFTGMVYQ TVLLAHRHSL RTGSLDESVT
     PNTSPAQWPG INFLIQLLNS SGEEAQSGLT VLLCEILTAV YLSLFIHGLA THSSNELFRI
     VAHPLNEKMW SAVFGGGAHV PSKGQANSKA LSVEGEKQNR HISPSKVSAR ESPVSSSSGN
     QEPPAVKEKF VPPELSIWDY FIAKPFLPPS QSRAEYDSEE SLESDDEEEE DDDDALPSGL
     QLHEHSNSNS FSWSLMRLAM VQLVLNNLKT FYPFAGHDLA ELPVSSPLCH AVLKTLQCWE
     QVLLRRLEIH GGPPQNYISS HTSEENVSAG PAILRHKALL EPTNTPFKSK NHLALSVKRL
     WQYLVKQEEI QETFIRNIFT KKRCLNEIEA DLGYPGGKAR IIHKESDIIT AFAVNRANRN
     CIAIASSHDV QELDVSAILA TQIYTWVDDD TETETKGSED FLVIHARDDL SAVQGSTPYT
     HSNPGTPINM PWLGSTQTGR GASVMLKKAI NNVRRMTSHP TLPYYLTGAQ DGSVRMFEWG
     HSQQITCFRS GGNSRITRMR FNYQGNKFGI VDADGYLSLY QTNWKCCPVT GSMPKPYLAW
     QCHNKTANDF VFVSSSSLIA TAGLSSDNRN ICLWDTLVAP ANSLVHAFTC HDSGATVLAY
     APKHQLLISG GRKGFTCIFD LRQRQQRQLF QSHDSPVKAI AIDPTEEYFV TGSAEGNIKI
     WSLSSFSLLH TFINEHARQS IFRNIGTGVM QIETGPANHI FSCGADGTMK MRILPDQFSP
     LNEVLKNDVK FML
//
ID   Q6Q476_MOUSE            Unreviewed;       104 AA.
AC   Q6Q476;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   SubName: Full=Plasma membrane Ca++ transporting ATPase 4 splice variant a;
DE   Flags: Fragment;
GN   Name=Atp2b4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c;
RX   PubMed=15078889; DOI=10.1074/jbc.M312599200;
RA   Schuh K., Cartwright E.J., Jankevics E., Bundschu K., Liebermann J.,
RA   Williams J.C., Armesilla A.L., Emerson M., Oceandy D., Knobeloch K.P.,
RA   Neyses L.;
RT   "Plasma membrane Ca2+ ATPase 4 is required for sperm motility and male
RT   fertility.";
RL   J. Biol. Chem. 279:28220-28226(2004).
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DR   EMBL; AY560896; AAT01507.1; -; mRNA.
DR   IPI; IPI00463589; -.
DR   UniGene; Mm.440679; -.
DR   STRING; Q6Q476; -.
DR   Ensembl; ENSMUST00000125659; ENSMUSP00000116941; ENSMUSG00000026463.
DR   UCSC; uc007cqu.1; mouse.
DR   MGI; MGI:88111; Atp2b4.
DR   GeneTree; ENSGT00510000046331; -.
DR   ArrayExpress; Q6Q476; -.
DR   Bgee; Q6Q476; -.
DR   Genevestigator; Q6Q476; -.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:MGI.
DR   GO; GO:0006816; P:calcium ion transport; TAS:MGI.
DR   InterPro; IPR022141; ATP_Ca_trans_C.
DR   Pfam; PF12424; ATP_Ca_trans_C; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   104 AA;  11521 MW;  EA99D8AFAC021B1F CRC64;
     DISRDTEGMD EIDLAEMELR RGQILWVRGL NRIQTQIDVI NKFQTEAPLK RVRENMTQHL
     DVKLVPSSYS AAVASLRTCP SISSAISSAV TSPPVGNQSR QTVP
//
ID   RICTR_MOUSE             Reviewed;        1708 AA.
AC   Q6QI06; Q0VAV4; Q69Z40; Q6PDL2; Q6RI74; Q8BPH9; Q8CBF2;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Rapamycin-insensitive companion of mTOR;
DE   AltName: Full=AVO3 homolog;
DE            Short=mAVO3;
DE   AltName: Full=Protein pianissimo;
GN   Name=Rictor; Synonyms=Kiaa1999;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND IDENTIFICATION IN TORC2
RP   COMPLEX.
RC   STRAIN=C3H;
RX   PubMed=15467718; DOI=10.1038/ncb1183;
RA   Jacinto E., Loewith R., Schmidt A., Lin S., Ruegg M.A., Hall A.,
RA   Hall M.N.;
RT   "Mammalian TOR complex 2 controls the actin cytoskeleton and is
RT   rapamycin insensitive.";
RL   Nat. Cell Biol. 6:1122-1128(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, IDENTIFICATION IN
RP   TORC2 COMPLEX, AND DISRUPTION PHENOTYPE.
RC   STRAIN=LAF1;
RX   PubMed=16962829; DOI=10.1016/j.devcel.2006.08.013;
RA   Shiota C., Woo J.-T., Lindner J., Shelton K.D., Magnuson M.A.;
RT   "Multiallelic disruption of the rictor gene in mice reveals that mTOR
RT   complex 2 is essential for fetal growth and viability.";
RL   Dev. Cell 11:583-589(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-825 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1347-1708 (ISOFORM 1/2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 826-1708 (ISOFORM 1/2).
RC   TISSUE=Thymus;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [6]
RP   FUNCTION.
RX   PubMed=16221682; DOI=10.1074/jbc.M508361200;
RA   Hresko R.C., Mueckler M.;
RT   "mTOR.RICTOR is the Ser473 kinase for Akt/protein kinase B in 3T3-L1
RT   adipocytes.";
RL   J. Biol. Chem. 280:40406-40416(2005).
RN   [7]
RP   FUNCTION, AND IDENTIFICATION IN TORC2 COMPLEX.
RX   PubMed=16962653; DOI=10.1016/j.cell.2006.08.033;
RA   Jacinto E., Facchinetti V., Liu D., Soto N., Wei S., Jung S.Y.,
RA   Huang Q., Qin J., Su B.;
RT   "SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt
RT   phosphorylation and substrate specificity.";
RL   Cell 127:125-137(2006).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17141160; DOI=10.1016/j.devcel.2006.10.007;
RA   Guertin D.A., Stevens D.M., Thoreen C.C., Burds A.A., Kalaany N.Y.,
RA   Moffat J., Brown M., Fitzgerald K.J., Sabatini D.M.;
RT   "Ablation in mice of the mTORC components raptor, rictor, or mLST8
RT   reveals that mTORC2 is required for signaling to Akt-FOXO and
RT   PKCalpha, but not S6K1.";
RL   Dev. Cell 11:859-871(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-1176, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Subunit of mTORC2, which regulates cell growth and
CC       survival in response to hormonal signals. mTORC2 is activated by
CC       growth factors, but, in contrast to mTORC1, seems to be nutrient-
CC       insensitive. mTORC2 seems to function upstream of Rho GTPases to
CC       regulate the actin cytoskeleton, probably by activating one or
CC       more Rho-type guanine nucleotide exchange factors. mTORC2 promotes
CC       the serum-induced formation of stress-fibers or F-actin. mTORC2
CC       plays a critical role in AKT1 'Ser-473' phosphorylation, which may
CC       facilitate the phosphorylation of the activation loop of AKT1 on
CC       'Thr-308' by PDK1 which is a prerequisite for full activation.
CC       mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2
CC       also modulates the phosphorylation of PRKCA on 'Ser-657'. Plays an
CC       essential role in embryonic growth and development.
CC   -!- SUBUNIT: Part of the mammalian target of rapamycin complex 2
CC       (mTORC2) which contains MTOR, LST8, PRR5, RICTOR and MAPKAP1.
CC       Contrary to mTORC1, mTORC2 does not bind to and is not sensitive
CC       to FKBP12-rapamycin. Binds directly to MTOR and PRR5 within the
CC       TORC2 complex. May interact with PRR5L.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6QI06-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6QI06-2; Sequence=VSP_052583;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated by MTOR; when part of mTORC2 (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice develop normally until E9.5, and then
CC       display growth arrest and embryonic lethality by E11.5.
CC   -!- SIMILARITY: Belongs to the pianissimo family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AY497009; AAR89074.1; -; mRNA.
DR   EMBL; AY540053; AAS46920.1; -; mRNA.
DR   EMBL; BC058643; AAH58643.1; -; mRNA.
DR   EMBL; BC120903; AAI20904.1; -; mRNA.
DR   EMBL; AK036149; BAC29321.2; -; mRNA.
DR   EMBL; AK075662; BAC35882.1; -; mRNA.
DR   EMBL; AK173326; BAD32604.1; -; mRNA.
DR   IPI; IPI00399440; -.
DR   IPI; IPI00869420; -.
DR   RefSeq; NP_084444.3; NM_030168.3.
DR   UniGene; Mm.275811; -.
DR   ProteinModelPortal; Q6QI06; -.
DR   DIP; DIP-46323N; -.
DR   STRING; Q6QI06; -.
DR   PhosphoSite; Q6QI06; -.
DR   PRIDE; Q6QI06; -.
DR   Ensembl; ENSMUST00000061656; ENSMUSP00000051809; ENSMUSG00000050310.
DR   GeneID; 78757; -.
DR   KEGG; mmu:78757; -.
DR   CTD; 78757; -.
DR   MGI; MGI:1926007; Rictor.
DR   HOVERGEN; HBG060827; -.
DR   InParanoid; Q6QI06; -.
DR   OrthoDB; EOG43XV2K; -.
DR   PhylomeDB; Q6QI06; -.
DR   NextBio; 349448; -.
DR   ArrayExpress; Q6QI06; -.
DR   Bgee; Q6QI06; -.
DR   CleanEx; MM_4921505C17RIK; -.
DR   Genevestigator; Q6QI06; -.
DR   GO; GO:0031932; C:TORC2 complex; IPI:UniProtKB.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR   GO; GO:0009790; P:embryo development; IMP:UniProtKB.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:MGI.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
DR   GO; GO:0051896; P:regulation of protein kinase B signaling cascade; IDA:UniProtKB.
DR   GO; GO:0032314; P:regulation of Rac GTPase activity; IMP:MGI.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 3.
DR   SUPFAM; SSF48371; ARM-type_fold; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Developmental protein;
KW   Phosphoprotein.
FT   CHAIN         1   1708       Rapamycin-insensitive companion of mTOR.
FT                                /FTId=PRO_0000308180.
FT   MOD_RES      21     21       Phosphoserine.
FT   MOD_RES     582    582       N6-acetyllysine (By similarity).
FT   MOD_RES    1174   1174       Phosphothreonine (By similarity).
FT   MOD_RES    1176   1176       Phosphoserine.
FT   MOD_RES    1281   1281       Phosphoserine (By similarity).
FT   MOD_RES    1283   1283       Phosphoserine (By similarity).
FT   MOD_RES    1294   1294       Phosphothreonine (By similarity).
FT   MOD_RES    1352   1352       Phosphoserine (By similarity).
FT   MOD_RES    1384   1384       Phosphoserine (By similarity).
FT   MOD_RES    1385   1385       Phosphotyrosine (By similarity).
FT   MOD_RES    1387   1387       Phosphoserine (By similarity).
FT   MOD_RES    1395   1395       Phosphoserine (By similarity).
FT   MOD_RES    1410   1410       Phosphoserine (By similarity).
FT   VAR_SEQ       1    152       Missing (in isoform 2).
FT                                /FTId=VSP_052583.
FT   CONFLICT     15     15       I -> V (in Ref. 1; AAR89074).
FT   CONFLICT    185    185       R -> Q (in Ref. 1; AAR89074).
FT   CONFLICT    405    405       L -> I (in Ref. 1; AAR89074).
FT   CONFLICT    698    698       L -> I (in Ref. 1; AAR89074, 3; AAI20904
FT                                and 4; BAC29321).
SQ   SEQUENCE   1708 AA;  191570 MW;  C09CEEEABF1F5A00 CRC64;
     MAAIGRGRSL KNLRIRGRND SGEENVPLDL TREPSDNLRE ILQNVAKLQG VSNMRKLGHL
     NNFTKLLCDI GHSEEKLGFN YEDIIICLRL ALLNEAKEVR AAGLRALRYL IQDSSILQKV
     LKLKVDYLIA RCIDIQQSNE VERTQALRLV RKMITVNASL FPSSVANSLI AVGNDGLQER
     DRMVRACIAI ICELALQNPE VVALRGGLNT ILKNVIDCQL SRINEALITT ILHLLNHPKT
     RQYVRADVEL ERILAPYTDF HYRHSPDTAE GQLKEDREAR FLASKMGIIA TFRSWAGIIN
     LCKPGNSGIQ SLIGVLCIPN MEIRRGLLEV LYDIFRLPLP VVTDEFIEAL LSVDPGRFQD
     SWRLSDGFVA AEAKTILPHR ARSRPDLMDN YLALILSAFI RNGLLEGLVE VITNSDDHIS
     VRATILLGEL LHMANTILPH SHSHHLHCLP TLMNMAASFD IPKEKRLRAS AALNCLNRFH
     EMKKRGPKPY SLHLDHIIQK AIATHHKRDQ YLRVQKDIFV LKDTEEALLI NLRDSQVLQH
     KENLDWDWNL IGTILKWPNV NLRNYKDEQL HRFVRRLLYF YKPSSKLYAS LDLDLAKSKQ
     LTVVGCQFTE FLLESEEDGQ GYLEDLVKDI VQWLNASSGV KPERSLQNNG LLTTLSQHYF
     LFIGTLSCHP HGVKMLEKCS VFQCLLNLCS LKNQDHLLKL TVSSLDYSRD GLARVILSKI
     LTAATDACRL YATKHLRVLL RANVEFFNNW GIELLVTQLH DKNKTISSEA LDILDEACED
     KANLHALIQM KPALSHLGDK GLLLLLRFLS IPKGFSYLNE RGYVAKQLEK WHKEYNSKYV
     DLIEEQLNEA LTTYRKPIDG DNYVRRSNQR LQRPHVYLPV HLYGQLVHHK TGCHLLEVQS
     IITELCHNVR TPDLDKWEDI KKLKASLWAL GNIGSSNWGL NLLQEENVIP DILKLAKQCE
     VLSIRGTCVY VLGLIAKTKQ GCDILKCHSW DSVRHSRKHL WPVVPDDVEQ LCNELSSVPS
     TLSLNSESTS SRHNSESESA PSSMFMLEDD RFGSTSTSTF FLDINEDAEP AFYDRPGPIK
     DKNSFPFFGS SKLVKNRILN SLTLPTKKHR SSSDPKGGKL SSENKTSNRR IRTLTEPSVD
     LNHSEDFTSS SAQKSLQLEP SFVGNKHLED AGSTPSIGEN DLKFPKSFGT ETHRENTSRE
     RLVVEGSASS HIKIRSQSFN TDTTTSGISS MSSSPSRETV AVDPTAMDTD CGSLSTVVST
     KTVKTSHYLT PQSNHLSLSK SNSVSLVPPG SSHTLPRRAQ SLKAPSIATI KSLADCNFSY
     TSSRDAFGYA TLKRLQQQRM HPSLSHSEAL ASPAKDVLFT DTITMKANSF ESRLTPSRFM
     KALSYASLDK EDLLSPINHN TLQRSSSVRS MVSSATYGGS DDYIGLALPV DINDIFQIKD
     VPYFQSKHVP PPDDRGARMF SHDGAGLSSG AGGLVKNSFH LLRQQMSLTE IMNSVHSDAS
     LFLESTEDTG LQEHTDDNCL YCVCIELLGF QPSNQLSSIC SHSDLQDIPY SDWCEQTIHN
     PLEVVPSKFS GISGCSDGAS QEEGSASSTK STELLLGVKT IPDDTPMCRI LLRKEVLRLV
     VNLSSSVSTK CHETGLLTIK EKYPQTFDDI CLYSEVSHLL SHCTFRLQCR RFIQELFQDV
     QFLQMHEEAE AVLAIPPIQP IVDESAES
//
ID   CK2N1_MOUSE             Reviewed;          78 AA.
AC   Q6QWF9;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Calcium/calmodulin-dependent protein kinase II inhibitor 1;
DE   AltName: Full=calcium/calmodulin-dependent protein kinase II inhibitor alpha;
DE            Short=mCaMKIINalpha;
GN   Name=Camk2n1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC   STRAIN=Swiss;
RX   PubMed=17010311; DOI=10.1016/j.bbrc.2006.09.066;
RA   Saha S., Ramanathan A., Rangarajan P.N.;
RT   "Regulation of Ca2+/calmodulin kinase II inhibitor alpha
RT   (CaMKIINalpha) in virus-infected mouse brain.";
RL   Biochem. Biophys. Res. Commun. 350:444-449(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   INDUCTION.
RX   PubMed=16819996; DOI=10.1111/j.1460-9568.2006.04830.x;
RA   Lepicard E.M., Mizuno K., Antunes-Martins A., von Hertzen L.S.,
RA   Giese K.P.;
RT   "An endogenous inhibitor of calcium/calmodulin-dependent kinase II is
RT   up-regulated during consolidation of fear memory.";
RL   Eur. J. Neurosci. 23:3063-3070(2006).
RN   [4]
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=17350603; DOI=10.1016/j.brainres.2007.02.018;
RA   Saha S., Datta K., Rangarajan P.;
RT   "Characterization of mouse neuronal Ca2+/calmodulin kinase II
RT   inhibitor alpha.";
RL   Brain Res. 1148:38-42(2007).
CC   -!- FUNCTION: Potent and specific inhibitor of CaM-kinase II (CAMK2)
CC       (By similarity).
CC   -!- SUBUNIT: Interacts with CAMK2B; the presence of Ca(2+)/calmodulin
CC       increases the interaction but is not essential (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, synaptosome. Cell
CC       junction, synapse, postsynaptic cell membrane, postsynaptic
CC       density.
CC   -!- TISSUE SPECIFICITY: Brain specific (at protein level).
CC   -!- INDUCTION: Up-regulated during consolidation of fear memory. Down-
CC       regulated in brain during Japanese encephalitis virus (JEV) and
CC       rabies virus infection.
CC   -!- SIMILARITY: Belongs to the CAMK2N family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AY523601; AAS02090.1; -; mRNA.
DR   EMBL; AL807249; CAM18882.1; -; Genomic_DNA.
DR   IPI; IPI00350301; -.
DR   RefSeq; NP_079727.1; NM_025451.2.
DR   UniGene; Mm.41603; -.
DR   STRING; Q6QWF9; -.
DR   PhosphoSite; Q6QWF9; -.
DR   PRIDE; Q6QWF9; -.
DR   Ensembl; ENSMUST00000050918; ENSMUSP00000060349; ENSMUSG00000046447.
DR   GeneID; 66259; -.
DR   KEGG; mmu:66259; -.
DR   UCSC; uc008vkz.1; mouse.
DR   CTD; 66259; -.
DR   MGI; MGI:1913509; Camk2n1.
DR   eggNOG; maNOG21169; -.
DR   GeneTree; ENSGT00390000004940; -.
DR   HOGENOM; HBG267584; -.
DR   HOVERGEN; HBG104926; -.
DR   InParanoid; Q6QWF9; -.
DR   OMA; NEEKLGH; -.
DR   OrthoDB; EOG48WC3R; -.
DR   PhylomeDB; Q6QWF9; -.
DR   NextBio; 321121; -.
DR   ArrayExpress; Q6QWF9; -.
DR   Bgee; Q6QWF9; -.
DR   Genevestigator; Q6QWF9; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Membrane; Postsynaptic cell membrane;
KW   Protein kinase inhibitor; Synapse; Synaptosome.
FT   CHAIN         1     78       Calcium/calmodulin-dependent protein
FT                                kinase II inhibitor 1.
FT                                /FTId=PRO_0000338394.
FT   REGION       43     68       Inhibitory domain (By similarity).
SQ   SEQUENCE   78 AA;  8513 MW;  A89A9E5DA11B8E61 CRC64;
     MSEVLPYGDE KLSPYGDGGD VGQIFSCRLQ DTNNFFGAGQ SKRPPKLGQI GRSKRVVIED
     DRIDDVLKTM TDKAPPGV
//
ID   GNAS1_MOUSE             Reviewed;        1133 AA.
AC   Q6R0H7; A2A607; A2A608; Q6R0H4; Q6R0H5; Q6R2J5; Q9JJX0; Q9Z1N8;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Guanine nucleotide-binding protein G(s) subunit alpha isoforms XLas;
DE   AltName: Full=Adenylate cyclase-stimulating G alpha protein;
DE   AltName: Full=Extra large alphas protein;
DE            Short=XLalphas;
GN   Name=Gnas; Synonyms=Gnas1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS XLAS-1; XLAS-2 AND XLAS-3), AND
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 935-1018 (ISOFORM XLAS-1).
RC   STRAIN=129/Sv, BALB/c, C57BL/6J, and FVB/N; TISSUE=Brain;
RX   PubMed=15148396; DOI=10.1073/pnas.0308758101;
RA   Abramowitz J., Grenet D., Birnbaumer M., Torres H.N., Birnbaumer L.;
RT   "XL alpha-s, the extra-long form of the alpha subunit of the Gs G
RT   protein, is significantly longer than suspected, and so is its
RT   companion Alex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:8366-8371(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-785.
RX   MEDLINE=20215313; PubMed=10749992; DOI=10.1093/hmg/9.5.835;
RA   Hayward B.E., Bonthron D.T.;
RT   "An imprinted antisense transcript at the human GNAS1 locus.";
RL   Hum. Mol. Genet. 9:835-841(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 357-1133 (ISOFORM XLAS-4).
RC   STRAIN=C57BL/6;
RX   MEDLINE=20517925; PubMed=10931851; DOI=10.1074/jbc.M006594200;
RA   Klemke M., Pasolli H.A., Kehlenbach R.H., Offermanns S., Schultz G.,
RA   Huttner W.B.;
RT   "Characterization of the extra-large G protein alpha-subunit XLalphas.
RT   II. Signal transduction properties.";
RL   J. Biol. Chem. 275:33633-33640(2000).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12145344; DOI=10.1210/me.2002-0054;
RA   Bastepe M., Gunes Y., Perez-Villamil B., Hunzelman J., Weinstein L.S.,
RA   Jueppner H.;
RT   "Receptor-mediated adenylyl cyclase activation through XLalpha(s), the
RT   extra-large variant of the stimulatory G protein alpha-subunit.";
RL   Mol. Endocrinol. 16:1912-1919(2002).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC       involved as modulators or transducers in various transmembrane
CC       signaling systems. The G(s) protein is involved in hormonal
CC       regulation of adenylate cyclase: it activates the cyclase in
CC       response to beta-adrenergic stimuli. XLas isoforms interact with
CC       the same set of receptors as Gnas isoforms.
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and
CC       gamma. The alpha chain contains the guanine nucleotide binding
CC       site. Interacts through its N-terminal region with ALEX which is
CC       produced from the same locus in a different open reading frame.
CC       This interaction may inhibit its adenylyl cyclase-stimulating
CC       activity (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=9;
CC       Name=XLas-1; Synonyms=XXL;
CC         IsoId=Q6R0H7-1; Sequence=Displayed;
CC       Name=XLas-2; Synonyms=XXLb1;
CC         IsoId=Q6R0H7-2; Sequence=VSP_052176, VSP_052180;
CC       Name=XLas-3; Synonyms=XXLb2;
CC         IsoId=Q6R0H7-3; Sequence=VSP_052177, VSP_052179;
CC       Name=XLas-4;
CC         IsoId=Q6R0H7-4; Sequence=VSP_052178;
CC       Name=Gnas-1;
CC         IsoId=P63094-1; Sequence=External;
CC       Name=Gnas-2;
CC         IsoId=P63094-2; Sequence=External;
CC       Name=Gnas-3; Synonyms=NTas;
CC         IsoId=P63094-3; Sequence=External;
CC       Name=Nesp55-1;
CC         IsoId=Q9Z0F1-1; Sequence=External;
CC         Note=Shares no sequence similarity with other isoforms (except
CC         isoform Nesp55-2) due to a novel first exon containing the
CC         entire reading frame spliced to shared exon 2 so that exons 2-13
CC         make up the 3'-UTR;
CC       Name=Nesp55-2;
CC         IsoId=Q9Z0F1-2; Sequence=External;
CC         Note=Shares no sequence similarity with other isoforms (except
CC         isoform Nesp55-1) due to a novel first exon containing the
CC         entire reading frame spliced to shared exon 2 so that exons 2-13
CC         make up the 3'-UTR;
CC   -!- DISRUPTION PHENOTYPE: Mice cells lacking XLas isoforms which are
CC       then transfected with these isoforms and a range of receptors
CC       demonstrate that the XLas isoforms are capable of functionally
CC       coupling to the same receptors as the Gnas isoforms including
CC       Adrb2, Crfr1, Pthr1 and Tshr.
CC   -!- MISCELLANEOUS: This protein is produced by a bicistronic gene
CC       which also produces the ALEX protein from an overlapping reading
CC       frame (By similarity).
CC   -!- MISCELLANEOUS: The GNAS locus is imprinted in a complex manner,
CC       giving rise to distinct paternally, maternally and biallelically
CC       expressed proteins. The XLas isoforms are paternally derived, the
CC       Gnas isoforms are biallelically derived and the Nesp55 isoforms
CC       are maternally derived.
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(s) subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD14686.1; Type=Erroneous initiation;
CC       Sequence=CAB83219.1; Type=Erroneous initiation;
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DR   EMBL; AY518305; AAR99380.1; -; Genomic_DNA.
DR   EMBL; AY518306; AAR99381.1; -; Genomic_DNA.
DR   EMBL; AY518307; AAR99382.1; -; Genomic_DNA.
DR   EMBL; AY518308; AAR99383.1; -; Genomic_DNA.
DR   EMBL; AY519501; AAS00601.1; -; mRNA.
DR   EMBL; AY519503; AAS00603.1; -; mRNA.
DR   EMBL; AY519504; AAS00604.1; -; mRNA.
DR   EMBL; AL593857; CAM24406.1; -; Genomic_DNA.
DR   EMBL; AL593857; CAM24407.1; -; Genomic_DNA.
DR   EMBL; AJ251761; CAB83219.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AF116268; AAD14686.1; ALT_INIT; mRNA.
DR   IPI; IPI00416906; -.
DR   IPI; IPI00469793; -.
DR   IPI; IPI00622913; -.
DR   IPI; IPI00798513; -.
DR   RefSeq; NP_001070975.1; NM_001077507.1.
DR   RefSeq; NP_034439.2; NM_010309.3.
DR   RefSeq; NP_963911.1; NM_201617.1.
DR   UniGene; Mm.125770; -.
DR   HSSP; P04896; 1AZT.
DR   ProteinModelPortal; Q6R0H7; -.
DR   SMR; Q6R0H7; 776-1130.
DR   STRING; Q6R0H7; -.
DR   PRIDE; Q6R0H7; -.
DR   Ensembl; ENSMUST00000080493; ENSMUSP00000079341; ENSMUSG00000027523.
DR   Ensembl; ENSMUST00000087876; ENSMUSP00000085184; ENSMUSG00000027523.
DR   Ensembl; ENSMUST00000087877; ENSMUSP00000085185; ENSMUSG00000027523.
DR   GeneID; 14683; -.
DR   KEGG; mmu:14683; -.
DR   UCSC; uc008oet.1; mouse.
DR   UCSC; uc008oev.1; mouse.
DR   CTD; 14683; -.
DR   MGI; MGI:95777; Gnas.
DR   HOGENOM; HBG281845; -.
DR   HOVERGEN; HBG079975; -.
DR   InParanoid; Q6R0H7; -.
DR   OrthoDB; EOG490792; -.
DR   PhylomeDB; Q6R0H7; -.
DR   NextBio; 286600; -.
DR   ArrayExpress; Q6R0H7; -.
DR   Bgee; Q6R0H7; -.
DR   Genevestigator; Q6R0H7; -.
DR   GermOnline; ENSMUSG00000027523; Mus musculus.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; TAS:MGI.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; TAS:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0007191; P:activation of adenylate cyclase activity by dopamine receptor signaling pathway; IGI:MGI.
DR   GO; GO:0007610; P:behavior; IMP:MGI.
DR   GO; GO:0051216; P:cartilage development; IMP:MGI.
DR   GO; GO:0006306; P:DNA methylation; IMP:MGI.
DR   GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:MGI.
DR   GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
DR   GO; GO:0001958; P:endochondral ossification; IMP:MGI.
DR   GO; GO:0006112; P:energy reserve metabolic process; IMP:MGI.
DR   GO; GO:0071514; P:genetic imprinting; IMP:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR   GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:MGI.
DR   GO; GO:0045672; P:positive regulation of osteoclast differentiation; IMP:MGI.
DR   GO; GO:0040032; P:post-embryonic body morphogenesis; IMP:MGI.
DR   GO; GO:0042493; P:response to drug; IMP:MGI.
DR   GO; GO:0043588; P:skin development; IMP:MGI.
DR   GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
DR   InterPro; IPR000367; Gprotein_alpha_S.
DR   InterPro; IPR001019; Gprotein_alpha_su.
DR   InterPro; IPR011025; GproteinA_insert.
DR   Gene3D; G3DSA:1.10.400.10; GproteinA_insert; 1.
DR   PANTHER; PTHR10218; Gprotein_alph_bd; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00443; GPROTEINAS.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF47895; Transducn_insert; 1.
PE   2: Evidence at transcript level;
KW   ADP-ribosylation; Alternative splicing; Cell membrane; Coiled coil;
KW   GTP-binding; Membrane; Nucleotide-binding; Phosphoprotein; Transducer.
FT   CHAIN         1   1133       Guanine nucleotide-binding protein G(s)
FT                                subunit alpha isoforms XLas.
FT                                /FTId=PRO_0000253985.
FT   NP_BIND     786    793       GTP (By similarity).
FT   NP_BIND     962    966       GTP (By similarity).
FT   NP_BIND    1031   1034       GTP (By similarity).
FT   COILED      737    761       Potential.
FT   COMPBIAS     19    303       Pro-rich.
FT   COMPBIAS    450    619       Ala-rich.
FT   MOD_RES     790    790       Phosphoserine (By similarity).
FT   MOD_RES     940    940       ADP-ribosylarginine; by cholera toxin (By
FT                                similarity).
FT   VAR_SEQ     787    876       AGESGKSTIVKQMRILHVNGFNGEGGEEDPQAARSNSDGEK
FT                                ATKVQDIKNNLKEAIETIVAAMSNLVPPVELANPENQFRVD
FT                                YILSVMNV -> RKVVPSDTEGRYRPEASASASDRRLDRRG
FT                                REVSPELLGWALRGSPGSIVRDRGGLGPSGCAPPPRLARLL
FT                                RLRQLVVGVCWCPFSVFACA (in isoform XLas-2).
FT                                /FTId=VSP_052176.
FT   VAR_SEQ     787    827       AGESGKSTIVKQMRILHVNGFNGEGGEEDPQAARSNSDGEK
FT                                -> RKVVPSDTEGRYRPEASASASDRRLDRRGREVLESLAK
FT                                APL (in isoform XLas-3).
FT                                /FTId=VSP_052177.
FT   VAR_SEQ     810    825       EGGEEDPQAARSNSDG -> DS (in isoform XLas-
FT                                4).
FT                                /FTId=VSP_052178.
FT   VAR_SEQ     828   1133       Missing (in isoform XLas-3).
FT                                /FTId=VSP_052179.
FT   VAR_SEQ     877   1133       Missing (in isoform XLas-2).
FT                                /FTId=VSP_052180.
FT   CONFLICT    371    371       A -> G (in Ref. 4; CAB83219).
FT   CONFLICT    381    381       P -> S (in Ref. 4; CAB83219).
FT   CONFLICT    578    591       SLSATPAARASLPA -> YSRYSQLLPPLGHPFLPR (in
FT                                Ref. 3).
FT   CONFLICT    595    596       Missing (in Ref. 3).
FT   CONFLICT    599    599       A -> Q (in Ref. 3).
FT   CONFLICT    613    617       SAAPS -> LPPH (in Ref. 3).
FT   CONFLICT    622    628       RPPSPEI -> DPQPRD (in Ref. 3).
SQ   SEQUENCE   1133 AA;  121505 MW;  C1497D45498172F7 CRC64;
     MGMFNCLHGN NMSGQHDIPP EVGEQPEQEP LEAPGAAAPG AGAGPAEEMA TEPDSEPSNN
     EPVPDETGSE ISGPPEDSKS DIQSPCQAFE EVRVGGDYSP PPEEAMPFET QQPSLGDFWP
     TLEQPGPSGT PSGLQAFNPA ILEPGTPTGA SPGLGAYTPP PEEAMPFEFN EPAQGDHSQP
     PLQVPDLAPG GPEALVPRAL PAEPGNIRFE NAGFREDYSP PPEESVPFQV GGEEFGGDSP
     PPGLPRVIPQ IGIGGEFPTV AVPSALCLAP AENAPPLWVR GAIDRPFREA VRSPPNFACD
     SPPMEITRPL LEIGRASIGV DDDTAVNMDS PPIASDGPPI EVSGAPDKSE CAERPPVERE
     AAEMEGSPTT ATAVEGKVPS PERGDGSSTQ PEAMDAKPAP AAQAVSTGSD AGAPTDSAML
     TDSQSDAGED GTAPGTPSDL QSDPEELEEA PAVRADPDGG AAPVAPATPA ESESEGSRDP
     AAEPASEAVP ATTAESASGA APVTQVEPAA AAVSATLAEP AARAAPITPK EPTTRAVPSA
     RAHPAAGAVP GAPAMSASAR AAAARAAYAG PLVWGARSLS ATPAARASLP ARAAAAARAA
     SAARAVAAGR SASAAPSRAH LRPPSPEIQV ADPPTPRPPP RPTAWPDKYE RGRSCCRYEA
     SSGICEIESS SDESEEGATG CFQWLLRRNR RPGLPRSHTV GSNPVRNFFT RAFGSCFGLS
     ECTRSRSLSP GKAKDPMEER RKQMRKEAIE MREQKRADKK RSKLIDKQLE EEKMDYMCTH
     RLLLLGAGES GKSTIVKQMR ILHVNGFNGE GGEEDPQAAR SNSDGEKATK VQDIKNNLKE
     AIETIVAAMS NLVPPVELAN PENQFRVDYI LSVMNVPNFD FPPEFYEHAK ALWEDEGVRA
     CYERSNEYQL IDCAQYFLDK IDVIKQADYV PSDQDLLRCR VLTSGIFETK FQVDKVNFHM
     FDVGGQRDER RKWIQCFNDV TAIIFVVASS SYNMVIREDN QTNRLQEALN LFKSIWNNRW
     LRTISVILFL NKQDLLAEKV LAGKSKIEDY FPEFARYTTP EDATPEPGED PRVTRAKYFI
     RDEFLRISTA SGDGRHYCYP HFTCAVDTEN IRRVFNDCRD IIQRMHLRQY ELL
//
ID   NEB2_MOUSE              Reviewed;         817 AA.
AC   Q6R891; Q8K0X7;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Neurabin-2;
DE   AltName: Full=Neurabin-II;
DE   AltName: Full=Protein phosphatase 1 regulatory subunit 9B;
DE   AltName: Full=Spinophilin;
GN   Name=Ppp1r9b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6;
RA   Allen P.B.;
RT   "Mouse spinophilin cDNA.";
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION BY PKA, PHOSPHORYLATION AT SER-94, AND
RP   DEPHOSPHORYLATION BY PP1 AND PP2A.
RX   PubMed=16300646; DOI=10.1111/j.1471-4159.2005.03491.x;
RA   Uematsu K., Futter M., Hsieh-Wilson L.C., Higashi H., Maeda H.,
RA   Nairn A.C., Greengard P., Nishi A.;
RT   "Regulation of spinophilin Ser94 phosphorylation in neostriatal
RT   neurons involves both DARPP-32-dependent and independent pathways.";
RL   J. Neurochem. 95:1642-1652(2005).
RN   [5]
RP   PHOSPHORYLATION BY MAPK1 AND CDK5, PHOSPHORYLATION AT SER-15; SER-17
RP   AND SER-205, AND MUTAGENESIS OF SER-15.
RX   PubMed=15728359; DOI=10.1073/pnas.0409802102;
RA   Futter M., Uematsu K., Bullock S.A., Kim Y., Hemmings H.C. Jr.,
RA   Nishi A., Greengard P., Nairn A.C.;
RT   "Phosphorylation of spinophilin by ERK and cyclin-dependent PK 5
RT   (Cdk5).";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3489-3494(2005).
CC   -!- FUNCTION: Seems to act as a scaffold protein in multiple signaling
CC       pathways. Modulates excitatory synaptic transmission and dendritic
CC       spine morphology. Binds to actin filaments (F-actin) and shows
CC       cross-linking activity. Binds along the sides of the F-actin. May
CC       play an important role in linking the actin cytoskeleton to the
CC       plasma membrane at the synaptic junction. Believed to target
CC       protein phosphatase 1/PP1 to dendritic spines, which are rich in
CC       F-actin, and regulates its specificity toward ion channels and
CC       other substrates, such as AMPA-type and NMDA-type glutamate
CC       receptors. Plays a role in regulation of G-protein coupled
CC       receptor signaling, including dopamine D2 receptors and alpha-
CC       adrenergic receptors. May establish a signaling complex for
CC       dopaminergic neurotransmission through D2 receptors by linking
CC       receptors downstream signaling molecules and the actin
CC       cytoskeleton. Binds to ADRA1B and RGS2 and mediates regulation of
CC       ADRA1B signaling. May confer to Rac signaling specificity by
CC       binding to both, RacGEFs and Rac effector proteins. Probably
CC       regulates p70 S6 kinase activity by forming a complex with TIAM1
CC       (By similarity).
CC   -!- SUBUNIT: Possibly exists as an homodimer, homotrimer or an
CC       homotetramer. Interacts with F-actin, PPP1CA, neurabin-1, TGN38
CC       and D(2) dopamine receptor. Interacts with RGS1, RGS2, RGS4, RGS19
CC       and ADRA1B, ADRA2A, ADRA2B, ADRA2C, CDKN2A, PPP1R2, RASGFR1 and
CC       TIAM1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Nucleus (By similarity). Cell projection, dendritic spine (By
CC       similarity). Cell junction, synapse. Note=Enriched at synapse and
CC       cadherin-based cell-cell adhesion sites. In neurons, both
CC       cytosolic and membrane-associated, and highly enriched in the
CC       post-synaptic density apposed to exitatory synapses. Colocalizes
CC       with PPP1R2 at actin-rich adherens junctions in epithelial cells
CC       and in dendritic spines (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6R891-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6R891-2; Sequence=VSP_017674, VSP_017675;
CC   -!- PTM: Stimulation of D1 (but not D2) dopamine receptors induces
CC       Ser-94 phosphorylation. Dephosphorylation of Ser-94 is mediated
CC       mainly by PP1 and to a lesser extent by PP2A. Phosphorylation of
CC       spinophilin disrupts its association with F-actin, but does not
CC       affect its binding to PP1 (By similarity).
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
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DR   EMBL; AY508450; AAR91608.1; -; mRNA.
DR   EMBL; AL606480; CAI23964.1; -; Genomic_DNA.
DR   EMBL; AL606480; CAI23965.1; -; Genomic_DNA.
DR   EMBL; BC029672; AAH29672.1; -; mRNA.
DR   IPI; IPI00420651; -.
DR   IPI; IPI00649394; -.
DR   RefSeq; NP_758465.2; NM_172261.3.
DR   UniGene; Mm.476821; -.
DR   ProteinModelPortal; Q6R891; -.
DR   SMR; Q6R891; 424-583.
DR   MINT; MINT-275541; -.
DR   STRING; Q6R891; -.
DR   PhosphoSite; Q6R891; -.
DR   PRIDE; Q6R891; -.
DR   Ensembl; ENSMUST00000038696; ENSMUSP00000041732; ENSMUSG00000038976.
DR   GeneID; 217124; -.
DR   KEGG; mmu:217124; -.
DR   UCSC; uc007kzr.1; mouse.
DR   UCSC; uc007kzs.1; mouse.
DR   CTD; 217124; -.
DR   MGI; MGI:2387581; Ppp1r9b.
DR   eggNOG; roNOG13918; -.
DR   HOGENOM; HBG715038; -.
DR   HOVERGEN; HBG005213; -.
DR   InParanoid; Q6R891; -.
DR   OMA; LQMGTTA; -.
DR   OrthoDB; EOG4S4PFV; -.
DR   PhylomeDB; Q6R891; -.
DR   NextBio; 375573; -.
DR   ArrayExpress; Q6R891; -.
DR   Bgee; Q6R891; -.
DR   CleanEx; MM_PPP1R9B; -.
DR   Genevestigator; Q6R891; -.
DR   GermOnline; ENSMUSG00000038976; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; IDA:MGI.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0030175; C:filopodium; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; TAS:MGI.
DR   GO; GO:0007015; P:actin filament organization; IPI:MGI.
DR   GO; GO:0016358; P:dendrite development; IMP:MGI.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IMP:MGI.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Cell junction; Cell projection;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW   Differentiation; Neurogenesis; Nucleus; Phosphoprotein; Synapse.
FT   CHAIN         1    817       Neurabin-2.
FT                                /FTId=PRO_0000228615.
FT   DOMAIN      496    584       PDZ.
FT   REGION        1    154       Actin-binding (By similarity).
FT   REGION      100    371       Interacts with D(2) dopamine receptor (By
FT                                similarity).
FT   REGION      164    282       Actin-binding (By similarity).
FT   REGION      169    255       Interacts with ADRA2A, ADRA2B and ADRA2C
FT                                (By similarity).
FT   REGION      417    494       Interacts with protein phosphatase 1 (By
FT                                similarity).
FT   REGION      480    525       Interacts with RGS2 (By similarity).
FT   REGION      595    816       Interacts with TGN38 (By similarity).
FT   COILED      595    616       Potential.
FT   COILED      665    816       Potential.
FT   MOTIF       575    578       PP1-binding motif.
FT   COMPBIAS    253    260       Poly-Pro.
FT   MOD_RES      15     15       Phosphoserine; by MAPK1.
FT   MOD_RES      17     17       Phosphoserine; by CDK5.
FT   MOD_RES      94     94       Phosphoserine; by PKA.
FT   MOD_RES     100    100       Phosphoserine (By similarity).
FT   MOD_RES     116    116       Phosphoserine (By similarity).
FT   MOD_RES     205    205       Phosphoserine; by MAPK1.
FT   MOD_RES     207    207       Phosphothreonine (By similarity).
FT   MOD_RES     339    339       Phosphoserine (By similarity).
FT   VAR_SEQ       1    424       Missing (in isoform 2).
FT                                /FTId=VSP_017674.
FT   VAR_SEQ     425    456       YEPESGCVEIPGLSEEEDPAPSRKIHFSTAPI -> MDTGL
FT                                HATQLAQGPSPANVLLPSYGPLRTAPP (in isoform
FT                                2).
FT                                /FTId=VSP_017675.
FT   MUTAGEN      15     15       S->E: Increases filopodial density.
SQ   SEQUENCE   817 AA;  89520 MW;  1654037C196F2F6B CRC64;
     MMKTEPRGPG GPLRSASPHR SAYEAGIQAL KPPDAPGPDE APKAAHHKKY GSNVHRIKSM
     FLQMGTTAGP PGEAGGGAGM AEAPRASDRG VRLSLPRASS LNENVDHSAL LKLGTSVSER
     VSRFDSKPAP SAQPAPPPHP PSRLQETRKL FERSVPAASG GDKEAVARRL LRQERAGLQD
     RKLDVVVRFN GSTEALDKLD ADAVSPTVSQ LSAVFEKADS RTGLHRAPGP PRAAGAPQVN
     SKLVTKRSRV FQPPPPPPAP SGDGATEKER GPGGQQPPQH RVAPARPPPK PREVRKIKPV
     EVEESGESEA ESAPGEVIQA EVTVHAALEN GSTPATTASP APEEPKAEAV PEEEAAASVA
     TLERGVDNGR APDMAPEEVD ESKKEDFSEA DLVDVSAYSG LGEDSGGSAL EEDDEEDEED
     GEPPYEPESG CVEIPGLSEE EDPAPSRKIH FSTAPIQVFS TYSNEDYDRR NEDVDPMAAS
     AEYELEKRVE RLELFPVELE KDSEGLGISI IGMGAGADMG LEKLGIFVKT VTEGGAAHRD
     GRIQVNDLLV EVDGTSLVGV TQSFAASVLR NTKGRVRFMI GRERPGEQSE VAQLIQQTLE
     QERWQREMME QRYAQYGEDD EETGEYATDE DEELSPTFPG GEMAIEVFEL AENEDALSPV
     EMEPEKLVHK FKELQIKHAV TEAEIQQLKR KLQSLEQEKG RWRVEKAQLE QSVEENKERM
     EKLEGYWGEA QSLCQAVDEH LRETQAQYQA LERKYSKAKR LIKDYQQKEI EFLKKETAQR
     RVLEESELAR KEEMDKLLDK ISELEGNLQT LRNSNST
//
ID   MAGI1_MOUSE             Reviewed;        1471 AA.
AC   Q6RHR9; O54893; O54894; O54895;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1;
DE   AltName: Full=BAI1-associated protein 1;
DE            Short=BAP-1;
DE   AltName: Full=Membrane-associated guanylate kinase inverted 1;
DE            Short=MAGI-1;
GN   Name=Magi1; Synonyms=Baiap1, Bap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH ESAM.
RC   STRAIN=129/SvHe; TISSUE=Brain endothelium;
RX   PubMed=15383320; DOI=10.1016/j.yexcr.2004.07.010;
RA   Wegmann F., Ebnet K., Du Pasquier L., Vestweber D., Butz S.;
RT   "Endothelial adhesion molecule ESAM binds directly to the multidomain
RT   adaptor MAGI-1 and recruits it to cell contacts.";
RL   Exp. Cell Res. 300:121-133(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6 X CBA;
RX   PubMed=9395497; DOI=10.1074/jbc.272.50.31589;
RA   Dobrosotskaya I.Y., Guy R.K., James G.L.;
RT   "MAGI-1, a membrane-associated guanylate kinase with a unique
RT   arrangement of protein-protein interaction domains.";
RL   J. Biol. Chem. 272:31589-31597(1997).
RN   [3]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH CTNNB1.
RX   PubMed=10772923; DOI=10.1006/bbrc.2000.2471;
RA   Dobrosotskaya I.Y., James G.L.;
RT   "MAGI-1 interacts with beta-catenin and is associated with cell-cell
RT   adhesion structures.";
RL   Biochem. Biophys. Res. Commun. 270:903-909(2000).
RN   [4]
RP   INTERACTION WITH NET1.
RX   PubMed=11350080; DOI=10.1006/bbrc.2001.4880;
RA   Dobrosotskaya I.Y.;
RT   "Identification of mNET1 as a candidate ligand for the first PDZ
RT   domain of MAGI-1.";
RL   Biochem. Biophys. Res. Commun. 283:969-975(2001).
RN   [5]
RP   INTERACTION WITH LRP2, TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
RX   PubMed=11274227;
RA   Patrie K.M., Drescher A.J., Goyal M., Wiggins R.C., Margolis B.;
RT   "The membrane-associated guanylate kinase protein MAGI-1 binds megalin
RT   and is present in glomerular podocytes.";
RL   J. Am. Soc. Nephrol. 12:667-677(2001).
RN   [6]
RP   INTERACTION WITH ACCN3, AND FUNCTION.
RX   PubMed=15317815; DOI=10.1074/jbc.M405874200;
RA   Hruska-Hageman A.M., Benson C.J., Leonard A.S., Price M.P.,
RA   Welsh M.J.;
RT   "PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have
RT   opposite effects on H+- gated current.";
RL   J. Biol. Chem. 279:46962-46968(2004).
RN   [7]
RP   INTERACTION WITH CXADR.
RX   PubMed=15304526; DOI=10.1242/jcs.01300;
RA   Ashbourne-Excoffon K.J.D., Hruska-Hageman A.M., Klotz M., Traver G.L.,
RA   Zabner J.;
RT   "A role for the PDZ-binding domain of the coxsackie B virus and
RT   adenovirus receptor (CAR) in cell adhesion and growth.";
RL   J. Cell Sci. 117:4401-4409(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-858, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: May play a role as scaffolding protein at cell-cell
CC       junctions. May regulate acid-induced ACCN3 currents by modulating
CC       its expression at the cell surface.
CC   -!- SUBUNIT: Interacts through its WW 2 domain with SYNPO and through
CC       its PDZ 5 domain with ACTN4. Interacts with cytoplasmic domain of
CC       BAI1. Interacts with AMOT and via its WW domains with DRPLA (By
CC       similarity). Interacts with ESAM, LRP2 and CXADR. Isoform 2
CC       interacts with CTNNB1. Interacts through its PDZ 1 domain with
CC       NET1. Interacts with ACCN3. Interacts with FCHSD2 (By similarity).
CC       Interacts with IGSF5/JAM4 and through its PDZ 2 and 3 domains with
CC       NPHS1 forming a tripartite complex (By similarity). Interacts with
CC       DDN (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm (Probable). Cell
CC       membrane; Peripheral membrane protein (Probable). Cell junction,
CC       tight junction (By similarity). Note=Localizes to epithelial cells
CC       tight junctions (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm (Probable). Cell
CC       membrane; Peripheral membrane protein (Probable).
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Nucleus (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1; Synonyms=MAGI1c alpha beta2 gamma, MAGI-1c;
CC         IsoId=Q6RHR9-1; Sequence=Displayed;
CC       Name=2; Synonyms=MAGI-1b;
CC         IsoId=Q6RHR9-2; Sequence=VSP_011673, VSP_011674, VSP_011675,
CC                                  VSP_011676, VSP_011677;
CC       Name=3; Synonyms=MAGI-1a;
CC         IsoId=Q6RHR9-3; Sequence=VSP_011678, VSP_011679, VSP_011677;
CC   -!- TISSUE SPECIFICITY: Widely expressed, including kidney glomeruli.
CC   -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC   -!- SIMILARITY: Contains 6 PDZ (DHR) domains.
CC   -!- SIMILARITY: Contains 2 WW domains.
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DR   EMBL; AY497557; AAS77818.1; -; mRNA.
DR   EMBL; AF027503; AAB91995.1; -; mRNA.
DR   EMBL; AF027504; AAB91996.1; -; mRNA.
DR   EMBL; AF027505; AAB91997.1; -; mRNA.
DR   IPI; IPI00454120; -.
DR   IPI; IPI00471107; -.
DR   IPI; IPI00471108; -.
DR   PIR; T42372; T42372.
DR   RefSeq; NP_001025021.1; NM_001029850.3.
DR   RefSeq; NP_034497.1; NM_010367.2.
DR   UniGene; Mm.217216; -.
DR   PDB; 2I04; X-ray; 2.15 A; A/B=463-546.
DR   PDBsum; 2I04; -.
DR   ProteinModelPortal; Q6RHR9; -.
DR   SMR; Q6RHR9; 2-107, 137-192, 293-401, 463-546, 632-713, 831-915, 986-1217.
DR   MINT; MINT-150460; -.
DR   STRING; Q6RHR9; -.
DR   PhosphoSite; Q6RHR9; -.
DR   PRIDE; Q6RHR9; -.
DR   Ensembl; ENSMUST00000055224; ENSMUSP00000062085; ENSMUSG00000045095.
DR   Ensembl; ENSMUST00000089317; ENSMUSP00000086730; ENSMUSG00000045095.
DR   GeneID; 14924; -.
DR   KEGG; mmu:14924; -.
DR   UCSC; uc009czi.1; mouse.
DR   UCSC; uc009czk.1; mouse.
DR   UCSC; uc009czl.1; mouse.
DR   CTD; 14924; -.
DR   MGI; MGI:1203522; Magi1.
DR   GeneTree; ENSGT00530000063259; -.
DR   HOGENOM; HBG315069; -.
DR   HOVERGEN; HBG007091; -.
DR   InParanoid; Q6RHR9; -.
DR   OMA; ETRNTTK; -.
DR   OrthoDB; EOG4CZBF2; -.
DR   PhylomeDB; Q6RHR9; -.
DR   NextBio; 287235; -.
DR   ArrayExpress; Q6RHR9; -.
DR   Bgee; Q6RHR9; -.
DR   CleanEx; MM_BAP1; -.
DR   Genevestigator; Q6RHR9; -.
DR   GermOnline; ENSMUSG00000045095; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF00595; PDZ; 5.
DR   Pfam; PF00397; WW; 2.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 6.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF50156; PDZ; 6.
DR   SUPFAM; SSF51045; WW_Rsp5_WWP; 2.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 6.
DR   PROSITE; PS01159; WW_DOMAIN_1; 2.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Cell junction;
KW   Cell membrane; Cytoplasm; Membrane; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Repeat; Tight junction.
FT   CHAIN         1   1471       Membrane-associated guanylate kinase, WW
FT                                and PDZ domain-containing protein 1.
FT                                /FTId=PRO_0000094590.
FT   DOMAIN       17    105       PDZ 1.
FT   DOMAIN       96    287       Guanylate kinase-like.
FT   DOMAIN      300    333       WW 1.
FT   DOMAIN      359    392       WW 2.
FT   DOMAIN      464    546       PDZ 2.
FT   DOMAIN      635    713       PDZ 3.
FT   DOMAIN      833    915       PDZ 4.
FT   DOMAIN      990   1074       PDZ 5.
FT   DOMAIN     1132   1214       PDZ 6.
FT   NP_BIND     103    110       ATP (By similarity).
FT   REGION      990   1074       Interaction with FCHSD2 (By similarity).
FT   COMPBIAS    237    242       Poly-Glu.
FT   COMPBIAS    402    410       Poly-Gln.
FT   COMPBIAS    970    980       Poly-Gly.
FT   COMPBIAS   1378   1381       Poly-Arg.
FT   MOD_RES     376    376       Phosphotyrosine (By similarity).
FT   MOD_RES     858    858       Phosphotyrosine.
FT   MOD_RES    1470   1470       Phosphoserine (By similarity).
FT   VAR_SEQ     348    359       Missing (in isoform 2).
FT                                /FTId=VSP_011673.
FT   VAR_SEQ     798    826       PMSPSPASGLSKGERDREINSTNFGECQI -> L (in
FT                                isoform 2).
FT                                /FTId=VSP_011674.
FT   VAR_SEQ    1019   1074       Missing (in isoform 2).
FT                                /FTId=VSP_011675.
FT   VAR_SEQ    1221   1268       DPSSDRNGPSTGAQGVPEVRPGPPDHRPHPALESSYPPELH
FT                                KSSQHAE -> AMIPPKIAACMRNEKLGEACFYLMGHNQTT
FT                                TPAATGTAPPPVHKVFRK (in isoform 2).
FT                                /FTId=VSP_011676.
FT   VAR_SEQ    1221   1236       DPSSDRNGPSTGAQGV -> GGSNYENIPSFPGMTP (in
FT                                isoform 3).
FT                                /FTId=VSP_011678.
FT   VAR_SEQ    1238   1268       Missing (in isoform 3).
FT                                /FTId=VSP_011679.
FT   VAR_SEQ    1269   1471       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_011677.
FT   CONFLICT    726    726       Missing (in Ref. 2; AAB91995).
FT   CONFLICT   1342   1342       A -> D (in Ref. 2; AAB91997).
FT   STRAND      463    468
FT   STRAND      473    480
FT   STRAND      488    493
FT   HELIX       498    502
FT   STRAND      510    514
FT   HELIX       524    532
FT   STRAND      539    545
SQ   SEQUENCE   1471 AA;  161974 MW;  6C780C71CAC37CB1 CRC64;
     MSKVIQKKNH WTGRVHECTV KRGPQGELGV TVLGGAEHGE FPYVGAVAAA EAAGLPGGGE
     GPKLAEGELL LEVQGVRVSG LPRYDVLGVI DSCKEAVTFK AVRQGGRLNK DLRHFLNQRF
     QKGSPDHELQ QTIRDNLYRH AVPCTTRSPR EGEVPGVDYS FLTVKEFLDL EQSGTLLEVG
     TYEGNYYGTP KPPSQPVSGK VITTDALHSL QSGSKQSTPK RTKSYNDMQN AGIVHPENEE
     EEDVPEMNSS FTADSGDQDE HTLQEATLPP VNSSILAAPI TDPSQKFPQY LPLSAEDNLG
     PLPENWEMAY TENGEVYFID HNTKTTSWLD PRCLNKQQKP LEECEDDEGV HTEELDSELE
     LPAGWEKIED PVYGVYYVDH INRKTQYENP VLEAKRKKQL EQQQQQQQPQ PPQPEEWTED
     HASVVPPVAP SHPPSNPEPA RETPLQGKPF FTRNPSELKG KFIHTKLRKS SRGFGFTVVG
     GDEPDEFLQI KSLVLDGPAA LDGKMETGDV IVSVNDTCVL GHTHAQVVKI FQSIPIGASV
     DLELCRGYPL PFDPDDPNTS LVTSVAILDK EPIIVNGQET YDSPASHSSK TGKVSSMKDA
     RPSSPADVAS NSSHGYPNDT VSLASSIATQ PELITVHIVK GPMGFGFTIA DSPGGGGQRV
     KQIVDSPRCR GLKEGDLIVE VNKKNVQALT HNQVVDMLIE CPKGSEVTLL VQRGGLPVPK
     KSPKSQPLER KDSQNSSQHS VSSHRSLHTA SPSHGIQVLP EYLPADAPAP DQTDSSGQKK
     PDPFKIWAQS RSMYENRPMS PSPASGLSKG ERDREINSTN FGECQIPDYQ EQDIFLWRKE
     TGFGFRILGG NEPGEPIYIG HIVPLGAADT DGRLRSGDEL ICVDGTPVIG KSHQLVVQLM
     QQAAKQGHVN LTVRRKVVFA VPKAENEVPS PASSHHSSNQ PASLTEEKRT PQGSQNSLNT
     VSSGSGSTSG IGSGGGGGSG VVSAVLQPYD VEIRRGENEG FGFVIVSSVS RPEAGTTFGR
     IIEGSPADRC GKLKVGDRIL AVNGCSITNK SHSDIVNLIK EAGNTVTLRI IPGDESSNAT
     LLTNAEKIAT ITTTHAPSQQ GTQETRTTTK PKQDSQFEFK GPQAAQEQDF YTVELERGAK
     GFGFSLRGGR EYNMDLYVLR LAEDGPAERC GKMRIGDEIL EINGETTKNM KHSRAIELIK
     NGGRRVRLFL RRGDGSVPEY DPSSDRNGPS TGAQGVPEVR PGPPDHRPHP ALESSYPPEL
     HKSSQHAEKR AHAKDPKGNR EHSKQPNEHH TWNGTSRKQD SGACRPKDRP PDAWREAQPE
     RTATNGSKRR SPEKRREGTR SADNTLERRE KHEKRREISP ERKRERSPTR RKDSSPSRRR
     RSLERLLDQR RSPERRRGGS PERRAKSTDR RRARSPERRR ERSLDKRNRD DKVGHREREE
     AGLKLEAGRS PRNPPEQRRR PYKECSTDLS I
//
ID   Q6TA13_MOUSE            Unreviewed;      1698 AA.
AC   Q6TA13;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   SubName: Full=Kinesin-related microtuble-based motor protein;
GN   Name=Kif1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ICR;
RX   PubMed=15885113; DOI=10.1111/j.1399-3011.2005.00255.x;
RA   Rashid D.J., Bononi J., Tripet B.P., Hodges R.S., Pierce D.W.;
RT   "Monomeric and dimeric states exhibited by the kinesin-related motor
RT   protein KIF1A.";
RL   J. Pept. Res. 65:538-549(2005).
CC   -!- SIMILARITY: Belongs to the kinesin-like protein family.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 kinesin-motor domain.
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DR   EMBL; AY426748; AAR04821.1; -; mRNA.
DR   IPI; IPI00626501; -.
DR   UniGene; Mm.276408; -.
DR   ProteinModelPortal; Q6TA13; -.
DR   SMR; Q6TA13; 4-353, 500-616.
DR   STRING; Q6TA13; -.
DR   Ensembl; ENSMUST00000086819; ENSMUSP00000084029; ENSMUSG00000014602.
DR   UCSC; uc007cde.1; mouse.
DR   MGI; MGI:108391; Kif1a.
DR   GeneTree; ENSGT00570000078823; -.
DR   HOVERGEN; HBG052251; -.
DR   InParanoid; Q6TA13; -.
DR   ArrayExpress; Q6TA13; -.
DR   Bgee; Q6TA13; -.
DR   Genevestigator; Q6TA13; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR022140; KIF1B.
DR   InterPro; IPR022164; Kinesin-like.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR008984; SMAD_FHA_domain.
DR   Gene3D; G3DSA:2.60.200.20; FHA; 1.
DR   Gene3D; G3DSA:3.40.850.10; kinesin_motor; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF12473; DUF3694; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF12423; KIF1B; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00240; FHA; 1.
DR   SMART; SM00129; KISc; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF49879; SMAD_FHA; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_DOMAIN1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_DOMAIN2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Microtubule; Motor protein; Nucleotide-binding.
SQ   SEQUENCE   1698 AA;  191810 MW;  AF50D080C185EA00 CRC64;
     MAGASVKVAV RVRPFNSREM SRDSKCIIQM SGSTTTIVNP KQPKETPKSF SFDYSYWSHT
     SPEDINYASQ KQVYRDIGEE MLQHAFEGYN VCIFAYGQTG AGKSYTMMGK QEKDQQGIIP
     QLCEDLFSRI NDTTNDNMSY SVEVSYMEIY CERVRDLLNP KNKGNLRVRE HPLLGPYVED
     LSKLAVTSYN DIQDLMDSGN KARTVAATNM NETSSRSHAV FNIIFTQKRH DAETNITTEK
     VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEMDS GPNKNKKKKK
     TDFIPYRDSV LTWLLRENLG GNSRTAMVAA LSPADINYDE TLSTLRYADR AKQIRCNAII
     NEDPNNKLIR ELKDEVTRLR DLLYAQGLGD ITDTNTVPGG PKLTNALVGM SPSSSLSALS
     SRAASVSSLH ERILFAPGSE EAIERLKETE KIIAELNETW EEKLRRTEAI RMEREALLAE
     MGVAMREDGG TLGVFSPKKT PHLVNLNEDP LMSECLLYYI KDGVTRVGRE DAERRQDIVL
     SGHFIKEEHC IFRSDSRGGG EAVVTLEPCE GADTYVNGKK VTEPSILRSG NRIIMGKSHV
     FRFNHPEQAR QERERTPCAE TPAEPVDWAF AQRELLEKQG IDMKQEMEQR LQELEDQYRR
     EREEATYLLE QQRLDYESKL EALQKQMDSR YYPEVNEEEE EPEDEVQWTE RECELALWAF
     RKWKWYQFTS LRDLLWGNAI FLKEANAISV ELKKKVQFQF VLLTDTLYSP LPPDLLPPEA
     AKDRETRPFP RTIVAVEVQD QKNGATHYWT LEKLRQRLDL MREMYDRAAE VPSSVVEDCD
     NVVTGGDPFY DRFPWFRLVG RAFVYLSNLL YPVPLVHRVA IVSEKGEVKG FLRVAVQAIS
     ADEEAPDYGS GVRQSGTAKI SFDDQHFEKF QSESCPVVGM SRSGTSQEEL RIVEGQGQGA
     DAGPSADEVN NNTCSAVPPE GLMDSPEKAA LDGPLDTALD HLRLGSTFTF RVTVLQASSI
     SAEYADIFCQ FNFIHRHDEA FSTEPLKNTG RGPPLGFYHV QNIAVEVTKS FIEYIKSQPI
     VFEVFGHYQQ HPFPPLCKDV LSPLRPSRRH FPRVMPLSKP VPATKLSTMT RPSPGPCHCK
     YDLLVYFEIC ELEANGDYIP AVVDHRGGMP CMGTFLLHQG IQRRITVTLL HETGSHIRWK
     EVRELVVGRI RNTPETDEAL IDPNILSLNI LSSGYVHPAQ DDRTFYQFEA AWDSSMHNSL
     LLNRVTPYRE KIYMTLSAYI EMENCTQPAV ITKDFCMVFY SRDAKLPASR SIRNLFGSGS
     LRATEGNRVT GVYELSLCHV ADAGSPGMQR RRRRVLDTSV AYVRGEENLA GWRPRSDSLI
     LDHQWELEKL SLLQEVEKTR HYLLLREKLE TTQRPGPEVL SPASSEDSES RSSSGASSPL
     SAEGQPSPLE APNERQRELA VKCLRLLMHT FNREYTHSHV CISASESKLS EMSVTLMRDP
     SMSPLGAATL TPSSTCPSLI EGRYGATDVR TPQPCSRPAS PEPELLPELD SKKTPSPVRA
     TETEKEPQRL LVPDIQEIRV SPIVSKKGYL HFLEPHTAGW AKRFVVVRRP YAYMYNSDKD
     TVERFVLNLS TAQVEYSEDQ QAMLKTPNTF AVCTEHRGIL LQANSDKDMH DWLYAFNPLL
     AGTIRSKLSR RRSAQMRV
//
ID   KLH17_MOUSE             Reviewed;         640 AA.
AC   Q6TDP3;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Kelch-like protein 17;
DE   AltName: Full=Actinfilin;
GN   Name=Klhl17;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Huang C.Q., Wu S.L., Shan Y.X.;
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Substrate-recognition component of some cullin-RING-
CC       based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex. The
CC       BCR(KLHL17) mediates the ubiquitination and subsequenct
CC       degradation of GLUR6. May play a role in the actin-based neuronal
CC       function (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with F-actin; the interaction disruptes the F-
CC       actin structures and leads to marked changes of neuronal
CC       morphology. Component of a complex, composed of PDZK1, SYNGAP1,
CC       KLHL17 and NMDA receptors. Interacts directly with PDZK1 (via PDZ1
CC       domain); the interaction is important for integrity of actin
CC       cytoskeleton structures in neurons. Interacts with DLG4 and
CC       SYNGAP1. Interacts (via kelch repeats) with GRIK2 (via C-
CC       terminus); the interaction targets GRIK2 for degradation via
CC       ubiquitin-proteasome pathway. Interacts with GRIK1. Interacts with
CC       (via BTB domain) CUL3; the inteaction regulates surface GRIK2
CC       expression (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane, postsynaptic density (By similarity). Cell junction,
CC       synapse (By similarity). Note=Postsynaptic density (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 BACK (BTB/Kelch associated) domain.
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC   -!- SIMILARITY: Contains 6 Kelch repeats.
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DR   EMBL; AY423764; AAR03711.1; -; mRNA.
DR   IPI; IPI00378808; -.
DR   RefSeq; NP_938047.1; NM_198305.2.
DR   UniGene; Mm.423038; -.
DR   ProteinModelPortal; Q6TDP3; -.
DR   SMR; Q6TDP3; 63-320, 339-622.
DR   PhosphoSite; Q6TDP3; -.
DR   PRIDE; Q6TDP3; -.
DR   Ensembl; ENSMUST00000105569; ENSMUSP00000101194; ENSMUSG00000078484.
DR   GeneID; 231003; -.
DR   KEGG; mmu:231003; -.
DR   UCSC; uc008wgs.1; mouse.
DR   CTD; 231003; -.
DR   MGI; MGI:2678948; Klhl17.
DR   GeneTree; ENSGT00590000082773; -.
DR   HOGENOM; HBG713858; -.
DR   HOVERGEN; HBG014286; -.
DR   InParanoid; Q6TDP3; -.
DR   OMA; RGFADTH; -.
DR   OrthoDB; EOG473PQZ; -.
DR   NextBio; 380354; -.
DR   Bgee; Q6TDP3; -.
DR   CleanEx; MM_KLHL17; -.
DR   Genevestigator; Q6TDP3; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR011705; BACK.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR013069; BTB_POZ.
DR   InterPro; IPR015916; Gal_Oxidase_b-propeller.
DR   InterPro; IPR017096; Kelch-like_gigaxonin.
DR   InterPro; IPR006652; Kelch_1.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Gene3D; G3DSA:2.130.10.80; Gal_Oxidase_b-propeller; 1.
DR   Pfam; PF07707; BACK; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF01344; Kelch_1; 5.
DR   PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
DR   SMART; SM00875; BACK; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00612; Kelch; 6.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Cell junction; Cell membrane; Kelch repeat; Membrane;
KW   Postsynaptic cell membrane; Repeat; Synapse; Ubl conjugation pathway.
FT   CHAIN         1    640       Kelch-like protein 17.
FT                                /FTId=PRO_0000119120.
FT   DOMAIN       90    157       BTB.
FT   DOMAIN      192    294       BACK.
FT   REPEAT      341    387       Kelch 1.
FT   REPEAT      388    434       Kelch 2.
FT   REPEAT      436    481       Kelch 3.
FT   REPEAT      482    528       Kelch 4.
FT   REPEAT      530    575       Kelch 5.
FT   REPEAT      576    622       Kelch 6.
FT   REGION      287    639       Interaction with F-actin (By similarity).
FT   REGION      638    640       Interaction with PDZK1 (By similarity).
FT   COMPBIAS     15     50       Pro-rich.
SQ   SEQUENCE   640 AA;  69732 MW;  911D9F08883DA1BC CRC64;
     MQPRGERPAG RTQSPEHSSP GPGPEAPPPP QPPAPEAERA RPRQARPAAP MEGAMQLLSR
     EGHSVAHNSK RHYHDAFVAM SRMRQRGLLC DIVLHVAAKE IRAHKVVLAS CSPYFHAMFT
     NEMSESRQTH VTLHDIDPQA LDQLVQFAYT AEIVVGEGNV QTLLPAASLL QLNGVRDACC
     KFLLSQLDPS NCLGIRGFAD THSCSDLLKA AHRYVLQHFV DVAKTEEFML LPLKQVLELV
     SSDSLNVPSE EDVYRAVLSW VKHDVDTRRQ HVPRLMKCVR LPLLSRDFLL GHVDAESLVR
     HHPDCKDLLI EALKFHLLPE QRGVLGTSRT RPRRCEGAGP VLFAVGGGSL FAIHGDCEAY
     DTRTDRWHVV ASMSTRRARV GVAAVGNRLY AVGGYDGTSD LATVESYDPV TNTWQPEVSM
     GTRRSCLGVA ALHGLLYAAG GYDGASCLNS AERYDPLTGT WTSIAAMSTR RRYVRVATLD
     GNLYAVGGYD SSSHLATVEK YEPQVNSWTP VASMLSRRSS AGVAVLEGAL YVAGGNDGTS
     CLNSVERYST KAGAWESVAP MNIRRSTHDL VAMDGWLYAV GGNDGSSSLN SIEKYNPRTN
     KWVAASCMFT RRSSVGVAVL ELLNFPPPSS PTLSVSSTSL
//
ID   FEZ2_MOUSE              Reviewed;         348 AA.
AC   Q6TYB5;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 44.
DE   RecName: Full=Fasciculation and elongation protein zeta-2;
DE   AltName: Full=Zygin II;
DE   AltName: Full=Zygin-2;
GN   Name=Fez2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CD-1; TISSUE=Testis;
RA   Lopez-Casas P.P., Del Mazo J.;
RT   "Fez2 expression in mouse testis.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Involved in axonal outgrowth and fasciculation (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer; difulfide-linked. May form heterodimers with
CC       FEZ1. Interacts with synaptotagmin (By similarity).
CC   -!- SIMILARITY: Belongs to the zygin family.
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DR   EMBL; AY382580; AAR36860.1; -; mRNA.
DR   EMBL; BC096619; AAH96619.1; -; mRNA.
DR   IPI; IPI00400435; -.
DR   RefSeq; NP_955519.1; NM_199448.2.
DR   UniGene; Mm.236835; -.
DR   ProteinModelPortal; Q6TYB5; -.
DR   PhosphoSite; Q6TYB5; -.
DR   PRIDE; Q6TYB5; -.
DR   Ensembl; ENSMUST00000070039; ENSMUSP00000068987; ENSMUSG00000056121.
DR   GeneID; 225020; -.
DR   KEGG; mmu:225020; -.
DR   UCSC; uc008dov.1; mouse.
DR   CTD; 225020; -.
DR   MGI; MGI:2675856; Fez2.
DR   GeneTree; ENSGT00390000017627; -.
DR   HOVERGEN; HBG005657; -.
DR   OrthoDB; EOG42Z4RC; -.
DR   PhylomeDB; Q6TYB5; -.
DR   NextBio; 377502; -.
DR   ArrayExpress; Q6TYB5; -.
DR   Bgee; Q6TYB5; -.
DR   Genevestigator; Q6TYB5; -.
DR   GermOnline; ENSMUSG00000056121; Mus musculus.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR011680; FEZ.
DR   PANTHER; PTHR12394; FEZ; 1.
DR   Pfam; PF07763; FEZ; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Disulfide bond.
FT   CHAIN         1    348       Fasciculation and elongation protein
FT                                zeta-2.
FT                                /FTId=PRO_0000189529.
FT   COILED      206    280       Potential.
FT   COMPBIAS    273    279       Poly-Lys.
FT   DISULFID    148    148       Interchain (By similarity).
SQ   SEQUENCE   348 AA;  39101 MW;  031D68EF532BB781 CRC64;
     MAADGDWQDF YEFQEPAGSV QEQENCNASP EAGAGAHAGG DSFPALASSL EEKLSLCFRP
     TSEAEPPRAA VRPITECSLL QGDEIWNALT DNYGNVMPVD WKSSHTRTLH LLTLNLSEKG
     MNDGLLFDAS DEEELREQLD MHSIIVSCVN EEPLFTADQV IEEIEEMMQE SPDPEDDETP
     TQSDRLSMLS QEIQTLKRSS MSSYEERVKR LSVSELNELL EEIEAAIKQY SEELVQQLAL
     RDELEFEKEV ENSFISALIE VQNKQKEHKE TAKKKKKLKS GSSQNGRSER SHMPGTYLTT
     VIPYEKKSGP PSVEDLQILT KILHAMKEDS EKVPSLLTDY ILKVLCPT
//
ID   Q6UIL4_MOUSE            Unreviewed;       677 AA.
AC   Q6UIL4;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   05-OCT-2010, entry version 26.
DE   SubName: Full=AHNAK;
DE   Flags: Fragment;
GN   Name=Ahnak;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129/SvEvTACfBr; TISSUE=Spleen;
RA   Petzhold D., Bader M., Bartsch H., Hohaus A., Morano I., Haase H.;
RT   "Mouse Ahnak (desmoyokin) homologous to human AHNAK.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY369977; AAQ82538.1; -; Genomic_DNA.
DR   IPI; IPI00553798; -.
DR   UniGene; Mm.203866; -.
DR   UniGene; Mm.392302; -.
DR   STRING; Q6UIL4; -.
DR   Ensembl; ENSMUST00000092956; ENSMUSP00000090633; ENSMUSG00000069833.
DR   MGI; MGI:1316648; Ahnak.
DR   InParanoid; Q6UIL4; -.
DR   ArrayExpress; Q6UIL4; -.
DR   Bgee; Q6UIL4; -.
DR   Genevestigator; Q6UIL4; -.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
FT   NON_TER     677    677
SQ   SEQUENCE   677 AA;  68759 MW;  3B499C6703D79E11 CRC64;
     GLNLKGPKIK GDVPSVGLEG PNIDLQGPEG KIKFPKFSLP KISAPGVKME GGSTEIGAQM
     PSLEGGLSTS DMKLEGPHLS LKGPGVDLPS VDLSMPKVSG PDLDMNLKGP SLKGDLGASS
     PSMKLHAPGL DLKGVGGKVH IGADGVKMSG IDATTALSVG APDVTLKGPS LQGDLAVSGD
     IKCPKVSVAT PDVSLEASEG AVKLPHMKLP QFGISTPGSD LDINIKGPQV CGELKGSGMD
     VNLKGPQISA PSMDFNLEGP KVKGSLGAAG ELKGPAIGGA LPGISIQGPQ GNLQMPGIKA
     SGCDVKLSSG QISGPEIKGD LKGSGLGLHG XVPDIGVKGP SFNVASPESD FGVSLKGPKV
     KGGVDVSGGV SVPDINLGEG HMSVKGSGVE WKGPQVSSSL NLDTSKLAGN LHFSGPKIEG
     DVKGGQTGLQ GSRAECVWAS RSLGSESGKV TFPKMKIPKF TFSGRELIGR EVGVDVNFPK
     VEANVQAGAG EGKWEESEVK LKKSKIKMPK HIFSKSKGKG GVTGSPEASI SGSKGDLKSS
     KASLGSLEGE VEAEASSPKG KFSLFKSKKP RHRSNSFSDE REFSAPSTPT GTLEFAGGDA
     KGKHGKLKFG TFGGLGSKSK GHYEVTGSDD EAGKLQGSGV SLASKKSRLS SSSSNDSGTK
     VGIQLPEVEL SVSTKKE
//
ID   SDK2_MOUSE              Reviewed;        2176 AA.
AC   Q6V4S5; Q3TTK1; Q5U5W7; Q6ZPP2;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Protein sidekick-2;
DE   Flags: Precursor;
GN   Name=Sdk2; Synonyms=Kiaa1514;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=FVB/N;
RX   PubMed=15213259; DOI=10.1097/01.ASN.0000128975.28958.C2;
RA   Kaufman L., Hayashi K., Ross M.J., Ross M.D., Klotman P.E.;
RT   "Sidekick-1 is upregulated in glomeruli in HIV-associated
RT   nephropathy.";
RL   J. Am. Soc. Nephrol. 15:1721-1730(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 183-2176 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
CC   -!- FUNCTION: Cell adhesion protein that guides axonal terminals to
CC       specific synapses in developing neurons (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6V4S5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6V4S5-2; Sequence=VSP_017526;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q6V4S5-3; Sequence=VSP_017527, VSP_017528;
CC         Note=Due to intron retention. No experimental confirmation
CC         available;
CC   -!- TISSUE SPECIFICITY: Expressed at low levels in the glomeruli.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in many fetal tissues,
CC       inlcuding kidney but shows markedly lower expression in adult
CC       organs. Expression in kidney is high throughout development with
CC       maximal expression occurring near birth.
CC   -!- SIMILARITY: Contains 13 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 6 Ig-like C2-type (immunoglobulin-like)
CC       domains.
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DR   EMBL; AY351699; AAQ57661.1; -; mRNA.
DR   EMBL; AK161326; BAE36324.1; -; mRNA.
DR   EMBL; BC038036; AAH38036.1; -; mRNA.
DR   EMBL; AK129379; BAC98189.1; -; mRNA.
DR   IPI; IPI00172906; -.
DR   IPI; IPI00648795; -.
DR   IPI; IPI00742366; -.
DR   RefSeq; NP_766388.2; NM_172800.2.
DR   UniGene; Mm.130504; -.
DR   UniGene; Mm.401394; -.
DR   ProteinModelPortal; Q6V4S5; -.
DR   SMR; Q6V4S5; 26-1926.
DR   PhosphoSite; Q6V4S5; -.
DR   PRIDE; Q6V4S5; -.
DR   Ensembl; ENSMUST00000041627; ENSMUSP00000038972; ENSMUSG00000041592.
DR   Ensembl; ENSMUST00000103044; ENSMUSP00000099333; ENSMUSG00000041592.
DR   GeneID; 237979; -.
DR   KEGG; mmu:237979; -.
DR   UCSC; uc007mfd.1; mouse.
DR   UCSC; uc007mfe.1; mouse.
DR   UCSC; uc007mfg.1; mouse.
DR   CTD; 237979; -.
DR   MGI; MGI:2443847; Sdk2.
DR   GeneTree; ENSGT00600000084210; -.
DR   HOGENOM; HBG402851; -.
DR   HOVERGEN; HBG080083; -.
DR   InParanoid; Q6V4S5; -.
DR   OMA; RMSVYNA; -.
DR   OrthoDB; EOG4CNQQ4; -.
DR   NextBio; 383620; -.
DR   ArrayExpress; Q6V4S5; -.
DR   Bgee; Q6V4S5; -.
DR   CleanEx; MM_SDK2; -.
DR   Genevestigator; Q6V4S5; -.
DR   GermOnline; ENSMUSG00000041592; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013151; Immunoglobulin.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 20.
DR   Pfam; PF00041; fn3; 13.
DR   Pfam; PF07679; I-set; 5.
DR   Pfam; PF00047; ig; 1.
DR   SMART; SM00060; FN3; 13.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 3.
DR   SUPFAM; SSF49265; FN_III-like; 13.
DR   PROSITE; PS50853; FN3; 13.
DR   PROSITE; PS50835; IG_LIKE; 6.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell adhesion; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Phosphoprotein; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25   2176       Protein sidekick-2.
FT                                /FTId=PRO_0000226979.
FT   TOPO_DOM     25   1936       Extracellular (Potential).
FT   TRANSMEM   1937   1957       Helical; (Potential).
FT   TOPO_DOM   1958   2176       Cytoplasmic (Potential).
FT   DOMAIN       30    112       Ig-like C2-type 1.
FT   DOMAIN      117    204       Ig-like C2-type 2.
FT   DOMAIN      219    298       Ig-like C2-type 3.
FT   DOMAIN      312    402       Ig-like C2-type 4.
FT   DOMAIN      406    495       Ig-like C2-type 5.
FT   DOMAIN      500    589       Ig-like C2-type 6.
FT   DOMAIN      594    687       Fibronectin type-III 1.
FT   DOMAIN      694    790       Fibronectin type-III 2.
FT   DOMAIN      795    894       Fibronectin type-III 3.
FT   DOMAIN      899    990       Fibronectin type-III 4.
FT   DOMAIN      997   1093       Fibronectin type-III 5.
FT   DOMAIN     1100   1198       Fibronectin type-III 6.
FT   DOMAIN     1203   1298       Fibronectin type-III 7.
FT   DOMAIN     1305   1397       Fibronectin type-III 8.
FT   DOMAIN     1404   1500       Fibronectin type-III 9.
FT   DOMAIN     1505   1621       Fibronectin type-III 10.
FT   DOMAIN     1627   1723       Fibronectin type-III 11.
FT   DOMAIN     1728   1822       Fibronectin type-III 12.
FT   DOMAIN     1829   1922       Fibronectin type-III 13.
FT   MOD_RES    2047   2047       Phosphoserine (By similarity).
FT   MOD_RES    2049   2049       Phosphothreonine (By similarity).
FT   CARBOHYD    197    197       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    747    747       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    940    940       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    952    952       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1106   1106       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1592   1592       N-linked (GlcNAc...) (Potential).
FT   DISULFID     52     95       By similarity.
FT   DISULFID    241    288       By similarity.
FT   DISULFID    334    384       By similarity.
FT   DISULFID    427    479       By similarity.
FT   DISULFID    521    573       By similarity.
FT   VAR_SEQ       1   1602       Missing (in isoform 2).
FT                                /FTId=VSP_017526.
FT   VAR_SEQ     534    542       VWEKDGATL -> SMQSGKGRL (in isoform 3).
FT                                /FTId=VSP_017527.
FT   VAR_SEQ     543   2176       Missing (in isoform 3).
FT                                /FTId=VSP_017528.
SQ   SEQUENCE   2176 AA;  239902 MW;  CAF12063E0A6EAD3 CRC64;
     MFSSMWRLPL WTLLALHRIH SAGAQDDVPP YFKTEPVRTQ VHLEGNRLVL TCMAEGSWPL
     EFKWLHNNRE LTRFSLEYRY MITSLDRTHA GFYRCIVRNR MGALLQRQTE VQVAYMGSFE
     EGEKRQSVNH GEAAVIRAPR ISSFPRPQVT WFRDGRKIPP SSRIAITLEN TLVILSTVAP
     DAGRYYVQAV NDKNGDNKTS QPITLAVENV GGPADPIAPT IIIPPKNTSV VAGTSEVTME
     CVANARPLIK LHIVWKKDGA PLSSGISDYN RRLTIANPTV SDAGYYECEA MLRSSSVAPV
     TRGAYLSVLE PPQFVREPER HITAEMEKVV DIPCRAKGVP PPSITWYKDA ALVEVGKLTR
     FKQRSDGGLQ ISGLLPDDTG MLQCFAHNAA GEAQTSTYLA VTSIAPNITR GPLDSTVIDG
     MSVVLACETS GAPRPAITWQ KGERILASGS VQLPRFTLLE SGSLLISPTH ISDAGTYTCL
     ATNSRGVDEA SADLVVWART RITKPPQDQS VIKGTQASMV CGVTHDPRVT VRYVWEKDGA
     TLAVETNPRI RLDRNGSLHI SQTWSGDIGT YTCRVLSAGG NDSRNAHLRV RQLPHAPEHP
     VATLSTVERR AINLTWAKPF DGNSPLMRYV LEMSENNAPW TILLASVDPE ATSVMVKGLV
     PARSYQFRLC AVNDVGKGQF SKDTERVSLP EEPPTAPPQN VIASGRTNQS IMIQWQPPPE
     SHQNGILKGY IIRYCLAGLP VGYQFKNITD ADVNNLLLED LIIWTNYEIE VAAYNSAGLG
     VYSSKVTEWT LQGVPTVPPG NVHAEATNST TIRFTWNAPS PQFINGINQG YKLIAWEPAQ
     EEEVTMVTAR PNFQDSIHVG FVSGLKKFTE YFTSVLCFTT PGDGPRSSPQ LVRTHEDVPG
     PVGHLSFNDI LDTSLKVSWQ EPGEKNGILT GYRISWEEYN RTNTRVTHYL PNVTLEYRVT
     GLTALTTYTI EVAAMTSKGQ GQVSASTISS GVPPELPGAP TNLGISNIGP RSVTLQFRPG
     YDGKTSISRW VVEAQVGVIG EGEEWLLIYQ LGNEPDARSM EVPDLNPFTY YSFRMRQVNI
     VGTSPPSQPS RKIQTLQAPP DIAPANVTLR TASETSLWLR WMPLPEMEYN GNPESVGYKI
     KYGRSDGHGK TLSHTVQDRV EREYTIEDLE EWTEYRVQVQ AFNAIGSGPW SQAVVGRTRE
     SVPSSGPTNV SALATTSSSM LVRWSEIPEA DRNGLVLGYK VRYKEKDSDS QPRFWLVEGN
     SSRSAQLTGL GKYVLYEVQV LAFTRIGDGS PSHPPILERT LDDVPGPPMG ILFPEVRTTS
     VRLIWQPPAA PNGIILAYQI THRLNATTAN TATVEVLAPS ARQYMATGLK PESVYLFRIT
     AQTRKGWGEA AEALVVTTEK RDRPQPPSKP VVQQEDVKAR SVLLSWEPGS DGLSPVRYYT
     IQTRELPSGR WALHSASVSH NASAFTVDRL KPFTSYKFRV KATNDIGDSE FSEESESLTT
     LQAAPDEAPT ILSVTPHTTT SVLIRWQPPS EDKINGILLG FRIRYRELLY DGLRGFTLRG
     INNPGAKWAE LTSLYSMRNL TRPSLTQYEL DNLSKHRRYE IRMSIYNAVG EGPLSPPQEV
     FVGEAVPTAA PQNVAIHSAT ATQLDVTWEP PPLDNQNGDI QGYKIYFWEV QRRNLTERVK
     TLFLAENSVK LKNLTGYTAY MVSVAAFNAA GDGPRSTPTR GQTQQAAPSA PGSVKFSELT
     TTSVNVSWDA PQFPNGPLEG YRLVYEPCTP VDGVSKIVTV DVKGNSPLWL KVKDLAEGMT
     YRFRIKAKTF TYGPEIEANI TTGPGEGAPG PPGVPIIVRY SSAIAIHWSS GDPGKGPITR
     YVIEARPSDE GLWDILIKDI PKEVTSYTFS MDILKPGVSY DFRVIAVNDY GFGTPSSPSQ
     SVPAQKASPF YEEWWFLVVI ALVGLIFILL LVFVLIIRGQ SKKYSKKTDS GGNTKSGALG
     HGEMLSLDES SFPALELNNR RLSVKNSFCR KNGLYTRSPP RPSPGSLHYS DEDVTKYNDL
     IPAESSSLTE KPSEISDSQG SDSEYEVDTN TQKAHSFVNH YISDPTYYNS WRRQQKGISR
     AQAYSYTESD SGEPDHVTVP NSNSTQQGSL FRPKASRTPT PQNPPNPQSQ QSTLYRPPSS
     LAPGSRAPIA GFSSFV
//
ID   WDFY3_MOUSE             Reviewed;        3508 AA.
AC   Q6VNB8; Q8C8H7;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=WD repeat and FYVE domain-containing protein 3;
DE   AltName: Full=Beach domain, WD repeat and FYVE domain-containing protein 1;
DE            Short=BWF1;
GN   Name=Wdfy3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC   STRAIN=ICR; TISSUE=Embryonic brain, and Embryonic liver;
RX   PubMed=15342963; DOI=10.1247/csf.29.35;
RA   Chen G.-Y., Muramatsu H., Ichihara-Tanaka K., Muramatsu T.;
RT   "Expression profile of mouse BWF1, a protein with a BEACH domain, WD40
RT   domain and FYVE domain.";
RL   Cell Struct. Funct. 29:35-42(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3317, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- INTERACTION:
CC       Q99J83:Atg5; NbExp=1; IntAct=EBI-2935491, EBI-2911848;
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Note=Co-localizes with autophagic structures in
CC       starved cells (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6VNB8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6VNB8-2; Sequence=VSP_019477, VSP_019478;
CC   -!- TISSUE SPECIFICITY: Detected in liver, kidney and testis.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in fetal brain. Levels
CC       decrease after 14 days of development, and continue to decrease in
CC       newborn mice to arrive at adult levels 3 days after birth.
CC   -!- SIMILARITY: Contains 1 BEACH domain.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 5 WD repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC32952.1; Type=Frameshift; Positions=34;
CC   -----------------------------------------------------------------------
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DR   EMBL; AY336569; AAQ84516.1; -; mRNA.
DR   EMBL; AK047077; BAC32952.1; ALT_FRAME; mRNA.
DR   IPI; IPI00227110; -.
DR   IPI; IPI00466992; -.
DR   RefSeq; NP_766470.2; NM_172882.3.
DR   UniGene; Mm.332522; -.
DR   UniGene; Mm.447999; -.
DR   ProteinModelPortal; Q6VNB8; -.
DR   SMR; Q6VNB8; 2517-2958, 3031-3230, 3390-3423, 3430-3496.
DR   IntAct; Q6VNB8; 2.
DR   STRING; Q6VNB8; -.
DR   PhosphoSite; Q6VNB8; -.
DR   PRIDE; Q6VNB8; -.
DR   Ensembl; ENSMUST00000043529; ENSMUSP00000039880; ENSMUSG00000043940.
DR   Ensembl; ENSMUST00000053177; ENSMUSP00000052607; ENSMUSG00000043940.
DR   GeneID; 72145; -.
DR   KEGG; mmu:72145; -.
DR   UCSC; uc008yis.1; mouse.
DR   UCSC; uc008yit.1; mouse.
DR   CTD; 72145; -.
DR   MGI; MGI:1096875; Wdfy3.
DR   eggNOG; roNOG12728; -.
DR   HOGENOM; HBG505246; -.
DR   HOVERGEN; HBG094156; -.
DR   InParanoid; Q6VNB8; -.
DR   OMA; RERGLWG; -.
DR   OrthoDB; EOG408N73; -.
DR   NextBio; 335556; -.
DR   ArrayExpress; Q6VNB8; -.
DR   Bgee; Q6VNB8; -.
DR   CleanEx; MM_WDFY3; -.
DR   Genevestigator; Q6VNB8; -.
DR   GermOnline; ENSMUSG00000043940; Mus musculus.
DR   GO; GO:0003831; F:beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR000409; Beige_BEACH.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 6.
DR   Gene3D; G3DSA:1.10.1540.10; Beige_BEACH; 1.
DR   Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 1.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF02138; Beach; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF00400; WD40; 2.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF81837; Beige_BEACH; 1.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS50197; BEACH; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Membrane; Metal-binding; Phosphoprotein; Repeat;
KW   WD repeat; Zinc; Zinc-finger.
FT   CHAIN         1   3508       WD repeat and FYVE domain-containing
FT                                protein 3.
FT                                /FTId=PRO_0000242694.
FT   DOMAIN     2665   2958       BEACH.
FT   REPEAT     3059   3097       WD 1.
FT   REPEAT     3107   3146       WD 2.
FT   REPEAT     3149   3188       WD 3.
FT   REPEAT     3192   3236       WD 4.
FT   REPEAT     3390   3429       WD 5.
FT   ZN_FING    3436   3496       FYVE-type.
FT   COMPBIAS    472    475       Poly-Ser.
FT   COMPBIAS   2498   2501       Poly-Glu.
FT   MOD_RES     653    653       Phosphotyrosine (By similarity).
FT   MOD_RES     817    817       Phosphoserine (By similarity).
FT   MOD_RES     818    818       Phosphothreonine (By similarity).
FT   MOD_RES     822    822       Phosphotyrosine (By similarity).
FT   MOD_RES    1696   1696       Phosphoserine (By similarity).
FT   MOD_RES    1699   1699       Phosphoserine (By similarity).
FT   MOD_RES    3317   3317       Phosphoserine.
FT   VAR_SEQ     782    809       Missing (in isoform 2).
FT                                /FTId=VSP_019477.
FT   VAR_SEQ     942   3508       Missing (in isoform 2).
FT                                /FTId=VSP_019478.
SQ   SEQUENCE   3508 AA;  392338 MW;  9718CB1AABCB3B8E CRC64;
     MNMVKRIMGR PRQEECSPQD NALGLMHLRR LFTELCHPPR HMTQKEQEEK LYMMLPVFNR
     VFGNAPPNTM TEKFSDLLQF TTQVSRLMVT EIRRRASNKS TEAASRAIVQ FLEINQSEEA
     SRGWMLLTTI NLLASSGQKT VDCMTTMSVP STLVKCLYLF FDLPHVPEAG GGAQNELPLA
     ERRGLLQKAF VQILVKLCSF VSPAEELAQK DDLQLLFSAI TSWCPPYNLP WRKSAGEVLM
     TISRHGLSVN VVKYIHEKEC LSTCVQNMQQ SDDLSPLEIV EMFAGLSCFL KDSSDVSQTL
     LDDFRIWQGY NFLCDLLLRL EQGKEAECRD ALKDLVSLVT SLTTYGVSEL KPAGVTTGAP
     FLLPGFAVPQ PAGKGHSVRN IQAFAVLQNA FLKAKTNFLA QIILDAITNI YMADNANYFI
     LESQHTLSQF AEKISKLPEV QNKYFEMLEF VVFSLNYIPC KELISVSILL KSSSSYHCSI
     IAMKTLLKFT RHDYIFKDVF REVGLLEVMV NLLHKYAALL KDPAQALNEQ GDSRNNSSVE
     DQKHLALLVM EALTVLLQGS NTNAGIFREF GGARCAHNIV KYPQCRQHAL MTIQQLVLSP
     NGEDDMGTLL GLMHSAPPTE LQLKTDILRA LLSVLRESHR SRTVFRKVGG FVYITSLLVA
     MERSLSSPPK NGWEKVSQSQ VLELLHTVFC TLTAALRYEP ANSHFFKTEI QYEKLADAVR
     FLGCFSDLRK ISAVNVFPSN TQPFQRLLEE GAVSVDSVSP TLRHCSKLFI YLYKVATDSF
     DSHAEQIPPC LTSESSLPSP WGTPALSRKR HAFHCVSTPP VYPAKNVTDL KLQVTSSPLQ
     SSDAVIIHPG AMLAMLDLLA SVGSVTQPEH ALDLQLAVAN ILQSLVHTER NQQVMCEAGL
     HARLLQRCGA ALADEDHSLH PPLQRMFERL ASQALEPMVL REFLRLASPL NCGAWDKKLL
     KQYRVHKPSS LSFEPEMRSS VITSLEGLGS DNVFSSHEDN HYRISKSLVK SAEGSTVPLT
     RVKCLVSMTT PHDIRLHGSS VTPAFVEFDT SLEGFGCLFL PSLAPHNAPT NNTVTTGLTD
     GAVVSGMGSG ERFFPPPSGL SYSCWFCIEH FSSPPNNHPV RLLTVVRRAN SSEQHYVCLA
     IVLSAKDRSL IVSTKEELLQ NYVDDFSEES SFYEILPCCA RFRCGELVVE GQWHHLALLM
     SRGMLKNSTA ALYLDGQLVS TVKLHYVHST PGGSGSANPP VLSTVYAYVG TPPAQRQIAS
     LVWRLGPTHF LEEVLPPSSV TTIYELGPNY VGSFQAVCVP CKDAKSEGVT PSPVSLVAEE
     KVSFGLYALS VSSLTVARIR KVYNKLDSKA IAKQLGISSH ENATPVKLVH NAAGHLNGPA
     RTIGAALIGY LGVRTFVPKP VATTLQYIGG AAAILGLVAM ASDVEGLYAA VKALVCVVKS
     NPLASKEMER IKGYQLLAML LKKKRSLLNS HILHLTFSLV GTVDSGHETS IIPNSTAFQD
     LLCDFEVWLH APYELHLSLF EHFIELLTES SEASKNAKLM REFQLIPKLL LTLRDMSLSQ
     PTIAAISNVL SFLLQGFPNS NDLLRFGQFI SSTLPTFAVC EKFVVMEINN EEKPDPGAEE
     EFGGLVSANL ILLRNRLLDI LLKLVYTSKE KTNINLQACE ELVRTLGFDW IMMFMEEHLH
     PTTVTAAMRI LVVLLSNQSI LIKFKEGLSG GGWLEQTDSV LTNKIGTVLG FNVGRSAGGR
     STVREINRDA CHFPGFLVLQ SFLPKHTNVP ALYFLLMALF LQQPVSELPE NLQVSVPVTS
     SRCKQGCQFD LDSIWTFIFG VPASSGTVVS SIHNVCTESA FLLLGMLRSM LNSPWQSEEE
     GSWLREYPVT LMQFFRYLYH NVPDLASMWL SPDFLCALAA TVFPFNIRPY SEMVTDLDDE
     VGSPAEEFKA FAADTGMNRS QSEYCNVGTK TYLTNHPAKK FVFDFMRVLI IDNLCLTPAS
     KQTPLIDLLL EASPERSTRT QQKEFQTHVL DSVMDHLLAA DVLLGEDASL PITSGGSYQV
     LVNNVFYFTQ RVVDKLWQGM FNKESKLLID FIIQLIAQSK RRSQGLSLDA VYHCLNRTIL
     YQFSRAHKTV PQQVALLDSL RVLTVNRNLI LGPGNHDQEF ISCLAHCLIN LHAGSVEGFG
     LEAEARMTTW HIMIPSDIEP DGGYSQDISE GRQLLIKAVN RVWTELIHSK KQVLEELFKV
     SLPVNDRGHV DIALARPLIE EAGLKCWQNH LAHEKKCISR GEALVPTTQS KLSRVSSGFG
     LSKLTGSRRN RKESGLHKHS PSPQEISQWM FTHIAVVRDL VDTQYKEYQE RQQNALKYVT
     EEWCQIECEL LRERGLWGPP IGSHLDKWML EMTEGPCRMR KKMVRNDMFY NHYPYVPETE
     QEASVGKPAR YRRAISYDSK EYYLRLASGN PAIVQDAIVE SSEGEATQQE PEHGEDTIAK
     VKGLVKPPLK RSRSAPDGGD EETQEQLQDQ IAESGSIEEE EKTDNATLLR LLEEGEKIQH
     MYRCARVQGL DTSEGLLLFG KEHFYVIDGF TMTATREIRD IETLPPNMHE PIIPRGARQG
     PSQLKRTCSI FAYEDIKEVH KRRYLLQPIA VEVFSGDGRN YLLAFQKGIR NKVYQRFLAV
     VPSLTDSSES VSGQRPNTSV EQGSGLLSTL VGEKSVTQRW ERGEISNFQY LMHLNTLAGR
     SYNDLMQYPV FPWILSDYDS EEVDLTNPKT FRNLAKPMGA QTDERLAQYK KRYKDWEDPN
     GETPAYHYGT HYSSAMIVAS YLVRMEPFTQ IFLRLQGGHF DLADRMFHSV REAWYSASKH
     NMADVKELIP EFFYLPEFLF NSNNFDLGCK QNGTKLGDVI LPPWAKGDPR EFIRVHREAL
     ECDYVSAHLH EWIDLIFGYK QQGPAAVEAV NVFHHLFYEG QVDIYNINDP LKETATIGFI
     NNFGQIPKQL FKKPHPPKRV RSRLNGDNIG ISVPPGATSD KIFFHHLDNL RPSLTPVKEL
     KEPVGQIVCT DKGILAVEQN KVLIPPAWNK TFAWGYADLS CRLGTYESDK AVTVYECLSE
     WGQILCAVCP NPKLVITGGT STVVCVWEMG TSKEKAKPLT LKQALLGHTD TVTCATASLA
     YHIIVSGSRD RTCIIWDLNK LSFLTQLRGH RAPVSALCIN ELTGDIVSCA GTYIHVWSIN
     GNPIVSVNTF TGRSQQIVCC CMSEMNEWDT QNVIVTGHSD GVVRFWRMEF LQVPETPAPE
     PVEDLEMQEG CPEAQIGQQA QDDDSSDSET EEPSVSQDPK DTSSQPSSTS HRPRAASCRA
     TATWCTDSGS DDSRRWSDQL SLDEKDGFIF VNYSEGQTRA HLQGPLAHPH PNPIEARSYS
     RLKPGYRWER QLVFRSKLTM HTAFDRKDNT HPAEVTALGV SKDHSRILVG DSRGRVFSWS
     VSDQPGRSAA DHWVKDEGGD SCSGCSVRFS LTERRHHCRN CGQLFCQKCS RFQSEIKRLK
     ISSPVRVCQN CYYSLQHERG AEDGPRNC
//
ID   NTRK3_MOUSE             Reviewed;         825 AA.
AC   Q6VNS1; A4QPD0; Q9Z2P9; Q9Z2Q0;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=NT-3 growth factor receptor;
DE            EC=2.7.10.1;
DE   AltName: Full=GP145-TrkC;
DE            Short=Trk-C;
DE   AltName: Full=Neurotrophic tyrosine kinase receptor type 3;
DE   AltName: Full=TrkC tyrosine kinase;
DE   Flags: Precursor;
GN   Name=Ntrk3; Synonyms=TrkC;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c;
RX   PubMed=14614136; DOI=10.1073/pnas.2336152100;
RA   Yamauchi J., Chan J.R., Shooter E.M.;
RT   "Neurotrophin 3 activation of TrkC induces Schwann cell migration
RT   through the c-Jun N-terminal kinase pathway.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:14421-14426(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=99017700; PubMed=9802700;
RX   DOI=10.1002/(SICI)1096-9861(19981109)401:1<47::AID-CNE4>3.0.CO;2-C;
RA   Menn B., Timsit S., Calothy G., Lamballe F.;
RT   "Differential expression of TrkC catalytic and noncatalytic isoforms
RT   suggests that they act independently or in association.";
RL   J. Comp. Neurol. 401:47-64(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-516; TYR-705; TYR-709
RP   AND TYR-710, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Receptor for neurotrophin-3 (NT-3). This is a tyrosine-
CC       protein kinase receptor. Known substrates for the Trk receptors
CC       are SHC1, PI 3-kinase, and PLC-gamma-1 (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBUNIT: Exists in a dynamic equilibrium between monomeric (low
CC       affinity) and dimeric (high affinity) structures. Binds SH2B2.
CC       Interacts with SQSTM1 and KIDINS220 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6VNS1-1; Sequence=Displayed;
CC       Name=2; Synonyms=TrkC NC1;
CC         IsoId=Q6VNS1-2; Sequence=VSP_021596, VSP_021597;
CC         Note=Non-catalytic;
CC       Name=3; Synonyms=TrkC NC2;
CC         IsoId=Q6VNS1-3; Sequence=VSP_021598, VSP_021599;
CC         Note=Non-catalytic;
CC   -!- TISSUE SPECIFICITY: Isoform 2 expression is restricted to specific
CC       areas in adult brain. Isoform 3 transcripts are readily detected
CC       early during embryogenesis and are expressed predominantly in
CC       adult brain and gonads.
CC   -!- PTM: Ligand-mediated auto-phosphorylation (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Insulin receptor subfamily.
CC   -!- SIMILARITY: Contains 2 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SIMILARITY: Contains 2 LRR (leucine-rich) repeats.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AY336094; AAP94280.1; -; mRNA.
DR   EMBL; AF035399; AAC72289.1; -; mRNA.
DR   EMBL; AF035400; AAC72290.1; -; mRNA.
DR   EMBL; BC139764; AAI39765.1; -; mRNA.
DR   IPI; IPI00131278; -.
DR   IPI; IPI00380220; -.
DR   IPI; IPI00807839; -.
DR   RefSeq; NP_032772.3; NM_008746.5.
DR   RefSeq; NP_877961.1; NM_182809.2.
DR   UniGene; Mm.33496; -.
DR   UniGene; Mm.421361; -.
DR   HSSP; Q16288; 1WWC.
DR   ProteinModelPortal; Q6VNS1; -.
DR   SMR; Q6VNS1; 32-401, 531-815.
DR   STRING; Q6VNS1; -.
DR   PhosphoSite; Q6VNS1; -.
DR   PRIDE; Q6VNS1; -.
DR   Ensembl; ENSMUST00000039431; ENSMUSP00000037909; ENSMUSG00000059146.
DR   Ensembl; ENSMUST00000039438; ENSMUSP00000038324; ENSMUSG00000059146.
DR   GeneID; 18213; -.
DR   KEGG; mmu:18213; -.
DR   UCSC; uc009hxf.1; mouse.
DR   UCSC; uc009hxh.1; mouse.
DR   UCSC; uc009hxi.1; mouse.
DR   CTD; 18213; -.
DR   MGI; MGI:97385; Ntrk3.
DR   GeneTree; ENSGT00590000082855; -.
DR   HOGENOM; HBG402948; -.
DR   HOVERGEN; HBG056735; -.
DR   InParanoid; Q6VNS1; -.
DR   OMA; ESTDNFV; -.
DR   OrthoDB; EOG4W3SM8; -.
DR   PhylomeDB; Q6VNS1; -.
DR   BRENDA; 2.7.10.1; 244.
DR   NextBio; 293614; -.
DR   ArrayExpress; Q6VNS1; -.
DR   Bgee; Q6VNS1; -.
DR   CleanEx; MM_NTRK3; -.
DR   Genevestigator; Q6VNS1; -.
DR   GermOnline; ENSMUSG00000059146; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005887; C:integral to plasma membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:EC.
DR   GO; GO:0042490; P:mechanoreceptor differentiation; IMP:MGI.
DR   GO; GO:0048691; P:positive regulation of axon extension involved in regeneration; IGI:MGI.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR000372; LRR-contain_N.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR020446; Tyr_kin_neurotrophic_rcpt_3.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   InterPro; IPR020777; Tyr_prot_kinase_NGF_rcpt.
DR   InterPro; IPR002011; Tyr_prot_kinase_rcpt_2_CS.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF01462; LRRNT; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PRINTS; PR01939; NTKRECEPTOR.
DR   PRINTS; PR01942; NTKRECEPTOR3.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00013; LRRNT; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51450; LRR; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Developmental protein;
KW   Differentiation; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Kinase; Leucine-rich repeat; Membrane; Neurogenesis;
KW   Nucleotide-binding; Phosphoprotein; Receptor; Repeat; Signal;
KW   Transferase; Transmembrane; Transmembrane helix;
KW   Tyrosine-protein kinase.
FT   SIGNAL        1     31       By similarity.
FT   CHAIN        32    825       NT-3 growth factor receptor.
FT                                /FTId=PRO_0000260434.
FT   TOPO_DOM     32    429       Extracellular (Potential).
FT   TRANSMEM    430    453       Helical; (Potential).
FT   TOPO_DOM    454    825       Cytoplasmic (Potential).
FT   REPEAT      102    125       LRR 1.
FT   REPEAT      126    149       LRR 2.
FT   DOMAIN      210    300       Ig-like C2-type 1.
FT   DOMAIN      309    382       Ig-like C2-type 2.
FT   DOMAIN      538    825       Protein kinase.
FT   NP_BIND     544    552       ATP (By similarity).
FT   ACT_SITE    679    679       Proton acceptor (By similarity).
FT   BINDING     572    572       ATP (By similarity).
FT   SITE        516    516       Interaction with SHC1 (By similarity).
FT   SITE        820    820       Interaction with PLC-gamma-1 (By
FT                                similarity).
FT   MOD_RES     516    516       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     705    705       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     709    709       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     710    710       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     820    820       Phosphotyrosine (By similarity).
FT   CARBOHYD     68     68       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     72     72       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     79     79       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    133    133       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    163    163       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    203    203       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    218    218       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    232    232       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    259    259       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    267    267       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    272    272       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    294    294       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    375    375       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    388    388       N-linked (GlcNAc...) (Potential).
FT   DISULFID    320    362       By similarity.
FT   VAR_SEQ     467    502       PVAVISGEEDSASPLHHINHGITTPSSLDAGPDTVV -> K
FT                                VLFFQSQEFHGFHLLIKRYCTSICSLRKPLVTGPW (in
FT                                isoform 2).
FT                                /FTId=VSP_021596.
FT   VAR_SEQ     503    825       Missing (in isoform 2).
FT                                /FTId=VSP_021597.
FT   VAR_SEQ     529    612       YVQHIKRRDIVLKRELGEGAFGKVFLAECYNLSPTKDKMLV
FT                                AVKALKDPTLAARKDFQREAELLTNLQHEHIVKFYGVCGDG
FT                                DP -> WVFSNIDNHGILNLKDNRDHLVPSTHYIYEEPEVQ
FT                                SGDVSYPRSHGFREIMLNPISLSGHSKPLNHGIYVEDVNVY
FT                                FSKGRHGF (in isoform 3).
FT                                /FTId=VSP_021598.
FT   VAR_SEQ     613    825       Missing (in isoform 3).
FT                                /FTId=VSP_021599.
FT   CONFLICT    366    366       N -> K (in Ref. 2; AAC72289).
SQ   SEQUENCE   825 AA;  92760 MW;  4DE08AB546CC5BD6 CRC64;
     MDVSLCPAKC SFWRIFLLGS VWLDYVGSVL ACPANCVCSK TEINCRRPDD GNLFPLLEGQ
     DSGNSNGNAS INITDISRNI TSIHIENWRG LHTLNAVDME LYTGLQKLTI KNSGLRNIQP
     RAFAKNPHLR YINLSSNRLT TLSWQLFQTL SLRELRLEQN FFNCSCDIRW MQLWQEQGEA
     RLDSQSLYCI SADGSQLPLF RMNISQCDLP EISVSHVNLT VREGDNAVIT CNGSGSPLPD
     VDWIVTGLQS INTHQTNLNW TNVHAINLTL VNVTSEDNGF TLTCIAENVV GMSNASVALT
     VYYPPRVVSL VEPEVRLEHC IEFVVRGNPT PTLHWLYNGQ PLRESKIIHM DYYQEGEVSE
     GCLLFNKPTH YNNGNYTLIA KNALGTANQT INGHFLKEPF PESTDFFDFE SDASPTPPIT
     VTHKPEEDTF GVSIAVGLAA FACVLLVVLF IMINKYGRRS KFGMKGPVAV ISGEEDSASP
     LHHINHGITT PSSLDAGPDT VVIGMTRIPV IENPQYFRQG HNCHKPDTYV QHIKRRDIVL
     KRELGEGAFG KVFLAECYNL SPTKDKMLVA VKALKDPTLA ARKDFQREAE LLTNLQHEHI
     VKFYGVCGDG DPLIMVFEYM KHGDLNKFLR AHGPDAMILV DGQPRQAKGE LGLSQMLHIA
     SQIASGMVYL ASQHFVHRDL ATRNCLVGAN LLVKIGDFGM SRDVYSTDYY RVGGHTMLPI
     RWMPPESIMY RKFTTESDVW SFGVILWEIF TYGKQPWFQL SNTEVIECIT QGRVLERPRV
     CPKEVYDVML GCWQREPQQR LNIKEIYKIL HALGKATPIY LDILG
//
ID   ANPRB_MOUSE             Reviewed;        1047 AA.
AC   Q6VVW5; Q6VVW3; Q6VVW4; Q8CGA9;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Atrial natriuretic peptide receptor 2;
DE            EC=4.6.1.2;
DE   AltName: Full=Atrial natriuretic peptide receptor type B;
DE            Short=ANP-B;
DE            Short=ANPR-B;
DE            Short=NPR-B;
DE   AltName: Full=Guanylate cyclase B;
DE            Short=GC-B;
DE   Flags: Precursor;
GN   Name=Npr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=129S6/SvEvTac; TISSUE=Spleen;
RX   PubMed=14514678; DOI=10.1074/jbc.M308680200;
RA   Tamura N., Garbers D.L.;
RT   "Regulation of the guanylyl cyclase-B receptor by alternative
RT   splicing.";
RL   J. Biol. Chem. 278:48880-48889(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=15572448; DOI=10.1073/pnas.0407894101;
RA   Tamura N., Doolittle L.K., Hammer R.E., Shelton J.M., Richardson J.A.,
RA   Garbers D.L.;
RT   "Critical roles of the guanylyl cyclase B receptor in endochondral
RT   ossification and development of female reproductive organs.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:17300-17305(2004).
CC   -!- FUNCTION: Receptor for the C-type natriuretic peptide NPPC/CNP
CC       hormone. Has guanylate cyclase activity upon binding of its
CC       ligand. May play a role in the regulation of skeletal growth.
CC   -!- CATALYTIC ACTIVITY: GTP = 3',5'-cyclic GMP + diphosphate.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=GC-B1;
CC         IsoId=Q6VVW5-1; Sequence=Displayed;
CC       Name=2; Synonyms=GC-B2;
CC         IsoId=Q6VVW5-2; Sequence=VSP_013583;
CC         Note=Binds ligand, but no cyclase activation;
CC       Name=3; Synonyms=GC-B3;
CC         IsoId=Q6VVW5-3; Sequence=VSP_013584, VSP_013585;
CC         Note=Fail to bind the ligand;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed in the columnar
CC       proliferating and prehypertrophic chondrocyte layers of the tibia.
CC   -!- PTM: Phosphorylation of the protein kinase-like domain is required
CC       for full activation by CNP (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice mainly display dwarfism associated with
CC       impairment of endochondral ossification, reduced growth of
CC       longitudinal vertebra and limb-bone. Self-clasping and priapism
CC       that could be due to neuronal disorder are detected. The
CC       development of the female reproductive organ is affected.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
CC       cyclase family.
CC   -!- SIMILARITY: Contains 1 guanylate cyclase domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AY323833; AAQ02634.1; -; Genomic_DNA.
DR   EMBL; AY323832; AAQ02634.1; JOINED; Genomic_DNA.
DR   EMBL; AY323833; AAQ02635.1; -; Genomic_DNA.
DR   EMBL; AY323832; AAQ02635.1; JOINED; Genomic_DNA.
DR   EMBL; AY323833; AAQ02636.1; -; Genomic_DNA.
DR   EMBL; AY323832; AAQ02636.1; JOINED; Genomic_DNA.
DR   EMBL; BC042470; AAH42470.1; -; mRNA.
DR   IPI; IPI00466676; -.
DR   IPI; IPI00828491; -.
DR   IPI; IPI00890312; -.
DR   RefSeq; NP_776149.1; NM_173788.3.
DR   UniGene; Mm.103477; -.
DR   ProteinModelPortal; Q6VVW5; -.
DR   SMR; Q6VVW5; 24-450, 486-1037.
DR   STRING; Q6VVW5; -.
DR   PhosphoSite; Q6VVW5; -.
DR   PRIDE; Q6VVW5; -.
DR   Ensembl; ENSMUST00000030191; ENSMUSP00000030191; ENSMUSG00000028469.
DR   Ensembl; ENSMUST00000107874; ENSMUSP00000103506; ENSMUSG00000028469.
DR   Ensembl; ENSMUST00000107877; ENSMUSP00000103509; ENSMUSG00000028469.
DR   GeneID; 230103; -.
DR   KEGG; mmu:230103; -.
DR   UCSC; uc008sqm.1; mouse.
DR   CTD; 230103; -.
DR   MGI; MGI:97372; Npr2.
DR   HOGENOM; HBG714686; -.
DR   HOVERGEN; HBG051862; -.
DR   InParanoid; Q6VVW5; -.
DR   OrthoDB; EOG4TF0JG; -.
DR   BRENDA; 4.6.1.2; 244.
DR   ArrayExpress; Q6VVW5; -.
DR   Bgee; Q6VVW5; -.
DR   CleanEx; MM_NPR2; -.
DR   Genevestigator; Q6VVW5; -.
DR   GermOnline; ENSMUSG00000028469; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; TAS:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004383; F:guanylate cyclase activity; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR   GO; GO:0016941; F:natriuretic peptide receptor activity; IDA:MGI.
DR   GO; GO:0008528; F:peptide receptor activity, G-protein coupled; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0060348; P:bone development; IMP:MGI.
DR   GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR001170; Ntpep_rcpt_N.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   Gene3D; G3DSA:3.30.70.1230; A/G_cyclase; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PRINTS; PR00255; NATPEPTIDER.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; A/G_cyclase; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00458; ANF_RECEPTORS; 1.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; cGMP biosynthesis; Disulfide bond; Glycoprotein;
KW   GTP-binding; Lyase; Membrane; Nucleotide-binding; Osteogenesis;
KW   Phosphoprotein; Receptor; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     16       Potential.
FT   CHAIN        17   1047       Atrial natriuretic peptide receptor 2.
FT                                /FTId=PRO_0000012365.
FT   TOPO_DOM     17    458       Extracellular (Potential).
FT   TRANSMEM    459    478       Helical; (Potential).
FT   TOPO_DOM    479   1047       Cytoplasmic (Potential).
FT   DOMAIN      513    786       Protein kinase.
FT   DOMAIN      861    991       Guanylate cyclase.
FT   MOD_RES     513    513       Phosphoserine (By similarity).
FT   MOD_RES     516    516       Phosphothreonine (By similarity).
FT   MOD_RES     518    518       Phosphoserine (By similarity).
FT   MOD_RES     523    523       Phosphoserine (By similarity).
FT   MOD_RES     526    526       Phosphoserine (By similarity).
FT   MOD_RES     529    529       Phosphothreonine (By similarity).
FT   CARBOHYD     24     24       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     35     35       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    161    161       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    195    195       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    244    244       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    277    277       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    349    349       N-linked (GlcNAc...) (Potential).
FT   DISULFID     75    101       By similarity.
FT   DISULFID    439    439       Interchain (By similarity).
FT   DISULFID    448    448       Interchain (By similarity).
FT   VAR_SEQ     407    418       PAAHYSGAEKQI -> VMGERTGRRDWS (in isoform
FT                                3).
FT                                /FTId=VSP_013584.
FT   VAR_SEQ     419   1047       Missing (in isoform 3).
FT                                /FTId=VSP_013585.
FT   VAR_SEQ     520    544       Missing (in isoform 2).
FT                                /FTId=VSP_013583.
FT   CONFLICT    990    990       K -> M (in Ref. 2; AAH42470).
SQ   SEQUENCE   1047 AA;  117057 MW;  34E0C60E501B6D87 CRC64;
     MALPSLLLVV AALAGGVRPP GARNLTLAVV LPEHNLSYAW AWPRVGPAVA LAVEALGRAL
     PVDLRFVSSE LDGACSEYLA PLRAVDLKLY HDPDLLLGPG CVYPAASVAR FASHWRLPLL
     TAGAVASGFA AKNEHYRTLV RTGPSAPKLG EFVVTLHGHF NWTARAALLY LDARTDDRPH
     YFTIEGVFEA LQGSNLSVQH QVYAREPGGP EQATHFIRAN GRIVYICGPL EMLHEILLQA
     QRENLTNGDY VFFYLDVFGE SLRAGPTRAT GRPWQDNRTQ EQAQALREAF QTVLVITYRE
     PPNPEYQEFQ NRLLIRARED FGVELAPSLM NLIAGCFYDG ILLYAQVLNE TIQEGGTRED
     GLRIVEKMQG RRYHGVTGLV VMDKNNDRET DFVLWAMGDL DSGDFQPAAH YSGAEKQIWW
     TGRPIPWVKG APPLDNPPCA FDLDDPSCDK TPLSTLAIVA LGTGVTFIMF GVSSFLIFRK
     LMLEKELASM LWRIRWEELQ FGNSDRYHKG AGSRLTLSLR GSSYGSLMTA HGKYQIFANT
     GHFKGNVVAI KHVNKKRIEL TRQVLFELKH MRDVQFNHLT RFIGACIDPP NICIVTEYCP
     RGSLQDILEN DSINLDWMFR YSLINDLVKG MAFLHNSIIS SHGSLKSSNC VVDSRFVLKI
     TDYGLASFRS TAEPDDSHAL YAKKLWTAPE LLSGNPLPTT GMQKADVYSF AIILQEIALR
     SGPFYLEGLD LSPKEIVQKV RNGQRPYFRP SIDRTQLNEE LVLLMERCWA QDPTERPDFG
     QIKGFIRRFN KEGGTSILDN LLLRMEQYAN NLEKLVEERT QAYLEEKRKA EALLYQILPH
     SVAEQLKRGE TVQAEAFDSV TIYFSDIVGF TALSAESTPM QVVTLLNDLY TCFDAIIDNF
     DVYKVETIGD AYMVVSGLPG RNGQRHAPEI ARMALALLDA VSSFRIRHRP HDQLRLRIGV
     HTGPVCAGVV GLKMPRYCLF GDTVNTASRK ESNGQALKIH VSSTTKDALD ELGCFQLELR
     GDVEMKGKGK MRTYWLLGEQ KGPPGLL
//
ID   UBR2_MOUSE              Reviewed;        1755 AA.
AC   Q6WKZ8; Q6DIB9; Q80U31; Q8BUL9; Q8CGW0; Q8K2I6; Q8R0V7; Q8R130;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=E3 ubiquitin-protein ligase UBR2;
DE            EC=6.3.2.-;
DE   AltName: Full=N-recognin-2;
DE   AltName: Full=Ubiquitin-protein ligase E3-alpha-2;
DE   AltName: Full=Ubiquitin-protein ligase E3-alpha-II;
GN   Name=Ubr2; Synonyms=Kiaa0349;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH UBE2B,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, AND DISRUPTION
RP   PHENOTYPE.
RX   MEDLINE=22948832; PubMed=14585983;
RX   DOI=10.1128/MCB.23.22.8255-8271.2003;
RA   Kwon Y.T., Xia Z., An J.Y., Tasaki T., Davydov I.V., Seo J.W.,
RA   Sheng J., Xie Y., Varshavsky A.;
RT   "Female lethality and apoptosis of spermatocytes in mice lacking the
RT   UBR2 ubiquitin ligase of the N-end rule pathway.";
RL   Mol. Cell. Biol. 23:8255-8271(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   INDUCTION.
RC   STRAIN=C3H/HeN;
RX   PubMed=15548684; DOI=10.1158/0008-5472.CAN-04-2102;
RA   Kwak K.S., Zhou X., Solomon V., Baracos V.E., Davis J., Bannon A.W.,
RA   Boyle W.J., Lacey D.L., Han H.Q.;
RT   "Regulation of protein catabolism by muscle-specific and cytokine-
RT   inducible ubiquitin ligase E3alpha-II during cancer cachexia.";
RL   Cancer Res. 64:8193-8198(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Brain, Mammary gland, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1058 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=16311597; DOI=10.1038/ng1681;
RA   Zenker M., Mayerle J., Lerch M.M., Tagariello A., Zerres K.,
RA   Durie P.R., Beier M., Hulskamp G., Guzman C., Rehder H., Beemer F.A.,
RA   Hamel B.C.J., Vanlieferinghen P., Gershoni-Baruch R., Vieira M.W.,
RA   Dumic M., Auslender R., Gil-da-Silva-Lopes V.L., Steinlicht S.,
RA   Rauh M., Shalev S.A., Thiel C., Winterpacht A., Kwon Y.T.,
RA   Varshavsky A., Reis A.;
RT   "Deficiency of UBR1, a ubiquitin ligase of the N-end rule pathway,
RT   causes pancreatic dysfunction, malformations and mental retardation
RT   (Johanson-Blizzard syndrome).";
RL   Nat. Genet. 37:1345-1350(2005).
RN   [7]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=16488448; DOI=10.1016/j.mrfmmm.2005.12.016;
RA   Ouyang Y., Kwon Y.T., An J.Y., Eller D., Tsai S.-C., Diaz-Perez S.,
RA   Troke J.J., Teitell M.A., Marahrens Y.;
RT   "Loss of Ubr2, an E3 ubiquitin ligase, leads to chromosome fragility
RT   and impaired homologous recombinational repair.";
RL   Mutat. Res. 596:64-75(2006).
RN   [8]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=16606826; DOI=10.1073/pnas.0601700103;
RA   An J.Y., Seo J.W., Tasaki T., Lee M.J., Varshavsky A., Kwon Y.T.;
RT   "Impaired neurogenesis and cardiovascular development in mice lacking
RT   the E3 ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6212-6217(2006).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH UBE2B AND HISTONE
RP   H2A.
RX   PubMed=20080676; DOI=10.1073/pnas.0910267107;
RA   An J.Y., Kim E.-A., Jiang Y., Zakrzewska A., Kim D.E., Lee M.J.,
RA   Mook-Jung I., Zhang Y., Kwon Y.T.;
RT   "UBR2 mediates transcriptional silencing during spermatogenesis via
RT   histone ubiquitination.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:1912-1917(2010).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which is a component of the
CC       N-end rule pathway. Recognizes and binds to proteins bearing
CC       specific N-terminal residues that are destabilizing according to
CC       the N-end rule, leading to their ubiquitination and subsequent
CC       degradation. Plays a critical role in chromatin inactivation and
CC       chromosome-wide transcriptional silencing during meiosis via
CC       ubiquitination of histone H2A. Binds leucine and is a negative
CC       regulator of the leucine-mTOR signaling pathway, thereby
CC       controlling cell growth (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with UBE2B; promotes the UBE2B-H2A interaction
CC       and the ubiquitination of histone H2A by UBE2B and UBR2. Interacts
CC       with RECQL4 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Associated with chromatin
CC       during meiosis.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6WKZ8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6WKZ8-2; Sequence=VSP_015173;
CC       Name=3;
CC         IsoId=Q6WKZ8-3; Sequence=VSP_015172, VSP_015173;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle. Also
CC       expressed in heart, kidney and testis. Expressed in acinar cells
CC       of the pancreas. In testes, expressed primarily in spermatocytes.
CC   -!- INDUCTION: In models of cancer cachexia, induced specifically at
CC       the onset and during the progression of muscle wasting.
CC   -!- DOMAIN: The RING-H2 zinc finger is an atypical RING finger with a
CC       His ligand in place of the fourth Cys of the classical motif.
CC   -!- DISRUPTION PHENOTYPE: Male mice are viable but not fertile, due to
CC       massive apoptosis of spermatocytes. Female mice show severe
CC       prenatal lethality, but the rare surviving are fertile. Fibroblast
CC       cells display spontaneous chromosome instability and fragility.
CC       UBR1/UBR2 double-knockout embryos die at midgestation, with
CC       defects in neurogenesis and cardiovascular development. These
CC       defects included reduced proliferation as well as precocious
CC       migration and differentiation of neural progenitor cells.
CC   -!- SIMILARITY: Belongs to the UBR1 family.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SIMILARITY: Contains 1 UBR-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH25617.1; Type=Erroneous initiation;
CC       Sequence=AAH31403.1; Type=Erroneous initiation;
CC       Sequence=BAC65536.3; Type=Miscellaneous discrepancy; Note=Intron retention;
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DR   EMBL; AY280958; AAQ17202.1; -; mRNA.
DR   EMBL; AY061885; AAL32102.1; -; mRNA.
DR   EMBL; AK122254; BAC65536.3; ALT_SEQ; Unassigned_DNA.
DR   EMBL; BC025617; AAH25617.1; ALT_INIT; mRNA.
DR   EMBL; BC026391; AAH26391.1; -; mRNA.
DR   EMBL; BC031403; AAH31403.1; ALT_INIT; mRNA.
DR   EMBL; BC075642; AAH75642.1; -; mRNA.
DR   EMBL; AK083320; BAC38864.1; -; mRNA.
DR   IPI; IPI00405095; -.
DR   IPI; IPI00468701; -.
DR   IPI; IPI00648087; -.
DR   RefSeq; NP_001170845.1; NM_001177374.1.
DR   RefSeq; NP_666190.2; NM_146078.3.
DR   UniGene; Mm.28234; -.
DR   ProteinModelPortal; Q6WKZ8; -.
DR   SMR; Q6WKZ8; 98-167, 222-303.
DR   PhosphoSite; Q6WKZ8; -.
DR   PRIDE; Q6WKZ8; -.
DR   Ensembl; ENSMUST00000075833; ENSMUSP00000075230; ENSMUSG00000023977.
DR   Ensembl; ENSMUST00000113335; ENSMUSP00000108961; ENSMUSG00000023977.
DR   Ensembl; ENSMUST00000113337; ENSMUSP00000108963; ENSMUSG00000023977.
DR   GeneID; 224826; -.
DR   KEGG; mmu:224826; -.
DR   NMPDR; fig|10090.3.peg.3058; -.
DR   UCSC; uc008cup.1; mouse.
DR   UCSC; uc008cuq.1; mouse.
DR   CTD; 224826; -.
DR   MGI; MGI:1861099; Ubr2.
DR   GeneTree; ENSGT00530000063055; -.
DR   HOVERGEN; HBG080426; -.
DR   InParanoid; Q6WKZ8; -.
DR   OMA; EGFRPDF; -.
DR   OrthoDB; EOG42NHZG; -.
DR   PhylomeDB; Q6WKZ8; -.
DR   NextBio; 377401; -.
DR   ArrayExpress; Q6WKZ8; -.
DR   Bgee; Q6WKZ8; -.
DR   Genevestigator; Q6WKZ8; -.
DR   GermOnline; ENSMUSG00000023977; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IGI:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007141; P:male meiosis I; IMP:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:MGI.
DR   InterPro; IPR003769; ClpS_core.
DR   InterPro; IPR014719; Ribosomal_L7/12_C/ClpS-like.
DR   InterPro; IPR003126; Znf_N-recognin.
DR   InterPro; IPR013993; Znf_N-recognin_met.
DR   InterPro; IPR001841; Znf_RING.
DR   Gene3D; G3DSA:3.30.1390.10; Ribosomal_L7/12_C/ClpS-like; 1.
DR   Pfam; PF02617; ClpS; 1.
DR   Pfam; PF02207; zf-UBR; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00396; ZnF_UBR1; 1.
DR   SUPFAM; SSF54736; Ribosomal_L7/12_C/ClpS-like; 1.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; FALSE_NEG.
DR   PROSITE; PS51157; ZF_UBR; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Ligase; Metal-binding; Nucleus;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1   1755       E3 ubiquitin-protein ligase UBR2.
FT                                /FTId=PRO_0000056141.
FT   ZN_FING      97    168       UBR-type.
FT   ZN_FING    1108   1214       RING-type; atypical.
FT   COILED     1019   1054       Potential.
FT   VAR_SEQ       1    197       Missing (in isoform 3).
FT                                /FTId=VSP_015172.
FT   VAR_SEQ     397    426       RQLQRDFMEDDHERAVSVTALSVQFFTAPT -> ERLQRDY
FT                                VTDDHDREFSVADLSVQIFTVPS (in isoform 2 and
FT                                isoform 3).
FT                                /FTId=VSP_015173.
FT   CONFLICT     59     59       Q -> L (in Ref. 1; AAQ17202).
FT   CONFLICT    137    137       R -> Q (in Ref. 1; AAQ17202 and 3;
FT                                BAC65536).
FT   CONFLICT    143    143       S -> W (in Ref. 1; AAQ17202).
FT   CONFLICT    271    271       S -> P (in Ref. 2; AAL32102).
FT   CONFLICT    429    435       RMLLTEE -> PNAPHRKK (in Ref. 1;
FT                                AAQ17202).
FT   CONFLICT    656    656       L -> P (in Ref. 1; AAQ17202).
FT   CONFLICT    979    979       A -> S (in Ref. 1; AAQ17202).
FT   CONFLICT   1050   1050       S -> F (in Ref. 5; BAC38864).
FT   CONFLICT   1332   1332       C -> W (in Ref. 1; AAQ17202).
FT   CONFLICT   1619   1619       C -> S (in Ref. 4; AAH26391).
SQ   SEQUENCE   1755 AA;  199155 MW;  E6D413D674FBBFDA CRC64;
     MASEMEPEVQ AIDRSLLECS AEEIAGRWLQ ATDLNREVYQ HLAHCVPKIY CRGPNPFPQK
     EDTLAQHILL GPMEWYICAE DPALGFPKLE QANKPSHLCG RVFKVGEPTY SCRDCAVDPT
     CVLCMECFLG SIHRDHRYRM TTSGGGGFCD CGDTEAWKEG PYCQKHKLSS SEVVEEEDPL
     VHLSEDVIAR TYNIFAIMFR YAVDILTWEK ESELPEDLEV AEKSDTYYCM LFNDEVHTYE
     QVIYTLQKAV NCTQKEAIGF ATTVDRDGRR SVRYGDFQYC DQAKTVIVRN TSRQTKPLKV
     QVMHSSVAAH QNFGLKALSW LGSVIGYSDG LRRILCQVGL QEGPDGENSS LVDRLMLNDS
     KLWKGARSVY HQLFMSSLLM DLKYKKLFAL RFAKNYRQLQ RDFMEDDHER AVSVTALSVQ
     FFTAPTLARM LLTEENLMTV IIKAFMDHLK HRDAQGRFQF ERYTALQAFK FRRVQSLILD
     LKYVLISKPT EWSDELRQKF LQGFDAFLEL LKCMQGMDPI TRQVGQHIEM EPEWEAAFTL
     QMKLTHVISM VQDWCALDEK VLIEAYKKCL AVLTQCHGGF TDGEQPITLS ICGHSVETIR
     YCVSQEKVSI HLPISRLLAG LHVLLSKSEV AYKFPELLPL SELSPPMLIE HPLRCLVLCA
     QVHAGMWRRN GFSLVNQIYY YHNVKCRREM FDKDIVMLQT GVSMMDPNHF LMIMLSRFEL
     YQLFSTPDYG KRFSSEVTHK DVVQQNNTLI EEMLYLIIML VGERFNPGVG QVAATDEIKR
     EIIHQLSIKP MAHSELVKSL PEDENKETGM ESVIESVAHF KKPGLTGRGM YELKPECAKE
     FNLYFYHFSR AEQSKAEEAQ RKLKRENKED TALPPPALPP FCPLFASLVN ILQCDVMLYI
     MGTILQWAVE HHGSAWSESM LQRVLHLIGM ALQEEKHHLE NAVEGHVQTF TFTQKISKPG
     DAPHNSPSIL AMLETLQNAP SLEAHKDMIR WLLKMFNAIK KIRECSSSSP VAEAEGTIME
     ESSRDKDKAE RKRKAEIARL RREKIMAQMS EMQRHFIDEN KELFQQTLEL DTSASATLDS
     SPPVSDAALT ALGPAQTQVP EPRQFVTCIL CQEEQEVTVG SRAMVLAAFV QRSTVLSKDR
     TKTIADPEKY DPLFMHPDLS CGTHTGSCGH VMHAHCWQRY FDSVQAKEQR RQQRLRLHTS
     YDVENGEFLC PLCECLSNTV IPLLLPPRSI LSRRLNFSDQ PDLAQWTRAV TQQIKVVQML
     RRKHNAADTS SSEDTEAMNI IPIPEGFRPD FYPRNPYSDS IKEMLTTFGT AAYKVGLKVH
     PNEGDPRVPI LCWGTCAYTI QSIERILSDE EKPVFGPLPC RLDDCLRSLT RFAAAHWTVA
     LLPVVQGHFC KLFASLVPSD SYEDLPCILD IDMFHLLVGL VLAFPALQCQ DFSGSSLATG
     DLHIFHLVTM AHIVQILLTS CTEENGMDQE NPTGEEELAI LSLHKTLHQY TGSALKEAPS
     GWHLWRSVRA AIMPFLKCSA LFFHYLNGVP APPDLQVSGT SHFEHLCNYL SLPTNLIHLF
     QENSDIMNSL IESWCQNSEV KRYLNGERGA ISYPRGANKL IDLPEDYSSL INQASNFSCP
     KSGGDKSRAP TLCLVCGSLL CSQSYCCQAE LEGEDVGACT AHTYSCGSGA GIFLRVRECQ
     VLFLAGKTKG CFYSPPYLDD YGETDQGLRR GNPLHLCQER FRKIQKLWQQ HSITEEIGHA
     QEANQTLVGI DWQHL
//
ID   KCD12_MOUSE             Reviewed;         327 AA.
AC   Q6WVG3; Q3T9E3;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=BTB/POZ domain-containing protein KCTD12;
DE   AltName: Full=Pfetin;
DE   AltName: Full=Predominantly fetal expressed T1 domain;
GN   Name=Kctd12; Synonyms=Pfet1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Czech II;
RX   PubMed=15357420; DOI=10.1007/s10162-003-4042-x;
RA   Resendes B.L., Kuo S.F., Robertson N.G., Giersch A.B., Honrubia D.,
RA   Ohara O., Adams J.C., Morton C.C.;
RT   "Isolation from cochlea of a novel human intronless gene with
RT   predominant fetal expression.";
RL   J. Assoc. Res. Otolaryngol. 5:185-202(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-119, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187 AND THR-198, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187; SER-189 AND
RP   THR-198, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   FUNCTION, INTERACTION WITH GABRB1 AND GABRB2, TETRAMERIZATION,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=20400944; DOI=10.1038/nature08964;
RA   Schwenk J., Metz M., Zolles G., Turecek R., Fritzius T., Bildl W.,
RA   Tarusawa E., Kulik A., Unger A., Ivankova K., Seddik R., Tiao J.Y.,
RA   Rajalu M., Trojanova J., Rohde V., Gassmann M., Schulte U., Fakler B.,
RA   Bettler B.;
RT   "Native GABA(B) receptors are heteromultimers with a family of
RT   auxiliary subunits.";
RL   Nature 465:231-235(2010).
CC   -!- FUNCTION: Auxiliary subunit of GABA-B receptors that determine the
CC       pharmacology and kinetics of the receptor response. Increases
CC       agonist potency and markedly alter the G-protein signaling of the
CC       receptors by accelerating onset and promoting desensitization.
CC   -!- SUBUNIT: Interacts as a tetramer with GABRB1 and GABRB2.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, presynaptic cell
CC       membrane. Cell junction, synapse, postsynaptic cell membrane.
CC       Note=Colocalizes with GABRB1.
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, mainly in the
CC       hippocampus and cerebellum.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
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DR   EMBL; AY267461; AAP92150.1; -; Genomic_DNA.
DR   EMBL; AK172581; BAE43079.1; -; mRNA.
DR   IPI; IPI00421206; -.
DR   RefSeq; NP_808383.3; NM_177715.4.
DR   UniGene; Mm.246466; -.
DR   ProteinModelPortal; Q6WVG3; -.
DR   SMR; Q6WVG3; 28-131.
DR   PhosphoSite; Q6WVG3; -.
DR   PRIDE; Q6WVG3; -.
DR   GeneID; 239217; -.
DR   KEGG; mmu:239217; -.
DR   CTD; 239217; -.
DR   MGI; MGI:2145823; Kctd12.
DR   HOVERGEN; HBG052218; -.
DR   Genevestigator; Q6WVG3; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Synapse.
FT   CHAIN         1    327       BTB/POZ domain-containing protein KCTD12.
FT                                /FTId=PRO_0000191296.
FT   MOD_RES     119    119       Phosphotyrosine.
FT   MOD_RES     173    173       Phosphoserine (By similarity).
FT   MOD_RES     178    178       Phosphoserine (By similarity).
FT   MOD_RES     187    187       Phosphoserine.
FT   MOD_RES     189    189       Phosphoserine.
FT   MOD_RES     198    198       Phosphothreonine.
FT   MOD_RES     200    200       Phosphoserine (By similarity).
FT   MOD_RES     202    202       Phosphoserine (By similarity).
FT   MOD_RES     206    206       Phosphoserine (By similarity).
FT   CONFLICT      7      7       A -> T (in Ref. 2; BAE43079).
FT   CONFLICT     88     88       F -> L (in Ref. 2; BAE43079).
SQ   SEQUENCE   327 AA;  35892 MW;  0C84A1AB0CDFEAF5 CRC64;
     MALADSARGL PNGGGGGGGS GSSSSSAEPP LFPDIVELNV GGQVYVTRRC TVVSVPDSLL
     WRMFTQQQPQ ELARDSKGRF FLDRDGFFFR YILDYLRDLQ LVLPDYFPER SRLQREAEYF
     ELPELVRRLG APQQPGPGPP PPHSRRGVHK EGSLGDELLP LGYAEPEPQE GASAGAPSPT
     LELASRSPSG GAAGPLLTPS QSLDGSRRSG YITIGYRGSY TIGRDAQADA KFRRVARITV
     CGKTSLAKEV FGDTLNESRD PDRPPERYTS RYYLKFNFLE QAFDKLSESG FHMVACSSTG
     TCAFASSTDQ SEDKIWTSYT EYVFCRE
//
ID   Q6XE40_MOUSE            Unreviewed;       585 AA.
AC   Q6XE40;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   SubName: Full=Membrane associated guanylate kinase-like protein;
DE   SubName: Full=Membrane protein palmitoylated 3 (MAGUK p55 subfamily member 3);
DE   SubName: Full=Mpp3 protein;
GN   Name=Mpp3; ORFNames=RP23-398F7.5-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Behrends S.;
RT   "A variant of the mouse DLGH3 cDNA with higher homology to the human
RT   DLG3 gene on human chromosome 17q12-q21.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Garner P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
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DR   EMBL; BC062642; AAH62642.1; -; mRNA.
DR   EMBL; AY236514; AAO65586.1; -; mRNA.
DR   EMBL; AL591145; CAM23246.1; -; Genomic_DNA.
DR   IPI; IPI00351246; -.
DR   RefSeq; NP_031889.2; NM_007863.2.
DR   UniGene; Mm.20449; -.
DR   HSSP; P31016; 1JXO.
DR   ProteinModelPortal; Q6XE40; -.
DR   SMR; Q6XE40; 68-220, 229-582.
DR   STRING; Q6XE40; -.
DR   PRIDE; Q6XE40; -.
DR   Ensembl; ENSMUST00000062801; ENSMUSP00000055469; ENSMUSG00000052373.
DR   Ensembl; ENSMUST00000100400; ENSMUSP00000097969; ENSMUSG00000052373.
DR   Ensembl; ENSMUST00000107168; ENSMUSP00000102786; ENSMUSG00000052373.
DR   GeneID; 13384; -.
DR   KEGG; mmu:13384; -.
DR   UCSC; uc007lqc.1; mouse.
DR   CTD; 13384; -.
DR   MGI; MGI:1328354; Mpp3.
DR   GeneTree; ENSGT00560000077018; -.
DR   HOGENOM; HBG446173; -.
DR   HOVERGEN; HBG001858; -.
DR   InParanoid; Q6XE40; -.
DR   OMA; RYQHQPG; -.
DR   PhylomeDB; Q6XE40; -.
DR   NextBio; 283736; -.
DR   ArrayExpress; Q6XE40; -.
DR   Bgee; Q6XE40; -.
DR   Genevestigator; Q6XE40; -.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR004172; L27.
DR   InterPro; IPR014775; L27_C.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF02828; L27; 2.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00569; L27; 2.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS51022; L27; 2.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   Kinase; Transferase.
SQ   SEQUENCE   585 AA;  66486 MW;  FCF0286E23A82518 CRC64;
     MPVLSEDSGL HETLALLTSQ LRPDSNHREE MGFLRDVFSE KSLSYLMKIH EKLRYYERQS
     PTPVLHSAMA LAEDVMEELQ AASVHSDERE LLQLLSTPHL RAVLMVHDTV AQKNFDPVLP
     PLPDNIDEDF EEESVKIVRL VKNKEPLGAT IRRDEHSGAV VVARIMRGGA ADRSGLVHVG
     DELREVNGIA VLHKRPDEIS QILAQSQGSI TLKIIPATQE EDRFKDSKVF MRALFHYDPR
     EDRAIPCQEA GLPFQRRQVL EVVSQDDPTW WQAKRVGDTN LRAGLIPSKQ FQERRLSYRR
     TTGTLPSPQN FKKPPYDQPC DKETCDCDGY FKGHYVAGLR RSFRLGCRER LGGSQEAKVP
     TGAESQVLLT YEEVARYQHQ PGERPRLVVL IGSLGAHLHE LKQRVVAEDP QQFAVAVPHT
     TRPRKSHERD GVEYHFVSKQ AFEADVHHNK FLEHGEYKEN LYGTSLEAIQ AVMAKNKVCL
     VDVEPEALRH LRTPEFKPYV IFVKPAIQER RKTPPVSPDS EDIASSLDEQ QQEMAASAAF
     IDQHYGHLID TVLVRQDLQE ACSQLRAVIE TLSKDTSWVP ISWVR
//
ID   TACC1_MOUSE             Reviewed;         774 AA.
AC   Q6Y685; Q05A66; Q6Y686;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Transforming acidic coiled-coil-containing protein 1;
GN   Name=Tacc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Spinal cord;
RX   PubMed=15207008; DOI=10.1186/1471-2148-4-16;
RA   Still I.H., Vettaikkorumakankauv A.K., DiMatteo A., Liang P.;
RT   "Structure-function evolution of the transforming acidic coiled coil
RT   genes revealed by analysis of phylogenetically diverse organisms.";
RL   BMC Evol. Biol. 4:16-16(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Likely involved in the processes that promote cell
CC       division prior to the formation of differentiated tissues.
CC   -!- SUBUNIT: Interacts with CH-TOG and YEATS4. Interacts with the
CC       Aurora kinases A and B (STK6 and AURKB). Interacts with LSM7,
CC       TDRD7 and SNRPG. Interacts with GCN5L2 and PCAF (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Cytoplasm, cytoskeleton, centrosome (By similarity).
CC       Note=Nucleus during interphase. Weakly concentrated at centrosomes
CC       during mitosis (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Long;
CC         IsoId=Q6Y685-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short;
CC         IsoId=Q6Y685-2; Sequence=VSP_012650, VSP_012651;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the TACC family.
CC   -!- SIMILARITY: Contains 2 SPAZ (Ser/Pro-rich AZU-1) domains.
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DR   EMBL; AY177412; AAO53447.1; -; mRNA.
DR   EMBL; AY177413; AAO53448.1; -; mRNA.
DR   EMBL; BC125389; AAI25390.1; -; mRNA.
DR   EMBL; BC145709; AAI45710.1; -; mRNA.
DR   IPI; IPI00399972; -.
DR   IPI; IPI00420499; -.
DR   RefSeq; NP_796063.3; NM_177089.4.
DR   RefSeq; NP_955355.1; NM_199323.2.
DR   UniGene; Mm.308452; -.
DR   ProteinModelPortal; Q6Y685; -.
DR   SMR; Q6Y685; 590-623, 727-762.
DR   STRING; Q6Y685; -.
DR   PhosphoSite; Q6Y685; -.
DR   PRIDE; Q6Y685; -.
DR   Ensembl; ENSMUST00000084030; ENSMUSP00000081043; ENSMUSG00000065954.
DR   Ensembl; ENSMUST00000084512; ENSMUSP00000081560; ENSMUSG00000065954.
DR   GeneID; 320165; -.
DR   KEGG; mmu:320165; -.
DR   UCSC; uc009lfs.1; mouse.
DR   UCSC; uc009lft.1; mouse.
DR   CTD; 320165; -.
DR   MGI; MGI:2443510; Tacc1.
DR   GeneTree; ENSGT00530000063855; -.
DR   HOGENOM; HBG443557; -.
DR   HOVERGEN; HBG105967; -.
DR   InParanoid; Q6Y685; -.
DR   OrthoDB; EOG4RJG22; -.
DR   NextBio; 396157; -.
DR   ArrayExpress; Q6Y685; -.
DR   Bgee; Q6Y685; -.
DR   Genevestigator; Q6Y685; -.
DR   GermOnline; ENSMUSG00000065954; Mus musculus.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR   GO; GO:0022027; P:interkinetic nuclear migration; IMP:MGI.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR   GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR   GO; GO:0032886; P:regulation of microtubule-based process; IMP:MGI.
DR   InterPro; IPR007707; TACC.
DR   PANTHER; PTHR13924; TACC; 1.
DR   Pfam; PF05010; TACC; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Cell division; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein; Repeat.
FT   CHAIN         1    774       Transforming acidic coiled-coil-
FT                                containing protein 1.
FT                                /FTId=PRO_0000179987.
FT   DOMAIN      216    294       SPAZ 1.
FT   DOMAIN      354    504       SPAZ 2.
FT   REGION        1     56       Interaction with LSM7 and SNRPG (By
FT                                similarity).
FT   REGION      153    255       Interaction with TDRD7 (By similarity).
FT   REGION      207    424       Interaction with YEATS4 (By similarity).
FT   REGION      670    774       Interaction with CH-TOG (By similarity).
FT   COILED      579    774
FT   MOTIF       452    468       Bipartite nuclear localization signal
FT                                (Potential).
FT   MOD_RES      45     45       Phosphoserine (By similarity).
FT   MOD_RES      51     51       Phosphoserine (By similarity).
FT   MOD_RES      53     53       Phosphoserine (By similarity).
FT   MOD_RES      55     55       Phosphoserine (By similarity).
FT   MOD_RES      56     56       Phosphoserine (By similarity).
FT   MOD_RES      58     58       Phosphoserine (By similarity).
FT   MOD_RES     401    401       Phosphoserine.
FT   VAR_SEQ      55     55       S -> R (in isoform 2).
FT                                /FTId=VSP_012650.
FT   VAR_SEQ      56    461       Missing (in isoform 2).
FT                                /FTId=VSP_012651.
SQ   SEQUENCE   774 AA;  83952 MW;  AE9D412E63180976 CRC64;
     MAFSPWQILS PVQWAKWTWS AVRGSGAGED EAGGPEGDPE EEEDSQAETK SLSFSSDSEG
     NFETPEAETP IRSPLKESCD SSPGLAEPEA KPQESREADE QLVAEVIEKC SPDTCSRSSE
     NEAPQATVDS HPVKDVRGKA EHDVSKISVV RPFSIETRNC TDDPAALGTA AAHGCVPVLP
     GMALPSTTPE ATQDEPVMDR GMGVTLEAFT EASLKTGGPC PEPVASRSKL RKPKPVSLRK
     KMAPEPEMLM EGSPLPKASS PWLPDGLDQN ANPSVLRGSG AQRSPLNLKE TAGVLSNDTS
     DSGVEVAPGS PPLQLEDDFT EDGENVKIRS ALPKQSGRKP SNKLAPSIRK DGVSKPVGVE
     QPSDPTVQDA LLDQMSPKLD PSKRSHPPAN FFGSGPILQN SPPLSSKCSH HFDPNNINTD
     DSGDPCKPTP ALTSSGFCPA TGNHVNEILD SPKKAKSRLI TSGCKVKKYE AQPLDLDACS
     QDEGAVISKI SEIPNRDGHA TDEEKLASTS SCAQKSAGAG VKGIEKETCQ KMEKEELAVH
     GLLESSSEKA PVSVACGGES PLDGICLSEA DKTAVLTLIR EEIITKEIEA NEWKKKYEET
     REEVLEMRKI VAEYEKTIAQ MIEDEQRTSM SSQKSFQQLT MEKEQALADL NSVERSLSDL
     FRRYENLKGV LEGFKKNEEA LKKCAQDYLA RVKQEEQRYQ ALKVHAEEKL DRANEEIAQV
     RSKAKAESAA LHAGLRKEQM KVESLERALQ QKNQEIEELT KICDELIAKL GKTD
//
ID   PERQ2_MOUSE             Reviewed;        1291 AA.
AC   Q6Y7W8; Q0VGQ7; Q3UNS2; Q63ZU9; Q80TV1; Q8K0R0; Q8R0A3;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 47.
DE   RecName: Full=PERQ amino acid-rich with GYF domain-containing protein 2;
DE   AltName: Full=GRB10-interacting GYF protein 2;
DE   AltName: Full=Trinucleotide repeat-containing gene 15 protein;
GN   Name=Gigyf2; Synonyms=Kiaa0642, Perq2, Tnrc15;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
RP   INTERACTION WITH GRB10, AND FUNCTION.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   MEDLINE=22803289; PubMed=12771153; DOI=10.1074/jbc.M211572200;
RA   Giovannone B., Lee E., Laviola L., Giorgino F., Cleveland K.A.,
RA   Smith R.J.;
RT   "Two novel proteins that are linked to insulin-like growth factor
RT   (IGF-I) receptors by the Grb10 adapter and modulate IGF-I signaling.";
RL   J. Biol. Chem. 278:31564-31573(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, Eye, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-878 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 244-1291 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-383, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May act cooperatively with GRB10 to regulate tyrosine
CC       kinase receptor signaling, including IGF1 and insulin receptors.
CC   -!- SUBUNIT: Interacts with GRB10.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6Y7W8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6Y7W8-2; Sequence=VSP_022247;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in heart and liver, in kidney and
CC       brain as well as in testis.
CC   -!- SIMILARITY: Belongs to the PERQ family.
CC   -!- SIMILARITY: Contains 1 GYF domain.
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DR   EMBL; AY176043; AAO46887.1; -; mRNA.
DR   EMBL; BC027137; AAH27137.1; -; mRNA.
DR   EMBL; BC030845; AAH30845.1; -; mRNA.
DR   EMBL; BC082811; AAH82811.1; -; mRNA.
DR   EMBL; BC089036; AAH89036.1; -; mRNA.
DR   EMBL; AK144058; BAE25675.1; -; mRNA.
DR   EMBL; AK122337; BAC65619.1; -; mRNA.
DR   IPI; IPI00473912; -.
DR   IPI; IPI00816882; -.
DR   RefSeq; NP_001103682.1; NM_001110212.1.
DR   RefSeq; NP_666224.3; NM_146112.4.
DR   UniGene; Mm.23065; -.
DR   HSSP; Q9FT92; 1WH2.
DR   ProteinModelPortal; Q6Y7W8; -.
DR   SMR; Q6Y7W8; 532-591.
DR   MINT; MINT-266607; -.
DR   STRING; Q6Y7W8; -.
DR   PhosphoSite; Q6Y7W8; -.
DR   PRIDE; Q6Y7W8; -.
DR   Ensembl; ENSMUST00000027475; ENSMUSP00000027475; ENSMUSG00000048000.
DR   GeneID; 227331; -.
DR   KEGG; mmu:227331; -.
DR   UCSC; uc007bwt.1; mouse.
DR   CTD; 227331; -.
DR   MGI; MGI:2138584; Gigyf2.
DR   HOVERGEN; HBG082121; -.
DR   InParanoid; Q6Y7W8; -.
DR   OMA; APPPHMG; -.
DR   OrthoDB; EOG40VVP7; -.
DR   PhylomeDB; Q6Y7W8; -.
DR   NextBio; 378560; -.
DR   ArrayExpress; Q6Y7W8; -.
DR   Bgee; Q6Y7W8; -.
DR   CleanEx; MM_GIGYF2; -.
DR   Genevestigator; Q6Y7W8; -.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR   GO; GO:0044267; P:cellular protein metabolic process; IMP:MGI.
DR   GO; GO:0007631; P:feeding behavior; IMP:MGI.
DR   GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
DR   GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IMP:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR   GO; GO:0050881; P:musculoskeletal movement; IMP:MGI.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0000084; P:S phase of mitotic cell cycle; IMP:MGI.
DR   GO; GO:0021522; P:spinal cord motor neuron differentiation; IMP:MGI.
DR   InterPro; IPR003169; GYF.
DR   Pfam; PF02213; GYF; 1.
DR   SMART; SM00444; GYF; 1.
DR   SUPFAM; SSF55277; GYF; 1.
DR   PROSITE; PS50829; GYF; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1   1291       PERQ amino acid-rich with GYF domain-
FT                                containing protein 2.
FT                                /FTId=PRO_0000270838.
FT   DOMAIN      534    582       GYF.
FT   REGION      548    564       Required for GRB10-binding.
FT   COMPBIAS    119    273       Arg-rich.
FT   COMPBIAS    437    474       Pro-rich.
FT   COMPBIAS    608   1031       Gln-rich.
FT   COMPBIAS    739    889       Glu-rich.
FT   COMPBIAS   1204   1244       Gln-rich.
FT   MOD_RES      19     19       Phosphoserine (By similarity).
FT   MOD_RES      20     20       Phosphoserine (By similarity).
FT   MOD_RES      25     25       Phosphothreonine.
FT   MOD_RES      26     26       Phosphoserine (By similarity).
FT   MOD_RES      30     30       Phosphoserine (By similarity).
FT   MOD_RES     159    159       Phosphoserine (By similarity).
FT   MOD_RES     161    161       Phosphoserine (By similarity).
FT   MOD_RES     190    190       Phosphoserine (By similarity).
FT   MOD_RES     237    237       Phosphoserine (By similarity).
FT   MOD_RES     243    243       Phosphoserine (By similarity).
FT   MOD_RES     374    374       Phosphothreonine (By similarity).
FT   MOD_RES     377    377       Phosphoserine (By similarity).
FT   MOD_RES     383    383       Phosphothreonine.
FT   MOD_RES     594    594       Phosphoserine (By similarity).
FT   VAR_SEQ       1    868       Missing (in isoform 2).
FT                                /FTId=VSP_022247.
FT   CONFLICT     13     13       E -> G (in Ref. 3; BAE25675).
FT   CONFLICT    549    549       P -> S (in Ref. 4; BAC65619).
SQ   SEQUENCE   1291 AA;  149193 MW;  D05938427E72580A CRC64;
     MAAETQTLNF GPEWLRALSS GGSITSPPLS PALPKYKLAD YRYGREEMLA LFLKDYKIPF
     DLLEKEFLPI LQEEPLPPLA LVPFTEEEQR NFSMSVNSAA VLRLTGRGGG GGTVVGAPRG
     RSSSRGRGRG RGECGFYQRS FDEVEGVFGR GGGREMHRSQ SWEERGDRRF EKPGRKDVGR
     PNFEESGPTS VGRKHEFIRS ESENWRIFRE EQNGEDEDGG WRLAGSRRDG ERWRPHSPDG
     PRSTGWREHM ERRRRFEFDF RDRDDERGYR RVRSGSGSID DDRDSLPEWC LEDAEEEMGT
     FDSSGAFLSL KKVQKEPIPE EQEMDFRPVE EGEERSDSDS SHNEEAKEPD KTNRREGEKT
     DRAGAEASEE VPQTSLSSAR PGTPSDHQPQ EATQFERKDE PKAEQVEKAE EENRSENSLS
     AKVPSRGDET VPASQQPSTP LPPDTASPLL ILSPPVPTPS SASRPVETAA VEAPGMSSVS
     TEPDDEEGLK HLEQQAEKMV AYLQDSALDD ERLTSKLQEH RAKGVSIPLM HEAMQKWYYK
     DPQGEIQGPF NNQEMAEWFQ AGYFTMSLLV KRACDESFQP LGDIMKMWGR VPFSPGPAPP
     PHMGELDQER LTRQQELTAL YQMQHLQYQQ FLIQQQYAQV LAQQQKAALS SQQQQQLALL
     LQQFQALKMR MSDQNIIPSV TRSVSVPDTG SIWELQPAAS QPAVWEGGSV WDLPLDTTAP
     GPSLEQLQQL EKAKAAKLEQ ERREAEMRAK REEEERKRQE ELRRQQEEIL RRQQEEERKR
     REEEELARRK QEEALRRQRE QEIALRRQRE EEERQQQEEA LRRLEERRRE EEERRKQEEL
     LRKQEEEAAK WAREEEEAQR RLEENRLRME EEAARLRHEE EERKRKELEL QRQKDLMRQR
     QQQQEALRRL QQQQQQQQLA QMKLPSSSTW GQQSNTATCQ SQATLSLAEI QKLEEERERQ
     LREEQRRQQR ELMKALQQQQ QQQQQQKLSG WGNVSKPAGT TKSLLEIQQE EARQMQKQQQ
     QQQQQQQQHQ QSNRARNSTH SNLHTSLGNS VWGSINTGPS NQWASELVSS IWSNADTKNS
     NMGFWDDAVK EVGPRNSTNK NKNNASLSKS VGVSNRQNKK VEEEEKLLKL FQGVNKAQDG
     FTQWCEQMLH ALNTANNLDV PTFVSFLKEV ESPYEVHDYT RAYLGDTSEA KEFAKQFLER
     RAKQKVNQQR QQQQQQQQQQ DSVWGMNHST LHSVFQTNQS NNQQSNFEAV QSGKKKKKQK
     MVRADPSLLG FSVNASSERL NMGEIETLDD Y
//
ID   MTMR5_MOUSE             Reviewed;        1867 AA.
AC   Q6ZPE2; Q4QQM2; Q8BK68; Q8K2Z0;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   08-FEB-2011, entry version 45.
DE   RecName: Full=Myotubularin-related protein 5;
DE   AltName: Full=SET-binding factor 1;
DE            Short=Sbf1;
GN   Name=Sbf1; Synonyms=Kiaa3020, Mtmr5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 822-1867.
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1522-1867.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1749, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   STRUCTURE BY NMR OF 1762-1865.
RG   RIKEN structural genomics initiative (RSGI);
RT   "solution structure of the C-terminal pleckstrin homology domain of
RT   Sbf1 from mouse.";
RL   Submitted (MAY-2004) to the PDB data bank.
CC   -!- FUNCTION: Probable pseudophosphatase. Lacks several amino acids in
CC       the catalytic pocket which renders it catalytically inactive as a
CC       phosphatase. The pocket is however sufficiently preserved to bind
CC       phosphorylated substrates, and maybe protect them from
CC       phosphatases. Inhibits myoblast differentiation in vitro and
CC       induces oncogenic transformation in fibroblasts (By similarity).
CC   -!- SUBUNIT: Interacts with the SET domain of MLL/HRX. Interacts with
CC       SUV39H1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class myotubularin subfamily.
CC   -!- SIMILARITY: Contains 1 dDENN domain.
CC   -!- SIMILARITY: Contains 1 DENN domain.
CC   -!- SIMILARITY: Contains 1 GRAM domain.
CC   -!- SIMILARITY: Contains 1 myotubularin phosphatase domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 uDENN domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH29156.1; Type=Erroneous initiation;
CC       Sequence=BAC36139.1; Type=Erroneous initiation;
CC       Sequence=BAC98295.1; Type=Erroneous initiation;
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DR   EMBL; AK129485; BAC98295.1; ALT_INIT; mRNA.
DR   EMBL; BC029156; AAH29156.1; ALT_INIT; mRNA.
DR   EMBL; BC098209; AAH98209.1; -; mRNA.
DR   EMBL; AK076039; BAC36139.1; ALT_INIT; mRNA.
DR   IPI; IPI00875821; -.
DR   RefSeq; NP_001074499.2; NM_001081030.2.
DR   UniGene; Mm.35483; -.
DR   PDB; 1V5U; NMR; -; A=1762-1865.
DR   PDBsum; 1V5U; -.
DR   ProteinModelPortal; Q6ZPE2; -.
DR   SMR; Q6ZPE2; 1764-1865.
DR   STRING; Q6ZPE2; -.
DR   PhosphoSite; Q6ZPE2; -.
DR   PRIDE; Q6ZPE2; -.
DR   Ensembl; ENSMUST00000123791; ENSMUSP00000120725; ENSMUSG00000036529.
DR   GeneID; 77980; -.
DR   KEGG; mmu:77980; -.
DR   UCSC; uc007xfy.1; mouse.
DR   CTD; 77980; -.
DR   MGI; MGI:1925230; Sbf1.
DR   eggNOG; roNOG05349; -.
DR   GeneTree; ENSGT00560000076715; -.
DR   HOGENOM; HBG358271; -.
DR   HOVERGEN; HBG052527; -.
DR   InParanoid; Q6ZPE2; -.
DR   PhylomeDB; Q6ZPE2; -.
DR   ArrayExpress; Q6ZPE2; -.
DR   Bgee; Q6ZPE2; -.
DR   CleanEx; MM_SBF1; -.
DR   Genevestigator; Q6ZPE2; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   GO; GO:0001691; F:pseudophosphatase activity; TAS:MGI.
DR   GO; GO:0001558; P:regulation of cell growth; TAS:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   InterPro; IPR005112; dDENN.
DR   InterPro; IPR001194; DENN.
DR   InterPro; IPR004182; GRAM.
DR   InterPro; IPR010569; Myotub-related.
DR   InterPro; IPR017906; Myotubularin_phosphatase_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR022096; SBF2.
DR   InterPro; IPR005113; uDENN.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF03455; dDENN; 1.
DR   Pfam; PF02141; DENN; 1.
DR   Pfam; PF02893; GRAM; 1.
DR   Pfam; PF06602; Myotub-related; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF12335; SBF2; 1.
DR   Pfam; PF03456; uDENN; 1.
DR   SMART; SM00801; dDENN; 1.
DR   SMART; SM00799; DENN; 1.
DR   SMART; SM00568; GRAM; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00800; uDENN; 1.
DR   PROSITE; PS50947; DDENN; 1.
DR   PROSITE; PS50211; DENN; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR   PROSITE; PS50946; UDENN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Nucleus; Phosphoprotein.
FT   CHAIN         1   1867       Myotubularin-related protein 5.
FT                                /FTId=PRO_0000293476.
FT   DOMAIN       18     86       UDENN.
FT   DOMAIN      128    310       DENN.
FT   DOMAIN      363    432       dDENN.
FT   DOMAIN      880    968       GRAM.
FT   DOMAIN     1120   1596       Myotubularin phosphatase.
FT   DOMAIN     1761   1865       PH.
FT   MOD_RES    1137   1137       Phosphothreonine (By similarity).
FT   MOD_RES    1749   1749       Phosphothreonine.
FT   STRAND     1762   1770
FT   STRAND     1774   1776
FT   STRAND     1779   1786
FT   TURN       1787   1790
FT   STRAND     1791   1799
FT   STRAND     1806   1808
FT   HELIX      1809   1811
FT   STRAND     1812   1816
FT   STRAND     1826   1828
FT   TURN       1830   1832
FT   STRAND     1834   1840
FT   STRAND     1842   1846
FT   HELIX      1850   1861
SQ   SEQUENCE   1867 AA;  208693 MW;  16C7033FAA62CB1A CRC64;
     MARLADYFVL VAFGPHPRGS GEGQGQILQR FPEKDWEDNP FPQGIELFCQ PSGWQLCPER
     NPPTFFVAVL TDINSERHYC ACLTFWEPVE STQEVVCTDN ATEKEEEADG GGQARLSSTA
     PAQPGQLFAP KTLVLVSRLD HAEVFRNSLG LIYAIHVEGL NVSLENVIGN LLTCTVPLAG
     GSQRTISLGA GDRQVIQTPL VDSLPVSRCS VALLFRQLGI TNVLSLFCAA LTEHKVLFLS
     RSYQRLADAC RGLLALLFPL RYSFTYVPIL PAQLLEVLST PTPFIIGVNA AFQAETQELL
     DVIVADLDGG TVTVPECVHI PPLPEPLQSQ THNVLSMVLD PELELADLAF PPPTTSASSL
     KMQDKELRAV FLRLFAQLLQ GYRWCLHIVR IHPEPVIRFH KAAFLGQRGL VEDDFLMKVL
     EGMAFAGFVS ERGVPYRATD LFDELVAHEV ARMRADESHP HRVLRHVQEL AEQLYKNENP
     YPAVAMHKVQ RPGEASHLRR THRPFPRLDE GTIQWIVDQA AAKMQGAPPA VKAERRSTVP
     SGPPMTAILE RCSGPHINSA RRLEVVRNCI SYVFEGKMLE AKKLLPAVLR ALKGRAARRC
     LAHELHLHVQ QNRAVLDHQQ FDFVVRMMNC CLQDCTSLDE HGIASALLPL VTAFCRKLSP
     GVTQFAYSCV QEHVVWSTPQ FWEAMFYGDV QTHIRALYLE PSDGVSPTQE TGEAQSQDDE
     RSALDVASEQ RRLWPTLSRE KQQELVQKEE STVFSQAIHY ANRMSYLLLP LDSSKSRLLR
     ERAGLGDLES ASNSLVTNSM AGSVAESYDT ESGFEDAETC DVAGAVVRFI NRFVDKVCTE
     SGVTSDHLKG LHVMVPDIVQ MHIETLEAVH RESKRLPPIQ KPKLLRPRLL PGEECVLDGL
     RVYLLPDGRE EGVGGSGGGP ALLPAEGAVF LTTYRVIFTG MPTDPLVGEQ VVVRSFPVAA
     LTKEKRISVQ TPVDQLLQDG LQLRSCTFQL LKMAFDEEVG SDSAELFRKQ LHKLRYPPDI
     RATFAFTLGS AHTPGRPPRV TKDKGPSFRT LSRNLMKNAK KTIGRQYVTR KKYNPPGWEH
     RGQPPPEDQE DEISVSEELE PSTLTPSSAL KPSDRMTMSS LVERACCRDY QRLGLGTLSS
     SLSRAKSEPF RISPVNRMYA ICRSYPGLLI VPQSIQDNAL QRVSRCYRQN RFPVVCWRSG
     RSKAVLLRSG GLHGKGVVGL FKAQNTPSPG QAQADSSSLE QEKYLQAVVS SMPRYADSSG
     RNTLSSFSSA HMGGHGKWSS VRASGRSSGL GSDVGSRLAG RDLLSTPHTN GAPPDSGFLR
     PQRAALYIIG DKAQLKGVRP DPLQQWELVP IEVFEARQVK ASFKKLLKAC VPGCPATEPS
     PASFLRSLED SEWLIQIHKL LQISVLVVEL LDSGSSVLVS LEDGWDITTQ VVSLVQLLSD
     PFYRTLEGFR LLVEKEWLSF GHRFSHRGAH TLAGQSSGFT PVFLQFLDCV HQVHLQFPME
     FEFSQFYLKF LGYHHTSRRF RTFLLDSDYE RIELGLLYEE KGERRGQLAC KSVWEYVDRL
     SKRTPMFYNY TYAPEDTEVL RPYSNVSNLK VWDFYTEETL AEGPPYDWEL AQGPPEPPEE
     ERPDGGAPQS RRRVVWPCYD SRPRVQPDAI SRLLEELQRL ETELGRPSER WKDTWDRVKA
     AQRLESRQDG RGTPSSLLVS AVPHHRRSLG VYLQEGPVGS TLSLSLDSDQ SSGSTTSSSR
     QAARRSTSTL YSQFQTAESE NRSYEGILYK KGAFMKPWKA RWFVLDKTKH QLRYYDHRMD
     TECKGVIDLA EVEAVAPGTP TIGAPKTVDE KAFFDVKTTR RVYNFCAQDV PSAQQWVDRI
     QSCLSDA
//
ID   Q6ZPE9_MOUSE            Unreviewed;      1461 AA.
AC   Q6ZPE9;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 50.
DE   SubName: Full=MKIAA3013 protein;
DE   Flags: Fragment;
GN   Name=Scaf11; Synonyms=Sfrs2ip, Srsf2ip, mKIAA3013;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
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DR   EMBL; AK129478; BAC98288.1; -; mRNA.
DR   IPI; IPI00874991; -.
DR   RefSeq; NP_082424.2; NM_028148.2.
DR   UniGene; Mm.324474; -.
DR   ProteinModelPortal; Q6ZPE9; -.
DR   STRING; Q6ZPE9; -.
DR   PhosphoSite; Q6ZPE9; -.
DR   Ensembl; ENSMUST00000109230; ENSMUSP00000104853; ENSMUSG00000033228.
DR   GeneID; 72193; -.
DR   KEGG; mmu:72193; -.
DR   UCSC; uc007xkf.1; mouse.
DR   CTD; 72193; -.
DR   MGI; MGI:1919443; Scaf11.
DR   eggNOG; roNOG13663; -.
DR   GeneTree; ENSGT00530000063661; -.
DR   HOGENOM; HBG281596; -.
DR   HOVERGEN; HBG101126; -.
DR   InParanoid; Q6ZPE9; -.
DR   OrthoDB; EOG4G7BXK; -.
DR   NextBio; 335663; -.
DR   ArrayExpress; Q6ZPE9; -.
DR   Bgee; Q6ZPE9; -.
DR   Genevestigator; Q6ZPE9; -.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Zinc; Zinc-finger.
FT   NON_TER       1      1
SQ   SEQUENCE   1461 AA;  162453 MW;  97C3030FFA01CE57 CRC64;
     RRTDGDRASC AGAAAGPRPQ EIPSQGEMKK KSVYNQNVGD QECDDMEGEE NSNTADASGL
     LYSEADRCPI CLSCLLGKEV GFPESCNHVF CMACILKWAE ILASCPIDRK PFQAVFELSA
     FEGCAKIQVK RRLRETEDKE NQRSFKKQLF YHESSKGNKR KRNTIREDLL CERSDGLKVL
     YRNISNKMDG KKNATVKTNK VQRSNQCTDS CIRNEMSSVF SCGSHSWGPR THRASCTESI
     EVNEISALIR QKRQELELSW FPNTLPGNGR VGSVPWSVET AFLSLASSGL PRTVFPASTT
     SLEHFGTSHK GYALAHTQGG GEKKQTSGTS NTRGSRRKPA ATAPTRRSTR NTRAETVSQS
     QKSPVSNYSE CDAPGNSNSS VSISPPAESE KQTRQAPKRK SVRRGRKPPL LKKKLRRSVP
     PAEKSSSDSV EEETVDSDTP PVLEKEQQSC VESSSICSVQ TDEENHLHLE SCSEQTEENE
     QANNHEIEEQ TESLNSESCT QDPPGLVGED TGIEAKEFCA DHDISPDTSL RGRDSAEHQE
     QLSGSSESEV QALVCSESPP EGSPTCPPSD IEHQPVSSPL GEVSDNTTPV VSDERAEESL
     TVESTDLNDE RTGESLTVES TDLNDSAVNI EAFVESPKME SCEGETAQGL DRHCVPSSDS
     ELPEHIQTEN TEIIPACEHI QTENTEIIPA CEHIQTENTE IIPVCGTLEN ENSDAVQDCE
     DNLLKHNLDN SQSDKFLEET TESLVEHPIH AELPHKEVDQ SEKHFSEDNN ESVPMECDSF
     CSDQNESEVE SSANTDSKQL SENSVPHSSE DKLSSDPAVE KVETVAQPAE SLVDKAPKPR
     TRRSRFHSPS TTWSPNKDAA QEKRRAQSPS PKRETVVESQ SSQSPSPKRE SARGRRKSRS
     LSPKKDVARE RRQSRSPKRE NAREAKRSES GSPRRDTSRE NQRSQSRVKD SSSREKSRSR
     SRERESDREA QRRERDRERR ARRWSRSRSR SRSPSRLRTK SKSSSFGRNE RDNYSPRWKE
     RWTNDGWRCP RGNDRYRRND SEKQNENTRN EKNDITADSN DPSSTDKHRS DCPSWVTEKI
     NSGPDPRTRN PEKLKDSHWE ENRNENSGNS WTKNFGPGWM SSRGRGGRGK GAYRGNFACN
     DQSENRWQSR TPLSGSDSFK SAEQQPSKRK SEQELSFGTA ADRSGWTSAS SWAVRKTLPA
     DVQSYYSSGP QSGWMRQEEE TPEQDSNLKD QTNQVDGSQL PVNMMQPHMS VMQPPVNAPM
     MNMQRNPFTM HPPMPLHPHT GVPLMQVAAP ASIPQGPPPP PPPPPSQQVS YVASQPDGKQ
     VQGLSSASHV SNNMNTQVLP APSAAPANTG SVQGPSSGNT SSSSHVQASN AAVKLAESKK
     LQIQEKAAQE VKLAIKPFYQ NKDITKEEYK EIVRKAVDKV CHSKSGEVNS TKVANLVKAY
     VDKYRYSRKK ALEEPGSTEK T
//
ID   TIAM2_MOUSE             Reviewed;        1715 AA.
AC   Q6ZPF3; Q3TSM6; Q3TZ33; Q6AXF2; Q6NXJ2; Q9JLY2; Q9WVS3;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=T-lymphoma invasion and metastasis-inducing protein 2;
DE            Short=TIAM-2;
DE   AltName: Full=SIF and TIAM1-like exchange factor;
GN   Name=Tiam2; Synonyms=Kiaa2016, Stef;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP   AND DEVELOPMENTAL STAGE.
RC   TISSUE=Brain;
RX   MEDLINE=99292752; PubMed=10364228; DOI=10.1074/jbc.274.25.17837;
RA   Hoshino M., Sone M., Fukata M., Kuroda S., Kaibuchi K., Nabeshima Y.,
RA   Hama C.;
RT   "Identification of the stef gene that encodes a novel guanine
RT   nucleotide exchange factor specific for Rac1.";
RL   J. Biol. Chem. 274:17837-17844(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Inner ear, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1232-1498, DEVELOPMENTAL STAGE, AND
RP   TISSUE SPECIFICITY.
RX   MEDLINE=99443873; PubMed=10512681; DOI=10.1006/geno.1999.5936;
RA   Chiu C.-Y., Leng S., Martin K.A., Kim E., Gorman S., Duhl D.M.;
RT   "Cloning and characterization of T-cell lymphoma invasion and
RT   metastasis 2 (TIAM2), a novel guanine nucleotide exchange factor
RT   related to TIAM1.";
RL   Genomics 61:66-73(1999).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=11707441; DOI=10.1074/jbc.M106186200;
RA   Matsuo N., Hoshino M., Yoshizawa M., Nabeshima Y.;
RT   "Characterization of STEF, a guanine nucleotide exchange factor for
RT   Rac1, required for neurite growth.";
RL   J. Biol. Chem. 277:2860-2868(2002).
RN   [7]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=11900975; DOI=10.1016/S0925-4773(01)00650-5;
RA   Yoshizawa M., Hoshino M., Sone M., Nabeshima Y.;
RT   "Expression of stef, an activator of Rac1, correlates with the stages
RT   of neuronal morphological development in the mouse brain.";
RL   Mech. Dev. 113:65-68(2002).
RN   [8]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=12912917; DOI=10.1093/emboj/cdg413;
RA   Kawauchi T., Chihama K., Nabeshima Y., Hoshino M.;
RT   "The in vivo roles of STEF/Tiam1, Rac1 and JNK in cortical neuronal
RT   migration.";
RL   EMBO J. 22:4190-4201(2003).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=14550769; DOI=10.1016/S1044-7431(03)00122-2;
RA   Matsuo N., Terao M., Nabeshima Y., Hoshino M.;
RT   "Roles of STEF/Tiam1, guanine nucleotide exchange factors for Rac1, in
RT   regulation of growth cone morphology.";
RL   Mol. Cell. Neurosci. 24:69-81(2003).
RN   [10]
RP   FUNCTION, INTERACTION WITH MAP1A; MAP1B; PARP1 AND YWHAE,
RP   PHOSPHORYLATION AT THR-1662, AND MUTAGENESIS OF SER-1655; THR-1656;
RP   THR-1662; THR-1668 AND SER-1672.
RX   PubMed=17320046; DOI=10.1016/j.bbrc.2007.02.028;
RA   Takefuji M., Mori K., Morita Y., Arimura N., Nishimura T.,
RA   Nakayama M., Hoshino M., Iwamatsu A., Murohara T., Kaibuchi K.,
RA   Amano M.;
RT   "Rho-kinase modulates the function of STEF, a Rac GEF, through its
RT   phosphorylation.";
RL   Biochem. Biophys. Res. Commun. 355:788-794(2007).
CC   -!- FUNCTION: Modulates the activity of RHO-like proteins and connects
CC       extracellular signals to cytoskeletal activities. Acts as a GDP-
CC       dissociation stimulator protein that stimulates the GDP-GTP
CC       exchange activity of RHO-like GTPases and activates them.
CC       Activates specifically RAC1, but not CDC42 and RHOA. Mediates
CC       extracellular laminin signals to activate Rac1, contributing to
CC       neurite growth. Involved in lamellipodial formation and
CC       advancement of the growth cone of embryonic hippocampal neurons.
CC       Promotes migration of neurons in the cerebral cortex. When
CC       overexpressed, induces membrane ruffling accompanied by the
CC       accumulation of actin filaments along the altered plasma membrane.
CC   -!- SUBUNIT: Interacts with MAP1A, MAP1B, PARP1 and YWHAE.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell projection, lamellipodium.
CC       Cell projection, filopodium. Cell projection, growth cone.
CC       Note=Localizes to the plasma membrane in neurites.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q6ZPF3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZPF3-2; Sequence=VSP_030977;
CC       Name=3;
CC         IsoId=Q6ZPF3-3; Sequence=VSP_030976;
CC       Name=4;
CC         IsoId=Q6ZPF3-4; Sequence=VSP_030978, VSP_030979;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in fetal brain (at protein level).
CC       Expressed in the olfactory bulb, cortical plate of the cerebral
CC       cortex, caudate putamen, hippocampus, ependymal cells of the
CC       lateral surface of the lateral ventricles of the brain. Weakly
CC       expressed in heart, lung, liver, skeletal muscle, kidney and
CC       testis.
CC   -!- DEVELOPMENTAL STAGE: Expressed in cerebral cortex, predominantly
CC       in the cortical plate and intermediate zone and weakly in the
CC       ventricular zone, in neurites and the growth cone of neurites of
CC       the hippocampus at 15 dpc (at protein level). Expressed in embryo
CC       at 7, 11, 15 and 17 dpc. Expressed in the preplate which consists
CC       of the Cajal-Retzius cells and the precursors of subplate neurons,
CC       in neurons of the telecephalon, in primordia of cerebral cortex
CC       and hippocampus at 12 dpc. Expressed in the cortical plate,
CC       striatum and fourth ventricle of the brain, in the cartilaginous
CC       tissues including Meckel, costal, vertebral and tracheal cartilage
CC       at 14.5 dpc. Expressed in cerebral cortex, hippocampus, olfactory
CC       bulbs, rostral migratory pathway and the striatum at 17 dpc.
CC   -!- DOMAIN: The PH 1 domain and amino acids 619-780 (a region called
CC       TSS; otherwise known as CC-Ex) are necessary for membrane
CC       localization. PH 1 and TSS domains are necessary for Rac1
CC       activity. The PH 2 domain is engaged in the enhancement of the
CC       catalytic activity of the adjacent DH domain. The PH 1, TSS and DH
CC       domains are necessary to induce neurite-like structure.
CC   -!- PTM: Phosphorylated on serine and threonine residues.
CC       Phosphorylated on Thr-1662 by Rho-kinase. Its phosphorylation by
CC       Rho-kinase inhibits its guanine nucleotide exchange activity, its
CC       interaction with MAP1A, MAP1B, PARP1 and YWHAE and reduces its
CC       ability to promote neurite growth.
CC   -!- SIMILARITY: Belongs to the TIAM family.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -!- SIMILARITY: Contains 1 RBD (Ras-binding) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98284.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AB022915; BAA81823.1; -; mRNA.
DR   EMBL; AK129474; BAC98284.1; ALT_INIT; mRNA.
DR   EMBL; AK158137; BAE34377.1; -; mRNA.
DR   EMBL; AK161947; BAE36649.1; -; mRNA.
DR   EMBL; BC067048; AAH67048.1; -; mRNA.
DR   EMBL; BC079600; AAH79600.1; -; mRNA.
DR   EMBL; AF121102; AAF28865.1; -; mRNA.
DR   IPI; IPI00453791; -.
DR   IPI; IPI00885471; -.
DR   IPI; IPI00885555; -.
DR   IPI; IPI00885882; -.
DR   RefSeq; NP_001116470.1; NM_001122998.1.
DR   RefSeq; NP_036008.2; NM_011878.2.
DR   UniGene; Mm.137134; -.
DR   PDB; 3A8P; X-ray; 2.10 A; A/B/C/D=500-757.
DR   PDB; 3A8Q; X-ray; 3.20 A; A/B/C/D=500-757.
DR   PDBsum; 3A8P; -.
DR   PDBsum; 3A8Q; -.
DR   ProteinModelPortal; Q6ZPF3; -.
DR   SMR; Q6ZPF3; 504-741, 907-994, 1115-1482.
DR   STRING; Q6ZPF3; -.
DR   PhosphoSite; Q6ZPF3; -.
DR   PRIDE; Q6ZPF3; -.
DR   Ensembl; ENSMUST00000072156; ENSMUSP00000072020; ENSMUSG00000023800.
DR   GeneID; 24001; -.
DR   KEGG; mmu:24001; -.
DR   CTD; 24001; -.
DR   MGI; MGI:1344338; Tiam2.
DR   eggNOG; roNOG12293; -.
DR   GeneTree; ENSGT00600000084055; -.
DR   HOVERGEN; HBG059279; -.
DR   InParanoid; Q6ZPF3; -.
DR   OMA; SSESSWY; -.
DR   OrthoDB; EOG43R3KW; -.
DR   PhylomeDB; Q6ZPF3; -.
DR   NextBio; 303925; -.
DR   ArrayExpress; Q6ZPF3; -.
DR   Bgee; Q6ZPF3; -.
DR   CleanEx; MM_TIAM2; -.
DR   Genevestigator; Q6ZPF3; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR   GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR   GO; GO:0005057; F:receptor signaling protein activity; IEA:InterPro.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR003116; Raf-like_ras-bd.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00455; RBD; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50898; RBD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell projection; Coiled coil;
KW   Cytoplasm; Guanine-nucleotide releasing factor; Lipoprotein;
KW   Myristate; Phosphoprotein; Repeat.
FT   INIT_MET      1      1       Removed (Potential).
FT   CHAIN         2   1715       T-lymphoma invasion and metastasis-
FT                                inducing protein 2.
FT                                /FTId=PRO_0000317468.
FT   DOMAIN      504    618       PH 1.
FT   DOMAIN      831    902       RBD.
FT   DOMAIN      911    997       PDZ.
FT   DOMAIN     1120   1314       DH.
FT   DOMAIN     1347   1478       PH 2.
FT   COILED      665    692       Potential.
FT   COMPBIAS    215    335       Ser-rich.
FT   COMPBIAS   1512   1564       Ser-rich.
FT   MOD_RES    1662   1662       Phosphothreonine.
FT   LIPID         2      2       N-myristoyl glycine (Potential).
FT   VAR_SEQ       1   1096       Missing (in isoform 3).
FT                                /FTId=VSP_030976.
FT   VAR_SEQ     616    616       Missing (in isoform 2).
FT                                /FTId=VSP_030977.
FT   VAR_SEQ     786    788       MFD -> VSS (in isoform 4).
FT                                /FTId=VSP_030978.
FT   VAR_SEQ     789   1715       Missing (in isoform 4).
FT                                /FTId=VSP_030979.
FT   MUTAGEN    1655   1655       S->A: No change of phosphorylation by
FT                                Rho-kinase.
FT   MUTAGEN    1656   1656       T->A: No change of phosphorylation by
FT                                Rho-kinase.
FT   MUTAGEN    1662   1662       T->A: Strongly decrease phosphorylation
FT                                by Rho-kinase. No change in promoting
FT                                neurite growth; when associated with A-
FT                                1668 and A-1672.
FT   MUTAGEN    1668   1668       T->A: Slight decrease phosphorylation by
FT                                Rho-kinase. No change in promoting
FT                                neurite growth; when associated with A-
FT                                1662 and A-1672.
FT   MUTAGEN    1672   1672       S->A: Slight decrease phosphorylation by
FT                                Rho-kinase. No change in promoting
FT                                neurite growth; when associated with A-
FT                                1662 and A-1668.
FT   CONFLICT     45     45       G -> D (in Ref. 3; BAE34377).
FT   CONFLICT     98     98       T -> A (in Ref. 2; BAC98284).
FT   CONFLICT    261    261       E -> D (in Ref. 2; BAC98284).
FT   CONFLICT    803    803       K -> Q (in Ref. 1; BAA81823).
FT   CONFLICT    856    856       V -> I (in Ref. 1; BAA81823).
FT   CONFLICT    860    860       V -> A (in Ref. 1; BAA81823 and 2;
FT                                BAC98284).
FT   CONFLICT   1077   1077       L -> P (in Ref. 1; BAA81823).
FT   CONFLICT   1234   1234       R -> K (in Ref. 5; AAF28865).
FT   CONFLICT   1248   1248       F -> C (in Ref. 5; AAF28865).
FT   CONFLICT   1397   1397       N -> D (in Ref. 5; AAF28865).
FT   CONFLICT   1446   1446       I -> V (in Ref. 5; AAF28865).
FT   CONFLICT   1611   1611       I -> L (in Ref. 2; BAC98284).
FT   STRAND      511    520
FT   HELIX       521    523
FT   STRAND      524    527
FT   STRAND      534    540
FT   STRAND      544    549
FT   STRAND      563    567
FT   STRAND      572    575
FT   STRAND      583    589
FT   STRAND      595    599
FT   HELIX       603    624
FT   HELIX       630    659
FT   HELIX       665    699
FT   HELIX       707    711
FT   HELIX       716    721
FT   HELIX       730    739
SQ   SEQUENCE   1715 AA;  192567 MW;  96C1E063BC6F36C0 CRC64;
     MGNSESQYTF QGSKNHSNTV TGAKQKPCSL KIRSVHAKDE KSLHGWTHGS SGAGYKSRSL
     ARSCLSHFKN HQPYATRLSG PTCKVSKGTT YSKHRANTPG NDFQGNSGAF LPENGFHYVD
     RESEESHITS NGHLLTCYGR KESLASTPPG EDHRSPRVLI KTLGKLDGCL RVEFHNGGNP
     HKGTSEDPSG PVRLLRYSPT LASETCPVRE TRRHSAAGSP SSQRPSPTDS RLRSSKGSSL
     SSESSWYDSP WGNAGEVSEV EGSFLAPSTP DPSLPSSFPP SDTKKPFNQS SSLSSLRELY
     KDPNLGCRSP SGTCLSSNEY ISSQVSLNNR VSFASDMDVP SRVDHRDPLH YSSFTLPCRK
     SKALTEDAAK KDTLKARMRR FSDWTGSLSR KKRKLQEPRS MEGSEYFDSH SDGLNAEGQV
     PAQTSSLLWS GGSAQTLPHR SESTHAISVD PLRQNIYENF MRELEMSRSN TEHVETSTET
     MESSSESVSS LEQLDLLFEK EQGVVRKAGW LFFKPLVTLQ KERKLELVAR RKWKQYWVTL
     KGCTLLFYET YGKNSTEQNS APRCALFAED SIVQSVPEHP KKEHVFCLSN SCGDVYLFQA
     TSQTDLENWV TAIHSACASL FAKKHGKEDT VRLLKSQTRS LLQKIDMDSK MKKMAELQLS
     VVSDPKNRKA IENQIRQWEQ NLEKFHMDLF RMRCYLASLQ GGELPNPKSL LAATSRPSKL
     ALGRLGVLSV SSFHALVCSR DDSTLRKRTL SLTQRGKSKK GIFSSLKGLD TLARKGREKR
     ASITQMFDSS HSHGFLGTQL PQKSTNSNKA HDLHLYGSAV DSALRDSMWE VQTYVHFQDN
     EGVTVTIKPE HRVEDVLALV CKMRQLEPTH YGLQLRKVVD KSVEWCVPAL YEYMQEQVYD
     EIEVFPLSVY DVQLTKTGDM TDFGFAVTVQ VDEHQHLNRI FISDVLPDSL AYGGGLRKGN
     EITSLNGEPV SDLDIQQMEA LFSEKSVGLT LVARPVTTRR TLCASWSDSD LFSRDQKSLP
     PSPNQSQLLE EFLDNFRKTA TSDFSNVPEI TTGLKRSQTE GTLDQVPHRE KMEQTFLSAD
     QIAELCRDLN NTHTNSMEAP TESHDPPPRP LARHLSDADR LRKVIQELVD TEKSYVKDLS
     CLFELYLEPL QNETFLTQDE MESLFGSLPE MLEFQKVFLE TLEDAISASS DFSVLETPSQ
     FRKLLFSLGG SFLYYADHFK LYSGFCANHI KVQRVLERAK TDKAFKAFLD ARNPTKQHSS
     TLESYLIKPV QRVLKYPLLL KELVSLTDHE SEEHYHLTEA LKAMEKVASH INEMQKIYED
     YGMVFDQLVA EQSGTEKEVT ELSMGELLMH STVSWLNPFL SLGKARKDIE LTVFVFKRAV
     ILVYKENCKL KKKLPSNSRP AHNSADLDPF KFRWLIPISA LQVRLGNTAG TENNSTWELI
     HTKSEIEGRP ETIFQLCCSD SENKTSIVKV IRSILRENFR RHIKCELPLE KTCKDRLVPL
     KNRVPVSAKL ASSRSLKGLR TSSSSEWPSE PSKGNSLDSD ECSLSSGTQS SGCPVAESRR
     DSKSTELEKD AQEGLAEFPD GLIKESDILS DEDEDFHHPL KQGSPTKDIE IQFQRLKISE
     ESDVHPVGQQ PLTESGEQPK LVRGHFCPIK RKANSTKRGR GTLLKAQTRH QSLDSHPETA
     SIDLNLVLER EFSVQSLTSV VNEEGFYETQ SHGKS
//
ID   TEX2_MOUSE              Reviewed;        1128 AA.
AC   Q6ZPJ0; B1ATR1;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Testis-expressed sequence 2 protein;
GN   Name=Tex2; Synonyms=Kiaa1738;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-268, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161; THR-261; SER-264;
RP   SER-265; SER-752; SER-791 AND SER-795, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294 AND SER-591, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98244.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK129434; BAC98244.1; ALT_INIT; mRNA.
DR   EMBL; AL663053; CAM24359.1; -; Genomic_DNA.
DR   IPI; IPI00420516; -.
DR   RefSeq; NP_938034.2; NM_198292.3.
DR   UniGene; Mm.102407; -.
DR   STRING; Q6ZPJ0; -.
DR   PhosphoSite; Q6ZPJ0; -.
DR   PRIDE; Q6ZPJ0; -.
DR   Ensembl; ENSMUST00000042780; ENSMUSP00000041985; ENSMUSG00000040548.
DR   GeneID; 21763; -.
DR   KEGG; mmu:21763; -.
DR   UCSC; uc007lzb.1; mouse.
DR   CTD; 21763; -.
DR   MGI; MGI:102465; Tex2.
DR   GeneTree; ENSGT00390000000463; -.
DR   HOGENOM; HBG402821; -.
DR   HOVERGEN; HBG062867; -.
DR   InParanoid; Q6ZPJ0; -.
DR   OMA; HVQRSVS; -.
DR   OrthoDB; EOG49ZXNM; -.
DR   PhylomeDB; Q6ZPJ0; -.
DR   NextBio; 301084; -.
DR   ArrayExpress; Q6ZPJ0; -.
DR   Bgee; Q6ZPJ0; -.
DR   CleanEx; MM_TEX2; -.
DR   Genevestigator; Q6ZPJ0; -.
DR   GermOnline; ENSMUSG00000040548; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR019411; DUF2404.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Pfam; PF10296; DUF2404; 1.
DR   SMART; SM00233; PH; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   1128       Testis-expressed sequence 2 protein.
FT                                /FTId=PRO_0000244480.
FT   TRANSMEM    473    493       Helical; (Potential).
FT   TRANSMEM    495    515       Helical; (Potential).
FT   COMPBIAS     43     51       Poly-Glu.
FT   COMPBIAS    134    195       Ser-rich.
FT   COMPBIAS    817    822       Poly-Glu.
FT   COMPBIAS   1040   1043       Poly-Pro.
FT   MOD_RES     161    161       Phosphoserine.
FT   MOD_RES     164    164       Phosphoserine (By similarity).
FT   MOD_RES     195    195       Phosphoserine (By similarity).
FT   MOD_RES     261    261       Phosphothreonine.
FT   MOD_RES     264    264       Phosphoserine.
FT   MOD_RES     265    265       Phosphoserine.
FT   MOD_RES     268    268       Phosphothreonine.
FT   MOD_RES     269    269       Phosphoserine (By similarity).
FT   MOD_RES     294    294       Phosphoserine.
FT   MOD_RES     591    591       Phosphoserine.
FT   MOD_RES     607    607       Phosphotyrosine (By similarity).
FT   MOD_RES     752    752       Phosphoserine.
FT   MOD_RES     791    791       Phosphoserine.
FT   MOD_RES     795    795       Phosphoserine.
FT   CARBOHYD    593    593       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   1128 AA;  125226 MW;  38C2201896B5E479 CRC64;
     MTSLNGRHAE KTIDMPKPSA PKVHVQRSVS RDTIAIHFSA SGEEEEEEEE EFRGYLEEGL
     DDQSIVTGLE AKEDLYLESQ GGHDPAGPVS TAPADGLSVS ESPAILPVSE NTVKLLESPA
     PALQVLSPVP LALSPGSSSS GPLASSPSVS SLSEQKTSSS SPLSSPSKSP VLSSSASSSA
     LSSAKPFMSL VKSLSTEVEP KESPHPPRHR HLMKTLVKSL STDTSRQESD TVSYKPPDSK
     LNLHLFKQFT QPRNTGGDSK TAPSSPLTSP SDTRSFFKVP EMEAKIEDTK RRLSEVIYEP
     FQLLSKIIGE ESGSHRPKAL SASASELSSL SGLNGHLESN NYSIKEEEGD SEGEGYGSDS
     NTSRSDHLKP TEDASKEVEP KGSQASSLKD LGLKTSSLVL EKCSLSALVS KEDEEFCELY
     TEDFELETEG EGRLDKTLDL PLKPEVLASD GVALESEDEE DSATEHQELP VKTLGFFIMC
     VYAYLILPLP YYMSGLFLGV GLGFMTAVCM IWFFTPPSAH KHHKSLKALR HQSTRSLDIK
     EPEILKGWMN EIYNYDPETY HATLTHSVFV RLEGGTLRLS KPNKNISRRA SYNETKPEVT
     YISQKIYDLS DSKIYLVPKS LARKRIWNKK YPICIELGRQ DDFMSKAQSD KEATEEKPPP
     EKELPSEDLK KPPQPQEGTK SSQRDPILYL FGRTGREKEE WFRRFILASR LKSELRKPAG
     VSGSKSGLLP AHSRHSSPSG HLSHSRSSSK GSVEEMMSQP KQKELVGSVR QKMLLDYSVY
     MGRCVPQDNR SPHRSPVQSA ESSPTASKKL PEAPPSEEEE QEAWVNALLG RIFWDFLGEK
     YWSDVVSKKI QMKLSKIKLP YFMNELTLTE LDMGVAVPKI LQAFKPYVDH QGLWIDLEMS
     YNGSFLMTLE TKMNLTKLGK EPLVEALKVG EIGKEGCRPR AYCLADSDEE SSSAGSSEED
     DPPEPTAGDK QPLPGAEGYV GGHRTSKIMR FVDKITKSKY FQKATETEFI KKKIEEVSNT
     PLLLTVEVQE CRGTLAVNIP PPPTDRIWYG FRKPPYVELK ARPKLGEREV TLVHVTEWIE
     KKLEQELQKV FVMPNMDDVY IPIMHSAMDP RSTSCLLKEP PVETSDQL
//
ID   UBE2O_MOUSE             Reviewed;        1288 AA.
AC   Q6ZPJ3; Q60800; Q6PCR9; Q7TPN2; Q8BLE8;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 O;
DE            EC=6.3.2.19;
DE   AltName: Full=Ubiquitin carrier protein O;
DE   AltName: Full=Ubiquitin-conjugating enzyme E2 of 230 kDa;
DE            Short=Ubiquitin-conjugating enzyme E2-230K;
DE   AltName: Full=Ubiquitin-protein ligase O;
GN   Name=Ube2o; Synonyms=Kiaa1734;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 103-628, TISSUE SPECIFICITY, AND
RP   INDUCTION.
RC   TISSUE=Reticulocyte;
RX   MEDLINE=95281580; PubMed=7761435; DOI=10.1073/pnas.92.11.4982;
RA   Wefes I., Mastrandrea L.D., Haldeman M., Koury S.T., Tamburlin J.,
RA   Pickart C.M., Finley D.;
RT   "Induction of ubiquitin-conjugating enzymes during terminal erythroid
RT   differentiation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:4982-4986(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 124-1288.
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 867-1288.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   ENZYME REGULATION.
RX   PubMed=8634298; DOI=10.1021/bi952105y;
RA   Berleth E.S., Pickart C.M.;
RT   "Mechanism of ubiquitin conjugating enzyme E2-230K: catalysis
RT   involving a thiol relay?";
RL   Biochemistry 35:1664-1671(1996).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-84; SER-833 AND
RP   SER-836, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-84 AND SER-893,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC       diphosphate + protein N-ubiquityllysine.
CC   -!- ENZYME REGULATION: Inhibited by inorganic arsenite such as
CC       phenylarsenoxides.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- TISSUE SPECIFICITY: Highly expressed in reticulocytes.
CC   -!- INDUCTION: By EPO/Erythropoietin which induces erythroid
CC       differentiation.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA69916.1; Type=Frameshift; Positions=344, 367, 374, 411;
CC       Sequence=AAH59193.1; Type=Erroneous initiation;
CC       Sequence=BAC32345.1; Type=Erroneous initiation;
CC       Sequence=BAC98241.1; Type=Erroneous initiation;
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DR   EMBL; AK129431; BAC98241.1; ALT_INIT; mRNA.
DR   EMBL; U20780; AAA69916.1; ALT_FRAME; mRNA.
DR   EMBL; BC059193; AAH59193.1; ALT_INIT; mRNA.
DR   EMBL; AK045398; BAC32345.1; ALT_INIT; mRNA.
DR   IPI; IPI00453803; -.
DR   PIR; I49264; I49264.
DR   RefSeq; NP_776116.2; NM_173755.3.
DR   UniGene; Mm.243950; -.
DR   HSSP; Q16763; 1ZDN.
DR   ProteinModelPortal; Q6ZPJ3; -.
DR   SMR; Q6ZPJ3; 932-1147.
DR   MINT; MINT-7034165; -.
DR   STRING; Q6ZPJ3; -.
DR   PhosphoSite; Q6ZPJ3; -.
DR   PRIDE; Q6ZPJ3; -.
DR   Ensembl; ENSMUST00000082152; ENSMUSP00000080791; ENSMUSG00000020802.
DR   GeneID; 217342; -.
DR   KEGG; mmu:217342; -.
DR   UCSC; uc007mln.1; mouse.
DR   CTD; 217342; -.
DR   MGI; MGI:2444266; Ube2o.
DR   GeneTree; ENSGT00590000082815; -.
DR   HOGENOM; HBG716545; -.
DR   HOVERGEN; HBG080116; -.
DR   InParanoid; Q6ZPJ3; -.
DR   OrthoDB; EOG45DWP7; -.
DR   BRENDA; 6.3.2.19; 244.
DR   NextBio; 375789; -.
DR   ArrayExpress; Q6ZPJ3; -.
DR   Bgee; Q6ZPJ3; -.
DR   CleanEx; MM_UBE2O; -.
DR   Genevestigator; Q6ZPJ3; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:EC.
DR   GO; GO:0043687; P:post-translational protein modification; IEA:InterPro.
DR   GO; GO:0051246; P:regulation of protein metabolic process; IEA:InterPro.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Gene3D; G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SUPFAM; SSF54495; UBQ-conjugat/RWD-like; 1.
DR   PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; FALSE_NEG.
DR   PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Coiled coil; Ligase; Nucleotide-binding; Phosphoprotein;
KW   Ubl conjugation pathway.
FT   CHAIN         1   1288       Ubiquitin-conjugating enzyme E2 O.
FT                                /FTId=PRO_0000280638.
FT   COILED      809    879       Potential.
FT   COMPBIAS      2     38       Ala-rich.
FT   ACT_SITE   1037   1037       Glycyl thioester intermediate (By
FT                                similarity).
FT   MOD_RES      82     82       Phosphoserine.
FT   MOD_RES      84     84       Phosphoserine.
FT   MOD_RES     394    394       Phosphoserine (By similarity).
FT   MOD_RES     436    436       Phosphoserine (By similarity).
FT   MOD_RES     833    833       Phosphoserine.
FT   MOD_RES     835    835       Phosphothreonine (By similarity).
FT   MOD_RES     836    836       Phosphoserine.
FT   MOD_RES     838    838       Phosphothreonine (By similarity).
FT   MOD_RES     893    893       Phosphoserine.
FT   CONFLICT    309    309       C -> S (in Ref. 2; AAA69916).
FT   CONFLICT    317    319       SPP -> CPR (in Ref. 2; AAA69916).
FT   CONFLICT    343    343       Q -> H (in Ref. 2; AAA69916).
FT   CONFLICT   1160   1160       P -> L (in Ref. 4; BAC32345).
SQ   SEQUENCE   1288 AA;  140818 MW;  D990F5B36A686CA1 CRC64;
     MADPAAPAPA QAQAAAAPTP AAAPAAAAPP PAPATDSASG PSSDSGPEAG SQRLLFSHDL
     VSGRYRGSVH FGLVRLIHGE DSDSEGDDDG RGSSGCSEAG GAGHEEGRAS PLRRGYVRVQ
     WYPEGVKQHV KETKLKLEDR SVVPRDVVRH MRSTDSQCGT VIDVNIDCAV KLIGTNCIIY
     PVNSKDLQHI WPFMYGDYIA YDCWLGKVYD LKNQIILKLS NGARCSMNTE DGAKLYDVCP
     HVSDSGLFFD DSYGFYPGQV LIGPAKIFSS VQWLSGVKPV LSTKSKFRVV VEEVQVVELK
     VTWITKSFCP GGTDSVSPPP SIITQENLGR VKRLGCFDHA QRQLGERCLY VFPAKVEPAK
     IAWECPEKNC AQGEGSMAKK VKRLLKKQVV RIMSCTPDTQ CPRDHSMEDP DKKGEARAGS
     EIGSASPEEQ PDGSASPVEM QDEGSEELQE TCEPLPPFLL KEGGDDGLHS AEQDADDEAA
     DDTDDTSSVT SSASSTTSSQ SGSGTGRKKS IPLSIKNLKR KHKRKKNKVT RDFKPGDRVA
     VEVVTTMTSA DVMWQDGSVE CNIRSNDLFP VHHLDNNEFC PGDFVVDKRV QSCPDPAVYG
     VVQSGDHVGR TCMVKWFKLR PSGDDVELIG EEEDVSVYDI ADHPDFRFRT TDIVIRIGNT
     EDGALPKEDE PSVGQVARVD VSSKVEVVWA DNSKTIILPQ HLYNIESEIE ESDYDSVEGS
     SSGASSDEWE DDSDSWETDN GLVDDEHPKI EELAAILPAE QPTAPEEDKG VVISEEAATA
     AIQGAVAMAA PVAGLMEKAG KDGPPKSFRE LKEAIKILES LKNMTVEQLL TGSPTSPTVE
     PEKPTREKKF LDDIKKLQEN LKKTLDNVAI AEEEKMEAVP DTERKEEKPE VQSPVKAEWP
     SETPVLCQQC GGRPGVTFTS AKGEVFSVLE FAPSNHSFKK IEFQPPEAKK FFSTVRKEMA
     LLATSLPDGI MVKTFEDRMD LFSALIKGPT RTPYEDGLYL FDIQLPNIYP AVPPHFCYLS
     QCSGRLNPNL YDNGKVCVSL LGTWIGKGTE RWTSKSSLLQ VLISIQGLIL VNEPYYNEAG
     FDSDRGLQEG YENSRCYNEM ALIRVVQSMT QLVRRPPEVF EQEIRQHFSV GGWRLVNRIE
     SWLETHAMQE RAQVMPNGAP KDSSSLEPMA AAELSDSGRE EPEDVGMAPG EASQGSDSEG
     GAQGPASASR DHTEQTETAP DASAPPSVRP KRRRKSYRSF LPEKSGYPDI GFPLFPLSKG
     FIKSIRGVLT QFRAALLEAG MPESTEDK
//
ID   Q6ZPK1_MOUSE            Unreviewed;      1205 AA.
AC   Q6ZPK1;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   SubName: Full=MKIAA1686 protein;
DE   Flags: Fragment;
GN   Name=Plekha5; Synonyms=mKIAA1686;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SIMILARITY: Contains 1 PH domain.
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DR   EMBL; AK129423; BAC98233.1; -; mRNA.
DR   IPI; IPI00229810; -.
DR   RefSeq; NP_659169.3; NM_144920.3.
DR   UniGene; Mm.247670; -.
DR   ProteinModelPortal; Q6ZPK1; -.
DR   STRING; Q6ZPK1; -.
DR   Ensembl; ENSMUST00000087622; ENSMUSP00000084904; ENSMUSG00000030231.
DR   GeneID; 109135; -.
DR   KEGG; mmu:109135; -.
DR   UCSC; uc009eob.1; mouse.
DR   CTD; 109135; -.
DR   MGI; MGI:1923802; Plekha5.
DR   eggNOG; roNOG12712; -.
DR   GeneTree; ENSGT00530000063012; -.
DR   HOGENOM; HBG713535; -.
DR   HOVERGEN; HBG053615; -.
DR   InParanoid; Q6ZPK1; -.
DR   OrthoDB; EOG4B8JCC; -.
DR   NextBio; 361680; -.
DR   ArrayExpress; Q6ZPK1; -.
DR   Bgee; Q6ZPK1; -.
DR   Genevestigator; Q6ZPK1; -.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
FT   NON_TER       1      1
SQ   SEQUENCE   1205 AA;  137122 MW;  7A06CE75F0D11791 CRC64;
     EAYTFEGARY YINHNERKVT CKHPVTGQPS QDNCIFVVND QTVATMTSED KKERPISMIN
     EASNYNMASD YAVHPMSPVG RTSRASKKVH NFGKRSNSIK RNPNAPVVRR GWLYKQDSTG
     MKLWKKRWFV LSDLCLFYYR DEKEEGILGS ILLPSFQIAM LTAEDHINRK YAFKAAHPNM
     RTYYFCTDTG KEMELWMKAM LDAALVQTEP VKRITFNFRV DKITTDSAST KETNNIPNHR
     VLIRPEVQNH QKNKEISKIE EKRALEAERY GFQKDGQDRP LTKINSVKLN SLLSEYESGP
     DCPPQNVHYR PINVNSSDGK AVNVSLADVR GGSHPNAGPL ATEADRVIQR TNSMQQLEQW
     IKVQKGRGLE EEPRGVISYQ TLPRNMPSHR AQILARCPEG YRTLPRNSKT RPESICSVTS
     SGHEKTGPGA EEKRRSMRDD TMWQLYEWQQ RQFYHKQSTL PRHGCLSSPK AMVQVSDQTM
     HSIPTSPSHG SAAAYQGFSP QRTYRSEVTS PIQRGDVTID RRHRPHHPKH VYVADRRSMP
     AGLTLQAVSP QSLQGRTPEE LTLLLIKLRR QQAELSSVRE HTLAQLMQLK LEAHSPKNEI
     LSHHLQRNTI YLDHQMKENE PIITMVHTMI ENSALRPQLY QQFLRQKNKI SLYCLSQDEC
     RGTLYKYRPE EAGIDAKLSR LCEQDKVVRA LEEKLQQLHK EKYTLEQALL SASQEIEMNA
     DNPAAIQTVV LQRDDLQNGL LSTCRELSRA TAELERAWRE YDKLEYDVTV TRDQMQGQLD
     RLGEVQSESA GIQRAQIQKE LWRIQDVMEG LSKHKQQRGS SETGLAGSKP FSSVKYKSEE
     EEVVPPRPPL PRSYDFTEQP PIIPPLPSDS SSLLCYSRGP VHLPEDKKIH QVQGYPRNGS
     HCGPDYRLYK SEPELTTVAE VDESNGEEKS EPVSETEAPV VKGSHFPVGV PLRTKSPTPE
     SSTIASYVTL RKTKKMVELR TERPRSAVEQ LCLAESARPR MTVEEQLERI RRHQQACLRE
     KKKGLSVLGA SDPSDVRDSP LRLTQTLRRD DNVKELDTVH RENDVKPDYE TPAAQCAHLE
     DAEPQNADIG RKLKRSEMLY TPEPNGMASE EVTEKERQKE QVHADGSCSP QEETAMTEHQ
     MEGPPEEAES LHEEEETLAS CEPAPEIPRE NQTTVRSLSP SPDSSTAADP PTPPQLREGS
     HFMCV
//
ID   LST2_MOUSE              Reviewed;         905 AA.
AC   Q6ZPK7; B2RSX8;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Lateral signaling target protein 2 homolog;
DE   AltName: Full=Zinc finger FYVE domain-containing protein 28;
GN   Name=Zfyve28; Synonyms=Kiaa1643, Lst2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=19460345; DOI=10.1016/j.devcel.2009.03.015;
RA   Mosesson Y., Chetrit D., Schley L., Berghoff J., Ziv T., Carvalho S.,
RA   Milanezi F., Admon A., Schmitt F., Ehrlich M., Yarden Y.;
RT   "Monoubiquitinylation regulates endosomal localization of Lst2, a
RT   negative regulator of EGF receptor signaling.";
RL   Dev. Cell 16:687-698(2009).
CC   -!- FUNCTION: Negative regulator of epidermal growth factor receptor
CC       (EGFR) signaling. Acts by promoting EGFR degradation in endosomes
CC       when not monoubiquitinated (By similarity).
CC   -!- SUBUNIT: Interacts with TRIM3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Early endosome membrane.
CC       Note=Localizes to early endosome membrane in absence of Lys-87
CC       monoubiquitination. Localizes to cytosol when monoubiquitinated
CC       (By similarity).
CC   -!- TISSUE SPECIFICITY: Enriched in brain (at protein level).
CC   -!- DOMAIN: The FYVE-type zinc finger mediates the interaction with
CC       phosphatidylinositol 3-phosphate (PI3P) and localization to early
CC       endosome membranes when not monoubiquitinated at Lys-87 (By
CC       similarity).
CC   -!- PTM: Monoubiquitination at Lys-87 prevents binding to
CC       phosphatidylinositol 3-phosphate (PI3P) and localization to early
CC       endosome membranes (By similarity).
CC   -!- SIMILARITY: Belongs to the lst-2 family.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98224.1; Type=Erroneous initiation;
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DR   EMBL; AK129414; BAC98224.1; ALT_INIT; mRNA.
DR   EMBL; BC139050; AAI39051.1; -; mRNA.
DR   EMBL; BC139051; AAI39052.1; -; mRNA.
DR   IPI; IPI00757775; -.
DR   RefSeq; NP_001015039.1; NM_001015039.1.
DR   UniGene; Mm.113388; -.
DR   HSSP; Q960X8; 1DVP.
DR   ProteinModelPortal; Q6ZPK7; -.
DR   SMR; Q6ZPK7; 831-892.
DR   PRIDE; Q6ZPK7; -.
DR   Ensembl; ENSMUST00000094868; ENSMUSP00000092464; ENSMUSG00000037224.
DR   GeneID; 231125; -.
DR   KEGG; mmu:231125; -.
DR   UCSC; uc008xca.1; mouse.
DR   CTD; 231125; -.
DR   MGI; MGI:2684992; Zfyve28.
DR   eggNOG; roNOG07326; -.
DR   HOGENOM; HBG444671; -.
DR   InParanoid; Q6ZPK7; -.
DR   PhylomeDB; Q6ZPK7; -.
DR   NextBio; 380413; -.
DR   ArrayExpress; Q6ZPK7; -.
DR   Bgee; Q6ZPK7; -.
DR   Genevestigator; Q6ZPK7; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007175; P:negative regulation of epidermal growth factor receptor activity; ISS:UniProtKB.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Endosome; Isopeptide bond; Membrane; Metal-binding;
KW   Phosphoprotein; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1    905       Lateral signaling target protein 2
FT                                homolog.
FT                                /FTId=PRO_0000378953.
FT   ZN_FING     835    895       FYVE-type.
FT   MOD_RES     888    888       Phosphothreonine; by MAP2K (By
FT                                similarity).
FT   CROSSLNK     87     87       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
SQ   SEQUENCE   905 AA;  99787 MW;  E713EAB3E4DB0FEB CRC64;
     MMNRFRKWLY KPKRSDPQLL AQFYYADEEL NQVAAELDSL DGRKEPQRCT LLVSQFRSCQ
     DNVLNIINQI MEECIPQDRA PRDFCVKFPE EIRHDNLAGQ LWFGAECLAA GSIIMNRELE
     SMAMRPLAKE LTRSLEDVRG TLRDQALRDL NTYTEKMREA LRRFDVLFAE FELSYVSAMV
     PVKSPREYYV QQEVIVLFCE TVERALDFGY LTQDMIDDYE PALMFTIPRL AIVCGLVVYA
     DGPLNLDRKV EDMSELFRPF HTLLRKIRDL LQALTEEELH TLERSLCVSQ DVELPIRADT
     QAPSALAPTF SASLPPEETL SASANNPEAE LACSMQYDDQ ELEELSRMVH RAGDEMSSLL
     SPPSACQSPA HRPGSEASPR GEASPARARL KSGSDEEERV FFMDDVEVTE SPARPESPGN
     TFELTQGNAQ QRGQDGQSGE VGVEAPALVK EEDWSNNNVE GDKIKLASLM GSTSCSCLDS
     QLYLDGWEVS AEDAETAEMI AHRTGGMKLS ATVIFNPKSP TSQDSAVAAQ EAPGHGTSPL
     EPRAEGTGDN SHKLSTTATN CLLHSCVCCG SCGDSRDDAV ERLREKCGPG SVISASNPSV
     SLAKGGDKEP ERIDEAQPSD VTLPAEDASN RQEPKAPASS KCLAHTSGPQ VDTASRLQGE
     GEVKGQPEPE ARKQDPEKSP VVSGDSPRGD VAQTEHQHLL GSSSTVGSCS LDNTRLDVAT
     AAMPVTPMAT REKIRSRFHG SHDLIHRLFV CISGVADQLQ TNYASDLRSI LKTLFEVMAT
     KPETDDKEKL KKVTQTLRSA ALEDCALCQE TVSSSELAAK TRDGDFEDPP EWVPDEACGF
     CTSCKAPFTV IRRKHHCRSC GKIFCSRCSS HSAPLPRYGQ VKPVRVCTHC YMFHVTPFYS
     DKTGM
//
ID   PITM2_MOUSE             Reviewed;        1335 AA.
AC   Q6ZPQ6; Q9R1P5;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Membrane-associated phosphatidylinositol transfer protein 2;
DE   AltName: Full=Drosophila retinal degeneration B homolog 2;
DE            Short=RdgB2;
DE   AltName: Full=Phosphatidylinositol transfer protein, membrane-associated 2;
DE            Short=PITPnm 2;
DE   AltName: Full=Pyk2 N-terminal domain-interacting receptor 3;
DE            Short=NIR-3;
GN   Name=Pitpnm2; Synonyms=Kiaa1457, Nir3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Retina;
RX   MEDLINE=99389861; PubMed=10460238;
RA   Lu C., Vihtelic T.S., Hyde D.R., Li T.;
RT   "A neuronal-specific mammalian homolog of the Drosophila retinal
RT   degeneration B gene with expression restricted to the retina and
RT   dentate gyrus.";
RL   J. Neurosci. 19:7317-7325(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1263, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Catalyzes the transfer of phosphatidylinositol and
CC       phosphatidylcholine between membranes (in vitro). Binds calcium
CC       ions (By similarity).
CC   -!- SUBUNIT: Interacts with PTK2B via its C-terminus (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane
CC       protein (Probable). Cytoplasm, cytoskeleton (Probable). Note=May
CC       associate with the cytoskeleton.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6ZPQ6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZPQ6-2; Sequence=VSP_017964;
CC   -!- TISSUE SPECIFICITY: Detected in retina and in the dentate gyrus of
CC       the cerebellum.
CC   -!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI
CC       transfer class IIA subfamily.
CC   -!- SIMILARITY: Contains 1 DDHD domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98174.1; Type=Erroneous initiation;
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DR   EMBL; AF058693; AAD51375.1; -; mRNA.
DR   EMBL; AK129364; BAC98174.1; ALT_INIT; mRNA.
DR   IPI; IPI00128947; -.
DR   IPI; IPI00754562; -.
DR   RefSeq; NP_035386.1; NM_011256.2.
DR   UniGene; Mm.44261; -.
DR   ProteinModelPortal; Q6ZPQ6; -.
DR   PhosphoSite; Q6ZPQ6; -.
DR   PRIDE; Q6ZPQ6; -.
DR   Ensembl; ENSMUST00000031353; ENSMUSP00000031353; ENSMUSG00000029406.
DR   Ensembl; ENSMUST00000086123; ENSMUSP00000083292; ENSMUSG00000029406.
DR   GeneID; 19679; -.
DR   KEGG; mmu:19679; -.
DR   UCSC; uc008zpb.1; mouse.
DR   UCSC; uc008zpc.1; mouse.
DR   CTD; 19679; -.
DR   MGI; MGI:1336192; Pitpnm2.
DR   GeneTree; ENSGT00550000074351; -.
DR   HOGENOM; HBG444305; -.
DR   HOVERGEN; HBG052733; -.
DR   InParanoid; Q6ZPQ6; -.
DR   OMA; TKDVAVY; -.
DR   OrthoDB; EOG479F68; -.
DR   PhylomeDB; Q6ZPQ6; -.
DR   NextBio; 297000; -.
DR   ArrayExpress; Q6ZPQ6; -.
DR   Bgee; Q6ZPQ6; -.
DR   Genevestigator; Q6ZPQ6; -.
DR   GermOnline; ENSMUSG00000029406; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005625; C:soluble fraction; IDA:MGI.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:InterPro.
DR   InterPro; IPR004177; DDHD.
DR   InterPro; IPR023214; HAD-like_dom.
DR   InterPro; IPR013209; LNS2.
DR   InterPro; IPR001666; PI_transfer.
DR   Gene3D; G3DSA:3.40.50.1000; HAD-like_dom; 1.
DR   PANTHER; PTHR10658; PI_transfer; 1.
DR   Pfam; PF02862; DDHD; 1.
DR   Pfam; PF02121; IP_trans; 1.
DR   Pfam; PF08235; LNS2; 1.
DR   PRINTS; PR00391; PITRANSFER.
DR   SMART; SM00775; LNS2; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   PROSITE; PS51043; DDHD; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cytoplasm; Cytoskeleton; Lipid-binding;
KW   Membrane; Metal-binding; Phosphoprotein.
FT   CHAIN         1   1335       Membrane-associated phosphatidylinositol
FT                                transfer protein 2.
FT                                /FTId=PRO_0000232742.
FT   DOMAIN      701    949       DDHD.
FT   COMPBIAS    576    689       Ser-rich.
FT   MOD_RES    1263   1263       Phosphoserine.
FT   VAR_SEQ     843    897       KGPSSLNHTPSIRRLSLLALPPPSPTTQGPRARARQVSPNL
FT                                ERAPCLPDLDIGEV -> I (in isoform 2).
FT                                /FTId=VSP_017964.
SQ   SEQUENCE   1335 AA;  148035 MW;  6119814AF6D15CBC CRC64;
     MIIKEYRIPL PMTVDEYRIA QLYMIQKKSR NETHGQGSGV EILENRPYTD GPGGSGQYTH
     KVYHVGMHIP GWFRSILPKA ALRVVEESWN AYPYTRTRFT CPFVEKFSID IETFYKTDTG
     ENNNVFNLSP VEKSQLITDI IDIVKDPVPP SEYKTEEDPK LFQSVKTCRG PLSENWIQEY
     KKRLLPIMCA YKLCKVEFRY WGMQSKIERF IHDTGLRRVM VRAHRQAWCW QDEWYGLTME
     KIRELEREVQ LMLSRKMAQF SEEGPSELSK DSATKDQASG TTSDPGSKNG EPLGRGLKKQ
     WSTSSKSSRS SKRGASPSRH SISEWRMQSI ARDSDEGSEE EFFDAHENLY CTEEKQAKDM
     TKWNSNDLMD KMESPEPEES QDEIYQQSGS EFRVASSVEQ LNIIEDEVSQ PLAAPPSKIH
     VLLLVLHGGT ILDTGAGDPS SKQGDTNTIT NVFDTVMRVH YPSALGHLAI RLVPCPPICA
     DAFALVSNLS PYGHDEGCLS SSQDHIPLAA LPLLATSSPQ YQEAVATVIQ RANLAYGDFI
     KSQEGVTFNG QVCLIGDCVG GILAFDALCY SGQPVSESQS SSRRGSVVSM QDADLLSPGT
     LANAAHCSGG SGGGGSGGSS LESSRHLSRS NIDIPRSNGT EDSRRQLPRK RSDSSTYELD
     TIQQHQAFLS SLHASVLRNE PSSRRSSSST MLDGAGALGK FDFEIADLFL FGCPLGLVLA
     LRKTVIPSLD VFQLRPACQQ VYNLFHPADP SASRLEPLLE RRFHSLPPFS IPRYQRYPLG
     DGCSTLLADV LQTHNTVFQE HAAPSSPGTA PAGRGFRRAS EISIASQVSG MAESYTASSI
     AQKGPSSLNH TPSIRRLSLL ALPPPSPTTQ GPRARARQVS PNLERAPCLP DLDIGEVAAK
     WWGQKRIDYA LYCPDALTAF PTVALPHLFH ASYWESTDVV SFLLRQVMRH DSSSILELDG
     KEVSVFTPSQ PRERWQRKRT HVKLRNVAAN HRINDAVANE DGPQVVTGRF MYGPLDMVTL
     TGEKVDVHIM TQPPSGEWLH LDTLVTNSSG RVSYTIPETH RLGVGVYPIK MVVRGDHTFA
     DSYITVLPRG TEFVVFSIDG SFAASVSIMG SDPKVRAGAV DVVRHWQDLG YLIIYVTGRP
     DMQKQRVVAW LAQHNFPHGV VSFCDGLVHD PLRHKANFLK LLISELHLRA HAAYGSTKDV
     AVYNSISLSP MHIYIVGRPT KKLQQQCQFI TDGYAAHLAQ LKYNHRARPA RNTATRMALR
     KGSFGLPGQS DFLRSRNHLL RTISAQPSGP SHRHDRTQTQ MDSEQRGQRS MSVAASCWGR
     AMAGRLEPGA ATGPK
//
ID   K1430_MOUSE             Reviewed;         541 AA.
AC   Q6ZPR1; Q9D462;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   08-MAR-2011, entry version 31.
DE   RecName: Full=UPF0501 protein KIAA1430;
GN   Name=Kiaa1430;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160 AND SER-161, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SIMILARITY: Belongs to the UPF0501 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98168.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK129358; BAC98168.1; ALT_INIT; mRNA.
DR   EMBL; AK016776; BAB30422.1; -; mRNA.
DR   EMBL; BC058092; AAH58092.1; -; mRNA.
DR   IPI; IPI00857828; -.
DR   RefSeq; NP_080023.1; NM_025747.3.
DR   UniGene; Mm.133623; -.
DR   ProteinModelPortal; Q6ZPR1; -.
DR   PhosphoSite; Q6ZPR1; -.
DR   PRIDE; Q6ZPR1; -.
DR   Ensembl; ENSMUST00000034048; ENSMUSP00000034048; ENSMUSG00000031631.
DR   GeneID; 66756; -.
DR   KEGG; mmu:66756; -.
DR   MGI; MGI:1914006; 4933411K20Rik.
DR   HOVERGEN; HBG057516; -.
DR   OrthoDB; EOG44MXS1; -.
DR   NextBio; 322558; -.
DR   ArrayExpress; Q6ZPR1; -.
DR   Bgee; Q6ZPR1; -.
DR   CleanEx; MM_4933411K20RIK; -.
DR   Genevestigator; Q6ZPR1; -.
PE   1: Evidence at protein level;
KW   Coiled coil; Phosphoprotein.
FT   CHAIN         1    541       UPF0501 protein KIAA1430.
FT                                /FTId=PRO_0000309225.
FT   COILED      382    459       Potential.
FT   COMPBIAS    170    247       Ser-rich.
FT   MOD_RES     155    155       Phosphothreonine (By similarity).
FT   MOD_RES     160    160       Phosphoserine.
FT   MOD_RES     161    161       Phosphoserine.
SQ   SEQUENCE   541 AA;  60837 MW;  EEC54FB097C957EA CRC64;
     MDRFGDISEG EVDHSFFDSD FEDAKKCESN SIFDKQNDDD LKEGINKDTK NVNLKFGVQN
     DHLKEKIDNN TENVNLKLGL QTTENYLTQK GNERKANFSS KEQHIENDPT QARSSSVLTS
     SRSKKSCDAT KGHKLNLPVP DRIPKIVKGE DDYYTDGEES SDDGKKYVRS KSAKPSSNLK
     KNVSKKYSSS SLSSSSSRSN SDCSDMGSDR QRRSESHSSG KCVSSVTPSS PKQRCKSGRK
     SSAQPSSTKQ KTGDYHESEG NVPDITPLST PDVSPAQSLE LGQPPDQKVK VKKQENVSRD
     VYEDAEALKN DSRCVKSAKR KEKHGQSFAP KSSVLDANLD RRSKQKVLHD TMDLNHLLKA
     FLQLDKKGPQ KHHFEQPAII PRKNYSFTRE EVRQIDRENQ RLLKELSRQA EKPGSKSTIP
     GRSIGHPPKL YHSALNRQRE QQRIERENMA LLKRLEAVKP TVGMKRSEQL MDYHRNMSYL
     NPSPSVRRVR STLGHYSPLR GASRTSSATS GLSCKTDRSV LDTSNGFLLR PKPPNVRTAW
     L
//
ID   KCNT1_MOUSE             Reviewed;        1224 AA.
AC   Q6ZPR4; B2RUK3; Q8C3E7;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   11-JAN-2011, entry version 61.
DE   RecName: Full=Potassium channel subfamily T member 1;
GN   Name=Kcnt1; Synonyms=Kiaa1422;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-297.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 160-1224.
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
CC   -!- FUNCTION: Outwardly rectifying potassium channel subunit that may
CC       co-assemble with other Slo-type channel subunits. Activated by
CC       high intracellular sodium or chloride levels. Activated upon
CC       stimulation of G-protein coupled receptors, such as CHRM1 and
CC       GRIA1. May be regulated by calcium in the absence of sodium ions
CC       (in vitro) (By similarity).
CC   -!- SUBUNIT: Interacts with CRBN via its cytoplasmic C-terminus (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- PTM: Phosphorylated by protein kinase C. Phosphorylation of the C-
CC       terminal domain increases channel activity (By similarity).
CC   -!- SIMILARITY: Belongs to the potassium channel family. Calcium-
CC       activated (TC 1.A.1.3) subfamily. KCa4.1/KCNT1 sub-subfamily.
CC   -!- SIMILARITY: Contains 1 RCK N-terminal domain.
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DR   EMBL; BC141190; AAI41191.1; -; mRNA.
DR   EMBL; BC171963; AAI71963.1; -; mRNA.
DR   EMBL; AK086119; BAC39614.1; -; mRNA.
DR   EMBL; AK129355; BAC98165.1; -; mRNA.
DR   IPI; IPI00409177; -.
DR   RefSeq; NP_780671.2; NM_175462.3.
DR   UniGene; Mm.119462; -.
DR   ProteinModelPortal; Q6ZPR4; -.
DR   SMR; Q6ZPR4; 267-318.
DR   STRING; Q6ZPR4; -.
DR   PRIDE; Q6ZPR4; -.
DR   Ensembl; ENSMUST00000038506; ENSMUSP00000046284; ENSMUSG00000058740.
DR   GeneID; 227632; -.
DR   KEGG; mmu:227632; -.
DR   UCSC; uc008itp.1; mouse.
DR   CTD; 227632; -.
DR   MGI; MGI:1924627; Kcnt1.
DR   HOVERGEN; HBG055190; -.
DR   PhylomeDB; Q6ZPR4; -.
DR   NextBio; 378702; -.
DR   ArrayExpress; Q6ZPR4; -.
DR   Bgee; Q6ZPR4; -.
DR   CleanEx; MM_KCNT1; -.
DR   Genevestigator; Q6ZPR4; -.
DR   GermOnline; ENSMUSG00000058740; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0015269; F:calcium-activated potassium channel activity; IEA:InterPro.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   InterPro; IPR013099; Ion_trans_2.
DR   InterPro; IPR003929; K_chnl_Ca-activ_BK_asu.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF03493; BK_channel_a; 1.
DR   Pfam; PF07885; Ion_trans_2; 1.
DR   PROSITE; PS51201; RCK_N; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Calcium; Cell membrane; Glycoprotein; Ion transport; Ionic channel;
KW   Membrane; Phosphoprotein; Potassium; Potassium channel;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1   1224       Potassium channel subfamily T member 1.
FT                                /FTId=PRO_0000054091.
FT   TOPO_DOM      1     83       Cytoplasmic (Potential).
FT   TRANSMEM     84    104       Helical; Name=Segment S1; (Potential).
FT   TOPO_DOM    105    141       Extracellular (Potential).
FT   TRANSMEM    142    162       Helical; Name=Segment S2; (Potential).
FT   TOPO_DOM    163    173       Cytoplasmic (Potential).
FT   TRANSMEM    174    194       Helical; Name=Segment S3; (Potential).
FT   TOPO_DOM    195    199       Extracellular (Potential).
FT   TRANSMEM    200    212       Helical; Name=Segment S4; (Potential).
FT   TOPO_DOM    213    237       Cytoplasmic (Potential).
FT   TRANSMEM    238    258       Helical; Name=Segment S5; (Potential).
FT   TOPO_DOM    259    267       Extracellular (Potential).
FT   INTRAMEM    268    288       Pore-forming; (Potential).
FT   TOPO_DOM    289    290       Extracellular (Potential).
FT   TRANSMEM    291    311       Helical; Name=Segment S6; (Potential).
FT   TOPO_DOM    312   1224       Cytoplasmic (Potential).
FT   DOMAIN      461    582       RCK N-terminal.
FT   CARBOHYD    119    119       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    123    123       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   1224 AA;  138106 MW;  7F343893D70E506B CRC64;
     MARAKLPRSP SEGKAGPGDT PAGAAAPEEP HGLSPLLPAR GGGSVGSDVG QRVQVEFYVN
     ENTFKERLKL FFIKNQRSSL RIRLFNFSLK LLTCLLYIVR VLLDNPDQGI GCWGCTKYNY
     TFNGSSSEFH WAPILWVERK MALWVIQVIV ATISFLETML IIYLSYKGNI WEQIFHVSFV
     LEMINTLPFI ITVFWPPLRN LFIPVFLNCW LAKHALENMI NDFHRAILRT QSAMFNQVLI
     LFCTLLCLVF TGTCGIQHLE RAGGNLNLLT SFYFCIVTFS TVGFGDVTPK IWPSQLLVVI
     LICVTLVVLP LQFEELVYLW MERQKSGGNY SRHRARTEKH VVLCVSSLKI DLLMDFLNEF
     YAHPRLQDYY VVILCPSEMD VQVRRVLQIP LWSQRVIYLQ GSALKDQDLM RAKMDNGEAC
     FILSSRNEVD RTAADHQTIL RAWAVKDFAP NCPLYVQILK PENKFHVKFA DHVVCEEECK
     YAMLALNCIC PATSTLITLL VHTSRGQEGQ ESPEQWQRTY GRCSGNEVYH IRMGDSKFFR
     EYEGKSFTYA AFHAHKKYGV CLIGLKREEN KSILLNPGPR HILAASDTCF YINITKEENS
     AFIFKQEEKQ KRRGLAGQAL YEGPSRLPVH SIIASMGTVA MDLQNTDCRP SQGGSGGDGT
     KLTLPTENGS GSRRPSIAPV LELADSSALL PCDLLSDQSE DEVTPSDDEG LSVVEYVKGY
     PPNSPYIGSS PTLCHLLPVK APFCCLRLDK GCKHNSYEDA KAYGFKNKLI IVSAETAGNG
     LYNFIVPLRA YYRSRRELNP IVLLLDNKPD HHFLEAICCF PMVYYMEGSV DNLDSLLQCG
     IIYADNLVVV DKESTMSAEE DYMADAKTIV NVQTMFRLFP SLSITTELTH PSNMRFMQFR
     AKDSYSLALS KLEKQERENG SNLAFMFRLP FAAGRVFSIS MLDTLLYQSF VKDYMITITR
     LLLGLDTTPG SGYLCAMKVT EDDLWIRTYG RLFQKLCSSS AEIPIGIYRT ECHVFSEPHD
     VRAQSQISVN MEDCEDTREA KGPWGTRAAS GSGSTHGRHG GSADPVEHPL LRRKSLQWAR
     KLSRKSTKQA GKAPVATDWI TQQRLSLYRR SERQELSELV KNRMKHLGLP TTGYEDVANL
     TASDVMNRVN LGYLQDEMND HHQNTLSYVL INPPPDTRLE PNDIVYLIRS DPLAHVASSS
     QSRKSSCSNK LSSCNPETRD ETQL
//
ID   AKIB1_MOUSE             Reviewed;        1085 AA.
AC   Q6ZPS6; Q6AXE1;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Ankyrin repeat and IBR domain-containing protein 1;
GN   Name=Ankib1; Synonyms=Kiaa1386;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 568-1085.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-738, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-738, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Might act as an E3 ubiquitin-protein ligase, or as part
CC       of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-
CC       conjugating enzymes and then transfers it to substrates (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the RBR family.
CC   -!- SIMILARITY: Contains 2 ANK repeats.
CC   -!- SIMILARITY: Contains 1 IBR-type zinc finger.
CC   -!- SIMILARITY: Contains 2 RING-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 UIM (ubiquitin-interacting motif) repeat.
CC   -!- CAUTION: Lacks one Cys residue in the IBR-type zinc finger domain
CC       that is one of the conserved features of the family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH79620.1; Type=Erroneous termination; Positions=616; Note=Translated as Glu;
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DR   EMBL; AK129343; BAC98153.1; -; mRNA.
DR   EMBL; BC079620; AAH79620.1; ALT_SEQ; mRNA.
DR   IPI; IPI00467355; -.
DR   RefSeq; NP_001003909.2; NM_001003909.3.
DR   UniGene; Mm.130148; -.
DR   ProteinModelPortal; Q6ZPS6; -.
DR   SMR; Q6ZPS6; 5-202, 330-480, 512-571.
DR   PhosphoSite; Q6ZPS6; -.
DR   PRIDE; Q6ZPS6; -.
DR   Ensembl; ENSMUST00000043551; ENSMUSP00000040946; ENSMUSG00000040351.
DR   GeneID; 70797; -.
DR   KEGG; mmu:70797; -.
DR   UCSC; uc008who.1; mouse.
DR   CTD; 70797; -.
DR   MGI; MGI:1918047; Ankib1.
DR   eggNOG; roNOG14033; -.
DR   GeneTree; ENSGT00600000084159; -.
DR   HOVERGEN; HBG083226; -.
DR   InParanoid; Q6ZPS6; -.
DR   OrthoDB; EOG47D9FF; -.
DR   PhylomeDB; Q6ZPS6; -.
DR   NextBio; 332274; -.
DR   ArrayExpress; Q6ZPS6; -.
DR   Bgee; Q6ZPS6; -.
DR   CleanEx; MM_ANKIB1; -.
DR   Genevestigator; Q6ZPS6; -.
DR   GermOnline; ENSMUSG00000040351; Mus musculus.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR003903; Ubiquitin-int_motif.
DR   InterPro; IPR002867; Znf_C6HC.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF01485; IBR; 2.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00184; RING; 2.
DR   SMART; SM00726; UIM; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50330; UIM; 1.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Coiled coil; Metal-binding; Phosphoprotein; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1085       Ankyrin repeat and IBR domain-containing
FT                                protein 1.
FT                                /FTId=PRO_0000066893.
FT   REPEAT       45     75       ANK 1.
FT   REPEAT      145    174       ANK 2.
FT   REPEAT      846    865       UIM.
FT   ZN_FING     334    384       RING-type 1; atypical.
FT   ZN_FING     403    479       IBR-type 1; degenerate.
FT   ZN_FING     520    549       RING-type 2.
FT   COILED      576    641       Potential.
FT   MOD_RES     738    738       Phosphoserine.
SQ   SEQUENCE   1085 AA;  121876 MW;  EAB5F58A624F3972 CRC64;
     MGNTTTKFRK ALINGDENLA CQIYENNPQL KESLDPNISY GEPYQHNTPL HYAARHGMNR
     ILGTFLFGRD GNPNKRNVHN ETSMHLLCMG PQIMISEGTL HPRLARPVED DFRRADCLQM
     ILQWKGAKLD QGEYERAAID AVDNKKNTPL HYAAASGMKA CVELLVKHGG DLFAENENRD
     TPCDCAEKQQ HKDLALSLES QMVFSRDPEA EEIEAEYAAL DKREPYEGLR PQDLRRLKDM
     LIVETADMLQ APLFTAEALL RAHDWDREKL LEAWMSNPEN CCQRSGVQMP TPPPSGYNAW
     DTLPSPRTPR TTRSSVTSPD EISLSPGDLD TSLCDICMCS ISVFEDPVDM PCGHDFCRGC
     WEAFLNLKIQ EGEAHNIFCP AYECFQLVPV DVIESVVSKE MDKRYLQFDI KAFVENNPAI
     KWCPTAGCER AVRLTKQGSN PSGSDTLSFP LLRAPAVDCG KGHLFCWECL GEAHEPCDCQ
     TWKNWLQKIT EMKPEELVGV SEAYEDAANC LWLLTNSKPC ANCKSPIQKN EGCNHMQCAK
     CKYDFCWICL EEWKKHSSST GGYYRCTRYE VIQHVEEQSK EMTVEAEKKH KRFQELDRFM
     HYYTRYKNHE HSYQLEQRLL KTAKEKMEQL SRALKETEGG CPDTTFIEDA VHVLLKTRRI
     LKCSYPYGFF LEPKSTKKEI FELMQTDLEM VTEDLAQKVN RPYLRTPRHK IIRAACLVQQ
     KRQEFLASVA RGVAPADSPD APRRSFAGGT WDWEYLGFAS PEYRRRHRQQ RRRGDVHSLL
     SNPTDLDEPS ESTFDLPEGS SGRRPGASVV SSASMSVLHS SSLRDYSPAS RSANQDSLQA
     LSSLDEDDPN ILLAIQLSLQ ESGLDMDEET RDFLSNETSL GAIGSSLPSR LDSVPRSTES
     PRAALSSSEL LELGDSLMRL GADSDPFSTD TLSSRPLSET RSDFCPSSSD LDSAGQDPSA
     NDNLLGNIMA WFHDMNPQSI ALIPPAATTE ISAEPQLPCI RDGSEGVRDM ELVPPEDSVS
     KDTGVHEGER AQMEENPLEE NILAREELSQ AGDSSNEAVG RGDRPDAASQ TPQTSSDWLE
     QVHSV
//
ID   KLHL9_MOUSE             Reviewed;         617 AA.
AC   Q6ZPT1; Q505G5;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Kelch-like protein 9;
GN   Name=Klhl9; Synonyms=Kiaa1354;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC       ubiquitin-protein ligase complex required for mitotic progression
CC       and cytokinesis. The BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex
CC       mediates the ubiquitination of AURKB and controls the dynamic
CC       behavior of AURKB on mitotic chromosomes and thereby coordinates
CC       faithful mitotic progression and completion of cytokinesis (By
CC       similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Component of the BCR(KLHL9-KLHL13) E3 ubiquitin ligase
CC       complex, at least composed of CUL3, KLHL9, KLHL13 and RBX1.
CC       Interacts with AURKB (By similarity).
CC   -!- SIMILARITY: Contains 1 BACK (BTB/Kelch associated) domain.
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC   -!- SIMILARITY: Contains 6 Kelch repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98148.1; Type=Erroneous initiation;
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CC   -----------------------------------------------------------------------
DR   EMBL; AK129338; BAC98148.1; ALT_INIT; mRNA.
DR   EMBL; BC094556; AAH94556.1; -; mRNA.
DR   EMBL; AL928605; CAM14922.1; -; Genomic_DNA.
DR   IPI; IPI00420555; -.
DR   RefSeq; NP_766459.2; NM_172871.2.
DR   UniGene; Mm.260601; -.
DR   ProteinModelPortal; Q6ZPT1; -.
DR   SMR; Q6ZPT1; 23-281, 297-599.
DR   PhosphoSite; Q6ZPT1; -.
DR   PRIDE; Q6ZPT1; -.
DR   Ensembl; ENSMUST00000094993; ENSMUSP00000092602; ENSMUSG00000070923.
DR   GeneID; 242521; -.
DR   KEGG; mmu:242521; -.
DR   UCSC; uc008tnk.1; mouse.
DR   CTD; 242521; -.
DR   MGI; MGI:2180122; Klhl9.
DR   HOGENOM; HBG715942; -.
DR   HOVERGEN; HBG106526; -.
DR   InParanoid; Q6ZPT1; -.
DR   OMA; GEFVKLP; -.
DR   OrthoDB; EOG447FSR; -.
DR   NextBio; 385392; -.
DR   ArrayExpress; Q6ZPT1; -.
DR   Bgee; Q6ZPT1; -.
DR   CleanEx; MM_KLHL9; -.
DR   Genevestigator; Q6ZPT1; -.
DR   GermOnline; ENSMUSG00000036782; Mus musculus.
DR   GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0000910; P:cytokinesis; ISS:UniProtKB.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   InterPro; IPR011705; BACK.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR013069; BTB_POZ.
DR   InterPro; IPR015916; Gal_Oxidase_b-propeller.
DR   InterPro; IPR017096; Kelch-like_gigaxonin.
DR   InterPro; IPR006652; Kelch_1.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Gene3D; G3DSA:2.130.10.80; Gal_Oxidase_b-propeller; 1.
DR   Pfam; PF07707; BACK; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF01344; Kelch_1; 5.
DR   PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
DR   SMART; SM00875; BACK; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00612; Kelch; 6.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Kelch repeat; Mitosis; Phosphoprotein;
KW   Repeat; Ubl conjugation pathway.
FT   CHAIN         1    617       Kelch-like protein 9.
FT                                /FTId=PRO_0000119111.
FT   DOMAIN       50    119       BTB.
FT   DOMAIN      154    255       BACK.
FT   REPEAT      299    347       Kelch 1.
FT   REPEAT      348    399       Kelch 2.
FT   REPEAT      400    446       Kelch 3.
FT   REPEAT      448    493       Kelch 4.
FT   REPEAT      495    545       Kelch 5.
FT   REPEAT      546    594       Kelch 6.
FT   MOD_RES     419    419       Phosphotyrosine (By similarity).
SQ   SEQUENCE   617 AA;  69400 MW;  E4670F700065ABFE CRC64;
     MKVSLGNGDM GVSAHLQPCK SGTTRFFTSN THSSVVLQGF DQLRIEGLLC DVTLVPGDGE
     EIFPVHRAMM ASASDYFKAM FTGGMKEKDL MCIKLHGVNK VGLKKIIDFI YTAKLSLNMD
     NLQDTLEAAS FLQILPVLDF CKVFLISGVS LDNCVEVGRI ANTYNLIEVD KYVNNFILKN
     FPALLNTGEF LKLPFERLAF VLSSNSLKHC SELELFKAAC RWLRLEDPRM DYAAKLMKNI
     RFPLMTPQDL INYVQTVDFM RTDNTCVNLL LEASNYQMMP YMQPVMQSDR TAIRSDSTHL
     VTLGGVLRQQ LVVSKELRMY DERAQEWKSL APMDAPRYQH GIAVIGNFLY VVGGQSNYDT
     KGKTAVDTVF RFDPRYNKWM QVASLNEKRT FFHLSALKGH LYAVGGRSAA GELATVECYN
     PRMNEWSYVA KMSEPHYGHA GTVYGGLMYI SGGITHDTFQ NELMCFDPDT DKWTQKAPMT
     TVRGLHCMCT VGDKLYVIGG NHFRGTSDYD DVLSCEYYSP TLDQWTPIAA MLRGQSDVGV
     AVFENKIYVV GGYSWNNRCM VEIVQKYDPE KDEWHKVFDL PESLGGIRAC TLTVFPPEEN
     PGSPSRESPL SAPSDHS
//
ID   Q6ZPV6_MOUSE            Unreviewed;      1074 AA.
AC   Q6ZPV6;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   SubName: Full=MKIAA1227 protein;
DE   Flags: Fragment;
GN   Name=Zfp295; Synonyms=mKIAA1227;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
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DR   EMBL; AK129313; BAC98123.1; -; mRNA.
DR   IPI; IPI00453824; -.
DR   RefSeq; NP_001075153.1; NM_001081684.1.
DR   RefSeq; NP_001075154.1; NM_001081685.1.
DR   RefSeq; NP_780637.2; NM_175428.3.
DR   UniGene; Mm.1465; -.
DR   UniGene; Mm.474489; -.
DR   ProteinModelPortal; Q6ZPV6; -.
DR   STRING; Q6ZPV6; -.
DR   PhosphoSite; Q6ZPV6; -.
DR   PRIDE; Q6ZPV6; -.
DR   Ensembl; ENSMUST00000113734; ENSMUSP00000109363; ENSMUSG00000046962.
DR   GeneID; 114565; -.
DR   KEGG; mmu:114565; -.
DR   UCSC; uc008adv.1; mouse.
DR   CTD; 114565; -.
DR   MGI; MGI:1927240; Zfp295.
DR   HOGENOM; HBG443595; -.
DR   HOVERGEN; HBG056929; -.
DR   InParanoid; Q6ZPV6; -.
DR   ArrayExpress; Q6ZPV6; -.
DR   Bgee; Q6ZPV6; -.
DR   Genevestigator; Q6ZPV6; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR013069; BTB_POZ.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 2.
DR   Pfam; PF00651; BTB; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 8.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE   2: Evidence at transcript level;
KW   Metal-binding; Nucleus; Zinc.
FT   NON_TER       1      1
SQ   SEQUENCE   1074 AA;  119131 MW;  BF524487A0CBA605 CRC64;
     RNSEIKCRME GLLHYINPAH AISLLSALNE ERLKGQLCDV LLIVGDQKFR AHKNVLAASS
     EYFQSLFTNK ENEAQTVFQL DFCEPDAFDN VLNYIYSSSL FVEKGSLAAV QELGYSLGIS
     FLTNIVAKAP QAPFPACPNR KRVPVEDDET SSQKRSVIVC QGRSEVPGKA SGPAMQDLSH
     TARASPSASV KTTISKPHVA KPPEQLHSLP LTEKSWTKDS AAVYAKSLEQ AGALDDPNRG
     SLVKRNTVLP PKPSQDREAT DDKPGVSSQL PKGKAIELAL KRPRPPVLSL HSSSETPYLL
     KETSKGGGQG EDRNLLYYSK LGLVVPSGGP ASANQSIDRS GPLVKSLLRR SLSMDSQVPV
     YSPSIDLKSS QGSSTAANEA PGSVFCSMSQ KSSLKDCSEK KALDDRPQVL QPHRLRSFSA
     SQSTDREEAS PVTEVRIKTE PSSPLSDPSD IIRVTVGGDA AAAAVAAAAA AAATRDLPLK
     TEEDQRDMSR LPAKRRFQTD RRSPLKKAKA NEHGPAVSEE NCEEGRSPPS LDSNFPDSDL
     NREEFGELEG TRPNKKFKCK HCLKIFRSTA GLHRHVNMYH NPEKPYACDI CHKRFHTNFK
     VWTHCQTQHG IVKNPSPASS SHAVLDEKFQ RKLIDIVRER EIKKALIIKL RRSKPGFQGQ
     SSSPAQQVIK RNLRSRAKGA YICAYCGKAY RFLSQFKQHI KMHPGERPLG VSRAAKPKER
     ALARAVENKE VYPCRLCNAK LSSLLEQGNH ERLCRNATVC PYCSLRFFSP ALKQEHEDRC
     EYKKLTCLEC MRTFKSSFSI WRHQVEVHNQ NNMALAENFA LATLDHNGEV AAASRPQTEP
     SKVNHVATPK EDTAFSDSSE QVNFDSEDSS CLPEDLSLSK QLKVQVKEEP VEEAEEEAPE
     ASAAPREAGP SKETGLWPCE KCGKMFTAHK QLERHQELLC SVKPFICHVC YKAFRTNFRL
     WSHFQTHMSQ ATEEPVQKES EVCPVPTNSP SPPPLPPPPP LPKIQPLEPD SPTGLPENPT
     PATEKLFAPQ ESDTLFYHAP PLSAITFKRQ FMCKLCHRTF KTAFSLWSHE QTHN
//
ID   Q6ZPY3_MOUSE            Unreviewed;       723 AA.
AC   Q6ZPY3;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 31.
DE   SubName: Full=MKIAA1087 protein;
DE   Flags: Fragment;
GN   Name=Slc8a2; Synonyms=mKIAA1087;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
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CC   -----------------------------------------------------------------------
DR   EMBL; AK129285; BAC98095.1; -; mRNA.
DR   IPI; IPI00170310; -.
DR   UniGene; Mm.241147; -.
DR   STRING; Q6ZPY3; -.
DR   Ensembl; ENSMUST00000006175; ENSMUSP00000006175; ENSMUSG00000030376.
DR   MGI; MGI:107996; Slc8a2.
DR   HOVERGEN; HBG006441; -.
DR   InParanoid; Q6ZPY3; -.
DR   ArrayExpress; Q6ZPY3; -.
DR   Bgee; Q6ZPY3; -.
DR   Genevestigator; Q6ZPY3; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005432; F:calcium:sodium antiporter activity; IEA:InterPro.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   InterPro; IPR003644; Calx_beta.
DR   InterPro; IPR004836; Na_Ca_Ex.
DR   InterPro; IPR004837; NaCa_Exmemb.
DR   Pfam; PF03160; Calx-beta; 2.
DR   Pfam; PF01699; Na_Ca_ex; 2.
DR   PRINTS; PR01259; NACAEXCHNGR.
DR   SMART; SM00237; Calx_beta; 2.
DR   TIGRFAMs; TIGR00845; caca; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   NON_TER       1      1
SQ   SEQUENCE   723 AA;  79756 MW;  7571B6DF2C88D9FC CRC64;
     FVTASWSIFA YVWLYLILAV FSPGVVQVWE ALLTLIFFPV CVVFAWMADK RLLFYKYVYK
     RYRTDPRSGI IIGAEGDPPK SIELDGTFVG TEVPGELGAL GTGPAEAREL DASRREVIQI
     LKDLKQKHPD KDLEQLMGIA KYYALLHQQK SRAFYRIQAT RLMTGAGNVL RRHAADAARR
     PGATDGAPDD EDDGASRIFF EPSLYHCLEN CGSVLLSVAC QGGEGNSTFY VDYRTEDGSA
     KAGSDYEYSE GTLVFKPGET QKDLRIGIID DDIFEEDEHF FVRLLNLRVG DAQGMFEPDG
     GGRPKGRLVA PLLATVTILD DDHAGIFSFQ DRLLHVSECM GTVDVRVVRS SGARGTVRLP
     YRTVDGTARG GGVHYEDACG ELEFGDDETM KTLQVKIVDD EEYEKKDNFF IELGQPQWLK
     RGISALLLNQ GNGDKKITAE QEEAQRIAEM GKPVLGENNR LEVIIEESYD FKNTVDKLIK
     KTNLALVIGT HSWREQFIEA VTVSAGDEEE DEDGPREERL PSCFDYVMHF LTVFWKVLFA
     CVPPTEYCNG WACFGVCILV IGVLTALIGD LASHFGCTVG LKDSVNAVVF VALGTSIPDT
     FASKVAALQD QCADASIGNV TGSNAVNVFL GLGVAWSVAA VYWAVQGRPF EVRAGTLAFS
     VTLFTVFAFV CIAVLLYRRR PQIGGELGGP RGPKLATTAL FLGLWFLYIL FSSLEAYCHI
     RGF
//
ID   ZC3H4_MOUSE             Reviewed;        1304 AA.
AC   Q6ZPZ3;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Zinc finger CCCH domain-containing protein 4;
GN   Name=Zc3h4; Synonyms=Kiaa1064;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 310-1304 (ISOFORM 2).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-897, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1104; SER-1109 AND
RP   SER-1276, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-94, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6ZPZ3-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q6ZPZ3-2; Sequence=VSP_018209;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 3 C3H1-type zinc fingers.
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DR   EMBL; AC148972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK129275; BAC98085.1; -; mRNA.
DR   IPI; IPI00625723; -.
DR   IPI; IPI00750931; -.
DR   RefSeq; NP_941033.2; NM_198631.2.
DR   UniGene; Mm.333594; -.
DR   UniGene; Mm.470298; -.
DR   ProteinModelPortal; Q6ZPZ3; -.
DR   SMR; Q6ZPZ3; 416-502.
DR   PhosphoSite; Q6ZPZ3; -.
DR   PRIDE; Q6ZPZ3; -.
DR   Ensembl; ENSMUST00000086119; ENSMUSP00000083288; ENSMUSG00000059273.
DR   Ensembl; ENSMUST00000098791; ENSMUSP00000096388; ENSMUSG00000059273.
DR   GeneID; 330474; -.
DR   KEGG; mmu:330474; -.
DR   CTD; 330474; -.
DR   MGI; MGI:2682314; Zc3h4.
DR   GeneTree; ENSGT00530000063288; -.
DR   HOGENOM; HBG446706; -.
DR   HOVERGEN; HBG108366; -.
DR   InParanoid; Q6ZPZ3; -.
DR   OMA; FARTVLW; -.
DR   OrthoDB; EOG4Z62N1; -.
DR   ArrayExpress; Q6ZPZ3; -.
DR   Bgee; Q6ZPZ3; -.
DR   CleanEx; MM_ZC3H4; -.
DR   Genevestigator; Q6ZPZ3; -.
DR   GermOnline; ENSMUSG00000059273; Mus musculus.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR000571; Znf_CCCH.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   SMART; SM00356; ZnF_C3H1; 3.
DR   PROSITE; PS50103; ZF_C3H1; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Metal-binding; Phosphoprotein;
KW   Repeat; Zinc; Zinc-finger.
FT   CHAIN         1   1304       Zinc finger CCCH domain-containing
FT                                protein 4.
FT                                /FTId=PRO_0000234069.
FT   ZN_FING     389    416       C3H1-type 1.
FT   ZN_FING     418    445       C3H1-type 2.
FT   ZN_FING     446    469       C3H1-type 3.
FT   COILED       94    128       Potential.
FT   COILED      778    809       Potential.
FT   COMPBIAS      5     51       Pro-rich.
FT   COMPBIAS    233    373       Gly-rich.
FT   COMPBIAS    505    773       Pro-rich.
FT   COMPBIAS    988   1124       Pro-rich.
FT   MOD_RES      92     92       Phosphoserine.
FT   MOD_RES      94     94       Phosphoserine.
FT   MOD_RES     816    816       Phosphoserine (By similarity).
FT   MOD_RES     817    817       Phosphoserine (By similarity).
FT   MOD_RES     897    897       Phosphoserine.
FT   MOD_RES     913    913       Phosphoserine (By similarity).
FT   MOD_RES     917    917       Phosphoserine (By similarity).
FT   MOD_RES    1104   1104       Phosphoserine.
FT   MOD_RES    1109   1109       Phosphoserine.
FT   MOD_RES    1115   1115       Phosphoserine (By similarity).
FT   MOD_RES    1270   1270       Phosphoserine (By similarity).
FT   MOD_RES    1276   1276       Phosphoserine.
FT   VAR_SEQ     726    808       Missing (in isoform 2).
FT                                /FTId=VSP_018209.
SQ   SEQUENCE   1304 AA;  140967 MW;  F2D02AAC15148C8B CRC64;
     MEAVPGTPPP PPSESPPPPS PPPPSTPSPP PCSPDGRAAT PHLLHHRLPL PDDREDGELE
     EGELEDDGAE EVQDPPGGQE RSRKEKGEKH HSDSEEEKSH RRLKRKRKKE REKEKRRSKK
     RRKSKHKRHA SSSDDFSDFS DDSDFSPSEK SHRKYRDYSP PYAPSHQQYS SSHNAPLPKK
     SYSKMDSKGY SMYEDYENEQ YGEYEGDEEE DMGKEDYDDF TKELNQYRRA KEGSSRGRGS
     RGRGRGYRGR GSRGGSRGRG MGRGSRGRGR GSMGEHPEDE EDLYEEEIEY GESEEPMGDD
     DYDDYSKELN QYRRSKDSRG RGLSRGRGRG SRGGRGKGMG RGRGRGGRGG MSKGGMNDDE
     DFYDDDMGDG GGGSYRRSDH DKPHQQSDKK GKVICKYFVE GRCTWGDHCN FSHDIELPKK
     RELCKFYITG FCARAENCPY MHGDFPCKLY HTTGNCINGD DCMFSHDPLT EETRELLDKM
     LADDAEAGAE DEKEVEELKK QGINPLPKPP PGVGLLPTPP RPPGPPAPTS PNGRPMQGGP
     PPPPPPPPPP PGPPQMSLPT HEPLSPQQLQ QDMYNKKIPS LFEIVVRPTG QLAEKLGVRF
     PGPGGPSGPM GPGPNMGPPG PMGGPMHPDM HPDMHPDMHP DMHPDMHPDM HPDMHPDMHP
     DMPMGPGMNP GPPMGPGGPP MMPYGPGDSP HSGMMPPIPP AQNFYENFYP QQEGMEMEPG
     LVGDAEDYGH YEELPGQPGE PLFPEHPLEP DSFPEGGPPG RPKAGAGVPD FLPSAQRALY
     LRIQQKQQEE ERARRLAESS KQDRENEEGD TGNWYSSDED EGGSSVTSIL KTLRQQTSSR
     PQASVGEPSS SGLGDPRLQK GHPTGSRLSD PRLSRDPRLS RHAETSGGSG PGDSGPSDPR
     LARALPTSKA EGSLHSSPAG PSSSKGQPPA EEEEGERALR EKAVNIPLDP LPGHPLRDPR
     SQLQQFSHIK KDVTLSKPSF ARTVLWNPED LIPLPIPKQD VPPVPAALQS LPALDPRLHR
     STPPGPPNTR QRPGSTDPST SGSNLPDFEL LSRILKTVNV NTPGQSEKPS DPRVRKTPTD
     PRLQKPADPV AASRAAKPCP TEASPPAASP SGDSSPPATA PYDPRVLAAG GLGQGSSSGQ
     SSVLSGISLY DPRTPNAGGK TAEPASDTSA QPKGPEGNGK GSASKAKEPP FVRKSALEQP
     ETGKASTDGA TATDRYNSYN RPRPKATAAP TAASSTPPPE GATPQPGVHN LPVPTLFGTV
     KPAPKTGTGS PFAGNSPARE GEQDAGSLKD VFKGFDPTAS PFCQ
//
ID   EFR3B_MOUSE             Reviewed;         817 AA.
AC   Q6ZQ18; B2RXT1;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   08-MAR-2011, entry version 41.
DE   RecName: Full=Protein EFR3 homolog B;
GN   Name=Efr3b; Synonyms=Kiaa0953;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 117-817 (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-693, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6ZQ18-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZQ18-2; Sequence=VSP_029808;
CC   -!- SIMILARITY: Belongs to the EFR3 family.
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DR   EMBL; AC111092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC147643; AAI47644.1; -; mRNA.
DR   EMBL; BC157968; AAI57969.1; -; mRNA.
DR   EMBL; AK129247; BAC98057.1; -; mRNA.
DR   IPI; IPI00754572; -.
DR   IPI; IPI00876418; -.
DR   RefSeq; NP_001075952.1; NM_001082483.1.
DR   UniGene; Mm.210266; -.
DR   PhosphoSite; Q6ZQ18; -.
DR   PRIDE; Q6ZQ18; -.
DR   Ensembl; ENSMUST00000077156; ENSMUSP00000076399; ENSMUSG00000020658.
DR   Ensembl; ENSMUST00000111178; ENSMUSP00000106809; ENSMUSG00000020658.
DR   GeneID; 668212; -.
DR   KEGG; mmu:668212; -.
DR   NMPDR; fig|10090.3.peg.25888; -.
DR   CTD; 668212; -.
DR   MGI; MGI:2444851; Efr3b.
DR   eggNOG; roNOG05609; -.
DR   GeneTree; ENSGT00390000002143; -.
DR   HOGENOM; HBG445179; -.
DR   HOVERGEN; HBG060233; -.
DR   InParanoid; Q6ZQ18; -.
DR   OrthoDB; EOG4MW85F; -.
DR   NextBio; 434301; -.
DR   ArrayExpress; Q6ZQ18; -.
DR   Bgee; Q6ZQ18; -.
DR   CleanEx; MM_EFR3B; -.
DR   Genevestigator; Q6ZQ18; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR016024; ARM-type_fold.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    817       Protein EFR3 homolog B.
FT                                /FTId=PRO_0000312296.
FT   MOD_RES     693    693       Phosphoserine.
FT   VAR_SEQ     575    618       Missing (in isoform 2).
FT                                /FTId=VSP_029808.
SQ   SEQUENCE   817 AA;  92406 MW;  84726F2CF744145B CRC64;
     MYGVCGCCGA LRPRYKRLVD NIFPEDPEDG LVKTNMEKLT FYALSAPEKL DRIGAYLSER
     LIRDVGRHRY GYVCIAMEAL DQLLMACHCQ SINLFVESFL KMVAKLLESE KPNLQILGTN
     SFVKFANIEE DTPSYHRSYD FFVSRFSEMC HSSHDDLEIK TKIRMSGIKG LQGVVRKTVN
     DELQANIWDP QHMDKIVPSL LFNLQHVEEA ESRSPSPLQA PEKEKENPAE LAERCLRELL
     GRAAFGNIKN AIKPVLIHLD NHSLWEPKVF ATRCFKIIMY SIQPQHSHLV IQQLLSHLDA
     NSRSAATVRA GIVEVLSEAA IIAATGSVGP TVLEMFNTLL RQLRLSIDYA LTGSYDGAVS
     LGSKIIKEHE ECMFQEAVIK TIGSFASTLP TYQRSEVILF IMSKVPLPSV HHPVETGRTG
     ENRNRLTQIM LLKSLLQVST GFQCNNMMSA LPSNFLDRLL STALMEDAEI RLFVLEILIS
     FIDRHGNRHK FSTISTLGDI SVLKLKVDKC SRQDTVFMKK HSQQLYRHIY LSCKEETNIQ
     KHYEALYGLL ALISIELANE EVVVDLIRLV LAVQDVAQVN EENLPTYNRC ALYALGAAYL
     NLISQLTTVP AFCQHIHEVI ETRKKEAPYM LPEDVFVEKP RLSQNLDGVV IEFLFRQSKI
     SEVLGGSGYN SDRLCLPYIP QLTDEDRLSK RKSIGETISL QVEVESRNSP EKEERVPAEE
     ITYETLKKAI VDSVAVEEQE RERQRQVVEK FQKAPFEEIA AHCGARASLL QSKLNQIFEI
     TIRPPPSPSG TISAAYGQPQ NHSIPVYEMK FPDLCVY
//
ID   TAOK2_MOUSE             Reviewed;        1240 AA.
AC   Q6ZQ29; Q7TSS8;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 3.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Serine/threonine-protein kinase TAO2;
DE            EC=2.7.11.1;
DE   AltName: Full=Thousand and one amino acid protein 2;
GN   Name=Taok2; Synonyms=Kiaa0881;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, and Czech II; TISSUE=Brain, and Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-43, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Isoform 1, but not isoform 2, plays a role in apoptotic
CC       morphological changes. May affect microtubule organization and
CC       stability. May play a role in the osmotic stress-MAPK8 pathway.
CC       Activates the JNK MAP kinase pathway through the specific
CC       activation of the upstream MKK3 and MKK6 kinases. Prevents MAP3K7-
CC       mediated activation of IKKA, and thus NF-kappa-B activation.
CC       Phosphorylates itself, MBP, activated MAPK8 and tubulins (By
CC       similarity). Isoform 2, but not isoform 1, is required for PCDH8
CC       endocytosis. Following homophilic interactions between PCDH8
CC       extracellular domains, isoform 2 phosphorylates and activates
CC       MAPK14/p38 MAPK which in turn phosphorylates isoform 2. This
CC       process leads to PCDH8 endocytosis and CDH2 cointernalization (By
CC       similarity). Both isoforms are involved in MAPK14/p38 MAPK
CC       phosphorylation (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SUBUNIT: Interacts with MKK3 and MKK6 (By similarity). Self-
CC       associates. Interacts with tubulins. Interacts with MAP3K7 and
CC       interfers with MAP3K7-binding to IKKA and thus prevents NF-kappa-B
CC       activation (By similarity). Isoform 2 interacts with PCDH8; this
CC       complex may also include CDH2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Multi-pass
CC       membrane protein (By similarity). Cytoplasm, cytoskeleton (By
CC       similarity). Note=Found to be perinuclear and localized to
CC       vesicular compartment (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cell projection, dendrite (By
CC       similarity). Note=In dendrites, colocalizes with PCDH8 (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6ZQ29-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZQ29-2; Sequence=VSP_040543, VSP_040544;
CC   -!- PTM: isoform 2 is phosphorylated at 'Ser-1037' by MAPK14. This
CC       phosphorylation is required PCDH8 for endocytosis (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH52933.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N- and C-terminal parts;
CC       Sequence=BAC98045.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; AK129235; BAC98045.1; ALT_INIT; mRNA.
DR   EMBL; BC052933; AAH52933.1; ALT_SEQ; mRNA.
DR   EMBL; BC085152; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00420553; -.
DR   RefSeq; NP_001157246.1; NM_001163774.1.
DR   UniGene; Mm.259634; -.
DR   ProteinModelPortal; Q6ZQ29; -.
DR   STRING; Q6ZQ29; -.
DR   PhosphoSite; Q6ZQ29; -.
DR   PRIDE; Q6ZQ29; -.
DR   Ensembl; ENSMUST00000071268; ENSMUSP00000071246; ENSMUSG00000059981.
DR   GeneID; 381921; -.
DR   KEGG; mmu:381921; -.
DR   UCSC; uc009jtg.1; mouse.
DR   CTD; 381921; -.
DR   MGI; MGI:1915919; Taok2.
DR   GeneTree; ENSGT00600000084021; -.
DR   HOVERGEN; HBG088996; -.
DR   OMA; PYQPEME; -.
DR   OrthoDB; EOG4Q58NS; -.
DR   PhylomeDB; Q6ZQ29; -.
DR   BRENDA; 2.7.11.1; 244.
DR   ArrayExpress; Q6ZQ29; -.
DR   Bgee; Q6ZQ29; -.
DR   CleanEx; MM_TAOK2; -.
DR   Genevestigator; Q6ZQ29; -.
DR   GermOnline; ENSMUSG00000059981; Mus musculus.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell projection; Coiled coil;
KW   Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Kinase; Magnesium;
KW   Membrane; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   1240       Serine/threonine-protein kinase TAO2.
FT                                /FTId=PRO_0000086734.
FT   TRANSMEM    972    992       Helical; (Potential).
FT   TRANSMEM    994   1014       Helical; (Potential).
FT   TRANSMEM   1019   1039       Helical; (Potential).
FT   TRANSMEM   1045   1065       Helical; (Potential).
FT   TRANSMEM   1175   1195       Helical; (Potential).
FT   DOMAIN       28    281       Protein kinase.
FT   NP_BIND      34     42       ATP (By similarity).
FT   COILED      493    528       Potential.
FT   COILED      581    608       Potential.
FT   COILED      688    720       Potential.
FT   COILED      805    934       Potential.
FT   COMPBIAS    353    376       Ser-rich.
FT   COMPBIAS    384    414       Glu-rich.
FT   COMPBIAS    990   1083       Pro-rich.
FT   ACT_SITE    151    151       Proton acceptor (By similarity).
FT   BINDING      57     57       ATP (By similarity).
FT   MOD_RES       9      9       Phosphoserine (By similarity).
FT   MOD_RES      43     43       Phosphotyrosine.
FT   MOD_RES     181    181       Phosphoserine (By similarity).
FT   MOD_RES     456    456       Phosphoserine (By similarity).
FT   MOD_RES     480    480       Phosphoserine (By similarity).
FT   MOD_RES     493    493       Phosphoserine (By similarity).
FT   MOD_RES     500    500       Phosphoserine (By similarity).
FT   MOD_RES     782    782       Phosphoserine (By similarity).
FT   MOD_RES     830    830       Phosphoserine (By similarity).
FT   MOD_RES     832    832       Phosphoserine (By similarity).
FT   VAR_SEQ     752   1055       VRAGQLPMGLPATGALGPLSTGTPSEEQPCSSGQEAILDQR
FT                                MLGEEEEAVPERRILGKEGTTLEPEEQRILGEEMGTFSSSP
FT                                QKHRSLANEEDWDISEEMKEIRVPSLASQERNIIGQEEAAA
FT                                WSLWEKEGGNLVDVEFKLGWVQGPVLTPVPEEEEEEEEEGG
FT                                APIGTHRDPGDGCPSPDIPPEPPPSHLRQYPTSQLPGLLSH
FT                                GLLAGLSFAVGSSSGLLPLLLLLLLPLLAAQGGGGLQAALL
FT                                ALEVGLVGLGASYLFLCTALHLPPGLFLLLAQGTALLAVLS
FT                                LSWRRGLMGVPLGLGAA -> SKELQIKKQFQETCKIQTRQ
FT                                YKALRAHLLETTPKAQHKSLLKRLKEEQTRKLAILAEQYDQ
FT                                SISEMLSSQALRLDETQEAEFQALRQQLQQELELLNAYQSK
FT                                IKIRTESQHERELRELEQRVALRRALLEQRVEEELLALQTG
FT                                RSERIRSLLERQAREIEAFDAESMRLGFSSMALGGIPAEAA
FT                                AQGYPAPPPAPAWPSRPVPRSGAHWSHGPPPPGMPPPAWRQ
FT                                PALLAPPGPPNWLGPPTQSGTPRGGALLLLRNSPQPLRRAA
FT                                SGGSSGENVGPPAAVPGPLSRSTSVASHILNGSSHFYS
FT                                (in isoform 2).
FT                                /FTId=VSP_040543.
FT   VAR_SEQ    1056   1240       Missing (in isoform 2).
FT                                /FTId=VSP_040544.
SQ   SEQUENCE   1240 AA;  139297 MW;  E6A989CD16B1AE54 CRC64;
     MPAGGRAGSL KDPDVAELFF KDDPEKLFSD LREIGHGSFG AVYFARDVRN SEVVAIKKMS
     YSGKQSNEKW QDIIKEVRFL QKLRHPNTIQ YRGCYLREHT AWLVMEYCLG SASDLLEVHK
     KPLQEVEIAA VTHGALQGLA YLHSHNMIHR DVKAGNILLS EPGLVKLGDF GSASIMAPAN
     SFVGTPYWMA PEVILAMDEG QYDGKVDVWS LGITCIELAE RKPPLFNMNA MSALYHIAQN
     ESPALQSGHW SEYFRNFVDS CLQKIPQDRP TSEVLLKHRF VLRERPPTVI MDLIQRTKDA
     VRELDNLQYR KMKKILFQEA PNGPGAEAPE EEELTPCSQE AEPYTHRAGT LTSLESSHSV
     PSMSISASSQ SSSVNSLADA SDNEEEEEEE EEEEEEEEEE GPESREMAMM QEGEHTVTSH
     SSIIHRLPGS DNLYDDPYQP EMTPGPLQPP AAPPTSTSSS ARRRAYCRNR DHFATIRTAS
     LVSRQIQEHE QDSALREQLS GYKRMRRQHQ KQLLALESRL RGEREEHSGR LQRELEAQRA
     GFGTEAEKLA RRHQAIGEKE ARAAQAEERK FQQHILGQQK KELAALLEAQ KRTYKLRKEQ
     LKEELQENPS TPKREKAEWL LRQKEQLQQC QAEEEAGLLR RQRQYFELQC RQYKRKMLLA
     RHSLDQDLLR EDLNKKQTQK DLECALLLRQ HEATRELELR QLQAVQRTRA ELTRLQHQTE
     LGNQLEYNKR REQELRQKHA AQVRQQPKSL KVRAGQLPMG LPATGALGPL STGTPSEEQP
     CSSGQEAILD QRMLGEEEEA VPERRILGKE GTTLEPEEQR ILGEEMGTFS SSPQKHRSLA
     NEEDWDISEE MKEIRVPSLA SQERNIIGQE EAAAWSLWEK EGGNLVDVEF KLGWVQGPVL
     TPVPEEEEEE EEEGGAPIGT HRDPGDGCPS PDIPPEPPPS HLRQYPTSQL PGLLSHGLLA
     GLSFAVGSSS GLLPLLLLLL LPLLAAQGGG GLQAALLALE VGLVGLGASY LFLCTALHLP
     PGLFLLLAQG TALLAVLSLS WRRGLMGVPL GLGAAWLLAW PSLALPLAAM AAGGKWVRQQ
     GPQMRRGISR LWLRILLRLS PMVFRALQGC GAVGDRGLFA LYPKTNKNGF RSRLPVPWPR
     QGNPRTTQHP LAQLTRVWAV CKGWNWRLAR ASHRLASCLP PWAVHILASW GLLKGERPSR
     IPRLLPRSQR RLGLSASRQL PPGTVAGRRS QTRRTLPPWR
//
ID   Q6ZQ33_MOUSE            Unreviewed;      1353 AA.
AC   Q6ZQ33;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 47.
DE   SubName: Full=MKIAA0857 protein;
DE   Flags: Fragment;
GN   Name=Rab11fip5; Synonyms=mKIAA0857;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SIMILARITY: Contains 1 C2 domain.
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DR   EMBL; AK129230; BAC98040.1; -; mRNA.
DR   IPI; IPI00480432; -.
DR   RefSeq; NP_001003955.1; NM_001003955.2.
DR   RefSeq; NP_803417.3; NM_177466.4.
DR   UniGene; Mm.220334; -.
DR   ProteinModelPortal; Q6ZQ33; -.
DR   STRING; Q6ZQ33; -.
DR   Ensembl; ENSMUST00000089579; ENSMUSP00000087007; ENSMUSG00000051343.
DR   GeneID; 52055; -.
DR   KEGG; mmu:52055; -.
DR   UCSC; uc009cpn.1; mouse.
DR   CTD; 52055; -.
DR   MGI; MGI:1098586; Rab11fip5.
DR   GeneTree; ENSGT00530000063203; -.
DR   InParanoid; Q6ZQ33; -.
DR   OMA; HHLPCSP; -.
DR   OrthoDB; EOG49CQ7C; -.
DR   NextBio; 308438; -.
DR   ArrayExpress; Q6ZQ33; -.
DR   Bgee; Q6ZQ33; -.
DR   Genevestigator; Q6ZQ33; -.
DR   GO; GO:0015031; P:protein transport; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR019018; Rab11-bd_FIP_dom_C.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF09457; RBD-FIP; 1.
DR   SMART; SM00239; C2; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   PROSITE; PS50004; C2; 1.
PE   1: Evidence at protein level;
FT   NON_TER       1      1
SQ   SEQUENCE   1353 AA;  142909 MW;  064FEE010C4655D5 CRC64;
     QPAAAAVGAL QAARGSRLLT ASRGCHVCHS VPGSAMALVR DPEPAAGSSR WLPTHVQVTV
     LRASGLRGKS SGAGSTSDAY TVIQVGREKY STSVVEKTQG CPEWCEECSF ELPPGALDGL
     LRAQEADAGP APWASGPNAA CELVLTTMHR SLIGVDKFLG RATVALDEVF RAGRAQHTQW
     YRLHSKPGKK EKERGEIQVT IQFTRNNLSA SMFDLSMKDK PRSPFSKLKD RVKGKKKYDL
     ESASAILPSS ALEDPELGSL GKMGKAKGFF LRNKLRKSSL TQSNTSLGSD STLSSTSGSL
     VYQGPGAELL TRSPSHSSWL STEGGRDSIQ SPKLLTHKRT YSDEASQLRA APPRALLELQ
     GHLDGASRSS LCVNGSHVYN EEPQPPLRHR SSISGPFPPS SSLHSVPPRS SEEGSRSSDD
     SWGRGSHGTS SSEAVPGQEE LSKQAKGASC SGEEEGARLP EGKPVQVATP MVASSEAVAA
     EKDRKPRMGL FHHHHHQGLS RSEQGRRGSV GEKGSPSLGA SPHHSSTGEE KAKSSWFGLR
     ESKEPTQKPS LDVSPQVESD PAAPHPCSPQ ALAPPPAPAA APMLSTNLFA VTSPAAATAA
     AATIVLEATP SGFLGVTNPF LNSLQSNPFF EDLKADIALN SPSPAPSLPS ASRASLAPLA
     SPGKALPEWD DTFNIFAAGR LQQEAGSGIL APAGMGLEED GLQDPGPRTM AVKATEPQGE
     PGRGRRGSNI WLEPKVSVDS ELDQPSTSMS DPGPFGSSGS GPSSRASQLH LQASASTPDR
     ELPASEGGAG QSPADSGASL FSSPEVLSVW ERFPGSDDTP GGRDEEAPQD GSQLFQELNT
     VEDSWPWDVI TISPTAEVAS PVMKGESDGV LSSQVQPESP DTVPPMGSEG LPALLEPEPE
     QGLDEGPWLG PPPPKPPRLF TPTNSQVEEE DKEEEENATG RQSSRGPGVE KDSTPRALAI
     GPQESKEEWV NPELEKLHRL PSGTLIGKPE LEDPVGETSS PVFGDCPPRP TSCPEGPVPR
     PHNSISSTLL SQKVLGTSET EEGFETKSQE LAKEGFGPLS VPSQQSSMRA KEEEEGEEEE
     EEGEEEEALE TSNSFLCQES QDPPSFPSIS PPGSRGSSIH SGPEELPTPP EPAFPPPPLP
     PWASHRHGVP GPPCPPLPIA WPLTSSSSPP EESASPLGPP ELSPTGGSPT SYGEDHAAAT
     PASPLVLLPL ETRPAEEPQP SGSPHPVKPL TAAPVEASPD RKQPRTSLST ALSSGLERLK
     TVTSGGIQSV LPASQLGSSV DTKRPKDSAV LDQSAKYYHL THDELIGLLL QRERELSQRD
     EHVQELESYI DRLLVRIMET SPTLLQISPG PPK
//
ID   CAND1_MOUSE             Reviewed;        1230 AA.
AC   Q6ZQ38; Q6PFR0; Q9CV45;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Cullin-associated NEDD8-dissociated protein 1;
DE   AltName: Full=Cullin-associated and neddylation-dissociated protein 1;
DE   AltName: Full=p120 CAND1;
GN   Name=Cand1; Synonyms=D10Ertd516e, Kiaa0829;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 342-1230.
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1007-1230.
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Enhances transcription from various types of promoters.
CC       Regulatory protein that interferes with the assembly of the SCF
CC       (SKP1-CUL1-F-box protein) ubiquitin ligase complex and thereby
CC       down-regulates ubiquitination of target proteins. Prevents
CC       neddylation of CUL1 by physically blocking access to the
CC       neddylation site. Disrupts interactions between CUL1 and SKP1A and
CC       between CUL1 and F-box proteins (By similarity).
CC   -!- SUBUNIT: Part of a complex that contains CUL1 and RBX1. Binds
CC       unneddylated CUL1, but cannot bind CUL1 once it has been
CC       neddylated. Binds CUL2, CUL3, CUL4A, CUL4B and CUL5. Binds TBP (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the CAND family.
CC   -!- SIMILARITY: Contains 27 HEAT repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH57457.1; Type=Erroneous initiation;
CC       Sequence=BAB26438.1; Type=Erroneous initiation;
CC       Sequence=BAC98035.1; Type=Erroneous initiation;
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DR   EMBL; AK129225; BAC98035.1; ALT_INIT; mRNA.
DR   EMBL; BC057457; AAH57457.1; ALT_INIT; mRNA.
DR   EMBL; AK009683; BAB26438.1; ALT_INIT; mRNA.
DR   IPI; IPI00896727; -.
DR   RefSeq; NP_082270.1; NM_027994.1.
DR   UniGene; Mm.203965; -.
DR   ProteinModelPortal; Q6ZQ38; -.
DR   IntAct; Q6ZQ38; 4.
DR   STRING; Q6ZQ38; -.
DR   PhosphoSite; Q6ZQ38; -.
DR   PRIDE; Q6ZQ38; -.
DR   Ensembl; ENSMUST00000020315; ENSMUSP00000020315; ENSMUSG00000020114.
DR   GeneID; 71902; -.
DR   KEGG; mmu:71902; -.
DR   UCSC; uc007hec.1; mouse.
DR   CTD; 71902; -.
DR   MGI; MGI:1261820; Cand1.
DR   GeneTree; ENSGT00390000017740; -.
DR   HOGENOM; HBG560547; -.
DR   HOVERGEN; HBG053467; -.
DR   InParanoid; Q6ZQ38; -.
DR   OMA; MLEFFQA; -.
DR   OrthoDB; EOG441Q9N; -.
DR   NextBio; 334892; -.
DR   ArrayExpress; Q6ZQ38; -.
DR   Bgee; Q6ZQ38; -.
DR   CleanEx; MM_CAND1; -.
DR   Genevestigator; Q6ZQ38; -.
DR   GermOnline; ENSMUSG00000020114; Mus musculus.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0016563; F:transcription activator activity; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; ISS:UniProtKB.
DR   GO; GO:0043086; P:negative regulation of catalytic activity; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR013932; TATA-bd_TIP120.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 2.
DR   Pfam; PF08623; TIP120; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Acetylation; Nucleus; Phosphoprotein; Repeat; Transcription;
KW   Transcription regulation; Ubl conjugation pathway.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1230       Cullin-associated NEDD8-dissociated
FT                                protein 1.
FT                                /FTId=PRO_0000089294.
FT   REPEAT        2     39       HEAT 1.
FT   REPEAT       44     81       HEAT 2.
FT   REPEAT       83    119       HEAT 3.
FT   REPEAT      131    165       HEAT 4.
FT   REPEAT      171    208       HEAT 5.
FT   REPEAT      210    247       HEAT 6.
FT   REPEAT      248    282       HEAT 7.
FT   REPEAT      289    366       HEAT 8.
FT   REPEAT      370    407       HEAT 9.
FT   REPEAT      424    467       HEAT 10.
FT   REPEAT      471    510       HEAT 11.
FT   REPEAT      515    552       HEAT 12.
FT   REPEAT      563    602       HEAT 13.
FT   REPEAT      606    643       HEAT 14.
FT   REPEAT      646    683       HEAT 15.
FT   REPEAT      688    725       HEAT 16.
FT   REPEAT      729    768       HEAT 17.
FT   REPEAT      770    808       HEAT 18.
FT   REPEAT      809    845       HEAT 19.
FT   REPEAT      852    889       HEAT 20.
FT   REPEAT      890    927       HEAT 21.
FT   REPEAT      928    960       HEAT 22.
FT   REPEAT      961    998       HEAT 23.
FT   REPEAT     1002   1039       HEAT 24.
FT   REPEAT     1043   1097       HEAT 25.
FT   REPEAT     1099   1133       HEAT 26.
FT   REPEAT     1140   1189       HEAT 27.
FT   COMPBIAS    314    344       Asp-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     335    335       Phosphoserine (By similarity).
FT   MOD_RES     340    340       Phosphoserine (By similarity).
FT   MOD_RES     624    624       Phosphothreonine (By similarity).
FT   MOD_RES     971    971       N6-acetyllysine (By similarity).
SQ   SEQUENCE   1230 AA;  136332 MW;  20B6BFB4ED250825 CRC64;
     MASASYHISN LLEKMTSSDK DFRFMATNDL MTELQKDSIK LDDDSERKVV KMILRLLEDK
     NGEVQNLAVK CLGPLVSKVK EYQVETIVDT LCTNMLSDKE QLRDISSIGL KTVIGELPPA
     SSGSALAANV CKKITGRLTS AIAKQEDVSV QLEALDIMAD MLSRQGGLLV NFHPSILTCL
     LPQLTSPRLA VRKRTIIALG HLVMSCGNIV FVDLIEHLLS ELSKNDSMST TRTYIQCIAA
     ISRQAGHRIG EYLEKIIPLV VKFCNVDDDE LREYCIQAFE SFVRRCPKEV YPHVSTIINI
     CLKYLTYDPN YNYDDEDEDE NAMDADGGDD DDQGSDDEYS DDDDMSWKVR RAAAKCLDAV
     VSTRHEMLPE FYKTVSPALI ARFKEREENV KADVFHAYLS LLKQTRPVQS WLCDPDAMEQ
     GDTPLTMLQS QVPNIVKALH KQMKEKSVKT RQCCFNMLTE LVNVLPGALT QHIPVLVPGI
     IFSLNDKSSS SNLKIDALSC LYVILCNHSP QVFHPHVQAL VPPVVACVGD PFYKITSEAL
     LVTQQLVKVI RPLDQPSSFD ATPYIKDLFT CTIKRLKAAD IDQEVKERAI SCMGQIICNL
     GDNLGPDLSN TLQIFLERLK NEITRLTTVK ALTLIAGSPL KIDLRPVLGE GVPILASFLR
     KNQRALKLGT LSALDILIKN YSDSLTAAMI DAVLDELPPL ISESDMHVSQ MAISFLTTLA
     KVYPSSLSKI SGSILNELIG LVRSPLLQGG ALSAMLDFFQ ALVVTGTNNL GYMDLLRMLT
     GPVYSQSTAL THKQSYYSIA KCVAALTRAC PKEGPAVVGQ FIQDVKNSRS TDSIRLLALL
     SLGEVGHHID LSGQLELKSV ILEAFSSPSE EVKSAASYAL GSISVGNLPE YLPFVLQEIT
     SQPKRQYLLL HSLKEIISSA SVAGLKPYVE NIWALLLKHC ECAEEGTRNV VAECLGKLTL
     IDPETLLPRL KGYLISGSSY ARSSVVTAVK FTISDHPQPI DPLLKNCIGD FLKTLEDPDL
     NVRRVALVTF NSAAHNKPSL IRDLLDSVLP HLYNETKVRK ELIREVEMGP FKHTVDDGLD
     IRKAAFECMY TLLDSCLDRL DIFEFLNHVE DGLKDHYDIK MLTFLMLVRL STLCPSAVLQ
     RLDRLVEPLR ATCTTKVKAN SVKQEFEKQD ELKRSAMRAV AALLTIPEAE KSPLMSEFQS
     QISSNPELAA IFESIQKDSS STNLESMDTS
//
ID   Q6ZQ46_MOUSE            Unreviewed;      1078 AA.
AC   Q6ZQ46;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   05-OCT-2010, entry version 35.
DE   SubName: Full=MKIAA0790 protein;
DE   Flags: Fragment;
GN   Name=Sash1; Synonyms=mKIAA0790;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
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DR   EMBL; AK129216; BAC98026.1; -; mRNA.
DR   IPI; IPI00338954; -.
DR   UniGene; Mm.338275; -.
DR   HSSP; P29355; 1K76.
DR   ProteinModelPortal; Q6ZQ46; -.
DR   STRING; Q6ZQ46; -.
DR   Ensembl; ENSMUST00000015449; ENSMUSP00000015449; ENSMUSG00000015305.
DR   MGI; MGI:1917347; Sash1.
DR   HOVERGEN; HBG103373; -.
DR   InParanoid; Q6ZQ46; -.
DR   ArrayExpress; Q6ZQ46; -.
DR   Bgee; Q6ZQ46; -.
DR   Genevestigator; Q6ZQ46; -.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR021090; SAM/SH3_domain-containing.
DR   InterPro; IPR011510; SAM_2.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 2.
DR   Pfam; PF07647; SAM_2; 2.
DR   Pfam; PF07653; SH3_2; 1.
DR   Pfam; PF12485; SLY; 1.
DR   SMART; SM00454; SAM; 2.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF47769; SAM_homology; 2.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 2.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   1078 AA;  118517 MW;  B42C737FF7400DF7 CRC64;
     KNQKGIMRQT SKGEDVGYVA SEITMSDEER IQLMMMVKEK MITIEEALAR LKEYEAQHRQ
     SSTLDPADWP DGSYPTLDGS STCNSREQSD DETEDSVKFK RLHKLVNSTR RVRKKLIRVE
     EMKKPSTEGG EEHVFENSPV QDERSALYSG VHKKPFFYDG SPEKPPEDDA DSLTPSPSSS
     SLDTWGAGRK LVKTFSKGES RGLIKPPKKM GTFFSYPEEE KAQKVSRSLT EGEMKKGLGS
     LSHGRTCSFG GFDLTNRSLH VGSNNSDPAG KEGDFVYKEV IKSPSAPRIS LGKKVRSVKE
     TMRKRMSKKY SSPVSEQDSG LDGMPSSPAS GKPDSEHVDK PKLKAGGSVE SLRSSLSGQS
     SMSGQTVSTT DSSTSNRESV KSEDGDDEEP PYRGPFCGRA RVHTDFTPSP YDTDSLKLKK
     GDIIDIISKP PMGTWMGLLN NKVGTFKFIY VDVLNEEEEK PKRPTRRRKK GRPSQPKSVE
     DLLDRINLKE HMPTFLFNGY EDLDTFKLLE EEDLDELNIR DPEHRAVLLT AVELLQEYDS
     NSDQSGSQEK LLVDNQGLSG RSPRDSGCYE SSENLENAKT HKPSVLSTKS STESNLKSFT
     RSQPGNYPTL PLMKSGEVRK QGEEGRLGRG LAPDTAKSCD VPSVTDLSKN RRSLPVSICR
     SCETLEGPEP VESWPRSHSL DDLQGDADVG KNVPTEMPET CSQNVPEVPQ KTSACTSKAL
     PRGRDPTADV MLLTQSKRFS DPPKTMAKKL DGSVVASNLG IAPPQCIPRD FEAQPPVKPG
     LTRTSLEGLR KGHDHHPLGT KEGVDGEQSA PETRTQSRHP SQPPPVPAKK SRERLANGLH
     LVPSPEAPIL PLKKASPASP VSPSDCPSPR EPRPSSGTEP GSPACTRPPP WLAELPESTS
     LQEHGVKLGP VLSRKVSCVR GVDLEMLTEN KLQAEGIDLT EEPYSDKHGR CGIPEALVQR
     YAEDLEQPER DVATNMDQIR VKLLRKQHRM AIPSGGLTEI CRKPLSPGCV ASMSDWLISI
     GLPMYTSTLS DAGFSTLSQV PSLSHSCLQE AGITEERHIR KLITAARLFK LPPNPEAM
//
ID   LARP1_MOUSE             Reviewed;        1072 AA.
AC   Q6ZQ58; A2AFQ8; Q7TSF7;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=La-related protein 1;
DE   AltName: Full=La ribonucleoprotein domain family member 1;
GN   Name=Larp1; Synonyms=Kiaa0731, Larp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 709-1072 (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   DEVELOPMENTAL STAGE.
RX   MEDLINE=20340711; PubMed=10878606;
RX   DOI=10.1002/1097-0177(200007)218:3<401::AID-DVDY1009>3.0.CO;2-6;
RA   Chauvet S., Maurel-Zaffran C., Miassod R., Jullien N., Pradel J.,
RA   Aragnol D.;
RT   "dlarp, a new candidate Hox target in Drosophila whose orthologue in
RT   mouse is expressed at sites of epithelium/mesenchymal interactions.";
RL   Dev. Dyn. 218:401-413(2000).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604; SER-608; SER-751;
RP   SER-828 AND SER-1032, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-503 AND SER-525, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81 AND SER-201, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604 AND SER-608, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299; SER-302; THR-503;
RP   SER-525 AND SER-751, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6ZQ58-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZQ58-2; Sequence=VSP_015116;
CC         Note=No experimental confirmation available;
CC   -!- DEVELOPMENTAL STAGE: At E10.5, expressed in dorsal root ganglia,
CC       spinal cord, and branchial arches. At E14.5, expressed in
CC       olfactory epithelium and cranial sensory ganglia. Also expressed
CC       in salivary glands, lungs, gut, kidney, teeth and vibrissae.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the LARP family.
CC   -!- SIMILARITY: Contains 1 HTH La-type RNA-binding domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AL672182; CAM19966.1; -; Genomic_DNA.
DR   EMBL; BC053449; AAH53449.1; -; mRNA.
DR   EMBL; AK129202; BAC98012.1; -; mRNA.
DR   IPI; IPI00929761; -.
DR   IPI; IPI00929786; -.
DR   UniGene; Mm.248843; -.
DR   ProteinModelPortal; Q6ZQ58; -.
DR   SMR; Q6ZQ58; 378-452.
DR   PRIDE; Q6ZQ58; -.
DR   Ensembl; ENSMUST00000071487; ENSMUSP00000071421; ENSMUSG00000037331.
DR   UCSC; uc007jah.1; mouse.
DR   MGI; MGI:1890165; Larp1.
DR   eggNOG; roNOG13503; -.
DR   GeneTree; ENSGT00390000000523; -.
DR   HOGENOM; HBG713047; -.
DR   HOVERGEN; HBG054322; -.
DR   InParanoid; Q6ZQ58; -.
DR   OMA; NARTPRT; -.
DR   OrthoDB; EOG4PZJ64; -.
DR   ArrayExpress; Q6ZQ58; -.
DR   Bgee; Q6ZQ58; -.
DR   CleanEx; MM_LARP1; -.
DR   Genevestigator; Q6ZQ58; -.
DR   GermOnline; ENSMUSG00000037331; Mus musculus.
DR   InterPro; IPR006607; DM15.
DR   InterPro; IPR006630; Lupus_La_RNA-bd.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF05383; La; 1.
DR   SMART; SM00684; DM15; 3.
DR   SMART; SM00715; LA; 1.
DR   PROSITE; PS50961; HTH_LA; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1072       La-related protein 1.
FT                                /FTId=PRO_0000207610.
FT   DOMAIN      372    462       HTH La-type RNA-binding.
FT   COMPBIAS     95    175       Pro-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      68     68       Phosphoserine (By similarity).
FT   MOD_RES      81     81       Phosphoserine.
FT   MOD_RES     138    138       Phosphoserine (By similarity).
FT   MOD_RES     201    201       Phosphoserine.
FT   MOD_RES     299    299       Phosphoserine.
FT   MOD_RES     302    302       Phosphoserine.
FT   MOD_RES     503    503       Phosphothreonine.
FT   MOD_RES     523    523       Phosphoserine (By similarity).
FT   MOD_RES     525    525       Phosphoserine.
FT   MOD_RES     599    599       Phosphothreonine (By similarity).
FT   MOD_RES     601    601       Phosphothreonine (By similarity).
FT   MOD_RES     604    604       Phosphoserine.
FT   MOD_RES     608    608       Phosphoserine.
FT   MOD_RES     610    610       Phosphotyrosine (By similarity).
FT   MOD_RES     626    626       Phosphothreonine (By similarity).
FT   MOD_RES     701    701       Phosphothreonine (By similarity).
FT   MOD_RES     743    743       Phosphoserine (By similarity).
FT   MOD_RES     751    751       Phosphoserine.
FT   MOD_RES     762    762       Phosphothreonine (By similarity).
FT   MOD_RES     765    765       Phosphothreonine (By similarity).
FT   MOD_RES     800    800       Phosphoserine (By similarity).
FT   MOD_RES     801    801       Phosphoserine (By similarity).
FT   MOD_RES     822    822       Phosphothreonine (By similarity).
FT   MOD_RES     824    824       Phosphoserine (By similarity).
FT   MOD_RES     826    826       Phosphoserine (By similarity).
FT   MOD_RES     827    827       Phosphoserine (By similarity).
FT   MOD_RES     828    828       Phosphoserine.
FT   MOD_RES     830    830       Phosphoserine (By similarity).
FT   MOD_RES     839    839       Phosphotyrosine (By similarity).
FT   MOD_RES     869    869       N6-acetyllysine (By similarity).
FT   MOD_RES     994    994       N6-acetyllysine (By similarity).
FT   MOD_RES    1032   1032       Phosphoserine.
FT   MOD_RES    1047   1047       Phosphothreonine (By similarity).
FT   VAR_SEQ       1   1006       Missing (in isoform 2).
FT                                /FTId=VSP_015116.
SQ   SEQUENCE   1072 AA;  121152 MW;  83BA6D304BC06485 CRC64;
     MATQVEPLLP AGAPLLQAEE HGLARKKPAP DAQAESGPGD GGGEPDGGVR RPRPACARPG
     RDGAERESPR PPAAAEAPAG SDGEDGGRRD FVEAPPPKVN PWTKHAPPPA AVNGQPPPEP
     SAPAKVVRAA APKPRKGSKV GDFGDAVNWP TPGEIAHKSV QPQSHKPQPA RKLPPKKDMK
     EQEKGDGSDS KESPKTKSDE SGEEKNGDED CQRGGQKKKG NKHKWVPLQI DMKPEVPREK
     LASRPTRPQE PRHTPAVRGE MKGSEPATYM PVSVAPPTPA WQPETKVEPA WHDQDETSSV
     KSDGAGGARA SFRGRGRGRG RGRGRGRGGT RTHFDYQFGY RKFDGTEGPR THKYMNNITY
     YFDNVSSNEI YSMDQELLKD YIKRQIEYYF SVDNLERDFF LRRKMDADGF LPITLIASFH
     RVQALTTDIS LIFAALKDSK VVEMVEEKVR RREEPEKWPL PGPPIVDYSQ TDFSQLLNCP
     EFVPRQHYQK ETESAPGSPR AVTPVPTKTE EVSNLKTLPK GLSASLPDLD SESWIEVKKR
     PRPSPARPKK PEEPRFSHPT ALPQQLPSQQ LMSKDQDEQE ELDFLFDEEM EQMDGRKNTF
     TAWSEEDSDY EIDDRDVNKI LIVTQTPPYM RRHPGGDRTG NHTSRAKMSA ELAKVINDGL
     FYYEQDLWTE KFEPEYSQIK QEVENFKKVN MISREQFDTL TPEPPVDPNQ EVPPGPPRFQ
     QVPTDALANK LFGAPEPSTI ARSLPTTVPE SPNYRNARTP RTPRTPQLKD SSQTPRFYPV
     VKEGRTLDAK MPRKRKTRHS SNPPLESHVG WVMDSREHRP RTASISSSPS EGTPAVGSYG
     CTPQSLPKFQ HPSHELLKEN GFTQHVYHKY RRRCLNERKR LGIGQSQEMN TLFRFWSFFL
     RDHFNKKMYE EFKQLALEDA KEGYRYGLEC LFRYYSYGLE KKFRLDIFKD FQEETVKDYE
     AGQLYGLEKF WAFLKYSKAK NLDIDPKLQE YLGKFRRLED FRVDPPMGEE GNHKRHPVVA
     GGSGEGRKRC PSQSSSRPAT GISQPPTTPT GQATREDAKW TSQHSDTLTL RK
//
ID   Q6ZQ70_MOUSE            Unreviewed;       647 AA.
AC   Q6ZQ70;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-JAN-2011, entry version 27.
DE   SubName: Full=MKIAA0683 protein;
DE   Flags: Fragment;
GN   Name=Telo2; Synonyms=mKIAA0683;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
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DR   EMBL; AK129189; BAC97999.1; -; Transcribed_RNA.
DR   IPI; IPI00460721; -.
DR   UniGene; Mm.288702; -.
DR   STRING; Q6ZQ70; -.
DR   Ensembl; ENSMUST00000115180; ENSMUSP00000110834; ENSMUSG00000024170.
DR   MGI; MGI:1918968; Telo2.
DR   HOVERGEN; HBG108557; -.
DR   ArrayExpress; Q6ZQ70; -.
DR   Bgee; Q6ZQ70; -.
DR   Genevestigator; Q6ZQ70; -.
DR   InterPro; IPR019337; Telomere_length_regulation_dom.
DR   Pfam; PF10193; Telomere_reg-2; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   647 AA;  71918 MW;  3C80FC2384C41C90 CRC64;
     RRTLFCRMDP ALSAVRLTVQ EAIHTLSSSE DAGHILSTLG TLKRYLGGTE DPVLPEEKEE
     FATVHFSAVL RCLVSKLSPG WLELSPGGQL ERLWESFFLD GPPDQAFLVL MEAIESTAGP
     SFRLMKMAQL LDTFLSTGRV AALMEEQCRP QTKPSFPLFQ ETLLSKVVGL PDLLGNCLQR
     DNLTQFFPQN YFPLLGQEVV QALKAVVNFL QGGLDCSVSF VSRVLGKVCI QGRKREILSV
     LVPQLTVLTQ DSCLWQRVCW RLVEQVPDRA VEAVLTGLVE AAPRPEVLSR LLGNLVVKNK
     KARFVVTRKL LLLQYQHTEL LASMMAGVKC RLDSSLPPVR RLGMIVAEVI SSRIHPEGPL
     LKFQYEDDEM SRELLALATP EPAGDCSSVS RGPSPAPADT EPPVEMPEKA VESDVPPTQP
     QGSDSELDSD DEFIPYDMSG DRELKNSKEP LYIRDCVEAL TTSEDMERWE ASLKGLEGLV
     YRSPAATREV SVELAKVLLH LEEKTCVAEF EQLRQSALVA VTVTDPEQVA KYLTSQFYGL
     NYSLRQRMDI LDVLVLAAQA LSRPKSLQRR SQHGSLVPGT MCSPALAVSQ TGNVAAPDWQ
     MVVEERIRSK TRRFSKGCPQ RELSGVPNEF SSVAGYFFFP LLQHFDR
//
ID   Q6ZQ80_MOUSE            Unreviewed;      1023 AA.
AC   Q6ZQ80;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 30.
DE   SubName: Full=MKIAA0629 protein;
DE   Flags: Fragment;
GN   Name=Akap11; Synonyms=mKIAA0629;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
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DR   EMBL; AK129178; BAC97988.1; -; mRNA.
DR   IPI; IPI00849717; -.
DR   UniGene; Mm.89413; -.
DR   PhosphoSite; Q6ZQ80; -.
DR   Ensembl; ENSMUST00000123853; ENSMUSP00000116015; ENSMUSG00000022016.
DR   MGI; MGI:2684060; Akap11.
DR   eggNOG; roNOG08432; -.
DR   GeneTree; ENSGT00530000063606; -.
DR   HOVERGEN; HBG050471; -.
DR   OrthoDB; EOG4ZW594; -.
DR   Bgee; Q6ZQ80; -.
DR   Genevestigator; Q6ZQ80; -.
DR   InterPro; IPR008382; SPHK1-interactor_AKAP_110.
DR   PANTHER; PTHR10226; AKAP_110; 1.
PE   1: Evidence at protein level;
FT   NON_TER       1      1
SQ   SEQUENCE   1023 AA;  112286 MW;  80A4690C23B01C7A CRC64;
     NTVARFAADL AEELVFEGIM EVCQFSCPQT PASSQCQSFD FEDKVVKSYA KDLSESVIQE
     AFIELSQTNV TFTTKAAVNV SMGNVKYVSA ESVSPTQTFT FSSSFSGQAV MMTKPMQEHK
     KEYTVQQALF CTSGIVTSIP VPLAGSALLP YHMSSTLYPS KCLSSEPSKA SGGSTQEHIA
     IERSAEEVDC LRSTCLPSEL NPCNQNDFKP TNGDIDRQSP SKLMSGPVII SNFSAAMVHT
     IVNETLESMT SFKATKTIDT NADYLTKTIK GKACSPSLCD QAAPQENKAS SKDMFAEQLS
     KSIIKHSLDK SKSMLPNRDK KPGSKEHVLV LGEESQMTLG ETPKFLDFSD NSPHRSLLVG
     NYCVAECKDS VGFGFSLEAL PPCSMMTNQK SDLKEVVKDK EVTRHNLNNT ALEPMPFGQE
     SSFRHSQTFS SAVLTCVDGL HEEDKQKIRD RNVIPDTPPS TPLVPSQTSS EWDIKTLSKQ
     LKGELAKEFA PATPPSTPHN SSVGSLSENE QTTIEKEEFM LKLMRSLSEE VESSEGEEHP
     GMHVKAEHPG KKVQFAEAFA THIISLATEA AASHLDHETT QEFKVQNPHL NVPSQRNVLP
     ALSHSDESIQ TCTFASDMAA DVIAEAEKIA NARSCMLFRH ERNICHVEGG RGKAEEKLDV
     EDVAHPREVD TCVLSLPSGM PGLTYKYPSC ESVTDEYAGH VIQVLQQQGG SGELIMEQYA
     SRLAYRSVTA AAREAAKTVK MKCGSKLFPL HGCHGKTNKE LLVFSSKERH QEVDRQRKRN
     GSHLCKYQTC ERTQDPCRNE LSELYSFSAS LASSITRDAK KQLTAPKVDL PKSSTDGCFF
     EKSECVDSSE NVTGPERSKS CQPLQSHGFC QNTGYLSGYS CAENAQAIEQ YARKVVGDTL
     ELSLGPTVFH NSETTASADR ITYAEKLSPL INEACRYCDL KEFHGCTRNS AQLFSKQSPC
     ASAKPSSRSK LSSIRQKSRI FHLDVPQIHV NLDKRAVLAE KIVAEAIEKA ERMCVCVCAC
     VRG
//
ID   UBP34_MOUSE             Reviewed;        3582 AA.
AC   Q6ZQ93; A2AF26; A2AF27; A2AF77; Q3UF93; Q3UPN0; Q6P563; Q7TMJ6;
AC   Q8CCH0;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 3.
DT   08-FEB-2011, entry version 51.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 34;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 34;
DE   AltName: Full=Ubiquitin thiolesterase 34;
DE   AltName: Full=Ubiquitin-specific-processing protease 34;
GN   Name=Usp34; Synonyms=Kiaa0570, Murr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 225-639; 2096-2278 AND
RP   2437-3582 (ISOFORM 4).
RC   STRAIN=C57BL/6J; TISSUE=Ovary, Sympathetic ganglion, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2279-3582 (ISOFORM 3).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2346-2569 AND 3160-3376.
RC   STRAIN=C57BL/6, and Czech II; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   IDENTIFICATION.
RX   PubMed=9001233;
RA   Nabetani A., Hatada I., Morisaki H., Oshimura M., Mukai T.;
RT   "Mouse U2af1-rs1 is a neomorphic imprinted gene.";
RL   Mol. Cell. Biol. 17:789-798(1997).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2525, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2582, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-
CC       terminal Gly of ubiquitin. Involved in the processing of poly-
CC       ubiquitin precursors as well as that of ubiquinated proteins (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q6ZQ93-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZQ93-2; Sequence=VSP_035641, VSP_035642;
CC       Name=3;
CC         IsoId=Q6ZQ93-3; Sequence=VSP_035641, VSP_035642, VSP_020465;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q6ZQ93-4; Sequence=VSP_035641, VSP_035642, VSP_020464;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH55938.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=CAM20294.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AL672049; CAM16931.1; -; Genomic_DNA.
DR   EMBL; AL672049; CAM16940.1; -; Genomic_DNA.
DR   EMBL; AL672004; CAM16940.1; JOINED; Genomic_DNA.
DR   EMBL; AL772359; CAM16940.1; JOINED; Genomic_DNA.
DR   EMBL; AL928722; CAM16940.1; JOINED; Genomic_DNA.
DR   EMBL; AL672004; CAM17339.1; -; Genomic_DNA.
DR   EMBL; AL672004; CAM17340.1; -; Genomic_DNA.
DR   EMBL; AL672049; CAM17340.1; JOINED; Genomic_DNA.
DR   EMBL; AL772359; CAM17340.1; JOINED; Genomic_DNA.
DR   EMBL; AL928722; CAM17340.1; JOINED; Genomic_DNA.
DR   EMBL; AL772359; CAM20294.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL672004; CAM20294.1; JOINED; Genomic_DNA.
DR   EMBL; AL672049; CAM20294.1; JOINED; Genomic_DNA.
DR   EMBL; AL928722; CAM20294.1; JOINED; Genomic_DNA.
DR   EMBL; AL928722; CAO77877.1; -; Genomic_DNA.
DR   EMBL; AL672004; CAO77877.1; JOINED; Genomic_DNA.
DR   EMBL; AL672049; CAO77877.1; JOINED; Genomic_DNA.
DR   EMBL; AL772359; CAO77877.1; JOINED; Genomic_DNA.
DR   EMBL; AK033182; BAC28186.1; -; mRNA.
DR   EMBL; AK143407; BAE25365.1; -; mRNA.
DR   EMBL; AK148805; BAE28668.1; -; mRNA.
DR   EMBL; AK129165; BAC97975.1; -; mRNA.
DR   EMBL; BC055938; AAH55938.1; ALT_SEQ; mRNA.
DR   EMBL; BC063062; AAH63062.1; -; mRNA.
DR   IPI; IPI00649643; -.
DR   IPI; IPI00668474; -.
DR   IPI; IPI00788320; -.
DR   IPI; IPI00914688; -.
DR   UniGene; Mm.119155; -.
DR   ProteinModelPortal; Q6ZQ93; -.
DR   SMR; Q6ZQ93; 1914-2303.
DR   PhosphoSite; Q6ZQ93; -.
DR   PRIDE; Q6ZQ93; -.
DR   Ensembl; ENSMUST00000070402; ENSMUSP00000067347; ENSMUSG00000056342.
DR   Ensembl; ENSMUST00000101465; ENSMUSP00000099007; ENSMUSG00000056342.
DR   MGI; MGI:109473; Usp34.
DR   eggNOG; roNOG10220; -.
DR   GeneTree; ENSGT00600000084366; -.
DR   HOVERGEN; HBG092616; -.
DR   InParanoid; Q6ZQ93; -.
DR   BRENDA; 3.1.2.15; 244.
DR   ArrayExpress; Q6ZQ93; -.
DR   Bgee; Q6ZQ93; -.
DR   CleanEx; MM_USP34; -.
DR   Genevestigator; Q6ZQ93; -.
DR   GermOnline; ENSMUSG00000056342; Mus musculus.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:EC.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; 1.
DR   PROSITE; PS50235; UCH_2_3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; Phosphoprotein; Protease;
KW   Thiol protease; Ubl conjugation pathway.
FT   CHAIN         1   3582       Ubiquitin carboxyl-terminal hydrolase 34.
FT                                /FTId=PRO_0000249520.
FT   ACT_SITE   1940   1940       Nucleophile (By similarity).
FT   ACT_SITE   2201   2201       Proton acceptor (By similarity).
FT   MOD_RES     352    352       Phosphoserine (By similarity).
FT   MOD_RES     355    355       Phosphoserine (By similarity).
FT   MOD_RES     684    684       Phosphoserine (By similarity).
FT   MOD_RES    1540   1540       Phosphoserine (By similarity).
FT   MOD_RES    2525   2525       Phosphoserine.
FT   MOD_RES    2582   2582       Phosphothreonine.
FT   MOD_RES    3395   3395       Phosphoserine (By similarity).
FT   MOD_RES    3396   3396       Phosphoserine (By similarity).
FT   MOD_RES    3418   3418       Phosphothreonine (By similarity).
FT   MOD_RES    3443   3443       Phosphoserine (By similarity).
FT   VAR_SEQ       1    151       Missing (in isoform 2, isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_035641.
FT   VAR_SEQ     152    160       DEKEKLLLC -> MRRKNYYYV (in isoform 2,
FT                                isoform 3 and isoform 4).
FT                                /FTId=VSP_035642.
FT   VAR_SEQ    2569   3582       Missing (in isoform 4).
FT                                /FTId=VSP_020464.
FT   VAR_SEQ    3124   3206       Missing (in isoform 3).
FT                                /FTId=VSP_020465.
FT   CONFLICT   2163   2163       K -> Q (in Ref. 2; BAE25365).
SQ   SEQUENCE   3582 AA;  408214 MW;  27BA0032ED7E06A2 CRC64;
     MCENCADLVE VLNEISDIEG GDGLQLRKEH TLKIFAYINS WTQRQCLCCF KEYKHLEIFN
     QVVCALINLV IAQVQVLRDQ LCKHCTTINI DSTWQDESNQ AEEPLSIDRE CNEGNTERQK
     SIEKKSNSTR TCNLTEEESS KSSDPFSLWN TDEKEKLLLC VAKIFQIQFP LYTAYKHNTH
     PTIEDISTQE SNILGAFCDM NDVEVPLHLL RYVCLFCGKN GLSLMKDCFE YGTPETLPFL
     IAHAFITVVS NIRIWLHIPA VMQHIIPFRT YVIRYLCKLS DQELRQSAAR NMADLMWSTV
     KEPLDTTLCF DKESLDLAFK YFMSPTLTMR LAGLSQITNQ LHTFNDVCNN ESLVSDTETS
     IAKELADWLI SNNVVEHIFG PNLHIEIIKQ CQVILNFLAA EGRLSTQHID CIWAAAQLKH
     CSRYIHDLFP SLIKNLDPVP LRHLLNLVSA LEPGVHTEQT LYLASMLIKA LWNNALAAKA
     QLSKQSSFAS LLNTNMPIGN KKEEEELRRA APSPWSPAAS PQSSDNSDTH QSGASDIEMD
     EQLINRNKHV QQRLSDTEES MQGSSDETAN SGEDGSSGPG SSSGHSDGSS NEVNSSHASQ
     SAGSPGSEVQ SEDIADIEAL KEEEEEEEEE EEEEEEEDDE EEEDEEEDDD DDDDHGHNPA
     KNTCGTELRN RKLENPAGIC LGESQGTSER NGTNSGTGKD LVFNTEPLPS VDNRIRMLDA
     CAHSEDPEHG ISGEVSSAHL AQGSQEACIT RSGDFLGETI GNELFNCRQF IGPQHHHHHH
     HHHHHHHHHH HHHHHHHDGH MVDDMLSADD VSCSSSQVSA KSEKNMADFD GEESGCEEEL
     VQINSHAELT SHLQQHLPNL ASIYHEHLSQ GPAVHKHQFS SNAVTDINLD NVCKKGNTLL
     WDIVQDDDAI NLSEGLINEA EKLLCSLVCW FTDRQIRMRF IEGCLENLGN NRSVVISLRL
     LPKLFGTFQQ FGSSYDTHWI TMWAEKELNM MKLFFDNLVY YIQGIREGRQ KHALYSHSAE
     VQVRLQFLTC VFSTLGSPDH FRLSLEQVDI LWHCLVEDSE CYDDALHWFL NQVRSKDQHA
     MGMETYKHLF LEKMPQLKPE TISMTGLNLF QHLCNLARLA TSAYDGGSNS ELCGMDQFWG
     IALRAQSGDV SRAAIQYINS YYINGKTGLE KEQEFISKCM ESLMIASSSL EQESHSSLTV
     IERGLLMLKT HLEAFRRRFA YHLRQWQIEG TGISSHLKAL SDKQSLPLRV VCQPAGLPDK
     MTIEMYPSDQ VADLRAEVTH WYENLQKEQI NQQAQLQEFG QSSRKGEFPG GLMGPVRMIS
     SGHELTTDYD EKALHELGFK DMQMVFVSLG APRRERKGEG VQLPASCLPP PQKDNIPMLL
     LLQEPHLTTL FDLLEMLASF KPPSGKVAVD DSESLKCEEL HLHAENLSRR VWELLMLLPT
     CPNMLTAFQN VSDEQSNDGL NWKELLKIKS AHKLLYALEI IEALGKPNRR IRRESTGSYS
     DLYPDSDDSS EDQVENSKNS WTCKFVAAGG LQQLLEIFNS AILEPKEQES WTVWQLDCLA
     CLLKLICQFA VDPSDLDLAY HDVFAWSGIA ESHRKRTWPG KSRKAAGDHA KSLHIPRLTE
     VFLVLVQGTS LIQRLMSVAY TYDNLAPRVL KAQSDHRSRH EVSHYSMWLL VSWAHCCSLV
     KSSLADSDHL QDWLKQLTLL IPETAVRHES CNGLYKLSLS GLDGGDSIHR SFLLLAASTL
     LKFLPDAQAL KPPRIDDYEE EPLLKPGCKE YFWLLCKLVD NIHIKDASQT TLLDLDALAR
     HLADCIRSRE ILDHLDGSIE DDGLSGLLRL ATSVIKHKPP FKFSREGQEF LRDIFNLLFL
     LPSLKDRRQP KCKSHSCRAA AYDLLVEMVK GSVENYRLIH NWVMAQHMQS HAPYKWDYWP
     HEDVRAECRF VGLTNLGATC YLASTIQQLY MIPEARQAVF TAKYSEDMKH KTTLLELQKM
     FTYLMESECK AYNPRPFCKT YTMDKQPLNT GEQKDMTEFF TDLITKVEEM SPELKNTVKS
     LFGGVITNNV VSLDCEHVSQ TAEEFYTVRC QVADMKNIYE SLDEVTIKDT LEGDNMYTCS
     HCGKKVRAEK RACFKKLPRI LSFNTMRYTF NMVTMMKEKV NTHFSFPLRL DMTPYTEDFL
     MGKSDRKEGF KDVGDRSKDT ESYEYDLIGV TVHTGTADGG HYYSFIRDIV NPHAYKNNKW
     YLFNDAEVKP FDSAQLASEC FGGEMTTKTY DSVTDKFMDF SFEKTHSAYM LFYKRMEPEE
     ENGREYKFDV SSELLEWIWH DNMQFLQDKN IFEHTYFGFM WQLCSCIPST LPDPKAVSLM
     TAKLSTSFVL ETFIHSKEKP TMLQWIELLT KQFNNSQAAC EWFLDRMADD DWWPMQILIK
     CPNQIVRQMF QRLCIHVIQR LRPVHAHLYL QPGMEDGSDD MDASVEDIGG RSCVTRFVRT
     LLLIMEHGVK PHSKHLTEYF AFLYEFAKMG EEESQFLLSL QAISTMVHFY MGTKGPENPQ
     VEVLSEEEGE EEEEEEDILS LAEEKYRPAA LEKMIALVAL LVEQSRSERH LTLSQTDMAA
     LTGGKGFPFL FQHIRDGINI RQTCNLIFSL CRYNNRLAEH IVSMLFTSIA KLTPEAANPF
     FKLLTMLMEF AGGPPGMPPF ASYILQRIWE VIEYNPSQCL DWLAVQTPRN KLAHSWVLQN
     MENWVERFLL AHNYPRVRTS AAYLLVSLIP SNSFRQMFRS TRSLHIPTRD LPLSPDTTVV
     LHQVYNVLLG LLSRAKLYVD AAVHGTTKLV PYLSFMTYCL ISKTEKLMFS TYFMDLWNLF
     QPKLSEPAIA TNHNKQALLS FWYNVCADCP ENIRLIVQNP VVTKNIAFNY ILADHDDQDV
     VLFNRGMLPA YYGILRLCCE QSPAFTRQLA SHQNIQWAFK NLTPHASQYP GAVEELFNLM
     QLFIAQRPDM REEELEDIKQ FKKTTISCYL RCLDGRSCWT TLISAFRILL ESDEDRLLVV
     FNRGLILMTE SFNTLHMMYH EATACHVTGD LVELLSIFLS VLKSTRPYLQ RKDVKQALIQ
     WQERIEFAHK LLTLLNSYSP PELRNACIDV LKELVLLSPH DFLHTLVPFL QHNHCTYHHS
     NIPMSLGPYF PCRENIKLIG GKSNIRPPRP ELNMCLLPTM VETSKGKDDV YDRMLLDYFF
     SYHQFIHLLC RVAINCEKFT ETLVKLSVLV AYEGLPLHLA LFPKLWTELC QTQSAMSKNC
     IKLLCEDPVF AEYIKCILMD ERTFLNNNIV YTFMTHFLLK VQSQVFSEAN CASLISTLIT
     NLINQYQNLQ SDFTNRVEIS KASAALNGDL RALALLLSVH TPKQLNPALI PTLQELLNKC
     RTCLQQRNSL QEQEAKERKT KDDEGATPVK RRRVSSDEEH TVDSCIGDIK TETREVLTPT
     STSDNETRDS SIIDPGTEQD LPSPENSSVK EYRMEGPSSF SEDGSHIRSQ HAEEQSNNGR
     FDDCKEFKDH CSKDTTLAED ESEFPSTSIS AVLSDLADLR SCDGQALSSQ DPEAAVSLSC
     GHSRGLISHM QQHDILDTLC RTIESTIHVV TRISGKGNQA AS
//
ID   Q6ZQA5_MOUSE            Unreviewed;      1520 AA.
AC   Q6ZQA5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 32.
DE   SubName: Full=MKIAA0467 protein;
DE   Flags: Fragment;
GN   Name=Szt2; Synonyms=BC059842, mKIAA0467;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
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DR   EMBL; AK129152; BAC97962.2; -; Transcribed_RNA.
DR   IPI; IPI00662762; -.
DR   UniGene; Mm.415218; -.
DR   MINT; MINT-2791544; -.
DR   PhosphoSite; Q6ZQA5; -.
DR   Ensembl; ENSMUST00000048347; ENSMUSP00000043262; ENSMUSG00000033253.
DR   MGI; MGI:3033336; Szt2.
DR   GeneTree; ENSGT00390000018402; -.
DR   ArrayExpress; Q6ZQA5; -.
DR   Bgee; Q6ZQA5; -.
DR   Genevestigator; Q6ZQA5; -.
DR   GO; GO:0007417; P:central nervous system development; IMP:MGI.
DR   GO; GO:0043473; P:pigmentation; IMP:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   1520 AA;  167404 MW;  308F061003C697B7 CRC64;
     FVAAGQQPGG LHGEPPSAAW TWHNHEDRAE DAEGEVLTAS PQVPGSLEDS EGTPLISLPS
     LSQGGSQPGP NRGLSLMSSQ GSVDSDHLGY DGGSSGSDSE GPGETLGEKA LFTLRTPPGP
     APPQPSLPVL PGPSLPDFWL IVRILQDRVE VYAHARSLSR EDGGPGAECR HLQQFLVRRV
     GEICREVNQR LLLQDLHDSH VCNSLLVAES EEDLWRSETP FHSRQRAVLP SDDFAADESC
     APRGYLAATM QFVPGHFSCD VVWGTVIRVH SRLKMGPSMG VSRAIQALRS VLNAFSVVNR
     KNMFVYQERA TKAVYYLRLL ETSCSDRPWE GDTLPPSLAL SRSQEPISSE DSMAPRSPLD
     MASSRSSDAV RPVGQVDRHI QLLVHGVGQA GPEITDELVR VLRRRLDEAT LDIITVMLVR
     NCKLTPADVE FIQPPGSLPS EVLHLVLPPS CRPCLPALAW YLRQNLLTFL HSPKYTDSNS
     RNHFQHPLPA QGGLPDLDIY LYNKPGGQGT GGKGVACITL AFVEEGGTPI SLASWPPSSP
     GPPDPLREEE FEQLTQVIRC PNTLDSCSAQ DGSPRLRLDV WEKGNISIVQ LEEKLRAAAR
     QALADAIMEL RLLPASLCTE DIPPGSLKSG PLDTKSPACR ANTFPCTPVS GEPVTPPSKA
     GRRSFWDMLG SEPDVFSPCS PGQLGPAPRP AAQRHLLLLG RNFAQWRRPT QQAAKAVQRF
     ESGGDGSPGR SAPRQRLLLL EVTDKKLQLL TYNWAPDLGA ALGRALIRLV QWQNARAHLI
     SCLLSQKLGL FHHCGQLDFP MRDGKEPNPF LLPTMEVETL IRNASPPLSR EQGRLSGSSR
     GGGPLSLDTF PFDEALRDIT AARPSSTGGP APRPPDPVTY HGQQFLEIKM TERKELERQM
     KMENLFVTWQ QRSAPASMPI SAGELETLKQ SSRLVHYCAT ALLFDPAAWL HGPPETCAPS
     EGQRRPRPES GSGSREVPTS CESLDVPPPG AREEPWLKEL SLAFLQQYVQ YLQSIGFVLV
     PLRPPSPARS TSRLRAMAIL GTEGRGSFSC PKAKAEGSPK STSTPVTTYH LQRALPGGII
     LMELTFQGCY FCVKQFALEC SRIPMGQAVN SQLSLLFTEE CDKVRDLMHV HSFSYDFHLR
     LVHQHVLGAH LALRHGYHLT TFLQHFLAHH PDGPHFGRNH IYQGTLELPT PLIAAHQLYN
     YVADHASSYH MKPLRMARSG GPEHNEYALV SAWHSSGSYL DSEGLRHQDD FDVSLLVCHS
     AAPFEEQGEA ERHVLRLQFF VVLTSQRELF PRLTADMRRF RKPSRLPLEP ETPGSLVGSP
     REASGMMLAP GPAPLFPPLA AEVGMARARL AQLVRLAGGH CRRDTLWKRL FLLEPPGPDR
     LRLGGRLALA ELEELLEAVH AKSIADIDPQ LDCFLSMTVS WYQSLIKVLL SRFPQSCRHF
     QSPDLGTQYL VVLNQKFTDC FVLVFLDSHL GKTSLTVVFR EPFPVQPQDS ESPPAQLVST
     YHHLESVINT ACFTLWTRLL
//
ID   IGSF3_MOUSE             Reviewed;        1194 AA.
AC   Q6ZQA6; A0A4X9; Q7TPV3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Immunoglobulin superfamily member 3;
DE            Short=IgSF3;
DE   Flags: Precursor;
GN   Name=Igsf3; Synonyms=Kiaa0466;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C3H/He; TISSUE=Osteoblast;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 717-1194.
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1077, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- SIMILARITY: Contains 8 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97961.1; Type=Erroneous initiation;
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DR   EMBL; AK129151; BAC97961.1; ALT_INIT; mRNA.
DR   EMBL; BC052892; AAH52892.1; -; mRNA.
DR   EMBL; AK052454; BAC35000.1; -; mRNA.
DR   IPI; IPI00420589; -.
DR   RefSeq; NP_997088.2; NM_207205.2.
DR   UniGene; Mm.257997; -.
DR   UniGene; Mm.396180; -.
DR   UniGene; Mm.458336; -.
DR   ProteinModelPortal; Q6ZQA6; -.
DR   SMR; Q6ZQA6; 24-248, 283-325, 359-385, 418-452, 492-519, 685-786, 819-862, 888-919.
DR   STRING; Q6ZQA6; -.
DR   PRIDE; Q6ZQA6; -.
DR   Ensembl; ENSMUST00000043983; ENSMUSP00000048900; ENSMUSG00000042035.
DR   GeneID; 78908; -.
DR   KEGG; mmu:78908; -.
DR   UCSC; uc008qrg.1; mouse.
DR   CTD; 78908; -.
DR   MGI; MGI:1926158; Igsf3.
DR   eggNOG; roNOG08435; -.
DR   GeneTree; ENSGT00390000010278; -.
DR   HOGENOM; HBG447074; -.
DR   HOVERGEN; HBG107998; -.
DR   InParanoid; Q6ZQA6; -.
DR   OMA; VEFHDLV; -.
DR   OrthoDB; EOG4TXBR3; -.
DR   PhylomeDB; Q6ZQA6; -.
DR   NextBio; 349722; -.
DR   Bgee; Q6ZQA6; -.
DR   CleanEx; MM_IGSF3; -.
DR   Genevestigator; Q6ZQA6; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 9.
DR   Pfam; PF07686; V-set; 6.
DR   SMART; SM00409; IG; 8.
DR   PROSITE; PS50835; IG_LIKE; 8.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW   Phosphoprotein; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     19       Potential.
FT   CHAIN        20   1194       Immunoglobulin superfamily member 3.
FT                                /FTId=PRO_0000320135.
FT   TOPO_DOM     20   1124       Extracellular (Potential).
FT   TRANSMEM   1125   1145       Helical; (Potential).
FT   TOPO_DOM   1146   1194       Cytoplasmic (Potential).
FT   DOMAIN       20    138       Ig-like C2-type 1.
FT   DOMAIN      143    262       Ig-like C2-type 2.
FT   DOMAIN      276    386       Ig-like C2-type 3.
FT   DOMAIN      401    539       Ig-like C2-type 4.
FT   DOMAIN      545    661       Ig-like C2-type 5.
FT   DOMAIN      676    803       Ig-like C2-type 6.
FT   DOMAIN      813    945       Ig-like C2-type 7.
FT   DOMAIN      949   1097       Ig-like C2-type 8.
FT   MOTIF       250    252       EWI motif.
FT   MOD_RES     617    617       Phosphothreonine (By similarity).
FT   MOD_RES     625    625       Phosphoserine (By similarity).
FT   CARBOHYD     43     43       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    418    418       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    842    842       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1077   1077       N-linked (GlcNAc...).
FT   DISULFID     42    120       By similarity.
FT   DISULFID    167    246       By similarity.
FT   DISULFID    302    376       By similarity.
FT   DISULFID    432    511       By similarity.
FT   DISULFID    566    645       By similarity.
FT   DISULFID    701    782       By similarity.
FT   DISULFID    838    918       By similarity.
FT   DISULFID    974   1080       By similarity.
FT   CONFLICT    523    523       E -> G (in Ref. 2; AAH52892).
FT   CONFLICT    800    800       E -> D (in Ref. 2; AAH52892).
SQ   SEQUENCE   1194 AA;  134710 MW;  2A76F53A8B1FD3C3 CRC64;
     MKCFFPVLSC LAVLGVVSAQ RQVTVQEGPL YRTESSHITI WCNVSGYQGP SEQNFQWSIY
     LPSAPEREVQ IVSTVDSSFP YAIYTQRVRG GKIYVERIQG NSALLHITDL QARDAGEYEC
     HTPNTDERYF GSYSAKMNLV VIPDSLQTTA VPQTLHKVEQ DPLELSCEVA TETVQHTHLS
     VSWLRQKGGE NPVEVISLSR DFILHSSSEY AQRQSLGEVR LDKLGRSTFR LTIFHLQPSD
     QGEFYCEAAE WIQDPDGSWY AMTRKRSEGA VVNVQPTDKE FTVRLETDKR LHTVGEPVEF
     RCILEAQNIP DRYFAVSWAF NSSLIATMGP NAVPVLNSDF AHREAKGQLK VAKESDGVFV
     LKIYHLRQED SGKYNCRVTE REKTVTGEFI DKESKRPKNI PIVVLPLKSS ISVEVASNAS
     VVLEGEDLHF SCTVRTVGRL QARFSVIWQL VDRQNRRSNV MWLDRDGTLQ PGSAYWERSS
     YGGIQMEQVQ PNSFSLGIFN SRKEDEGQYE CHVTEWVRAV DGEWQIVGER RASTLVSITA
     LETGFAVTAI SRTPGVTYSD SFDLQCIIKP HYPARVPVSV TWRFQPVGTV EFHDLVTFTR
     DGGVQWGDKS STFRTRTAIE KAESSNNVRL SISRASDTEA GKYQCVAELW RRNYNNTWTR
     LAERTSNLLE IRVLQPVTKL QVSKSKRTLT LVENRAIQLN CSVKSQTSPN SHFAVLWYVH
     KPSDADGKLI LKTTHSSAFE YGTYAEEEGL RGRLQFERHV SGGLFSLTVQ RAEVSDSGSY
     YCHVEEWLLS PNYAWYKLAE EVSGRTEVTV KQPDSRLKLS QVQGSLSVLE TRQIQLECVV
     LNRTSVASQL LVEWFVWKPN HPEREVVAHL SRDATFHYGE QAAKNNLKGR LHAESPSSGV
     YRLFIQNVAV QDSGTYSCRV EEWLPSPSGV WYKRAEDTAG QTAVTVMRPD AALQVDTVVP
     NATVTEKAAF QLDCSILSRS SQDSRFAVAW YSLRTKGGGK RGSLGIDEQE EEEEEEDISQ
     EEDSEDPTER TVLLSVGPDA VFGPEGSPWE GRLRFQRLSP LLYRLTVLEA SPQDTGNYSC
     HVEEWLPSPQ KEWYRLTEEE SAPIGIRVLD TSSTLQSLIC SNDALFYFVF FYPFPIFGIL
     IITILLVRFK SRNSSKNSEG KNGVPLLWIK EPHLNYSPTC LEPPVLSIHP GAID
//
ID   VIP2_MOUSE              Reviewed;        1129 AA.
AC   Q6ZQB6; Q3TM75; Q3UUA3; Q7TPU4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2;
DE            EC=2.7.4.21;
DE            EC=2.7.4.24;
DE   AltName: Full=Diphosphoinositol pentakisphosphate kinase 2;
DE   AltName: Full=Histidine acid phosphatase domain-containing protein 1;
DE   AltName: Full=InsP6 and PP-IP5 kinase 2;
DE   AltName: Full=VIP1 homolog 2;
DE            Short=mmVIP2;
GN   Name=Ppip5k2; Synonyms=Hisppd1, Kiaa0433, Vip2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Lung, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-1129 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, ENZYME ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=17690096; DOI=10.1074/jbc.M704656200;
RA   Fridy P.C., Otto J.C., Dollins D.E., York J.D.;
RT   "Cloning and characterization of two human VIP1-like inositol
RT   hexakisphosphate and diphosphoinositol pentakisphosphate kinases.";
RL   J. Biol. Chem. 282:30754-30762(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1066, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223 AND SER-226, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Bifunctional inositol kinase that catalyzes the
CC       formation of diphosphoinositol pentakisphosphate (InsP7 or PP-
CC       InsP5) and bi-diphosphoinositol tetrakisphosphate (InsP8 or PP2-
CC       InsP4). Converts inositolitol hexakisphosphate (InsP6) to InsP7.
CC       Also able to convert InsP7 to InsP8. Probably specifically
CC       mediates the formation of 4PP-InsP5 and 6PP-InsP5 InsP7 isomers
CC       but not of 5PP-IP5 InsP7 isomer.
CC   -!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol hexakisphosphate = ADP +
CC       5-diphospho-1D-myo-inositol (1,2,3,4,6)pentakisphosphate.
CC   -!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 1,3,4,5,6-
CC       pentakisphosphate = ADP + diphospho-1D-myo-inositol
CC       tetrakisphosphate (isomeric configuration unknown).
CC   -!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 5-diphosphate
CC       pentakisphosphate = ADP + 1D-myo-inositol bisdiphosphate
CC       tetrakisphosphate (isomeric configuration unknown).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.23 uM for InsP6;
CC         KM=0.54 uM for InsP7;
CC         Vmax=1.70 nmol/min/mg enzyme with InsP6 as substrate;
CC         Vmax=5.23 nmol/min/mg enzyme with InsP7 as substrate;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6ZQB6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZQB6-2; Sequence=VSP_030637, VSP_030638;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family. VIP1
CC       subfamily.
CC   -!- CAUTION: Although related to histidine acid phosphatases, it lacks
CC       the conserved active sites, suggesting that it has no phosphatase
CC       activity.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH53396.1; Type=Erroneous initiation;
CC       Sequence=BAC97950.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK129140; BAC97950.1; ALT_INIT; mRNA.
DR   EMBL; AK138622; BAE23724.1; -; mRNA.
DR   EMBL; AK166095; BAE38567.1; -; mRNA.
DR   EMBL; BC053396; AAH53396.1; ALT_INIT; mRNA.
DR   IPI; IPI00420593; -.
DR   IPI; IPI00882083; -.
DR   RefSeq; NP_776121.3; NM_173760.4.
DR   UniGene; Mm.220817; -.
DR   UniGene; Mm.417682; -.
DR   ProteinModelPortal; Q6ZQB6; -.
DR   SMR; Q6ZQB6; 519-592.
DR   PhosphoSite; Q6ZQB6; -.
DR   PRIDE; Q6ZQB6; -.
DR   Ensembl; ENSMUST00000042509; ENSMUSP00000043401; ENSMUSG00000040648.
DR   GeneID; 227399; -.
DR   KEGG; mmu:227399; -.
DR   UCSC; uc007cfj.1; mouse.
DR   CTD; 227399; -.
DR   MGI; MGI:2142810; Ppip5k2.
DR   HOVERGEN; HBG108657; -.
DR   OrthoDB; EOG41VK25; -.
DR   BRENDA; 2.7.4.21; 244.
DR   BRENDA; 2.7.4.24; 244.
DR   NextBio; 378596; -.
DR   ArrayExpress; Q6ZQB6; -.
DR   Bgee; Q6ZQB6; -.
DR   CleanEx; MM_HISPPD1; -.
DR   Genevestigator; Q6ZQB6; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0033857; F:diphosphoinositol-pentakisphosphate kinase activity; ISS:UniProtKB.
DR   GO; GO:0000827; F:inositol 1,3,4,5,6-pentakisphosphate kinase activity; ISS:UniProtKB.
DR   GO; GO:0000832; F:inositol hexakisphosphate 5-kinase activity; ISS:UniProtKB.
DR   GO; GO:0006020; P:inositol metabolic process; ISS:UniProtKB.
DR   InterPro; IPR013651; ATP-grasp_RimK-type.
DR   InterPro; IPR000560; His_Pase_superF_clade-2.
DR   Pfam; PF00328; Acid_phosphat_A; 1.
DR   Pfam; PF08443; RimK; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR   PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Transferase.
FT   CHAIN         1   1129       Inositol hexakisphosphate and
FT                                diphosphoinositol-pentakisphosphate
FT                                kinase 2.
FT                                /FTId=PRO_0000315693.
FT   MOD_RES      44     44       Phosphoserine (By similarity).
FT   MOD_RES     223    223       Phosphoserine.
FT   MOD_RES     226    226       Phosphoserine.
FT   MOD_RES     510    510       Phosphoserine (By similarity).
FT   MOD_RES    1058   1058       Phosphoserine (By similarity).
FT   MOD_RES    1066   1066       Phosphoserine.
FT   MOD_RES    1071   1071       Phosphothreonine (By similarity).
FT   VAR_SEQ     545    545       Missing (in isoform 2).
FT                                /FTId=VSP_030637.
FT   VAR_SEQ    1051   1129       SSMATRSSPGMRRKISLNTYTPTKILPTPPAALKSSKASSK
FT                                AAAGGPSQAMAPHTSSRMKSINSKTEGHEPKKSTGKKR ->
FT                                CMEFTFIVT (in isoform 2).
FT                                /FTId=VSP_030638.
FT   CONFLICT    197    197       A -> V (in Ref. 1; BAE38567).
FT   CONFLICT    582    582       A -> T (in Ref. 3; AAH53396).
FT   CONFLICT    729    729       I -> V (in Ref. 3; AAH53396).
FT   CONFLICT   1035   1035       S -> P (in Ref. 3; AAH53396).
FT   CONFLICT   1109   1109       M -> K (in Ref. 3; AAH53396).
SQ   SEQUENCE   1129 AA;  128430 MW;  A563826CC4D37E3C CRC64;
     MSNSRKMSEP PRFFVGPEDA EINPGNYRRF FHHAEEEEEE EDESPPERQI VVGICSMAKK
     SKSKPMKEIL ERISLFKYIT VVVFEEEIIL NEPVENWPLC DCLISFHSKG FPLDKAVAYA
     KLRNPFVIND LNMQYLIQDR RDVYSILQAE GILLPRYAIL NRDPNNPKEC NLIEGEDHVE
     VNGEVFQKPF VEKPVSAEDH NVYIYYPTSA GGGSQRLFRK IGSRSSVYSP ESNVRKTGSY
     IYEEFMPTDG TDVKVYTVGP DYAHAEARKS PALDGKVERD SEGKEVRYPV ILNAREKLIA
     WKVCLAFKQT VCGFDLLRAN GQSYVCDVNG FSFVKNSMKY YDDCAKILGN IVMRELAPQF
     HIPWSIPLEA EDIPIVPTTS GTMMELRCVI AVIRHGDRTP KQKMKMEVRH QKFFDLFEKC
     DGYKSGKLKL KKPKQLQEVL DIARQLLMEL GQNNDSEIEE NKSKLEQLKT VLEMYGHFSG
     INRKVQLTYL PHGCPKTSSE EEDNRREEPS LLLVLKWGGE LTPAGRVQAE ELGRAFRCMY
     PGGQGDYAGF PGCGLLRLHS TYRHDLKIYA SDEGRVQMTA AAFAKGLLAL EGELTPILVQ
     MVKSANMNGL LDSDSDSLSS CQQRVKARLH EILQKDRDFT AEDYEKLTPS GSISVIKSMH
     LIKNPVKTCD KVYSLIQSLT SQIRYRMEDP KSADIQLYHS ETLELMLRRW SKLEKDFKTK
     NGRYDISKIP DIYDCIKYDV QHNGSLKLEN TMELYRLSKA LADIVIPQEY GITKAEKLEI
     AKGYCTPLVR KIRSDLQRTQ DDDTVNKLHP VYSRGVLSPE RHVRTRLYFT SESHVHSLLS
     ILRYGALCDD SKDEQWKRAM DYLNVVNELN YMTQIVIMLY EDPNKDLSSE ERFHVELHFS
     PGAKGCEEDK NLPSGYGYRP ASRENEGRRS LKTDDDEPHT SKRDEVDRAV MLFKPLVSEP
     IHIHRKSPLP RSRKITANEV VSENANYLRT PRNLVEQKQN PTVGFELYSM VPSICPLETL
     HNALFLKQVD DFLASIASPS TEVLRKVPEM SSMATRSSPG MRRKISLNTY TPTKILPTPP
     AALKSSKASS KAAAGGPSQA MAPHTSSRMK SINSKTEGHE PKKSTGKKR
//
ID   Q6ZQB7_MOUSE            Unreviewed;       773 AA.
AC   Q6ZQB7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 38.
DE   SubName: Full=MKIAA0429 protein;
DE   SubName: Full=Metastasis suppressor 1, isoform CRA_d;
DE   Flags: Fragment;
GN   Name=Mtss1; Synonyms=mKIAA0429; ORFNames=mCG_116708;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK129139; BAC97949.1; -; mRNA.
DR   EMBL; CH466545; EDL29320.1; -; Genomic_DNA.
DR   IPI; IPI00460831; -.
DR   RefSeq; NP_001139652.1; NM_001146180.1.
DR   RefSeq; NP_659049.2; NM_144800.2.
DR   UniGene; Mm.215481; -.
DR   UniGene; Mm.394414; -.
DR   ProteinModelPortal; Q6ZQB7; -.
DR   STRING; Q6ZQB7; -.
DR   PRIDE; Q6ZQB7; -.
DR   Ensembl; ENSMUST00000036782; ENSMUSP00000040073; ENSMUSG00000022353.
DR   GeneID; 211401; -.
DR   KEGG; mmu:211401; -.
DR   UCSC; uc007vtz.1; mouse.
DR   CTD; 211401; -.
DR   MGI; MGI:2384818; Mtss1.
DR   eggNOG; roNOG10381; -.
DR   GeneTree; ENSGT00390000002637; -.
DR   HOVERGEN; HBG052530; -.
DR   OrthoDB; EOG4SJ5DB; -.
DR   PhylomeDB; Q6ZQB7; -.
DR   ArrayExpress; Q6ZQB7; -.
DR   Bgee; Q6ZQB7; -.
DR   Genevestigator; Q6ZQB7; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IDA:MGI.
DR   GO; GO:0008093; F:cytoskeletal adaptor activity; IEA:InterPro.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:InterPro.
DR   GO; GO:0030041; P:actin filament polymerization; IDA:MGI.
DR   GO; GO:0046847; P:filopodium assembly; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR013606; IRSp53/MIM_homology_IMD.
DR   InterPro; IPR003124; WH2_actin-bd.
DR   Gene3D; G3DSA:1.20.1270.80; IRSp53/MIM_homology_IMD; 1.
DR   Pfam; PF08397; IMD; 1.
DR   SMART; SM00246; WH2; 1.
DR   PROSITE; PS51338; IMD; 1.
DR   PROSITE; PS51082; WH2; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   773 AA;  83767 MW;  6ACFCDAC1357A887 CRC64;
     NRSRAERARP RAQCSRPESV SCPRRAGKME AVIEKECSAL GGLFQTIISD MKGSYPVWED
     FINKAGKLQS QLRTTVVAAA AFLDAFQKVA DMATNTRGGT REIGSALTRM CMRHRSIEAK
     LRQFSSALID CLINPLQEQM EEWKKVANQL DKDHAKEYKK ARQEIKKKSS DTLKLQKKAK
     KGRGDIQPQL DSALQDVNDK YLLLEETEKQ AVRKALIEER GRFCTFISML RPVIEEEISM
     LGEITHLQTI SEDLKSLTMD PHKLPSSSEQ VILDLKGSDY SWSYQTPPSS PSTTMSRKSS
     VCSSLNSVNS SDSRSSGSHS HSPSSHYRYR SSNLAQQAPV RLSSVSSHDS GFISQDAFQS
     KSPSPMPPEA ANQNSSSSAS SEASETCQSV SECSSPTSVS SGSTMGAWVS TEKDWAKPGP
     YDQPLVNTLQ RRKEKREPDS NGGGPTTTGG PPAGAEEAQR PRSMTVSAAT RPGEEMAACE
     ELTLALSRGL QLDVQRSSRD SLQCSSGYST QTTTPCCSED TIPSQGTRRP ACRPAFRAGP
     VSDYDYFSVS GDQEAEQQEF DKSSTIPRNS DISQSYRRMF QAKRPASTAG LPTTLGPAMV
     TPGVATIRRT PSTKPSVRRG TIGAGPIPIK TPVIPVKTPT VPDLPGVLPS PPDGPEERGE
     HSPESPSAGE GPQGVSNIPS SLWSGQAPVN PPLPGPKPSI PEEHRQAIPE SEAEDQERDP
     PSATVSPGPI PESDPADLSP RESPQGEDML NAIRRGVKLK KTTTNDRSAP RFS
//
ID   NU188_MOUSE             Reviewed;        1759 AA.
AC   Q6ZQH8; Q4VA15; Q80UL4; Q8C7A1; Q8R3F1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   08-MAR-2011, entry version 43.
DE   RecName: Full=Nucleoporin NUP188 homolog;
GN   Name=Nup188; Synonyms=Kiaa0169;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=B5/EGFP, FVB/N, and NMRI;
RC   TISSUE=Mammary tumor, and Trophoblast stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-798.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PROTEIN SEQUENCE OF 1061-1070, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: May function as a component of the nuclear pore complex
CC       (NPC).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex (Probable).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH25526.1; Type=Erroneous initiation;
CC       Sequence=BAC97883.1; Type=Erroneous initiation;
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DR   EMBL; AK129073; BAC97883.1; ALT_INIT; mRNA.
DR   EMBL; AL954388; CAM23164.1; -; Genomic_DNA.
DR   EMBL; BC025526; AAH25526.1; ALT_INIT; mRNA.
DR   EMBL; BC050199; AAH50199.1; -; mRNA.
DR   EMBL; BC096591; AAH96591.1; -; mRNA.
DR   EMBL; AK052272; BAC34911.1; -; mRNA.
DR   IPI; IPI00420602; -.
DR   RefSeq; NP_938046.2; NM_198304.2.
DR   UniGene; Mm.330119; -.
DR   STRING; Q6ZQH8; -.
DR   PhosphoSite; Q6ZQH8; -.
DR   PRIDE; Q6ZQH8; -.
DR   Ensembl; ENSMUST00000064447; ENSMUSP00000065836; ENSMUSG00000052533.
DR   GeneID; 227699; -.
DR   KEGG; mmu:227699; -.
DR   CTD; 227699; -.
DR   MGI; MGI:2446190; Nup188.
DR   GeneTree; ENSGT00390000005742; -.
DR   HOGENOM; HBG357560; -.
DR   HOVERGEN; HBG055598; -.
DR   InParanoid; Q6ZQH8; -.
DR   OMA; PYRVEYA; -.
DR   OrthoDB; EOG4HDSSM; -.
DR   PhylomeDB; Q6ZQH8; -.
DR   NextBio; 378764; -.
DR   ArrayExpress; Q6ZQH8; -.
DR   Bgee; Q6ZQH8; -.
DR   CleanEx; MM_NUP188; -.
DR   Genevestigator; Q6ZQH8; -.
DR   GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:UniProtKB-KW.
DR   InterPro; IPR018864; Nucleoporin.
DR   Pfam; PF10487; Nup188; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; mRNA transport;
KW   Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW   Translocation; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1759       Nucleoporin NUP188 homolog.
FT                                /FTId=PRO_0000299173.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      38     38       N6-acetyllysine (By similarity).
FT   MOD_RES    1718   1718       Phosphoserine (By similarity).
FT   MOD_RES    1719   1719       Phosphoserine (By similarity).
FT   MOD_RES    1727   1727       Phosphoserine (By similarity).
FT   CONFLICT    798    798       S -> R (in Ref. 4; BAC34911).
SQ   SEQUENCE   1759 AA;  196696 MW;  9067785281A0BF98 CRC64;
     MAAAAGGPCV RSSRELWTIL LGRSALRELN QIEAELNKYW QRLLEGLSYY KPPSPSSAER
     VKANKDVASP LKELGLRVSK FLGLDEEQSV QLLQCYLQED YRGTRDSLKT VLQDERQSQA
     LTLKIADYYY EERTCILRCV LHLLTYFQDE RHPYRAEYAD CVDKLEKELV LKYRQQFEEL
     YRTEAPTWET HGNLMTERQV SRWLVQCLRE QSMLLEIIFL YYAYFEMAPS DLLVLTKMFK
     EQGFGSRQTS RHLVGGTMDP FVDRIGYFSA LILVEGMDIE SLHKYALDDR RELHQFAQDG
     LICQDMDRAM LTLGDIPHHA PVLLAWALLR HTLSPEETSS VVRKIGGTAI QLNVFQYLTR
     LLRSLASGGN DCTTSTACMC VYGLLSFALT SLELHTLGNQ QDVIDTACEV LADPSLPELF
     WGTEPTSGLG IILDSVCGMF PHLLSPLLQL LRALVSGKST AKKVYSFLDK MSFYNELHKH
     KPHDVLSHED GTLWRRQTPK LLYPLGGQTN LRIPQGTVGQ VMLDDRAYLV RWEYSYSSWT
     LFTCEIEMLL HVVSTADVIQ HCQRVKPIID LVHKVISTDL SIADCLLPIT SRIYMLLQRL
     TTVISPPVNV IASCVNCLTV LAARNPAKVW TDLRHTGFLP FVAHPVSNMT QMISAEGMNA
     GGYGSLLMNS EQPQGEYGVT IAFLRLVTTL VKGQLGSTQS QGLVPCVMFV LKEMLPSYHK
     WRYNSHGVRE LIGCLILELI HAILNLCQET ELHSSHTPSL PSLCICSLAY TEAGQTVISI
     MGIGVDTIDM VMAAQPRSDG PEGQGQGQLL IKTVKLAFSV TNNVIRLKPP SNVVSPLEQA
     LTQHGAHGNN LIAVLAKYIY HRHDPALPRL AIQLLKRLAT VAPMSVYACL GSDAAAIRDA
     FLTRLQSKIE DMRIKVMILE FLTVAVETQP GLIELFLNLE VKDGSNGSKE FSLGVWSCLH
     VVLELIDSQQ QDRYWCPPLL HRAAIAFLHA LWQDRRDSAM LVLRTKPKFW ENLTSPLFGT
     LSPPSETSEP SVLETCALIM KIICLEIYYV VKGSLDQSLK DTLKKFSSEK RFAYWSGYVK
     SLAVYMADTE GSSCTSLLEY QMLVSAWRIL LIIAASHADV MHLTDMAVRR QLFLDVLDGT
     KALLLVAASV NCLRLGSMMC TLLLILLRQW KRELGAVEKI LGPLTEILEG VLQADQQLME
     KTKAKVFSAF ITVLQMKELR VGDIPQYSQL VLNVCETLQE EVIALFDQTR HSLASDSAAE
     DKDSMETDDC PRPRHKDQRD GVCVLGLHLA KELCEVDEDG DSWLQVTRRL PILPTLLTTL
     EVSLRMKQNL HFTEAALHLL LTLARTQQGA TAVAGAGITQ SICLPLLSVY QLSSNGTGQT
     PSTSRKSLDA PSWPGVYRLS MSLMERLLKT LRYNFLTEAL DFVGVHQERT LQCLNAVKTV
     QSLACLEEAD HTVGFILQLS HFRKEWHFHL PQLMRDVQVN LGYLCQACTS LLHSRKMLQH
     YLQNKNGDGL PSAVTPRAQR PSTTTTTTTT TTALATPAGC SSKQPTADTE ASEQRALHTV
     QYGLLKILSR TLAALRHFTP DVCQILLDQS LDLAEYNFLF ALSFTTPTFD SEVAPSFGTL
     LATVNVALNM LGELDKKKES LTQAVGLSTQ AEGTRTLKSL LMFTMENCFY LLISQAVRYL
     RDPAVHPRDK QRMKQELSSE LSTLLSSLSR YFRRGAPSSP AAGVLPSPQG KATSLSKASP
     ESQEPLIQLV QAFVRHVQR
//
ID   ACAP2_MOUSE             Reviewed;         770 AA.
AC   Q6ZQK5; Q3UHL4; Q811F3; Q9CTS8;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2;
DE   AltName: Full=Centaurin-beta-2;
DE            Short=Cnt-b2;
GN   Name=Acap2; Synonyms=Centb2, Kiaa0041;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 405-770.
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation
CC       factor 6 (ARF6) (By similarity).
CC   -!- ENZYME REGULATION: GAP activity stimulated by phosphatidylinositol
CC       4,5-bisphosphate (PIP2) and phosphatidic acid (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6ZQK5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZQK5-2; Sequence=VSP_052554;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 3 ANK repeats.
CC   -!- SIMILARITY: Contains 1 Arf-GAP domain.
CC   -!- SIMILARITY: Contains 1 BAR domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97851.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK129041; BAC97851.1; ALT_INIT; mRNA.
DR   EMBL; AK020591; BAB32141.3; -; mRNA.
DR   EMBL; AK147319; BAE27843.1; -; mRNA.
DR   EMBL; BC046455; AAH46455.1; -; mRNA.
DR   IPI; IPI00785394; -.
DR   IPI; IPI00867895; -.
DR   RefSeq; NP_084414.1; NM_030138.2.
DR   UniGene; Mm.274646; -.
DR   HSSP; Q8TDY4; 2B0O.
DR   ProteinModelPortal; Q6ZQK5; -.
DR   SMR; Q6ZQK5; 3-364, 400-726.
DR   STRING; Q6ZQK5; -.
DR   PRIDE; Q6ZQK5; -.
DR   Ensembl; ENSMUST00000058033; ENSMUSP00000061501; ENSMUSG00000049076.
DR   Ensembl; ENSMUST00000100008; ENSMUSP00000097587; ENSMUSG00000049076.
DR   GeneID; 78618; -.
DR   KEGG; mmu:78618; -.
DR   NMPDR; fig|10090.3.peg.31143; -.
DR   UCSC; uc007yxb.1; mouse.
DR   CTD; 78618; -.
DR   MGI; MGI:1925868; Acap2.
DR   eggNOG; roNOG12761; -.
DR   GeneTree; ENSGT00600000084109; -.
DR   HOGENOM; HBG314594; -.
DR   HOVERGEN; HBG050889; -.
DR   InParanoid; Q6ZQK5; -.
DR   OrthoDB; EOG48SGSK; -.
DR   PhylomeDB; Q6ZQK5; -.
DR   NextBio; 349208; -.
DR   ArrayExpress; Q6ZQK5; -.
DR   Bgee; Q6ZQK5; -.
DR   Genevestigator; Q6ZQK5; -.
DR   GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR001164; ArfGAP.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF57863; ArfGAP; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS51021; BAR; FALSE_NEG.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ANK repeat; Coiled coil; GTPase activation;
KW   Metal-binding; Phosphoprotein; Repeat; Zinc; Zinc-finger.
FT   CHAIN         1    770       Arf-GAP with coiled-coil, ANK repeat and
FT                                PH domain-containing protein 2.
FT                                /FTId=PRO_0000306385.
FT   DOMAIN        1    226       BAR.
FT   DOMAIN      266    361       PH.
FT   DOMAIN      399    520       Arf-GAP.
FT   REPEAT      632    661       ANK 1.
FT   REPEAT      665    694       ANK 2.
FT   REPEAT      698    727       ANK 3.
FT   ZN_FING     414    437       C4-type.
FT   MOD_RES     379    379       Phosphoserine (By similarity).
FT   MOD_RES     384    384       Phosphoserine (By similarity).
FT   MOD_RES     521    521       Phosphoserine.
FT   MOD_RES     734    734       Phosphotyrosine (By similarity).
FT   MOD_RES     742    742       Phosphotyrosine (By similarity).
FT   MOD_RES     767    767       Phosphoserine (By similarity).
FT   VAR_SEQ      78     95       Missing (in isoform 2).
FT                                /FTId=VSP_052554.
FT   CONFLICT    526    526       E -> K (in Ref. 3; AAH46455).
SQ   SEQUENCE   770 AA;  87211 MW;  8882864BB7D248F2 CRC64;
     MKMTVDFEEC LKDSPRFRAA LEEVEGDVAE LELKLDKLVK LCIAMIDTGK AFCVANKQFM
     NGIRDLAQYS SNDAVVETSL TKFSDSLQEM INFHTILFDQ TQRSIKAQLQ NFVKEDLRKF
     KDAKKQFEKV SEEKENALVK NAQVQRNKQH EVEEAANILT ATRKCFRHIA LDYVLQINVL
     QSKRRSEILK SMLSFMYAHL AFFHQGYDLF SELGPYMKDL GAQLDRLVVD AAKEKREMEQ
     KHSTIQQKDF SSDDSKLEYN VDAANGIVME GYLFKRASNA FKTWNRRWFS IQNNQLVYQK
     KFKDSPTVVV EDLRLCTVKH CEDIERRFCF EVVSPTKSCM LQADSEKLRQ AWIKAVQTSI
     ATAYREKGDE SEKLDKKSSP STGSLDSGNE SKEKLLKGES ALQRVQCIPG NTSCCDCGLA
     DPRWASINLG ITLCIECSGI HRSLGVHFSK VRSLTLDTWE PELLKLMCEL GNDVINRVYE
     AKLEKMGVKK PQPGQRQEKE AYIRAKYVER KFVDKYSALL SPSEQEKRII SKSCEDQRLS
     HARASVHTPV KSNDSGIQQC SEDGRESLPS TVSANSLYEP EGERQESSVF LDSKHLNPGL
     QLYRASYEKN LPKMAEALAH GADVNWANSD ENQATPLIQA VLGGSLVTCE FLLQNGANVN
     QRDVQGRGPL HHATVLGHTG QVCLFLKRGA NQHATDEEGK DPLSIAVEAA NADIVTLLRL
     ARMNEEMRES EGLYGQPGDE TYQDIFRDFS QMASNNPEKL NRFQQDSQKF
//
ID   RFFL_MOUSE              Reviewed;         377 AA.
AC   Q6ZQM0; Q5SVC2; Q5SVC4; Q9D543; Q9D9B1;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=E3 ubiquitin-protein ligase rififylin;
DE            EC=6.3.2.-;
DE   AltName: Full=RING finger and FYVE-like domain-containing protein 1;
DE            Short=Fring;
GN   Name=Rffl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J;
RA   Hong W.;
RT   "Fring, a protein with a modified FYVE domain and a RING domain.";
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15229288; DOI=10.1091/mbc.E04-04-0274;
RA   Coumailleau F., Das V., Alcover A., Raposo G., Vandormael-Pournin S.,
RA   Le Bras S., Baldacci P., Dautry-Varsat A., Babinet C.,
RA   Cohen-Tannoudji M.;
RT   "Over-expression of Rififylin, a new RING finger and FYVE-like domain-
RT   containing protein, inhibits recycling from the endocytic recycling
RT   compartment.";
RL   Mol. Biol. Cell 15:4444-4456(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Has E3 ubiquitin protein ligase activity. Regulates the
CC       levels of CASP8 and CASP10 by targeting them for proteasomal
CC       degradation. Has anti-apoptotic activity. May bind
CC       phosphatidylinositol phosphates (By similarity). Overexpression
CC       slows protein traffic through recycling endosomes.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Binds CASP8 and CASP10 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Membrane;
CC       Peripheral membrane protein. Note=Associated with perinuclear
CC       vesicles.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q6ZQM0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZQM0-2; Sequence=VSP_015753;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q6ZQM0-3; Sequence=VSP_015753, VSP_015754;
CC       Name=4;
CC         IsoId=Q6ZQM0-4; Sequence=VSP_015753, VSP_015754, VSP_015755,
CC                                  VSP_015756;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Detected in heart, brain, spleen,
CC       lung, liver, skeletal muscle, kidney, testis, thymus, whole embryo
CC       and embryonic stem cells.
CC   -!- PTM: Auto-ubiquitinated (in vitro) (By similarity).
CC   -!- PTM: Palmitoylated (By similarity).
CC   -!- PTM: Rapidly degraded after stimulation with TNFSF10, probably by
CC       caspases (By similarity).
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SIMILARITY: Contains 2 SAP domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF434814; AAL30769.1; -; mRNA.
DR   EMBL; AK007189; BAB24891.1; -; mRNA.
DR   EMBL; AK015806; BAB29984.1; -; mRNA.
DR   EMBL; AK028095; BAC25744.1; -; mRNA.
DR   EMBL; AK128983; BAC87665.1; -; mRNA.
DR   EMBL; AL645594; CAI25096.1; -; Genomic_DNA.
DR   EMBL; AL645594; CAI25097.1; -; Genomic_DNA.
DR   EMBL; AL645594; CAI25098.1; -; Genomic_DNA.
DR   IPI; IPI00317244; -.
DR   IPI; IPI00620212; -.
DR   IPI; IPI00875615; -.
DR   IPI; IPI00890329; -.
DR   RefSeq; NP_001007466.1; NM_001007465.3.
DR   RefSeq; NP_001158042.1; NM_001164570.1.
DR   RefSeq; NP_080373.1; NM_026097.3.
DR   UniGene; Mm.341608; -.
DR   ProteinModelPortal; Q6ZQM0; -.
DR   SMR; Q6ZQM0; 59-153, 325-377.
DR   STRING; Q6ZQM0; -.
DR   PhosphoSite; Q6ZQM0; -.
DR   PRIDE; Q6ZQM0; -.
DR   Ensembl; ENSMUST00000071152; ENSMUSP00000071150; ENSMUSG00000020696.
DR   Ensembl; ENSMUST00000093975; ENSMUSP00000091510; ENSMUSG00000020696.
DR   Ensembl; ENSMUST00000108169; ENSMUSP00000103804; ENSMUSG00000020696.
DR   Ensembl; ENSMUST00000108171; ENSMUSP00000103806; ENSMUSG00000020696.
DR   Ensembl; ENSMUST00000108173; ENSMUSP00000103808; ENSMUSG00000020696.
DR   GeneID; 67338; -.
DR   KEGG; mmu:67338; -.
DR   UCSC; uc007knh.1; mouse.
DR   UCSC; uc007kni.1; mouse.
DR   CTD; 67338; -.
DR   MGI; MGI:1914588; Rffl.
DR   GeneTree; ENSGT00390000012719; -.
DR   HOVERGEN; HBG055079; -.
DR   PhylomeDB; Q6ZQM0; -.
DR   NextBio; 324290; -.
DR   ArrayExpress; Q6ZQM0; -.
DR   Bgee; Q6ZQM0; -.
DR   Genevestigator; Q6ZQM0; -.
DR   GermOnline; ENSMUSG00000020696; Mus musculus.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; IDA:MGI.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 2.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS50800; SAP; FALSE_NEG.
DR   PROSITE; PS50178; ZF_FYVE; FALSE_NEG.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Cytoplasm; Ligase; Lipoprotein;
KW   Membrane; Metal-binding; Palmitate; Phosphoprotein; Repeat;
KW   Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    377       E3 ubiquitin-protein ligase rififylin.
FT                                /FTId=PRO_0000056026.
FT   DOMAIN      115    134       SAP 1.
FT   DOMAIN      264    278       SAP 2.
FT   ZN_FING      55    107       FYVE-type.
FT   ZN_FING     330    365       RING-type.
FT   MOD_RES      48     48       Phosphotyrosine (By similarity).
FT   MOD_RES     240    240       Phosphoserine (By similarity).
FT   MOD_RES     243    243       Phosphoserine (By similarity).
FT   MOD_RES     254    254       Phosphoserine.
FT   MOD_RES     256    256       Phosphoserine (By similarity).
FT   VAR_SEQ       1     14       Missing (in isoform 2, isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_015753.
FT   VAR_SEQ     211    238       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_015754.
FT   VAR_SEQ     318    335       GGAVPSGLEENLCKICMD -> ASHLLWEVFFDLMFHSYV
FT                                (in isoform 4).
FT                                /FTId=VSP_015755.
FT   VAR_SEQ     336    377       Missing (in isoform 4).
FT                                /FTId=VSP_015756.
FT   CONFLICT     52     52       P -> L (in Ref. 2; BAB29984).
SQ   SEQUENCE   377 AA;  42249 MW;  B0E9E87D446902D1 CRC64;
     MSQPSLWKDS HYFIMWASCC NWFCLDGQPE EAPPPQGART QAYSNPGYSS FPSPTGSEPS
     CKACGVHFAS TTRKQTCLDC KKNFCMTCSS QEGNGPRLCL LCLRFRATAF QREELMKMKV
     KDLRDYLSLH DISTEMCREK EELVFLVLGQ QPVISEADRT RVPHLPQAFP EQQAFLTQPQ
     TSTVPPTSPG LPSSPAQVTS VPLAQDQETQ QAVGHVSQDH EEPIFPESTA RVPTEDETQS
     VDSEDSFVPG RRASLSDLTH LEDIEGLTVR QLKEILARNF VNYKGCCEKW ELMERVTRLY
     KDQKGLQHLV SGNEDQNGGA VPSGLEENLC KICMDSPIDC VLLECGHMVT CTKCGKRMNE
     CPICRQYVIR AVHVFRS
//
ID   SYNE2_MOUSE             Reviewed;        6874 AA.
AC   Q6ZWQ0; Q640M5;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Nesprin-2;
DE   AltName: Full=Nuclear envelope spectrin repeat protein 2;
DE   AltName: Full=Nucleus and actin connecting element protein;
DE            Short=Protein NUANCE;
DE   AltName: Full=Synaptic nuclear envelope protein 2;
DE            Short=Syne-2;
GN   Name=Syne2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=18477613; DOI=10.1242/jcs.019075;
RA   Luke Y., Zaim H., Karakesisoglou I., Jaeger V.M., Sellin L., Lu W.,
RA   Schneider M., Neumann S., Beijer A., Munck M., Padmakumar V.C.,
RA   Gloy J., Walz G., Noegel A.A.;
RT   "Nesprin-2 Giant (NUANCE) maintains nuclear envelope architecture and
RT   composition in skin.";
RL   J. Cell Sci. 121:1887-1898(2008).
RN   [5]
RP   SUBCELLULAR LOCATION, INTERACTION WITH TMEM67, AND FUNCTION.
RX   PubMed=19596800; DOI=10.1242/jcs.043794;
RA   Dawe H.R., Adams M., Wheway G., Szymanska K., Logan C.V., Noegel A.A.,
RA   Gull K., Johnson C.A.;
RT   "Nesprin-2 interacts with meckelin and mediates ciliogenesis via
RT   remodelling of the actin cytoskeleton.";
RL   J. Cell Sci. 122:2716-2726(2009).
RN   [6]
RP   FUNCTION, INTERACTION WITH F-ACTIN, AND MUTAGENESIS OF ILE-128 AND
RP   ILE-131.
RX   PubMed=20724637; DOI=10.1126/science.1189072;
RA   Luxton G.W., Gomes E.R., Folker E.S., Vintinner E., Gundersen G.G.;
RT   "Linear arrays of nuclear envelope proteins harness retrograde actin
RT   flow for nuclear movement.";
RL   Science 329:956-959(2010).
CC   -!- FUNCTION: Multi-isomeric modular protein which forms a linking
CC       network between organelles and the actin cytoskeleton to maintain
CC       the subcellular spatial organization. Component of SUN-protein-
CC       containing multivariate complexes also called LINC complexes which
CC       link the nucleoskeleton and cytoskeleton by providing versatile
CC       outer nuclear membrane attachment sites for cytoskeletal
CC       filaments. Involved in the maintenance of nuclear organization and
CC       structural integrity. Probable anchoring protein which tethers the
CC       nucleus to the cytoskeleton. Connects nuclei to the cytoskeleton
CC       by interacting with the nuclear envelope and with F-actin in the
CC       cytoplasm. Specifically, Syne2 and Sun2 assemble in arrays of
CC       transmembrane actin-associated nuclear (TAN) lines which are bound
CC       to F-actin cables and couple the nucleus to retrograde actin flow
CC       during actin-dependent nuclear movement. Required for centrosome
CC       migration to the apical cell surface during early ciliogenesis.
CC   -!- SUBUNIT: Component of LINC complexes composed of SUN domain-
CC       containing proteins (SUN1 or SUN2) coupled to KASH domain-
CC       containing proteins (SYNE1, SYNE2 or SYNE3) also called nesprins.
CC       Interacts with EMD, LMNA and F-actin via its N-terminal domain (By
CC       similarity). Interacts with TMEM67. Several isoforms form
CC       complexes within the nuclear envelope (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus outer membrane; Single-pass type IV
CC       membrane protein; Cytoplasmic side. Sarcoplasmic reticulum
CC       membrane; Single-pass type IV membrane protein (By similarity).
CC       Cell membrane; Single-pass membrane protein. Cytoplasm,
CC       cytoskeleton. Mitochondrion (By similarity). Nucleus, nucleoplasm
CC       (By similarity). Note=Different isoform patterns are found in the
CC       different compartments of the cell. The isoforms having the C-
CC       terminal transmembrane span can be found in several organellar
CC       membranes like the nuclear envelope, the sarcoplasmic reticulum of
CC       myoblasts, or the lamellipodia and focal adhesions at the cell
CC       membrane. The largest part of the outer nuclear membrane-
CC       associated protein is cytoplasmic, while its C-terminal part is
CC       associated with the nuclear envelope, most probably the outer
CC       nuclear membrane. Remains associated with the nuclear envelope
CC       during its breakdown in mitotic cells. Shorter solubles isoforms
CC       can be found in the cytoplasm and within the nucleus (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Nesprin-2 Giant, NUANCE;
CC         IsoId=Q6ZWQ0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZWQ0-2; Sequence=VSP_038800, VSP_038801;
CC       Name=3;
CC         IsoId=Q6ZWQ0-3; Sequence=VSP_038799, VSP_038802;
CC   -!- TISSUE SPECIFICITY: C-terminal isoforms are highly expressed in
CC       the brain, hert and skeletal muscle. Isoform 1 (Nesprin-2 Giant)
CC       is most prevalent in the brain, skin, kidney and skeletal muscle.
CC   -!- DOMAIN: The KASH domain, which contains a transmembrane domain,
CC       mediates the nuclear envelope targeting and is involved in the
CC       binding to SUN1 and SUN2 through recognition of their SUN domains
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the nesprin family.
CC   -!- SIMILARITY: Contains 1 actin-binding domain.
CC   -!- SIMILARITY: Contains 2 CH (calponin-homology) domains.
CC   -!- SIMILARITY: Contains 1 KASH domain.
CC   -!- SIMILARITY: Contains 17 spectrin repeats.
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DR   EMBL; AK052521; BAC35023.1; -; mRNA.
DR   EMBL; AC115714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC159897; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC164121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC166991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC082586; AAH82586.1; -; mRNA.
DR   IPI; IPI00845851; -.
DR   IPI; IPI00918857; -.
DR   IPI; IPI00919041; -.
DR   RefSeq; NP_001005510.2; NM_001005510.2.
DR   UniGene; Mm.26652; -.
DR   ProteinModelPortal; Q6ZWQ0; -.
DR   SMR; Q6ZWQ0; 21-293.
DR   STRING; Q6ZWQ0; -.
DR   Ensembl; ENSMUST00000067436; ENSMUSP00000069507; ENSMUSG00000063450.
DR   Ensembl; ENSMUST00000143031; ENSMUSP00000119120; ENSMUSG00000063450.
DR   Ensembl; ENSMUST00000150317; ENSMUSP00000118142; ENSMUSG00000063450.
DR   GeneID; 319565; -.
DR   KEGG; mmu:319565; -.
DR   UCSC; uc007nxn.1; mouse.
DR   CTD; 319565; -.
DR   MGI; MGI:2449316; Syne2.
DR   eggNOG; roNOG13976; -.
DR   GeneTree; ENSGT00600000084318; -.
DR   HOVERGEN; HBG065764; -.
DR   InParanoid; Q6ZWQ0; -.
DR   OrthoDB; EOG4TTGGX; -.
DR   ArrayExpress; Q6ZWQ0; -.
DR   Bgee; Q6ZWQ0; -.
DR   Genevestigator; Q6ZWQ0; -.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR   GO; GO:0051642; P:centrosome localization; IMP:UniProtKB.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:MGI.
DR   GO; GO:0010761; P:fibroblast migration; IMP:MGI.
DR   GO; GO:0006998; P:nuclear envelope organization; IMP:MGI.
DR   GO; GO:0031022; P:nuclear migration along microfilament; IMP:UniProtKB.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR   GO; GO:0034504; P:protein localization to nucleus; IMP:MGI.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR012315; KASH.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 2.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF10541; KASH; 1.
DR   Pfam; PF00435; Spectrin; 3.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00150; SPEC; 17.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS51049; KASH; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Cell membrane; Cytoplasm;
KW   Cytoskeleton; Membrane; Mitochondrion; Nucleus; Phosphoprotein;
KW   Repeat; Sarcoplasmic reticulum; Transmembrane; Transmembrane helix.
FT   CHAIN         1   6874       Nesprin-2.
FT                                /FTId=PRO_0000392210.
FT   TOPO_DOM      1   6823       Cytoplasmic (Potential).
FT   TRANSMEM   6824   6844       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   TOPO_DOM   6845   6874       Perinuclear space (Potential).
FT   DOMAIN        1    286       Actin-binding.
FT   DOMAIN       31    136       CH 1.
FT   DOMAIN      183    288       CH 2.
FT   REPEAT     1427   1525       Spectrin 1.
FT   REPEAT     1528   1632       Spectrin 2.
FT   REPEAT     2034   2131       Spectrin 3.
FT   REPEAT     2720   2820       Spectrin 4.
FT   REPEAT     4827   4926       Spectrin 5.
FT   REPEAT     4933   5038       Spectrin 6.
FT   REPEAT     5048   5152       Spectrin 7.
FT   REPEAT     5159   5259       Spectrin 8.
FT   REPEAT     5263   5371       Spectrin 9.
FT   REPEAT     5583   5681       Spectrin 10.
FT   REPEAT     5800   5900       Spectrin 11.
FT   REPEAT     5907   6005       Spectrin 12.
FT   REPEAT     6012   6119       Spectrin 13.
FT   REPEAT     6126   6228       Spectrin 14.
FT   REPEAT     6235   6335       Spectrin 15.
FT   REPEAT     6539   6642       Spectrin 16.
FT   REPEAT     6649   6753       Spectrin 17.
FT   DOMAIN     6815   6874       KASH.
FT   COMPBIAS   6790   6797       Poly-Glu.
FT   COMPBIAS   6826   6838       Poly-Leu.
FT   MOD_RES    2645   2645       Phosphoserine (By similarity).
FT   MOD_RES    4096   4096       Phosphoserine (By similarity).
FT   MOD_RES    4098   4098       Phosphoserine (By similarity).
FT   MOD_RES    6348   6348       Phosphoserine (By similarity).
FT   VAR_SEQ       1   4994       Missing (in isoform 3).
FT                                /FTId=VSP_038799.
FT   VAR_SEQ     472    482       INNVLGKNFIP -> FVIVPVHKLCE (in isoform
FT                                2).
FT                                /FTId=VSP_038800.
FT   VAR_SEQ     483   6874       Missing (in isoform 2).
FT                                /FTId=VSP_038801.
FT   VAR_SEQ    6781   6789       SPRPRWTFL -> FGV (in isoform 3).
FT                                /FTId=VSP_038802.
FT   MUTAGEN     128    128       I->A: Impairs interaction with F-actin;
FT                                when assocoated with A-131.
FT   MUTAGEN     131    131       I->A: Impairs interaction with F-actin;
FT                                when assocoated with A-128.
SQ   SEQUENCE   6874 AA;  782725 MW;  379792E42B95B7DB CRC64;
     MAASPVLPTE DGEGFLGIDD LHFSLQAEQE DTQKKTFTCW INSQLAKHTP PSVVSDLFAD
     IKKGHVLLDL LEVLSGQQLP RDKGSNTFQC RINIEHALTF LKNRSIKLIN IHVADIVEGN
     PSIILGLIWT IILHFHIEKL AQTLSCDYNQ PSPEVVSVAA SSPTSSPPTK KCSKAQAQAR
     WQWSAKKALL QWAQEQCARS ESVNVTDFKS SWRNGMAFLA VIHALRPDLI DMDSMRHRSN
     KDNLKEAFRI AEHELKIPKL LEPEDVDVVN PDEKSIMTYV AQFLKYSKDA PGPGDSTQAK
     VRDALVWLTL QEKRFQKMLK DSASETYCNK YHSLLSFMES LNEEKESFID VLSLKGRMGE
     LNEDESRLRQ GWTSLMHQVA AWRAQLDDAL PSPLKETEAW LKDIEGVVQE GVPTSQSYSE
     ARTLIQGKLS SFKSLMGSFD YHSDVLMAFQ SNAEKSLPAV PPVKLEEMTR RINNVLGKNF
     IPLLEFHDSK CSVLALLDEA KAKLDVWNGT YESKESVEVL LEDWHKFTGE KKFLIQLDAS
     FQKCEEMYKN SARECESIRE EYMMLEKNVH SCRQYIHNTK ATLQRALMSW ATFEEDLALL
     KASFDLTKKE QIKEVPVETL LQWNTKHTSL NEVGSFLIGV SSREVAASIS KELRRLNKRW
     RKFITKTPLL KLPLVKIQDQ PPGNSSGTSL SKESAMAAEP GGSRGEDVKA AEKQEVEDEE
     SAGQLKVNEE VEGLIKQVTI WESQTKSILD LLQHGDHADG SSADTLQHLI AKGSVYEELL
     ARTEDTLQMD VQSPSNLEPF QNVLRAGLQA KIQEAKQGVQ ITMVELSAVL KNLSDEPLEL
     DLGLKVEEAQ KELEVSILRA EQLLGQRERP GGFLLKYKEA LEILNTNSLA KYLRAVEELK
     RTVPGGAKLQ LEEQSRVASA KWEPLRHEIS LYLQQLKIAI EEEKLRDNIA RLEKQINKEK
     KLIRRGRTRG LRKEHEACLS PESIKCQLEH HVGVLRVLCE ELTSPEDQQE LKRALRDYEQ
     KIARLLKCAS EIHTTLQSSQ GGALEERSAL ITTENGRRDA DGEVPLEIPD NQLSTEKAME
     PIKNFSQTSE LKPQQEESIM EKEGKDCSAS LSDLQERYDT QRGLLEQHLQ DSKSRVTSDF
     ASEQERSSAC LQSKLAELQV LLADTDAHWE KFEITSLNLR RLMSDAEKPV LNQERDLLKG
     NEQVLHGLLN TRMESLEMAL QIVLPLEKEC SLLCASDLPL CTVAVQDLHP VEIDGVYQNL
     RDIRDSIAKQ IRVCTSLEEP SNSVPRELHT LDQCAIQDIV LKCRLQLETM NQKVEMREDA
     LDALEGFLAS LRAAKLSAEL PADRPAPKAP EVLSEDILLM KEKAGPLDER LRTLGINIKD
     AEGGENTTCE RLVGALSVNL VAMDGQSKEE GPPEDKKLLE ACSSKNLELF KNIQDLQNQI
     SKIGLKDPTA PAVKHRKKSL LRLDKDLDGL EEEKVRIQKI AGSLPRFKDG SEKNVIQQCE
     DTAALWESTK ASVTESLEQC GSALELLRQY QNIKNNLTAL IQKEEGIISQ QASYMGKDNL
     KKKIAEIETV KEEFSDHLEV VDKINQICKN LQYHLNKMKT FEDPPFEKEA NAIVDRWLDI
     NEKTEEYGEN LGRALALWDK LFIIKNNIDE WTEQILGKAE SHELTEEDRG RLKEELKVLE
     EQSAEFSRRV ADIQSLLQSN EKPLELQVME SSVLSKMKDV KTHVAGGSNS YAPSGSTAEL
     REDLDQAKTQ MGMTESLLNA LSPSDSLEIF TKLEEIQQQI FQQKHSMTVL ENQIGCLTPE
     LSELKRQYAS VSNLFNTKKN ALQDHFATFL NEQCKNFNDW FSNVKTNLQE CFEPPETKLS
     LEQRLQKLSD FLTLGGGNSK IQQVETVLQH VKMLLPKAHV KELDSWLRSQ ELELENMESI
     CQARAGELNN SFQQLLRLED DCRSLSKWLT NQEENWGKME VSGERMDLFS QALTRKREQF
     ETVAQLSDSL KEHGLTEGEE TIKESTHLID RYQALWRQLH EIEEEDKLPA AEDQSFNDLA
     DDVIHWIKEI KESLMALNSS EGKMPLEERI QKIKEIIALK PEGDAKIQMV MRQAEHCEAP
     LAQETFTDLS NQWDSTLHLA NTYLSHQEKL VLEGEKYLQS KEDLRLMLTE LKKQQEAGFA
     LQPGLPEKQA QLKIYKKFLQ KAQDLTSLLE ELKSQGNYLL ECTKNPSFSE EPWLEVKHLH
     ESLLQQLQDS VQKLEGHVQE HSSYQVCLTD LSSTLDDISK EYFSLCDGSK DQIMAKERMQ
     KLQELESRLR FQGGALKKAS ALAKSIKQNT SSVGQKIIKD DIRSLKYKQK DLENRIESAK
     QETENGLNSI LKSKSSTEKH VKFSLPVEEM PATSEVPKPT RESAAVGESG GARETNTNSA
     VEMILSKQLS LNVQESMQNA QDEREVNELQ NQPLELDIML RNEQLKGMEE LSTHLEARRA
     AIELLEQSQH LNQTEEQALV LPAARPSVCH LGSLQQELHT LKKTKERQYG LLSGFQDQLV
     MAEASLNTSL AEVESLKIGS LDSATYLGKI KKFLGSVENQ QGSLSKLRTE WAHLSSLLAA
     ADQKLVESQM KHLEHGWELV EQLAHRKCFQ QATEHSELTC LLEKLQDLKV SLHQQQQRLT
     LSLNSPGQQA AIVDMVTPAA ELQAIKCEFS GLKWQAELHM KRLWGEKDKK TLEDAINNLN
     KQMEALEPLN REVENRIKKC ELQNRIKETL SWVKNTMAEL VVPIALLPDN ILSQIRKCKL
     IHDGILGNQQ AVELLVEEVR GITPSLAPCE GDGLNALLED LQSQHQALLL KSTERSQQLE
     LKLEEKSKLF AIIGKVQLTL EESETLMSPT GDRASTEAEL ERRLAILKAS QQQLQDTESA
     LSAHLQELTN AYKDANVFER LFLDDQLKNL KARTNRTQRF LQNNGSELKQ KMESYREFHD
     KAAVLQKEAE CILHGGLLPL RQELEQDAKE QLGNLRDKLA AIRGSLSQVL TSEEVFDTIG
     LSWDGSLLAR LQTQVLERER EVEGKIKQLD TFLIARDRHQ ASISKIRAVD LQIKKGAESL
     LKVPSMSPES TLLNAQTLIQ KIEKSKRLRD EIIRKLSKNE AFDDSFKESE MQRLKLCAEE
     NSRLQEALQN MLLELQPREM GEKEFREKLE NALHVLKQIQ SRLQQPLCVN LGVQHIQHEK
     ETWEAFGEQV EAEMCGLRAV RITEEQREEN DSGTGGMEAK LRDIEGLHME LSKSISLRAD
     VLNDAYDSAN RYDELVAGAL RIITSLEATL LSYRVDLHNP QKTLELAHLK QEELQSSVAD
     LRSLTETLGA ISSPEAKEQL RCTLEVLAAK NSALKAGLEA QEAEEERCLE NYKCFRKMKE
     EICSRLRKME MDLGQSIFPL PRSYKEALAR LEQSKALTSN LLSTKEDLVK LRQLLRHLRC
     RSTENDATCA LGVASALWEK WLSLLEAARE WQQWGGELKR EWKFISEEIE REAIILETLQ
     EDLPEISKTN AAPTEELWQL LDSLCQHQES VEKQQLLLAL LLQRVRSIQN IPEGTETGET
     IPALQEIGSM QERCDRLLHT TRKNKDLVQA EIQAQQSFLK EIKDVKRVFE QISTSFPNLA
     PEGHPERAEQ FEELRSILQK GKLSFENIME KLRIKYSEMY SIVPAEIGSQ VEECRSALED
     AEEKMSSEVS KSSPSSIMRR KIERINNGLH CVEKMLQQKS RNIEEAHEIQ KKIWDELDLW
     HSKLNELDSE VQDFVEQDPG QAQEWMDNLM APFQQHQQVS QRAESRTSQL NKATIKMEEY
     NDLLKSTEVW IEKTSCLLAN PACYDSSRTL SHRASTLQMA LEDSEQKHSL LHSIFTDLED
     LSIIFETDDL IQTIHELSDQ VAALQQQIME ALPHVQQVAD DVVAIESEVK AMEKKVAKIK
     AILLSKEIFD FPPEEHLKHG EVILENIHPM KKTIAEIMTY QVELRLPQTG TKPLPVFQRT
     SQLLQDVKLL ENVTQEQNEL LKVVIKQTAE CDEEIDSLKQ MLTNYSAEIS PEHVSQNQVA
     DLPSLQGEME RLEKQILNLN QKKEDLLVDL KTAVLNLHEH LKQEQQEVGD KPSAGASECT
     VAERDASERK LSRTNSMSFL PVVKEEAEES SVKSEDGRRR TEPPSASWSF LGKHSKDLEG
     DGASSSSSAT IVQDADGRIS TCDSSMVHII APDSGSTEEG PAPSPRLSQT DEGATPPIEA
     ALLDFPREQG AFESTVERSR PRPADILRVC KTQVAKLELW LQQANVAFEP ETVDADMQQV
     VEEELAGCQA MLTEIEYKVA SLLETCKDQG LGDCGTTQQE AEALSWKLKT VKCNLEKVQM
     VLQEKFSEDQ HPSTLKKPSE PHDVDQPAGL SELDSVLTER PQFSRQKDAP QPQILELKPS
     EQKDLIKFTE LNAKKTWLQG HQENEDANRQ SASSSKVPSP GNAASDSTLP LQAQSGDKWQ
     YLHHELTSRP NPSVPQLVEP QVALTTSTLP SVSVYNFRCP TADELQAYTT QLEELRQEAN
     TIQTQGSMTE ETYISLDKRL FELFLSLSRC LGSVEGLLQR PGLLREDACA QQVFFQKLAL
     ELKKLYLALG DKKDDFLKAV TWPGKEATLL PECIDALTVS LESVQSRAAW RDASLKAGLE
     HSRSYQNEVK RLYSQLIKKK TALQQSLNEI SGQSISKQLQ KADVHTAELQ NSEKQVAKLR
     DEGERLRFPH GLLQDVYKLE DVLDSMWGIL RARYLELSSP FLSKSLQTLL QGMAELVSIG
     KGKLAADPLQ HAKSKAALQA QLQDHKAFFQ KLVADMLLIQ TYSATMFPPS LQKGEGFGAE
     QVAEVRALEE EACLRGAQLQ SMLQKWEEFD DNYASLEKDL EALISSLPSV SLVEETEERL
     LERISFYQQI KRNIDGKHAR LCQTLNEGRQ LAASVSCPEP EGQIARLEEQ WLSLNKRIDQ
     ELHRLQTLLK HLLSYSRDSD ELTRWLETSQ QTLNYWKEQS LNVSQDLNTI RSNIDRFFKF
     SKEVDERSSL KSAVMSTGNQ LLHLKEADTA TLRASLAQFE QKWTVLITQL PDIQEKLHQL
     QMEKLPSREA ISEMISWMNA VEPQAAGKDT ELSKSSASQV KHLLQKLKEF RMEMDYKQWV
     VDFVNQSLLQ LSTCDVESKR YERTEFAEHL GEMNRQWQRV HGTLNRKIQH LEQLLESITE
     NENKVQNLNS WLEAQEERLK MLQKPESAVS MEKLLLDCQD IENQLALKSK ALDELRQSSL
     TMDGGDVPLL EDMASGIVEL FQKKNNVTSQ VHQLRASVQS VLQEWKACDK LYDEATMRTT
     QLTYSMEHSK PAVLSLQALA CQVQNLEALQ DEAENGERSW EKLQEVIGRL KASCPSMAGI
     IEEKCQDAHS RWTQVNQDLA DQLQEARGQL QLWKAPHNAH AEAAAWLQQQ EAKFQQLANT
     NLSGDNLADI LPRALKDIKG LQSDLQKTKE AFLENSTLSD QLPQPEERST PGLHSGQRHS
     LQTAAYLEKM LLAKSNEFEI VLAQFKDFTD RLAYSKDLIV HKEENLNKLY HEEKEEVPDL
     FLNHVLALTA QSPDIERLNE ESLRLPLSDV TIKTLQSLNR QWIRATATAL DHYSELQGNG
     LNEKFLHYCE RWIQVLEKIQ ESLSVEVAHS LPALLEQQKT YEILEAEVST NQAVADAYVT
     QSLQLLDTAE IEKRPEFVSE FSKLSDQWQR AARGVRQRKC DISRLVTQWR FFTTSVEDLL
     RFLADTSQLL SAVKEQDCYS LCQTRRLVHE LKSKEIHLQR WRTTYALALE AGEKLRNTPS
     PETREFVDGQ ISRLQESWKD TELSLGEVIS RLQSTAETWD QCKKKIKKLK KRLQALKAQS
     EDPLPELHEA LHEEKELIKE VEKSLANWTH SLKELQTMKA DLSQHILAED VTVLKEQIQL
     LHRQWEDLCL RVAIRKQEIE DRLNSWIVFN EKNKELCAWL VQMENKVLQT ADVSIEEMIE
     KLQKDCMEEI SLFTENKLQL KQMGDQLIKA SSKAKAAELE EKLSKINDRW QHLFDVIGSR
     VKKLKETFAF IQQLDKNMSN LRTWLARIES ELSKPVVYDV CDNQEIQKRL AEQQDLQRDI
     EQHSAGVESV FNICDVLLHD SDACANETEC DSIQQTTRSL DRRWRNICAM SMERRMKIEE
     TWRLWQKFLD DYSRFEDWLK SAERTAACPN SSEVLYTNAK EELKRFEAFQ RQIHERLTQL
     ELINKQYRRL ARENRTDTAS KLKQMVHEGN QRWDNLQKRV TAILRRLRYF TNQREEFEGT
     RESILVWLTE MDLQLTNVEH FSESDAEDKM RQLNGFQQEI TLNTNKIDQL IVFGEQLIQK
     SEPLDAVLIE DELEELHRYC QEVFGRVSRF HRRLTSHTPG LDDEKEASEN ETDIEDPREI
     QADSWRKRRE SEEPTSPQSL CHLVPPALGH ERSGCETPVS VDSIPLEWDH TGDVGGSSSH
     EDDEEGPFYS ALSGKSISEG HPWHVPDSPS HSKHHYKHME GDRTEAPVPT DASTPFKSDY
     VKLLLRQGTD DSKEGLKEAQ QEDEQLATLT GQQPGAFDRW ELIQAQELHS KLRLKQTVQQ
     LKSDIGSIAA WLGKTEAELE ALKLAEPPSD IQEIALRVKR LQEILKAFDT YKALMVSVNV
     SHKEYLPSQS PEATELQNRL HQLSLSWDSV QGVLDSWRGD LRQSLMQCQD FHQLSQDLLL
     WLATAESRRQ KAHVTSPEAD RQVLLECQKD LMRLEKELVA RQPQVSSLRE ISSSLLVKGQ
     GEDYIEAEEK VHVIEKKLKQ LQEQVAQDLM SLQRSLDPDA SLTSFDEVDS GEQLPAAFAK
     SPRPRWTFLE EEEEEEETDS RMPHLDSPGS SQPRRSFLSR VIRAALPLQL LLLLLLLLAC
     LLPASEDDYS CTQANNFARS FYPMLRYTNG PPPT
//
ID   SYNE1_MOUSE             Reviewed;        8799 AA.
AC   Q6ZWR6; Q8K3T7; Q9ERT7; Q9ERT8;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 2.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Nesprin-1;
DE   AltName: Full=Enaptin;
DE   AltName: Full=Myocyte nuclear envelope protein 1;
DE            Short=Myne-1;
DE   AltName: Full=Nuclear envelope spectrin repeat protein 1;
DE   AltName: Full=Synaptic nuclear envelope protein 1;
DE            Short=Syne-1;
GN   Name=Syne1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE [MRNA]
RP   OF 6808-8799 (ISOFORM 4).
RX   MEDLINE=20493580; PubMed=10878022; DOI=10.1074/jbc.M004775200;
RA   Apel E.D., Lewis R.M., Grady R.M., Sanes J.R.;
RT   "Syne-1, a dystrophin- and Klarsicht-related protein associated with
RT   synaptic nuclei at the neuromuscular junction.";
RL   J. Biol. Chem. 275:31986-31995(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), TISSUE SPECIFICITY,
RP   ACTIN-BINDING, AND SUBCELLULAR LOCATION.
RC   STRAIN=BALB/c;
RX   PubMed=15093733; DOI=10.1016/j.yexcr.2004.01.014;
RA   Padmakumar V.C., Abraham S., Braune S., Noegel A.A., Tunggal B.,
RA   Karakesisoglou I., Korenbaum E.;
RT   "Enaptin, a giant actin-binding protein, is an element of the nuclear
RT   membrane and the actin cytoskeleton.";
RL   Exp. Cell Res. 295:330-339(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8308, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8227, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   FUNCTION.
RX   PubMed=19596800; DOI=10.1242/jcs.043794;
RA   Dawe H.R., Adams M., Wheway G., Szymanska K., Logan C.V., Noegel A.A.,
RA   Gull K., Johnson C.A.;
RT   "Nesprin-2 interacts with meckelin and mediates ciliogenesis via
RT   remodelling of the actin cytoskeleton.";
RL   J. Cell Sci. 122:2716-2726(2009).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19509342; DOI=10.1073/pnas.0812037106;
RA   Lei K., Zhang X., Ding X., Guo X., Chen M., Zhu B., Xu T., Zhuang Y.,
RA   Xu R., Han M.;
RT   "SUN1 and SUN2 play critical but partially redundant roles in
RT   anchoring nuclei in skeletal muscle cells in mice.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:10207-10212(2009).
CC   -!- FUNCTION: Multi-isomeric modular protein which forms a linking
CC       network between organelles and the actin cytoskeleton to maintain
CC       the subcellular spatial organization. Component of SUN-protein-
CC       containing multivariate complexes also called LINC complexes which
CC       link the nucleoskeleton and cytoskeleton by providing versatile
CC       outer nuclear membrane attachment sites for cytoskeletal
CC       filaments. Involved in the maintenance of nuclear organization and
CC       structural integrity. Connects nuclei to the cytoskeleton by
CC       interacting with the nuclear envelope and with F-actin in the
CC       cytoplasm (By similarity). Required for centrosome migration to
CC       the apical cell surface during early ciliogenesis.
CC   -!- SUBUNIT: Component of LINC complexes composed of SUN domain-
CC       containing proteins (SUN1 or SUN2) coupled to KASH domain-
CC       containing proteins (SYNE1, SYNE2 or SYNE3) also called nesprins.
CC       Interacts with MUSK, with F-actin via its N-terminal domain, and
CC       with EMD and LMNA in vitro (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus outer membrane; Single-pass type IV
CC       membrane protein; Cytoplasmic side (Potential). Cytoplasm,
CC       cytoskeleton. Cytoplasm, myofibril, sarcomere (By similarity).
CC       Note=The largest part of the protein is cytoplasmic, while its C-
CC       terminal part is associated with the nuclear envelope, most
CC       probably the outer nuclear membrane. In skeletal and smooth
CC       muscles, a significant amount is found in the sarcomeres (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1; Synonyms=Nesprin-1 Giant, Enaptin;
CC         IsoId=Q6ZWR6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZWR6-2; Sequence=VSP_038791, VSP_038796, VSP_038797,
CC                                  VSP_038798;
CC       Name=3; Synonyms=Syne-1A;
CC         IsoId=Q6ZWR6-3; Sequence=VSP_038791, VSP_038796, VSP_038797;
CC       Name=4; Synonyms=Syne-1B;
CC         IsoId=Q6ZWR6-4; Sequence=VSP_038797;
CC         Note=Incomplete sequence;
CC       Name=5; Synonyms=Enaptin-165;
CC         IsoId=Q6ZWR6-5; Sequence=VSP_038792, VSP_038793, VSP_038794,
CC                                  VSP_038795;
CC   -!- DOMAIN: The KASH domain, which contains a transmembrane domain,
CC       mediates the nuclear envelope targeting and is involved in the
CC       binding to SUN1 and SUN2 through recognition of their SUN domains
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the nesprin family.
CC   -!- SIMILARITY: Contains 1 actin-binding domain.
CC   -!- SIMILARITY: Contains 2 CH (calponin-homology) domains.
CC   -!- SIMILARITY: Contains 9 HAT repeats.
CC   -!- SIMILARITY: Contains 1 KASH domain.
CC   -!- SIMILARITY: Contains 44 spectrin repeats.
CC   -!- SIMILARITY: Contains 11 TPR repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG24393.1; Type=Frameshift; Positions=6810, 7656, 7658;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF281869; AAG24392.1; -; mRNA.
DR   EMBL; AF281870; AAG24393.1; ALT_FRAME; mRNA.
DR   EMBL; AF535143; AAN03487.1; -; mRNA.
DR   EMBL; AK036828; BAC29595.1; -; mRNA.
DR   EMBL; AC156392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC156393; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC157020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC159748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC161829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC162381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC162385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00403993; -.
DR   IPI; IPI00461474; -.
DR   IPI; IPI00473373; -.
DR   IPI; IPI00816892; -.
DR   IPI; IPI00890038; -.
DR   RefSeq; NP_001073154.1; NM_001079686.1.
DR   UniGene; Mm.331626; -.
DR   ProteinModelPortal; Q6ZWR6; -.
DR   SMR; Q6ZWR6; 18-292, 1733-1759, 3212-3237.
DR   STRING; Q6ZWR6; -.
DR   PRIDE; Q6ZWR6; -.
DR   Ensembl; ENSMUST00000092721; ENSMUSP00000090396; ENSMUSG00000019769.
DR   GeneID; 64009; -.
DR   KEGG; mmu:64009; -.
DR   UCSC; uc007egt.1; mouse.
DR   CTD; 64009; -.
DR   MGI; MGI:1927152; Syne1.
DR   GeneTree; ENSGT00600000084318; -.
DR   HOVERGEN; HBG056327; -.
DR   InParanoid; Q9ERT7; -.
DR   OMA; SLNSKCK; -.
DR   OrthoDB; EOG4ZKJK9; -.
DR   NextBio; 319851; -.
DR   ArrayExpress; Q6ZWR6; -.
DR   Bgee; Q6ZWR6; -.
DR   Genevestigator; Q6ZWR6; -.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0040023; P:establishment of nucleus localization; IMP:MGI.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR012315; KASH.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 2.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF10541; KASH; 1.
DR   Pfam; PF00435; Spectrin; 8.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00150; SPEC; 42.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS51049; KASH; 1.
DR   PROSITE; PS50005; TPR; FALSE_NEG.
DR   PROSITE; PS50293; TPR_REGION; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW   Membrane; Nucleus; Phosphoprotein; Repeat; TPR repeat; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   8799       Nesprin-1.
FT                                /FTId=PRO_0000392209.
FT   TOPO_DOM      1   8748       Cytoplasmic (Potential).
FT   TRANSMEM   8749   8769       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   TOPO_DOM   8770   8799       Perinuclear space (Potential).
FT   DOMAIN        1    289       Actin-binding.
FT   DOMAIN       27    134       CH 1.
FT   DOMAIN      178    283       CH 2.
FT   REPEAT      592    624       HAT 1.
FT   REPEAT      915    949       TPR 1.
FT   REPEAT     1015   1048       TPR 2.
FT   REPEAT     1103   1135       HAT 2.
FT   REPEAT     1127   1229       Spectrin 1.
FT   REPEAT     1423   1455       HAT 3.
FT   REPEAT     1447   1546       Spectrin 2.
FT   REPEAT     1538   1572       TPR 3.
FT   REPEAT     1553   1649       Spectrin 3.
FT   REPEAT     1656   1759       Spectrin 4.
FT   REPEAT     2087   2191       Spectrin 5.
FT   REPEAT     2305   2402       Spectrin 6.
FT   REPEAT     2407   2509       Spectrin 7.
FT   REPEAT     2516   2618       Spectrin 8.
FT   REPEAT     2703   2742       HAT 4.
FT   REPEAT     2841   2982       Spectrin 9.
FT   REPEAT     2947   2980       TPR 4.
FT   REPEAT     3065   3167       Spectrin 10.
FT   REPEAT     3174   3274       Spectrin 11.
FT   REPEAT     3281   3383       Spectrin 12.
FT   REPEAT     3390   3486       Spectrin 13.
FT   REPEAT     3479   3512       TPR 5.
FT   REPEAT     3490   3593       Spectrin 14.
FT   REPEAT     3817   3916       Spectrin 15.
FT   REPEAT     3923   4030       Spectrin 16.
FT   REPEAT     4138   4236       Spectrin 17.
FT   REPEAT     4345   4447       Spectrin 18.
FT   REPEAT     4454   4556       Spectrin 19.
FT   REPEAT     4563   4665       Spectrin 20.
FT   REPEAT     4580   4613       TPR 6.
FT   REPEAT     4672   4772       Spectrin 21.
FT   REPEAT     4885   4987       Spectrin 22.
FT   REPEAT     4994   5095       Spectrin 23.
FT   REPEAT     5078   5110       HAT 5.
FT   REPEAT     5102   5205       Spectrin 24.
FT   REPEAT     5212   5317       Spectrin 25.
FT   REPEAT     5426   5521       Spectrin 26.
FT   REPEAT     5514   5547       TPR 7.
FT   REPEAT     5528   5626       Spectrin 27.
FT   REPEAT     5736   5769       TPR 8.
FT   REPEAT     5747   5867       Spectrin 28.
FT   REPEAT     5961   5994       TPR 9.
FT   REPEAT     5975   6078       Spectrin 29.
FT   REPEAT     6702   6794       Spectrin 30.
FT   REPEAT     6777   6809       HAT 6.
FT   REPEAT     6801   6906       Spectrin 31.
FT   REPEAT     6917   7021       Spectrin 32.
FT   REPEAT     7004   7036       HAT 7.
FT   REPEAT     7028   7129       Spectrin 33.
FT   REPEAT     7136   7238       Spectrin 34.
FT   REPEAT     7214   7253       HAT 8.
FT   REPEAT     7358   7455       Spectrin 35.
FT   REPEAT     7462   7562       Spectrin 36.
FT   REPEAT     7569   7672       Spectrin 37.
FT   REPEAT     7679   7779       Spectrin 38.
FT   REPEAT     7786   7884       Spectrin 39.
FT   REPEAT     7891   7998       Spectrin 40.
FT   REPEAT     7978   8010       HAT 9.
FT   REPEAT     8005   8107       Spectrin 41.
FT   REPEAT     8025   8058       TPR 10.
FT   REPEAT     8114   8214       Spectrin 42.
FT   REPEAT     8131   8165       TPR 11.
FT   REPEAT     8445   8548       Spectrin 43.
FT   REPEAT     8555   8659       Spectrin 44.
FT   DOMAIN     8740   8799       KASH.
FT   COMPBIAS   8665   8731       Ser-rich.
FT   MOD_RES    1325   1325       Phosphoserine (By similarity).
FT   MOD_RES    2089   2089       Phosphotyrosine (By similarity).
FT   MOD_RES    2375   2375       Phosphoserine (By similarity).
FT   MOD_RES    8227   8227       Phosphoserine.
FT   MOD_RES    8274   8274       Phosphoserine (By similarity).
FT   MOD_RES    8278   8278       Phosphothreonine (By similarity).
FT   MOD_RES    8281   8281       Phosphoserine (By similarity).
FT   MOD_RES    8284   8284       Phosphoserine (By similarity).
FT   MOD_RES    8308   8308       Phosphoserine.
FT   MOD_RES    8348   8348       Phosphoserine (By similarity).
FT   VAR_SEQ       1   7828       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_038791.
FT   VAR_SEQ     103    103       K -> KSMYRGSP (in isoform 5).
FT                                /FTId=VSP_038792.
FT   VAR_SEQ     297    313       Missing (in isoform 5).
FT                                /FTId=VSP_038793.
FT   VAR_SEQ    1435   1441       DIKTMEM -> EYVLHHF (in isoform 5).
FT                                /FTId=VSP_038794.
FT   VAR_SEQ    1442   8799       Missing (in isoform 5).
FT                                /FTId=VSP_038795.
FT   VAR_SEQ    7829   7878       IAVAQENKIQLQEMGERLAKASHESKASEIQYKLSRVKDRW
FT                                QHLLDLMAA -> MVVAEDLHGPRMAEDSSVDADLPDCDCD
FT                                VS (in isoform 2 and isoform 3).
FT                                /FTId=VSP_038796.
FT   VAR_SEQ    8218   8219       Missing (in isoform 2, isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_038797.
FT   VAR_SEQ    8328   8328       S -> SDVVIPENPEAYVKLTENAIRNTS (in isoform
FT                                2).
FT                                /FTId=VSP_038798.
FT   CONFLICT   1086   1086       G -> W (in Ref. 2; AAN03487).
FT   CONFLICT   1150   1150       I -> T (in Ref. 2; AAN03487).
FT   CONFLICT   7187   7187       E -> G (in Ref. 1; AAG24393).
FT   CONFLICT   7876   7876       M -> I (in Ref. 1; AAG24393).
FT   CONFLICT   8266   8266       P -> L (in Ref. 1; AAG24392/AAG24393).
SQ   SEQUENCE   8799 AA;  1009926 MW;  2A457DC081969CF0 CRC64;
     MATSRASSRS HRDITNVMQR LQDEQEIVQK RTFTKWINSH LAKRKPPMVV DDLFEDMKDG
     IKLLALLEVL SGQKLPCEQG HRVKRIHAVA NIGTALKFLE GRKIKLVNIN ATDIADGRPS
     IVLGLMWTII LYFQIEELTS NLPQLQSLSS SASSVDSMVS TETASPPSKR KVAAKIQGNA
     KKTLLKWVQH TAGKQMGIEV KDFGKSWRTG LAFHSVIHAI QPELVDLEKV KTRSNRENLE
     DAFTIAETQL GIPRLLDPED VDVDKPDEKS IMTYVAQFLT QYPDIHGAGC DGQEDDVVFV
     GFTNNIALLL GFQRDDRLIL KETKVWIEQF ERDFTRAQMT ESSLQDKYQA FKHFRVQYEM
     KRKQVEHIIQ PLQRDGKLTL DQALVKQCWE RVSSRLFDWH IQLDKSLPAP LGTIGAWLYR
     AEVALREEIT IQQVHEETAN TIQRKLEQHK DLLQNTDAHK RAFHEIYQTR SVNGIPMPPD
     QLEDMAERFH FVSSTSELHL MKMEFLELKY RLLSLLVLAE SKLKSWIIKY GRRESVELLL
     QSYISFIENS KFFEQYEVTY QILKQTADIY VKAEGSVEEA ENVMKFMSEA TAQWRNLSVE
     VRSVRSMLEE VISNWDRYGD TVASLQAWLE DAEKMLSQSE HAKKDFFRNL PHWIQQHTAM
     NDAGNFLIET CDEIVSRDLK QQLLLLNGRW RELFMEVKQY ARADEMDRMK KEYIDVTTTL
     FGFATEAHRK LSEPLEVSFI NVKLLIQDLE DLEKRVPVMD AQYKMIAKKA HLFAKESPQE
     EANEMLTTMS KLKEQLSKVK ECCSPLLYEA QQLTVPLEEL ETQITSFYDS LGKINEILSV
     LEQEAQSSTL FKQKHQELLA SQENCKKSLT LIEKGSQSVQ KLVTSSQARK PWDHTKLQKQ
     IADVHHAFQS MIKKTGDWKK HVEANSRLMK KFEESRAELE KVLRVAQEGL EEKGDPEELL
     RRHTEFFSQL DQRVLNAFLK ACDELTDILP EQEQQGLQEA VRKLHKQWKD LQGEAPYHLL
     HLKIAVEKDR FSAAVEECRA ELEQETKLAP QEGSEKIIKE HRVFFSDKGP HHLCEKRLQL
     IEELCGKLPV QDPVRDTCGA CHTALKELKA SIDNTYTMLV DDPDKWKDYT SRFSEFSSWV
     SAKKACLKKI KDEPIDTGNH DEVKHMVDEI RNDITKKGES LSWLKSRLKY LIDISSENEA
     QKRGDELAEL SSSFKALVAL LSEVEKLLSN FGECVQYKEI VKSSLEGLIS GPQESKEEAE
     MILDSKNLLE AQQLLLHHQQ KTKMISAKKR DLQEQMEQAQ QGGQAGPGQE ELRKLESTLT
     GLEQSRERQE RRIQVSLRKW ERFETNKETV VRYLFQTGSS HERFLSFSSL ESLSSELEQT
     KEFSKRTESI ATQAENLVKE AAELPLGPRN KRVLQRQAKS IKEQVTTLED TLEEDIKTME
     MVKSKWDHFG SNFETLSIWI LEKENELSSL EASASAADVQ ISQIKVTIQE IESKIDSIVG
     LEEEAQSFAQ FVTTGESARI KAKLTQIRRY WEELQEHARG LEGTILGHLS QQQKFEENLR
     KIRQSVSEFA ERLADPIKIC SSAAETYKVL QEHMDLCQAV ESLSSTVTMF SASAQKAVNR
     ESCTQEAAAL QQQYEEILHK AKEMQTALED LLARWQRLEK GLSPFLTWLE RCEAIASSPE
     KDISADRGKV ESELQLIQAL QNEVVSQASL YSNLLQLKEA LFSVASKEDV AVMKLQLEQL
     DERWGDLPQI ISKRMHFLQS VLAEHKQFDE LLFSFSVWIK QFLGELQRTS EINLRDHQVA
     LTRHKDHAAE IEKKRGEITH LQGHLSQLRS LGRAQDLHPL QSKVDDCFQL FEEASQVVER
     RKLALAQLAE FLQSHACMST LLYQLRQTVE ATKSMSKKQS DSLKTDLHSA IQDVKTLESS
     AISLDGTLTK AQCHLKSASP EERTSCRATT DQLSLEVERI QNLLGTKQSE ADALVALKEA
     FREQKEELLR SIEDIEERMD RERLKVPTRQ ALQHRLRVFN QLEDELNSHE HELCWLKDKA
     KQIAQKDVAF APEVDREING LEATWDDTRR QIHENQGQCC GLIDLVREYQ SLKSTVCNVL
     EDASNVVVMR ATIKDQGDLK WAFSKHETSR NEMNSKQKEL DSFTSKGKHL LSELKKIHSG
     DFSLVKTDME STLDKWLDVS ERIEENMDML RVSLSIWDDV LSRKDEIEGW SNSSLPKLAE
     NISNLNNSLR AEELLKELES EVKIKALKLE DLHSKINNLK ELTKNPETPT ELQFIEADLR
     QKLEHAKEIT EEARGTLKDF TAQRTQVERF VKDITAWLIN VEESLTRCAQ TETCEGLKKA
     KDIRKELQSQ QNSITSTQEE LNSLCRKHHS VELESLGRAM TGLIKKHEAT SQLCSQTQAR
     IQDSLEKHFS GSMKEFQEWF LGAKAAARES SNLTGDSQIL EARLHNLQGV LDSLSDGQSK
     LDVVTQEGQT LYAHLPKQIV SSIQEQITKA NEEFQAFLKQ CLKEKQALQD CVSELGSFED
     QHRKLNLWIH EMEERLKTEN LGESKHHISE KKNEVRKVEM FLGELLAARE SLDKLSQRGQ
     LLSEESHSAG KGGCRSTQLL TSYQSLLRVT KEKLRSCQLA LKEHEALEEA TQSMWARVKD
     VQDRLACAES TLGNKETLEG RLSQIQDILL MKGEGEVKLN LAIGKGDQAL RSSNKEGQQA
     IQDQLEMLKK AWAEAMNSAV HAQSTLESVI DQWNDYLEKK SQLEQWMESV DQRLEHPLQL
     QPGLKEKFSL LDHFQSIVSE AEDHTGALQQ LAAKSRELYQ KTQDESFKEA GQEELRTQFQ
     DIMTVAKEKM RTVEDLVKDH LMYLDAVQEF ADWLHSAKEE LHRWSDTSGD PSATQKKLLK
     IKELIDSREI GAGRLSRVES LAPAVKQNTA ASGCELLNSE MQALRADWRQ WEDCLFQTQS
     SLESLVSEMA LSEQEFFGQV TQLEQALEQF CTLLKTWAQQ LTLLEGKNSD EEILECWHKG
     REILDALQKA EPMTEDLKSQ LNELCRFSRD LSPYSEKVSG LIKEYNCLCL QASKGCQNKE
     QILQERFQKA SRGFQQWLVN AKITTAKCFD LPQNLSEVSS SLQKIQEFLS ESENGQHKLN
     TMLFKGELLS SLLTEEKAQA VQAKVLTAKE EWKSFHANLH QKESALENLK IQMKDFEVSA
     ELVQNWLSKT ERLVQESSNR LYDLPAKRRE QQKLQSVLEE IQCYEPQLHR LKEKARQLWE
     GQAASKSFVH RVSQLSSQYL ALSNVTKEKV SRLDRIIAEH NRFSQGVKEL QDWMSDAVHM
     LDSYCLPTSD KSVLDSRMLK LEALLSVRQE KEIQMKMVVT RGEYVLQSTS LEGSAAVQQQ
     LQAVKDMWES LLSAAIRCKS QLEGALSKWT SYQDDVRQFS SWMDSVEVSL TESEKQHTEL
     REKITALGKA KLLNEEVLSH SSLLETIEVK RAAMTEHYVT QLELQDLQER HQALKEKAKE
     AVTKLEKLVR LHQEYQRDLK AFESWLEQEQ EKLDRCSVHE GDTNAHETML RDLQELQVRC
     AEGQALLNSV LHTREDVIPS GLPQAEDRVL ESLRQDWQVY QHRLAEARMQ LNNVVNKLRL
     MEQKFQQADE WLKRMEEKIN FRSECQSSRS DKEIQLLQLK KWHEDLSAHR DEVEEVGTRA
     QGILDETHIS SRMGCQATQL TSRYQALLLQ VLEQIKFFEE ELQCLEETES SLSSYSDWYG
     STHKNFKNVA TKIDKVDESM MGKKLKTLEV LLKDMEKGHS LLKSAREKGE RAMKFLAEHE
     AEALRKEIHT YMEQLKNLTS TVRKECMSLE KGLHLAKEFS DKYKVLAQWM AEYQEILCTP
     EEPKMELYEK KAQLSKYKSL QQMVLSHEPS VTSVQEKSEA LLELVQDQSL KDKIQKLQSD
     FQDLCSRAKE RVFSLEAKVK DHEDYNTELQ EVEKWLLQMS GRLVAPDLLE MSSLETITQQ
     LAHHKAMMEE IAGFEDRLDN LKAKGDTLIG QCPEHLQAKQ KQTVQAHLQG TKDSYSAICS
     TAQRVYRSLE YELQKHVSSQ DTLQQCQAWI SAVQPDLKPS PQPPLSRAEA VKQVKHFRAL
     QEQARTYLDL LCSMCDLSNS SVKNTAKDIQ QTEQLIEQRL VQAQNLTQGW EEIKSLKAEL
     WIYLQDADQQ LQNMKRRHTE LEINIAQNMV MQVKDFIKQL QCKQVSVSTI VEKVDKLTKN
     QESPEHKEIT HLNDQWQDLC LQSDKLCAQR EQDLQRTSSY HDHMRVVEAF LEKFTTEWDS
     LARSNAESTA IHLEALKKLA LALQEEMYAI DDLKDCKQKL IEQLGLDDRE LVREQTSHLE
     QRWFQLQDLV KRKIQVSVTN LEELNVIQSR FQELMEWAEE QQPNIVEALK QSPPPGMAQH
     LLMDHLAICS ELEAKQVLLK SLMKDADRVM ADLGLNERKV IQKALSEAQK HVSCLSDLVG
     QRRKYLNKAL SEKTQFLMAV FQATSQIQQH ERKIVFREYI CLLPDDVSKQ VKTCKTAQAS
     LKTYQNEVTG LCAQGRELMK GITKQEQEEV LGKLQELQTV YDTVLQKCSH RLQELEKSLV
     SRKHFKEDFD KACHWLKQAD IVTFPEINLM NEKTELHAQL DKYQSILEQS PEYENLLLTL
     QTTGQAMLPS LNEVDHSYLS EKLSALPQQF NVIVALAKDK FYKTQEAILA RKEYTSLIEL
     TTQSLGDLED QFLKMRKMPS DLIVEESVSL QQSCSALLGE VVALGEAVNE LNQKKESFRS
     TGQPWQPEKM LQLATLYHRL KRQAEQRVSF LEDTTSVYKE HAQMCRQLES QLEVVKREQA
     KVNEETLPAE EKLKVYHSLA GSLQDSGILL KRVATHLEDL SPHLDPTAYE KAKSQVQSWQ
     EELKQMTSDV GELVTECESR MVQSIDFQTE MSRSLDWLRR VKAELSGPVC LDLSLQDIQE
     EIRKIQIHQE EVLSSLRIMS ALSHKEQEKF TKAKELISAD LEHTLAELQE LDGDVQEALR
     TRQATLTEIY SRCQRYYQVF QAANDWLDDA QEMLQLAGNG LDVESAEENL RSHMEFFKTE
     GQFHSNMEEL RGLVARLDPL IKATGKEELA QKMASLEKRS QGIIQESHTQ RDLLQRCMVQ
     WQEYQKAREG VIELMNDAEK KLSEFAVLKT SSIHEAEEKL SKHKALVSVV DSFHEKIVAL
     EEKASQLEQT GNDTSKATLS RSMTTVWQRW TRLRAVAQDQ EKILEDAVDE WKRLSAKVKE
     TTEVINQLQG RLPGSSTEKA SKAELMTLLE SHDTYLMDLE SQQLTLGVLQ QRALSMLQDR
     AFPGTEEEVP ILRAITALQD QCLNMQEKVK NHGKLVKQEL QEREAVETRI NSVKSWVQET
     KDYLGNPTIE IDTQLEELKR LLAEATSHQE SIEKIAEEQK NKYLGLYTVL PSEISLQLAE
     VALDLKIHDQ IQEKVQEIEE GKAMSQEFSC KIQKVTKDLT TILTKLKAKT DDLVHAKAEH
     KMLGEELDGC NSKLMELDAA IQTFSERHSQ LGQPLAKKIG KLTELHQQTI RQAENRLSKL
     NQALSHMEEY NEMLETVRKW IEKAKVLVHG NIAWNSASQL QEQYILHQTL LEESGEIDSD
     LEAMAEKVQH LANVYCTGKL SQQVTQFGRE MEELRQAIRV RLRNLQDAAK DMKKFEGELR
     NLQVALEQAQ TILTSPEVGR RSLKEQLCHR QHLLSEMESL KPKMQAVQLC QSALRIPEDV
     VASLPLCHAA LRLQEEASQL QHTAIQQCNI MQAKKHSLIF PPKEAVVQYE QYKQEMKHLQ
     QLIEEAHREI EDKPVATSNI QELQAQISLH EELAQKIKGY QEQIDSLNSK CKMLTMKAKH
     ATMLLTVTEV EGLAEGTEDL DRELHPTPSA HPSVVMMTAG RCHTLLSPVT EESGEEGTNS
     EISSPPACRS PSPVANTEAA VNQDIAYYQA LSAEGLQTDA ARIPPSAAVS QELYEPGLEP
     SATAKLGDLQ RSWETLKNVI SEKQRTLYEV LERQQKYQDS LQSISTKMEA MEMKLGESLE
     PSRSPESQMA EHQALMDEVQ MLQDEINGLQ VSLAEELVAE SQESDPAEQL ALQSTLTVLA
     ERMSTIRMKA AGKRQLLEEK LSDQLEEQRQ EQALQRYRCE ADELDHWLLN TKATLDVALG
     TSQEPMDMDA QLVDCQNMLV EIEQKVVALS QLSVHNENLL LEGKAHTKEE AEQLAVKLRL
     LKGSLGELQR ALHDRQLDMQ GVTQEKEEND VDFTDTQSPG VQEWLAQART TRTHQRQSSL
     QQQKEFEQEL AEQKSLLRSV ASRGEEILTQ HSTAEGSGGL GEKPDVLSQE LGIAEDQMRV
     KWESLHQEFS AKQKLLQNIL EQEQEQVLYS SPNRLLSGVL PFRGEAQTQD KTSVTSLLDG
     LSQAFGEASS QSGGTDRQSI HLEQKLYDGV SATSTWLNDV EERLFVATAP LPEETEACLF
     NQEALAKDIK EMSEEMDKNK NLFSQAFPED SDNRDVIEDT LGCLLGRLSL LDSVVDQRCH
     QMKERLQQIL RFQNDLKVLF TSLADSKYII LQKLANVFEQ PIVEQMQAIQ QAEEGLRDLE
     GGISELKRWA DKLQVEQSAV QELSKLQDMY DELLMTVSSR RSSLHQNLAL KSQYDKALQD
     LVDLLDTGQE KMTGDQKIIV CSKEEIQQLL GKHKEYFQGL ESHMILTEIL FRKIVGFAAV
     KETQFHTDCM AQASAVLKQA HKRGVELEYI LEMWSHLDEN RQELSRQLEV IENSIPSVGL
     VEESEDRLVE RTNLYQHLKS SLNEYQPKLY QALDDGKRLL MSVSCSELES QLNQLGEHWL
     SNTNKVSKEL HRLETILKHW TRYQSEAAAL NHWLQCAKDR LAFWTQQSVT VPQELEMVRD
     HLSAFLEFSK EVDAKSALKS SVTSTGNQLL RLKKVDTAAL RAELSRMDSQ WTDLLTGIPV
     VQEKLHQLQM DKLPSRHAIS EVMSWISLME SVILKDEEDI RNAIGYKAIH EYLQKYKGFK
     IDLNCKQLTA DFVNQSVLQI SSQDVESKRS DKTDFAEQLG AMNKSWQLLQ GRVGEKIQML
     EGLLESWSEY ENSVQSLKAW FANQERKLKE QHLLGDRNSV ENALKDCQEL EDLIKAKEKE
     VEKIEQNGLA LIQNKREEVS GSVMSTLQEL RQTWISLDRT VEQLKIQLTS ALGQWSNHKA
     ACDEINGHLM EARYSLSRFR LLTGSSEAVQ VQVDNLQNLH DELEKQEGGL QKFGSITNQL
     LKECHPPVAE TLSSTLQEVN MRWNNLLEEI AEQLHSSKAL LQLWQRYKDY SKQCASAIQR
     QEEQTSVLLK AATNKDIADD EVTKWIQDCN DLLKGLETVK DSLFILRELG EQLGQQVDVS
     AAAAIQCEQL CFSQRLGALE QALCKQQAVL QAGVVDYETF AKSLEALEVW MVEAEGILQG
     QDPTHSSDLS TIQERMEELK GQMLKFSSLA PDLDRLNELG YRLPLNDKEI KRMQNLNRHW
     SLTSSQTTER FSKLQSFLLQ HQTFLEKCET WMEFLVQTEH KLAVEISGNY QHLLEQQRAH
     ELFQAEMFSR QQILHSIIVD GQNLLEQGQV DDREEFSLKL TLLSNQWQGV IRRAQQRRGI
     IDSQIRQWQR YREMAEKLRK WLAEVSHLPL SGLGNIPVPL QQVRMLFDEV QFKEKVFLRQ
     QGSYILTVEA GKQLLLSADS GAEAALQAEL TDIQEKWKAA SMHLEEQKKK LAFLLKDWEK
     CERGIANSLE KLRMFKKRLS QPLPDHHEEL HAEQMRCKEL ENAVGRWTDD LTELMLVRDA
     LAVYLSAEDI SMLKERVELL QRQWEELCHQ VSLRRQQVSE RLNEWAVFSE KNKELCEWLT
     QMESKVSQNG DILIEEMIEK LKKDYQEEIA VAQENKIQLQ EMGERLAKAS HESKASEIQY
     KLSRVKDRWQ HLLDLMAARV KKLKETLVAV QQLDKNMGSL RTWLAHMESE LAKPIVYDSC
     NSEEIQRKLN EQQELQRDIE KHSTGVASVL NLCEVLLHDC DACATDAECD SIQQATRNLD
     RRWRNICAMS MERRLKIEET WRLWQKFLDD YSRFEDWLEV SERTAAFPSS SGVLYTVAKE
     ELKKFEAFQR QVHESLTQLE LINKQYRRLA RENRTDSACS LRQMVHGGNQ RWDDLQKRVT
     SILRRLKHFI SQREEFETAR DSILVWLTEM DLQLTNIEHF SECDVQAKIK QLKAFQQEIS
     LNHNKIEQII AQGEQLIEKS EPLDAAVIEE ELDELRRYCQ EVFGRVERYH KKLIRLPVRL
     PDDHDLSDRE LDLEDSTALS DLRWQDPSAD GMPSPQPSSN PSLSLPQPLR SERSGRDTPA
     SVDSIPLEWD HDYDLSRDLE SASRTLPSED EEGEEDKEFY LRGAVGLSGD PSSLESQMRQ
     LDKALDDSRF QIQQTANILR SKTPTGPDLD TSYKGYMKLL GECSGSIDSV RRLEHKLAEE
     ESFPGFVNLN STETQTAGVI DRWELLQAQA MSKELRMKQN LQKWQQFNSD LNNIWAWLGE
     TEEELDRLQH LALSTDIHTI ESHIKKLKEL QKAVDHRKAI ILSINLCSSE FTQADSKESH
     DLQDRLSQMN GRWDRVCSLL EDWRGLLQDA LMQCQEFHEM SHALLLMLEN IDRRKNEIVP
     IDSTLDPETL QDHHKQLMQI KQELLKSQLR VASLQDMSRQ LLVNAEGSDC LEAKEKVHVI
     GNRLKLLLKE VSHHIKDLEK LLDMSSSQQD LSSWSSADEL DTSGSVSPTS GRSTPNRQKS
     PRGKCSLSQP GPSVSSPKSR STRDGSDSSR SDPRPERVGR AFLFRILRAA LPFQLLLLLL
     IGLTCLVPMS EKDYSCALSN NFARSFHPML RYTNGPPPL
//
ID   Q6ZWS7_MOUSE            Unreviewed;       495 AA.
AC   Q6ZWS7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Camk2g;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Forelimb;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Forelimb;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Forelimb;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Forelimb;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Forelimb;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Forelimb;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Forelimb;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Forelimb;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK031213; BAC27303.1; -; mRNA.
DR   IPI; IPI00228045; -.
DR   RefSeq; NP_001034228.1; NM_001039139.1.
DR   UniGene; Mm.235182; -.
DR   ProteinModelPortal; Q6ZWS7; -.
DR   SMR; Q6ZWS7; 3-302, 355-489.
DR   STRING; Q6ZWS7; -.
DR   PRIDE; Q6ZWS7; -.
DR   Ensembl; ENSMUST00000100837; ENSMUSP00000098398; ENSMUSG00000021820.
DR   GeneID; 12325; -.
DR   KEGG; mmu:12325; -.
DR   CTD; 12325; -.
DR   MGI; MGI:88259; Camk2g.
DR   HOVERGEN; HBG108055; -.
DR   NextBio; 280908; -.
DR   ArrayExpress; Q6ZWS7; -.
DR   Bgee; Q6ZWS7; -.
DR   Genevestigator; Q6ZWS7; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:InterPro.
DR   GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; IMP:MGI.
DR   InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF08332; CaMKII_AD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding.
SQ   SEQUENCE   495 AA;  55961 MW;  168EA409723DF4C4 CRC64;
     MATTATCTRF TDDYQLFEEL GKGAFSVVRR CVKKTSTQEY AAKIINTKKL SARDHQKLER
     EARICRLLKH PNIVRLHDSI SEEGFHYLVF DLVTGGELFE DIVAREYYSE ADASHCIHQI
     LESVNHIHQH DIVHRDLKPE NLLLASKCKG AAVKLADFGL AIEVQGEQQA WFGFAGTPGY
     LSPEVLRKDP YGKPVDIWAC GVILYILLVG YPPFWDEDQH KLYQQIKAGA YDFPSPEWDT
     VTPEAKNLIN QMLTINPAKR ITADQALKHP WVCQRSTVAS MMHRQETVEC LRKFNARRKL
     KGAILTTMLV SRNFSAAKSL LNKKSDGGVK EPQTTVVHNA TDGIKGSTES CNTTTEDEDL
     KVRKQEIIKI TEQLIEAINN GDFEAYTKIC DPGLTSFEPE ALGNLVEGMD FHKFYFENLL
     SKNSKPIHTT ILNPHVHVIG EDAACIAYIR LTQYIDGQGR PRTSQSEETR VWHRRDGKWL
     NVHYHCSGAP AAPLQ
//
ID   RS27_MOUSE              Reviewed;          84 AA.
AC   Q6ZWU9; Q3TLE3;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=40S ribosomal protein S27;
GN   Name=Rps27;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Head, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N-3; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-31, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (Potential).
CC   -!- SIMILARITY: Belongs to the ribosomal protein S27e family.
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DR   EMBL; AK014294; BAB29250.1; -; mRNA.
DR   EMBL; AK088320; BAC40279.1; -; mRNA.
DR   EMBL; AK166551; BAE38849.1; -; mRNA.
DR   EMBL; BC048352; AAH48352.1; -; mRNA.
DR   EMBL; BC055693; AAH55693.1; -; mRNA.
DR   IPI; IPI00173160; -.
DR   RefSeq; NP_001177187.1; NM_001190258.1.
DR   RefSeq; NP_081291.1; NM_027015.4.
DR   UniGene; Mm.270283; -.
DR   UniGene; Mm.371611; -.
DR   UniGene; Mm.458329; -.
DR   ProteinModelPortal; Q6ZWU9; -.
DR   SMR; Q6ZWU9; 31-80.
DR   MINT; MINT-1212966; -.
DR   STRING; Q6ZWU9; -.
DR   PhosphoSite; Q6ZWU9; -.
DR   PRIDE; Q6ZWU9; -.
DR   Ensembl; ENSMUST00000053150; ENSMUSP00000060523; ENSMUSG00000050621.
DR   GeneID; 100043813; -.
DR   GeneID; 57294; -.
DR   KEGG; mmu:100043813; -.
DR   KEGG; mmu:57294; -.
DR   UCSC; uc008qbl.1; mouse.
DR   CTD; 57294; -.
DR   MGI; MGI:1888676; Rps27.
DR   eggNOG; roNOG17386; -.
DR   GeneTree; ENSGT00390000013514; -.
DR   HOGENOM; HBG392194; -.
DR   HOVERGEN; HBG000252; -.
DR   InParanoid; Q6ZWU9; -.
DR   OMA; FINIICK; -.
DR   OrthoDB; EOG4H19XB; -.
DR   PhylomeDB; Q6ZWU9; -.
DR   NextBio; 457172; -.
DR   ArrayExpress; Q6ZWU9; -.
DR   Bgee; Q6ZWU9; -.
DR   CleanEx; MM_RPS27; -.
DR   Genevestigator; Q6ZWU9; -.
DR   GermOnline; ENSMUSG00000050621; Mus musculus.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR000592; Ribosomal_S27e.
DR   InterPro; IPR011332; Ribosomal_zn-bd_dom.
DR   PANTHER; PTHR11594; Ribosomal_S27E; 1.
DR   Pfam; PF01667; Ribosomal_S27e; 1.
DR   ProDom; PD004466; Ribosomal_S27e; 1.
DR   SUPFAM; SSF57829; Ribosomal_zn-bd; 1.
DR   PROSITE; PS01168; RIBOSOMAL_S27E; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Metal-binding; Phosphoprotein; Ribonucleoprotein;
KW   Ribosomal protein; Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2     84       40S ribosomal protein S27.
FT                                /FTId=PRO_0000149052.
FT   ZN_FING      38     60       C4-type.
FT   MOD_RES       5      5       N6-acetyllysine (By similarity).
FT   MOD_RES      11     11       Phosphoserine.
FT   MOD_RES      27     27       Phosphoserine (By similarity).
FT   MOD_RES      30     30       Phosphoserine (By similarity).
FT   MOD_RES      31     31       Phosphotyrosine.
FT   MOD_RES      78     78       Phosphoserine (By similarity).
SQ   SEQUENCE   84 AA;  9461 MW;  242C4466AC8A8900 CRC64;
     MPLAKDLLHP SPEEEKRKHK KKRLVQSPNS YFMDVKCPGC YKITTVFSHA QTVVLCVGCS
     TVLCQPTGGK ARLTEGCSFR RKQH
//
ID   Q6ZWX2_MOUSE            Unreviewed;        44 AA.
AC   Q6ZWX2;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-FEB-2011, entry version 50.
DE   SubName: Full=Putative uncharacterized protein;
DE   SubName: Full=Thymosin, beta 4, X chromosome;
DE   SubName: Full=Thymosin, beta 4, X chromosome, isoform CRA_a;
GN   Name=Tmsb4x; ORFNames=RP23-139P21.1-001, mCG_115770;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Thymus, Stomach, and Lung;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Thymus, Stomach, and Lung;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Thymus, Stomach, and Lung;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Thymus, Stomach, and Lung;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Thymus, Stomach, and Lung;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Thymus, Stomach, and Lung;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Thymus, Stomach, and Lung;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Adachi J., Aizawa K., Akahira S., Akimura T., Arai A., Aono H.,
RA   Arakawa T., Bono H., Carninci P., Fukuda S., Fukunishi Y., Furuno M.,
RA   Hanagaki T., Hara A., Hayatsu N., Hiramoto K., Hiraoka T., Hori F.,
RA   Imotani K., Ishii Y., Itoh M., Izawa M., Kasukawa T., Kato H.,
RA   Kawai J., Kojima Y., Konno H., Kouda M., Koya S., Kurihara C.,
RA   Matsuyama T., Miyazaki A., Nishi K., Nomura K., Numazaki R., Ohno M.,
RA   Okazaki Y., Okido T., Owa C., Saito H., Saito R., Sakai C., Sakai K.,
RA   Sano H., Sasaki D., Shibata K., Shibata Y., Shinagawa A., Shiraki T.,
RA   Sogabe Y., Suzuki H., Tagami M., Tagawa A., Takahashi F., Tanaka T.,
RA   Tejima Y., Toya T., Yamamura T., Yasunishi A., Yoshida K., Yoshino M.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RA   Brown J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [11]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD, and C57BL/6J; TISSUE=Thymus, Stomach, and Lung;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [13]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II;
RC   TISSUE=Mammary tumor metastatized to lung. Tumor arose spontaneously;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC018286; AAH18286.1; -; mRNA.
DR   EMBL; AK010659; BAB27097.1; -; mRNA.
DR   EMBL; AK162286; BAE36832.1; -; mRNA.
DR   EMBL; AK169108; BAE40890.1; -; mRNA.
DR   EMBL; AK169718; BAE41328.1; -; mRNA.
DR   EMBL; AL731735; CAM14945.1; -; Genomic_DNA.
DR   EMBL; CH466571; EDL40711.1; -; Genomic_DNA.
DR   EMBL; CH466571; EDL40712.1; -; Genomic_DNA.
DR   EMBL; CH466571; EDL40714.1; -; Genomic_DNA.
DR   IPI; IPI00228757; -.
DR   RefSeq; NP_067253.1; NM_021278.2.
DR   UniGene; Mm.142729; -.
DR   UniGene; Mm.409203; -.
DR   ProteinModelPortal; Q6ZWX2; -.
DR   SMR; Q6ZWX2; 2-42.
DR   STRING; Q6ZWX2; -.
DR   PRIDE; Q6ZWX2; -.
DR   Ensembl; ENSMUST00000056887; ENSMUSP00000053093; ENSMUSG00000049775.
DR   Ensembl; ENSMUST00000112172; ENSMUSP00000107795; ENSMUSG00000049775.
DR   Ensembl; ENSMUST00000112175; ENSMUSP00000107797; ENSMUSG00000049775.
DR   Ensembl; ENSMUST00000112176; ENSMUSP00000107798; ENSMUSG00000049775.
DR   GeneID; 19241; -.
DR   KEGG; mmu:19241; -.
DR   UCSC; uc009uwx.1; mouse.
DR   CTD; 19241; -.
DR   MGI; MGI:99510; Tmsb4x.
DR   GeneTree; ENSGT00390000007040; -.
DR   HOVERGEN; HBG012534; -.
DR   InParanoid; Q6ZWX2; -.
DR   NextBio; 296050; -.
DR   ArrayExpress; Q6ZWX2; -.
DR   Bgee; Q6ZWX2; -.
DR   Genevestigator; Q6ZWX2; -.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0030334; P:regulation of cell migration; IDA:MGI.
DR   GO; GO:0042989; P:sequestering of actin monomers; IEA:InterPro.
DR   InterPro; IPR001152; Thymosin_b4.
DR   InterPro; IPR016323; Thymosin_b4_chordata.
DR   Gene3D; G3DSA:1.20.5.520; Thymosin_b4; 1.
DR   Pfam; PF01290; Thymosin; 1.
DR   PIRSF; PIRSF001828; Thymosin_beta; 1.
DR   ProDom; PD005116; Thymosin_b4; 1.
DR   SMART; SM00152; THY; 1.
DR   PROSITE; PS00500; THYMOSIN_B4; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   44 AA;  5053 MW;  440C6158482DAAD0 CRC64;
     MSDKPDMAEI EKFDKSKLKK TETQEKNPLP SKETIEQEKQ AGES
//
ID   IF2A_MOUSE              Reviewed;         315 AA.
AC   Q6ZWX6; Q3TIQ0;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Eukaryotic translation initiation factor 2 subunit 1;
DE   AltName: Full=Eukaryotic translation initiation factor 2 subunit alpha;
DE            Short=eIF-2-alpha;
DE            Short=eIF-2A;
DE            Short=eIF-2alpha;
GN   Name=Eif2s1; Synonyms=Eif2a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N; TISSUE=Eye, Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION IN AN EIF2 COMPLEX WITH CELF1; EIF2S2; CALR; CALR3;
RP   HSPA5 AND HSP90B1.
RX   PubMed=16931514; DOI=10.1074/jbc.M605701200;
RA   Timchenko L.T., Salisbury E., Wang G.-L., Nguyen H., Albrecht J.H.,
RA   Hershey J.W., Timchenko N.A.;
RT   "Age-specific CUGBP1-eIF2 complex increases translation of
RT   CCAAT/enhancer-binding protein beta in old liver.";
RL   J. Biol. Chem. 281:32806-32819(2006).
CC   -!- FUNCTION: Functions in the early steps of protein synthesis by
CC       forming a ternary complex with GTP and initiator tRNA. This
CC       complex binds to a 40S ribosomal subunit, followed by mRNA binding
CC       to form a 43S preinitiation complex. Junction of the 60S ribosomal
CC       subunit to form the 80S initiation complex is preceded by
CC       hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP
CC       binary complex. In order for eIF-2 to recycle and catalyze another
CC       round of initiation, the GDP bound to eIF-2 must exchange with GTP
CC       by way of a reaction catalyzed by eIF-2B (By similarity).
CC   -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma
CC       chain. Interacts with ABCF1. Associates with ribosomes (By
CC       similarity). Component of an EIF2 complex at least composed of
CC       CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5.
CC   -!- INTERACTION:
CC       P62137:Ppp1ca; NbExp=1; IntAct=EBI-1202234, EBI-357187;
CC       P63087-1:Ppp1cc; NbExp=1; IntAct=EBI-1202234, EBI-450267;
CC   -!- PTM: Substrate for at least 4 kinases: EIF2AK3/PERK, GCN2, HRI and
CC       PKR. Phosphorylation stabilizes the eIF-2/GDP/eIF-2B complex and
CC       prevents GDP/GTP exchange reaction, thus impairing the recycling
CC       of eIF-2 between successive rounds of initiation and leading to
CC       global inhibition of translation (By similarity).
CC   -!- SIMILARITY: Belongs to the eIF-2-alpha family.
CC   -!- SIMILARITY: Contains 1 S1 motif domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK010592; BAB27049.1; -; mRNA.
DR   EMBL; AK143499; BAE25400.1; -; mRNA.
DR   EMBL; AK167763; BAE39796.1; -; mRNA.
DR   EMBL; BC005463; AAH05463.1; -; mRNA.
DR   EMBL; BC016448; AAH16448.1; -; mRNA.
DR   EMBL; BC016497; AAH16497.1; -; mRNA.
DR   IPI; IPI00474446; -.
DR   RefSeq; NP_080390.1; NM_026114.3.
DR   UniGene; Mm.196220; -.
DR   ProteinModelPortal; Q6ZWX6; -.
DR   SMR; Q6ZWX6; 4-303.
DR   IntAct; Q6ZWX6; 10.
DR   STRING; Q6ZWX6; -.
DR   PRIDE; Q6ZWX6; -.
DR   Ensembl; ENSMUST00000071230; ENSMUSP00000071214; ENSMUSG00000021116.
DR   GeneID; 13665; -.
DR   KEGG; mmu:13665; -.
DR   UCSC; uc007nzk.1; mouse.
DR   CTD; 13665; -.
DR   MGI; MGI:95299; Eif2s1.
DR   eggNOG; roNOG13172; -.
DR   HOGENOM; HBG499933; -.
DR   HOVERGEN; HBG001910; -.
DR   InParanoid; Q6ZWX6; -.
DR   OMA; TNCRFYE; -.
DR   OrthoDB; EOG4BZN35; -.
DR   PhylomeDB; Q6ZWX6; -.
DR   NextBio; 284416; -.
DR   ArrayExpress; Q6ZWX6; -.
DR   Bgee; Q6ZWX6; -.
DR   CleanEx; MM_EIF2A; -.
DR   Genevestigator; Q6ZWX6; -.
DR   GermOnline; ENSMUSG00000021116; Mus musculus.
DR   GO; GO:0005850; C:eukaryotic translation initiation factor 2 complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR   GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR   GO; GO:0043558; P:regulation of translational initiation in response to stress; IDA:MGI.
DR   InterPro; IPR011488; EIF_2_alpha.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR016027; NA-bd_OB-fold-like.
DR   InterPro; IPR003029; Rbsml_prot_S1_RNA-bd_dom.
DR   InterPro; IPR022967; RNA-binding_domain_S1.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   Pfam; PF07541; EIF_2_alpha; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR   PROSITE; PS50126; S1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW   RNA-binding; Translation regulation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    315       Eukaryotic translation initiation factor
FT                                2 subunit 1.
FT                                /FTId=PRO_0000137383.
FT   DOMAIN       17     88       S1 motif.
FT   MOD_RES      49     49       Phosphoserine; by HRI (By similarity).
FT   MOD_RES      52     52       Phosphoserine; by EIF2AK3, GCN2, HRI and
FT                                PKR (By similarity).
FT   MOD_RES     141    141       N6-acetyllysine (By similarity).
SQ   SEQUENCE   315 AA;  36108 MW;  018480B89175D118 CRC64;
     MPGLSCRFYQ HKFPEVEDVV MVNVRSIAEM GAYVSLLEYN NIEGMILLSE LSRRRIRSIN
     KLIRIGRNEC VVVIRVDKEK GYIDLSKRRV SPEEAIKCED KFTKSKTVYS ILRHVAEVLE
     YTKDEQLESL FQRTAWVFDD KYKRPGYGAY DAFKHAVSDP SILDSLDLNE DEREVLINNI
     NRRLTPQAVK IRADIEVACY GYEGIDAVKE ALRAGLNCST ETMPIKINLI APPRYVMTTT
     TLERTEGLSV LNQAMAVIKE KIEEKRGVFN VQMEPKVVTD TDETELARQL ERLERENAEV
     DGDDDAEEME AKAED
//
ID   AKAP9_MOUSE             Reviewed;        3797 AA.
AC   Q70FJ1; Q3TH74; Q80TR6;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   08-MAR-2011, entry version 41.
DE   RecName: Full=A-kinase anchor protein 9;
DE            Short=AKAP-9;
DE   AltName: Full=Protein kinase A-anchoring protein 9;
DE            Short=PRKA9;
GN   Name=Akap9; Synonyms=Kiaa0803;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=BALB/c; TISSUE=Brain;
RA   Kemmner W.A.;
RT   "Cloning mouse AKAP9.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-582 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Binds to type II regulatory subunits of protein kinase
CC       A. Scaffolding protein that assembles several protein kinases and
CC       phosphatases on the centrosome and Golgi apparatus. May be
CC       required to maintain the integrity of the Golgi apparatus (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with the regulatory region of protein kinase N
CC       (PKN), protein phosphatase 2A (PP2A), protein phosphatase 1 (PP1)
CC       and the immature non-phosphorylated form of PKC epsilon. Interacts
CC       with chloride intracellular channel proteins CLIC1, CLIC4 and
CC       CLIC5 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytoskeleton, centrosome (By similarity). Golgi apparatus (By
CC       similarity). Note=Cytoplasmic in parietal cells (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q70FJ1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q70FJ1-2; Sequence=VSP_039481;
CC         Note=Incomplete sequence;
CC       Name=3;
CC         IsoId=Q70FJ1-3; Sequence=VSP_039482;
CC         Note=Incomplete sequence;
CC   -!- DOMAIN: RII-binding site, predicted to form an amphipathic helix,
CC       could participate in protein-protein interactions with a
CC       complementary surface on the R-subunit dimer (By similarity).
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AJ582913; CAE46960.1; -; mRNA.
DR   EMBL; AK122374; BAC65656.2; -; Transcribed_RNA.
DR   EMBL; AK168404; BAE40324.1; -; mRNA.
DR   IPI; IPI00623749; -.
DR   IPI; IPI00968897; -.
DR   IPI; IPI00969009; -.
DR   RefSeq; NP_919444.2; NM_194462.2.
DR   UniGene; Mm.46044; -.
DR   IntAct; Q70FJ1; 1.
DR   STRING; Q70FJ1; -.
DR   PhosphoSite; Q70FJ1; -.
DR   PRIDE; Q70FJ1; -.
DR   Ensembl; ENSMUST00000044492; ENSMUSP00000046129; ENSMUSG00000040407.
DR   GeneID; 100986; -.
DR   KEGG; mmu:100986; -.
DR   UCSC; uc008wid.1; mouse.
DR   CTD; 100986; -.
DR   MGI; MGI:2178217; Akap9.
DR   eggNOG; roNOG12395; -.
DR   HOGENOM; HBG507066; -.
DR   HOVERGEN; HBG050481; -.
DR   InParanoid; Q70FJ1; -.
DR   OrthoDB; EOG4SBDX1; -.
DR   NextBio; 354718; -.
DR   ArrayExpress; Q70FJ1; -.
DR   Bgee; Q70FJ1; -.
DR   Genevestigator; Q70FJ1; -.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000242; C:pericentriolar material; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR019528; PACT_domain.
DR   Pfam; PF10495; PACT_coil_coil; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Golgi apparatus.
FT   CHAIN         1   3797       A-kinase anchor protein 9.
FT                                /FTId=PRO_0000395481.
FT   REGION     2498   2510       PKA-RII subunit binding domain (By
FT                                similarity).
FT   COILED      140    607       Potential.
FT   COILED      640    976       Potential.
FT   COILED     1808   2377       Potential.
FT   COILED     2975   3325       Potential.
FT   COMPBIAS    220    281       Gln-rich.
FT   COMPBIAS   3143   3337       Gln-rich.
FT   VAR_SEQ     104    121       Missing (in isoform 2).
FT                                /FTId=VSP_039481.
FT   VAR_SEQ    3436   3454       Missing (in isoform 3).
FT                                /FTId=VSP_039482.
FT   CONFLICT     62     62       S -> N (in Ref. 1; CAE46960).
FT   CONFLICT   2388   2388       S -> L (in Ref. 1; CAE46960).
FT   CONFLICT   2775   2775       L -> Q (in Ref. 1; CAE46960).
SQ   SEQUENCE   3797 AA;  436214 MW;  CA30D11FF5696124 CRC64;
     MEDEERQRKL AAGKAKLARF RQRKAQYDGD IPKKQKKKRT SSSKHDSSLH TDQQSGELCS
     ESSQRVDLAG NPDCSGPERK HGQVFSAEPE SEISTTADEC SSEINGCNSV MKPRKPTDPL
     REEEFSLDDS SSEQGAQSSQ TCLQMVEKEL AEKQHDIEEL TQELEEMRAS FGTEGLKQLQ
     EFEAAIKQRD GIITQLTANL QQARREKDDT MVEFLELTEQ SQKLQIQFQH LQANETLQNS
     TLSRTATDLL QAKRQIFTQQ QQLQDYQKKE EDLQAQISFL QEKLRAFEME KDRKIENLNA
     KEIQEKQALI DELNTRVVEE EKKTVELKNK VTTADELLGG LHEQLTQRNQ EIQSLKLELG
     NSQQNERKCS EEIKELMRTV EELQKRNLKD SWLETSAVRR VEQETQRKLS HLQAELDEMY
     GKQIVQMKQE LINQHMSQIE ELKSQHKREM ENTLKSDTNA AISKEQVNLM NAAINELNVR
     LQETHAQKEE LKGELGVVLG EKSALQSQSN DLLEEVRFLR EQVQKARQTI AEQENRLSEA
     RKSLSTVEDL KAEIVAASES RKELELKHEA EITNYKIKLE MLEKEKNAVL DRMAESQEAE
     LERLRTQPLF SHEEELSKLK EDLEVEHRIN IEKLKDNLGI HYKQQIDGLQ NEMNRKMESM
     QCETDNLITQ QNQLILENSK LRDLQECLVN SKSEEMNLQI NELQKEIEIL KQEEKEKGTL
     EQEVQELQLK TEQLEKQLKE KEDDLQEKCA QLDAENNILK EEKRVLEDKL KMYSPSEQEE
     RSIAVDPSTS KLADSRWQKE VAMLRKETED LQQQCLYLNE EIEKQRNTFA FAEKNFEVNY
     QELQREYTCL LKIRDDLEAT QTKQALEYES KLRALEEELL SKRGNPXAPK GKSSGIFPSE
     TLEIGEVVEK DTTELMEKLE VTKREKLELS EKVSGLSEQL KQTHCTINSL SAEXRALKQE
     KEQLLLRCGE LELLANPSGT ENAAVCPVQM SSYQAGLVMG KVGDSGGSIS KISKDLAEES
     KPMIEDKIPF KESGREQLLL PTRAQEPSHA TVEPCESEKL QQELHALKAE QDDLRLQMEA
     QRICLFVVYS THADQVRAHM EKEREEALCS LKDELISAQQ KKIDELHKMH QCQLQNVKIQ
     ETGDEPLQVL IERLQKAVSE KCFHISKTLN NVFDECYTPL KCEMNIEEKE NSGVYTSQNQ
     SPELQEYRYE VQDFQESMQV LLGKVTEECR KLSGLQTRLG KIHEQQTDGV ALEFAEQNAA
     EEEAGLLSGC SQSALQSTDV SLESKVSSLP ASEKNRECER QVQELQSPVA AGQLQLTETE
     ASHRAEIECL QQRLEAASEA PVQPSLSIDS VVFKGSGAQK PVYCGSCLRE YVDGTAKFSD
     RFEVRQETNM VNLMEKQYQE RLEEEIAKVI VSMSIAFAQQ TELSRLSEGK ENTIQSEQAH
     TLCSQNKHQL NDITSQSQVG LQTFEATDKB FKEEFKPLSK ELGEYRKAVP LSSHDDLDDI
     LKSEEHGLAI SEEIFSKDET FIVRKSMHDE VLVSSMDTSR QLILNEQLED MRQELVRQYE
     EHQQATEMLR QAHMQQMERQ REDQEQLQEE IKRLNEQLTQ KSSIDTEHVV SERERVLLEE
     LEALKQLPLA GRKELCCELR HSSTQTQDGH DDQEVEEQTL KDKTLERSPE DALLDRNLSN
     ERYALKKANN RLLKILLEVV KTTSAAEETI GRHVLGILDR SSKGQTASSL LWRSEADASA
     TTCAPEDCAR AMDESIPSYP GTAIATHDSI WSKVTEEGAE LSQRLVRSGF AGPVIDPENE
     ELMLNISSRL QAAVEKLLEA ISETNTQLEH AKVTQTELMR ESFRQKQEAT ESLHCLEELR
     ERLQEESRAR EQLAEELNKA ESVIDGYSDE KTLFERQIQE KTDIIEHLEQ EVLCMNNRLQ
     ELESDQRRVE EERQLLCRQR EAMRAEAGPV EQQFLQETEK LMKEKLEVQC QAEKVRGDLQ
     KQVKALEIDV EEQVSRFIEL EQEKNAELTD LRQQSQALEK QLEKMRKFLD EQAIDREHER
     DVFQQEIQKL EHQLKAAPRI QPVSEHQARE VEQLTNHLKE KTDRCSELLL SKEQLQRDIQ
     ERNEEIEKLE CRVRELEQAL LASAEPFPKV EDQKRSGAVA ADPELSLEVQ LQAERDATDR
     KQKEITNLEE QLEQFREELE NKNDEVQELL MQLEIQRKES TTRLQELQQE NRLFKDEIEK
     LGFAMKESDS VSTRDQPMLF GKFAQLIQEK EIEIDRLNEQ FIKLQQQLKL TTDNKVIEEQ
     KEQIQDLETQ IERLMSEREH EKKQREEEVE QLTGVVEKLQ QEVVSTEQQR EGARTLPEDE
     ESFKHQLDKV TAEKLVLEQQ VETTNQVMTH MNNVLKEINF KMDQITQSLC NLNKECASNE
     ELPSLPKESV HMTVHELGSD NLQPEDAPAQ DVTKPLEKQT SLTRLQESPE ASRTQEIESL
     ASSVGAKDVE LTQCREQTET IQEQAQSETD RLQKKLTDLQ RSLEKFAAAL VSQVQMEAAQ
     EYVPFHQEKQ PVSSAPGSTD IQNANGLTGA STESLIPTVT LRLAEVESRV AEVHSGTMSE
     KLVGIVGGNA SETEKRVIEL QKLLEEAEER PEEGGEQSSR DGEVRESYMT SLQKDLGQVK
     DPLTEAKEKL SYSLEKEKRT GEQESREAPI PEPPSVEVGG CSGLTERTDK VSSSGNQTLQ
     ILLRDAAIQT DLQSESSQEE VRDTINQLTK KMEHIQELHA AEILDMESRH ILETESLKKE
     HYVAIQLLTK ECETLKEMTQ CLRCKEGSSI PELADSVAYQ SREVYSSDSE SDWGQSQGFD
     TAIEGREEGE TSADLFPKKI KGLVKAVHSE GMQVLSLSSP LCDDGEDRSI QQLSESWLKE
     RQAYLNTISS LKDLISKMQV RRETEVYDRC HLSDWRGELL LACQRVFIKE RSVLLATFQT
     ELTSLSTRDV DGLLNSLEQR IQEQGIEYHT AMDCLQKADR RSLLAEIEDL RAQINGGKMT
     LEREQGTEKS SQELLDCSMQ QKQSLEMQLE LSSLRDRAAE LQEQLSSEKM VVAELKSELA
     QAKLELGTTL KAQHKRLKEL EAFRSEVKEK TDEIHFLSDT LAREQKNSLE LQWALEKEKA
     RSGHHEEREK EELEDLKFSL EDQKRRNTQL NLLLEQQKQL LNESQQKIES QKMLHDAQLS
     EEQGRNLGLQ ALLESEQVRI QEMKSTLDKE RELYAQLQSR EDGGQPPPAL PSEDLLKELQ
     KQLEEKHSRI VELLSETEKY KLDSLQTRQQ MEKDRQVHQK TLQTEQEANT QGQKKMQELQ
     SKVEELQRQL QEKRQQVYKL DLEGKRLQGL MQEFQKQELE PEEKPGSRGL VDQNLNEPAT
     WNFTDDRTRN WVLQQKMGEA KDRNFTKLIE INGGELDHNH DLEMIRQTLQ HVASKLQHVA
     QKACSRLQFE TAGDDAFIWI QENIDGIILQ LQKLTGQPGD EHSLGPPSSS CGSLTESLMR
     QNTELTRLIN QLTEEKNTLR SIVIKLEELN RCYWHTGASR DCCSRFSFID PADIEAIIAS
     EKEVWNREKL SLQKALKRAE AKVYKLKAEL RNDALLRNLG PDTDHAALQK IYNKYLRASS
     FRKALIYQKK YLLLLLGGFQ ECEDVTLGVL ARMGGHLALK DSKTITNHPK AFSRFRSAVR
     VSIAISRMKF LVRRWQQVTS TSSININRDG FGLSPGIEKT DPFYHSPGGL ELYGEPRHTM
     YRSRFDLDYP RSLLPLQNRY PGTPGDLNSI SMASSQLHQY NPDKSLTDYV TRLEALRRRL
     GAIQSGSTTQ FHFGMRR
//
ID   SYNEM_MOUSE             Reviewed;        1561 AA.
AC   Q70IV5; Q3UPZ4; Q6A081; Q70IV3; Q70IV4;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 2.
DT   08-FEB-2011, entry version 51.
DE   RecName: Full=Synemin;
DE   AltName: Full=Desmuslin;
GN   Name=Synm; Synonyms=Dmn, Kiaa0353;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Skeletal muscle;
RX   PubMed=15265691; DOI=10.1016/j.yexcr.2004.04.023;
RA   Xue Z., Cheraud Y., Brocheriou V., Izmiryan A., Titeux M., Paulin D.,
RA   Li Z.;
RT   "The mouse synemin gene encodes three intermediate filament proteins
RT   generated by alternative exon usage and different open reading
RT   frames.";
RL   Exp. Cell Res. 298:431-444(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 270-1560 (ISOFORM 1).
RC   TISSUE=Embryonic intestine;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [5]
RP   INTERACTION WITH GFAP AND VIM, SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=17356066; DOI=10.1242/jcs.03423;
RA   Jing R., Wilhelmsson U., Goodwill W., Li L., Pan Y., Pekny M.,
RA   Skalli O.;
RT   "Synemin is expressed in reactive astrocytes in neurotrauma and
RT   interacts differentially with vimentin and GFAP intermediate filament
RT   networks.";
RL   J. Cell Sci. 120:1267-1277(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599 AND SER-1049, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=19124017; DOI=10.1016/j.yexcr.2008.12.009;
RA   Izmiryan A., Franco C.A., Paulin D., Li Z., Xue Z.;
RT   "Synemin isoforms during mouse development: multiplicity of partners
RT   in vascular and neuronal systems.";
RL   Exp. Cell Res. 315:769-783(2009).
CC   -!- FUNCTION: Type-VI intermediate filament (IF) which plays an
CC       important cytoskeletal role within the muscle cell cytoskeleton.
CC       It forms heteropolymeric IFs with desmin and/or vimentin, and via
CC       its interaction with cytoskeletal proteins alpha-dystrobrevin,
CC       dystrophin, talin-1, utrophin and vinculin, is able to link these
CC       heteropolymeric IFs to adherens-type junctions, such as to the
CC       costameres, neuromuscular junctions, and myotendinous junctions
CC       within striated muscle cells (By similarity).
CC   -!- SUBUNIT: Interacts with DES, DMD, DTNA, TLN1, UTRN and VCL (By
CC       similarity). Isoform 1 and isoform 2 interact with GFAP and VIM.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction,
CC       adherens junction (By similarity). Note=There are at least two
CC       distinct SYNM subpopulations, one in which SYMN interacts with DES
CC       within the Z-lines, and another in which it interacts with both
CC       DTNA and DES at the costamere (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=H;
CC         IsoId=Q70IV5-1; Sequence=Displayed;
CC       Name=2; Synonyms=M;
CC         IsoId=Q70IV5-2; Sequence=VSP_053035;
CC       Name=3; Synonyms=L;
CC         IsoId=Q70IV5-3; Sequence=VSP_053033, VSP_053034;
CC   -!- TISSUE SPECIFICITY: Isoform 2 and isoform 3 are detected in adult
CC       skeletal muscle, heart and bladder, whereas isoform 1 is only
CC       detected in adult bladder (at protein level).
CC   -!- DEVELOPMENTAL STAGE: At E11.5, isoform 1 and isoform 2 are widely
CC       expressed in the developing nervous and vascular systems and are
CC       also found specifically associated with vimentin in endothelial
CC       cells. By E15, isoform 1, isoform 2 and isoform 3, are found
CC       coexpressed with neurofilament, peripherin and internexin in the
CC       peripheral nervous system (at protein level). In the developing
CC       embryo, isoform 2 is detected as early as E5, whereas isoform 1 is
CC       first observed at E9 in the nervous system and mesodermic
CC       derivatives. Isoform 3 is observed later in neurons at E15.
CC   -!- INDUCTION: Up-regulated in reactive astrocytes following
CC       neurotrauma (at protein level).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AJ579700; CAE30277.1; -; mRNA.
DR   EMBL; AJ579701; CAE30278.1; -; mRNA.
DR   EMBL; AJ579702; CAE30279.1; -; mRNA.
DR   EMBL; AK143019; BAE25250.1; -; mRNA.
DR   EMBL; AC158296; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK172937; BAD32215.1; -; mRNA.
DR   IPI; IPI00402765; -.
DR   IPI; IPI00411045; -.
DR   IPI; IPI00469184; -.
DR   RefSeq; NP_899135.3; NM_183312.3.
DR   RefSeq; NP_964001.2; NM_201639.2.
DR   RefSeq; NP_997546.2; NM_207663.3.
DR   UniGene; Mm.60526; -.
DR   HSSP; P08670; 1GK7.
DR   ProteinModelPortal; Q70IV5; -.
DR   SMR; Q70IV5; 56-158.
DR   STRING; Q70IV5; -.
DR   PRIDE; Q70IV5; -.
DR   Ensembl; ENSMUST00000074233; ENSMUSP00000073855; ENSMUSG00000030554.
DR   GeneID; 233335; -.
DR   KEGG; mmu:233335; -.
DR   UCSC; uc009hiw.1; mouse.
DR   CTD; 233335; -.
DR   MGI; MGI:2661187; Synm.
DR   GeneTree; ENSGT00560000076873; -.
DR   HOGENOM; HBG277852; -.
DR   HOVERGEN; HBG008974; -.
DR   InParanoid; Q70IV5; -.
DR   OMA; RLCAQEA; -.
DR   PhylomeDB; Q70IV5; -.
DR   ArrayExpress; Q70IV5; -.
DR   Bgee; Q70IV5; -.
DR   Genevestigator; Q70IV5; -.
DR   GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR   GO; GO:0043034; C:costamere; ISS:UniProtKB.
DR   GO; GO:0005882; C:intermediate filament; ISS:UniProtKB.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0060053; C:neurofilament cytoskeleton; IDA:MGI.
DR   GO; GO:0019215; F:intermediate filament binding; IDA:UniProtKB.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0008307; F:structural constituent of muscle; ISS:UniProtKB.
DR   GO; GO:0017166; F:vinculin binding; ISS:UniProtKB.
DR   InterPro; IPR016044; F.
DR   InterPro; IPR001664; IF.
DR   InterPro; IPR018039; Intermediate_filament_CS.
DR   PANTHER; PTHR23239; IF; 1.
DR   Pfam; PF00038; Filament; 1.
DR   PROSITE; PS00226; IF; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Intermediate filament; Phosphoprotein.
FT   CHAIN         1   1561       Synemin.
FT                                /FTId=PRO_0000364438.
FT   REGION        1     10       Head.
FT   REGION       11    320       Interaction with DMD and UTRN (By
FT                                similarity).
FT   REGION       11    300       Rod.
FT   REGION       11     49       Coil 1A.
FT   REGION       50     58       Linker 1.
FT   REGION       59    163       Coil 1B.
FT   REGION      164    186       Linker 12.
FT   REGION      187    300       Coil 2.
FT   REGION      301   1561       Tail.
FT   REGION     1152   1453       Interaction with TLN1 and VCL (By
FT                                similarity).
FT   REGION     1242   1557       Interaction with DMD and UTRN (By
FT                                similarity).
FT   MOD_RES     599    599       Phosphoserine.
FT   MOD_RES     655    655       Phosphoserine (By similarity).
FT   MOD_RES    1044   1044       Phosphoserine (By similarity).
FT   MOD_RES    1049   1049       Phosphoserine.
FT   MOD_RES    1179   1179       Phosphoserine (By similarity).
FT   MOD_RES    1182   1182       Phosphoserine (By similarity).
FT   MOD_RES    1425   1425       Phosphoserine (By similarity).
FT   VAR_SEQ     336    371       EPRNTSYRYTNSVLQRKNEKNLFPRRKTPWAAVNHS -> D
FT                                GFERHESDPQLDPRHRVGSGSSRRVSPWWLENCTQ (in
FT                                isoform 3).
FT                                /FTId=VSP_053033.
FT   VAR_SEQ     372   1561       Missing (in isoform 3).
FT                                /FTId=VSP_053034.
FT   VAR_SEQ    1152   1453       Missing (in isoform 2).
FT                                /FTId=VSP_053035.
FT   CONFLICT    122    122       E -> K (in Ref. 1; CAE30277/CAE30278/
FT                                CAE30279).
FT   CONFLICT    223    223       A -> S (in Ref. 1; CAE30277/CAE30278/
FT                                CAE30279).
FT   CONFLICT    577    577       E -> G (in Ref. 1; CAE30277/CAE30278).
FT   CONFLICT    830    830       Y -> C (in Ref. 1; CAE30277/CAE30278).
FT   CONFLICT    835    835       P -> S (in Ref. 1; CAE30277 and 4;
FT                                BAD32215).
FT   CONFLICT    896    896       A -> T (in Ref. 1; CAE30277/CAE30278).
FT   CONFLICT    993    993       A -> V (in Ref. 1; CAE30277/CAE30278).
FT   CONFLICT   1064   1064       L -> F (in Ref. 1; CAE30277/CAE30278).
FT   CONFLICT   1072   1072       E -> D (in Ref. 1; CAE30277/CAE30278).
FT   CONFLICT   1077   1077       S -> F (in Ref. 1; CAE30277/CAE30278).
FT   CONFLICT   1114   1114       S -> F (in Ref. 1; CAE30277/CAE30278).
FT   CONFLICT   1123   1123       S -> F (in Ref. 1; CAE30277/CAE30278).
FT   CONFLICT   1129   1129       L -> I (in Ref. 1; CAE30277/CAE30278).
FT   CONFLICT   1167   1167       R -> P (in Ref. 1; CAE30277).
FT   CONFLICT   1206   1206       V -> A (in Ref. 1; CAE30277).
FT   CONFLICT   1241   1241       T -> A (in Ref. 1; CAE30277).
FT   CONFLICT   1348   1348       H -> Q (in Ref. 1; CAE30277).
FT   CONFLICT   1499   1499       S -> F (in Ref. 1; CAE30277/CAE30278).
FT   CONFLICT   1556   1556       Missing (in Ref. 1; CAE30277/CAE30278).
SQ   SEQUENCE   1561 AA;  173209 MW;  1DFC4DA574CC6A43 CRC64;
     MLSWRLQTGS EKAELQELNA RLYDYVCRVR ELERENLLLE EELRSRLSRE DRWAEDQALY
     AEEARSLRQQ LDELNWSTAL AEGERDALRR ELLELQREGV EAGTARSRLD AELGAQRREL
     EEALGARAAL EALLGRLETE RRDLDAAHER QVRDLRARAA SLTMHFRARA TSPAAPPPRL
     RDVHDSYALL VAESWRESVQ LYEDEVRELE QALRRGQESR LQAEDEARLC AQEADALRNQ
     ALELEQLRAR LEDELLRMRE EYGMQAEERQ RVIDSLEDEK EALTLAMADR LRDYQELLQV
     KTGLSLEVAT YRALLEGESN PEILIWTENI ENVPQEPRNT SYRYTNSVLQ RKNEKNLFPR
     RKTPWAAVNH SSASYSNWPG HLDSQTTTAV GSAARRGLLT SRHSSSATTS GQQKPLEKTI
     SSRANLRPVT PTHGFLRNTD AQMKTLPHRS KVEGTGDTHA RRATESVITR ESYRGHQGHV
     AAGAVSSTPS NERTVILGKK LEAQATKEQE RDRSGVIRIK PEEKMFDSKE KASEERNLRW
     EELTKLDRDA RKRESRHLRD EAREKEALKE RSVKEREVPI SLEVSRGSRA EVSTIHLQSP
     GRKDVSHSGG REAETKETRF RLDTQDTASS LQSDSTTETI AESIVTTILK QFTQSPGAEE
     EATSFPDTKV TYVDRKEFPG DGKTKTEIVV ESKLTDVVDV SDEAGLDYLL SKDVKEVGLK
     GKSTETMIGE MINLGLKGRE GRAKVVNVEI VEEPMSYIGG GKIDFSTPFQ VEEVDDVSPS
     PKGFVEEEDG EGETHMAFSM RPHQTKQPQG TIPHVEEVTE AGDSEGEQSY FVSTPDEYPG
     GHDREDDGSV YGQIHIEEES TIRYSWQDEI AQGTWRRKMR GDVGGEKPVK VLEVPALSLG
     GAIGSAHLKE EASGELRAEP TVIEKEIKIP HEFHTSIKGV FSSEPRHQLV EVIGQLEETL
     PERMKEELSA LTRQSQGESG SVSVDVKKVQ SAAGGSVTLM AEVNLSQTVD ADQLDLEQLS
     RDEAGEIERA VESVVRESLA KRSSPVPRSP DREDGEEVPA GGILFKRWAT RELYSPSGER
     DDAGQVSPSS DQRVTQGPVS ATVEVTSPTG FVQSHVLEDV SQSVRHVKLG PTEMWRTEQV
     TFGGPTAQVV EVSGDFSEAV SSEGASRSVR HITLGPHQSQ VSTEVIFRGS VPTWQETGDT
     EKPGPVVLSV GADISGSGRM PGSERSHTEK EIRFQGPVSG TAQVGGNFAT EESVGSQTFV
     RSLQLGPKEG FREEIQFIAP IPDKVGWGEE DSEHTKVSLE RATSIQRIDI VPQRYLASKQ
     MAPQTLEFRD SEDMVMVEGS AGTIQATHNF TSDREILQNK ENTFQRVISG SPPDSVGDTG
     AEVTANVSRS FRHIQIGPTE EEPSEYFVTG RPVSKTFVLD GSVASPGLVG GADGGSTPCR
     IALGPKETSF TFQMDLSDTR AIRSWTRDTG SEVEAHGVSH RGGWRIAHSR DERVASTGSG
     ASPGDAHQAP GEKGTEQAGF DKTVQLQRMV DQRSVASDEK KVALLYLDNE EEEEEEGEGW
     F
//
ID   D19L3_MOUSE             Reviewed;         716 AA.
AC   Q71B07; Q6PB46; Q80W29; Q8BLA9; Q8BZL3; Q8BZW5;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   08-MAR-2011, entry version 43.
DE   RecName: Full=Protein dpy-19 homolog 3;
DE   AltName: Full=Dpy-19-like protein 3;
GN   Name=Dpy19l3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RA   Ding P., Han W., Rui M., Wang Y., Song Q., Zhang Y., Ma D.;
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, Diencephalon, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the dpy-19 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH59897.1; Type=Frameshift; Positions=495;
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DR   EMBL; AF538322; AAQ10888.1; -; mRNA.
DR   EMBL; AK033395; BAC28266.1; -; mRNA.
DR   EMBL; AK034217; BAC28636.1; -; mRNA.
DR   EMBL; AK045758; BAC32483.1; -; mRNA.
DR   EMBL; BC050065; AAH50065.1; -; mRNA.
DR   EMBL; BC059897; AAH59897.1; ALT_FRAME; mRNA.
DR   IPI; IPI00468697; -.
DR   RefSeq; NP_848819.2; NM_178704.3.
DR   UniGene; Mm.257808; -.
DR   ProteinModelPortal; Q71B07; -.
DR   PRIDE; Q71B07; -.
DR   Ensembl; ENSMUST00000051377; ENSMUSP00000054747; ENSMUSG00000043671.
DR   GeneID; 233115; -.
DR   KEGG; mmu:233115; -.
DR   CTD; 233115; -.
DR   MGI; MGI:2443952; Dpy19l3.
DR   eggNOG; roNOG11310; -.
DR   GeneTree; ENSGT00530000063023; -.
DR   HOGENOM; HBG446819; -.
DR   HOVERGEN; HBG107792; -.
DR   InParanoid; Q71B07; -.
DR   OMA; LFSLTWQ; -.
DR   OrthoDB; EOG46MBJB; -.
DR   PhylomeDB; Q71B07; -.
DR   NextBio; 381573; -.
DR   ArrayExpress; Q71B07; -.
DR   Bgee; Q71B07; -.
DR   CleanEx; MM_DPY19L3; -.
DR   Genevestigator; Q71B07; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR018732; Dpy-19.
DR   Pfam; PF10034; DUF2211; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    716       Protein dpy-19 homolog 3.
FT                                /FTId=PRO_0000311902.
FT   TRANSMEM     48     68       Helical; (Potential).
FT   TRANSMEM    156    174       Helical; (Potential).
FT   TRANSMEM    179    195       Helical; (Potential).
FT   TRANSMEM    215    235       Helical; (Potential).
FT   TRANSMEM    241    258       Helical; (Potential).
FT   TRANSMEM    270    292       Helical; (Potential).
FT   TRANSMEM    302    324       Helical; (Potential).
FT   TRANSMEM    341    361       Helical; (Potential).
FT   TRANSMEM    417    437       Helical; (Potential).
FT   TRANSMEM    461    481       Helical; (Potential).
FT   TRANSMEM    489    509       Helical; (Potential).
FT   TRANSMEM    520    540       Helical; (Potential).
FT   COMPBIAS    231    358       Leu-rich.
FT   CONFLICT    208    208       T -> A (in Ref. 3; AAH50065).
FT   CONFLICT    210    210       P -> T (in Ref. 2; BAC28266).
FT   CONFLICT    382    383       FG -> LV (in Ref. 1; AAQ10888).
FT   CONFLICT    539    539       S -> P (in Ref. 2; BAC28636).
FT   CONFLICT    590    590       G -> R (in Ref. 3; AAH50065).
FT   CONFLICT    650    650       G -> S (in Ref. 3; AAH50065).
SQ   SEQUENCE   716 AA;  82990 MW;  E801A69F9E8F9E93 CRC64;
     MMYIRQRKET KPIEVSEDFP SPKEDVKLEK KLPSGCASGR FWKILSSAVG GTVALCIGLL
     TSVYLATLHE NDLWFSNIKE VEREISFRTE CGLYYSYYKQ MLQAPTLLQG FHGLIYDNKT
     ESMRTINLLQ RMNIYQEVFL SVLYRVLPIQ KYLEPVYFYI YTLFGLQAVY VTALYITSWL
     LSGTWLSGLL AALWYVTNRI DTTRVEFTIP LRENWALPFF AIQIAAITYF LRPNLQPLSE
     RLTLLAIFVS TFLFSLTWQF NQFMMLLQAL VLFILDSLDM LPAMKATWLY GIQISCLLLV
     CTLQFFNSMI LGSLLISFNL SVLIVRKLQK NLKTGSFLTR IWKLLLHLLL VFCLTLFLNN
     IIKKVLNLKS DEHIFKFLKA KFGFGATRDF DANLYLCEEA FGLLPLNTFQ RLSETLLFYA
     YMFVLVVTVV TASVVAFHNL SDSTSLKSMD QTRKRAVDLK PEAAYNLIHT ILFGVLALST
     MRMKYLWTSH MCVFASFGLC SSEVWELLLR LVHLCNPKRI WVLRYLVPVL TLLYLCYKSW
     PGVMDELSEL KEFYDPDTVE LMTWINSNTP RKAVFAGSMQ LLAGVKLCTG RTLTNHPHYE
     DKSLRERTQA VYQIYAKRSP EEVHALLRSF GTDFVILEDS ICYERRHHRG CRLRDLLDVA
     NGHEMDGPGE SDPDLRPADH PRFCEEIKRN LPSYAAHFTR VFQNKTFHVY KLSRNK
//
ID   ZNRF2_MOUSE             Reviewed;         238 AA.
AC   Q71FD5;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=E3 ubiquitin-protein ligase ZNRF2;
DE            EC=6.3.2.-;
DE   AltName: Full=Zinc/RING finger protein 2;
GN   Name=Znrf2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=22923786; PubMed=14561866;
RA   Araki T., Milbrandt J.;
RT   "ZNRF proteins constitute a family of presynaptic E3 ubiquitin
RT   ligases.";
RL   J. Neurosci. 23:9385-9394(2003).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-113, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: May play a role in the establisment and maintenance of
CC       neuronal transmission and plasticity via its ubiquitin ligase
CC       activity. E3 ubiquitin ligases accept ubiquitin from an E2
CC       ubiquitin-conjugating enzyme in the form of a thioester and then
CC       directly transfer the ubiquitin to targeted substrates (By
CC       similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with UBE2N (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane
CC       protein (By similarity). Lysosome membrane; Peripheral membrane
CC       protein (By similarity). Cell junction, synapse, presynaptic cell
CC       membrane; Peripheral membrane protein (By similarity).
CC       Note=Present in presynaptic plasma membranes in neurons (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Expressed primarily in the nervous system.
CC       Expression is more intense in the granular cell layer of
CC       hippocampus, Purkinje cell layer of the cerebellum and the
CC       granular cell layer of the olfactory bulb. Detected in sensory
CC       neurons but not expressed in sympatic or enteric neurons.
CC       Expressed in testis, adipose tissue, columnar epithelial cells of
CC       the gut.
CC   -!- DOMAIN: The RING-type zinc finger domain is required for E3 ligase
CC       activity (By similarity).
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF513708; AAQ08116.1; -; mRNA.
DR   IPI; IPI00467930; -.
DR   RefSeq; NP_954594.1; NM_199143.2.
DR   UniGene; Mm.286149; -.
DR   UniGene; Mm.392146; -.
DR   HSSP; Q9LRB7; 1IYM.
DR   ProteinModelPortal; Q71FD5; -.
DR   SMR; Q71FD5; 190-238.
DR   STRING; Q71FD5; -.
DR   PhosphoSite; Q71FD5; -.
DR   PRIDE; Q71FD5; -.
DR   Ensembl; ENSMUST00000079869; ENSMUSP00000078795; ENSMUSG00000058446.
DR   GeneID; 387524; -.
DR   KEGG; mmu:387524; -.
DR   UCSC; uc009cae.1; mouse.
DR   CTD; 387524; -.
DR   MGI; MGI:1196246; Znrf2.
DR   GeneTree; ENSGT00390000013068; -.
DR   HOGENOM; HBG444901; -.
DR   HOVERGEN; HBG094200; -.
DR   InParanoid; Q71FD5; -.
DR   OMA; GSQDSVH; -.
DR   PhylomeDB; Q71FD5; -.
DR   NextBio; 405928; -.
DR   ArrayExpress; Q71FD5; -.
DR   Bgee; Q71FD5; -.
DR   CleanEx; MM_ZNRF2; -.
DR   Genevestigator; Q71FD5; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Endosome; Ligase; Lipoprotein; Lysosome;
KW   Membrane; Metal-binding; Myristate; Phosphoprotein; Synapse;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed (Potential).
FT   CHAIN         2    238       E3 ubiquitin-protein ligase ZNRF2.
FT                                /FTId=PRO_0000277804.
FT   ZN_FING     195    236       RING-type; atypical.
FT   COMPBIAS     25     32       Poly-Gly.
FT   COMPBIAS     33     92       Ala-rich.
FT   COMPBIAS     99    103       Poly-Gly.
FT   MOD_RES      17     17       Phosphotyrosine (By similarity).
FT   MOD_RES      18     18       Phosphoserine.
FT   MOD_RES      75     75       Phosphoserine (By similarity).
FT   MOD_RES     113    113       Phosphoserine.
FT   MOD_RES     141    141       Phosphoserine.
FT   MOD_RES     147    147       Phosphoserine (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (Potential).
SQ   SEQUENCE   238 AA;  23705 MW;  40422C7ECCC173CC CRC64;
     MGAKQSGPAA NGRTRAYSGS DLPSGTGSGG GGADGARAAR FAAPVSGAQQ PSASAGAAAA
     AAAAASAPAA PRSRSLGGAV GSASGGRAAQ SAFSIPSAGG GGGPYGSQDS VHSSPEDSVG
     ARDRDRPAGG GPGGPRLVIG SLPAHLSPHL FGGFKCPVCS KFVPSDEMDL HLVMCLTKPR
     ITYNEDVLSK DTGECAICLE ELQQGDTIAR LPCLCIYHKG CIDEWFEVNR SCPEHPSD
//
ID   Q71H74_MOUSE            Unreviewed;       223 AA.
AC   Q71H74;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   08-FEB-2011, entry version 38.
DE   SubName: Full=Collapsin response mediator protein 4A;
DE   Flags: Fragment;
GN   Name=Dpysl3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Swiss Webster/NIH;
RX   MEDLINE=22699123; PubMed=12814366;
RX   DOI=10.1046/j.1460-9568.2003.02664.x;
RA   Yuasa-Kawada J., Suzuki R., Kano F., Ohkawara T., Murata M., Noda M.;
RT   "Axonal morphogenesis controlled by antagonistic roles of two CRMP
RT   subtypes in microtubule organization.";
RL   Eur. J. Neurosci. 17:2329-2343(2003).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
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DR   EMBL; AF501324; AAQ07444.1; -; mRNA.
DR   IPI; IPI00406447; -.
DR   UniGene; Mm.428551; -.
DR   UniGene; Mm.8180; -.
DR   HSSP; P97427; 1KCX.
DR   ProteinModelPortal; Q71H74; -.
DR   STRING; Q71H74; -.
DR   Ensembl; ENSMUST00000121805; ENSMUSP00000112928; ENSMUSG00000024501.
DR   MGI; MGI:1349762; Dpysl3.
DR   GeneTree; ENSGT00550000074371; -.
DR   InParanoid; Q71H74; -.
DR   ArrayExpress; Q71H74; -.
DR   Bgee; Q71H74; -.
DR   Genevestigator; Q71H74; -.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0007399; P:nervous system development; IDA:MGI.
DR   InterPro; IPR006680; Amidohydro_1.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Metalo_hydrolase; 1.
PE   1: Evidence at protein level;
FT   NON_TER     223    223
SQ   SEQUENCE   223 AA;  23946 MW;  35A785DBA2DDE068 CRC64;
     MASGRRGWDS SHEDDLPVYL ARPGTTDQVP RQKYGGMFCN VEGAFESKTL DFDALSVGQR
     GAKTPRSSQG SGRGAGNRPG MEVDARRGPG REESREPAPE SPKPAGVEIR SATGKEVLQN
     LGPKDKSDRL LIKGGRIVND DQSFYADIYM EDGLIKQIGD NLIVPGGVKT IEANGKMVIP
     GGIDVHTHFQ MPYKGMTTVD DFFQGTKAAL AGGTTMIIDH VVP
//
ID   Q71LX8_MOUSE            Unreviewed;       724 AA.
AC   Q71LX8;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   11-JAN-2011, entry version 75.
DE   SubName: Full=Heat shock protein 84b;
DE   SubName: Full=Heat shock protein 90 alpha (Cytosolic), class B member 1;
DE   SubName: Full=MCG18238;
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Hsp90ab1; Synonyms=Hsp84b, Hspcb; ORFNames=mCG_18238;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6;
RX   PubMed=19845467; DOI=10.1089/neu.2009.0926;
RA   Shen H.Y., Zhao Y., Chen X.Y., Xiong R.P., Lu J.L., Chen J.F.,
RA   Chen L.Y., Zhou Y.G.;
RT   "Differential alteration of heat shock protein 90 in mice modifies
RT   glucocorticoid receptor function and susceptibility to trauma.";
RL   J. Neurotrauma 27:373-381(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C, and C57BL/6J;
RC   TISSUE=Mullerian duct includes surrounding region;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C, and C57BL/6J;
RC   TISSUE=Mullerian duct includes surrounding region;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C, and C57BL/6J;
RC   TISSUE=Mullerian duct includes surrounding region;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C, and C57BL/6J;
RC   TISSUE=Mullerian duct includes surrounding region;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C, and C57BL/6J;
RC   TISSUE=Mullerian duct includes surrounding region;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C, and C57BL/6J;
RC   TISSUE=Mullerian duct includes surrounding region;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C, and C57BL/6J;
RC   TISSUE=Mullerian duct includes surrounding region;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [11]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/C, and C57BL/6J;
RC   TISSUE=Mullerian duct includes surrounding region;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC088985; AAH88985.1; -; mRNA.
DR   EMBL; AF465639; AAQ04842.1; -; mRNA.
DR   EMBL; AK135366; BAE22506.1; -; mRNA.
DR   EMBL; AK146205; BAE26978.1; -; mRNA.
DR   EMBL; CH466559; EDL23450.1; -; Genomic_DNA.
DR   IPI; IPI00229080; -.
DR   RefSeq; NP_032328.2; NM_008302.3.
DR   UniGene; Mm.2180; -.
DR   HSSP; P02829; 1AH8.
DR   ProteinModelPortal; Q71LX8; -.
DR   SMR; Q71LX8; 11-219, 285-688.
DR   STRING; Q71LX8; -.
DR   PRIDE; Q71LX8; -.
DR   Ensembl; ENSMUST00000024739; ENSMUSP00000024739; ENSMUSG00000023944.
DR   GeneID; 15516; -.
DR   KEGG; mmu:15516; -.
DR   UCSC; uc008cqz.1; mouse.
DR   CTD; 15516; -.
DR   MGI; MGI:96247; Hsp90ab1.
DR   HOVERGEN; HBG007374; -.
DR   InParanoid; Q71LX8; -.
DR   OMA; FYSAFAK; -.
DR   PhylomeDB; Q71LX8; -.
DR   NextBio; 288432; -.
DR   ArrayExpress; Q71LX8; -.
DR   Bgee; Q71LX8; -.
DR   Genevestigator; Q71LX8; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:HAMAP.
DR   GO; GO:0001890; P:placenta development; IMP:MGI.
DR   GO; GO:0006457; P:protein folding; IEA:HAMAP.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   HAMAP; MF_00505; HSP90; 1; -.
DR   InterPro; IPR003594; ATPase-like_ATP-bd.
DR   InterPro; IPR019805; Heat_shock_protein_90_CS.
DR   InterPro; IPR001404; Hsp90.
DR   InterPro; IPR020575; Hsp90_N.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   Gene3D; G3DSA:3.30.565.10; ATP_bd_ATPase; 2.
DR   PANTHER; PTHR11528; Hsp90; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATP_bd_ATPase; 1.
DR   SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR   PROSITE; PS00298; HSP90; 1.
PE   2: Evidence at transcript level;
KW   Stress response.
SQ   SEQUENCE   724 AA;  83281 MW;  CE323E81CE173ECB CRC64;
     MPEEVHHGEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA LDKIRYESLT
     DPSKLDSGKE LKIDIIPNPQ ERTLTLVDTG IGMTKADLIN NLGTIAKSGT KAFMEALQAG
     ADISMIGQFG VGFYSAYLVA EKVVVITKHN DDEQYAWESS AGGSFTVRAD HGEPIGRGTK
     VILHLKEDQT EYLEERRVKE VVKKHSQFIG YPITLYLEKE REKEISDDEA EEEKGEKEEE
     DKEDEEKPKI EDVGSDEEDD SGKDKKKKTK KIKEKYIDQE ELNKTKPIWT RNPDDITQEE
     YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFIPRRAP FDLFENKKKK NNIKLYVRRV
     FIMDSCDELI PEYLNFIRGV VDSEDLPLNI SREMLQQSKI LKVIRKNIVK KCLELFSELA
     EDKENYKKFY EAFSKNLKLG IHEDSTNRRR LSELLRYHTS QSGDEMTSLS EYVSRMKETQ
     KSIYYITGES KEQVANSAFV ERVRKRGFEV VYMTEPIDEY CVQQLKEFDG KSLVSVTKEG
     LELPEDEEEK KKMEESKAKF ENLCKLMKEI LDKKVEKVTI SNRLVSSPCC IVTSTYGWTA
     NMERIMKAQA LRDNSTMGYM MAKKHLEINP DHPIVETLRQ KAEADKNDKA VKDLVVLLFE
     TALLSSGFSL EDPQTHSNRI YRMIKLGLGI DEDEVTAEEP SAAVPDEIPP LEGDEDASRM
     EEVD
//
ID   CSPG5_MOUSE             Reviewed;         566 AA.
AC   Q71M36; Q71M37; Q7TNT8; Q8BPJ5; Q9QY32;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Chondroitin sulfate proteoglycan 5;
DE   AltName: Full=Acidic leucine-rich EGF-like domain-containing brain protein;
DE   AltName: Full=Neuroglycan C;
DE   Flags: Precursor;
GN   Name=Cspg5; Synonyms=Caleb, Ngc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY,
RP   GLYCOSYLATION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=20085050; PubMed=10617623; DOI=10.1074/jbc.275.1.337;
RA   Aono S., Keino H., Ono T., Yasuda Y., Tokita Y., Matsui F.,
RA   Taniguchi M., Sonta S., Oohira A.;
RT   "Genomic organization and expression pattern of mouse neuroglycan C in
RT   the cerebellar development.";
RL   J. Biol. Chem. 275:337-342(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 202-566 (ISOFORM 4).
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=99133557; PubMed=9950058; DOI=10.1016/S0168-0102(98)00098-4;
RA   Yasuda Y., Tokita Y., Aono S., Matsui F., Ono T., Sonta S.,
RA   Watanabe E., Nakanishi Y., Oohira A.;
RT   "Cloning and chromosomal mapping of the human gene of neuroglycan C
RT   (NGC), a neural transmembrane chondroitin sulfate proteoglycan with an
RT   EGF module.";
RL   Neurosci. Res. 32:313-322(1998).
RN   [5]
RP   INTERACTION WITH TNR.
RX   MEDLINE=21269264; PubMed=11069908; DOI=10.1074/jbc.M007234200;
RA   Schumacher S., Jung M., Noerenberg U., Dorner A.,
RA   Chiquet-Ehrismann R., Stuermer C.A.O., Rathjen F.G.;
RT   "CALEB binds via its acidic stretch to the fibrinogen-like domain of
RT   tenascin-C or tenascin-R and its expression is dynamically regulated
RT   after optic nerve lesion.";
RL   J. Biol. Chem. 276:7337-7345(2001).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12885772; DOI=10.1074/jbc.M305577200;
RA   Hassel B., Schreff M., Stuebe E.-M., Blaich U., Schumacher S.;
RT   "CALEB/NGC interacts with the Golgi-associated protein PIST.";
RL   J. Biol. Chem. 278:40136-40143(2003).
RN   [7]
RP   TISSUE SPECIFICITY, MUTAGENESIS OF SER-38 AND SER-123, GLYCOSYLATION
RP   AT SER-123, AND SUBCELLULAR LOCATION.
RX   PubMed=15331613; DOI=10.1074/jbc.M403263200;
RA   Aono S., Tokita Y., Shuo T., Yamauchi S., Matsui F., Nakanishi K.,
RA   Hirano K., Sano M., Oohira A.;
RT   "Glycosylation site for chondroitin sulfate on the neural part-time
RT   proteoglycan, neuroglycan C.";
RL   J. Biol. Chem. 279:46536-46541(2004).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15848802; DOI=10.1016/j.neuron.2005.02.027;
RA   Juettner R., More M.I., Das D., Babich A., Meier J., Henning M.,
RA   Erdmann B., Mueller E.-C., Otto A., Grantyn R., Rathjen F.G.;
RT   "Impaired synapse function during postnatal development in the absence
RT   of CALEB, an EGF-like protein processed by neuronal activity.";
RL   Neuron 46:233-245(2005).
CC   -!- FUNCTION: May function as a growth and differentiation factor
CC       involved in neuritogenesis. May induce ERBB3 activation.
CC   -!- SUBUNIT: Binds TNR and probably TNC (By similarity). Interacts
CC       with ERBB3 and GOPC.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein (By similarity). Endoplasmic reticulum membrane; Single-
CC       pass type I membrane protein. Golgi apparatus membrane; Single-
CC       pass type I membrane protein. Note=Partially enriched in lipid
CC       rafts (By similarity). In neurons, localizes to synaptic
CC       junctions. Also detected in the endoplasmic reticulum and the
CC       Golgi.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=NGC-III;
CC         IsoId=Q71M36-1; Sequence=Displayed;
CC       Name=2; Synonyms=NGC-I;
CC         IsoId=Q71M36-2; Sequence=VSP_015763;
CC         Note=Major isoform;
CC       Name=3; Synonyms=NGC-II;
CC         IsoId=Q71M36-3; Sequence=VSP_015762, VSP_015763;
CC       Name=4;
CC         IsoId=Q71M36-4; Sequence=VSP_015764;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in olfactory bulb, hippocampus,
CC       brain stem, spinal cord, cerebrum and cerebellum. Expressed by
CC       Purkinje cells in the cerebellum (at protein level). Expressed in
CC       immature and mature cerebellum (isoform 1, isoform 2 and isoform
CC       3).
CC   -!- DEVELOPMENTAL STAGE: The proteoglycan form decreases from birth to
CC       adulthood in the cerebellum concomitant with non-proteoglycan form
CC       increase. In the cerebrum the maximum of expression of the
CC       proteoglycan is detected 15 days after birth and then decreases
CC       gradually to reach an half-level at adulthood (at protein level).
CC   -!- PTM: N-glycosylated (By similarity).
CC   -!- PTM: O-glycosylated; contains chondroitin sulfate glycans. Part-
CC       time proteoglycan, expressed in part as a proteoglycan exhibiting
CC       chondroitin sulfate glycans and in part as a non-proteoglycan
CC       form. The relative amount of both forms depends on tissues and
CC       tissues maturation. In the cerebellum the 2 forms coexist while in
CC       the cerebrum the proteoglycan form is predominant.
CC   -!- PTM: Phosphorylated; in intracellular and extracellular parts (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Altered synaptic transmission at early
CC       developmental stages.
CC   -!- MISCELLANEOUS: Different forms of various molecular weight have
CC       been observed. Such forms are possibly due to different levels of
CC       glycosylation, phosphorylation and/or protein cleavage.
CC   -!- SIMILARITY: Contains 1 EGF-like domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAQ04778.1; Type=Erroneous initiation;
CC       Sequence=BAC35578.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF133700; AAF23362.1; -; mRNA.
DR   EMBL; AF461090; AAQ04777.1; -; mRNA.
DR   EMBL; AF461091; AAQ04778.1; ALT_INIT; mRNA.
DR   EMBL; AF461092; AAQ04779.1; -; mRNA.
DR   EMBL; BC055736; AAH55736.1; -; mRNA.
DR   EMBL; AK053891; BAC35578.1; ALT_INIT; mRNA.
DR   IPI; IPI00454159; -.
DR   IPI; IPI00458238; -.
DR   IPI; IPI00652233; -.
DR   IPI; IPI00653847; -.
DR   RefSeq; NP_001159745.1; NM_001166273.1.
DR   RefSeq; NP_038912.3; NM_013884.3.
DR   UniGene; Mm.38496; -.
DR   STRING; Q71M36; -.
DR   PRIDE; Q71M36; -.
DR   Ensembl; ENSMUST00000035058; ENSMUSP00000035058; ENSMUSG00000032482.
DR   GeneID; 29873; -.
DR   KEGG; mmu:29873; -.
DR   UCSC; uc009rtr.1; mouse.
DR   UCSC; uc009rts.1; mouse.
DR   UCSC; uc009rtt.1; mouse.
DR   UCSC; uc009rtu.1; mouse.
DR   CTD; 29873; -.
DR   MGI; MGI:1352747; Cspg5.
DR   eggNOG; roNOG08044; -.
DR   GeneTree; ENSGT00440000034270; -.
DR   HOGENOM; HBG127139; -.
DR   HOVERGEN; HBG081361; -.
DR   InParanoid; Q71M36; -.
DR   OrthoDB; EOG4XWFXN; -.
DR   NextBio; 307106; -.
DR   ArrayExpress; Q71M36; -.
DR   Bgee; Q71M36; -.
DR   CleanEx; MM_CSPG5; -.
DR   Genevestigator; Q71M36; -.
DR   GermOnline; ENSMUSG00000032482; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030660; C:Golgi-associated vesicle membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   GO; GO:0050804; P:regulation of synaptic transmission; IMP:MGI.
DR   InterPro; IPR010555; Chon_Sulph_att.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR009505; Neural_ProG_Cyt.
DR   Pfam; PF06566; Chon_Sulph_att; 1.
DR   Pfam; PF06567; Neural_ProG_Cyt; 1.
DR   SMART; SM00181; EGF; 1.
DR   PROSITE; PS00022; EGF_1; FALSE_NEG.
DR   PROSITE; PS01186; EGF_2; FALSE_NEG.
DR   PROSITE; PS50026; EGF_3; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Developmental protein;
KW   Differentiation; Disulfide bond; EGF-like domain;
KW   Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW   Growth regulation; Membrane; Neurogenesis; Phosphoprotein;
KW   Proteoglycan; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     30       Potential.
FT   CHAIN        31    566       Chondroitin sulfate proteoglycan 5.
FT                                /FTId=PRO_0000042152.
FT   TOPO_DOM     31    423       Extracellular (Potential).
FT   TRANSMEM    424    444       Helical; (Potential).
FT   TOPO_DOM    445    566       Cytoplasmic (Potential).
FT   DOMAIN      371    413       EGF-like.
FT   REGION      265    301       Interaction with TNC and TNR.
FT   REGION      442    460       Interaction with GOPC (By similarity).
FT   CARBOHYD     57     57       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     76     76       O-linked (GalNAc...) (Potential).
FT   CARBOHYD    123    123       O-linked (Xyl...) (chondroitin sulfate).
FT   CARBOHYD    132    132       O-linked (GalNAc...) (Potential).
FT   CARBOHYD    143    143       O-linked (GalNAc...) (Potential).
FT   CARBOHYD    144    144       O-linked (GalNAc...) (Potential).
FT   CARBOHYD    153    153       O-linked (GalNAc...) (Potential).
FT   CARBOHYD    155    155       O-linked (GalNAc...) (Potential).
FT   CARBOHYD    156    156       O-linked (GalNAc...) (Potential).
FT   CARBOHYD    160    160       O-linked (GalNAc...) (Potential).
FT   CARBOHYD    235    235       O-linked (GalNAc...) (Potential).
FT   CARBOHYD    355    355       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    367    367       N-linked (GlcNAc...) (Potential).
FT   DISULFID    374    387       By similarity.
FT   DISULFID    381    397       By similarity.
FT   DISULFID    399    412       By similarity.
FT   VAR_SEQ       1     81       Missing (in isoform 3).
FT                                /FTId=VSP_015762.
FT   VAR_SEQ     487    513       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_015763.
FT   VAR_SEQ     514    566       DDPSAPHKIQDPLKSRLKEEESFNIQNSMSPKLEGGKGDQD
FT                                DLGVNCLQNNLT -> VTYLPHISPFACLCPCLPLPPCPLA
FT                                LSQSRQSPNSFEDQLRATQWCRERCIDSLTV (in
FT                                isoform 4).
FT                                /FTId=VSP_015764.
FT   MUTAGEN      38     38       S->A: No effect on chondroitin sulfate
FT                                attachment.
FT   MUTAGEN     123    123       S->A: No chondroitin sulfate attachment.
FT                                no effect on transport to the cell
FT                                surface.
FT   CONFLICT    317    317       N -> T (in Ref. 2; AAH55736 and 3;
FT                                BAC35578).
FT   CONFLICT    318    318       N -> H (in Ref. 2; AAH55736).
SQ   SEQUENCE   566 AA;  60419 MW;  8AB1A9A1ACBEFBDE CRC64;
     MGRAGGGGPD WGPPPVLLLL GVTLVLTAGA VPARETGSAI EAEELVRSSL AWESRANDTR
     EEAGLPAAGE DETSWTERGS EMAAVGPGVG PEEALEASAA VTGTAWLEAD GPGLGGVTAE
     AGSGDAQTLP ATLQAPDEAL GSSTMPPAIP EATETSGPPS PAVHDKPSVG PELPKEIPLE
     VRLNLGGSTP EPTFPLQGTL ETQPASDIID IDYFEGLDSE GRGADMGSFP GSPGTSENHP
     DTEGETPSWS LLDLYDDFTP FDESDFYPTT SFYDDLEEEE EEEEDKDTVG GGDLEDENDL
     LLPSQKPGVG PGTGQPNNRW HAVPPQHTLG MVPGSSISLR PRPGDPGKDL ASGENGTECR
     VGFVRHNGSC RSVCDLFPSY CHNGGQCYLV ENIGAFCRCN TQDYIWHKGM RCESIITDFQ
     VMCVAVGSAA LVLLLLFMMT VFFAKKLYLL KTENTKLRRT NKFRTPSELH NDNFSLSTIA
     EGSHPNVRKF CDTPRVSSPH ARALAHYDNI VCQDDPSAPH KIQDPLKSRL KEEESFNIQN
     SMSPKLEGGK GDQDDLGVNC LQNNLT
//
ID   SC6A5_MOUSE             Reviewed;         799 AA.
AC   Q761V0; Q8CFM5; Q91ZQ2;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Sodium- and chloride-dependent glycine transporter 2;
DE            Short=GlyT-2;
DE            Short=GlyT2;
DE   AltName: Full=Solute carrier family 6 member 5;
GN   Name=Slc6a5; Synonyms=Glyt2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), AND TISSUE SPECIFICITY.
RC   STRAIN=129/Sv;
RX   PubMed=15081419; DOI=10.1016/j.bbrc.2004.03.125;
RA   Ebihara S., Yamamoto T., Obata K., Yanagawa Y.;
RT   "Gene structure and alternative splicing of the mouse glycine
RT   transporter type-2.";
RL   Biochem. Biophys. Res. Commun. 317:857-864(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RC   STRAIN=BALB/c; TISSUE=Brain;
RA   Liu Q.-R., Li Q.-F.;
RT   "Cloning and expression of mouse sodium-dependent glycine transporter
RT   2 (Glyt2).";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Terminates the action of glycine by its high affinity
CC       sodium-dependent reuptake into presynaptic terminals. May be
CC       responsible for the termination of neurotransmission at
CC       strychnine-sensitive glycinergic synapses (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=a;
CC         IsoId=Q761V0-1; Sequence=Displayed;
CC       Name=b;
CC         IsoId=Q761V0-2; Sequence=VSP_051603;
CC   -!- TISSUE SPECIFICITY: Isoform a and isoform b are expressed at high
CC       levels in brain stem and spinal cord. Isoform a is also expressed
CC       in the cerebellum.
CC   -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF)
CC       (TC 2.A.22) family. SLC6A5 subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB118159; BAD16781.1; -; mRNA.
DR   EMBL; AF411042; AAL17054.1; -; mRNA.
DR   EMBL; AY147186; AAN11408.1; -; mRNA.
DR   IPI; IPI00404338; -.
DR   IPI; IPI00459445; -.
DR   UniGene; Mm.207053; -.
DR   ProteinModelPortal; Q761V0; -.
DR   SMR; Q761V0; 192-732.
DR   STRING; Q761V0; -.
DR   TCDB; 2.A.22.2.6; neurotransmitter:sodium symporter (NSS) family.
DR   PRIDE; Q761V0; -.
DR   Ensembl; ENSMUST00000056442; ENSMUSP00000058699; ENSMUSG00000039728.
DR   Ensembl; ENSMUST00000107605; ENSMUSP00000103230; ENSMUSG00000039728.
DR   UCSC; uc009hbv.1; mouse.
DR   MGI; MGI:105090; Slc6a5.
DR   GeneTree; ENSGT00600000084044; -.
DR   HOGENOM; HBG702834; -.
DR   HOVERGEN; HBG071421; -.
DR   InParanoid; Q761V0; -.
DR   OrthoDB; EOG4HDST0; -.
DR   NextBio; 356802; -.
DR   ArrayExpress; Q761V0; -.
DR   Bgee; Q761V0; -.
DR   Genevestigator; Q761V0; -.
DR   GermOnline; ENSMUSG00000039728; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; IEA:InterPro.
DR   GO; GO:0005328; F:neurotransmitter:sodium symporter activity; IEA:InterPro.
DR   InterPro; IPR000175; Na/ntran_symport.
DR   PANTHER; PTHR11616; Na/ntran_symport; 1.
DR   Pfam; PF00209; SNF; 1.
DR   PRINTS; PR00176; NANEUSMPORT.
DR   PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR   PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
DR   PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Membrane;
KW   Neurotransmitter transport; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    799       Sodium- and chloride-dependent glycine
FT                                transporter 2.
FT                                /FTId=PRO_0000214763.
FT   TOPO_DOM      1    201       Cytoplasmic (Potential).
FT   TRANSMEM    202    222       Helical; Name=1; (Potential).
FT   TRANSMEM    229    249       Helical; Name=2; (Potential).
FT   TRANSMEM    273    293       Helical; Name=3; (Potential).
FT   TOPO_DOM    294    396       Extracellular (Potential).
FT   TRANSMEM    397    417       Helical; Name=4; (Potential).
FT   TRANSMEM    433    453       Helical; Name=5; (Potential).
FT   TRANSMEM    472    492       Helical; Name=6; (Potential).
FT   TRANSMEM    510    530       Helical; Name=7; (Potential).
FT   TRANSMEM    565    585       Helical; Name=8; (Potential).
FT   TRANSMEM    611    631       Helical; Name=9; (Potential).
FT   TRANSMEM    640    660       Helical; Name=10; (Potential).
FT   TRANSMEM    677    697       Helical; Name=11; (Potential).
FT   TRANSMEM    717    737       Helical; Name=12; (Potential).
FT   TOPO_DOM    738    799       Cytoplasmic (Potential).
FT   CARBOHYD    345    345       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    355    355       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    360    360       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    366    366       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    714    714       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1      8       Missing (in isoform b).
FT                                /FTId=VSP_051603.
FT   CONFLICT    151    151       V -> E (in Ref. 2; AAL17054/AAN11408).
SQ   SEQUENCE   799 AA;  87861 MW;  92AC7750C7023D45 CRC64;
     MDCSAPKEMN KQPANILEAA VPGHRDSPRA PRTSPEQDLP AEAPAATVQP PRVPRSASTG
     AQTFQSADAR ACEAQQSGVG FCNLSSPRAQ ATSAALRDLS EGHSAQANPP SGPAGAGNAL
     HCKIPALRGP EEDANVSVGK GTLEHNNTPA VGWVNMSQST VVLGTDGIAS VLPGSVATTT
     IPEDEQGDEN KARGNWSSKL DFILSMVGYA VGLGNVWRFP YLAFQNGGGA FLIPYLMMLA
     LAGLPIFFLE VSLGQFASQG PVSVWKAIPA LQGCGIAMLI ISVLIAIYYN VIICYTLFYL
     FASFVSVLPW GSCNNPWNTP ECKDKTKLLL DSCVIGDHPK IQIKNSTFCM TAYPNLTMVN
     FTSQTNKTFV SGSEEYFKYF VLKISAGIEY PGEIRWPLAF CLFLAWVIVY ASLAKGIKSS
     GKVVYFTATF PYVVLVILLI RGVTLPGAGA GIWYFITPKW EKLTDATVWK DAATQIFFSL
     SAAWGGLITL SSYNKFHNNC YRDTLIVTCT NSATSIFAGF VIFSVIGFMA NERKVNIENV
     ADQGPGIAFV VYPEALTRLP LSPFWAIIFF LMLLTLGLDT MFATIETIVT SISDEFPKYL
     RTHKPVFTLG CCICFFIMGF PMITQGGIYM FQLVDTYAAS YALVIIAIFE LVGISYVYGL
     QRFCEDIEMM IGFKPNIFWK VCWAFVTPTI LTFILCFSFY QWEPMTYGSY RYPNWSMVLG
     WLMLACSVIW IPIMFVIKMY LAPGRFIERL KLVCSPQPDW GPFLAQHRGE RYKNMIDPLG
     TSSLGLKLPV KDLELGTQC
//
ID   SSH1_MOUSE              Reviewed;        1042 AA.
AC   Q76I79; Q3TDG3; Q69ZM4; Q811E5;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Protein phosphatase Slingshot homolog 1;
DE            EC=3.1.3.16;
DE            EC=3.1.3.48;
DE   AltName: Full=SSH-like protein 1;
DE            Short=SSH-1L;
DE            Short=mSSH-1L;
GN   Name=Ssh1; Synonyms=Kiaa1298, Ssh1l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
RP   ACTIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND MUTAGENESIS OF CYS-393.
RX   MEDLINE=22894424; PubMed=14531860;
RX   DOI=10.1046/j.1365-2443.2003.00678.x;
RA   Ohta Y., Kousaka K., Nagata-Ohashi K., Ohashi K., Muramoto A.,
RA   Shima Y., Niwa R., Uemura T., Mizuno K.;
RT   "Differential activities, subcellular distribution and tissue
RT   expression patterns of three members of Slingshot family phosphatases
RT   that dephosphorylate cofilin.";
RL   Genes Cells 8:811-824(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryonic tail;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 539-1042 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 166-1042 (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH LIMK1.
RX   PubMed=15660133; DOI=10.1038/sj.emboj.7600543;
RA   Soosairajah J., Maiti S., Wiggan O., Sarmiere P., Moussi N.,
RA   Sarcevic B., Sampath R., Bamburg J.R., Bernard O.;
RT   "Interplay between components of a novel LIM kinase-slingshot
RT   phosphatase complex regulates cofilin.";
RL   EMBO J. 24:473-486(2005).
CC   -!- FUNCTION: Protein phosphatase which regulates actin filament
CC       dynamics. Dephosphorylates and activates the actin
CC       binding/depolymerizing factor cofilin, which subsequently binds to
CC       actin filaments and stimulates their disassembly. Inhibitory
CC       phosphorylation of cofilin is mediated by LIMK1, which may also be
CC       dephosphorylated and inactivated by this protein.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- SUBUNIT: Interacts with the 14-3-3 proteins YWHAB, YWHAG, YWHAQ,
CC       and YWHAZ. Interaction with 14-3-3 proteins inhibits phosphatase
CC       activity and also blocks recruitment to lamellipodia and
CC       stimulation by actin (By similarity). Interacts with actin and
CC       this stimulates phosphatase activity. Interacts with LIMK1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cleavage furrow (By
CC       similarity). Midbody (By similarity). Note=Localized to the
CC       cleavage furrow and the midbody during cytokinesis (By
CC       similarity). Also colocalizes with F-actin in the cytoplasm and
CC       the cell periphery, which may allow local control of actin
CC       dynamics at sites of cell locomotion.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q76I79-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q76I79-2; Sequence=VSP_016320;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney and thymus.
CC       Also expressed at lower levels in liver, skeletal muscle, small
CC       intestine and spleen.
CC   -!- DEVELOPMENTAL STAGE: Ubiquitously expressed in the embryo at
CC       E14.5.
CC   -!- PTM: Phosphorylated. Inhibitory phosphorylation by PAK4 promotes
CC       binding to YWHAZ. Phosphorylation at Ser-970 is decreased by
CC       stimuli which promote actin reorganization and lamellipodia
CC       formation. Can be dephosphorylated and activated by
CC       PPP3CA/calcineurin A. Phosphorylation decreases immediately prior
CC       to telophase (By similarity).
CC   -!- MISCELLANEOUS: Tyrosine phosphatase activity has not been
CC       demonstrated for this protein to date.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32422.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB099287; BAC97810.1; -; mRNA.
DR   EMBL; AK173144; BAD32422.1; ALT_INIT; mRNA.
DR   EMBL; AK155557; BAE33323.1; -; mRNA.
DR   EMBL; AK170212; BAE41639.1; -; mRNA.
DR   EMBL; AK171556; BAE42524.1; -; mRNA.
DR   EMBL; BC046529; AAH46529.1; -; mRNA.
DR   IPI; IPI00467332; -.
DR   IPI; IPI00625071; -.
DR   RefSeq; NP_932777.2; NM_198109.4.
DR   UniGene; Mm.389682; -.
DR   ProteinModelPortal; Q76I79; -.
DR   SMR; Q76I79; 254-303, 309-449.
DR   STRING; Q76I79; -.
DR   PhosphoSite; Q76I79; -.
DR   PRIDE; Q76I79; -.
DR   Ensembl; ENSMUST00000077689; ENSMUSP00000076873; ENSMUSG00000042121.
DR   Ensembl; ENSMUST00000112298; ENSMUSP00000107917; ENSMUSG00000042121.
DR   GeneID; 231637; -.
DR   KEGG; mmu:231637; -.
DR   UCSC; uc008yyx.1; mouse.
DR   UCSC; uc008yyz.1; mouse.
DR   CTD; 231637; -.
DR   MGI; MGI:2686240; Ssh1.
DR   eggNOG; roNOG05760; -.
DR   GeneTree; ENSGT00590000082789; -.
DR   HOGENOM; HBG402830; -.
DR   HOVERGEN; HBG094001; -.
DR   InParanoid; Q76I79; -.
DR   OMA; EHDAIFG; -.
DR   OrthoDB; EOG480HVX; -.
DR   PhylomeDB; Q76I79; -.
DR   BRENDA; 3.1.3.16; 244.
DR   BRENDA; 3.1.3.48; 244.
DR   NextBio; 380673; -.
DR   ArrayExpress; Q76I79; -.
DR   Bgee; Q76I79; -.
DR   CleanEx; MM_SSH1; -.
DR   Genevestigator; Q76I79; -.
DR   GermOnline; ENSMUSG00000042121; Mus musculus.
DR   GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   InterPro; IPR014876; DEK_C.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR020422; Dual-sp_phosphatase_subgr_cat.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   Pfam; PF08766; DEK_C; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   SMART; SM00195; DSPc; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Alternative splicing; Cytoplasm;
KW   Cytoskeleton; Hydrolase; Phosphoprotein; Protein phosphatase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1042       Protein phosphatase Slingshot homolog 1.
FT                                /FTId=PRO_0000094842.
FT   DOMAIN      308    448       Tyrosine-protein phosphatase.
FT   REGION      889   1042       Interaction with YWHAG (By similarity).
FT   ACT_SITE    393    393       Phosphocysteine intermediate (Probable).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     970    970       Phosphoserine (By similarity).
FT   MOD_RES    1035   1035       Phosphoserine (By similarity).
FT   VAR_SEQ     158    179       Missing (in isoform 2).
FT                                /FTId=VSP_016320.
FT   MUTAGEN     393    393       C->S: Abrogates phosphatase activity.
FT   CONFLICT    526    526       E -> D (in Ref. 4; AAH46529).
FT   CONFLICT    550    550       V -> A (in Ref. 3; BAE41639).
FT   CONFLICT    569    569       D -> E (in Ref. 3; BAE41639).
FT   CONFLICT    867    867       A -> V (in Ref. 4; AAH46529).
FT   CONFLICT   1010   1010       E -> G (in Ref. 3; BAE41639).
FT   CONFLICT   1035   1035       S -> N (in Ref. 4; AAH46529).
SQ   SEQUENCE   1042 AA;  115297 MW;  19A34E4937FA48FA CRC64;
     MALVTLQRSP TPSAASSSAS NSELEAGSDE ERKLNLSLSE SFFMVKGAAL FLQQGNSPQG
     QRSLQHPHKH AGDLPQHLQV MINLLRCEDR IKLAVRLESV WTDRVRYMVV VYTSGRQDTE
     ENILLGVDFS SKESKSCTIG MVLRLWSDTK IHLDGDGGFS VSTAGRMHIF KPVSVQAMWS
     ALQVLHKACE VARRHNYFPG GVALIWATYY ESCISSEQSC INEWNAMQDL ESTRPDSPAL
     FVDKPTEGER TERLIKAKLR SIMMSQDLEN VTSKEIRNEL EKQMNCNLKE FKEFIDNEML
     LILGQMDKPS LIFDHLYLGS EWNASNLEEL QGSGVDYILN VTREIDNFFP GLFAYHNIRV
     YDEETTDLLA HWNEAYHFIN KAKRNHSKCL VHCKMGVSRS ASTVIAYAMK EFGWPLEKAY
     NYVKQKRSIT RPNAGFMRQL SEYEGILDAS KQRHNKLWRQ QPTDDTIAEP SEFLPETLDG
     ALDAQLPCLD DTTHPGLPRS LAPGGPALPC CFRRLSDPLL LPHHDETGGL VHLEDLEKDA
     LLEEEESQPV EVHKLVQHPQ EGARLCEKDV KRKLEFGNSK PRSDSLPQVE ELEKDGSPRT
     GRWRRASTQL DRSLLDQENL NNNNSKRSCP DDLERDAMFG ILSKVKPPYT SCADCMYPTA
     GGTPEAYMER HEDPSSSAIC TQPTFLPHVT SSPMAHASSR SRAPERPASG PANTSPFLLP
     AGSRKPDVSG SGAGAAPEPP ASLLEPSRET SKALPKSLQL KNPHCDKNAA NMEVSAKEEP
     SPKKDPKPAK DLRLLFSNEA EKPTTNSYLM QHQESIIQLQ KAGLVRKHTK ELERLKSLPS
     DSPAACRDSA TCRLEASIPE EGSQEPAHPA LCSQAGSEEQ PVGGTLQKSP TSTLPRLDHT
     SNFSKDFLKT VCYTPTSSSI SSNLTRSSSS DSIHSVRGKP GLVKQRAQEI ETRLRLAGLT
     VSSPLKRSHS LAKLGSLNFS TEDLSSEADT STIADSQDAK CGLSSSFLPE PQSAPRDPAA
     TSKSSGKSAP EHLKSPSRVN KS
//
ID   SEM6D_MOUSE             Reviewed;        1073 AA.
AC   Q76KF0; A2AW72; Q76KF1; Q76KF2; Q76KF3; Q76KF4; Q80TD0;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Semaphorin-6D;
DE   Flags: Precursor;
GN   Name=Sema6d; Synonyms=Kiaa1479;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4; 5 AND 6), AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=14715272; DOI=10.1016/j.bbrc.2003.12.083;
RA   Taniguchi M., Shimizu T.;
RT   "Characterization of a novel member of murine semaphorin family.";
RL   Biochem. Biophys. Res. Commun. 314:242-248(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Shows growth cone collapsing activity on dorsal root
CC       ganglion (DRG) neurons in vitro. May be a stop signal for the DRG
CC       neurons in their target areas, and possibly also for other
CC       neurons. May also be involved in the maintenance and remodeling of
CC       neuronal connections (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=4;
CC         IsoId=Q76KF0-1; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q76KF0-2; Sequence=VSP_016568, VSP_016569;
CC       Name=2;
CC         IsoId=Q76KF0-3; Sequence=VSP_016569;
CC       Name=3;
CC         IsoId=Q76KF0-4; Sequence=VSP_016571;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q76KF0-5; Sequence=VSP_016568, VSP_016571;
CC       Name=6;
CC         IsoId=Q76KF0-6; Sequence=VSP_016570;
CC   -!- TISSUE SPECIFICITY: Expressed in brain and lung.
CC   -!- SIMILARITY: Belongs to the semaphorin family.
CC   -!- SIMILARITY: Contains 1 PSI domain.
CC   -!- SIMILARITY: Contains 1 Sema domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65797.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AB091532; BAD05168.1; -; mRNA.
DR   EMBL; AB091533; BAD05169.1; -; mRNA.
DR   EMBL; AB091534; BAD05170.1; -; mRNA.
DR   EMBL; AB091535; BAD05171.1; -; mRNA.
DR   EMBL; AB091536; BAD05172.1; -; mRNA.
DR   EMBL; AK122515; BAC65797.1; ALT_INIT; mRNA.
DR   EMBL; AL935323; CAM20227.1; -; Genomic_DNA.
DR   EMBL; BC060680; AAH60680.1; -; mRNA.
DR   IPI; IPI00396759; -.
DR   IPI; IPI00408849; -.
DR   IPI; IPI00469540; -.
DR   IPI; IPI00469637; -.
DR   IPI; IPI00675977; -.
DR   IPI; IPI00754823; -.
DR   RefSeq; NP_766125.2; NM_172537.3.
DR   RefSeq; NP_954708.1; NM_199238.2.
DR   RefSeq; NP_954709.1; NM_199239.2.
DR   RefSeq; NP_954710.1; NM_199240.2.
DR   RefSeq; NP_954711.1; NM_199241.2.
DR   UniGene; Mm.330536; -.
DR   ProteinModelPortal; Q76KF0; -.
DR   SMR; Q76KF0; 23-565.
DR   STRING; Q76KF0; -.
DR   PhosphoSite; Q76KF0; -.
DR   PRIDE; Q76KF0; -.
DR   Ensembl; ENSMUST00000051419; ENSMUSP00000061123; ENSMUSG00000027200.
DR   Ensembl; ENSMUST00000076335; ENSMUSP00000075674; ENSMUSG00000027200.
DR   Ensembl; ENSMUST00000077847; ENSMUSP00000077014; ENSMUSG00000027200.
DR   Ensembl; ENSMUST00000078621; ENSMUSP00000077691; ENSMUSG00000027200.
DR   Ensembl; ENSMUST00000103239; ENSMUSP00000099529; ENSMUSG00000027200.
DR   GeneID; 214968; -.
DR   KEGG; mmu:214968; -.
DR   UCSC; uc008mbk.1; mouse.
DR   UCSC; uc008mbo.1; mouse.
DR   UCSC; uc008mbp.1; mouse.
DR   UCSC; uc008mbr.1; mouse.
DR   UCSC; uc008mbt.1; mouse.
DR   CTD; 214968; -.
DR   MGI; MGI:2387661; Sema6d.
DR   GeneTree; ENSGT00580000081327; -.
DR   HOGENOM; HBG713978; -.
DR   HOVERGEN; HBG072910; -.
DR   InParanoid; Q76KF0; -.
DR   OMA; IYRSMGD; -.
DR   PhylomeDB; Q76KF0; -.
DR   NextBio; 374545; -.
DR   ArrayExpress; Q76KF0; -.
DR   Bgee; Q76KF0; -.
DR   Genevestigator; Q76KF0; -.
DR   GermOnline; ENSMUSG00000027200; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004872; F:receptor activity; IEA:InterPro.
DR   GO; GO:0030215; F:semaphorin receptor binding; IPI:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   InterPro; IPR003659; Plexin-like.
DR   InterPro; IPR016201; Plexin-like_fold.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR001627; Semaphorin/CD100_Ag.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF01437; PSI; 1.
DR   Pfam; PF01403; Sema; 1.
DR   SMART; SM00423; PSI; 1.
DR   SMART; SM00630; Sema; 1.
DR   SUPFAM; SSF103575; Plexin-like_fold; 1.
DR   SUPFAM; SSF101912; Sema; 1.
DR   PROSITE; PS51004; SEMA; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Developmental protein; Differentiation;
KW   Disulfide bond; Glycoprotein; Membrane; Neurogenesis; Phosphoprotein;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21   1073       Semaphorin-6D.
FT                                /FTId=PRO_0000044616.
FT   TOPO_DOM     21    662       Extracellular (Potential).
FT   TRANSMEM    663    683       Helical; (Potential).
FT   TOPO_DOM    684   1073       Cytoplasmic (Potential).
FT   DOMAIN       27    512       Sema.
FT   DOMAIN      514    569       PSI.
FT   MOD_RES    1026   1026       Phosphoserine (By similarity).
FT   CARBOHYD     51     51       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    283    283       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    435    435       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    461    461       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    631    631       N-linked (GlcNAc...) (Potential).
FT   DISULFID    108    118       By similarity.
FT   DISULFID    136    145       By similarity.
FT   DISULFID    259    370       By similarity.
FT   DISULFID    284    329       By similarity.
FT   VAR_SEQ     549    549       L -> LLLTEDFFAFHNHS (in isoform 1 and
FT                                isoform 5).
FT                                /FTId=VSP_016568.
FT   VAR_SEQ     570    644       Missing (in isoform 1 and isoform 2).
FT                                /FTId=VSP_016569.
FT   VAR_SEQ     570    588       Missing (in isoform 6).
FT                                /FTId=VSP_016570.
FT   VAR_SEQ     589    644       Missing (in isoform 3 and isoform 5).
FT                                /FTId=VSP_016571.
SQ   SEQUENCE   1073 AA;  119815 MW;  D985053A2D37DA2A CRC64;
     MGFLLLWFCV LFLLVSRLRA VSFPEDDEPL NTVDYHYSRQ YPVFRGRPSG NESQHRLDFQ
     LMLKIRDTLY IAGRDQVYTV NLNEIPQTEV IPSKKLTWRS RQQDRENCAM KGKHKDECHN
     FIKVFVPRND EMVFVCGTNA FNPMCRYYRL RTLEYDGEEI SGLARCPFDA RQTNVALFAD
     GKLYSATVAD FLASDAVIYR SMGDGSALRT IKYDSKWIKE PHFLHAIEYG NYVYFFFREI
     AVEHNNLGKA VYSRVARICK NDMGGSQRVL EKHWTSFLKA RLNCSVPGDS FFYFDVLQSI
     TDIIQINGIP TVVGVFTTQL NSIPGSAVCA FSMDDIEKVF KGRFKEQKTP DSVWTAVPED
     KVPKPRPGCC AKHGLAEAYK TSIDFPDDTL AFIKSHPLMD SAVPPIADEP WFTKTRVRYR
     LTAIEVDRSA GPYQNYTVIF VGSEAGVVLK VLAKTSPFSL NDSVLLEEIE AYNPAKCSAE
     SEEDRKVVSL QLDKDHHALY VAFSSCVVRI PLSRCERYGS CKKSCIASRD PYCGWLSQGV
     CERVTLGMLP GGYEQDTEYG NTAHLGDCHE SLPPSTTPDY KIFGGPTSDM EVSSSSVTTV
     ASSPEITSKV IDTWRPKLTS SRKFVVQDDP NTSDFTDTIS GIPKGVRWEV QSGESNQMVH
     MNVLITCVFA AFVLGAFIAG VAVYCYRDMF VRKNRKIHKD AESAQSCTDS SGSFAKLNGL
     FDSPVKEYQQ NIDSPKLYSN LLTSRKELPP NTDTKSMAVD HRGQPPELAA LPTPESTPVL
     HQKTLQAMKS HSEKAHSHGA SRKEHPQFFP SSPPPHSPLS HGHIPSAIVL PNATHDYNTS
     FSNSNAHKAE KKLQSMDHPL TKSSSKREHR RSVDSRNTLN DLLKHLNDPN SNPKAILGEI
     HMAHQTLMLD PVGPMAEVPP KVPNREASLY SPPSTLPRNS PTKRVDVPTT PGVPMTSLER
     QRGYHKNSSQ RHSISAVPKN LNSPNGVLLS RQPSMNRGGY MPTPTGAKVD YIQGTPVSVH
     LQPSLSRQSS YTSNGTLPRT GLKRTPSLKP DVPPKPSFVP QTTSVRPLNK YTY
//
ID   FHOD3_MOUSE             Reviewed;        1578 AA.
AC   Q76LL6; B2RQR3; Q5DTV7; Q76HP7; Q76LL5;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=FH1/FH2 domain-containing protein 3;
DE   AltName: Full=Formin homolog overexpressed in spleen 2;
DE            Short=mFHOS2;
GN   Name=Fhod3; Synonyms=Fhos2, Kiaa1695;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4), TISSUE SPECIFICITY,
RP   AND FUNCTION.
RX   PubMed=15966898; DOI=10.1111/j.1365-2443.2005.00867.x;
RA   Kanaya H., Takeya R., Takeuchi K., Watanabe N., Jing N., Sumimoto H.;
RT   "Fhos2, a novel formin-related actin-organizing protein, probably
RT   associates with the nestin intermediate filament.";
RL   Genes Cells 10:665-678(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 120-1578 (ISOFORM 3).
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Actin-organizing protein that may cause stress fiber
CC       formation together with cell elongation.
CC   -!- SUBUNIT: Interacts with nestin/NES-based interfilament (IF) (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Main part of
CC       the protein localizes to actin fibers and the remaining part
CC       displays filamentous staining (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Named isoforms=3;
CC       Name=1; Synonyms=FHOS2L;
CC         IsoId=Q76LL6-1; Sequence=Displayed;
CC         Note=Major form in heart;
CC       Name=2; Synonyms=FHOS2S;
CC         IsoId=Q76LL6-2; Sequence=VSP_024400;
CC         Note=Major form in kidney and brain;
CC       Name=3;
CC         IsoId=Q76LL6-3; Sequence=VSP_024400, VSP_024401;
CC         Note=No experimental confirmation available;
CC       Name=4; Synonyms=FHOS2M;
CC         IsoId=Q76LL6-4; Sequence=VSP_024399;
CC   -!- TISSUE SPECIFICITY: Expressed in the heart, kidney and brain.
CC   -!- SIMILARITY: Belongs to the formin homology family.
CC   -!- SIMILARITY: Contains 1 DAD (diaphanous autoregulatory) domain.
CC   -!- SIMILARITY: Contains 1 FH1 (formin homology 1) domain.
CC   -!- SIMILARITY: Contains 1 FH2 (formin homology 2) domain.
CC   -!- SIMILARITY: Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology
CC       3) domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AB078608; BAC98302.1; -; mRNA.
DR   EMBL; AB078609; BAC98303.1; -; mRNA.
DR   EMBL; AB100088; BAC98348.1; -; mRNA.
DR   EMBL; BC138046; AAI38047.1; -; mRNA.
DR   EMBL; AK220413; BAD90459.1; -; mRNA.
DR   IPI; IPI00420975; -.
DR   IPI; IPI00622053; -.
DR   IPI; IPI00844798; -.
DR   IPI; IPI00844816; -.
DR   RefSeq; NP_780485.2; NM_175276.3.
DR   UniGene; Mm.329322; -.
DR   ProteinModelPortal; Q76LL6; -.
DR   SMR; Q76LL6; 2-327, 1112-1436.
DR   PhosphoSite; Q76LL6; -.
DR   PRIDE; Q76LL6; -.
DR   Ensembl; ENSMUST00000037097; ENSMUSP00000041361; ENSMUSG00000034295.
DR   Ensembl; ENSMUST00000091991; ENSMUSP00000089617; ENSMUSG00000034295.
DR   Ensembl; ENSMUST00000115819; ENSMUSP00000111486; ENSMUSG00000034295.
DR   Ensembl; ENSMUST00000115820; ENSMUSP00000111487; ENSMUSG00000034295.
DR   GeneID; 225288; -.
DR   KEGG; mmu:225288; -.
DR   UCSC; uc008ehb.1; mouse.
DR   CTD; 225288; -.
DR   MGI; MGI:1925847; Fhod3.
DR   eggNOG; roNOG15486; -.
DR   GeneTree; ENSGT00560000076948; -.
DR   HOGENOM; HBG446794; -.
DR   HOVERGEN; HBG051615; -.
DR   InParanoid; Q76LL6; -.
DR   OMA; NPRELRI; -.
DR   OrthoDB; EOG4N04DC; -.
DR   PhylomeDB; Q76LL6; -.
DR   NextBio; 377609; -.
DR   ArrayExpress; Q76LL6; -.
DR   Bgee; Q76LL6; -.
DR   CleanEx; MM_FHOD3; -.
DR   Genevestigator; Q76LL6; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   InterPro; IPR003104; Actin-bd_FH2/DRF_autoreg.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR014767; Diaphanous_autoregulatory.
DR   InterPro; IPR015425; FH2_actin-bd.
DR   InterPro; IPR014768; GTPase-bd/formin_homology_3.
DR   Pfam; PF02181; FH2; 1.
DR   SMART; SM00498; FH2; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF101447; FH2_actin_bd; 1.
DR   PROSITE; PS51231; DAD; 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Alternative splicing; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Phosphoprotein.
FT   CHAIN         1   1578       FH1/FH2 domain-containing protein 3.
FT                                /FTId=PRO_0000283792.
FT   DOMAIN       18    405       GBD/FH3.
FT   DOMAIN      985   1016       FH1.
FT   DOMAIN     1039   1435       FH2.
FT   DOMAIN     1515   1547       DAD.
FT   COILED      597    645       Potential.
FT   COMPBIAS    553    596       Ser-rich.
FT   COMPBIAS    784    793       Poly-Ser.
FT   COMPBIAS    985   1016       Pro-rich.
FT   MOD_RES     376    376       Phosphoserine (By similarity).
FT   MOD_RES     379    379       Phosphothreonine (By similarity).
FT   MOD_RES     380    380       Phosphoserine (By similarity).
FT   VAR_SEQ     400    432       KDEEEEEEEEQPITEPNSEEEREDDAQCQGKDS -> N
FT                                (in isoform 4).
FT                                /FTId=VSP_024399.
FT   VAR_SEQ     401    551       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_024400.
FT   VAR_SEQ     992   1005       Missing (in isoform 3).
FT                                /FTId=VSP_024401.
FT   CONFLICT    575    575       Y -> S (in Ref. 3; BAD90459).
FT   CONFLICT    690    690       S -> P (in Ref. 3; BAD90459).
FT   CONFLICT    856    856       G -> S (in Ref. 3; BAD90459).
SQ   SEQUENCE   1578 AA;  175655 MW;  F9EE9B7354D51A70 CRC64;
     MATLACRVQF LDDTDPFNST NFPEPSRPPL FTFREDLALG TQLAGVHRLL RAPHKLDDCT
     LQLSHNGAYL DLEATLAEQR DELEGFQDDT GRGKKNSIIL RTQLSVRVHA CIEKLYNSSG
     RDLRRALFSL KQIFQDDKDL VHEFVIAEGL TCLIKVGAEA DQNYQNYILR ALGQIMLYVD
     GMNGVINHSE TIQWLYTLVG SKFRLVVKTA LKLLLVFVEY SESNAPLLIQ AVSAVDTKRG
     VKPWSNIMEI LEEKDGVDTE LLVYAMTLVN KTLAGLPDQD TFYDVVDCLE ELGIAAVSQR
     HLNKKGTDLD LLEQFNIYEV ALRHEDGDET AEPPPSGHRD RRRASMCSGG TVGEQQGLDR
     RRSRRHSIQN IKSPLSAPTS PCSPSVPAFK PSQVRDLCEK DEEEEEEEEQ PITEPNSEEE
     REDDAQCQGK DSKASSASGQ SSPGKDAAPE SSALHTTSSP TSQGRWLSAS TAARSPVLGG
     TSGPEASRPA ARLLPPSPGL ATRPSTAPKV SPTIDKLPYV PHSPFHLFSY DFEDSPLLTK
     DKGGDSQTEN RYSNFSSNSF QSSRPSPGPS GSPSYASSFS SPQDTRSSPS GLLTSSFRQH
     QESLAAERER RRQEREERLQ RIEREERNKF NREYLDKREE QRQARGERYK YLEQLAAETQ
     EKEPRSQSVS RGRADLSLDL SLPAAPAPPS PSSQSPSADS QEALPVPSSP PTLQCPQVSG
     KDHEPELEAE AGQGADEASQ DIASAHRGAE SQEEPVLELE PEERASLSEK ERQNEEVNER
     DNCSASSISS SSSTLEREEK EDKLSEDRAT GLWSTSLQDV GVNGQCGDIL TSKRFMLDML
     YAHNRKSTED EEKDDGEPGR SAQEVEAVAS LATRISTLQA NSQAPEESIK RVDIGCLDNR
     GSVKAFAEKF NSGEVGRGAI SPDVESQDKV PDTPPAQLKT ESDYIWDQLM ANPRELRIQD
     MDFTDLGEED DIDVLDVDLG HREAPGPPPP PPPTFLGLPP PPPPPLLDSV PPPPVPGNLL
     ASPVFNTPQG LGWSQVPRGQ PAFTKKKKTI RLFWNEVRPF EWPSKNNRRC REFLWSKLEP
     IKVDTSRLEH LFESKSKELS VTKKTAADGK RQEIIVLDSK RSNAINIGLT VLPPPRTIKI
     AILNFDEYAL NKEGIEKILT MIPTEEEKQK IQEAQLANPE VPLGSAEQFL LTLSSISELS
     ARLHLWAFKM DYETTEKEVA EPLLDLKEGI DQLENNKTLG FILSTLLAIG NFLNGTNAKA
     FELSYLEKVP EVKDTVHKQS LLHHVCTMVV ENFPDSSDLY SEIGAITRSA KVDFDQLQDN
     LCQMERRCKA SWDHLKAIAK HEMKPVLKQR MSEFLKDCAE RIIILKIVHR RIINRFHSFL
     LFMGHPPYAI REVNINKFCR IISEFALEYR TTRERVLQQK QKRANHRERN KTRGKMITDS
     GKFSGSSPAA PSQPQGLSYA EDAAEHENMK AVLKTSSPAL EDATPVLGVR TRSRASRGST
     SSWTMGTEES PSVTDDAADE IMDRIVKSAT QVPSQRVVPR ERKRSRANRK SLRRTLKSGL
     TPEEARALGL VGTSELQL
//
ID   FA63A_MOUSE             Reviewed;         468 AA.
AC   Q76LS9; Q3TEF4; Q52KE4; Q566I9; Q6PES4; Q80V14; Q8CB41; Q8CHR2;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   RecName: Full=Protein FAM63A;
DE   AltName: Full=NF-E2 inducible protein;
GN   Name=Fam63a; Synonyms=Ni;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Nagata Y., Oda M., Haruta H., Todokoro K.;
RT   "NF-E2 inducible megakaryocyte specific novel gene.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Thymus, and Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6, Czech II, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382 AND SER-440, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-440, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q76LS9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q76LS9-2; Sequence=VSP_034718;
CC       Name=3;
CC         IsoId=Q76LS9-3; Sequence=VSP_034716, VSP_034717;
CC   -!- SIMILARITY: Belongs to the FAM63 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH39762.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential vector sequence;
CC   -----------------------------------------------------------------------
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DR   EMBL; AB075603; BAD06451.1; -; mRNA.
DR   EMBL; AK036838; BAC29601.1; -; mRNA.
DR   EMBL; AK169673; BAE41294.1; -; mRNA.
DR   EMBL; BC039762; AAH39762.1; ALT_SEQ; mRNA.
DR   EMBL; BC051048; AAH51048.1; -; mRNA.
DR   EMBL; BC057901; AAH57901.1; -; mRNA.
DR   EMBL; BC093521; AAH93521.1; -; mRNA.
DR   EMBL; BC094388; AAH94388.1; -; mRNA.
DR   EMBL; BC132301; AAI32302.1; -; mRNA.
DR   IPI; IPI00454014; -.
DR   IPI; IPI00669013; -.
DR   IPI; IPI00830404; -.
DR   RefSeq; NP_598619.2; NM_133858.4.
DR   RefSeq; NP_955769.1; NM_199475.1.
DR   UniGene; Mm.279287; -.
DR   STRING; Q76LS9; -.
DR   PRIDE; Q76LS9; -.
DR   Ensembl; ENSMUST00000039537; ENSMUSP00000043910; ENSMUSG00000038712.
DR   Ensembl; ENSMUST00000107187; ENSMUSP00000102805; ENSMUSG00000038712.
DR   GeneID; 75007; -.
DR   KEGG; mmu:75007; -.
DR   CTD; 75007; -.
DR   MGI; MGI:1922257; Fam63a.
DR   GeneTree; ENSGT00390000016607; -.
DR   HOVERGEN; HBG054318; -.
DR   InParanoid; Q76LS9; -.
DR   OMA; VDQDYLI; -.
DR   OrthoDB; EOG4XH006; -.
DR   PhylomeDB; Q76LS9; -.
DR   NextBio; 341996; -.
DR   ArrayExpress; Q76LS9; -.
DR   Bgee; Q76LS9; -.
DR   Genevestigator; Q76LS9; -.
DR   InterPro; IPR007518; DUF544.
DR   PANTHER; PTHR18063; DUF544; 1.
DR   Pfam; PF04424; DUF544; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    468       Protein FAM63A.
FT                                /FTId=PRO_0000344038.
FT   COMPBIAS    386    432       Gln-rich.
FT   MOD_RES     103    103       Phosphoserine.
FT   MOD_RES     382    382       Phosphoserine.
FT   MOD_RES     440    440       Phosphoserine.
FT   VAR_SEQ       1    169       Missing (in isoform 3).
FT                                /FTId=VSP_034716.
FT   VAR_SEQ     170    191       LGNCLLSIKPQEKSEGLQLNFQ -> MKHGMVGGREGRLDQ
FT                                PSCLFSH (in isoform 3).
FT                                /FTId=VSP_034717.
FT   VAR_SEQ     392    400       Missing (in isoform 2).
FT                                /FTId=VSP_034718.
FT   CONFLICT     61     61       Q -> E (in Ref. 2; BAE41294).
FT   CONFLICT    324    324       T -> A (in Ref. 3; AAH94388).
SQ   SEQUENCE   468 AA;  51226 MW;  1C52C022A3D5DBA9 CRC64;
     MEQPQTENPA PSKATSAETV ESENHEALSG PEKHPQDKDG ADADGAAGEQ EPGDQTLPPA
     QDGENLECPP PEASSSPPGP ACGTSPKVET AEVCSRPQEL PQSPRIQQPE LDFYCVKWIP
     WKGERTPIIT QSTNGPCPLL AIMNILFLQW KVKLPPQKEV ITSDELLTHL GNCLLSIKPQ
     EKSEGLQLNF QQNVDDAMTV LPKLATGLDV NVRFTGVSDF EYTPECSIFD LLGIPLYHGW
     LVDPQSPEAV SAVGKLSYNQ LVEKIITCKH SSDSNLVTEG LVAEQFLETT AAQLTYHGLC
     ELTAAATEDE LSVFFRNNHF STMTKHKSHL YLLVTDQGFL QEEQVVWESL HNVDGDSCFC
     DSDFHLSHSL GKSHGAEGGG GSPEKQLQVD QDYLIALSLQ QQQQPQGTLG LSDLELAQQL
     QQEEYQQQQA VQPVRTRAPS PQGRGATSGR PAGERRQRSK TESDCVLL
//
ID   STALP_MOUSE             Reviewed;         436 AA.
AC   Q76N33; Q76LY0; Q8VEK5;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=AMSH-like protease;
DE            Short=AMSH-LP;
DE            EC=3.4.19.-;
DE   AltName: Full=AMSH family protein;
DE            Short=AMSH-FP;
DE   AltName: Full=STAM-binding protein-like 1;
GN   Name=Stambpl1; Synonyms=Amshlp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=22824679; PubMed=12943674; DOI=10.1016/S0006-291X(03)01550-X;
RA   Kitajima K., Matsumoto K., Tahara M., Takahashi H., Nakamura T.,
RA   Nakamura T.;
RT   "A newly identified AMSH-family protein is specifically expressed in
RT   haploid stages of testicular germ cells.";
RL   Biochem. Biophys. Res. Commun. 309:135-142(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Ishii N., Sugamura K.;
RT   "Cloning of a gene for the mouse AMSH-like-protein.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Zinc metalloprotease that specifically cleaves 'Lys-63'-
CC       linked polyubiquitin chains. Does not cleave 'Lys-48'-linked
CC       polyubiquitin chains (By similarity).
CC   -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=AMSH-FPalpha, ALM alpha;
CC         IsoId=Q76N33-1; Sequence=Displayed;
CC       Name=2; Synonyms=AMSH-FPbeta, ALM beta;
CC         IsoId=Q76N33-2; Sequence=VSP_014649;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed. Isoform 1 is widely
CC       expressed while isoform 2 is testis-specific.
CC   -!- DOMAIN: The JAMM motif is essential for the protease activity (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the peptidase M67C family.
CC   -!- SIMILARITY: Contains 1 MPN (JAB/Mov34) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH18343.1; Type=Erroneous initiation;
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DR   EMBL; AB066211; BAD00166.1; -; mRNA.
DR   EMBL; AB066212; BAD00167.1; -; mRNA.
DR   EMBL; AB066213; BAD00168.1; -; mRNA.
DR   EMBL; AB010121; BAD06408.1; -; mRNA.
DR   EMBL; AB010122; BAD06409.1; -; mRNA.
DR   EMBL; BC018343; AAH18343.1; ALT_INIT; mRNA.
DR   IPI; IPI00312188; -.
DR   IPI; IPI00608113; -.
DR   RefSeq; NP_083958.3; NM_029682.4.
DR   UniGene; Mm.130952; -.
DR   ProteinModelPortal; Q76N33; -.
DR   SMR; Q76N33; 263-436.
DR   STRING; Q76N33; -.
DR   MEROPS; M67.003; -.
DR   PhosphoSite; Q76N33; -.
DR   PRIDE; Q76N33; -.
DR   Ensembl; ENSMUST00000054956; ENSMUSP00000059927; ENSMUSG00000024776.
DR   Ensembl; ENSMUST00000119603; ENSMUSP00000112938; ENSMUSG00000024776.
DR   GeneID; 76630; -.
DR   KEGG; mmu:76630; -.
DR   UCSC; uc008hgc.1; mouse.
DR   UCSC; uc008hge.1; mouse.
DR   CTD; 76630; -.
DR   MGI; MGI:1923880; Stambpl1.
DR   GeneTree; ENSGT00390000015439; -.
DR   HOGENOM; HBG443817; -.
DR   HOVERGEN; HBG058519; -.
DR   InParanoid; Q76N33; -.
DR   OMA; PRDLCHK; -.
DR   OrthoDB; EOG415GDF; -.
DR   PhylomeDB; Q76N33; -.
DR   BRENDA; 3.1.2.15; 244.
DR   NextBio; 345496; -.
DR   ArrayExpress; Q76N33; -.
DR   Bgee; Q76N33; -.
DR   CleanEx; MM_STAMBPL1; -.
DR   Genevestigator; Q76N33; -.
DR   GermOnline; ENSMUSG00000024776; Mus musculus.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:EC.
DR   InterPro; IPR000555; Mov34_MPN_PAD1.
DR   Pfam; PF01398; Mov34; 1.
DR   SMART; SM00232; JAB_MPN; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Hydrolase; Metal-binding; Metalloprotease;
KW   Phosphoprotein; Protease; Ubl conjugation pathway; Zinc.
FT   CHAIN         1    436       AMSH-like protease.
FT                                /FTId=PRO_0000194875.
FT   DOMAIN      264    373       MPN.
FT   MOTIF       347    360       JAMM motif.
FT   METAL       347    347       Zinc 1; catalytic (By similarity).
FT   METAL       349    349       Zinc 1; catalytic (By similarity).
FT   METAL       360    360       Zinc 1; catalytic (By similarity).
FT   METAL       362    362       Zinc 2 (By similarity).
FT   METAL       402    402       Zinc 2 (By similarity).
FT   METAL       408    408       Zinc 2 (By similarity).
FT   METAL       410    410       Zinc 2 (By similarity).
FT   SITE        292    292       Indirect zinc-binding (By similarity).
FT   MOD_RES      25     25       Phosphoserine (By similarity).
FT   MOD_RES     242    242       Phosphoserine (By similarity).
FT   VAR_SEQ       1    166       Missing (in isoform 2).
FT                                /FTId=VSP_014649.
FT   CONFLICT    194    194       I -> M (in Ref. 3; AAH18343).
FT   CONFLICT    201    201       V -> M (in Ref. 3; AAH18343).
SQ   SEQUENCE   436 AA;  49640 MW;  6AF263DF5EC4FD9B CRC64;
     MEQPFTVNSL KKLAAMPDHT DVSLSPEERV RALSKLGCNI SINEDITPRR YFRSGVEMER
     MASVYLEEGN LENAFVLYNK FITLFVEKLP SHRDYQQCAV PEKQDIMKKL KEIAFPRTDE
     LKTDLLRKYN IEYQEYLQSK NKYKAEILKK LEHQRLIEAE RQRIAQMRQQ QLESEQFLFF
     EDQLKKQELA RGQIRGQDSP VLSEQTDGSA LSCFSTHQSN SLRNAFADHP HKSDGSNFAN
     YSPPVNRALK PAATLSAVQN LVVEGLRCVV LSRDLCHKFL LLADSNTVRG IETCGILCGK
     LTHNEFTITH VVVPKQSAGP DYCDVENVEE LFNVQDQHGL LTLGWIHTHP TQTAFLSSVD
     LHTHCSYQLM LPEAIAIVCS PKHKDTGIFR LTNAGMLEVS TCKKKGFHPH TKDPKLFSIC
     SHVLVKDIKT TVLDLR
//
ID   USMG5_MOUSE             Reviewed;          58 AA.
AC   Q78IK2; Q9ER48;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Up-regulated during skeletal muscle growth protein 5;
GN   Name=Usmg5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/10; TISSUE=Skeletal muscle;
RA   Sadusky T.J., Kemp T.J.;
RT   "Isolation and characterisation of genes expressed in response to
RT   active stretch of skeletal muscle.";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-16 AND LYS-17, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Single-pass membrane
CC       protein (By similarity).
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DR   EMBL; AJ290947; CAC03620.1; -; mRNA.
DR   EMBL; BC087919; AAH87919.1; -; mRNA.
DR   IPI; IPI00624653; -.
DR   RefSeq; NP_075700.2; NM_023211.4.
DR   RefSeq; XP_003085299.1; XM_003085251.1.
DR   RefSeq; XP_003086413.1; XM_003086365.1.
DR   RefSeq; XP_003086874.1; XM_003086826.1.
DR   UniGene; Mm.29722; -.
DR   STRING; Q78IK2; -.
DR   PhosphoSite; Q78IK2; -.
DR   PRIDE; Q78IK2; -.
DR   Ensembl; ENSMUST00000096014; ENSMUSP00000093713; ENSMUSG00000071528.
DR   GeneID; 100503459; -.
DR   GeneID; 100504912; -.
DR   GeneID; 66477; -.
DR   KEGG; mmu:100503459; -.
DR   KEGG; mmu:100504912; -.
DR   KEGG; mmu:66477; -.
DR   UCSC; uc008huo.1; mouse.
DR   CTD; 66477; -.
DR   MGI; MGI:1891435; Usmg5.
DR   eggNOG; roNOG17541; -.
DR   GeneTree; ENSGT00390000015489; -.
DR   HOGENOM; HBG125797; -.
DR   HOVERGEN; HBG094140; -.
DR   InParanoid; Q78IK2; -.
DR   OMA; LRPKKTP; -.
DR   OrthoDB; EOG4BRWNG; -.
DR   NextBio; 321798; -.
DR   ArrayExpress; Q78IK2; -.
DR   Bgee; Q78IK2; -.
DR   CleanEx; MM_USMG5; -.
DR   Genevestigator; Q78IK2; -.
DR   GermOnline; ENSMUSG00000071528; Mus musculus.
DR   GermOnline; ENSMUSG00000071791; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   InterPro; IPR009125; DAPIT.
DR   PRINTS; PR01821; DAPIT.
PE   1: Evidence at protein level;
KW   Acetylation; Membrane; Mitochondrion; Transmembrane;
KW   Transmembrane helix.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2     58       Up-regulated during skeletal muscle
FT                                growth protein 5.
FT                                /FTId=PRO_0000231579.
FT   TRANSMEM     23     45       Helical; (Potential).
FT   MOD_RES      16     16       N6-acetyllysine.
FT   MOD_RES      17     17       N6-acetyllysine.
FT   CONFLICT      5      5       E -> K (in Ref. 1; CAC03620).
FT   CONFLICT     27     27       R -> K (in Ref. 1; CAC03620).
FT   CONFLICT     55     55       V -> A (in Ref. 1; CAC03620).
FT   CONFLICT     58     58       T -> TMDFEMSDLTC (in Ref. 1).
SQ   SEQUENCE   58 AA;  6382 MW;  7CE34D192253564D CRC64;
     MAGAESDGQF QFTGIKKYFN SYTLTGRMNC VLATYGGIAL LVLYFKLRPK KTPAVKAT
//
ID   APOOL_MOUSE             Reviewed;         265 AA.
AC   Q78IK4;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Apolipoprotein O-like;
DE   AltName: Full=Protein FAM121A;
DE   Flags: Precursor;
GN   Name=Apool; Synonyms=Fam121a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Secreted (Potential).
CC   -!- SIMILARITY: Belongs to the apolipoprotein O family.
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DR   EMBL; BC024334; AAH24334.1; -; mRNA.
DR   IPI; IPI00112493; -.
DR   RefSeq; NP_080841.1; NM_026565.2.
DR   UniGene; Mm.161014; -.
DR   ProteinModelPortal; Q78IK4; -.
DR   PRIDE; Q78IK4; -.
DR   Ensembl; ENSMUST00000026599; ENSMUSP00000026599; ENSMUSG00000025525.
DR   GeneID; 68117; -.
DR   KEGG; mmu:68117; -.
DR   UCSC; uc009udh.1; mouse.
DR   CTD; 68117; -.
DR   MGI; MGI:1915367; Apool.
DR   eggNOG; roNOG13709; -.
DR   GeneTree; ENSGT00530000063666; -.
DR   HOVERGEN; HBG055885; -.
DR   OrthoDB; EOG4T1HNV; -.
DR   PhylomeDB; Q78IK4; -.
DR   NextBio; 326466; -.
DR   ArrayExpress; Q78IK4; -.
DR   Bgee; Q78IK4; -.
DR   CleanEx; MM_APOOL; -.
DR   Genevestigator; Q78IK4; -.
DR   GermOnline; ENSMUSG00000025525; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   InterPro; IPR019166; Apolipoprotein_O.
DR   Pfam; PF09769; ApoO; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Secreted; Signal.
FT   SIGNAL        1     26       Potential.
FT   CHAIN        27    265       Apolipoprotein O-like.
FT                                /FTId=PRO_0000042054.
FT   CARBOHYD    189    189       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   265 AA;  29261 MW;  3DBAFD5D0AA3DC78 CRC64;
     MAAFRMGKLT TIPAGLIYAS INVRLAKEEE PKKQLVRPDQ LPIYTAPPLH SKYVEEQPGN
     LQRGFASIRT TTVYYIGWCK SIYLFMKNGV MDTVQFGKDA YVYLKNPPQD FLPKMGVITA
     SGLAGLLSAR KGSRFKKIAY PLGLATLGAT VCYPAQSVII AKITGKKAYA TSQQIFQAIK
     SLWTQKSENE SLPEPKEESK EGRSDEIHAS LPDLKHSVSL PKELASATVI KSESTSGTTQ
     FIPDPKLMDH GQSHPDDKDM YSTRS
//
ID   SND1_MOUSE              Reviewed;         910 AA.
AC   Q78PY7; Q3TT46; Q922L5; Q9R0S1;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Staphylococcal nuclease domain-containing protein 1;
DE   AltName: Full=100 kDa coactivator;
DE   AltName: Full=p100 co-activator;
GN   Name=Snd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Tsuchiya N., Fukuda H., Yamaguchi A., Sugimura T., Nagao M.,
RA   Nakagama H.;
RT   "Cloning and characterization of a cDNA encoding a mouse p100 co-
RT   activator.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Pituitary, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH STAT5.
RX   PubMed=12819296; DOI=10.1210/me.2002-0256;
RA   Paukku K., Yang J., Silvennoinen O.;
RT   "Tudor and nuclease-like domains containing protein p100 function as
RT   coactivators for signal transducer and activator of transcription 5.";
RL   Mol. Endocrinol. 17:1805-1814(2003).
CC   -!- FUNCTION: Functions as a bridging factor between STAT6 and the
CC       basal transcription factor. Plays a role in PIM1 regulation of MYB
CC       activity. Plays a role in cell viability (By similarity).
CC       Functions as a transcriptional coactivator for STAT5.
CC   -!- SUBUNIT: Interacts with GTF2E1 and GTF2E2. Forms a ternary complex
CC       with STAT6 and POLR2A (By similarity). Interacts with STAT5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Melanosome (By similarity). Note=In IL-4 stimulated
CC       cells colocalizes with STAT6 in the nucleus (By similarity).
CC   -!- PTM: Phosphorylated by PIM1 in vitro (By similarity).
CC   -!- SIMILARITY: Contains 4 TNase-like domains.
CC   -!- SIMILARITY: Contains 1 Tudor domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA84944.1; Type=Erroneous initiation;
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DR   EMBL; AB021491; BAA84944.1; ALT_INIT; mRNA.
DR   EMBL; AK088028; BAC40105.1; -; mRNA.
DR   EMBL; AK161591; BAE36479.1; -; mRNA.
DR   EMBL; BC007126; AAH07126.3; -; mRNA.
DR   IPI; IPI00123129; -.
DR   RefSeq; NP_062750.2; NM_019776.2.
DR   UniGene; Mm.439987; -.
DR   ProteinModelPortal; Q78PY7; -.
DR   SMR; Q78PY7; 243-327, 340-897.
DR   STRING; Q78PY7; -.
DR   PhosphoSite; Q78PY7; -.
DR   PRIDE; Q78PY7; -.
DR   Ensembl; ENSMUST00000001460; ENSMUSP00000001460; ENSMUSG00000001424.
DR   GeneID; 56463; -.
DR   KEGG; mmu:56463; -.
DR   UCSC; uc009bct.1; mouse.
DR   CTD; 56463; -.
DR   MGI; MGI:1929266; Snd1.
DR   GeneTree; ENSGT00510000047270; -.
DR   HOGENOM; HBG398223; -.
DR   HOVERGEN; HBG057234; -.
DR   InParanoid; Q78PY7; -.
DR   OMA; PQDEDAR; -.
DR   OrthoDB; EOG45755W; -.
DR   PhylomeDB; Q78PY7; -.
DR   NextBio; 312718; -.
DR   ArrayExpress; Q78PY7; -.
DR   Bgee; Q78PY7; -.
DR   Genevestigator; Q78PY7; -.
DR   GermOnline; ENSMUSG00000001424; Mus musculus.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016442; C:RNA-induced silencing complex; IEA:InterPro.
DR   GO; GO:0004518; F:nuclease activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0016246; P:RNA interference; IEA:InterPro.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR008191; Maternal_tudor.
DR   InterPro; IPR016685; Silence_cplx_Nase-comp_TudorSN.
DR   InterPro; IPR016071; Staphylococal_nuclease_OB-fold.
DR   InterPro; IPR006021; Staphylococcal_nuclease.
DR   InterPro; IPR002071; Thermonucl_AS.
DR   InterPro; IPR002999; Tudor.
DR   InterPro; IPR018351; Tudor_subgroup.
DR   Gene3D; G3DSA:2.40.50.90; SNase; 5.
DR   Pfam; PF00565; SNase; 5.
DR   Pfam; PF00567; TUDOR; 1.
DR   PIRSF; PIRSF017179; RISC-Tudor-SN; 1.
DR   SMART; SM00318; SNc; 4.
DR   SMART; SM00333; TUDOR; 1.
DR   SUPFAM; SSF50199; Staphylococal_nuclease_OB-fold; 5.
DR   PROSITE; PS01123; TNASE_1; FALSE_NEG.
DR   PROSITE; PS01284; TNASE_2; 1.
DR   PROSITE; PS50830; TNASE_3; 4.
DR   PROSITE; PS50304; TUDOR; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Repeat;
KW   Transcription; Transcription regulation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    910       Staphylococcal nuclease domain-containing
FT                                protein 1.
FT                                /FTId=PRO_0000183181.
FT   DOMAIN       18    166       TNase-like 1.
FT   DOMAIN      193    328       TNase-like 2.
FT   DOMAIN      341    496       TNase-like 3.
FT   DOMAIN      525    660       TNase-like 4.
FT   DOMAIN      729    787       Tudor.
FT   MOTIF       321    325       Nuclear localization signal (Potential).
FT   MOTIF       388    392       Nuclear localization signal (Potential).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       4      4       Phosphoserine (By similarity).
FT   MOD_RES      10     10       Phosphoserine (By similarity).
FT   MOD_RES     109    109       Phosphotyrosine (By similarity).
FT   MOD_RES     193    193       N6-acetyllysine (By similarity).
FT   MOD_RES     429    429       Phosphothreonine (By similarity).
FT   MOD_RES     641    641       N6-acetyllysine (By similarity).
FT   MOD_RES     752    752       N6-acetyllysine (By similarity).
FT   MOD_RES     908    908       Phosphotyrosine (By similarity).
FT   MOD_RES     909    909       Phosphoserine (By similarity).
FT   CONFLICT    208    208       V -> A (in Ref. 1; BAA84944).
FT   CONFLICT    908    910       Missing (in Ref. 1; BAA84944).
SQ   SEQUENCE   910 AA;  102088 MW;  7A31459E9274D0B6 CRC64;
     MASSAQSSGS SGGPAVPTVQ RGIVKMVLSG CAIIVRGQPR GGPPPERQIN LSNIRAGNLA
     RRAAATQPDG KDTPDEPWAF PAREFLRKKL IGKEVCFTIE NKTPQGREYG MIYLGKDTNG
     ENIAESLVAE GLATRREGMR ANNPEQNRLS ECEEQAKASK KGMWSEGNGS HTIRDLKYTI
     ENPRHFVDSH HQKPVNAIIE HVRDGSVVRA LLLPGHHLVT VMLSGIKCPT FRRETDGSET
     PEPFAAEAKF FTESRLLQRD VQIILESCHN QNLLGTILHP NGNITELLLK EGFARCVDWS
     IAVYTRGAEK LRAAERFAKE RRLRIWRDYV PPTANLDQKD KQFVAKVMQV LNADAIVVKL
     NSGDYKTIHL SSIRPPRLEG DNIQDKNKKL RPLYDIPYMF EAREFLRKKL IGKKVNVTVD
     YIRPASPATE TVPAFSERTC ATVTIGGINI AEALVSKGLA TVIRYRQDDD QRSSHYDELL
     AAEARAIKNG KGLHSKKEVP IHRVADISGD TQKAKQFLPF LQRAGRSEAV VEYVFSGSRL
     KLYLPKETCL ITFLLAGIEC PRGARNLPGL VQEGEPFSEE ATLFTKELVL QREVEVEVES
     MDKAGNFIGW LHMDGANLSV LLVEQALSKV HFTAERSAYY KPLLSAEEAA KQRKEKVWAH
     YEERPVEEVM PVLEEKERSA SYKPVFVTEI TDDLHFYVQD VETGTQLEKL MENMRNDISS
     HPPVEGSYAP RRGEFCIAKF VDGEWYRARV EKVESPAKVH VFYIDYGNRE ILPSTRLGTL
     PPAFSTRVLP AQATEYAFAF IQVPQDEDAR TDAVDSVVRD IQNTQCLLNV EHLSASCPHV
     TLQFADSKGD VGLGLVKEGL VMVEVRKEKQ FQKVITEYLN AQESAKSARL NLWRYGDFRA
     DDADEFGYSR
//
ID   F102A_MOUSE             Reviewed;         392 AA.
AC   Q78T81; Q8K2K5;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Protein FAM102A;
GN   Name=Fam102a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-392.
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May play a role in estrogen action (By similarity).
CC   -!- SIMILARITY: Belongs to the FAM102 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH31157.1; Type=Erroneous initiation;
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DR   EMBL; AK049032; BAC33519.1; -; mRNA.
DR   EMBL; AK157331; BAE34050.1; -; mRNA.
DR   EMBL; AK157490; BAE34101.1; -; mRNA.
DR   EMBL; AK170536; BAE41864.1; -; mRNA.
DR   EMBL; AK170847; BAE42070.1; -; mRNA.
DR   EMBL; AK170951; BAE42135.1; -; mRNA.
DR   EMBL; AK172536; BAE43056.1; -; mRNA.
DR   EMBL; BC031157; AAH31157.1; ALT_INIT; mRNA.
DR   IPI; IPI00221437; -.
DR   RefSeq; NP_705788.1; NM_153560.4.
DR   UniGene; Mm.4065; -.
DR   UniGene; Mm.472003; -.
DR   ProteinModelPortal; Q78T81; -.
DR   PhosphoSite; Q78T81; -.
DR   PRIDE; Q78T81; -.
DR   Ensembl; ENSMUST00000048375; ENSMUSP00000044731; ENSMUSG00000039157.
DR   GeneID; 98952; -.
DR   KEGG; mmu:98952; -.
DR   UCSC; uc008jfs.1; mouse.
DR   CTD; 98952; -.
DR   MGI; MGI:2138935; Fam102a.
DR   GeneTree; ENSGT00390000011832; -.
DR   HOGENOM; HBG446042; -.
DR   HOVERGEN; HBG057729; -.
DR   InParanoid; Q78T81; -.
DR   OMA; FQTTFTL; -.
DR   OrthoDB; EOG4D52Z1; -.
DR   PhylomeDB; Q78T81; -.
DR   NextBio; 353719; -.
DR   ArrayExpress; Q78T81; -.
DR   Bgee; Q78T81; -.
DR   Genevestigator; Q78T81; -.
DR   GermOnline; ENSMUSG00000039157; Mus musculus.
DR   InterPro; IPR019448; Oestrogen-resp_Fam102A/B_N.
DR   Pfam; PF10358; Eeig1; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    392       Protein FAM102A.
FT                                /FTId=PRO_0000261635.
FT   COMPBIAS    157    273       Ser-rich.
FT   MOD_RES     252    252       Phosphoserine.
SQ   SEQUENCE   392 AA;  42830 MW;  F4DB10650412E91C CRC64;
     MAFLMKKKKF KFQTTFTLEE LTAVPFVNGV LFCKVRLLDG GDFVSLSSRE EVQENCVRWR
     KRFTFVCKMS ANPATGLLDP CIFRVSVRKE LKGGKAYSKL GFTDLNLAEF AGSGSTVRCC
     LLEGYDTKNT RQDNSILKVT IGMFLLSGDP CFKTPPSTAK SISIPGQDSS LQLTCKGGGT
     SSGGSSSTNS LTGSRPPKTR PTILGSGLPE EPDQSLSSPE EVFHSGHSRN SSYASQQSKL
     SGYSTEHSRS SSLSDLTHRR NTSTSSSASG GLSMAVEGPE GMEREHRPSE KPPRPPEKPP
     RPPRPLHLSD RSFRRKKDSV ESHPTWVDDT RIDADDIVEK IMQSQDFTDG SNTEDSNLRL
     FVSRDGSTTL SGIQLGNRVS SGVYEPVVIE SH
//
ID   NP1L4_MOUSE             Reviewed;         375 AA.
AC   Q78ZA7; O88701;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=Nucleosome assembly protein 1-like 4;
GN   Name=Nap1l4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=98282243; PubMed=9618174; DOI=10.1093/hmg/7.7.1149;
RA   Paulsen M., Davies K.R., Bowden L.M., Villar A.J., Franck O.,
RA   Fuermann M., Dean W.L., Moore T.F., Rodrigues N., Davies K.E.,
RA   Hu R.-J., Feinberg A.P., Maher E.R., Reik W., Walter J.;
RT   "Syntenic organization of the mouse distal chromosome 7 imprinting
RT   cluster and the Beckwith-Wiedemann syndrome region in chromosome
RT   11p15.5.";
RL   Hum. Mol. Genet. 7:1149-1159(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=20519229; PubMed=11063728; DOI=10.1093/hmg/9.18.2691;
RA   Engemann S., Stroedicke M., Paulsen M., Franck O., Reinhardt R.,
RA   Lane N., Reik W., Walter J.;
RT   "Sequence and functional comparison in the Beckwith-Wiedemann region:
RT   implications for a novel imprinting centre and extended imprinting.";
RL   Hum. Mol. Genet. 9:2691-2706(2000).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   POLYGLUTAMYLATION.
RC   STRAIN=C57BL/6; TISSUE=Testis;
RX   PubMed=17499049; DOI=10.1016/j.molcel.2007.04.012;
RA   van Dijk J., Rogowski K., Miro J., Lacroix B., Edde B., Janke C.;
RT   "A targeted multienzyme mechanism for selective microtubule
RT   polyglutamylation.";
RL   Mol. Cell 26:437-448(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND SER-125, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- PTM: Polyglutamylated and polyglycylated. These 2 modifications
CC       occur exclusively on glutamate residues and result in either
CC       polyglutamate or polyglycine chains on the gamma-carboxyl group.
CC       Both modifications can coexist on the same protein on adjacent
CC       residues, and lowering polyglycylation levels increases
CC       polyglutamylation, and reciprocally. Polyglutamylated by TTLL4.
CC   -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP)
CC       family.
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DR   EMBL; AJ002198; CAA05245.1; -; mRNA.
DR   EMBL; AJ276505; CAC16399.1; -; Genomic_DNA.
DR   IPI; IPI00876202; -.
DR   RefSeq; NP_032698.1; NM_008672.2.
DR   UniGene; Mm.294625; -.
DR   ProteinModelPortal; Q78ZA7; -.
DR   SMR; Q78ZA7; 41-344.
DR   IntAct; Q78ZA7; 1.
DR   STRING; Q78ZA7; -.
DR   PRIDE; Q78ZA7; -.
DR   Ensembl; ENSMUST00000072727; ENSMUSP00000072510; ENSMUSG00000059119.
DR   GeneID; 17955; -.
DR   KEGG; mmu:17955; -.
DR   UCSC; uc009kpk.1; mouse.
DR   CTD; 17955; -.
DR   MGI; MGI:1316687; Nap1l4.
DR   GeneTree; ENSGT00480000042668; -.
DR   HOVERGEN; HBG052653; -.
DR   NextBio; 292875; -.
DR   ArrayExpress; Q78ZA7; -.
DR   Bgee; Q78ZA7; -.
DR   CleanEx; MM_NAP1L4; -.
DR   Genevestigator; Q78ZA7; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   InterPro; IPR002164; NAP_family.
DR   PANTHER; PTHR11875; NAP_family; 1.
DR   Pfam; PF00956; NAP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Nucleus; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    375       Nucleosome assembly protein 1-like 4.
FT                                /FTId=PRO_0000236213.
FT   MOTIF       265    271       Nuclear localization signal (Potential).
FT   COMPBIAS    126    131       Poly-Glu.
FT   COMPBIAS    301    310       Asp/Glu-rich (acidic).
FT   COMPBIAS    347    370       Asp/Glu-rich (acidic).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       5      5       Phosphoserine (By similarity).
FT   MOD_RES       7      7       Phosphoserine (By similarity).
FT   MOD_RES      49     49       Phosphoserine.
FT   MOD_RES      51     51       Phosphothreonine (By similarity).
FT   MOD_RES      53     53       Phosphoserine (By similarity).
FT   MOD_RES     125    125       Phosphoserine.
FT   MOD_RES     304    304       Phosphoserine (By similarity).
SQ   SEQUENCE   375 AA;  42679 MW;  A249E440F09072A6 CRC64;
     MAENSLSDGG PADSVEAAKN ASNTEKLTDQ VMQNPQVLAA LQERLDNVSH TPSSYIETLP
     KAVKRRINAL KQLQVRCAHI EAKFYEEVHD LERKYAALYQ PLFDKRREFI TGDVEPTDAE
     SAWHSENEEE DKLAGDMKNK VVIAEKEAAT VEELNPKGIP EFWFTIFRNV DMLSELVQEY
     DEPILKHLQD IKVKFSDPGQ PMSFVLEFHF EPNDYFTNPV LTKTYKMKSE PDKADPFSFE
     GPEIVDCDGC TIDWKKGKNV TVKTIKKKQK HKGRGTVRTI TKQVPNESFF NFFSPLKASG
     DGESLDEDSE FTLASDFEIG HFFRERIVPR AVLYFTGEAI EDDDNFEEGE EGEEEELEGD
     EEGEDEDDAD VNPKV
//
ID   MTCH1_MOUSE             Reviewed;         389 AA.
AC   Q791T5; Q3U4W7; Q791V6; Q8R0T0; Q8R1T8; Q8R2T2; Q9QZA5; Q9QZP4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Mitochondrial carrier homolog 1;
DE   AltName: Full=Mitochondrial carrier-like protein 1;
GN   Name=Mtch1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RA   Jang J.S., Hahn Y., Park C., Chung J.H.;
RT   "Evolutionarily conserved mitochondrial carrier gene family in mouse,
RT   human, and zebrafish.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RA   Brathwaite M.E., Waeltz P., Qian Y., Dudekula D., Schlessinger D.,
RA   Nagaraja R.;
RT   "Genomic sequence analysis in the mouse T-complex region.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-389 (ISOFORM 2).
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-389 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-389 (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Kidney, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Potential mitochondrial transporter. May play a role in
CC       apoptosis (By similarity).
CC   -!- SUBUNIT: Interacts with PSEN1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC       membrane protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q791T5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q791T5-2; Sequence=VSP_017883;
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier family.
CC   -!- SIMILARITY: Contains 2 Solcar repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH23135.1; Type=Erroneous initiation;
CC       Sequence=AAH26436.1; Type=Erroneous initiation;
CC       Sequence=AAH27274.1; Type=Erroneous initiation;
CC       Sequence=BAE32313.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB040292; BAA92860.1; -; Genomic_DNA.
DR   EMBL; AB040292; BAA92861.1; -; Genomic_DNA.
DR   EMBL; AF176007; AAD52645.2; -; mRNA.
DR   EMBL; AF192558; AAF12792.2; -; mRNA.
DR   EMBL; AY301264; AAP45196.1; -; Genomic_DNA.
DR   EMBL; AY301264; AAP45202.1; -; Genomic_DNA.
DR   EMBL; AK154010; BAE32313.1; ALT_INIT; mRNA.
DR   EMBL; BC023135; AAH23135.1; ALT_INIT; mRNA.
DR   EMBL; BC026436; AAH26436.1; ALT_INIT; mRNA.
DR   EMBL; BC027274; AAH27274.1; ALT_INIT; mRNA.
DR   IPI; IPI00137173; -.
DR   IPI; IPI00742287; -.
DR   RefSeq; NP_063933.1; NM_019880.3.
DR   UniGene; Mm.285322; -.
DR   ProteinModelPortal; Q791T5; -.
DR   STRING; Q791T5; -.
DR   PhosphoSite; Q791T5; -.
DR   PRIDE; Q791T5; -.
DR   Ensembl; ENSMUST00000095427; ENSMUSP00000093077; ENSMUSG00000024012.
DR   GeneID; 56462; -.
DR   KEGG; mmu:56462; -.
DR   UCSC; uc008bst.1; mouse.
DR   UCSC; uc008bsu.1; mouse.
DR   CTD; 56462; -.
DR   MGI; MGI:1929261; Mtch1.
DR   eggNOG; roNOG16091; -.
DR   GeneTree; ENSGT00390000000020; -.
DR   HOVERGEN; HBG058632; -.
DR   InParanoid; Q791T5; -.
DR   OMA; TYARHIV; -.
DR   OrthoDB; EOG44BB2J; -.
DR   NextBio; 312714; -.
DR   ArrayExpress; Q791T5; -.
DR   Bgee; Q791T5; -.
DR   CleanEx; MM_MTCH1; -.
DR   Genevestigator; Q791T5; -.
DR   GermOnline; ENSMUSG00000024012; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0006919; P:activation of caspase activity; ISS:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptosis; ISS:UniProtKB.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   Pfam; PF00153; Mito_carr; 1.
DR   PROSITE; PS50920; SOLCAR; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Phosphoprotein; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    389       Mitochondrial carrier homolog 1.
FT                                /FTId=PRO_0000232386.
FT   TRANSMEM    248    268       Helical; (Potential).
FT   TRANSMEM    315    335       Helical; (Potential).
FT   REPEAT       81    176       Solcar 1.
FT   REPEAT      192    280       Solcar 2.
FT   MOD_RES     381    381       Phosphoserine.
FT   VAR_SEQ     286    302       Missing (in isoform 2).
FT                                /FTId=VSP_017883.
FT   CONFLICT     10     10       P -> A (in Ref. 3; BAE32313).
FT   CONFLICT     46     46       A -> G (in Ref. 3; BAE32313).
SQ   SEQUENCE   389 AA;  41565 MW;  CCD3B23B6DF3CB02 CRC64;
     MGASDPEVAP WAPGGAAGMA GAGAGAGARG GAPAGVEARA RDPPPAHRAH PRHPRPAAQP
     SARRMDGGPG APGSGDNAPT TEALFVALGA GVTALSHPLL YVKLLIQVGH EPMPPTLGTN
     VLGRKVLYLP SFFTYAKYIV QVDGKIGLFR GLSPRLMSNA LSTVTRGSMK KVFPPDEMEQ
     VSNKDDMKTS LKKVVKETSY EMMMQCVSRM LAHPLHVISM RCMVQFVGRE AKYSGVLSSI
     GKIFKEEGLL GFFVGLIPHL LGDVVFLWGC NLLAHFINAY LVDDSVSDTP GGLGNDQNPG
     SQFSQALAIR SYTKFVMGIA VSMLTYPFLL VGDLMAVNNC GLRAGLPPYS PVFKSWIHCW
     KYLSVQGQLF RGSSLLFRRV SSGSCFALE
//
ID   MTCH2_MOUSE             Reviewed;         303 AA.
AC   Q791V5; Q3TPS5; Q99LZ6; Q9D060; Q9D7Y2; Q9QZP3;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Mitochondrial carrier homolog 2;
GN   Name=Mtch2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Jang J.S., Hahn Y., Park C., Chung J.H.;
RT   "Identification of an evolutionary conserved mitochondrial carrier
RT   family from various organisms.";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Heart, Hippocampus, Small intestine, Stomach, Testis, and
RC   Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 69-77; 91-119 AND 172-185, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-158, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- FUNCTION: The substrate transported is not yet known. Induces
CC       mitochondrial depolarization (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC       membrane protein (Potential).
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier family.
CC   -!- SIMILARITY: Contains 2 Solcar repeats.
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DR   EMBL; AF176009; AAD52647.1; -; mRNA.
DR   EMBL; AK003100; BAB22565.1; -; mRNA.
DR   EMBL; AK008487; BAB25694.1; -; mRNA.
DR   EMBL; AK008712; BAB25848.1; -; mRNA.
DR   EMBL; AK011785; BAB27839.1; -; mRNA.
DR   EMBL; AK011874; BAB27892.1; -; mRNA.
DR   EMBL; AK075890; BAC36033.1; -; mRNA.
DR   EMBL; AK161441; BAE36399.1; -; mRNA.
DR   EMBL; AK164169; BAE37660.1; -; mRNA.
DR   EMBL; BC002152; AAH02152.1; -; mRNA.
DR   EMBL; BC038899; AAH38899.1; -; mRNA.
DR   EMBL; BC038916; AAH38916.1; -; mRNA.
DR   IPI; IPI00132039; -.
DR   RefSeq; NP_062732.1; NM_019758.2.
DR   UniGene; Mm.28023; -.
DR   ProteinModelPortal; Q791V5; -.
DR   STRING; Q791V5; -.
DR   PhosphoSite; Q791V5; -.
DR   PRIDE; Q791V5; -.
DR   Ensembl; ENSMUST00000136872; ENSMUSP00000121851; ENSMUSG00000027282.
DR   GeneID; 56428; -.
DR   KEGG; mmu:56428; -.
DR   UCSC; uc008ktn.1; mouse.
DR   CTD; 56428; -.
DR   MGI; MGI:1929260; Mtch2.
DR   GeneTree; ENSGT00390000000020; -.
DR   HOVERGEN; HBG058632; -.
DR   OrthoDB; EOG4J9N0H; -.
DR   PhylomeDB; Q791V5; -.
DR   NextBio; 312594; -.
DR   ArrayExpress; Q791V5; -.
DR   Bgee; Q791V5; -.
DR   CleanEx; MM_MTCH2; -.
DR   Genevestigator; Q791V5; -.
DR   GermOnline; ENSMUSG00000027282; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   Pfam; PF00153; Mito_carr; 1.
DR   PROSITE; PS50920; SOLCAR; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    303       Mitochondrial carrier homolog 2.
FT                                /FTId=PRO_0000090638.
FT   TRANSMEM      8     28       Helical; (Potential).
FT   TRANSMEM    175    195       Helical; (Potential).
FT   TRANSMEM    224    244       Helical; (Potential).
FT   REPEAT        2     98       Solcar 1.
FT   REPEAT      118    206       Solcar 2.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     158    158       N6-acetyllysine.
FT   CONFLICT    206    206       Y -> C (in Ref. 2; BAB27839).
FT   CONFLICT    207    207       A -> T (in Ref. 2; BAB25848).
SQ   SEQUENCE   303 AA;  33499 MW;  248F8A1E4CF29975 CRC64;
     MADAASQVLL GSGLTILSQP LMYVKVLIQV GYEPLPPTIG RNIFGRQVCQ LPGLFCYAQH
     IASIDGRRGL FTGLTPRLCS GVLGTVVHGK VLQYYQESEK PEELGSVTVQ KEYSSSFDRV
     IKETTREMIA RSAATLITHP FHVITLRSMV QFIGRESKYC GLCDSIVTIY REEGIVGFFA
     GLIPRLLGDI ISLWLCNSLA YLINTYALDS GVSTMNEMKS YSQAVTGFFA SMLTYPFVLV
     SNLMAVNNCG LAGGSPPYSP IYTSWIDCWC MLQKAGNMSR GNSLFFRKVP CGKTYCYDLR
     MLI
//
ID   PICA_MOUSE              Reviewed;         660 AA.
AC   Q7M6Y3; Q3TS04; Q811P1; Q8BUF6; Q8CIH8; Q8R0A9; Q8R3E1; Q8VDN5;
AC   Q921L0;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Phosphatidylinositol-binding clathrin assembly protein;
DE   AltName: Full=Clathrin assembly lymphoid myeloid leukemia;
DE            Short=CALM;
GN   Name=Picalm; Synonyms=Calm, Fit1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=BALB/cRl; TISSUE=Liver;
RX   MEDLINE=22735908; PubMed=12832620; DOI=10.1073/pnas.1432634100;
RA   Klebig M.L., Wall M.D., Potter M.D., Rowe E.L., Carpenter D.A.,
RA   Rinchik E.M.;
RT   "Mutations in the clathrin-assembly gene Picalm are responsible for
RT   the hematopoietic and iron metabolism abnormalities in fit1 mice.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:8360-8365(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4; 5 AND 6).
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 143-660 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Epididymis, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   FUNCTION.
RX   PubMed=9292517;
RA   Potter M.D., Shinpock S.G., Popp R.A., Godfrey V., Carpenter D.A.,
RA   Bernstein A., Johnson D.K., Rinchik E.M.;
RT   "Mutations in the murine fitness 1 gene result in defective
RT   hematopoiesis.";
RL   Blood 90:1850-1857(1997).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Assembly protein recruiting clathrin and adaptor protein
CC       complex 2 (AP2) to cell membranes at sites of coated-pit formation
CC       and clathrin-vesicle assembly. May be required to determine the
CC       amount of membrane to be recycled, possibly by regulating the size
CC       of the clathrin cage. Involved in AP2-dependent clathrin-mediated
CC       endocytosis at the neuromuscular junction. Plays a crucial role in
CC       fetal and adult hematopoiesis, and normal prenatal and postnatal
CC       growth and viability.
CC   -!- SUBUNIT: Binds clathrin and phosphatidylinositol-4,5-bisphosphate
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit (By
CC       similarity). Golgi apparatus (By similarity). Cytoplasmic vesicle,
CC       clathrin-coated vesicle (By similarity). Note=Colocalized with
CC       clathrin in the Golgi area (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q7M6Y3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7M6Y3-2; Sequence=VSP_050684, VSP_050685, VSP_050686;
CC       Name=3;
CC         IsoId=Q7M6Y3-3; Sequence=VSP_050684, VSP_050685;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q7M6Y3-4; Sequence=VSP_050684;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q7M6Y3-5; Sequence=VSP_050685;
CC       Name=6;
CC         IsoId=Q7M6Y3-6; Sequence=VSP_050686;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Skins and livers of 1-week-old mice.
CC   -!- SIMILARITY: Contains 1 ENTH (epsin N-terminal homology) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC39454.2; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY206701; AAO17153.1; -; mRNA.
DR   EMBL; BK001028; DAA01470.1; -; mRNA.
DR   EMBL; BC011470; AAH11470.1; -; mRNA.
DR   EMBL; BC021491; AAH21491.1; -; mRNA.
DR   EMBL; BC023843; AAH23843.1; -; mRNA.
DR   EMBL; BC025566; AAH25566.1; -; mRNA.
DR   EMBL; BC027116; AAH27116.1; -; mRNA.
DR   EMBL; BC057683; AAH57683.1; -; mRNA.
DR   EMBL; AK085472; BAC39454.2; ALT_INIT; mRNA.
DR   EMBL; AK162360; BAE36872.1; -; mRNA.
DR   IPI; IPI00264501; -.
DR   IPI; IPI00321378; -.
DR   IPI; IPI00404434; -.
DR   IPI; IPI00404435; -.
DR   IPI; IPI00404436; -.
DR   IPI; IPI00404438; -.
DR   RefSeq; NP_666306.2; NM_146194.3.
DR   UniGene; Mm.235175; -.
DR   UniGene; Mm.393563; -.
DR   ProteinModelPortal; Q7M6Y3; -.
DR   SMR; Q7M6Y3; 19-281.
DR   STRING; Q7M6Y3; -.
DR   PhosphoSite; Q7M6Y3; -.
DR   PRIDE; Q7M6Y3; -.
DR   Ensembl; ENSMUST00000049537; ENSMUSP00000051092; ENSMUSG00000039361.
DR   Ensembl; ENSMUST00000107223; ENSMUSP00000102841; ENSMUSG00000039361.
DR   Ensembl; ENSMUST00000107224; ENSMUSP00000102843; ENSMUSG00000039361.
DR   GeneID; 233489; -.
DR   KEGG; mmu:233489; -.
DR   UCSC; uc009igq.1; mouse.
DR   UCSC; uc009igr.1; mouse.
DR   UCSC; uc009igs.1; mouse.
DR   UCSC; uc009igt.1; mouse.
DR   UCSC; uc009igu.1; mouse.
DR   UCSC; uc009igv.1; mouse.
DR   CTD; 233489; -.
DR   MGI; MGI:2385902; Picalm.
DR   eggNOG; roNOG11951; -.
DR   GeneTree; ENSGT00390000008805; -.
DR   HOVERGEN; HBG049391; -.
DR   InParanoid; Q7M6Y3; -.
DR   OrthoDB; EOG4C87RV; -.
DR   PhylomeDB; Q7M6Y3; -.
DR   NextBio; 381725; -.
DR   ArrayExpress; Q7M6Y3; -.
DR   Bgee; Q7M6Y3; -.
DR   Genevestigator; Q7M6Y3; -.
DR   GO; GO:0030118; C:clathrin coat; IEA:InterPro.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005905; C:coated pit; IDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030276; F:clathrin binding; ISS:UniProtKB.
DR   GO; GO:0005545; F:1-phosphatidylinositol binding; ISS:UniProtKB.
DR   GO; GO:0007409; P:axonogenesis; IMP:BHF-UCL.
DR   GO; GO:0048268; P:clathrin coat assembly; IEA:InterPro.
DR   GO; GO:0048813; P:dendrite morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0030097; P:hemopoiesis; IMP:UniProtKB.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB.
DR   InterPro; IPR011417; ANTH.
DR   InterPro; IPR014712; Clathrin_Pinositid-bd_GAT-like.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR013809; Epsin-like_N.
DR   Gene3D; G3DSA:1.25.40.90; ENTH_VHS; 1.
DR   Gene3D; G3DSA:1.20.58.150; Pinositid-bd_clathrin_GAT-like; 1.
DR   Pfam; PF07651; ANTH; 1.
DR   SMART; SM00273; ENTH; 1.
DR   SUPFAM; SSF48464; ENTH_VHS; 1.
DR   PROSITE; PS50942; ENTH; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coated pit; Cytoplasmic vesicle;
KW   Developmental protein; Endocytosis; Golgi apparatus; Membrane;
KW   Phosphoprotein.
FT   CHAIN         1    660       Phosphatidylinositol-binding clathrin
FT                                assembly protein.
FT                                /FTId=PRO_0000187063.
FT   DOMAIN       14    145       ENTH.
FT   MOD_RES     443    443       Phosphoserine.
FT   VAR_SEQ     420    469       Missing (in isoform 2, isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_050684.
FT   VAR_SEQ     506    510       Missing (in isoform 2, isoform 3 and
FT                                isoform 5).
FT                                /FTId=VSP_050685.
FT   VAR_SEQ     594    601       Missing (in isoform 2 and isoform 6).
FT                                /FTId=VSP_050686.
FT   CONFLICT    522    522       N -> S (in Ref. 2; AAH21491/AAH23843/
FT                                AAH25566/AAH57683).
SQ   SEQUENCE   660 AA;  71543 MW;  7FB206508281BCDF CRC64;
     MSGQSLTDRI TAAQHSVTGS AVSKTVCKAT THEIMGPKKK HLDYLIQCTN EMNVNIPQLA
     DSLFERTTNS SWVVVFKSLI TTHHLMVYGN ERFIQYLASR NTLFNLSNFL DKSGLQGYDM
     STFIRRYSRY LNEKAVSYRQ VAFDFTKVKR GADGVMRTMN TEKLLKTVPI IQNQMDALLD
     FNVNSNELTN GVINAAFMLL FKDAIRLFAA YNEGIINLLE KYFDMKKNQC KEGLDIYKKF
     LTRMTRISEF LKVAEQVGID RGDIPDLSQA PSSLLDALEQ HLASLEGKKI KDSTAASRAT
     TLSNAVSSLA STGLSLTKVD EREKQAALEE EQARLKALKE QRLKELAKKP HTSLTTAASP
     VSTSAGGIMT APAIDIFSTP SSSNSTSKLP NDLLDLQQPT FHPSVHAMSA APQGASTWGD
     PFSATLDAVE DAIPSLNPFL TKSSGDVHLP IASDVSTFTT RTPTHEMFVG FSPSPVAQPH
     SSAGLNVDFE SVFGNKSTNV AVDSGGFDEL GGLLKPTVAS QNQSLPVAKL PPNKLVSDDL
     DSSLANLVGN LGIGNGTTKN DVSWSQPGEK KLTGGSNWQP KVAPTTAWSA ATMNGMHFPQ
     YAPPVMAYPA TTPTGMIGYG IPPQMGSVPV MTQPTLIYSQ PVMRPPNPFG PVSGAQIQFM
//
ID   OPALI_MOUSE             Reviewed;         143 AA.
AC   Q7M750; Q6P903;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   08-MAR-2011, entry version 47.
DE   RecName: Full=Opalin;
DE   AltName: Full=Oligodendrocytic myelin paranodal and inner loop protein;
DE   AltName: Full=Transmembrane protein 10;
GN   Name=Opalin; Synonyms=Tmem10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   IDENTIFICATION.
RX   MEDLINE=21673991; PubMed=11814680; DOI=10.1016/S0378-1119(01)00846-0;
RA   Nobile C., Hinzmann B., Scannapieco P., Siebert R., Zimbello R.,
RA   Perez-Tur J., Sarafidou T., Moschonas N.K., French L., Deloukas P.,
RA   Ciccodicola A., Gesk S., Poza J.J., Lo Nigro C., Seri M.,
RA   Schlegelberger B., Rosenthal A., Valle G., Lopez de Munain A.,
RA   Tassinari C.A., Michelucci R.;
RT   "Identification and characterization of a novel human brain-specific
RT   gene, homologous to S. scrofa tmp83.5, in the chromosome 10q24
RT   critical region for temporal lobe epilepsy and spastic paraplegia.";
RL   Gene 282:87-94(2002).
RN   [3]
RP   FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=17442045; DOI=10.1111/j.1471-4159.2007.04583.x;
RA   Aruga J., Yoshikawa F., Nozaki Y., Sakaki Y., Toyoda A., Furuichi T.;
RT   "An oligodendrocyte enhancer in a phylogenetically conserved intron
RT   region of the mammalian myelin gene Opalin.";
RL   J. Neurochem. 102:1533-1547(2007).
RN   [4]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=18439243; DOI=10.1186/1471-2202-9-40;
RA   Kippert A., Trajkovic K., Fitzner D., Opitz L., Simons M.;
RT   "Identification of Tmem10/Opalin as a novel marker for
RT   oligodendrocytes using gene expression profiling.";
RL   BMC Neurosci. 9:40-40(2008).
RN   [5]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   GLYCOSYLATION AT ASN-6; ASN-12 AND THR-14, AND MUTAGENESIS OF ASN-6;
RP   ASN-12 AND THR-14.
RX   PubMed=18490449; DOI=10.1074/jbc.M801314200;
RA   Yoshikawa F., Sato Y., Tohyama K., Akagi T., Hashikawa T.,
RA   Nagakura-Takagi Y., Sekine Y., Morita N., Baba H., Suzuki Y.,
RA   Sugano S., Sato A., Furuichi T.;
RT   "Opalin, a transmembrane sialylglycoprotein located in the central
RT   nervous system myelin paranodal loop membrane.";
RL   J. Biol. Chem. 283:20830-20840(2008).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Note=In the CNS, enriched in the myelin paranodal and
CC       inner loop membranes, but not that of the PNS.
CC   -!- TISSUE SPECIFICITY: Expressed specifically in oligodendrocytes of
CC       the brain.
CC   -!- DEVELOPMENTAL STAGE: Expression in the cerebellum increases
CC       dramatically after the first postnatal week. Selectively expressed
CC       in brain at P21, and not expressed in any other tissues tested
CC       including thymus, lung, heart, liver, spleen, kidney and testis.
CC   -!- INDUCTION: By leukemia inhibitory factor (LIF) and cAMP analogs.
CC       Suppressed in the presence of astrocytic or neural-stem-like
CC       differentiation factors such as bone morphotic protein (BMP) and
CC       fetal calf serum.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC060980; AAH60980.1; -; mRNA.
DR   EMBL; BK000002; DAA00020.1; -; mRNA.
DR   IPI; IPI00460127; -.
DR   RefSeq; NP_705740.1; NM_153520.1.
DR   UniGene; Mm.54119; -.
DR   PRIDE; Q7M750; -.
DR   Ensembl; ENSMUST00000087176; ENSMUSP00000084422; ENSMUSG00000050121.
DR   GeneID; 226115; -.
DR   KEGG; mmu:226115; -.
DR   NMPDR; fig|10090.3.peg.5060; -.
DR   UCSC; uc008hlq.1; mouse.
DR   CTD; 226115; -.
DR   MGI; MGI:2657025; Opalin.
DR   GeneTree; ENSGT00390000009395; -.
DR   HOGENOM; HBG282666; -.
DR   HOVERGEN; HBG054559; -.
DR   InParanoid; Q7M750; -.
DR   OMA; WWLIPRL; -.
DR   OrthoDB; EOG418BPX; -.
DR   NextBio; 377998; -.
DR   ArrayExpress; Q7M750; -.
DR   Bgee; Q7M750; -.
DR   Genevestigator; Q7M750; -.
DR   GermOnline; ENSMUSG00000050121; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    143       Opalin.
FT                                /FTId=PRO_0000072592.
FT   TRANSMEM     31     51       Helical; (Potential).
FT   CARBOHYD      6      6       N-linked (GlcNAc...).
FT   CARBOHYD     12     12       N-linked (GlcNAc...).
FT   CARBOHYD     14     14       O-linked (GalNAc...).
FT   MUTAGEN       6      6       N->Q: Impairs cell surface expression.
FT   MUTAGEN      12     12       N->Q: Impairs cell surface expression.
FT   MUTAGEN      14     14       T->A: Impairs cell surface expression.
FT   CONFLICT    133    133       L -> F (in Ref. 1; AAH60980).
SQ   SEQUENCE   143 AA;  15833 MW;  A5DF69DB05C72B41 CRC64;
     MSFSLNFTLP SNTTSSPVVT SAKATDCGPS IGLAAGIPSL LATALLVALL FTLIQRRRTI
     DDEPVEETEI PCEISELYDN PKISENPRRS PTHEMNPRGS QEGHIYVKTV SGSEEPLPDT
     YRPPEELERR RGLWWLVPSL SLE
//
ID   F108B_MOUSE             Reviewed;         288 AA.
AC   Q7M759; Q58EV9; Q8K275;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Abhydrolase domain-containing protein FAM108B1;
DE            EC=3.-.-.-;
DE   Flags: Precursor;
GN   Name=Fam108b1; Synonyms=Fam108b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 106-288.
RC   STRAIN=Czech II, and FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=22722134; PubMed=12838346; DOI=10.1038/nrg1111;
RA   Puente X.S., Sanchez L.M., Overall C.M., Lopez-Otin C.;
RT   "Human and mouse proteases: a comparative genomic approach.";
RL   Nat. Rev. Genet. 4:544-558(2003).
CC   -!- SUBCELLULAR LOCATION: Secreted (Potential).
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. FAM108
CC       family.
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DR   EMBL; AK152807; BAE31512.1; -; mRNA.
DR   EMBL; AC133649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC032261; AAH32261.1; -; mRNA.
DR   EMBL; BC091733; AAH91733.1; -; mRNA.
DR   EMBL; BN000127; CAD67578.1; -; mRNA.
DR   IPI; IPI00108883; -.
DR   RefSeq; NP_666208.2; NM_146096.3.
DR   UniGene; Mm.28796; -.
DR   ProteinModelPortal; Q7M759; -.
DR   SMR; Q7M759; 88-193.
DR   MEROPS; S09.055; -.
DR   PhosphoSite; Q7M759; -.
DR   PRIDE; Q7M759; -.
DR   Ensembl; ENSMUST00000052556; ENSMUSP00000056099; ENSMUSG00000047368.
DR   GeneID; 226016; -.
DR   KEGG; mmu:226016; -.
DR   UCSC; uc008gzb.1; mouse.
DR   CTD; 226016; -.
DR   MGI; MGI:1917816; Fam108b.
DR   eggNOG; roNOG09827; -.
DR   GeneTree; ENSGT00390000000948; -.
DR   HOGENOM; HBG678036; -.
DR   HOVERGEN; HBG061270; -.
DR   InParanoid; Q7M759; -.
DR   OMA; FVAHELV; -.
DR   OrthoDB; EOG46MBK6; -.
DR   PhylomeDB; Q7M759; -.
DR   NextBio; 377917; -.
DR   ArrayExpress; Q7M759; -.
DR   Bgee; Q7M759; -.
DR   Genevestigator; Q7M759; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR001375; Peptidase_S9.
DR   Pfam; PF00326; Peptidase_S9; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Secreted; Signal.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21    288       Abhydrolase domain-containing protein
FT                                FAM108B1.
FT                                /FTId=PRO_0000281112.
FT   ACT_SITE    170    170       Charge relay system (By similarity).
FT   ACT_SITE    235    235       Charge relay system (By similarity).
FT   ACT_SITE    264    264       Charge relay system (By similarity).
SQ   SEQUENCE   288 AA;  32201 MW;  4A797F710C99EC72 CRC64;
     MNNLSFSELC CLFCCPPCPG KIASKLAFLP PDPTYTLMCD ESGSRWTLHL SERADWQYSS
     REKDAIECFM TRTSKGNRIA CMFVRCSPNA KYTLLFSHGN AVDLGQMSSF YIGLGSRINC
     NIFSYDYSGY GASSGKPTEK NLYADVEAAW LALRTRYGIR PENVIIYGQS IGTVPSVDLA
     ARYESAAVIL HSPLTSGMRV AFPDTKKTYC FDAFPNIDKI SKITSPVLII HGTEDEVIDF
     SHGLALFERC QRPVEPLWVE GAGHNDVELY GQYLERLKQF VSQELVNL
//
ID   ASAP2_MOUSE             Reviewed;         958 AA.
AC   Q7SIG6; Q501K1; Q66JN2;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 3.
DT   08-FEB-2011, entry version 84.
DE   RecName: Full=Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2;
DE   AltName: Full=Development and differentiation-enhancing factor 2;
DE   AltName: Full=Paxillin-associated protein with ARF GAP activity 3;
DE            Short=PAG3;
DE   AltName: Full=Pyk2 C-terminus-associated protein;
DE            Short=PAP;
GN   Name=Asap2; Synonyms=Ddef2, Gm1523, Gm592;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 425-432, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [3]
RP   FUNCTION, PHOSPHORYLATION, INTERACTION WITH PTK2B AND SRC, AND
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=99147068; PubMed=10022920;
RA   Andreev J., Simon J.-P., Sabatini D.D., Kam J., Plowman G.,
RA   Randazzo P.A., Schlessinger J.;
RT   "Identification of a new Pyk2 target protein with Arf-GAP activity.";
RL   Mol. Cell. Biol. 19:2338-2350(1999).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ARF6 AND ACTIN
RP   FILAMENTS.
RX   MEDLINE=21201228; PubMed=11304556; DOI=10.1084/jem.193.8.955;
RA   Uchida H., Kondo A., Yoshimura Y., Mazaki Y., Sabe H.;
RT   "PAG3/Papalpha/KIAA0400, a GTPase-activating protein for ADP-
RT   ribosylation factor (ARF), regulates ARF6 in Fcgamma receptor-mediated
RT   phagocytosis of macrophages.";
RL   J. Exp. Med. 193:955-966(2001).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-704, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 421-679 IN COMPLEX WITH A
RP   ZINC ION, AND MUTAGENESIS OF TRP-449; ILE-460; ARG-467; LEU-481 AND
RP   ASP-482.
RX   MEDLINE=20069319; PubMed=10601011; DOI=10.1093/emboj/18.24.6890;
RA   Mandiyan V., Andreev J., Schlessinger J., Hubbard S.R.;
RT   "Crystal structure of the ARF-GAP domain and ankyrin repeats of PYK2-
RT   associated protein beta.";
RL   EMBO J. 18:6890-6898(1999).
CC   -!- FUNCTION: Activates the small GTPases ARF1, ARF5 and ARF6.
CC       Regulates the formation of post-Golgi vesicles and modulates
CC       constitutive secretion. Modulates phagocytosis mediated by Fc
CC       gamma receptor and ARF6. Modulates PXN recruitment to focal
CC       contacts and cell migration (By similarity).
CC   -!- SUBUNIT: Binds PXN, ARF1, ARF5, ARF6, PTK2B and SRC.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, Golgi stack
CC       membrane; Peripheral membrane protein. Cell membrane; Peripheral
CC       membrane protein. Note=Colocalizes with F-actin and ARF6 in
CC       phagocytic cups.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7SIG6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7SIG6-2; Sequence=VSP_014776, VSP_014777;
CC   -!- DOMAIN: The conserved Arg-467 in the Arf-GAP domain probably
CC       becomes part of the active site of bound small GTPases and is
CC       necessary for GTP hydrolysis.
CC   -!- PTM: Phosphorylated on tyrosine residues by SRC and PTK2B (By
CC       similarity).
CC   -!- SIMILARITY: Contains 2 ANK repeats.
CC   -!- SIMILARITY: Contains 1 Arf-GAP domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; BC096022; AAH96022.1; -; mRNA.
DR   EMBL; BC080847; AAH80847.1; -; mRNA.
DR   IPI; IPI00355808; -.
DR   IPI; IPI00462750; -.
DR   RefSeq; NP_001004364.2; NM_001004364.2.
DR   RefSeq; NP_001091637.1; NM_001098168.1.
DR   RefSeq; NP_001128664.1; NM_001135192.1.
DR   UniGene; Mm.358946; -.
DR   PDB; 1DCQ; X-ray; 2.10 A; A=421-697.
DR   PDBsum; 1DCQ; -.
DR   ProteinModelPortal; Q7SIG6; -.
DR   SMR; Q7SIG6; 310-409, 422-697, 891-958.
DR   STRING; Q7SIG6; -.
DR   PhosphoSite; Q7SIG6; -.
DR   PRIDE; Q7SIG6; -.
DR   Ensembl; ENSMUST00000090834; ENSMUSP00000088344; ENSMUSG00000052632.
DR   Ensembl; ENSMUST00000101562; ENSMUSP00000099098; ENSMUSG00000052632.
DR   GeneID; 211914; -.
DR   KEGG; mmu:211914; -.
DR   UCSC; uc007ndi.1; mouse.
DR   CTD; 211914; -.
DR   MGI; MGI:2685438; Asap2.
DR   GeneTree; ENSGT00600000084109; -.
DR   HOVERGEN; HBG051327; -.
DR   NextBio; 373381; -.
DR   ArrayExpress; Q7SIG6; -.
DR   Bgee; Q7SIG6; -.
DR   Genevestigator; Q7SIG6; -.
DR   GermOnline; ENSMUSG00000052632; Mus musculus.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR001164; ArfGAP.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF57863; ArfGAP; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ANK repeat; Cell membrane;
KW   Coiled coil; Cytoplasm; Direct protein sequencing; Golgi apparatus;
KW   GTPase activation; Membrane; Metal-binding; Phosphoprotein; Repeat;
KW   SH3 domain; Zinc.
FT   CHAIN         1    958       Arf-GAP with SH3 domain, ANK repeat and
FT                                PH domain-containing protein 2.
FT                                /FTId=PRO_0000074199.
FT   DOMAIN      308    400       PH.
FT   DOMAIN      424    546       Arf-GAP.
FT   REPEAT      587    619       ANK 1.
FT   REPEAT      623    655       ANK 2.
FT   DOMAIN      896    958       SH3.
FT   COILED      259    286       Potential.
FT   COMPBIAS    774    888       Pro-rich.
FT   MOD_RES     704    704       Phosphoserine.
FT   VAR_SEQ     284    286       Missing (in isoform 2).
FT                                /FTId=VSP_014776.
FT   VAR_SEQ     345    490       Missing (in isoform 2).
FT                                /FTId=VSP_014777.
FT   MUTAGEN     449    449       W->A: Strongly reduces Arf-GAP mediated
FT                                stimulation of GTP hydrolysis.
FT   MUTAGEN     460    460       I->A: Reduces Arf-GAP mediated
FT                                stimulation of GTP hydrolysis 100-fold
FT                                and abolishes Arf-GAP mediated
FT                                stimulation of GTP hydrolysis; when
FT                                associated with A-306.
FT   MUTAGEN     467    467       R->A: Abolishes Arf-GAP mediated
FT                                stimulation of GTP hydrolysis.
FT   MUTAGEN     467    467       R->K: Reduces Arf-GAP mediated
FT                                stimulation of GTP hydrolysis more than
FT                                10000-fold.
FT   MUTAGEN     481    481       L->A: Reduces Arf-GAP mediated
FT                                stimulation of GTP hydrolysis 100-fold
FT                                and abolishes Arf-GAP mediated
FT                                stimulation of GTP hydrolysis; when
FT                                associated with A-285.
FT   MUTAGEN     482    482       D->A: Reduces Arf-GAP mediated
FT                                stimulation of GTP hydrolysis 1000-fold.
FT   HELIX       423    432
FT   TURN        434    437
FT   TURN        440    442
FT   STRAND      449    451
FT   TURN        452    454
FT   HELIX       460    469
FT   TURN        471    473
FT   STRAND      476    478
FT   TURN        479    481
FT   HELIX       486    489
FT   HELIX       490    494
FT   HELIX       497    504
FT   TURN        505    507
FT   STRAND      510    512
FT   HELIX       522    533
FT   STRAND      543    545
FT   HELIX       546    558
FT   HELIX       562    570
FT   HELIX       591    598
FT   TURN        601    603
FT   HELIX       604    613
FT   HELIX       627    633
FT   HELIX       637    645
FT   HELIX       660    666
FT   HELIX       670    680
SQ   SEQUENCE   958 AA;  106805 MW;  2CA0056C2AD14D7E CRC64;
     MPDQISVSEF VAETHEDYKA PTASSFTTRT AQCRNTVAAI EEALDVDRMV LYKMKKSVKA
     INISGLAHVE NEEQYTQALE KFGGNCVCRD DPDLGSAFLK FSVFTKELTA LFKNLIQNMN
     NIISFPLDSL LKGDLKGVKG DLKKPFDKAW KDYETKITKI EKEKKEHAKL HGMIRTEISG
     AEIAEEMEKE RRFFQLQMCE YLLKVNEIKV KKGVDLLQNL IKYFHAQCNF FQDGLKAVES
     LKPSIETLST DLHTIKQAQD EERRQLIQLR DILKSALQVE QKESRRDSQL RQSTAYSLHQ
     PQGNKEHGTE RNGNLYKKSD GIRKVWQKRK CSVKNGFLTI SHGTANRPPA KLNLLTCQVK
     TNPEEKKCFD LISHDRTYHF QAEDEQECQI WMSVLQNSKE EALNNAFKGD DNTGENNIVQ
     ELTKEIISEV QRMTGNDVCC DCGAPDPTWL STNLGILTCI ECSGIHRELG VHYSRMQSLT
     LDVLGTSELL LAKNIGNAGF NEIMECCLPS EDPVKPNPGS DMIARKDYIT AKYMERRYAR
     KKHADTAAKL HSLCEAVKTR DIFGLLQAYA DGVDLTEKIP LANGHEPDET ALHLAVRSVD
     RTSLHIVDFL VQNSGNLDKQ TGKGSTALHY CCLTDNAECL KLLLRGKASI EIANESGETP
     LDIAKRLKHE HCEELLTQAL SGRFNSHVHV EYEWRLLHED LDESDDDVDE KLQPSPNRRE
     DRPVSFYQLG SSQFQSNAVS LARDTANLTK DKQRGFGPSI LQNETYGAIL SGSPPSSQSI
     PPSTTSAPPL PPRNVGKDPL TTTPPPPVAK TSGTLEAMNQ PSKSSQPGTS QSKPPPLPPQ
     PPSRLPQKKP ASGTDKPTPL TNKGQPRGPE ASGPLSNAMA LQPPAPMPRK SQATKSKPKR
     VKALYNCVAD NPDELTFSEG DVIIVDGEED QEWWIGHIDG EPSRKGAFPV SFVHFIAD
//
ID   CYFP1_MOUSE             Reviewed;        1253 AA.
AC   Q7TMB8; O88558; Q3U7Q7; Q5DU50; Q7TSZ5; Q80VN6; Q8CE85; Q99LY1;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Cytoplasmic FMR1-interacting protein 1;
DE   AltName: Full=Specifically Rac1-associated protein 1;
DE            Short=Sra-1;
GN   Name=Cyfip1; Synonyms=Kiaa0068, Shyc, Sra1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   MEDLINE=98427792; PubMed=9756361; DOI=10.1016/S0304-3940(98)00531-X;
RA   Koester F., Schinke B., Niemann S., Hermans-Borgmeyer I.;
RT   "Identification of shyc, a novel gene expressed in the murine
RT   developing and adult nervous system.";
RL   Neurosci. Lett. 252:69-71(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, COMPONENT OF WAVE2
RP   COMPLEX, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=14765121; DOI=10.1038/sj.emboj.7600084;
RA   Steffen A., Rottner K., Ehinger J., Innocenti M., Scita G.,
RA   Wehland J., Stradal T.E.B.;
RT   "Sra-1 and Nap1 link Rac to actin assembly driving lamellipodia
RT   formation.";
RL   EMBO J. 23:749-759(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Amnion, Bone marrow macrophage, Embryo, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and FVB/N;
RC   TISSUE=Brain, Mammary gland, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   FUNCTION, INTERACTION WITH FMR1, AND SUBCELLULAR LOCATION.
RX   MEDLINE=21352978; PubMed=11438699; DOI=10.1073/pnas.151231598;
RA   Schenck A., Bardoni B., Moro A., Bagni C., Mandel J.-L.;
RT   "A highly conserved protein family interacting with the fragile X
RT   mental retardation protein (FMRP) and displaying selective
RT   interactions with FMRP-related proteins FXR1P and FXR2P.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:8844-8849(2001).
RN   [7]
RP   FUNCTION, INTERACTION WITH EIF4E AND FMR1, AND MUTAGENESIS OF ASP-724;
RP   LYS-725; ARG-726 AND GLU-730.
RX   PubMed=18805096; DOI=10.1016/j.cell.2008.07.031;
RA   Napoli I., Mercaldo V., Boyl P.P., Eleuteri B., Zalfa F.,
RA   De Rubeis S., Di Marino D., Mohr E., Massimi M., Falconi M., Witke W.,
RA   Costa-Mattioli M., Sonenberg N., Achsel T., Bagni C.;
RT   "The fragile X syndrome protein represses activity-dependent
RT   translation through CYFIP1, a new 4E-BP.";
RL   Cell 134:1042-1054(2008).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19524508; DOI=10.1016/j.cell.2009.04.013;
RA   Silva J.M., Ezhkova E., Silva J., Heart S., Castillo M., Campos Y.,
RA   Castro V., Bonilla F., Cordon-Cardo C., Muthuswamy S.K., Powers S.,
RA   Fuchs E., Hannon G.J.;
RT   "Cyfip1 is a putative invasion suppressor in epithelial cancers.";
RL   Cell 137:1047-1061(2009).
CC   -!- FUNCTION: Component of the CYFIP1-EIF4E-FMR1 complex which binds
CC       to the mRNA cap and mediates translational repression. In the
CC       CYFIP1-EIF4E-FMR1 complex this subunit is an adapter between EIF4E
CC       and FMR1. Promotes the translation repression activity of FMR1 in
CC       brain probably by mediating its association with EIF4E and mRNA.
CC       Involved in formation of membrane ruffles and lamellipodia
CC       protrusions and in axon outgrowth. Binds to F-actin but not to
CC       RNA. Regulator of epithelial morphogenesis. May act as an invasion
CC       suppressor in cancers.
CC   -!- SUBUNIT: Interacts with the active GTP-bound form of RAC1.
CC       Component of the CYFIP1-EIF4E-FMR1 complex which is composed of
CC       CYFIP, EIF4E and FMR1. Interacts with FMR1 but does not bind to
CC       related proteins FXR1 or FXR2. Interaction with EIF4E stimulates
CC       FMR1 binding. Component of the WAVE2 complex composed of ABI1,
CC       CYFIP1/SRA1, NCKAP1/NAP1 and WASF2/WAVE2. Interacts through its C-
CC       terminus with the C-terminus of DPYSL2/CRMP2 which is necessary
CC       for DPYSL2-induced axon outgrowth.
CC   -!- INTERACTION:
CC       P63073:Eif4e; NbExp=1; IntAct=EBI-772928, EBI-2000006;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
CC       Cell projection, lamellipodium. Cell projection, ruffle. Cell
CC       junction, synapse, synaptosome. Note=Highly expressed in the
CC       perinuclear region. Enriched in synaptosomes, membrane ruffles and
CC       at the tips of lamellipodia.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7TMB8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TMB8-2; Sequence=VSP_052348;
CC   -!- TISSUE SPECIFICITY: Highly expressed in embryonic and adult
CC       developing nervous system.
CC   -!- DISRUPTION PHENOTYPE: Mice display greatly reduced lamellipodium
CC       formation in response to growth factor stimulation or aluminum
CC       fluoride treatment. Abnormal epithelial morphogenesis in vitro,
CC       and cooperation with oncogenic Ras to produce invasive carcinomas
CC       in vivo.
CC   -!- SIMILARITY: Belongs to the CYFIP family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90235.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF072697; AAC25773.1; -; mRNA.
DR   EMBL; AJ567911; CAD99196.1; -; mRNA.
DR   EMBL; AK028811; BAC26130.1; -; mRNA.
DR   EMBL; AK146613; BAE27303.1; -; mRNA.
DR   EMBL; AK152558; BAE31312.1; -; mRNA.
DR   EMBL; AK157773; BAE34191.1; -; mRNA.
DR   EMBL; AK220320; BAD90235.1; ALT_INIT; mRNA.
DR   EMBL; BC002174; AAH02174.1; -; mRNA.
DR   EMBL; BC047135; AAH47135.2; -; mRNA.
DR   EMBL; BC052713; AAH52713.1; -; mRNA.
DR   EMBL; BC054429; AAH54429.1; -; mRNA.
DR   IPI; IPI00330476; -.
DR   IPI; IPI00831544; -.
DR   PIR; T14349; T14349.
DR   RefSeq; NP_001158133.1; NM_001164661.1.
DR   RefSeq; NP_001158134.1; NM_001164662.1.
DR   RefSeq; NP_035500.2; NM_011370.3.
DR   UniGene; Mm.333893; -.
DR   UniGene; Mm.37249; -.
DR   IntAct; Q7TMB8; 25.
DR   STRING; Q7TMB8; -.
DR   PhosphoSite; Q7TMB8; -.
DR   PRIDE; Q7TMB8; -.
DR   Ensembl; ENSMUST00000032629; ENSMUSP00000032629; ENSMUSG00000030447.
DR   Ensembl; ENSMUST00000085255; ENSMUSP00000082353; ENSMUSG00000030447.
DR   GeneID; 20430; -.
DR   KEGG; mmu:20430; -.
DR   UCSC; uc009hdm.1; mouse.
DR   CTD; 20430; -.
DR   MGI; MGI:1338801; Cyfip1.
DR   eggNOG; roNOG09488; -.
DR   HOVERGEN; HBG053209; -.
DR   InParanoid; Q7TMB8; -.
DR   OMA; KSGDGEN; -.
DR   OrthoDB; EOG4R7V8X; -.
DR   PhylomeDB; Q7TMB8; -.
DR   NextBio; 298450; -.
DR   ArrayExpress; Q7TMB8; -.
DR   Bgee; Q7TMB8; -.
DR   CleanEx; MM_CYFIP1; -.
DR   CleanEx; MM_SRA1; -.
DR   Genevestigator; Q7TMB8; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0005845; C:mRNA cap binding complex; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR   GO; GO:0019717; C:synaptosome; IDA:UniProtKB.
DR   GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR   GO; GO:0005522; F:profilin binding; TAS:MGI.
DR   GO; GO:0048365; F:Rac GTPase binding; ISS:UniProtKB.
DR   GO; GO:0048675; P:axon extension; ISS:UniProtKB.
DR   GO; GO:0030032; P:lamellipodium assembly; IDA:MGI.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0031529; P:ruffle organization; ISS:UniProtKB.
DR   InterPro; IPR008081; Cytoplasmic_FMR1-int.
DR   InterPro; IPR016536; Cytoplasmic_FMR1-int_sub.
DR   PANTHER; PTHR12195; FragX_IP; 1.
DR   Pfam; PF05994; FragX_IP; 1.
DR   PIRSF; PIRSF008153; FMR1_interacting; 1.
DR   PRINTS; PR01698; CYTOFMRPINTP.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Alternative splicing; Cell junction;
KW   Cell projection; Cell shape; Cytoplasm; Developmental protein;
KW   Differentiation; Neurogenesis; Phosphoprotein; Synapse; Synaptosome.
FT   CHAIN         1   1253       Cytoplasmic FMR1-interacting protein 1.
FT                                /FTId=PRO_0000279707.
FT   REGION      724    732       EIF4E-binding.
FT   MOD_RES     108    108       Phosphotyrosine (By similarity).
FT   MOD_RES    1068   1068       Phosphothreonine (By similarity).
FT   MOD_RES    1197   1197       N6-acetyllysine (By similarity).
FT   VAR_SEQ     570    609       IADKSGSKKTLRSSLEGPTILDIEKFHRESFFYTHLINFS
FT                                -> SSAELLRQLKSLGMERLLHVVNAFLRQSYTYPPLLTFG
FT                                (in isoform 2).
FT                                /FTId=VSP_052348.
FT   MUTAGEN     724    724       D->A: EIF4E-binding reduced by 20%; when
FT                                associated with A-726.
FT   MUTAGEN     724    724       D->K: EIF4E-binding reduced by 60%; when
FT                                associated with E-725, E-726 and K-730.
FT   MUTAGEN     725    725       K->E: EIF4E-binding reduced by 70%.
FT                                EIF4E-binding reduced by 60%; when
FT                                associated with K-724, E-726 and K-730.
FT   MUTAGEN     726    726       R->A: EIF4E-binding reduced by 20%; when
FT                                associated with A-724.
FT   MUTAGEN     726    726       R->E: EIF4E-binding reduced by 60%; when
FT                                associated with K-724, E-725 and K-730.
FT   MUTAGEN     730    730       E->K: EIF4E-binding reduced by 60%; when
FT                                associated with K-724, E-725 and E-726.
FT   CONFLICT    169    169       A -> G (in Ref. 1; AAC25773).
FT   CONFLICT    342    342       Q -> H (in Ref. 5; AAH47135).
FT   CONFLICT    408    408       V -> A (in Ref. 1; AAC25773).
FT   CONFLICT    561    561       M -> L (in Ref. 5; AAH52713).
FT   CONFLICT    566    566       L -> A (in Ref. 5; AAH52713).
FT   CONFLICT    984    984       V -> A (in Ref. 1; AAC25773).
FT   CONFLICT   1079   1079       D -> H (in Ref. 1; AAC25773).
FT   CONFLICT   1222   1222       L -> Q (in Ref. 3; BAC26130).
FT   CONFLICT   1233   1233       S -> T (in Ref. 1; AAC25773).
FT   CONFLICT   1238   1238       H -> Y (in Ref. 3; BAE27303/BAE31312).
SQ   SEQUENCE   1253 AA;  145241 MW;  793986FB417CF19B CRC64;
     MAAQVTLEDA LSNVDLLEEL PLPDQQPCIE PPPSSLLYQP NFNTNFEDRN AFVTGIARYI
     EQATVHSSMN EMLEEGQEYA VMLYTWRSCS RAIPQVKCNE QPNRVEIYEK TVEVLEPEVT
     KLMNFMYFQR NAIERFCGEV RRLCHAERRK DFVSEAYLIT LGKFINMFAV LDELKNMKCS
     VKNDHSAYKR AAQFLRKMAD PQSIQESQNL SMFLANHNKI TQSLQQQLEV ISGYEELLAD
     IVNLCVDYYE NRMYLTPSEK HMLLKVMGFG LYLMDGSVSN IYKLDAKKRI NLSKIDKYFK
     QLQVVPLFGD MQIELARYIK TSAHYEENKS RWTCASSSSS PQYNICEQMI QIREDHMRFI
     SELARYSNSE VVTGSGRQEA QKTDAEYRKL FDLALQGLQL LSQWSAHVME VYSWKLVHPT
     DKYSNKDCPD NAEEYERATR YNYTTEEKFA LVEVIAMIKG LQVLMGRMES VFNHAIRHTV
     YAALQDFSQV TLREPLRQAI KKKKNVIQSV LQAIRKTVCD WETGHEPFND PALRGEKDPK
     SGFDIKVPRR AVGPSSTQLY MVRTMLESLI ADKSGSKKTL RSSLEGPTIL DIEKFHRESF
     FYTHLINFSE TLQQCCDLSQ LWFREFFLEL TMGRRIQFPI EMSMPWILTD HILETKEASM
     MEYVLYSLDL YNDSAHYALT KFNKQFLYDE IEAEVNLCFD QFVYKLADQI FAYYKVMAGS
     LLLDKRLRSE CKNQGATIHL PPSNRYETLL KQRHVQLLGR SIDLNRLITQ RVSAAMYKSL
     ELAIGRFESE DLTSVVELDG LLEINRMTHK LLSRYLTLDS FDAMFREANH NVSAPYGRIT
     LHVFWELNYD FLPNYCYNGS TNRFVRTVLP FSQEFQRDKQ PNAQPQYLHG SKALNLAYSS
     IYGSYRNFVG PPHFQVICRL LGYQGIAVVM EELLKVVKSL LQGTILQYVK TLMEVMPKIC
     RLPRHEYGSP GILEFFHHQL KDIVEYAELK TVCFQNLREV GNAVLFCLLI EQSLSLEEVC
     DLLHAAPFQN ILPRIHVKEG ERVDAKMKRL ESKYAPLHLV PLIERLGTPQ QIAIAREGDL
     LTKERLCCGL SMFEVILTRI RTFLDDPIWR GPLPSNGVMH VDECVEFHRL WSAMQFVYCI
     PVGTHEFTVE QCFGDGLHWA GCMIIVLLGQ QRRFAVLDFC YHLLKVQKHD GKDEIIKNVP
     LKKMVERIRK FQILNDEIIT ILDKYLKSGD GESTPVEHVR CFQPPIHQSL ASS
//
ID   LPPR4_MOUSE             Reviewed;         766 AA.
AC   Q7TME0; B2RQ15; Q6ZQA8; Q8BV73; Q8BXK2; Q8R3R6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Lipid phosphate phosphatase-related protein type 4;
DE            EC=3.1.3.4;
DE   AltName: Full=Brain-specific phosphatidic acid phosphatase-like protein 1;
DE   AltName: Full=Plasticity-related gene 1 protein;
DE            Short=PRG-1;
GN   Name=Lppr4; Synonyms=D3Bwg0562e, Kiaa0455, Prg1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/J, and BALB/c; TISSUE=Brain, and Testis;
RX   MEDLINE=22656544; PubMed=12730698; DOI=10.1038/nn1052;
RA   Braeuer A.U., Savaskan N.E., Kuehn H., Prehn S., Ninnemann O.,
RA   Nitsch R.;
RT   "A new phospholipid phosphatase, PRG-1, is involved in axon growth and
RT   regenerative sprouting.";
RL   Nat. Neurosci. 6:572-578(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347 AND THR-417, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Hydrolyzes lysophosphatidic acid (LPA). Facilitates
CC       axonal outgrowth during development and regenerative sprouting. In
CC       the outgrowing axons acts as an ecto-enzyme and attenuates
CC       phospholipid-induced axon collapse in neurons and facilitates
CC       outgrowth in the hippocampus (By similarity).
CC   -!- CATALYTIC ACTIVITY: A 1,2-diacylglycerol 3-phosphate + H(2)O = a
CC       1,2-diacyl-sn-glycerol + phosphate.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC37711.1; Type=Erroneous initiation;
CC       Sequence=BAC97959.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY266266; AAP41099.1; -; mRNA.
DR   EMBL; AY266267; AAP41100.1; -; mRNA.
DR   EMBL; AF541279; AAP57768.1; -; mRNA.
DR   EMBL; AK129149; BAC97959.1; ALT_INIT; mRNA.
DR   EMBL; AK046782; BAC32865.1; -; mRNA.
DR   EMBL; AK079635; BAC37711.1; ALT_INIT; mRNA.
DR   EMBL; BC024711; AAH24711.1; -; mRNA.
DR   EMBL; BC137701; AAI37702.1; -; mRNA.
DR   EMBL; BC137702; AAI37703.1; -; mRNA.
DR   IPI; IPI00420590; -.
DR   RefSeq; NP_808332.3; NM_177664.5.
DR   UniGene; Mm.140138; -.
DR   ProteinModelPortal; Q7TME0; -.
DR   STRING; Q7TME0; -.
DR   PhosphoSite; Q7TME0; -.
DR   PRIDE; Q7TME0; -.
DR   Ensembl; ENSMUST00000061071; ENSMUSP00000052306; ENSMUSG00000044667.
DR   GeneID; 229791; -.
DR   KEGG; mmu:229791; -.
DR   CTD; 229791; -.
DR   MGI; MGI:106530; D3Bwg0562e.
DR   eggNOG; roNOG06146; -.
DR   GeneTree; ENSGT00550000074203; -.
DR   HOGENOM; HBG443683; -.
DR   HOVERGEN; HBG103365; -.
DR   InParanoid; Q7TME0; -.
DR   OMA; SSDGIAH; -.
DR   OrthoDB; EOG4JWVD5; -.
DR   BRENDA; 3.1.3.4; 244.
DR   NextBio; 379679; -.
DR   ArrayExpress; Q7TME0; -.
DR   Bgee; Q7TME0; -.
DR   Genevestigator; Q7TME0; -.
DR   GO; GO:0008195; F:phosphatidate phosphatase activity; IEA:EC.
DR   InterPro; IPR016118; P_Acid_Pase/Cl_peroxidase_N.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   Gene3D; G3DSA:1.20.144.10; P_Acid_Pase/Cl_peroxidase_N; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; AcPase_VanPerase; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Hydrolase; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    766       Lipid phosphate phosphatase-related
FT                                protein type 4.
FT                                /FTId=PRO_0000317437.
FT   TRANSMEM     68     88       Helical; (Potential).
FT   TRANSMEM    120    140       Helical; (Potential).
FT   TRANSMEM    179    199       Helical; (Potential).
FT   TRANSMEM    248    268       Helical; (Potential).
FT   TRANSMEM    277    297       Helical; (Potential).
FT   TRANSMEM    309    329       Helical; (Potential).
FT   COMPBIAS    698    701       Poly-His.
FT   MOD_RES     218    218       Phosphoserine.
FT   MOD_RES     347    347       Phosphoserine.
FT   MOD_RES     417    417       Phosphothreonine.
FT   CARBOHYD    215    215       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    220    220       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    269    269       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    363    363       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    433    433       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    456    456       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    515    515       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    545    545       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    570    570       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    451    451       Q -> R (in Ref. 3; BAC32865).
FT   CONFLICT    495    496       DH -> ED (in Ref. 4; AAH24711).
FT   CONFLICT    500    500       G -> S (in Ref. 4; AAH24711).
FT   CONFLICT    543    543       Q -> K (in Ref. 3; BAC32865).
FT   CONFLICT    568    568       A -> D (in Ref. 1; AAP41099/AAP41100/
FT                                AAP57768).
FT   CONFLICT    653    653       K -> E (in Ref. 3; BAC37711).
FT   CONFLICT    654    654       A -> V (in Ref. 1; AAP41099/AAP41100/
FT                                AAP57768).
FT   CONFLICT    737    737       I -> V (in Ref. 3; BAC32865).
SQ   SEQUENCE   766 AA;  83290 MW;  371D9FA1A829B5B1 CRC64;
     MQRAGSSGAR GECDISGAGR LRLEQAARLG GRTVHTSPGG GLGARQAAGM SAKERPKGKV
     IKDSVTLLPC FYFVELPILA SSVVSLYFLE LTDVFKPVHS GFSCYDRSLS MPYIEPTQEA
     IPFLMLLSLA FAGPAITIMV GEGILYCCLS KRRNGAGLEP NINAGGCNFN SFLRRAVRFV
     GVHVFGLCST ALITDIIQLS TGYQAPYFLT VCKPNYTSLN VSCKENSYIV EDICSGSDLT
     VINSGRKSFP SQHATLAAFA AVYVSMYFNS TLTDSSKLLK PLLVFTFIIC GIICGLTRIT
     QYKNHPVDVY CGFLIGGGIA LYLGLYAVGN FLPSEDSMLQ HRDALRSLTD LNQDPSRVLS
     AKNGSSGDGI AHTEGILNRN HRDASSLTNL KRANADVEII TPRSPMGKES MVTFSNTLPR
     ANTPSVEDPV RRNASIHASM DSARSKQLLT QWKSKNESRK MSLQVMDTEP EGQSPPRSIE
     MRSSSEPSRV GVNGDHHVPG NQYLKIQPGT VPGCNNSMPG GPRVSIQSRP GSSQLVHIPE
     ETQENISTSP KSSSARAKWL KAAEKTVACN RSNNQPRIMQ VIAMSKQQGV LQSSPKNAEG
     STVTCTGSIR YKTLTDHEPS GIVRVEAHPE NNRPIIQIPS STEGEGSGSW KWKAPEKSSL
     RQTYELNDLN RDSESCESLK DSFGSGDRKR SNIDSNEHHH HGITTIRVTP VEGSEIGSET
     LSVSSSRDST LRRKGNIILI PERSNSPENT RNIFYKGTSP TRAYKD
//
ID   HNRPQ_MOUSE             Reviewed;         623 AA.
AC   Q7TMK9; O88991; Q2YDV8; Q68ED6; Q80YV6; Q8BGP1; Q8C5K6; Q8CGC2;
AC   Q91ZR0; Q99KU9; Q9QYF4;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Heterogeneous nuclear ribonucleoprotein Q;
DE            Short=hnRNP Q;
DE   AltName: Full=Glycine- and tyrosine-rich RNA-binding protein;
DE            Short=GRY-RBP;
DE   AltName: Full=NS1-associated protein 1;
DE   AltName: Full=Synaptotagmin-binding, cytoplasmic RNA-interacting protein;
DE   AltName: Full=pp68;
GN   Name=Syncrip; Synonyms=Hnrpq, Nsap1, Nsap1l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Du G., Pan M., Zhou Y., Chen J., Yao H., Yuan J., Qiang B.;
RT   "Cloning of human and mouse GRY-RBP cDNA.";
RL   Chin. Sci. Bull. 45:343-349(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 257-282,
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, RNA-BINDING, AND INTERACTION
RP   WITH SYT7; SYT8 AND SYT9.
RC   STRAIN=ddY; TISSUE=Brain, and Cerebellum;
RX   MEDLINE=20200483; PubMed=10734137; DOI=10.1074/jbc.275.13.9823;
RA   Mizutani A., Fukuda M., Ibata K., Shiraishi Y., Mikoshiba K.;
RT   "SYNCRIP, a cytoplasmic counterpart of heterogeneous nuclear
RT   ribonucleoprotein R, interacts with ubiquitous synaptotagmin
RT   isoforms.";
RL   J. Biol. Chem. 275:9823-9831(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, C57BL/6J, Czech II, and FVB/N;
RC   TISSUE=Embryo, Embryonic brain, Kidney, Mammary tumor, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 66-561 (ISOFORM 2).
RA   Zhou M., Raschke W.C.;
RT   "Mus musculus RRM RNA binding protein, NSAP1.";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION,
RP   PHOSPHORYLATION AT TYROSINE RESIDUES, AND ASSOCIATION WITH POLYSOMES.
RC   TISSUE=Adipocyte;
RX   PubMed=11994298; DOI=10.1074/jbc.M202556200;
RA   Hresko R.C., Mueckler M.;
RT   "Identification of pp68 as the tyrosine-phosphorylated form of
RT   SYNCRIP/NSAP1. A cytoplasmic RNA-binding protein.";
RL   J. Biol. Chem. 277:25233-25238(2002).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=99102562; PubMed=9847309;
RA   Harris C.E., Boden R.A., Astell C.R.;
RT   "A novel heterogeneous nuclear ribonucleoprotein-like protein
RT   interacts with NS1 of the minute virus of mice.";
RL   J. Virol. 73:72-80(1999).
RN   [8]
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH SMN.
RX   PubMed=11773003; DOI=10.1093/hmg/11.1.93;
RA   Rossoll W., Kroening A.-K., Ohndorf U.-M., Steegborn C., Jablonka S.,
RA   Sendtner M.;
RT   "Specific interaction of Smn, the spinal muscular atrophy determining
RT   gene product, with hnRNP-R and gry-rbp/hnRNP-Q: a role for Smn in RNA
RT   processing in motor axons?";
RL   Hum. Mol. Genet. 11:93-105(2002).
RN   [9]
RP   IDENTIFICATION IN A HISTONE PRE-MRNA COMPLEX, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=19470752; DOI=10.1128/MCB.00296-09;
RA   Yang X.-C., Torres M.P., Marzluff W.F., Dominski Z.;
RT   "Three proteins of the U7-specific Sm ring function as the molecular
RT   ruler to determine the site of 3'-end processing in mammalian histone
RT   pre-mRNA.";
RL   Mol. Cell. Biol. 29:4045-4056(2009).
CC   -!- FUNCTION: Heterogeneous nuclear ribonucleoprotein (hnRNP)
CC       implicated in mRNA processing mechanisms. Component of the CRD-
CC       mediated complex that promotes MYC mRNA stability. Isoform 1 and
CC       isoform 2 are associated in vitro with pre-mRNA, splicing
CC       intermediates and mature mRNA protein complexes. Isoform 1 binds
CC       to apoB mRNA AU-rich sequences (By similarity). Isoform 1 is part
CC       of the APOB mRNA editosome complex and may modulate the
CC       postranscriptional C to U RNA-editing of the APOB mRNA through
CC       either by binding to A1CF (APOBEC1 complementation factor), to
CC       APOBEC1 or to RNA itself (By similarity). May be involved in
CC       translationally coupled mRNA turnover. Implicated with other RNA-
CC       binding proteins in the cytoplasmic deadenylation/translational
CC       and decay interplay of the FOS mRNA mediated by the major coding-
CC       region determinant of instability (mCRD) domain (By similarity).
CC       Interacts in vitro preferentially with poly(A) and poly(U) RNA
CC       sequences. Isoform 2 may be involved in cytoplasmic vesicle-based
CC       mRNA transport through interaction with synaptotagmins.
CC   -!- SUBUNIT: Identified in the spliceosome C complex, at least
CC       composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23,
CC       DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1,
CC       GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK,
CC       HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1,
CC       PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B,
CC       PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2,
CC       SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2,
CC       SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2,
CC       SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8.
CC       Component of the coding region determinant (CRD)-mediated complex,
CC       composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identified in
CC       a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU,
CC       IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and
CC       YBX1. Identified in a mRNP granule complex, at least composed of
CC       ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD,
CC       HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1,
CC       NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8,
CC       RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs (By
CC       similarity). Isoform 1 is a component of the APOB mRNA editosome
CC       complex. Isoform 1 interacts with APOBEC1 and A1CF. Part of a
CC       complex associated with the FOS mCRD domain and consisting of
CC       PABPC1, PAIP1, CSDE1/UNR, HNRPD and SYNCRIP. Isoform 2 interacts
CC       with HNRPR. Interacts with POLR2A hyperphosphorylated C-terminal
CC       domain. Interacts with minute virus of mice (MVM) NS1 protein (By
CC       similarity). Identified in a histone pre-mRNA complex, at least
CC       composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1. Isoform 1
CC       and isoform 2 interact with SMN. Isoform 2 interacts through its
CC       C-terminal domain with SYT7, SYT8 and SYT9. The non-phosphorylated
CC       and phosphorylated forms are colocalized with PAIP1 in polysomes.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Localized in
CC       cytoplasmic mRNP granules containing untranslated mRNAs. Isoforms
CC       1 and 2 are expressed predominantly in the nucleoplasm (By
CC       similarity). According to PubMed:10734137, isoform 2 is
CC       predominantly found in cytoplasm. The tyrosine phosphorylated form
CC       bound to RNA is found in microsomes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7TMK9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TMK9-2; Sequence=VSP_009585, VSP_009586;
CC         Note=May be due to a competing donor splice site and to an exon
CC         inclusion. Ref.2 (BAA88342) and Ref.4 (AAH41148) sequences are
CC         in conflict in positions: 549:GQ->G;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Detected in heart, brain, spleen,
CC       lung, liver, skeletal muscle, adipocytes, kidney and testis.
CC   -!- DEVELOPMENTAL STAGE: Expressed in spinal cord at 14 dpc and
CC       onwards.
CC   -!- DOMAIN: The domain containing eight Arg-Gly-Gly repeats may be
CC       involved in RNA-binding and protein-protein interactions.
CC   -!- PTM: Phosphorylated on tyrosine. The membrane-bound form found in
CC       microsomes is phosphorylated in vitro by insulin receptor tyrosine
CC       kinase (INSR). Phosphorylation is inhibited upon binding to RNA,
CC       whereas the cytoplasmic form is poorly phosphorylated.
CC       Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH55863.1; Type=Erroneous initiation;
CC       Sequence=AAH58807.1; Type=Erroneous initiation;
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DR   EMBL; AF093821; AAC62511.1; -; mRNA.
DR   EMBL; AB035725; BAA88342.1; -; mRNA.
DR   EMBL; AK034845; BAC28852.1; -; mRNA.
DR   EMBL; AK077588; BAC36880.1; -; mRNA.
DR   EMBL; AK078158; BAC37152.1; -; mRNA.
DR   EMBL; BC004001; AAH04001.1; ALT_SEQ; mRNA.
DR   EMBL; BC041148; AAH41148.2; -; mRNA.
DR   EMBL; BC050079; AAH50079.2; -; mRNA.
DR   EMBL; BC055863; AAH55863.1; ALT_INIT; mRNA.
DR   EMBL; BC058807; AAH58807.1; ALT_INIT; mRNA.
DR   EMBL; BC080309; AAH80309.1; -; mRNA.
DR   EMBL; BC108363; AAI08364.2; -; mRNA.
DR   EMBL; AF408434; AAL11726.1; -; mRNA.
DR   IPI; IPI00406117; -.
DR   IPI; IPI00406118; -.
DR   RefSeq; NP_062640.2; NM_019666.2.
DR   RefSeq; NP_062770.1; NM_019796.4.
DR   UniGene; Mm.260545; -.
DR   ProteinModelPortal; Q7TMK9; -.
DR   SMR; Q7TMK9; 159-423.
DR   STRING; Q7TMK9; -.
DR   PhosphoSite; Q7TMK9; -.
DR   REPRODUCTION-2DPAGE; IPI00406117; -.
DR   PRIDE; Q7TMK9; -.
DR   Ensembl; ENSMUST00000069221; ENSMUSP00000063744; ENSMUSG00000032423.
DR   GeneID; 56403; -.
DR   KEGG; mmu:56403; -.
DR   UCSC; uc009qyo.1; mouse.
DR   UCSC; uc009qyr.1; mouse.
DR   CTD; 56403; -.
DR   MGI; MGI:1891690; Syncrip.
DR   eggNOG; roNOG12756; -.
DR   GeneTree; ENSGT00550000074366; -.
DR   HOVERGEN; HBG051917; -.
DR   InParanoid; Q7TMK9; -.
DR   OMA; THMYDEY; -.
DR   OrthoDB; EOG4FN4HM; -.
DR   NextBio; 312520; -.
DR   ArrayExpress; Q7TMK9; -.
DR   Bgee; Q7TMK9; -.
DR   Genevestigator; Q7TMK9; -.
DR   GermOnline; ENSMUSG00000032423; Mus musculus.
DR   GO; GO:0070937; C:CRD-mediated mRNA stability complex; ISS:UniProtKB.
DR   GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; IDA:UniProtKB.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0008143; F:poly(A) RNA binding; IDA:MGI.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR006535; HnRNP_R/Q_splicing_fac.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 3.
DR   Pfam; PF00076; RRM_1; 3.
DR   SMART; SM00360; RRM; 3.
DR   TIGRFAMs; TIGR01648; hnRNP-R-Q; 1.
DR   PROSITE; PS50102; RRM; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm;
KW   Direct protein sequencing; Isopeptide bond; mRNA processing;
KW   mRNA splicing; Nucleus; Phosphoprotein; Repeat; Ribonucleoprotein;
KW   RNA-binding; Spliceosome; Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    623       Heterogeneous nuclear ribonucleoprotein
FT                                Q.
FT                                /FTId=PRO_0000081868.
FT   DOMAIN      162    241       RRM 1.
FT   DOMAIN      243    325       RRM 2.
FT   DOMAIN      338    408       RRM 3.
FT   REPEAT      448    450       1-1.
FT   REPEAT      451    453       1-2.
FT   REPEAT      460    464       2-1.
FT   REPEAT      469    472       2-2.
FT   REPEAT      478    480       1-3.
FT   REPEAT      485    488       2-3.
FT   REPEAT      498    500       1-4.
FT   REPEAT      526    528       1-5.
FT   REPEAT      539    541       1-6.
FT   REPEAT      554    556       1-7.
FT   REPEAT      557    559       1-8.
FT   REGION      400    561       Interaction with APOBEC1 (By similarity).
FT   REGION      448    559       8 X 3 AA repeats of R-G-G.
FT   REGION      460    488       3 X 4 AA repeats of Y-Y-G-Y.
FT   REGION      518    549       Interaction with SMN (By similarity).
FT   MOTIF       564    578       Bipartite nuclear localization signal
FT                                (Potential).
FT   COMPBIAS    431    434       Poly-Tyr.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     221    221       N6-acetyllysine (By similarity).
FT   MOD_RES     363    363       N6-acetyllysine (By similarity).
FT   MOD_RES     373    373       Phosphotyrosine (By similarity).
FT   MOD_RES     587    587       Phosphoserine (By similarity).
FT   CROSSLNK    123    123       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   VAR_SEQ     550    562       VRGARGGRGGNVG -> QGKGVEAGPDLLQ (in
FT                                isoform 2).
FT                                /FTId=VSP_009585.
FT   VAR_SEQ     563    623       Missing (in isoform 2).
FT                                /FTId=VSP_009586.
FT   CONFLICT    143    143       K -> E (in Ref. 4; AAH58807).
FT   CONFLICT    194    194       M -> T (in Ref. 4; AAH50079).
FT   CONFLICT    201    201       L -> LTGL (in Ref. 1; AAC62511).
FT   CONFLICT    220    220       V -> A (in Ref. 1; AAC62511).
FT   CONFLICT    291    291       L -> Q (in Ref. 1; AAC62511).
FT   CONFLICT    298    298       T -> A (in Ref. 1; AAC62511).
FT   CONFLICT    407    407       K -> N (in Ref. 3; BAC37152).
FT   CONFLICT    411    411       Q -> K (in Ref. 3; BAC37152).
FT   CONFLICT    421    421       Q -> H (in Ref. 3; BAC37152).
FT   CONFLICT    528    528       G -> A (in Ref. 1; AAC62511).
FT   CONFLICT    543    543       Missing (in Ref. 1; AAC62511).
FT   CONFLICT    582    582       N -> H (in Ref. 1; AAC62511).
SQ   SEQUENCE   623 AA;  69633 MW;  8139FF9E2C8FB304 CRC64;
     MATEHVNGNG TEEPMDTTSA VIHSENFQTL LDAGLPQKVA EKLDEIYVAG LVAHSDLDER
     AIEALKEFNE DGALAVLQQF KDSDLSHVQN KSAFLCGVMK TYRQREKQGT KVADSSKGPD
     EAKIKALLER TGYTLDVTTG QRKYGGPPPD SVYSGQQPSV GTEIFVGKIP RDLFEDELVP
     LFEKAGPIWD LRLMMDPLTG LNRGYAFVTF CTKEAAQEAV KLYNNHEIRS GKHIGVCISV
     ANNRLFVGSI PKSKTKEQIL EEFSKVTEGL TDVILYHQPD DKKKNRGFCF LEYEDHKTAA
     QARRRLMSGK VKVWGNVGTV EWADPIEDPD PEVMAKVKVL FVRNLANTVT EEILEKSFSQ
     FGKLERVKKL KDYAFIHFDE RDGAVKAMEE MNGKDLEGEN IEIVFAKPPD QKRKERKAQR
     QAAKNQMYDD YYYYGPPHMP PPTRGRGRGG RGGYGYPPDY YGYEDYYDYY GYDYHNYRGG
     YEDPYYGYED FQVGARGRGG RGARGAAPSR GRGAAPPRGR AGYSQRGGPG SARGVRGARG
     GAQQQRGRGV RGARGGRGGN VGGKRKADGY NQPDTKRRQT NNQNWGSQPI AQQPLQGGDH
     SGNYGYKSEN QEFYQDTFGQ QWK
//
ID   TBB2A_MOUSE             Reviewed;         445 AA.
AC   Q7TMM9;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Tubulin beta-2A chain;
GN   Name=Tubb2a; Synonyms=Tubb2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 104-121; 253-262 AND 381-390, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   POLYGLUTAMYLATION.
RX   PubMed=15890843; DOI=10.1126/science.1113010;
RA   Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M.,
RA   Temurak N., van Dijk J., Boucher D., van Dorsselaer A.,
RA   Suryavanshi S., Gaertig J., Edde B.;
RT   "Tubulin polyglutamylase enzymes are members of the TTL domain protein
RT   family.";
RL   Science 308:1758-1762(2005).
RN   [5]
RP   POLYGLYCYLATION.
RX   PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA   Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M.,
RA   Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J.,
RA   Janke C.;
RT   "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT   polyglycylation.";
RL   Cell 137:1076-1087(2009).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. It
CC       binds two moles of GTP, one at an exchangeable site on the beta
CC       chain and one at a non-exchangeable site on the alpha-chain (By
CC       similarity).
CC   -!- SUBUNIT: Dimer of alpha and beta chains (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC   -!- PTM: Some glutamate residues at the C-terminus are either
CC       polyglutamylated or polyglycylated. These 2 modifications occur
CC       exclusively on glutamate residues and result in either
CC       polyglutamate or polyglycine chains on the gamma-carboxyl group.
CC       Glycylation is mainly limited to tubulin incorporated into
CC       axonemes (cilia and flagella) whereas glutamylation is prevalent
CC       in neuronal cells, centrioles, axonemes, and the mitotic spindle.
CC       Both modifications can coexist on the same protein on adjacent
CC       residues, and lowering polyglycylation levels increases
CC       polyglutamylation, and reciprocally. The precise function of such
CC       modifications is still unclear but they are regulate the assembly
CC       and dynamics of axonemal microtubules.
CC   -!- SIMILARITY: Belongs to the tubulin family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK134545; BAE22178.1; -; mRNA.
DR   EMBL; BC055441; AAH55441.1; -; mRNA.
DR   IPI; IPI00338039; -.
DR   RefSeq; NP_033476.1; NM_009450.2.
DR   UniGene; Mm.469917; -.
DR   HSSP; P02554; 1FFX.
DR   ProteinModelPortal; Q7TMM9; -.
DR   SMR; Q7TMM9; 2-428.
DR   STRING; Q7TMM9; -.
DR   PhosphoSite; Q7TMM9; -.
DR   UCD-2DPAGE; Q7TMM9; -.
DR   PRIDE; Q7TMM9; -.
DR   Ensembl; ENSMUST00000056427; ENSMUSP00000060246; ENSMUSG00000058672.
DR   GeneID; 22151; -.
DR   KEGG; mmu:22151; -.
DR   UCSC; uc007qbb.1; mouse.
DR   CTD; 22151; -.
DR   MGI; MGI:107861; Tubb2a.
DR   eggNOG; roNOG14625; -.
DR   HOGENOM; HBG750007; -.
DR   HOVERGEN; HBG000089; -.
DR   InParanoid; Q7TMM9; -.
DR   OMA; YNEAGSN; -.
DR   OrthoDB; EOG4DFPNJ; -.
DR   PhylomeDB; Q7TMM9; -.
DR   NextBio; 302062; -.
DR   ArrayExpress; Q7TMM9; -.
DR   Bgee; Q7TMM9; -.
DR   CleanEx; MM_TUBB2A; -.
DR   Genevestigator; Q7TMM9; -.
DR   GermOnline; ENSMUSG00000058672; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR   InterPro; IPR013838; Beta-tubulin_BS.
DR   InterPro; IPR002453; Beta_tubulin.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR023123; Tubulin_C.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   Gene3D; G3DSA:3.30.1330.20; Tubulin/FtsZ_2-layer-sand-dom; 1.
DR   Gene3D; G3DSA:1.10.287.600; Tubulin_C; 1.
DR   Gene3D; G3DSA:3.40.50.1440; Tubulin_FtsZ; 1.
DR   PANTHER; PTHR11588; Tubulin; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01163; BETATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF55307; Tub_FtsZ_C; 1.
DR   SUPFAM; SSF52490; Tubulin_FtsZ; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
DR   PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding;
KW   Microtubule; Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1    445       Tubulin beta-2A chain.
FT                                /FTId=PRO_0000262650.
FT   NP_BIND     140    146       GTP (Potential).
FT   MOD_RES      78     78       Phosphoserine (By similarity).
FT   MOD_RES      95     95       Phosphoserine (By similarity).
SQ   SEQUENCE   445 AA;  49907 MW;  93B3213EB2A9367B CRC64;
     MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEAAGNKYV
     PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
     RKESESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVM PSPKVSDTVV
     EPYNATLSVH QLVENTDETY SIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL
     RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDSKNMM
     AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG
     LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDATA DEQGEFEEEE GEDEA
//
ID   WDR91_MOUSE             Reviewed;         748 AA.
AC   Q7TMQ7; Q80XN1;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=WD repeat-containing protein 91;
GN   Name=Wdr91;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N, and FVB/N-3; TISSUE=Liver, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 7 WD repeats.
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DR   EMBL; BC043682; AAH43682.1; -; mRNA.
DR   EMBL; BC055046; AAH55046.1; -; mRNA.
DR   IPI; IPI00339693; -.
DR   RefSeq; NP_001013384.1; NM_001013366.1.
DR   UniGene; Mm.152120; -.
DR   UniGene; Mm.474518; -.
DR   ProteinModelPortal; Q7TMQ7; -.
DR   SMR; Q7TMQ7; 403-439, 542-635.
DR   PhosphoSite; Q7TMQ7; -.
DR   PRIDE; Q7TMQ7; -.
DR   Ensembl; ENSMUST00000081214; ENSMUSP00000079974; ENSMUSG00000058486.
DR   GeneID; 101240; -.
DR   KEGG; mmu:101240; -.
DR   UCSC; uc009bhz.1; mouse.
DR   CTD; 101240; -.
DR   MGI; MGI:2141558; Wdr91.
DR   eggNOG; roNOG06467; -.
DR   GeneTree; ENSGT00390000001566; -.
DR   HOGENOM; HBG445297; -.
DR   HOVERGEN; HBG057115; -.
DR   InParanoid; Q7TMQ7; -.
DR   OMA; DSEGNYM; -.
DR   OrthoDB; EOG4W6NVC; -.
DR   NextBio; 354834; -.
DR   ArrayExpress; Q7TMQ7; -.
DR   Bgee; Q7TMQ7; -.
DR   CleanEx; MM_WDR91; -.
DR   Genevestigator; Q7TMQ7; -.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 4.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   1: Evidence at protein level;
KW   Coiled coil; Phosphoprotein; Repeat; WD repeat.
FT   CHAIN         1    748       WD repeat-containing protein 91.
FT                                /FTId=PRO_0000295747.
FT   REPEAT      407    446       WD 1.
FT   REPEAT      449    489       WD 2.
FT   REPEAT      512    556       WD 3.
FT   REPEAT      561    600       WD 4.
FT   REPEAT      603    642       WD 5.
FT   REPEAT      665    703       WD 6.
FT   REPEAT      710    748       WD 7.
FT   COILED      183    228       Potential.
FT   MOD_RES     255    255       Phosphoserine (By similarity).
FT   MOD_RES     257    257       Phosphoserine.
FT   CONFLICT    590    590       F -> L (in Ref. 1; AAH43682).
SQ   SEQUENCE   748 AA;  83421 MW;  3973DC3AD76DFA13 CRC64;
     MAEAVERTDE LVREYLLFRG FTHTLRQLDA EIKADKEKGF RVDKIVDQLQ QLMQVYDLAA
     LRDYWSYLER RLFSRLEDIY RPTINKLKTS LFRFYLVYTI QTNRNDKAQE FFAKQATELQ
     NQAEWKDWFV LPFLPSPDTN PTFATYFSRQ WADTFIISLH NFLSVLFQCM PVPVILNFDA
     ECQRTNQVQE ENEVLRQKLF ALQAEIHRLK KEEQQQEEEA AALVQHKLPP YVSSMDRLGD
     SELALVCSQR PASLSQSPRV GFLSSLLPQS KKSPSRLSPA QGPPQAQSSA KKDSFSSQAT
     KGKDSVPGAK DGKSLLSGPV PGEASWTHQR QRRLQDHGKE RRELLSTSSS QSQCAERKPE
     VSGAEAEPCL ELHMGPVEVL ARVSTAGSEG DRPEQPFIVL SQEEYGEHHS SIMHCRVDCS
     GRRVASLDVD GVIKVWSFNP IMQTKASSIS KSPLLSLEWA TKRDRLLLLG SGVGTVRLYD
     TEAKKNLCEI NINDDMPRIL SLACSPNGAS FVCSAAAPSL TSQTDSSAPD IGSKGMNQVP
     GKLLLWDTKT MKQQLQFSLD PEPIAINCTA FNHNGNLLVT GAADGVIRLF DMQQHECAMS
     WKAHCGEVYS VEFSCDENAV YSIGEDRKFI QWNIHKSGLK VSESNLPSDA TGPFVLSGYS
     GYKQVQVPRG RLFAFDSEGN YMLTCSATGG LIYKLGSEEK VLENCLSLGG HRAPVVTVDW
     STAMDCGTCL TASMDGKIKL TTLLAHKL
//
ID   HUWE1_MOUSE             Reviewed;        4377 AA.
AC   Q7TMY8; Q4G2Z1; Q5BMM7; Q6NS61; Q8BNJ7; Q8CFH2; Q8VD14; Q921M5;
AC   Q9R0P2;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 4.
DT   30-NOV-2010, entry version 72.
DE   RecName: Full=E3 ubiquitin-protein ligase HUWE1;
DE            EC=6.3.2.-;
DE   AltName: Full=E3Histone;
DE   AltName: Full=HECT, UBA and WWE domain-containing protein 1;
DE   AltName: Full=Upstream regulatory element-binding protein 1;
DE            Short=URE-B1;
DE            Short=URE-binding protein 1;
GN   Name=Huwe1; Synonyms=Kiaa0312, Ureb1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   PubMed=15989956; DOI=10.1016/j.cell.2005.03.037;
RA   Chen D., Kon N., Li M., Zhang W., Qin J., Gu W.;
RT   "ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor.";
RL   Cell 121:1071-1083(2005).
RN   [2]
RP   SEQUENCE REVISION TO 253; 1728; 2009-2010; 2032 AND 3034-3035.
RA   Chen D., Kon N., Li M., Zhang W., Qin J., Gu W.;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC   STRAIN=C57BL/6J;
RX   PubMed=15767685; DOI=10.1128/MCB.25.7.2819-2831.2005;
RA   Liu Z., Oughtred R., Wing S.S.;
RT   "Characterization of E3Histone, a novel testis ubiquitin protein
RT   ligase which ubiquitinates histones.";
RL   Mol. Cell. Biol. 25:2819-2831(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1445-4377 (ISOFORM 1).
RC   TISSUE=Embryonic intestine;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [5]
RP   SEQUENCE REVISION.
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PROTEIN SEQUENCE OF 1627-1655; 3127-3133 AND 3245-3253, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1630-4377 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3283-4377 (ISOFORM 3).
RC   STRAIN=C57BL/6, and FVB/N-3; TISSUE=Brain, Eye, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3421-4377 (ISOFORM 4).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4005-4377 (ISOFORMS 1/3).
RA   Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.;
RT   "Mouse homolog to KIAA0312.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3758, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1907, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3758 AND SER-3810, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [13]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=17823942; DOI=10.1002/dvdy.21302;
RA   Liu Z., Miao D., Xia Q., Hermo L., Wing S.S.;
RT   "Regulated expression of the ubiquitin protein ligase,
RT   E3(Histone)/LASU1/Mule/ARF-BP1/HUWE1, during spermatogenesis.";
RL   Dev. Dyn. 236:2889-2898(2007).
RN   [14]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=18488021; DOI=10.1038/ncb1727;
RA   Zhao X., Heng J.I.-T., Guardavaccaro D., Jiang R., Pagano M.,
RA   Guillemot F., Iavarone A., Lasorella A.;
RT   "The HECT-domain ubiquitin ligase Huwe1 controls neural
RT   differentiation and proliferation by destabilizing the N-Myc
RT   oncoprotein.";
RL   Nat. Cell Biol. 10:643-653(2008).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1907, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which mediates
CC       ubiquitination and subsequent proteasomal degradation of target
CC       proteins. Regulates apoptosis by catalyzing the polyubiquitination
CC       and degradation of MCL1. Also ubiquitinates the p53 tumor
CC       suppressor and core histones including H1, H2A, H2B, H3 and H4.
CC       Binds to an upstream initiator-like sequence in the
CC       preprodynorphin gene (By similarity). Regulates neural
CC       differentiation and proliferation by catalyzing the
CC       polyubiquitination and degradation of MYCN. May regulate abundance
CC       of CDC6 after DNA damage by polyubiquitinating and targeting CDC6
CC       to degradation (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with isoform p19ARF of CDKN2A which strongly
CC       inhibits HUWE1 ubiquitin ligase activity (By similarity).
CC       Interacts with MYCN and CDC6 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Mainly expressed in
CC       the cytoplasm of most tissues, except in the nucleus of
CC       spermatogonia, primary spermatocytes and neuronal cells.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q7TMY8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TMY8-2; Sequence=VSP_011147, VSP_011148;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q7TMY8-3; Sequence=VSP_011149;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q7TMY8-4; Sequence=VSP_011150, VSP_011151;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- DEVELOPMENTAL STAGE: Expression increases during neuronal
CC       differentation such that the cortical plate contains the highest
CC       level.
CC   -!- DOMAIN: The HECT domain mediates inhibition of the transcriptional
CC       activity of p53 (By similarity).
CC   -!- PTM: Phosphorylated on tyrosine; phosphorylation is probably
CC       required for its ability to inhibit TP53 transactivation (By
CC       similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 HECT (E6AP-type E3 ubiquitin-protein
CC       ligase) domain.
CC   -!- SIMILARITY: Contains 1 UBA domain.
CC   -!- SIMILARITY: Contains 1 UIM (ubiquitin-interacting motif) repeat.
CC   -!- SIMILARITY: Contains 1 WWE domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AY772010; AAV90839.3; -; mRNA.
DR   EMBL; AY929611; AAX24124.1; -; mRNA.
DR   EMBL; AB093227; BAC41411.2; -; mRNA.
DR   EMBL; BC011391; AAH11391.1; -; mRNA.
DR   EMBL; BC017642; AAH17642.2; -; mRNA.
DR   EMBL; BC054372; AAH54372.1; -; mRNA.
DR   EMBL; BC070444; AAH70444.1; -; mRNA.
DR   EMBL; AK083499; BAC38936.1; -; mRNA.
DR   EMBL; AB025966; BAA84697.1; -; mRNA.
DR   IPI; IPI00453613; -.
DR   IPI; IPI00453615; -.
DR   IPI; IPI00463909; -.
DR   IPI; IPI00655012; -.
DR   RefSeq; NP_067498.4; NM_021523.4.
DR   UniGene; Mm.27372; -.
DR   ProteinModelPortal; Q7TMY8; -.
DR   SMR; Q7TMY8; 1310-1356, 4003-4369.
DR   IntAct; Q7TMY8; 1.
DR   STRING; Q7TMY8; -.
DR   PhosphoSite; Q7TMY8; -.
DR   PRIDE; Q7TMY8; -.
DR   Ensembl; ENSMUST00000112622; ENSMUSP00000108241; ENSMUSG00000025261.
DR   GeneID; 59026; -.
DR   KEGG; mmu:59026; -.
DR   CTD; 59026; -.
DR   MGI; MGI:1926884; Huwe1.
DR   HOVERGEN; HBG080254; -.
DR   ArrayExpress; Q7TMY8; -.
DR   Bgee; Q7TMY8; -.
DR   CleanEx; MM_HUWE1; -.
DR   Genevestigator; Q7TMY8; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0016574; P:histone ubiquitination; ISS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR010309; E3_Ub_ligase_DUF908.
DR   InterPro; IPR010314; E3_Ub_ligase_DUF913.
DR   InterPro; IPR000569; HECT.
DR   InterPro; IPR009060; UBA-like.
DR   InterPro; IPR000449; UBA/transl_elong_EF1B_N.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   InterPro; IPR004170; WWE-dom.
DR   Pfam; PF06012; DUF908; 1.
DR   Pfam; PF06025; DUF913; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00627; UBA; 1.
DR   Pfam; PF02825; WWE; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF56204; HECT; 1.
DR   SUPFAM; SSF46934; UBA_like; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS50030; UBA; 1.
DR   PROSITE; PS50330; UIM; FALSE_NEG.
DR   PROSITE; PS50918; WWE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Differentiation;
KW   Direct protein sequencing; DNA-binding; Ligase; Nucleus;
KW   Phosphoprotein; Ubl conjugation pathway.
FT   CHAIN         1   4377       E3 ubiquitin-protein ligase HUWE1.
FT                                /FTId=PRO_0000120341.
FT   DOMAIN     1316   1355       UBA.
FT   REPEAT     1370   1389       UIM.
FT   DOMAIN     1603   1680       WWE.
FT   DOMAIN     4041   4377       HECT.
FT   COMPBIAS   2295   2469       Glu-rich.
FT   COMPBIAS   2427   2490       Asp-rich.
FT   COMPBIAS   3484   3552       Thr-rich.
FT   ACT_SITE   4344   4344       Glycyl thioester intermediate (By
FT                                similarity).
FT   MOD_RES     509    509       N6-acetyllysine (By similarity).
FT   MOD_RES    1084   1084       Phosphoserine (By similarity).
FT   MOD_RES    1368   1368       Phosphoserine (By similarity).
FT   MOD_RES    1370   1370       Phosphoserine (By similarity).
FT   MOD_RES    1395   1395       Phosphoserine (By similarity).
FT   MOD_RES    1840   1840       N6-acetyllysine (By similarity).
FT   MOD_RES    1903   1903       Phosphoserine (By similarity).
FT   MOD_RES    1907   1907       Phosphoserine.
FT   MOD_RES    2248   2248       N6-acetyllysine (By similarity).
FT   MOD_RES    2362   2362       Phosphoserine (By similarity).
FT   MOD_RES    2365   2365       Phosphoserine (By similarity).
FT   MOD_RES    2366   2366       Phosphothreonine (By similarity).
FT   MOD_RES    2377   2377       Phosphoserine (By similarity).
FT   MOD_RES    2391   2391       Phosphoserine (By similarity).
FT   MOD_RES    2526   2526       Phosphoserine (By similarity).
FT   MOD_RES    2595   2595       Phosphoserine (By similarity).
FT   MOD_RES    2619   2619       Phosphoserine (By similarity).
FT   MOD_RES    2746   2746       Phosphothreonine (By similarity).
FT   MOD_RES    2751   2751       Phosphothreonine (By similarity).
FT   MOD_RES    2887   2887       Phosphoserine (By similarity).
FT   MOD_RES    2888   2888       Phosphoserine (By similarity).
FT   MOD_RES    2889   2889       Phosphothreonine (By similarity).
FT   MOD_RES    2918   2918       Phosphoserine (By similarity).
FT   MOD_RES    3116   3116       Phosphoserine (By similarity).
FT   MOD_RES    3374   3374       Phosphoserine (By similarity).
FT   MOD_RES    3378   3378       Phosphoserine (By similarity).
FT   MOD_RES    3663   3663       Phosphoserine (By similarity).
FT   MOD_RES    3753   3753       Phosphoserine (By similarity).
FT   MOD_RES    3758   3758       Phosphoserine.
FT   MOD_RES    3760   3760       Phosphoserine (By similarity).
FT   MOD_RES    3798   3798       Phosphoserine (By similarity).
FT   MOD_RES    3810   3810       Phosphoserine.
FT   MOD_RES    3818   3818       Phosphoserine (By similarity).
FT   MOD_RES    3824   3824       Phosphothreonine (By similarity).
FT   MOD_RES    3922   3922       Phosphoserine (By similarity).
FT   MOD_RES    3927   3927       Phosphothreonine (By similarity).
FT   MOD_RES    3930   3930       Phosphothreonine (By similarity).
FT   MOD_RES    4274   4274       Phosphotyrosine (By similarity).
FT   VAR_SEQ    3347   3364       FPSHFTQQRTKETNCESD -> RSLKESLTPGFFGHQHLG
FT                                (in isoform 2).
FT                                /FTId=VSP_011147.
FT   VAR_SEQ    3365   4377       Missing (in isoform 2).
FT                                /FTId=VSP_011148.
FT   VAR_SEQ    3780   3794       Missing (in isoform 3).
FT                                /FTId=VSP_011149.
FT   VAR_SEQ    3795   3832       SESSNQSETSVRREESPMDVDQPSPSAQDTQSIVISDG ->
FT                                VSMMPVAPHSFLYPPSCTMSSVGVHCPYLVCFCITFAK
FT                                (in isoform 4).
FT                                /FTId=VSP_011150.
FT   VAR_SEQ    3833   4377       Missing (in isoform 4).
FT                                /FTId=VSP_011151.
FT   CONFLICT   1728   1728       S -> I (in Ref. 2 and 4).
FT   CONFLICT   2032   2032       E -> EG (in Ref. 2 and 4).
SQ   SEQUENCE   4377 AA;  482663 MW;  11A1F7C7E630C983 CRC64;
     MKVDRTKLKK TPTEAPADCR ALIDKLKVCN DEQLLLELQQ IKTWNIGKCE LYHWVDLLDR
     FDGILADAGQ TVENMSWMLV CDRPEKEQLK MLLLAVLNFT ALLIEYSFSR HLYSSIEHLT
     TLLASSDMQV VLAVLNLLYV FSKRSNYITR LGSDKRTPLL TRLQHLAESW GGKENGFGLA
     ECCRDLQMLK YPPSATTLHF EFYADPGAEV KIEKRTTSNT LHYIHIEQLD KISESPSEIM
     ESLTKMYSIP KDRQMLLFTH IRLAHGFSNH RKRLQAVQAR LHAISILVYS NALQESANSI
     LYNGLIEELV DVLQITDKQL MEIKAASLRT LTSIVHLERT PKLSSIIDCT GTASYHGFLP
     VLVRNCIQAM IDPSMDPYPH QFATALFSFL YHLASYDAGG EALVSCGMME ALLKVIKFLG
     DEQDQITFVT RAVRVVDLIT NLDMAAFQSH SGLSIFIYRL EHEVDLCRKE CPFVIKPKIQ
     RPSTTQEGEE METDMDGVQC IPQRAALLKS MLNFLKKAIQ DPAFSDGIRH VMDGSLPTSL
     KHIISNAEYY GPSLFLLATE VVTVFVFQEP SLLSSLQDNG LTDVMLHALL IKDVPATREV
     LGSLPNVFSA LCLNARGLQS FVQCQPFERL FKVLLSPDYL PAMRRRRSSD PLGDTASNLG
     SAVDELMRHQ PTLKTDATTA IIKLLEEICN LGRDPKYICQ KPSIQKADGT ATAPPPRSNH
     AAEEASSEDE EEEEVQAMQS FNSAQQNETE PNQQVVGTEE RIPIPLMDYI LNVMKFVESI
     LSNNTTDDHC QEFVNQKGLL PLVTILGLPN LPIDFPTSAA CQAVAGVCKS ILTLSHEPKV
     LQEGLLQLDL ILSSLEPLHR PIESPGGSVL LRELACAGNV ADATLSAQAT PLLHALTAAH
     AYIMMFVHTC RVGQSEIRSI SVNQWGSQLG LSVLSKLSQL YCSLVWESTV LLSLCTPNSL
     PSGCEFGQAD MQKLVPKDEK AGTTQGGKRS DGEQDGTAGS MDASAQGLLE GIELDGDTLA
     PMETDEPSSS DSKGKSKITP AMAARIKQIK PLLSASSRLG RALAELFGLL VKLCVGSPVR
     QRRSHHAAST TTAPTPAARS TASALTKLLT KGLSWQPPPY TPTPRFRLTF FICSVGFTSP
     MLFDERKYPY HLMLQKFLCS GGHNALFETF NWALSMGGKV PVSEGLEHSD LPDGTGEFLD
     AWLMLVEKMV NPTTVLESPH SLPAKLPGGV QSFPQFSALR FLVVTQKAAF TCIKNLWNRK
     PLKVYGGRMA ESMLAILCHI LRGEPVIRER LSKEKEGSRG EEEAGQEEGG SRREPQVNQQ
     QLQQLMDMGF TREHAMEALL NTSTMEQATE YLLTHPPPII GGVVRDLSMS EEDQMMRAIA
     MSLGQDIPMD QRAESPEEVA CRKEEEERKA REKQEEEEAK CLEKFQDADP LEQDELHTFT
     DTMLPGCFHL LDELPDTVYR VCDLIMTAIK RNGADYRDMI LKQVVNQVWE AADVLIKAAL
     PLTTSDTKTV SEWISQMATL PQASNLATRI LLLTLLFEEL KLPCAWVVES SGILNVLIKL
     LEVVQPCLQA AKEQKEVQTP KWITPVLLLI DFYEKTAISS KRRAQMTKYL QSNSNNWRWF
     DDRSGRWCSY SASNNSTIDS AWKSGETSVR FTAGRRRYTV QFTTMVQVNE ETGNRRPVML
     TLLRVPRLSK NSKSSNGQEL EKTLEESKET DIKHKENKGN DIPLALESTN TEKEASLDET
     KIGEILIQGL TEDMVTVLIR ACVSMLGVPV DPDTLHATLR LCLRLTRDHK YAMMFAELKS
     TRMILNLTQS SGFNGFTPLV TLLLRHIIED PCTLRHTMEK VVRSAATSGA GSTTSGVVSG
     SLGSREINYI LRVLGPAACR NPDIFTEVAN CCIRIALPAP RGSGTASDDE FENLRIKGPN
     AVQLVKTTPL KPSSLPVIPD TIKEVIYDML NALAAYHAPE EADKSDPKPG GTTQEVGQLL
     QDMGDDVYQQ YRSLTRQSSD FDTQSGFSLN SQVFAADGAP AETSTTGTSQ GEASTPEETR
     EGKKDKEGDR TSEEGKQKSK GSKPLMPTST ILRLLAELVR SYVGIATLIA NYSYTVGQSE
     LIKEDCSVLA FVLDHLLPHT QNAEDKDTPA LARLFLASLA AAGSGTDAQV ALVNEVKAAL
     GRALAMAEST EKHARLQAVM CIISTIMESC PSTSSFYSSA TAKTQHNGMN NIIRLFLKKG
     LVNDLARVPH SLDLSSPNMA NTVNAALKPL ETLSRIVNQP SSLFGSKSAS SKNKSEQDAQ
     GASQDSSSHQ QDPGEPGEAE VQEEDHDVTQ TEVADGDIMD GEAETDSVVI AGQPEVLSSQ
     EMQVENELED LIDELLERDG GSGNSTIIVS RSGEDESQED VLMDEAPSNL SQASTLQANR
     EDSMNILDPE DEEEHTQEED SSGSNEDEDD SQDEEEEEEE DEEDDQEDDE GEEGDEDDDD
     DGSEMELDED YPDMNASPLV RFERFDREDD LIIEFDNMFS SATDIPPSPG NIPTTHPLMV
     RHADHSSLTL GSGSSTTRLT QGIGRSQRTL RQLTANTGHT IHVHYPGNRQ PNPPLILQRL
     LGPSAAADIL QLSSSLPLQS RGRARLLVGN DDVHIIARSD DELLDDFFHD QSTATSQAGT
     LSSIPTALTR WTEECKVLDA ESMHDCVSVV KVPIVNHLEF LRDEELEERR EKRRKQLAEE
     ETKIIDKGKE DKENRDQSAQ CTVTKTNDST EQNVSDGTPM PDSYPTTPSS TDAPTSESKE
     TLGTLQPSQQ QPALPPPPSL GEIPQELQSP AEEVANSTQL LMPIELEELG PTRPSGEAET
     TQMELSPAPT ITSLSPERAE DSDALTAVSS QLEGSPMDTS SLASCTLEEA VGDTPAAGSS
     EQPTAGSSTP GDAPSVVAEV QGRPDVSRES NQPPEDSSPP ASSESSSTRD SAVAISGADS
     RGILEEPLPS TSSEEEDPLA GISLPEGVDP SFLAALPDDI RREVLQNQLG IRPPTRSAPS
     SNSSAPAVVG NPGVTEVSPE FLAALPPAIQ EEVLAQQRAE QQRRELAQNA SSDTPMDPVT
     FIQTLPSDLR RSVLEDMEDS VLAVMPPDIA AEAQALRREQ EARQRQLMHE RLFGHSSTSA
     LSAILRSPAF TSRLSGNRGV QYTRLAVQRG GTFQMGGSSS HNRPSGSNVD TLLRLRGRLL
     LDHEALSCLL VLLFVDEPKL NTSRLHRVLR NLCYHAQTRH WVIRSLLSIL QRSSESELCI
     ETPKLSTSEE RGKKSSKSCA SSSHENRPLD LLHKMESKSS NQLSWLSVSM DAALGCRTNI
     FQIQRSGGRK HTEKHASSGS TVHIHPQAAP VVCRHVLDTL IQLAKVFPSH FTQQRTKETN
     CESDRERGSK QACSPCSSQS SSSGICTDFW DLLVKLDNMN VSRKGKNSVK SVPVSSGGEG
     ETSPHSLEAS PLGQLMNMLS HPVIRRSSLL TEKLLRLLSL ISIALPENKV SEVQTNSSNS
     GSSTAATSNT STTTTTTTTA TAPTPTPPAA TTPVTSAPAL VAATAISTIT VAASTTVTTP
     TTATTTVSTS TTKGSKSPAK VGEGGSGIDF KMVSSGLTEN QLQLSVEVLT SHSCSEEGLE
     DAANVLLQLS RGDSGTRDTV LKLLLNGARH LGYTLCKQIG TLLAELREYN LEQQRRAQCE
     TLSPDGLPEE QPQTTKLKGK MQSRFDMAEN VVIVASQKRP LGGRELQLPS MSMLTSKTST
     QKFFLRVLQV IIQLRDDTRR ANKKAKQTGR LGSSGLGSAS SIQAAVRQLE AEADAIIQMV
     REGQRARRQQ QAATSESSNQ SETSVRREES PMDVDQPSPS AQDTQSIVIS DGTPQGEKEK
     EEKPPELPLL SEQLSLDELW DMLGECLKEL EESHDQHAVL VLQPAVEAFF LVHATERESK
     PPVRDTRESQ LAHIKDEPPP LSPAPLTPAT PSSLDPFFSR EPSSMHISSS LPPDTQKFLR
     FAETHRTVLN QILRQSTTHL ADGPFAVLVD YIRVLDFDVK RKYFRQELER LDEGLRKEDM
     AVHVRRDHVF EDSYRELHRK SPEEMKNRLY IVFEGEEGQD AGGLLREWYM IISREMFNPM
     YALFRTSPGD RVTYTINPSS HCNPNHLSYF KFVGRIVAKA VYDNRLLECY FTRSFYKHIL
     GKSVRYTDME SEDYHFYQGL VYLLENDVST LGYDLTFSTE VQEFGVCEVR DLKPNGANIL
     VTEENKKEYV HLVCQMRMTG AIRKQLAAFL EGFYEIIPKR LISIFTEQEL ELLISGLPTI
     DIDDLKSNTE YHKYQSNSIQ IQWFWRALRS FDQADRAKFL QFVTGTSKVP LQGFAALEGM
     NGIQKFQIHR DDRSTDRLPS AHTCFNQLDL PAYESFEKLR HMLLLAIQEC SEGFGLA
//
ID   SMAP2_MOUSE             Reviewed;         428 AA.
AC   Q7TN29; Q3U798;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Stromal membrane-associated protein 2;
DE   AltName: Full=Stromal membrane-associated protein 1-like;
GN   Name=Smap2; Synonyms=Smap1l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Fetal brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   FUNCTION, INTERACTION WITH ARF1; PICALM AND CLATHRIN HEAVY CHAINS,
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-56; 187-LEU--ASP-191 AND
RP   212-ASP--LEU-214.
RX   PubMed=16571680; DOI=10.1091/mbc.E05-10-0909;
RA   Natsume W., Tanabe K., Kon S., Yoshida N., Watanabe T., Torii T.,
RA   Satake M.;
RT   "SMAP2, a novel ARF GTPase-activating protein, interacts with clathrin
RT   and clathrin assembly protein and functions on the AP-1-positive early
RT   endosome/trans-Golgi network.";
RL   Mol. Biol. Cell 17:2592-2603(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: GTPase activating protein that acts on ARF1. Can also
CC       activate ARF6 (in vitro). May play a role in clathrin-dependent
CC       retrograde transport from early endosomes to the trans-Golgi
CC       network.
CC   -!- SUBUNIT: Interacts with ARF1. Interacts with PICALM and clathrin
CC       heavy chains.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Detected in multiple foci
CC       throughout the cytoplasm and in juxtanuclear structures.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7TN29-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TN29-2; Sequence=VSP_018505, VSP_018506;
CC   -!- SIMILARITY: Contains 1 Arf-GAP domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK152757; BAE31472.1; -; mRNA.
DR   EMBL; BC052413; AAH52413.1; -; mRNA.
DR   IPI; IPI00655222; -.
DR   IPI; IPI00756510; -.
DR   RefSeq; NP_598477.2; NM_133716.3.
DR   UniGene; Mm.271819; -.
DR   ProteinModelPortal; Q7TN29; -.
DR   SMR; Q7TN29; 10-131.
DR   STRING; Q7TN29; -.
DR   PhosphoSite; Q7TN29; -.
DR   PRIDE; Q7TN29; -.
DR   Ensembl; ENSMUST00000043200; ENSMUSP00000035800; ENSMUSG00000032870.
DR   GeneID; 69780; -.
DR   KEGG; mmu:69780; -.
DR   UCSC; uc008unw.1; mouse.
DR   CTD; 69780; -.
DR   MGI; MGI:1917030; Smap2.
DR   GeneTree; ENSGT00530000062917; -.
DR   HOGENOM; HBG714275; -.
DR   HOVERGEN; HBG055260; -.
DR   InParanoid; Q7TN29; -.
DR   OMA; GMNFCGA; -.
DR   OrthoDB; EOG4868DC; -.
DR   PhylomeDB; Q7TN29; -.
DR   NextBio; 330318; -.
DR   ArrayExpress; Q7TN29; -.
DR   Bgee; Q7TN29; -.
DR   Genevestigator; Q7TN29; -.
DR   GermOnline; ENSMUSG00000032870; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR   InterPro; IPR001164; ArfGAP.
DR   Pfam; PF01412; ArfGap; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SUPFAM; SSF57863; ArfGAP; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; GTPase activation; Metal-binding;
KW   Phosphoprotein; Zinc; Zinc-finger.
FT   CHAIN         1    428       Stromal membrane-associated protein 2.
FT                                /FTId=PRO_0000235842.
FT   DOMAIN       13    139       Arf-GAP.
FT   ZN_FING      28     51       C4-type.
FT   REGION      163    231       Interaction with clathrin heavy chains.
FT   REGION      339    428       Interaction with PICALM.
FT   COMPBIAS    278    410       Met-rich.
FT   MOD_RES     219    219       Phosphoserine.
FT   MOD_RES     224    224       Phosphoserine (By similarity).
FT   MOD_RES     239    239       Phosphoserine.
FT   VAR_SEQ     227    245       AVGSMPTAGSAGSVPENLN -> SQGANQKKQARNSSPRTP
FT                                S (in isoform 2).
FT                                /FTId=VSP_018505.
FT   VAR_SEQ     246    428       Missing (in isoform 2).
FT                                /FTId=VSP_018506.
FT   MUTAGEN      56     56       R->Q: Loss of GTPase activation.
FT   MUTAGEN     187    191       LLGLD->AAAAA: Loss of interaction with
FT                                clathrin heavy chains; when associated
FT                                with 212-AAA-214.
FT   MUTAGEN     212    214       DLL->AAA: Loss of interaction with
FT                                clathrin heavy chains; when associated
FT                                with 187-AAAAA-191.
FT   CONFLICT     89     89       A -> V (in Ref. 2; AAH52413).
FT   CONFLICT    179    179       K -> E (in Ref. 2; AAH52413).
SQ   SEQUENCE   428 AA;  46578 MW;  5F27D6677C3B1AAF CRC64;
     MTGKSVKDVD RYQAVLANLL LEEDNKFCAD CQSKGPRWAS WNIGVFICIR CAGIHRNLGV
     HISRVKSVNL DQWTQEQIQC MQEMGNGKAN RLYEAYLPET FRRPQIDPAV EGFIRDKYEK
     KKYMDRSLDI NVLRKEKDDK WKRGNEPAPE KKMEPVVFEK VKMPQKKEDA QLPRKSSPKS
     AAPVMDLLGL DAPVACSIAN SKTSNALEKD LDLLASVPSP SSVSRKAVGS MPTAGSAGSV
     PENLNLFPEP GSKSEETGKK QLSKDSILSL YGSQTPQMPA QAMFMAPAQM AYPTAYPSFP
     GVTPPNSIMG GMVPPPVGMV AQPGASGMLT PMAMPAGYMG GMQASMMGVP NGMMTTQQAG
     YMASMAAMPQ TVYGVQPAQQ LQWNLTQMTQ QMAGMNFYGA NGMMNYGQSM GGGNGQAANQ
     TLSPQMWK
//
ID   CELF6_MOUSE             Reviewed;         460 AA.
AC   Q7TN33; Q8BJ35;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=CUGBP Elav-like family member 6;
DE            Short=CELF-6;
DE   AltName: Full=Bruno-like protein 6;
DE   AltName: Full=CUG-BP- and ETR-3-like factor 6;
DE   AltName: Full=RNA-binding protein BRUNOL-6;
GN   Name=Celf6; Synonyms=Brunol6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: RNA-binding protein implicated in the regulation of pre-
CC       mRNA alternative splicing. Mediates exon inclusion and/or
CC       exclusion in pre-mRNA that are subject to tissue-specific and
CC       developmentally regulated alternative splicing. Specifically
CC       activates exon 5 inclusion of TNNT2 in a muscle-specific splicing
CC       enhancer (MSE)-dependent manner. Promotes also exon exclusion of
CC       INSR pre-mRNA (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7TN33-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TN33-2; Sequence=VSP_026849;
CC   -!- SIMILARITY: Belongs to the CELF/BRUNOL family.
CC   -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK034216; BAC28635.1; -; mRNA.
DR   EMBL; BC052406; AAH52406.1; -; mRNA.
DR   EMBL; BC057083; AAH57083.1; -; mRNA.
DR   IPI; IPI00222250; -.
DR   IPI; IPI00853853; -.
DR   RefSeq; NP_780444.2; NM_175235.3.
DR   UniGene; Mm.265415; -.
DR   HSSP; Q92879; 2CPZ.
DR   ProteinModelPortal; Q7TN33; -.
DR   SMR; Q7TN33; 31-217, 351-458.
DR   PRIDE; Q7TN33; -.
DR   Ensembl; ENSMUST00000034840; ENSMUSP00000034840; ENSMUSG00000032297.
DR   GeneID; 76183; -.
DR   KEGG; mmu:76183; -.
DR   UCSC; uc009pxx.1; mouse.
DR   CTD; 76183; -.
DR   MGI; MGI:1923433; Celf6.
DR   eggNOG; maNOG19186; -.
DR   GeneTree; ENSGT00560000076837; -.
DR   HOVERGEN; HBG107646; -.
DR   OMA; GHIEECT; -.
DR   OrthoDB; EOG4RJG30; -.
DR   PhylomeDB; Q7TN33; -.
DR   NextBio; 344727; -.
DR   ArrayExpress; Q7TN33; -.
DR   Bgee; Q7TN33; -.
DR   CleanEx; MM_BRUNOL6; -.
DR   Genevestigator; Q7TN33; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 3.
DR   Pfam; PF00076; RRM_1; 3.
DR   SMART; SM00360; RRM; 3.
DR   PROSITE; PS50102; RRM; 3.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; mRNA processing; Nucleus; Repeat;
KW   RNA-binding.
FT   CHAIN         1    460       CUGBP Elav-like family member 6.
FT                                /FTId=PRO_0000295230.
FT   DOMAIN       46    127       RRM 1.
FT   DOMAIN      134    214       RRM 2.
FT   DOMAIN      375    453       RRM 3.
FT   COMPBIAS    242    294       Ala-rich.
FT   VAR_SEQ       1    115       Missing (in isoform 2).
FT                                /FTId=VSP_026849.
SQ   SEQUENCE   460 AA;  48206 MW;  D032BA0FFE8C67C6 CRC64;
     MAAAPGGSAP PAGPSPRLAF STADSGGGMS GLNPGPAVPM KDHDAIKLFV GQIPRGLDEQ
     DLKPLFEEFG RIYELTVLKD RLTGLHKGCA FLTYCARDSA LKAQSALHEQ KTLPGMNRPI
     QVKPAASEGR GEDRKLFVGM LGKQQGEEDV RRLFQPFGHI EECTVLRSPD GTSKGCAFVK
     FGSQGEAQAA IQGLHGSRTM TGASSSLVVK LADTDRERAL RRMQQMAGQL GAFHPAPLPL
     GACGAYTTAI LQHQAALLAA AQGPGLGQVA AVAAQMQHVA AFSLVAAPLL PAAANTSPGG
     NGPGALPGLP APMGVNGFGS LTPQSNGQPG SDTLYNNGVS PYPAAYPSAY APASTAFSQQ
     PSALPQQQRE GPEGCNLFIY HLPQEFGDAE LIQTFLPFGA VVSAKVFVDR ATNQSKCFGF
     VSFDNPTSAQ TAIQAMNGFQ IGMKRLKVQL KRPKDANRPY
//
ID   CPEB4_MOUSE             Reviewed;         729 AA.
AC   Q7TN98; A6H6G0; Q69ZD7;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=Cytoplasmic polyadenylation element-binding protein 4;
DE            Short=CPE-BP4;
DE            Short=CPE-binding protein 4;
DE            Short=mCPEB-4;
GN   Name=Cpeb4; Synonyms=Kiaa1673;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), ALTERNATIVE
RP   SPLICING, INDUCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=22784672; PubMed=12871996; DOI=10.1073/pnas.1133424100;
RA   Theis M., Si K., Kandel E.R.;
RT   "Two previously undescribed members of the mouse CPEB family of genes
RT   and their inducible expression in the principal cell layers of the
RT   hippocampus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:9602-9607(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1; Synonyms=mCPEB-4a;
CC         IsoId=Q7TN98-1; Sequence=Displayed;
CC       Name=2; Synonyms=mCPEB-4b;
CC         IsoId=Q7TN98-2; Sequence=VSP_022046;
CC       Name=3; Synonyms=mCPEB-4c;
CC         IsoId=Q7TN98-3; Sequence=VSP_022044;
CC       Name=4; Synonyms=mCPEB-4d;
CC         IsoId=Q7TN98-4; Sequence=VSP_022043;
CC       Name=5;
CC         IsoId=Q7TN98-5; Sequence=VSP_022045;
CC   -!- TISSUE SPECIFICITY: Strongly expressed in kidney, lung and heart.
CC       Weakly expressed in liver, spleen, ovary and in granular cells of
CC       dentate gyrus and the pyramidal cells of CA3 and CA1 of the
CC       hippocampus.
CC   -!- INDUCTION: Up-regulated in granular cells of the dentate gyrus of
CC       CA1 and CA3 after kainate-induced seizures.
CC   -!- SIMILARITY: Belongs to the RRM CPEB family.
CC   -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY313775; AAQ20844.1; -; mRNA.
DR   EMBL; AK173229; BAD32507.1; -; mRNA.
DR   EMBL; BC115430; AAI15431.1; -; mRNA.
DR   EMBL; BC115431; AAI15432.1; -; mRNA.
DR   EMBL; BC145863; AAI45864.1; -; mRNA.
DR   EMBL; BC145865; AAI45866.1; -; mRNA.
DR   IPI; IPI00454005; -.
DR   IPI; IPI00620866; -.
DR   IPI; IPI00816891; -.
DR   IPI; IPI00816970; -.
DR   IPI; IPI00816984; -.
DR   RefSeq; NP_080528.2; NM_026252.3.
DR   UniGene; Mm.339792; -.
DR   ProteinModelPortal; Q7TN98; -.
DR   SMR; Q7TN98; 471-659.
DR   STRING; Q7TN98; -.
DR   PhosphoSite; Q7TN98; -.
DR   PRIDE; Q7TN98; -.
DR   Ensembl; ENSMUST00000020543; ENSMUSP00000020543; ENSMUSG00000020300.
DR   Ensembl; ENSMUST00000093220; ENSMUSP00000090908; ENSMUSG00000020300.
DR   Ensembl; ENSMUST00000109412; ENSMUSP00000105039; ENSMUSG00000020300.
DR   Ensembl; ENSMUST00000109413; ENSMUSP00000105040; ENSMUSG00000020300.
DR   GeneID; 67579; -.
DR   KEGG; mmu:67579; -.
DR   UCSC; uc007iiq.1; mouse.
DR   UCSC; uc007iir.1; mouse.
DR   UCSC; uc007iis.1; mouse.
DR   CTD; 67579; -.
DR   MGI; MGI:1914829; Cpeb4.
DR   HOGENOM; HBG506657; -.
DR   HOVERGEN; HBG058010; -.
DR   InParanoid; Q7TN98; -.
DR   OMA; AHNIQDE; -.
DR   OrthoDB; EOG4JM7P9; -.
DR   PhylomeDB; Q7TN98; -.
DR   NextBio; 324961; -.
DR   ArrayExpress; Q7TN98; -.
DR   Bgee; Q7TN98; -.
DR   Genevestigator; Q7TN98; -.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Phosphoprotein; Repeat; RNA-binding.
FT   CHAIN         1    729       Cytoplasmic polyadenylation element-
FT                                binding protein 4.
FT                                /FTId=PRO_0000269265.
FT   DOMAIN      472    563       RRM 1.
FT   DOMAIN      580    662       RRM 2.
FT   COMPBIAS    232    246       His-rich.
FT   COMPBIAS    302    310       Poly-Gly.
FT   MOD_RES      97     97       Phosphoserine (By similarity).
FT   MOD_RES      99     99       Phosphoserine (By similarity).
FT   MOD_RES     252    252       Phosphoserine (By similarity).
FT   MOD_RES     255    255       Phosphoserine (By similarity).
FT   MOD_RES     326    326       Phosphothreonine (By similarity).
FT   MOD_RES     332    332       Phosphoserine (By similarity).
FT   VAR_SEQ     402    427       Missing (in isoform 4).
FT                                /FTId=VSP_022043.
FT   VAR_SEQ     402    419       Missing (in isoform 3).
FT                                /FTId=VSP_022044.
FT   VAR_SEQ     404    428       Missing (in isoform 5).
FT                                /FTId=VSP_022045.
FT   VAR_SEQ     420    427       Missing (in isoform 2).
FT                                /FTId=VSP_022046.
SQ   SEQUENCE   729 AA;  80122 MW;  7CB042EDE4B7C0CA CRC64;
     MGDYGFGVLV QSNTGNKSAF PVRFHPHLQP PHHHQNATPN PAAFINNNTA ANGSSAGSAW
     LFPAPATHNI QDEILGSEKA KSQQQEQQDP LEKQQLSPSP GQEAGILPET EKAKAEENPG
     DSSSENSNGK EKLRIESPVL TGFDYQEATG LGTSTQPLTS SASSLTGFSN WSAAIAPSSS
     TIINEDASFF HQGGVPGASA NNGALLFQNF PHHVSPGFGG SFSPQIGPLS QHHPHHPHFQ
     HHHSQHQQQR RSPASPHPPP FTHRSAAFNQ LPHLANNLNK PPSPWSSYQS PSPTPSSSWS
     PGGGGYGGWG ASQGRDHRRG LNGGITPLNS ISPLKKNFAS NHIQLQKYAR PSSAFAPKSW
     MEDSLNRADN IFPFPERPRT FDMHSLESSL IDIMRAENDS IKGRLNYSYP GSDSSLLINA
     RTYGRRRGQS SLFPMEDGFL DDGRGDQPLH SGLGSPHCFT HQNGERVERY SRKVFVGGLP
     PDIDEDEITA SFRRFGPLIV DWPHKAESKS YFPPKGYAFL LFQDESSVQA LIDACIEEDG
     KLYLCVSSPT IKDKPVQIRP WNLSDSDFVM DGSQPLDPRK TIFVGGVPRP LRAVELAMIM
     DRLYGGVCYA GIDTDPELKY PKGAGRVAFS NQQSYIAAIS ARFVQLQHGE IDKRVEVKPY
     VLDDQLCDEC QGARCGGKFA PFFCANVTCL QYYCEYCWAA IHSRAGREFH KPLVKEGGDR
     PRHISFRWN
//
ID   CPEB3_MOUSE             Reviewed;         716 AA.
AC   Q7TN99; Q3TT89; Q3UHR6; Q8CHC2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Cytoplasmic polyadenylation element-binding protein 3;
DE            Short=CPE-BP3;
DE            Short=CPE-binding protein 3;
DE            Short=mCPEB-3;
GN   Name=Cpeb3; Synonyms=Kiaa0940;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), INDUCTION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=22784672; PubMed=12871996; DOI=10.1073/pnas.1133424100;
RA   Theis M., Si K., Kandel E.R.;
RT   "Two previously undescribed members of the mouse CPEB family of genes
RT   and their inducible expression in the principal cell layers of the
RT   hippocampus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:9602-9607(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1; Synonyms=mCPEB-3a;
CC         IsoId=Q7TN99-1; Sequence=Displayed;
CC       Name=2; Synonyms=mCPEB-3b;
CC         IsoId=Q7TN99-2; Sequence=VSP_022037;
CC       Name=3; Synonyms=mCPEB-3c;
CC         IsoId=Q7TN99-3; Sequence=VSP_022036;
CC       Name=4; Synonyms=mCPEB-3d;
CC         IsoId=Q7TN99-4; Sequence=VSP_022036, VSP_022037;
CC       Name=5;
CC         IsoId=Q7TN99-5; Sequence=VSP_022036, VSP_022038, VSP_022039;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and heart, less in
CC       liver, kidney, embryo, skeletal muscle, lung and ovary. Weakly
CC       expressed in granular cells of dentate gyrus and the pyramidal
CC       cells of CA3 and CA1 of the hippocampus.
CC   -!- INDUCTION: Up-regulated in granular cells of the dentate gyrus and
CC       the pyramidal cells of CA1 and CA3 after kainate-induced seizures.
CC   -!- SIMILARITY: Belongs to the RRM CPEB family.
CC   -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC41458.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY313774; AAQ20843.1; -; mRNA.
DR   EMBL; AK147243; BAE27791.1; -; mRNA.
DR   EMBL; AK161513; BAE36436.1; -; mRNA.
DR   EMBL; AB093274; BAC41458.1; ALT_INIT; mRNA.
DR   IPI; IPI00229624; -.
DR   IPI; IPI00816841; -.
DR   IPI; IPI00816854; -.
DR   IPI; IPI00816949; -.
DR   IPI; IPI00817036; -.
DR   RefSeq; NP_938042.2; NM_198300.2.
DR   UniGene; Mm.391176; -.
DR   ProteinModelPortal; Q7TN99; -.
DR   SMR; Q7TN99; 458-629.
DR   STRING; Q7TN99; -.
DR   PhosphoSite; Q7TN99; -.
DR   PRIDE; Q7TN99; -.
DR   Ensembl; ENSMUST00000044716; ENSMUSP00000044575; ENSMUSG00000039652.
DR   Ensembl; ENSMUST00000079754; ENSMUSP00000078690; ENSMUSG00000039652.
DR   GeneID; 208922; -.
DR   KEGG; mmu:208922; -.
DR   UCSC; uc008hhy.1; mouse.
DR   UCSC; uc008hhz.1; mouse.
DR   UCSC; uc008hia.1; mouse.
DR   UCSC; uc008hic.1; mouse.
DR   CTD; 208922; -.
DR   MGI; MGI:2443075; Cpeb3.
DR   eggNOG; roNOG05759; -.
DR   GeneTree; ENSGT00390000012886; -.
DR   HOGENOM; HBG506657; -.
DR   HOVERGEN; HBG058010; -.
DR   InParanoid; Q7TN99; -.
DR   OrthoDB; EOG48D0VB; -.
DR   NextBio; 372461; -.
DR   ArrayExpress; Q7TN99; -.
DR   Bgee; Q7TN99; -.
DR   Genevestigator; Q7TN99; -.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein; Repeat; RNA-binding.
FT   CHAIN         1    716       Cytoplasmic polyadenylation element-
FT                                binding protein 3.
FT                                /FTId=PRO_0000269262.
FT   DOMAIN      459    550       RRM 1.
FT   DOMAIN      567    649       RRM 2.
FT   COMPBIAS     13     31       Gln-rich.
FT   COMPBIAS     32    202       Pro-rich.
FT   COMPBIAS    226    236       Poly-Ala.
FT   MOD_RES     194    194       Phosphoserine (By similarity).
FT   MOD_RES     197    197       Phosphoserine.
FT   VAR_SEQ     367    389       Missing (in isoform 3, isoform 4 and
FT                                isoform 5).
FT                                /FTId=VSP_022036.
FT   VAR_SEQ     409    416       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_022037.
FT   VAR_SEQ     581    584       VELA -> GEWK (in isoform 5).
FT                                /FTId=VSP_022038.
FT   VAR_SEQ     585    716       Missing (in isoform 5).
FT                                /FTId=VSP_022039.
FT   CONFLICT    372    372       N -> P (in Ref. 2; BAE27791 and 3;
FT                                BAC41458).
SQ   SEQUENCE   716 AA;  78335 MW;  1FA1D8125FD69819 CRC64;
     MQDDLLMDKS KTQPQSQQQQ RQQQQQQQQL QPEPGAAEAP STPLSSEIPK PEDSSAVPAL
     SPASAPPAPN GPDKMQMESP LLPGLSFHQP PQQPPPPQEP TAPGASLSPS FGSTWSTGTT
     NAVEDSFFQG ITPVNGTMLF QNFPHHVNPV FGGTFSPQIG LAQTQHHQQP PPPAPQPPQP
     AQPPQAQPSQ QRRSPASPSQ APYAQRSAAA YGHQPIMTSK PSSSSAVAAA AAAAAASSAS
     SSWNTHQSVN AAWSAPSNPW GGLQAGRDPR RAVGVGVGVG VGVPSPLNPI SPLKKPFSSN
     VIAPPKFPRA APLTSKSWME DNAFRTDNGN NLLPFQDRSR PYDTFNLHSL ENSLMDMIRT
     DHEPLKGKHY PNSGPPMSFA DIMWRNHFAG RMGINFHHPG TDNIMALNTR SYGRRRGRSS
     LFPFEDAFLD DSHGDQALSS GLSSPTRCQN GERVERYSRK VFVGGLPPDI DEDEITASFR
     RFGPLVVDWP HKAESKSYFP PKGYAFLLFQ EESSVQALID ACLEEDGKLY LCVSSPTIKD
     KPVQIRPWNL SDSDFVMDGS QPLDPRKTIF VGGVPRPLRA VELAMIMDRL YGGVCYAGID
     TDPELKYPKG AGRVAFSNQQ SYIAAISARF VQLQHNDIDK RVEVKPYVLD DQMCDECQGT
     RCGGKFAPFF CANVTCLQYY CEYCWASIHS RAGREFHKPL VKEGGDRPRH VPFRWS
//
ID   KI26B_MOUSE             Reviewed;        2112 AA.
AC   Q7TNC6; Q0VB48; Q8BHX2; Q8BKH6;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Kinesin-like protein KIF26B;
GN   Name=Kif26b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 494-2112.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1274-2112.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (Probable).
CC   -!- SIMILARITY: Belongs to the kinesin-like protein family. KIF26
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 kinesin-motor domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH56349.1; Type=Erroneous initiation;
CC       Sequence=BAC36343.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC117695; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC117756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC117766; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC140776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC056349; AAH56349.1; ALT_INIT; mRNA.
DR   EMBL; AK076435; BAC36343.1; ALT_INIT; mRNA.
DR   IPI; IPI00869465; -.
DR   UniGene; Mm.138659; -.
DR   HSSP; P33173; 1I5S.
DR   ProteinModelPortal; Q7TNC6; -.
DR   SMR; Q7TNC6; 450-806.
DR   PhosphoSite; Q7TNC6; -.
DR   PRIDE; Q7TNC6; -.
DR   Ensembl; ENSMUST00000027771; ENSMUSP00000027771; ENSMUSG00000026494.
DR   UCSC; uc007dvg.1; mouse.
DR   MGI; MGI:2447076; Kif26b.
DR   eggNOG; roNOG14747; -.
DR   GeneTree; ENSGT00530000064038; -.
DR   HOGENOM; HBG444581; -.
DR   HOVERGEN; HBG108063; -.
DR   InParanoid; Q7TNC6; -.
DR   OrthoDB; EOG4QVCB7; -.
DR   NextBio; 392711; -.
DR   ArrayExpress; Q7TNC6; -.
DR   Bgee; Q7TNC6; -.
DR   CleanEx; MM_KIF26B; -.
DR   Genevestigator; Q7TNC6; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   Gene3D; G3DSA:3.40.850.10; kinesin_motor; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_DOMAIN1; FALSE_NEG.
DR   PROSITE; PS50067; KINESIN_MOTOR_DOMAIN2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Microtubule; Motor protein;
KW   Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1   2112       Kinesin-like protein KIF26B.
FT                                /FTId=PRO_0000307302.
FT   DOMAIN      447    739       Kinesin-motor.
FT   NP_BIND     546    553       ATP (Potential).
FT   COMPBIAS     58    126       Gly-rich.
FT   COMPBIAS   1015   1119       Ser-rich.
FT   COMPBIAS   1648   1947       Ser-rich.
FT   MOD_RES    2090   2090       Phosphoserine (By similarity).
FT   CONFLICT   1547   1547       H -> R (in Ref. 3; BAC36343).
FT   CONFLICT   2050   2050       R -> K (in Ref. 3; BAC36343).
SQ   SEQUENCE   2112 AA;  225555 MW;  99BEBF44E7D291D3 CRC64;
     MNSVAGNKER LAVSTRGKKY GVNEMCSPTK PSAPCSPESW YRKAYEESRA GSRPTPEGAG
     SALGSSGTPS PGSGTSSPSS FTGSPGPASP GIGTSSPGSL GGSPGFGTGS PGSGSGGGSS
     PGSDRGVWCE NCNARLVELK RQALKLLLPG PLPGKDPAFS AVIHDKLQVP NTIRKSWNDR
     DNRCDICATH LNQLKQEAIQ MVLTLEQAAG SEHYDTSLGS PPPISSIPTL VGSRHMGGLQ
     QPREWAFVPA PYATSTYTGL VNKHSGKPNS LGVSNGAEKK SGSPTHQAKV SLQMATSPSN
     GNILNSVAIQ AHQYLDGTWS LSRTNGVTLY PYQISQLMTE TGREGLTESA LNRYNADKPA
     ASSVPAPQGS CVASETSTGT SVAASFFARA AQKLNLSSKK KKHRPSTPSV AEAPLFATSF
     SGILQTSPPP APPCLLRAVN KVKDTPGMGK VKVMLRICST SARDTSESSS FLKVDPRKKQ
     ITLYDPLTCG GQNAFQKRSS QVPPKMFAFD AVFPQDASQA EVCAGTVAEV IQSVVNGADG
     CVFCFGHAKL GKSYTMIGRD DSMQNLGIIP CAISWLFKLI NERKEKTGAR FSVRISAVEV
     WGKEENLRDL LSEVATGSLQ DGQSPGVYLC EDPICGTQLQ NQSELRAPTA EKAAFFLDAA
     IASRRSNQQD CDEDDHRNSH MLFTLHIYQY RMEKSGKGGM SGGRSRLHLI DLGSCVKALS
     KNREGGSGLC LSLSALGNVI LALVNGSKHI PYKESKLTML LRESLGNVNC RTTMIAHISA
     AASSYAETLS TIQIASRVLR MKKKKTKYTS SSSGGESSCE EGRMRRPTQL RPFHARAPVD
     PEFPLAPLSS DPDYSSSSEQ SCDTVIYIGL NGTALSDKEL TDNEGPPDFV PIVPALQKTR
     GDSRPGEAAE AAASKSERDC LKCNTFAELQ ERLDCIDGSE EPSKFPFEEL PIQFGPEQAG
     RCAPLSQAVG PDTPSESEKE DNGSDNGQLT EREGTELPAS KAQRNRSPAP TVTRSSSPSP
     ASPRSIPGSS SQHSTSQLTQ SPSLQSSRES LNSCGFVEGK PRPMGSPRLG IASLSKTSEY
     KPPSSPSQRC KVYTQKGVLP SSAPPPSLSK DSGMVSSESL LQPDVRTPPV GMSPQVLKKS
     MSAGSEGFPG TLVDGEDQEG PPADSKKEIL STTMVTVQQP LELNGEDELV FTLVEELTIS
     GVLDSGRPTS IISFNSDCSV QALASGSRPV SIISSISEDL ECYSSMAPVS EVSITQFLPL
     PKLGLDEKAR DAGSRRSSIS SWLSEMSAGS DGEQSCHSFI AQTCFGHGEA MAEPPASEFV
     SSIQNTAVVC REKPEVGPDN LLILSEMGEE SGNKAAPIKG CKISTVGKAM VTISNTASLS
     SCEGYIPMKT NITVYPCIAM SPRNVQEPES STATPKVSPK ASQAQESKEP STRREMKFED
     PWLKREEEVK RENAYSSEEG VKCEPLPSSL KTEGKSEQEL DGRPSSGNRL SSSSSEAAAF
     QGTDNVRRVV DGCEMALPGL VAQSPLHVNR NLKSSSLPRA FQKADRHEEL DSFYHCLADS
     NGFSAASGIP SSKTTLERKV ASPKHCVLAR PKGTPPLPPV RKSSLDQKNR ASPQHGGGSS
     NTSSPLNQPA TFLACFPDES NGKTKDVSSS SKLFSAKLEQ LASRSNSLGR TTVSHYECLS
     LERAESLSSV SSRMHAGKDS TMPRTGRSLG RSTGASPPSC GITQSTGASP KASQSKISAV
     SKLLLASPKS RSSLSTSTTK TLSFSTKSLP QSVGQSSNLP PSGKHMSWST QSLSRNRGSG
     LASKLPLRAV NGRISELLQG SAGPRSAQLR AEAEERSGAP SEDKPAAAHL LPSPYSKITP
     PRKPHRCSSG HGSDNSSVLS GELPPAMGKT ALFYHSGGSS GYESMMRDSE ATGSASSAQD
     SMSENSSSVG GRCRSLKNQK KRSNSGSQRR RLIPALSLDT PSPVRKTASS TGVRWVDGPL
     RSTQRSLGEP FEIKVYEIDD VERLQRRRGA TSKEVMCFNA KLKILEHRQQ RIAEVRAKYE
     WLMKELEATR QYLMLDPNKW LREFDLEQVL QLDSLEYLEA LEGVTERLES RVNFCKAHLM
     MITCFDITSR RR
//
ID   DOC2A_MOUSE             Reviewed;         405 AA.
AC   Q7TNF0;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Double C2-like domain-containing protein alpha;
DE            Short=Doc2-alpha;
GN   Name=Doc2a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=18354201;
RA   Higashio H., Nishimura N., Ishizaki H., Miyoshi J., Orita S.,
RA   Sakane A., Sasaki T.;
RT   "Doc2 alpha and Munc13-4 regulate Ca(2+) -dependent secretory lysosome
RT   exocytosis in mast cells.";
RL   J. Immunol. 180:4774-4784(2008).
RN   [3]
RP   FUNCTION.
RX   PubMed=20150444; DOI=10.1126/science.1183765;
RA   Groffen A.J., Martens S., Diez Arazola R., Cornelisse L.N.,
RA   Lozovaya N., de Jong A.P., Goriounova N.A., Habets R.L., Takai Y.,
RA   Borst J.G., Brose N., McMahon H.T., Verhage M.;
RT   "Doc2b is a high-affinity Ca2+ sensor for spontaneous neurotransmitter
RT   release.";
RL   Science 327:1614-1618(2010).
CC   -!- FUNCTION: Calcium sensor which most probably regulates fusion of
CC       vesicles with membranes. Binds calcium and phospholipids. May be
CC       involved in calcium dependent neurotransmitter release through the
CC       interaction with UNC13A. May be involved in calcium-dependent
CC       spontaneous release of neurotransmitter in absence of action
CC       potentials in neuronal cells. Regulates Ca(2+)-dependent secretory
CC       lysosome exocytosis in mast cells.
CC   -!- SUBUNIT: Interacts (via N-terminus) with UNC13A. Interacts with
CC       cytoplasmic dynein light chain DYNLT1 (By similarity). Interacts
CC       with UNC13D (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane; Peripheral membrane protein (By
CC       similarity). Cell junction, synapse, synaptosome (By similarity).
CC       Lysosome (By similarity).
CC   -!- TISSUE SPECIFICITY: Brain and mast cells.
CC   -!- DOMAIN: C2 domain 1 is involved in binding calcium and
CC       phospholipids (By similarity).
CC   -!- SIMILARITY: Contains 2 C2 domains.
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DR   EMBL; BC055768; AAH55768.1; -; mRNA.
DR   IPI; IPI00407951; -.
DR   RefSeq; NP_034199.1; NM_010069.1.
DR   UniGene; Mm.266301; -.
DR   ProteinModelPortal; Q7TNF0; -.
DR   SMR; Q7TNF0; 94-394.
DR   PhosphoSite; Q7TNF0; -.
DR   PRIDE; Q7TNF0; -.
DR   Ensembl; ENSMUST00000064110; ENSMUSP00000070119; ENSMUSG00000052301.
DR   GeneID; 13446; -.
DR   KEGG; mmu:13446; -.
DR   UCSC; uc009jtb.1; mouse.
DR   CTD; 13446; -.
DR   MGI; MGI:109446; Doc2a.
DR   GeneTree; ENSGT00600000084227; -.
DR   HOGENOM; HBG716633; -.
DR   HOVERGEN; HBG051388; -.
DR   InParanoid; Q7TNF0; -.
DR   OMA; DDITHKV; -.
DR   OrthoDB; EOG4PRSR0; -.
DR   PhylomeDB; Q7TNF0; -.
DR   NextBio; 283891; -.
DR   ArrayExpress; Q7TNF0; -.
DR   Bgee; Q7TNF0; -.
DR   CleanEx; MM_DOC2A; -.
DR   Genevestigator; Q7TNF0; -.
DR   GermOnline; ENSMUSG00000052301; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019717; C:synaptosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   GO; GO:0017158; P:regulation of calcium ion-dependent exocytosis; IMP:UniProtKB.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   InterPro; IPR014638; Doc2.
DR   InterPro; IPR001565; Synaptotagmin.
DR   Pfam; PF00168; C2; 2.
DR   PIRSF; PIRSF036931; Doc2; 1.
DR   PRINTS; PR00360; C2DOMAIN.
DR   PRINTS; PR00399; SYNAPTOTAGMN.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 2.
PE   2: Evidence at transcript level;
KW   Calcium; Calcium/phospholipid-binding; Cell junction;
KW   Cytoplasmic vesicle; Exocytosis; Lysosome; Membrane; Repeat; Synapse;
KW   Synaptosome.
FT   CHAIN         1    405       Double C2-like domain-containing protein
FT                                alpha.
FT                                /FTId=PRO_0000079966.
FT   DOMAIN       96    200       C2 1.
FT   DOMAIN      258    361       C2 2.
FT   REGION        1     94       Interaction with UNC13D and DYNLT1 (By
FT                                similarity).
FT   REGION      220    405       Interaction with UNC13D (By similarity).
SQ   SEQUENCE   405 AA;  44609 MW;  B9EDCC03C977CCE7 CRC64;
     MRGRRGDRMT INIQEHMAIN VCPGPIRPIR QISDYFPRRG PGPEGGGGGG GTGCGEAPAH
     LAPLALAPPA ALLGATTPDD GAEVDSYDSD DTTALGTLEF DLLYDQASCM LHCRILRAKG
     LKPMDFNGLA DPYVKLHLLP GACKANKLKT KTQRNTLNPV WNEELTYSGI TDDDITHKVL
     RISVCDEDKL SHNEFIGEIR VPLRRLKPSQ KKHFNICLER QVPLPSPSSM SAALRGISCY
     LKELEQAEQG PGLLEERGRI LLSLSYSSRR HGLLVGIVRC AHLAAMDVNG YSDPYVKTYL
     RPDVDKKSKH KTCVKKKTLN PEFNEEFFYE IELSTLATKT LEVTVWDYDI GKSNDFIGGV
     SLGPGARGEA QKHWNDCLHQ PDTALERWHT LTSELPPAAG AYPLA
//
ID   Q7TNL5_MOUSE            Unreviewed;       595 AA.
AC   Q7TNL5;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   SubName: Full=Protein phosphatase 2, regulatory subunit B (B56), delta isoform, isoform CRA_a;
DE   SubName: Full=Protein phosphatase 2A B56 delta subunit;
GN   Name=Ppp2r5d; ORFNames=mCG_2696;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CD-1; TISSUE=Ovary;
RA   Ortega J.C., Del Mazo J.;
RT   "Developmental expression pattern of PP2A B56 delta in mouse testis.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY338234; AAQ01559.1; -; mRNA.
DR   EMBL; CH466559; EDL23530.1; -; Genomic_DNA.
DR   IPI; IPI00380331; -.
DR   UniGene; Mm.295009; -.
DR   UniGene; Mm.443214; -.
DR   ProteinModelPortal; Q7TNL5; -.
DR   SMR; Q7TNL5; 107-481.
DR   STRING; Q7TNL5; -.
DR   PhosphoSite; Q7TNL5; -.
DR   PRIDE; Q7TNL5; -.
DR   Ensembl; ENSMUST00000002839; ENSMUSP00000002839; ENSMUSG00000059409.
DR   UCSC; uc008cub.1; mouse.
DR   MGI; MGI:2388481; Ppp2r5d.
DR   eggNOG; roNOG10764; -.
DR   HOGENOM; HBG602178; -.
DR   HOVERGEN; HBG000009; -.
DR   InParanoid; Q7TNL5; -.
DR   OMA; AVIMFSV; -.
DR   OrthoDB; EOG4RXXZV; -.
DR   PhylomeDB; Q7TNL5; -.
DR   ArrayExpress; Q7TNL5; -.
DR   Bgee; Q7TNL5; -.
DR   Genevestigator; Q7TNL5; -.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0008601; F:protein phosphatase type 2A regulator activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002554; PP2A_B56.
DR   PANTHER; PTHR10257; B56; 1.
DR   Pfam; PF01603; B56; 1.
DR   PIRSF; PIRSF028043; PP2A_B56; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   595 AA;  69123 MW;  714B5643E49A8562 CRC64;
     MSYKLKKDKQ EPSKLAKGTA KPSSSSKDGG GENTDEAQPQ PQSQSPSSNK RPSNSTPPPT
     QLSKIKYSGG PQIVKKERRQ SSFPFNLNKN RELQKLPALK DSPTQEREEL FIQKLRQCCV
     LFDFVSDPLS DLKCKEVKRA GLNEMVEYIT HSRDVVTEAI YPEAVTMFSV NLFRTLPPSS
     NPTGAEFDPE EDEPTLEAAW PHLQLVYEFF LRFLESPDFQ PNIAKKYIDQ KFVLALLDLF
     DSEDPRERDF LKTILHRIYG KFLGLRAYIR RQINHIFYRF IYETEHHNGI AELLEILGSI
     INGFALPLKE EHKVFLVRVL LPLHKVKSLS VYHPQLAYCV VQFLEKESSL TEPVIVGLLK
     FWPKTHSPKE VMFLNELEEI LDVIEPSEFS KVMEPLFRQL AKCVSSPHFQ VAERALYYWN
     NEYIMSLISD NAARILPIMF PALYRNSKSH WNKTIHGLIY NALKLFMEMN QKLFDDCTQQ
     YKAEKQKGRF RMKEREEMWQ KIEELARLNP QYPMFRAPPP LPPVYSMETE TPTAEDIQLL
     KRTVETEAVQ MLKDIKKDKV LLRRKSELPQ DVYTIKALEA HKRAEEFLTA SQEAL
//
ID   TRI46_MOUSE             Reviewed;         759 AA.
AC   Q7TNM2; Q60717; Q6P1I9;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Tripartite motif-containing protein 46;
DE   AltName: Full=Gene Y protein;
DE            Short=GeneY;
DE   AltName: Full=Tripartite, fibronectin type-III and C-terminal SPRY motif protein;
GN   Name=Trim46; Synonyms=Trific;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6;
RX   PubMed=16434393; DOI=10.1074/jbc.M512755200;
RA   Short K.M., Cox T.C.;
RT   "Subclassification of the RBCC/TRIM superfamily reveals a novel motif
RT   necessary for microtubule binding.";
RL   J. Biol. Chem. 281:8970-8980(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 630-759 (ISOFORM 1).
RC   STRAIN=BALB/c;
RX   MEDLINE=96169575; PubMed=8597643; DOI=10.1007/BF00539013;
RA   Vos H.L., Mockensturm-Wilson M., Rood P.M.L., Maas A.M., Duhig T.,
RA   Gendler S.J., Bornstein P.;
RT   "A tightly organized, conserved gene cluster on mouse chromosome 3
RT   (E3-F1).";
RL   Mamm. Genome 6:820-822(1995).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7TNM2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TNM2-2; Sequence=VSP_011985, VSP_011986, VSP_011987;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC   -!- SIMILARITY: Contains 1 B box-type zinc finger.
CC   -!- SIMILARITY: Contains 1 B30.2/SPRY domain.
CC   -!- SIMILARITY: Contains 1 COS domain.
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC   -!- SIMILARITY: Contains 2 RING-type zinc fingers.
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DR   EMBL; AY251388; AAP51208.1; -; mRNA.
DR   EMBL; BC065049; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; U16175; AAA98539.1; -; Genomic_DNA.
DR   IPI; IPI00378619; -.
DR   IPI; IPI00463173; -.
DR   RefSeq; NP_898858.1; NM_183037.2.
DR   UniGene; Mm.331156; -.
DR   UniGene; Mm.393984; -.
DR   ProteinModelPortal; Q7TNM2; -.
DR   SMR; Q7TNM2; 29-59, 168-265, 429-528.
DR   PhosphoSite; Q7TNM2; -.
DR   PRIDE; Q7TNM2; -.
DR   Ensembl; ENSMUST00000041022; ENSMUSP00000036053; ENSMUSG00000042766.
DR   Ensembl; ENSMUST00000107463; ENSMUSP00000103087; ENSMUSG00000042766.
DR   GeneID; 360213; -.
DR   KEGG; mmu:360213; -.
DR   UCSC; uc008pyk.1; mouse.
DR   CTD; 360213; -.
DR   MGI; MGI:2673000; Trim46.
DR   GeneTree; ENSGT00580000081333; -.
DR   HOGENOM; HBG444447; -.
DR   HOVERGEN; HBG059072; -.
DR   InParanoid; Q7TNM2; -.
DR   OMA; GPAAGCT; -.
DR   OrthoDB; EOG4G7BXS; -.
DR   PhylomeDB; Q7TNM2; -.
DR   NextBio; 400912; -.
DR   ArrayExpress; Q7TNM2; -.
DR   Bgee; Q7TNM2; -.
DR   CleanEx; MM_TRIM46; -.
DR   Genevestigator; Q7TNM2; -.
DR   GermOnline; ENSMUSG00000042766; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001870; B302/SPRY.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR017903; COS_domain.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 3.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
DR   SUPFAM; SSF49265; FN_III-like; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS51262; COS; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Metal-binding; Zinc; Zinc-finger.
FT   CHAIN         1    759       Tripartite motif-containing protein 46.
FT                                /FTId=PRO_0000056269.
FT   DOMAIN      370    427       COS.
FT   DOMAIN      430    525       Fibronectin type-III.
FT   DOMAIN      526    747       B30.2/SPRY.
FT   ZN_FING      33     73       RING-type 1; degenerate.
FT   ZN_FING     172    231       RING-type 2; degenerate.
FT   ZN_FING     222    263       B box-type.
FT   COILED      322    400       Potential.
FT   VAR_SEQ       1     23       MAEGEDMQTFTSIMDALVRISTS -> MGGALEINAINPEM
FT                                EGWRQTS (in isoform 2).
FT                                /FTId=VSP_011985.
FT   VAR_SEQ     429    447       VPEAPVIDTQRTFAYDQIF -> GCGHRGLCSGAPQCPRRP
FT                                S (in isoform 2).
FT                                /FTId=VSP_011986.
FT   VAR_SEQ     448    759       Missing (in isoform 2).
FT                                /FTId=VSP_011987.
FT   CONFLICT    743    743       G -> A (in Ref. 3; AAA98539).
SQ   SEQUENCE   759 AA;  83432 MW;  8126C4C79841A536 CRC64;
     MAEGEDMQTF TSIMDALVRI STSMKNMEKE LLCPVCQEMY KQPLVLPCTH NVCQACAREV
     LGQQGYIGHG GDPSSEPTSP ASTPSTRSPR LSRRTLPKPD RLDRLLKSGF GTYPGRKRGA
     LHPQTILFPC PACQGDVELG ERGLSGLFRN LTLERVVERY RQSVSVGGAI LCQLCKPPPL
     EATKGCTECR ATFCNECFKL FHPWGTQKAQ HEPTLPTLSF RPKGLMCPDH KEEVTHYCKT
     CQRLVCQLCR VRRTHSGHKI TPVLSAYQAL KDKLTKSLAY ILGNQDTVQT QICELEETIR
     HTEVSGQQAK EEVSQLVRGL GAVLEEKRAS LLQAIEECQQ ERLSRLSAQI HEHQSLLDGS
     GLVGYAQEVL KETDQPCFVQ AAKQLHNRIA RATEALQTFR PAASSSFRHC QLDVGREMKL
     LTELSFLRVP EAPVIDTQRT FAYDQIFLCW RLPPHSPPAW HYTVEFRRTD VPAQPGPTRW
     QRREEVRGTS ALLENPDTGS VYVLRVRGCN KAGYGEYSED VHLHTPPAPV LHFFLDGRWG
     ASRERLAISK DQRAVRSIPG LPLLLAAERL LTGCHLSVDV VLGDVAVTQG RSYWACAVDP
     ASYLVKVGVG LESKLQESFQ GAPDVISPRY DPDSGHDSGA EDAAVEALPP FAFLTIGMGK
     ILLGSGASSN AGLTGRDGPT ASCTVPLPPR LGICLDYERG RVSFLDAVSF RGLLECPLDC
     SGPVCPAFCF IGGGAVQLQE PVGTKPERKV TIGGFAKLD
//
ID   Q7TNS5_MOUSE            Unreviewed;       333 AA.
AC   Q7TNS5;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   SubName: Full=Novel protein similar to F-box and leucine-rich repeat protein 17 (Fbxl17);
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=B630019K06Rik; Synonyms=RP23-245M18.4;
GN   ORFNames=RP23-245M18.4-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RA   Leongamornlert D.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC055780; AAH55780.1; -; mRNA.
DR   EMBL; AL731692; CAM18476.1; -; Genomic_DNA.
DR   IPI; IPI00227157; -.
DR   RefSeq; NP_780536.2; NM_175327.4.
DR   UniGene; Mm.41588; -.
DR   ProteinModelPortal; Q7TNS5; -.
DR   PRIDE; Q7TNS5; -.
DR   Ensembl; ENSMUST00000064196; ENSMUSP00000070261; ENSMUSG00000052364.
DR   GeneID; 102941; -.
DR   KEGG; mmu:102941; -.
DR   UCSC; uc009spi.1; mouse.
DR   MGI; MGI:2147918; B630019K06Rik.
DR   eggNOG; maNOG20431; -.
DR   HOVERGEN; HBG066418; -.
DR   InParanoid; Q7TNS5; -.
DR   OMA; CKELGLA; -.
DR   OrthoDB; EOG45HS0F; -.
DR   ArrayExpress; Q7TNS5; -.
DR   Bgee; Q7TNS5; -.
DR   Genevestigator; Q7TNS5; -.
PE   1: Evidence at protein level;
SQ   SEQUENCE   333 AA;  34857 MW;  F9B92027B6F166F2 CRC64;
     MGHLLSKEPR NRASQKKPRC CSWCRRRRPL IRLPGRTPTK SSPQPAAAAA RNRDCFFRGP
     CMLCFIVHSP SGPAPAGPEE EPPLSPPLPR DGAYATSPLQ HLEPRYAALA AEDCAAAARR
     FLLSSAAAAA ASSASSPATR CKELGLAAAA AWEQQGRSLF VASMGPLRFL GPPAAVQLFQ
     GLPPQTEHPL APDLVCNWKD DELPDYTYCS QPRCGGGGSG GGGGGGGGGP VGGGGLLLQP
     LDAGYCQAPE QPLPVIGSRP TSPASECSFI EATGDTLRAG SITAWSAQHQ AESRNADCPR
     LPDPCEFLRD SPPEPLDINQ LPGSIVLEVD LDD
//
ID   ACCN4_MOUSE             Reviewed;         539 AA.
AC   Q7TNS7; Q80XK4;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Amiloride-sensitive cation channel 4;
DE   AltName: Full=Acid-sensing ion channel 4;
DE            Short=ASIC4;
GN   Name=Accn4; Synonyms=Asic4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Probable cation channel with high affinity for sodium.
CC   -!- SUBUNIT: Homotrimer or heterotrimer with other ASIC proteins (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- MISCELLANEOUS: In vitro, has no proton-gated channel activity.
CC   -!- SIMILARITY: Belongs to the amiloride-sensitive sodium channel
CC       (TC 1.A.6) family. ACCN4 subfamily.
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DR   EMBL; BC046481; AAH46481.1; -; mRNA.
DR   EMBL; BC055772; AAH55772.1; -; mRNA.
DR   IPI; IPI00380344; -.
DR   RefSeq; NP_898843.1; NM_183022.3.
DR   UniGene; Mm.110790; -.
DR   ProteinModelPortal; Q7TNS7; -.
DR   SMR; Q7TNS7; 64-469.
DR   STRING; Q7TNS7; -.
DR   PhosphoSite; Q7TNS7; -.
DR   PRIDE; Q7TNS7; -.
DR   Ensembl; ENSMUST00000037708; ENSMUSP00000045598; ENSMUSG00000033007.
DR   GeneID; 241118; -.
DR   KEGG; mmu:241118; -.
DR   UCSC; uc007bpg.1; mouse.
DR   CTD; 241118; -.
DR   MGI; MGI:2652846; Accn4.
DR   eggNOG; roNOG08015; -.
DR   GeneTree; ENSGT00550000074208; -.
DR   HOGENOM; HBG447044; -.
DR   HOVERGEN; HBG004150; -.
DR   InParanoid; Q7TNS7; -.
DR   OMA; ARGYLTW; -.
DR   OrthoDB; EOG4B8JCX; -.
DR   PhylomeDB; Q7TNS7; -.
DR   NextBio; 384894; -.
DR   ArrayExpress; Q7TNS7; -.
DR   Bgee; Q7TNS7; -.
DR   CleanEx; MM_ACCN4; -.
DR   Genevestigator; Q7TNS7; -.
DR   GermOnline; ENSMUSG00000033007; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005272; F:sodium channel activity; IEA:UniProtKB-KW.
DR   InterPro; IPR001873; Na+channel_ASC.
DR   InterPro; IPR020903; Na+channel_ASC_CS.
DR   PANTHER; PTHR11690; Na+channel_ASC; 1.
DR   Pfam; PF00858; ASC; 1.
DR   PRINTS; PR01078; AMINACHANNEL.
DR   PROSITE; PS01206; ASC; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Ion transport; Ionic channel; Membrane;
KW   Sodium; Sodium channel; Sodium transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    539       Amiloride-sensitive cation channel 4.
FT                                /FTId=PRO_0000181305.
FT   TOPO_DOM      1     68       Cytoplasmic (Potential).
FT   TRANSMEM     69     89       Helical; (Potential).
FT   TOPO_DOM     90    438       Extracellular (Potential).
FT   TRANSMEM    439    459       Helical; (Potential).
FT   TOPO_DOM    460    539       Cytoplasmic (Potential).
FT   CARBOHYD    191    191       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    243    243       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    341    341       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    376    376       N-linked (GlcNAc...) (Potential).
FT   DISULFID    118    202       By similarity.
FT   DISULFID    180    187       By similarity.
FT   DISULFID    296    375       By similarity.
FT   DISULFID    318    371       By similarity.
FT   DISULFID    322    369       By similarity.
FT   DISULFID    331    353       By similarity.
FT   DISULFID    333    345       By similarity.
SQ   SEQUENCE   539 AA;  59216 MW;  25A4B1E73D67FE9A CRC64;
     MPIEIVCKIK FAEEDAKPKE KEAGDEQSLL GAAQGPAAPR DLATFASTST LHGLGRACGP
     GPHGLRRTLW ALALLTSLAA FLYQAASLAR GYLTRPHLVA MDPAAPAPVA GFPAVTLCNI
     NRFRHSALSD ADIFHLANLT GLPPKDRDGH RAAGLRYPEP DMVDILNRTG HQLADMLKSC
     NFSGHHCSAS NFSVVYTRYG KCYTFNADPQ SSLPSRAGGM GSGLEIMLDI QQEEYLPIWR
     ETNETSFEAG IRVQIHSQEE PPYIHQLGFG VSPGFQTFVS CQEQRLTYLP QPWGNCRAES
     ELREPELQGY SAYSVSACRL RCEKEAVLQR CHCRMVHMPG NETICPPNIY IECADHTLDS
     LGGGSEGPCF CPTPCNLTRY GKEISMVKIP NRGSARYLAR KYNRNETYIR ENFLVLDVFF
     EALTSEAMEQ QAAYGLSALL GDLGGQMGLF IGASILTLLE ILDYIYEVSW DRLKRVWRRP
     KTPLRTSTGG ISTLGLQELK EQSPCPSRGR AEGGGASSLL PNHHHPHGPP GSLFEDFAC
//
ID   LPPR3_MOUSE             Reviewed;         716 AA.
AC   Q7TPB0; Q4V781; Q68FN2; Q6NZQ9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Lipid phosphate phosphatase-related protein type 3;
DE            EC=3.1.3.4;
DE   AltName: Full=Plasticity-related gene 2 protein;
DE            Short=PRG-2;
GN   Name=Lppr3; Synonyms=Kiaa4076, Prg2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=22656544; PubMed=12730698; DOI=10.1038/nn1052;
RA   Braeuer A.U., Savaskan N.E., Kuehn H., Prehn S., Ninnemann O.,
RA   Nitsch R.;
RT   "A new phospholipid phosphatase, PRG-1, is involved in axon growth and
RT   regenerative sprouting.";
RL   Nat. Neurosci. 6:572-578(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: A 1,2-diacylglycerol 3-phosphate + H(2)O = a
CC       1,2-diacyl-sn-glycerol + phosphate.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7TPB0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TPB0-2; Sequence=VSP_031007, VSP_031008;
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family.
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DR   EMBL; AF541278; AAP57767.1; -; mRNA.
DR   EMBL; BC066006; AAH66006.1; -; mRNA.
DR   EMBL; BC079534; AAH79534.1; -; mRNA.
DR   EMBL; BC098099; AAH98099.1; -; mRNA.
DR   IPI; IPI00117580; -.
DR   IPI; IPI00607990; -.
DR   RefSeq; NP_001164406.1; NM_001170935.1.
DR   RefSeq; NP_859009.2; NM_181681.2.
DR   UniGene; Mm.29678; -.
DR   ProteinModelPortal; Q7TPB0; -.
DR   PhosphoSite; Q7TPB0; -.
DR   PRIDE; Q7TPB0; -.
DR   Ensembl; ENSMUST00000046458; ENSMUSP00000043447; ENSMUSG00000035835.
DR   Ensembl; ENSMUST00000092325; ENSMUSP00000089979; ENSMUSG00000035835.
DR   GeneID; 216152; -.
DR   KEGG; mmu:216152; -.
DR   MGI; MGI:2388640; BC005764.
DR   eggNOG; roNOG06146; -.
DR   GeneTree; ENSGT00550000074203; -.
DR   HOGENOM; HBG443683; -.
DR   HOVERGEN; HBG103365; -.
DR   InParanoid; Q7TPB0; -.
DR   OrthoDB; EOG4BRWK9; -.
DR   BRENDA; 3.1.3.4; 244.
DR   NextBio; 375016; -.
DR   ArrayExpress; Q7TPB0; -.
DR   Bgee; Q7TPB0; -.
DR   CleanEx; MM_BC005764; -.
DR   CleanEx; MM_PRG2; -.
DR   Genevestigator; Q7TPB0; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008195; F:phosphatidate phosphatase activity; IEA:EC.
DR   InterPro; IPR016118; P_Acid_Pase/Cl_peroxidase_N.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   Gene3D; G3DSA:1.20.144.10; P_Acid_Pase/Cl_peroxidase_N; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; AcPase_VanPerase; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Hydrolase; Membrane;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    716       Lipid phosphate phosphatase-related
FT                                protein type 3.
FT                                /FTId=PRO_0000317530.
FT   TRANSMEM     18     38       Helical; (Potential).
FT   TRANSMEM     70     90       Helical; (Potential).
FT   TRANSMEM    131    151       Helical; (Potential).
FT   TRANSMEM    205    225       Helical; (Potential).
FT   TRANSMEM    231    251       Helical; (Potential).
FT   TRANSMEM    261    281       Helical; (Potential).
FT   COMPBIAS    435    458       Glu-rich.
FT   COMPBIAS    508    512       Poly-Ser.
FT   COMPBIAS    562    571       Poly-Ser.
FT   CARBOHYD    167    167       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    316    316       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     408    463       EWKQKSLEGRGLGLPDEASPVHLRAPAEQVAEEEEEEEEEE
FT                                EEEEEEEEEEGPVPP -> SSPAAHHRRRLGNPGNNRKQKN
FT                                RAVSWQRNSGSGKKKKWEGRGGKKKVAKHRSVNT (in
FT                                isoform 2).
FT                                /FTId=VSP_031007.
FT   VAR_SEQ     464    716       Missing (in isoform 2).
FT                                /FTId=VSP_031008.
FT   CONFLICT    520    520       V -> M (in Ref. 2; AAH66006/AAH79534).
SQ   SEQUENCE   716 AA;  76693 MW;  86605748DED3F5B6 CRC64;
     MLAMKEKNKT PKDSMTLLPC FYFVELPIVA SSIVSLYFLE LTDLFKPAKV GFQCYDRALS
     MPYVETNEEL IPLLMLLSLA FAAPAASIMV GEGMVYCLQS RLWGRGPGGV EGSINAGGCN
     FNSFLRRTVR FVGVHVFGLC ATALVTDVIQ LATGYHTPFF LTVCKPNYTL LGTSCESNPY
     ITQDICSGHD THAILSARKT FPSQHATLSA FAAVYVSMYF NAVISDTTKL LKPILVFAFA
     IAAGVCGLTQ ITQYRSHPVD VYAGFLIGAG IAAYLACHAV GNFQAPPAEK VPTPAPAKDA
     LRALTQRGHE SMYQQNKSVS TDELGPPGRL EGVPRPVARE KTSLGSLKRA SVDVDLLAPR
     SPMGKEGMVT FSNTLPRVST PSLDDPARRH MTIHVPLDAS RSRQLIGEWK QKSLEGRGLG
     LPDEASPVHL RAPAEQVAEE EEEEEEEEEE EEEEEEEEGP VPPSLYPTVQ ARPGLGPRVI
     LPPRPGPQPL VHIPEEGVQA GAGLSPKSSS SSVRAKWLSV AEKGGGPVAV APSQPRVANP
     PRLLQVIAMS KAAGGPKAET ASSSSASSDS SQYRSPSDRD SASIVTIDAH APHHPVVHLS
     AGSTPWEWKA KVVEGEGSYE LGDLARGFRS SCKQPGMGPG SPVSDVDQEE PRFGAVATVN
     LATGEGLPPP GASEGALGAG SRESTLRRQV GGLAEREVEA EAESYYRRMQ ARRYQD
//
ID   INT3_MOUSE              Reviewed;        1041 AA.
AC   Q7TPD0; A0A4X0; A0A4X3; Q99LK7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Integrator complex subunit 3;
DE            Short=Int3;
DE   AltName: Full=SOSS complex subunit A;
DE   AltName: Full=Sensor of single-strand DNA complex subunit A;
DE            Short=SOSS-A;
DE            Short=Sensor of ssDNA subunit A;
GN   Name=Ints3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 460-1041 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, and Czech II; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1038 AND SER-1040, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Component of the Integrator complex. The Integrator
CC       complex is involved in the small nuclear RNAs (snRNA) U1 and U2
CC       transcription and in their 3'-box-dependent processing. The
CC       Integrator complex is associated with the C-terminal domain (CTD)
CC       of RNA polymerase II largest subunit (POLR2A) and is recruited to
CC       the U1 and U2 snRNAs genes (By similarity).
CC   -!- FUNCTION: Component of the SOSS complex, a multiprotein complex
CC       that functions downstream of the MRN complex to promote DNA repair
CC       and G2/M checkpoint. The SOSS complex associates with single-
CC       stranded DNA at DNA lesions and influences diverse endpoints in
CC       the cellular DNA damage response including cell-cycle checkpoint
CC       activation, recombinational repair and maintenance of genomic
CC       stability. The SOSS complex is required for efficient homologous
CC       recombination-dependent repair of double-strand breaks (DSBs) and
CC       ATM-dependent signaling pathways. In the SOSS complex, it is
CC       required for the assembly of the complex and for stabilization of
CC       the complex at DNA damage sites (By similarity).
CC   -!- SUBUNIT: Belongs to the multiprotein complex Integrator, at least
CC       composed of INTS1, INTS2, INTS3, INTS4, INTS5, INTS6, INTS7,
CC       INTS8, INTS9/RC74, INTS10, CPSF3L/INTS11 and INTS12. Component of
CC       the SOSS complex, composed of SOSS-B (SOSS-B1/OBFC2B or SOSS-
CC       B2/OBFC2A), SOSS-A/INTS3 and SOSS-C/SSBIP1. SOSS complexes
CC       containing SOSS-B1/OBFC2B are more abundant than complexes
CC       containing SOSS-B2/OBFC2A. Interacts with SOSS-B1/OBFC2B, SOSS-
CC       B2/OBFC2A and SOSS-C/SSBIP1; the interaction is direct. Interacts
CC       with NBN/NBS1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Note=Localizes to
CC       nuclear foci following DNA damage (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7TPD0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TPD0-2; Sequence=VSP_038133, VSP_038134;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the Integrator subunit 3 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC31492.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK040147; BAC30523.1; -; mRNA.
DR   EMBL; AK043206; BAC31492.1; ALT_INIT; mRNA.
DR   EMBL; BC003209; AAH03209.2; -; mRNA.
DR   EMBL; BC055344; AAH55344.1; -; mRNA.
DR   IPI; IPI00380394; -.
DR   IPI; IPI00944687; -.
DR   RefSeq; NP_663515.2; NM_145540.2.
DR   RefSeq; NP_849207.2; NM_178876.2.
DR   UniGene; Mm.268564; -.
DR   ProteinModelPortal; Q7TPD0; -.
DR   STRING; Q7TPD0; -.
DR   PhosphoSite; Q7TPD0; -.
DR   PRIDE; Q7TPD0; -.
DR   Ensembl; ENSMUST00000029542; ENSMUSP00000029542; ENSMUSG00000027933.
DR   Ensembl; ENSMUST00000071488; ENSMUSP00000071422; ENSMUSG00000027933.
DR   GeneID; 229543; -.
DR   KEGG; mmu:229543; -.
DR   UCSC; uc008qcd.1; mouse.
DR   CTD; 229543; -.
DR   MGI; MGI:2140050; Ints3.
DR   GeneTree; ENSGT00390000014184; -.
DR   HOGENOM; HBG357723; -.
DR   HOVERGEN; HBG081800; -.
DR   InParanoid; Q7TPD0; -.
DR   OMA; MEMDNHL; -.
DR   OrthoDB; EOG483D3T; -.
DR   ArrayExpress; Q7TPD0; -.
DR   Bgee; Q7TPD0; -.
DR   CleanEx; MM_INTS3; -.
DR   Genevestigator; Q7TPD0; -.
DR   GermOnline; ENSMUSG00000027933; Mus musculus.
DR   GO; GO:0032039; C:integrator complex; ISS:HGNC.
DR   GO; GO:0070876; C:SOSS complex; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR   GO; GO:0031576; P:G2/M transition checkpoint; ISS:UniProtKB.
DR   GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR   GO; GO:0016180; P:snRNA processing; ISS:HGNC.
DR   InterPro; IPR019333; Integrator_3.
DR   Pfam; PF10189; DUF2356; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA damage; DNA repair; Nucleus; Phosphoprotein.
FT   CHAIN         1   1041       Integrator complex subunit 3.
FT                                /FTId=PRO_0000259535.
FT   COMPBIAS      9     33       Ala/Gly-rich.
FT   MOD_RES     500    500       Phosphoserine (By similarity).
FT   MOD_RES     535    535       Phosphoserine (By similarity).
FT   MOD_RES    1038   1038       Phosphoserine.
FT   MOD_RES    1040   1040       Phosphoserine.
FT   VAR_SEQ     321    330       FGQQKRYQDW -> SSVHRRRSYR (in isoform 2).
FT                                /FTId=VSP_038133.
FT   VAR_SEQ     331   1041       Missing (in isoform 2).
FT                                /FTId=VSP_038134.
FT   CONFLICT    553    553       H -> P (in Ref. 1; BAC31492).
FT   CONFLICT    948    948       Q -> H (in Ref. 2; AAH55344).
SQ   SEQUENCE   1041 AA;  117938 MW;  852920EFDAA5688E CRC64;
     MELQKGKGTV AAAASGAAGG GGGGAGAGAP GGGRLLLSTS LDAKDELEER LERCMSIVTS
     MTAGVSEREA NDALNAYVCK GPPQHEEICL GLFTLVLTEP AQAQKCYRDL ALVSRDGMNI
     VLNKINQLLM EKYLKLQDTC RTQLVWLVRE LVKSGVLGAD GVCMTFMKQI AGGDVTAKNI
     WLAESVLDIL TEQREWVLKS SILIAMAVYT YLRLIVDHHG TAQLQTLRQK EVDFCISLLR
     ERFMECLMIG RDLVRLLQNV ARIPEFELLW KDIIHNPQAL SPQFTGILQL LQSRTSRKFL
     ACRLTPDMET KLLFMTSRVR FGQQKRYQDW FQRQYLSTPD SQSLRCDLIR YICGVVHPSN
     EVLSSDILPR WAIIGWLLTT CTSNVAASNA KLALFYDWLF FSPEKDSIMN IEPAILVMHH
     SMKPHPAITA TLLDFMCRII PNFYPPLEGH VRQGVFSSLN HIVEKRVLAH LAPLFDNPKL
     DKELRSMLRE KFPEFCSSPS PPVEVKIEEP VSMEMDNHLS DKDESCYDNA EAAFSDDEED
     LNSKGKKREF RFHPIKETVV EEPVDVTPYL DQLDESLRDK VLQLQKGSDT EAQCEVMQEI
     VDQVLEEDFD SEQLSVLASC LQELFKAHFR GEVLPEEVTE ESLEESVGKP LYLIFRNLCQ
     MQEDNSSFSL LLDLLSELYQ KQPKIGYHLL YYLRASKAAA GKMNLYESFA QATQLGDLHT
     CLMMDMKACQ EDDVRLLCHL TPSIYTEFPD ETLRSGELLN MIVAVIDSAQ LQELVCHVMM
     GNLVMFRKDS VLNILIQSLD WETFEQYCAW QLFLAHNIPL ETIIPILQHL KYKEHPEALS
     CLLLQLRREK PSEEMVKMVL SRPCHPDDQF TTSILRHWCM KHDELLAEHI KALLIKNNSL
     PRKRQSLRSS SSKLAQLTLE QILEHLDNLR LNLANTKQNF FSQTPILQAL QHVQASCDEA
     HKMKFSDLFS LAEEYEDSST KPPKSRRKAA LSSPRSRKNA TQPPNAEEES GSSSASEEED
     TKPKPTKRKR KGSSAVGSDS D
//
ID   ROBO2_MOUSE             Reviewed;        1470 AA.
AC   Q7TPD3; Q8BJ59;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 2.
DT   08-FEB-2011, entry version 79.
DE   RecName: Full=Roundabout homolog 2;
DE   Flags: Precursor;
GN   Name=Robo2; Synonyms=Kiaa1568;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 679-1470 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=15091338; DOI=10.1016/S0896-6273(04)00179-5;
RA   Long H., Sabatier C., Ma L., Plump A., Yuan W., Ornitz D.M.,
RA   Tamada A., Murakami F., Goodman C.S., Tessier-Lavigne M.;
RT   "Conserved roles for slit and robo proteins in midline commissural
RT   axon guidance.";
RL   Neuron 42:213-223(2004).
CC   -!- FUNCTION: Receptor for SLIT2, and probably SLIT1, which are
CC       thought to act as molecular guidance cue in cellular migration,
CC       including axonal navigation at the ventral midline of the neural
CC       tube and projection of axons to different regions during neuronal
CC       development.
CC   -!- SUBUNIT: Interacts with SLIT2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7TPD3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TPD3-2; Sequence=VSP_010648, VSP_010649;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in embryonal spinal chord.
CC   -!- DEVELOPMENTAL STAGE: Expressed at E11.5 in spinal chord.
CC   -!- DISRUPTION PHENOTYPE: Mice show defects in commissural axon
CC       guidance in spinal chord including an altered lateral and ventral
CC       funiculi projection. The phenotype resembles that of a
CC       SLIT1;SLIT2;SLIT3 triple mutant.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. ROBO
CC       family.
CC   -!- SIMILARITY: Contains 3 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 5 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC055333; AAH55333.1; -; mRNA.
DR   EMBL; AK129396; BAC98206.1; -; mRNA.
DR   IPI; IPI00420290; -.
DR   IPI; IPI00776029; -.
DR   UniGene; Mm.171736; -.
DR   ProteinModelPortal; Q7TPD3; -.
DR   SMR; Q7TPD3; 24-839.
DR   STRING; Q7TPD3; -.
DR   PhosphoSite; Q7TPD3; -.
DR   PRIDE; Q7TPD3; -.
DR   Ensembl; ENSMUST00000064435; ENSMUSP00000069846; ENSMUSG00000052516.
DR   MGI; MGI:1890110; Robo2.
DR   GeneTree; ENSGT00590000082947; -.
DR   HOVERGEN; HBG073476; -.
DR   ArrayExpress; Q7TPD3; -.
DR   Bgee; Q7TPD3; -.
DR   CleanEx; MM_ROBO2; -.
DR   Genevestigator; Q7TPD3; -.
DR   GO; GO:0030673; C:axolemma; IDA:MGI.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
DR   GO; GO:0016199; P:axon midline choice point recognition; IGI:UniProtKB.
DR   GO; GO:0007156; P:homophilic cell adhesion; ISS:UniProtKB.
DR   GO; GO:0001656; P:metanephros development; IMP:MGI.
DR   GO; GO:0021891; P:olfactory bulb interneuron development; IMP:UniProtKB.
DR   GO; GO:0050772; P:positive regulation of axonogenesis; ISS:UniProtKB.
DR   GO; GO:0031290; P:retinal ganglion cell axon guidance; IMP:UniProtKB.
DR   GO; GO:0001657; P:ureteric bud development; IMP:UniProtKB.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 9.
DR   Pfam; PF00041; fn3; 3.
DR   Pfam; PF07679; I-set; 5.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00408; IGc2; 5.
DR   SUPFAM; SSF49265; FN_III-like; 3.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS50835; IG_LIKE; 5.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Chemotaxis; Developmental protein;
KW   Differentiation; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Membrane; Neurogenesis; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     21       Potential.
FT   CHAIN        22   1470       Roundabout homolog 2.
FT                                /FTId=PRO_0000031037.
FT   TOPO_DOM     22    863       Extracellular (Potential).
FT   TRANSMEM    864    884       Helical; (Potential).
FT   TOPO_DOM    885   1470       Cytoplasmic (Potential).
FT   DOMAIN       31    127       Ig-like C2-type 1.
FT   DOMAIN      133    220       Ig-like C2-type 2.
FT   DOMAIN      225    309       Ig-like C2-type 3.
FT   DOMAIN      318    413       Ig-like C2-type 4.
FT   DOMAIN      422    508       Ig-like C2-type 5.
FT   DOMAIN      526    611       Fibronectin type-III 1.
FT   DOMAIN      638    728       Fibronectin type-III 2.
FT   DOMAIN      740    830       Fibronectin type-III 3.
FT   CARBOHYD    123    123       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    430    430       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    756    756       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    786    786       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    793    793       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    849    849       N-linked (GlcNAc...) (Potential).
FT   DISULFID     52    110       Potential.
FT   DISULFID    154    203       Potential.
FT   DISULFID    246    293       Potential.
FT   DISULFID    339    395       Potential.
FT   DISULFID    443    492       Potential.
FT   VAR_SEQ     807    946       GLFPGIQYRVEVAASTSAGVGVKSEPQPIIIGGRNEVVITE
FT                                NNNSITEQITDVVKQPAFIAGIGGACWVILMGFSIWLYWRR
FT                                KKRKGLSNYAVTFQRGDGGLMSNGSRPGLLNAGDPNYPWLA
FT                                DSWPATSLPVNNSNSGP -> ASTSRPPEWNYSGI (in
FT                                isoform 2).
FT                                /FTId=VSP_010648.
FT   VAR_SEQ     947   1470       Missing (in isoform 2).
FT                                /FTId=VSP_010649.
SQ   SEQUENCE   1470 AA;  161190 MW;  3C61DE40DA39109E CRC64;
     MNPLMFTLLL LFGFLCIQID GSRLRQEDFP PRIVEHPSDV IVSKGEPTTL NCKAEGRPTP
     TIEWYKDGER VETDKDDPRS HRMLLPSGSL FFLRIVHGRR SKPDEGSYVC VARNYLGEAV
     SRNASLEVAL LRDDFRQNPT DVVVAAGEPA ILECQPPRGH PEPTIYWKKD KVRIDDKEER
     ISIRGGKLMI SNTRKSDAGM YTCVGTNMVG ERDSDPAELT VFERPTFLRR PINQVVLEEE
     AVEFRCQVQG DPQPTVRWKK DDADLPRGRY DIKDDYTLRI KKAMSTDEGT YVCIAENRVG
     KVEASATLTV RVRPVAPPQF VVRPRDQIVA QGRTVTFPCE TKGNPQPAVF WQKEGSQNLL
     FPNQPQQPNS RCSVSPTGDL TITNIQRSDA GYYICQALTV AGSILAKAQL EVTDVLTDRP
     PPIILQGPIN QTLAVDGTAL LKCKATGEPL PVISWLKEGF TFLGRDPRAT IQDQGTLQIK
     NLRISDTGTY TCVATSSSGE TSWSAVLDVT ESGATISKNY DMNDLPGPPS KPQVTDVSKN
     SVTLSWQPGT PGVLPASAYI IEAFSQSVSN SWQTVANHVK TTLYTVRGLR PNTIYLFMVR
     AINPQGLSDP SPMSDPVRTQ DISPPAQGVD HRQVQKELGD VVVRLHNPVV LTPTTVQVTW
     TVDRQPQFIQ GYRVMYRQTS GLQASTVWQN LDAKVPTERS AVLVNLKKGV TYEIKVRPYF
     NEFQGMDSES KTVRTTEEAP SAPPQSVTVL TVGSHNSTSI SVSWDPPPAD HQNGIIQEYK
     IWCLGNETRF HINKTVDAAI RSVVIGGLFP GIQYRVEVAA STSAGVGVKS EPQPIIIGGR
     NEVVITENNN SITEQITDVV KQPAFIAGIG GACWVILMGF SIWLYWRRKK RKGLSNYAVT
     FQRGDGGLMS NGSRPGLLNA GDPNYPWLAD SWPATSLPVN NSNSGPNEIG NFGRGDVLPP
     VPGQGDKTAT MLSDGAIYSS IDFTTKTTYN SSSQITQATP YATTQILHSN SIHELAVDLP
     DPQWKSSVQQ KTDLMGFGYS LPDQNKGNNG GKGGKKKKTK NSSKAQKNNG STWANVPLPP
     PPVQPLPGTE LGHYAAEQEN GYDSDSWCPP LPVQTYLHQG MEDELEEDED RVPTPPVRGV
     ASSPAISFGQ QSTATLTPSP REEMQPMLQA HLDELTRAYQ FDIAKQTWHI QSNTPPPQPP
     APPLGYVSGA LISDLETDVP DEDADDEEEP LEIPRPLRAL DQTPGSSMDN LDSSVTGKAF
     SSSQRQRPTS PFSTDSNTSA AQNQSQRPRP TKKHKGGRMD PQPVLPHRRE GMPDDLPPPP
     DPPPGQGLRQ QIGLSQHSGN VENSTERKGS SLERQQAANL EDTKSSLDCP AKTVLEWQRQ
     TQDWINSTER QEETRKAPHK QGVGSEESLV PYSKPSFPSP GGHSSSGTSS SKGSTGPRKA
     DVLRGSHQRN ANDLLDIGYV GSNSQGQFTE
//
ID   S7A6O_MOUSE             Reviewed;         306 AA.
AC   Q7TPE5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Protein SLC7A6OS;
DE   AltName: Full=Solute carrier family 7 member 6 opposite strand transcript homolog;
GN   Name=Slc7a6os;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=ICR; TISSUE=Trophoblast stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SIMILARITY: Belongs to the SLC7A6OS family.
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DR   EMBL; AK146733; BAE27395.1; -; mRNA.
DR   EMBL; BC054118; AAH54118.1; -; mRNA.
DR   IPI; IPI00127547; -.
DR   RefSeq; NP_001007568.1; NM_001007567.2.
DR   UniGene; Mm.269029; -.
DR   ProteinModelPortal; Q7TPE5; -.
DR   PhosphoSite; Q7TPE5; -.
DR   PRIDE; Q7TPE5; -.
DR   Ensembl; ENSMUST00000035925; ENSMUSP00000039029; ENSMUSG00000033106.
DR   GeneID; 66432; -.
DR   KEGG; mmu:66432; -.
DR   UCSC; uc009nfp.1; mouse.
DR   CTD; 66432; -.
DR   MGI; MGI:1916951; Slc7a6os.
DR   eggNOG; roNOG14271; -.
DR   GeneTree; ENSGT00390000015672; -.
DR   HOGENOM; HBG268919; -.
DR   HOVERGEN; HBG054901; -.
DR   InParanoid; Q7TPE5; -.
DR   OMA; VNDDQEP; -.
DR   OrthoDB; EOG405S23; -.
DR   PhylomeDB; Q7TPE5; -.
DR   NextBio; 321671; -.
DR   ArrayExpress; Q7TPE5; -.
DR   Bgee; Q7TPE5; -.
DR   CleanEx; MM_SLC7A6OS; -.
DR   Genevestigator; Q7TPE5; -.
DR   InterPro; IPR013883; TF_Iwr1.
DR   Pfam; PF08574; DUF1762; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    306       Protein SLC7A6OS.
FT                                /FTId=PRO_0000289170.
FT   MOD_RES       6      6       Phosphothreonine (By similarity).
FT   MOD_RES     156    156       Phosphoserine.
FT   MOD_RES     299    299       Phosphoserine (By similarity).
FT   MOD_RES     305    305       Phosphoserine.
SQ   SEQUENCE   306 AA;  35041 MW;  B7818376BB37589D CRC64;
     MEAGRTAVLR VKRKRNAEPA EALVLACKRP RSSEVESAAR ETPEGQEAAA AERNVFQLVA
     TVRSQEEPIQ QLVRAALRPS RSSQLRIRRD LRASVREVRK EGRYRVVSSH RSSGTSNSLE
     PQCGSEAVGD AGFQLLDLVH EEENPEAAAT DCRKTSDPDV ILCNSVELIR ERLTVSEDGS
     QVNHQEDPKH NDDYVYDIYY MEMAPPGWIE NIMSVQPYSQ EWELVNDDEQ SEDIYEDEDD
     ENSENNWRNE YPDEESSDRD EDSRGSDEYN SLSEEERSCE RLMWSKYPLD VQKEFDYDSP
     HGLDSD
//
ID   MYCB2_MOUSE             Reviewed;        4711 AA.
AC   Q7TPH6; Q6PCM8;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Probable E3 ubiquitin-protein ligase MYCBP2;
DE            EC=6.3.2.-;
DE   AltName: Full=Myc-binding protein 2;
DE   AltName: Full=Pam/highwire/rpm-1 protein;
DE   AltName: Full=Protein associated with Myc;
GN   Name=Mycbp2; Synonyms=Pam, Phr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP   AND DISRUPTION PHENOTYPE.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=14729956; DOI=10.1128/MCB.24.3.1096-1105.2004;
RA   Burgess R.W., Peterson K.A., Johnson M.J., Roix J.J., Welsh I.C.,
RA   O'Brien T.P.;
RT   "Evidence for a conserved function in synapse formation reveals Phr1
RT   as a candidate gene for respiratory failure in newborn mice.";
RL   Mol. Cell. Biol. 24:1096-1105(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 2327-2352 AND 2866-2875, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3250-4711 (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1583 AND THR-3954, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   INTERACTION WITH FBXO45.
RX   PubMed=19398581; DOI=10.1128/MCB.00364-09;
RA   Saiga T., Fukuda T., Matsumoto M., Tada H., Okano H.J., Okano H.,
RA   Nakayama K.I.;
RT   "Fbxo45 forms a novel ubiquitin ligase complex and is required for
RT   neuronal development.";
RL   Mol. Cell. Biol. 29:3529-3543(2009).
CC   -!- FUNCTION: Probable E3 ubiquitin-protein ligase which mediates
CC       ubiquitination and subsequent proteasomal degradation of target
CC       proteins. May have a role during synaptogenesis; candidate for
CC       respiratory distress and ventilatory disorders that arise from
CC       defective neuronal control of breathing. May function as a
CC       facilitator or regulator of transcriptional activation by MYC.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with MYC. Interacts with TSC2 (tuberin) when
CC       TSC2 is in complex with TSC1 (hamartin) (By similarity). Interacts
CC       with FBXO45.
CC   -!- INTERACTION:
CC       Q63633:Slc12a5 (xeno); NbExp=4; IntAct=EBI-1811542, EBI-1811510;
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7TPH6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TPH6-2; Sequence=VSP_014184;
CC   -!- TISSUE SPECIFICITY: Dynamically expressed in embryonic nervous
CC       system from E8.5 through E18.5. During postnatal development,
CC       expression is particularly strong in the cerebellum, hippocampus
CC       and retina. Lower levels of expression are observed throughout the
CC       cerebral cortex.
CC   -!- DISRUPTION PHENOTYPE: Mice display incomplete innervation of the
CC       diaphragm by the phrenic nerve. Intercostal muscles are completely
CC       innervated, but show dysmorphic nerve terminals. Sensory neuron
CC       terminals in the diaphragm are abnormal and neuromuscular
CC       junctions show excessive sprouting of nerve terminals, consistent
CC       with inadequate presynaptic stimulation of the muscle.
CC   -!- SIMILARITY: Belongs to the highwire family.
CC   -!- SIMILARITY: Contains 1 B box-type zinc finger.
CC   -!- SIMILARITY: Contains 1 DOC domain.
CC   -!- SIMILARITY: Contains 1 filamin repeat.
CC   -!- SIMILARITY: Contains 5 RCC1 repeats.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
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DR   EMBL; AY325887; AAP88591.1; -; mRNA.
DR   EMBL; BC059257; AAH59257.1; -; mRNA.
DR   IPI; IPI00380409; -.
DR   IPI; IPI00608114; -.
DR   RefSeq; NP_997098.2; NM_207215.2.
DR   UniGene; Mm.6478; -.
DR   PDB; 3GBW; X-ray; 1.32 A; A=1191-1352.
DR   PDB; 3HWJ; X-ray; 2.25 A; A/B=1685-1845.
DR   PDBsum; 3GBW; -.
DR   PDBsum; 3HWJ; -.
DR   ProteinModelPortal; Q7TPH6; -.
DR   SMR; Q7TPH6; 491-678, 901-1028, 1189-1349, 1685-1844, 4452-4517.
DR   IntAct; Q7TPH6; 4.
DR   STRING; Q7TPH6; -.
DR   PhosphoSite; Q7TPH6; -.
DR   PRIDE; Q7TPH6; -.
DR   Ensembl; ENSMUST00000039876; ENSMUSP00000045930; ENSMUSG00000033004.
DR   GeneID; 105689; -.
DR   KEGG; mmu:105689; -.
DR   UCSC; uc007uwl.1; mouse.
DR   CTD; 105689; -.
DR   MGI; MGI:2179432; Mycbp2.
DR   eggNOG; roNOG08127; -.
DR   GeneTree; ENSGT00390000011403; -.
DR   HOGENOM; HBG358672; -.
DR   HOVERGEN; HBG053153; -.
DR   InParanoid; Q7TPH6; -.
DR   OrthoDB; EOG4VQ9NB; -.
DR   NextBio; 357830; -.
DR   ArrayExpress; Q7TPH6; -.
DR   Bgee; Q7TPH6; -.
DR   CleanEx; MM_MYCBP2; -.
DR   CleanEx; MM_PAM; -.
DR   Genevestigator; Q7TPH6; -.
DR   GermOnline; ENSMUSG00000033004; Mus musculus.
DR   GO; GO:0005680; C:anaphase-promoting complex; IEA:InterPro.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0021785; P:branchiomotor neuron axon guidance; IMP:MGI.
DR   GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IMP:MGI.
DR   GO; GO:0051493; P:regulation of cytoskeleton organization; IMP:MGI.
DR   GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IEA:InterPro.
DR   GO; GO:0032880; P:regulation of protein localization; IMP:MGI.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR004939; Ananphase-promot_cplx_su10_DOC.
DR   InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR012983; PHR.
DR   InterPro; IPR000408; Reg_chr_condens.
DR   InterPro; IPR009091; Reg_csome_cond/b-lactamase_inh.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Gene3D; G3DSA:2.130.10.30; Reg_csome_cond/b-lactamase_inh; 2.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00630; Filamin; 1.
DR   Pfam; PF08005; PHR; 2.
DR   Pfam; PF00415; RCC1; 1.
DR   PRINTS; PR00633; RCCNDNSATION.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF49785; Gal_bind_like; 1.
DR   SUPFAM; SSF81296; Ig_E-set; 1.
DR   SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR   PROSITE; PS51284; DOC; 1.
DR   PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR   PROSITE; PS00625; RCC1_1; FALSE_NEG.
DR   PROSITE; PS00626; RCC1_2; 1.
DR   PROSITE; PS50012; RCC1_3; 3.
DR   PROSITE; PS50119; ZF_BBOX; FALSE_NEG.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing;
KW   Direct protein sequencing; Ligase; Metal-binding; Nucleus;
KW   Phosphoprotein; Repeat; Transcription; Transcription regulation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1   4711       Probable E3 ubiquitin-protein ligase
FT                                MYCBP2.
FT                                /FTId=PRO_0000055964.
FT   REPEAT      562    617       RCC1 1.
FT   REPEAT      661    717       RCC1 2.
FT   REPEAT      869    919       RCC1 3.
FT   REPEAT      920    971       RCC1 4.
FT   REPEAT      973   1028       RCC1 5.
FT   REPEAT     2293   2400       Filamin.
FT   DOMAIN     3751   3929       DOC.
FT   ZN_FING    4461   4512       RING-type; atypical.
FT   ZN_FING    4615   4665       B box-type.
FT   COMPBIAS     65     88       Lys-rich.
FT   COMPBIAS    728    776       Cys-rich.
FT   COMPBIAS   2754   2878       Ser-rich.
FT   COMPBIAS   2847   2955       Pro-rich.
FT   COMPBIAS   3228   3248       Lys-rich.
FT   COMPBIAS   3296   3327       Gly-rich.
FT   MOD_RES     140    140       Phosphoserine (By similarity).
FT   MOD_RES     143    143       Phosphoserine (By similarity).
FT   MOD_RES     145    145       Phosphoserine (By similarity).
FT   MOD_RES    1583   1583       Phosphoserine.
FT   MOD_RES    1787   1787       N6-acetyllysine (By similarity).
FT   MOD_RES    2417   2417       N6-acetyllysine (By similarity).
FT   MOD_RES    2821   2821       Phosphoserine (By similarity).
FT   MOD_RES    2823   2823       Phosphoserine (By similarity).
FT   MOD_RES    2846   2846       Phosphoserine (By similarity).
FT   MOD_RES    2903   2903       Phosphoserine (By similarity).
FT   MOD_RES    2954   2954       Phosphoserine (By similarity).
FT   MOD_RES    3124   3124       Phosphoserine (By similarity).
FT   MOD_RES    3494   3494       Phosphoserine (By similarity).
FT   MOD_RES    3512   3512       Phosphoserine (By similarity).
FT   MOD_RES    3539   3539       Phosphoserine (By similarity).
FT   MOD_RES    3829   3829       Phosphoserine (By similarity).
FT   MOD_RES    3954   3954       Phosphothreonine.
FT   MOD_RES    3964   3964       Phosphoserine (By similarity).
FT   MOD_RES    3965   3965       Phosphoserine (By similarity).
FT   VAR_SEQ    3972   3974       Missing (in isoform 2).
FT                                /FTId=VSP_014184.
FT   CONFLICT   3647   3647       G -> E (in Ref. 3; AAH59257).
FT   CONFLICT   4598   4598       E -> G (in Ref. 3; AAH59257).
FT   STRAND     1194   1197
FT   STRAND     1214   1222
FT   STRAND     1224   1226
FT   STRAND     1238   1246
FT   STRAND     1260   1263
FT   STRAND     1267   1269
FT   STRAND     1285   1287
FT   STRAND     1292   1300
FT   STRAND     1313   1315
FT   STRAND     1321   1326
FT   STRAND     1343   1347
SQ   SEQUENCE   4711 AA;  517738 MW;  03C9A3975EED7552 CRC64;
     MPVPDGSVAA AGLGLGLPTT DSRGHYQLLL SGRALADRYR RIYTTALSDR DQAGSSTGHP
     ASRNKKILNK KKLKRKQKSK SKVKTRSKSE NVENTVIIPD IKLHSNPSAF NIYCNVRHCV
     LEWQKKETSL AAASKNSVQS GESDSDEEEE SREPPIKLPK IIEVGLCEVF ELIKETRFSH
     PSLCLRSLQA LLNVLQGQQP EGLQSEPPEV LESLFQLLLE ITVRSTGMND STGQSLTALS
     CACLFSLVAS WGETGRTLQA ISAILTNNGS HACQTIQVPT ILNSLQRSVQ AVLVGKIQVQ
     DWFSNGIKKA ALMHKWPLKE VSVDEDDQCL LQNDGFFLYL LCKDGLYKIG SGYSGTVRGH
     IYNSTSRIRN RKEKKSWLGY AQGYLLYRDL NNHSMTAIRI SPETLEQDGT VLLPDCHTEG
     QNILFTDGEY INQIAASRDD GFVVRIFATS TEPVLQQELQ LKLARKCLHA CGISLFDLEK
     DLHIISTGFD EESAILGAGR EFALMKTANG KIYYTGKYQS LGIKQGGPSA GKWVELPITK
     SPKIVHFSVG HDGSHALLVA EDGSVFFTGS ASKGEDGEST KSRRQSKPYK PKKIIKMEGK
     IVVYTACNNG SSSVISKDGE LYMFGKDAIY SDSSSLVSDL KGHFVTQVAM GKAHTCVLMK
     NGEVWTFGVN NKGQCGRDTG AMNQGGKGFG VENMATAMDE DLEEELDEKD EKSMMCPPGM
     HKWKLEQCMV CTVCGDCTGY GASCVSSGRP DRVPGGICGC GSGESGCAVC GCCKACAREL
     DGQEARQRGI LDAVKEMIPL DLLLAVPVPG VNIEEHLQLR QKEKRQRVIR RHRLEDGRGP
     LVFAGPIFMN HREQALARLR SHPAQLKHKR DKHKDGSGDR GEKDASKITT YPPGSVRFDC
     ELRAVQVSCG FHHSVVLMEN GDVYTFGYGQ HGQLGHGDVN SRGCPTLVQA LPGPSTQVTA
     CSNHTAVLLM DGQVFTFGSF SKGQLGRPIL DIPYWNAKPA PMPNIGSKYG RKATWIGASG
     DQTFLRIDEA LINSHVLATS EIFASKHIIG LVPASISEPP PFKCLLINKV DGSCKTFNDS
     EQEDLQGFGV CLDPVYDVLW RFRPSTRELW CYNAVVADAR LPSATDMQSR CSILSPELAL
     PTGSRALTTR SHAALHILGC LDTLAAMQDL KMGIASTEEE TQAVMKVYSK EDYSVVNRFE
     SHGGGWGYSA HSVEAIRFSA DTDILLGGLG LFGGRGEYTA KIKLFELGPD GGDHETDGDL
     LAETDVLAYD CAAREKYAMM FDEPVLLQAG WWYVAWARVS GPSSDCGSHG QASITTDDGV
     IFQFKSSKKS NNGTDVNAGQ IPQLLYRLPT SDGSTSKGKQ QTSEPVHILK RSFARTVSVE
     CFESLLSILH WSWTTLVLGV EELRGLKGFQ FTATLLDLER LRFVGTCCLR LLRVYTCEIY
     PVSATGKAVV EETSKLAECI GKTRTLLRKI LSEGVDHCMV KLDNDPQGYL SQPLRLLEAV
     LQECHNTFTA CFHSFYPTPA LQWACLCDLL NCLDQEANFK TSSSRLLAAV MSALCHTSVK
     LTSLFPIAYD GEVLLRSIVK QVSTENDSTL VHRFPLLVGH MEKLSQSEEN ISGMTSFREV
     LEKMLVIVVL PVRNSLRRES ELFSSHLVSN TCGLLASIVS ELTASALGSE VDGLNSLHSV
     KASANRFTKT SQGRSWNTGN GSPDAICFAV DKPGIVVVGF AVYGGGGIHE YELEVLVDDS
     EHAGDSTHSH RWTSLELVKG TYTTDDSPSD IAEIRLDKVV PLKENVKYAV RLSNYGSRTA
     NGDGGMTTVQ CPDGVTFTFS TCSLSSNGTN QTRGQIPQIL YYRSEFDGDL QSQLLSKANE
     EDKNCSRALS VVSTVVRAAK DLLHRALAVD ADDIPELLSS SSLFSMLLPL IIAYIGPVAA
     AIPKVAVEVF GLVQQLLPSV AILNQKYASP AFNPNQSTDS TTGNQPEQGL SACTTSNHYA
     VIESEHPYKP ACVMHYKVTF PECVRWMTIE FDPQCGTAQS EDVIRLLIPV RTIQNSGYGA
     KLTSVHENLN SWVELKKYSG SSGWPTMVLV LPGNEALFSL ETASDYVKDD KASFYGFKCF
     AIGYEFSPGP DEGVIQLEKE LANLGGVCAA ALMKKDLALP VGNELEEDLE ILEEAALQVC
     KTHSGILGKG LALSHSPTIL EALEGNLPLQ IQSNEQSFLD DFIACVPGSS GGRLARWLQP
     DSYADPQKTS LILNKDDIRC GWPTTITVQT KDQYGDVVHV PNMKVEVKAV PVSQKKTSLQ
     QDQGKKCQRI PGSPSAAASS ADMTFGGLAS PKLDVSYEPM IVKEARYIAI TMMKVYENYS
     FEELRFASPT PKRPSENMLI RVNNDGTYCA NWTPGAIGLY TVHVTIDGIE IDAGLEVKVK
     DPPKGMIPPG TQLVKPKADP QPNKIRKFVA KDSAGLRIRS HPSLQSEQIG IVRVNGTITF
     IDEIHNDDGV WLRLNEETIK KYVPNMNGYT EAWCLSFNQH LGKSLLVPVD NIFNASQGVR
     DLDVFSWTSK AFFPQEPKTN TDDFFKDMNS CGPQEATMQE RDHPFLRGGP GMYKVVKTGP
     SGHNIRSCPN LRGIPIGMLV LGNKVKAVGE VTNSEGAWVQ LDKNSMVEFC ESDEGEAWSL
     ARDRGGNQYL RHEDEQVLLD QNSQPPPPSP FSVQAFNKGA SCSAQGFDYG LGNNKGDQLS
     AILNSIQSRP NLPAPSIFDQ AAKPPSSLVH SPFVFGQPLS FQQRQLQSDR GTISTSSRPV
     STSGKSELPS KHSRSVKPDG HVSRTPADQK KPRGTEGLSA SESLMLKSDA AKLRSDSHSR
     SLSPNHNTLQ TLKSDGRTSS GFRAESPGPG SRSSSPKPKP LPTPRSSPSG ASSPRSSSPQ
     DKNLPQKSTA PAKTKLDPPR ERSKSDSYTL DPDTLRKKKM PLTEPLRGRS TSPKPKPVPK
     DPKDSPGSEN RAPSPHVVQE NLHSEVVEVC TSSTLKTNGV TDSTCDDSGD LKSVDEGSNK
     VHFSIGKAPL KDEQEMRASP KISRKCANRH TRPKKEKSNF LFKGDGTKSL EPAKQAMSPS
     VAECARAVFA SFLWHEGIVH DAMACSSFLK FNPDLSKEHA PIRSSLNSQP PTEEKEIKLK
     NRHSLEISSA LNMFNIAPHG PDISKMGSIN KNKVLSMLKE PPLHEKCEDG KSEATFEMSM
     HHTMKSKSPL PLTLQHLVAF WEDISLATIK AASQNMIFPS PGSCAVLKKK ECEKENKKTK
     KEKKKKEKTE IRPRGNLFGE MAQLAVGGPE KDTICELCGE SHPYPVTYHM RQAHPGCGRY
     AGGQGYNSIG HFCGGWAGNC GDGGMGGSTW YLVCDRCREK YLREKQAAAR EKVKQSRRKP
     MQVKTPRALP TMEAHQVIKA NALFLLSLSS AAEPSILCYH PAKPFQSQLP IVKEGVSEDL
     PVKMPCLYLQ TLARHHHENF VGYQDDNLFQ DEMRYLRSTS VPAPYISVTP DASPNVFEEP
     ESNMKSMPPS LETSPITDTD LAKRTVFQRS YSVVASEYDK QHSILPARVK AIPRRRVNSG
     DTVGSSLLRH PSPELSRLIS AHSSLSKGER NFQWPVLAFV IQHHDLEGLE IAMKQALRKS
     ACRVFAMEAF NWLLCNVIQT TSLHDILWHF VAALTPSPVE AEEDEDGDNK SNKENAEQEK
     DTRVCEHPLS DIVIAGEAAH PLPHTFHRLL QTISDLMMSL PSGSSLQQMA LRCWSLKFKQ
     SDHQFLHQSN VFHHINNILS KSDDGDSEES FSISVQSGFE AMSQELCIVM CLKDLTSIVD
     IKTSSRPAMI GSLTDGSTET FWESGDEDKN KTKNITINCV KGINARYVSV HVDNSRDLGN
     KVTSMTFLTG KAVEELCRIK QVDLDSRHIG WVTSELPGGD NQIIKIELKG PENTLRVRQV
     KVLGWKDGES TKIAGQISAS VAQQRSCEAE TLRVFRLITS QVFGKLISGD AEPTPEQEEK
     ALLSSPEGEE KVYNATSDAD LKEHMVGIIF SRSKLTNLQK QVCAHIVQAI RMEATRVREE
     WEHAISSKEN ANSQPSDEDA SSDAYCFELL SMVLALSGSN VGRQYLAQQL TLLQDLFSLL
     HTASPRVQRQ VTSLLRRVLP EVTPNRLASI IGVKSLPPAD ISDIIHSTEK GDWNKLGILD
     MFLGCIAKAL TVQLKAKGTT ITGTAGTTVG KGVTTVTLPM IFNSSYLRRG ESHWWMKGST
     PTQISEIIIR LIKDMAAGHL SEAWSRVTKN AIAETIIALT KMEEEFRSPV RCIATTRLWL
     ALASLCVLDQ DHVDRLSSGR WMGKDGQQKQ MPMCDNHDDG ETAAIILCNI CGNLCTDCDR
     FLHLHRRTKT HQRQVFKEEE EAIKVDLHEG CGRTKLFWLM ALADSKTMKA MVEFREHTGK
     PTTSSSEACR FCGSRSGTEL SAVGSVCSDA DCQEYAKIAC SKTHPCGHPC GGVRNEEHCL
     PCLHGCDKSA TTLKQDADDM CMICFTEALS AAPAIQLDCS HVFHLQCCRR VLENRWLGPR
     ITFGFISCPI CKNKINHIVL KDLLDPIKEL YEDVRRKALM RLEYEGLHKS EAITTPGVRF
     YNDAAGYAMN RYAYYVCYKC RKAYFGGEAR CDAEAGQEDD YDPRELICGA CSDVSRAQMC
     PKHGTDFLEY KCRYCCSVAV FFCFGTTHFC NACHDDFQRM TSIPKEELPH CPAGPKGKQL
     EGTECPLHVV HPPTGEEFAL GCGVCRNAHT F
//
ID   PRC2B_MOUSE             Reviewed;        1486 AA.
AC   Q7TPM1; A2AN31; Q8C755;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Protein PRRC2B;
DE   AltName: Full=HLA-B-associated transcript 2-like 1;
DE   AltName: Full=Proline-rich coiled-coil protein 2B;
GN   Name=Prrc2b; Synonyms=Bat2l, Bat2l1, Kiaa0515;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621 AND SER-1007, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7TPM1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TPM1-2; Sequence=VSP_022764, VSP_022765;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK052511; BAC35022.1; -; mRNA.
DR   EMBL; AL808027; CAM15833.1; -; Genomic_DNA.
DR   EMBL; BC055116; AAH55116.1; -; mRNA.
DR   IPI; IPI00380415; -.
DR   IPI; IPI00405591; -.
DR   RefSeq; NP_001153106.1; NM_001159634.1.
DR   RefSeq; NP_766249.2; NM_172661.3.
DR   UniGene; Mm.25504; -.
DR   PhosphoSite; Q7TPM1; -.
DR   PRIDE; Q7TPM1; -.
DR   Ensembl; ENSMUST00000036691; ENSMUSP00000035734; ENSMUSG00000039262.
DR   Ensembl; ENSMUST00000069817; ENSMUSP00000064892; ENSMUSG00000039262.
DR   GeneID; 227723; -.
DR   KEGG; mmu:227723; -.
DR   UCSC; uc008jem.1; mouse.
DR   CTD; 227723; -.
DR   MGI; MGI:1923304; Prrc2b.
DR   GeneTree; ENSGT00530000063496; -.
DR   HOVERGEN; HBG095505; -.
DR   OrthoDB; EOG4MSCXD; -.
DR   PhylomeDB; Q7TPM1; -.
DR   NextBio; 378792; -.
DR   PMAP-CutDB; Q7TPM1; -.
DR   ArrayExpress; Q7TPM1; -.
DR   Bgee; Q7TPM1; -.
DR   Genevestigator; Q7TPM1; -.
DR   InterPro; IPR009738; BAT2_N.
DR   Pfam; PF07001; BAT2_N; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Isopeptide bond; Phosphoprotein;
KW   Ubl conjugation.
FT   CHAIN         1   1486       Protein PRRC2B.
FT                                /FTId=PRO_0000274482.
FT   COILED      494    544       Potential.
FT   COILED      880    904       Potential.
FT   COMPBIAS    600    611       Ser-rich.
FT   COMPBIAS    638    664       Gln-rich.
FT   MOD_RES     166    166       Phosphoserine (By similarity).
FT   MOD_RES     168    168       Phosphoserine (By similarity).
FT   MOD_RES     224    224       Phosphoserine (By similarity).
FT   MOD_RES     226    226       Phosphoserine (By similarity).
FT   MOD_RES     387    387       Phosphoserine.
FT   MOD_RES     415    415       Phosphoserine (By similarity).
FT   MOD_RES     621    621       Phosphoserine.
FT   MOD_RES     753    753       Phosphothreonine (By similarity).
FT   MOD_RES     762    762       Phosphoserine (By similarity).
FT   MOD_RES     793    793       Phosphoserine (By similarity).
FT   MOD_RES     806    806       Phosphoserine (By similarity).
FT   MOD_RES     808    808       Phosphotyrosine (By similarity).
FT   MOD_RES    1007   1007       Phosphoserine.
FT   MOD_RES    1159   1159       Phosphoserine (By similarity).
FT   CROSSLNK    827    827       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   VAR_SEQ       1    766       Missing (in isoform 2).
FT                                /FTId=VSP_022764.
FT   VAR_SEQ    1475   1486       QSEWMKNPAWEP -> PSSASPSGKPSGSAVNMGSVQGHYV
FT                                QQAKRVDEKPGLGTVKLQEASSATSQMKRTGAIKPRAVKVE
FT                                GSKA (in isoform 2).
FT                                /FTId=VSP_022765.
FT   CONFLICT   1342   1342       P -> S (in Ref. 1; BAC35022).
SQ   SEQUENCE   1486 AA;  160913 MW;  53BF3D0BD583D731 CRC64;
     MSDRLGQITQ GKDGKSKYST LSLFDKYKGR SVGAVRSSVI PRHGLQSLGK VATARRMPPP
     ANLPSLKSEN KGNDPNIVIV PKDGTGWANK QDQQDPKSSS VTASQPPESQ PQPGLQKSVS
     NLQKPTQSIS QENTNSVPGG PKSWAQLSGK PVGHEGGLRG SSRLLSFSPE EFPTLKAAGG
     QDKAGKEKGA LDLSYGPGPS LRPQNVTSWR EGGGRNIISA ASLSASPTEL GSRNASGADG
     APSLACTSDS KEPSLRPAQP SRRGASQFMG HGYQPPTYHD MLPAFMCSPQ SSENQTTVER
     SSFPLPQLRL EPRVPFRQFQ MNDQDGKERP GVARPVRPLR QLVERAPRPT IINAENLKGL
     DDLDTDADDG WAGLHEEVDY SEKLKFSDDE DEEDVVKDGR SKWNNWDPRR QRALSLSSAD
     STDAKRTQEE GKDWSGTAGG SRVIRKVPEP QPPSRKLHSW ASGPDYQKPT MGSMFRQHSA
     EDKEDKPPPR QKFIQSEMSE AVERARKRRE EEERRAREER LAACAAKLKQ LDQKCRQAQK
     ANETPKPVEK EVPRSPGIEK VSPPENGPVV RKGSPEFPVQ EAPTMFLEET PATSPTVAQS
     NSSSSSSSSS SIEEEVRESG SPAQEFSKYQ KSLPPRFQRQ QQQQQQQQQQ QQQQEQLYKM
     QHWQPVYPPP SHPQRTFYPH HPQMLGFDPR WMMMPSYMDP RITPTRTPVD FYPSALHPSG
     LMKPMMPQES LSGTGCRSED QNCVPSLQER KVTALDPAPV WSPEGYMALQ NKGYSLPHPK
     SADTLAMGMH VRSPDEALPG GLGSHSPYAL ERTTHASSDG PETPSKKSER EVSLPTQRAS
     EQEEARKQFD LGYGNALIDN CASSPGEENE ASSVVGEGFI EVLTKKQRRL LEEERRKKEQ
     AAQVPVKGRG LSSRIPPRFA KKQNGLCLEQ DVTVPGSSLG TEIWENSSQA LPVQGAASDS
     WRTAVTAFSS TEPGTSEQGF KSSQGDSGVD LSAESRESSA TSSQRSSPYG TLKPEEISGP
     GLAESKADSH KDQAQKQAEH KDSEQGSAQS KEHRPGPIGN ERSLKNRKGS EGAERLPGAV
     VPPVNGVEIH VDSVLPVPPI EFGVSPKDSD FSLPPGSVSG PVGNPVAKLQ DVLASNAGLT
     QSIPILRRDH HMQRAIGLSP MSFPTADLTL KMESARKAWE NSPSLPEQSS PGGAGSGIQP
     PSSVGASNGV NYSSFGGVSM PPMPVASVAP SASIPGSHLP PLYLDGHVFA SQPRLVPQTI
     PQQQSYQQAA TAQQIPISLH TSLQAQAQLG LRGGLPVSQS QEIFSSLQPF RSQVYMHPSL
     SPPSTMILSG GTALKPPYSA FPGIQPLEMV KPQSGSPYQP MSGNQALVYE GQLGQAAGLG
     TSQMLDSQLP QLTMPLPRYG SGQQPLILPQ SIQLPPGQSL SVGAPRRVPP PGSQPPVLNT
     SRESAPMELK GFHFADSKQN VPTGGSAPSP QAYRQSEWMK NPAWEP
//
ID   FSD1_MOUSE              Reviewed;         496 AA.
AC   Q7TPM6; Q3UNE6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Fibronectin type III and SPRY domain-containing protein 1;
GN   Name=Fsd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in microtubule organization and
CC       stabilization (By similarity).
CC   -!- SUBUNIT: Oligomerization is required for binding to microtubules
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome (By
CC       similarity). Nucleus (By similarity). Cytoplasm (By similarity).
CC       Cleavage furrow (By similarity). Note=Cell-cycle-dependent
CC       association with the centrosome. Colocalizes with a subpopulation
CC       of microtubules. Does not associates with microtubules during
CC       mitosis but reassociates with microtubules during cytokinesis.
CC       Localizes to the central portions of a small subset of
CC       microtubules in interphase cells and a subpopulation of
CC       microtubules in the cleavage furrow, not present in the mitotic
CC       spindle (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7TPM6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TPM6-2; Sequence=VSP_030767;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: B30.2 box contains a microtubule-binding site.
CC   -!- SIMILARITY: Contains 1 B30.2/SPRY domain.
CC   -!- SIMILARITY: Contains 1 COS domain.
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK140132; BAE24249.1; -; mRNA.
DR   EMBL; AK144257; BAE25801.1; -; mRNA.
DR   EMBL; BC055106; AAH55106.1; -; mRNA.
DR   IPI; IPI00338998; -.
DR   IPI; IPI00886318; -.
DR   RefSeq; NP_899001.1; NM_183178.2.
DR   UniGene; Mm.270660; -.
DR   HSSP; Q92859; 1X5F.
DR   ProteinModelPortal; Q7TPM6; -.
DR   SMR; Q7TPM6; 164-260.
DR   STRING; Q7TPM6; -.
DR   PhosphoSite; Q7TPM6; -.
DR   PRIDE; Q7TPM6; -.
DR   Ensembl; ENSMUST00000011733; ENSMUSP00000011733; ENSMUSG00000011589.
DR   GeneID; 240121; -.
DR   KEGG; mmu:240121; -.
DR   UCSC; uc008dan.1; mouse.
DR   CTD; 240121; -.
DR   MGI; MGI:1934858; Fsd1.
DR   eggNOG; roNOG05432; -.
DR   GeneTree; ENSGT00560000076722; -.
DR   HOGENOM; HBG446524; -.
DR   HOVERGEN; HBG107931; -.
DR   InParanoid; Q7TPM6; -.
DR   OMA; AKHANKA; -.
DR   OrthoDB; EOG4B5P50; -.
DR   NextBio; 384472; -.
DR   ArrayExpress; Q7TPM6; -.
DR   Bgee; Q7TPM6; -.
DR   Genevestigator; Q7TPM6; -.
DR   GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   InterPro; IPR001870; B302/SPRY.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR017903; COS_domain.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003877; SPRY_rcpt.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00060; FN3; 1.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
DR   SUPFAM; SSF49265; FN_III-like; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS51262; COS; 1.
DR   PROSITE; PS50853; FN3; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell cycle; Cell division; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Microtubule; Mitosis; Nucleus;
KW   Phosphoprotein.
FT   CHAIN         1    496       Fibronectin type III and SPRY domain-
FT                                containing protein 1.
FT                                /FTId=PRO_0000316539.
FT   DOMAIN      105    162       COS.
FT   DOMAIN      165    267       Fibronectin type-III.
FT   DOMAIN      290    477       B30.2/SPRY.
FT   COILED        4     99       Potential.
FT   MOD_RES     313    313       Phosphoserine (By similarity).
FT   MOD_RES     317    317       Phosphoserine (By similarity).
FT   MOD_RES     324    324       Phosphoserine (By similarity).
FT   VAR_SEQ      81     97       Missing (in isoform 2).
FT                                /FTId=VSP_030767.
SQ   SEQUENCE   496 AA;  55525 MW;  A5CBCBDA3015E8FF CRC64;
     MEDQREALRK IITTLAMKNE ETQTFIYSLK QMLLNVEANS AKVQEDLEAE FQSLTSVLEE
     LKESMLMKIK QDRASRTYEL QNQLAACTRA LESSEELLET ANQTLQASDS EDFSQAAKEI
     KDGITMAPAF RLSLKAKVSD NMSHLMVDFA QERQMLQALK FLPVPSAPTI DLAESLVSDN
     CVTLVWHMPD EDSKIDHYVL EYRKTNFEGP PRLKEDHPWM VVEGIRQTEH TLTGLKFDMK
     YMNIRVKACN KAVAGEFSEP VTLETPAFMF RLDGSTSHQN LRVEDLSAEW DAMGGKVQDI
     KAREKEGKGR TASPVNSPAR GTPSPKRMSS GRGGRDRFTA ESYTVLGDTL IDGGEHYWEV
     RFEPDSKAFG LGVAYRSLGR FEQLGKTAAS WCLHANNWLQ ASFTAKHANK VKVLDSPVPD
     CLGVHCDFHQ GLLSFYNART KQLLHTFKAK FTQPLLPAFT VWCGSFQVTT GLQVPSAVRC
     LQKRGSATSS SNTSLT
//
ID   K0528_MOUSE             Reviewed;        1016 AA.
AC   Q7TPS5; Q3TQY6; Q6A052; Q80VA1; Q8C0U3; Q8CID5; Q9CS85;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Uncharacterized protein KIAA0528;
GN   Name=Kiaa0528;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 710-1016 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Egg, Embryo, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 513-1016 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Egg, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-659, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260 AND SER-262, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q7TPS5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TPS5-2; Sequence=VSP_019992, VSP_019993;
CC       Name=3;
CC         IsoId=Q7TPS5-3; Sequence=VSP_019991;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32244.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK172966; BAD32244.1; ALT_INIT; mRNA.
DR   EMBL; AK017577; BAB30814.1; -; mRNA.
DR   EMBL; AK029825; BAC26634.1; -; mRNA.
DR   EMBL; AK163233; BAE37246.1; -; mRNA.
DR   EMBL; BC027763; AAH27763.1; -; mRNA.
DR   EMBL; BC049905; AAH49905.1; -; mRNA.
DR   EMBL; BC053913; AAH53913.1; -; mRNA.
DR   IPI; IPI00408171; -.
DR   IPI; IPI00462743; -.
DR   IPI; IPI00776032; -.
DR   RefSeq; NP_001103158.1; NM_001109688.1.
DR   RefSeq; NP_083357.2; NM_029081.2.
DR   RefSeq; NP_084173.1; NM_029897.1.
DR   UniGene; Mm.130260; -.
DR   ProteinModelPortal; Q7TPS5; -.
DR   SMR; Q7TPS5; 3-96, 700-725.
DR   PhosphoSite; Q7TPS5; -.
DR   PRIDE; Q7TPS5; -.
DR   Ensembl; ENSMUST00000087485; ENSMUSP00000084758; ENSMUSG00000030279.
DR   Ensembl; ENSMUST00000111758; ENSMUSP00000107388; ENSMUSG00000030279.
DR   GeneID; 74741; -.
DR   KEGG; mmu:74741; -.
DR   UCSC; uc009epx.1; mouse.
DR   UCSC; uc009epy.1; mouse.
DR   UCSC; uc009epz.1; mouse.
DR   MGI; MGI:1921991; 5730419I09Rik.
DR   eggNOG; roNOG12014; -.
DR   GeneTree; ENSGT00390000000212; -.
DR   HOVERGEN; HBG081824; -.
DR   InParanoid; Q7TPS5; -.
DR   OMA; AVIIHGF; -.
DR   OrthoDB; EOG4C2H8T; -.
DR   PhylomeDB; Q7TPS5; -.
DR   NextBio; 341536; -.
DR   ArrayExpress; Q7TPS5; -.
DR   Bgee; Q7TPS5; -.
DR   CleanEx; MM_5730419I09RIK; -.
DR   Genevestigator; Q7TPS5; -.
DR   GermOnline; ENSMUSG00000030279; Mus musculus.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   Pfam; PF00168; C2; 1.
DR   SMART; SM00239; C2; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   PROSITE; PS50004; C2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1   1016       Uncharacterized protein KIAA0528.
FT                                /FTId=PRO_0000247451.
FT   DOMAIN        1     90       C2.
FT   MOD_RES     249    249       Phosphoserine (By similarity).
FT   MOD_RES     250    250       Phosphoserine (By similarity).
FT   MOD_RES     260    260       Phosphoserine.
FT   MOD_RES     262    262       Phosphoserine.
FT   MOD_RES     278    278       Phosphothreonine (By similarity).
FT   MOD_RES     280    280       Phosphoserine (By similarity).
FT   MOD_RES     281    281       Phosphoserine (By similarity).
FT   MOD_RES     284    284       Phosphoserine (By similarity).
FT   MOD_RES     292    292       Phosphotyrosine (By similarity).
FT   MOD_RES     293    293       Phosphoserine (By similarity).
FT   MOD_RES     295    295       Phosphoserine (By similarity).
FT   MOD_RES     304    304       Phosphoserine (By similarity).
FT   MOD_RES     305    305       Phosphoserine (By similarity).
FT   MOD_RES     306    306       Phosphoserine (By similarity).
FT   MOD_RES     307    307       Phosphoserine (By similarity).
FT   MOD_RES     314    314       Phosphothreonine (By similarity).
FT   MOD_RES     317    317       Phosphothreonine (By similarity).
FT   MOD_RES     321    321       Phosphoserine (By similarity).
FT   MOD_RES     323    323       Phosphoserine (By similarity).
FT   MOD_RES     339    339       Phosphothreonine (By similarity).
FT   MOD_RES     601    601       Phosphothreonine (By similarity).
FT   MOD_RES     606    606       Phosphoserine (By similarity).
FT   MOD_RES     637    637       Phosphoserine (By similarity).
FT   MOD_RES     643    643       Phosphoserine (By similarity).
FT   MOD_RES     657    657       Phosphoserine (By similarity).
FT   MOD_RES     659    659       Phosphoserine.
FT   MOD_RES     661    661       Phosphoserine (By similarity).
FT   MOD_RES     662    662       Phosphoserine (By similarity).
FT   MOD_RES     671    671       Phosphoserine (By similarity).
FT   MOD_RES     812    812       Phosphoserine (By similarity).
FT   MOD_RES     817    817       Phosphoserine (By similarity).
FT   MOD_RES     864    864       Phosphothreonine (By similarity).
FT   MOD_RES     869    869       Phosphoserine (By similarity).
FT   VAR_SEQ       1    198       Missing (in isoform 3).
FT                                /FTId=VSP_019991.
FT   VAR_SEQ     268    316       IPFNEDPNPNTHSSGPSTPLKNQTYSFSPSKSYSRQSSSSD
FT                                TDLSLTPK -> SPLVHPPSHGCRSTHNSPIHTATGSRLTQ
FT                                NFSVSVPTLIY (in isoform 2).
FT                                /FTId=VSP_019992.
FT   VAR_SEQ     845    861       Missing (in isoform 2).
FT                                /FTId=VSP_019993.
FT   CONFLICT     11     11       A -> S (in Ref. 2; BAC26634).
FT   CONFLICT    590    590       P -> T (in Ref. 2; BAC26634).
FT   CONFLICT    632    632       T -> S (in Ref. 1; BAD32244 and 3;
FT                                AAH27763/AAH49905).
FT   CONFLICT    793    793       A -> V (in Ref. 3; AAH53913).
FT   CONFLICT    868    868       A -> T (in Ref. 2; BAB30814).
SQ   SEQUENCE   1016 AA;  111664 MW;  A1E3614203DFCD03 CRC64;
     MPGKLKVKIV AGRHLPVMDR ASDLTDAFVE VKFGNTTFKT DVYLKSLNPQ WNSEWFKFEV
     DDEDLQDEPL QITVLDHDTY SANDAIGKVY IDIDPLLYSE AATVISGWFP IYDTIHGIRG
     EINVVVKVDL FNDSNRFRQS SCGVKFFCTT SIPKCYRAVV IHGFVEELVV NEDPEYQWID
     RIRTPRASNE ARQRLISLMS GELQRKIGLK VLEMRGNAVV GYLQCFDLEG ESGLVVRAIG
     TACTLDKLSS PAAFLPACSS PSRELKEIPF NEDPNPNTHS SGPSTPLKNQ TYSFSPSKSY
     SRQSSSSDTD LSLTPKTGMG SGSAGKEGGP FKALLRQQTQ SALEQREFPF LTLTAFPPGL
     LVHVGGVVSA RSVKLLDRIH NPDEPETRDA WWAEIRQEIK SHAKALGCHA VVGYSESTSI
     CEEVCILSAS GTAAVLNPRF LQEGTVEGCL EQRIEENLPV GCGFCHIPYD ELNMPFPAHL
     TYCYNCRKQK VPDVLFTTID LPTDAVVVGK GCLIQARLCR LKKKAQAEAN ATAISNLLPF
     MEYEVHTQLM NKLKLKGMNA LFGLRIQITV GETMLMGLAS ATGVYLAALP TPGGIQIAGK
     TPNDGSYEQH ISHMQKRIND TIAKNKELYE ITPPEVSEEM IGSPIPEPRQ RSRLLRSQSE
     SSDEVTELDL SHGKKDAFVL EIDDTDAMED VHSLLTDAPP PSGFYSCNTE IMPGINNWTS
     EIQMFTSVRV VRLSSLNLTN QALNKNFNGL CENLLKSLYF KLRSMTPCCL CHVNFTVSLP
     EDELIQVTVT AVAITFDKNQ ALQTTKPHVE KSLQRASTDN EELLQFPLEL CSDSLPPHPF
     PAAKEHLESA NSNSGIPAAQ RAVTVEKASA MGDGNFRNRS APPCASPTVG VVKMTPLSFI
     PGAKITKYLG IINMFFIRET TSLREEGGVS GFLHAFIAEV FAMVRAHVAA LGGNAVVSYI
     MKQCVFMENP SKNQAQCLIN VSGDAVVFVR DSDLEVMSSQ QPAANCQPSC TGEVTT
//
ID   DZIP3_MOUSE             Reviewed;        1204 AA.
AC   Q7TPV2; Q148V3; Q80TU4; Q8BYK7;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=E3 ubiquitin-protein ligase DZIP3;
DE            EC=6.3.2.-;
DE   AltName: Full=DAZ-interacting protein 3 homolog;
GN   Name=Dzip3; Synonyms=Kiaa0675;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C3H/He; TISSUE=Osteoblast;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-787 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 767-1133 (ISOFORM 1).
RC   TISSUE=Head, and Retina;
RG   The MGC Project Team;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1062-1204 (ISOFORM 1).
RA   Tanaka T.S., Jaradat S.A., Lim M.K., Kargul G.J., Wang X.,
RA   Grahovac M.J., Pantano S., Sano Y., Piao Y., Nagaraja R., Doi H.,
RA   Wood W.H. III, Becker K.G., Ko M.S.H.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E3 Ubiquitin ligase proteins mediate ubiquitination and
CC       subsequent proteasomal degradation of target proteins. E3
CC       ubiquitin ligases accept ubiquitin from an E2 ubiquitin-
CC       conjugating enzyme in the form of a thioester and then directly
CC       transfers the ubiquitin to targeted substrates. Able to
CC       specifically bind RNA (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Probably interacts with DAZL (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q7TPV2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TPV2-2; Sequence=VSP_010977;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q7TPV2-3; Sequence=VSP_010973, VSP_010974, VSP_010975,
CC                                  VSP_010976;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65626.1; Type=Erroneous initiation;
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DR   EMBL; AK122344; BAC65626.1; ALT_INIT; mRNA.
DR   EMBL; BC052893; AAH52893.1; -; mRNA.
DR   EMBL; BC117953; AAI17954.1; -; mRNA.
DR   EMBL; BC117954; AAI17955.1; -; mRNA.
DR   EMBL; AK039172; BAC30265.1; -; mRNA.
DR   EMBL; BI736207; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; CN535823; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BG070132; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00330236; -.
DR   IPI; IPI00453804; -.
DR   IPI; IPI00453805; -.
DR   RefSeq; NP_001103487.1; NM_001110017.1.
DR   RefSeq; NP_081617.1; NM_027341.2.
DR   UniGene; Mm.275138; -.
DR   ProteinModelPortal; Q7TPV2; -.
DR   SMR; Q7TPV2; 1139-1187.
DR   STRING; Q7TPV2; -.
DR   PhosphoSite; Q7TPV2; -.
DR   PRIDE; Q7TPV2; -.
DR   Ensembl; ENSMUST00000023327; ENSMUSP00000023327; ENSMUSG00000064061.
DR   Ensembl; ENSMUST00000121869; ENSMUSP00000113344; ENSMUSG00000064061.
DR   GeneID; 224170; -.
DR   KEGG; mmu:224170; -.
DR   UCSC; uc007zjy.1; mouse.
DR   UCSC; uc007zjz.1; mouse.
DR   CTD; 224170; -.
DR   MGI; MGI:1917433; Dzip3.
DR   eggNOG; roNOG04971; -.
DR   GeneTree; ENSGT00530000063254; -.
DR   HOGENOM; HBG125515; -.
DR   HOVERGEN; HBG051428; -.
DR   InParanoid; Q7TPV2; -.
DR   OrthoDB; EOG4V1700; -.
DR   ArrayExpress; Q7TPV2; -.
DR   Bgee; Q7TPV2; -.
DR   CleanEx; MM_DZIP3; -.
DR   Genevestigator; Q7TPV2; -.
DR   GermOnline; ENSMUSG00000064061; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Ligase; Metal-binding;
KW   RNA-binding; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1   1204       E3 ubiquitin-protein ligase DZIP3.
FT                                /FTId=PRO_0000055899.
FT   ZN_FING    1144   1184       RING-type; atypical.
FT   COILED      746    861       Potential.
FT   COILED      906    941       Potential.
FT   COMPBIAS    657    664       Poly-Lys.
FT   COMPBIAS    954    960       Poly-Pro.
FT   COMPBIAS   1137   1142       Poly-Glu.
FT   VAR_SEQ       1    889       Missing (in isoform 3).
FT                                /FTId=VSP_010973.
FT   VAR_SEQ     382    587       Missing (in isoform 2).
FT                                /FTId=VSP_010977.
FT   VAR_SEQ     890    899       QLARVTHMAA -> MFPLCLLFYI (in isoform 3).
FT                                /FTId=VSP_010974.
FT   VAR_SEQ    1135   1153       DNEEEEEEPCVICHENLSP -> VRPNLLTVNTFRSERKRM
FT                                V (in isoform 3).
FT                                /FTId=VSP_010975.
FT   VAR_SEQ    1154   1204       Missing (in isoform 3).
FT                                /FTId=VSP_010976.
FT   CONFLICT    306    306       D -> G (in Ref. 2; AAH52893).
FT   CONFLICT    650    650       V -> I (in Ref. 2; AAH52893).
SQ   SEQUENCE   1204 AA;  138021 MW;  9522730708DB570C CRC64;
     MDSLAEEFFV SGNPDVEEQT KEETEIIAEK PVTQLDKQKM DISADPEPVN ALLEIKKVLN
     PISALPKGVF PNIEKFIQED FSFQTMQREV TTHSQTGEEI VPALTLHFLI TQLEMALRNI
     QASNYTAQQI NVGYYLTLLF LYGVALTERA KKEDCIEAEN KFLVMKMVIQ ESEICENFMC
     LVYFGRGLLR CAQKRYNGAL LEFYKSLQEI GDTDDNWFEV DPTDDEDLPT TFKDSLNNFI
     KTTESNIMKE TICSYLDCER SCEADILKNT NYKGFFQLMC SKSCCIYFHK ICWKKFKNLK
     YPGESDQSFS GQKCLKEGCP GDMVRMLQCD VPGIVKILFE VVRKDEYITI ENLGASYKNL
     MSLELTDTDI RPKFNLKPNT KDEVPIFKLD YNYFYHLLHI IIISGTDMVR QIFDEAMPPT
     LLKKELLIHK NVLEPYYNHL WTNHPLGGSW HLLYPPNKEL PQSKQFDLCL LLALIKHLNV
     FPAPRKGWDM EPPSSDLSKS ADILRLCKYR DILLSEILMN GLTELQFNSI WKKVSDILLR
     LGMKQDDLDK VKENPIENIS LDYHQLSIYL GIPVPEIIQR MLSCYQQGIT LQSITGSQRL
     DVEEFQNDEE DLSPPVMEYN IDVKSNTEIQ LAEINKDVAS IPSESSTESV KDLQEVKSKT
     KKKKRTKSNK KDKDSEDEQV SYMVEKDDQL ETEQVDVNTL STYMKTDTSD AQEDSAAEDK
     FCSLDELHIL DMVEQGSSGK ESTDFKETEK ERLAHQHQLY KLQYECEDYK RQLKTVTFRW
     QENQMLIKKK EKIIVSLNQQ VAFGINKMSK LQRQIHAKDD EIKNLKDQLS LKRSQWEMEK
     HNLESTVKTY LNKLNAETSR ALTAEVYFLQ CRRDFGLLHL EQTEKECLNQ LARVTHMAAS
     NLESLQLKAA VDSWNAIVAD VRNKIAFLRT QYNEQINKVK QGFALSTLPP VQLPPPPPSP
     EILIQQFLGR PLVKESFFRP ILTVPQMPAV CPGVISAAVQ PRPPLMPGIT WAMPTPIGDT
     VSPSASLCSE PLMINWERIT DRLKTAFPQQ TRKELTDFLQ QLKDSHGKSV SRLTFDEIVY
     KISQMIEPKK SESEEKSAQD GNNASPSHTA SQPNAPQDPK SAQGSATWEG DKDMDNEEEE
     EEPCVICHEN LSPENLSVLP CAHKFHSQCI RPWLMQQGTC PTCRLHVLQP EEFPGHPNGQ
     LPKI
//
ID   MBB1A_MOUSE             Reviewed;        1344 AA.
AC   Q7TPV4; O35851; Q80Y66; Q8R4X2; Q99KP0;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Myb-binding protein 1A;
DE   AltName: Full=Myb-binding protein of 160 kDa;
GN   Name=Mybbp1a; Synonyms=P160;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 43-53; 205-211;
RP   286-290; 458-465 AND 488-496, INTERACTION WITH JUN AND MYB,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=9447996;
RA   Tavner F.J., Simpson R., Tashiro S., Favier D., Jenkins N.A.,
RA   Gilbert D.J., Copeland N.G., Macmillan E.M., Lutwyche J., Keough R.A.,
RA   Ishii S., Gonda T.J.;
RT   "Molecular cloning reveals that the p160 Myb-binding protein is a
RT   novel, predominantly nucleolar protein which may play a role in
RT   transactivation by Myb.";
RL   Mol. Cell. Biol. 18:989-1002(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Keough R.A., Gonda T.J.;
RT   "Structural organization of the murine myb-binding protein p160
RT   (Mybbp1a) gene.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C3H/He; TISSUE=Eye, Mammary gland, and Osteoblast;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PARTIAL PROTEIN SEQUENCE, FUNCTION, AND INTERACTION WITH AHR.
RX   PubMed=11956195; DOI=10.1074/jbc.M200740200;
RA   Jones L.C., Okino S.T., Gonda T.J., Whitlock J.P. Jr.;
RT   "Myb-binding protein 1a augments AhR-dependent gene expression.";
RL   J. Biol. Chem. 277:22515-22519(2002).
RN   [6]
RP   SUBCELLULAR LOCATION, INTERACTION WITH KPNA2, MUTAGENESIS OF LEU-249;
RP   VAL-251; LEU-272 AND LEU-274, AND DOMAINS NES AND NLS.
RX   MEDLINE=22822554; PubMed=12941609; DOI=10.1016/S0014-4827(03)00262-3;
RA   Keough R.A., Macmillan E.M., Lutwyche J.K., Gardner J.M., Tavner F.J.,
RA   Jans D.A., Henderson B.R., Gonda T.J.;
RT   "Myb-binding protein 1a is a nucleocytoplasmic shuttling protein that
RT   utilizes CRM1-dependent and independent nuclear export pathways.";
RL   Exp. Cell Res. 289:108-123(2003).
RN   [7]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
RP   PPARGC1A.
RX   PubMed=14744933; DOI=10.1101/gad.1152204;
RA   Fan M., Rhee J., St Pierre J., Handschin C., Puigserver P., Lin J.,
RA   Jaeger S., Erdjument-Bromage H., Tempst P., Spiegelman B.M.;
RT   "Suppression of mitochondrial respiration through recruitment of p160
RT   myb binding protein to PGC-1alpha: modulation by p38 MAPK.";
RL   Genes Dev. 18:278-289(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1253, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-1164; SER-1198;
RP   SER-1253; THR-1277 AND SER-1280, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-722, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1253, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: May activate or repress transcription via interactions
CC       with sequence specific DNA-binding proteins. Repression may be
CC       mediated at least in part by histone deacetylase activity (HDAC
CC       activity).
CC   -!- SUBUNIT: Component of the B-WICH complex, at least composed of
CC       SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and
CC       DDX21 (By similarity). Binds to and represses JUN and MYB via the
CC       leucine zipper regions present in these proteins. Also binds to
CC       and represses PPARGC1A: this interaction is abrogated when
CC       PPARGC1A is phosphorylated by MAPK1/ERK. Binds to and stimulates
CC       transcription by AHR. Binds to KPNA2.
CC   -!- INTERACTION:
CC       O43918:AIRE (xeno); NbExp=1; IntAct=EBI-1373622, EBI-1753081;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm.
CC       Note=Predominantly nucleolar. Also shuttles between the nucleus
CC       and cytoplasm. Nuclear import may be mediated by KPNA2, while
CC       export appears to depend partially on XPO1/CRM1.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
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DR   EMBL; U63648; AAC39954.1; -; mRNA.
DR   EMBL; AF345640; AAL83748.1; -; Genomic_DNA.
DR   EMBL; AL662812; CAI52004.1; -; Genomic_DNA.
DR   EMBL; BC004078; AAH04078.1; -; mRNA.
DR   EMBL; BC048858; AAH48858.1; -; mRNA.
DR   EMBL; BC052889; AAH52889.1; -; mRNA.
DR   IPI; IPI00331361; -.
DR   PIR; T34188; T34188.
DR   RefSeq; NP_058056.2; NM_016776.2.
DR   UniGene; Mm.147946; -.
DR   ProteinModelPortal; Q7TPV4; -.
DR   IntAct; Q7TPV4; 9.
DR   STRING; Q7TPV4; -.
DR   PhosphoSite; Q7TPV4; -.
DR   PRIDE; Q7TPV4; -.
DR   Ensembl; ENSMUST00000045633; ENSMUSP00000044827; ENSMUSG00000040463.
DR   GeneID; 18432; -.
DR   KEGG; mmu:18432; -.
DR   UCSC; uc007jyy.1; mouse.
DR   CTD; 18432; -.
DR   MGI; MGI:106181; Mybbp1a.
DR   GeneTree; ENSGT00390000017457; -.
DR   HOGENOM; HBG715810; -.
DR   HOVERGEN; HBG081961; -.
DR   InParanoid; Q7TPV4; -.
DR   OMA; HKTARIF; -.
DR   OrthoDB; EOG4RFKRW; -.
DR   PhylomeDB; Q7TPV4; -.
DR   NextBio; 294102; -.
DR   PMAP-CutDB; Q7TPV4; -.
DR   ArrayExpress; Q7TPV4; -.
DR   Bgee; Q7TPV4; -.
DR   CleanEx; MM_MYBBP1A; -.
DR   Genevestigator; Q7TPV4; -.
DR   GermOnline; ENSMUSG00000040463; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0042564; C:NLS-dependent protein nuclear import complex; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro.
DR   GO; GO:0008134; F:transcription factor binding; TAS:UniProtKB.
DR   GO; GO:0016564; F:transcription repressor activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; TAS:UniProtKB.
DR   GO; GO:0006913; P:nucleocytoplasmic transport; IDA:UniProtKB.
DR   GO; GO:0022904; P:respiratory electron transport chain; IDA:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR007015; DNA_pol_V.
DR   PANTHER; PTHR13213; DNA_pol_V; 1.
DR   Pfam; PF04931; DNA_pol_phi; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Cytoplasm; Direct protein sequencing; Nucleus;
KW   Phosphoprotein; Repressor; Transcription; Transcription regulation.
FT   CHAIN         1   1344       Myb-binding protein 1A.
FT                                /FTId=PRO_0000096256.
FT   REGION        1    580       Interaction with MYB.
FT   REGION     1152   1344       Required for nuclear and nucleolar
FT                                localization.
FT   MOTIF       238    256       Nuclear export signal 1.
FT   MOTIF       261    279       Nuclear export signal 2.
FT   COMPBIAS    698    752       Asp-rich.
FT   MOD_RES       6      6       Phosphoserine.
FT   MOD_RES      58     58       Phosphotyrosine (By similarity).
FT   MOD_RES      69     69       N6-acetyllysine (By similarity).
FT   MOD_RES     156    156       N6-acetyllysine (By similarity).
FT   MOD_RES     722    722       Phosphoserine.
FT   MOD_RES    1160   1160       Phosphoserine (By similarity).
FT   MOD_RES    1162   1162       Phosphothreonine (By similarity).
FT   MOD_RES    1164   1164       Phosphoserine.
FT   MOD_RES    1167   1167       Phosphoserine (By similarity).
FT   MOD_RES    1187   1187       Phosphoserine (By similarity).
FT   MOD_RES    1191   1191       Phosphothreonine (By similarity).
FT   MOD_RES    1198   1198       Phosphoserine.
FT   MOD_RES    1219   1219       Phosphoserine (By similarity).
FT   MOD_RES    1244   1244       Phosphoserine (By similarity).
FT   MOD_RES    1253   1253       Phosphoserine.
FT   MOD_RES    1256   1256       Phosphothreonine (By similarity).
FT   MOD_RES    1277   1277       Phosphothreonine.
FT   MOD_RES    1280   1280       Phosphoserine.
FT   MOD_RES    1303   1303       Phosphoserine (By similarity).
FT   MOD_RES    1308   1308       Phosphoserine (By similarity).
FT   MOD_RES    1318   1318       Phosphoserine (By similarity).
FT   MOD_RES    1323   1323       Phosphoserine (By similarity).
FT   MOD_RES    1325   1325       Phosphoserine (By similarity).
FT   MOD_RES    1329   1329       Phosphoserine (By similarity).
FT   MUTAGEN     249    249       L->A: Reduced nuclear export; when
FT                                associated with A-251.
FT   MUTAGEN     251    251       V->A: Reduced nuclear export; when
FT                                associated with A-249.
FT   MUTAGEN     272    272       L->A: Reduced nuclear export; when
FT                                associated with A-274.
FT   MUTAGEN     274    274       L->A: Reduced nuclear export; when
FT                                associated with A-272.
FT   CONFLICT     87     87       R -> T (in Ref. 1; AAC39954 and 2;
FT                                AAL83748).
FT   CONFLICT     88     88       P -> A (in Ref. 1; AAC39954).
FT   CONFLICT    505    508       DRNR -> HASG (in Ref. 4; AAH04078).
FT   CONFLICT   1282   1282       I -> V (in Ref. 4; AAH52889).
SQ   SEQUENCE   1344 AA;  152037 MW;  64D3420981CD0767 CRC64;
     MAEMKSPTKA EPATPAEAAQ SDRHSLLEHS REFLDFFWDI AKPDQETRLR ATEKLLEYLR
     TRPNDSEMKY ALKRLITGLG VGREAARPCY SLALAQLLQS FEDIPLCDIL DQIQEKYSLQ
     AMNKAMMRPS LFANLFGVLA LFQSGRLVKD KEALMKSVQL LKILSQHPNH LQGQPIKALV
     DILSEVPESM FQEILPKVLK GNMKVILRSP KYLELFLLAK QRVPTKLESL MGSVDLFSED
     NIPSLVNILK VAANSVKKEH KLPNVALDLL RLALKESRFE LFWKKVLEEG LLKNPSWTSS
     YMCFRLLGAS LPLLSEEQLQ LVMRGDLIRH FGENMVISKP QNLFKIIPEI STYVGTFLEG
     CQDDPKRQLT MMVAFTTITN QGLPVMPTFW RVTRFLNAEA LQSYVAWLRD MFLQPDLNSL
     VDFSTANQKR AQDASLNVPE RAVFRLRKWI IHRLVSLVDH LHLEKDEAVV EQIARFCLFH
     AFFKTKKATP QIPETKQHFS FPLDDRNRGV FVSAFFSLLQ TLSVKFRQTP DLAENGKPWT
     YRLVQLADML LNHNRNVTSV TSLTTQQRQA WDQMMSTLKE LEARSSETRA IAFQHLLLLV
     GLHIFKSPAE SCDVLGDIQT CIKKSMEQNP RRSRSRAKAS QEPVWVEVMV EILLSLLAQP
     SNLMRQVVRS VFGHICPHLT PRCLQLILAV LSPVTNEDED DNVVVTDDAD EKQLQHGEDE
     DSDNEDNKNS ESDMDSEDGE ESEEEDRDKD VDPGFRQQLM EVLKAGNALG GVDNEEEEEL
     GDEAMMALDQ NLASLFKEQK MRIQARNEEK NKLQKEKKLR RDFQIRALDL IEVLVTKQPE
     HPLILELLEP LLNVIQHSMR SKGSTKQEQD LLHKTARIFM HHLCRARRYC HEVGPCAEAL
     HAQVERLVQQ AGSQADASVA LYYFNASLYL LRVLKGNTNK RHQDGHKLHG ADTEDSEDQA
     ANCLDLDFVT RVYSASLESL LTKRNSSLTV PMFLSLFSRY PVICKNLLPV LAQHVAGPSR
     PRHQAQACLM LQKTLSAREL RVCFEDPEWE QLITQLLGKA TQTLQTLGEA QSKGEHQKEL
     SILELLNTLL RTVNHEKLSV DLTAPLGVLQ SKQQKLQQSL QQGNHSSGSN RLYDLYWQAM
     RMLGVQRPKS EKKNAKDIPS DTQSPVSTKR KKKGFLPETK KRKKLKSEGT TPEKNAASQQ
     DAVTEGAMPA ATGKDQPPST GKKKRKRVKA STPSQVNGIT GAKSPAPSNP TLSPSTPAKT
     PKLQKKKEKL SQVNGATPVS PIEPESKKHH QEALSTKEVI RKSPHPQSAL PKKRARLSLV
     SRSPSLLQSG VKKRRVASRR VQTP
//
ID   Q7TPW0_MOUSE            Unreviewed;       375 AA.
AC   Q7TPW0;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   11-JAN-2011, entry version 37.
DE   SubName: Full=Arht1 protein;
DE   Flags: Fragment;
GN   Name=Rhot1; Synonyms=Arht1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC052882; AAH52882.1; -; mRNA.
DR   IPI; IPI00222930; -.
DR   UniGene; Mm.480354; -.
DR   ProteinModelPortal; Q7TPW0; -.
DR   STRING; Q7TPW0; -.
DR   Ensembl; ENSMUST00000017831; ENSMUSP00000017831; ENSMUSG00000017686.
DR   MGI; MGI:1926078; Rhot1.
DR   HOVERGEN; HBG079778; -.
DR   ArrayExpress; Q7TPW0; -.
DR   Bgee; Q7TPW0; -.
DR   Genevestigator; Q7TPW0; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR013566; EF_hand_assoc_1.
DR   InterPro; IPR020860; MIRO.
DR   InterPro; IPR013684; MIRO-like.
DR   Pfam; PF08355; EF_assoc_1; 1.
DR   Pfam; PF08477; Miro; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS51423; MIRO; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   375 AA;  43215 MW;  8EAAC63FFF7A94F5 CRC64;
     RGNPLDLTPE YLFPLLKIPP DCTTELNHHA YLFLQSTFDK HDLDRDCALS PDELKDLFQV
     FPYIPWGPDV NNTVCTNERG WITYQGFLSQ WTLTTYLDVQ RCLEYLGYLG YSILTEQESQ
     ASAITVTRDK KIDLQKKQTQ RNVFRCNVIG VKGCGKTGVL QSLLGRNLMR QKKIRDDHKS
     YYAINTVYVY GQEKYLLLHD ISESEFLTEA ETICDVVCLV YDVTNPKSFE YCARIFKQHF
     MDSRIPCLIV AAKSDLHEVK QEHSISPTDF CRKHKMPPPQ AFTCNTADAP SKDIFVKLTT
     MAMYPEDHYR GSLSRDMGST DRIENLRKIW VFLKTALHVT QADLKSSTFW LRASFGATVF
     AVVGFAMYRA LLKQR
//
ID   NEXN_MOUSE              Reviewed;         607 AA.
AC   Q7TPW1; Q3TQP3; Q3UWU2; Q3UWU6; Q3UX39;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Nexilin;
DE   AltName: Full=F-actin-binding protein;
GN   Name=Nexn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-314 AND 386-607.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: Involved in regulating cell migration through
CC       association with the actin cytoskeleton (By similarity). Has an
CC       essential role in the maintenance of Z-disk and sarcomere
CC       integrity (By similarity).
CC   -!- SUBUNIT: Interacts with F-actin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Cell junction, adherens junction (By similarity). Cytoplasm,
CC       myofibril, sarcomere, Z-disk (By similarity). Note=Localizes to
CC       the cell-matrix AJ. Not found at the cell-cell AJ (By similarity).
CC   -!- SIMILARITY: Contains 1 Ig-like (immunoglobulin-like) domain.
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DR   EMBL; BC052878; AAH52878.1; -; mRNA.
DR   EMBL; AK135919; BAE22724.1; -; mRNA.
DR   EMBL; AK136097; BAE22818.1; -; mRNA.
DR   EMBL; AK136102; BAE22822.1; -; mRNA.
DR   EMBL; AK163414; BAE37339.1; -; mRNA.
DR   IPI; IPI00400168; -.
DR   RefSeq; NP_955759.2; NM_199465.2.
DR   UniGene; Mm.200188; -.
DR   HSSP; P56276; 1FHG.
DR   ProteinModelPortal; Q7TPW1; -.
DR   SMR; Q7TPW1; 510-605.
DR   STRING; Q7TPW1; -.
DR   PhosphoSite; Q7TPW1; -.
DR   PRIDE; Q7TPW1; -.
DR   Ensembl; ENSMUST00000046045; ENSMUSP00000037120; ENSMUSG00000039103.
DR   GeneID; 68810; -.
DR   KEGG; mmu:68810; -.
DR   UCSC; uc008rtb.1; mouse.
DR   CTD; 68810; -.
DR   MGI; MGI:1916060; Nexn.
DR   eggNOG; roNOG09553; -.
DR   GeneTree; ENSGT00600000084370; -.
DR   HOGENOM; HBG403129; -.
DR   HOVERGEN; HBG066529; -.
DR   InParanoid; Q7TPW1; -.
DR   OrthoDB; EOG4GF3F5; -.
DR   NextBio; 327979; -.
DR   ArrayExpress; Q7TPW1; -.
DR   Bgee; Q7TPW1; -.
DR   CleanEx; MM_NEXN; -.
DR   Genevestigator; Q7TPW1; -.
DR   GO; GO:0005924; C:cell-substrate adherens junction; ISS:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0030018; C:Z disc; ISS:UniProtKB.
DR   GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR   GO; GO:0008307; F:structural constituent of muscle; ISS:UniProtKB.
DR   GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR   GO; GO:0051493; P:regulation of cytoskeleton organization; ISS:UniProtKB.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR020675; Myosin_light_chain_kin-rel.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   PANTHER; PTHR22964; Myosin_light_chain_kin-rel; 1.
DR   Pfam; PF07679; I-set; 1.
DR   SMART; SM00409; IG; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Cell junction; Cytoplasm; Cytoskeleton;
KW   Immunoglobulin domain; Phosphoprotein.
FT   CHAIN         1    607       Nexilin.
FT                                /FTId=PRO_0000302086.
FT   DOMAIN      513    601       Ig-like.
FT   COMPBIAS      9    506       Glu-rich.
FT   MOD_RES      16     16       Phosphoserine.
FT   MOD_RES     288    288       Phosphoserine (By similarity).
FT   MOD_RES     296    296       Phosphoserine (By similarity).
FT   MOD_RES     301    301       Phosphothreonine (By similarity).
FT   MOD_RES     500    500       Phosphoserine (By similarity).
FT   CONFLICT    123    123       D -> N (in Ref. 1; AAH52878).
FT   CONFLICT    268    268       L -> I (in Ref. 2; BAE22822).
FT   CONFLICT    454    454       T -> A (in Ref. 2; BAE22724).
SQ   SEQUENCE   607 AA;  72138 MW;  1C33C922D73EE932 CRC64;
     MNDVSQKAEI KEMLASDDEE ESSPKIEKAY VPKLTGTVKG KFDEMEKHRQ EEQRKRTEEE
     RKRRIEQDLL EKRKIQRELA KRAEQIEDIN NTGTESASEE GDDSLLITVV PAKSYKTPGK
     TKDPEDLDRE EGNGRTNHEE DKMRYEEECR VLKEAKCLSL VMDDETEAKK ESHFPGKLKS
     TFEELERQRQ ENRKKQAEEE ARRRLEEERR SFEEARRHMV NEEDENQDRE TVFKEYRPGK
     LKLSFEEIER QRREDEKRKA EEEARRRLEE EKAAFAEARR SMVLDDDSPE IYKTVSQESL
     TPGKLEINFE QLLRQKMEEE RRRTEEERRH KLEMEKQEFE QLRQEMGKEE EENESFGLSR
     EYEELIKLKR SGSIQAKNLK SKFEKIGQLS EKEVQKKIEE ERAKRRAIDL EIKEREAENF
     HEDDDVDVRP AKKSESPFTH KVNMKARFEQ MAKTREEEEQ RRIEEQKLLR MQFEQKEIDA
     ALQKKREDEE EEEGSIVNGS TTEDEEQTRS GAPWFKKPLR NTSVVDSEPV RFTVKVTGEP
     KPEITWWFEG EILQDGEDYQ YIERGETYCL YLPETFPEDG GEYMCKAVNN KGSAASTCIL
     TIEMDDY
//
ID   LNP_MOUSE               Reviewed;         425 AA.
AC   Q7TQ95; A2ASL9; Q69ZC5; Q6PAQ1; Q6PEN8;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Protein lunapark;
DE   AltName: Full=Protein ulnaless;
GN   Name=Lnp; Synonyms=Kiaa1715, Uln;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=22617799; PubMed=12732147; DOI=10.1016/S0092-8674(03)00310-6;
RA   Spitz F., Gonzalez F., Duboule D.;
RT   "A global control region defines a chromosomal regulatory landscape
RT   containing the HoxD cluster.";
RL   Cell 113:405-417(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cecum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May be involved in limb and central nervous system
CC       development.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- TISSUE SPECIFICITY: Expressed in most tissues at basal level, with
CC       reinforcement in distal limb buds, genital bud, and in parts of
CC       the central nervous system.
CC   -!- DEVELOPMENTAL STAGE: Strongly expressed in both limb and genital
CC       buds as is the case for Evx2 and Hoxd genes, in particular Hoxd13.
CC       In developing limb buds, it is first seen in 10.5 days old
CC       fetuses, in the posterior distal bud, to subsequently extend
CC       throughout the distal aspect, in presumptive digits.
CC   -!- MISCELLANEOUS: Was named 'Lunapark' because the protein sequence
CC       contains the word 'LNPARK'.
CC   -!- SIMILARITY: Belongs to the lunapark family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32519.1; Type=Erroneous initiation;
CC       Sequence=BC060153; Type=Frameshift; Positions=34;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY312281; AAP76388.1; -; mRNA.
DR   EMBL; AK173241; BAD32519.1; ALT_INIT; mRNA.
DR   EMBL; AK136506; BAE23015.1; -; mRNA.
DR   EMBL; AL928644; CAM20518.1; -; Genomic_DNA.
DR   EMBL; BC057961; AAH57961.2; -; mRNA.
DR   EMBL; BC060153; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00469947; -.
DR   RefSeq; NP_001103679.1; NM_001110209.1.
DR   RefSeq; NP_081409.1; NM_027133.3.
DR   UniGene; Mm.156113; -.
DR   ProteinModelPortal; Q7TQ95; -.
DR   STRING; Q7TQ95; -.
DR   PhosphoSite; Q7TQ95; -.
DR   PRIDE; Q7TQ95; -.
DR   Ensembl; ENSMUST00000064503; ENSMUSP00000066891; ENSMUSG00000009207.
DR   GeneID; 69605; -.
DR   KEGG; mmu:69605; -.
DR   UCSC; uc008kdq.1; mouse.
DR   CTD; 69605; -.
DR   MGI; MGI:1918115; Lnp.
DR   GeneTree; ENSGT00390000001859; -.
DR   HOGENOM; HBG445576; -.
DR   HOVERGEN; HBG079498; -.
DR   InParanoid; Q7TQ95; -.
DR   OMA; AKECEPP; -.
DR   OrthoDB; EOG4ZS943; -.
DR   PhylomeDB; Q7TQ95; -.
DR   NextBio; 329896; -.
DR   ArrayExpress; Q7TQ95; -.
DR   Bgee; Q7TQ95; -.
DR   CleanEx; MM_LNP; -.
DR   Genevestigator; Q7TQ95; -.
DR   GermOnline; ENSMUSG00000009207; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007596; P:blood coagulation; IMP:MGI.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; IGI:MGI.
DR   GO; GO:0035115; P:embryonic forelimb morphogenesis; IMP:MGI.
DR   InterPro; IPR019273; DUF2296.
DR   Pfam; PF10058; DUF2296; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Developmental protein; Membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    425       Protein lunapark.
FT                                /FTId=PRO_0000248311.
FT   TOPO_DOM      1     45       Cytoplasmic (Potential).
FT   TRANSMEM     46     66       Helical; (Potential).
FT   TOPO_DOM     67     77       Extracellular (Potential).
FT   TRANSMEM     78     98       Helical; (Potential).
FT   TOPO_DOM     99    425       Cytoplasmic (Potential).
FT   COILED       15     41       Potential.
FT   COILED      101    128       Potential.
FT   COMPBIAS    178    245       Pro-rich.
FT   MOD_RES     177    177       Phosphoserine (By similarity).
FT   MOD_RES     182    182       Phosphoserine (By similarity).
FT   MOD_RES     194    194       Phosphoserine (By similarity).
FT   MOD_RES     222    222       Phosphoserine (By similarity).
FT   MOD_RES     316    316       Phosphoserine (By similarity).
FT   MOD_RES     411    411       Phosphoserine.
FT   MOD_RES     418    418       Phosphoserine (By similarity).
FT   MOD_RES     421    421       Phosphoserine (By similarity).
SQ   SEQUENCE   425 AA;  47500 MW;  829A31984BB48DD6 CRC64;
     MGGLFSRWRA KPSTVEVLEN IDKEIQALEE FREKNQRLQK LWVGRLIIYS SILYLFTCLI
     VYLWYLPDEF TARLVMTLPF FAFPLIIWTL RTVLIFFFSK RTERNNEALD DLKSQKKKIL
     EEVMEKETYK TAKLILERFD PDSKKAKEFE PPSAGAAVTA KPGQEIRQRT AAQRNLSPAP
     ASSSQGPPPQ GPVSPGPAKD ASAPGGPPER TVAPALPRRL GSPATSVPGM GLHPPGPPLA
     RPILPRERGA LDRIVEYLVG DGPQNRYALI CQQCFSHNGM ALKEEFEYIA FRCAYCFFLN
     PARKTRPQAP RLPEFSFEKR QAVEGSSSTG PTLLESVPSA ESQLIEDSLE EQDVLDNSTE
     QRDDKIPVTE QTSQVIEKTS GPEEPAENQE ETENEETSTN EAKSPVLRAD SVPNLEPSEE
     SLVTK
//
ID   GPTC2_MOUSE             Reviewed;         527 AA.
AC   Q7TQC7; Q8BNJ9; Q8BPM1; Q8CDH9;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 2.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=G patch domain-containing protein 2;
GN   Name=Gpatch2; Synonyms=Gpatc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Eye, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q7TQC7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TQC7-2; Sequence=VSP_010529;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q7TQC7-3; Sequence=VSP_010530;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 G-patch domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK030026; BAC26744.1; -; mRNA.
DR   EMBL; AK053781; BAC35520.1; -; mRNA.
DR   EMBL; AK083471; BAC38928.1; -; mRNA.
DR   EMBL; BC054810; AAH54810.1; -; mRNA.
DR   IPI; IPI00416341; -.
DR   IPI; IPI00416342; -.
DR   IPI; IPI00416343; -.
DR   RefSeq; NP_080643.4; NM_026367.4.
DR   UniGene; Mm.138321; -.
DR   ProteinModelPortal; Q7TQC7; -.
DR   PhosphoSite; Q7TQC7; -.
DR   PRIDE; Q7TQC7; -.
DR   Ensembl; ENSMUST00000065573; ENSMUSP00000065009; ENSMUSG00000039210.
DR   Ensembl; ENSMUST00000110943; ENSMUSP00000106568; ENSMUSG00000039210.
DR   GeneID; 67769; -.
DR   KEGG; mmu:67769; -.
DR   UCSC; uc007dzy.1; mouse.
DR   CTD; 67769; -.
DR   MGI; MGI:1915019; Gpatch2.
DR   HOGENOM; HBG713835; -.
DR   HOVERGEN; HBG062801; -.
DR   InParanoid; Q7TQC7; -.
DR   OMA; VPWWEKE; -.
DR   PhylomeDB; Q7TQC7; -.
DR   NextBio; 325513; -.
DR   ArrayExpress; Q7TQC7; -.
DR   Bgee; Q7TQC7; -.
DR   CleanEx; MM_GPATCH2; -.
DR   Genevestigator; Q7TQC7; -.
DR   GermOnline; ENSMUSG00000039210; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   InterPro; IPR000467; G_patch.
DR   Pfam; PF01585; G-patch; 1.
DR   SMART; SM00443; G_patch; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    527       G patch domain-containing protein 2.
FT                                /FTId=PRO_0000087567.
FT   DOMAIN      466    512       G-patch.
FT   MOD_RES      49     49       Phosphothreonine (By similarity).
FT   MOD_RES     114    114       Phosphoserine (By similarity).
FT   MOD_RES     116    116       Phosphoserine (By similarity).
FT   VAR_SEQ       1     23       Missing (in isoform 2).
FT                                /FTId=VSP_010529.
FT   VAR_SEQ     388    425       DHWFSPGARTEHGQHQLLRDNRAERGHKKSCSLKTASR ->
FT                                E (in isoform 3).
FT                                /FTId=VSP_010530.
FT   CONFLICT    251    251       D -> Y (in Ref. 1; BAC26744).
FT   CONFLICT    367    367       S -> P (in Ref. 2; AAH54810).
SQ   SEQUENCE   527 AA;  58218 MW;  4F4F29FA56BE06B7 CRC64;
     MFGADGRPAI GTAAGKSWHF SRTMEELVHD LVSALEESSE QARGGFAETG EHSRNLSCPL
     KRQARKRRGR KRRSYNVHHP WETGHCLSEG SDSSLEEPSK DYREKHSNNK KDRSDSDDQM
     LVAKRRPSSN LSSSVRGKRL LWHESDFAVD SLGNRTLRRR RKVKRMAVDL PQDVSSKRTM
     TQLPEGCRDQ DMDNDRASQY PEFTRKKVKK RKLKGIRPGP KTQEEGGVLE SEERSQPNKD
     RMEYEEQKAS DELRSESDTS SLSSTDAGLF TNDEGRQGDD EQSDWFYEKE SGGACGIAGV
     VPWWEKDEPA ELDTNLPDPV FESILSGSFP LMSHPGRGGF QARLSRLHGT PSKNIKKSSG
     APPSMLSAPG PGSNKRMVHF SPDAHRHDHW FSPGARTEHG QHQLLRDNRA ERGHKKSCSL
     KTASRQTSMH LGSLCTGDIK RRRKAAPLPG PTAAGIVGEN AQPILESNIG NRMLQSMGWT
     PGSGLGRDGR GIAEPVQAVQ RPKGLGLGFP LPKSSPTSPA PTSGNPA
//
ID   TPPP_MOUSE              Reviewed;         218 AA.
AC   Q7TQD2;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Tubulin polymerization-promoting protein;
DE            Short=TPPP;
GN   Name=Tppp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 11-25; 30-55; 89-101; 109-124; 156-164 AND
RP   192-205, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15 AND SER-31, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452088; DOI=10.1074/mcp.T500040-MCP200;
RA   Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G.,
RA   Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F.,
RA   Maltby D.A., Schoepfer R., Burlingame A.L.;
RT   "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT   preparations using lectin weak affinity chromatography and mass
RT   spectrometry.";
RL   Mol. Cell. Proteomics 5:923-934(2006).
RN   [5]
RP   FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=18028908; DOI=10.1016/j.yexcr.2007.08.012;
RA   Acevedo K., Li R., Soo P., Suryadinata R., Sarcevic B., Valova V.A.,
RA   Graham M.E., Robinson P.J., Bernard O.;
RT   "The phosphorylation of p25/TPPP by LIM kinase 1 inhibits its ability
RT   to assemble microtubules.";
RL   Exp. Cell Res. 313:4091-4106(2007).
CC   -!- FUNCTION: May play a role in the polymerization of tubulin into
CC       microtubules, microtubule bundling and the stabilization of
CC       existing microtubules, thus maintaining the integrity of the
CC       microtubule network. May play a role in mitotic spindle assembly
CC       and nuclear envelope breakdown.
CC   -!- SUBUNIT: Homodimer (By similarity). Binds tubulin; binding is
CC       inhibited by GTP (By similarity). Interacts with GSK3 (By
CC       similarity). Interacts with MAPK1 (By similarity). Interacts with
CC       LIMK1 (via the PDZ domain); the interaction is direct (By
CC       similarity). Interacts with GAPDH; the interaction is direct (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Nucleus.
CC   -!- TISSUE SPECIFICITY: Widely expressed with higher expression in
CC       brain (at protein level).
CC   -!- PTM: Poor substrate for GSK3 (By similarity). Phosphorylated by
CC       LIMK1 on serine residues (By similarity). Phosphorylation may
CC       alter the tubulin polymerization activity (By similarity).
CC   -!- SIMILARITY: Belongs to the TPPP family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC054803; AAH54803.1; -; mRNA.
DR   IPI; IPI00119067; -.
DR   RefSeq; NP_878259.1; NM_182839.2.
DR   UniGene; Mm.39752; -.
DR   ProteinModelPortal; Q7TQD2; -.
DR   SMR; Q7TQD2; 43-215.
DR   STRING; Q7TQD2; -.
DR   PhosphoSite; Q7TQD2; -.
DR   PRIDE; Q7TQD2; -.
DR   Ensembl; ENSMUST00000022057; ENSMUSP00000022057; ENSMUSG00000021573.
DR   GeneID; 72948; -.
DR   KEGG; mmu:72948; -.
DR   UCSC; uc007reo.1; mouse.
DR   CTD; 72948; -.
DR   MGI; MGI:1920198; Tppp.
DR   GeneTree; ENSGT00390000014993; -.
DR   HOGENOM; HBG520967; -.
DR   HOVERGEN; HBG036683; -.
DR   InParanoid; Q7TQD2; -.
DR   OMA; KGKSCRT; -.
DR   OrthoDB; EOG4HQDKK; -.
DR   PhylomeDB; Q7TQD2; -.
DR   NextBio; 337199; -.
DR   ArrayExpress; Q7TQD2; -.
DR   Bgee; Q7TQD2; -.
DR   CleanEx; MM_TPPP; -.
DR   Genevestigator; Q7TQD2; -.
DR   GermOnline; ENSMUSG00000021573; Mus musculus.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC.
DR   GO; GO:0005625; C:soluble fraction; ISS:HGNC.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008017; F:microtubule binding; ISS:HGNC.
DR   GO; GO:0001578; P:microtubule bundle formation; ISS:HGNC.
DR   GO; GO:0046785; P:microtubule polymerization; IDA:UniProtKB.
DR   GO; GO:0032273; P:positive regulation of protein polymerization; ISS:HGNC.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR008907; P25-alpha.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   PANTHER; PTHR12932; P25-alpha; 1.
DR   Pfam; PF05517; p25-alpha; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; Glycoprotein;
KW   Microtubule; Nucleus; Phosphoprotein.
FT   CHAIN         1    218       Tubulin polymerization-promoting protein.
FT                                /FTId=PRO_0000221136.
FT   REGION        1    115       Mediates interaction with LIMK1 (By
FT                                similarity).
FT   MOD_RES      15     15       Phosphothreonine.
FT   MOD_RES      19     19       Phosphoserine (By similarity).
FT   MOD_RES      31     31       Phosphoserine.
FT   MOD_RES      34     34       Phosphoserine (By similarity).
FT   MOD_RES     159    159       Phosphoserine (By similarity).
FT   CARBOHYD    151    151       O-linked (GlcNAc).
SQ   SEQUENCE   218 AA;  23575 MW;  EF929B3E0D01CE19 CRC64;
     MADSKAKPAK AANKTPPKSP GDPARAAKRL SLESEGANEG ATAAPELSAL EEAFRRFAVH
     GDTRATGKEM HGKNWSKLCK DCHVIDGKNV TVTDVDIVFS KIKGKSCRTI TFEQFQEALE
     ELAKKRFKDK SSEEAVREVH RLIEGRAPVI SGVTKAVSSP TVSRLTDTSK FTGSHKERFD
     QSGKGKGKAG RVDLVDESGY VPGYKHAGTY DQKVQGGK
//
ID   FBX10_MOUSE             Reviewed;         950 AA.
AC   Q7TQF2; A2ANI6; Q6AXG0; Q7TQM0;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=F-box only protein 10;
GN   Name=Fbxo10; Synonyms=Gm634;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 829-835, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-
CC       box protein)-type E3 ubiquitin ligase complex (By similarity).
CC   -!- SUBUNIT: Directly interacts with SKP1A and CUL1 (By similarity).
CC   -!- SIMILARITY: Contains 1 F-box domain.
CC   -!- SIMILARITY: Contains 17 PbH1 repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH54731.1; Type=Erroneous initiation;
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DR   EMBL; AL824706; CAM17797.1; -; Genomic_DNA.
DR   EMBL; BC052485; AAH52485.1; -; mRNA.
DR   EMBL; BC054731; AAH54731.1; ALT_INIT; mRNA.
DR   EMBL; BC079571; AAH79571.1; -; mRNA.
DR   IPI; IPI00938451; -.
DR   RefSeq; NP_001019313.1; NM_001024142.1.
DR   UniGene; Mm.389552; -.
DR   ProteinModelPortal; Q7TQF2; -.
DR   SMR; Q7TQF2; 2-159, 718-847.
DR   PRIDE; Q7TQF2; -.
DR   Ensembl; ENSMUST00000052236; ENSMUSP00000058233; ENSMUSG00000048232.
DR   GeneID; 269529; -.
DR   KEGG; mmu:269529; -.
DR   NMPDR; fig|10090.3.peg.9515; -.
DR   UCSC; uc008ssf.1; mouse.
DR   CTD; 269529; -.
DR   MGI; MGI:2686937; Fbxo10.
DR   GeneTree; ENSGT00530000063425; -.
DR   HOGENOM; HBG714326; -.
DR   HOVERGEN; HBG080399; -.
DR   InParanoid; Q7TQF2; -.
DR   OMA; LPRSDTK; -.
DR   OrthoDB; EOG4MPHPD; -.
DR   ArrayExpress; Q7TQF2; -.
DR   Bgee; Q7TQF2; -.
DR   CleanEx; MM_FBXO10; -.
DR   Genevestigator; Q7TQF2; -.
DR   InterPro; IPR006633; Carb-bd_sugar_hydrolysis-dom.
DR   InterPro; IPR001810; F-box_dom_cyclin-like.
DR   InterPro; IPR022364; F-box_dom_Skp2-like.
DR   InterPro; IPR022441; Para_beta_helix_rpt-2.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   Gene3D; G3DSA:2.160.20.10; Pectin_lyas_fold; 3.
DR   Pfam; PF00646; F-box; 1.
DR   SMART; SM00722; CASH; 3.
DR   SMART; SM00256; FBOX; 1.
DR   SMART; SM00710; PbH1; 17.
DR   SUPFAM; SSF81383; F-box_dom_Skp2-like; 1.
DR   SUPFAM; SSF51126; Pectin_lyas_like; 3.
DR   TIGRFAMs; TIGR03804; Para_beta_helix; 3.
DR   PROSITE; PS50181; FBOX; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Repeat; Ubl conjugation pathway.
FT   CHAIN         1    950       F-box only protein 10.
FT                                /FTId=PRO_0000307718.
FT   DOMAIN        1     48       F-box.
FT   REPEAT      198    217       PbH1 1.
FT   REPEAT      238    260       PbH1 2.
FT   REPEAT      423    444       PbH1 3.
FT   REPEAT      467    489       PbH1 4.
FT   REPEAT      490    512       PbH1 5.
FT   REPEAT      513    535       PbH1 6.
FT   REPEAT      536    558       PbH1 7.
FT   REPEAT      559    581       PbH1 8.
FT   REPEAT      582    604       PbH1 9.
FT   REPEAT      605    627       PbH1 10.
FT   REPEAT      628    650       PbH1 11.
FT   REPEAT      651    673       PbH1 12.
FT   REPEAT      713    735       PbH1 13.
FT   REPEAT      736    758       PbH1 14.
FT   REPEAT      760    782       PbH1 15.
FT   REPEAT      783    805       PbH1 16.
FT   REPEAT      828    850       PbH1 17.
FT   CONFLICT    192    192       I -> T (in Ref. 2; AAH54731).
SQ   SEQUENCE   950 AA;  104478 MW;  D526F93603113458 CRC64;
     METGGLPLEL WRMILAYLHL PDLGRCSLVC RAWYELILSL DSTRWRQLCL GCTECRHPNW
     PNQPDVEPES WREAFKQHYL ASKTWTKNAL DLESSICFSL FRRKKERRTL SVGPGHEFDS
     LGSALAMASL YDRIVLFPGV YEEQGEIILK VPVEIVGQGK LGEVALLASI DQHCSTTRVC
     NLVFMPAWFS PIMYKTTSGH IQFDNCNFEN GHIQVHGPGT CQVKFCTFKN THVFLHNVPL
     CMLENCEFVG SENNCVTVEG HPSADKNWAY KYLLGLIKSS PIFLPAEDHD FLMSLDLESR
     DQAWSPRTCD IVIEGSQSPT SPVCSSPKPG SKEAEVGSDG ERVAQTPDSS DGGLSPSGED
     EDDEQLTYRL SYQVQGPRPV LGGSFLGPPL PGASIQLPSC LVLNSLHQEL QKDKEAMALA
     SSVQGCLIRK CLFRDGKGGV FVCSYGRAKM EGNVFRNLTY AVRCIHNSKI VMLRNDIYRC
     RASGIFLRLE GGGLIAGNNI YHNAEAGVDI RKKSNPLILC NQIHHGLRSG IVVLGNGKGV
     IRNNQIFSNK EAGIYILYHG NPIVSGNHIF KGRAAGIAVN ENGKGLITEN VIRENQWGGV
     DIRRGGVPIL RSNLICFGYS DGVVVGDEGK GLIEGNTIYA NKGCGVWMMS SSLPHVTSNH
     VSYNGLYGVA VFSQKDGEFP GGHGAQENFS EDGDAILWEA ELEKEDDPLR RPITVALVES
     NSINHNGASG IFVQSSEALQ VVANVIHANG DRGITIVQSS QLTRVANNSI SCNRQSGVKV
     EFQCKVELRG NGIYDNRGHG IITKGDGTAV VENDIIGNRG SGLQLLPRSD TKVLKNRIHS
     FRAYGIAVRG RVKALVQENI IFQGKTNKTI FQQITNNREC IMQNNKFLVF KKKSDTWRLV
     NPPARPHLEN SLRGSSAAHS GHKVTAMATR ITARVEGGYH SNRSIFCTIL
//
ID   AMPH_MOUSE              Reviewed;         686 AA.
AC   Q7TQF7; Q8R1C4;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Amphiphysin;
GN   Name=Amph; Synonyms=Amph1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 AND THR-297, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250 AND SER-500, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: May participate in mechanisms of regulated exocytosis in
CC       synapses and certain endocrine cell types. May control the
CC       properties of the membrane associated cytoskeleton (By
CC       similarity).
CC   -!- SUBUNIT: Heterodimer with BIN1. Binds SH3GLB1. Interacts with
CC       AP2B1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity). Cytoplasm, cytoskeleton (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 BAR domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; BC024817; AAH24817.1; -; mRNA.
DR   EMBL; BC054718; AAH54718.1; -; mRNA.
DR   IPI; IPI00400180; -.
DR   RefSeq; NP_778172.1; NM_175007.1.
DR   UniGene; Mm.101650; -.
DR   ProteinModelPortal; Q7TQF7; -.
DR   SMR; Q7TQF7; 35-234, 606-685.
DR   MINT; MINT-1592321; -.
DR   STRING; Q7TQF7; -.
DR   PhosphoSite; Q7TQF7; -.
DR   PRIDE; Q7TQF7; -.
DR   Ensembl; ENSMUST00000003345; ENSMUSP00000003345; ENSMUSG00000021314.
DR   GeneID; 218038; -.
DR   KEGG; mmu:218038; -.
DR   UCSC; uc007pom.1; mouse.
DR   CTD; 218038; -.
DR   MGI; MGI:103574; Amph.
DR   eggNOG; roNOG04480; -.
DR   HOGENOM; HBG713912; -.
DR   HOVERGEN; HBG004224; -.
DR   InParanoid; Q7TQF7; -.
DR   OMA; MICNLAE; -.
DR   OrthoDB; EOG49078R; -.
DR   PhylomeDB; Q7TQF7; -.
DR   NextBio; 376138; -.
DR   ArrayExpress; Q7TQF7; -.
DR   Bgee; Q7TQF7; -.
DR   CleanEx; MM_AMPH; -.
DR   Genevestigator; Q7TQF7; -.
DR   GermOnline; ENSMUSG00000021314; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007612; P:learning; IMP:MGI.
DR   GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:MGI.
DR   InterPro; IPR003005; Amphiphysin.
DR   InterPro; IPR003017; Amphiphysin_1.
DR   InterPro; IPR004148; BAR.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF03114; BAR; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR01251; AMPHIPHYSIN.
DR   PRINTS; PR01252; AMPHIPHYSIN1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00721; BAR; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS51021; BAR; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW   Cytoskeleton; Membrane; Phosphoprotein; SH3 domain; Synapse.
FT   CHAIN         1    686       Amphiphysin.
FT                                /FTId=PRO_0000192948.
FT   DOMAIN       24    240       BAR.
FT   DOMAIN      613    686       SH3.
FT   COILED       10     83       Potential.
FT   COILED      144    191       Potential.
FT   COMPBIAS    261    311       Pro-rich.
FT   MOD_RES       6      6       Phosphothreonine (By similarity).
FT   MOD_RES     250    250       Phosphoserine.
FT   MOD_RES     295    295       Phosphoserine.
FT   MOD_RES     297    297       Phosphothreonine.
FT   MOD_RES     500    500       Phosphoserine.
SQ   SEQUENCE   686 AA;  75013 MW;  D292E24653A442A5 CRC64;
     MADIKTGIFA KNVQKRLNRA QEKVLQKLGK ADETKDEQFE EYVQNFKRQE AEGTRLQREL
     RGYLAAIKGM QEASMKLTES LHEVYEPDWY GREDVKMVGE KCDVLWEDFH QKLVDGSLLT
     LDTYLGQFPD IKNRIAKRSR KLVDYDSARH HLEALQSSKR KDESRISKAE EEFQKAQKVF
     EEFNVDLQEE LPSLWSSRVG FYVNTFKNVS SLEAKFHKEI AVLCHKLYEV MTKLGDQHAD
     KAFSIQGAPS DSGPLRIAKT PSPPEEPSPL PSPTASPNHT LAPASPAPVR PRSPSQTRKG
     PPVPPLPKVT PTKELKQENI INFFEDNFVP EINVTTPSQN EVLEVKKEET LLDLDFDPFK
     PDVAPAGSAA ATHSPMSQTL PWDLWTTSTD LVQPASGGSF NDFTQAQDTS LFTMQTDQNM
     AETEQALPTE PQAEEPPATA AAPTAGLDLG LEMEEPKEEA VIPPATDTGE TVETAVPTEG
     APVEEAEAEK AALPAGEGGS PEGAKIDGES TELAISESPQ PVEPEAGAPQ VIPSVVIEPA
     SNHEGEGEHQ ETATGTEPRE AAEDVAAQGS AGEKQEVATE PTPLDSQATL PASAGAVDAS
     LSAGDATQEL PPGFLYKVET LHDFEAANSD ELNLQRGDVV LVVPSDSEAD QDAGWLVGVK
     ESDWLQYRDL ATYKGLFPEN FTRRLE
//
ID   PKHA6_MOUSE             Reviewed;        1173 AA.
AC   Q7TQG1; Q8K0J5;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-FEB-2011, entry version 65.
DE   RecName: Full=Pleckstrin homology domain-containing family A member 6;
DE            Short=PH domain-containing family A member 6;
DE   AltName: Full=Phosphoinositol 3-phosphate-binding protein 3;
DE            Short=PEPP-3;
GN   Name=Plekha6; Synonyms=Pepp3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Colon, and Fetal brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472; SER-476 AND
RP   SER-901, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-492, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-816; THR-819 AND
RP   SER-901, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-868 AND SER-901, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-925, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SIMILARITY: Contains 1 PH domain.
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DR   EMBL; BC031183; AAH31183.1; -; mRNA.
DR   EMBL; BC054547; AAH54547.1; -; mRNA.
DR   IPI; IPI00279128; -.
DR   RefSeq; NP_891846.1; NM_182930.2.
DR   UniGene; Mm.253559; -.
DR   ProteinModelPortal; Q7TQG1; -.
DR   SMR; Q7TQG1; 47-160.
DR   STRING; Q7TQG1; -.
DR   PhosphoSite; Q7TQG1; -.
DR   PRIDE; Q7TQG1; -.
DR   Ensembl; ENSMUST00000038295; ENSMUSP00000048214; ENSMUSG00000041757.
DR   GeneID; 240753; -.
DR   KEGG; mmu:240753; -.
DR   UCSC; uc007cpu.1; mouse.
DR   CTD; 240753; -.
DR   MGI; MGI:2388662; Plekha6.
DR   GeneTree; ENSGT00530000063012; -.
DR   HOGENOM; HBG443707; -.
DR   HOVERGEN; HBG099912; -.
DR   InParanoid; Q7TQG1; -.
DR   OMA; SVRATRT; -.
DR   PhylomeDB; Q7TQG1; -.
DR   NextBio; 384715; -.
DR   ArrayExpress; Q7TQG1; -.
DR   Bgee; Q7TQG1; -.
DR   Genevestigator; Q7TQG1; -.
DR   GermOnline; ENSMUSG00000041757; Mus musculus.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1   1173       Pleckstrin homology domain-containing
FT                                family A member 6.
FT                                /FTId=PRO_0000053885.
FT   DOMAIN       59    158       PH.
FT   COMPBIAS    791    836       Pro-rich.
FT   MOD_RES     472    472       Phosphoserine.
FT   MOD_RES     476    476       Phosphoserine.
FT   MOD_RES     492    492       Phosphotyrosine.
FT   MOD_RES     816    816       Phosphoserine.
FT   MOD_RES     819    819       Phosphothreonine.
FT   MOD_RES     868    868       Phosphothreonine.
FT   MOD_RES     901    901       Phosphoserine.
FT   MOD_RES     925    925       Phosphoserine.
FT   MOD_RES     973    973       Phosphoserine (By similarity).
FT   MOD_RES     979    979       Phosphoserine (By similarity).
FT   MOD_RES     992    992       Phosphoserine (By similarity).
SQ   SEQUENCE   1173 AA;  131427 MW;  A71B82D513EE8B36 CRC64;
     MSNKTGGKRS ATINSDIANH NMVSEVPPER PNIRATRTSR KAIAFGKRAH SMKRNPNAPV
     TKAGWLYKQA SSGVKQWNKR WFVLVDRCLF YYKDEKQESI LGSIPLLSFR VAAVQPSDNI
     SRKHTFKAEH AGVRTYFFSA ESPEEQEAWI QAMGEAARVQ IPPAQKSVPQ PVRHSLEKPD
     SENIPPSKHH QQPPHNNLTK LEPEAKTRGE GDGRGCEKAE RRPERPEVKK ETLVKANGLP
     SGPETASEPG SPYPDGPRVP GGGEHPAQPN GWQYSSPSRP GSTAFPPHDG DSGGQRRSFP
     PRTDPDKIAQ RKSSMNQLQQ WVNLRRGVPP PEDLRSPSRF YPMPRRVPDY YNPYSSQYPD
     DYQYYPPGVR PDSICSMPAY DRISPPWALE DKRHSFRNGG GPTYQLHEWK ESTSYGRQDG
     TVWIPSPSRQ PVFYDELDAA SGSLRRLSLQ PRSHSVPRSP SQGSYSRARI YSPVRSPSAR
     FDRLPPRSED IYADPAAYVM RRSISSPKYD YLGDRRPVPA GLFPYNYPSS PTVHDKMDEL
     LDLQLQRNLE YLDQQMSESE TLISMVNRMV ENSSPRAHLF MQVPAYPEVF RDGLHTFKLN
     EQDTDKLLGK LCEQNKVVRE QERLVQQLRA EKESLESALM GTHQELEMFG SQPAYPEKLL
     HKKESLQNQL INIRVELSQA TTALTNSTVV YENLESEVSA LHDELWEQLN LDIQNEVLNR
     QIQKEIWRIQ DVMEGLRKNN PSRGTDTAKH RGGLGPSATY SSNSPASPLS SASLTSPLSP
     FSMVSGSQGS PTKPGSSEEP GPPRPPLPKA YVPLESPPTV PPLPNESRFW PYPNSPSWHR
     SGETAKGQPK TGYETSKKDP SQTSPLGTPR DINLVPTRQE VEAEKQAALN KVGIVPPRTK
     SPAEEELTPS AVVRRTTNGL TNGLSSRQER PKSAVFSGEG KVKMSVEEQM DRMRRHQSGS
     MKEKRRSLQL PASPAPEPST RPAYKVVRRH RSIHEVDISN LEAALRAEEP GGQAYETPRE
     EIARLRKMEL EPQHYDVDIS KELSTPDKVL IPERYIDLEP DTPLSPEELK EKQKKVERIK
     TLIAKSSMQN VVPIGEGDSV DVPQDSESQL QEQEKRIEIS CALATEASRR GRMLSVQCAT
     PSPPTSPASP TPPVNPLSSD RPRGADSSHT MRV
//
ID   ATX2L_MOUSE             Reviewed;        1049 AA.
AC   Q7TQH0; Q80XN9; Q8K059;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Ataxin-2-like protein;
GN   Name=Atxn2l; Synonyms=A2lp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 239-1049 (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 266-1049 (ISOFORM 3).
RC   TISSUE=Colon, Kidney, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496; SER-499 AND
RP   SER-562, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- SUBUNIT: Interacts with MPL/TPOR and EPOR and dissociates after
CC       ligand stimulation (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q7TQH0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TQH0-2; Sequence=VSP_011595, VSP_011596;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q7TQH0-3; Sequence=VSP_011595;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Thrombopoietin triggers the phosphorylation on tyrosine
CC       residues in a way that is dependent on MPL C-terminal domain (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the ataxin-2 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC034083; AAH34083.1; -; mRNA.
DR   EMBL; BC043451; AAH43451.1; -; mRNA.
DR   EMBL; BC054483; AAH54483.1; -; mRNA.
DR   IPI; IPI00169500; -.
DR   IPI; IPI00458001; -.
DR   IPI; IPI00458002; -.
DR   RefSeq; NP_898841.1; NM_183020.1.
DR   UniGene; Mm.231450; -.
DR   ProteinModelPortal; Q7TQH0; -.
DR   SMR; Q7TQH0; 126-196.
DR   STRING; Q7TQH0; -.
DR   PhosphoSite; Q7TQH0; -.
DR   PRIDE; Q7TQH0; -.
DR   Ensembl; ENSMUST00000040202; ENSMUSP00000035415; ENSMUSG00000032637.
DR   GeneID; 233871; -.
DR   KEGG; mmu:233871; -.
DR   UCSC; uc009jrr.1; mouse.
DR   UCSC; uc009jrs.1; mouse.
DR   UCSC; uc009jru.1; mouse.
DR   CTD; 233871; -.
DR   MGI; MGI:2446242; Atxn2l.
DR   GeneTree; ENSGT00530000063565; -.
DR   HOGENOM; HBG715226; -.
DR   HOVERGEN; HBG050623; -.
DR   InParanoid; Q7TQH0; -.
DR   OMA; PSQQLPF; -.
DR   OrthoDB; EOG4F4SB7; -.
DR   NextBio; 381891; -.
DR   PMAP-CutDB; Q7TQH0; -.
DR   ArrayExpress; Q7TQH0; -.
DR   Bgee; Q7TQH0; -.
DR   CleanEx; MM_ATXN2L; -.
DR   Genevestigator; Q7TQH0; -.
DR   GermOnline; ENSMUSG00000032637; Mus musculus.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR009818; Ataxin-2_C.
DR   InterPro; IPR009604; LsmAD_domain.
DR   Pfam; PF06741; LsmAD; 1.
DR   Pfam; PF07145; PAM2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Membrane; Methylation;
KW   Phosphoprotein.
FT   CHAIN         1   1049       Ataxin-2-like protein.
FT                                /FTId=PRO_0000064755.
FT   REGION       96    119       Interaction with MPL (By similarity).
FT   COMPBIAS      4     61       Pro-rich.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     109    109       Phosphoserine.
FT   MOD_RES     116    116       Phosphotyrosine (By similarity).
FT   MOD_RES     236    236       Phosphoserine (By similarity).
FT   MOD_RES     262    262       Phosphotyrosine (By similarity).
FT   MOD_RES     307    307       Phosphotyrosine (By similarity).
FT   MOD_RES     333    333       Phosphoserine (By similarity).
FT   MOD_RES     337    337       Phosphoserine (By similarity).
FT   MOD_RES     339    339       Phosphoserine (By similarity).
FT   MOD_RES     346    346       N6-acetyllysine (By similarity).
FT   MOD_RES     347    347       Phosphotyrosine (By similarity).
FT   MOD_RES     359    359       Omega-N-methylated arginine (By
FT                                similarity).
FT   MOD_RES     388    388       Phosphoserine (By similarity).
FT   MOD_RES     389    389       Phosphoserine (By similarity).
FT   MOD_RES     407    407       Phosphoserine (By similarity).
FT   MOD_RES     453    453       Phosphoserine (By similarity).
FT   MOD_RES     496    496       Phosphoserine.
FT   MOD_RES     499    499       Phosphoserine.
FT   MOD_RES     560    560       Phosphoserine (By similarity).
FT   MOD_RES     561    561       Phosphoserine (By similarity).
FT   MOD_RES     562    562       Phosphoserine.
FT   MOD_RES     592    592       Phosphoserine (By similarity).
FT   MOD_RES     597    597       Phosphoserine (By similarity).
FT   MOD_RES     600    600       Phosphoserine (By similarity).
FT   MOD_RES     601    601       Phosphoserine (By similarity).
FT   MOD_RES     633    633       Phosphoserine (By similarity).
FT   MOD_RES     637    637       Phosphoserine (By similarity).
FT   MOD_RES     687    687       Phosphoserine (By similarity).
FT   VAR_SEQ     439    444       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_011595.
FT   VAR_SEQ    1034   1049       VQSHPSQQLPFHPPGN -> GEQPGQAPGFPGGADDRIREF
FT                                SLAGGIWHGRAEGLQVGQDARVLGGD (in isoform
FT                                2).
FT                                /FTId=VSP_011596.
SQ   SEQUENCE   1049 AA;  110649 MW;  27ECCFE500688D45 CRC64;
     MLKPQPPQQT SQPQQPPPTQ QAVARRSPGG TSPPNGGLPG PLTATAAPPG PPAAVSPCLG
     PAAAAGSGLR RGAESILAAS APPQHQERPG AVAIGSVRGQ TTGKGPPQSP VFEGVYNNSR
     MLHFLTAVVG STCDVKVKNG TTYEGIFKTL SSKFELAVDA VHRKASEPAG GPRREDIVDT
     MVFKPSDVLL VHFRNVDFNY ATKDKFTDSA IAMNSKVNGE HKEKVLQRWE GGDSNSDDYD
     LESDMSNGWD PNEMFKFNEE NYGVKTTYDS SLSSYTVPLE KDNSEEFRQR ELRAAQLARE
     IESSPQYRLR IAMENDDGRT EEEKHSAVQR QGSGRESPSL VSREGKYIPL PQRVREGPRG
     GVRCSSSRGG RPGLSSLPPR GPHHLDNSSP GPGSEARGIN GGPSRMSPKA QRPLRGAKTL
     SSPSNRPSGE ASVPPTSAAL PFLPVGRMYP PRSPKSAAPA PVSASCPEPP IGSAVASSAS
     IPVTSSVVDP GAGSISPASP KLSLTPTDVK ELPTKEPSRN LEAQELARIA GKVPGLQNEQ
     KRFQLEELRK FGAQFKLQPS SSPETGLDPF PSRILKEEAK GKEKEVDGLL TSDPMGSPVS
     SKTESILDKE DKVPMAGVGG TEGPEQLPAP CPSQTGSPPV GLIKGDEKEE GPVTEQVKKS
     TLNPNAKEFN PTKPLLSVNK STSTPTSPGP RTHSTPSIPV LTAGQSGLYS PQYISYIPQI
     HMGPAVQAPQ MYPYPVSNSV PGQQGKYRGA KGSLPPQRSD QHQPASAPPM MQAAAAAAGP
     PLVAATPYSS YIPYNPQQFP GQPAMMQPMA HYPSQPVFAP MLQSNPRMLT SGSHPQAIVS
     SSTPQYPAAE QPTPQALYAT VHQSYPHHAT QLHGHQPQPA TTPTGSQPQS QHAAPSPVQH
     QAGQAPHLGS GQPQQNLYHP GALTGTPPSL PPGPSAQSPQ SSFPQPAAVY AIHPHQQLPH
     GFTNMAHVTQ AHVQTGVTAA PPPHPGAPHP PQVMLLHPPQ GHGGPPQGAV PPSGVPALSA
     STPSPYPYIG HPQVQSHPSQ QLPFHPPGN
//
ID   OTUB1_MOUSE             Reviewed;         271 AA.
AC   Q7TQI3; Q3ULV9; Q3V408; Q8C326; Q8R5F2;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Ubiquitin thioesterase OTUB1;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme OTUB1;
DE   AltName: Full=OTU domain-containing ubiquitin aldehyde-binding protein 1;
DE   AltName: Full=Otubain-1;
DE   AltName: Full=Ubiquitin-specific-processing protease OTUB1;
GN   Name=Otub1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Corpora quadrigemina, Embryo, Mammary gland, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 189-198, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [4]
RP   FUNCTION.
RX   PubMed=14661020; DOI=10.1038/ni1017;
RA   Soares L., Seroogy C., Skrenta H., Anandasabapathy N., Lovelace P.,
RA   Chung C.D., Engleman E., Fathman C.G.;
RT   "Two isoforms of otubain 1 regulate T cell anergy via GRAIL.";
RL   Nat. Immunol. 5:45-54(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from
CC       proteins in vitro and may therefore play an important regulatory
CC       role at the level of protein turnover by preventing degradation.
CC       Regulator of T-cell anergy, a phenomenon that occurs when T-cells
CC       are rendered unresponsive to antigen rechallenge and no longer
CC       respond to their cognate antigen. Acts via its interaction with
CC       RNF128/GRAIL. Surprisingly, it regulates RNF128-mediated
CC       ubiquitination, but does not deubiquitinate polyubiquitinated
CC       RNF128. Deubiquitinates estrogen receptor alpha (ESR1). Mediates
CC       deubiquitination of 'Lys-48'-linked polyubiquitin chains, but not
CC       'Lys-63'-linked polyubiquitin chains. Not able to cleave di-
CC       ubiquitin. Also capable of removing NEDD8 from NEDD8 conjugates,
CC       but with a nuch lower preference compared to 'Lys-48'-linked
CC       ubiquitin.
CC   -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- SUBUNIT: Interacts with RNF128. Forms a ternary complex with
CC       RNF128 and USP8. Interacts with FUS, ESR1 and GNB2L1/RACK1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase C65 family.
CC   -!- SIMILARITY: Contains 1 OTU domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK027996; BAE20433.1; -; mRNA.
DR   EMBL; AK140070; BAE24227.1; -; mRNA.
DR   EMBL; AK145273; BAE26339.1; -; mRNA.
DR   EMBL; AK145970; BAE26795.1; -; mRNA.
DR   EMBL; BC022575; AAH22575.1; -; mRNA.
DR   EMBL; BC054410; AAH54410.1; -; mRNA.
DR   IPI; IPI00154004; -.
DR   RefSeq; NP_598911.1; NM_134150.2.
DR   UniGene; Mm.203921; -.
DR   ProteinModelPortal; Q7TQI3; -.
DR   SMR; Q7TQI3; 45-271.
DR   STRING; Q7TQI3; -.
DR   MEROPS; C65.001; -.
DR   PhosphoSite; Q7TQI3; -.
DR   REPRODUCTION-2DPAGE; Q7TQI3; -.
DR   PRIDE; Q7TQI3; -.
DR   Ensembl; ENSMUST00000025679; ENSMUSP00000025679; ENSMUSG00000024767.
DR   GeneID; 107260; -.
DR   KEGG; mmu:107260; -.
DR   UCSC; uc008gki.1; mouse.
DR   CTD; 107260; -.
DR   MGI; MGI:2147616; Otub1.
DR   eggNOG; maNOG17115; -.
DR   GeneTree; ENSGT00390000006979; -.
DR   HOGENOM; HBG521362; -.
DR   HOVERGEN; HBG053383; -.
DR   InParanoid; Q7TQI3; -.
DR   OMA; RRDGNCF; -.
DR   OrthoDB; EOG47H5QS; -.
DR   PhylomeDB; Q7TQI3; -.
DR   NextBio; 459530; -.
DR   ArrayExpress; Q7TQI3; -.
DR   Bgee; Q7TQI3; -.
DR   CleanEx; MM_OTUB1; -.
DR   Genevestigator; Q7TQI3; -.
DR   GermOnline; ENSMUSG00000024767; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019784; F:NEDD8-specific protease activity; ISS:UniProtKB.
DR   GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR   GO; GO:0004843; F:ubiquitin-specific protease activity; ISS:UniProtKB.
DR   GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR   InterPro; IPR003323; OTU.
DR   InterPro; IPR019400; Peptidase_C65_otubain.
DR   InterPro; IPR016615; Ubiquitin_thioesterase_Otubain.
DR   Pfam; PF10275; Peptidase_C65; 1.
DR   PIRSF; PIRSF013503; Ubiquitin_thioesterase_Otubain; 1.
DR   PROSITE; PS50802; OTU; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Adaptive immunity; Cytoplasm; Direct protein sequencing;
KW   Hydrolase; Immunity; Phosphoprotein; Protease; Thiol protease;
KW   Ubl conjugation pathway.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    271       Ubiquitin thioesterase OTUB1.
FT                                /FTId=PRO_0000221009.
FT   DOMAIN       80    271       OTU.
FT   ACT_SITE     88     88       By similarity.
FT   ACT_SITE     91     91       Nucleophile (By similarity).
FT   ACT_SITE    265    265       By similarity.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      16     16       Phosphoserine.
FT   MOD_RES     188    188       N6-acetyllysine (By similarity).
FT   CONFLICT    186    186       E -> D (in Ref. 1; BAE20433).
SQ   SEQUENCE   271 AA;  31270 MW;  32F78EE1DC5FD679 CRC64;
     MAAEEPQQQK QEPLGSDSEG VNCLAYDEAI MAQQDRIQQE IAVQNPLVSE RLELSVLYKE
     YAEDDNIYQQ KIKDLHKKYS YIRKTRPDGN CFYRAFGFSH LEALLDDSKE LQRFKAVSAK
     SKEDLVSQGF TEFTIEDFHN TFMDLIEQVE KQTSVADLLA SFNDQSTSDY LVVYLRLLTS
     GYLQRESKFF EHFIEGGRTV KEFCQQEVEP MCKESDHIHI IALAQALSVS IQVEYMDRGE
     GGTTNPHVFP EGSEPKVYLL YRPGHYDILY K
//
ID   Q7TRM4_MOUSE            Unreviewed;       354 AA.
AC   Q7TRM4;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 2.
DT   08-MAR-2011, entry version 64.
DE   SubName: Full=Olfactory receptor Olfr735;
GN   Name=Olfr735;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=22974002; PubMed=14611657; DOI=10.1186/gb-2003-4-11-r71;
RA   Young J.M., Shykind B.M., Lane R.P., Tonnes-Priddy L., Ross J.A.,
RA   Walker M., Williams E.M., Trask B.J.;
RT   "Odorant receptor expressed sequence tags demonstrate olfactory
RT   expression of over 400 genes, extensive alternate splicing and unequal
RT   expression levels.";
RL   Genome Biol. 4:R71.1-R71.13(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Sanders K.;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RA   Young J.M.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
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DR   EMBL; AY317860; AAP71198.2; -; Genomic_DNA.
DR   IPI; IPI00380634; -.
DR   RefSeq; NP_001011754.1; NM_001011754.2.
DR   UniGene; Mm.482035; -.
DR   ProteinModelPortal; Q7TRM4; -.
DR   SMR; Q7TRM4; 60-341.
DR   STRING; Q7TRM4; -.
DR   PRIDE; Q7TRM4; -.
DR   Ensembl; ENSMUST00000049729; ENSMUSP00000056851; ENSMUSG00000046210.
DR   GeneID; 257909; -.
DR   KEGG; mmu:257909; -.
DR   UCSC; uc007tky.1; mouse.
DR   CTD; 257909; -.
DR   MGI; MGI:3030569; Olfr735.
DR   eggNOG; maNOG16449; -.
DR   GeneTree; ENSGT00580000081417; -.
DR   HOGENOM; HBG755317; -.
DR   HOVERGEN; HBG017625; -.
DR   InParanoid; Q7TRM4; -.
DR   OrthoDB; EOG4WWRK7; -.
DR   PhylomeDB; Q7TRM4; -.
DR   NextBio; 387788; -.
DR   ArrayExpress; Q7TRM4; -.
DR   Genevestigator; Q7TRM4; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0004984; F:olfactory receptor activity; IEA:InterPro.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR000725; Olfact_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00245; OLFACTORYR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   G-protein coupled receptor; Membrane; Receptor; Transducer;
KW   Transmembrane.
SQ   SEQUENCE   354 AA;  40221 MW;  8D43C26D39CD0E21 CRC64;
     MVHADKQEVL SHNFSFLFNL TYLVQFNFSS TRSLDTLGLE KNKNSSDVSR FVLLGLSSSW
     ELQLFLFFTF LLIYLVIVLG NLLIVMVVQA DAHLFQSPMY YFLSHLSFID LCLSCVAVPK
     MLGDFLQKEK TISFSGCLAQ VFFLHFLGAS EMFLLTVMAY DRYVAICNPL HYLTVMNNHL
     RLRLVFGCWC GGFIHSITQV MIVIQLPFCG PNELDNFYCD VPQVVKLACM DTYLVEVLMV
     SNSGILSLVC FLVLLFSYAL ILITLRTHLH RGQSKALSTC ASHLTVVSLI FVPCVFIYLR
     PFCTFSVDKV VSVFYTVITP MLNPLIYTLR NADMKQAIEK LRKKQVASHC FAKG
//
ID   Q7TS40_MOUSE            Unreviewed;       306 AA.
AC   Q7TS40;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   SubName: Full=Olfactory receptor 198;
DE   SubName: Full=Olfactory receptor Olfr198;
GN   Name=Olfr198; ORFNames=mCG_141734;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=22974002; PubMed=14611657; DOI=10.1186/gb-2003-4-11-r71;
RA   Young J.M., Shykind B.M., Lane R.P., Tonnes-Priddy L., Ross J.A.,
RA   Walker M., Williams E.M., Trask B.J.;
RT   "Odorant receptor expressed sequence tags demonstrate olfactory
RT   expression of over 400 genes, extensive alternate splicing and unequal
RT   expression levels.";
RL   Genome Biol. 4:R71.1-R71.13(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Sanders K.;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC147215; AAI47216.1; -; mRNA.
DR   EMBL; AY317283; AAP70786.1; -; Genomic_DNA.
DR   EMBL; CH466521; EDK98212.1; -; Genomic_DNA.
DR   IPI; IPI00408456; -.
DR   RefSeq; NP_001011808.1; NM_001011808.1.
DR   UniGene; Mm.390851; -.
DR   ProteinModelPortal; Q7TS40; -.
DR   SMR; Q7TS40; 3-157.
DR   STRING; Q7TS40; -.
DR   PRIDE; Q7TS40; -.
DR   Ensembl; ENSMUST00000064452; ENSMUSP00000065535; ENSMUSG00000052537.
DR   GeneID; 258036; -.
DR   KEGG; mmu:258036; -.
DR   UCSC; uc007zow.1; mouse.
DR   CTD; 258036; -.
DR   MGI; MGI:3030032; Olfr198.
DR   eggNOG; maNOG19088; -.
DR   GeneTree; ENSGT00550000074564; -.
DR   HOGENOM; HBG755317; -.
DR   HOVERGEN; HBG017625; -.
DR   InParanoid; Q7TS40; -.
DR   OMA; FIQSFTF; -.
DR   OrthoDB; EOG4ZPDVX; -.
DR   PhylomeDB; Q7TS40; -.
DR   NextBio; 388128; -.
DR   Genevestigator; Q7TS40; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0004984; F:olfactory receptor activity; IEA:InterPro.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR000725; Olfact_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00245; OLFACTORYR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   G-protein coupled receptor; Membrane; Receptor; Transducer;
KW   Transmembrane.
SQ   SEQUENCE   306 AA;  34815 MW;  3D925B0BEB8BF647 CRC64;
     MTVENQTVVA VFVLTGLTER PELQVPLFLV FFTIYLITMV GNLGLIALIW KDPHLHTPMY
     LFLGSLAFAD ACASSSVTPK MLVNFLSKDH RTFLVECFTQ FYFFGSSATT ECFLLSVMAY
     DRYVAICNPL LYPVMMSNSL CMKFIHVSYI VGFLHSAIHV GLLVRLNFCK SNIIHYFYCE
     ILQLFKISCT DPTMNVLLVL IFSALIQGLT FMTIIVSYFS VLLAILKTKS ERGRRKAFST
     CSAHLLSVSL FYGTLFLMYV RPGSGSGEDK DRMYSLFYTI IIPFLNPFIY SLRNKEVTAA
     LRRKMK
//
ID   Q7TS51_MOUSE            Unreviewed;       313 AA.
AC   Q7TS51;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   SubName: Full=Olfactory receptor Olfr171;
GN   Name=Olfr171;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=22974002; PubMed=14611657; DOI=10.1186/gb-2003-4-11-r71;
RA   Young J.M., Shykind B.M., Lane R.P., Tonnes-Priddy L., Ross J.A.,
RA   Walker M., Williams E.M., Trask B.J.;
RT   "Odorant receptor expressed sequence tags demonstrate olfactory
RT   expression of over 400 genes, extensive alternate splicing and unequal
RT   expression levels.";
RL   Genome Biol. 4:R71.1-R71.13(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Sanders K.;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
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CC   -----------------------------------------------------------------------
DR   EMBL; AY317255; AAP70765.1; -; Genomic_DNA.
DR   IPI; IPI00127303; -.
DR   RefSeq; NP_667169.2; NM_146958.2.
DR   UniGene; Mm.377771; -.
DR   ProteinModelPortal; Q7TS51; -.
DR   Ensembl; ENSMUST00000079891; ENSMUSP00000078814; ENSMUSG00000060480.
DR   GeneID; 258960; -.
DR   KEGG; mmu:258960; -.
DR   NMPDR; fig|10090.3.peg.31013; -.
DR   UCSC; uc007ypa.1; mouse.
DR   CTD; 258960; -.
DR   MGI; MGI:3030005; Olfr171.
DR   eggNOG; roNOG14230; -.
DR   HOVERGEN; HBG017625; -.
DR   InParanoid; Q7TS51; -.
DR   OMA; CEIPAML; -.
DR   OrthoDB; EOG4N8R5B; -.
DR   PhylomeDB; Q7TS51; -.
DR   NextBio; 391313; -.
DR   Genevestigator; Q7TS51; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0004984; F:olfactory receptor activity; IEA:InterPro.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR000725; Olfact_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00245; OLFACTORYR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   3: Inferred from homology;
KW   G-protein coupled receptor; Membrane; Receptor; Transducer;
KW   Transmembrane.
SQ   SEQUENCE   313 AA;  35877 MW;  F9C24DED55C7E3B5 CRC64;
     MERENYTFNS DFILLGLFSS SKISLTFFSV IFFIFIMTIT ENALMILLIH RDSRLHTPMY
     FLLSHLSFMD ILHISNIVPK MIADFLSGSR TISFAGCAFQ IFLSLTLLGG ECLLLAVMSY
     DRYVAICHPL RYPVLMRDNF SGLLAAGSWL VGILNSIVHT AFVLHFPFCH SRAIDHFFCE
     VPAMLKLSCI DTTHYERGVY VSGIIFLLIP FSMISISYVQ ILLTVFQMHS SGARQKSFST
     CLFHMVVVIM YYGPFIFTYM RPRSYHTPGQ DKFLAIFYTI LTPTLNPIIY SFRNKDVLMA
     LKNIVQSNIL NKE
//
ID   PRC2A_MOUSE             Reviewed;        2158 AA.
AC   Q7TSC1; Q923A9; Q9Z1R1;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Protein PRRC2A;
DE   AltName: Full=HLA-B-associated transcript 2;
DE   AltName: Full=Proline-rich and coiled-coil-containing protein 2A;
GN   Name=Prrc2a; Synonyms=Bat2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129;
RX   PubMed=14656967; DOI=10.1101/gr.1736803;
RA   Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
RA   Campbell R.D., Hood L.;
RT   "Analysis of the gene-dense major histocompatibility complex class III
RT   region and its comparison to mouse.";
RL   Genome Res. 13:2621-2636(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 82-89, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-782, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-609; SER-1002 AND
RP   SER-1217, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759; SER-761; SER-1087;
RP   SER-1090 AND SER-1217, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342; SER-350; SER-1087
RP   AND SER-1090, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-808 AND SER-1217, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: May play a role in the regulation of pre-mRNA splicing
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AF109719; AAC82480.1; -; Genomic_DNA.
DR   EMBL; BC006664; AAH06664.1; -; mRNA.
DR   EMBL; BC053522; AAH53522.1; -; mRNA.
DR   IPI; IPI00380722; -.
DR   RefSeq; NP_001185973.1; NM_001199044.1.
DR   RefSeq; NP_064411.2; NM_020027.3.
DR   UniGene; Mm.272462; -.
DR   ProteinModelPortal; Q7TSC1; -.
DR   IntAct; Q7TSC1; 1.
DR   STRING; Q7TSC1; -.
DR   PhosphoSite; Q7TSC1; -.
DR   PRIDE; Q7TSC1; -.
DR   Ensembl; ENSMUST00000025253; ENSMUSP00000025253; ENSMUSG00000024393.
DR   GeneID; 53761; -.
DR   KEGG; mmu:53761; -.
DR   UCSC; uc008cgi.1; mouse.
DR   CTD; 53761; -.
DR   MGI; MGI:1915467; Prrc2a.
DR   HOGENOM; HBG269398; -.
DR   HOVERGEN; HBG004820; -.
DR   InParanoid; Q7TSC1; -.
DR   OMA; PRRAGPI; -.
DR   OrthoDB; EOG4G7BXH; -.
DR   NextBio; 310575; -.
DR   ArrayExpress; Q7TSC1; -.
DR   Bgee; Q7TSC1; -.
DR   CleanEx; MM_BAT2; -.
DR   Genevestigator; Q7TSC1; -.
DR   GermOnline; ENSMUSG00000024393; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR009738; BAT2_N.
DR   Pfam; PF07001; BAT2_N; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Nucleus;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1   2158       Protein PRRC2A.
FT                                /FTId=PRO_0000064831.
FT   REPEAT       41     95       1-1.
FT   REPEAT       98    154       1-2.
FT   REPEAT      281    337       1-3.
FT   REPEAT      337    428       2-1.
FT   REPEAT      486    559       2-2.
FT   REPEAT     1756   1811       1-4.
FT   REPEAT     1917   1966       3-1.
FT   REPEAT     1983   2032       3-2.
FT   REPEAT     2058   2107       3-3.
FT   REGION       41   1811       4 X 57 AA type A repeats.
FT   REGION      337    559       2 X type B repeats.
FT   REGION     1917   2107       3 X 50 AA type C repeats.
FT   COMPBIAS    401    413       Poly-Pro.
FT   COMPBIAS    464    469       Poly-Arg.
FT   COMPBIAS    470    473       Poly-Glu.
FT   COMPBIAS    657    669       Poly-Gln.
FT   COMPBIAS    696    700       Poly-Pro.
FT   COMPBIAS    826    833       Poly-Pro.
FT   COMPBIAS    912    915       Poly-Pro.
FT   COMPBIAS    954    957       Poly-Pro.
FT   COMPBIAS   1234   1239       Poly-Arg.
FT   COMPBIAS   1292   1295       Poly-Pro.
FT   COMPBIAS   1409   1417       Poly-Gly.
FT   COMPBIAS   1447   1453       Poly-Pro.
FT   MOD_RES      27     27       N6-acetyllysine (By similarity).
FT   MOD_RES     114    114       Phosphoserine (By similarity).
FT   MOD_RES     166    166       Phosphoserine.
FT   MOD_RES     204    204       Phosphoserine (By similarity).
FT   MOD_RES     342    342       Phosphoserine.
FT   MOD_RES     350    350       Phosphoserine.
FT   MOD_RES     378    378       Phosphoserine (By similarity).
FT   MOD_RES     381    381       Phosphoserine (By similarity).
FT   MOD_RES     454    454       Phosphoserine (By similarity).
FT   MOD_RES     608    608       Phosphothreonine (By similarity).
FT   MOD_RES     609    609       Phosphothreonine.
FT   MOD_RES     759    759       Phosphoserine.
FT   MOD_RES     761    761       Phosphoserine.
FT   MOD_RES     764    764       Phosphoserine (By similarity).
FT   MOD_RES     766    766       Phosphoserine (By similarity).
FT   MOD_RES     782    782       Phosphothreonine.
FT   MOD_RES     808    808       Phosphoserine.
FT   MOD_RES     995    995       Phosphothreonine (By similarity).
FT   MOD_RES    1002   1002       Phosphoserine.
FT   MOD_RES    1012   1012       Phosphoserine (By similarity).
FT   MOD_RES    1083   1083       Phosphoserine (By similarity).
FT   MOD_RES    1085   1085       Phosphothreonine (By similarity).
FT   MOD_RES    1087   1087       Phosphoserine.
FT   MOD_RES    1090   1090       Phosphoserine.
FT   MOD_RES    1092   1092       Phosphotyrosine (By similarity).
FT   MOD_RES    1145   1145       Phosphoserine (By similarity).
FT   MOD_RES    1194   1194       N6-acetyllysine (By similarity).
FT   MOD_RES    1217   1217       Phosphoserine.
FT   MOD_RES    1302   1302       Phosphoserine (By similarity).
FT   MOD_RES    1343   1343       Phosphothreonine (By similarity).
FT   MOD_RES    1349   1349       Phosphothreonine (By similarity).
FT   CONFLICT   1846   1846       Missing (in Ref. 1; AAC82480).
SQ   SEQUENCE   2158 AA;  229203 MW;  85A5CBDCDA84A256 CRC64;
     MSDRSGPTAK GKDGKKYSSL NLFDTYKGKS LEIQKPAVAP RHGLQSLGKV AIARRMPPPA
     NLPSLKAENK GNDPNVSLVP KDGTGWASKQ EQSDPKSSDA STAQPPESQP LPASQTPASN
     QPKRPPTAPE NTPSVPSGVK SWAQASVTHG AHGDGGRASN LLSRFSREEF PTLQAAGDQD
     KAAKERESAE QSSGPGPSLR PQNSTTWRDG GGRGPDDLEG PDSKLHHGHD PRGGLQPSGP
     PQFPPYRGMM PPFMYPPYLP FPPPYGPQGP YRYPTPDGPS RFPRVAGPRG SGPPMRLVEP
     VGRPSILKED NLKEFDQLDQ ENDDGWAGAH EEVDYTEKLK FSDEEDGRDS DEEGAEGHKD
     SQSAAAEEPE TDGKKGTSPG SELPPPKTAW TENARPSETE PAPPTPKPPP PPPHRGPVGN
     WGPPGDYPDR GGPPCKPPAP EDEDEAWRQR RKQSSSEISL AVERARRRRE EEERRMQEER
     RAACAEKLKR LDEKFGAPDK RLKAEPAAPP VTPAAPALPP VVPKEIPAAP ALPPTPTPTP
     EKEPEEPAQA PPVQAAPSPG VAPVPTLVSG GGCTANSNSS GSFEASPVEP QLPSKEGPEP
     PEEVPPPTTP PAPKMEPKGD GVGSTRQPPS QGLGYPKYQK SLPPRFQRQQ QEQLLKQQQQ
     QQQWQQQQQG TAPPAPVPPS PPQPVTLGAV PAPQAPPPPP KALYPGALGR PPPMPPMNFD
     PRWMMIPPYV DPRLLQGRPP LDFYPPGVHP SGLVPRERSD SGGSSSEPFE RHAPPLLRER
     GTPPVDPKLA WVGDVFTTTP TDPRPLTSPL RQAADEEEKS MRSETPPVPP PPPYLANYPG
     FPENGTPGPP ISRFPLEESA PPGPRPLPWP PGNDEAAKMQ APPPKKEPSK EEPPQLSGPE
     AGRKPARGGQ GPPPPRRENR TETRWGPRPG SCRRGIPPEE PGVPPRRAGP IKKPPPPVKV
     EELPPKSLEQ GDETPKVPKP DALKTAKGKV GPKETPPGGN LSPAPRLRRD YSYERVGPTS
     CRGRGRGEYF ARGRGFRGTY GGRGRGARSR EFRSYREFRG DDGRGGGSGG TNHPSAPRGR
     TASETRSEGS EYEEIPKRRR QRGSETGSET HESDLAPSDK EAPPPKEGVL GQVPLAPPQP
     GAPPSPAPAR FSTARGGRVF TPRGVPSRRG RGGGRPPPVC SGWSPPAKSL VPKKPPTGPL
     PPSKEPLKEK LISGPLSPMS RAGNMGVGME DGERPRRRRH GRAQQQDKPP RFRRLKQERE
     NAARGADGKP PSLTLAASTP GPEETLTAAT VPPPPRRTAA KSPDLSNQNS DQANEEWETA
     SESSDFASER RGDKETPPAA LMTSKAVGTP GANAGGAGPG ISAMSRGDLS QRAKDLSKRS
     FSSQRPGMDR QNRRPGTGGK TGSGGGSSGG GGAGPGGRTG PGRGDKRSWP SPKNRSRPPE
     ERPPGLPLPP PPPSSSAVFR LDQVIHSNPA GIQQALAQLS SRQGNVTAPG GHPRPKPGPP
     QAPQGSSPRP PTRYDPPRAS SAISSDPHFE EPGPMVRGVG GTPRDSAGVN PFPPKRRERP
     PRKPELLQEE TVPASHSSGF LGSKPEVPGP QEESRDSGTE ALTPHIWNRL HTATSRKSYQ
     PGSIEPWMEP LSPFEDVAGT EMSQSDSGVD LSGDSQVSSG PCSQRSSPDG GLKGSAEGPP
     KRPGGPSPLN AVPGESASGS EPSEPPRRRP PASHEGERKE LPREQPLPPG PIGTERSQRT
     DRGPEPGPLR PAHRPGSQVE FGTTNKDSDL CLVVGDTLKG EKELVASATE AVPISRDWEL
     LPSASTSAEP QPKSLGSGQC VPEPSPSGQR PYPEVFYGSP GPPNSQQVSG GAPIDSQLHP
     NSGGFRPGTP SLHQYRSQPL YLPPGPAPPS ALLSGVALKG QFLDFSALQA TELGKLPAGG
     VLYPPPSFLY SAAFCPSPLP DPPLLQVRQD LPSPSDFYST PLQPGGQSGF LPSGAPAQQM
     LLPVVDSQLP VVNFGSLPPA PPPAPPPLSL LPVGPALQPP NLAVRPPPAP AARVLPSPAR
     PFAPSLGRAE LHPVELKPFQ DYRKLSSNLG GPGSSRTPPS GRPFSGLNSR LKAPPSTYSG
     VFRTQRIDLY QQASPPDALR WMPKPWERAG PPSREGPPRR AEEPGSRGEK EPGLPPPR
//
ID   CQ076_MOUSE             Reviewed;         339 AA.
AC   Q7TSF4; Q3UIX7; Q811G5;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 47.
DE   RecName: Full=Leucine-rich repeat-containing protein C17orf76 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Amnion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II; TISSUE=Limb, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7TSF4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TSF4-2; Sequence=VSP_025136;
CC   -!- SIMILARITY: Contains 2 LRR (leucine-rich) repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK146714; BAE27379.1; -; mRNA.
DR   EMBL; AL596181; CAI24668.1; -; Genomic_DNA.
DR   EMBL; BC046404; AAH46404.1; -; mRNA.
DR   EMBL; BC053455; AAH53455.1; -; mRNA.
DR   IPI; IPI00353176; -.
DR   IPI; IPI00752176; -.
DR   RefSeq; NP_942561.1; NM_198861.1.
DR   UniGene; Mm.339972; -.
DR   ProteinModelPortal; Q7TSF4; -.
DR   SMR; Q7TSF4; 154-290.
DR   PhosphoSite; Q7TSF4; -.
DR   PRIDE; Q7TSF4; -.
DR   Ensembl; ENSMUST00000057194; ENSMUSP00000062489; ENSMUSG00000046417.
DR   GeneID; 192976; -.
DR   KEGG; mmu:192976; -.
DR   UCSC; uc007jjo.1; mouse.
DR   MGI; MGI:2682293; BC046404.
DR   eggNOG; roNOG17914; -.
DR   GeneTree; ENSGT00390000004841; -.
DR   HOGENOM; HBG505803; -.
DR   HOVERGEN; HBG066484; -.
DR   InParanoid; Q7TSF4; -.
DR   OMA; CRQLTYH; -.
DR   OrthoDB; EOG4TF0MB; -.
DR   PhylomeDB; Q7TSF4; -.
DR   NextBio; 371398; -.
DR   ArrayExpress; Q7TSF4; -.
DR   Bgee; Q7TSF4; -.
DR   CleanEx; MM_BC046404; -.
DR   Genevestigator; Q7TSF4; -.
PE   1: Evidence at protein level;
KW   Alternative splicing; Leucine-rich repeat; Phosphoprotein; Repeat.
FT   CHAIN         1    339       Leucine-rich repeat-containing protein
FT                                C17orf76 homolog.
FT                                /FTId=PRO_0000286625.
FT   REPEAT      203    216       LRR 1.
FT   REPEAT      228    241       LRR 2.
FT   MOD_RES     322    322       Phosphoserine.
FT   VAR_SEQ       1     85       Missing (in isoform 2).
FT                                /FTId=VSP_025136.
SQ   SEQUENCE   339 AA;  37574 MW;  A5674A624291CE84 CRC64;
     MGTRQTKGSL AERASPGAAP GPRRERPDFW ASLLLRAGDK AGRAGSGLPP YHRRVGMVQE
     LLRMVRQGRR EEAGTLLQHL RQDLGMESTS LDDVLYRYAS FRNLVDPITH DLIISLARYI
     HCPKPEGDAM GAMEKLCRQL TYHLSPHSQW RRHRGLKRKP QACLKALLSG NPPDNMVDLS
     GIPLTSRDLE RVTSYLQRCG EQVDSVELGF TGLTDDMVLQ LLPALSTLPR LTTLALNGNR
     LTRALLRDLT DTLKDPSKFP NVTWIDLGNN VDIFSLPQPF LLSLRKRSPK QGHLPTILEL
     GEGPGTGEEA REGTDQQDPI GSPVTPARGQ ESTECVIQT
//
ID   CTDP1_MOUSE             Reviewed;         960 AA.
AC   Q7TSG2; Q7TSS7; Q9D4S8;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=RNA polymerase II subunit A C-terminal domain phosphatase;
DE            EC=3.1.3.16;
DE   AltName: Full=TFIIF-associating CTD phosphatase;
GN   Name=Ctdp1; Synonyms=Fcp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryo, and Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502; SER-860 AND
RP   SER-863, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Processively dephosphorylates 'Ser-2' and 'Ser-5' of the
CC       heptad repeats YSPTSPS in the C-terminal domain of the largest RNA
CC       polymerase II subunit. This promotes the activity of RNA
CC       polymerase II (By similarity).
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- SUBUNIT: Homodimer. Interacts with GTF2F1 (By similarity).
CC       Interacts with WDR77, SNRPB and SNRNP70 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7TSG2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TSG2-2; Sequence=VSP_009866, VSP_009867;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated. In the presence of TFIIF, the phosphorylated
CC       form has an increased CTD phosphatase activity. The
CC       phosphorylation is required for the physical interaction with
CC       GTF2F1 (By similarity).
CC   -!- SIMILARITY: Contains 1 BRCT domain.
CC   -!- SIMILARITY: Contains 1 FCP1 homology domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK016213; BAB30150.1; -; mRNA.
DR   EMBL; BC052934; AAH52934.1; -; mRNA.
DR   EMBL; BC053435; AAH53435.1; -; mRNA.
DR   IPI; IPI00338904; -.
DR   IPI; IPI00411156; -.
DR   RefSeq; NP_080571.2; NM_026295.2.
DR   UniGene; Mm.312893; -.
DR   ProteinModelPortal; Q7TSG2; -.
DR   SMR; Q7TSG2; 21-111, 157-720.
DR   STRING; Q7TSG2; -.
DR   PhosphoSite; Q7TSG2; -.
DR   PRIDE; Q7TSG2; -.
DR   Ensembl; ENSMUST00000036229; ENSMUSP00000038938; ENSMUSG00000033323.
DR   Ensembl; ENSMUST00000114707; ENSMUSP00000110355; ENSMUSG00000033323.
DR   GeneID; 67655; -.
DR   KEGG; mmu:67655; -.
DR   UCSC; uc008ftb.1; mouse.
DR   CTD; 67655; -.
DR   MGI; MGI:1926953; Ctdp1.
DR   GeneTree; ENSGT00390000015641; -.
DR   HOGENOM; HBG403000; -.
DR   HOVERGEN; HBG051213; -.
DR   InParanoid; Q7TSG2; -.
DR   OMA; THLIAAR; -.
DR   OrthoDB; EOG4HMJ8T; -.
DR   PhylomeDB; Q7TSG2; -.
DR   BRENDA; 3.1.3.16; 244.
DR   NextBio; 325156; -.
DR   ArrayExpress; Q7TSG2; -.
DR   Bgee; Q7TSG2; -.
DR   Genevestigator; Q7TSG2; -.
DR   GermOnline; ENSMUSG00000033323; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR001357; BRCT.
DR   InterPro; IPR015388; FCP1_C.
DR   InterPro; IPR011947; FCP1_euk.
DR   InterPro; IPR023214; HAD-like_dom.
DR   InterPro; IPR004274; NIF.
DR   Gene3D; G3DSA:3.40.50.1000; HAD-like_dom; 2.
DR   Pfam; PF09309; FCP1_C; 1.
DR   Pfam; PF03031; NIF; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SMART; SM00577; CPDc; 1.
DR   SUPFAM; SSF52113; BRCT; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR02250; FCP1_euk; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS50969; FCP1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Hydrolase; Nucleus; Phosphoprotein;
KW   Protein phosphatase.
FT   CHAIN         1    960       RNA polymerase II subunit A C-terminal
FT                                domain phosphatase.
FT                                /FTId=PRO_0000212565.
FT   DOMAIN      178    341       FCP1 homology.
FT   DOMAIN      619    718       BRCT.
FT   COMPBIAS    414    417       Poly-Ser.
FT   COMPBIAS    568    572       Poly-Glu.
FT   COMPBIAS    573    578       Poly-Asp.
FT   MOD_RES     502    502       Phosphoserine.
FT   MOD_RES     664    664       Phosphoserine (By similarity).
FT   MOD_RES     730    730       Phosphoserine (By similarity).
FT   MOD_RES     770    770       N6-acetyllysine (By similarity).
FT   MOD_RES     860    860       Phosphoserine.
FT   MOD_RES     863    863       Phosphoserine.
FT   VAR_SEQ       1    788       Missing (in isoform 2).
FT                                /FTId=VSP_009866.
FT   VAR_SEQ     789    796       NHGEPSSF -> MSRIILVV (in isoform 2).
FT                                /FTId=VSP_009867.
FT   CONFLICT    759    761       PEV -> GTR (in Ref. 2; AAH52934).
FT   CONFLICT    897    897       V -> I (in Ref. 2; AAH52934).
SQ   SEQUENCE   960 AA;  104554 MW;  7D1EB42C6D15C95C CRC64;
     MEAPPAAGVP TECTPAVAGA EVRCPGPTPL RLLEWKVAAG ATVRIGSVLA VCETAASAQP
     AGPAPARAAS GGCVRAARTE RRLRSERAGV VRELCAQPGQ VVAPGALLVR LEGCSHPVVM
     KGLCAECGQD LTQLQSKNGR QQVPLSTATV SMVHSVPELM VSSEQAEKLG REDQQRLHRN
     RKLVLMVDLD QTLIHTTEQH CPQMSNKGIF HFQLGRGEPM LHTRLRPHCK DFLEKIAKLY
     ELHVFTFGSR LYAHTIAGFL DPEKKLFSHR ILSRDECIDP FSKTGNLRNL FPCGDSMVCI
     IDDREDVWKF APNLITVKKY VYFPGTGDVN APPAARETQA RRKVNHSSKG GDALEQALSV
     RDPEDGRPAP GVEHSNGLGK ASRELNGGEA VPGVFPSKAD EKEAWPLTRA SPASSSSGHE
     PTEAPELPVS CEWDGRTTPG VQPTQGDAAT QDLDFDLSSD SESSESSSRS EGQRAPAPQE
     RTKAAPEHSG PQDTSGGRAA ASPLGESGPS IHPHDKGSDL DTQEEGERDS LCGLGNGSVD
     RKEAETESQN SEQSGVTAGE SLDQSVGEEE EEDTDDDDHL IHLEEILVRV HTDYYTKYDR
     YLNKELEEAP DIRKIVPELK SKVLADVAVI FSGLHPTNFP VEKTREHYHA TALGAKVLTQ
     LVLSPDAPDR ATHLIAARAG TEKVRQAQEC KHLHVVSPDW LWSCLERWDK VEEQLFPLID
     DDTRTHRDNS PAVFPDRHSV LPTALFHPTP IHSKAHPGPE VRIYDSNTGK LIRMGPQGSA
     PAPSSAPLNH GEPSSFRAVQ PHQQQMFGEE LPESQDGEQP GPARRKRQPS MSEAMPLYTL
     CKEDLESMDK EVDDILGEGS DDSDIEKKKP EDQDNEQERA PKPRKPRAPG IRREQPVGLP
     SSGERSTPGM RGPRGHKRKL NEEDAASESS GESSNDDEEG SSSEADEMAA ALEAELNDLM
//
ID   KPBB_MOUSE              Reviewed;        1085 AA.
AC   Q7TSH2;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Phosphorylase b kinase regulatory subunit beta;
DE            Short=Phosphorylase kinase subunit beta;
GN   Name=Phkb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-693, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of
CC       serine in certain substrates, including troponin I. The beta chain
CC       acts as a regulatory unit and modulates the activity of the
CC       holoenzyme in response to phosphorylation (By similarity).
CC   -!- ENZYME REGULATION: By phosphorylation of various serine residues
CC       (By similarity).
CC   -!- PATHWAY: Glycan biosynthesis; glycogen metabolism.
CC   -!- SUBUNIT: Polymer of 16 chains, four each of alpha, beta, gamma,
CC       and delta. Alpha and beta are regulatory chains, gamma is the
CC       catalytic chain, and delta is calmodulin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- PTM: Although the final Cys may be farnesylated, the terminal
CC       tripeptide is probably not removed, and the C-terminus is not
CC       methylated (By similarity).
CC   -!- SIMILARITY: Belongs to the phosphorylase b kinase regulatory chain
CC       family.
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DR   EMBL; BC053105; AAH53105.1; -; mRNA.
DR   IPI; IPI00380735; -.
DR   RefSeq; NP_955517.1; NM_199446.1.
DR   UniGene; Mm.237296; -.
DR   ProteinModelPortal; Q7TSH2; -.
DR   STRING; Q7TSH2; -.
DR   PhosphoSite; Q7TSH2; -.
DR   PRIDE; Q7TSH2; -.
DR   Ensembl; ENSMUST00000053771; ENSMUSP00000050788; ENSMUSG00000036879.
DR   GeneID; 102093; -.
DR   KEGG; mmu:102093; -.
DR   UCSC; uc009mqj.1; mouse.
DR   CTD; 102093; -.
DR   MGI; MGI:97578; Phkb.
DR   GeneTree; ENSGT00520000055553; -.
DR   HOGENOM; HBG383495; -.
DR   HOVERGEN; HBG097309; -.
DR   InParanoid; Q7TSH2; -.
DR   OMA; QRNVSMR; -.
DR   OrthoDB; EOG44BB1G; -.
DR   PhylomeDB; Q7TSH2; -.
DR   NextBio; 355270; -.
DR   ArrayExpress; Q7TSH2; -.
DR   Bgee; Q7TSH2; -.
DR   CleanEx; MM_PHKB; -.
DR   Genevestigator; Q7TSH2; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA:InterPro.
DR   GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR008928; 6-hairpin_glycosidase-like.
DR   InterPro; IPR011613; Glyco_hydro_15-rel.
DR   InterPro; IPR008734; PHK_AB.
DR   PANTHER; PTHR10749; PHK_AB; 1.
DR   Pfam; PF00723; Glyco_hydro_15; 1.
DR   SUPFAM; SSF48208; Glyco_trans_6hp; 1.
PE   1: Evidence at protein level;
KW   Calmodulin-binding; Carbohydrate metabolism; Cell membrane;
KW   Glycogen metabolism; Lipoprotein; Membrane; Phosphoprotein;
KW   Prenylation.
FT   CHAIN         1   1085       Phosphorylase b kinase regulatory subunit
FT                                beta.
FT                                /FTId=PRO_0000057737.
FT   REGION      760    787       Calmodulin-binding (Potential).
FT   REGION      912    943       Calmodulin-binding (Potential).
FT   MOD_RES      17     17       Phosphoserine (By similarity).
FT   MOD_RES      19     19       Phosphoserine.
FT   MOD_RES      21     21       Phosphotyrosine (By similarity).
FT   MOD_RES     692    692       Phosphoserine (By similarity).
FT   MOD_RES     693    693       Phosphoserine.
FT   LIPID      1082   1082       S-farnesyl cysteine (By similarity).
SQ   SEQUENCE   1085 AA;  123889 MW;  8EC52645AD89FDF5 CRC64;
     MANSPDAAFS SPALLRSGSV YEPLKSINLP RPDNETLWDK LDHYYRIVKS TMLMYQSPTT
     GLFPTKTCGG EEKSKVHESL YCAAGAWALA LAYRRIDDDK GRTHELEHSA IKCMRGILYC
     YMRQADKVQQ FKQDPRPTTC LHSVFSVHTG DELLSYEEYG HLQINAVSLF LLYLVEMISS
     GLQIIYNTDE VSFIQNLVFC VERVYRVPDF GVWERGSKYN NGSTELHSSS VGLAKAALEA
     INGFNLFGNQ GCSWSVIFVD LDAHNRNRQT LCSLLPRESR SHNTDAALLP CISYPAFALD
     DEALFSQTLD KVIRKLKGKY GFKRFLRDGY RTPLEDPNRR YYKPAEIKLF DGIECEFPIF
     FLYMMIDGVF RGNLEQVKEY QDLLTPLLHQ TTEGYPVVPK YYYVPADFVE CEKRNPGSQK
     RFPSNCGRDG KLFLWGQALY IIAKLLADEL ISPKDIDPVQ RFVPLQNQRN VSMRYSNQGP
     LENDLVVHVA LVAESQRLQV FLNTYGIQTQ TPQQVEPIQI WPQQELVKAY FHLGINEKLG
     LSGRPDRPIG CLGTSKIYRI LGKTVVCYPI IFDLSDFYMS QDVLLLIDDI KNALQFIKQY
     WKMHGRPLFL VLIREDNIRG SRFNPILDML AAFKKGIIGG VKVHVDRLQT LISGAVVEQL
     DFLRISDTEK LPEFKSFEEL EFPKHSKVKR QSSTADAPEA QHEPGITITE WKNKSTHEIL
     QKLNDCGCLA GQTILLGILL KREGPNFITM EGTVSDHIER VYRRAGSKKL WSVVRRAASL
     LNKVVDSLAP SITNVLVQGK QVTLGAFGHE EEVISNPLSP RVIKNIIYYK CNTHDEREAV
     IQQELVIHIG WIISNSPELF SGMLKIRIGW IIHAMEYELQ VRGGDKPAVD LYQLSPSEVK
     QLLLDILQPQ QSGRCWLNRR QIDGSLNRTP PEFYDRVWQI LERTPNGIVV AGKHLPQQPT
     LSDMTMYEMN FSLLVEDMLG NIDQPKYRQI IVELLMVVSI VLERNPELEF QDKVDLDRLV
     KEAFHEFQKD ESRLKEIEKQ DDMTSFYNTP PLGKRGTCSY LTKVVMNSLL EGEVKPSNED
     SCLVS
//
ID   CP110_MOUSE             Reviewed;        1004 AA.
AC   Q7TSH4; Q6A072;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Centrosomal protein CP110;
DE   AltName: Full=Centrosomal protein of 110 kDa;
DE            Short=Cep110;
GN   Name=Cep110; Synonyms=Cp110, Kiaa0419;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 165-959.
RC   TISSUE=Embryonic intestine;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
CC   -!- FUNCTION: Necessary for centrosome duplication at different stages
CC       of procentriole formation. Collaborates with CEP97, being involved
CC       in the suppression of a cilia assembly program. Required for
CC       correct spindle formation and has a role in regulating cytokinesis
CC       and genome stability via cooperation with CALM1 and CETN2 (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with CALM1, CETN2, CEP76 and CEP97. Interacts
CC       with CCNF (By similarity).
CC   -!- INTERACTION:
CC       Q9CZA6:Nde1; NbExp=2; IntAct=EBI-646843, EBI-309934;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome,
CC       centriole (By similarity). Note=Recruited early and then
CC       associates with the growing distal tips (By similarity).
CC   -!- PTM: Phosphorylated by CDKs (By similarity).
CC   -!- PTM: Ubiquitinated by the SCF(Cyclin F) during G2 phase, leading
CC       to its degradation by the proteasome and preventing centrosome
CC       reduplication (By similarity).
CC   -----------------------------------------------------------------------
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DR   EMBL; BC053103; AAH53103.1; -; mRNA.
DR   EMBL; AK172946; BAD32224.1; -; mRNA.
DR   IPI; IPI00337872; -.
DR   RefSeq; NP_892040.1; NM_182995.1.
DR   UniGene; Mm.23279; -.
DR   ProteinModelPortal; Q7TSH4; -.
DR   IntAct; Q7TSH4; 7.
DR   STRING; Q7TSH4; -.
DR   PhosphoSite; Q7TSH4; -.
DR   PRIDE; Q7TSH4; -.
DR   Ensembl; ENSMUST00000038650; ENSMUSP00000038881; ENSMUSG00000033904.
DR   Ensembl; ENSMUST00000106557; ENSMUSP00000102167; ENSMUSG00000033904.
DR   GeneID; 101565; -.
DR   KEGG; mmu:101565; -.
DR   UCSC; uc009jkj.1; mouse.
DR   MGI; MGI:2141942; 6330503K22Rik.
DR   HOGENOM; HBG278100; -.
DR   HOVERGEN; HBG050873; -.
DR   InParanoid; Q7TSH4; -.
DR   OMA; KDTMEFI; -.
DR   OrthoDB; EOG40ZQX3; -.
DR   PhylomeDB; Q7TSH4; -.
DR   NextBio; 355018; -.
DR   ArrayExpress; Q7TSH4; -.
DR   Bgee; Q7TSH4; -.
DR   CleanEx; MM_6330503K22RIK; -.
DR   CleanEx; MM_CEP110; -.
DR   Genevestigator; Q7TSH4; -.
DR   GermOnline; ENSMUSG00000033904; Mus musculus.
DR   GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein; Ubl conjugation.
FT   CHAIN         1   1004       Centrosomal protein CP110.
FT                                /FTId=PRO_0000089461.
FT   REGION        1    221       CEP97 binding (By similarity).
FT   REGION       64     82       Calmodulin-binding (By similarity).
FT   REGION      349    564       Interaction with CEP76 (By similarity).
FT   REGION      773    813       Calmodulin-binding (By similarity).
FT   REGION      901    916       Calmodulin-binding (By similarity).
FT   COILED       51     90       Potential.
FT   COILED      641    699       Potential.
FT   MOD_RES     364    364       Phosphoserine (By similarity).
FT   MOD_RES     368    368       Phosphoserine (By similarity).
FT   MOD_RES     370    370       Phosphoserine (By similarity).
SQ   SEQUENCE   1004 AA;  111139 MW;  C8D81F5F2FE213A8 CRC64;
     MEEYEEFCEK ALGRAQEASL STGSFLPAQA ESVSLIRFHG VAVLSPLLTI EKRKKIQEEK
     QKALDVQSRK QANRKKALLT RVQEILENVQ VRKAPNASDF DQWATETIYS NPEVTDLNVP
     VRVPNSLPSP TEHCTSVKLE KITGLLPVNN EDQQTPKRVG LPGDSEVSGS LRQCESPESR
     QAEDGAALRL SSASPQETII SDVLGKEEQD PSCLAEVTPD PYIMSLQNLM KRSKEYVERE
     LSSRSLRNSL KRSVNETHSD RENDAAKASD CVKEKAPPMP IGRHCGSAIP DKPSLNKSNV
     LLQGASQASS MGTAGLASFS KIDLPAGAAP PAAPDAGSDF TVIPTFVTEN KVKSLKGPYA
     KLPSPEPSMS PTMHRRHSRS ASACQILINN PVNACELSPK GKEEAVDRTA PAAAETTNES
     ETVPKSPTDL TGVCSSNVSA TKITSESTRE MVVGKPSQRQ QALGAHLGNN VTVERSAMEG
     PFIADDRGAQ KVDGTCMAVP KLHELQPSSQ CVSSQTLEDV CELKSASLLA KNSCNLQMEL
     NKSYDVKHPS PLLTQTQTSR QQMDTPPVFR GNEQFVDNSF EKVKRRLDLD VDSLQKENCP
     YIITAGVAEQ ERDRLLERRY PKGFVHINKN KMLETSPKEG QELLKSKMLA FEEMRKRLEE
     QHAQQLSLLI AEQEREQEQL QKEIEEQEKM LKEKAVTTDV SDLNSALEWR QRTDSALLET
     MLSQVDSLQT SNNSGFITSA LQYSFGSAGE APFYLWGSLT SGVTRVSGTR PCGRAQAKWS
     QVFNPEIHAK FNKITAVAKG FLTRKLMQTD KLKQLRQTVK DTMEFIRSFQ SEAPLKRGVV
     SAQDASLQER VLAQLRAALY GIHDIFFVMD AAERMSILHH DREARKEKLL RQMDKMKSPR
     VALSVATQKS LDRKKFMKVA EMGMPNKKFL LKQNPSETRV LQPNQGQNAP VHRLLSRQGT
     PKTSVKGVVQ NRQKPSQSRV PNRAPVSGAY AGKTQRKRPN VATI
//
ID   KCNF1_MOUSE             Reviewed;         493 AA.
AC   Q7TSH7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Potassium voltage-gated channel subfamily F member 1;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv5.1;
GN   Name=Kcnf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Putative voltage-gated potassium channel (By
CC       similarity).
CC   -!- SUBUNIT: Heteromultimer with KCNG3, KCNG4 and KCNV2. Interacts
CC       with DLG1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position (By similarity).
CC   -!- SIMILARITY: Belongs to the potassium channel family. F
CC       (TC 1.A.1.2) subfamily. Kv5.1/KCNF1 sub-subfamily.
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DR   EMBL; AK137367; BAE23327.1; -; mRNA.
DR   EMBL; BC053089; AAH53089.1; -; mRNA.
DR   IPI; IPI00400257; -.
DR   RefSeq; NP_963289.2; NM_201531.3.
DR   UniGene; Mm.40173; -.
DR   HSSP; P63142; 2A79.
DR   ProteinModelPortal; Q7TSH7; -.
DR   SMR; Q7TSH7; 20-416.
DR   PhosphoSite; Q7TSH7; -.
DR   PRIDE; Q7TSH7; -.
DR   Ensembl; ENSMUST00000057678; ENSMUSP00000061409; ENSMUSG00000051726.
DR   GeneID; 382571; -.
DR   KEGG; mmu:382571; -.
DR   NMPDR; fig|10090.3.peg.25983; -.
DR   UCSC; uc007ncn.1; mouse.
DR   CTD; 382571; -.
DR   MGI; MGI:2687399; Kcnf1.
DR   eggNOG; maNOG07328; -.
DR   GeneTree; ENSGT00560000076807; -.
DR   HOGENOM; HBG445693; -.
DR   HOVERGEN; HBG052230; -.
DR   InParanoid; Q7TSH7; -.
DR   OMA; FKNEMEF; -.
DR   OrthoDB; EOG4W3SNB; -.
DR   PhylomeDB; Q7TSH7; -.
DR   NextBio; 403395; -.
DR   ArrayExpress; Q7TSH7; -.
DR   Bgee; Q7TSH7; -.
DR   Genevestigator; Q7TSH7; -.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003971; K_chnl_volt-dep_Kv9.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01494; KV9CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
PE   2: Evidence at transcript level;
KW   Ion transport; Ionic channel; Membrane; Potassium; Potassium channel;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN         1    493       Potassium voltage-gated channel subfamily
FT                                F member 1.
FT                                /FTId=PRO_0000320105.
FT   TOPO_DOM      1    183       Cytoplasmic (Potential).
FT   TRANSMEM    184    204       Helical; Name=Segment S1; (Potential).
FT   TRANSMEM    224    244       Helical; Name=Segment S2; (Potential).
FT   TOPO_DOM    245    249       Cytoplasmic (Potential).
FT   TRANSMEM    250    270       Helical; Name=Segment S3; (Potential).
FT   TRANSMEM    290    310       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TOPO_DOM    311    324       Cytoplasmic (Potential).
FT   TRANSMEM    325    345       Helical; Name=Segment S5; (Potential).
FT   INTRAMEM    358    378       Pore-forming; Name=Segment H5;
FT                                (Potential).
FT   TRANSMEM    386    406       Helical; Name=Segment S6; (Potential).
FT   TOPO_DOM    407    493       Cytoplasmic (Potential).
FT   MOTIF       370    375       Selectivity filter (By similarity).
SQ   SEQUENCE   493 AA;  55647 MW;  F5C55969DF79FAD3 CRC64;
     MDASAEQSLP EPGSQDSVAG EDIEIVVNVG GVRQVLYGDL LSQYPETRLA ELINCLAGGY
     DTIFSLCDDY DPGKREFYFD RDPDAFKCVI EVYYFGEVHM KKGICPICFK NEMDFWKVDL
     KFLDDCCKSH LSEKREELEE IARRVQLILD DLGVDAAEGR WRRCQKCVWK FLEKPESSCP
     ARVVAVLSFL LILVSSVVMC MGTIPELQVV DSEGNRVEHP TLENVETACI GWFTLEYLLR
     LFSSPNKLHF ALSFMNIVDV LAILPFYVSL TLTHLGARMM ELTNVQQAVQ ALRIMRIARI
     FKLARHSSGL QTLTYALKRS FKELGLLLMY LAVGIFVFSA LGYTMEQSHP ETLFKSIPQS
     FWWAIITMTT VGYGDIYPKT TLGKLNAAIS FLCGVIAIAL PIHPIINNFV RYYNKQRVLE
     TAAKHELELM ELNSSSAEGK PGGSRSDLDT LPPEPAAREG PSWGSRLKLS HSDTFIPLLT
     EEKHHRTRLQ SCK
//
ID   K0195_MOUSE             Reviewed;        1360 AA.
AC   Q7TSH8; B1AT99; Q80U66; Q8BL05; Q8K0Q0; Q91VY1;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Uncharacterized protein KIAA0195;
GN   Name=Kiaa0195;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, Colon, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 548-1360.
RC   STRAIN=C57BL/6J; TISSUE=Corpus striatum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221 AND SER-225, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65499.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK122217; BAC65499.1; ALT_INIT; mRNA.
DR   EMBL; AL645852; CAM21974.1; -; Genomic_DNA.
DR   EMBL; BC007157; AAH07157.1; -; mRNA.
DR   EMBL; BC030865; AAH30865.1; -; mRNA.
DR   EMBL; BC053088; AAH53088.1; -; mRNA.
DR   EMBL; AK047622; BAC33103.1; -; mRNA.
DR   IPI; IPI00380739; -.
DR   RefSeq; NP_082290.2; NM_028014.3.
DR   UniGene; Mm.23168; -.
DR   ProteinModelPortal; Q7TSH8; -.
DR   SMR; Q7TSH8; 166-206, 842-875.
DR   PhosphoSite; Q7TSH8; -.
DR   PRIDE; Q7TSH8; -.
DR   Ensembl; ENSMUST00000093912; ENSMUSP00000091440; ENSMUSG00000020747.
DR   Ensembl; ENSMUST00000103033; ENSMUSP00000099322; ENSMUSG00000020747.
DR   GeneID; 71947; -.
DR   KEGG; mmu:71947; -.
DR   UCSC; uc007mil.1; mouse.
DR   MGI; MGI:1919197; 2310067B10Rik.
DR   GeneTree; ENSGT00390000016550; -.
DR   HOGENOM; HBG402855; -.
DR   HOVERGEN; HBG052173; -.
DR   InParanoid; Q7TSH8; -.
DR   OMA; KFSEDTL; -.
DR   OrthoDB; EOG49KFPR; -.
DR   NextBio; 335020; -.
DR   ArrayExpress; Q7TSH8; -.
DR   Bgee; Q7TSH8; -.
DR   CleanEx; MM_2310067B10RIK; -.
DR   Genevestigator; Q7TSH8; -.
DR   GermOnline; ENSMUSG00000020747; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015662; F:ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism; IEA:InterPro.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006812; P:cation transport; IEA:InterPro.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom.
DR   Gene3D; G3DSA:1.20.1110.10; ATPase_P-typ_TM_dom; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   1360       Uncharacterized protein KIAA0195.
FT                                /FTId=PRO_0000050732.
FT   TRANSMEM     65     85       Helical; (Potential).
FT   TRANSMEM     94    114       Helical; (Potential).
FT   TRANSMEM    274    294       Helical; (Potential).
FT   TRANSMEM    321    341       Helical; (Potential).
FT   TRANSMEM   1097   1117       Helical; (Potential).
FT   TRANSMEM   1125   1145       Helical; (Potential).
FT   TRANSMEM   1173   1193       Helical; (Potential).
FT   TRANSMEM   1233   1253       Helical; (Potential).
FT   TRANSMEM   1270   1290       Helical; (Potential).
FT   TRANSMEM   1311   1331       Helical; (Potential).
FT   MOD_RES     221    221       Phosphoserine.
FT   MOD_RES     225    225       Phosphoserine.
FT   MOD_RES     367    367       Phosphoserine (By similarity).
FT   MOD_RES     368    368       Phosphoserine (By similarity).
FT   MOD_RES     444    444       Phosphoserine (By similarity).
FT   MOD_RES     445    445       Phosphoserine.
FT   MOD_RES     517    517       Phosphoserine (By similarity).
FT   MOD_RES     644    644       Phosphothreonine (By similarity).
FT   MOD_RES     672    672       Phosphoserine (By similarity).
FT   MOD_RES     802    802       Phosphoserine (By similarity).
FT   MOD_RES     804    804       Phosphoserine (By similarity).
FT   MOD_RES     805    805       Phosphoserine (By similarity).
FT   MOD_RES     945    945       Phosphoserine (By similarity).
FT   CARBOHYD    479    479       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    520    520       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    599    599       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    759    759       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1206   1206       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1209   1209       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   1360 AA;  151796 MW;  E526BD5111D0F73C CRC64;
     MDLREKHLGE PPLALGLSTR KALSVLKEQL EAVLEKHLKE RKKSLTWKEA WRSSFLHLSN
     RCSCFHWPGA SLMLLAVLLL LCCCGGQPAG SQGVELVNAS ALFLLLLLNL VLIGRQDRLK
     RREVERRLRG IIDQIQDALR DGKEIKWPNS MYPDLHMPFA PSWSLHWAYR DGHLVNLPVS
     LLVEGDIIAL RPGQESFASL RGIKDDEHIV LEPGDLFPPF SPPPSPRGEV KRGPQNPQQH
     RLFRVLETPV IDNIRWCLDT ALSRPVTALD NERFTVQSVM LHYAVPVVLA GFLITNALRF
     MFKAPGVTSW QYTLLQLQVN GMLPILPLLF PVLWVLATAC GEARVLAQMS KASPSSLLAK
     FSEDTLSSYT EAVSSQEMLR CIWGHFLRVI QGTSPTLSHS ASLLHSLGSV TVLCCVDKQG
     ILSWPNPSPE TVLFFSGKVE PPHSSHEDLT DDLSTRSFCH PEVEEEPHEH DALLAGSLNN
     TLHLSNEQER SDWLADGPKP SEPYPHHKGH GRSKHPSGSN VSFSRDTEGG EEEPSKAQPG
     TEGDPYEAED FVCDYHLEML SLSQDQQNPS CIQFDDSNWQ SHLTSLKPLG LNVLLNLCNA
     SVTERLCRFS DHLCNIALQE SHSAVLPVHV PWGLCELARL IGFTPGAKEL FKQENHLALY
     RLPSAETLKE TSLGRPSCVT KRRPPLSHMI SLFIKDTATS TEQMLSHGSA DVVVEACTDF
     WDGADIYPLS GSDRKKVLDF YQRACLSGYC SAFAYKPMNC TLSSQLNGKC IELVQVPGQN
     SIFTMCELPS TIPIKPNNRR SSWSSDEGIG EVLEKEDCMQ ALSGQIFMGM VSSQYQARLD
     IVRLIDGLVN ACIRFVYFSL EDELRSKVFA EKMGLETGWN CHISLTPNGD MPGSEIPPSS
     PSHAGSLHDD LNQVSRDDAE GLLLLEEEGH SDLISFQPTD SDIPSFLEDC NRAKLPRGIH
     QVRPHLQNID NVPLLVPLFT DCTPDTMCEM IKIMQEYGEV TCCLGSSANL RNSCLFLQSD
     VSIALDPLYP SRCSWETFGY ATSTTMAQAS DGLSPLQLSG QLNSLPCSLT FRQEESISII
     RLIEQARHAT YGIRKCFLFL LQCQLTLVVI QFLSCLVQLP PLLSTTDILW LSCFCYPLLS
     ISLLGKPPHS SIMSMATGKN LQSIPKKTQH YFLLCFLLKF SLTISSCLVC FGFTLQSFCD
     SARARNLTNC SSVMLCSNDD RAPAWFEDFA NGLLSAQKLT AALIVLHTVF ISITHVHRTK
     PLWRKSPLTN LWWAVTVPVV LLGQVVQTVV DLQLWTHRDS RVHFGLEDVP LLTWLLGCLS
     LVLVVVTNEI VKLHEIRVRV RYQKRQKLQF ETKLGMNSPF
//
ID   PP6R1_MOUSE             Reviewed;         856 AA.
AC   Q7TSI3; Q80TJ4;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Serine/threonine-protein phosphatase 6 regulatory subunit 1;
DE   AltName: Full=SAPS domain family member 1;
GN   Name=Ppp6r1; Synonyms=Kiaa1115, Pp6r1, Saps1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=16769727; DOI=10.1074/jbc.M601772200;
RA   Stefansson B., Brautigan D.L.;
RT   "Protein phosphatase 6 subunit with conserved Sit4-associated protein
RT   domain targets IkappaBepsilon.";
RL   J. Biol. Chem. 281:22624-22634(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529; SER-530; SER-531
RP   AND SER-826, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Regulatory subunit of protein phospatase 6 (PP6). May
CC       function as a scaffolding PP6 subunit. Involved in the PP6-
CC       mediated dephosphorylation of NFKBIE opposing its degradation in
CC       response to TNF-alpha (By similarity).
CC   -!- SUBUNIT: Protein phospatase 6 (PP6) holoenzyme is proposed to be a
CC       heterotrimeric complex formed of the catalytic subunit, a SAPS
CC       domain-containing subunit (PP6R) and an ankyrin repeat-domain
CC       containing regulatory subunit (ARS). Interacts with PPP6C and
CC       NFKBIE. Interacts with ANKRD28, ANKRD44 and ANKRD52 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitous with highest expression in lung,
CC       spleen and bladder.
CC   -!- SIMILARITY: Belongs to the SAPS family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65732.3; Type=Miscellaneous discrepancy; Note=Derived from pre-RNA;
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DR   EMBL; AK122450; BAC65732.3; ALT_SEQ; Transcribed_RNA.
DR   EMBL; BC053076; AAH53076.1; -; mRNA.
DR   IPI; IPI00380742; -.
DR   RefSeq; NP_766482.2; NM_172894.2.
DR   UniGene; Mm.258670; -.
DR   ProteinModelPortal; Q7TSI3; -.
DR   STRING; Q7TSI3; -.
DR   PhosphoSite; Q7TSI3; -.
DR   PRIDE; Q7TSI3; -.
DR   Ensembl; ENSMUST00000064099; ENSMUSP00000066736; ENSMUSG00000052296.
DR   GeneID; 243819; -.
DR   KEGG; mmu:243819; -.
DR   UCSC; uc009eyb.1; mouse.
DR   CTD; 243819; -.
DR   MGI; MGI:2442163; Ppp6r1.
DR   eggNOG; roNOG12831; -.
DR   HOGENOM; HBG505370; -.
DR   HOVERGEN; HBG069733; -.
DR   InParanoid; Q7TSI3; -.
DR   OMA; GAWQGSQ; -.
DR   OrthoDB; EOG4P2Q1M; -.
DR   PhylomeDB; Q7TSI3; -.
DR   NextBio; 385934; -.
DR   ArrayExpress; Q7TSI3; -.
DR   Bgee; Q7TSI3; -.
DR   CleanEx; MM_SAPS1; -.
DR   Genevestigator; Q7TSI3; -.
DR   GermOnline; ENSMUSG00000052296; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR007587; SAPS.
DR   PANTHER; PTHR12634; SAPS; 1.
DR   Pfam; PF04499; SAPS; 2.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein.
FT   CHAIN         1    856       Serine/threonine-protein phosphatase 6
FT                                regulatory subunit 1.
FT                                /FTId=PRO_0000046097.
FT   REGION       10    403       Interaction with PPP6C (By similarity).
FT   COMPBIAS    623    629       Poly-Glu.
FT   MOD_RES     529    529       Phosphoserine.
FT   MOD_RES     530    530       Phosphoserine.
FT   MOD_RES     531    531       Phosphoserine.
FT   MOD_RES     633    633       Phosphoserine (By similarity).
FT   MOD_RES     636    636       Phosphoserine (By similarity).
FT   MOD_RES     662    662       Phosphoserine (By similarity).
FT   MOD_RES     665    665       Phosphoserine (By similarity).
FT   MOD_RES     666    666       Phosphothreonine (By similarity).
FT   MOD_RES     668    668       Phosphoserine (By similarity).
FT   MOD_RES     698    698       Phosphoserine (By similarity).
FT   MOD_RES     739    739       Phosphoserine (By similarity).
FT   MOD_RES     826    826       Phosphoserine.
FT   CONFLICT    309    309       D -> N (in Ref. 1; BAC65732).
FT   CONFLICT    683    685       AEQ -> G (in Ref. 1; BAC65732).
SQ   SEQUENCE   856 AA;  94527 MW;  CC6D541FDBBDBC1A CRC64;
     MFWKFDLHTS SHLDTLLEKE DLSLPELLDE EDVLQECKVV NRKLLDFLLQ PSHLQAMVAW
     VTQEPPASGE ERLRYKYPSV ACEILTSDVP QINDALGADE SLLNRLYGFL QSGDSLNPLL
     ASFFSKVMGI LINRKTDQLV SFLRKKDDFV DLLLRHIGTS AIMDLLLRLL TCVERPQLRQ
     DVFNWLNEEK IVQRLIEQIH PSKDDNQHSN ASQSLCDIIR LSREQMIQGQ DSPEPDQLLA
     TLEKQETIEQ LLSNMFEGEQ CQSVIVSGIQ VLLTLLEPRR PRSDSVTMNN FFSSVDGQLE
     LLAQGALDDA LSSMGALHAL RPRLDRFHQL LLEPPKLEPL QMTWGSLAPP LGNTRLHVVK
     LLASALSANA AALTQELLVL DVPNTLLDLF FHYVFNNFLH AQVEVCVSAM LSSGPPPDSS
     SETPVPNPIV KHLLQHCRLV ERILASWEEN DRVQSGGGPR KGYMGHLTRV ANAVVQNAEQ
     GPNAEQLGQL LKELPEEQQQ RWEAFVSGPL AETNKKNTVD LVNTHHLHSS SDDEDDRLKE
     FNFPEEAVLQ QAFMDFQMQR MTSAFIDHFG FNDEEFGEQE ESVNAPFDKT ANITFSLNAD
     DENPNANLLE ICYKDRIQQF DDEEEEEEEG QGSAESDGEY GAWQGSQPVR ASQASQPPGV
     RSGGSTDSEE EDEEEDEEED EGAEQAACGR TSPSSFPSPS TQPPGPSWTA TFDTVPMDAP
     TGPPVSKEAD MSSIQIPSSP PAHGSPQLRS QDPTHPSAPQ EVTDSSKVAE PLAPCQALVS
     VADVQATLHG MRSAPSSLDS ATRDPSTSVP DFKAHQSPQT MEGKRSPEHL GLPQSQSALE
     MPNGSTPGGP ISSGSQ
//
ID   MAP6_MOUSE              Reviewed;         906 AA.
AC   Q7TSJ2; O55129; O70586; O70587; Q78DV4; Q78DV5;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=Microtubule-associated protein 6;
DE            Short=MAP-6;
DE   AltName: Full=Stable tubule-only polypeptide;
DE            Short=STOP;
GN   Name=Map6; Synonyms=Mtap6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS
RP   1 AND 2).
RC   STRAIN=129/SvJ; TISSUE=Liver;
RX   MEDLINE=98162614; PubMed=9501006; DOI=10.1006/bbrc.1998.8179;
RA   Denarier E., Aguezzoul M., Jolly C., Vourc'h C., Roure A.,
RA   Andrieux A., Bosc C., Job D.;
RT   "Genomic structure and chromosomal mapping of the mouse STOP gene
RT   (Mtap6).";
RL   Biochem. Biophys. Res. Commun. 243:791-796(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=Swiss Webster / NIH; TISSUE=Fibroblast;
RX   MEDLINE=98263307; PubMed=9600916; DOI=10.1073/pnas.95.11.6055;
RA   Denarier E., Fourest-Lieuvin A., Bosc C., Pirollet F., Chapel A.,
RA   Margolis R.L., Job D.;
RT   "Nonneuronal isoforms of STOP protein are responsible for microtubule
RT   cold stability in mammalian fibroblasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:6055-6060(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=12231625; DOI=10.1101/gad.223302;
RA   Andrieux A., Salin P.A., Vernet M., Kujala P., Baratier J.,
RA   Gory-Faure S., Bosc C., Pointu H., Proietto D., Schweitzer A.,
RA   Denarier E., Klumperman J., Job D.;
RT   "The suppression of brain cold-stable microtubules in mice induces
RT   synaptic defects associated with neuroleptic-sensitive behavioral
RT   disorders.";
RL   Genes Dev. 16:2350-2364(2002).
RN   [5]
RP   INTERACTION WITH CALMODULIN.
RX   PubMed=14516200; DOI=10.1021/bi034746w;
RA   Bouvier D., Vanhaverbeke C., Simorre J.P., Arlaud G.J., Bally I.,
RA   Forge V., Margolis R.L., Gans P., Kleman J.P.;
RT   "Unusual Ca(2+)-calmodulin binding interactions of the microtubule-
RT   associated protein F-STOP.";
RL   Biochemistry 42:11484-11493(2003).
RN   [6]
RP   ALTERNATIVE PROMOTER USAGE, DEVELOPMENTAL STAGE, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=12782132; DOI=10.1016/S0888-7543(03)00053-3;
RA   Aguezzoul M., Andrieux A., Denarier E.;
RT   "Overlap of promoter and coding sequences in the mouse STOP gene
RT   (Mtap6).";
RL   Genomics 81:623-627(2003).
RN   [7]
RP   ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX   PubMed=15389836; DOI=10.1002/jnr.20260;
RA   Galiano M.R., Bosc C., Schweitzer A., Andrieux A., Job D.,
RA   Hallak M.E.;
RT   "Astrocytes and oligodendrocytes express different STOP protein
RT   isoforms.";
RL   J. Neurosci. Res. 78:329-337(2004).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16837464; DOI=10.1074/jbc.M603380200;
RA   Gory-Faure S., Windscheid V., Bosc C., Peris L., Proietto D.,
RA   Franck R., Denarier E., Job D., Andrieux A.;
RT   "STOP-like protein 21 is a novel member of the STOP family, revealing
RT   a Golgi localization of STOP proteins.";
RL   J. Biol. Chem. 281:28387-28396(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; SER-632; SER-687;
RP   SER-832 AND SER-905, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-141, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Involved in microtubule stabilization in many cell
CC       types, including neuronal cells. Specifically has microtubule cold
CC       stabilizing activity.
CC   -!- SUBUNIT: Interacts with calmodulin (via C-terminus); the
CC       interaction is dependent on Ca(2+).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Golgi apparatus.
CC       Note=Isoform 1 and isoform 2 associate with axonal microtubules in
CC       neurons. Isoform 3 associates with microtubules in fibroblasts.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
CC         Comment=Comment: Additional isoforms seem to exist;
CC       Name=1; Synonyms=N-STOP, Neuronal STOP;
CC         IsoId=Q7TSJ2-1; Sequence=Displayed;
CC         Note=Produced by alternative promoter usage;
CC       Name=2; Synonyms=E-STOP, Early STOP;
CC         IsoId=Q7TSJ2-2; Sequence=VSP_034727;
CC         Note=Produced by alternative splicing of isoform 1;
CC       Name=3; Synonyms=F-STOP, Fibroblastic STOP;
CC         IsoId=Q7TSJ2-3; Sequence=VSP_034724, VSP_034725, VSP_034726;
CC         Note=Produced by alternative promoter usage;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is specifically expressed in adult
CC       brain. Isoform 2 is predominantly expressed in embryonic brain;
CC       expression persists at low levels in the adult brain. Isoform 3 is
CC       expressed at high levels in lung and at lower levels in testis,
CC       heart, muscle and kidney (at protein level). Oligodendrocytes
CC       express a major isoform of 89 kDa (O-STOP). Astrocytes also
CC       express an isoform of 60 kDa (A-STOP).
CC   -!- DEVELOPMENTAL STAGE: Isoform 2 is expressed in embryonic brain.
CC   -!- DISRUPTION PHENOTYPE: Mice are devoid of cold-stable microtubules
CC       and show no detectable defects in brain anatomy but show synaptic
CC       defects, with depleted synaptic vesicle pools and impaired
CC       synaptic plasticity, associated with severe behavioral disorders,
CC       including a disorganized activity with disruption of normal
CC       behavioral sequences and episodes of hyperlocomotion or apparent
CC       prostration, anxiety, severe social withdrawal and complete
CC       nurturing defects. The behavioral defects are alleviated by long-
CC       term treatment with neuroleptics.
CC   -!- SIMILARITY: Belongs to the STOP family.
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DR   EMBL; Y14754; CAA75049.1; -; Genomic_DNA.
DR   EMBL; Y14755; CAA75049.1; JOINED; Genomic_DNA.
DR   EMBL; Y14756; CAA75049.1; JOINED; Genomic_DNA.
DR   EMBL; Y16008; CAA75930.1; -; Genomic_DNA.
DR   EMBL; Y16032; CAA75989.1; -; mRNA.
DR   EMBL; BC053039; AAH53039.1; -; mRNA.
DR   IPI; IPI00115833; -.
DR   IPI; IPI00788315; -.
DR   IPI; IPI00788359; -.
DR   PIR; JC5963; JC5963.
DR   RefSeq; NP_001036820.2; NM_001043355.2.
DR   RefSeq; NP_001041632.1; NM_001048167.1.
DR   RefSeq; NP_034967.2; NM_010837.3.
DR   UniGene; Mm.154087; -.
DR   ProteinModelPortal; Q7TSJ2; -.
DR   STRING; Q7TSJ2; -.
DR   PhosphoSite; Q7TSJ2; -.
DR   PRIDE; Q7TSJ2; -.
DR   Ensembl; ENSMUST00000068973; ENSMUSP00000064787; ENSMUSG00000055407.
DR   Ensembl; ENSMUST00000107100; ENSMUSP00000102717; ENSMUSG00000055407.
DR   GeneID; 17760; -.
DR   KEGG; mmu:17760; -.
DR   UCSC; uc009ilg.1; mouse.
DR   CTD; 17760; -.
DR   MGI; MGI:1201690; Mtap6.
DR   eggNOG; roNOG05697; -.
DR   GeneTree; ENSGT00530000063947; -.
DR   HOGENOM; HBG126743; -.
DR   HOVERGEN; HBG053112; -.
DR   InParanoid; Q7TSJ2; -.
DR   OMA; KDQGSVV; -.
DR   OrthoDB; EOG4CC41W; -.
DR   PhylomeDB; Q7TSJ2; -.
DR   NextBio; 292441; -.
DR   ArrayExpress; Q7TSJ2; -.
DR   Bgee; Q7TSJ2; -.
DR   Genevestigator; Q7TSJ2; -.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR   InterPro; IPR007882; STOP.
DR   PANTHER; PTHR14759; STOP; 1.
DR   Pfam; PF05217; STOP; 2.
PE   1: Evidence at protein level;
KW   Alternative promoter usage; Alternative splicing; Calmodulin-binding;
KW   Cytoplasm; Cytoskeleton; Golgi apparatus; Lipoprotein; Microtubule;
KW   Palmitate; Phosphoprotein; Repeat.
FT   CHAIN         1    906       Microtubule-associated protein 6.
FT                                /FTId=PRO_0000344045.
FT   REPEAT      222    267       Mc-1.
FT   REPEAT      268    313       Mc-2.
FT   REPEAT      314    359       Mc-3.
FT   REPEAT      360    405       Mc-4.
FT   REGION        1     15       Calmodulin-binding (By similarity).
FT   REGION      116    139       Mn 1 (By similarity).
FT   REGION      124    138       Calmodulin-binding (By similarity).
FT   REGION      151    174       Mn 2 (By similarity).
FT   REGION      160    174       Calmodulin-binding (By similarity).
FT   REGION      187    201       Calmodulin-binding (By similarity).
FT   REGION      222    405       4 X approximate tandem repeat Mc.
FT   REGION      235    249       Calmodulin-binding (By similarity).
FT   REGION      280    294       Calmodulin-binding (By similarity).
FT   REGION      325    339       Calmodulin-binding (By similarity).
FT   REGION      375    389       Calmodulin-binding (By similarity).
FT   REGION      427    450       Mn 3 (By similarity).
FT   REGION      435    449       Calmodulin-binding (By similarity).
FT   REGION      486    500       Calmodulin-binding (By similarity).
FT   REGION      513    527       Calmodulin-binding (By similarity).
FT   MOD_RES     108    108       Phosphoserine.
FT   MOD_RES     141    141       Phosphotyrosine.
FT   MOD_RES     632    632       Phosphoserine.
FT   MOD_RES     687    687       Phosphoserine.
FT   MOD_RES     832    832       Phosphoserine.
FT   MOD_RES     905    905       Phosphoserine.
FT   LIPID         5      5       S-palmitoyl cysteine (By similarity).
FT   LIPID        10     10       S-palmitoyl cysteine (By similarity).
FT   LIPID        11     11       S-palmitoyl cysteine (By similarity).
FT   VAR_SEQ       1    203       Missing (in isoform 3).
FT                                /FTId=VSP_034724.
FT   VAR_SEQ     503    509       VEKPSVQ -> EPGQTHQ (in isoform 3).
FT                                /FTId=VSP_034725.
FT   VAR_SEQ     510    906       Missing (in isoform 3).
FT                                /FTId=VSP_034726.
FT   VAR_SEQ     569    906       Missing (in isoform 2).
FT                                /FTId=VSP_034727.
FT   CONFLICT     81     81       P -> L (in Ref. 1; CAA75049).
FT   CONFLICT     87     87       V -> G (in Ref. 1; CAA75930).
FT   CONFLICT    344    344       E -> K (in Ref. 1; CAA75930 and 2;
FT                                CAA75989).
FT   CONFLICT    405    405       G -> S (in Ref. 1; CAA75049).
FT   CONFLICT    755    757       MVP -> VVH (in Ref. 1; CAA75930).
FT   CONFLICT    755    755       M -> V (in Ref. 1; CAA75049).
FT   CONFLICT    825    825       P -> S (in Ref. 1; CAA75930).
SQ   SEQUENCE   906 AA;  96450 MW;  F3CED1FCF1E2CD83 CRC64;
     MAWPCITRAC CIARFWNQLD KADIAVPLVF TKYSEATEHP GAPPQPPAPL QPALAPPSRA
     VAIETQPAQG ESDAVARATG PAPGPSVDRE TVAAPGRSGL GLGAASASTS GSGPADSVMR
     QDYRAWKVQR PEPSCRPRSE YQPSDAPFER ETQYQKDFRA WPLPRRGDHP WIPKPVQIPA
     TSQPSQPVLG VPKRRPQSQE RGPMQLSADA RDPEGAGGAG VLAAGKASGV DQRDTRRKAG
     PAWMVTRNEG HEEKPLPPAQ SQTQEGGPAA GKASGADQRD TRRKAGPAWM VTRSEGHEEK
     PLPPAQSQTQ EGGPAAGKAS GADQRDTRRK AGPAWMVTRT EGHEETPLPP AQSQTQEGGP
     AAGKASGADE RDTRRKAGPA WMVRRSEGHE QTPAAHAQGT GPEGGKGRAV ADALNRQIRE
     EVASTVSSSY RNEFRAWTDI KPVKPIKAKP QYKPPDDKMV HETSYSAQFK GEANKPSAAD
     NKAMDRRRIR SLYSEPFKEC PKVEKPSVQS SKPKKTSTSH KPPRKAKDKQ VVSGQAAKKK
     TTEGPSATKP DDKEQSKEMN NKLAEAKESR VKPTSDASKN RGPVTKEPHK DQGSVAPGLP
     KGQEPLKDQG PVVPGLPKDQ VPVVPGSLKG QSPTAPGPTK DQGAVLLGPV KDLGPVAPAP
     IKVQDHIASE LLKNKDSVPL APAKAQSPLL PEPLKNQSPV VPASTKDQSF PTPAPRKDPG
     PVIPEPEKDR APTVPERRKD QHVSIMASLK NEAPMVPESV KNQGLAGPEL VKDTGTDTTA
     PRYLKGHDSV FVAPVKNQGP VIPEPVKSQD PIIPALAKDQ GPMLPEPPKN QSPVVLGPIK
     NQDPIIPVPL KGQDPLVPAP TKDQGPTAPD PLKTQGPKGT QLPTVSPSPP VMIPTVPHTE
     YIEGSP
//
ID   PCDH8_MOUSE             Reviewed;        1070 AA.
AC   Q7TSK3; Q05BD0; Q8C824; Q9JKP3;
DT   08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Protocadherin-8;
DE   AltName: Full=Arcadlin;
DE   AltName: Full=Paraxial protocadherin;
DE   Flags: Precursor;
GN   Name=Pcdh8; Synonyms=Papc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Yamamoto A., Kemp C.R., De Robertis E.M.;
RT   "Mouse PAPC.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6; TISSUE=Embryonic brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION.
RX   PubMed=17988630; DOI=10.1016/j.neuron.2007.08.020;
RA   Yasuda S., Tanaka H., Sugiura H., Okamura K., Sakaguchi T., Tran U.,
RA   Takemiya T., Mizoguchi A., Yagita Y., Sakurai T., De Robertis E.M.,
RA   Yamagata K.;
RT   "Activity-induced protocadherin arcadlin regulates dendritic spine
RT   number by triggering N-cadherin endocytosis via TAO2beta and p38 MAP
RT   kinases.";
RL   Neuron 56:456-471(2007).
CC   -!- FUNCTION: Calcium-dependent cell-adhesion protein (By similarity).
CC       May play a role in activity-induced synaptic reorganization
CC       underlying long term memory (By similarity). Could be involved in
CC       CDH2 internalization through TAOK2/p38 MAPK pathway (By
CC       similarity). In hippocampal neurons, may play a role in the down-
CC       regulation of dendritic spines, maybe through its action on CDH2
CC       endocytosis.
CC   -!- SUBUNIT: The N-terminal extracellular domain forms homophilic
CC       interactions; these interactions activate p38 MAPK via TAOK2 and
CC       trigger endocytosis (By similarity). Interacts with CDH2; this
CC       interaction may lead to CDH2 cointernalization (By similarity).
CC       Interacts with CDH11 (By similarity). Interacts with TAOK2 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein (By similarity). Cell projection, dendrite (By
CC       similarity). Cell junction, synapse, presynaptic cell membrane.
CC       Cell junction, synapse, postsynaptic cell membrane (By
CC       similarity). Note=Expressed in neuronal cell bodies and dendrites
CC       (By similarity). Localized to excitatory, but not with inhibitory,
CC       synapses (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q7TSK3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7TSK3-2; Sequence=VSP_040562;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q7TSK3-3; Sequence=VSP_040563, VSP_040564;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 6 cadherin domains.
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DR   EMBL; AF231125; AAF63319.1; -; mRNA.
DR   EMBL; AK048638; BAC33404.1; -; mRNA.
DR   EMBL; CH466535; EDL35755.1; -; Genomic_DNA.
DR   EMBL; BC052388; AAH52388.1; -; mRNA.
DR   EMBL; BC053008; AAH53008.1; -; mRNA.
DR   IPI; IPI00123256; -.
DR   RefSeq; NP_067518.2; NM_021543.3.
DR   UniGene; Mm.390715; -.
DR   ProteinModelPortal; Q7TSK3; -.
DR   SMR; Q7TSK3; 24-139, 141-346, 401-601.
DR   STRING; Q7TSK3; -.
DR   PhosphoSite; Q7TSK3; -.
DR   Ensembl; ENSMUST00000039568; ENSMUSP00000045333; ENSMUSG00000036422.
DR   GeneID; 18530; -.
DR   KEGG; mmu:18530; -.
DR   UCSC; uc007uti.1; mouse.
DR   CTD; 18530; -.
DR   MGI; MGI:1306800; Pcdh8.
DR   HOVERGEN; HBG054878; -.
DR   InParanoid; Q7TSK3; -.
DR   OMA; QRLRGAH; -.
DR   PhylomeDB; Q7TSK3; -.
DR   NextBio; 294294; -.
DR   ArrayExpress; Q7TSK3; -.
DR   Bgee; Q7TSK3; -.
DR   Genevestigator; Q7TSK3; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:MGI.
DR   GO; GO:0001756; P:somitogenesis; IMP:MGI.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR013164; Cadherin_N.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 6.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF08266; Cadherin_2; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 6.
DR   SUPFAM; SSF49313; Cadherin; 6.
DR   PROSITE; PS00232; CADHERIN_1; 5.
DR   PROSITE; PS50268; CADHERIN_2; 6.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Calcium; Cell adhesion; Cell junction;
KW   Cell membrane; Cell projection; Glycoprotein; Membrane;
KW   Postsynaptic cell membrane; Repeat; Signal; Synapse; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     29       Potential.
FT   CHAIN        30   1070       Protocadherin-8.
FT                                /FTId=PRO_0000404296.
FT   TOPO_DOM     30    747       Extracellular (Potential).
FT   TRANSMEM    748    768       Helical; (Potential).
FT   TOPO_DOM    769   1070       Cytoplasmic (Potential).
FT   DOMAIN       30    135       Cadherin 1.
FT   DOMAIN      136    245       Cadherin 2.
FT   DOMAIN      247    354       Cadherin 3.
FT   DOMAIN      393    497       Cadherin 4.
FT   DOMAIN      498    609       Cadherin 5.
FT   DOMAIN      615    721       Cadherin 6.
FT   CARBOHYD    616    616       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     779    875       Missing (in isoform 2).
FT                                /FTId=VSP_040562.
FT   VAR_SEQ     876    966       PYGASPGFGKEPAAPPVAVWKGHSFNTISGREAEKFSGKDS
FT                                GKGDSDFNDSDSDISGDALKKDLINHMQSGLWACTAECKIL
FT                                GHSDRCWSP -> VRPSFGWAPPSVLCGQAGRRETGGVRVG
FT                                SHREMFNLSHLLFCVLSNPHTFPPPPFPAAALRCLSRLREG
FT                                ACCAPCYSLEGSFIQHHLGPRS (in isoform 3).
FT                                /FTId=VSP_040563.
FT   VAR_SEQ     967   1070       Missing (in isoform 3).
FT                                /FTId=VSP_040564.
FT   CONFLICT     58     58       S -> F (in Ref. 1; AAF63319).
FT   CONFLICT    160    160       V -> A (in Ref. 1; AAF63319).
FT   CONFLICT    222    222       R -> TG (in Ref. 1; AAF63319).
FT   CONFLICT    237    237       D -> G (in Ref. 2; BAC33404).
FT   CONFLICT    393    393       Q -> H (in Ref. 1; AAF63319).
FT   CONFLICT    403    403       E -> Q (in Ref. 1; AAF63319).
FT   CONFLICT    590    590       S -> P (in Ref. 4; AAH52388).
SQ   SEQUENCE   1070 AA;  113260 MW;  FFC2D87D63F6856E CRC64;
     MSPAKRWGSP CLFPLQLFSL CWVLSVAQSK TVRYSTFEED APGTVIGTLA EDLHMKVSGD
     TSFRLMKQFN SSLLRVREGD GQLTVGDAGL DRERLCGPSP QCVLAFDVVS FSQEQFRLVH
     VEVEVRDVND HAPRFPRAQI PVEVSESAPV GTRIPLEVPV DEDVGANGLQ SVRLAEPHSP
     FRVELQTRAD GAQCADLVLL QELDRESQAS YSLELVAQDG GRPPRSATAA LSVRVLDAND
     HSPAFPQGAV AEVELAEDAP VGSLLLDLDA ADPDEGPNGD VVFTFGARTP PEARHLFRLD
     PRSGRLTLAG QVDYERQDTY ELDVRAQDRG PGPRTATCKV IVRIRDVNDN APEISITPLA
     APGAPATSPF AAAAAAAALG GADAASSTGS GTQEAGITSL VPEGAARESL VALVSTSDRD
     SGANGQVRCA LYGHEHFRLQ PAYAGSYLVV TAASLDRERI AEYNLTLVAE DRGTPPLRTV
     RPYTVRVGDE NDNAPIFTKP VYEVSVRENN PPGAYLATVA ARDPDVGRNG QVTYRLVEAE
     VGRSGEAVST YVSVDPATGA IYALRSFDYE TLRQLDVRVQ ASDGGSPQLS SNALVQVRVL
     DQNDHSPILV HPAPANGSLE VAVPGRSTKD TAVARIQARD ADEGANGELA FDLLQQEPRE
     AFSIGRHTGE IMLTGDLSQE PPGRVFKALL VISDGGRPPL TTTATVSFVV TAGGGSAVPA
     SSGSPEHSRP PGSRLAPSGP SLQWDTPLIV IIVLAGSCTL LLAAIIAIAT TCNRRKKEVR
     KGGALREERP GAAGGGASAP GSPDETARGT GPRPNMFDVL TFPGSGKAPF GSPAADAPPP
     AVAAAEVPGS EGGSATGESA CHFEGQQRLR GAHAEPYGAS PGFGKEPAAP PVAVWKGHSF
     NTISGREAEK FSGKDSGKGD SDFNDSDSDI SGDALKKDLI NHMQSGLWAC TAECKILGHS
     DRCWSPSCAG PNVHPPPHPP AQMSTFCKST SLPRDPLRRD NYYQAQLPKT VGLQSVYEKV
     LHRDYDRTVT LLSPPRPGRL PDLQEIGVPL YESPPGSRYV SPKKGINENV
//
ID   PDPR_MOUSE              Reviewed;         878 AA.
AC   Q7TSQ8; Q6ZPF5;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Pyruvate dehydrogenase phosphatase regulatory subunit, mitochondrial;
DE            Short=PDPr;
DE   Flags: Precursor;
GN   Name=Pdpr; Synonyms=Kiaa1990;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RA   Jang J.S., Ackerman S.L.;
RT   "An alternatively spliced form of a gene encoding pyruvate
RT   dehydrogenase phosphatase regulatory subunit.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Decreases the sensitivity of PDP1 to magnesium ions, and
CC       this inhibition is reversed by the polyamine spermine (By
CC       similarity).
CC   -!- SUBUNIT: Heterodimer of a catalytic (PDP1) and a regulatory (PDPR)
CC       subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- SIMILARITY: Belongs to the gcvT family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98282.1; Type=Erroneous initiation;
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DR   EMBL; AY223867; AAP20649.1; -; mRNA.
DR   EMBL; AK129472; BAC98282.1; ALT_INIT; mRNA.
DR   EMBL; BC120745; AAI20746.1; -; mRNA.
DR   EMBL; BC125425; AAI25426.1; -; mRNA.
DR   IPI; IPI00453792; -.
DR   RefSeq; NP_938050.1; NM_198308.1.
DR   UniGene; Mm.28350; -.
DR   UniGene; Mm.370024; -.
DR   ProteinModelPortal; Q7TSQ8; -.
DR   SMR; Q7TSQ8; 38-422, 455-868.
DR   PRIDE; Q7TSQ8; -.
DR   Ensembl; ENSMUST00000039333; ENSMUSP00000046639; ENSMUSG00000033624.
DR   GeneID; 319518; -.
DR   KEGG; mmu:319518; -.
DR   NMPDR; fig|10090.3.peg.19262; -.
DR   UCSC; uc009nlw.1; mouse.
DR   CTD; 319518; -.
DR   MGI; MGI:2442188; 4930402E16Rik.
DR   eggNOG; roNOG10416; -.
DR   GeneTree; ENSGT00530000063120; -.
DR   HOGENOM; HBG322775; -.
DR   HOVERGEN; HBG103854; -.
DR   InParanoid; Q7TSQ8; -.
DR   OMA; NGVYKRF; -.
DR   OrthoDB; EOG4NZTSJ; -.
DR   PhylomeDB; Q7TSQ8; -.
DR   NextBio; 394896; -.
DR   ArrayExpress; Q7TSQ8; -.
DR   Bgee; Q7TSQ8; -.
DR   Genevestigator; Q7TSQ8; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004047; F:aminomethyltransferase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0006546; P:glycine catabolic process; IEA:InterPro.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   InterPro; IPR013977; GCV_T_C.
DR   InterPro; IPR006222; GCV_T_N.
DR   Pfam; PF01266; DAO; 1.
DR   Pfam; PF01571; GCV_T; 1.
DR   Pfam; PF08669; GCV_T_C; 1.
PE   2: Evidence at transcript level;
KW   Mitochondrion; Transit peptide.
FT   TRANSIT       1     93       Mitochondrion (Potential).
FT   CHAIN        94    878       Pyruvate dehydrogenase phosphatase
FT                                regulatory subunit, mitochondrial.
FT                                /FTId=PRO_0000328741.
FT   CONFLICT    438    438       P -> H (in Ref. 2; BAC98282).
SQ   SEQUENCE   878 AA;  99230 MW;  16A8C9ED77613525 CRC64;
     MLYRLLSIVQ RQRTSPGWQT WSSARSSTST AEAHSIALPA QAQVVICGGG IMGTSVAYHL
     SKMGWQDIVL LEQGRLAAGS TRFCAGILST ARHSSVEQKM ANYSNKLYHQ LEQETGIQTG
     YLRTGSISLA QTQDRLISLK RINSRLNVVG IPSEIISPKK VAELHPLLNV HDLVGAMYVP
     EDAVVSSADV ALALASAASQ NGVQIYDRTS VLHVLIKKGQ VTGVETDKGQ IECQYFVNCA
     GQWAYELGLS NEEPLSIPLH ACEHFYLLTR PWDTPLQSNT PTIVDADGRI YIRNWQGGIL
     SGGFEKNPKP IFTEGKNQLE IQNLREDWDH FEPLLSSLLR RMPALETLEI LKLVNCPETF
     TPDMKCIMGE SPVVQGYFVL AGMNSAGLSL GGGAGKFLAE WMVYGYPSEN VWELDLQRFG
     ALQSSRTFLR HRVMEVMPLI YDLKVPRWDF QTGRQLRTSP LYDRLDAQGA RWMEKHGFER
     PKYFVPPNKD LLALEQSKTF YKPDWFDIVE SEVKCCKEAV CVIDMSSFTK FEITSTGDEA
     LESLQYLFCN DLDVPVGHIV HTGMLNEYGG YENDCSIARL TKRSFFMISP TDQQVHCWAW
     LNKYLPKDSN LLLEDVTWKY TALNLIGPRA VDVLSELSYA PMTPDHFPTL FCKEMSVGYA
     NGIRVMSMTH TGEPGFMLYI PIEYALHVYN EVMSVGQKYG IRNAGYYALR SLRIEKFFAF
     WGQDLNTLTT PLECGGESRV KLEKGIDFIG RDALLQQKQT GVYKRLAMFI LDDHDTDLDL
     WPWWGEPIYR NGKYAGKTTS SAYSYTLERH VCLGYVHNFS EDSGEEQVVT TDFINRGEYE
     IDIAGHRFQA KAKLYPVTSF FTHKRRKDDV ELSDFHGK
//
ID   Q7TSV1_MOUSE            Unreviewed;       806 AA.
AC   Q7TSV1;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   02-NOV-2010, entry version 49.
DE   SubName: Full=Tns1 protein;
DE   Flags: Fragment;
GN   Name=Tns1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
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DR   EMBL; BC052740; AAH52740.1; -; mRNA.
DR   IPI; IPI00378438; -.
DR   UniGene; Mm.309975; -.
DR   HSSP; P16277; 1BLK.
DR   ProteinModelPortal; Q7TSV1; -.
DR   STRING; Q7TSV1; -.
DR   Ensembl; ENSMUST00000068832; ENSMUSP00000065635; ENSMUSG00000055322.
DR   UCSC; uc007blg.1; mouse.
DR   MGI; MGI:104552; Tns1.
DR   HOGENOM; HBG715389; -.
DR   HOVERGEN; HBG066510; -.
DR   InParanoid; Q7TSV1; -.
DR   ArrayExpress; Q7TSV1; -.
DR   Bgee; Q7TSV1; -.
DR   Genevestigator; Q7TSV1; -.
DR   GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; TAS:MGI.
DR   GO; GO:0016477; P:cell migration; IMP:MGI.
DR   GO; GO:0007044; P:cell-substrate junction assembly; IMP:MGI.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR013625; PTB.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   InterPro; IPR000980; SH2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF08416; PTB; 1.
DR   Pfam; PF00017; SH2; 1.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM00252; SH2; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   1: Evidence at protein level;
FT   NON_TER       1      1
SQ   SEQUENCE   806 AA;  84160 MW;  0B9C95A85224EAC6 CRC64;
     ENQSPEATSP RSPGVRSPVQ CVSPELALTI ALNPGGRPKE PHLHSYKEAF EEMEGTSPSS
     PPHSVARSPP GLAKTPLSAL GLKPHNPADI LLHPTGEPRS YVESVARTAV AGPRAQDVEP
     KSFSAPAAHA YGHETPLRNG TPGGSFVSPS PLSTSSPILS ADSTSVGSFP SVVSSDQGPR
     TPFQPMLDSS IRSGSLGQPS PAALSYQSSS PVPVGGSSYN SPDYSLQPFS SSPESQGQPQ
     YSAASVHMVP GSPQARHRTV GTNTPPSPGF GRRAVNPTMA APGSPSLSHR QVMGPSGPGF
     HGNVVSGHPA SAATTPGSPS LGRHPVGSHQ VPGLHSSVVT TPGSPSLGRH PGAHQGNLAS
     SLHSNAVISP GSPSLGRHLG GSGSVVPGSP SLDRHAAYGG YSTPEDRRPT LSRQSSASGY
     QAPSTPSFPV SPAYYPGLSS PATSPSPDSA AFRQGSPTPA LPEKRRMSVG DRAGSLPNYA
     TINGKVSSSP VANGMASGSS TVSFSHTLPD FSKYSMPDNS PETRAKVKFV QDTSKYWYKP
     EISREQAIAL LKDQEPGAFI IRDSHSFRGA YGLAMKVSSP PPTITQQGKK GDMTHELVRH
     FLIETGPRGV KLKGCPNEPN FGSLSALVYQ HSVIPLALPC KLVIPSRDPT DESKDSSGPA
     NSTTDLLKQG AACNVLFVNS VDMESLTGPQ AISKATSETL AADPTPAATI VHFKVSAQGI
     TLTDNQRKLF FRRHYPLNTV TFCDLERKWM KTEGGAPAKL FGFVARKQGS TTDNACHLFA
     ELDPNQPASA IVNFVSKVML SAGQKR
//
ID   NACC1_MOUSE             Reviewed;         514 AA.
AC   Q7TSZ8; Q80X97; Q9CZ72;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Nucleus accumbens-associated protein 1;
DE            Short=NAC-1;
DE   AltName: Full=BTB/POZ domain-containing protein 14B;
GN   Name=Nacc1; Synonyms=Btbd14b, Nac1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
RX   PubMed=14521994; DOI=10.1016/S0306-4522(03)00376-2;
RA   Mackler S.A., Homan Y.X., Korutla L., Conti A.C., Blendy J.A.;
RT   "The mouse Nac1 gene, encoding a cocaine-regulated bric-a-brac
RT   tramtrac broad complex/pox virus and zinc finger protein, is regulated
RT   by AP1.";
RL   Neuroscience 121:355-361(2003).
RN   [4]
RP   FUNCTION.
RX   PubMed=17130457; DOI=10.1073/pnas.0604083103;
RA   Nakayama K., Nakayama N., Davidson B., Sheu J.-J.C., Jinawath N.,
RA   Santillan A., Salani R., Bristow R.E., Morin P.J., Kurman R.J.,
RA   Wang T.-L., Shih I.-M.;
RT   "A BTB/POZ protein, NAC-1, is related to tumor recurrence and is
RT   essential for tumor growth and survival.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18739-18744(2006).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17945361; DOI=10.1016/j.bbr.2007.08.036;
RA   Mackler S., Pacchioni A., Degnan R., Homan Y., Conti A.C., Kalivas P.,
RA   Blendy J.A.;
RT   "Requirement for the POZ/BTB protein NAC1 in acute but not chronic
RT   psychomotor stimulant response.";
RL   Behav. Brain Res. 187:48-55(2008).
CC   -!- FUNCTION: Functions as a transcriptional repressor. Seems to
CC       function as a transcriptional corepressor in neuronal cells
CC       through recruitment of HDAC3 and HDAC4. Contributes to tumor
CC       progression, and tumor cell proliferation and survival. This may
CC       be mediated at least in part through repressing transcriptional
CC       activity of GADD45GIP1. Required for recruiting the proteasome
CC       from the nucleus to the cytoplasm and dendritic spines. Involved
CC       in the acute behavioral and neurological responses to cocaine and
CC       amphetamines.
CC   -!- SUBUNIT: Homooligomer; mediated by the BTB domain. Interacts with
CC       HDAC3 and HDAC4. Interacts (via BTB domain) with CUL3, PSMD7 AND
CC       RCOR1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Distribution in the
CC       cytoplasm is dependent on phosphorylation (By similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed with higher expression
CC       in the brain, kidney and liver, and at lower levels in heart, lung
CC       and testes.
CC   -!- DISRUPTION PHENOTYPE: Mice are viable with no obvious
CC       developmental or physiological impairments. In addition, they do
CC       not display alterations in chronic responses to cocaine and
CC       amphetamine administration, but do however display significantly
CC       diminished acute behavioral and neurochemical responses to these
CC       drugs.
CC   -!- SIMILARITY: Contains 1 BEN domain.
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK012935; BAB28558.1; -; mRNA.
DR   EMBL; BC048157; AAH48157.1; -; mRNA.
DR   EMBL; BC052706; AAH52706.1; -; mRNA.
DR   EMBL; BC054800; AAH54800.1; -; mRNA.
DR   IPI; IPI00378026; -.
DR   RefSeq; NP_080064.3; NM_025788.3.
DR   UniGene; Mm.289698; -.
DR   HSSP; Q05516; 1CS3.
DR   ProteinModelPortal; Q7TSZ8; -.
DR   SMR; Q7TSZ8; 2-123.
DR   DIP; DIP-29930N; -.
DR   STRING; Q7TSZ8; -.
DR   PhosphoSite; Q7TSZ8; -.
DR   PRIDE; Q7TSZ8; -.
DR   Ensembl; ENSMUST00000001975; ENSMUSP00000001975; ENSMUSG00000001910.
DR   GeneID; 66830; -.
DR   KEGG; mmu:66830; -.
DR   UCSC; uc009mmu.1; mouse.
DR   CTD; 66830; -.
DR   MGI; MGI:1914080; Nacc1.
DR   eggNOG; roNOG15599; -.
DR   GeneTree; ENSGT00580000081504; -.
DR   HOGENOM; HBG446537; -.
DR   HOVERGEN; HBG052875; -.
DR   InParanoid; Q7TSZ8; -.
DR   OMA; FETASHD; -.
DR   OrthoDB; EOG4MKNG3; -.
DR   PhylomeDB; Q7TSZ8; -.
DR   NextBio; 322761; -.
DR   ArrayExpress; Q7TSZ8; -.
DR   Bgee; Q7TSZ8; -.
DR   Genevestigator; Q7TSZ8; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016604; C:nuclear body; ISS:UniProtKB.
DR   GO; GO:0016566; F:specific transcriptional repressor activity; ISS:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; ISS:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR018379; BEN_domain.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR013069; BTB_POZ.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF10523; BEN; 1.
DR   Pfam; PF00651; BTB; 1.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   PROSITE; PS51457; BEN; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Nucleus; Phosphoprotein; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    514       Nucleus accumbens-associated protein 1.
FT                                /FTId=PRO_0000274042.
FT   DOMAIN       30     94       BTB.
FT   DOMAIN      360    457       BEN.
FT   MOD_RES     245    245       Phosphoserine; by PKC (By similarity).
FT   CONFLICT    401    401       S -> R (in Ref. 1; BAB28558).
FT   CONFLICT    403    403       G -> V (in Ref. 2; AAH48157).
SQ   SEQUENCE   514 AA;  56537 MW;  C83C23891B097626 CRC64;
     MAQTLQMEIP NFGNSILECL NEQRLQGLYC DVSVVVKGHA FKAHRAVLAA SSSYFRDLFN
     SSRSAVVELP AAVQPQSFQQ ILTFCYTGRL SMNMGDQFLL IYTAGFLQIQ EIMEKGTEFF
     LKVSSPSCDS QGLHPEEAPS SEPQSPVAQT LGWPACSTPL PLVSRVKTEQ ELDSVQCTPM
     AKRLWDSSQK EAGGSGGNNG SRKMAKFSTP DLALNRMPQP LSMATATAAV AVVAVGGCVS
     GPSMSERTSP GTSSAYTSDS PSSYHNEEDE EEDAGEEGTD EQYRQICNMY TMYSMLNVGQ
     TAEKVEALPE QVVLESRSRI RVRQDLASLP AELINQIGNR CHPKLYDEGD PSEKLELVTG
     TNVYITRAQL MNCHVSAGTR HKVLLRRLLA SFFDRNTLAN SCGTGIRSST NDPRRKPLDS
     RVLHAVKYYC QNFAPNFKES EMNAIAADMC TNARRVVRKS WLPKTKPLHL VEGDNYSSFI
     SDTCKIEPDM MSMEHSFETA SHDGEAGPSA EVLQ
//
ID   RRAGD_MOUSE             Reviewed;         449 AA.
AC   Q7TT45; Q6GTT2; Q9CYC2;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 2.
DT   08-FEB-2011, entry version 50.
DE   RecName: Full=Ras-related GTP-binding protein D;
DE            Short=Rag D;
DE            Short=RagD;
GN   Name=Rragd; Synonyms=Ragd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-258.
RA   Shan Z., Popescu N.C.;
RT   "Isolation and characterization of a mouse GTP-binding protein.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 67-449.
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 111-449.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Has guanine nucleotide-binding activity but lacks
CC       intrinsic GTPase activity. Probably required for the amino acid-
CC       induced relocalization of mTORC1 to the lysosomes and its
CC       subsequent activation by the GTPase RHEB. This is a crucial step
CC       in the activation of the TOR signaling cascade by amino acids (By
CC       similarity).
CC   -!- SUBUNIT: Forms a heterodimer with RRAGA in a sequence-independent
CC       manner. Binds GTP. Interacts with NOL8 and RRAGB (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Lysosome (By similarity). Note=Predominantly
CC       cytoplasmic. May shuttle between the cytoplasm and nucleus,
CC       depending on the bound nucleotide state of associated RRAGA (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the GTR/RAG GTP-binding protein family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF490406; AAP40334.1; -; mRNA.
DR   EMBL; BC038137; AAH38137.1; -; mRNA.
DR   EMBL; AK017818; BAB30954.2; -; mRNA.
DR   IPI; IPI00187271; -.
DR   RefSeq; NP_081767.2; NM_027491.2.
DR   UniGene; Mm.300814; -.
DR   UniGene; Mm.396693; -.
DR   ProteinModelPortal; Q7TT45; -.
DR   SMR; Q7TT45; 110-288.
DR   PhosphoSite; Q7TT45; -.
DR   PRIDE; Q7TT45; -.
DR   Ensembl; ENSMUST00000029946; ENSMUSP00000029946; ENSMUSG00000028278.
DR   GeneID; 52187; -.
DR   KEGG; mmu:52187; -.
DR   UCSC; uc008sfl.1; mouse.
DR   CTD; 52187; -.
DR   MGI; MGI:1098604; Rragd.
DR   GeneTree; ENSGT00550000074708; -.
DR   HOVERGEN; HBG059482; -.
DR   InParanoid; Q7TT45; -.
DR   NextBio; 308622; -.
DR   ArrayExpress; Q7TT45; -.
DR   Bgee; Q7TT45; -.
DR   CleanEx; MM_RRAGD; -.
DR   Genevestigator; Q7TT45; -.
DR   GermOnline; ENSMUSG00000028278; Mus musculus.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR006762; Gtr1_RagA.
DR   PANTHER; PTHR11259; Gtr1_RagA; 1.
DR   Pfam; PF04670; Gtr1_RagA; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; GTP-binding; Lysosome; Nucleotide-binding; Nucleus.
FT   CHAIN         1    449       Ras-related GTP-binding protein D.
FT                                /FTId=PRO_0000239954.
FT   NP_BIND     118    126       GTP (By similarity).
FT   NP_BIND     166    170       GTP (By similarity).
FT   NP_BIND     228    231       GTP (By similarity).
FT   CONFLICT    111    111       K -> M (in Ref. 3; BAB30954).
FT   CONFLICT    115    115       L -> S (in Ref. 3; BAB30954).
FT   CONFLICT    184    184       F -> L (in Ref. 3; BAB30954).
FT   CONFLICT    192    192       F -> C (in Ref. 2; AAH38137).
FT   CONFLICT    383    383       K -> M (in Ref. 3; BAB30954).
SQ   SEQUENCE   449 AA;  51232 MW;  6D9AC2A86DE5784A CRC64;
     MSQVLGKPQP QGEDGGEDQE EDELVGLAGY EDGPESSDAE LDSGPEEGES RRNSWMPRSW
     CSEATRHECW EPGLWRSSHL LGIGGGWRML RRQRQADFFL DFSDPFSTEV KPRILLMGLR
     RSGKSSIQKV VFHKMSPSET LFLESTNRIC REDVSNSSFV NFQIWDFPGQ IDFFDPTFDY
     EMIFRGTGAL IFVIDSQDDY MEALARLHLT VTRAYKVNTD INFEVFIHKV DGLSDDHKIE
     TQRDIHQRAN DDLADAGLEK IHLSFYLTSI YDHSIFEAFS KVVQKLIPQL PTLENLLNIF
     ISNSGIEKAF LFDVVSKIYI ATDSTPVDMQ TYELCCDMID VVIDISCIYG LKEDGAGAPY
     DKDSTAIIKL NNTTVLYLKE VTKFLALVCF VREESFERKG LIDYNFHCFR KAIHEVFEVR
     MKMVKSRKAQ SRLPKKTGAT PNGTPRVLL
//
ID   MRCKB_MOUSE             Reviewed;        1713 AA.
AC   Q7TT50; Q69ZR5; Q80W33;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Serine/threonine-protein kinase MRCK beta;
DE            EC=2.7.11.1;
DE   AltName: Full=CDC42-binding protein kinase beta;
DE   AltName: Full=DMPK-like beta;
DE   AltName: Full=Myotonic dystrophy kinase-related CDC42-binding kinase beta;
DE            Short=MRCK beta;
DE            Short=Myotonic dystrophy protein kinase-like beta;
GN   Name=Cdc42bpb; Synonyms=Kiaa1124;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Huang C.Q., Wu S.L., Cheng Z.;
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 628-1713.
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 633-642, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1139-1713.
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-954, AND MASS
RP   SPECTROMETRY.
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1692 AND SER-1695, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1692, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May act as a downstream effector of CDC42 in
CC       cytoskeletal reorganization. Contributes to the actomyosin
CC       contractility required for cell invasion, through the regulation
CC       of MYPT1 and thus MLC2 phosphorylation (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Maintained in an inactive, closed conformation
CC       by an interaction between the kinase domain and the negative
CC       autoregulatory C-terminal coiled-coil region. Agonist binding to
CC       the phorbol ester binding site disrupts this, releasing the kinase
CC       domain to allow N-terminus-mediated dimerization and kinase
CC       activation by transautophosphorylation (By similarity).
CC   -!- SUBUNIT: Homodimer and homotetramer via the coiled coil regions.
CC       Interacts tightly with GTP-bound but not GDP-bound CDC42 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=Displays a
CC       dispersed punctate distribution and concentrates along the cell
CC       periphery, especially at the leading edge and cell-cell junction.
CC       This concentration is PH-domain dependent (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. DMPK subfamily.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 CNH domain.
CC   -!- SIMILARITY: Contains 1 CRIB domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY277589; AAP34402.1; -; mRNA.
DR   EMBL; AK173103; BAD32381.1; -; mRNA.
DR   EMBL; BC049921; AAH49921.1; -; mRNA.
DR   IPI; IPI00114613; -.
DR   UniGene; Mm.479890; -.
DR   ProteinModelPortal; Q7TT50; -.
DR   SMR; Q7TT50; 12-414, 896-934, 1024-1084, 1097-1219.
DR   STRING; Q7TT50; -.
DR   PhosphoSite; Q7TT50; -.
DR   PRIDE; Q7TT50; -.
DR   Ensembl; ENSMUST00000041965; ENSMUSP00000042565; ENSMUSG00000021279.
DR   UCSC; uc007pct.1; mouse.
DR   MGI; MGI:2136459; Cdc42bpb.
DR   eggNOG; roNOG05220; -.
DR   GeneTree; ENSGT00600000084128; -.
DR   HOGENOM; HBG444706; -.
DR   HOVERGEN; HBG055933; -.
DR   InParanoid; Q7TT50; -.
DR   OrthoDB; EOG4640B1; -.
DR   PhylomeDB; Q7TT50; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 376071; -.
DR   ArrayExpress; Q7TT50; -.
DR   Bgee; Q7TT50; -.
DR   CleanEx; MM_CDC42BPB; -.
DR   Genevestigator; Q7TT50; -.
DR   GermOnline; ENSMUSG00000021279; Mus musculus.
DR   GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR   GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0005083; F:small GTPase regulator activity; IEA:InterPro.
DR   GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR001180; Citron.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR014930; Myotonic_dystrophy_kinase_coil.
DR   InterPro; IPR000095; PAK_box_Rho-bd.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF08826; DMPK_coil; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   ProDom; PD011252; Myotonic_dystrophy_kinase_coil; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00285; PBD; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Coiled coil; Cytoplasm; Direct protein sequencing;
KW   Kinase; Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1   1713       Serine/threonine-protein kinase MRCK
FT                                beta.
FT                                /FTId=PRO_0000086395.
FT   DOMAIN       76    342       Protein kinase.
FT   DOMAIN      343    413       AGC-kinase C-terminal.
FT   DOMAIN     1096   1215       PH.
FT   DOMAIN     1241   1515       CNH.
FT   DOMAIN     1585   1598       CRIB.
FT   NP_BIND      82     90       ATP (By similarity).
FT   ZN_FING    1026   1076       Phorbol-ester/DAG-type.
FT   COILED      434    649       Potential.
FT   COILED      681    815       Potential.
FT   COILED      878    939       Potential.
FT   ACT_SITE    200    200       Proton acceptor (By similarity).
FT   BINDING     105    105       ATP (By similarity).
FT   MOD_RES     221    221       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     233    233       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     239    239       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     362    362       Phosphoserine (By similarity).
FT   MOD_RES     363    363       Phosphoserine (By similarity).
FT   MOD_RES     914    914       Phosphoserine (By similarity).
FT   MOD_RES     954    954       Phosphotyrosine.
FT   MOD_RES    1197   1197       Phosphothreonine (By similarity).
FT   MOD_RES    1688   1688       Phosphoserine (By similarity).
FT   MOD_RES    1692   1692       Phosphoserine.
FT   MOD_RES    1695   1695       Phosphoserine.
SQ   SEQUENCE   1713 AA;  194781 MW;  0D63976EAC61DDE1 CRC64;
     MSAKVRLKKL EQLLLDGPWR NDSALSVETL LDVLVCLYTE CSHSALRRDK YVAEFLEWAK
     PFTQLVKDMQ LHREDFEIIK VIGRGAFGEV AVVKMRNTER IYAMKILNKW EMLKRAETAC
     FREERDVLVN GDCQWITALH YAFQDENYLY LVMDYYVGGD LLTLLSKFED KLPEDMARFY
     IGEMVLAIDS IHQLHYVHRD IKPDNVLLDV NGHIRLADFG SCLKMNDDGT VQSSVAVGTP
     DYISPEILQA MEDGMGKYGP ECDWWSLGVC MYEMLYGETP FYAESLVETY GKIMNHEERF
     QFPSHVTDVS EEAKDLIQRL ICSRERRLGQ NGIEDFKKHA FFEGLNWENI RNLEAPYIPD
     VSSPSDTSNF DVDDDMLRNI EILPPGSHTG FSGLHLPFIG FTFTTESCFS DRGSLKSMTQ
     SNTLTKDEDV QRDLENSLQI EAYERRIRRL EQEKLELSRK LQESTQTVQS LHGSTRALGN
     SNRDKEIKRL NEELERMKSK MADSNRLERQ LEDTVTLRQE HEDSTHRLKG LEKQYRLARQ
     EKEELHKQLV EASERLKSQT KELKDAHQQR KRALQEFSEL NERMSELRSL KQKVSRQLRD
     KEEEMEVAMQ KIDSMRQDLR KSEKSRKELE ARLEDAAAEA SKERKLREHS ESFCKQMERE
     LEALKVKQGG RGPGAASEHQ QEISKIRSEL EKKVLFYEEE LVRREASHVL EVKNVKKEVH
     DSESHQLALQ KEVLMLKDKL EKSKRERHSE MEEAIGTVKD KYERERAMLF DENKKLTAEN
     EKLCSFVDKL TAQNRQLEDE LQDLASKKES VAHWEAQIAE IIQWVSDEKD ARGYLQALAS
     KMTEELETLR SSSLGSRTLD PLWKVRRSQK LDMSARLELQ SALEAEIRAK QLVQEELRKV
     KDSSLAFESK LKESEAKNRE LLEEMQSLRK RMEEKFRADT GLKLPDFQDS IFEYFNTAPL
     AHDLTFRTSS ASDQETQASK MDLSPSVSVA TSTEQQEDMA RPQQRPSPVP LPSTQALAMA
     GPKPKAHQFS IKSFPSPTQC SHCTSLMVGL IRQGYACEVC AFSCHVSCKD SAPQVCPIPP
     EQSKRPLGVD VQRGIGTAYK GYVKVPKPTG VKKGWQRAYA VVCDCKLFLY DLPEGKSTQP
     GVVASQVLDL RDEEFAVSSV LASDVIHATR RDIPCIFRVT ASLLGSPSKT SSLLILTENE
     NEKRKWVGIL EGLQAILHKN RLKSQVVHVA QEAYDSSLPL IKAVLAAAIV DGDRIAVGLE
     EGLYVIELTR DVIVRAADCK KVYQIELAPK EKIAILLCGR NHHVHLYPWS SFDGAEASNF
     DIKLPETKGC QLIATGTLRK SSSTCLFVAV KRLILCYEIQ RTKPFHRKFS ELVAPGHVQW
     MAVFKDRLCV GYPSGFSLLS IQGDGPPLDL VNPTDPSLAF LSQQSFDALC AVELKSEEYL
     LCFSHMGLYV DPQGRRSRMQ ELMWPAAPVA CSCSPTHVTV YSEYGVDVFD VRTMEWVQTI
     GLRRIRPLNS DGSLNLLGCE PPRLIYFKNK FSGTILNVPD TSDNSKKQML RTRSKRRFVF
     KVPEEERLQQ RREMLRDPEL RSKMISNPTN FNHVAHMGPG DGMQVLMDLP LSAAPTVQEE
     KQGPTPAGLP RQPPSRSKPY VSWPSSGGSE PGVPVPLRSM SDPDQDFDKE PDSDSTKHST
     PSNSSNPSGP PSPNSPHRSQ LPMEGLDQPS CDA
//
ID   SAHH2_MOUSE             Reviewed;         530 AA.
AC   Q80SW1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Putative adenosylhomocysteinase 2;
DE            Short=AdoHcyase 2;
DE            EC=3.3.1.1;
DE   AltName: Full=IP3R-binding protein released with inositol 1,4,5-trisphosphate;
DE   AltName: Full=S-adenosyl-L-homocysteine hydrolase 2;
DE   AltName: Full=S-adenosylhomocysteine hydrolase-like protein 1;
GN   Name=Ahcyl1; Synonyms=Irbit;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH ITPR1.
RC   TISSUE=Cerebellum;
RX   MEDLINE=22526701; PubMed=12525476; DOI=10.1074/jbc.M210119200;
RA   Ando H., Mizutani A., Matsu-ura T., Mikoshiba K.;
RT   "IRBIT, a novel inositol 1,4,5-trisphosphate (IP3) receptor-binding
RT   protein, is released from the IP3 receptor upon IP3 binding to the
RT   receptor.";
RL   J. Biol. Chem. 278:10602-10612(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 74-80, INTERACTION WITH ITPR1, MUTAGENESIS OF
RP   70-SER--ASP-73; ASP-73; 82-THR--ASP-88 AND 86-ASP--GLU-88, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=16527252; DOI=10.1016/j.bbrc.2006.02.119;
RA   Devogelaere B., Nadif Kasri N., Derua R., Waelkens E., Callewaert G.,
RA   Missiaen L., Parys J.B., De Smedt H.;
RT   "Binding of IRBIT to the IP3 receptor: determinants and functional
RT   effects.";
RL   Biochem. Biophys. Res. Commun. 343:49-56(2006).
RN   [4]
RP   PROTEIN SEQUENCE OF 479-486, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   IDENTIFICATION.
RX   MEDLINE=21901265; PubMed=11904675; DOI=10.1007/s00251-001-0402-z;
RA   Dekker J.W., Budhia S., Angel N.Z., Cooper B.J., Clark G.J.,
RA   Hart D.N., Kato M.;
RT   "Identification of an S-adenosylhomocysteine hydrolase-like transcript
RT   induced during dendritic cell differentiation.";
RL   Immunogenetics 53:993-1001(2002).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-82; SER-84 AND SER-85,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-homocysteine + H(2)O = L-
CC       homocysteine + adenosine.
CC   -!- COFACTOR: Binds 1 NAD per subunit (By similarity).
CC   -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L-
CC       homocysteine from S-adenosyl-L-homocysteine: step 1/1.
CC   -!- SUBUNIT: Interacts with ITPR1. Competes with IP3 for interaction
CC       with ITPR1 and attenuates IP3-induced Ca(2+) release through the
CC       ITPR1 from the non-mitochondrial intracellular stores.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum.
CC   -!- DOMAIN: The PEST region is essential for the interaction with
CC       ITPR1. The PDZ-binding region is required for maximal interaction
CC       with ITPR1 and is also responsible for the IP3-insensitive
CC       interaction with ITPR1.
CC   -!- SIMILARITY: Belongs to the adenosylhomocysteinase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB092504; BAC65166.1; -; mRNA.
DR   EMBL; BC018218; AAH18218.2; -; mRNA.
DR   EMBL; BK000547; DAA00059.1; -; mRNA.
DR   IPI; IPI00162781; -.
DR   RefSeq; NP_663517.2; NM_145542.3.
DR   UniGene; Mm.220328; -.
DR   ProteinModelPortal; Q80SW1; -.
DR   SMR; Q80SW1; 101-530.
DR   STRING; Q80SW1; -.
DR   PhosphoSite; Q80SW1; -.
DR   PRIDE; Q80SW1; -.
DR   Ensembl; ENSMUST00000029490; ENSMUSP00000029490; ENSMUSG00000027893.
DR   GeneID; 229709; -.
DR   KEGG; mmu:229709; -.
DR   UCSC; uc008qxj.1; mouse.
DR   CTD; 229709; -.
DR   MGI; MGI:2385184; Ahcyl1.
DR   eggNOG; roNOG14611; -.
DR   GeneTree; ENSGT00390000003626; -.
DR   HOGENOM; HBG352029; -.
DR   HOVERGEN; HBG005041; -.
DR   InParanoid; Q80SW1; -.
DR   OMA; KQIQFVE; -.
DR   OrthoDB; EOG4GMTWR; -.
DR   PhylomeDB; Q80SW1; -.
DR   BRENDA; 3.3.1.1; 244.
DR   NextBio; 379631; -.
DR   ArrayExpress; Q80SW1; -.
DR   Bgee; Q80SW1; -.
DR   CleanEx; MM_AHCYL1; -.
DR   Genevestigator; Q80SW1; -.
DR   GermOnline; ENSMUSG00000027893; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0004013; F:adenosylhomocysteinase activity; IEA:EC.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000043; Adenosylhomocysteinase.
DR   InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd.
DR   InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS.
DR   PANTHER; PTHR23420; Ad_hcy_hydrolase; 1.
DR   Pfam; PF05221; AdoHcyase; 1.
DR   Pfam; PF00670; AdoHcyase_NAD; 1.
DR   PIRSF; PIRSF001109; Ad_hcy_hydrolase; 1.
DR   TIGRFAMs; TIGR00936; ahcY; 1.
DR   PROSITE; PS00738; ADOHCYASE_1; 1.
DR   PROSITE; PS00739; ADOHCYASE_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Hydrolase; NAD;
KW   One-carbon metabolism; Phosphoprotein.
FT   CHAIN         1    530       Putative adenosylhomocysteinase 2.
FT                                /FTId=PRO_0000230300.
FT   NP_BIND     318    322       NAD (By similarity).
FT   NP_BIND     397    399       NAD (By similarity).
FT   REGION       65     92       PEST.
FT   REGION      281    448       NAD binding (By similarity).
FT   REGION      520    530       PDZ-binding.
FT   BINDING     155    155       Substrate (By similarity).
FT   BINDING     229    229       Substrate (By similarity).
FT   BINDING     254    254       Substrate (By similarity).
FT   BINDING     284    284       Substrate (By similarity).
FT   BINDING     288    288       Substrate (By similarity).
FT   BINDING     341    341       NAD (By similarity).
FT   BINDING     376    376       NAD (By similarity).
FT   MOD_RES      28     28       Phosphotyrosine (By similarity).
FT   MOD_RES      82     82       Phosphothreonine.
FT   MOD_RES      84     84       Phosphoserine.
FT   MOD_RES      85     85       Phosphoserine.
FT   MOD_RES     391    391       Phosphoserine (By similarity).
FT   MOD_RES     400    400       Phosphoserine (By similarity).
FT   MOD_RES     402    402       Phosphothreonine (By similarity).
FT   MOD_RES     407    407       Phosphothreonine (By similarity).
FT   MUTAGEN      70     73       Missing: Inhibits interaction with ITPR1.
FT   MUTAGEN      73     73       D->R: Inhibits interaction with ITPR1.
FT   MUTAGEN      82     88       Missing: Inhibits interaction with ITPR1.
FT   MUTAGEN      86     88       DDE->KKK: Does not inhibits interaction
FT                                with ITPR1.
SQ   SEQUENCE   530 AA;  58951 MW;  974D23361A245D04 CRC64;
     MSMPDAMPLP GVGEELKQAK EIEDAEKYSF MATVTKAPKK QIQFADDMQE FTKFPTKTGR
     RSLSRSISQS STDSYSSAAS YTDSSDDEVS PREKQQTNSK GSSNFCVKNI KQAEFGRREI
     EIAEQDMSAL ISLRKRAQGE KPLAGAKIVG CTHITAQTAV LIETLCALGA QCRWSACNIY
     STQNEVAAAL AEAGVAVFAW KGESEDDFWW CIDRCVNMDG WQANMILDDG GDLTHWVYKK
     YPNVFKKIRG IVEESVTGVH RLYQLSKAGK LCVPAMNVND SVTKQKFDNL YCCRESILDG
     LKRTTDVMFG GKQVVVCGYG EVGKGCCAAL KALGAIVYIT EIDPICALQA CMDGFRVVKL
     NEVIRQVDVV ITCTGNKNVV TREHLDRMKN SCIVCNMGHS NTEIDVTSLR TPELTWERVR
     SQVDHVIWPD GKRVVLLAEG RLLNLSCSTV PTFVLSITAT TQALALIELY NAPEGRYKQD
     VYLLPKKMDE YVASLHLPSF DAHLTELTDD QAKYLGLNKN GPFKPNYYRY
//
ID   MIB1_MOUSE              Reviewed;        1006 AA.
AC   Q80SY4; Q5XK51; Q6IS57; Q6YI52; Q6ZPT8; Q8BNR1; Q8C6W2; Q921Q1;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=E3 ubiquitin-protein ligase MIB1;
DE            EC=6.3.2.-;
DE   AltName: Full=DAPK-interacting protein 1;
DE            Short=DIP-1;
DE   AltName: Full=Mind bomb homolog 1;
GN   Name=Mib1; Synonyms=Dip1, Kiaa1323, Mib;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   UBIQUITINATION.
RC   TISSUE=Urinary bladder;
RX   MEDLINE=22344653; PubMed=12351649; DOI=10.1074/jbc.M208585200;
RA   Jin Y., Blue E.K., Dixon S., Shao Z., Gallagher P.J.;
RT   "A death-associated protein kinase (DAPK)-interacting protein, DIP-1,
RT   is an E3 ubiquitin ligase that promotes tumor necrosis factor-induced
RT   apoptosis and regulates the cellular levels of DAPK.";
RL   J. Biol. Chem. 277:46980-46986(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C3H;
RX   MEDLINE=22419263; PubMed=12530964; DOI=10.1016/S1534-5807(02)00409-4;
RA   Itoh M., Kim C.-H., Palardy G., Oda T., Jiang Y.-J., Maust D.,
RA   Yeo S.-Y., Lorick K., Wright G.J., Ariza-McNaughton L., Weissman A.M.,
RA   Lewis J., Chandrasekharappa S.C., Chitnis A.B.;
RT   "Mind bomb is a ubiquitin ligase that is essential for efficient
RT   activation of Notch signaling by Delta.";
RL   Dev. Cell 4:67-82(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND UBIQUITINATION.
RX   PubMed=15824097; DOI=10.1074/jbc.M501631200;
RA   Koo B.-K., Yoon K.-J., Yoo K.-W., Lim H.-S., Song R., So J.-H.,
RA   Kim C.-H., Kong Y.-Y.;
RT   "Mind bomb-2 is an E3 ligase for Notch ligand.";
RL   J. Biol. Chem. 280:22335-22342(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 349-1006.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 547-1006.
RC   STRAIN=129, and FVB/N; TISSUE=Embryo, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 864-1006.
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination
CC       of Delta receptors, which act as ligands of Notch proteins.
CC       Positively regulates the Delta-mediated Notch signaling by
CC       ubiquitinating the intracellular domain of Delta, leading to
CC       endocytosis of Delta receptors (By similarity). Probably mediates
CC       ubiquitination and subsequent proteasomal degradation of DAPK1,
CC       thereby antagonizing anti-apoptotic effects of DAPK1 to promote
CC       TNF-induced apoptosis.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Localizes to
CC       the plasma membrane.
CC   -!- TISSUE SPECIFICITY: Detected in all tissues tested. Present in
CC       embryo, embryonic stem cells, bladder, skeletal muscle, bladder,
CC       uterus, testis, stomach, colon, ileum, trachea, lung, aorta,
CC       kidney, spleen, liver and vas deferens (at protein level). Highly
CC       expressed in testis.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed both in embryos and adult
CC       tissues. In E9.5 and E10.5 embryos, it is expressed in the tail
CC       bud, limb buds and somites. Expressed in the same pattern than
CC       MIB2 in the skin and intestine at postnatal day 1 (P1) and in the
CC       hair follicle in the skin in the adult.
CC   -!- PTM: Ubiquitinated. Possibly via autoubiquitination.
CC   -!- SIMILARITY: Contains 9 ANK repeats.
CC   -!- SIMILARITY: Contains 2 MIB/HERC2 domains.
CC   -!- SIMILARITY: Contains 3 RING-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 ZZ-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH11287.1; Type=Erroneous initiation;
CC       Sequence=AAH69870.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA;
CC       Sequence=AAN18022.1; Type=Erroneous initiation;
CC       Sequence=BAC38042.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part;
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DR   EMBL; AY245539; AAO91933.1; -; mRNA.
DR   EMBL; AY149907; AAN75492.1; -; mRNA.
DR   EMBL; AY147848; AAN18022.1; ALT_INIT; mRNA.
DR   EMBL; AY974091; AAX84653.1; -; mRNA.
DR   EMBL; AK053035; BAC35245.1; -; mRNA.
DR   EMBL; AK080847; BAC38042.1; ALT_SEQ; mRNA.
DR   EMBL; BC011287; AAH11287.1; ALT_INIT; mRNA.
DR   EMBL; BC069870; AAH69870.1; ALT_SEQ; mRNA.
DR   EMBL; BC083072; AAH83072.1; -; mRNA.
DR   EMBL; AK129331; BAC98141.1; -; mRNA.
DR   IPI; IPI00330112; -.
DR   RefSeq; NP_659109.2; NM_144860.2.
DR   UniGene; Mm.21500; -.
DR   ProteinModelPortal; Q80SY4; -.
DR   SMR; Q80SY4; 14-72, 83-130, 138-224, 430-784, 862-909, 954-1002.
DR   IntAct; Q80SY4; 1.
DR   MINT; MINT-1550820; -.
DR   STRING; Q80SY4; -.
DR   PRIDE; Q80SY4; -.
DR   Ensembl; ENSMUST00000052838; ENSMUSP00000054428; ENSMUSG00000024294.
DR   GeneID; 225164; -.
DR   KEGG; mmu:225164; -.
DR   UCSC; uc008ebc.1; mouse.
DR   CTD; 225164; -.
DR   MGI; MGI:2443157; Mib1.
DR   GeneTree; ENSGT00590000082925; -.
DR   HOVERGEN; HBG068386; -.
DR   InParanoid; Q80SY4; -.
DR   OMA; DVGKVDT; -.
DR   OrthoDB; EOG461435; -.
DR   PhylomeDB; Q80SY4; -.
DR   NextBio; 377558; -.
DR   ArrayExpress; Q80SY4; -.
DR   Bgee; Q80SY4; -.
DR   CleanEx; MM_MIB1; -.
DR   Genevestigator; Q80SY4; -.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR   GO; GO:0001947; P:heart looping; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:MGI.
DR   GO; GO:0001841; P:neural tube formation; IMP:MGI.
DR   GO; GO:0007219; P:Notch signaling pathway; IMP:MGI.
DR   GO; GO:0045807; P:positive regulation of endocytosis; IDA:MGI.
DR   GO; GO:0001756; P:somitogenesis; IMP:MGI.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR010606; Mib_Herc2.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR000433; Znf_ZZ.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 2.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00023; Ank; 5.
DR   Pfam; PF06701; MIB_HERC2; 2.
DR   Pfam; PF00569; ZZ; 1.
DR   SMART; SM00248; ANK; 9.
DR   SMART; SM00184; RING; 3.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF48403; ANK; 2.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 6.
DR   PROSITE; PS51416; MIB_HERC2; 2.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 3.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Cell membrane; Coiled coil; Cytoplasm; Ligase; Membrane;
KW   Metal-binding; Notch signaling pathway; Repeat; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1   1006       E3 ubiquitin-protein ligase MIB1.
FT                                /FTId=PRO_0000055944.
FT   DOMAIN        6     74       MIB/HERC2 1.
FT   DOMAIN      143    221       MIB/HERC2 2.
FT   REPEAT      430    460       ANK 1.
FT   REPEAT      463    492       ANK 2.
FT   REPEAT      496    525       ANK 3.
FT   REPEAT      529    558       ANK 4.
FT   REPEAT      562    591       ANK 5.
FT   REPEAT      595    627       ANK 6.
FT   REPEAT      631    661       ANK 7.
FT   REPEAT      665    694       ANK 8.
FT   REPEAT      698    729       ANK 9.
FT   ZN_FING      79    126       ZZ-type.
FT   ZN_FING     819    854       RING-type 1.
FT   ZN_FING     866    901       RING-type 2.
FT   ZN_FING     963    996       RING-type 3.
FT   COILED      935    962       Potential.
FT   CONFLICT    742    742       L -> F (in Ref. 4; BAC38042).
FT   CONFLICT    907    907       R -> K (in Ref. 3; AAN18022/AAX84653).
SQ   SEQUENCE   1006 AA;  110088 MW;  5A8FE2A1BEE638DE CRC64;
     MSNSRNNRVM VEGVGARVVR GPDWKWGKQD GGEGHVGTVR SFESPEEVVV VWDNGTAANY
     RCSGAYDLRI LDSAPTGIKH DGTMCDTCRQ QPIIGIRWKC AECTNYDLCT VCYHGDKHHL
     RHRFYRITTP GSERVLLESR RKSKKITARG IFAGARVVRG VDWQWEDQDG GNGRRGKVTE
     IQDWSASSPH SAAYVLWDNG AKNLYRVGFE GMSDLKCVQD AKGGSFYRDH CPVLGEQNGN
     RNPGGLQIGD LVNIDLDLEI VQSLQHGHGG WTDGMFETLT TTGTVCGIDE DHDIVVQYPS
     GNRWTFNPAV LTKANIVRSG DAAQGAEGGT SQFQVGDLVQ VCYDLERIKL LQRGHGEWAE
     AMLPTLGKVG RVQQIYSDSD LKVEVCGTSW TYNPAAVSKV APAGSAISNA SGERLSQLLK
     KLFETQESGD LNEELVKAAA NGDVAKVEDL LKRPDVDVNG QCAGHTAMQA ASQNGHVDIL
     KLLLKQNVDV EAEDKDGDRA VHHAAFGDEG AVIEVLHRGS ADLNARNKRR QTPLHIAVNK
     GHLQVVKTLL DFGCHPSLQD SEGDTPLHDA ISKKRDDILA VLLEAGADVT ITNNNGFNAL
     HHAALRGNPS AMRVLLSKLP RPWIVDEKKD DGYTALHLAA LNNHVEVAEL LVHQGNANLD
     IQNVNQQTAL HLAVERQHTQ IVRLLVRAGA KLDIQDKDGD TPLHEALRHH TLSQLRQLQD
     MQDVGKVDAA WEPSKNTLIM GLGTQGAEKK SAASIACFLA ANGADLSIRN KKGQSPLDLC
     PDPSLCKALA KCHKEKVSGQ VGSRSPSMIS NDSETLEECM VCSDMKRDTL FGPCGHIATC
     SLCSPRVKKC LICKEQVQSR TKIEECVVCS DKKAAVLFQP CGHMCACENC ASLMKKCVQC
     RAVVERRVPF ITCCGGKSSE DPSDEISSGN IPVLQKDKDN TNVNADVQKL QQQLQDIKEQ
     TMCPVCLDRL KNMIFLCGHG TCQLCGDRMS ECPICRKAIE RRILLY
//
ID   GABR2_MOUSE             Reviewed;         940 AA.
AC   Q80T41; A2AL05;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Gamma-aminobutyric acid type B receptor subunit 2;
DE            Short=GABA-B receptor 2;
DE            Short=GABA-B-R2;
DE            Short=GABA-BR2;
DE            Short=GABABR2;
DE            Short=Gb2;
DE   AltName: Full=G-protein coupled receptor 51;
DE   Flags: Precursor;
GN   Name=Gabbr2; Synonyms=Gm425, Gpr51;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 869-940.
RX   MEDLINE=22584407; PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA   Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA   Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA   Bergmann J.E., Gaitanaris G.A.;
RT   "The G protein-coupled receptor repertoires of human and mouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
CC   -!- FUNCTION: Receptor for GABA. The activity of this receptor is
CC       mediated by G-proteins that inhibit adenylyl cyclase activity,
CC       stimulates phospholipase A2, activates potassium channels,
CC       inactivates voltage-dependent calcium-channels and modulates
CC       inositol phospholipids hydrolysis. Plays a critical role in the
CC       fine-tuning of inhibitory synaptic transmission. Pre-synaptic
CC       GABA-B-R inhibit neurotransmitter release by down-regulating high-
CC       voltage activated calcium channels, whereas postsynaptic GABA-B-R
CC       decrease neuronal excitability by activating a prominent inwardly
CC       rectifying potassium (Kir) conductance that underlies the late
CC       inhibitory postsynaptic potentials. Not only implicated in
CC       synaptic inhibition but also in hippocampal long-term
CC       potentiation, slow wave sleep, muscle relaxation and
CC       antinociception (By similarity).
CC   -!- SUBUNIT: Heterodimer of GABA-B-R1 and GABA-B-R2. Neither of which
CC       is effective on its own and homodimeric assembly does not seem to
CC       happen. Interacts with ATF4 via its C-terminal region (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity). Cell junction, synapse, postsynaptic cell
CC       membrane; Multi-pass membrane protein (By similarity).
CC       Note=Moreover coexpression of GABA-B-R1 and GABA-B-R2 appears to
CC       be a prerequisite for maturation and transport of GABA-B-R1 to the
CC       plasma membrane (By similarity).
CC   -!- DOMAIN: Alpha-helical parts of the C-terminal intracellular region
CC       mediate heterodimeric interaction with GABA-B receptor 1 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC       GABA-B receptor subfamily.
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DR   EMBL; AL772399; CAM17855.1; -; Genomic_DNA.
DR   EMBL; AL831741; CAM17855.1; JOINED; Genomic_DNA.
DR   EMBL; AL844224; CAM17855.1; JOINED; Genomic_DNA.
DR   EMBL; BX005247; CAM17855.1; JOINED; Genomic_DNA.
DR   EMBL; BX571848; CAM17855.1; JOINED; Genomic_DNA.
DR   EMBL; AL831741; CAM21407.1; -; Genomic_DNA.
DR   EMBL; AL772399; CAM21407.1; JOINED; Genomic_DNA.
DR   EMBL; AL844224; CAM21407.1; JOINED; Genomic_DNA.
DR   EMBL; BX005247; CAM21407.1; JOINED; Genomic_DNA.
DR   EMBL; BX571848; CAM21407.1; JOINED; Genomic_DNA.
DR   EMBL; BX005247; CAM22528.1; -; Genomic_DNA.
DR   EMBL; AL772399; CAM22528.1; JOINED; Genomic_DNA.
DR   EMBL; AL831741; CAM22528.1; JOINED; Genomic_DNA.
DR   EMBL; AL844224; CAM22528.1; JOINED; Genomic_DNA.
DR   EMBL; BX571848; CAM22528.1; JOINED; Genomic_DNA.
DR   EMBL; BX571848; CAM27679.1; -; Genomic_DNA.
DR   EMBL; AL772399; CAM27679.1; JOINED; Genomic_DNA.
DR   EMBL; AL831741; CAM27679.1; JOINED; Genomic_DNA.
DR   EMBL; AL844224; CAM27679.1; JOINED; Genomic_DNA.
DR   EMBL; BX005247; CAM27679.1; JOINED; Genomic_DNA.
DR   EMBL; AL844224; CAM27833.1; -; Genomic_DNA.
DR   EMBL; AL772399; CAM27833.1; JOINED; Genomic_DNA.
DR   EMBL; AL831741; CAM27833.1; JOINED; Genomic_DNA.
DR   EMBL; BX005247; CAM27833.1; JOINED; Genomic_DNA.
DR   EMBL; BX571848; CAM27833.1; JOINED; Genomic_DNA.
DR   EMBL; AY255605; AAO85117.1; -; mRNA.
DR   IPI; IPI00409336; -.
DR   RefSeq; NP_001074610.1; NM_001081141.1.
DR   UniGene; Mm.101909; -.
DR   ProteinModelPortal; Q80T41; -.
DR   STRING; Q80T41; -.
DR   PhosphoSite; Q80T41; -.
DR   PRIDE; Q80T41; -.
DR   Ensembl; ENSMUST00000107749; ENSMUSP00000103378; ENSMUSG00000039809.
DR   GeneID; 242425; -.
DR   KEGG; mmu:242425; -.
DR   CTD; 242425; -.
DR   MGI; MGI:2386030; Gabbr2.
DR   eggNOG; maNOG12479; -.
DR   GeneTree; ENSGT00530000063129; -.
DR   HOGENOM; HBG444485; -.
DR   HOVERGEN; HBG080355; -.
DR   InParanoid; Q80T41; -.
DR   OMA; HENIDDV; -.
DR   OrthoDB; EOG4PG606; -.
DR   NextBio; 385343; -.
DR   Bgee; Q80T41; -.
DR   CleanEx; MM_GABBR2; -.
DR   Genevestigator; Q80T41; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR000337; GPCR_3.
DR   InterPro; IPR017978; GPCR_3_C.
DR   InterPro; IPR017979; GPCR_3_CS.
DR   InterPro; IPR002455; GPCR_3_GABA_rcpt_B.
DR   InterPro; IPR002457; GPCR_3_GABA_rcpt_B2.
DR   Pfam; PF00003; 7tm_3; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   PRINTS; PR01178; GABAB2RECPTR.
DR   PRINTS; PR01176; GABABRECEPTR.
DR   PRINTS; PR00248; GPCRMGR.
DR   PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; FALSE_NEG.
DR   PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; FALSE_NEG.
DR   PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
DR   PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Coiled coil; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Phosphoprotein; Postsynaptic cell membrane;
KW   Receptor; Signal; Synapse; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     40       Potential.
FT   CHAIN        41    940       Gamma-aminobutyric acid type B receptor
FT                                subunit 2.
FT                                /FTId=PRO_0000306250.
FT   TOPO_DOM     41    482       Extracellular (Potential).
FT   TRANSMEM    483    503       Helical; Name=1; (Potential).
FT   TOPO_DOM    504    521       Cytoplasmic (Potential).
FT   TRANSMEM    522    542       Helical; Name=2; (Potential).
FT   TOPO_DOM    543    550       Extracellular (Potential).
FT   TRANSMEM    551    571       Helical; Name=3; (Potential).
FT   TOPO_DOM    572    596       Cytoplasmic (Potential).
FT   TRANSMEM    597    617       Helical; Name=4; (Potential).
FT   TOPO_DOM    618    653       Extracellular (Potential).
FT   TRANSMEM    654    674       Helical; Name=5; (Potential).
FT   TOPO_DOM    675    690       Cytoplasmic (Potential).
FT   TRANSMEM    691    711       Helical; Name=6; (Potential).
FT   TOPO_DOM    712    719       Extracellular (Potential).
FT   TRANSMEM    720    740       Helical; Name=7; (Potential).
FT   TOPO_DOM    741    940       Cytoplasmic (Potential).
FT   COILED      781    818       Potential.
FT   COMPBIAS      4     54       Pro-rich.
FT   MOD_RES     883    883       Phosphoserine (By similarity).
FT   CARBOHYD     89     89       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    297    297       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    388    388       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    403    403       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    452    452       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   940 AA;  105666 MW;  B364DC0A54EE9206 CRC64;
     MASPPSSGQP RPPPPPPPPA RLLLPLLLSL LLSLAPGAWG WARGAPRPPP SSPPLSIMGL
     MPLTKEVAKG SIGRGVLPAV ELAIEQIRNE SLLRPYFLDL RLYDTECDNA KGLKAFYDAI
     KYGPNHLMVF GGVCPSVTSI IAESLQGWNL VQLSFAATTP VLADKKKYPY FFRTVPSDNA
     VNPAILKLLK HFRWRRVGTL TQDVQRFSEV RNDLTGVLYG EDIEISDTES FSNDPCTSVK
     KLKGNDVRII LGQFDQNMAA KVFCCAFEES MFGSKYQWII PGWYEPAWWE QVHVEANSSR
     CLRRSLLAAM EGYIGVDFEP LSSKQIKTIS GKTPQQYERE YNSKRSGVGP SKFHGYAYDG
     IWVIAKTLQR AMETLHASSR HQRIQDFNYT DHTLGRIILN AMNETNFFGV TGQVVFRNGE
     RMGTIKFTQF QDSREVKVGE YNAVADTLEI INDTIRFQGS EPPKDKTIIL EQLRKISLPL
     YSILSALTIL GMIMASAFLF FNIKNRNQKL IKMSSPYMNN LIILGGMLSY ASIFLFGLDG
     SFVSEKTFET LCTVRTWILT VGYTTAFGAM FAKTWRVHAI FKNVKMKKKI IKDQKLLVIV
     GGMLLIDLCI LICWQAVDPL RRTVERYSME PDPAGRDISI RPLLEHCENT HMTIWLGIVY
     AYKGLLMLFG CFLAWETRNV SIPALNDSKY IGMSVYNVGI MCIIGAAVSF LTRDQPNVQF
     CIVALVIIFC STITLCLVFV PKLITLRTNP DAATQNRRFQ FTQNQKKEDS KTSTSVTSVN
     QASTSRLEGL QSENHRLRMK ITELDKDLEE VTMQLQDTPE KTTYIKQNHY QELNDILSLG
     NFTESTDGGK AILKNHLDQN PQLQWNTTEP SRTCKDPIED INSPEHIQRR LSLQLPILHH
     AYLPSIGGVD ASCVSPCVSP TASPRHRHVP PSFRVMVSGL
//
ID   GP101_MOUSE             Reviewed;         511 AA.
AC   Q80T62; Q3UUI9;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Probable G-protein coupled receptor 101;
GN   Name=Gpr101; Synonyms=Gm365;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 141-217.
RX   MEDLINE=22584407; PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA   Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA   Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA   Bergmann J.E., Gaitanaris G.A.;
RT   "The G protein-coupled receptor repertoires of human and mouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
CC   -!- FUNCTION: Orphan receptor.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK138185; BAE23572.1; -; mRNA.
DR   EMBL; AK138370; BAE23636.1; -; mRNA.
DR   EMBL; AY255576; AAO85088.1; -; mRNA.
DR   IPI; IPI00664250; -.
DR   RefSeq; NP_001028532.1; NM_001033360.3.
DR   UniGene; Mm.336070; -.
DR   UniGene; Mm.481815; -.
DR   ProteinModelPortal; Q80T62; -.
DR   SMR; Q80T62; 116-147.
DR   STRING; Q80T62; -.
DR   PRIDE; Q80T62; -.
DR   Ensembl; ENSMUST00000057645; ENSMUSP00000058183; ENSMUSG00000036357.
DR   GeneID; 245424; -.
DR   KEGG; mmu:245424; -.
DR   UCSC; uc009thn.1; mouse.
DR   CTD; 245424; -.
DR   MGI; MGI:2685211; Gpr101.
DR   GeneTree; ENSGT00590000083050; -.
DR   HOGENOM; HBG127496; -.
DR   HOVERGEN; HBG051766; -.
DR   InParanoid; Q80T62; -.
DR   OMA; THLFAFA; -.
DR   OrthoDB; EOG4VT5XK; -.
DR   NextBio; 386691; -.
DR   ArrayExpress; Q80T62; -.
DR   Bgee; Q80T62; -.
DR   CleanEx; MM_GPR101; -.
DR   Genevestigator; Q80T62; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Receptor; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    511       Probable G-protein coupled receptor 101.
FT                                /FTId=PRO_0000069602.
FT   TOPO_DOM      1     35       Extracellular (Potential).
FT   TRANSMEM     36     56       Helical; Name=1; (Potential).
FT   TOPO_DOM     57     67       Cytoplasmic (Potential).
FT   TRANSMEM     68     90       Helical; Name=2; (Potential).
FT   TOPO_DOM     91    106       Extracellular (Potential).
FT   TRANSMEM    107    127       Helical; Name=3; (Potential).
FT   TOPO_DOM    128    149       Cytoplasmic (Potential).
FT   TRANSMEM    150    170       Helical; Name=4; (Potential).
FT   TOPO_DOM    171    196       Extracellular (Potential).
FT   TRANSMEM    197    217       Helical; Name=5; (Potential).
FT   TOPO_DOM    218    398       Cytoplasmic (Potential).
FT   TRANSMEM    399    419       Helical; Name=6; (Potential).
FT   TOPO_DOM    420    432       Extracellular (Potential).
FT   TRANSMEM    433    453       Helical; Name=7; (Potential).
FT   TOPO_DOM    454    511       Cytoplasmic (Potential).
FT   CARBOHYD      7      7       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     13     13       N-linked (GlcNAc...) (Potential).
FT   DISULFID    104    182       By similarity.
SQ   SEQUENCE   511 AA;  56245 MW;  0E224DE2FA43C7E6 CRC64;
     MPPSCTNSTQ ENNGSRVCLP LSKMPISVAH GIIRSVVLLV ILGVAFLGNV VLGYVLHRKP
     NLLQVTNRFI FNLLVTDLLQ VALVAPWVVS TAIPFFWPLN IHFCTALVSL THLFAFASVN
     TIVVVSVDRY LTIIHPLSYP SKMTNRRSYI LLYGTWIAAF LQSTPPLYGW GHATFDDRNA
     FCSMIWGASP AYTVVSVVSF LVIPLGVMIA CYSVVFGAAR RQQALLYKAK SHRLEVRVED
     SVVHENEEGA KKRDEFQDKN EFQGQDGGGQ AEAKGSSSME ESPMVAEGSS QKTGKGSLDF
     SAGIMEGKDS DEVSNGSMEG LEVITEFQAS SAKADTGRID ANQCNIDVGE DDVEFGMDEI
     HFNDDVEAMR IPESSPPSRR NSTSDPPLPP CYECKAARVI FVIISTYVLS LGPYCFLAVL
     AVWVDIDTRV PQWVITIIIW LFFLQCCIHP YVYGYMHKSI KKEIQEVLKK LICKKSPPVE
     DSHPDLHETE AGTEGGIEGK AVPSHDSATS P
//
ID   VAT1L_MOUSE             Reviewed;         417 AA.
AC   Q80TB8; Q6PGM9;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Synaptic vesicle membrane protein VAT-1 homolog-like;
DE            EC=1.-.-.-;
GN   Name=Vat1l; Synonyms=Kiaa1576;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. Quinone oxidoreductase subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65809.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK122527; BAC65809.1; ALT_INIT; mRNA.
DR   EMBL; BC056927; AAH56927.1; -; mRNA.
DR   IPI; IPI00222759; -.
DR   RefSeq; NP_766604.2; NM_173016.3.
DR   UniGene; Mm.334825; -.
DR   ProteinModelPortal; Q80TB8; -.
DR   SMR; Q80TB8; 38-378.
DR   PhosphoSite; Q80TB8; -.
DR   PRIDE; Q80TB8; -.
DR   Ensembl; ENSMUST00000049509; ENSMUSP00000053431; ENSMUSG00000046844.
DR   GeneID; 270097; -.
DR   KEGG; mmu:270097; -.
DR   UCSC; uc009noa.1; mouse.
DR   CTD; 270097; -.
DR   MGI; MGI:2142534; Vat1l.
DR   HOGENOM; HBG753318; -.
DR   HOVERGEN; HBG002466; -.
DR   InParanoid; Q80TB8; -.
DR   OMA; QMIEKEA; -.
DR   OrthoDB; EOG4Q58PK; -.
DR   PhylomeDB; Q80TB8; -.
DR   NextBio; 393208; -.
DR   ArrayExpress; Q80TB8; -.
DR   Bgee; Q80TB8; -.
DR   Genevestigator; Q80TB8; -.
DR   GermOnline; ENSMUSG00000046844; Mus musculus.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR013149; ADH_C.
DR   InterPro; IPR013154; ADH_GroES-like.
DR   InterPro; IPR002085; ADH_SF_Zn.
DR   InterPro; IPR011032; GroES-like.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR002364; Quin_OxRdtase/zeta-crystal_CS.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   PANTHER; PTHR11695; ADH_Sf_Zn; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SUPFAM; SSF50129; GroES_like; 1.
DR   PROSITE; PS01162; QOR_ZETA_CRYSTAL; 1.
PE   2: Evidence at transcript level;
KW   Oxidoreductase.
FT   CHAIN         1    417       Synaptic vesicle membrane protein VAT-1
FT                                homolog-like.
FT                                /FTId=PRO_0000160923.
SQ   SEQUENCE   417 AA;  45817 MW;  604E25BDFC698CB2 CRC64;
     MAKEGVEKAE ETEQMIEKET SKEPAEGGDG SHRLGDAQEM RAVVLAGFGG LNKLRLSRKA
     MPEPQDGELK IRVKACGLNF IDLMVRQGNI DNPPKTPLVP GFECSGIVEA LGDSVKGYEI
     GDRVMAFVNY NAWAEVVCTP VEFVYKIPDD MSFSEAAAFP MNFVTAYTML FEIANLREGM
     SVLVHSAGGG VGQAVAQLCS TVPNVTVFGT ASTFKHEAIK DSVTHLFDRN ADYVQEVKRI
     SAEGVDIVLD CLCGDNTGKG LSLLKPLGTY ILYGSSNMVT GETKSFFSFA KSWWQVEKVN
     PIKLYEENKV IAGFSLLNLL FKQGRSGLIR GVVEKLIGLY NQKKIKPVVD SLWALEEVKE
     AMQRIHDRGN IGKLILDVEK TPTPLMANDS TETSEAGEEE EDHEGDSENK ERMPFIQ
//
ID   Q80TE2_MOUSE            Unreviewed;      1098 AA.
AC   Q80TE2;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   SubName: Full=MKIAA1400 protein;
DE   Flags: Fragment;
GN   Name=Pcdh10; Synonyms=mKIAA1400;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
CC   -!- FUNCTION: Potential calcium-dependent cell-adhesion protein. May
CC       be involved in the establishment and maintenance of specific
CC       neuronal connections in the brain (By similarity).
CC   -!- SIMILARITY: Contains 6 cadherin domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK122503; BAC65785.1; -; mRNA.
DR   IPI; IPI00849380; -.
DR   RefSeq; NP_001091641.1; NM_001098171.1.
DR   UniGene; Mm.242644; -.
DR   UniGene; Mm.473002; -.
DR   HSSP; P15116; 1NCJ.
DR   ProteinModelPortal; Q80TE2; -.
DR   STRING; Q80TE2; -.
DR   Ensembl; ENSMUST00000051181; ENSMUSP00000053795; ENSMUSG00000049100.
DR   GeneID; 18526; -.
DR   KEGG; mmu:18526; -.
DR   CTD; 18526; -.
DR   MGI; MGI:1338042; Pcdh10.
DR   HOGENOM; HBG447181; -.
DR   HOVERGEN; HBG054878; -.
DR   InParanoid; Q80TE2; -.
DR   NextBio; 294284; -.
DR   ArrayExpress; Q80TE2; -.
DR   Bgee; Q80TE2; -.
DR   Genevestigator; Q80TE2; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion; IDA:MGI.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR013164; Cadherin_N.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 6.
DR   Pfam; PF00028; Cadherin; 4.
DR   Pfam; PF08266; Cadherin_2; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 6.
DR   SUPFAM; SSF49313; Cadherin; 6.
DR   PROSITE; PS00232; CADHERIN_1; 5.
DR   PROSITE; PS50268; CADHERIN_2; 6.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell membrane; Membrane; Repeat;
KW   Transmembrane; Transmembrane helix.
FT   NON_TER       1      1
SQ   SEQUENCE   1098 AA;  119625 MW;  194842F7A31431CC CRC64;
     NEAKGIKILI QPQEPPPHAA HFYLYFLDYY YSFCGGGWGA VIGVAGWLQG SCFLFLLEMI
     VLLFFALLWM VDGVFSQLHY TVQEEQEHGT FVGNIAEDLG LDITKLSARR FQTVANSRTP
     YLDLNLETGV LYVNEKIDRE QICKQSPSCV LHLEVFLENP LELFRVEIEV LDINDNPPSF
     PEPDLTVEIS ESATPGTRFP LESAFDPDVG TNSLRDYEIT PNSYFSLDVQ TQGDGNRFAE
     LVLEKPLDRE QQAVHRYVLT AVDGGGGGGG GEGGGGGGGA GLPPQQQRTG TALLTIRVLD
     SNDNVPAFDQ PVYTVSLPEN SPPGTLVIQL NATDPDEGQN GEVVYSFSSH ISPRARELFG
     LSPRTGRLEV SGELDYEESP VYQVYVQAKD LGPNAVPAHC KVLVRVLDAN DNAPEISFST
     VKEAVSEGAA PGTVVALFSV TDRDSEENGQ VQCELLGDVP FRLKSSFKNY YTIVTEAPLD
     REAGDSYTLT VVARDRGEPA LSTSKSIQVQ VSDVNDNAPR FSQPVYDVYV TENNVPGAYI
     YAVSATDRDE GANAKLTYSI LECQIQGMSV FTYVSINSDN GYLYALRSFD YEQIKDFSFQ
     VEARDAGSPQ ALAGNATVNI LIVDQNDNAP AIVAPLPGRN GTPAREVLPR SAEPGYLLTR
     VAAVDADDGE NARLTYSIVR GNEMNLFRLD WRTGELRTAR RVPAKRDPQR PYELVIEVRD
     HGQPPLSSTA TLVVQLVDGA VEPQGGGGDR GGGSGEHLRP SRSGGGETSL DLTLILIIAL
     GSVSFIFLLA MIVLAVRCQK EKKLNIYTCL ASDCCLCCCC CGNGSSTCCG RQARARKKKL
     SKSDIMLVQS ANVPSNPAQV PVEESGGFGS HHHNQNYCYQ VCLTPESAKT DLMFLKPCSP
     SRSTDAEHNP CGAIVTGYSD QQPDIISNGS ILSNENKHQR AELSYLVDRP RRVNSSAFQE
     ADIVSSKDSG HGDSEQGDSD HDVTNRGQSA GMDLFSNCTE ECKALGHSDR CWMPSFVPSD
     GRQAADYRSN LHVPGMDSVP DTEVFEPPEV QPGAERSFST FGKEKALHGT LERKELDGLL
     SNTRAPYKPP YLTRKRIC
//
ID   SI1L2_MOUSE             Reviewed;        1722 AA.
AC   Q80TE4; Q6PDY1;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Signal-induced proliferation-associated 1-like protein 2;
DE            Short=SIPA1-like protein 2;
GN   Name=Sipa1l2; Synonyms=Kiaa0545;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 538-1722 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1406, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1245, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80TE4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80TE4-2; Sequence=VSP_016999;
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 Rap-GAP domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC058408; AAH58408.1; -; mRNA.
DR   EMBL; BC072593; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK122501; BAC65783.1; -; mRNA.
DR   IPI; IPI00125484; -.
DR   IPI; IPI00673176; -.
DR   UniGene; Mm.271668; -.
DR   UniGene; Mm.463243; -.
DR   ProteinModelPortal; Q80TE4; -.
DR   SMR; Q80TE4; 475-821, 950-1028.
DR   PhosphoSite; Q80TE4; -.
DR   PRIDE; Q80TE4; -.
DR   Ensembl; ENSMUST00000047850; ENSMUSP00000045483; ENSMUSG00000001995.
DR   Ensembl; ENSMUST00000108775; ENSMUSP00000104405; ENSMUSG00000001995.
DR   UCSC; uc009nye.1; mouse.
DR   UCSC; uc009nyf.1; mouse.
DR   MGI; MGI:2676970; Sipa1l2.
DR   eggNOG; roNOG14984; -.
DR   GeneTree; ENSGT00550000074284; -.
DR   HOGENOM; HBG445166; -.
DR   HOVERGEN; HBG056135; -.
DR   InParanoid; Q80TE4; -.
DR   OrthoDB; EOG4QNMV9; -.
DR   ArrayExpress; Q80TE4; -.
DR   Bgee; Q80TE4; -.
DR   CleanEx; MM_SIPA1L2; -.
DR   Genevestigator; Q80TE4; -.
DR   GermOnline; ENSMUSG00000001995; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR021818; DUF3401.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR000331; Rap_GAP.
DR   Pfam; PF11881; DUF3401; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF02145; Rap_GAP; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50085; RAPGAP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; GTPase activation; Phosphoprotein.
FT   CHAIN         1   1722       Signal-induced proliferation-associated
FT                                1-like protein 2.
FT                                /FTId=PRO_0000056750.
FT   DOMAIN      596    813       Rap-GAP.
FT   DOMAIN      951   1027       PDZ.
FT   COILED     1652   1712       Potential.
FT   COMPBIAS     53     56       Poly-Ser.
FT   COMPBIAS     58     64       Poly-Gly.
FT   COMPBIAS   1126   1129       Poly-Ser.
FT   COMPBIAS   1322   1366       Ser-rich.
FT   MOD_RES     149    149       Phosphoserine (By similarity).
FT   MOD_RES     161    161       Phosphoserine (By similarity).
FT   MOD_RES    1030   1030       Phosphoserine (By similarity).
FT   MOD_RES    1245   1245       Phosphoserine.
FT   MOD_RES    1406   1406       Phosphoserine.
FT   MOD_RES    1461   1461       Phosphoserine (By similarity).
FT   MOD_RES    1478   1478       Phosphoserine (By similarity).
FT   MOD_RES    1488   1488       Phosphoserine (By similarity).
FT   MOD_RES    1549   1549       Phosphoserine (By similarity).
FT   MOD_RES    1552   1552       Phosphoserine (By similarity).
FT   VAR_SEQ    1587   1605       Missing (in isoform 2).
FT                                /FTId=VSP_016999.
FT   CONFLICT   1361   1361       G -> S (in Ref. 2; BAC65783).
FT   CONFLICT   1649   1649       R -> Q (in Ref. 2; BAC65783).
SQ   SEQUENCE   1722 AA;  189370 MW;  39FEBBC8FB14B4DF CRC64;
     MSDPRPSQAE KHKLGRAAAK LKDPSRTMQA DDYFARKFKA INGSMGPATL NTSSSSEGGG
     GGGGPANGTP AVPKMGVRAR VSEWPPKKDC SKDLACKTLW ESRSQSSYES VTSIIQNGQN
     DQGDRQPEEQ LDLDFVEAKY TIGDIFVHSP QRGLHPIRQR SNSDITISDI DTEDVLDQHA
     VNPNTGAALH REYGSTSSID RQGLSGENVF AMLRGYRIES YDPKVTGSFG FPDFFPCDTA
     ISPSLHAAAQ ISRGEFVRIS GLDYMDGGLL MGRDRDKPFK RRLKSESVET SLFRKLRAVK
     SEHETFKFTS DLEEGRLDRG IRPWSCQRCF AHYDVQSILF NINEAMATRA SVGKRKNITT
     GASAASQTPV PVGPAGGCES PLGSKEDLNS KENPDADEGD GKSNDLVLSC PYFRNETGGE
     GDRRIALSRA NSASFSSGES CSFESSLSSH CTNAGVSVLE VPRESQPIHR EKVKRYIIEH
     VDLGAYYYRK FFYGKEHQNY FGIDENLGPV AVSIRREKVE DPREKEGSQF NYRVAFRTSE
     LTTLRGAILE DAVPSTARHG TARGLPLKEV LEYVIPELSI QCLRQAANSP KVPEQLLKLD
     EQGLSFQHKI GILYCRAGQS TEEEMYNNET AGPAFEEFLD LLGQRVRLKG FSKYRAQLDN
     KTDSTGTHSL YTTYKDFELM FHVSTLLPYM PNNRQQLLRK RHIGNDIVTI VFQEPGALPF
     TPKNIRSHFQ HVFVIVKVHN PCTENVCYSV GVSRSKDVPP FGPPIPKGVT FPKSAVFRDF
     LLAKVINAEN AAHKSEKFRA MATRTRQEYL KDLAENFVTT ATVDTSAKFS FITLGAKKKE
     RVKPRKDAHL FSIGAIMWHV VARDFGQSAD IECLLGISNE FIMLIEKDSK NVVFNCSCRD
     VIGWTSGLVS IKAFYERGEC LLLSSVDNRS EDIREIVQRL LIVTRGCETV EMTLRRNGLG
     QLGFHVNFEG IVADVEPFGF AWKAGLRQGS RLVEICKVAV ATLTHEQMID LLRTSVTVKV
     VIIQPHEDGS PRRGCSELCR IPMVEYKLDS EGTPCEYKTP FRRNTTWHRV PTPALQPVSR
     ASPVPGTPDR LQCQPLLQQA QAAIPRSTSF DRKLPDGTRS SPSNQSSSSD PGPGGSGPWR
     PQVGYDGCPS PLLLEHQGPG SVECDGTGEQ EDLLEGGRLP ETKWHGPPSK VLSSYKERVL
     QKDGSCKESP NKLSHIGDKS CSSHSSSNTL SSNTSSNSDD KHFGSGDLMD PELLGLTYIK
     GASTDSGIDT TPCMPATILG PVHLTGSRSL MHSRAEQWAD AADVSVADDD PAKMYALHGY
     ASAISSSAAD GSMGDLSEVS SHSSGSQHSG SPSAHCSKST GSLDSSKGYI VTHGGGQQAP
     GAVTKPYHRQ GAANKYVIGW KKSEGSPPPE EPEVTECPRI YGEMDIMSTA TQHPAVVGDS
     VSETQHVLSK DDFLKLMLPD SPLVEEGRRK FSFYGNVSPR RSLYRTLSDE SVCSNRRGSS
     FASSRSSILE QALPNDILFS TTPPYHSTLP PRTHPAPSMG SLRNEFWFSD GSLSDKSKCA
     DPGLMPLPDT AAGLDWSHLV DAARAFEGLD SDEELGLLCH HASYLDQRVA SFCTLTDLQH
     GQELEGAPEL SLCVDPTSGK EFMDTPGERS PSTLTGKVNQ LELILRQLQT DLRKEKQDKA
     VLQAEVQHLR QDNMRLQEES QTATAQLRKF TEWFFSTIDK KA
//
ID   LRRC7_MOUSE             Reviewed;        1490 AA.
AC   Q80TE7;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Leucine-rich repeat-containing protein 7;
DE   AltName: Full=Densin-180;
DE   AltName: Full=Protein LAP1;
GN   Name=Lrrc7; Synonyms=Kiaa1365, Lap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-850; SER-933; SER-949
RP   AND SER-1392, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-850; THR-865; SER-949
RP   AND SER-1392, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: May be involved in the organization of synaptic cell-
CC       cell contacts.
CC   -!- SUBUNIT: Interacts with CAMKII and CTNND2/Catenin delta-2.
CC       Interacts with CNKSR2 and DLG4 and forms a complex with N-cadherin
CC       through CTNND2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the LAP (LRR and PDZ) protein family.
CC   -!- SIMILARITY: Contains 18 LRR (leucine-rich) repeats.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65780.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK122498; BAC65780.1; ALT_INIT; mRNA.
DR   IPI; IPI00831714; -.
DR   UniGene; Mm.132162; -.
DR   ProteinModelPortal; Q80TE7; -.
DR   SMR; Q80TE7; 21-408, 1381-1487.
DR   STRING; Q80TE7; -.
DR   PhosphoSite; Q80TE7; -.
DR   PRIDE; Q80TE7; -.
DR   Ensembl; ENSMUST00000029826; ENSMUSP00000029826; ENSMUSG00000028176.
DR   UCSC; uc008rvw.1; mouse.
DR   MGI; MGI:2676665; Lrrc7.
DR   GeneTree; ENSGT00600000084222; -.
DR   HOVERGEN; HBG052305; -.
DR   PhylomeDB; Q80TE7; -.
DR   ArrayExpress; Q80TE7; -.
DR   Bgee; Q80TE7; -.
DR   CleanEx; MM_LRRC7; -.
DR   Genevestigator; Q80TE7; -.
DR   GermOnline; ENSMUSG00000028176; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF00560; LRR_1; 3.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS51450; LRR; 15.
DR   PROSITE; PS50106; PDZ; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Leucine-rich repeat; Phosphoprotein; Repeat.
FT   CHAIN         1   1490       Leucine-rich repeat-containing protein 7.
FT                                /FTId=PRO_0000188299.
FT   REPEAT       21     44       LRR 1.
FT   REPEAT       45     68       LRR 2.
FT   REPEAT       70     90       LRR 3.
FT   REPEAT       91    114       LRR 4.
FT   REPEAT      116    136       LRR 5.
FT   REPEAT      137    159       LRR 6.
FT   REPEAT      160    182       LRR 7.
FT   REPEAT      183    208       LRR 8.
FT   REPEAT      210    228       LRR 9.
FT   REPEAT      229    251       LRR 10.
FT   REPEAT      252    274       LRR 11.
FT   REPEAT      275    298       LRR 12.
FT   REPEAT      300    320       LRR 13.
FT   REPEAT      321    344       LRR 14.
FT   REPEAT      346    366       LRR 15.
FT   REPEAT      367    390       LRR 16.
FT   REPEAT      393    416       LRR 17.
FT   REPEAT      947    970       LRR 18.
FT   DOMAIN     1398   1488       PDZ.
FT   MOD_RES      90     90       Phosphoserine (By similarity).
FT   MOD_RES     197    197       Phosphoserine (By similarity).
FT   MOD_RES     850    850       Phosphoserine.
FT   MOD_RES     865    865       Phosphothreonine.
FT   MOD_RES     933    933       Phosphoserine.
FT   MOD_RES     949    949       Phosphoserine.
FT   MOD_RES    1392   1392       Phosphoserine.
SQ   SEQUENCE   1490 AA;  166901 MW;  A27F2892981A2982 CRC64;
     MTTKRKLIGR LVPCRCFRGE EEIISVLDYS HCSLQQVPKE VFNFERTLEE LYLDANQIEE
     LPKQLFNCQA LRKLSIPDND LSSLPTSIAS LVNLKELDIS KNGVQEFPEN IKCCKCLTII
     EASVNPISKL PDGFTQLLNL TQLYLNDAFL EFLPANFGRL VKLRILELRE NHLKTLPKSM
     HKLAQLERLD LGNNEFSELP EVLDQIQNLR ELWMDNNALQ VLPGSIGKLK MLVYLDMSKN
     RIETVDMDIS GCEALEDLLL SSNMLQQLPD SIGLLKKLTT LKVDDNQLTM LPNTIGNLSL
     LEEFDCSCNE LESLPPTIGY LHSLRTLAVD ENFLPELPRE IGSCKNVTVM SLRSNKLEFL
     PEEIGQMQRL RVLNLSDNRL KNLPFSFTKL KELAALWLSD NQSKALIPLQ TEAHPETKQR
     VLTNYMFPQQ PRGDEDFQSD SDSFNPTLWE EQRQQRMTVA FEFEDKKEDD ESAGKVKALS
     CQAPWDRGQR GITLQPARLS GDCCTPWARC DQQIQDMPVP QSDPQLAWGC ISGLQQERSM
     CAPLPVAAQS TTLPSLSGRQ VEINLKRYPT PYPEDLKNMV KSVQNLVGKP SHGVRVENSN
     PTANTEQTVK EKFEHKWPVA PKEITVEDSF VHPANEMRIG ELHPSLAETP LYPPKLVLLG
     KDKKESTDES EVDKTHCLNN SVSSGTYSDY SPSQASSASS NTRMKVGSLQ ATAKDAVHNS
     LWGNRIAPPF PQPLDAKPLL SQREAVPPGN IPQRPDRLPM SDAFPDNWTD GSHYDNTGFV
     SEEAAGENAN NNPLLSSKAR SVPAHGRRPL IRQERIVGVP LELEQSTHRH TPETEVPPSN
     PWQNWTRTPS PFEDRTAFPS KLETTPTTSP LPERKDHMKE PTETPGPFSP GVPWEYHDPT
     PNRSLGNVFS QIHCRPDSSK GVIAISKSTE RLSPLMKDIK SNKFKKSQSI DEIDVGTYKV
     YNIPLENYAS GSDHLGSHER PDKFLGPEHG MSSMSRSQSV PMLDDEMLMY GSSKGPPQQK
     ASMTKKVYQF DQSFNPQGAV EVKAEKRIPP PFAHNSEYVQ QPSKNIAKDL VSPRAYRGYP
     PMEQMFSFSQ PSVNEDAMVN AQFASQGPRA GFLRRADSLA SSTEMAMFRR VSEPHELPPG
     DRYGRATYRG GLEGQSSISM TDPQFLKRNG RYEDEHPSYQ EVKAQAGSFP AKNLTQRRPL
     SARSYSTESY GASQTRPVSA RPTMAALLEK IPSDYNLGNY GDKTSDNSDI KTRPTPVKGE
     ESCGKMPADW RQQLLRHIEA RRLDRTPSQQ SNILDNGQED VSPSGQWNPY PLGRRDVPPD
     TITKKAGSHI QTLMGSQSLQ HRSREQQPYE GNINKVTIQQ FQSPLPIQIP SSQATRGPQP
     GRCLIQTKGQ RSMDGYPEQF CVRIEKNPGL GFSISGGISG QGNPFKPSDK GIFVTRVQPD
     GPASNLLQPG DKILQANGHS FVHMEHEKAV LLLKSFQNTV DLVIQRELTV
//
ID   PCD19_MOUSE             Reviewed;        1145 AA.
AC   Q80TF3; Q8BL13;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   08-FEB-2011, entry version 74.
DE   RecName: Full=Protocadherin-19;
DE   Flags: Precursor;
GN   Name=Pcdh19; Synonyms=Kiaa1313;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-776.
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 177-1145.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
CC   -!- FUNCTION: Potential calcium-dependent cell-adhesion protein (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Contains 6 cadherin domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC32847.1; Type=Frameshift; Positions=32;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK046726; BAC32847.1; ALT_FRAME; mRNA.
DR   EMBL; AK122492; BAC65774.1; -; mRNA.
DR   IPI; IPI00750735; -.
DR   RefSeq; NP_001098715.1; NM_001105245.1.
DR   RefSeq; NP_001098716.1; NM_001105246.1.
DR   UniGene; Mm.39738; -.
DR   ProteinModelPortal; Q80TF3; -.
DR   SMR; Q80TF3; 22-668.
DR   PRIDE; Q80TF3; -.
DR   Ensembl; ENSMUST00000060309; ENSMUSP00000049889; ENSMUSG00000051323.
DR   GeneID; 279653; -.
DR   KEGG; mmu:279653; -.
DR   UCSC; uc009uew.1; mouse.
DR   CTD; 279653; -.
DR   MGI; MGI:2685563; Pcdh19.
DR   GeneTree; ENSGT00560000076797; -.
DR   HOGENOM; HBG447181; -.
DR   HOVERGEN; HBG054878; -.
DR   InParanoid; Q80TF3; -.
DR   NextBio; 394002; -.
DR   ArrayExpress; Q80TF3; -.
DR   Bgee; Q80TF3; -.
DR   CleanEx; MM_PCDH19; -.
DR   Genevestigator; Q80TF3; -.
DR   GermOnline; ENSMUSG00000051323; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR013164; Cadherin_N.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 6.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF08266; Cadherin_2; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 6.
DR   SUPFAM; SSF49313; Cadherin; 6.
DR   PROSITE; PS00232; CADHERIN_1; 5.
DR   PROSITE; PS50268; CADHERIN_2; 6.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane;
KW   Phosphoprotein; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     21       Potential.
FT   CHAIN        22   1145       Protocadherin-19.
FT                                /FTId=PRO_0000004004.
FT   TOPO_DOM     22    678       Extracellular (Potential).
FT   TRANSMEM    679    699       Helical; (Potential).
FT   TOPO_DOM    700   1145       Cytoplasmic (Potential).
FT   DOMAIN       22    129       Cadherin 1.
FT   DOMAIN      130    238       Cadherin 2.
FT   DOMAIN      239    346       Cadherin 3.
FT   DOMAIN      350    453       Cadherin 4.
FT   DOMAIN      454    563       Cadherin 5.
FT   DOMAIN      569    672       Cadherin 6.
FT   MOD_RES      37     37       Phosphothreonine (By similarity).
FT   CARBOHYD    261    261       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    420    420       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    485    485       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    546    546       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    570    570       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    676    676       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   1145 AA;  126064 MW;  A2EA69FEE95A2CF8 CRC64;
     MESLLLPVLL LLAVLWTQAA ALINLKYSVE EEQRAGTVIA NVAKDAREAG FALDPRQASA
     FRVVSNSAPH LVDINPSSGL LVTKQKIDRD LLCRQSPKCI ISLEVMSSSM EICDIKVEIK
     DLNDNAPTFP AAQIQLEISE AASPGTRIPL DSAYDPDSGS FGVQTYELTP NELFGLEIKT
     RGDGSRFAEL VVEKSLDRET QSHYSFRITA LDGGDPPHMG TVGLSIKVTD SNDNNPVFGE
     STYSVSVPEN SPPNTPVIRL NASDPDEGTN GQVVYSFYGY VNDRTRELFQ IDPHSGLVTV
     TGALDYEEGH VYELDVQAKD LGPNSIPAHC KVTVSVLDTN DNPPIINLLS VNSELVEVSE
     SAPPGYVIAL VRVSDRDSGL NGRVQCRLLG NVPFRLQEYE SFSTILVDGR LDREQHDQYN
     LTIQARDSGV PMLQSAKSFT VRITDENDNH PHFSKPYYQV IVQENNTPGA YLLSVSARDP
     DMGLNGSVSY QIVPSQVRDM PVFTYVSINP NSGDIYALRS FNHEQTKAFE FKVLAKDGGL
     PSLQSNATVR VIILDVNDNT PVITAPPLIN GTAEVYIPRN SGIGYLVTVV KADDYDEGEN
     GRVTYDMTEG DRGFFEIDQV NGEVRTTRTF NENSKPSYEL IVVAHDHGKT SLSASALVLI
     YLSPALDAQE SMGSVNLSLI FIIALGSIAG ILFVTMIFVA IKCKRDNKEI RTYNCSNCLT
     ITCLLGCFIK GQNSKCLHCI SVSPNSEEQD KKAEEKVSLR GKRIAEYSYG HQKKSSKKKK
     ISKNDIRLVP RDVEETDKMN VVSCSSLTSS LNYFDYHQQT LPLGCRRSES TFLNVENQNT
     RNTTASHIYH HSFNSQGPQQ PDLIINGVPL PETENYSFDS NYVNSRAHLI KSSSTFKDLE
     GNSLKDSGHE ESDQTDSEHD VQRSLYCDTA VNDVLNTSVT SMGSQMPDHD QNEGFHCREE
     CRILGHSDRC WMPRNPMPTR SKSPEHVRNI IALSIEATAA DVEAYDDCGP TKRTFATFGK
     DVSSHRAEER PILKGKRTVD VTICSPKVNS AIREAGNGCE AISPVTSPLH LKSPLPTKPS
     ISYTVALAPP AHDLEHHANS GASRPSEAEP RGADNEKVMH EVNPIRKDGR DKESPSVKRL
     KDIVL
//
ID   LRFN2_MOUSE             Reviewed;         788 AA.
AC   Q80TG9; B9EIF8; Q9CYK3;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Leucine-rich repeat and fibronectin type-III domain-containing protein 2;
DE   Flags: Precursor;
GN   Name=Lrfn2; Synonyms=Kiaa1246, Salm1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, INTERACTION WITH DLG4, DEVELOPMENTAL STAGE, TISSUE
RP   SPECIFICITY, GLYCOSYLATION, SUBCELLULAR LOCATION, TOPOLOGY, AND
RP   MUTAGENESIS OF 787-THR-VAL-788.
RX   PubMed=16828986; DOI=10.1016/j.gene.2006.05.014;
RA   Morimura N., Inoue T., Katayama K., Aruga J.;
RT   "Comparative analysis of structure, expression and PSD95-binding
RT   capacity of Lrfn, a novel family of neuronal transmembrane proteins.";
RL   Gene 380:72-83(2006).
CC   -!- FUNCTION: Promotes neurite outgrowth in hippocampal neurons.
CC       Enhances the cell surface expression of 2 NMDA receptor subunits
CC       GRIN1 and GRIN2A (By similarity). May play a role in
CC       redistributing DLG4 to the cell periphery.
CC   -!- SUBUNIT: Forms heteromeric complexes with LRFN1, LRFN3, LRFN4 and
CC       LRFN5. Can form homomeric complexes, but not across cell junctions
CC       (By similarity). Interacts with DLG4. Directly interacts with
CC       DLG1, DLG2 and DLG3 (By similarity). Directly interacts with 2
CC       NMDA receptor subunits GRIN1 and GRIN2A (By similarity).
CC   -!- INTERACTION:
CC       Q811D0:Dlg1; NbExp=2; IntAct=EBI-877092, EBI-514290;
CC       P70175:Dlg3; NbExp=1; IntAct=EBI-877092, EBI-396969;
CC       Q62108:Dlg4; NbExp=2; IntAct=EBI-877092, EBI-300895;
CC       P35439:Grin1 (xeno); NbExp=2; IntAct=EBI-877092, EBI-877897;
CC       P35439-1:Grin1 (xeno); NbExp=1; IntAct=EBI-877092, EBI-877923;
CC       P35439-4:Grin1 (xeno); NbExp=1; IntAct=EBI-877092, EBI-877935;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein. Cell junction, synapse. Cell junction, synapse,
CC       postsynaptic cell membrane (By similarity).
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in the brain, with a
CC       weak, but broad expression in the cerebral cortex and diencephalic
CC       nuclei. Strongly expressed in both the pyramidal layer and the
CC       dentate gyrus of the hippocampus. Also detected in other parts of
CC       the central nervous system, including the olfactory bulb, pons,
CC       cerebellum, and medulla oblongata, as well as in the peripheral
CC       nervous system, such as the ganglia of cranial nerves and the
CC       dorsal root ganglion during gestation.
CC   -!- DEVELOPMENTAL STAGE: Expression starts around 11.5-12.5 dpc. At
CC       11.5 dpc, detected in the outer layer of the telencephalic
CC       vesicles. This pattern of expression continues until 17.5 dpc with
CC       expression in the cortical plate, but not in the inner layer of
CC       the cerebral cortex, including subplate, ventricular zone, and
CC       subventricular zone. As also detected in the hippocampus, amygdala
CC       and widely in diencephalic nuclei.
CC   -!- DOMAIN: The PDZ-binding motif is required for cell surface
CC       expression, neurite outgrowth promotion and interaction with DLG1,
CC       DLG3 and DLG4 (By similarity).
CC   -!- PTM: Glycosylated.
CC   -!- SIMILARITY: Belongs to the LRFN family.
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC   -!- SIMILARITY: Contains 1 Ig-like (immunoglobulin-like) domain.
CC   -!- SIMILARITY: Contains 6 LRR (leucine-rich) repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65758.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; AK017594; BAB30828.1; -; mRNA.
DR   EMBL; AK044375; BAC31891.1; -; mRNA.
DR   EMBL; AK122476; BAC65758.1; ALT_INIT; mRNA.
DR   EMBL; CH466559; EDL23629.1; -; Genomic_DNA.
DR   EMBL; BC139418; AAI39419.1; -; mRNA.
DR   IPI; IPI00330152; -.
DR   RefSeq; NP_081728.2; NM_027452.3.
DR   UniGene; Mm.133607; -.
DR   UniGene; Mm.478631; -.
DR   ProteinModelPortal; Q80TG9; -.
DR   SMR; Q80TG9; 21-377, 419-501.
DR   IntAct; Q80TG9; 15.
DR   STRING; Q80TG9; -.
DR   PRIDE; Q80TG9; -.
DR   Ensembl; ENSMUST00000046254; ENSMUSP00000047573; ENSMUSG00000040490.
DR   GeneID; 70530; -.
DR   KEGG; mmu:70530; -.
DR   UCSC; uc008cyd.1; mouse.
DR   CTD; 70530; -.
DR   MGI; MGI:1917780; Lrfn2.
DR   GeneTree; ENSGT00600000084152; -.
DR   HOGENOM; HBG444166; -.
DR   HOVERGEN; HBG052352; -.
DR   InParanoid; Q80TG9; -.
DR   OMA; RMIPASN; -.
DR   OrthoDB; EOG469QT6; -.
DR   NextBio; 331801; -.
DR   ArrayExpress; Q80TG9; -.
DR   Bgee; Q80TG9; -.
DR   Genevestigator; Q80TG9; -.
DR   GermOnline; ENSMUSG00000040490; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR000372; LRR-contain_N.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00560; LRR_1; 1.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00369; LRR_TYP; 3.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00013; LRRNT; 1.
DR   SUPFAM; SSF49265; FN_III-like; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51450; LRR; 6.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Leucine-rich repeat; Membrane;
KW   Postsynaptic cell membrane; Repeat; Signal; Synapse; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21    788       Leucine-rich repeat and fibronectin type-
FT                                III domain-containing protein 2.
FT                                /FTId=PRO_0000014840.
FT   TOPO_DOM     21    534       Extracellular (Potential).
FT   TRANSMEM    535    555       Helical; (Potential).
FT   TOPO_DOM    556    788       Cytoplasmic (Potential).
FT   REPEAT       75     98       LRR 1.
FT   REPEAT       99    122       LRR 2.
FT   REPEAT      124    146       LRR 3.
FT   REPEAT      148    171       LRR 4.
FT   REPEAT      172    195       LRR 5.
FT   REPEAT      196    220       LRR 6.
FT   DOMAIN      289    375       Ig-like.
FT   DOMAIN      419    510       Fibronectin type-III.
FT   MOTIF       785    788       PDZ-binding.
FT   CARBOHYD     29     29       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    332    332       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    341    341       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    384    384       N-linked (GlcNAc...) (Potential).
FT   DISULFID    310    359       By similarity.
FT   MUTAGEN     787    788       Missing: Loss of DLG4-binding.
FT   CONFLICT     42     42       G -> R (in Ref. 1; BAB30828).
FT   CONFLICT    530    530       L -> K (in Ref. 1; BAB30828).
SQ   SEQUENCE   788 AA;  84963 MW;  65B70CA475E99D6B CRC64;
     METLLGGLLA FGMAFAVVDA CPKYCVCQNL SESLGTLCPS KGLLFVPPDI DRRTVELRLG
     GNFIIHIGRQ DFANMTGLVD LTLSRNTISH IQPFSFLDLE SLRSLHLDSN RLPSLGEDTL
     RGLVNLQHLI VNNNQLGGIA DDAFEDFLLT LEDLDLSYNN LHGLPWDSVR RMVNLHQLSL
     DHNLLDHIAE GTFADLQKLA RLDLTSNRLQ KLPPDPIFAR SQASLLTATP FAPPLSFSFG
     GNPLHCNCEL LWLRRLERDD DLETCGSPGS LKGRYFWHIR EEEFVCEPPL ITQHTHKLLV
     LEGQAATLKC KAIGDPSPLI HWVAPDDRLV GNSSRTAVYD NGTLDILITT SQDSGPFTCI
     AANAAGEATA TVEVSIVQLP HLSNSTSRMA PPKSRLSDIT GSSKTSRGGG GSGAGEPPKS
     TPERAVLVSD VTTTSALVKW SVSKSAPRVK MYQLQYNCSD DEVLIYRMIP ASNKAFVVNN
     LVSGTGYDLC VLAMWDDTAT TLTATNIVGC AQFFTKADYP QCQSMHSQIL GGTMILVIGG
     IIVATLLVFI VILMVRYKVC NHDTPGKMAA ATVSNVYSQT NGSQPPPLGG IPVGQLPQAP
     PKVVVRNELM DFSTSLARAC DSSSSSSLGS GEAAGLGRGP WRLPPPAPRP KPSLDRLMGA
     FASLDLKSQR KEELLDSRTP AGRGAGTSSR GHHSDREPLL GPPATRARSL LPLPLEGKAK
     RSHSFDMGDF AAAAAAVPGG YSPPRRVSNI WTKRSLSVNG MLLPFEESDL VGARGTFGSS
     EWVMESTV
//
ID   Q80TH1_MOUSE            Unreviewed;       950 AA.
AC   Q80TH1;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   SubName: Full=Discs, large homolog 3 (Drosophila), isoform CRA_c;
DE   SubName: Full=MKIAA1232 protein;
DE   Flags: Fragment;
GN   Name=Dlg3; Synonyms=Dlgh3, mKIAA1232; ORFNames=mCG_116782;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SIMILARITY: Contains 3 PDZ (DHR) domains.
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DR   EMBL; AK122474; BAC65756.1; -; mRNA.
DR   EMBL; CH466564; EDL14167.1; -; Genomic_DNA.
DR   IPI; IPI00136350; -.
DR   RefSeq; NP_001171249.1; NM_001177778.1.
DR   UniGene; Mm.4615; -.
DR   HSSP; Q12959; 1PDR.
DR   ProteinModelPortal; Q80TH1; -.
DR   STRING; Q80TH1; -.
DR   Ensembl; ENSMUST00000113736; ENSMUSP00000109365; ENSMUSG00000000881.
DR   GeneID; 53310; -.
DR   KEGG; mmu:53310; -.
DR   UCSC; uc009twn.1; mouse.
DR   CTD; 53310; -.
DR   MGI; MGI:1888986; Dlg3.
DR   GeneTree; ENSGT00560000076879; -.
DR   HOVERGEN; HBG107814; -.
DR   PhylomeDB; Q80TH1; -.
DR   ArrayExpress; Q80TH1; -.
DR   Bgee; Q80TH1; -.
DR   Genevestigator; Q80TH1; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR016313; M-assoc_guanylate_kinase.
DR   InterPro; IPR019590; MAGUK_PEST_N.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR019583; PDZ_assoc.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF10608; MAGUK_N_PEST; 1.
DR   Pfam; PF00595; PDZ; 3.
DR   Pfam; PF10600; PDZ_assoc; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PIRSF; PIRSF001741; MAGUK_DLGH; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 3.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50156; PDZ; 3.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 3.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   SH3 domain.
FT   NON_TER       1      1
SQ   SEQUENCE   950 AA;  103832 MW;  18E11E864B3EBDD8 CRC64;
     LHSDPSWGPE QKRFSPHLAF AWAPDSSLPL GLGPEATTGD TEPPVLEGEP WVRGSVGAEA
     PGRPPGPRPR SARAPPRVPP PSWSEQCECA REPGGGGGGV ETGVGWGVRA AGGSAMHKHQ
     HCCKCPECYE VTRLAALRRL EPPGYGDWQV PDPYGPSGGN GASSGYGGYS SQTLPSQAGA
     TPTPRTKAKL IPTGRDVGPV PPKPVPGKST PKLNGSGPGW WPECTCTNRD WYEQASPAPL
     LVNPEALEPS LSVNGSDGMF KYEEIVLERG NSGLGFSIAG GIDNPHVPDD PGIFITKIIP
     GGAAAMDGRL GVNDCVLRVN EVDVSEVVHS RAVEALKEAG PVVRLVVRRR QPPPETIMEV
     NLLKGPKGLG FSIAGGIGNQ HIPGDNSIYI TKIIEGGAAQ KDGRLQIGDR LLAVNNTNLQ
     DVRHEEAVAS LKNTSDMVYL KVAKPGSIHL NDMYAPPDYA STFTALADNH ISHNSSLGYL
     GAVESKVTYP APPQVPPTRY SPIPRHMLAE EDFTREPRKI ILHKGSTGLG FNIVGGEDGE
     GIFVSFILAG GPADLSGELR RGDRILSVNG VNLRNATHEQ AAAALKRAGQ SVTIVAQYRP
     EEYSRFESKI HDLREQMMNS SMSSGSGSLR TSEKRSLYVR ALFDYDRTRD SCLPSQGLSF
     SYGDILHVIN ASDDEWWQAR LVTPHGESEQ IGVIPSKKRV EKKERARLKT VKFHARTGMI
     ESNRDFPGLS DDYYGAKNLK GQEDAILSYE PVTRQEIHYA RPVIILGPMK DRVNDDLISE
     FPHKFGSCVP HTTRPRRDNE VDGQDYHFVV SREQMEKDIQ DNKFIEAGQF NDNLYGTSIQ
     SVRAVAERGK HCILDVSGNA IKRLQQAQLY PIAIFIKPKS IEALMEMNRR QTYEQANKIF
     DKAMKLEQEF GEYFTAIVQG DSLEEIYNKI KQIIEDQSGH YIWVPSPEKL
//
ID   LAP2_MOUSE              Reviewed;        1402 AA.
AC   Q80TH2; Q8BQ14; Q8CE41; Q8K171; Q99JU3; Q9JI47;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Protein LAP2;
DE   AltName: Full=Densin-180-like protein;
DE   AltName: Full=Erbb2-interacting protein;
DE            Short=Erbin;
GN   Name=Erbb2ip; Synonyms=Erbin, Kiaa1225, Lap2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 308-1376 (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Skin, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 721-1402 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1160-1402 (ISOFORM 1).
RC   TISSUE=Colon, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 908-1402 (ISOFORM 3).
RX   MEDLINE=20342794; PubMed=10878805; DOI=10.1038/35017038;
RA   Borg J.-P., Marchetto S., Le Bivic A., Ollendorff V.,
RA   Jaulin-Bastard F., Saito H., Fournier E., Adelaide J., Margolis B.,
RA   Birnbaum D.;
RT   "ERBIN: a basolateral PDZ protein that interacts with the mammalian
RT   ERBB2/HER2 receptor.";
RL   Nat. Cell Biol. 2:407-414(2000).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1097, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-850, PHOSPHORYLATION
RP   [LARGE SCALE ANALYSIS] AT SER-1231 AND SER-1234 (ISOFORM 2), AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-595; SER-599; SER-600;
RP   SER-712; SER-869 AND SER-1171, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599; SER-600; SER-712;
RP   SER-854 AND SER-1276, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Acts as an adapter for the receptor ERBB2, in epithelia.
CC       By binding the unphosphorylated ERBB2 'Tyr-1248' receptor, it may
CC       contribute to stabilize this unphosphorylated state (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with ERBB2, BPAG1 and ITGB4. May favor the
CC       localization of ERBB2, by restricting its presence to the
CC       basolateral membrane of epithelial cells. Also found to interact
CC       with ARVCF and delta catenin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, hemidesmosome (By
CC       similarity). Note=Found in hemidesmosomes, which are cell-
CC       substrate adhesion complexes in stratified epithelia. In
CC       transfected cells, either diffusely distributed over the cytoplasm
CC       or concentrated at the basolateral membrane (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=3;
CC         IsoId=Q80TH2-3; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q80TH2-1; Sequence=VSP_010809;
CC       Name=2;
CC         IsoId=Q80TH2-2; Sequence=VSP_010808;
CC         Note=Phosphorylated on Ser-1231 and Ser-1234;
CC   -!- PTM: Isoform 2 is phosphorylated on Ser-1231 and Ser-1234.
CC   -!- SIMILARITY: Belongs to the LAP (LRR and PDZ) protein family.
CC   -!- SIMILARITY: Contains 17 LRR (leucine-rich) repeats.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65755.1; Type=Erroneous initiation;
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DR   EMBL; AK122473; BAC65755.1; ALT_INIT; mRNA.
DR   EMBL; AK051733; BAC34742.1; -; mRNA.
DR   EMBL; AK029054; BAC26267.1; -; mRNA.
DR   EMBL; BC005691; AAH05691.3; -; mRNA.
DR   EMBL; BC028256; AAH28256.1; -; mRNA.
DR   EMBL; AF263743; AAF77047.1; -; mRNA.
DR   IPI; IPI00454039; -.
DR   IPI; IPI00457485; -.
DR   IPI; IPI00896710; -.
DR   RefSeq; NP_001005868.1; NM_001005868.1.
DR   RefSeq; NP_067538.2; NM_021563.2.
DR   UniGene; Mm.277354; -.
DR   ProteinModelPortal; Q80TH2; -.
DR   SMR; Q80TH2; 14-454, 1233-1402.
DR   MINT; MINT-138078; -.
DR   STRING; Q80TH2; -.
DR   PhosphoSite; Q80TH2; -.
DR   PRIDE; Q80TH2; -.
DR   Ensembl; ENSMUST00000022222; ENSMUSP00000022222; ENSMUSG00000021709.
DR   Ensembl; ENSMUST00000053927; ENSMUSP00000057956; ENSMUSG00000021709.
DR   Ensembl; ENSMUST00000091269; ENSMUSP00000088813; ENSMUSG00000021709.
DR   GeneID; 59079; -.
DR   KEGG; mmu:59079; -.
DR   UCSC; uc007rsl.1; mouse.
DR   UCSC; uc007rsm.1; mouse.
DR   CTD; 59079; -.
DR   MGI; MGI:1890169; Erbb2ip.
DR   eggNOG; roNOG10923; -.
DR   GeneTree; ENSGT00600000084222; -.
DR   HOVERGEN; HBG052305; -.
DR   OrthoDB; EOG41JZBG; -.
DR   NextBio; 314720; -.
DR   ArrayExpress; Q80TH2; -.
DR   Bgee; Q80TH2; -.
DR   CleanEx; MM_ERBB2IP; -.
DR   Genevestigator; Q80TH2; -.
DR   GermOnline; ENSMUSG00000021709; Mus musculus.
DR   GO; GO:0030056; C:hemidesmosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0006605; P:protein targeting; IDA:MGI.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF00560; LRR_1; 2.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS51450; LRR; 12.
DR   PROSITE; PS50106; PDZ; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Leucine-rich repeat;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1   1402       Protein LAP2.
FT                                /FTId=PRO_0000188302.
FT   REPEAT       21     44       LRR 1.
FT   REPEAT       45     68       LRR 2.
FT   REPEAT       70     90       LRR 3.
FT   REPEAT       91    114       LRR 4.
FT   REPEAT      116    136       LRR 5.
FT   REPEAT      137    159       LRR 6.
FT   REPEAT      160    183       LRR 7.
FT   REPEAT      185    208       LRR 8.
FT   REPEAT      210    228       LRR 9.
FT   REPEAT      229    252       LRR 10.
FT   REPEAT      254    274       LRR 11.
FT   REPEAT      275    298       LRR 12.
FT   REPEAT      300    320       LRR 13.
FT   REPEAT      321    344       LRR 14.
FT   REPEAT      346    366       LRR 15.
FT   REPEAT      367    390       LRR 16.
FT   REPEAT      754    775       LRR 17.
FT   DOMAIN     1311   1400       PDZ.
FT   COMPBIAS    928    931       Poly-Ser.
FT   MOD_RES     440    440       Phosphoserine (By similarity).
FT   MOD_RES     483    483       Phosphotyrosine (By similarity).
FT   MOD_RES     485    485       Phosphothreonine (By similarity).
FT   MOD_RES     487    487       Phosphotyrosine (By similarity).
FT   MOD_RES     595    595       Phosphoserine.
FT   MOD_RES     599    599       Phosphoserine.
FT   MOD_RES     600    600       Phosphoserine.
FT   MOD_RES     712    712       Phosphoserine.
FT   MOD_RES     730    730       Phosphotyrosine (By similarity).
FT   MOD_RES     794    794       Phosphoserine (By similarity).
FT   MOD_RES     850    850       Phosphothreonine.
FT   MOD_RES     854    854       Phosphoserine.
FT   MOD_RES     869    869       Phosphoserine.
FT   MOD_RES     914    914       Phosphothreonine (By similarity).
FT   MOD_RES     917    917       Phosphotyrosine (By similarity).
FT   MOD_RES     928    928       Phosphoserine (By similarity).
FT   MOD_RES     931    931       Phosphoserine (By similarity).
FT   MOD_RES     970    970       Phosphotyrosine (By similarity).
FT   MOD_RES     979    979       Phosphotyrosine (By similarity).
FT   MOD_RES    1058   1058       Phosphoserine (By similarity).
FT   MOD_RES    1097   1097       Phosphotyrosine.
FT   MOD_RES    1124   1124       Phosphotyrosine (By similarity).
FT   MOD_RES    1150   1150       Phosphoserine (By similarity).
FT   MOD_RES    1156   1156       Phosphotyrosine (By similarity).
FT   MOD_RES    1171   1171       Phosphoserine.
FT   MOD_RES    1261   1261       Phosphoserine (By similarity).
FT   MOD_RES    1276   1276       Phosphoserine.
FT   MOD_RES    1283   1283       Phosphotyrosine (By similarity).
FT   VAR_SEQ    1203   1203       K -> KSMLSRSFNSNLTAVSSSHYGSSRDLHGSQGSLALS
FT                                VADGRGSGGHIFR (in isoform 2).
FT                                /FTId=VSP_010808.
FT   VAR_SEQ    1243   1268       Missing (in isoform 1).
FT                                /FTId=VSP_010809.
FT   CONFLICT    721    723       DKK -> HAS (in Ref. 3; AAH28256).
FT   CONFLICT    908    910       VRS -> ASG (in Ref. 4; AAF77047).
SQ   SEQUENCE   1402 AA;  157232 MW;  42BEE5BDE4B8DE78 CRC64;
     MTTKRSLFVR LVPCRCLRGE EETVTTLDYS HCSLEQVPKE IFTFEKTLEE LYLDANQIEE
     LPKQLFNCQS LHKLSLPDND LTTLPASIAN LINLRELDVS KNGIQEFPEN IKNCKVLTIV
     EASVNPISKL PDGFSQLLNL TQLYLNDAFL EFLPANFGRL TKLQILELRE NQLKMLPKTM
     NRLTQLERLD LGSNEFTEVP EVLEQLSGLR EFWMDGNRLT FIPGFIGSLR QLTYLDVSKN
     NIEMVEEGIS TCENPQDFLL SSNSLQQLPE TIGSLKNVTT LKIDENQLMY LPDSIGGLRS
     IEELDCSFNE IEALPSSIGQ LTNMRTFAAD HNYLQQLPPE IGNWKNITVL FLHCNKLETL
     PEEMGDMQKL KVINLSDNRL KNLPFSFTKL QQLTAMWLSD NQSKPLIPLQ KETDTETQKM
     VLTNYMFPQQ PRTEDVMFIS DNESFNPALW EEQRKQRAQV AFECDEDKDE REAPPREGNL
     KRYPTPYPDE LKNMVKTVQT IVHRLKDEET NEESGRDLKQ HEDQQVVNKD KCVKTSESTT
     TKSKLDEREK YMNSVQKMSE PEAETNGGNL PVTASMKLSG NLKHIVNHDD VFEESEELSS
     DEEMKMAEMR PPLIESSINQ PKVVALSNNK KDDAKDADSL SDEVTHNSNQ NNSNCSSPSR
     MSDSVSLNTD SSQDTSLCSP VKQTPVDSNS KVRQEDENFN SLLQNGVNLN NSPEEKFKIN
     DKKDFKLPEY DLNIEEQLVL IEKDIDSKAT SDDSRQLDHI NMNINKLVTN NIFQPEVMER
     SKMQDIVLGT GFLSIHPKNE AEHIENGAKF PNLESINKVN GLCEDTAPSP GRVEPQKASS
     SADVGISKST EDLSPQRSGP TGAVVKSHSI TNMETGGLKI YDILGDDGPQ PPSAAVKIAS
     AVDGKNIVRS KSATLLYDQP LQVFTAASSS SELLSGTKAV FKFDSNHNPE EPDIIRAATV
     SGPQSTPHLY GPPQYNVQYS GSATVKDTLW HPKQNPQIDP VSFPPQRLPR SESAENHSYA
     KHSANMNFSN HNNVRANTGY HLQQRLAPAR HGEMWAISPN DRLVPAVTRT TIQRQSSVSS
     TASVNLGDPT RRTEGDYLSY RELHSMGRTP VMSGSQRPLS ARAYSIDGPN TSRPQSARPS
     INEIPERTMS VSDFNYSRTS PSKRPNTRVG SEHSLLDPPG KSKVPHDWRE QVLRHIEAKK
     LEKHPQTSSP GECCQDDRFM SEEQNHPSGA LSHRGLPDSL MKMPLSNGQM GQPLRPQAHY
     SQTHHPPQAS VARHPSREQL IDYLMLKVAH QPPYTHPHCS PRQGHELAKQ EIRVRVEKDP
     ELGFSISGGV GGRGNPFRPD DDGIFVTRVQ PEGPASKLLQ PGDKIIQANG YSFINIEHGQ
     AVSLLKTFHN AVDLIIVREV SS
//
ID   Q80TH9_MOUSE            Unreviewed;       284 AA.
AC   Q80TH9;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 39.
DE   SubName: Full=MKIAA1203 protein;
DE   Flags: Fragment;
GN   Name=Usp31; Synonyms=mKIAA1203;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
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DR   EMBL; AK122466; BAC65748.1; -; mRNA.
DR   IPI; IPI00762403; -.
DR   UniGene; Mm.122538; -.
DR   MEROPS; C19.071; -.
DR   PhosphoSite; Q80TH9; -.
DR   Ensembl; ENSMUST00000046929; ENSMUSP00000040037; ENSMUSG00000063317.
DR   MGI; MGI:1923429; Usp31.
DR   eggNOG; roNOG04751; -.
DR   GeneTree; ENSGT00600000084034; -.
DR   InParanoid; Q80TH9; -.
DR   OMA; LDSAIPV; -.
DR   OrthoDB; EOG43TZTQ; -.
DR   ArrayExpress; Q80TH9; -.
DR   Bgee; Q80TH9; -.
DR   Genevestigator; Q80TH9; -.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   284 AA;  30089 MW;  1D7C9C961E835ADE CRC64;
     MKPARCRSKA DSSRTSGRHS SSSSTQPKKE SSPRSQESMS SPSPQKQKSA SAFTYSSSSI
     SAKKAPSPVT RGPFPSGKSR TSDRSLSREG SRQSLGSDRA SVTSTSTSKP SSPRVNQARA
     GDNRVDGKHV RSSSMASLRS PSTSVRSGLK RDSKSEDKGL SFFKSALRQK ETRRSTDLGK
     TTLLSKKAGG SSVKSVSKNT ADDKTEKGHQ PPGSQQPNTN AVGKEQLVSK DPAKHSLLSA
     RRSKSSQLDS GAPLSPSSRS TTEKGSKKLS SSMQTSARPS QKPQ
//
ID   GRM1B_MOUSE             Reviewed;         738 AA.
AC   Q80TI0; Q6NS56; Q8BZZ1; Q9CTQ2;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   08-FEB-2011, entry version 49.
DE   RecName: Full=GRAM domain-containing protein 1B;
GN   Name=Gramd1b; Synonyms=Kiaa1201;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-158 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Retina, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q80TI0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80TI0-2; Sequence=VSP_025473;
CC       Name=3;
CC         IsoId=Q80TI0-3; Sequence=VSP_025474;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q80TI0-4; Sequence=VSP_025475, VSP_025476;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 GRAM domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65747.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK122465; BAC65747.1; ALT_INIT; mRNA.
DR   EMBL; AK020827; BAB32220.1; -; mRNA.
DR   EMBL; AK033156; BAC28174.1; -; mRNA.
DR   EMBL; BC070451; AAH70451.1; -; mRNA.
DR   IPI; IPI00227757; -.
DR   IPI; IPI00845535; -.
DR   IPI; IPI00845682; -.
DR   IPI; IPI00845844; -.
DR   RefSeq; NP_766356.1; NM_172768.1.
DR   UniGene; Mm.138434; -.
DR   PhosphoSite; Q80TI0; -.
DR   PRIDE; Q80TI0; -.
DR   Ensembl; ENSMUST00000121357; ENSMUSP00000112564; ENSMUSG00000040111.
DR   GeneID; 235283; -.
DR   KEGG; mmu:235283; -.
DR   UCSC; uc009ozp.1; mouse.
DR   CTD; 235283; -.
DR   MGI; MGI:1925037; Gramd1b.
DR   eggNOG; roNOG04687; -.
DR   GeneTree; ENSGT00580000081380; -.
DR   HOVERGEN; HBG062004; -.
DR   OMA; AEVITHD; -.
DR   NextBio; 382563; -.
DR   ArrayExpress; Q80TI0; -.
DR   Bgee; Q80TI0; -.
DR   CleanEx; MM_GRAMD1B; -.
DR   Genevestigator; Q80TI0; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR004182; GRAM.
DR   Pfam; PF02893; GRAM; 1.
DR   SMART; SM00568; GRAM; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    738       GRAM domain-containing protein 1B.
FT                                /FTId=PRO_0000287450.
FT   TRANSMEM    623    643       Helical; (Potential).
FT   DOMAIN       96    163       GRAM.
FT   MOD_RES      21     21       Phosphoserine.
FT   MOD_RES     274    274       Phosphoserine (By similarity).
FT   MOD_RES     389    389       Phosphotyrosine (By similarity).
FT   MOD_RES     394    394       Phosphothreonine (By similarity).
FT   MOD_RES     581    581       Phosphoserine (By similarity).
FT   MOD_RES     585    585       Phosphothreonine (By similarity).
FT   MOD_RES     587    587       Phosphothreonine (By similarity).
FT   VAR_SEQ       1     40       Missing (in isoform 2).
FT                                /FTId=VSP_025473.
FT   VAR_SEQ       1      8       MKGFKLSC -> MASS (in isoform 3).
FT                                /FTId=VSP_025474.
FT   VAR_SEQ       1      8       MKGFKLSC -> MPAANMMENLQLPALQVPEPQGAPEGSAV
FT                                WSSSSTPTLRRRRFKMRRMKNVQEQSLEAGLVAPDLPGVLA
FT                                PGKEFLQLPSIEITPSSDEDTPWSNCSTPSASPRRKRFLLR
FT                                KWLRVRERKECSESSSQQSSQQSSHDDDSSRFLSPRVRDES
FT                                (in isoform 4).
FT                                /FTId=VSP_025475.
FT   VAR_SEQ     631    634       Missing (in isoform 4).
FT                                /FTId=VSP_025476.
SQ   SEQUENCE   738 AA;  85355 MW;  DF329AE53B090858 CRC64;
     MKGFKLSCTA SNSNRSTPAC SPILRKRSRS PTPQNQDGDT MVEKGSDHSS DKSPSTPEQG
     VQRSCSSQSG RSGGKNSKKS QSWYNVLSPT YKQRNEDFRK LFKQLPDTER LIVDYSCALQ
     RDILLQGRLY LSENWICFYS NIFRWETLLT VRLKDICSMT KEKTARLIPN AIQVCTDSEK
     HFFTSFGARD RTYMMMFRLW QNALLEKPLC PKELWHFVHQ CYGNELGLTS DDEDYVPPDD
     DFNTMGYCEE IPIEENEVND SSSKSSIETK PDASPQLPKK SITNSTLTST GSSEAPVSFD
     GLPLEEEVME GDGSLEKELA IDNIIGEKIE IMAPVTSPSL DFNDNEDIPT ELSDSSDTHD
     EGEVQAFYED LSGRQYVNEV FNFSVDKLYD LLFTNSPFLR DFMEQRRFSD IIFHPWKKEE
     NGNQSRVILY TITLTNPLAP KTATVRETQT MYKASQESEC YVIDAEVLTH DVPYHDYFYT
     INRYTLTRVA RNKSRLRVST ELRYRKQPWG FVKTFIEKNF WSGLEDYFRH LETELTKTES
     TYLAEIHRQS PKEKASKSSA VRRRKRPHAH LRVPHLEEVM SPVTTPTDED VGHRIKHVAG
     STQTRHIPED TPDGFHLQSV SKLLLVISCV ICFSLVLLVV LNMMLFYKLW MLEYTTQTLT
     AWQGLRLQER LPQSQTEWAQ LLESQQKYHD TELQKWREII KSSVLLLDQM KDSLINLQNG
     IRSRDYTAES DEKRNRYH
//
ID   PKHH1_MOUSE             Reviewed;        1356 AA.
AC   Q80TI1; Q3UPN4; Q8BWF3; Q8K334; Q99JL2;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Pleckstrin homology domain-containing family H member 1;
DE            Short=PH domain-containing family H member 1;
GN   Name=Plekhh1; Synonyms=Kiaa1200;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Ovary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 726-1356.
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80TI1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80TI1-2; Sequence=VSP_029350, VSP_029351;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -!- SIMILARITY: Contains 1 MyTH4 domain.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65746.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK122464; BAC65746.1; ALT_INIT; mRNA.
DR   EMBL; AK052692; BAC35099.1; -; mRNA.
DR   EMBL; AK143387; BAE25361.1; -; mRNA.
DR   EMBL; BC006045; AAH06045.1; -; mRNA.
DR   EMBL; BC028900; AAH28900.1; -; mRNA.
DR   IPI; IPI00226258; -.
DR   IPI; IPI00460337; -.
DR   RefSeq; NP_851418.2; NM_181073.3.
DR   UniGene; Mm.478321; -.
DR   HSSP; P42331; 1V89.
DR   ProteinModelPortal; Q80TI1; -.
DR   SMR; Q80TI1; 573-666, 681-789.
DR   PRIDE; Q80TI1; -.
DR   Ensembl; ENSMUST00000021546; ENSMUSP00000021546; ENSMUSG00000060716.
DR   Ensembl; ENSMUST00000039928; ENSMUSP00000049460; ENSMUSG00000060716.
DR   GeneID; 211945; -.
DR   KEGG; mmu:211945; -.
DR   CTD; 211945; -.
DR   MGI; MGI:2144989; Plekhh1.
DR   eggNOG; roNOG14068; -.
DR   GeneTree; ENSGT00390000007630; -.
DR   HOGENOM; HBG505586; -.
DR   HOVERGEN; HBG108258; -.
DR   InParanoid; Q80TI1; -.
DR   OMA; EPEKMEM; -.
DR   OrthoDB; EOG40CHG5; -.
DR   ArrayExpress; Q80TI1; -.
DR   Bgee; Q80TI1; -.
DR   Genevestigator; Q80TI1; -.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR000857; MyTH4_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF00784; MyTH4; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00139; MyTH4; 1.
DR   SMART; SM00233; PH; 2.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   PROSITE; PS00660; FERM_1; FALSE_NEG.
DR   PROSITE; PS00661; FERM_2; FALSE_NEG.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS51016; MYTH4; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Repeat.
FT   CHAIN         1   1356       Pleckstrin homology domain-containing
FT                                family H member 1.
FT                                /FTId=PRO_0000310949.
FT   DOMAIN      572    666       PH 1.
FT   DOMAIN      681    790       PH 2.
FT   DOMAIN      826    980       MyTH4.
FT   DOMAIN      991   1327       FERM.
FT   COILED       27    172       Potential.
FT   COILED      359    407       Potential.
FT   VAR_SEQ       1    681       Missing (in isoform 2).
FT                                /FTId=VSP_029350.
FT   VAR_SEQ     682    690       PTVKGWLTK -> MCVCSCCSL (in isoform 2).
FT                                /FTId=VSP_029351.
FT   CONFLICT     93     93       R -> K (in Ref. 1; BAC65746).
FT   CONFLICT    726    726       Q -> E (in Ref. 3; AAH28900).
FT   CONFLICT    800    803       YEQL -> HASV (in Ref. 3; AAH06045).
FT   CONFLICT   1016   1016       F -> L (in Ref. 3; AAH28900).
FT   CONFLICT   1156   1156       T -> A (in Ref. 1; BAC65746 and 3;
FT                                AAH06045/AAH28900).
FT   CONFLICT   1159   1172       QHLLQQVLDRFYPR -> PRPGWTVLCFCFLH (in Ref.
FT                                3; AAH06045).
FT   CONFLICT   1257   1257       Missing (in Ref. 3; AAH28900).
SQ   SEQUENCE   1356 AA;  150909 MW;  023328737EF57F44 CRC64;
     MAEVKVEVAS IDWQKRCLSL ETQLFRFRLQ ASKIRELLAD KMQELEQRLL EAEQRAENAE
     TQVGVMEEKI KLSNLKSVDS TGTLHQKYQE LLRAVQGKDE LISQLQAQLE KQKQTRAEEA
     KIVQEKAAKI KEWVTVKLAE LEMENQQLKT CNQQLVEQVA ALQDALEDLR MTPSEELLVV
     PEGTPERDPV PSGPSDQPVE QDSNPHTQIL KVAVPTPSLG TLQSRDSLSE ARSLEDLRFS
     MVHPGETAEA KTLQSHLQKE GSPSQLCMKP GNPKHGSASY RESLVTAQGG TFPGTKTSAR
     EGGPGSSLTL PKVRAPSIPR DSFQVAKRHH SQPQVGPGHC DHVVSIEIGA LSALHSPGSS
     KSEARAKVRE EAEKMEMEAL PPSGKQEERE SLKSRRGELE DVELENKPPT PPLHRFPSWE
     SRIYAMATSG MQLSEVSSRR SNAACYASGP SALAFPGAFS GLVYKNVTVP VYTALKGKAT
     QISNVPFVDE SSGSDDDCGS QASFRMSVPC SEYRKTSGLG SPRAIKRGVS MSSLSSEGDY
     AIPPDACSLD SDYSEPEHKL QRTSSYSTDG EALEKSGYLL KMGSRVKTWK RRWFVLRQGQ
     ILYYKSPSDV IRKPQGQVDL NSHCQIVREE EAQTFQLISG NKTYYLTAES PSLLEEWIRV
     LQSLLKVQVT GPPALHQGGT KPTVKGWLTK VKHGHSKLVW CALVGKTFYY YRSHEDKRPL
     GCLPVQDAHI EEVDRSCDSD EDYEAGGTGR LLSSHCTLVI HPPEHSPTYL LIGTKHEKDT
     WLYHLTVAAG GSNAKVGTVY EQLIGKLMDG EGNPDSPLWR HPMLCYSQEG LCASLTTLPS
     EALQTEALKL FKSCQLFINV PVEAASVDYH VSLAQTALQV CLVHPELQSE IYCQLMKQIS
     CRPPQKYSLM QCWQLLALCA PLFLPQHHFL WYVKQQLQRH ADPRSETGQY AIYCQRAVER
     TLQTGEREAR PSRMEVVSIL LRNPFHHSLP FSIPVHFANG TYQVVGFDGS STVDEFLQRL
     NQETGMRKPS QSGFALFTDD PSGRDLEHCL QGRVKICDAI SKWEQTLKEL HPGKSEGGTR
     VVKLMYKNRL YFRSQVKGET ERERLLLAFQ ASGEIVAGRF PVTKELALEM AALMAQVEYG
     DLEKPTLPGP GGTPPTKAQH LLQQVLDRFY PRRYRNGAPP EQLRHLADMM ATKWAALQGC
     SPPECIRIYL TVARKWPLFG AKLFAAQPAQ LSPKENTVVW IAVNEDGVSI LDHRTMQVNI
     TYPYSSVTTF GGCRDDFMLV IRSIPDQSSG KTRIDKLTFR MPAPKITETT LMMASYMNHC
     SATVNLSAKL PAARQPRDLD GQFFASVSCT KGSALL
//
ID   CAPS1_MOUSE             Reviewed;        1355 AA.
AC   Q80TJ1; Q3TSP2; Q61374; Q6AXB4; Q6PGF0;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Calcium-dependent secretion activator 1;
DE   AltName: Full=Calcium-dependent activator protein for secretion 1;
DE            Short=CAPS-1;
GN   Name=Cadps; Synonyms=Caps, Caps1, Kiaa1121;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=BALB/c; TISSUE=Brain;
RA   Namikawa K., Su Q.N., Toki H., Kiyama H.;
RT   "Down-regulation of CAPS (Ca(2+)-dependent activator for secretion)
RT   during nerve regeneration.";
RL   Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 693-1355.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 763-1355 (ISOFORM 4).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=14530279; DOI=10.1074/jbc.M304727200;
RA   Speidel D., Varoqueaux F., Enk C., Nojiri M., Grishanin R.N.,
RA   Martin T.F.J., Hofmann K., Brose N., Reim K.;
RT   "A family of Ca2+-dependent activator proteins for secretion:
RT   comparative analysis of structure, expression, localization, and
RT   function.";
RL   J. Biol. Chem. 278:52802-52809(2003).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=15820695; DOI=10.1016/j.neuron.2005.02.019;
RA   Speidel D., Bruederle C.E., Enk C., Voets T., Varoqueaux F., Reim K.,
RA   Becherer U., Fornai F., Ruggieri S., Holighaus Y., Weihe E., Bruns D.,
RA   Brose N., Rettig J.;
RT   "CAPS1 regulates catecholamine loading of large dense-core vesicles.";
RL   Neuron 46:75-88(2005).
RN   [7]
RP   REVIEW.
RX   PubMed=15820687; DOI=10.1016/j.neuron.2005.03.017;
RA   Suedhof T.C.;
RT   "CAPS in search of a lost function.";
RL   Neuron 46:2-4(2005).
CC   -!- FUNCTION: Calcium-binding protein involved in exocytosis of
CC       vesicles filled with neurotransmitters and neuropeptides. Probably
CC       acts upstream of fusion in the biogenesis or maintenance of mature
CC       secretory vesicles. Regulates catecholamine loading of DCVs. May
CC       specifically mediate the Ca(2+)-dependent exocytosis of large
CC       dense-core vesicles (DCVs) and other dense-core vesicles by acting
CC       as a PtdIns(4,5)P2-binding protein that acts at prefusion step
CC       following ATP-dependent priming and participates in DCVs-membrane
CC       fusion. However, it may also participate in small clear synaptic
CC       vesicles (SVs) exocytosis and it is unclear whether its function
CC       is related to Ca(2+) triggering (By similarity).
CC   -!- SUBUNIT: Homodimer. Interacts with the dopamine receptor DRD2 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral
CC       membrane protein; Cytoplasmic side (Potential). Cell junction,
CC       synapse (By similarity). Note=Membrane-associated to vesicles.
CC       Strongly enriched in synaptic fractions. May preferentially binds
CC       to DCVs but not to SVs. Probably localizes to different vesicles
CC       compared to CADPS2. Binds phosphoinosides, with a strong
CC       selectivity for PtdIns(4,5)P2 over PtdIns(3,4,5)P3.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q80TJ1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80TJ1-2; Sequence=VSP_016809, VSP_016811, VSP_016813;
CC       Name=4;
CC         IsoId=Q80TJ1-4; Sequence=VSP_016814;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Present in brain and adrenal glands (at
CC       protein level). Specifically expressed in neural and endocrine
CC       secretory tissues. Strongly expressed in almost all nerve cells of
CC       the brain, although it is absent from glial cells.
CC   -!- DEVELOPMENTAL STAGE: During brain development, its expression is
CC       similar to that of synaptic markers. Expression is first
CC       detectable late in embryogenesis (E14) and increases to reach a
CC       plateau about 20 days after birth, when most synapses have been
CC       formed (at protein level).
CC   -!- DOMAIN: The PH domain is essential for regulated exocytosis and
CC       binds phospholipids and plasma membrane. It however does not
CC       mediate binding to DCVs (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice die within 30 minutes after birth but
CC       do not display obvious developmental or biochemical abnormalities.
CC       They show a strong reduction in the frequency of amperometrically
CC       detectable release events of transmitter-filled vesicles, while
CC       the total number of fusing vesicles, as judged by capacitance
CC       recordings or total internal reflection microscopy, remains
CC       unchanged.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 MHD1 (MUNC13 homology domain 1) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA13044.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown due to a duplication of 90 bp after position 107;
CC       Sequence=BAC65735.1; Type=Erroneous initiation;
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DR   EMBL; D86214; BAA13044.1; ALT_SEQ; mRNA.
DR   EMBL; AK122453; BAC65735.1; ALT_INIT; mRNA.
DR   EMBL; AK161919; BAE36633.1; -; mRNA.
DR   EMBL; BC057065; AAH57065.1; -; mRNA.
DR   IPI; IPI00330163; -.
DR   IPI; IPI00668903; -.
DR   IPI; IPI00670114; -.
DR   RefSeq; NP_001036082.1; NM_001042617.1.
DR   UniGene; Mm.260881; -.
DR   ProteinModelPortal; Q80TJ1; -.
DR   SMR; Q80TJ1; 520-632.
DR   IntAct; Q80TJ1; 2.
DR   STRING; Q80TJ1; -.
DR   PhosphoSite; Q80TJ1; -.
DR   PRIDE; Q80TJ1; -.
DR   Ensembl; ENSMUST00000067491; ENSMUSP00000064706; ENSMUSG00000054423.
DR   Ensembl; ENSMUST00000112657; ENSMUSP00000108276; ENSMUSG00000054423.
DR   Ensembl; ENSMUST00000112658; ENSMUSP00000108277; ENSMUSG00000054423.
DR   GeneID; 27062; -.
DR   KEGG; mmu:27062; -.
DR   UCSC; uc007sfu.1; mouse.
DR   UCSC; uc007sfv.1; mouse.
DR   CTD; 27062; -.
DR   MGI; MGI:1350922; Cadps.
DR   eggNOG; roNOG07313; -.
DR   GeneTree; ENSGT00590000083094; -.
DR   HOVERGEN; HBG080678; -.
DR   OrthoDB; EOG4DNF3M; -.
DR   NextBio; 305029; -.
DR   ArrayExpress; Q80TJ1; -.
DR   Bgee; Q80TJ1; -.
DR   CleanEx; MM_CADPS; -.
DR   Genevestigator; Q80TJ1; -.
DR   GermOnline; ENSMUSG00000054423; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0050432; P:catecholamine secretion; IMP:MGI.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0016050; P:vesicle organization; IMP:MGI.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR010439; Ca-dep_secretion_activator.
DR   InterPro; IPR014770; Munc13_1.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF06292; DUF1041; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS50004; C2; FALSE_NEG.
DR   PROSITE; PS51258; MHD1; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell junction; Cytoplasmic vesicle;
KW   Exocytosis; Lipid-binding; Membrane; Metal-binding; Protein transport;
KW   Synapse; Transport.
FT   CHAIN         1   1355       Calcium-dependent secretion activator 1.
FT                                /FTId=PRO_0000053865.
FT   DOMAIN      398    479       C2.
FT   DOMAIN      519    622       PH.
FT   DOMAIN      933   1113       MHD1.
FT   REGION      792   1131       Interaction with DRD2 (By similarity).
FT   REGION     1179   1355       Mediates targeting and association with
FT                                DCVs (By similarity).
FT   VAR_SEQ     654    658       SGLKD -> Y (in isoform 2).
FT                                /FTId=VSP_016809.
FT   VAR_SEQ     863    869       ENQKDAE -> GKKREMYEHPVFCLASQVMDLTIQ (in
FT                                isoform 2).
FT                                /FTId=VSP_016811.
FT   VAR_SEQ     904    910       Missing (in isoform 2).
FT                                /FTId=VSP_016813.
FT   VAR_SEQ     905    910       PHVDKG -> GK (in isoform 4).
FT                                /FTId=VSP_016814.
FT   CONFLICT     86     86       R -> W (in Ref. 2; BAC65735).
FT   CONFLICT    908    908       D -> V (in Ref. 4; BAE36633).
FT   CONFLICT   1034   1034       P -> S (in Ref. 4; BAE36633).
FT   CONFLICT   1252   1252       E -> G (in Ref. 4; BAE36633).
FT   CONFLICT   1354   1354       D -> E (in Ref. 1; BAA13044).
SQ   SEQUENCE   1355 AA;  153044 MW;  ADB5D841502FB921 CRC64;
     MLDPSSSEEE SDEILEEESG KDVLGSAASG ARLSPSRTSE GSAGSAGMGG SGAGAGVGAG
     GGGGSGASSG GGAGGLQPSS RAGGGRPSSP SPSVVSEKEK EELERLQKEE EERKKRLQLY
     VFVMRCIAYP FNAKQPTDMA RRQQKISKQQ LQTVKDRFQA FLNGETQIVA DEAFMNAVQS
     YYEVFLKSDR VARMVQSGGC SANDSREVFK KHIEKRVRSL PEIDGLSKET VLSSWMAKFD
     AIYRGEEDPR KQQARMTASA ASELILSKEQ LYEMFQNILG IKKFEHQLLY NACQLDNPDE
     QAAQIRRELD GRLQMADQIA RERKFPKFVS KEMENMYIEE LKSSVNLLMA NLESMPVSKG
     GEFKLQKLKR SHNASIIDMG EESENQLSKS DVLLSFSLEV VIMEVQGLKS LAPNRIVYCT
     MEVEGGEKLQ TDQAEASKPT WGTQGDFSTT HALPAVKVKL FTESTGVLAL EDKELGRVIL
     HPTPNSPKQS EWHKMTVSKN CPDQDLKIKL AVRMDKPQNM KHSGYLWTIG KNVWKRWKKR
     FFVLVQVSQY TFAMCSYREK KAEPQELLQL DGYTVDYTDP QPGLEGGRAF FNAVKEGDTV
     IFASDDEQDR ILWVQAMYRA TGQSHKPVPP TQVQKLNAKG GNVPQLDAPI SQFSGLKDAD
     RAQKHGMDEF ISSNPCNFDH ASLFEMVQRL TLDHRLNDSY SCLGWFSPGQ VFVLDEYCAR
     NGVRGCHRHL CYLRDLLERA ENGAMIDPTL LHYSFAFCAS HVHGNRPDGI GTVTVEEKER
     FEEIKERLRV LLENQITHFR YCFPFGRPEG ALKATLSLLE RVLMKDIVTP VPQEEVKTVI
     RKCLEQAALV NYSRLSEYAK IEENQKDAEN VGRLITPAKK LEDTIRLAEL VIEVLQQNEE
     HHAEPHVDKG EAFAWWSDLM VEHAETFLSL FAVDMDAALE VQPPDTWDSF PLFQLLNDFL
     RTDYNLCNGK FHKHLQDLFA PLVVRYVDLM ESSIAQSIHR GFERESWEPV KSLTSNLPNV
     NLPNVNLPKV PNLPVNIPLG IPQMPTFSAP SWMAAIYDAD NGSGTSEDLF WKLDALQTFI
     RDLHWPEEEF GKHLEQRLKL MASDMIESCV KRTRIAFEVK LQKTSRSTDF RVPQSICTMF
     NVMVDAKAQS TKLCSMEMGQ EHQYHSKIDE LIEETVKEMI TLLVAKFVTI LEGVLAKLSR
     YDEGTLFSSF LSFTVKAASK YVDVPKPGMD VADAYVTFVR HSQDVLRDKV NEEMYIERLF
     DQWYNSSMNI ICTWLTDRMD LQLHIYQLKT LIRMVKKTYR DFRLQGVLDS TLNSKTYETI
     RNRLTVEEAT ASVSEGGGLQ GISMKDSDEE DEEDD
//
ID   PHF8_MOUSE              Reviewed;        1023 AA.
AC   Q80TJ7; A2ABU8; A2ABV0; A2ABV2; Q8BLX8; Q8BLY0; Q8BZ61; Q8CG26;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Histone lysine demethylase PHF8;
DE            EC=1.14.11.27;
DE   AltName: Full=PHD finger protein 8;
GN   Name=Phf8; Synonyms=Kiaa1111;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-490 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Bone;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-1023 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-899.
RC   STRAIN=129/Sv;
RX   PubMed=15112104; DOI=10.1007/s00335-003-2329-1;
RA   Abe K., Yuzuriha M., Sugimoto M., Ko M.S., Brathwaite M.E., Waeltz P.,
RA   Nagaraja R.;
RT   "Gene content of the 750-kb critical region for mouse embryonic
RT   ectoderm lethal tcl-w5.";
RL   Mamm. Genome 15:265-276(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   STRUCTURE BY NMR OF 1-66.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of PHD domain in protein AA017385.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Histone lysine demethylase with selectivity for the di-
CC       and monomethyl states that plays a key role cell cycle
CC       progression, rDNA transcription and brain development.
CC       Demethylates mono- and dimethylated histone H3 'Lys-9' residue
CC       (H3K9Me1 and H3K9Me2), dimethylated H3 'Lys-27' (H3K27Me2) and
CC       monomethylated histone H4 'Lys-20' residue (H4K20Me1). Acts as a
CC       transcription activator as H3K9Me1, H3K9Me2, H3K27Me2 and H4K20Me1
CC       are epigenetic repressive marks. Involved in cell cycle
CC       progression by being required to control G1-S transition. Acts as
CC       a coactivator of rDNA transcription, by activating polymerase I
CC       (pol I) mediated transcription of rRNA genes. Required for brain
CC       development, probably by regulating expression of neuron-specific
CC       genes. Has activity toward H4K20Me1 only when nucleosome is used
CC       as a substrate and when not histone octamer is used as substrate.
CC       May also have weak activity toward dimethylated H3 'Lys-36'
CC       (H3K36Me2), however, the relevance of this result remains unsure
CC       in vivo. Specifically binds trimethylated 'Lys-4' of histone H3
CC       (H3K4me3), affecting histone demethylase specificity: has weak
CC       activity toward H3K9Me2 in absence of H3K4me3, while it has high
CC       activity toward H3K9me2 when binding H3K4me3 (By similarity).
CC   -!- CATALYTIC ACTIVITY: Protein N(6),N(6)-dimethyl-L-lysine + 2-
CC       oxoglutarate + O(2) = protein N(6)-methyl-L-lysine + succinate +
CC       formaldehyde + CO(2).
CC   -!- CATALYTIC ACTIVITY: Protein N(6)-methyl-L-lysine + 2-oxoglutarate
CC       + O(2) = protein L-lysine + succinate + formaldehyde + CO(2).
CC   -!- COFACTOR: Binds 1 Fe(2+) ion per subunit (By similarity).
CC   -!- SUBUNIT: Interacts with POLR1B, UBTF, SETD1A, HCFC1, E2F1 and
CC       ZNF711 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Nucleus, nucleolus
CC       (By similarity). Note=Recruited to H3K4me3 sites on chromatin
CC       during interphase. Dissociates from chromatin when cells enter
CC       mitosis (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q80TJ7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80TJ7-2; Sequence=VSP_014966, VSP_014969, VSP_014970;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q80TJ7-3; Sequence=VSP_014967, VSP_014968;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC       Binding to H3K4me3 promotes its access to H3K9me2 (By similarity).
CC   -!- DOMAIN: The linker region is a critical determinant of demethylase
CC       specificity. It enables the active site of JmjC to reach the
CC       target H3K9me2 when the PHD-type zinc finger binds to H3K4me3 (By
CC       similarity).
CC   -!- PTM: Phosphorylation at Ser-33 and Ser-84 are required for
CC       dissociation from chromatin and accumulation of H4K20Me1 levels
CC       during prophase (By similarity).
CC   -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family.
CC       JHDM1D subfamily.
CC   -!- SIMILARITY: Contains 1 JmjC domain.
CC   -!- SIMILARITY: Contains 1 PHD-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM17163.1; Type=Erroneous gene model prediction;
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DR   EMBL; AK036609; BAC29505.1; -; mRNA.
DR   EMBL; AK040943; BAC30755.2; -; mRNA.
DR   EMBL; AK040969; BAC30763.1; -; mRNA.
DR   EMBL; AL662922; CAM17161.1; -; Genomic_DNA.
DR   EMBL; AL840642; CAM15464.1; -; Genomic_DNA.
DR   EMBL; AL662922; CAM15464.1; JOINED; Genomic_DNA.
DR   EMBL; AL662922; CAM17159.1; -; Genomic_DNA.
DR   EMBL; AL840642; CAM17159.1; JOINED; Genomic_DNA.
DR   EMBL; AL662922; CAM17163.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AK122447; BAC65729.1; -; mRNA.
DR   EMBL; AF528164; AAO17385.1; ALT_SEQ; Genomic_DNA.
DR   IPI; IPI00109676; -.
DR   IPI; IPI00227351; -.
DR   IPI; IPI00649181; -.
DR   RefSeq; NP_001009544.1; NM_001009544.2.
DR   RefSeq; NP_001106825.1; NM_001113354.1.
DR   RefSeq; NP_796175.1; NM_177201.5.
DR   UniGene; Mm.17156; -.
DR   UniGene; Mm.84774; -.
DR   PDB; 1WEP; NMR; -; A=1-63.
DR   PDBsum; 1WEP; -.
DR   ProteinModelPortal; Q80TJ7; -.
DR   SMR; Q80TJ7; 3-447.
DR   STRING; Q80TJ7; -.
DR   PhosphoSite; Q80TJ7; -.
DR   PRIDE; Q80TJ7; -.
DR   Ensembl; ENSMUST00000046950; ENSMUSP00000040765; ENSMUSG00000041229.
DR   GeneID; 320595; -.
DR   GeneID; 74042; -.
DR   KEGG; mmu:320595; -.
DR   KEGG; mmu:74042; -.
DR   UCSC; uc009upd.1; mouse.
DR   UCSC; uc009upe.1; mouse.
DR   UCSC; uc009upf.1; mouse.
DR   CTD; 320595; -.
DR   MGI; MGI:2444341; Phf8.
DR   GeneTree; ENSGT00550000074396; -.
DR   HOGENOM; HBG445752; -.
DR   HOVERGEN; HBG045631; -.
DR   InParanoid; Q80TJ7; -.
DR   OMA; MSNGSTK; -.
DR   OrthoDB; EOG4G4GPT; -.
DR   PhylomeDB; Q80TJ7; -.
DR   NextBio; 397037; -.
DR   ArrayExpress; Q80TJ7; -.
DR   Bgee; Q80TJ7; -.
DR   CleanEx; MM_PHF8; -.
DR   Genevestigator; Q80TJ7; -.
DR   GermOnline; ENSMUSG00000041229; Mus musculus.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0071558; F:histone demethylase activity (H3-K27 specific); ISS:UniProtKB.
DR   GO; GO:0051864; F:histone demethylase activity (H3-K36 specific); ISS:UniProtKB.
DR   GO; GO:0032454; F:histone demethylase activity (H3-K9 specific); ISS:UniProtKB.
DR   GO; GO:0035575; F:histone demethylase activity (H4-K20 specific); ISS:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR   GO; GO:0035064; F:methylated histone residue binding; ISS:UniProtKB.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0061188; P:negative regulation of chromatin silencing at rDNA; ISS:UniProtKB.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0045943; P:positive regulation of transcription from RNA polymerase I promoter; ISS:UniProtKB.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR013129; TF_JmjC.
DR   InterPro; IPR003347; TF_JmjC_AAH.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; Cell cycle;
KW   Chromatin regulator; Dioxygenase; Iron; Metal-binding; Nucleus;
KW   Oxidoreductase; Phosphoprotein; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1   1023       Histone lysine demethylase PHF8.
FT                                /FTId=PRO_0000059296.
FT   DOMAIN      195    351       JmjC.
FT   ZN_FING       5     56       PHD-type.
FT   REGION       65     79       Linker (By similarity).
FT   COMPBIAS    733    771       Ser-rich.
FT   METAL       247    247       Iron; catalytic (By similarity).
FT   METAL       249    249       Iron; catalytic (By similarity).
FT   METAL       319    319       Iron; catalytic (By similarity).
FT   BINDING     244    244       Substrate (By similarity).
FT   BINDING     264    264       Substrate (By similarity).
FT   MOD_RES      33     33       Phosphoserine; by CDK1 (By similarity).
FT   MOD_RES      84     84       Phosphoserine; by CDK1 (By similarity).
FT   MOD_RES     615    615       Phosphoserine.
FT   MOD_RES     669    669       Phosphothreonine (By similarity).
FT   MOD_RES     670    670       Phosphothreonine (By similarity).
FT   MOD_RES     686    686       Phosphoserine (By similarity).
FT   MOD_RES     768    768       Phosphoserine (By similarity).
FT   MOD_RES     817    817       Phosphoserine (By similarity).
FT   MOD_RES     820    820       Phosphoserine.
FT   MOD_RES     843    843       Phosphoserine (By similarity).
FT   VAR_SEQ     442    542       Missing (in isoform 2).
FT                                /FTId=VSP_014966.
FT   VAR_SEQ     442    464       DIFQQNVGKTSNIFGLQRIFPAG -> VRSMGEGKAFGKGW
FT                                RLKWQVRTL (in isoform 3).
FT                                /FTId=VSP_014967.
FT   VAR_SEQ     465   1023       Missing (in isoform 3).
FT                                /FTId=VSP_014968.
FT   VAR_SEQ     883    896       ELQKAQKKKYIKKK -> VRVDTQLVALLLMT (in
FT                                isoform 2).
FT                                /FTId=VSP_014969.
FT   VAR_SEQ     897   1023       Missing (in isoform 2).
FT                                /FTId=VSP_014970.
FT   STRAND       16     18
FT   STRAND       20     23
FT   TURN         24     26
FT   STRAND       29     31
FT   HELIX        32     35
FT   HELIX        39     42
FT   STRAND       46     48
FT   TURN         51     56
SQ   SEQUENCE   1023 AA;  113553 MW;  7B9351944C000487 CRC64;
     MASVPVYCLC RLPYDVTRFM IECDMCQDWF HGSCVGVEEE KAADIDLYHC PNCEVLHGPS
     IMKKRRGSSK GHDNHKGKPL KTGSSMFIRE LRGRTFDSSD EVILKPTGSQ LTVEFLEENS
     FSVPILVLKK DGLGMTLPSP SFTVRDVEHY VGSDKEIDVI DVARQADCKM KLGDFVKYYY
     SGKREKVLNV ISLEFSDTRL SNLVETPRIV RKLSWVENLW PEECVFERPN VQKYCLMSVR
     DSYTDFHIDF GGTSVWYHVL KGEKIFYLIR PTNANLTLFE CWSSSSNQNE MFFGDQVEKC
     YKCSVKQGQT LFIPTGWIHA VLTPVDCLAF GGNFLHSLNI EMQLKAYEIE KRLSTADLFK
     FPNFETICWY VGKHILDIFR GLRENRRHPA SYLVHGGKAL NLAFRAWTKK EALPDHEDEI
     PETVRTVQLI KDLAREIRLV EDIFQQNVGK TSNIFGLQRI FPAGSIPLTK PAHSTSVSMS
     KLSLPSKNGS KKKGLKPKDI FKKAERKGKQ SSALGPAGQL SYNLMDPYSH QALKTGPSQK
     AKFNMSGTSL NDSDDDSADM DLDGSENPLA LLMANGSTKR MKSVSKSRRA KIAKKVDSAR
     LVAEQVMGDE FDLDSDDELQ IDERLGKEKA NLLIRSKFPR KLPRAKPCSD PNRIREPGEV
     EFDIEEDYTT DEDMVEGVES KLGNGSGAGG ILDLLKASRQ VGGPDYAALT EAPASPSTQE
     AIQGMLCMAN LQSSSSSPAT SSLQAWWTGG QERSSGSSSS GLGTVSSSPA SQRTPGKRPI
     KRPAYWKNES EEEENASLDE QDSLGACFKD AEYIYPSLES DDDDPALKSR PKKKKNSDDA
     PWSPKARVTP TLPKQDRPVR EGTRVASIET GLAAAAAKLA QQELQKAQKK KYIKKKPLLK
     EVEQPRPQDS NPIMTMPAPT VATTPQPDTS SSPQPPPEPK QEALSGSLAD HEYTARPNAF
     GMAQANRSTT PMAPGVFLTQ RRPSVGSQSS QAGQGKRPKK GLATAKQRLG RILKIHRNGK
     LLL
//
ID   K1107_MOUSE             Reviewed;        1369 AA.
AC   Q80TK0; Q3TPG8; Q8BRQ7; Q8BRS6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 4.
DT   08-MAR-2011, entry version 36.
DE   RecName: Full=Uncharacterized protein KIAA1107;
GN   Name=Kiaa1107;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 107-1099.
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 134-1369.
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC31589.1; Type=Erroneous initiation;
CC       Sequence=BAC31628.1; Type=Frameshift; Positions=182;
CC       Sequence=BAE37768.1; Type=Erroneous initiation;
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DR   EMBL; AC134411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK043587; BAC31589.1; ALT_INIT; mRNA.
DR   EMBL; AK043720; BAC31628.1; ALT_FRAME; mRNA.
DR   EMBL; AK164388; BAE37768.1; ALT_INIT; mRNA.
DR   EMBL; AK122444; BAC65726.3; -; Transcribed_RNA.
DR   IPI; IPI00330169; -.
DR   RefSeq; NP_001007575.2; NM_001007574.2.
DR   UniGene; Mm.261891; -.
DR   PhosphoSite; Q80TK0; -.
DR   PRIDE; Q80TK0; -.
DR   Ensembl; ENSMUST00000100951; ENSMUSP00000098511; ENSMUSG00000044060.
DR   GeneID; 231570; -.
DR   KEGG; mmu:231570; -.
DR   MGI; MGI:2445097; A830010M20Rik.
DR   HOGENOM; HBG506189; -.
DR   HOVERGEN; HBG108026; -.
DR   InParanoid; Q80TK0; -.
DR   OrthoDB; EOG4NS39V; -.
DR   ArrayExpress; Q80TK0; -.
DR   Bgee; Q80TK0; -.
DR   CleanEx; MM_A830010M20RIK; -.
DR   Genevestigator; Q80TK0; -.
PE   2: Evidence at transcript level;
KW   Phosphoprotein.
FT   CHAIN         1   1369       Uncharacterized protein KIAA1107.
FT                                /FTId=PRO_0000320678.
FT   MOD_RES     852    852       Phosphoserine (By similarity).
FT   CONFLICT    141    141       A -> V (in Ref. 2; BAC31589).
FT   CONFLICT    310    310       A -> V (in Ref. 2; BAC31628).
FT   CONFLICT    387    387       Missing (in Ref. 2; BAC31628).
FT   CONFLICT    761    761       N -> D (in Ref. 2; BAC31589).
SQ   SEQUENCE   1369 AA;  148696 MW;  27947B4FF49BA95D CRC64;
     MESDRLIMGL PRVKWTEAAL SMASQLQEEC VTFIVENFSQ IIESENFTLL LQSQAMSSTA
     HLLDKIFKAI EDNITAENSC SLLMALDTLL NSESTKEMGF TCRIQAVRGK LWAFLVQSFY
     AVRHTGSWKL MHLDDQQKIQ AAALDKGDDR RLGRKPVLTS SQQRRQGSDV DVLKIKPWTE
     NNKKPCQTSL STNQKMRSDG LGASGHASST NRNSINKVSK HGDSTKMSKV VKEMKTGGKY
     VSGKSKTMVK PQTENSDHTK IEGLSSTVVG RPSRVTAAGR KDPVHGKGVQ NQEVETTGAR
     PKVLTANLNA QARAKPLQTL RGKDSTCPAS VGPSSRSTHS STELLASMGS VDETKENGSV
     EDKCRDGKPY VSDSPGQMVS NGVMSTAAVK SRAVARITNG TASNKSFTHE QDSHGNSSVI
     KRGDGKGLSA SAPQTAAKKR GSSNGCTAAQ PRTKSAPPTL AQAQGSQGES PHSVKSSVSS
     RQSDENVTRL RHGTDKQIPK RKVVKQGHTT LQKVNAKLVP MPKIPSQPKK GGTVNSKDSK
     QKVLPGQIML QSHASQRPSK PEVAEKSVLH GVSDSRNHVS KQRPHESPCT LACDTSGPEV
     SQIPCRPQPQ SPLGSQEKKR LELACQDRST LGDSVKRELR SELAGIEQSH TSAYKDSSQC
     NGNPNCGSIA ALKSVISNPN ENLINSNPVH NSDSANTEQA YLSDRERETG RENTDTEPSM
     SCINGKAFLC VPEGTSSTLN PTQSDRRLTF HGAAQSQLPD NCATEDSKCA TVTSAVSSKC
     LLGQPSEKNC KNMEMSETPE SHGTPEAPFV GPWDLNTGAT HQRESPESDT GSATTSSDDI
     KPRSEDYDAG GSQDDEGSHD RGISKCSTAL CHDFLGRSSS DTSTPEELKV HEGDLRTEVR
     VRKQGGGDHQ IHSASDDEIP RKKPEPWSRS TIGYPREKGS TPRGSIPSAQ EGDQVSSSAD
     ETEDERSEAE NVGENSSPCS SGTQQVQGII NLAFDDGAEH ESREFSATKK FRRSVLLSVD
     ECEEVGSDEG EGHTPFQPSL DSLSPSDVFD GVSYEHHGRT GYSRFFKENE ATTAEHNHNK
     GNGGYKNESF LLNSRSKDFE KQDKQCVSTD QKTRLDVPPK GSQQLFPENE EVISKREAAH
     NFQQHSTFMD GDTKSQERPC HLELHQRELS SNIPKISSVK SLDSCPSQGL PQEGQVKESR
     PTPPKGANNA VFSGNVDDCD TMAQTSMYDH RPSKTLSPIY EMSLTAACEQ EVESETHVAD
     RGSEDEQHFA KQDWTLLRQL LSEQDANLNI TSSLPEDLSL AQYLINQTLL LARDSSKPQG
     SAHADTWNRW SELSSPLDDS ATSATTASVS STDCSPQGEW TILELETQH
//
ID   PPM1E_MOUSE             Reviewed;         749 AA.
AC   Q80TL0; Q5SX30; Q8BGM6; Q8CB81;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Protein phosphatase 1E;
DE            EC=3.1.3.16;
DE   AltName: Full=Ca(2+)/calmodulin-dependent protein kinase phosphatase N;
DE            Short=CaMKP-N;
DE   AltName: Full=CaMKP-nucleus;
DE            Short=CaMKN;
DE   AltName: Full=Partner of PIX 1;
DE   AltName: Full=Partner of PIX-alpha;
DE            Short=Partner of PIXA;
GN   Name=Ppm1e; Synonyms=Camkn, Kiaa1072;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone, Cerebellum, and Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 85-749.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   PROTEIN SEQUENCE OF 198-205, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: Protein phosphatase that inactivates multifunctional CaM
CC       kinases such as CAMK4 and CAMK2. Dephosphorylates and inactivates
CC       PAK. May play a role in the inhibition of actin fiber stress
CC       breakdown and in morphological changes driven by TNK2/CDC42 (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- COFACTOR: Binds 2 magnesium or manganese ions per subunit (By
CC       similarity).
CC   -!- SUBUNIT: Heterotrimer. Interacts with PAX1 and ARHGEF6 (or
CC       ARHGEF7) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=A truncated form,
CC       major form, with the C-terminal part missing, is mostly found in
CC       the cytoplasm and a little in the nucleus. The full length, minor
CC       form, is found in the nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the PP2C family.
CC   -!- SIMILARITY: Contains 1 PP2C-like domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK036583; BAC29490.1; -; mRNA.
DR   EMBL; AK046962; BAC32927.1; -; mRNA.
DR   EMBL; AK053696; BAC35479.1; -; mRNA.
DR   EMBL; AL596130; CAI24490.1; -; Genomic_DNA.
DR   EMBL; AK122434; BAC65716.1; -; mRNA.
DR   IPI; IPI00461286; -.
DR   RefSeq; NP_796141.2; NM_177167.4.
DR   UniGene; Mm.341988; -.
DR   HSSP; P35813; 1A6Q.
DR   ProteinModelPortal; Q80TL0; -.
DR   SMR; Q80TL0; 228-486.
DR   PRIDE; Q80TL0; -.
DR   Ensembl; ENSMUST00000055438; ENSMUSP00000061278; ENSMUSG00000046442.
DR   GeneID; 320472; -.
DR   KEGG; mmu:320472; -.
DR   CTD; 320472; -.
DR   MGI; MGI:2444096; Ppm1e.
DR   eggNOG; roNOG09096; -.
DR   GeneTree; ENSGT00540000070009; -.
DR   HOGENOM; HBG715807; -.
DR   HOVERGEN; HBG098260; -.
DR   InParanoid; Q80TL0; -.
DR   OMA; PVEMFGP; -.
DR   OrthoDB; EOG48SGSJ; -.
DR   PhylomeDB; Q80TL0; -.
DR   BRENDA; 3.1.3.16; 244.
DR   NextBio; 396789; -.
DR   ArrayExpress; Q80TL0; -.
DR   Bgee; Q80TL0; -.
DR   CleanEx; MM_PPM1E; -.
DR   Genevestigator; Q80TL0; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008287; C:protein serine/threonine phosphatase complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   InterPro; IPR001932; PP2C-like.
DR   InterPro; IPR000222; PP2C_Mn2_Asp60_BS.
DR   InterPro; IPR014045; PP2C_N.
DR   InterPro; IPR015655; Protein_Pase_2C.
DR   Gene3D; G3DSA:3.60.40.10; PP2C-related; 1.
DR   PANTHER; PTHR13832; PP2C; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-related; 1.
DR   PROSITE; PS01032; PP2C; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Hydrolase; Magnesium; Manganese;
KW   Metal-binding; Nucleus; Protein phosphatase; Repeat.
FT   CHAIN         1    749       Protein phosphatase 1E.
FT                                /FTId=PRO_0000286821.
FT   REPEAT       31     32       1.
FT   REPEAT       33     34       2.
FT   REPEAT       35     36       3.
FT   REPEAT       37     38       4; approximate.
FT   REPEAT       39     40       5.
FT   REPEAT       41     42       6.
FT   REPEAT       43     44       7.
FT   DOMAIN      243    485       PP2C-like.
FT   REGION       31     44       7 X 2 AA tandem repeats of P-E.
FT   COMPBIAS      7    101       Glu-rich.
FT   COMPBIAS    111    127       Pro-rich.
FT   METAL       270    270       Manganese 1 (By similarity).
FT   METAL       270    270       Manganese 2 (By similarity).
FT   METAL       271    271       Manganese 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       432    432       Manganese 2 (By similarity).
FT   METAL       476    476       Manganese 2 (By similarity).
FT   CONFLICT    107    107       H -> D (in Ref. 1; BAC29490).
SQ   SEQUENCE   749 AA;  83419 MW;  C59BC6CAC3E268B0 CRC64;
     MAGCIPEEKT YRRFLELFLG EFRGPCGGGE PEPEPESEPE PEPEAELVAA EAAEASGEEP
     GEDAATVEAT EEGEQDQDPE PEDEAVEEET ATEGEEEEEE EAAAPGHSAV PPPPQPQLPP
     LPPLPRPLSE RITREEVEGE SLDLCLQQLY KYNCPSFLAA ALARATSDEV LQSDLSAHCI
     PKETDGTEGT VEIETVKLAR SVFSKLHEIC CSWVKDFPLR RRPQIYYETS IHAIKNMRRK
     MEDKHVCIPD FNMLFNLEDQ EEQAYFAVFD GHGGVDAAIY ASVHLHVNLV RQEMFPHDPA
     EALCRAFRVT DERFVQKAAR ESLRCGTTGV VTFIRGNMLH VAWVGDSQVM LVRKGQAVEL
     MKPHKPDRED EKQRIEALGG CVVWFGAWRV NGSLSVSRAI GDAEHKPYIC GDADSASTVL
     DGTEDYLILA CDGFYDTVNP DEAVKVVSDH LKENNGDSSM VAHKLVASAR DAGSSDNITV
     IVVFLRDMNK AVNVSEESEW TENSFQGGQE DGGDDKETHG ECKRPWPQHQ CSAPADLGYE
     GRVDSFTDRT SLSPGPQINV LEDPDYLDLT QIEASKPHST QFLPPVEMIG PGAPKKDLNE
     LIMEERSVKS SLPERSGAGE PRVSFNLGST GQQICRMENL SPVSSGLENE QFKSRGKTAS
     RLYHLRHHYS KRQRGFRFNP KFYSFLSARE PSHKIGISLS SLTRSGKRNK MLRSSLPWRE
     NSWEGYSGNV KIRKRNDIPC PDFPWSYKI
//
ID   ADCY2_MOUSE             Reviewed;        1090 AA.
AC   Q80TL1; Q8CFU6;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 2.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Adenylate cyclase type 2;
DE            EC=4.6.1.1;
DE   AltName: Full=ATP pyrophosphate-lyase 2;
DE   AltName: Full=Adenylate cyclase type II;
DE   AltName: Full=Adenylyl cyclase 2;
GN   Name=Adcy2; Synonyms=Kiaa1060;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: This is a membrane-bound, calmodulin-insensitive
CC       adenylyl cyclase (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
CC   -!- COFACTOR: Binds 2 magnesium ions per subunit (By similarity).
CC   -!- ENZYME REGULATION: Insensitive to calcium/calmodulin. Stimulated
CC       by the G protein beta and gamma subunit complex (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
CC       cyclase family.
CC   -!- SIMILARITY: Contains 2 guanylate cyclase domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65714.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK122432; BAC65714.1; ALT_INIT; mRNA.
DR   EMBL; BC037107; AAH37107.1; -; mRNA.
DR   IPI; IPI00377680; -.
DR   UniGene; Mm.390617; -.
DR   ProteinModelPortal; Q80TL1; -.
DR   SMR; Q80TL1; 277-463, 877-1058.
DR   STRING; Q80TL1; -.
DR   PhosphoSite; Q80TL1; -.
DR   PRIDE; Q80TL1; -.
DR   Ensembl; ENSMUST00000022013; ENSMUSP00000022013; ENSMUSG00000021536.
DR   UCSC; uc007rcf.1; mouse.
DR   MGI; MGI:99676; Adcy2.
DR   GeneTree; ENSGT00590000083071; -.
DR   HOVERGEN; HBG050458; -.
DR   InParanoid; Q80TL1; -.
DR   OrthoDB; EOG48D0TJ; -.
DR   PhylomeDB; Q80TL1; -.
DR   BRENDA; 4.6.1.1; 244.
DR   ArrayExpress; Q80TL1; -.
DR   Bgee; Q80TL1; -.
DR   CleanEx; MM_ADCY2; -.
DR   Genevestigator; Q80TL1; -.
DR   GermOnline; ENSMUSG00000021536; Mus musculus.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; TAS:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:MGI.
DR   GO; GO:0007188; P:G-protein signaling, coupled to cAMP nucleotide second messenger; TAS:MGI.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   InterPro; IPR009398; Aden_cycl-like.
DR   Gene3D; G3DSA:3.30.70.1230; A/G_cyclase; 2.
DR   Pfam; PF06327; DUF1053; 1.
DR   Pfam; PF00211; Guanylate_cyc; 2.
DR   SMART; SM00044; CYCc; 2.
DR   SUPFAM; SSF55073; A/G_cyclase; 2.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 2.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; cAMP biosynthesis; Glycoprotein; Lyase; Magnesium;
KW   Membrane; Metal-binding; Nucleotide-binding; Repeat; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   1090       Adenylate cyclase type 2.
FT                                /FTId=PRO_0000195685.
FT   TOPO_DOM      1     44       Cytoplasmic (Potential).
FT   TRANSMEM     45     65       Helical; (Potential).
FT   TRANSMEM     75     95       Helical; (Potential).
FT   TRANSMEM    107    127       Helical; (Potential).
FT   TRANSMEM    132    152       Helical; (Potential).
FT   TRANSMEM    157    177       Helical; (Potential).
FT   TRANSMEM    186    206       Helical; (Potential).
FT   TOPO_DOM    207    600       Cytoplasmic (Potential).
FT   TRANSMEM    601    621       Helical; (Potential).
FT   TRANSMEM    626    646       Helical; (Potential).
FT   TRANSMEM    679    699       Helical; (Potential).
FT   TRANSMEM    734    754       Helical; (Potential).
FT   TRANSMEM    763    783       Helical; (Potential).
FT   TRANSMEM    800    820       Helical; (Potential).
FT   TOPO_DOM    821   1090       Cytoplasmic (Potential).
FT   METAL       294    294       Magnesium 1 (By similarity).
FT   METAL       294    294       Magnesium 2 (By similarity).
FT   METAL       295    295       Magnesium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       338    338       Magnesium 1 (By similarity).
FT   METAL       338    338       Magnesium 2 (By similarity).
FT   CARBOHYD    712    712       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    717    717       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    723    723       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   1090 AA;  123270 MW;  461CDF5E6C828CCB CRC64;
     MRRRRYLRDR AEAAAAAAAG GGEGLQRSRD WLYESYYCMS QQHPLIVFLL LIVMGACLAL
     LAVFFALGLE VEDHVAFLIT VPTALAIFFA IFILVCIESV FKKLLRVFSL VIWICLVAMG
     YLFMCFGGTV SAWDQVSFFL FIIFVVYTML PFNMRDAIIA SVLTSSSHTI VLSVYLSATP
     GAKEHLFWQI LANVIIFICG NLAGAYHKHL MELALQQTYR DTCNCIKSRI KLEFEKRQQE
     RLLLSLLPAH IAMEMKAEII QRLQGPKAGQ MENTNNFHNL YVKRHTNVSI LYADIVGFTR
     LASDCSPGEL VHMLNELFGK FDQIAKENEC MRIKILGDCY YCVSGLPISL PNHAKNCVKM
     GLDMCEAIKK VRDATGVDIN MRVGVHSGNV LCGVIGLQKW QYDVWSHDVT LANHMEAGGV
     PGRVHISSVT LEHLNGAYKV EEGDGEIRDP YLKQHLVKTY FVINPKGERR SPQHLFRPRH
     TLDGAKMRAS VRMTRYLESW GAAKPFAHLH HRDSMTTENG KISTTDVPMG QHNFQNRTLR
     TKSQKKRFEE ELNERMIQAI DGINAQKQWL KSEDIQRISL FFYNKNIEKE YRATALPAFK
     YYVTCACLIF LCIFIVQILV LPKTSILGFS FGAAFLSLIF ILFVCFAGQL LQCSKKASAS
     LLWLLKSSGI IANRPWPRIS LTIVTTAIIL TMAVFNMFFL SNSEETTLPT ANASNANVSV
     PDNQTAILHA RNLFFLPYFI YSCILGLISC SVFLRVNYEL KMLIMMVALV GYNIILLHTH
     AHVLDAYSQV LFQRPGIWKD LKTMGSVSLS IFFITLLVLG RQSEYYCRLD FLWKNKFKKE
     REEIETMENL NRVLLENVLP AHVAEHFLAR SLKNEELYHQ SYDCVCVMFA SIPDFKEFYT
     ESDVNKEGLE CLRLLNEIIA DFDDLLSKPK FSGVEKIKTI GSTYMAATGL SAVPSQEHAQ
     EPERQYMHIG TMVEFAYALV GKLDAINKHS FNDFKLRVGI NHGPVIAGVI GAQKPQYDIW
     GNTVNVASRM DSTGVLDKIQ VTEETSLILQ TLGYTCTCRG IINVKGKGDL KTYFVNTEMS
     RSLSQSNLAS
//
ID   K1045_MOUSE             Reviewed;         400 AA.
AC   Q80TL4; A2AG28; Q8BH08;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Protein KIAA1045;
GN   Name=Kiaa1045;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80TL4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80TL4-2; Sequence=VSP_014952;
CC   -!- SIMILARITY: Contains 1 PHD-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65710.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK122428; BAC65710.1; ALT_INIT; mRNA.
DR   EMBL; AK038528; BAC30029.1; -; mRNA.
DR   EMBL; AK046283; BAC32670.1; -; mRNA.
DR   EMBL; AL672276; CAM14311.1; -; Genomic_DNA.
DR   EMBL; BC057092; AAH57092.1; -; mRNA.
DR   IPI; IPI00377681; -.
DR   IPI; IPI00647986; -.
DR   RefSeq; NP_766278.1; NM_172690.2.
DR   UniGene; Mm.240965; -.
DR   ProteinModelPortal; Q80TL4; -.
DR   SMR; Q80TL4; 123-319.
DR   PhosphoSite; Q80TL4; -.
DR   PRIDE; Q80TL4; -.
DR   Ensembl; ENSMUST00000107975; ENSMUSP00000103609; ENSMUSG00000036062.
DR   Ensembl; ENSMUST00000107976; ENSMUSP00000103610; ENSMUSG00000036062.
DR   GeneID; 230085; -.
DR   KEGG; mmu:230085; -.
DR   UCSC; uc008soi.1; mouse.
DR   UCSC; uc008soj.1; mouse.
DR   CTD; 230085; -.
DR   MGI; MGI:2140712; N28178.
DR   GeneTree; ENSGT00390000002865; -.
DR   HOGENOM; HBG715464; -.
DR   HOVERGEN; HBG056700; -.
DR   InParanoid; Q80TL4; -.
DR   OMA; HRGHIEW; -.
DR   OrthoDB; EOG48GW3M; -.
DR   NextBio; 457855; -.
DR   ArrayExpress; Q80TL4; -.
DR   Bgee; Q80TL4; -.
DR   CleanEx; MM_N28178; -.
DR   Genevestigator; Q80TL4; -.
DR   GermOnline; ENSMUSG00000036062; Mus musculus.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Metal-binding; Phosphoprotein; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    400       Protein KIAA1045.
FT                                /FTId=PRO_0000059332.
FT   ZN_FING     129    190       PHD-type.
FT   MOD_RES      43     43       Phosphoserine (By similarity).
FT   MOD_RES     348    348       Phosphoserine.
FT   VAR_SEQ      17     53       Missing (in isoform 2).
FT                                /FTId=VSP_014952.
SQ   SEQUENCE   400 AA;  45223 MW;  77B618690C0E4661 CRC64;
     MGVLMSKRQT VEQVQKVSLA VSAFKDGLRD RPSIRRGGEL PGSRRGTVEG SVQEVQEEKE
     AEASAPVVQE ESSINRAAWE RLRDGRGVEP EEFDRTSRFT PPAFIRPTRK LDDDKPPDIC
     LEPREPVVND EMCDVCEVWT AESLFPCRVC TRVFHDGCLR RMGYLQGDSA VEVTEMAHTE
     TGWSCYYCDN LNLLLTEEEM YSLTETFQRC KVIPDCSLTL EDFVRYRHQA AKRGESSRAL
     TDEQEEQAAR QFAALDPEQR GHVEWSDFLS HESLLLLLQL RPQNSLLRLL TVKERERARA
     TFLARGRGST ISEAECHHAR HSWFCKRLTE APSCSVSISH VGPIADSSPA ASSSKSQEKA
     LLPTEQESRY VDWPTFLREN VIYILAARPN SGAIHLKPPG
//
ID   MON2_MOUSE              Reviewed;        1715 AA.
AC   Q80TL7; Q3TRE3; Q8BTA8; Q8K4V3;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 2.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Protein MON2 homolog;
DE   AltName: Full=Protein SF21;
GN   Name=Mon2; Synonyms=Kiaa1040, Sf21;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Inagaki S.;
RT   "A novel mouse gene showing weak similarity to C. elegans F11A10.4
RT   hypothetical protein.";
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 891-1715 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   IDENTIFICATION.
RX   PubMed=16219684; DOI=10.1242/jcs.02599;
RA   Efe J.A., Plattner F., Hulo N., Kressler D., Emr S.D., Deloche O.;
RT   "Yeast Mon2p is a highly conserved protein that functions in the
RT   cytoplasm-to-vacuole transport pathway and is required for Golgi
RT   homeostasis.";
RL   J. Cell Sci. 118:4751-4764(2005).
CC   -!- FUNCTION: May be required for traffic between late Golgi and early
CC       endosomes (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80TL7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80TL7-2; Sequence=VSP_027394, VSP_027395;
CC   -!- SIMILARITY: Belongs to the MON2 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC25345.1; Type=Frameshift; Positions=1122;
CC       Sequence=BAC65707.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB014059; BAC11706.1; -; mRNA.
DR   EMBL; AK011826; BAC25345.1; ALT_FRAME; mRNA.
DR   EMBL; AK122425; BAC65707.1; ALT_INIT; mRNA.
DR   EMBL; AK162859; BAE37087.1; -; mRNA.
DR   IPI; IPI00330176; -.
DR   IPI; IPI00469486; -.
DR   RefSeq; NP_001156496.1; NM_001163024.1.
DR   RefSeq; NP_700444.2; NM_153395.2.
DR   UniGene; Mm.169924; -.
DR   UniGene; Mm.478725; -.
DR   ProteinModelPortal; Q80TL7; -.
DR   STRING; Q80TL7; -.
DR   PhosphoSite; Q80TL7; -.
DR   PRIDE; Q80TL7; -.
DR   Ensembl; ENSMUST00000037557; ENSMUSP00000037568; ENSMUSG00000034602.
DR   Ensembl; ENSMUST00000073792; ENSMUSP00000073462; ENSMUSG00000034602.
DR   GeneID; 67074; -.
DR   KEGG; mmu:67074; -.
DR   CTD; 67074; -.
DR   MGI; MGI:1914324; Mon2.
DR   GeneTree; ENSGT00390000013286; -.
DR   HOGENOM; HBG445790; -.
DR   HOVERGEN; HBG108142; -.
DR   InParanoid; Q80TL7; -.
DR   OrthoDB; EOG4NKBTP; -.
DR   PhylomeDB; Q80TL7; -.
DR   NextBio; 323498; -.
DR   ArrayExpress; Q80TL7; -.
DR   Bgee; Q80TL7; -.
DR   CleanEx; MM_MON2; -.
DR   Genevestigator; Q80TL7; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0006895; P:Golgi to endosome transport; ISS:HGNC.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR015403; DUF1981_SEC7_assoc.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 5.
DR   Pfam; PF09324; DUF1981; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1   1715       Protein MON2 homolog.
FT                                /FTId=PRO_0000297903.
FT   MOD_RES     204    204       Phosphoserine (By similarity).
FT   VAR_SEQ     820    820       Missing (in isoform 2).
FT                                /FTId=VSP_027394.
FT   VAR_SEQ    1391   1396       Missing (in isoform 2).
FT                                /FTId=VSP_027395.
FT   CONFLICT   1065   1065       V -> I (in Ref. 1; BAC11706).
FT   CONFLICT   1126   1126       T -> N (in Ref. 3; BAE37087).
FT   CONFLICT   1195   1195       L -> F (in Ref. 1; BAC11706).
SQ   SEQUENCE   1715 AA;  189078 MW;  0D4761F77C7A6490 CRC64;
     MSCTNSPEAV KKLLENMQSD LRALSLECKK KFPPVKEAAE SGIIKVKTIA ARNTEILAAL
     KENSSEVVQP FLMGCGTKEP KITQLCLAAI QRLMSHEVVS ETAAGNIINM LWQLMENSLE
     ELKLLQTVLV LLTTNTVVHD EALSKAIVLC FRLHFTKDNI TNNTAAATVR QVVTVVFERM
     VAEDDRHRDI EPPVPIQGNS NRRSVSTLRP CAKDAYMLFQ DLCQLVNADA PYWLVGMTEM
     TRTFGLELLE SVLNDFPQVF LQHQEFSFLL KERVCPLVIK LFSPNIKFRQ GSSTSSSPAP
     VEKPYFPICM RLLRVVSVLI KQFYSLLVTE CEIFLSLLVK FLDSDKPQWL RAVAVESIHR
     LCVQPQLLRS FCQSYDMKQH STKVFRDIVN ALGSFIQSLF LVPPTGNPAT ANQAGNNNAG
     GPASAPANSG VVGVGGGVTL LPAFEYRGAW IPILTVTVQG SAKATYLEML DKVEPPTIPE
     GYAMSVAFHC LLDLVRGITT MIEGELGEVE AEGPSVTEGA SSQSSERRDE QAASDPMDQE
     TVSRAVWEEM VSACWCGLLA ALSLLLDAST DEAATENILK AELTMAALCG RLGLVTSRDA
     FITAICKGSL PPHYALTVLN ATTAATLSNK SYSIQGQSVM MISPSSESHQ QVVAVGQPLA
     VQPQGTVMLT SKNIQCMRTL LNLAHCHGAV LGTSWQLVLA TLQHLVWILG LKPSSGGALK
     PGRAVEGPST VLTTAVMTDL PVISNILSRL FESSQYLDDV SLHHLINALC SLSLEAMDMA
     YGNNKEPSLF AVAKLLETGL VNMHRIEILW RPLTGHLLEK VCQHPNSRMR EWGAEALTSL
     IRAGLTFSHE PPLPQNQRLQ LLLLNPLKEM SNINHPDIRL KQLECVLQIL QSQGDSLGPG
     WPLVLGVMGA IRNDQGESLI RTAFQCLQLV VTDFLPTMPC SCLQIVVDVA GSFGLHNQEL
     NISLTSIGLL WNISDYFFQR GETIEKELNK EEAAQQKQAE EKGVSLNRPF HPAPPFDCLW
     LCLYAKLGEL CVDPRPAVRK SAGQTLFSTI GAHGTLLQHS TWHTVIWKVL FHLLDRVRES
     STTADKEKIE SGGGNILIHH SRDTAEKQWA ETWVLTLAGV ARIFNTRRYL LQPLGDFSRA
     WDVLLDHIQS AALSKNNEVS LAALKSFQEI LQIVSPVRDS EKPEPPAVSV PVPVLLGNLS
     GPGLSRPFVR TDSIGEKLGR CGSETPVVTD ELEDLKLWWA AWNTWHRTGS ESTEPPSSVD
     ELTFIPSQPF LTALVQIFPA LYQHIKAGFS MADLQKLGVI LHSAVSVPIS SDASPFILPS
     YTEAVLTSLQ EAVLTALDVL QKAICVGPEN MQIMYPAIFD QLLAFVEFSC KPPQYGQLET
     KHIANAKYNQ IQLFAPAEWV ALNYVPFAER SLEVVVDLYQ KTACHKAVVN EKVLQNIIKT
     LRVPLSLKYS CPSESTWKLA VASLLKVLSI GLPVARQHAS SGKFDSMWPE LASTLEDFLF
     TKSIPPDNLS IQEFQRNESI DVEVVQLISA EILPYANLIP KAFVGQMMTM LNKGSIHSQP
     CSFTEAEIDI RLREEFSKMC FETLLQFSFS NKVTTPQEGY ISRMALSVLL KRSQDVLHRY
     IEDERLSGKC PLPRQQVTEI IFVLKAVSTL IDSLKKTQPE NVDGNTWSQV IALYPTLVEC
     ITCSSSDVGS ALKEALAPFK DFMQPPASRV QNGES
//
ID   R3HD2_MOUSE             Reviewed;        1044 AA.
AC   Q80TM6; Q80YB1; Q8BLS5; Q9CW50;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 2.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=R3H domain-containing protein 2;
GN   Name=R3hdm2; Synonyms=Kiaa1002;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 289-1044 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 132-1044 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 57-1044 (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q80TM6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80TM6-2; Sequence=VSP_010553, VSP_010554;
CC       Name=3;
CC         IsoId=Q80TM6-3; Sequence=VSP_010553;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q80TM6-4; Sequence=VSP_010555, VSP_010556;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 R3H domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AK043545; Type=Frameshift; Positions=1010;
CC       Sequence=BAB23642.2; Type=Erroneous initiation;
CC       Sequence=BAC65698.1; Type=Erroneous initiation;
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DR   EMBL; AK122416; BAC65698.1; ALT_INIT; mRNA.
DR   EMBL; AK004884; BAB23642.2; ALT_INIT; mRNA.
DR   EMBL; AK043545; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC043083; AAH43083.1; -; mRNA.
DR   EMBL; BC064442; AAH64442.1; -; mRNA.
DR   IPI; IPI00416731; -.
DR   IPI; IPI00416732; -.
DR   IPI; IPI00416733; -.
DR   IPI; IPI00416734; -.
DR   RefSeq; NP_001161764.1; NM_001168292.1.
DR   RefSeq; NP_082176.4; NM_027900.4.
DR   UniGene; Mm.29342; -.
DR   ProteinModelPortal; Q80TM6; -.
DR   SMR; Q80TM6; 152-257.
DR   PhosphoSite; Q80TM6; -.
DR   PRIDE; Q80TM6; -.
DR   Ensembl; ENSMUST00000064793; ENSMUSP00000069724; ENSMUSG00000025404.
DR   Ensembl; ENSMUST00000077046; ENSMUSP00000076303; ENSMUSG00000025404.
DR   Ensembl; ENSMUST00000105249; ENSMUSP00000100884; ENSMUSG00000025404.
DR   Ensembl; ENSMUST00000105250; ENSMUSP00000100885; ENSMUSG00000025404.
DR   Ensembl; ENSMUST00000105251; ENSMUSP00000100886; ENSMUSG00000025404.
DR   GeneID; 71750; -.
DR   KEGG; mmu:71750; -.
DR   UCSC; uc007hjl.1; mouse.
DR   UCSC; uc007hjm.1; mouse.
DR   UCSC; uc007hjo.1; mouse.
DR   UCSC; uc007hjp.1; mouse.
DR   CTD; 71750; -.
DR   MGI; MGI:1919000; R3hdm2.
DR   GeneTree; ENSGT00440000038338; -.
DR   HOGENOM; HBG444909; -.
DR   HOVERGEN; HBG052192; -.
DR   InParanoid; Q80TM6; -.
DR   OMA; SRQGSTE; -.
DR   OrthoDB; EOG41G33F; -.
DR   PhylomeDB; Q80TM6; -.
DR   ArrayExpress; Q80TM6; -.
DR   Bgee; Q80TM6; -.
DR   CleanEx; MM_R3HDM2; -.
DR   Genevestigator; Q80TM6; -.
DR   GermOnline; ENSMUSG00000025404; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   InterPro; IPR001374; R3H_ss-bd.
DR   Pfam; PF01424; R3H; 1.
DR   SMART; SM00393; R3H; 1.
DR   PROSITE; PS51061; R3H; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Nucleus; Phosphoprotein.
FT   CHAIN         1   1044       R3H domain-containing protein 2.
FT                                /FTId=PRO_0000050788.
FT   DOMAIN      169    232       R3H.
FT   COMPBIAS    320    323       Poly-Ser.
FT   COMPBIAS    436    447       Poly-Gln.
FT   MOD_RES     380    380       Phosphoserine (By similarity).
FT   MOD_RES     921    921       Phosphoserine (By similarity).
FT   MOD_RES     923    923       Phosphoserine (By similarity).
FT   VAR_SEQ     271    302       Missing (in isoform 4).
FT                                /FTId=VSP_010555.
FT   VAR_SEQ     313    330       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_010553.
FT   VAR_SEQ     469    502       Missing (in isoform 2).
FT                                /FTId=VSP_010554.
FT   VAR_SEQ     490    502       Missing (in isoform 4).
FT                                /FTId=VSP_010556.
FT   CONFLICT     28     28       K -> R (in Ref. 2; AK043545).
FT   CONFLICT    964    964       K -> T (in Ref. 2; AK043545).
FT   CONFLICT   1015   1015       L -> I (in Ref. 2; AK043545).
FT   CONFLICT   1029   1029       A -> D (in Ref. 2; AK043545).
SQ   SEQUENCE   1044 AA;  114583 MW;  529D97E3E3EBEFBE CRC64;
     MSNSNTTQET LEIMKESEKK LVEESVNKNK FISKTPSKED VEKEGEENGL RQETQRRTSS
     HGHARKRAKS NSKLKLVRSL AVCEESSTPF VDGPLDTQDI IQLHISCPSD KEEEKSTKDV
     SEKEDKDKSK EKVPRKMLSR DSSQEYTDST GIDLHEFLVN TLKKNPRDRM MLLKLEQEIL
     DFINDNNNQF KKFPQMTSYH RMLLHRVAAY FGMDHNVDQT GKAVIINKTS STRIPEQRFS
     EHIKDEKNTE FQQRFILKRD DASMDRDDNQ MRVPLQDGRR SKSIEEREEE YQRVRERIFA
     RETGQNGYLN DIRLSKEAFS SSSHKRRQIF RGNREGLSRT SSSRQSSTDS ELKSLEPRPW
     SSTDSDGSVR SMRPPVTKAS SFSGISILTR GDSIGSSKGG SAGRLSRPGM ALGAPEVCNQ
     VTSPQSVRGL LPCTAQQQQQ QQQQQQQLPA LPPTPQHQPP LNNHMISQPV PALQPSPQPV
     QFSPSSCPQV LLPVSPPQQY NMAEDLSNPF GQMSLSRQGS TEAADPSSAL FQPPLISQHP
     QQASFIMASA GQPLPTSNYS TSSHAPPTQQ VLPPQGYMQP PQQIQVSYYP PGQYPNSNQQ
     YRPLSHPVAY SPQRGQQLPQ ASQQPGLQPM MSNQQQTAYQ GMLGVQQPQN QGLLSNQRSS
     MGGQMQGLVV QYTPLPSYQV PVGSDSQNVV QPSFQQPMLV PASQSVQGGL PTGGVPVYYS
     MIPPAQQNGT SPSVGFLQPP GSEQYQMPQS PSPCSPPQMS QQYSGVSPSG PGVVVMQLNV
     PNGPQAPQNP SMVQWSHCKY YSVEQRGQKP GDLYSPDGSP QANAQMGSSP VTSPTQSPAP
     SPVTSLSNVC TGLSPLPVLT PFPRPGGPAQ GDGRYSLLGQ PLQYNLSICP PLLHGQSTYT
     VHQGQSGLKH GNRGKRQALK SASTDLGTAD VVLGRVLEVT DLPEGITRTE ADKLFTQLAM
     SGAKIQWLKD AQGLPGAGGG DNSGTAENGR HPDLAALYTI VAVFPSPLAA QNASLRLNNS
     VSRFKLRVAK KNYDLRILER ASSQ
//
ID   NISCH_MOUSE             Reviewed;        1593 AA.
AC   Q80TM9; Q2YDV7; Q8C354; Q8C4X9; Q8CBH0; Q91XW6; Q99LG6; Q9EPW8;
AC   Q9WUM6;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Nischarin;
DE   AltName: Full=Imidazoline receptor 1;
DE            Short=I-1;
DE            Short=IR1;
DE   AltName: Full=Imidazoline receptor I-1-like protein;
DE   AltName: Full=Imidazoline-1 receptor;
DE            Short=I1R;
GN   Name=Nisch; Synonyms=Kiaa0975;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH
RP   ITGA5, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=20571837; PubMed=11121431; DOI=10.1083/jcb.151.6.1141;
RA   Alahari S.K., Lee J.W., Juliano R.L.;
RT   "Nischarin, a novel protein that interacts with the integrin alpha5
RT   subunit and inhibits cell migration.";
RL   J. Cell Biol. 151:1141-1154(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 7).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 215-1593 (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1238-1593 (ISOFORM 1).
RC   TISSUE=Carcinoma;
RA   Bailey T.L., Smith D.R., McGaugh B.D., Mitchell J.;
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1386-1593 (ISOFORM 1).
RC   TISSUE=Lung;
RA   Cain D., Carter J., McLean W., Robbins L.;
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   FUNCTION.
RX   PubMed=12915132; DOI=10.1016/S0014-4827(03)00233-7;
RA   Alahari S.K.;
RT   "Nischarin inhibits Rac induced migration and invasion of epithelial
RT   cells by affecting signaling cascades involving PAK.";
RL   Exp. Cell Res. 288:415-424(2003).
RN   [9]
RP   INTERACTION WITH ITGA5.
RX   PubMed=14535848; DOI=10.1042/BJ20030411;
RA   Alahari S.K., Nasrallah H.;
RT   "A membrane proximal region of the integrin alpha5 subunit is
RT   important for its interaction with nischarin.";
RL   Biochem. J. 377:449-457(2004).
RN   [10]
RP   FUNCTION, IDENTIFICATION IN A COMPLEX WITH ITGA5 AND PAK1, INTERACTION
RP   WITH PAK1, AND SUBCELLULAR LOCATION.
RX   PubMed=15229651; DOI=10.1038/sj.emboj.7600291;
RA   Alahari S.K., Reddig P.J., Juliano R.L.;
RT   "The integrin-binding protein Nischarin regulates cell migration by
RT   inhibiting PAK.";
RL   EMBO J. 23:2777-2788(2004).
RN   [11]
RP   FUNCTION, INTERACTION WITH RAC1, AND SUBCELLULAR LOCATION.
RX   PubMed=16002401; DOI=10.1074/jbc.M502546200;
RA   Reddig P.J., Xu D., Juliano R.L.;
RT   "Regulation of p21-activated kinase-independent Rac1 signal
RT   transduction by Nischarin.";
RL   J. Biol. Chem. 280:30994-31002(2005).
RN   [12]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16678176; DOI=10.1016/j.febslet.2006.04.058;
RA   Zhang J., Abdel-Rahman A.A.;
RT   "Nischarin as a functional imidazoline (I1) receptor.";
RL   FEBS Lett. 580:3070-3074(2006).
RN   [13]
RP   FUNCTION, IDENTIFICATION IN A COMPLEX WITH LIMK1 AND PAK1, AND
RP   INTERACTION WITH LIMK1 AND LIMK2.
RX   PubMed=18332102; DOI=10.1128/MCB.01832-07;
RA   Ding Y., Milosavljevic T., Alahari S.K.;
RT   "Nischarin inhibits LIM kinase to regulate cofilin phosphorylation and
RT   cell invasion.";
RL   Mol. Cell. Biol. 28:3742-3756(2008).
CC   -!- FUNCTION: Acts either as the functional imidazoline-1 receptor
CC       (I1R) candidate or as a membrane-associated mediator of the I1R
CC       signaling. Binds numerous imidazoline ligands that induces
CC       initiation of cell-signaling cascades triggering to cell survival,
CC       growth and migration. Its activation by the agonist rilmenidine
CC       induces an increase in phosphorylation of mitogen-activated
CC       protein kinases MAPK1 and MAPK3 in rostral ventrolateral medulla
CC       (RVLM) neurons that exhibited rilmenidine-evoked hypotension (By
CC       similarity). Blocking its activation with efaroxan abolished
CC       rilmenidine-induced mitogen-activated protein kinase
CC       phosphorylation in RVLM neurons (By similarity). Acts as a
CC       modulator of Rac-regulated signal transduction pathways.
CC       Suppresses Rac1-stimulated cell migration by interacting with PAK1
CC       and inhibiting its kinase activity. Also blocks Pak-independent
CC       Rac signaling by interacting with RAC1 and inhibiting Rac1-
CC       stimulated NF-kB response element and cyclin D1 promoter
CC       activation. Inhibits also LIMK1 kinase activity by reducing LIMK1
CC       'Tyr-508' phosphorylation. Inhibits Rac-induced cell migration and
CC       invasion in breast and colon epithelial cells. Inhibits
CC       lamellipodia formation, when overexpressed. Plays a role in
CC       protection against apoptosis (By similarity). Involved in
CC       association with IRS4 in the enhancement of insulin activation of
CC       MAPK1 and MAPK3 (By similarity). When overexpressed, induces a
CC       redistribution of cell surface ITGA5 integrin to intracellular
CC       endosomal structures (By similarity).
CC   -!- SUBUNIT: Homooligomer (By similarity). Interacts with GRB2 (By
CC       similarity). Interacts with PIK3R1; probably associates with the
CC       PI3-kinase complex (By similarity). Interacts with IRS4 (By
CC       similarity). Found in a complex with ITGA5 and PAK1. Found in a
CC       complex with LIMK1 and PAK1. Interacts with ITGA5 (via cytoplasmic
CC       domain); this interaction is direct. Interacts with PAK1 (via
CC       kinase domain); this interaction is direct and is increased upon
CC       activation of PAK1. Interacts with LIMK1 (via PDZ and kinase
CC       domain); this interaction is direct. Interacts with LIMK2; this
CC       interaction depends on LIMK2 activity. Interacts with RAC1
CC       (activated state).
CC   -!- SUBCELLULAR LOCATION: Cell membrane (By similarity). Cytoplasm.
CC       Early endosome (By similarity). Recycling endosome (By
CC       similarity). Note=Enriched in the early/sorting and recycling
CC       endosomes (By similarity). Colocalized in early/sorting endosomes
CC       with EEA1 and SNX2 and in recycling endosomes with transferrin
CC       receptor (By similarity). Colocalized with MAPK1 and MAPK3 in RVLM
CC       neurons (By similarity). Detected in the perinuclear region
CC       partially associated with punctate structures. Colocalizes with
CC       PAK1 in cytoplasm, vesicular structures in the perinuclear area
CC       and membrane ruffles. Colocalizes with RAC1 in the cytoplasm and
CC       vesicles structures.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=1;
CC         IsoId=Q80TM9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80TM9-2; Sequence=VSP_035141;
CC       Name=3;
CC         IsoId=Q80TM9-3; Sequence=VSP_035136;
CC       Name=4;
CC         IsoId=Q80TM9-4; Sequence=VSP_035142, VSP_035143;
CC       Name=5;
CC         IsoId=Q80TM9-5; Sequence=VSP_035139, VSP_035140;
CC         Note=No experimental confirmation available;
CC       Name=6;
CC         IsoId=Q80TM9-6; Sequence=VSP_035144, VSP_035145;
CC       Name=7;
CC         IsoId=Q80TM9-7; Sequence=VSP_035137, VSP_035138;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and kidney.
CC       Moderately expressed in heart, liver, lung and skeletal muscle.
CC       Not detected in spleen and testis.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryo at 7 day dpc onwards.
CC   -!- DOMAIN: Both the presence of the PX domain and the coiled coil
CC       region are necessary for its endosomal targeting (By similarity).
CC   -!- MISCELLANEOUS: 'Nischarin' means 'slowness of motion' in classic
CC       Sanskrit.
CC   -!- SIMILARITY: Contains 6 LRR (leucine-rich) repeats.
CC   -!- SIMILARITY: Contains 1 PX (phox homology) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH03270.1; Type=Erroneous initiation;
CC       Sequence=AAI08365.1; Type=Frameshift; Positions=1550;
CC       Sequence=AAK52087.1; Type=Erroneous initiation;
CC       Sequence=BAC65694.1; Type=Erroneous initiation;
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DR   EMBL; AF315344; AAG42100.1; -; mRNA.
DR   EMBL; AK122412; BAC65694.1; ALT_INIT; mRNA.
DR   EMBL; AK036043; BAC29286.1; -; mRNA.
DR   EMBL; AK080441; BAC37917.1; -; mRNA.
DR   EMBL; AK086880; BAC39757.1; -; mRNA.
DR   EMBL; AC108416; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154446; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC003270; AAH03270.1; ALT_INIT; mRNA.
DR   EMBL; BC108364; AAI08365.1; ALT_FRAME; mRNA.
DR   EMBL; AY032852; AAK52087.1; ALT_INIT; mRNA.
DR   EMBL; AF144133; AAD31521.1; -; mRNA.
DR   IPI; IPI00110435; -.
DR   IPI; IPI00459191; -.
DR   IPI; IPI00903350; -.
DR   IPI; IPI00903374; -.
DR   IPI; IPI00903378; -.
DR   IPI; IPI00903425; -.
DR   IPI; IPI00903427; -.
DR   RefSeq; NP_073147.2; NM_022656.2.
DR   UniGene; Mm.298728; -.
DR   ProteinModelPortal; Q80TM9; -.
DR   SMR; Q80TM9; 19-122, 174-449.
DR   PhosphoSite; Q80TM9; -.
DR   PRIDE; Q80TM9; -.
DR   Ensembl; ENSMUST00000022469; ENSMUSP00000022469; ENSMUSG00000021910.
DR   GeneID; 64652; -.
DR   KEGG; mmu:64652; -.
DR   UCSC; uc007swz.1; mouse.
DR   CTD; 64652; -.
DR   MGI; MGI:1928323; Nisch.
DR   eggNOG; roNOG04597; -.
DR   HOVERGEN; HBG108189; -.
DR   InParanoid; Q80TM9; -.
DR   OMA; GPFGTSN; -.
DR   OrthoDB; EOG4N5VW2; -.
DR   NextBio; 320127; -.
DR   ArrayExpress; Q80TM9; -.
DR   Bgee; Q80TM9; -.
DR   Genevestigator; Q80TM9; -.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005178; F:integrin binding; IDA:MGI.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IDA:MGI.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   GO; GO:0030336; P:negative regulation of cell migration; IDA:MGI.
DR   GO; GO:0016601; P:Rac protein signal transduction; IDA:MGI.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR001683; Phox.
DR   Gene3D; G3DSA:3.30.1520.10; PX; 1.
DR   Pfam; PF00560; LRR_1; 2.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; PX; 1.
DR   PROSITE; PS51450; LRR; 6.
DR   PROSITE; PS50195; PX; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Apoptosis; Cell membrane;
KW   Coiled coil; Cytoplasm; Endosome; Leucine-rich repeat; Membrane;
KW   Phosphoprotein; Receptor; Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1593       Nischarin.
FT                                /FTId=PRO_0000348266.
FT   DOMAIN       12    122       PX.
FT   REPEAT      288    311       LRR 1.
FT   REPEAT      312    333       LRR 2.
FT   REPEAT      334    358       LRR 3.
FT   REPEAT      360    378       LRR 4.
FT   REPEAT      379    402       LRR 5.
FT   REPEAT      403    426       LRR 6.
FT   REPEAT     1081   1086       1.
FT   REPEAT     1087   1092       2.
FT   REPEAT     1093   1098       3.
FT   REPEAT     1099   1104       4.
FT   REPEAT     1105   1110       5.
FT   REPEAT     1111   1116       6.
FT   REPEAT     1123   1128       7.
FT   REPEAT     1129   1134       8.
FT   REPEAT     1135   1140       9.
FT   REPEAT     1141   1146       10.
FT   REGION        2    134       Necessary for binding to
FT                                phosphoinositide-3-P; not sufficient for
FT                                targeting to endosomes (By similarity).
FT   REGION      121    695       Necessary for homooligomerization and
FT                                targeting to endosomes (By similarity).
FT   REGION      246    869       Interaction with PAK1.
FT   REGION      661    869       Interaction with LIMK.
FT   REGION      709    807       Interaction with ITGA5.
FT   REGION     1081   1146       10 X 6 AA tandem repeat of A-E-A-P-A-A.
FT   COILED      624    694       Potential.
FT   COMPBIAS    631    691       Glu-rich.
FT   COMPBIAS   1041   1193       Ala/Pro-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES    1373   1373       Phosphoserine (By similarity).
FT   VAR_SEQ       1    245       Missing (in isoform 3).
FT                                /FTId=VSP_035136.
FT   VAR_SEQ     122    153       EVNGVTAALAEELFEKGEQLLGAGEVFAIRPL -> VSSFG
FT                                ALCFAYEPTATKAVGLGFEETQTGPWP (in isoform
FT                                7).
FT                                /FTId=VSP_035137.
FT   VAR_SEQ     154   1593       Missing (in isoform 7).
FT                                /FTId=VSP_035138.
FT   VAR_SEQ     332    334       HLY -> ATS (in isoform 5).
FT                                /FTId=VSP_035139.
FT   VAR_SEQ     335   1593       Missing (in isoform 5).
FT                                /FTId=VSP_035140.
FT   VAR_SEQ     348    500       Missing (in isoform 2).
FT                                /FTId=VSP_035141.
FT   VAR_SEQ     437    472       ICLDDVATTEKELDTVEVLKAIQKAKDVKSKLSNTE -> V
FT                                SPRSSSRAQRDWQGKPSLSAKADRGKAVHSVLVFF (in
FT                                isoform 4).
FT                                /FTId=VSP_035142.
FT   VAR_SEQ     473   1593       Missing (in isoform 4).
FT                                /FTId=VSP_035143.
FT   VAR_SEQ     513    516       MFVQ -> LGDE (in isoform 6).
FT                                /FTId=VSP_035144.
FT   VAR_SEQ     517   1593       Missing (in isoform 6).
FT                                /FTId=VSP_035145.
FT   CONFLICT    607    607       R -> P (in Ref. 2; BAC65694).
FT   CONFLICT   1123   1128       Missing (in Ref. 2; BAC65694).
FT   CONFLICT   1172   1172       R -> RGPAPAG (in Ref. 1; AAG42100).
FT   CONFLICT   1518   1518       A -> G (in Ref. 6; AAK52087).
SQ   SEQUENCE   1593 AA;  175012 MW;  90B407A165A4C1F8 CRC64;
     MAAATLSFGP EREAEPAKEA RVVGSELVDT YTVYVIQVTD GNHEWTIKHR YSDFHDLHEK
     LVAERKIDKS LLPPKKIIGK NSRSLVEKRE RDLEVYLQTL LTTFPDVAPR VLAHFLHFHL
     YEVNGVTAAL AEELFEKGEQ LLGAGEVFAI RPLQLYAITE QLQQGKPTCA SGDAKTDLGH
     ILDFTCRLKY LKVSGTEGPF GTSNIKEQLL PFDLSIFKSL HQVEISHCDA KHIRGLVTSK
     PTLATMSVRF SATSMKEVLA PEASEFDEWE PEGTATLGGP VTAIIPTWQA LTTLDLSHNS
     ICEIDESVKL IPKIEYLDLS HNGLRVVDNL QHLYNLVHLD LSYNKLSSLE GVHTKLGNVK
     TLNLAGNFLE SLSGLHKLYS LVNVDLRDNR IEQLDEVKSI GSLPCLERLT LLNNPLSIIP
     DYRTKVLSQF GERASEICLD DVATTEKELD TVEVLKAIQK AKDVKSKLSN TEKKAGEDFR
     LPPAPCIRPG GSPPAAPASA SLPQPILSNQ GIMFVQEEAL ASSLSSTDSL PPEDHRPIAR
     ACSDSLESIP AGQVASDDLR DVPGAVGGVS PDHAEPEVQV VPGSGQIIFL PFTCIGYTAT
     NQDFIQRLST LIRQAIERQL PAWIEAANQR EEAHGEQGEE EEEEEEEEDV AENRYFEMGP
     PDAEEEEGSG QGEEDEEDED EEAEEERLAL EWALGADEDF LLEHIRILKV LWCFLIHVQG
     SIRQFAACLV LTDFGIAVFE IPHQESRGSS QHILSSLRFV FCFPHGDLTE FGFLMPELCL
     VLKVRHSENT LFIISDAANL HEFHADLRSC FAPQHMAMLC SPILYGSHTT LQEFLRQLLT
     FYKVAGGSQE RSQGCFPVYL VYSDKRMVQT PAGDYSGNIE WASCTLCSAV RRSCCAPSEA
     VKSAAIPYWL LLTSQHLNVI KADFNPMPNR GTHNCRNRNS FKLSRVPLST VLLDPTRSCT
     QPRGAFADGH VLELLVGYRF VTAIFVLPHE KFHFLRVYNQ LRASLQDLKT VVISKNPSAK
     PRNQPAKSRA SAEQRLQETP ADAPAPAAVP PTASAPAPAE ALAPDLAPVQ APGEDRGLTS
     AEAPAAAEAP AAAEAPAAAE APAAAEAPAA AEAPAAAEAP APAEAPAAAE APAAAEAPAA
     AEAPAAAEAP ASAEAPAPNQ APAPARGPAP ARGPAPAGGP APAEALAQAE VPAQYPSERL
     IQSTSEENQI PSHLPVCPSL QHIARLRGRA IIDLFHNSIA EVENEELRHL LWSSVVFYQT
     PGLEVTACVL LSSKAVYFIL HDGLRRYFSE PLQDFWHQKN TDYNNSPFHV SQCFVLKLSD
     LQSVNVGLFD QYFRLTGSSP TQVVTCLTRD SYLTHCFLQH LMLVLSSLER TPSPEPVDKD
     FYSEFGDKNT GKMENYELIH SSRVKFTYPS EEEVGDLTYI VAQKMADPAK NPALSILLYI
     QAFQVVTPHL GRGRGPLRPK TLLLTSAEIF LLDEDYIHYP LPEFAKEPPQ RDRYRLDDGR
     RVRDLDRVLM GYYPYPQALT LVFDDTQGHD LMGSVTLDHF GEMPGGPGRV GQGREVQWQV
     FVPSAESREK LISLLARQWE ALCGRELPVE LTG
//
ID   NAV3_MOUSE              Reviewed;        2359 AA.
AC   Q80TN7;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=Neuron navigator 3;
DE   AltName: Full=Pore membrane and/or filament-interacting-like protein 1;
GN   Name=Nav3; Synonyms=Kiaa0938, Pomfil1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 724-2359.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   PROTEIN SEQUENCE OF 1173-1182, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   IDENTIFICATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP   DEVELOPMENTAL STAGE, INDUCTION, AND FUNCTION.
RX   PubMed=12062803; DOI=10.1016/S0378-1119(02)00567-X;
RA   Coy J.F., Wiemann S., Bechmann I., Baechner D., Nitsch R., Kretz O.,
RA   Christiansen H., Poustka A.;
RT   "Pore membrane and/or filament interacting like protein 1 (POMFIL1) is
RT   predominantly expressed in the nervous system and encodes different
RT   protein isoforms.";
RL   Gene 290:73-94(2002).
CC   -!- FUNCTION: May regulate IL2 production by T-cells. May be involved
CC       in neuron regeneration.
CC   -!- SUBCELLULAR LOCATION: Nucleus outer membrane.
CC   -!- TISSUE SPECIFICITY: Present in neurons from central and peripheral
CC       nervous systems (at protein level). Highly expressed in brain
CC       cortex, midbrain, cerebellum and hippocampus.
CC   -!- DEVELOPMENTAL STAGE: Specifically expressed in neuronal cells
CC       during development. First detectable at E9.5 in prosencephalon. At
CC       E16.5, expressed in all brain areas, spinal cord and spinal
CC       ganglia. Within the brain, highest expression is found in maturing
CC       zones where neurons differentiate and lowest expression is found
CC       in ventricular zones where proliferation takes place. Brain
CC       expression remains high at later embryonic stages and during
CC       postnatal brain development.
CC   -!- INDUCTION: In astrocytes after brain injury.
CC   -!- SIMILARITY: Belongs to the Nav/unc-53 family.
CC   -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65686.1; Type=Erroneous termination; Positions=978; Note=Translated as Gln;
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DR   EMBL; AC100120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC122011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC129336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK122404; BAC65686.1; ALT_SEQ; mRNA.
DR   IPI; IPI00138068; -.
DR   UniGene; Mm.225050; -.
DR   UniGene; Mm.394160; -.
DR   UniGene; Mm.461280; -.
DR   ProteinModelPortal; Q80TN7; -.
DR   SMR; Q80TN7; 77-188, 2014-2118.
DR   STRING; Q80TN7; -.
DR   PhosphoSite; Q80TN7; -.
DR   PRIDE; Q80TN7; -.
DR   Ensembl; ENSMUST00000032719; ENSMUSP00000032719; ENSMUSG00000020181.
DR   MGI; MGI:2183703; Nav3.
DR   eggNOG; roNOG04082; -.
DR   GeneTree; ENSGT00530000063334; -.
DR   HOGENOM; HBG713155; -.
DR   HOVERGEN; HBG058814; -.
DR   InParanoid; Q80TN7; -.
DR   OrthoDB; EOG4C5CJH; -.
DR   ArrayExpress; Q80TN7; -.
DR   Bgee; Q80TN7; -.
DR   CleanEx; MM_NAV3; -.
DR   Genevestigator; Q80TN7; -.
DR   GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR001715; CH-domain.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF00307; CH; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00033; CH; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS50021; CH; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Direct protein sequencing; Membrane; Nucleus.
FT   CHAIN         1   2359       Neuron navigator 3.
FT                                /FTId=PRO_0000286977.
FT   DOMAIN       77    184       CH.
FT   COILED      680    708       Potential.
FT   COILED     1565   1656       Potential.
FT   COILED     1768   1835       Potential.
FT   COMPBIAS    619    622       Poly-Gln.
FT   COMPBIAS   1035   1563       Ser-rich.
FT   COMPBIAS   1697   1702       Poly-Lys.
SQ   SEQUENCE   2359 AA;  252301 MW;  4C5F57AFC87D3367 CRC64;
     MPVLGVASKL RQPAVGPKPV HAALPIPNLG ISVSRRCSSR PLEFATPERS MLSCQLTLKS
     TCEFGEKKAL QGTAKEIEDS KIYTDWANHY LAKSGHKRLI KDLQQDIADG VLLADIIQII
     ANEKVEDING CPRSQSQMIE NVDVCLSFLA ARGVNVQGLS AEEIRNGNLK AILGLFFSLS
     RYKQQQHHQQ QYYQSLVELQ QRVTHTAPQS EASQAKTQQD MQSSLTARYA AQSKHSGIAT
     SQKKPTRLPG PSRVPAASSS NKAQGASNLN RRSQSFNSID KNKPPNYANG NEKDSPKGPQ
     PSSGINGNTQ PPSTSGQPPA SAIPSPSASK PWRSKSMNVK HSATSTMLTV KQPSPATSPT
     PSSDRLKPPV TEGVKSAPSG QKSMLEKFKL VNARTALRPP QAPSSGPNDG GREDDAFSES
     GEMEGFNSGL NSGGSTNSSP KVSPKLTPPK AGSKNFSNKK SLLQPKEKEE KTRDKNKACA
     EKSGKEEKDQ VTTEAAPKKT SKIASLIPKG SKTAAAKKES LIPSSSGIPK PGSKVPTPKQ
     TISPGSAASK ESEKFRTSKG SSSQAFPKAI TAEKASTPSL STPLDGREAG QASPSSSCVM
     QVTHSSGQSP GNGAVQLPQQ QQHSHPNTAT VAPFIYRAHS ENEGTSLPPA DSCTSPTKMD
     SSYSKTAKQC LEEISGEDPE ARRMRTVKNI ADLRQNLEET MSSLRGTQIS HSTLETTFDT
     TVTTEVNGRA IPNLTSRPSP MTWRLGQACP RLQAGDAPSM GAGYSRSGTS RFIHTDPSRF
     MYTTPLRRAA VSRLGNMSQI DMSEKASSDL DVSSEVDVGG YMSDGDILGK SLRADDINSG
     YMTDGGLNLY TRSLNRVPDT ATSRDVIQRG VHDVTVDADS WDDSSSVSSG LSDTLDNIST
     DDLNTTSSIS SYSNITVPSR KNTQLKTDAE KRSTTDETWD SPEELKKAEG DCDSHGDGAA
     KWKGATSGLA EDSEKTGQKA SLSVSQTGSW RRGMSAQGGT PATARQKTST SALKTPGKTD
     DAKASEKGKT PLKGSSLQRS PSDAGKSSGD EGKKPPSGIG RSTASSSFGY KKPSGVGAST
     MITSSGATIT SGSATLGKIP KSAAIGGKSN AGRKTSLDGS QNQDDVVLHV SSKTTLQYRS
     LPRPSKSSTS GIPGRGGHRS STSSIDSNVS SKSAGATTSK LREPTKIGSG RSSPVTVNQT
     DKEKEKVAVS DSESVSLSGS PKSSPTSASA CGTQGLRQPG SKYPDIASPT FRRLFGAKAG
     GKSASAPNTE GAKSSSVVLS PSTSLARQGS LESPSSGTGS MGSAGGLSGS SSPLFNKPSD
     LTTDVISLSH SLASSPASVH SFTSGGLVWA ANLSSSSAGS KDTPSYQSMT SLHTSSESID
     LPLSHHGSLS GLTTGTHEVQ SLLMRTGSVR STLSESMQLD RNTLPKKGLR YTPSSRQANQ
     EEGKEWLRSH STGGLQDTGN QSPLVSPSAM SSSATGKYHF SNLVSPTNLS QFNLPAPSMM
     RSSSIPAQDS SFDLYDDAQL CGSATSLEER PRAVSHSGSF RDSMEEVHGS SLSLVSSTSS
     LYSTAEEKAH SEQIHKLRRE LVASQEKVAT LTSQLSANAH LVAAFEKSLG NMTGRLQSLT
     MTAEQKESEL IELRETIEML KAQNSAAQAA IQGALNGPDH PPKDLRIRRQ HSSESVSSIN
     SATSHSSIGS GNDADSKKKK KKNWLRSSFK QAFGKKKSTK PPSSHSDIEE LTDSSLPASP
     KLPHNAGESG SSSMKPSQSA SAICECTEAE AEIILQLKSE LREKELKLTD IRLEALSSAH
     HLDQIREAMN RMQNEIEILK AENDRLKAET GNTAKPARPP SDSSSTASSS SSRQSLGLSL
     NNLNITESVT SDILLDDTGD ATGHKDGRSV KIIVSISKGY GRAKDQKSQA YLIGSIGVSG
     KTKWDVLDGV IRRLFKEYVF RIDTSSSLGL SSDCIASYCI GDLIRSHNLE VPELLPCGYL
     VGDNNIITVN LKGVEENSLD SFVFDTLIPK PITQRYFNLL MEHHRIILSG PSGTGKTYLA
     NKLAEYVITK SGRKKTEDAI ATFNVDHKSS KELQQYLANL AEQCSADNNG VELPVVIILD
     NLHHVGSLSD IFNGFLNCKY NKCPYIIGTM NQGVSSSPNL ELHHNFRWVL CANHTEPVKG
     FLGRYLRRKL IEMEIERNIR NNDLVKIIDW IPKTWHHLNS FLETHSSSDV TIGPRLFLPC
     PMDVEGSRVW FMDLWNYSLV PYVLEAVREG LQMYGKRAPW EDPSKWVLDT YPWSSASLPQ
     EGPALLQLRP EDVGYEACTS TKEATTSKHI PQTDTEGDPL MNMLMKLQEA ANYPSTQSCD
     GDSVSHREDI LDTSIESTL
//
ID   Q80TP9_MOUSE            Unreviewed;       899 AA.
AC   Q80TP9;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   30-NOV-2010, entry version 29.
DE   SubName: Full=MKIAA0874 protein;
DE   Flags: Fragment;
GN   Name=Ankrd12; Synonyms=AI447928, mKIAA0874;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
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DR   EMBL; AK122392; BAC65674.1; -; mRNA.
DR   IPI; IPI00330318; -.
DR   RefSeq; NP_001020743.1; NM_001025572.1.
DR   UniGene; Mm.34706; -.
DR   UniGene; Mm.441953; -.
DR   Ensembl; ENSMUST00000038116; ENSMUSP00000039035; ENSMUSG00000034647.
DR   GeneID; 106585; -.
DR   KEGG; mmu:106585; -.
DR   CTD; 106585; -.
DR   MGI; MGI:1914357; Ankrd12.
DR   HOGENOM; HBG446071; -.
DR   InParanoid; Q80TP9; -.
DR   ArrayExpress; Q80TP9; -.
DR   Bgee; Q80TP9; -.
DR   Genevestigator; Q80TP9; -.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   899 AA;  100377 MW;  8D814934865DFD72 CRC64;
     SNRSQSVDNR NVLNLGKPSY ISESGSNRSP RSEGERLGLS SRSVSMLSVA SSEDSCHTVT
     TPRPLVEYDS DFMLEGSESQ LSFSQSPFLP NAKSPALYER ELEGLTELPD RLKPPYTNRL
     PVCHLRSSSV EDVKLITNEV RPAVEIRRCS MPSVICEPIK HFQVSEESSQ GNLAVPRETC
     LSPKPEVSSA VPERGLSHVS DLHPNCTGSP TRSANSSYIS SDVNVIKSAT LVGTLIDSSM
     HLEPSNQVGV IPSKSWETPV DKLESLSTND FICPDSNISD QDSSAQSFYN SENKMLREQN
     TDCLPPHQPE LPGNSCAQDP ASFLSSPQPC SFSNQPLAGA DSVPKPVSLS YVVSQEPGVL
     QQKSAAQMAS SVLDSDNNFP EDVENTFVLA DIQKTNSFLP AYSESTVQEA LPSFEKANTL
     LVLPSEKDFN GSDTAQPNTH YAFSKLTYKS SNSQEIEKGP DDTQIISHEK ENKLQSLVLT
     QLSKCDSDLY EMNAGLPKGN LNEQDNPKHG LDSEKYSLST EDEESQQSTL SSVENHSQQS
     AQPEMHKYDQ LSKVELEENA EDDKTENQTP QRVTRNKAST VVNPSKPMLA GCALVAEKDN
     ESSPRGRIRL TEEDDPQIHH PRKRKVSRVP QPVQVSPSLL QAKEKTQQSL AAIVDSLKLD
     EIEPYSSERA NPYFEYLHIR KKIEEKRKLL CSVIPQAPQY YDEYVTFNGS YLLDGNPLSK
     ICIPTITPPP SLSDPLKELF RQQEVVRMKL RLQHSIEREK LIVSNEQEVL RVHYRAARTL
     ANQTLPFSAC TVLLDAEVYN VPLDSQSDDS KTSVRDRFNA RQFMSWLQDV DDKFDKLKTC
     LLMRQQHEAA ALNAVQRLEW QLKLQELDPA TYKSLSIYEI QEFYVPLVDV NDDFELTPI
//
ID   CYLD_MOUSE              Reviewed;         952 AA.
AC   Q80TQ2; Q80VB3; Q8BXZ3; Q8BYL9; Q8CGB0;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase CYLD;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme CYLD;
DE   AltName: Full=Ubiquitin thiolesterase CYLD;
DE   AltName: Full=Ubiquitin-specific-processing protease CYLD;
GN   Name=Cyld; Synonyms=Cyld1, Kiaa0849;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-620 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH BCL3, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=16713561; DOI=10.1016/j.cell.2006.03.041;
RA   Massoumi R., Chmielarska K., Hennecke K., Pfeifer A., Fassler R.;
RT   "Cyld inhibits tumor cell proliferation by blocking Bcl-3-dependent
RT   NF-kappaB signaling.";
RL   Cell 125:665-677(2006).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16501569; DOI=10.1038/ni1315;
RA   Reiley W.W., Zhang M., Jin W., Losiewicz M., Donohue K.B.,
RA   Norbury C.C., Sun S.C.;
RT   "Regulation of T cell development by the deubiquitinating enzyme
RT   CYLD.";
RL   Nat. Immunol. 7:411-417(2006).
RN   [6]
RP   FUNCTION, INTERACTION WITH MAP3K7, AND DISRUPTION PHENOTYPE.
RX   PubMed=17548520; DOI=10.1084/jem.20062694;
RA   Reiley W.W., Jin W., Lee A.J., Wright A., Wu X., Tewalt E.F.,
RA   Leonard T.O., Norbury C.C., Fitzpatrick L., Zhang M., Sun S.C.;
RT   "Deubiquitinating enzyme CYLD negatively regulates the ubiquitin-
RT   dependent kinase Tak1 and prevents abnormal T cell responses.";
RL   J. Exp. Med. 204:1475-1485(2007).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18643924; DOI=10.1111/j.1462-5822.2008.01204.x;
RA   Lim J.H., Ha U.H., Woo C.H., Xu H., Li J.D.;
RT   "CYLD is a crucial negative regulator of innate immune response in
RT   Escherichia coli pneumonia.";
RL   Cell. Microbiol. 10:2247-2256(2008).
RN   [8]
RP   DISRUPTION PHENOTYPE, FUNCTION, INTERACTION WITH SQSTM1,
RP   IDENTIFICATION IN A COMPLEX WITH TRAF6 AND SQSTM1, AND INDUCTION.
RX   PubMed=18382763; DOI=10.1172/JCI34257;
RA   Jin W., Chang M., Paul E.M., Babu G., Lee A.J., Reiley W., Wright A.,
RA   Zhang M., You J., Sun S.C.;
RT   "Deubiquitinating enzyme CYLD negatively regulates RANK signaling and
RT   osteoclastogenesis in mice.";
RL   J. Clin. Invest. 118:1858-1866(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [10]
RP   FUNCTION.
RX   PubMed=20194890; DOI=10.1182/blood-2009-10-248526;
RA   Gao J., Sun L., Huo L., Liu M., Li D., Zhou J.;
RT   "CYLD regulates angiogenesis by mediating vascular endothelial cell
RT   migration.";
RL   Blood 115:4130-4137(2010).
RN   [11]
RP   FUNCTION, INTERACTION WITH HDAC6, BCL3 AND MICROTUBULES, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=19893491; DOI=10.1038/emboj.2009.317;
RA   Wickstrom S.A., Masoumi K.C., Khochbin S., Fassler R., Massoumi R.;
RT   "CYLD negatively regulates cell-cycle progression by inactivating
RT   HDAC6 and increasing the levels of acetylated tubulin.";
RL   EMBO J. 29:131-144(2010).
CC   -!- FUNCTION: Protease that specifically cleaves 'Lys-63'-linked
CC       polyubiquitin chains. Has endodeubiquitinase activity. Plays an
CC       important role in the regulation of pathways leading to NF-kappa-B
CC       activation. Contributes to the regulation of cell survival,
CC       proliferation and differentiation via its effects on NF-kappa-B
CC       activation. Negative regulator of Wnt signaling. Inhibits HDAC6
CC       and thereby promotes acetylation of alpha-tubulin and
CC       stabilization of microtubules. Plays a role in the regulation of
CC       microtubule dynamics, and thereby contributes to the regulation of
CC       cell proliferation, cell polarization, cell migration, and
CC       angiogenesis. Required for normal cell cycle progress and normal
CC       cytokinesis. Inhibits nuclear translocation of NF-kappa-B (By
CC       similarity). Plays a role in the regulation of inflammation and
CC       the innate immune response, via its effects on NF-kappa-B
CC       activation. Dispensable for the maturation of intrathymic natural
CC       killer cells, but required for the continued survival of immature
CC       natural killer cells. Negatively regulates TNFRSF11A signaling and
CC       osteoclastogenesis.
CC   -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- SUBUNIT: Interacts (via CAP-Gly domain) with IKBKG/NEMO (via
CC       proline-rich C-terminal region). Interacts with TRAF2 and TRIP.
CC       Interacts with PLK1, DVL1, DVL3, MAVS, TBK1, IKKE and DDX58 (By
CC       similarity). Interacts (via CAP-Gly domain) with microtubules.
CC       Interacts with HDAC6 and BCL3. Interacts with SQSTM1 and MAP3K7.
CC       Identified in a complex with TRAF6 and SQSTM1.
CC   -!- INTERACTION:
CC       Q9Z2F6:Bcl3; NbExp=1; IntAct=EBI-943859, EBI-943884;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
CC       Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane
CC       protein; Cytoplasmic side (By similarity). Note=Detected at the
CC       microtubule cytoskeleton during interphase. Detected at the
CC       midbody during telophase.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=2;
CC         IsoId=Q80TQ2-1; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q80TQ2-2; Sequence=VSP_011278;
CC       Name=3;
CC         IsoId=Q80TQ2-3; Sequence=VSP_011279, VSP_011280;
CC   -!- INDUCTION: Up-regulated by TNFRSF11A.
CC   -!- PTM: Phosphorylated on several serine residues by IKKA and/or IKKB
CC       in response to immune stimuli. Phosphorylation requires IKBKG.
CC       Phosphorylation abolishes TRAF2 deubiquitination, interferes with
CC       the activation of Jun kinases, and strongly reduces CD40-dependent
CC       gene activation by NF-kappa-B (By similarity).
CC   -!- DISRUPTION PHENOTYPE: No obvious phenotype, but mice are highly
CC       susceptible to carcinogens and are prone to chemically induced
CC       skin tumors. The number of natural killer T-cells is much reduced.
CC       Animals are highly susceptible to bacteria-induced pneumonia, due
CC       to an over active innate immune response. Animals spontaneously
CC       develop colonic inflammation, due to constitutive expression of
CC       several proinflammatory genes in the colon. Animals exhibit
CC       abnormal osteoclast differentiation, leading to osteoporosis.
CC   -!- SIMILARITY: Belongs to the peptidase C67 family.
CC   -!- SIMILARITY: Contains 3 CAP-Gly domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65671.1; Type=Erroneous initiation;
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DR   EMBL; AK122389; BAC65671.1; ALT_INIT; mRNA.
DR   EMBL; AK039054; BAC30222.1; -; mRNA.
DR   EMBL; AK042764; BAC31357.1; -; mRNA.
DR   EMBL; BC042438; AAH42438.1; -; mRNA.
DR   EMBL; BC049879; AAH49879.1; -; mRNA.
DR   IPI; IPI00277703; -.
DR   IPI; IPI00463126; -.
DR   IPI; IPI00875098; -.
DR   RefSeq; NP_001121641.1; NM_001128169.1.
DR   RefSeq; NP_001121642.1; NM_001128170.1.
DR   RefSeq; NP_001121643.1; NM_001128171.1.
DR   RefSeq; NP_775545.1; NM_173369.2.
DR   UniGene; Mm.24282; -.
DR   ProteinModelPortal; Q80TQ2; -.
DR   SMR; Q80TQ2; 125-206, 228-306, 453-546, 579-952.
DR   IntAct; Q80TQ2; 4.
DR   MINT; MINT-7561827; -.
DR   STRING; Q80TQ2; -.
DR   MEROPS; C67.001; -.
DR   PhosphoSite; Q80TQ2; -.
DR   PRIDE; Q80TQ2; -.
DR   Ensembl; ENSMUST00000043526; ENSMUSP00000039834; ENSMUSG00000036712.
DR   Ensembl; ENSMUST00000109622; ENSMUSP00000105251; ENSMUSG00000036712.
DR   Ensembl; ENSMUST00000109626; ENSMUSP00000105254; ENSMUSG00000036712.
DR   GeneID; 74256; -.
DR   KEGG; mmu:74256; -.
DR   UCSC; uc009mrt.1; mouse.
DR   UCSC; uc009mrw.1; mouse.
DR   CTD; 74256; -.
DR   MGI; MGI:1921506; Cyld.
DR   GeneTree; ENSGT00390000018123; -.
DR   HOVERGEN; HBG051281; -.
DR   OMA; MQVELPP; -.
DR   PhylomeDB; Q80TQ2; -.
DR   BRENDA; 3.1.2.15; 244.
DR   NextBio; 340262; -.
DR   ArrayExpress; Q80TQ2; -.
DR   Bgee; Q80TQ2; -.
DR   CleanEx; MM_CYLD; -.
DR   Genevestigator; Q80TQ2; -.
DR   GermOnline; ENSMUSG00000036712; Mus musculus.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005840; C:ribosome; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:EC.
DR   GO; GO:0004843; F:ubiquitin-specific protease activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0042347; P:negative regulation of NF-kappaB import into nucleus; ISS:UniProtKB.
DR   GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR023092; CAP-Gly_CS.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19.
DR   InterPro; IPR001593; Ribosomal_S3Ae.
DR   Gene3D; G3DSA:2.30.30.190; CAP-Gly_domain; 3.
DR   PANTHER; PTHR11830; Ribosomal_S3AE; 1.
DR   Pfam; PF01302; CAP_GLY; 3.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF74924; CAP-Gly_domain; 3.
DR   PROSITE; PS00845; CAP_GLY_1; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 2.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; FALSE_NEG.
DR   PROSITE; PS50235; UCH_2_3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasm; Cytoskeleton;
KW   Hydrolase; Membrane; Metal-binding; Microtubule; Phosphoprotein;
KW   Protease; Repeat; Thiol protease; Ubl conjugation pathway;
KW   Wnt signaling pathway; Zinc.
FT   CHAIN         1    952       Ubiquitin carboxyl-terminal hydrolase
FT                                CYLD.
FT                                /FTId=PRO_0000080699.
FT   DOMAIN      153    198       CAP-Gly 1.
FT   DOMAIN      253    286       CAP-Gly 2.
FT   DOMAIN      488    531       CAP-Gly 3.
FT   REGION      106    589       Interaction with TRIP (By similarity).
FT   REGION      390    465       Interaction with TRAF2 (By similarity).
FT   REGION      466    680       Interaction with IKBKG/NEMO (By
FT                                similarity).
FT   ACT_SITE    597    597       Nucleophile (By similarity).
FT   ACT_SITE    867    867       Proton acceptor (By similarity).
FT   METAL       784    784       Zinc 1 (By similarity).
FT   METAL       787    787       Zinc 1 (By similarity).
FT   METAL       795    795       Zinc 2 (By similarity).
FT   METAL       798    798       Zinc 2 (By similarity).
FT   METAL       813    813       Zinc 1 (By similarity).
FT   METAL       816    816       Zinc 1 (By similarity).
FT   METAL       821    821       Zinc 2 (By similarity).
FT   METAL       829    829       Zinc 2 (By similarity).
FT   MOD_RES     395    395       Phosphoserine (By similarity).
FT   MOD_RES     414    414       Phosphoserine.
FT   VAR_SEQ     304    304       P -> PALS (in isoform 1).
FT                                /FTId=VSP_011278.
FT   VAR_SEQ     305    318       DSVTQERRPPKLAF -> GTSKNILDQQLKGK (in
FT                                isoform 3).
FT                                /FTId=VSP_011279.
FT   VAR_SEQ     319    952       Missing (in isoform 3).
FT                                /FTId=VSP_011280.
FT   CONFLICT    403    403       M -> V (in Ref. 2; BAC30222).
SQ   SEQUENCE   952 AA;  106586 MW;  0AC0C7D4FF215A9C CRC64;
     MSSGLWSQEK VTSPYWEERI FYLLLQECSV TDKQTQKLLK VPKGSIGQYI QDRSVGHSRV
     PSTKGKKNQI GLKILEQPHA VLFVDEKDVV EINEKFTELL LAITNCEERL SLFRNRLRLS
     KGLQVDVGSP VKVQLRSGEE KFPGVVRFRG PLLAERTVSG IFFGVELLEE GRGQGFTDGV
     YQGKQLFQCD EDCGVFVALD KLELIEDDDN GLESDFAGPG DTMQVEPPPL EINSRVSLKV
     GESTESGTVI FCDVLPGKES LGYFVGVDMD NPIGNWDGRF DGVQLCSFAS VESTILLHIN
     DIIPDSVTQE RRPPKLAFMS RGVGDKGSSS HNKPKVTGST SDPGSRNRSE LFYTLNGSSV
     DSQQSKSKNP WYIDEVAEDP AKSLTEMSSD FGHSSPPPQP PSMNSLSSEN RFHSLPFSLT
     KMPNTNGSMA HSPLSLSVQS VMGELNSTPV QESPPLPISS GNAHGLEVGS LAEVKENPPF
     YGVIRWIGQP PGLSDVLAGL ELEDECAGCT DGTFRGTRYF TCALKKALFV KLKSCRPDSR
     FASLQPVSNQ IERCNSLAFG GYLSEVVEEN TPPKMEKEGL EIMIGKKKGI QGHYNSCYLD
     STLFCLFAFS SALDTVLLRP KEKNDIEYYS ETQELLRTEI VNPLRIYGYV CATKIMKLRK
     ILEKVEAASG FTSEEKDPEE FLNILFHDIL RVEPLLKIRS AGQKVQDCNF YQIFMEKNEK
     VGVPTIQQLL EWSFINSNLK FAEAPSCLII QMPRFGKDFK LFKKIFPSLE LNITDLLEDT
     PRQCRICGGL AMYECRECYD DPDISAGKIK QFCKTCSTQV HLHPRRLNHS YHPVSLPKDL
     PDWDWRHGCI PCQKMELFAV LCIETSHYVA FVKYGKDDSA WLFFDSMADR DGGQNGFNIP
     QVTPCPEVGE YLKMSLEDLH SLDSRRIQGC ARRLLCDAYM CMYQSPTMSL YK
//
ID   PKHM2_MOUSE             Reviewed;        1018 AA.
AC   Q80TQ5; A2ADE1; Q3U0Q7; Q6PD22;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=Pleckstrin homology domain-containing family M member 2;
DE            Short=PH domain-containing family M member 2;
GN   Name=Plekhm2; Synonyms=Kiaa0842;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=NOD; TISSUE=Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-1018 (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-558, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May play a role in the regulation of conventional
CC       kinesin activity. Required for maintenance of the Golgi apparatus
CC       organization. May play a role in membrane tubulation (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with KIF5B (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q80TQ5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80TQ5-2; Sequence=VSP_029163, VSP_029164;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q80TQ5-3; Sequence=VSP_029162, VSP_029163, VSP_029164;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 RUN domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65668.1; Type=Erroneous initiation;
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DR   EMBL; AK122386; BAC65668.1; ALT_INIT; mRNA.
DR   EMBL; AK156652; BAE33794.1; -; mRNA.
DR   EMBL; AL670446; CAM19908.1; -; Genomic_DNA.
DR   EMBL; BC058984; AAH58984.1; -; mRNA.
DR   IPI; IPI00874992; -.
DR   IPI; IPI00875604; -.
DR   IPI; IPI00929909; -.
DR   RefSeq; NP_001028322.1; NM_001033150.1.
DR   UniGene; Mm.33220; -.
DR   ProteinModelPortal; Q80TQ5; -.
DR   SMR; Q80TQ5; 7-161, 770-874.
DR   PhosphoSite; Q80TQ5; -.
DR   PRIDE; Q80TQ5; -.
DR   Ensembl; ENSMUST00000030751; ENSMUSP00000030751; ENSMUSG00000028917.
DR   Ensembl; ENSMUST00000084203; ENSMUSP00000081221; ENSMUSG00000028917.
DR   Ensembl; ENSMUST00000105783; ENSMUSP00000101409; ENSMUSG00000028917.
DR   GeneID; 69582; -.
DR   KEGG; mmu:69582; -.
DR   CTD; 69582; -.
DR   MGI; MGI:1916832; Plekhm2.
DR   GeneTree; ENSGT00390000015175; -.
DR   HOVERGEN; HBG059073; -.
DR   OrthoDB; EOG4VT5WF; -.
DR   ArrayExpress; Q80TQ5; -.
DR   Bgee; Q80TQ5; -.
DR   Genevestigator; Q80TQ5; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR004012; Run.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF02759; RUN; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00593; RUN; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50826; RUN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Phosphoprotein.
FT   CHAIN         1   1018       Pleckstrin homology domain-containing
FT                                family M member 2.
FT                                /FTId=PRO_0000309456.
FT   DOMAIN       36    158       RUN.
FT   DOMAIN      770    872       PH.
FT   REGION        1    289       Interaction with KIF5B (By similarity).
FT   COMPBIAS    296    299       Poly-Lys.
FT   COMPBIAS    302    307       Poly-Lys.
FT   COMPBIAS    485    488       Poly-Glu.
FT   COMPBIAS    592    595       Poly-Leu.
FT   MOD_RES     423    423       Phosphoserine (By similarity).
FT   MOD_RES     558    558       Phosphoserine.
FT   VAR_SEQ       1    165       Missing (in isoform 3).
FT                                /FTId=VSP_029162.
FT   VAR_SEQ     217    217       E -> EDYDFGDVFPAVPSVPSTDWE (in isoform 2
FT                                and isoform 3).
FT                                /FTId=VSP_029163.
FT   VAR_SEQ     527    532       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_029164.
FT   CONFLICT    490    490       G -> GG (in Ref. 3; CAM19908 and 4;
FT                                AAH58984).
FT   CONFLICT    500    500       V -> L (in Ref. 3; CAM19908 and 4;
FT                                AAH58984).
FT   CONFLICT    612    612       R -> L (in Ref. 4; AAH58984).
SQ   SEQUENCE   1018 AA;  112734 MW;  1024AD61CE90767D CRC64;
     MEPREVKDRI LENISLSVKK LQSYFAACED ETPAIRNHDK VLQRLCEHLD HALLYGLQDL
     SSGYWVLVVH FTRREAIRQI EVLQHVATNL GRSRAWLYLA LNENSLESYL RLFQENLGLL
     QKYYVRNALV CSHDHLTLFL TLVSGLEFIR FDLDLDAPYL DLAPYMPDYY KPQYLLDFED
     RLPSSVHGSD SLSLNSFNSV TSTNLEWDDS AIAPSSEDGD LTDTISGPRS TASDLTSSKT
     STKSPTQRHN PFNEEQAETA SSDTTPVHTT SQEKEEAQAP DQPDACTELE VIRVTKKKKI
     GKKKKTKLDE DASPLHPTSS QQKCGQQGEG DGLVGTPGLA RDPSDTVLAS PQEQGEGLSS
     TAGSSELSEL SQMGLLIPEM KDTSMECLGQ PLSKVIDKLH GQLDPSTWCS HADPPEQSFR
     AGSPGEAPEK PPFCDFSEGL PAPMDFYRFT VESPSTVAPG GGHHDPPGPS QPLHVPGSPA
     AALQEEEEGG RGEGQTSQPV EDRQGEEIQE PEPQEPDSQL PLVSQEPLVS QEPVPEPVSQ
     PEPGTHEALC KLKRDQPSPC LSSAEDSGVE EGQGSPSEMT HPSEFRVDNN HLLLLMIHVF
     RENEEQLFKM IRMSTGHMEG NLQLLYVLLT DCYVYLLRKG ATEKPYLVEE AVSYNELDYV
     SVGLDQQTVK LVCTNRRKQF LLDTADVALA ELFLASLKSA MIKGCREPPY PSILTDATME
     KLALAKFVAQ ESKCEASAVT VHFYGLVHWE DPMEEALGPV PCQCSPAEGT ITKEGMLHYK
     ASTSYLGKEH WKACFVVLSN GILYQYPDRT DVIPLLSVNM GGEQCGGCRR SNTTDRPHAF
     QVILADRPCL ELSADSEAEM ADWMQHLCQA VSKGVIPQGI APSPCIPCCL VITEDRLFTC
     HEDCQTSFFR SLGTARLADI TAISTELGKE YCVLEFSQDS PQLLQPWVIY LSCTSELDRF
     LTALSSGWKA IYQVDLPHKA IHEASIKQKF EDALSLIHSA WQRSDSLCRG RASRDPWC
//
ID   LPHN1_MOUSE             Reviewed;        1466 AA.
AC   Q80TR1; Q3UH90; Q7TNE5; Q80T49;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   08-FEB-2011, entry version 88.
DE   RecName: Full=Latrophilin-1;
DE   AltName: Full=Calcium-independent alpha-latrotoxin receptor 1;
DE            Short=CIRL-1;
DE   AltName: Full=Lectomedin-2;
DE   Flags: Precursor;
GN   Name=Lphn1; Synonyms=Kiaa0821, Lec2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 61-1466 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 814-978.
RX   MEDLINE=22584407; PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA   Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA   Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA   Bergmann J.E., Gaitanaris G.A.;
RT   "The G protein-coupled receptor repertoires of human and mouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1145-1466.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1369, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Calcium-independent receptor of high affinity for alpha-
CC       latrotoxin, an excitatory neurotoxin present in black widow spider
CC       venom which triggers massive exocytosis from neurons and
CC       neuroendocrine cells. Receptor propably implicated in the
CC       regulation of exocytosis (By similarity).
CC   -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular
CC       region (p120) non-covalently linked to a seven-transmembrane
CC       moiety (p85). Interacts with syntaxin and with proteins of the
CC       SHANK family via the PDZ domain (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80TR1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80TR1-2; Sequence=VSP_022137;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The extracellular domain coupled to the a single
CC       transmembrane region are sufficient for full responsiveness to
CC       alpha-latrotoxin (By similarity).
CC   -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular
CC       subunit and a seven-transmembrane subunit. This proteolytic
CC       processing takes place early in the biosynthetic pathway, either
CC       in the endoplasmic reticulum or in the early compartment of the
CC       Golgi apparatus (By similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       LN-TM7 subfamily.
CC   -!- SIMILARITY: Contains 1 GPS domain.
CC   -!- SIMILARITY: Contains 1 olfactomedin-like domain.
CC   -!- SIMILARITY: Contains 1 SUEL-type lectin domain.
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DR   EMBL; AK147519; BAE27967.1; -; mRNA.
DR   EMBL; AK122380; BAC65662.1; -; mRNA.
DR   EMBL; AC156028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY255594; AAO85106.1; -; mRNA.
DR   EMBL; BC055793; AAH55793.1; -; mRNA.
DR   IPI; IPI00623958; -.
DR   IPI; IPI00816879; -.
DR   RefSeq; NP_851382.2; NM_181039.2.
DR   UniGene; Mm.260733; -.
DR   PDB; 2JX9; NMR; -; A=29-131.
DR   PDB; 2JXA; NMR; -; A=29-131.
DR   PDBsum; 2JX9; -.
DR   PDBsum; 2JXA; -.
DR   ProteinModelPortal; Q80TR1; -.
DR   SMR; Q80TR1; 29-131, 472-530.
DR   STRING; Q80TR1; -.
DR   MEROPS; S63.013; -.
DR   PhosphoSite; Q80TR1; -.
DR   PRIDE; Q80TR1; -.
DR   Ensembl; ENSMUST00000045393; ENSMUSP00000048422; ENSMUSG00000013033.
DR   Ensembl; ENSMUST00000116450; ENSMUSP00000112151; ENSMUSG00000013033.
DR   GeneID; 330814; -.
DR   KEGG; mmu:330814; -.
DR   UCSC; uc009mlh.1; mouse.
DR   UCSC; uc009mli.1; mouse.
DR   CTD; 330814; -.
DR   MGI; MGI:1929461; Lphn1.
DR   eggNOG; roNOG12907; -.
DR   GeneTree; ENSGT00600000084303; -.
DR   HOGENOM; HBG443791; -.
DR   HOVERGEN; HBG052337; -.
DR   InParanoid; Q80TR1; -.
DR   OMA; EYASWED; -.
DR   NextBio; 399562; -.
DR   ArrayExpress; Q80TR1; -.
DR   Bgee; Q80TR1; -.
DR   CleanEx; MM_LPHN1; -.
DR   Genevestigator; Q80TR1; -.
DR   GermOnline; ENSMUSG00000013033; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005529; F:sugar binding; IEA:UniProtKB-KW.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:InterPro.
DR   InterPro; IPR022624; DUF3497.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR001879; GPCR_2_extracellular_dom.
DR   InterPro; IPR003924; GPCR_2_latrophilin.
DR   InterPro; IPR003334; GPCR_2_latrophilin_rcpt_C.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR   InterPro; IPR000203; GPS_dom.
DR   InterPro; IPR000922; Lectin_gal-bd_dom.
DR   InterPro; IPR003112; Olfac-like.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF12003; DUF3497; 1.
DR   Pfam; PF02140; Gal_Lectin; 1.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF02793; HRM; 1.
DR   Pfam; PF02354; Latrophilin; 1.
DR   Pfam; PF02191; OLF; 1.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   PRINTS; PR01444; LATROPHILIN.
DR   SMART; SM00303; GPS; 1.
DR   SMART; SM00008; HormR; 1.
DR   SMART; SM00284; OLF; 1.
DR   PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG.
DR   PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR   PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
DR   PROSITE; PS51132; OLF; 1.
DR   PROSITE; PS50228; SUEL_LECTIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Lectin; Membrane;
KW   Phosphoprotein; Receptor; Signal; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     28       Potential.
FT   CHAIN        29   1466       Latrophilin-1.
FT                                /FTId=PRO_0000070342.
FT   TOPO_DOM     29    852       Extracellular (Potential).
FT   TRANSMEM    853    873       Helical; Name=1; (Potential).
FT   TOPO_DOM    874    887       Cytoplasmic (Potential).
FT   TRANSMEM    888    908       Helical; Name=2; (Potential).
FT   TOPO_DOM    909    914       Extracellular (Potential).
FT   TRANSMEM    915    935       Helical; Name=3; (Potential).
FT   TOPO_DOM    936    958       Cytoplasmic (Potential).
FT   TRANSMEM    959    979       Helical; Name=4; (Potential).
FT   TOPO_DOM    980    996       Extracellular (Potential).
FT   TRANSMEM    997   1017       Helical; Name=5; (Potential).
FT   TOPO_DOM   1018   1044       Cytoplasmic (Potential).
FT   TRANSMEM   1045   1065       Helical; Name=6; (Potential).
FT   TOPO_DOM   1066   1069       Extracellular (Potential).
FT   TRANSMEM   1070   1090       Helical; Name=7; (Potential).
FT   TOPO_DOM   1091   1466       Cytoplasmic (Potential).
FT   DOMAIN       40    129       SUEL-type lectin.
FT   DOMAIN      134    393       Olfactomedin-like.
FT   DOMAIN      793    844       GPS.
FT   COMPBIAS    408    411       Poly-Thr.
FT   COMPBIAS   1402   1412       Poly-Pro.
FT   SITE        832    833       Cleavage (By similarity).
FT   MOD_RES    1369   1369       Phosphoserine.
FT   MOD_RES    1432   1432       Phosphotyrosine (By similarity).
FT   CARBOHYD     98     98       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    526    526       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    635    635       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    736    736       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    795    795       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    800    800       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    821    821       N-linked (GlcNAc...) (Potential).
FT   DISULFID    135    317       By similarity.
FT   VAR_SEQ       1    171       Missing (in isoform 2).
FT                                /FTId=VSP_022137.
FT   STRAND       36     41
FT   STRAND       45     49
FT   STRAND       54     63
FT   STRAND       68     71
FT   HELIX        75     78
FT   HELIX        87     96
FT   STRAND       99    105
FT   STRAND      121    131
SQ   SEQUENCE   1466 AA;  161686 MW;  937199B072336C9E CRC64;
     MARLAAALWS LCVTTVLVTS ATQGLSRAGL PFGLMRRELA CEGYPIELRC PGSDVIMVEN
     ANYGRTDDKI CDADPFQMEN VQCYLPDAFK IMSQRCNNRT QCVVVAGSDA FPDPCPGTYK
     YLEVQYDCVP YIFVCPGTLQ KVLEPTSTHE SEHQSGAWCK DPLQAGDRIY VMPWIPYRTD
     TLTEYASWED YVAARHTTTY RLPNRVDGTG FVVYDGAVFY NKERTRNIVK YDLRTRIKSG
     ETVINTANYH DTSPYRWGGK TDIDLAVDEN GLWVIYATEG NNGRLVVSQL NPYTLRFEGT
     WETGYDKRSA SNAFMVCGVL YVLRSVYVDD DSEAAGNRVD YAFNTNANRE EPVSLAFPNP
     YQFVSSVDYN PRDNQLYVWN NYFVVRYSLE FGPPDPSAGP ATSPPLSTTT TARPTPLTST
     ASPAATTPLR RAPLTTHPVG AINQLGPDLP PATAPAPSTR RPPAPNLHVS PELFCEPREV
     RRVQWPATQQ GMLVERPCPK GTRGIASFQC LPALGLWNPR GPDLSNCTSP WVNQVAQKIK
     SGENAANIAS ELARHTRGSI YAGDVSSSVK LMEQLLDILD AQLQALRPIE RESAGKNYNK
     MHKRERTCKD YIKAVVETVD NLLRPEALES WKDMNATEQV HTATMLLDVL EEGAFLLADN
     VREPARFLAA KQNVVLEVTV LNTEGQVQEL VFPQEYPSEN SIQLSANTIK QNSRNGVVKV
     VFILYNNLGL FLSTENATVK LAGEAGTGGP GGASLVVNSQ VIAASINKES SRVFLMDPVI
     FTVAHLEAKN HFNANCSFWN YSERSMLGYW STQGCRLVES NKTHTTCACS HLTNFAVLMA
     HREIYQGRIN ELLLSVITWV GIVISLVCLA ICISTFCFLR GLQTDRNTIH KNLCINLFLA
     ELLFLVGIDK TQYEVACPIF AGLLHYFFLA AFSWLCLEGV HLYLLLVEVF ESEYSRTKYY
     YLGGYCFPAL VVGIAAAIDY RSYGTEKACW LRVDNYFIWS FIGPVSFVIV VNLVFLMVTL
     HKMIRSSSVL KPDSSRLDNI KSWALGAIAL LFLLGLTWAF GLLFINKESV VMAYLFTTFN
     AFQGVFIFVF HCALQKKVHK EYSKCLRHSY CCIRSPPGGT HGSLKTSAMR SNTRYYTGTQ
     SRIRRMWNDT VRKQTESSFM AGDINSTPTL NRGTMGNHLL TNPVLQPRGG TSPYNTLIAE
     SVGFNPSSPP VFNSPGSYRE PKHPLGGREA CGMDTLPLNG NFNNSYSLRS GDFPPGDGGP
     EPPRGRNLAD AAAFEKMIIS ELVHNNLRGA SGGAKGPPPE PPVPPVPGVS EDEAGGPGSA
     DRAEIELLYK ALEEPLLLPR AQSVLYQSDL DESESCTAED GATSRPLSSP PGRDSLYASG
     ANLRDSPSYP DSSPEGPNEA LPPPPPAPPG PPEIYYTSRP PALVARNPLQ GYYQVRRPSH
     EGYLAAPSLE GPGPDGDGQM QLVTSL
//
ID   LPHN3_MOUSE             Reviewed;        1537 AA.
AC   Q80TS3; Q3UHI7; Q3UM79; Q504Z9; Q5HZJ6; Q80T56;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 3.
DT   08-FEB-2011, entry version 84.
DE   RecName: Full=Latrophilin-3;
DE   AltName: Full=Lectomedin-3;
DE   Flags: Precursor;
GN   Name=Lphn3; Synonyms=Kiaa0768, Lec3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 672-1537 (ISOFORM 5).
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 6).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 481-1537 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 803-981.
RX   MEDLINE=22584407; PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA   Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA   Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA   Bergmann J.E., Gaitanaris G.A.;
RT   "The G protein-coupled receptor repertoires of human and mouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1535, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular
CC       region (p120) non-covalently linked to a seven-transmembrane
CC       moiety (p85) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q80TS3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80TS3-2; Sequence=VSP_010121, VSP_010122, VSP_010123;
CC       Name=3;
CC         IsoId=Q80TS3-3; Sequence=VSP_022142;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q80TS3-4; Sequence=VSP_022138;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q80TS3-5; Sequence=VSP_010121;
CC         Note=No experimental confirmation available;
CC       Name=6;
CC         IsoId=Q80TS3-6; Sequence=VSP_022139, VSP_022140, VSP_022141;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular
CC       subunit and a seven-transmembrane subunit (By similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       LN-TM7 subfamily.
CC   -!- SIMILARITY: Contains 1 GPS domain.
CC   -!- SIMILARITY: Contains 1 olfactomedin-like domain.
CC   -!- SIMILARITY: Contains 1 SUEL-type lectin domain.
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DR   EMBL; AK145069; BAE26219.1; -; mRNA.
DR   EMBL; AK147374; BAE27870.1; -; mRNA.
DR   EMBL; BC058992; AAH58992.1; -; mRNA.
DR   EMBL; BC088989; AAH88989.1; -; mRNA.
DR   EMBL; BC094668; AAH94668.1; -; mRNA.
DR   EMBL; AK122367; BAC65649.1; -; mRNA.
DR   EMBL; AY255584; AAO85096.1; -; mRNA.
DR   IPI; IPI00411157; -.
DR   IPI; IPI00411158; -.
DR   IPI; IPI00619988; -.
DR   IPI; IPI00816961; -.
DR   IPI; IPI00816972; -.
DR   IPI; IPI00816975; -.
DR   RefSeq; NP_941991.1; NM_198702.2.
DR   UniGene; Mm.273631; -.
DR   UniGene; Mm.461016; -.
DR   ProteinModelPortal; Q80TS3; -.
DR   SMR; Q80TS3; 93-197.
DR   STRING; Q80TS3; -.
DR   MEROPS; S63.014; -.
DR   PhosphoSite; Q80TS3; -.
DR   PRIDE; Q80TS3; -.
DR   Ensembl; ENSMUST00000036068; ENSMUSP00000045342; ENSMUSG00000037605.
DR   Ensembl; ENSMUST00000072521; ENSMUSP00000072336; ENSMUSG00000037605.
DR   Ensembl; ENSMUST00000113420; ENSMUSP00000109047; ENSMUSG00000037605.
DR   Ensembl; ENSMUST00000113424; ENSMUSP00000109051; ENSMUSG00000037605.
DR   GeneID; 319387; -.
DR   KEGG; mmu:319387; -.
DR   UCSC; uc008xwm.1; mouse.
DR   UCSC; uc008xwn.1; mouse.
DR   UCSC; uc008xwp.1; mouse.
DR   CTD; 319387; -.
DR   MGI; MGI:2441950; Lphn3.
DR   eggNOG; roNOG12907; -.
DR   GeneTree; ENSGT00600000084303; -.
DR   HOVERGEN; HBG052337; -.
DR   OMA; NIKLEVA; -.
DR   ArrayExpress; Q80TS3; -.
DR   Bgee; Q80TS3; -.
DR   CleanEx; MM_LPHN3; -.
DR   Genevestigator; Q80TS3; -.
DR   GermOnline; ENSMUSG00000037605; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005529; F:sugar binding; IEA:UniProtKB-KW.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:InterPro.
DR   InterPro; IPR022624; DUF3497.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR001879; GPCR_2_extracellular_dom.
DR   InterPro; IPR003924; GPCR_2_latrophilin.
DR   InterPro; IPR015630; GPCR_2_latrophilin3.
DR   InterPro; IPR003334; GPCR_2_latrophilin_rcpt_C.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR   InterPro; IPR000203; GPS_dom.
DR   InterPro; IPR000922; Lectin_gal-bd_dom.
DR   InterPro; IPR003112; Olfac-like.
DR   PANTHER; PTHR12011:SF60; Latrophilin3; 1.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF12003; DUF3497; 1.
DR   Pfam; PF02140; Gal_Lectin; 1.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF02793; HRM; 1.
DR   Pfam; PF02354; Latrophilin; 2.
DR   Pfam; PF02191; OLF; 1.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   PRINTS; PR01444; LATROPHILIN.
DR   SMART; SM00303; GPS; 1.
DR   SMART; SM00284; OLF; 1.
DR   PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG.
DR   PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR   PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
DR   PROSITE; PS51132; OLF; 1.
DR   PROSITE; PS50228; SUEL_LECTIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Lectin; Membrane;
KW   Phosphoprotein; Receptor; Signal; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     19       Potential.
FT   CHAIN        20   1537       Latrophilin-3.
FT                                /FTId=PRO_0000070344.
FT   TOPO_DOM     20    949       Extracellular (Potential).
FT   TRANSMEM    950    970       Helical; Name=1; (Potential).
FT   TOPO_DOM    971    978       Cytoplasmic (Potential).
FT   TRANSMEM    979    999       Helical; Name=2; (Potential).
FT   TOPO_DOM   1000   1007       Extracellular (Potential).
FT   TRANSMEM   1008   1028       Helical; Name=3; (Potential).
FT   TOPO_DOM   1029   1050       Cytoplasmic (Potential).
FT   TRANSMEM   1051   1071       Helical; Name=4; (Potential).
FT   TOPO_DOM   1072   1088       Extracellular (Potential).
FT   TRANSMEM   1089   1109       Helical; Name=5; (Potential).
FT   TOPO_DOM   1110   1142       Cytoplasmic (Potential).
FT   TRANSMEM   1143   1163       Helical; Name=6; (Potential).
FT   TOPO_DOM   1164   1169       Extracellular (Potential).
FT   TRANSMEM   1170   1190       Helical; Name=7; (Potential).
FT   TOPO_DOM   1191   1537       Cytoplasmic (Potential).
FT   DOMAIN      103    192       SUEL-type lectin.
FT   DOMAIN      202    461       Olfactomedin-like.
FT   DOMAIN      883    934       GPS.
FT   COMPBIAS   1470   1473       Poly-Ala.
FT   MOD_RES     678    678       Phosphothreonine (By similarity).
FT   MOD_RES    1535   1535       Phosphothreonine.
FT   CARBOHYD    161    161       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    532    532       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    617    617       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    827    827       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    840    840       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    885    885       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    911    911       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1000   1000       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1166   1166       N-linked (GlcNAc...) (Potential).
FT   DISULFID    203    385       By similarity.
FT   VAR_SEQ       1    239       Missing (in isoform 4).
FT                                /FTId=VSP_022138.
FT   VAR_SEQ     195    200       KVEQKV -> I (in isoform 6).
FT                                /FTId=VSP_022139.
FT   VAR_SEQ     650    650       H -> Q (in isoform 6).
FT                                /FTId=VSP_022140.
FT   VAR_SEQ     651   1537       Missing (in isoform 6).
FT                                /FTId=VSP_022141.
FT   VAR_SEQ    1132   1140       Missing (in isoform 2 and isoform 5).
FT                                /FTId=VSP_010121.
FT   VAR_SEQ    1272   1351       EGLLNNARDTSVMDTLPLNGNHGNSYSIAGGEYLSNCVQII
FT                                DRGYNHNETALEKKILKELTSNYIPSYLNNHERSSEQNR
FT                                -> GAMANHLISNALLRPHGTNNPYNTLLGEPAVCNNPSIS
FT                                MYNTQEPYRETSMGVKLNIAYQIGASEQCQGYKCHGYSTTE
FT                                W (in isoform 2).
FT                                /FTId=VSP_010122.
FT   VAR_SEQ    1272   1272       E -> EPYRETK (in isoform 3).
FT                                /FTId=VSP_022142.
FT   VAR_SEQ    1352   1537       Missing (in isoform 2).
FT                                /FTId=VSP_010123.
FT   CONFLICT    381    381       A -> S (in Ref. 2; AAH94668).
FT   CONFLICT   1252   1252       K -> R (in Ref. 1; BAE27870).
FT   CONFLICT   1375   1375       A -> T (in Ref. 1; BAE26219).
FT   CONFLICT   1495   1495       V -> M (in Ref. 1; BAE26219).
SQ   SEQUENCE   1537 AA;  171080 MW;  F55EAB142C987A69 CRC64;
     MWPPQLLILT MLLAPVVHGG KHNERHPALA APLRHAERSP GGALPPRHLL QQPAAERSTA
     HRGQGPRGAA RGVRGPGAPG AQIAAQAFSR APIPMAVVRR ELSCESYPIE LRCPGTDVIM
     IESANYGRTD DKICDSDPAQ MENIRCYLPD AYKIMSQRCN NRTQCAVVAG PDVFPDPCPG
     TYKYLEVQYE CVPYKVEQKV FLCPGLLKGV YQSEHLFESD HQSGAWCKDP LQASDKIYYM
     PWTPYRTDTL TEYSSKDDFI AGRPTTTYKL PHRVDGTGFV VYDGALFFNK ERTRNIVKFD
     LRTRIKSGEA IIANANYHDT SPYRWGGKSD IDLAVDENGL WVIYATEQNN GKIVISQLNP
     YTLRIEGTWD TAYDKRSASN AFMICGILYV VKSVYEDDDN EATGNKIDYI YNTDQSKDSL
     VDVPFPNSYQ YIAAVDYNPR DNLLYVWNNY HVVKYSLDFG PLDSRSGPVH HGQVSYISPP
     IHLDSELERP PVRGISTTGS LGMGSTTTST TLRTTTWNIG RSTTASLPGR RNRSTSTPSP
     AVEVLDDVTT HLPSAASQIP AMEESCEAVE AREIMWFKTR QGQVAKQPCP AGTIGVSTYL
     CLAPDGIWDP QGPDLSNCSS PWVNHITQKL KSGETAANIA RELAEQTRNH LNAGDITYSV
     RAMDQLVGLL DVQLRNLTPG GKDSAARSLN KLQKRERSCR AYVQAMVETV NNLLQPQALN
     AWRDLTTSDQ LRAATMLLDT VEESAFVLAD NLLKTDIVRE NTDNIQLEVA RLSTEGNLED
     LKFPENMGHG STIQLSANTL KQNGRNGEIR VAFVLYNNLG PYLSTENASM KLGTEAMSTN
     HSVIVNSPVI TAAINKEFSN KVYLADPVVF TVKHIKQSEE NFNPNCSFWS YSKRTMTGYW
     STQGCRLLTT NKTHTTCSCN HLTNFAVLMA HVEVKHSDAV HDLLLDVITW VGILLSLVCL
     LICIFTFCFF RGLQSDRNTI HKNLCISLFV AELLFLIGIN RTDQPIACAV FAALLHFFFL
     AAFTWMFLEG VQLYIMLVEV FESEHSRRKY FYLVGYGMPA LIVAVSAAVD YRSYGTDKVC
     WLRLDTYFIW SFIGPATLII MLNVIFLGIA LYKMFHHTAI LKPESGCLDN INYEDNRPFI
     KSWVIGAIAL LCLLGLTWAF GLMYINESTV IMAYLFTIFN SLQGMFIFIF HCVLQKKVRK
     EYGKCLRTHC CSGKSTESSI GSGKTSGSRT PGRYSTGSQS RIRRMWNDTV RKQSESSFIT
     GDINSSASLN REGLLNNARD TSVMDTLPLN GNHGNSYSIA GGEYLSNCVQ IIDRGYNHNE
     TALEKKILKE LTSNYIPSYL NNHERSSEQN RNMMNKLVNN LGSGSEDDAI VLDDAASFNH
     EESLGLELIH EESDAPLLPP RVYSTDNHQP HHYSRRRFPQ DHSESFFPLL TDEHTEDLQS
     PHRDSLYTSM PALAGVPAAD SVTTSTQTEA AAAKGGDAED VYYKSMPNLG SRNHVHPLHA
     YYQLGRGSSD GFIVPPNKDG ASPEGTSKGP AHLVTSL
//
ID   DEND_MOUSE              Reviewed;         710 AA.
AC   Q80TS7; Q3TPT2; Q3TY46;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 3.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=Dendrin;
GN   Name=Ddn; Synonyms=Gm748, Kiaa0749;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-710.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 49-710.
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=17251388; DOI=10.1681/ASN.2006060675;
RA   Patrakka J., Xiao Z., Nukui M., Takemoto M., He L., Oddsson A.,
RA   Perisic L., Kaukinen A., Szigyarto C.A.-K., Uhlen M., Jalanko H.,
RA   Betsholtz C., Tryggvason K.;
RT   "Expression and subcellular distribution of novel glomerulus-
RT   associated proteins Dendrin, Ehd3, Sh2d4a, Plekhh2, and
RT   2310066E14Rik.";
RL   J. Am. Soc. Nephrol. 18:689-697(2007).
RN   [6]
RP   FUNCTION, INTERACTION WITH CD2AP; NPHS1 AND NPHS2, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=17537921; DOI=10.1073/pnas.0700917104;
RA   Asanuma K., Campbell K.N., Kim K., Faul C., Mundel P.;
RT   "Nuclear relocation of the nephrin and CD2AP-binding protein dendrin
RT   promotes apoptosis of podocytes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10134-10139(2007).
RN   [7]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=18356187; DOI=10.1093/ndt/gfn100;
RA   Duner F., Patrakka J., Xiao Z., Larsson J., Vlamis-Gardikas A.,
RA   Pettersson E., Tryggvason K., Hultenby K., Wernerson A.;
RT   "Dendrin expression in glomerulogenesis and in human minimal change
RT   nephrotic syndrome.";
RL   Nephrol. Dial. Transplant. 23:2504-2511(2008).
CC   -!- FUNCTION: Promotes apoptosis of kidney glomerular podocytes.
CC       Podocytes are highly specialized cells essential to the
CC       ultrafiltration of blood, resulting in the extraction of urine and
CC       the retention of protein.
CC   -!- SUBUNIT: Forms a ternary complex with MAGI2 and SH3KBP1; recruits
CC       DDN to the cytoplasm (By similarity). Interacts with MAGI1 (By
CC       similarity). Interacts with ACTN1 and may interact with WWC1 (By
CC       similarity). Interacts with the podocyte slit diaphragm proteins
CC       CD2AP, NPHS1 and NPHS2; the interaction with CD2AP and NPHS1 is
CC       direct.
CC   -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine membrane;
CC       Peripheral membrane protein (By similarity). Cytoplasm.
CC       Endoplasmic reticulum membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity). Perikaryon (By similarity).
CC       Nucleus. Note=Enriched at the cytoplasmic insertion of the slit
CC       diaphragm into the foot process of podocytes and associated with
CC       polyribosomes in dendrites (By similarity).
CC   -!- TISSUE SPECIFICITY: Two forms of 81 kDa and 89 kDa are expressed
CC       in brain. The 81 kDa form is the only one found in kidney
CC       podocytes.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the developing podocytes during
CC       glomerulogenesis.
CC   -!- MISCELLANEOUS: The 81 and 89 kDa forms are detected by an antibody
CC       raised against a C-terminal peptide arguing for alternative N-
CC       terminal sequences.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI57996.1; Type=Erroneous initiation;
CC       Sequence=AAI57997.1; Type=Erroneous initiation;
CC       Sequence=BAE34717.1; Type=Erroneous initiation;
CC       Sequence=EDL04165.1; Type=Erroneous initiation;
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DR   EMBL; AK158894; BAE34717.1; ALT_INIT; mRNA.
DR   EMBL; AK164154; BAE37653.1; -; mRNA.
DR   EMBL; CH466550; EDL04165.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AK122363; BAC65645.1; -; mRNA.
DR   EMBL; BC157995; AAI57996.1; ALT_INIT; mRNA.
DR   EMBL; BC157996; AAI57997.1; ALT_INIT; mRNA.
DR   IPI; IPI00675094; -.
DR   RefSeq; NP_001013763.1; NM_001013741.1.
DR   UniGene; Mm.390810; -.
DR   STRING; Q80TS7; -.
DR   PhosphoSite; Q80TS7; -.
DR   PRIDE; Q80TS7; -.
DR   Ensembl; ENSMUST00000075444; ENSMUSP00000074895; ENSMUSG00000059213.
DR   GeneID; 13199; -.
DR   KEGG; mmu:13199; -.
DR   CTD; 13199; -.
DR   MGI; MGI:108101; Ddn.
DR   eggNOG; roNOG04050; -.
DR   GeneTree; ENSGT00390000016495; -.
DR   HOGENOM; HBG505458; -.
DR   HOVERGEN; HBG107808; -.
DR   InParanoid; Q80TS7; -.
DR   OrthoDB; EOG4GF3F0; -.
DR   ArrayExpress; Q80TS7; -.
DR   Bgee; Q80TS7; -.
DR   CleanEx; MM_DDN; -.
DR   Genevestigator; Q80TS7; -.
DR   GermOnline; ENSMUSG00000059213; Mus musculus.
DR   GO; GO:0032591; C:dendritic spine membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW   Endoplasmic reticulum; Membrane; Nucleus; Phosphoprotein.
FT   CHAIN         1    710       Dendrin.
FT                                /FTId=PRO_0000079862.
FT   REGION      113    131       Nuclear localization (By similarity).
FT   REGION      186    236       Interaction with MAGI2 (By similarity).
FT   REGION      341    435       Interaction with ACTN1 (By similarity).
FT   REGION      407    708       Interaction with CD2AP and NPHS1 (By
FT                                similarity).
FT   COILED      103    134       Potential.
FT   MOD_RES     567    567       Phosphoserine (By similarity).
FT   CONFLICT    679    679       S -> I (in Ref. 1; BAE37653).
SQ   SEQUENCE   710 AA;  76407 MW;  8EDF4A92AE6A9BB7 CRC64;
     MLDGPLFSEG PDSPRELQDE ESGSCLWVQK SKLLVIEVKT ISCHYSRRAP SRQSMDIQAS
     YWARGPQSRT CRLRPGSPEP PPRRPWASRV LQEATNWRAG PPAEVRAREQ EKRKAASQER
     EAKETERKRR KAGGARRSPL GQPRPEPRNA LRAAQPTGFP VFSRPERFGQ VGRAPRPSVL
     PQGDPGVAWA GPWGGRRPGP PSYEAHLLLR GSAGTAPRRR WDRPPPYVAP PSYEGPHRTL
     GTKRGPELSR APTSSAPVPA TTRTEGGRTK KRLDPRIYRD VLGAWGLRQG RGLLGGAPGC
     TAARARPESC KGAIEKSSGL VAAGLNSAGD SHSQGKTTGG PGTDAALSRS AISSPPRPVP
     RSRQHLRGSR KGKEGSEQIW LPTCWLASPK KPPVRHSQTL PRPWAPGGTG WKESLGQREG
     AEHETLEVWK VTRRAHTLPR ISRGPAGREG IFVIDATCVV IKSQYVPTPR TQQGQLVPSG
     ESCSVSDSLS QPKPCHEEEG EGAAANPSVC QKRLLSSRVL NQPSEGRECE AEVGQQGDSS
     LEERSSSGLG FPVGEVNPRD APTQPGSQEH PTLGPAAPVC AGSLKGSEAA GVPRRAGGGW
     ARTPGPYAGA LREAVSRIRR HTAPDSDSDE AEDLSVHSGS SDGSDTDAPG ASWRNERTLP
     ALGNTRPREG GKTAGLSDSI REIVDVISQT EEGFIREDTR KTPQGNRERE
//
ID   BAIP3_MOUSE             Reviewed;        1134 AA.
AC   Q80TT2; Q6RUT4;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 2.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=BAI1-associated protein 3;
DE            Short=BAP3;
GN   Name=Baiap3; Synonyms=Gm937, Kiaa0734;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RA   Brathwaite M.E., Waeltz P., Qian Y., Dudekula D., Schlessinger D.,
RA   Nagaraja R.;
RT   "Genomic sequence analysis in the mouse T-complex region.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Interacts with BAI1 (By similarity).
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -!- SIMILARITY: Contains 1 MHD1 (MUNC13 homology domain 1) domain.
CC   -!- SIMILARITY: Contains 1 MHD2 (MUNC13 homology domain 2) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65640.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK122358; BAC65640.1; ALT_INIT; Transcribed_RNA.
DR   EMBL; AY491413; AAS21653.1; -; Genomic_DNA.
DR   IPI; IPI00944020; -.
DR   UniGene; Mm.328859; -.
DR   ProteinModelPortal; Q80TT2; -.
DR   SMR; Q80TT2; 155-334, 974-1072.
DR   STRING; Q80TT2; -.
DR   PhosphoSite; Q80TT2; -.
DR   PRIDE; Q80TT2; -.
DR   Ensembl; ENSMUST00000056357; ENSMUSP00000049805; ENSMUSG00000047507.
DR   MGI; MGI:2685783; Baiap3.
DR   eggNOG; roNOG07754; -.
DR   HOVERGEN; HBG050658; -.
DR   InParanoid; Q80TT2; -.
DR   OrthoDB; EOG49ZXNG; -.
DR   ArrayExpress; Q80TT2; -.
DR   Bgee; Q80TT2; -.
DR   CleanEx; MM_BAIAP3; -.
DR   Genevestigator; Q80TT2; -.
DR   GermOnline; ENSMUSG00000047507; Mus musculus.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR014770; Munc13_1.
DR   InterPro; IPR014772; Munc13_dom-2.
DR   InterPro; IPR019558; Munc13_subgr_dom-2.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF10540; Membr_traf_MHD; 1.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS51258; MHD1; 1.
DR   PROSITE; PS51259; MHD2; 1.
PE   2: Evidence at transcript level;
KW   Repeat.
FT   CHAIN         1   1134       BAI1-associated protein 3.
FT                                /FTId=PRO_0000064820.
FT   DOMAIN      145    280       C2 1.
FT   DOMAIN      610    731       MHD1.
FT   DOMAIN      835    943       MHD2.
FT   DOMAIN      959   1066       C2 2.
FT   CONFLICT    178    179       Missing (in Ref. 2; AAS21653).
FT   CONFLICT    182    182       Y -> D (in Ref. 2; AAS21653).
FT   CONFLICT    200    200       Q -> R (in Ref. 2; AAS21653).
FT   CONFLICT    584    584       R -> G (in Ref. 2; AAS21653).
SQ   SEQUENCE   1134 AA;  127191 MW;  62EC9A52BF441EC9 CRC64;
     MSTLLDIKSS VLRQVQVCPS FRRKTEQEPE VTNSQEPPTG AWKPGDGVEF FAHMRLILKK
     GDGRQGLPCP EVLLRSGSPA PAEPVDPNRG LRTLTQEEVE MLYEEALYTV LHRAGTMGPD
     QVDDEEVLLS YLQQVFGTSS EEHMEAIMRV KKAKAPTYAL KVSVMRAKNL LAKDPNGFSD
     PYCMLGILPA SSAPQESSGQ KEQRFGFRKG SKRSSPLPAK CIQVTEVKNS TLNPVWKEHF
     LFEIDDVNTD QLHLDIWDHD DDVSLAEACR KLNEVIGLKG MTRYFKQIVK SARANGTAGP
     TEDHTDDFLG CLNIPIREVP VAGADRWFKL EPRSSASRVQ GDCHLVLKLI TTQRDTVMNQ
     RGRSGFLSYL LLLSRVLRFE HRVEEPNSSS WRGELSGPGT TVLCLHGAQS NLSPLQLAVL
     HWQVSSRHHQ TRTLDYGYLL GLLEDVQAHW EEAASLPQEQ EESLADSFSA FSEFGLRLLR
     QLRDYFPATN STAVYRLELL LKCLEKLQLF QPAFEICPFE TELSMDIAAA LKRGNREWYD
     QLLNTKSPRE QPGPQRLAGL VELADIIYED LQLCYGVYAS LFHRQVAEEA WVLTEELSPK
     MNLEVASGLF ELYLTLADTQ RFWSCIPGRE SRSLALAGIH TPFLPAVKLW LQVLRDQAKW
     RLQGAVDVDT LEPVDAASKH SSSAATASLC LSHIQELWVR LAWPDPSQAQ GLGTQLSQDM
     CEASLFYTEL LRKKVDTQPG AAGEAVSEQL CVVLNNVELV RRASGQALRG LAWSEGASGL
     EGVLPRPLLS CIQALDEDLH REAHTVTAHL TSKMVADIRK YIQHISLSPD SIQNDEAVAP
     LLKYLDEKLA LLNDALVKEN LNRVLEALWE LLLQAILQAL SANRDVSADF YGRFHFTLEA
     LVSFFHAEGQ GLPLENLRDG SYKRLQEELR LHKCSTRECI EQFYLDKLKQ RSLEQNRFGR
     LTVRCHYEAA EQRLAVEVLH AADLLPLDAN GLSDPFVIVE LGPPHLFPLV RSQRTQVKAR
     TLHPVYDELF HFSVPAEACR RRGACVLFTV MDHDWLSTND FAGEAALGLG GISGIARPHV
     GGGMRPGQPI TLHLRRPRAQ VRSALRMLEG RTSREAQEFV KKLKELEKCM EADL
//
ID   Q80TT4_MOUSE            Unreviewed;       626 AA.
AC   Q80TT4;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 46.
DE   SubName: Full=MKIAA0719 protein;
DE   Flags: Fragment;
GN   Name=Tomm70a; Synonyms=D16Wsu109e, mKIAA0719;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
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DR   EMBL; AK122356; BAC65638.1; -; mRNA.
DR   IPI; IPI00751137; -.
DR   UniGene; Mm.213292; -.
DR   HSSP; P31948; 1ELW.
DR   ProteinModelPortal; Q80TT4; -.
DR   STRING; Q80TT4; -.
DR   PRIDE; Q80TT4; -.
DR   Ensembl; ENSMUST00000023433; ENSMUSP00000023433; ENSMUSG00000022752.
DR   MGI; MGI:106295; Tomm70a.
DR   HOGENOM; HBG714569; -.
DR   HOVERGEN; HBG062335; -.
DR   InParanoid; Q80TT4; -.
DR   ArrayExpress; Q80TT4; -.
DR   Bgee; Q80TT4; -.
DR   Genevestigator; Q80TT4; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR001440; TPR-1.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 4.
DR   Pfam; PF00515; TPR_1; 2.
DR   SMART; SM00028; TPR; 10.
DR   PROSITE; PS50005; TPR; 7.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   2: Evidence at transcript level;
KW   Repeat; TPR repeat.
FT   NON_TER       1      1
SQ   SEQUENCE   626 AA;  69531 MW;  2EE46C7BEBDD25B9 CRC64;
     PWRPRPARRR RRTVVMAASK PIEAAMAAAA APGSGNGVGG GGGTAGPGSG AGTLPRWHVA
     LAIGAPLLLG AGAMYLWSRR RRRREAGGRG DASGLKRNSE RKTPEGRASP ALGSGHHDGS
     GDSLEMSSLD RAQAAKNKGN KYFKAGKYEQ AIQCYTEAIS LCPTEKNVDL STFYQNRAAA
     FEQLQKWKEV AQDCTKAVEL NPKYVKALFR RAKAHEKLDN KKECLEDVTA VCILEGFQNE
     QSMLLADKVL KLLGKENAKE KYKNREPLMP SPQFIKSYFS SFTDDIISQP MLKGEKSDED
     KDKEGEALEV KENSGYLKAK QYMEEENYDK IISECSKEID AQGKYMAEAL LLRATFYLLI
     GSANAAKPDL DKVISLKEAN VKLRANALIK RGTMCMQQQQ PMLSTQDFNM AAEIDPMNSD
     VYHHRGQLKI LLDLVEEAVA DFDACIRLRP KFALAQAQKC FALYRQAYTA NNSSQVQAAM
     KGFEEIIKKF PRCAEGYALY AQALTDQQQF GKADEMYDKC IDLEPDNATT YVHKGLLQLQ
     WKQDLDKGLE LISKAIEIDN KCDFAYETMG TIEVQRGNME KAIDMFNKAI NLAKSEMEMA
     HLYSLCDAAH AQTEVAKKYG LKPPTL
//
ID   CUL9_MOUSE              Reviewed;        1865 AA.
AC   Q80TT8; Q8BKL9; Q8CGC0; Q8R363;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Cullin-9;
DE            Short=CUL-9;
DE   AltName: Full=p53-associated parkin-like cytoplasmic protein;
GN   Name=Cul9; Synonyms=Kiaa0708, Parc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC   TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 102-1865 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
CC   -!- FUNCTION: Cytoplasmic anchor protein in p53-associated protein
CC       complex. Regulates the subcellular localization of p53 and
CC       subsequent function. Seems to be part of an atypical cullin-RING-
CC       based E3 ubiquitin-protein ligase complex. In vitro, complexes of
CC       CUL9/PARC with either CUL7 or TP53 contain E3 ubiquitin-protein
CC       ligase activity (By similarity).
CC   -!- SUBUNIT: Forms a complex with p53/TP53 in the cytoplasm of
CC       unstressed cells. Interacts with UBCH7 and UBCH8. Interacts with
CC       CUL7 and RBX1. The CUL7-CUL9 heterodimer seems to interact
CC       specifically with TP53 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q80TT8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80TT8-2; Sequence=VSP_009576;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q80TT8-3; Sequence=VSP_009577, VSP_009578;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q80TT8-4; Sequence=VSP_009579, VSP_009580;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The IBR domain is required for interaction with UBCH7 and
CC       UBCH8.
CC   -!- SIMILARITY: Belongs to the cullin family.
CC   -!- SIMILARITY: Contains 1 DOC domain.
CC   -!- SIMILARITY: Contains 1 IBR-type zinc finger.
CC   -!- SIMILARITY: Contains 2 RING-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AK051474; Type=Frameshift; Positions=1664;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK051474; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC026469; AAH26469.1; -; mRNA.
DR   EMBL; BC041674; AAH41674.1; -; mRNA.
DR   EMBL; AK122351; BAC65633.1; -; Transcribed_RNA.
DR   IPI; IPI00378253; -.
DR   IPI; IPI00407573; -.
DR   IPI; IPI00407575; -.
DR   IPI; IPI00624086; -.
DR   UniGene; Mm.329076; -.
DR   ProteinModelPortal; Q80TT8; -.
DR   SMR; Q80TT8; 483-635, 1206-1291, 1472-1543, 1567-1623.
DR   STRING; Q80TT8; -.
DR   PhosphoSite; Q80TT8; -.
DR   PRIDE; Q80TT8; -.
DR   Ensembl; ENSMUST00000066026; ENSMUSP00000067736; ENSMUSG00000040327.
DR   Ensembl; ENSMUST00000113441; ENSMUSP00000109068; ENSMUSG00000040327.
DR   UCSC; uc008ctb.1; mouse.
DR   UCSC; uc008ctf.1; mouse.
DR   MGI; MGI:1925559; Cul9.
DR   eggNOG; roNOG15166; -.
DR   GeneTree; ENSGT00600000084159; -.
DR   HOGENOM; HBG714264; -.
DR   InParanoid; Q80TT8; -.
DR   OrthoDB; EOG4P2Q1C; -.
DR   ArrayExpress; Q80TT8; -.
DR   Bgee; Q80TT8; -.
DR   CleanEx; MM_PARC; -.
DR   Genevestigator; Q80TT8; -.
DR   GermOnline; ENSMUSG00000040327; Mus musculus.
DR   GO; GO:0005680; C:anaphase-promoting complex; IEA:InterPro.
DR   GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR004939; Ananphase-promot_cplx_su10_DOC.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR016157; Cullin_CS.
DR   InterPro; IPR016158; Cullin_homology.
DR   InterPro; IPR001373; Cullin_N.
DR   InterPro; IPR019559; Cullin_neddylation_domain.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR002867; Znf_C6HC.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 3.
DR   Pfam; PF03256; APC10; 1.
DR   Pfam; PF00888; Cullin; 1.
DR   Pfam; PF01485; IBR; 2.
DR   SMART; SM00884; Cullin_Nedd8; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF75632; Cullin_homology; 1.
DR   SUPFAM; SSF49785; Gal_bind_like; 1.
DR   PROSITE; PS01256; CULLIN_1; 1.
DR   PROSITE; PS50069; CULLIN_2; 1.
DR   PROSITE; PS51284; DOC; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Coiled coil; Cytoplasm;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Repeat;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1   1865       Cullin-9.
FT                                /FTId=PRO_0000119816.
FT   DOMAIN      480    659       DOC.
FT   NP_BIND     700    707       ATP (Potential).
FT   ZN_FING    1409   1459       RING-type 1; atypical.
FT   ZN_FING    1479   1542       IBR-type.
FT   ZN_FING    1575   1604       RING-type 2.
FT   COILED     1794   1835       Potential.
FT   COMPBIAS   1426   1435       Cys-rich.
FT   COMPBIAS   1800   1862       Glu-rich.
FT   MOD_RES     284    284       Phosphoserine (By similarity).
FT   VAR_SEQ       1    908       Missing (in isoform 2).
FT                                /FTId=VSP_009576.
FT   VAR_SEQ     134    144       ALKMLAIANSS -> VSTLGRAGQSD (in isoform
FT                                3).
FT                                /FTId=VSP_009577.
FT   VAR_SEQ     145   1865       Missing (in isoform 3).
FT                                /FTId=VSP_009578.
FT   VAR_SEQ     944   1009       LLSLGSSWLEGAVLEQIGPCFPNRLPQLMLQSLHTSEELQH
FT                                RFHLFQLQQLDRQLLEQGDQEEWRP -> RLEENSLQTQDQ
FT                                PFPSWSCHRAAGRSPHCAICTTPESTYRRSSAMPWSASPAS
FT                                TATVRSWGQEAGA (in isoform 4).
FT                                /FTId=VSP_009579.
FT   VAR_SEQ    1010   1865       Missing (in isoform 4).
FT                                /FTId=VSP_009580.
FT   CONFLICT   1102   1102       L -> F (in Ref. 1; AK051474).
FT   CONFLICT   1104   1119       Missing (in Ref. 3; BAC65633).
FT   CONFLICT   1111   1119       LNTVQMWLL -> TVQMWLLLN (in Ref. 1;
FT                                AK051474).
FT   CONFLICT   1183   1183       F -> V (in Ref. 1; AK051474).
FT   CONFLICT   1592   1592       T -> N (in Ref. 1; AK051474).
SQ   SEQUENCE   1865 AA;  209160 MW;  9956A32BE5BC5803 CRC64;
     MARALRGPGP RSSLDQHVAA VLATVQISSL DTNLQLSGLC ALSQAVEEVT ERDHPLVRPD
     RPLREKLVKT LVDLLTNQVG EKMVVVMALR LLYLLMTKHE WRPLFAREGG IYAVLICMQE
     YKTSVLVQQA GLAALKMLAI ANSSDVPTFI PSRDSIQPLF DTQMTREIFA SIDSATRPGS
     ESLLLSVPAA VVLMLNTEGC SSAVRNGLLL LNLLLCNHHT LGDQIITQEL RDTLFRHSGI
     APGTEPMPTT RTILTMLLSR YSEPRGSPER AVLETPSTQG QDGSPESLIR SLVGDLSAEL
     FLDLERVLCH EGSPPAAVRP LLRRLQQETQ PFLLLLRTLD APGPNRTLLL TILRVMTRLL
     DHPETMVLPW HEVLEPCLNC LNGPSSDSEV VQEVTCFLHR LALMQKDYAV VLCCLGGKEA
     LSKVLDKHST QLLLASELRH LVAECEKYSQ LCSNLTSSIL AGCIQMVLGQ IEDHRRTYKP
     ITIPFFDVFL RHLCQGSSVE VKEDRCWEKV EVSSNPHRAS KLTDRNPKTY WESNGSTGSH
     SITLHMHRGV LIRQLTLLVA SEDSSYMPAR VVVFGGDNVG CISTELNTVN VMPSASRVTL
     LENLTRFWPI IQIRIKRCQQ GGIDTRVRGV EVLGPKPTFW PLFREQLCRR TCLFYTIRAQ
     AWSRDIAEDR QRLLQLYPRL NRVLRHEQNF ADRFLPDDEA AQALGKTCWE ALVSPLVQNI
     TSPDAGGVSS LGWLLDQYLE HRESTRSRQG PAASFASQVR RLCHLLVHVE APPGPSPEPS
     SQPLSKNSKG QDGSPTPAPT PVCPSTSLRN LTQCWLSVVQ GQVSRFLAAA WRASDFVPRY
     CSLYQRLQSA GSELFGPRAA FTLALRSGFS GALLQQSFLT AAHISEQFAR HIDQQIHGGL
     LGGAAGVGML GRLQRHLEPI MVLSGLELAT TFEHFYQHYM ADRLLSLGSS WLEGAVLEQI
     GPCFPNRLPQ LMLQSLHTSE ELQHRFHLFQ LQQLDRQLLE QGDQEEWRPE KVEEDDEGQE
     TGRELFTDPG PAISVLVLSP RCWPVSPLCY LHHPRKHLQA ELCDALERFS SFYSHSQNCP
     VLDIGPHRRL QWTWLGRAEL QLGDQTLHVS LNTVQMWLLF NQSEEVSVET LLRNSDLSPE
     LLHQALLPLT SDNGPLTLEE TQDYPQGGVL RLREPRSQTH EEFLWLIPPQ TYLSVEKDEG
     RTLEQKRNLL SCLLVRILKA HREKGLHIDQ LVCLVLEAWQ KGPDPPGRLG NAAAVGVACS
     STDVLSCILH LLGQGYVERR DDRPQVLMYA TPEPMGPCRG QADVPFCGNK NTETSRPSPE
     AVVALASLQL PAGRTMSPQE VEGLMEQTVR QVQETLNLEP DVAQHLLAHS HWGTEQLLQS
     YSDDPEPLLL AAGLRVPQAQ VVPTRPDQCP VCVTPLGPHD DSPSLCCLHC CCKSCWNEYL
     TTRIEQNFVL NCTCPIADCP AQPTGAFIRN IVSSPEVISK YEKALLRGYV ESCSNLTWCT
     NPQGCDRILC RQGLGSGTTC SKCGWASCFS CSFPEAHYPA SCGHMSQWVD DGGYYDGMSV
     EAQSKHLAKL ISKRCPSCQA PIEKNEGCLH MTCARCNHGF CWRCLKSWKP SHKDYYNCSA
     MVSKAARQEK RFQDYNERCT FHHQAREFAV NLRNQASAIQ EVPPPKSFTF LQDACRALEQ
     ARKVLAYACV YSFYSQDTEY MDVVEQQTEN LELHTNALQI LLEETLLRCR DLASSLRFLR
     ADCLSTGTEL LRRIQERLLA ILQHSTQDFR VGLQSPSVET REVKGSNVPS DQPQGSSGLE
     VEDEEEEEEE EEEEEEEEEE DVPEWQHEFD EELDNDSFSY DEESENLDRE TFFFGDEDED
     DESYD
//
ID   Q80TU6_MOUSE            Unreviewed;      1266 AA.
AC   Q80TU6;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   08-FEB-2011, entry version 51.
DE   SubName: Full=MKIAA0670 protein;
DE   Flags: Fragment;
GN   Name=Acin1; Synonyms=mKIAA0670;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
CC   -!- SIMILARITY: Contains 1 SAP domain.
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DR   EMBL; AK122342; BAC65624.1; -; mRNA.
DR   IPI; IPI00911143; -.
DR   RefSeq; NP_001078942.2; NM_001085473.2.
DR   UniGene; Mm.297078; -.
DR   ProteinModelPortal; Q80TU6; -.
DR   STRING; Q80TU6; -.
DR   Ensembl; ENSMUST00000147714; ENSMUSP00000119080; ENSMUSG00000022185.
DR   GeneID; 56215; -.
DR   KEGG; mmu:56215; -.
DR   CTD; 56215; -.
DR   MGI; MGI:1891824; Acin1.
DR   GeneTree; ENSGT00570000079212; -.
DR   HOVERGEN; HBG050449; -.
DR   InParanoid; Q80TU6; -.
DR   ArrayExpress; Q80TU6; -.
DR   Bgee; Q80TU6; -.
DR   Genevestigator; Q80TU6; -.
DR   GO; GO:0005730; C:nucleolus; IDA:MGI.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR003034; SAP_DNA-bd.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF02037; SAP; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00513; SAP; 1.
DR   PROSITE; PS50800; SAP; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   1266 AA;  142853 MW;  4346CE06E2397DD0 CRC64;
     ELEEVTLDGK PLQALRVTDL KAALEQRGLA KSGQKSALVK RLKGALMLEN LQKHSTPHAA
     FQPNSQIGEE MSQNSFIKQY LEKQQELLRQ RLEREAREAA ELEEASAESE DEMTHPEGVA
     SLLPPDFQSS LNRPELELST HSPRKSSSFS EEKGESDDEK PRKGERRSSR VRQAKSKLPE
     YSQAAEEEED QETPSRNLRV RADRNLKIEE EEEEEEEEED DDDEEEEEVD EAQKSREAEA
     PTLKQFEDEE GEERTRAKPE KVVDEKPLNI RSQEKGELEK GGRVTRSQEE ARRSHLARQQ
     QEKETQIVSL PQEENEVKSS QGLEEKSQSP SPPPLPEDLE KAPVVLQPEQ IVSEEETPPP
     LLTKEASSPP THIQLQEEME PVEGPAPPVL IQLSPPNTDA GAREPLASPH PAQLVRSLSP
     LSGTTDTKAE SPAGRVSDES VLPLAQKSSL PECSAQKGVE SEREKSAPLP LTVEELAPAK
     GITEEPMKKQ SLEQKEDRRA SHALFPEYSG KQSADSSSSR SSSPSSSSSP SRSPSPDSAA
     SRPQSSPGSK QRDGAQARVH ANPHERPKMG SRSTSESRSR SRSRSRSASS SSRKSLSPGV
     SRDSNTSYTE TKDPSCGQEA AAPSGPQLQV LEPKEKAPTF SASVRGRHLS HPEPEQQHVI
     QRLQPEQGSP KKCEAEEAEP PAATQPQTSE TQISHLPESE RTHHTVEEKE EVTMDTSENR
     PENEVPEPPL PVADQVSNDE RPEGGAEEEE KKESSMPKSF KRKISVVSAT KGVQAGNSDT
     EGGQPGRKRR WGASTAATQK KPSISITTES LKEAVVDLHA DDSRISEDET ERNGDDGTHD
     KGLKICRTVT QVVPAEGQEN GQREEEEEKE PEAEPPAPPQ VSVEVALPPP VEHEVKKVTL
     GDTLTRRSIS QQKSGVSITI DDPVRTAQVP SPPRGKISNI VHISNLVRPF TLGQLKELLG
     RTGTLVEEAF WIDKIKSHCF VTYSTVEEAV ATRTALHGVK WPQSNPKFLC ADYAEQDELD
     YHRGLLVDRP SETKAEEQGA PRPLHPPPPP PVQPPPHPRA EQREQERAVR EQWAEREREM
     ERRERTRSER EWDRDKVREG PRSRSRSRDR RRKERAKSKE KKSEKKEKAQ EEPPAKLLDD
     LFRKTKAAPC IYWLPLTESQ IVQKEAEQAE RAKEREKRRK EREEEEQKER EKEAERERNR
     QLEREKRREH SRERERDRER ERDRGDRERE RERDRDRGRE RDRRDTKRHS RSRSRSTPVR
     DRGGRR
//
ID   CLAP1_MOUSE             Reviewed;        1535 AA.
AC   Q80TV8; Q505G6; Q6DI75; Q6PG14; Q8BNS4; Q99JH5; Q99JI2; Q9CVU1;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=CLIP-associating protein 1;
DE   AltName: Full=Cytoplasmic linker-associated protein 1;
GN   Name=Clasp1; Synonyms=Kiaa0622;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-306 (ISOFORMS 1/2), NUCLEOTIDE
RP   SEQUENCE [MRNA] OF 1251-1535 (ISOFORMS 1/2), INTERACTION WITH CLIP2
RP   AND RSN, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=21185938; PubMed=11290329; DOI=10.1016/S0092-8674(01)00288-4;
RA   Akhmanova A., Hoogenraad C.C., Drabek K., Stepanova T., Dortland B.,
RA   Verkerk T., Vermeulen W., Burgering B.M., de Zeeuw C.I., Grosveld F.,
RA   Galjart N.;
RT   "Clasps are CLIP-115 and -170 associating proteins involved in the
RT   regional regulation of microtubule dynamics in motile fibroblasts.";
RL   Cell 104:923-935(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-393 (ISOFORMS 1/2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1187-1535 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 735-1535 (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 985-1535 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 997-1535 (ISOFORM 2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1193 AND SER-1220, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545; SER-598 AND
RP   SER-600, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Microtubule plus-end tracking protein that promotes the
CC       stabilization of dynamic microtubules. Involved in the nucleation
CC       of noncentrosomal microtubules originating from the trans-Golgi
CC       network (TGN). Required for the polarization of the cytoplasmic
CC       microtubule arrays in migrating cells towards the leading edge of
CC       the cell. May act at the cell cortex to enhance the frequency of
CC       rescue of depolymerizing microtubules by attaching their plus-ends
CC       to cortical platforms composed of ERC1 and PHLDB2. This cortical
CC       microtubule stabilizing activity is regulated at least in part by
CC       phosphatidylinositol 3-kinase signaling. Also performs a similar
CC       stabilizing function at the kinetochore which is essential for the
CC       bipolar alignment of chromosomes on the mitotic spindle (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with ERC1, MAPRE1, MAPRE3, microtubules, and
CC       PHLDB2. The interaction with ERC1 may be mediated by PHLDB2.
CC       Interacts with GCC2; recruits CLASP1 to Golgi membranes (By
CC       similarity). Interacts with CLIP2 and RSN.
CC   -!- INTERACTION:
CC       Q922J3:Clip1; NbExp=1; IntAct=EBI-908322, EBI-776187;
CC       O55156:Clip2 (xeno); NbExp=3; IntAct=EBI-908322, EBI-349416;
CC       Q9Z0H8:Clip2; NbExp=1; IntAct=EBI-908322, EBI-775282;
CC       Q9JK25:Rsn (xeno); NbExp=2; IntAct=EBI-908322, EBI-908338;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Cytoplasm, cytoskeleton, centrosome (By similarity). Chromosome,
CC       centromere, kinetochore (By similarity). Cytoplasm, cytoskeleton,
CC       spindle (By similarity). Golgi apparatus, trans-Golgi network (By
CC       similarity). Note=Localizes to microtubule plus ends (By
CC       similarity). Localizes to centrosomes, kinetochores and the
CC       mitotic spindle from prometaphase (By similarity). Subsequently
CC       localizes to the spindle midzone from anaphase and to the midbody
CC       from telophase (By similarity). In migrating cells localizes to
CC       the plus ends of microtubules within the cell body and to the
CC       entire microtubule lattice within the lamella (By similarity).
CC       Localizes to the cell cortex and this requires ERC1 and PHLDB2 (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80TV8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80TV8-2; Sequence=VSP_022390, VSP_022391, VSP_022392;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and heart and at
CC       lower levels in kidney, lung, skeletal muscle and testis.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the CLASP family.
CC   -!- SIMILARITY: Contains 7 HEAT repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB24639.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAC38020.1; Type=Miscellaneous discrepancy; Note=Intron retention;
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DR   EMBL; AC109294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC131804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC136636; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AJ276962; CAC35162.1; -; mRNA.
DR   EMBL; AJ288061; CAC35163.1; -; mRNA.
DR   EMBL; AK006534; BAB24639.2; ALT_INIT; mRNA.
DR   EMBL; AK080782; BAC38020.1; ALT_SEQ; mRNA.
DR   EMBL; AK122330; BAC65612.1; -; mRNA.
DR   EMBL; BC057312; AAH57312.1; -; mRNA.
DR   EMBL; BC075708; AAH75708.1; -; mRNA.
DR   EMBL; BC094554; AAH94554.1; -; mRNA.
DR   IPI; IPI00669522; -.
DR   IPI; IPI00672213; -.
DR   RefSeq; NP_083985.2; NM_029709.2.
DR   RefSeq; NP_808216.2; NM_177548.2.
DR   UniGene; Mm.138740; -.
DR   ProteinModelPortal; Q80TV8; -.
DR   IntAct; Q80TV8; 9.
DR   STRING; Q80TV8; -.
DR   PhosphoSite; Q80TV8; -.
DR   PRIDE; Q80TV8; -.
DR   Ensembl; ENSMUST00000049404; ENSMUSP00000042266; ENSMUSG00000064302.
DR   Ensembl; ENSMUST00000070989; ENSMUSP00000067858; ENSMUSG00000064302.
DR   GeneID; 76707; -.
DR   KEGG; mmu:76707; -.
DR   UCSC; uc007cif.1; mouse.
DR   CTD; 76707; -.
DR   MGI; MGI:1923957; Clasp1.
DR   GeneTree; ENSGT00390000001762; -.
DR   HOVERGEN; HBG079692; -.
DR   InParanoid; Q80TV8; -.
DR   OrthoDB; EOG42Z4PC; -.
DR   NextBio; 345659; -.
DR   ArrayExpress; Q80TV8; -.
DR   Bgee; Q80TV8; -.
DR   CleanEx; MM_CLASP1; -.
DR   Genevestigator; Q80TV8; -.
DR   GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IDA:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0034453; P:microtubule anchoring; ISS:UniProtKB.
DR   GO; GO:0007020; P:microtubule nucleation; ISS:UniProtKB.
DR   GO; GO:0031023; P:microtubule organizing center organization; ISS:UniProtKB.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:MGI.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000357; HEAT.
DR   InterPro; IPR021133; HEAT_type_2.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 4.
DR   Pfam; PF02985; HEAT; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 2.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Cell division; Centromere;
KW   Chromosome; Coiled coil; Cytoplasm; Cytoskeleton; Golgi apparatus;
KW   Kinetochore; Microtubule; Mitosis; Phosphoprotein; Repeat.
FT   CHAIN         1   1535       CLIP-associating protein 1.
FT                                /FTId=PRO_0000272274.
FT   REPEAT       87    124       HEAT 1.
FT   REPEAT      163    200       HEAT 2.
FT   REPEAT      405    440       HEAT 3.
FT   REPEAT      441    477       HEAT 4.
FT   REPEAT      971   1008       HEAT 5.
FT   REPEAT     1339   1376       HEAT 6.
FT   REPEAT     1457   1494       HEAT 7.
FT   REGION      662    782       Interaction with microtubules, MAPRE1 and
FT                                MAPRE3 (By similarity).
FT   REGION     1251   1535       Interaction with CLIP2 and RSN.
FT   REGION     1251   1535       Interaction with PHLDB2 (By similarity).
FT   REGION     1253   1535       Localization to kinetochores (By
FT                                similarity).
FT   COILED     1296   1327       Potential.
FT   COMPBIAS    530    762       Ser-rich.
FT   MOD_RES     545    545       Phosphoserine.
FT   MOD_RES     559    559       Phosphoserine (By similarity).
FT   MOD_RES     568    568       Phosphoserine (By similarity).
FT   MOD_RES     594    594       Phosphoserine (By similarity).
FT   MOD_RES     598    598       Phosphoserine.
FT   MOD_RES     600    600       Phosphoserine.
FT   MOD_RES     609    609       Phosphoserine (By similarity).
FT   MOD_RES     636    636       Phosphoserine (By similarity).
FT   MOD_RES     646    646       Phosphoserine (By similarity).
FT   MOD_RES     647    647       Phosphoserine (By similarity).
FT   MOD_RES     649    649       Phosphoserine (By similarity).
FT   MOD_RES     651    651       Phosphothreonine (By similarity).
FT   MOD_RES     656    656       Phosphothreonine (By similarity).
FT   MOD_RES     688    688       Phosphoserine (By similarity).
FT   MOD_RES     695    695       Phosphoserine (By similarity).
FT   MOD_RES     708    708       Phosphothreonine (By similarity).
FT   MOD_RES     711    711       Phosphoserine (By similarity).
FT   MOD_RES     794    794       Phosphoserine (By similarity).
FT   MOD_RES    1088   1088       Phosphoserine (By similarity).
FT   MOD_RES    1096   1096       Phosphothreonine (By similarity).
FT   MOD_RES    1193   1193       Phosphoserine.
FT   MOD_RES    1220   1220       Phosphoserine.
FT   VAR_SEQ     770    770       L -> LASRRHSRSTSALSTAESVGQS (in isoform
FT                                2).
FT                                /FTId=VSP_022390.
FT   VAR_SEQ     805    805       L -> LLLGDARSK (in isoform 2).
FT                                /FTId=VSP_022391.
FT   VAR_SEQ    1120   1158       Missing (in isoform 2).
FT                                /FTId=VSP_022392.
FT   CONFLICT   1231   1231       I -> K (in Ref. 3; BAB24639).
FT   CONFLICT   1417   1417       P -> S (in Ref. 5; AAH75708).
SQ   SEQUENCE   1535 AA;  169227 MW;  5EE40CCE493C64D2 CRC64;
     MEPRMESCLA QVLQKDVGKR LQVGQELIDY FSDRQKSADL EHDQTLLDKL VDGLATSWVN
     SSNYKVVLLG MDILSALVTR LQDRFKAQIG TVLPSLIDRL GDAKDSVREQ DQTLLLKIMD
     QAANPQYVWD RMLGGFKHKN FRTREGICLC LIATLNASGA QTLTLSKIVP HICNLLGDPN
     SQVRDAAINS LVEIYRHVGE RVRADLSKKG LPQSRLNVIF TKFDEVQKSG NMIQSANEKN
     FDDEDSVDGN RPSSASSSSS KAPSSSRRNV NLGTTRRLMS SSLGSKSSAA KEGAGAVDEE
     DFIKAFDDVP VVQIYSSRDL EESINKIREI LSDDKHDWEQ RVNALKKIRS LLLAGAAEYD
     NFFQHLRLLD GAFKLSAKDL RSQVVREACI TLGHLSSVLG NKFDHGAEAI MPTIFNLIPN
     SAKIMATSGV VAVRLIIRHT HIPRLIPVIT SNCTSKSVAV RRRCFEFLDL LLQEWQTHSL
     ERHISVLAET IKKGIHDADS EARIEARKCY WGFHSHFSRE AEHLYHTLES SYQKALQSHL
     KNSDSIVSLP QSDRSSSSSQ ESLNRPLSAK RSPTGSTASR GSTVSTKSVS TTGSLQRSRS
     DIDVNAAASA KSKVSSSSGS PAFSSAAALP PGSYASLGRI RTRRQSSGST TNVASTPDSR
     GRSRAKVVSQ SQRSRSANPA GAGSRSSSPG KLLGSGLAGG SSRGPPVTPS SEKRSKIPRS
     QGCSRETSPN RIGLARSSRI PRPSMSQGCS RDTSRESSRD TSPARGFTPL DRFGLGQSGR
     IPGSVNAMRV LSTSTDLEAA VADALKKPVR RRYEPYGMYS DDDANSDASS VCSERSYGSR
     NGGIPHYLRQ TEDVAEVLNH CASSNWSERK EGLLGLQNLL KSQRTLSRVE LKRLCEIFTR
     MFADPHSKRV FSMFLETLVD FIIIHKDDLQ DWLFVLLTQL LKKMGADLLG SVQAKVQKAL
     DVTRDSFPFD QQFNILMRFI VDQTQTPNLK VKVAILKYIE SLARQMDPTD FVNSSETRLA
     VSRIITWTTE PKSSDVRKAA QIVLISLFEL NTPEFTMLLG ALPKTFQDGA TKLLHNHLKN
     SSNTGVGSPS NTIGRTPSRH PSSRTSPLTS PTNCSHGGLS PSRLWGWSAD GLSKPPPPFS
     QPNSIPTAPS HKTLRRSYSP SMLDYDTENL NSEEIYSSLR GVTEAIEKFS FRSQEDLNEP
     IKRDGKKDCD IVSRDGGAAS PATEGRGGSE IEGGRMALDN KTSLLNTQPP RAFPGPRARE
     YNPYPYSDTI NTYDKTALKE AVFDDDMEQL RDVPIDHSDL VADLLKELSN HNERVEERKG
     ALLELLKITR EDSLGVWEEH FKTILLLLLE TLGDKDHSIR ALALRVLREI LRNQPARFKN
     YAELTIMKTL EAHKDSHKEV VRAAEEAAST LASSIHPEQC IKVLCPIIQT ADYPINLAAI
     KMQTKVVERI TKESLLQLLV DIIPGLLQGY DNTESSVRKA SVFCLVAIYS VIGEDLKPHL
     AQLTGSKMKL LNLYIKRAQT TNSNSSSSSD VSTHS
//
ID   FNBP1_MOUSE             Reviewed;         616 AA.
AC   Q80TY0; A2AQ40; A2AQ46; Q3TA45; Q3TCW9; Q3U081; Q3UPI7; Q8C727;
AC   Q99L37;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Formin-binding protein 1;
DE   AltName: Full=Formin-binding protein 17;
GN   Name=Fnbp1; Synonyms=Fbp17, Kiaa0554;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 169-616 (ISOFORM 5).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Dendritic cell, Embryo, Kidney, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=15252009; DOI=10.1074/jbc.M404899200;
RA   Kamioka Y., Fukuhara S., Sawa H., Nagashima K., Masuda M., Matsuda M.,
RA   Mochizuki N.;
RT   "A novel dynamin-associating molecule, formin-binding protein 17,
RT   induces tubular membrane invaginations and participates in
RT   endocytosis.";
RL   J. Biol. Chem. 279:40091-40099(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296 AND SER-299, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496 AND TYR-499, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-294 AND SER-496, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Required to coordinate membrane tubulation with
CC       reorganization of the actin cytoskeleton during endocytosis. Binds
CC       to lipids such as phosphatidylinositol 4,5-bisphosphate and
CC       phosphatidylserine and promotes membrane invagination and the
CC       formation of tubules. Also enhances actin polymerization via the
CC       recruitment of WASL/N-WASP, which in turn activates the Arp2/3
CC       complex. Actin polymerization may promote the fission of membrane
CC       tubules to form endocytic vesicles. May act as a link between RND2
CC       signaling and regulation of the actin cytoskeleton. May be
CC       required for the lysosomal retention of FASLG/FASL (By
CC       similarity).
CC   -!- SUBUNIT: Self-associates and can polymerize to form filamentous
CC       structures. Interacts specifically with GTP-bound RND2 and CDC42.
CC       Interacts with AKAP9, ARHGAP17, DAAM1, DIAPH1, DIAPH2, DNM1, DNM2,
CC       DNM3, FASLG/FASL, microtubules, PDE6G, SNX2 and WASL/N-WASP. May
CC       interact with TNKS (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity). Cytoplasm, cell cortex (By
CC       similarity). Lysosome (By similarity). Cytoplasmic vesicle (By
CC       similarity). Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity). Note=Enriched in cortical
CC       regions coincident with F-actin (By similarity). Also localizes to
CC       endocytic vesicles and lysosomes (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q80TY0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80TY0-2; Sequence=VSP_021698;
CC       Name=3;
CC         IsoId=Q80TY0-3; Sequence=VSP_021698, VSP_021703;
CC       Name=4;
CC         IsoId=Q80TY0-4; Sequence=VSP_021697, VSP_021699, VSP_021702;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q80TY0-5; Sequence=VSP_021700, VSP_021701;
CC   -!- TISSUE SPECIFICITY: Expressed in brain and testis.
CC   -!- SIMILARITY: Belongs to the FNBP1 family.
CC   -!- SIMILARITY: Contains 1 FCH domain.
CC   -!- SIMILARITY: Contains 1 REM (Hr1) repeat.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65590.1; Type=Erroneous initiation;
CC       Sequence=BAE33974.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK122308; BAC65590.1; ALT_INIT; mRNA.
DR   EMBL; AK052652; BAC35082.1; -; mRNA.
DR   EMBL; AK143512; BAE25408.1; -; mRNA.
DR   EMBL; AK157135; BAE33974.1; ALT_INIT; mRNA.
DR   EMBL; AK170497; BAE41836.1; -; mRNA.
DR   EMBL; AK172100; BAE42825.1; -; mRNA.
DR   EMBL; AL844546; CAM18436.1; -; Genomic_DNA.
DR   EMBL; AL844546; CAM18442.1; -; Genomic_DNA.
DR   EMBL; BC003867; AAH03867.1; -; mRNA.
DR   IPI; IPI00116278; -.
DR   IPI; IPI00626520; -.
DR   IPI; IPI00719992; -.
DR   IPI; IPI00755941; -.
DR   IPI; IPI00808090; -.
DR   RefSeq; NP_001033789.1; NM_001038700.2.
DR   RefSeq; NP_001171119.1; NM_001177648.1.
DR   RefSeq; NP_001171120.1; NM_001177649.1.
DR   RefSeq; NP_001171121.1; NM_001177650.1.
DR   RefSeq; NP_062279.1; NM_019406.3.
DR   UniGene; Mm.440993; -.
DR   UniGene; Mm.52297; -.
DR   HSSP; Q15642; 2CT4.
DR   ProteinModelPortal; Q80TY0; -.
DR   SMR; Q80TY0; 1-288, 554-607.
DR   STRING; Q80TY0; -.
DR   PhosphoSite; Q80TY0; -.
DR   PRIDE; Q80TY0; -.
DR   Ensembl; ENSMUST00000113552; ENSMUSP00000109181; ENSMUSG00000075415.
DR   Ensembl; ENSMUST00000113560; ENSMUSP00000109190; ENSMUSG00000075415.
DR   Ensembl; ENSMUST00000113562; ENSMUSP00000109192; ENSMUSG00000075415.
DR   Ensembl; ENSMUST00000113564; ENSMUSP00000109194; ENSMUSG00000075415.
DR   GeneID; 14269; -.
DR   KEGG; mmu:14269; -.
DR   UCSC; uc008jdh.1; mouse.
DR   UCSC; uc008jdi.1; mouse.
DR   UCSC; uc008jdj.1; mouse.
DR   UCSC; uc008jdk.1; mouse.
DR   UCSC; uc008jdm.1; mouse.
DR   CTD; 14269; -.
DR   MGI; MGI:109606; Fnbp1.
DR   GeneTree; ENSGT00510000046403; -.
DR   HOVERGEN; HBG002489; -.
DR   OrthoDB; EOG40S0FF; -.
DR   NextBio; 285633; -.
DR   ArrayExpress; Q80TY0; -.
DR   Bgee; Q80TY0; -.
DR   CleanEx; MM_FNBP1; -.
DR   Genevestigator; Q80TY0; -.
DR   GermOnline; ENSMUSG00000075415; Mus musculus.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   InterPro; IPR001060; FCH.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50133; FCH; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell membrane; Coiled coil;
KW   Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Endocytosis;
KW   Lipid-binding; Lysosome; Membrane; Phosphoprotein; SH3 domain.
FT   CHAIN         1    616       Formin-binding protein 1.
FT                                /FTId=PRO_0000261431.
FT   DOMAIN        1     65       FCH.
FT   REPEAT      415    490       REM.
FT   DOMAIN      549    610       SH3.
FT   REGION        1    334       Interaction with microtubules (By
FT                                similarity).
FT   REGION        1    284       Self-association, lipid-binding and
FT                                induction of membrane tubulation (By
FT                                similarity).
FT   REGION        1     79       Required for self-association and
FT                                induction of membrane tubulation (By
FT                                similarity).
FT   REGION      251    616       Required for self-association and
FT                                induction of membrane tubulation (By
FT                                similarity).
FT   REGION      399    551       Interaction with RND2 (By similarity).
FT   REGION      494    616       Interaction with PDE6G (By similarity).
FT   REGION      513    616       Required for interaction with TNKS (By
FT                                similarity).
FT   REGION      534    616       Interaction with DNM1 and DNM3 (By
FT                                similarity).
FT   REGION      549    616       Interaction with ARHGAP17, DAAM1, DIAPH1
FT                                and DIAPH2 (By similarity).
FT   REGION      552    609       Interaction with FASLG (By similarity).
FT   REGION      552    608       Interaction with DNM2 and WASL (By
FT                                similarity).
FT   COILED      132    177       Potential.
FT   COMPBIAS    336    365       Pro-rich.
FT   MOD_RES      27     27       N6-acetyllysine (By similarity).
FT   MOD_RES      66     66       N6-acetyllysine (By similarity).
FT   MOD_RES     110    110       N6-acetyllysine (By similarity).
FT   MOD_RES     132    132       N6-acetyllysine (By similarity).
FT   MOD_RES     294    294       Phosphothreonine.
FT   MOD_RES     296    296       Phosphoserine.
FT   MOD_RES     299    299       Phosphoserine.
FT   MOD_RES     348    348       Phosphoserine (By similarity).
FT   MOD_RES     358    358       Phosphoserine (By similarity).
FT   MOD_RES     496    496       Phosphoserine.
FT   MOD_RES     499    499       Phosphotyrosine.
FT   MOD_RES     521    521       Phosphotyrosine (By similarity).
FT   VAR_SEQ       1     79       Missing (in isoform 4).
FT                                /FTId=VSP_021697.
FT   VAR_SEQ     329    394       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_021698.
FT   VAR_SEQ     329    338       Missing (in isoform 4).
FT                                /FTId=VSP_021699.
FT   VAR_SEQ     329    338       LMSLLTSPHQ -> VLAIWTLRGL (in isoform 5).
FT                                /FTId=VSP_021700.
FT   VAR_SEQ     339    616       Missing (in isoform 5).
FT                                /FTId=VSP_021701.
FT   VAR_SEQ     390    394       Missing (in isoform 4).
FT                                /FTId=VSP_021702.
FT   VAR_SEQ     515    515       E -> ES (in isoform 3).
FT                                /FTId=VSP_021703.
SQ   SEQUENCE   616 AA;  71344 MW;  947BFCFCCA4BD1E2 CRC64;
     MSWGTELWDQ FDNLEKHTQW GIDILEKYIK FVKERTEIEL SYAKQLRNLS KKYQPKKNSK
     EEEEYKYTAC KAFLSTLNEM NDYAGQHEVI SENMTSQITV DLMRYVQELK QERKSNFHDG
     RKAQQHIETC WKQLESSKRR FERDCKEADR AQQYFEKMDA DINVTKADVE KARQQAQIRQ
     QMAEDSKADY SLILQRFNQE QWEYYHTHIP NIFQKIQEME ERRIVRIGES MKTYAEVDRQ
     VIPIIGKCLD GIVKAAESID QKNDSQLVVE AYKSGFEPPG DIEFEDYTQP MKRTVSDNSL
     SSSKEGKPEL RFGGKSRGKL WPFIKKNKLM SLLTSPHQPP PPPPASASPS AVPNGPQSPK
     QPKEPLSHRF NEFMTSKPKI HCFRSLKRGL SLKLGVTPED FSNFPPEQRR KKLQQKVDDL
     NREIQKETDQ RDAITKMKDV YLKNPQMGDP ASLDQKLTEV TQNIEKLRLE AQKFEAWLAE
     VEGRLPARSE QARRQSGLYD GQTHQTVTNC AQDRESPDGS YTEEQSQESE HKVLAPDFDD
     EFDDEEPLPA IGTCKALYTF EGQNEGTISV VEGETLSVIE EDKGDGWTRI RRNEDEEGYV
     PTSYVEVYLD KNAKGS
//
ID   AUXI_MOUSE              Reviewed;         938 AA.
AC   Q80TZ3; B1B0B9; Q6P2K9; Q8C7L9;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   08-FEB-2011, entry version 63.
DE   RecName: Full=Putative tyrosine-protein phosphatase auxilin;
DE            EC=3.1.3.48;
DE   AltName: Full=DnaJ homolog subfamily C member 6;
GN   Name=Dnajc6; Synonyms=Kiaa0473;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain, Hippocampus, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Recruits HSPA8/HSC70 to clathrin-coated vesicles and
CC       promotes uncoating of clathrin-coated vesicles (By similarity).
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- SUBUNIT: Interacts with HSPA8/HSC70. Interacts with CLTC.
CC       Interacts with AP2A2 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q80TZ3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80TZ3-2; Sequence=VSP_019582;
CC       Name=3;
CC         IsoId=Q80TZ3-3; Sequence=VSP_019583;
CC   -!- SIMILARITY: Contains 1 C2 tensin-type domain.
CC   -!- SIMILARITY: Contains 1 J domain.
CC   -!- SIMILARITY: Contains 1 phosphatase tensin-type domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH60734.1; Type=Erroneous initiation;
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DR   EMBL; AK122293; BAC65575.1; -; mRNA.
DR   EMBL; AK049935; BAC33992.1; -; mRNA.
DR   EMBL; AK147570; BAE28000.1; -; mRNA.
DR   EMBL; AK147637; BAE28039.1; -; mRNA.
DR   EMBL; AK163657; BAE37443.1; -; mRNA.
DR   EMBL; BX323551; CAM16148.1; -; Genomic_DNA.
DR   EMBL; BC060734; AAH60734.1; ALT_INIT; mRNA.
DR   EMBL; BC064460; AAH64460.1; -; mRNA.
DR   IPI; IPI00330269; -.
DR   IPI; IPI00650037; -.
DR   IPI; IPI00762713; -.
DR   RefSeq; NP_001158055.1; NM_001164583.1.
DR   RefSeq; NP_001158056.1; NM_001164584.1.
DR   RefSeq; NP_001158057.1; NM_001164585.1.
DR   RefSeq; NP_940804.1; NM_198412.2.
DR   UniGene; Mm.76494; -.
DR   ProteinModelPortal; Q80TZ3; -.
DR   SMR; Q80TZ3; 81-427, 762-938.
DR   STRING; Q80TZ3; -.
DR   PhosphoSite; Q80TZ3; -.
DR   PRIDE; Q80TZ3; -.
DR   Ensembl; ENSMUST00000038207; ENSMUSP00000044251; ENSMUSG00000028528.
DR   Ensembl; ENSMUST00000094953; ENSMUSP00000092560; ENSMUSG00000028528.
DR   Ensembl; ENSMUST00000106933; ENSMUSP00000102546; ENSMUSG00000028528.
DR   GeneID; 72685; -.
DR   KEGG; mmu:72685; -.
DR   UCSC; uc008tvq.1; mouse.
DR   UCSC; uc008tvs.1; mouse.
DR   UCSC; uc008tvt.1; mouse.
DR   CTD; 72685; -.
DR   MGI; MGI:1919935; Dnajc6.
DR   eggNOG; roNOG11198; -.
DR   GeneTree; ENSGT00550000074191; -.
DR   HOVERGEN; HBG004322; -.
DR   OMA; EDVFHPS; -.
DR   PhylomeDB; Q80TZ3; -.
DR   BRENDA; 3.1.3.48; 244.
DR   NextBio; 336731; -.
DR   ArrayExpress; Q80TZ3; -.
DR   Bgee; Q80TZ3; -.
DR   CleanEx; MM_DNAJC6; -.
DR   Genevestigator; Q80TZ3; -.
DR   GermOnline; ENSMUSG00000028528; Mus musculus.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR001623; DnaJ_N.
DR   InterPro; IPR014019; Phosphatase_tensin-typ.
DR   InterPro; IPR014020; Tensin_phosphatase_C2-dom.
DR   Gene3D; G3DSA:1.10.287.110; DnaJ_N; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF10409; PTEN_C2; 1.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF46565; DnaJ_N; 1.
DR   PROSITE; PS51182; C2_TENSIN; 1.
DR   PROSITE; PS00636; DNAJ_1; FALSE_NEG.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51181; PPASE_TENSIN; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Chaperone; Hydrolase; Phosphoprotein;
KW   Protein phosphatase; Repeat; SH3-binding.
FT   CHAIN         1    938       Putative tyrosine-protein phosphatase
FT                                auxilin.
FT                                /FTId=PRO_0000244517.
FT   REPEAT       61     64       1.
FT   REPEAT       65     68       2.
FT   REPEAT       69     72       3.
FT   DOMAIN       80    247       Phosphatase tensin-type.
FT   DOMAIN      253    391       C2 tensin-type.
FT   DOMAIN      874    938       J.
FT   REGION       61     72       3 X 4 AA approximate tandem repeats.
FT   MOTIF       434    442       SH3-binding (Potential).
FT   COMPBIAS    491    785       Pro-rich.
FT   ACT_SITE    189    189       Phosphocysteine intermediate (Potential).
FT   MOD_RES     591    591       Phosphoserine (By similarity).
FT   MOD_RES     595    595       Phosphoserine (By similarity).
FT   MOD_RES     597    597       Phosphothreonine (By similarity).
FT   MOD_RES     721    721       Phosphothreonine (By similarity).
FT   MOD_RES     734    734       Phosphoserine (By similarity).
FT   VAR_SEQ       1     38       Missing (in isoform 2).
FT                                /FTId=VSP_019582.
FT   VAR_SEQ       1     32       MTNPKSGVAESAGLACSRAAAGENRMKDSENK -> MSLLG
FT                                SYRKKTSSDGYESLQLVDSHGDSSARGAAAGTQRATAGAVR
FT                                SPARQPPHRASTTDSS (in isoform 3).
FT                                /FTId=VSP_019583.
FT   CONFLICT    442    442       P -> T (in Ref. 1; BAC65575).
SQ   SEQUENCE   938 AA;  102299 MW;  3DFB7D9275BEF3F6 CRC64;
     MTNPKSGVAE SAGLACSRAA AGENRMKDSE NKGASSPDME PSYGGGLFDM VKGGAGRLFS
     NLKDNLKDTL KDTSSRVIQS VSSYTKGDLD FTYVTSRIIV MSFPVDSVDI GFRNQVDDIR
     SFLDSRHLDH YTVYNLSPKS YRTAKFHSRV SECSWPIRQA PSLHNLFAVC RNMYNWLLQN
     PKNVCVVHCL DGRAASSILV GAMFIFCNLY STPGPAVRLL YAKRPGIGLS PSHRRYLGYM
     CDLLADKPYR PHFKPLTIKA ITVSPVPFFN KQRNGCRPYC DVLIGETKIY STCTDFERMK
     EYRVQDGKIF IPLNITVQGD VIVSMYHLRS TIGSRLQAKV TNTQIFQLQF HSGFIPLDTT
     VLKFTKPELD ACDVPEKYPQ LFQVTLDIEV QPQDKVIDLT PPWEHYCTKD VNPSILFSSQ
     QEHQDTLALG GQAPADLPPD HPRNLGQGGF FASLCWQDQK SEKSRCEEDH AALVNQESEQ
     SDDELLTLSS PHGNAEGDKP HGAKKPGKKQ QEPAAPPPPE EVDLLGLEGS DVSTNFSSLA
     APPSNSELLS DLFGGVGATG PAQAGQAGVE DVFHPSGPVS AQSTPRRTAT SASASPTLRV
     GEGATFDPFG APAKPPGQDL LGSFLNTSSA SSDPFLQPTR SPSPTVHASS TPAVNIQPDI
     AGGWDWHTKP GGFGMGSKSA ATSPTGSSHG TPTHQSKPQT LDPFADLGTL GSSSFASKPT
     TPTGLGGGFP PLSSPQKASP QPMGGGWQQP AGYNWQQTQS KPQSSMPHSS PQNRPNYNVS
     FSAMPAGQSE RGKGSTNLEG KQKAADFEDL LSSQGFNAHK DKKGPRTIAE MRKEEMAKEM
     DPEKLKILEW IEGKERNIRA LLSTMHTVLW AGETKWKPVG MADLVTPEQV KKVYRRAVLV
     VHPDKATGQP YEQYAKMIFM ELNDAWSEFE NQGQKPLY
//
ID   RERE_MOUSE              Reviewed;        1558 AA.
AC   Q80TZ9;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, sequence version 2.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Arginine-glutamic acid dipeptide repeats protein;
DE   AltName: Full=Atrophin-2;
GN   Name=Rere; Synonyms=Atr2, Kiaa0458;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 673-1558.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   FUNCTION, INTERACTION WITH ATN1 AND HDAC1, DEVELOPMENTAL STAGE, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=14645126; DOI=10.1242/dev.00908;
RA   Zoltewicz J.S., Stewart N.J., Leung R., Peterson A.S.;
RT   "Atrophin 2 recruits histone deacetylase and is required for the
RT   function of multiple signaling centers during mouse embryogenesis.";
RL   Development 131:3-14(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-675 AND
RP   SER-679, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600 AND SER-656, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Plays a role as a transcriptional repressor during
CC       development. May play a role in the control of cell survival.
CC   -!- SUBUNIT: Interacts with HDAC1 and ATN1. Interaction with ATN1 is
CC       improved when the poly-Gln region of ATN1 is extended.
CC   -!- INTERACTION:
CC       Q13547:HDAC1 (xeno); NbExp=1; IntAct=EBI-904076, EBI-301834;
CC       O09106:Hdac1; NbExp=1; IntAct=EBI-904076, EBI-301912;
CC   -!- SUBCELLULAR LOCATION: Nucleus, PML body (By similarity).
CC       Note=Localized in nuclear bodies of variables size. Colocalized
CC       with PML and BAX in nuclear PODs (By similarity).
CC   -!- DEVELOPMENTAL STAGE: At E8.25 expression is strongly elevated in
CC       the anterior midline. At E8.5 expression is elevated throughout
CC       the anteroposterior extent of the notochord and is down-regulated
CC       in the heart. At E8.75 expression is increased in the ventral
CC       brain. At E9.5 strong expression appears besides the notochord
CC       including the apical ectodermal ridge (AER), the isthmus and the
CC       ventral diencephalon. At E10.5 expression increases in the
CC       notochord, the AER and spinal and brain neurons.
CC   -!- DOMAIN: The interaction with ATN1 is mediated by the coiled domain
CC       (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice embryos exhibit a variety of patterning
CC       defects that first appear at E8.0. Defects include a specific
CC       failure in ventralization of the anterior neural plate, loss of
CC       heart looping and irregular partitioning of somites. In mutant
CC       embryos, Shh expression fails to initiate along the anterior
CC       midline at E8.0, and Fgf8 is delocalized from the anterior neural
CC       ridge at E8.5.
CC   -!- SIMILARITY: Contains 1 BAH domain.
CC   -!- SIMILARITY: Contains 1 ELM2 domain.
CC   -!- SIMILARITY: Contains 1 GATA-type zinc finger.
CC   -!- SIMILARITY: Contains 1 SANT domain.
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DR   EMBL; AL606982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL606988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL691453; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK122287; BAC65569.1; -; Transcribed_RNA.
DR   IPI; IPI00330272; -.
DR   UniGene; Mm.291274; -.
DR   ProteinModelPortal; Q80TZ9; -.
DR   SMR; Q80TZ9; 392-446.
DR   IntAct; Q80TZ9; 2.
DR   STRING; Q80TZ9; -.
DR   PhosphoSite; Q80TZ9; -.
DR   PRIDE; Q80TZ9; -.
DR   Ensembl; ENSMUST00000037916; ENSMUSP00000042832; ENSMUSG00000039852.
DR   Ensembl; ENSMUST00000105682; ENSMUSP00000101307; ENSMUSG00000039852.
DR   UCSC; uc008vxr.1; mouse.
DR   MGI; MGI:2683486; Rere.
DR   GeneTree; ENSGT00580000081398; -.
DR   HOGENOM; HBG446647; -.
DR   HOVERGEN; HBG079774; -.
DR   InParanoid; Q80TZ9; -.
DR   OrthoDB; EOG4XGZZB; -.
DR   ArrayExpress; Q80TZ9; -.
DR   Bgee; Q80TZ9; -.
DR   CleanEx; MM_RERE; -.
DR   Genevestigator; Q80TZ9; -.
DR   GO; GO:0000118; C:histone deacetylase complex; IPI:MGI.
DR   GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006338; P:chromatin remodeling; IPI:MGI.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR002951; Atrophin-like.
DR   InterPro; IPR001025; BAH_dom.
DR   InterPro; IPR000949; ELM2_dom.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR001005; SANT_DNA-bd.
DR   InterPro; IPR017884; SANT_eukarya.
DR   InterPro; IPR000679; Znf_GATA.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   Gene3D; G3DSA:3.30.50.10; Znf_NHR/GATA; 1.
DR   Pfam; PF03154; Atrophin-1; 1.
DR   Pfam; PF01426; BAH; 1.
DR   Pfam; PF01448; ELM2; 1.
DR   Pfam; PF00320; GATA; 1.
DR   SMART; SM00439; BAH; 1.
DR   SMART; SM00717; SANT; 1.
DR   SMART; SM00401; ZnF_GATA; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
DR   PROSITE; PS51038; BAH; 1.
DR   PROSITE; PS51156; ELM2; 1.
DR   PROSITE; PS00344; GATA_ZN_FINGER_1; FALSE_NEG.
DR   PROSITE; PS50114; GATA_ZN_FINGER_2; FALSE_NEG.
DR   PROSITE; PS51293; SANT; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Developmental protein; Metal-binding; Nucleus;
KW   Phosphoprotein; Repressor; Transcription; Transcription regulation;
KW   Zinc; Zinc-finger.
FT   CHAIN         1   1558       Arginine-glutamic acid dipeptide repeats
FT                                protein.
FT                                /FTId=PRO_0000083505.
FT   DOMAIN      103    283       BAH.
FT   DOMAIN      284    387       ELM2.
FT   DOMAIN      391    443       SANT.
FT   ZN_FING     507    532       GATA-type.
FT   COILED     1148   1203       Potential.
FT   COMPBIAS    738   1110       Pro-rich.
FT   COMPBIAS   1171   1196       Arg/Glu-rich (mixed charge).
FT   COMPBIAS   1292   1314       Arg/Glu-rich (mixed charge).
FT   COMPBIAS   1417   1437       His-rich.
FT   COMPBIAS   1443   1502       Pro-rich.
FT   MOD_RES      53     53       Phosphoserine (By similarity).
FT   MOD_RES      56     56       Phosphoserine (By similarity).
FT   MOD_RES     304    304       Phosphoserine (By similarity).
FT   MOD_RES     594    594       Phosphoserine (By similarity).
FT   MOD_RES     600    600       Phosphoserine.
FT   MOD_RES     613    613       Phosphoserine (By similarity).
FT   MOD_RES     642    642       Phosphoserine (By similarity).
FT   MOD_RES     656    656       Phosphoserine.
FT   MOD_RES     675    675       Phosphoserine.
FT   MOD_RES     679    679       Phosphoserine.
FT   MOD_RES    1098   1098       Phosphoserine (By similarity).
FT   MOD_RES    1105   1105       Phosphoserine (By similarity).
FT   MOD_RES    1107   1107       Phosphoserine (By similarity).
SQ   SEQUENCE   1558 AA;  171725 MW;  FAB068C0077B1300 CRC64;
     MTADKDKDKD KEKDRDRDRD RERDKRDKAR ESENARPRRS CTLEGGAKNY AESDHSEDED
     NDNNSATTEE SNKKSRKKPP KKKSRYERTD TGEITSYITE DDVVYRPGDC VYIESRRPNT
     PYFICSIQDF KLVHSSQACC RSPAPAFCDP PACSLPVAPQ PPQHLSEAGR GPGGSKRDHL
     LMNVKWYYRQ SEVPDSVYQH LVQDRHNEND SGRELVITDP VIKNRELFIS DYVDTYHAAA
     LRGKCNISHF SDIFAAREFK ARVDSFFYIL GYNPETRRLN STQGEIRVGP SHQAKLPDLQ
     PFPSPDGDTV TQHEELVWMP GVSDCDLLMY LRAARSMAAF AGMCDGGSTE DGCVAASRDD
     TTLNALNTLH ESSYDAGKAL QRLVKKPVPK LIEKCWTEDE VKRFVKGLRQ YGKNFFRIRK
     ELLPSKETGE LITFYYYWKK TPEAASSRAH RRHRRQAVFR RIKTRTASTP VNTPSRPPSS
     EFLDLSSASE DDFDSEDSEQ ELKGYACRHC FTTTSKDWHH GGRENILLCT DCRIHFKKYG
     ELPPIEKPVD PPPFMFKPVK EEDDGLSGKH SMRTRRSRGS MSTLRSGRKK QPTSPDGRAS
     PINEDIRSSG RNSPSAASTS SNDSKAETVK KSAKKVKEEA ASPLKSTKRQ REKVASDTED
     TDRITSKKTK TQEISRPNSP SEGEGESSDS RSVNDEGSSD PKDIDQDNRS TSPSIPSPQD
     NESDSDSSAQ QQMLQAQPPA LQAPSGAASA PSTAPPGTPQ LPTQGPTPSA TAVPPQGSPA
     TSQPPNQTQS TVAPAAHTHI QQAPTLHPPR LPSPHPPLQP MTAPPSQSSA QPHPQPSLHG
     QGPPGPHSLQ TGPLLQHPGP PQPFGLPSQP SQGQGPLGPS PAAAHPHSTI QLPASQSALQ
     PQQPPREQPL PPAPLAMPHI KPPPTTPIPQ LPAPQAHKHP PHLSGPSPFS LNANLPPPPA
     LKPLSSLSTH HPPSAHPPPL QLMPQSQPLP SSPAQPPGLT QSQSLPPPAA SHPTTGLHQV
     PSQSPFPQHP FVPGGPPPIT PPSCPPTSTP PAGPSSSSQP PCSAAVSSGG SVPGAPSCPL
     PAVQIKEEAL DEAEEPESPP PPPRSPSPEP TVVDTPSHAS QSARFYKHLD RGYNSCARTD
     LYFMPLAGSK LAKKREEAIE KAKREAEQKA REEREREKEK EKERERERER EREAERAAKA
     SSSAHEGRLS DPQLSGPGHM RPSFEPPPTT IAAVPPYIGP DTPALRTLSE YARPHVMSPT
     NRNHPFYMPL NPTDPLLAYH MPGLYNVDPT IRERELRERE IREREIRERE LRERMKPGFE
     VKPPELDPLH PATNPMEHFA RHSALTIPPA AGPHPFASFH PGLNPLERER LALAGPQLRP
     EMSYPDRLAA ERIHAERMAS LTSDPLARLQ MFNVTPHHHQ HSHIHSHLHL HQQDPLHQGS
     AGPVHPLVDP LTAGPHLARF PYPPGTLPNP LLGQPPHEHE MLRHPVFGTP YPRDLPGAIP
     PPMSAAHQLQ AMHAQSAELQ RLAMEQQWLH GHPHMHGGHL PSQEDYYSRL KKEGDKQL
//
ID   PJA2_MOUSE              Reviewed;         707 AA.
AC   Q80U04; Q3TH95; Q810E3; Q91W46; Q99KC0;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=E3 ubiquitin-protein ligase Praja-2;
DE            Short=Praja2;
DE            EC=6.3.2.-;
DE   AltName: Full=RING finger protein 131;
GN   Name=Pja2; Synonyms=Kiaa0438, Rnf131;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
RP   UBE2D2.
RC   STRAIN=129/SvJ;
RX   MEDLINE=22032989; PubMed=12036302; DOI=10.1006/geno.2002.6770;
RA   Yu P., Chen Y., Tagle D.A., Cai T.;
RT   "PJA1, encoding a RING-H2 finger ubiquitin ligase, is a novel human X
RT   chromosome gene abundantly expressed in brain.";
RL   Genomics 79:869-874(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 326-707 (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 8-18, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: Has E2-dependent E3 ubiquitin-protein ligase activity.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Binds ubiquitin-conjugating enzymes (E2s). In vitro,
CC       interacts with the ubiquitin-conjugating enzyme, UBE2D2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum membrane;
CC       Peripheral membrane protein. Golgi apparatus membrane; Peripheral
CC       membrane protein. Cell junction, synapse (By similarity). Cell
CC       junction, synapse, postsynaptic cell membrane, postsynaptic
CC       density (By similarity). Note=Localizes at the cytoplasmic side of
CC       endoplasmic reticulum and Golgi apparatus. Expressed in the
CC       postsynaptic density region of synapses (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80U04-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80U04-2; Sequence=VSP_023199;
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65564.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF493070; AAO85470.1; -; mRNA.
DR   EMBL; AK122282; BAC65564.1; ALT_INIT; mRNA.
DR   EMBL; AK144586; BAE25949.1; -; mRNA.
DR   EMBL; AK168371; BAE40303.1; -; mRNA.
DR   EMBL; BC004742; AAH04742.1; -; mRNA.
DR   EMBL; BC017130; AAH17130.1; -; mRNA.
DR   IPI; IPI00127272; -.
DR   IPI; IPI00377724; -.
DR   RefSeq; NP_001020480.1; NM_001025309.1.
DR   RefSeq; NP_659108.1; NM_144859.2.
DR   UniGene; Mm.478022; -.
DR   HSSP; Q9LRB7; 1IYM.
DR   ProteinModelPortal; Q80U04; -.
DR   SMR; Q80U04; 564-677.
DR   IntAct; Q80U04; 1.
DR   STRING; Q80U04; -.
DR   PhosphoSite; Q80U04; -.
DR   PRIDE; Q80U04; -.
DR   Ensembl; ENSMUST00000024888; ENSMUSP00000024888; ENSMUSG00000024083.
DR   Ensembl; ENSMUST00000024889; ENSMUSP00000024889; ENSMUSG00000024083.
DR   GeneID; 224938; -.
DR   KEGG; mmu:224938; -.
DR   CTD; 224938; -.
DR   MGI; MGI:2159342; Pja2.
DR   GeneTree; ENSGT00530000062967; -.
DR   HOGENOM; HBG283654; -.
DR   HOVERGEN; HBG003815; -.
DR   InParanoid; Q80U04; -.
DR   OMA; WSASLPH; -.
DR   OrthoDB; EOG4D52XB; -.
DR   PhylomeDB; Q80U04; -.
DR   NextBio; 377480; -.
DR   ArrayExpress; Q80U04; -.
DR   Bgee; Q80U04; -.
DR   CleanEx; MM_PJA2; -.
DR   Genevestigator; Q80U04; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell junction; Cell membrane;
KW   Cytoplasm; Direct protein sequencing; Endoplasmic reticulum;
KW   Golgi apparatus; Ligase; Membrane; Metal-binding; Phosphoprotein;
KW   Postsynaptic cell membrane; Synapse; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    707       E3 ubiquitin-protein ligase Praja-2.
FT                                /FTId=PRO_0000278231.
FT   ZN_FING     633    674       RING-type; atypical.
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES     320    320       Phosphoserine (By similarity).
FT   MOD_RES     377    377       Phosphotyrosine (By similarity).
FT   MOD_RES     378    378       Phosphoserine (By similarity).
FT   MOD_RES     381    381       Phosphothreonine (By similarity).
FT   MOD_RES     426    426       Phosphoserine (By similarity).
FT   MOD_RES     427    427       Phosphoserine (By similarity).
FT   MOD_RES     430    430       Phosphoserine (By similarity).
FT   VAR_SEQ     426    488       SSECSDGEWSASLPHRFSGTEKDQSSSDDSWETLPGKDEND
FT                                PELQSDSSGPEEENQELSLQEG -> R (in isoform
FT                                2).
FT                                /FTId=VSP_023199.
FT   CONFLICT    230    230       E -> A (in Ref. 3; BAE40303).
SQ   SEQUENCE   707 AA;  77958 MW;  F0D45E2267CC7EAA CRC64;
     MSQYTEKEPS VMDQESSKAA WPKPAGGYQT ITGRRYGRRH AYVSFKPCMT RHERSLGRAG
     DDYEVLELDD VPKENTSGSS SLDQVHPALP NEPTVEKSET EISTCGPALN QSTESSPSIA
     TVCHSEEVRE TLESNTNLHN RTETEHTPAV CNVSSVQNGI MLVHTDSYDP DSKHDENGSL
     QLGAEAVEGG RHQKGLGRAV FELENGEAEI YADLSPSVPS LNGEISEAFE ELDSAPLEKS
     STADAELVHQ NGQEFQRSSE DGVVRKRRQD DTDQGRQTEN STEDADCAPG HVEQNTSDRA
     NHHGSSPEQV VRPKVRKVIS SSQVDQEIGF NRHEAKQRSV QRWREALEVE ECSSDDPIIK
     CDDYDGDHDC MFLTPTYSRV TQRETERNRV TSENGATASG RQESRDNAFW NACGEYYQLF
     DKDEDSSECS DGEWSASLPH RFSGTEKDQS SSDDSWETLP GKDENDPELQ SDSSGPEEEN
     QELSLQEGEQ TSLEEGEIPW LQYNEVNESS SDEGNEPANE FAQPEAFMLD GNNNLEDDSS
     VSEDLDVDWS LFDGFADGLG VAEAISYVDP QFLTYMALEE RLAQAMETAL AHLESLAVDV
     EVANPPASKE SIDGLPETLV LEDHTAIGQE QCCPICCSEY IKDDIATELP CHHFFHKPCV
     SIWLQKSGTC PVCRRHFPPA VIDASAAASS DPDPDASPAN DNAEEAP
//
ID   DAAM2_MOUSE             Reviewed;        1115 AA.
AC   Q80U19; Q6TAB7; Q810J5;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 3.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Disheveled-associated activator of morphogenesis 2;
GN   Name=Daam2; Synonyms=Kiaa0381;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   PubMed=15533824; DOI=10.1016/j.modgep.2004.06.001;
RA   Nakaya M.-A., Habas R., Biris K., Dunty W.C. Jr., Kato Y., He X.,
RA   Yamaguchi T.P.;
RT   "Identification and comparative expression analyses of Daam genes in
RT   mouse and Xenopus.";
RL   Gene Expr. Patterns 5:97-105(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=15464228; DOI=10.1016/j.devbrainres.2004.07.014;
RA   Kida Y., Shiraishi T., Ogura T.;
RT   "Identification of chick and mouse Daam1 and Daam2 genes and their
RT   expression patterns in the central nervous system.";
RL   Brain Res. Dev. Brain Res. 153:143-150(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80U19-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80U19-2; Sequence=VSP_008005, VSP_008006;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: In early embryogenesis, expression is confined
CC       to embryonic ectoderm. Highly dynamic expression in later stages
CC       of gastrulation. In early somite stages, detected in posterior
CC       node and persists until 9-10 somites have developed when
CC       expression is concentrated in the chordoneural hinge. During
CC       organogenesis, expressed in the CNS, PNS, liver primordia, limb
CC       buds and genital tubercle.
CC   -!- SIMILARITY: Belongs to the formin homology family.
CC   -!- SIMILARITY: Contains 1 DAD (diaphanous autoregulatory) domain.
CC   -!- SIMILARITY: Contains 1 FH1 (formin homology 1) domain.
CC   -!- SIMILARITY: Contains 1 FH2 (formin homology 2) domain.
CC   -!- SIMILARITY: Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology
CC       3) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65548.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC       Sequence=BAC65548.2; Type=Miscellaneous discrepancy; Note=Wrong choice of CDS;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY426536; AAR05119.1; -; mRNA.
DR   EMBL; AK122266; BAC65548.2; ALT_SEQ; Transcribed_RNA.
DR   EMBL; BC050043; AAH50043.1; -; mRNA.
DR   IPI; IPI00338570; -.
DR   IPI; IPI00421126; -.
DR   RefSeq; NP_001008232.2; NM_001008231.2.
DR   UniGene; Mm.211275; -.
DR   ProteinModelPortal; Q80U19; -.
DR   SMR; Q80U19; 48-420, 590-1085.
DR   STRING; Q80U19; -.
DR   PhosphoSite; Q80U19; -.
DR   PRIDE; Q80U19; -.
DR   Ensembl; ENSMUST00000057610; ENSMUSP00000052085; ENSMUSG00000040260.
DR   Ensembl; ENSMUST00000086917; ENSMUSP00000084135; ENSMUSG00000040260.
DR   GeneID; 76441; -.
DR   KEGG; mmu:76441; -.
DR   UCSC; uc008cyn.1; mouse.
DR   CTD; 76441; -.
DR   MGI; MGI:1923691; Daam2.
DR   eggNOG; roNOG09539; -.
DR   GeneTree; ENSGT00600000084372; -.
DR   HOGENOM; HBG357301; -.
DR   HOVERGEN; HBG101333; -.
DR   InParanoid; Q80U19; -.
DR   OrthoDB; EOG4MKNFH; -.
DR   NextBio; 345162; -.
DR   ArrayExpress; Q80U19; -.
DR   Bgee; Q80U19; -.
DR   Genevestigator; Q80U19; -.
DR   GermOnline; ENSMUSG00000040260; Mus musculus.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   InterPro; IPR003104; Actin-bd_FH2/DRF_autoreg.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR014767; Diaphanous_autoregulatory.
DR   InterPro; IPR010472; Drf_FH3.
DR   InterPro; IPR010473; Drf_GTPase-bd.
DR   InterPro; IPR015425; FH2_actin-bd.
DR   InterPro; IPR014768; GTPase-bd/formin_homology_3.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF06367; Drf_FH3; 1.
DR   Pfam; PF06371; Drf_GBD; 1.
DR   Pfam; PF02181; FH2; 1.
DR   SMART; SM00498; FH2; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF101447; FH2_actin_bd; 1.
DR   PROSITE; PS51231; DAD; 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil.
FT   CHAIN         1   1115       Disheveled-associated activator of
FT                                morphogenesis 2.
FT                                /FTId=PRO_0000194910.
FT   DOMAIN       40    416       GBD/FH3.
FT   DOMAIN      518    694       FH1.
FT   DOMAIN      595   1042       FH2.
FT   DOMAIN     1065   1095       DAD.
FT   COILED      434    515       Potential.
FT   COMPBIAS    518    604       Pro-rich.
FT   VAR_SEQ     516    524       TGPVSSPPP -> VRGHHPHPI (in isoform 2).
FT                                /FTId=VSP_008005.
FT   VAR_SEQ     525   1115       Missing (in isoform 2).
FT                                /FTId=VSP_008006.
FT   CONFLICT    994    994       R -> G (in Ref. 2; BAC65548).
FT   CONFLICT    997    997       D -> E (in Ref. 2; BAC65548).
SQ   SEQUENCE   1115 AA;  128455 MW;  FD3B0BE2CED5A85B CRC64;
     MALRKRSPHG LGFLCCFGGS DLPEIDLRDS HPLQYLEFSG PIPNPEELNV RFAELVDELD
     LTDKNREAVF ALPPEKKWQI YCSKRKEQED PNKLATSWPE YYIDRINAMA AMQNLYETED
     EETDKRNQVV EDLKTALRTQ PMRFVTRFID LEGLTCLLNF LRGMDHTTCE SRIHTSLIGC
     IKALMNNSQG RAHVLAQPEA ISIIAQSLRT ENSKTKVAVL EILGAVCLVP GGHKKVLQAM
     LHYQAYAAER TRFQTLLNEL DRSLGRYRDE VNLKTAIMSF INAVLNAGAG EDNLEFRLHL
     RYEFLMLGIQ PVIDKLRQHE NAILDKHLDF FEMVRNEDDL ELARRFDMVH IDTKSASQMF
     ELIHKKLKHT EAYPCLLSVL HHCLQMPYKR NGGYFQQWQL LDRILQQIVL QDERGVDPDL
     APLENFNVKN IVNMLINENE VKQWRDQAEK FRKEHMELMS RLERKERECE TKTLEKEEMM
     RTLNKMKDKL ARESQELRQA RGQVAELVAR HNESSTGPVS SPPPPGGPLT LSSSRTTNDL
     PPPPPPLPFD SCPPPPAPPL PPGGPPIPPG APPCFSSGPP PSHDPFSSNE APLRKKRIPQ
     PSHPLKSFNW VKLNEERVSG TVWNEIDDSQ VFRILDLEDF EKMFSAYQRH QACMQEGPQR
     ERGNVRDGGA ASRPLPAVEA SAHRTEKASR SMVSATGAKK ELGSTEDIYI TSRKVKELSV
     IDGRRAQNCI ILLSKLKLSN DEIRQAILRM DEQEDLAKDM LEQLLKFIPE KSDIDLLEEH
     KHEIERMARA DRFLYEMSRI DHYQQRLQAL FFKKKFQERL AEAKPKVEAI LLASRELTLS
     QRLKQMLEVV LAIGNFMNKG QRGGAYGFRV ASLNKIADTK SSIDRNISLL HYLIMILEKH
     FPDILNMPSE LKHLSEAAKV NLAELEKEVS ILRRGLRAVE VELEYQRHQA RDPNDKFVPV
     MSDFITVSSF SFSELEDQLN EARDKFAKAL THFREQDSKM QPDEFFGIFD TFLQAFLEAR
     QDLEAMRRRK EEDERRARME FMLKEQREKE RWQRQRKVLA GGALEESGEF DDLVSALRSG
     EVFDKDLSKF KRNRKRPGSQ VPEVTRERAI NRLNY
//
ID   RUSC2_MOUSE             Reviewed;        1514 AA.
AC   Q80U22; Q8R1D6;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Iporin;
DE   AltName: Full=Interacting protein of Rab1;
DE   AltName: Full=RUN and SH3 domain-containing protein 2;
GN   Name=Rusc2; Synonyms=Kiaa0375;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 857-1514 (ISOFORM 2).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1491, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SUBUNIT: Interacts with active RAB1A and RAB1B, and with GOLGA2
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Note=Cytosolic punctate
CC       distribution. Also observed in the perinuclear region (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80U22-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80U22-2; Sequence=VSP_010858, VSP_010859;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The RUN domain is required for the interaction with RAB1A
CC       and RAB1B (By similarity).
CC   -!- SIMILARITY: Contains 1 RUN domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65545.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK122263; BAC65545.1; ALT_INIT; mRNA.
DR   EMBL; BC024790; AAH24790.1; -; mRNA.
DR   IPI; IPI00153354; -.
DR   IPI; IPI00454192; -.
DR   UniGene; Mm.235730; -.
DR   ProteinModelPortal; Q80U22; -.
DR   SMR; Q80U22; 1458-1504.
DR   STRING; Q80U22; -.
DR   PhosphoSite; Q80U22; -.
DR   PRIDE; Q80U22; -.
DR   Ensembl; ENSMUST00000035645; ENSMUSP00000038379; ENSMUSG00000035969.
DR   Ensembl; ENSMUST00000098106; ENSMUSP00000095710; ENSMUSG00000035969.
DR   MGI; MGI:2140371; Rusc2.
DR   HOVERGEN; HBG059413; -.
DR   InParanoid; Q80U22; -.
DR   OrthoDB; EOG4DNF3P; -.
DR   ArrayExpress; Q80U22; -.
DR   Bgee; Q80U22; -.
DR   CleanEx; MM_RUSC2; -.
DR   Genevestigator; Q80U22; -.
DR   GermOnline; ENSMUSG00000035969; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   InterPro; IPR004012; Run.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF02759; RUN; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00593; RUN; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50826; RUN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Phosphoprotein; SH3 domain.
FT   CHAIN         1   1514       Iporin.
FT                                /FTId=PRO_0000097535.
FT   DOMAIN     1026   1170       RUN.
FT   DOMAIN     1445   1504       SH3.
FT   COMPBIAS    209    311       Ser-rich.
FT   MOD_RES     511    511       Phosphoserine.
FT   MOD_RES     534    534       Phosphoserine (By similarity).
FT   MOD_RES     651    651       Phosphoserine (By similarity).
FT   MOD_RES    1378   1378       Phosphoserine (By similarity).
FT   MOD_RES    1491   1491       Phosphothreonine.
FT   VAR_SEQ    1448   1453       CEVQAL -> WYAQGN (in isoform 2).
FT                                /FTId=VSP_010858.
FT   VAR_SEQ    1454   1514       Missing (in isoform 2).
FT                                /FTId=VSP_010859.
SQ   SEQUENCE   1514 AA;  161139 MW;  90E8E0FE3A42BFE1 CRC64;
     MDSPPKLTGE TLIVHHIPLV HCQVPDRQCC GGAGGGGGGT RANPFCPPEL GLTQPDHDLG
     QADSLLYPSL HSAPGAPTGS SDSVKSRSRD GRGPGAPKRH NPFLVQEGVG ETGLGDLHDS
     STGDSVTQQS FHLHSASQPF HLSSFQLPPS GPGQGRPWGA THSRPGVVEG QEQDPATALG
     TQCSTSHCCR PELEAERMEL DECGGHGGSG SGGGTSDISG FSFEQEWKIS SDESPRHPGR
     SGSGTQHCHC SSTSSQSEAA DQSMGYVSDS SCNSSDGVLV TFSTLYNKMH SSSRANLNSV
     PQSCSDSSFC SHADPGAFYL DLQPSPAESR MSCESHHPEN GDREEGCGCP HVSSPELDAN
     CNAYHPHSEP CPAVADLTAC FQSQARLVVA TQNYYKLVTC DLSSQSSPSP AGSSITSCSE
     EHTKISPPPG PCPDPDPNQP SEYYLFQKPD IQPEEQEAVG SPAEAATAMG PTVLEGQVYT
     NTSPPNLNTG RQRSRSYDRS LERSPPVRLG SLERMLSCPV RLSEGPAALA GPASPPRRVT
     SFAELAKGRK KAAGSGSPPL RASVGDSSQE FSPIQEAQQD RAAPLDEGTR CSHSLPSLPL
     GPSLDLLGPE PWSTPVCQGS QSSEMPLPSL RAAGQGPLAQ LMDPGPAFSG SPATSHTQRD
     SRARADGGGT ESRPVLRYSK EQRPTTLPIQ PFVFQHHFPK QLAKARALHS LSQLYSLSGC
     SRAQQPAPLV ISTAQGPAPA PSGEPQPFTS QASGRGARNA GPEPETSRPS PLGSYSPVRS
     AGPFGSSTDS SASTSCSPPP EQGTAADSVS PWSHTCPPTV RPATSQQPPK EDQKIPTLAE
     YRLHGTGSLP PLGSWRSGFT RAESLVRGGG EGSMANRPNN ANHLSPQALK WREYRRKNPL
     GPPGLSGSLD RRPPEARLAR RNPIFEFPGS FGTTSHLNCR LNGQISKPLS LTCPDLQDPF
     SLTEKPPAEF CLSPDGNSEA ISIDILQKKG LVKAVNTAVD LIVAHFGTSR DPGVKAKLGN
     SSVSPNVGHL VLKYLCPAVQ AVLEDGLKAF VLDVIIGQRK NMPWSVVEAS TQLGPSTKVL
     HGLYNKVSQF PELTSHTMRF NAFILGLLNI RSLEFWFNHL YNHEDIIQTH YQPWGFLRAA
     HTVCPGLFEE LLLLLQPLAL LPFSLDLLFQ HRLLQSGRQQ RQHKELLRVS QDLLLSAHST
     LQLARSRGQE GPGDMDRVAP GERVKGVGAS EGGEEDEEDA EEVAVVAGSS DHGKWARGGQ
     AGWWYQLMQS SQVYIDGTAE GSRFPRSSSS SSGSGSEKKK GVGSGGPSQA PPPPPREGVV
     EGAEACPAPE EALGQERGWP FWMGSPPDSV LAELRRSRER EGPVAPPTEN EEGTAEPSPG
     GIKWGHLFGS RKSQREARPT NRLPSDWLSL DKSVFQLVAQ TMGARREPEP RENLQESHPP
     AVPSKPPCEV QALCHHLATG PGQLSFHKGD ILRVLGPARG DWLRCSRGPD TGLVPLAYVT
     LPPTPSSPPG SSQN
//
ID   SNPH_MOUSE              Reviewed;         495 AA.
AC   Q80U23; A2AT08; A2AT09; A2AT10; A2AT11; A4FUV3; A4VCI7; Q4VA51;
AC   Q6GQX4; Q8C8B8;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 3.
DT   08-MAR-2011, entry version 44.
DE   RecName: Full=Syntaphilin;
GN   Name=Snph; Synonyms=Kiaa0374;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-293, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Inhibits SNARE complex formation by absorbing free
CC       syntaxin-1 (By similarity).
CC   -!- SUBUNIT: Binds to syntaxin-1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential). Cell junction, synapse, synaptosome.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q80U23-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80U23-2; Sequence=VSP_037439;
CC       Name=3;
CC         IsoId=Q80U23-3; Sequence=VSP_037440;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH72567.1; Type=Erroneous initiation;
CC       Sequence=AAH96541.1; Type=Erroneous initiation;
CC       Sequence=AAI39793.1; Type=Erroneous initiation;
CC       Sequence=BAC33090.1; Type=Erroneous initiation;
CC       Sequence=BAC65544.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK122262; BAC65544.1; ALT_INIT; mRNA.
DR   EMBL; AK047568; BAC33090.1; ALT_INIT; mRNA.
DR   EMBL; AL928719; CAM23821.1; -; Genomic_DNA.
DR   EMBL; AL928719; CAM23822.1; -; Genomic_DNA.
DR   EMBL; AL928719; CAM23823.1; -; Genomic_DNA.
DR   EMBL; AL928719; CAM23824.1; -; Genomic_DNA.
DR   EMBL; BC072567; AAH72567.1; ALT_INIT; mRNA.
DR   EMBL; BC096541; AAH96541.1; ALT_INIT; mRNA.
DR   EMBL; BC117896; AAI17897.1; -; mRNA.
DR   EMBL; BC117897; AAI17898.1; -; mRNA.
DR   EMBL; BC139792; AAI39793.1; ALT_INIT; mRNA.
DR   IPI; IPI00227035; -.
DR   IPI; IPI00608013; -.
DR   IPI; IPI00757808; -.
DR   RefSeq; NP_937857.1; NM_198214.2.
DR   UniGene; Mm.39312; -.
DR   STRING; Q80U23; -.
DR   PhosphoSite; Q80U23; -.
DR   PRIDE; Q80U23; -.
DR   Ensembl; ENSMUST00000028951; ENSMUSP00000028951; ENSMUSG00000027457.
DR   Ensembl; ENSMUST00000109875; ENSMUSP00000105501; ENSMUSG00000027457.
DR   GeneID; 241727; -.
DR   KEGG; mmu:241727; -.
DR   UCSC; uc008ned.1; mouse.
DR   CTD; 241727; -.
DR   MGI; MGI:2139270; Snph.
DR   GeneTree; ENSGT00520000055634; -.
DR   HOVERGEN; HBG006785; -.
DR   InParanoid; Q80U23; -.
DR   OMA; SGVDCGP; -.
DR   OrthoDB; EOG4VDQ03; -.
DR   NextBio; 385129; -.
DR   ArrayExpress; Q80U23; -.
DR   Bgee; Q80U23; -.
DR   CleanEx; MM_SNPH; -.
DR   Genevestigator; Q80U23; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR   GO; GO:0019717; C:synaptosome; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Coiled coil; Membrane;
KW   Phosphoprotein; Synapse; Synaptosome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    495       Syntaphilin.
FT                                /FTId=PRO_0000284137.
FT   TRANSMEM    427    446       Helical; (Potential).
FT   COILED       79    161       Potential.
FT   COMPBIAS     32     42       Poly-Ser.
FT   COMPBIAS    403    408       Poly-Glu.
FT   COMPBIAS    409    412       Poly-Ala.
FT   MOD_RES      20     20       Phosphoserine.
FT   MOD_RES     293    293       Phosphotyrosine.
FT   VAR_SEQ      16     16       R -> RSGGTLGRSGLAVFAQCPQVPASQNEQRPLLPAS
FT                                (in isoform 2).
FT                                /FTId=VSP_037439.
FT   VAR_SEQ      17     52       Missing (in isoform 3).
FT                                /FTId=VSP_037440.
FT   CONFLICT    156    156       L -> V (in Ref. 2; BAC33090).
FT   CONFLICT    165    165       K -> M (in Ref. 4; AAH96541).
FT   CONFLICT    358    358       D -> Y (in Ref. 2; BAC33090).
FT   CONFLICT    456    456       I -> V (in Ref. 4; AAI17897).
SQ   SEQUENCE   495 AA;  53753 MW;  D1BA1C0702446C97 CRC64;
     MAMSLQGSRR ASAGSRRRTS PPVSVRDAYG TSSLSSSSNS GSCKGSDSSP TPRRSMKYTL
     CSDNHGIKPP TPEQYLTPLQ QKEVCIRHLK ARLKDTQDRL QDRDTEIDDL KTQLSRMQED
     WIEEECHRVE AQLALKEARK EIRQLKQVID TVKNNLIDKD KGLQKYFVDI NIQNKKLETL
     LHSMEVAQNG VAKEEGTGES AGGSPARSLT RSSTYTKLSD PAVCGDRQPG DPSNTSAEDG
     ADSGYVAADD TLSRTDALEA SSLLSSGVDC GLEEASLHSS FNLGPRFPAS NTYEKLLCGM
     EAGVQVSCMQ ERAIQTDFVQ YQPDLNTILE KVGQAQVCGS VLKDRHSELD PHPSGPRDPD
     SAVVVTVGDE LEAPEPITCG PATHRPAVNS NPGLPVSVVC PVEEEEEEAA AATTTEKEPK
     SYWSRHYIVD LLAVVVPAVP TVAWLCRSQR RQGQPIYNIS SLLRGCCTVA LHSIRRISCR
     SLGQPSSSTA GGSQL
//
ID   Q80U25_MOUSE            Unreviewed;       370 AA.
AC   Q80U25;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   08-FEB-2011, entry version 34.
DE   SubName: Full=MKIAA0365 protein;
DE   Flags: Fragment;
GN   Name=Sugp2; Synonyms=Sfrs14, Srsf14, mKIAA0365;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
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DR   EMBL; AK122260; BAC65542.1; -; mRNA.
DR   IPI; IPI00405760; -.
DR   UniGene; Mm.284505; -.
DR   Ensembl; ENSMUST00000093458; ENSMUSP00000091167; ENSMUSG00000036054.
DR   Ensembl; ENSMUST00000131489; ENSMUSP00000114833; ENSMUSG00000036054.
DR   MGI; MGI:2678085; Sugp2.
DR   GeneTree; ENSGT00410000025695; -.
DR   HOVERGEN; HBG079176; -.
DR   InParanoid; Q80U25; -.
DR   ArrayExpress; Q80U25; -.
DR   Bgee; Q80U25; -.
DR   Genevestigator; Q80U25; -.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   InterPro; IPR000061; Surp.
DR   SMART; SM00648; SWAP; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   370 AA;  41328 MW;  246A58D36629F1C5 CRC64;
     KTKNCFFEII KPFDKSIMRL QDRLLKGVTP LLMACNAYEL SVKMKTLTSP LDLAMAMETT
     NSLCRKSLAL LGQTFSLASS FRKEKILEAV GLQDIAPSPA YFPNFEDSTL FGREYIDHLK
     AWLMASGYPL QLKRAVPPES REQKTTAQTW ASSTLSQVPQ RADHRVVDTI DQLVMRVIQG
     RLSPRERTLL LQDPAYWFLS DESSLEYKYY KLKLAESQRL NHSWPIVERR PTPAQCAVRA
     MLYAQAVRSL KRRLLPWQRR RLLRSQGPRG LKAKKATTAQ QTSLSSGTRQ KHHGRQASGS
     LRVKPPPRDS SDAAQDCLSE PAKPCPQPSS PGALGPSPRP TGADDSEALP ASSRCPSANS
     RCPPLPHPVP
//
ID   ARHGH_MOUSE             Reviewed;        2057 AA.
AC   Q80U35; Q8BZY4;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Rho guanine nucleotide exchange factor 17;
GN   Name=Arhgef17; Synonyms=Kiaa0337;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1865-2057.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142 AND SER-994, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Acts as guanine nucleotide exchange factor (GEF) for
CC       RhoA GTPases (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80U35-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q80U35-2; Sequence=VSP_025104, VSP_025105;
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65532.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK122250; BAC65532.1; ALT_INIT; mRNA.
DR   EMBL; AC116586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC150744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK033211; BAC28199.2; ALT_SEQ; mRNA.
DR   IPI; IPI00465761; -.
DR   IPI; IPI00671520; -.
DR   RefSeq; NP_001074585.1; NM_001081116.1.
DR   UniGene; Mm.29954; -.
DR   ProteinModelPortal; Q80U35; -.
DR   SMR; Q80U35; 1052-1245, 1866-1893.
DR   STRING; Q80U35; -.
DR   PhosphoSite; Q80U35; -.
DR   PRIDE; Q80U35; -.
DR   Ensembl; ENSMUST00000037681; ENSMUSP00000044676; ENSMUSG00000032875.
DR   Ensembl; ENSMUST00000107032; ENSMUSP00000102647; ENSMUSG00000032875.
DR   GeneID; 207212; -.
DR   KEGG; mmu:207212; -.
DR   UCSC; uc009inu.1; mouse.
DR   CTD; 207212; -.
DR   MGI; MGI:2673002; Arhgef17.
DR   eggNOG; roNOG09344; -.
DR   GeneTree; ENSGT00600000084097; -.
DR   HOGENOM; HBG283276; -.
DR   HOVERGEN; HBG095607; -.
DR   InParanoid; Q80U35; -.
DR   OMA; CSEKPMA; -.
DR   OrthoDB; EOG4G4GPN; -.
DR   NextBio; 371889; -.
DR   ArrayExpress; Q80U35; -.
DR   Bgee; Q80U35; -.
DR   CleanEx; MM_ARHGEF17; -.
DR   Genevestigator; Q80U35; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00741; DH_1; FALSE_NEG.
DR   PROSITE; PS50010; DH_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Guanine-nucleotide releasing factor;
KW   Phosphoprotein.
FT   CHAIN         1   2057       Rho guanine nucleotide exchange factor
FT                                17.
FT                                /FTId=PRO_0000286590.
FT   DOMAIN     1059   1247       DH.
FT   COMPBIAS    196    199       Poly-Arg.
FT   COMPBIAS    230    234       Poly-Ser.
FT   COMPBIAS    251    255       Poly-Glu.
FT   COMPBIAS    700    703       Poly-Arg.
FT   COMPBIAS    955   1047       Pro-rich.
FT   COMPBIAS   1986   1990       Poly-Pro.
FT   COMPBIAS   2035   2038       Poly-Gly.
FT   MOD_RES     138    138       Phosphoserine (By similarity).
FT   MOD_RES     142    142       Phosphoserine.
FT   MOD_RES     994    994       Phosphoserine.
FT   VAR_SEQ       1   1009       Missing (in isoform 2).
FT                                /FTId=VSP_025104.
FT   VAR_SEQ    1010   1057       DVPAPGPVDLPCLPPSAPPSTETKPSGAARATPDEPAPASK
FT                                CCSKPQV -> MLQMVKTLAQFTIALEDMRDLGSAAASGES
FT                                AGGGDGGSDTAEEPGEAQ (in isoform 2).
FT                                /FTId=VSP_025105.
FT   CONFLICT   1366   1366       I -> V (in Ref. 1; BAC65532).
FT   CONFLICT   1566   1566       N -> K (in Ref. 1; BAC65532).
SQ   SEQUENCE   2057 AA;  221671 MW;  CCB48100B1ECE03C CRC64;
     MADGSPRPPL YRSVSFKLLE RWSGGPGPRE EDADTPGLRR RASCRPAAAV PGQPSRRVSK
     LASGPPAAPA QPRPLRSLSP SVRQLSRRFD AAGLDDDSTG TRDGGCSSGT TEEAAEGSER
     GAWPSVTEMR KLFGGPSSRR PSMDSEALGS TSPDRVSWEP PTRDPRQPPT PPPRTCFPLA
     GLRSARPLSG PGIEGRRRRQ HQQQERAQRP ADGLHSWHSF SQPQAGARAS SSSSIASSYP
     VSRSRAASSS EEEEEGPQSQ LGPQSPAYLG GHSSGSDEDP NGEDGRRWRG RGLRPGRSQL
     VHGCSQDSDE LNPGGLGSAG GVGSPEPPTS PRTSMDEWGT GTQPCLPGPQ ESLRPMSDTG
     GAPFRVAKVS FPAYLASPAG SRGSSRYSST ETLKDDDLWS SRSSVGWGVY RSPSFGTGDG
     LLLRPQTRSR SKGPVGTARP LRDGGLDLDK NRQRKSLSNP DIASETLTLL SFLRSDLSEL
     RVRKPSGGPG NRPLDGRDSP SAGSPMEQSE STLSQSPTSP TTRPTLKDLT ATLRRAKSFS
     CSEKPMARRL LRTSALKPSS SELLLAGSGA EEDPLPLVVQ DQYVQEARQV FEKIQRMGAQ
     QDDGNDVCPT SPDWAGDMTQ GHRSQEELSG PESNLTDEGI GADPEPLGAA FCSLDPAGVW
     RPLSSTSAQT NHHLGAGTED SLGGRALVSP ETPPTPGALR RRRKVPPSGP NGTELSNGEA
     SEAYRSLSDP IPQRHRAATS EEPSGFSVDS NLLGSLNSKT GLPVTPAMDE GLTSGHSDWS
     VVSEENKDYQ EVIQSIVQGP GALGRMGEDR IAGKTPKKKS LSDPSRRGEL TGPGFEGPGG
     EPIREVEPML PPSSSEPILA EQWTEPEDPA PARGRAQSER SLPAPPASST AHHDFHLDPK
     LTSVLSPRLT RRGSKKRPAR SSHQELRREE GNQDQTGSLT QTRSSSKHVR HASVPATFTP
     IVVPEPAMSV GPPVAAPEPV GFPVRGHPAL QAPSLEDVTK RYMLTLHSGD VPAPGPVDLP
     CLPPSAPPST ETKPSGAARA TPDEPAPASK CCSKPQVDMR KHVTMTLLDT EQSYVESLRT
     LMQGYMQPLK QPENSLLCDP SLVDEIFDQI PELLEHHEQF LEQVRHCVQT WHAQQKVGAL
     LVQSFSKDVL VNIYSAYIDN FLNAKDAVRV AKEARPAFLK FLEQSMRENK EKQALSDLMI
     KPVQRIPRYE LLVKDLLKHT PEDHPDHPLL LDAQRNIKQV AERINKGVRS AEEAERHARV
     LQEIEAHIEG MEDLQAPLRR FLRQEMVIEV KAIGGKKDRS LFLFTDLIVC TTLKRKSGSL
     RRSSMSLYTA ASVIDTASKY KMLWKLPLED TDIIKGASQA TNRETIQKAI SRLDEDLATL
     GQMSKLSESL GFPHQSLDDA LRDLSAAMHR DLSEKQALCC SLAFPPTKLE LCATRPEGTD
     SYIFEFPHPD ARLGFEQAFD EAKRKLASSK SCLDPEFLKA IPIMKTRSGM QFSCAAPTFS
     SCPEPAPEVW VCNSDGYVGQ VCLLSLRAEP DVEACIAVCS ARILCIGAVP GLQPRCPREQ
     PEPLRNPPET TLESTGPELD VEATAEEEAA TTLAEPGPQP CLHISISGSG LEMEPGPAKG
     DPQPELVPFD SDSDDESSPS PSGTLQSQAS QSTISSSFGN EETPSSKEAT AETTSSEEEQ
     EPGFLSLSGS FGPGGPCGTS PMDGRALRRS SRGSFTRGSL EDLLSVDPEA YQSSVWLGTE
     DGCVHVYQSS DSIRDRRNSM KLQHAASVTC ILYLNNKVFV SLANGELVVY QREAGRFWDP
     QNFKSMTLGS QGSPITKMVS VGGRLWCGCQ NRVLVLSPDT LQLEHTFYVG QDSSRSVACM
     VDSSLGVWVT LKGSAHVCLY HPDTFEQLAE VDVTPPVHRM LAGSDAIIRQ HKAACLRITA
     LLVCAELLWV GTSAGVVLTI PTSPSTVSCP RAPLSPAGLC QGHTGHVRFL AAVQLPEGFN
     LLCSTPPPPP DTGPEKLPSL DHRDSPRRRG PTSARPKMLV ISGGDGSEDF RLSSGGGGSS
     ETVGRDDSTN HLLLWRV
//
ID   KHNYN_MOUSE             Reviewed;         671 AA.
AC   Q80U38; Q14B94; Q8BGJ6; Q8C082;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Protein KHNYN;
DE   AltName: Full=KH and NYN domain-containing protein;
GN   Name=Khnyn; Synonyms=Kiaa0323;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cecum, Head, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the N4BP1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC27665.1; Type=Frameshift; Positions=59;
CC       Sequence=BAC65529.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK032037; BAC27665.1; ALT_FRAME; mRNA.
DR   EMBL; AK033704; BAC28436.1; -; mRNA.
DR   EMBL; AK047955; BAC33200.1; -; mRNA.
DR   EMBL; AK122247; BAC65529.1; ALT_INIT; Transcribed_RNA.
DR   EMBL; BC116260; AAI16261.1; -; mRNA.
DR   EMBL; BC116261; AAI16262.1; -; mRNA.
DR   IPI; IPI00395037; -.
DR   RefSeq; NP_081419.1; NM_027143.2.
DR   UniGene; Mm.37592; -.
DR   UniGene; Mm.479587; -.
DR   PhosphoSite; Q80U38; -.
DR   PRIDE; Q80U38; -.
DR   Ensembl; ENSMUST00000022831; ENSMUSP00000022831; ENSMUSG00000047153.
DR   GeneID; 219094; -.
DR   KEGG; mmu:219094; -.
DR   NMPDR; fig|10090.3.peg.29138; -.
DR   UCSC; uc007ubb.1; mouse.
DR   CTD; 219094; -.
DR   MGI; MGI:2451333; Khnyn.
DR   HOGENOM; HBG717280; -.
DR   HOVERGEN; HBG052182; -.
DR   InParanoid; Q80U38; -.
DR   OMA; HCIFLGA; -.
DR   OrthoDB; EOG4V437T; -.
DR   NextBio; 376563; -.
DR   ArrayExpress; Q80U38; -.
DR   Bgee; Q80U38; -.
DR   CleanEx; MM_9130227C08RIK; -.
DR   Genevestigator; Q80U38; -.
DR   GermOnline; ENSMUSG00000047153; Mus musculus.
DR   InterPro; IPR021869; RNase_Zc3h12.
DR   Pfam; PF11977; RNase_Zc3h12a; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein.
FT   CHAIN         1    671       Protein KHNYN.
FT                                /FTId=PRO_0000084291.
FT   COMPBIAS    350    365       Pro-rich.
FT   MOD_RES     118    118       Phosphoserine (By similarity).
FT   MOD_RES     125    125       Phosphothreonine (By similarity).
FT   MOD_RES     349    349       Phosphoserine (By similarity).
FT   MOD_RES     355    355       Phosphoserine (By similarity).
FT   CONFLICT    106    106       S -> G (in Ref. 1; BAC27665).
FT   CONFLICT    155    155       P -> H (in Ref. 1; BAC27665).
SQ   SEQUENCE   671 AA;  74565 MW;  92071C233535A55A CRC64;
     MSTWGFASPT PDRFAVSAEA EDKVREQQTR LERIFNVGMS VLSKDCPENP HIWLQLEGPK
     ENVCRAKEYL KGLCSPELQS EIHYPPRLHC IFLGAHGFFL DCLAWSTSAH LVPLLPGSLM
     ISGLTEAFVM AQSRVEELVQ RLSWDLQLQS CPGAPDNGGV LRDFSALLQT REDAYTEALL
     RLPLAVQEEL LSLVQEASRG QGPSREVGSS GLLSPQFQGV RAPLNEGREF VGTRVAGSGK
     SPAVRGQSHT VEKEERKQDA VRDMGSGRKE LSGEEVWEPG VAYRSQLAGG GAEEVAPLKG
     KASGKQEVPQ QRGGFSVQGE PSGAHVPCQR AAPIRGASLL QRLHNGSASP PRVPSPPPAP
     EPPWPCGDRD RDRDRGDRGD KQQAGARGRG SPWKRGTRGG NLVTGTQRFQ EALQDPFTLC
     LANVPGQPDL RHIVIDGSNV AMVHGLQHYF SSRGIALAVQ YFWDRGHRDI TVFVPQWRFS
     KDSKVRESHF LQKLYSLSLL SLTPSRVMDG KRISSYDDRF MVKLAEETDG IIVSNDQFRD
     LAEESDKWMA IIRERLLPFT FVGNLFMVPD DPLGRNGPTL DEFLKKPVRK QGSSKTQQPS
     KGSTEQANQQ QGKDADRSNG GIRKTRETER LRRQLLEVFW GQDHKVDFIL QREPYCRDIN
     QLSEALLSLN F
//
ID   K0284_MOUSE             Reviewed;        1574 AA.
AC   Q80U49; Q3UH33; Q3UHG1; Q80UM2;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Protein KIAA0284;
GN   Name=Kiaa0284;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Trophoblast stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1341, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-978, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-965; THR-968
RP   AND THR-971, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Plays a role in microtubule organization (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80U49-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80U49-2; Sequence=VSP_024249;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the CEP170 family.
CC   -!- SIMILARITY: Contains 1 FHA domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65518.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK122236; BAC65518.1; ALT_INIT; mRNA.
DR   EMBL; AK147410; BAE27896.1; -; mRNA.
DR   EMBL; AK147612; BAE28024.1; -; mRNA.
DR   EMBL; BC050077; AAH50077.1; -; mRNA.
DR   IPI; IPI00380953; -.
DR   IPI; IPI00626986; -.
DR   RefSeq; NP_001019773.2; NM_001024602.3.
DR   UniGene; Mm.23689; -.
DR   ProteinModelPortal; Q80U49; -.
DR   SMR; Q80U49; 16-99.
DR   PhosphoSite; Q80U49; -.
DR   PRIDE; Q80U49; -.
DR   Ensembl; ENSMUST00000092279; ENSMUSP00000089930; ENSMUSG00000072825.
DR   Ensembl; ENSMUST00000101018; ENSMUSP00000098580; ENSMUSG00000072825.
DR   GeneID; 217882; -.
DR   KEGG; mmu:217882; -.
DR   MGI; MGI:2145043; AW555464.
DR   eggNOG; roNOG15380; -.
DR   GeneTree; ENSGT00510000046748; -.
DR   HOGENOM; HBG714398; -.
DR   HOVERGEN; HBG108016; -.
DR   InParanoid; Q80U49; -.
DR   OMA; WLVQNDP; -.
DR   OrthoDB; EOG4548XT; -.
DR   NextBio; 376091; -.
DR   ArrayExpress; Q80U49; -.
DR   Bgee; Q80U49; -.
DR   CleanEx; MM_AW555464; -.
DR   Genevestigator; Q80U49; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR008984; SMAD_FHA_domain.
DR   Gene3D; G3DSA:2.60.200.20; FHA; 1.
DR   Pfam; PF00498; FHA; 1.
DR   SMART; SM00240; FHA; 1.
DR   SUPFAM; SSF49879; SMAD_FHA; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Cytoskeleton; Isopeptide bond;
KW   Microtubule; Phosphoprotein; Ubl conjugation.
FT   CHAIN         1   1574       Protein KIAA0284.
FT                                /FTId=PRO_0000282890.
FT   DOMAIN       23     73       FHA.
FT   MOD_RES     360    360       Phosphoserine.
FT   MOD_RES     595    595       Phosphoserine (By similarity).
FT   MOD_RES     653    653       Phosphoserine (By similarity).
FT   MOD_RES     744    744       Phosphoserine (By similarity).
FT   MOD_RES     746    746       Phosphoserine (By similarity).
FT   MOD_RES     749    749       Phosphoserine (By similarity).
FT   MOD_RES     751    751       Phosphoserine (By similarity).
FT   MOD_RES     882    882       Phosphoserine.
FT   MOD_RES     965    965       Phosphoserine.
FT   MOD_RES     968    968       Phosphothreonine.
FT   MOD_RES     971    971       Phosphothreonine.
FT   MOD_RES     978    978       Phosphoserine.
FT   MOD_RES     981    981       Phosphoserine (By similarity).
FT   MOD_RES    1122   1122       Phosphoserine (By similarity).
FT   MOD_RES    1168   1168       Phosphothreonine (By similarity).
FT   MOD_RES    1289   1289       Phosphothreonine (By similarity).
FT   MOD_RES    1341   1341       Phosphoserine.
FT   MOD_RES    1530   1530       Phosphoserine (By similarity).
FT   MOD_RES    1533   1533       Phosphoserine (By similarity).
FT   CROSSLNK    289    289       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   VAR_SEQ     259   1174       Missing (in isoform 2).
FT                                /FTId=VSP_024249.
FT   CONFLICT     54     54       E -> V (in Ref. 2; BAE28024).
FT   CONFLICT    237    237       P -> L (in Ref. 3; AAH50077).
FT   CONFLICT   1365   1365       E -> G (in Ref. 2; BAE27896).
FT   CONFLICT   1428   1428       L -> P (in Ref. 3; AAH50077).
SQ   SEQUENCE   1574 AA;  170821 MW;  9CB9DB93413B3B1F CRC64;
     MSVTSWFLVS SSGTRHRLPR ELIFVGRDEC ELMLQSRSVD KQHAVINYDQ DRDEHWVKDL
     GSLNGTFVND VRIPDQKYIT LKLNDVIRFG YDSNMYVLER VQHRVPEEAL KHEKYTSQLQ
     VSVKVSAPKR GDALPDHTPY CESSQPRPEK GDRRHGAEAV AYRTPLYGQP SWWGEDDSGA
     PSEDRHQEEP YSERPKDLAQ QNGELDSCRA PAEPPDYSFR REPSYFEIPT KETPQPPRLP
     EVPTQEVPTK DQEAGVGGTA PVVQSHASFT IEFDDCSPGK VKIKDHITKF SLRQRRAPSK
     ETTPVETVSA ETKVADWLVQ NDPSLLRRDG PGDDRHSTKS DLPVHTRTLK GHKHEDGTQS
     DSEDPLAKTA SVSGASAEAS GEQVRLQRQI KRDPQELLHN QQAFVIEFFD GDTPRKKRSQ
     SFTHTPPADP KADKRRGPGT SDRDRPGVSV RATGSSSGPQ RASSLKREKT EERLGNTSPV
     PRASTRSFGS VGRRSRLAQD FMAQCMRDSS PATRPAPEKT PPVLPAPLTP RGASPVTPST
     TPPPPTDPQL TKARKQEEDD SLSDAGTYTI ETEAQDQEVE EARRMIDQVF GVFESPELSR
     VSSATFRPVI RGDKDESSDG GMAQRMALLQ EFASRAPGMA PQMEQQSLLV PGSPGGQKWV
     SRWASLADSY SDAGLPEDGP GRRTGEPEGP LPVRTRRLLP QLPSGRADSP AGLEAARRNG
     PGPPELGSEP ANCLIGQEDL DPDSLSDASG SDGGRGPEPG TERQEDLAWV RGRRSPRAPG
     ELVPTSFFIG DQNGEATFPK KSFVGPGEVD GPGRVVQTSP SARDGLYVSS NGRMVIQLRS
     GRSPEPDPAP PKETLTFARQ ESFTKEPTSG PPAPGKLPHI SSHPLLQDLA AARASRLDFH
     AQDTHLILKE TETALAALEA RLRSKSADEC DGGSTPRPPE DSLSGDSDVD TASTISLLSG
     KNGPSPTTPQ TPGPQKESPL SPPTVPDPGG ATPGSARERM SERQHRPTPA DLGPGDTSRR
     AAMRRGHGSR GSLDWPEEER GSGLAHLPSS NHETPEATLA GRQGPRRKPA APPPSPAARE
     EQSRSSATAQ KVQQALTRSN SLSTPRPTRA SRLRRARLGD ASDTEAVDGE RGTAANPEPA
     NRAAPEQAKK LTRLDILAMP RKRAGSFTGP SDSETAPART GFSGRSAELY STSRKPTIAE
     ARAAAKKAAA TAANTGPRQP FSRARPGSAR YSSNTRRRQQ GSDYTSTSEE EYGSHHSSPK
     HTRSHASTAT QTPRGSSSTR ARSQGPRDTD DDEEEPDPYG FIVQTAEIAE IARLSQTLVK
     DVAILAREIH DVAGDGDSLG SPGPTRSPSL GNVPNTPAST ISAREELVQR IPEASLNFQK
     VPPGSMNSHN LDQNMNDSRD DALTNKTRPR NREEVIFDNL MLNPVSQLSH AIRENTEHLA
     EKMKVLFQNT GRAWEDLEAR INSENEVPIL KTSNKEISSI LKELRRVQKQ LEVINAIVDP
     SLNLDLLMGN RAPSGSGQPG LGKARPAAQS STSPASVDTL LPALPLRSFP QRANCGPPGL
     PEPAFLPDAE RFLI
//
ID   AVL9_MOUSE              Reviewed;         649 AA.
AC   Q80U56; Q149B3;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=Late secretory pathway protein AVL9 homolog;
GN   Name=Avl9; Synonyms=Kiaa0241;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the AVL9 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65510.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK122228; BAC65510.1; ALT_INIT; mRNA.
DR   EMBL; BC117878; AAI17879.1; -; mRNA.
DR   IPI; IPI00929806; -.
DR   RefSeq; NP_084511.1; NM_030235.1.
DR   UniGene; Mm.105343; -.
DR   PhosphoSite; Q80U56; -.
DR   PRIDE; Q80U56; -.
DR   Ensembl; ENSMUST00000031805; ENSMUSP00000031805; ENSMUSG00000029787.
DR   GeneID; 78937; -.
DR   KEGG; mmu:78937; -.
DR   UCSC; uc009cbl.1; mouse.
DR   CTD; 78937; -.
DR   MGI; MGI:1926187; Avl9.
DR   GeneTree; ENSGT00390000010255; -.
DR   HOGENOM; HBG443812; -.
DR   HOVERGEN; HBG072150; -.
DR   InParanoid; Q80U56; -.
DR   OMA; TVYGVSC; -.
DR   OrthoDB; EOG4ZS92Q; -.
DR   PhylomeDB; Q80U56; -.
DR   ArrayExpress; Q80U56; -.
DR   Bgee; Q80U56; -.
DR   Genevestigator; Q80U56; -.
DR   GermOnline; ENSMUSG00000029787; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR018307; Secretory_pathway_prot_Avl9.
DR   Pfam; PF09794; Avl9; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    649       Late secretory pathway protein AVL9
FT                                homolog.
FT                                /FTId=PRO_0000247179.
FT   TRANSMEM    204    229       Helical; (Potential).
SQ   SEQUENCE   649 AA;  72186 MW;  B95EC289580D610F CRC64;
     MEKSGRESDG APCGPVLHIV VVGFHHKKGC QVEFSYPPLI PGDGHDSHTL PEEWKYLPFL
     ALPDGAHNYQ EDTVFFHLPP RNGNGATVYG ISCYRQIEAK ALKVRQADIT RETVQKSVCV
     LSKLPLYGLL QAKLQLITHA YFEEKDFSQI SILKELYEHM NSSLGGASLE GSQVYLGLSP
     RDLVLHFRHK VLILFKLILL EKKVLFYISP VNRLVGALMT VLSLFPGMIE HGLSDCSQYR
     PRKSMSEDAG PQESNPSADD FTSESTSDVL NTSLETVTRV MAVNHGEDAV PKTEKPYFQV
     EGNNNKGQEP SDSGRYLELP PRPSPESSES DWETLDPSVL EDASLKEREQ MGSDQTHLFQ
     KDSLPSDSPP ITVQPQANNR QVVLIPGLIS GLEEDQYGMP LAIFTKGYLC LPYMALQQHH
     LLSDVTVRGF VAGATNILFR QQKHLSDAIV EVEEALIQIH DPELRKLLNP TTADLRFADY
     LVRHVTENRD DVFLDGTGWE GGDEWIRAQF AVYIHALLAA TLQLDNEKML SDYGTTFVAA
     WKNTHNYRVW NSNKHPALSE INPNHPFQGQ YSVSDMKLRF SHSVQNSERG KKIGSVMVTT
     SRNVVQTGKA VGQSVGGAFS SAKTAMSSWL STFTTSTPQS LPEPPNGKP
//
ID   RIMS3_MOUSE             Reviewed;         307 AA.
AC   Q80U57;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 2.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Regulating synaptic membrane exocytosis protein 3;
DE            Short=Nim3;
DE   AltName: Full=RIM3 gamma;
DE   AltName: Full=Rab-3-interacting molecule 3;
DE            Short=RIM 3;
GN   Name=Rims3; Synonyms=Kiaa0237;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=22508184; PubMed=12620390; DOI=10.1016/S0888-7543(02)00024-1;
RA   Wang Y., Suedhof T.C.;
RT   "Genomic definition of RIM proteins: evolutionary amplification of a
RT   family of synaptic regulatory proteins.";
RL   Genomics 81:126-137(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 45-307.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Regulates synaptic membrane exocytosis (By similarity).
CC   -!- SUBUNIT: Binds PPFIA3 (By similarity). Does not bind RAB3.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 C2 domain.
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DR   EMBL; AY326953; AAQ01680.1; -; mRNA.
DR   EMBL; AK122226; BAC65508.2; -; mRNA.
DR   IPI; IPI00330250; -.
DR   RefSeq; NP_891559.1; NM_182929.2.
DR   UniGene; Mm.479706; -.
DR   ProteinModelPortal; Q80U57; -.
DR   SMR; Q80U57; 141-287.
DR   STRING; Q80U57; -.
DR   PhosphoSite; Q80U57; -.
DR   PRIDE; Q80U57; -.
DR   Ensembl; ENSMUST00000071093; ENSMUSP00000068178; ENSMUSG00000032890.
DR   Ensembl; ENSMUST00000106283; ENSMUSP00000101890; ENSMUSG00000032890.
DR   GeneID; 242662; -.
DR   KEGG; mmu:242662; -.
DR   UCSC; uc008unr.1; mouse.
DR   CTD; 242662; -.
DR   MGI; MGI:2443331; Rims3.
DR   GeneTree; ENSGT00550000074588; -.
DR   HOGENOM; HBG444874; -.
DR   HOVERGEN; HBG056381; -.
DR   InParanoid; Q80U57; -.
DR   OMA; IPATYVK; -.
DR   OrthoDB; EOG45X7WP; -.
DR   PhylomeDB; Q80U57; -.
DR   NextBio; 385476; -.
DR   ArrayExpress; Q80U57; -.
DR   Bgee; Q80U57; -.
DR   CleanEx; MM_RIMS3; -.
DR   Genevestigator; Q80U57; -.
DR   GermOnline; ENSMUSG00000032890; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   Pfam; PF00168; C2; 1.
DR   SMART; SM00239; C2; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   PROSITE; PS50004; C2; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Exocytosis; Neurotransmitter transport; Phosphoprotein;
KW   Synapse; Transport.
FT   CHAIN         1    307       Regulating synaptic membrane exocytosis
FT                                protein 3.
FT                                /FTId=PRO_0000190205.
FT   DOMAIN      155    257       C2.
FT   MOD_RES     244    244       Phosphotyrosine (By similarity).
FT   MOD_RES     294    294       Phosphoserine (By similarity).
FT   MOD_RES     296    296       Phosphoserine.
SQ   SEQUENCE   307 AA;  32589 MW;  FB6D0AAF6A41C704 CRC64;
     MFNGEPGPAS AGASRNVVRS SSISGEICGS QQAGGGAGTT TAKKRRSSLG AKMVAIVGLT
     QWSKSTLQLP QPEGATKKLR SNIRRSTETG IAVEMRSRVT RQGSRESTDG STNSNSSEGT
     FIFPTRLGAE SQFSDFLDGL GPAQIVGRQT LATPPMGDVH IAIMDRSGQL EVEVIEARGL
     TPKPGSKSLP ATYIKAYLLE NGACVAKKKT KVAKKTCDPL YQQALLFDEG PQGKVLQVIV
     WGDYGRMDHK CFMGMAQIML DELDLSAAVT GWYKLFPTSS VADSTLGSLT RRLSQSSLES
     ATSPSCS
//
ID   PUM2_MOUSE              Reviewed;        1066 AA.
AC   Q80U58; Q80UZ9; Q91YW4; Q925A0; Q9ERC7;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   02-FEB-2004, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Pumilio homolog 2;
GN   Name=Pum2; Synonyms=Kiaa0235;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), RNA-BINDING, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=C57BL/6;
RX   PubMed=11780640;
RA   White E.K., Moore-Jarrett T., Ruley H.E.;
RT   "PUM2, a novel murine puf protein, and its consensus RNA-binding
RT   site.";
RL   RNA 7:1855-1866(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J;
RX   PubMed=12667987; DOI=10.1016/S1079-9796(03)00003-2;
RA   Spassov D.S., Jurecic R.;
RT   "Mouse Pum1 and Pum2 genes, members of the Pumilio family of RNA-
RT   binding proteins, show differential expression in fetal and adult
RT   hematopoietic stem cells and progenitors.";
RL   Blood Cells Mol. Dis. 30:55-69(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136 AND SER-587, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Sequence-specific RNA-binding protein that regulates
CC       translation and mRNA stability by binding the 3'-UTR of mRNA
CC       targets. Its interactions and tissue specificity suggest that it
CC       may be required to support proliferation and self-renewal of stem
CC       cells by regulating the translation of key transcripts (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer; homodimerizes in vitro. Interacts with DAZ,
CC       DAZL and NANOS1 via its pumilio repeats (By similarity). Binds to
CC       a RNA consensus sequence, that is related to the Nanos Response
CC       Element (NRE), a 16 bp sequence found in the 3'-UTR of the
CC       Drosophila hb mRNA. Also binds to the NRE.
CC   -!- INTERACTION:
CC       Q9NQZ3:DAZ1 (xeno); NbExp=1; IntAct=EBI-998056, EBI-997955;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q80U58-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80U58-2; Sequence=VSP_009322, VSP_009323;
CC       Name=3;
CC         IsoId=Q80U58-3; Sequence=VSP_009321, VSP_009322, VSP_009323;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed in embryonic stem
CC       cells, heart, kidney, lung, skin, intestine, spleen and thymus.
CC       Expressed at intermediate level in brain and liver. Weakly or not
CC       expressed in muscles and stomach. Expressed at various stages of
CC       myeloid and lymphoid cell development.
CC   -!- DOMAIN: The pumilio repeats mediate the association with RNA by
CC       packing together to form a right-handed superhelix that
CC       approximates a half donut. The number as well as the specific
CC       sequence of the repeats determine the specificity for target mRNAs
CC       (By similarity).
CC   -!- SIMILARITY: Contains 1 PUM-HD domain.
CC   -!- SIMILARITY: Contains 8 pumilio repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65507.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY027917; AAK21966.1; -; mRNA.
DR   EMBL; AF315590; AAG31805.1; -; mRNA.
DR   EMBL; AK122225; BAC65507.1; ALT_INIT; mRNA.
DR   EMBL; BC013765; AAH13765.1; -; mRNA.
DR   EMBL; BC041773; AAH41773.1; -; mRNA.
DR   IPI; IPI00112203; -.
DR   IPI; IPI00400191; -.
DR   IPI; IPI00400192; -.
DR   RefSeq; NP_001153691.1; NM_001160219.1.
DR   RefSeq; NP_001153694.1; NM_001160222.1.
DR   RefSeq; NP_109648.2; NM_030723.2.
DR   UniGene; Mm.341243; -.
DR   PDB; 3GVO; X-ray; 1.60 A; A=706-1056.
DR   PDB; 3GVT; X-ray; 2.80 A; A/B=706-1056.
DR   PDBsum; 3GVO; -.
DR   PDBsum; 3GVT; -.
DR   ProteinModelPortal; Q80U58; -.
DR   SMR; Q80U58; 706-1049.
DR   IntAct; Q80U58; 1.
DR   STRING; Q80U58; -.
DR   PhosphoSite; Q80U58; -.
DR   PRIDE; Q80U58; -.
DR   Ensembl; ENSMUST00000020915; ENSMUSP00000020915; ENSMUSG00000020594.
DR   Ensembl; ENSMUST00000111122; ENSMUSP00000106751; ENSMUSG00000020594.
DR   Ensembl; ENSMUST00000111123; ENSMUSP00000106752; ENSMUSG00000020594.
DR   GeneID; 80913; -.
DR   KEGG; mmu:80913; -.
DR   UCSC; uc007mzw.1; mouse.
DR   UCSC; uc007mzy.1; mouse.
DR   CTD; 80913; -.
DR   MGI; MGI:1931751; Pum2.
DR   GeneTree; ENSGT00390000017241; -.
DR   HOGENOM; HBG445218; -.
DR   HOVERGEN; HBG049462; -.
DR   InParanoid; Q80U58; -.
DR   OMA; LFDYSSQ; -.
DR   OrthoDB; EOG4P8FHP; -.
DR   PhylomeDB; Q80U58; -.
DR   NextBio; 350290; -.
DR   ArrayExpress; Q80U58; -.
DR   Bgee; Q80U58; -.
DR   CleanEx; MM_PUM2; -.
DR   Genevestigator; Q80U58; -.
DR   GermOnline; ENSMUSG00000020594; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003723; F:RNA binding; IDA:MGI.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR001313; Pumilio_RNA-bd_rpt.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF00806; PUF; 8.
DR   SMART; SM00025; Pumilio; 8.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50302; PUM; 8.
DR   PROSITE; PS50303; PUM_HD; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW   Phosphoprotein; Repeat; RNA-binding; Translation regulation.
FT   CHAIN         1   1066       Pumilio homolog 2.
FT                                /FTId=PRO_0000075920.
FT   DOMAIN      706   1048       PUM-HD.
FT   REPEAT      726    761       Pumilio 1.
FT   REPEAT      762    797       Pumilio 2.
FT   REPEAT      798    835       Pumilio 3.
FT   REPEAT      836    871       Pumilio 4.
FT   REPEAT      872    907       Pumilio 5.
FT   REPEAT      908    943       Pumilio 6.
FT   REPEAT      944    979       Pumilio 7.
FT   REPEAT      980   1022       Pumilio 8.
FT   COMPBIAS    277    486       Ala-rich.
FT   COMPBIAS    358    404       Gln-rich.
FT   COMPBIAS    520    687       Ser-rich.
FT   MOD_RES      82     82       Phosphoserine (By similarity).
FT   MOD_RES     136    136       Phosphoserine.
FT   MOD_RES     177    177       Phosphoserine (By similarity).
FT   MOD_RES     181    181       Phosphoserine (By similarity).
FT   MOD_RES     183    183       Phosphothreonine (By similarity).
FT   MOD_RES     587    587       Phosphoserine.
FT   MOD_RES     672    672       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1     56       Missing (in isoform 3).
FT                                /FTId=VSP_009321.
FT   VAR_SEQ     574    652       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_009322.
FT   VAR_SEQ     829    830       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_009323.
FT   CONFLICT    461    461       M -> I (in Ref. 3; BAC65507).
FT   CONFLICT    547    547       G -> A (in Ref. 2; AAG31805).
FT   CONFLICT    553    553       F -> C (in Ref. 2; AAG31805).
FT   CONFLICT    559    560       LG -> VR (in Ref. 2; AAG31805).
FT   CONFLICT    570    570       F -> C (in Ref. 2; AAG31805).
FT   CONFLICT    592    592       S -> A (in Ref. 2; AAG31805).
FT   CONFLICT    628    628       S -> G (in Ref. 2; AAG31805).
FT   HELIX       709    715
FT   HELIX       724    727
FT   HELIX       731    735
FT   HELIX       742    748
FT   HELIX       753    763
FT   HELIX       764    766
FT   HELIX       767    771
FT   HELIX       778    785
FT   HELIX       789    799
FT   HELIX       803    807
FT   HELIX       814    822
FT   HELIX       825    828
FT   HELIX       831    834
FT   HELIX       835    837
FT   HELIX       841    846
FT   HELIX       852    860
FT   HELIX       863    865
FT   HELIX       867    872
FT   HELIX       877    881
FT   HELIX       888    896
FT   HELIX       899    910
FT   HELIX       913    917
FT   HELIX       924    931
FT   HELIX       935    943
FT   HELIX       949    953
FT   HELIX       958    968
FT   HELIX       971    982
FT   HELIX       991    997
FT   HELIX      1001   1011
FT   HELIX      1014   1024
FT   HELIX      1025   1027
FT   HELIX      1028   1031
FT   HELIX      1039   1047
SQ   SEQUENCE   1066 AA;  114314 MW;  027AC00FA91B055E CRC64;
     MNHDFQALAL ESRGMGELLP TKKFWEPDDS TKDGQKGIFL GDDEWRETAW GTSHHSMSQP
     IMVQRRSGQS FHGNSEVNAI LSPRSESGGL GVSMVEYVLS SSPADKLDSR FRKGTFGTRD
     AETDGPEKGD QKGKASPFEE DQNRDLKQDD EDSKINGRGL PNGMDADCKD FNRTPGSRQA
     SPTEVVERLG PSTNPPEGLG PLPNPTANKP LVEEFSNPET QNLDAMDQVG LDSLQFDYPG
     NQVPMDSSGA TVGLFDYNSQ QQLFQRTSAL TVQQLTAAQQ QQYALAAAQQ PHIAGVFSAG
     LAPAAFVPNP YIISAAPPGT DPYTAAGLAA AATLAGPAVV PPQYYGVPWG VYPANLFQQQ
     AAAAASNTAN QQAASQAQPG QQQVLRPGAG QRPITPSQGQ QGQQAESLAA AANPTLAFGQ
     SLAAGMPGYQ VLAPTAYYDQ TGALVVGPGA RTGLGAPVRL MAPTPVLISS TAAQAAAAAA
     AAGGTANSLT GSTNGLFRPI GTQPPQQQQQ QQQPSTNLQS NSFYGSSSLT NSSQSSSLFS
     HGPGQPGSAS LGFGSGSSLG AAIGSALSGF GSSVGSSASS SATRRESLST SSDLYKRSSS
     SLAPIGQPFY NSLGFSSSPS PIGMPLPSQT PGHSLTPPPS LSSHGSSSSL HLGGLTNGSG
     RYISAAPGAE AKYRSASSTS SLFSSSSQLF PPSRLRYNRS DIMPSGRSRL LEDFRNNRFP
     NLQLRDLIGH IVEFSQDQHG SRFIQQKLER ATPAERQIVF NEILQAAYQL MTDVFGNYVI
     QKFFEFGSLD QKLALATRIR GHVLPLALQM YGCRVIQKAL ESISSDQQVI SEMVKELDGH
     VLKCVKDQNG NHVVQKCIEC VQPQSLQFII DAFKGQVFVL STHPYGCRVI QRILEHCTAE
     QTLPILEELH QHTEQLVQDQ YGNYVIQHVL EHGRPEDKSK IVSEIRGKVL ALSQHKFASN
     VVEKCVTHAS RAERALLIDE VCCQNDGPHS ALYTMMKDQY ANYVVQKMID MAEPAQRKII
     MHKIRPHITT LRKYTYGKHI LAKLEKYYLK NSPDLGPIGG PPNGML
//
ID   K0232_MOUSE             Reviewed;        1396 AA.
AC   Q80U59; Q3U6T9; Q3UTK1; Q3UYU6; Q504Z4; Q80XC4; Q8BJI7; Q8BZV3;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   08-FEB-2011, entry version 49.
DE   RecName: Full=Uncharacterized protein KIAA0232;
GN   Name=Kiaa0232; Synonyms=D5Ertd579e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-1276 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Brain cortex, Colon, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 347-1396 (ISOFORM 1).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-1396 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q80U59-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80U59-2; Sequence=VSP_021649, VSP_021650;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q80U59-3; Sequence=VSP_021647, VSP_021648;
CC         Note=No experimental confirmation available;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK033480; BAC28310.2; -; mRNA.
DR   EMBL; AK083736; BAC39009.1; -; mRNA.
DR   EMBL; AK134363; BAE22115.1; -; mRNA.
DR   EMBL; AK139370; BAE23979.1; -; mRNA.
DR   EMBL; AK152987; BAE31635.1; -; mRNA.
DR   EMBL; CAAA01061871; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CAAA01088923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC051182; AAH51182.1; -; mRNA.
DR   EMBL; BC094673; AAH94673.1; -; mRNA.
DR   EMBL; AK122224; BAC65506.1; -; mRNA.
DR   IPI; IPI00281680; -.
DR   IPI; IPI00675293; -.
DR   IPI; IPI00808101; -.
DR   RefSeq; NP_001074701.2; NM_001081232.2.
DR   UniGene; Mm.384483; -.
DR   UniGene; Mm.478818; -.
DR   PRIDE; Q80U59; -.
DR   Ensembl; ENSMUST00000031091; ENSMUSP00000031091; ENSMUSG00000029190.
DR   GeneID; 320661; -.
DR   KEGG; mmu:320661; -.
DR   UCSC; uc008xey.1; mouse.
DR   CTD; 320661; -.
DR   MGI; MGI:1261849; D5Ertd579e.
DR   eggNOG; roNOG07525; -.
DR   GeneTree; ENSGT00390000018549; -.
DR   HOVERGEN; HBG081818; -.
DR   InParanoid; Q80U59; -.
DR   NextBio; 397163; -.
DR   ArrayExpress; Q80U59; -.
DR   Bgee; Q80U59; -.
DR   CleanEx; MM_D5ERTD579E; -.
DR   Genevestigator; Q80U59; -.
DR   GermOnline; ENSMUSG00000029190; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1   1396       Uncharacterized protein KIAA0232.
FT                                /FTId=PRO_0000261138.
FT   NP_BIND      88     95       ATP (Potential).
FT   COMPBIAS    197    299       Ser-rich.
FT   COMPBIAS    352    357       Poly-Ser.
FT   MOD_RES     157    157       Phosphoserine (By similarity).
FT   VAR_SEQ      78     83       ENDILS -> VGIDAC (in isoform 3).
FT                                /FTId=VSP_021647.
FT   VAR_SEQ      84   1396       Missing (in isoform 3).
FT                                /FTId=VSP_021648.
FT   VAR_SEQ     174    204       YEAFPPLSEKPVCLQEIMTVWNKSKPCSYSS -> VRLLSL
FT                                KYVLLKPVSLLPHGFHFCHLYDFLI (in isoform 2).
FT                                /FTId=VSP_021649.
FT   VAR_SEQ     205   1396       Missing (in isoform 2).
FT                                /FTId=VSP_021650.
FT   CONFLICT    107    107       M -> V (in Ref. 1; BAC39009).
FT   CONFLICT    356    356       S -> C (in Ref. 1; BAC28310).
FT   CONFLICT    409    409       I -> F (in Ref. 1; BAE22115).
FT   CONFLICT   1007   1007       R -> S (in Ref. 1; BAE23979 and 3;
FT                                AAH94673).
FT   CONFLICT   1143   1143       H -> Q (in Ref. 1; BAE23979 and 3;
FT                                AAH94673).
SQ   SEQUENCE   1396 AA;  154778 MW;  FEF8C1172D85B0DB CRC64;
     MRPVCTVVVD GLPSESTSSS YPGPVSVSDM SLLHALGPVQ TWLGQELEKC GIDAMIYSRY
     ILSLLLHDSY DYDLQEQEND ILSWEKGAYK KWGRSKKKCS DLTLEEMKKQ AAVQCLRSAS
     DESSGIETLV EELCCRLKDL QSEQEEKIHK KLEGSPSPEE ELSPTAKDQV EMYYEAFPPL
     SEKPVCLQEI MTVWNKSKPC SYSSSSSSST VPPASTDTSS PKDCNSESEA VRERSSVASV
     PMHEKAQSRS RHEKESKLSS STIEEKPAFY KRQIRHKPEG KTRPRSWSSG SSEAGSSSSG
     NQGELKASMK YVKVRHKARE IRNRKGRNGQ NRHSLKHCGK AERGVHAGSG GSSSSSSNGS
     IRQLCKRGKR PAKETGRSDS GNTAVKDLYV DSRNNKEYKE EPLWYTEPIA EYFVPLSRKS
     KLETTYRNRE DTSTLTAEAV EDLSDSVRGL CISNSNIHRT YLAAGTFIDG HFVEMPAVIN
     EDIDLAGTSL CSLPEDNKYL DDIHLSELTH FYEVDIDQSM LDPGASETMQ GESRILNMIR
     QKSKENTDFE AECCIVLDGM ELQGERAIWT DSTSSVGAEG FFLQDLGNLA QFWECCSSSS
     GDADGESFGG DSPVRLSPIL DSTMLSSHIL AGNQEPFSNI NEGSGINSCF SVFEVQCSNS
     VLPFSFETLN LGSEHADSSA NMLGKTQSRL LIWTKNSAFE ENEHCSNLST RTCSPWSHSE
     EARSDNETLN IQFEESTQFT AEDINYVVPR VSSDFVDEEL LDFLQDETCQ QNSRTLGEIP
     TLVFKKRSKL ESVCGIQLEQ KAESKNFETT HACSESSPHG DGYSSGVIKD IWTKMVGRSS
     VAAVETERTG EELFSTDVNN YCCCLDTEAK MEALQEPSRA VQRSEYHLWE GQKENMEKRA
     FVSSELSKVD GGDYTTPSKP WDVAQDKENT FILGGVYGEL KTFNSDGEWA VVPPGHTKGS
     LLQCAASDVV TIAGTDVFMT PGNSFAPGHR QLWKPFVSFE QSDMPKRGEN GVNKGFSFIF
     HEDLLGACSN FQVEDPGLEY SLSSFDLSNP FSQVLHVECS FEPEGIASFS PSFKPKSILC
     SDSDSEVFHP RICGVERTQY RAIRISPRTH FRPISASELS PGGGSESEFE SEKDEASVPI
     PSHVDVFEDP QADLKPLEED AEKEGHYYGK LELESGKFLP RLKKSGMEKS AQTSLDSQEE
     ATGILPKQNQ CLECNFNESL EINLESSAAN CKIMTQCEEE MSEFCSCKAG CQFPACEDNP
     VSSGQLEEFP VLNTDVQEVT RNQEKQSWWE KALYSPLFPT SECEECYTNA KGENGIEECP
     DAKETPSREE RLLDFNRVSS VYEARCTGER GSETKPNGLH RKMCSSASSD TGDTGSEAGG
     EWVGPSREEL FSRTHL
//
ID   MFN2_MOUSE              Reviewed;         757 AA.
AC   Q80U63; A2A7Y7; A8Y5E4; Q3V3B8; Q80WP4; Q80XK3; Q8BHF0; Q8BKV5;
AC   Q8R535; Q923X2;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 3.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Mitofusin-2;
DE            EC=3.6.5.-;
DE   AltName: Full=Hypertension-related protein 1;
DE   AltName: Full=Mitochondrial assembly regulatory factor;
DE            Short=HSG protein;
DE   AltName: Full=Transmembrane GTPase MFN2;
GN   Name=Mfn2; Synonyms=Kiaa0214, Marf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND MULTIMERIZATION.
RC   STRAIN=FVB;
RX   MEDLINE=22426329; PubMed=12527753; DOI=10.1083/jcb.200211046;
RA   Chen H., Detmer S.A., Ewald A.J., Griffin E.E., Fraser S.E.,
RA   Chan D.C.;
RT   "Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion
RT   and are essential for embryonic development.";
RL   J. Cell Biol. 160:189-200(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=22615896; PubMed=12598526; DOI=10.1074/jbc.M212754200;
RA   Bach D., Pich S., Soriano F.X., Vega N., Baumgartner B., Oriola J.,
RA   Daugaard J.R., Lloberas J., Camps M., Zierath J.R., Rabasa-Lhoret R.,
RA   Wallberg-Henriksson H., Laville M., Palacin M., Vidal H., Rivera F.,
RA   Brand M., Zorzano A.;
RT   "Mitofusin-2 determines mitochondrial network architecture and
RT   mitochondrial metabolism. A novel regulatory mechanism altered in
RT   obesity.";
RL   J. Biol. Chem. 278:17190-17197(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Honda S., Hirose S.;
RT   "Characterization of mouse fzo.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=BALB/c;
RX   PubMed=15322553; DOI=10.1038/ncb1161;
RA   Chen K.-H., Guo X., Ma D., Guo Y., Li Q., Yang D., Li P., Qiu X.,
RA   Wen S., Xiao R.-P., Tang J.;
RT   "Dysregulation of HSG triggers vascular proliferative disorders.";
RL   Nat. Cell Biol. 6:872-883(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [6]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   PROTEIN SEQUENCE OF 421-428, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [11]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=21947835; PubMed=11950885;
RA   Rojo M., Legros F., Chateau D., Lombes A.;
RT   "Membrane topology and mitochondrial targeting of mitofusins,
RT   ubiquitous mammalian homologs of the transmembrane GTPase Fzo.";
RL   J. Cell Sci. 115:1663-1674(2002).
CC   -!- FUNCTION: Essential transmembrane GTPase, which mediates
CC       mitochondrial fusion. Fusion of mitochondria occurs in many cell
CC       types and constitutes an important step in mitochondria
CC       morphology, which is balanced between fusion and fission. MFN2
CC       acts independently of the cytoskeleton. It therefore plays a
CC       central role in mitochondrial metabolism and may be associated
CC       with obesity and/or apoptosis processes. Overexpression induces
CC       the formation of mitochondrial networks. Plays an important role
CC       in the regulation of vascular smooth muscle cell proliferation.
CC   -!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate.
CC   -!- SUBUNIT: Forms homomultimers and heteromultimers with MFN2.
CC       Oligomerization, which is probably mediated by the coiled coil
CC       region, may play an essential role in mitochondrion fusion.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass
CC       membrane protein (By similarity). Note=Colocalizes with BAX during
CC       apoptosis (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80U63-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80U63-2; Sequence=VSP_010365, VSP_010366;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Expression is markedly reduced in
CC       ApoE-knockout mouse atherosclerotic arteries.
CC   -!- MISCELLANEOUS: MFN2 deficient mice die early during embryonic
CC       development, due to altered mitochondria morphology, which are
CC       fragmented, showing that mitochondrial fusion is essential for
CC       embryonic development.
CC   -!- SIMILARITY: Belongs to the mitofusin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65502.2; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY123975; AAM88577.1; -; mRNA.
DR   EMBL; AY028170; AAK27416.1; -; mRNA.
DR   EMBL; AB048831; BAB39351.1; -; mRNA.
DR   EMBL; AF384100; AAK66559.1; -; mRNA.
DR   EMBL; AK042080; BAE20620.1; -; mRNA.
DR   EMBL; AK049583; BAC33826.1; -; mRNA.
DR   EMBL; AK052689; BAC35096.1; -; mRNA.
DR   EMBL; AK122220; BAC65502.2; ALT_INIT; Transcribed_RNA.
DR   EMBL; AL607066; CAM23513.1; -; Genomic_DNA.
DR   EMBL; AL607066; CAP19097.1; -; Genomic_DNA.
DR   EMBL; BC046503; AAH46503.1; -; mRNA.
DR   IPI; IPI00312244; -.
DR   IPI; IPI00415517; -.
DR   RefSeq; NP_573464.2; NM_133201.2.
DR   UniGene; Mm.154312; -.
DR   ProteinModelPortal; Q80U63; -.
DR   SMR; Q80U63; 94-132, 693-754.
DR   STRING; Q80U63; -.
DR   PhosphoSite; Q80U63; -.
DR   PRIDE; Q80U63; -.
DR   Ensembl; ENSMUST00000030884; ENSMUSP00000030884; ENSMUSG00000029020.
DR   Ensembl; ENSMUST00000105715; ENSMUSP00000101340; ENSMUSG00000029020.
DR   Ensembl; ENSMUST00000105716; ENSMUSP00000101341; ENSMUSG00000029020.
DR   GeneID; 170731; -.
DR   KEGG; mmu:170731; -.
DR   UCSC; uc008vtg.1; mouse.
DR   UCSC; uc008vtj.1; mouse.
DR   CTD; 170731; -.
DR   MGI; MGI:2442230; Mfn2.
DR   GeneTree; ENSGT00390000013727; -.
DR   HOVERGEN; HBG052465; -.
DR   InParanoid; Q80U63; -.
DR   OMA; QDRLRFI; -.
DR   OrthoDB; EOG43JC43; -.
DR   NextBio; 370262; -.
DR   ArrayExpress; Q80U63; -.
DR   Bgee; Q80U63; -.
DR   CleanEx; MM_MFN2; -.
DR   Genevestigator; Q80U63; -.
DR   GermOnline; ENSMUSG00000029020; Mus musculus.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031306; C:intrinsic to mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0001825; P:blastocyst formation; IMP:MGI.
DR   GO; GO:0048593; P:camera-type eye morphogenesis; IMP:MGI.
DR   GO; GO:0008053; P:mitochondrial fusion; IMP:MGI.
DR   GO; GO:0007006; P:mitochondrial membrane organization; ISS:UniProtKB.
DR   GO; GO:0051646; P:mitochondrion localization; ISS:UniProtKB.
DR   GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; ISS:UniProtKB.
DR   GO; GO:0006626; P:protein targeting to mitochondrion; ISS:UniProtKB.
DR   InterPro; IPR001401; Dynamin_GTPase.
DR   InterPro; IPR006884; Fzo/mitofusin_HR2.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   Pfam; PF04799; Fzo_mitofusin; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Developmental protein;
KW   Direct protein sequencing; GTP-binding; Hydrolase; Membrane;
KW   Mitochondrion; Mitochondrion outer membrane; Nucleotide-binding;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    757       Mitofusin-2.
FT                                /FTId=PRO_0000127676.
FT   TOPO_DOM      1    604       Cytoplasmic (Potential).
FT   TRANSMEM    605    625       Helical; Name=1; (Potential).
FT   TOPO_DOM    626    626       Mitochondrial intermembrane (Potential).
FT   TRANSMEM    627    647       Helical; Name=2; (Potential).
FT   TOPO_DOM    648    757       Cytoplasmic (Potential).
FT   NP_BIND     103    110       GTP (Probable).
FT   NP_BIND     199    203       GTP (Probable).
FT   NP_BIND     258    261       GTP (Probable).
FT   COILED      406    434       Potential.
FT   COILED      696    738       Potential.
FT   MOD_RES     243    243       N6-acetyllysine (By similarity).
FT   VAR_SEQ     573    605       VQRPLPLTPANPSMPPLPQSSLTQEELMVSMVT -> ARSS
FT                                FPWCIMGDHPDTRYGSQSTTAGVLRAEAI (in isoform
FT                                2).
FT                                /FTId=VSP_010365.
FT   VAR_SEQ     606    757       Missing (in isoform 2).
FT                                /FTId=VSP_010366.
FT   CONFLICT    123    123       P -> L (in Ref. 9; AAH46503).
FT   CONFLICT    167    167       L -> I (in Ref. 7; BAC33826).
FT   CONFLICT    332    332       Q -> K (in Ref. 2; AAK27416).
FT   CONFLICT    344    344       Q -> R (in Ref. 3 and 4).
FT   CONFLICT    437    437       E -> G (in Ref. 3; BAB39351).
FT   CONFLICT    570    570       S -> N (in Ref. 2; AAK27416).
FT   CONFLICT    592    592       S -> G (in Ref. 2; AAK27416).
FT   CONFLICT    601    601       V -> G (in Ref. 2; AAK27416).
FT   CONFLICT    633    635       LIA -> IIP (in Ref. 2; AAK27416).
FT   CONFLICT    656    656       A -> T (in Ref. 2; AAK27416).
FT   CONFLICT    659    659       R -> K (in Ref. 2; AAK27416).
FT   CONFLICT    666    666       V -> A (in Ref. 4; AAK66559).
FT   CONFLICT    667    667       E -> D (in Ref. 3; BAB39351).
FT   CONFLICT    676    676       I -> T (in Ref. 3; BAB39351).
FT   CONFLICT    697    697       A -> G (in Ref. 2; AAK27416).
FT   CONFLICT    730    730       R -> K (in Ref. 2; AAK27416).
SQ   SEQUENCE   757 AA;  86188 MW;  25B0EAE8301F4D1A CRC64;
     MSLLFSRCNS IVTVKKDKRH MAEVNASPLK HFVTAKKKIN GIFEQLGAYI QESASFLEDT
     HRNTELDPVT TEEQVLDVKG YLSKVRGISE VLARRHMKVA FFGRTSNGKS TVINAMLWDK
     VLPSGIGHTT NCFLRVGGTD GHEAFLLTEG SEEKKSVKTV NQLAHALHQD EQLHAGSMVS
     VMWPNSKCPL LKDDLVLMDS PGIDVTTELD SWIDKFCLDA DVFVLVANSE STLMQTEKQF
     FHKVSERLSR PNIFILNNRW DASASEPEYM EEVRRQHMER CTSFLVDELG VVDRAQAGDR
     IFFVSAKEVL SARVQKAQGM PEGGGALAEG FQVRMFEFQN FERQFEECIS QSAVKTKFEQ
     HTVRAKQIAE AVRLIMDSLH IAAQEQRVYC LEMREERQDR LRFIDKQLEL LAQDYKLRIK
     QITEEVERQV STAMAEEIRR LSVLVDEYQM DFHPSPVVLK VYKNELHRHI EEGLGRNLSD
     RCSTAIASSL QTMQQDMIDG LKPLLPVSMR NQIDMLVPRQ CFSLSYDLNC DKLCADFQED
     IEFHFSLGWT MLVNRFLGPK NSRRALLGYS DQVQRPLPLT PANPSMPPLP QSSLTQEELM
     VSMVTGLASL TSRTSMGILV VGGVVWKAVG WRLIALSFGL YGLLYVYERL TWTTKAKERA
     FKRQFVEYAS EKLQLIISYT GSNCSHQVQQ ELSGTFAHLC QQVDITRDNL EQEIAAMNKK
     VEALDSLQSR AKLLRNKAGW LDSELNMFTH QYLQPSR
//
ID   SCRIB_MOUSE             Reviewed;        1612 AA.
AC   Q80U72; Q6P5H7; Q7TPH8; Q80VB1; Q8CI48; Q8VII1; Q922S3;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Protein scribble homolog;
DE            Short=Scribble;
DE   AltName: Full=Protein LAP4;
GN   Name=Scrib; Synonyms=Kiaa0147, Lap4, Scrib1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Cerebellum;
RA   Mattock K.L., Kurschner C.;
RT   "Molecular cloning of mouse Scribble cDNA.";
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 694-1336 (ISOFORM 1).
RX   PubMed=15649318; DOI=10.1186/1471-2121-6-1;
RA   Petit M.M.R., Meulemans S.M.P., Alen P., Ayoubi T.A.Y., Jansen E.,
RA   Van de Ven W.J.M.;
RT   "The tumor suppressor Scrib interacts with the zyxin-related protein
RT   LPP, which shuttles between cell adhesion sites and the nucleus.";
RL   BMC Cell Biol. 6:1-1(2005).
RN   [5]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=12499390; DOI=10.1093/hmg/ddg014;
RA   Murdoch J.N., Henderson D.J., Doudney K., Gaston-Massuet C.,
RA   Phillips H.M., Paternotte C., Arkell R., Stanier P., Copp A.J.;
RT   "Disruption of scribble (Scrb1) causes severe neural tube defects in
RT   the circletail mouse.";
RL   Hum. Mol. Genet. 12:87-98(2003).
RN   [6]
RP   INTERACTION WITH ARHGEF7 AND GIT1.
RX   PubMed=15182672; DOI=10.1016/j.cub.2004.05.051;
RA   Audebert S., Navarro C., Nourry C., Chasserot-Golaz S., Lecine P.,
RA   Bellaiche Y., Dupont J.-L., Premont R.T., Sempere C., Strub J.-M.,
RA   Van Dorsselaer A., Vitale N., Borg J.-P.;
RT   "Mammalian Scribble forms a tight complex with the betaPIX exchange
RT   factor.";
RL   Curr. Biol. 14:987-995(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1548, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=15806148; DOI=10.1038/sj.onc.1208632;
RA   Navarro C., Nola S., Audebert S., Santoni M.-J., Arsanto J.-P.,
RA   Ginestier C., Marchetto S., Jacquemier J., Isnardon D., Le Bivic A.,
RA   Birnbaum D., Borg J.-P.;
RT   "Junctional recruitment of mammalian Scribble relies on E-cadherin
RT   engagement.";
RL   Oncogene 24:4330-4339(2005).
RN   [9]
RP   INTERACTION WITH APC AND CTNNB1, AND SUBCELLULAR LOCATION.
RX   PubMed=16611247; DOI=10.1111/j.1365-2443.2006.00954.x;
RA   Takizawa S., Nagasaka K., Nakagawa S., Yano T., Nakagawa K.,
RA   Yasugi T., Takeuchi T., Kanda T., Huibregtse J.M., Akiyama T.,
RA   Taketani Y.;
RT   "Human scribble, a novel tumor suppressor identified as a target of
RT   high-risk HPV E6 for ubiquitin-mediated degradation, interacts with
RT   adenomatous polyposis coli.";
RL   Genes Cells 11:453-464(2006).
RN   [10]
RP   INTERACTION WITH VANGL2.
RX   PubMed=16687519; DOI=10.1523/JNEUROSCI.4680-05.2006;
RA   Montcouquiol M., Sans N., Huss D., Kach J., Dickman J.D., Forge A.,
RA   Rachel R.A., Copeland N.G., Jenkins N.A., Bogani D., Murdoch J.,
RA   Warchol M.E., Wenthold R.J., Kelley M.W.;
RT   "Asymmetric localization of Vangl2 and Fz3 indicate novel mechanisms
RT   for planar cell polarity in mammals.";
RL   J. Neurosci. 26:5265-5275(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-674; THR-675 AND
RP   SER-1206, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [13]
RP   FUNCTION.
RX   PubMed=19041750; DOI=10.1016/j.cell.2008.09.045;
RA   Zhan L., Rosenberg A., Bergami K.C., Yu M., Xuan Z., Jaffe A.B.,
RA   Allred C., Muthuswamy S.K.;
RT   "Deregulation of scribble promotes mammary tumorigenesis and reveals a
RT   role for cell polarity in carcinoma.";
RL   Cell 135:865-878(2008).
RN   [14]
RP   FUNCTION IN CELL MIGRATION, AND INTERACTION WITH PAK1 AND PAK2.
RX   PubMed=18716323; DOI=10.1093/hmg/ddn248;
RA   Nola S., Sebbagh M., Marchetto S., Osmani N., Nourry C., Audebert S.,
RA   Navarro C., Rachel R., Montcouquiol M., Sans N.,
RA   Etienne-Manneville S., Borg J.-P., Santoni M.-J.;
RT   "Scrib regulates PAK activity during the cell migration process.";
RL   Hum. Mol. Genet. 17:3552-3565(2008).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1361, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1206; SER-1457 AND
RP   SER-1548, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [17]
RP   FUNCTION, AND INTERACTION WITH CTNNB1.
RX   PubMed=19458197; DOI=10.1091/mbc.E08-12-1172;
RA   Sun Y., Aiga M., Yoshida E., Humbert P.O., Bamji S.X.;
RT   "Scribble interacts with beta-catenin to localize synaptic vesicles to
RT   synapses.";
RL   Mol. Biol. Cell 20:3390-3400(2009).
CC   -!- FUNCTION: Scaffold protein involved in different aspects of
CC       polarized cells differentiation regulating epithelial and neuronal
CC       morphogenesis. Most probably functions in the establishment of
CC       apico-basal cell polarity. May function in cell proliferation
CC       regulating progression from G1 to S phase and as a positive
CC       regulator of apoptosis for instance during acinar morphogenesis of
CC       the mammary epithelium. May also function in cell migration and
CC       adhesion and hence regulate cell invasion through MAPK signaling.
CC       May play a role in exocytosis and in the targeting synaptic
CC       vesicles to synapses. Functions as an activator of Rac GTPase
CC       activity.
CC   -!- SUBUNIT: Interacts with UBE3A. Interacts with PAK1 and PAK2.
CC       Interacts (via PDZ domains) with LPP and TRIP6; the interaction is
CC       direct. Interacts (via PDZ domains) with TJP2. Interacts (via PDZ
CC       domains) with TSHR; regulates TSHR trafficking and function (By
CC       similarity). Interacts (via PDZ domains) with VANGL2. Interacts
CC       with ARHGEF7 and GIT1; interacts directly with ARHGEF7. Interacts
CC       (via PDZ domains) with APC; may mediate APC targeting to adherens
CC       junctions of epithelial cells. Interacts with CTNNB1. Interacts
CC       with MCC (By similarity).
CC   -!- INTERACTION:
CC       Q149L7:Crtam; NbExp=2; IntAct=EBI-1766028, EBI-1766072;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       (By similarity). Cell junction, adherens junction (By similarity).
CC       Cytoplasm (By similarity). Note=Targeting to cell-cell junctions
CC       which is CDH1-dependent is required for the pro-apoptotic
CC       activity. Localizes to neuronal post- and pre-synaptic regions (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q80U72-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80U72-2; Sequence=VSP_010911;
CC       Name=3;
CC         IsoId=Q80U72-3; Sequence=VSP_010910, VSP_010911;
CC       Name=4;
CC         IsoId=Q80U72-4; Sequence=VSP_010909, VSP_010910;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Found in a wide range of tissues including
CC       liver, brain, kidney and spleen.
CC   -!- DEVELOPMENTAL STAGE: First detected at E7.5 in the neuroepithelium
CC       at the time of initial neural tube closure. Also expressed in
CC       cranial mesenchyme, branchial arches, somitic mesoderm and lateral
CC       mesoderm. At later stages it is expressed in the eyelid
CC       epithelium, submandibular glands, whisker and hair follicles,
CC       sympathetic glanglia, inner ear, thymus, testis, kidney,
CC       esophagus, lung, stomach, trigeminal and dorsal root glanglia.
CC   -!- PTM: Ubiquitinated; targeted for UBE3A-dependent
CC       multiubiquitination and degraded (By similarity).
CC   -!- MISCELLANEOUS: The circletail (Crc) mice exhibit
CC       craniorachishicisis a severe form of neural tube defect. This is
CC       due to a single base insertion in the Scrib gene creating a
CC       frameshift which leads to synthesis of a truncated protein.
CC   -!- SIMILARITY: Belongs to the LAP (LRR and PDZ) protein family.
CC   -!- SIMILARITY: Contains 16 LRR (leucine-rich) repeats.
CC   -!- SIMILARITY: Contains 4 PDZ (DHR) domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65493.1; Type=Erroneous initiation;
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DR   EMBL; AF441233; AAL32469.1; -; mRNA.
DR   EMBL; AK122211; BAC65493.1; ALT_INIT; mRNA.
DR   EMBL; BC006859; AAH06859.1; -; mRNA.
DR   EMBL; BC037480; AAH37480.1; -; mRNA.
DR   EMBL; BC049942; AAH49942.1; -; mRNA.
DR   EMBL; BC062888; AAH62888.1; -; mRNA.
DR   EMBL; AF271735; AAP88019.1; -; mRNA.
DR   IPI; IPI00129388; -.
DR   IPI; IPI00454104; -.
DR   IPI; IPI00454106; -.
DR   IPI; IPI00474285; -.
DR   RefSeq; NP_598850.1; NM_134089.1.
DR   UniGene; Mm.25568; -.
DR   ProteinModelPortal; Q80U72; -.
DR   SMR; Q80U72; 8-396, 704-1185.
DR   IntAct; Q80U72; 9.
DR   STRING; Q80U72; -.
DR   PhosphoSite; Q80U72; -.
DR   PRIDE; Q80U72; -.
DR   Ensembl; ENSMUST00000002603; ENSMUSP00000002603; ENSMUSG00000022568.
DR   Ensembl; ENSMUST00000063747; ENSMUSP00000068056; ENSMUSG00000022568.
DR   Ensembl; ENSMUST00000109945; ENSMUSP00000105571; ENSMUSG00000022568.
DR   Ensembl; ENSMUST00000109946; ENSMUSP00000105572; ENSMUSG00000022568.
DR   GeneID; 105782; -.
DR   KEGG; mmu:105782; -.
DR   UCSC; uc007wig.1; mouse.
DR   UCSC; uc007wih.1; mouse.
DR   UCSC; uc007wii.1; mouse.
DR   CTD; 105782; -.
DR   MGI; MGI:2145950; Scrib.
DR   eggNOG; roNOG06605; -.
DR   GeneTree; ENSGT00600000084222; -.
DR   OMA; RRNEAYT; -.
DR   OrthoDB; EOG44BB1C; -.
DR   PhylomeDB; Q80U72; -.
DR   NextBio; 357886; -.
DR   ArrayExpress; Q80U72; -.
DR   Bgee; Q80U72; -.
DR   CleanEx; MM_SCRIB; -.
DR   Genevestigator; Q80U72; -.
DR   GermOnline; ENSMUSG00000022568; Mus musculus.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0005913; C:cell-cell adherens junction; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0032863; P:activation of Rac GTPase activity; ISS:UniProtKB.
DR   GO; GO:0060561; P:apoptosis involved in morphogenesis; ISS:UniProtKB.
DR   GO; GO:0008105; P:asymmetric protein localization; IMP:MGI.
DR   GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR   GO; GO:0008283; P:cell proliferation; ISS:UniProtKB.
DR   GO; GO:0016337; P:cell-cell adhesion; ISS:UniProtKB.
DR   GO; GO:0035089; P:establishment of apical/basal cell polarity; ISS:UniProtKB.
DR   GO; GO:0060603; P:mammary gland duct morphogenesis; IMP:UniProtKB.
DR   GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR   GO; GO:0050918; P:positive chemotaxis; IMP:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptosis; ISS:UniProtKB.
DR   GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:UniProtKB.
DR   GO; GO:0016080; P:synaptic vesicle targeting; IMP:UniProtKB.
DR   GO; GO:0042060; P:wound healing; IGI:MGI.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF00560; LRR_1; 2.
DR   Pfam; PF00595; PDZ; 4.
DR   SMART; SM00369; LRR_TYP; 2.
DR   SMART; SM00228; PDZ; 4.
DR   SUPFAM; SSF50156; PDZ; 4.
DR   PROSITE; PS51450; LRR; 13.
DR   PROSITE; PS50106; PDZ; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Coiled coil;
KW   Cytoplasm; Developmental protein; Differentiation;
KW   Leucine-rich repeat; Membrane; Phosphoprotein; Repeat;
KW   Ubl conjugation.
FT   CHAIN         1   1612       Protein scribble homolog.
FT                                /FTId=PRO_0000188304.
FT   REPEAT       11     34       LRR 1.
FT   REPEAT       35     57       LRR 2.
FT   REPEAT       58     81       LRR 3.
FT   REPEAT       83    105       LRR 4.
FT   REPEAT      107    126       LRR 5.
FT   REPEAT      127    149       LRR 6.
FT   REPEAT      150    172       LRR 7.
FT   REPEAT      173    195       LRR 8.
FT   REPEAT      196    219       LRR 9.
FT   REPEAT      221    241       LRR 10.
FT   REPEAT      242    265       LRR 11.
FT   REPEAT      267    287       LRR 12.
FT   REPEAT      288    310       LRR 13.
FT   REPEAT      311    334       LRR 14.
FT   REPEAT      336    357       LRR 15.
FT   REPEAT      359    380       LRR 16.
FT   DOMAIN      714    801       PDZ 1.
FT   DOMAIN      848    936       PDZ 2.
FT   DOMAIN      990   1079       PDZ 3.
FT   DOMAIN     1086   1180       PDZ 4.
FT   REGION        1    804       Sufficient for targeting to adherens
FT                                junction and to inhibit cell
FT                                proliferation (By similarity).
FT   REGION      703   1215       Interaction with ARHGEF7 (By similarity).
FT   COILED      455    475       Potential.
FT   COILED      653    687       Potential.
FT   COILED     1362   1393       Potential.
FT   COMPBIAS    656    682       Glu-rich.
FT   COMPBIAS    656    664       Poly-Glu.
FT   COMPBIAS    709    712       Poly-Glu.
FT   COMPBIAS   1079   1082       Poly-Pro.
FT   MOD_RES      35     35       Phosphoserine (By similarity).
FT   MOD_RES     583    583       Phosphoserine.
FT   MOD_RES     674    674       Phosphothreonine.
FT   MOD_RES     675    675       Phosphothreonine.
FT   MOD_RES     735    735       Phosphothreonine (By similarity).
FT   MOD_RES     812    812       Phosphothreonine (By similarity).
FT   MOD_RES     820    820       Phosphotyrosine (By similarity).
FT   MOD_RES     821    821       Phosphoserine (By similarity).
FT   MOD_RES     861    861       Phosphoserine (By similarity).
FT   MOD_RES     925    925       Phosphoserine (By similarity).
FT   MOD_RES     927    927       Phosphothreonine (By similarity).
FT   MOD_RES    1126   1126       Phosphoserine (By similarity).
FT   MOD_RES    1206   1206       Phosphoserine.
FT   MOD_RES    1209   1209       Phosphoserine (By similarity).
FT   MOD_RES    1211   1211       Phosphoserine (By similarity).
FT   MOD_RES    1212   1212       Phosphoserine (By similarity).
FT   MOD_RES    1218   1218       Phosphoserine (By similarity).
FT   MOD_RES    1284   1284       Phosphoserine (By similarity).
FT   MOD_RES    1292   1292       Phosphoserine (By similarity).
FT   MOD_RES    1325   1325       Phosphothreonine (By similarity).
FT   MOD_RES    1331   1331       Phosphoserine (By similarity).
FT   MOD_RES    1343   1343       Phosphotyrosine (By similarity).
FT   MOD_RES    1361   1361       Phosphoserine.
FT   MOD_RES    1421   1421       Phosphoserine (By similarity).
FT   MOD_RES    1430   1430       Phosphoserine (By similarity).
FT   MOD_RES    1457   1457       Phosphoserine.
FT   MOD_RES    1468   1468       Phosphoserine (By similarity).
FT   MOD_RES    1490   1490       Phosphoserine (By similarity).
FT   MOD_RES    1529   1529       Phosphoserine (By similarity).
FT   MOD_RES    1543   1543       Phosphoserine (By similarity).
FT   MOD_RES    1548   1548       Phosphoserine.
FT   VAR_SEQ     692    712       Missing (in isoform 4).
FT                                /FTId=VSP_010909.
FT   VAR_SEQ    1289   1289       Q -> QTKPGVIQPLAQAWPRNSPAPRGRGGPCS (in
FT                                isoform 3 and isoform 4).
FT                                /FTId=VSP_010910.
FT   VAR_SEQ    1547   1547       L -> LPLSGKKFDYRAFAALPSSRPVYDIQ (in
FT                                isoform 2 and isoform 3).
FT                                /FTId=VSP_010911.
FT   CONFLICT    588    588       P -> L (in Ref. 3; AAH62888).
FT   CONFLICT    676    683       EEDDKEEA -> GRVGGRVG (in Ref. 3;
FT                                AAH06859).
FT   CONFLICT    947    949       HSS -> RVR (in Ref. 3; AAH37480).
FT   CONFLICT   1080   1080       P -> H (in Ref. 4; AAP88019).
FT   CONFLICT   1109   1109       A -> T (in Ref. 4; AAP88019).
SQ   SEQUENCE   1612 AA;  174059 MW;  8C85DB322D738EDE CRC64;
     MLKCIPLWRC NRHVESVDKR HCSLQVVPEE IYRYSRSLEE LLLDANQLRE LPKPFFRLLN
     LRKLGLSDNE IQRLPPEVAN FMQLVELDVS RNDIPEIPES IKFCKALEIA DFSGNPLSRL
     PDGFTQLRSL AHLALNDVSL QALPGDVGNL ANLVTLELRE NLLKSLPASL SFLVKLEQLD
     LGGNDLEVLP DTLGALPNLR ELWLDRNQLS ALPPELGNLR RLVCLDVSEN RLEELPVELG
     GLALLTDLLL SQNLLQRLPE GIGQLKQLSI LKVDQNRLCE VTEAIGDCEN LSELILTENL
     LTALPHSLGK LTKLTNLNVD RNHLEVLPPE IGGCVALSVL SLRDNRLAVL PPELAHTAEL
     HVLDVAGNRL RSLPFALTHL NLKALWLAEN QAQPMLRFQT EDDAQTGEKV LTCYLLPQQP
     LPSLEDAGQQ SSPSESCSDA PLSRVSVIQF EDTLEGEEDA EEAAAEKRGL QRRATPHPSE
     LKVMKRGIEE RRNEAFVCKP DPSPPSPSEE EKRLSAESAL SGGSVPSAST ASEGEPEILP
     AEVQGLGQHE AMPAQEEYTE DDYNEPTVHF AEDTLIPRED GESEEGQPEA AWPLPSGRQR
     LIRKDTPHYK KHFKISKLPQ PEAVVALLQG VQTDREGPTA GWHNGPHTPW APRAHEEEEE
     EEEENRDEEE GEATTEEDDK EEAVASAPSV KGVSFDQANN LLIEPARIEE EELTLTIVRQ
     TGGLGISIAG GKGSTPYKGD DEGIFISRVS EEGPAARAGV RVGDKLLEVN GVALQDAEHH
     EAVEALRGAG AAVQMRVWRE RMVEPENAVT ITPLRPEDDY SPREWRGGGL RLPLLQPETP
     VSLRQRHAAC LVRSEKGLGF SIAGGKGSTP YRAGDGGIFI SRIAEGGAAH RAGTLQVGDR
     VLSINGVDMT EARHDHAVSL LTAASPTISL LLERETGGTY PPSPPPHSSP TPAATVAATV
     STAVPGEPLL PRLSPSLLAT ALEGPYPVEE ICLPRAGGPL GLSIVGGSDH SSHPFGVQDP
     GVFISKVLPR GLAARCGLRV GDRILAVNGQ DVREATHQEA VSALLRPCLE LCLLVRRDPP
     PPGMRELCIQ KAPGEKLGIS IRGGAKGHAG NPCDPTDEGI FISKVSPTGA AGRDGRLRVG
     LRLLEVNQQS LLGLTHAEAV QLLRSVGDTL TVLVCDGFDT STTTALEVSP GVIANPFAAG
     LGHRNSLESI SSIDRELSPE GPGKEKELAS QALPWESESA ETTGRNLEPL KLDYRALAAL
     PSAGSLQRGP SATTGGKTTE APCSPGSQQP PSPDELPANV KQAYRAFAAV PTVHPPENSA
     TQPPTPGPAA SPEQLSFRER QKYFELEVRV PQAEGPPKRV SLVGADDLRK MQEEEARKLQ
     QKRAQMLREE AVTSGPDMGL ASDRESPDDQ QEAEQPWAVP SHAGGSSPSS PPPLGGNAPV
     RTAKAERRHQ ERLRMQSPEL PAPERALSPA ERRALEAEKR ALWRAARMKS LEQDALRAQM
     VLSKSQEGRG KRGPLERLAE APSPAPTPSP TPLEDFGLQT SASPGRLSPD FVEELRTLEA
     SPSPGSQEED GEVALVLLGR PSPGAVGPED MTLCSSRRSV RPGRRGLGPV PS
//
ID   PUM1_MOUSE              Reviewed;        1189 AA.
AC   Q80U78; Q80X96; Q80YU8; Q8BPV7; Q9EPU6;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   02-FEB-2004, sequence version 2.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Pumilio homolog 1;
GN   Name=Pum1; Synonyms=Kiaa0099;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J;
RX   PubMed=12667987; DOI=10.1016/S1079-9796(03)00003-2;
RA   Spassov D.S., Jurecic R.;
RT   "Mouse Pum1 and Pum2 genes, members of the Pumilio family of RNA-
RT   binding proteins, show differential expression in fetal and adult
RT   hematopoietic stem cells and progenitors.";
RL   Blood Cells Mol. Dis. 30:55-69(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-710, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Sequence-specific RNA-binding protein that regulates
CC       translation and mRNA stability by binding the 3'-UTR of mRNA
CC       targets. May be required to support proliferation and self-renewal
CC       of stem cells (By similarity).
CC   -!- SUBUNIT: Binds in a sequence-specific manner to the 3'-UTR of some
CC       mRNAs.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q80U78-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80U78-2; Sequence=VSP_009317, VSP_009318;
CC       Name=3;
CC         IsoId=Q80U78-3; Sequence=VSP_009317;
CC       Name=4;
CC         IsoId=Q80U78-4; Sequence=VSP_009315, VSP_009316;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed in brain, heart,
CC       kidney, liver, lung, skin, intestine, spleen, testis and thymus.
CC       Weakly or not expressed in muscles and stomach. Expressed at
CC       various stages of myeloid and lymphoid cell development.
CC   -!- DOMAIN: The pumilio repeats mediate the association with RNA by
CC       packing together to form a right-handed superhelix that
CC       approximates a half donut. The number as well as the specific
CC       sequence of the repeats determine the specificity for target mRNAs
CC       (By similarity).
CC   -!- SIMILARITY: Contains 1 PUM-HD domain.
CC   -!- SIMILARITY: Contains 8 pumilio repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65487.1; Type=Erroneous initiation;
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DR   EMBL; AF321909; AAG42319.1; -; mRNA.
DR   EMBL; AK122205; BAC65487.1; ALT_INIT; mRNA.
DR   EMBL; AK052145; BAC34857.1; -; mRNA.
DR   EMBL; BC048174; AAH48174.1; -; mRNA.
DR   EMBL; BC050747; AAH50747.1; -; mRNA.
DR   IPI; IPI00330262; -.
DR   IPI; IPI00400349; -.
DR   IPI; IPI00400350; -.
DR   IPI; IPI00400351; -.
DR   RefSeq; NP_001153075.1; NM_001159603.1.
DR   RefSeq; NP_001153076.1; NM_001159604.1.
DR   RefSeq; NP_001153077.1; NM_001159605.1.
DR   RefSeq; NP_001153078.1; NM_001159606.1.
DR   RefSeq; NP_109647.2; NM_030722.2.
DR   UniGene; Mm.440206; -.
DR   ProteinModelPortal; Q80U78; -.
DR   SMR; Q80U78; 829-1171.
DR   STRING; Q80U78; -.
DR   PhosphoSite; Q80U78; -.
DR   PRIDE; Q80U78; -.
DR   Ensembl; ENSMUST00000030315; ENSMUSP00000030315; ENSMUSG00000028580.
DR   Ensembl; ENSMUST00000097863; ENSMUSP00000095475; ENSMUSG00000028580.
DR   GeneID; 80912; -.
DR   KEGG; mmu:80912; -.
DR   UCSC; uc008uzl.1; mouse.
DR   UCSC; uc008uzn.1; mouse.
DR   UCSC; uc008uzo.1; mouse.
DR   CTD; 80912; -.
DR   MGI; MGI:1931749; Pum1.
DR   GeneTree; ENSGT00390000017241; -.
DR   HOGENOM; HBG445218; -.
DR   HOVERGEN; HBG049462; -.
DR   InParanoid; Q80U78; -.
DR   OMA; NGLPVQN; -.
DR   OrthoDB; EOG4P8FHP; -.
DR   PhylomeDB; Q80U78; -.
DR   NextBio; 350286; -.
DR   ArrayExpress; Q80U78; -.
DR   Bgee; Q80U78; -.
DR   CleanEx; MM_PUM1; -.
DR   Genevestigator; Q80U78; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR001313; Pumilio_RNA-bd_rpt.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF00806; PUF; 8.
DR   SMART; SM00025; Pumilio; 8.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50302; PUM; 8.
DR   PROSITE; PS50303; PUM_HD; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Phosphoprotein; Repeat; RNA-binding;
KW   Translation regulation.
FT   CHAIN         1   1189       Pumilio homolog 1.
FT                                /FTId=PRO_0000075918.
FT   DOMAIN      829   1171       PUM-HD.
FT   REPEAT      849    884       Pumilio 1.
FT   REPEAT      885    920       Pumilio 2.
FT   REPEAT      921    958       Pumilio 3.
FT   REPEAT      959    994       Pumilio 4.
FT   REPEAT      995   1030       Pumilio 5.
FT   REPEAT     1031   1066       Pumilio 6.
FT   REPEAT     1067   1102       Pumilio 7.
FT   REPEAT     1106   1145       Pumilio 8.
FT   COMPBIAS    393    614       Ala-rich.
FT   COMPBIAS    476    524       Gln-rich.
FT   COMPBIAS    643    816       Ser-rich.
FT   MOD_RES      19     19       Phosphoserine (By similarity).
FT   MOD_RES      75     75       Phosphoserine (By similarity).
FT   MOD_RES     124    124       Phosphoserine.
FT   MOD_RES     209    209       Phosphoserine (By similarity).
FT   MOD_RES     710    710       Phosphoserine.
FT   MOD_RES     715    715       Phosphoserine (By similarity).
FT   MOD_RES     807    807       Phosphoserine (By similarity).
FT   VAR_SEQ     181    189       DHSVSQPIM -> GNLALASLL (in isoform 4).
FT                                /FTId=VSP_009315.
FT   VAR_SEQ     190   1189       Missing (in isoform 4).
FT                                /FTId=VSP_009316.
FT   VAR_SEQ     418    418       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_009317.
FT   VAR_SEQ     952    953       Missing (in isoform 2).
FT                                /FTId=VSP_009318.
FT   CONFLICT    186    186       Q -> H (in Ref. 1; AAG42319).
FT   CONFLICT    545    545       A -> D (in Ref. 1; AAG42319).
FT   CONFLICT    552    552       P -> T (in Ref. 1; AAG42319).
FT   CONFLICT    555    555       A -> G (in Ref. 1; AAG42319).
SQ   SEQUENCE   1189 AA;  126619 MW;  CCB18634FBE3468A CRC64;
     MSVACVLKRK AVLWQDSFSP HLKHHPQEPA NPNMPVVLTS GTGSQAQPQP AANQALAAGT
     HSSPVPGSIG VAGRSQDDAM VDYFFQRQHG EQLGGGGSGG GGYNTSKHRW PTGDNIHAEH
     QVRSMDELNH DFQALALEGR AMGEQLLPGK KFWETDESSK DGPKGIFLGD QWRDSAWGTS
     DHSVSQPIMV QRRPGQSFHV NSEVNSVLSP RSESGGLGVS MVEYVLSSSP GDSCLRKGGF
     GPRDADSDEN DKGEKKNKGT FDGDKLGDLK EEGDVMDKTN GLPVQNGIDA DVKDFSRTPG
     NCQNSANEVD LLGPNQNGSE GLAQLTSTNG AKPVEDFSNM ESQSVPLDPM EHVGMEPLQF
     DYSGTQVPVD SAAATVGLFD YNSQQQLFQR PNALAVQQLT AAQQQQYALA AAHQPHIAGL
     APAAFVPNPY IISAAPPGTD PYTAGLAAAA TLGPAVVPHQ YYGVTPWGVY PASLFQQQAA
     AAAAATNSAT QQSAPQAQQG QQQVLRGGAS QRPLTPNQNQ QGQQTDPLVA AAAVNSALAF
     GQGLAAGMPG YPVLAPAAYY DQTGALVVNA GARNGLGAPV RLVAPAPVII SSSAAQAAVA
     AAAASANGAA GGLAGTTNGP FRPLGTQQPQ PQPQQQPSNN LASSSFYGNN SLSSNSQSSS
     LFSQGSAQPA NTSLGFGSSS SLGATLGSAL GGFGTAVANS NTGSGSRRDS LTGSSDLYKR
     TSSSLAPIGH SFYSSLSYSS SPGPVGMPLP SQGPGHSQTP PPSLSSHGSS SSLNLGGLTN
     GSGRYISAAP GAEAKYRSAS SASSLFSPSS TLFSSSRLRY GMSDVMPSGR SRLLEDFRNN
     RYPNLQLREI AGHIMEFSQD QHGSRFIQLK LERATAAERQ LVFNEILQAA YQLMVDVFGN
     YVIQKFFEFG SHEQKLALAE RIRGHVLSLA LQMYGCRVIQ KALEFIPSDQ QVINEMVREL
     DGHVLKCVKD QNGNHVVQKC IECVQPQSLQ FIIDAFKGQV FALSTHPYGC RVIQRILEHC
     LPDQTLPILE ELHQHTEQLV QDQYGNYVIQ HVLEHGRPED KSKIVAEIRG NVLVLSQHKF
     ASNVVEKCVT HASRTERAVL IDEVCTMNDG PHSALYTMMK DQYANYVVQK MIDVAEPGQR
     KIVMHKIRPH IATLRKYTYG KHILAKLEKY YMKNGVDLGP ICGPPNGII
//
ID   UBP8_MOUSE              Reviewed;        1080 AA.
AC   Q80U87; A2AI53; Q80YP2; Q8R0D3; Q9EQU1; Q9WVP5;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 8;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 8;
DE   AltName: Full=Ubiquitin isopeptidase Y;
DE            Short=mUBPy;
DE   AltName: Full=Ubiquitin thiolesterase 8;
DE   AltName: Full=Ubiquitin-specific-processing protease 8;
GN   Name=Usp8; Synonyms=Kiaa0055, Ubpy;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SH3-BINDING, INTERACTION WITH STAM2, AND
RP   MUTAGENESIS OF PRO-405; GLN-406; VAL-407; ASP-408; ARG-409; THR-410;
RP   LYS-411; LYS-412 AND PRO-413.
RX   MEDLINE=20545486; PubMed=10982817; DOI=10.1074/jbc.M007251200;
RA   Kato M., Miyazawa K., Kitamura N.;
RT   "A deubiquitinating enzyme UBPY interacts with the Src homology 3
RT   domain of Hrs-binding protein via a novel binding motif
RT   PX(V/I)(D/N)RXXKP.";
RL   J. Biol. Chem. 275:37481-37487(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   INTERACTION WITH RASGRF1.
RC   TISSUE=Embryo;
RX   PubMed=11500497; DOI=10.1074/jbc.M103454200;
RA   Gnesutta N., Ceriani M., Innocenti M., Mauri I., Zippel R.,
RA   Sturani E., Borgonovo B., Berruti G., Martegani E.;
RT   "Cloning and characterization of mouse UBPy, a deubiquitinating enzyme
RT   that interacts with the ras guanine nucleotide exchange factor
RT   CDC25(Mm)/Ras-GRF1.";
RL   J. Biol. Chem. 276:39448-39454(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RNF41, FUNCTION,
RP   AND MUTAGENESIS OF CYS-748.
RX   PubMed=15314180; DOI=10.1128/MCB.24.17.7748-7757.2004;
RA   Wu X., Yen L., Irwin L., Sweeney C., Carraway K.L. III;
RT   "Stabilization of the E3 ubiquitin ligase Nrdp1 by the
RT   deubiquitinating enzyme USP8.";
RL   Mol. Cell. Biol. 24:7748-7757(2004).
RN   [7]
RP   INTERACTION WITH OTUB1 AND RNF128, AND MUTAGENESIS OF CYS-748.
RX   PubMed=14661020; DOI=10.1038/ni1017;
RA   Soares L., Seroogy C., Skrenta H., Anandasabapathy N., Lovelace P.,
RA   Chung C.D., Engleman E., Fathman C.G.;
RT   "Two isoforms of otubain 1 regulate T cell anergy via GRAIL.";
RL   Nat. Immunol. 5:45-54(2004).
RN   [8]
RP   TISSUE SPECIFICITY, AND INTERACTION WITH DNAJB3.
RX   PubMed=15342353; DOI=10.1095/biolreprod.104.030866;
RA   Berruti G., Martegani E.;
RT   "The deubiquitinating enzyme mUBPy interacts with the sperm-specific
RT   molecular chaperone MSJ-1: the relation with the proteasome, acrosome,
RT   and centrosome in mouse male germ cells.";
RL   Biol. Reprod. 72:14-21(2005).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION, AND MUTAGENESIS OF
RP   CYS-748.
RX   PubMed=16120644; DOI=10.1091/mbc.E05-06-0560;
RA   Mizuno E., Iura T., Mukai A., Yoshimori T., Kitamura N., Komada M.;
RT   "Regulation of epidermal growth factor receptor down-regulation by
RT   UBPY-mediated deubiquitination at endosomes.";
RL   Mol. Biol. Cell 16:5163-5174(2005).
RN   [10]
RP   FUNCTION, MUTAGENESIS OF CYS-748, AND INTERACTION WITH ESP15.
RX   PubMed=16771824; DOI=10.1111/j.1600-0854.2006.00452.x;
RA   Mizuno E., Kobayashi K., Yamamoto A., Kitamura N., Komada M.;
RT   "A deubiquitinating enzyme UBPY regulates the level of protein
RT   ubiquitination on endosomes.";
RL   Traffic 7:1017-1031(2006).
RN   [11]
RP   PHOSPHORYLATION, INTERACTION WITH EGFR, AND FUNCTION.
RX   PubMed=17121848; DOI=10.1074/jbc.M604711200;
RA   Alwan H.A., van Leeuwen J.E.;
RT   "UBPY-mediated epidermal growth factor receptor (EGFR) de-
RT   ubiquitination promotes EGFR degradation.";
RL   J. Biol. Chem. 282:1658-1669(2007).
RN   [12]
RP   PHOSPHORYLATION AT SER-680, INTERACTION WITH YWHAE, MUTAGENESIS OF
RP   SER-680, AND SUBCELLULAR LOCATION.
RX   PubMed=16944949; DOI=10.1021/pr060206k;
RA   Ballif B.A., Cao Z., Schwartz D., Carraway K.L. III, Gygi S.P.;
RT   "Identification of 14-3-3epsilon substrates from embryonic murine
RT   brain.";
RL   J. Proteome Res. 5:2372-2379(2006).
RN   [13]
RP   FUNCTION, PHOSPHORYLATION AT SER-680, INTERACTION WITH YWHAE; YWHAG
RP   AND YWHAZ, MUTAGENESIS OF SER-680, AND SUBCELLULAR LOCATION.
RX   PubMed=17720156; DOI=10.1016/j.yexcr.2007.07.028;
RA   Mizuno E., Kitamura N., Komada M.;
RT   "14-3-3-dependent inhibition of the deubiquitinating activity of UBPY
RT   and its cancellation in the M phase.";
RL   Exp. Cell Res. 313:3624-3634(2007).
RN   [14]
RP   FUNCTION, PHOSPHORYLATION AT THR-907, AND MUTAGENESIS OF THR-907.
RX   PubMed=17210635; DOI=10.1128/MCB.01245-06;
RA   Cao Z., Wu X., Yen L., Sweeney C., Carraway K.L. III;
RT   "Neuregulin-induced ErbB3 downregulation is mediated by a protein
RT   stability cascade involving the E3 ubiquitin ligase Nrdp1.";
RL   Mol. Cell. Biol. 27:2180-2188(2007).
RN   [15]
RP   FUNCTION.
RX   PubMed=17452457; DOI=10.1128/MCB.01566-06;
RA   Niendorf S., Oksche A., Kisser A., Lohler J., Prinz M., Schorle H.,
RA   Feller S., Lewitzky M., Horak I., Knobeloch K.P.;
RT   "Essential role of ubiquitin-specific protease 8 for receptor tyrosine
RT   kinase stability and endocytic trafficking in vivo.";
RL   Mol. Cell. Biol. 27:5029-5039(2007).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-680, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [17]
RP   FUNCTION, ASSOCIATION WITH THE ESCRT-0 COMPLEX, AND
RP   MICROTUBULE-BINDING.
RX   PubMed=20130268; DOI=10.1095/biolreprod.109.081679;
RA   Berruti G., Ripolone M., Ceriani M.;
RT   "USP8, a regulator of endosomal sorting, is involved in mouse acrosome
RT   biogenesis through interaction with the spermatid ESCRT-0 complex and
RT   microtubules.";
RL   Biol. Reprod. 82:930-939(2010).
CC   -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from
CC       proteins and therefore plays an important regulatory role at the
CC       level of protein turnover by preventing degradation. Converts both
CC       'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity
CC       is enhanced in the M phase. Involved in cell proliferation.
CC       Required to enter into S phase in response to serum stimulation.
CC       May regulate T-cell anergy mediated by RNF128 via the formation of
CC       a complex containing RNF128 and OTUB1. Probably regulates the
CC       stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin
CC       dynamics, cargo sorting, membrane traffic at early endosomes, and
CC       maintenance of ESCRT-0 stability. The level of protein
CC       ubiquitination on endosomes is essential for maintaining the
CC       morphology of the organelle. Deubiquitinates EPS15 and controles
CC       tyrosine kinase stability. Removes conjugated ubiquitin from EGFR
CC       thus regulating EGFR degradation and downstream MAPK signaling.
CC       Involved in acrosome biogenesis through interaction with the
CC       spermatid ESCRT-0 complex and microtubules.
CC   -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- SUBUNIT: Forms a ternary complex with RNF128 and OTUB1. Interacts
CC       (via C-terminal UCH catalytic domain) with OTUB1 isoform 1.
CC       Interacts with STAM2 (via SH3 domain). Interacts with DNAJB3,
CC       EGFR, EPS15, RASGRF1, RNF41, YWHAE, YWHAG and YWHAZ. Interacts
CC       with NBR1, RASGRF1, RNF41 and IST1 (By similarity). Associates
CC       with the ESCRT-0 complex and with microtubules.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Endosome membrane;
CC       Peripheral membrane protein (By similarity). Cell membrane;
CC       Peripheral membrane protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis. Expressed at
CC       intermediate level in brain.
CC   -!- DOMAIN: The MIT domain is required for endosomal localization,
CC       CHMP1B-binding, maintenance of ESCRT-0 stability and EGFR
CC       degradation (By similarity).
CC   -!- DOMAIN: The rhodanese domain is sufficent for RNF41-binding.
CC   -!- PTM: Phosphorylation of Ser-680 is essential for interaction with
CC       YWHAE and for cytosol localization. Undergoes dephosphorylation at
CC       Ser-680 in the M phase. Tyrosine-phosphorylated in its N-terminal
CC       half in an EGFR-dependent manner.
CC   -!- PTM: Ubiquitinated. Inactive form is mostly monoubiquitinated, but
CC       polyubiquitination happens too. Ubiquitination is increased in
CC       EGF-stimulated cells. Ubiquitination of active form is
CC       undetectable, suggesting a possibility that USP8 deubiquitinates
CC       itself, thereby regulating its own function.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC   -!- SIMILARITY: Contains 1 MIT domain.
CC   -!- SIMILARITY: Contains 1 rhodanese domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65477.1; Type=Erroneous initiation;
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DR   EMBL; AB045709; BAB18534.1; -; mRNA.
DR   EMBL; AF057146; AAD38869.1; -; mRNA.
DR   EMBL; AK122195; BAC65477.1; ALT_INIT; mRNA.
DR   EMBL; AL732330; CAM14544.1; -; Genomic_DNA.
DR   EMBL; BC027052; AAH27052.1; -; mRNA.
DR   EMBL; BC050947; AAH50947.1; -; mRNA.
DR   EMBL; BC061465; AAH61465.1; -; mRNA.
DR   EMBL; BC066126; AAH66126.1; -; mRNA.
DR   IPI; IPI00171977; -.
DR   RefSeq; NP_062703.2; NM_019729.2.
DR   UniGene; Mm.272629; -.
DR   ProteinModelPortal; Q80U87; -.
DR   SMR; Q80U87; 6-132, 181-316, 718-1072.
DR   MINT; MINT-144852; -.
DR   STRING; Q80U87; -.
DR   MEROPS; C19.011; -.
DR   PhosphoSite; Q80U87; -.
DR   PRIDE; Q80U87; -.
DR   Ensembl; ENSMUST00000028841; ENSMUSP00000028841; ENSMUSG00000027363.
DR   GeneID; 84092; -.
DR   KEGG; mmu:84092; -.
DR   UCSC; uc008meb.1; mouse.
DR   CTD; 84092; -.
DR   MGI; MGI:1934029; Usp8.
DR   GeneTree; ENSGT00600000084018; -.
DR   HOVERGEN; HBG012631; -.
DR   OrthoDB; EOG4XKV6B; -.
DR   PhylomeDB; Q80U87; -.
DR   BRENDA; 3.1.2.15; 244.
DR   NextBio; 350878; -.
DR   ArrayExpress; Q80U87; -.
DR   Bgee; Q80U87; -.
DR   CleanEx; MM_USP8; -.
DR   Genevestigator; Q80U87; -.
DR   GermOnline; ENSMUSG00000027363; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0031313; C:extrinsic to endosome membrane; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:EC.
DR   GO; GO:0004843; F:ubiquitin-specific protease activity; IDA:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0007032; P:endosome organization; IMP:UniProtKB.
DR   GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
DR   GO; GO:0007265; P:Ras protein signal transduction; IPI:MGI.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR015063; DUF1873.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19.
DR   InterPro; IPR001763; Rhodanese-like.
DR   Gene3D; G3DSA:3.40.250.10; Rhodanese-like; 1.
DR   Pfam; PF08969; DUF1873; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52821; Rhodanese-like; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; 1.
DR   PROSITE; PS50235; UCH_2_3; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell membrane; Cytoplasm; Endosome; Hydrolase; Membrane;
KW   Nucleus; Phosphoprotein; Protease; SH3-binding; Thiol protease;
KW   Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN         1   1080       Ubiquitin carboxyl-terminal hydrolase 8.
FT                                /FTId=PRO_0000080628.
FT   DOMAIN       33    116       MIT.
FT   DOMAIN      195    313       Rhodanese.
FT   MOTIF       405    413       SH3-binding.
FT   ACT_SITE    748    748       Nucleophile.
FT   ACT_SITE   1029   1029       Proton acceptor (By similarity).
FT   MOD_RES     446    446       Phosphoserine (By similarity).
FT   MOD_RES     680    680       Phosphoserine.
FT   MOD_RES     681    681       Phosphoserine (By similarity).
FT   MOD_RES     907    907       Phosphothreonine.
FT   MUTAGEN     405    405       P->A: Abolishes interaction with the SH3
FT                                domain of STAM2.
FT   MUTAGEN     406    406       Q->A: Does not affect interaction with
FT                                the SH3 domain of STAM2.
FT   MUTAGEN     407    407       V->A: Reduces interaction with the SH3
FT                                domain of STAM2.
FT   MUTAGEN     408    408       D->A: Reduces interaction with the SH3
FT                                domain of STAM2.
FT   MUTAGEN     409    409       R->A: Abolishes interaction with the SH3
FT                                domain of STAM2.
FT   MUTAGEN     410    410       T->A: Does not affect interaction with
FT                                the SH3 domain of STAM2.
FT   MUTAGEN     411    411       K->A: Does not affect interaction with
FT                                the SH3 domain of STAM2.
FT   MUTAGEN     412    412       K->A: Abolishes interaction with the SH3
FT                                domain of STAM2.
FT   MUTAGEN     413    413       P->A: Abolishes interaction with the SH3
FT                                domain of STAM2.
FT   MUTAGEN     680    680       S->A: Abolishes the interaction with
FT                                YWHAE and leads to accumulation in the
FT                                nucleus.
FT   MUTAGEN     748    748       C->A: Impairs deubiquitination of EPS15,
FT                                RNF128 and RNF41.
FT   MUTAGEN     907    907       T->A: Reduces stabilization activity on
FT                                RNF41.
FT   CONFLICT    139    139       Q -> P (in Ref. 2; AAD38869).
FT   CONFLICT    151    151       K -> R (in Ref. 1; BAB18534).
FT   CONFLICT    349    349       T -> A (in Ref. 1; BAB18534).
FT   CONFLICT    370    370       E -> G (in Ref. 1; BAB18534).
FT   CONFLICT    557    557       D -> N (in Ref. 1; BAB18534).
FT   CONFLICT    576    576       P -> L (in Ref. 1; BAB18534).
FT   CONFLICT    837    837       F -> S (in Ref. 1; BAB18534).
FT   CONFLICT    865    873       DLQAAEHAW -> EPAGGRARL (in Ref. 1;
FT                                BAB18534).
FT   CONFLICT    885    886       VA -> RL (in Ref. 1; BAB18534).
FT   CONFLICT    894    894       S -> A (in Ref. 1; BAB18534).
SQ   SEQUENCE   1080 AA;  122611 MW;  7F458E3B1AF0B7FA CRC64;
     MPAVASVPKE LYLSSSLKDL NKKTEVKPEK TSTKNYIHSA QKIFKTAEEC RLDRDEERAY
     VLYMKYVAVY NLIKKRPDFK QQQDYYLSIL GPANIKKAIE EAERLSESLK LRYEEAEVRK
     QLEEKDRREE EQLQQQKRQE MGREDSGAAA KRSVENLLDS KTKTQRINGE KSEGAAAAER
     GAITAKELYT MMMDKNTSLI IMDARKIQDY QHSCILDSLS VPEEAISPGV TASWIEANLS
     DDSKDTWKKR GSVDYVVLLD WFSSAKDLLL GTTLRSLKDA LFKWESKTVL RHEPLVLEGG
     YENWLLCYPQ FTTNAKVTPP PRSRAEEVSV SLDFTYPSLE EPVPSKLPTQ MPPPPIETNE
     KALLVTDQDE KLRLSTQPAL AGPGAAPRAE ASPIIQPAPA TKSVPQVDRT KKPSVKLPED
     HRIKSENTDQ SGRVLSDRST KPVFPSPTTM LTDEEKARIH QETALLMEKN KQEKELWDKQ
     QKEQKEKLRR EEQERKAGKT QDADERDSTE NQHKAKDGQE KKDSKQTKTE DRELSADGAQ
     EATGTQRQSK SEHEASDAKV PVEGKRCPTS EAQKRPADVS PASVSGELNA GKAQREPLTR
     ARSEEMGRIV PGLPLGWAKF LDPITGTFRY YHSPTNTVHM YPPEMAPSSA PPSTPPTHKV
     KPQVPAERDR EPSKLKRSYS SPDITQALQE EEKRRPAVTP MVNRENKPPC YPKAEISRLS
     ASQIRNLNPV FGGSGPALTG LRNLGNTCYM NSILQCLCNA PHLADYFNRN CYQDDINRSN
     LLGHKGEVAE EFGIIMKALW TGQYRYISPK DFKVTIGKIN DQFAGSSQQD SQELLLFLMD
     GLHEDLNKAD NRKRHKEENN EHLDDLQAAE HAWQKHKQLN ESIIVALFQG QFKSTVQCLT
     CRRRSRTFEA FMYLSLPLAS TSKCTLQDCL RLFSKEEKLT DNNRFYCSHC RARRDSLKKI
     EIWKLPPVLL VHLKRFSYDG RWKQKLQTSV DFPLENLDLS QYVIGPKNSL KKYNLFSVSN
     HYGGLDGGHY TAYCKNAARQ RWFKFDDHEV SDISVSSVRS SAAYILFYTS LGPRITDVAT
//
ID   Q80UD0_MOUSE            Unreviewed;        74 AA.
AC   Q80UD0;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 32.
DE   SubName: Full=G protein-coupled receptor TM7SF1L2;
DE   Flags: Fragment;
GN   Name=Gpr137c; Synonyms=Gm908;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=22584407; PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA   Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA   Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA   Bergmann J.E., Gaitanaris G.A.;
RT   "The G protein-coupled receptor repertoires of human and mouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
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DR   EMBL; AY255546; AAO85058.1; -; mRNA.
DR   IPI; IPI00761628; -.
DR   UniGene; Mm.343793; -.
DR   Ensembl; ENSMUST00000100682; ENSMUSP00000098249; ENSMUSG00000049092.
DR   Ensembl; ENSMUST00000146150; ENSMUSP00000120015; ENSMUSG00000049092.
DR   MGI; MGI:1917963; Gpr137c.
DR   eggNOG; roNOG05168; -.
DR   GeneTree; ENSGT00390000008320; -.
DR   HOGENOM; HBG505574; -.
DR   InParanoid; Q80UD0; -.
DR   OrthoDB; EOG4H9XKT; -.
DR   Bgee; Q80UD0; -.
DR   Genevestigator; Q80UD0; -.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Receptor.
FT   NON_TER       1      1
FT   NON_TER      74     74
SQ   SEQUENCE   74 AA;  8533 MW;  BF57A75045A816C5 CRC64;
     LFLWEHVPAW SVVLFFRAQR LNQNLAPAGM ISSHSYSSRA FFFDNPRRYD SDDDLPRLGN
     SREGSLSNSQ TLGW
//
ID   Q80UE4_MOUSE            Unreviewed;       794 AA.
AC   Q80UE4;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   05-OCT-2010, entry version 54.
DE   SubName: Full=Protein 4.1G;
GN   Name=Epb4.1l2; Synonyms=EBP4.1L2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=98198473; PubMed=9531554; DOI=10.1083/jcb.141.1.143;
RA   Walensky L.D., Gascard P., Fields M.E., Blackshaw S., Conboy J.G.,
RA   Mohandas N., Snyder S.H.;
RT   "The 13-kD FK506 binding protein, FKBP13, interacts with a novel
RT   homologue of the erythrocyte membrane cytoskeletal protein 4.1.";
RL   J. Cell Biol. 141:143-153(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c; TISSUE=Brain;
RA   Phillips G.W., Keating L.A., Bignone P.A., Maggs A.M., Pinder J.C.,
RA   Gascard P.D., Baines A.J.;
RT   "The activities and structure of protein 4.1G are controlled by
RT   complex tissue and development-specific mRNA splicing.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 FERM domain.
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DR   EMBL; AJ539143; CAD62252.1; -; mRNA.
DR   IPI; IPI00330290; -.
DR   UniGene; Mm.306026; -.
DR   HSSP; P11171; 1GG3.
DR   ProteinModelPortal; Q80UE4; -.
DR   SMR; Q80UE4; 209-540.
DR   STRING; Q80UE4; -.
DR   PRIDE; Q80UE4; -.
DR   Ensembl; ENSMUST00000092644; ENSMUSP00000090313; ENSMUSG00000019978.
DR   UCSC; uc007erp.1; mouse.
DR   MGI; MGI:103009; Epb4.1l2.
DR   HOVERGEN; HBG007777; -.
DR   ArrayExpress; Q80UE4; -.
DR   Bgee; Q80UE4; -.
DR   Genevestigator; Q80UE4; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0019898; C:extrinsic to membrane; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0042731; F:PH domain binding; IDA:MGI.
DR   GO; GO:0030507; F:spectrin binding; IDA:MGI.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR008379; Band_4.1_C.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR021187; Band_41_protein.
DR   InterPro; IPR000798; Ez/rad/moesin.
DR   InterPro; IPR014847; FERM-adjacent.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH_type.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF05902; 4_1_CTD; 1.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   PIRSF; PIRSF002304; Membrane_skeletal_4_1; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   794 AA;  88462 MW;  A57D5FBAF523C34B CRC64;
     MTTEVGSASE VKKGSDQAGA DASKEKAKEV ENEQTPVSEP EEEKGSQPGP PVERQSTPRL
     RKRGKDPSEN RGISRFIPPW LKKQRSYNLV VAKDGGDKKE PTQADVEDQI LGKEESLPEE
     ESRAKGDAEE MAQRKHLEVQ VEVREAKPAL KSSVETQPAE EVRKDKEETI QDTQEEKLEG
     GAAKRETKEV QTSELKAEVA SQKATKKTKT VLAKVTLLDG TEYSCDLEKR AKGQVLFDRV
     CEHLNLLEKD YFGLLFQDHP EQKNWLDPAK EIKRQLKNLP WLFTFNVKFY PPDPSQLTED
     ITRYFLCLQL RQDIASGRLP CSFVTHALLG SYTLQAEHGD YDPEEYDSID LGDFQFAPAH
     TKELEEKVSE LHKTHRGLSP AQADSQFLEN AKRLSMYGVD LHHAKDSEGV DIKLGVCANG
     LLIYKDRLRI NRFAWPKILK ISYKRSNFYI KVRPAELEQF ESTIGFKLPN HRAAKRLWKV
     CVEHHTFYRL VSPEQPPKTK FLTLGSKFRY SGRTQAQTRE ASTLIDRPAP QFERASSKRV
     SRSLDGAPIG VVDQSPPGEG SVPGPGVISY TTIQDGRRDS KSPTKATPLP AEGKSSHETL
     NVVEEKKRAE VGKDESVITE EMNGKEMSPG HGPGETRKVE PVAHKDSTSL SSESSSSSSE
     SEEDVGEYQP HHRVTEGTIR EEQEECDEEL EEEPGQGAKI DGGAGGDSGV LLTAQTITSE
     SASTTTTTHI TKTVKGGISE TRIEKRIVIT GDAALDHDQA LAQAIREARE QHPDMSVTRV
     VVHKETELAE EGEE
//
ID   PLXA4_MOUSE             Reviewed;        1893 AA.
AC   Q80UG2; Q5DTW8; Q8BKK9;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 2.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Plexin-A4;
DE   Flags: Precursor;
GN   Name=Plxna4; Synonyms=Kiaa1550;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Embryonic brain;
RX   MEDLINE=22480023; PubMed=12591607; DOI=10.1016/S0925-4773(02)00421-5;
RA   Suto F., Murakami Y., Nakamura F., Goshima Y., Fujisawa H.;
RT   "Identification and characterization of a novel mouse plexin, plexin-
RT   A4.";
RL   Mech. Dev. 120:385-396(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1042-1893.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1695-1893.
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms a receptor complex with neuropilin-1 and can
CC       propagate semaphorin-3A elicited inhibitory signals into cells and
CC       neurons.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- TISSUE SPECIFICITY: Expressed in the developing nervous system.
CC       Widely expressed in both the central and peripheral nervous
CC       systems. Expressed in the peripheral ganglia, somatosensory,
CC       olfactory, visual, auditory and equilibrium systems.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the plexin family.
CC   -!- SIMILARITY: Contains 4 IPT/TIG domains.
CC   -!- SIMILARITY: Contains 3 PSI domains.
CC   -!- SIMILARITY: Contains 1 Sema domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC56599.1; Type=Erroneous initiation;
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DR   EMBL; AB073228; BAC56599.1; ALT_INIT; mRNA.
DR   EMBL; AK051614; BAC34692.1; -; mRNA.
DR   EMBL; AK220402; BAD90257.1; -; mRNA.
DR   IPI; IPI00187545; -.
DR   RefSeq; NP_786926.2; NM_175750.3.
DR   UniGene; Mm.444029; -.
DR   ProteinModelPortal; Q80UG2; -.
DR   SMR; Q80UG2; 37-701, 796-1041, 1263-1890.
DR   STRING; Q80UG2; -.
DR   PhosphoSite; Q80UG2; -.
DR   PRIDE; Q80UG2; -.
DR   Ensembl; ENSMUST00000115096; ENSMUSP00000110748; ENSMUSG00000029765.
DR   GeneID; 243743; -.
DR   KEGG; mmu:243743; -.
DR   UCSC; uc009bgm.1; mouse.
DR   CTD; 243743; -.
DR   MGI; MGI:2179061; Plxna4.
DR   eggNOG; roNOG10635; -.
DR   GeneTree; ENSGT00560000076899; -.
DR   HOGENOM; HBG716170; -.
DR   HOVERGEN; HBG105711; -.
DR   InParanoid; Q80UG2; -.
DR   OrthoDB; EOG4N30N0; -.
DR   NextBio; 385902; -.
DR   ArrayExpress; Q80UG2; -.
DR   Bgee; Q80UG2; -.
DR   CleanEx; MM_PLXNA4; -.
DR   Genevestigator; Q80UG2; -.
DR   GermOnline; ENSMUSG00000029765; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0017154; F:semaphorin receptor activity; IGI:MGI.
DR   GO; GO:0021960; P:anterior commissure morphogenesis; IMP:MGI.
DR   GO; GO:0071445; P:cellular response to protein stimulus; IMP:MGI.
DR   GO; GO:0021793; P:chemorepulsion of branchiomotor axon; IMP:MGI.
DR   GO; GO:0021610; P:facial nerve morphogenesis; IMP:MGI.
DR   GO; GO:0021615; P:glossopharyngeal nerve morphogenesis; IMP:MGI.
DR   GO; GO:0021784; P:postganglionic parasympathetic nervous system development; IMP:MGI.
DR   GO; GO:0048841; P:regulation of axon extension involved in axon guidance; IMP:MGI.
DR   GO; GO:0050923; P:regulation of negative chemotaxis; IMP:MGI.
DR   GO; GO:0071526; P:semaphorin-plexin signaling pathway; IMP:MGI.
DR   GO; GO:0048485; P:sympathetic nervous system development; IMP:MGI.
DR   GO; GO:0021636; P:trigeminal nerve morphogenesis; IMP:MGI.
DR   GO; GO:0021644; P:vagus nerve morphogenesis; IMP:MGI.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002909; IPT_TIG_rcpt.
DR   InterPro; IPR003659; Plexin-like.
DR   InterPro; IPR016201; Plexin-like_fold.
DR   InterPro; IPR013548; Plexin_cytoplasmic_RasGAP_dom.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR001627; Semaphorin/CD100_Ag.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 4.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF08337; Plexin_cytopl; 1.
DR   Pfam; PF01437; PSI; 3.
DR   Pfam; PF01403; Sema; 1.
DR   Pfam; PF01833; TIG; 4.
DR   SMART; SM00429; IPT; 4.
DR   SMART; SM00423; PSI; 3.
DR   SMART; SM00630; Sema; 1.
DR   SUPFAM; SSF81296; Ig_E-set; 4.
DR   SUPFAM; SSF103575; Plexin-like_fold; 2.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   SUPFAM; SSF101912; Sema; 1.
DR   PROSITE; PS51004; SEMA; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW   Receptor; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     23       Potential.
FT   CHAIN        24   1893       Plexin-A4.
FT                                /FTId=PRO_0000240284.
FT   TOPO_DOM     24   1236       Extracellular (Potential).
FT   TRANSMEM   1237   1257       Helical; (Potential).
FT   TOPO_DOM   1258   1893       Cytoplasmic (Potential).
FT   DOMAIN       24    506       Sema.
FT   DOMAIN      508    558       PSI 1.
FT   DOMAIN      654    701       PSI 2.
FT   DOMAIN      802    855       PSI 3.
FT   DOMAIN      857    951       IPT/TIG 1.
FT   DOMAIN      953   1036       IPT/TIG 2.
FT   DOMAIN     1039   1138       IPT/TIG 3.
FT   DOMAIN     1141   1229       IPT/TIG 4.
FT   MOD_RES     945    945       Phosphoserine (By similarity).
FT   MOD_RES    1349   1349       N6-acetyllysine (By similarity).
FT   CARBOHYD    654    654       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1006   1006       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1131   1131       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1179   1179       N-linked (GlcNAc...) (Potential).
FT   DISULFID    129    137       By similarity.
FT   DISULFID    283    392       By similarity.
FT   DISULFID    299    355       By similarity.
FT   CONFLICT   1607   1607       V -> E (in Ref. 2; BAC34692).
SQ   SEQUENCE   1893 AA;  212561 MW;  32AE2D9EC6FC5314 CRC64;
     MKAMPWNWTC LLSHLLVVGM GSSTLLPRQP PQLSQKPSFV TFRGEPAEGF NHLVVDERTG
     HIYLGAVNRI YKLSSDLKVL VTHQTGPDED NPKCYPPRIV QTCNEPLAST NNVNKMLLID
     YKENRLIACG SLYQGICKLL RLEDLFKLGE PFHKKEHYLS GVNESGSVFG VIVSYSNFDD
     KLFIATAVDG KPEYFPTISS RKLTKNSEAD GMFAYVFHDE FVASMIKIPS DTFTVIPDFD
     IYYVYGFSSG NFVYFLTLQP EMVSPPGSTT KEQVYTSKLV RLCKEDTAFN SYVEVPIGCE
     RNGVEYRLLQ AAYLSKAGAV LGRTLGVRPD DDLLFTVFSK GQKRKMKSLD ESALCIFILK
     QINDRIKDRL QSCYRGEGTL DLAWLKVKDI PCSSALLTID DNFCGLDMNA PLGVSEMVRG
     IPVFTEDRDR MTSVIAYVYK NHSLAFVGTK SGKLKKIRVD GPKGNALQYE TVQVVDSGPV
     LRDMAFSKDH EQLYIMSERQ LTRVPVESCG QYRSCGECLG SGDPHCGWCV LHNTCTRKER
     CERSREPRRF ASEMKQCVRL TVHPNNISVS QYNVLLVLET YNVPELSAGV NCTFEDLSEM
     DGLVIGNQIQ CYSPAAKEVP RIITENGDHH VVQLQLKSKE TGMTFASTSF VFYNCSVHNS
     CLSCVESPYR CHWCKYRHVC THGRNTCSFQ EGRVKLPEDC PQLLRVDKIL VPVEVIKPIT
     LKAKNLPQPQ SGQRGYECIL NIQGIEQRVP ALRFNSSSVQ CQNTSYSYEG MEINNLPVEL
     TVVWNGHFNI DNPAQNKVYL YKCGAMRESC GLCLKADPDF ECGWCQSPGQ CTLRQHCPAH
     ESRWLELSGA NSKCTNPRIT EIIPVTGPRE GGTKVTIRGE NLGLEFRDIA SHVKVAGVEC
     SPLVDGYIPA EQIVCEMGEA KPSQHAGFVE ICVAVCRPEF MARSSQLYYF MTLTLADLKP
     NRGPMSGGTQ VTITGTNLNA GSNVVVMFGS QPCLFHRRSP SYIICNTTSS EEVLDMKVTV
     QVDRARIRQD LVFQYVEDPT IVRIEPEWSI VSGNTPIAVW GTHLDLIQNP QIRAKHGGKE
     HINICEVLNA TEMTCQAPAL ALGPDHQSDL TERPEEFGFI LDNVQSLLIL NKTNFTYYPN
     PVFEAFSPSG ILELKPGTPI ILKGKNLIPP VAGGNVKLNY TVLVGEKPCT VTVSDVQLLC
     ESPNLIGRHK VMARVGGMEY SPGMVYIAPD SPLSLPAIVS IAVAGGLLII FIVAVLIAYK
     RKSRESDLTL KRLQMQMDNL ESRVALECKE AFAELQTDIH ELTSDLDGAG IPFLDYRTYT
     MRVLFPGIED HPVLRDLEVP GYRQERVEKG LKLFAQLINN KVFLLSFIRT LESQRSFSMR
     DRGNVASLIM TVLQSKLEYA TDVLKQLLAD LIDKNLESKN HPKLLLRRTE SVAEKMLTNW
     FTFLLYKFLK ECAGEPLFSL FCAIKQQMEK GPIDAITGEA RYSLSEDKLI RQQIEYKTLV
     LSCVSPDNVN SPEVPVKILN CDTITQVKEK ILDAIFKNVP CSHRPKAADM DLEWRQGSGA
     RMILQDEDIT TKIENDWKRL NTVAHYQVPD GSVVALVSKQ VTAYNAVNNS TVSRTSASKY
     ENMIRYTGSP DSLRSRTPMI TPDLESGVKL WHLVKNHEHG DQKEGDRGSK MVSEIYLTRL
     LATKGTLQKF VDDLFETIFS TAHRGSALPL AIKYMFDFLD EQADKHGIHD PHVRHTWKSN
     CLPLRFWVNM IKNPQFVFDI HKNSITDACL SVVAQTFMDS CSTSEHRLGK DSPSNKLLYA
     KDIPSYKNWV ERYYSDIGKM PAISDQDMNA YLAEQSRMHM NEFNTMSALS EIFSYVGKYS
     EEILGPLDHD DQCGKQKLAY KLEQVITLMS LDS
//
ID   SEPT9_MOUSE             Reviewed;         583 AA.
AC   Q80UG5; A2A6U2; A2A6U4; A2A6U6; Q3URP2; Q80TM7; Q9QYX9;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Septin-9;
DE   AltName: Full=SL3-3 integration site 1 protein;
GN   Name=Sept9; Synonyms=Kiaa0991, Sint1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX   MEDLINE=20130405; PubMed=10666245;
RX   DOI=10.1128/JVI.74.5.2161-2168.2000;
RA   Soerensen A.B., Lund A.H., Ethelberg S., Copeland N.G., Jenkins N.A.,
RA   Pedersen F.S.;
RT   "Sint1, a common integration site in SL3-3-induced T-cell lymphomas,
RT   harbors a putative proto-oncogene with homology to the septin gene
RT   family.";
RL   J. Virol. 74:2161-2168(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2),
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=22035356; PubMed=12039034; DOI=10.1016/S0378-1119(02)00406-7;
RA   Soerensen A.B., Warming S., Fuechtbauer E.-M., Pedersen F.S.;
RT   "Alternative splicing, expression, and gene structure of the septin-
RT   like putative proto-oncogene Sint1.";
RL   Gene 285:79-89(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=129; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   PROTEIN SEQUENCE OF 548-559, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17546647; DOI=10.1002/humu.20554;
RA   Sudo K., Ito H., Iwamoto I., Morishita R., Asano T., Nagata K.;
RT   "SEPT9 sequence alternations causing hereditary neuralgic amyotrophy
RT   are associated with altered interactions with SEPT4/SEPT11 and
RT   resistance to Rho/Rhotekin-signaling.";
RL   Hum. Mutat. 28:1005-1013(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30 AND SER-161, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Filament-forming cytoskeletal GTPase (By similarity).
CC       May play a role in cytokinesis (Potential).
CC   -!- SUBUNIT: Septins polymerize into heterooligomeric protein
CC       complexes that form filaments, and associate with cellular
CC       membranes, actin filaments, and microtubules. GTPase activity is
CC       required for filament formation. Interacts with SEPT2, SEPT6,
CC       SEPT7, SEPT11 and SEPT14. Interacts with RTKN and ARHGEF18 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=In an
CC       epithelial cell line, concentrates at cell-cell contact areas.
CC       After TGF-beta1 treatment and induction of epithelial to
CC       mesenchymal transition, colocalizes with actin stress fibers.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q80UG5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80UG5-2; Sequence=VSP_012341;
CC       Name=3;
CC         IsoId=Q80UG5-3; Sequence=VSP_012342;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined except
CC       muscle. Isoforms are differentially expressed in testes, kidney,
CC       liver, heart, spleen and brain.
CC   -!- DEVELOPMENTAL STAGE: At 8 dpc mainly expressed in the lateral
CC       plate mesoderm and the somites. Beginning at 9 dpc the lateral
CC       plate expression is clearly focused in the developing fore- and
CC       hindlimb buds. In the cephalic region, expressed in the first and
CC       second branchial arch, in the nasal process and around the otic
CC       pit. At 9.5 dpc strongest expression is observed in the mesenchyme
CC       of the branchial arches, the limbs, and the developing dorsal root
CC       ganglia. Weak to intermediate expression is found in the neural
CC       epithelium. Expression is seen in the newly formed somites in the
CC       tail bud of older embryos. During formation of the digits,
CC       expression seems to outline the surviving tissue bordering it
CC       towards the apoptotic webbing. Expression is seen in the
CC       developing outer ear and in several areas known to be regulated by
CC       intensive epithelial mesenchymal interactions, like the viscera
CC       follicles and the developing mammary glands.
CC   -!- DISEASE: Note=Putative proto-oncogene involved in T-cell
CC       lymphomagenesis. May play a role in leukemogenesis.
CC   -!- MISCELLANEOUS: Targeted by proviral insertion in T-cell lymphomas
CC       induced by the murine retrovirus SL3-3 MuLV.
CC   -!- SIMILARITY: Belongs to the septin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65697.2; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AJ250723; CAB59833.1; -; mRNA.
DR   EMBL; AF450142; AAL50685.1; -; Genomic_DNA.
DR   EMBL; AF450141; AAL50685.1; JOINED; Genomic_DNA.
DR   EMBL; AK031757; BAC27538.1; -; mRNA.
DR   EMBL; AK122415; BAC65697.2; ALT_INIT; mRNA.
DR   EMBL; AK141312; BAE24646.1; -; mRNA.
DR   EMBL; AL603868; CAM13312.1; -; Genomic_DNA.
DR   EMBL; AL611935; CAM13312.1; JOINED; Genomic_DNA.
DR   EMBL; AL645975; CAM13312.1; JOINED; Genomic_DNA.
DR   EMBL; AL645975; CAM15613.1; -; Genomic_DNA.
DR   EMBL; AL603868; CAM15613.1; JOINED; Genomic_DNA.
DR   EMBL; AL611935; CAM15613.1; JOINED; Genomic_DNA.
DR   EMBL; AL611935; CAM19703.1; -; Genomic_DNA.
DR   EMBL; AL603868; CAM19703.1; JOINED; Genomic_DNA.
DR   EMBL; AL645975; CAM19703.1; JOINED; Genomic_DNA.
DR   EMBL; BC046524; AAH46524.1; -; mRNA.
DR   IPI; IPI00457611; -.
DR   IPI; IPI00467599; -.
DR   IPI; IPI00515330; -.
DR   RefSeq; NP_001106958.1; NM_001113486.1.
DR   RefSeq; NP_001106959.1; NM_001113487.1.
DR   RefSeq; NP_001106960.1; NM_001113488.1.
DR   RefSeq; NP_059076.1; NM_017380.2.
DR   UniGene; Mm.38450; -.
DR   UniGene; Mm.451420; -.
DR   ProteinModelPortal; Q80UG5; -.
DR   SMR; Q80UG5; 293-564.
DR   STRING; Q80UG5; -.
DR   PhosphoSite; Q80UG5; -.
DR   PRIDE; Q80UG5; -.
DR   Ensembl; ENSMUST00000019038; ENSMUSP00000019038; ENSMUSG00000059248.
DR   Ensembl; ENSMUST00000093907; ENSMUSP00000091435; ENSMUSG00000059248.
DR   Ensembl; ENSMUST00000106351; ENSMUSP00000101958; ENSMUSG00000059248.
DR   Ensembl; ENSMUST00000106354; ENSMUSP00000101961; ENSMUSG00000059248.
DR   GeneID; 53860; -.
DR   KEGG; mmu:53860; -.
DR   UCSC; uc007mnd.1; mouse.
DR   UCSC; uc007mne.1; mouse.
DR   UCSC; uc007mnf.1; mouse.
DR   CTD; 53860; -.
DR   MGI; MGI:1858222; Sept9.
DR   GeneTree; ENSGT00590000082767; -.
DR   HOGENOM; HBG715249; -.
DR   HOVERGEN; HBG098529; -.
DR   InParanoid; Q80UG5; -.
DR   OMA; EYQVNGR; -.
DR   OrthoDB; EOG4WDDBR; -.
DR   PhylomeDB; Q80UG5; -.
DR   NextBio; 310701; -.
DR   ArrayExpress; Q80UG5; -.
DR   Bgee; Q80UG5; -.
DR   CleanEx; MM_SEPT9; -.
DR   Genevestigator; Q80UG5; -.
DR   GermOnline; ENSMUSG00000059248; Mus musculus.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   InterPro; IPR000038; Cell_Div_GTP-bd.
DR   PANTHER; PTHR18884; Cell_Div_GTP_bd; 1.
DR   Pfam; PF00735; Septin; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell cycle; Cell division;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding;
KW   Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1    583       Septin-9.
FT                                /FTId=PRO_0000173536.
FT   NP_BIND     303    310       GTP (By similarity).
FT   NP_BIND     443    451       GTP (By similarity).
FT   BINDING     337    337       GTP (By similarity).
FT   BINDING     363    363       GTP; via amide nitrogen (By similarity).
FT   BINDING     499    499       GTP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     514    514       GTP (By similarity).
FT   MOD_RES      30     30       Phosphoserine.
FT   MOD_RES      42     42       Phosphothreonine (By similarity).
FT   MOD_RES      49     49       Phosphothreonine (By similarity).
FT   MOD_RES      80     80       Phosphoserine (By similarity).
FT   MOD_RES      82     82       Phosphoserine (By similarity).
FT   MOD_RES      85     85       Phosphoserine.
FT   MOD_RES      89     89       Phosphoserine (By similarity).
FT   MOD_RES     143    143       Phosphothreonine (By similarity).
FT   MOD_RES     161    161       Phosphoserine.
FT   MOD_RES     168    168       Phosphothreonine (By similarity).
FT   MOD_RES     276    276       Phosphotyrosine (By similarity).
FT   MOD_RES     350    350       N6-acetyllysine (By similarity).
FT   MOD_RES     429    429       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1    249       Missing (in isoform 2).
FT                                /FTId=VSP_012341.
FT   VAR_SEQ       1     25       MKKSYSGVTRTSSGRLRRLADPTGP -> MSDPAVNAQLDG
FT                                IISDFE (in isoform 3).
FT                                /FTId=VSP_012342.
SQ   SEQUENCE   583 AA;  65575 MW;  174D2F1E8EA382FC CRC64;
     MKKSYSGVTR TSSGRLRRLA DPTGPALKRS FEVEEIEPPN STPPRRVQTP LLRATVASSS
     QKFQDLGVKN SEPAARLVDS LSQRSPKPSL RRVELAGAKA PEPMSRRTEI SIDISSKQVE
     STASAAGPSR FGLKRAEVLG HKTPEPVPRR TEITIVKPQE SVLRRVETPA SKIPEGSAVP
     ATDAAPKRVE IQVPKPAEAP NCPLPSQTLE NSEAPMSQLQ SRLEPRPSVA EVPYRNQEDS
     EVTPSCVGDM ADNPRDAMLK QAPASRNEKA PMEFGYVGID SILEQMRRKA MKQGFEFNIM
     VVGQSGLGKS TLINTLFKSK ISRKSVQPTS EERIPKTIEI KSITHDIEEK GVRMKLTVID
     TPGFGDHINN ENCWQPIMKF INDQYEKYLQ EEVNINRKKR IPDTRVHCCL YFIPATGHSL
     RPLDIEFMKR LSKVVNIVPV IAKADTLTLE ERVYFKQRIT ADLLSNGIDV YPQKEFDEDA
     EDRLVNEKFR EMIPFAVVGS DHEYQVNGKR ILGRKTKWGT IEVENTTHCE FAYLRDLLIR
     THMQNIKDIT SNIHFEAYRV KRLNEGNSAM ANGIEKEPEA QEM
//
ID   RB3GP_MOUSE             Reviewed;         981 AA.
AC   Q80UJ7; Q6A0D7; Q8C4Y0; Q8C679; Q8C6A5; Q8K324;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Rab3 GTPase-activating protein catalytic subunit;
DE   AltName: Full=RAB3 GTPase-activating protein 130 kDa subunit;
DE   AltName: Full=Rab3-GAP p130;
DE            Short=Rab3-GAP;
GN   Name=Rab3gap1; Synonyms=Kiaa0066, Rab3gap;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15696165; DOI=10.1038/ng1517;
RA   Aligianis I.A., Johnson C.A., Gissen P., Chen D., Hampshire D.,
RA   Hoffmann K., Maina E.N., Morgan N.V., Tee L., Morton J.,
RA   Ainsworth J.R., Horn D., Rosser E., Cole T.R.P., Stolte-Dijkstra I.,
RA   Fieggen K., Clayton-Smith J., Megarbane A., Shield J.P.,
RA   Newbury-Ecob R., Dobyns W.B., Graham J.M., Kjaer K.W., Warburg M.,
RA   Bond J., Trembath R.C., Harris L.W., Takai Y., Mundlos S.,
RA   Tannahill D., Woods C.G., Maher E.R.;
RT   "Mutations of the catalytic subunit of RAB3GAP cause Warburg Micro
RT   syndrome.";
RL   Nat. Genet. 37:221-223(2005).
CC   -!- FUNCTION: Probable catalytic subunit of a GTPase activating
CC       protein that has specificity for Rab3 subfamily (RAB3A, RAB3B,
CC       RAB3C and RAB3D). Rab3 proteins are involved in regulated
CC       exocytosis of neurotransmitters and hormones. Specifically
CC       converts active Rab3-GTP to the inactive form Rab3-GDP. Required
CC       for normal eye and brain development. May participate in
CC       neurodevelopmental processes such as proliferation, migration and
CC       differentiation before synapse formation, and non-synaptic
CC       vesicular release of neurotransmitters (By similarity).
CC   -!- SUBUNIT: The Rab3 GTPase-activating complex is a heterodimer
CC       composed of RAB3GAP and RAB3-GAP150. The Rab3 GTPase-activating
CC       complex interacts with DMXL2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=In neurons,
CC       it is enriched in the synaptic soluble fraction (By similarity).
CC   -!- TISSUE SPECIFICITY: In the eye, it is highly expressed within the
CC       lens, particularly in the anterior lens epithelium and in a ring
CC       corresponding to the equatorial region where anterior cells are
CC       differentiating into lens fibers. Also highly expressed in the
CC       retina.
CC   -!- DEVELOPMENTAL STAGE: From E10 to E12, it is weakly expressed
CC       throughout the embryo. At E14.5, it is predominantly expressed in
CC       a number of organ systems, including the central and peripheral
CC       nervous systems.
CC   -!- SIMILARITY: Belongs to the Rab3-GAP catalytic subunit family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32159.1; Type=Erroneous initiation;
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DR   EMBL; AK172881; BAD32159.1; ALT_INIT; mRNA.
DR   EMBL; AK076244; BAC36271.1; -; mRNA.
DR   EMBL; AK076399; BAC36323.1; -; mRNA.
DR   EMBL; AK080432; BAC37915.1; -; mRNA.
DR   EMBL; BC028996; AAH28996.1; -; mRNA.
DR   EMBL; BC046297; AAH46297.1; -; mRNA.
DR   IPI; IPI00469255; -.
DR   RefSeq; NP_848805.2; NM_178690.4.
DR   UniGene; Mm.476343; -.
DR   STRING; Q80UJ7; -.
DR   PhosphoSite; Q80UJ7; -.
DR   PRIDE; Q80UJ7; -.
DR   Ensembl; ENSMUST00000037649; ENSMUSP00000042070; ENSMUSG00000036104.
DR   GeneID; 226407; -.
DR   KEGG; mmu:226407; -.
DR   CTD; 226407; -.
DR   MGI; MGI:2445001; Rab3gap1.
DR   GeneTree; ENSGT00390000006705; -.
DR   HOVERGEN; HBG079116; -.
DR   InParanoid; Q80UJ7; -.
DR   OrthoDB; EOG495ZR7; -.
DR   ArrayExpress; Q80UJ7; -.
DR   Bgee; Q80UJ7; -.
DR   CleanEx; MM_RAB3GAP1; -.
DR   Genevestigator; Q80UJ7; -.
DR   GermOnline; ENSMUSG00000036104; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
PE   2: Evidence at transcript level;
KW   Cytoplasm; GTPase activation; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    981       Rab3 GTPase-activating protein catalytic
FT                                subunit.
FT                                /FTId=PRO_0000191656.
FT   MOD_RES     579    579       Phosphoserine (By similarity).
FT   MOD_RES     581    581       Phosphoserine (By similarity).
FT   MOD_RES     590    590       Phosphoserine (By similarity).
FT   CONFLICT     56     56       G -> D (in Ref. 2; BAC36271).
FT   CONFLICT     64     64       E -> K (in Ref. 2; BAC36271).
FT   CONFLICT     71     71       R -> K (in Ref. 2; BAC36271).
FT   CONFLICT     88     88       G -> R (in Ref. 2; BAC36271/BAC36323/
FT                                BAC37915).
FT   CONFLICT    106    106       C -> S (in Ref. 2; BAC36271).
FT   CONFLICT    116    117       HC -> TS (in Ref. 2; BAC36271).
FT   CONFLICT    124    124       L -> Q (in Ref. 2; BAC36271).
FT   CONFLICT    175    175       R -> P (in Ref. 2; BAC36271).
FT   CONFLICT    216    217       IG -> LS (in Ref. 2; BAC37915).
FT   CONFLICT    321    321       Q -> H (in Ref. 2; BAC36271).
FT   CONFLICT    619    619       R -> P (in Ref. 2; BAC36323).
SQ   SEQUENCE   981 AA;  110098 MW;  32AAEC4AEEFB00AC CRC64;
     MAADSEPESE VFEITDFTTA SEWERFISKV EEVLNDWKLI GPSLGKPLEK GIFTSGTWEE
     RSDEISFADF RFSVTHHYLV QESPDKEGKD EELEDAIPQS MQDLLCMNND FPPRAHCLVR
     WYGLREFVVI APAAHSDAVL SESKCNLLLS SISIALGNTG CQVPLFVQIH HKWRRMYMGE
     CQGPGVRTDF EMVHLRKVPS QYTHLSGLLD IFKSKIGCPL TPLPPVSIAI RLTYVLQDWQ
     QYFWPQQPPD IDALVGGEVG GLEFGKLPFG ACEDPISELH LATTWPHLTE GIIVDNDVYS
     DLDPVQAPHW SVRVRKADNP QCLLGDFVTE FLKICRRKES TDEILGRSTF EEEGREVADI
     THALSKLTEP APVPIHKLSV SNMVHTAKKK IRKHRGEESP LNSDVLNTIL LFLFPDAVSE
     KPLDGTTSID NSIPAPEAGD YTLYNQFKSA PSDSLTYKLA LCLCMINFYH GGLKGVAHLW
     QEFVLEMRFR WENNFLIPGL ASGSPDLRCC LLHQKLQMLN CCIERKKARD EGKKTSLSDS
     TTSAYPGDAG KTGGQLGLDH LRDTEKEKGE VGKSWDSWSD SEEEFFECLS DTEDLKGNGQ
     ESGKKGGPKE MANLKPEGRL HQHGKLTLLH NGEPLYIPVT QEPAPMTEDL LEEQSEVLAK
     LGTSAEGAHL RARMQSACLL SDMESFKAAN PGCFLEDFVR WYSPRDYIEE EVTDEKGNVV
     LKGELSARMK IPSNMWVEAW ETAKPVPARR QRRLFDDTRE AEKVLHYLAM QKPADLARHL
     LPCVIHAAVL KVKEEESLEN IPSVKKIIKQ IIAHSSKVLH FPNPEDKKLE EIILQITTVE
     AIIARARSLK AKFGTEKCEH EEEKEGLERF VSCLLEQPEV SVTGAGRGHA GRIIHKLFVN
     AQRAAAVALP EEELKKSGCP EERRQTLVSD FPPPAGRELI LRATVPRPAP YSKALPQRMY
     SVLTKEDFRL AGAFSSDTSF F
//
ID   Q80UM4_MOUSE            Unreviewed;       775 AA.
AC   Q80UM4;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   SubName: Full=Protein tyrosine phosphatase, non-receptor type 12;
DE   SubName: Full=Protein tyrosine phosphatase, non-receptor type 12, isoform CRA_c;
GN   Name=Ptpn12; ORFNames=mCG_6416;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Mouse;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [11]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [12]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC051980; AAH51980.1; -; mRNA.
DR   EMBL; AK154107; BAE32381.1; -; mRNA.
DR   EMBL; CH466586; EDL03216.1; -; Genomic_DNA.
DR   IPI; IPI00387213; -.
DR   RefSeq; NP_035333.2; NM_011203.2.
DR   UniGene; Mm.319117; -.
DR   HSSP; P29352; 1JEG.
DR   ProteinModelPortal; Q80UM4; -.
DR   SMR; Q80UM4; 3-300.
DR   STRING; Q80UM4; -.
DR   PhosphoSite; Q80UM4; -.
DR   PRIDE; Q80UM4; -.
DR   Ensembl; ENSMUST00000030556; ENSMUSP00000030556; ENSMUSG00000028771.
DR   GeneID; 19248; -.
DR   KEGG; mmu:19248; -.
DR   UCSC; uc008woh.1; mouse.
DR   CTD; 19248; -.
DR   MGI; MGI:104673; Ptpn12.
DR   GeneTree; ENSGT00600000084181; -.
DR   HOVERGEN; HBG007666; -.
DR   InParanoid; Q80UM4; -.
DR   OMA; TVWQDND; -.
DR   PhylomeDB; Q80UM4; -.
DR   NextBio; 296078; -.
DR   ArrayExpress; Q80UM4; -.
DR   Bgee; Q80UM4; -.
DR   Genevestigator; Q80UM4; -.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR012266; Tyr_Pase_non-rcpt_typ-12.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PIRSF; PIRSF000932; Tyr-Ptase_nr12; 1.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00194; PTPc; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Protein phosphatase; Receptor.
SQ   SEQUENCE   775 AA;  86526 MW;  ED1A7A577CE4352C CRC64;
     MEQVEILRRF IQRVQAMKSP DHNGEDNFAR DFMRLRRLST KYRTEKIYPT ATGEKEENVK
     KNRYKDILPF DHSRVKLTLK TPSQDSDYIN ANFIKGVYGP KAYVATQGPL ANTVIDFWRM
     IWEYNVVIIV MACREFEMGR KKCERYWPLY GEDPITFAPF KISCENEQAR TDYFIRTLLL
     EFQNESRRLY QFHYVNWPDH DVPSSFDSIL DMISLMRKYQ EHEDVPICIH CSAGCGRTGA
     ICAIDYTWNL LKAGKIPEEF NVFNLIQEMR TQRHSAVQTK EQYELVHRAI AQLFEKQLQL
     YEIHGAQKIA DGNEITTGTM VSSIDSEKQD SPPPKPPRTR SCLVEGDAKE EILQPPEPHP
     VPPILTPSPP SAFPTVTTVW QDSDRYHPKP VLHMASPEQH PADLNRSYDK SADPMGKSES
     AIEHIDKKLE RNLSFEIKKV PLQEGPKSFD GNTLLNRGHA IKIKSASSSV VDRTSKPQEL
     SAGALKVDDV SQNSCADCSA AHSHRAAESS EESQSNSHTP PRPDCLPLDK KGHVTWSLHG
     PENATPVPDS PDGKSPDNHS QTLKTVSSTP NSTAEEEAHD LTEHHNSSPL LKAPLSFTNP
     LHSDDSDSDG GSSDGAVTRN KTSISTASAT VSPASSAESA CTRRVLPMSI ARQEVAGTPH
     SGAEKDADVS EESPPPLPER TPESFVLADM PVRPEWHELP NQEWSEQRES EGLTTSGNEK
     HDAGGIHTEA SADSPPAFSD KKDQITKSPA EVTDIGFGNR CGKPKGPREP PSEWT
//
ID   S20A2_MOUSE             Reviewed;         656 AA.
AC   Q80UP8; Q3TBZ8; Q9ES96;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Sodium-dependent phosphate transporter 2;
DE   AltName: Full=Phosphate transporter 2;
DE            Short=PiT-2;
DE   AltName: Full=Solute carrier family 20 member 2;
DE   AltName: Full=Type III sodium-dependent phosphate transporter;
GN   Name=Slc20a2; Synonyms=Pit2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION AS SODIUM-PHOSPHATE SYMPORTER,
RP   AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Intestine;
RX   MEDLINE=20459441; PubMed=11003594;
RA   Bai L., Collins J.F., Ghishan F.K.;
RT   "Cloning and characterization of a type III Na-dependent phosphate
RT   cotransporter from mouse intestine.";
RL   Am. J. Physiol. 279:C1135-C1143(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Sodium-phosphate symporter which seems to play a
CC       fundamental housekeeping role in phosphate transport by absorbing
CC       phosphate from interstitial fluid for normal cellular functions
CC       such as cellular metabolism, signal transduction, and nucleic acid
CC       and lipid synthesis. In vitro, sodium-dependent phosphate uptake
CC       is not siginificantly affected by acidic and alkaline conditions,
CC       however sodium-independent phosphate uptake occurs at acidic
CC       conditions. May play a role in extracellular matrix, cartilage and
CC       vascular calcification. Functions as a retroviral receptor (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed including intestine, kidney,
CC       heart, liver, brain, testis and skin. Expressed througout the
CC       vertcal crypt-axial axis of intestinal epithelium.
CC   -!- SIMILARITY: Belongs to the inorganic phosphate transporter (PiT)
CC       (TC 2.A.20) family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF196476; AAG28493.1; -; mRNA.
DR   EMBL; AK157206; BAE33999.1; -; mRNA.
DR   EMBL; AK170985; BAE42159.1; -; mRNA.
DR   EMBL; BC046510; AAH46510.1; -; mRNA.
DR   IPI; IPI00311767; -.
DR   UniGene; Mm.323901; -.
DR   UniGene; Mm.378231; -.
DR   STRING; Q80UP8; -.
DR   PRIDE; Q80UP8; -.
DR   Ensembl; ENSMUST00000067786; ENSMUSP00000065935; ENSMUSG00000037656.
DR   UCSC; uc009ldf.1; mouse.
DR   MGI; MGI:97851; Slc20a2.
DR   GeneTree; ENSGT00390000014879; -.
DR   HOGENOM; HBG681698; -.
DR   HOVERGEN; HBG053358; -.
DR   InParanoid; Q80UP8; -.
DR   OrthoDB; EOG40S0F7; -.
DR   ArrayExpress; Q80UP8; -.
DR   Bgee; Q80UP8; -.
DR   Genevestigator; Q80UP8; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0044419; P:interspecies interaction between organisms; IEA:UniProtKB-KW.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001204; Phos_transporter.
DR   PANTHER; PTHR11101; Phos_transporter; 1.
DR   Pfam; PF01384; PHO4; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Host-virus interaction; Ion transport;
KW   Membrane; Phosphate transport; Phosphoprotein; Receptor; Sodium;
KW   Sodium transport; Symport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    656       Sodium-dependent phosphate transporter 2.
FT                                /FTId=PRO_0000341269.
FT   TOPO_DOM      1      5       Extracellular (Potential).
FT   TRANSMEM      6     26       Helical; (Potential).
FT   TOPO_DOM     27     46       Cytoplasmic (Potential).
FT   TRANSMEM     47     67       Helical; (Potential).
FT   TOPO_DOM     68     86       Extracellular (Potential).
FT   TOPO_DOM    108    109       Cytoplasmic (Potential).
FT   TRANSMEM    110    130       Helical; (Potential).
FT   TOPO_DOM    131    142       Extracellular (Potential).
FT   TRANSMEM    143    163       Helical; (Potential).
FT   TOPO_DOM    164    190       Cytoplasmic (Potential).
FT   TRANSMEM    191    211       Helical; (Potential).
FT   TOPO_DOM    212    213       Extracellular (Potential).
FT   TRANSMEM    214    234       Helical; (Potential).
FT   TOPO_DOM    235    483       Cytoplasmic (Potential).
FT   TRANSMEM    484    504       Helical; (Potential).
FT   TOPO_DOM    505    531       Extracellular (Potential).
FT   TRANSMEM    532    552       Helical; (Potential).
FT   TOPO_DOM    553    572       Cytoplasmic (Potential).
FT   TRANSMEM    573    587       Helical; (Potential).
FT   TOPO_DOM    588    594       Extracellular (Potential).
FT   TRANSMEM    595    610       Helical; (Potential).
FT   TOPO_DOM    611    622       Cytoplasmic (Potential).
FT   TRANSMEM    623    643       Helical; (Potential).
FT   TOPO_DOM    644    655       Extracellular (Potential).
FT   MOD_RES     268    268       Phosphoserine.
FT   MOD_RES     377    377       Phosphotyrosine (By similarity).
FT   CARBOHYD     81     81       N-linked (GlcNAc...) (Potential).
FT   CONFLICT     55     55       E -> A (in Ref. 1; AAG28493).
FT   CONFLICT    123    123       I -> T (in Ref. 1; AAG28493).
FT   CONFLICT    387    387       T -> A (in Ref. 1; AAG28493).
FT   CONFLICT    487    487       L -> F (in Ref. 1; AAG28493).
FT   CONFLICT    614    614       A -> T (in Ref. 2; BAE42159).
FT   CONFLICT    644    656       LLMYICGLFSSSR -> SFMYGILPYV (in Ref. 1;
FT                                AAG28493).
SQ   SEQUENCE   656 AA;  70852 MW;  37D1EBAFCD5CEA72 CRC64;
     MAMDGYLWMV ILGFIIAFIL AFSVGANDVA NSFGTAVGSG VVTLRQACIL ASVFETTGSV
     LLGAKVGETI RKGIIDVNLY NETVETLMAG EVSAMVGSAV WQLIASFLRL PISGTHCIVG
     STIGFSLVAI GPKGVQWMEL VKIVASWFIS PLLSGFMSGV LFILIRMFIL TKEDPVPNGL
     QALPLFYAAT IAINVFSIMY TGAPVLGLSL PIWAIALISF GVALLFAFFV WLFVCPWMKR
     KIAGRLEKES ALSRASDESL RKVQEAESPG FKELPGAKPS DDSAVPLTSL AGEAVGASEG
     TSAGNHPRAS YGRALSMTHG SAKSPISNGT FGFEGHMRND GHVYHTVHKD SGLYKDLLHK
     IHVDRGSEEK PTQENNYRLL RRNNSYTCYT AAICGMPVHT TFRASDTSSA PEDSEKLVGD
     SVSYSKKRLR YDSYSSYCNA VAEAEIEAEE GGVEMRLASE LADPDRPHED PTEEEKEEKD
     SAEVHLLFHF LQVLTACFGS FAHGGNDVSN AIGPLVALWL IYQQGGVTQE AATPVWLLFY
     GGVGICTGLW VWGRRVIQTM GKDLTPITPS SGFTIELASA FTVVIASNIG LPVSTTHCKV
     GSVVAVGWIR SRKAVDWRLF RNIFVAWFVT VPVAGLFSAA IMALLMYICG LFSSSR
//
ID   PGRC2_MOUSE             Reviewed;         217 AA.
AC   Q80UU9;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Membrane-associated progesterone receptor component 2;
GN   Name=Pgrmc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-217.
RC   STRAIN=129; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND THR-205, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Receptor for steroids (Potential).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- DOMAIN: The cytochrome b5 heme-binding domain lacks the conserved
CC       iron-binding His residues at positions 131 and 155 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome b5 family. MAPR subfamily.
CC   -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC100511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC044759; AAH44759.1; -; mRNA.
DR   IPI; IPI00351206; -.
DR   RefSeq; NP_081834.1; NM_027558.1.
DR   UniGene; Mm.40321; -.
DR   ProteinModelPortal; Q80UU9; -.
DR   SMR; Q80UU9; 95-195.
DR   STRING; Q80UU9; -.
DR   PhosphoSite; Q80UU9; -.
DR   PRIDE; Q80UU9; -.
DR   Ensembl; ENSMUST00000058578; ENSMUSP00000056643; ENSMUSG00000049940.
DR   GeneID; 70804; -.
DR   KEGG; mmu:70804; -.
DR   UCSC; uc008pce.1; mouse.
DR   CTD; 70804; -.
DR   MGI; MGI:1918054; Pgrmc2.
DR   eggNOG; maNOG17116; -.
DR   GeneTree; ENSGT00530000063049; -.
DR   HOVERGEN; HBG059971; -.
DR   InParanoid; Q80UU9; -.
DR   OMA; RWRAVMA; -.
DR   OrthoDB; EOG4SXNDQ; -.
DR   PhylomeDB; Q80UU9; -.
DR   NextBio; 332296; -.
DR   ArrayExpress; Q80UU9; -.
DR   Bgee; Q80UU9; -.
DR   CleanEx; MM_PGRMC2; -.
DR   Genevestigator; Q80UU9; -.
DR   GermOnline; ENSMUSG00000049940; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR   InterPro; IPR001199; Cyt_B5.
DR   Gene3D; G3DSA:3.10.120.10; Cyt_B5; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   SUPFAM; SSF55856; Cyt_B5; 1.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; FALSE_NEG.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Lipid-binding; Membrane; Phosphoprotein; Receptor; Steroid-binding;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    217       Membrane-associated progesterone receptor
FT                                component 2.
FT                                /FTId=PRO_0000121744.
FT   TRANSMEM     40     62       Helical; (Potential).
FT   DOMAIN       96    195       Cytochrome b5 heme-binding.
FT   MOD_RES      84     84       Phosphoserine (By similarity).
FT   MOD_RES      98     98       Phosphoserine (By similarity).
FT   MOD_RES     202    202       Phosphoserine.
FT   MOD_RES     204    204       Phosphotyrosine (By similarity).
FT   MOD_RES     205    205       Phosphothreonine.
SQ   SEQUENCE   217 AA;  23334 MW;  0291B0EFE8AD3403 CRC64;
     MAAGDGDVKL STLGSGGESG GDGSPGGAGA TAARSSWVAA LLATGGEMLL NVALVALVLL
     GAYRLWVRWG RRGLCSGPGA GEESPAATLP RMKKRDFSLE QLRQYDGART PRILLAVNGK
     VFDVTKGSKF YGPAGPYGIF AGRDASRGLA TFCLDKDALR DEYDDLSDLN AVQMESVREW
     EMQFKEKYDY VGRLLKPGEE PSEYTDEEDT KDHSKQD
//
ID   KCMF1_MOUSE             Reviewed;         381 AA.
AC   Q80UY2; Q9WUM2;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=E3 ubiquitin-protein ligase KCMF1;
DE            EC=6.3.2.-;
DE   AltName: Full=Differentially expressed in branching tubulogenesis 91;
DE            Short=Debt-91;
GN   Name=Kcmf1; Synonyms=Debt91;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INDUCTION, TISSUE SPECIFICITY,
RP   AND DEVELOPMENTAL STAGE.
RX   MEDLINE=22694172; PubMed=12810064; DOI=10.1016/S0006-291X(03)00875-1;
RA   Li Z., Stuart R.O., Eraly S.A., Gittes G., Beier D.R., Nigam S.K.;
RT   "Debt91, a putative zinc finger protein differentially expressed
RT   during epithelial morphogenesis.";
RL   Biochem. Biophys. Res. Commun. 306:623-628(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Has intrinsic E3 ubiquitin ligase activity and promotes
CC       ubiquitination (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80UY2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80UY2-2; Sequence=VSP_035227;
CC   -!- TISSUE SPECIFICITY: Testis, liver, kidney, heart and skeletal
CC       muscle.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic development,
CC       with much higher expression after day 15, when many organs
CC       including the kidney are undergoing extensive branching
CC       morphogenesis.
CC   -!- INDUCTION: Up-regulated during growth factor-induced branching
CC       tubulogenesis.
CC   -!- SIMILARITY: Belongs to the KCMF1 family.
CC   -!- SIMILARITY: Contains 1 C2H2-type zinc finger.
CC   -!- SIMILARITY: Contains 1 ZZ-type zinc finger.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF143859; AAD31040.1; -; mRNA.
DR   EMBL; AK142436; BAE25063.1; -; mRNA.
DR   EMBL; BC043330; AAH43330.1; -; mRNA.
DR   IPI; IPI00395040; -.
DR   IPI; IPI00848966; -.
DR   RefSeq; NP_062689.2; NM_019715.2.
DR   UniGene; Mm.29194; -.
DR   ProteinModelPortal; Q80UY2; -.
DR   SMR; Q80UY2; 2-58.
DR   IntAct; Q80UY2; 1.
DR   PhosphoSite; Q80UY2; -.
DR   PRIDE; Q80UY2; -.
DR   Ensembl; ENSMUST00000068697; ENSMUSP00000064410; ENSMUSG00000055239.
DR   GeneID; 74287; -.
DR   KEGG; mmu:74287; -.
DR   UCSC; uc009cjd.1; mouse.
DR   CTD; 74287; -.
DR   MGI; MGI:1921537; Kcmf1.
DR   eggNOG; roNOG10489; -.
DR   GeneTree; ENSGT00510000047171; -.
DR   HOGENOM; HBG715572; -.
DR   HOVERGEN; HBG101229; -.
DR   InParanoid; Q80UY2; -.
DR   OMA; QQTIQNS; -.
DR   OrthoDB; EOG4JT066; -.
DR   NextBio; 340352; -.
DR   ArrayExpress; Q80UY2; -.
DR   Bgee; Q80UY2; -.
DR   Genevestigator; Q80UY2; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR008598; Di19_RING_finger_144.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR000433; Znf_ZZ.
DR   Pfam; PF05605; Di19; 1.
DR   Pfam; PF00569; ZZ; 1.
DR   SMART; SM00355; ZnF_C2H2; 1.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; FALSE_NEG.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Ligase; Metal-binding;
KW   Phosphoprotein; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    381       E3 ubiquitin-protein ligase KCMF1.
FT                                /FTId=PRO_0000349220.
FT   ZN_FING       3     50       ZZ-type.
FT   ZN_FING      78    101       C2H2-type.
FT   COILED      224    259       Potential.
FT   COMPBIAS    333    336       Poly-Ser.
FT   COMPBIAS    376    380       Poly-Pro.
FT   MOD_RES       2      2       Phosphoserine (By similarity).
FT   VAR_SEQ       1     85       Missing (in isoform 2).
FT                                /FTId=VSP_035227.
SQ   SEQUENCE   381 AA;  41791 MW;  4A15FC5CF60CF246 CRC64;
     MSRHEGVSCD ACLKGNFRGR RYKCLICYDY DLCASCYESG ATTTRHTTDH PMQCILTRVD
     FDLYYGGEAF SVEQPQSFTC PYCGKMGYTE TSLQEHVTSE HAETSTEVIC PICAALPGGD
     PNHVTDDFAA HLTLEHRAPR DLDESSGVRH VRRMFHPGRG LGGPRARRSN MHFTSSSTGG
     LSSSQSSYSP SSREAMDPIA ELLSQLSGVR RSAGGQLNSS GPSASQLQQL QMQLQLERQH
     AQAARQQLET ARNASRRTNT SSVTTTITQA TATANTANTE NSPQALHNSQ FLLTRLNDPK
     MSEAERQSME SERADRSLFV QELLLSTLVR EESSSSDEDD RGEMADFGAM GCVDIMPLDV
     ALENLNLKES NKGNEPPPPP L
//
ID   Q80V17_MOUSE            Unreviewed;       849 AA.
AC   Q80V17;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   SubName: Full=Setd1a protein;
GN   Name=Setd1a; Synonyms=BC010250;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NMRI; TISSUE=Mammary tumor. WAP-Tag model. 5 months old;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains 1 SET domain.
CC   -!- SIMILARITY: Contains 1 post-SET domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC049883; AAH49883.1; -; mRNA.
DR   IPI; IPI00323238; -.
DR   UniGene; Mm.435494; -.
DR   ProteinModelPortal; Q80V17; -.
DR   SMR; Q80V17; 709-849.
DR   STRING; Q80V17; -.
DR   PRIDE; Q80V17; -.
DR   Ensembl; ENSMUST00000047075; ENSMUSP00000047672; ENSMUSG00000042308.
DR   Ensembl; ENSMUST00000047157; ENSMUSP00000037600; ENSMUSG00000042308.
DR   MGI; MGI:2446244; Setd1a.
DR   eggNOG; roNOG12683; -.
DR   HOGENOM; HBG283305; -.
DR   HOVERGEN; HBG067119; -.
DR   InParanoid; Q80V17; -.
DR   OrthoDB; EOG4JT04S; -.
DR   ArrayExpress; Q80V17; -.
DR   Bgee; Q80V17; -.
DR   Genevestigator; Q80V17; -.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR015722; Histone-lysine_MeTfrase.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   PANTHER; PTHR22884:SF10; MLL; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS50868; POST_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; Nucleus; Transferase.
SQ   SEQUENCE   849 AA;  93293 MW;  0BABB1A610F7888A CRC64;
     MKLKEPGMLS LVDWAKSGGI TGIEAFAFGS GLRGALRLPS FKVKRKEPSE ISEASEEKRP
     RPSTPAEEDE DDPEREKEAG EPGRPGTKPP KRDEERGKTQ GKHRKSFTLD SEGEEASQES
     SSEKDEDDDD EDEEDEEQEE AVDATKKEAE ASDGEDEDSD SSSQCSLYAD SDGENGSTSD
     SESGSSSSSS SSSSSSSSSS SSESSSEEEE QSAVIPSASP PREVPEPLPA PDEKPETDGL
     VDSPVMPLSE KETLPTQPAG PAEEPPPSVP QPPAEPPAGP PDAAPRLDER PSSPIPLLPP
     PKKRRKTVSF SAAEEAPVPE PSTAAPLQAK SSGPVSRKVP RVVERTIRNL PLDHASLVKS
     WPEEVARGGR NRAGGRVRST EEEEATESGT EVDLAVLADL ALTPARRGLA TLPTGDDSEA
     TETSDEAERP SPLLSHILLE HNYALAIKPP PTTPAPRPLE PAPALAALFS SPADEVLEAP
     EVVVAEAEEP KQQLQQQHPE QEGEEEEEDE EEESESSESS SSSSSDEEGA IRRRSLRSHT
     RRRRPPLPPP PPPPPSFEPR SEFEQMTILY DIWNSGLDLE DMSYLRLTYE RLLQQTSGAD
     WLNDTHWVQH TITNLSTPKR KRRPQDGPRE HQTGSARSEG YYPISKKEKD KYLDVCPVSA
     RQLEGGDTQG TNRVLSERRS EQRRLLSAIG TSAIMDSDLL KLNQLKFRKK KLRFGRSRIH
     EWGLFAMEPI AADEMVIEYV GQNIRQMVAD MREKRYVQEG IGSSYLFRVD HDTIIDATKC
     GNLARFINHC CTPNCYAKVI TIESQKKIVI YSKQPIGVDE EITYDYKFPL EDNKIPCLCG
     TESCRGSLN
//
ID   CAMP3_MOUSE             Reviewed;        1252 AA.
AC   Q80VC9; Q5DTW9; Q8BUZ0;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Calmodulin-regulated spectrin-associated protein 3;
DE   AltName: Full=Protein Nezha;
GN   Name=Kiaa1543; Synonyms=Camsap3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 198-1252 (ISOFORM 2).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 704-713, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1083, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   STRUCTURE BY NMR OF 1112-1240.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of a murine hypothetical protein from RIKEN cDNA
RT   2310057j16.";
RL   Submitted (JUN-2003) to the PDB data bank.
CC   -!- FUNCTION: Microtubule minus-end binding protein that acts as a
CC       regulator of microtubule dynamics. Specifically required for
CC       zonula adherens biogenesis and maintenance by anchoring
CC       microtubules at their minus-ends to zonula adherens, leading to
CC       recruit KIFC3 kinesin to junctional site (By similarity).
CC   -!- SUBUNIT: Interacts with PLEKHA7 (By similarity).
CC   -!- INTERACTION:
CC       Q6IQ23:PLEKHA7 (xeno); NbExp=1; IntAct=EBI-2125556, EBI-2125301;
CC   -!- SUBCELLULAR LOCATION: Cell junction, adherens junction (By
CC       similarity). Cytoplasm (By similarity). Cytoplasm, cytoskeleton
CC       (Potential). Note=Scattered in the cytoplasm. Localizes along
CC       zonula adherens only at mature cell-cell contacts (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80VC9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80VC9-2; Sequence=VSP_013705;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The CKK domain binds microtubules (By similarity).
CC   -!- SIMILARITY: Belongs to the CAMSAP1 family.
CC   -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC   -!- SIMILARITY: Contains 1 CKK domain.
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DR   EMBL; AK081728; BAC38313.1; -; mRNA.
DR   EMBL; BC048787; AAH48787.1; -; mRNA.
DR   EMBL; AK220401; BAD90256.1; -; Transcribed_RNA.
DR   IPI; IPI00225761; -.
DR   IPI; IPI00554840; -.
DR   RefSeq; NP_001157221.1; NM_001163749.1.
DR   RefSeq; NP_081447.2; NM_027171.3.
DR   UniGene; Mm.390010; -.
DR   PDB; 1UGJ; NMR; -; A=1112-1240.
DR   PDBsum; 1UGJ; -.
DR   ProteinModelPortal; Q80VC9; -.
DR   SMR; Q80VC9; 225-318, 1111-1247.
DR   IntAct; Q80VC9; 2.
DR   STRING; Q80VC9; -.
DR   PhosphoSite; Q80VC9; -.
DR   PRIDE; Q80VC9; -.
DR   Ensembl; ENSMUST00000057028; ENSMUSP00000058958; ENSMUSG00000044433.
DR   Ensembl; ENSMUST00000111066; ENSMUSP00000106695; ENSMUSG00000044433.
DR   GeneID; 69697; -.
DR   KEGG; mmu:69697; -.
DR   UCSC; uc009krw.1; mouse.
DR   MGI; MGI:1916947; 2310057J16Rik.
DR   eggNOG; maNOG09833; -.
DR   GeneTree; ENSGT00390000010026; -.
DR   InParanoid; Q80VC9; -.
DR   OMA; GGAEHVP; -.
DR   OrthoDB; EOG4G1MFN; -.
DR   NextBio; 330108; -.
DR   ArrayExpress; Q80VC9; -.
DR   Bgee; Q80VC9; -.
DR   CleanEx; MM_2310057J16RIK; -.
DR   Genevestigator; Q80VC9; -.
DR   GermOnline; ENSMUSG00000044433; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005915; C:zonula adherens; ISS:UniProtKB.
DR   GO; GO:0051011; F:microtubule minus-end binding; ISS:UniProtKB.
DR   GO; GO:0090136; P:epithelial cell-cell adhesion; ISS:UniProtKB.
DR   GO; GO:0034453; P:microtubule anchoring; ISS:UniProtKB.
DR   GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0045218; P:zonula adherens maintenance; ISS:UniProtKB.
DR   InterPro; IPR014797; CAMSAP_C.
DR   InterPro; IPR022613; CAMSAP_CH.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR011033; PRC_barrell-like.
DR   Pfam; PF11971; CAMSAP_CH; 1.
DR   Pfam; PF08683; DUF1781; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   SUPFAM; SSF50346; PRCH_cytoplasmic; 1.
DR   PROSITE; PS50021; CH; FALSE_NEG.
DR   PROSITE; PS51508; CKK; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell junction; Cytoplasm;
KW   Cytoskeleton; Direct protein sequencing; Microtubule; Phosphoprotein.
FT   CHAIN         1   1252       Calmodulin-regulated spectrin-associated
FT                                protein 3.
FT                                /FTId=PRO_0000050800.
FT   DOMAIN      163    312       CH.
FT   DOMAIN     1112   1246       CKK.
FT   COMPBIAS    496    549       Pro-rich.
FT   COMPBIAS    728    839       Pro-rich.
FT   MOD_RES     184    184       Phosphothreonine (By similarity).
FT   MOD_RES     193    193       Phosphoserine (By similarity).
FT   MOD_RES     334    334       Phosphoserine.
FT   MOD_RES     347    347       Phosphoserine (By similarity).
FT   MOD_RES     349    349       Phosphoserine (By similarity).
FT   MOD_RES     351    351       Phosphoserine (By similarity).
FT   MOD_RES     368    368       Phosphoserine (By similarity).
FT   MOD_RES     555    555       Phosphoserine (By similarity).
FT   MOD_RES     561    561       Phosphoserine (By similarity).
FT   MOD_RES     683    683       Phosphoserine (By similarity).
FT   MOD_RES     767    767       Phosphoserine (By similarity).
FT   MOD_RES     797    797       Phosphothreonine (By similarity).
FT   MOD_RES    1077   1077       Phosphoserine (By similarity).
FT   MOD_RES    1083   1083       Phosphoserine.
FT   VAR_SEQ    1042   1111       Missing (in isoform 2).
FT                                /FTId=VSP_013705.
FT   CONFLICT    199    207       DGASPAQPS -> LTSLSSCPQ (in Ref. 3;
FT                                BAD90256).
FT   CONFLICT    892    892       K -> E (in Ref. 1; BAC38313).
FT   HELIX      1125   1134
FT   TURN       1135   1137
FT   HELIX      1143   1155
FT   STRAND     1161   1169
FT   STRAND     1171   1178
FT   STRAND     1185   1192
FT   STRAND     1194   1196
FT   TURN       1198   1200
FT   STRAND     1201   1208
FT   TURN       1209   1212
FT   STRAND     1213   1216
FT   STRAND     1218   1221
FT   STRAND     1227   1231
FT   TURN       1234   1236
SQ   SEQUENCE   1252 AA;  135175 MW;  1E14AA8640108CF4 CRC64;
     MVEAAPAGSG PLRRTFLVPE IKSLDQYDFS RAKAAASLAW VLRAAFGGAE HVPPELWEPF
     YTDQYAQEHV KPPVTRLLLS AELYCRAWRQ ALPQLEPSPS PSALLALLAR RGTVPSLPEH
     PVREADLKHQ PILMGAHLAV IDALMVAFSF EWTKTLPGPL ALSSLEHKLL FWVDTTVRRL
     QEKTEQEAAQ RASPAAPLDG ASPAQPSIRY RKDRAIARRA PCFPNVTTLQ DLASGAALAA
     TIHCYCPQLL RLEEVCLKDP MSVADSLYNL QLVQDFCASH LPRGCPLSLE DLLYVPPPLK
     VNLVVLLAEM YMCFEVLKPD FVQAKDLPDG HAVSPRNTET VPSQNNSGSS SPVFNFRHPL
     LSPGGPQSPL RGSTGSLKSS PSMSHMEALG KAWNRQLSRP LSQAVSFSTP FGLDSDVDVV
     MGDPVLLRSV SSDSLGPPRP VSTSSRNSAQ PAPESGDLPT IEEALQIIHS AEPRLLPDGA
     ADGSFYLHSP EGLSKPPLSP YPPEGASKPL SDRLNKAPIY ISHPENPSKS SPCSTGEILK
     PPPPSEGSPK AVASSPAANN SEVKMTSFAE RKKQLVKAEA ESGLGSPTST PVAPEALSSE
     MSELGARLEE KRRAIEAQKR RIEAIFAKHR QRLGKSAFLQ VQPREAAGEA EEEAELGSVP
     GGERPAGEGQ GEPSLRHKSV TFSPDLGPVP PEGLGDYNRA VSKLSAALSS LQRDMQRLTD
     QQQRLLAPPE APGPAPPPAA WVIPGPATGP KAASPSPARR APAARRSPGP GPSPTPRSPK
     HARPAELKLA PLTRVLTPPH DVDSLPHLRK FSPSQVPVQT RSSILLSEGT PPEEPTTKPA
     LIEIPLASLG EPAADEEGDG SPPGAEDSLE EEASSEGEPR SGLGFFYKDE DKPEDEMAQK
     RASLLERQQR RVEEARRRKQ WQEAEKEQKR EEAARLAQEA PGLAFTTPVV ASAAPVATLA
     PTTRAMAPAE EEVGPRRGDF TRLEYERRAQ LKLMDDLDKV LRPRASGTGG PGRGGRRATR
     PRSGCCDDSA LARSPARGLL GSRLSKVYSQ STLSLSTVAN EAPNNLGVKR PTSRAPSPSG
     LMSPSRLPGS RERDWENGSN ASSPASVPEY TGPRLYKEPS AKSNKFIIHN ALSHCCLAGK
     VNEPQKNRIL EEIEKSKANH FLILFRDSSC QFRALYTLSG ETEELSRLAG YGPRTVTPAM
     VEGIYKYNSD RKRFTQIPAK TMSMSVDAFT IQGHLWQSKK PTTPKKGGGT PK
//
ID   Q80VE5_MOUSE            Unreviewed;       505 AA.
AC   Q80VE5;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   SubName: Full=TBC1 domain family, member 22B;
GN   Name=Tbc1d22b; Synonyms=BC045600; ORFNames=mCG_117108;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N;
RC   TISSUE=Mammary tumor. Metallothionien-TGF alpha model. 10 month old
RC   virgin mouse. Taken by biopsy.;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC045600; AAH45600.1; -; mRNA.
DR   EMBL; CH466606; EDL22624.1; -; Genomic_DNA.
DR   IPI; IPI00330437; -.
DR   RefSeq; NP_941049.1; NM_198647.1.
DR   UniGene; Mm.328934; -.
DR   HSSP; Q08484; 1FKM.
DR   ProteinModelPortal; Q80VE5; -.
DR   SMR; Q80VE5; 184-500.
DR   PhosphoSite; Q80VE5; -.
DR   PRIDE; Q80VE5; -.
DR   Ensembl; ENSMUST00000048677; ENSMUSP00000046877; ENSMUSG00000042203.
DR   GeneID; 381085; -.
DR   KEGG; mmu:381085; -.
DR   UCSC; uc008btd.1; mouse.
DR   CTD; 381085; -.
DR   MGI; MGI:2681867; Tbc1d22b.
DR   GeneTree; ENSGT00510000046400; -.
DR   HOGENOM; HBG714500; -.
DR   HOVERGEN; HBG057030; -.
DR   InParanoid; Q80VE5; -.
DR   OMA; SEYVEED; -.
DR   PhylomeDB; Q80VE5; -.
DR   NextBio; 461261; -.
DR   ArrayExpress; Q80VE5; -.
DR   Bgee; Q80VE5; -.
DR   Genevestigator; Q80VE5; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005097; F:Rab GTPase activator activity; IEA:InterPro.
DR   GO; GO:0032313; P:regulation of Rab GTPase activity; IEA:InterPro.
DR   InterPro; IPR000195; RabGAP/TBC_dom.
DR   Pfam; PF00566; TBC; 1.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; RabGAP_TBC; 2.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   505 AA;  59128 MW;  76B40E0E63A311F1 CRC64;
     MAAENSKQFW KRSAKLPGSI QPVYGAQHPP LDPRLTKNFI KERSKVNSVP LKNKKASSFH
     EFARNTSDAW DIGDDEEEDF SSPPFQTLNS KVALATAAQV LENHSKLRVK PERSQSTTSD
     VPANYKVIKS SSDAQLSRNS SDTCLRNPLH KQQSLPLRPI IPLVARISDQ NASGAPPMTV
     REKTRLEKFR QLLSSHNTDL DELRKWSWPG VPREVRPVTW RLLSGYLPAN TERRKLTLQR
     KREEYFGFIE QYYDSRNEEH HQDTYRQIHI DIPRTNPLIP LFQQPLVQEI FERILFIWAI
     RHPASGYVQG INDLVTPFFV VFLSEYVEED VENFDVTNLS QDMLRSIEAD SFWCMSKLLD
     GIQDNYTFAQ PGIQKKVKAL EELVSRIDEQ VHSHFRRYEV EYLQFAFRWM NNLLMRELPL
     RCTIRLWDTY QSEPEGFSHF HLYVCAAFLI KWRKEILDEE DFQGLLMLLQ NLPTIHWGNE
     EIGLLLAEAY RLKYMFADAP NHYRR
//
ID   Q80VL5_MOUSE            Unreviewed;       232 AA.
AC   Q80VL5;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 37.
DE   SubName: Full=Dst protein;
DE   Flags: Fragment;
GN   Name=Dst;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC048929; AAH48929.1; -; mRNA.
DR   IPI; IPI00230689; -.
DR   RefSeq; NP_598594.2; NM_133833.2.
DR   RefSeq; NP_604443.2; NM_134448.2.
DR   UniGene; Mm.478284; -.
DR   STRING; Q80VL5; -.
DR   Ensembl; ENSMUST00000097785; ENSMUSP00000095392; ENSMUSG00000026131.
DR   Ensembl; ENSMUST00000097786; ENSMUSP00000095393; ENSMUSG00000026131.
DR   GeneID; 13518; -.
DR   KEGG; mmu:13518; -.
DR   CTD; 13518; -.
DR   MGI; MGI:104627; Dst.
DR   GeneTree; ENSGT00600000084106; -.
DR   HOVERGEN; HBG077776; -.
DR   InParanoid; Q80VL5; -.
DR   ArrayExpress; Q80VL5; -.
DR   Bgee; Q80VL5; -.
DR   Genevestigator; Q80VL5; -.
DR   GO; GO:0060053; C:neurofilament cytoskeleton; IDA:MGI.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:MGI.
DR   GO; GO:0008090; P:retrograde axon cargo transport; IMP:MGI.
DR   InterPro; IPR003108; GAS2_dom.
DR   PROSITE; PS51460; GAR; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   232 AA;  24596 MW;  76A6DADFC42D023E CRC64;
     LDEFLVKNDP CRVHHHGSKM LRSESNSSIT ATQPTLAKGR TNMELREKFI LADGASQGMA
     AFRPRGRRSR PSSRGASPNR STSASSHACQ AASPPVPAAA STPKGTPIQG SKLRLPGYLS
     GKGFHSGEDS ALITTAAARV RTQFAESRKT PSRPGSRAGS KAGSRASSRR GSDASDFDIS
     EIQSVCSDVE TVPQTHRPVP RAGSRPSTAK PSKIPTPQRR SPASKLDKSS KR
//
ID   PNML1_MOUSE             Reviewed;         430 AA.
AC   Q80VM8; Q8C533;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   RecName: Full=PNMA-like protein 1;
GN   Name=Pnmal1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-246.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SIMILARITY: Belongs to the PNMA family.
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DR   EMBL; BC048228; AAH48228.1; -; mRNA.
DR   EMBL; AK079661; BAC37719.1; -; mRNA.
DR   IPI; IPI00330472; -.
DR   RefSeq; NP_001007570.1; NM_001007569.1.
DR   UniGene; Mm.275673; -.
DR   ProteinModelPortal; Q80VM8; -.
DR   PRIDE; Q80VM8; -.
DR   Ensembl; ENSMUST00000038163; ENSMUSP00000040929; ENSMUSG00000041141.
DR   GeneID; 71691; -.
DR   KEGG; mmu:71691; -.
DR   UCSC; uc009fip.1; mouse.
DR   CTD; 71691; -.
DR   MGI; MGI:1918941; Pnmal1.
DR   eggNOG; roNOG17353; -.
DR   GeneTree; ENSGT00530000062986; -.
DR   HOGENOM; HBG126835; -.
DR   HOVERGEN; HBG108276; -.
DR   InParanoid; Q80VM8; -.
DR   OMA; RSRRKKQ; -.
DR   OrthoDB; EOG412M5J; -.
DR   NextBio; 334243; -.
DR   ArrayExpress; Q80VM8; -.
DR   Bgee; Q80VM8; -.
DR   CleanEx; MM_PNMAL1; -.
DR   Genevestigator; Q80VM8; -.
PE   2: Evidence at transcript level;
FT   CHAIN         1    430       PNMA-like protein 1.
FT                                /FTId=PRO_0000325838.
SQ   SEQUENCE   430 AA;  48062 MW;  BA5722230F40CA77 CRC64;
     MSEPVAMTLL EDWCRGMGMD IHRSLLVTGI PEYCSHAEIE ETLNGVLLPL GTYRVLNKIF
     LRQENVKAAL VEVSEGVNLS SIPREFPGRG GVWRVVCRDP TQDDDFLKNL NEFLDGEGRT
     WEDMVRLLKL NPNPPLPNSN QPPPNWAEAL GLLLGAVVQV IFYMDAAIRS RDEEARAEEA
     AEAELMEAWA STARKRVKKE PGLGVEVGSA FKMEDRNYWK NTEDHGDPPK PLVRRPGGKI
     RSRRRKQKKN LKQEPICWRK SQGSNYNSNY NKVNLEAGEA AQSSEIPESV KSNKKPFVKQ
     EETVWKKKRV WRDPSDLPRS ALPAADSPGN LEDSDQDGGP ENPAKKKAMT WASNKIPVPT
     RKKKKMVSLG TLSYVLLDAE ATKNKTAILK KGLGARRAVS VPHDAPASTS RPQKTKLGAF
     PRVSKDSRKL
//
ID   TCPR1_MOUSE             Reviewed;        1166 AA.
AC   Q80VP0; Q8CHA3; Q8R3E0; Q99KQ5; Q9CVC6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Tectonin beta-propeller repeat-containing protein 1;
GN   Name=Tecpr1; Synonyms=Kiaa1358;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II, and FVB/N;
RC   TISSUE=Mammary tumor, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80VP0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80VP0-2; Sequence=VSP_033862;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the UPF0584 family.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 9 TECPR repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH25567.1; Type=Erroneous initiation;
CC       Sequence=BAC41478.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AB093295; BAC41478.1; ALT_INIT; mRNA.
DR   EMBL; AK008701; BAB25841.1; -; mRNA.
DR   EMBL; AK169888; BAE41437.1; -; mRNA.
DR   EMBL; AK170108; BAE41568.1; -; mRNA.
DR   EMBL; BC004058; AAH04058.1; -; mRNA.
DR   EMBL; BC025567; AAH25567.1; ALT_INIT; mRNA.
DR   EMBL; BC046968; AAH46968.1; -; mRNA.
DR   IPI; IPI00336291; -.
DR   IPI; IPI00894600; -.
DR   RefSeq; NP_081686.1; NM_027410.1.
DR   UniGene; Mm.239412; -.
DR   UniGene; Mm.458463; -.
DR   ProteinModelPortal; Q80VP0; -.
DR   SMR; Q80VP0; 65-173, 825-928.
DR   PhosphoSite; Q80VP0; -.
DR   PRIDE; Q80VP0; -.
DR   Ensembl; ENSMUST00000085701; ENSMUSP00000082844; ENSMUSG00000066621.
DR   GeneID; 70381; -.
DR   KEGG; mmu:70381; -.
DR   UCSC; uc009alj.1; mouse.
DR   CTD; 70381; -.
DR   MGI; MGI:1917631; Tecpr1.
DR   eggNOG; roNOG06756; -.
DR   GeneTree; ENSGT00510000047886; -.
DR   HOGENOM; HBG446248; -.
DR   InParanoid; Q80VP0; -.
DR   OMA; YMWSDAS; -.
DR   OrthoDB; EOG4ZPDTG; -.
DR   NextBio; 331501; -.
DR   ArrayExpress; Q80VP0; -.
DR   Bgee; Q80VP0; -.
DR   Genevestigator; Q80VP0; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   InterPro; IPR006624; Beta-propeller_rpt_TECPR.
DR   InterPro; IPR006614; Ferlin/Peroxisome_membrane.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000772; Ricin_B_lectin.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF06462; Hyd_WA; 8.
DR   SMART; SM00694; DysFC; 2.
DR   SMART; SM00693; DysFN; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00706; TECPR; 11.
DR   PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Disulfide bond; Phosphoprotein; Repeat.
FT   CHAIN         1   1166       Tectonin beta-propeller repeat-containing
FT                                protein 1.
FT                                /FTId=PRO_0000337061.
FT   REPEAT      209    240       TECPR 1.
FT   REPEAT      254    285       TECPR 2.
FT   REPEAT      301    332       TECPR 3.
FT   REPEAT      344    376       TECPR 4.
FT   DOMAIN      616    722       PH.
FT   REPEAT      734    761       TECPR 5.
FT   REPEAT      958    989       TECPR 6.
FT   REPEAT     1003   1034       TECPR 7.
FT   REPEAT     1049   1080       TECPR 8.
FT   REPEAT     1092   1132       TECPR 9.
FT   COMPBIAS    384    391       Poly-Ser.
FT   MOD_RES     943    943       Phosphoserine (By similarity).
FT   MOD_RES     948    948       Phosphoserine (By similarity).
FT   DISULFID     45     59       By similarity.
FT   VAR_SEQ       1    141       Missing (in isoform 2).
FT                                /FTId=VSP_033862.
FT   CONFLICT    725    725       R -> W (in Ref. 1; BAC41478).
FT   CONFLICT   1014   1014       A -> T (in Ref. 3; AAH04058).
FT   CONFLICT   1159   1159       R -> C (in Ref. 3; AAH04058).
SQ   SEQUENCE   1166 AA;  130266 MW;  5DA166A7ACA30908 CRC64;
     MPTSVLWAVD LFGRVYTLST AGQYWELCKD VQLEFKRVSA ATQCCWGIAG DNQVYLYVCS
     SDVPIRHREE AYENQRWNPM GGFCEKLLPS DRWPWSDVSG LQHRPLDGVA LPSPHWEWES
     DWYVDENFGG EPTEKGGWTY AMDFPATYTR DKKWNSCVRR RKWIRYRRYK SRDSWAKIPS
     KDDPKELPDP FNDLSVGGWE ITEEPVGRLS VWAVSLQGKV WYREDVSHPN PEGSSWSLVE
     TPGEVVQISC GPHDLIWATL WEGQALVREG VCRNNPKGSY WSMVEPPGSE NGIMHVSAGV
     SVVWAITKDR KVWFRRGVNS HNPCGTSWIE MVGEMTMVNV GLNDQVWGIS CEDRAVYFRQ
     GVTPSELSGK TWKAIVVGRE SDRSHSGSSS SLLSAGCFFG DEVRGSGTES APSDTDASLE
     VERQGPEQPL PKEALDNSTN LKGSLSKGHE TSGNTDHSTE NACLTEGKEK APETSRSDEC
     RGPASTPAEL PWTNIDLKEP KKVSNQPAAG FPETAGLSSL GLFPMGMEEP YGADDHPLWA
     WVSGGACAVE AGSTLKWFTI QSGLSPSVQT LSLSITPAQT AAWRKQIFQQ LTERTKRELE
     SFRHYEQAVE QSVWVKTGAL QWWCDWKPHK WVDVRVALEQ FTGHDGARDS ILFIYYVVHE
     EKKYLHVFLN EVTVLVPVLN EAKHSFALYT PERTRQRWPV RLAAATEQDM NDWLALLSLS
     CCESRKVHGR PSPQAIWSVT CKGDIFVSEP SPDLEARERL LPCDQMFWRQ MGGHLRIIEA
     NSRGVVWGIG YDHTAWVYTG GYGGGCFQGL ASSTSNIYTQ SDVKSVYIYE NQRWNPVTGY
     TSRGLPTDRF MWSDVTGLQE CTKAGTKPPS LQWTWVSDWY VDFSVPGGTD QEGWQYASDF
     PASYHGYKTM KDFVRRRCWA RKCKLVTSGP WLEVAPITLS DVSIIPESAH ADGRGHNVAL
     WAVSDKGDVL CRLGVSELNP AGSSWLHVGT DQPFASVSIG ACYQVWAVAR DGSAFYRGSV
     SPSQPAGDCW YHIPSPPKQK LTQVSVGQTS VYALDENGNL WYRAGITPSY PQGSSWEHVS
     NNVRKVSVGP LDQVWVIANK VQGSHGLSRG TVCRRMGVQP REPKGQGWDY GIGGGWDHIS
     VRANATRVPR NMSRDREARG PGPVCC
//
ID   EPN1_MOUSE              Reviewed;         575 AA.
AC   Q80VP1; O70446; Q6NX78;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 3.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Epsin-1;
DE   AltName: Full=EPS-15-interacting protein 1;
DE   AltName: Full=Intersectin-EH-binding protein 1;
DE            Short=Ibp1;
GN   Name=Epn1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Colon, Limb, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 365-575 (ISOFORM 2), AND INTERACTION
RP   WITH ITSN1.
RC   TISSUE=Embryo;
RX   MEDLINE=99030416; PubMed=9813051; DOI=10.1074/jbc.273.47.31401;
RA   Yamabhai M., Hoffman N.G., Hardison N.L., McPherson P.S.,
RA   Castagnoli L., Cesareni G., Kay B.K.;
RT   "Intersectin, a novel adaptor protein with two eps15 homology and five
RT   src homology 3 domains.";
RL   J. Biol. Chem. 273:31401-31407(1998).
RN   [3]
RP   PHOSPHORYLATION, AND INTERACTION WITH AP2A1 AND AP2A2.
RX   MEDLINE=99121054; PubMed=9920862; DOI=10.1074/jbc.274.6.3257;
RA   Chen H., Slepnev V.I., Di Fiore P.P., De Camilli P.;
RT   "The interaction of epsin and Eps15 with the clathrin adaptor AP-2 is
RT   inhibited by mitotic phosphorylation and enhanced by stimulation-
RT   dependent dephosphorylation in nerve terminals.";
RL   J. Biol. Chem. 274:3257-3260(1999).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-469, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Binds to membranes enriched in phosphatidylinositol-4,5-
CC       biphosphate (PtdIns(4,5)P2). Modifies membrane curvature and
CC       facilitates the formation of clathrin-coated invaginations (By
CC       similarity). Regulates receptor-mediated endocytosis.
CC   -!- SUBUNIT: Monomer. Binds clathrin, ZBTB16/ZNF145, ITSN1, REPS2,
CC       EPS15, AP2A1 and AP2A2. Binds ubiquitinated proteins. Interacts
CC       with RALBP1 in a complex also containing NUMB and TFAP2A during
CC       interphase and mitosis. Interacts with AP2B1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane;
CC       Peripheral membrane protein (By similarity). Nucleus (By
CC       similarity). Membrane, clathrin-coated pit (By similarity).
CC       Note=Associated with the cytoplasmic membrane at sites where
CC       clathrin-coated pits are forming. Colocalizes with clathrin and
CC       AP-2 in a punctate pattern on the plasma membrane. Detected in
CC       presynaptic nerve terminals and in Golgi stacks. May shuttle to
CC       the nucleus when associated with ZBTB16/ZNF145 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80VP1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80VP1-2; Sequence=VSP_009153;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The NPF repeat domain is involved in EPS15 binding.
CC   -!- DOMAIN: The DPW repeat domain is involved in AP2A2 and clathrin
CC       binding.
CC   -!- DOMAIN: The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates
CC       interaction the AP-2 complex subunit AP2B1 (By similarity).
CC   -!- PTM: Phosphorylated on serine and/or threonine residues in mitotic
CC       cells. Phosphorylation reduces interaction with REPS2, AP-2 and
CC       the membrane fraction. Depolarization of synaptosomes results in
CC       dephosphorylation.
CC   -!- PTM: Ubiquitinated (By similarity).
CC   -!- SIMILARITY: Belongs to the epsin family.
CC   -!- SIMILARITY: Contains 1 ENTH (epsin N-terminal homology) domain.
CC   -!- SIMILARITY: Contains 3 UIM (ubiquitin-interacting motif) repeats.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=The bubble's bend -
CC       Issue 42 of January 2004;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt042.shtml";
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC046962; AAH46962.2; -; mRNA.
DR   EMBL; BC067206; AAH67206.1; -; mRNA.
DR   EMBL; BC099682; AAH99682.1; -; mRNA.
DR   EMBL; AF057285; AAC97475.1; -; mRNA.
DR   IPI; IPI00330477; -.
DR   IPI; IPI00407944; -.
DR   RefSeq; NP_034277.1; NM_010147.3.
DR   UniGene; Mm.3091; -.
DR   ProteinModelPortal; Q80VP1; -.
DR   SMR; Q80VP1; 1-158.
DR   MINT; MINT-4094555; -.
DR   STRING; Q80VP1; -.
DR   PhosphoSite; Q80VP1; -.
DR   PRIDE; Q80VP1; -.
DR   Ensembl; ENSMUST00000045277; ENSMUSP00000043340; ENSMUSG00000035203.
DR   Ensembl; ENSMUST00000098845; ENSMUSP00000096445; ENSMUSG00000035203.
DR   Ensembl; ENSMUST00000108570; ENSMUSP00000104210; ENSMUSG00000035203.
DR   GeneID; 13854; -.
DR   KEGG; mmu:13854; -.
DR   UCSC; uc009ezx.1; mouse.
DR   CTD; 13854; -.
DR   MGI; MGI:1333763; Epn1.
DR   eggNOG; roNOG13892; -.
DR   GeneTree; ENSGT00550000074611; -.
DR   HOVERGEN; HBG006690; -.
DR   OMA; APTSDPW; -.
DR   OrthoDB; EOG4SF97B; -.
DR   PhylomeDB; Q80VP1; -.
DR   NextBio; 284718; -.
DR   ArrayExpress; Q80VP1; -.
DR   Bgee; Q80VP1; -.
DR   CleanEx; MM_EPN1; -.
DR   Genevestigator; Q80VP1; -.
DR   GermOnline; ENSMUSG00000035203; Mus musculus.
DR   GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR013809; Epsin-like_N.
DR   InterPro; IPR001026; Epsin_dom_N.
DR   InterPro; IPR003903; Ubiquitin-int_motif.
DR   Gene3D; G3DSA:1.25.40.90; ENTH_VHS; 1.
DR   Pfam; PF01417; ENTH; 1.
DR   Pfam; PF02809; UIM; 2.
DR   SMART; SM00273; ENTH; 1.
DR   SMART; SM00726; UIM; 3.
DR   SUPFAM; SSF48464; ENTH_VHS; 1.
DR   PROSITE; PS50942; ENTH; 1.
DR   PROSITE; PS50330; UIM; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Coated pit; Cytoplasm;
KW   Endocytosis; Lipid-binding; Membrane; Nucleus; Phosphoprotein; Repeat;
KW   Ubl conjugation.
FT   CHAIN         1    575       Epsin-1.
FT                                /FTId=PRO_0000074514.
FT   DOMAIN       12    144       ENTH.
FT   REPEAT      183    202       UIM 1.
FT   REPEAT      208    227       UIM 2.
FT   REPEAT      233    252       UIM 3.
FT   REPEAT      274    276       1.
FT   REPEAT      294    296       2.
FT   REPEAT      306    308       3.
FT   REPEAT      319    321       4.
FT   REPEAT      332    334       5.
FT   REPEAT      349    351       6.
FT   REPEAT      367    369       7.
FT   REPEAT      377    379       8.
FT   REPEAT      501    503       1.
FT   REPEAT      517    519       2.
FT   REPEAT      571    573       3.
FT   REGION      274    379       8 X 3 AA repeats of D-P-W.
FT   REGION      501    573       3 X 3 AA repeats of N-P-F.
FT   MOTIF       401    410       [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif.
FT   COMPBIAS    267    572       Ala/Gly/Pro-rich.
FT   BINDING      11     11       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   BINDING      25     25       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   BINDING      30     30       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   BINDING      63     63       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   BINDING      73     73       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   MOD_RES     382    382       Phosphoserine (By similarity).
FT   MOD_RES     419    419       Phosphoserine.
FT   MOD_RES     434    434       Phosphoserine (By similarity).
FT   MOD_RES     453    453       Phosphoserine (By similarity).
FT   MOD_RES     459    459       Phosphothreonine (By similarity).
FT   MOD_RES     463    463       Phosphothreonine (By similarity).
FT   MOD_RES     469    469       Phosphothreonine.
FT   MOD_RES     493    493       Phosphothreonine (By similarity).
FT   VAR_SEQ     392    392       A -> AA (in isoform 2).
FT                                /FTId=VSP_009153.
SQ   SEQUENCE   575 AA;  60212 MW;  70B8011EB3AE5C4C CRC64;
     MSTSSLRRQM KNIVHNYSEA EIKVREATSN DPWGPSSSLM SEIADLTYNV VAFSEIMSMI
     WKRLNDHGKN WRHVYKAMTL MEYLIKTGSE RVSQQCKENM YAVQTLKDFQ YVDRDGKDQG
     VNVREKAKQL VALLRDEDRL REERAHALKT KEKLAQTATA SSAAVGSGPP PEAEQAWPQS
     SGEEELQLQL ALAMSKEEAD QPPSCGPEDD VQLQLALSLS REEHDKEERI RRGDDLRLQM
     AIEESKRETG GKEESSLMDL ADVFTTPAPP QASDPWGGPA SVPTAVPVAA AASDPWGGPA
     VPPAADPWGG AAPTPASGDP WRPAAPTGPS VDPWGGTPAP AAGEGPTPDP WGSSDGGAPV
     SGPPSSDPWA PAPAFSDPWG GSPAKPSSNG TAVGGFDTEP DEFSDFDRLR TALPTSGSST
     GELELLAGEV PARSPGAFDM SGVGGSLAES VGSPPPAATP TPTPPTRKTP ESFLGPNAAL
     VDLDSLVSRP GPTPPGSKAS NPFLPSGAPP TGPSVTNPFQ PAPPATLTLN QLRLSPVPPV
     PGAPPTYISP LGGGPGLPPM MPPGPPAPNT NPFLL
//
ID   CA183_MOUSE             Reviewed;         300 AA.
AC   Q80VY2; Q8C5H0; Q8CCA1;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   RecName: Full=Uncharacterized protein C1orf183 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Colon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80VY2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80VY2-2; Sequence=VSP_028174;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK033558; BAC28358.1; -; mRNA.
DR   EMBL; AK078368; BAC37240.1; -; mRNA.
DR   EMBL; BC052371; AAH52371.1; -; mRNA.
DR   IPI; IPI00337991; -.
DR   IPI; IPI00830942; -.
DR   RefSeq; NP_001156828.1; NM_001163356.1.
DR   RefSeq; NP_780607.2; NM_175398.4.
DR   UniGene; Mm.212591; -.
DR   ProteinModelPortal; Q80VY2; -.
DR   PRIDE; Q80VY2; -.
DR   Ensembl; ENSMUST00000066610; ENSMUSP00000069212; ENSMUSG00000048458.
DR   GeneID; 109050; -.
DR   KEGG; mmu:109050; -.
DR   UCSC; uc008qvc.1; mouse.
DR   MGI; MGI:1923497; 6530418L21Rik.
DR   eggNOG; roNOG05306; -.
DR   GeneTree; ENSGT00530000063849; -.
DR   HOGENOM; HBG446953; -.
DR   HOVERGEN; HBG107564; -.
DR   InParanoid; Q80VY2; -.
DR   OMA; QMNSMMG; -.
DR   OrthoDB; EOG4R23VR; -.
DR   PhylomeDB; Q80VY2; -.
DR   NextBio; 361604; -.
DR   ArrayExpress; Q80VY2; -.
DR   Bgee; Q80VY2; -.
DR   CleanEx; MM_6530418L21RIK; -.
DR   Genevestigator; Q80VY2; -.
PE   2: Evidence at transcript level;
KW   Alternative splicing.
FT   CHAIN         1    300       Uncharacterized protein C1orf183 homolog.
FT                                /FTId=PRO_0000304995.
FT   VAR_SEQ       1     19       Missing (in isoform 2).
FT                                /FTId=VSP_028174.
FT   CONFLICT    195    195       G -> R (in Ref. 1; BAC28358).
SQ   SEQUENCE   300 AA;  33233 MW;  6A2006152573C324 CRC64;
     MTKESKDMDC YLRRLKQELM SMKEVGDGLQ DQMNCMMGAL QELKLLQVQT ALEQLEISGG
     TPTFSCPESS QEQPECPRWQ GSGGPAGPAA WTSSSQPSFD SSPKLPCRRS VCGKELAVLP
     KTQLPEEHQS CTQQGTEWVE PDDWTSTLMS RGRNRQPLVL GDNVFADLVG NWLDLPELEK
     GGEKGETGGS IEPKGEKGQS RELGRKFALT ANIFRKFLRS VRPDRDRLLK EKPGWMTPMV
     SESRAGRSKK VKKRSLSKGS GRFPFSSTGE PRHIETPATS SPKALEPSCR GFDINTAVWV
//
ID   Q80VZ2_MOUSE            Unreviewed;       986 AA.
AC   Q80VZ2;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Ephrin receptor;
DE            EC=2.7.10.1;
GN   Name=Epha4; ORFNames=mCG_119512;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [11]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Ephrin receptor subfamily.
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; BC052164; AAH52164.1; -; mRNA.
DR   EMBL; AK147698; BAE28081.1; -; mRNA.
DR   EMBL; CH466548; EDL00429.1; -; Genomic_DNA.
DR   IPI; IPI00337992; -.
DR   RefSeq; NP_031962.2; NM_007936.3.
DR   UniGene; Mm.400747; -.
DR   PDB; 2HEL; X-ray; 2.35 A; A=591-896.
DR   PDBsum; 2HEL; -.
DR   ProteinModelPortal; Q80VZ2; -.
DR   SMR; Q80VZ2; 30-205, 595-981.
DR   STRING; Q80VZ2; -.
DR   PRIDE; Q80VZ2; -.
DR   Ensembl; ENSMUST00000027451; ENSMUSP00000027451; ENSMUSG00000026235.
DR   GeneID; 13838; -.
DR   KEGG; mmu:13838; -.
DR   UCSC; uc007bpz.1; mouse.
DR   CTD; 13838; -.
DR   MGI; MGI:98277; Epha4.
DR   HOVERGEN; HBG062180; -.
DR   InParanoid; Q80VZ2; -.
DR   OMA; RFIRESQ; -.
DR   NextBio; 284664; -.
DR   ArrayExpress; Q80VZ2; -.
DR   Bgee; Q80VZ2; -.
DR   Genevestigator; Q80VZ2; -.
DR   GO; GO:0005887; C:integral to plasma membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005003; F:ephrin receptor activity; IEA:InterPro.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0007411; P:axon guidance; IMP:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   InterPro; IPR001090; Ephrin_rcpt_lig-bd.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR011510; SAM_2.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   InterPro; IPR016257; Tyr_prot_kinase_ephrin_rcpt.
DR   InterPro; IPR001426; Tyr_prot_kinase_rcpt_V_CS.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF01404; Ephrin_lbd; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00615; EPH_lbd; 1.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; FN_III-like; 2.
DR   SUPFAM; SSF49785; Gal_bind_like; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
DR   PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Membrane; Nucleotide-binding; Receptor;
KW   Transferase; Transmembrane; Transmembrane helix.
SQ   SEQUENCE   986 AA;  109814 MW;  89BEB2C7CDB54A55 CRC64;
     MAGIFYFILF SFLFGICDAV TGSRVYPANE VTLLDSRSVQ GELGWIASPL EGGWEEVSIM
     DEKNTPIRTY QVCNVMEASQ NNWLRTDWIT REGAQRVYIE IKFTLRDCNS LPGVMGTCKE
     TFNLYYYESD NDKERFIRES QFGKIDTIAA DESFTQVDIG DRIMKLNTEI RDVGPLSKKG
     FYLAFQDVGA CIALVSVRVF YKKCPLTVRN LAQFPDTITG ADTSSLVEVR GSCVNNSEEK
     DVPKMYCGAD GEWLVPIGNC LCNAGHEEQN GECQACKIGY YKALSTDASC AKCPPHSYSV
     WEGATSCTCD RGFFRADNDA ASMPCTRPPS APLNLISNVN ETSVNLEWSS PQNTGGRQDI
     SYNVVCKKCG AGDPSKCRPC GSGVHYTPQQ NGLKTTRVSI TDLLAHTNYT FEIWAVNGVS
     KYNPSPDQSV SVTVTTNQAA PSSIALVQAK EVTRYSVALA WLEPDRPNGV ILEYEVKYYE
     KDQNERSYRI VRTAARNTDI KGLNPLTSYV FHVRARTAAG YGDFSEPLEV TTNTVPSRII
     GDGANSTVLL VSVSGSVVLV VILIAAFVIS RRRSKYSKAK QEADEEKHLN QGVRTYVDPF
     TYEDPNQAVR EFAKEIDASC IKIEKVIGVG EFGEVCSGRL KVPGKREICV AIKTLKAGYT
     DKQRRDFLSE ASIMGQFDHP NIIHLEGVVT KCKPVMIITE YMENGSLDAF LRKNDGRFTV
     IQLVGMLRGI GSGMKYLSDM SYVHRDLAAR NILVNSNLVC KVSDFGMSRV LEDDPEAAYT
     TRGGKIPIRW TAPEAIAYRK FTSASDVWSY GIVMWEVMSY GERPYWDMSN QDVIKAIEEG
     YRLPPPMDCP IALHQLMLDC WQKERSDRPK FGQIVNMLDK LIRNPNSLKR TGSESSRPNT
     ALLDPSSPEF SAVVSVGDWL QAIKMDRYKD NFTAAGYTTL EAVVHMSQDD LARIGITAIT
     HQNKILSSVQ AMRTQMQQMH GRMVPV
//
ID   PP1RA_MOUSE             Reviewed;         888 AA.
AC   Q80W00; B1B179; Q811B6; Q8C6T7; Q8K2U8;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Serine/threonine-protein phosphatase 1 regulatory subunit 10;
DE   AltName: Full=MHC class I region proline-rich protein CAT53;
GN   Name=Ppp1r10; Synonyms=Cat53, Pnuts;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Raha-Chowdhury R., Andrews S.R., Gruen J.R., Weissman S.M.;
RT   "Genes from major histocompatibility complex (MHC) class I region from
RT   HLA-C to HLA-A.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary cancer;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-273.
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   IDENTIFICATION IN THE PTW/PP1 PHOSPHATASE COMPLEX, FUNCTION,
RP   SUBCELLULAR LOCATION, INTERACTION WITH PPP1CA; TOX4 AND WDR82, AND
RP   MUTAGENESIS OF TRP-401.
RX   PubMed=20516061; DOI=10.1074/jbc.M110.109801;
RA   Lee J.H., You J., Dobrota E., Skalnik D.G.;
RT   "Identification and characterization of a novel human PP1 phosphatase
RT   complex.";
RL   J. Biol. Chem. 285:24466-24476(2010).
CC   -!- FUNCTION: Scaffold protein which mediates the formation of the
CC       PTW/PP1 phosphatase complex by providing a binding platform to
CC       each component of the complex. The PTW/PP1 phosphatase complex
CC       plays a role in the control of chromatin structure and cell cycle
CC       progression during the transition from mitosis into interphase.
CC       Mediates interaction of WDR82 and PPP1CA. Inhibitor of PPP1CA and
CC       PPP1CC phosphatase activities. Has inhibitory activity on PPP1CA
CC       only when phosphorylated. Binds to mRNA, single-stranded DNA
CC       (ssDNA), poly(A) and poly(G) homopolymers.
CC   -!- SUBUNIT: Component of the PTW/PP1 phosphatase complex, composed of
CC       PPP1R10/PNUTS, TOX4, WDR82, and PPP1CA or PPP1CB or PPP1CC.
CC       Interacts with PPP1CC (By similarity). Interacts with PPP1CA,
CC       WDR82 and TOX4.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Note=Found in
CC       discrete nucleoplasmic bodies and within nucleoli (By similarity).
CC       Associates with chromatin during interphase, excluded from
CC       condensed chromosomes during early mitosis and is reloaded onto
CC       chromosomes at the late telophase.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80W00-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80W00-2; Sequence=VSP_013155;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated on Thr-398 and Thr-400 by PKA within the
CC       region necessary for interaction with PPP1CA (By similarity).
CC   -!- SIMILARITY: Contains 1 C3H1-type zinc finger.
CC   -!- SIMILARITY: Contains 1 TFIIS N-terminal domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AJ504718; CAD44294.1; -; mRNA.
DR   EMBL; CR974451; CAM27669.1; -; Genomic_DNA.
DR   EMBL; BC029765; AAH29765.1; -; mRNA.
DR   EMBL; BC052059; AAH52059.1; -; mRNA.
DR   EMBL; AK053183; BAC35301.1; -; mRNA.
DR   IPI; IPI00330483; -.
DR   IPI; IPI00553250; -.
DR   RefSeq; NP_001157290.1; NM_001163818.1.
DR   RefSeq; NP_787948.2; NM_175934.3.
DR   UniGene; Mm.29385; -.
DR   ProteinModelPortal; Q80W00; -.
DR   SMR; Q80W00; 79-145.
DR   DIP; DIP-48511N; -.
DR   STRING; Q80W00; -.
DR   PhosphoSite; Q80W00; -.
DR   PRIDE; Q80W00; -.
DR   Ensembl; ENSMUST00000087210; ENSMUSP00000084460; ENSMUSG00000039220.
DR   Ensembl; ENSMUST00000087211; ENSMUSP00000084461; ENSMUSG00000039220.
DR   Ensembl; ENSMUST00000113771; ENSMUSP00000109401; ENSMUSG00000039220.
DR   GeneID; 52040; -.
DR   KEGG; mmu:52040; -.
DR   CTD; 52040; -.
DR   MGI; MGI:1289273; Ppp1r10.
DR   GeneTree; ENSGT00530000063820; -.
DR   HOGENOM; HBG355356; -.
DR   HOVERGEN; HBG053646; -.
DR   InParanoid; Q80W00; -.
DR   OMA; MGGGHRP; -.
DR   OrthoDB; EOG451DQK; -.
DR   PhylomeDB; Q80W00; -.
DR   NextBio; 308416; -.
DR   ArrayExpress; Q80W00; -.
DR   Bgee; Q80W00; -.
DR   CleanEx; MM_PPP1R10; -.
DR   Genevestigator; Q80W00; -.
DR   GermOnline; ENSMUSG00000039220; Mus musculus.
DR   GO; GO:0072357; C:PTW/PP1 phosphatase complex; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0003702; F:RNA polymerase II transcription factor activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   GO; GO:0006354; P:transcription elongation, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR   InterPro; IPR017923; TFIIS_N.
DR   InterPro; IPR000571; Znf_CCCH.
DR   Gene3D; G3DSA:1.20.930.10; TFIIS_N_fun-typ; 1.
DR   Pfam; PF08711; TFIIS; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   SMART; SM00509; TFS2N; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   SUPFAM; SSF47676; TFIIS_conserved; 1.
DR   PROSITE; PS51319; TFIIS_N; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; DNA-binding; Metal-binding;
KW   Nucleus; Phosphoprotein; Protein phosphatase inhibitor; RNA-binding;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    888       Serine/threonine-protein phosphatase 1
FT                                regulatory subunit 10.
FT                                /FTId=PRO_0000071512.
FT   DOMAIN       73    147       TFIIS N-terminal.
FT   ZN_FING     854    882       C3H1-type.
FT   REGION        1    348       Interaction with TOX4.
FT   REGION      382    450       Essential for PPP1CA inhibition (By
FT                                similarity).
FT   REGION      388    417       Necessary for interaction with PPP1CA.
FT   REGION      393    408       Necessary for interaction with PPP1CC (By
FT                                similarity).
FT   REGION      418    619       Interaction with WDR82.
FT   MOTIF       420    423       PP1-binding motif.
FT   COMPBIAS    304    310       Poly-Lys.
FT   COMPBIAS    540    852       Gly-rich.
FT   MOD_RES     207    207       N6-acetyllysine (By similarity).
FT   MOD_RES     239    239       N6-acetyllysine (By similarity).
FT   MOD_RES     313    313       Phosphoserine.
FT   MOD_RES     545    545       Phosphoserine (By similarity).
FT   MOD_RES     591    591       Phosphoserine (By similarity).
FT   VAR_SEQ     756    769       Missing (in isoform 2).
FT                                /FTId=VSP_013155.
FT   MUTAGEN     401    401       W->A: Loss of interaction with PPP1CA but
FT                                no effect on interaction with TOX4 or
FT                                WDR82. Cell cycle arrest at mitosis and
FT                                cell death. Exhibits normal association
FT                                with chromososmes but shows defects in
FT                                the process of chromosome decondensation
FT                                at late telophase.
FT   CONFLICT     30     30       G -> A (in Ref. 1; CAD44294).
FT   CONFLICT     85     85       T -> N (in Ref. 1; CAD44294).
FT   CONFLICT    171    171       P -> H (in Ref. 1; CAD44294).
FT   CONFLICT    239    239       K -> N (in Ref. 1; CAD44294).
SQ   SEQUENCE   888 AA;  94372 MW;  F32889274EF3632D CRC64;
     MGSGPIDPKE LLKGLDSFLT RDGEVKSVDG ISKIFSLMKE ARKMVSRCTY LNIILQTRAP
     EVLVKFIDVG GYKLLNNWLT YSKTTNNIPL LQQILLTLQH LPLTVDHLKQ NNTAKLVKQL
     SKSSEDEELR KLASVLVSDW MAVIRSQSST QPAEKDKKKR KEEGKSRTTL PERPLTEVKA
     ETRAEEAPEK KKEKPKSLRT TAPSHAKFRS TGLELDTPSL VPVKKNSSTV VVSDKYNLKP
     IPLKRQSATA APGDAAPPAE KKYKPLNTAP NTTKEIKVKI IPPQPMEGLG FLDALNSAPV
     PGIKIKKKKK VLSPTAAKPS PFEGKTSTEQ STAKPSSPEP APPAEPMDTD RPGTPVPPVE
     VPELMDAASS EPGALDAKPV DSPGDPNQLT RKGRKRKTVT WPEEGKLREY FYFELDETER
     VNVNKIKDFG EAAKREILSD RHAFETARRL SHDNMEEKVP WVCPRPLVLP SPLVIPGSNS
     QERYIQAERE KGILQELFLN KESPHEPDPE PYEPIPPKLI PLDEECAMDE TPYVETLEPG
     GSGGSPDGAG GSKLPPVLAN LMGSMGAGKS PQGPGGGGIN VQEILTSIMG SPNSHPSEEL
     LKQPDYSDKL KQMLVPHGLL GPGPVANGFP PGGPGGPKGM QHFPPGPGGP MPGPHGGPGG
     PVGPRLLGPP PPSRGGDPFW DGPGDPMRGG PMRGGPGPAP GPYHRGRGGR GGNEPPPPPP
     FRGARGGRSG GGPPNGRGGP GGGGMVGGGG HRPHEGPGGS MGSGHRSHDG PGGNMGSGHR
     SHDGPGGNMG GSGGHRSHEG PGHGGPHGHR PHDVPSHRGH DHRGPPPHEH RGHDGHGGGG
     HRGHDGGHSH GGDMSNRPVC RHFMMKGNCR YENNCAFYHP GVNGPPLP
//
ID   TMCC2_MOUSE             Reviewed;         706 AA.
AC   Q80W04; Q6A061;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Transmembrane and coiled-coil domains protein 2;
GN   Name=Tmcc2; Synonyms=Kiaa0481;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-706.
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461; THR-463 AND
RP   SER-467, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-478, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the TEX28 family.
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DR   EMBL; BC052035; AAH52035.1; -; mRNA.
DR   EMBL; AK172957; BAD32235.1; -; mRNA.
DR   IPI; IPI00321243; -.
DR   RefSeq; NP_849205.1; NM_178874.2.
DR   UniGene; Mm.273785; -.
DR   ProteinModelPortal; Q80W04; -.
DR   PhosphoSite; Q80W04; -.
DR   PRIDE; Q80W04; -.
DR   Ensembl; ENSMUST00000045473; ENSMUSP00000038369; ENSMUSG00000042066.
DR   GeneID; 68875; -.
DR   KEGG; mmu:68875; -.
DR   UCSC; uc007cot.1; mouse.
DR   CTD; 68875; -.
DR   MGI; MGI:1916125; Tmcc2.
DR   GeneTree; ENSGT00390000007639; -.
DR   HOGENOM; HBG443696; -.
DR   HOVERGEN; HBG057342; -.
DR   InParanoid; Q80W04; -.
DR   OMA; CKSDELQ; -.
DR   OrthoDB; EOG4229K8; -.
DR   PhylomeDB; Q80W04; -.
DR   NextBio; 328093; -.
DR   ArrayExpress; Q80W04; -.
DR   Bgee; Q80W04; -.
DR   CleanEx; MM_TMCC2; -.
DR   Genevestigator; Q80W04; -.
DR   GermOnline; ENSMUSG00000042066; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR019394; Predicted_TM_coiled-coil_2.
DR   Pfam; PF10267; Tmemb_cc2; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    706       Transmembrane and coiled-coil domains
FT                                protein 2.
FT                                /FTId=PRO_0000184598.
FT   TRANSMEM    646    666       Helical; (Potential).
FT   TRANSMEM    679    699       Helical; (Potential).
FT   COILED      330    365       Potential.
FT   COILED      511    630       Potential.
FT   MOD_RES     461    461       Phosphoserine.
FT   MOD_RES     463    463       Phosphothreonine.
FT   MOD_RES     467    467       Phosphoserine.
FT   MOD_RES     478    478       Phosphoserine.
SQ   SEQUENCE   706 AA;  77054 MW;  2BB4604A276C94B2 CRC64;
     MKRCKSDELQ QQQGEEDGAG MEDAACLLPG ADLRHGEASS ANSAGGPTSD AGAAVAPNPG
     PRSKPPDLKK IQQLSEGSMF GHGLKHLFHS RRRSREREHQ ASQEAQQQQQ QQGLSDQDSP
     DEKERSPEMH RVSYAVSLHD LPARPTAFNR VLQQIRSRPS IKRGASLHSS GGSGGRRAKS
     SSLEPQRGSP HLLRKAPQDS SLAAILHQHQ GRPRSSSTTD TALLLADGSS AYLLAEEAES
     IGDKGDKGDL VALSLPSGPG HGDSDGPISL DVPDGAPDPQ RTKAAIEHLH QKILKITEQI
     KIEQEARDDN VAEYLKLANN ADKQQVSRIK QVFEKKNQKS AQTIAQLHKK LEHYRRRLKE
     IEQNGPSRQP KDVLRDMQQG LKDVGANMRA GISGFGGGVV EGVKGSLSGL SQATHTAVVS
     KPREFASLIR NKFGSADNIA HLKDPMEDGP PEEAARALSG SATLVSSPKY GSDDECSSAS
     ASSAGAGSNS GAGPGGALGS PRSNTLYGAP GNLDTLLEEL REIKEGQSHL EDSMEDLKTQ
     LQRDYTYMTQ CLQEERYRYE RLEEQLNDLT ELHQNEMTNL KQELASMEEK VAYQSYERAR
     DIQEAVESCL TRVTKLELQQ QQQQVVQLEG VENANARALL GKFINVILAL MAVLLVFVST
     IANFITPLMK TRLRITSTAL LLLVLFLLWK HWASLTYLLE HVLLPS
//
ID   WIPI2_MOUSE             Reviewed;         445 AA.
AC   Q80W47;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=WD repeat domain phosphoinositide-interacting protein 2;
DE            Short=WIPI-2;
GN   Name=Wipi2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Amnion, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394 AND SER-395, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Probable early component of the autophagy machinery
CC       being involved in formation of preautophagosomal structures and
CC       their maturation into mature phagosomes in response to PtdIns3P
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane;
CC       Peripheral membrane protein; Cytoplasmic side (By similarity).
CC       Note=Enriched at preautophagosomal structure membranes in response
CC       to ptdIns3P. Dissociates from mature phagosome membranes (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the WD repeat SVP1 family.
CC   -!- SIMILARITY: Contains 3 WD repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK155113; BAE33057.1; -; mRNA.
DR   EMBL; AK169051; BAE40839.1; -; mRNA.
DR   EMBL; AK172030; BAE42786.1; -; mRNA.
DR   EMBL; BC044894; AAH44894.1; -; mRNA.
DR   IPI; IPI00131321; -.
DR   RefSeq; NP_848485.1; NM_178398.4.
DR   UniGene; Mm.29432; -.
DR   ProteinModelPortal; Q80W47; -.
DR   PhosphoSite; Q80W47; -.
DR   PRIDE; Q80W47; -.
DR   Ensembl; ENSMUST00000036872; ENSMUSP00000045201; ENSMUSG00000029578.
DR   GeneID; 74781; -.
DR   KEGG; mmu:74781; -.
DR   UCSC; uc009aiy.1; mouse.
DR   CTD; 74781; -.
DR   MGI; MGI:1923831; Wipi2.
DR   eggNOG; roNOG13339; -.
DR   GeneTree; ENSGT00530000062939; -.
DR   HOGENOM; HBG443829; -.
DR   HOVERGEN; HBG056639; -.
DR   InParanoid; Q80W47; -.
DR   OMA; FNQDNTS; -.
DR   OrthoDB; EOG4S4PG4; -.
DR   PhylomeDB; Q80W47; -.
DR   NextBio; 341626; -.
DR   ArrayExpress; Q80W47; -.
DR   Bgee; Q80W47; -.
DR   CleanEx; MM_WIPI2; -.
DR   Genevestigator; Q80W47; -.
DR   GermOnline; ENSMUSG00000029578; Mus musculus.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0034045; C:pre-autophagosomal structure membrane; ISS:UniProtKB.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISS:UniProtKB.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR   GO; GO:0000045; P:autophagic vacuole assembly; ISS:UniProtKB.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00320; WD40; 3.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR   PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Autophagy; Membrane; Phosphoprotein; Repeat; WD repeat.
FT   CHAIN         1    445       WD repeat domain phosphoinositide-
FT                                interacting protein 2.
FT                                /FTId=PRO_0000051441.
FT   REPEAT      182    222       WD 1.
FT   REPEAT      228    267       WD 2.
FT   REPEAT      311    349       WD 3.
FT   MOD_RES     394    394       Phosphoserine.
FT   MOD_RES     395    395       Phosphoserine.
SQ   SEQUENCE   445 AA;  48477 MW;  A4D4FF973B104D93 CRC64;
     MNLASQSGEA GAGQLLFANF NQDNTSLAVG SKSGYKFFSL SSVDKLEQIY ECTDTEDVCI
     VERLFSSSLV AIVSLKAPRK LKVCHFKKGT EICNYSYSNT ILAVKLNRQR LIVCLEESLY
     IHNIRDMKVL HTIRETPPNP AGLCALSINN DNCYLAYPGS ASIGEVQVFD TINLRAANMI
     PAHDSPLAAL AFDASGTKLA TASEKGTVIR VFSIPEGQKL FEFRRGVKRC VSICSLAFSM
     DGMFLSASSN TETVHIFKLE AVREKPPEEP TTWTGYFGKV LMASTSYLPS QVTEMFNQGR
     AFATVRLPFC GHKNICSLTT IQKIPRLLVG ASDGYLYMYN LDPQEGGECA LMRQHRLDGS
     METTSEIVDS ASHDCPLATQ TYGTAAAKGA YVPSSPTRLG KGQDANLEAY TDDLGAVGGA
     CLEDEASALR LDEDSEHPPM ILRTD
//
ID   LRC8A_MOUSE             Reviewed;         810 AA.
AC   Q80WG5; A2AQZ0;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Leucine-rich repeat-containing protein 8A;
GN   Name=Lrrc8a; Synonyms=Lrrc8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=14660746; DOI=10.1172/JCI200318937;
RA   Sawada A., Takihara Y., Kim J.Y., Matsuda-Hashii Y., Tokimasa S.,
RA   Fujisaki H., Kubota K., Endo H., Onodera T., Ohta H., Ozono K.,
RA   Hara J.;
RT   "A congenital mutation of the novel gene LRRC8 causes
RT   agammaglobulinemia in humans.";
RL   J. Clin. Invest. 112:1707-1713(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Involved in B-cell development. Required for the pro-B
CC       cell to pre-B cell transition.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- TISSUE SPECIFICITY: High levels detected in the bone marrow; lower
CC       levels found in peripheral blood cells.
CC   -!- SIMILARITY: Contains 17 LRR (leucine-rich) repeats.
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CC   -----------------------------------------------------------------------
DR   EMBL; AL845258; CAM20568.1; -; Genomic_DNA.
DR   EMBL; CH466542; EDL08450.1; -; Genomic_DNA.
DR   EMBL; BC048152; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00126759; -.
DR   RefSeq; NP_808393.1; NM_177725.4.
DR   UniGene; Mm.389232; -.
DR   UniGene; Mm.475219; -.
DR   ProteinModelPortal; Q80WG5; -.
DR   SMR; Q80WG5; 396-802.
DR   STRING; Q80WG5; -.
DR   PhosphoSite; Q80WG5; -.
DR   PRIDE; Q80WG5; -.
DR   Ensembl; ENSMUST00000007620; ENSMUSP00000007620; ENSMUSG00000007476.
DR   Ensembl; ENSMUST00000095078; ENSMUSP00000092690; ENSMUSG00000007476.
DR   Ensembl; ENSMUST00000113654; ENSMUSP00000109284; ENSMUSG00000007476.
DR   GeneID; 241296; -.
DR   KEGG; mmu:241296; -.
DR   UCSC; uc008jbu.1; mouse.
DR   CTD; 241296; -.
DR   MGI; MGI:2652847; Lrrc8a.
DR   GeneTree; ENSGT00600000084236; -.
DR   HOGENOM; HBG445357; -.
DR   HOVERGEN; HBG052360; -.
DR   InParanoid; Q80WG5; -.
DR   OMA; QCRKLRT; -.
DR   OrthoDB; EOG45B1DW; -.
DR   PhylomeDB; Q80WG5; -.
DR   NextBio; 384965; -.
DR   ArrayExpress; Q80WG5; -.
DR   Bgee; Q80WG5; -.
DR   Genevestigator; Q80WG5; -.
DR   GermOnline; ENSMUSG00000007476; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0002329; P:pre-B cell differentiation; IMP:UniProtKB.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR021040; LRR_protein-8_N.
DR   Pfam; PF12534; DUF3733; 2.
DR   Pfam; PF00560; LRR_1; 3.
DR   SMART; SM00369; LRR_TYP; 2.
DR   PROSITE; PS51450; LRR; 11.
PE   1: Evidence at protein level;
KW   Acetylation; Differentiation; Glycoprotein; Leucine-rich repeat;
KW   Membrane; Phosphoprotein; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN         1    810       Leucine-rich repeat-containing protein
FT                                8A.
FT                                /FTId=PRO_0000084500.
FT   TRANSMEM     26     45       Helical; (Potential).
FT   TRANSMEM    124    146       Helical; (Potential).
FT   TRANSMEM    263    285       Helical; (Potential).
FT   TRANSMEM    320    342       Helical; (Potential).
FT   REPEAT      373    401       LRR 1.
FT   REPEAT      402    424       LRR 2.
FT   REPEAT      425    447       LRR 3.
FT   REPEAT      448    470       LRR 4.
FT   REPEAT      471    494       LRR 5.
FT   REPEAT      495    518       LRR 6.
FT   REPEAT      519    545       LRR 7.
FT   REPEAT      546    568       LRR 8.
FT   REPEAT      569    592       LRR 9.
FT   REPEAT      593    615       LRR 10.
FT   REPEAT      616    640       LRR 11.
FT   REPEAT      641    663       LRR 12.
FT   REPEAT      664    686       LRR 13.
FT   REPEAT      687    706       LRR 14.
FT   REPEAT      707    732       LRR 15.
FT   REPEAT      733    755       LRR 16.
FT   REPEAT      756    777       LRR 17.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     217    217       Phosphoserine.
FT   CARBOHYD     83     83       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    191    191       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    526    526       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    554    554       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    592    592       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    660    660       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    696    696       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    755    755       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   810 AA;  94120 MW;  E3B125BC9977DBB0 CRC64;
     MIPVTELRYF ADTQPAYRIL KPWWDVFTDY ISIVMLMIAV FGGTLQVTQD KMICLPCKWV
     TKDSCNDSFR GWAASSPEPT YPNSTVLPTP DTGPTGIKYD LDRHQYNYVD AVCYENRLHW
     FAKYFPYLVL LHTLIFLACS NFWFKFPRTS SKLEHFVSIL LKCFDSPWTT RALSETVVEE
     SDPKPAFSKM NGSMDKKSST VSEDVEATVP MLQRTKSRIE QGIVDRSETG VLDKKEGEQA
     KALFEKVKKF RTHVEEGDIV YRLYMRQTII KVIKFALIIC YTVYYVHNIK FDVDCTVDIE
     SLTGYRTYRC AHPLATLFKI LASFYISLVI FYGLICMYTL WWMLRRSLKK YSFESIREES
     SYSDIPDVKN DFAFMLHLID QYDPLYSKRF AVFLSEVSEN KLRQLNLNNE WTLDKLRQRL
     TKNAQDKLEL HLFMLSGIPD TVFDLVELEV LKLELIPDVT IPPSIAQLTG LKELWLYHTA
     AKIEAPALAF LRENLRALHI KFTDIKEIPL WIYSLKTLEE LHLTGNLSAE NNRYIVIDGL
     RELKRLKVLR LKSNLSKLPQ VVTDVGVHLQ KLSINNEGTK LIVLNSLKKM VNLTELELIR
     CDLERIPHSI FSLHNLQEID LKDNNLKTIE EIISFQHLHR LTCLKLWYNH IAYIPIQIGN
     LTNLERLYLN RNKIEKIPTQ LFYCRKLRYL DLSHNNLTFL PADIGLLQNL QNLAVTANRI
     EALPPELFQC RKLRALHLGN NVLQSLPSRV GELTNLTQIE LRGNRLECLP VELGECPLLK
     RSGLVVEEDL FSTLPPEVKE RLWRADKEQA
//
ID   LYRIC_MOUSE             Reviewed;         579 AA.
AC   Q80WJ7; B2RSG8; Q05CM0; Q3U9F8; Q3UAQ8; Q8BN67; Q8CBT9; Q8CDL0;
AC   Q8CGI7; Q9D052;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Protein LYRIC;
DE   AltName: Full=3D3/LYRIC;
DE   AltName: Full=Lysine-rich CEACAM1 co-isolated protein;
DE   AltName: Full=Metadherin;
DE   AltName: Full=Metastasis adhesion protein;
GN   Name=Mtdh; Synonyms=Lyric;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Mammary tumor;
RX   PubMed=15093543; DOI=10.1016/S1535-6108(04)00079-0;
RA   Brown D.M., Ruoslahti E.;
RT   "Metadherin, a cell surface protein in breast tumors that mediates
RT   lung metastasis.";
RL   Cancer Cell 5:365-374(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=129; TISSUE=Teratocarcinoma;
RX   PubMed=14980505; DOI=10.1016/j.yexcr.2003.11.020;
RA   Sutherland H.G.E., Lam Y.W., Briers S., Lamond A.I., Bickmore W.A.;
RT   "3D3/lyric: a novel transmembrane protein of the endoplasmic reticulum
RT   and nuclear envelope, which is also present in the nucleolus.";
RL   Exp. Cell Res. 294:94-105(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow macrophage, Embryo, Testis, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N; TISSUE=Colon, Embryo, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294 AND SER-297, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Downregulates SLC1A2/EAAT2 promoter activity when
CC       expressed ectopically. Activates the nuclear factor kappa-B (NF-
CC       kappa-B) transcription factor. Promotes anchorage-independent
CC       growth of immortalized melanocytes and astrocytes which is a key
CC       component in tumor cell expansion. Promotes lung metastasis and
CC       also has an effect on bone and brain metastasis, possibly by
CC       enhancing the seeding of tumor cells to the target organ
CC       endothelium. Induces chemoresistance (By similarity).
CC   -!- SUBUNIT: Interacts with BCIPP, CREBBP/CBP and RELA/p65 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       membrane protein (By similarity). Nucleus membrane; Single-pass
CC       membrane protein (By similarity). Cell junction, tight junction
CC       (By similarity). Nucleus, nucleolus (By similarity). Cytoplasm,
CC       perinuclear region (By similarity). Note=In epithelial cells,
CC       recruited to tight junctions (TJ) during the maturation of the TJ
CC       complexes. A nucleolar staining may be due to nuclear targeting of
CC       an isoform lacking the transmembrane domain. TNF-alpha causes
CC       translocation from the cytoplasm to the nucleus (By similarity).
CC   -!- TISSUE SPECIFICITY: In the mammary gland, expressed at the apical
CC       surface of epithelial cells lining ducts, as well as in the
CC       mammary fat pad. Not detected in the spleen, kidney, lung, or
CC       skin; minute amounts seen in the liver. Expressed in Purkinje
CC       neurons in the early postnatal and adult cerebellum. Overexpressed
CC       in mammary tumors (at protein level).
CC   -!- CAUTION: Was originally (PubMed:15093543) thought to be a type II
CC       membrane protein but this is inconsistent with the results of
CC       multiple phosphorylation studies because this topology would
CC       locate the phosphorylation sites in the lumen or extracellularly
CC       rather than in the cytoplasm.
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DR   EMBL; AY553638; AAS68097.1; -; mRNA.
DR   EMBL; AF501309; AAP30790.1; -; mRNA.
DR   EMBL; AK011808; BAB27854.1; -; mRNA.
DR   EMBL; AK029915; BAC26673.1; -; mRNA.
DR   EMBL; AK035302; BAC29022.1; -; mRNA.
DR   EMBL; AK151269; BAE30256.1; -; mRNA.
DR   EMBL; AK151810; BAE30709.1; -; mRNA.
DR   EMBL; BC023115; AAH23115.1; -; mRNA.
DR   EMBL; BC036994; AAH36994.1; -; mRNA.
DR   EMBL; BC138858; AAI38859.1; -; mRNA.
DR   EMBL; BC138859; AAI38860.1; -; mRNA.
DR   IPI; IPI00330599; -.
DR   RefSeq; NP_080278.3; NM_026002.4.
DR   UniGene; Mm.130883; -.
DR   ProteinModelPortal; Q80WJ7; -.
DR   STRING; Q80WJ7; -.
DR   PhosphoSite; Q80WJ7; -.
DR   PRIDE; Q80WJ7; -.
DR   Ensembl; ENSMUST00000022865; ENSMUSP00000022865; ENSMUSG00000022255.
DR   GeneID; 67154; -.
DR   KEGG; mmu:67154; -.
DR   UCSC; uc007vlh.1; mouse.
DR   CTD; 67154; -.
DR   MGI; MGI:1914404; Mtdh.
DR   eggNOG; roNOG05036; -.
DR   GeneTree; ENSGT00390000004343; -.
DR   HOVERGEN; HBG052379; -.
DR   InParanoid; Q80WJ7; -.
DR   OMA; KKKQGED; -.
DR   OrthoDB; EOG4WWRJD; -.
DR   PhylomeDB; Q80WJ7; -.
DR   NextBio; 323742; -.
DR   ArrayExpress; Q80WJ7; -.
DR   Bgee; Q80WJ7; -.
DR   CleanEx; MM_MTDH; -.
DR   Genevestigator; Q80WJ7; -.
DR   GermOnline; ENSMUSG00000022255; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0051059; F:NF-kappaB binding; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
PE   1: Evidence at protein level;
KW   Cell junction; Cytoplasm; Endoplasmic reticulum; Membrane; Nucleus;
KW   Phosphoprotein; Tight junction; Transmembrane; Transmembrane helix.
FT   CHAIN         1    579       Protein LYRIC.
FT                                /FTId=PRO_0000084534.
FT   TOPO_DOM      1     48       Lumenal (Potential).
FT   TRANSMEM     49     69       Helical; (Potential).
FT   TOPO_DOM     70    579       Cytoplasmic (Potential).
FT   REGION        1     71       Activation of NF-kappa-B (By similarity).
FT   REGION       72    168       Interaction with BCCIP (By similarity).
FT   REGION      100    204       Interaction with RELA (By similarity).
FT   REGION      378    440       Lung-homing for mammary tumors.
FT   COMPBIAS     59     67       Poly-Leu.
FT   COMPBIAS    438    448       Poly-Lys.
FT   COMPBIAS    570    574       Poly-Lys.
FT   MOD_RES     294    294       Phosphoserine.
FT   MOD_RES     297    297       Phosphoserine.
FT   MOD_RES     341    341       Phosphoserine (By similarity).
FT   MOD_RES     366    366       Phosphoserine (By similarity).
FT   MOD_RES     423    423       Phosphoserine.
FT   MOD_RES     565    565       Phosphoserine (By similarity).
FT   CONFLICT    190    190       A -> I (in Ref. 3; BAB27854).
FT   CONFLICT    264    264       G -> R (in Ref. 3; BAE30709).
FT   CONFLICT    271    271       S -> T (in Ref. 3; BAC26673).
FT   CONFLICT    296    296       L -> F (in Ref. 3; BAE30709).
SQ   SEQUENCE   579 AA;  63846 MW;  E47E98303F588126 CRC64;
     MAARSWQDEL AQQAEEGSAR LRELLSVGLG FLRTELGLDL GLEPKRYPGW VILVGTGALG
     LLLLFLLGYG WAAACAGARK KRRSPPRKRE EAAPPTPAPD DLAQLKNLRS EEQKKKNRKK
     LPEKPKPNGR TVEVPEDEVV RNPRSITAKQ APETDKKNEK SKKNKKKSKS DAKAVQNSSR
     HDGKEVDEGA WETKISHREK RQQRKRDKVL TDSGSLDSTI PGIENIITVT TEQLTTASFP
     VGSKKNKGDS HLNVQVSNFK SGKGDSTLQV SSRLNENLTV NGGGWSEKSV KLSSQLSEEK
     WNSVPPASAG KRKTEPSAWT QDTGDTNANG KDWGRNWSDR SIFSGIGSTA EPVSQSTTSD
     YQWDVSRNQP YIDDEWSGLN GLSSADPSSD WNAPAEEWGN WVDEDRASLL KSQEPISNDQ
     KVSDDDKEKG EGALPTGKSK KKKKKKKKQG EDNSHTQDTE DLEKDTREEL PVNTSKARPK
     QEKACSLKTM STSDPAEVLI KNSQPVKTLP PAISAEPSIT LSKGDSDNSS SQVPPMLQDT
     DKPKSNAKQN SVPPSQTKSE TNWESPKQIK KKKKARRET
//
ID   K1456_MOUSE             Reviewed;         447 AA.
AC   Q80WQ4; Q5DTX8; Q8CA94; Q8CAM3;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Putative methyltransferase KIAA1456;
DE            EC=2.1.1.-;
GN   Name=Kiaa1456;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, Hypothalamus, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q80WQ4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80WQ4-2; Sequence=VSP_032795;
CC       Name=3;
CC         IsoId=Q80WQ4-3; Sequence=VSP_032796, VSP_032797;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90446.1; Type=Erroneous initiation;
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DR   EMBL; AK038497; BAC30018.1; -; mRNA.
DR   EMBL; AK039253; BAC30293.1; -; mRNA.
DR   EMBL; AK141601; BAE24758.1; -; mRNA.
DR   EMBL; AK220392; BAD90446.1; ALT_INIT; mRNA.
DR   EMBL; BC052184; AAH52184.1; -; mRNA.
DR   IPI; IPI00330620; -.
DR   IPI; IPI00881848; -.
DR   IPI; IPI00890279; -.
DR   RefSeq; NP_795926.2; NM_176952.4.
DR   UniGene; Mm.180924; -.
DR   ProteinModelPortal; Q80WQ4; -.
DR   SMR; Q80WQ4; 13-146.
DR   PRIDE; Q80WQ4; -.
DR   Ensembl; ENSMUST00000036363; ENSMUSP00000046985; ENSMUSG00000039620.
DR   GeneID; 319582; -.
DR   KEGG; mmu:319582; -.
DR   UCSC; uc009llm.1; mouse.
DR   MGI; MGI:2442328; 6430573F11Rik.
DR   eggNOG; roNOG12011; -.
DR   GeneTree; ENSGT00530000063536; -.
DR   HOGENOM; HBG714071; -.
DR   HOVERGEN; HBG055799; -.
DR   InParanoid; Q80WQ4; -.
DR   OMA; NRALCSQ; -.
DR   OrthoDB; EOG4SBDZ7; -.
DR   PhylomeDB; Q80WQ4; -.
DR   NextBio; 395024; -.
DR   ArrayExpress; Q80WQ4; -.
DR   Bgee; Q80WQ4; -.
DR   Genevestigator; Q80WQ4; -.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR013216; Methyltransf_11.
DR   Pfam; PF08241; Methyltransf_11; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Methyltransferase; Transferase.
FT   CHAIN         1    447       Putative methyltransferase KIAA1456.
FT                                /FTId=PRO_0000328793.
FT   VAR_SEQ       1     87       Missing (in isoform 2).
FT                                /FTId=VSP_032795.
FT   VAR_SEQ     110    110       V -> G (in isoform 3).
FT                                /FTId=VSP_032796.
FT   VAR_SEQ     111    447       Missing (in isoform 3).
FT                                /FTId=VSP_032797.
FT   CONFLICT    184    184       R -> T (in Ref. 2; BAD90446).
FT   CONFLICT    274    274       A -> G (in Ref. 2; BAD90446).
FT   CONFLICT    337    337       G -> E (in Ref. 2; BAD90446).
SQ   SEQUENCE   447 AA;  50277 MW;  831CE496E09C7165 CRC64;
     MDPEAVELEK RHVHSVYENT APYFTDLQSK AWPRVRQFLQ DQKPGSLVAD IGCGTGKYLK
     VNSQVHTLGC DYCGPLVEIA RNRGCEVMVC DNLNLPFRDQ GFDAIISIGV IHHFSTKERR
     IRAIKEMARV LAPGGQLMIY VWAMEQKNRR FEKQDVLVPW NRALCSRLLS ESHQSWGHHC
     EHPRSRGFQG PGSVCGCAVC FKGRCDSKRS HSMDYGSAVA RTCCEAISKE GERENGLYSN
     FGKSFRSWFF SRSLDESTLR KQIERVRPMK IPEAWANSTV SQQPSRHPSL DLHAPEPFST
     KGPNLDEVFV DTSSQRHLGW LRTPGTSDNF SGHKGGGSRR KEGGNFLDIT DTGDSVAASN
     SSDPSARKIL RRVSAFDSND SNSEDSSFLE AQRDATDSKA FMRYYHVFRE GELSSLLQES
     VSELQVLSSG NDHGNWCIIA EKKRSWD
//
ID   Q80WR0_MOUSE            Unreviewed;      1462 AA.
AC   Q80WR0;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   11-JAN-2011, entry version 55.
DE   SubName: Full=Nucleoporin 153;
GN   Name=Nup153;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC052173; AAH52173.1; -; mRNA.
DR   IPI; IPI00330624; -.
DR   UniGene; Mm.255398; -.
DR   ProteinModelPortal; Q80WR0; -.
DR   SMR; Q80WR0; 709-745, 770-814, 846-881.
DR   STRING; Q80WR0; -.
DR   PhosphoSite; Q80WR0; -.
DR   PRIDE; Q80WR0; -.
DR   Ensembl; ENSMUST00000021803; ENSMUSP00000021803; ENSMUSG00000021374.
DR   UCSC; uc007qhj.1; mouse.
DR   MGI; MGI:2385621; Nup153.
DR   HOGENOM; HBG444915; -.
DR   HOVERGEN; HBG052679; -.
DR   InParanoid; Q80WR0; -.
DR   NextBio; 376192; -.
DR   ArrayExpress; Q80WR0; -.
DR   Bgee; Q80WR0; -.
DR   Genevestigator; Q80WR0; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR013913; Nucleoporin_Nup153.
DR   InterPro; IPR018892; Retro-transposon_transp_CS.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   Pfam; PF08604; Nup153; 1.
DR   Pfam; PF10599; Nup_retrotrp_bd; 1.
DR   Pfam; PF00641; zf-RanBP; 4.
DR   SMART; SM00547; ZnF_RBZ; 4.
DR   PROSITE; PS01358; ZF_RANBP2_1; 4.
DR   PROSITE; PS50199; ZF_RANBP2_2; 4.
PE   1: Evidence at protein level;
SQ   SEQUENCE   1462 AA;  152068 MW;  FF8E959D0B09018E CRC64;
     MASEAGGIGG GGGGGKIRTR RCHQGPVKPY QQGRPQHQGI LSRVTESVKN IVPGWLQRYF
     NKSENACSCS PDADEVPPWP ENREDEHAIY ADENTNTDDG RITPDPAGSN TEEPSTTSTA
     SNYPDVLTRP SLHRSHLNFS VLESPALHCQ PSTSSAFPIG SSGFSLVKEI KDSTFQHDDD
     NISTTSGFSS RASEKDIAVS KNTSLPPLWS PEAERSHSLS QHTAISSKKP AFNLSAFGTL
     STSLGNSSIL KTSQLGDSPF YPGKTTYGGA AAAVRQNKVR STPYQAPVRR QMKAKQLNAQ
     SYGVTSSTAR RILQSLEKMS SPLADAKRIP SAVSSPLNSP LDRSGIDNTV FQAKKEKVDS
     QYPPVQRLMT PKPVSIATNR TVYFKPSLTP SGDLRKTNQR IDKKNSTVDE KSISRQNREQ
     ESGFSYPNFS IPAANGLSSG VGGGGGKMRR ERTHFVAPKP PENEEVEAPL LPQISLPISS
     SSLPTFSFSS PVTSASPSPV SSSQPLPNKV QMTSLGSTGS PVFTFSSPIV KSTQAAVLPP
     ASIGFTFSVP LAKTEFSGSN SSSETVLSSS AQDITAVNSS SYKKRSAPCE DPFTPAKILR
     EGSVLDILKT PGFASPKVDS PALQPTTTSS IVYTRPAIST FSSSGIEYGE SLKAGSSWQC
     DTCLLQNKVT DNKCIACQAA KLPLKETAKQ TGTGTPSKSD KPASTSGTGF GDKFKPAIGT
     WDCDTCLVQN KPEAVKCVAC ETPKPGTGVK RALTLTVASE SPVTASSSTT VTTGTLGFGD
     KFKRPVGSWE CPVCCVCNKA EDNRCVSCTS EKPGLVSASS SSPAPVSLSS GGCLGLDKFK
     KPEGSWDCEV CLVQNKADSA KCIACESAKP GTKSEFKGFG TSSSLNPAPS AFKFGIPSSS
     SGLSQTLTST GNFKFGDQGG FKLGTSSDSG STNTMNTNFK FSKPTGDFKF GVLSDSKPEE
     VKNDNKNDNF QFGSSSGLTN PASSAPFQFG VSTLGQQEKK EELPKSSPAG FSFGAGVNNP
     PNAAIDTTAT SENKSGFNFG TLDTKSVSVT PFTYKTTEAK KEDAPATKGG FTFGKVGSSS
     LPSSSMFVLG RTEEKQQEPV TSTSLVFGKK ADSEEPKCQP VFSFGNSEQT KDESSKPTFS
     FSVAKPSGKE SEQLAKATFA FGNQTNTTTD QGAAKPVFSF LNSSSSSSSA PATSSSGGIF
     GSSTSSSNPP VAAFVFGQAS NPVSSSAFGN AAESSTSQSL LFPQESEPAT TSSTAPAASP
     FVFGTGASSN SVSSGFTFGA TTTSSSSGSS FVFGTGHSAP SASPAFGANQ TPTFGQSQGA
     SQPNPPSFGS ISSSTALFSA GSQPVPPPIF GTVSSSSQPP VFGQQPSQSA FGSGTANASS
     VFQFGSSTTN FNFTNNNPSG VFTFGASPST PAASAQPSGS GVFSFSQSPA SFTVGSNGKN
     MFSSSGTSVS GRKIKTAVRR KK
//
ID   JPH4_MOUSE              Reviewed;         628 AA.
AC   Q80WT0; Q8BMI1;
DT   09-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Junctophilin-4;
DE            Short=JP-4;
DE   AltName: Full=Junctophilin-like 1 protein;
GN   Name=Jph4; Synonyms=Jphl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Forelimb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane
CC       protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80WT0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80WT0-2; Sequence=VSP_008197, VSP_008198;
CC         Note=Due to intron retention. No experimental confirmation
CC         available;
CC   -!- DOMAIN: The MORN (membrane occupation and recognition nexus)
CC       repeats contribute to the plasma membrane binding, possibly by
CC       interacting with phospholipids (By similarity).
CC   -!- SIMILARITY: Belongs to the junctophilin family.
CC   -!- SIMILARITY: Contains 8 MORN repeats.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK031092; BAC27249.1; -; mRNA.
DR   EMBL; BC052049; AAH52049.1; -; mRNA.
DR   EMBL; BC052376; AAH52376.1; -; mRNA.
DR   EMBL; BC052722; AAH52722.1; -; mRNA.
DR   IPI; IPI00223030; -.
DR   IPI; IPI00330641; -.
DR   RefSeq; NP_001003829.1; NM_001003829.2.
DR   RefSeq; NP_796023.2; NM_177049.4.
DR   UniGene; Mm.19047; -.
DR   ProteinModelPortal; Q80WT0; -.
DR   SMR; Q80WT0; 79-145, 280-342.
DR   STRING; Q80WT0; -.
DR   PRIDE; Q80WT0; -.
DR   Ensembl; ENSMUST00000022819; ENSMUSP00000022819; ENSMUSG00000022208.
DR   GeneID; 319984; -.
DR   KEGG; mmu:319984; -.
DR   UCSC; uc007tyg.1; mouse.
DR   UCSC; uc007tyi.1; mouse.
DR   CTD; 319984; -.
DR   MGI; MGI:2443113; Jph4.
DR   GeneTree; ENSGT00600000084242; -.
DR   HOGENOM; HBG715737; -.
DR   HOVERGEN; HBG031648; -.
DR   InParanoid; Q80WT0; -.
DR   OMA; WGPFSSP; -.
DR   OrthoDB; EOG4T4CV7; -.
DR   PhylomeDB; Q80WT0; -.
DR   NextBio; 395782; -.
DR   ArrayExpress; Q80WT0; -.
DR   Bgee; Q80WT0; -.
DR   CleanEx; MM_JPH4; -.
DR   Genevestigator; Q80WT0; -.
DR   GermOnline; ENSMUSG00000022208; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   InterPro; IPR017191; Junctophilin.
DR   InterPro; IPR003409; MORN.
DR   Pfam; PF02493; MORN; 8.
DR   PIRSF; PIRSF037387; Junctophilin; 1.
DR   SMART; SM00698; MORN; 6.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Membrane; Repeat; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    628       Junctophilin-4.
FT                                /FTId=PRO_0000159853.
FT   TOPO_DOM      1    606       Cytoplasmic (Potential).
FT   TRANSMEM    607    628       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   REPEAT       15     37       MORN 1.
FT   REPEAT       39     60       MORN 2.
FT   REPEAT       61     82       MORN 3.
FT   REPEAT       83    105       MORN 4.
FT   REPEAT      106    128       MORN 5.
FT   REPEAT      129    151       MORN 6.
FT   REPEAT      282    304       MORN 7.
FT   REPEAT      305    327       MORN 8.
FT   COMPBIAS    170    180       Poly-Pro.
FT   VAR_SEQ     385    406       AADALLKAVAASSVAEKAVEAA -> WASGAQIQLGLRGEV
FT                                PLGTNHT (in isoform 2).
FT                                /FTId=VSP_008197.
FT   VAR_SEQ     407    628       Missing (in isoform 2).
FT                                /FTId=VSP_008198.
SQ   SEQUENCE   628 AA;  66000 MW;  97B6BEA4A02C6143 CRC64;
     MSPGGKFDFD DGGCYVGGWE AGRAHGYGVC TGPGAQGEYS GCWAHGFESL GVFTGPGGHS
     YQGHWQQGKR EGLGVERKSR WTYRGEWLGG LKGRSGVWES VSGLRYAGLW KDGFQDGYGT
     ETYSDGGTYQ GQWQAGKRHG YGVRQSVPYH QAALLRSPRR TSLDSGHSDP PTPPPPLPLP
     GDEGGSPASG SRGGFVLAGP GDADGASSRK RTPAAGGFFR RSLLLSGLRA GGRRSSLGSK
     RGSLRSEVSS EVGSTGPPGS EASGPPIPAP PALIEGSATE VYAGEWRADR RSGYGVSQRS
     NGLRYEGEWL GNRRHGYGRT TRPDGSREEG KYKRNRLVHG GRVRSLLPLA LRRGKVKEKV
     DRAVEGARRA VSAARQRQEI AAARAADALL KAVAASSVAE KAVEAARMAK LIAQDLQPML
     EAPGRRPRQD SGGSDTEPLD EDSPGVYENG LTPSEGSPEL PSSPASSHQP WRAPACRSPL
     PPGGNWGPFS SPKAWPEEWG GPGEQAEELA GYEAEDEAGV QGPGPRDGSP LLGGCSDSSG
     SLREEEGEDE ESLPQLRAPG GSESEPVTTP VLRGLSSRGP DAGCLTEEVE EPAPTERPAQ
     PGAANPLVVG AVALLDLSLA FLFSQLLT
//
ID   AFTIN_MOUSE             Reviewed;         931 AA.
AC   Q80WT5; Q5SSE6; Q99KJ1;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Aftiphilin;
GN   Name=Aftph; Synonyms=Afth;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May play a role in membrane trafficking (By similarity).
CC   -!- SUBUNIT: Interacts with GGA1, GGA3, AP1G1 and AP1G2 via their GAE
CC       domain (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=Colocalizes
CC       with AP1G1 and clathrin (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80WT5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80WT5-2; Sequence=VSP_013242;
CC   -!- DOMAIN: The WXXF motifs mediate binding of accessory proteins to
CC       the ear-domain of AP-1, GGAs and AP-2 through hydrophobic
CC       interactions. Selective binding to the GAE domains of AP-1 or to
CC       the alpha-ear domain of AP-2 is tuned by the acidic context
CC       surrounding the motif and the properties of the second residue of
CC       the motif itself (By similarity).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI24910.1; Type=Erroneous gene model prediction;
CC       Sequence=CAI25738.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL663115; CAI25737.1; -; Genomic_DNA.
DR   EMBL; AL645599; CAI25737.1; JOINED; Genomic_DNA.
DR   EMBL; AL663115; CAI25738.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL645599; CAI25738.1; JOINED; Genomic_DNA.
DR   EMBL; AL645599; CAI24909.1; -; Genomic_DNA.
DR   EMBL; AL663115; CAI24909.1; JOINED; Genomic_DNA.
DR   EMBL; AL645599; CAI24910.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL663115; CAI24910.1; JOINED; Genomic_DNA.
DR   EMBL; BC004630; AAH04630.1; -; mRNA.
DR   EMBL; BC052036; AAH52036.1; -; mRNA.
DR   IPI; IPI00314905; -.
DR   IPI; IPI00555087; -.
DR   RefSeq; NP_852076.1; NM_181411.2.
DR   UniGene; Mm.356580; -.
DR   ProteinModelPortal; Q80WT5; -.
DR   MINT; MINT-1344435; -.
DR   STRING; Q80WT5; -.
DR   PhosphoSite; Q80WT5; -.
DR   PRIDE; Q80WT5; -.
DR   Ensembl; ENSMUST00000035350; ENSMUSP00000036778; ENSMUSG00000049659.
DR   Ensembl; ENSMUST00000094376; ENSMUSP00000091938; ENSMUSG00000049659.
DR   GeneID; 216549; -.
DR   KEGG; mmu:216549; -.
DR   UCSC; uc007idh.1; mouse.
DR   CTD; 216549; -.
DR   MGI; MGI:1923012; Aftph.
DR   HOGENOM; HBG445096; -.
DR   HOVERGEN; HBG050464; -.
DR   InParanoid; Q80WT5; -.
DR   OMA; REQCKTE; -.
DR   OrthoDB; EOG4PVNZ0; -.
DR   NextBio; 375204; -.
DR   ArrayExpress; Q80WT5; -.
DR   Bgee; Q80WT5; -.
DR   CleanEx; MM_AFTPH; -.
DR   Genevestigator; Q80WT5; -.
DR   GermOnline; ENSMUSG00000049659; Mus musculus.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Phosphoprotein; Protein transport;
KW   Repeat; Transport.
FT   CHAIN         1    931       Aftiphilin.
FT                                /FTId=PRO_0000064489.
FT   REGION      821    825       Clathrin-binding (Potential).
FT   MOTIF        28     31       WXXF motif 1.
FT   MOTIF       433    436       WXXF motif 2.
FT   MOTIF       476    479       WXXF motif 3.
FT   MOD_RES     151    151       Phosphoserine.
FT   MOD_RES     515    515       Phosphoserine (By similarity).
FT   MOD_RES     613    613       Phosphothreonine (By similarity).
FT   VAR_SEQ     815    841       Missing (in isoform 2).
FT                                /FTId=VSP_013242.
SQ   SEQUENCE   931 AA;  101131 MW;  FE1C64F3B7270620 CRC64;
     MEPDIIRMYS SSPPPLDNGA EDDEEDEFGE FGGFSEVSPS GVGFVDFDTP DYTRPKEDFV
     PSNHFMPIHE YSEDVDSLTS FKSVQNGNDK DITAELSTPV KSQSDVVLST TSKEMIPSKT
     LDPSIDGMES LEDLDKVVVQ GPSTGQLRSF SPGDFRTDKN IVHQTKQLES CNGEKPPCLE
     ILTNGFAGLE TVNPQGTDDL DNVADSKGSK PLNTCGTECI LESAASHATE FADFSTFSQT
     ERTQLEEIEC PVLNDGDTLT IQGNSKGPRV KELNCVKEVT LDGSFEDTGN TEREHQVCVS
     EIHAVADRGL SVEKQDLQTL QQDEFLNSRI QSEAWSLVDS SENSEAITKE RCKMEKNDLF
     ASKCADLSMD SVKTSDVNEI GSSKEENRKL TNPKSPDPDP TGQNALDDSA ASMKNGDSGN
     GFVTCHDTNE DDFGDFGTAN GTTPPFVTST QDSMSDVTFE DSSEHFLHLS EPGDDFGEFE
     DTNAVSCQEE MRFTESDLRQ TSDGLSEECP LAGESGGKDS KPDSKLKNGQ DSEFGDFDSV
     PNTQGSAFQD SDDFADFSSA GPSQAVDWNA FEDEQKDGCS WAAFGDQQET ESHHLKEVWQ
     SQRTDETMGT LGTPKMHSVS SAASKGAVAS GHLQEPGTSV QTALLNRLER IFEACFPSVF
     VPDVEEEVSS LKHLLETHSS PAKTREALAD RGELRGVWTE LQDIHDAHGL RYQWGGSHSN
     KKLLCSLGID TRNILFTGNK KQPVIVPMYA AGLGMLEPTK EPLKPLSAAE KIASIGQTTV
     MTPEINTCTS DPFQESLPPV QFDWSSSGLT NPLDASGGST LLNLDFFGPV DDSSSSSSTI
     PGVDPELYEL TTAKLETSTS SLRVTDAFAK LMSTVEKTST STRKPKREEH LSEEAMKVIA
     SLPDLTFMHA KVLMFPATLT PSMSSQEQAD A
//
ID   SRRM3_MOUSE             Reviewed;         648 AA.
AC   Q80WV7; Q9CUV5; Q9JJ91;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   RecName: Full=Serine/arginine repetitive matrix protein 3;
GN   Name=Srrm3; ORFNames=MNCb-4760;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S.,
RA   Hashimoto K.;
RT   "Isolation of full-length cDNA clones from mouse brain cDNA library
RT   made by oligo-capping method.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 113-231.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80WV7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80WV7-2; Sequence=VSP_034270, VSP_034271;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the CWC21 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB29002.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB041661; BAA95106.1; -; mRNA.
DR   EMBL; BC051947; AAH51947.1; -; mRNA.
DR   EMBL; AK013812; BAB29002.1; ALT_INIT; mRNA.
DR   IPI; IPI00475184; -.
DR   IPI; IPI00874513; -.
DR   RefSeq; NP_067378.2; NM_021403.3.
DR   UniGene; Mm.271230; -.
DR   ProteinModelPortal; Q80WV7; -.
DR   PRIDE; Q80WV7; -.
DR   Ensembl; ENSMUST00000013615; ENSMUSP00000013615; ENSMUSG00000039860.
DR   Ensembl; ENSMUST00000111157; ENSMUSP00000106787; ENSMUSG00000090184.
DR   GeneID; 58212; -.
DR   KEGG; mmu:58212; -.
DR   UCSC; uc008zzc.1; mouse.
DR   CTD; 58212; -.
DR   MGI; MGI:1920309; Srrm3.
DR   eggNOG; roNOG15827; -.
DR   GeneTree; ENSGT00580000081375; -.
DR   InParanoid; Q80WV7; -.
DR   OMA; APPDAAN; -.
DR   OrthoDB; EOG48PMMW; -.
DR   PhylomeDB; Q80WV7; -.
DR   NextBio; 314211; -.
DR   ArrayExpress; Q80WV7; -.
DR   Bgee; Q80WV7; -.
DR   Genevestigator; Q80WV7; -.
DR   InterPro; IPR013170; mRNA_splic_Cwf21.
DR   Pfam; PF08312; cwf21; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing.
FT   CHAIN         1    648       Serine/arginine repetitive matrix protein
FT                                3.
FT                                /FTId=PRO_0000341376.
FT   COMPBIAS    169    241       Lys-rich.
FT   COMPBIAS    256    645       Ser-rich.
FT   COMPBIAS    372    577       Arg-rich.
FT   VAR_SEQ     112    112       I -> M (in isoform 2).
FT                                /FTId=VSP_034270.
FT   VAR_SEQ     113    648       Missing (in isoform 2).
FT                                /FTId=VSP_034271.
FT   CONFLICT     93     93       Q -> P (in Ref. 1; BAA95106).
SQ   SEQUENCE   648 AA;  71104 MW;  AA30FC7A02C070AE CRC64;
     MSSTVNNGAT GMPAPPDAAN GFPQPGASSG SWPRAEEELR AAEPGLVKRA HREILDHERK
     RRVELKCMEL QEMMEEQGYS EEEIRQKVGT FRQMLMEKEG VLTREDRPGA HIVAETPRRM
     EGLEPGLEYP PFDEDDGPVD CDCPVSCYRG HRGYRTKHWS SSSASPPPKK KKKKKGSHRR
     SRKKRRLESE CSCGSASPLR KKKKNVKKHR RDRSDSGSRR KRRYRSRSLK SKRKEKNKER
     KRPHTESPGR RFHHHSSASS HSPSMSSHYS DSGSPSRLSP KHRDDGRKTG SQRSSGSRSP
     SPSGGSGWGS PQQNGGSRQR SGAHGGRPGS AHSPPDKPSS PRACDKAAAA PTPPARGKDS
     QSPRSAPSSQ GRGGRAAGGT ARRRRRRRRR RRSRSSANAP RRRGRRRTKP APPRGSSRSL
     SGAHSSSDSG GGAPGPGPEP CSERGHGGHG KRAKERPPRA RPASTSPSPG TRGRRGGPEG
     NSSSRSPGPH QGSWSSSRSP SKSHSRSPDK RTRSPSLSPS PKKPLGRDKD SEGRARHAEA
     EAARTRRRSR SYSPIRKRRR DSPSFMEPRR ITSARKRPIP YYRPSPSSSS SCLSTDYSSR
     SHSRSPSPGH SHGSYSSRSH GTRSRSCSAS RSRSPSYHSR SSSESGGF
//
ID   CE024_MOUSE             Reviewed;         188 AA.
AC   Q80X32; Q8C2G2;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-FEB-2011, entry version 50.
DE   RecName: Full=UPF0461 protein C5orf24 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster / NIH;
RA   Konstantinopoulou V.;
RT   "Physical and hematopoietic transcript map of a 5q31 critical
RT   subregion associated with the 5q- syndrome.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-78.
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the UPF0461 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC40508.2; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ492504; CAD37799.1; -; mRNA.
DR   EMBL; BC051430; AAH51430.1; -; mRNA.
DR   EMBL; AK088693; BAC40508.2; ALT_INIT; mRNA.
DR   IPI; IPI00330644; -.
DR   RefSeq; NP_851795.1; NM_181278.2.
DR   UniGene; Mm.28449; -.
DR   ProteinModelPortal; Q80X32; -.
DR   PhosphoSite; Q80X32; -.
DR   PRIDE; Q80X32; -.
DR   Ensembl; ENSMUST00000109900; ENSMUSP00000105526; ENSMUSG00000045767.
DR   GeneID; 78521; -.
DR   KEGG; mmu:78521; -.
DR   UCSC; uc007qrx.1; mouse.
DR   MGI; MGI:1925771; B230219D22Rik.
DR   eggNOG; roNOG07229; -.
DR   GeneTree; ENSGT00390000014889; -.
DR   HOGENOM; HBG715907; -.
DR   HOVERGEN; HBG097615; -.
DR   InParanoid; Q80X32; -.
DR   OMA; HKPIACQ; -.
DR   NextBio; 349015; -.
DR   ArrayExpress; Q80X32; -.
DR   Bgee; Q80X32; -.
DR   CleanEx; MM_B230219D22RIK; -.
DR   Genevestigator; Q80X32; -.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    188       UPF0461 protein C5orf24 homolog.
FT                                /FTId=PRO_0000295709.
FT   MOD_RES      37     37       Phosphoserine (By similarity).
FT   MOD_RES     187    187       Phosphoserine.
SQ   SEQUENCE   188 AA;  20139 MW;  ECAB59940BCBD7AC CRC64;
     MMHPVAGSNP AFCGPGKPSC LNEDAMRAAD QFDLYSSQQN KYSHTVSHKP MVCQRQDPLN
     ETHLQPTSGR NIEIKDELKK KKNLNRSGKR GRPSGTTKSA GYRTSTGRPL GTTKAAGFKT
     SPGRPLGTTK AAGYKVSPGR PPGSIKALSR LADLGYGCGT AAFPYPMMHS RVVHGLQETS
     GEVKPPSE
//
ID   UBP2L_MOUSE             Reviewed;        1107 AA.
AC   Q80X50; Q8BIT6; Q8BIW4; Q8BJ01; Q8CIG7; Q8K102; Q9CRT6;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Ubiquitin-associated protein 2-like;
GN   Name=Ubap2l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic head, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), AND
RP   VARIANT SER-374.
RC   STRAIN=C57BL/6, and FVB/N;
RC   TISSUE=Brain, Eye, Mammary gland, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-625 AND SER-629, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [6]
RP   STRUCTURE BY NMR OF 19-109.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of RSGI RUH-015, a UBA domain from mouse cDNA.";
RL   Submitted (SEP-2005) to the PDB data bank.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q80X50-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80X50-2; Sequence=VSP_019418, VSP_019421;
CC       Name=3;
CC         IsoId=Q80X50-3; Sequence=VSP_019419, VSP_019422;
CC       Name=4;
CC         IsoId=Q80X50-4; Sequence=VSP_019423;
CC       Name=5;
CC         IsoId=Q80X50-5; Sequence=VSP_019420;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 UBA domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC37777.1; Type=Frameshift; Positions=444, 462, 476;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK014274; BAB29236.1; -; mRNA.
DR   EMBL; AK048286; BAC33295.1; -; mRNA.
DR   EMBL; AK079895; BAC37777.1; ALT_FRAME; mRNA.
DR   EMBL; AK088702; BAC40514.1; -; mRNA.
DR   EMBL; BC023906; AAH23906.1; -; mRNA.
DR   EMBL; BC029075; AAH29075.1; -; mRNA.
DR   EMBL; BC050910; AAH50910.1; -; mRNA.
DR   IPI; IPI00407835; -.
DR   IPI; IPI00622375; -.
DR   IPI; IPI00761172; -.
DR   IPI; IPI00761299; -.
DR   IPI; IPI00761937; -.
DR   RefSeq; NP_001159455.1; NM_001165983.1.
DR   RefSeq; NP_001159456.1; NM_001165984.1.
DR   RefSeq; NP_001159457.1; NM_001165985.1.
DR   RefSeq; NP_001159458.1; NM_001165986.1.
DR   RefSeq; NP_082751.1; NM_028475.2.
DR   UniGene; Mm.25610; -.
DR   UniGene; Mm.441742; -.
DR   PDB; 1WJ7; NMR; -; A=19-109.
DR   PDBsum; 1WJ7; -.
DR   ProteinModelPortal; Q80X50; -.
DR   SMR; Q80X50; 19-111.
DR   PhosphoSite; Q80X50; -.
DR   PRIDE; Q80X50; -.
DR   Ensembl; ENSMUST00000029553; ENSMUSP00000029553; ENSMUSG00000042520.
DR   Ensembl; ENSMUST00000064639; ENSMUSP00000066138; ENSMUSG00000042520.
DR   Ensembl; ENSMUST00000080538; ENSMUSP00000079381; ENSMUSG00000042520.
DR   Ensembl; ENSMUST00000090908; ENSMUSP00000088424; ENSMUSG00000042520.
DR   GeneID; 74383; -.
DR   KEGG; mmu:74383; -.
DR   UCSC; uc008qal.1; mouse.
DR   UCSC; uc008qam.1; mouse.
DR   UCSC; uc008qao.1; mouse.
DR   UCSC; uc008qap.1; mouse.
DR   UCSC; uc008qas.1; mouse.
DR   CTD; 74383; -.
DR   MGI; MGI:1921633; Ubap2l.
DR   GeneTree; ENSGT00390000003453; -.
DR   HOVERGEN; HBG058387; -.
DR   InParanoid; Q80X50; -.
DR   OMA; LKNPNDS; -.
DR   OrthoDB; EOG4V9TQ4; -.
DR   PhylomeDB; Q80X50; -.
DR   NextBio; 340605; -.
DR   ArrayExpress; Q80X50; -.
DR   Bgee; Q80X50; -.
DR   CleanEx; MM_UBAP2L; -.
DR   Genevestigator; Q80X50; -.
DR   GermOnline; ENSMUSG00000042520; Mus musculus.
DR   InterPro; IPR022166; DUF3697_Uba2.
DR   InterPro; IPR009060; UBA-like.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   Pfam; PF12478; DUF3697; 1.
DR   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF46934; UBA_like; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Phosphoprotein;
KW   Polymorphism.
FT   CHAIN         1   1107       Ubiquitin-associated protein 2-like.
FT                                /FTId=PRO_0000240665.
FT   DOMAIN       49     89       UBA.
FT   COMPBIAS    124    190       Arg/Gly-rich.
FT   COMPBIAS    469    472       Poly-Pro.
FT   COMPBIAS    473    799       Ser/Thr-rich.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     380    380       Phosphoserine (By similarity).
FT   MOD_RES     436    436       Phosphoserine (By similarity).
FT   MOD_RES     439    439       Phosphothreonine (By similarity).
FT   MOD_RES     473    473       Phosphoserine (By similarity).
FT   MOD_RES     474    474       Phosphoserine (By similarity).
FT   MOD_RES     478    478       Phosphoserine (By similarity).
FT   MOD_RES     480    480       Phosphoserine (By similarity).
FT   MOD_RES     481    481       Phosphothreonine (By similarity).
FT   MOD_RES     482    482       Phosphoserine (By similarity).
FT   MOD_RES     487    487       Phosphoserine (By similarity).
FT   MOD_RES     490    490       Phosphoserine (By similarity).
FT   MOD_RES     491    491       Phosphoserine (By similarity).
FT   MOD_RES     495    495       Phosphoserine (By similarity).
FT   MOD_RES     496    496       Phosphoserine (By similarity).
FT   MOD_RES     497    497       Phosphoserine.
FT   MOD_RES     624    624       Phosphoserine (By similarity).
FT   MOD_RES     625    625       Phosphoserine.
FT   MOD_RES     627    627       Phosphoserine (By similarity).
FT   MOD_RES     628    628       Phosphoserine (By similarity).
FT   MOD_RES     629    629       Phosphoserine.
FT   MOD_RES     854    854       Phosphotyrosine (By similarity).
FT   MOD_RES     855    855       Phosphotyrosine (By similarity).
FT   MOD_RES     864    864       Phosphothreonine (By similarity).
FT   MOD_RES     867    867       Phosphothreonine (By similarity).
FT   MOD_RES     872    872       Phosphoserine (By similarity).
FT   MOD_RES     879    879       Phosphoserine (By similarity).
FT   VAR_SEQ     150    150       F -> CMHGALSKPAVV (in isoform 2).
FT                                /FTId=VSP_019418.
FT   VAR_SEQ     235    255       RLDFIGVEGSNYPRKFETAPG -> S (in isoform
FT                                3).
FT                                /FTId=VSP_019419.
FT   VAR_SEQ     255    255       G -> GMIHPG (in isoform 5).
FT                                /FTId=VSP_019420.
FT   VAR_SEQ     989   1107       VSVTSSNTGVPDISGSVYSKTQQSFEKQGFHSGTPAASFNL
FT                                PSALGSGGPINPATAAAYPPAPFMHILTPHQQPHSQILHHH
FT                                LQQDGQTGSGQRSQTSSIPQKPQTNKSAYNSYSWGAN ->
FT                                RKYPPPYKHFWTAES (in isoform 2).
FT                                /FTId=VSP_019421.
FT   VAR_SEQ    1077   1107       TGSGQRSQTSSIPQKPQTNKSAYNSYSWGAN -> DILTLV
FT                                DDQLGE (in isoform 3).
FT                                /FTId=VSP_019422.
FT   VAR_SEQ    1077   1107       TGSGQRSQTSSIPQKPQTNKSAYNSYSWGAN -> LPYLQM
FT                                ILCCQRQQEEQDILTLVDDQLGE (in isoform 4).
FT                                /FTId=VSP_019423.
FT   VARIANT     374    374       G -> S (in strain: FVB/N).
FT   CONFLICT    303    303       D -> G (in Ref. 1; BAC33295).
FT   CONFLICT   1010   1010       Missing (in Ref. 2; AAH23906).
FT   STRAND       28     32
FT   HELIX        33     44
FT   HELIX        48     60
FT   HELIX        65     75
FT   HELIX        79     87
FT   STRAND       90     92
FT   STRAND      105    110
SQ   SEQUENCE   1107 AA;  116799 MW;  F4A4FB502B619C51 CRC64;
     MMTSVGTNRA RGNWEQPQNQ NQTQHKQRPQ ATAEQIRLAQ MISDHNDADF EEKVKQLIDI
     TGKNQDECVI ALHDCNGDVN RAINVLLEGN PDTHSWEMVG KKKGVSGQKD GGQTESNEEG
     KENRDRDRDY SRRRGGPPRR GRGASRGREF RGQENGLDGT KSGGPSGRGT DRGRRGRGRG
     RGSSGRRGGR FSAQGMGTFN PADYAEPANT DDNYGNSSGN TWNNTGHFEP DDGTRLDFIG
     VEGSNYPRKF ETAPGAWRTA TEEWGTEDWN EDLSETKIFT ASNVSSVPLP AENVTITAGQ
     RIDLAVLLGK TPSSMENDSS NLDPSQAPSL AQPLVFSNSK QNAISQPASG STFSHHSMVS
     MLGKGFGDVG EAKGGSTTGS QFLEQFKTAQ ALAQLAAQHS QSGSTTTSSW DMGSTTQSPS
     LVQYDLKSAN DSTVHSPFTK RQAFTPSSTM MEVFLQEKPP AVATSTAAPP PPSSPLPSKS
     TSAPQMSPGS SDNQSSSPQP AQQKLKQQKK KTSLTSKIPA LAVEMPGSAD ISGLNLQFGA
     LQFGSEPVLS DYESTPTTSA SSSQAPSSLY TSTASESSST VSSNQSQESG YQSGPIQSTT
     YTSQNNAQGP LYEQRSTQTR RYPSSISSSP QKDLTQAKNG FSSVQATQLQ TTQSVEGATG
     SAVKSESPST SSIPSLNETV PAASLLTTAN QHSSSLSGLS HTEEIPNTTT TQHSSALSTQ
     QNTLSSSTSS GRTSTSTLLH TSVESEANLH SSSSTFSTTS STVSAPPPVV SVSSSLNSGS
     SLGLSLGSNS TVTASTRSSV ATTSGKAPPN LPPGVPPLLP NPYIMAPGLL HAYPPQVYGY
     DDLQMLQTRF PLDYYSIPFP TPTTPLTGRD GSLASNPYSG DLTKFGRGDA SSPAPATTLA
     QPQQNQTQTH HTTQQTFLNP ALPPGYSYTS LPYYTGVPGL PSTFQYGPAV FPVAPTSSKQ
     HGVNVSVNAS ATPFQQPSGY GSHGYNTGVS VTSSNTGVPD ISGSVYSKTQ QSFEKQGFHS
     GTPAASFNLP SALGSGGPIN PATAAAYPPA PFMHILTPHQ QPHSQILHHH LQQDGQTGSG
     QRSQTSSIPQ KPQTNKSAYN SYSWGAN
//
ID   Q80X68_MOUSE            Unreviewed;       466 AA.
AC   Q80X68;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Citrate synthase;
GN   Name=Csl; ORFNames=mCG_19869;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [11]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the citrate synthase family.
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DR   EMBL; BC050750; AAH50750.1; -; mRNA.
DR   EMBL; AK161295; BAE36302.1; -; mRNA.
DR   EMBL; CH466539; EDL21651.1; -; Genomic_DNA.
DR   IPI; IPI00118825; -.
DR   RefSeq; NP_082221.2; NM_027945.3.
DR   UniGene; Mm.280604; -.
DR   HSSP; P00889; 1CTS.
DR   ProteinModelPortal; Q80X68; -.
DR   SMR; Q80X68; 28-464.
DR   STRING; Q80X68; -.
DR   PRIDE; Q80X68; -.
DR   Ensembl; ENSMUST00000056085; ENSMUSP00000052373; ENSMUSG00000046934.
DR   GeneID; 71832; -.
DR   KEGG; mmu:71832; -.
DR   NMPDR; fig|10090.3.peg.22790; -.
DR   UCSC; uc007gxo.1; mouse.
DR   CTD; 71832; -.
DR   MGI; MGI:1919082; Csl.
DR   eggNOG; roNOG11355; -.
DR   HOGENOM; HBG309523; -.
DR   HOVERGEN; HBG005336; -.
DR   InParanoid; Q80X68; -.
DR   OMA; ALPKESH; -.
DR   OrthoDB; EOG4FBHSR; -.
DR   PhylomeDB; Q80X68; -.
DR   ArrayExpress; Q80X68; -.
DR   Bgee; Q80X68; -.
DR   Genevestigator; Q80X68; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0004108; F:citrate (Si)-synthase activity; IEA:InterPro.
DR   GO; GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR   InterPro; IPR002020; Citrate_synthase-like.
DR   InterPro; IPR016141; Citrate_synthase-like_core.
DR   InterPro; IPR019810; Citrate_synthase_AS.
DR   InterPro; IPR010109; Citrate_synthase_euk.
DR   Gene3D; G3DSA:1.10.580.10; Citrate_synthase_lrg_a-sub; 1.
DR   PANTHER; PTHR11739; Citrate_synth; 1.
DR   Pfam; PF00285; Citrate_synt; 1.
DR   PRINTS; PR00143; CITRTSNTHASE.
DR   SUPFAM; SSF48256; Citrate_synthase_core; 1.
DR   TIGRFAMs; TIGR01793; cit_synth_euk; 1.
DR   PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE   2: Evidence at transcript level;
KW   Transferase.
SQ   SEQUENCE   466 AA;  52325 MW;  023DFF788917491C CRC64;
     MALLTAAAWF LGTKNPPCLV LAARHASASS TNLKDVLRNL IPKEQARIKT FRKKHGKTVV
     GQITVDMMYG GMRGMKGLVY ETSVLDPDEG IRFRGYSIPE CQKLLPKAKG GKEPLPEGLF
     WLLVTGQMPT EEQVSWLSQE WVKRAALPSH VVTMLDNFPT KLHPMSQLSA AITVLNNESN
     FARAYAQGMN RTKYWELTYE DCMDLLAKLP CVAAKIYRNL YREDRNIEAI DSKLDWSHNF
     TNMLGYTDPQ FTELMRLYLT IHSDHEGGNV SAHTSHLVGS ALSDPYLSFA AALNGLAGPL
     HGLANQEVLV WLTQLQKEVG EDASDEKLKN YIWNTLNSGR VVPGYGHAVL RKTDPRYSCQ
     REFALKHLPK DPMFKLVGQL YKIVPDILLE QGKAKNPWPN VDAHSGVLLQ YYGMREMNYY
     TVLFGVSRAL GVLSQLIWSR ALGFPLERPK SMSTDALMKF VNSESG
//
ID   C2C2L_MOUSE             Reviewed;         706 AA.
AC   Q80X80;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 2.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=C2 domain-containing protein 2-like;
DE   AltName: Full=Transmembrane protein 24;
GN   Name=C2cd2l; Synonyms=Tmem24;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358; SER-464; SER-613;
RP   SER-619 AND SER-660, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein (By
CC       similarity).
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DR   EMBL; BC049875; AAH49875.1; -; mRNA.
DR   EMBL; BC060156; AAH60156.1; -; mRNA.
DR   IPI; IPI00119785; -.
DR   UniGene; Mm.33869; -.
DR   ProteinModelPortal; Q80X80; -.
DR   SMR; Q80X80; 285-389.
DR   STRING; Q80X80; -.
DR   PhosphoSite; Q80X80; -.
DR   PRIDE; Q80X80; -.
DR   Ensembl; ENSMUST00000065080; ENSMUSP00000065233; ENSMUSG00000032120.
DR   MGI; MGI:1919014; C2cd2l.
DR   HOGENOM; HBG715883; -.
DR   HOVERGEN; HBG058857; -.
DR   InParanoid; Q80X80; -.
DR   OrthoDB; EOG4BZN2B; -.
DR   ArrayExpress; Q80X80; -.
DR   Bgee; Q80X80; -.
DR   Genevestigator; Q80X80; -.
DR   GermOnline; ENSMUSG00000032120; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    706       C2 domain-containing protein 2-like.
FT                                /FTId=PRO_0000072597.
FT   TRANSMEM     10     30       Helical; (Potential).
FT   MOD_RES     358    358       Phosphoserine.
FT   MOD_RES     417    417       Phosphothreonine (By similarity).
FT   MOD_RES     420    420       Phosphoserine (By similarity).
FT   MOD_RES     430    430       Phosphothreonine (By similarity).
FT   MOD_RES     464    464       Phosphoserine.
FT   MOD_RES     468    468       Phosphoserine (By similarity).
FT   MOD_RES     613    613       Phosphoserine.
FT   MOD_RES     619    619       Phosphoserine.
FT   MOD_RES     623    623       Phosphoserine (By similarity).
FT   MOD_RES     660    660       Phosphoserine.
FT   MOD_RES     691    691       Phosphoserine (By similarity).
FT   MOD_RES     703    703       Phosphoserine (By similarity).
FT   CONFLICT    550    550       V -> A (in Ref. 1; AAH49875).
SQ   SEQUENCE   706 AA;  76357 MW;  2F8B63D26FF1F791 CRC64;
     MDPDWGQRDV GWAALLVLFA ASLITVLGWM LQYARGLWLS RADGGRDSRP ASAAEPGGSL
     RELGVWRSLL RLRATRTSTP EEAGVRGLLA SLFAFKSFRE NWQRAWVRAL NEQACRDGSS
     IQIAFEEIPQ LPPRASISHV TCVDQSERTM VLHCQLSAEE VRFPISVTQQ SPAAVSMETY
     HVTLTLPPTQ LEVSLEEIPD EGLLVSWAFT DRPELSLKVL PKLQTRERDE EQPELSTVEE
     LIKDAIVSTQ PAMMVNLRAC SAPGGLVPSE KPPTMSQAQP SIPRPTRLFL RQLRASHLGS
     ELGGTEELCC AAELDNPMQQ KWTKPMRAGP EVEWTEDLAL DLGPQSRELT LKVLRSSSCG
     DAELLGQATL PVGSPSRPMS RRQVCPLTPG PGKSLSPAAT VTAELHYEQG SPRNLGTPTS
     STPRPSITPT KKIELDRTIM PDGTVVTTVT TVQSRPRVDG KLDSPSRSPS KVEVTEKMTT
     VLSESSGPSN ASHSSSRESH LSNGLDPVAE TAIRQLTEPS GRAAKKTPTK RSTLIISGVS
     KVPIAQDELV LSLGYAASLE ASMQDDAGTS GGPSSPPSDP SATSPGPVDA LSSPTSVQEA
     DETTRSDISE RPSVDDVESE TGSTGALETR SLKDHKVSFL RSGTKLIFRR RPRQKEAGLS
     QSHDDLSNTT ATPSVRKKAG SFSRRLIKRF SFKSKPKANG NPSPQL
//
ID   FLNB_MOUSE              Reviewed;        2602 AA.
AC   Q80X90; Q8VHX4; Q8VHX7; Q99KY3;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   07-NOV-2003, sequence version 2.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Filamin-B;
DE            Short=FLN-B;
DE   AltName: Full=ABP-280-like protein;
DE   AltName: Full=Actin-binding-like protein;
DE   AltName: Full=Beta-filamin;
GN   Name=Flnb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   RECONSTRUCTION FROM ESTS AND GENOMIC SEQUENCE, AND CONCEPTUAL
RP   TRANSLATION.
RA   Stutz A.;
RL   Unpublished observations (MAY-2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1663-1752 AND 2031-2181.
RC   STRAIN=C3H;
RX   MEDLINE=21666190; PubMed=11807098; DOI=10.1083/jcb.200103037;
RA   van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M.,
RA   Takafuta T., Shapiro S.S., Sonnenberg A.;
RT   "Different splice variants of filamin-B affect myogenesis, subcellular
RT   distribution, and determine binding to integrin (beta) subunits.";
RL   J. Cell Biol. 156:361-376(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1884-2602.
RC   STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   MEDLINE=22281257; PubMed=12393796; DOI=10.1093/hmg/11.23.2845;
RA   Sheen V.L., Feng Y., Graham D., Takafuta T., Shapiro S.S., Walsh C.A.;
RT   "Filamin A and filamin B are co-expressed within neurons during
RT   periods of neuronal migration and can physically interact.";
RL   Hum. Mol. Genet. 11:2845-2854(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1557, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Connects cell membrane constituents to the actin
CC       cytoskeleton. May promote orthogonal branching of actin filaments
CC       and links actin filaments to membrane glycoproteins. Anchors
CC       various transmembrane proteins to the actin cytoskeleton (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer. Interacts with FLNA, FLNC, INPPL1, ITGB1A,
CC       ITGB1D, ITGB3, ITGB6, MYOT, MYOZ1, PSEN1 and PSEN2 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Cytoplasm,
CC       myofibril, sarcomere, Z-disk (By similarity). Cytoplasm,
CC       cytoskeleton. Note=May localize also at actin stress fibers and
CC       within the Z-lines (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in hippocampus, cortex, cerebellar
CC       Purkinje cells and granule cell layers.
CC   -!- DEVELOPMENTAL STAGE: Expressed within the ventricular,
CC       periventricular and subventricular zones at 12.5 dpc; olfactory
CC       epithelium, radial glial fibers, cortical plate and lateral
CC       ventricles at 16 dpc; in a lesser degree in lung, renal cortices
CC       and alimentary tract.
CC   -!- DOMAIN: Comprised of a NH2-terminal actin-binding domain, 24
CC       internally homologous repeats and two hinge regions. Repeat 24 and
CC       the second hinge domain are important for dimer formation. The
CC       first hinge region prevents binding to ITGA and ITGB subunits (By
CC       similarity).
CC   -!- PTM: ISGylation prevents ability to interact with the upstream
CC       activators of the JNK cascade and inhibits IFNA-induced JNK
CC       signaling (By similarity).
CC   -!- SIMILARITY: Belongs to the filamin family.
CC   -!- SIMILARITY: Contains 1 actin-binding domain.
CC   -!- SIMILARITY: Contains 2 CH (calponin-homology) domains.
CC   -!- SIMILARITY: Contains 24 filamin repeats.
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DR   EMBL; AF353669; AAL68445.1; -; mRNA.
DR   EMBL; AF353672; AAL68448.1; -; mRNA.
DR   EMBL; BC003959; AAH03959.1; -; mRNA.
DR   EMBL; BC048835; AAH48835.1; -; mRNA.
DR   IPI; IPI00663627; -.
DR   UniGene; Mm.28095; -.
DR   ProteinModelPortal; Q80X90; -.
DR   SMR; Q80X90; 12-240, 252-2602.
DR   STRING; Q80X90; -.
DR   PhosphoSite; Q80X90; -.
DR   PRIDE; Q80X90; -.
DR   Ensembl; ENSMUST00000052678; ENSMUSP00000052020; ENSMUSG00000025278.
DR   UCSC; uc007sek.1; mouse.
DR   MGI; MGI:2446089; Flnb.
DR   GeneTree; ENSGT00590000082997; -.
DR   HOGENOM; HBG357078; -.
DR   HOVERGEN; HBG004163; -.
DR   InParanoid; Q80X90; -.
DR   OrthoDB; EOG4V436R; -.
DR   ArrayExpress; Q80X90; -.
DR   Bgee; Q80X90; -.
DR   CleanEx; MM_FLNB; -.
DR   Genevestigator; Q80X90; -.
DR   GermOnline; ENSMUSG00000025278; Mus musculus.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR   GO; GO:0001725; C:stress fiber; IDA:MGI.
DR   GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IDA:MGI.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR001298; Filamin.
DR   InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 2.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 24.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF00630; Filamin; 23.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00557; IG_FLMN; 24.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   SUPFAM; SSF81296; Ig_E-set; 24.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS50194; FILAMIN_REPEAT; 24.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Cytoplasm; Cytoskeleton; Isopeptide bond;
KW   Phosphoprotein; Repeat; Ubl conjugation.
FT   CHAIN         1   2602       Filamin-B.
FT                                /FTId=PRO_0000087299.
FT   DOMAIN        1    239       Actin-binding.
FT   DOMAIN       16    122       CH 1.
FT   DOMAIN      139    239       CH 2.
FT   REPEAT      249    347       Filamin 1.
FT   REPEAT      349    446       Filamin 2.
FT   REPEAT      447    543       Filamin 3.
FT   REPEAT      544    636       Filamin 4.
FT   REPEAT      640    736       Filamin 5.
FT   REPEAT      737    839       Filamin 6.
FT   REPEAT      840    938       Filamin 7.
FT   REPEAT      939   1034       Filamin 8.
FT   REPEAT     1035   1127       Filamin 9.
FT   REPEAT     1128   1222       Filamin 10.
FT   REPEAT     1223   1322       Filamin 11.
FT   REPEAT     1323   1415       Filamin 12.
FT   REPEAT     1416   1511       Filamin 13.
FT   REPEAT     1512   1608       Filamin 14.
FT   REPEAT     1609   1704       Filamin 15.
FT   REPEAT     1729   1813       Filamin 16.
FT   REPEAT     1816   1908       Filamin 17.
FT   REPEAT     1919   1994       Filamin 18.
FT   REPEAT     1997   2089       Filamin 19.
FT   REPEAT     2091   2185       Filamin 20.
FT   REPEAT     2188   2280       Filamin 21.
FT   REPEAT     2282   2375       Filamin 22.
FT   REPEAT     2379   2471       Filamin 23.
FT   REPEAT     2507   2601       Filamin 24.
FT   REGION     1705   1728       Hinge 1 (By similarity).
FT   REGION     2472   2602       Self-association site, tail (By
FT                                similarity).
FT   REGION     2472   2506       Hinge 2 (By similarity).
FT   MOD_RES     519    519       Phosphothreonine (By similarity).
FT   MOD_RES     658    658       Phosphoserine (By similarity).
FT   MOD_RES     681    681       N6-acetyllysine (By similarity).
FT   MOD_RES     886    886       Phosphoserine (By similarity).
FT   MOD_RES     983    983       Phosphoserine (By similarity).
FT   MOD_RES    1028   1028       Phosphoserine (By similarity).
FT   MOD_RES    1316   1316       Phosphoserine (By similarity).
FT   MOD_RES    1433   1433       Phosphoserine (By similarity).
FT   MOD_RES    1505   1505       Phosphoserine (By similarity).
FT   MOD_RES    1530   1530       Phosphotyrosine (By similarity).
FT   MOD_RES    1557   1557       Phosphothreonine.
FT   MOD_RES    1602   1602       Phosphoserine (By similarity).
FT   MOD_RES    1684   1684       Phosphotyrosine (By similarity).
FT   MOD_RES    2083   2083       Phosphoserine (By similarity).
FT   MOD_RES    2170   2170       N6-acetyllysine (By similarity).
FT   MOD_RES    2369   2369       Phosphoserine (By similarity).
FT   MOD_RES    2478   2478       Phosphoserine (By similarity).
FT   MOD_RES    2481   2481       Phosphoserine (By similarity).
FT   MOD_RES    2502   2502       Phosphotyrosine (By similarity).
FT   MOD_RES    2576   2576       N6-acetyllysine (By similarity).
FT   CROSSLNK   2468   2468       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ISG15) (By
FT                                similarity).
SQ   SEQUENCE   2602 AA;  277753 MW;  480B607489CB71B8 CRC64;
     MPVTEKDLAE DAPWKKIQQN TFTRWCNEHL KCVNKRIGNL QTDLSDGLRL IALLEVLSQK
     RMHHKYHQRP TFRQMKLENV SVALEFLDHE SIKLVSIDSK AIVDGNLKLI LGLVWTLILH
     YSISMPVWED EGDDDAKKQT PKQRLLGWIQ NKIPYLPITN FNQNWQDGKA LGALVDSCAP
     GLCPDWESWD PRKPVDNARE AMQQADDWLG VPQVITPEEI IHPDVDEHSV MTYLSQFPKA
     KLKPGAPLKP KLNPKKARAY GRGIEPTGNM VKQPAKFTVD TISAGQGDVM VFVEDPEGNK
     EEARVTPDSD KNKTYSVEYL PKVTGLHKVI VLFAGQHISK SPFEVNVDKA QGDASKVTAK
     GPGLETTGNI ANKPTYFDIY TAGAGVGDIG IEVEDPQGKN SVELLVEDRG NQVYRCVYKP
     VQPGPHVVKV SFAGDAIPKS PFGVQIGEAC NPNACRASGR GLQPKGVRIR ETADFKVDTK
     AAGSGELGVT VKGPGGLEEL VKQKGFLDGV YSFEYYPSTP GKYSVAVTWG GHHIPKSPFE
     VQVGPEAGMQ KVRAWGPGLH GGIVGRSADF VVESIGSEVG TLGFAIEGPS QAKIEYDDQN
     DGSCDVKYWP KEPGEYAVHI MCDDEDIKDS PYMAFIHPAT GDYNPDLVQA YGPGLEKSGC
     TINNPAEFIV DPKDAGSAPL KILAQDGEGQ PIDIQMKSRM DGTYACSYTP LKAIKHTIAV
     VWGGVNIPHS PYRVNIGQGS HPQKVKVFGP GVERSGLKAN EPTHFTVDCT EAGEGDVSVG
     IKCDARVLSD DEEDVDFDII HNANDTFTVK YVPPAPGRYT IKVLFASQEI PASPFRVKVD
     PSHDASKVKA EGPGLSKAGV ENGKPTHFTV HTKGAGKAPL IVQFSSPLPG EAVKDLDIID
     NYDYSHTVKY TPTQQGNMQV LVTYGGDPIP KSPFTVGVAA PLDLSKIKIN GLENRVEVGK
     DQEFAIDTNG AGGQGKLDVT ILSPSRKVVP CLVAPVAGRE CSTAKFIPRE EGLFAVDVTY
     DGHPVPGSPY TVEASLPPDP TKVKAHGPGL EGGLVGKPAE FTIDTKGAGT GGLGLTVEGP
     CEAKIECSDN GDGTCSVSYL PTKPGEYFVN ILFEEVHIPG SPFKADIEMP FDPSKVVASG
     PGLEHGKVGE PGILCVDCSE AGPGTLGLEA VSDSGAKAEV SIQNNKDGTY AVTYVPLTAG
     MYTLTMKYGG ELVPHFPAWV KVEPAIDTSG IKAFGPGIEG KDVFREATTD FTVDSRPLTQ
     VGGDHIKAQI TNPSGASTEC FVKDNADGTY QVEYTPFEKG FHVVEVTYDD VPIPNSPFKV
     AVTEGCQPSR VHAQGPGLKE AFTNKSNVFT VVTRGAGIGG LGITVEGPSE SKINCRDNKD
     GSCSAEYIPF APGDYDVNIT YGGVHIPGSP FRVPSKDVVD PSKVKIAGPG LSSCVRACIP
     QSFTVDSSKA GLAPLEVRVL GPRGLVEPVN VVDNGDGTHT VTYTPSQEGP YIVSVKYADE
     EIPRSPFKVK VLPTYDASKV TASGPGLSAY GVPASLPVEF AIDARDAGEG LLAVQITDQE
     GKPQRATVHD NKDGTYAVTY IPDKTGRYMI GVTYGGDNIP LSPYRIRATQ TGDASKCLAT
     GPGIAPTVKT GEEVGFVVDA KTAGKGKVTC VILTPDGTEA EADVIENEDG TYDIFYTAAK
     PGTYVIYVRF GGVDIPNSPF TVMATDGEVT AMEEAPVNAC PPGFRPWVTE EAYVPVSDMN
     GLGFKPFDLV IPFAVRKGEI TGTVHMPSGK KATPEIVDNK DGTVTVRYAP TEVGLHEMHI
     KYRGSHIPES PLQFYVNYPN SGSVSAYGPG LVYGVANKTA TFTIVTEDAG EGGLDLAIEG
     PSKAEISCID NKDGTCTVTY LPTLPGDYSI LVKYNDKHIP GSPFTAKITD DNRRCSQVKL
     GSAADFLLDI SETDLSTLTA SIKAPSGRDE PCLLKRLPNN HIGISFIPRE VGEHLVSIKK
     NGNHVANSPV SIMVVQSEIG DARRAKVYGQ GLSEGRTFEM SDFIVDTRDA GYGGISLAVE
     GPSKVDIQTE DLEDGTCKVS YFPTVPGVYI VSTKFADEHV PGSPFTVKIS GEGRVRESIT
     RTSRAPAVAT VGSICDLNLK IPEINSSDMS AHVTSPSGHV TEAEIVPMGK NSHCVRFVPQ
     EMGVHTVSVK YRGQHVTGSP FQFTVGPLGE GGAHKVRAGG PGLERGEAGI PAEFSIWTRE
     AGAGGLSIAV EGPSKAEITF DDHKNGSCGV SYIAQEPGNY EVSIKFNDEH IPDSPYLVPV
     IAPSDDARCL TVLSLQESGL KVNQPASFAI RLNGAKGKID AKVHSPSGAV EECHVSELEP
     DKYAVRFIPH ENGIHTIDVK FNGSHVVGSP FKVRVGEPGQ AGNPALVSAY GAGLETGTTG
     IQSEFFINTT QAGPGTLSVT IEGPSKVKMD CQEIPEGYKV MYTPMAPGNY LIGVKYGGPN
     HISRSPFKAK VTGQRLVSPG SANETSSILV ESVTRSSTET CYSAIPKSSS DASKVTSKGA
     GLSKAFVGQK SSFLVDCSKA GSNMLLIGVH GPTTPCEEVS MKHVGKQQYN VTYVVKERGD
     YVLAVKWGEE HIPGSPFHVT VP
//
ID   US6NL_MOUSE             Reviewed;         819 AA.
AC   Q80XC3; A2AR45; A2AR46; Q3U2W3; Q6ZQK8;
DT   30-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   30-JUL-2004, sequence version 2.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=USP6 N-terminal-like protein;
GN   Name=Usp6nl; Synonyms=Kiaa0019;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=NOD; TISSUE=Dendritic cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-662, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Acts as a GTPase-activating protein for RAB5A. Involved
CC       in receptor trafficking. In complex with EPS8 inhibits
CC       internalization of EGFR (By similarity).
CC   -!- SUBUNIT: Interacts with EPS8 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80XC3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80XC3-2; Sequence=VSP_011153;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 Rab-GAP TBC domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97847.1; Type=Erroneous initiation;
CC       Sequence=BC051184; Type=Frameshift; Positions=671;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK129037; BAC97847.1; ALT_INIT; mRNA.
DR   EMBL; AK155073; BAE33027.1; -; mRNA.
DR   EMBL; AL845275; CAM13701.1; -; Genomic_DNA.
DR   EMBL; AL845515; CAM13701.1; JOINED; Genomic_DNA.
DR   EMBL; AL845275; CAM13702.1; -; Genomic_DNA.
DR   EMBL; AL845515; CAM13702.1; JOINED; Genomic_DNA.
DR   EMBL; AL845515; CAM18814.1; -; Genomic_DNA.
DR   EMBL; AL845275; CAM18814.1; JOINED; Genomic_DNA.
DR   EMBL; AL845515; CAM18815.1; -; Genomic_DNA.
DR   EMBL; AL845275; CAM18815.1; JOINED; Genomic_DNA.
DR   EMBL; BC051184; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00461338; -.
DR   IPI; IPI00461339; -.
DR   RefSeq; NP_001074017.1; NM_001080548.1.
DR   RefSeq; NP_852064.2; NM_181399.3.
DR   UniGene; Mm.40673; -.
DR   ProteinModelPortal; Q80XC3; -.
DR   SMR; Q80XC3; 72-342.
DR   STRING; Q80XC3; -.
DR   PhosphoSite; Q80XC3; -.
DR   PRIDE; Q80XC3; -.
DR   Ensembl; ENSMUST00000042503; ENSMUSP00000043178; ENSMUSG00000039046.
DR   Ensembl; ENSMUST00000091473; ENSMUSP00000089055; ENSMUSG00000039046.
DR   Ensembl; ENSMUST00000114937; ENSMUSP00000110587; ENSMUSG00000039046.
DR   GeneID; 98910; -.
DR   KEGG; mmu:98910; -.
DR   UCSC; uc008igk.1; mouse.
DR   UCSC; uc008igl.1; mouse.
DR   CTD; 98910; -.
DR   MGI; MGI:2138893; Usp6nl.
DR   eggNOG; roNOG10945; -.
DR   GeneTree; ENSGT00550000074322; -.
DR   HOVERGEN; HBG059159; -.
DR   OMA; HGNSPKH; -.
DR   OrthoDB; EOG4NKBVT; -.
DR   PhylomeDB; Q80XC3; -.
DR   NextBio; 353705; -.
DR   ArrayExpress; Q80XC3; -.
DR   Bgee; Q80XC3; -.
DR   CleanEx; MM_USP6NL; -.
DR   Genevestigator; Q80XC3; -.
DR   GermOnline; ENSMUSG00000039046; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005097; F:Rab GTPase activator activity; IEA:InterPro.
DR   GO; GO:0032313; P:regulation of Rab GTPase activity; IEA:InterPro.
DR   InterPro; IPR000195; RabGAP/TBC_dom.
DR   Pfam; PF00566; TBC; 1.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; RabGAP_TBC; 2.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; GTPase activation; Phosphoprotein.
FT   CHAIN         1    819       USP6 N-terminal-like protein.
FT                                /FTId=PRO_0000208057.
FT   DOMAIN      100    292       Rab-GAP TBC.
FT   COMPBIAS    567    659       Pro-rich.
FT   MOD_RES     389    389       Phosphoserine (By similarity).
FT   MOD_RES     394    394       Phosphoserine (By similarity).
FT   MOD_RES     544    544       Phosphoserine.
FT   MOD_RES     574    574       Phosphoserine (By similarity).
FT   MOD_RES     662    662       Phosphoserine.
FT   MOD_RES     669    669       Phosphoserine (By similarity).
FT   MOD_RES     699    699       Phosphotyrosine (By similarity).
FT   MOD_RES     704    704       Phosphoserine (By similarity).
FT   MOD_RES     717    717       Phosphotyrosine (By similarity).
FT   VAR_SEQ       1      2       MN -> MIQVLQLVKELVTPSRQKAATAKED (in
FT                                isoform 2).
FT                                /FTId=VSP_011153.
FT   CONFLICT    446    446       E -> G (in Ref. 2; BAE33027).
FT   CONFLICT    765    765       A -> V (in Ref. 2; BAE33027).
SQ   SEQUENCE   819 AA;  93574 MW;  AD6B72BB42A00B54 CRC64;
     MNSDQDVALK LAQERAEIVA KYDRGREGAE IEPWEDADYL VYKVTDRFGF LHEEELPYHN
     AAADRQKQLE IERTSKWLKM LKKWERYKNT EKFHRRIYKG IPLQLRGEVW ALLLEIPKMK
     EETRDLYSKL KHRARGCSPD IRQIDLDVNR TFRDHIMFRD RYGVKQQSLF HVLAAYSIYN
     TEVGYCQGMS QITALLLMYM NEEDAFWALV KLFSGPKHAM HGFFVQGFPK LLRFQEHHEK
     ILNKFLSKLK QHLDSQEIYT SFYTMKWFFQ CFLDRTPFRL NLRIWDIYIF EGERVLTAMS
     YTILKLHKKH LMKLSMEELV EFLQETLAKD FFFEDDFVIE QLQVSMAELK RAKLDLPEPG
     KEDEYPKKPL GQLPPESACV NHLSNGQRSV GRPSPKTSSR REDGSPRKNH EHSPVHHSRN
     GTPERAGQSR RKSVDEGSKN LKHEAESQRK PSPGMQDSSR HYNHAAANQN SNAISNVRKE
     FMPKWRKPSD ASAIERTTKY AVEGKSHSAL PALPVAIPGS AETRLPNSRQ KMKALDGGEG
     KRGSNASQYD NVPGGESEHG ASAEEGPERT HPHSPRKHPE PSPSPPKVPN KFTFKVQPPS
     HVRYPPQLPE EDHRAAYPPS YSNPPVYHGN SPKHVPTAHS GFVSTQISPR PQINPSRRPY
     GSSLSVDTSP EKAYSRPTPV VLPSSRIEVL PIDMGARGYG SSGSPKNGQF ILPPVDYLPE
     NRKWSEVSYT YRPEMHGQSW TRDAHRSHLS NLPNYAAFQH IPFQAHGLPE VSVDSPVRYK
     MSAAVEDASP PGYPYAGPSP SAHHYRNGEG LSVQESVLL
//
ID   Q80XD3_MOUSE            Unreviewed;       470 AA.
AC   Q80XD3;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   SubName: Full=Rgs7 protein;
GN   Name=Rgs7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 RGS domain.
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DR   EMBL; BC051133; AAH51133.1; -; mRNA.
DR   IPI; IPI00118769; -.
DR   RefSeq; NP_001185932.1; NM_001199003.1.
DR   RefSeq; NP_036010.2; NM_011880.3.
DR   UniGene; Mm.7956; -.
DR   HSSP; O46469; 1FQI.
DR   ProteinModelPortal; Q80XD3; -.
DR   SMR; Q80XD3; 26-113, 254-307, 320-450.
DR   STRING; Q80XD3; -.
DR   PRIDE; Q80XD3; -.
DR   Ensembl; ENSMUST00000085853; ENSMUSP00000083014; ENSMUSG00000026527.
DR   GeneID; 24012; -.
DR   KEGG; mmu:24012; -.
DR   UCSC; uc007dtl.1; mouse.
DR   CTD; 24012; -.
DR   MGI; MGI:1346089; Rgs7.
DR   GeneTree; ENSGT00560000076525; -.
DR   HOGENOM; HBG385421; -.
DR   HOVERGEN; HBG007404; -.
DR   InParanoid; Q80XD3; -.
DR   OMA; TSLVQSY; -.
DR   PhylomeDB; Q80XD3; -.
DR   ArrayExpress; Q80XD3; -.
DR   Bgee; Q80XD3; -.
DR   Genevestigator; Q80XD3; -.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005096; F:GTPase activator activity; TAS:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; IDA:MGI.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR015898; G-protein_gamma_dom.
DR   InterPro; IPR000342; Regulat_G_prot_signal.
DR   InterPro; IPR016137; Regulat_G_prot_signal_superfam.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:4.10.260.10; G-protein_gamma_dom; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF00631; G-gamma; 1.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00049; DEP; 1.
DR   SMART; SM00224; GGL; 1.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48670; G-protein_gamma-like; 1.
DR   SUPFAM; SSF48097; Regulat_G_prot_signal_superfam; 1.
DR   PROSITE; PS50186; DEP; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   470 AA;  55014 MW;  1C488730592A7307 CRC64;
     MAQGNNYGQT SNGVADESPN MLVYRKMEDV IARMQDEKNG IPIRTVKSFL SKIPSVFSGS
     DIVQWLIKNL TIEDPVEALH LGTLMAAHGY FFPISDHVLT LKDDGTFYRF QTPYFWPSNC
     WEPENTDYAV YLCKRTMQNK ARLELADYEA ESLARLQRAF ARKWEFIFMQ AEAQAKVDKK
     RDKIERKILD SQERAFWDVH RPVPGCVNTT EVDIKKSSRM RNPHKTRKSV YGLQNDIRSH
     SPTHTPTPET KPPTEDELHQ QIKYWQIQLD RHRLKMSKVA DSLLSYTEQY VEYDPFLVPP
     DPSNPWLSDD TTFWELEASK EPSQQRVKRW GFGMDEALKD PVGREQFLKF LESEFSSENL
     RFWLAVEDLK RRPIREVPSR VQEIWQEFLA PGAPSAINLD SKSYDKTTQN VKEPGRYTFE
     DAQEHIYKLM KSDSYPRFIR SSAYQELLQA KRKRCHERLL HAVLSPRAFV
//
ID   Q80XD5_MOUSE            Unreviewed;      1301 AA.
AC   Q80XD5;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 44.
DE   SubName: Full=Fryl protein;
GN   Name=Fryl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
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CC   -----------------------------------------------------------------------
DR   EMBL; BC051118; AAH51118.1; -; mRNA.
DR   IPI; IPI00229629; -.
DR   RefSeq; NP_082470.2; NM_028194.2.
DR   UniGene; Mm.480322; -.
DR   ProteinModelPortal; Q80XD5; -.
DR   STRING; Q80XD5; -.
DR   PRIDE; Q80XD5; -.
DR   Ensembl; ENSMUST00000094700; ENSMUSP00000092289; ENSMUSG00000070733.
DR   Ensembl; ENSMUST00000101127; ENSMUSP00000098687; ENSMUSG00000070733.
DR   GeneID; 72313; -.
DR   KEGG; mmu:72313; -.
DR   UCSC; uc008xsm.1; mouse.
DR   CTD; 72313; -.
DR   MGI; MGI:1919563; Fryl.
DR   HOVERGEN; HBG067116; -.
DR   InParanoid; Q80XD5; -.
DR   ArrayExpress; Q80XD5; -.
DR   Bgee; Q80XD5; -.
DR   Genevestigator; Q80XD5; -.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR016024; ARM-type_fold.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
PE   1: Evidence at protein level;
SQ   SEQUENCE   1301 AA;  144384 MW;  20EB2248756A33A4 CRC64;
     MTDSGLSSSS TSSSISLGNN SAAISHLHTT LLGEVDLSVE QDGKVKTLME FITSRKRGPL
     WNHEDVSSKN PSIKSADQLA TFLKHVVSVF KQSNAEGIHL ERHLSEVALQ TALSCSSRHY
     AGRSFQIFRA LKQPLSADTL SDVLSRLVET VGDPGEDAQG FVIELLLTLE SAIDTLAETM
     KHYDLLSALS QSSYHDPVMG NKYAANRKST GQLNLSTSPI NSSGHLGCNG DTRSNSLRLS
     LVGDRRGDRR RSNTLDITDG RINHGGSLAR TRSLSSLREK GVYDTQPPTE PSNLMATIFW
     IATSLLESDY EYEYLLALRL LSKLLTHLPL DKSESREKIE NVQSKLKWSN FPGLQQLFLK
     GFTSVSTQEM TVHLLSQLIS VSKHTLVDPS QVSGFPLNIL CLLPHLIQHF DSPTQFCKET
     ASRIAKVCAE EKCPTLVNLA HMMSLYSTHT YSRDCSNWIN VVCRYLHDSF SEATFSLVTY
     LAELLEKGLS SMQQSLLQII YSLLSHIDLS AAPVKQFNLE IIKIIGKYVQ SPYWKEALNI
     LKLVVSRSAS LVVPNDIPKA YGVDVGSPEI SFAKIFNNVS KELPGKTLDF HFDISETPII
     GNKYGGQHSA AGRNGKAKVI AVTRSTSSTS SGSTSNALVP VSWKRPQLSQ RRTREKLMSV
     LSLCGPESGL PKNPSVVFSS NEDLEVGDQQ TSLISTTEDI IQEEEVAVED NSSEQQFGVF
     KDFDFLDVEL EDAEGESMDN FNWGVRRRSL DSIDKGDTPS LQEYPCSSST PSLTLTNQED
     TDESSEEEAA LTASQILSRT QMLNSDCVTE DMMPEHQDLL QSQDSASSNT TEDVLQIRDE
     TPSLEACLDN ASSQLPEGTS SVLKEEHVTA FEDEGSYVIP DQQDPLVCRG ILDLEETDMP
     EPLAPESYPE SICEEDVTLA LKELDERCEE EEADFSGLSS QEEDEQDGFP EVQTSPLPTP
     FLSAIIAAFQ PMAYEDEEEA WRCHVNQTLS DTDGSCAVFT FHVFSRLFQT IQRKFGEITK
     EAVGFLGESL QRIGTKFKSS LEVMMACSEC PTVFVDAETL MACGLLETLK FGVLELQEHL
     DTYTTKREAA EQWLDNCKRT FGANEDIYRM NTNAHELELC RRLYRLHFQL LLLFQAYCKL
     INQVNTIKNE AEVINMSEEL AQLEGILKEA EAASENEEID ISKAAQTTIE TAIHSLIETL
     KNKEFVSAVA QVKAFRTLWP NDIFGSCDDD PVQTLLHIYF HHQTLGQTGS FAVISSNLDM
     SEANCKLMEL NLEIRESLRT VQSYPLLAQT KPVGNMTSTG F
//
ID   LRRT4_MOUSE             Reviewed;         590 AA.
AC   Q80XG9; Q8C030; Q8JZS8;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Leucine-rich repeat transmembrane neuronal protein 4;
DE   Flags: Precursor;
GN   Name=Lrrtm4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6;
RX   MEDLINE=22563398; PubMed=12676565; DOI=10.1016/S0888-7543(03)00030-2;
RA   Lauren J., Airaksinen M.S., Saarma M., Timmusk T.T.;
RT   "A novel gene family encoding leucine-rich repeat transmembrane
RT   proteins differentially expressed in the nervous system.";
RL   Genomics 81:411-421(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-590 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: May play a role in the development and maintenance of
CC       the vertebrate nervous system (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80XG9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80XG9-2; Sequence=VSP_014193, VSP_014194;
CC   -!- TISSUE SPECIFICITY: Expressed in neuronal tissues.
CC   -!- SIMILARITY: Belongs to the LRRTM family.
CC   -!- SIMILARITY: Contains 10 LRR (leucine-rich) repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC27887.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AY182031; AAO67552.1; -; mRNA.
DR   EMBL; BC037216; AAH37216.1; -; mRNA.
DR   EMBL; AK032470; BAC27887.1; ALT_INIT; mRNA.
DR   IPI; IPI00170371; -.
DR   IPI; IPI00269563; -.
DR   RefSeq; NP_848846.3; NM_178731.5.
DR   UniGene; Mm.473274; -.
DR   UniGene; Mm.94135; -.
DR   ProteinModelPortal; Q80XG9; -.
DR   SMR; Q80XG9; 33-360.
DR   STRING; Q80XG9; -.
DR   PRIDE; Q80XG9; -.
DR   Ensembl; ENSMUST00000074662; ENSMUSP00000074232; ENSMUSG00000052581.
DR   GeneID; 243499; -.
DR   KEGG; mmu:243499; -.
DR   UCSC; uc009ckf.1; mouse.
DR   CTD; 243499; -.
DR   MGI; MGI:2389180; Lrrtm4.
DR   eggNOG; roNOG12902; -.
DR   GeneTree; ENSGT00600000084202; -.
DR   HOGENOM; HBG443538; -.
DR   HOVERGEN; HBG052362; -.
DR   InParanoid; Q80XG9; -.
DR   ArrayExpress; Q80XG9; -.
DR   Bgee; Q80XG9; -.
DR   CleanEx; MM_LRRTM4; -.
DR   Genevestigator; Q80XG9; -.
DR   GermOnline; ENSMUSG00000052581; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR000372; LRR-contain_N.
DR   Pfam; PF00560; LRR_1; 3.
DR   SMART; SM00369; LRR_TYP; 2.
DR   SMART; SM00013; LRRNT; 1.
DR   PROSITE; PS51450; LRR; 9.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Leucine-rich repeat; Membrane;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     30       Potential.
FT   CHAIN        31    590       Leucine-rich repeat transmembrane
FT                                neuronal protein 4.
FT                                /FTId=PRO_0000018359.
FT   TOPO_DOM     31    424       Extracellular (Potential).
FT   TRANSMEM    425    445       Helical; (Potential).
FT   TOPO_DOM    446    590       Cytoplasmic (Potential).
FT   REPEAT       60     83       LRR 1.
FT   REPEAT       84    107       LRR 2.
FT   REPEAT      108    131       LRR 3.
FT   REPEAT      132    155       LRR 4.
FT   REPEAT      157    179       LRR 5.
FT   REPEAT      180    203       LRR 6.
FT   REPEAT      205    227       LRR 7.
FT   REPEAT      228    251       LRR 8.
FT   REPEAT      252    275       LRR 9.
FT   REPEAT      276    299       LRR 10.
FT   CARBOHYD     58     58       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    126    126       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    291    291       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     518    518       I -> V (in isoform 2).
FT                                /FTId=VSP_014193.
FT   VAR_SEQ     519    590       Missing (in isoform 2).
FT                                /FTId=VSP_014194.
FT   CONFLICT      1      1       M -> MP (in Ref. 2).
SQ   SEQUENCE   590 AA;  67148 MW;  B67EB72235A55DC1 CRC64;
     MGFRLITQLK GMSVFLVLFP TLLLVMLTGA QRACPKNCRC DGKIVYCESH AFADIPENIS
     GGSQGLSLRF NSIQKLKSNQ FAGLNQLIWL YLDHNYISSV DEDAFQGIRR LKELILSSNK
     ITYLHNKTFH PVPNLRNLDL SYNKLQTLQS EQFKGLRKLI ILHLRSNSLK TVPIRVFQDC
     RNLDFLDLGY NRLRSLSRNA FAGLLKLKEL HLEHNQFSKI NFAHFPRLFN LRSIYLQWNR
     IRSVSQGLTW TWSSLHTLDL SGNDIQAIEP GTFKCLPNLQ KLNLDSNKLT NVSQETVNAW
     ISLISITLSG NMWECSRSIC PLFYWLKNFK GNKESTMICA GPKHIQGEKV SDAVETYNIC
     SDVQVVNTER SHLAPQTPQK PPFIPKPTIF KPDAVPATLE AVSPSPGFQI PGTDHEYEHV
     SFHKIIAGSV ALFLSVAMIL LVIYVSWKRY PASMKQLQQH SLMKRRRKKA RESERQMNSP
     LQEYYVDYKP TNSETMDISV NGSGPCTYTI SGSRECEIPH HVKPLPYYSY DQPVIGYCQA
     HQPLHINKAY EAVSIEQDDS PSLELGRDHS FIATIARSAA PAIYLERITN
//
ID   IF4G3_MOUSE             Reviewed;        1579 AA.
AC   Q80XI3; Q6GQV5; Q80Y69; Q8BJ68; Q8BQF3; Q8C6Q3; Q8CIH0;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 2.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Eukaryotic translation initiation factor 4 gamma 3;
DE            Short=eIF-4-gamma 3;
DE            Short=eIF-4G 3;
DE            Short=eIF4G 3;
DE   AltName: Full=eIF-4-gamma II;
DE            Short=eIF4GII;
GN   Name=Eif4g3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-217 AND 807-1579 (ISOFORM
RP   2), AND NUCLEOTIDE SEQUENCE OF 1-135 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Adipose tissue, Head, and Oviduct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 164-492.
RG   The MGC Project Team;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC   STRAIN=C57BL/6, and FVB/N;
RC   TISSUE=Brain, Colon, Kidney, Liver, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470 AND SER-472, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Probable component of the protein complex eIF4F, which
CC       is involved in the recognition of the mRNA cap, ATP-dependent
CC       unwinding of 5'-terminal secondary structure and recruitment of
CC       mRNA to the ribosome. Thought to be a functional homolog of EIF4G1
CC       (By similarity).
CC   -!- SUBUNIT: Interacts with EIF4A, EIF4E, eIF3 and PABPC1. Part of a
CC       complex with EIF4E. eIF4F is a multi-subunit complex, the
CC       composition of which varies with external and internal
CC       environmental conditions. It is composed of at least EIF4A, EIF4E
CC       and EIF4G1/EIF4G3. EIF4G1/EIF4G3 interacts through its C-terminus
CC       with the serine/threonine kinases MKNK1, and with MKNK2. Appears
CC       to act as a scaffold protein, holding these enzymes in place to
CC       phosphorylate eIF4E. Non-phosphorylated EIF4EBP1 competes with
CC       EIF4G1/EIFG3 to interact with EIF4E; insulin stimulated MAP-kinase
CC       (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes dissociation
CC       of the complex allowing EIF4G1/EIF4G3 to bind and consequent
CC       initiation of translation. EIF4G1/EIF4G3 interacts with PABPC1 to
CC       bring about circularization of the mRNA (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q80XI3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80XI3-2; Sequence=VSP_010491;
CC       Name=3;
CC         IsoId=Q80XI3-3; Sequence=VSP_010490;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q80XI3-4; Sequence=VSP_026029, VSP_010491;
CC   -!- SIMILARITY: Belongs to the eIF4G family.
CC   -!- SIMILARITY: Contains 5 HEAT repeats.
CC   -!- SIMILARITY: Contains 1 MI domain.
CC   -!- SIMILARITY: Contains 1 MIF4G domain.
CC   -!- SIMILARITY: Contains 1 W2 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH23898.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC       Sequence=AAH23898.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part;
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK029440; BAC26452.1; -; mRNA.
DR   EMBL; AK050887; BAC34445.1; -; mRNA.
DR   EMBL; AK054068; BAC35644.1; -; mRNA.
DR   EMBL; CB522417; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; CF743072; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC023898; AAH23898.1; ALT_INIT; mRNA.
DR   EMBL; BC047531; AAH47531.1; -; mRNA.
DR   EMBL; BC048848; AAH48848.1; -; mRNA.
DR   EMBL; BC057913; AAH57913.1; -; mRNA.
DR   EMBL; BC072600; AAH72600.1; -; mRNA.
DR   IPI; IPI00417153; -.
DR   IPI; IPI00417154; -.
DR   IPI; IPI00417155; -.
DR   IPI; IPI00626707; -.
DR   RefSeq; NP_766291.2; NM_172703.2.
DR   UniGene; Mm.268903; -.
DR   ProteinModelPortal; Q80XI3; -.
DR   SMR; Q80XI3; 136-161, 740-981, 1207-1572.
DR   STRING; Q80XI3; -.
DR   PhosphoSite; Q80XI3; -.
DR   PRIDE; Q80XI3; -.
DR   Ensembl; ENSMUST00000084214; ENSMUSP00000081232; ENSMUSG00000028760.
DR   Ensembl; ENSMUST00000084215; ENSMUSP00000081233; ENSMUSG00000028760.
DR   Ensembl; ENSMUST00000105831; ENSMUSP00000101457; ENSMUSG00000028760.
DR   Ensembl; ENSMUST00000105832; ENSMUSP00000101458; ENSMUSG00000028760.
DR   GeneID; 230861; -.
DR   KEGG; mmu:230861; -.
DR   UCSC; uc008vkd.1; mouse.
DR   CTD; 230861; -.
DR   MGI; MGI:1923935; Eif4g3.
DR   GeneTree; ENSGT00530000063038; -.
DR   HOVERGEN; HBG052083; -.
DR   OrthoDB; EOG45X7V7; -.
DR   NextBio; 380218; -.
DR   ArrayExpress; Q80XI3; -.
DR   Bgee; Q80XI3; -.
DR   Genevestigator; Q80XI3; -.
DR   GermOnline; ENSMUSG00000028760; Mus musculus.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007128; P:meiotic prophase I; IMP:MGI.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:MGI.
DR   GO; GO:0045727; P:positive regulation of translation; IMP:MGI.
DR   GO; GO:0016070; P:RNA metabolic process; IEA:InterPro.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003307; eIF5C.
DR   InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR   InterPro; IPR016021; MIF4-like_typ_1/2/3.
DR   InterPro; IPR003890; MIF4G-like_typ-3.
DR   Gene3D; G3DSA:1.25.40.180; MIF4-like_typ_1/2/3; 2.
DR   Pfam; PF02847; MA3; 1.
DR   Pfam; PF02854; MIF4G; 1.
DR   Pfam; PF02020; W2; 1.
DR   SMART; SM00515; eIF5C; 1.
DR   SMART; SM00544; MA3; 1.
DR   SMART; SM00543; MIF4G; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 3.
DR   PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
DR   PROSITE; PS51366; MI; 1.
DR   PROSITE; PS51363; W2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Initiation factor;
KW   Phosphoprotein; Protein biosynthesis; Repeat; RNA-binding;
KW   Translation regulation.
FT   CHAIN         1   1579       Eukaryotic translation initiation factor
FT                                4 gamma 3.
FT                                /FTId=PRO_0000213330.
FT   REPEAT      740    778       HEAT 1.
FT   DOMAIN      750    978       MIF4G.
FT   REPEAT      779    826       HEAT 2.
FT   REPEAT      827    900       HEAT 3.
FT   REPEAT      901    939       HEAT 4.
FT   REPEAT      940    979       HEAT 5.
FT   DOMAIN     1215   1337       MI.
FT   DOMAIN     1410   1579       W2.
FT   REGION      134    162       PABPC1-binding (By similarity).
FT   REGION      614    625       EIF4E-binding (By similarity).
FT   REGION      694   1014       eIF3/EIF4A-binding (By similarity).
FT   REGION     1427   1579       EIF4A-binding (By similarity).
FT   REGION     1565   1579       Necessary but not sufficient for MKNK1-
FT                                binding (By similarity).
FT   COILED      989   1018       Potential.
FT   COILED     1154   1176       Potential.
FT   COILED     1406   1438       Potential.
FT   MOD_RES     230    230       Phosphoserine (By similarity).
FT   MOD_RES     232    232       Phosphoserine (By similarity).
FT   MOD_RES     240    240       Phosphoserine.
FT   MOD_RES     267    267       Phosphoserine.
FT   MOD_RES     470    470       Phosphoserine.
FT   MOD_RES     472    472       Phosphoserine.
FT   MOD_RES     490    490       Phosphoserine (By similarity).
FT   MOD_RES     939    939       N6-acetyllysine (By similarity).
FT   MOD_RES    1150   1150       Phosphoserine; by CaMK1 (By similarity).
FT   VAR_SEQ      10     10       P -> PFAAGPRPAHHQGGFRPIQ (in isoform 4).
FT                                /FTId=VSP_026029.
FT   VAR_SEQ      11     11       F -> FAAGPRPAHHQF (in isoform 3).
FT                                /FTId=VSP_010490.
FT   VAR_SEQ    1084   1102       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_010491.
FT   CONFLICT    183    183       Missing (in Ref. 2; CF743072).
FT   CONFLICT    410    410       A -> G (in Ref. 2; CF743072).
FT   CONFLICT    492    492       A -> P (in Ref. 2; CB522417).
FT   CONFLICT   1324   1324       E -> G (in Ref. 1; BAC26452 and 3;
FT                                AAH72600).
SQ   SEQUENCE   1579 AA;  174890 MW;  EB4854590D250450 CRC64;
     MNSQPQARSP FFQRPQIQPP RAAIPNSSPS IRPGVQTPTA VYQANQHIMM VNHLPMPYPV
     TQGHQYCIPQ YRHSGPPYVG PPQQYPVQPP GPGPFYPGPG PGDFANAYGT PFYPSQPVYQ
     SAPIIVPTQQ QPPPAKREKK TIRIRDPNQG GKDITEEIMS GGGSRNPTPP IGRPASTPTP
     PQQLPSQVPE HSPVVYGTVE SAHLAASTPV TAASDQKQEE KPKPDPVFQS PSTVLRLVLS
     GEKKEQAGQM PETAAGEPTP EPPRTSSPTS LPPLARSSLP SPMSAALSSQ PLFTAEDKCE
     LPSSKEEDAP PVPSPTSCTA ASGPSLTDNS DICKKPCSVA PHDSQLISST ILINEMNGVG
     EKLSAKENTV GMLRQEVLPL TLELEILEHP QEELKVECTP TPIAPSMLPA FSPAPPTPPT
     SPPCPPVVLS AAIARSPAVA TEVQRVADEG ESLRTCLSKD AKEMQDKAES ESDGQAEETA
     DPQSLHSGRS PAPVQTATTA PKSWKKTKEQ TRTPDEVLEA EAEPKAEEEL AVDSVLEPEQ
     EKMSQGFPSE RDPSALKRGK AEEGNGEEAE PVRNGAESAS EGEGGDGNSG SADSSADGLT
     FPFKAESWKP ADTEGKKQYD REFLLDIQFM PACIQKPEGL PPISDVVLDK INQPRLSMRT
     LDPRILPRGP DFTPAFADFP RQTPGGRGVP LLNVGPRRSQ PGQRREPRKI ITVSVKEDVH
     LRKAENAWKP SQKRDSHADD PESIKTQELF RKVRSILNKL TPQMFNQLMK QVSALTVDTE
     ERLKGVIDLV FEKAIDEPSF SVAYANMCRC LVTLKVPMAD KPGNTVNFRK LLLNRCQKEF
     EKDKADDDVF EKKQKELEAA SAPEERTRLH DELEEAKDKA RRRSIGNIKF IGELFKLKML
     TEAIMHDCVV KLLKNHDEES LECLCRLLTT IGKDLDFEKA KPRMDQYFNQ MEKIVKERKT
     SSRIRFMLQD VIDLRLCNWV SRRADQGPKT IEQIHKEAKI EEQEEQRKVQ QLMTKEKRRP
     GVQRVDEGGW NTVQGAKNSR VLDPSKFLKI TKPTIDEKIQ LVPKAQLGSW GKGSSGGAKA
     SESDALRSSA SSLNRFSPLQ PPAPSGSPSA TPLEFDSRRA LTSRGSMGRE KSDKPIPAGT
     ARPNTFLRGS SKDLLDNQSQ EEQRREMLET VKQLTGGLDA ERASTEADRS KTRELAKSEM
     CAVPAPDKPA LSEEEVERKS KSIIDEFLHI NDFKEATQCI EELSAQGPLH VFVKVGVEFT
     LERSQITRDH MGHLLYQLVQ SEKLSKQDFF KGFSETLELA DDMAIDIPHI WLYLAELVTP
     MLKEGGISMR ELIVEFSKPL LPVGRAGVLL SEILHLLCRQ MSHKKVGALW READLSWKDF
     LPEGEDVHHF LLEQKLDFTE SEGPCSSEAL SKKELSAEEL SQRLEKLIME EKADDERIFD
     WVEANLDESQ MSSPTFLRAL MTAVCKAAII ADCSTFRVDT AVIKQRVPIL LKYLDSDTEK
     ELQALYALQA SIVKLDQPAN LLRMFFDCLY DEEVISEDAF YKWESSKDPA EQAGKGVALK
     SVTAFFTWLR EAEEESEDN
//
ID   PI42B_MOUSE             Reviewed;         416 AA.
AC   Q80XI4; Q8VHB2;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Phosphatidylinositol-5-phosphate 4-kinase type-2 beta;
DE            EC=2.7.1.149;
DE   AltName: Full=1-phosphatidylinositol-5-phosphate 4-kinase 2-beta;
DE   AltName: Full=Diphosphoinositide kinase 2-beta;
DE   AltName: Full=Phosphatidylinositol-5-phosphate 4-kinase type II beta;
DE            Short=PI(5)P 4-kinase type II beta;
DE            Short=PIP4KII-beta;
DE   AltName: Full=PtdIns(5)P-4-kinase isoform 2-beta;
GN   Name=Pip4k2b; Synonyms=Pip5k2b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 25-416.
RC   STRAIN=Swiss Webster / NIH;
RX   PubMed=12438746; DOI=10.1159/000064062;
RA   Kleiter N., Artner I., Gmachl N., Ghaffari-Tabrizi N., Kratochwil K.;
RT   "Mutagenic transgene insertion into a region of high gene density and
RT   multiple linkage disruptions on mouse chromosome 11.";
RL   Cytogenet. Genome Res. 97:100-105(2002).
RN   [3]
RP   PROTEIN SEQUENCE OF 79-86; 110-123; 189-202; 267-275; 291-301 AND
RP   389-405, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: Participates in the biosynthesis of
CC       phosphatidylinositol-4,5-bisphosphate (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 5-
CC       phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
CC   -!- SUBUNIT: Homodimer. Binds TNFRSF1A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein (By similarity). Cell membrane; Peripheral
CC       membrane protein (By similarity). Note=Associated with the plasma
CC       membrane and the endoplasmic reticulum (By similarity).
CC   -!- PTM: Phosphorylated on serine residues (By similarity).
CC   -!- SIMILARITY: Contains 1 PIPK domain.
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DR   EMBL; BC047282; AAH47282.1; -; mRNA.
DR   EMBL; AY050219; AAL18245.1; -; mRNA.
DR   IPI; IPI00336318; -.
DR   RefSeq; NP_473392.1; NM_054051.1.
DR   UniGene; Mm.39700; -.
DR   ProteinModelPortal; Q80XI4; -.
DR   SMR; Q80XI4; 34-416.
DR   STRING; Q80XI4; -.
DR   PhosphoSite; Q80XI4; -.
DR   PRIDE; Q80XI4; -.
DR   Ensembl; ENSMUST00000018691; ENSMUSP00000018691; ENSMUSG00000018547.
DR   GeneID; 108083; -.
DR   KEGG; mmu:108083; -.
DR   UCSC; uc007leq.1; mouse.
DR   CTD; 108083; -.
DR   MGI; MGI:1934234; Pip4k2b.
DR   HOGENOM; HBG314662; -.
DR   HOVERGEN; HBG000072; -.
DR   InParanoid; Q80XI4; -.
DR   OMA; ECENDGM; -.
DR   OrthoDB; EOG4SQWX1; -.
DR   PhylomeDB; Q80XI4; -.
DR   BRENDA; 2.7.1.149; 244.
DR   NextBio; 360024; -.
DR   ArrayExpress; Q80XI4; -.
DR   Bgee; Q80XI4; -.
DR   Genevestigator; Q80XI4; -.
DR   GermOnline; ENSMUSG00000018547; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016309; F:1-phosphatidylinositol-5-phosphate 4-kinase activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; IDA:MGI.
DR   InterPro; IPR002498; PInositol-4-P-5-kinase_core.
DR   InterPro; IPR016034; PInositol-4P-5-kinase_core_sub.
DR   PANTHER; PTHR23086; PIP5K; 1.
DR   Pfam; PF01504; PIP5K; 1.
DR   SMART; SM00330; PIPKc; 1.
DR   PROSITE; PS51455; PIPK; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cell membrane; Direct protein sequencing;
KW   Endoplasmic reticulum; Kinase; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Transferase.
FT   CHAIN         1    416       Phosphatidylinositol-5-phosphate 4-kinase
FT                                type-2 beta.
FT                                /FTId=PRO_0000185471.
FT   DOMAIN       38    415       PIPK.
FT   COMPBIAS    303    308       Poly-Glu.
FT   MOD_RES      17     17       Phosphoserine (By similarity).
FT   MOD_RES      98     98       Phosphotyrosine (By similarity).
FT   MOD_RES     150    150       N6-acetyllysine (By similarity).
FT   MOD_RES     322    322       Phosphothreonine (By similarity).
FT   MOD_RES     326    326       Phosphoserine (By similarity).
SQ   SEQUENCE   416 AA;  47319 MW;  F967720CF3979550 CRC64;
     MSSNCTSTTA VAVAPLSASK TKTKKKHFVC QKVKLFRASE PILSVLMWGV NHTINELSNV
     PVPVMLMPDD FKAYSKIKVD NHLFNKENLP SRFKFKEYCP MVFRNLRERF GIDDQDYQNS
     VTRSAPINSD SQGRCGTRFL TTYDRRFVIK TVSSEDVAEM HNILKKYHQF IVECHGNTLL
     PQFLGMYRLT VDGVETYMVV TRNVFSHRLT VHRKYDLKGS TVAREASDKE KAKDLPTFKD
     NDFLNEGQKL HVGEESKKNF LEKLKRDVEF LAQLKIMDYS LLVGIHDVDR AEQEEMEVEE
     RAEEEECEND GVGGSLLCSY GTPPDSPGNL LSFPRFFGPG EFDPSVDVYA MKSHESAPKK
     EVYFMAIIDI LTPYDAKKKA AHAAKTVKHG AGAEISTVNP EQYSKRFNEF MSNILT
//
ID   M3K11_MOUSE             Reviewed;         850 AA.
AC   Q80XI6; Q8K0M8; Q9JJ15;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Mitogen-activated protein kinase kinase kinase 11;
DE            EC=2.7.11.25;
DE   AltName: Full=Mixed lineage kinase 3;
GN   Name=Map3k11; Synonyms=Mlk3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Ola;
RX   MEDLINE=20354997; PubMed=10894943;
RA   Saridaki A., Ferraz C., Demaille J., Scherer G., Roux A.-F.;
RT   "Genomic sequencing reveals the structure of the Kcnk6 and map3k11
RT   genes and their close vicinity to the sipa1 gene on mouse chromosome
RT   19.";
RL   Cytogenet. Cell Genet. 89:85-88(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon, Eye, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Activates the JUN N-terminal pathway. Required for
CC       serum-stimulated cell proliferation and for mitogen and cytokine
CC       activation of MAPK14 (p38), MAPK3 (ERK) and MAPK8 (JNK1). Plays a
CC       role in mitogen-stimulated phosphorylation and activation of BRAF,
CC       but does not phosphorylate BRAF directly. Influences microtubule
CC       organization during the cell cycle (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Homodimerization via the leucine zipper domains
CC       is required for autophosphorylation and subsequent activation (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer; undergoes dimerization during activation (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome.
CC       Note=Location is cell cycle dependent (By similarity).
CC   -!- PTM: Autophosphorylation on serine and threonine residues within
CC       the activation loop plays a role in enzyme activation. Thr-278 is
CC       likely to be the main autophosphorylation site. Phosphorylation of
CC       Ser-556 and Ser-557 is induced by CDC42 (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF155142; AAF73281.1; -; Genomic_DNA.
DR   EMBL; BC030928; AAH30928.1; -; mRNA.
DR   EMBL; BC047152; AAH47152.1; -; mRNA.
DR   EMBL; BC095963; AAH95963.1; -; mRNA.
DR   IPI; IPI00330731; -.
DR   RefSeq; NP_071295.2; NM_022012.3.
DR   UniGene; Mm.185026; -.
DR   HSSP; Q07912; 1U4D.
DR   ProteinModelPortal; Q80XI6; -.
DR   SMR; Q80XI6; 43-380.
DR   IntAct; Q80XI6; 2.
DR   STRING; Q80XI6; -.
DR   PhosphoSite; Q80XI6; -.
DR   PRIDE; Q80XI6; -.
DR   Ensembl; ENSMUST00000004156; ENSMUSP00000004156; ENSMUSG00000004054.
DR   GeneID; 26403; -.
DR   KEGG; mmu:26403; -.
DR   UCSC; uc008get.1; mouse.
DR   CTD; 26403; -.
DR   MGI; MGI:1346880; Map3k11.
DR   eggNOG; roNOG09382; -.
DR   GeneTree; ENSGT00600000084346; -.
DR   HOGENOM; HBG716519; -.
DR   HOVERGEN; HBG067662; -.
DR   InParanoid; Q80XI6; -.
DR   OMA; SNYVSRG; -.
DR   OrthoDB; EOG4PNXGN; -.
DR   PhylomeDB; Q80XI6; -.
DR   BRENDA; 2.7.11.25; 244.
DR   NextBio; 304369; -.
DR   ArrayExpress; Q80XI6; -.
DR   Bgee; Q80XI6; -.
DR   CleanEx; MM_MAP3K11; -.
DR   Genevestigator; Q80XI6; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR015785; MAPKKK-like.
DR   InterPro; IPR016231; MAPKKK9/10/11.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   PANTHER; PTHR23257:SF87; MAPKKK-like; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   PIRSF; PIRSF000556; MAPKKK9_11; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Repeat; Serine/threonine-protein kinase; SH3 domain;
KW   Transferase.
FT   CHAIN         1    850       Mitogen-activated protein kinase kinase
FT                                kinase 11.
FT                                /FTId=PRO_0000277828.
FT   DOMAIN       42    106       SH3.
FT   DOMAIN      118    380       Protein kinase.
FT   DOMAIN      404    425       Leucine-zipper 1.
FT   DOMAIN      439    460       Leucine-zipper 2.
FT   NP_BIND     124    132       ATP (By similarity).
FT   COMPBIAS     18     29       Poly-Gly.
FT   COMPBIAS    473    476       Poly-Arg.
FT   COMPBIAS    600    823       Pro-rich.
FT   ACT_SITE    242    242       Proton acceptor (By similarity).
FT   BINDING     145    145       ATP (By similarity).
FT   MOD_RES      35     35       Phosphoserine (By similarity).
FT   MOD_RES     278    278       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     282    282       Phosphoserine; by autocatalysis and
FT                                MAP4K1 (By similarity).
FT   MOD_RES     395    395       Phosphoserine (By similarity).
FT   MOD_RES     494    494       Phosphoserine (By similarity).
FT   MOD_RES     508    508       Phosphoserine (By similarity).
FT   MOD_RES     525    525       Phosphoserine (By similarity).
FT   MOD_RES     549    549       Phosphoserine (By similarity).
FT   MOD_RES     556    556       Phosphoserine (By similarity).
FT   MOD_RES     557    557       Phosphoserine (By similarity).
FT   MOD_RES     570    570       Phosphoserine (By similarity).
FT   MOD_RES     655    655       Phosphoserine (By similarity).
FT   MOD_RES     704    704       Phosphothreonine (By similarity).
FT   MOD_RES     709    709       Phosphoserine (By similarity).
FT   MOD_RES     712    712       Phosphothreonine (By similarity).
FT   MOD_RES     728    728       Phosphoserine (By similarity).
FT   MOD_RES     731    731       Phosphoserine (By similarity).
FT   MOD_RES     741    741       Phosphothreonine (By similarity).
FT   MOD_RES     743    743       Phosphoserine.
FT   MOD_RES     749    749       Phosphoserine (By similarity).
FT   MOD_RES     751    751       Phosphoserine (By similarity).
FT   MOD_RES     755    755       Phosphothreonine (By similarity).
FT   MOD_RES     758    758       Phosphothreonine (By similarity).
FT   MOD_RES     761    761       Phosphoserine (By similarity).
FT   MOD_RES     773    773       Phosphoserine (By similarity).
FT   MOD_RES     792    792       Phosphoserine (By similarity).
FT   MOD_RES     796    796       Phosphoserine (By similarity).
FT   MOD_RES     818    818       Phosphoserine (By similarity).
FT   CONFLICT    457    458       EL -> DV (in Ref. 1; AAF73281).
FT   CONFLICT    840    841       AQ -> CP (in Ref. 1; AAF73281).
SQ   SEQUENCE   850 AA;  93226 MW;  96DE238A1A0E2564 CRC64;
     MEPLKNLFLK SPLGSWNGSG SGGGGGTGGV RPEGSPKATA AYANPVWTAL FDYEPNGQDE
     LALRKGDRVE VLSRDAAISG DEGWWAGQVG GQVGIFPSNY VSRGGGPPPC EVASFQELRL
     EEVIGIGGFG KVYRGSWRGE LVAVKAARQD PDEDISVTAE SVRQEARLFA MLAHPNIIAL
     KAVCLEEPNL CLVMEYAAGG PLSRALAGRR VPPHVLVNWA VQIARGMHYL HCEALVPVIH
     RDLKSNNILL LQPIEGDDME HKTLKITDFG LAREWHKTTQ MSAAGTYAWM APEVIKASTF
     SKGSDVWSFG VLLWELLTGE VPYRGIDCLA VAYGVAVNKL TLPIPSTCPE PFAQLMADCW
     AQDPHRRPDF ASILQQLEAL EAQVLREMPR DSFHSMQEGW KREIQGLFDE LRAKEKELLS
     REEELTRAAR EQRSQAEQLR RREHLLAQWE LEVFERELTL LLQQVDRERP HVRRRRGTFK
     RSKLRARDGG ERISMPLDFK HRITVQASPG LDRRRNVFEV GAGDSPTFPR FRAIQLEPTE
     SGQTWGRQSP RRLEDSSNGE RRACWAWGPS SPKPGEAQNG RRRSRMDEAT WYLDSDDSSP
     LGSPSTPPAL NGNPPRPSPE PEEPRRAGPT ERGNSSGTPK LIQRALLRGT ALLASLGLGR
     DLQPPGGLSR ERGESPTAPP PAQMPSPCPP ELPSTPLIRL SQTTPDAHSS PTPGPLLLDL
     GVPSGQPSAK SPRREETRGR TVSPPPGISR SAPGTPGTPR SPPLGLISRP RPSPLRSRID
     PWSFVSAGPR PSPLPSPQPA PRRAPWTLFP DSDPFWDSPP ANPFRGGSQD CRTQTKDMGA
     QAPWAPEAGP
//
ID   RN168_MOUSE             Reviewed;         565 AA.
AC   Q80XJ2;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 3.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF168;
DE            EC=6.3.2.-;
DE   AltName: Full=RING finger protein 168;
GN   Name=Rnf168;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase required for accumulation of
CC       repair proteins to sites of DNA damage. Acts with UBE2N/UBC13 to
CC       amplify the RNF8-dependent histone ubiquitination. Recruited to
CC       sites of DNA damage at double-strand breaks (DSBs) by binding to
CC       ubiquitinated histone H2A and ubiquitinates histone H2A and H2AX,
CC       leading to amplify the RNF8-dependent H2A ubiquitination and
CC       promoting the formation of 'Lys-63'-linked ubiquitin conjugates.
CC       This leads to concentrate ubiquitinated histones H2A and H2AX at
CC       DNA lesions to the threshold required for recruitment of TP53BP1
CC       and BRCA1 (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with UBE2N/UBC13 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Note=Localizes to
CC       sites of DNA damage (By similarity).
CC   -!- DOMAIN: The MIU motifs (motif interacting with ubiquitin) mediate
CC       the interaction with ubiquitin and the localization at sites of
CC       DNA damage.
CC   -!- SIMILARITY: Belongs to the RNF168 family.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH46815.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=AAH46815.1; Type=Erroneous termination; Positions=551; Note=Translated as Gln;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC126265; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC046815; AAH46815.1; ALT_SEQ; mRNA.
DR   IPI; IPI00330736; -.
DR   RefSeq; NP_081631.2; NM_027355.2.
DR   UniGene; Mm.228263; -.
DR   ProteinModelPortal; Q80XJ2; -.
DR   SMR; Q80XJ2; 1-112.
DR   STRING; Q80XJ2; -.
DR   PhosphoSite; Q80XJ2; -.
DR   PRIDE; Q80XJ2; -.
DR   Ensembl; ENSMUST00000014218; ENSMUSP00000014218; ENSMUSG00000014074.
DR   GeneID; 70238; -.
DR   KEGG; mmu:70238; -.
DR   UCSC; uc007yyo.1; mouse.
DR   CTD; 70238; -.
DR   MGI; MGI:1917488; Rnf168.
DR   eggNOG; roNOG14238; -.
DR   HOGENOM; HBG282499; -.
DR   HOVERGEN; HBG067220; -.
DR   InParanoid; Q80XJ2; -.
DR   OMA; KSIFQMF; -.
DR   OrthoDB; EOG4THVT2; -.
DR   NextBio; 331230; -.
DR   ArrayExpress; Q80XJ2; -.
DR   Bgee; Q80XJ2; -.
DR   CleanEx; MM_RNF168; -.
DR   Genevestigator; Q80XJ2; -.
DR   GermOnline; ENSMUSG00000014074; Mus musculus.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR   GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR   GO; GO:0070535; P:histone H2A K63-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR   GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; DNA damage; DNA repair; Ligase; Metal-binding;
KW   Nucleus; Phosphoprotein; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    565       E3 ubiquitin-protein ligase RNF168.
FT                                /FTId=PRO_0000245597.
FT   ZN_FING      16     55       RING-type.
FT   MOTIF       168    191       MIU motif 1.
FT   MOTIF       438    461       MIU motif 2.
FT   COMPBIAS    115    177       Glu-rich.
FT   MOD_RES     413    413       Phosphoserine (By similarity).
FT   MOD_RES     414    414       Phosphoserine (By similarity).
FT   MOD_RES     420    420       Phosphothreonine (By similarity).
SQ   SEQUENCE   565 AA;  64779 MW;  F862617604CB1229 CRC64;
     MAAPKTSIPS LAECQCGICM EILLEPVTLP CNHTLCNPCF QSTVEKANLC CPFCRRRVSS
     WTRYHTRRNS LVNTDLWEII QKHYAKECKL RISGQESKEI IDECQPVRRL SEPGELRREY
     EEEISRVEAE RQASKEEENK ASEEYIQRLL AEEEEEEKRQ REKRRSEMEE QLRGDEELAR
     SLSTSINSNY ERNTLASPLS SRKSDPVTNK SQKKNTSKQK TFGDIQKYLS PKLKPGTALA
     CKAELEEDIC KSKETDRSDT KSPVLQDTEI EKNIPTLSPQ TCLETQEQGS ESSAGIPGPQ
     LCVGDTKESL EGKVETVSTS PDDLCIVNDD GPRATVFYSN EAAVNSSSKI ENEEYSVTGV
     PQLTGGNRVP TESRVYHLLV EEEISDRENQ ESVFEEVMDP CFSAKRRKIF IESSSDQEET
     EVNFTQKLID LEHMLFERHK QEEQDRLLAL QLQKEVDKEQ MVPNRQKGSP DQYQLRTPSP
     PDRLLNRQRK NSKDRNSLQQ TNADHSKSPR NTKGDYWEPF KNTWKDSVNG TKMPTSTQDN
     CNVSKSAYTV QHRKSQRSIV QMFQR
//
ID   ATG2B_MOUSE             Reviewed;        2075 AA.
AC   Q80XK6; A0PJL7; Q8BIQ4; Q8BIV0; Q8R1H5; Q9CWK6;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 3.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Autophagy-related protein 2 homolog B;
GN   Name=Atg2b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-797 (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryonic stem cell, Heart, Hippocampus, and Wolffian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Colon, Limb, and Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1581, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q80XK6-2; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80XK6-4; Sequence=VSP_035038;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q80XK6-5; Sequence=VSP_035039;
CC   -!- SIMILARITY: Belongs to the ATG2 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH46427.3; Type=Erroneous initiation;
CC       Sequence=AK085790; Type=Frameshift; Positions=32, 52, 352;
CC       Sequence=BAC28052.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK010577; BAB27040.1; -; mRNA.
DR   EMBL; AK032840; BAC28052.1; ALT_INIT; mRNA.
DR   EMBL; AK083213; BAC38812.1; -; mRNA.
DR   EMBL; AK085790; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC024533; AAH24533.1; -; mRNA.
DR   EMBL; BC046427; AAH46427.3; ALT_INIT; mRNA.
DR   EMBL; BC062182; AAH62182.1; -; mRNA.
DR   IPI; IPI00377925; -.
DR   IPI; IPI00377926; -.
DR   IPI; IPI00903395; -.
DR   RefSeq; NP_083930.5; NM_029654.4.
DR   UniGene; Mm.114362; -.
DR   UniGene; Mm.125279; -.
DR   PhosphoSite; Q80XK6; -.
DR   PRIDE; Q80XK6; -.
DR   Ensembl; ENSMUST00000041055; ENSMUSP00000037441; ENSMUSG00000041341.
DR   GeneID; 76559; -.
DR   KEGG; mmu:76559; -.
DR   UCSC; uc007oyo.1; mouse.
DR   CTD; 76559; -.
DR   MGI; MGI:1923809; Atg2b.
DR   eggNOG; roNOG04369; -.
DR   GeneTree; ENSGT00580000081561; -.
DR   HOGENOM; HBG315549; -.
DR   HOVERGEN; HBG079553; -.
DR   InParanoid; Q80XK6; -.
DR   OMA; KHGEFWL; -.
DR   OrthoDB; EOG49S65D; -.
DR   ArrayExpress; Q80XK6; -.
DR   Bgee; Q80XK6; -.
DR   Genevestigator; Q80XK6; -.
DR   GermOnline; ENSMUSG00000041341; Mus musculus.
DR   InterPro; IPR015412; Autophagy-rel_C.
DR   Pfam; PF09333; ATG_C; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1   2075       Autophagy-related protein 2 homolog B.
FT                                /FTId=PRO_0000089910.
FT   MOD_RES     240    240       Phosphoserine (By similarity).
FT   MOD_RES     496    496       Phosphoserine (By similarity).
FT   MOD_RES    1581   1581       Phosphoserine.
FT   VAR_SEQ       1   1890       Missing (in isoform 2).
FT                                /FTId=VSP_035038.
FT   VAR_SEQ     577   2075       Missing (in isoform 3).
FT                                /FTId=VSP_035039.
FT   CONFLICT    128    128       A -> T (in Ref. 2; BAC28052).
FT   CONFLICT    356    356       R -> Q (in Ref. 2; BAC38812).
FT   CONFLICT   1577   1577       I -> IS (in Ref. 1; AAH46427).
FT   CONFLICT   1914   1914       K -> R (in Ref. 1; AAH62182).
SQ   SEQUENCE   2075 AA;  231399 MW;  CF44446E4810C1EF CRC64;
     MPWPFSESIK KRACRYLLQR YLGHFLQEKL SLEQLSLDLY QGTGSLAQVP LDKWCLNEIL
     ESADAPLEVT EGFIQSISLS VPWGSLLQDN CALEVRGLEM VFRPRPRVAT GSEPMYWSSF
     MTSSMQLAKE CLSQKLTDEQ GEASQPFEGL EKFAETIETV LRRVKVTFID TVLRIEHVPE
     NSKTGAALEI RVDRTVYCDE TADESSGVNV HQPTAFAHKL LQLSGVSLFW DEFSASAKSS
     PVCSTAPVET EPKLSPSWNP KIVYEPHPQL TRTLPEIAPS DPVQIGRLLG RLELSLTLKQ
     NEVLPGAKLD VDGQIDSFHL FLSPRQVHLL LDMLAAIAGP ENSSKIGLAN KDRKNRPMQQ
     EDEYRIQMEL NRYYLRKDSL SMGVSSEKSF YETETARTPS SREEEVFFSM ADMDMSHSLS
     SLPPLGDPPH MDLELSLTST YTNTPAGSPL SATVLQPTWG EFADHKEQPV RGPAFQSDVV
     HPASLQKAAL SSRSASVDES RPEFICRLAL GIFSVSVLHI DPLSPAETSL NVNPLTRMAT
     DFFSCVEKMD PAIFSTGDFK SFRAVFAEAC SHDHLRFIGT GIKVSYEQRQ RSASRHFSTD
     MSVGQMEFLE CLFPTDCHSV PSHYTELLTF HSKEGTDAHL PVCLQLHYKH SETRGPQGNQ
     ARLSSVPQKA ELQIKLNPVC CELDISIVDR LNSLLQPQKL TTVEMMASHM YASYNKHISL
     HKAFTEVFLD DSHSPANRRV SVQVATPALH LSVRFPIPDL RSDQERGPWF KKSLQKETLH
     LEFTDLESKT EFVGGSTPEQ TKLELTFREL SGSFQEEKGG PSVKFFHVSG GVDGDTASSD
     DFDWPRMVLK INPPAMHSIL ERIAAEEEEE NDGHYQEEED GGAHSLKDVC DLRRPAPSPF
     SSRRVMFENE QMVMPGDPVE MTEFQDKAIS NSHYVLELLL PNIHLTLPNK GFYEKLYNRI
     FNDLLLWEPT APSPVETLEN VSYGIGLSVA SQLINTFSKD SFSPFKSAVH YDEDSGSEEE
     TLQYFSAVDP NYRSRRKKKL DSQNKNSQSF LSVLLSINHG LMAVFTDVKQ ENGDPMESKH
     GEFWLEFNSG SFFCVTKYEG FEDKHYICLH SSSLRLYHKG IVDGAILPTE TRLPCSTRPH
     WLEPTIYSSE EDGLSRTASD GVGGDNLNML SVAVKILSDK SESNTKEFLV AVGLKGATLQ
     HRVLPAGLSW HEQILNFLNI ADEPVLGYNP PTSFTTFHVH LWSCALDYRP LHLPLRSLLT
     VETFSISSSV ALDKSSSTLR IIMDEAALHL SDKCNTVTVN LNRDYVRVMD MGLLELTITA
     VKSDSDGEQT APRFELHCSS DVVHIRTCSD SCAALMNLIQ YVASYGDLHG PHKAEMKPGV
     PQRKPKVDSS ARSSSHGPVL PEADQQILRD LMSDAMEEID LQQASAPVGP QANGVLDEKS
     HTQEPCCSDL FLFPDESGNV SQESSPAYPS LTHHLISDAV TGVTAENDDF CILFAPKTVV
     QEKEEEPVIK IMVDDAIVIK DDYFSLPITR TDSSKAPLHF PIPAVRYVVK EVSLVWHLYG
     GKDFATAPPT SPAKSYIPHS SPSQTPTRHG RHTVCGGKGR NHDFLMEIQL SKVKFQHEVY
     PPCKPECESS LLEHPVSRQV FIVQDLEIRD RLATSQMNKF LYLYCSKDMP RKAHSNMLTI
     KALHVRPESG RSPQECCLRV SLMPLRLNID QDALFFLKDF FTSLSTEVEL LLTPDPEVTK
     SPGADVTCSL PRHLSTSKEP NLVVSFPGPK QASPNHRANS AEGGNGLEED VSAEETSFSD
     QPVFFREFRF TAEVPIRLDY HGKHVSMDQG TLAGILIGLA QLNCSELKLK RLFYRHGLLG
     IDKLFSYAIS EWLSDIKKNQ LPGILGGVGP MHSLVQLVQG LKDLVWLPIE QYRKDGRIVR
     GFQRGAASFG TSTAMAALEL TNRMVQTIQA AAETAYDMVS PSTLSIEPKK AKRFPHHRLA
     HQPVDLREGV AKAYSVVKEG ITDTAQTIYE TAAREHESRG VTGAVGEVLR QIPPAVVRPL
     IVATEATSNV LGGMRNQIRP DVRQDESQKW RHGED
//
ID   Q80XN6_MOUSE            Unreviewed;       448 AA.
AC   Q80XN6;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   SubName: Full=F-box and WD-40 domain protein 9, isoform CRA_b;
DE   SubName: Full=Fbxw9 protein;
DE   Flags: Fragment;
GN   Name=Fbxw9; ORFNames=mCG_14329;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 F-box domain.
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DR   EMBL; BC043658; AAH43658.1; -; mRNA.
DR   EMBL; CH466525; EDL10992.1; -; Genomic_DNA.
DR   IPI; IPI00762234; -.
DR   UniGene; Mm.374815; -.
DR   ProteinModelPortal; Q80XN6; -.
DR   PhosphoSite; Q80XN6; -.
DR   Ensembl; ENSMUST00000095220; ENSMUSP00000092845; ENSMUSG00000008167.
DR   UCSC; uc009mpd.1; mouse.
DR   MGI; MGI:1915878; Fbxw9.
DR   HOGENOM; HBG446095; -.
DR   HOVERGEN; HBG051598; -.
DR   InParanoid; Q80XN6; -.
DR   ArrayExpress; Q80XN6; -.
DR   Bgee; Q80XN6; -.
DR   Genevestigator; Q80XN6; -.
DR   InterPro; IPR001810; F-box_dom_cyclin-like.
DR   InterPro; IPR022364; F-box_dom_Skp2-like.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 5.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00256; FBOX; 1.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF81383; F-box_dom_Skp2-like; 1.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS50181; FBOX; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Repeat; WD repeat.
FT   NON_TER       1      1
SQ   SEQUENCE   448 AA;  49541 MW;  320AEB49B26D7B39 CRC64;
     PRSCEEESDP EPDPDPDTQA EAYVARVLTP PKLGLTPRRT SLQSMFSASL GVPERKAASK
     VPAVRLPGLL SLPPELLLEI CAYLDARVVL QVLPCVCQAL HDLVRDRVTW RLRAQRRVRA
     PYPVVEEENF DWPAACIELE QHLARWAEDG QRTEYFCLAD GHFASIDAVL LLQGGALCLS
     GSRDRNVNLW DLRHLGKDPS RVLVKALGTQ GNSTHKGWVW SLAAQDHRVC SGSWDSTVKL
     WDMAADGQQF GEIKGKAAVL CLSYQPDILV TGTYDKKVTI YDPRAGLALV KSRRLHSSAV
     LAVLADDRHV ISGSEDHSLV VFDRRANSVL QRLQLDSYLL CMSYQEPQLW AGDNQGLLHV
     FANRDGCFQL VRSFDVGHQS QITGIKHSLG TLYTTSTDKT IRVHVPTDPP RTICTRSHHN
     VLNGICAEGN VVVAASGGLS LEVWRLLA
//
ID   FA76B_MOUSE             Reviewed;         339 AA.
AC   Q80XP8; Q3UMA6; Q80YR1; Q8CI69;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Protein FAM76B;
GN   Name=Fam76b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, Embryo, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80XP8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80XP8-2; Sequence=VSP_019774, VSP_019775, VSP_019776,
CC                                  VSP_019777;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the FAM76 family.
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DR   EMBL; AK145026; BAE26192.1; -; mRNA.
DR   EMBL; BC036328; AAH36328.1; -; mRNA.
DR   EMBL; BC043120; AAH43120.1; -; mRNA.
DR   EMBL; BC050870; AAH50870.1; -; mRNA.
DR   IPI; IPI00330763; -.
DR   IPI; IPI00776391; -.
DR   RefSeq; NP_789806.1; NM_176836.3.
DR   UniGene; Mm.246174; -.
DR   ProteinModelPortal; Q80XP8; -.
DR   PhosphoSite; Q80XP8; -.
DR   PRIDE; Q80XP8; -.
DR   Ensembl; ENSMUST00000059579; ENSMUSP00000062642; ENSMUSG00000037808.
DR   GeneID; 72826; -.
DR   KEGG; mmu:72826; -.
DR   UCSC; uc009oef.1; mouse.
DR   UCSC; uc009oeh.1; mouse.
DR   CTD; 72826; -.
DR   MGI; MGI:1920076; Fam76b.
DR   eggNOG; roNOG12535; -.
DR   GeneTree; ENSGT00390000014462; -.
DR   HOGENOM; HBG314249; -.
DR   HOVERGEN; HBG080224; -.
DR   InParanoid; Q80XP8; -.
DR   OMA; ACTKCNQ; -.
DR   OrthoDB; EOG4N04FF; -.
DR   PhylomeDB; Q80XP8; -.
DR   NextBio; 336999; -.
DR   ArrayExpress; Q80XP8; -.
DR   Bgee; Q80XP8; -.
DR   CleanEx; MM_2810485I05RIK; -.
DR   Genevestigator; Q80XP8; -.
DR   GermOnline; ENSMUSG00000037808; Mus musculus.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Coiled coil; Isopeptide bond;
KW   Phosphoprotein; Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    339       Protein FAM76B.
FT                                /FTId=PRO_0000245764.
FT   COILED      248    328       Potential.
FT   COMPBIAS    151    160       Poly-Ser.
FT   COMPBIAS    167    187       His-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      22     22       Phosphoserine (By similarity).
FT   MOD_RES     193    193       Phosphoserine (By similarity).
FT   CROSSLNK    225    225       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   VAR_SEQ       1    208       Missing (in isoform 2).
FT                                /FTId=VSP_019774.
FT   VAR_SEQ     209    230       AAIQNETPKKKPKLESKPSNGD -> MQFEHLQIFLLLYVI
FT                                PFYFFLF (in isoform 2).
FT                                /FTId=VSP_019775.
FT   VAR_SEQ     311    319       AKNRELLKQ -> VNGVIYVRC (in isoform 2).
FT                                /FTId=VSP_019776.
FT   VAR_SEQ     320    339       Missing (in isoform 2).
FT                                /FTId=VSP_019777.
FT   CONFLICT    180    180       H -> HH (in Ref. 1; BAE26192).
FT   CONFLICT    233    233       Missing (in Ref. 2; AAH50870).
SQ   SEQUENCE   339 AA;  38556 MW;  9A64D910ECC71178 CRC64;
     MAASALYACT KCTQRYPFEE LSQGQQLCKE CRIAHPIVKC TYCRSEFQQE SKTNTICKKC
     AQNVKQFGTP KPCQYCNIIA AFIGTKCQRC TNSEKKYGAP QTCEQCKQQC AFDRKEEGRR
     KVDGKLLCWL CTLSYKRVLQ KTKEQRKSLG SSHSNSSSSS LTEKDQHHSK HHHHHHHHHH
     RHSSGHHKVS SLSPEQEQGL WKQSHKSSAA IQNETPKKKP KLESKPSNGD SSSINQSADS
     GGTDNFVLIS QLKEEVMSLK RLLQQRDQTI LEKDKKLTEL KADFQYQESN LRTKMNSMEK
     AHKETVEQLQ AKNRELLKQV AALSKGKKFD KSGSVLTSP
//
ID   WNK3_MOUSE              Reviewed;        1789 AA.
AC   Q80XP9;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Serine/threonine-protein kinase WNK3;
DE            EC=2.7.11.1;
DE   AltName: Full=Protein kinase lysine-deficient 3;
DE   AltName: Full=Protein kinase with no lysine 3;
GN   Name=Wnk3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1328-1789.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activation requires autophosphorylation of Ser-
CC       307. Phosphorylation of Ser-303 also promotes increased activity
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. WNK subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- CAUTION: Cys-175 is present instead of the conserved Lys which is
CC       expected to be an active site residue. Lys-158 appears to fulfill
CC       the required catalytic function.
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DR   EMBL; AL732420; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL807396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC043119; AAH43119.1; -; mRNA.
DR   EMBL; BC060731; AAH60731.1; -; mRNA.
DR   IPI; IPI00750069; -.
DR   UniGene; Mm.441474; -.
DR   ProteinModelPortal; Q80XP9; -.
DR   SMR; Q80XP9; 135-406.
DR   STRING; Q80XP9; -.
DR   PhosphoSite; Q80XP9; -.
DR   PRIDE; Q80XP9; -.
DR   UCSC; uc009upa.1; mouse.
DR   MGI; MGI:2652875; Wnk3.
DR   eggNOG; roNOG07073; -.
DR   HOGENOM; HBG716131; -.
DR   HOVERGEN; HBG050346; -.
DR   InParanoid; Q80XP9; -.
DR   OrthoDB; EOG4894KK; -.
DR   BRENDA; 2.7.11.1; 244.
DR   ArrayExpress; Q80XP9; -.
DR   CleanEx; MM_WNK3; -.
DR   Genevestigator; Q80XP9; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1   1789       Serine/threonine-protein kinase WNK3.
FT                                /FTId=PRO_0000278775.
FT   DOMAIN      146    404       Protein kinase.
FT   NP_BIND     152    160       ATP (By similarity).
FT   ACT_SITE    274    274       Proton acceptor (By similarity).
FT   BINDING     158    158       ATP (By similarity).
FT   MOD_RES     303    303       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     307    307       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     732    732       Phosphoserine (By similarity).
FT   CONFLICT   1613   1613       N -> D (in Ref. 2; AAH60731/AAH43119).
SQ   SEQUENCE   1789 AA;  197545 MW;  106310503A7DBC66 CRC64;
     MATDSGEPAS TEDSEKPDGV SFENRAARAV APLTVEARIK EKYSTFSASG ENIERKRFFR
     KSVEMTEDDK VAESSRRDER KAATNISRVD KVPTNVLRGG QEVKYEQCSK ATSESSKDCF
     KEKTEKEMEE EAEMKAVATS PSGRFLKFDI ELGRGAFKTV YKGLDTETWV EVAWCELQDR
     KLTKAEQQRF KEEAEMLKGL QHPNIVRFYD SWESTLKGKK CIVLVTELMT SGTLKTYLKR
     FKVMKPKVLR SWCRQILKGL QFLHTRTPPI IHRDLKCDNI FITGPTGSVK IGDLGLATLM
     RTSFAKSVIG TPEFMAPEMY EEHYDESVDV YAFGMCMLEM ATSEYPYSEC QNAAQIYRKV
     TSGIKPASFN KVTDPEVKEI IEGCIRQNKS ERLSIKDLLN HAFFAEDTGL RVELAEEDDC
     SNSSLALRLW VEDPKKLKGK HKDNEAIEFS FNLEADTPEE VAYEMVKSGF FHESDSKAVA
     KSIRDRVTLI KKIREKKPAG CLEERRDSQC KYVRNVLPQQ QTATLQPTPG PHTAAEYEET
     EVDQHVRQQF LQGKPQQQSS SVRGDTSSEP TAGPVLHSDT SSHPTVAYSS NQTTSSQVFS
     SILQAYISVP EQIHSSYQLL GYCQISGLQE QPKLTQSPVL PVVQGQSSVM PIYAAGVGVV
     SQSQISPLTI QKVSQIKPVS QPIGAEQQAT LQNPDFVRSL NQDVTSVKEN TNNPDTPSGN
     GKQDRNKQRR ASCPRPEKGT KFQLTVLQVS VSGDNMVECQ LETHNNKMVT FKFDVDGDAP
     EDIADYMVED NFVLENEKEK FVEELRAIVG QAQEILHVHS AVEKSIGVDS VALESNSNQT
     GSSEQVLINS ASTQTSNESA PQSSPVGRWR FCINQTIKNR EAQSPPSLQP SMAMVPGLHP
     FPSSRNTSNQ AISQNTVFTI ENNPGHRELF TSKLDHKDVV DGKIGEHASI ETEQSSISYQ
     VEDDRQIMTP ATDNSNYSAA LVCPVPGECE ALTSQAGMFM PTYPNQQAAV LADVHIAYPG
     ESVPIGGNAA LTSVLVSSDQ KPQSLSVQQP TIDAEFISKE GETTVNTETS SPKAVIATQT
     PGFEPAVILP ATILESDGER PPKMEFADNR IKTLDEKLRN LLYQEHSISS ICPESQKDTQ
     SIDSPFSSSA EDILSYSMPE VIAISHCGIQ DSPAQSPNFQ QTGSKILSNV AASQPAHISV
     FKKDLNVITS VPSELCLHEM SPDASLPGDP EAYPAAVSSD GTIHLQTGGG YFGLSFTCPS
     LKNPISRKSW TRKLKSWAYR LRQSTSFFKR SKVRQVETED KRSAIASDPI PLTREFSSDT
     RALSRCKAMS GSFQRGRFQV ITVPQQQPVK MMSFGKDHRP PFNKTTVQSS EQALTFAEAA
     VSQLIEVEPA MPTHKASVSS RKLRTLYETF KEDKGDPEQG DIVSYSTACE TSVSSVATEK
     NVTSTTEVSV QSGSEPLDKE KNESTPGKQT CTNEFSATLA GNRKSVTKTR PEGDQYLPLR
     EEQAYAQTQN SLFYSPSSPM SSDNESEIED EDLKVELQRL REKHIQEVVS LQTQQNKELQ
     ELYERLRATK DNKAQSSEVP LSPASPRRPR SFKSKLRSRP QSMTHSDNLV VKNALGVESN
     TVSCQQSPAS KKGMFTDDLH KLVDDWTRET VGHFPSKPSL NQLKQSQQKS EAENWNKSCE
     STPSTMGYTS NWISSLSQIR GAAPTSLPQG LPLPSFHGPL ASYGMPHVCQ YNAVGAAGYP
     VQWVGISGPA QQSVVLPTQS GGLFQPGMNL QSFPAPPVQN PASIPPGPK
//
ID   TBCD5_MOUSE             Reviewed;         815 AA.
AC   Q80XQ2;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   30-NOV-2010, entry version 48.
DE   RecName: Full=TBC1 domain family member 5;
GN   Name=Tbc1d5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546; SER-565 AND
RP   SER-568, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May act as a GTPase-activating protein for Rab family
CC       protein(s).
CC   -!- SIMILARITY: Contains 1 Rab-GAP TBC domain.
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DR   EMBL; BC043113; AAH43113.1; -; mRNA.
DR   IPI; IPI00119109; -.
DR   RefSeq; NP_082438.3; NM_028162.3.
DR   UniGene; Mm.120650; -.
DR   ProteinModelPortal; Q80XQ2; -.
DR   PhosphoSite; Q80XQ2; -.
DR   PRIDE; Q80XQ2; -.
DR   Ensembl; ENSMUST00000095246; ENSMUSP00000092875; ENSMUSG00000023923.
DR   GeneID; 72238; -.
DR   KEGG; mmu:72238; -.
DR   UCSC; uc008cyy.1; mouse.
DR   CTD; 72238; -.
DR   MGI; MGI:1919488; Tbc1d5.
DR   HOVERGEN; HBG062913; -.
DR   NextBio; 335783; -.
DR   ArrayExpress; Q80XQ2; -.
DR   Bgee; Q80XQ2; -.
DR   CleanEx; MM_TBC1D5; -.
DR   Genevestigator; Q80XQ2; -.
DR   GermOnline; ENSMUSG00000023923; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005097; F:Rab GTPase activator activity; IEA:InterPro.
DR   GO; GO:0032313; P:regulation of Rab GTPase activity; IEA:InterPro.
DR   InterPro; IPR000195; RabGAP/TBC_dom.
DR   Pfam; PF00566; TBC; 1.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; RabGAP_TBC; 2.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
PE   1: Evidence at protein level;
KW   GTPase activation; Phosphoprotein.
FT   CHAIN         1    815       TBC1 domain family member 5.
FT                                /FTId=PRO_0000208029.
FT   DOMAIN       81    359       Rab-GAP TBC.
FT   COMPBIAS    510    539       Gln-rich.
FT   MOD_RES      44     44       Phosphoserine (By similarity).
FT   MOD_RES      45     45       Phosphothreonine (By similarity).
FT   MOD_RES     546    546       Phosphoserine.
FT   MOD_RES     563    563       Phosphoserine (By similarity).
FT   MOD_RES     565    565       Phosphoserine.
FT   MOD_RES     568    568       Phosphoserine.
FT   MOD_RES     578    578       Phosphoserine (By similarity).
SQ   SEQUENCE   815 AA;  91853 MW;  2D06D23B362E3844 CRC64;
     MYKSVSETRH PLQSEEQEVG IDPLFSYSNK TRGDLSQNGR GSNSTLDTEG TFNSYMKEWE
     ELFVNNNYLA TVRQKGINGQ LRSSRFRSIC WKLFLCVLPQ DKSQWISKIK ELRAWYSSIK
     EIHITNPRKA AGQQDLMINN PLSQDEGSLW NKFFQDKELR SMIEQDVKRT FPEMQFFQQE
     NVRKILTDVL FCYARENEQL LYKQGMHELL APIIFTLHCD HQAFLHASES AQPSEEMKTL
     LNPEYLEHDA YAMFSQLMET AEPWFSTFEH DGQKGKETLM APIPFARPQD LGPTVAIVTK
     VNQIQDHLLK KHDIELYMHL NRLEIAPQIY GLRWVRLLFG REFPLQDLLV VWDALFADSL
     NLSLVDYVFT AMLLYIRDAL ISSNYQTCLG LLMHYPIIGD IHSLILKALF LRDPKRNPRP
     ATYQFHPNLD YYKARGADLM NKSRTNARGA PLNIHKVSNS LINFGRKLIS PASAPGSMGG
     PVPGNNSSSS FSAAIPTRTS TEAPRHHLLQ QQQQQQHQQQ QQQQPQQQQQ QHQQQQQQQR
     LMKSESMPVQ LNKGQSSKTI SSSPSIESLP GGREFTGSPP PSATKKDSFF SNIARSRSHS
     KTMGRKESEE ELEAQISFLQ GQLNDLDAMC KYCAKVMDMH LVNIQDVVLQ ENLEKEDQIL
     VSLAGLKQIK DILKGSLRFN QSQLEAGENE QITIADDHYC SSGQDQGSQV PRAAKQASSE
     MPGCTGGTTP DDFILVSKED EGHRARGAFS GQAQPLLTLR STSGKSRAPS CSPLLFSDPL
     MGPASASASS SNPSSSPDDD SSKESGFTIV SPLDI
//
ID   SMAG2_MOUSE             Reviewed;         687 AA.
AC   Q80XS6;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Protein Smaug homolog 2;
DE            Short=Smaug 2;
DE            Short=mSmaug2;
DE   AltName: Full=Sterile alpha motif domain-containing protein 4B;
GN   Name=Samd4b; Synonyms=Smaug2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the SMAUG family.
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
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DR   EMBL; BC042901; AAH42901.1; -; mRNA.
DR   IPI; IPI00330780; -.
DR   UniGene; Mm.54120; -.
DR   HSSP; Q23972; 1OXJ.
DR   ProteinModelPortal; Q80XS6; -.
DR   SMR; Q80XS6; 288-523.
DR   PhosphoSite; Q80XS6; -.
DR   PRIDE; Q80XS6; -.
DR   Ensembl; ENSMUST00000040531; ENSMUSP00000040486; ENSMUSG00000037513.
DR   UCSC; uc009fyw.1; mouse.
DR   MGI; MGI:2448542; Samd4b.
DR   eggNOG; roNOG08062; -.
DR   GeneTree; ENSGT00390000015877; -.
DR   InParanoid; Q80XS6; -.
DR   OrthoDB; EOG4H72B4; -.
DR   NextBio; 381478; -.
DR   ArrayExpress; Q80XS6; -.
DR   Bgee; Q80XS6; -.
DR   CleanEx; MM_SAMD4B; -.
DR   Genevestigator; Q80XS6; -.
DR   GermOnline; ENSMUSG00000037513; Mus musculus.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR015327; Smaug_PHAT.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Gene3D; G3DSA:1.25.40.170; Smaug_PHAT; 2.
DR   Pfam; PF00536; SAM_1; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Phosphoprotein.
FT   CHAIN         1    687       Protein Smaug homolog 2.
FT                                /FTId=PRO_0000260081.
FT   DOMAIN      299    372       SAM.
FT   MOD_RES     264    264       Phosphothreonine (By similarity).
FT   MOD_RES     271    271       Phosphoserine (By similarity).
FT   MOD_RES     400    400       Phosphothreonine (By similarity).
FT   MOD_RES     585    585       Phosphoserine (By similarity).
FT   MOD_RES     593    593       Phosphoserine (By similarity).
FT   MOD_RES     599    599       Phosphothreonine (By similarity).
SQ   SEQUENCE   687 AA;  75024 MW;  EBB38E58E2535CB6 CRC64;
     MMFRDQVGIL ASWFKGWNEC EQTVALLSLL KRVTRTQARF LQLCLEHSLA DCNDIHLLES
     EANSAAIVSQ WQQESKEKVV SLLLSHLPLL QPGNTEAKSE YMRLLQKVLA YSIESNAFIE
     ESRQLLSYAL IHPATTLEDR NALALWLSHL EERLASGFRT RPEPSYHSRQ GSDEWGGPAE
     LAPGEAGPGW QDKPPRENGH VPFHPSSSVP PAINSIGSNA NTGLPCQIHP SPLKRSMSLI
     PTSPQAPGEW PSPEELGARA AFTTPDHAPL SPQSSVASSG SEQTEEQGSS RNTFQEDGSG
     MKDVPSWLKS LRLHKYAALF SQMSYEEMMT LTEQHLESQN VTKGARHKIA LSIQKLRERQ
     SVLKSLEKDV LEGGNLWNAL QELQQIIITP IKAYSVLQAT PTAKDEGRGE PLLPGAEPPL
     THPGSDKGTE AKDPPAAENY PPPPAPAPSD SSEPAPAPVA DGDIPSQFTR VMGKVCTQLL
     VSRPDEENIT SYLQLIEKCL THEAFTETQK KRLLSWKQQV LKLLRTFPRK AALDMQSYRQ
     QKGWAFGSNS LPIAGSVGMG VARRTQRQFP MPPRALPPGR MGLLSPSGIG GVSPRHALTS
     PSLGGQGRQN LWFANPGGSN SMPSQSRSSV QRTHSLPVHS SPQAILMFPP DCPVPGPDLE
     INPTLESLCL SMTEHALGDG TDKTSTI
//
ID   NUCKS_MOUSE             Reviewed;         234 AA.
AC   Q80XU3; Q8BVD8;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Nuclear ubiquitous casein and cyclin-dependent kinases substrate;
DE   AltName: Full=JC7;
GN   Name=Nucks1; Synonyms=Nucks;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yoshitaka T.;
RT   "A search for cell proliferation related new genes.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; THR-179 AND SER-181,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-113, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-58; SER-61 AND
RP   SER-214, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-61, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-58; SER-61;
RP   THR-179; SER-181 AND SER-214, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-58; SER-61;
RP   SER-130; SER-132 AND SER-214, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-58; SER-61;
RP   SER-75; SER-79; SER-113; SER-130; SER-132; THR-179; SER-181; THR-202;
RP   SER-204; SER-214; SER-220; SER-225; SER-230 AND SER-231, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-181, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- PTM: Phosphorylated by CDK1 and casein kinase. Phosphorylated upon
CC       DNA damage, probably by ATM or ATR (By similarity).
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DR   EMBL; AB049825; BAC06821.1; -; mRNA.
DR   EMBL; AK078816; BAC37408.1; -; mRNA.
DR   EMBL; BC039951; AAH39951.1; -; mRNA.
DR   IPI; IPI00341869; -.
DR   RefSeq; NP_001139276.1; NM_001145804.1.
DR   RefSeq; NP_780503.2; NM_175294.3.
DR   UniGene; Mm.246869; -.
DR   STRING; Q80XU3; -.
DR   PhosphoSite; Q80XU3; -.
DR   PRIDE; Q80XU3; -.
DR   Ensembl; ENSMUST00000062264; ENSMUSP00000062576; ENSMUSG00000026434.
DR   GeneID; 98415; -.
DR   KEGG; mmu:98415; -.
DR   NMPDR; fig|10090.3.peg.1034; -.
DR   UCSC; uc007cnx.1; mouse.
DR   CTD; 98415; -.
DR   MGI; MGI:1934811; Nucks1.
DR   eggNOG; roNOG17630; -.
DR   GeneTree; ENSGT00530000063784; -.
DR   HOGENOM; HBG717419; -.
DR   HOVERGEN; HBG052687; -.
DR   InParanoid; Q80XU3; -.
DR   OMA; EKPAARG; -.
DR   OrthoDB; EOG4C2HC7; -.
DR   NextBio; 353468; -.
DR   ArrayExpress; Q80XU3; -.
DR   Bgee; Q80XU3; -.
DR   Genevestigator; Q80XU3; -.
DR   GermOnline; ENSMUSG00000026434; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein.
FT   CHAIN         1    234       Nuclear ubiquitous casein and cyclin-
FT                                dependent kinases substrate.
FT                                /FTId=PRO_0000057979.
FT   COMPBIAS    140    145       Poly-Asp.
FT   COMPBIAS    150    206       Lys-rich.
FT   MOD_RES      14     14       Phosphoserine.
FT   MOD_RES      19     19       Phosphoserine.
FT   MOD_RES      26     26       Phosphotyrosine (By similarity).
FT   MOD_RES      54     54       Phosphoserine (By similarity).
FT   MOD_RES      58     58       Phosphoserine.
FT   MOD_RES      61     61       Phosphoserine.
FT   MOD_RES      73     73       Phosphoserine (By similarity).
FT   MOD_RES      75     75       Phosphoserine.
FT   MOD_RES      79     79       Phosphoserine.
FT   MOD_RES      97     97       Phosphoserine (By similarity).
FT   MOD_RES     101    101       Phosphoserine (By similarity).
FT   MOD_RES     113    113       Phosphoserine.
FT   MOD_RES     130    130       Phosphoserine.
FT   MOD_RES     132    132       Phosphoserine.
FT   MOD_RES     144    144       Phosphoserine (By similarity).
FT   MOD_RES     149    149       Phosphoserine (By similarity).
FT   MOD_RES     177    177       Phosphothreonine (By similarity).
FT   MOD_RES     179    179       Phosphothreonine.
FT   MOD_RES     181    181       Phosphoserine.
FT   MOD_RES     202    202       Phosphothreonine.
FT   MOD_RES     204    204       Phosphoserine.
FT   MOD_RES     214    214       Phosphoserine.
FT   MOD_RES     220    220       Phosphoserine.
FT   MOD_RES     225    225       Phosphoserine.
FT   MOD_RES     230    230       Phosphoserine.
FT   MOD_RES     231    231       Phosphoserine.
FT   CONFLICT    128    129       KD -> N (in Ref. 2; BAC37408).
FT   CONFLICT    154    154       K -> Q (in Ref. 2; BAC37408).
FT   CONFLICT    161    161       K -> Q (in Ref. 2; BAC37408).
FT   CONFLICT    168    168       K -> E (in Ref. 2; BAC37408).
FT   CONFLICT    171    171       K -> Q (in Ref. 2; BAC37408).
FT   CONFLICT    174    174       L -> V (in Ref. 2; BAC37408).
FT   CONFLICT    186    186       K -> Q (in Ref. 2; BAC37408).
FT   CONFLICT    206    206       K -> Q (in Ref. 2; BAC37408).
SQ   SEQUENCE   234 AA;  26313 MW;  CB2075863AA0E87A CRC64;
     MSRPVRNRKV VDYSQFQESD DADEDYGRDS GPPAKKIRSS PREAKNKRRS GKNSQEDSED
     SEEKDVKTKK DDSHSAEDSE DEKDDHKNVR QQRQAASKAA SKQREMLLED VGSEEEPEED
     DEAPFQEKDS GSDEDFLMED DDDSDYGSSK KKNKKMVKKS KPERKEKKMP KPRLKATVTP
     SPVKGKAKVG RPTASKKSKE KTPSPKEEDE EAESPPEKKS GDEGSEDEAS SGED
//
ID   LRFN4_MOUSE             Reviewed;         636 AA.
AC   Q80XU8; Q3TQG8; Q460G5; Q8K3C4;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Leucine-rich repeat and fibronectin type-III domain-containing protein 4;
DE   Flags: Precursor;
GN   Name=Lrfn4; Synonyms=Salm3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   PubMed=16495444; DOI=10.1523/JNEUROSCI.3799-05.2006;
RA   Wang C.Y., Chang K., Petralia R.S., Wang Y.X., Seabold G.K.,
RA   Wenthold R.J.;
RT   "A novel family of adhesion-like molecules that interacts with the
RT   NMDA receptor.";
RL   J. Neurosci. 26:2174-2183(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, INTERACTION WITH DLG4, DEVELOPMENTAL STAGE, TISSUE
RP   SPECIFICITY, GLYCOSYLATION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=16828986; DOI=10.1016/j.gene.2006.05.014;
RA   Morimura N., Inoue T., Katayama K., Aruga J.;
RT   "Comparative analysis of structure, expression and PSD95-binding
RT   capacity of Lrfn, a novel family of neuronal transmembrane proteins.";
RL   Gene 380:72-83(2006).
RN   [5]
RP   INTERACTION WITH LRFN1; LRFN2; LRFN3 AND LRFN5, SUBCELLULAR LOCATION,
RP   AND TOPOLOGY.
RX   PubMed=18227064; DOI=10.1074/jbc.M709456200;
RA   Seabold G.K., Wang P.Y., Chang K., Wang C.Y., Wang Y.X.,
RA   Petralia R.S., Wenthold R.J.;
RT   "The SALM family of adhesion-like molecules forms heteromeric and
RT   homomeric complexes.";
RL   J. Biol. Chem. 283:8395-8405(2008).
RN   [6]
RP   FUNCTION.
RX   PubMed=18585462; DOI=10.1016/j.mcn.2008.05.019;
RA   Wang P.Y., Seabold G.K., Wenthold R.J.;
RT   "Synaptic adhesion-like molecules (SALMs) promote neurite outgrowth.";
RL   Mol. Cell. Neurosci. 39:83-94(2008).
CC   -!- FUNCTION: Promotes neurite outgrowth in hippocampal neurons. May
CC       play a role in redistributing DLG4 to the cell periphery.
CC   -!- SUBUNIT: Can form heteromeric complexes with LRFN1, LRFN2, LRFN3
CC       and LRFN5. Unable to form homophilic interactions across cell
CC       junctions. Interacts with DLG1, DLG2 and DLG3 (By similarity).
CC       Also interacts with DLG4.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Expressed in brain and testis. In the brain,
CC       weak, but broad expression in the cerebral cortex and diencephalic
CC       nuclei. Also detected in other parts of the central nervous
CC       system, including the olfactory bulb, pons, cerebellum, and
CC       medulla oblongata, as well as in the peripheral nervous system,
CC       such as the ganglia of cranial nerves and the dorsal root ganglion
CC       during gestation.
CC   -!- DEVELOPMENTAL STAGE: Low expression from 4.5 dpc onwards.
CC       Expression increases at 10.5 dpc and decreases after 15.5 dpc. At
CC       11.5 dpc, broadly expressed in the telencephalic and diencephalic
CC       vesicles. This pattern of expression continues until 17.5 dpc.
CC   -!- DOMAIN: The PDZ-binding motif is required for neurite outgrowth
CC       promotion. This motif is also involved in DLG1-, DLG3- and DLG4-
CC       binding (By similarity).
CC   -!- PTM: Glycosylated.
CC   -!- SIMILARITY: Belongs to the LRFN family.
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC   -!- SIMILARITY: Contains 1 Ig-like (immunoglobulin-like) domain.
CC   -!- SIMILARITY: Contains 7 LRR (leucine-rich) repeats.
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DR   EMBL; DQ078786; AAZ23615.1; -; mRNA.
DR   EMBL; AK081560; BAC38259.1; -; mRNA.
DR   EMBL; AK163603; BAE37415.1; -; mRNA.
DR   EMBL; BC023036; AAH23036.1; -; mRNA.
DR   EMBL; BC023156; AAH23156.1; -; mRNA.
DR   IPI; IPI00330802; -.
DR   RefSeq; NP_700437.2; NM_153388.4.
DR   UniGene; Mm.329675; -.
DR   ProteinModelPortal; Q80XU8; -.
DR   SMR; Q80XU8; 15-373, 402-483.
DR   PhosphoSite; Q80XU8; -.
DR   PRIDE; Q80XU8; -.
DR   Ensembl; ENSMUST00000053597; ENSMUSP00000050039; ENSMUSG00000045045.
DR   Ensembl; ENSMUST00000113822; ENSMUSP00000109453; ENSMUSG00000045045.
DR   GeneID; 225875; -.
DR   KEGG; mmu:225875; -.
DR   UCSC; uc008gah.1; mouse.
DR   CTD; 225875; -.
DR   MGI; MGI:2385612; Lrfn4.
DR   eggNOG; roNOG15298; -.
DR   GeneTree; ENSGT00600000084152; -.
DR   HOGENOM; HBG444166; -.
DR   HOVERGEN; HBG052352; -.
DR   InParanoid; Q80XU8; -.
DR   OMA; PHGGNGS; -.
DR   OrthoDB; EOG4GTKCM; -.
DR   PhylomeDB; Q80XU8; -.
DR   NextBio; 377837; -.
DR   ArrayExpress; Q80XU8; -.
DR   Bgee; Q80XU8; -.
DR   Genevestigator; Q80XU8; -.
DR   GermOnline; ENSMUSG00000045045; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR000372; LRR-contain_N.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00560; LRR_1; 1.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00369; LRR_TYP; 2.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00013; LRRNT; 1.
DR   SUPFAM; SSF49265; FN_III-like; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Leucine-rich repeat; Membrane; Phosphoprotein; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     16       Potential.
FT   CHAIN        17    636       Leucine-rich repeat and fibronectin type-
FT                                III domain-containing protein 4.
FT                                /FTId=PRO_0000014844.
FT   TOPO_DOM     17    518       Extracellular (Potential).
FT   TRANSMEM    519    539       Helical; (Potential).
FT   TOPO_DOM    540    636       Cytoplasmic (Potential).
FT   REPEAT       46     70       LRR 1.
FT   REPEAT       71     94       LRR 2.
FT   REPEAT       95    118       LRR 3.
FT   REPEAT      120    142       LRR 4.
FT   REPEAT      144    167       LRR 5.
FT   REPEAT      168    191       LRR 6.
FT   REPEAT      193    216       LRR 7.
FT   DOMAIN      281    367       Ig-like.
FT   DOMAIN      407    492       Fibronectin type-III.
FT   MOTIF       633    636       PDZ-binding.
FT   MOD_RES     627    627       Phosphoserine (By similarity).
FT   CARBOHYD     25     25       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     70     70       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    324    324       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    333    333       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    376    376       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    440    440       N-linked (GlcNAc...) (Potential).
FT   DISULFID    302    351       By similarity.
FT   CONFLICT    503    503       T -> N (in Ref. 1; AAZ23615 and 3;
FT                                AAH23156).
SQ   SEQUENCE   636 AA;  67252 MW;  1EE86E96CB88BA91 CRC64;
     MAPPLLLLLL ASGAAACPLP CVCQNLSESL STLCAHRGLL FVPPNVDRRT VELRLADNFI
     QALGPPDFRN MTGLVDLTLS RNAITRIGAR SFGDLESLRS LHLDGNRLVE LGSSSLRGPV
     NLQHLILSGN QLGRIAPGAF DDFLDSLEDL DVSYNNLRQV PWAGIGSMPA LHTLNLDHNL
     IDALPPGVFA QLSQLSRLDL TSNRLATLAP DPLFSRGRDA EASPSPLVLS FSGNPLHCNC
     ELLWLRRLAR PDDLETCASP PTLAGRYFWA VPEGEFSCEP PLIARHTQRL WVLEGQRATL
     RCRALGDPVP TMHWVGPDDR LVGNSSRAWA FPNGTLEIGV TGAGDAGAYT CIATNPAGEA
     TARVELRVLA LPHGGNTSAE GGRPGPSDIA ASARTAAEGE GTLESEPAVQ VTEVTATSGL
     VSWGLGRPAD PVWMFQIQYN SSEDETLIYR IVPASSHHFL LKHLVPGADY DLCLLALSPA
     AGPSDLTATR LLGCAHFSTL PATPLCHALQ AHVLGGTLTV AVGGVLVAAL LVFTVALLVR
     GRGAGNGRLP LKLSHVQSQT NGGTSPMPKS HPPRSPPPRP QRSCSLDLGD TGGCYGYARR
     LGGAWARRSH SVHGGLLGAG CRGVGGSAER LEESVV
//
ID   L2GL1_MOUSE             Reviewed;        1036 AA.
AC   Q80Y17; Q61856; Q7TNV3; Q8BN92;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Lethal(2) giant larvae protein homolog 1;
DE            Short=LLGL;
DE   AltName: Full=Mgl-1;
DE   AltName: Full=Mlgl;
GN   Name=Llgl1; Synonyms=Llglh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR;
RX   MEDLINE=93368661; PubMed=8103190; DOI=10.1038/365069a0;
RA   Tomotsune D., Shoji H., Wakamatsu Y., Kondoh H., Takahashi N.;
RT   "A mouse homologue of the Drosophila tumour-suppressor gene l(2)gl
RT   controlled by Hox-C8 in vivo.";
RL   Nature 365:69-72(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye, and Osteoclast;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH PARD6A, AND PHOSPHORYLATION.
RX   PubMed=12629547; DOI=10.1038/ncb948;
RA   Plant P.J., Fawcett J.P., Lin D.C., Holdorf A.D., Binns K.,
RA   Kulkarni S., Pawson T.;
RT   "A polarity complex of mPar-6 and atypical PKC binds, phosphorylates
RT   and regulates mammalian Lgl.";
RL   Nat. Cell Biol. 5:301-308(2003).
RN   [6]
RP   INTERACTION WITH STX4A.
RX   PubMed=11809830; DOI=10.1091/mbc.01-10-0496;
RA   Musch A., Cohen D., Yeaman C., Nelson W.J., Rodriguez-Boulan E.,
RA   Brennwald P.J.;
RT   "Mammalian homolog of Drosophila tumor suppressor lethal (2) giant
RT   larvae interacts with basolateral exocytic machinery in Madin-Darby
RT   canine kidney cells.";
RL   Mol. Biol. Cell 13:158-168(2002).
RN   [7]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=15037549; DOI=10.1101/gad.1178004;
RA   Klezovitch O., Fernandez T.E., Tapscott S.J., Vasioukhin V.;
RT   "Loss of cell polarity causes severe brain dysplasia in Lgl1 knockout
RT   mice.";
RL   Genes Dev. 18:559-571(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-957, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-964, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Cortical cytoskeleton protein found in a complex
CC       involved in maintaining cell polarity and epithelial integrity.
CC       Involved in the regulation of mitotic spindle orientation,
CC       proliferation, differentiation and tissue organization of
CC       neuroepithelial cells.
CC   -!- SUBUNIT: Associated with nonmuscle myosin II heavy chain.
CC       Interacts with PRKCI/aPKC, PARD6B/Par-6 and PARD6A (By
CC       similarity). Interacts with STX4A.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Note=Localized to the lateral membrane during the polarization and
CC       formation cell-cell contacts (By similarity).
CC   -!- PTM: Phosphorylated by PRKCI on at least one of the following Ser
CC       residues: Ser 654, Ser-658, Ser-662, Ser-669 and Ser-672.
CC       Phosphorylation is important for appropriated cell polarization.
CC       Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- DISRUPTION PHENOTYPE: Mice exhibit disorganization and disruption
CC       of the apical junctional complex, resulting in hyper-proliferation
CC       of neuroblasts and brain dysplasia. Loss of Lgl1 in mice results
CC       in formation of neuroepithelial rosette-like structures, similar
CC       to the neuroblastic rosettes in human primitive neuroectodermal
CC       tumors. The newborn Lgl1(-/-) pups develop severe hydrocephalus
CC       and die neonatally. Due to the loss of mitotic spindle
CC       orientation, a large proportion of Lgl1(-/-) neural progenitor
CC       cells fails to exit the cell cycle and differentiate, and,
CC       instead, continues to proliferate and dies by apoptosis. Dividing
CC       Lgl1(-/-) cells are unable to asymmetrically localize the Notch
CC       inhibitor Numb, and the resulting failure of asymmetric cell
CC       divisions may be responsible for the hyperproliferation and the
CC       lack of differentiation.
CC   -!- SIMILARITY: Belongs to the WD repeat L(2)GL family.
CC   -!- SIMILARITY: Contains 14 WD repeats.
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DR   EMBL; D16141; BAA03712.1; -; mRNA.
DR   EMBL; AK084386; BAC39171.1; -; mRNA.
DR   EMBL; AK159412; BAE35062.1; -; mRNA.
DR   EMBL; AL596215; CAI35271.1; -; Genomic_DNA.
DR   EMBL; AL596215; CAI35272.1; -; Genomic_DNA.
DR   EMBL; BC050913; AAH50913.1; -; mRNA.
DR   EMBL; BC055399; AAH55399.1; -; mRNA.
DR   IPI; IPI00649658; -.
DR   PIR; S36758; S36758.
DR   RefSeq; NP_001152876.1; NM_001159404.1.
DR   RefSeq; NP_001152877.1; NM_001159405.1.
DR   RefSeq; NP_032528.1; NM_008502.2.
DR   UniGene; Mm.285453; -.
DR   ProteinModelPortal; Q80Y17; -.
DR   SMR; Q80Y17; 190-270, 438-463, 516-542, 596-628.
DR   STRING; Q80Y17; -.
DR   PRIDE; Q80Y17; -.
DR   Ensembl; ENSMUST00000052346; ENSMUSP00000060749; ENSMUSG00000020536.
DR   Ensembl; ENSMUST00000108719; ENSMUSP00000104359; ENSMUSG00000020536.
DR   GeneID; 16897; -.
DR   KEGG; mmu:16897; -.
DR   UCSC; uc007jge.1; mouse.
DR   CTD; 16897; -.
DR   MGI; MGI:102682; Llgl1.
DR   eggNOG; roNOG13808; -.
DR   HOGENOM; HBG402819; -.
DR   HOVERGEN; HBG052711; -.
DR   InParanoid; Q80Y17; -.
DR   OrthoDB; EOG4SJ5D2; -.
DR   PhylomeDB; Q80Y17; -.
DR   NextBio; 290922; -.
DR   ArrayExpress; Q80Y17; -.
DR   Bgee; Q80Y17; -.
DR   CleanEx; MM_LLGL1; -.
DR   Genevestigator; Q80Y17; -.
DR   GermOnline; ENSMUSG00000020536; Mus musculus.
DR   GO; GO:0007420; P:brain development; TAS:UniProtKB.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0035090; P:maintenance of apical/basal cell polarity; IMP:MGI.
DR   InterPro; IPR000664; Lethal2_giant.
DR   InterPro; IPR013577; LLGL2.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
DR   Pfam; PF08366; LLGL; 1.
DR   Pfam; PF00400; WD40; 1.
DR   PRINTS; PR00962; LETHAL2GIANT.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Exocytosis; Phosphoprotein; Repeat;
KW   WD repeat.
FT   CHAIN         1   1036       Lethal(2) giant larvae protein homolog 1.
FT                                /FTId=PRO_0000232726.
FT   REPEAT       38     71       WD 1.
FT   REPEAT       78    119       WD 2.
FT   REPEAT      139    175       WD 3.
FT   REPEAT      199    233       WD 4.
FT   REPEAT      239    271       WD 5.
FT   REPEAT      289    331       WD 6.
FT   REPEAT      339    373       WD 7.
FT   REPEAT      395    473       WD 8.
FT   REPEAT      517    592       WD 9.
FT   REPEAT      601    662       WD 10.
FT   REPEAT      722    782       WD 11.
FT   REPEAT      791    843       WD 12.
FT   REPEAT      848    901       WD 13.
FT   REPEAT      915    938       WD 14.
FT   MOD_RES     508    508       Phosphotyrosine (By similarity).
FT   MOD_RES     662    662       Phosphoserine (By similarity).
FT   MOD_RES     703    703       Phosphothreonine (By similarity).
FT   MOD_RES     957    957       Phosphothreonine.
FT   MOD_RES     964    964       Phosphoserine.
FT   CONFLICT    321    321       C -> F (in Ref. 2; BAC39171).
FT   CONFLICT    684    685       Missing (in Ref. 1; BAA03712).
FT   CONFLICT   1036   1036       G -> GSPEDSEKNLRNLEADDACRAYTLLIK (in Ref.
FT                                4; AAH55399).
SQ   SEQUENCE   1036 AA;  112618 MW;  715EFC11A45CD001 CRC64;
     MMKFRFRRQG ADPQREKLKQ ELFAFHKTVE HGFPNQPSAL AFDPELRIMA IGTRSGAVKI
     YGAPGVEFTG LHRDAATVTQ MHFLPGQGRL LTLLDDSSLH LWEIIHHNGC AHLEEGLSFH
     PPSRPSFDNA SFPASLTRVT VVLLVAGNTA ALGTESGSIF FLDVATLALL EGQTLSPDVV
     LRSVPDDYRC GKALGPVESL QGHLQDPSKI LIGYSRGLLV IWSQATQSVD NVFLGNQQLE
     SLCWGRDGSS IISSHSDGSY AIWSTDTGSP PTLQPTVVTT PYGPFPCKAI NKILWRSCES
     GDHFIIFSGG MPRASYGDRH CVSVLRAETL VTLDFTSRVI DFFTVHSTQP EDECDNPQAL
     AVLLEEELVV LDLQTPGWPA VPAPYLAPLH SSAITCSAHV ANVPSKLWAR IVSAGEQQSP
     QPASSALSWP ITGGRNLAQE PSQRGLLLTG HEDGTVRFWD ASGVALRPLY KLSTAGLFQT
     DCEHADSLAQ AVEDDWPPFR KVGCFDPYSD DPRLGIQKVA LCKYTAQMVV AGTAGQVLVL
     ELSEVPAEHA VSVANVDLLQ DREGFTWKGH ERLNPHTGLL PWPAGFQPRM LIQCLPPAAV
     TAVTLHAEWS LVAFGTSHGF GLFDYQRKSP VLARCTLHPN DSLAMEGPLS RVKSLKKSLR
     QSFRRIRKSR VSGKKRTPAA SSKLQEANAQ LAEQTCPHDL EMTPVQRRIE PRSADDSLSG
     VVRCLYFADT FLRDATHHGP TMWAGTNSGS VFAYALEVPA ATAGGEKRPE QAVEAVLGKE
     VQLMHRAPVV AIAVLDGRGR PLPEPYEASR DLAQAPDMQG GHAVLIASEE QFKVFTLPKV
     SAKTKFKLTA HEGCRVRKVA LATFASVMSE DYAETCLACL TNLGDVHVFS VPGLRPQVHY
     SCIRKEDISG IASCVFTRHG QGFYLISPSE FERFSLSARN ITEPLCSLDI SWPQNATQPR
     LQESPKLSQA NGTRDIILAP ESCEGSPSSA HSKRADTMEP PEAALSPVSI DSAASGDTML
     DTTGDVTVEY VKDFLG
//
ID   PRIC2_MOUSE             Reviewed;         845 AA.
AC   Q80Y24;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Prickle-like protein 2;
DE   Flags: Precursor;
GN   Name=Prickle2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   IDENTIFICATION, AND CHARACTERIZATION.
RX   PubMed=12525887;
RA   Katoh M., Katoh M.;
RT   "Identification and characterization of human PRICKLE1 and PRICKLE2
RT   genes as well as mouse Prickle1 and Prickle2 genes homologous to
RT   Drosophila tissue polarity gene prickle.";
RL   Int. J. Mol. Med. 11:249-256(2003).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-696, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND SER-732, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696 AND SER-807, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane (Potential).
CC   -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC   -!- SIMILARITY: Contains 3 LIM zinc-binding domains.
CC   -!- SIMILARITY: Contains 1 PET domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH50793.1; Type=Erroneous initiation;
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DR   EMBL; BC050793; AAH50793.1; ALT_INIT; mRNA.
DR   IPI; IPI00349970; -.
DR   RefSeq; NP_001127933.1; NM_001134461.1.
DR   UniGene; Mm.248820; -.
DR   ProteinModelPortal; Q80Y24; -.
DR   SMR; Q80Y24; 126-312.
DR   STRING; Q80Y24; -.
DR   PhosphoSite; Q80Y24; -.
DR   PRIDE; Q80Y24; -.
DR   Ensembl; ENSMUST00000032093; ENSMUSP00000032093; ENSMUSG00000030020.
DR   Ensembl; ENSMUST00000113445; ENSMUSP00000109072; ENSMUSG00000030020.
DR   Ensembl; ENSMUST00000113446; ENSMUSP00000109073; ENSMUSG00000030020.
DR   Ensembl; ENSMUST00000113447; ENSMUSP00000109074; ENSMUSG00000030020.
DR   GeneID; 243548; -.
DR   KEGG; mmu:243548; -.
DR   UCSC; uc009cyx.1; mouse.
DR   CTD; 243548; -.
DR   MGI; MGI:1925144; Prickle2.
DR   eggNOG; roNOG05204; -.
DR   GeneTree; ENSGT00550000074438; -.
DR   HOVERGEN; HBG053679; -.
DR   InParanoid; Q80Y24; -.
DR   OrthoDB; EOG45MN4W; -.
DR   ArrayExpress; Q80Y24; -.
DR   Bgee; Q80Y24; -.
DR   CleanEx; MM_PRICKLE2; -.
DR   Genevestigator; Q80Y24; -.
DR   GO; GO:0016327; C:apicolateral plasma membrane; IDA:MGI.
DR   GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IDA:MGI.
DR   GO; GO:0031175; P:neuron projection development; IMP:MGI.
DR   InterPro; IPR010442; PET_domain.
DR   InterPro; IPR001781; Znf_LIM.
DR   Gene3D; G3DSA:2.10.110.10; Znf_LIM; 3.
DR   Pfam; PF00412; LIM; 3.
DR   Pfam; PF06297; PET; 1.
DR   SMART; SM00132; LIM; 3.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR   PROSITE; PS51303; PET; 1.
PE   1: Evidence at protein level;
KW   LIM domain; Lipoprotein; Membrane; Metal-binding; Methylation;
KW   Nucleus; Phosphoprotein; Prenylation; Repeat; Zinc.
FT   CHAIN         1    842       Prickle-like protein 2.
FT                                /FTId=PRO_0000075892.
FT   PROPEP      843    845       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000396719.
FT   DOMAIN       18    126       PET.
FT   DOMAIN      128    193       LIM zinc-binding 1.
FT   DOMAIN      193    253       LIM zinc-binding 2.
FT   DOMAIN      253    317       LIM zinc-binding 3.
FT   COMPBIAS    504    511       Poly-Glu.
FT   COMPBIAS    669    731       Arg-rich.
FT   COMPBIAS    780    785       Poly-Ser.
FT   MOD_RES      92     92       Phosphoserine.
FT   MOD_RES     544    544       Phosphoserine.
FT   MOD_RES     696    696       Phosphoserine.
FT   MOD_RES     732    732       Phosphoserine.
FT   MOD_RES     807    807       Phosphoserine.
FT   MOD_RES     842    842       Cysteine methyl ester (By similarity).
FT   LIPID       842    842       S-farnesyl cysteine (By similarity).
SQ   SEQUENCE   845 AA;  95839 MW;  F182D8597A5EDCC2 CRC64;
     MVTVMPLEME KTISKLMFDF QRSSTSDDDS GCALEEYAWV PPGLKPEQVH QYYSCLPEEK
     VPYVNSAGEK LRIKQLLHQL PPHDNEVRYC NSLDEEEKRE LKLFSNQRKR ENLGRGNVRP
     FPVTMTGAIC EQCGGQIKGG DIAVFASRAG HGICWHPPCF VCTVCNELLV DLIYFYQDGK
     IYCGRHHAEC LKPRCAACDE IIFADECTEA EGRHWHMRHF CCFECETVLG GQRYIMKEGR
     PYCCHCFESL YAEYCDTCAQ HIGIDQGQMT YDDQHWHATE TCFCCAHCKK SLLGRPFLPK
     QGQIFCSRAC SAGEDPNGSD SSDSAFQNAR AKESRRSAKI GKNKGKTEEA MLNQHSQLQV
     SSNRLSADVD PLSVQMDLLS LSSQTPSLNR DPIWRSREEP FHYGNKMEQN QSQSPLQLLS
     QCNIRTSYSP GGQGAGAQPD MWAKHFSNPK RSSSMALKGH GGSFIQECRE DYYPGRLMSQ
     ESYSDMSSQS FNETRGSIPV PKYEEEEEEE EGGISTQQCR PRRPLSSLKY TEDMTPTEQT
     PRGSMESLAL SNATGLSAEG GAKRQEHLSR FSMPDLSKDS GMNVSEKLSN MGTLNSSMQF
     RSAESVRSLL SAQQYQEMEG NLHQLSNPLG YRDLQSHGRM HQSFDFDGGI ASSKLPGQEG
     VHIQPMSERT RRRTTSRDDN RRFRPHRSRR SRRSRSDNAL HLASEREVIA RLKERPPLRA
     REDYDQFMRQ RSFQESLGQG SRRDLYSQCP RTVSDLALQN AFGERWGPYF TEYDWCSTCS
     SSSESDNEGY FLGEPIPQPA RLRYVTSDEL LHKYSSYGVP KSSTLGGRGQ LHSRKRQKSK
     NCIIS
//
ID   Q80Y35_MOUSE            Unreviewed;      2094 AA.
AC   Q80Y35;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   30-NOV-2010, entry version 49.
DE   SubName: Full=Nuclear mitotic apparatus protein 1;
GN   Name=Numa1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
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DR   EMBL; BC049791; AAH49791.1; -; mRNA.
DR   IPI; IPI00263048; -.
DR   RefSeq; NP_598708.3; NM_133947.3.
DR   UniGene; Mm.27259; -.
DR   ProteinModelPortal; Q80Y35; -.
DR   STRING; Q80Y35; -.
DR   PhosphoSite; Q80Y35; -.
DR   PRIDE; Q80Y35; -.
DR   Ensembl; ENSMUST00000084852; ENSMUSP00000081912; ENSMUSG00000066306.
DR   GeneID; 101706; -.
DR   KEGG; mmu:101706; -.
DR   UCSC; uc009iqb.1; mouse.
DR   CTD; 101706; -.
DR   MGI; MGI:2443665; Numa1.
DR   HOGENOM; HBG283277; -.
DR   HOVERGEN; HBG052694; -.
DR   InParanoid; Q80Y35; -.
DR   NextBio; 355078; -.
DR   ArrayExpress; Q80Y35; -.
DR   Bgee; Q80Y35; -.
DR   Genevestigator; Q80Y35; -.
PE   1: Evidence at protein level;
SQ   SEQUENCE   2094 AA;  235658 MW;  CBE2E38B6BC4A0E5 CRC64;
     MTLHATRAAT LLSWVNSLHV ADPVETVLQL QDCSIFIKII NTIHDTKEGQ QILQQPLPER
     LDFVCSFLQK NRKHPSSTQC LVSVQKVIEG SEMELAKMIM LFLYQSTMSS RNLRDWEQFE
     YGVQAELAVI LKFMLDHEES LNLTEDLESF LEKVPYTHAS TLSEELSPPS HQTKRKIRFL
     EIQRIASSSS ENNFLSGSPS SPMGDILQTP QFQMRRLKKQ LADERSNRDD LELELSESLK
     LLTEKDAQIA MMQQRIDHLA LLNEKQAASS QEPSELEELR GKNESLTVRL HETLKQCQNL
     KTEKSQMDRK ISQLSEENGD LSFKVREFAN HLQQLQGAFN DLIEEHSKAS QEWAEKQARL
     ENELSTALQD KKCLEEKNEI LQGKLSQLED QATRLQESPA PEKGEVLGDA LQLDTLKQEA
     AKLATDNTQL QTRVETLECE RGKQEAQLLA ERSRFEDEKQ QLASLIADLQ SSVSNLSQAK
     EELEQASQAQ GAQLTAQLTS MTGLNATLQQ RDQELASLKE QAKKEQAQML QTMQEQEQVA
     QGLRQQVEQL SSSLKLKEQQ LEEAAKEQEA TRQDHAQQLA IVAEAREASL RERDTARQQL
     ETVEKEKDAK LESLQQQLQA ANDARDNAQT SVTQAQQEKA ELSQKIGELH ACIEASHQEQ
     RQVQARVTEL EAQLKAEQQK TTEREKVVQE KAQLQEQLRA LEESLKITKG SLEEEKRRAA
     DALKEQQCRA TEMEAESRSL MEQREREQKE LEQEKAGRKG LEARIQQLEE AHQAETEALR
     HELAEATASQ HRAESECERL IREVESRQKR FEARQQEEAR YGAMFQEQLM ALKGEKTGQE
     VQEEAVEIHS EGQPGQQQSQ LAQLHASLAK AIQQVQEKEV RAQKLVDDLS ALQEKMAATN
     KEVACLKTLV LKAGEQQETA SLELLKEPPR AANRASDQLG EQQGRPFSST HAAVKAMERE
     AEQMGGELER LRAALIKSQG QQQEERGQQE REVARLTQER GQAQADLAQE KAAKAELEMR
     LQNTLNEQRV EFAALQEALA HALTEKEGTD QELAKLRGQE AAQRTELKEL QQTLEQLKIQ
     LVKKEKEHPA GGASGEDASG PGTQSETAGK TDAPGPELQA LRAEISKLEQ QCQQQQQQVE
     GLTHSLKSER ACRAEQDKAL ETLQGQLEEK ARELGHNQAA SASAQRELQA LRAKAQDHSK
     AEEEWKAQVA RGQQEAERKS SLISSLEEEV SILNRQVLEK EGESKELKRL VVAESEKSQK
     LEERLRLLQV ETASNSARAA ERSSALREEV QSLREEVEKQ RVVSENSRQE LASQAERAEE
     LGQELKAWQE KFFQKEQALS ALQLEHTSTQ ALVSELLPAK HLCQQLQAEQ AAAEKRFREE
     LEQSKQAAGG LQAELMRAQR ELGELGSLRQ KIVEQERAAQ QLRAEKASYA EQLSMLKKAH
     GLLAEENRGL GERANLGRQF LEVELDQARE KYVQELAAVR TDAETHLAEM RQEAQSTSRE
     LEVMTAKYEG AKVKVLEERQ RFQEERQKLT AQVEELSKKL TEHDQASKVQ QQKLKAFQAQ
     RGESQQEVQR LQTQLNELQA QLSQKEQAAE HYKLQMEKAK THYDAKKQQN QKLQEQLQDL
     EELQKENKEL RSEAERLGRE LQQAGLKTKE AEQTCRHLTA QVRSLEAQVA HADQQLRDLG
     KFQVATDALK SREPQVKPQL DLSIDSLDLS LEEGTPCSVA SKLPRTQPDG TSVPGEPASP
     ISQRLPPKVE SLESLYFTPT PARGQAPLET SLDSLGDAFP DSGRKTRSAR RRTTQIINIT
     MTKKLELEEP DSANSSFYST QSAPASQANL RATSSTQSLA RLGSPDDGNS ALLSLPGYRP
     TTRSSARRSQ ARMSSGAPQG RNSFYMGTCQ DEPEQLDDWN RIAELQQRNR VCPPHLKTCY
     PLESRPTLSL ATITDEEMKT GDPRETLRRA SMQPAQIAEG VGITTRQQRK RVSSETHQGP
     GTPESKKATS CFPRPMTPRD RHEGRKQSST ADTQKKAAPV LKQADRRQSM AFSILNTPKK
     LGNSLLRRGA SKKTPAKVSP NPRSGTRRSP RIATTTTGTA TVATTPRAKG KVKH
//
ID   BSDC1_MOUSE             Reviewed;         427 AA.
AC   Q80Y55; B2KGE2; Q8BI04; Q8VDP1;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=BSD domain-containing protein 1;
GN   Name=Bsdc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NOD;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- INTERACTION:
CC       Q9NW68:BSDC1 (xeno); NbExp=1; IntAct=EBI-2553836, EBI-721848;
CC   -!- SIMILARITY: Contains 1 BSD domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH21480.1; Type=Erroneous initiation;
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DR   EMBL; AK037201; BAC29751.1; -; mRNA.
DR   EMBL; AK144053; BAE25672.1; -; mRNA.
DR   EMBL; CU302431; CAQ51564.1; -; Genomic_DNA.
DR   EMBL; CH466552; EDL30194.1; -; Genomic_DNA.
DR   EMBL; BC021480; AAH21480.1; ALT_INIT; mRNA.
DR   EMBL; BC049111; AAH49111.1; -; mRNA.
DR   IPI; IPI00330806; -.
DR   RefSeq; NP_598650.2; NM_133889.2.
DR   UniGene; Mm.17918; -.
DR   ProteinModelPortal; Q80Y55; -.
DR   IntAct; Q80Y55; 1.
DR   PRIDE; Q80Y55; -.
DR   Ensembl; ENSMUST00000048162; ENSMUSP00000048742; ENSMUSG00000040859.
DR   GeneID; 100383; -.
DR   KEGG; mmu:100383; -.
DR   UCSC; uc008uxb.1; mouse.
DR   CTD; 100383; -.
DR   MGI; MGI:1913466; Bsdc1.
DR   eggNOG; roNOG08246; -.
DR   GeneTree; ENSGT00390000009361; -.
DR   HOGENOM; HBG713060; -.
DR   HOVERGEN; HBG106482; -.
DR   InParanoid; Q80Y55; -.
DR   OMA; RVFELNS; -.
DR   OrthoDB; EOG4RJG20; -.
DR   PhylomeDB; Q80Y55; -.
DR   NextBio; 354418; -.
DR   ArrayExpress; Q80Y55; -.
DR   Bgee; Q80Y55; -.
DR   CleanEx; MM_BSDC1; -.
DR   Genevestigator; Q80Y55; -.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   InterPro; IPR005607; BSD.
DR   Pfam; PF03909; BSD; 1.
DR   SMART; SM00751; BSD; 1.
DR   PROSITE; PS50858; BSD; 1.
PE   1: Evidence at protein level;
FT   CHAIN         1    427       BSD domain-containing protein 1.
FT                                /FTId=PRO_0000282640.
FT   DOMAIN      146    198       BSD.
FT   CONFLICT    338    338       G -> S (in Ref. 4; AAH21480).
FT   CONFLICT    413    413       D -> G (in Ref. 1; BAC29751).
SQ   SEQUENCE   427 AA;  46953 MW;  0261E1E9AFBB2BA1 CRC64;
     MAEGEDVGWW RSWLQQSYQA VKEKSTEALE FMKRDLTEFT QVVQHDTACT IAATASVVKE
     KLATEGSSGA TEKVKKGLSD FLGVISDTFA PSPDKTIDCD VITLMGTPSG TAEPYDGTKA
     RLYSLQSDPA TYCNEPDGPP ELFDAWLSEF CLEEKKGEIS ELLVGSPSIR ALYTKMVPAA
     VSHSEFWHRY FYKVHQLEQE QARRDALKQR ADQSISEEPG WEEEEEELEG IVPSPKEAKI
     PKETKTTTSP EDEPAPQSPC EETPVEPPAE ATPSESSESI SLVTQVANPA AAPEAPELPK
     DLSQKLFEAS LEEQSLAEDE GETGPPPPPP SKPLTPAGRA SGPEPRPPAR VETLREEVPT
     DLRVFELNSD SGKSTPSNNG KKGSSTDISE DWEKDFDLDM TEEEVQMALS KVDASGELED
     VEWEDWE
//
ID   RBNS5_MOUSE             Reviewed;         783 AA.
AC   Q80Y56; Q8K0L6; Q9CTW0;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Rabenosyn-5;
DE   AltName: Full=FYVE finger-containing Rab5 effector protein rabenosyn-5;
DE   AltName: Full=Zinc finger FYVE domain-containing protein 20;
GN   Name=Zfyve20;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-384.
RC   STRAIN=C57BL/6J; TISSUE=Pituitary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Rab4/Rab5 effector protein acting in early endocytic
CC       membrane fusion and membrane trafficking of recycling endosomes.
CC       Required for endosome fusion either homotypically or with clathrin
CC       coated vesicles. Plays a role in the lysosomal trafficking of
CC       CTSD/cathepsin D from the Golgi to lysosomes. Also promotes the
CC       recycling of transferrin directly from early endosomes to the
CC       plasma membrane. Binds phospholipid vesicles containing
CC       phosphatidylinositol 3-phosphate (PtdInsP3) (By similarity).
CC   -!- SUBUNIT: Interacts with EHD1, RAB4A, RAB5A, RAB22A, RAB24 and
CC       VPS45. Binds simultaneously to RAB4A and RAB5A in vitro. Interacts
CC       with RAB4A and RAB5A that has been activated by GTP binding (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (By similarity). Early endosome membrane; Lipid-anchor (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 C2H2-type zinc finger.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 1 UIM (ubiquitin-interacting motif) repeat.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC031135; AAH31135.1; -; mRNA.
DR   EMBL; BC049106; AAH49106.1; -; mRNA.
DR   EMBL; AK019909; BAB31910.1; -; mRNA.
DR   IPI; IPI00453559; -.
DR   RefSeq; NP_084357.2; NM_030081.2.
DR   UniGene; Mm.290734; -.
DR   ProteinModelPortal; Q80Y56; -.
DR   SMR; Q80Y56; 11-38, 100-262, 457-500, 733-783.
DR   STRING; Q80Y56; -.
DR   PhosphoSite; Q80Y56; -.
DR   PRIDE; Q80Y56; -.
DR   Ensembl; ENSMUST00000014694; ENSMUSP00000014694; ENSMUSG00000014550.
DR   GeneID; 78287; -.
DR   KEGG; mmu:78287; -.
DR   UCSC; uc009cyv.1; mouse.
DR   CTD; 78287; -.
DR   MGI; MGI:1925537; Zfyve20.
DR   GeneTree; ENSGT00390000007159; -.
DR   HOGENOM; HBG716169; -.
DR   HOVERGEN; HBG067237; -.
DR   InParanoid; Q80Y56; -.
DR   OMA; YEKLRLC; -.
DR   OrthoDB; EOG4G1MG0; -.
DR   PhylomeDB; Q80Y56; -.
DR   NextBio; 348629; -.
DR   ArrayExpress; Q80Y56; -.
DR   Bgee; Q80Y56; -.
DR   CleanEx; MM_ZFYVE20; -.
DR   Genevestigator; Q80Y56; -.
DR   GermOnline; ENSMUSG00000014550; Mus musculus.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR021565; Rbsn.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 2.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF11464; Rbsn; 2.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00355; ZnF_C2H2; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS50330; UIM; FALSE_NEG.
DR   PROSITE; PS50178; ZF_FYVE; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell membrane; Coiled coil; Endosome; Lipoprotein;
KW   Membrane; Metal-binding; Phosphoprotein; Protein transport; Transport;
KW   Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    783       Rabenosyn-5.
FT                                /FTId=PRO_0000098712.
FT   REPEAT      495    514       UIM.
FT   ZN_FING      14     37       C2H2-type.
FT   ZN_FING     156    259       FYVE-type.
FT   REGION       99    262       Necessary for the correct targeting to
FT                                endosomes (By similarity).
FT   REGION      263    783       Necessary for the interaction with EHD1
FT                                (By similarity).
FT   REGION      263    499       Necessary for the interaction with RAB4A
FT                                (By similarity).
FT   REGION      627    783       Necessary for the interaction with RAB5A
FT                                (By similarity).
FT   COILED      377    412       Potential.
FT   COILED      471    531       Potential.
FT   COMPBIAS    203    238       Ser-rich.
FT   COMPBIAS    668    671       Poly-Glu.
FT   COMPBIAS    680    718       Pro-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     213    213       Phosphothreonine (By similarity).
FT   MOD_RES     214    214       Phosphoserine (By similarity).
FT   MOD_RES     216    216       Phosphoserine (By similarity).
FT   MOD_RES     601    601       Phosphoserine (By similarity).
FT   CONFLICT    227    227       R -> Q (in Ref. 1; AAH31135).
FT   CONFLICT    698    698       P -> S (in Ref. 1; AAH31135).
SQ   SEQUENCE   783 AA;  88491 MW;  80103992F296CCD6 CRC64;
     MASLDDPGEV REGFLCPLCL KDLQSFYQLQ SHYEEEHLED RDVKGQIKNL VQKARKAKNK
     LLKREGDDRV EPGTQGYESF SYGGVDPYMW EPQELGAMRS HLSDFKKHRA ARIDHYVVEV
     NKLIIRLEKL TAFDRTNTET SKIRAIEKSV VPWVNDQDVP FCPDCGNKFS IRNRRHHCRL
     CGSIMCKKCM ELIGLPLAHK LTSASKDSLS THTSPSQSPN SVHGSRRGSI SSMSSVSSVL
     DEKDDDRIRC CTHCKDKLLK REQQMDEKEH TPDIVKLYEK LRLCMEKVDQ KAPEYIRMAA
     SLNAGETTYN LEHANDLRVE VQKVYELIDA LSKKILTLGL NQDPSPHPNT LRLQRMIRYS
     ATLFVQEKLL GLMSLPTKEQ FEELKKKRKQ DLEQKRTVER QAALESRRKL EERQSGLASH
     TANGDVRSLR GIPPPLRKAE GWLPLSEGQG QSEDPDPLLQ QIYNITSFIR QAKAAGRTDE
     VRTLQENLRQ LQDEYDQQQT EKAIELSRKQ AEEEELQREQ LQMLRKRELE REQEQFLAAS
     LQTRTRVLEL REVIPFQLEA SRGPHIDLSY SLDQDSSPVQ SSTAPDILTP GSALAPMHLW
     SGPPALGQET LPQSTMSQQS DKASLNPFDE DDLSSPTEGA ISPAAVEAFL GPPAAVTKEY
     NPFEEDAEEE EVAELGAGNP FTDPDSPAPN PFDEDDGPRP ASPAAPGNPF EECPSTNPFE
     VDSDSGMEAE EHIEEELLLQ QIDNIKAYIF DAKQCGRMDE VEVLTENLRE LKCTLAKQKG
     APN
//
ID   RNZ2_MOUSE              Reviewed;         831 AA.
AC   Q80Y81; B1ATP6; Q99MF0; Q99MF1; Q9CTA2; Q9D1A8; Q9EPZ2;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Zinc phosphodiesterase ELAC protein 2;
DE            EC=3.1.26.11;
DE   AltName: Full=ElaC homolog protein 2;
DE   AltName: Full=Ribonuclease Z 2;
DE            Short=RNase Z 2;
DE   AltName: Full=tRNA 3 endonuclease 2;
DE   AltName: Full=tRNase Z 2;
GN   Name=Elac2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=11175785; DOI=10.1038/84808;
RA   Tavtigian S.V., Simard J., Teng D.H.F., Abtin V., Baumgard M.,
RA   Beck A., Camp N.J., Carillo A.R., Chen Y., Dayananth P.,
RA   Desrochers M., Dumont M., Farnham J.M., Frank D., Frye C.,
RA   Ghaffari S., Gupte J.S., Hu R., Iliev D., Janecki T., Kort E.N.,
RA   Laity K.E., Leavitt A., Leblanc G., McArthur-Morrison J., Pederson A.,
RA   Penn B., Peterson K.T., Reid J.E., Richards S., Schroeder M.,
RA   Smith R., Snyder S.C., Swedlund B., Swensen J., Thomas A.,
RA   Tranchant M., Woodland A.-M., Labrie F., Skolnick M.H., Neuhausen S.,
RA   Rommens J., Cannon-Albright L.A.;
RT   "A candidate prostate cancer susceptibility gene at chromosome 17p.";
RL   Nat. Genet. 27:172-180(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 397-831 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 581-831 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195 AND SER-200, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-792, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-815, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191; SER-195 AND
RP   SER-200, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'-
CC       processing endonuclease activity. Probably involved in tRNA
CC       maturation, by removing a 3'-trailer from precursor tRNA (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of RNA, removing
CC       extra 3' nucleotides from tRNA precursor, generating 3' termini of
CC       tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-
CC       phosphoryl group is left at the trailer molecule.
CC   -!- COFACTOR: Zinc (Probable).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80Y81-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80Y81-2; Sequence=VSP_009173;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Belongs to the RNase Z family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF308696; AAG24918.2; -; mRNA.
DR   EMBL; AF348157; AAK29420.1; -; Genomic_DNA.
DR   EMBL; AF348157; AAK29421.1; -; Genomic_DNA.
DR   EMBL; AL663045; CAI24609.1; -; Genomic_DNA.
DR   EMBL; BC048235; AAH48235.1; -; mRNA.
DR   EMBL; AK003759; BAB22981.2; -; mRNA.
DR   EMBL; AK004136; BAB23185.1; -; mRNA.
DR   IPI; IPI00400401; -.
DR   IPI; IPI00400402; -.
DR   RefSeq; NP_075968.2; NM_023479.2.
DR   UniGene; Mm.157711; -.
DR   ProteinModelPortal; Q80Y81; -.
DR   SMR; Q80Y81; 476-750.
DR   STRING; Q80Y81; -.
DR   PhosphoSite; Q80Y81; -.
DR   PRIDE; Q80Y81; -.
DR   Ensembl; ENSMUST00000071891; ENSMUSP00000071788; ENSMUSG00000020549.
DR   GeneID; 68626; -.
DR   KEGG; mmu:68626; -.
DR   CTD; 68626; -.
DR   MGI; MGI:1890496; Elac2.
DR   eggNOG; roNOG13824; -.
DR   GeneTree; ENSGT00530000063605; -.
DR   HOGENOM; HBG446263; -.
DR   HOVERGEN; HBG050042; -.
DR   InParanoid; Q80Y81; -.
DR   OMA; LVHTSGW; -.
DR   OrthoDB; EOG4FTW05; -.
DR   PhylomeDB; Q80Y81; -.
DR   BRENDA; 3.1.26.11; 244.
DR   NextBio; 327580; -.
DR   ArrayExpress; Q80Y81; -.
DR   Bgee; Q80Y81; -.
DR   CleanEx; MM_ELAC2; -.
DR   Genevestigator; Q80Y81; -.
DR   GermOnline; ENSMUSG00000020549; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR001279; Blactmase-like.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   SMART; SM00849; Lactamase_B; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endonuclease; Hydrolase; Metal-binding;
KW   Nuclease; Nucleus; Phosphoprotein; tRNA processing; Zinc.
FT   CHAIN         1    831       Zinc phosphodiesterase ELAC protein 2.
FT                                /FTId=PRO_0000155830.
FT   MOD_RES     191    191       Phosphoserine.
FT   MOD_RES     195    195       Phosphoserine.
FT   MOD_RES     200    200       Phosphoserine.
FT   MOD_RES     792    792       Phosphothreonine.
FT   MOD_RES     815    815       Phosphoserine.
FT   VAR_SEQ     821    831       ESVANTLGARV -> VRAQ (in isoform 2).
FT                                /FTId=VSP_009173.
FT   CONFLICT     27     27       S -> P (in Ref. 1; AAK29420/AAK29421).
FT   CONFLICT    397    397       T -> S (in Ref. 4; BAB23185).
FT   CONFLICT    435    435       L -> P (in Ref. 1; AAG24918).
FT   CONFLICT    714    714       E -> G (in Ref. 1; AAG24918).
SQ   SEQUENCE   831 AA;  92719 MW;  77E3876AE2862224 CRC64;
     MWALRSLLRP LGLRTMSQGS ARRPRPSKDP LRHLRTREKR GPGPGGPNTV YLQVVAAGGR
     DAGAALYVFS EYNRYLFNCG EGVQRLMQEH KLKVARLDNI FLTRMHWSNV GGLCGMILTL
     KETGLPKCVL SGPPQLEKYL EAIKIFSGPL KGIELAVRPH SAPEYKDETM TVYQVPIHSE
     RRCGKQQPSQ SPRTSPNRLS PKQSSDSGSA ENGQCPPEDS SAGANRKAWG RDPSLVVAFV
     CKLHLRKGNF LVLKAKELGL PVGTAAIAPI IAAVKDGKSI TYEGREIAAE ELCTPPDPGL
     VFIVVECPDE GFILPICEND TFKRYQAEAD APVALVVHIA PESVLIDSRY QQWMERFGPD
     TQHLILNENC PSVHNLRSHK IQTQLSLIHP DIFPQLTSFY SKEEGSTLSV PTVRGECLLK
     YQLRPKREWQ RDTTLDCNTD EFIAEALELP SFQESVEEYR KNVQENPAPA EKRSQYPEIV
     FLGTGSAIPM KIRNVSSTLV NLSPDKSVLL DCGEGTFGQL CRHYGQQIDR VLCSLTAVFV
     SHLHADHHTG LLNILLQREH ALASLGKPFQ PLLVVAPTQL RAWLQQYHNH CQEILHHVSM
     IPAKCLQKGA EVSNTTLERL ISLLLETCDL EEFQTCLVRH CKHAFGCALV HSSGWKVVYS
     GDTMPCEALV QMGKDATLLI HEATLEDGLE EEAVEKTHST TSQAINVGMR MNAEFIMLNH
     FSQRYAKIPL FSPDFNEKVG IAFDHMKVCF GDFPTVPKLI PPLKALFAGD IEEMVERREK
     RELRLVRAAL LTQQADSPED REPQQKRAHT DEPHSPQSKK ESVANTLGAR V
//
ID   DDHD2_MOUSE             Reviewed;         699 AA.
AC   Q80Y98; Q0VF66; Q6A008; Q9CVE9;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=Phospholipase DDHD2;
DE            EC=3.1.1.-;
DE   AltName: Full=DDHD domain-containing protein 2;
DE   AltName: Full=SAM, WWE and DDHD domain-containing protein 1;
GN   Name=Ddhd2; Synonyms=Kiaa0725, Samwd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-149 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Phospholipase that hydrolyzes preferentially
CC       phosphatidic acid and phosphatidylethanolamine. May be involved in
CC       the maintenance of the endoplasmic reticulum and/or Golgi
CC       structures (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasmic
CC       granule (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q80Y98-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80Y98-2; Sequence=VSP_029141, VSP_029143;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q80Y98-3; Sequence=VSP_029142, VSP_029144;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the PA-PLA1 family.
CC   -!- SIMILARITY: Contains 1 DDHD domain.
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
CC   -!- SIMILARITY: Contains 1 WWE domain.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-31 is the initiator.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH46229.1; Type=Erroneous initiation;
CC       Sequence=AAI18963.1; Type=Frameshift; Positions=149;
CC       Sequence=BAD32288.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK173010; BAD32288.1; ALT_INIT; Transcribed_RNA.
DR   EMBL; BC046229; AAH46229.1; ALT_INIT; mRNA.
DR   EMBL; BC118962; AAI18963.1; ALT_FRAME; mRNA.
DR   EMBL; AK008529; BAB25722.1; -; mRNA.
DR   IPI; IPI00381071; -.
DR   IPI; IPI00666427; -.
DR   IPI; IPI00875605; -.
DR   RefSeq; NP_082378.1; NM_028102.1.
DR   UniGene; Mm.246875; -.
DR   ProteinModelPortal; Q80Y98; -.
DR   SMR; Q80Y98; 386-449.
DR   PhosphoSite; Q80Y98; -.
DR   PRIDE; Q80Y98; -.
DR   Ensembl; ENSMUST00000033975; ENSMUSP00000033975; ENSMUSG00000061313.
DR   Ensembl; ENSMUST00000098860; ENSMUSP00000096459; ENSMUSG00000061313.
DR   GeneID; 72108; -.
DR   KEGG; mmu:72108; -.
DR   UCSC; uc009lgv.1; mouse.
DR   CTD; 72108; -.
DR   MGI; MGI:1919358; Ddhd2.
DR   eggNOG; roNOG12328; -.
DR   GeneTree; ENSGT00530000063155; -.
DR   HOGENOM; HBG403107; -.
DR   HOVERGEN; HBG057256; -.
DR   InParanoid; Q80Y98; -.
DR   OrthoDB; EOG4BK53G; -.
DR   ArrayExpress; Q80Y98; -.
DR   Bgee; Q80Y98; -.
DR   CleanEx; MM_DDHD2; -.
DR   Genevestigator; Q80Y98; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR004177; DDHD.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   InterPro; IPR004170; WWE-dom.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF02862; DDHD; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   Pfam; PF02825; WWE; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS51043; DDHD; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; FALSE_NEG.
DR   PROSITE; PS50918; WWE; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Hydrolase; Lipid degradation;
KW   Phosphoprotein.
FT   CHAIN         1    699       Phospholipase DDHD2.
FT                                /FTId=PRO_0000309331.
FT   DOMAIN       30    112       WWE.
FT   DOMAIN      383    445       SAM.
FT   DOMAIN      484    688       DDHD.
FT   ACT_SITE    351    351       Probable.
FT   MOD_RES     447    447       Phosphoserine.
FT   VAR_SEQ       1      1       M -> MRGQKVRFSSFKASAQARPPVRVPHAPSACPARARR
FT                                PTSARRRSQVSRESPSPHRTSRDTSEDLSAPPALTGSAASA
FT                                GALLSTAGALRSPRCGDWGAAAGSARPPRPAWESEM (in
FT                                isoform 2).
FT                                /FTId=VSP_029141.
FT   VAR_SEQ     283    382       IDLQRITLPSINRLRHFTNDTILDVFFYNSPTYCQTIVDTV
FT                                ASEMNRIYTLFLQRNPDFKGGVSIAGHSLGSLILFDILTNQ
FT                                KNSIGDIDSEKGSLSSAE -> M (in isoform 3).
FT                                /FTId=VSP_029142.
FT   VAR_SEQ     448    528       Missing (in isoform 2).
FT                                /FTId=VSP_029143.
FT   VAR_SEQ     529    562       Missing (in isoform 3).
FT                                /FTId=VSP_029144.
SQ   SEQUENCE   699 AA;  79604 MW;  BB03118F9200B1DA CRC64;
     MSSGESHQEQ LSQSDPSPSP NSCSSFELID MDASSSYEPV SPHWFYCKVL DSKELWIPFN
     SEDSQQLEDA YGSGKDCNER IVPTDGGRYD VHLGERMRYA VYWDELPSEV RRCTWFYKGD
     KDNKYVPYSE SFSQVLEDTY MLAVTLDEWK KKIESPNREI IVLHNPKLMV HYQPIAGSDE
     WGSTSTEQGR PRSVKRGVEN IPVDIHCGEP LQIDHLVFVV HGIGPACDLR FRSIVQCVND
     FRSVSLNLLQ THFKKAQENE QIGRVEFLPV NWHSPLHSTG VDIDLQRITL PSINRLRHFT
     NDTILDVFFY NSPTYCQTIV DTVASEMNRI YTLFLQRNPD FKGGVSIAGH SLGSLILFDI
     LTNQKNSIGD IDSEKGSLSS AEDRGDASTL EEDLKKLQLS EFVTVFEKEK VDREALALCT
     DRDLQEMGIP LGPRKKILNH FSARKNSVSI NRPAMSASEV NISKENGDYL DVGIGQVSVK
     YPRLNYKPEI FFAFGSPIGM FLTVRGLRRI DPNYKFPTCK GFFNIYHPFD PVAYRIEPMV
     APGIEFEPML IPHHKGRKRM HLELREGLTR MSMDLKNNLL GSLRMAWKSF TRGPYPALQA
     SETAEETEAE PESSSEKSNE ANTEEPPVEV KEEAPINVGM LNGGQRIDYV LQEKPIESFN
     EYLFALQSHL CYWESEDTVL LVLKEIYQTQ GVFLDQPLQ
//
ID   CNKR2_MOUSE             Reviewed;        1032 AA.
AC   Q80YA9; Q80TP2;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Connector enhancer of kinase suppressor of ras 2;
DE            Short=Connector enhancer of KSR 2;
DE   AltName: Full=CNK homolog protein 2;
DE            Short=CNK2;
GN   Name=Cnksr2; Synonyms=Kiaa0902;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248; SER-467 AND
RP   SER-906, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325; THR-846 AND
RP   SER-906, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: May function as an adapter protein or regulator of Ras
CC       signaling pathways.
CC   -!- SUBUNIT: Interacts with RAF1, RAB2L and RAL GTPase proteins (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane;
CC       Peripheral membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80YA9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80YA9-2; Sequence=VSP_010890;
CC   -!- PTM: Phosphorylated on tyrosine (By similarity).
CC   -!- SIMILARITY: Belongs to the CNKSR family.
CC   -!- SIMILARITY: Contains 1 CRIC domain.
CC   -!- SIMILARITY: Contains 1 DUF1170 domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65681.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK122399; BAC65681.1; ALT_INIT; mRNA.
DR   EMBL; BC043093; AAH43093.1; -; mRNA.
DR   EMBL; BC060716; AAH60716.1; -; mRNA.
DR   IPI; IPI00228877; -.
DR   IPI; IPI00474100; -.
DR   RefSeq; NP_808419.1; NM_177751.2.
DR   UniGene; Mm.197074; -.
DR   ProteinModelPortal; Q80YA9; -.
DR   SMR; Q80YA9; 6-80, 211-299, 571-671.
DR   PhosphoSite; Q80YA9; -.
DR   PRIDE; Q80YA9; -.
DR   Ensembl; ENSMUST00000026750; ENSMUSP00000026750; ENSMUSG00000025658.
DR   Ensembl; ENSMUST00000112515; ENSMUSP00000108134; ENSMUSG00000025658.
DR   GeneID; 245684; -.
DR   KEGG; mmu:245684; -.
DR   UCSC; uc009ush.1; mouse.
DR   UCSC; uc009usi.1; mouse.
DR   CTD; 245684; -.
DR   MGI; MGI:2661175; Cnksr2.
DR   GeneTree; ENSGT00390000017199; -.
DR   HOGENOM; HBG403049; -.
DR   HOVERGEN; HBG051040; -.
DR   InParanoid; Q80YA9; -.
DR   OMA; NSPADRC; -.
DR   OrthoDB; EOG4G1MFQ; -.
DR   PhylomeDB; Q80YA9; -.
DR   NextBio; 386914; -.
DR   ArrayExpress; Q80YA9; -.
DR   Bgee; Q80YA9; -.
DR   CleanEx; MM_CNKSR2; -.
DR   Genevestigator; Q80YA9; -.
DR   GermOnline; ENSMUSG00000025658; Mus musculus.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR   InterPro; IPR010599; CNKSR2.
DR   InterPro; IPR017874; CRIC_domain.
DR   InterPro; IPR019555; CRIC_domain_Chordata.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF10534; CRIC_ras_sig; 1.
DR   Pfam; PF06663; DUF1170; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS51290; CRIC; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Membrane;
KW   Phosphoprotein.
FT   CHAIN         1   1032       Connector enhancer of kinase suppressor
FT                                of ras 2.
FT                                /FTId=PRO_0000089971.
FT   DOMAIN       11     76       SAM.
FT   DOMAIN       84    178       CRIC.
FT   DOMAIN      215    297       PDZ.
FT   DOMAIN      302    515       DUF1170.
FT   DOMAIN      570    669       PH.
FT   COILED      874    917       Potential.
FT   COMPBIAS    354    357       Poly-Pro.
FT   COMPBIAS    703    706       Poly-Pro.
FT   COMPBIAS    875    886       Poly-Glu.
FT   MOD_RES     248    248       Phosphoserine.
FT   MOD_RES     325    325       Phosphoserine.
FT   MOD_RES     390    390       Phosphoserine.
FT   MOD_RES     467    467       Phosphoserine.
FT   MOD_RES     846    846       Phosphothreonine.
FT   MOD_RES     906    906       Phosphoserine.
FT   VAR_SEQ     271    319       Missing (in isoform 2).
FT                                /FTId=VSP_010890.
SQ   SEQUENCE   1032 AA;  117396 MW;  FE97ED5E3CDB75BF CRC64;
     MALIMEPVSK WSPSQVVDWM KGLDDCLQQY IKNFEREKIS GDQLLRITHQ ELEDLGVSRI
     GHQELILEAV DLLCALNYGL ETENLKTLSH KLNASAKNLQ NFITGRRRSG HYDGRTSRKL
     PNDFLTSVVD LIGAAKSLLA WLDRSPFAAV TDYSVTRNNV IQLCLELTTI VQQDCTVYET
     ENKILHVCKT LSGVCDHIIS LSSDPLVSQS AHLEVIQLAN IKPSEGLGMY IKSTYDGLHV
     ITGTTENSPA DRCKKIHAGD EVIQVNHQTV VGWQLKNLVN ALREDPSGVI LTLKKRPQSM
     LTSAPALLKN MRWKPLALQP LIPRSPTSSV ATPSSTISTP TKRDSSALQD LYIPPPPAEP
     YIPRDEKGNL PCEDLRGHMV GKPVHKGSES PNSFLDQEYR KRFNIVEEDT VLYCYEYEKG
     RSSSQGRRES TPTYGKLRPI SMPVEYNWVG DYEDPNKMKR DSRRENSLLR YMSNEKIAQE
     EYMFQRNSKK DTGKKSKKKG DKSNSPAHYS LLPSLQMDAL RQDIMGTPVP ETTLYHTFQQ
     SSLQHKSKKK NKGAISGKSK RRISCKDLGR GDCEGWLWKK KDAKSYFSQK WKKYWFVLKD
     ASLYWYINEE DEKAEGFISL PEFKIDRASE CRKKYAFKAC HPKIKSFYFA AEHLDDMNRW
     LNRINMLTAG YAERERIKQE QDYWSESDKE EADTPSTPKQ DSPPPPYDTY PRPPSMSCAS
     PYVEAKHSRL SSTETSQSQS SHEEFRQEVT GSSAVSPIRK TASQRRSWQD LIETPLTSSG
     LHYLQTLPLE DSVFSDSAAI SPEHRRQSTL PTQKCHLQDH YGPYPLAESE RMQVLNGNGG
     KPRSFTLPRD SGFNHCCLNT PVSACDPQDD IQPPEVEEEE EEEEEEAAGE NVGEKNENRE
     EKLGDSLQDL YRALEEASLS PLGEHRISTK MEYKLSFIKR CNDPVMNEKL HRLRILKSTL
     KAREGEVAII DKVLDNPDLT SKEFQQWKQM YLDLFLDICQ STTSNDPLSI SSEVDVLTSS
     LTHTHSYIET HV
//
ID   SUV3_MOUSE              Reviewed;         779 AA.
AC   Q80YD1; Q50HX5;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=ATP-dependent RNA helicase SUPV3L1, mitochondrial;
DE            EC=3.6.4.13;
DE   AltName: Full=Suppressor of var1 3-like protein 1;
DE            Short=SUV3-like protein 1;
DE   Flags: Precursor;
GN   Name=Supv3l1; Synonyms=Suv3l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Zhang C., Yang T., Liu G., Chen Q.;
RT   "A null mutation existed in SUV3L1 of SAMP8/Ta.";
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: ATPase and DNA/RNA helicase able to unwind DNA/DNA,
CC       DNA/RNA and RNA/RNA duplexes in the 5'-3' direction. May protect
CC       cells from apoptosis (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- COFACTOR: Magnesium or manganese (By similarity).
CC   -!- SUBUNIT: Interacts with HBXIP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC       Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the helicase family.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AJ968954; CAI92124.1; -; mRNA.
DR   EMBL; BC049796; AAH49796.1; -; mRNA.
DR   IPI; IPI00314919; -.
DR   RefSeq; NP_852088.1; NM_181423.2.
DR   UniGene; Mm.235898; -.
DR   ProteinModelPortal; Q80YD1; -.
DR   STRING; Q80YD1; -.
DR   PhosphoSite; Q80YD1; -.
DR   PRIDE; Q80YD1; -.
DR   Ensembl; ENSMUST00000020273; ENSMUSP00000020273; ENSMUSG00000020079.
DR   GeneID; 338359; -.
DR   KEGG; mmu:338359; -.
DR   UCSC; uc007fhd.1; mouse.
DR   CTD; 338359; -.
DR   MGI; MGI:2441711; Supv3l1.
DR   eggNOG; roNOG09041; -.
DR   GeneTree; ENSGT00390000003100; -.
DR   HOGENOM; HBG383122; -.
DR   HOVERGEN; HBG108522; -.
DR   InParanoid; Q80YD1; -.
DR   OMA; TYHAIQR; -.
DR   OrthoDB; EOG4SXNBZ; -.
DR   NextBio; 400135; -.
DR   ArrayExpress; Q80YD1; -.
DR   Bgee; Q80YD1; -.
DR   CleanEx; MM_SUPV3L1; -.
DR   Genevestigator; Q80YD1; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR022192; SUV3_C.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF12513; SUV3_C; 1.
DR   SMART; SM00490; HELICc; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; FALSE_NEG.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Helicase; Hydrolase; Mitochondrion;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Transit peptide.
FT   TRANSIT       1     40       Mitochondrion (Potential).
FT   CHAIN        41    779       ATP-dependent RNA helicase SUPV3L1,
FT                                mitochondrial.
FT                                /FTId=PRO_0000310546.
FT   DOMAIN      194    334       Helicase ATP-binding.
FT   DOMAIN      353    521       Helicase C-terminal.
FT   NP_BIND     207    214       ATP (By similarity).
FT   REGION      650    779       Interaction with HBXIP, important for
FT                                protein stability (By similarity).
FT   MOD_RES      99     99       N6-acetyllysine (By similarity).
FT   MOD_RES     725    725       Phosphoserine (By similarity).
FT   CONFLICT    109    109       L -> R (in Ref. 1; CAI92124).
FT   CONFLICT    157    157       D -> G (in Ref. 1; CAI92124).
SQ   SEQUENCE   779 AA;  87005 MW;  877F2B611FEEE1A9 CRC64;
     MSLPRCTLLW ARLPAGRGAG PRAAPCSALR ALVGSFPGAS GRVPCLAASS SASGGSKAPN
     TSLFVPLTVK PQGPSADGDV GAELTRPLDK NEVKKILDKF YKRQEIQKLS ADYGLDARLF
     HQAFISFRNY IMQSHSLDVD IHIVLNDICF SAAHVDDLFP FFLRHAKQIF PVLECKDDLR
     KISDLRIPPN WYPEARARQR KIIFHSGPTN SGKTYHAIQR YLSATSGVYC GPLKLLAHEI
     FEKSNAAGVP CDLVTGEERL TVEPEGKQAT HVSCTVEMCN VATPYEVAVI DEIQMIRDPA
     RGWAWTRALL GLCAEEVHLC GESAAINLVS ELLYTTGEEV EVQKYERLTP ISVLDHALES
     LDNLQPGDCI VCFSKNDIYS VSRQIEIRGL ESAVIYGSLP PGTKLAQARK FNDPNDPCKI
     LVATDAIGMG LNLSIRRIIF YSLIKPSINE KGEKELEPIT TSQALQIAGR AGRFSSHFKE
     GQVTTMHRDD LALLKDILNR PVDPIQAAGL HPTAEQIEMF AYHLPETTLS NLIDIFVDFA
     QVDGQYFVCN MDDFKFSAEL IQHIPLSLRV RYVFCTAPIN KKQPFVCSSL LQFARQYSRN
     EPLTFAWLRR YIKWPLLPPK NIKDLMDLEA VHDVFDLYLW LSYRFIDMFP DSSLVRSLQK
     ELDAIIQEGV HNITKLIKIS ESRKLLNLES LPSGDQSRLS GASKSPARRT RGTKSAGNKA
     TEPLSPSDKE LPLASRLVQQ GLLTADMLRQ LQKEWLTQQP EHSREKVGTR RKKKDPDSD
//
ID   LMTK1_MOUSE             Reviewed;        1365 AA.
AC   Q80YE4; O35211; Q3U2U5; Q3UHR8; Q66JN3; Q80YE3; Q8CB63; Q8CHE2;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Serine/threonine-protein kinase LMTK1;
DE            EC=2.7.11.1;
DE   AltName: Full=Apoptosis-associated tyrosine kinase;
DE            Short=AATYK;
DE   AltName: Full=Brain apoptosis-associated tyrosine kinase;
DE   AltName: Full=Lemur tyrosine kinase 1;
GN   Name=Aatk; Synonyms=Aatyk, Kiaa0641, Lmr1, Lmtk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INDUCTION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Bone marrow;
RX   MEDLINE=98105706; PubMed=9444961; DOI=10.1038/sj.onc.1201575;
RA   Gaozza E., Baker S.J., Vora R.K., Reddy E.P.;
RT   "AATYK: a novel tyrosine kinase induced during growth arrest and
RT   apoptosis of myeloid cells.";
RL   Oncogene 15:3127-3135(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), INDUCTION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=129/SvJ; TISSUE=Brain;
RX   MEDLINE=21214502; PubMed=11314039; DOI=10.1038/sj.onc.1204209;
RA   Baker S.J., Sumerson R., Reddy C.D., Berrebi A.S., Flynn D.C.,
RA   Reddy E.P.;
RT   "Characterization of an alternatively spliced AATYK mRNA: expression
RT   pattern of AATYK in the brain and neuronal cells.";
RL   Oncogene 20:1015-1021(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [4]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   TISSUE SPECIFICITY, PHOSPHORYLATION, AND MUTAGENESIS OF ASP-254.
RX   PubMed=11314040; DOI=10.1038/sj.onc.1204210;
RA   Tomomura M., Fernandez-Gonzales A., Yano R., Yuzaki M.;
RT   "Characterization of the apoptosis-associated tyrosine kinase (AATYK)
RT   expressed in the CNS.";
RL   Oncogene 20:1022-1032(2001).
CC   -!- FUNCTION: May be involved in neuronal differentiation (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts with CDK5 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein. Cytoplasm. Cytoplasm, perinuclear region (By similarity).
CC       Note=Predominantly perinuclear (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q80YE4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80YE4-2; Sequence=VSP_020230;
CC       Name=3;
CC         IsoId=Q80YE4-3; Sequence=VSP_020231;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q80YE4-4; Sequence=VSP_020229, VSP_020232;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, and, to a lower extent, in
CC       kidney, heart, lung and skeletal muscle.
CC   -!- INDUCTION: Up-regulated during the apoptotic death of myeloid
CC       cells induced by cytokine withdrawal, such as IL3, and during G-
CC       CSF-induced terminal differentiation of myeloblasts to
CC       granulocytes.
CC   -!- PTM: Autophosphorylated. Phosphorylated by CDK5 (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC41437.2; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF011908; AAB71837.1; -; mRNA.
DR   EMBL; AY236858; AAO92350.1; -; mRNA.
DR   EMBL; AY236859; AAO92351.1; -; mRNA.
DR   EMBL; AB093253; BAC41437.2; ALT_INIT; mRNA.
DR   EMBL; AK036705; BAC29541.1; -; mRNA.
DR   EMBL; AK147239; BAE27789.1; -; mRNA.
DR   EMBL; AK155100; BAE33045.1; -; mRNA.
DR   EMBL; BC080846; AAH80846.1; -; mRNA.
DR   IPI; IPI00407649; -.
DR   IPI; IPI00625847; -.
DR   IPI; IPI00785372; -.
DR   IPI; IPI00785527; -.
DR   PIR; T03748; T03748.
DR   RefSeq; NP_001185716.1; NM_001198787.1.
DR   RefSeq; NP_031403.2; NM_007377.4.
DR   UniGene; Mm.6826; -.
DR   HSSP; Q62838; 1LUF.
DR   ProteinModelPortal; Q80YE4; -.
DR   SMR; Q80YE4; 116-400.
DR   IntAct; Q80YE4; 2.
DR   STRING; Q80YE4; -.
DR   PhosphoSite; Q80YE4; -.
DR   PRIDE; Q80YE4; -.
DR   Ensembl; ENSMUST00000064307; ENSMUSP00000067181; ENSMUSG00000025375.
DR   GeneID; 11302; -.
DR   KEGG; mmu:11302; -.
DR   UCSC; uc007mrk.1; mouse.
DR   UCSC; uc007mrl.1; mouse.
DR   UCSC; uc007mro.1; mouse.
DR   CTD; 11302; -.
DR   MGI; MGI:1197518; Aatk.
DR   eggNOG; roNOG10766; -.
DR   GeneTree; ENSGT00600000084075; -.
DR   HOVERGEN; HBG080533; -.
DR   InParanoid; Q80YE4; -.
DR   BRENDA; 2.7.11.1; 244.
DR   ArrayExpress; Q80YE4; -.
DR   Bgee; Q80YE4; -.
DR   CleanEx; MM_AATK; -.
DR   Genevestigator; Q80YE4; -.
DR   GermOnline; ENSMUSG00000025375; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IDA:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN         1   1365       Serine/threonine-protein kinase LMTK1.
FT                                /FTId=PRO_0000248301.
FT   TRANSMEM     32     52       Helical; (Potential).
FT   DOMAIN      126    396       Protein kinase.
FT   NP_BIND     132    140       ATP (By similarity).
FT   COMPBIAS     84     87       Poly-Ala.
FT   ACT_SITE    254    254       Proton acceptor (By similarity).
FT   BINDING     157    157       ATP (By similarity).
FT   VAR_SEQ       1    168       Missing (in isoform 4).
FT                                /FTId=VSP_020229.
FT   VAR_SEQ       1     48       Missing (in isoform 2).
FT                                /FTId=VSP_020230.
FT   VAR_SEQ       1      1       M -> MLIALLALAM (in isoform 3).
FT                                /FTId=VSP_020231.
FT   VAR_SEQ    1354   1365       PAAGAGGRYTEA -> MSVVGAEVEQRDTTNGDL (in
FT                                isoform 4).
FT                                /FTId=VSP_020232.
FT   MUTAGEN     254    254       D->V: No change in phosphorylation.
FT   CONFLICT    270    270       V -> D (in Ref. 5; BAC29541).
FT   CONFLICT    345    345       R -> G (in Ref. 5; BAC29541/BAE27789/
FT                                BAE33045 and 6; AAH80846).
FT   CONFLICT    773    773       T -> K (in Ref. 5; BAE33045).
FT   CONFLICT    988    988       G -> S (in Ref. 5; BAE27789).
FT   CONFLICT   1317   1317       A -> S (in Ref. 5; BAC29541).
SQ   SEQUENCE   1365 AA;  144607 MW;  051A53505EDAF502 CRC64;
     MSSSFFNPSF AFSSHFDPDG APLSELSWSS SLAVVAVSFS GIFTVVILML ACLCCKKGGI
     GFKEFENAEG DEYVADFSEQ GSPAAAAQTG PDVYVLPLTE VSLPMAKQPG RSVQLLKSTD
     LGRHSLLYLK EIGHGWFGKV FLGEVHSGVS GTQVVVKELK VSASVQEQMQ FLEEAQPYRA
     LQHSNLLQCL AQCAEVTPYL LVMEFCPLGD LKGYLRSCRV TESMAPDPLT LQRMACEVAC
     GVLHLHRHNY VHSDLALRNC LLTADLTVKV GDYGLSHCKY REDYLVTADQ LWVPLRWIAP
     ELVDEVHGNL LVVDQTKSSN VWSLGVTIWE LFELGAQPYP QHSDRQVLAY AVREQQLKLP
     KPQLQLALSD RWYEVMQFCW LQPEQRPTAE EVHLLLSYLC AKGTTELEEE FERRWRSLRP
     GGSTGLGSGS AAPAAATAAS AELTAASSFP LLERFTSDGF HVDSDDVLTV TETSHGLNFE
     YKWEAGCGAE EYPPSGAASS PGSAARLQEL CAPDSSPPGV VPVLSAHSPS VGSEYFIRLE
     GAVPAAGHDP DCAGCAPSPQ AVTDQDNNSE ESTVASLAME PLLGHAPPTE GLWGPCDHHS
     HRRQGSPCPS RSPSPGTPML PAEDIDWGVA TFCPPFFDDP LGASPSGSPG AQPSPSDEEP
     EEGKVGLAAQ CGHWSSNMSA NNNSASRDPE SWDPGYVSSF TDSYRDDCSS LEQTPRASPE
     VGHLLSQEDP RDFLPGLVAV SPGQEPSRPF NLLPLCPAKG LAPAACLITS PWTEGAVGGA
     ENPIVEPKLA QEAEGSAEPQ LPLPSVPSPS CEGASLPSEE ASAPDILPAS PTPAAGSWVT
     VPEPAPTLES SGSSLGQEAP SSEDEDTTEA TSGVFTDLSS DGPHTEKSGI VPALRSLQKQ
     VGTPDSLDSL DIPSSASDGG CEVLSPSAAG PPGGQPRAVD SGYDTENYES PEFVLKEAHE
     SSEPEAFGEP ASEGESPGPD PLLSVSLGGL SKKSPYRDSA YFSDLDAESE PTFGPEKHSG
     IQDSQKEQDL RSPPSPGHQS VQAFPRSAVS SEVLSPPQQS EEPLPEVPRP EPLGAQGPVG
     VQPVPGPSHS KCFPLTSVPL ISEGSGTEPQ GPSGQLSGRA QQGQMGNPST PRSPLCLALP
     GHPGALEGRP EEDEDTEDSE ESDEELRCYS VQEPSEDSEE EPPAVPVVVA ESQSARNLRS
     LLKMPSLLSE AFCDDLERKK KAVSFFDDVT VYLFDQESPT RETGEPFPST KESLPTFLEG
     GPSSPSATGL PLRAGHSPDS SAPEPGSRFE WDGDFPLVPG KAALVTELDP ADPVLAAPPT
     PAAPFSRFTV SPTPASRFSI THISDSDAQS VGGPAAGAGG RYTEA
//
ID   DAPK1_MOUSE             Reviewed;        1442 AA.
AC   Q80YE7; Q80YE6; Q8R341; Q8VDN6; Q9CSD4; Q9JJP7;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2003, sequence version 3.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Death-associated protein kinase 1;
DE            Short=DAP kinase 1;
DE            EC=2.7.11.1;
GN   Name=Dapk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Embryo;
RX   MEDLINE=21523887; PubMed=11485996; DOI=10.1074/jbc.M101886200;
RA   Jin Y., Blue E.K., Dixon S., Hou L., Wysolmerski R.B., Gallagher P.J.;
RT   "Identification of a new form of death-associated protein kinase that
RT   promotes cell survival.";
RL   J. Biol. Chem. 276:39667-39678(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RA   Kimchi A.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1203-1442 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Calcium/calmodulin-dependent serine/threonine kinase.
CC       Isoform 1 is a negative regulator of apoptosis in direct contrast
CC       to its human homolog. Isoform 2 has no effect on apoptosis and its
CC       function is unknown.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: Negatively regulated by autophosphorylation on
CC       Ser-308 (By similarity).
CC   -!- SUBUNIT: Interacts with KLHL20 (By similarity).
CC   -!- INTERACTION:
CC       Q01097:Grin2b; NbExp=3; IntAct=EBI-2584874, EBI-400125;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Beta;
CC         IsoId=Q80YE7-1; Sequence=Displayed;
CC       Name=2; Synonyms=Alpha;
CC         IsoId=Q80YE7-2; Sequence=VSP_050629;
CC   -!- TISSUE SPECIFICITY: High levels in bladder, uterus, vas deferens,
CC       lung, liver and kidney.
CC   -!- PTM: Ubiquitinated by the BCR(KLHL20) E3 ubiquitin ligase complex,
CC       leading to its degradation by the proteasome (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. DAP kinase subfamily.
CC   -!- SIMILARITY: Contains 10 ANK repeats.
CC   -!- SIMILARITY: Contains 1 death domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH21490.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AY245540; AAO91934.2; -; mRNA.
DR   EMBL; AY245541; AAO91935.1; -; mRNA.
DR   EMBL; X97048; CAA65762.1; -; mRNA.
DR   EMBL; BC021490; AAH21490.1; ALT_INIT; mRNA.
DR   EMBL; BC026671; AAH26671.1; -; mRNA.
DR   EMBL; BC057317; AAH57317.1; -; mRNA.
DR   EMBL; BC060161; AAH60161.1; -; mRNA.
DR   EMBL; AK013153; BAB28681.1; -; mRNA.
DR   IPI; IPI00395143; -.
DR   IPI; IPI00395144; -.
DR   RefSeq; NP_083929.2; NM_029653.2.
DR   UniGene; Mm.24103; -.
DR   ProteinModelPortal; Q80YE7; -.
DR   SMR; Q80YE7; 3-320, 344-742, 1294-1397.
DR   IntAct; Q80YE7; 10.
DR   STRING; Q80YE7; -.
DR   PhosphoSite; Q80YE7; -.
DR   PRIDE; Q80YE7; -.
DR   Ensembl; ENSMUST00000044083; ENSMUSP00000040825; ENSMUSG00000021559.
DR   Ensembl; ENSMUST00000077453; ENSMUSP00000076666; ENSMUSG00000021559.
DR   GeneID; 69635; -.
DR   KEGG; mmu:69635; -.
DR   UCSC; uc007qvm.1; mouse.
DR   UCSC; uc007qvn.1; mouse.
DR   CTD; 69635; -.
DR   MGI; MGI:1916885; Dapk1.
DR   GeneTree; ENSGT00600000084057; -.
DR   HOGENOM; HBG446459; -.
DR   HOVERGEN; HBG051296; -.
DR   InParanoid; Q80YE7; -.
DR   OMA; MDIHASD; -.
DR   OrthoDB; EOG4KD6K6; -.
DR   PhylomeDB; Q80YE7; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 329950; -.
DR   ArrayExpress; Q80YE7; -.
DR   Bgee; Q80YE7; -.
DR   CleanEx; MM_DAPK1; -.
DR   Genevestigator; Q80YE7; -.
DR   GermOnline; ENSMUSG00000021559; Mus musculus.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006916; P:anti-apoptosis; IMP:UniProtKB.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0008624; P:induction of apoptosis by extracellular signals; TAS:ProtInc.
DR   GO; GO:0007243; P:intracellular protein kinase cascade; IDA:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR000488; Death.
DR   InterPro; IPR020676; Death-assoc_prot_kinase.
DR   InterPro; IPR011029; DEATH-like.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR020675; Myosin_light_chain_kin-rel.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 3.
DR   Gene3D; G3DSA:1.10.533.10; DEATH_like; 1.
DR   PANTHER; PTHR22964:SF1; Death-assoc_prot_kinase; 1.
DR   PANTHER; PTHR22964; Myosin_light_chain_kin-rel; 1.
DR   Pfam; PF00023; Ank; 6.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00248; ANK; 9.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF47986; DEATH_like; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 7.
DR   PROSITE; PS50017; DEATH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ANK repeat; Apoptosis; ATP-binding;
KW   Calmodulin-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Repeat; Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT   CHAIN         1   1442       Death-associated protein kinase 1.
FT                                /FTId=PRO_0000085911.
FT   DOMAIN       13    275       Protein kinase.
FT   REPEAT      378    407       ANK 1.
FT   REPEAT      411    440       ANK 2.
FT   REPEAT      444    473       ANK 3.
FT   REPEAT      477    506       ANK 4.
FT   REPEAT      510    539       ANK 5.
FT   REPEAT      543    572       ANK 6.
FT   REPEAT      576    605       ANK 7.
FT   REPEAT      609    638       ANK 8.
FT   REPEAT      875    904       ANK 9.
FT   REPEAT     1164   1196       ANK 10.
FT   DOMAIN     1312   1396       Death.
FT   NP_BIND      19     27       ATP (By similarity).
FT   REGION      267    334       Calmodulin-binding (By similarity).
FT   ACT_SITE    139    139       Proton acceptor (By similarity).
FT   BINDING      42     42       ATP (By similarity).
FT   MOD_RES     308    308       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   VAR_SEQ    1431   1442       Missing (in isoform 2).
FT                                /FTId=VSP_050629.
FT   CONFLICT    354    354       D -> N (in Ref. 2; CAA65762).
FT   CONFLICT    441    441       K -> Q (in Ref. 3; AAH57317/AAH60161).
FT   CONFLICT    461    461       V -> A (in Ref. 2; CAA65762).
FT   CONFLICT    960    960       S -> P (in Ref. 2; CAA65762).
FT   CONFLICT   1000   1000       N -> T (in Ref. 2; CAA65762).
FT   CONFLICT   1038   1042       RWLCT -> PMALH (in Ref. 2; CAA65762).
FT   CONFLICT   1105   1105       A -> V (in Ref. 1; AAO91934/AAO91935).
SQ   SEQUENCE   1442 AA;  161442 MW;  243A14D7C6598F63 CRC64;
     MTVFRQENVD DYYDTGEELG SGQFAVVKKC REKSTGLQYA AKFIKKRRTK SSRRGVSRED
     IEREVSILKE IRHPNVITLH EVYENKTDVI LILELVAGGE LFDFLAEKES LTEEEATEFL
     KQILSGVYYL HSLQIAHFDL KPENIMLLDR NVPKPRIKII DFGLAHKIDF GNEFKNIFGT
     PEFVAPEIVN YEPLGLEADM WSIGVITYIL LSGASPFLGD TKQETLANVS AVNYDFEEEF
     FRNTSTLAKD FIRRLLVKDP KKRMTIQDSL QHPWIKPKDT QQALSRKASA VNMEKFKKFA
     ARKKWKQSVR LISLCQRLSR SFLSRSNMSV ARSDDTLDEE DSFVMKAIIH AINDDNVPGL
     QHLLGSLSSY DVNQPNKHGT PPLLIAAGCG NIQMLQLLIK RGSRIDVQDK GGSNAIYWAS
     RHGHVDTLKF LNENKCPLDV KDKSGETALH VAARYGHADV VQLLCSFGSN PDFQDKEEET
     PLHCAAWHGY YSVAKALCEV GCNVNIKNRE GETPLLTASA RGYHDIVECL AEHGADLNAS
     DKDGHIALHL AVRRCQMEVI KTLLGHGSFV DFQDRHGNTP LHVACKDGSA PIVVALCEAS
     CNLDISNKYG RTPLHLAANN GILDVVRYLC LMGANVEALT SDGKTAEDLA KAEQHEHVAG
     LLARLRKDTH RGLFIQQLRP TQNLQPRIKL KLFGHSGSGK STLVESLKCG LLRSFFRRRR
     PRLSSTNSTR FPPSPLAAKP TVSVSINNLY PGCENVSVRS RSMMFEPGLT KGMLEVFVAP
     SHHLHCSTDD QSTKAIDIQN AYLNGVGDFS VWEFSGNPVY FCCYDYFAAN DPTSIHIIVF
     SLEEPYEIQL NQVIFWLSFL KSLVPVEEPI AFGGKLKNPL RVVLVATHAD IMNIPRPAGG
     EFGYDKDTSL LKEIRNRFGN DLHVSNKLFV LDAGASGSKD IKVLRNHLQE IRSQIVSGCS
     PMTHLCEKII STLPSWRKLN GPNQLMSLQQ FVYDVQDQLN PLASEDDLRR IAQQLHSTGE
     INIMQSETVQ DVLLLDPRWL CTNVLGKLLS VETPRALHHY RGRYTMEDIQ RLVPDSDVEE
     LLQILDAMDI CARDLSSGTM VDIPALIKTD SLQRSWADEE DEVMVYGGVR IVPVEHLTPF
     PCGIFHKVQV NLCRWIHQQS AEGDADIRLW VSGCRIANRG AELLVLLVNH GQGIEVQVRG
     LETEKIKCCL LLDSVCSTIE TVMATTLPGL LTVKHYLSPQ QLREHHEPVM VYQPRDFFRA
     QTLKESSLTN TMGGYKESFS SITCFGCHDV YSQASLGMDI HASDLSLLTR RKLSRLLDPP
     DPMGKDWCLL AMNLGLPDMV AKHNVNNRAS RDFLPSPVHA LLQEWTSYPE STVGILISKL
     RELGRRDAAD FLLKASSVFK INLDGNGQEA YASSCNSGTS YNSISSVVSR RDSHAWTPLY
     DL
//
ID   RHG33_MOUSE             Reviewed;        1305 AA.
AC   Q80YF9; Q6P7W6;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Rho GTPase-activating protein 33;
DE   AltName: Full=Rho-type GTPase-activating protein 33;
DE   AltName: Full=Sorting nexin-26;
DE   AltName: Full=Tc10/CDC42 GTPase-activating protein;
GN   Name=Arhgap33; Synonyms=Snx26, Tcgap;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP   INDUCTION, INTERACTION WITH CDC42 AND RHOQ, AND POSSIBLE FUNCTION.
RC   TISSUE=Adipocyte;
RX   MEDLINE=22658047; PubMed=12773384; DOI=10.1093/emboj/cdg262;
RA   Chiang S.-H., Hwang J., Legendre M., Zhang M., Kimura A.,
RA   Saltiel A.R.;
RT   "TCGAP, a multidomain Rho GTPase-activating protein involved in
RT   insulin-stimulated glucose transport.";
RL   EMBO J. 22:2679-2691(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 220-1305.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1188, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: May be involved in several stages of intracellular
CC       trafficking (By similarity). Could play an important role in the
CC       regulation of glucose transport by insulin. May act as a
CC       downstream effector of RHOQ/TC10 in the regulation of insulin-
CC       stimulated glucose transport.
CC   -!- SUBUNIT: Specifically interacts with CDC42 and RHOQ/TC10 through
CC       its Rho-GAP domain.
CC   -!- INTERACTION:
CC       P39688:Fyn; NbExp=1; IntAct=EBI-1210140, EBI-524514;
CC   -!- SUBCELLULAR LOCATION: Cell membrane. Note=Translocates to the
CC       plasma membrane in response to insulin in adipocytes.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and testis. Also
CC       expressed in white adipose tissue (WAT) and muscle at a low level.
CC   -!- INDUCTION: Dramatically induced during adipocyte differentiation.
CC   -!- DOMAIN: The N-terminal PX domain interacts specifically with
CC       phosphatidylinositol-(4,5)-biphosphate.
CC   -!- SIMILARITY: Belongs to the PX domain-containing GAP family.
CC   -!- SIMILARITY: Contains 1 PX (phox homology) domain.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH61471.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY217764; AAO89073.1; -; mRNA.
DR   EMBL; BC065086; AAH65086.1; -; mRNA.
DR   EMBL; BC065166; AAH65166.1; -; mRNA.
DR   EMBL; BC066047; AAH66047.1; -; mRNA.
DR   EMBL; BC061471; AAH61471.1; ALT_INIT; mRNA.
DR   IPI; IPI00265207; -.
DR   RefSeq; NP_839983.1; NM_178252.2.
DR   UniGene; Mm.190704; -.
DR   ProteinModelPortal; Q80YF9; -.
DR   SMR; Q80YF9; 85-275, 335-535.
DR   IntAct; Q80YF9; 1.
DR   STRING; Q80YF9; -.
DR   PhosphoSite; Q80YF9; -.
DR   PRIDE; Q80YF9; -.
DR   Ensembl; ENSMUST00000044338; ENSMUSP00000038412; ENSMUSG00000036882.
DR   GeneID; 233071; -.
DR   KEGG; mmu:233071; -.
DR   UCSC; uc009geq.1; mouse.
DR   CTD; 233071; -.
DR   MGI; MGI:2673998; Arhgap33.
DR   GeneTree; ENSGT00600000084016; -.
DR   HOVERGEN; HBG079688; -.
DR   InParanoid; Q80YF9; -.
DR   OMA; GPPCGIP; -.
DR   OrthoDB; EOG4NP730; -.
DR   PhylomeDB; Q80YF9; -.
DR   NextBio; 381531; -.
DR   ArrayExpress; Q80YF9; -.
DR   Bgee; Q80YF9; -.
DR   CleanEx; MM_SNX26; -.
DR   Genevestigator; Q80YF9; -.
DR   GermOnline; ENSMUSG00000036882; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0030675; F:Rac GTPase activator activity; IDA:MGI.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR001683; Phox.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:3.30.1520.10; PX; 1.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF64268; PX; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50195; PX; FALSE_NEG.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; GTPase activation; Membrane; Phosphoprotein;
KW   Protein transport; SH3 domain; Transport.
FT   CHAIN         1   1305       Rho GTPase-activating protein 33.
FT                                /FTId=PRO_0000056722.
FT   DOMAIN       83    192       PX; atypical.
FT   DOMAIN      210    272       SH3.
FT   DOMAIN      339    534       Rho-GAP.
FT   COMPBIAS    150    153       Poly-Pro.
FT   COMPBIAS    701    721       Poly-Ser.
FT   COMPBIAS    909    913       Poly-Pro.
FT   COMPBIAS   1158   1161       Poly-Pro.
FT   COMPBIAS   1202   1207       Poly-Ser.
FT   COMPBIAS   1284   1291       Poly-Pro.
FT   MOD_RES     594    594       Phosphoserine.
FT   MOD_RES    1188   1188       Phosphotyrosine.
FT   CONFLICT    357    357       R -> C (in Ref. 2; AAH61471).
SQ   SEQUENCE   1305 AA;  139801 MW;  AA8723BDF4A3CBB6 CRC64;
     MLQAQKQSDP ILPWGASWAG RGQTLRARST DSLDGPGEGS VQPVPTTGGP GTKGKPGKRL
     SAPRGPFPRL ADCAHFHYEN VDFGHIQLLL SPEREGPSLS GENELVFGVQ VTCQGRSWPV
     LRSYDDFRSL DAHLHRCIFD RRFSCLPELP PPPEGTRAAQ MLVPLLLQYL ETLSGLVDSN
     LNCGPVLTWM ELDNHGRRLL LSEEASLNIP AVAAAHVVKR YTAQAPDELS FEVGDIVSVI
     DMPPTEDRSW WRGKRGFQVG FFPSECVELF TERPGPGLKA DADSPLCGIP APQGISSLTS
     AVPRPRGKLA GLLRTFMRSR PSRQRLRQRG ILRQRVFGCD LGEHLSNSGQ DVPQVLRCCS
     EFIEAHGVVD GIYRLSGVSS NIQRLRHEFD SERIPELSGP AFLQDIHSVS SLCKLYFREL
     PNPLLTYQLY GKFSEAMSVP GEEERLVRVH DVIQQLPPPH YRTLEYLLRH LARMARHSAN
     TSMHARNLAI VWAPNLLRSM ELESVGLGGA AAFREVRVQS VVVEFLLTHV EVLFSDTFTS
     AGLDPAGRCL LPRPKSLAGS SPSTRLLTLE EAQARTQGRL GTPTEPTTPK TPASPVERRK
     RERAEKQRKP GGSSWKTFFA LGRGPSIPRK KPLPWLGGSR APPQPSGSRP DTVTLRSAKS
     EESLSSQASG AGLQRLHRLR RPHSSSDAFP VGPAPAGSCE SLSSSSSSSS SSSSSSSSES
     SAGGLGPLSG SPSHRTSAWL DDGDDLDFSP PRCLEGLRGL DFDPLTFRCS SPTPGDPAPP
     ASPAPPASAS AFPPRATPQA LSPHGPTKPA SPTALDISEP LAVSVPPAVL ELLGAGGTPA
     SATPTPALSP HLIPLLLRGA EAQLSDTCQQ EISSKLAPTR GAPGQQSPGG MDSPLLPPPL
     PLLRPGGAPP PPPKNPARLM ALALAERAQQ VAEQQSQQEQ GGTPPAPHSP FRRSLSLEVG
     GEPVGTSGSG IHPPSLAHPG AWAPGPPPYL PRQQSDGSLV RSQRPLGTSR RSPRGPSQVS
     AHLRASGAYR DAPEMAAQSP CSVPSQGSNP SFFSTPRECL PPFLGVPKQG LYSLGPPSFP
     PSSPAPVWRN SLGAPSALDR GENLYYEIGV GEGTSYSGPS RSWSPFRSMP PDRHNASYGM
     LGQSPPLHRS PDFLLSYPPP PSCFPPEHLT HSVSQRLARR PTRPEPLYVN LALGPRGPSP
     ASSSSSSPPA HPRSRSDPGP PVPRLPQKQR APWGPHTPHR VPGPWGSPEP FLLYRPAPPS
     YGRGGEVRGS LYRNGGHRGE GAGPPPPYPT PSWSLHSEGQ TRSYC
//
ID   R12BA_MOUSE             Reviewed;         836 AA.
AC   Q80YR9; B1AZ74; Q7TQK7; Q8CD70; Q9CRY6;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=RNA-binding protein 12B-A;
DE   AltName: Full=RNA-binding motif protein 12B-A;
GN   Name=Rbm12ba; Synonyms=Rbm12b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Limb, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-82 AND 114-836.
RC   STRAIN=C57BL/6J; TISSUE=Head, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277 AND SER-279, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SIMILARITY: Contains 4 RRM (RNA recognition motif) domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH54081.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK031339; BAC27354.1; -; mRNA.
DR   EMBL; AL929413; CAM27695.1; -; Genomic_DNA.
DR   EMBL; BC050844; AAH50844.1; -; mRNA.
DR   EMBL; BC054081; AAH54081.1; ALT_INIT; mRNA.
DR   EMBL; AK013872; BAB29027.1; -; mRNA.
DR   IPI; IPI00134417; -.
DR   RefSeq; NP_082502.2; NM_028226.2.
DR   UniGene; Mm.430709; -.
DR   HSSP; Q8R4X3; 2CQP.
DR   ProteinModelPortal; Q80YR9; -.
DR   SMR; Q80YR9; 3-80, 148-240, 280-372, 400-484, 762-834.
DR   PhosphoSite; Q80YR9; -.
DR   PRIDE; Q80YR9; -.
DR   Ensembl; ENSMUST00000050069; ENSMUSP00000053555; ENSMUSG00000046667.
DR   Ensembl; ENSMUST00000069128; ENSMUSP00000064195; ENSMUSG00000046667.
DR   GeneID; 72397; -.
DR   KEGG; mmu:72397; -.
DR   UCSC; uc008san.1; mouse.
DR   CTD; 72397; -.
DR   MGI; MGI:1919647; Rbm12b.
DR   eggNOG; roNOG12931; -.
DR   GeneTree; ENSGT00550000074195; -.
DR   HOGENOM; HBG282019; -.
DR   HOVERGEN; HBG057691; -.
DR   InParanoid; Q80YR9; -.
DR   OMA; QEHFRRP; -.
DR   OrthoDB; EOG4NKBVV; -.
DR   PhylomeDB; Q80YR9; -.
DR   NextBio; 336186; -.
DR   ArrayExpress; Q80YR9; -.
DR   Bgee; Q80YR9; -.
DR   Genevestigator; Q80YR9; -.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 5.
DR   Pfam; PF00076; RRM_1; 3.
DR   SMART; SM00360; RRM; 4.
DR   PROSITE; PS50102; RRM; 4.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Repeat; RNA-binding.
FT   CHAIN         1    836       RNA-binding protein 12B-A.
FT                                /FTId=PRO_0000273368.
FT   DOMAIN      154    229       RRM 1.
FT   DOMAIN      283    359       RRM 2.
FT   DOMAIN      401    478       RRM 3.
FT   DOMAIN      760    836       RRM 4.
FT   MOD_RES     277    277       Phosphoserine.
FT   MOD_RES     279    279       Phosphoserine.
FT   CONFLICT    592    592       S -> P (in Ref. 2; AAH50844).
FT   CONFLICT    605    605       R -> H (in Ref. 2; AAH50844).
FT   CONFLICT    637    637       E -> Q (in Ref. 2; AAH50844).
SQ   SEQUENCE   836 AA;  96596 MW;  C39C6A45A6BA606A CRC64;
     MAVVIRLLGL PFIAGPVDIR HFFKGLTIPD GGVHIIGGKV GEAFIIFATD EDARRAISRS
     GGFIKDSSVE LFLSSKVEMQ KTIEMKRTAR VGRGRPGSGA SGVGNVYHFS DALKEEESYS
     GYGSSVNRDA GFHTNGTGLD LRPRKTRPLK AENPYLFLRG LPYLVNEDDV RVFFSGLCVD
     GVILLKHHDG RNNGDAIVKF ASCVDASGGL KCHRSFMGSR FIEVMQGSEQ QWIEFGGTAT
     EGGDTPRMRS EEHSPSRRIN GRHFRKRSHS KSPRARSRSP LGFYVHLKNL SLNTNKRDLR
     NLFRDTDLTN DQIKFVYKDE RRTRYAFVMF KNQKDYNTAL GLHKTVLQYR PVLIDPVSRK
     EMVRIIECYE KKRPESLEKE RPGRVSQKYS QEGFSGSGQK LCIYIRNLPF DVTKGEVQKF
     FADFSLVEDD IYLLCDDKGV GLGEALVRFK SEEQAMKAER LNRQRFLGIE VLLRLISEEQ
     MQEFGVKSSW LSNERTQACS RSHDGDDCSC LFDLKDPSSC SFGQSESLRY HPKDLRKMGH
     FKHPQGYFRQ SDRRSPEDFR HSPEDYRHPW EEHTSHSREE DWRLPLEDWK WSQEDDFRQC
     HEKDRRQLRS PWEEDFRRPS QEHFRRSYQE HIRQPPEEHF RRSREEDFRH VADEDFRQAS
     DEDFRTSQED LRYPTDEDFR RVSVEDLREV PEKDLRLPKN FRSPGEEFWT PPDFRGQHPF
     GNFDHLQGGK FDFEKYKFGS FPDAKVTSDL NLNCVSDKII PVKISNLPFK ANASEILDFF
     HGYKVIPDSV SLQYNEQGLP IGEAIVAMTN YNEALAAVKD LSGRPVGPRK VKLSLL
//
ID   AFAP1_MOUSE             Reviewed;         731 AA.
AC   Q80YS6; Q3UGX1; Q6ZPE4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Actin filament-associated protein 1;
DE   AltName: Full=110 kDa actin filament-associated protein;
DE            Short=AFAP-110;
GN   Name=Afap1; Synonyms=Kiaa3018;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Melanocyte, Placenta, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-669, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-547, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Can cross-link actin filaments into both network and
CC       bundle structures. May modulate changes in actin filament
CC       integrity and induce lamellipodia formation. May function as an
CC       adapter molecule that links other proteins, such as SRC and PKC to
CC       the actin cytoskeleton (By similarity).
CC   -!- SUBUNIT: Monomer and homomultimer. Interacts via its C-terminus
CC       with F-actin; probably involving AFAP1 multimers. Interacts with
CC       activated SRC SH3-SH2 domains. Interacts via its PH 1 domain with
CC       PRKCA, PRKCB and PRKCI (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Note=Localizes with stress fibers in quiescent cells, concentrated
CC       in cell motility structures such as lamellipodia, filopodia and
CC       membrane ruffles (By similarity).
CC   -!- PTM: Phosphorylated on tyrosine residues by SRC (By similarity).
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98293.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK129483; BAC98293.1; ALT_INIT; mRNA.
DR   EMBL; AK147706; BAE28086.1; -; mRNA.
DR   EMBL; AK148000; BAE28280.1; -; mRNA.
DR   EMBL; AK161385; BAE36364.1; -; mRNA.
DR   EMBL; BC050814; AAH50814.1; -; mRNA.
DR   IPI; IPI00467327; -.
DR   RefSeq; NP_081649.1; NM_027373.2.
DR   UniGene; Mm.125167; -.
DR   HSSP; Q8N4X5; 2COF.
DR   ProteinModelPortal; Q80YS6; -.
DR   SMR; Q80YS6; 156-247, 344-448.
DR   STRING; Q80YS6; -.
DR   PhosphoSite; Q80YS6; -.
DR   PRIDE; Q80YS6; -.
DR   Ensembl; ENSMUST00000064571; ENSMUSP00000067779; ENSMUSG00000029094.
DR   GeneID; 70292; -.
DR   KEGG; mmu:70292; -.
DR   UCSC; uc008xej.1; mouse.
DR   CTD; 70292; -.
DR   MGI; MGI:1917542; Afap1.
DR   HOGENOM; HBG443857; -.
DR   HOVERGEN; HBG106875; -.
DR   InParanoid; Q80YS6; -.
DR   OMA; KVIKEAY; -.
DR   OrthoDB; EOG4J117M; -.
DR   PhylomeDB; Q80YS6; -.
DR   NextBio; 331322; -.
DR   ArrayExpress; Q80YS6; -.
DR   Bgee; Q80YS6; -.
DR   CleanEx; MM_AFAP1; -.
DR   Genevestigator; Q80YS6; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Pfam; PF00169; PH; 2.
DR   SMART; SM00233; PH; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
PE   1: Evidence at protein level;
KW   Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW   Repeat; SH3-binding.
FT   CHAIN         1    731       Actin filament-associated protein 1.
FT                                /FTId=PRO_0000317659.
FT   DOMAIN      152    248       PH 1.
FT   DOMAIN      348    442       PH 2.
FT   REGION      595    638       Interaction with F-actin (By similarity).
FT   COILED      558    649       Potential.
FT   MOTIF        70     73       SH3-binding (By similarity).
FT   MOTIF        93     96       SH2-binding 1 (By similarity).
FT   MOTIF       452    457       SH2-binding 2 (By similarity).
FT   COMPBIAS     59    105       Pro-rich.
FT   MOD_RES     278    278       Phosphoserine (By similarity).
FT   MOD_RES     279    279       Phosphoserine (By similarity).
FT   MOD_RES     283    283       Phosphoserine (By similarity).
FT   MOD_RES     284    284       Phosphoserine (By similarity).
FT   MOD_RES     337    337       Phosphoserine (By similarity).
FT   MOD_RES     338    338       Phosphothreonine (By similarity).
FT   MOD_RES     342    342       Phosphothreonine (By similarity).
FT   MOD_RES     343    343       Phosphoserine (By similarity).
FT   MOD_RES     344    344       Phosphoserine (By similarity).
FT   MOD_RES     547    547       Phosphothreonine.
FT   MOD_RES     664    664       Phosphothreonine (By similarity).
FT   MOD_RES     665    665       Phosphoserine (By similarity).
FT   MOD_RES     666    666       Phosphoserine (By similarity).
FT   MOD_RES     669    669       Phosphoserine.
FT   MOD_RES     680    680       Phosphoserine (By similarity).
FT   MOD_RES     687    687       Phosphothreonine (By similarity).
FT   MOD_RES     688    688       Phosphoserine (By similarity).
FT   CONFLICT     43     43       G -> R (in Ref. 2; BAE28086).
FT   CONFLICT     52     52       K -> R (in Ref. 2; BAE28086).
FT   CONFLICT    232    232       S -> G (in Ref. 1; BAC98293).
FT   CONFLICT    249    249       G -> D (in Ref. 1; BAC98293).
SQ   SEQUENCE   731 AA;  80615 MW;  58D3D31BED5C2FCD CRC64;
     MEELIVELRL FLELLDHEYL TSTVREKKAV LTNILLRLQS SKGFEVKDHA QKAEANNLPA
     PPQMPLPEIP QPWLPPDSGP PPLPTSSLPE GYYEEAVPLS PGKAPEYITS NYDSDAMSSS
     YESYDEEEED GKGKKTRHQW PSEEASMDLV KDAKICAFLL RKKRFGQWTK LLCVIKDTKL
     LCYKSSKDQQ PQMELPLQGC SITYIPRDSK KKKHELKITQ QGTDPLVLAV QSKEQAEQWL
     KVIKEAYSGC SGPVDPECSP PPSTSAPVNK AELEKKLSSE RPSSDGEGGV ENGVTTCNGK
     EQAKRKKPSK SEAKGTVSKV TGKKITKIIG LGKKKPSTDE QTSSAEEDVP TCGYLNVLSN
     SRWRERWCRV KDSKLILHKD RADLKTHLVS IPLRGCEVIP GLDSKHPLTF RLLRNGQEVA
     VLEASSSEDM GRWIGILLAE TGSSTDPGAL HYDYIDVEMS ANVIQTAKQT FCFMNRRAVS
     TSPYLGSLSN GYAHPSGTAL HYDDVPCVNG SLKNKKPPAS SNGVPVKGKA PSSQQKKVET
     AGGVKRTASN AEQYKYGKNR VEADAKRLQS KEEELLKRKE ALRNRLAQLR KERKDLRAAI
     EVNAGRKTQA ALEDKLKRLE EECKQREAER VSLELELTEV KESLKKALAG GVTLGLAIEP
     RSGTSSPQSP VFRHRTLENS PISSCDTSDA EGPLPVNSAA VLKKSQPSSG SSPCRGHVLQ
     KAKEWELKNG T
//
ID   TENA_MOUSE              Reviewed;        2110 AA.
AC   Q80YX1; Q64706; Q80YX2;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Tenascin;
DE            Short=TN;
DE   AltName: Full=Hexabrachion;
DE   AltName: Full=Tenascin-C;
DE            Short=TN-C;
DE   Flags: Precursor;
GN   Name=Tnc; Synonyms=Hxb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=GRS; TISSUE=Mammary tumor;
RX   MEDLINE=92009211; PubMed=1717349; DOI=10.1016/0378-1119(91)90248-A;
RA   Saga Y., Tsukamoto T., Jing N., Kusakabe M., Sakakura T.;
RT   "Murine tenascin: cDNA cloning, structure and temporal expression of
RT   isoforms.";
RL   Gene 104:177-185(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5), DEVELOPMENTAL STAGE,
RP   AND GLYCOSYLATION.
RC   STRAIN=NMRI X 129; TISSUE=Embryo;
RX   MEDLINE=91107734; PubMed=1703162; DOI=10.1083/jcb.112.2.355;
RA   Weller A., Beck S., Ekblom P.;
RT   "Amino acid sequence of mouse tenascin and differential expression of
RT   two tenascin isoforms during embryogenesis.";
RL   J. Cell Biol. 112:355-362(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16553788; DOI=10.1111/j.1460-9568.2006.04657.x;
RA   Morellini F., Schachner M.;
RT   "Enhanced novelty-induced activity, reduced anxiety, delayed
RT   resynchronization to daylight reversal and weaker muscle strength in
RT   tenascin-C-deficient mice.";
RL   Eur. J. Neurosci. 23:1255-1268(2006).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1394, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Plasma;
RX   PubMed=16944957; DOI=10.1021/pr060186m;
RA   Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J.,
RA   Gevaert K.;
RT   "Proteome-wide characterization of N-glycosylation events by diagonal
RT   chromatography.";
RL   J. Proteome Res. 5:2438-2447(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70 AND SER-72, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Extracellular matrix protein implicated in guidance of
CC       migrating neurons as well as axons during development, synaptic
CC       plasticity as well as neuronal regeneration. Promotes neurite
CC       outgrowth when provided to neurons in culture. May play a role in
CC       supporting the growth of epithelial tumors. Ligand for integrins
CC       alpha-8/beta-1, alpha-9/beta-1, alpha-V/beta-3 and alpha-V/beta-6.
CC   -!- SUBUNIT: Homohexamer; disulfide-linked. A homotrimer may be formed
CC       in the triple coiled-coil region and may be stabilized by
CC       disulfide rings at both ends. Two of such half-hexabrachions may
CC       be disulfide linked within the central globule. Interacts with
CC       CSPG4 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q80YX1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80YX1-2; Sequence=VSP_052147;
CC       Name=3;
CC         IsoId=Q80YX1-3; Sequence=VSP_052146;
CC       Name=4;
CC         IsoId=Q80YX1-4; Sequence=VSP_052145;
CC       Name=5;
CC         IsoId=Q80YX1-5; Sequence=VSP_052144;
CC   -!- TISSUE SPECIFICITY: High levels of isoform 2 in lung and brain of
CC       newborn mice. High levels of isoform 5 in thymus, moderate levels
CC       in brain of newborn and adult mice. Low level of isoform 2 in
CC       adult brain.
CC   -!- DEVELOPMENTAL STAGE: In kidney, isoform 2 is expressed at birth
CC       and isoform 5 at 2 weeks of age. In intestine, isoform 5 is
CC       expressed in day 13 embryos and isoform 2 at birth. In cerebellum,
CC       high levels of isoform 2 in day 17 embryos are down-regulated to
CC       moderate levels in newborn mice and undetectable levels in adult
CC       mice. Similarly, moderate levels of isoform 2 expressed in
CC       cerebrum of day 17 embryos are gradually down-regulated to
CC       undetectable levels in adult mice.
CC   -!- PTM: N-glycosylated.
CC   -!- DISRUPTION PHENOTYPE: Mice show enhanced novelty-induced activity,
CC       reduced anxiety, delayed resynchronization to daylight reversal
CC       and weaker muscle strength.
CC   -!- SIMILARITY: Belongs to the tenascin family.
CC   -!- SIMILARITY: Contains 12 EGF-like domains.
CC   -!- SIMILARITY: Contains 1 fibrinogen C-terminal domain.
CC   -!- SIMILARITY: Contains 14 fibronectin type-III domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D90343; BAA14355.1; -; mRNA.
DR   EMBL; X56304; CAA39751.1; -; mRNA.
DR   EMBL; AL732556; CAD83047.1; -; Genomic_DNA.
DR   EMBL; AL732556; CAD83048.1; -; Genomic_DNA.
DR   IPI; IPI00403938; -.
DR   IPI; IPI00420656; -.
DR   IPI; IPI00785310; -.
DR   IPI; IPI00785346; -.
DR   IPI; IPI00785360; -.
DR   PIR; JQ1322; JQ1322.
DR   RefSeq; NP_035737.2; NM_011607.3.
DR   UniGene; Mm.454219; -.
DR   HSSP; P24821; 1TEN.
DR   ProteinModelPortal; Q80YX1; -.
DR   SMR; Q80YX1; 207-1339, 1346-2098.
DR   STRING; Q80YX1; -.
DR   PhosphoSite; Q80YX1; -.
DR   PRIDE; Q80YX1; -.
DR   Ensembl; ENSMUST00000030056; ENSMUSP00000030056; ENSMUSG00000028364.
DR   Ensembl; ENSMUST00000070019; ENSMUSP00000065512; ENSMUSG00000028364.
DR   Ensembl; ENSMUST00000107372; ENSMUSP00000102995; ENSMUSG00000028364.
DR   Ensembl; ENSMUST00000107374; ENSMUSP00000102997; ENSMUSG00000028364.
DR   Ensembl; ENSMUST00000107375; ENSMUSP00000102998; ENSMUSG00000028364.
DR   Ensembl; ENSMUST00000107377; ENSMUSP00000103000; ENSMUSG00000028364.
DR   Ensembl; ENSMUST00000107379; ENSMUSP00000103002; ENSMUSG00000028364.
DR   GeneID; 21923; -.
DR   KEGG; mmu:21923; -.
DR   UCSC; uc008the.1; mouse.
DR   CTD; 21923; -.
DR   MGI; MGI:101922; Tnc.
DR   eggNOG; roNOG09424; -.
DR   HOGENOM; HBG446404; -.
DR   HOVERGEN; HBG008949; -.
DR   InParanoid; Q80YX1; -.
DR   OMA; YTLRIFA; -.
DR   OrthoDB; EOG4MSCX9; -.
DR   PhylomeDB; Q80YX1; -.
DR   ArrayExpress; Q80YX1; -.
DR   Bgee; Q80YX1; -.
DR   CleanEx; MM_TNC; -.
DR   Genevestigator; Q80YX1; -.
DR   GermOnline; ENSMUSG00000028364; Mus musculus.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0005102; F:receptor binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0060739; P:mesenchymal-epithelial cell signaling involved in prostate gland development; IMP:MGI.
DR   GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR   GO; GO:0060740; P:prostate gland epithelium morphogenesis; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR002181; Fibrinogen_a/b/g_C.
DR   InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR   InterPro; IPR014715; Fibrinogen_a/b/g_C_2.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Gene3D; G3DSA:3.90.215.10; Fibrinogen_a/b/g_C_1; 1.
DR   Gene3D; G3DSA:4.10.530.10; Fibrinogen_a/b/g_C_2; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 14.
DR   Pfam; PF07974; EGF_2; 14.
DR   Pfam; PF00147; Fibrinogen_C; 1.
DR   Pfam; PF00041; fn3; 14.
DR   SMART; SM00181; EGF; 12.
DR   SMART; SM00186; FBG; 1.
DR   SMART; SM00060; FN3; 14.
DR   SUPFAM; SSF56496; Fibrinogen_a/b/g_C; 1.
DR   SUPFAM; SSF49265; FN_III-like; 14.
DR   PROSITE; PS00022; EGF_1; 15.
DR   PROSITE; PS01186; EGF_2; 14.
DR   PROSITE; PS50026; EGF_3; 5.
DR   PROSITE; PS00514; FIBRINOGEN_C_1; FALSE_NEG.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR   PROSITE; PS50853; FN3; 14.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Coiled coil; Disulfide bond;
KW   EGF-like domain; Extracellular matrix; Glycoprotein; Phosphoprotein;
KW   Repeat; Secreted; Signal.
FT   SIGNAL        1     22       By similarity.
FT   CHAIN        23   2110       Tenascin (By similarity).
FT                                /FTId=PRO_0000248607.
FT   DOMAIN      174    185       EGF-like 1; incomplete.
FT   DOMAIN      186    216       EGF-like 2.
FT   DOMAIN      217    247       EGF-like 3.
FT   DOMAIN      248    279       EGF-like 4.
FT   DOMAIN      280    310       EGF-like 5.
FT   DOMAIN      311    341       EGF-like 6.
FT   DOMAIN      342    372       EGF-like 7.
FT   DOMAIN      373    403       EGF-like 8.
FT   DOMAIN      404    434       EGF-like 9.
FT   DOMAIN      435    465       EGF-like 10.
FT   DOMAIN      466    496       EGF-like 11.
FT   DOMAIN      497    527       EGF-like 12.
FT   DOMAIN      528    558       EGF-like 13.
FT   DOMAIN      559    589       EGF-like 14.
FT   DOMAIN      590    621       EGF-like 15.
FT   DOMAIN      622    710       Fibronectin type-III 1.
FT   DOMAIN      713    801       Fibronectin type-III 2.
FT   DOMAIN      802    891       Fibronectin type-III 3.
FT   DOMAIN      892    983       Fibronectin type-III 4.
FT   DOMAIN      984   1071       Fibronectin type-III 5.
FT   DOMAIN     1073   1164       Fibronectin type-III 6.
FT   DOMAIN     1166   1253       Fibronectin type-III 7.
FT   DOMAIN     1257   1344       Fibronectin type-III 8.
FT   DOMAIN     1348   1435       Fibronectin type-III 9.
FT   DOMAIN     1437   1526       Fibronectin type-III 10.
FT   DOMAIN     1528   1617       Fibronectin type-III 11.
FT   DOMAIN     1618   1706       Fibronectin type-III 12.
FT   DOMAIN     1707   1794       Fibronectin type-III 13.
FT   DOMAIN     1795   1882       Fibronectin type-III 14.
FT   DOMAIN     1884   2099       Fibrinogen C-terminal.
FT   COILED      118    142       Potential.
FT   MOD_RES      70     70       Phosphoserine.
FT   MOD_RES      72     72       Phosphoserine.
FT   CARBOHYD     38     38       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    166    166       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    184    184       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    327    327       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    788    788       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1018   1018       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1079   1079       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1093   1093       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1119   1119       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1184   1184       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1210   1210       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1275   1275       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1301   1301       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1354   1354       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1364   1364       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1394   1394       N-linked (GlcNAc...).
FT   CARBOHYD   1443   1443       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1718   1718       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1969   1969       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2071   2071       N-linked (GlcNAc...) (Potential).
FT   DISULFID    190    200       By similarity.
FT   DISULFID    194    205       By similarity.
FT   DISULFID    207    216       By similarity.
FT   DISULFID    221    231       By similarity.
FT   DISULFID    225    236       By similarity.
FT   DISULFID    238    247       By similarity.
FT   DISULFID    252    263       By similarity.
FT   DISULFID    256    268       By similarity.
FT   DISULFID    270    279       By similarity.
FT   DISULFID    284    294       By similarity.
FT   DISULFID    288    299       By similarity.
FT   DISULFID    301    310       By similarity.
FT   DISULFID    315    325       By similarity.
FT   DISULFID    319    330       By similarity.
FT   DISULFID    332    341       By similarity.
FT   DISULFID    346    356       By similarity.
FT   DISULFID    350    361       By similarity.
FT   DISULFID    363    372       By similarity.
FT   DISULFID    377    387       By similarity.
FT   DISULFID    381    392       By similarity.
FT   DISULFID    394    403       By similarity.
FT   DISULFID    408    418       By similarity.
FT   DISULFID    412    423       By similarity.
FT   DISULFID    425    434       By similarity.
FT   DISULFID    439    449       By similarity.
FT   DISULFID    443    454       By similarity.
FT   DISULFID    456    465       By similarity.
FT   DISULFID    470    480       By similarity.
FT   DISULFID    474    485       By similarity.
FT   DISULFID    487    496       By similarity.
FT   DISULFID    501    511       By similarity.
FT   DISULFID    505    516       By similarity.
FT   DISULFID    518    527       By similarity.
FT   DISULFID    532    542       By similarity.
FT   DISULFID    536    547       By similarity.
FT   DISULFID    549    558       By similarity.
FT   DISULFID    563    573       By similarity.
FT   DISULFID    567    578       By similarity.
FT   DISULFID    580    589       By similarity.
FT   DISULFID    594    604       By similarity.
FT   DISULFID    598    609       By similarity.
FT   DISULFID    611    620       By similarity.
FT   VAR_SEQ    1072   1616       Missing (in isoform 5).
FT                                /FTId=VSP_052144.
FT   VAR_SEQ    1163   1616       Missing (in isoform 4).
FT                                /FTId=VSP_052145.
FT   VAR_SEQ    1254   1616       Missing (in isoform 3).
FT                                /FTId=VSP_052146.
FT   VAR_SEQ    1436   1526       Missing (in isoform 2).
FT                                /FTId=VSP_052147.
FT   CONFLICT    202    202       D -> E (in Ref. 2; CAA39751).
FT   CONFLICT    318    318       D -> S (in Ref. 2; CAA39751).
FT   CONFLICT   1019   1019       Y -> S (in Ref. 2; CAA39751).
FT   CONFLICT   1025   1025       Q -> H (in Ref. 2; CAA39751).
FT   CONFLICT   1306   1306       G -> S (in Ref. 2; CAA39751).
SQ   SEQUENCE   2110 AA;  231807 MW;  A1FEA96F8BC2FE51 CRC64;
     MGAVTWLLPG IFLALFALTP EGGVLKKIIR HKRESGLNMT LPEENQPVVF NHIYNIKLPM
     GSQCSVDLES ASGEKDLTPT PESSGSFQEH TVDGENQIVF THRINIPRRA CGCAAAPDVK
     ELLSRLEELE LLVSSLREQC TMGTGCCLQP AEGRLDTRPF CSGRGNFSAE GCGCVCEPGW
     KGPNCSEPDC PGNCNLRGQC LDGQCICDEG FTGEDCSQLA CPNDCNDQGR CVNGVCVCFE
     GYAGPDCGLE VCPVPCSEEH GMCVDGRCVC KDGFAGEDCN EPLCLNNCYN RGRCVENECV
     CDEGFTGEDC SELICPNDCF DRGRCINGTC YCEEGFTGED CGELTCPNDC QGRGQCEEGQ
     CVCNEGFAGA DCSEKRCPAD CHHRGRCLNG QCECDDGFTG ADCGDLQCPN GCSGHGRCVN
     GQCVCDEGYT GEDCSQRRCP NDCHNRGLCV QGKCICEQGF KGFDCSEMSC PNDCHQHGRC
     VNGMCICDDD YTGEDCRDRR CPRDCSQRGR CVDGQCICED GFTGPDCAEL SCPSDCHGHG
     RCVNGQCICH EGFTGKDCKE QRCPSDCHGQ GRCEDGQCIC HEGFTGLDCG QRSCPNDCSN
     QGQCVSGRCI CNEGYTGIDC SEVSPPKDLI VTEVTEETVN LAWDNEMRVT EYLIMYTPTH
     ADGLEMQFRV PGDQTSTTIR ELEPGVEYFI RVFAILENKR SIPVSARVAT YLPAPEGLKF
     KSIKETSVEV EWDPLDIAFE TWEIIFRNMN KEDEGEITKS LRRPETSYRQ TGLAPGQEYE
     ISLHIVKNNT RGPGLKKVTT TRLDAPSHIE VKDVTDTTAL ITWFKPLAEI DSIELSYGIK
     DVPGDRTTID LTHEDNQYSI GNLRPDTEYE VSLISRRVDM ASNPAKETFI TGLDAPRNLR
     RVSQTDNSIT LEWRNVKADI DSYRIKYAPI SGGDHAEIDV PKSQQATTKT TLTGLRPGTE
     YGIGVSAVKG DKESDPATIN AATEIDAPKD LRVSETTQDS LTFFWTTPLA KFDRYRLNYS
     LPTGQSMEVQ LPKDATSHVL TDLEPGQEYT VLLIAEKGRH KSKPARVKAS TEEVPSLENL
     TVTEAGWDGL RLNWTADDLA YEYFVIQVQE ANNVETAHNF TVPGNLRAAD IPGLKVATSY
     RVSIYGVARG YRTPVLSAET STGTTPNLGE VTVAEVGWDA LTLNWTAPEG AYKNFFIQVL
     EADTTQTVQN LTVPGGLRSV DLPGLKAATR YYITLRGVTQ DFGTAPLSVE VLTEDLPQLG
     GLSVTEVSWD GLTLNWTTDD LAYKHFVVQV QEANNVEAAQ NLTVPGSLRA VDIPGLKADT
     PYRVSIYGVI QGYRTPMLST DVSTAREPEI GNLNVSDVTP KSFNLSWTAT DGIFDMFTIE
     IIDSNRLLQT AEHNISGAER TAHISGLPPS TDFIVYLSGI APSIRTKTIS TTATTEALPL
     LENLTISDTN PYGFTVSWTA SENAFDSFLV TVVDSGKLLD PQEFTLSGTQ RKLELRGLIT
     GIGYEVLVSG FTQGHQTKPL RAETITEAEP EVDNLLVSDA TPDGFRLSWT ADEGIFDSFV
     IRIRDTKKQS EPQEISLPSP ERTRDITGLR EATEYEIELY GISRGRRSQP VSAIATTAMG
     SPKEIMFSDI TENAATVSWR APTAQVESFR ITYVPMTGGA PSMVTVDGTD TETRLVKLTP
     GVEYRVSVIA MKGFEESDPV SGTLITALDG PSGLLIANIT DSEALAMWQP AIATVDSYVI
     SYTGERVPEV TRTVSGNTVE YELHDLEPAT EYILSIFAEK GQQKSSTIAT KFTTDLDSPR
     EFTATEVQSE TALLTWRPPR ASVTGYLLVY ESVDGTVKEV IVGPDTTSYS LADLSPSTHY
     SARIQALSGS LRSKLIQTIF TTIGLLYPFP RDCSQAMLNG DTTSGLYTIY INGDKTQALE
     VYCDMTSDGG GWIVFLRRKN GREDFYRNWK AYAAGFGDRR EEFWLGLDNL SKITAQGQYE
     LRVDLQDHGE SAYAVYDRFS VGDAKSRYKL KVEGYSGTAG DSMNYHNGRS FSTYDKDTDS
     AITNCALSYK GAFWYKNCHR VNLMGRYGDN NHSQGVNWFH WKGHEYSIQF AEMKLRPSNF
     RNLEGRRKRA
//
ID   ASTN2_MOUSE             Reviewed;        1352 AA.
AC   Q80Z10; Q6A031; Q811X9; Q811Y0; Q811Y1; Q811Y2;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=Astrotactin-2;
DE   Flags: Precursor;
GN   Name=Astn2; Synonyms=Kiaa0634;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80Z10-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80Z10-2; Sequence=VSP_028938;
CC   -!- SIMILARITY: Belongs to the astrotactin family.
CC   -!- SIMILARITY: Contains 3 EGF-like domains.
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32265.1; Type=Erroneous initiation;
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DR   EMBL; AK172987; BAD32265.1; ALT_INIT; mRNA.
DR   EMBL; AL691454; CAD62275.2; -; Genomic_DNA.
DR   EMBL; AL691438; CAD62275.2; JOINED; Genomic_DNA.
DR   EMBL; AL691456; CAD62275.2; JOINED; Genomic_DNA.
DR   EMBL; AL691474; CAD62275.2; JOINED; Genomic_DNA.
DR   EMBL; AL691475; CAD62275.2; JOINED; Genomic_DNA.
DR   EMBL; AL713878; CAD62275.2; JOINED; Genomic_DNA.
DR   EMBL; AL731829; CAD62275.2; JOINED; Genomic_DNA.
DR   EMBL; AL691456; CAD62277.2; -; Genomic_DNA.
DR   EMBL; AL691438; CAD62277.2; JOINED; Genomic_DNA.
DR   EMBL; AL691454; CAD62277.2; JOINED; Genomic_DNA.
DR   EMBL; AL691474; CAD62277.2; JOINED; Genomic_DNA.
DR   EMBL; AL691475; CAD62277.2; JOINED; Genomic_DNA.
DR   EMBL; AL713878; CAD62277.2; JOINED; Genomic_DNA.
DR   EMBL; AL731829; CAD62277.2; JOINED; Genomic_DNA.
DR   EMBL; AL691438; CAD62278.2; -; Genomic_DNA.
DR   EMBL; AL691454; CAD62278.2; JOINED; Genomic_DNA.
DR   EMBL; AL691456; CAD62278.2; JOINED; Genomic_DNA.
DR   EMBL; AL691474; CAD62278.2; JOINED; Genomic_DNA.
DR   EMBL; AL691475; CAD62278.2; JOINED; Genomic_DNA.
DR   EMBL; AL713878; CAD62278.2; JOINED; Genomic_DNA.
DR   EMBL; AL731829; CAD62278.2; JOINED; Genomic_DNA.
DR   EMBL; AL691475; CAD62279.2; -; Genomic_DNA.
DR   EMBL; AL691438; CAD62279.2; JOINED; Genomic_DNA.
DR   EMBL; AL691454; CAD62279.2; JOINED; Genomic_DNA.
DR   EMBL; AL691456; CAD62279.2; JOINED; Genomic_DNA.
DR   EMBL; AL691474; CAD62279.2; JOINED; Genomic_DNA.
DR   EMBL; AL713878; CAD62279.2; JOINED; Genomic_DNA.
DR   EMBL; AL731829; CAD62279.2; JOINED; Genomic_DNA.
DR   EMBL; AL731829; CAD62280.2; -; Genomic_DNA.
DR   EMBL; AL691438; CAD62280.2; JOINED; Genomic_DNA.
DR   EMBL; AL691454; CAD62280.2; JOINED; Genomic_DNA.
DR   EMBL; AL691456; CAD62280.2; JOINED; Genomic_DNA.
DR   EMBL; AL691474; CAD62280.2; JOINED; Genomic_DNA.
DR   EMBL; AL691475; CAD62280.2; JOINED; Genomic_DNA.
DR   EMBL; AL713878; CAD62280.2; JOINED; Genomic_DNA.
DR   EMBL; AL691474; CAM23507.1; -; Genomic_DNA.
DR   EMBL; AL691438; CAM23507.1; JOINED; Genomic_DNA.
DR   EMBL; AL691454; CAM23507.1; JOINED; Genomic_DNA.
DR   EMBL; AL691456; CAM23507.1; JOINED; Genomic_DNA.
DR   EMBL; AL691475; CAM23507.1; JOINED; Genomic_DNA.
DR   EMBL; AL713878; CAM23507.1; JOINED; Genomic_DNA.
DR   EMBL; AL731829; CAM23507.1; JOINED; Genomic_DNA.
DR   EMBL; AL713878; CAM24738.1; -; Genomic_DNA.
DR   EMBL; AL691438; CAM24738.1; JOINED; Genomic_DNA.
DR   EMBL; AL691454; CAM24738.1; JOINED; Genomic_DNA.
DR   EMBL; AL691456; CAM24738.1; JOINED; Genomic_DNA.
DR   EMBL; AL691474; CAM24738.1; JOINED; Genomic_DNA.
DR   EMBL; AL691475; CAM24738.1; JOINED; Genomic_DNA.
DR   EMBL; AL731829; CAM24738.1; JOINED; Genomic_DNA.
DR   IPI; IPI00462733; -.
DR   IPI; IPI00869418; -.
DR   RefSeq; NP_996992.1; NM_207109.2.
DR   UniGene; Mm.445312; -.
DR   ProteinModelPortal; Q80Z10; -.
DR   PhosphoSite; Q80Z10; -.
DR   PRIDE; Q80Z10; -.
DR   Ensembl; ENSMUST00000030064; ENSMUSP00000030064; ENSMUSG00000028373.
DR   Ensembl; ENSMUST00000068214; ENSMUSP00000065786; ENSMUSG00000028373.
DR   GeneID; 56079; -.
DR   KEGG; mmu:56079; -.
DR   CTD; 56079; -.
DR   MGI; MGI:1889277; Astn2.
DR   GeneTree; ENSGT00390000003140; -.
DR   HOVERGEN; HBG050597; -.
DR   OrthoDB; EOG4R7V8Z; -.
DR   NextBio; 311878; -.
DR   ArrayExpress; Q80Z10; -.
DR   Bgee; Q80Z10; -.
DR   Genevestigator; Q80Z10; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR020864; MACPF.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF01823; MACPF; 1.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00457; MACPF; 1.
DR   SUPFAM; SSF49265; FN_III-like; 1.
DR   PROSITE; PS00022; EGF_1; FALSE_NEG.
DR   PROSITE; PS01186; EGF_2; FALSE_NEG.
DR   PROSITE; PS50026; EGF_3; FALSE_NEG.
DR   PROSITE; PS50853; FN3; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Membrane; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     51       Potential.
FT   CHAIN        52   1352       Astrotactin-2.
FT                                /FTId=PRO_0000308253.
FT   TOPO_DOM     52    218       Extracellular (Potential).
FT   TRANSMEM    219    239       Helical; (Potential).
FT   TOPO_DOM    240    447       Cytoplasmic (Potential).
FT   TRANSMEM    448    468       Helical; (Potential).
FT   TOPO_DOM    469   1352       Extracellular (Potential).
FT   DOMAIN      523    563       EGF-like 1.
FT   DOMAIN      664    708       EGF-like 2.
FT   DOMAIN      712    764       EGF-like 3.
FT   DOMAIN     1079   1201       Fibronectin type-III.
FT   CARBOHYD    180    180       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    796    796       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1033   1033       N-linked (GlcNAc...) (Potential).
FT   DISULFID    527    539       By similarity.
FT   DISULFID    535    546       By similarity.
FT   DISULFID    548    562       By similarity.
FT   DISULFID    668    681       By similarity.
FT   DISULFID    675    692       By similarity.
FT   DISULFID    694    707       By similarity.
FT   DISULFID    716    728       By similarity.
FT   DISULFID    724    748       By similarity.
FT   DISULFID    750    763       By similarity.
FT   VAR_SEQ     597    600       Missing (in isoform 2).
FT                                /FTId=VSP_028938.
SQ   SEQUENCE   1352 AA;  149390 MW;  76D88651761FB04B CRC64;
     MAAAGARRSP GRGLGLRGRP RLGFHPGPPP PPPPPLLLLF LLLLPPPPLL AGATAAAASR
     EPDSPCRLKT VTVSTLPALR ESDIGWSGAR TGAAAGAGAG TGAGAGAAAA AASAASPGSA
     GSAGTAAESR LLLFVRNELP GRIAVQDDLD NTELPFFTLE MSGTAADISL VHWRQQWLEN
     GTLYFHVSMS SSGQLAQATA PTLQEPSEIV EEQMHILHIS VMGGLIALLL LLLVFTVALY
     AQRRWQKRRR IPQKSASTEA THEIHYIPSV LLGPQARESF RSSRLQTHNS VIGVPIRETP
     ILDDYDYEEE EEPPRRANHV SREDEFGSQM THALDSLGRP GEEKVEFEKK AAAEATQETV
     ESLMQKFKES FRANTPVEIG QLQPASRSST SAGKRKRRNK SRGGISFGRT KGTSGSEADD
     ETQLTFYTEQ YRSRRRSKGL LKSPVNKTAL TLIAVSSCIL AMVCGNQMSC PLTVKVTLHV
     PEHFIADGSS FVVSEGSYLD ISDWLNPAKL SLYYQINATS PWVRDLCGQR TTDACEQLCD
     PDTGECSCHE GYAPDPVHRH LCVRSDWGQS EGPWPYTTLE RGYDLVTGEQ APEKILRSTF
     SLGQGLWLPV SKSFVVPPVE LSINPLASCK TDVLVTEDPA DVREEAMLST YFETINDLLS
     SFGPVRDCSR NNGGCTRNFK CVSDRQVDSS GCVCPEELKP MKDGSGCYDH SKGIDCSDGF
     NGGCEQLCLQ QTLPLPYDTT SSTIFMFCGC VEEYKLAPDG KSCLMLSDVC EGPKCLKPDS
     KFNDTLFGEM LHGYNNRTQH VNQGQVFQMT FRENNFIKDF PQLADGLLVI PLPVEEQCRG
     VLSEPLPDLQ LLTGDIRYDE AMGYPMVQQW RVRSNLYRVK LSTITLSAGF TNVLKILTKE
     SSRDELLSFI QHYGSHYIAE ALYGSELTCI IHFPSKKVQQ QLWLQYQKET TELGSKKELK
     SMPFITYLSG LLTAQMLSDD QLISGVEIRC EEKGRCPSTC HLCRRPGKEQ LSPTPVLLEI
     NRVVPLYTLI QDNGTKEAFK NALMSSYWCS GKGDVIDDWC RCDLSAFDAS GLPNCSPLPQ
     PVLRLSPTVE PSSTVVSLEW VDVQPAIGTK VSDYILQHKK VDEYTDTDLY TGEFLSFADD
     LLSGLGTSCV AAGRSHGEVP EVSIYSVIFK CLEPDGLYKF TLYAVDTRGR HSELSTVTLR
     TACPLVDDNK AEEIADKIYN LYNGYTSGKE QQTAYNTLME VSASMLFRVQ HHYNSHYEKF
     GDFVWRSEDE LGPRKAHLIL RRLERVSSHC SSLLRSAYIQ SRVDTIPYLF CRSEEVRPAG
     MVWYSILKDT KITCEEKMVS MARNTYGETK GR
//
ID   AMGO1_MOUSE             Reviewed;         492 AA.
AC   Q80ZD8; A2AE40; Q69ZQ0; Q8R5D4; Q921U9;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Amphoterin-induced protein 1;
DE   AltName: Full=AMIGO-1;
DE   AltName: Full=Alivin-2;
DE   Flags: Precursor;
GN   Name=Amigo1; Synonyms=Ali2, Amigo, Kiaa1163;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=22529230; PubMed=12629050; DOI=10.1083/jcb.200209074;
RA   Kuja-Panula J., Kiiltomaeki M., Yamashiro T., Rouhiainen A.,
RA   Rauvala H.;
RT   "AMIGO, a transmembrane protein implicated in axon tract development,
RT   defines a novel protein family with leucine-rich repeats.";
RL   J. Cell Biol. 160:963-973(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RA   Ono T.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Promotes growth and fasciculation of neurites from
CC       cultured hippocampal neurons. May be involved in fasciculation as
CC       well as myelination of developing neural axons. May have a role in
CC       regeneration as well as neural plasticity in the adult nervous
CC       system. May mediate homophilic as well as heterophilic cell-cell
CC       interaction and contribute to signal transduction through its
CC       intracellular domain (By similarity).
CC   -!- SUBUNIT: Binds itself as well as AMIGO2 and AMIGO3 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential). Note=Associated with axons of neuronal cells
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80ZD8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80ZD8-2; Sequence=VSP_014166, VSP_014167;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: High levels in cerebellum, cerebrum, and
CC       retina. Low levels in liver, kidney, small intestine, spleen, lung
CC       and heart.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. AMIGO
CC       family.
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 6 LRR (leucine-rich) repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH22907.1; Type=Frameshift; Positions=113;
CC       Sequence=BAD32396.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY237008; AAO48949.1; -; mRNA.
DR   EMBL; AB167509; BAD12541.1; -; mRNA.
DR   EMBL; AK035960; BAC29259.1; -; mRNA.
DR   EMBL; AK173118; BAD32396.1; ALT_INIT; mRNA.
DR   EMBL; AL671854; CAM27260.1; -; Genomic_DNA.
DR   EMBL; BC010598; AAH10598.2; -; mRNA.
DR   EMBL; BC022907; AAH22907.1; ALT_FRAME; mRNA.
DR   IPI; IPI00122248; -.
DR   IPI; IPI00608009; -.
DR   RefSeq; NP_001004293.1; NM_001004293.1.
DR   RefSeq; NP_666249.2; NM_146137.2.
DR   UniGene; Mm.275752; -.
DR   ProteinModelPortal; Q80ZD8; -.
DR   SMR; Q80ZD8; 34-242, 277-358.
DR   PhosphoSite; Q80ZD8; -.
DR   PRIDE; Q80ZD8; -.
DR   Ensembl; ENSMUST00000050909; ENSMUSP00000061244; ENSMUSG00000050947.
DR   Ensembl; ENSMUST00000106656; ENSMUSP00000102267; ENSMUSG00000050947.
DR   Ensembl; ENSMUST00000106659; ENSMUSP00000102270; ENSMUSG00000050947.
DR   Ensembl; ENSMUST00000106661; ENSMUSP00000102272; ENSMUSG00000050947.
DR   GeneID; 229715; -.
DR   KEGG; mmu:229715; -.
DR   UCSC; uc008qyg.1; mouse.
DR   CTD; 229715; -.
DR   MGI; MGI:2653612; Amigo1.
DR   GeneTree; ENSGT00530000063545; -.
DR   HOVERGEN; HBG080231; -.
DR   InParanoid; Q80ZD8; -.
DR   OrthoDB; EOG4TB4BP; -.
DR   NextBio; 379639; -.
DR   ArrayExpress; Q80ZD8; -.
DR   Bgee; Q80ZD8; -.
DR   CleanEx; MM_AMIGO1; -.
DR   Genevestigator; Q80ZD8; -.
DR   GermOnline; ENSMUSG00000050947; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007413; P:axonal fasciculation; ISS:UniProtKB.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion; ISS:UniProtKB.
DR   GO; GO:0007156; P:homophilic cell adhesion; ISS:UniProtKB.
DR   GO; GO:0042552; P:myelination; ISS:UniProtKB.
DR   GO; GO:0050772; P:positive regulation of axonogenesis; ISS:UniProtKB.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR000372; LRR-contain_N.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00560; LRR_1; 3.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00369; LRR_TYP; 2.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00013; LRRNT; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51450; LRR; 6.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell adhesion; Developmental protein;
KW   Differentiation; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Leucine-rich repeat; Membrane; Neurogenesis; Phosphoprotein; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     27       Potential.
FT   CHAIN        28    492       Amphoterin-induced protein 1.
FT                                /FTId=PRO_0000014507.
FT   TOPO_DOM     28    371       Extracellular (Potential).
FT   TRANSMEM    372    392       Helical; (Potential).
FT   TOPO_DOM    393    492       Cytoplasmic (Potential).
FT   REPEAT       59     83       LRR 1.
FT   REPEAT       85    108       LRR 2.
FT   REPEAT      110    132       LRR 3.
FT   REPEAT      134    156       LRR 4.
FT   REPEAT      157    180       LRR 5.
FT   REPEAT      184    207       LRR 6.
FT   DOMAIN      269    352       Ig-like C2-type.
FT   MOD_RES     476    476       Phosphoserine (By similarity).
FT   CARBOHYD     72     72       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    269    269       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    315    315       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    348    348       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    359    359       N-linked (GlcNAc...) (Potential).
FT   DISULFID    290    340       By similarity.
FT   VAR_SEQ     290    309       CDTKQQGMTKVWVSPSNEQV -> TLPPTVYTRLANLRAHG
FT                                LYN (in isoform 2).
FT                                /FTId=VSP_014166.
FT   VAR_SEQ     310    492       Missing (in isoform 2).
FT                                /FTId=VSP_014167.
SQ   SEQUENCE   492 AA;  55343 MW;  EF1CCD6BA61FE222 CRC64;
     MQPQRDLRGL WLLLLSVFLL LFEVARAGRS VVSCPANCLC ASNILSCSKQ QLPNVPQSLP
     SYTALLDLSH NNLSRLRAEW TPTRLTNLHS LLLSHNHLNF ISSEAFVPVP NLRYLDLSSN
     HLHTLDEFLF SDLQALEVLL LYNNHIVVVD RNAFEDMAQL QKLYLSQNQI SRFPVELIKD
     GNKLPKLMLL DLSSNKLKKL PLTDLQKLPA WVKNGLYLHN NPLECDCKLY QLFSHWQYRQ
     LSSVMDFQED LYCMHSKKLH NIFSLDFFNC SEYKESAWEA HLGDTLTIRC DTKQQGMTKV
     WVSPSNEQVL SQGSNGSVSV RNGDLFFKKV QVEDGGVYTC YAMGETFNET LSVELKVYNF
     TLHGHHDTLN TAYTTLVGCI LSVVLVLIYL YLTPCRCWCR GVEKPSSHQG DSLSSSMLST
     TPNHDPMAGG DKDDGFDRRV AFLEPAGPGQ GQNGKLKPGN TLPVPEATGK GQRRMSDPES
     VSSVFSDTPI VV
//
ID   BAI3_MOUSE              Reviewed;        1522 AA.
AC   Q80ZF8;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-FEB-2011, entry version 67.
DE   RecName: Full=Brain-specific angiogenesis inhibitor 3;
DE   Flags: Precursor;
GN   Name=Bai3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Brain;
RA   Kim K.K., Kee H.J., Koh J.T.;
RT   "Mouse brain-specific angiogenesis inhibitor 3.";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1220 AND SER-1411, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Might be involved in angiogenesis inhibition and
CC       suppression of glioblastoma (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       LN-TM7 subfamily.
CC   -!- SIMILARITY: Contains 1 CUB domain.
CC   -!- SIMILARITY: Contains 1 GPS domain.
CC   -!- SIMILARITY: Contains 4 TSP type-1 domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY168406; AAO27431.1; -; mRNA.
DR   IPI; IPI00187338; -.
DR   UniGene; Mm.336569; -.
DR   UniGene; Mm.477270; -.
DR   ProteinModelPortal; Q80ZF8; -.
DR   SMR; Q80ZF8; 291-452, 455-510.
DR   STRING; Q80ZF8; -.
DR   PhosphoSite; Q80ZF8; -.
DR   PRIDE; Q80ZF8; -.
DR   Ensembl; ENSMUST00000041838; ENSMUSP00000035612; ENSMUSG00000033569.
DR   UCSC; uc007amw.1; mouse.
DR   MGI; MGI:2441837; Bai3.
DR   HOGENOM; HBG714232; -.
DR   HOVERGEN; HBG004813; -.
DR   InParanoid; Q80ZF8; -.
DR   ArrayExpress; Q80ZF8; -.
DR   Bgee; Q80ZF8; -.
DR   CleanEx; MM_BAI3; -.
DR   Genevestigator; Q80ZF8; -.
DR   GermOnline; ENSMUSG00000033569; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:InterPro.
DR   InterPro; IPR022624; DUF3497.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR008077; GPCR_2_brain-spec_angio_inhib.
DR   InterPro; IPR001879; GPCR_2_extracellular_dom.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR   InterPro; IPR000203; GPS_dom.
DR   InterPro; IPR000884; Thrombospondin_1_rpt.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF12003; DUF3497; 1.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF02793; HRM; 1.
DR   Pfam; PF00090; TSP_1; 4.
DR   PRINTS; PR01694; BAIPRECURSOR.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   SMART; SM00303; GPS; 1.
DR   SMART; SM00008; HormR; 1.
DR   SMART; SM00209; TSP1; 4.
DR   SUPFAM; SSF82895; TSP1; 4.
DR   PROSITE; PS01180; CUB; FALSE_NEG.
DR   PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG.
DR   PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR   PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
DR   PROSITE; PS50092; TSP1; 4.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Phosphoprotein; Receptor; Repeat; Signal;
KW   Transducer; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     25       Potential.
FT   CHAIN        26   1522       Brain-specific angiogenesis inhibitor 3.
FT                                /FTId=PRO_0000012866.
FT   TOPO_DOM     26    880       Extracellular (Potential).
FT   TRANSMEM    881    901       Helical; Name=1; (Potential).
FT   TOPO_DOM    902    910       Cytoplasmic (Potential).
FT   TRANSMEM    911    931       Helical; Name=2; (Potential).
FT   TOPO_DOM    932    939       Extracellular (Potential).
FT   TRANSMEM    940    960       Helical; Name=3; (Potential).
FT   TOPO_DOM    961    981       Cytoplasmic (Potential).
FT   TRANSMEM    982   1002       Helical; Name=4; (Potential).
FT   TOPO_DOM   1003   1023       Extracellular (Potential).
FT   TRANSMEM   1024   1044       Helical; Name=5; (Potential).
FT   TOPO_DOM   1045   1098       Cytoplasmic (Potential).
FT   TRANSMEM   1099   1119       Helical; Name=6; (Potential).
FT   TOPO_DOM   1120   1125       Extracellular (Potential).
FT   TRANSMEM   1126   1146       Helical; Name=7; (Potential).
FT   TOPO_DOM   1147   1522       Cytoplasmic (Potential).
FT   DOMAIN       30    159       CUB.
FT   DOMAIN      291    343       TSP type-1 1.
FT   DOMAIN      345    398       TSP type-1 2.
FT   DOMAIN      400    453       TSP type-1 3.
FT   DOMAIN      455    508       TSP type-1 4.
FT   DOMAIN      816    868       GPS.
FT   MOD_RES     619    619       Phosphoserine (By similarity).
FT   MOD_RES    1220   1220       Phosphoserine.
FT   MOD_RES    1411   1411       Phosphoserine.
FT   CARBOHYD     51     51       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     54     54       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     82     82       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    105    105       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    241    241       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    337    337       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    418    418       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    540    540       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    625    625       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    779    779       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    812    812       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    828    828       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    937    937       N-linked (GlcNAc...) (Potential).
FT   DISULFID    303    336       By similarity.
FT   DISULFID    307    342       By similarity.
FT   DISULFID    318    326       By similarity.
FT   DISULFID    357    392       By similarity.
FT   DISULFID    361    397       By similarity.
FT   DISULFID    372    382       By similarity.
FT   DISULFID    412    447       By similarity.
FT   DISULFID    416    452       By similarity.
FT   DISULFID    427    437       By similarity.
FT   DISULFID    467    502       By similarity.
FT   DISULFID    471    507       By similarity.
FT   DISULFID    482    492       By similarity.
SQ   SEQUENCE   1522 AA;  171340 MW;  5E18196D6043C2F4 CRC64;
     MKAVRNLLIY IFSTYLLVMF GFNAAQDFWC STLVKGVIYG SYSVSEMFPK NFTNCTWTLE
     NPDPTKYSIY LKFSKKDLSC SNFSLLAYQF DHFSHEKIKD LLRKNHSIMQ LCSSKNAFVF
     LQYDKNFIQI RRVFPTDFPG LQKKVEEDQK SFFEFLVLNK VSPSQFGCHV LCTWLESCLK
     SENGRTESCG IMYTKCTCPQ HLGEWGIDDQ SLVLVNNVVL PLNEQTEGCL TQELQTTQVC
     NLTREAKRPP KEEFGMMGDH TIKSQRPRSV HEKRVPQEQA DAAKFMAQTG ESGVEEWSQW
     SACSVTCGQG SQVRTRTCVS PYGTHCSGPL RESRVCNNTA LCPVHGVWEE WSPWSLCSFT
     CGRGQRTRTR SCTPPQYGGR PCEGPETHHK PCNIALCPVD GQWQEWSSWS HCSVTCSNGT
     QQRSRQCTAA AHGGSECRGP WAESRECYNP ECTANGQWNQ WGHWSGCSKS CDGGWERRMR
     TCQGAAVTGQ QCEGTGEEVR RCSEQRCPAP YEICPEDYLI SMVWKRTPAG DLAFNQCPLN
     ATGTTSRRCS LSLHGVASWE QPSFARCISN EYRHLQHSIK EHLAKGQRML AGDGMSQVTK
     TLLDLTQRKN FYAGDLLVSV EILRNVTDTF KRASYIPASD GVQNFFQIVS NLLDEENKEK
     WEDAQQIYPG SIELMQVIED FIYIVGMGMM DFQNSYLMTG NVVASIQKLP AASVLTDINF
     PMKGRKGMVD WARNSEDRVV IPKSIFTPVS SKELDESSVF VLGAVLYKNL DLILPTLRNY
     TVINSKVIVV TIRPEPKTTD SFLEIELAHL ANGTLNPYCV LWDDSKSNES LGTWSTQGCK
     TVLTDASHTK CLCDRLSTFA ILAQQPREIV MESSGTPSVT LIVGSGLSCL ALITLAVVYA
     ALWRYIRSER SIILINFCLS IISSNILILV GQTQTHNKSI CTTTTAFLHF FFLASFCWVL
     TEAWQSYMAV TGKIRTRLIR KRFLCLGWGL PALVVATSVG FTRTKGYGTD HYCWLSLEGG
     LLYAFVGPAA AVVLVNMVIG ILVFNKLVSR DGILDKKLKH RAGQMSEPHS GLTLKCAKCG
     VVSTTALSAT TASNAMASLW SSCVVLPLLA LTWMSAVLAM TDKRSILFQI LFAVFDSLQG
     FVIVMVHCIL RREVQDAFRC RLRNCQDPIN ADSSSSFPNG HAQIMTDFEK DVDIACRSVL
     HKDIGPCRAA TITGTLSRIS LNDDEEEKGT NPEGLSYSTL PGNVISKVII QQPTGLHMPM
     SMNELSNPCL KKENTELRRT VYLCTDDNLR GADMDIVHPQ ERMMESDYIV MPRSSVSTQP
     SMKEESKMNI GMETLPHERL LHYKVNPEFN MNPPVMDQFN MNLDQHLAPQ EHMQNLPFEP
     RTAVKNFMAS ELDDNVGLSR SETGSTISMS SLERRKSRYS DLDFEKVMHT RKRHMELFQE
     LNQKFQTLDR FRDIPNTSSM ENPAPNKNPW DTFKPPSEYQ HYTTINVLDT EAKDTLELRP
     AEWEKCLNLP LDVQEGDFQT EV
//
ID   RAP2A_MOUSE             Reviewed;         183 AA.
AC   Q80ZJ1; Q3USK1; Q7TSK4; Q810A2; Q9D3D5;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 2.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Ras-related protein Rap-2a;
DE   Flags: Precursor;
GN   Name=Rap2a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 6-16; 109-124 AND 151-162, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   INTERACTION WITH RUNDC3A, DOMAIN, AND MUTAGENESIS OF SER-17 AND
RP   THR-35.
RX   PubMed=9523700; DOI=10.1046/j.1432-1327.1998.2520290.x;
RA   Janoueix-Lerosey I., Pasheva E., de Tand M.-F., Tavitian A.,
RA   de Gunzburg J.;
RT   "Identification of a specific effector of the small GTP-binding
RT   protein Rap2.";
RL   Eur. J. Biochem. 252:290-298(1998).
RN   [5]
RP   FUNCTION.
RX   PubMed=12133960;
RA   McLeod S.J., Li A.H., Lee R.L., Burgess A.E., Gold M.R.;
RT   "The Rap GTPases regulate B cell migration toward the chemokine
RT   stromal cell-derived factor-1 (CXCL12): potential role for Rap2 in
RT   promoting B cell migration.";
RL   J. Immunol. 169:1365-1371(2002).
RN   [6]
RP   FUNCTION, AND TRANSGENIC MICE.
RX   PubMed=18701680; DOI=10.1523/JNEUROSCI.1944-08.2008;
RA   Ryu J., Futai K., Feliu M., Weinberg R., Sheng M.;
RT   "Constitutively active Rap2 transgenic mice display fewer dendritic
RT   spines, reduced extracellular signal-regulated kinase signaling,
RT   enhanced long-term depression, and impaired spatial learning and fear
RT   extinction.";
RL   J. Neurosci. 28:8178-8188(2008).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, PALMITOYLATION, AND MUTAGENESIS OF
RP   CYS-176; CYS-177 AND CYS-180.
RX   PubMed=19061864; DOI=10.1016/j.bbrc.2008.11.107;
RA   Uechi Y., Bayarjargal M., Umikawa M., Oshiro M., Takei K.,
RA   Yamashiro Y., Asato T., Endo S., Misaki R., Taguchi T., Kariya K.;
RT   "Rap2 function requires palmitoylation and recycling endosome
RT   localization.";
RL   Biochem. Biophys. Res. Commun. 378:732-737(2009).
RN   [8]
RP   INTERACTION WITH NEDD4 AND TNIK, AND UBIQUITINATION BY NEDD4.
RX   PubMed=20159449; DOI=10.1016/j.neuron.2010.01.007;
RA   Kawabe H., Neeb A., Dimova K., Young S.M. Jr., Takeda M.,
RA   Katsurabayashi S., Mitkovski M., Malakhova O.A., Zhang D.E.,
RA   Umikawa M., Kariya K., Goebbels S., Nave K.A., Rosenmund C., Jahn O.,
RA   Rhee J., Brose N.;
RT   "Regulation of Rap2A by the ubiquitin ligase Nedd4-1 controls neurite
RT   development.";
RL   Neuron 65:358-372(2010).
CC   -!- FUNCTION: Small GTP-binding protein which cycles between a GDP-
CC       bound inactive and a GTP-bound active form. In its active form
CC       interacts with and regulates several effectors including MAP4K4,
CC       MINK1 and TNIK. Part of a signaling complex composed of NEDD4,
CC       RAP2A and TNIK which regulates neuronal dendrite extension and
CC       arborization during development. More generally, it is part of
CC       several signaling cascades and may regulate cytoskeletal
CC       rearrangements, cell migration, cell adhesion and cell spreading.
CC   -!- ENZYME REGULATION: Activated by the guanine nucleotide-exchange
CC       factors RAPGEF3 and RAPGEF4 in a cAMP-dependent manner. Nucleotide
CC       exchange is also specifically stimulated by RAPGEF5, RASGEF1A and
CC       RASGEF1B (By similarity).
CC   -!- SUBUNIT: Interacts with PLCE1. Interacts with ARHGAP29, SGSM1,
CC       SGSM2 and SGSM3. Interacts (GTP-bound form preferentially) with
CC       MAP4K4. Interacts with MINK1. Interacts with cytoskeletal actin
CC       (By similarity). Interacts (GTP-bound form) with RUNDC3A.
CC       Interacts (GTP-bound form preferentially) with TNIK (via the CNH
CC       domain); the interaction is direct and recruits RAP2A to the E3
CC       ubiquitin ligase NEDD4.
CC   -!- SUBCELLULAR LOCATION: Recycling endosome membrane; Lipid-anchor;
CC       Cytoplasmic side. Note=May also localize to the Golgi and the
CC       gelatinase-containing granules of neutrophils (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80ZJ1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80ZJ1-2; Sequence=VSP_013381;
CC   -!- DOMAIN: The effector domain mediates the interaction with RUNDC3A.
CC   -!- PTM: Ubiquitinated; undergoes 'Lys-63' monoubiquitination and
CC       diubiquitination by NEDD4. Multiple lysine residues are probably
CC       modified. Ubiquitination requires TNIK, prevents interaction with
CC       effectors and inactivates RAP2A.
CC   -!- PTM: Palmitoylated. Palmitoylation is required for association
CC       with recycling endosome membranes and activation of TNIK.
CC   -!- MISCELLANEOUS: Transgenic mice expressing a constitutively active
CC       form of Rap2a display impaired spatial learning and defective
CC       extinction of contextual fear.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK018024; BAB31042.1; -; mRNA.
DR   EMBL; AK140318; BAE24330.1; -; mRNA.
DR   EMBL; BC043066; AAH43066.2; -; mRNA.
DR   EMBL; BC049084; AAH49084.2; -; mRNA.
DR   EMBL; BC053003; AAH53003.1; -; mRNA.
DR   IPI; IPI00396701; -.
DR   IPI; IPI00555002; -.
DR   RefSeq; NP_083795.2; NM_029519.3.
DR   UniGene; Mm.261448; -.
DR   ProteinModelPortal; Q80ZJ1; -.
DR   SMR; Q80ZJ1; 1-167.
DR   STRING; Q80ZJ1; -.
DR   PRIDE; Q80ZJ1; -.
DR   Ensembl; ENSMUST00000062117; ENSMUSP00000056433; ENSMUSG00000051615.
DR   GeneID; 76108; -.
DR   KEGG; mmu:76108; -.
DR   UCSC; uc007uzx.1; mouse.
DR   CTD; 76108; -.
DR   MGI; MGI:97855; Rap2a.
DR   eggNOG; roNOG15845; -.
DR   GeneTree; ENSGT00560000076632; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; Q80ZJ1; -.
DR   OMA; DCPFMET; -.
DR   OrthoDB; EOG4P2Q3G; -.
DR   PhylomeDB; Q80ZJ1; -.
DR   NextBio; 344609; -.
DR   ArrayExpress; Q80ZJ1; -.
DR   Bgee; Q80ZJ1; -.
DR   CleanEx; MM_RAP2A; -.
DR   Genevestigator; Q80ZJ1; -.
DR   GermOnline; ENSMUSG00000051615; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR   GO; GO:0034613; P:cellular protein localization; ISS:UniProtKB.
DR   GO; GO:0030336; P:negative regulation of cell migration; IDA:MGI.
DR   GO; GO:0031954; P:positive regulation of protein autophosphorylation; IDA:MGI.
DR   GO; GO:0032486; P:Rap protein signal transduction; IDA:UniProtKB.
DR   GO; GO:0048814; P:regulation of dendrite morphogenesis; ISS:UniProtKB.
DR   GO; GO:0046328; P:regulation of JNK cascade; ISS:UniProtKB.
DR   InterPro; IPR003577; GTPase_Ras.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR020849; Ras_small_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00173; RAS; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing; Endosome;
KW   GTP-binding; Lipoprotein; Membrane; Methylation; Nucleotide-binding;
KW   Palmitate; Prenylation; Ubl conjugation.
FT   CHAIN         1    180       Ras-related protein Rap-2a.
FT                                /FTId=PRO_0000082688.
FT   PROPEP      181    183       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000281337.
FT   NP_BIND      10     17       GTP (By similarity).
FT   NP_BIND      57     61       GTP (By similarity).
FT   NP_BIND     116    119       GTP (By similarity).
FT   MOTIF        32     40       Effector region (By similarity).
FT   MOD_RES     180    180       Cysteine methyl ester (By similarity).
FT   LIPID       180    180       S-farnesyl cysteine (By similarity).
FT   VAR_SEQ     106    183       Missing (in isoform 2).
FT                                /FTId=VSP_013381.
FT   MUTAGEN      17     17       S->N: Loss of affinity for GTP and loss
FT                                of interaction with RUNDC3A.
FT   MUTAGEN      35     35       T->A: Loss of interaction with RUNDC3A.
FT   MUTAGEN     176    176       C->G: Loss of association with the
FT                                recycling endosome membranes and loss of
FT                                TNIK activation; when associated with C-
FT                                177.
FT   MUTAGEN     177    177       C->G: Loss of association with the
FT                                recycling endosome membranes and loss of
FT                                TNIK activation; when associated with C-
FT                                176.
FT   MUTAGEN     180    180       C->A: Loss of association with membranes.
SQ   SEQUENCE   183 AA;  20642 MW;  A46054762765E431 CRC64;
     MREYKVVVLG SGGVGKSALT VQFVTGTFIE KYDPTIEDFY RKEIEVDSSP SVLEILDTAG
     TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI IRVKRYEKVP VILVGNKVDL
     ESEREVSSNE GRALAEEWGC PFMETSAKSK TMVDELFAEI VRQMNYAAQP DKDDPCCSAC
     NIQ
//
ID   WDTC1_MOUSE             Reviewed;         677 AA.
AC   Q80ZK9;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=WD and tetratricopeptide repeats protein 1;
GN   Name=Wdtc1; Synonyms=Gm695;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Brain, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SIMILARITY: Contains 2 TPR repeats.
CC   -!- SIMILARITY: Contains 7 WD repeats.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC048824; AAH48824.1; -; mRNA.
DR   EMBL; BC057107; AAH57107.1; -; mRNA.
DR   IPI; IPI00108450; -.
DR   RefSeq; NP_955010.1; NM_199306.4.
DR   UniGene; Mm.226576; -.
DR   UniGene; Mm.479972; -.
DR   ProteinModelPortal; Q80ZK9; -.
DR   SMR; Q80ZK9; 36-219, 518-611.
DR   STRING; Q80ZK9; -.
DR   PhosphoSite; Q80ZK9; -.
DR   PRIDE; Q80ZK9; -.
DR   Ensembl; ENSMUST00000043305; ENSMUSP00000040647; ENSMUSG00000037622.
DR   GeneID; 230796; -.
DR   KEGG; mmu:230796; -.
DR   UCSC; uc008vcq.1; mouse.
DR   CTD; 230796; -.
DR   MGI; MGI:2685541; Wdtc1.
DR   HOGENOM; HBG356683; -.
DR   HOVERGEN; HBG059105; -.
DR   InParanoid; Q80ZK9; -.
DR   OMA; KAPHNAM; -.
DR   OrthoDB; EOG4CRKZJ; -.
DR   PhylomeDB; Q80ZK9; -.
DR   NextBio; 461005; -.
DR   ArrayExpress; Q80ZK9; -.
DR   Bgee; Q80ZK9; -.
DR   CleanEx; MM_WDTC1; -.
DR   Genevestigator; Q80ZK9; -.
DR   GermOnline; ENSMUSG00000037622; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0004857; F:enzyme inhibitor activity; IDA:MGI.
DR   GO; GO:0042393; F:histone binding; IPI:MGI.
DR   GO; GO:0042826; F:histone deacetylase binding; IPI:MGI.
DR   GO; GO:0055082; P:cellular chemical homeostasis; IMP:MGI.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IMP:MGI.
DR   GO; GO:0006006; P:glucose metabolic process; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR   GO; GO:0045717; P:negative regulation of fatty acid biosynthetic process; IDA:MGI.
DR   GO; GO:0010553; P:negative regulation of gene-specific transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0008361; P:regulation of cell size; IMP:MGI.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 3.
DR   Pfam; PF00400; WD40; 5.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS50005; TPR; FALSE_NEG.
DR   PROSITE; PS50293; TPR_REGION; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Repeat; TPR repeat; WD repeat.
FT   CHAIN         1    677       WD and tetratricopeptide repeats protein
FT                                1.
FT                                /FTId=PRO_0000051435.
FT   REPEAT       45     84       WD 1.
FT   REPEAT       88    129       WD 2.
FT   REPEAT      132    172       WD 3.
FT   REPEAT      182    222       WD 4.
FT   REPEAT      265    305       WD 5.
FT   REPEAT      361    394       TPR 1.
FT   REPEAT      396    431       TPR 2.
FT   REPEAT      535    575       WD 6.
FT   REPEAT      578    617       WD 7.
FT   MOD_RES     511    511       Phosphoserine.
SQ   SEQUENCE   677 AA;  75733 MW;  CDB5F09E80E6C625 CRC64;
     MAKVNITRDL IRRQVKERGA LSFERRYHVT DPFIRRLGLE AELQGHSGCV NCLEWNEKGD
     LLASGSDDQH TIVWDPLHHK KLLSMHTGHT ANIFSVKFLP HAGDRILITG AADSKVHVHD
     LTVKETIHMF GDHTNRVKRI ATAPMWPNTF WSAAEDGLIR QYDLRENSKH SEVLIDLTEY
     CGPMVEAKCL TVNPQDNNCL AVGASGPFVR LYDIRMIHNH RKSMRQSPSA GVHTFCDRQK
     PLPDGAAQYY VAGHLPVKLP DYNSRLRVLV ATYVTFSPNG TELLVNMGGE QVYLFDLTYK
     QRPYTFLLPR KCHSVEVQNG KMSTNGVSNG VSNGLHLHSN GFRLPESKGC ISPQVELPPY
     LERVKQQANE AFACQQWTQA IQLYSQAVQK APHNAMLYGN RAAAYMKRKW DGDHYDALRD
     CLKAISLNPC HLKAHFRLAR CLFELKYVAE ALECLDDFKG KFPEQAHSSA CDALGRDITA
     ALFSKSDGEE KKAAGGGGGP VRLRSTSRKD SISEDEMVLR ERSYDYQFRY CGHCNTTTDI
     KEANFFGSNA QYIVSGSDDG SFFIWEKETT NLVRVLQGDE SIVNCLQPHP SYCFLATSGI
     DPVVRLWNPR PESEDLTGRV VEDMEGASQA NQRRMNANPL EAMLLDMGYR ITGLSSGGAG
     ASDDEDSAEG QVQCRPS
//
ID   Q80ZQ8_MOUSE            Unreviewed;        68 AA.
AC   Q80ZQ8;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 53.
DE   SubName: Full=Prkcb protein;
GN   Name=Prkcb; Synonyms=Prkcb1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
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DR   EMBL; BC048553; AAH48553.1; -; mRNA.
DR   IPI; IPI00458184; -.
DR   UniGene; Mm.207496; -.
DR   UniGene; Mm.446371; -.
DR   ProteinModelPortal; Q80ZQ8; -.
DR   PhosphoSite; Q80ZQ8; -.
DR   PRIDE; Q80ZQ8; -.
DR   eggNOG; veNOG05821; -.
DR   Genevestigator; Q80ZQ8; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR017892; Pkinase_C.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding; Kinase; Nucleotide-binding;
KW   Serine/threonine-protein kinase; Transferase.
SQ   SEQUENCE   68 AA;  7828 MW;  23A4E0444A7CCF4E CRC64;
     MFAAASASVL MCSLSIWQRD KRDTSNFDKE FTRQPVELTP TDKLFIMNLD QNEFAGFSYT
     NPEFVINV
//
ID   Q80ZV7_MOUSE            Unreviewed;       631 AA.
AC   Q80ZV7;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   08-FEB-2011, entry version 38.
DE   SubName: Full=Ncor2 protein;
DE   Flags: Fragment;
GN   Name=Ncor2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC047524; AAH47524.1; -; mRNA.
DR   IPI; IPI00222492; -.
DR   UniGene; Mm.278646; -.
DR   HSSP; Q9Y618; 1KKQ.
DR   STRING; Q80ZV7; -.
DR   Ensembl; ENSMUST00000055256; ENSMUSP00000055954; ENSMUSG00000029478.
DR   Ensembl; ENSMUST00000111393; ENSMUSP00000107024; ENSMUSG00000029478.
DR   Ensembl; ENSMUST00000111394; ENSMUSP00000107025; ENSMUSG00000029478.
DR   Ensembl; ENSMUST00000111398; ENSMUSP00000107029; ENSMUSG00000029478.
DR   Ensembl; ENSMUST00000111400; ENSMUSP00000107031; ENSMUSG00000029478.
DR   Ensembl; ENSMUST00000111401; ENSMUSP00000107032; ENSMUSG00000029478.
DR   Ensembl; ENSMUST00000111402; ENSMUSP00000107033; ENSMUSG00000029478.
DR   MGI; MGI:1337080; Ncor2.
DR   GeneTree; ENSGT00550000074554; -.
DR   HOGENOM; HBG716746; -.
DR   InParanoid; Q80ZV7; -.
DR   ArrayExpress; Q80ZV7; -.
DR   Bgee; Q80ZV7; -.
DR   Genevestigator; Q80ZV7; -.
DR   GO; GO:0000118; C:histone deacetylase complex; IDA:MGI.
DR   GO; GO:0016604; C:nuclear body; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0016566; F:specific transcriptional repressor activity; IMP:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; IMP:MGI.
DR   GO; GO:0021846; P:cell proliferation in forebrain; IMP:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0003007; P:heart morphogenesis; IGI:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:MGI.
DR   GO; GO:0021537; P:telencephalon development; IMP:MGI.
DR   GO; GO:0050872; P:white fat cell differentiation; IMP:MGI.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   631 AA;  66870 MW;  CC1F52630A984D6E CRC64;
     VTSVEPGTPT VLRWARSTST SSPVRPAATF PPATHCPLGG TLEGVYPTLM EPVLLPKETS
     RVARPERPRV DAGHAFLTKP PAREPASSPS KSSEPRSLAP PSSSHTAIAR TPAKNLAPHH
     ASPDPPAPTS ASDLHREKTQ SKPFSIQELE LRSLGYHSGA GYSPDGVEPI SPVSSPSLTH
     DKGLSKPLEE LEKSHLEGEL RHKQPGPMKL SAEAAHLPHL RPLPESQPSS SPLLQTAPGI
     KGHQRVVTSA QHISEVITQD YTRHHPQQLS GPLPAPLYSF PGASCPVLDL RRPPSDLYLP
     PPDHGTPARG SPHSEGGKRS PEPSKTSVLG SSEDAIEPVS PPEGMTEPGH ARSTAYPLLY
     RDGEQGEPRM GSKSPGNTSQ PPAFFSKLTE SNSAMVKSKK QEINKKLNTH NRNEPEYNIG
     QPGTEIFNMP AITGAGLMTC RSQAVQEHAS TNMGLEAIIR KALMGKYDQW EEPPPLGANA
     FNPLNASASL PAAAMPITTA DGRSDHALTS PGGGGKAKVS GRPSSRKAKS PAPGLASGDR
     PPSVSSVHSE GDCNRRTPLT NRVWEDRPSS AGSTPFPYNP LIMRLQAGVM ASPPPPGLAA
     GSGPLAGPHH AWDEEPKPLL CSQYETLSDS E
//
ID   CH055_MOUSE             Reviewed;         207 AA.
AC   Q80ZW2;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 47.
DE   RecName: Full=UPF0670 protein C8orf55 homolog;
DE   Flags: Precursor;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Secreted (Potential).
CC   -!- SIMILARITY: Belongs to the UPF0670 family.
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DR   EMBL; BC047266; AAH47266.1; -; mRNA.
DR   IPI; IPI00331014; -.
DR   RefSeq; NP_941009.1; NM_198607.1.
DR   UniGene; Mm.268603; -.
DR   ProteinModelPortal; Q80ZW2; -.
DR   SMR; Q80ZW2; 48-190.
DR   PRIDE; Q80ZW2; -.
DR   Ensembl; ENSMUST00000070923; ENSMUSP00000069692; ENSMUSG00000056665.
DR   GeneID; 223626; -.
DR   KEGG; mmu:223626; -.
DR   UCSC; uc007wfs.1; mouse.
DR   MGI; MGI:1925301; 4930572J05Rik.
DR   eggNOG; maNOG16678; -.
DR   GeneTree; ENSGT00390000004859; -.
DR   HOGENOM; HBG446065; -.
DR   HOVERGEN; HBG059534; -.
DR   InParanoid; Q80ZW2; -.
DR   OMA; GWYLVRV; -.
DR   OrthoDB; EOG4QRH53; -.
DR   PhylomeDB; Q80ZW2; -.
DR   NextBio; 376759; -.
DR   ArrayExpress; Q80ZW2; -.
DR   Bgee; Q80ZW2; -.
DR   CleanEx; MM_4930572J05RIK; -.
DR   Genevestigator; Q80ZW2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR006683; Thioestr_supf.
DR   Pfam; PF03061; 4HBT; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Secreted; Signal.
FT   SIGNAL        1     21       Potential.
FT   CHAIN        22    207       UPF0670 protein C8orf55 homolog.
FT                                /FTId=PRO_0000285637.
FT   CARBOHYD    188    188       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   207 AA;  23803 MW;  26CF2FA726955063 CRC64;
     MLELLVASLS LALAFFALLD GWYLVRVPCA VLRARLLQPR VRDLLAEQRY AGRVLPSDLD
     LLLHMNNARY LREADVARAA HLTRCGVLGA LRDLNAHTVL AASCARYRRS LRLFEPFEVH
     TRLQGWDDRA FYLEARFVSL RDGFVCALLR FRQHVLGTSP DRVVQHLCKR RVEPPELPED
     LKHWISYNET SSQLLRAESG LSDRKDQ
//
ID   SPAG1_MOUSE             Reviewed;         901 AA.
AC   Q80ZX8; Q8CCK7; Q9QZJ3; Q9QZJ4;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Sperm-associated antigen 1;
DE   AltName: Full=Infertility-related sperm protein Spag-1;
DE   AltName: Full=TPR-containing protein involved in spermatogenesis;
DE            Short=TPIS;
GN   Name=Spag1; Synonyms=Tpis;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), DEVELOPMENTAL STAGE,
RP   AND TISSUE SPECIFICITY.
RC   STRAIN=ICR; TISSUE=Fetal skin, and Testis;
RX   MEDLINE=99458625; PubMed=10527845; DOI=10.1006/bbrc.1999.1477;
RA   Takaishi M., Huh N.-H.;
RT   "A tetratricopeptide repeat-containing protein gene, tpis, whose
RT   expression is induced with differentiation of spermatogenic cells.";
RL   Biochem. Biophys. Res. Commun. 264:81-85(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-739 AND SER-740, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Plays a role in fertilization. Binds GTP and has GTPase
CC       activity (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q80ZX8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80ZX8-2; Sequence=VSP_012684;
CC       Name=3;
CC         IsoId=Q80ZX8-3; Sequence=VSP_012685;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Detected in cerebellum, tongue, esophagus,
CC       forestomach, sperm and testis.
CC   -!- DEVELOPMENTAL STAGE: Expression is very low in embryonic epidermis
CC       at E13.5 and increases from E14.5 to E16.5. In young mice
CC       expression increases in the testis of 2 to 6 weeks old animals,
CC       and then remains stable.
CC   -!- MISCELLANEOUS: Antibodies against SPAG1 interfere with
CC       fertilization (By similarity).
CC   -!- SIMILARITY: Contains 8 TPR repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC27944.1; Type=Erroneous initiation;
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DR   EMBL; AF181252; AAF06160.1; -; mRNA.
DR   EMBL; AF181253; AAF06161.1; -; mRNA.
DR   EMBL; AK032601; BAC27944.1; ALT_INIT; mRNA.
DR   EMBL; BC046313; AAH46313.1; -; mRNA.
DR   IPI; IPI00551151; -.
DR   IPI; IPI00551464; -.
DR   IPI; IPI00624261; -.
DR   PIR; JC7111; JC7111.
DR   RefSeq; NP_036161.2; NM_012031.3.
DR   UniGene; Mm.295539; -.
DR   ProteinModelPortal; Q80ZX8; -.
DR   SMR; Q80ZX8; 212-330, 430-541, 606-701.
DR   STRING; Q80ZX8; -.
DR   PhosphoSite; Q80ZX8; -.
DR   PRIDE; Q80ZX8; -.
DR   Ensembl; ENSMUST00000047348; ENSMUSP00000047335; ENSMUSG00000037617.
DR   GeneID; 26942; -.
DR   KEGG; mmu:26942; -.
DR   UCSC; uc007vmn.1; mouse.
DR   UCSC; uc007vmp.1; mouse.
DR   CTD; 26942; -.
DR   MGI; MGI:1349387; Spag1.
DR   eggNOG; roNOG10630; -.
DR   GeneTree; ENSGT00600000084276; -.
DR   HOGENOM; HBG715936; -.
DR   HOVERGEN; HBG079204; -.
DR   InParanoid; Q80ZX8; -.
DR   OMA; EDYKEKT; -.
DR   OrthoDB; EOG4FFD17; -.
DR   PhylomeDB; Q80ZX8; -.
DR   NextBio; 304865; -.
DR   ArrayExpress; Q80ZX8; -.
DR   Bgee; Q80ZX8; -.
DR   Genevestigator; Q80ZX8; -.
DR   GermOnline; ENSMUSG00000037617; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR   InterPro; IPR001440; TPR-1.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 3.
DR   Pfam; PF00515; TPR_1; 4.
DR   SMART; SM00028; TPR; 8.
DR   PROSITE; PS50005; TPR; 6.
DR   PROSITE; PS50293; TPR_REGION; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Fertilization; GTP-binding;
KW   Hydrolase; Nucleotide-binding; Phosphoprotein; Repeat; TPR repeat.
FT   CHAIN         1    901       Sperm-associated antigen 1.
FT                                /FTId=PRO_0000106325.
FT   REPEAT      213    246       TPR 1.
FT   REPEAT      247    279       TPR 2.
FT   REPEAT      280    313       TPR 3.
FT   REPEAT      430    464       TPR 4.
FT   REPEAT      472    505       TPR 5.
FT   REPEAT      507    539       TPR 6.
FT   REPEAT      606    639       TPR 7.
FT   REPEAT      640    673       TPR 8.
FT   NP_BIND     756    763       GTP (Potential).
FT   MOD_RES     180    180       Phosphotyrosine (By similarity).
FT   MOD_RES     351    351       Phosphoserine (By similarity).
FT   MOD_RES     739    739       Phosphoserine.
FT   MOD_RES     740    740       Phosphoserine.
FT   MOD_RES     766    766       Phosphoserine (By similarity).
FT   VAR_SEQ       1    372       Missing (in isoform 2).
FT                                /FTId=VSP_012684.
FT   VAR_SEQ       1    233       Missing (in isoform 3).
FT                                /FTId=VSP_012685.
FT   CONFLICT    115    115       C -> R (in Ref. 1; AAF06160).
FT   CONFLICT    364    364       E -> A (in Ref. 1; AAF06160).
FT   CONFLICT    419    419       H -> Y (in Ref. 1; AAF06160/AAF06161).
FT   CONFLICT    664    664       E -> D (in Ref. 1; AAF06160/AAF06161).
SQ   SEQUENCE   901 AA;  100670 MW;  C8D14100AD00D69F CRC64;
     MTAKAKDCPS LWGFGTTKTF KIPIEHLDFK YIENCSDVKH LEKILYVLRS GEEGYYPELT
     EFCEKCLTNL APKSRALRKD KPAETASSFS AEEWEKIDSD LKSWVSEIKR EENTCHFHDP
     ENHPGVEDPL PPVRGSTCCP HSGKETYSKS KTAKKRIPRD YAEWDKFDVE KECSKIDEDY
     KEKTVINNKA HLSKIETKIE TAGLTEKEKS FLANREKGKG NEAFYSGDYE EAVMYYTRSL
     SALPTAIAYN NRAQAEIKLQ RWSSALEDCE KALELDPGNV KALLRRATTY KHQNKLQEAV
     DDLRKVLQVE PDNDLAKKTL SEVERDLKNS EPVSELQTKG KRMVIEEVEN SGDEGGKGSA
     DEREDGGSDE AAMGNIQKKL MVRRSEGGRR SRRGRTPGPR AEQQGGLRET ATASTGDSHY
     PEEPRAADNP SGLKRRGNEL FRGGQFAEAA AQYSVAIAQL EPTGSANADE LSILYSNRAA
     CYLKEGNCRD CIQDCNRALE LHPFSVKPLL RRAMAYETLE QYRNAYVDYK TVLQIDCGIQ
     LASDSANRIA RILTELDGSK WRERLPPIPA VPTSEPLRVW LPAAETPDQD PCPNNCMPSI
     TDEKMFQALK EEGNQLVKDK NYKDAISKYN ECLKINSKAC AIYTNRALCY LKLGQFEEAK
     LDCEQALQID GENVKASHRL ALAQKGLENC RESGVDPSQV LLSPDSSEAA RHLDTKNDTA
     PPSKGRERRR IQVQEVDGSS DEEPERPAEA SATSAPARDG VEDGGSAEPA EKLDVSKPTN
     AYEFGQVLST ISARKDEEAC AHLLAITAPK DLPLLLSNKL EGDTFLLLIQ SLKSHLVAKD
     PSLVYEHLLY LSKAERFKTM LTLINKGQKE QMAQLFDGLS DTQSDGLTAE DVQALRRQYE
     L
//
ID   DDX42_MOUSE             Reviewed;         929 AA.
AC   Q810A7; Q3TAN3; Q3TE60; Q8BWZ7; Q9D8Q2;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 3.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=ATP-dependent RNA helicase DDX42;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 42;
GN   Name=Ddx42;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Embryonic stem cell, Pancreas, Spleen, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 616-626, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-109 AND
RP   SER-111, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-111, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: ATP-dependent RNA helicase. Binds to partially double-
CC       stranded RNAs (dsRNAs) in order to unwind RNA secondary
CC       structures. Unwinding is promoted in the presence of single-strand
CC       binding proteins. Mediates also RNA duplex formation thereby
CC       displacing the single-strand RNA binding protein. ATP and ADP
CC       modulate its activity: ATP binding and hydrolysis by DDX42
CC       triggers RNA strand separation, whereas the ADP-bound form of the
CC       protein triggers annealing of complementary RNA strands. Involved
CC       in the survival of cells by interacting with TP53BP2 and thereby
CC       counteracting the apoptosis-stimulating activity of TP53BP2.
CC       Relocalizes TP53BP2 to the cytoplasm (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Component of splicing factor SF3B which is composed of at
CC       least eight subunits; SF3B1/SAP155/SF3B155, SF3B2/SAP145/SF3B155,
CC       SF3B3/SAP130/SF3B130, SF3B4/SAP49/SF3B49, SF3B14A, PHF5A/SF3B14B,
CC       SF3B10 and SF3B125. Interacts (via the C-terminus) with TP53BP2;
CC       the interaction is not inhibitied by TP53BP2 ubiquitination and is
CC       independent of p53/TP53 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus speckle
CC       (By similarity). Nucleus, Cajal body (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q810A7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q810A7-2; Sequence=VSP_023519;
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX42
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH43036.4; Type=Erroneous initiation;
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DR   EMBL; AK007805; BAB25270.3; -; mRNA.
DR   EMBL; AK049311; BAC33675.1; -; mRNA.
DR   EMBL; AK169816; BAE41388.1; -; mRNA.
DR   EMBL; AK171730; BAE42635.1; -; mRNA.
DR   EMBL; AL604045; CAM23778.1; -; Genomic_DNA.
DR   EMBL; BC043036; AAH43036.4; ALT_INIT; mRNA.
DR   IPI; IPI00329839; -.
DR   IPI; IPI00830514; -.
DR   RefSeq; NP_082350.3; NM_028074.4.
DR   UniGene; Mm.41367; -.
DR   HSSP; P09052; 2DB3.
DR   ProteinModelPortal; Q810A7; -.
DR   SMR; Q810A7; 230-628.
DR   IntAct; Q810A7; 1.
DR   PhosphoSite; Q810A7; -.
DR   PRIDE; Q810A7; -.
DR   Ensembl; ENSMUST00000021046; ENSMUSP00000021046; ENSMUSG00000020705.
DR   GeneID; 72047; -.
DR   KEGG; mmu:72047; -.
DR   UCSC; uc007lyk.1; mouse.
DR   CTD; 72047; -.
DR   MGI; MGI:1919297; Ddx42.
DR   eggNOG; roNOG13290; -.
DR   HOGENOM; HBG357033; -.
DR   HOVERGEN; HBG081425; -.
DR   InParanoid; Q810A7; -.
DR   OMA; GANDGRN; -.
DR   OrthoDB; EOG47WNN9; -.
DR   PhylomeDB; Q810A7; -.
DR   NextBio; 335308; -.
DR   ArrayExpress; Q810A7; -.
DR   Bgee; Q810A7; -.
DR   CleanEx; MM_DDX42; -.
DR   Genevestigator; Q810A7; -.
DR   GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008104; P:protein localization; ISS:UniProtKB.
DR   GO; GO:0045767; P:regulation of anti-apoptosis; ISS:UniProtKB.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Coiled coil;
KW   Cytoplasm; Direct protein sequencing; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; RNA-binding.
FT   CHAIN         1    929       ATP-dependent RNA helicase DDX42.
FT                                /FTId=PRO_0000280059.
FT   DOMAIN      284    459       Helicase ATP-binding.
FT   DOMAIN      487    632       Helicase C-terminal.
FT   NP_BIND     297    304       ATP (By similarity).
FT   REGION      739    828       Necessary for interaction with TP53BP2
FT                                (By similarity).
FT   COILED      116    157       Potential.
FT   MOTIF       253    281       Q motif.
FT   MOTIF       407    410       DEAD box.
FT   COMPBIAS     43     46       Poly-Ser.
FT   COMPBIAS    175    178       Poly-Glu.
FT   COMPBIAS    654    659       Poly-Gly.
FT   COMPBIAS    675    678       Poly-Asn.
FT   COMPBIAS    784    878       Gly-rich.
FT   MOD_RES       5      5       N6-acetyllysine (By similarity).
FT   MOD_RES      10     10       Phosphothreonine (By similarity).
FT   MOD_RES      96     96       Phosphoserine (By similarity).
FT   MOD_RES     104    104       Phosphoserine.
FT   MOD_RES     109    109       Phosphoserine.
FT   MOD_RES     111    111       Phosphoserine.
FT   MOD_RES     185    185       Phosphoserine.
FT   MOD_RES     752    752       Phosphoserine (By similarity).
FT   VAR_SEQ       1    119       Missing (in isoform 2).
FT                                /FTId=VSP_023519.
FT   CONFLICT    503    503       L -> M (in Ref. 1; BAB25270).
FT   CONFLICT    537    537       R -> G (in Ref. 1; BAE42635).
FT   CONFLICT    859    859       H -> Y (in Ref. 1; BAC33675).
SQ   SEQUENCE   929 AA;  101965 MW;  0E8F3D30D07BDFCF CRC64;
     MNWNKGGPGT KRGFGFGGFA ISAGKKEEAK LPQQSHSAFG AASSSSGFGK SAPPQLPSFY
     KIGSKRANFD EENAYFEDEE EDSSNVDLPY IPAENSPTRQ QFHSKPADSD SDDDPLEAFM
     AEVEDQAARD MKRLEEKDKE RKNVKGIRDD IEEEDDQEAY FRYMAENPTA GVVQEEEEDN
     LEYDSDGNPI APSKKIIDPL PPIDHSEIDY PPFEKNFYNE HEEITNLTPQ QLIDLRHKLN
     LRVSGAAPPR PGSSFAHFGF DEQLMHQIRK SEYTQPTPIQ CQGVPVALSG RDMIGIAKTG
     SGKTAAFIWP MLIHIMDQKE LEPGDGPIAV IVCPTRELCQ QIHAECKRFG KAYNLRSVAV
     YGGGSMWEQA KALQEGAEIV VCTPGRLIDH VKKKATNLQR VSYLVFDEAD RMFDMGFEYQ
     VRSIASHVRP DRQTLLFSAT FRKKIEKLAR DILIDPIRVV QGDIGEANED VTQIVEILHS
     GPSKWNWLTR RLVEFTSSGS VLLFVTKKAN AEELASNLKQ EGHNLGLLHG DMDQSERNKV
     ISDFKKKDIP VLVATDVAAR GLDIPSIKTV INYDVARDID THTHRIGRTG RAGEKGVAYT
     LLTPKDSNFA GDLVRNLEGA NQHVSKELLD LAMQNAWFRK SRFKGGKGKK LNIGGGGLGY
     RERPGLGSEN SDRGNNNNVM SNYEAYKPST GAMGDRLTAM KAAFQSQYKS HFVAASLSNQ
     KAGTSSAGAS GWTSAGSLNS VPTNSAQQGH NSPDNPMTSS TKNIPGFNNS GNISSAPVTY
     PSIGAQGVNN TASGNNSREG IGGGNGKRER YTENRGGSRH SHGDGGNRHG DGGRHGDGYR
     YPESGSRHTD GHRHGETRHG GSAGRHGESR GANDGRNGES RKEGFNRENK MDPKVDSSRM
     DKVDSKTDKT PDGFAVPEPP KRKKSRWDS
//
ID   SLIK5_MOUSE             Reviewed;         957 AA.
AC   Q810B7; Q9CT21;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=SLIT and NTRK-like protein 5;
DE   Flags: Precursor;
GN   Name=Slitrk5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=14550773; DOI=10.1016/S1044-7431(03)00129-5;
RA   Aruga J., Mikoshiba K.;
RT   "Identification and characterization of Slitrk, a novel neuronal
RT   transmembrane protein family controlling neurite outgrowth.";
RL   Mol. Cell. Neurosci. 24:117-129(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 830-957 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Suppresses neurite outgrowth.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q810B7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q810B7-2; Sequence=VSP_050708, VSP_050709, VSP_050710;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: In the adult, significant expression is
CC       detected only in the brain. In the embryo, expressed in the
CC       subventricular zone, cortical plate, pyramidal layer of
CC       hippocampus, thalamus and hypothalamus.
CC   -!- SIMILARITY: Belongs to the SLITRK family.
CC   -!- SIMILARITY: Contains 18 LRR (leucine-rich) repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AK011457; Type=Frameshift; Positions=836;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB097574; BAC67208.1; -; Genomic_DNA.
DR   EMBL; BC065107; AAH65107.1; -; mRNA.
DR   EMBL; AK011457; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00329844; -.
DR   IPI; IPI00410889; -.
DR   RefSeq; NP_942565.1; NM_198865.1.
DR   UniGene; Mm.235097; -.
DR   UniGene; Mm.417152; -.
DR   ProteinModelPortal; Q810B7; -.
DR   SMR; Q810B7; 45-285, 371-610.
DR   STRING; Q810B7; -.
DR   PhosphoSite; Q810B7; -.
DR   PRIDE; Q810B7; -.
DR   Ensembl; ENSMUST00000042767; ENSMUSP00000041499; ENSMUSG00000033214.
DR   Ensembl; ENSMUST00000095558; ENSMUSP00000093214; ENSMUSG00000033214.
DR   GeneID; 75409; -.
DR   KEGG; mmu:75409; -.
DR   UCSC; uc007uye.1; mouse.
DR   CTD; 75409; -.
DR   MGI; MGI:2679448; Slitrk5.
DR   GeneTree; ENSGT00550000074348; -.
DR   HOGENOM; HBG444133; -.
DR   HOVERGEN; HBG056407; -.
DR   InParanoid; Q810B7; -.
DR   OMA; HHRGPAL; -.
DR   OrthoDB; EOG4X97GH; -.
DR   PhylomeDB; Q810B7; -.
DR   NextBio; 342932; -.
DR   ArrayExpress; Q810B7; -.
DR   Bgee; Q810B7; -.
DR   CleanEx; MM_SLITRK5; -.
DR   Genevestigator; Q810B7; -.
DR   GermOnline; ENSMUSG00000033214; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR000372; LRR-contain_N.
DR   Pfam; PF00560; LRR_1; 4.
DR   SMART; SM00369; LRR_TYP; 4.
DR   SMART; SM00082; LRRCT; 2.
DR   SMART; SM00013; LRRNT; 1.
DR   PROSITE; PS51450; LRR; 11.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Leucine-rich repeat; Membrane;
KW   Phosphoprotein; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     40       Potential.
FT   CHAIN        41    957       SLIT and NTRK-like protein 5.
FT                                /FTId=PRO_0000032682.
FT   TOPO_DOM     41    664       Extracellular (Potential).
FT   TRANSMEM    665    685       Helical; (Potential).
FT   TOPO_DOM    686    957       Cytoplasmic (Potential).
FT   REPEAT       80    103       LRR 1.
FT   REPEAT      104    127       LRR 2.
FT   REPEAT      128    151       LRR 3.
FT   REPEAT      153    175       LRR 4.
FT   REPEAT      176    199       LRR 5.
FT   REPEAT      201    223       LRR 6.
FT   REPEAT      225    248       LRR 7.
FT   REPEAT      262    285       LRR 8.
FT   REPEAT      384    408       LRR 9.
FT   REPEAT      409    431       LRR 10.
FT   REPEAT      432    455       LRR 11.
FT   REPEAT      456    479       LRR 12.
FT   REPEAT      481    503       LRR 13.
FT   REPEAT      504    527       LRR 14.
FT   REPEAT      529    551       LRR 15.
FT   REPEAT      553    579       LRR 16.
FT   REPEAT      780    803       LRR 17.
FT   REPEAT      931    956       LRR 18.
FT   MOD_RES     832    832       Phosphotyrosine (By similarity).
FT   CARBOHYD    103    103       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    644    644       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     706    722       DVSSFNMQYSVYGGGGG -> AATAPAAAPSADADAAW
FT                                (in isoform 2).
FT                                /FTId=VSP_050708.
FT   VAR_SEQ     726    755       GHPHAHVHHRGPALPKVKTPAGHVYEYIPH -> EAGKPPF
FT                                EEPRLQRQHHRAPRGPTVAGAGR (in isoform 2).
FT                                /FTId=VSP_050709.
FT   VAR_SEQ     756    957       Missing (in isoform 2).
FT                                /FTId=VSP_050710.
FT   CONFLICT    153    153       E -> D (in Ref. 2; AAH65107).
SQ   SEQUENCE   957 AA;  107165 MW;  0CB89BD7FE2D18AF CRC64;
     MHVCCPPVTL EQDLHRKMHS WMLQTLAFAV TSLVLSCAET IDYYGEICDN ACPCEEKDGI
     LTVSCENRGI ISLSEISPPR FPIYHLLLSG NLLSRLYPNE FVNYTGASIL HLGSNVIQDI
     ETGAFHGLRG LRRLHLNNNK LELLRDDTFL GLENLEYLQV DYNYISVIEP NAFGKLHMLQ
     VLILNDNLLS GLPNNLFRFV PLTHLDLRGN RLKLLPYVGL LQHMDKVVEL QLEENPWNCS
     CELISLKDWL DSISYSALVG DVVCETPFRL HGRDLDEVSK QELCPRKLIS DYEMRPQTPL
     STTGYLHTTP ASVNSVATSS SAVYKPPLKP PKGTRQPNKP RVRPTSRQPS KDLGYSNYGP
     SIAYQTKSPV PLECPTACTC NLQISDLGLN VNCQERKIES IAELQPKPYN PKKMYLTENY
     ITVVRRTDFL EATGLDLLHL GNNRISMIQD RAFGDLGNLR RLYLNGNRIE RLSPELFYGL
     QSLQYLFLQY NLIREIQAGT FDPVPNLQLL FLNNNQLQAM PSGVFSGLTL LRLNLRGNSF
     TSLPVSGVLD QLTSLIQIDL HDNPWDCTCD VVGMKLWIEQ LKVGVLVDEV ICKAPKKFAE
     TYMRSIKSEL LCPDYSDVVV STPTPSSIQV PSRTNAATPA VRLNSTGTPA GLGAGTGASS
     VPLSVLILSL LLVFIMSVFV AAGLFVLVMK RRKKNQSDHT STNNSDVSSF NMQYSVYGGG
     GGGGGGHPHA HVHHRGPALP KVKTPAGHVY EYIPHPLGHM CKNPIYRSRE GNSVEDYKDL
     HELKVTYSSN HHLQQQPPPP PQQPQQQPPP QMQMQPGEEE RRESHHLRSP AYSVSTIEPR
     EDLLSPVQDA DRFYRGILEP DKHCSTTPAG SSLPEYPKFP CSPAAYTFSP NYDLRRPHQY
     LHPGAGESRL REPVLYSPPG AVFVEPNRNE YLELKAKLNV EPDYLEVLEK QTTFSQF
//
ID   SLIK1_MOUSE             Reviewed;         696 AA.
AC   Q810C1; Q9CXL0;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=SLIT and NTRK-like protein 1;
DE   Flags: Precursor;
GN   Name=Slitrk1; Synonyms=Sltk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=14550773; DOI=10.1016/S1044-7431(03)00129-5;
RA   Aruga J., Mikoshiba K.;
RT   "Identification and characterization of Slitrk, a novel neuronal
RT   transmembrane protein family controlling neurite outgrowth.";
RL   Mol. Cell. Neurosci. 24:117-129(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 369-696.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Enhances neuronal dendrite outgrowth.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- TISSUE SPECIFICITY: In the adult, significant expression is
CC       detected only in the brain. Broadly expressed in embryonic brain
CC       with highest expression in subventricular zone, subplate, cortical
CC       plate, pyramidal cell layer of hippocampus, thalamus and
CC       hypothalamus where levels are highest in ventromedial hypothalamus
CC       and medial part of periaqueductal gray matter. Also expressed in
CC       mantle layer of spinal cord and in lateral and medial motor
CC       columns.
CC   -!- DEVELOPMENTAL STAGE: In the embryo, expressed from day 10-12 and
CC       continues through later gestational development and into
CC       adulthood.
CC   -!- SIMILARITY: Belongs to the SLITRK family.
CC   -!- SIMILARITY: Contains 13 LRR (leucine-rich) repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; AB097570; BAC67204.1; -; Genomic_DNA.
DR   EMBL; AK014285; BAB29244.2; -; mRNA.
DR   IPI; IPI00110451; -.
DR   RefSeq; NP_951020.1; NM_199065.2.
DR   UniGene; Mm.257268; -.
DR   ProteinModelPortal; Q810C1; -.
DR   SMR; Q810C1; 38-256, 357-577.
DR   STRING; Q810C1; -.
DR   PhosphoSite; Q810C1; -.
DR   PRIDE; Q810C1; -.
DR   Ensembl; ENSMUST00000100322; ENSMUSP00000097897; ENSMUSG00000075478.
DR   GeneID; 76965; -.
DR   KEGG; mmu:76965; -.
DR   UCSC; uc007uyc.1; mouse.
DR   CTD; 76965; -.
DR   MGI; MGI:2679446; Slitrk1.
DR   GeneTree; ENSGT00550000074348; -.
DR   HOVERGEN; HBG056407; -.
DR   InParanoid; Q810C1; -.
DR   OMA; VICEAPT; -.
DR   OrthoDB; EOG428211; -.
DR   NextBio; 346195; -.
DR   ArrayExpress; Q810C1; -.
DR   Bgee; Q810C1; -.
DR   CleanEx; MM_SLITRK1; -.
DR   Genevestigator; Q810C1; -.
DR   GermOnline; ENSMUSG00000075478; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR000372; LRR-contain_N.
DR   Pfam; PF00560; LRR_1; 2.
DR   SMART; SM00369; LRR_TYP; 2.
DR   SMART; SM00082; LRRCT; 2.
DR   SMART; SM00013; LRRNT; 1.
DR   PROSITE; PS51450; LRR; 12.
PE   2: Evidence at transcript level;
KW   Leucine-rich repeat; Membrane; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     17       Potential.
FT   CHAIN        18    696       SLIT and NTRK-like protein 1.
FT                                /FTId=PRO_0000032674.
FT   TOPO_DOM     18    622       Extracellular (Potential).
FT   TRANSMEM    623    643       Helical; (Potential).
FT   TOPO_DOM    644    696       Cytoplasmic (Potential).
FT   REPEAT       57     80       LRR 1.
FT   REPEAT       81    104       LRR 2.
FT   REPEAT      105    128       LRR 3.
FT   REPEAT      130    152       LRR 4.
FT   REPEAT      153    176       LRR 5.
FT   REPEAT      178    200       LRR 6.
FT   REPEAT      214    237       LRR 7.
FT   REPEAT      374    397       LRR 8.
FT   REPEAT      399    421       LRR 9.
FT   REPEAT      423    445       LRR 10.
FT   REPEAT      446    469       LRR 11.
FT   REPEAT      470    493       LRR 12.
FT   REPEAT      495    517       LRR 13.
SQ   SEQUENCE   696 AA;  77817 MW;  B3F23AF1A28B9E1B CRC64;
     MLLWILLLET SLCFAAGNVT GDVCKEKICS CNEIEGDLHV DCEKKGFTSL QRFTAPTSQF
     YHLFLHGNSL TRLFPNEFAN FYNAVSLHME NNGLHEIVPG AFLGLQLVKR LHINNNKIKS
     FRKQTFLGLD DLEYLQADFN LLRDIDPGAF QDLNKLEVLI LNDNLISTLP ANVFQYVPIT
     HLDLRGNRLK TLPYEEVLEQ IPGIAEILLE DNPWDCTCDL LSLKEWLENI PKNALIGRVV
     CEAPTRLQGK DLNETTEQDL CPLKNRVDSS LPAPPAQEET FAPGPLPTPF KTNGQDEHAT
     PGAVPNGGTK IPGNWQLKIK PTPPIATGSA RNKPPVHGLP CPGGCSCDHI PGSGLKMNCN
     NRNVSSLADL KPKLSNVQEL FLRDNKIHSI RKSHFVDYKN LILLDLGNNN IANIENNTFK
     NLLDLRWLYM DSNYLDTLSR EKFAGLQNLE YLNVEYNAIQ LILPGTFNAM PKLRILILNN
     NLLRSLPVDV FAGVSLSKLS LHNNYFMYLP VAGVLDQLTS IIQIDLHGNP WECSCTIVPF
     KQWAERLGSE VLMSDLKCET PVNFFRKDFM LLSNEEICPQ LYARISPTLT SHSKNSTGLA
     ETGTHSNSYL DTSRVSISVL VPGLLLVFVT SAFTVVGMLV FILRNRKRSK RRDANSSASE
     INSLQTVCDS SYWHNGPYNA DGSHRVYDCG SHSLSD
//
ID   ZFYV1_MOUSE             Reviewed;         777 AA.
AC   Q810J8;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Zinc finger FYVE domain-containing protein 1;
GN   Name=Zfyve1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBUNIT: Binds to phosphatidylinositol-3-phosphate (PtdIns3P)
CC       through its FYVE-type zinc finger (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack (By
CC       similarity). Note=Resides predominantly in the cisternal stacks of
CC       the Golgi (By similarity).
CC   -!- SIMILARITY: Contains 2 FYVE-type zinc fingers.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC050015; AAH50015.1; -; mRNA.
DR   IPI; IPI00329871; -.
DR   UniGene; Mm.59257; -.
DR   ProteinModelPortal; Q810J8; -.
DR   SMR; Q810J8; 182-270, 595-658, 703-773.
DR   PRIDE; Q810J8; -.
DR   Ensembl; ENSMUST00000048319; ENSMUSP00000042224; ENSMUSG00000042628.
DR   MGI; MGI:3026685; Zfyve1.
DR   GeneTree; ENSGT00390000016097; -.
DR   HOGENOM; HBG314178; -.
DR   HOVERGEN; HBG057679; -.
DR   InParanoid; Q810J8; -.
DR   OrthoDB; EOG4DNF3T; -.
DR   ArrayExpress; Q810J8; -.
DR   Bgee; Q810J8; -.
DR   CleanEx; MM_ZFYVE1; -.
DR   Genevestigator; Q810J8; -.
DR   GermOnline; ENSMUSG00000042628; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005795; C:Golgi stack; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005545; F:1-phosphatidylinositol binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 2.
DR   Pfam; PF01363; FYVE; 2.
DR   SMART; SM00064; FYVE; 2.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 2.
DR   PROSITE; PS50178; ZF_FYVE; 2.
PE   2: Evidence at transcript level;
KW   Golgi apparatus; Metal-binding; Repeat; Zinc; Zinc-finger.
FT   CHAIN         1    777       Zinc finger FYVE domain-containing
FT                                protein 1.
FT                                /FTId=PRO_0000098714.
FT   ZN_FING     598    659       FYVE-type 1.
FT   ZN_FING     715    775       FYVE-type 2.
SQ   SEQUENCE   777 AA;  86956 MW;  B6BE08D473D04B9C CRC64;
     MSAQTSLAEK GLNPGLMCQE SYACSGTDEA IFECDECCSL QCLRCEEELH RQERLRNHER
     IRLKAGHVPY CDPCKGPNGH SPGVRQRAAV RCQTCKINLC LECQKRTHSG GNKRRHPITV
     YLVSKVQESL EGEEMDEETK RKKMTERVVS FLLVDENEEI QVTNEEDFIR KLDCKPDQHL
     KVVSVFGNTG DGKSHTLNHT FFYSREVFKT SPAQESCTVG VWAAYDPVHK VAVIDTEGLL
     GATVNLSQRT RLLLKVLAIS DLVIYRTHAD RLHNDLFKFL GDASEAYLKH FTKELKATTA
     RCGLDVPLST LGPAVIIFHE TVHTQLLGSD HPSEAPEKLI QDRFRKLGRF PEAFSSIHYK
     GTRTYNPPTD FSGLRRALEQ LLENNTTRSP RHPGVIFKAL KALSDRFSGE IPDDQMAHSS
     FFPDEYFTCS SLCLSCGAGC KNSMNHGKEG VPHEAKSRCR YSHQYDNRVY TCKACYERGK
     EVSVVPKTSA STDSPWMGLA KYAWSGYVIE CPNCGVVYRS RQYWFGNQDP VDTVVRTEIV
     HVWPGTDAFL KDNNNAAQRL LDGMNFMAQS VSELSLGPTK AVTSWLTDQI APAYWRPNSQ
     ILSCNQCATS FKDNDTKHHC RACGEGFCDS CSSKTRPVPE RGWGPAPVRV CDSCYDARNV
     QLDVTEAQAD DEGGTLIARK VGEAVQNTLG AVVTAIDIPL GLVKDAARPA YWVPDHEILH
     CHNCRKEFSV KLSKHHCRAC GQGFCDECSH DCRAVPSRGW DHPVRVCFNC NKKPGDL
//
ID   NFASC_MOUSE             Reviewed;        1240 AA.
AC   Q810U3;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Neurofascin;
DE   Flags: Precursor;
GN   Name=Nfasc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster; TISSUE=Brain;
RA   Dirks P., Montag-Sallaz M., Montag D.;
RT   "Expression patterns of L1-family cell recognition molecules L1, CHL1,
RT   NrCAM, and neurofascin in the mouse brain.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 96-104; 243-260; 335-355; 387-396; 493-509;
RP   573-585; 633-642; 681-719; 810-829 AND 1057-1076, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1226 AND SER-1227, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
CC   -!- FUNCTION: Cell adhesion, ankyrin-binding protein which may be
CC       involved in neurite extension, axonal guidance, synaptogenesis,
CC       myelination and neuron-glial cell interactions (By similarity).
CC   -!- SUBUNIT: Probable constituent of a neurofascin/NRCAM/ankyrin-G
CC       complex. Associates with the sodium channel beta-1 (SCN1B) and
CC       beta-3 (SCN3B) subunits. Interacts with GLDN/gliomedin (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC       L1/neurofascin/NgCAM family.
CC   -!- SIMILARITY: Contains 4 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 6 Ig-like C2-type (immunoglobulin-like)
CC       domains.
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DR   EMBL; AJ543322; CAD65849.1; -; mRNA.
DR   IPI; IPI00329927; -.
DR   RefSeq; NP_874385.1; NM_182716.4.
DR   UniGene; Mm.326702; -.
DR   ProteinModelPortal; Q810U3; -.
DR   SMR; Q810U3; 37-918.
DR   STRING; Q810U3; -.
DR   PhosphoSite; Q810U3; -.
DR   PRIDE; Q810U3; -.
DR   Ensembl; ENSMUST00000094569; ENSMUSP00000092148; ENSMUSG00000026442.
DR   GeneID; 269116; -.
DR   KEGG; mmu:269116; -.
DR   UCSC; uc007cpe.1; mouse.
DR   CTD; 269116; -.
DR   MGI; MGI:104753; Nfasc.
DR   GeneTree; ENSGT00590000082983; -.
DR   HOVERGEN; HBG000144; -.
DR   NextBio; 392698; -.
DR   ArrayExpress; Q810U3; -.
DR   Bgee; Q810U3; -.
DR   CleanEx; MM_NFASC; -.
DR   Genevestigator; Q810U3; -.
DR   GermOnline; ENSMUSG00000026442; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0033010; C:paranodal junction; IDA:MGI.
DR   GO; GO:0033270; C:paranode region of axon; IDA:BHF-UCL.
DR   GO; GO:0007411; P:axon guidance; IDA:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0030913; P:paranodal junction assembly; IMP:MGI.
DR   GO; GO:0071205; P:protein localization to juxtaparanode region of axon; IMP:MGI.
DR   GO; GO:0002175; P:protein localization to paranode region of axon; IMP:MGI.
DR   GO; GO:0050808; P:synapse organization; IMP:MGI.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 10.
DR   Pfam; PF00041; fn3; 4.
DR   Pfam; PF07679; I-set; 5.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 4.
DR   SUPFAM; SSF49265; FN_III-like; 4.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS50835; IG_LIKE; 6.
PE   1: Evidence at protein level;
KW   Cell adhesion; Cell membrane; Direct protein sequencing;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW   Phosphoprotein; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25   1240       Neurofascin.
FT                                /FTId=PRO_0000015050.
FT   TOPO_DOM     25   1110       Extracellular (Potential).
FT   TRANSMEM   1111   1131       Helical; (Potential).
FT   TOPO_DOM   1132   1240       Cytoplasmic (Potential).
FT   DOMAIN       41    137       Ig-like C2-type 1.
FT   DOMAIN      143    230       Ig-like C2-type 2.
FT   DOMAIN      244    332       Ig-like C2-type 3.
FT   DOMAIN      337    424       Ig-like C2-type 4.
FT   DOMAIN      430    517       Ig-like C2-type 5.
FT   DOMAIN      521    603       Ig-like C2-type 6.
FT   DOMAIN      628    720       Fibronectin type-III 1.
FT   DOMAIN      727    820       Fibronectin type-III 2.
FT   DOMAIN      825    918       Fibronectin type-III 3.
FT   DOMAIN     1008   1094       Fibronectin type-III 4.
FT   COMPBIAS    924   1006       Thr-rich.
FT   MOD_RES     471    471       Phosphoserine (By similarity).
FT   MOD_RES     481    481       Phosphotyrosine (By similarity).
FT   MOD_RES     485    485       Phosphoserine (By similarity).
FT   MOD_RES    1226   1226       Phosphoserine.
FT   MOD_RES    1227   1227       Phosphoserine.
FT   CARBOHYD    305    305       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    409    409       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    446    446       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    483    483       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    752    752       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    778    778       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    866    866       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    881    881       N-linked (GlcNAc...) (Potential).
FT   DISULFID     63    118       Potential.
FT   DISULFID    162    213       Potential.
FT   DISULFID    268    316       Potential.
FT   DISULFID    358    408       Potential.
FT   DISULFID    452    501       Potential.
FT   DISULFID    543    592       Potential.
SQ   SEQUENCE   1240 AA;  137975 MW;  6DE8935B5B02E965 CRC64;
     MARQQAPPWV HIALILFLLS LGGAIEIPMD PSIQNELTQP PTITKQSVKD HIVDPRDNIL
     IECEAKGNPA PSFHWTRNSR FFNIAKDPRV SMRRRSGTLV IDFRSGGRPE EYEGEYQCFA
     RNKFGTALSN RIRLQVSKSP LWPKENLDPV VVQEGAPLTL QCNPPPGLPS PVIFWMSSSM
     EPITQDKRVS QGHNGDLYFS NVMLQDMQTD YSCNARFHFT HTIQQKNPFT LKVLTTRGVA
     ERTPSFMYPQ GTSSSQMVLR GMDLLLECIA SGVPTPDIAW YKKGGDLPSN KAKFENFNKA
     LRITNVSEED SGEYFCLASN KMGSIRHTIS VRVKAAPYWL DEPKNLILAP GEDGRLVCRA
     NGNPKPTVQW MVNGEPLQSA PPNPNREVAG DTIIFRDTQI SSRAVYQCNT SNEHGYLLAN
     AFVSVLDVPP RMLSARNQLI RVILYNRTRL DCPFFGSPIP TLRWFKNGQG SNLDGGNYHV
     YENGSLEIKM IRKEDQGIYT CVATNILGKA ENQVRLEVKD PTRIYRMPED QVAKRGTTVQ
     LECRVKHDPS LKLTVSWLKD DEPLYIGNRM KKEDDSLTIF GVAERDQGSY TCMASTELDQ
     DLAKAYLTVL ADQATPTNRL AALPKGRPDR PRDLELTDLA ERSVRLTWIP GDDNNSPITD
     YVVQFEEDQF QPGVWHDHSR FPGSVNSAVL HLSPYVNYQF RVIAVNEVGS SHPSLPSERY
     RTSGAPPESN PSDVKGEGTR KNNMEITWTP MNATSAFGPN LRYIVKWRRR ETRETWNNVT
     VWGSRYVVGQ TPVYVPYEIR VQAENDFGKG PEPDTIIGYS GEDLPSAPRR FRVRQPNLET
     INLEWDHPEH PNGILIGYIL RYVPFNGTKL GKQMVENFSP NQTKFSVQRA DPVSRYRFSL
     SARTQVGSGE AATEESPAPP NEATPTAAPP TLPPTTVGTT GLVSSTDATA LAATSEATTV
     PIIPTVVPTT VATTIATTTT TTAATTTTTT TESPPTTTAG TKIHETAPDE QSIWNVTVLP
     NSKWANITWK HNFRPGTDFV VEYIDSNHTK KTVPVKAQAQ PIQLTDLFPG MTYTLRVYSR
     DNEGISSTVI TFMTSTAYTN NQADIATQGW FIGLMCAIAL LVLILLIVCF IKRSRGGKYP
     VREKKDVPLG PEDPKEEDGS FDYSDEDNKP LQGSQTSLDG TIKQQESDDS LVDYGEGGEG
     QFNEDGSFIG QYTVKKDKEE TEGNESSEAT SPVNAIYSLA
//
ID   NRCAM_MOUSE             Reviewed;        1256 AA.
AC   Q810U4; Q80U33; Q8BLG8; Q8BX92; Q8BYJ8;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2003, sequence version 2.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Neuronal cell adhesion molecule;
DE            Short=Nr-CAM;
DE   AltName: Full=Neuronal surface protein Bravo;
DE            Short=mBravo;
DE   AltName: Full=NgCAM-related cell adhesion molecule;
DE            Short=Ng-CAM-related;
DE   Flags: Precursor;
GN   Name=Nrcam; Synonyms=Kiaa0343;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=Swiss Webster; TISSUE=Brain;
RA   Dirks P., Montag-Sallaz M., Montag D.;
RT   "Expression patterns of L1-family cell recognition molecules L1, CHL1,
RT   NrCAM, and neurofascin in the mouse brain.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1094-1256 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PROTEIN SEQUENCE OF 432-449 AND 705-723, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   FUNCTION, AND INTERACTION WITH GLDN.
RX   PubMed=16039564; DOI=10.1016/j.neuron.2005.06.026;
RA   Eshed Y., Feinberg K., Poliak S., Sabanay H., Sarig-Nadir O.,
RA   Spiegel I., Bermingham J.R. Jr., Peles E.;
RT   "Gliomedin mediates Schwann cell-axon interaction and the molecular
RT   assembly of the nodes of Ranvier.";
RL   Neuron 47:215-229(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1247, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1178, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Cell adhesion, ankyrin-binding protein involved in
CC       neuron-neuron adhesion. May play a role in the molecular assembly
CC       of the nodes of Ranvier.
CC   -!- SUBUNIT: Probable constituent of a neurofascin/NRCAM/ankyrin-G
CC       complex (By similarity). Interacts with GLDN/gliomedin.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q810U4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q810U4-2; Sequence=VSP_008926, VSP_008927;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q810U4-3; Sequence=VSP_008930;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q810U4-4; Sequence=VSP_008923, VSP_008925;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q810U4-5; Sequence=VSP_008921, VSP_008922, VSP_008924;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC       L1/neurofascin/NgCAM family.
CC   -!- SIMILARITY: Contains 4 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 6 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65534.1; Type=Erroneous initiation;
CC       Sequence=CAD65848.1; Type=Erroneous initiation;
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DR   EMBL; AJ543321; CAD65848.1; ALT_INIT; mRNA.
DR   EMBL; AK122252; BAC65534.1; ALT_INIT; mRNA.
DR   EMBL; AK039322; BAC30318.1; -; mRNA.
DR   EMBL; AK048567; BAC33377.1; -; mRNA.
DR   EMBL; AK045259; BAC32284.1; -; mRNA.
DR   IPI; IPI00226573; -.
DR   IPI; IPI00338880; -.
DR   IPI; IPI00395042; -.
DR   IPI; IPI00395043; -.
DR   IPI; IPI00403536; -.
DR   RefSeq; NP_001139503.1; NM_001146031.1.
DR   RefSeq; NP_795904.3; NM_176930.4.
DR   UniGene; Mm.208439; -.
DR   ProteinModelPortal; Q810U4; -.
DR   SMR; Q810U4; 36-1035.
DR   MINT; MINT-3090404; -.
DR   STRING; Q810U4; -.
DR   PhosphoSite; Q810U4; -.
DR   PRIDE; Q810U4; -.
DR   Ensembl; ENSMUST00000020939; ENSMUSP00000020939; ENSMUSG00000020598.
DR   Ensembl; ENSMUST00000110748; ENSMUSP00000106376; ENSMUSG00000020598.
DR   Ensembl; ENSMUST00000110750; ENSMUSP00000106378; ENSMUSG00000020598.
DR   Ensembl; ENSMUST00000110751; ENSMUSP00000106379; ENSMUSG00000020598.
DR   GeneID; 319504; -.
DR   KEGG; mmu:319504; -.
DR   UCSC; uc007nls.1; mouse.
DR   UCSC; uc007nlt.1; mouse.
DR   UCSC; uc007nlu.1; mouse.
DR   UCSC; uc007nlv.1; mouse.
DR   UCSC; uc007nlw.1; mouse.
DR   CTD; 319504; -.
DR   MGI; MGI:104750; Nrcam.
DR   GeneTree; ENSGT00590000082983; -.
DR   HOVERGEN; HBG000144; -.
DR   OMA; SPLWTKE; -.
DR   OrthoDB; EOG4GTKC3; -.
DR   NextBio; 394866; -.
DR   ArrayExpress; Q810U4; -.
DR   Bgee; Q810U4; -.
DR   CleanEx; MM_NRCAM; -.
DR   Genevestigator; Q810U4; -.
DR   GermOnline; ENSMUSG00000020598; Mus musculus.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0030506; F:ankyrin binding; ISS:UniProtKB.
DR   GO; GO:0007411; P:axon guidance; IDA:UniProtKB.
DR   GO; GO:0016337; P:cell-cell adhesion; IDA:UniProtKB.
DR   GO; GO:0007417; P:central nervous system development; IDA:UniProtKB.
DR   GO; GO:0045162; P:clustering of voltage-gated sodium channels; ISS:UniProtKB.
DR   GO; GO:0019227; P:neuronal action potential propagation; IMP:MGI.
DR   GO; GO:0008104; P:protein localization; IDA:MGI.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003006; Ig/MHC_CS.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 11.
DR   Pfam; PF00041; fn3; 4.
DR   Pfam; PF07679; I-set; 5.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 5.
DR   SUPFAM; SSF49265; FN_III-like; 4.
DR   PROSITE; PS50853; FN3; 5.
DR   PROSITE; PS50835; IG_LIKE; 6.
DR   PROSITE; PS00290; IG_MHC; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Cell membrane;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Phosphoprotein; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     29       Potential.
FT   CHAIN        30   1256       Neuronal cell adhesion molecule.
FT                                /FTId=PRO_0000015058.
FT   TOPO_DOM     30   1119       Extracellular (Potential).
FT   TRANSMEM   1120   1142       Helical; (Potential).
FT   TOPO_DOM   1143   1256       Cytoplasmic (Potential).
FT   DOMAIN       40    128       Ig-like C2-type 1.
FT   DOMAIN      135    229       Ig-like C2-type 2.
FT   DOMAIN      261    350       Ig-like C2-type 3.
FT   DOMAIN      355    442       Ig-like C2-type 4.
FT   DOMAIN      448    535       Ig-like C2-type 5.
FT   DOMAIN      539    626       Ig-like C2-type 6.
FT   DOMAIN      641    733       Fibronectin type-III 1.
FT   DOMAIN      740    834       Fibronectin type-III 2.
FT   DOMAIN      839    940       Fibronectin type-III 3.
FT   DOMAIN      946   1040       Fibronectin type-III 4.
FT   MOD_RES     421    421       Phosphoserine.
FT   MOD_RES    1178   1178       Phosphoserine.
FT   MOD_RES    1247   1247       Phosphoserine.
FT   CARBOHYD     77     77       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    217    217       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    239    239       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    245    245       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    270    270       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    308    308       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    371    371       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    427    427       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    501    501       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    613    613       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    710    710       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    796    796       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    852    852       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    987    987       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1003   1003       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1013   1013       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1067   1067       N-linked (GlcNAc...) (Potential).
FT   DISULFID     62    117       Potential.
FT   DISULFID    161    212       Potential.
FT   DISULFID    286    334       Potential.
FT   DISULFID    376    426       Potential.
FT   DISULFID    470    519       Potential.
FT   DISULFID    561    610       Potential.
FT   VAR_SEQ      35     35       D -> DPKLLHD (in isoform 5).
FT                                /FTId=VSP_008921.
FT   VAR_SEQ     235    254       VDELNDTIAANLSDTEFYGA -> GKSSASGLSFNGVYLCG
FT                                SNY (in isoform 5).
FT                                /FTId=VSP_008922.
FT   VAR_SEQ     254    259       AKSSKE -> GELQWL (in isoform 4).
FT                                /FTId=VSP_008923.
FT   VAR_SEQ     255   1256       Missing (in isoform 5).
FT                                /FTId=VSP_008924.
FT   VAR_SEQ     260   1256       Missing (in isoform 4).
FT                                /FTId=VSP_008925.
FT   VAR_SEQ     629    638       Missing (in isoform 2).
FT                                /FTId=VSP_008926.
FT   VAR_SEQ    1045   1107       AGIPPPDVGAGKGKEEWRKEIVNGSRSFFGLKGLMPGTAYK
FT                                VRVGAEGDSGFVSSEDVFETGP -> GKK (in isoform
FT                                2).
FT                                /FTId=VSP_008927.
FT   VAR_SEQ    1177   1177       Y -> YRSFE (in isoform 3).
FT                                /FTId=VSP_008930.
SQ   SEQUENCE   1256 AA;  138522 MW;  F3F698C2AF3FCFFA CRC64;
     MQLKIMPKKK HLSAGGVPLI LFLCQMISAL DVPLDLVQPP TITQQSPKDY IIDPRENIVI
     QCEAKGKPPP SFSWTRNGTH FDIDKDPLVT MKPGSGTLVI NIMSEGKAET YEGVYQCTAR
     NERGAAVSNN IVVRPSRSPL WTKERLEPIV LQNGQSLVLP CRPPIGLPPA IIFWMDNSFQ
     RLPQSERVSQ GLNGDLYFSN VLPEDTREDY ICYARFNHTQ TIQQKQPISL KVISVDELND
     TIAANLSDTE FYGAKSSKER PPTFLTPEGN ESHKEELRGN VLSLECIAEG LPTPIIYWIK
     EDGMLPANRT FYRNFKKTLQ ITHVSEADSG NYQCIAKNAL GAVHHTISVT VKAAPYWIVA
     PQNLVLSPGE NGTLICRANG NPKPRISWLT NGVPIEIALD DPSRKIDGDT IIFSNVQESS
     SAVYQCNASN KYGYLLANAF VNVLAEPPRI LTSANTLYQV IANRPALLDC AFFGSPMPTI
     EWFKGTKGSA LHEDIYVLHD NGTLEIPVAQ KDSTGTYTCV ARNKLGMAKN EVHLEIKDPT
     RIIKQPEYAV VQRGSKVSFE CRVKHDHTLI PTIMWLKDNG ELPNDERFST DKDHLVVSDV
     KDDDGGTYTC TANTTLDSAS ASAVLRVVAP TPTPAPIYDV PNPPFDLELT NQLDKSVQLT
     WTPGDDNNSP ITKFIIEYED AMHDAGLWRH QAEVSGTQTT AQLKLSPYVN YSFRVMAENS
     IGRSMPSEAS EQYLTKAAEP DQNPMAVEGL GTEPDNLVIT WKPLNGFQSN GPGLQYKVSW
     RQKDGDDEWT SVVVANVSKY IVSGTPTFVP YLIKVQALND VGFAPEPAAV MGHSGEDLPM
     VAPGNVRVSV VNSTLAEVHW DPVPPKSVRG HLQGYRIYYW KTQSSSKRNR RHIEKKILTF
     QGTKTHGMLP GLQPYSHYAL NVRVVNGKGE GPASTDRGFH TPEGVPSAPS SLKIVNPTLD
     SLTLEWDPPS HPNGILTEYI LQYQPINSTH ELGPLVDLKI PANKTRWTLK NLNFSTRYKF
     YFYAQTSVGP GSQITEEAIT TVDEAGIPPP DVGAGKGKEE WRKEIVNGSR SFFGLKGLMP
     GTAYKVRVGA EGDSGFVSSE DVFETGPAMA SRQVDIATQG WFIGLMCAVA LLILILLIVC
     FIRRNKGGKY PVKEKEDAHA DPEIQPMKED DGTFGEYSDA EDHKPLKKGS RTPSDRTVKK
     EDSDDSLVDY GEGVNGQFNE DGSFIGQYSG KKEKEPAEGN ESSEAPSPVN AMNSFV
//
ID   MPP10_MOUSE             Reviewed;         681 AA.
AC   Q810V0;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=U3 small nucleolar ribonucleoprotein protein MPP10;
DE   AltName: Full=M phase phosphoprotein 10;
GN   Name=Mphosph10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244 AND SER-247, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Component of the 60-80S U3 small nucleolar
CC       ribonucleoprotein (U3 snoRNP). Required for the early cleavages
CC       during pre-18S ribosomal RNA processing (By similarity).
CC   -!- SUBUNIT: Component of a heterotrimeric complex containing IMP3,
CC       IMP4 and MPHOSPH10. Interacts with IMP3 and IMP4 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity).
CC       Chromosome (By similarity). Note=Fibrillar region of the
CC       nucleolus. After dissolution of the nucleolus in early M phase
CC       becomes associated with chromosomes through metaphase and
CC       anaphase. In telophase localized to small cellular prenucleolar
CC       bodies that not always contain fibrillarin. The reassociation with
CC       nucleolus is preceeded by the arrival of fibrillarin (By
CC       similarity).
CC   -!- PTM: Phosphorylated in M (mitotic) phase (By similarity).
CC   -!- SIMILARITY: Belongs to the MPP10 family.
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DR   EMBL; BC049270; AAH49270.1; -; mRNA.
DR   IPI; IPI00402911; -.
DR   UniGene; Mm.26973; -.
DR   STRING; Q810V0; -.
DR   PhosphoSite; Q810V0; -.
DR   PRIDE; Q810V0; -.
DR   Ensembl; ENSMUST00000032735; ENSMUSP00000032735; ENSMUSG00000030521.
DR   UCSC; uc009hgg.1; mouse.
DR   MGI; MGI:1915223; Mphosph10.
DR   HOGENOM; HBG505735; -.
DR   HOVERGEN; HBG052502; -.
DR   InParanoid; Q810V0; -.
DR   OrthoDB; EOG4ZKJMS; -.
DR   ArrayExpress; Q810V0; -.
DR   Bgee; Q810V0; -.
DR   Genevestigator; Q810V0; -.
DR   GermOnline; ENSMUSG00000030521; Mus musculus.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR007151; Mpp10.
DR   InterPro; IPR012173; snoRNP_Mpp10.
DR   PANTHER; PTHR17039; Mpp10; 1.
DR   Pfam; PF04006; Mpp10; 1.
DR   PIRSF; PIRSF017300; snoRNP_Mpp10; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chromosome; Coiled coil; Nucleus; Phosphoprotein;
KW   Ribonucleoprotein; Ribosome biogenesis; rRNA processing.
FT   CHAIN         1    681       U3 small nucleolar ribonucleoprotein
FT                                protein MPP10.
FT                                /FTId=PRO_0000121536.
FT   COILED      109    139       Potential.
FT   COILED      349    383       Potential.
FT   COILED      471    491       Potential.
FT   COILED      575    604       Potential.
FT   COMPBIAS    292    298       Poly-Glu.
FT   COMPBIAS    666    671       Poly-Lys.
FT   MOD_RES      61     61       Phosphoserine (Potential).
FT   MOD_RES     120    120       Phosphoserine (By similarity).
FT   MOD_RES     140    140       Phosphoserine (By similarity).
FT   MOD_RES     164    164       Phosphoserine.
FT   MOD_RES     168    168       Phosphoserine (By similarity).
FT   MOD_RES     172    172       Phosphoserine.
FT   MOD_RES     244    244       Phosphoserine.
FT   MOD_RES     247    247       Phosphoserine.
FT   MOD_RES     277    277       Phosphoserine (By similarity).
FT   MOD_RES     609    609       N6-acetyllysine (By similarity).
SQ   SEQUENCE   681 AA;  78675 MW;  131EEA3B10D94AF7 CRC64;
     MAPRVFRRQT LERCLREIRK ATNRPECFLT IQNGLASNFT SLTKVLYDFN KVLENGRISG
     SPLQKLEINS FDDEQIWQQL ELQNEPVLQY FQNAVSETIE DEDISLLPEC EDEECEEDAS
     EVEADNQENL ETDLEEEQLS DEGGDVPKGR DRAKSSRKSD PRKSPVFSDE DSDLDFDIGK
     LEQQTKMQIK PPGKPREKSV VDDKFFKLSE MESFLEKVEK EEEKRPDGEE EDEEDIDLFE
     DIDSDESEGG LFGRQKIKSN KSSRNLKYKD FFDPVESDED ITGVDEELGP DEEKEEEEGF
     AEEADESISD TDEDNDLEED ENSDQHKGGL KRVTFALPDD EAEDTSPLAV KQESDEVKSS
     FEKRQEKMNE KIASLEKELL DKKPWQLQGE VTAQKRPENS LLEETLHFDH AVRMAPVITE
     ETTLHLEDII KQRIRDQAWD DVERKEKPKE DAYEYKKRLT LDHEKSKLSL AEIYEQEYLK
     LNQQKTAEED NPEHVEIQKM MDSLFLKLDA LSNFHFIPKP PVPEIKVVSN LPAITMEEVA
     PVSVSDAALL APEEIKEKNK AGDLKTAAEK TATDKKRERR KKKYQKRLKI KEKEKRKKLL
     EKNNPDQSKS SRAAASEKLK QLTKTGKVSL LKDERKDKPL KSSQAFFSKL QDQVKMQIND
     AKQPEKIKKK KQDISVHKLK L
//
ID   ANR26_MOUSE             Reviewed;        1581 AA.
AC   Q811D2; Q69ZS2; Q9CS61;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Ankyrin repeat domain-containing protein 26;
GN   Name=Ankrd26; Synonyms=Kiaa1074;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-729, AND VARIANTS ASN-114;
RP   ALA-142 AND ILE-218.
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-528, AND VARIANTS HIS-399
RP   AND SER-450.
RC   STRAIN=C57BL/6J; TISSUE=Mammary tumor;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 539-1581.
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   IDENTIFICATION.
RX   PubMed=16364570; DOI=10.1016/j.gene.2005.07.045;
RA   Hahn Y., Bera T.K., Pastan I.H., Lee B.;
RT   "Duplication and extensive remodeling shaped POTE family genes
RT   encoding proteins containing ankyrin repeat and coiled coil domains.";
RL   Gene 366:238-245(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SIMILARITY: Contains 5 ANK repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC047067; AAH47067.1; ALT_SEQ; mRNA.
DR   EMBL; AK017783; BAB30930.1; -; mRNA.
DR   EMBL; AK173096; BAD32374.1; -; Transcribed_RNA.
DR   IPI; IPI00464279; -.
DR   UniGene; Mm.276116; -.
DR   ProteinModelPortal; Q811D2; -.
DR   SMR; Q811D2; 48-204.
DR   STRING; Q811D2; -.
DR   PhosphoSite; Q811D2; -.
DR   PRIDE; Q811D2; -.
DR   Ensembl; ENSMUST00000007971; ENSMUSP00000007971; ENSMUSG00000007827.
DR   UCSC; uc009dlr.1; mouse.
DR   MGI; MGI:1917887; Ankrd26.
DR   eggNOG; roNOG04956; -.
DR   GeneTree; ENSGT00560000076605; -.
DR   HOVERGEN; HBG079895; -.
DR   OrthoDB; EOG4JT04K; -.
DR   ArrayExpress; Q811D2; -.
DR   Bgee; Q811D2; -.
DR   CleanEx; MM_ANKRD26; -.
DR   Genevestigator; Q811D2; -.
DR   GermOnline; ENSMUSG00000007827; Mus musculus.
DR   GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:MGI.
DR   GO; GO:0046621; P:negative regulation of organ growth; IMP:MGI.
DR   GO; GO:0019217; P:regulation of fatty acid metabolic process; IMP:MGI.
DR   GO; GO:0060259; P:regulation of feeding behavior; IMP:MGI.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR021885; DUF3496.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 2.
DR   Pfam; PF12001; DUF3496; 1.
DR   SMART; SM00248; ANK; 4.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
PE   1: Evidence at protein level;
KW   ANK repeat; Coiled coil; Phosphoprotein; Polymorphism; Repeat.
FT   CHAIN         1   1581       Ankyrin repeat domain-containing protein
FT                                26.
FT                                /FTId=PRO_0000240844.
FT   REPEAT       46     76       ANK 1.
FT   REPEAT       80    109       ANK 2.
FT   REPEAT      113    142       ANK 3.
FT   REPEAT      146    175       ANK 4.
FT   REPEAT      179    208       ANK 5.
FT   COILED      715    845       Potential.
FT   COILED      876   1345       Potential.
FT   COILED     1396   1470       Potential.
FT   COILED     1521   1550       Potential.
FT   MOD_RES     239    239       Phosphoserine.
FT   MOD_RES     282    282       Phosphothreonine (By similarity).
FT   VARIANT     114    114       S -> N.
FT   VARIANT     142    142       V -> A.
FT   VARIANT     218    218       M -> I.
FT   VARIANT     399    399       D -> H.
FT   VARIANT     450    450       N -> S.
FT   CONFLICT    469    469       M -> MGMEKN (in Ref. 2; BAB30930).
FT   CONFLICT    476    476       V -> A (in Ref. 2; BAB30930).
FT   CONFLICT    527    527       K -> R (in Ref. 2; BAB30930).
FT   CONFLICT    601    601       A -> V (in Ref. 1; AAH47067).
FT   CONFLICT    604    604       A -> T (in Ref. 1; AAH47067).
SQ   SEQUENCE   1581 AA;  180647 MW;  6C298F79B3731DC9 CRC64;
     MKKIFGFRSK GPSPLGPSAR PRSNCVGFGR ESASGSHVPR YHIHDKDMGK IHKAASVGDV
     AKVQHILILG KSGVNDRDKK DRTALHLACA YGHPEVVTLL VERKCEIDAR DSESSTALIK
     AVQCQEEECA AILLDHGADP NVMDSSGNTA LHYAVYSENT SMAAKLLAHN ANIEAKNKDD
     LTPMLLAVKE NKQHIVEFLV KKKASIHAVD QLGSNRQMFE YDGKRLQRSE NSNPVDNGSE
     DGSLTRSYNT PGPADSWPTS DEEDYNFDNK NVPKINLTEL WTAAQQSRKN QTKCGFEELD
     NGARFDDSDS PSESEDAIEV EPAPSVRVQT LSPSRQSPDP VEGATELAIE GEENGTDVIE
     SASQEQPNHD NLTRADGWHK SNKSEMMSAL GLGEDEDEDS PWDSESISES VSLKDVGHFS
     GTADQTGKRR AHGQIEDVTY IPSCMSGSRN FKMAKLEESR NVGLPVAHME APRKYVIMEP
     TIERRAPVLN KTETVGMTDA QTFKSEPESV SREEQTRLSG SEDSQQKVEE KRKYKNNEAE
     PSGNLYSGAA DGGADVKPQS GDTENQQSPR EGSEGRGSGP ALLMKEAKKM ENEKWVSREP
     ARTAMSERTG LPTGGWPQMQ DGSCWSDTDQ SEARPTKKTS SKHNKDSGQT AAVDNLDDFT
     ESSETASEDH ELQGPDSESI LCAIEHLRLE CKDTASLLKI RDAVYSYKRL IELKRSHCEL
     LTGKLKRMEN KYKGLQKEMS ETEEVKSRLE HEKVGWEQEL CRLRFALKQE EEKRRSADQL
     SEKTMEQLRR KGEQCQSEVE ARQQLEASLR TLEMELKTVK SHLNQVLEER NETQRQLSRE
     QNARMLQDGI LASHLCKQKE IEMTQKKMTS EVSVSHEKEK DLLHKNQRLQ DEVAVLRLEM
     DTIKSHNQEK EKRYLEDIKI ANEKNDNLQR MVKLNMLSSK LDNEKQNKER LETDVESFRS
     RLASALHDHA EIQTAKRDLE IAFQRARDEW FRVKDKMNFD MSNLRDNNEV LSQQLSKTER
     KLNSLEIEFH HTKDELREKT LALKHAQRDL SQTQCQMKEV EHMFQDEQGK VSKFMGKQES
     IEERLAQLQS ENTLLRQQLD DAANKAESKD KTIVNIQDQF QDVLTRFQAE SQRHSLRLED
     RNQELVSECS HLRERLCQYE NEKAEREVVV RQLQQELADT LKKQSMSEAS LEVSSRYRSN
     LEEEARDLKK KLGQLRSQLQ EARDQHREAV HHAEKMEDHL QKLELEKSKF EITIKKQSEE
     IDQLQENLSR VNLSEEDKEK LQKLTELKES LECTVDQEQK RSSALEKELM RTIQKKCGKL
     EKNKKQLEQE VVNLRSHMEK NMVEHSQAQQ YAREVEERAR QDLVEKLKQV NLFLQAQAAS
     QESLEQLREN SNASVRSQME LRIKDLESQL YRMKAQEDFD KIELEKYKQL YQEEFRARKS
     LSSKLNKTSE KLEEASSKLL LEEQQNRSLL STLSTRPVVE CPCVGSLHNS LVFNRTLIPR
     ENIVVPTSGL QPSNKRVEIY LTKMHQELEK SINRELKEAT AELESEFCRV SPLGSATKAS
     QDQLSDASQE FIDILKKKYM I
//
ID   MAST4_MOUSE             Reviewed;        2618 AA.
AC   Q811L6; Q3UVE7; Q62489; Q6ZQE0; Q8BME3;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Microtubule-associated serine/threonine-protein kinase 4;
DE            EC=2.7.11.1;
GN   Name=Mast4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Cerebellum, and Wolffian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 522-2618 (ISOFORM 2).
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1671-2618 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2398-2498 (ISOFORM 1).
RC   TISSUE=Cochlea;
RX   MEDLINE=97237053; PubMed=9119401; DOI=10.1006/geno.1996.4526;
RA   Crozet F., El-Amraoui A., Blanchard S., Lenoir M., Ripoll C., Vago P.,
RA   Hamel C., Fizames C., Levi-Acobas F., Depetris D., Mattei M.-G.,
RA   Weil D., Pujol R., Petit C.;
RT   "Cloning of the genes encoding two murine and human cochlear
RT   unconventional type I myosins.";
RL   Genomics 40:332-341(1997).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1521, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q811L6-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q811L6-2; Sequence=VSP_052478, VSP_052479, VSP_052480;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH42511.1; Type=Erroneous initiation;
CC       Sequence=AK090136; Type=Frameshift; Positions=1682;
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DR   EMBL; AK032755; BAC28008.1; -; mRNA.
DR   EMBL; AK090136; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK137360; BAE23322.1; -; mRNA.
DR   EMBL; AC112791; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC124387; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AC165290; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC042511; AAH42511.1; ALT_INIT; mRNA.
DR   EMBL; AK129114; BAC97924.1; -; mRNA.
DR   EMBL; Z78145; CAB01547.1; -; mRNA.
DR   IPI; IPI00346104; -.
DR   IPI; IPI00465600; -.
DR   UniGene; Mm.202606; -.
DR   UniGene; Mm.447520; -.
DR   UniGene; Mm.461754; -.
DR   HSSP; P31751; 1MRY.
DR   ProteinModelPortal; Q811L6; -.
DR   SMR; Q811L6; 379-479, 564-872, 1138-1229.
DR   PhosphoSite; Q811L6; -.
DR   PRIDE; Q811L6; -.
DR   Ensembl; ENSMUST00000091273; ENSMUSP00000088817; ENSMUSG00000034751.
DR   Ensembl; ENSMUST00000099202; ENSMUSP00000096808; ENSMUSG00000034751.
DR   MGI; MGI:1918885; Mast4.
DR   eggNOG; roNOG05919; -.
DR   GeneTree; ENSGT00530000063286; -.
DR   HOGENOM; HBG506781; -.
DR   HOVERGEN; HBG108118; -.
DR   InParanoid; Q811L6; -.
DR   OrthoDB; EOG4255S2; -.
DR   BRENDA; 2.7.11.1; 244.
DR   ArrayExpress; Q811L6; -.
DR   Bgee; Q811L6; -.
DR   Genevestigator; Q811L6; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR015022; MA_Ser/thr_Kinase_dom.
DR   InterPro; IPR023142; MAST_pre-PK_dom.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF08926; DUF1908; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Kinase; Magnesium;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1   2618       Microtubule-associated serine/threonine-
FT                                protein kinase 4.
FT                                /FTId=PRO_0000293629.
FT   DOMAIN      568    841       Protein kinase.
FT   DOMAIN      842    904       AGC-kinase C-terminal.
FT   DOMAIN     1139   1227       PDZ.
FT   NP_BIND     574    582       ATP (By similarity).
FT   ACT_SITE    691    691       Proton acceptor (By similarity).
FT   BINDING     597    597       ATP (By similarity).
FT   MOD_RES    1417   1417       Phosphoserine (By similarity).
FT   MOD_RES    1521   1521       Phosphoserine.
FT   MOD_RES    1909   1909       Phosphothreonine (By similarity).
FT   MOD_RES    1913   1913       Phosphoserine (By similarity).
FT   MOD_RES    2549   2549       Phosphoserine (By similarity).
FT   VAR_SEQ    1030   1096       Missing (in isoform 2).
FT                                /FTId=VSP_052478.
FT   VAR_SEQ    1263   1282       SLFKKLAKQPSPLLHTSRSF -> DRKKKKKRELSSRCLPS
FT                                SNR (in isoform 2).
FT                                /FTId=VSP_052479.
FT   VAR_SEQ    1283   2618       Missing (in isoform 2).
FT                                /FTId=VSP_052480.
FT   CONFLICT    546    546       M -> T (in Ref. 3; AAH42511).
FT   CONFLICT   1963   1963       A -> T (in Ref. 4; BAC97924).
FT   CONFLICT   1977   1977       K -> I (in Ref. 1; BAC28008).
FT   CONFLICT   2143   2143       S -> G (in Ref. 1; BAC28008).
FT   CONFLICT   2181   2181       A -> ATA (in Ref. 4; BAC97924).
FT   CONFLICT   2444   2444       S -> G (in Ref. 1; BAC28008).
FT   CONFLICT   2507   2507       D -> E (in Ref. 1; BAE23322).
SQ   SEQUENCE   2618 AA;  284052 MW;  2D70C374B37CEAEC CRC64;
     MGEKVSEAPE PVPRGCSGHG ARTLFSSAAA VSSEGASSAE SSSGSETLSE EGEPSRFSCR
     SQPPRPPGGA LGTRLPAAWA PARVALERGV PTLPLPHPGG AVLPVPQVSS ASQEEQDEEL
     DHILSPPPMP FRKCSNPDVA CGLGKSLKYK RQLSEDGKQL RRGSLGGALT GRYLLPNPVA
     GQAWPASAET SNLVRMRSQA LGQSAPSLTA SLKELSLPRR GSLCRTSNRK SLIGNGQSPA
     LPRPHSPLSA HAGNSPQDSP RNFSPSASAH FSFARRTDGR RWSLASLPSS GYGTNTPSST
     VSSSCSSQEK LHQLPYQPTP DELHFLSKHF CTTESIATEN RCRNTPMRPR SRSLSPGRSP
     ACCDHEIIMM NHVYKERFPK ATAQMEERLK EIITSYSPDH VLPLADGVLS FTHHQIIELA
     RDCLDKSHQG LITSRYFFEL QHKLDKLLQE AHDRSESGEL AFIKQLVRKI LIVIARPARL
     LECLEFDPEE FYYLLEAAEG HAKEGQGIKT DIPRYIISQL GLNKDPLEEM AQLGNYDSRT
     AETPEMDESV SSSNTSLRLR RKPRESDFET IKLISNGAYG AVYFVRHKES RQRFAMKKIN
     KQNLILRNQI QQAFVERDIL TFAENPFVVS MYCSFETRRH LCMVMEYVEG GDCATLMKNM
     GPLPVDMARM YFAETVLALE YLHNYGIVHR DLKPDNLLVT SMGHIKLTDF GLSKVGLMSM
     TTNLYEGHIE KDAREFLDKQ VCGTPEYIAP EVILRQGYGK PVDWWAMGII LYEFLVGCVP
     FFGDTPEELF GQVISDEINW PEKDEAPPPD AQELITLLLR QNPLERLGTG GAYEVKQHRF
     FRSLDWNSLL RQKAEFIPQL ESEDDTSYFD TRSEKYHHME TEEEDDTNDE DFTVEIRQFS
     SCSHRFSKVF SSIDRITQNS GEDKDDSEDK TKSTTLPSTE TLSWSSEYSE MQQLSTSNSS
     DTESNRCKLS SGLLPKLAIS TDGEQDEAVP CSGDPREEPE KPVPPSEECT QEEPEVTTPA
     STISSSTLSV GSFSEHLDQI NGRSECVDST DNSSKPSSEP TSHVARQRLE STEKKKISGK
     VTKSLSASAL SLMIPGDMFA VSPLGSPMSP HSLSSDPSSS RDSSPSRDSS AASASPHQPI
     VIHSSGKNYG FTIRAIRVYV GDSDIYTVHH IVWNVEEGSP AYQAGLKAGD LITHINGEPV
     HGLVHTEVIE LLLKSGNKVS ITTTPFENTS IKTGPARRNS YKGRMVRRSK KSKKKESLER
     RRSLFKKLAK QPSPLLHTSR SFSCLNRSLS SGESLPGSPT HSLSPRSPTP SYRSTPDFPS
     GTNSSQSSSP SSSAPNSPAG SGHIRPSTLH GLAPKLSGQR YRSGRRKSAG SIPLSPLART
     PSPTPQPTSP QRSPSPLLGH SLGNAKITQA FPSKMHSPPT IVRHIVRPKS AEPPRSPLLK
     RVQSEEKLSP SYGSDKKLLC SRKHSLEVTQ EEVQREQCQR EVTLQSLEEN VCDAPSLSRA
     RPVEQGCLKR PVSRKVGRQE SVDDLDRDKL KAKVVVKKPE EKHESHQKPH SLGGDSESYA
     LFRLEEREKK VYSKGLERSG HFENTSAELP SVGSLLKDTL HKQASVRASE GVTSDGAACS
     LTPGEHSQSL GDFKRASASG ILHDSVCPIS DRPAPGKVEY SEKASQAKEL LRSEKLDSKL
     ANIDYLRKKM SLDDKDDSHC AILKPKITSS AHECLPGNPI RPMAGQQETP PASENRAFIN
     STHTPQMSAV SFVPLKALAG RVENGGEKAG LAAPESPVRK SPSEYKLEGR SVSCLKPIEG
     TLDIALLSGP HASKTELLSP EPAQSPSPGI NVGPCVPLAL PGSSGKKGDS TSLREPSSAN
     LKVNKSYLLE PRFLPPSRAL QDSLAASGPE PKSKPERKLI HPSARSPATV TESNLQQKEG
     GPATHQDRST DTRNLPGPGQ TLHNVDLPRL CTRAPLPPEG TPAKEKPCLK EPSAKVKSEW
     SAVRDDGHRD PCAKLCPAET GKASDSSKPL PSGGRTQPDF YKQTQTSEKA WAHAKTNHKD
     SQDEVKSLAR EDSASLLYEK EIGRARKGPE PKPEVPATRC PPQPPGIEGE KREKLSAAPS
     LQKQAPKEPD RKEQTSQRPG GSGPQQPPPT KELSNSASWQ HGSSPSHTLK KEPGTKAAAA
     EPSTSLHDTP RSATATTTAI ATTTTTTSAG HSDCSSHKAR PGPDPSPSKS KHQDRSLSSQ
     KLSAGSAKGK EPVTQPLGGS IREGKGGSKG PVDTFSAVLT TQGKASDVLV QGEGRVSIIV
     HTEECPLDAK LKNTNGGCPP EMQAKHPPRQ GHLSEAADQK PLIAGEKQSP SPKHPKPSTV
     KDYPSLCRQT DRSPSHQATT GDRKAEGKKC TDALYVAAPE GYKPEASPSL HHGETGLRGS
     ERPPMGMGKG FSEPKGKGPG PQKSLAETGK PSGMKRSPSA TVQSSLRSAA PPEKSLSYSA
     SFPEAQPGVR EVPAANSSPS SAKATGGTSE FPAPSSRDHR KLQSGGDGRS QMIKSDSLPS
     FRLSTSALES HFQDPQVPIA SGHRGRALSV TAATGEPKGR ELAQPPPVRK QNACREATRA
     PPAPSTDRSL PLSSEKDFVV RQRRGKETLR SSPHKKAS
//
ID   RHG32_MOUSE             Reviewed;        2089 AA.
AC   Q811P8; B9EHJ8; Q6A010;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Rho GTPase-activating protein 32;
DE   AltName: Full=Brain-specific Rho GTPase-activating protein;
DE   AltName: Full=GAB-associated Cdc42/Rac GTPase-activating protein;
DE   AltName: Full=GC-GAP;
DE   AltName: Full=Rho-type GTPase-activating protein 32;
DE   AltName: Full=Rho/Cdc42/Rac GTPase-activating protein RICS;
DE   AltName: Full=RhoGAP involved in the beta-catenin-N-cadherin and NMDA receptor signaling;
DE   AltName: Full=p200RhoGAP;
DE   AltName: Full=p250GAP;
GN   Name=Arhgap32; Synonyms=Grit, Kiaa0712, Rics;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY,
RP   AND DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6;
RX   MEDLINE=22829943; PubMed=12819203; DOI=10.1074/jbc.M304594200;
RA   Zhao C., Ma H., Bossy-Wetzel E., Lipton S.A., Zhang Z., Feng G.S.;
RT   "GC-GAP, a Rho family GTPase-activating protein that interacts with
RT   signaling adapters Gab1 and Gab2.";
RL   J. Biol. Chem. 278:34641-34653(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1584-2089.
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [5]
RP   ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), INTERACTION WITH CTTNB1;
RP   GRIN2B; DLG4 AND CDH2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND DOMAIN PX.
RX   PubMed=17663722; DOI=10.1111/j.1365-2443.2007.01101.x;
RA   Hayashi T., Okabe T., Nasu-Nishimura Y., Sakaue F., Ohwada S.,
RA   Matsuura K., Akiyama T., Nakamura T.;
RT   "PX-RICS, a novel splicing variant of RICS, is a main isoform
RT   expressed during neural development.";
RL   Genes Cells 12:929-939(2007).
RN   [6]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12454018; DOI=10.1074/jbc.M207789200;
RA   Moon S.Y., Zang H., Zheng Y.;
RT   "Characterization of a brain-specific Rho GTPase-activating protein,
RT   p200RhoGAP.";
RL   J. Biol. Chem. 278:4151-4159(2003).
RN   [7]
RP   FUNCTION, INTERACTION WITH CTTNB1; GRIN2B; DLG4 AND CDH2, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=12531901; DOI=10.1074/jbc.M208872200;
RA   Okabe T., Nakamura T., Nishimura Y.N., Kohu K., Ohwada S.,
RA   Morishita Y., Akiyama T.;
RT   "RICS, a novel GTPase-activating protein for Cdc42 and Rac1, is
RT   involved in the beta-catenin-N-cadherin and N-methyl-D-aspartate
RT   receptor signaling.";
RL   J. Biol. Chem. 278:9920-9927(2003).
RN   [8]
RP   INTERACTION WITH GRIN2B, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=12857875; DOI=10.1091/mbc.E02-09-0623;
RA   Nakazawa T., Watabe A.M., Tezuka T., Yoshida Y., Yokoyama K.,
RA   Umemori H., Inoue A., Okabe S., Manabe T., Yamamoto T.;
RT   "p250GAP, a novel brain-enriched GTPase-activating protein for Rho
RT   family GTPases, is involved in the N-methyl-d-aspartate receptor
RT   signaling.";
RL   Mol. Biol. Cell 14:2921-2934(2003).
RN   [9]
RP   FUNCTION, INTERACTION WITH CDC42, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=16716191; DOI=10.1111/j.1365-2443.2006.00966.x;
RA   Nasu-Nishimura Y., Hayashi T., Ohishi T., Okabe T., Ohwada S.,
RA   Hasegawa Y., Senda T., Toyoshima C., Nakamura T., Akiyama T.;
RT   "Role of the Rho GTPase-activating protein RICS in neurite
RT   outgrowth.";
RL   Genes Cells 11:607-614(2006).
RN   [10]
RP   FUNCTION, INTERACTION WITH RASA1, AND MUTAGENESIS OF ARG-58.
RX   PubMed=17272280; DOI=10.1074/jbc.M609375200;
RA   Shang X., Moon S.Y., Zheng Y.;
RT   "p200 RhoGAP promotes cell proliferation by mediating cross-talk
RT   between Ras and Rho signaling pathways.";
RL   J. Biol. Chem. 282:8801-8811(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856; SER-892 AND
RP   SER-952, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706 AND SER-952, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: GTPase-activating protein (GAP) promoting GTP hydrolysis
CC       on RHOA, CDC42 and RAC1 small GTPases. May be involved in the
CC       differentiation of neuronal cells during the formation of neurite
CC       extensions. Involved in NMDA receptor activity-dependent actin
CC       reorganization in dendritic spines. May mediate cross-talks
CC       between Ras- and Rho-regulated signaling pathways in cell growth
CC       regulation. Isoform 2 has higher GAP activity.
CC   -!- SUBUNIT: Interacts with NTRK1 (via cytoplasmic domain); the
CC       interaction is independent of the phosphorylation state of NTRK1
CC       (By similarity). Interacts with SHC3 (via SH2 domain) (By
CC       similarity). Interacts with RASA1 (via SH3 domain); the
CC       interaction is necessary for the Ras activation and cell
CC       transforming activities of ARHGAP32. Interacts with GAB1 and GAB2.
CC       Interacts with CRK and CRKL. Found in a complex with CRKL and
CC       BCAR1; upon EGF stimulation BCAR1 may be replaced by EGFR (By
CC       similarity). Interacts with NCK1 (via SH3 domain); NCK1 recruits
CC       phosphorylated BCAR1 to the complex. Isoform 2 interacts with FYN;
CC       the interaction appears to be dependent on tyrosine
CC       phosphorylation of ARHGAP32 (By similarity). Interacts with EGFR;
CC       the interaction requires EGF stimulation and is increased by SHC3.
CC       Interacts with CDC42; the interaction requires constitutively
CC       active CDC42. Interacts with CTNNB1, DLG4, CDH2 and GRIN2B.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane, postsynaptic density. Cell projection, dendritic spine.
CC       Cytoplasm, cell cortex. Endosome membrane. Golgi apparatus
CC       membrane. Endoplasmic reticulum membrane. Membrane.
CC       Note=Association to membrane via PX domain (By similarity).
CC       Associated with cortical actin in undifferentiated neuroblastoma
CC       cells, but localized to dendritic spine and postsynaptic density
CC       after differentiation. Colocalizes with EGFR at the cell membrane
CC       upon EGF treatment (By similarity). Colocalizes with GAB2 at the
CC       cell membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=PX-RICS;
CC         IsoId=Q811P8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q811P8-2; Sequence=VSP_034937;
CC   -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are highly expressed
CC       in brain, specially in cortex, corpus striatum, hippocampus and
CC       thalamus. Low levels in cerebellum, colon, small intestine, and
CC       kidney.
CC   -!- DEVELOPMENTAL STAGE: Isoform 1 is detectable by embryonic day 13,
CC       whereas isoform 2 is detected postnatally.
CC   -!- DOMAIN: The N-terminal PX domain interacts specifically with
CC       phosphatidylinositides.
CC   -!- PTM: Isoform 2 is phosphorylated on multiple tyrosine residues by
CC       FYN (By similarity). Phosphorylated tyrosine residues undergo
CC       dephosphorylation after stimulation of NMDA receptors.
CC       Phosphorylated in vitro by CaMK2 in the presence of calmodulin and
CC       calcium; which inhibits GAP activity.
CC   -!- DISRUPTION PHENOTYPE: Mice are fertile but display abnormal
CC       neurite growth.
CC   -!- SIMILARITY: Belongs to the PX domain-containing GAP family.
CC   -!- SIMILARITY: Contains 1 PX (phox homology) domain.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; AY194286; AAO43676.1; -; mRNA.
DR   EMBL; AC134607; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC132390; AAI32391.1; -; mRNA.
DR   EMBL; BC138042; AAI38043.1; -; mRNA.
DR   EMBL; AK173008; BAD32286.1; -; mRNA.
DR   IPI; IPI00274140; -.
DR   IPI; IPI00900399; -.
DR   RefSeq; NP_001182561.1; NM_001195632.1.
DR   RefSeq; NP_796353.3; NM_177379.4.
DR   UniGene; Mm.426933; -.
DR   UniGene; Mm.46683; -.
DR   HSSP; P52757; 1XA6.
DR   ProteinModelPortal; Q811P8; -.
DR   SMR; Q811P8; 264-321, 368-569.
DR   MINT; MINT-268399; -.
DR   STRING; Q811P8; -.
DR   PhosphoSite; Q811P8; -.
DR   PRIDE; Q811P8; -.
DR   Ensembl; ENSMUST00000047637; ENSMUSP00000048601; ENSMUSG00000041444.
DR   GeneID; 330914; -.
DR   KEGG; mmu:330914; -.
DR   UCSC; uc009orv.1; mouse.
DR   CTD; 330914; -.
DR   MGI; MGI:2450166; Arhgap32.
DR   GeneTree; ENSGT00600000084016; -.
DR   HOGENOM; HBG445290; -.
DR   HOVERGEN; HBG108407; -.
DR   InParanoid; Q811P8; -.
DR   OMA; HQEASHR; -.
DR   OrthoDB; EOG46MBHP; -.
DR   NextBio; 399621; -.
DR   ArrayExpress; Q811P8; -.
DR   Bgee; Q811P8; -.
DR   Genevestigator; Q811P8; -.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR   GO; GO:0005938; C:cell cortex; IDA:MGI.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR001683; Phox.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:3.30.1520.10; PX; 1.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF64268; PX; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50195; PX; FALSE_NEG.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW   Cytoplasm; Endoplasmic reticulum; Endosome; Golgi apparatus;
KW   GTPase activation; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; SH3 domain; Synapse.
FT   CHAIN         1   2089       Rho GTPase-activating protein 32.
FT                                /FTId=PRO_0000345204.
FT   DOMAIN      131    245       PX; atypical.
FT   DOMAIN      259    321       SH3.
FT   DOMAIN      372    567       Rho-GAP.
FT   REGION     1395   1714       Interaction with GAB2 (By similarity).
FT   REGION     1688   2089       Interaction with FYN (By similarity).
FT   COMPBIAS   1033   1038       Poly-Pro.
FT   COMPBIAS   1309   1314       Poly-Pro.
FT   MOD_RES     613    613       Phosphoserine (By similarity).
FT   MOD_RES     706    706       Phosphoserine.
FT   MOD_RES     856    856       Phosphoserine.
FT   MOD_RES     871    871       Phosphoserine (By similarity).
FT   MOD_RES     892    892       Phosphoserine.
FT   MOD_RES     952    952       Phosphoserine.
FT   MOD_RES    1206   1206       Phosphoserine (By similarity).
FT   MOD_RES    1560   1560       Phosphotyrosine (By similarity).
FT   VAR_SEQ       1    349       Missing (in isoform 2).
FT                                /FTId=VSP_034937.
FT   MUTAGEN      58     58       R->K: Does not affect RhoA or CDC42
FT                                activity.
SQ   SEQUENCE   2089 AA;  229719 MW;  C7C4BD904D903F02 CRC64;
     METESETSSL GDDSVFWLDC EGVTQLTDGD EEEREESFRK MKSSIHSEED DFVPELHRNV
     HPRERPDWEE TLSAMARGAD VPEIPGDLTL KSCGSTASTK VKHVKKLPFT KGHFPKMAEC
     AHFHYENVEF GSIQLSLSEE QNEVMKNGCE SKELVYLVQI ACQGKSWIVK RSYEDFRVLD
     KHLHLCIYDR RFSQLTELPR SDVLKDSPES VTQMLTAYLS RLSTIAGNKI NCGPALTWME
     IDNKGNHLLV HEESSINTPA VGAAHVIKRY TARAPDELTL EVGDIVSVID MPPKVLSTWW
     RGKHGFQVGL FPGHCVELIN QKVPQSVTNS VPKPVSKKHG KLITFLRTFM KSRPTKQKLK
     QRGILKERVF GCDLGEHLLN SGFEVPQVLQ SCTAFIERYG IVDGIYRLSG VASNIQRLRH
     EFDSEHVPDL TKEPYVQDIH SVGSLCKLYF RELPNPLLTY QLYEKFSDAV SAATDEERLI
     KIHDVIQQLP PPHYRTLEFL MRHLSLLADY CSITNMHAKN LAIVWAPNLL RSKQIESACF
     SGTAAFMEVR IQSVVVEFIL NHVDVLFSGK ISAVMQEGAA SLSRPKSLLV SSPSTKLLTL
     EEAQARTQAQ VSSPIVTENK YIEVGEGPAA LQGKFHTVIE FPLERKRPQN KMKKSPVGSW
     RSFFNLGKSS SVSKRKLQRN ESEPSEMKAM ALKGGRAEGT LRSAKSEESL TSLHAVDGDS
     KLFRPRRPRS SSDALSASFN GDVLGNRCNS YDNLPHDNES EEEVGLLHIP ALVSPHSAED
     VDLSPPDIGV ASLDFDPMSF QCSPPKAESE CLESGASFLD SLGYTRDKLS PSKKDAEAGG
     SQSQTPGSTA SSEPVSPVQE KLSPFFTLDL SPTDDKSSKP SSFTEKVVYA FSPKIGRKLS
     KSPSMNISEP ISVTLPPRVS EVIGTVSNTV AQNASPTSWD KSVEERDVIN RSPTQLQLGK
     MKAGEREAQE TCEPEAQPLE QGAAEEVELP GTEERPVLSS QSKAVPSGQS QTGAVTHDPP
     QDPVPVSSVS LIPPPPPPKN VARMLALALA ESAQQASSQT LKRPGASQAG CTSYGDTAVV
     PSEEKLPSSY SSLTLDKTCF QTDRPAEQFH PQINGLGNCN QPLPEAAAMG GPTQSNTTDS
     GEQLHQVDLI GNSLHRNHIS GDPEKARSTS APLTDSEKSD DHGSFPEDHA GKSSVSTVSF
     LEQDQSPLHF SCGDQPLSYL GTSVDKPHHS SELTDKSPMP STLPRDKAHH PLSGSPEENS
     STATMAYMMA TPARAEPSNS EASRVLAEQP SAADFVAATL QRTHRTNRPL PPPPSQRPAE
     QPPVVGQVQE APSIGLNNSH KVQGTAPAPE RPPESRAMGD PAPIFLSDGT AAAQCPMGAS
     APQPGLPEKV RESSRAPPLH LRAESFPGHS CGFAAPVPPT RTMESKMAAA LHSSAADATS
     SSNYHSFVPS SASVDDVMPV PLPVSQPKHA SQKIAYSSFA RPDVTAEPFG PENCLHFNMT
     PNCQFRPQSV PPHHNKLEPH QVYGARSEPP ASMGPRYNTY VAPGRNMSGH HSKPCSRVEY
     VSSLGSSVRN PCCPEDILPY PTIRRVQSLH APPPSMIRSV PISRTEVPPD DEPAYCPRPV
     YQYKPYQSSQ ARSDYHVTQL QPYFENGRVH YRYSPYSSSS SSYYSPEGAL CDVDAYGTVQ
     LRPLHRLSSR DFAFYNPRLQ GKNVYNYAGL PPRPRANATG YFSGNDHNVV TMPPTADGKH
     TYTSWDLEDM EKYRMQSIRR ESRARQKVKG PIMSQYDNMT PAVQEDLGGI YVIHLRSKSD
     PGKTGLLSVA EGKEGRHPAK AVSPEGDERF YRKHPESEFD RAHHHGGYGS TQAEKPSLPQ
     KQSSLRNRKL HDMGCSLPEH RAHQEASHRQ LCESKNGPPY PQGAGQLDYG SKGMPDTSEP
     SNYHNSGKYM TSGQGSLTLN HKEVRLPKDL DRPRARQPPG PEKHSRDCYK EEEHFSQSMV
     PPPKPERSHS LKLHHTQNLE RDPSVLYQYQ THSKRQSSMT VVSQYDNLED YHSLPQHQRG
     GFGGAGMGAY VPSGFVHPQS RTYATALGQG AFLPTELSLP HPDTQIHAE
//
ID   PCY1B_MOUSE             Reviewed;         369 AA.
AC   Q811Q9; Q3UEW0; Q80Y63; Q811Q8; Q8BKD2; Q8C085;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Choline-phosphate cytidylyltransferase B;
DE            EC=2.7.7.15;
DE   AltName: Full=CCT-beta;
DE   AltName: Full=CTP:phosphocholine cytidylyltransferase B;
DE            Short=CCT B;
DE            Short=CT B;
DE   AltName: Full=Phosphorylcholine transferase B;
GN   Name=Pcyt1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND FUNCTION.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=22726134; PubMed=12842190; DOI=10.1016/S1388-1981(03)00067-2;
RA   Karim M., Jackson P., Jackowski S.;
RT   "Gene structure, expression and identification of a new
RT   CTP:phosphocholine cytidylyltransferase beta isoform.";
RL   Biochim. Biophys. Acta 1633:1-12(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 18-369 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Eye, Medulla oblongata, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=15143167; DOI=10.1128/MCB.24.11.4720-4733.2004;
RA   Jackowski S., Rehg J.E., Zhang Y.-M., Wang J., Miller K., Jackson P.,
RA   Karim M.A.;
RT   "Disruption of CCTbeta2 expression leads to gonadal dysfunction.";
RL   Mol. Cell. Biol. 24:4720-4733(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-319 AND
RP   THR-325, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
CC   -!- FUNCTION: Controls phosphatidylcholine synthesis.
CC   -!- CATALYTIC ACTIVITY: CTP + choline phosphate = diphosphate + CDP-
CC       choline.
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine
CC       biosynthesis; phosphatidylcholine from phosphocholine: step 1/2.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=CCTbeta2;
CC         IsoId=Q811Q9-1; Sequence=Displayed;
CC       Name=2; Synonyms=CCTbeta3;
CC         IsoId=Q811Q9-2; Sequence=VSP_020041, VSP_020042;
CC         Note=Enzymatic activity identical to isoform 1. Not expressed in
CC         embryo. Expression starts at 5 weeks;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain (at protein level).
CC       Expressed at lower levels in lung and gonads.
CC   -!- DEVELOPMENTAL STAGE: Expression is low at E7, reaches a maximum at
CC       E15 and decreases at E17.
CC   -!- DISRUPTION PHENOTYPE: Female mice lacking isoform 1 have reduced
CC       fecundity due to failure in ovary maturation. Male mice lacking
CC       isoform 1 have reduced fecundity due to testicular degeneration.
CC   -!- SIMILARITY: Belongs to the cytidylyltransferase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC27658.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AY189949; AAO39004.1; -; mRNA.
DR   EMBL; AY189950; AAO39005.1; -; mRNA.
DR   EMBL; AK032027; BAC27658.1; ALT_INIT; mRNA.
DR   EMBL; AK053577; BAC35435.1; -; mRNA.
DR   EMBL; AK149304; BAE28801.1; -; mRNA.
DR   EMBL; BC048917; AAH48917.1; -; mRNA.
DR   IPI; IPI00118337; -.
DR   IPI; IPI00410759; -.
DR   RefSeq; NP_808214.1; NM_177546.2.
DR   RefSeq; NP_997593.1; NM_211138.1.
DR   UniGene; Mm.166467; -.
DR   ProteinModelPortal; Q811Q9; -.
DR   SMR; Q811Q9; 41-216.
DR   STRING; Q811Q9; -.
DR   PRIDE; Q811Q9; -.
DR   Ensembl; ENSMUST00000045898; ENSMUSP00000044280; ENSMUSG00000035246.
DR   Ensembl; ENSMUST00000113933; ENSMUSP00000109566; ENSMUSG00000035246.
DR   GeneID; 236899; -.
DR   KEGG; mmu:236899; -.
DR   UCSC; uc009tsv.1; mouse.
DR   UCSC; uc009tsw.1; mouse.
DR   CTD; 236899; -.
DR   MGI; MGI:2147987; Pcyt1b.
DR   GeneTree; ENSGT00390000000269; -.
DR   HOGENOM; HBG587468; -.
DR   HOVERGEN; HBG053531; -.
DR   InParanoid; Q811Q9; -.
DR   OMA; FADETNC; -.
DR   OrthoDB; EOG45X7WJ; -.
DR   PhylomeDB; Q811Q9; -.
DR   BRENDA; 2.7.7.15; 244.
DR   NextBio; 383139; -.
DR   ArrayExpress; Q811Q9; -.
DR   Bgee; Q811Q9; -.
DR   Genevestigator; Q811Q9; -.
DR   GermOnline; ENSMUSG00000035246; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0004105; F:choline-phosphate cytidylyltransferase activity; IEA:EC.
DR   GO; GO:0001541; P:ovarian follicle development; IMP:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   InterPro; IPR004821; Cyt_trans-rel.
DR   InterPro; IPR004820; Cytidylyltransf.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Pfam; PF01467; CTP_transf_2; 1.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endoplasmic reticulum; Nucleotidyltransferase;
KW   Phospholipid biosynthesis; Phosphoprotein; Transferase.
FT   CHAIN         1    369       Choline-phosphate cytidylyltransferase B.
FT                                /FTId=PRO_0000247762.
FT   REGION       74    235       Catalytic (Potential).
FT   MOD_RES     233    233       Phosphoserine (By similarity).
FT   MOD_RES     315    315       Phosphoserine.
FT   MOD_RES     319    319       Phosphoserine.
FT   MOD_RES     325    325       Phosphothreonine.
FT   VAR_SEQ       1     24       Missing (in isoform 2).
FT                                /FTId=VSP_020041.
FT   VAR_SEQ      25     39       ETMEEIEHTCPQPRL -> MDKDEFSRK (in isoform
FT                                2).
FT                                /FTId=VSP_020042.
FT   CONFLICT     73     73       V -> G (in Ref. 1; AAO39004/AAO39005).
FT   CONFLICT     77     77       V -> I (in Ref. 2; BAE28801).
SQ   SEQUENCE   369 AA;  41900 MW;  841B0E2E9EE22615 CRC64;
     MPVLTTDAES ETGIPKSLSN EPPSETMEEI EHTCPQPRLT LTAPAPFADE SSCQCQAPHE
     KLTVAQARLG TPVDRPVRVY ADGIFDLFHS GHARALMQAK TLFPNSYLLV GVCSDDLTHK
     FKGFTVMNEA ERYEALRHCR YVDEVIRDAP WTLTPEFLEK HKIDFVAHDD IPYSSAGSDD
     VYKHIKEAGM FVPTQRTEGI STSDIITRIV RDYDVYARRN LQRGYTAKEL NVSFINEKKY
     RFQNQVDKMK EKVKNVEERS KEFVNRVEEK SHDLIQKWEE KSREFIGNFL ELFGPDGAWK
     QMFQERSSRM LQALSPKQSP VSSPTRSRSP SRSPSPTFSW LPNKTSPPSS PKAASASISS
     MSEGDEDEK
//
ID   SRGP2_MOUSE             Reviewed;        1099 AA.
AC   Q812A2; Q80U09; Q8BKP4; Q8BLD0; Q925I2;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=SLIT-ROBO Rho GTPase-activating protein 3;
DE            Short=srGAP3;
DE   AltName: Full=Rho GTPase-activating protein 14;
DE   AltName: Full=WAVE-associated Rac GTPase-activating protein;
DE            Short=WRP;
DE   AltName: Full=srGAP2;
GN   Name=Srgap3; Synonyms=Arhgap14, Kiaa0411, Srgap2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=22350134; PubMed=12447388; DOI=10.1038/ncb886;
RA   Soderling S.H., Binns K.L., Wayman G.A., Davee S.M., Ong S.H.,
RA   Pawson T., Scott J.D.;
RT   "The WRP component of the WAVE-1 complex attenuates Rac-mediated
RT   signalling.";
RL   Nat. Cell Biol. 4:970-975(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-671.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-471.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 27-1099.
RC   STRAIN=BALB/c;
RA   Crowley M.R., Slon K.E., Nowak N.J., Asch H.L., Asch B.B.;
RT   "Identification of a novel RhoGAP through analysis of an ecotropic
RT   MuLV integration site.";
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1070, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: GTPase-activating protein for RAC1 and perhaps CDC42,
CC       but not for RhoA small GTPase. May attenuate RAC1 signaling in
CC       neurons (By similarity).
CC   -!- SUBUNIT: Interacts with WASF1. Probably interacts with ROBO1.
CC       Interacts with FASLG (By similarity).
CC   -!- SIMILARITY: Contains 1 FCH domain.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK52474.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=AAK52474.1; Type=Frameshift; Positions=90, 98, 104, 110, 120;
CC       Sequence=BAC34580.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC       Sequence=BAC65558.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC       Sequence=BAC65558.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact. Aberrant splice sites;
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DR   EMBL; AF496547; AAM46845.1; -; mRNA.
DR   EMBL; AK122276; BAC65558.1; ALT_SEQ; mRNA.
DR   EMBL; AK045508; BAC32400.1; -; mRNA.
DR   EMBL; AK051262; BAC34580.1; ALT_SEQ; mRNA.
DR   EMBL; AF338472; AAK52474.1; ALT_FRAME; mRNA.
DR   IPI; IPI00330039; -.
DR   RefSeq; NP_536696.4; NM_080448.4.
DR   UniGene; Mm.236401; -.
DR   ProteinModelPortal; Q812A2; -.
DR   SMR; Q812A2; 493-697, 749-800.
DR   STRING; Q812A2; -.
DR   PhosphoSite; Q812A2; -.
DR   PRIDE; Q812A2; -.
DR   Ensembl; ENSMUST00000088373; ENSMUSP00000085712; ENSMUSG00000030257.
DR   Ensembl; ENSMUST00000113169; ENSMUSP00000108794; ENSMUSG00000030257.
DR   GeneID; 259302; -.
DR   KEGG; mmu:259302; -.
DR   UCSC; uc009deh.1; mouse.
DR   UCSC; uc009dei.1; mouse.
DR   UCSC; uc009dej.1; mouse.
DR   CTD; 259302; -.
DR   MGI; MGI:2152938; Srgap3.
DR   eggNOG; roNOG09609; -.
DR   HOGENOM; HBG356471; -.
DR   HOVERGEN; HBG051637; -.
DR   InParanoid; Q812A2; -.
DR   OrthoDB; EOG4JT04N; -.
DR   NextBio; 392051; -.
DR   ArrayExpress; Q812A2; -.
DR   Bgee; Q812A2; -.
DR   CleanEx; MM_SRGAP2; -.
DR   CleanEx; MM_SRGAP3; -.
DR   Genevestigator; Q812A2; -.
DR   GermOnline; ENSMUSG00000030257; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR001060; FCH.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50133; FCH; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; GTPase activation; Phosphoprotein;
KW   SH3 domain.
FT   CHAIN         1   1099       SLIT-ROBO Rho GTPase-activating protein
FT                                3.
FT                                /FTId=PRO_0000056770.
FT   DOMAIN       22     87       FCH.
FT   DOMAIN      506    694       Rho-GAP.
FT   DOMAIN      744    803       SH3.
FT   COILED      352    392       Potential.
FT   COILED      952    987       Potential.
FT   MOD_RES     220    220       N6-acetyllysine (By similarity).
FT   MOD_RES     222    222       N6-acetyllysine (By similarity).
FT   MOD_RES     224    224       N6-acetyllysine (By similarity).
FT   MOD_RES     602    602       Phosphoserine (By similarity).
FT   MOD_RES     837    837       Phosphoserine (By similarity).
FT   MOD_RES     858    858       Phosphoserine (By similarity).
FT   MOD_RES    1070   1070       Phosphoserine.
FT   CONFLICT     67     67       L -> V (in Ref. 4; AAK52474).
FT   CONFLICT    122    122       N -> T (in Ref. 4; AAK52474).
FT   CONFLICT    523    523       A -> V (in Ref. 2; BAC65558).
SQ   SEQUENCE   1099 AA;  124420 MW;  C033CD7DE43C1B2C CRC64;
     MSSQTKFKKD KEIIAEYEAQ IKEIRTQLVE QFKCLEQQSE SRLQLLQDLQ EFFRRKAEIE
     LEYSRSLEKL AERFSSKIRS SREHQFKKDQ YLLSPVNCWY LVLHQTRRES RDHATLNDIF
     MNNVIVRLSQ ISEDVIRLFK KSKEIGLQMH EELLKVTNEL YTVMKTYHMY HAESISAESK
     LKEAEKQEEK QFNKSGELSM NLLRHEDRPQ RRSSVKKIEK MKEKRQAKYS ENKLKCTKAR
     NDYLLNLAAT NAAISKYYIH DVSDLIDCCD LGFHASLART FRTYLSAEYN LETSRHEGLD
     VIENAVDNLD SRSDKHTVMD MCSQVFCPPL KFEFQPHMGD EVCQVSAQQP VQTELLMRYH
     QLQSRLATLK IENEEVRKTL DATMQTLQDM LTVEDFDVSD AFQHSRSTES IKSAASETYM
     SKINIAKRRA NQQETEMFYF TKFKEYVNGS NLITKLQAKH DLLKQTLGEG ERAECGTTRP
     PCLPPKPQKM RRPRPLSVYS HKLFNGSMEA FIKDSGQAIP LVAESCIRFI NLYGLQQQGI
     FRVPGSQVEV NDIKNSFERG EDPLVDDQNE RDINSVAGVL KLYFRGLENP LFPKERFQDL
     ISTIKLENPA DRVHPIQQIL ITLPRVVIVV MRYLFAFLNH LSQYSDENMM DPYNLAICFG
     PTLMHIPDGQ DPVSCQAHVN EVIKTIIIHH EAIFPSPREL EGPVYEKCMA GGEEYCDSPH
     SEPGTIDEVD HDNGTEPHTS DEEVEQIEAI AKFDYVGRSP RELSFKKGAS LLLYHRASED
     WWEGRHNGVD GLIPHQYIVV QDMDDAFSDS LSQKADSEAS SGPLLDDKAS SKNDLQSPTE
     HISDYGFGGV MGRVRLRSDG AAIPRRRSGG DTHSPPRGLG PSIDTPPRAA ACPSSPHKIP
     LSRGRIESPE KRRMATFGSA GSINYPDKKA LTEGLSMRST CGSTRHSSLG DHKSLEAEAL
     AEDIEKTMST ALHELRELER QNTVKQAPDV VLDTLEPLKN PPGPISSEPA SPLHTIVIRD
     PDAAMRRSSS SSTEMMTTFK PALSARLAGA QLRPPPMRPV RPVVQHRSSS SSSSGVGSPA
     VTPTEKMFPN SSSDKSGTM
//
ID   CPEB2_MOUSE             Reviewed;         521 AA.
AC   Q812E0;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Cytoplasmic polyadenylation element-binding protein 2;
DE            Short=CPE-BP2;
DE            Short=CPE-binding protein 2;
DE            Short=mCPEB-2;
GN   Name=Cpeb2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], RNA-BINDING, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   MEDLINE=22702765; PubMed=12672660; DOI=10.1095/biolreprod.103.015677;
RA   Kurihara Y., Tokuriki M., Myojin R., Hori T., Kuroiwa A., Matsuda Y.,
RA   Sakurai T., Kimura M., Hecht N.B., Uesugi S.;
RT   "CPEB2, a novel putative translational regulator in mouse haploid germ
RT   cells.";
RL   Biol. Reprod. 69:261-268(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY, AND ABSENCE OF INDUCTION.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=22784672; PubMed=12871996; DOI=10.1073/pnas.1133424100;
RA   Theis M., Si K., Kandel E.R.;
RT   "Two previously undescribed members of the mouse CPEB family of genes
RT   and their inducible expression in the principal cell layers of the
RT   hippocampus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:9602-9607(2003).
RN   [4]
RP   INTERACTION WITH PAPD4.
RX   PubMed=17927953; DOI=10.1016/j.bbrc.2007.09.096;
RA   Nakanishi T., Kumagai S., Kimura M., Watanabe H., Sakurai T.,
RA   Kimura M., Kashiwabara S., Baba T.;
RT   "Disruption of mouse poly(A) polymerase mGLD-2 does not alter
RT   polyadenylation status in oocytes and somatic cells.";
RL   Biochem. Biophys. Res. Commun. 364:14-19(2007).
CC   -!- FUNCTION: May play a role in translational regulation of stored
CC       mRNAs in transcriptionally inactive haploid spermatids. Binds to
CC       poly(U) RNA oligomers.
CC   -!- SUBUNIT: Interacts with PAPD4/GLD2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Expressed in embryo, cerebellum, salivary
CC       gland, thymus, heart, liver, lung, spleen, kidney, intestine,
CC       ovary and round spermatids. Weakly expressed in granular cells of
CC       dentate gyrus and the pyramidal cells of CA3 and CA1 of the
CC       hippocampus.
CC   -!- INDUCTION: Not induced by kainate.
CC   -!- SIMILARITY: Belongs to the RRM CPEB family.
CC   -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
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DR   EMBL; AB100307; BAC57076.1; -; mRNA.
DR   EMBL; BC107349; AAI07350.1; -; mRNA.
DR   EMBL; BC107350; AAI07351.1; -; mRNA.
DR   IPI; IPI00187243; -.
DR   UniGene; Mm.7233; -.
DR   ProteinModelPortal; Q812E0; -.
DR   SMR; Q812E0; 263-451.
DR   PhosphoSite; Q812E0; -.
DR   PRIDE; Q812E0; -.
DR   Ensembl; ENSMUST00000051378; ENSMUSP00000060593; ENSMUSG00000039782.
DR   Ensembl; ENSMUST00000114065; ENSMUSP00000109699; ENSMUSG00000039782.
DR   UCSC; uc008xhi.1; mouse.
DR   MGI; MGI:2442640; Cpeb2.
DR   eggNOG; roNOG13378; -.
DR   GeneTree; ENSGT00390000012886; -.
DR   HOVERGEN; HBG058010; -.
DR   OrthoDB; EOG4P5K8X; -.
DR   PhylomeDB; Q812E0; -.
DR   NextBio; 380453; -.
DR   ArrayExpress; Q812E0; -.
DR   Bgee; Q812E0; -.
DR   Genevestigator; Q812E0; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0008187; F:poly-pyrimidine tract binding; IDA:MGI.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   Cytoplasm; Repeat; RNA-binding; Translation regulation.
FT   CHAIN         1    521       Cytoplasmic polyadenylation element-
FT                                binding protein 2.
FT                                /FTId=PRO_0000269260.
FT   DOMAIN      264    355       RRM 1.
FT   DOMAIN      372    454       RRM 2.
SQ   SEQUENCE   521 AA;  58442 MW;  88B0D73942770A17 CRC64;
     MNLPQQQPPA AAPQQPQSRR SPVSPQLQQQ HQAAAAAFLQ QRNSYNHHQP LLKQSPWSNH
     QNSGWGTASM SWGAMHGRDH RRSGNMGIPG TMNQISPLKK PFSGNVIAPP KFTRSTPSLT
     PKSWIEDNVF RTDNNSNTLL PLQVRSSLQL PAWGSDSLQD SWCTAAGTSR IDQDRSRMYD
     SLNMHSLENS LIDIMRAEHD PLKGRLSYPH PGTDNLLMLN GRSSLFPIDD SLLDDGHSDQ
     VGVLNSPTCY SAHQNGERIE RFSRKVFVGG LPPDIDEDEI TASFRRFGPL VVDWPHKAES
     KSYFPPKGYA FLLFQEESSV QALIDACIEE DGKLYLCVSS PTIKDKPVQI RPWNLSDSDF
     VMDGSQPLDP RKTIFVGGVP RPLRAVELAM IMDRLYGGVC YAGIDTDPEL KYPKGAGRVA
     FSNQQSYIAA ISARFVQLQH GDIDKRVEVK PYVLDDQMCD ECQGARCGGK FAPFFCANVT
     CLQYYCEFCW ANIHSRAGRE FHKPLVKEGA DRPRQIHFRW N
//
ID   Q812E2_MOUSE            Unreviewed;       735 AA.
AC   Q812E2;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   08-MAR-2011, entry version 44.
DE   SubName: Full=Anion exchange transporter;
GN   Name=Slc26a6; Synonyms=slc26a6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c; TISSUE=Kidney;
RA   Nozawa T., Sugiura S., Hashino Y., Tsuji A., Tamai I.;
RT   "Role of Anion Exchange Transporter PAT1 (slc26a6) on the Intestinal
RT   Absorption of Organic Anions.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the SLC26A/SulP transporter (TC 2.A.53)
CC       family.
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DR   EMBL; AB099881; BAC55182.1; -; mRNA.
DR   IPI; IPI00652463; -.
DR   UniGene; Mm.45201; -.
DR   ProteinModelPortal; Q812E2; -.
DR   STRING; Q812E2; -.
DR   Ensembl; ENSMUST00000098376; ENSMUSP00000095979; ENSMUSG00000023259.
DR   Ensembl; ENSMUST00000098377; ENSMUSP00000095980; ENSMUSG00000023259.
DR   MGI; MGI:2159728; Slc26a6.
DR   HOVERGEN; HBG000639; -.
DR   InParanoid; Q812E2; -.
DR   PhylomeDB; Q812E2; -.
DR   ArrayExpress; Q812E2; -.
DR   Bgee; Q812E2; -.
DR   Genevestigator; Q812E2; -.
DR   GO; GO:0005887; C:integral to plasma membrane; IDA:MGI.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0015301; F:anion:anion antiporter activity; IDA:MGI.
DR   GO; GO:0015108; F:chloride transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0015499; F:formate transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015701; P:bicarbonate transport; IDA:MGI.
DR   InterPro; IPR018045; S04_transporter_CS.
DR   InterPro; IPR002645; SO4_transptr/STAS.
DR   InterPro; IPR001902; SulP_transpt.
DR   InterPro; IPR011547; Sulph_transpt.
DR   Gene3D; G3DSA:3.30.750.24; STAS; 2.
DR   Pfam; PF01740; STAS; 1.
DR   Pfam; PF00916; Sulfate_transp; 1.
DR   SUPFAM; SSF52091; STAS; 1.
DR   TIGRFAMs; TIGR00815; sulP; 1.
DR   PROSITE; PS01130; SLC26A; 1.
DR   PROSITE; PS50801; STAS; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
SQ   SEQUENCE   735 AA;  80424 MW;  441B74742D0A98A6 CRC64;
     MGLQRRDYHV ERPLLNQEQL EDLGHWGPAA KTHQWRTWFR CSRARAHSLL LQHVPVLGWL
     PRYPVREWLL GDLLSGLSVA IMQLPQGLAY ALLAGLPPMF GLYSSFYPVF IYFLFGTSRH
     ISVGTFAVMS VMVGSVTESL TADKAFVQGL NATADDARVQ VAYTLSFLVG LFQVGLGLVH
     FGFVVTYLSE PLVRSYTTAA SVQVLVSQLK YVFGIKLSSH SGPLSVIYTV LEVCAQLPET
     VPGTVVTAIV AGVALVLVKL LNEKLHRRLP LPIPGELLTL IGATGISYGV KLNDRFKVDV
     VGNITTGLIP PVAPKTELFA TLVGNAFAIA VVGFAIAISL GKIFALRHGY RVDSNQELVA
     LGLSNLIGGF FQCFPVSCSM SRSLVQESTG GNTQVAGAVS SLFILLIIVK LGELFRDLPK
     AVLAAVIIVN LKGMMKQFSD ICSLWKANRV DLLIWLVTFV ATILLNLDIG LAVSIVFSLL
     LVVVRMQLPH YSVLGQVPDT DIYRDVAEYS GAKEVPGVKV FRSSATLYFA NAELYSDSLK
     EKCGVDVDRL ITQKKKRIKK QEMKLKRMKK AKKSQKQDAS SKISSVSVNV NTNLEDVKSN
     DVEGSEAKVH QGEELQDVVS SNQEDAKAPT MTSLKSLGLP QPGFHSLILD LSTLSFVDTV
     CIKSLKNIFR DFREIEVEVY IAACYSPVVA QLEAGHFFDE SITKQHVFAS VHDAVTFALS
     HRKSVPKSPV LATKL
//
ID   SVOP_MOUSE              Reviewed;         548 AA.
AC   Q8BFT9; Q6PB56; Q8BKY9;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Synaptic vesicle 2-related protein;
DE            Short=SV2-related protein;
GN   Name=Svop;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Corpus striatum, and Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-31, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK047764; BAC33150.1; -; mRNA.
DR   EMBL; AK053833; BAC35546.1; -; mRNA.
DR   EMBL; AK082744; BAC38595.1; -; mRNA.
DR   EMBL; BC059878; AAH59878.1; -; mRNA.
DR   IPI; IPI00621203; -.
DR   RefSeq; NP_081081.1; NM_026805.1.
DR   UniGene; Mm.63584; -.
DR   ProteinModelPortal; Q8BFT9; -.
DR   PhosphoSite; Q8BFT9; -.
DR   PRIDE; Q8BFT9; -.
DR   Ensembl; ENSMUST00000058472; ENSMUSP00000050730; ENSMUSG00000042078.
DR   GeneID; 68666; -.
DR   KEGG; mmu:68666; -.
DR   UCSC; uc008yzb.1; mouse.
DR   CTD; 68666; -.
DR   MGI; MGI:1915916; Svop.
DR   eggNOG; roNOG12492; -.
DR   GeneTree; ENSGT00550000074384; -.
DR   HOGENOM; HBG715489; -.
DR   HOVERGEN; HBG057057; -.
DR   InParanoid; Q8BFT9; -.
DR   OMA; QYGRKTG; -.
DR   OrthoDB; EOG4MKNFZ; -.
DR   NextBio; 327652; -.
DR   ArrayExpress; Q8BFT9; -.
DR   Bgee; Q8BFT9; -.
DR   CleanEx; MM_SVOP; -.
DR   Genevestigator; Q8BFT9; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015075; F:ion transmembrane transporter activity; IEA:InterPro.
DR   InterPro; IPR020846; Major_facilitator_SF.
DR   InterPro; IPR011701; MFS_1.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   InterPro; IPR004749; Orgcat_transp.
DR   InterPro; IPR005828; Sub_transporter.
DR   Pfam; PF07690; MFS_1; 1.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
DR   TIGRFAMs; TIGR00898; 2A0119; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cytoplasmic vesicle; Membrane; Phosphoprotein; Synapse;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    548       Synaptic vesicle 2-related protein.
FT                                /FTId=PRO_0000279453.
FT   TOPO_DOM      1     87       Cytoplasmic (Potential).
FT   TRANSMEM     88    108       Helical; (Potential).
FT   TOPO_DOM    109    122       Vesicular (Potential).
FT   TRANSMEM    123    143       Helical; (Potential).
FT   TOPO_DOM    144    156       Cytoplasmic (Potential).
FT   TRANSMEM    157    177       Helical; (Potential).
FT   TOPO_DOM    178    180       Vesicular (Potential).
FT   TRANSMEM    181    201       Helical; (Potential).
FT   TOPO_DOM    202    209       Cytoplasmic (Potential).
FT   TRANSMEM    210    230       Helical; (Potential).
FT   TOPO_DOM    231    238       Vesicular (Potential).
FT   TRANSMEM    239    259       Helical; (Potential).
FT   TOPO_DOM    260    316       Cytoplasmic (Potential).
FT   TRANSMEM    317    337       Helical; (Potential).
FT   TOPO_DOM    338    373       Vesicular (Potential).
FT   TRANSMEM    374    394       Helical; (Potential).
FT   TOPO_DOM    395    401       Cytoplasmic (Potential).
FT   TRANSMEM    402    422       Helical; (Potential).
FT   TOPO_DOM    423    424       Vesicular (Potential).
FT   TRANSMEM    425    445       Helical; (Potential).
FT   TOPO_DOM    446    457       Cytoplasmic (Potential).
FT   TRANSMEM    458    478       Helical; (Potential).
FT   TOPO_DOM    479    489       Vesicular (Potential).
FT   TRANSMEM    490    510       Helical; (Potential).
FT   TOPO_DOM    511    548       Cytoplasmic (Potential).
FT   MOD_RES      25     25       Phosphoserine.
FT   MOD_RES      31     31       Phosphoserine.
FT   CONFLICT     11     11       L -> F (in Ref. 2; AAH59878).
FT   CONFLICT     23     23       A -> T (in Ref. 1; BAC33150).
SQ   SEQUENCE   548 AA;  60769 MW;  ED9779BD305DFB83 CRC64;
     MEEDLFQLRQ LPVVKFRRTG ESARSEDDAA SGEHDIQIEG VRVGLEAIEL DDGAAVPKEF
     ANPTDDTFMV EDAVEAIGFG RFQWKLSVLT GLAWMADAME MMILSILAPQ LHCEWRLPSW
     QVALLTSVVF IGMMSSSTLW GNISDQYGRK TGLKISVLWT LYYGILSAFA PVYSWILVLR
     GLVGFGIGGV PQSVTLYAEF LPMKARAKCI LLIEVFWAIG TVFEVLLAVF VMPSLGWRWL
     LLLSAAPLLL FAVLCFWLPE SARYDVLSGN QEKAIATLKR IATENGAPMP LGKLIISRQE
     DRGKMRDLFT PHFRWTTLLL WFIWFSNAFS YYGLVLLTTE LFQAGDVCSI SSRKKAVEAK
     CSLACEYLSK EDYMDLLWTT LSEFPGVLVT LWVIDRLGRK KTMALCFIIF SLCSLLLFIC
     IGRNVLTLLL FIARAFISGG FQAAYVYTPE VYPTATRALG LGTCSGMARV GALITPFIAQ
     VMLESSVYLT LAVYSGCCLL AGVASCFLPI ETKGRALQES SHREWGQEMV GRGTNSAGVP
     RSDSGSQE
//
ID   RN214_MOUSE             Reviewed;         668 AA.
AC   Q8BFU3; Q3UWM9; Q6P3A7; Q80VI8; Q8BNZ6; Q8CC56; Q8CCP2; Q8CE92;
AC   Q8R5B9;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=RING finger protein 214;
GN   Name=Rnf214;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5).
RC   STRAIN=C57BL/6, and C57BL/6J;
RC   TISSUE=Diencephalon, Egg, Eye, Olfactory bulb, Skin, Spinal ganglion,
RC   and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, C57BL/6J, FVB/N, and FVB/N-3;
RC   TISSUE=Brain, Mammary gland, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q8BFU3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BFU3-2; Sequence=VSP_023774, VSP_023775;
CC       Name=3;
CC         IsoId=Q8BFU3-3; Sequence=VSP_023773;
CC         Note=May be produced at very low levels due to a premature stop
CC         codon in the mRNA, leading to nonsense-mediated mRNA decay;
CC       Name=4;
CC         IsoId=Q8BFU3-4; Sequence=VSP_023776;
CC         Note=May be produced at very low levels due to a premature stop
CC         codon in the mRNA, leading to nonsense-mediated mRNA decay;
CC       Name=5;
CC         IsoId=Q8BFU3-5; Sequence=VSP_023774;
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH49909.1; Type=Erroneous initiation;
CC       Sequence=BAC28499.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC       Sequence=BAC37365.1; Type=Erroneous initiation;
CC       Sequence=BAE22885.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK028768; BAC26109.1; -; mRNA.
DR   EMBL; AK030208; BAC26843.1; -; mRNA.
DR   EMBL; AK032376; BAC27844.1; -; mRNA.
DR   EMBL; AK033867; BAC28499.1; ALT_SEQ; mRNA.
DR   EMBL; AK051527; BAC34663.1; -; mRNA.
DR   EMBL; AK078706; BAC37365.1; ALT_INIT; mRNA.
DR   EMBL; AK136229; BAE22885.1; ALT_INIT; mRNA.
DR   EMBL; BC023073; AAH23073.1; -; mRNA.
DR   EMBL; BC049909; AAH49909.1; ALT_INIT; mRNA.
DR   EMBL; BC064100; AAH64100.1; -; mRNA.
DR   EMBL; BC094247; AAH94247.1; -; mRNA.
DR   IPI; IPI00153987; -.
DR   IPI; IPI00221464; -.
DR   IPI; IPI00830301; -.
DR   IPI; IPI00831547; -.
DR   IPI; IPI00831655; -.
DR   RefSeq; NP_848824.1; NM_178709.4.
DR   UniGene; Mm.220945; -.
DR   UniGene; Mm.3255; -.
DR   ProteinModelPortal; Q8BFU3; -.
DR   SMR; Q8BFU3; 587-667.
DR   PhosphoSite; Q8BFU3; -.
DR   PRIDE; Q8BFU3; -.
DR   Ensembl; ENSMUST00000057333; ENSMUSP00000059310; ENSMUSG00000042790.
DR   Ensembl; ENSMUST00000058720; ENSMUSP00000060941; ENSMUSG00000042790.
DR   GeneID; 235315; -.
DR   KEGG; mmu:235315; -.
DR   CTD; 235315; -.
DR   MGI; MGI:2444451; Rnf214.
DR   eggNOG; roNOG17628; -.
DR   GeneTree; ENSGT00530000063254; -.
DR   HOVERGEN; HBG093913; -.
DR   InParanoid; Q8BFU3; -.
DR   OMA; VGPHGPH; -.
DR   OrthoDB; EOG4J6RQH; -.
DR   PhylomeDB; Q8BFU3; -.
DR   NextBio; 382589; -.
DR   ArrayExpress; Q8BFU3; -.
DR   Bgee; Q8BFU3; -.
DR   CleanEx; MM_RNF214; -.
DR   Genevestigator; Q8BFU3; -.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Coiled coil; Metal-binding;
KW   Phosphoprotein; Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    668       RING finger protein 214.
FT                                /FTId=PRO_0000280547.
FT   ZN_FING     623    665       RING-type; atypical.
FT   COILED      220    379       Potential.
FT   COMPBIAS    432    551       Pro-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      25     25       Phosphoserine (By similarity).
FT   MOD_RES      53     53       Phosphoserine (By similarity).
FT   MOD_RES     497    497       Phosphoserine (By similarity).
FT   MOD_RES     500    500       Phosphoserine (By similarity).
FT   MOD_RES     511    511       Phosphoserine (By similarity).
FT   MOD_RES     516    516       Phosphoserine (By similarity).
FT   VAR_SEQ       1     55       Missing (in isoform 3).
FT                                /FTId=VSP_023773.
FT   VAR_SEQ      52    206       Missing (in isoform 2 and isoform 5).
FT                                /FTId=VSP_023774.
FT   VAR_SEQ     615    615       Q -> QPLGRIRALHPAPLAQISPPMFLPSAQVSYPGRSSH
FT                                (in isoform 2).
FT                                /FTId=VSP_023775.
FT   VAR_SEQ     616    668       APPTCKLCLMCQKLVQPSELHPMACTHALHKECIKFWAQTN
FT                                TNDTCPFCPTLK -> VRGASGRELRPAERLRKKPTRRSGH
FT                                EEIRARNICSAFLIIRSEFLLPSFLPSFLPSFLPSFLPFFL
FT                                SFLLVKFICVYVCVCVLCGSRKTTCGSPFSSTM (in
FT                                isoform 4).
FT                                /FTId=VSP_023776.
FT   CONFLICT    361    361       E -> K (in Ref. 1; BAE22885).
FT   CONFLICT    512    512       P -> H (in Ref. 1; BAC37365).
FT   CONFLICT    579    579       Q -> H (in Ref. 1; BAC37365).
SQ   SEQUENCE   668 AA;  73625 MW;  ECF534164BCCDE7E CRC64;
     MAASEVAGLG AGTPSPSESS ALCASKSDES LPDGLSPKDS AQKQKNLSPP SVSSQMITKE
     SNRNAHLEHP EQNPGSSVGD TSAAHEEVVG ENLVATALCL SGNGSQSDLK DLTNPAGEEG
     DTSLRESLHP VTRSLKAGCH SKQLASGNCS EEKCPAASVL KEGSRDAGLD LLPVVPPANG
     VEGVRVDQDD DQDSSSLKLS QNIAVQTDFK TADSEVNTDQ DIEKNLDKMM TERTLLKERY
     QEVLDKQRQV ESQLQVQLKQ LQQRREEEMK NHQEILKAIQ DVTIKREETK KKIEKEKKEF
     LQKEQDLKAE IEKLCEKGRR EVWEMELDRL KNQDGEINRN IMEETERAWK AEILSLESRK
     ELLVLKLEEA EKEAELHLTY LKSTPPTLET VRSKQEWETR LNGVRIMKKN VRDQFNSHIQ
     LVRNGAKLSS LPQIPTPTLP PPPSEADFML QVFQPSPSLT PRMPFSIGQV TMPMVMPSAD
     PRSLSFPILN PALSQSSQPS PPLPGSHGRN SPGLGSLVSP HGPHMPPAAS IPPPPGLGGI
     KASSETPRPQ PVDKLEKILE KLLTRFPQCN KAQMTNILQQ IKTARTTMAG LTMEELIQLV
     AARLAEHERV ASSTQAPPTC KLCLMCQKLV QPSELHPMAC THALHKECIK FWAQTNTNDT
     CPFCPTLK
//
ID   KCTD3_MOUSE             Reviewed;         815 AA.
AC   Q8BFX3; Q6P7X4;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=BTB/POZ domain-containing protein KCTD3;
GN   Name=Kctd3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Ovary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BFX3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BFX3-2; Sequence=VSP_020070, VSP_020071;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the KCTD3 family.
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC   -!- SIMILARITY: Contains 5 WD repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK049362; BAC33709.1; -; mRNA.
DR   EMBL; AK087865; BAC40028.1; -; mRNA.
DR   EMBL; BC061458; AAH61458.1; -; mRNA.
DR   EMBL; BC079581; AAH79581.1; -; mRNA.
DR   IPI; IPI00221502; -.
DR   IPI; IPI00776076; -.
DR   RefSeq; NP_766238.1; NM_172650.2.
DR   UniGene; Mm.209880; -.
DR   UniGene; Mm.471891; -.
DR   ProteinModelPortal; Q8BFX3; -.
DR   SMR; Q8BFX3; 15-109.
DR   STRING; Q8BFX3; -.
DR   PhosphoSite; Q8BFX3; -.
DR   PRIDE; Q8BFX3; -.
DR   Ensembl; ENSMUST00000085678; ENSMUSP00000082821; ENSMUSG00000026608.
DR   GeneID; 226823; -.
DR   KEGG; mmu:226823; -.
DR   UCSC; uc007eai.1; mouse.
DR   CTD; 226823; -.
DR   MGI; MGI:2444629; Kctd3.
DR   eggNOG; roNOG12393; -.
DR   GeneTree; ENSGT00390000013581; -.
DR   HOGENOM; HBG386524; -.
DR   HOVERGEN; HBG061001; -.
DR   InParanoid; Q8BFX3; -.
DR   OMA; VWHAMTQ; -.
DR   OrthoDB; EOG4SF959; -.
DR   NextBio; 378359; -.
DR   ArrayExpress; Q8BFX3; -.
DR   Bgee; Q8BFX3; -.
DR   Genevestigator; Q8BFX3; -.
DR   GermOnline; ENSMUSG00000026608; Mus musculus.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 3.
DR   Pfam; PF02214; K_tetra; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00320; WD40; 3.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR   PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Phosphoprotein; Repeat; WD repeat.
FT   CHAIN         1    815       BTB/POZ domain-containing protein KCTD3.
FT                                /FTId=PRO_0000247840.
FT   DOMAIN       18     87       BTB.
FT   REPEAT      225    272       WD 1.
FT   REPEAT      277    314       WD 2.
FT   REPEAT      316    351       WD 3.
FT   REPEAT      420    458       WD 4.
FT   REPEAT      538    578       WD 5.
FT   MOD_RES     712    712       Phosphoserine (By similarity).
FT   VAR_SEQ     382    403       VSGNWIEIAYGTSSGAVRVIVQ -> QYTVSAETGLRSPMV
FT                                RALEPCE (in isoform 2).
FT                                /FTId=VSP_020070.
FT   VAR_SEQ     404    815       Missing (in isoform 2).
FT                                /FTId=VSP_020071.
SQ   SEQUENCE   815 AA;  88862 MW;  E2A45B4169A6E40C CRC64;
     MAGGHCGSFA ASAASSGEIV QLNVGGTRFS TSRQTLMWIP DSFFSSLLSG RISTLRDETG
     AIFIDRDPAA FAPILNFLRT KELDLRGVSI NVLRHEAEFY GITPLVRRLL LCEELERSSC
     GSVLFHGYLP PPGIPSRKVT NTARSSVDAR NGLNSMEGEA RGNGTQPVLA GNGEDTIRLG
     VPVDPRKVLI VAGHHNWIVA AYAHFAVCYR IKESSGWQQV FTSPYLDWTI ERVALNAKVV
     GGPHGDKDKM VAVASESSII LWSVQDGGSG SEIGVFSLGV PVDALFFIGN QLVATSHTGK
     VGVWNAVTQH WQVQDVVPIT SYDTAGSFLL LGCNNGSIYY IDMQKFPLRM KDNDLLVTEL
     YHDPSNDAVT ALSVYLTPKT SVSGNWIEIA YGTSSGAVRV IVQHPETVGS GPQLFQTFTV
     HRSPVTKIML SEKHLVSVCA DNNHVRTWTV TRFRGMISTQ PGSTPLASFK ILSLEETESH
     GSYSSGNDIG PFGERDDQQV FIQKVVPITN KLFVRLSSTG KRICEIQAVD CTTISSFTVR
     ECEGSSRMGS RPRRYLFTGH TNGSIQMWDL TTAMDMVNKT EDKDAGGPTE EELLKLLDQC
     DLSTSRCATP NISPATSVLQ HSRLRESSSS LQLQHHETIH EAATYGATRP YRESPLLARA
     RRTESFHSYR DFQTLNLNRS IERPVPENGH MGPAQTEVKG AAGECAMSER RSPGTEVRCG
     RESDGGLEVH RTAEGLSEPK KRSAEDENEH KVEFRKKGFE AGGFLGRKKV PYLASSPSTS
     DGGTDSPGTA SPSPTKTTPS PRHKKSDSSG QEYSL
//
ID   Q8BFX6_MOUSE            Unreviewed;       328 AA.
AC   Q8BFX6;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Cdk14; Synonyms=Pftk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Parthenogenote, and Spinal ganglion;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Parthenogenote, and Spinal ganglion;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Parthenogenote, and Spinal ganglion;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Parthenogenote, and Spinal ganglion;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Parthenogenote, and Spinal ganglion;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Parthenogenote, and Spinal ganglion;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Parthenogenote, and Spinal ganglion;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Parthenogenote;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily.
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DR   EMBL; AK045083; BAC32212.1; -; mRNA.
DR   EMBL; AK083790; BAC39020.1; -; mRNA.
DR   IPI; IPI00474969; -.
DR   RefSeq; NP_035204.2; NM_011074.2.
DR   UniGene; Mm.389061; -.
DR   UniGene; Mm.404502; -.
DR   HSSP; P24941; 1OIQ.
DR   ProteinModelPortal; Q8BFX6; -.
DR   SMR; Q8BFX6; 133-306.
DR   STRING; Q8BFX6; -.
DR   PRIDE; Q8BFX6; -.
DR   GeneID; 18647; -.
DR   KEGG; mmu:18647; -.
DR   UCSC; uc008wil.1; mouse.
DR   CTD; 18647; -.
DR   MGI; MGI:894318; Cdk14.
DR   HOVERGEN; HBG014652; -.
DR   NextBio; 294648; -.
DR   Genevestigator; Q8BFX6; -.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding;
KW   Serine/threonine-protein kinase; Transferase.
SQ   SEQUENCE   328 AA;  37210 MW;  E224C81A20C77E80 CRC64;
     MCDLIEPQPA EKIGKMKKLR RTLSESFSRI ALKKEDTTFD EICVTKMSTR NCQGTDSVIK
     HLDTIPEDKK VRVQRTQSTF DPFEKPANQV KRVHSENNAC INFKSSSAGK ESPKVRRHSS
     PSSPTSPKFG KADSYEKLEK LGEGSYATVY KGKSKVNGKL VALKVIRLQE EEGTPFTAIR
     EASLLKGLKH ANIVLLHDII HTKETLTLVF EYVHTDLCQY MDKHPGGLHP DNVKLFLFQL
     LRGLSYIHQR YILHRDLKPQ NLLISDTGEL KLADFGRKAV NYRSICHTVR VLGRWWHCLC
     LGAVPLPPQI MGNSFLSGMK KLLLPFEK
//
ID   LPPR1_MOUSE             Reviewed;         325 AA.
AC   Q8BFZ2; Q4V9R3; Q5DTF2; Q8BID2; Q8BIQ1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Lipid phosphate phosphatase-related protein type 1;
DE   AltName: Full=Plasticity-related gene 3 protein;
DE            Short=PRG-3;
GN   Name=Lppr1; Synonyms=Kiaa4247, Prg3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=14750979; DOI=10.1046/j.1460-9568.2003.03078.x;
RA   Savaskan N.E., Brauer A.U., Nitsch R.;
RT   "Molecular cloning and expression regulation of PRG-3, a new member of
RT   the plasticity-related gene family.";
RL   Eur. J. Neurosci. 19:212-220(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain cortex, Corpus striatum, Diencephalon, and Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=CD-1; TISSUE=Neural stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BFZ2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BFZ2-2; Sequence=VSP_031009;
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90332.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AY345342; AAR09144.1; -; mRNA.
DR   EMBL; AK220568; BAD90332.1; ALT_INIT; mRNA.
DR   EMBL; AK034251; BAC28649.1; -; mRNA.
DR   EMBL; AK043762; BAC31647.1; -; mRNA.
DR   EMBL; AK047614; BAC33101.1; -; mRNA.
DR   EMBL; AK087439; BAC39874.1; -; mRNA.
DR   EMBL; AK087514; BAC39907.1; -; mRNA.
DR   EMBL; AK160897; BAE36076.1; -; mRNA.
DR   EMBL; AL928612; CAM24757.1; -; Genomic_DNA.
DR   EMBL; AL808138; CAM24757.1; JOINED; Genomic_DNA.
DR   EMBL; BX537352; CAM24757.1; JOINED; Genomic_DNA.
DR   EMBL; AL808138; CAM27127.1; -; Genomic_DNA.
DR   EMBL; AL928612; CAM27127.1; JOINED; Genomic_DNA.
DR   EMBL; BX537352; CAM27127.1; JOINED; Genomic_DNA.
DR   EMBL; BX537352; CAM27900.1; -; Genomic_DNA.
DR   EMBL; AL808138; CAM27900.1; JOINED; Genomic_DNA.
DR   EMBL; AL928612; CAM27900.1; JOINED; Genomic_DNA.
DR   EMBL; BC096762; AAH96762.1; -; mRNA.
DR   IPI; IPI00221526; -.
DR   IPI; IPI00885510; -.
DR   RefSeq; NP_848871.1; NM_178756.4.
DR   UniGene; Mm.299460; -.
DR   ProteinModelPortal; Q8BFZ2; -.
DR   PhosphoSite; Q8BFZ2; -.
DR   PRIDE; Q8BFZ2; -.
DR   Ensembl; ENSMUST00000076670; ENSMUSP00000075966; ENSMUSG00000063446.
DR   GeneID; 272031; -.
DR   KEGG; mmu:272031; -.
DR   UCSC; uc008svp.1; mouse.
DR   MGI; MGI:2445015; E130309F12Rik.
DR   eggNOG; roNOG07570; -.
DR   GeneTree; ENSGT00550000074203; -.
DR   HOGENOM; HBG445665; -.
DR   HOVERGEN; HBG108093; -.
DR   InParanoid; Q8BFZ2; -.
DR   OMA; TSADCRA; -.
DR   OrthoDB; EOG4K6G4N; -.
DR   PhylomeDB; Q8BFZ2; -.
DR   NextBio; 393547; -.
DR   ArrayExpress; Q8BFZ2; -.
DR   Bgee; Q8BFZ2; -.
DR   CleanEx; MM_E130309F12RIK; -.
DR   CleanEx; MM_PRG3; -.
DR   Genevestigator; Q8BFZ2; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   InterPro; IPR016118; P_Acid_Pase/Cl_peroxidase_N.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   Gene3D; G3DSA:1.20.144.10; P_Acid_Pase/Cl_peroxidase_N; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; AcPase_VanPerase; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Glycoprotein; Membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    325       Lipid phosphate phosphatase-related
FT                                protein type 1.
FT                                /FTId=PRO_0000317533.
FT   TRANSMEM     13     33       Helical; (Potential).
FT   TRANSMEM     67     87       Helical; (Potential).
FT   TRANSMEM    127    147       Helical; (Potential).
FT   TRANSMEM    201    218       Helical; (Potential).
FT   TRANSMEM    230    247       Helical; (Potential).
FT   TRANSMEM    257    277       Helical; (Potential).
FT   MOD_RES     307    307       Phosphoserine.
FT   CARBOHYD      5      5       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    163    163       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    316    316       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     129    158       Missing (in isoform 2).
FT                                /FTId=VSP_031009.
FT   CONFLICT     58     58       P -> L (in Ref. 5; AAH96762).
FT   CONFLICT    190    190       E -> G (in Ref. 3; BAC39874).
SQ   SEQUENCE   325 AA;  35932 MW;  DB884AEAFB759094 CRC64;
     MAVENNTQRS YSIIPCFIFV ELVIMAGTVL LAYYFECTDT FQVHIQGFFC QDGDLMKPYP
     GTEEESFISP LVLYCVLAAT PTAIIFIGEI SMYFIKSTRE SLIAEEKMIL TGDCCYLSPL
     LRRIIRFIGV FAFGLFATDI FVNAGQVVTG HLTPYFLTVC QPNYTSTDCR AHQQFINNGN
     ICTGDLEVIE KARRSFPSKH AALSIYSALY ATMYITSTIK TKSSRLAKPV LCLGTLCTAF
     LTGLNRVSEY RNHCSDVIAG FILGTAVALF LGMCVVHNFR GTQGSPSKPK PEDPRGVPLM
     AFPRIESPLE TLSAQNHSAS MTEVT
//
ID   2ABG_MOUSE              Reviewed;         447 AA.
AC   Q8BG02;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B gamma isoform;
DE   AltName: Full=PP2A subunit B isoform B55-gamma;
DE   AltName: Full=PP2A subunit B isoform PR55-gamma;
DE   AltName: Full=PP2A subunit B isoform R2-gamma;
DE   AltName: Full=PP2A subunit B isoform gamma;
GN   Name=Ppp2r2c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Zhou G., Huang X., Yu L.;
RT   "Cloning of mouse protein phosphatase 2 (formerly 2A), regulatory
RT   subunit B.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: The B regulatory subunit might modulate substrate
CC       selectivity and catalytic activity, and also might direct the
CC       localization of the catalytic enzyme to a particular subcellular
CC       compartment (By similarity).
CC   -!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme,
CC       composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa
CC       constant regulatory subunit (PR65 or subunit A), that associates
CC       with a variety of regulatory subunits. Proteins that associate
CC       with the core dimer include three families of regulatory subunits
CC       B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56
CC       families), the 48 kDa variable regulatory subunit, viral proteins,
CC       and cell signaling molecules (By similarity).
CC   -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B
CC       family.
CC   -!- SIMILARITY: Contains 7 WD repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY348866; AAQ55226.1; -; mRNA.
DR   EMBL; AK032023; BAC27654.1; -; mRNA.
DR   EMBL; AK049830; BAC33942.1; -; mRNA.
DR   EMBL; BC059811; AAH59811.1; -; mRNA.
DR   IPI; IPI00221411; -.
DR   RefSeq; NP_766582.1; NM_172994.2.
DR   UniGene; Mm.41694; -.
DR   ProteinModelPortal; Q8BG02; -.
DR   SMR; Q8BG02; 21-442.
DR   STRING; Q8BG02; -.
DR   PhosphoSite; Q8BG02; -.
DR   PRIDE; Q8BG02; -.
DR   Ensembl; ENSMUST00000031003; ENSMUSP00000031003; ENSMUSG00000029120.
DR   GeneID; 269643; -.
DR   KEGG; mmu:269643; -.
DR   UCSC; uc008xfe.1; mouse.
DR   CTD; 269643; -.
DR   MGI; MGI:2442660; Ppp2r2c.
DR   eggNOG; roNOG04944; -.
DR   GeneTree; ENSGT00390000006311; -.
DR   HOGENOM; HBG443924; -.
DR   HOVERGEN; HBG000012; -.
DR   InParanoid; Q8BG02; -.
DR   OMA; MGEDTDT; -.
DR   OrthoDB; EOG4M0F1K; -.
DR   PhylomeDB; Q8BG02; -.
DR   NextBio; 392963; -.
DR   ArrayExpress; Q8BG02; -.
DR   Bgee; Q8BG02; -.
DR   Genevestigator; Q8BG02; -.
DR   GermOnline; ENSMUSG00000029120; Mus musculus.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:InterPro.
DR   GO; GO:0008601; F:protein phosphatase type 2A regulator activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR000009; PP2A_PR55.
DR   InterPro; IPR018067; PP2A_PR55_CS.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
DR   PANTHER; PTHR11871; Pp2A_PR55; 1.
DR   Pfam; PF00400; WD40; 1.
DR   PIRSF; PIRSF037309; PP2A_PR55; 1.
DR   PRINTS; PR00600; PP2APR55.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS01024; PR55_1; 1.
DR   PROSITE; PS01025; PR55_2; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR   PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Repeat; WD repeat.
FT   CHAIN         1    447       Serine/threonine-protein phosphatase 2A
FT                                55 kDa regulatory subunit B gamma
FT                                isoform.
FT                                /FTId=PRO_0000071430.
FT   REPEAT       22     61       WD 1.
FT   REPEAT       87    128       WD 2.
FT   REPEAT      171    209       WD 3.
FT   REPEAT      220    260       WD 4.
FT   REPEAT      279    317       WD 5.
FT   REPEAT      334    375       WD 6.
FT   REPEAT      410    446       WD 7.
SQ   SEQUENCE   447 AA;  51462 MW;  D94D0156CB4A3035 CRC64;
     MGEDTDTRKI NHSFLRDHSY VTEADVISTV EFNHTGELLA TGDKGGRVVI FQREPESKNA
     PHSQGEYDVY STFQSHEPEF DYLKSLEIEE KINKIKWLPQ QNAAHSLLST NDKTIKLWKI
     TERDKRPEGY NLKDEEGKLK DLSTVTSLQV PVLKPMDLMV EVSPRRTFAN GHTYHINSIS
     VNSDCETYMS ADDLRINLWH LAITDRSFNI VDIKPANMED LTEVITASEF HPHHCNLFVY
     SSSKGSLRLC DMRAAALCDK HSKLFEEPED PSNRSFFSEI ISSVSDVKFS HSGRYMLTRD
     YLTVKVWDLN MEARPIETYQ VHDYLRSKLC SLYESDCIFD KFECAWNGSD SVIMTGAYNN
     FFRMFDRNTK RDVTLEASRE SSKPRAVLKP RRVCVGGKRR RDDISVDSLD FTKKILHTAW
     HPAENIIAIA ATNNLYIFQD KVNSDMH
//
ID   T184B_MOUSE             Reviewed;         407 AA.
AC   Q8BG09; Q3TY97; Q8BJ02;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Transmembrane protein 184B;
GN   Name=Tmem184b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Embryo, Head, Liver, Skin, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May activate the MAP kinase signaling pathway (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the TMEM184 family.
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DR   EMBL; AK028196; BAC25805.1; -; mRNA.
DR   EMBL; AK029129; BAC26312.1; -; mRNA.
DR   EMBL; AK048138; BAC33254.1; -; mRNA.
DR   EMBL; AK149366; BAE28837.1; -; mRNA.
DR   EMBL; AK158789; BAE34666.1; -; mRNA.
DR   EMBL; AK170086; BAE41556.1; -; mRNA.
DR   EMBL; BC046959; AAH46959.1; -; mRNA.
DR   IPI; IPI00221420; -.
DR   RefSeq; NP_766196.1; NM_172608.1.
DR   UniGene; Mm.323358; -.
DR   PhosphoSite; Q8BG09; -.
DR   PRIDE; Q8BG09; -.
DR   Ensembl; ENSMUST00000074991; ENSMUSP00000074518; ENSMUSG00000009035.
DR   GeneID; 223693; -.
DR   KEGG; mmu:223693; -.
DR   UCSC; uc007wti.1; mouse.
DR   CTD; 223693; -.
DR   MGI; MGI:2445179; Tmem184b.
DR   GeneTree; ENSGT00530000063204; -.
DR   HOGENOM; HBG389350; -.
DR   HOVERGEN; HBG051270; -.
DR   InParanoid; Q8BG09; -.
DR   OMA; WQNFFIC; -.
DR   OrthoDB; EOG4Z0B5P; -.
DR   PhylomeDB; Q8BG09; -.
DR   NextBio; 376822; -.
DR   ArrayExpress; Q8BG09; -.
DR   Bgee; Q8BG09; -.
DR   CleanEx; MM_TMEM184B; -.
DR   Genevestigator; Q8BG09; -.
DR   GermOnline; ENSMUSG00000009035; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR005178; DUF300.
DR   PANTHER; PTHR23423; DUF300; 1.
DR   Pfam; PF03619; DUF300; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    407       Transmembrane protein 184B.
FT                                /FTId=PRO_0000211556.
FT   TRANSMEM     40     60       Helical; (Potential).
FT   TRANSMEM     84    104       Helical; (Potential).
FT   TRANSMEM    121    141       Helical; (Potential).
FT   TRANSMEM    178    198       Helical; (Potential).
FT   TRANSMEM    214    234       Helical; (Potential).
FT   TRANSMEM    249    269       Helical; (Potential).
FT   TRANSMEM    290    310       Helical; (Potential).
FT   COMPBIAS     16     19       Poly-Thr.
FT   MOD_RES     398    398       Phosphothreonine (By similarity).
FT   MOD_RES     402    402       Phosphoserine (By similarity).
FT   MOD_RES     403    403       Phosphoserine (By similarity).
FT   CONFLICT    327    327       Q -> QVLTYGPY (in Ref. 1; BAC33254).
SQ   SEQUENCE   407 AA;  45589 MW;  D708E141A34DEC73 CRC64;
     MTVRGAALAP DPASPTTTTA SPSVSATPEG SPTAMEHPVF LMTTAAQAIS GFFVWTALLI
     TCHQIYMHLR CYSRPNEQRH IVRILFIVPI YAFDSWLSLL FFTNDQYYVY FGTVRDCYEA
     FVIYNFLSLC YEYLGGESAI MSEIRGKAIE SSCMYGTCCL WGKTYSIGFL RFCKQATLQF
     CVVKPLMAVS TVILQAFGKY RDGDFDVTSG YLYVTIIYNI SVSLALYALF LFYFATRELL
     SPYSPVLKFF MVKSVIFLSF WQGMLLAILE KCGAIPKINS ARVSVGEGTV AAGYQDFIIC
     VEMFFAALAL RHAFTYKVYA DKRLDAQGRC APMKSISSSL KETMNPHDIV QDAIHNFSPA
     YQQYTQQSTL EPGPTWRGGT HSLSRSHSLS GARDNEKTLL LSSDDEF
//
ID   S6A15_MOUSE             Reviewed;         729 AA.
AC   Q8BG16;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Orphan sodium- and chloride-dependent neurotransmitter transporter NTT73;
DE   AltName: Full=Orphan transporter v7-3;
DE   AltName: Full=Solute carrier family 6 member 15;
GN   Name=Slc6a15; Synonyms=Ntt73;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6;
RA   Liu Q.-R., Uhl G.R.;
RT   "Mouse sodium-dependent orphan neurotransmitter transporter V73
RT   cDNA.";
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129/SvJ;
RA   Liu Q.-R., Uhl G.R.;
RT   "Characterization of orphan neurotransmitter transporter V73 genomic
RT   structure.";
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Not yet known, orphan transporter.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF)
CC       (TC 2.A.22) family. SLC6A15 subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; AY149280; AAN75437.1; -; mRNA.
DR   EMBL; AY149281; AAN75438.1; -; mRNA.
DR   EMBL; AY149282; AAN75439.1; -; Genomic_DNA.
DR   EMBL; AK036136; BAC29315.1; -; mRNA.
DR   EMBL; BC076593; AAH76593.1; -; mRNA.
DR   IPI; IPI00221428; -.
DR   RefSeq; NP_780537.1; NM_175328.2.
DR   UniGene; Mm.458408; -.
DR   ProteinModelPortal; Q8BG16; -.
DR   PhosphoSite; Q8BG16; -.
DR   PRIDE; Q8BG16; -.
DR   Ensembl; ENSMUST00000074204; ENSMUSP00000073829; ENSMUSG00000019894.
DR   GeneID; 103098; -.
DR   KEGG; mmu:103098; -.
DR   UCSC; uc007gyj.1; mouse.
DR   CTD; 103098; -.
DR   MGI; MGI:2143484; Slc6a15.
DR   HOGENOM; HBG702834; -.
DR   HOVERGEN; HBG071421; -.
DR   InParanoid; Q8BG16; -.
DR   OMA; SFVYGID; -.
DR   OrthoDB; EOG4N04DJ; -.
DR   PhylomeDB; Q8BG16; -.
DR   NextBio; 355783; -.
DR   ArrayExpress; Q8BG16; -.
DR   Bgee; Q8BG16; -.
DR   Genevestigator; Q8BG16; -.
DR   GermOnline; ENSMUSG00000019894; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; IEA:InterPro.
DR   GO; GO:0005328; F:neurotransmitter:sodium symporter activity; IEA:InterPro.
DR   InterPro; IPR000175; Na/ntran_symport.
DR   InterPro; IPR002438; Na/ntran_symport_orphan.
DR   PANTHER; PTHR11616; Na/ntran_symport; 1.
DR   Pfam; PF00209; SNF; 1.
DR   PRINTS; PR00176; NANEUSMPORT.
DR   PRINTS; PR01206; ORPHTRNSPORT.
DR   PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR   PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
DR   PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Neurotransmitter transport; Phosphoprotein;
KW   Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    729       Orphan sodium- and chloride-dependent
FT                                neurotransmitter transporter NTT73.
FT                                /FTId=PRO_0000214799.
FT   TOPO_DOM      1     69       Cytoplasmic (Potential).
FT   TRANSMEM     70     90       Helical; Name=1; (Potential).
FT   TRANSMEM     98    117       Helical; Name=2; (Potential).
FT   TRANSMEM    142    162       Helical; Name=3; (Potential).
FT   TOPO_DOM    163    225       Extracellular (Potential).
FT   TRANSMEM    226    244       Helical; Name=4; (Potential).
FT   TRANSMEM    253    270       Helical; Name=5; (Potential).
FT   TRANSMEM    306    323       Helical; Name=6; (Potential).
FT   TRANSMEM    335    356       Helical; Name=7; (Potential).
FT   TOPO_DOM    357    452       Extracellular (Potential).
FT   TRANSMEM    453    472       Helical; Name=8; (Potential).
FT   TRANSMEM    496    514       Helical; Name=9; (Potential).
FT   TRANSMEM    530    550       Helical; Name=10; (Potential).
FT   TRANSMEM    571    592       Helical; Name=11; (Potential).
FT   TRANSMEM    620    642       Helical; Name=12; (Potential).
FT   TOPO_DOM    643    729       Cytoplasmic (Potential).
FT   MOD_RES      55     55       Phosphoserine (By similarity).
FT   MOD_RES     687    687       Phosphoserine (By similarity).
FT   MOD_RES     699    699       Phosphoserine (By similarity).
FT   MOD_RES     701    701       Phosphoserine (By similarity).
FT   CARBOHYD    187    187       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    276    276       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    383    383       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    394    394       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   729 AA;  81792 MW;  D336735E9D1E9B97 CRC64;
     MPKNSKVVKR DLDDDVIESV KDLLSNEDSV EEVSKKSELI VDVQEEKDTD AEDGSEADDE
     RPAWNSKLQY ILAQVGFSVG LGNVWRFPYL CQKNGGGAYL LPYLILLLVI GIPLFFLELS
     VGQRIRRGSI GVWNYISPKL GGIGFASCVV CYFVALYYNV IIGWTLFYFS QSFQQPLPWD
     QCPLVKNASH TYVEPECEQS SATTYYWYRE ALDITSSISD SGGLNWKMTV CLLVAWVMVC
     LAMIKGIQSS GKIMYFSSLF PYVVLICFLI RSLLLNGSID GIRHMFTPKL EMMLEPKVWR
     EAATQVFFAL GLGFGGVIAF SSYNKRDNNC HFDAVLVSFI NFFTSVLATL VVFAVLGFKA
     NIVNEKCISQ NSEMILKLLK MGNISWDVIP HHINLSAVTV EDYRLVYDII QKVKEEEFAV
     LHLNACQIED ELNKAVQGTG LAFIAFTEAM THFPASPFWS VMFFLMLINL GLGSMFGTIE
     GIITPIVDTF KVRKEILTVI CCLLAFCIGL IFVQRSGNYF VTMFDDYSAT LPLLIVVILE
     NIAVSFVYGI DKFIEDLTDM LGFAPSKYYY YMWKYISPLM LLTLLIASIV NMGLSPPGYN
     AWIKEKASEE FLSYPMWGMV VCFSLMVLAI LPVPVVFIIR RCNLIDDSSG NLASVTYKRG
     RVLKEPVNLE GDDASLIHGK IPSEMSSPNF GKNIYRKQSG SPTLDTAPNG RYGIGYLMAD
     MPDMPESDL
//
ID   NECA1_MOUSE             Reviewed;         352 AA.
AC   Q8BG18; Q80W91;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=N-terminal EF-hand calcium-binding protein 1;
DE            Short=EF-hand calcium-binding protein 1;
GN   Name=Necab1; Synonyms=Efcbp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Kunming;
RA   Wu H., Yu L., Li D.;
RT   "Cloning and characterization of human and mouse NECAB1.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, Liver, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=12044471; DOI=10.1016/S0306-4522(02)00063-5;
RA   Sugita S., Ho A., Suedhof T.C.;
RT   "NECABs: a family of neuronal Ca(2+)-binding proteins with an unusual
RT   domain structure and a restricted expression pattern.";
RL   Neuroscience 112:51-63(2002).
CC   -!- SUBUNIT: Interacts with STX1 and CPNE6 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC       Expressed in the cerebral cortex only in layer 4, thalamic nuclei
CC       (the mediodorsal nucleus), hippocampus (a small band of pyramidal
CC       neurons at the boundary between CA1 and CA3), interneurons
CC       interspersed throughout the hippocampus proper, interneurons in
CC       the hilus, bodies of the neurons but also their dendritic
CC       projections (at protein level).
CC   -!- SIMILARITY: Contains 1 ABM domain.
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY278200; AAP32077.1; -; mRNA.
DR   EMBL; AK039240; BAC30290.1; -; mRNA.
DR   EMBL; AK050307; BAC34179.1; -; mRNA.
DR   EMBL; AK081951; BAC38379.1; -; mRNA.
DR   EMBL; AL732571; CAM18343.1; -; Genomic_DNA.
DR   EMBL; AL831792; CAM18343.1; JOINED; Genomic_DNA.
DR   EMBL; AL929383; CAM18343.1; JOINED; Genomic_DNA.
DR   EMBL; AL929383; CAM20237.1; -; Genomic_DNA.
DR   EMBL; AL732571; CAM20237.1; JOINED; Genomic_DNA.
DR   EMBL; AL831792; CAM20237.1; JOINED; Genomic_DNA.
DR   EMBL; AL831792; CAM22572.1; -; Genomic_DNA.
DR   EMBL; AL732571; CAM22572.1; JOINED; Genomic_DNA.
DR   EMBL; AL929383; CAM22572.1; JOINED; Genomic_DNA.
DR   EMBL; BC067055; AAH67055.1; -; mRNA.
DR   IPI; IPI00221430; -.
DR   RefSeq; NP_848732.3; NM_178617.4.
DR   UniGene; Mm.389031; -.
DR   HSSP; P02633; 1HT9.
DR   ProteinModelPortal; Q8BG18; -.
DR   SMR; Q8BG18; 31-94, 248-334.
DR   PRIDE; Q8BG18; -.
DR   Ensembl; ENSMUST00000041606; ENSMUSP00000038165; ENSMUSG00000040536.
DR   Ensembl; ENSMUST00000108273; ENSMUSP00000103908; ENSMUSG00000040536.
DR   GeneID; 69352; -.
DR   KEGG; mmu:69352; -.
DR   UCSC; uc008sbi.1; mouse.
DR   CTD; 69352; -.
DR   MGI; MGI:1916602; Necab1.
DR   eggNOG; roNOG14818; -.
DR   GeneTree; ENSGT00390000009734; -.
DR   HOGENOM; HBG446692; -.
DR   HOVERGEN; HBG050433; -.
DR   InParanoid; Q8BG18; -.
DR   OMA; WNSHLQT; -.
DR   OrthoDB; EOG4F7NKP; -.
DR   PhylomeDB; Q8BG18; -.
DR   NextBio; 329196; -.
DR   ArrayExpress; Q8BG18; -.
DR   Bgee; Q8BG18; -.
DR   CleanEx; MM_NECAB1; -.
DR   Genevestigator; Q8BG18; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR   InterPro; IPR007138; Antibiotic_mOase.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   Pfam; PF03992; ABM; 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF54909; Dimer_A_B_barrel; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   1: Evidence at protein level;
KW   Calcium; Coiled coil; Cytoplasm; Repeat.
FT   CHAIN         1    352       N-terminal EF-hand calcium-binding
FT                                protein 1.
FT                                /FTId=PRO_0000282610.
FT   DOMAIN       26     61       EF-hand 1.
FT   DOMAIN       60     95       EF-hand 2.
FT   DOMAIN      260    322       ABM.
FT   CA_BIND      39     50       1 (Potential).
FT   COILED      135    163       Potential.
FT   COILED      209    275       Potential.
FT   CONFLICT    244    244       E -> G (in Ref. 1; AAP32077).
SQ   SEQUENCE   352 AA;  40934 MW;  D2B069AA7BA97036 CRC64;
     MEDSRETSPS SNNSSEELSS TLQLSKGMSI FLDILRRADK NDDGKLSFEE FKAYFADGVL
     SGEELHELFH TIDTHNTNNL DTEELCEYFS QHLGEYENVL AALEDLNLSI LKAMGKTKKD
     YQEASNLEQF VTRFLLKETL NQLQSLQNSL ECAMETTEEQ TRQERQGPSK PEVLSIQWPG
     KRSSRRVQRH NSFSPNSPQF NVSSPALLEE DNQWMTQINR LQKLIDRLEK KDLKLEPLEE
     EIIEENTKPH IMLVQRQMSV TEEDLEEFQL ALKHYVESAS AQSGCLRISI QKLSNESRYM
     IYEFWENSSV WNRHLQTNYS KTFQRSNVDF LETPELTSTM LVPASWWILN NN
//
ID   RUSC1_MOUSE             Reviewed;         893 AA.
AC   Q8BG26; Q6PHT9;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=RUN and SH3 domain-containing protein 1;
GN   Name=Rusc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Olfactory bulb, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Putative signaling adapter which may play a role in
CC       neuronal differentiation. May be involved in regulation of NGF-
CC       dependent neurite outgrowth. Seems to be involved in signaling
CC       pathways that are regulated by the prolonged activation of MAPK
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Translocated to the nuclear envelope upon
CC       stimulation with NGF (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BG26-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BG26-2; Sequence=VSP_010856;
CC       Name=3;
CC         IsoId=Q8BG26-3; Sequence=VSP_010857;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The RUN domain is necessary for NGF induced nuclear
CC       redistribution (By similarity).
CC   -!- PTM: Phosphorylated on serine residues following nuclear
CC       translocation (By similarity).
CC   -!- SIMILARITY: Contains 1 RUN domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC27820.1; Type=Erroneous initiation;
CC       Sequence=BAC30411.1; Type=Erroneous initiation;
CC       Sequence=BAC31333.1; Type=Erroneous termination; Positions=462; Note=Translated as Trp;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK032334; BAC27820.1; ALT_INIT; mRNA.
DR   EMBL; AK039664; BAC30411.1; ALT_INIT; mRNA.
DR   EMBL; AK042689; BAC31333.1; ALT_SEQ; mRNA.
DR   EMBL; BC056360; AAH56360.1; -; mRNA.
DR   EMBL; BC057034; AAH57034.1; -; mRNA.
DR   IPI; IPI00420953; -.
DR   IPI; IPI00453889; -.
DR   IPI; IPI00453890; -.
DR   RefSeq; NP_001077276.1; NM_001083807.1.
DR   RefSeq; NP_001077277.1; NM_001083808.1.
DR   RefSeq; NP_082464.2; NM_028188.2.
DR   UniGene; Mm.27687; -.
DR   ProteinModelPortal; Q8BG26; -.
DR   SMR; Q8BG26; 840-890.
DR   STRING; Q8BG26; -.
DR   PhosphoSite; Q8BG26; -.
DR   PRIDE; Q8BG26; -.
DR   Ensembl; ENSMUST00000052539; ENSMUSP00000056640; ENSMUSG00000041263.
DR   Ensembl; ENSMUST00000090929; ENSMUSP00000088447; ENSMUSG00000041263.
DR   GeneID; 72296; -.
DR   KEGG; mmu:72296; -.
DR   UCSC; uc008pxl.1; mouse.
DR   UCSC; uc008pxm.1; mouse.
DR   UCSC; uc008pxn.1; mouse.
DR   CTD; 72296; -.
DR   MGI; MGI:1919546; Rusc1.
DR   GeneTree; ENSGT00530000063878; -.
DR   HOVERGEN; HBG058522; -.
DR   OMA; LVPQAKK; -.
DR   OrthoDB; EOG4ZGPCS; -.
DR   NextBio; 335934; -.
DR   ArrayExpress; Q8BG26; -.
DR   Bgee; Q8BG26; -.
DR   CleanEx; MM_RUSC1; -.
DR   Genevestigator; Q8BG26; -.
DR   GermOnline; ENSMUSG00000041263; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR004012; Run.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF02759; RUN; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00593; RUN; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50826; RUN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein; SH3 domain.
FT   CHAIN         1    893       RUN and SH3 domain-containing protein 1.
FT                                /FTId=PRO_0000097533.
FT   DOMAIN      515    659       RUN.
FT   DOMAIN      835    893       SH3.
FT   MOD_RES       3      3       Phosphoserine (By similarity).
FT   VAR_SEQ       1    462       Missing (in isoform 2).
FT                                /FTId=VSP_010856.
FT   VAR_SEQ     445    446       VV -> VAGPSLFPRPPVFRFSADGRPLLEGGGAGAPGSLL
FT                                FTPLTGWSNSRLRLLGAASPPEEQLLPVRLSPVGAYSPPTR
FT                                GALPCLASPELALLLSPLFPRSSTFPAAAPLPRQVPAPPLP
FT                                TPPCPPTAPRWTRRPPPPPRQL (in isoform 3).
FT                                /FTId=VSP_010857.
FT   CONFLICT    345    345       P -> Q (in Ref. 1; BAC27820).
SQ   SEQUENCE   893 AA;  95195 MW;  B7CB4102A3CFAAB2 CRC64;
     MLSPQRALLC NLNHIHLQHV SLGLHLSRRP ELREGPLSTP PPPGDTGGKE SRGPCSGTLV
     DANSNSPAVP CRCCQEHGSS IENQQDPSQE EEAVSPSDPG CSSSLSSCSD LSPDESPVSV
     YSRDLPGNED ANPQPSTLEL GSPLAPAGPS TCSPDSFCCS PDSCSGISSP PGPDLDSNCN
     ALTTCQDLPS PGLEEEEDSG EQDLATSELS ETEDGRIDAG KAEPSWKINP IWKIDTEKTE
     AGWKTIEDSD SGRKTDENTN SSLKTESGKL ASCLNTNSGS KIDAGKTDGG WRGDVSQEPV
     PHRTITSFHE LAQKRKRGPG LPLVPQAKKD RSDWLIVFSP DTELPPTGSL GGSLAPPREV
     TTFKELRSRS RAQPPPVPPR DPPAGWALVP PRPPPPPVPP RRKKNRLGLQ PIAEGLSEEG
     RAASPRAGEE ASASQEPEEP RAHAVVRSSW SFAGVPGAQR LWMAEAQSGT GQLQEQKKGL
     LIAVSASVDK IISHFGAARN LVQKAQLGDS RLSPDVGHLV LTTLCPALHA LVADGLKPFR
     KDLITGQRRS SPWSVVEASV KPGSCTHSMG SLYSQVSRLA PLSSSRSRFH AFILGLLNTK
     QLELWFSSLQ EDAGLLSLLY LPTGFFSLAR GSCPSLATEL LLLLQPLSVL TFHLDLLFEH
     HHHLPVGLQQ APAPSCPPPA LQQTMQAVLH WGERLAQSLR GTSGESTTDS STPSARPPAG
     SWWDQLTQAS RVYASGGTEG FPLLRWGPRR HGTTAEAAQE APPPTEQTTP GRSVWLGRLF
     GVPGCPSETE SGAFKSRRPS SWLPPTVSVL ALVKRGTPPE TPPEALVSSP GSVVQADRAV
     RALCDHTAAG PDQLSFQRGE LLRVIATVDE DWLRCGRDGV EGLVPVGYTS LVL
//
ID   SV2B_MOUSE              Reviewed;         683 AA.
AC   Q8BG39; Q80TT1; Q9ES95;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Synaptic vesicle glycoprotein 2B;
DE            Short=Synaptic vesicle protein 2B;
GN   Name=Sv2b; Synonyms=Kiaa0735;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain cortex, Corpora quadrigemina, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-150, AND FUNCTION.
RC   STRAIN=129/Sv;
RX   MEDLINE=20088300; PubMed=10624962; DOI=10.1016/S0896-6273(00)81046-6;
RA   Janz R., Goda Y., Geppert M., Missler M., Suedhof T.C.;
RT   "SV2A and SV2B function as redundant Ca2+ regulators in
RT   neurotransmitter release.";
RL   Neuron 24:1003-1016(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 96-683.
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=10611374; DOI=10.1073/pnas.96.26.15268;
RA   Crowder K.M., Gunther J.M., Jones T.A., Hale B.D., Zhang H.Z.,
RA   Peterson M.R., Scheller R.H., Chavkin C., Bajjalieh S.M.;
RT   "Abnormal neurotransmission in mice lacking synaptic vesicle protein
RT   2A (SV2A).";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:15268-15273(1999).
RN   [6]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=12687700; DOI=10.1002/cne.10636;
RA   Wang M.M., Janz R., Belizaire R., Frishman L.J., Sherry D.M.;
RT   "Differential distribution and developmental expression of synaptic
RT   vesicle protein 2 isoforms in the mouse retina.";
RL   J. Comp. Neurol. 460:106-122(2003).
RN   [7]
RP   INTERACTION WITH SYT1; SYNTAXIN-1 AND SNAP25.
RX   PubMed=15466855; DOI=10.1074/jbc.M407502200;
RA   Lazzell D.R., Belizaire R., Thakur P., Sherry D.M., Janz R.;
RT   "SV2B regulates synaptotagmin 1 by direct interaction.";
RL   J. Biol. Chem. 279:52124-52131(2004).
RN   [8]
RP   FUNCTION AS A BOTA RECEPTOR, AND DISRUPTION PHENOTYPE.
RX   PubMed=16543415; DOI=10.1126/science.1123654;
RA   Dong M., Yeh F., Tepp W.H., Dean C., Johnson E.A., Janz R.,
RA   Chapman E.R.;
RT   "SV2 is the protein receptor for botulinum neurotoxin A.";
RL   Science 312:592-596(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-423, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Probably plays a role in the control of regulated
CC       secretion in neural and endocrine cells (By similarity).
CC   -!- FUNCTION: Receptor for the botulinium neurotoxin type A/BOTA.
CC   -!- SUBUNIT: Interacts with SYT1 in a calcium-independent manner.
CC       Forms a complex with SYT1, syntaxin-1 and SNAP25.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane; Multi-pass membrane protein (By
CC       similarity). Cytoplasmic vesicle, secretory vesicle, acrosome (By
CC       similarity). Note=Associated with synaptic-like microvesicles but
CC       not with insulin-containing vesicles in insulin-secreting cells of
CC       the pancreas. Localizes to microvesicles in the pinealocytes.
CC       Localizes to the acrosome in spermatids (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in ribbon synapses of the retina (at
CC       protein level).
CC   -!- DEVELOPMENTAL STAGE: Expressed during synaptogenesis in the retina
CC       (at protein level).
CC   -!- INDUCTION: Up-regulated upon Sv2a depletion.
CC   -!- PTM: N-glycosylated (By similarity).
CC   -!- PTM: The N-terminal cytoplasmic domain is phosphorylated by CK1
CC       (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice display no particular phenotype. Mice
CC       lacking both Sv2a and Sv2b experience severe epileptic seizures
CC       and die immediately or shortly after birth similarly to mice
CC       lacking only Sv2a.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK029736; BAC26590.1; -; mRNA.
DR   EMBL; AK043830; BAC31669.1; -; mRNA.
DR   EMBL; AK139478; BAE24029.1; -; mRNA.
DR   EMBL; AK140104; BAE24238.1; -; mRNA.
DR   EMBL; AK147261; BAE27804.1; -; mRNA.
DR   EMBL; BC060224; AAH60224.1; -; mRNA.
DR   EMBL; AF196782; AAG28491.1; -; Genomic_DNA.
DR   EMBL; AK122359; BAC65641.1; -; mRNA.
DR   IPI; IPI00221456; -.
DR   RefSeq; NP_001103223.1; NM_001109753.1.
DR   RefSeq; NP_705807.2; NM_153579.4.
DR   UniGene; Mm.273082; -.
DR   ProteinModelPortal; Q8BG39; -.
DR   STRING; Q8BG39; -.
DR   PhosphoSite; Q8BG39; -.
DR   PRIDE; Q8BG39; -.
DR   Ensembl; ENSMUST00000085164; ENSMUSP00000082254; ENSMUSG00000053025.
DR   GeneID; 64176; -.
DR   KEGG; mmu:64176; -.
DR   UCSC; uc009hwj.1; mouse.
DR   CTD; 64176; -.
DR   MGI; MGI:1927338; Sv2b.
DR   eggNOG; roNOG13437; -.
DR   HOGENOM; HBG445732; -.
DR   HOVERGEN; HBG053967; -.
DR   InParanoid; Q8BG39; -.
DR   OMA; MNTLILA; -.
DR   OrthoDB; EOG4K0QMZ; -.
DR   NextBio; 319946; -.
DR   ArrayExpress; Q8BG39; -.
DR   Bgee; Q8BG39; -.
DR   CleanEx; MM_SV2B; -.
DR   Genevestigator; Q8BG39; -.
DR   GermOnline; ENSMUSG00000053025; Mus musculus.
DR   GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR   GO; GO:0007268; P:synaptic transmission; TAS:MGI.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR020846; Major_facilitator_SF.
DR   InterPro; IPR011701; MFS_1.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   InterPro; IPR005828; Sub_transporter.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   InterPro; IPR022308; SV2_chordata.
DR   Pfam; PF07690; MFS_1; 1.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
DR   TIGRFAMs; TIGR01299; synapt_SV2; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cytoplasmic vesicle; Glycoprotein; Membrane;
KW   Neurotransmitter transport; Phosphoprotein; Receptor; Synapse;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    683       Synaptic vesicle glycoprotein 2B.
FT                                /FTId=PRO_0000239769.
FT   TOPO_DOM      1    110       Cytoplasmic (Potential).
FT   TRANSMEM    111    131       Helical; (Potential).
FT   TOPO_DOM    132    148       Extracellular (Potential).
FT   TRANSMEM    149    169       Helical; (Potential).
FT   TOPO_DOM    170    182       Cytoplasmic (Potential).
FT   TRANSMEM    183    203       Helical; (Potential).
FT   TOPO_DOM    204    205       Extracellular (Potential).
FT   TRANSMEM    206    226       Helical; (Potential).
FT   TOPO_DOM    227    237       Cytoplasmic (Potential).
FT   TRANSMEM    238    258       Helical; (Potential).
FT   TOPO_DOM    259    277       Extracellular (Potential).
FT   TRANSMEM    278    298       Helical; (Potential).
FT   TOPO_DOM    299    390       Cytoplasmic (Potential).
FT   TRANSMEM    391    411       Helical; (Potential).
FT   TOPO_DOM    412    535       Extracellular (Potential).
FT   TRANSMEM    536    556       Helical; (Potential).
FT   TOPO_DOM    557    565       Cytoplasmic (Potential).
FT   TRANSMEM    566    586       Helical; (Potential).
FT   TOPO_DOM    587    592       Extracellular (Potential).
FT   TRANSMEM    593    613       Helical; (Potential).
FT   TOPO_DOM    614    626       Cytoplasmic (Potential).
FT   TRANSMEM    627    649       Helical; (Potential).
FT   TOPO_DOM    650    653       Extracellular (Potential).
FT   TRANSMEM    654    672       Helical; (Potential).
FT   TOPO_DOM    673    683       Cytoplasmic (Potential).
FT   REGION      486    523       BOTA-binding (By similarity).
FT   MOD_RES     423    423       Phosphotyrosine.
FT   CARBOHYD    441    441       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    491    491       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    516    516       N-linked (GlcNAc...) (Potential).
FT   CONFLICT     18     18       G -> D (in Ref. 3; AAG28491).
SQ   SEQUENCE   683 AA;  77457 MW;  CBDC19B281B9E4F3 CRC64;
     MDDYRYRDNY EGYAPSDGYY RSNEQNQEED AQSDVTEGHD EEDEIYEGEY QGIPHPDDVK
     SKQTKMAPSR ADGLGGQADL MAERMEDEEE LAHQYETIID ECGHGRFQWT LFFVLGLALM
     ADGVEIFVVS FALPSAEKDM CLSSSKKGML GLIVYLGMMA GAFILGGLAD KLGRKKVLSM
     SLAINASFAS LSSFVQGYGA FLFCRLISGI GIGGSLPIVF AYFSEFLSRE KRGEHLSWLG
     IFWMTGGIYA SAMAWSIIPH YGWGFSMGTN YHFHSWRVFV IVCALPATVS MVALKFMPES
     PRFLLEMGKH DEAWMILKQV HDTNMRAKGT PEKVFTVSHI KTPKQMDEFI EIQSSTGTWY
     QRWLVRFMTI FKQVWDNALY CVMGPYRMNT LILAVVWFTM ALSYYGLTVW FPDMIRYFQD
     EEYKSKMKVF FGEHVHGATI NFTMENQIHQ HGKLVNDKFI KMYFKHVLFE DTFFDKCYFE
     DVTSTDTYFK NCTIESTTFY NTDLYKHKFI NCRFINSTFL EQKEGCHMDF EEDNDFLIYL
     VSFLGSLSVL PGNIISALLM DRIGRLKMIG GSMLISAVCC FFLFFGNSES AMIGWQCLFC
     GTSIAAWNAL DVITVELYPT NQRATAFGIL NGLCKFGAIL GNTIFASFVG ITKVVPILLA
     AASLVGGGLI ALRLPETREQ VLM
//
ID   TM169_MOUSE             Reviewed;         297 AA.
AC   Q8BG50;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Transmembrane protein 169;
GN   Name=Tmem169;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
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CC   -----------------------------------------------------------------------
DR   EMBL; AK034935; BAC28886.1; -; mRNA.
DR   EMBL; AK043681; BAC31618.1; -; mRNA.
DR   EMBL; BC116730; AAI16731.1; -; mRNA.
DR   EMBL; BC117087; AAI17088.1; -; mRNA.
DR   IPI; IPI00221472; -.
DR   RefSeq; NP_780773.1; NM_175564.4.
DR   UniGene; Mm.80318; -.
DR   PRIDE; Q8BG50; -.
DR   Ensembl; ENSMUST00000027380; ENSMUSP00000027380; ENSMUSG00000026188.
DR   GeneID; 271711; -.
DR   KEGG; mmu:271711; -.
DR   UCSC; uc007bkk.1; mouse.
DR   CTD; 271711; -.
DR   MGI; MGI:2442781; Tmem169.
DR   eggNOG; roNOG09123; -.
DR   GeneTree; ENSGT00390000015276; -.
DR   HOGENOM; HBG403118; -.
DR   HOVERGEN; HBG062102; -.
DR   InParanoid; Q8BG50; -.
DR   OMA; VVLWTLV; -.
DR   OrthoDB; EOG4NP743; -.
DR   PhylomeDB; Q8BG50; -.
DR   NextBio; 393493; -.
DR   ArrayExpress; Q8BG50; -.
DR   Bgee; Q8BG50; -.
DR   CleanEx; MM_TMEM169; -.
DR   Genevestigator; Q8BG50; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    297       Transmembrane protein 169.
FT                                /FTId=PRO_0000271040.
FT   TOPO_DOM      1    159       Extracellular (Potential).
FT   TRANSMEM    160    180       Helical; (Potential).
FT   TOPO_DOM    181    210       Cytoplasmic (Potential).
FT   TRANSMEM    211    231       Helical; (Potential).
FT   TOPO_DOM    232    297       Extracellular (Potential).
SQ   SEQUENCE   297 AA;  33424 MW;  C758198DB0AB34A7 CRC64;
     MEESAPVESQ GQLPSPHHGS LRRAVAAVLA LDGESTLGRR KKRRKDSRPE SIIIYRSDNE
     KTDEEPEESE GGDRPKEEEG EDFLDYPGDD GVWNMPLDSR YVTLTGTITR GKKKGQMVDI
     HVTLTEKELQ ELTKPKELSR EAAPEGRRAC QVGADQGPHV VLWTLVCLPV VFVLSFVVSF
     YYGTITWYNI FLVYNEERTF WHKISCCPCL ILFYPVLIMT MASSLGLYAA VAQLSWSWAA
     WWRAACDMEK GFCGWLCSKL GLEDCSPYSI VELLESDNIS GNLSNKDPIQ EVETSTV
//
ID   EFR3A_MOUSE             Reviewed;         819 AA.
AC   Q8BG67; Q6ZQI4; Q8BXQ7; Q8C0Q0; Q922I2;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Protein EFR3 homolog A;
DE   AltName: Full=Protein EFR3-like;
GN   Name=Efr3a; Synonyms=Kiaa0143;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15363888; DOI=10.1016/j.molbrainres.2004.06.022;
RA   Munemoto Y., Houtani T., Kase M., Sakuma S., Baba K., Yamashita T.,
RA   Sugimoto T.;
RT   "Mouse homolog of KIAA0143 protein: hearing deficit induces specific
RT   changes of expression in auditory brainstem neurons.";
RL   Brain Res. Mol. Brain Res. 128:131-140(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain cortex, Olfactory bulb, Retina, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-692, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SUBCELLULAR LOCATION: Cell membrane. Note=Localizes to plasma
CC       membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BG67-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BG67-2; Sequence=VSP_022219;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in neurons of the superior olivary
CC       complex of the auditory brainstem. Also expressed at lower levels
CC       in the cochlear nucleus, the lateral leminiscal nuclei and the
CC       inferior collicus.
CC   -!- INDUCTION: Expression is reduced in animals with impaired hearing.
CC   -!- SIMILARITY: Belongs to the EFR3 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97875.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AB158474; BAD52086.1; -; mRNA.
DR   EMBL; AK129065; BAC97875.1; ALT_INIT; mRNA.
DR   EMBL; AK030074; BAC26768.1; -; mRNA.
DR   EMBL; AK032461; BAC27881.1; -; mRNA.
DR   EMBL; AK044000; BAC31732.1; -; mRNA.
DR   EMBL; AK044475; BAC31942.1; -; mRNA.
DR   EMBL; AK161250; BAE36269.1; -; mRNA.
DR   EMBL; BC007482; AAH07482.1; -; mRNA.
DR   IPI; IPI00453863; -.
DR   IPI; IPI00551399; -.
DR   RefSeq; NP_598527.2; NM_133766.3.
DR   UniGene; Mm.260647; -.
DR   ProteinModelPortal; Q8BG67; -.
DR   PRIDE; Q8BG67; -.
DR   Ensembl; ENSMUST00000015146; ENSMUSP00000015146; ENSMUSG00000015002.
DR   Ensembl; ENSMUST00000067248; ENSMUSP00000065622; ENSMUSG00000015002.
DR   GeneID; 76740; -.
DR   KEGG; mmu:76740; -.
DR   UCSC; uc007vzu.1; mouse.
DR   CTD; 76740; -.
DR   MGI; MGI:1923990; Efr3a.
DR   GeneTree; ENSGT00390000002143; -.
DR   HOVERGEN; HBG060233; -.
DR   OrthoDB; EOG4MCWZR; -.
DR   NextBio; 345723; -.
DR   ArrayExpress; Q8BG67; -.
DR   Bgee; Q8BG67; -.
DR   CleanEx; MM_EFR3A; -.
DR   Genevestigator; Q8BG67; -.
DR   GO; GO:0005622; C:intracellular; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 2.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Membrane; Phosphoprotein.
FT   CHAIN         1    819       Protein EFR3 homolog A.
FT                                /FTId=PRO_0000270766.
FT   MOD_RES     420    420       Phosphoserine (By similarity).
FT   MOD_RES     692    692       Phosphoserine.
FT   VAR_SEQ     786    819       PPPSPSGTLTVTSGHTQYQSVPVYEMKFPDLCVY -> QRR
FT                                ESMLYKTEAEPCYTQPMAWGQRRIKEKYKAVVK (in
FT                                isoform 2).
FT                                /FTId=VSP_022219.
FT   CONFLICT     70     70       R -> H (in Ref. 3; BAC31942).
FT   CONFLICT    364    364       V -> I (in Ref. 4; AAH07482).
FT   CONFLICT    585    585       D -> G (in Ref. 3; BAC31942).
FT   CONFLICT    693    693       R -> T (in Ref. 3; BAC26768).
SQ   SEQUENCE   819 AA;  92613 MW;  BF3BCD87C508CD1A CRC64;
     MPTRVCCCCS ALRPRYKRLV DNIFPEDPKD GLVKADMEKL TFYAVSAPEK LDRIGAYLAE
     RLSRDVVRHR SGYVLIAMEA LDQLLMACHS QSIKPFVESF LHMVAKLLES GEPKLQVLGT
     NSFVKFANIE EDTPSYHRRY DFFVSRFSAM CHSCHSDPEI RTEIRIAGIR GIQGVVRKTV
     NDELRATIWE PQHMDKIVPS LLFNMQKIEE VDSRLGPPSS PSAADKEENP AVLAESCFRE
     LLGRATFGNM NNAVRPVFAH LDHHKLWDPN EFAVHCFKII MYSIQAQYSH HVIQEILGHL
     DARRKDSPRV RAGIIQVLLE AVAIAAKGSI GPTVLEVFNT LLKHLRLSVE LEANDSQKGS
     VGSVTVSSKD NDEKIVQNAV IQTIGFFGSN LPDYQRSEIM MFIMGKVPVF GTSTHTLDIS
     QLGDLGTRRI QIMLLRSLLM VTSGYKAKTI VTALPGSFLD PLLSPSLMED YELRQLVLEV
     MHNLMDRHDN RAKLRGIRII PDVADLKIKR EKICRQDTSF MKKNGQQLYR HIYLGCKEED
     NVQKNYELLY TSLALITIEL ANEEVVIDLI RLAIALQDSA IINEDNLSMF HRCGIMALVA
     AYLNFVSQMI AVPAFCQHVS KVIETRTMEA PYFLPEHIFR DKCMLPKSLE KHDKNLYFLT
     NKIAESLGGS GYSVERLTVP YVPQVTDEDR LSRRKSIVDT VSIQVDILSN SVPSDDVVSN
     TEEITFEALK KAIDTNGMEE QEKEKRRLVI EKFQKAPFEE IAAQCESKAN LLHDRLAQIL
     ELTIRPPPSP SGTLTVTSGH TQYQSVPVYE MKFPDLCVY
//
ID   SH3L2_MOUSE             Reviewed;         107 AA.
AC   Q8BG73; Q3TV64;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 57.
DE   RecName: Full=SH3 domain-binding glutamic acid-rich-like protein 2;
GN   Name=Sh3bgrl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Placenta, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 58-86, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the SH3BGR family.
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CC   -----------------------------------------------------------------------
DR   EMBL; BC038473; AAH38473.1; -; mRNA.
DR   EMBL; AK076202; BAC36251.1; -; mRNA.
DR   EMBL; AK160357; BAE35756.1; -; mRNA.
DR   IPI; IPI00874453; -.
DR   RefSeq; NP_766095.1; NM_172507.5.
DR   UniGene; Mm.479969; -.
DR   ProteinModelPortal; Q8BG73; -.
DR   SMR; Q8BG73; 1-103.
DR   PRIDE; Q8BG73; -.
DR   Ensembl; ENSMUST00000113215; ENSMUSP00000108841; ENSMUSG00000032261.
DR   GeneID; 212531; -.
DR   KEGG; mmu:212531; -.
DR   UCSC; uc009qwl.1; mouse.
DR   CTD; 212531; -.
DR   MGI; MGI:1915350; Sh3bgrl2.
DR   eggNOG; roNOG17179; -.
DR   GeneTree; ENSGT00440000039098; -.
DR   HOVERGEN; HBG054781; -.
DR   NextBio; 373620; -.
DR   ArrayExpress; Q8BG73; -.
DR   Bgee; Q8BG73; -.
DR   Genevestigator; Q8BG73; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   InterPro; IPR006993; Glut_rich_SH3-bd.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   PANTHER; PTHR12232; Glut_rich_SH3_bd; 1.
DR   Pfam; PF04908; SH3BGR; 1.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Nucleus; SH3-binding.
FT   CHAIN         1    107       SH3 domain-binding glutamic acid-rich-
FT                                like protein 2.
FT                                /FTId=PRO_0000220748.
FT   MOTIF        61     67       SH3-binding (Potential).
SQ   SEQUENCE   107 AA;  12255 MW;  BADE6662937029EF CRC64;
     MVVRVFVASC SGFVAIKKKQ QDVVRFLEAN KIEFEEVDIT MSEEQRQWMY KNIPPEKKPA
     QGNPLPPQIF NGDRYCGDYD SFFESKESNT VFSFLGLKPR PASTAEP
//
ID   TM198_MOUSE             Reviewed;         360 AA.
AC   Q8BG75;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Transmembrane protein 198;
GN   Name=Tmem198;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Hypothalamus, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the TMEM198 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC059868; AAH59868.1; -; mRNA.
DR   EMBL; AK038957; BAC30183.1; -; mRNA.
DR   EMBL; AK082334; BAC38470.1; -; mRNA.
DR   EMBL; AK158863; BAE34699.1; -; mRNA.
DR   IPI; IPI00221504; -.
DR   RefSeq; NP_796030.1; NM_177056.4.
DR   UniGene; Mm.44401; -.
DR   PhosphoSite; Q8BG75; -.
DR   PRIDE; Q8BG75; -.
DR   Ensembl; ENSMUST00000050899; ENSMUSP00000057865; ENSMUSG00000051703.
DR   Ensembl; ENSMUST00000113575; ENSMUSP00000109205; ENSMUSG00000051703.
DR   GeneID; 319998; -.
DR   KEGG; mmu:319998; -.
DR   UCSC; uc007bpl.1; mouse.
DR   CTD; 319998; -.
DR   MGI; MGI:2443133; Tmem198.
DR   eggNOG; roNOG17105; -.
DR   GeneTree; ENSGT00390000016940; -.
DR   HOGENOM; HBG713281; -.
DR   HOVERGEN; HBG060418; -.
DR   InParanoid; Q8BG75; -.
DR   OMA; RDSHTEV; -.
DR   OrthoDB; EOG4GTKDG; -.
DR   NextBio; 395823; -.
DR   ArrayExpress; Q8BG75; -.
DR   Bgee; Q8BG75; -.
DR   CleanEx; MM_TMEM198; -.
DR   Genevestigator; Q8BG75; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    360       Transmembrane protein 198.
FT                                /FTId=PRO_0000326031.
FT   TRANSMEM     36     56       Helical; (Potential).
FT   TRANSMEM     59     79       Helical; (Potential).
FT   TRANSMEM     93    113       Helical; (Potential).
FT   TRANSMEM    116    136       Helical; (Potential).
FT   TRANSMEM    145    165       Helical; (Potential).
FT   TRANSMEM    177    197       Helical; (Potential).
FT   TRANSMEM    218    238       Helical; (Potential).
FT   COMPBIAS     64    233       Leu-rich.
FT   COMPBIAS    252    301       Arg-rich.
SQ   SEQUENCE   360 AA;  39752 MW;  BAA607299E462B8C CRC64;
     MPGTMETLRF QLLPPEPDDT FWGAPCEQPL ERRYQALPAL VCIMCCLFGV VYCFFGYRCF
     KAVLFLTGLL FGSVVIFLLC YRERVLETQL SAGASAGIAL GIGLLCGLVA MLVRSVGLFL
     VGLLLGLLLA AAALLGSAPY YQPGSVWGPL GLLLGGGLLC ALLTLRWPRP LTTLATAVTG
     AALIATAADY FAELLLLGRY VVERLRAAPV PPLCWRSWAL LALWPLLSLM GVLVQWRVTT
     ERDSHTEVVI SRQRRRVQLM RIRQQEERKE KRRKKRPPRA PPRGPRAPPR PGPPDPAYRR
     RPVPIKRFNG DVLSPSYIQS FRDRQTGSSL SSFMASPTDT DYEYGSRGPL TACSGPPVRV
//
ID   CLVS2_MOUSE             Reviewed;         327 AA.
AC   Q8BG92; Q8BKA5;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Clavesin-2;
DE   AltName: Full=Retinaldehyde-binding protein 1-like 2;
GN   Name=Clvs2; Synonyms=Rlbp1l2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain cortex, Eye, Hippocampus, Spinal cord, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Required for normal morphology of late endosomes and/or
CC       lysosomes in neurons. Binds phosphatidylinositol 3,5-bisphosphate
CC       (PtdIns(3,5)P2) (By similarity).
CC   -!- SUBUNIT: Forms a complex with clathrin heavy chain and gamma-
CC       adaptin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC       membrane; Peripheral membrane protein (By similarity). Early
CC       endosome membrane; Peripheral membrane protein (By similarity).
CC       Cytoplasmic vesicle, clathrin-coated vesicle (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BG92-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BG92-2; Sequence=VSP_027326, VSP_027327;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The CRAL-TRIO domain is required for targeting to the
CC       membrane and for binding PtdIns(3,5)P2 (By similarity).
CC   -!- MISCELLANEOUS: Binding to PtdIns(3,5)P2 is not required for
CC       localization (By similarity).
CC   -!- SIMILARITY: Contains 1 CRAL-TRIO domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK039308; BAC30312.1; -; mRNA.
DR   EMBL; AK049896; BAC33976.1; -; mRNA.
DR   EMBL; AK053797; BAC35529.1; -; mRNA.
DR   EMBL; AK139409; BAE23998.1; -; mRNA.
DR   EMBL; AK169009; BAE40806.1; -; mRNA.
DR   EMBL; BC058539; AAH58539.1; -; mRNA.
DR   IPI; IPI00221527; -.
DR   IPI; IPI00457674; -.
DR   RefSeq; NP_780657.1; NM_175448.3.
DR   UniGene; Mm.417656; -.
DR   UniGene; Mm.94461; -.
DR   HSSP; P49638; 1R5L.
DR   ProteinModelPortal; Q8BG92; -.
DR   SMR; Q8BG92; 3-265.
DR   PRIDE; Q8BG92; -.
DR   Ensembl; ENSMUST00000019920; ENSMUSP00000019920; ENSMUSG00000019785.
DR   GeneID; 215890; -.
DR   KEGG; mmu:215890; -.
DR   UCSC; uc007eue.1; mouse.
DR   CTD; 215890; -.
DR   MGI; MGI:2443223; Clvs2.
DR   eggNOG; roNOG06341; -.
DR   GeneTree; ENSGT00550000074253; -.
DR   HOGENOM; HBG716080; -.
DR   HOVERGEN; HBG101105; -.
DR   InParanoid; Q8BG92; -.
DR   OMA; NHFEAFR; -.
DR   OrthoDB; EOG4RXZ0J; -.
DR   PhylomeDB; Q8BG92; -.
DR   NextBio; 374892; -.
DR   ArrayExpress; Q8BG92; -.
DR   Bgee; Q8BG92; -.
DR   CleanEx; MM_RLBP1L2; -.
DR   Genevestigator; Q8BG92; -.
DR   GO; GO:0030136; C:clathrin-coated vesicle; ISS:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISS:UniProtKB.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   GO; GO:0007040; P:lysosome organization; ISS:UniProtKB.
DR   InterPro; IPR001071; CRAL-bd_toc_tran.
DR   InterPro; IPR001251; CRAL-bd_TRIO_C.
DR   InterPro; IPR008273; CRAL-bd_TRIO_N.
DR   InterPro; IPR011074; Sec14p-like_N.
DR   Gene3D; G3DSA:3.40.525.10; CRAL_bd_TRIO_C; 1.
DR   Pfam; PF00650; CRAL_TRIO; 1.
DR   Pfam; PF03765; CRAL_TRIO_N; 1.
DR   PRINTS; PR00180; CRETINALDHBP.
DR   SMART; SM00516; SEC14; 1.
DR   SUPFAM; SSF52087; CRAL_TRIO_C; 1.
DR   SUPFAM; SSF46938; Sec14p_like_N; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasmic vesicle; Endosome; Golgi apparatus;
KW   Lipid-binding; Membrane.
FT   CHAIN         1    327       Clavesin-2.
FT                                /FTId=PRO_0000297653.
FT   DOMAIN       96    257       CRAL-TRIO.
FT   VAR_SEQ     189    227       DSFPARFGGIHFVNQPWYIHALYTVIRPFLKEKTRKRIF
FT                                -> VRVHHCYCFFVSCMVLALFVMYWVSYEIVKTPNQKFID
FT                                F (in isoform 2).
FT                                /FTId=VSP_027326.
FT   VAR_SEQ     228    327       Missing (in isoform 2).
FT                                /FTId=VSP_027327.
SQ   SEQUENCE   327 AA;  37954 MW;  B3F9F8D35E025B77 CRC64;
     MTHLQAGLSP ETLEKARLEL NENPDTLHQD IQEVRDMVIT RPDIGFLRTD DAFILRFLRA
     RKFHHFEAFR LLAQYFEYRQ QNLDMFKSFK ATDPGIKQAL KDGFPGGLAN LDHYGRKILV
     LFAANWDQSR YTLVDILRAI LLSLEAMIED PELQVNGFVL IIDWSNFTFK QASKLTPNML
     RLAIEGLQDS FPARFGGIHF VNQPWYIHAL YTVIRPFLKE KTRKRIFLHG NNLNSLHQLI
     HPEILPSEFG GMLPPYDMGT WARTLLDHEY DDDSEYNVDS YNMPVKDVDK ELSPKSMKRS
     QSVVDPTALK RMDKSEEENM QPLLALD
//
ID   MYPT2_MOUSE             Reviewed;         976 AA.
AC   Q8BG95; Q8BXY7; Q9D8S6;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 12B;
DE   AltName: Full=Myosin phosphatase-targeting subunit 2;
DE            Short=Myosin phosphatase target subunit 2;
GN   Name=Ppp1r12b; Synonyms=Mypt2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-484 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain, Cerebellum, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-502, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Regulates myosin phosphatase activity. Augments Ca(2+)
CC       sensitivity of the contractile apparatus (By similarity).
CC   -!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or
CC       PPP1CC, and one or several targeting or regulatory subunits.
CC       PPP1R12B mediates binding to myosin. Isoform 3 and isoform 4 bind
CC       PPP1R12A, but not isoform 1 of PPP1R12B itself. Binds IL16 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=Along
CC       actomyosin filaments and stress fibers (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BG95-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BG95-2; Sequence=VSP_009260, VSP_009261;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 5 ANK repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK007727; BAB25216.1; -; mRNA.
DR   EMBL; AK042847; BAC31381.1; -; mRNA.
DR   EMBL; AK046012; BAC32572.1; -; mRNA.
DR   EMBL; AK046167; BAC32618.1; -; mRNA.
DR   EMBL; AK080855; BAC38046.1; -; mRNA.
DR   EMBL; AC117827; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC131591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00111941; -.
DR   IPI; IPI00876214; -.
DR   UniGene; Mm.188709; -.
DR   UniGene; Mm.451578; -.
DR   ProteinModelPortal; Q8BG95; -.
DR   SMR; Q8BG95; 11-308.
DR   STRING; Q8BG95; -.
DR   PhosphoSite; Q8BG95; -.
DR   PRIDE; Q8BG95; -.
DR   Ensembl; ENSMUST00000045665; ENSMUSP00000047463; ENSMUSG00000073557.
DR   Ensembl; ENSMUST00000112166; ENSMUSP00000107790; ENSMUSG00000073557.
DR   UCSC; uc007csn.1; mouse.
DR   MGI; MGI:1916417; Ppp1r12b.
DR   eggNOG; roNOG09895; -.
DR   GeneTree; ENSGT00600000084108; -.
DR   HOVERGEN; HBG052561; -.
DR   OrthoDB; EOG4XD3QD; -.
DR   ArrayExpress; Q8BG95; -.
DR   Bgee; Q8BG95; -.
DR   Genevestigator; Q8BG95; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR017401; Pase-1_reg_su_12A/B/C_euk.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 3.
DR   PIRSF; PIRSF038141; PP1_12ABC_vert; 1.
DR   SMART; SM00248; ANK; 5.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; ANK repeat; Cytoplasm; Phosphoprotein; Repeat.
FT   CHAIN         1    976       Protein phosphatase 1 regulatory subunit
FT                                12B.
FT                                /FTId=PRO_0000067029.
FT   REPEAT       57     86       ANK 1.
FT   REPEAT       90    119       ANK 2.
FT   REPEAT      123    152       ANK 3.
FT   REPEAT      216    245       ANK 4.
FT   REPEAT      249    278       ANK 5.
FT   COMPBIAS    336    379       Glu-rich.
FT   MOD_RES     502    502       Phosphoserine.
FT   MOD_RES     833    833       Phosphoserine.
FT   MOD_RES     941    941       Phosphoserine (By similarity).
FT   VAR_SEQ      98    105       ACIDENLD -> RNHKPRGS (in isoform 2).
FT                                /FTId=VSP_009260.
FT   VAR_SEQ     106    976       Missing (in isoform 2).
FT                                /FTId=VSP_009261.
SQ   SEQUENCE   976 AA;  109049 MW;  7694AC50766A8890 CRC64;
     MAELEHLGGK RAESARARRA EQLRRWRGSL TEQEPAERQG AGRQLQTRRG SPRVRFEDGA
     VFLAACSSGD TDEVKKLLAR GADINTVNVD GLTALHQACI DENLDMVKFL VENRANVNQQ
     DNEGWTPLHA AASCGYLNIA EYFISHGASV GIVNSEGEVP SDLAEEPAMK DLLLEQVKKQ
     GVDLEQSRKE EEQQMLQDAR QWLNSGRIED VRQARSGATA LHVAAAKGYS EVLRLLIQAG
     YELNVQDHDG WTPLHAAAHW GVKEACSILA EALCDMDIRN KLGQTPFDVA DEGLVEHLEM
     LQKKQDVLRS EKETRNKLIE SDLNSKFQSG LFKNKEKMLY EEEIPKSQDT EEENKESSSS
     SSEEEEGEDE VSESETEKEA DKKPEATVNH SNSEIKSRIM EQIPAPAQNT FSASSARRLS
     SLFNKAEEPK DESPSSWRLG LRKTGSHNML SEVANSREAL RDRGSSIYRS SSSPRISALL
     DDKDKERENK SYFSMLVPRR LSSTSDIEEK ENRESAVNLV RSGSHTRQLW RDEAKGSETP
     QTIAPSTYTS TYLKRTPYKS QADSTAEKTA DSVSSSTPLC VITNRPAPST ANGVPAATVF
     SSAGTDPSVE AREKRRSYLT PVRDEEAESL RKARSRQARQ TRRSTQGVTL TDLQEAEKTF
     SRSRAERQAQ EQPGEKLEDP GGLEGSTKKQ EPSAAPTKGA GEGRSLEEEP IYHRLRYPTQ
     PDKPTTPVSP SASRPSLYTG SHLLRTSRAS GPDSENSETS THATAAKEMD TSEKGEADLD
     DQSSNRLSVR ERRRAKDRRR GTGINFWTND EDETDVSEEV KEALHERLSR LESGGTNPTS
     SDSYSDRASA RARREAREAR LASLTSRVEE DSNRDYKKLY ESALTENQKL KTKLQEAQLE
     LADIKAKLEK MAQQKQEKTS DRSSVLEVEK RERRALERKM SEMEEEMKVL TELKSDNQRL
     KDENGALIRV ISKLSK
//
ID   IF4B_MOUSE              Reviewed;         611 AA.
AC   Q8BGD9; Q3TD64;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Eukaryotic translation initiation factor 4B;
DE            Short=eIF-4B;
GN   Name=Eif4b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93 AND SER-597, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Required for the binding of mRNA to ribosomes. Functions
CC       in close association with EIF4-F and EIF4-A. Binds near the 5'-
CC       terminal cap of mRNA in presence of EIF-4F and ATP. Promotes the
CC       ATPase activity and the ATP-dependent RNA unwinding activity of
CC       both EIF4-A and EIF4-F (By similarity).
CC   -!- SUBUNIT: Self-associates and interacts with EIF3 p170 subunit (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK045250; BAC32280.1; -; mRNA.
DR   EMBL; AK077423; BAC36793.1; -; mRNA.
DR   EMBL; AK170354; BAE41740.1; -; mRNA.
DR   IPI; IPI00221581; -.
DR   RefSeq; NP_663600.2; NM_145625.3.
DR   UniGene; Mm.290022; -.
DR   UniGene; Mm.391795; -.
DR   ProteinModelPortal; Q8BGD9; -.
DR   SMR; Q8BGD9; 96-176.
DR   MINT; MINT-1954873; -.
DR   STRING; Q8BGD9; -.
DR   PhosphoSite; Q8BGD9; -.
DR   PRIDE; Q8BGD9; -.
DR   Ensembl; ENSMUST00000078635; ENSMUSP00000077705; ENSMUSG00000058655.
DR   GeneID; 75705; -.
DR   KEGG; mmu:75705; -.
DR   UCSC; uc007xuk.1; mouse.
DR   CTD; 75705; -.
DR   MGI; MGI:95304; Eif4b.
DR   eggNOG; roNOG07011; -.
DR   HOGENOM; HBG505466; -.
DR   HOVERGEN; HBG006129; -.
DR   InParanoid; Q8BGD9; -.
DR   OMA; VPKGQSG; -.
DR   OrthoDB; EOG4SQWWX; -.
DR   PhylomeDB; Q8BGD9; -.
DR   NextBio; 343748; -.
DR   ArrayExpress; Q8BGD9; -.
DR   Bgee; Q8BGD9; -.
DR   CleanEx; MM_EIF4B; -.
DR   Genevestigator; Q8BGD9; -.
DR   GermOnline; ENSMUSG00000058655; Mus musculus.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW   RNA-binding.
FT   CHAIN         1    611       Eukaryotic translation initiation factor
FT                                4B.
FT                                /FTId=PRO_0000081617.
FT   DOMAIN       96    173       RRM.
FT   COMPBIAS    164    440       Arg-rich.
FT   COMPBIAS    169    325       Asp-rich.
FT   MOD_RES      16     16       Phosphoserine (By similarity).
FT   MOD_RES      93     93       Phosphoserine.
FT   MOD_RES     192    192       Phosphoserine (By similarity).
FT   MOD_RES     211    211       Phosphotyrosine (By similarity).
FT   MOD_RES     219    219       Phosphoserine (By similarity).
FT   MOD_RES     283    283       Phosphoserine (By similarity).
FT   MOD_RES     406    406       Phosphoserine.
FT   MOD_RES     420    420       Phosphothreonine (By similarity).
FT   MOD_RES     422    422       Phosphoserine (By similarity).
FT   MOD_RES     424    424       Phosphoserine (By similarity).
FT   MOD_RES     425    425       Phosphoserine (By similarity).
FT   MOD_RES     445    445       Phosphoserine.
FT   MOD_RES     459    459       Phosphoserine (By similarity).
FT   MOD_RES     461    461       Phosphothreonine (By similarity).
FT   MOD_RES     462    462       Phosphoserine (By similarity).
FT   MOD_RES     495    495       Phosphoserine (By similarity).
FT   MOD_RES     497    497       Phosphoserine.
FT   MOD_RES     498    498       Phosphoserine.
FT   MOD_RES     500    500       Phosphothreonine (By similarity).
FT   MOD_RES     504    504       Phosphoserine (By similarity).
FT   MOD_RES     586    586       N6-acetyllysine (By similarity).
FT   MOD_RES     597    597       Phosphoserine.
SQ   SEQUENCE   611 AA;  68840 MW;  A3254EBF55EDB6F2 CRC64;
     MAASAKKKNK KGKTISLTDF LAEDGGTGGG STYVPKPVSW ADETDDLEGD VSTTWHSNDD
     DVYRAPPIDR SILPTAPRAA REPNIDRSRL PKSPPYTAFL GNLPYDVTED SIKDFFRGLN
     ISAVRLPREP SNPDRLKGFG YAEFEDLDSL LSALSLNEES LGNRRIRVDV ADQAQDKDRD
     DRSFGRDRNR DSDKTDTDWR ARPTTDSFDD YPPRRGDDSF GDKYRDRYDS DRYRDGYRDG
     YRDGPRRDMD RYGGRDRYDD RGSRDYDRGY DSRIGSGRRA FGSGYRRDDD YRGGGDRYED
     RYDRRDDRSW SSRDDYSRDD YRRDDRGPPQ RPRLNLKPRS APKEDDASAS TSQSSRAASI
     FGGAKPVDTA AREREVEERL QKEQEKLQRQ LDEPKLDRRP RERHPSWRSE ETQERERSRT
     GSESSQTGAS ATSGRNTRRR ESEKSLENET LNKEEDCHSP TSKPPKPDQP LKVMPAPPPK
     ENAWVKRSSN PPARSQSSDT EQPSPTSGGG KVAAVQPPEE GPSRKDGNKV DVVGATQGQA
     GSCSRGPGDG GSRDHWKDLD RKDGKKDQDS RSAPEPKKPE ENPASKFSSA SKYAALSVDG
     EDEDEGDDCT E
//
ID   ATG4B_MOUSE             Reviewed;         393 AA.
AC   Q8BGE6; Q6ZQ22; Q8R098;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Cysteine protease ATG4B;
DE            EC=3.4.22.-;
DE   AltName: Full=AUT-like 1 cysteine endopeptidase;
DE   AltName: Full=Autophagin-1;
DE   AltName: Full=Autophagy-related cysteine endopeptidase 1;
DE   AltName: Full=Autophagy-related protein 4 homolog B;
GN   Name=Atg4b; Synonyms=Apg4b, Autl1, Kiaa0943;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   PubMed=12446702; DOI=10.1074/jbc.M208247200;
RA   Marino G., Uria J.A., Puente X.S., Quesada V., Bordallo J.,
RA   Lopez-Otin C.;
RT   "Human autophagins, a family of cysteine proteinases potentially
RT   implicated in cell degradation by autophagy.";
RL   J. Biol. Chem. 278:3671-3678(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pancreas, Skin, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 128-393.
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Cysteine protease required for autophagy, which cleaves
CC       the C-terminal part of either MAP1LC3, GABARAPL2 or GABARAP,
CC       allowing the liberation of form I. A subpopulation of form I is
CC       subsequently converted to a smaller form (form II). Form II, with
CC       a revealed C-terminal glycine, is considered to be the
CC       phosphatidylethanolamine (PE)-conjugated form, and has the
CC       capacity for the binding to autophagosomes.
CC   -!- ENZYME REGULATION: Inhibited by N-ethylmaleimide (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the peptidase C54 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AJ504653; CAD43220.1; -; mRNA.
DR   EMBL; AK028712; BAC26079.1; -; mRNA.
DR   EMBL; AK031570; BAC27455.1; -; mRNA.
DR   EMBL; AK075796; BAC35965.1; -; mRNA.
DR   EMBL; AK088811; BAC40587.1; -; mRNA.
DR   EMBL; BC027184; AAH27184.1; -; mRNA.
DR   EMBL; AK129242; BAC98052.1; -; mRNA.
DR   IPI; IPI00387185; -.
DR   RefSeq; NP_777363.1; NM_174874.3.
DR   UniGene; Mm.29087; -.
DR   ProteinModelPortal; Q8BGE6; -.
DR   SMR; Q8BGE6; 10-373.
DR   STRING; Q8BGE6; -.
DR   MEROPS; C54.003; -.
DR   PhosphoSite; Q8BGE6; -.
DR   PRIDE; Q8BGE6; -.
DR   Ensembl; ENSMUST00000027502; ENSMUSP00000027502; ENSMUSG00000026280.
DR   GeneID; 66615; -.
DR   KEGG; mmu:66615; -.
DR   UCSC; uc007cej.1; mouse.
DR   CTD; 66615; -.
DR   MGI; MGI:1913865; Atg4b.
DR   GeneTree; ENSGT00530000063000; -.
DR   HOGENOM; HBG403051; -.
DR   HOVERGEN; HBG050536; -.
DR   InParanoid; Q8BGE6; -.
DR   OrthoDB; EOG4JWVDK; -.
DR   PhylomeDB; Q8BGE6; -.
DR   ArrayExpress; Q8BGE6; -.
DR   Bgee; Q8BGE6; -.
DR   CleanEx; MM_ATG4B; -.
DR   Genevestigator; Q8BGE6; -.
DR   GermOnline; ENSMUSG00000026280; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR005078; Peptidase_C54.
DR   PANTHER; PTHR22624; Peptidase_C54; 1.
DR   Pfam; PF03416; Peptidase_C54; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Autophagy; Cytoplasm; Hydrolase; Phosphoprotein;
KW   Protease; Protein transport; Thiol protease; Transport;
KW   Ubl conjugation pathway.
FT   CHAIN         1    393       Cysteine protease ATG4B.
FT                                /FTId=PRO_0000215845.
FT   ACT_SITE     74     74       Nucleophile (By similarity).
FT   ACT_SITE    278    278       Potential.
FT   ACT_SITE    280    280       By similarity.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      34     34       Phosphoserine.
FT   MOD_RES     316    316       Phosphoserine (By similarity).
FT   MOD_RES     383    383       Phosphoserine.
FT   MOD_RES     392    392       Phosphoserine (By similarity).
FT   CONFLICT    128    153       IAQMGVGEGKSIGQWYGPNTVAQVLK -> NCLNCHCCGVM
FT                                LMLYKAHGSVLAFCR (in Ref. 3).
FT   CONFLICT    190    190       A -> V (in Ref. 1; CAD43220 and 2;
FT                                BAC26079/BAC27455/BAC35965).
FT   CONFLICT    325    325       T -> K (in Ref. 2; BAC40587, 3 and 4).
SQ   SEQUENCE   393 AA;  44375 MW;  EB9BF54B06F79135 CRC64;
     MDAATLTYDT LRFAEFEDFP ETSEPVWILG RKYSIFTEKD EILSDVASRL WFTYRRNFPA
     IGGTGPTSDT GWGCMLRCGQ MIFAQALVCR HLGRDWRWTQ RKRQPDSYFN VLNAFLDRKD
     SYYSIHQIAQ MGVGEGKSIG QWYGPNTVAQ VLKKLAVFDT WSSLAVHIAM DNTVVMEEIR
     RLCRANLPCA GAAALPTDSE RHCNGFPAGA EVTNRPSAWR PLVLLIPLRL GLTDINEAYV
     ETLKHCFMMP QSLGVIGGKP NSAHYFIGYV GEELIYLDPH TTQPAVELTD SCFIPDESFH
     CQHPPSRMGI GELDPSIAVG FFCKTEEDFN DWCQQVKKLS QLGGALPMFE LVEQQPSHLA
     CQDVLNLSLD SSDVERLERF FDSEDEDFEI LSL
//
ID   PAN2_MOUSE              Reviewed;        1200 AA.
AC   Q8BGF7; Q3TZK5; Q68FH6; Q6ZQ63;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=PAB-dependent poly(A)-specific ribonuclease subunit 2;
DE            EC=3.1.13.4;
DE   AltName: Full=Inactive ubiquitin carboxyl-terminal hydrolase 52;
GN   Name=Pan2; Synonyms=Kiaa0710, Usp52;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Embryonic head, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Embryonic brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Functions in cytoplasmic mRNA decay. As part of the Pan
CC       nuclease complex, shortens poly(A) tails of RNA when the poly(A)
CC       stretch is bound by polyadenylate-binding protein (By similarity).
CC   -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage of poly(A) to 5'-AMP.
CC   -!- SUBUNIT: Interacts with PAN3 to form the Pan nuclease complex
CC       which in turn interacts with the polyadenylate-binding protein
CC       through PAN3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Shuttles between nucleus and cytoplasm (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8BGF7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BGF7-2; Sequence=VSP_023752;
CC       Name=3;
CC         IsoId=Q8BGF7-3; Sequence=VSP_023750, VSP_023752;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q8BGF7-4; Sequence=VSP_023751;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. PAN2 subfamily.
CC   -!- SIMILARITY: Contains 1 exonuclease domain.
CC   -!- CAUTION: Has probably no ubiquitin carboxyl terminal hydrolase
CC       activity since it lacks a conserved catalytic Cys at position 524.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98006.2; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK129196; BAC98006.2; ALT_INIT; Transcribed_RNA.
DR   EMBL; AK047887; BAC33183.1; -; mRNA.
DR   EMBL; AK089001; BAC40693.1; -; mRNA.
DR   EMBL; AK157800; BAE34203.1; -; mRNA.
DR   EMBL; BC075686; AAH75686.1; -; mRNA.
DR   EMBL; BC079841; AAH79841.1; -; mRNA.
DR   IPI; IPI00221595; -.
DR   IPI; IPI00830428; -.
DR   IPI; IPI00831588; -.
DR   IPI; IPI00831685; -.
DR   RefSeq; NP_598753.1; NM_133992.2.
DR   UniGene; Mm.244183; -.
DR   ProteinModelPortal; Q8BGF7; -.
DR   SMR; Q8BGF7; 333-358, 972-1156.
DR   STRING; Q8BGF7; -.
DR   MEROPS; C19.978; -.
DR   PhosphoSite; Q8BGF7; -.
DR   PRIDE; Q8BGF7; -.
DR   Ensembl; ENSMUST00000005825; ENSMUSP00000005825; ENSMUSG00000005682.
DR   Ensembl; ENSMUST00000105236; ENSMUSP00000100870; ENSMUSG00000005682.
DR   Ensembl; ENSMUST00000105237; ENSMUSP00000100871; ENSMUSG00000005682.
DR   GeneID; 103135; -.
DR   KEGG; mmu:103135; -.
DR   UCSC; uc007hme.1; mouse.
DR   CTD; 103135; -.
DR   MGI; MGI:1918984; Pan2.
DR   HOGENOM; HBG357383; -.
DR   HOVERGEN; HBG089847; -.
DR   InParanoid; Q8BGF7; -.
DR   OMA; ATFIPLM; -.
DR   OrthoDB; EOG4HQDHH; -.
DR   PhylomeDB; Q8BGF7; -.
DR   BRENDA; 3.1.13.4; 244.
DR   NextBio; 355801; -.
DR   ArrayExpress; Q8BGF7; -.
DR   Bgee; Q8BGF7; -.
DR   Genevestigator; Q8BGF7; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:EC.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR006055; Exonuclease.
DR   InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR   InterPro; IPR001394; Peptidase_C19.
DR   InterPro; IPR012337; RNaseH-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00929; Exonuc_X-T; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00479; EXOIII; 1.
DR   SUPFAM; SSF53098; RNaseH_fold; 1.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS50235; UCH_2_3; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Exonuclease; Hydrolase;
KW   Nonsense-mediated mRNA decay; Nuclease; Nucleus; Phosphoprotein.
FT   CHAIN         1   1200       PAB-dependent poly(A)-specific
FT                                ribonuclease subunit 2.
FT                                /FTId=PRO_0000280522.
FT   DOMAIN      973   1146       Exonuclease.
FT   MOD_RES     784    784       Phosphoserine (By similarity).
FT   MOD_RES    1188   1188       Phosphoserine (By similarity).
FT   VAR_SEQ      95    112       Missing (in isoform 3).
FT                                /FTId=VSP_023750.
FT   VAR_SEQ     687    722       DKTGKNYDFAQVLKRSICLEQNTQAWCDNCEKYQPT -> G
FT                                S (in isoform 4).
FT                                /FTId=VSP_023751.
FT   VAR_SEQ     826    834       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_023752.
FT   CONFLICT    175    175       Q -> L (in Ref. 3; BAE34203).
SQ   SEQUENCE   1200 AA;  135253 MW;  9CE98D3BE9FCE182 CRC64;
     MNFEGLDPGL AEFSPAMHST LDPVLDAHLN PSLLQNVELD PEGVALEALP VQESVHIMEG
     VYSELHSVVA EVGVPVSVSH FDLHEEMLWV GSHGGHATSF FGPALERYSS FQVNGGDDIR
     QIQSLENGIL FLTKNNLKYM ARGGLIIFDY LLDENEDMHS VLLTDNSTLL VGGLQNHVLE
     IDLNTVQETQ KYAVETPGVT IMRQTNRFFF CGHTSGKVSL RDLRSFKVEH EFDAFSGSLS
     DFDVHGNLLA ACGFSSRLTG LACDRFLKVY DLRMMRAITP LQVHVDPAFL RFIPTYTSRL
     AIISQSGQCQ FCEPTGLANP ADIFHVNPVG PLLMTFDVSA SKQALAFGDS EGCVHLWTDS
     PEPSFNPYSR ETEFALPCLV DSLPPLDWSQ DLLPLSLIPV PLTTDALLSD WPAANSAPAP
     RRAPPVDAEI LRTMKKVGFI GYAPNPRTRL RNQIPYRLKE SDHEFDNFSQ VTESPTGREE
     EPLHTVSKKY RKVTIKYSKL GLEDFDFKHY NKTLFAGLEP HIPNAYCNCM IQVLYFLEPV
     RCLIQNHLCQ KEFCLACELG FLFHMLDLSR GDPCQGSNFL RAFRTIPEAS ALGLILADSD
     EASGKGSLAR LIQRWNRFIL TQLHQDMQEL EVPQAYRGAG GSFCSSGDSI IGQLFSCEME
     NCSLCRCGSE TVRASSTLLF TLSYPEDKTG KNYDFAQVLK RSICLEQNTQ AWCDNCEKYQ
     PTIQTRNIRH LPDILVINCE VNSSKEADFW RLQAEVAFKI AVKKYGGEMK SKEFALADRK
     ELRSPEGFLC SSIEELKNVW LPFSIRMKMT KNKGLDVCNW ADEHELSSLG APSQWGPARA
     EEELGVYVYD LMATVVHILD SRTGGSLVAH IKVGETYHQR KEGVTHQQWY LFNDFLIEPI
     DKYEAVQFDM NWKVPAILYY VKRNLNSRYN LNIKNPIEAS VLLAEASLAR KQRKTHTTFI
     PLMLNEMPQV GDLVGLDAEF VTLNEEEAEL RSDGTKSTIK PSQMSVARIT CVRGQGPNEG
     IPFIDDYIST QEQVVDYLTQ YSGIKPGDLD AKISSKHLTT LKSTYLKLRF LIDIGVKFVG
     HGLQKDFRVI NLMVPKDQVL DTVYLFHMPR KRMISLRFLA WYFLDLKIQG ETHDSIEDAR
     TALQLYRKYL ELSKNGTEPE SFHKVLKGLY EKGRKMDWKV PEPESQTSPK NAAVFSVLAL
//
ID   S35D3_MOUSE             Reviewed;         422 AA.
AC   Q8BGF8; Q9CXD4;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Solute carrier family 35 member D3;
DE   AltName: Full=Fringe connection-like protein 1;
GN   Name=Slc35d3; Synonyms=Frcl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Corpus striatum, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=17062724; DOI=10.1182/blood-2006-08-040196;
RA   Chintala S., Tan J., Gautam R., Rusiniak M.E., Guo X., Li W.,
RA   Gahl W.A., Huizing M., Spritz R.A., Hutton S., Novak E.K., Swank R.T.;
RT   "The Slc35d3 gene, encoding an orphan nucleotide sugar transporter,
RT   regulates platelet-dense granules.";
RL   Blood 109:1533-1540(2007).
CC   -!- FUNCTION: May play a role in hemostasis as a regulator of the
CC       biosynthesis of platelet-dense granules.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- TISSUE SPECIFICITY: Expressed in brain.
CC   -!- SIMILARITY: Belongs to the TPT transporter family. SLC35D
CC       subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB31067.1; Type=Frameshift; Positions=264;
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DR   EMBL; AK018094; BAB31067.1; ALT_SEQ; mRNA.
DR   EMBL; AK042761; BAC31356.1; -; mRNA.
DR   EMBL; AK044973; BAC32165.1; -; mRNA.
DR   EMBL; AK047610; BAC33098.1; -; mRNA.
DR   IPI; IPI00221596; -.
DR   RefSeq; NP_083805.1; NM_029529.3.
DR   UniGene; Mm.477281; -.
DR   UniGene; Mm.74324; -.
DR   ProteinModelPortal; Q8BGF8; -.
DR   PRIDE; Q8BGF8; -.
DR   Ensembl; ENSMUST00000059805; ENSMUSP00000060589; ENSMUSG00000050473.
DR   GeneID; 76157; -.
DR   KEGG; mmu:76157; -.
DR   UCSC; uc007enk.1; mouse.
DR   CTD; 76157; -.
DR   MGI; MGI:1923407; Slc35d3.
DR   eggNOG; maNOG06707; -.
DR   GeneTree; ENSGT00390000014204; -.
DR   HOGENOM; HBG713710; -.
DR   HOVERGEN; HBG106477; -.
DR   InParanoid; Q8BGF8; -.
DR   OMA; AVLITTC; -.
DR   OrthoDB; EOG4W6NW8; -.
DR   PhylomeDB; Q8BGF8; -.
DR   NextBio; 344687; -.
DR   ArrayExpress; Q8BGF8; -.
DR   Bgee; Q8BGF8; -.
DR   CleanEx; MM_SLC35D3; -.
DR   Genevestigator; Q8BGF8; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR   InterPro; IPR004853; DUF250.
DR   Pfam; PF03151; TPT; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Sugar transport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    422       Solute carrier family 35 member D3.
FT                                /FTId=PRO_0000307728.
FT   TRANSMEM      9     29       Helical; (Potential).
FT   TRANSMEM     38     58       Helical; (Potential).
FT   TRANSMEM     64     84       Helical; (Potential).
FT   TRANSMEM    103    123       Helical; (Potential).
FT   TRANSMEM    131    151       Helical; (Potential).
FT   TRANSMEM    155    175       Helical; (Potential).
FT   TRANSMEM    187    207       Helical; (Potential).
FT   TRANSMEM    224    244       Helical; (Potential).
FT   TRANSMEM    257    277       Helical; (Potential).
FT   TRANSMEM    280    300       Helical; (Potential).
FT   CONFLICT    383    383       S -> F (in Ref. 1; BAB31067).
SQ   SEQUENCE   422 AA;  44917 MW;  9CACD625C45507D8 CRC64;
     MRQLCRGRVL GISVAIAHGV FSGSLNILLK FLISRYQFSF LTLVQCLTSS TAALSLELLR
     RLGLIAVPPF GLSLARSFAG VAVLSTLQSS LTLWSLRGLS LPMYVVFKRC LPLVTMLIGV
     LVLKNGAPSP GVLAAVLITT CGAALAGAGD LTGDPIGYVT GVLAVLVHAA YLVLIQKASA
     DTEHGPLTAQ YVIAVSATPL LVICSFASTD SIHAWTFPGW KDPAMVSIFV ACILIGCAMN
     FTTLHCTYIN SAVTTSFVGV VKSIATITVG MVAFSDVEPT SLFIAGVVVN TLGSIIYCVA
     KFLETRRQSN YEDLESQAEG EERQPSGDQL PFVMEELPAK SGNSEPESAE GAGDSVQQGG
     QESRGSIRGI SLAARSSRAE GHSDEVGRRS LKDTYLEVWR LVRGTKYMKK DYLMENEALP
     SP
//
ID   REEP1_MOUSE             Reviewed;         201 AA.
AC   Q8BGH4;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Receptor expression-enhancing protein 1;
GN   Name=Reep1; Synonyms=D6Ertd253e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH OLFR992,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15550249; DOI=10.1016/j.cell.2004.11.021;
RA   Saito H., Kubota M., Roberts R.W., Chi Q., Matsunami H.;
RT   "RTP family members induce functional expression of mammalian odorant
RT   receptors.";
RL   Cell 119:679-691(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Diencephalon, Embryo, Lung, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-152, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May enhance the cell surface expression of odorant
CC       receptors.
CC   -!- SUBUNIT: Interacts with OLFR992.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane
CC       protein (By similarity). Note=A small proportion is detected at
CC       the cell surface (PubMed:15550249).
CC   -!- TISSUE SPECIFICITY: Detected in olfactory sensory neurons of the
CC       olfactory epithelium, and in total brain.
CC   -!- SIMILARITY: Belongs to the DP1 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY562229; AAT70674.1; -; mRNA.
DR   EMBL; AK035238; BAC28995.1; -; mRNA.
DR   EMBL; AK045056; BAC32200.1; -; mRNA.
DR   EMBL; AK053158; BAC35288.1; -; mRNA.
DR   EMBL; AK136916; BAE23168.1; -; mRNA.
DR   EMBL; BC046826; AAH46826.1; -; mRNA.
DR   IPI; IPI00404079; -.
DR   RefSeq; NP_848723.1; NM_178608.3.
DR   UniGene; Mm.146332; -.
DR   STRING; Q8BGH4; -.
DR   PhosphoSite; Q8BGH4; -.
DR   PRIDE; Q8BGH4; -.
DR   Ensembl; ENSMUST00000121469; ENSMUSP00000112662; ENSMUSG00000052852.
DR   GeneID; 52250; -.
DR   KEGG; mmu:52250; -.
DR   NMPDR; fig|10090.3.peg.14620; -.
DR   UCSC; uc009chc.1; mouse.
DR   CTD; 52250; -.
DR   MGI; MGI:1098827; Reep1.
DR   eggNOG; roNOG11111; -.
DR   GeneTree; ENSGT00550000074535; -.
DR   HOGENOM; HBG716753; -.
DR   HOVERGEN; HBG056861; -.
DR   InParanoid; Q8BGH4; -.
DR   OrthoDB; EOG4D7Z6W; -.
DR   PhylomeDB; Q8BGH4; -.
DR   NextBio; 308710; -.
DR   ArrayExpress; Q8BGH4; -.
DR   Bgee; Q8BGH4; -.
DR   CleanEx; MM_REEP1; -.
DR   Genevestigator; Q8BGH4; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR004345; TB2_DP1_HVA22.
DR   PANTHER; PTHR12300; TB2_DP1_HVA22; 1.
DR   Pfam; PF03134; TB2_DP1_HVA22; 1.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    201       Receptor expression-enhancing protein 1.
FT                                /FTId=PRO_0000101822.
FT   TRANSMEM      1     21       Helical; (Potential).
FT   TRANSMEM     35     55       Helical; (Potential).
FT   COMPBIAS    170    173       Poly-Pro.
FT   MOD_RES     150    150       Phosphoserine.
FT   MOD_RES     152    152       Phosphoserine.
SQ   SEQUENCE   201 AA;  22285 MW;  99C33D74A71FB6B7 CRC64;
     MVSWIISRLV VLIFGTLYPA YYSYKAVKSK DIKEYVKWMM YWIIFALFTT AETFTDIFLC
     WFPFYYELKI AFVAWLLSPY TKGSSLLYRK FVHPTLSSKE KEIDDCLVQA KDRSYDALVH
     FGKRGLNVAA TAAVMAASKG QGALSERLRS FSMQDLTTIR GDGAPAPSGP PPPGTGRSSG
     KHSQPKMSRS ASESAGSSGT A
//
ID   C42S2_MOUSE             Reviewed;          84 AA.
AC   Q8BGH7; Q3UKN9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=CDC42 small effector protein 2;
GN   Name=Cdc42se2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, DBA/2, and NOD;
RC   TISSUE=Cerebellum, Egg, Lung, Placenta, Spinal cord, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=15840583; DOI=10.1074/jbc.M500128200;
RA   Ching K.H., Kisailus A.E., Burbelo P.D.;
RT   "The role of SPECs, small Cdc42-binding proteins, in F-actin
RT   accumulation at the immunological synapse.";
RL   J. Biol. Chem. 280:23660-23667(2005).
CC   -!- FUNCTION: Probably involved in the organization of the actin
CC       cytoskeleton by acting downstream of CDC42, inducing actin
CC       filament assembly. Alters CDC42-induced cell shape changes. In
CC       activated T-cells, may play a role in CDC42-mediated F-actin
CC       accumulation at the immunological synapse. May play a role in
CC       early contractile events in phagocytosis in macrophages (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with CDC42 (in GTP-bound form). Interacts
CC       weakly with RAC1 and not at all with RHOA (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Cell membrane; Lipid-anchor (By similarity). Cell projection,
CC       phagocytic cup (By similarity). Note=Recruited to the activated
CC       TCR prior actin polymerization (By similarity). Localizes at the
CC       phagocytic cup of macrophages (By similarity).
CC   -!- TISSUE SPECIFICITY: Detected in spleen, thymus and lung (at
CC       protein level).
CC   -!- DOMAIN: The CRIB domain mediates interaction with CDC42 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the CDC42SE/SPEC family.
CC   -!- SIMILARITY: Contains 1 CRIB domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK039301; BAC30311.1; -; mRNA.
DR   EMBL; AK080473; BAC37927.1; -; mRNA.
DR   EMBL; AK088090; BAC40139.1; -; mRNA.
DR   EMBL; AK090381; BAC41193.1; -; mRNA.
DR   EMBL; AK135775; BAE22655.1; -; mRNA.
DR   EMBL; AK145931; BAE26762.1; -; mRNA.
DR   EMBL; AK146313; BAE27068.1; -; mRNA.
DR   EMBL; AK160934; BAE36099.1; -; mRNA.
DR   EMBL; AL607091; CAI35284.1; -; Genomic_DNA.
DR   EMBL; AL954817; CAI35284.1; JOINED; Genomic_DNA.
DR   EMBL; AL954817; CAI26192.1; -; Genomic_DNA.
DR   EMBL; AL607091; CAI26192.1; JOINED; Genomic_DNA.
DR   EMBL; BC048935; AAH48935.1; -; mRNA.
DR   IPI; IPI00221611; -.
DR   RefSeq; NP_848741.1; NM_178626.3.
DR   UniGene; Mm.29476; -.
DR   UniGene; Mm.431861; -.
DR   ProteinModelPortal; Q8BGH7; -.
DR   STRING; Q8BGH7; -.
DR   PRIDE; Q8BGH7; -.
DR   Ensembl; ENSMUST00000064104; ENSMUSP00000070725; ENSMUSG00000052298.
DR   GeneID; 72729; -.
DR   KEGG; mmu:72729; -.
DR   UCSC; uc007iyf.1; mouse.
DR   CTD; 72729; -.
DR   MGI; MGI:1919979; Cdc42se2.
DR   eggNOG; roNOG16977; -.
DR   GeneTree; ENSGT00390000010375; -.
DR   HOGENOM; HBG717437; -.
DR   HOVERGEN; HBG107546; -.
DR   InParanoid; Q8BGH7; -.
DR   OMA; ISANVQM; -.
DR   OrthoDB; EOG4G7C10; -.
DR   PhylomeDB; Q8BGH7; -.
DR   NextBio; 336814; -.
DR   ArrayExpress; Q8BGH7; -.
DR   Bgee; Q8BGH7; -.
DR   Genevestigator; Q8BGH7; -.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005198; F:structural molecule activity; ISS:UniProtKB.
DR   GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0009966; P:regulation of signal transduction; ISS:UniProtKB.
DR   InterPro; IPR000095; PAK_box_Rho-bd.
DR   Pfam; PF00786; PBD; 1.
DR   PROSITE; PS50108; CRIB; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell projection; Cell shape; Cytoplasm; Cytoskeleton;
KW   Lipoprotein; Membrane; Palmitate; Phagocytosis.
FT   CHAIN         1     84       CDC42 small effector protein 2.
FT                                /FTId=PRO_0000334640.
FT   DOMAIN       29     42       CRIB.
FT   COMPBIAS     20     23       Poly-Arg.
FT   LIPID        10     10       S-palmitoyl cysteine (By similarity).
FT   LIPID        11     11       S-palmitoyl cysteine (By similarity).
FT   CONFLICT     76     76       M -> T (in Ref. 1; BAE26762).
SQ   SEQUENCE   84 AA;  9223 MW;  98C5E82176DA990A CRC64;
     MSEFWLCFNC CIAEQPQPKR RRRIDRSMIG EPTNFVHTAH VGSGDLFSGM NSVSSIQNQM
     QSKGGYGGGM PANVQMQLVD TKAG
//
ID   S35F1_MOUSE             Reviewed;         408 AA.
AC   Q8BGK5; Q3TNT3; Q8BKD4; Q8BVI2; Q8BX52;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Solute carrier family 35 member F1;
GN   Name=Slc35f1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain cortex, Cerebellum, Embryonic spinal ganglion, Eye,
RC   Hypothalamus, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Putative solute transporter (Potential).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the SLC35F solute transporter family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC37158.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA;
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DR   EMBL; AK038601; BAC30061.1; -; mRNA.
DR   EMBL; AK048957; BAC33499.1; -; mRNA.
DR   EMBL; AK053426; BAC35383.1; -; mRNA.
DR   EMBL; AK053545; BAC35422.1; -; mRNA.
DR   EMBL; AK078169; BAC37158.1; ALT_SEQ; mRNA.
DR   EMBL; AK083768; BAC39016.1; -; mRNA.
DR   EMBL; AK139331; BAE23959.1; -; mRNA.
DR   EMBL; AK165021; BAE38004.1; -; mRNA.
DR   EMBL; BC059075; AAH59075.1; -; mRNA.
DR   IPI; IPI00396670; -.
DR   RefSeq; NP_848790.2; NM_178675.4.
DR   UniGene; Mm.338690; -.
DR   ProteinModelPortal; Q8BGK5; -.
DR   PRIDE; Q8BGK5; -.
DR   Ensembl; ENSMUST00000105473; ENSMUSP00000101113; ENSMUSG00000038602.
DR   GeneID; 215085; -.
DR   KEGG; mmu:215085; -.
DR   UCSC; uc007fbk.1; mouse.
DR   CTD; 215085; -.
DR   MGI; MGI:2139810; Slc35f1.
DR   eggNOG; roNOG06494; -.
DR   GeneTree; ENSGT00390000015655; -.
DR   HOGENOM; HBG445285; -.
DR   HOVERGEN; HBG058983; -.
DR   InParanoid; Q8BGK5; -.
DR   OMA; YVAQDPR; -.
DR   OrthoDB; EOG43BMPS; -.
DR   PhylomeDB; Q8BGK5; -.
DR   NextBio; 374600; -.
DR   ArrayExpress; Q8BGK5; -.
DR   Bgee; Q8BGK5; -.
DR   CleanEx; MM_SLC35F1; -.
DR   Genevestigator; Q8BGK5; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR009262; DUF914_euk.
DR   PANTHER; PTHR14233; DUF914_euk; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    408       Solute carrier family 35 member F1.
FT                                /FTId=PRO_0000307308.
FT   TRANSMEM     60     80       Helical; (Potential).
FT   TRANSMEM     94    114       Helical; (Potential).
FT   TRANSMEM    129    147       Helical; (Potential).
FT   TRANSMEM    159    179       Helical; (Potential).
FT   TRANSMEM    186    206       Helical; (Potential).
FT   TRANSMEM    221    241       Helical; (Potential).
FT   TRANSMEM    247    267       Helical; (Potential).
FT   TRANSMEM    284    304       Helical; (Potential).
FT   TRANSMEM    311    331       Helical; (Potential).
FT   TRANSMEM    335    355       Helical; (Potential).
FT   COMPBIAS      3     20       Pro-rich.
FT   CONFLICT      3      3       P -> S (in Ref. 1; BAC33499).
FT   CONFLICT    112    112       L -> Q (in Ref. 1; BAE38004).
FT   CONFLICT    326    326       C -> F (in Ref. 1; BAC35422).
SQ   SEQUENCE   408 AA;  45304 MW;  8E9669BC21CF6C55 CRC64;
     MIPPEPPQPQ LQPPPPPAPP NHVVTTIENL PAEGSGGVSL SASSRASMRQ RIRKVLNREM
     LISVALGQVL SLLVCGIGLT SKYLAEDFHA NTPVFQSFLN YILLFLVYTT TLAVRQGEEN
     LLAILRRRWW KYMILGLIDL EANYLVVKAY QYTTLTSVQL LDCFVIPVVI LLSWFFLLIR
     YKAVHFIGIV VCILGMGCMV GADVLVGRHQ GAGENKLVGD LLVLGGATLY GISNVWEESI
     IRTLSRVEFL GMIGLFGAFF SGIQLAIMEH KELLKVPWDW QIGLLYVGFS ACMFGLYSFM
     PVVIKKTSAT SVNLSLLTAD LYSLFCGLFL FHYKFSGLYL LSFFTILIGL VLYSSTSTYI
     AQDPRVYKQF RNPSGPVVDL PSTAQVEPSV TYTSLGQETE EEPHVRVA
//
ID   YLAT2_MOUSE             Reviewed;         515 AA.
AC   Q8BGK6; Q3TMY5; Q3U084; Q6ZQF5; Q8CFY3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Y+L amino acid transporter 2;
DE   AltName: Full=Solute carrier family 7 member 6;
DE   AltName: Full=y(+)L-type amino acid transporter 2;
DE            Short=Y+LAT2;
DE            Short=y+LAT-2;
GN   Name=Slc7a6; Synonyms=Kiaa0245;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Embryo, Embryonic stem cell, Embryonic stomach, Eye, Lung, and
RC   Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 140-293 (ISOFORM 1), AND TISSUE
RP   SPECIFICITY.
RX   PubMed=10903140;
RA   Broeer A., Wagner C.A., Lang F., Broeer S.;
RT   "The heterodimeric amino acid transporter 4F2hc/y+LAT2 mediates
RT   arginine efflux in exchange with glutamine.";
RL   Biochem. J. 349:787-795(2000).
CC   -!- FUNCTION: Involved in the sodium-independent uptake of dibasic
CC       amino acids and sodium-dependent uptake of some neutral amino
CC       acids. Requires co-expression with SLC3A2/4F2hc to mediate the
CC       uptake of arginine, leucine and glutamine. Also acts as an
CC       arginine/glutamine exchanger, following an antiport mechanism for
CC       amino acid transport, influencing arginine release in exchange for
CC       extracellular amino acids. Plays a role in nitric oxide synthesis
CC       via transport of L-arginine. Involved in the transport of L-
CC       arginine in monocytes. Reduces uptake of ornithine in retinal
CC       pigment epithelial cells (By similarity).
CC   -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid
CC       transport protein SLC3A2/4F2hc (By similarity).
CC   -!- SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BGK6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BGK6-2; Sequence=VSP_052833, VSP_052834;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Strongest expression in brain but also
CC       detected in testis, parotis, small intestine, heart and kidney.
CC       Weakly expressed in spleen, lung and liver.
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8)
CC       family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH38404.1; Type=Frameshift; Positions=345;
CC       Sequence=BAC97909.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK129099; BAC97909.1; ALT_INIT; mRNA.
DR   EMBL; AK049478; BAC33770.1; -; mRNA.
DR   EMBL; AK053899; BAC35581.1; -; mRNA.
DR   EMBL; AK157127; BAE33971.1; -; mRNA.
DR   EMBL; AK164666; BAE37866.1; -; mRNA.
DR   EMBL; AK165629; BAE38304.1; -; mRNA.
DR   EMBL; AK165979; BAE38497.1; -; mRNA.
DR   EMBL; BC038404; AAH38404.1; ALT_FRAME; mRNA.
DR   IPI; IPI00221632; -.
DR   IPI; IPI00895980; -.
DR   RefSeq; NP_848913.1; NM_178798.3.
DR   UniGene; Mm.46749; -.
DR   ProteinModelPortal; Q8BGK6; -.
DR   STRING; Q8BGK6; -.
DR   PhosphoSite; Q8BGK6; -.
DR   PRIDE; Q8BGK6; -.
DR   Ensembl; ENSMUST00000034378; ENSMUSP00000034378; ENSMUSG00000031904.
DR   GeneID; 330836; -.
DR   KEGG; mmu:330836; -.
DR   UCSC; uc009nfm.1; mouse.
DR   CTD; 330836; -.
DR   MGI; MGI:2142598; Slc7a6.
DR   eggNOG; maNOG09827; -.
DR   GeneTree; ENSGT00600000084149; -.
DR   HOGENOM; HBG714539; -.
DR   HOVERGEN; HBG000476; -.
DR   InParanoid; Q8BGK6; -.
DR   OMA; IFSWTIP; -.
DR   OrthoDB; EOG4255SN; -.
DR   PhylomeDB; Q8BGK6; -.
DR   NextBio; 399586; -.
DR   ArrayExpress; Q8BGK6; -.
DR   Bgee; Q8BGK6; -.
DR   Genevestigator; Q8BGK6; -.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015171; F:amino acid transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004841; AA-permease_dom.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   PANTHER; PTHR11785; AA/rel_permease1; 1.
DR   Pfam; PF00324; AA_permease; 1.
DR   PIRSF; PIRSF006060; AA_transporter; 1.
DR   PROSITE; PS00218; AMINO_ACID_PERMEASE_1; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Amino-acid transport; Antiport; Cell membrane;
KW   Disulfide bond; Membrane; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    515       Y+L amino acid transporter 2.
FT                                /FTId=PRO_0000341478.
FT   TOPO_DOM      1     44       Cytoplasmic (Potential).
FT   TRANSMEM     45     65       Helical; (Potential).
FT   TOPO_DOM     66     78       Extracellular (Potential).
FT   TRANSMEM     79     99       Helical; (Potential).
FT   TOPO_DOM    100    114       Cytoplasmic (Potential).
FT   TRANSMEM    115    135       Helical; (Potential).
FT   TOPO_DOM    136    167       Extracellular (Potential).
FT   TRANSMEM    168    188       Helical; (Potential).
FT   TOPO_DOM    189    194       Cytoplasmic (Potential).
FT   TRANSMEM    195    215       Helical; (Potential).
FT   TOPO_DOM    216    235       Extracellular (Potential).
FT   TRANSMEM    236    256       Helical; (Potential).
FT   TOPO_DOM    257    266       Cytoplasmic (Potential).
FT   TRANSMEM    267    287       Helical; (Potential).
FT   TOPO_DOM    288    311       Extracellular (Potential).
FT   TRANSMEM    312    332       Helical; (Potential).
FT   TOPO_DOM    333    363       Cytoplasmic (Potential).
FT   TRANSMEM    364    384       Helical; (Potential).
FT   TOPO_DOM    385    385       Extracellular (Potential).
FT   TRANSMEM    386    406       Helical; (Potential).
FT   TOPO_DOM    407    424       Cytoplasmic (Potential).
FT   TRANSMEM    425    445       Helical; (Potential).
FT   TOPO_DOM    446    451       Extracellular (Potential).
FT   TRANSMEM    452    472       Helical; (Potential).
FT   TOPO_DOM    473    515       Cytoplasmic (Potential).
FT   VAR_SEQ       1    164       Missing (in isoform 2).
FT                                /FTId=VSP_052833.
FT   VAR_SEQ     165    216       ACRLLAAACVCLLTFVNCAYVKWGTRVQDTFTYAKVLALIA
FT                                IIIMGLVKLCQ -> MFFFLPLPCFLSLFFFLLLFHLFNSP
FT                                SVFFLFFTFLLSPFSFAWSPTRLCPT (in isoform
FT                                2).
FT                                /FTId=VSP_052834.
FT   CONFLICT    129    129       W -> R (in Ref. 2; BAE33971).
FT   CONFLICT    132    132       L -> P (in Ref. 2; BAE38304).
SQ   SEQUENCE   515 AA;  56771 MW;  8DF8352607228507 CRC64;
     MEAQELGSPT PTYHLLPKAN QHTVKEDAGS PSQGSPETMQ LKKEISLLNG VSLVVGNMIG
     SGIFVSPKGV LKYTASYGLS LIVWAIGGLF SVVGALCYAE LGTTITKSGA SYAYILEAFG
     GFIAFIRLWV SLLIVEPTSQ AIIAITFANY IIKPSFPTCD PPYVACRLLA AACVCLLTFV
     NCAYVKWGTR VQDTFTYAKV LALIAIIIMG LVKLCQGHTE HFQDAFKGSS WNVGDLSLAL
     YSALFSYSGW DTLNFVTEEI KNPERNLPLA IGISMPIVTL IYILTNVAYY TVLNIQDVHK
     SDAVAVTFAD QTFGMFSWTI PIAVALSCFG GLNASIFASS RLFFVGSREG HLPNLLSMIH
     IERFTPVPAL LFNCTMTLIY LVVKDVFLLI NYFSFSYWFF VGLSVVGQLY LRWKEPDWPR
     PLKLSLFFPI VFCVCSLFLV AVPLFSDTIN SLIGIGIALS GVPVYFLGVY LPESRRPLFI
     RNVLATVTRV TQKLCFCVLT ELDVTEEKNV ERKTD
//
ID   Q8BGM0_MOUSE            Unreviewed;       517 AA.
AC   Q8BGM0;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 81.
DE   SubName: Full=Gardner-Rasheed feline sarcoma viral (Fgr) oncogene homolog;
DE   SubName: Full=Gardner-Rasheed feline sarcoma viral (Fgr) oncogene homolog, isoform CRA_a;
GN   Name=Fgr; ORFNames=RP23-125F21.1-001, mCG_20826;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone, and Thymus;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone, and Thymus;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone, and Thymus;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone, and Thymus;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone, and Thymus;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone, and Thymus;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone, and Thymus;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone, and Thymus;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RA   Pelan S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [11]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK036438; BAC29429.1; -; mRNA.
DR   EMBL; AK036476; BAC29445.1; -; mRNA.
DR   EMBL; AK038141; BAC29939.1; -; mRNA.
DR   EMBL; AK155902; BAE33493.1; -; mRNA.
DR   EMBL; AL627184; CAM14378.1; -; Genomic_DNA.
DR   EMBL; CH466552; EDL30081.1; -; Genomic_DNA.
DR   EMBL; CH466552; EDL30082.1; -; Genomic_DNA.
DR   IPI; IPI00308065; -.
DR   RefSeq; NP_034338.3; NM_010208.4.
DR   UniGene; Mm.271665; -.
DR   HSSP; P00523; 2PTK.
DR   ProteinModelPortal; Q8BGM0; -.
DR   SMR; Q8BGM0; 67-515.
DR   STRING; Q8BGM0; -.
DR   PRIDE; Q8BGM0; -.
DR   Ensembl; ENSMUST00000030693; ENSMUSP00000030693; ENSMUSG00000028874.
DR   GeneID; 14191; -.
DR   KEGG; mmu:14191; -.
DR   UCSC; uc008vcb.1; mouse.
DR   CTD; 14191; -.
DR   MGI; MGI:95527; Fgr.
DR   GeneTree; ENSGT00600000084003; -.
DR   HOVERGEN; HBG008761; -.
DR   InParanoid; Q8BGM0; -.
DR   OMA; RGDHVKH; -.
DR   PhylomeDB; Q8BGM0; -.
DR   NextBio; 285410; -.
DR   ArrayExpress; Q8BGM0; -.
DR   Bgee; Q8BGM0; -.
DR   Genevestigator; Q8BGM0; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IGI:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; SH3 domain; Transferase;
KW   Tyrosine-protein kinase.
SQ   SEQUENCE   517 AA;  58867 MW;  87DF5B19BF3F4734 CRC64;
     MGCVFCKKLE PASKEDVGLE GDFRSQTAEE RYFPDPTQGR TSSVFPQPTS PAFLNTGNMR
     SISGTGVTIF VALYDYEART GDDLTFTKGE KFHILNNTEY DWWEARSLSS GHRGYVPSNY
     VAPVDSIQAE EWYFGKISRK DAERQLLSSG NPQGAFLIRE SETTKGAYSL SIRDWDQNRG
     DHIKHYKIRK LDTGGYYITT RAQFDSIQDL VRHYMEVNDG LCYLLTAPCT TTKPQTLGLA
     KDAWEIDRNS IALERRLGTG CFGDVWLGTW NCSTKVAVKT LKPGTMSPKA FLEEAQIMKL
     LRHDKLVQLY AVVSEEPIYI VTEFMCYGSL LDFLKDREGQ NLMLPHLVDM AAQVAEGMAY
     MERMNYIHRD LRAANILVGE YLICKIADFG LARLIEDNEY NPQQGTKFPI KWTAPEAALF
     GRFTVKSDVW SFGILLTELI TKGRVPYPGM NNREVLEQVE HGYHMPCPPG CPASLYEVME
     QAWRLDPEER PTFEYLQSFL EDYFTSTEPQ YQPGDQT
//
ID   SYNPR_MOUSE             Reviewed;         265 AA.
AC   Q8BGN8; Q8C5J4; Q9DB89;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Synaptoporin;
GN   Name=Synpr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Olfactory bulb, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 150-159 AND 210-217, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Intrinsic membrane protein of small synaptic vesicles.
CC       Probable vesicular channel protein (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane; Multi-pass membrane protein (By
CC       similarity). Cell junction, synapse, synaptosome (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BGN8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BGN8-2; Sequence=VSP_008550;
CC   -!- SIMILARITY: Belongs to the synaptophysin/synaptobrevin family.
CC   -!- SIMILARITY: Contains 1 MARVEL domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK005132; BAB23831.1; -; mRNA.
DR   EMBL; AK032442; BAC27871.1; -; mRNA.
DR   EMBL; AK049661; BAC33864.1; -; mRNA.
DR   EMBL; AK078223; BAC37181.1; -; mRNA.
DR   EMBL; BC026512; AAH26512.1; -; mRNA.
DR   IPI; IPI00331165; -.
DR   IPI; IPI00378621; -.
DR   RefSeq; NP_001156504.1; NM_001163032.1.
DR   RefSeq; NP_082328.3; NM_028052.4.
DR   UniGene; Mm.317515; -.
DR   STRING; Q8BGN8; -.
DR   PRIDE; Q8BGN8; -.
DR   Ensembl; ENSMUST00000112656; ENSMUSP00000108275; ENSMUSG00000056296.
DR   GeneID; 72003; -.
DR   KEGG; mmu:72003; -.
DR   UCSC; uc007sfy.1; mouse.
DR   UCSC; uc007sgb.1; mouse.
DR   CTD; 72003; -.
DR   MGI; MGI:1919253; Synpr.
DR   eggNOG; roNOG10862; -.
DR   GeneTree; ENSGT00390000010039; -.
DR   HOVERGEN; HBG006681; -.
DR   OMA; NQQASLG; -.
DR   NextBio; 335200; -.
DR   ArrayExpress; Q8BGN8; -.
DR   Bgee; Q8BGN8; -.
DR   CleanEx; MM_SYNPR; -.
DR   Genevestigator; Q8BGN8; -.
DR   GermOnline; ENSMUSG00000056296; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0030285; C:integral to synaptic vesicle membrane; TAS:MGI.
DR   GO; GO:0019717; C:synaptosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   InterPro; IPR008253; Marvel.
DR   InterPro; IPR021128; MARVEL-like_dom.
DR   InterPro; IPR001285; Synaptophysin/porin.
DR   PANTHER; PTHR10306; Synaptophysin; 1.
DR   Pfam; PF01284; MARVEL; 1.
DR   PRINTS; PR00220; SYNAPTOPHYSN.
DR   PROSITE; PS51225; MARVEL; 1.
DR   PROSITE; PS00604; SYNAPTOP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cytoplasmic vesicle;
KW   Direct protein sequencing; Glycoprotein; Membrane; Repeat; Synapse;
KW   Synaptosome; Transmembrane; Transmembrane helix.
FT   CHAIN         1    265       Synaptoporin.
FT                                /FTId=PRO_0000179158.
FT   TOPO_DOM      1      4       Cytoplasmic (Potential).
FT   TRANSMEM      5     25       Helical; (Potential).
FT   TOPO_DOM     26     81       Vesicular (Potential).
FT   TRANSMEM     82    102       Helical; (Potential).
FT   TOPO_DOM    103    114       Cytoplasmic (Potential).
FT   TRANSMEM    115    135       Helical; (Potential).
FT   TOPO_DOM    136    177       Vesicular (Potential).
FT   TRANSMEM    178    198       Helical; (Potential).
FT   TOPO_DOM    199    265       Cytoplasmic (Potential).
FT   DOMAIN        1    202       MARVEL.
FT   REPEAT      210    214       1.
FT   REPEAT      222    226       2.
FT   REPEAT      227    231       3.
FT   REPEAT      232    236       4.
FT   REPEAT      238    242       5.
FT   REGION      210    242       5 X approximate repeats.
FT   CARBOHYD     33     33       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     38     38       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1      8       MCMVIFAP -> MDPVSQVASAGTFRALKEPLAFLRALEL
FT                                (in isoform 2).
FT                                /FTId=VSP_008550.
FT   CONFLICT    230    230       E -> K (in Ref. 1; BAC37181).
SQ   SEQUENCE   265 AA;  29228 MW;  81DD473A422815E5 CRC64;
     MCMVIFAPLF AMFAFATCGG YSGGLRLSVD CVNKTESNLS IDIAFAYPFR LQQVTFEVPT
     CEGKEQQKLA LVGDSSSSAE FFVTVAVFAF LYSLAATVVY IFFQNKYREN NRGPLIDFIV
     TVVFSFLWLV GSSAWAKGLS DVKVATDPKE VLLLMSACKQ PSNKCMAVHS PVMSSLNTSV
     VFGFLNFILW AGNIWFVFKE TGWHSSGQRY LSDPMEKHSS SYNQGRYNQE SYGSSGGYSQ
     QANLGPTSDE FGQQPSGPTS FNNQI
//
ID   VIPAR_MOUSE             Reviewed;         491 AA.
AC   Q8BGQ1; Q8BL55; Q8CIK4; Q91YI3;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=VPS33B-interacting protein;
DE   AltName: Full=Protein spe-39 homolog;
GN   Name=Vipar;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain, Cerebellum, Diencephalon, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-122, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   FUNCTION, INTERACTION WITH RAB11A, AND KNOCKDOWN.
RX   PubMed=20190753; DOI=10.1038/ng.538;
RA   Cullinane A.R., Straatman-Iwanowska A., Zaucker A., Wakabayashi Y.,
RA   Bruce C.K., Luo G., Rahman F., Gurakan F., Utine E., Ozkan T.B.,
RA   Denecke J., Vukovic J., Di Rocco M., Mandel H., Cangul H.,
RA   Matthews R.P., Thomas S.G., Rappoport J.Z., Arias I.M., Wolburg H.,
RA   Knisely A.S., Kelly D.A., Muller F., Maher E.R., Gissen P.;
RT   "Mutations in VIPAR cause an arthrogryposis, renal dysfunction and
RT   cholestasis syndrome phenotype with defects in epithelial
RT   polarization.";
RL   Nat. Genet. 42:303-312(2010).
CC   -!- FUNCTION: Plays a role in lysosomal trafficking (By similarity).
CC       May play a role in epithelial polarization through stabilization
CC       of apical membrane protein content, possibly via the RAB11A-
CC       dependent apical recycling pathway. Also involved in direct or
CC       indirect transcriptional regulation of E-cadherin.
CC   -!- SUBUNIT: Associates with the HOPS complex. Interacts with VPS33A
CC       and VPS33B (By similarity). Interacts with RAB11A.
CC   -!- SUBCELLULAR LOCATION: Early endosome (By similarity). Recycling
CC       endosome (By similarity). Late endosome (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BGQ1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BGQ1-2; Sequence=VSP_009285;
CC         Note=No experimental confirmation available;
CC   -!- MISCELLANEOUS: Vipar-deficient inner medullary collecting duct
CC       cells display abnormal expression of membrane proteins such as
CC       Ceacam5, structural and functional tight junction defects and
CC       reduced E-cadherin expression.
CC   -!- SIMILARITY: Belongs to the VIPAR family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK046322; BAC32680.1; -; mRNA.
DR   EMBL; AK049643; BAC33854.1; -; mRNA.
DR   EMBL; AK079055; BAC37516.1; -; mRNA.
DR   EMBL; AK082261; BAC38449.1; -; mRNA.
DR   EMBL; BC016646; AAH16646.1; -; mRNA.
DR   EMBL; BC023716; AAH23716.1; -; mRNA.
DR   IPI; IPI00229865; -.
DR   IPI; IPI00400395; -.
DR   RefSeq; NP_001136052.1; NM_001142580.1.
DR   RefSeq; NP_001136053.1; NM_001142581.1.
DR   RefSeq; NP_598805.2; NM_134044.3.
DR   UniGene; Mm.208750; -.
DR   ProteinModelPortal; Q8BGQ1; -.
DR   STRING; Q8BGQ1; -.
DR   PhosphoSite; Q8BGQ1; -.
DR   PRIDE; Q8BGQ1; -.
DR   Ensembl; ENSMUST00000021426; ENSMUSP00000021426; ENSMUSG00000021038.
DR   Ensembl; ENSMUST00000072744; ENSMUSP00000072527; ENSMUSG00000021038.
DR   GeneID; 104799; -.
DR   KEGG; mmu:104799; -.
DR   UCSC; uc007oip.1; mouse.
DR   UCSC; uc007oiq.1; mouse.
DR   CTD; 104799; -.
DR   MGI; MGI:2144805; Vipar.
DR   GeneTree; ENSGT00390000013955; -.
DR   HOGENOM; HBG505592; -.
DR   HOVERGEN; HBG051031; -.
DR   InParanoid; Q8BGQ1; -.
DR   OMA; PVGSISW; -.
DR   OrthoDB; EOG4FXR7Q; -.
DR   PhylomeDB; Q8BGQ1; -.
DR   NextBio; 357292; -.
DR   ArrayExpress; Q8BGQ1; -.
DR   Bgee; Q8BGQ1; -.
DR   CleanEx; MM_AI413782; -.
DR   Genevestigator; Q8BGQ1; -.
DR   GermOnline; ENSMUSG00000021038; Mus musculus.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR019177; Golgin_subfamily_A_member_5.
DR   Pfam; PF09787; Golgin_A5; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endosome; Phosphoprotein; Protein transport;
KW   Transcription; Transcription regulation; Transport.
FT   CHAIN         1    491       VPS33B-interacting protein.
FT                                /FTId=PRO_0000089936.
FT   MOD_RES      11     11       Phosphotyrosine (By similarity).
FT   MOD_RES      21     21       Phosphothreonine.
FT   MOD_RES     119    119       Phosphoserine.
FT   MOD_RES     122    122       Phosphoserine.
FT   MOD_RES     130    130       Phosphothreonine (By similarity).
FT   VAR_SEQ     148    166       Missing (in isoform 2).
FT                                /FTId=VSP_009285.
FT   CONFLICT    131    131       P -> R (in Ref. 1; BAC32680).
FT   CONFLICT    316    316       I -> V (in Ref. 2; AAH16646).
SQ   SEQUENCE   491 AA;  56625 MW;  7F143EAA3D009E9A CRC64;
     MNRTKGDEEE YWNSSKFKAF TFDDEDDELS QLKESKRAVN SLRDIVDDDD DDDLERVSWT
     GEPVGSISWS IKETAGSSGS TPEGREQLKG RNSFYTQLPK PPSTYSLSSF FRGRTRPGSF
     QSLSDALSDT PAKSYAPELG RPKGEYRDYS NDWSLSDTVQ RLRRGKVCSL ERFRSLQDKL
     QLLEEAVSMH DGNVITAVLI FLKRTLSKEI LFRELEVRQV ALRHLIHFLK EIGDQKLLLD
     LFRFLDRAEE LALSHYREHL NIQDPEKRKE FLKTCIGLPF SAEDAAHVQD HYTLLERQII
     IEANDRHLES SGQTDIFRKH PRKASILNMP LVTTLFYACF YHYTESEGTF SSPINLKKTF
     KIPDKQYVLT ALAARAKLRA WNDVDALFTT KNWLGYTKKR APIGFHRVVE ILHKNSAPVQ
     ILQEYVNLVE DVDTKLNLAT KFKCHDVVID TCRDLKDRQQ LLAYRSKVDK GSAEEEKIDA
     ILSSSQIRWK N
//
ID   LRC8D_MOUSE             Reviewed;         859 AA.
AC   Q8BGR2; Q3UVA9; Q8CI13;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Leucine-rich repeat-containing protein 8D;
DE   AltName: Full=Leucine-rich repeat-containing protein 5;
GN   Name=Lrrc8d; Synonyms=Lrrc5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone, Corpora quadrigemina, Liver, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Contains 12 LRR (leucine-rich) repeats.
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DR   EMBL; AK046249; BAC32656.1; -; mRNA.
DR   EMBL; AK050400; BAC34237.1; -; mRNA.
DR   EMBL; AK080722; BAC37994.1; -; mRNA.
DR   EMBL; AK137459; BAE23361.1; -; mRNA.
DR   EMBL; BC037717; AAH37717.1; -; mRNA.
DR   IPI; IPI00350794; -.
DR   RefSeq; NP_001116240.1; NM_001122768.1.
DR   RefSeq; NP_848816.3; NM_178701.3.
DR   UniGene; Mm.23837; -.
DR   ProteinModelPortal; Q8BGR2; -.
DR   SMR; Q8BGR2; 441-857.
DR   PhosphoSite; Q8BGR2; -.
DR   PRIDE; Q8BGR2; -.
DR   Ensembl; ENSMUST00000060531; ENSMUSP00000057293; ENSMUSG00000046079.
DR   Ensembl; ENSMUST00000120847; ENSMUSP00000113603; ENSMUSG00000046079.
DR   GeneID; 231549; -.
DR   KEGG; mmu:231549; -.
DR   UCSC; uc008ylg.1; mouse.
DR   CTD; 231549; -.
DR   MGI; MGI:1922368; Lrrc8d.
DR   GeneTree; ENSGT00600000084236; -.
DR   HOGENOM; HBG445357; -.
DR   HOVERGEN; HBG052360; -.
DR   InParanoid; Q8BGR2; -.
DR   OMA; AFSFLRD; -.
DR   OrthoDB; EOG4HX50B; -.
DR   PhylomeDB; Q8BGR2; -.
DR   NextBio; 380602; -.
DR   ArrayExpress; Q8BGR2; -.
DR   Bgee; Q8BGR2; -.
DR   CleanEx; MM_LRRC8D; -.
DR   Genevestigator; Q8BGR2; -.
DR   GermOnline; ENSMUSG00000046079; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR021040; LRR_protein-8_N.
DR   Pfam; PF12534; DUF3733; 2.
DR   Pfam; PF00560; LRR_1; 3.
DR   SMART; SM00369; LRR_TYP; 1.
DR   PROSITE; PS51450; LRR; 9.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Leucine-rich repeat; Membrane; Phosphoprotein; Repeat;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    859       Leucine-rich repeat-containing protein
FT                                8D.
FT                                /FTId=PRO_0000084494.
FT   TRANSMEM     23     43       Helical; (Potential).
FT   TRANSMEM    165    185       Helical; (Potential).
FT   TRANSMEM    366    386       Helical; (Potential).
FT   REPEAT       38     64       LRR 1.
FT   REPEAT      490    513       LRR 2.
FT   REPEAT      537    560       LRR 3.
FT   REPEAT      588    610       LRR 4.
FT   REPEAT      635    657       LRR 5.
FT   REPEAT      658    682       LRR 6.
FT   REPEAT      684    705       LRR 7.
FT   REPEAT      706    729       LRR 8.
FT   REPEAT      731    751       LRR 9.
FT   REPEAT      752    775       LRR 10.
FT   REPEAT      777    797       LRR 11.
FT   REPEAT      798    821       LRR 12.
FT   MOD_RES     242    242       Phosphoserine (By similarity).
FT   MOD_RES     243    243       Phosphoserine (By similarity).
FT   MOD_RES     247    247       Phosphoserine (By similarity).
FT   CARBOHYD    256    256       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    599    599       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    606    606       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    741    741       N-linked (GlcNAc...) (Potential).
FT   CONFLICT     75     75       I -> V (in Ref. 2; AAH37717).
FT   CONFLICT    128    128       A -> V (in Ref. 2; AAH37717).
SQ   SEQUENCE   859 AA;  98113 MW;  7A8DD3CF52AB982D CRC64;
     MFTLAEVASL NDIQPTYRIL KPWWDVFMDY LAVVMLMVAI FAGTMQLTKD QVVCLPVLPS
     PANSKAHTPP GNADITTEVP RMETATHQDQ NGQTTTNDVA FGTSAVTPDI PLQATHPHAE
     STLPNQEAKK EKRDPTGRKT NLDFQQYVFI NQMCYHLALP WYSKYFPYLA LIHTIILMVS
     SNFWFKYPKT CSKVEHFVSI LGKCFESPWT TKALSETACE DSEENKQRIT GAQTLPKHVS
     TSSDEGSPSA STPMINKTGF KFSAEKPVIE VPSMTILDKK DGEQAKALFE KVRKFRAHVE
     DSDLIYKLYV VQTLIKTAKF IFILCYTANF VNAISFEHVC KPKVEHLTGY EVFECTHNMA
     YMLKKLLISY ISIICVYGFI CLYTLFWLFR IPLKEYSFEK VREESSFSDI PDVKNDFAFL
     LHMVDQYDQL YSKRFGVFLS EVSENKLREI SLNHEWTFEK LRQHVSRNAQ DKQELHLFML
     SGVPDAVFDL TDLDVLKLEL IPEAKIPAKI SQMTNLQELH LCHCPAKVEQ TAFSFLRDHL
     RCLHVKFTDV AEIPAWVYLL KNLRELYLIG NLNSENNKMI GLESLRELRH LKILHVKSNL
     TKVPSNITDV APHLTKLVIH NDGTKLLVLN SLKKMMNVAE LELQNCELER IPHAIFSLSN
     LQELDLKSNN IRTIEEIISF QHLKRLTCLK LWHNKIVAIP PSITHVKNLE SLYFSNNKLE
     SLPTAVFSLQ KLRCLDVSYN NISTIPIEIG LLQNLQHLHI TGNKVDILPK QLFKCVKLRT
     LNLGQNCIAS LPEKISQLTQ LTQLELKGNC LDRLPAQLGQ CRMLKKSGLV VEDQLFDTLP
     LEVKEALNQD VNVPFANGI
//
ID   ZKSC1_MOUSE             Reviewed;         561 AA.
AC   Q8BGS3; Q7TS88; Q8BJ55; Q9CRN6;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Zinc finger protein with KRAB and SCAN domains 1;
GN   Name=Zkscan1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of FLJ genes:
RT   the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:127-135(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Egg, Ovary, Skin, and Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BGS3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BGS3-2; Sequence=VSP_016958;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family.
CC   -!- SIMILARITY: Contains 6 C2H2-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 KRAB domain.
CC   -!- SIMILARITY: Contains 1 SCAN box domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC27539.1; Type=Frameshift; Positions=479;
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DR   EMBL; AK131148; BAD21398.1; -; mRNA.
DR   EMBL; AK020039; BAB31975.1; -; mRNA.
DR   EMBL; AK028932; BAC26200.1; -; mRNA.
DR   EMBL; AK031759; BAC27539.1; ALT_FRAME; mRNA.
DR   EMBL; AK036807; BAC29584.1; -; mRNA.
DR   EMBL; AK054323; BAC35730.1; -; mRNA.
DR   EMBL; AK135999; BAE22767.1; -; mRNA.
DR   EMBL; BC052441; AAH52441.1; -; mRNA.
DR   IPI; IPI00221695; -.
DR   IPI; IPI00408477; -.
DR   RefSeq; NP_084145.1; NM_029869.1.
DR   RefSeq; NP_598667.2; NM_133906.4.
DR   UniGene; Mm.213114; -.
DR   ProteinModelPortal; Q8BGS3; -.
DR   SMR; Q8BGS3; 50-138, 343-543.
DR   PhosphoSite; Q8BGS3; -.
DR   PRIDE; Q8BGS3; -.
DR   Ensembl; ENSMUST00000019660; ENSMUSP00000019660; ENSMUSG00000029729.
DR   Ensembl; ENSMUST00000066617; ENSMUSP00000068480; ENSMUSG00000029729.
DR   GeneID; 74570; -.
DR   KEGG; mmu:74570; -.
DR   UCSC; uc009aej.1; mouse.
DR   UCSC; uc009aek.1; mouse.
DR   CTD; 74570; -.
DR   MGI; MGI:1921820; Zkscan1.
DR   eggNOG; roNOG06261; -.
DR   GeneTree; ENSGT00600000084138; -.
DR   HOGENOM; HBG717200; -.
DR   HOVERGEN; HBG018163; -.
DR   InParanoid; Q8BGS3; -.
DR   OMA; RFQKEFG; -.
DR   OrthoDB; EOG4DJJW3; -.
DR   PhylomeDB; Q8BGS3; -.
DR   NextBio; 341125; -.
DR   ArrayExpress; Q8BGS3; -.
DR   Bgee; Q8BGS3; -.
DR   CleanEx; MM_ZKSCAN1; -.
DR   Genevestigator; Q8BGS3; -.
DR   GermOnline; ENSMUSG00000029729; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   GO; GO:0016032; P:viral reproduction; IEA:InterPro.
DR   InterPro; IPR001909; Krueppel-associated_box.
DR   InterPro; IPR008916; Retrov_capsid_C.
DR   InterPro; IPR003309; Tscrpt_reg_SCAN.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 6.
DR   Pfam; PF01352; KRAB; 1.
DR   Pfam; PF02023; SCAN; 1.
DR   Pfam; PF00096; zf-C2H2; 5.
DR   SMART; SM00349; KRAB; 1.
DR   SMART; SM00431; SCAN; 1.
DR   SMART; SM00355; ZnF_C2H2; 6.
DR   SUPFAM; SSF109640; Krueppel-associated_box; 1.
DR   SUPFAM; SSF47353; Retrov_capsid_C; 1.
DR   PROSITE; PS50805; KRAB; FALSE_NEG.
DR   PROSITE; PS50804; SCAN_BOX; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE   2: Evidence at transcript level;
KW   Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW   Phosphoprotein; Repeat; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    561       Zinc finger protein with KRAB and SCAN
FT                                domains 1.
FT                                /FTId=PRO_0000047754.
FT   DOMAIN       56    138       SCAN box.
FT   DOMAIN      225    304       KRAB.
FT   ZN_FING     375    397       C2H2-type 1.
FT   ZN_FING     403    425       C2H2-type 2.
FT   ZN_FING     431    453       C2H2-type 3.
FT   ZN_FING     459    481       C2H2-type 4.
FT   ZN_FING     487    509       C2H2-type 5.
FT   ZN_FING     515    537       C2H2-type 6.
FT   MOD_RES      13     13       Phosphoserine (By similarity).
FT   MOD_RES     469    469       Phosphoserine (By similarity).
FT   VAR_SEQ     192    264       Missing (in isoform 2).
FT                                /FTId=VSP_016958.
FT   CONFLICT    244    244       L -> M (in Ref. 2; BAC27539).
SQ   SEQUENCE   561 AA;  63439 MW;  757C4FD2CFB28DDB CRC64;
     MMTAESRETT GLSPQAAQEK DGIVIVKVEE EDEEDHMWGQ DSSLQETPPP DPEVFRQRFR
     RFCYQNTFGP REALNRLKEL CHQWLRPEVN SKEQILELLV LEQFLSILPK ELQVWLQEYR
     PDSGEEAVTL LEDLELDLSG QQVPGQVHGP EMLARGVVPL DPVQESSSFD HHETAQSHFK
     HSSRKPRLLS RALPATHVPA PHHEGNPRDQ AMASALLTAD SQAMVKIEDM AVSLILEEWG
     CQNLARRNLN RDSRQMNLGN VFSQGSENRN GNESTSKAEV KEDSTSHGEI AGRFQKEFGE
     KREQQGRVVE RQQKNPEEKT GKEKKEPGPP TAKEKKPSTG ERGPREKGKG LGRSFSLSAN
     FNNTPEEAPS GAKTHRCDEC GKCFTRSSSL IRHKIIHTGE KPYECNECGK AFSLNSNLVL
     HQRIHTGEKP HECNECGKAF SHSSNLILHQ RIHSGEKPYE CNECGKAFSQ SSDLTKHQRI
     HTGEKPYECS ECGKAFNRNS YLILHRRIHT REKPYKCTKC GKAFTRSSTL TLHHRIHARE
     RTSEYSPASL DAFGAFLKSC V
//
ID   MILK1_MOUSE             Reviewed;         870 AA.
AC   Q8BGT6; Q8BJ60;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=MICAL-like protein 1;
DE   AltName: Full=Molecule interacting with Rab13;
DE            Short=MIRab13;
GN   Name=Micall1; Synonyms=D15Mit260, Kiaa1668, Mirab13;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494 AND SER-496, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May be a cytoskeletal regulator.
CC   -!- SUBUNIT: Binds to Rab13 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BGT6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BGT6-2; Sequence=VSP_009851;
CC       Name=3;
CC         IsoId=Q8BGT6-3; Sequence=VSP_009852, VSP_009853;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC   -!- SIMILARITY: Contains 1 LIM zinc-binding domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98229.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK129419; BAC98229.1; ALT_INIT; mRNA.
DR   EMBL; AK031386; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK076763; BAC36472.1; -; mRNA.
DR   EMBL; AK077217; BAC36689.1; -; mRNA.
DR   IPI; IPI00403239; -.
DR   IPI; IPI00411026; -.
DR   IPI; IPI00411027; -.
DR   RefSeq; NP_803412.1; NM_177461.1.
DR   UniGene; Mm.196480; -.
DR   ProteinModelPortal; Q8BGT6; -.
DR   SMR; Q8BGT6; 2-113, 157-227.
DR   PhosphoSite; Q8BGT6; -.
DR   PRIDE; Q8BGT6; -.
DR   Ensembl; ENSMUST00000040320; ENSMUSP00000042053; ENSMUSG00000033039.
DR   GeneID; 27008; -.
DR   KEGG; mmu:27008; -.
DR   UCSC; uc007wsm.1; mouse.
DR   UCSC; uc007wsn.1; mouse.
DR   UCSC; uc007wso.1; mouse.
DR   CTD; 27008; -.
DR   MGI; MGI:105870; Micall1.
DR   GeneTree; ENSGT00600000084263; -.
DR   HOGENOM; HBG278726; -.
DR   HOVERGEN; HBG052475; -.
DR   InParanoid; Q8BGT6; -.
DR   OrthoDB; EOG4PK288; -.
DR   NextBio; 304945; -.
DR   ArrayExpress; Q8BGT6; -.
DR   Bgee; Q8BGT6; -.
DR   Genevestigator; Q8BGT6; -.
DR   GermOnline; ENSMUSG00000033039; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR022735; DUF3585.
DR   InterPro; IPR001781; Znf_LIM.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 1.
DR   Gene3D; G3DSA:2.10.110.10; Znf_LIM; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF12130; DUF3585; 1.
DR   Pfam; PF00412; LIM; 1.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00132; LIM; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW   LIM domain; Metal-binding; Phosphoprotein; Zinc.
FT   CHAIN         1    870       MICAL-like protein 1.
FT                                /FTId=PRO_0000075849.
FT   DOMAIN        2    105       CH.
FT   DOMAIN      163    226       LIM zinc-binding.
FT   COILED      689    722       Potential.
FT   COILED      806    840       Potential.
FT   COMPBIAS    277    558       Pro-rich.
FT   COMPBIAS    424    432       Poly-Glu.
FT   COMPBIAS    559    576       Ser-rich.
FT   COMPBIAS    816    819       Poly-Glu.
FT   MOD_RES     291    291       Phosphoserine (By similarity).
FT   MOD_RES     305    305       Phosphoserine (By similarity).
FT   MOD_RES     314    314       Phosphothreonine (By similarity).
FT   MOD_RES     477    477       Phosphothreonine (By similarity).
FT   MOD_RES     480    480       Phosphoserine (By similarity).
FT   MOD_RES     481    481       Phosphoserine (By similarity).
FT   MOD_RES     494    494       Phosphoserine.
FT   MOD_RES     496    496       Phosphoserine.
FT   MOD_RES     628    628       Phosphoserine (By similarity).
FT   VAR_SEQ       1    357       Missing (in isoform 2).
FT                                /FTId=VSP_009851.
FT   VAR_SEQ     113    133       AAASPPKPGKDPAPPSPTSTS -> GERGPSPSGRLPWAVY
FT                                FFAEQ (in isoform 3).
FT                                /FTId=VSP_009852.
FT   VAR_SEQ     134    870       Missing (in isoform 3).
FT                                /FTId=VSP_009853.
FT   CONFLICT    588    590       PQV -> LQA (in Ref. 1; BAC36472/
FT                                BAC36689).
SQ   SEQUENCE   870 AA;  94091 MW;  CB727A2876615C00 CRC64;
     MAGPRGALLA WCRRQCEGYR GVDIRDLSSS FRDGLAFCAI LHRHRPDLLD FQSLSKENVF
     ENNRLAFEVA EKELGIPALL DPNDMVSMSV PDCLSIMTYV SQYYNHFTSS GQAAASPPKP
     GKDPAPPSPT STSPAVQPGE EAQGDDLSPD SLSEQGKQQP PSSACAACGQ RVHLVQRYLA
     EGRLYHRHCF RCRQCSSTLV PGSYSSGPEE GTFVCAERCT RLGPGSRSGT RLLSQQRQQP
     AAAEAKDAED NDPSLSVAAV AEADRLQASS EVQFHTPTKP PLPSKPQELA SPPGGRPTPA
     PRKASESSAL TPPTPRPRSS LQQDGTVEQS VSSGLVNGRL QEPPVPKPRG TPKLSERMAA
     PRKDPPWITL VQTEPKKKPA PQPPSSGPGP LSQAYRQVED GGLEEQTQKS SGTEPEPKPY
     NPFEEEEEEE GEPAPPVPSP SLAPPVPSPS PAPPVPSPAP APSEATPKSL HPWYGITPTS
     SPKTKKRPAP RAPSASPLAI HASRLSHSEP PSATPSPALS VESLSSESSS HTANAEPLEP
     PAVPKSSSDP AVHVPGTPGT SGNSVTPSAN SSLSSSGELG QPSGEQMPQV RTKGSAGTHS
     TKPFSGATPT PFLLAGDRNP APPVGSASPQ LQIKSSCKEN PFNRKPSPSA SPTVRKATKG
     AKPVRPPAPG HGFPLIKRKV QADQYIPEED IYGEMDNIER QLDALEHSGV LLEEKLRGGA
     NEGSEDDMLV DWFKLIHEKH LLVRRESELI YVFKQQNLEQ RQADVEFELR CLLNKPEKDW
     TDEDRAREKV LMQELMTLIE QRDAIVNCLD EDRQREEEED KMLETMIKKK DFQREAESDS
     KKKGKFKTIK VLKFLGNKRE AKSKAPGDKS
//
ID   PHIPL_MOUSE             Reviewed;         375 AA.
AC   Q8BGT8; A4FVA0; Q8BZJ1; Q8C0X3; Q8CFU1; Q8R0C1;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Phytanoyl-CoA hydroxylase-interacting protein-like;
GN   Name=Phyhipl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Diencephalon, Olfactory bulb, Spinal cord, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 10-375 (ISOFORM 2).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in the development of the central system
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BGT8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BGT8-2; Sequence=VSP_034070;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the PHYHIP family.
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI25000.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part;
CC       Sequence=BAC28713.1; Type=Frameshift; Positions=109;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK029522; BAC26493.1; -; mRNA.
DR   EMBL; AK032166; BAC27735.1; -; mRNA.
DR   EMBL; AK034448; BAC28713.1; ALT_FRAME; mRNA.
DR   EMBL; AK083011; BAC38729.1; -; mRNA.
DR   EMBL; BC027081; AAH27081.1; -; mRNA.
DR   EMBL; BC037618; AAH37618.2; -; mRNA.
DR   EMBL; BC124999; AAI25000.1; ALT_SEQ; mRNA.
DR   IPI; IPI00224093; -.
DR   IPI; IPI00896093; -.
DR   RefSeq; NP_001156318.1; NM_001162846.1.
DR   RefSeq; NP_848736.2; NM_178621.4.
DR   UniGene; Mm.19825; -.
DR   ProteinModelPortal; Q8BGT8; -.
DR   PRIDE; Q8BGT8; -.
DR   Ensembl; ENSMUST00000046513; ENSMUSP00000045807; ENSMUSG00000037747.
DR   GeneID; 70911; -.
DR   KEGG; mmu:70911; -.
DR   UCSC; uc007fnz.1; mouse.
DR   CTD; 70911; -.
DR   MGI; MGI:1918161; Phyhipl.
DR   eggNOG; roNOG11333; -.
DR   GeneTree; ENSGT00390000014563; -.
DR   HOGENOM; HBG443953; -.
DR   HOVERGEN; HBG053596; -.
DR   InParanoid; Q8BGT8; -.
DR   OMA; KISWDMD; -.
DR   OrthoDB; EOG4ZCT4N; -.
DR   PhylomeDB; Q8BGT8; -.
DR   NextBio; 332575; -.
DR   ArrayExpress; Q8BGT8; -.
DR   Bgee; Q8BGT8; -.
DR   Genevestigator; Q8BGT8; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF00041; fn3; 1.
DR   SMART; SM00060; FN3; 1.
DR   SUPFAM; SSF49265; FN_III-like; 1.
DR   PROSITE; PS50853; FN3; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein.
FT   CHAIN         1    375       Phytanoyl-CoA hydroxylase-interacting
FT                                protein-like.
FT                                /FTId=PRO_0000338642.
FT   DOMAIN       48    153       Fibronectin type-III.
FT   CARBOHYD     22     22       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     36     36       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     199    375       Missing (in isoform 2).
FT                                /FTId=VSP_034070.
FT   CONFLICT     15     15       S -> I (in Ref. 1; BAC26493).
FT   CONFLICT     78     78       R -> H (in Ref. 1; BAC28713).
SQ   SEQUENCE   375 AA;  42341 MW;  7091CC98C802941A CRC64;
     MEVPRLDHAL SSPSSPCEEI KNLSLEAIQL CDRDGNKSQD SGIAEMEELP VPHNIKINNI
     TCDSFKISWD MDSKSKDRIT HYFIDLNKKE NKNSNKFKHK DVPTKLVAKA VPLPMTVRGH
     WFLSPRTEYT VAVQTASKQV DGDYVVSEWS EIIEFCTADY SKVHLTQLLE KADVIAGRML
     KFSVFYRNQH KEYFDYVREH YGNAMQPSIK DNSGSHGSPI SGKLEGIFFS CSTEFNTGKP
     PQDSPYGRYR FEIAAEKLFN PNTNLYFGDF YCMYTAYHYV ILVIAPVGSP GDEFCKQRLP
     QLNSKDNNFL TCTEEDGVLV YHHAQDVILE VIYTDPVALS LGTVAEITGH QLMSLSTANA
     KKDPSCKTCN ISVGR
//
ID   CCNY_MOUSE              Reviewed;         341 AA.
AC   Q8BGU5; Q8CI87; Q9CYN5;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Cyclin-Y;
DE   AltName: Full=Cyclin fold protein 1;
GN   Name=Ccny; Synonyms=Cfp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Skin, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=Czech II, and FVB/N; TISSUE=Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324 AND SER-326, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-326, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25; SER-83 AND SER-326,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-326, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Positive regulatory subunit of the cyclin-dependent
CC       kinase CDK14/PFTK1. Acts as a cell-cycle regulator of Wnt
CC       signaling pathway during G2/M phase by recruiting CDK14/PFTK1 to
CC       the plasma membrane and promoting phosphorylation of LRP6, leading
CC       to the activation of the Wnt signaling pathway (By similarity).
CC   -!- SUBUNIT: Interacts with CDK14 and LRP6 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BGU5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BGU5-2; Sequence=VSP_014835;
CC   -!- PTM: Ubiquitinated; leading to its degradation (By similarity).
CC   -!- SIMILARITY: Belongs to the cyclin family. Cyclin Y subfamily.
CC   -!- SIMILARITY: Contains 1 cyclin N-terminal domain.
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DR   EMBL; AK017493; BAB30772.1; -; mRNA.
DR   EMBL; AK028696; BAC26071.1; -; mRNA.
DR   EMBL; AK076556; BAC36391.1; -; mRNA.
DR   EMBL; BC023321; AAH23321.1; -; mRNA.
DR   EMBL; BC035524; AAH35524.1; -; mRNA.
DR   IPI; IPI00308149; -.
DR   IPI; IPI00471272; -.
DR   RefSeq; NP_080760.2; NM_026484.3.
DR   UniGene; Mm.376607; -.
DR   UniGene; Mm.86523; -.
DR   ProteinModelPortal; Q8BGU5; -.
DR   MINT; MINT-4125949; -.
DR   PhosphoSite; Q8BGU5; -.
DR   PRIDE; Q8BGU5; -.
DR   Ensembl; ENSMUST00000053917; ENSMUSP00000050001; ENSMUSG00000024286.
DR   Ensembl; ENSMUST00000115867; ENSMUSP00000111533; ENSMUSG00000024286.
DR   GeneID; 67974; -.
DR   KEGG; mmu:67974; -.
DR   UCSC; uc008eai.1; mouse.
DR   CTD; 67974; -.
DR   MGI; MGI:1915224; Ccny.
DR   eggNOG; roNOG04437; -.
DR   GeneTree; ENSGT00390000006626; -.
DR   HOGENOM; HBG381758; -.
DR   HOVERGEN; HBG058985; -.
DR   InParanoid; Q8BGU5; -.
DR   OMA; YINHHPP; -.
DR   OrthoDB; EOG43JC51; -.
DR   PhylomeDB; Q8BGU5; -.
DR   NextBio; 458322; -.
DR   ArrayExpress; Q8BGU5; -.
DR   Bgee; Q8BGU5; -.
DR   CleanEx; MM_CCNY; -.
DR   Genevestigator; Q8BGU5; -.
DR   GermOnline; ENSMUSG00000024286; Mus musculus.
DR   GO; GO:0000308; C:cytoplasmic cyclin-dependent protein kinase holoenzyme complex; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016538; F:cyclin-dependent protein kinase regulator activity; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0045737; P:positive regulation of cyclin-dependent protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0060828; P:regulation of canonical Wnt receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR006670; Cyclin.
DR   InterPro; IPR011028; Cyclin-like.
DR   InterPro; IPR013763; Cyclin-related.
DR   InterPro; IPR006671; Cyclin_N.
DR   InterPro; IPR012399; UCP_CG14939_cyclin-contain.
DR   Gene3D; G3DSA:1.10.472.10; Cyclin_related; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   PIRSF; PIRSF028934; Cyclin_CG14939; 1.
DR   SMART; SM00385; CYCLIN; 1.
DR   SUPFAM; SSF47954; Cyclin_like; 1.
DR   PROSITE; PS00292; CYCLINS; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Cell division; Cell membrane;
KW   Cyclin; Lipoprotein; Membrane; Myristate; Phosphoprotein;
KW   Ubl conjugation; Wnt signaling pathway.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    341       Cyclin-Y.
FT                                /FTId=PRO_0000080515.
FT   DOMAIN      143    265       Cyclin N-terminal.
FT   MOD_RES      21     21       Phosphoserine.
FT   MOD_RES      25     25       Phosphoserine.
FT   MOD_RES      83     83       Phosphoserine.
FT   MOD_RES     102    102       Phosphoserine.
FT   MOD_RES     324    324       Phosphoserine.
FT   MOD_RES     326    326       Phosphoserine.
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
FT   VAR_SEQ      52     76       Missing (in isoform 2).
FT                                /FTId=VSP_014835.
FT   CONFLICT    257    257       L -> P (in Ref. 1; BAB30772).
SQ   SEQUENCE   341 AA;  39395 MW;  6F16CE5B14559FCB CRC64;
     MGNTTSCCVS SSPKLRRNAH SRLESYRPDT DLSREDTGCN LQHISDRENI DDLNMEFNPS
     DHPRASTIFL SKSQTDVREK RKSLFINHHP PGQTSRKYSS CSTIFLDDST VSQPNLKYTI
     KCVALAIYYH IKNRDPDGRM LLDIFDENLH PLSKSEVPPD YDKHNPEQKQ IYRFVRTLFS
     AAQLTAECAI VTLVYLERLL TYAEIDICPA NWKRIVLGAI LLASKVWDDQ AVWNVDYCQI
     LKDITVEDMN ELERQFLELL QFNINVPSSV YAKYYFDLRS LAEANNLSFP LEPLSRERAH
     KLEAISRLCE DKYKDLRKPM RKRSASADNL ILPRWSPAII S
//
ID   SMC7L_MOUSE             Reviewed;         463 AA.
AC   Q8BGV8; Q8C4Y9;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Smith-Magenis syndrome chromosomal region candidate gene 7 protein-like;
GN   Name=Smcr7l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus, Pancreas, Retina, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the SMCR7 family.
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DR   EMBL; AK038466; BAC30010.1; -; mRNA.
DR   EMBL; AK044773; BAC32082.1; -; mRNA.
DR   EMBL; AK050546; BAC34317.1; -; mRNA.
DR   EMBL; AK080375; BAC37896.1; -; mRNA.
DR   IPI; IPI00308161; -.
DR   RefSeq; NP_848834.2; NM_178719.5.
DR   UniGene; Mm.307163; -.
DR   PhosphoSite; Q8BGV8; -.
DR   PRIDE; Q8BGV8; -.
DR   Ensembl; ENSMUST00000023048; ENSMUSP00000023048; ENSMUSG00000022412.
DR   GeneID; 239555; -.
DR   KEGG; mmu:239555; -.
DR   UCSC; uc007wvh.1; mouse.
DR   CTD; 239555; -.
DR   MGI; MGI:2146020; Smcr7l.
DR   eggNOG; roNOG11780; -.
DR   GeneTree; ENSGT00390000013127; -.
DR   HOGENOM; HBG445132; -.
DR   HOVERGEN; HBG054078; -.
DR   InParanoid; Q8BGV8; -.
DR   OMA; SGKRSWE; -.
DR   OrthoDB; EOG44QT0T; -.
DR   PhylomeDB; Q8BGV8; -.
DR   NextBio; 384173; -.
DR   ArrayExpress; Q8BGV8; -.
DR   Bgee; Q8BGV8; -.
DR   Genevestigator; Q8BGV8; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    463       Smith-Magenis syndrome chromosomal region
FT                                candidate gene 7 protein-like.
FT                                /FTId=PRO_0000310449.
FT   TRANSMEM     24     46       Helical; (Potential).
FT   MOD_RES      55     55       Phosphoserine (By similarity).
FT   MOD_RES      58     58       Phosphothreonine (By similarity).
FT   MOD_RES      59     59       Phosphoserine.
FT   MOD_RES      94     94       Phosphoserine (By similarity).
FT   CONFLICT    444    444       D -> N (in Ref. 1; BAC37896).
SQ   SEQUENCE   463 AA;  51184 MW;  69C8869807974024 CRC64;
     MAGAGERKGK KDDNGIGTAI DFVLSNARLV LGVGGAAMLG IATLAVKRMY DRAISAPTSP
     TRLSHSGKRS WEEPNWMGSP RLLNKDMKAG LSRSLQTLPT DSSAFDTDTF CPPRPKPLAR
     RGQVDLKKSR LRMSLQEKLL SYYRNRAAIP AGEQARAKQA AVDICAELRS FLRAKLPDMP
     LRDMYLSGSL YDDLQVVTAD HIQLIVPLVL EQNLWSCIPG EDTIMNVPGF FLVRRENPEY
     FPRGSSYWDR CVVGGYLSPK TVADTFEKVV AGSINWPAIG SLLDYVIRPA PPPEALTLEV
     QYEKDKHLVI DFLPSVTLGD TVLVARPHRL AQYDNLWRLS LRPAETARLR ALDQADSGCR
     SLCLKILKAI CKSTPALGHL TASQLTNVIL HLAQEEADWS PDMLADRFLQ ALRGLISYLE
     AGVLPSALNP KVNLFAELTP QEIDELGYTL YCSLSEPEVL LQT
//
ID   OPA1L_MOUSE             Reviewed;         348 AA.
AC   Q8BGW2; Q3TF48; Q3U3M2; Q6PD43; Q8R0W8;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 56.
DE   RecName: Full=Outcome predictor in acute leukemia 1 homolog;
GN   Name=Opal1; Synonyms=D19Wsu162e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic gonad, Heart, Kidney, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=FVB/N; TISSUE=Brain, and Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8BGW2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BGW2-2; Sequence=VSP_019444;
CC       Name=3;
CC         IsoId=Q8BGW2-3; Sequence=VSP_019442;
CC       Name=4;
CC         IsoId=Q8BGW2-4; Sequence=VSP_019443;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH26369.1; Type=Erroneous initiation;
CC       Sequence=AAH58949.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK052400; BAC34974.1; -; mRNA.
DR   EMBL; AK078491; BAC37305.1; -; mRNA.
DR   EMBL; AK142695; BAE25164.1; -; mRNA.
DR   EMBL; AK154686; BAE32763.1; -; mRNA.
DR   EMBL; AK169294; BAE41050.1; -; mRNA.
DR   EMBL; BC026369; AAH26369.1; ALT_INIT; mRNA.
DR   EMBL; BC058949; AAH58949.1; ALT_INIT; mRNA.
DR   IPI; IPI00153302; -.
DR   IPI; IPI00762048; -.
DR   IPI; IPI00762733; -.
DR   IPI; IPI00762882; -.
DR   RefSeq; NP_001171283.1; NM_001177812.1.
DR   RefSeq; NP_001171284.1; NM_001177813.1.
DR   RefSeq; NP_666211.3; NM_146099.3.
DR   UniGene; Mm.329895; -.
DR   PRIDE; Q8BGW2; -.
DR   Ensembl; ENSMUST00000059990; ENSMUSP00000057161; ENSMUSG00000047731.
DR   Ensembl; ENSMUST00000099376; ENSMUSP00000096975; ENSMUSG00000047731.
DR   Ensembl; ENSMUST00000111855; ENSMUSP00000107486; ENSMUSG00000047731.
DR   Ensembl; ENSMUST00000111856; ENSMUSP00000107487; ENSMUSG00000047731.
DR   GeneID; 226178; -.
DR   KEGG; mmu:226178; -.
DR   UCSC; uc008htw.1; mouse.
DR   UCSC; uc008htx.1; mouse.
DR   UCSC; uc008hty.1; mouse.
DR   UCSC; uc008htz.1; mouse.
DR   CTD; 226178; -.
DR   MGI; MGI:107577; D19Wsu162e.
DR   eggNOG; roNOG07470; -.
DR   GeneTree; ENSGT00530000063663; -.
DR   HOVERGEN; HBG106189; -.
DR   OMA; YLLPPYE; -.
DR   NextBio; 378048; -.
DR   ArrayExpress; Q8BGW2; -.
DR   Bgee; Q8BGW2; -.
DR   Genevestigator; Q8BGW2; -.
DR   GermOnline; ENSMUSG00000047731; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR021684; Uncharacterised_WW-bd.
DR   Pfam; PF11669; WBP-1; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    348       Outcome predictor in acute leukemia 1
FT                                homolog.
FT                                /FTId=PRO_0000241451.
FT   TRANSMEM     42     62       Helical; (Potential).
FT   COMPBIAS    101    187       Pro-rich.
FT   VAR_SEQ       1     44       MPFLWGLRQDKEACVGTNNQSYICDTGHCCGQSQCCNYYYE
FT                                LWW -> MNSGVSPCPGGSWHPRVPVTASAPWETAGWPAFS
FT                                DSLGDSVG (in isoform 2).
FT                                /FTId=VSP_019444.
FT   VAR_SEQ       1      8       MPFLWGLR -> MERRRLLGGMALLLLQALPSPLSVRAEPP
FT                                (in isoform 3).
FT                                /FTId=VSP_019442.
FT   VAR_SEQ       1      8       MPFLWGLR -> MERRRLLGGMALLLLQALPSPLSVRAEPP
FT                                QVRLRSQKTVGLVRAY (in isoform 4).
FT                                /FTId=VSP_019443.
FT   CONFLICT    150    150       A -> T (in Ref. 2; AAH26369).
SQ   SEQUENCE   348 AA;  38347 MW;  68FCC6832E852998 CRC64;
     MPFLWGLRQD KEACVGTNNQ SYICDTGHCC GQSQCCNYYY ELWWFWLVWT VVIILSCCCV
     CHHRRAKHRL QAQQRQHEIN LIAYREAHNY SALPFYFRFL PNSLLPPYEE VVNRPPTPPP
     PYSAFQLQQQ QQLLPPPPQG GPPGGSPPGA DPPPQGSQGA QSSPLSGPSR SSTRPPSVAD
     PQSPEVPTDR EATKASGTES GSPMAGHGEL DPGAFLDQDS ECKEELLKDS RSERGGVSPD
     SEDKTPGRHR RFTGDSGIEV CVCNRGHHDD DLKEFNTLID DALDGPLDFC DSCHVRPPVD
     EEEGLCLSSE GQAREHGHPH LPRPPACLLL NTINEQDSPN SQHSGSPS
//
ID   SC5A7_MOUSE             Reviewed;         580 AA.
AC   Q8BGY9; Q99PK3; Q9ESW5;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=High affinity choline transporter 1;
DE   AltName: Full=Hemicholinium-3-sensitive choline transporter;
DE            Short=CHT;
DE   AltName: Full=Solute carrier family 5 member 7;
GN   Name=Slc5a7; Synonyms=Cht1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Spinal cord;
RX   PubMed=11709061; DOI=10.1042/0300-5127:0290711;
RA   Apparsundaram S., Ferguson S.M., Blakely R.D.;
RT   "Molecular cloning and characterization of a murine hemicholinium-3-
RT   sensitive choline transporter.";
RL   Biochem. Soc. Trans. 29:711-716(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ; TISSUE=Brain stem;
RA   Wieland A., Bonisch H., Bruess M.;
RT   "Molecular cloning of the human and murine high affinity choline
RT   transporters and characterization of the human gene structure.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon, and Embryonic head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Embryonic brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION BY PKC.
RC   TISSUE=Corpus striatum, and Hippocampus;
RX   PubMed=15064333; DOI=10.1124/jpet.104.066795;
RA   Gates J. Jr., Ferguson S.M., Blakely R.D., Apparsundaram S.;
RT   "Regulation of choline transporter surface expression and
RT   phosphorylation by protein kinase C and protein phosphatase 1/2A.";
RL   J. Pharmacol. Exp. Ther. 310:536-545(2004).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15173594; DOI=10.1073/pnas.0401667101;
RA   Ferguson S.M., Bazalakova M., Savchenko V., Tapia J.C., Wright J.,
RA   Blakely R.D.;
RT   "Lethal impairment of cholinergic neurotransmission in hemicholinium-
RT   3-sensitive choline transporter knockout mice.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:8762-8767(2004).
CC   -!- FUNCTION: Imports choline from the extracellular space to the
CC       neuron with high affinity. Rate-limiting step in acetylcholine
CC       synthesis. Sodium ion and chloride ion dependent.
CC   -!- INTERACTION:
CC       P51693:APLP1 (xeno); NbExp=1; IntAct=EBI-2010752, EBI-74648;
CC       Q06481:APLP2 (xeno); NbExp=1; IntAct=EBI-2010752, EBI-79306;
CC       P05067:APP (xeno); NbExp=1; IntAct=EBI-2010752, EBI-77613;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Found in spinal cord, brain-stem, mid-brain
CC       and striatum. Specific for cholinergic neurons.
CC   -!- PTM: Phosphorylated by PKC and dephosphorylated by PP1/PP2A.
CC   -!- DISRUPTION PHENOTYPE: Although morphologically normal at birth,
CC       knockout mice become immobile, breathe irregularly, appear
CC       cyanotic, and die within an hour. Mice had developmental changes
CC       in neuromuscular junction morphology reminiscent of changes in
CC       mutant mice lacking ACh synthesis.
CC   -!- MISCELLANEOUS: Specifically inhibited by nanomolar concentrations
CC       of hemicholinium 3.
CC   -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF)
CC       (TC 2.A.21) family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF276872; AAG36945.2; -; mRNA.
DR   EMBL; AJ401467; CAC03719.1; -; mRNA.
DR   EMBL; AK034415; BAC28702.1; -; mRNA.
DR   EMBL; AK053063; BAC35253.1; -; mRNA.
DR   EMBL; BC065089; AAH65089.1; -; mRNA.
DR   IPI; IPI00308200; -.
DR   RefSeq; NP_071308.2; NM_022025.4.
DR   UniGene; Mm.155241; -.
DR   ProteinModelPortal; Q8BGY9; -.
DR   DIP; DIP-46467N; -.
DR   IntAct; Q8BGY9; 4.
DR   STRING; Q8BGY9; -.
DR   PRIDE; Q8BGY9; -.
DR   Ensembl; ENSMUST00000071756; ENSMUSP00000071668; ENSMUSG00000023945.
DR   Ensembl; ENSMUST00000095712; ENSMUSP00000093379; ENSMUSG00000023945.
DR   GeneID; 63993; -.
DR   KEGG; mmu:63993; -.
DR   UCSC; uc008czx.1; mouse.
DR   CTD; 63993; -.
DR   MGI; MGI:1927126; Slc5a7.
DR   GeneTree; ENSGT00550000074437; -.
DR   HOGENOM; HBG383760; -.
DR   HOVERGEN; HBG054160; -.
DR   InParanoid; Q8BGY9; -.
DR   OMA; NICISYL; -.
DR   OrthoDB; EOG4PVNZB; -.
DR   PhylomeDB; Q8BGY9; -.
DR   NextBio; 319843; -.
DR   ArrayExpress; Q8BGY9; -.
DR   Bgee; Q8BGY9; -.
DR   Genevestigator; Q8BGY9; -.
DR   GermOnline; ENSMUSG00000023945; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; NAS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0008292; P:acetylcholine biosynthetic process; IMP:UniProtKB.
DR   GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:MGI.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; IMP:MGI.
DR   InterPro; IPR001734; Na/solute_symporter.
DR   PANTHER; PTHR11819; Na/solut_symport; 1.
DR   Pfam; PF00474; SSF; 1.
DR   PROSITE; PS00456; NA_SOLUT_SYMP_1; FALSE_NEG.
DR   PROSITE; PS00457; NA_SOLUT_SYMP_2; FALSE_NEG.
DR   PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Ion transport; Membrane; Neurotransmitter biosynthesis;
KW   Phosphoprotein; Sodium; Sodium transport; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    580       High affinity choline transporter 1.
FT                                /FTId=PRO_0000105392.
FT   TOPO_DOM      1      6       Cytoplasmic (Potential).
FT   TRANSMEM      7     27       Helical; (Potential).
FT   TOPO_DOM     28     48       Extracellular (Potential).
FT   TRANSMEM     49     69       Helical; (Potential).
FT   TOPO_DOM     70     81       Cytoplasmic (Potential).
FT   TRANSMEM     82    102       Helical; (Potential).
FT   TOPO_DOM    103    125       Extracellular (Potential).
FT   TRANSMEM    126    146       Helical; (Potential).
FT   TOPO_DOM    147    164       Cytoplasmic (Potential).
FT   TRANSMEM    165    185       Helical; (Potential).
FT   TOPO_DOM    186    191       Extracellular (Potential).
FT   TRANSMEM    192    212       Helical; (Potential).
FT   TOPO_DOM    213    237       Cytoplasmic (Potential).
FT   TRANSMEM    238    258       Helical; (Potential).
FT   TOPO_DOM    259    274       Extracellular (Potential).
FT   TRANSMEM    275    295       Helical; (Potential).
FT   TOPO_DOM    296    317       Cytoplasmic (Potential).
FT   TRANSMEM    318    338       Helical; (Potential).
FT   TOPO_DOM    339    376       Extracellular (Potential).
FT   TRANSMEM    377    397       Helical; (Potential).
FT   TOPO_DOM    398    406       Cytoplasmic (Potential).
FT   TRANSMEM    407    427       Helical; (Potential).
FT   TOPO_DOM    428    435       Extracellular (Potential).
FT   TRANSMEM    436    456       Helical; (Potential).
FT   TOPO_DOM    457    580       Cytoplasmic (Potential).
FT   CARBOHYD    371    371       N-linked (GlcNAc...) (Potential).
FT   CONFLICT      2      2       S -> P (in Ref. 1; AAG36945).
FT   CONFLICT     38     38       R -> H (in Ref. 2; CAC03719).
FT   CONFLICT     73     73       E -> V (in Ref. 2; CAC03719).
FT   CONFLICT     86     86       Q -> H (in Ref. 1; AAG36945).
FT   CONFLICT    119    119       Q -> K (in Ref. 1; AAG36945).
FT   CONFLICT    275    275       F -> Y (in Ref. 2; CAC03719).
SQ   SEQUENCE   580 AA;  63365 MW;  6154CE6622772A41 CRC64;
     MSFHVEGLVA IILFYLLIFL VGIWAAWKTK NSGNPEERSE AIIVGGRDIG LLVGGFTMTA
     TWVGGGYING TAEAVYGPGC GLAWAQAPIG YSLSLILGGL FFAKPMRSKG YVTMLDPFQQ
     IYGKRMGGLL FIPALMGEMF WAAAIFSALG ATISVIIDVD VNISVIVSAL IAILYTLVGG
     LYSVAYTDVV QLFCIFIGLW ISVPFALSHP AVTDIGFTAV HAKYQSPWLG TIESVEVYTW
     LDNFLLLMLG GIPWQAYFQR VLSSSSATYA QVLSFLAAFG CLVMALPAIC IGAIGASTDW
     NQTAYGYPDP KTKEEADMIL PIVLQYLCPV YISFFGLGAV SAAVMSSADS SILSASSMFA
     RNIYQLSFRQ NASDKEIVWV MRITVLVFGA SATAMALLTK TVYGLWYLSS DLVYIIIFPQ
     LLCVLFIKGT NTYGAVAGYI FGLFLRITGG EPYLYLQPLI FYPGYYSDKN GIYNQRFPFK
     TLSMVTSFFT NICVSYLAKY LFESGTLPPK LDVFDAVVAR HSEENMDKTI LVRNENIKLN
     ELAPVKPRQS LTLSSTFTNK EALLDVDSSP EGSGTEDNLQ
//
ID   CDC23_MOUSE             Reviewed;         597 AA.
AC   Q8BGZ4; Q6PD06; Q8C0F1;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2003, sequence version 2.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Cell division cycle protein 23 homolog;
DE   AltName: Full=Anaphase-promoting complex subunit 8;
DE            Short=APC8;
DE   AltName: Full=Cyclosome subunit 8;
GN   Name=Cdc23; Synonyms=Anapc8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Head, Hypothalamus, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-562 AND SER-578, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND THR-596, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC       (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls
CC       progression through mitosis and the G1 phase of the cell cycle.
CC       The APC/C complex acts by mediating ubiquitination and subsequent
CC       degradation of target proteins: it mainly mediates the formation
CC       of 'Lys-11'-linked polyubiquitin chains and, to a lower extent,
CC       the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin
CC       chains (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: The APC/C is composed of at least 12 subunits (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BGZ4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BGZ4-2; Sequence=VSP_037679;
CC   -!- PTM: Phosphorylated. Phosphorylation on Thr-562 occurs
CC       specifically during mitosis (By similarity).
CC   -!- SIMILARITY: Belongs to the APC8/CDC23 family.
CC   -!- SIMILARITY: Contains 9 TPR repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK031459; BAC27415.1; -; mRNA.
DR   EMBL; AK038523; BAC30026.1; -; mRNA.
DR   EMBL; AK048246; BAC33283.1; -; mRNA.
DR   EMBL; AK081461; BAC38224.1; -; mRNA.
DR   EMBL; BC059013; AAH59013.1; -; mRNA.
DR   IPI; IPI00221793; -.
DR   IPI; IPI00943370; -.
DR   RefSeq; NP_848124.1; NM_178347.4.
DR   UniGene; Mm.196638; -.
DR   ProteinModelPortal; Q8BGZ4; -.
DR   SMR; Q8BGZ4; 152-216, 231-543.
DR   STRING; Q8BGZ4; -.
DR   PhosphoSite; Q8BGZ4; -.
DR   PRIDE; Q8BGZ4; -.
DR   Ensembl; ENSMUST00000025228; ENSMUSP00000025228; ENSMUSG00000024370.
DR   GeneID; 52563; -.
DR   KEGG; mmu:52563; -.
DR   UCSC; uc008elb.1; mouse.
DR   CTD; 52563; -.
DR   MGI; MGI:1098815; Cdc23.
DR   GeneTree; ENSGT00550000074886; -.
DR   HOGENOM; HBG323794; -.
DR   HOVERGEN; HBG050858; -.
DR   InParanoid; Q8BGZ4; -.
DR   OrthoDB; EOG4J9MZH; -.
DR   PhylomeDB; Q8BGZ4; -.
DR   ArrayExpress; Q8BGZ4; -.
DR   Bgee; Q8BGZ4; -.
DR   CleanEx; MM_CDC23; -.
DR   Genevestigator; Q8BGZ4; -.
DR   GermOnline; ENSMUSG00000024370; Mus musculus.
DR   GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IEA:InterPro.
DR   InterPro; IPR007192; APC8.
DR   InterPro; IPR001440; TPR-1.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR008490; Transposase_InsH_N.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 3.
DR   Pfam; PF04049; APC8; 1.
DR   Pfam; PF05598; DUF772; 1.
DR   Pfam; PF00515; TPR_1; 2.
DR   SMART; SM00028; TPR; 6.
DR   PROSITE; PS50005; TPR; 6.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell cycle; Cell division; Mitosis;
KW   Phosphoprotein; Repeat; TPR repeat; Ubl conjugation pathway.
FT   CHAIN         1    597       Cell division cycle protein 23 homolog.
FT                                /FTId=PRO_0000106271.
FT   REPEAT       83    116       TPR 1.
FT   REPEAT      169    202       TPR 2.
FT   REPEAT      228    261       TPR 3.
FT   REPEAT      263    296       TPR 4.
FT   REPEAT      331    364       TPR 5.
FT   REPEAT      366    398       TPR 6.
FT   REPEAT      400    432       TPR 7.
FT   REPEAT      433    466       TPR 8.
FT   REPEAT      468    500       TPR 9.
FT   MOD_RES     273    273       Phosphotyrosine (By similarity).
FT   MOD_RES     467    467       N6-acetyllysine (By similarity).
FT   MOD_RES     562    562       Phosphothreonine.
FT   MOD_RES     576    576       Phosphoserine (By similarity).
FT   MOD_RES     578    578       Phosphoserine.
FT   MOD_RES     582    582       Phosphothreonine (By similarity).
FT   MOD_RES     584    584       Phosphothreonine (By similarity).
FT   MOD_RES     588    588       Phosphoserine.
FT   MOD_RES     593    593       Phosphoserine (By similarity).
FT   MOD_RES     596    596       Phosphothreonine.
FT   VAR_SEQ       1    118       Missing (in isoform 2).
FT                                /FTId=VSP_037679.
FT   CONFLICT    468    468       K -> M (in Ref. 1; BAC27415 and 2;
FT                                AAH59013).
SQ   SEQUENCE   597 AA;  68562 MW;  B1BF1D878CB531CE CRC64;
     MAANSSVVSV AAAATAVPGV STVADFSDLQ EIKKQLLLIA GLTRERGLLH SSKWSAELAF
     SLPALPLSEL QPPPPLTEED AQDVDAYTLA KAYFDVKEYD RAAHFLHGCN SKKAYFLYMY
     SRYLSGEKKK DDETVDSLGP LEKGQVKNEA LRELRVELSR KHQARGLDGF GLYLYGVVLR
     KLDLVKEAID VFVEATHVLP LHWGAWLELC NLITDKEMLK FLSLPDTWMK EFFLAHIYTE
     LQLIEEALQK YQHLIDVGFS KSSYIVSQIA VAYHNIRDID KALSIFNELR KQDPYRIENM
     DTFSNLLYVR SMKSELSYLA HNLCEIDKYR VETCCVIGNY YSLRSQHEKA ALYFQRALKL
     NPRYLGAWTL MGHEYMEMKN TSAAIQAYRH AIEVNKRDYR AWYGLGQTYE ILKMPFYCLY
     YYRRAHQLRP NDSRMLVALG ECYEKLNQLV EAKKCYWRAY AVGDVEKKAL VKLAKLHEQL
     TESEQAAQCY IKYIQDIYSC GETVEHLEES TAFRYLAQYY FKCKLWDEAS TCAQKCCAFN
     DTREEGKALL RQILQLRNQG ETPTSDTPGT FFLPASLSAN NTPTRRVSPL NLSSVTP
//
ID   PCKGM_MOUSE             Reviewed;         640 AA.
AC   Q8BH04; Q8BMM9; Q91Z10;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Phosphoenolpyruvate carboxykinase [GTP], mitochondrial;
DE            Short=PEPCK-M;
DE            EC=4.1.1.32;
DE   AltName: Full=Phosphoenolpyruvate carboxylase;
DE   Flags: Precursor;
GN   Name=Pck2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pituitary, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Catalyzes the conversion of oxaloacetate (OAA) to
CC       phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic
CC       pathway that produces glucose from lactate and other precursors
CC       derived from the citric acid cycle (By similarity).
CC   -!- CATALYTIC ACTIVITY: GTP + oxaloacetate = GDP + phosphoenolpyruvate
CC       + CO(2).
CC   -!- COFACTOR: Manganese (By similarity).
CC   -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity).
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- MISCELLANEOUS: In eukaryotes there are two isozymes: a cytoplasmic
CC       one and a mitochondrial one.
CC   -!- SIMILARITY: Belongs to the phosphoenolpyruvate carboxykinase [GTP]
CC       family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC26991.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK030501; BAC26991.1; ALT_INIT; mRNA.
DR   EMBL; AK031612; BAC27477.1; -; mRNA.
DR   EMBL; AK034927; BAC28883.1; -; mRNA.
DR   EMBL; BC010318; AAH10318.1; -; mRNA.
DR   IPI; IPI00223060; -.
DR   RefSeq; NP_083270.1; NM_028994.2.
DR   UniGene; Mm.480341; -.
DR   ProteinModelPortal; Q8BH04; -.
DR   SMR; Q8BH04; 32-640.
DR   STRING; Q8BH04; -.
DR   PhosphoSite; Q8BH04; -.
DR   PRIDE; Q8BH04; -.
DR   Ensembl; ENSMUST00000048781; ENSMUSP00000038555; ENSMUSG00000040618.
DR   GeneID; 74551; -.
DR   KEGG; mmu:74551; -.
DR   NMPDR; fig|10090.3.peg.29102; -.
DR   UCSC; uc007tyy.1; mouse.
DR   CTD; 74551; -.
DR   MGI; MGI:1860456; Pck2.
DR   HOGENOM; HBG484437; -.
DR   HOVERGEN; HBG053651; -.
DR   InParanoid; Q8BH04; -.
DR   OrthoDB; EOG47SSD8; -.
DR   BRENDA; 4.1.1.32; 244.
DR   NextBio; 341064; -.
DR   ArrayExpress; Q8BH04; -.
DR   Bgee; Q8BH04; -.
DR   Genevestigator; Q8BH04; -.
DR   GermOnline; ENSMUSG00000040618; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004613; F:phosphoenolpyruvate carboxykinase (GTP) activity; IEA:EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR018091; PEP_carboxykin_GTP_CS.
DR   InterPro; IPR013035; PEP_carboxykinase_C.
DR   InterPro; IPR008209; PEP_carboxykinase_GTP.
DR   InterPro; IPR008210; PEP_carboxykinase_N.
DR   Gene3D; G3DSA:3.90.228.20; PEP_carboxykinase_C; 2.
DR   Gene3D; G3DSA:3.40.449.10; PEP_carboxykinase_N; 1.
DR   PANTHER; PTHR11561; PEP_carboxykin; 1.
DR   Pfam; PF00821; PEPCK; 1.
DR   PIRSF; PIRSF001348; PEP_carboxykinase_GTP; 1.
DR   SUPFAM; SSF68923; PEP_carboxykinase_N; 1.
DR   PROSITE; PS00505; PEPCK_GTP; 1.
PE   2: Evidence at transcript level;
KW   Decarboxylase; Gluconeogenesis; GTP-binding; Lyase; Manganese;
KW   Metal-binding; Mitochondrion; Nucleotide-binding; Transit peptide.
FT   TRANSIT       1     32       Mitochondrion (By similarity).
FT   CHAIN        33    640       Phosphoenolpyruvate carboxykinase [GTP],
FT                                mitochondrial.
FT                                /FTId=PRO_0000023569.
FT   NP_BIND     305    310       GTP (By similarity).
FT   NP_BIND     548    551       GTP (By similarity).
FT   REGION      421    423       Substrate binding (By similarity).
FT   ACT_SITE    306    306       By similarity.
FT   METAL       262    262       Manganese (By similarity).
FT   METAL       282    282       Manganese (By similarity).
FT   METAL       329    329       Manganese (By similarity).
FT   BINDING     104    104       Substrate (By similarity).
FT   BINDING     255    255       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING     262    262       Substrate (By similarity).
FT   BINDING     304    304       Substrate (By similarity).
FT   BINDING     423    423       GTP (By similarity).
FT   BINDING     454    454       GTP (By similarity).
FT   CONFLICT     31     31       H -> R (in Ref. 2; AAH10318).
FT   CONFLICT    542    542       R -> C (in Ref. 2; AAH10318).
SQ   SEQUENCE   640 AA;  70528 MW;  5CE06D4DF5BBF44E CRC64;
     MAAMYLPGLR LSRHGLRPWC WSPCRSIQTL HVLSGDMSQL PAGVRDFVAR SAHLCQPEGI
     HICDGTEAEN TAILALLEEQ GLIRKLPKYK NCWLARTDPK DVARVESKTV IVTPSQRDTV
     PLLAGGARGQ LGNWMSPDEF QRAVDERFPG CMQGRIMYVL PFSMGPVGSP LSRIGVQLTD
     SAYVVASMRI MTRLGTPVLQ ALGDGDFIKC LHSVGQPLTG HGDPVGQWPC NPEKTLIGHV
     PDQREIVSFG SGYGGNSLLG KKCFALRIAS RLARDEGWLA EHMLILGITN PAGKKRYVAA
     AFPSACGKTN LAMMRPALPG WKVECVGDDI AWMRFDSEGQ LRAINPENGF FGVAPGTSAA
     TNPNAMATIQ SNTLFTNVAE TSDGGVYWEG IDQPLPPGVT ITSWLGKPWK PGDKEPCAHP
     NSRFCVPARQ CPIMDPAWEA PEGVPIDAII FGGRRPKGVP LVYEAFNWRH GVFVGSAMRS
     ESTAAAEHKG KTIMHDPFAM RPFFGYNFGR YLEHWLSMEG QKGARLPRIF HVNWFRRDEA
     GRFLWPGFGE NARVLDWICR RLEGEDSAQE TPIGLVPKEG ALDLSGLSAV DTSQLFSIPK
     DFWEQEVRDI RGYLTEQVNQ DLPKEVLAEL EALEGRVQKM
//
ID   ORAI2_MOUSE             Reviewed;         250 AA.
AC   Q8BH10; Q8C953;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Protein orai-2;
DE   AltName: Full=Transmembrane protein 142B;
GN   Name=Orai2; Synonyms=Tmem142b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Ca(2+) release-activated Ca(2+)-like (CRAC-like) channel
CC       subunit which mediates Ca(2+) influx and increase in Ca(2+)-
CC       selective current by synergy with the Ca(2+) sensor, STIM1 (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with EFCAB4B/CRACR2A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the Orai family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC31410.1; Type=Frameshift; Positions=9;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK036013; BAC29276.1; -; mRNA.
DR   EMBL; AK042940; BAC31410.1; ALT_FRAME; mRNA.
DR   EMBL; AK079619; BAC37704.1; -; mRNA.
DR   EMBL; BC066070; AAH66070.1; -; mRNA.
DR   IPI; IPI00758107; -.
DR   RefSeq; NP_848866.2; NM_178751.3.
DR   UniGene; Mm.308396; -.
DR   ProteinModelPortal; Q8BH10; -.
DR   STRING; Q8BH10; -.
DR   TCDB; 1.A.52.1.3; Ca2+ release-activated Ca2+ (CRAC) channel (CRAC-C) family.
DR   PRIDE; Q8BH10; -.
DR   Ensembl; ENSMUST00000041048; ENSMUSP00000037137; ENSMUSG00000039747.
DR   GeneID; 269717; -.
DR   KEGG; mmu:269717; -.
DR   UCSC; uc009aad.1; mouse.
DR   CTD; 269717; -.
DR   MGI; MGI:2443195; Orai2.
DR   GeneTree; ENSGT00390000015354; -.
DR   HOVERGEN; HBG081343; -.
DR   InParanoid; Q8BH10; -.
DR   OMA; PACSEPG; -.
DR   OrthoDB; EOG4DV5MR; -.
DR   PhylomeDB; Q8BH10; -.
DR   NextBio; 393011; -.
DR   ArrayExpress; Q8BH10; -.
DR   Bgee; Q8BH10; -.
DR   Genevestigator; Q8BH10; -.
DR   GermOnline; ENSMUSG00000039747; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR012446; DUF1650.
DR   Pfam; PF07856; DUF1650; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    250       Protein orai-2.
FT                                /FTId=PRO_0000234392.
FT   TRANSMEM     66     83       Helical; (Potential).
FT   TRANSMEM     94    114       Helical; (Potential).
FT   TRANSMEM    148    168       Helical; (Potential).
FT   TRANSMEM    192    212       Helical; (Potential).
SQ   SEQUENCE   250 AA;  28199 MW;  5B9F804800844911 CRC64;
     MSAELNVPMD PSAPACPEPG HKGMDYRDWV RRSYLELVTS NHHSVQALSW RKLYLSRAKL
     KASSRTSALL SGFAMVAMVE VQLETKYQYP QPLLIAFSAC TTVLVAVHLF ALLISTCILP
     NVEAVSNIHN LNSISESPHE RMHPYIELAW GFSTVLGILL FLAEVVLLCW IKFLPVDAKD
     QPGSHSHTGW QAALVSTIIM VPVGLIFVVF TIHFYRSLVR HKTERHNREI EELHKLKVQL
     DGHERSLQVV
//
ID   MFSD8_MOUSE             Reviewed;         519 AA.
AC   Q8BH31; Q91VS1; Q9CZ06;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Major facilitator superfamily domain-containing protein 8;
GN   Name=Mfsd8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-519.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be a carrier that transport small solutes by using
CC       chemiosmotic ion gradients (Potential).
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK013144; BAB28676.1; -; mRNA.
DR   EMBL; AK032080; BAC27687.1; -; mRNA.
DR   EMBL; AK077957; BAC37083.1; -; mRNA.
DR   EMBL; BC010483; AAH10483.1; -; mRNA.
DR   EMBL; BC113183; AAI13184.1; -; mRNA.
DR   EMBL; BC113790; AAI13791.1; -; mRNA.
DR   IPI; IPI00308132; -.
DR   RefSeq; NP_082416.2; NM_028140.4.
DR   UniGene; Mm.130610; -.
DR   ProteinModelPortal; Q8BH31; -.
DR   STRING; Q8BH31; -.
DR   PhosphoSite; Q8BH31; -.
DR   PRIDE; Q8BH31; -.
DR   Ensembl; ENSMUST00000026859; ENSMUSP00000026859; ENSMUSG00000025759.
DR   GeneID; 72175; -.
DR   KEGG; mmu:72175; -.
DR   UCSC; uc008pbp.1; mouse.
DR   CTD; 72175; -.
DR   MGI; MGI:1919425; Mfsd8.
DR   eggNOG; roNOG10407; -.
DR   GeneTree; ENSGT00530000063854; -.
DR   HOGENOM; HBG443861; -.
DR   HOVERGEN; HBG061584; -.
DR   InParanoid; Q8BH31; -.
DR   OMA; YYMLVAR; -.
DR   OrthoDB; EOG40CHH4; -.
DR   PhylomeDB; Q8BH31; -.
DR   NextBio; 335627; -.
DR   ArrayExpress; Q8BH31; -.
DR   Bgee; Q8BH31; -.
DR   CleanEx; MM_MFSD8; -.
DR   Genevestigator; Q8BH31; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR020846; Major_facilitator_SF.
DR   InterPro; IPR011701; MFS_1.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   2: Evidence at transcript level;
KW   Lysosome; Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    519       Major facilitator superfamily domain-
FT                                containing protein 8.
FT                                /FTId=PRO_0000311233.
FT   TOPO_DOM      1     41       Cytoplasmic (Potential).
FT   TRANSMEM     42     62       Helical; (Potential).
FT   TOPO_DOM     63     75       Extracellular (Potential).
FT   TRANSMEM     76     96       Helical; (Potential).
FT   TOPO_DOM     97    106       Cytoplasmic (Potential).
FT   TRANSMEM    107    127       Helical; (Potential).
FT   TOPO_DOM    128    140       Extracellular (Potential).
FT   TRANSMEM    141    161       Helical; (Potential).
FT   TOPO_DOM    162    174       Cytoplasmic (Potential).
FT   TRANSMEM    175    195       Helical; (Potential).
FT   TOPO_DOM    196    212       Extracellular (Potential).
FT   TRANSMEM    213    233       Helical; (Potential).
FT   TOPO_DOM    234    267       Cytoplasmic (Potential).
FT   TRANSMEM    268    288       Helical; (Potential).
FT   TOPO_DOM    289    310       Extracellular (Potential).
FT   TRANSMEM    311    331       Helical; (Potential).
FT   TOPO_DOM    332    338       Cytoplasmic (Potential).
FT   TRANSMEM    339    359       Helical; (Potential).
FT   TOPO_DOM    360    416       Extracellular (Potential).
FT   TRANSMEM    417    439       Helical; (Potential).
FT   TOPO_DOM    440    452       Cytoplasmic (Potential).
FT   TRANSMEM    453    473       Helical; (Potential).
FT   TOPO_DOM    474    483       Extracellular (Potential).
FT   TRANSMEM    484    504       Helical; (Potential).
FT   TOPO_DOM    505    519       Cytoplasmic (Potential).
FT   CONFLICT     25     25       S -> G (in Ref. 2; AAH10483).
FT   CONFLICT     39     39       S -> F (in Ref. 1; BAB28676).
FT   CONFLICT     50     50       S -> N (in Ref. 1; BAB28676).
FT   CONFLICT    116    116       V -> G (in Ref. 1; BAB28676).
FT   CONFLICT    129    129       A -> T (in Ref. 1; BAB28676).
FT   CONFLICT    313    313       L -> F (in Ref. 2; AAH10483).
FT   CONFLICT    391    391       S -> P (in Ref. 2; AAH10483).
SQ   SEQUENCE   519 AA;  57569 MW;  552FF574371BE4FE CRC64;
     MANLGSEAER EPLLGPGSPG SREWSEIETQ EHYKSRWKSV RILYLTMFLS SVGFSIVIMS
     IWPYLQKIDQ TADASFLGWV IASYSLGQMV ASPLFGLWSN YRPRKEPLIV SISISVAANC
     LYAYVHVPAA HNKYYMLIAR GLVGFGAGNV AVVRSYIAGA TSLQERTNAM ANTSTCQALG
     FILGPVFQTC FALIGEKGVT WDIIKLQVNM YTAPVLLAAF LGILNIILIL FILREHRVDD
     LGRQCKSVNF QEENTDEPQI PEGSIDQVAV VATNIVFFVV LFIFAVYETI LTPLTLDMYA
     WTQEQAVLYD GILLVAFGVE AVLVFMGVKL LSKKIGERAI LLGGFVVVWV GFFILLPWGN
     QFPKIQWEDL HNSSTPNTTF GEIIIGLWNS SREDHSEQPT GCPIEQTWCL YTPVIHLAQF
     LTAAVLIGTG YPACSVMSYT LYSKVLGPKP QGIYMGWLTT SGSAARILGP VFISHVYTYL
     GPRWAFSLVC GIVVLTILLI GAVYKRLVAF SVRYMRIQE
//
ID   COR2B_MOUSE             Reviewed;         480 AA.
AC   Q8BH44; Q6P5U9;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Coronin-2B;
GN   Name=Coro2b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in the reorganization of neuronal actin
CC       structure (By similarity).
CC   -!- SUBUNIT: Binds to F-actin and to vinculin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC   -!- SIMILARITY: Belongs to the WD repeat coronin family.
CC   -!- SIMILARITY: Contains 5 WD repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH62649.1; Type=Erroneous initiation;
CC       Sequence=BAC33080.1; Type=Erroneous initiation;
CC       Sequence=BAC39865.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK047527; BAC33080.1; ALT_INIT; mRNA.
DR   EMBL; AK087414; BAC39865.1; ALT_INIT; mRNA.
DR   EMBL; BC062649; AAH62649.1; ALT_INIT; mRNA.
DR   IPI; IPI00221725; -.
DR   RefSeq; NP_780693.2; NM_175484.3.
DR   UniGene; Mm.335229; -.
DR   ProteinModelPortal; Q8BH44; -.
DR   SMR; Q8BH44; 14-406.
DR   PRIDE; Q8BH44; -.
DR   Ensembl; ENSMUST00000048043; ENSMUSP00000041826; ENSMUSG00000041729.
DR   Ensembl; ENSMUST00000113985; ENSMUSP00000109618; ENSMUSG00000041729.
DR   GeneID; 235431; -.
DR   KEGG; mmu:235431; -.
DR   UCSC; uc009qaj.1; mouse.
DR   CTD; 235431; -.
DR   MGI; MGI:2444283; Coro2b.
DR   eggNOG; roNOG14438; -.
DR   GeneTree; ENSGT00550000074317; -.
DR   HOGENOM; HBG735393; -.
DR   HOVERGEN; HBG059978; -.
DR   InParanoid; Q8BH44; -.
DR   OMA; REHCFDG; -.
DR   OrthoDB; EOG45QHD0; -.
DR   PhylomeDB; Q8BH44; -.
DR   NextBio; 382660; -.
DR   ArrayExpress; Q8BH44; -.
DR   Bgee; Q8BH44; -.
DR   CleanEx; MM_CORO2B; -.
DR   Genevestigator; Q8BH44; -.
DR   GermOnline; ENSMUSG00000041729; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR015505; Coronin.
DR   InterPro; IPR015048; DUF1899.
DR   InterPro; IPR015049; DUF1900.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   PANTHER; PTHR10856; Coronin; 1.
DR   Pfam; PF08953; DUF1899; 1.
DR   Pfam; PF08954; DUF1900; 1.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton; Repeat;
KW   WD repeat.
FT   CHAIN         1    480       Coronin-2B.
FT                                /FTId=PRO_0000050931.
FT   REPEAT       85    125       WD 1.
FT   REPEAT      135    177       WD 2.
FT   REPEAT      179    217       WD 3.
FT   REPEAT      220    263       WD 4.
FT   REPEAT      265    308       WD 5.
FT   COILED      436    479       Potential.
FT   CONFLICT    203    203       K -> N (in Ref. 2; AAH62649).
SQ   SEQUENCE   480 AA;  54936 MW;  DD3D9E9C12EF41FE CRC64;
     MTVTKMSWRP QYRSSKFRNV YGKAANREHC FDGIPITKNV HDNHFCAVNA RFLAIVTESA
     GGGSFLVIPL EQTGRIEPNY PKVCGHQGNV LDIKWNPFID NIIASCSEDT SVRIWEIPDG
     GLKRNMTEAL LELHGHSRRV GLVEWHPTTN NILFSAGYDY KVLIWNLDIG EPVKMIDCHT
     DVILCMSFNT DGSLLTTTCK DKKLRVIEPR SGRVLQEANC KNHRVNRVVF LGNMKRLLTT
     GVSRWNTRQI ALWDQEDLSM PMIEEEIDGL SGLLFPFYDA DTHMLYLAGK GDGNIRYYEI
     STEKPYLSYL MEFRSPAPQK GLGVMPKHGL DVSACEVFRF YKLVTLKGLI EPISMIVPRR
     SDSYQEDIYP MTPGTEPALT PDEWLGGINR DPVLMSLKEG YKKSSKVVFK APIREKKSVV
     VNGIDLLENV PPRTENELLR MFFRQQDEIR RLKEELAQKD IRLRQLQLEL KNLRNNPKNC
//
ID   UBAP1_MOUSE             Reviewed;         502 AA.
AC   Q8BH48; Q8BQ80; Q8BSW6; Q9D749; Q9ERV5;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Ubiquitin-associated protein 1;
DE            Short=UBAP-1;
GN   Name=Ubap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   MEDLINE=21485291; PubMed=11599797; DOI=10.1007/s004320100252;
RA   Qian J., Yang J., Zhang X., Zhang B., Wang J., Zhou M., Tang K.,
RA   Li W., Zeng Z., Zhao X., Shen S., Li G.;
RT   "Isolation and characterization of a novel cDNA, UBAP1, derived from
RT   the tumor suppressor locus in human chromosome 9p21-22.";
RL   J. Cancer Res. Clin. Oncol. 127:613-618(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryo, Pituitary, Skin, Spinal ganglion, Testis, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 246-251, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BH48-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BH48-2; Sequence=VSP_013651;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in heart, liver,
CC       brain, kidney, spleen, skeletal muscle, stomach, testis and lung.
CC   -!- SIMILARITY: Contains 2 UBA domains.
CC   -!- SIMILARITY: Contains 1 UMA domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG09810.3; Type=Frameshift; Positions=440, 464;
CC       Sequence=BAC26927.1; Type=Frameshift; Positions=483;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF275549; AAG09810.3; ALT_FRAME; mRNA.
DR   EMBL; AK028477; BAC25970.1; -; mRNA.
DR   EMBL; AK028670; BAC26057.1; -; mRNA.
DR   EMBL; AK009596; BAB26382.1; -; mRNA.
DR   EMBL; AK030370; BAC26927.1; ALT_FRAME; mRNA.
DR   EMBL; AK033121; BAC28160.1; -; mRNA.
DR   EMBL; AK051346; BAC34609.1; -; mRNA.
DR   EMBL; AK076078; BAC36165.1; -; mRNA.
DR   EMBL; BC065996; AAH65996.1; -; mRNA.
DR   IPI; IPI00109614; -.
DR   IPI; IPI00224859; -.
DR   RefSeq; NP_075794.3; NM_023305.3.
DR   UniGene; Mm.289795; -.
DR   ProteinModelPortal; Q8BH48; -.
DR   SMR; Q8BH48; 381-430, 462-498.
DR   PhosphoSite; Q8BH48; -.
DR   PRIDE; Q8BH48; -.
DR   Ensembl; ENSMUST00000072866; ENSMUSP00000072643; ENSMUSG00000028437.
DR   Ensembl; ENSMUST00000108060; ENSMUSP00000103695; ENSMUSG00000028437.
DR   GeneID; 67123; -.
DR   KEGG; mmu:67123; -.
DR   UCSC; uc008sin.1; mouse.
DR   CTD; 67123; -.
DR   MGI; MGI:2149543; Ubap1.
DR   GeneTree; ENSGT00390000008092; -.
DR   HOGENOM; HBG713196; -.
DR   HOVERGEN; HBG060426; -.
DR   InParanoid; Q8BH48; -.
DR   OMA; MSFSKTH; -.
DR   OrthoDB; EOG4J6RR9; -.
DR   NextBio; 323643; -.
DR   ArrayExpress; Q8BH48; -.
DR   Bgee; Q8BH48; -.
DR   CleanEx; MM_UBAP1; -.
DR   Genevestigator; Q8BH48; -.
DR   GermOnline; ENSMUSG00000028437; Mus musculus.
DR   InterPro; IPR009060; UBA-like.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   InterPro; IPR023340; UMA.
DR   SUPFAM; SSF46934; UBA_like; 1.
DR   PROSITE; PS50030; UBA; 2.
DR   PROSITE; PS51497; UMA; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing; Phosphoprotein;
KW   Repeat.
FT   CHAIN         1    502       Ubiquitin-associated protein 1.
FT                                /FTId=PRO_0000211018.
FT   DOMAIN       17     63       UMA.
FT   DOMAIN      389    430       UBA 1.
FT   DOMAIN      451    498       UBA 2.
FT   MOD_RES     205    205       Phosphoserine (By similarity).
FT   VAR_SEQ     362    422       Missing (in isoform 2).
FT                                /FTId=VSP_013651.
SQ   SEQUENCE   502 AA;  55028 MW;  4DE473D8AF0EA510 CRC64;
     MASKKLGTDV HGTFSYLDDV PFKIGDKFKT PAKVGLPIGF SLPDCLQVVR EMQYDFSLEK
     KTIEWAEDIK LIQEAQREAE RKAEEAEAKV NSKSGPEGDS KVSFPKTHNT ATMPPPINPI
     LASLQHNNIL TPTRVSSSAT KQKVLSPPHT KADFNPADFE CEEDPFDNLE LKTIDEKEEL
     RNILVGTTGP IMAQLLDSNT ARGSSGAVLQ DEEVLASLEQ ATLDFKPLHK PNGFITLPQL
     GNCEKMSLSS KVSLPPIPTV SNIKSLSFPK LDSDDSNQKT VKLASTFHST SCLRSGASRS
     LLKPSTQSSA SELNGDHTLG LSALNLNSGT EVPTLTSSQM PSLSSVSVCT EESSPPDPCP
     TVTPLNFSVS QVPNMPSCPQ AYLELQALSP SERQCVETVV NMGYSYDCVL RAMRKKGENI
     EQILDYLFAH GQLCEKGFDP LLVEEALEMH QCSEEKMMEF LQLMSKFKEM GFELKDIKEV
     LLLHNNDQDN ALEDLMARAG AS
//
ID   CR025_MOUSE             Reviewed;         245 AA.
AC   Q8BH50; Q3TQ72; Q8BU43;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Uncharacterized protein C18orf25 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BH50-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BH50-2; Sequence=VSP_014754, VSP_014755;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK033209; BAC28197.1; -; mRNA.
DR   EMBL; AK046785; BAC32868.1; -; mRNA.
DR   EMBL; AK087799; BAC40007.1; -; mRNA.
DR   EMBL; AK163840; BAE37513.1; -; mRNA.
DR   IPI; IPI00466384; -.
DR   IPI; IPI00874579; -.
DR   RefSeq; NP_848785.2; NM_178670.3.
DR   UniGene; Mm.158164; -.
DR   PRIDE; Q8BH50; -.
DR   Ensembl; ENSMUST00000074653; ENSMUSP00000074225; ENSMUSG00000047466.
DR   GeneID; 212163; -.
DR   KEGG; mmu:212163; -.
DR   UCSC; uc008frq.1; mouse.
DR   MGI; MGI:2444951; 8030462N17Rik.
DR   GeneTree; ENSGT00390000016167; -.
DR   HOVERGEN; HBG056975; -.
DR   InParanoid; Q8BH50; -.
DR   OrthoDB; EOG4CG08J; -.
DR   PhylomeDB; Q8BH50; -.
DR   NextBio; 373486; -.
DR   ArrayExpress; Q8BH50; -.
DR   Bgee; Q8BH50; -.
DR   CleanEx; MM_8030462N17RIK; -.
DR   Genevestigator; Q8BH50; -.
DR   GermOnline; ENSMUSG00000047466; Mus musculus.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Phosphoprotein.
FT   CHAIN         1    245       Uncharacterized protein C18orf25 homolog.
FT                                /FTId=PRO_0000079313.
FT   COILED      175    200       Potential.
FT   COMPBIAS    221    224       Poly-Asp.
FT   MOD_RES      39     39       Phosphoserine (By similarity).
FT   MOD_RES      66     66       Phosphoserine (By similarity).
FT   MOD_RES      69     69       Phosphoserine (By similarity).
FT   MOD_RES      76     76       Phosphoserine (By similarity).
FT   MOD_RES     145    145       Phosphoserine (By similarity).
FT   VAR_SEQ     160    162       SSD -> LQR (in isoform 2).
FT                                /FTId=VSP_014754.
FT   VAR_SEQ     163    245       Missing (in isoform 2).
FT                                /FTId=VSP_014755.
SQ   SEQUENCE   245 AA;  26446 MW;  4BFF251349BA3C8E CRC64;
     MKMEEAVGKV EELIESAAPP KASEQETAKE EDGSVELESQ VQKDGVADST VLSSMPCLLM
     ELRRDSSESQ LASTESDKPT TGRVYESDSS NHCMLSPSSS GHLADSDTLS SVEENEPSQA
     ETTVEGDTSG VSGATVGRKS RRSRSESETS TMAAKKNRQS SDKQNGRVTK VKGHRSQKHK
     ERIRLLRQKR EAAARKKYNL LQDSSTSDSD LTCDSSTSSS DDDDEVSGSS KTITAEIPGR
     GCFLN
//
ID   WDR48_MOUSE             Reviewed;         676 AA.
AC   Q8BH57; Q80TD4; Q80XI0; Q8BRM0; Q8CBK0; Q922Z9; Q9CRR1; Q9CSL0;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=WD repeat-containing protein 48;
DE   AltName: Full=USP1-associated factor 1;
GN   Name=Wdr48; Synonyms=Kiaa1449, Uaf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain cortex, Cecum, Cerebellum, Lung, Testis, and
RC   Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-28, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-338, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Regulator of deubiquitinating complexes. Acts as a
CC       strong activator of USP1 by enhancing the USP1-mediated
CC       deubiquitination of FANCD2; USP1 being almost inactive by itself.
CC       Also activates deubiquitinating activity of complexes containing
CC       USP12 and USP46, respectively. Activates deubiquitination by
CC       increasing the catalytic turnover without increasing the affinity
CC       of deubiquitinating enzymes for the substrate. May play a role in
CC       vesicular transport or membrane fusion events necessary for
CC       transport to lysosomes (By similarity).
CC   -!- SUBUNIT: Interacts with USP1, USP12 and USP46 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity). Lysosome (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BH57-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BH57-2; Sequence=VSP_016778;
CC       Name=3;
CC         IsoId=Q8BH57-3; Sequence=VSP_016779, VSP_016780;
CC   -!- DOMAIN: The WD repeats are required for the interaction with
CC       deubiquitinating enzymes USP1, USP12 and USP46 (By similarity).
CC   -!- SIMILARITY: Belongs to the WD repeat WDR48 family.
CC   -!- SIMILARITY: Contains 8 WD repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65793.3; Type=Erroneous initiation;
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DR   EMBL; AK122511; BAC65793.3; ALT_INIT; mRNA.
DR   EMBL; AK012599; BAB28345.1; -; mRNA.
DR   EMBL; AK018396; BAB31193.3; ALT_TERM; mRNA.
DR   EMBL; AK030041; BAC26755.1; -; mRNA.
DR   EMBL; AK033631; BAC28400.1; -; mRNA.
DR   EMBL; AK035273; BAC29010.1; -; mRNA.
DR   EMBL; AK035864; BAC29218.1; -; mRNA.
DR   EMBL; AK043970; BAC31719.1; -; mRNA.
DR   EMBL; BC006679; AAH06679.1; -; mRNA.
DR   EMBL; BC048155; AAH48155.1; -; mRNA.
DR   EMBL; BC062967; AAH62967.1; -; mRNA.
DR   IPI; IPI00336198; -.
DR   IPI; IPI00659186; -.
DR   IPI; IPI00677198; -.
DR   RefSeq; NP_080512.1; NM_026236.3.
DR   UniGene; Mm.104789; -.
DR   UniGene; Mm.473239; -.
DR   ProteinModelPortal; Q8BH57; -.
DR   SMR; Q8BH57; 27-389.
DR   STRING; Q8BH57; -.
DR   PhosphoSite; Q8BH57; -.
DR   PRIDE; Q8BH57; -.
DR   Ensembl; ENSMUST00000036561; ENSMUSP00000042509; ENSMUSG00000032512.
DR   GeneID; 67561; -.
DR   KEGG; mmu:67561; -.
DR   UCSC; uc009sbm.1; mouse.
DR   UCSC; uc009sbn.1; mouse.
DR   UCSC; uc009sbo.1; mouse.
DR   CTD; 67561; -.
DR   MGI; MGI:1914811; Wdr48.
DR   eggNOG; roNOG07830; -.
DR   GeneTree; ENSGT00520000055738; -.
DR   HOVERGEN; HBG079413; -.
DR   InParanoid; Q8BH57; -.
DR   OMA; QVSFVIR; -.
DR   OrthoDB; EOG4HHP1W; -.
DR   PhylomeDB; Q8BH57; -.
DR   NextBio; 324921; -.
DR   ArrayExpress; Q8BH57; -.
DR   Bgee; Q8BH57; -.
DR   CleanEx; MM_WDR48; -.
DR   Genevestigator; Q8BH57; -.
DR   GermOnline; ENSMUSG00000032512; Mus musculus.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR   InterPro; IPR021772; DUF3337.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
DR   Pfam; PF11816; DUF3337; 1.
DR   Pfam; PF00400; WD40; 6.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Lysosome; Nucleus;
KW   Phosphoprotein; Repeat; Ubl conjugation pathway; WD repeat.
FT   CHAIN         1    676       WD repeat-containing protein 48.
FT                                /FTId=PRO_0000051401.
FT   REPEAT       28     67       WD 1.
FT   REPEAT       73    112       WD 2.
FT   REPEAT      115    154       WD 3.
FT   REPEAT      166    205       WD 4.
FT   REPEAT      208    247       WD 5.
FT   REPEAT      250    289       WD 6.
FT   REPEAT      292    334       WD 7.
FT   REPEAT      358    397       WD 8.
FT   MOD_RES      28     28       Phosphotyrosine.
FT   MOD_RES     121    121       N6-acetyllysine (By similarity).
FT   MOD_RES     214    214       N6-acetyllysine (By similarity).
FT   MOD_RES     338    338       Phosphotyrosine.
FT   MOD_RES     578    578       N6-acetyllysine (By similarity).
FT   VAR_SEQ     414    427       Missing (in isoform 2).
FT                                /FTId=VSP_016778.
FT   VAR_SEQ     557    576       KNMPKFNKIPFYLQPHASSG -> VSVLHSHFVLCFSQTLS
FT                                LTL (in isoform 3).
FT                                /FTId=VSP_016779.
FT   VAR_SEQ     577    676       Missing (in isoform 3).
FT                                /FTId=VSP_016780.
FT   CONFLICT     85     85       C -> S (in Ref. 3; BAC29218).
FT   CONFLICT    238    238       S -> F (in Ref. 1; BAC65793).
FT   CONFLICT    642    642       C -> W (in Ref. 3; BAC31719).
SQ   SEQUENCE   676 AA;  76007 MW;  4996ED13D73DA235 CRC64;
     MAAHHRQNTA GRRKVQVSYV IRDEVEKYNR NGVNALQLDP ALNRLFTAGR DSIIRIWSVN
     QHKQDPYIAS MEHHTDWVND VVLCCNGKTL ISASSDTTVK VWNAHKGFCM STLRTHKDYV
     KALAYAKDKE LVASAGLDRQ IFLWDVNTLT ALTASNNTVT TSSLSGNKDS IYSLAMNQLG
     TIIVSGSTEK VLRVWDPRTC AKLMKLKGHT DNVKALLLHR DGTQCLSGSS DGTIRLWSLG
     QQRCIATYRV HDEGVWALQV NDAFTHVYSG GRDRKIYCTD LRNPDIRVLI CEEKAPVLKM
     ELDRSADPPP AIWVATTKST VNKWTLKGIH NFRASGDYDN DCTNPITPLC TQPDQVIKGG
     ASIIQCHILN DKRHILTKDT NNNVAYWDVL KACKVEDLGK VDFEDEIKKR FKMVYVPNWF
     SVDLKTGMLT ITLDESDCFA AWVSAKDAGF SSPDGSDPKL NLGGLLLQAL LEYWPRTHVT
     PMDEEENEVN HVSGGQESRV QKGNGYFQVP PHTPVIFGEA GGRTLFRLLC RDSGGETEAM
     LLNETVPQWV IDITVDKNMP KFNKIPFYLQ PHASSGAKTL KKDRLSASDM LQVRKVMEHV
     YEKIINLDNE SQTTSSSNNE KPEQEKEEDI AVLAEEKIEL LCQDQVLDPN MDLRTVKHFI
     WKSGGDLTLH YRQKST
//
ID   CMC1_MOUSE              Reviewed;         677 AA.
AC   Q8BH59; A2BFG0;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Calcium-binding mitochondrial carrier protein Aralar1;
DE   AltName: Full=Mitochondrial aspartate glutamate carrier 1;
DE   AltName: Full=Solute carrier family 25 member 12;
GN   Name=Slc25a12; Synonyms=Aralar1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, and Pituitary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 18-68; 144-163; 174-190; 234-243; 245-259;
RP   284-309; 330-351; 359-370; 382-403; 407-414; 454-482; 491-543;
RP   552-565; 570-578; 587-622; 625-659 AND 662-671.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Calcium-dependent mitochondrial aspartate and glutamate
CC       carrier. May have a function in the urea cycle (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- MISCELLANEOUS: Binds calcium (By similarity).
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier family.
CC   -!- SIMILARITY: Contains 4 EF-hand domains.
CC   -!- SIMILARITY: Contains 3 Solcar repeats.
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DR   EMBL; AK030595; BAC27037.1; -; mRNA.
DR   EMBL; AK083156; BAC38787.1; -; mRNA.
DR   EMBL; BX284624; CAM20071.1; -; Genomic_DNA.
DR   EMBL; BC060505; AAH60505.1; -; mRNA.
DR   IPI; IPI00308162; -.
DR   RefSeq; NP_766024.1; NM_172436.3.
DR   UniGene; Mm.146696; -.
DR   UniGene; Mm.30928; -.
DR   ProteinModelPortal; Q8BH59; -.
DR   SMR; Q8BH59; 16-220, 242-292, 329-601.
DR   STRING; Q8BH59; -.
DR   PRIDE; Q8BH59; -.
DR   Ensembl; ENSMUST00000151937; ENSMUSP00000122103; ENSMUSG00000027010.
DR   GeneID; 78830; -.
DR   KEGG; mmu:78830; -.
DR   NMPDR; fig|10090.3.peg.6124; -.
DR   UCSC; uc008kan.1; mouse.
DR   CTD; 78830; -.
DR   MGI; MGI:1926080; Slc25a12.
DR   GeneTree; ENSGT00530000062944; -.
DR   HOGENOM; HBG357440; -.
DR   HOVERGEN; HBG005350; -.
DR   InParanoid; Q8BH59; -.
DR   OMA; AQNAIRY; -.
DR   OrthoDB; EOG4BVRT4; -.
DR   PhylomeDB; Q8BH59; -.
DR   NextBio; 349608; -.
DR   ArrayExpress; Q8BH59; -.
DR   Bgee; Q8BH59; -.
DR   Genevestigator; Q8BH59; -.
DR   GermOnline; ENSMUSG00000027010; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0015183; F:L-aspartate transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0005313; F:L-glutamate transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0043490; P:malate-aspartate shuttle; ISS:UniProtKB.
DR   GO; GO:0051592; P:response to calcium ion; ISS:UniProtKB.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR002067; Mit_carrier.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00926; MITOCARRIER.
DR   SMART; SM00054; EFh; 3.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    677       Calcium-binding mitochondrial carrier
FT                                protein Aralar1.
FT                                /FTId=PRO_0000090599.
FT   TRANSMEM    330    347       Helical; Name=1; (Potential).
FT   TRANSMEM    391    410       Helical; Name=2; (Potential).
FT   TRANSMEM    434    447       Helical; Name=3; (Potential).
FT   TRANSMEM    483    502       Helical; Name=4; (Potential).
FT   TRANSMEM    522    539       Helical; Name=5; (Potential).
FT   TRANSMEM    579    598       Helical; Name=6; (Potential).
FT   DOMAIN       40     85       EF-hand 1.
FT   DOMAIN       86    121       EF-hand 2.
FT   DOMAIN      122    156       EF-hand 3.
FT   DOMAIN      157    192       EF-hand 4.
FT   REPEAT      324    416       Solcar 1.
FT   REPEAT      424    508       Solcar 2.
FT   REPEAT      516    604       Solcar 3.
FT   CA_BIND      65     76       1 (By similarity).
FT   CA_BIND      99    110       2 (By similarity).
FT   CA_BIND     170    181       3 (By similarity).
SQ   SEQUENCE   677 AA;  74570 MW;  488ABC7EB8227571 CRC64;
     MAVKVHTTKR GDPHELRNIF LQYASTEVDG EHYMTPEDFV QRYLGLYNDP NSNPKIVQLL
     AGVADQTKDG LISYQEFLAF ESVLCAPDSM FIVAFQLFDK SGNGEVTFEN VKEIFGQTII
     HHHIPFNWDC EFIRLHFGHN RKKHLNYVEF TQFLQELQLE HARQAFALKD KSKSGMISGL
     DFSDVMVTIR SHMLTPFVEE NLVSAAGGGT SHQVSFSYFN AFNSLLNNME LVRKIYSTLA
     GTRKDIEVTK EEFAQSAIRY GQVTPLEIDI LYQLADLYNA SGRLTLADIE RIAPLAEGAL
     PYNLAELQRQ QSPGLGRPIW LQIAESAYRF TLGSVAGAVG ATAVYPIDLV KTRMQNQRGT
     GSVVGELMYK NSFDCFKKVL RYEGFFGLYR GLIPQLIGVA PEKAIKLTVN DFVRDKFTKR
     DGSIPLPAEI LAGGCAGGSQ VIFTNPLEIV KIRLQVAGEI TTGPRVSALN VLQDLGLFGL
     YKGAKACFLR DIPFSAIYFP VYAHCKLLLA DENGRVGGIN LLTAGALAGV PAASLVTPAD
     VIKTRLQVAA RAGQTTYSGV VDCFRKILRE EGPSAFWKGT AARVFRSSPQ FGVTLVTYEL
     LQRWFYIDFG GLKPSGSEPT PKSRIADLPP ANPDHIGGYR LATATFAGIE NKFGLYLPKF
     KSPSVAVAQP KAAAAAQ
//
ID   EHD2_MOUSE              Reviewed;         543 AA.
AC   Q8BH64; Q8BL28;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=EH domain-containing protein 2;
GN   Name=Ehd2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH EHBP1,
RP   SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6;
RX   PubMed=14676205; DOI=10.1074/jbc.M307702200;
RA   Guilherme A., Soriano N.A., Bose S., Holik J., Bose A.,
RA   Pomerleau D.P., Furcinitti P., Leszyk J., Corvera S., Czech M.P.;
RT   "EHD2 and the novel EH domain binding protein EHBP1 couple endocytosis
RT   to the actin cytoskeleton.";
RL   J. Biol. Chem. 279:10593-10605(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Adipose tissue, Embryonic eye, Embryonic head, Embryonic lung,
RC   Forelimb, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   FUNCTION, INTERACTION WITH MYOF, MUTAGENESIS OF GLY-65, MASS
RP   SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX   PubMed=18502764; DOI=10.1074/jbc.M802306200;
RA   Doherty K.R., Demonbreun A.R., Wallace G.Q., Cave A., Posey A.D.,
RA   Heretis K., Pytel P., McNally E.M.;
RT   "The endocytic recycling protein EHD2 interacts with myoferlin to
RT   regulate myoblast fusion.";
RL   J. Biol. Chem. 283:20252-20260(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN COMPLEX WITH ATP ANALOG AND
RP   CALCIUM IONS, SUBUNIT, SUBCELLULAR LOCATION, ENZYME REGULATION, AND
RP   MUTAGENESIS OF THR-72; THR-94; ILE-157; ARG-167; PHE-322; LYS-324;
RP   LYS-327; LYS-328 AND LYS-329.
RX   PubMed=17914359; DOI=10.1038/nature06173;
RA   Daumke O., Lundmark R., Vallis Y., Martens S., Butler P.J.G.,
RA   McMahon H.T.;
RT   "Architectural and mechanistic insights into an EHD ATPase involved in
RT   membrane remodelling.";
RL   Nature 449:923-927(2007).
CC   -!- FUNCTION: Plays a role in membrane reorganization in response to
CC       nucleotide hydrolysis. Binds to liposomes and deforms them into
CC       tubules. Plays a role in membrane trafficking between the plasma
CC       membrane and endosomes. Important for the internalization of
CC       GLUT4. Required for normal fusion of myoblasts to skeletal muscle
CC       myotubes. Binds ATP; does not bind GTP.
CC   -!- ENZYME REGULATION: The very low intrinsic ATPase activity is
CC       increased upon interaction with liposomes.
CC   -!- SUBUNIT: Interacts with EHD1 and MYOF. May also interact with EHD3
CC       and EHD4 (By similarity). Interacts with Asn-Pro-Phe (NPF) motifs
CC       in target proteins. Homodimer and homooligomer. Interacts with
CC       MYOF and EHBP1.
CC   -!- INTERACTION:
CC       Q9NZM1:MYOF (xeno); NbExp=1; IntAct=EBI-1994334, EBI-1994363;
CC       Q69ZN7:Myof; NbExp=2; IntAct=EBI-1994334, EBI-1994301;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Endosome membrane; Peripheral membrane protein
CC       (By similarity). Note=Colocalizes with GLUT4 in intracellular
CC       tubulovesicular structures that are associated with cortical F-
CC       actin.
CC   -!- TISSUE SPECIFICITY: Detected in lung and adipocytes. Detected at
CC       lower levels in heart and skeletal muscle.
CC   -!- DOMAIN: The EH domain interacts with Asn-Pro-Phe (NPF) motifs of
CC       target proteins.
CC   -!- SIMILARITY: Contains 1 EF-hand domain.
CC   -!- SIMILARITY: Contains 1 EH domain.
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DR   EMBL; AY531389; AAS48536.1; -; mRNA.
DR   EMBL; AK031203; BAC27298.1; -; mRNA.
DR   EMBL; AK046566; BAC32789.1; -; mRNA.
DR   EMBL; AK048356; BAC33310.1; -; mRNA.
DR   EMBL; AK050243; BAC34142.1; -; mRNA.
DR   EMBL; AK084455; BAC39188.1; -; mRNA.
DR   EMBL; AK085016; BAC39339.1; -; mRNA.
DR   EMBL; BC113161; AAI13162.1; -; mRNA.
DR   IPI; IPI00402968; -.
DR   RefSeq; NP_694708.2; NM_153068.3.
DR   UniGene; Mm.138215; -.
DR   UniGene; Mm.438817; -.
DR   PDB; 2QPT; X-ray; 3.10 A; A=1-543.
DR   PDBsum; 2QPT; -.
DR   ProteinModelPortal; Q8BH64; -.
DR   SMR; Q8BH64; 19-538.
DR   IntAct; Q8BH64; 3.
DR   STRING; Q8BH64; -.
DR   PhosphoSite; Q8BH64; -.
DR   PRIDE; Q8BH64; -.
DR   Ensembl; ENSMUST00000098799; ENSMUSP00000096397; ENSMUSG00000074364.
DR   GeneID; 259300; -.
DR   KEGG; mmu:259300; -.
DR   UCSC; uc009fgt.1; mouse.
DR   CTD; 259300; -.
DR   MGI; MGI:2154274; Ehd2.
DR   HOGENOM; HBG317590; -.
DR   HOVERGEN; HBG018183; -.
DR   InParanoid; Q8BH64; -.
DR   OMA; RVHAHII; -.
DR   OrthoDB; EOG4V437F; -.
DR   NextBio; 392043; -.
DR   ArrayExpress; Q8BH64; -.
DR   Bgee; Q8BH64; -.
DR   CleanEx; MM_EHD2; -.
DR   Genevestigator; Q8BH64; -.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0019904; F:protein domain specific binding; IDA:MGI.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IDA:MGI.
DR   GO; GO:0006897; P:endocytosis; IDA:MGI.
DR   InterPro; IPR001401; Dynamin_GTPase.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR000261; EPS15_homology.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   SMART; SM00027; EH; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS50031; EH; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Calcium; Cell membrane; Endosome;
KW   Hydrolase; Membrane; Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1    543       EH domain-containing protein 2.
FT                                /FTId=PRO_0000322643.
FT   DOMAIN      449    537       EH.
FT   DOMAIN      481    516       EF-hand.
FT   NP_BIND      65     72       ATP.
FT   CA_BIND     494    505
FT   BINDING     220    220       ATP.
FT   BINDING     258    258       ATP.
FT   MOD_RES     438    438       Phosphoserine.
FT   MOD_RES     458    458       Phosphotyrosine (By similarity).
FT   MOD_RES     468    468       Phosphoserine.
FT   MUTAGEN      65     65       G->R: Inhibits myoblast fusion.
FT   MUTAGEN      72     72       T->A: Abolishes ATP binding.
FT   MUTAGEN      94     94       T->A: Abolishes increase of intrinsic
FT                                ATPase activity upon interaction with
FT                                membranes.
FT   MUTAGEN     157    157       I->Q: Increases intrinsic ATPase
FT                                activity.
FT   MUTAGEN     167    167       R->E: Increases intrinsic ATPase
FT                                activity.
FT   MUTAGEN     322    322       F->A: Abolishes localization at the
FT                                plasma membrane; reduces increase of
FT                                intrinsic ATPase activity upon
FT                                interaction with membranes.
FT   MUTAGEN     324    324       K->D: Abolishes localization at the
FT                                plasma membrane.
FT   MUTAGEN     327    327       K->D: Abolishes localization at the
FT                                plasma membrane; abolishes increase of
FT                                intrinsic ATPase activity upon
FT                                interaction with membranes.
FT   MUTAGEN     328    328       K->D: Abolishes localization at the
FT                                plasma membrane; reduces increase of
FT                                intrinsic ATPase activity upon
FT                                interaction with membranes.
FT   MUTAGEN     329    329       K->D: Abolishes localization at the
FT                                plasma membrane.
FT   CONFLICT    181    181       R -> S (in Ref. 2; BAC32789).
FT   HELIX        21     32
FT   HELIX        34     39
FT   TURN         53     55
FT   STRAND       60     64
FT   HELIX        72     79
FT   STRAND       96    101
FT   STRAND      136    140
FT   HELIX       144    148
FT   STRAND      150    153
FT   HELIX       171    181
FT   STRAND      183    190
FT   HELIX       198    203
FT   HELIX       211    213
FT   STRAND      214    219
FT   HELIX       221    223
FT   HELIX       226    232
FT   HELIX       236    239
FT   STRAND      258    260
FT   HELIX       268    282
FT   HELIX       286    288
FT   HELIX       289    317
FT   HELIX       325    333
FT   HELIX       335    344
FT   HELIX       356    365
FT   HELIX       368    370
FT   HELIX       376    401
FT   TURN        445    449
FT   HELIX       450    459
FT   HELIX       472    476
FT   TURN        483    485
FT   HELIX       489    493
FT   HELIX       503    517
FT   HELIX       528    530
SQ   SEQUENCE   543 AA;  61174 MW;  47637795B0B1096E CRC64;
     MFSWLKKGGA RGQRPEAIRT VTSSLKELYR TKLLPLEEHY RFGSFHSPAL EDADFDGKPM
     VLVAGQYSTG KTSFIQYLLE QEVPGSRVGP EPTTDCFVAV MHGETEGTVP GNALVVDPEK
     PFRKLNPFGN TFLNRFMCAQ LPNQVLESIS IIDTPGILSG AKQRVSRGYD FPAVLRWFAE
     RVDLIILLFD AHKLEISDEF SEAIGALRGH EDKIRVVLNK ADMVETQQLM RVYGALMWAL
     GKVVGTPEVL RVYIGSFWSQ PLLVPDNRRL FELEEQDLFR DIQGLPRHAA LRKLNDLVKR
     ARLVRVHAYI ISYLKKEMPT VFGKENKKKQ LILKLPVIFA KIQLEHHISP GDFPDCQKMQ
     ELLMAHDFTK FHSLKPKLLE ALDDMLAQDI AKLMPLLRQE ELESVEAGVQ GGAFEGTRMG
     PFVERGPDEA IEDGEEGSED DAEWVVTKDK SKYDEIFYNL APADGKLSGS KAKTWMVGTK
     LPNSVLGRIW KLSDVDRDGM LDDEEFALAS HLIEAKLEGH GLPTNLPRRL VPPSKRRQKG
     SAE
//
ID   ATLA1_MOUSE             Reviewed;         558 AA.
AC   Q8BH66; Q8BJH5;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Atlastin-1;
DE            EC=3.6.5.-;
DE   AltName: Full=Spastic paraplegia 3A homolog;
GN   Name=Atl1; Synonyms=Spg3a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Liver, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-22 AND SER-23,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-23, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   INTERACTION WITH REEP5 AND RTN3.
RX   PubMed=19665976; DOI=10.1016/j.cell.2009.05.025;
RA   Hu J., Shibata Y., Zhu P.-P., Voss C., Rismanchi N., Prinz W.A.,
RA   Rapoport T.A., Blackstone C.;
RT   "A class of dynamin-like GTPases involved in the generation of the
RT   tubular ER network.";
RL   Cell 138:549-561(2009).
CC   -!- FUNCTION: GTPase tethering membranes through formation of trans-
CC       homooligomer and mediating homotypic fusion of endoplasmic
CC       reticulum membranes. Functions in endoplasmic reticulum tubular
CC       network biogenesis. May also regulate Golgi biogenesis. May
CC       regulate axonal development (By similarity).
CC   -!- SUBUNIT: Homooligomer. Interacts (via N-terminal region) with
CC       MAP4K4 (via CNH regulatory domain). Interacts with SPAST;
CC       interaction is direct (By similarity). Interacts with REEP5, RTN3
CC       and probably RTN4 (via the transmembrane region).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity). Golgi apparatus membrane; Multi-
CC       pass membrane protein (By similarity). Cell projection, axon (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the GBP family. Atlastin subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK046919; BAC32920.1; -; mRNA.
DR   EMBL; AK050339; BAC34198.1; -; mRNA.
DR   EMBL; BC050784; AAH50784.1; -; mRNA.
DR   EMBL; AK083918; BAC39062.1; -; mRNA.
DR   IPI; IPI00221754; -.
DR   RefSeq; NP_848743.1; NM_178628.5.
DR   UniGene; Mm.474462; -.
DR   ProteinModelPortal; Q8BH66; -.
DR   STRING; Q8BH66; -.
DR   PhosphoSite; Q8BH66; -.
DR   PRIDE; Q8BH66; -.
DR   Ensembl; ENSMUST00000021466; ENSMUSP00000021466; ENSMUSG00000021066.
DR   GeneID; 73991; -.
DR   KEGG; mmu:73991; -.
DR   UCSC; uc007nsy.1; mouse.
DR   CTD; 73991; -.
DR   MGI; MGI:1921241; Atl1.
DR   GeneTree; ENSGT00390000008959; -.
DR   HOGENOM; HBG443778; -.
DR   HOVERGEN; HBG062891; -.
DR   InParanoid; Q8BH66; -.
DR   OMA; ATHRHLY; -.
DR   OrthoDB; EOG49078Q; -.
DR   NextBio; 339480; -.
DR   ArrayExpress; Q8BH66; -.
DR   Bgee; Q8BH66; -.
DR   CleanEx; MM_GBP3; -.
DR   Genevestigator; Q8BH66; -.
DR   GermOnline; ENSMUSG00000021066; Mus musculus.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0000137; C:Golgi cis cisterna; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; ISS:UniProtKB.
DR   GO; GO:0005792; C:microsome; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; ISS:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR   InterPro; IPR003191; Guanylate-bd_C.
DR   InterPro; IPR015894; Guanylate-bd_N.
DR   Gene3D; G3DSA:1.20.1000.10; Guanylate-bd_C; 1.
DR   Pfam; PF02263; GBP; 1.
DR   Pfam; PF02841; GBP_C; 1.
DR   SUPFAM; SSF48340; GBP; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Coiled coil; Endoplasmic reticulum; Golgi apparatus;
KW   GTP-binding; Hydrolase; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    558       Atlastin-1.
FT                                /FTId=PRO_0000190973.
FT   TOPO_DOM      1    449       Cytoplasmic (By similarity).
FT   TRANSMEM    450    470       Helical; (Potential).
FT   TOPO_DOM    471    471       Lumenal (Potential).
FT   TRANSMEM    472    492       Helical; (Potential).
FT   TOPO_DOM    493    558       Cytoplasmic (By similarity).
FT   NP_BIND      74     81       GTP (Potential).
FT   NP_BIND     146    150       GTP (Potential).
FT   REGION      448    558       Sufficient for membrane association (By
FT                                similarity).
FT   COILED      412    439       Potential.
FT   MOD_RES      10     10       Phosphoserine.
FT   MOD_RES      18     18       Phosphoserine.
FT   MOD_RES      22     22       Phosphoserine.
FT   MOD_RES      23     23       Phosphoserine.
SQ   SEQUENCE   558 AA;  63377 MW;  4734A5D99A9171AC CRC64;
     MAKSRRDRNS WGGFSEKSSD WSSEEEEPVR KAGPVQVLIV KDDHSFELDE AALNRILLSQ
     AVRDKEVVAV SVAGAFRKGK SFLMDFMLRY MYNQESVDWV GDYNEPLTGF SWRGGSERET
     TGIQIWSEVF LINKLDGKKV AVLLMDTQGT FDSQSTLRDS ATVFALSTMI SSIQVYNLSQ
     NVQEDDLQHL QLFTEYGRLA MEETFLKPFQ SLIFLVRDWS FPYEFSYGAD GGAKFLEKRL
     KVSGNQHEEL QNVRKHIHSC FTNISCFLLP HPGLKVATNP NFDGKLKEID DEFIKNLKIL
     IPWLLSPERL DIKEINGNKI TCRGLLEYFK AYIKIYQGEE LPHPKSMLQA TAEANNLAAV
     ATAKDTYNKK MEEVCGGDKP FLAPNDLQSK HLQLKEESVK LFRGVKKMGG EEFSRRYLQQ
     LESEIDELYI QYIKHNDSKN IFHAARTPAT LFVVIFITYV IAGVTGFIGL DIIASLCNMI
     MGLTLITLCT WAYIRYSGEY RELGAVIDQV AAALWDQGST NEALYKLYSA AATHRHLCHQ
     AFPAPKSEPT QQPEKKKI
//
ID   FBXL4_MOUSE             Reviewed;         621 AA.
AC   Q8BH70;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=F-box/LRR-repeat protein 4;
DE   AltName: Full=F-box and leucine-rich repeat protein 4;
GN   Name=Fbxl4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SUBUNIT: Part of a SCF (SKP1-cullin-F-box) protein ligase complex
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 F-box domain.
CC   -!- SIMILARITY: Contains 8 LRR (leucine-rich) repeats.
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DR   EMBL; AK032391; BAC27850.1; -; mRNA.
DR   EMBL; AK051429; BAC34636.1; -; mRNA.
DR   EMBL; AL683854; CAM18296.1; -; Genomic_DNA.
DR   EMBL; AL772230; CAM18296.1; JOINED; Genomic_DNA.
DR   EMBL; AL772230; CAM22633.1; -; Genomic_DNA.
DR   EMBL; AL683854; CAM22633.1; JOINED; Genomic_DNA.
DR   IPI; IPI00221762; -.
DR   RefSeq; NP_766576.1; NM_172988.3.
DR   UniGene; Mm.40708; -.
DR   ProteinModelPortal; Q8BH70; -.
DR   SMR; Q8BH70; 277-614.
DR   STRING; Q8BH70; -.
DR   PhosphoSite; Q8BH70; -.
DR   PRIDE; Q8BH70; -.
DR   Ensembl; ENSMUST00000039234; ENSMUSP00000042219; ENSMUSG00000040410.
DR   GeneID; 269514; -.
DR   KEGG; mmu:269514; -.
DR   UCSC; uc008sdo.1; mouse.
DR   CTD; 269514; -.
DR   MGI; MGI:2140367; Fbxl4.
DR   GeneTree; ENSGT00560000077113; -.
DR   HOGENOM; HBG281231; -.
DR   HOVERGEN; HBG051588; -.
DR   InParanoid; Q8BH70; -.
DR   OMA; VLYRTKV; -.
DR   OrthoDB; EOG4XSKPD; -.
DR   PhylomeDB; Q8BH70; -.
DR   NextBio; 392870; -.
DR   ArrayExpress; Q8BH70; -.
DR   Bgee; Q8BH70; -.
DR   CleanEx; MM_FBXL4; -.
DR   Genevestigator; Q8BH70; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR001810; F-box_dom_cyclin-like.
DR   InterPro; IPR022364; F-box_dom_Skp2-like.
DR   InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR   Pfam; PF00646; F-box; 1.
DR   SMART; SM00256; FBOX; 1.
DR   SMART; SM00367; LRR_CC; 1.
DR   SUPFAM; SSF81383; F-box_dom_Skp2-like; 1.
DR   PROSITE; PS50181; FBOX; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Leucine-rich repeat; Nucleus; Repeat;
KW   Ubl conjugation pathway.
FT   CHAIN         1    621       F-box/LRR-repeat protein 4.
FT                                /FTId=PRO_0000307719.
FT   DOMAIN      277    332       F-box.
FT   REPEAT      400    421       LRR 1.
FT   REPEAT      425    449       LRR 2.
FT   REPEAT      450    475       LRR 3.
FT   REPEAT      478    503       LRR 4.
FT   REPEAT      504    524       LRR 5.
FT   REPEAT      532    558       LRR 6.
FT   REPEAT      559    583       LRR 7.
FT   REPEAT      584    609       LRR 8.
SQ   SEQUENCE   621 AA;  70269 MW;  458544AD66711119 CRC64;
     MSPVFPMLTV LTMFYYMCLR RRARTATRGD MMNSHRTIVS NSRTSPLNAE VVQYAKEVVD
     FSSHYGSENS MSYTMWNLAG VPNVFPSSGD FTQTAVFRTY GTWWDQCPSA SLPFRRTPSS
     FQSQDYVELT FEQQVYPTAV HVLETYHPGA VIRILACSAN PYSPNPPAEV RWEILWSERP
     MKVNASQARQ FKPCIKQINF PTNLIRLEVN SSLLDYYTEL DAVVLHGTKD KPLLSLKTAL
     VDMNDLEDDD YEEKDGCEMD ALNKKFSSAA LGDGPHNGYF DKLPYELIQL ILNHLSLPDL
     CRLAQTCRLL HQHCCDPLQY IHLNLQPYWA RLDDTSLEFL QARCVLVQWL NLSWTGNRGF
     ISVSGFSRFL KVCGSELVRL ELSCSHFLND TCLEVISEMC PNLQDLNLSS CDKLPPQAFG
     HIAKLCSLKR LVLYRTKVEQ TALLSILNFC AELQHLSLGS CVMIEDYDVI ASMIGAKCKN
     LRTLDLWRCK NITENGIAEL ASGCVLLEEL DLGWCPTLQS STGCFVRLAR QLPNLQKLFL
     TANRSVCDTD IEELASNCTR LQQLDILGTR MVSPASLRKL LESCKDLSLL DVSFCSQIDN
     KAVLELNASF PKVFIKKSFT Q
//
ID   RB39B_MOUSE             Reviewed;         213 AA.
AC   Q8BHC1; Q3TUJ3;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Ras-related protein Rab-39B;
GN   Name=Rab39b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, and Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=20159109; DOI=10.1016/j.ajhg.2010.01.011;
RA   Giannandrea M., Bianchi V., Mignogna M.L., Sirri A., Carrabino S.,
RA   D'Elia E., Vecellio M., Russo S., Cogliati F., Larizza L.,
RA   Ropers H.H., Tzschach A., Kalscheuer V., Oehl-Jaschkowitz B.,
RA   Skinner C., Schwartz C.E., Gecz J., Van Esch H., Raynaud M.,
RA   Chelly J., de Brouwer A.P., Toniolo D., D'Adamo P.;
RT   "Mutations in the small GTPase gene RAB39B are responsible for X-
RT   linked mental retardation associated with autism, epilepsy, and
RT   macrocephaly.";
RL   Am. J. Hum. Genet. 86:185-195(2010).
CC   -!- FUNCTION: May be involved in vesicular trafficking. Play a role in
CC       synapse formation.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential). Golgi apparatus. Note=Partial colocalization
CC       with markers that cycle from the cell surface to the trans-Golgi
CC       network.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in neuron and neuronal
CC       precursors in the brain. Expression is high in all regions of the
CC       brain with highest levels observed in the hippocampus.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK039013; BAC30206.1; -; mRNA.
DR   EMBL; AK048981; BAC33503.1; -; mRNA.
DR   EMBL; AK160737; BAE35978.1; -; mRNA.
DR   EMBL; BC050853; AAH50853.1; -; mRNA.
DR   EMBL; BC052472; AAH52472.1; -; mRNA.
DR   IPI; IPI00272230; -.
DR   RefSeq; NP_780331.1; NM_175122.5.
DR   UniGene; Mm.45148; -.
DR   ProteinModelPortal; Q8BHC1; -.
DR   SMR; Q8BHC1; 3-178.
DR   PRIDE; Q8BHC1; -.
DR   Ensembl; ENSMUST00000033545; ENSMUSP00000033545; ENSMUSG00000031202.
DR   GeneID; 67790; -.
DR   KEGG; mmu:67790; -.
DR   UCSC; uc009tqe.1; mouse.
DR   CTD; 67790; -.
DR   MGI; MGI:1915040; Rab39b.
DR   GeneTree; ENSGT00600000084094; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; Q8BHC1; -.
DR   OMA; TKSDRRC; -.
DR   OrthoDB; EOG43JC5J; -.
DR   PhylomeDB; Q8BHC1; -.
DR   NextBio; 325571; -.
DR   ArrayExpress; Q8BHC1; -.
DR   Bgee; Q8BHC1; -.
DR   CleanEx; MM_RAB39B; -.
DR   Genevestigator; Q8BHC1; -.
DR   GermOnline; ENSMUSG00000031202; Mus musculus.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0050808; P:synapse organization; IMP:UniProtKB.
DR   GO; GO:0016192; P:vesicle-mediated transport; IMP:UniProtKB.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Golgi apparatus; GTP-binding; Lipoprotein; Membrane;
KW   Methylation; Nucleotide-binding; Prenylation; Protein transport;
KW   Transport.
FT   CHAIN         1    213       Ras-related protein Rab-39B.
FT                                /FTId=PRO_0000121256.
FT   NP_BIND      15     22       GTP (By similarity).
FT   NP_BIND      64     68       GTP (By similarity).
FT   NP_BIND     123    126       GTP (By similarity).
FT   MOTIF        37     45       Effector region (By similarity).
FT   MOD_RES     213    213       Cysteine methyl ester (By similarity).
FT   LIPID       211    211       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   LIPID       213    213       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   213 AA;  24636 MW;  338F5B35C61FA88E CRC64;
     MEAIWLYQFR LIVIGDSTVG KSCLIRRFTE GRFAQVSDPT VGVDFFSRLV EIEPGKRIKL
     QIWDTAGQER FRSITRAYYR NSVGGLLLFD ITNRRSFQNV HEWLEETKVH VQPYQIVFVL
     VGHKCDLDTQ RQVTRHEAEK LAAAYGMKYI ETSARDAINV EKAFTDLTRD IYELVKRGEI
     TIQEGWEGVK SGFVPNVVHS SEEVIKSERR CLC
//
ID   FRMD3_MOUSE             Reviewed;         595 AA.
AC   Q8BHD4; A2BEJ6; Q3UF23; Q5SPU0; Q5SPU1; Q8C045;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=FERM domain-containing protein 3;
GN   Name=Frmd3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryo, Head, Olfactory bulb, and Sympathetic ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Putative tumor suppressor gene that may be implicated in
CC       the origin and progression of lung cancer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BHD4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BHD4-2; Sequence=VSP_031168;
CC         Note=Gene prediction based on EST data;
CC       Name=3;
CC         IsoId=Q8BHD4-3; Sequence=VSP_031169, VSP_031170;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK032348; BAC27827.1; -; mRNA.
DR   EMBL; AK034956; BAC28893.1; -; mRNA.
DR   EMBL; AK048561; BAC33375.1; -; mRNA.
DR   EMBL; AK149095; BAE28738.1; -; mRNA.
DR   EMBL; AL844607; CAI26161.2; -; Genomic_DNA.
DR   EMBL; BX088570; CAI26161.2; JOINED; Genomic_DNA.
DR   EMBL; BX957282; CAI26161.2; JOINED; Genomic_DNA.
DR   EMBL; AL844607; CAI26162.2; -; Genomic_DNA.
DR   EMBL; BX088570; CAI26162.2; JOINED; Genomic_DNA.
DR   EMBL; BX957282; CAI26162.2; JOINED; Genomic_DNA.
DR   EMBL; BX957282; CAI26189.2; -; Genomic_DNA.
DR   EMBL; AL844607; CAI26189.2; JOINED; Genomic_DNA.
DR   EMBL; BX088570; CAI26189.2; JOINED; Genomic_DNA.
DR   EMBL; BX957282; CAI26190.2; -; Genomic_DNA.
DR   EMBL; AL844607; CAI26190.2; JOINED; Genomic_DNA.
DR   EMBL; BX088570; CAI26190.2; JOINED; Genomic_DNA.
DR   EMBL; BX088570; CAM19942.1; -; Genomic_DNA.
DR   EMBL; AL844607; CAM19942.1; JOINED; Genomic_DNA.
DR   EMBL; BX957282; CAM19942.1; JOINED; Genomic_DNA.
DR   EMBL; BX088570; CAM19943.1; -; Genomic_DNA.
DR   EMBL; AL844607; CAM19943.1; JOINED; Genomic_DNA.
DR   EMBL; BX957282; CAM19943.1; JOINED; Genomic_DNA.
DR   EMBL; BC112419; AAI12420.1; -; mRNA.
DR   EMBL; BC113795; AAI13796.1; -; mRNA.
DR   EMBL; BC118964; AAI18965.1; -; mRNA.
DR   IPI; IPI00624683; -.
DR   IPI; IPI00648734; -.
DR   IPI; IPI00885747; -.
DR   RefSeq; NP_001157204.1; NM_001163732.1.
DR   RefSeq; NP_766457.1; NM_172869.4.
DR   UniGene; Mm.221597; -.
DR   HSSP; P11171; 1GG3.
DR   ProteinModelPortal; Q8BHD4; -.
DR   SMR; Q8BHD4; 29-342.
DR   PhosphoSite; Q8BHD4; -.
DR   PRIDE; Q8BHD4; -.
DR   Ensembl; ENSMUST00000084474; ENSMUSP00000081514; ENSMUSG00000049122.
DR   GeneID; 242506; -.
DR   KEGG; mmu:242506; -.
DR   UCSC; uc008tjg.1; mouse.
DR   CTD; 242506; -.
DR   MGI; MGI:2442466; Frmd3.
DR   HOGENOM; HBG446778; -.
DR   HOVERGEN; HBG057180; -.
DR   InParanoid; Q8BHD4; -.
DR   OMA; FLCEIRQ; -.
DR   OrthoDB; EOG4S1T6X; -.
DR   PhylomeDB; Q8BHD4; -.
DR   NextBio; 385376; -.
DR   ArrayExpress; Q8BHD4; -.
DR   Bgee; Q8BHD4; -.
DR   CleanEx; MM_FRMD3; -.
DR   Genevestigator; Q8BHD4; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0019898; C:extrinsic to membrane; IEA:InterPro.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR000798; Ez/rad/moesin.
DR   InterPro; IPR014847; FERM-adjacent.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH_type.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; FALSE_NEG.
DR   PROSITE; PS50057; FERM_3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    595       FERM domain-containing protein 3.
FT                                /FTId=PRO_0000318099.
FT   TRANSMEM    529    549       Helical; (Potential).
FT   DOMAIN       32    312       FERM.
FT   MOD_RES     414    414       Phosphoserine.
FT   VAR_SEQ       1    352       Missing (in isoform 3).
FT                                /FTId=VSP_031169.
FT   VAR_SEQ     353    356       PEVH -> MSVF (in isoform 3).
FT                                /FTId=VSP_031170.
FT   VAR_SEQ     551    595       GIDLSFLCEIRQTPEFEQFHYEYYCPLKEWVAGKVNIVLYM
FT                                LGCS -> VSMP (in isoform 2).
FT                                /FTId=VSP_031168.
FT   CONFLICT    405    405       M -> V (in Ref. 1; BAC27827).
SQ   SEQUENCE   595 AA;  68448 MW;  2EB221C15159EE61 CRC64;
     MFASCHCAPR GRRTMKMIHF RSSSIKSLNQ EMKCTIRLLD DSEVSCHIQR ETKGQFLIEY
     ICNYYSLLEK DYFGIRYVDP EKQRHWLEPN KSIFKQMKSH PPYTMCFRVK FYPHEPLKIK
     EELTRYLLYL QIKRDIFHGR LLCSFSDAAY LGACIVQAEF GDYYPDEHPE NYISEFEIFP
     KQSQKLERKI MEIHNNELRG QSPAIAEFNL LLKAHTLETY GVDPHPCKDS RGATAFLGFT
     AAGFVVFQGN KRIHLRKWSD VCKLKFEGKT FYVIGSQKEK NAVLAFHTST PAACKHLWKC
     GVENQAFYKY AKSSQIKTVS SSKIFFKGSR FRYSGKVAKE VVEASSKIQR DPPEVHRVNI
     TQSRSFHSLN KQLIINMEPL QPLLPSPTEQ EEEVPVGEGV PLPKMDVSEP LIASSPVKGA
     QCADPPDEEE DRVKEDPLTI SELAYNPSAS LLPTPVDDDE INMLFDCPSR LELEREDTDS
     FEELEADENA FLIAEEEELK EARQALSWSY SILTGHIWVN PLVKSFSRLL VVGLGLLLFV
     FPLLLLLLES GIDLSFLCEI RQTPEFEQFH YEYYCPLKEW VAGKVNIVLY MLGCS
//
ID   ATCAY_MOUSE             Reviewed;         372 AA.
AC   Q8BHE3; Q3TR94;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Caytaxin;
GN   Name=Atcay;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DISEASE, AND TISSUE SPECIFICITY.
RX   MEDLINE=22954658; PubMed=14556008; DOI=10.1038/ng1255;
RA   Bomar J.M., Benke P.J., Slattery E.L., Puttagunta R., Taylor L.P.,
RA   Seong E., Nystuen A., Chen W., Albin R.L., Patel P.D., Kittles R.A.,
RA   Sheffield V.C., Burmeister M.;
RT   "Mutations in a novel gene encoding a CRAL-TRIO domain cause human
RT   Cayman ataxia and ataxia/dystonia in the jittery mouse.";
RL   Nat. Genet. 35:264-269(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, Hypothalamus, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- TISSUE SPECIFICITY: Neuronal tissues specific. Strongly expressed
CC       in brain. Expressed in virtually all parts of the adult brain,
CC       including cortex, cerebellum and olfactory bulbs. In embryos, it
CC       is also completely restricted to neuronal tissues, including
CC       brain, dorsal root ganglia and enteric nervous system.
CC   -!- DOMAIN: The CRAL-TRIO domain is known to bind small hydrophobic
CC       molecules (By similarity).
CC   -!- DISEASE: Note=Defects in Atcay are the cause of jittery phenotype,
CC       which is characterized by severe truncal and limb ataxia and die
CC       of starvation and dehydration by 3-4 weeks of age.
CC   -!- SIMILARITY: Contains 1 CRAL-TRIO domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY349150; AAQ90064.1; -; mRNA.
DR   EMBL; AK028298; BAC25867.1; -; mRNA.
DR   EMBL; AK038483; BAC30014.1; -; mRNA.
DR   EMBL; AK038990; BAC30195.1; -; mRNA.
DR   EMBL; AK039411; BAC30342.1; -; mRNA.
DR   EMBL; AK162959; BAE37136.1; -; mRNA.
DR   EMBL; BC048903; AAH48903.1; -; mRNA.
DR   IPI; IPI00221845; -.
DR   RefSeq; NP_848777.1; NM_178662.3.
DR   UniGene; Mm.127681; -.
DR   ProteinModelPortal; Q8BHE3; -.
DR   STRING; Q8BHE3; -.
DR   PRIDE; Q8BHE3; -.
DR   Ensembl; ENSMUST00000047408; ENSMUSP00000036721; ENSMUSG00000034958.
DR   GeneID; 16467; -.
DR   KEGG; mmu:16467; -.
DR   UCSC; uc007ggo.1; mouse.
DR   CTD; 16467; -.
DR   MGI; MGI:2448730; Atcay.
DR   eggNOG; maNOG07332; -.
DR   GeneTree; ENSGT00420000029688; -.
DR   HOGENOM; HBG445458; -.
DR   HOVERGEN; HBG054692; -.
DR   InParanoid; Q8BHE3; -.
DR   OMA; MRVVTHG; -.
DR   OrthoDB; EOG480HX8; -.
DR   PhylomeDB; Q8BHE3; -.
DR   NextBio; 289741; -.
DR   ArrayExpress; Q8BHE3; -.
DR   Bgee; Q8BHE3; -.
DR   CleanEx; MM_ATCAY; -.
DR   Genevestigator; Q8BHE3; -.
DR   GermOnline; ENSMUSG00000034958; Mus musculus.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR022181; Bcl2-/adenovirus-E1B.
DR   InterPro; IPR001251; CRAL-bd_TRIO_C.
DR   Gene3D; G3DSA:3.40.525.10; CRAL_bd_TRIO_C; 1.
DR   Pfam; PF12496; BNIP2; 1.
DR   Pfam; PF00650; CRAL_TRIO; 1.
DR   SUPFAM; SSF52087; CRAL_TRIO_C; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
PE   2: Evidence at transcript level;
KW   Transport.
FT   CHAIN         1    372       Caytaxin.
FT                                /FTId=PRO_0000210769.
FT   DOMAIN      171    328       CRAL-TRIO.
SQ   SEQUENCE   372 AA;  42178 MW;  299146667F722C11 CRC64;
     MGTTEATLRM ENVDVRDEWQ DEDLPRPLPE DTGVERLGGA VEDSSSPPST LNLSGAHRKR
     KTLVAPEINI SLDQSEGSLL SDDFLDTPDD LDINVDDIET PDETDSLEFL GNGNELEWED
     DTPVATAKNM PGDSADLFGD GSAEDGSAAN GRLWRTVIIG EQEHRIDLHM IRPYMKVVTH
     GGYYGEGLNA IIVFAACFLP DSSSPDYHYI MENLFLYVIS SLELLVAEDY MIVYLNGATP
     RRRMPGIGWL KKCYHMIDRR LRKNLKSLII VHPSWFIRTV LAISRPFISV KFISKIQYVH
     SLEELERLIP MEHVQLPDCV LQYEEQRLRA KRESTRPPQP EFLLPRSEEK PETVEEEDRA
     AEATEDQETS MS
//
ID   TM108_MOUSE             Reviewed;         574 AA.
AC   Q8BHE4; Q80WR9;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Transmembrane protein 108;
DE   Flags: Precursor;
GN   Name=Tmem108;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Heart, and Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
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DR   EMBL; AK044989; BAC32171.1; -; mRNA.
DR   EMBL; AK141589; BAE24751.1; -; mRNA.
DR   EMBL; AK052330; BAC34940.1; -; mRNA.
DR   EMBL; AK047474; BAC33068.1; -; mRNA.
DR   EMBL; BC052085; AAH52085.2; -; mRNA.
DR   IPI; IPI00221846; -.
DR   RefSeq; NP_848753.1; NM_178638.4.
DR   UniGene; Mm.384704; -.
DR   ProteinModelPortal; Q8BHE4; -.
DR   PhosphoSite; Q8BHE4; -.
DR   PRIDE; Q8BHE4; -.
DR   Ensembl; ENSMUST00000049452; ENSMUSP00000046021; ENSMUSG00000042757.
DR   GeneID; 81907; -.
DR   KEGG; mmu:81907; -.
DR   UCSC; uc009rgx.1; mouse.
DR   CTD; 81907; -.
DR   MGI; MGI:1932411; Tmem108.
DR   eggNOG; maNOG16037; -.
DR   GeneTree; ENSGT00390000000626; -.
DR   HOGENOM; HBG279473; -.
DR   HOVERGEN; HBG094052; -.
DR   InParanoid; Q8BHE4; -.
DR   OMA; QALYCQL; -.
DR   OrthoDB; EOG4T4CV8; -.
DR   NextBio; 350481; -.
DR   ArrayExpress; Q8BHE4; -.
DR   Bgee; Q8BHE4; -.
DR   CleanEx; MM_TMEM108; -.
DR   Genevestigator; Q8BHE4; -.
DR   GermOnline; ENSMUSG00000042757; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     28       Potential.
FT   CHAIN        29    574       Transmembrane protein 108.
FT                                /FTId=PRO_0000243914.
FT   TOPO_DOM     29    467       Extracellular (Potential).
FT   TRANSMEM    468    488       Helical; (Potential).
FT   TOPO_DOM    489    574       Cytoplasmic (Potential).
FT   CARBOHYD    201    201       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    223    223       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    445    445       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   574 AA;  59642 MW;  29901D7013C07DC1 CRC64;
     MKRSLQALYC QLLSFLLTLA LTKALVLAVH EPSPRESLQT LPSGSPPGTM VTAPHSPTRL
     SSVLTLNPTP DGPSSQAAAT LETTVSHPEG HPPTDTTSTV MGTAAVPHPE SPLPTGSPPA
     AMTTTPSHSE SLPPGDATPT TTLPTKPAGT TSRPTVAPRA TTRRPPRPPG SSRKGAGGST
     RTLTPVPGGH LARKESQRGR NQSSAHLGPK RPLGKIFQIY KGNFTGSAEP DPSALTPRTP
     LGGYFSSTQP QTVSPATAPR STSRVPPTTS LVPVKDKPGF IRSNQGSGPI LTSPGGEPAA
     TAATGAPAST QPAPVPSQSP HGDVQDSASH SDSWLAVTPD TDRPTSASSG VFTAATGPTQ
     AAFDATVSAP SPGIPQGPSA TPQAPTRPSG VSESTVSPAE EEAEASPTTT DRGPRPLSTV
     LSTATGNFLN RLVPAGTWKP GTVANISHVA EGDKPQHRAT ICLSKMDIAW VIVAISVPIS
     SCSVLLTVCC MRRKKKTANP ENNLSYWNNA ITMDYFNRHA VELPREIQSL ETSEDQLSEP
     RSPANGDYRD TGMVLVNPFC QETLFVGNDQ VSEI
//
ID   RAB9B_MOUSE             Reviewed;         201 AA.
AC   Q8BHH2;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Ras-related protein Rab-9B;
GN   Name=Rab9b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Involved in the transport of proteins between the
CC       endosomes and the trans Golgi network (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR   EMBL; AK034442; BAC28710.1; -; mRNA.
DR   EMBL; AK049693; BAC33876.1; -; mRNA.
DR   IPI; IPI00221865; -.
DR   RefSeq; NP_795945.1; NM_176971.2.
DR   UniGene; Mm.44557; -.
DR   ProteinModelPortal; Q8BHH2; -.
DR   SMR; Q8BHH2; 3-175.
DR   PRIDE; Q8BHH2; -.
DR   Ensembl; ENSMUST00000058814; ENSMUSP00000049739; ENSMUSG00000043463.
DR   GeneID; 319642; -.
DR   KEGG; mmu:319642; -.
DR   UCSC; uc009uje.1; mouse.
DR   CTD; 319642; -.
DR   MGI; MGI:2442454; Rab9b.
DR   GeneTree; ENSGT00600000084038; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; Q8BHH2; -.
DR   OMA; PERFPFV; -.
DR   OrthoDB; EOG4R7VBS; -.
DR   PhylomeDB; Q8BHH2; -.
DR   NextBio; 395140; -.
DR   ArrayExpress; Q8BHH2; -.
DR   Bgee; Q8BHH2; -.
DR   CleanEx; MM_RAB9B; -.
DR   Genevestigator; Q8BHH2; -.
DR   GermOnline; ENSMUSG00000043463; Mus musculus.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; GTP-binding; Lipoprotein; Membrane; Nucleotide-binding;
KW   Prenylation; Protein transport; Transport.
FT   CHAIN         1    201       Ras-related protein Rab-9B.
FT                                /FTId=PRO_0000121143.
FT   NP_BIND      14     22       GTP (By similarity).
FT   NP_BIND      62     66       GTP (By similarity).
FT   NP_BIND     124    127       GTP (By similarity).
FT   NP_BIND     154    156       GTP (By similarity).
FT   MOTIF        36     44       Effector region (By similarity).
FT   LIPID       200    200       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   LIPID       201    201       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   201 AA;  22704 MW;  1E28B18F8F8DDDFD CRC64;
     MSGKSLLLKV ILLGDGGVGK SSLMNRYVTN KFDSQAFHTI GVEFLNRDLE VDGRFVTLQI
     WDTAGQERFK SLRTPFYRGA DCCLLTFSVD DRQSFENLGN WQKEFIYYAD VKDPDHFPFV
     VLGNKVDKED RQVTTEEAQA WCMENGNYPY LETSAKDDTN VTVAFEEAVR QVLAVEEQLE
     HCMLGHTIDL NSGSKASSSC C
//
ID   SLU7_MOUSE              Reviewed;         585 AA.
AC   Q8BHJ9; Q3KQQ3; Q5SRU1; Q63ZX3; Q6P923; Q8BL59; Q8BXD5; Q8R5C1;
AC   Q91YV6;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Pre-mRNA-splicing factor SLU7;
GN   Name=Slu7; Synonyms=D11Ertd730e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Corpora quadrigemina, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Heart, Kidney, Lung, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Participates in the second catalytic step of pre-mRNA
CC       splicing, when the free hydroxyl group of exon I attacks the 3'-
CC       splice site to generate spliced mRNA and the excised lariat
CC       intron. Required for holding exon 1 properly in the spliceosome
CC       and for correct AG identification when more than one possible AG
CC       exists in 3'-splicing site region. May be involved in the
CC       activation of proximal AG. Probably also involved in alternative
CC       splicing regulation (By similarity).
CC   -!- SUBUNIT: Component of late spliceosomal complexes. Associates with
CC       the spliceosome prior to recognition of the 3'-splice site for
CC       step II, probably during catalysis of step I (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity). Note=Predominantly nuclear. Shuttling between the
CC       nucleus and the cytoplasm is regulated by the CCHC-type zinc
CC       finger (By similarity).
CC   -!- DOMAIN: The CCHC-type zinc finger is required to retain the
CC       protein within the nucleus and prevent its shuttle back to the
CC       cytoplasm via the CRM1 pathway (By similarity).
CC   -!- SIMILARITY: Belongs to the SLU7 family.
CC   -!- SIMILARITY: Contains 1 CCHC-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH13810.1; Type=Erroneous initiation;
CC       Sequence=CAI24831.1; Type=Erroneous gene model prediction;
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DR   EMBL; AK029117; BAC26306.1; -; mRNA.
DR   EMBL; AK046262; BAC32662.1; -; mRNA.
DR   EMBL; AK047597; BAC33093.1; -; mRNA.
DR   EMBL; AK049178; BAC33589.1; -; mRNA.
DR   EMBL; AL670472; CAI24830.1; -; Genomic_DNA.
DR   EMBL; AL670472; CAI24831.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC013810; AAH13810.1; ALT_INIT; mRNA.
DR   EMBL; BC023057; AAH23057.1; -; mRNA.
DR   EMBL; BC060954; AAH60954.1; -; mRNA.
DR   EMBL; BC082780; AAH82780.1; ALT_TERM; mRNA.
DR   EMBL; BC106099; AAI06100.1; -; mRNA.
DR   IPI; IPI00221882; -.
DR   RefSeq; NP_683514.2; NM_148673.3.
DR   RefSeq; NP_945174.1; NM_198936.1.
DR   UniGene; Mm.28200; -.
DR   ProteinModelPortal; Q8BHJ9; -.
DR   STRING; Q8BHJ9; -.
DR   PhosphoSite; Q8BHJ9; -.
DR   PRIDE; Q8BHJ9; -.
DR   Ensembl; ENSMUST00000020681; ENSMUSP00000020681; ENSMUSG00000020409.
DR   GeneID; 193116; -.
DR   KEGG; mmu:193116; -.
DR   UCSC; uc007imp.1; mouse.
DR   CTD; 193116; -.
DR   MGI; MGI:2385598; Slu7.
DR   eggNOG; roNOG09213; -.
DR   HOVERGEN; HBG053287; -.
DR   InParanoid; Q8BHJ9; -.
DR   OMA; PQTLMEM; -.
DR   OrthoDB; EOG42RD76; -.
DR   PhylomeDB; Q8BHJ9; -.
DR   NextBio; 371430; -.
DR   ArrayExpress; Q8BHJ9; -.
DR   Bgee; Q8BHJ9; -.
DR   CleanEx; MM_SLU7; -.
DR   Genevestigator; Q8BHJ9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; ISS:HGNC.
DR   GO; GO:0030532; C:small nuclear ribonucleoprotein complex; ISS:HGNC.
DR   GO; GO:0005681; C:spliceosomal complex; ISS:HGNC.
DR   GO; GO:0030628; F:pre-mRNA 3'-splice site binding; ISS:HGNC.
DR   GO; GO:0000386; F:second spliceosomal transesterification activity; ISS:HGNC.
DR   GO; GO:0008270; F:zinc ion binding; ISS:HGNC.
DR   GO; GO:0000380; P:alternative nuclear mRNA splicing, via spliceosome; ISS:HGNC.
DR   GO; GO:0000389; P:nuclear mRNA 3'-splice site recognition; ISS:HGNC.
DR   InterPro; IPR021715; Slu7.
DR   InterPro; IPR001878; Znf_CCHC.
DR   Pfam; PF11708; Slu7; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   PROSITE; PS50158; ZF_CCHC; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Cytoplasm; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW   Phosphoprotein; Spliceosome; Zinc; Zinc-finger.
FT   CHAIN         1    585       Pre-mRNA-splicing factor SLU7.
FT                                /FTId=PRO_0000289196.
FT   ZN_FING     118    135       CCHC-type.
FT   MOTIF       129    169       Bipartite nuclear localization signal (By
FT                                similarity).
FT   MOD_RES     215    215       Phosphoserine.
FT   MOD_RES     235    235       Phosphoserine.
FT   MOD_RES     243    243       Phosphotyrosine (By similarity).
FT   CONFLICT     43     43       R -> K (in Ref. 1; BAC32662).
FT   CONFLICT    102    102       Y -> H (in Ref. 1; BAC33093).
SQ   SEQUENCE   585 AA;  68080 MW;  1020FE4B6D65668B CRC64;
     MSAAAVDPVS ATPMTGSKEM SLEEPKKMTR EDWRKKKELE EQRKLGNAPA EVDEEGKDIN
     PHIPQYISSV PWYIDPSKRP TLKHQRPQPE KQKQFSSSGE WYKRGVKENS ITTKYRKGAC
     ENCGAMTHKR KDCFERPRRV GAKFTGTNIA PDEHVQPQLM FDYDGKRDRW NGYNPEEHMK
     IVEEYAKVDL AKRTLKAQKL QEELASGKLV EQANSPKHQW GEEEPNSQME KDHNSEDEDE
     DKYADDIDMP GQNFDSKRRI TVRNLRIRED IAKYLRNLDP NSAYYDPKTR AMRENPYANA
     GKNPDEVSYA GDNFVRYTGD TISMAQTQLF AWEAYDKGSE VHLQADPTKL ELLYKSFKVK
     KEDFKEQQKE SILEKYGGQE HLDAPPAELL LAQTEDYVEY SRHGTVIKGQ ERAVACSKYE
     EDVKINNHTH IWGSYWKEGR WGYKCCHSFF KYSYCTGEAG KESVNSEECI ITGATAEESV
     KKPQALLELH QEKLKEEKKK KKKKKKHRKS SSDSDDEERK QEKLKKALNA EEARLLHVKE
     IMQIDERKRP YNSIYETREP TEEEMEAYRM KRQRPDDPMA SFLGQ
//
ID   TB10B_MOUSE             Reviewed;         798 AA.
AC   Q8BHL3; Q6GQW9; Q6PIZ5; Q91XR3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=TBC1 domain family member 10B;
DE   AltName: Full=Protein wz3-85;
GN   Name=Tbc1d10b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 180-798.
RC   TISSUE=Spleen;
RA   Tian W., Chua K., Strober W., Chu C.C.;
RT   "Characterization of an unknown wz3-85 gene.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 119-798.
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664 AND SER-693, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-673, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664 AND SER-673, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Acts as GTPase-activating protein for RAB3A, RAB22A,
CC       RAB27A, AND RAB35. Does not act on RAB2A and RAB6A (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 Rab-GAP TBC domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH25889.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=AAH72576.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=AAK82984.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAC33022.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAC33025.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; AK047320; BAC33022.1; ALT_INIT; mRNA.
DR   EMBL; AK047327; BAC33025.1; ALT_INIT; mRNA.
DR   EMBL; AC122537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF285112; AAK82984.1; ALT_INIT; mRNA.
DR   EMBL; BC025889; AAH25889.1; ALT_INIT; mRNA.
DR   EMBL; BC072576; AAH72576.2; ALT_INIT; mRNA.
DR   IPI; IPI00469012; -.
DR   RefSeq; NP_653105.3; NM_144522.5.
DR   UniGene; Mm.41420; -.
DR   ProteinModelPortal; Q8BHL3; -.
DR   SMR; Q8BHL3; 320-598.
DR   PhosphoSite; Q8BHL3; -.
DR   PRIDE; Q8BHL3; -.
DR   Ensembl; ENSMUST00000035643; ENSMUSP00000038318; ENSMUSG00000042492.
DR   Ensembl; ENSMUST00000120705; ENSMUSP00000113307; ENSMUSG00000042492.
DR   GeneID; 68449; -.
DR   KEGG; mmu:68449; -.
DR   CTD; 68449; -.
DR   MGI; MGI:1915699; Tbc1d10b.
DR   eggNOG; roNOG07245; -.
DR   GeneTree; ENSGT00550000074322; -.
DR   HOGENOM; HBG601038; -.
DR   HOVERGEN; HBG070028; -.
DR   InParanoid; Q8BHL3; -.
DR   OrthoDB; EOG4D7Z5V; -.
DR   NextBio; 327197; -.
DR   ArrayExpress; Q8BHL3; -.
DR   Bgee; Q8BHL3; -.
DR   CleanEx; MM_TBC1D10B; -.
DR   Genevestigator; Q8BHL3; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005097; F:Rab GTPase activator activity; ISS:UniProtKB.
DR   GO; GO:0032313; P:regulation of Rab GTPase activity; ISS:UniProtKB.
DR   InterPro; IPR000195; RabGAP/TBC_dom.
DR   Pfam; PF00566; TBC; 1.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; RabGAP_TBC; 2.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; GTPase activation; Phosphoprotein.
FT   CHAIN         1    798       TBC1 domain family member 10B.
FT                                /FTId=PRO_0000315717.
FT   DOMAIN      346    534       Rab-GAP TBC.
FT   COILED      702    769       Potential.
FT   MOD_RES     644    644       Phosphoserine (By similarity).
FT   MOD_RES     647    647       Phosphoserine (By similarity).
FT   MOD_RES     664    664       Phosphoserine.
FT   MOD_RES     673    673       Phosphoserine.
FT   MOD_RES     693    693       Phosphoserine.
FT   MOD_RES     695    695       Phosphothreonine (By similarity).
FT   CONFLICT     31     31       G -> R (in Ref. 1; BAC33022/BAC33025).
FT   CONFLICT    221    221       P -> S (in Ref. 3; AAK82984).
FT   CONFLICT    697    697       N -> S (in Ref. 3; AAK82984).
FT   CONFLICT    751    751       Q -> R (in Ref. 3; AAK82984).
SQ   SEQUENCE   798 AA;  87275 MW;  B9CB616C2BA01913 CRC64;
     METGPAPLVA PPRRHGAPAA PSPPPRGSRA GSHLVVEPGP PVTTATSAPV ELVAPGEARP
     ACVPGSSQTS ASTPTTATSS TVVMLTLEAS PEAAKTQEFP APAAETGAET SVALALGTDT
     QKTEEVRASP VPGPGTPTRT PSRMAPGALT AKPPLAPKPG TTVASGVTAR GGVGQVAGGH
     EAATSASAGS VPEDPSGPVT GPPGTCEAPA PTPVAVVTVT PAPEPVENFQ DLGSTSSLGP
     GISGPRGQAP DTLSYLDSVS LMSGTLESLP DDVSSMGSDS EINGMALRKT DKYGFLGGSQ
     YSGSLESSIP VDVARQRELK WLEMFSNWDK WLSRRFQKVK LRCRKGIPSS LRAKAWQYLS
     NSKELLEQNP GKFEELERAA GDPKWLDVIE KDLHRQFPFH EMFAARGGHG QQDLYRILKA
     YTIYRPDEGY CQAQAPVAAV LLMHMPAEQA FWCLVQICDK YLPGYYSAGL EAIQLDGEIF
     FALLRRVSPL AHRHLRRQRI DPVLYMTEWF MCIFARTLPW ASVLRVWDMF FCEGVKIIFR
     VALVLLRHTL GSVEKLRSCQ GMYETMEQLR NLPQQCMQED FLVHEVTNLP VTEAWIEREN
     AAQLKKWRET RGELQYRPSR RLHGSRAIHE ERRRQQPPLG PSSSLLSLPS LKSRGSRAVG
     GAPSPPPPVR RASAGPVPGA VVIAEGLHPS LPSPTGNSTP LGTSKEIRRQ EKERQKQEKD
     REKERQRQEK ERERQEKERQ KWEKEQEKEQ QKQEKERQKL EKKGQGRKLS LRRRADGPPA
     SHDGGDRSAA EARQDAYF
//
ID   ELMO2_MOUSE             Reviewed;         732 AA.
AC   Q8BHL5; A2A5A6; Q5GMG3; Q8BHL9; Q8BQG1; Q8CBM8; Q8CC50; Q8CH98;
AC   Q91ZU2; Q9CT75;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Engulfment and cell motility protein 2;
DE   AltName: Full=Protein ced-12 homolog A;
GN   Name=Elmo2; Synonyms=Kiaa1834;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C3H;
RX   MEDLINE=21479119; PubMed=11595183; DOI=10.1016/S0092-8674(01)00520-7;
RA   Gumienny T.L., Brugnera E., Tosello-Trampont A.-C., Kinchen J.M.,
RA   Haney L.B., Nishiwaki K., Walk S.F., Nemergut M.E., Macara I.G.,
RA   Francis R., Schedl T., Qin Y., Van Aelst L., Hengartner M.O.,
RA   Ravichandran K.S.;
RT   "CED-12/ELMO, a novel member of the CrkII/Dock180/Rac pathway, is
RT   required for phagocytosis and cell migration.";
RL   Cell 107:27-41(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain, Cerebellum, Diencephalon, Embryo, Eye, Hypothalamus,
RC   Medulla oblongata, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 265-732.
RC   TISSUE=Brain;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-48 AND TYR-729, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-48, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Involved in cytoskeletal rearrangements required for
CC       phagocytosis of apoptotic cells and cell motility. Acts in
CC       assocation with DOCK1 and CRK. Was initially proposed to be
CC       required in complex with DOCK1 to activate Rac Rho small GTPases.
CC       May enhance the guanine nucleotide exchange factor (GEF) activity
CC       of DOCK1 (By similarity).
CC   -!- SUBUNIT: Interacts directly with the SH3-domain of DOCK1 via its
CC       SH3-binding site. Probably forms a heterotrimeric complex with
CC       DOCK1 and RAC1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BHL5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BHL5-2; Sequence=VSP_007488;
CC       Name=3;
CC         IsoId=Q8BHL5-3; Sequence=VSP_007488, VSP_007489;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 ELMO domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF398884; AAL14465.1; -; mRNA.
DR   EMBL; AK004448; BAB23307.1; -; mRNA.
DR   EMBL; AK032033; BAC27662.1; -; mRNA.
DR   EMBL; AK033918; BAC28514.1; -; mRNA.
DR   EMBL; AK035710; BAC29162.1; -; mRNA.
DR   EMBL; AK038455; BAC30007.1; -; mRNA.
DR   EMBL; AK045428; BAC32361.1; -; mRNA.
DR   EMBL; AK047040; BAC32945.1; -; mRNA.
DR   EMBL; AK050823; BAC34424.1; -; mRNA.
DR   EMBL; AK053574; BAC35433.1; -; mRNA.
DR   EMBL; AL591430; CAI51618.2; -; Genomic_DNA.
DR   EMBL; AL591430; CAM23849.1; -; Genomic_DNA.
DR   EMBL; BC023954; AAH23954.1; -; mRNA.
DR   EMBL; AB093301; BAC41483.3; -; Transcribed_RNA.
DR   IPI; IPI00402900; -.
DR   IPI; IPI00468079; -.
DR   IPI; IPI00756692; -.
DR   RefSeq; NP_525026.2; NM_080287.2.
DR   RefSeq; NP_997588.1; NM_207705.1.
DR   RefSeq; NP_997589.1; NM_207706.1.
DR   UniGene; Mm.35064; -.
DR   ProteinModelPortal; Q8BHL5; -.
DR   SMR; Q8BHL5; 535-729.
DR   IntAct; Q8BHL5; 2.
DR   STRING; Q8BHL5; -.
DR   PhosphoSite; Q8BHL5; -.
DR   PRIDE; Q8BHL5; -.
DR   Ensembl; ENSMUST00000071699; ENSMUSP00000071619; ENSMUSG00000017670.
DR   Ensembl; ENSMUST00000074046; ENSMUSP00000073691; ENSMUSG00000017670.
DR   Ensembl; ENSMUST00000094329; ENSMUSP00000091887; ENSMUSG00000017670.
DR   Ensembl; ENSMUST00000103088; ENSMUSP00000099377; ENSMUSG00000017670.
DR   GeneID; 140579; -.
DR   KEGG; mmu:140579; -.
DR   UCSC; uc008nxk.1; mouse.
DR   UCSC; uc008nxl.1; mouse.
DR   UCSC; uc008nxm.1; mouse.
DR   CTD; 140579; -.
DR   MGI; MGI:2153045; Elmo2.
DR   GeneTree; ENSGT00390000014155; -.
DR   HOVERGEN; HBG051463; -.
DR   OMA; LYLAKFH; -.
DR   NextBio; 369891; -.
DR   ArrayExpress; Q8BHL5; -.
DR   Bgee; Q8BHL5; -.
DR   Genevestigator; Q8BHL5; -.
DR   GermOnline; ENSMUSG00000017670; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR006816; Engulfment_cell_motility_ELMO.
DR   InterPro; IPR011993; PH_type.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF04727; ELMO_CED12; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS51335; ELMO; 1.
DR   PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Cytoplasm; Phagocytosis;
KW   Phosphoprotein; SH3-binding.
FT   CHAIN         1    732       Engulfment and cell motility protein 2.
FT                                /FTId=PRO_0000153715.
FT   DOMAIN      323    497       ELMO.
FT   DOMAIN      565    686       PH.
FT   MOTIF       712    719       SH3-binding.
FT   MOD_RES      48     48       Phosphotyrosine.
FT   MOD_RES     729    729       Phosphotyrosine.
FT   VAR_SEQ     253    264       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_007488.
FT   VAR_SEQ     667    732       YCIWIDGLSALLGKDMSSELTKSDLDTLLSMEMKLRLLDLE
FT                                NIQIPEAPPPVPKEPSSYDFVYHYG -> VSSVPHCLEHQC
FT                                PHCEEVSVPHCLEHQCSHCEEVWPAQRYPHKPGSQNGSLSL
FT                                WTFYHWAGLPTSHRGLSSSAFRGLGLELCATTPNLSLCALE
FT                                QLAWHREGFPLCNLAVTFPRRVESQLPGANLVRLWSQMDLP
FT                                LLTRDSQFT (in isoform 3).
FT                                /FTId=VSP_007489.
FT   CONFLICT    102    102       D -> G (in Ref. 2; BAC28514).
FT   CONFLICT    143    144       Missing (in Ref. 1; AAL14465).
FT   CONFLICT    519    523       ILRLR -> NSAVA (in Ref. 2; BAC29162).
FT   CONFLICT    613    613       I -> V (in Ref. 5; BAC41483).
FT   CONFLICT    682    682       M -> I (in Ref. 2; BAC34424).
SQ   SEQUENCE   732 AA;  83887 MW;  087A80728DC43A23 CRC64;
     MPPPSDIVKV AIEWPGANAQ LLEIDQKRPL ASIIKEVCDG WSLPNPEYYT LRYADGPQLY
     VTEQTRNDIK NGTILQLAVS PSRAARQLME RTQSSSMETR LDAMKELAKL SADVTFATEF
     INMDGIIVLT RLVESGTKLL SHYSEMLAFT LTAFLELMDH GIVSWDMVSV TFIKQIAGYV
     SQPMVDVSIL QRSLAILESM VLNSQSLYQK IAEEITVGQL ISHLQVSNQE IQTYAIALIN
     ALFLKAPEDK RQDKHLNPLD LPVTDMANAF AQKHLRSIIL NHVIRGNRPI KTEMAHQLYV
     LQVLTFNLLE ERMMTKMDPN DQAQRDIIFE LRRIAFDAES DPSNVPGSGT EKRKAMYTKD
     YKMLGFTNHI NPALDFTQTP PGMLALDNML YLAKVHQDTY IRIVLENSSR EDKHECPFGR
     SAIELTKMLC EILQVGELPN EGRNDYHPMF FTHDRAFEEL FGICIQLLNK TWKEMRATAE
     DFNKVMQVVR EQITRALPSK PNSLDQFKSK LRSLSYSEIL RLRQSERMSQ DDFQSPPIVE
     LREKIQPEIL ELIKQQRLNR LCEGSSFRKI GNRRRQERFW HCRLALNHKV LHYGDLDDNP
     QGEVTFESLQ EKIPVADIKA IVTGKDCPHM KEKSALKQNK EVLELAFSIL YDPDETLNFI
     APNKYEYCIW IDGLSALLGK DMSSELTKSD LDTLLSMEMK LRLLDLENIQ IPEAPPPVPK
     EPSSYDFVYH YG
//
ID   PSMF1_MOUSE             Reviewed;         271 AA.
AC   Q8BHL8; Q8C0G9;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Proteasome inhibitor PI31 subunit;
GN   Name=Psmf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Colon, Corpora quadrigemina, Oviduct, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Plays an important role in control of proteasome
CC       function. Inhibits the hydrolysis of protein and peptide
CC       substrates by the 20S proteasome. Also inhibits the activation of
CC       the proteasome by the proteasome regulatory proteins PA700 and
CC       PA28 (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SIMILARITY: Belongs to the proteasome inhibitor PI31 family.
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DR   EMBL; AK031363; BAC27368.1; -; mRNA.
DR   EMBL; AK045891; BAC32522.1; -; mRNA.
DR   EMBL; AK053924; BAC35596.1; -; mRNA.
DR   EMBL; AK078867; BAC37430.1; -; mRNA.
DR   IPI; IPI00403055; -.
DR   RefSeq; NP_997611.1; NM_212446.1.
DR   UniGene; Mm.146984; -.
DR   ProteinModelPortal; Q8BHL8; -.
DR   SMR; Q8BHL8; 1-142.
DR   STRING; Q8BHL8; -.
DR   PhosphoSite; Q8BHL8; -.
DR   REPRODUCTION-2DPAGE; Q8BHL8; -.
DR   PRIDE; Q8BHL8; -.
DR   Ensembl; ENSMUST00000042452; ENSMUSP00000041184; ENSMUSG00000032869.
DR   Ensembl; ENSMUST00000109869; ENSMUSP00000105495; ENSMUSG00000032869.
DR   GeneID; 228769; -.
DR   KEGG; mmu:228769; -.
DR   UCSC; uc008nek.1; mouse.
DR   CTD; 228769; -.
DR   MGI; MGI:1346072; Psmf1.
DR   GeneTree; ENSGT00390000012257; -.
DR   HOGENOM; HBG278851; -.
DR   HOVERGEN; HBG053746; -.
DR   InParanoid; Q8BHL8; -.
DR   OMA; HPHTSRQ; -.
DR   OrthoDB; EOG4GHZPQ; -.
DR   PhylomeDB; Q8BHL8; -.
DR   NextBio; 379114; -.
DR   ArrayExpress; Q8BHL8; -.
DR   Bgee; Q8BHL8; -.
DR   Genevestigator; Q8BHL8; -.
DR   GermOnline; ENSMUSG00000032869; Mus musculus.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   InterPro; IPR021625; Inhibitor_PI31.
DR   InterPro; IPR013886; PI31_Prot_Reg.
DR   Pfam; PF11566; Inhibitor_PI31; 1.
DR   Pfam; PF08577; PI31_Prot_Reg; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein; Proteasome.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    271       Proteasome inhibitor PI31 subunit.
FT                                /FTId=PRO_0000220921.
FT   COMPBIAS    154    264       Pro-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     153    153       Phosphoserine.
FT   MOD_RES     251    251       Phosphothreonine (By similarity).
FT   MOD_RES     252    252       Phosphoserine (By similarity).
FT   CONFLICT     78     78       L -> H (in Ref. 1; BAC27368).
SQ   SEQUENCE   271 AA;  29664 MW;  0592EAAE8D90B6B0 CRC64;
     MAGLEVLFAS AAPSMSCPQD ALVCFLHWEV VTNGYYALGT GDQPGPSDKK SELLPAKWNS
     NKELYALRYE SKDGARKLLL KAVSVENGMI INVLELGTQQ VADLTLNLDD YIDAEDLSDF
     HRTYKNSEEL RSQIRSGIIT PIHEQWEKAR ANSPPREFPP ATAREVDPLQ ISSHRPHTSR
     QPAWRDPLSP FAVGGDDLDP FGCQRGGMIV DPLRSGFPRV LIDPSSGLPN RLPPGAVPPG
     ARFDPFGPIG TSPSGPNPDH LPPPGYDDMY L
//
ID   TXLNG_MOUSE             Reviewed;         524 AA.
AC   Q8BHN1; A2AFJ5; Q148Z8; Q2LGB1; Q2PMX1; Q8BP11;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Gamma-taxilin;
DE   AltName: Full=Factor inhibiting ATF4-mediated transcription;
DE            Short=FIAT;
DE   AltName: Full=Lipopolysaccharide-responsive gene protein;
GN   Name=Txlng; Synonyms=Lrg;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF
RP   1-523 (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE
RP   SPLICING, AND INDUCTION.
RX   PubMed=19913514; DOI=10.1016/j.bbrc.2009.11.047;
RA   Du K., Chen Y., Dai Z., Bi Y., Cai T., Hou L., Chai Y., Song Q.,
RA   Chen S., Luo W., Chen J.;
RT   "Molecular cloning and functional characterization of a mouse gene
RT   upregulated by lipopolysaccharide treatment reveals alternative
RT   splicing.";
RL   Biochem. Biophys. Res. Commun. 391:267-271(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex, Head, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=15911876; DOI=10.1083/jcb.200412139;
RA   Yu V.W., Ambartsoumian G., Verlinden L., Moir J.M., Prud'homme J.,
RA   Gauthier C., Roughley P.J., St-Arnaud R.;
RT   "FIAT represses ATF4-mediated transcription to regulate bone mass in
RT   transgenic mice.";
RL   J. Cell Biol. 169:591-601(2005).
RN   [6]
RP   DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX   PubMed=19232401; DOI=10.1016/j.gep.2009.02.002;
RA   Yu V.W., Akhouayri O., St-Arnaud R.;
RT   "FIAT is co-expressed with its dimerization target ATF4 in early
RT   osteoblasts, but not in osteocytes.";
RL   Gene Expr. Patterns 9:335-340(2009).
RN   [7]
RP   FUNCTION.
RX   PubMed=19016261; DOI=10.1002/jcb.21995;
RA   Yu V.W., El-Hoss J., St-Arnaud R.;
RT   "FIAT inhibition increases osteoblast activity by modulating Atf4-
RT   dependent functions.";
RL   J. Cell. Biochem. 106:186-192(2009).
CC   -!- FUNCTION: May be involved in intracellular vesicle traffic (By
CC       similarity). Inhibits ATF4-mediated transcription, possibly by
CC       dimerizing with ATF4 to form inactive dimers that cannot bind DNA.
CC       May be involved in regulating bone mass density through an ATF4-
CC       dependent pathway. May be involved in cell cycle progression.
CC   -!- SUBUNIT: Binds to the C-terminal coiled coil region of syntaxin
CC       family members STX1A, STX3A and STX4A (By similarity). Forms a
CC       heterodimer with ATF4 in osteoblasts.
CC   -!- SUBCELLULAR LOCATION: Nucleus membrane. Cytoplasm, cytosol.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=LrgW;
CC         IsoId=Q8BHN1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BHN1-2; Sequence=VSP_011835, VSP_011836, VSP_011837;
CC         Note=No experimental confirmation available;
CC       Name=3; Synonyms=LrgS;
CC         IsoId=Q8BHN1-3; Sequence=VSP_011835;
CC   -!- DEVELOPMENTAL STAGE: At E16.5, expressed in osteoblasts
CC       surrounding newly formed trabecular bone. At postnatal day 2,
CC       detected in most osteoblasts and lining cells, and also strongly
CC       expressed in osteocytes. By postnatal week 4, strongly expressed
CC       in osteocytes (at protein level).
CC   -!- INDUCTION: By LPS.
CC   -!- SIMILARITY: Belongs to the taxilin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABC47035.1; Type=Erroneous termination; Positions=518; Note=Translated as Gln;
CC       Sequence=ABC47035.1; Type=Frameshift; Positions=520;
CC       Sequence=ABC60327.1; Type=Erroneous termination; Positions=518; Note=Translated as Gln;
CC       Sequence=ABC60327.1; Type=Frameshift; Positions=520;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; DQ316984; ABC47035.1; ALT_SEQ; mRNA.
DR   EMBL; DQ320011; ABC60327.1; ALT_SEQ; mRNA.
DR   EMBL; AK030100; BAC26785.1; -; mRNA.
DR   EMBL; AK031783; BAC27547.1; -; mRNA.
DR   EMBL; AK044130; BAC31791.1; -; mRNA.
DR   EMBL; AK078477; BAC37296.1; -; mRNA.
DR   EMBL; AL672123; CAM24319.1; -; Genomic_DNA.
DR   EMBL; AL672123; CAM24320.1; -; Genomic_DNA.
DR   EMBL; BC117898; AAI17899.1; -; mRNA.
DR   EMBL; BC117899; AAI17900.1; -; mRNA.
DR   IPI; IPI00474617; -.
DR   IPI; IPI00474869; -.
DR   IPI; IPI00831011; -.
DR   RefSeq; NP_849266.1; NM_178935.4.
DR   UniGene; Mm.270186; -.
DR   UniGene; Mm.371732; -.
DR   ProteinModelPortal; Q8BHN1; -.
DR   STRING; Q8BHN1; -.
DR   PhosphoSite; Q8BHN1; -.
DR   PRIDE; Q8BHN1; -.
DR   Ensembl; ENSMUST00000041370; ENSMUSP00000038615; ENSMUSG00000038344.
DR   GeneID; 353170; -.
DR   KEGG; mmu:353170; -.
DR   UCSC; uc009uuh.1; mouse.
DR   UCSC; uc009uul.1; mouse.
DR   CTD; 353170; -.
DR   MGI; MGI:3590652; Txlng.
DR   GeneTree; ENSGT00390000001482; -.
DR   HOGENOM; HBG443670; -.
DR   HOVERGEN; HBG104385; -.
DR   InParanoid; Q8BHN1; -.
DR   OMA; RQKFEIG; -.
DR   OrthoDB; EOG49GKGR; -.
DR   PhylomeDB; Q8BHN1; -.
DR   NextBio; 400319; -.
DR   ArrayExpress; Q8BHN1; -.
DR   Bgee; Q8BHN1; -.
DR   CleanEx; MM_4932441K18RIK; -.
DR   Genevestigator; Q8BHN1; -.
DR   GermOnline; ENSMUSG00000038344; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR019132; Taxilin.
DR   Pfam; PF09728; Taxilin; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Coiled coil; Cytoplasm; Membrane;
KW   Nucleus; Phosphoprotein; Transcription; Transcription regulation.
FT   CHAIN         1    524       Gamma-taxilin.
FT                                /FTId=PRO_0000189427.
FT   COILED      153    465       Potential.
FT   MOD_RES      86     86       Phosphoserine (By similarity).
FT   MOD_RES      97     97       Phosphoserine (By similarity).
FT   MOD_RES     386    386       Phosphothreonine (By similarity).
FT   MOD_RES     512    512       Phosphoserine (By similarity).
FT   VAR_SEQ      55    103       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_011835.
FT   VAR_SEQ     289    290       HI -> VI (in isoform 2).
FT                                /FTId=VSP_011836.
FT   VAR_SEQ     291    524       Missing (in isoform 2).
FT                                /FTId=VSP_011837.
FT   CONFLICT     72     72       G -> D (in Ref. 1; ABC47035).
FT   CONFLICT     84     84       E -> D (in Ref. 1; ABC47035).
FT   CONFLICT    306    306       A -> G (in Ref. 1; ABC47035/ABC60327).
FT   CONFLICT    446    446       N -> T (in Ref. 1; ABC60327).
FT   CONFLICT    494    494       L -> W (in Ref. 1; ABC47035).
FT   CONFLICT    514    514       G -> S (in Ref. 1; ABC60327).
SQ   SEQUENCE   524 AA;  60309 MW;  0228777633E4ED7C CRC64;
     MATRLEEVTR GRGGGTEEAS EGGRGGRRRS PPQKFEIGTM EEARICGLGV KADMVCNSQA
     NDILQHQDPS CGGTTKKHSL EGDEGSDFIT KNRNLVSSVF CTQEKREEIP GREARTGPPD
     GQQDSECSRN KEKTLGKEVL LLMQALNTLS TPEEKLAALC KKYADLLEES RNVQKQMKIL
     QKKQAQIVKE KVHLQSEHSK AILARSKLES LCRELQRHNK TLKEENMQQA REEEERRKEA
     TAHFQITLNE IQAQLEQHDI HNAKLRQENI ELGEKLKKLI EQYALREEHI DKVFKHKELQ
     QQLVDAKLQQ TTQLIKEADE KHQREREFLL KEATESRHKY EQMKQQEVQL KQQLSLYMDK
     FEEFQTTMAK SNELFTTFRQ EMEKMTKKIK KLEKETIIWR TKWENNNKAL LQMAEEKTVR
     DKEYKAFQIK LERLEKLCRA LQTERNELNE KVEVLKEQVS IKAADGDLVS PATQPCAVLD
     SFKETSRRTL GMHLEARAKS VCEKSAAQKP SSSGSPAQGI ESVD
//
ID   ARMX3_MOUSE             Reviewed;         379 AA.
AC   Q8BHS6; A2AKS4; Q91VP8; Q9DC32;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Armadillo repeat-containing X-linked protein 3;
GN   Name=Armcx3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Contains 3 ARM repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK004598; BAB23399.1; -; mRNA.
DR   EMBL; AK030729; BAC27102.1; -; mRNA.
DR   EMBL; AL772348; CAM20585.1; -; Genomic_DNA.
DR   EMBL; BC011101; AAH11101.1; -; mRNA.
DR   EMBL; BC051113; AAH51113.1; -; mRNA.
DR   IPI; IPI00308332; -.
DR   RefSeq; NP_082146.2; NM_027870.3.
DR   UniGene; Mm.425471; -.
DR   UniGene; Mm.67949; -.
DR   ProteinModelPortal; Q8BHS6; -.
DR   SMR; Q8BHS6; 117-233.
DR   STRING; Q8BHS6; -.
DR   PhosphoSite; Q8BHS6; -.
DR   PRIDE; Q8BHS6; -.
DR   Ensembl; ENSMUST00000081834; ENSMUSP00000080518; ENSMUSG00000049047.
DR   Ensembl; ENSMUST00000086880; ENSMUSP00000084093; ENSMUSG00000049047.
DR   Ensembl; ENSMUST00000086884; ENSMUSP00000084097; ENSMUSG00000049047.
DR   GeneID; 71703; -.
DR   KEGG; mmu:71703; -.
DR   UCSC; uc009ugo.1; mouse.
DR   CTD; 71703; -.
DR   MGI; MGI:1918953; Armcx3.
DR   GeneTree; ENSGT00550000074488; -.
DR   HOGENOM; HBG127433; -.
DR   HOVERGEN; HBG080349; -.
DR   InParanoid; Q8BHS6; -.
DR   OMA; LAENPAM; -.
DR   OrthoDB; EOG41G34H; -.
DR   PhylomeDB; Q8BHS6; -.
DR   NextBio; 457769; -.
DR   ArrayExpress; Q8BHS6; -.
DR   Bgee; Q8BHS6; -.
DR   CleanEx; MM_ARMCX3; -.
DR   Genevestigator; Q8BHS6; -.
DR   GermOnline; ENSMUSG00000049047; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR006911; DUF634.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF04826; DUF634; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 1.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN         1    379       Armadillo repeat-containing X-linked
FT                                protein 3.
FT                                /FTId=PRO_0000191368.
FT   TRANSMEM      7     29       Helical; (Potential).
FT   REPEAT      111    151       ARM 1.
FT   REPEAT      153    192       ARM 2.
FT   REPEAT      233    272       ARM 3.
FT   MOD_RES      61     61       Phosphoserine.
FT   MOD_RES      67     67       Phosphoserine (By similarity).
FT   CONFLICT      4      4       A -> T (in Ref. 3; AAH11101).
FT   CONFLICT     53     53       S -> P (in Ref. 1; BAB23399).
FT   CONFLICT     68     68       N -> Y (in Ref. 1; BAB23399).
FT   CONFLICT    333    333       L -> P (in Ref. 1; BAB23399).
SQ   SEQUENCE   379 AA;  42620 MW;  6EA7B87544652055 CRC64;
     MGYARKVGWV TAGLVIGAGA CYCIYRLTRG RKQNKEKMAE GGSGDVDDAG DCSGARYNDW
     SDDDDDSNES KSIVWYPPWA RIGTEAGTRA RARARARATR ARRAVQKRAS PNSDDTVLSP
     QELQKVLCLV EMSEKPYILE AALIALGNNA AYAFNRDIIR DLGGLPIVAK ILNTRDPIVK
     EKALIVLNNL SVNAENQRRL KVYMNQVCDD TVTSRLNSSV QLAGLRLLTN MTVTNEYQHI
     LANSISDFFR LFSAGNEETK LQVLKLLLNL AENPAMTREL LRAQVPSSLG SLFNKKEYKE
     VILKLLIIFE NINDNFKWEE NEPAQNHFSE GSLFFFLKEF QVCADKVLGI ESRHDFQVRV
     KVGKFVAKLT ERMFPKSQE
//
ID   SYBU_MOUSE              Reviewed;         665 AA.
AC   Q8BHS8; Q3TQN7; Q401F3; Q401F4; Q571C1; Q6P1J2; Q80XH0; Q8BHS7;
AC   Q8BI27;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Syntabulin;
DE   AltName: Full=Golgi-localized syntaphilin-related protein;
DE            Short=m-Golsyn;
DE   AltName: Full=Syntaxin-1-binding protein;
GN   Name=Sybu; Synonyms=Golsyn, Kiaa1472;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4).
RC   TISSUE=Brain;
RX   PubMed=15656992; DOI=10.1016/j.gene.2004.10.024;
RA   Funakoshi E., Nakagawa K.-Y., Hamano A., Hori T., Shimizu A.,
RA   Asakawa S., Shimizu N., Ito F.;
RT   "Molecular cloning and characterization of gene for Golgi-localized
RT   syntaphilin-related protein on human chromosome 8q23.";
RL   Gene 344:259-271(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Corpora quadrigemina, Embryo, Pituitary anterior lobe, and
RC   Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pancreatic islet;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 6).
RC   STRAIN=C57BL/6; TISSUE=Eye, and Fetal brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
CC   -!- FUNCTION: Part of a kinesin motor-adapter complex that is critical
CC       for the anterograde axonal transport of active zone components and
CC       contributes to activity-dependent presynaptic assembly during
CC       neuronal development (By similarity).
CC   -!- SUBUNIT: Interacts with STX1A and KIF5B (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass
CC       membrane protein (By similarity). Note=Colocalizes with syntaxin
CC       vesicles along microtubules in neuronal processes (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q8BHS8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BHS8-2; Sequence=VSP_019727;
CC       Name=3; Synonyms=Golsyn B;
CC         IsoId=Q8BHS8-3; Sequence=VSP_019725, VSP_019728;
CC       Name=4; Synonyms=Golsyn A;
CC         IsoId=Q8BHS8-4; Sequence=VSP_019726;
CC       Name=5;
CC         IsoId=Q8BHS8-5; Sequence=VSP_019724;
CC       Name=6;
CC         IsoId=Q8BHS8-6; Sequence=VSP_019723;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90193.1; Type=Erroneous initiation;
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DR   EMBL; AB232447; BAE19961.1; -; mRNA.
DR   EMBL; AB232448; BAE19962.1; -; mRNA.
DR   EMBL; AB232449; BAE19963.1; -; mRNA.
DR   EMBL; AK029072; BAC26277.1; -; mRNA.
DR   EMBL; AK030482; BAC26984.1; -; mRNA.
DR   EMBL; AK030720; BAC27098.1; -; mRNA.
DR   EMBL; AK163432; BAE37345.1; -; mRNA.
DR   EMBL; AK220268; BAD90193.1; ALT_INIT; mRNA.
DR   EMBL; BC048945; AAH48945.1; -; mRNA.
DR   EMBL; BC065045; AAH65045.1; -; mRNA.
DR   IPI; IPI00221955; -.
DR   IPI; IPI00651917; -.
DR   IPI; IPI00654139; -.
DR   IPI; IPI00761601; -.
DR   IPI; IPI00762188; -.
DR   IPI; IPI00762632; -.
DR   RefSeq; NP_001027899.1; NM_001032727.1.
DR   RefSeq; NP_795972.2; NM_176998.4.
DR   RefSeq; NP_848880.2; NM_178765.3.
DR   UniGene; Mm.207715; -.
DR   ProteinModelPortal; Q8BHS8; -.
DR   STRING; Q8BHS8; -.
DR   PhosphoSite; Q8BHS8; -.
DR   PRIDE; Q8BHS8; -.
DR   Ensembl; ENSMUST00000090057; ENSMUSP00000087511; ENSMUSG00000022340.
DR   Ensembl; ENSMUST00000110267; ENSMUSP00000105896; ENSMUSG00000022340.
DR   Ensembl; ENSMUST00000110269; ENSMUSP00000105898; ENSMUSG00000022340.
DR   GeneID; 319613; -.
DR   KEGG; mmu:319613; -.
DR   UCSC; uc007vqc.1; mouse.
DR   UCSC; uc007vqd.1; mouse.
DR   UCSC; uc007vqf.1; mouse.
DR   UCSC; uc007vqg.1; mouse.
DR   UCSC; uc007vqh.1; mouse.
DR   CTD; 319613; -.
DR   MGI; MGI:2442392; Sybu.
DR   eggNOG; roNOG13556; -.
DR   GeneTree; ENSGT00520000055634; -.
DR   HOVERGEN; HBG006785; -.
DR   InParanoid; Q8BHS8; -.
DR   OMA; NIHPSYA; -.
DR   OrthoDB; EOG4ZS930; -.
DR   NextBio; 395080; -.
DR   ArrayExpress; Q8BHS8; -.
DR   Bgee; Q8BHS8; -.
DR   CleanEx; MM_5730410E15RIK; -.
DR   Genevestigator; Q8BHS8; -.
DR   GermOnline; ENSMUSG00000022340; Mus musculus.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Golgi apparatus; Membrane;
KW   Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    665       Syntabulin.
FT                                /FTId=PRO_0000245510.
FT   TRANSMEM    609    629       Helical; (Potential).
FT   REGION        2    421       Sufficient for interaction with KIF5B (By
FT                                similarity).
FT   REGION      314    421       Sufficient for interaction with STX1A (By
FT                                similarity).
FT   COILED      275    357       Potential.
FT   COMPBIAS     46    245       Ser-rich.
FT   MOD_RES     199    199       Phosphoserine (By similarity).
FT   MOD_RES     557    557       Phosphoserine.
FT   VAR_SEQ       1    167       Missing (in isoform 6).
FT                                /FTId=VSP_019723.
FT   VAR_SEQ       1    123       Missing (in isoform 5).
FT                                /FTId=VSP_019724.
FT   VAR_SEQ       1     72       Missing (in isoform 3).
FT                                /FTId=VSP_019725.
FT   VAR_SEQ       1      1       M -> MRPHLPVQSLRPPATVPTCSEAPGAAVLAPEVKRPR
FT                                GPERAGSCRTTCANRAGGAGGAGRGWFLQPQRKPLATRCVA
FT                                GRRPSPAQASRAFGDTVWTAQWTRSAKETVPPPGRRRRRQR
FT                                RRGEPAGSSEM (in isoform 4).
FT                                /FTId=VSP_019726.
FT   VAR_SEQ       8      8       Missing (in isoform 2).
FT                                /FTId=VSP_019727.
FT   VAR_SEQ      73     80       ISSNSFCS -> MDTVCKGN (in isoform 3).
FT                                /FTId=VSP_019728.
FT   CONFLICT    210    210       S -> C (in Ref. 2; BAC27098).
FT   CONFLICT    458    458       S -> T (in Ref. 2; BAC27098).
FT   CONFLICT    548    548       R -> G (in Ref. 2; BAE37345).
SQ   SEQUENCE   665 AA;  73024 MW;  2DADB83A2BE20BBD CRC64;
     MGPLRESKKE QRVQHQEKEI SRSRIPRLIL RPHRPQQQQQ QQNKVSPASE SPFSEEESRE
     FNPSSSGRSA RTISSNSFCS DDTGCPSSQS VSPVKTPSDT GHSPIGFCPG SDEDFTRKKC
     RIGMVGEGSI QSARHKKEPK GGIIKPGSEA DFSSSSSTGS ISAPEVHMST TGNKRASFSR
     NRGPHGRSNG ASSHKSGSSP PSPREKDLVS MLCRNPLSPS NIHPSYAPSS PSSSNSGSYK
     GSDCSPVMRR SGRYMSCGEN HGVKPPNPEQ YLTPLQQKEV TVRHLRTKLK ESERRLHERE
     SEIMELKSQL ARMREDWIEE ECHRVEAQLA LKEARKEIKQ LKQVIETMRS SLADKDKGIQ
     KYFVDINIQN KKLESLLQSM EMAHNSSLRD ELCLDFSFDS PEKSLPLSST FDKLPDGLSL
     EEQITEEGAD SELLVGDSMA EGTDLLDEMV TATTTESSGL EFVHSTPGPQ ALKALPLVSH
     EEGIAVMEQA VQTDVVPFSP AISELIQSVL KLQDYCPTSS ASPDESGADS MESFSESISA
     LMLDLTPRSP NSAILLSPVE IPFSKGAMEA HANRLMRELD FAAYTEERLD SVLSLSQGSV
     VRQYWSSNFL VDLLAVAAPV VPTVLWAFST QRGGTDPVYN IGALLRGCCV VALHSLRRTA
     FHMKT
//
ID   Q8BHZ1_MOUSE            Unreviewed;       495 AA.
AC   Q8BHZ1;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 2.
DT   08-FEB-2011, entry version 45.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Snx14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK046839; BAC32893.2; -; mRNA.
DR   IPI; IPI00222042; -.
DR   UniGene; Mm.439873; -.
DR   STRING; Q8BHZ1; -.
DR   PhosphoSite; Q8BHZ1; -.
DR   Ensembl; ENSMUST00000034995; ENSMUSP00000034995; ENSMUSG00000032422.
DR   UCSC; uc009qyn.1; mouse.
DR   MGI; MGI:2155664; Snx14.
DR   GeneTree; ENSGT00530000062922; -.
DR   HOVERGEN; HBG056713; -.
DR   InParanoid; Q8BHZ1; -.
DR   ArrayExpress; Q8BHZ1; -.
DR   Bgee; Q8BHZ1; -.
DR   Genevestigator; Q8BHZ1; -.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   InterPro; IPR003114; Phox_assoc.
DR   InterPro; IPR000342; Regulat_G_prot_signal.
DR   InterPro; IPR016137; Regulat_G_prot_signal_superfam.
DR   Pfam; PF02194; PXA; 1.
DR   Pfam; PF00615; RGS; 1.
DR   SUPFAM; SSF48097; Regulat_G_prot_signal_superfam; 1.
DR   PROSITE; PS51207; PXA; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   2: Evidence at transcript level;
FT   NON_TER     495    495
SQ   SEQUENCE   495 AA;  57685 MW;  5B0F7D9BCC4867DC CRC64;
     MGSWVRTICG RLKQRLRLDV GREICRQYPL FCFLLLCLSV ASLLLNRYLH VLMIFWSFVA
     GVVTFYCSLG PDSLLPNIFF TIKYKPKQLG LQELFPQGHS CAVCGKVKCK RHRPSLLLEN
     YQPWLDLKVS SKVDASLSEV LELVLENFVY PWYRDVTDDE SFVDELRITL RFFASVLVRR
     IHKVDIPSII TKKLLKAAMK HIEVIVKARQ KVKNTEYLQQ AGLEEYGPEL HVALRSRRDE
     LQYLRKLTEL LFPYILPPKA TDCRSLTLLI REILSGSVLL PSLDFLADPD TVNHLLIIFI
     DDSPPEKATE PASPLVPFLQ KFAEPRNKKP SVLKLELKQI REQQDLLFRF MNFLKQEGAV
     HVLQFCLTVE EFNDRILRPE LSNDEMLSLH EELQKIYKTY CLDESIDKIR FDPFIVEEIQ
     RIAEGPYIDV VKLQTMRCLF EAYEHVLSLL ENVFTPMFCH SDEYFRQLLR GAESPTRNSK
     FNRGSLSLDD FRSTR
//
ID   Q8BI47_MOUSE            Unreviewed;       736 AA.
AC   Q8BI47;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 68.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Pde8b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK083166; BAC38791.1; -; mRNA.
DR   IPI; IPI00221980; -.
DR   RefSeq; NP_758467.2; NM_172263.2.
DR   UniGene; Mm.100167; -.
DR   HSSP; Q07343; 1F0J.
DR   ProteinModelPortal; Q8BI47; -.
DR   SMR; Q8BI47; 396-724.
DR   STRING; Q8BI47; -.
DR   PRIDE; Q8BI47; -.
DR   Ensembl; ENSMUST00000022192; ENSMUSP00000022192; ENSMUSG00000021684.
DR   Ensembl; ENSMUST00000162292; ENSMUSP00000124068; ENSMUSG00000021684.
DR   GeneID; 218461; -.
DR   KEGG; mmu:218461; -.
DR   UCSC; uc007rma.1; mouse.
DR   CTD; 218461; -.
DR   MGI; MGI:2443999; Pde8b.
DR   GeneTree; ENSGT00590000082978; -.
DR   HOGENOM; HBG715538; -.
DR   HOVERGEN; HBG053544; -.
DR   InParanoid; Q8BI47; -.
DR   OMA; GSDCECN; -.
DR   PhylomeDB; Q8BI47; -.
DR   ArrayExpress; Q8BI47; -.
DR   Bgee; Q8BI47; -.
DR   Genevestigator; Q8BI47; -.
DR   GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000156; F:two-component response regulator activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR003607; Metal-dep_PHydrolase_HD_dom.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR023174; PDEase_CS.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Gene3D; G3DSA:1.10.1300.10; PDEase_catalytic_dom; 1.
DR   Pfam; PF00233; PDEase_I; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00471; HDc; 1.
DR   PROSITE; PS00126; PDEASE_I; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding.
SQ   SEQUENCE   736 AA;  82610 MW;  375577078FECA2D8 CRC64;
     MPPSRAAGPP GAVRVRRSRA ELGSGSSTGS SGPATTTCRG RRRHCCSSAE AETQTSYTSV
     KQVSSAEVRI GPMRLTQDPI QVLLIFAKED SQSDGFWWAC DRAGYRCNIA RTPESALECF
     LDKHHEIIVI DHRQSRNFDA EAVCRSIRAT NPSEHTVILA VVSQASDDHE EASVLPLLHA
     GFNRRFMENS SIIACYNELI QIEHGEVRSQ FKLRACNSVF TALDHCHEAI EITSDDHVIQ
     IHRIHRDSGD NSQTEPHSFR HKSRRKESID VKSISSRGSD APSLQNRRYP SMARIHSMTI
     EAPITKVINI INAAQENSPV TVAEALDRVL EILRTTELYS PQLGTKDEDP HTSDLVGGLM
     TDGLRRLSGN EYVFTKNVHH SHSHLSMPIT INDVPPSIAQ LLDNEESWDF NIFELEAVTH
     KRPLVYLGLK VFSRFGVCEF LNCTETTLRA WLQVIEANYH SSNAYHNSTH AADVLHATAF
     FLGKERVKGS LDQLDEVAAL IAATVHDVDH PGRTNSFLCN AGSELAVLYN DTAVLESHHT
     ALAFQLTVKD TKCNIFKNID RNHYRTLRQA IIDMVLATEM TKHFEHVNKF VNSINKPLAA
     ESEGSDCECN PTGKNFPENQ ILIKRMMIKC ADVANPCRPL DLCIEWAGRI SEEYFAQTDE
     EKRQGLPVVM PVFDRNTCSI PKSQISFIDY FITDMFDAWD AFAHLPALMQ HLADNYKHWK
     TLDDLKCKTL RLPSDS
//
ID   MIA3_MOUSE              Reviewed;        1930 AA.
AC   Q8BI84; A0JLX8; Q3UFI9; Q571D7; Q8BJE9; Q8BL31; Q8C5B9;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Melanoma inhibitory activity protein 3;
DE   AltName: Full=Transport and Golgi organization protein 1;
DE            Short=TANGO1;
DE   Flags: Precursor;
GN   Name=Mia3; Synonyms=Kiaa0268;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-1382 (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1726-1930 (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cecum, Corpora quadrigemina, Fetal eye, Pancreas, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1467-1930.
RC   TISSUE=Pancreatic islet;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1469-1930.
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   IDENTIFICATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=15183315; DOI=10.1016/j.modgep.2003.12.002;
RA   Bosserhoff A.K., Moser M., Buettner R.;
RT   "Characterization and expression pattern of the novel MIA homolog
RT   TANGO.";
RL   Gene Expr. Patterns 4:473-479(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-371, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820; SER-1754; SER-1764;
RP   SER-1765; SER-1915 AND SER-1918, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1915, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Required for collagen VII (COL7A1) secretion by loading
CC       COL7A1 into transport carriers. May participate in cargo loading
CC       of COL7A1 at endoplasmic reticulum exit sites by binding to COPII
CC       coat subunits Sec23/24 and guiding SH3-bound COL7A1 into a growing
CC       carrier. Does not play a role in global protein secretion and is
CC       apparently specific to COL7A1 cargo loading. However, it may
CC       participate in secretion of other proteins in cells that do not
CC       secrete COL7A1 (By similarity).
CC   -!- SUBUNIT: Interacts (via SH3 domain) with COL7A1. Associates with
CC       the COPII coat subunits Sec23/Sec24 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       type I membrane protein (By similarity). Note=Localizes at
CC       endoplasmic reticulum exit sites. After loading of COL7A1 into
CC       transport carriers, it is not incorporated into COPII carriers and
CC       remains in the endoplasmic reticulum membrane (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BI84-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BI84-2; Sequence=VSP_025867, VSP_025868;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8BI84-3; Sequence=VSP_025865, VSP_025866;
CC   -!- DEVELOPMENTAL STAGE: Ubiquitously expressed during embryogenesis,
CC       starting at E8.
CC   -!- DOMAIN: The proline-rich region (PRD) mediates the interaction
CC       with COPII coat subunits Sec23/24 (By similarity).
CC   -!- DOMAIN: Although 2 transmembrane domains are predicted, it only
CC       contains one transmembrane domain. The other predicted
CC       transmembrane region is probably a hairpin-type region embedded
CC       into the membrane, which does not cross the membrane. It is
CC       unclear which of the 2 predicted transmembrane regions is the
CC       transmembrane or the hairpin-type region.
CC   -!- SIMILARITY: Belongs to the MIA/OTOR family. Tango1 subfamily.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; AK044749; BAC32064.1; -; mRNA.
DR   EMBL; AK046506; BAC32759.1; -; mRNA.
DR   EMBL; AK078951; BAC37474.1; -; mRNA.
DR   EMBL; AK084344; BAC39164.1; -; mRNA.
DR   EMBL; AK148470; BAE28571.1; ALT_TERM; mRNA.
DR   EMBL; CAAA01083517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK220252; BAD90177.1; -; mRNA.
DR   EMBL; BC125472; AAI25473.1; -; mRNA.
DR   IPI; IPI00222037; -.
DR   IPI; IPI00845556; -.
DR   IPI; IPI00850156; -.
DR   RefSeq; NP_796363.2; NM_177389.3.
DR   UniGene; Mm.41152; -.
DR   HSSP; Q15080; 1W70.
DR   ProteinModelPortal; Q8BI84; -.
DR   SMR; Q8BI84; 46-105, 1608-1637.
DR   STRING; Q8BI84; -.
DR   PhosphoSite; Q8BI84; -.
DR   PRIDE; Q8BI84; -.
DR   Ensembl; ENSMUST00000069922; ENSMUSP00000064801; ENSMUSG00000056050.
DR   GeneID; 338366; -.
DR   KEGG; mmu:338366; -.
DR   CTD; 338366; -.
DR   MGI; MGI:2443183; Mia3.
DR   eggNOG; roNOG15246; -.
DR   GeneTree; ENSGT00530000063635; -.
DR   HOVERGEN; HBG108133; -.
DR   InParanoid; Q8BI84; -.
DR   OrthoDB; EOG4JM7PQ; -.
DR   NextBio; 400163; -.
DR   Bgee; Q8BI84; -.
DR   CleanEx; MM_MIA3; -.
DR   Genevestigator; Q8BI84; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; ISS:UniProtKB.
DR   GO; GO:0006887; P:exocytosis; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50002; SH3; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Endoplasmic reticulum;
KW   ER-Golgi transport; Exocytosis; Glycoprotein; Membrane;
KW   Phosphoprotein; Protein transport; SH3 domain; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25   1930       Melanoma inhibitory activity protein 3.
FT                                /FTId=PRO_0000288999.
FT   TOPO_DOM     25   1171       Extracellular (Potential).
FT   INTRAMEM   1172   1192       Potential.
FT   TOPO_DOM   1193   1202       Extracellular (Potential).
FT   TRANSMEM   1203   1223       Helical; (Potential).
FT   TOPO_DOM   1224   1930       Cytoplasmic (Potential).
FT   DOMAIN       45    107       SH3.
FT   COILED     1236   1329       Potential.
FT   COILED     1359   1422       Potential.
FT   COILED     1514   1662       Potential.
FT   COMPBIAS    317    324       Poly-Glu.
FT   COMPBIAS    693    699       Poly-Glu.
FT   COMPBIAS   1020   1110       Pro-rich.
FT   COMPBIAS   1667   1916       Pro-rich.
FT   MOD_RES     362    362       Phosphoserine.
FT   MOD_RES     371    371       Phosphothreonine.
FT   MOD_RES     820    820       Phosphoserine.
FT   MOD_RES    1754   1754       Phosphoserine.
FT   MOD_RES    1764   1764       Phosphoserine.
FT   MOD_RES    1765   1765       Phosphoserine.
FT   MOD_RES    1915   1915       Phosphoserine.
FT   MOD_RES    1918   1918       Phosphoserine.
FT   CARBOHYD    360    360       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    631    631       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1   1149       Missing (in isoform 3).
FT                                /FTId=VSP_025865.
FT   VAR_SEQ    1150   1186       GDVQKQLETIAEEPAAVPPLESAFGSLYAFILYLSKM ->
FT                                MDSLPATVPAVTASPGDPELLGPLSVLYAALIAKLLE (in
FT                                isoform 3).
FT                                /FTId=VSP_025866.
FT   VAR_SEQ    1232   1239       KSRVYQVT -> SKLNYLIT (in isoform 2).
FT                                /FTId=VSP_025867.
FT   VAR_SEQ    1240   1930       Missing (in isoform 2).
FT                                /FTId=VSP_025868.
SQ   SEQUENCE   1930 AA;  213675 MW;  7C80FC1260136D7F CRC64;
     MAAAPGLLFW LFVLGALWWV PGQSDLSHGR RFSDLKVCGD EECSMLMYRG KALEDFTGPD
     CRFVNFKKGD DVYVYYKLAG GSLELWAGSV EHSFGYFPKD LIKVLHKYTE EELHIPADET
     DFVCFEGGRD DFNSYNVEEL LGSLELEDSV PEESKKAEEV SQHREKSPEE SRGRELDPVP
     EPEAFRADSE DGEGAFSEST EGLQGQPSAQ ESHPHTSGPA ANAQGVQSSL DTFEEILHDK
     LKVPGSESRT GNSSPASVER EKTDAYKVLK TEMSLDLKTK FGSTADALVS DDEATRLVTS
     LEDGFDEALD AEYYPMEEEE EVEEDADSSD ELPLLTFSDK DEKVPGKPMI EKYLTDKDPN
     LSEEDKVEPP TWGDAFFSIV TGGEGKPGVV DLERSIEEEE DVSVSSSHQR KPQPAAGYTD
     SEDEGDDLFV EEPKTNDVKD SETDPELVIT GEEKDIQESR KGLVQPESQS EDAKSETASA
     YRLQGSKLNP LSAAEKGRDF TLKAVFEKKE NGLKESVIHI SKETLHEDKT REIQRDSLES
     ELVHRALGSS VTENNKPKSL GVAPLLGNNK PDASKDSTEV PDGSVSGPKA GQQEGFLEPG
     LKTQHQPRFS PPEETGPSRE LGGKVPISGR NLSWQQEQDV AAVVGKHANE KTGFPEEESR
     EDGTDAEQAR AIRRPQEAES PEVLSVQPGR PDEEEEEEEG DNYPPEGLME DENAVSAQQS
     RENSPSARDG RSDMNSQVFE KVILGTLNLN TEKTKQPANM ILETGQESET TSEEAGDVGK
     ESGHSVVVDS EESHLADMRA QRPSQVHGLR DETAAQTPGS GEAVLSKNPN DLQKDNPEEE
     LVNTLGLEDP GVGEISEGEP EDTKEFGVSE SQGTDAEDLR DDPSRQATPE IPDIVLKSIR
     EDLPIINSFF KDDQQSLHRF LKYFDVRELE GLLEDMSIRL RSAHQNSLPY NMEKVLDKVF
     RASESRILSM AEKMLDTGVA KNRDLGSKES SPLEEAEVLD DIQDLIYFVR YQYSGVETAP
     LVTPPPPEEG WARPGEERQP PQQDSLPQEN TGDLSVQPPE EPELSDQPVT SVQPPEEPEL
     SDQPVTSVQP PEEPELSDQP VTSVQPPEEP ELSDQPVTGY TSTSEVSQKP DTKKDIDLGP
     VMEGGPVGAG DVQKQLETIA EEPAAVPPLE SAFGSLYAFI LYLSKMLLAT LPDNVQPGPD
     FYGLPWQPVI ITAVLGIVSF AIFSWRTILV VKSRVYQVTE KQISEKLENI KKENAELMQK
     LSSYEQKIKE SKKYVQETKK QNMILSDEAV KYKDKIKILE ETNVSLGDKA KSLRLQLESE
     REQNVKNQDL ILENKKSIEK LKDVISMNAS ELSEVQVALN EAKLSEENVK SECHRVQEEN
     ARLKKKKEQL QQQVEEWSKS HAELTGQIKS FEKSQEDLEI ALTHKDDNIS ALTNCITQLN
     RLECELESED PDKGGNESDD LANGETGGDR SEKIRNRIKQ MMDVSRTQTA VSIVEEDLKL
     LQLKLRASMS TKCNLEDQIK KLEDDRSSLQ TAKAGLEDEC KTLRQKVEIL NELYQQKEMA
     LQKKLSQEEY ERQDREQRLT AADEKVVLAA EEVKTYKRRI EEMEEELQKT ERSFKNQIAA
     HEKKAHDNWL KARAAERAMA EEKREAANLR HKLLEMTQKM AMRQDEPVIV KPMPGRPNTQ
     NPPRRGLLSQ NGSFGPSPVS GGECSPPLPA EPPGRPLSAT LSRRDTPRSE FGSLDRHLPR
     PRWPSEASGK HSASDPGPAP VVNSSSRSSS PAKAVDEGKV NMAPKGPPPF PGVPLMGGPV
     PPPIRYGPPP QLCGGPFGPR PLPPPFVPGM HPPLGVREYA PGVLPGKRDL PLDPREFLPG
     HTPFRPPGSL GPREFFIPGT RLPPPTHGPQ EYPPPPPAVR DSLPSGPREE AKPASPSSVQ
     DRSQASKPTP
//
ID   FRM4A_MOUSE             Reviewed;        1020 AA.
AC   Q8BIE6; B1AXK1; B1AXK2; Q6PDJ4; Q8CHA6;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=FERM domain-containing protein 4A;
GN   Name=Frmd4a; Synonyms=Frmd4, Kiaa1294;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 354-1020 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-785, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-679, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BIE6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BIE6-2; Sequence=VSP_035378, VSP_019592;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH58672.1; Type=Erroneous initiation;
CC       Sequence=CAM46015.1; Type=Erroneous gene model prediction;
CC       Sequence=CAM46271.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK082365; BAC38478.1; -; mRNA.
DR   EMBL; AL807832; CAM46014.1; -; Genomic_DNA.
DR   EMBL; AL928947; CAM46014.1; JOINED; Genomic_DNA.
DR   EMBL; AL807832; CAM46015.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL928947; CAM46015.1; JOINED; Genomic_DNA.
DR   EMBL; AL928947; CAM46270.1; -; Genomic_DNA.
DR   EMBL; AL807832; CAM46270.1; JOINED; Genomic_DNA.
DR   EMBL; AL928947; CAM46271.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL807832; CAM46271.1; JOINED; Genomic_DNA.
DR   EMBL; BC058672; AAH58672.1; ALT_INIT; mRNA.
DR   EMBL; AB093292; BAC41475.1; -; mRNA.
DR   IPI; IPI00222107; -.
DR   IPI; IPI00465706; -.
DR   RefSeq; NP_001171314.1; NM_001177843.1.
DR   RefSeq; NP_766063.3; NM_172475.3.
DR   UniGene; Mm.37932; -.
DR   UniGene; Mm.408418; -.
DR   UniGene; Mm.480116; -.
DR   ProteinModelPortal; Q8BIE6; -.
DR   SMR; Q8BIE6; 4-311.
DR   PhosphoSite; Q8BIE6; -.
DR   PRIDE; Q8BIE6; -.
DR   Ensembl; ENSMUST00000075767; ENSMUSP00000075172; ENSMUSG00000026657.
DR   Ensembl; ENSMUST00000115042; ENSMUSP00000110694; ENSMUSG00000026657.
DR   GeneID; 209630; -.
DR   KEGG; mmu:209630; -.
DR   UCSC; uc008ieo.1; mouse.
DR   UCSC; uc008ies.1; mouse.
DR   CTD; 209630; -.
DR   MGI; MGI:1919850; Frmd4a.
DR   eggNOG; roNOG12707; -.
DR   GeneTree; ENSGT00560000077123; -.
DR   HOVERGEN; HBG062800; -.
DR   OrthoDB; EOG4XPQF8; -.
DR   NextBio; 372751; -.
DR   ArrayExpress; Q8BIE6; -.
DR   Bgee; Q8BIE6; -.
DR   CleanEx; MM_FRMD4A; -.
DR   Genevestigator; Q8BIE6; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR021774; DUF3338.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH_type.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF11819; DUF3338; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   PRINTS; PR00935; BAND41.
DR   SMART; SM00295; B41; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Phosphoprotein.
FT   CHAIN         1   1020       FERM domain-containing protein 4A.
FT                                /FTId=PRO_0000219445.
FT   DOMAIN        5    307       FERM.
FT   COILED      367    401       Potential.
FT   COMPBIAS    613    741       Ser-rich.
FT   COMPBIAS    916    988       Ser-rich.
FT   MOD_RES     614    614       Phosphoserine (By similarity).
FT   MOD_RES     679    679       Phosphoserine.
FT   MOD_RES     785    785       Phosphoserine.
FT   VAR_SEQ       1      1       M -> MEGLLSPMRTKM (in isoform 2).
FT                                /FTId=VSP_035378.
FT   VAR_SEQ     999   1020       EATENSPIMDGSESPTHQSTDE -> SYSDSCFLDSSLYPE
FT                                LADVQWYGQEKAKPGTLV (in isoform 2).
FT                                /FTId=VSP_019592.
FT   CONFLICT    758    758       E -> G (in Ref. 1; BAC38478).
SQ   SEQUENCE   1020 AA;  113879 MW;  68E4E578FB91BF45 CRC64;
     MTEGRRCQVH LLDDRKLELL VQPKLLAKEL LDLVASHFNL KEKEYFGIAF TDETGHLNWL
     QLDRRVLEHD FPKKSGPVVL YFCVRFYIES ISYLKDNATI ELFFLNAKSC IYKELIDVDS
     EVVFELASYI LQEAKGDFSS NEVVRSDLKK LPALPTQALK EHPSLAYCED RVIEYYKKLN
     GQTRGQAIVN YMSIVESLPT YGVHYYAVKD KQGIPWWLGL SYKGIFQYDY HDKVKPRKIF
     QWRQLENLYF REKKFSVEVH DPRRASVTRR TFGHSGIAVH TWYACPALIK SIWAMAISQH
     QFYLDRKQSK SKIHAARSLS EIAIDLTETG TLKTSKLANM GSKGKIISGS SGSLLSSGSQ
     ESDSSQSAKK DMLAALKSRQ EALEETLRQR LEELKRLCLR EAELTGKLPV EYPLDPGEEP
     PIVRRRIGTA FKLDEQKILP KGEEAELERL EREFAIQSQI TEAARRLASD PNVSKKLKKQ
     RKTSYLNALK KLQEIENAIN ENRIKSGKKP TQRASLVIDD GNIASEDSSL SDALVLEDED
     SQVTSTISPL QSPHKGLPPR PPSSHNRPPP PQSLEGLRQL HYHRTDYDKS PLKPKMWSES
     SLDEPYEKVK KRSSHGHSSS HKRFPSTGSC TEAGVSSSLQ NSPIRSLPHW NSQSSMPSTP
     DLRVRSPHYV HSTRSVDISP TRLHSLALHF RHRSSSLESQ GKLLGSENDT GSPDFYTPRT
     RSSNGSDPMD DCSSCTSHSS SEHYYPAQMN ANYSTLAEDS PSKARQRQRQ RQRAAGALGS
     ASSGSMPNLA ARSGAASTGG GVYLHSQSQP SSQYRIKEYP LYIEGSATPV VVRSLESDQE
     GHYSVKAQFK TSNSYTAGGL FKESWRGGGD EGDAGRLTPS RSQILRTPSL GRDGAHDKGS
     GRAAVSDELR QWYQRSTASH KEHSRLSHTS STSSDSGSQY STSSQSTFVA HSRVTRMPQM
     CKATSAALPQ SQRSSTPSSE IGATPPSSPH HILTWQTGEA TENSPIMDGS ESPTHQSTDE
//
ID   DOCK9_MOUSE             Reviewed;        2055 AA.
AC   Q8BIK4; Q921Y6;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   03-JUL-2003, sequence version 2.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Dedicator of cytokinesis protein 9;
DE   AltName: Full=Cdc42 guanine nucleotide exchange factor zizimin-1;
GN   Name=Dock9; Synonyms=D14Wsu89e, Kiaa1058;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 212-2055 (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-936, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Guanine nucleotide-exchange factor (GEF) that activates
CC       CDC42 by exchanging bound GDP for free GTP. Overexpression induces
CC       filopodia formation (By similarity).
CC   -!- SUBUNIT: Interacts preferentially with nucleotide-depleted CDC42
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endomembrane system (By similarity).
CC       Note=Associated with membranes (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BIK4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BIK4-2; Sequence=VSP_007712, VSP_007713, VSP_007714,
CC                                  VSP_007715;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8BIK4-3; Sequence=VSP_007711;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The DHR-2 domain is necessary and sufficient for the GEF
CC       activity (By similarity).
CC   -!- MISCELLANEOUS: 'Zizim' means 'spike' in Hebrew.
CC   -!- SIMILARITY: Belongs to the DOCK family.
CC   -!- SIMILARITY: Contains 1 DHR-1 (CZH-1) domain.
CC   -!- SIMILARITY: Contains 1 DHR-2 (CZH-2) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH09134.1; Type=Erroneous initiation;
CC       Sequence=BAC65713.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK122431; BAC65713.1; ALT_INIT; mRNA.
DR   EMBL; AK045750; BAC32480.1; -; mRNA.
DR   EMBL; BC009134; AAH09134.1; ALT_INIT; mRNA.
DR   EMBL; BC046250; AAH46250.1; -; mRNA.
DR   IPI; IPI00337050; -.
DR   IPI; IPI00462129; -.
DR   IPI; IPI00896597; -.
DR   UniGene; Mm.441054; -.
DR   ProteinModelPortal; Q8BIK4; -.
DR   SMR; Q8BIK4; 182-318, 1618-2054.
DR   STRING; Q8BIK4; -.
DR   PhosphoSite; Q8BIK4; -.
DR   PRIDE; Q8BIK4; -.
DR   Ensembl; ENSMUST00000100298; ENSMUSP00000097871; ENSMUSG00000025558.
DR   Ensembl; ENSMUST00000100299; ENSMUSP00000097872; ENSMUSG00000025558.
DR   UCSC; uc007vam.1; mouse.
DR   MGI; MGI:106321; Dock9.
DR   GeneTree; ENSGT00600000084424; -.
DR   HOVERGEN; HBG107819; -.
DR   OrthoDB; EOG4255RV; -.
DR   ArrayExpress; Q8BIK4; -.
DR   Bgee; Q8BIK4; -.
DR   CleanEx; MM_DOCK9; -.
DR   Genevestigator; Q8BIK4; -.
DR   GermOnline; ENSMUSG00000025558; Mus musculus.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0017048; F:Rho GTPase binding; IPI:MGI.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IDA:MGI.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR010703; DOCK.
DR   InterPro; IPR021816; DUF3398.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF06920; Ded_cyto; 1.
DR   Pfam; PF11878; DUF3398; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Guanine-nucleotide releasing factor; Membrane;
KW   Phosphoprotein.
FT   CHAIN         1   2055       Dedicator of cytokinesis protein 9.
FT                                /FTId=PRO_0000190000.
FT   DOMAIN      185    292       PH.
FT   DOMAIN      650    888       DHR-1.
FT   DOMAIN     1514   2046       DHR-2.
FT   MOD_RES     936    936       Phosphoserine.
FT   MOD_RES    1195   1195       Phosphoserine (By similarity).
FT   VAR_SEQ       1   1366       Missing (in isoform 3).
FT                                /FTId=VSP_007711.
FT   VAR_SEQ    1364   1364       R -> RNQEGLGPIGHDRKSQTLPVSRNR (in isoform
FT                                2).
FT                                /FTId=VSP_007712.
FT   VAR_SEQ    1661   1661       K -> KEADLALQREPPAFPYSHSTCQRKSWG (in
FT                                isoform 2).
FT                                /FTId=VSP_007713.
FT   VAR_SEQ    1777   1790       Missing (in isoform 2).
FT                                /FTId=VSP_007714.
FT   VAR_SEQ    2054   2055       MG -> ICPLEEKTSVLPNSLHIFNAISGTPTSTVVQGLTS
FT                                SSSVV (in isoform 2).
FT                                /FTId=VSP_007715.
FT   CONFLICT    441    441       A -> T (in Ref. 3; AAH46250).
FT   CONFLICT   1288   1288       Missing (in Ref. 3; AAH46250).
FT   CONFLICT   1602   1602       P -> R (in Ref. 1; BAC65713).
SQ   SEQUENCE   2055 AA;  235312 MW;  D2AC9C53F6177A66 CRC64;
     MGCTTSVILF KGIRTVFERN CAYMCKQPGE SNALEYTAYN WSKEDSELSI AFCLAKPKLI
     EPLDYENVIV QKKTQILNDC LREMLLFPYD DFQTAILRRQ GRYLRSTVPA NAEEEAQSLF
     VTECIKTYNS DWHLVTYKYE DYSGEFRQLP NKVPKLDKLP VHVYEVDEEA DKDEDAASLG
     SQKGGITKHG WLYKGNMNSA ISVTMRSFKR RFFHLIQLGD GSYNLNFYKD EKISKEPKGS
     IFLDSCMGVI QNNRVRRFAF ELKMQDKSSY LLAADSEAEM EEWVTVLNKI LQLNFEAAMQ
     EKRNGDPHED DEQSKLEGSG SGLDSYLPEL AKSTREAEIK LKSESRVKLF YLDPDTQKLD
     FSSAEPEVKP FEEKFGKRIL VKCNDLSFNL QCCVAENEEG PTTNVEPFFV TLSLFDIKYN
     RKISADFHVD LNHFSVRQML APTSPALMNG GQSPPAFQDA LHTAMQYPKQ GIFSVTCPHP
     DIFLVARIEK VLQGSITHCA EPYMRSSDSS KVAQKVLKNA KQACQRLGQY RMPFAWAART
     LFKDTSGNLD KNARFSAIYR QDSNKLSNDD MLKLLADFRK PEKMAKLPVI LGNLDITIDS
     VSCDFPNYLN SSYIPMRQFE TCSKSPITFE VEEFVPCIPK HTQPYTVYSN HLYVYPKYLK
     YDSQKSFAKA RNIAICIEFK DSDEEDSQPL KCIYGRPGGP VFTRSALAAV LHHQQNPEFY
     DEIKIELPAQ LHERHHLLFT FFHVSCDNST KGSTKKKDAV ETQVGFSWLP LLKDGRVLTS
     EQHIPVSANL PSGYLGYQEL GMGRHYGPEV KWVEGGKPLL KISTHLVSTV YTQDQHLHNF
     FQYCQKTESG AQASGSELVK YLKSLHAMEG HVMIAFLPTI LNQLFRVLTR ATQEEVAVNV
     TRVIIHVVAQ CHEEGLESHL RSYVKFAYKA EPYVASEYKT VHEELTKSMT TILKPSADFL
     TSNKLLKYSW FFFDVLIKSM AQHLIENNKV KLLRNQRFPA SYHHAVETVV NMLMPHITQK
     FRDNPEASKN ANHSLAVFIK RCFTFMDRGF VFKQINNYIS CFAPGDPKTL FEYKFEFLRV
     VCNHEHYIPL NLPMPFGKGR IQRYQDLQLD YSLTDEFCRN HFLVGLLLRE VGTALQEFRE
     VRVIAISMLK NLLIKHSFDD RYNSRSHQAR IATLYLPLFG LLIENVQRIN VRDVSPFPVN
     PGSIVKDEAL AVPAGNPLMT PQKGNTLDHS LHKDLLGAIS GIASPYTAST PNINSVRNAD
     SRGSLISTDS GNSLPDRNPE KSNSLDKQQQ SGMLGNSVVR CDKLDQSEIK SLLMCFLYVL
     KSMSDDALFT YWNKASTAEL MDFFTISEVC LHQFQYMGKR YIARTGMMHA RLQQLGSLDN
     SVTFNHSYGH SEADVVHQSL LEANIATEVC LTALDTLSLF TLAFKNQLLA DHGHNPLMKK
     VFDVYLCFLQ KHQSEMALKN VFTALRSLIY KFPSAFYEGR ADMCASLCYE VLKCCNSKLS
     SIRTEASQLL YFLMRNNFDY TGKKSFVRTH LQVIISVSQL IADVVGIGGT RFQQSLSIIN
     NCANSDRIIK HTSFSSDVKD LTKRIRTVLM ATAQMKEHEN DPEMLVDLQY SLAKSYASTP
     ELRKTWLDSM ARIHVKNGDL SEAAMCYVHV TALVAEYLTR KGMFRQGCTA FRVITPNIDE
     EASMMEDVGM QDVHFNEDVL MELLEQCADG LWKAERYELI ADIYKLIIPI YEKRRDFERL
     AHLYDTLHRA YSKVTEVMHS GRRLLGTYFR VAFFGQAAQY QFTDSETDVE GFFEDEDGKE
     YIYKEPKLTP LSEISQRLLK LYSDKFGSEN VKMIQDSGKV NPKDLDSKFA YIQVTHVTPF
     FDEKELQERR TEFERCHNIR RFMFEMPFTQ TGKRQGGVEE QCKRRTILTA IHCFPYVKKR
     IPVMYQHHTD LNPIEVAIDE MSKKVAELRQ LCSSAEVDMI KLQLKLQGSV SVQVNAGPLA
     YARAFLDDTN TKRYPDNKVK LLKEVFRQFV EACGQALAVN ERLIKEDQLE YQEEMKANYR
     EMAKELSDIM REQMG
//
ID   Q8BIN3_MOUSE            Unreviewed;       203 AA.
AC   Q8BIN3;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   SubName: Full=Expressed sequence AI854703, isoform CRA_a;
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=AI854703; ORFNames=mCG_128038;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK039299; BAC30310.1; -; mRNA.
DR   EMBL; CH466597; EDK98554.1; -; Genomic_DNA.
DR   EMBL; CH466597; EDK98555.1; -; Genomic_DNA.
DR   EMBL; CH466597; EDK98556.1; -; Genomic_DNA.
DR   IPI; IPI00403202; -.
DR   UniGene; Mm.26678; -.
DR   HSSP; P07248; 2ADR.
DR   ProteinModelPortal; Q8BIN3; -.
DR   SMR; Q8BIN3; 37-188.
DR   PRIDE; Q8BIN3; -.
DR   eggNOG; KOG1721; -.
DR   HOVERGEN; HBG018163; -.
DR   OMA; THARMPT; -.
DR   ArrayExpress; Q8BIN3; -.
DR   Genevestigator; Q8BIN3; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 5.
DR   Pfam; PF00096; zf-C2H2; 4.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   203 AA;  22612 MW;  09460C36F1685022 CRC64;
     MTELVSSRGG SPTGDGEEGL GDDQGLVIHH PAEEQCHRCP LCGQTFSQQP SLVRHQKAHV
     GAGRAAAFVC PECGKAFSVK HNLEVHQRTH TGERPFACPE CGRCFSLKQN LLTHQRIHSG
     EKPHQCAQCG RCFREPRFLL NHQRTHARMP TPHPRRPGVF GERRPYFCPR CGKSFAREGS
     LKTHQRSHGH GPESQAAHLS RVL
//
ID   SYDM_MOUSE              Reviewed;         653 AA.
AC   Q8BIP0; Q5FWV4;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Aspartyl-tRNA synthetase, mitochondrial;
DE            EC=6.1.1.12;
DE   AltName: Full=Aspartate--tRNA ligase;
DE            Short=AspRS;
DE   Flags: Precursor;
GN   Name=Dars2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartate + tRNA(Asp) = AMP +
CC       diphosphate + L-aspartyl-tRNA(Asp).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; AK037337; BAC29789.1; -; mRNA.
DR   EMBL; AK138809; BAE23785.1; -; mRNA.
DR   EMBL; BC076606; AAH76606.1; -; mRNA.
DR   EMBL; BC089191; AAH89191.1; -; mRNA.
DR   IPI; IPI00273767; -.
DR   RefSeq; NP_766232.1; NM_172644.3.
DR   UniGene; Mm.28125; -.
DR   HSSP; P36419; 1L0W.
DR   ProteinModelPortal; Q8BIP0; -.
DR   SMR; Q8BIP0; 48-635.
DR   STRING; Q8BIP0; -.
DR   PhosphoSite; Q8BIP0; -.
DR   PRIDE; Q8BIP0; -.
DR   Ensembl; ENSMUST00000035430; ENSMUSP00000041851; ENSMUSG00000026709.
DR   GeneID; 226539; -.
DR   KEGG; mmu:226539; -.
DR   NMPDR; fig|10090.3.peg.1326; -.
DR   UCSC; uc007dey.1; mouse.
DR   CTD; 226539; -.
DR   MGI; MGI:2442510; Dars2.
DR   eggNOG; roNOG07016; -.
DR   GeneTree; ENSGT00550000074971; -.
DR   HOGENOM; HBG396032; -.
DR   HOVERGEN; HBG055815; -.
DR   InParanoid; Q8BIP0; -.
DR   OMA; AFPKTQQ; -.
DR   OrthoDB; EOG4M91R5; -.
DR   PhylomeDB; Q8BIP0; -.
DR   BRENDA; 6.1.1.12; 244.
DR   NextBio; 378214; -.
DR   ArrayExpress; Q8BIP0; -.
DR   Bgee; Q8BIP0; -.
DR   CleanEx; MM_DARS2; -.
DR   Genevestigator; Q8BIP0; -.
DR   GermOnline; ENSMUSG00000026709; Mus musculus.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:InterPro.
DR   InterPro; IPR004364; Aminoacyl-tRNA-synt_II.
DR   InterPro; IPR018150; Aminoacyl-tRNA-synt_II-like.
DR   InterPro; IPR006195; Aminoacyl-tRNA-synth_II.
DR   InterPro; IPR004524; Asp-tRNA-synth_IIb_bac/mt.
DR   InterPro; IPR018153; Asp-tRNA-synth_IIb_C_bac/mt.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR004115; GAD_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR016027; NA-bd_OB-fold-like.
DR   InterPro; IPR004365; NA-bd_OB_tRNA-helicase.
DR   Gene3D; G3DSA:3.30.1360.30; GAD_dom; 1.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   PANTHER; PTHR22594; aa-tRNA-synt_II; 1.
DR   PANTHER; PTHR22594:SF5; AspS_bac; 1.
DR   Pfam; PF02938; GAD; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR   TIGRFAMs; TIGR00459; aspS_bact; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Ligase;
KW   Mitochondrion; Nucleotide-binding; Protein biosynthesis;
KW   Transit peptide.
FT   TRANSIT       1     46       Mitochondrion (Potential).
FT   CHAIN        47    653       Aspartyl-tRNA synthetase, mitochondrial.
FT                                /FTId=PRO_0000250737.
FT   MOD_RES     234    234       N6-acetyllysine (By similarity).
FT   MOD_RES     626    626       N6-acetyllysine (By similarity).
FT   CONFLICT     71     71       I -> V (in Ref. 2; AAH89191).
FT   CONFLICT    104    104       R -> G (in Ref. 2; AAH89191).
FT   CONFLICT    540    540       V -> A (in Ref. 2; AAH89191).
SQ   SEQUENCE   653 AA;  74102 MW;  8A02D2E62E914E99 CRC64;
     MYLGFWLSRL CRGLSRPIGK TMRPIWGSLS RNLALSSQRI PEFSSFVART NTCGELRSSH
     LGQEVTLCGW IQYRRQNTFL VLRDCHGLVQ ILIPQDESAA SVRRILCEAP VESVVRVSGT
     VISRPPGQEN PKMPTGEIEI KVKTAELLNA CKKLPFEIKD FVKKTEALRL QYRYLDLRSF
     QMQYNLRLRS QMVMKMREYL CNLHGFVDIE TPTLFKRTPG GAKEFLVPSR EPGKFYSLPQ
     SPQQFKQLLM VGGLDRYFQV ARCYRDEGSR PDRQPEFTQI DIEMSFVEQT GIQRLVEGLL
     QYSWPGDKDP LVTPFPSMTF AEALATYGTD KPDTRFGMKI VDVSDVFRNT ELRFLQDALA
     KPQGTVKAIC VHDGAKYLRK EDIEFIRKFA VHHFSQEVLP IFLNAKKNWS SPFAKFIMEE
     ERLELARSME IQEEDIVLLT AGEHEKACSL LGKLRLECAD LLEMRGAVLR DPAVFSFLWV
     VDFPLFLAKE ESPTELESAH HPFTAPNSSD IHLLYTEPEK VRGQHYDLVL NGNEIGGGSV
     RIHDAQLQRY ILETLLKEDV KLLSHLLQAL DYGAPPHGGI ALGLDRLVCL VTGAPSIRDV
     IAFPKSYRGQ DLMSNAPDSV SPEELKPYHI HVLWPADSEE ESASATPSKH LSS
//
ID   ANS1B_MOUSE             Reviewed;        1259 AA.
AC   Q8BIZ1; Q4KMR9; Q8BJ47; Q8BJ49;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 2.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Ankyrin repeat and sterile alpha motif domain-containing protein 1B;
DE   AltName: Full=Amyloid-beta protein intracellular domain-associated protein 1;
DE            Short=AIDA-1;
DE   AltName: Full=E2A-PBX1-associated protein;
DE            Short=EB-1;
GN   Name=Anks1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Corpus striatum, Hippocampus, Medulla oblongata, and
RC   Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-900, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY (ISOFORM 4), AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=15169875; DOI=10.1074/mcp.M400045-MCP200;
RA   Jordan B.A., Fernholz B.D., Boussac M., Xu C., Grigorean G.,
RA   Ziff E.B., Neubert T.A.;
RT   "Identification and verification of novel rodent postsynaptic density
RT   proteins.";
RL   Mol. Cell. Proteomics 3:857-871(2004).
CC   -!- FUNCTION: Isoform 2 may participate in the regulation of
CC       nucleoplasmic coilin protein interactions in neuronal and
CC       transformed cells (By similarity).
CC   -!- SUBUNIT: Interacts with EPHA8. Isoform 2 interacts with COIL (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Nucleus (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 4: Cell junction, synapse,
CC       postsynaptic cell membrane, postsynaptic density. Cell projection,
CC       dendritic spine. Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q8BIZ1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BIZ1-2; Sequence=VSP_032715, VSP_032716, VSP_032717;
CC       Name=3;
CC         IsoId=Q8BIZ1-3; Sequence=VSP_032714, VSP_032719;
CC       Name=4;
CC         IsoId=Q8BIZ1-4; Sequence=VSP_032715, VSP_032716, VSP_032718;
CC       Name=5;
CC         IsoId=Q8BIZ1-5; Sequence=VSP_032713;
CC   -!- SIMILARITY: Contains 7 ANK repeats.
CC   -!- SIMILARITY: Contains 1 PID domain.
CC   -!- SIMILARITY: Contains 2 SAM (sterile alpha motif) domains.
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DR   EMBL; AK032061; BAC27677.1; -; mRNA.
DR   EMBL; AK032211; BAC27761.1; -; mRNA.
DR   EMBL; AK049899; BAC33978.1; -; mRNA.
DR   EMBL; AK163750; BAE37478.1; -; mRNA.
DR   EMBL; AC107661; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC122212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC132093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC132131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC132328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC132465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC138719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC151984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC134539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC098373; AAH98373.1; -; mRNA.
DR   IPI; IPI00457583; -.
DR   IPI; IPI00457597; -.
DR   IPI; IPI00664176; -.
DR   IPI; IPI00673967; -.
DR   IPI; IPI00890253; -.
DR   RefSeq; NP_001170867.1; NM_001177396.1.
DR   RefSeq; NP_001170868.1; NM_001177397.1.
DR   RefSeq; NP_001170869.1; NM_001177398.1.
DR   RefSeq; NP_852063.1; NM_181398.3.
DR   UniGene; Mm.440605; -.
DR   UniGene; Mm.474914; -.
DR   UniGene; Mm.477107; -.
DR   HSSP; Q02410; 1AQC.
DR   ProteinModelPortal; Q8BIZ1; -.
DR   SMR; Q8BIZ1; 4-281, 804-873, 886-943, 1052-1193.
DR   STRING; Q8BIZ1; -.
DR   PhosphoSite; Q8BIZ1; -.
DR   PRIDE; Q8BIZ1; -.
DR   Ensembl; ENSMUST00000078569; ENSMUSP00000077646; ENSMUSG00000058589.
DR   Ensembl; ENSMUST00000092221; ENSMUSP00000089867; ENSMUSG00000058589.
DR   Ensembl; ENSMUST00000099364; ENSMUSP00000096965; ENSMUSG00000058589.
DR   Ensembl; ENSMUST00000099366; ENSMUSP00000096967; ENSMUSG00000058589.
DR   GeneID; 77531; -.
DR   KEGG; mmu:77531; -.
DR   CTD; 77531; -.
DR   MGI; MGI:1924781; Anks1b.
DR   GeneTree; ENSGT00530000063104; -.
DR   HOGENOM; HBG446677; -.
DR   HOVERGEN; HBG050506; -.
DR   InParanoid; Q8BIZ1; -.
DR   OrthoDB; EOG4FN4HZ; -.
DR   NextBio; 347068; -.
DR   ArrayExpress; Q8BIZ1; -.
DR   Bgee; Q8BIZ1; -.
DR   Genevestigator; Q8BIZ1; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 3.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 2.
DR   Pfam; PF00023; Ank; 4.
DR   Pfam; PF00640; PID; 1.
DR   Pfam; PF00536; SAM_1; 2.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM00454; SAM; 2.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF47769; SAM_homology; 2.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
DR   PROSITE; PS01179; PID; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; ANK repeat; Cell junction; Cell membrane;
KW   Cell projection; Cytoplasm; Membrane; Nucleus; Phosphoprotein;
KW   Postsynaptic cell membrane; Repeat; Synapse.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1259       Ankyrin repeat and sterile alpha motif
FT                                domain-containing protein 1B.
FT                                /FTId=PRO_0000327260.
FT   REPEAT        2     31       ANK 1.
FT   REPEAT       58     87       ANK 2.
FT   REPEAT       91    120       ANK 3.
FT   REPEAT      127    156       ANK 4.
FT   REPEAT      160    189       ANK 5.
FT   REPEAT      193    222       ANK 6.
FT   REPEAT      225    254       ANK 7.
FT   DOMAIN      809    875       SAM 1.
FT   DOMAIN      883    948       SAM 2.
FT   DOMAIN     1055   1212       PID.
FT   MOD_RES     900    900       Phosphotyrosine.
FT   VAR_SEQ       1    993       Missing (in isoform 5).
FT                                /FTId=VSP_032713.
FT   VAR_SEQ       1    830       Missing (in isoform 3).
FT                                /FTId=VSP_032714.
FT   VAR_SEQ       1    773       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_032715.
FT   VAR_SEQ     774    806       SFTSEWEEIDKIMNSIDVGINSELEGMNGETTR -> MMWQ
FT                                CHPSAPDYRYYPVDGYSLLKRFPLHPLTG (in isoform
FT                                2 and isoform 4).
FT                                /FTId=VSP_032716.
FT   VAR_SEQ     962   1021       Missing (in isoform 2).
FT                                /FTId=VSP_032717.
FT   VAR_SEQ     962   1021       EPSGNHTPPQLSPSLSQSTYTTGGSLDVPHIIMQGDARRRR
FT                                NENYFDDIPRSKLERQMAQ -> QSSVCEIWTNQNAGFPFS
FT                                AIHQVHN (in isoform 4).
FT                                /FTId=VSP_032718.
FT   VAR_SEQ    1224   1259       QIDPSEQKTLANLPWIVEPGQEAKRGINTKYETTIF -> A
FT                                PQTSCPNRLV (in isoform 3).
FT                                /FTId=VSP_032719.
SQ   SEQUENCE   1259 AA;  139019 MW;  BCA415678094F8D2 CRC64;
     MGKDQELLEA ARTGNVALVE KLLSGRKGGI LGGGSGPLPL SNLLSIWRGP NVNCTDSSGY
     TALHHAALNG HKDIVLKLLQ YEASTNVADN KGYFPIHLAA WKGDVEIVKI LIHHGPSHSR
     VNEQNNENET ALHCAAQYGH SEVVAVLLEE LTDPTIRNSK LETPLDLAAL YGRLRVVKMI
     ISAHPNLMSC NTRKHTPLHL AARNGHKAVV QVLLEAGMDV SCQTEKGSAL HEAALFGKVD
     VVRVLLETGI DANIKDSLGR TVLDILKEHP SQKSLQIATL LQDYLEGAGR SAAVLEEHAQ
     EDTAQETHLS SPAESPQKTK SETVTGELSK LLDEIKLCQE KDYSFEDLCH TISDHYLDNL
     SKISEEELGK NGSQSVRTSS TINLSPGEVE DEEEDPNSCG PTGLWEALTP CNGCRNLGFP
     MLAQESYPKK RNFPMEMEPS ASLDTFPSEN ENFLCELVDT AVTKKPCSLE IARAPSPRTD
     NASEVAITAP GTSHHRNSST GPTPDCSPPS PDTALKNIVK VIRPQPKQRT SIVSSLDFQR
     MNHNQEYFEI STSTGCTSFT SSPAASPPTS SVETTEVKNE GAEHADDLSQ QEDDEPPKEY
     DAGQFAGLLH GSSPACESPE NPFHLYGKRN TCEDGPDEAS LANSPLPFKQ TPIENNPEPS
     VKKVKPKVVS RTIFHKRNHQ LENHTIVGTR MSRSGSRNGD QWGVNPGGFV ERACTLGRIR
     SLPKALIDMH LSKNVSKSDS DLIAYPSKDK ARVNWSKSST AERSSKDNSE RTPSFTSEWE
     EIDKIMNSID VGINSELEGM NGETTRPRCP VQTVGQWLES IGLPQYENHL MANGFDSVQF
     MGSNVMEDQD LLEIGILNSG HRQRILQAIQ LLPKMRPIGH DGYHPTSVAE WLDSIELGDY
     TKAFLINGYT SMDLLKKIWE LELINVLKIS LIGHRKRILA SLGDRLHDDP PQKPPRSITL
     REPSGNHTPP QLSPSLSQST YTTGGSLDVP HIIMQGDARR RRNENYFDDI PRSKLERQMA
     QTGDWGEPSI TLRPPNEATA STPVQYWQHH PEKLIFQSCD YKAFYLGSML IKELRGTEST
     QDACAKMRAN CQKSTEQMKK VPTIILSVSY KGVKFIDAAN KNIIAEHEIR NISCAAQDPE
     DLSTFAYITK DLKSNHHYCH VFTAFDVNLA YEIILTLGQA FEVAYQLALQ ARKGGHSSTL
     PESFENKPSK PIPKPRVSIR KSVQIDPSEQ KTLANLPWIV EPGQEAKRGI NTKYETTIF
//
ID   SNIP1_MOUSE             Reviewed;         383 AA.
AC   Q8BIZ6; Q3V106; Q8BIZ4;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Smad nuclear-interacting protein 1;
GN   Name=Snip1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryonic stem cell, Spleen, Testis, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-381, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Down-regulates NF-kappa-B signaling by competing with
CC       RELA for CREBBP/EP300 binding. Involved in the microRNA (miRNA)
CC       biogenesis (By similarity).
CC   -!- SUBUNIT: Binds SMAD4 and CREBBP/EP300. Binds the SMAD1/OAZ1/PSMB4
CC       complex. Interacts with DROSHA (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- PTM: Degraded by the proteasome upon binding to the
CC       SMAD1/OAZ1/PSMB4 complex (By similarity).
CC   -!- SIMILARITY: Contains 1 FHA domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK040571; BAE20582.1; -; mRNA.
DR   EMBL; AK049254; BAC33638.1; -; mRNA.
DR   EMBL; AK049318; BAC33680.1; -; mRNA.
DR   EMBL; AK132768; BAE21347.1; -; mRNA.
DR   EMBL; AK143801; BAE25543.1; -; mRNA.
DR   EMBL; BC064067; AAH64067.1; -; mRNA.
DR   IPI; IPI00308559; -.
DR   RefSeq; NP_780455.2; NM_175246.4.
DR   UniGene; Mm.479908; -.
DR   ProteinModelPortal; Q8BIZ6; -.
DR   SMR; Q8BIZ6; 219-360.
DR   STRING; Q8BIZ6; -.
DR   PhosphoSite; Q8BIZ6; -.
DR   PRIDE; Q8BIZ6; -.
DR   Ensembl; ENSMUST00000052183; ENSMUSP00000060721; ENSMUSG00000050213.
DR   GeneID; 76793; -.
DR   KEGG; mmu:76793; -.
DR   UCSC; uc008urq.1; mouse.
DR   CTD; 76793; -.
DR   MGI; MGI:2156003; Snip1.
DR   eggNOG; roNOG05314; -.
DR   GeneTree; ENSGT00510000047345; -.
DR   HOGENOM; HBG717219; -.
DR   HOVERGEN; HBG056615; -.
DR   InParanoid; Q8BIZ6; -.
DR   OMA; KQEREDH; -.
DR   OrthoDB; EOG451DRR; -.
DR   PhylomeDB; Q8BIZ6; -.
DR   NextBio; 345823; -.
DR   ArrayExpress; Q8BIZ6; -.
DR   Bgee; Q8BIZ6; -.
DR   CleanEx; MM_SNIP1; -.
DR   Genevestigator; Q8BIZ6; -.
DR   GermOnline; ENSMUSG00000050213; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007249; P:I-kappaB kinase/NF-kappaB cascade; IDA:MGI.
DR   GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IDA:MGI.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR008984; SMAD_FHA_domain.
DR   Gene3D; G3DSA:2.60.200.20; FHA; 1.
DR   Pfam; PF00498; FHA; 1.
DR   SMART; SM00240; FHA; 1.
DR   SUPFAM; SSF49879; SMAD_FHA; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Isopeptide bond; Nucleus; Phosphoprotein;
KW   RNA-mediated gene silencing; Ubl conjugation.
FT   CHAIN         1    383       Smad nuclear-interacting protein 1.
FT                                /FTId=PRO_0000072010.
FT   DOMAIN      268    331       FHA.
FT   COILED      153    194       Potential.
FT   COMPBIAS     62    180       Arg-rich.
FT   COMPBIAS    374    377       Poly-Glu.
FT   MOD_RES      18     18       Phosphoserine.
FT   MOD_RES      33     33       Phosphoserine.
FT   MOD_RES      48     48       Phosphoserine (By similarity).
FT   MOD_RES      50     50       Phosphoserine (By similarity).
FT   MOD_RES      81     81       Phosphoserine (By similarity).
FT   MOD_RES      83     83       Phosphoserine (By similarity).
FT   MOD_RES     145    145       Phosphoserine (By similarity).
FT   MOD_RES     381    381       Phosphoserine.
FT   CROSSLNK     28     28       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CONFLICT    223    223       T -> P (in Ref. 1; BAC33680).
SQ   SEQUENCE   383 AA;  44415 MW;  0ADD646D4CB952BE CRC64;
     MKAGKSERER SGRRRHRSGD ALTTVVVKQE RLSPEPVAHR RPDAPAASLS PPAAEPGHSG
     HRGSRARSPA KKKSKSSGRR SKSPRTKRSQ SPHYPMVKVK QEREDHPRRG REDRQHREPS
     EQEHRRARNS ERDRHRGHSR QGRSSDERPV SGQDRDRDSQ NLQAQEEERD FHNARRREHR
     QQNESAGSEA QEVIPRPAGN RSKEVPVKEK PSFELSGALL EDTNTFRGVV IKYSEPPEAR
     IPKKRWRLYP FKNDEVLPVM YIHRQSAYLL GRHRRIADIP IDHPSCSKQH AVFQYRLVEY
     TRADGTVGRR VKPYIIDLGS GNGTFLNNKR IEPQRYYELK EKDVLKFGFS SREYVLLHES
     SDTSELDRKE DEDDEEEEMV SDS
//
ID   ZC3HE_MOUSE             Reviewed;         735 AA.
AC   Q8BJ05; A0PJE7; A1A4A9; Q3TU70; Q8BIY8; Q8R3Q8; Q8R3R2; Q9DAA8;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Zinc finger CCCH domain-containing protein 14;
GN   Name=Zc3h14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Head, Liver, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 128-735 (ISOFORM 3).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=19303045; DOI=10.1016/j.gene.2009.02.022;
RA   Leung S.W., Apponi L.H., Cornejo O.E., Kitchen C.M., Valentini S.R.,
RA   Pavlath G.K., Dunham C.M., Corbett A.H.;
RT   "Splice variants of the human ZC3H14 gene generate multiple isoforms
RT   of a zinc finger polyadenosine RNA binding protein.";
RL   Gene 439:71-78(2009).
CC   -!- FUNCTION: Binds the polyadenosine RNA oligonucleotides (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8BJ05-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BJ05-2; Sequence=VSP_033179;
CC       Name=3;
CC         IsoId=Q8BJ05-3; Sequence=VSP_033180;
CC       Name=4;
CC         IsoId=Q8BJ05-4; Sequence=VSP_033177, VSP_033178, VSP_033180;
CC   -!- TISSUE SPECIFICITY: Expressed in kidney, liver, muscle, heart
CC       brain and testes.
CC   -!- SIMILARITY: Belongs to the ZC3H14 family.
CC   -!- SIMILARITY: Contains 5 C3H1-type zinc fingers.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK006009; BAB24364.1; -; mRNA.
DR   EMBL; AK048046; BAC33222.1; -; mRNA.
DR   EMBL; AK050226; BAC34134.1; -; mRNA.
DR   EMBL; AK160937; BAE36101.1; -; mRNA.
DR   EMBL; BC021797; AAH21797.1; -; mRNA.
DR   EMBL; BC024824; AAH24824.1; -; mRNA.
DR   EMBL; BC024856; AAH24856.1; -; mRNA.
DR   EMBL; BC026610; AAH26610.1; -; mRNA.
DR   IPI; IPI00118364; -.
DR   IPI; IPI00380641; -.
DR   IPI; IPI00408978; -.
DR   IPI; IPI00461416; -.
DR   RefSeq; NP_001008506.2; NM_001008506.2.
DR   RefSeq; NP_001153579.1; NM_001160107.1.
DR   RefSeq; NP_001153580.1; NM_001160108.1.
DR   RefSeq; NP_083610.2; NM_029334.2.
DR   UniGene; Mm.25549; -.
DR   ProteinModelPortal; Q8BJ05; -.
DR   SMR; Q8BJ05; 9-74, 594-639.
DR   STRING; Q8BJ05; -.
DR   PhosphoSite; Q8BJ05; -.
DR   PRIDE; Q8BJ05; -.
DR   Ensembl; ENSMUST00000021399; ENSMUSP00000021399; ENSMUSG00000021012.
DR   Ensembl; ENSMUST00000047981; ENSMUSP00000038586; ENSMUSG00000021012.
DR   Ensembl; ENSMUST00000057000; ENSMUSP00000055879; ENSMUSG00000021012.
DR   Ensembl; ENSMUST00000066979; ENSMUSP00000065569; ENSMUSG00000021012.
DR   GeneID; 75553; -.
DR   KEGG; mmu:75553; -.
DR   UCSC; uc007org.1; mouse.
DR   CTD; 75553; -.
DR   MGI; MGI:1919824; Zc3h14.
DR   eggNOG; roNOG14474; -.
DR   GeneTree; ENSGT00440000038430; -.
DR   HOVERGEN; HBG108760; -.
DR   OrthoDB; EOG4K3KW4; -.
DR   NextBio; 343342; -.
DR   ArrayExpress; Q8BJ05; -.
DR   Bgee; Q8BJ05; -.
DR   Genevestigator; Q8BJ05; -.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR000571; Znf_CCCH.
DR   SMART; SM00356; ZnF_C3H1; 3.
DR   PROSITE; PS50103; ZF_C3H1; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Metal-binding; Nucleus;
KW   Phosphoprotein; Repeat; RNA-binding; Zinc; Zinc-finger.
FT   CHAIN         1    735       Zinc finger CCCH domain-containing
FT                                protein 14.
FT                                /FTId=PRO_0000331313.
FT   ZN_FING     595    620       C3H1-type 1.
FT   ZN_FING     621    640       C3H1-type 2.
FT   ZN_FING     641    656       C3H1-type 3.
FT   ZN_FING     681    698       C3H1-type 4.
FT   ZN_FING     700    718       C3H1-type 5.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     357    357       N6-acetyllysine (By similarity).
FT   MOD_RES     409    409       Phosphoserine (By similarity).
FT   MOD_RES     450    450       Phosphoserine (By similarity).
FT   MOD_RES     515    515       Phosphoserine.
FT   MOD_RES     620    620       Phosphoserine (By similarity).
FT   VAR_SEQ       1    295       Missing (in isoform 4).
FT                                /FTId=VSP_033177.
FT   VAR_SEQ     296    426       LPVVSSVVKVKRFSHDGEEEEEDEDYGTRIGSLSSSVSVPA
FT                                KPERRPSLPPSKQANKNLILKAISEAQESVTKTTNYSAVPQ
FT                                KQTLPVAPRTRTSQEELLAEMVQGQNRAPRISPPVKEEEAK
FT                                GDNTGKSQ -> MKMSSRFSSPSLPVFLSPEPADLGSLTSA
FT                                SCSLNELGNISYLLRKIATDINEMKGMKAAILTVEANLFDL
FT                                NVRVSQNEAKISSLEVKMNEYLTSTSECNRQLEDFQERLEF
FT                                ESQSETTDANLIGFLTEVEK (in isoform 4).
FT                                /FTId=VSP_033178.
FT   VAR_SEQ     427    582       Missing (in isoform 2).
FT                                /FTId=VSP_033179.
FT   VAR_SEQ     452    582       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_033180.
FT   CONFLICT     27     27       D -> H (in Ref. 1; BAC34134).
FT   CONFLICT    665    665       T -> A (in Ref. 1; BAE36101).
SQ   SEQUENCE   735 AA;  82409 MW;  550696563E7E87C3 CRC64;
     MEIGTEISRK IRSAIKGKLQ ELGAYVDEEL PDYIMVMVAN KKSQDQMTED LSLFLGNNTI
     RFTVWLHGVL DKLRSVTTEP SSLKSPDASI FDSHVPSNKS SFSRGDERRH EAAVPPLAVS
     SSRPEKRDSR VSTSSQEQKS TNVRHSYDDG ASTRLMSTVK PLREPAPSED VIDIKPEPDD
     LIDEDLNFVQ ENPLSQKKPT VTLTYGSSRP SIEIYRPPAS RNADTGTHLN RLQLHPQQSS
     AHAAKQLDVQ SSQVSEAGRL CEPPVLSSVE DTYSPFFRNN LDKMSIEDEN FRKRKLPVVS
     SVVKVKRFSH DGEEEEEDED YGTRIGSLSS SVSVPAKPER RPSLPPSKQA NKNLILKAIS
     EAQESVTKTT NYSAVPQKQT LPVAPRTRTS QEELLAEMVQ GQNRAPRISP PVKEEEAKGD
     NTGKSQGTQQ RQLLSRLQID PVMVETMEMS QDYYDMESMV HADTRSFILK KPKLSEEIVV
     TPNQDSGMKT ADALRVLSGH LMQTRDLVQP DKPASPKFIV TLDGVPSPPG YMSDQEEEMC
     FEGMKPVNQT SASNKGLRGL LHPQQLHLLS RQLEDPDGSF SNAEMTDLSV AQKPEKLLER
     CKYWPACKNG DECVYHHPIS PCKAFPNCKF AEKCLFVHPN CKYDTKCTKA DCPFTHMSRR
     ASILTPKPVS SPAPSSNGQL CRYFPACKKM ECPFYHPKHC RFNTQCTRPD CTFYHPTITV
     PPRHALKWIR PQSSE
//
ID   DLGP2_MOUSE             Reviewed;        1059 AA.
AC   Q8BJ42; Q6XBF3;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   08-FEB-2011, entry version 62.
DE   RecName: Full=Disks large-associated protein 2;
DE            Short=DAP-2;
DE   AltName: Full=PSD-95/SAP90-binding protein 2;
DE   AltName: Full=SAP90/PSD-95-associated protein 2;
DE            Short=SAPAP2;
GN   Name=Dlgap2; Synonyms=Dap2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 80-1059 (ISOFORM 2), AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=ICR;
RX   PubMed=15024750; DOI=10.1002/cne.20060;
RA   Welch J.M., Wang D., Feng G.;
RT   "Differential mRNA expression and protein localization of the
RT   SAP90/PSD-95-associated proteins (SAPAPs) in the nervous system of the
RT   mouse.";
RL   J. Comp. Neurol. 472:24-39(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440; SER-450 AND
RP   SER-453, AND MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228; SER-440; SER-574;
RP   SER-1012; SER-1040 AND SER-1047, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-312, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-745 AND SER-1047, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: May play a role in the molecular organization of
CC       synapses and neuronal cell signaling. Could be an adapter protein
CC       linking ion channel to the subsynaptic cytoskeleton. May induce
CC       enrichment of PSD-95/SAP90 at the plasma membrane.
CC   -!- SUBUNIT: Interacts with DLG4/PSD-95 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       (By similarity). Cell junction, synapse, postsynaptic cell
CC       membrane, postsynaptic density (By similarity). Cell junction,
CC       synapse (By similarity). Note=Postsynaptic density of neuronal
CC       cells (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BJ42-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BJ42-2; Sequence=VSP_014817;
CC   -!- TISSUE SPECIFICITY: Expressed in various brain areas.
CC   -!- SIMILARITY: Belongs to the SAPAP family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK032564; BAC27927.1; -; mRNA.
DR   EMBL; AY243847; AAO89218.3; -; mRNA.
DR   IPI; IPI00222263; -.
DR   IPI; IPI00467058; -.
DR   RefSeq; NP_001139437.1; NM_001145965.1.
DR   RefSeq; NP_766498.2; NM_172910.3.
DR   UniGene; Mm.404697; -.
DR   UniGene; Mm.478217; -.
DR   STRING; Q8BJ42; -.
DR   PhosphoSite; Q8BJ42; -.
DR   PRIDE; Q8BJ42; -.
DR   Ensembl; ENSMUST00000110810; ENSMUSP00000106433; ENSMUSG00000047495.
DR   GeneID; 244310; -.
DR   KEGG; mmu:244310; -.
DR   UCSC; uc009kyy.1; mouse.
DR   UCSC; uc009kza.1; mouse.
DR   CTD; 244310; -.
DR   MGI; MGI:2443181; Dlgap2.
DR   GeneTree; ENSGT00550000074473; -.
DR   HOVERGEN; HBG018957; -.
DR   InParanoid; Q8BJ42; -.
DR   NextBio; 386221; -.
DR   ArrayExpress; Q8BJ42; -.
DR   Bgee; Q8BJ42; -.
DR   Genevestigator; Q8BJ42; -.
DR   GermOnline; ENSMUSG00000047495; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007267; P:cell-cell signaling; IEA:InterPro.
DR   InterPro; IPR005026; GKAP.
DR   Pfam; PF03359; GKAP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Membrane;
KW   Phosphoprotein; Postsynaptic cell membrane; Synapse.
FT   CHAIN         1   1059       Disks large-associated protein 2.
FT                                /FTId=PRO_0000174292.
FT   MOD_RES     228    228       Phosphoserine.
FT   MOD_RES     312    312       Phosphotyrosine.
FT   MOD_RES     440    440       Phosphoserine.
FT   MOD_RES     450    450       Phosphoserine.
FT   MOD_RES     453    453       Phosphoserine.
FT   MOD_RES     574    574       Phosphoserine.
FT   MOD_RES     745    745       Phosphoserine.
FT   MOD_RES    1012   1012       Phosphoserine.
FT   MOD_RES    1040   1040       Phosphoserine.
FT   MOD_RES    1047   1047       Phosphoserine.
FT   VAR_SEQ     725    738       Missing (in isoform 2).
FT                                /FTId=VSP_014817.
FT   CONFLICT    472    472       K -> R (in Ref. 1; BAC27927).
FT   CONFLICT    647    647       D -> G (in Ref. 1; BAC27927).
SQ   SEQUENCE   1059 AA;  119074 MW;  692A878032026054 CRC64;
     MGTAQVLPGI LQKHCCILPD RNTESQCTLC GEPEEEEGGD LAQPGLSFPG PAEEDIDQQY
     SWSPTQHFNE ERYSPAPRNM KGLTGSRNQP QLCAGHTCGL SPPDDCEHPH DHMHHGSDVR
     QPYLLSPAES CPMDHHRCSP RSSVHSECMM MPVMLGDHVS SSTFPRMHYS SHYDTRDDCA
     MSHTSTKVNR IPANLLDQFE KQLPLHRDGF HTLQYQRASA ATEQRNESPG RIRHLVHSVQ
     KLFTKSHSLE GSSKSNINGT KSDSRVDDHH QSHLSKHSKR SKSKERKPES KHKSGMSSWW
     SSDDNLDSDS TYRTPSVAHR HHMDHIPHCY PEALQSPFGD LSLKTSKSNN DVKCSACEGL
     ALTPDTRYMK RSSWSTLTVS QAKEAYRKSS LNLDKPLVHP EIKPSLRPCH YLQVPQDDWG
     AYPTGGKEEE IPCRRMRSGS YIKAMGDEES GESDSSPKTS PTVAIRPEPL LKPIIQRPLG
     DHQTQSYLQA ATEVPVGHSL NPSINYNSPK FRSRNQSYMR AVSTLSQASC VSQMSEAEVN
     GQFESVCESV FSEVESQAMD ALDLPGCFRT RSHSYLRAIQ AGYSQDDECI PVMTSSNMTS
     TIRSTAAVSY TNYKKTPPPV PPRTTSKPLI SVTAQSSTES TQDAYQDSRA QRMSPWPQDS
     RGGLYNSMDS LDSNKAMNLA LETAAAQRHA ADTQSSSTRS IDKAVLASKA EELLKSRCSS
     IGVQDSEFPD HQPYPRSDVE TATDSDTESR GLREYHSVGV QVEDEKRHGR FKRSNSVTAA
     VQADLELEGF PGHVSMEDKG LQFGSSFQRH SEPSTPTQYG ALRTVRTQGL FSYREDYRTQ
     VDTSTLPPPD PWLEPSLDTV ETGRMSPCRR DGSWFLKLLH TETKRMEGWC KEMEREAEEN
     DLLEDILGKI RSAVGSAQLL MSQKFQQFYW LCQQNMDPSA MPRPTSQDLA GYWDMLQLSV
     EDVSMKFDEL HQLKLNDWKI IESPERKEER KIPPPIPKKP PKGKFPITRE KSLDLPDRQR
     QEARRRLMAA KRAASFRQNS ATERADSIEI YIPEAQTRL
//
ID   HMBX1_MOUSE             Reviewed;         419 AA.
AC   Q8BJA3; Q80WC2; Q8BWE7; Q99LV1;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Homeobox-containing protein 1;
GN   Name=Hmbox1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC   STRAIN=FVB/N; TISSUE=Colon, Mammary gland, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Transcription factor. Acts as a transcriptional
CC       repressor (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity). Note=Predominantly detected in cytoplasm (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8BJA3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BJA3-2; Sequence=VSP_018114, VSP_018115;
CC       Name=3;
CC         IsoId=Q8BJA3-3; Sequence=VSP_018116;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q8BJA3-4; Sequence=VSP_018115;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH02212.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK052729; BAC35118.1; -; mRNA.
DR   EMBL; AK089782; BAC40961.1; -; mRNA.
DR   EMBL; BC002212; AAH02212.1; ALT_INIT; mRNA.
DR   EMBL; BC051457; AAH51457.1; -; mRNA.
DR   IPI; IPI00222355; -.
DR   IPI; IPI00330579; -.
DR   IPI; IPI00405482; -.
DR   IPI; IPI00753826; -.
DR   RefSeq; NP_796312.2; NM_177338.5.
DR   UniGene; Mm.344074; -.
DR   ProteinModelPortal; Q8BJA3; -.
DR   SMR; Q8BJA3; 143-351.
DR   PRIDE; Q8BJA3; -.
DR   Ensembl; ENSMUST00000022544; ENSMUSP00000022544; ENSMUSG00000021972.
DR   Ensembl; ENSMUST00000056878; ENSMUSP00000055515; ENSMUSG00000021972.
DR   Ensembl; ENSMUST00000067843; ENSMUSP00000066905; ENSMUSG00000021972.
DR   GeneID; 219150; -.
DR   KEGG; mmu:219150; -.
DR   UCSC; uc007uip.1; mouse.
DR   UCSC; uc007uiq.1; mouse.
DR   UCSC; uc007uir.1; mouse.
DR   UCSC; uc007uis.1; mouse.
DR   CTD; 219150; -.
DR   MGI; MGI:2445066; Hmbox1.
DR   eggNOG; roNOG11681; -.
DR   GeneTree; ENSGT00530000063140; -.
DR   HOGENOM; HBG507112; -.
DR   HOVERGEN; HBG061176; -.
DR   InParanoid; Q8BJA3; -.
DR   OMA; NQNGRES; -.
DR   OrthoDB; EOG49ZXPD; -.
DR   NextBio; 376615; -.
DR   ArrayExpress; Q8BJA3; -.
DR   Bgee; Q8BJA3; -.
DR   CleanEx; MM_HMBOX1; -.
DR   Genevestigator; Q8BJA3; -.
DR   GermOnline; ENSMUSG00000021972; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0016563; F:transcription activator activity; IEA:InterPro.
DR   GO; GO:0016564; F:transcription repressor activity; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; ISS:UniProtKB.
DR   InterPro; IPR006899; HNF-1_N.
DR   InterPro; IPR001356; Homeobox.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR010982; Lambda_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Pfam; PF04814; HNF-1_N; 1.
DR   Pfam; PF00046; Homeobox; 1.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
DR   SUPFAM; SSF47413; Lambda_like_DNA; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; FALSE_NEG.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; DNA-binding; Homeobox; Nucleus;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN         1    419       Homeobox-containing protein 1.
FT                                /FTId=PRO_0000233288.
FT   DNA_BIND    267    341       Homeobox.
FT   VAR_SEQ     343    343       I -> IE (in isoform 2).
FT                                /FTId=VSP_018114.
FT   VAR_SEQ     375    419       DDSTSHSDHQDPISLAVEMAAVNHTILALARQGANEIKTEA
FT                                LDDD -> SSFAGALIQLERQKGPPGCQQLPVLSGLL (in
FT                                isoform 2 and isoform 4).
FT                                /FTId=VSP_018115.
FT   VAR_SEQ     376    419       DSTSHSDHQDPISLAVEMAAVNHTILALARQGANEIKTEAL
FT                                DDD -> TWQARNGEEEEERSSEGGREAEKVEEERRI (in
FT                                isoform 3).
FT                                /FTId=VSP_018116.
SQ   SEQUENCE   419 AA;  47116 MW;  3F204060F1D0AE70 CRC64;
     MLSSFPVVLL ETMSHYTDEP RFTIEQIDLL QRLRRTGMTK HEILHALETL DRLDQEHSDK
     FGRRSSYGGS SYGNSTNNVP ASSSTATAST QTQHSGMSPS PSNSYDTSPL PCTTNQNGRE
     NNDRLSTSNG KMSPSRYHAN SMGQRSYSFE ASEEDLDVDD KVEELMRRDS SVIKEEIKAF
     LANRRISQAV VAQVTGISQS RISHWLLQQG SDLSEQKKRA FYRWYQLEKT NPGATLSMRP
     APIPIEDPEW RQTPPPVSAT PGTFRLRRGS RFTWRKECLA VMESYFNENQ YPDEAKREEI
     ANACNAVIQK PGKKLSDLER VTSLKVYNWF ANRRKEIKRR ANIAAILESH GIDVQSPGGH
     SNSDDVDGND YSEQDDSTSH SDHQDPISLA VEMAAVNHTI LALARQGANE IKTEALDDD
//
ID   CHM2B_MOUSE             Reviewed;         213 AA.
AC   Q8BJF9; Q80UZ4; Q9CT65;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Charged multivesicular body protein 2b;
DE   AltName: Full=Chromatin-modifying protein 2b;
DE            Short=CHMP2b;
GN   Name=Chmp2b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and Czech II; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=16041373; DOI=10.1038/ng1609;
RA   Skibinski G., Parkinson N.J., Brown J.M., Chakrabarti L., Lloyd S.L.,
RA   Hummerich H., Nielsen J.E., Hodges J.R., Spillantini M.G.,
RA   Thusgaard T., Brandner S., Brun A., Rossor M.N., Gade A.,
RA   Johannsen P., Soerensen S.A., Gydesen S., Fisher E.M.C., Collinge J.;
RT   "Mutations in the endosomal ESCRTIII-complex subunit CHMP2B in
RT   frontotemporal dementia.";
RL   Nat. Genet. 37:806-808(2005).
CC   -!- FUNCTION: Probable core component of the endosomal sorting
CC       required for transport complex III (ESCRT-III) which is involved
CC       in multivesicular bodies (MVBs) formation and sorting of endosomal
CC       cargo proteins into MVBs. MVBs contain intraluminal vesicles
CC       (ILVs) that are generated by invagination and scission from the
CC       limiting membrane of the endosome and mostly are delivered to
CC       lysosomes enabling degradation of membrane proteins, such as
CC       stimulated growth factor receptors, lysosomal enzymes and lipids.
CC       The MVB pathway appears to require the sequential function of
CC       ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly
CC       dissociate from the invaginating membrane before the ILV is
CC       released. The ESCRT machinery also functions in topologically
CC       equivalent membrane fission events, such as the terminal stages of
CC       cytokinesis. ESCRT-III proteins are believed to mediate the
CC       necessary vesicle extrusion and/or membrane fission activities,
CC       possibly in conjunction with the AAA ATPase VPS4 (By similarity).
CC   -!- SUBUNIT: Probable core component of the endosomal sorting required
CC       for transport complex III (ESCRT-III). ESCRT-III components are
CC       thought to multimerize to form a flat lattice on the perimeter
CC       membrane of the endosome. Several assembly forms of ESCRT-III may
CC       exist that interact and act sequentally. Interacts with CHMP2A.
CC       Interacts with VPS4A. Interacts with VPS4B; the interaction is
CC       direct (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity). Late
CC       endosome membrane; Peripheral membrane protein (By similarity).
CC   -!- TISSUE SPECIFICITY: In brain, it is expressed in all neuronal
CC       populations with a relatively enhanced expression in the
CC       hippocampus, frontal and temporal lobes and in both granule and
CC       Purkinje cells of the cerebellum. Not expressed in astrocytes or
CC       oligodendrocytes.
CC   -!- SIMILARITY: Belongs to the SNF7 family.
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DR   EMBL; AK004506; BAB23339.1; -; mRNA.
DR   EMBL; AK084111; BAC39118.1; -; mRNA.
DR   EMBL; BC042626; AAH42626.1; -; mRNA.
DR   EMBL; BC055809; AAH55809.1; -; mRNA.
DR   IPI; IPI00222386; -.
DR   RefSeq; NP_081155.1; NM_026879.2.
DR   UniGene; Mm.432944; -.
DR   ProteinModelPortal; Q8BJF9; -.
DR   SMR; Q8BJF9; 4-182.
DR   STRING; Q8BJF9; -.
DR   PhosphoSite; Q8BJF9; -.
DR   PRIDE; Q8BJF9; -.
DR   Ensembl; ENSMUST00000004965; ENSMUSP00000004965; ENSMUSG00000004843.
DR   GeneID; 68942; -.
DR   KEGG; mmu:68942; -.
DR   UCSC; uc007zqj.1; mouse.
DR   CTD; 68942; -.
DR   MGI; MGI:1916192; Chmp2b.
DR   eggNOG; roNOG12224; -.
DR   GeneTree; ENSGT00550000074737; -.
DR   HOGENOM; HBG464741; -.
DR   HOVERGEN; HBG102628; -.
DR   InParanoid; Q8BJF9; -.
DR   OMA; GNKEACK; -.
DR   OrthoDB; EOG469QW1; -.
DR   PhylomeDB; Q8BJF9; -.
DR   NextBio; 328237; -.
DR   ArrayExpress; Q8BJF9; -.
DR   Bgee; Q8BJF9; -.
DR   CleanEx; MM_CHMP2B; -.
DR   Genevestigator; Q8BJF9; -.
DR   GermOnline; ENSMUSG00000004843; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR005024; Snf7.
DR   Pfam; PF03357; Snf7; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Endosome; Membrane; Phosphoprotein;
KW   Protein transport; Transport.
FT   CHAIN         1    213       Charged multivesicular body protein 2b.
FT                                /FTId=PRO_0000211470.
FT   COILED       25     55       Potential.
FT   MOTIF       201    211       MIT-interacting motif.
FT   MOD_RES     199    199       Phosphoserine (By similarity).
FT   CONFLICT    131    131       E -> D (in Ref. 1; BAB23339).
SQ   SEQUENCE   213 AA;  23935 MW;  AC5B40ED59E4489B CRC64;
     MASLFKKKTV DDVIKEQNRE LRGTQRAIIR DRAALEKQEK QLELEIKKMA KIGNKEACRV
     LAKQLVHLRK QKTRTFAVSS KVTSMSTQTK VMNSQMKMAG AMSTTAKTMQ AVNKKMDPQK
     TLQTMQNFQK ENMKMEMTEE MINDTLDDIF DGSDDEEESQ DIVNQVLDEI GIEISGKMAK
     APSAARSLPS ASTSKATISD EEIERQLKAL GVD
//
ID   F164A_MOUSE             Reviewed;         324 AA.
AC   Q8BJH1; Q3TCP6;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Protein FAM164A;
GN   Name=Fam164a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BJH1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BJH1-2; Sequence=VSP_023580;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the UPF0418 family.
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DR   EMBL; AK083941; BAC39075.1; -; mRNA.
DR   EMBL; AK170609; BAE41909.1; -; mRNA.
DR   EMBL; BC087731; AAH87731.1; -; mRNA.
DR   IPI; IPI00222393; -.
DR   IPI; IPI00653324; -.
DR   RefSeq; NP_775273.1; NM_173181.3.
DR   UniGene; Mm.332366; -.
DR   ProteinModelPortal; Q8BJH1; -.
DR   PhosphoSite; Q8BJH1; -.
DR   PRIDE; Q8BJH1; -.
DR   Ensembl; ENSMUST00000051064; ENSMUSP00000054734; ENSMUSG00000043542.
DR   Ensembl; ENSMUST00000099249; ENSMUSP00000096855; ENSMUSG00000043542.
DR   Ensembl; ENSMUST00000108389; ENSMUSP00000104026; ENSMUSG00000043542.
DR   GeneID; 67306; -.
DR   KEGG; mmu:67306; -.
DR   UCSC; uc008oog.1; mouse.
DR   CTD; 67306; -.
DR   MGI; MGI:1914556; Fam164a.
DR   eggNOG; roNOG15126; -.
DR   GeneTree; ENSGT00390000003459; -.
DR   HOGENOM; HBG402978; -.
DR   HOVERGEN; HBG107871; -.
DR   InParanoid; Q8BJH1; -.
DR   OrthoDB; EOG4SQWXV; -.
DR   PhylomeDB; Q8BJH1; -.
DR   NextBio; 324186; -.
DR   ArrayExpress; Q8BJH1; -.
DR   Bgee; Q8BJH1; -.
DR   Genevestigator; Q8BJH1; -.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    324       Protein FAM164A.
FT                                /FTId=PRO_0000280247.
FT   MOD_RES     243    243       Phosphothreonine (By similarity).
FT   MOD_RES     291    291       Phosphoserine (By similarity).
FT   VAR_SEQ     235    270       Missing (in isoform 2).
FT                                /FTId=VSP_023580.
SQ   SEQUENCE   324 AA;  35152 MW;  E29BE2760095D167 CRC64;
     MDGLEENGSV VQVGDLLPCK ICGRTFFPLA LKKHGPICQK TATKKRKTFD SSRQRAEGTD
     IPTVKPLKPR PEPPKKPSNW RRKHEEFIAT IRAAKGLDQA LKEGGKLPPP PPPSYDPDYI
     QCPYCQRRFN ENAADRHINF CKEQAARISN KGKFSTDSKG KPASRPQYKP SPLKKSNPPG
     IPSSGSSRLP QPSTTSKTIV GVPTGKASSV NSPLGNKPQT LSPSHRAIAA PQAGANTKAR
     NTTPPSLARN SVAGVLTNKR KTLTENYAAR PDGDYTSSVN GGNSKGIEGN SSGHLPKFCH
     ECGTKYPVEW AKFCCECGIR RMIL
//
ID   S6A17_MOUSE             Reviewed;         727 AA.
AC   Q8BJI1; B2RUH5; Q8C057; Q8CGQ9;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Orphan sodium- and chloride-dependent neurotransmitter transporter NTT4;
DE   AltName: Full=Solute carrier family 6 member 17;
GN   Name=Slc6a17; Synonyms=Ntt4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RA   Liu Q.-R., Uhl G.R.;
RT   "Sodium and chloride dependent mouse orphan neurotransmitter
RT   transporter NTT4 cDNA.";
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-377, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-665; THR-700 AND
RP   THR-722, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Not yet known, orphan transporter.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF)
CC       (TC 2.A.22) family. SLC6A17 subfamily.
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DR   EMBL; AY155578; AAN75010.1; -; mRNA.
DR   EMBL; AK083807; BAC39024.1; -; mRNA.
DR   EMBL; AK032262; BAC27785.1; -; mRNA.
DR   EMBL; BC141148; AAI41149.1; -; mRNA.
DR   EMBL; BC171962; AAI71962.1; -; mRNA.
DR   IPI; IPI00229554; -.
DR   PIR; C46027; C46027.
DR   RefSeq; NP_758475.1; NM_172271.2.
DR   UniGene; Mm.212867; -.
DR   ProteinModelPortal; Q8BJI1; -.
DR   STRING; Q8BJI1; -.
DR   PhosphoSite; Q8BJI1; -.
DR   PRIDE; Q8BJI1; -.
DR   Ensembl; ENSMUST00000029499; ENSMUSP00000029499; ENSMUSG00000027894.
DR   GeneID; 229706; -.
DR   KEGG; mmu:229706; -.
DR   UCSC; uc008qxb.1; mouse.
DR   CTD; 229706; -.
DR   MGI; MGI:2442535; Slc6a17.
DR   GeneTree; ENSGT00590000082733; -.
DR   HOGENOM; HBG702834; -.
DR   HOVERGEN; HBG071421; -.
DR   InParanoid; Q8BJI1; -.
DR   OrthoDB; EOG4GMTWF; -.
DR   NextBio; 379623; -.
DR   ArrayExpress; Q8BJI1; -.
DR   Bgee; Q8BJI1; -.
DR   Genevestigator; Q8BJI1; -.
DR   GermOnline; ENSMUSG00000027894; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; IEA:InterPro.
DR   GO; GO:0005328; F:neurotransmitter:sodium symporter activity; IEA:InterPro.
DR   InterPro; IPR000175; Na/ntran_symport.
DR   InterPro; IPR002438; Na/ntran_symport_orphan.
DR   PANTHER; PTHR11616; Na/ntran_symport; 1.
DR   Pfam; PF00209; SNF; 1.
DR   PRINTS; PR00176; NANEUSMPORT.
DR   PRINTS; PR01206; ORPHTRNSPORT.
DR   PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR   PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
DR   PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Neurotransmitter transport; Phosphoprotein;
KW   Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    727       Orphan sodium- and chloride-dependent
FT                                neurotransmitter transporter NTT4.
FT                                /FTId=PRO_0000214804.
FT   TOPO_DOM      1     68       Cytoplasmic (Potential).
FT   TRANSMEM     69     89       Helical; Name=1; (Potential).
FT   TOPO_DOM     90     96       Extracellular (Potential).
FT   TRANSMEM     97    116       Helical; Name=2; (Potential).
FT   TOPO_DOM    117    140       Cytoplasmic (Potential).
FT   TRANSMEM    141    161       Helical; Name=3; (Potential).
FT   TOPO_DOM    162    224       Extracellular (Potential).
FT   TRANSMEM    225    243       Helical; Name=4; (Potential).
FT   TOPO_DOM    244    251       Cytoplasmic (Potential).
FT   TRANSMEM    252    269       Helical; Name=5; (Potential).
FT   TOPO_DOM    270    304       Extracellular (Potential).
FT   TRANSMEM    305    322       Helical; Name=6; (Potential).
FT   TOPO_DOM    323    333       Cytoplasmic (Potential).
FT   TRANSMEM    334    355       Helical; Name=7; (Potential).
FT   TOPO_DOM    356    451       Extracellular (Potential).
FT   TRANSMEM    452    471       Helical; Name=8; (Potential).
FT   TOPO_DOM    472    494       Cytoplasmic (Potential).
FT   TRANSMEM    495    513       Helical; Name=9; (Potential).
FT   TOPO_DOM    514    528       Extracellular (Potential).
FT   TRANSMEM    529    549       Helical; Name=10; (Potential).
FT   TOPO_DOM    550    569       Cytoplasmic (Potential).
FT   TRANSMEM    570    591       Helical; Name=11; (Potential).
FT   TOPO_DOM    592    618       Extracellular (Potential).
FT   TRANSMEM    619    641       Helical; Name=12; (Potential).
FT   TOPO_DOM    642    727       Cytoplasmic (Potential).
FT   MOD_RES     377    377       Phosphotyrosine.
FT   MOD_RES     665    665       Phosphoserine.
FT   MOD_RES     700    700       Phosphothreonine.
FT   MOD_RES     722    722       Phosphothreonine.
FT   CARBOHYD    186    186       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    393    393       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    434    436       Missing (in Ref. 1; AAN75010).
SQ   SEQUENCE   727 AA;  81071 MW;  0EAA2B192E77D7FA CRC64;
     MPKNSKVTQR EHSNEHVTES VADLLALEEP VDYKQSVLNV AGETGGKQKV AEEELDTEDR
     PAWNSKLQYI LAQIGFSVGL GNIWRFPYLC QKNGGGAYLV PYLVLLIIIG IPLFFLELAV
     GQRIRRGSIG VWHYVCPRLG GIGFSSCIVC LFVGLYYNVI IGWSVFYFFK SFQYPLPWSE
     CPVIRNGTVA VVEPECEKSS ATTYFWYREA LDISNSISES GGLNWKMTLC LLVAWSIVGM
     AVVKGIQSSG KVMYFSSLFP YVVLACFLVR GLLLRGAVDG ILHMFTPKLD KMLDPQVWRE
     AATQVFFALG LGFGGVIAFS SYNKQDNNCH FDAALVSFIN FFTSVLATLV VFAVLGFKAN
     IMNEKCVVEN AEKILGYLNS NVLSRDLIPP HVNFSHLTTK DYSEMYSVIM TVKEKQFPAL
     GLDPCLLEDE LDKSVQGTGL AFIAFTEAMT HFPASPFWSV MFFLMLINLG LGSMIGTMAG
     ITTPIIDTFK VPKEMFTVGC CVFAFFVGLL FVQRSGNYFV TMFDDYSATL PLTVIVILEN
     IAVAWIYGTK KFMQELTEML GFQPYRFYFY MWKFVSPLCM AVLTTASIIQ LGVSPPGYSA
     WIKEEAAERY LYFPNWAMAL LITLIAVATL PIPVVFILRH FHLLSDGSNT LSVSYKKGRM
     MKDISNLEEN DETRFILSKV PSEAPSPMPT HRSYLGPGST SPLDNSNNPN GRYGSGYLLA
     STPESEL
//
ID   Q8BJI6_MOUSE            Unreviewed;       822 AA.
AC   Q8BJI6;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Trappc8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
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DR   EMBL; AK083747; BAC39011.1; -; mRNA.
DR   IPI; IPI00465597; -.
DR   RefSeq; NP_083767.2; NM_029491.2.
DR   RefSeq; NP_796012.2; NM_177038.3.
DR   UniGene; Mm.273769; -.
DR   PhosphoSite; Q8BJI6; -.
DR   PRIDE; Q8BJI6; -.
DR   Ensembl; ENSMUST00000097658; ENSMUSP00000095262; ENSMUSG00000033382.
DR   GeneID; 75964; -.
DR   KEGG; mmu:75964; -.
DR   UCSC; uc008eey.1; mouse.
DR   CTD; 75964; -.
DR   MGI; MGI:2443008; Trappc8.
DR   GeneTree; ENSGT00390000000568; -.
DR   HOVERGEN; HBG036226; -.
DR   NextBio; 344347; -.
DR   ArrayExpress; Q8BJI6; -.
DR   Bgee; Q8BJI6; -.
DR   Genevestigator; Q8BJI6; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR011990; TPR-like_helical.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 2.
PE   1: Evidence at protein level;
SQ   SEQUENCE   822 AA;  92938 MW;  07E236E68D6B2F1C CRC64;
     MAQCVQSVQE LIPDSFVPCV AALCSDEAER LTRLNHLSFS ELLKPFSRLT SEVHMRDPNN
     QLHIIKNLKI AVSNIVTQPP QPGAIGKLLN DVVSGSQPAE GLVANVITAG DYDLNISATT
     PWFESYRETF LQSMPASDHE FLNHYLACML VASSGEAEPM EQFSKLSQEQ HRIQHNNDYS
     YPKWFIPNTL KYYVLLHDVT SGDEQRAESI YEEMKQKYGT QGCYLLKINS RAPNRASDEQ
     IPDPWSQYLQ KNSIQNQESY EDGPCTMTSS KNSDSNLLSL DGLDNEVKVD GLPNNFRIHP
     LQIDQCGDPP NNTDGSESKS ASSVHETKKA STAVIRGACL TLTDHDRIRQ FIQEFTFRGL
     LPHIEKTIRQ LNDQLISRKG LSRSLFSATK KWFSGSKVPE KSINELKNTS GLLYPPEAPE
     LQIRKMADLC FLVQHYDLAY SCYHTAKKDF LNDQAMLYAA GALEMAAVSA FLQPGAPRPY
     PAHYMDTAIQ TYRDICKNMV LAERCVLLSA EILKSQSKYS EAAALLIRLT SEDSDLRSAL
     LLEQAAHCFI NMKSPMVRKY AFHMILAGHR FSKAGQKKHA LRCYCQAMQV YKGKGWSLAE
     DHINFTIGRQ SYTLRQLDNA VSAFRHILIN ESKQSAAQQG AFLREYLYVY KNVNQLSPDG
     PLPQLPLPYI NSSATRVFFG HDRRPADGEK QAATHISLDQ EYDSESSQQW RELEEHVVAV
     ANKGVIPSSF YPTQYCLNSY SDNSRFPLAV VEEPITVEVA FRNPLKVPLL LSDLSLLWKF
     QPKDASGKDI EKVKERVSYC RYHDAPDFRC YHSVHLRDKP KV
//
ID   SUN2_MOUSE              Reviewed;         731 AA.
AC   Q8BJS4; Q3TBU0; Q3U160; Q6B4H2;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 3.
DT   08-FEB-2011, entry version 61.
DE   RecName: Full=SUN domain-containing protein 2;
DE   AltName: Full=Protein unc-84 homolog B;
DE   AltName: Full=Sad1/unc-84 protein-like 2;
GN   Name=Sun2; Synonyms=Unc84b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, SUBUNIT,
RP   AND ASSOCIATION WITH THE CENTROSOME.
RX   PubMed=17132086; DOI=10.1089/dna.2006.25.554;
RA   Wang Q., Du X., Cai Z., Greene M.I.;
RT   "Characterization of the structures involved in localization of the
RT   SUN proteins to the nuclear envelope and the centrosome.";
RL   DNA Cell Biol. 25:554-562(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA   Oshima A., Takahashi-Fujii A., Tanase T., Imose N., Takeuchi K.,
RA   Arita M., Musashino K., Yuuki H., Hara H., Sugiyama T., Irie R.,
RA   Otsuki T., Sato H., Ota T., Wakamatsu A., Ishii S., Yamamoto J.,
RA   Isono Y., Kawai-Hio Y., Saito K., Nishikawa T., Kimura K.,
RA   Yamashita H., Matsuo K., Nakamura Y., Sekine M., Kikuchi H., Kanda K.,
RA   Wagatsuma M., Murakawa K., Kanehori K., Sugiyama A., Kawakami B.,
RA   Suzuki Y., Sugano S., Nagahari K., Masuho Y., Nagai K., Isogai T.;
RT   "NEDO cDNA sequencing project.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Aorta, Dendritic cell, Spleen, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=12393179; DOI=10.1016/S0925-4439(02)00171-0;
RA   Sun G., Yuen Chan S., Yuan Y., Wang Chan K., Qiu G., Sun K.,
RA   Ping Leung M.;
RT   "Isolation of differentially expressed genes in human heart tissues.";
RL   Biochim. Biophys. Acta 1588:241-246(2002).
RN   [6]
RP   INTERACTION WITH SYNE2, AND FUNCTION OF THE LINC COMPLEXES.
RX   PubMed=16380439; DOI=10.1083/jcb.200509124;
RA   Crisp M., Liu Q., Roux K., Rattner J.B., Shanahan C., Burke B.,
RA   Stahl P.D., Hodzic D.;
RT   "Coupling of the nucleus and cytoplasm: role of the LINC complex.";
RL   J. Cell Biol. 172:41-53(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH LMNA AND SYN2.
RX   PubMed=19843581; DOI=10.1242/jcs.057075;
RA   Ostlund C., Folker E.S., Choi J.C., Gomes E.R., Gundersen G.G.,
RA   Worman H.J.;
RT   "Dynamics and molecular interactions of linker of nucleoskeleton and
RT   cytoskeleton (LINC) complex proteins.";
RL   J. Cell Sci. 122:4099-4108(2009).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-650, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SYNE2.
RX   PubMed=19874786; DOI=10.1016/j.neuron.2009.08.018;
RA   Zhang X., Lei K., Yuan X., Wu X., Zhuang Y., Xu T., Xu R., Han M.;
RT   "SUN1/2 and Syne/Nesprin-1/2 complexes connect centrosome to the
RT   nucleus during neurogenesis and neuronal migration in mice.";
RL   Neuron 64:173-187(2009).
RN   [11]
RP   FUNCTION.
RX   PubMed=19509342; DOI=10.1073/pnas.0812037106;
RA   Lei K., Zhang X., Ding X., Guo X., Chen M., Zhu B., Xu T., Zhuang Y.,
RA   Xu R., Han M.;
RT   "SUN1 and SUN2 play critical but partially redundant roles in
RT   anchoring nuclei in skeletal muscle cells in mice.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:10207-10212(2009).
RN   [12]
RP   SUBCELLULAR LOCATION, INTERACTION WITH EMD AND LMNA, DOMAIN, AND
RP   ASSOCIATION WITH THE NUCLEOSKELETON.
RX   PubMed=19933576; DOI=10.1074/jbc.M109.071910;
RA   Haque F., Mazzeo D., Patel J.T., Smallwood D.T., Ellis J.A.,
RA   Shanahan C.M., Shackleton S.;
RT   "Mammalian SUN protein interaction networks at the inner nuclear
RT   membrane and their role in laminopathy disease processes.";
RL   J. Biol. Chem. 285:3487-3498(2010).
RN   [13]
RP   FUNCTION.
RX   PubMed=20724637; DOI=10.1126/science.1189072;
RA   Luxton G.W., Gomes E.R., Folker E.S., Vintinner E., Gundersen G.G.;
RT   "Linear arrays of nuclear envelope proteins harness retrograde actin
RT   flow for nuclear movement.";
RL   Science 329:956-959(2010).
CC   -!- FUNCTION: Component of SUN-protein-containing multivariate
CC       complexes also called LINC complexes which link the nucleoskeleton
CC       and cytoskeleton by providing versatile outer nuclear membrane
CC       attachment sites for cytoskeletal filaments. Specifically, Syne2
CC       and Sun2 assemble in arrays of transmembrane actin-associated
CC       nuclear (TAN) lines which are bound to F-actin cables and couple
CC       the nucleus to retrograde actin flow during actin-dependent
CC       nuclear movement. Required for interkinetic nuclear migration
CC       (INM) and essential for nucleokinesis and centrosome-nucleus
CC       coupling during radial neuronal migration in the cerebral cortex
CC       and during glial migration. Anchors chromosome movement in the
CC       prophase of meiosis and is involved in selective gene expression
CC       of coding and non-coding RNAs needed for gametogenesis. Required
CC       for telomere attachment to nuclear envelope and gametogenesis. May
CC       also function on endocytic vesicles as a receptor for Rab5-GDP and
CC       participate in the activation of Rab5.
CC   -!- SUBUNIT: Component of LINC complexes composed of SUN domain-
CC       containing proteins SUN1 or SUN2 coupled to KASH domain-containing
CC       proteins (SYNE1, SYNE2 or SYNE3), also called nesprins. Interacts
CC       with EMD, LMNA and SYNE2. Interacts with RAB5A, SYNE1 and SYNE3
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus inner membrane; Single-pass type II
CC       membrane protein. Endosome membrane; Single-pass type II membrane
CC       protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BJS4-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q8BJS4-2; Sequence=VSP_039554;
CC       Name=3;
CC         IsoId=Q8BJS4-3; Sequence=VSP_039553;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart, placenta and
CC       muscle.
CC   -!- DOMAIN: The SUN domain may play a role in the nuclear anchoring
CC       and/or migration.
CC   -!- SIMILARITY: Contains 1 SUN domain.
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DR   EMBL; AY682987; AAT90499.1; -; mRNA.
DR   EMBL; AK128958; BAC87662.1; -; mRNA.
DR   EMBL; AK080116; BAC37829.1; -; mRNA.
DR   EMBL; AK156246; BAE33640.1; -; mRNA.
DR   EMBL; AK171058; BAE42217.1; -; mRNA.
DR   EMBL; CH466550; EDL04635.1; -; Genomic_DNA.
DR   IPI; IPI00380009; -.
DR   IPI; IPI00460291; -.
DR   IPI; IPI00969334; -.
DR   RefSeq; NP_919323.2; NM_194342.2.
DR   UniGene; Mm.202715; -.
DR   ProteinModelPortal; Q8BJS4; -.
DR   IntAct; Q8BJS4; 1.
DR   STRING; Q8BJS4; -.
DR   PhosphoSite; Q8BJS4; -.
DR   PRIDE; Q8BJS4; -.
DR   Ensembl; ENSMUST00000089311; ENSMUSP00000086724; ENSMUSG00000042524.
DR   GeneID; 223697; -.
DR   KEGG; mmu:223697; -.
DR   UCSC; uc007wug.1; mouse.
DR   CTD; 223697; -.
DR   MGI; MGI:2443011; Sun2.
DR   GeneTree; ENSGT00390000011587; -.
DR   HOVERGEN; HBG056957; -.
DR   NextBio; 376830; -.
DR   ArrayExpress; Q8BJS4; -.
DR   Bgee; Q8BJS4; -.
DR   CleanEx; MM_UNC84B; -.
DR   Genevestigator; Q8BJS4; -.
DR   GermOnline; ENSMUSG00000042524; Mus musculus.
DR   GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:MGI.
DR   GO; GO:0005637; C:nuclear inner membrane; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0051642; P:centrosome localization; IMP:UniProtKB.
DR   GO; GO:0031022; P:nuclear migration along microfilament; IMP:UniProtKB.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR   InterPro; IPR012919; Sad1_UNC_C.
DR   Pfam; PF07738; Sad1_UNC; 1.
DR   PROSITE; PS51469; SUN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Endosome; Glycoprotein; Membrane;
KW   Nucleus; Phosphoprotein; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    731       SUN domain-containing protein 2.
FT                                /FTId=PRO_0000218914.
FT   TOPO_DOM      1    226       Nuclear (By similarity).
FT   TRANSMEM    227    247       Helical; (Potential).
FT   TOPO_DOM    248    731       Perinuclear space.
FT   DOMAIN      569    730       SUN.
FT   REGION        1    128       LMNA-binding.
FT   COILED      396    452       Potential.
FT   COILED      486    519       Potential.
FT   MOD_RES      39     39       Phosphoserine.
FT   CARBOHYD    650    650       N-linked (GlcNAc...).
FT   VAR_SEQ     154    185       Missing (in isoform 3).
FT                                /FTId=VSP_039553.
FT   VAR_SEQ     217    218       Missing (in isoform 2).
FT                                /FTId=VSP_039554.
FT   CONFLICT    106    106       S -> G (in Ref. 3; BAE42217).
FT   CONFLICT    412    412       M -> V (in Ref. 2; BAC87662).
FT   CONFLICT    451    451       D -> Y (in Ref. 2; BAC87662).
FT   CONFLICT    579    579       E -> K (in Ref. 3; BAE42217).
SQ   SEQUENCE   731 AA;  81605 MW;  67830D40C33E3DBA CRC64;
     MSRRSQRLTR YSQDDNDGGS SSSGASSVAG SQGTVFKDSP LRTLKRKSSN MKHLSPAPQL
     GPSSDSHTSY YSESVVRESY IGSPRAVSLA RSALLDDHLH SEPYWSGDLR GRRRRGTGGS
     ESSKANGLTA ESKASEDFFG SSSGYSSEDD LAGYTDSDQH SSGSRLRSAA SRAGSFVWTL
     VTFPGRLFGL LYWWIGTTWY RLTTAASLLD VFVLTRSRHF SLNLKSFLWF LLLLLLLTGL
     TYGAWHFYPL GLQTLQPAVV SWWAAKESRK QPEVWESRDA SQHFQAEQRV LSRVHSLERR
     LEALAADFSS NWQKEAIRLE RLELRQGAAG HGGGSSLSHE DALSLLEGLV SRREATLKED
     LRRDTVAHIQ EELATLRAEH HQDSEDLFKK IVQASQESEA RVQQLKTEWK SMTQEAFQES
     SVKELGRLEA QLASLRQELA ALTLKQNSVA DEVGLLPQKI QAARADVESQ FPDWIRQFLL
     GDRGARSGLL QRDEMHAQLQ ELENKILTKM AEMQGKSARE AAASLGQILQ KEGIVGVTEE
     QVHRIVKQAL QRYSEDRIGM VDYALESGGA SVISTRCSET YETKTALLSL FGIPLWYHSQ
     SPRVILQPDV HPGNCWAFQG PQGFAVVRLS ARIRPTAVTL EHVPKALSPN STISSAPKDF
     AIFGFDEDLQ QEGTLLGTFA YDQDGEPIQT FYFQASKMAT YQVVELRILT NWGHPEYTCI
     YRFRVHGEPA H
//
ID   SGTA_MOUSE              Reviewed;         315 AA.
AC   Q8BJU0; Q8BGA6; Q99L52;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 2.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Small glutamine-rich tetratricopeptide repeat-containing protein alpha;
DE   AltName: Full=Alpha-SGT;
GN   Name=Sgta; Synonyms=Sgt;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-82, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-82 AND SER-307, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-82, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Co-chaperone that binds directly to HSC70 and HSP70 and
CC       regulates their ATPase activity (By similarity).
CC   -!- SUBUNIT: Homooligomerize (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BJU0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BJU0-2; Sequence=VSP_009300;
CC   -!- SIMILARITY: Belongs to the SGT family.
CC   -!- SIMILARITY: Contains 3 TPR repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK039966; BAC30486.1; -; mRNA.
DR   EMBL; AK051005; BAC34494.1; -; mRNA.
DR   EMBL; AK079168; BAC37566.1; -; mRNA.
DR   EMBL; BC003836; AAH03836.1; -; mRNA.
DR   IPI; IPI00116331; -.
DR   IPI; IPI00399631; -.
DR   RefSeq; NP_078775.1; NM_024499.1.
DR   UniGene; Mm.30068; -.
DR   ProteinModelPortal; Q8BJU0; -.
DR   SMR; Q8BJU0; 31-248.
DR   STRING; Q8BJU0; -.
DR   PhosphoSite; Q8BJU0; -.
DR   PRIDE; Q8BJU0; -.
DR   Ensembl; ENSMUST00000005067; ENSMUSP00000005067; ENSMUSG00000004937.
DR   GeneID; 52551; -.
DR   KEGG; mmu:52551; -.
DR   UCSC; uc007gft.1; mouse.
DR   UCSC; uc007gfu.1; mouse.
DR   CTD; 52551; -.
DR   MGI; MGI:1098703; Sgta.
DR   GeneTree; ENSGT00600000084385; -.
DR   HOGENOM; HBG736033; -.
DR   HOVERGEN; HBG000885; -.
DR   InParanoid; Q8BJU0; -.
DR   OMA; GAVRDCE; -.
DR   OrthoDB; EOG4DJJWZ; -.
DR   PhylomeDB; Q8BJU0; -.
DR   NextBio; 309129; -.
DR   ArrayExpress; Q8BJU0; -.
DR   Bgee; Q8BJU0; -.
DR   Genevestigator; Q8BJU0; -.
DR   GermOnline; ENSMUSG00000004937; Mus musculus.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR001440; TPR-1.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
DR   Pfam; PF00515; TPR_1; 3.
DR   SMART; SM00028; TPR; 3.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Chaperone; Phosphoprotein; Repeat;
KW   TPR repeat.
FT   CHAIN         1    315       Small glutamine-rich tetratricopeptide
FT                                repeat-containing protein alpha.
FT                                /FTId=PRO_0000106366.
FT   REPEAT       92    125       TPR 1.
FT   REPEAT      126    159       TPR 2.
FT   REPEAT      160    193       TPR 3.
FT   COMPBIAS    276    288       Gln-rich.
FT   MOD_RES      82     82       Phosphothreonine.
FT   MOD_RES     138    138       N6-acetyllysine (By similarity).
FT   MOD_RES     303    303       Phosphoserine (By similarity).
FT   MOD_RES     305    305       Phosphothreonine (By similarity).
FT   MOD_RES     307    307       Phosphoserine.
FT   VAR_SEQ      70     70       Missing (in isoform 2).
FT                                /FTId=VSP_009300.
FT   CONFLICT    207    207       L -> F (in Ref. 1; BAC37566).
SQ   SEQUENCE   315 AA;  34322 MW;  6FB8D3978CF56D4C CRC64;
     MDNRKRLAYA IIQFLHGQLR HGGLSCDAQE SLEVAIQCLE TAFGVTLEDS DLALPQTLPE
     IFEAATSSKQ EMPQDPRAPD RTPPSEEDSA EAERLKTEGN EQMKLENFEA AVHLYGKAIE
     LNPANAVYFC NRAAAYSKLG NYVGAVQDCE RAIGIDPGYS KAYGRMGLAL SSLNKHAEAV
     AYYKKALELD PDNDTYKSNL KIAELKLREA PSPTGGVGSL DIAGLLNNPH FITMASSLMN
     SPQLQQLMSG MISGGHNPLG TPGSSPQQSD LASLIQAGQQ FAQQMQQQNP EFVEQIRSQV
     VRSRTPSASH EEQQE
//
ID   FA73B_MOUSE             Reviewed;         593 AA.
AC   Q8BK03; A6PX05; Q3U4J7; Q3UST7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Protein FAM73B;
GN   Name=Fam73b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Corpora quadrigemina, Dendritic cell, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; THR-208; SER-224;
RP   SER-228; THR-273 AND SER-276, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BK03-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BK03-2; Sequence=VSP_030093, VSP_030094;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the FAM73 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE32434.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK077618; BAC36904.1; -; mRNA.
DR   EMBL; AK140122; BAE24244.1; -; mRNA.
DR   EMBL; AK154200; BAE32434.1; ALT_INIT; mRNA.
DR   EMBL; AL954388; CAM23170.1; -; Genomic_DNA.
DR   EMBL; BC051404; AAH51404.1; -; mRNA.
DR   IPI; IPI00222443; -.
DR   IPI; IPI00652506; -.
DR   RefSeq; NP_780601.1; NM_175392.3.
DR   UniGene; Mm.254974; -.
DR   PhosphoSite; Q8BK03; -.
DR   PRIDE; Q8BK03; -.
DR   Ensembl; ENSMUST00000077977; ENSMUSP00000077127; ENSMUSG00000026858.
DR   Ensembl; ENSMUST00000100214; ENSMUSP00000097787; ENSMUSG00000026858.
DR   GeneID; 108958; -.
DR   KEGG; mmu:108958; -.
DR   UCSC; uc008jcg.1; mouse.
DR   CTD; 108958; -.
DR   MGI; MGI:1922035; Fam73b.
DR   GeneTree; ENSGT00390000008565; -.
DR   HOGENOM; HBG507162; -.
DR   HOVERGEN; HBG106606; -.
DR   InParanoid; Q8BK03; -.
DR   OMA; ALATACW; -.
DR   OrthoDB; EOG4320Z1; -.
DR   PhylomeDB; Q8BK03; -.
DR   NextBio; 361520; -.
DR   ArrayExpress; Q8BK03; -.
DR   Bgee; Q8BK03; -.
DR   CleanEx; MM_5730472N09RIK; -.
DR   Genevestigator; Q8BK03; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR019392; DUF2217.
DR   Pfam; PF10265; DUF2217; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    593       Protein FAM73B.
FT                                /FTId=PRO_0000313659.
FT   TRANSMEM     11     31       Helical; (Potential).
FT   TRANSMEM     42     62       Helical; (Potential).
FT   COMPBIAS     67     70       Poly-Arg.
FT   COMPBIAS    105    156       Ser-rich.
FT   MOD_RES     137    137       Phosphoserine.
FT   MOD_RES     208    208       Phosphothreonine.
FT   MOD_RES     220    220       Phosphoserine (By similarity).
FT   MOD_RES     224    224       Phosphoserine.
FT   MOD_RES     228    228       Phosphoserine.
FT   MOD_RES     273    273       Phosphothreonine.
FT   MOD_RES     276    276       Phosphoserine.
FT   MOD_RES     286    286       Phosphoserine (By similarity).
FT   MOD_RES     288    288       Phosphothreonine (By similarity).
FT   MOD_RES     289    289       Phosphoserine (By similarity).
FT   MOD_RES     295    295       Phosphoserine (By similarity).
FT   MOD_RES     297    297       Phosphothreonine (By similarity).
FT   VAR_SEQ     391    443       SPKGFLESYEEMLSYALRPETWATTRLELEGRGVACMSFFD
FT                                IVLDFILMDAFE -> VAGVGLLQIPLRTLPQAGLLLCFVL
FT                                FCRLLTGFLTQKSWACEVTQWVQDWQPE (in isoform
FT                                2).
FT                                /FTId=VSP_030093.
FT   VAR_SEQ     444    593       Missing (in isoform 2).
FT                                /FTId=VSP_030094.
SQ   SEQUENCE   593 AA;  65548 MW;  24992DA0CB628794 CRC64;
     MAFRRTEGMS MIQALAMTVA EIPVFLYTTF GQSAFSQLRL TPGLRKVLFA TALGTVALAL
     AAHQLKRRRR KKKQVGPEMG GEQLGTVPMP ILMARKVPSV KKGCSSRRVQ SPSSKSNDTL
     SGISSIEPSK HSGSSHSLAS MVVVNSSSPT AACSGSWEAR GMEESVPTTD GSAESLYVQG
     MELFEEALQK WEQALSVGQR GDGGSTPTPG DSLQNPDTAS EALSEPESQR REFAEKLESL
     LHRAYHLQEE FGSTFPSDSM LLDLERTLML PLTEGSLRLR ADDEDSLTSE DSFFSATEIF
     ESLQIGEYPL PLSRPAAAYE EALQLVKEGR VPCRTLRTEL LGCYSDQDFL AKLHCVRQAF
     EGLLEERSNQ IFFGEVGRQM VTGLMTKAEK SPKGFLESYE EMLSYALRPE TWATTRLELE
     GRGVACMSFF DIVLDFILMD AFEDLENPPS SVLAVLRNRW LSDSFKETAL ATACWSVLKA
     KRRLLMVPDG FISHFYSVSE HVSPVLAFGF LGPKPQLSEV CAFFKHQIVQ YLRDMFDLDN
     VRYTSVPALA EDILQLSRRR SEILLGYLGA PVASSIGLNG PLPRENGPLE ELQ
//
ID   NDUV3_MOUSE             Reviewed;         104 AA.
AC   Q8BK30;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   30-NOV-2010, entry version 49.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial;
DE   AltName: Full=Complex I-9kD;
DE            Short=CI-9kD;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 9 kDa subunit;
DE   Flags: Precursor;
GN   Name=Ndufv3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Accessory subunit of the mitochondrial membrane
CC       respiratory chain NADH dehydrogenase (Complex I), that is believed
CC       not to be involved in catalysis. Complex I functions in the
CC       transfer of electrons from NADH to the respiratory chain. The
CC       immediate electron acceptor for the enzyme is believed to be
CC       ubiquinone (By similarity).
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits. This is a
CC       component of the flavoprotein-sulfur (FP) fragment of the enzyme
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein; Matrix side (By similarity).
CC   -!- SIMILARITY: Belongs to the complex I NDUFV3 subunit family.
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DR   EMBL; AK077433; BAC36798.1; -; mRNA.
DR   IPI; IPI00403381; -.
DR   RefSeq; NP_001077360.1; NM_001083891.1.
DR   UniGene; Mm.28349; -.
DR   STRING; Q8BK30; -.
DR   PhosphoSite; Q8BK30; -.
DR   PRIDE; Q8BK30; -.
DR   Ensembl; ENSMUST00000064798; ENSMUSP00000066303; ENSMUSG00000024038.
DR   GeneID; 78330; -.
DR   KEGG; mmu:78330; -.
DR   UCSC; uc008bvf.1; mouse.
DR   CTD; 78330; -.
DR   MGI; MGI:1890894; Ndufv3.
DR   HOVERGEN; HBG082013; -.
DR   NextBio; 348711; -.
DR   ArrayExpress; Q8BK30; -.
DR   Bgee; Q8BK30; -.
DR   CleanEx; MM_1500032D16RIK; -.
DR   Genevestigator; Q8BK30; -.
DR   GermOnline; ENSMUSG00000024038; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Electron transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Respiratory chain; Transit peptide;
KW   Transport.
FT   TRANSIT       1     35       Mitochondrion (By similarity).
FT   CHAIN        36    104       NADH dehydrogenase [ubiquinone]
FT                                flavoprotein 3, mitochondrial.
FT                                /FTId=PRO_0000251883.
SQ   SEQUENCE   104 AA;  11813 MW;  0674772FC8C17CA6 CRC64;
     MAVSLLLRGG RIRALKAVLL EARVFPGELV SVVRLSTESE KSAKEKELHP KTQSVLKEPE
     PTDTTTYKNL QHHDYNTYTF LDLNLDLSKF RLPQPSSGRE SPRH
//
ID   SRRM4_MOUSE             Reviewed;         608 AA.
AC   Q8BKA3; Q8R1S5; Q9CW37;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Serine/arginine repetitive matrix protein 4;
DE   AltName: Full=Neural-specific serine/arginine repetitive splicing factor of 100 kDa;
DE            Short=Neural-specific SR-related protein of 100 kDa;
DE            Short=nSR100;
GN   Name=Srrm4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, RNA-BINDING, AND
RP   PHOSPHORYLATION.
RX   PubMed=19737518; DOI=10.1016/j.cell.2009.06.012;
RA   Calarco J.A., Superina S., O'Hanlon D., Gabut M., Raj B., Pan Q.,
RA   Skalska U., Clarke L., Gelinas D., van der Kooy D., Zhen M.,
RA   Ciruna B., Blencowe B.J.;
RT   "Regulation of vertebrate nervous system alternative splicing and
RT   development by an SR-related protein.";
RL   Cell 138:898-910(2009).
CC   -!- FUNCTION: Splicing factor specifically required for neural cell
CC       differentiation. Acts in conjuction with nPTB/PTBP2 by binding
CC       directly to its regulated target transcripts and promotes neural-
CC       specific exon inclusion in many genes that function in neural cell
CC       differentiation. Required to promote the inclusion of neural-
CC       specific exon 10 in nPTB/PTBP2, leading to increased expression of
CC       neural-specific nPTB/PTBP2. Also promotes the inclusion of exon 16
CC       in DAAM1 in neuron extracts.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BKA3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BKA3-2; Sequence=VSP_029639;
CC   -!- TISSUE SPECIFICITY: Specifically expressed in neuronal cells (at
CC       protein level). Expressed in adult nervous system and sensory
CC       organ tissues.
CC   -!- PTM: Phosphorylated.
CC   -!- SIMILARITY: Belongs to the nSR100 family.
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DR   EMBL; AK005085; BAB23809.1; -; mRNA.
DR   EMBL; AK053836; BAC35548.1; -; mRNA.
DR   EMBL; BC024130; AAH24130.1; -; mRNA.
DR   EMBL; BC056392; AAH56392.1; -; mRNA.
DR   IPI; IPI00222561; -.
DR   IPI; IPI00877199; -.
DR   RefSeq; NP_081162.1; NM_026886.3.
DR   UniGene; Mm.146779; -.
DR   ProteinModelPortal; Q8BKA3; -.
DR   PhosphoSite; Q8BKA3; -.
DR   PRIDE; Q8BKA3; -.
DR   Ensembl; ENSMUST00000076124; ENSMUSP00000075488; ENSMUSG00000063919.
DR   GeneID; 68955; -.
DR   KEGG; mmu:68955; -.
DR   UCSC; uc008zfc.1; mouse.
DR   CTD; 68955; -.
DR   MGI; MGI:1916205; Srrm4.
DR   GeneTree; ENSGT00580000081375; -.
DR   HOGENOM; HBG126483; -.
DR   InParanoid; Q8BKA3; -.
DR   OMA; HRHHRCP; -.
DR   OrthoDB; EOG4R5032; -.
DR   NextBio; 328283; -.
DR   ArrayExpress; Q8BKA3; -.
DR   Bgee; Q8BKA3; -.
DR   CleanEx; MM_1500001A10RIK; -.
DR   Genevestigator; Q8BKA3; -.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IMP:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IDA:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
DR   GO; GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Alternative splicing; Differentiation; mRNA processing; mRNA splicing;
KW   Nucleus; Phosphoprotein; RNA-binding.
FT   CHAIN         1    608       Serine/arginine repetitive matrix protein
FT                                4.
FT                                /FTId=PRO_0000311912.
FT   COMPBIAS    109    171       Lys-rich.
FT   COMPBIAS    123    605       Ser-rich.
FT   COMPBIAS    404    593       Arg-rich.
FT   VAR_SEQ       1    488       Missing (in isoform 2).
FT                                /FTId=VSP_029639.
SQ   SEQUENCE   608 AA;  67860 MW;  16DBEF71B68C301C CRC64;
     MASLQQGEKQ LFEKFWKGTF KAVATPRPES IIVASITARK PMPRTEPQSS LLLPDQDGPS
     EKLGQHLAPE ALGTNSWGRE KACRELDPAR AHSASQDRDP TPPPSSRGKK KKKKSTRKKR
     RRSPSYSPSP VKKKKKKSSK KHKRHRSFSK KRRHSSCSPK SKRREEKRHK KQSRSRKSHR
     HRHHRCPSRS QSSELRSPSC ESRHRGRSPE EGRKSRRTHS RRCSKNHCKV SPDARSSHLP
     SQPLPRLGFL SARGVITGSG SAADLFSKSA SPLAATRGRS QEYDSGNDTS SPPSTQTSSA
     RSRGQEKGSP GGDLSKSRDL NCGNTSDSGN SFTTSSPQNK GAVLETVSPA CRSRESRGFQ
     SPCLQCAEVK KSSLVPSTAR SSPIKECSRS SSYTSTRSSS PSSRSPNPRA SPRYTRSRST
     SSEKRSYSRS PSYSSKSGKR SPPSRSSRSR RSPSYSRYSP SRERDLKYGE KEPQPRERAR
     RRRRSYSPMR KRRRDSPSHL EARRITSARK RPIPYYRPSP SSSSSLSSAS SWYSSSSSSS
     SSSSRSPSRS YSRSRSPSRS HSSRSQTRSR TRTSRSSSSR SLSLGSRSRS RNRSLSYSSA
     ESYASTRR
//
ID   IPO5_MOUSE              Reviewed;        1097 AA.
AC   Q8BKC5; Q3TEG2; Q7TQC6; Q9EQ30;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Importin-5;
DE            Short=Imp5;
DE   AltName: Full=Importin subunit beta-3;
DE   AltName: Full=Karyopherin beta-3;
DE   AltName: Full=Ran-binding protein 5;
DE            Short=RanBP5;
GN   Name=Ipo5; Synonyms=Kpnb3, Ranbp5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Testis;
RA   Anway M.D., Li Y., Griswold M.D.;
RT   "Identification of testicular germ cell gene expression by
RT   differential display analysis.";
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Eye, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH HISTONES H2B; H2A; H3 AND H4.
RX   MEDLINE=21385002; PubMed=11493596; DOI=10.1093/embo-reports/kve168;
RA   Muehlhaeusser P., Mueller E.-C., Otto A., Kutay U.;
RT   "Multiple pathways contribute to nuclear import of core histones.";
RL   EMBO Rep. 2:690-696(2001).
CC   -!- FUNCTION: Functions in nuclear protein import as nuclear transport
CC       receptor. Serves as receptor for nuclear localization signals
CC       (NLS) in cargo substrates. Is thought to mediate docking of the
CC       importin/substrate complex to the nuclear pore complex (NPC)
CC       through binding to nucleoporin and the complex is subsequently
CC       translocated through the pore by an energy requiring, Ran-
CC       dependent mechanism. At the nucleoplasmic side of the NPC, Ran
CC       binds to the importin, the importin/substrate complex dissociates
CC       and importin is re-exported from the nucleus to the cytoplasm
CC       where GTP hydrolysis releases Ran. The directionality of nuclear
CC       import is thought to be conferred by an asymmetric distribution of
CC       the GTP- and GDP-bound forms of Ran between the cytoplasm and
CC       nucleus (By similarity). Mediates the nuclear import of ribosomal
CC       proteins RPL23A, RPS7 and RPL5. Binds to a beta-like import
CC       receptor binding (BIB) domain of RPL23A (By similarity). In vitro,
CC       mediates nuclear import of H2A, H2B, H3 and H4 histones.
CC   -!- SUBUNIT: Interacts with H2A, H2B, H3 and H4 histones. Binds
CC       RPL23A, RPS7 and RPL5 (By similarity).
CC   -!- INTERACTION:
CC       P70315:Was; NbExp=3; IntAct=EBI-643605, EBI-644195;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BKC5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BKC5-2; Sequence=VSP_009658;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the importin beta family.
CC   -!- SIMILARITY: Contains 6 HEAT repeats.
CC   -!- SIMILARITY: Contains 1 importin N-terminal domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG45965.2; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF294327; AAG45965.2; ALT_INIT; mRNA.
DR   EMBL; AK053681; BAC35471.1; -; mRNA.
DR   EMBL; AK169664; BAE41286.1; -; mRNA.
DR   EMBL; BC052392; AAH52392.1; -; mRNA.
DR   EMBL; BC054814; AAH54814.1; -; mRNA.
DR   IPI; IPI00409936; -.
DR   IPI; IPI00626994; -.
DR   RefSeq; NP_076068.1; NM_023579.4.
DR   UniGene; Mm.221452; -.
DR   UniGene; Mm.472208; -.
DR   ProteinModelPortal; Q8BKC5; -.
DR   SMR; Q8BKC5; 370-476.
DR   IntAct; Q8BKC5; 9.
DR   STRING; Q8BKC5; -.
DR   PhosphoSite; Q8BKC5; -.
DR   PRIDE; Q8BKC5; -.
DR   Ensembl; ENSMUST00000032898; ENSMUSP00000032898; ENSMUSG00000030662.
DR   GeneID; 70572; -.
DR   KEGG; mmu:70572; -.
DR   UCSC; uc007uzz.1; mouse.
DR   CTD; 70572; -.
DR   MGI; MGI:1917822; Ipo5.
DR   HOGENOM; HBG378569; -.
DR   HOVERGEN; HBG006156; -.
DR   InParanoid; Q8BKC5; -.
DR   OMA; GKLEEHF; -.
DR   OrthoDB; EOG4XGZZ8; -.
DR   PhylomeDB; Q8BKC5; -.
DR   NextBio; 331892; -.
DR   ArrayExpress; Q8BKC5; -.
DR   Bgee; Q8BKC5; -.
DR   Genevestigator; Q8BKC5; -.
DR   GermOnline; ENSMUSG00000030662; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000357; HEAT.
DR   InterPro; IPR001494; Importin-beta_N.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 3.
DR   Pfam; PF02985; HEAT; 2.
DR   SUPFAM; SSF48371; ARM-type_fold; 2.
DR   PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
DR   PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW   Protein transport; Repeat; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1097       Importin-5.
FT                                /FTId=PRO_0000120772.
FT   DOMAIN       28     99       Importin N-terminal.
FT   REPEAT      212    249       HEAT 1.
FT   REPEAT      395    432       HEAT 2.
FT   REPEAT      437    475       HEAT 3.
FT   REPEAT      859    897       HEAT 4.
FT   REPEAT      901    938       HEAT 5.
FT   REPEAT      942    979       HEAT 6.
FT   REGION      325    375       Ran-GTP binding (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     304    304       Phosphothreonine (By similarity).
FT   MOD_RES     652    652       Phosphoserine (By similarity).
FT   MOD_RES     827    827       Phosphoserine (By similarity).
FT   VAR_SEQ       1     60       Missing (in isoform 2).
FT                                /FTId=VSP_009658.
FT   CONFLICT      2      2       A -> TA (in Ref. 1).
FT   CONFLICT    397    397       L -> V (in Ref. 1; AAG45965).
FT   CONFLICT    800    801       KL -> NV (in Ref. 1; AAG45965).
FT   CONFLICT    853    853       Y -> H (in Ref. 3; AAH54814).
SQ   SEQUENCE   1097 AA;  123591 MW;  B3197CFC72F3377D CRC64;
     MAAAAAEQQQ FYLLLGNLLS PDNVVRKQAE ETYENIPGRS KITFLLQAIR NTTAAEEARQ
     MAAVLLRRLL SSAFDEVYPA LPSDVQTAIK SELLMIIQME TQSSMRKKIC DIAAELARNL
     IDEDGNNQWP EGLKFLFDSV SSQNMGLREA ALHIFWNFPG IFGNQQQHYL DVIKRMLVQC
     MQDQEHPSIR TLSARATAAF ILANEHNVAL FKHFADLLPG FLQAVNDSCY QNDDSVLKSL
     VEIADTVPKY LRPHLEATLQ LSLKLCGDTN LNNMQRQLAL EVIVTLSETA AAMLRKHTSL
     IAQTIPQMLA MMVDLEEDED WANADELEDD DFDSNAVAGE SALDRMACGL GGKLVLPMIK
     EHIMQMLQNP DWKYRHAGLM ALSAIGEGCH QQMEGILNEI VNFVLLFLQD PHPRVRYAAC
     NAVGQMATDF APGFQKKFHE KVIAALLQTM EDQGNQRVQA HAAAALINFT EDCPKSLLIP
     YLDNLVKHLH SIMVLKLQEL IQKGTKLVLE QVVTSIASVA DTAEEKFVPY YDLFMPSLKH
     IVENAVQKEL RLLRGKTIEC ISLIGLAVGK EKFMQDASDV MQLLLKTQTD FNDMEDDDPQ
     ISYMISAWAR MCKILGKEFQ QYLPVVMGPL MKTASIKPEV ALLDTQDMEN MSDDDGWEFV
     NLGDQQSFGI KTAGLEEKST ACQMLVCYAK ELKEGFVEYT EQVVKLMVPL LKFYFHDGVR
     VAAAESMPLL LECARVRGPE YLTQMWHFMC DALIKAIGTE PDSDVLSEIM HSFAKCIEVM
     GDGCLNNEHF EELGGILKAK LEEHFKNQEL RQVKRQDEDY DEQVEESLQD EDDNDVYILT
     KVSDILHSIF SSYKEKVLPW FEQLLPLIVN LICPQRPWPD RQWGLCIFDD IVEHCSPASF
     KYAEYFISPM LQYVCDNSPE VRQAAAYGLG VMAQFGGDNY RPFCTDALPL LVRVIQAPEA
     KTKENVNATE NCISAVGKIM KFKPDCVNVE EVLPHWLSWL PLHEDKEEAV QTFSYLCDLI
     ESNHPIVLGP NNTNLPKIFS IIAEGEMHEA IKHEDPCAKR LANVVRQVQT SGGLWTECIA
     QLSPEQQAAI QELLNSA
//
ID   SIN1_MOUSE              Reviewed;         522 AA.
AC   Q8BKH7; A2AN72; A2AN74; A2AR13; A2AR16; Q80UY4; Q8BMV5; Q8R2N9;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 67.
DE   RecName: Full=Target of rapamycin complex 2 subunit MAPKAP1;
DE            Short=TORC2 subunit MAPKAP1;
DE   AltName: Full=Mitogen-activated protein kinase 2-associated protein 1;
DE   AltName: Full=Stress-activated map kinase-interacting protein 1;
DE            Short=SAPK-interacting protein 1;
GN   Name=Mapkap1; Synonyms=Mip1, Sin1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Eye, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, and FVB/N;
RC   TISSUE=Brain, Mammary tumor, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16962653; DOI=10.1016/j.cell.2006.08.033;
RA   Jacinto E., Facchinetti V., Liu D., Soto N., Wei S., Jung S.Y.,
RA   Huang Q., Qin J., Su B.;
RT   "SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt
RT   phosphorylation and substrate specificity.";
RL   Cell 127:125-137(2006).
RN   [5]
RP   TISUE SPECIFICITY.
RX   PubMed=17054722; DOI=10.1111/j.1365-2443.2006.01016.x;
RA   Makino C., Sano Y., Shinagawa T., Millar J.B., Ishii S.;
RT   "Sin1 binds to both ATF-2 and p38 and enhances ATF-2-dependent
RT   transcription in an SAPK signaling pathway.";
RL   Genes Cells 11:1239-1251(2006).
CC   -!- FUNCTION: Subunit of mTORC2, which regulates cell growth and
CC       survival in response to hormonal signals. mTORC2 is activated by
CC       growth factors, but, in contrast to mTORC1, seems to be nutrient-
CC       insensitive. mTORC2 seems to function upstream of Rho GTPases to
CC       regulate the actin cytoskeleton, probably by activating one or
CC       more Rho-type guanine nucleotide exchange factors. mTORC2 promotes
CC       the serum-induced formation of stress-fibers or F-actin. mTORC2
CC       plays a critical role in AKT1 'Ser-473' phosphorylation, which may
CC       facilitate the phosphorylation of the activation loop of AKT1 on
CC       'Thr-308' by PDK1 which is a prerequisite for full activation.
CC       mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2
CC       also modulates the phosphorylation of PRKCA on 'Ser-657'. Within
CC       mTORC2, MAPKAP1 is required for complex formation and mTORC2
CC       kinase activity. MAPKAP1 inhibits MAP3K2 by preventing its
CC       dimerization and autophosphorylation. Inhibits HRAS and KRAS
CC       signaling. Enhances osmotic stress-induced phosphorylation of ATF2
CC       and ATF2-mediated transcription.
CC   -!- SUBUNIT: Component of the mammalian target of rapamycin complex 2
CC       (mTORC2) which contains MTOR, LST8, PRR5, RICTOR and MAPKAP1.
CC       Contrary to mTORC1, mTORC2 does not bind to and is not sensitive
CC       to FKBP12-rapamycin. Interacts with ATF2, MAP3K2 and MAPK8 (By
CC       similarity). Interacts with GTP-bound HRAS and KRAS (By
CC       similarity). Interacts with IFNAR2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       (By similarity). Cytoplasmic vesicle (By similarity). Nucleus (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BKH7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BKH7-2; Sequence=VSP_033209;
CC       Name=3;
CC         IsoId=Q8BKH7-3; Sequence=VSP_033208;
CC   -!- TISSUE SPECIFICITY: Uniquitously expresseed, with highest levels
CC       in testis, kidney and liver. Present in renal tubule cells (at
CC       protein level).
CC   -!- DISRUPTION PHENOTYPE: Death during early embryonic stages.
CC   -!- SIMILARITY: Belongs to the SIN1 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK027932; BAC25671.1; -; mRNA.
DR   EMBL; AK052045; BAC34838.1; -; mRNA.
DR   EMBL; AK132263; BAE21066.1; -; mRNA.
DR   EMBL; AL845262; CAM15450.1; -; Genomic_DNA.
DR   EMBL; AL808102; CAM15450.1; JOINED; Genomic_DNA.
DR   EMBL; AL845262; CAM15451.1; -; Genomic_DNA.
DR   EMBL; AL808102; CAM15451.1; JOINED; Genomic_DNA.
DR   EMBL; AL845262; CAM15454.1; -; Genomic_DNA.
DR   EMBL; AL808102; CAM15454.1; JOINED; Genomic_DNA.
DR   EMBL; AL808102; CAM17090.1; -; Genomic_DNA.
DR   EMBL; AL845262; CAM17090.1; JOINED; Genomic_DNA.
DR   EMBL; AL808102; CAM17091.1; -; Genomic_DNA.
DR   EMBL; AL845262; CAM17091.1; JOINED; Genomic_DNA.
DR   EMBL; AL808102; CAM17094.1; -; Genomic_DNA.
DR   EMBL; AL845262; CAM17094.1; JOINED; Genomic_DNA.
DR   EMBL; BC027377; AAH27377.1; -; mRNA.
DR   EMBL; BC031579; AAH31579.1; -; mRNA.
DR   EMBL; BC043296; AAH43296.1; -; mRNA.
DR   EMBL; BC090644; AAH90644.1; -; mRNA.
DR   EMBL; BC096618; AAH96618.1; -; mRNA.
DR   IPI; IPI00222598; -.
DR   IPI; IPI00753635; -.
DR   IPI; IPI00757217; -.
DR   RefSeq; NP_796319.1; NM_177345.3.
DR   UniGene; Mm.270866; -.
DR   ProteinModelPortal; Q8BKH7; -.
DR   STRING; Q8BKH7; -.
DR   PhosphoSite; Q8BKH7; -.
DR   PRIDE; Q8BKH7; -.
DR   Ensembl; ENSMUST00000040459; ENSMUSP00000035451; ENSMUSG00000038696.
DR   Ensembl; ENSMUST00000113126; ENSMUSP00000108751; ENSMUSG00000038696.
DR   Ensembl; ENSMUST00000113129; ENSMUSP00000108754; ENSMUSG00000038696.
DR   GeneID; 227743; -.
DR   KEGG; mmu:227743; -.
DR   UCSC; uc008jil.1; mouse.
DR   CTD; 227743; -.
DR   MGI; MGI:2444554; Mapkap1.
DR   eggNOG; roNOG06561; -.
DR   GeneTree; ENSGT00390000000642; -.
DR   HOVERGEN; HBG023148; -.
DR   InParanoid; Q8BKH7; -.
DR   OMA; STLEFCL; -.
DR   NextBio; 378816; -.
DR   ArrayExpress; Q8BKH7; -.
DR   Bgee; Q8BKH7; -.
DR   Genevestigator; Q8BKH7; -.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   InterPro; IPR008828; SIN1.
DR   PANTHER; PTHR13335; SIN1; 1.
DR   Pfam; PF05422; SIN1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell membrane; Cytoplasmic vesicle;
KW   Membrane; Nucleus; Phosphoprotein; Stress response.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    522       Target of rapamycin complex 2 subunit
FT                                MAPKAP1.
FT                                /FTId=PRO_0000328033.
FT   REGION        2    184       Interaction with MAP3K2 (By similarity).
FT   REGION      468    522       Interaction with ATF2 (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     270    270       Phosphoserine (By similarity).
FT   MOD_RES     510    510       Phosphoserine (By similarity).
FT   VAR_SEQ       1    192       Missing (in isoform 3).
FT                                /FTId=VSP_033208.
FT   VAR_SEQ     321    356       Missing (in isoform 2).
FT                                /FTId=VSP_033209.
FT   CONFLICT    516    516       E -> K (in Ref. 3; AAH43296).
SQ   SEQUENCE   522 AA;  59009 MW;  994C669D04065926 CRC64;
     MAFLDNPTII LAHIRQSHVT SDDTGMCEMV LIDHDVDLEK THPPSVPGDS GSEVQGSSGE
     TQGYIYAQSV DITSSWDFGI RRRSNTAQRL ERLRKERQNQ IKCKNIQWKE RNSKQSAQEL
     KSLFEKKSLK EKPPSSGKQS ILSVRLEQCP LQLNNPFNEY SKFDGKGHVG TTATKKIDVY
     LPLHSSQDRL LPMTVVTMAS ARVQDLIGLI CWQYTSEGRE PKLNDNVSAY CLHIAEDDGE
     VDTDFPPLDS NEPIHKFGFS TLALVEKYSS PGLTSKESLF VRINAAHGFS LIQVDNTKVT
     MKEILLKAVK RRKGSQKISG PQYRLEKQSE PNIAVDLEST LESQNAWEFC LVRENSSRAD
     GVFEEDSQID IATVQDMLSS HHYKSFKVSM IHRLRFTTDV QLGISGDKVE IDPVTNQKAS
     TKFWIKQKPI SIDCDLLCAC DLAEEKSPSH AVFKLTYLSS HDYKHLYFES DAATVSEIVL
     KVNYILESRA STARADYLAQ KQRKLNRRTS FSFQKEKKSG QQ
//
ID   TNR6B_MOUSE             Reviewed;        1810 AA.
AC   Q8BKI2; Q80TK4;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Trinucleotide repeat-containing gene 6B protein;
GN   Name=Tnrc6b; Synonyms=Kiaa1093;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1240-1810 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
CC   -!- FUNCTION: Plays a role in RNA-mediated gene silencing by both
CC       micro-RNAs (miRNAs) and short interfering RNAs (siRNAs). Required
CC       for miRNA-dependent translational repression and siRNA-dependent
CC       endonucleolytic cleavage of complementary mRNAs by argonaute
CC       family proteins (By similarity).
CC   -!- SUBUNIT: Interacts with EIF2C1/AGO1, EIF2C2/AGO2, EIF2C3/AGO3 and
CC       EIF2C4/AGO4 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body (By similarity).
CC       Note=Mammalian P-bodies are also known as GW bodies (GWBs) (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BKI2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BKI2-2; Sequence=VSP_037294, VSP_037295, VSP_037296,
CC                                  VSP_037297;
CC   -!- SIMILARITY: Belongs to the GW182 family.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR   EMBL; AC125540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC126682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK051922; BAC34813.1; -; mRNA.
DR   EMBL; AK122440; BAC65722.1; -; mRNA.
DR   IPI; IPI00226311; -.
DR   IPI; IPI00454102; -.
DR   RefSeq; NP_659061.2; NM_144812.2.
DR   UniGene; Mm.131328; -.
DR   UniGene; Mm.412092; -.
DR   ProteinModelPortal; Q8BKI2; -.
DR   SMR; Q8BKI2; 1085-1148, 1624-1695.
DR   DIP; DIP-48568N; -.
DR   STRING; Q8BKI2; -.
DR   PhosphoSite; Q8BKI2; -.
DR   PRIDE; Q8BKI2; -.
DR   Ensembl; ENSMUST00000060230; ENSMUSP00000056901; ENSMUSG00000047888.
DR   Ensembl; ENSMUST00000067689; ENSMUSP00000064336; ENSMUSG00000047888.
DR   GeneID; 213988; -.
DR   KEGG; mmu:213988; -.
DR   UCSC; uc007wvu.1; mouse.
DR   CTD; 213988; -.
DR   MGI; MGI:2443730; Tnrc6b.
DR   HOGENOM; HBG446435; -.
DR   InParanoid; Q8BKI2; -.
DR   OMA; TWGPGAS; -.
DR   OrthoDB; EOG4G4GQJ; -.
DR   ArrayExpress; Q8BKI2; -.
DR   Bgee; Q8BKI2; -.
DR   Genevestigator; Q8BKI2; -.
DR   GO; GO:0000932; C:cytoplasmic mRNA processing body; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   InterPro; IPR019486; Argonaute_hook_dom.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR009060; UBA-like.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   Pfam; PF10427; Ago_hook; 2.
DR   SUPFAM; SSF46934; UBA_like; 1.
DR   PROSITE; PS50102; RRM; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Phosphoprotein;
KW   RNA-binding; RNA-mediated gene silencing; Translation regulation.
FT   CHAIN         1   1810       Trinucleotide repeat-containing gene 6B
FT                                protein.
FT                                /FTId=PRO_0000373981.
FT   DOMAIN     1625   1697       RRM.
FT   COILED       33     75       Potential.
FT   MOD_RES     443    443       Phosphoserine (By similarity).
FT   MOD_RES     444    444       Phosphothreonine (By similarity).
FT   MOD_RES    1409   1409       Phosphoserine (By similarity).
FT   MOD_RES    1793   1793       Phosphoserine (By similarity).
FT   VAR_SEQ       1     36       Missing (in isoform 2).
FT                                /FTId=VSP_037294.
FT   VAR_SEQ      37     38       KQ -> MR (in isoform 2).
FT                                /FTId=VSP_037295.
FT   VAR_SEQ     970    979       VWSKSTPPAP -> GRYQLFSHRS (in isoform 2).
FT                                /FTId=VSP_037296.
FT   VAR_SEQ     980   1810       Missing (in isoform 2).
FT                                /FTId=VSP_037297.
FT   CONFLICT    904    904       D -> Y (in Ref. 2; BAC34813).
FT   CONFLICT   1576   1576       T -> P (in Ref. 3; BAC65722).
SQ   SEQUENCE   1810 AA;  191963 MW;  70F0A3A88CE7C7C5 CRC64;
     MQTNEGEVEE ESSSQVEQED FVMEGHGKTP PPGEESKQEK EQEREEQLME DKKRKKEDKK
     KKEATQKVTE QKTKVPEVTK PSLSQPTAAS PIGSSPSPPV NGGNNAKRVA VPNGQPPSAA
     RYMPREVPPR FRCQQDHKVL LKRGQPPPPS CMLLGGGAGP PPCTAPGANP NNNAQVTGAL
     LQSESGTAPE STLGGAAASN YANSTWGPGA SSNSGASPNP IHIWDKVIVD GSDMEEWPCI
     ASKDTESSSE NTTDNNSASN PGSEKSSLPG STTSNKGKGS QCQAASSGNE CNLGVWKSDP
     KAKSVQPPNS TSDSNNGLGN WRSTSGQDRI GPGSGFSNFN PNSNPSAWPA LVQEGTSRKG
     ALETESSSSS AQVSTVGQAS REQQSKMENA GVNFVVSGRE QAQIHNTDGP KNGNTNSLNL
     SSPNPMENKG MPFGMGLGNT SRSTDAPSQS TGDRKTGSVG SWGAARGPSG TDTVSGQSNS
     GNNGNNGKDR EDSWKGASVP KPTGSKSDSW DNNNRSTGGS WNFGPQDNND NKWGEGNKMT
     SGVSQGEWKQ PTGSDELKIG EWSGPNQPNS STGAWDNQKG HPLPENQGNA QAPCWGRSSS
     SAGSEVGGQS TGSNHKAGSS DSHNSGRRSY RPTHPDCQAV LQTLLSRTDL DPRVLSNTGW
     GQTQIKQDTV WDIEEVPRPE GKSDKGTEGW ESAATQTKNS GGWGDAPSQS NQMKSGWGEL
     SASTEWKDPK STGGWNDYKN NNSSNWGGGR ADEKTPSSWN ESSCKDQGWG GGRQPNQGWT
     SGKNGWGEEV DQVKNNNWES SANKPVSGWG EGGQNEIGTW GNGGNTNLAS KGGWEDCKRS
     PAWNETGRQP NSWNKQHQQQ QQPPPPQPEA SGSWGGPPPP PQGNVRPSNS NWSSGPQPTT
     PKDDEPSGWE EPSPQSISRK MDIDDGTSAW GDPNSYNYKN VNLWDKNSQG GPAPREPNLP
     TPMTGKSASV WSKSTPPAPD NGTSAWGEPN ESSPGWGEMD DAGASTTGWG NTPANAPNAM
     KPNSKSMQDG WGESDGPVTG ARHPSWEEED DGGVWNTAGS QGSTSSHNSA SWGQGGKKQM
     KCSLKGGNND SWMNPLAKQF SNMGLLSQTE DNPSSKMDLS VDKKFDVDKR TMNLGDFNDI
     MRKDRPGFRP PNSKDLGTTD SGPYFEKGGS HGLFGNSTAQ SRGLHTPVQP LSSSPGLRAQ
     VPPQFISPQV SASMLKQFPN SGLNPGLFNV GPQLSPQQIA MLSQLPQIPQ FQLACQLLLQ
     QQQQQQQLLQ NQRKISQAVR QQQEQQLARM VSALQQQQQQ QQQQQRQPSM KHSPSHPVGP
     KPHLDNMVPN ALNVGLPDLP TKGPIPGYGS GFSSGGMDYG MVGGKEAGTE SRFKQWTSMM
     EGLPSVATQE ATMHKNGAIV APGKTRGGSP YNQFDIIPGD TLGGHTGPAG DSWLPAKSPP
     TNKIGSKSSN ASWPPEFQPG VPWKGIQNID PESDPYVTPG SVLGGTTTSP IVDTDHQLLR
     DNTTGSNSSL NTSLPSPGAW PYSASDNSFT NVHSTSAKFP DYKSTWSPDP IGHNPTHLSN
     KMWKNHISSR NTTPLTRPPP GLTNPKPASP WSSTAPRSVR GWGTQDSRIA SASTWSDGGS
     VRPSYWLVLH NLTPQIDGST LRTICMQHGP LLTFHLNLTQ GTALIRYSTK QEAAKAQTAL
     HMCVLGNTTI LAEFATEDEV SRFLAQAQPP TPAATPSAPA TGWQSLETSQ NQADPVGPAL
     NLFGGSTGLG QWSSSAGGSS GADLAGTSLW GPPNYSSSLW GVPTVEDPHR MGSPAPLLPG
     DLLGGGSDSI
//
ID   Q8BKL2_MOUSE            Unreviewed;       406 AA.
AC   Q8BKL2;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   30-NOV-2010, entry version 43.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Arfgef1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK051592; BAC34685.1; -; mRNA.
DR   IPI; IPI00626782; -.
DR   UniGene; Mm.229141; -.
DR   STRING; Q8BKL2; -.
DR   PhosphoSite; Q8BKL2; -.
DR   Ensembl; ENSMUST00000088615; ENSMUSP00000085986; ENSMUSG00000067851.
DR   MGI; MGI:2442988; Arfgef1.
DR   eggNOG; roNOG12988; -.
DR   HOGENOM; HBG355338; -.
DR   HOVERGEN; HBG087060; -.
DR   InParanoid; Q8BKL2; -.
DR   ArrayExpress; Q8BKL2; -.
DR   Bgee; Q8BKL2; -.
DR   Genevestigator; Q8BKL2; -.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   406 AA;  46457 MW;  220400025D43F10C CRC64;
     QTEKAEWMTT TCNHALYAIC DVFTQYLEVL SDVLLDDIFA QLYWCVQQDN EQLARSGTNC
     LENVVILNGE KFTLEIWDKT CNCTLDIFKT TIPHALLTWR PTSGEAEPPS PSAVSEKPLD
     AISQKSVDIH DSIQPRSSDN RQQAPLVSVS TVSEEVSKVK STAKFPEQKL FAALLIKCVV
     QLELIQTIDN IVFFPATSKK EDAENLAAAQ RDAVDFDVRV DTQDQGMYRF LTSQQLFKLL
     DCLLESHRFA KAFNSNNEQR TALWKAGFKG KSKPNLLKQE TSSLACGLRI LFRMYMDESR
     VSAWEEVQQR LLNVCREALS YFLTLTSESH REAWTNLLLL FLTKVLKISD SRFKAHASFY
     YPLLCEIMQF DLIPELRAVL RRFFLRIGIV FQISQPPEQE LGINRQ
//
ID   TM87B_MOUSE             Reviewed;         555 AA.
AC   Q8BKU8; A2AN76; Q3T9D2; Q8K0G0; Q9D001;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Transmembrane protein 87B;
DE   Flags: Precursor;
GN   Name=Tmem87b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-555 (ISOFORM 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Liver, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-555 (ISOFORM 1).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BKU8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BKU8-2; Sequence=VSP_026220;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8BKU8-3; Sequence=VSP_026221;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the LU7TM family. TMEM87 subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB27940.1; Type=Frameshift; Positions=45;
CC       Sequence=CAM20453.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK011959; BAB27940.1; ALT_FRAME; mRNA.
DR   EMBL; AK050203; BAC34120.1; -; mRNA.
DR   EMBL; AK171811; BAE42677.1; -; mRNA.
DR   EMBL; AK172611; BAE43092.1; -; mRNA.
DR   EMBL; AL808104; CAM20452.1; -; Genomic_DNA.
DR   EMBL; AL808104; CAM20453.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BC031488; AAH31488.2; -; mRNA.
DR   IPI; IPI00660240; -.
DR   IPI; IPI00677395; -.
DR   IPI; IPI00850176; -.
DR   RefSeq; NP_082524.2; NM_028248.2.
DR   UniGene; Mm.259688; -.
DR   PhosphoSite; Q8BKU8; -.
DR   PRIDE; Q8BKU8; -.
DR   Ensembl; ENSMUST00000110325; ENSMUSP00000105954; ENSMUSG00000014353.
DR   GeneID; 72477; -.
DR   KEGG; mmu:72477; -.
DR   CTD; 72477; -.
DR   MGI; MGI:1919727; Tmem87b.
DR   eggNOG; roNOG13602; -.
DR   GeneTree; ENSGT00390000015417; -.
DR   HOGENOM; HBG387940; -.
DR   HOVERGEN; HBG068138; -.
DR   InParanoid; Q8BKU8; -.
DR   OMA; WKDILRI; -.
DR   OrthoDB; EOG466VKN; -.
DR   PhylomeDB; Q8BKU8; -.
DR   NextBio; 336308; -.
DR   ArrayExpress; Q8BKU8; -.
DR   Bgee; Q8BKU8; -.
DR   CleanEx; MM_TMEM87B; -.
DR   Genevestigator; Q8BKU8; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR009637; TM_rcpt_euk.
DR   PANTHER; PTHR21229; Lung7_TM_rcpt; 1.
DR   Pfam; PF06814; Lung_7-TM_R; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Membrane; Phosphoprotein; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     42       Potential.
FT   CHAIN        43    555       Transmembrane protein 87B.
FT                                /FTId=PRO_0000291754.
FT   TRANSMEM    217    237       Helical; (Potential).
FT   TRANSMEM    249    269       Helical; (Potential).
FT   TRANSMEM    324    344       Helical; (Potential).
FT   TRANSMEM    352    372       Helical; (Potential).
FT   TRANSMEM    395    415       Helical; (Potential).
FT   TRANSMEM    430    450       Helical; (Potential).
FT   MOD_RES     470    470       Phosphoserine (By similarity).
FT   CARBOHYD     68     68       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    160    160       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    198    198       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    275    275       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1     65       Missing (in isoform 2).
FT                                /FTId=VSP_026220.
FT   VAR_SEQ     371    373       FIS -> SFTMSFQNSWC (in isoform 3).
FT                                /FTId=VSP_026221.
FT   CONFLICT     15     15       L -> A (in Ref. 1; BAB27940).
FT   CONFLICT     92     92       H -> L (in Ref. 1; BAE42677/BAE43092).
FT   CONFLICT    223    223       V -> G (in Ref. 1; BAB27940).
FT   CONFLICT    266    266       V -> I (in Ref. 1; BAB27940).
FT   CONFLICT    291    291       I -> R (in Ref. 1; BAE42677/BAE43092).
FT   CONFLICT    376    376       Q -> E (in Ref. 1; BAB27940).
SQ   SEQUENCE   555 AA;  62898 MW;  814A2A7DD5C4DD25 CRC64;
     MAAACRSEAG LLPSLLCRRP AGAQLLRVAL CLLCWVPAAV DAVPELGLWT RTVNDKSGPL
     VFRKTMFNST EIKFSVKSFS CSGPVKFTIE WHLKYHTCHN DYPDLEEELS QRHELHADPD
     VCAYFKNIDC WTTKSENLDC SSDSQAFPSL NNKELTGIRN ISSQEGSTDV VARTQKDGFH
     IFIVSIKTEK TDAVWDLNVS LSMVGPHGYI SASDWPLMIF YMVMCIVYIL YGVLWLLWSA
     CYWKDILRIQ FWIAAVIFLG MLEKAVFYSE YQNINSTGLS TQGLLIFAEL ISAVKRTLAR
     LLVIIVSLGY GIVKPRLGTV MHRVIGLGLL YLIFAAIEGV MRVIGGSKHL AVVLTDIVLA
     VIDSIFVWFI FISLAQTMKT LRLRKNTVKF SLYRHFTNTL IFAVLASIVF MVWTTKTFRI
     AKCQSDWMEL WVDDAFWSFL FSVILIVIMF LWRPSANNQR YAFMPLIDDS DDEVEEFMVT
     SENLTEGIKL RASKTVSNGT AKPTSDNFDE DLKWVEENIP SSFTDVALPV LVDSDEEIMT
     RSEIAEKMFS SEKIM
//
ID   UBP54_MOUSE             Reviewed;        1588 AA.
AC   Q8BL06; Q149D8; Q149D9; Q6NZE1; Q8BZ28; Q9D2I9;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Inactive ubiquitin carboxyl-terminal hydrolase 54;
DE   AltName: Full=Inactive ubiquitin-specific peptidase 54;
GN   Name=Usp54;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1026-1588 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Corpus striatum, Testis, and Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 918-1588 (ISOFORM 1).
RC   STRAIN=CD-1; TISSUE=Neural stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
CC   -!- FUNCTION: Has no peptidase activity (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BL06-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BL06-2; Sequence=VSP_020488, VSP_035679, VSP_035680;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8BL06-3; Sequence=VSP_035679, VSP_035680;
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC   -!- CAUTION: Although the active site residues are conserved, lacks
CC       the conserved His residue which is normally found 9 residues
CC       before the catalytic His.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI17845.1; Type=Erroneous initiation;
CC       Sequence=AAI17846.1; Type=Erroneous initiation;
CC       Sequence=BAB31805.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK019588; BAB31805.1; ALT_INIT; mRNA.
DR   EMBL; AK036864; BAC29609.1; -; mRNA.
DR   EMBL; AK047620; BAC33102.1; -; mRNA.
DR   EMBL; AC146594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC066166; AAH66166.1; -; mRNA.
DR   EMBL; BC066175; AAH66175.1; -; mRNA.
DR   EMBL; BC117844; AAI17845.1; ALT_INIT; mRNA.
DR   EMBL; BC117845; AAI17846.1; ALT_INIT; mRNA.
DR   IPI; IPI00222648; -.
DR   IPI; IPI00757496; -.
DR   IPI; IPI00915079; -.
DR   RefSeq; NP_084456.2; NM_030180.2.
DR   UniGene; Mm.301173; -.
DR   ProteinModelPortal; Q8BL06; -.
DR   MEROPS; C19.080; -.
DR   PhosphoSite; Q8BL06; -.
DR   PRIDE; Q8BL06; -.
DR   Ensembl; ENSMUST00000022356; ENSMUSP00000022356; ENSMUSG00000034235.
DR   Ensembl; ENSMUST00000035340; ENSMUSP00000036214; ENSMUSG00000034235.
DR   GeneID; 78787; -.
DR   KEGG; mmu:78787; -.
DR   UCSC; uc007skc.1; mouse.
DR   CTD; 78787; -.
DR   MGI; MGI:1926037; Usp54.
DR   eggNOG; roNOG04130; -.
DR   GeneTree; ENSGT00440000033513; -.
DR   HOGENOM; HBG282381; -.
DR   HOVERGEN; HBG108646; -.
DR   InParanoid; Q8BL06; -.
DR   OMA; QASGYHS; -.
DR   OrthoDB; EOG4BVRVQ; -.
DR   NextBio; 349502; -.
DR   ArrayExpress; Q8BL06; -.
DR   Bgee; Q8BL06; -.
DR   CleanEx; MM_USP54; -.
DR   Genevestigator; Q8BL06; -.
DR   GermOnline; ENSMUSG00000034235; Mus musculus.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR001394; Peptidase_C19.
DR   Pfam; PF00443; UCH; 1.
DR   PROSITE; PS00972; UCH_2_1; FALSE_NEG.
DR   PROSITE; PS00973; UCH_2_2; FALSE_NEG.
DR   PROSITE; PS50235; UCH_2_3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Phosphoprotein.
FT   CHAIN         1   1588       Inactive ubiquitin carboxyl-terminal
FT                                hydrolase 54.
FT                                /FTId=PRO_0000249531.
FT   COILED      682    712       Potential.
FT   COMPBIAS    439    445       Poly-Ser.
FT   MOD_RES     227    227       Phosphoserine.
FT   VAR_SEQ       1     69       Missing (in isoform 2).
FT                                /FTId=VSP_020488.
FT   VAR_SEQ     383    402       HLTDSECNQKHTSKKGSLVE -> EQPSSPTPPYSQMVGSH
FT                                TQG (in isoform 2 and isoform 3).
FT                                /FTId=VSP_035679.
FT   VAR_SEQ     403   1588       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_035680.
FT   CONFLICT    925    925       G -> D (in Ref. 3; AAH66166/AAH66175).
FT   CONFLICT   1288   1288       R -> G (in Ref. 3; AAI17845).
FT   CONFLICT   1476   1476       L -> V (in Ref. 1; BAB31805).
FT   CONFLICT   1574   1574       G -> E (in Ref. 3; AAH66166/AAH66175).
SQ   SEQUENCE   1588 AA;  176664 MW;  4F211ACF4502D584 CRC64;
     MSWKRNYFSG SRGSVQGMFA PRSSMSIAPS KGLSNEPGQN SCFLNSALQV LWHLDIFRRS
     FRQLTTHKCM GDSCIFCALK GIFNQFQCSS EKVLPSDTLR SALAKTFQDE QRFQLGIMDD
     AAECFENLLM RIHFHIADET KEDICTAQHC ISHQKFAMTL FEQCVCSSCG ATSDPLPFIQ
     MVHYISTTAL CNQAICMLEK REKPSPSMFG ELLQNASTMG DLRNCPSNCG ERIRIRRVLM
     NAPQIITIGL VWDSEHSDLA EDVIHSLGTC LKLGDLFFRV TDDRAKQSEL YLVGMICYYG
     KHYSTFFFQT KIRKWMYFDD AHVKEIGPKW KDVVTKCIKG HYQPLLLLYA DPQGTPVSAQ
     DLPPHAQFLP YTKTCYDSED SGHLTDSECN QKHTSKKGSL VERRRSSGRV RRKGDEPQAS
     GYHSEGETLK EKQAPRNASK SSSSSRLKDF KETVSNMIHS RPSLASQTSA GSPCVGRAGD
     QLDKIPPRNF PLQARGWETE STSSEAKSSS SSKYRPTWRP KRESLNIDSI FSKDRRKHCG
     YTQLRTFPED AAKEFTPDEV SKPTANDIKD GGSRSQHKLW GTARPGSHLL EQHPRLIQRM
     ESGYESSERN SSSPVSLDAA PPDSVNVYRD QSTKRPVGFV PSWRHIPKSH SSSILEVDCT
     APMTSWTKTQ PLSDGEVTSR SELDELQEEV VRRAQEQELR KKREKELEAA KGFNPHPSRY
     MDLDELQNQG RSDGFERSLQ EANSIFEESL HLEQKGDCAA ALALCNEAIS KLRLTLHDAS
     SSTHSRALVD KKLQISIRKA RSLQDRMQQQ ASSQQPVQPS ASLPSQGGAL PQPTSEQPIT
     LQVLLNQEAQ LEPCKDTELG ATSSFFHSPA SCPELHSSLI PESPVSSVSQ HSPPGTSSLK
     LLTSFEVDSV NRSAFHRQGL PKATGRTEMN SQHECLPLDA LEDRLQGHRE DNSCCSKFPP
     REGRDIAQDQ LFEGKKNPAD ISMGMPWSYS TGEATSERVI YSLNSPSSSS AQPSIPPYSS
     CHPITSAASS PVLHAADPMQ KLNQHVQAQS LQTSLTSKVV RSSEEPYRLE FPSTKGLVRS
     LAEQFQKMQN TSTRDVIGSQ DRSLPNGVRK SSSPSDFMPP LSQGPGREHC RWVKQPRSPD
     GRERPPCWED PAAHPPLSMG SGLPDGETSR TAQPRLAEPD MYQGKLPQVT DIRSKELGSS
     VNLGTSLPLD SWVNVTRLCD SQVKPSAPGP GDKSSSHDSH PRATCLERSP ILLHPHWDQD
     TEQETSELES LYQASLQASS HTAYSDWRSQ DVAWQPLSLA GSADGMGRRL HSAPGLDLSK
     PLTAEMEHVL YEPSTVPVSQ DSSNVRKKTL ETGHHCSSSS SLPVIHDPPV FLLDPKLYPP
     QPQFLSPDVL MPSMAGEPYR PPGTSRSVHQ FLAMCDRDET PQGVKYTGRT LNYRSLPHRS
     RTDASWGPGS ETNQHIGARV LTMPACKPQL TYTATLPERH QGLQVPHAQS WGNLFHSPSH
     PSAVHPGSPP SSNLHVPLRS TWNSGPVLGS RTPGPRRIDM PPDDDWRQSS YPSQDRHRSP
     GEERIMFALS NAAGREQNRV RFLQHSRW
//
ID   UNK_MOUSE               Reviewed;         810 AA.
AC   Q8BL48; A2A853; Q8BVI6; Q99JZ8; Q99LL9;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=RING finger protein unkempt homolog;
DE   AltName: Full=Zinc finger CCCH domain-containing protein 5;
GN   Name=Unk; Synonyms=Kiaa1753, Zc3h5, Zc3hdc5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BL48-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BL48-2; Sequence=VSP_010274;
CC   -!- SIMILARITY: Belongs to the unkempt family.
CC   -!- SIMILARITY: Contains 5 C3H1-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98248.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK129438; BAC98248.1; ALT_INIT; mRNA.
DR   EMBL; AK046395; BAC32702.1; -; mRNA.
DR   EMBL; AK078095; BAC37123.1; -; mRNA.
DR   EMBL; AL607108; CAM24040.1; -; Genomic_DNA.
DR   EMBL; BC003195; AAH03195.1; -; mRNA.
DR   EMBL; BC005545; AAH05545.1; -; mRNA.
DR   EMBL; BC054452; AAH54452.1; -; mRNA.
DR   IPI; IPI00308784; -.
DR   IPI; IPI00411163; -.
DR   RefSeq; NP_766157.1; NM_172569.3.
DR   UniGene; Mm.297706; -.
DR   ProteinModelPortal; Q8BL48; -.
DR   SMR; Q8BL48; 90-326, 766-806.
DR   IntAct; Q8BL48; 2.
DR   STRING; Q8BL48; -.
DR   PhosphoSite; Q8BL48; -.
DR   PRIDE; Q8BL48; -.
DR   Ensembl; ENSMUST00000021116; ENSMUSP00000021116; ENSMUSG00000020770.
DR   GeneID; 217331; -.
DR   KEGG; mmu:217331; -.
DR   UCSC; uc007mjp.1; mouse.
DR   UCSC; uc007mjq.1; mouse.
DR   CTD; 217331; -.
DR   MGI; MGI:2442456; Unk.
DR   GeneTree; ENSGT00390000012005; -.
DR   HOGENOM; HBG356214; -.
DR   HOVERGEN; HBG061441; -.
DR   InParanoid; Q8BL48; -.
DR   OMA; VDKAVFH; -.
DR   OrthoDB; EOG4QRH3P; -.
DR   PhylomeDB; Q8BL48; -.
DR   NextBio; 375761; -.
DR   ArrayExpress; Q8BL48; -.
DR   Bgee; Q8BL48; -.
DR   CleanEx; MM_UNK; -.
DR   Genevestigator; Q8BL48; -.
DR   GermOnline; ENSMUSG00000020770; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR001841; Znf_RING.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00356; ZnF_C3H1; 5.
DR   PROSITE; PS50103; ZF_C3H1; 5.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Metal-binding; Nucleus;
KW   Phosphoprotein; Repeat; Zinc; Zinc-finger.
FT   CHAIN         1    810       RING finger protein unkempt homolog.
FT                                /FTId=PRO_0000213900.
FT   ZN_FING      84    113       C3H1-type 1.
FT   ZN_FING     124    154       C3H1-type 2.
FT   ZN_FING     215    241       C3H1-type 3.
FT   ZN_FING     251    285       C3H1-type 4.
FT   ZN_FING     293    321       C3H1-type 5.
FT   ZN_FING     766    801       RING-type; degenerate.
FT   COILED      643    727       Potential.
FT   COMPBIAS     70     73       Poly-Arg.
FT   MOD_RES     374    374       Phosphoserine (By similarity).
FT   MOD_RES     378    378       Phosphoserine (By similarity).
FT   MOD_RES     385    385       Phosphoserine.
FT   MOD_RES     412    412       Phosphotyrosine (By similarity).
FT   VAR_SEQ     356    369       VSPSSPHAPDLSAL -> L (in isoform 2).
FT                                /FTId=VSP_010274.
FT   CONFLICT    634    634       T -> A (in Ref. 2; BAC37123).
SQ   SEQUENCE   810 AA;  88058 MW;  78BA9F07530E92B5 CRC64;
     MSKGPGPGGS AASSAPPAAT AQVLQAQPEK PQHYTYLKEF RTEQCPLFVQ HKCTQHRPYT
     CFHWHFVNQR RRRSIRRRDG TFNYSPDVYC TKYDEATGLC PEGDECPFLH RTTGDTERRY
     HLRYYKTGIC IHETDSKGNC TKNGLHCAFA HGPHDLRSPV YDIRELQAME ALQNGQTTVE
     GSIEGQSAGA ASHAMIEKIL SEEPRWQETA YVLGNYKTEP CKKPPRLCRQ GYACPYYHNS
     KDRRRSPRKH KYRSSPCPNV KHGDEWGDPG KCENGDACQY CHTRTEQQFH PEIYKSTKCN
     DMQQAGSCPR GPFCAFAHIE PPPLSDDVQP SSAVSSPTQP GPVLYMPSAA GDSVPVSPSS
     PHAPDLSALL CRNSGLGSPS HLCSSPPGPS RKASNLEGLV FPGESSLAPG SYKKAPGFER
     EDQVGAEYLK NFKCQAKLKP HSLEPRSQEQ PLLQPKQDVL GILPVGSPLT SSISSSITSS
     LAATPPSPAG TNSTPGMNAN ALPFYPTSDT VESVIESALD DLDLNEFGVA ALEKTFDNSA
     VPHPSSVTIG GSLLQSSAPV NIPGSLGSSA SFHSASPSPP VSLSSHFLQQ PQGHLSQSEN
     TFLGTSASHG SLGLNGMNSS IWEHFASGSF SPGTSPAFLS GPGAAELARL RQELDEANGT
     IKQWEESWKQ AKQACDAWKK EAEEAGERAS AAGAECELAR EQRDALELRV KKLQEELERL
     HTVPEAQTLP AAPDLEALSL STLYSIQKQL RVHLEQVDKA VFHMQSVKCL KCQEQTRAVL
     PCQHAVLCEL CAEGSECPVC QPSRAHALQS
//
ID   ABLM2_MOUSE             Reviewed;         612 AA.
AC   Q8BL65; B2RUF8; Q6H8P8; Q80WK6; Q8BUT1; Q8BXI7;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Actin-binding LIM protein 2;
DE            Short=abLIM-2;
DE   AltName: Full=Actin-binding LIM protein family member 2;
GN   Name=Ablim2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Klimov E.A., Rakhmanaliev E.R., Rudco O.I.;
RT   "Structure and transcriptional activity of the ABLIM2 gene of human,
RT   mouse and rat.";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6;
RA   Xu Z.-P., Piatigorsky J.;
RT   "Identification of a novel actin-binding LIM protein (abLIM2) in
RT   developing cornea.";
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Corpora quadrigemina, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH F-ACTIN
RP   AND ABRA.
RX   PubMed=17194709; DOI=10.1074/jbc.M607549200;
RA   Barrientos T., Frank D., Kuwahara K., Bezprozvannaya S., Pipes G.C.T.,
RA   Bassel-Duby R., Richardson J.A., Katus H.A., Olson E.N., Frey N.;
RT   "Two novel members of the ABLIM protein family, ABLIM-2 and -3,
RT   associate with STARS and directly bind F-actin.";
RL   J. Biol. Chem. 282:8393-8403(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289; SER-294; SER-296
RP   AND SER-477, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: May act as scaffold protein. May stimulate ABRA activity
CC       and ABRA-dependent SRF transcriptional activity.
CC   -!- SUBUNIT: Interacts with F-actin and ABRA.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=In skeletal muscle,
CC       sarcomeric or cosarcomeric localization.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q8BL65-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BL65-2; Sequence=VSP_012122;
CC       Name=3;
CC         IsoId=Q8BL65-3; Sequence=VSP_012121, VSP_012122;
CC       Name=4;
CC         IsoId=Q8BL65-4; Sequence=VSP_012120, VSP_012121, VSP_012122;
CC       Name=5;
CC         IsoId=Q8BL65-5; Sequence=VSP_012121, VSP_012123, VSP_012124;
CC   -!- TISSUE SPECIFICITY: Expressed in brain. Highly expressed in
CC       caudate/putamen, moderately expressed in the olfactory bulb. In
CC       the hippocampus, expressed in the CA1, CA2 and CA3 fields. In the
CC       cerebellum, expressed in Purkinje cells.
CC   -!- DEVELOPMENTAL STAGE: At 15.5 dpc, predominantly expressed in
CC       skeletal muscle tissue, including diaphragm, and to a lesser
CC       extent in the central nervous system.
CC   -!- SIMILARITY: Contains 1 HP (headpiece) domain.
CC   -!- SIMILARITY: Contains 4 LIM zinc-binding domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AJ748602; CAG38377.1; -; mRNA.
DR   EMBL; AJ748603; CAG38378.1; -; mRNA.
DR   EMBL; AY274116; AAP23233.1; -; mRNA.
DR   EMBL; AK046243; BAC32651.1; -; mRNA.
DR   EMBL; AK046879; BAC32905.1; -; mRNA.
DR   EMBL; AK082707; BAC38580.1; -; mRNA.
DR   EMBL; BC141125; AAI41126.1; -; mRNA.
DR   IPI; IPI00226694; -.
DR   IPI; IPI00312739; -.
DR   IPI; IPI00463583; -.
DR   IPI; IPI00468743; -.
DR   IPI; IPI00480577; -.
DR   RefSeq; NP_001171168.1; NM_001177697.1.
DR   RefSeq; NP_001171170.1; NM_001177699.1.
DR   RefSeq; NP_001171171.1; NM_001177700.1.
DR   RefSeq; NP_808346.3; NM_177678.7.
DR   UniGene; Mm.254446; -.
DR   ProteinModelPortal; Q8BL65; -.
DR   SMR; Q8BL65; 21-271, 541-612.
DR   STRING; Q8BL65; -.
DR   PhosphoSite; Q8BL65; -.
DR   PRIDE; Q8BL65; -.
DR   Ensembl; ENSMUST00000054598; ENSMUSP00000050571; ENSMUSG00000029095.
DR   Ensembl; ENSMUST00000114206; ENSMUSP00000109844; ENSMUSG00000029095.
DR   Ensembl; ENSMUST00000114207; ENSMUSP00000109845; ENSMUSG00000029095.
DR   GeneID; 231148; -.
DR   KEGG; mmu:231148; -.
DR   UCSC; uc008xee.1; mouse.
DR   UCSC; uc008xeg.1; mouse.
DR   CTD; 231148; -.
DR   MGI; MGI:2385758; Ablim2.
DR   GeneTree; ENSGT00570000079028; -.
DR   HOVERGEN; HBG031499; -.
DR   OrthoDB; EOG4Z62NJ; -.
DR   NextBio; 380433; -.
DR   ArrayExpress; Q8BL65; -.
DR   Bgee; Q8BL65; -.
DR   CleanEx; MM_ABLIM2; -.
DR   Genevestigator; Q8BL65; -.
DR   GermOnline; ENSMUSG00000029095; Mus musculus.
DR   GO; GO:0030016; C:myofibril; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:MGI.
DR   InterPro; IPR003128; Villin_headpiece.
DR   InterPro; IPR001781; Znf_LIM.
DR   Gene3D; G3DSA:1.10.950.10; VHP; 1.
DR   Gene3D; G3DSA:2.10.110.10; Znf_LIM; 3.
DR   Pfam; PF00412; LIM; 4.
DR   Pfam; PF02209; VHP; 1.
DR   SMART; SM00132; LIM; 4.
DR   SMART; SM00153; VHP; 1.
DR   SUPFAM; SSF47050; VHP; 1.
DR   PROSITE; PS51089; HP; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; LIM domain; Metal-binding;
KW   Phosphoprotein; Repeat; Zinc.
FT   CHAIN         1    612       Actin-binding LIM protein 2.
FT                                /FTId=PRO_0000075700.
FT   DOMAIN       22     81       LIM zinc-binding 1.
FT   DOMAIN       81    141       LIM zinc-binding 2.
FT   DOMAIN      151    210       LIM zinc-binding 3.
FT   DOMAIN      210    270       LIM zinc-binding 4.
FT   DOMAIN      544    612       HP.
FT   COMPBIAS    364    412       Ser-rich.
FT   MOD_RES     289    289       Phosphoserine.
FT   MOD_RES     294    294       Phosphoserine.
FT   MOD_RES     296    296       Phosphoserine.
FT   MOD_RES     477    477       Phosphoserine.
FT   VAR_SEQ     350    350       E -> ESPQLLSPTPTE (in isoform 4).
FT                                /FTId=VSP_012120.
FT   VAR_SEQ     390    390       P -> PAGTVSVGTSSCLSLSQHPSPTSVFRHHYIPYFR
FT                                (in isoform 3, isoform 4 and isoform 5).
FT                                /FTId=VSP_012121.
FT   VAR_SEQ     507    546       RFPYSKPDTLPGPRKDGLDLRNANLAPCGADPDASWGTRE
FT                                -> Q (in isoform 2, isoform 3 and isoform
FT                                4).
FT                                /FTId=VSP_012122.
FT   VAR_SEQ     507    526       RFPYSKPDTLPGPRKDGLDL -> QCQPGPLWSRPGCQLGH
FT                                ARV (in isoform 5).
FT                                /FTId=VSP_012123.
FT   VAR_SEQ     527    612       Missing (in isoform 5).
FT                                /FTId=VSP_012124.
FT   CONFLICT    305    305       D -> N (in Ref. 3; BAC32905).
FT   CONFLICT    406    406       D -> N (in Ref. 3; BAC32905).
SQ   SEQUENCE   612 AA;  68107 MW;  97FE5A9C049AD455 CRC64;
     MSAVSQPQAA HAPLEKPAST AILCNTCGNV CKGEVLRVQN KYFHIRCFVC KACGCDLAEG
     GFFVRQGEHI CTRDYQRLYG TRCFSCDRFI EGEVVSALGK TYHPDCFVCA VCRLPFPPGD
     RVTFNGKECM CQKCSPPTLL GNSAHVAQGL RSCGGCGLEI KNGQALVALD KHWHLGCFKC
     KTCGKLLNAE YISKDGLPYC EADYHSKFGI RCDGCEKYIT GRVLEAGEKH YHPSCALCVR
     CGQMFSEGEE MYLQGSSIWH PACRQAARTE DKSKETRTSS ESIVSVPASS TSGSPSRVIY
     AKLGDEILDY RDLAALPKNK AIYNIDRPDM ISYSPYISHS AVGDRQSYGE GDQDDRSYKQ
     CRTSSPSSAG SVSLGHYTPT SRSPQHYSRP GSESGRSTPS LSVHSDSRPP SSTYQQAPRH
     FHVPDTGVKD NIYRKPPIYK QHAARRLDVE DSSFDQDSRK KTTWLLLKGD ADTRTNSPDL
     DSQSLSLSSG TDQEPLQRMA GDSLYSRFPY SKPDTLPGPR KDGLDLRNAN LAPCGADPDA
     SWGTREYKIY PYDSLIVTNR IRVKLPKDVD RTRLERHLSP EEFQEVFGMS IEEFDRLALW
     KRNDLKKKAL LF
//
ID   RHG22_MOUSE             Reviewed;         702 AA.
AC   Q8BL80; Q6QHH6; Q8BVH4; Q8CHY5;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Rho GTPase-activating protein 22;
DE   AltName: Full=Rho-type GTPase-activating protein 22;
DE   AltName: Full=p68RacGAP;
GN   Name=Arhgap22;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ARG-201.
RX   PubMed=14966113; DOI=10.1074/jbc.M311721200;
RA   Aitsebaomo J., Wennerberg K., Der C.J., Zhang C., Kedar V., Moser M.,
RA   Kingsley-Kallesen M.L., Zeng G.-Q., Patterson C.;
RT   "p68RacGAP is a novel GTPase-activating protein that interacts with
RT   vascular endothelial zinc finger-1 and modulates endothelial cell
RT   capillary formation.";
RL   J. Biol. Chem. 279:17963-17972(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Rho GTPase-activating protein involved in the signal
CC       transduction pathway that regulates endothelial cell capillary
CC       tube formation during angiogenesis. Acts as a GTPase activator for
CC       the RAC1 by converting it to an inactive GDP-bound state. Inhibits
CC       RAC1-dependent lamellipodia formation. May also play a role in
CC       transcription regulation via its interaction with VEZF1, by
CC       regulating activity of the endothelin-1 (EDN1) promoter.
CC   -!- SUBUNIT: Interacts with VEZF1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Mainly cytoplasmic.
CC       Some fraction is nuclear.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BL80-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BL80-2; Sequence=VSP_023706;
CC       Name=3;
CC         IsoId=Q8BL80-3; Sequence=VSP_023706, VSP_023707;
CC   -!- TISSUE SPECIFICITY: Predominantly present in endothelial cells (at
CC       protein level).
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC32603.1; Type=Frameshift; Positions=48;
CC       Sequence=BAC37178.1; Type=Frameshift; Positions=278;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY541447; AAS47033.1; -; mRNA.
DR   EMBL; AK046097; BAC32603.1; ALT_FRAME; mRNA.
DR   EMBL; AK078218; BAC37178.1; ALT_FRAME; mRNA.
DR   EMBL; BC038272; AAH38272.1; -; mRNA.
DR   IPI; IPI00222742; -.
DR   IPI; IPI00407698; -.
DR   IPI; IPI00831074; -.
DR   RefSeq; NP_722495.3; NM_153800.4.
DR   UniGene; Mm.318350; -.
DR   HSSP; P42331; 1V89.
DR   ProteinModelPortal; Q8BL80; -.
DR   SMR; Q8BL80; 39-153, 159-356.
DR   IntAct; Q8BL80; 1.
DR   STRING; Q8BL80; -.
DR   PhosphoSite; Q8BL80; -.
DR   REPRODUCTION-2DPAGE; Q8BL80; -.
DR   PRIDE; Q8BL80; -.
DR   Ensembl; ENSMUST00000052768; ENSMUSP00000049659; ENSMUSG00000063506.
DR   Ensembl; ENSMUST00000068112; ENSMUSP00000066114; ENSMUSG00000063506.
DR   Ensembl; ENSMUST00000111956; ENSMUSP00000107587; ENSMUSG00000063506.
DR   GeneID; 239027; -.
DR   KEGG; mmu:239027; -.
DR   NMPDR; fig|10090.3.peg.28819; -.
DR   UCSC; uc007szm.1; mouse.
DR   CTD; 239027; -.
DR   MGI; MGI:2443418; Arhgap22.
DR   eggNOG; roNOG15552; -.
DR   GeneTree; ENSGT00590000083061; -.
DR   HOGENOM; HBG715824; -.
DR   HOVERGEN; HBG058875; -.
DR   InParanoid; Q8BL80; -.
DR   OMA; ASMAWSG; -.
DR   OrthoDB; EOG4PRSQG; -.
DR   NextBio; 383951; -.
DR   ArrayExpress; Q8BL80; -.
DR   Bgee; Q8BL80; -.
DR   CleanEx; MM_ARHGAP22; -.
DR   Genevestigator; Q8BL80; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Angiogenesis; Coiled coil; Cytoplasm;
KW   Developmental protein; Differentiation; GTPase activation; Nucleus;
KW   Phosphoprotein; Transcription; Transcription regulation.
FT   CHAIN         1    702       Rho GTPase-activating protein 22.
FT                                /FTId=PRO_0000280470.
FT   DOMAIN       43    151       PH.
FT   DOMAIN      161    355       Rho-GAP.
FT   COILED      594    691       Potential.
FT   COMPBIAS    437    584       Ser-rich.
FT   MOD_RES     397    397       Phosphoserine (By similarity).
FT   VAR_SEQ       1    131       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_023706.
FT   VAR_SEQ     226    295       STTDVHTVASLLKLYLRELPEPVIPFARYEDFLSCAQLLTK
FT                                DEGEGTVELAKQVSNLPQANYNLLRYICK -> R (in
FT                                isoform 3).
FT                                /FTId=VSP_023707.
FT   MUTAGEN     201    201       R->A: Loss of function.
FT   CONFLICT    487    487       L -> R (in Ref. 2; BAC32603/BAC37178).
SQ   SEQUENCE   702 AA;  77786 MW;  48D0D339C89C2BED CRC64;
     MLPTASSKRR TFAARYFTRS KSLVMGEQSR SPGRPLVPHK LGPVLKAGWL RKQRSIMKNW
     QQRWFVLRGD QLFYYKDKDE SKPQGFISLQ GTQVTELLPD PEDPGKHLFE ITPGGATERE
     KVPANPEALL LMASSQRDME DWVQAIRRVI WAPLGRGIFG QRLEDTVHHE RKFGPRLAPL
     LVEQCVDFIR ERGLSEEGLF RMPGQANLVR DLQDSFDCGE KPLFDSTTDV HTVASLLKLY
     LRELPEPVIP FARYEDFLSC AQLLTKDEGE GTVELAKQVS NLPQANYNLL RYICKFLDEV
     QAHSDVNKMS VQNLATVFGP NILRPQIEDP VTIMEGTSLV QHLMTVLIRK HGQLFAATSL
     EEPASPHGTV EWGSEEVTRD HRGEPGSPGL PTHRTSSLDG PAAAVLSRTS PPRLGSQTGP
     AATSPGKKMH TLPVWKSSFR QQGSRSESPK GVNSSLEVPI ISSGGNWLIN GLSSLRSHRR
     ASSGDRLKDT GSAQRLSTYD NVPPSSQFSS TASVASTSWS VASSSREASV SSCTACRASN
     SSACSSLHTE WALEPSPLPS SSEGHQSPDL GHSLDEPCVG SGSSEPNDPG SPTQAHVRRC
     RALQGQVAEL RAELCQQRTE YKRSLKSIEE GSADLRKQMS RLEEELDQER KKYAMLEIKL
     RNSERAREDA ERRNQLLQRE MEEFFSTLGS LTTGTKGSRA PE
//
ID   MBLC2_MOUSE             Reviewed;         279 AA.
AC   Q8BL86;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Metallo-beta-lactamase domain-containing protein 2;
DE            EC=3.-.-.-;
GN   Name=Mblac2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
CC   -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC       Glyoxalase II family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK046032; BAC32577.1; -; mRNA.
DR   IPI; IPI00222749; -.
DR   RefSeq; NP_082648.1; NM_028372.1.
DR   UniGene; Mm.480734; -.
DR   ProteinModelPortal; Q8BL86; -.
DR   SMR; Q8BL86; 25-239.
DR   PRIDE; Q8BL86; -.
DR   Ensembl; ENSMUST00000057598; ENSMUSP00000051644; ENSMUSG00000051098.
DR   GeneID; 72852; -.
DR   KEGG; mmu:72852; -.
DR   UCSC; uc007ria.1; mouse.
DR   CTD; 72852; -.
DR   MGI; MGI:1920102; Mblac2.
DR   eggNOG; roNOG14053; -.
DR   GeneTree; ENSGT00390000017819; -.
DR   InParanoid; Q8BL86; -.
DR   OrthoDB; EOG41G34S; -.
DR   NextBio; 337043; -.
DR   ArrayExpress; Q8BL86; -.
DR   Bgee; Q8BL86; -.
DR   CleanEx; MM_2900024O10RIK; -.
DR   Genevestigator; Q8BL86; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR001279; Blactmase-like.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   SMART; SM00849; Lactamase_B; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding; Zinc.
FT   CHAIN         1    279       Metallo-beta-lactamase domain-containing
FT                                protein 2.
FT                                /FTId=PRO_0000325936.
FT   METAL        83     83       Zinc 1 (By similarity).
FT   METAL        85     85       Zinc 1 (By similarity).
FT   METAL        87     87       Zinc 2 (By similarity).
FT   METAL        88     88       Zinc 2 (By similarity).
FT   METAL       170    170       Zinc 1 (By similarity).
FT   METAL       189    189       Zinc 1 (By similarity).
FT   METAL       189    189       Zinc 2 (By similarity).
FT   METAL       231    231       Zinc 2 (By similarity).
SQ   SEQUENCE   279 AA;  31206 MW;  83F882FF44580DF1 CRC64;
     MSALEWYAHK SLGDGIFWIQ ERFYESGNRA NIWLVRGSEQ DVVIDTGLGL RSLPEYLYSS
     GLLQDCGSKE DAGRRPLLAV ATHVHFDHSG GLYQFDQVAV HRAEAEALAR GDNFETVTWL
     SDSEVVRAPS PGWRARQFRM QAVQPTLILP DGDVINLGDR QLTVMHMPGH SRGSICLHDK
     DRKVLFSGDV VYDGSLIDWL PYSRISDYVG TCERLIELVD RGLVEKVLPG HFNTFGAERL
     FRLASNYISK AGICHKVSTF AMRSLASLAL RVTNPRTSP
//
ID   SRSF7_MOUSE             Reviewed;         267 AA.
AC   Q8BL97; Q8BMC6; Q8BUR2; Q8R2N4; Q8R3E9; Q91YS1;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Serine/arginine-rich splicing factor 7;
DE   AltName: Full=Splicing factor, arginine/serine-rich 7;
GN   Name=Srsf7; Synonyms=Sfrs7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Wolffian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; SER-194; SER-196;
RP   SER-208; SER-210; SER-212; SER-216; SER-252; SER-254 AND SER-256, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Required for pre-mRNA splicing (By similarity).
CC   -!- SUBUNIT: Found in large molecular weight complexes containing
CC       CCNL1 and the p110 isoforms of either CDC2L1 or CDC2L2. Interacts
CC       with CCNL2 and CPSF6 (By similarity).
CC   -!- INTERACTION:
CC       Q6PFR5:Tra2a; NbExp=1; IntAct=EBI-913123, EBI-913075;
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Isoforms, lacking all or part of the RS domain, may be
CC         involved in modulating Srsf7 function;
CC       Name=1;
CC         IsoId=Q8BL97-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q8BL97-2; Sequence=VSP_013654;
CC       Name=3;
CC         IsoId=Q8BL97-3; Sequence=VSP_013654, VSP_013655, VSP_013656;
CC       Name=4;
CC         IsoId=Q8BL97-4; Sequence=VSP_013654, VSP_013657;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Extensively phosphorylated on serine residues in the RS
CC       domain (By similarity).
CC   -!- SIMILARITY: Belongs to the splicing factor SR family.
CC   -!- SIMILARITY: Contains 1 CCHC-type zinc finger.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR   EMBL; AK032861; BAC28058.1; -; mRNA.
DR   EMBL; AK045884; BAC32521.1; -; mRNA.
DR   EMBL; AK082848; BAC38650.1; -; mRNA.
DR   EMBL; BC014857; AAH14857.1; -; mRNA.
DR   EMBL; BC025529; AAH25529.1; -; mRNA.
DR   EMBL; BC027391; AAH27391.1; -; mRNA.
DR   IPI; IPI00153743; -.
DR   IPI; IPI00222763; -.
DR   IPI; IPI00474158; -.
DR   IPI; IPI00474169; -.
DR   RefSeq; NP_001182414.1; NM_001195485.1.
DR   RefSeq; NP_001182415.1; NM_001195486.1.
DR   RefSeq; NP_001182416.1; NM_001195487.1.
DR   RefSeq; NP_666195.1; NM_146083.2.
DR   UniGene; Mm.292016; -.
DR   ProteinModelPortal; Q8BL97; -.
DR   SMR; Q8BL97; 10-127.
DR   DIP; DIP-36580N; -.
DR   IntAct; Q8BL97; 7.
DR   STRING; Q8BL97; -.
DR   PhosphoSite; Q8BL97; -.
DR   PRIDE; Q8BL97; -.
DR   Ensembl; ENSMUST00000063403; ENSMUSP00000066393; ENSMUSG00000024097.
DR   Ensembl; ENSMUST00000063417; ENSMUSP00000070983; ENSMUSG00000024097.
DR   Ensembl; ENSMUST00000112421; ENSMUSP00000108040; ENSMUSG00000024097.
DR   GeneID; 225027; -.
DR   KEGG; mmu:225027; -.
DR   UCSC; uc008dqp.1; mouse.
DR   UCSC; uc008dqt.1; mouse.
DR   CTD; 225027; -.
DR   MGI; MGI:1926232; Srsf7.
DR   GeneTree; ENSGT00560000076881; -.
DR   HOGENOM; HBG756718; -.
DR   HOVERGEN; HBG107480; -.
DR   InParanoid; Q8BL97; -.
DR   OrthoDB; EOG4Z62PZ; -.
DR   NextBio; 377508; -.
DR   ArrayExpress; Q8BL97; -.
DR   Bgee; Q8BL97; -.
DR   CleanEx; MM_SFRS7; -.
DR   Genevestigator; Q8BL97; -.
DR   GermOnline; ENSMUSG00000024097; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR013084; Znf_CCH_retrovir.
DR   InterPro; IPR001878; Znf_CCHC.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Gene3D; G3DSA:4.10.60.10; Znf_CCH_retrovir; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Metal-binding; mRNA processing;
KW   mRNA splicing; Nucleus; Phosphoprotein; Repeat; RNA-binding; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    267       Serine/arginine-rich splicing factor 7.
FT                                /FTId=PRO_0000081933.
FT   DOMAIN       40    113       RRM.
FT   REPEAT      182    189       1.
FT   REPEAT      190    197       2.
FT   REPEAT      198    205       3.
FT   REPEAT      206    213       4.
FT   REPEAT      240    247       5; approximate.
FT   REPEAT      248    255       6; approximate.
FT   ZN_FING     133    150       CCHC-type.
FT   REGION      182    255       6 X 8 AA repeats of R-R-S-R-S-X-S-X.
FT   COMPBIAS    150    267       Arg/Ser-rich (RS domain).
FT   MOD_RES      53     53       N6-acetyllysine (By similarity).
FT   MOD_RES     192    192       Phosphoserine.
FT   MOD_RES     194    194       Phosphoserine.
FT   MOD_RES     196    196       Phosphoserine.
FT   MOD_RES     200    200       Phosphoserine (By similarity).
FT   MOD_RES     202    202       Phosphoserine (By similarity).
FT   MOD_RES     204    204       Phosphoserine (By similarity).
FT   MOD_RES     208    208       Phosphoserine.
FT   MOD_RES     210    210       Phosphoserine.
FT   MOD_RES     212    212       Phosphoserine.
FT   MOD_RES     216    216       Phosphoserine.
FT   MOD_RES     221    221       Phosphoserine (By similarity).
FT   MOD_RES     223    223       Phosphoserine (By similarity).
FT   MOD_RES     225    225       Phosphoserine (By similarity).
FT   MOD_RES     246    246       Phosphoserine (By similarity).
FT   MOD_RES     250    250       Phosphoserine (By similarity).
FT   MOD_RES     252    252       Phosphoserine.
FT   MOD_RES     254    254       Phosphoserine.
FT   MOD_RES     256    256       Phosphoserine.
FT   MOD_RES     260    260       Phosphoserine (By similarity).
FT   MOD_RES     262    262       Phosphoserine (By similarity).
FT   VAR_SEQ       1     38       MRSSARGRPLQAATAFFLSLFFFLRRFERGFWLWGGDS ->
FT                                MSRYGRYGG (in isoform 2, isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_013654.
FT   VAR_SEQ     159    186       SRSRSHSRSRGRRYSRSRSRSRGRRSRS -> YLINEGMVG
FT                                ILVNQSNSFISKAETSVFL (in isoform 3).
FT                                /FTId=VSP_013655.
FT   VAR_SEQ     187    267       Missing (in isoform 3).
FT                                /FTId=VSP_013656.
FT   VAR_SEQ     238    249       Missing (in isoform 4).
FT                                /FTId=VSP_013657.
FT   CONFLICT    155    155       R -> T (in Ref. 1; BAC28058).
FT   CONFLICT    208    212       SRSGS -> FRFGF (in Ref. 2; AAH14857).
FT   CONFLICT    218    220       Missing (in Ref. 1; BAC38650).
FT   CONFLICT    231    231       S -> F (in Ref. 2; AAH14857).
FT   CONFLICT    251    251       R -> C (in Ref. 2; AAH14857).
FT   CONFLICT    258    258       H -> P (in Ref. 2; AAH14857).
SQ   SEQUENCE   267 AA;  30818 MW;  F193FC4C3A7D8C7C CRC64;
     MRSSARGRPL QAATAFFLSL FFFLRRFERG FWLWGGDSET KVYVGNLGTG AGKGELERAF
     SYYGPLRTVW IARNPPGFAF VEFEDPRDAE DAVRGLDGKV ICGSRVRVEL STGMPRRSRF
     DRPPARRPFD PNDRCYECGE KGHYAYDCHR YSRRRRSRSR SRSHSRSRGR RYSRSRSRSR
     GRRSRSASPR RSRSVSLRRS RSASLRRSRS GSIIGSRYFQ SRSRSRSRSR SISRPRSSRS
     KSRSPSPKRS RSPSGSPHRS ASPERMD
//
ID   DOP1_MOUSE              Reviewed;        2399 AA.
AC   Q8BL99; Q80XM5; Q8BIX5; Q8BIY4; Q8BLK8;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 2.
DT   08-MAR-2011, entry version 47.
DE   RecName: Full=Protein dopey-1;
GN   Name=Dopey1; Synonyms=D9Ertd809e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-1252 (ISOFORM 6), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-726 (ISOFORM 5).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Corpora quadrigemina, Embryo, Lung, Ovary, and Wolffian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1240, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May be involved in protein traffic between late Golgi
CC       and early endosomes (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q8BL99-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BL99-2; Sequence=VSP_027424, VSP_027426;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8BL99-3; Sequence=VSP_027418, VSP_027427, VSP_027428,
CC                                  VSP_027429;
CC       Name=4;
CC         IsoId=Q8BL99-4; Sequence=VSP_027420, VSP_027421;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q8BL99-5; Sequence=VSP_027422;
CC       Name=6;
CC         IsoId=Q8BL99-6; Sequence=VSP_027419, VSP_027423, VSP_027425;
CC   -!- SIMILARITY: Belongs to the dopey family.
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DR   EMBL; AK044820; BAC32105.2; -; mRNA.
DR   EMBL; AK045873; BAC32517.1; -; mRNA.
DR   EMBL; AK052544; BAC35032.1; -; mRNA.
DR   EMBL; AK054511; BAC35807.1; -; mRNA.
DR   EMBL; AC157998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC043710; AAH43710.1; -; mRNA.
DR   IPI; IPI00118309; -.
DR   IPI; IPI00222766; -.
DR   IPI; IPI00661400; -.
DR   IPI; IPI00856654; -.
DR   IPI; IPI00857801; -.
DR   IPI; IPI00857898; -.
DR   UniGene; Mm.245500; -.
DR   UniGene; Mm.436359; -.
DR   STRING; Q8BL99; -.
DR   PhosphoSite; Q8BL99; -.
DR   PRIDE; Q8BL99; -.
DR   Ensembl; ENSMUST00000034987; ENSMUSP00000034987; ENSMUSG00000034973.
DR   Ensembl; ENSMUST00000098498; ENSMUSP00000096099; ENSMUSG00000034973.
DR   UCSC; uc009qxg.1; mouse.
DR   MGI; MGI:1289294; Dopey1.
DR   GeneTree; ENSGT00390000016421; -.
DR   HOVERGEN; HBG051222; -.
DR   OrthoDB; EOG44MXR4; -.
DR   Bgee; Q8BL99; -.
DR   CleanEx; MM_DOPEY1; -.
DR   Genevestigator; Q8BL99; -.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR007249; Dopey_N.
DR   Pfam; PF04118; Dopey_N; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1   2399       Protein dopey-1.
FT                                /FTId=PRO_0000297948.
FT   MOD_RES    1240   1240       Phosphothreonine.
FT   MOD_RES    1694   1694       Phosphotyrosine (By similarity).
FT   MOD_RES    1699   1699       Phosphoserine (By similarity).
FT   VAR_SEQ       1   1852       Missing (in isoform 3).
FT                                /FTId=VSP_027418.
FT   VAR_SEQ     294    302       Missing (in isoform 6).
FT                                /FTId=VSP_027419.
FT   VAR_SEQ     331    364       AMVGILQVNGFGEESTLMQDLKPFRILISLLDKP -> VTA
FT                                VFIILCLSYIEKA (in isoform 4).
FT                                /FTId=VSP_027420.
FT   VAR_SEQ     365   2399       Missing (in isoform 4).
FT                                /FTId=VSP_027421.
FT   VAR_SEQ     446    453       Missing (in isoform 5).
FT                                /FTId=VSP_027422.
FT   VAR_SEQ     492    492       L -> LPTRSMRVLCQ (in isoform 6).
FT                                /FTId=VSP_027423.
FT   VAR_SEQ     571    584       QVSSVSMENPAEVF -> VISVGVHFFGVEFH (in
FT                                isoform 2).
FT                                /FTId=VSP_027424.
FT   VAR_SEQ     571    571       Missing (in isoform 6).
FT                                /FTId=VSP_027425.
FT   VAR_SEQ     585   2399       Missing (in isoform 2).
FT                                /FTId=VSP_027426.
FT   VAR_SEQ    1853   1862       RKFSFRTGAD -> MLQFFYAYIQ (in isoform 3).
FT                                /FTId=VSP_027427.
FT   VAR_SEQ    2164   2164       Q -> QVPTLHSQVFLFFRVLLLRMSPQHLTSLWPTMITEL
FT                                (in isoform 3).
FT                                /FTId=VSP_027428.
FT   VAR_SEQ    2282   2298       Missing (in isoform 3).
FT                                /FTId=VSP_027429.
SQ   SEQUENCE   2399 AA;  269257 MW;  1567AD9CE4DBA01E CRC64;
     MNTEELELLS DSKYRNYVAA IDKALKNFEY SSEWADLISA LGKLNKVLQN NAKYQVVPKK
     LTIGKRLAQC LHPALPGGVH RKALETYEII FKIIGPKRLA KDLFLYSSGL FPLLANAAMS
     VKPALLGLYE MYYLPLGKTL KPGLQGLLTG ILPGLEEGSE YYERTNTLLE KVAAAVEQSA
     FYSALWGSLL TSPAVRLPGI TYVLAHLNRK LSMEDQLYII GSDIELMVEA VSTSVQDSSV
     LVQRSTLDLI LFCFPFHMSQ ATRPDMIRIL SAALHVVLRR DMSLNRRLYA WLLGFDNNGA
     IIGPRSTRHS NPEEHATYYF TTFSKELLVQ AMVGILQVNG FGEESTLMQD LKPFRILISL
     LDKPELGPVI LEDVLIEVFR TLYSQCKAEL DLQMEPPFSK DHAQLSSKLR ENKKTAELIK
     TANLLFNSFE PYYMWDYIAR WFEECCRQSF FLSRRTLHAR LQVGPGDSSD SSELQLTNFC
     LLVDFLLDIV SLETYIEIQT EHLPQLLLRM ISALTSHLQT LRLSELTDSL RLCSKILSKV
     QPPLLSAGNG GVVQFPSGQN STVKEWEDKK QVSSVSMENP AEVFEDGENP PSSRSSESGF
     TEFIQYQADR PDDLDRELNG QGAATIPIGS TSSETETAST VGSEETVIQP PSTFTQGAAG
     RSGKAVQKTA MQCCLEYVQQ FLSRLINLYI IHSDSFPQAL AADHQGDFSR IQRETSKWDR
     DSQGDAKERN IHTPKTSKEY LSAFLAACQL FLECSSFPVY IAEGNHTSES HSEKPDTDCE
     HAHPPQWLRT LMSACSQARD FRVQSAAVSL VMDLVGLTQS VAMVTGENIN SMEPAQPLSP
     NQGRVAVVIR PPLTQGNLKY IAEKTEFFKH VALTLWDQLG DGTPQHHQKS VELFYQLHNL
     VPSSSICEDV VSQQLTHKDK KIRMEAHAKF AVLWHLTRDL HINKSSFARS FDRSLFIMLD
     SLTSLDGSTS SVGQAWLNQV LQRHDIARVL EPLLLLLLHP KTQRVSVQRV QAERYWSKTS
     CYPGEENDKH FMQNFTCNNV SQVHLIASKG NGEKPLTMDE MENFSLTVNP LSDRLSLLST
     SSETIPMVVS DFDLPDQQME ILQSSDSGCS QSSAGDNFSY EVDPENANAH EDSHMAKASS
     PDDDVQQVVF DLICKVVSGL EAESESVTSE LEIESLQTKS SDLDPGKEAT KIEDQAPQHS
     QHVLLSDDSP RFLSVSTEEG CECLANGISR NSSSPCISGT AQTLNDSSVP SETKSRQRSH
     SSIQFSFKEK LSEKVSEKET IVKESGKQPG AKPKVKLARK KDEDKKKAAS EKLKQANVFF
     SEGLDLENWY SCGEGEISEI ESDMGSPGSR KSPNFNIHPL YQHVLLYLQL YDSSRTLYAF
     SAIKSILKTN PIAFVNAIST TSVNNAYTPQ LSLLQNLLAR HRISVMGKDF YSHIPVDSNH
     NFRSSMYIEI LISLCLYYMR SHYPTHVKVT TQDLIGNRNM QMMSIEILTL LFTELAKVIE
     SSAKGFPSFI SDMLSKCKVQ KVILHCLLSS IFSVQKWHSE KTAGKSMVAV EEGFSEDSLI
     NFSEDELDNG STLQSQLLRV LQRLIVLEHH VMTIPEENEA GFDFVVSDLE HISPHQPMTS
     LQYLHAQPIT CQGMFLCAVI RALHQHCACK MHPQWIGLIT STLPYMGKVL QRVVVSVTLQ
     LCRNLDNLIQ QYKYETGLSD SRPLWVASII PPDMILTLLE GITAIIHYCL LDPTTQYHQL
     LVNVDQKHLV EARSGILSIL HMIMSSVTLL WSILHQADAS EKMAVAASAS VTTINLGATK
     VIPAASEEQL LLVELVRSIS VMRAETVIQT VKEVLKQPPA IAKDKVRKLC FCRKFSFRTG
     ADRIPVPNIV DSWTSLLVLL KDSIQLSLPA PGQFLILGVL NEFIMKNPSL ENKKDQRDLQ
     DVTHKIVDAI GAIAGSSLEQ TTWLRRNLEV KPSPKIMVDG TNLESDVEDM LSPAMETSNI
     TPSVYSVHAL TLLSEVLAHL LDMVFYSDEK ERVIPLLVNI MHYVVPYLRN HSAHNAPSYR
     ACVQLLSSLS GYQYTRRAWK KEAFDLFMDP SFFQMDASCV SHWRAIMDNL MTHDKTTFRD
     LMTRVAVAQS SSLNLFANRD VELEQRAMLL KRLAFAVLSS ESDQYQKYLP DIQERLVESL
     RLPQVQVFLL MEQELTADED ISRTSGPSAA GLETTYTGGN GFSTSYNSQR WLNLYLSACK
     FLDLALALPS ENLPQFQMYR WAFIPEASDD SGLEVRRQGI HQREFKPYVV RLAKLLRKRA
     KDEEDFKILE GLEMAKHQKN PEEDCSGRTL GWEPGHLLLT LCTMRNMEQL LPFFNVLSQV
     FNSKVTSRCG GHSGSPVLYP NSFPNKDMKL ENHKAFSSKA RQKIEEMIEK DFLEGVIKT
//
ID   LMBL3_MOUSE             Reviewed;         883 AA.
AC   Q8BLB7; Q0VGT0; Q641L7; Q6ZPI2; Q8C0G4;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Lethal(3)malignant brain tumor-like protein 3;
DE            Short=L(3)mbt-like protein 3;
DE   AltName: Full=MBT-1;
GN   Name=L3mbtl3; Synonyms=Mbt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Fetal testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 123-883.
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   DISRUPTION PHENOTYPE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=15889154; DOI=10.1038/sj.emboj.7600654;
RA   Arai S., Miyazaki T.;
RT   "Impaired maturation of myeloid progenitors in mice lacking novel
RT   Polycomb group protein MBT-1.";
RL   EMBO J. 24:1863-1873(2005).
CC   -!- FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins
CC       maintain the transcriptionally repressive state of genes, probably
CC       via a modification of chromatin, rendering it heritably changed in
CC       its expressibility (By similarity). Required for normal maturation
CC       of myeloid progenitor cells.
CC   -!- SUBUNIT: Interacts with RNF2.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BLB7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BLB7-2; Sequence=VSP_013509;
CC       Name=3;
CC         IsoId=Q8BLB7-3; Sequence=VSP_013510, VSP_013511;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Detected in hematopoietic progenitor cells in
CC       fetal liver. Detected in adult bone marrow, heart, brain, spleen,
CC       lung, liver, kidney and testis.
CC   -!- DISRUPTION PHENOTYPE: Death at a late embryonic stage due
CC       defective erythropoiesis, defects in the maturation of other types
CC       of myeloid lineage cells and anemia.
CC   -!- SIMILARITY: Contains 3 MBT repeats.
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
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DR   EMBL; AK031398; BAC27386.1; -; mRNA.
DR   EMBL; AK045667; BAC32449.1; -; mRNA.
DR   EMBL; BC082309; AAH82309.1; -; mRNA.
DR   EMBL; BC085192; AAH85192.1; -; mRNA.
DR   EMBL; AK129443; BAC98253.1; -; mRNA.
DR   IPI; IPI00222779; -.
DR   IPI; IPI00556705; -.
DR   IPI; IPI00556736; -.
DR   RefSeq; NP_766375.1; NM_172787.2.
DR   UniGene; Mm.338439; -.
DR   ProteinModelPortal; Q8BLB7; -.
DR   SMR; Q8BLB7; 232-592, 805-873.
DR   STRING; Q8BLB7; -.
DR   PhosphoSite; Q8BLB7; -.
DR   PRIDE; Q8BLB7; -.
DR   Ensembl; ENSMUST00000040219; ENSMUSP00000037619; ENSMUSG00000039089.
DR   Ensembl; ENSMUST00000105519; ENSMUSP00000101158; ENSMUSG00000039089.
DR   GeneID; 237339; -.
DR   KEGG; mmu:237339; -.
DR   UCSC; uc007esa.1; mouse.
DR   UCSC; uc007esb.1; mouse.
DR   UCSC; uc007esd.1; mouse.
DR   CTD; 237339; -.
DR   MGI; MGI:2143628; L3mbtl3.
DR   HOGENOM; HBG444467; -.
DR   HOVERGEN; HBG071375; -.
DR   InParanoid; Q8BLB7; -.
DR   OMA; FKEYQSF; -.
DR   OrthoDB; EOG41VK2D; -.
DR   PhylomeDB; Q8BLB7; -.
DR   NextBio; 383306; -.
DR   ArrayExpress; Q8BLB7; -.
DR   Bgee; Q8BLB7; -.
DR   CleanEx; MM_L3MBTL3; -.
DR   Genevestigator; Q8BLB7; -.
DR   GermOnline; ENSMUSG00000039089; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR004092; Mbt.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF02820; MBT; 3.
DR   Pfam; PF00536; SAM_1; 1.
DR   SMART; SM00561; MBT; 3.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS51079; MBT; 3.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromatin regulator; Nucleus; Repeat;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    883       Lethal(3)malignant brain tumor-like
FT                                protein 3.
FT                                /FTId=PRO_0000084451.
FT   REPEAT      232    332       MBT 1.
FT   REPEAT      340    439       MBT 2.
FT   REPEAT      448    543       MBT 3.
FT   DOMAIN      811    875       SAM.
FT   COMPBIAS    667    770       Gln/Pro-rich.
FT   VAR_SEQ      72     96       Missing (in isoform 2).
FT                                /FTId=VSP_013509.
FT   VAR_SEQ     290    302       CGYRIKLHFDGYS -> SSALYLFGKRDDG (in
FT                                isoform 3).
FT                                /FTId=VSP_013510.
FT   VAR_SEQ     303    883       Missing (in isoform 3).
FT                                /FTId=VSP_013511.
FT   CONFLICT    146    146       H -> Y (in Ref. 3; BAC98253).
FT   CONFLICT    275    275       P -> H (in Ref. 1; BAC27386).
SQ   SEQUENCE   883 AA;  99137 MW;  7A6417202A0E5532 CRC64;
     MTESASSTSG QEFDVFSVMD WKDGVGTLPG SDLKFRVNEF GALEVITDES EMESVKKATA
     TTTWMVPTAQ DAPTSPPSSR PVFPPAYWTS PPGCPTVFSE KTGVPFRLKE QSKADGLQFC
     ENCCQYGNGD ECLSGGKYCS QNCARHAKDK DQKDERDGGE DNDEEDPKCS RKKKPKLSLK
     ADSKDDGEER DDEMENKQDG RILRGSQRAR RKRRGDSAVL KQGLPPKGKK TWCWASYLEE
     EKAVAVPTKL FKEHQSFPYN KNGFKVGMKL EGVDPDHQAM YCVLTVAEVC GYRIKLHFDG
     YSDCYDFWVN ADALDIHPVG WCEKTGHKLR PPKGYKEEEF NWQSYLKTCK AQAAPKSLFE
     NQNITVIPSG FRVGMKLEAA DKKSPSVICV ATVTDMVDNR FLVHFDNWDE SYDYWCESNS
     PHIHPVGWCK EHRRTLITPP GYSHVKHFSW DKYLEETNSL PAPARAFKVK PPHGFQKKMK
     LEAVDKRNPL FIRVATVADT DDHRIKVHFD GWSSCYDYWI DADSPDIHPV GWCSKTGHPL
     QAPLSPAELM EPSETGGCPT LGCRGVGHFK KSRYLGTQSG ANCPYSEINL SKERIFPDRL
     SGDTSPPTTP SFPRSKRMDT RESSSSPETR EKHANNFKED SEKKKENEVK TSAEAKVVRE
     EPTPSVQQSQ PPQQVQQVQH AQPPQQAQKA PQAQQAQQAQ QAQQAPQAPQ TPQPQQAPQV
     QQAQQAPQAQ QAQQPQQAQQ PQQAPPVQQP QQVQQAQPTQ QQAQTQQQAQ RRSAVFLSFK
     PPIPCLPLRW EQQSKLLPTV AGIPASRVSK WSTDEVSEFI QSLPGCEEHG KVFKDEQIDG
     EAFLLMTQTD IVKIMSIKLG PALKIFNSIL MFKAAEKNSH NEL
//
ID   KS6C1_MOUSE             Reviewed;        1056 AA.
AC   Q8BLK9; Q3UDY3; Q6PDY4; Q8BMQ5; Q8BX49;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Ribosomal protein S6 kinase delta-1;
DE            Short=S6K-delta-1;
DE            EC=2.7.11.1;
DE   AltName: Full=52 kDa ribosomal protein S6 kinase;
GN   Name=Rps6kc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 284-1056 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Cerebellum, Ovary, and Uterus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 436-1056 (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Cerebellum;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-577, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423 AND SER-634, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May be involved in transmitting sphingosine-1 phosphate
CC       (SPP)-mediated signaling into the cell (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts with SPHK1 and phosphatidylinositol 3-phosphate
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane. Note=Also found in some
CC       small dot-like or ring-shaped early endosome structures (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8BLK9-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q8BLK9-2; Sequence=VSP_018043, VSP_018044, VSP_018050,
CC                                  VSP_018051;
CC         Note=Due to a partial intron retention. No experimental
CC         confirmation available;
CC       Name=3;
CC         IsoId=Q8BLK9-3; Sequence=VSP_018046, VSP_018048, VSP_018049;
CC         Note=Due to a partial intron retention. No experimental
CC         confirmation available;
CC       Name=4;
CC         IsoId=Q8BLK9-4; Sequence=VSP_018045, VSP_018047;
CC         Note=May be produced at very low levels due to a premature stop
CC         codon in the mRNA, leading to nonsense-mediated mRNA decay. No
CC         experimental confirmation available;
CC   -!- DOMAIN: The first protein kinase domain appears to be a
CC       pseudokinase domain as it does not contain the classical
CC       characteristics, such as the ATP-binding motif, ATP-binding site
CC       and active site.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. S6 kinase subfamily.
CC   -!- SIMILARITY: Contains 1 MIT domain.
CC   -!- SIMILARITY: Contains 2 protein kinase domains.
CC   -!- SIMILARITY: Contains 1 PX (phox homology) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC33510.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; AK030313; BAC26894.1; -; mRNA.
DR   EMBL; AK044809; BAC32101.1; -; mRNA.
DR   EMBL; AK049003; BAC33510.1; ALT_INIT; mRNA.
DR   EMBL; AK149858; BAE29128.1; -; mRNA.
DR   EMBL; BC058403; AAH58403.1; -; mRNA.
DR   IPI; IPI00223078; -.
DR   IPI; IPI00268901; -.
DR   IPI; IPI00308854; -.
DR   IPI; IPI00750491; -.
DR   RefSeq; NP_848890.3; NM_178775.4.
DR   UniGene; Mm.220912; -.
DR   ProteinModelPortal; Q8BLK9; -.
DR   SMR; Q8BLK9; 14-126, 235-309, 850-1055.
DR   PhosphoSite; Q8BLK9; -.
DR   PRIDE; Q8BLK9; -.
DR   Ensembl; ENSMUST00000056178; ENSMUSP00000055339; ENSMUSG00000089872.
DR   Ensembl; ENSMUST00000061611; ENSMUSP00000061769; ENSMUSG00000089872.
DR   Ensembl; ENSMUST00000062296; ENSMUSP00000053088; ENSMUSG00000037581.
DR   Ensembl; ENSMUST00000097440; ENSMUSP00000095049; ENSMUSG00000089872.
DR   GeneID; 320119; -.
DR   KEGG; mmu:320119; -.
DR   UCSC; uc007ebh.1; mouse.
DR   UCSC; uc007ebi.1; mouse.
DR   CTD; 320119; -.
DR   MGI; MGI:2443419; Rps6kc1.
DR   eggNOG; roNOG07933; -.
DR   GeneTree; ENSGT00530000063268; -.
DR   HOGENOM; HBG713813; -.
DR   HOVERGEN; HBG078266; -.
DR   InParanoid; Q8BLK9; -.
DR   OrthoDB; EOG4TXBR9; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 396068; -.
DR   ArrayExpress; Q8BLK9; -.
DR   Bgee; Q8BLK9; -.
DR   CleanEx; MM_RPS6KC1; -.
DR   Genevestigator; Q8BLK9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR007330; MIT.
DR   InterPro; IPR001683; Phox.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   Gene3D; G3DSA:3.30.1520.10; PX; 1.
DR   Pfam; PF04212; MIT; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00745; MIT; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF64268; PX; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG.
DR   PROSITE; PS50195; PX; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Repeat;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1   1056       Ribosomal protein S6 kinase delta-1.
FT                                /FTId=PRO_0000233128.
FT   DOMAIN        8    132       PX.
FT   DOMAIN      276    304       MIT.
FT   DOMAIN      343    444       Protein kinase 1.
FT   DOMAIN      789   1046       Protein kinase 2.
FT   NP_BIND     795    803       ATP (By similarity).
FT   ACT_SITE    919    919       Proton acceptor (By similarity).
FT   BINDING     823    823       ATP (By similarity).
FT   MOD_RES     422    422       Phosphoserine (By similarity).
FT   MOD_RES     423    423       Phosphoserine.
FT   MOD_RES     426    426       Phosphoserine (By similarity).
FT   MOD_RES     577    577       Phosphoserine.
FT   MOD_RES     634    634       Phosphoserine.
FT   VAR_SEQ      36     47       Missing (in isoform 2).
FT                                /FTId=VSP_018043.
FT   VAR_SEQ      89    158       Missing (in isoform 2).
FT                                /FTId=VSP_018044.
FT   VAR_SEQ     279    336       ESSPTRREAVKRRTAEYLMRAESICSLRAAPQLHTGPQPPG
FT                                SLSSRPPWSLRSPAEEL -> KVRQCHHWLESLGSLQKSER
FT                                NLEKPSHTRAQQDIASPLVTKITKSHHLIICRSVHSSK
FT                                (in isoform 4).
FT                                /FTId=VSP_018045.
FT   VAR_SEQ     317    347       Missing (in isoform 3).
FT                                /FTId=VSP_018046.
FT   VAR_SEQ     337   1056       Missing (in isoform 4).
FT                                /FTId=VSP_018047.
FT   VAR_SEQ     932    947       HIQLTYFSRWSEVEDS -> QELSQMHFFLFAVASN (in
FT                                isoform 3).
FT                                /FTId=VSP_018048.
FT   VAR_SEQ     948   1056       Missing (in isoform 3).
FT                                /FTId=VSP_018049.
FT   VAR_SEQ     961    961       E -> G (in isoform 2).
FT                                /FTId=VSP_018050.
FT   VAR_SEQ     962   1056       Missing (in isoform 2).
FT                                /FTId=VSP_018051.
FT   CONFLICT    855    857       GSE -> DSD (in Ref. 2; AAH58403).
FT   CONFLICT    855    855       G -> D (in Ref. 1; BAC33510).
SQ   SEQUENCE   1056 AA;  115712 MW;  315E6BB9926E4F42 CRC64;
     MTSPWGHSAD LARFYTVTEP QRHPRGYTVY KVTARVVSRR NPEDVQEIIV WRRYSDFKKL
     HRELWQIHRN AFRHSELFPP FAKGTVFGRF DKTVIEERRQ CAEDLLQFSA NIPALYNSRQ
     LQDFFKGGVI SDGSELIGPA EAYPDSPANA FPECGTEGFS SDSDLLSLTV DADSLAEVDD
     GMASRQGSPS RTFGLSLSTD SSAVGAVASD SEPSRVEDRE SRSLFPSSLK PRLGRRDYLE
     KAGELIKLAL KKEEEDDYEA ASDFYRKGVD LLLEGVQGES SPTRREAVKR RTAEYLMRAE
     SICSLRAAPQ LHTGPQPPGS LSSRPPWSLR SPAEELKAFR VLGVIDKVLL VMDTRTEQTF
     ILKGLRKSSE CSRNRKTIIP RCVPNMVCLH TYIISEESVF LVLQRAEGGK LWSYISKFLN
     RSSQESLDIK EGRPSMPPRV CLQQPSASPQ GGSSFESRGS DTGSMLKALP LKTSLTPSSQ
     DDSNQEDDGQ PSSPKWLDSG SSSEDECTAG YLTLCNEYGQ EKMDLVSLSE ESVMQPEGDK
     ADTQAVSSPA SLATGSVSPS THLRVFSGGE DLEAVSSPPT SESLSRSKNS PMEFFRIDSK
     DSTSELLGLD FGEKLHSLKP EPLKALFTLE DGDSPSQSLD PGESKRESEA QDSVSRGSDD
     SVPVISFKEA AAEAISGAEE GRPDLLVNLP GELQPTKEAS AMDPKFSQAS AGRLDSKLLE
     APDVLCLRLS SEQCHGLGPE GPEELSDPTE FCPGGVIPEH DAQADPGVLF EAAVDHRSSP
     DQFLFSSLRS ESDRLGQVEV VVTAQALQES LFHISSPCSG ANKEHSAYAD TATSEEVLLF
     TEPTKEEANS LFQRGSEAQE RGVGAGEADK EIHQIFEDLD KRLAASSRFF IPEGCIQRWA
     AEMVVALDAL HREGIVCRDL NPNNILLNDG GHIQLTYFSR WSEVEDSCDS DAVARMYCAP
     EVGAVTEETE ACDWWSLGAV LFELLTGKTL VECHPAGINT HTTLNMPGCV SEEARSLIQQ
     LLQFNPMERL GAGVAGVEDI KSHPFFTPVD WAELTR
//
ID   UNC80_MOUSE             Reviewed;        3261 AA.
AC   Q8BLN6; B2KGE8; B2KGG4; Q69Z93; Q8BJN5; Q8BLP6;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 2.
DT   08-FEB-2011, entry version 50.
DE   RecName: Full=Protein unc-80 homolog;
DE            Short=mUNC-80;
GN   Name=Unc80; Synonyms=Kiaa1843;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-408.
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1783-3261.
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   FUNCTION, INTERACTION WITH NALCN AND UNC79, PHOSPHORYLATION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=19092807; DOI=10.1038/nature07579;
RA   Lu B., Su Y., Das S., Wang H., Wang Y., Liu J., Ren D.;
RT   "Peptide neurotransmitters activate a cation channel complex of NALCN
RT   and UNC-80.";
RL   Nature 457:741-744(2009).
CC   -!- FUNCTION: Component of the NALCN sodium channel complex, a cation
CC       channel activated either by neuropeptides substance P or
CC       neurotensin that controls neuronal excitability.
CC   -!- SUBUNIT: Interacts with NALCN and UNC79/KIAA1409.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BLN6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BLN6-2; Sequence=VSP_015007, VSP_015008;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in hippocampus and ventral tegmental
CC       area neurons.
CC   -!- PTM: Phosphorylated on tyrosine residues.
CC   -!- SIMILARITY: Belongs to the unc-80 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC31737.1; Type=Frameshift; Positions=387;
CC       Sequence=CAQ52181.1; Type=Erroneous gene model prediction;
CC       Sequence=CAQ52182.1; Type=Erroneous gene model prediction;
CC       Sequence=CAQ52184.1; Type=Erroneous gene model prediction;
CC       Sequence=CAQ52219.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK043914; BAC31702.1; -; mRNA.
DR   EMBL; AK044008; BAC31737.1; ALT_FRAME; mRNA.
DR   EMBL; AK081235; BAC38173.1; -; mRNA.
DR   EMBL; CU442760; CAQ52181.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CU329676; CAQ52181.1; JOINED; Genomic_DNA.
DR   EMBL; CU442760; CAQ52182.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CU392848; CAQ52182.1; JOINED; Genomic_DNA.
DR   EMBL; CU329676; CAQ52184.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CU442760; CAQ52184.1; JOINED; Genomic_DNA.
DR   EMBL; CU392848; CAQ52219.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CU442760; CAQ52219.1; JOINED; Genomic_DNA.
DR   EMBL; AK173273; BAD32551.1; -; mRNA.
DR   IPI; IPI00775839; -.
DR   IPI; IPI00856133; -.
DR   RefSeq; NP_780719.2; NM_175510.3.
DR   UniGene; Mm.44798; -.
DR   PRIDE; Q8BLN6; -.
DR   Ensembl; ENSMUST00000061620; ENSMUSP00000053692; ENSMUSG00000055567.
DR   Ensembl; ENSMUST00000114008; ENSMUSP00000109641; ENSMUSG00000055567.
DR   GeneID; 329178; -.
DR   KEGG; mmu:329178; -.
DR   UCSC; uc007bif.1; mouse.
DR   CTD; 329178; -.
DR   MGI; MGI:2652882; Unc80.
DR   eggNOG; roNOG04769; -.
DR   GeneTree; ENSGT00510000048023; -.
DR   HOVERGEN; HBG108650; -.
DR   InParanoid; Q8BLN6; -.
DR   ArrayExpress; Q8BLN6; -.
DR   Bgee; Q8BLN6; -.
DR   CleanEx; MM_C030018G13RIK; -.
DR   Genevestigator; Q8BLN6; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Alternative splicing; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   3261       Protein unc-80 homolog.
FT                                /FTId=PRO_0000089349.
FT   TRANSMEM   2271   2291       Helical; (Potential).
FT   TRANSMEM   2401   2421       Helical; (Potential).
FT   TRANSMEM   2788   2808       Helical; (Potential).
FT   TRANSMEM   2834   2854       Helical; (Potential).
FT   COMPBIAS    729    769       Gly-rich.
FT   VAR_SEQ     268    273       GLQVVS -> VSLLCL (in isoform 2).
FT                                /FTId=VSP_015007.
FT   VAR_SEQ     274   3261       Missing (in isoform 2).
FT                                /FTId=VSP_015008.
FT   CONFLICT   3251   3251       E -> D (in Ref. 3; BAD32551).
SQ   SEQUENCE   3261 AA;  363504 MW;  919D51BBA67225C0 CRC64;
     MVKRKSSEGQ EQDGGRGIPL PIQTFLWRQT SAFLRPKLGK QYEASCVSFE RVLVENKLHG
     LSPALSEAIQ SISRWELVQA ALPHVLHCTA TLLSNRNKLG HQDKLGVAET KLLHTLHWML
     LEAPQDCNND QFGGTDRGSS WGGSSSAFIH QIENQGSPGQ PCRSSSHDEE ENNRRKTFQN
     SMATVELFVF LFAPLVHRIK ESDLTFRLAS GLVIWQPMWE HRQPEVSGFT ALVKPIRNII
     TAKRSSPINS QSQTCESPNQ DTRQQGEGLQ VVSEALQSDS ISPKATISGC HQGNSFDGSL
     SSQTSQERGP SHSRASLVIP PCQRSRYATY FDVAVLRCLL QPHWSEEGTQ WSLMYYLQRL
     RHMLEEKPEK TPDPDIPLLP RPRSSSMVAA APSLVNTHKT QDLTMKCNEE EKSLSPEAFS
     KVSLTNLRRS AVPDLSSDLG MNIFKKFKSR KEDRERKGSI PFHHTGKRRP RRMGVPFLLH
     EDHLDVSPTR STFSFGSFSG LGEDRRGIEK GGWQTTILGK LTRRGSSDAA TEMESLSARH
     SHSHHTLVSD LPDHSNSHGE NTVKEVRSQI STITVATFNT TLASFNVGYA DFFSEHMRKL
     CSQVPIPEMP HEPLACANLP RSLTDSCINY SYLEDTEHID GTNNFVHKNG MLDLSVVLKA
     VYLVLNHDIS SRICDVALNI VECLLQLGVV PCVEKNRKKS ENKENESVEK RPSEGAFQFK
     GVSSSSTSGF GAPSASGAGD GGGEEGGGGD GGGGGGGGDG GGGGGGGGGP YEKNEKNQEK
     DDNIPVSNHR LALTMLIKIV KSLGCAYGCG EGHRGLSGDR LRHQVFRENA QNCLTKLYKL
     DKIQFRQTMR DYVNKDSLNN VVDFLHALLG FCMEPVTDNK AGFGNNFTTV DNKSTAQNVE
     GIIVGAMFKS LITRCASTTH ELHSPENLGL YCDIRQLVQF IKEAHGNVFR RVALSALLDS
     AEKLAPGKKV EENGQESKPV GSKRSEAGSI ADKGQVSSAP EECRSFMSGR PSQTPEHDEP
     MQGGNLGRKD FWRKMFKSQS AASDTSSQSE QDTSECTTAH SGNTSDRRAR SRSRRISLRK
     KLKLPIGKRN WLKRSSLSGL ADGVEDLLDI SSVDRLSFIR QSSKVKFTSA VKLSEGGPGS
     GMENGREEEE NFFKRLGCHS FDDHLSPNQD GGKSKNVVNL GAIRQGMKRF QFLLNCCEPG
     TIPDASILAA ALDLEAPVVA RAALFLECAR FVHRCNRGNW PEWMKGHHVN ITKKGLSRGR
     SPTVGNKRNQ KLQWSAAKLF YQWGDAIGIR LNELCHGESE SPANLLGLIY DEETKRRLRK
     EDEEEDFLDD STVNPSKCGC PFALKMAACQ LLLEITTFLR ETFSCLPRPR TEPLVDLESC
     RLRLDPELDR HRYERKISFA GVLDENEDSK DSLHSSSHTI KSDAGAEEKK EGSPWSASEP
     SIEPEGLSNA GTEENYHRNM SWLHVMILLC NQQSFICTHV DYCHPHCYLH HSRSCARLVR
     AIKLLYGDSV DSLRESNHIS NVALRGKKQK ECSDKSCLRT PSLKKRVSDV NLEGKKDSGM
     LKYIRFQVMS LSPAPLSLLI KAAPILTEEM YGDIQPAAWE LLLSMDEHMA GAAAAMFLLC
     AVKVPDAVSD MLMSEFHHAE TVQRLNAVLK FHTLWRFRYQ VWPRMEEGAQ QIFKIPPPSI
     NFTLPSPVLG MPSVPMFDPP WVPQCSGSVQ DPINEDQSKS FSARAVSRSH QRAEHILKNL
     QQEEEKKRLG REASLITAIP ITQEACYEPT CTPNSEPEEE VEEVANLTSR RLSVSPSCTS
     STSHRNYSFR RGSVWSVRSA VSAEDEEHAT EHTPNHHVPQ PPQAVFPACI CAAVLPIVHL
     MEDGEVREDG VAVSAVAQQV LWNCLIEDPS TVLRHFLEKL TISNRQDELM YMLRKLLLNI
     GDFPAQTSHI LFNYLVGLIM YFVRTPCEWG MDAISATLTF LWEVVGYVEG LFFKDLKQTM
     KKEQCEVKLL VTASMPGTKT LVVHGQNECD IPTQLPVHED TQFEALLKEC LEFFNIPESQ
     STHYFLMDKR WNLIHYNKTY VRDIYPFRRS VSPQLNLVHM HPEKGQELIQ KQVFTRKLEE
     VGRVLFLISL TQKIPTAHKQ SHVSMLQEDL LRLPSFPRSA IDAEFSLFSD PQAGKELFGL
     DTLQKSLWIQ LLEEMFLGMP SEFPWGDEIM LFLNVFNGAL ILHPEDSALL RQYAATVINT
     AVHFNHLFSL SGYQWILPTM LQVYSDYESN PQLRRAIEFA CHQFYILHRK PFVLQLFASV
     APLLEFPDAA NTGSSKGVSA QCLFDLLQSL EGETTDILDI LELVKAEKPL KSLDFCYGNE
     DLTFSISEAI KLCVTVVAYA PESFRSLQML MVLEALVPCY LQKMKRQTSQ VETVPAAREE
     IAATAALATS LQALLYSVEV LTRPMTAPQM SRSDQGHKGT TTANHTMSSG VNTRYPEQGA
     KLHFIRENLH LLEEGQGLPR EELDERISRE EFRRPRESLL NICTEFYKHC GPRLKILQNL
     AGEPRVTALE LLDVKSHMRL AEIAHSLLKL APYDTQTMES RGLRRYIMEM LPITDWSAEA
     VRPALILILK RLDRMFNKIH KMPTLRRQVE WEPASSLIEG VCLTLQRQPI ISFLPHLRSL
     INVCVNLVMG VVGPSSVADG LPLLHLSPYL SPPLPFSTAV VRLVALQIQA LKEDFPLSHV
     ISPFTNQERR EGMLLNLLIP FVLTVGSGSK DSPWLEQPEV QLLLQTVINV LLPPRIISTS
     RSKNFMLESS PAHCSTPGDA GKDLRKEGLA ESTSQAAYLA LKVILVCFER QLGSQWYWLS
     LQVKEMALRK VGGLALWDFL DFIVRTRIPI FVLLRPFIQC KLLAQPAENH EELSARQHIS
     DQLERRFIPR PLCKSSLIAE FNSELKILKE AVHSGSAYQG KTSISTVGTS TSAYRLSLAT
     MSRSNTGTGT VWEQDSEPSQ QASQDTLSRT DEEDEENDSV SMPSVVSEQE ACLLSTIGRR
     RFSSHVSSMS APQAEVGMLP SQSEPNVLDD SQGLAAEGSL SRVASIQSEP GQQNVLLQQP
     LGRKRGLRQL RRPLLSRQKT QTEPRNRHGA RLSTTRRSIQ PKTKPSVDQK RSVTFIEAQP
     EPTAAPTDIF PATGQPQSCS PGRARKPEGT EKPVLTSSPA IIIADLHSLS PKQSEPLLAE
     EGEKKEDEEI QGATAHCPLS TQLSDPDDFT GLETSSLLQH GDTVLHISEE NGTENPLLSS
     QFTFTPPELG ETDSALDESH V
//
ID   CADM2_MOUSE             Reviewed;         435 AA.
AC   Q8BLQ9; B1B1A5; B1B1A6; B2RTL0; Q8BXJ7; Q8BYP1; Q8BZP4;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Cell adhesion molecule 2;
DE   AltName: Full=Immunoglobulin superfamily member 4D;
DE            Short=IgSF4D;
DE   AltName: Full=Nectin-like protein 3;
DE            Short=NECL-3;
DE   Flags: Precursor;
GN   Name=Cadm2; Synonyms=Igsf4d, Necl3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain cortex, Diencephalon, Hypothalamus, and
RC   Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BLQ9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BLQ9-2; Sequence=VSP_026336, VSP_026337;
CC       Name=3;
CC         IsoId=Q8BLQ9-3; Sequence=VSP_026337;
CC   -!- SIMILARITY: Belongs to the nectin family.
CC   -!- SIMILARITY: Contains 2 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC       domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK038842; BAC30148.1; -; mRNA.
DR   EMBL; AK046800; BAC32876.1; -; mRNA.
DR   EMBL; AK033973; BAC28533.1; -; mRNA.
DR   EMBL; AK043760; BAC31646.1; -; mRNA.
DR   EMBL; AC154674; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CT010571; CAP19089.1; -; Genomic_DNA.
DR   EMBL; AC105980; CAP19089.1; JOINED; Genomic_DNA.
DR   EMBL; AC109233; CAP19089.1; JOINED; Genomic_DNA.
DR   EMBL; AC154428; CAP19089.1; JOINED; Genomic_DNA.
DR   EMBL; CT010571; CAP19090.1; -; Genomic_DNA.
DR   EMBL; AC105980; CAP19090.1; JOINED; Genomic_DNA.
DR   EMBL; AC109233; CAP19090.1; JOINED; Genomic_DNA.
DR   EMBL; AC154196; CAP19090.1; JOINED; Genomic_DNA.
DR   EMBL; AC154428; CAP19090.1; JOINED; Genomic_DNA.
DR   EMBL; BC139401; AAI39402.1; -; mRNA.
DR   EMBL; BC139402; AAI39403.1; -; mRNA.
DR   IPI; IPI00453537; -.
DR   IPI; IPI00850457; -.
DR   IPI; IPI00850833; -.
DR   RefSeq; NP_001139449.1; NM_001145977.1.
DR   RefSeq; NP_848836.2; NM_178721.4.
DR   UniGene; Mm.394300; -.
DR   PDB; 3M45; X-ray; 2.21 A; A/B/C/D=26-124.
DR   PDBsum; 3M45; -.
DR   ProteinModelPortal; Q8BLQ9; -.
DR   SMR; Q8BLQ9; 24-422.
DR   STRING; Q8BLQ9; -.
DR   PRIDE; Q8BLQ9; -.
DR   Ensembl; ENSMUST00000120594; ENSMUSP00000113500; ENSMUSG00000064115.
DR   GeneID; 239857; -.
DR   KEGG; mmu:239857; -.
DR   UCSC; uc007zqn.1; mouse.
DR   CTD; 239857; -.
DR   MGI; MGI:2442722; Cadm2.
DR   GeneTree; ENSGT00600000084002; -.
DR   HOGENOM; HBG402945; -.
DR   HOVERGEN; HBG057086; -.
DR   InParanoid; Q8BLQ9; -.
DR   OMA; GTANLTC; -.
DR   NextBio; 384323; -.
DR   ArrayExpress; Q8BLQ9; -.
DR   Bgee; Q8BLQ9; -.
DR   CleanEx; MM_CADM2; -.
DR   Genevestigator; Q8BLQ9; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   InterPro; IPR013162; CD80_C2-set.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR003585; Neurexin-like.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3.
DR   Pfam; PF08205; C2-set_2; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00294; 4.1m; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   PROSITE; PS50835; IG_LIKE; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25    435       Cell adhesion molecule 2.
FT                                /FTId=PRO_0000291971.
FT   TOPO_DOM     25    367       Extracellular (Potential).
FT   TRANSMEM    368    388       Helical; (Potential).
FT   TOPO_DOM    389    435       Cytoplasmic (Potential).
FT   DOMAIN       27    119       Ig-like V-type.
FT   DOMAIN      127    219       Ig-like C2-type 1.
FT   DOMAIN      227    312       Ig-like C2-type 2.
FT   COMPBIAS    343    352       Poly-Ser.
FT   CARBOHYD     31     31       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     51     51       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    291    291       N-linked (GlcNAc...) (Potential).
FT   DISULFID     44    104       By similarity.
FT   DISULFID    146    203       By similarity.
FT   DISULFID    248    296       By similarity.
FT   VAR_SEQ      20     20       Q -> QAAASKSKVK (in isoform 2).
FT                                /FTId=VSP_026336.
FT   VAR_SEQ     315    354       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_026337.
FT   CONFLICT    297    297       E -> K (in Ref. 1; BAC30148).
FT   CONFLICT    308    308       E -> K (in Ref. 1; BAC28533).
SQ   SEQUENCE   435 AA;  47559 MW;  B5F4AB448B2EA5E1 CRC64;
     MIWKRSAVLR FYSVCGLLLQ GSQGQFPLTQ NVTVVEGGTA ILTCRVDQND NTSLQWSNPA
     QQTLYFDDKK ALRDNRIELV RASWHELSIS VSDVSLSDEG QYTCSLFTMP VKTSKAYLTV
     LGVPEKPQIS GFSSPVMEGD LMQLTCKTSG SKPAADIRWF KNDKEIKDVK YLKEEDANRK
     TFTVSSTLDF RVDRSDDGVA VICRVDHESL NATPQVAMQV LEIHYTPSVK IIPSTPFPQE
     GQALTLTCES KGKPLPEPVL WTKDGAELPD PDRMVVSGRE LNILFLNKTD NGTYRCEATN
     TIGQSSAEYV LIVHDVPNTL LPTTIIPSLT TAPVTTSVTI TTSPSTSASS SSRRDPNSLA
     GQNGPDHALI GGIVAVVVFV TLCSIFLLGR YLARHKGTYL TNEAKGAEDA PDADTAIINA
     EGSQVNAEEK KEYFI
//
ID   ANR43_MOUSE             Reviewed;         548 AA.
AC   Q8BLS7; Q149C7;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Ankyrin repeat domain-containing protein 43;
DE   Flags: Precursor;
GN   Name=Ankrd43;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 126-548.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 2 ANK repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI17864.1; Type=Erroneous initiation;
CC       Sequence=BAC31573.1; Type=Frameshift; Positions=100, 122;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK043538; BAC31573.1; ALT_FRAME; mRNA.
DR   EMBL; AL596095; CAI24354.2; -; Genomic_DNA.
DR   EMBL; BC117863; AAI17864.1; ALT_INIT; mRNA.
DR   IPI; IPI00222893; -.
DR   RefSeq; NP_898996.2; NM_183173.2.
DR   UniGene; Mm.145208; -.
DR   ProteinModelPortal; Q8BLS7; -.
DR   SMR; Q8BLS7; 317-469.
DR   STRING; Q8BLS7; -.
DR   PhosphoSite; Q8BLS7; -.
DR   PRIDE; Q8BLS7; -.
DR   Ensembl; ENSMUST00000104955; ENSMUSP00000100561; ENSMUSG00000044352.
DR   GeneID; 237761; -.
DR   KEGG; mmu:237761; -.
DR   CTD; 237761; -.
DR   MGI; MGI:2687280; Ankrd43.
DR   eggNOG; roNOG05304; -.
DR   GeneTree; ENSGT00530000063547; -.
DR   HOGENOM; HBG282235; -.
DR   HOVERGEN; HBG100446; -.
DR   InParanoid; Q8BLS7; -.
DR   OMA; DRFKQFV; -.
DR   OrthoDB; EOG4T1HN2; -.
DR   NextBio; 383474; -.
DR   ArrayExpress; Q8BLS7; -.
DR   Bgee; Q8BLS7; -.
DR   CleanEx; MM_ANKRD43; -.
DR   Genevestigator; Q8BLS7; -.
DR   GermOnline; ENSMUSG00000044352; Mus musculus.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 1.
DR   SMART; SM00248; ANK; 2.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; ANK repeat; Repeat; Signal.
FT   INIT_MET      1      1       Removed (By similarity).
FT   SIGNAL        2     19       Potential.
FT   CHAIN        20    548       Ankyrin repeat domain-containing protein
FT                                43.
FT                                /FTId=PRO_0000244374.
FT   REPEAT      344    373       ANK 1.
FT   REPEAT      383    413       ANK 2.
FT   COMPBIAS      2     20       Ala-rich.
FT   COMPBIAS     85    225       Pro-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   CONFLICT    173    173       L -> V (in Ref. 1; BAC31573).
FT   CONFLICT    244    244       E -> K (in Ref. 3; AAI17864).
SQ   SEQUENCE   548 AA;  57749 MW;  BBE9044230D01D15 CRC64;
     MALAAAAAAA AAAAGVSQAA VLGFLREHGG QVRNSELLSR FKPLLDAGDP RGRAARRDRF
     KQFVNNVAVV KELDGVKFVV LRKKPRPPEG PEAPLPSSPG VPAALAQCAA VPAEDNCAPG
     APHSPQRSGE PPEDSSAPSE LQHTPETLPS EVTQVEAPSG SAPQPGGPED PALPRSSELA
     RPASVPSGLA LTSTESPGPE PAPPTAQVPP QKPCMLPVRC VVPGPAALRI RAEEQGLRRQ
     RSEEPSPRGS PMLLRRLSVE ESGLGLHLGP GRSPHLRRLS RAGPRLLSPD TEEMPVAPLP
     SPAVPLEPTE HEWLVRTASG RWSHQLHGLL LRDRGLAAKR DFMSGFTALH WAAKNGDREM
     ALQLVEVARR GGAPVDVNAR SHGGYTPLHL AALHGHEDAA VLLVVRLGAQ VHVRDYSGRR
     AYQYLRPGSS YALRRLLGDP GLRSMMEPDA ASGGSGSLVS RHPVQVAATI LSSTTSAFLG
     VLADDLMLQD LARGLKKSSS FSKFLGASPM APRKKTKIRG GLPSFTEISH RSTPGPLAGL
     VPSLPPPT
//
ID   SL9A7_MOUSE             Reviewed;         726 AA.
AC   Q8BLV3; A2ACD5; A2ACD6;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Sodium/hydrogen exchanger 7;
DE   AltName: Full=Na(+)/H(+) exchanger 7;
DE            Short=NHE-7;
DE   AltName: Full=Solute carrier family 9 member 7;
GN   Name=Slc9a7; Synonyms=Nhe7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Mediates electroneutral exchange of protons for Na(+)
CC       and K(+) across endomembranes. May contribute to Golgi volume and
CC       cation homeostasis (By similarity).
CC   -!- SUBUNIT: Interacts with SCAMP1, SCAMP2 and SCAMP5; may participate
CC       in its shuttling from trans-Golgi network to recycling endosomes
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC       membrane; Multi-pass membrane protein (By similarity). Recycling
CC       endosome membrane; Multi-pass membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BLV3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BLV3-2; Sequence=VSP_009498, VSP_009499;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1
CC       (CPA1) transporter (TC 2.A.36) family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK041169; BAC30848.1; -; mRNA.
DR   EMBL; AL663098; CAM18655.1; -; Genomic_DNA.
DR   EMBL; AL663098; CAM18656.1; -; Genomic_DNA.
DR   EMBL; BC058750; AAH58750.1; -; mRNA.
DR   IPI; IPI00222921; -.
DR   IPI; IPI00403540; -.
DR   RefSeq; NP_796327.1; NM_177353.3.
DR   UniGene; Mm.132983; -.
DR   ProteinModelPortal; Q8BLV3; -.
DR   SMR; Q8BLV3; 275-300, 369-395.
DR   STRING; Q8BLV3; -.
DR   PhosphoSite; Q8BLV3; -.
DR   PRIDE; Q8BLV3; -.
DR   Ensembl; ENSMUST00000072451; ENSMUSP00000072274; ENSMUSG00000037341.
DR   Ensembl; ENSMUST00000115393; ENSMUSP00000111051; ENSMUSG00000037341.
DR   GeneID; 236727; -.
DR   KEGG; mmu:236727; -.
DR   UCSC; uc009sst.1; mouse.
DR   CTD; 236727; -.
DR   MGI; MGI:2444530; Slc9a7.
DR   GeneTree; ENSGT00560000076802; -.
DR   HOGENOM; HBG443570; -.
DR   HOVERGEN; HBG055575; -.
DR   InParanoid; Q8BLV3; -.
DR   OMA; TRLVFPL; -.
DR   OrthoDB; EOG4J9MZD; -.
DR   PhylomeDB; Q8BLV3; -.
DR   NextBio; 383043; -.
DR   ArrayExpress; Q8BLV3; -.
DR   Bgee; Q8BLV3; -.
DR   Genevestigator; Q8BLV3; -.
DR   GO; GO:0016021; C:integral to membrane; ISS:UniProtKB.
DR   GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR   GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR   GO; GO:0015386; F:potassium:hydrogen antiporter activity; ISS:UniProtKB.
DR   GO; GO:0015385; F:sodium:hydrogen antiporter activity; ISS:UniProtKB.
DR   GO; GO:0006885; P:regulation of pH; ISS:UniProtKB.
DR   InterPro; IPR006153; Cation/H_exchanger.
DR   InterPro; IPR018422; Cation/H_exchanger_CPA1.
DR   InterPro; IPR002090; Na/H_exchanger_6.
DR   InterPro; IPR004709; NaH_exchanger.
DR   PANTHER; PTHR10110; Cation/H_exchanger_cons-reg; 1.
DR   Pfam; PF00999; Na_H_Exchanger; 1.
DR   PRINTS; PR01084; NAHEXCHNGR.
DR   PRINTS; PR01088; NAHEXCHNGR6.
DR   TIGRFAMs; TIGR00840; b_cpa1; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Antiport; Endosome; Golgi apparatus;
KW   Ion transport; Membrane; Phosphoprotein; Potassium;
KW   Potassium transport; Sodium; Sodium transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    726       Sodium/hydrogen exchanger 7.
FT                                /FTId=PRO_0000052364.
FT   TRANSMEM     71     91       Helical; (Potential).
FT   TRANSMEM     96    116       Helical; (Potential).
FT   TRANSMEM    176    196       Helical; (Potential).
FT   TRANSMEM    211    231       Helical; (Potential).
FT   TRANSMEM    252    272       Helical; (Potential).
FT   TRANSMEM    278    298       Helical; (Potential).
FT   TRANSMEM    324    344       Helical; (Potential).
FT   TRANSMEM    351    371       Helical; (Potential).
FT   TRANSMEM    373    393       Helical; (Potential).
FT   TRANSMEM    416    436       Helical; (Potential).
FT   TRANSMEM    444    464       Helical; (Potential).
FT   TRANSMEM    515    535       Helical; (Potential).
FT   TRANSMEM    613    633       Helical; (Potential).
FT   MOD_RES     696    696       Phosphoserine (By similarity).
FT   VAR_SEQ     540    548       VGVEELSEE -> YRFWNMIDR (in isoform 2).
FT                                /FTId=VSP_009498.
FT   VAR_SEQ     549    726       Missing (in isoform 2).
FT                                /FTId=VSP_009499.
FT   CONFLICT     46     46       A -> E (in Ref. 3; AAH58750).
SQ   SEQUENCE   726 AA;  80289 MW;  852266CCEC363B9C CRC64;
     MEPSDAARPG PGRAFRGLSP RLLLLPLLPV LLGRGLRAGA AASSGAAAED SSAMEELATE
     KEAEESHRQD SVSLLTFILL LTLTILTIWL FKHRRVRFLH ETGLAMIYGL IVGVILRYGT
     PATSGHDKSL SCTQEDRAFS TLLVNVSGKF FEYTLKGEIS PGKINNVEQN DMLRKVTFDP
     EVFFNILLPP IIFHAGYSLK KRHFFRNLGS ILAYAFLGTA VSCFIIGNLM YGVVKLMKIV
     GQLSDKFYYT DCLFFGAIIS ATDPVTVLAI FNELHADVDL YALLFGESVL NDAVAIVLSS
     SIVAYQPAGL NTHAFDAAAF FKSVGIFLGI FSGSFTMGAV TGVVTALVTK FTKLHCFPLL
     ETALFFLMSW STFLLAEACG FTGVVAVLFC GITQAHYTYN NLSVESRSRS KQLFEVLHFL
     AENFIFSYMG LALFTFQKHV FSPIFIIGAF VAIFLGRAAH IYPLSFFLNL GRRHKIGWNF
     QHMMMFSGLR GAMAFALAIR DTASYARQMM FTTTLLIVFF TVWVIGGGTT PMLSWLNIRV
     GVEELSEEDQ NENRWQYFRV GVDPDQDPPP NNDSFQVLQG DGMDSVGGSR TKQESAWIFR
     LWYIFDHNYL KPILTHSGPP LTTTLPAWCG LLARCLTSPQ VYDNQEPLRE DDSDFILTEG
     DLTLTYGDST VTANGSSSSY TASTSLECGR RTKSSSEEVL ERDLGMGDQK VSSRGTPLVF
     PLQENA
//
ID   K1486_MOUSE             Reviewed;         682 AA.
AC   Q8BM65; Q641L6; Q6ZPP8; Q8BWV8;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 41.
DE   RecName: Full=Uncharacterized protein KIAA1486;
GN   Name=Kiaa1486;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic breast, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 257-682 (ISOFORM 4).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-300, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8BM65-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BM65-2; Sequence=VSP_032436;
CC       Name=3;
CC         IsoId=Q8BM65-3; Sequence=VSP_032437;
CC       Name=4;
CC         IsoId=Q8BM65-4; Sequence=VSP_032438;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK034747; BAC28819.1; -; mRNA.
DR   EMBL; AK049778; BAC33918.1; -; mRNA.
DR   EMBL; AK137094; BAE23236.1; -; mRNA.
DR   EMBL; BC082310; AAH82310.1; -; mRNA.
DR   EMBL; AK129372; BAC98182.1; -; mRNA.
DR   IPI; IPI00222931; -.
DR   IPI; IPI00460693; -.
DR   IPI; IPI00752658; -.
DR   IPI; IPI00956773; -.
DR   RefSeq; NP_766437.2; NM_172849.3.
DR   UniGene; Mm.313904; -.
DR   PhosphoSite; Q8BM65; -.
DR   PRIDE; Q8BM65; -.
DR   Ensembl; ENSMUST00000068275; ENSMUSP00000065468; ENSMUSG00000054976.
DR   Ensembl; ENSMUST00000113491; ENSMUSP00000109119; ENSMUSG00000054976.
DR   Ensembl; ENSMUST00000113494; ENSMUSP00000109122; ENSMUSG00000054976.
DR   GeneID; 241134; -.
DR   KEGG; mmu:241134; -.
DR   UCSC; uc007brk.1; mouse.
DR   MGI; MGI:2443135; 9430031J16Rik.
DR   eggNOG; roNOG04313; -.
DR   GeneTree; ENSGT00450000040316; -.
DR   HOVERGEN; HBG108036; -.
DR   Bgee; Q8BM65; -.
DR   CleanEx; MM_9430031J16RIK; -.
DR   Genevestigator; Q8BM65; -.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    682       Uncharacterized protein KIAA1486.
FT                                /FTId=PRO_0000325831.
FT   COMPBIAS    344    485       Pro-rich.
FT   COMPBIAS    413    600       Ser-rich.
FT   MOD_RES     300    300       Phosphotyrosine.
FT   MOD_RES     463    463       Phosphoserine (By similarity).
FT   MOD_RES     465    465       Phosphoserine (By similarity).
FT   MOD_RES     467    467       Phosphoserine (By similarity).
FT   MOD_RES     535    535       Phosphothreonine (By similarity).
FT   MOD_RES     538    538       Phosphoserine (By similarity).
FT   VAR_SEQ     175    206       Missing (in isoform 2).
FT                                /FTId=VSP_032436.
FT   VAR_SEQ     639    682       EPKVSCKLGRSASTSGVPPPSVTPLRQASDLQQSQVPSSLA
FT                                NRD -> GKHDPVLPNGSKSLEAAHMQISLRKPSPQLSLLP
FT                                PRLAPQTHTLRSRHMKNATVPLFIAMARETMLLEALLCSSL
FT                                QLGKTLYQMSSKMTTGLNSSHCNL (in isoform 3).
FT                                /FTId=VSP_032437.
FT   VAR_SEQ     675    682       PSSLANRD -> ACMQWFHGDHTMLEMIEKKRCLCKEIKAR
FT                                QKTEKGLCKQDSMPILPSWKKNAGAKKYSPPPYSKQQTVFW
FT                                DTAI (in isoform 4).
FT                                /FTId=VSP_032438.
FT   CONFLICT     54     54       K -> N (in Ref. 1; BAC33918/BAE23236 and
FT                                2; AAH82310).
SQ   SEQUENCE   682 AA;  73897 MW;  76FDE6609FFDAC8F CRC64;
     MIPSKMMSAN PEEDPLDTFF QYIEDMGMKA YDGLVIQNAS DIARENDRLR NETKLAYLKE
     KNEKRRRQEE TIKRIGGEVG RGQDASYAGK HFRMGFMTMP APQDRLPHPC SSGFTVRSQS
     LHSVGGTEDD SSCGSRRQPP PKPKRDPSTK LSTSSETVNS TAASKSGRSL ERAEGKFTVP
     ASHSPPRAST SGHLFPSPGS QERNIKVSAK PRPHSDEYSK KIPPPKPKRN PNTQLSTSFD
     ETYIKKHVPR RTSLPRDSSL SQVCSPAADP EEEEPVYIEM VGNILRDFRK EEDDQSEAVY
     EEMKYPIFDD LGHDSKCDFD HHSCSSQCAT PTVPDLDFVK SSGPCTPKGL LCDIPPPFPN
     LLSHRPPLLV FPPAPVHCSP NSDESPLTPL EVTKLPVLEN VSYMKQPPGA CPSSLPSHGS
     SHAKDQTGAL GPAPGASILS SSPPPPSTLY RTQSPHGYPK SHSTSPSPVS MGRSLTPLSL
     KRPPPYDAVH SGSLSRSSSS VPHTTPRPVS QDGAKMVNAA VNTYSAAQSG SRSRTPTSPL
     EELTSLFTSG RSLLRKSSSG RRSKEPAEKS TEELKVRSHS TEPLPKLDSK ERGHYGSSSS
     REPVKAQEWD GTPGPPVVTS RMGRCSVSPT LLAGNHSSEP KVSCKLGRSA STSGVPPPSV
     TPLRQASDLQ QSQVPSSLAN RD
//
ID   CADH7_MOUSE             Reviewed;         785 AA.
AC   Q8BM92; Q3UVE2; Q67G09;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Cadherin-7;
DE   Flags: Precursor;
GN   Name=Cdh7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   PubMed=15273735; DOI=10.1038/sj.onc.1207675;
RA   Moore R., Champeval D., Denat L., Tan S.S., Faure F.,
RA   Julien-Grille S., Larue L.;
RT   "Involvement of cadherins 7 and 20 in mouse embryogenesis and
RT   melanocyte transformation.";
RL   Oncogene 23:6726-6735(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Cadherins are calcium dependent cell adhesion proteins.
CC       They preferentially interact with themselves in a homophilic
CC       manner in connecting cells; cadherins may thus contribute to the
CC       sorting of heterogeneous cell types (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Contains 5 cadherin domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; AY267034; AAP94032.1; -; mRNA.
DR   EMBL; AK034096; BAC28586.1; -; mRNA.
DR   EMBL; AK137369; BAE23328.1; -; mRNA.
DR   IPI; IPI00222958; -.
DR   RefSeq; NP_766441.1; NM_172853.2.
DR   UniGene; Mm.213407; -.
DR   HSSP; Q7ZYV7; 1ZVN.
DR   ProteinModelPortal; Q8BM92; -.
DR   SMR; Q8BM92; 48-595, 681-779.
DR   PRIDE; Q8BM92; -.
DR   Ensembl; ENSMUST00000027542; ENSMUSP00000027542; ENSMUSG00000026312.
DR   Ensembl; ENSMUST00000112701; ENSMUSP00000108321; ENSMUSG00000026312.
DR   GeneID; 241201; -.
DR   KEGG; mmu:241201; -.
DR   UCSC; uc007chw.1; mouse.
DR   CTD; 241201; -.
DR   MGI; MGI:2442792; Cdh7.
DR   GeneTree; ENSGT00600000084132; -.
DR   HOGENOM; HBG505775; -.
DR   HOVERGEN; HBG005217; -.
DR   InParanoid; Q8BM92; -.
DR   OMA; IITIQKD; -.
DR   OrthoDB; EOG40K7ZG; -.
DR   PhylomeDB; Q8BM92; -.
DR   NextBio; 384927; -.
DR   ArrayExpress; Q8BM92; -.
DR   Bgee; Q8BM92; -.
DR   CleanEx; MM_CDH7; -.
DR   Genevestigator; Q8BM92; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 5.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF01049; Cadherin_C; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 5.
DR   SUPFAM; SSF49313; Cadherin; 5.
DR   PROSITE; PS00232; CADHERIN_1; 3.
DR   PROSITE; PS50268; CADHERIN_2; 5.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell membrane;
KW   Cleavage on pair of basic residues; Glycoprotein; Membrane; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     27       Potential.
FT   PROPEP       28     47       Potential.
FT                                /FTId=PRO_0000320090.
FT   CHAIN        48    785       Cadherin-7.
FT                                /FTId=PRO_0000320091.
FT   TOPO_DOM     28    607       Extracellular (Potential).
FT   TRANSMEM    608    628       Helical; (Potential).
FT   TOPO_DOM    629    785       Cytoplasmic (Potential).
FT   DOMAIN       49    153       Cadherin 1.
FT   DOMAIN      154    262       Cadherin 2.
FT   DOMAIN      263    377       Cadherin 3.
FT   DOMAIN      378    482       Cadherin 4.
FT   DOMAIN      482    599       Cadherin 5.
FT   CARBOHYD    449    449       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    530    530       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    307    307       L -> V (in Ref. 1; AAP94032).
FT   CONFLICT    580    580       I -> V (in Ref. 2; BAE23328).
SQ   SEQUENCE   785 AA;  87202 MW;  112A1F409BF85CED CRC64;
     MKLGKVELCH FLQLIALFLC FSGMSQAELP RSRSKPYFQS GRSRTKRSWV WNQFFVLEEY
     MGSDPLYVGK LHSDVDKGDG SIKYILSGEG ASSIFIIDEN TGDIHATKRL DREEQAYYTL
     RAQALDRLTN KPVEPESEFV IKIQDINDNE PKFLDGPYTA GVPEMSPVGT SVVQVTATDA
     DDPTYGNSAR VVYSILQGQP YFSVEPKTGV IKTALPNMDR EAKDQYLLVI QAKDMVGQNG
     GLSGTTSVTV TLTDVNDNPP RFPRRSYQYN VPESLPVASV VARIKAADAD IGVNAEMEYK
     IVDGDGLGIF KISADKDTQE GIITIQKELD FEAKTSYTLR IEAANRDADP RFLSLGPFSD
     TTTVKIIVED VDEPPVFSSP LYPMEVSEAT QVGHIIGTVA AHDPDSSNSP VRYSIDRNTD
     LERYFNIDAN SGVITTAKSL DRETNAVHNI TVLAMESQNP SQVGRGYVAI TILDINDNAP
     EFAMDYETTV CENAQPGQVI QKISAVDKDE PSNGHQFYFS LTTDMTNNHN FSLKDNKDNT
     ASILTRRNGF RRQEQSVYYL PIFIVDSGSP SLSSTNTLTI RVCDCDADGI AQTCNAEAYV
     LPAGLSTGAL IAILACVLTL LVLILLIVTM RRRKKEPLIF DEERDIRENI VRYDDEGGGE
     EDTEAFDMAA LRNLNAIRDS KTRRDVTPEI QFLSRPTFKN IPDNVIFREF IWERLKEADV
     DPGAPPYDSL QTYAFEGNGS VAESLSSLDS ISSNSDQNYD YLSDWGPRFK RLAEMYGNGQ
     ESLYS
//
ID   CNKR3_MOUSE             Reviewed;         555 AA.
AC   Q8BMA3; Q3UDS2; Q8K2K0;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Connector enhancer of kinase suppressor of ras 3;
DE            Short=Connector enhancer of KSR 3;
DE   AltName: Full=CNK homolog protein 3;
DE            Short=CNK3;
DE   AltName: Full=CNKSR family member 3;
DE   AltName: Full=Maguin-like protein;
GN   Name=Cnksr3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N;
RA   Tzolovsky G., McGurk L., Pathirana S., Slee R., Hillier S.,
RA   Clinton M., Bownes M.;
RT   "Cloning, expression and comparison of human and mouse ML (maguin-
RT   like) genes, and expression in mouse oogenesis.";
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Muellerian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=19567370; DOI=10.1096/fj.09-134759;
RA   Ziera T., Irlbacher H., Fromm A., Latouche C., Krug S.M., Fromm M.,
RA   Jaisser F., Borden S.A.;
RT   "Cnksr3 is a direct mineralocorticoid receptor target gene and plays a
RT   key role in the regulation of the epithelial sodium channel.";
RL   FASEB J. 23:3936-3946(2009).
CC   -!- FUNCTION: Probably involved in transepithelial sodiun transport.
CC       Regulates aldosterone-induced and ENaC-mediated sodium transport
CC       possibly through regulation of the ERK pathway.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BMA3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BMA3-2; Sequence=VSP_029391, VSP_029615;
CC   -!- TISSUE SPECIFICITY: Expressed in kidney.
CC   -!- SIMILARITY: Belongs to the CNKSR family.
CC   -!- SIMILARITY: Contains 1 CRIC domain.
CC   -!- SIMILARITY: Contains 1 DUF1170 domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY151137; AAN72835.1; -; mRNA.
DR   EMBL; AK033015; BAC28127.1; -; mRNA.
DR   EMBL; AK149951; BAE29189.1; -; mRNA.
DR   EMBL; BC031194; AAH31194.1; -; mRNA.
DR   IPI; IPI00222975; -.
DR   IPI; IPI00874640; -.
DR   RefSeq; NP_766134.1; NM_172546.2.
DR   UniGene; Mm.37984; -.
DR   HSSP; Q969H4; 1WWV.
DR   ProteinModelPortal; Q8BMA3; -.
DR   SMR; Q8BMA3; 2-76, 206-293.
DR   STRING; Q8BMA3; -.
DR   PhosphoSite; Q8BMA3; -.
DR   PRIDE; Q8BMA3; -.
DR   Ensembl; ENSMUST00000015346; ENSMUSP00000015346; ENSMUSG00000015202.
DR   GeneID; 215748; -.
DR   KEGG; mmu:215748; -.
DR   NMPDR; fig|10090.3.peg.13307; -.
DR   UCSC; uc007efb.1; mouse.
DR   CTD; 215748; -.
DR   MGI; MGI:2674130; Cnksr3.
DR   eggNOG; roNOG13610; -.
DR   GeneTree; ENSGT00390000017199; -.
DR   HOGENOM; HBG445215; -.
DR   HOVERGEN; HBG051040; -.
DR   InParanoid; Q8BMA3; -.
DR   OMA; YIRGSRC; -.
DR   OrthoDB; EOG40VVP4; -.
DR   PhylomeDB; Q8BMA3; -.
DR   NextBio; 374837; -.
DR   ArrayExpress; Q8BMA3; -.
DR   Bgee; Q8BMA3; -.
DR   CleanEx; MM_CNKSR3; -.
DR   Genevestigator; Q8BMA3; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
DR   GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IMP:UniProtKB.
DR   GO; GO:0010765; P:positive regulation of sodium ion transport; IMP:UniProtKB.
DR   InterPro; IPR010599; CNKSR2.
DR   InterPro; IPR017874; CRIC_domain.
DR   InterPro; IPR019555; CRIC_domain_Chordata.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF10534; CRIC_ras_sig; 1.
DR   Pfam; PF06663; DUF1170; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS51290; CRIC; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    555       Connector enhancer of kinase suppressor
FT                                of ras 3.
FT                                /FTId=PRO_0000311106.
FT   DOMAIN        7     72       SAM.
FT   DOMAIN       80    174       CRIC.
FT   DOMAIN      211    293       PDZ.
FT   DOMAIN      325    546       DUF1170.
FT   MOD_RES     381    381       Phosphoserine.
FT   MOD_RES     383    383       Phosphoserine (By similarity).
FT   VAR_SEQ       1    241       Missing (in isoform 2).
FT                                /FTId=VSP_029391.
FT   VAR_SEQ     242    243       EN -> MQ (in isoform 2).
FT                                /FTId=VSP_029615.
FT   CONFLICT    243    243       N -> Q (in Ref. 3; AAH31194).
FT   CONFLICT    288    288       L -> Q (in Ref. 2; BAE29189).
SQ   SEQUENCE   555 AA;  61870 MW;  341AF9A4425904F2 CRC64;
     MEPVTKWSPK QVVDWTRGLD DCLQPYVHKF EREKIDGEQL LKISHQDLEE LGVTRIGHQE
     LVLEAVDLLC ALNYGLETDT MKNLVLKLRA SSHNLQNYIS SRRKSPAYDG NTSRKPPNEF
     LTSVVELIGA AKALLAWLDR APFTGITDLS VTKNKIIQLC LDLTTAVQKD CLIAEMEDKV
     LNVVKVLNGI CDKTMRSTTD PVMSQCACLE EVHLPNVRPG EGLGMYIKST YDGLHVITGT
     TENSPADRSQ KIHAGDEVIQ VNRQTVVGWQ LKNLVRKLRE NPTGVVLLLK KRPTGSFSFT
     PAPLKNLRWK PPLVQTSPPP TTTQSPESTM DASLKKEKPA ILDLYIPPPP AVPYSPRDEN
     VSFGYRGHSK SKQPLPVRKG SESPNSFLDQ ESQRRRFTIA DSDQLPGYSV ETNVLPTKMR
     GKTPSYGKPR PLSMPADGNW MGIVDPFAKP RGNGRKGEDA LCRYFSNERI TPITEESASP
     MYRFSRPLTE RHLVRGADYI RGSRCYINSD LHSSATIPFQ EEGSKKKSAS SSAKASSGEP
     SLLVSWLTRL KLLTH
//
ID   SRP68_MOUSE             Reviewed;         625 AA.
AC   Q8BMA6; Q6NS76;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Signal recognition particle 68 kDa protein;
DE            Short=SRP68;
GN   Name=Srp68;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Signal-recognition-particle assembly has a crucial role
CC       in targeting secretory proteins to the rough endoplasmic reticulum
CC       membrane. SRP68 binds the 7S RNA, SRP72 binds to this complex
CC       subsequently. This ribonucleoprotein complex might interact
CC       directly with the docking protein in the ER membrane and possibly
CC       participate in the elongation arrest function (By similarity).
CC   -!- SUBUNIT: Signal recognition particle consists of a 7S RNA molecule
CC       of 300 nucleotides and six protein subunits: SRP72, SRP68, SRP54,
CC       SRP19, SRP14 and SRP9.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus,
CC       nucleolus (By similarity).
CC   -!- DOMAIN: The RNA-binding domain is located near the N-terminus (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the SRP68 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK033010; BAC28124.1; -; mRNA.
DR   EMBL; BC070422; AAH70422.1; -; mRNA.
DR   IPI; IPI00222977; -.
DR   RefSeq; NP_666144.3; NM_146032.3.
DR   UniGene; Mm.29655; -.
DR   STRING; Q8BMA6; -.
DR   PhosphoSite; Q8BMA6; -.
DR   PRIDE; Q8BMA6; -.
DR   Ensembl; ENSMUST00000021133; ENSMUSP00000021133; ENSMUSG00000020780.
DR   GeneID; 217337; -.
DR   KEGG; mmu:217337; -.
DR   UCSC; uc007mkq.1; mouse.
DR   CTD; 217337; -.
DR   MGI; MGI:1917447; Srp68.
DR   HOGENOM; HBG314656; -.
DR   HOVERGEN; HBG059793; -.
DR   InParanoid; Q8BMA6; -.
DR   OrthoDB; EOG4V9TQB; -.
DR   PhylomeDB; Q8BMA6; -.
DR   NextBio; 375773; -.
DR   ArrayExpress; Q8BMA6; -.
DR   Bgee; Q8BMA6; -.
DR   CleanEx; MM_SRP68; -.
DR   Genevestigator; Q8BMA6; -.
DR   GermOnline; ENSMUSG00000020780; Mus musculus.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR011990; TPR-like_helical.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Ribonucleoprotein;
KW   RNA-binding; Signal recognition particle.
FT   CHAIN         1    625       Signal recognition particle 68 kDa
FT                                protein.
FT                                /FTId=PRO_0000135228.
FT   COMPBIAS      9     29       Poly-Gly.
FT   MOD_RES      47     47       Phosphoserine (By similarity).
FT   MOD_RES     240    240       Phosphoserine (By similarity).
FT   MOD_RES     451    451       N6-acetyllysine (By similarity).
FT   MOD_RES     616    616       Phosphotyrosine (By similarity).
FT   MOD_RES     625    625       Phosphoserine (By similarity).
FT   CONFLICT    176    176       Q -> R (in Ref. 2; AAH70422).
FT   CONFLICT    544    544       Y -> S (in Ref. 2; AAH70422).
SQ   SEQUENCE   625 AA;  70622 MW;  315AD1EE9F9C9E04 CRC64;
     MAAEKQIPGG GSGGGGSGSG GGGGGSGGGR SAGGDENKEN ERPSAGSKAN KEFGDSLSLE
     ILQIIKESQQ QHGLRHGDFQ RYRGYCSRRQ RRLRKTLNFK MGNRHKFTGK KVTEELLTDN
     RYLLLVLMDA ERAWSYAMQL KQEANTEPRK RFHLLSRLRK AVKHAEELER LCESNQVDAK
     TKLEAQAYTA YLSGMLRFEH QEWKSAIEAF NKCKTIYEKL ASAFTEEQAV LYNQRVEEIS
     PNIRYCAYNI GDQSAINELM QMRLRSGGTE GLLAEKLEAL ITQTRAKQAA TMSEVEWRGR
     TVPVKIDKVR IFLLGLADNE AAIVQAESEE TKERLFESML SECRDALQAV REELKPDQKQ
     RDYALDGESG KVSNLQYLHS YLTYIKLSTA IRRNENMAKG LHRALLQQQP EDDSKRSPRP
     QDLIRLYDII LQNLVELLQL PGLEEDRTFQ KEISLKTLVF KAYRCFFIAQ SYVLVKKWSE
     ALVLYDRVLK YANEVSSHGG ASKNSLKDLP DVQELITQVR SEKCSLQAAA ILDANDSHQT
     DTSYQVKDNT PLVERFESFC LDPSLVTKQA NLVHFPPGFQ PIPCKPLFFD LALNHVAFPP
     LEDKLEQKTK SGLTGYIKGI FGFRS
//
ID   EMSY_MOUSE              Reviewed;        1264 AA.
AC   Q8BMB0; Q5FWK5; Q80XU1; Q8VDW9;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Protein EMSY;
GN   Name=Emsy;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, Czech II, and FVB/N;
RC   TISSUE=Brain, Kidney, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-750 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Mesonephros;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH BRCA2.
RX   PubMed=14651845; DOI=10.1016/S0092-8674(03)00930-9;
RA   Hughes-Davies L., Huntsman D., Ruas M., Fuks F., Bye J., Chin S.-F.,
RA   Milner J., Brown L.A., Hsu F., Gilks B., Nielsen T., Schulzer M.,
RA   Chia S., Ragaz J., Cahn A., Linger L., Ozdag H., Cattaneo E.,
RA   Jordanova E.S., Schuuring E., Yu D.S., Venkitaraman A., Ponder B.,
RA   Doherty A., Aparicio S., Bentley D., Theillet C., Ponting C.P.,
RA   Caldas C., Kouzarides T.;
RT   "EMSY links the BRCA2 pathway to sporadic breast and ovarian cancer.";
RL   Cell 115:523-535(2003).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452088; DOI=10.1074/mcp.T500040-MCP200;
RA   Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G.,
RA   Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F.,
RA   Maltby D.A., Schoepfer R., Burlingame A.L.;
RT   "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT   preparations using lectin weak affinity chromatography and mass
RT   spectrometry.";
RL   Mol. Cell. Proteomics 5:923-934(2006).
CC   -!- FUNCTION: Regulator which is able to repress transcription,
CC       possibly via its interaction with a multiprotein chromatin
CC       remodeling complex that modifies the chromatin. Its interaction
CC       with BRCA2 suggests that it may play a central role in the DNA
CC       repair function of BRCA2 (By similarity).
CC   -!- SUBUNIT: Homodimer. Interacts with the transactivation domain of
CC       BRCA2. Interacts with the chromoshadow domain of CBX1 and with
CC       ZMYND11. Does not interact with CBX3 or CBX5 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Localizes to DNA damage
CC       markers in irradiated cells, suggesting that it participates in
CC       DNA repair process.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BMB0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BMB0-2; Sequence=VSP_010433, VSP_010434;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8BMB0-3; Sequence=VSP_010432;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 ENT (EMSY N-terminal) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH20109.1; Type=Erroneous initiation;
CC       Sequence=BC039956; Type=Frameshift; Positions=569;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC020109; AAH20109.1; ALT_INIT; mRNA.
DR   EMBL; BC039956; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC089304; AAH89304.1; -; mRNA.
DR   EMBL; AK032985; BAC28113.2; -; mRNA.
DR   IPI; IPI00416315; -.
DR   IPI; IPI00416316; -.
DR   IPI; IPI00416317; -.
DR   RefSeq; NP_758484.2; NM_172280.2.
DR   UniGene; Mm.387819; -.
DR   ProteinModelPortal; Q8BMB0; -.
DR   SMR; Q8BMB0; 9-126.
DR   STRING; Q8BMB0; -.
DR   PhosphoSite; Q8BMB0; -.
DR   PRIDE; Q8BMB0; -.
DR   Ensembl; ENSMUST00000038359; ENSMUSP00000038216; ENSMUSG00000035401.
DR   Ensembl; ENSMUST00000098271; ENSMUSP00000095872; ENSMUSG00000035401.
DR   Ensembl; ENSMUST00000107106; ENSMUSP00000102723; ENSMUSG00000035401.
DR   GeneID; 233545; -.
DR   KEGG; mmu:233545; -.
DR   UCSC; uc009iko.1; mouse.
DR   UCSC; uc009ikp.1; mouse.
DR   UCSC; uc009ikq.1; mouse.
DR   MGI; MGI:1924203; 2210018M11Rik.
DR   GeneTree; ENSGT00390000009554; -.
DR   HOGENOM; HBG402894; -.
DR   HOVERGEN; HBG051476; -.
DR   InParanoid; Q8BMB0; -.
DR   OMA; IASTTQK; -.
DR   OrthoDB; EOG43FGW4; -.
DR   NextBio; 381751; -.
DR   ArrayExpress; Q8BMB0; -.
DR   Bgee; Q8BMB0; -.
DR   CleanEx; MM_2210018M11RIK; -.
DR   Genevestigator; Q8BMB0; -.
DR   GermOnline; ENSMUSG00000035401; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR005491; ENT_N.
DR   Pfam; PF03735; ENT; 1.
DR   PROSITE; PS51138; ENT; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromatin regulator; DNA damage; DNA repair;
KW   Glycoprotein; Nucleus; Phosphoprotein; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   1264       Protein EMSY.
FT                                /FTId=PRO_0000086969.
FT   DOMAIN       16    114       ENT.
FT   REGION        1    442       Interaction with BRCA2 (By similarity).
FT   REGION      118    122       Interaction with ZMYND11 (By similarity).
FT   COMPBIAS    173    177       Poly-Ser.
FT   COMPBIAS    290    355       Ser-rich.
FT   COMPBIAS    359    428       Gln-rich.
FT   COMPBIAS    460    600       Thr-rich.
FT   COMPBIAS    683    687       Poly-Ser.
FT   COMPBIAS    895   1048       Gln-rich.
FT   MOD_RES     171    171       Phosphothreonine (By similarity).
FT   MOD_RES     173    173       Phosphoserine (By similarity).
FT   MOD_RES     177    177       Phosphoserine (By similarity).
FT   MOD_RES     202    202       Phosphoserine (By similarity).
FT   MOD_RES     226    226       Phosphothreonine (By similarity).
FT   MOD_RES     237    237       Phosphothreonine (By similarity).
FT   MOD_RES     238    238       Phosphothreonine (By similarity).
FT   MOD_RES    1079   1079       Phosphoserine (By similarity).
FT   MOD_RES    1085   1085       Phosphoserine (By similarity).
FT   CARBOHYD    192    192       O-linked (GlcNAc).
FT   VAR_SEQ      82     96       KMNLSLYLGERPSYS -> N (in isoform 3).
FT                                /FTId=VSP_010432.
FT   VAR_SEQ     802    802       T -> TERTDEGTEVAFPLL (in isoform 2).
FT                                /FTId=VSP_010433.
FT   VAR_SEQ    1040   1199       Missing (in isoform 2).
FT                                /FTId=VSP_010434.
FT   CONFLICT    975    975       V -> A (in Ref. 1; BC039956).
SQ   SEQUENCE   1264 AA;  135291 MW;  F4BA591D43912B2A CRC64;
     MPVVWPTLLD LSRDECKRIL RKLELEAYAG VISALRAQGD LTKEKKDLLG ELSKVLSIST
     ERHRAEVRRA VNDERLTTIA HKMNLSLYLG ERPSYSMSGP NSSSEWSIEG RRLVPLMPRL
     VPQTAFTVTA NAVANAAVQH NASLPVPAET ASKDGVSCSD EDEKPRKRRR TNSSSSSPVV
     LKEVPKAVVP VSKTITVPVS GSPKMSNIMQ SIANSLPPHM SPVKITFTKP STQTTNTTTQ
     KVIIVTTSPS STFVPNILSK SHNYAAVTKL VPTSVIASTT QKPPVVITAS QASLVTSSSN
     GNSSSTSSPI SSTVAVTTVV SSTPSVVMST VAQGVSTSAI KVASTRLPSP KSLVSGPTQI
     LAQFPKQHQQ SPKQQLQQVQ QQTQQPVAQP SSVSQQQQPQ QSALPPGIKP TIQIKQESGV
     KIITQQVQPS KILPKPVTAT LPTSSNSPIM VVSSNGAIMT TKLVTTPTGT QATYTRPTVS
     PSLGRVATTP GAATYVKTTS GSIITVVPKS LATLGGKIIS SNIVSGTTTK ITTIPMTSKP
     NVIVVQKTTG KGTTIQGLPG KNVVTTLLNA GGEKTLQTVP AGAKPAIITA TRPITKMIVT
     QPKGIGSAVQ PAAKIIPTKI VYGQQGKTQV LIKPKPVTFQ ATVVSEQTRQ LVTETLQQAS
     RVADASNSSA QEGKEEPQGY TDSSSSSTES SQSSQDSQPV VHVIASRRQD WSEHEIAMET
     SPTIIYQDVS SESQSATSTI KALLELQQTT VKEKLESKPR QPTIDLSQMA VPIQMTQEKR
     HSPESPSIAV VESELVAEYI TTVSHRSQPQ QPSQPQRTLL QHVAQSQTAT QTSVVVKSIP
     ASSPGAITHI MQQALSSHTA FTKHSEELGT EEGEVEEMDT LDPQTGLFYR SALTQSQSTK
     QQKLSQPQLE QTQLQVKTLQ CFQTKQKQTI HLQADQLQHK LTQMPQLSIR HQKLNPLQQE
     QAQPKPDAQH TQHTVVAKDR QLPTLMAQPP QTVVQVLAVK TTQQLPKLQQ APNQPKIYVQ
     PQTPQSQMAL PSSEKQPASQ VEQPIITQGS SVTKITFEGR QPPTVTKITG GSSVPKLTSP
     VTSISPIQAS EKTAVSDILQ MSLMEAQIDT NVEHMVVDPP KKALATNVLT GEAGALPSTH
     VVVAGMTKCR ESCSSPSAVG PPLTTRKIEA AGVPTTGQFM RIQNVGQKKA EESPTEIIIQ
     AIPQYAIPCH SSSNVVVEPS GLLELNNFTS QQLDDDETAM EQDIDSSTED GTEPSPSQSA
     VERS
//
ID   ODP2_MOUSE              Reviewed;         642 AA.
AC   Q8BMF4; Q8K2G8; Q8R339; Q91ZB1;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial;
DE            EC=2.3.1.12;
DE   AltName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex;
DE   AltName: Full=Pyruvate dehydrogenase complex component E2;
DE            Short=PDC-E2;
DE            Short=PDCE2;
DE   Flags: Precursor;
GN   Name=Dlat;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, FVB/N-3, and NMRI; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 84-642.
RC   TISSUE=Hepatoma;
RX   PubMed=12108679; DOI=10.1007/s005350200065;
RA   Wang L., Kaneko S., Kagaya M., Ohno H., Honda M., Kobayashi K.;
RT   "Molecular cloning, and characterization and expression of
RT   dihydrolipoamide acetyltransferase component of murine pyruvate
RT   dehydrogenase complex in bile duct cancer cells.";
RL   J. Gastroenterol. 37:449-454(2002).
RN   [4]
RP   PROTEIN SEQUENCE OF 93-109; 147-176; 282-295; 383-424; 469-477;
RP   486-499; 528-542; 548-569; 600-631 AND 633-642, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Klug S., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains
CC       multiple copies of three enzymatic components: pyruvate
CC       dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and
CC       lipoamide dehydrogenase (E3) (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine
CC       = CoA + enzyme N(6)-(S-acetyldihydrolipoyl)lysine.
CC   -!- COFACTOR: Binds 1 lipoyl cofactor covalently (By similarity).
CC   -!- SUBUNIT: 20 to 30 alpha(2)-beta(2) tetramers of E1 + 6 homodimers
CC       of E3 + 60 copies of E2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC   -!- SIMILARITY: Contains 2 lipoyl-binding domains.
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DR   EMBL; AK032124; BAC27715.1; -; mRNA.
DR   EMBL; BC026680; AAH26680.1; -; mRNA.
DR   EMBL; BC031495; AAH31495.1; -; mRNA.
DR   EMBL; BC069862; AAH69862.1; -; mRNA.
DR   EMBL; AY044265; AAL02400.1; -; mRNA.
DR   IPI; IPI00153660; -.
DR   RefSeq; NP_663589.3; NM_145614.4.
DR   UniGene; Mm.285076; -.
DR   UniGene; Mm.471144; -.
DR   HSSP; P10515; 1FYC.
DR   ProteinModelPortal; Q8BMF4; -.
DR   SMR; Q8BMF4; 91-181, 217-294, 348-390, 404-642.
DR   MINT; MINT-135876; -.
DR   STRING; Q8BMF4; -.
DR   PhosphoSite; Q8BMF4; -.
DR   REPRODUCTION-2DPAGE; IPI00153660; -.
DR   UCD-2DPAGE; Q8BMF4; -.
DR   PRIDE; Q8BMF4; -.
DR   Ensembl; ENSMUST00000034567; ENSMUSP00000034567; ENSMUSG00000000168.
DR   GeneID; 235339; -.
DR   KEGG; mmu:235339; -.
DR   CTD; 235339; -.
DR   MGI; MGI:2385311; Dlat.
DR   eggNOG; roNOG14419; -.
DR   HOGENOM; HBG630916; -.
DR   HOVERGEN; HBG005063; -.
DR   InParanoid; Q8BMF4; -.
DR   OMA; EGDKLNE; -.
DR   OrthoDB; EOG412M54; -.
DR   PhylomeDB; Q8BMF4; -.
DR   BRENDA; 2.3.1.12; 244.
DR   NextBio; 382617; -.
DR   ArrayExpress; Q8BMF4; -.
DR   Bgee; Q8BMF4; -.
DR   Genevestigator; Q8BMF4; -.
DR   GO; GO:0005967; C:mitochondrial pyruvate dehydrogenase complex; TAS:MGI.
DR   GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; TAS:MGI.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IC:MGI.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR006257; AcTrfase_Pyrv_DH_cplx_L.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom.
DR   InterPro; IPR004167; E3-bd.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Gene3D; G3DSA:3.30.559.10; CAT-like_dom; 1.
DR   Gene3D; G3DSA:4.10.320.10; E3_bd; 1.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 2.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; E3_bd; 1.
DR   SUPFAM; SSF51230; Hybrid_motif; 2.
DR   TIGRFAMs; TIGR01349; PDHac_trf_mito; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR   PROSITE; PS00189; LIPOYL; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Acyltransferase; Direct protein sequencing; Glycolysis;
KW   Lipoyl; Mitochondrion; Repeat; Transferase; Transit peptide.
FT   TRANSIT       1     85       Mitochondrion (By similarity).
FT   CHAIN        86    642       Dihydrolipoyllysine-residue
FT                                acetyltransferase component of pyruvate
FT                                dehydrogenase complex, mitochondrial.
FT                                /FTId=PRO_0000285717.
FT   DOMAIN       91    165       Lipoyl-binding 1.
FT   DOMAIN      218    292       Lipoyl-binding 2.
FT   REGION      353    384       E3- and/or E1-component binding domain
FT                                (Potential).
FT   REGION      466    642       Catalytic (By similarity).
FT   REGION      610    621       CoA-binding (By similarity).
FT   ACT_SITE    615    615       Potential.
FT   ACT_SITE    619    619       Potential.
FT   MOD_RES     258    258       N6-lipoyllysine (By similarity).
FT   MOD_RES     461    461       N6-acetyllysine (By similarity).
FT   CONFLICT     84     84       S -> Y (in Ref. 3; AAL02400).
FT   CONFLICT    198    198       P -> T (in Ref. 1; BAC27715).
FT   CONFLICT    225    225       L -> P (in Ref. 3; AAL02400).
FT   CONFLICT    393    393       A -> V (in Ref. 2; AAH31495).
FT   CONFLICT    604    604       A -> V (in Ref. 2; AAH31495).
SQ   SEQUENCE   642 AA;  67942 MW;  1294FAC4857FC29C CRC64;
     MWRVCARRAR SAVPRDGFRA RWAALKEGPG APCGSPRIGP AAVRCGSGIP RYGVRSLCGW
     SSGSGTVPRN RLLRQLLGSP SRRSYSLPPH QKVPLPSLSP TMQAGTIARW EKKEGEKISE
     GDLIAEVETD KATVGFESLE ECYMAKILVP EGTRDVPVGS IICITVEKPQ DIEAFKNYTL
     DLAAAAAPQA APAAAPAPAA APAAPSASAP GSSYPTHMQI VLPALSPTMT MGTVQRWEKK
     VGEKLSEGDL LAEIETDKAT IGFEVQEEGY LAKILVPEGT RDVPLGAPLC IIVEKQEDIA
     AFADYRPTEV TSLKPQAAPP APPPVAAVPP TPQPVAPTPS AAPAGPKGRV FVSPLAKKLA
     AEKGIDLTQV KGTGPEGRII KKDIDSFVPS KAAPAAAAAM APPGPRVAPA PAGVFTDIPI
     SNIRRVIAQR LMQSKQTIPH YYLSVDVNMG EVLLVRKELN KMLEGKGKIS VNDFIIKASA
     LACLKVPEAN SSWMDTVIRQ NHVVDVSVAV STPAGLITPI VFNAHIKGLE TIASDVVSLA
     SKAREGKLQP HEFQGGTFTI SNLGMFGIKN FSAIINPPQA CILAIGASED KLIPADNEKG
     FDVASVMSVT LSCDHRVVDG AVGAQWLAEF KKYLEKPITM LL
//
ID   RBGPR_MOUSE             Reviewed;        1366 AA.
AC   Q8BMG7; Q6PEU0; Q80TQ6; Q8BX72;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 2.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Rab3 GTPase-activating protein non-catalytic subunit;
DE   AltName: Full=Rab3 GTPase-activating protein 150 kDa subunit;
DE   AltName: Full=Rab3-GAP p150;
DE            Short=Rab3-GAP150;
DE   AltName: Full=Rab3-GAP regulatory subunit;
GN   Name=Rab3gap2; Synonyms=Kiaa0839;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 319-1366 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Forelimb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 283-1366 (ISOFORM 1).
RC   STRAIN=NMRI; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 432-1364 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Regulatory subunit of a GTPase activating protein that
CC       has specificity for Rab3 subfamily (RAB3A, RAB3B, RAB3C and
CC       RAB3D). Rab3 proteins are involved in regulated exocytosis of
CC       neurotransmitters and hormones. Rab3 GTPase-activating complex
CC       specifically converts active Rab3-GTP to the inactive form Rab3-
CC       GDP. Required for normal eye and brain development. May
CC       participate in neurodevelopmental processes such as proliferation,
CC       migration and differentiation before synapse formation, and non-
CC       synaptic vesicular release of neurotransmitters (By similarity).
CC   -!- SUBUNIT: The Rab3 GTPase-activating complex is a heterodimer
CC       composed of RAB3GAP and RAB3-GAP150. The Rab3 GTPase-activating
CC       complex interacts with DMXL2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=In neurons,
CC       it is enriched in the synaptic soluble fraction (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BMG7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BMG7-2; Sequence=VSP_013313;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the Rab3-GAP regulatory subunit family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH57872.1; Type=Erroneous initiation;
CC       Sequence=BAC27296.1; Type=Erroneous initiation;
CC       Sequence=BAC65667.2; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA;
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DR   EMBL; AK031191; BAC27296.1; ALT_INIT; mRNA.
DR   EMBL; AK048759; BAC33447.1; -; mRNA.
DR   EMBL; AC129195; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC131084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC158963; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC057872; AAH57872.1; ALT_INIT; mRNA.
DR   EMBL; AK122385; BAC65667.2; ALT_SEQ; Transcribed_RNA.
DR   IPI; IPI00555130; -.
DR   IPI; IPI00944792; -.
DR   RefSeq; NP_001157226.1; NM_001163754.1.
DR   UniGene; Mm.275841; -.
DR   STRING; Q8BMG7; -.
DR   PhosphoSite; Q8BMG7; -.
DR   PRIDE; Q8BMG7; -.
DR   Ensembl; ENSMUST00000069652; ENSMUSP00000066325; ENSMUSG00000039318.
DR   GeneID; 98732; -.
DR   KEGG; mmu:98732; -.
DR   UCSC; uc007dyu.1; mouse.
DR   CTD; 98732; -.
DR   MGI; MGI:1916043; Rab3gap2.
DR   eggNOG; roNOG05736; -.
DR   HOGENOM; HBG282729; -.
DR   HOVERGEN; HBG067039; -.
DR   InParanoid; Q8BMG7; -.
DR   OrthoDB; EOG470TGK; -.
DR   ArrayExpress; Q8BMG7; -.
DR   Bgee; Q8BMG7; -.
DR   CleanEx; MM_RAB3GAP2; -.
DR   Genevestigator; Q8BMG7; -.
DR   GermOnline; ENSMUSG00000039318; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005625; C:soluble fraction; ISS:UniProtKB.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; GTPase activation; Phosphoprotein.
FT   CHAIN         1   1366       Rab3 GTPase-activating protein non-
FT                                catalytic subunit.
FT                                /FTId=PRO_0000191663.
FT   MOD_RES     448    448       Phosphoserine.
FT   MOD_RES     899    899       Phosphothreonine (By similarity).
FT   VAR_SEQ       1   1068       Missing (in isoform 2).
FT                                /FTId=VSP_013313.
FT   CONFLICT    727    727       I -> V (in Ref. 1; BAC27296).
FT   CONFLICT    747    747       K -> E (in Ref. 1; BAC27296 and 2).
FT   CONFLICT    862    862       E -> V (in Ref. 1; BAC27296 and 2).
FT   CONFLICT    906    906       S -> T (in Ref. 3; AAH57872).
FT   CONFLICT   1021   1021       Q -> H (in Ref. 3; AAH57872).
SQ   SEQUENCE   1366 AA;  152535 MW;  A84C2C1416F673BA CRC64;
     MACSIVQFCS FQDLQSARDF LFPHLREETP GALKRDPSKT SSWEDDSWGA WEETEPREPE
     EEGNTSKTQK NSWLQECVLS LSPTSDLMVI AREQKAAFLV RKWKHGDKGK EEMQFAVGWS
     GSVSAEEGEY VTSALCIPLA SQKRSSTGRP DWTCIVVGFT SGYVRFYTEG VLLLAQLLNE
     DKVLQLKCRT YEIPRHPGVT EQNEELSILY PAAIVTIDGF SLFQSLRACR NQVAKAAASG
     NENIQPPPLA YKKWGLQDID TIIDHASVGI MTLSPFDQMK TASNIGGFNA AIKNSPPAMS
     QYITVGSSPF TGFFYALEGS TQPLLSHVAL AVASKLTSAL FSAASGWLGW KSKHEEDTVQ
     KQKPKMEPAT PLAVRFGLPD SRRHGESICL SPCNTLAAVT DDFGRVILLD VARGIAIRMW
     KGYRDAQVGW IQIVEDLHER VPEKGGFSPF GNTQGPSRVA QFLVIYAPRR GILEVWNTQQ
     GPRVGAFNVG KHCRLLYPGY KIMGLNNVTS QSWQPQTYQI CLVDPVSASV KAVNVPFHLA
     LSDKKSERAK DLHLVKKLSA LLRAKSPRPD SFETEIKELI LDIKYPATKK QALESILASD
     RLSFSCLRNV TQTLMDTLKN QELESVDEGL LQFCASKLKL LHLYESVSQL NTLDFHSDTP
     FSDNDLAVLL RLDDKELLKL RALLEKYKQE NTKATVRFSE DADRVLPVKT FLEYLEYEKD
     ALSIRKIGEE ECVALGSFFF WKCLHGKSST EEMCHSLESA GLSPQQLLSL LLSVWLSKEK
     DILDKPQSVC CLHTMLSLLS KMKVAIDETW DSQSVSPWWQ QMRMACIQSE NSGAALLSAH
     VGHSVAAQMS SGATDKKFSQ MELDADAEAL TDSWEALSLD TEYWKLLLRQ LEDCLILQTL
     LHSKLSPPAA KAPSLQSEPL PRLSVKKLLE GGKGGIADSV AKWIFKQDLS PELLKCANKE
     RDVENPDEPR EDLLHLAYEQ FPCSLELDVL HAHCCWEYVV QWNKDPEEAR FLVRSIEHLK
     QILNPHVQNG IALMMWNTFL VKRFSAATYL MDKVGKSPKD RLCRRDVGMS DTALTSFLGS
     CLELLQTSLE ADISRDEVQV PVLDTEDAWL SVEGPISIVE LALEQKPIHY PLVEHHSVLC
     SILYASMRFS LKSVKPLALF DSKGKNAFFK DLTSIQLLPS GEMDPNFISV RQQFLLKVVS
     AAVQAQHSKD KDPSAEAANT HWKDLNWPGL AVDLAHHLQV SDDVIRRHYV GELYSHGADL
     LGEEAIFQVQ DKEVLASQLL VLTGQRLAHA LFHTQTKEGM ELLARLPPTL CTWLKAMNPQ
     DLQNTGVPIA ATAKLVHKVM ELLPEKHGQY SLALHLIDAV EAMATL
//
ID   GGA3_MOUSE              Reviewed;         718 AA.
AC   Q8BMI3; Q80U71;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=ADP-ribosylation factor-binding protein GGA3;
DE   AltName: Full=Golgi-localized, gamma ear-containing, ARF-binding protein 3;
GN   Name=Gga3; Synonyms=Kiaa0154;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Forelimb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Plays a role in protein sorting and trafficking between
CC       the trans-Golgi network (TGN) and endosomes. Mediates the ARF-
CC       dependent recruitment of clathrin to the TGN and binds
CC       ubiquitinated proteins and membrane cargo molecules with a
CC       cytosolic acidic cluster-dileucine (AC-LL) motif (By similarity).
CC   -!- SUBUNIT: Monomer. Interacts with GGA1 and GGA2. Binds to clathrin
CC       and activated ARFs. Binds RABEP1 and RABGEF1. Interacts with the
CC       type-I membrane proteins SORT1, SORL1, LRP3, M6PR/CD-MPR,
CC       IGF2R/CI-MPR and BACE1. Binds the accessory proteins P56, P200,
CC       SYNRG, EPN4, NECAP1, NECAP2 and AFTPH/aftiphilin. Interacts with
CC       TSG101 and UBC (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC       membrane; Peripheral membrane protein (By similarity). Endosome
CC       membrane; Peripheral membrane protein (By similarity).
CC   -!- DOMAIN: The VHS domain functions as a recognition module for
CC       sorting signals composed of an acidic cluster followed by two
CC       leucines (AC-LL motif) (By similarity).
CC   -!- DOMAIN: The GAT domain is responsible for interaction with ARF-
CC       GTP, UBC and RABEP1. Required for recruitment to the TGN it
CC       prevents ARF-GTP hydrolysis (By similarity).
CC   -!- DOMAIN: The unstructured hinge region contains clathrin-binding
CC       and an autoinhibitory (AC-LL) motifs (By similarity).
CC   -!- DOMAIN: The GAE domain binds accessory proteins regulating GGAs
CC       function (By similarity).
CC   -!- PTM: Phosphorylated by CK2 and dephosphorylated by PP2A.
CC       Phosphorylation of GGA3 allows the internal AC-LL motif to bind
CC       the VHS domain and to inhibit the recognition of cargo signals (By
CC       similarity).
CC   -!- PTM: Ubiquitinated (By similarity).
CC   -!- SIMILARITY: Belongs to the GGA protein family.
CC   -!- SIMILARITY: Contains 1 GAE domain.
CC   -!- SIMILARITY: Contains 1 GAT domain.
CC   -!- SIMILARITY: Contains 1 VHS domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65494.2; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK122212; BAC65494.2; ALT_INIT; mRNA.
DR   EMBL; AK031086; BAC27246.1; -; mRNA.
DR   IPI; IPI00403332; -.
DR   UniGene; Mm.119479; -.
DR   ProteinModelPortal; Q8BMI3; -.
DR   SMR; Q8BMI3; 1-157, 168-300, 574-718.
DR   STRING; Q8BMI3; -.
DR   PhosphoSite; Q8BMI3; -.
DR   PRIDE; Q8BMI3; -.
DR   Ensembl; ENSMUST00000019135; ENSMUSP00000019135; ENSMUSG00000020740.
DR   MGI; MGI:2384159; Gga3.
DR   GeneTree; ENSGT00600000084107; -.
DR   HOGENOM; HBG717353; -.
DR   HOVERGEN; HBG015945; -.
DR   InParanoid; Q8BMI3; -.
DR   OrthoDB; EOG4W0XCS; -.
DR   PhylomeDB; Q8BMI3; -.
DR   ArrayExpress; Q8BMI3; -.
DR   Bgee; Q8BMI3; -.
DR   Genevestigator; Q8BMI3; -.
DR   GermOnline; ENSMUSG00000020740; Mus musculus.
DR   GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR013041; Clathrin/coatomer_app_Ig-like.
DR   InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR   InterPro; IPR008153; Clathrin_g-adaptin_app.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR004152; GAT.
DR   InterPro; IPR002014; VHS.
DR   InterPro; IPR018205; VHS_subgroup.
DR   Gene3D; G3DSA:2.60.40.1230; Clathrin_g-adaptin_app; 1.
DR   Gene3D; G3DSA:1.25.40.90; ENTH_VHS; 1.
DR   Pfam; PF02883; Alpha_adaptinC2; 1.
DR   Pfam; PF03127; GAT; 1.
DR   Pfam; PF00790; VHS; 1.
DR   SMART; SM00809; Alpha_adaptinC2; 1.
DR   SMART; SM00288; VHS; 1.
DR   SUPFAM; SSF49348; Clath_adapt; 1.
DR   SUPFAM; SSF48464; ENTH_VHS; 1.
DR   PROSITE; PS50180; GAE; 1.
DR   PROSITE; PS50909; GAT; 1.
DR   PROSITE; PS50179; VHS; 1.
PE   2: Evidence at transcript level;
KW   Endosome; Golgi apparatus; Membrane; Phosphoprotein;
KW   Protein transport; Transport; Ubl conjugation.
FT   CHAIN         1    718       ADP-ribosylation factor-binding protein
FT                                GGA3.
FT                                /FTId=PRO_0000212685.
FT   DOMAIN       16    146       VHS.
FT   DOMAIN      171    298       GAT.
FT   DOMAIN      589    710       GAE.
FT   REGION      299    588       Unstructured hinge.
FT   MOTIF       387    391       Autoinhibitory (By similarity).
FT   COMPBIAS    335    500       Pro-rich.
FT   CONFLICT    151    151       T -> P (in Ref. 1; BAC65494).
FT   CONFLICT    433    433       A -> V (in Ref. 1; BAC65494).
SQ   SEQUENCE   718 AA;  77977 MW;  7A33CC7F091989B8 CRC64;
     MAEAEGESLE SWLNKATNPS NRQEDWEYII GFCDQINKEL EGPQIAVRLL AHKIQSPQEW
     EAVQALTVLE ACMKNCGRRL HNEVGKFRFL NELIKVVSPK YLGDRVSEKV KTKVIELLFS
     WTLALPEEAK IKDAYHMLKR QGIVQSDPPI TMDRTLIPSP PPRPKNPVFD DEEKSKLLAR
     LLKSKNPDDL QEANRLIKSM VKEDEARIQK VTKRLHTLEE VNNNVKLLHE MLLHYSQEYS
     SDADKELMKE LFDRCENKRR TLFKLASETE DNDNSLGDIL QASDNLSRVI NSYKTIIEGQ
     IVNGEVTTST MPDSEGNSHC GNQGALIDLA ELDAPSNSSP ALAPPTSGIP ILPPPPQTSG
     PPRSRSSSQA EAPPGSDSTN NALSLLDEEL LCLGLTDPAP TAPKESPGSS QWHLFQNEPP
     SDLDFFSPRP VPAASCPSDG PQLPPPVSTS SMSQAPLPAA FPAPVVPASA PTHSTGSFMF
     SSGPAPALAP KAEPKGPEYP SSSTSHRLDA LDQLLEEAKV TSGLVKPVSC FSPGPTASPL
     LPASAPARPL LPFSTGPGSP LFQSQGSPQK GPELSLASVH VPLESIKPSS ALPVTAYDKN
     GFRILFHFAK ECPPGRPDVL VVVVSMLNTA PLPVKSIVLQ AAVPKSMKVK LQPPSGTELS
     PFSPIQPPAA ITQVMLLANP MKEKVRLRYK LTFALGEQLS TELGEVDQFP PVEQWGNL
//
ID   CCD21_MOUSE             Reviewed;         761 AA.
AC   Q8BMK0; Q8BUF1; Q8K0E6;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Coiled-coil domain-containing protein 21;
GN   Name=Ccdc21;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the CCDC21 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK030742; BAC27110.1; -; mRNA.
DR   EMBL; AK085545; BAC39468.1; -; mRNA.
DR   EMBL; BC031729; AAH31729.1; -; mRNA.
DR   IPI; IPI00223045; -.
DR   RefSeq; NP_653110.3; NM_144527.3.
DR   UniGene; Mm.26542; -.
DR   ProteinModelPortal; Q8BMK0; -.
DR   PhosphoSite; Q8BMK0; -.
DR   PRIDE; Q8BMK0; -.
DR   Ensembl; ENSMUST00000040271; ENSMUSP00000039889; ENSMUSG00000037443.
DR   GeneID; 70012; -.
DR   KEGG; mmu:70012; -.
DR   NMPDR; fig|10090.3.peg.10551; -.
DR   UCSC; uc008ved.1; mouse.
DR   CTD; 70012; -.
DR   MGI; MGI:1917262; Ccdc21.
DR   HOGENOM; HBG444525; -.
DR   HOVERGEN; HBG058148; -.
DR   InParanoid; Q8BMK0; -.
DR   OMA; RDKHINN; -.
DR   OrthoDB; EOG4PNXGB; -.
DR   PhylomeDB; Q8BMK0; -.
DR   NextBio; 330803; -.
DR   ArrayExpress; Q8BMK0; -.
DR   Bgee; Q8BMK0; -.
DR   CleanEx; MM_CCDC21; -.
DR   Genevestigator; Q8BMK0; -.
DR   GermOnline; ENSMUSG00000037443; Mus musculus.
PE   2: Evidence at transcript level;
KW   Coiled coil; Phosphoprotein.
FT   CHAIN         1    761       Coiled-coil domain-containing protein 21.
FT                                /FTId=PRO_0000233661.
FT   COILED      333    656       Potential.
FT   COILED      723    749       Potential.
FT   COMPBIAS    659    662       Poly-Ser.
FT   MOD_RES      16     16       Phosphoserine (By similarity).
FT   CONFLICT     68     68       E -> G (in Ref. 1; BAC27110).
FT   CONFLICT    301    302       Missing (in Ref. 2; AAH31729).
SQ   SEQUENCE   761 AA;  85340 MW;  43504973E2F620DF CRC64;
     MAMQEKYPND RSHATSPGSN VIQKGSSLGT EWQTPVISET FRSRFSRCSS IADSGDTAIG
     TSCSDIAEDF CSSSGSPSFQ PIKSHITIPT AHVMPSTLGA SPAKPNSAPS GPSSAKLPLS
     GLTEGVGMTR NGDFGAVKRS PGLARDFMYL PSAAGENGSQ QSWFPAVGHE REGEMRKFDV
     PSMESTLNQP AMLETLYSDP HYRAHFPNPR PDTNKDVYKV LPESKKAPGS GAVFERNGPH
     ASSSGVLPLG LQPAPGLSKS LSSQVWQPSP DPWHPGEQSC ELSTCRQQLE LIRLQMEQMQ
     LQNGAMCHHP AAFAPLLPTL EPAQWLSILN SNEHLLKEKE LLIDKQRKHI SQLEQKVRES
     ELQVHSALLG RPAPFGDVCL LRLQELQREN TFLRAQFAQK TEALSKEKME LEKKLSASEV
     EIQLIRESLK VTLQKHSEEG KKQEERVKGR DKHINNLKKK CQKESEQNRE KQQRIETLER
     YLADLPTLED HQKQTEQLKD AELKNTELQE RVAELETLLE DTQATCREKE VQLESLRQRE
     ADLSSARHSF QDKQSVEEAN GENLRVDMES QQKECDSLRK MVERQQLKME QLHSQVQSQK
     QELAQEEGIN QALREEAQRR ETALQQMRTA VKELSVQNQD LIEKNLTLQE HLRQAQPGSS
     SSPDSAQLAC ELHQELASCL QDLQAVCSIV TQRAQGHNPN LSLLLGIHST QHPGTQLDLQ
     KPDVIRRKLE EVQQLRHDIE DLRTSLSDRY AQDMGENCAT Q
//
ID   CKAP4_MOUSE             Reviewed;         575 AA.
AC   Q8BMK4; B2RRB4; Q8BTK8; Q8R3F2;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Cytoskeleton-associated protein 4;
DE   AltName: Full=63 kDa membrane protein;
DE            Short=p63;
GN   Name=Ckap4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-575.
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Submandibular gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC       compartment membrane; Single-pass membrane protein (By
CC       similarity).
CC   -!- PTM: Reversibly palmitoylated (By similarity).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH25522.1; Type=Erroneous initiation;
CC       Sequence=AAH25522.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Vector contamination at the N-terminus;
CC       Sequence=BAC41005.1; Type=Erroneous initiation;
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DR   EMBL; AC140333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC150314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC025522; AAH25522.1; ALT_INIT; mRNA.
DR   EMBL; BC138318; AAI38319.1; -; mRNA.
DR   EMBL; BC138320; AAI38321.1; -; mRNA.
DR   EMBL; AK030708; BAC27092.1; -; mRNA.
DR   EMBL; AK089935; BAC41005.1; ALT_INIT; mRNA.
DR   IPI; IPI00223047; -.
DR   RefSeq; NP_780660.1; NM_175451.1.
DR   UniGene; Mm.334999; -.
DR   ProteinModelPortal; Q8BMK4; -.
DR   STRING; Q8BMK4; -.
DR   PhosphoSite; Q8BMK4; -.
DR   PRIDE; Q8BMK4; -.
DR   Ensembl; ENSMUST00000053871; ENSMUSP00000050336; ENSMUSG00000046841.
DR   GeneID; 216197; -.
DR   KEGG; mmu:216197; -.
DR   UCSC; uc007gkq.1; mouse.
DR   CTD; 216197; -.
DR   MGI; MGI:2444926; Ckap4.
DR   eggNOG; maNOG06859; -.
DR   GeneTree; ENSGT00390000015968; -.
DR   HOGENOM; HBG278737; -.
DR   HOVERGEN; HBG101940; -.
DR   InParanoid; Q8BMK4; -.
DR   OMA; EAQLSLY; -.
DR   OrthoDB; EOG4QRH48; -.
DR   NextBio; 375070; -.
DR   ArrayExpress; Q8BMK4; -.
DR   Bgee; Q8BMK4; -.
DR   CleanEx; MM_CKAP4; -.
DR   Genevestigator; Q8BMK4; -.
DR   GermOnline; ENSMUSG00000046841; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0033116; C:ER-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR010356; Haemolysin_E.
DR   Gene3D; G3DSA:1.20.1170.10; Haemolysin_E; 2.
PE   2: Evidence at transcript level;
KW   Coiled coil; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    575       Cytoskeleton-associated protein 4.
FT                                /FTId=PRO_0000252418.
FT   TRANSMEM     86    108       Helical; (Potential).
FT   COILED      125    193       Potential.
FT   COILED      236    438       Potential.
FT   COILED      507    575       Potential.
FT   MOD_RES      17     17       Phosphoserine (By similarity).
FT   MOD_RES     292    292       Phosphoserine (By similarity).
FT   MOD_RES     296    296       Phosphothreonine (By similarity).
FT   MOD_RES     310    310       Phosphoserine (By similarity).
FT   CONFLICT    243    243       K -> M (in Ref. 2; AAH25522).
FT   CONFLICT    281    281       M -> I (in Ref. 3; BAC41005).
SQ   SEQUENCE   575 AA;  63692 MW;  6967F47741C7033D CRC64;
     MPSAKQRGSK GGHGAASPSD KGAHPSGGAD DVAKKPPAAP QQPQPPAPHP PQHPQNQAHR
     GGHRGRSSAA TANASSASCS RRLGRVLNFL FYLSLVAAAA FSGWYVHHVL EEVQQVRRGH
     QDFSRQRDEL GQGLQGVEQK VQSLQATFGT FESLLRNSQH KQDLTEKAVK EGESELNRIS
     EVLQKLQNEI LKDLSDGIHV VKDARERDFT SLENTVEERL TELTKSINDN IAIFTDVQKR
     SQKEINEVKM KVASLEESKG DRSQDVKTLK DAVKEVQASM MSRERDIEAL KSSLQTMESD
     VYTEVRELVS LKQEQQAFKQ AADSERLALQ ALTEKLLRSE ESSSRLPEDI RRLEEELQQL
     KVGAHGSEEG AVFKDSKALE ELQRQIEGLG ARLQYVEDGV YSMQVASARH TESLESLLSK
     SQEYEQRLAM LQEHVGNLGS SSDLASTVRS LGETQLALSS DLKELKQSLG ELPGTVESLQ
     EQVLSLLSQD QAQAEGLPPQ DFLDRLSSLD NLKSSVSQVE SDLKMLRTAV DSLVAYSVKI
     ETNENNLESA KGLLDDLRND LDRLFLKVEK IHEKI
//
ID   TF3C4_MOUSE             Reviewed;         817 AA.
AC   Q8BMQ2; Q8BKZ4;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=General transcription factor 3C polypeptide 4;
DE            EC=2.3.1.48;
DE   AltName: Full=TF3C-delta;
DE   AltName: Full=Transcription factor IIIC 90 kDa subunit;
DE            Short=TFIIIC 90 kDa subunit;
DE            Short=TFIIIC90;
DE   AltName: Full=Transcription factor IIIC subunit delta;
GN   Name=Gtf3c4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Corpus striatum, and Pituitary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-607, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Essential for RNA polymerase III to make a number of
CC       small nuclear and cytoplasmic RNAs, including 5S RNA, tRNA, and
CC       adenovirus-associated (VA) RNA of both cellular and viral origin.
CC       Has histone acetyltransferase activity (HAT) with unique
CC       specificity for free and nucleosomal H3. May cooperate with GTF3C5
CC       in facilitating the recruitment of TFIIIB and RNA polymerase
CC       through direct interactions with BRF1, POLR3C and POLR3F. May be
CC       localized close to the A box (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + [histone] = CoA + acetyl-
CC       [histone].
CC   -!- SUBUNIT: Part of the TFIIIC subcomplex TFIIIC2, consisting of six
CC       subunits, GTF3C1, GTF3C2, GTF3C3, GTF3C4, GTF3C5 and GTF3C6.
CC       Interacts with BRF1, GTF3C1, GTF3C2, GTF3C5, GTF3C6, POLR3C and
CC       POLR3F (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BMQ2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BMQ2-2; Sequence=VSP_010577;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8BMQ2-3; Sequence=VSP_010578;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the TFIIIC subunit 4 family.
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DR   EMBL; AK030351; BAC26916.1; -; mRNA.
DR   EMBL; AK047698; BAC33130.1; -; mRNA.
DR   EMBL; BC061476; AAH61476.1; -; mRNA.
DR   IPI; IPI00223076; -.
DR   IPI; IPI00417149; -.
DR   IPI; IPI00417150; -.
DR   UniGene; Mm.26043; -.
DR   ProteinModelPortal; Q8BMQ2; -.
DR   STRING; Q8BMQ2; -.
DR   PhosphoSite; Q8BMQ2; -.
DR   PRIDE; Q8BMQ2; -.
DR   Ensembl; ENSMUST00000037117; ENSMUSP00000042265; ENSMUSG00000035666.
DR   UCSC; uc008ize.1; mouse.
DR   MGI; MGI:2138937; Gtf3c4.
DR   GeneTree; ENSGT00390000011873; -.
DR   HOGENOM; HBG715456; -.
DR   HOVERGEN; HBG059337; -.
DR   InParanoid; Q8BMQ2; -.
DR   OrthoDB; EOG40CHG9; -.
DR   BRENDA; 2.3.1.48; 244.
DR   NextBio; 392756; -.
DR   ArrayExpress; Q8BMQ2; -.
DR   Bgee; Q8BMQ2; -.
DR   CleanEx; MM_GTF3C4; -.
DR   Genevestigator; Q8BMQ2; -.
DR   GermOnline; ENSMUSG00000035666; Mus musculus.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:EC.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Acetylation; Acyltransferase; Alternative splicing; DNA-binding;
KW   Nucleus; Phosphoprotein; Transcription; Transferase.
FT   CHAIN         1    817       General transcription factor 3C
FT                                polypeptide 4.
FT                                /FTId=PRO_0000209714.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     607    607       Phosphoserine.
FT   VAR_SEQ       1    323       Missing (in isoform 2).
FT                                /FTId=VSP_010577.
FT   VAR_SEQ     270    817       Missing (in isoform 3).
FT                                /FTId=VSP_010578.
FT   CONFLICT     21     21       Q -> E (in Ref. 1; AAH61476).
FT   CONFLICT    703    703       H -> P (in Ref. 1; BAC26916).
SQ   SEQUENCE   817 AA;  91652 MW;  FBEA4197AD75266F CRC64;
     MSEADQALVG PKADEPSPPA QEKDEGGGKE AAADAAPGPS ASFRLMVTRR EPAVKLQYAV
     SGLEPLSWSE DHRVSVSTAR SVAVLELICD VHNPGQDLVI HRTSVPAPLN SCLLKVGSKT
     EVAECKEKFA SSKDPTISQT FMLDRMFNPE GKALPPMRGF KYTSWSPMGC DANGRCLLAA
     LTMDNRLTVQ VNLNRLQWVQ LVDLTEIYGD RLYETSYRLS KNEAPEGNLG DFAEFQRRHS
     MQTPVRMEWS SICTTQQVKH NNECRDVSSV LLAVLFENGN IAVWQFQLPF VGKESISSCN
     TIESGISSPS VLFWWEYEHN NRKMSGLIVG SAFGPVKILP VNLKAVKGYF TLRQPVVLWK
     EMDKLPVHSI KCVPLYHPYQ KCSCSLVVAA RGSYVFWCLL LISKAGLNVH NSHVTGLHSL
     PIVSITADKQ NGTVYTCSSD GKVRQLIPIF TDVALKFEHQ LIKLSDVFGS VRTHGIAVSP
     CGAYLAIITT EGMMNGLHPV NKNYQVQFVT LKTFEEAAAQ LLESSVQNLF KQVDLIDLVR
     WKILKDKHIP QFLHEALEKK IESSGVTYFW RFKLFLLRIL YQSMQKSPSE ALWKPTHEDS
     KILLVDSPGM GDGEDEQQEE GTSKQGTKAG LQEKSKEGDT EETPEDSLTA GGDTGGREPV
     EEKLLEIQGK IEAVEMHLTR EHMKRVLGEV YLHTWITENT SIHTRGLCNF LMSDEDYDDR
     TAQVLIGHIS KKMNKQTFPE RCSLCKEILP FTDRKQAVCS NGHIWLRCFL TYQSCQSLIY
     RRCLLHDSIA RHPVPEDPDW IKRLLQSPCP FCDSPVF
//
ID   ECHA_MOUSE              Reviewed;         763 AA.
AC   Q8BMS1; Q3TCY3; Q5U5Y5; Q8QZU4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Trifunctional enzyme subunit alpha, mitochondrial;
DE   AltName: Full=TP-alpha;
DE   Includes:
DE     RecName: Full=Long-chain enoyl-CoA hydratase;
DE              EC=4.2.1.17;
DE   Includes:
DE     RecName: Full=Long chain 3-hydroxyacyl-CoA dehydrogenase;
DE              EC=1.1.1.211;
DE   Flags: Precursor;
GN   Name=Hadha;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Eye, Liver, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-129; LYS-326; LYS-350;
RP   LYS-569 AND LYS-728, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- FUNCTION: Bifunctional subunit.
CC   -!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-
CC       CoA + H(2)O.
CC   -!- CATALYTIC ACTIVITY: (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA
CC       + NADH.
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC   -!- SUBUNIT: Octamer of 4 alpha (HADHA) and 4 beta (HADHB) subunits
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- PTM: Acetylation of Lys-569 and Lys-728 is observed in liver
CC       mitochondria from fasted mice but not from fed mice.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the enoyl-CoA
CC       hydratase/isomerase family.
CC   -!- SIMILARITY: In the central section; belongs to the 3-hydroxyacyl-
CC       CoA dehydrogenase family.
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DR   EMBL; AK029017; BAC26245.1; -; mRNA.
DR   EMBL; AK170478; BAE41822.1; -; mRNA.
DR   EMBL; AK170683; BAE41956.1; -; mRNA.
DR   EMBL; BC027156; AAH27156.1; -; mRNA.
DR   EMBL; BC037009; AAH37009.1; -; mRNA.
DR   EMBL; BC046978; AAH46978.1; -; mRNA.
DR   EMBL; BC058569; AAH58569.1; -; mRNA.
DR   IPI; IPI00223092; -.
DR   RefSeq; NP_849209.1; NM_178878.2.
DR   UniGene; Mm.200497; -.
DR   HSSP; P14604; 2DUB.
DR   ProteinModelPortal; Q8BMS1; -.
DR   SMR; Q8BMS1; 40-763.
DR   STRING; Q8BMS1; -.
DR   PhosphoSite; Q8BMS1; -.
DR   REPRODUCTION-2DPAGE; IPI00223092; -.
DR   PRIDE; Q8BMS1; -.
DR   Ensembl; ENSMUST00000156859; ENSMUSP00000120976; ENSMUSG00000025745.
DR   GeneID; 97212; -.
DR   KEGG; mmu:97212; -.
DR   NMPDR; fig|10090.3.peg.11342; -.
DR   UCSC; uc008wvc.1; mouse.
DR   CTD; 97212; -.
DR   MGI; MGI:2135593; Hadha.
DR   GeneTree; ENSGT00530000063042; -.
DR   HOGENOM; HBG691737; -.
DR   HOVERGEN; HBG005557; -.
DR   InParanoid; Q8BMS1; -.
DR   OMA; HATTSDE; -.
DR   OrthoDB; EOG4FBHSD; -.
DR   PhylomeDB; Q8BMS1; -.
DR   BRENDA; 1.1.1.211; 244.
DR   BRENDA; 4.2.1.17; 244.
DR   NextBio; 352627; -.
DR   ArrayExpress; Q8BMS1; -.
DR   Bgee; Q8BMS1; -.
DR   Genevestigator; Q8BMS1; -.
DR   GO; GO:0016507; C:fatty acid beta-oxidation multienzyme complex; IEA:InterPro.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; TAS:MGI.
DR   GO; GO:0016509; F:long-chain-3-hydroxyacyl-CoA dehydrogenase activity; IDA:MGI.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IMP:MGI.
DR   InterPro; IPR006180; 3-OHacyl-CoA_DH_CS.
DR   InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR   InterPro; IPR006108; 3HC_DH_C.
DR   InterPro; IPR008927; 6-PGluconate_DH_C-like.
DR   InterPro; IPR001753; Crotonase_core.
DR   InterPro; IPR013328; DH_multihelical.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   InterPro; IPR012803; Fa_ox_alpha_mit.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:1.10.1040.10; Opine_DH; 2.
DR   Pfam; PF00725; 3HCDH; 2.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   Pfam; PF00378; ECH; 1.
DR   SUPFAM; SSF48179; 6DGDH_C_like; 2.
DR   TIGRFAMs; TIGR02441; fa_ox_alpha_mit; 1.
DR   PROSITE; PS00067; 3HCDH; 1.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Fatty acid metabolism; Lipid metabolism; Lyase;
KW   Mitochondrion; Multifunctional enzyme; NAD; Oxidoreductase;
KW   Transit peptide.
FT   TRANSIT       1     36       Mitochondrion (Potential).
FT   CHAIN        37    763       Trifunctional enzyme subunit alpha,
FT                                mitochondrial.
FT                                /FTId=PRO_0000322639.
FT   SITE        151    151       Important for catalytic activity (By
FT                                similarity).
FT   SITE        173    173       Important for catalytic activity (By
FT                                similarity).
FT   MOD_RES     129    129       N6-acetyllysine.
FT   MOD_RES     295    295       N6-acetyllysine (By similarity).
FT   MOD_RES     303    303       N6-acetyllysine (By similarity).
FT   MOD_RES     326    326       N6-acetyllysine.
FT   MOD_RES     350    350       N6-acetyllysine.
FT   MOD_RES     353    353       N6-acetyllysine (By similarity).
FT   MOD_RES     359    359       N6-acetyllysine (By similarity).
FT   MOD_RES     406    406       N6-acetyllysine (By similarity).
FT   MOD_RES     505    505       N6-acetyllysine (By similarity).
FT   MOD_RES     540    540       N6-acetyllysine (By similarity).
FT   MOD_RES     569    569       N6-acetyllysine.
FT   MOD_RES     644    644       N6-acetyllysine (By similarity).
FT   MOD_RES     728    728       N6-acetyllysine.
FT   CONFLICT    196    196       A -> D (in Ref. 1; BAE41822).
FT   CONFLICT    459    459       L -> S (in Ref. 2; AAH37009).
SQ   SEQUENCE   763 AA;  82670 MW;  73D203795D5C1141 CRC64;
     MVASRAIGSL SRFSAFRILR SRGCICRSFT TSSALLTRTH INYGVKGDVA VIRINSPNSK
     VNTLNKEVQS EFIEVMNEIW ANDQIRSAVL ISSKPGCFVA GADINMLSSC TTPQEATRIS
     QEGQRMFEKL EKSPKPVVAA ISGSCLGGGL ELAIACQYRI ATKDRKTVLG VPEVLLGILP
     GAGGTQRLPK MVGVPAAFDM MLTGRNIRAD RAKKMGLVDQ LVEPLGPGIK SPEERTIEYL
     EEVAVNFAKG LADRKVSAKQ SKGLVEKLTT YAMTVPFVRQ QVYKTVEEKV KKQTKGLYPA
     PLKIIDAVKA GLEQGSDAGY LAESQKFGEL ALTKESKALM GLYNGQVLCK KNKFGAPQKN
     VQQLAILGAG LMGAGIAQVS VDKGLKTLLK DTTVTGLGRG QQQVFKGLND KVKKKALTSF
     ERDSIFSNLI GQLDYKGFEK ADMVIEAVFE DLGVKHKVLK EVESVTPEHC IFASNTSALP
     INQIAAVSKR PEKVIGMHYF SPVDKMQLLE IITTDKTSKD TTASAVAVGL RQGKVIIVVK
     DGPGFYTTRC LAPMMSEVMR ILQEGVDPKK LDALTTGFGF PVGAATLADE VGVDVAQHVA
     EDLGKAFGER FGGGSVELLK QMVSKGFLGR KSGKGFYIYQ EGSKNKSLNS EMDNILANLR
     LPAKPEVSSD EDVQYRVITR FVNEAVLCLQ EGILATPAEG DIGAVFGLGF PPCLGGPFRF
     VDLYGAQKVV DRLRKYESAY GTQFTPCQLL LDHANNSSKK FYQ
//
ID   Q8BN38_MOUSE            Unreviewed;      1310 AA.
AC   Q8BN38;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   11-JAN-2011, entry version 40.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Lyst;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK089635; BAC40935.1; -; mRNA.
DR   IPI; IPI00399954; -.
DR   UniGene; Mm.342337; -.
DR   STRING; Q8BN38; -.
DR   Ensembl; ENSMUST00000050664; ENSMUSP00000059413; ENSMUSG00000019726.
DR   Ensembl; ENSMUST00000110559; ENSMUSP00000106188; ENSMUSG00000019726.
DR   MGI; MGI:107448; Lyst.
DR   HOGENOM; HBG714194; -.
DR   HOVERGEN; HBG106635; -.
DR   InParanoid; Q8BN38; -.
DR   ArrayExpress; Q8BN38; -.
DR   Bgee; Q8BN38; -.
DR   Genevestigator; Q8BN38; -.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0007596; P:blood coagulation; IMP:MGI.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
DR   GO; GO:0042832; P:defense response to protozoan; IMP:MGI.
DR   GO; GO:0051607; P:defense response to virus; IMP:MGI.
DR   GO; GO:0030595; P:leukocyte chemotaxis; IMP:MGI.
DR   GO; GO:0007040; P:lysosome organization; IMP:MGI.
DR   GO; GO:0033364; P:mast cell secretory granule organization; IMP:MGI.
DR   GO; GO:0032438; P:melanosome organization; IMP:MGI.
DR   GO; GO:0007017; P:microtubule-based process; IMP:MGI.
DR   GO; GO:0002446; P:neutrophil mediated immunity; IMP:MGI.
DR   GO; GO:0055091; P:phospholipid homeostasis; IMP:MGI.
DR   GO; GO:0006644; P:phospholipid metabolic process; IMP:MGI.
DR   GO; GO:0032816; P:positive regulation of natural killer cell activation; IMP:MGI.
DR   GO; GO:0042493; P:response to drug; IMP:MGI.
DR   GO; GO:0033299; P:secretion of lysosomal enzymes; IMP:MGI.
DR   GO; GO:0002456; P:T cell mediated immunity; IMP:MGI.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
FT   NON_TER    1310   1310
SQ   SEQUENCE   1310 AA;  146043 MW;  1E1E97EBBBC45BFA CRC64;
     NAVVQRAEAR EEEEEETHMA TLGQYLVHGR GFLLLTKLNS IIDQALTCRE ELLTLLLSLL
     PLVWKIPVQE QQATDFNLPL SSDIILTKEK NSSLQKSTQG KLYLEGSAPS GQVSAKVNLF
     RKIRRQRKST HRYSVRDARK TQLSTSDSEG NSDEKSTVVS KHRRLHALPR FLTQSPKEGH
     LVAKPDPSAT KEQVLSDTMS VENSREVILR QDSNGDILSE PAALSILSNM NNSPFDLCHV
     LLSLLEKVCK FDIALNHNSS LALSVVPTLT EFLAGFGDCC NQSDTLEGQL VSAGWTEEPV
     ALVQRMLFRT VLHLMSVDVS TAEAMPESLR KNLTELLRAA LKIRACLEKQ PEPFSPRQKK
     TLQEVQEGFV FSKYRHRALL LPELLEGVLQ LLISCLQSAA SNPFYFSQAM DLVQEFIQHQ
     GFNLFETAVL QMEWLLSRDG VPSEAAEHLK ALINSVIKIM STVKKVKSEQ LHHSMCTRKR
     HRRCEYSHFM QHHRDLSGLL VSAFKNQLSK SPFEETAEGD VQYPERCCCI AVCAHQCLRL
     LQQVSLSTTC VQILSGVHSV GICCCMDPKS VIVPLLHAFK LPALKAFQQH ILNVLSKLLL
     DQLGGAELSP RIKKAACNIC TVDSDQLAKL GETLQGTLCG AGPTSGLPSP SYRFQGILPS
     SGSEDLLWKW DALEAYQSFV FQEDRLHNIQ IANHICNLIQ KGNVVVQWKL YNYIFNPVLQ
     RGVELVHHCQ QLSIPSAQTH MCSQLKQYLP QEVLQIYLKT LPVLLKSRVI RDLFLSCNGV
     NQIIELNYLD GIRSHSLKAF ETLIVSLGEQ QKDAAVLDVD GLDIQQELPS LSVGPSLHKQ
     QASSDSPCSL RKFYASLREP DPKKRKTIHQ DVHINTINLF LCVAFLCVSK EADSDRESAN
     ESEDTSGYDS TASEPLSHML PCLSLENVVL PSPECLHHAA DIWSMCRWIY MLNSVFQKQF
     HRLGGFQVCH ELIFMIIQKL FRSHTEDQGR RQGEMSRNEN QELIRISYPE LTLKGDVSSA
     TAPDLGFLRK SADSVRGFQS QPVLPTSAEQ IVATESVPGE RKAFMSQQSE TSLQSIRLLE
     SLLAICLHSA RACQQKMELE LPSQGLSVEN ILCELREHLS QSKVAETELA KPLFDALLRV
     ALGNHSADLG PGDAVTEKSH PSEEELLSQP GDFSEEAEDS QCCSLKLLGE EEGYEADSES
     NPEDVDTQDD GVELNPEAEG FSGSIVSNNL LENLTHGEII YPEICMLGLN LLSASKAKLD
     VLAHVFESFL KIVRQKEKNI SLLIQQGTVK ILLGGFLNIL TQTNSDFQAC
//
ID   FAT3_MOUSE              Reviewed;        4555 AA.
AC   Q8BNA6; Q08ED4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Protocadherin Fat 3;
DE   AltName: Full=FAT tumor suppressor homolog 3;
DE   Flags: Precursor;
GN   Name=Fat3; Synonyms=Gm1132, Gm510;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1464-4555 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   POSSIBLE FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=16059920; DOI=10.1002/dvdy.20515;
RA   Rock R., Schrauth S., Gessler M.;
RT   "Expression of mouse dchs1, fjx1, and fat-j suggests conservation of
RT   the planar cell polarity pathway identified in Drosophila.";
RL   Dev. Dyn. 234:747-755(2005).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=17131403; DOI=10.1002/dvdy.21030;
RA   Nagae S., Tanoue T., Takeichi M.;
RT   "Temporal and spatial expression profiles of the Fat3 protein, a giant
RT   cadherin molecule, during mouse development.";
RL   Dev. Dyn. 236:534-543(2007).
CC   -!- FUNCTION: May play a role in the interactions between neurites
CC       derived from specific subsets of neurons during development.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BNA6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BNA6-2; Sequence=VSP_032330, VSP_032331;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8BNA6-3; Sequence=VSP_032329, VSP_032332, VSP_032333;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Restricted to the nervous system, mainly in
CC       brain. In brain, it is highly expressed in the olfactory bulb and
CC       retina. In the developing olfactory bulb, it localizes along the
CC       dendrites of these cells as well as in their axons to some extent.
CC       In retina, it cocentrates in the inner plexiform layer throughout
CC       development (at protein level).
CC   -!- SIMILARITY: Contains 33 cadherin domains.
CC   -!- SIMILARITY: Contains 4 EGF-like domains.
CC   -!- SIMILARITY: Contains 1 laminin G-like domain.
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DR   EMBL; AC154406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC161370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC161421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC162903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC117744; AAI17745.1; -; mRNA.
DR   EMBL; AK084245; BAC39147.1; -; mRNA.
DR   IPI; IPI00357173; -.
DR   IPI; IPI00828569; -.
DR   IPI; IPI00889292; -.
DR   UniGene; Mm.195010; -.
DR   ProteinModelPortal; Q8BNA6; -.
DR   SMR; Q8BNA6; 49-1457, 1474-1668, 2278-2391, 2702-3548, 3796-3828, 3835-4135.
DR   PhosphoSite; Q8BNA6; -.
DR   PRIDE; Q8BNA6; -.
DR   Ensembl; ENSMUST00000082170; ENSMUSP00000080808; ENSMUSG00000074505.
DR   Ensembl; ENSMUST00000098977; ENSMUSP00000096576; ENSMUSG00000074505.
DR   MGI; MGI:2444314; Fat3.
DR   eggNOG; roNOG11369; -.
DR   GeneTree; ENSGT00600000084230; -.
DR   HOGENOM; HBG444162; -.
DR   HOVERGEN; HBG005641; -.
DR   InParanoid; Q8BNA6; -.
DR   OrthoDB; EOG4CNQQ3; -.
DR   ArrayExpress; Q8BNA6; -.
DR   Bgee; Q8BNA6; -.
DR   CleanEx; MM_FAT3; -.
DR   Genevestigator; Q8BNA6; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR001881; EGF_Ca-bd.
DR   InterPro; IPR013091; EGF_Ca-bd_2.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR012680; Laminin_G_2.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 34.
DR   Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 1.
DR   Pfam; PF00028; Cadherin; 27.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF02210; Laminin_G_2; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 32.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00282; LamG; 1.
DR   SUPFAM; SSF49313; Cadherin; 34.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00232; CADHERIN_1; 19.
DR   PROSITE; PS50268; CADHERIN_2; 32.
DR   PROSITE; PS00022; EGF_1; 3.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell adhesion; Developmental protein;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     31       Potential.
FT   CHAIN        32   4555       Protocadherin Fat 3.
FT                                /FTId=PRO_0000324635.
FT   TOPO_DOM     32   4153       Extracellular (Potential).
FT   TRANSMEM   4154   4174       Helical; (Potential).
FT   TOPO_DOM   4175   4555       Cytoplasmic (Potential).
FT   DOMAIN       43    157       Cadherin 1.
FT   DOMAIN      158    262       Cadherin 2.
FT   DOMAIN      263    374       Cadherin 3.
FT   DOMAIN      376    471       Cadherin 4.
FT   DOMAIN      472    577       Cadherin 5.
FT   DOMAIN      578    680       Cadherin 6.
FT   DOMAIN      726    830       Cadherin 7.
FT   DOMAIN      831    935       Cadherin 8.
FT   DOMAIN      936   1042       Cadherin 9.
FT   DOMAIN     1043   1147       Cadherin 10.
FT   DOMAIN     1148   1253       Cadherin 11.
FT   DOMAIN     1254   1358       Cadherin 12.
FT   DOMAIN     1362   1459       Cadherin 13.
FT   DOMAIN     1460   1565       Cadherin 14.
FT   DOMAIN     1566   1768       Cadherin 15.
FT   DOMAIN     1769   1882       Cadherin 16.
FT   DOMAIN     1883   1985       Cadherin 17.
FT   DOMAIN     1982   2083       Cadherin 18.
FT   DOMAIN     2084   2185       Cadherin 19.
FT   DOMAIN     2186   2286       Cadherin 20.
FT   DOMAIN     2287   2393       Cadherin 21.
FT   DOMAIN     2394   2495       Cadherin 22.
FT   DOMAIN     2496   2599       Cadherin 23.
FT   DOMAIN     2600   2707       Cadherin 24.
FT   DOMAIN     2708   2813       Cadherin 25.
FT   DOMAIN     2814   2923       Cadherin 26.
FT   DOMAIN     2924   3028       Cadherin 27.
FT   DOMAIN     3029   3130       Cadherin 28.
FT   DOMAIN     3131   3235       Cadherin 29.
FT   DOMAIN     3236   3340       Cadherin 30.
FT   DOMAIN     3341   3445       Cadherin 31.
FT   DOMAIN     3446   3550       Cadherin 32.
FT   DOMAIN     3551   3660       Cadherin 33.
FT   DOMAIN     3794   3832       EGF-like 1.
FT   DOMAIN     3834   4017       Laminin G-like.
FT   DOMAIN     4020   4057       EGF-like 2.
FT   DOMAIN     4059   4095       EGF-like 3.
FT   DOMAIN     4097   4133       EGF-like 4; calcium-binding (Potential).
FT   COMPBIAS   4404   4466       Pro-rich.
FT   CARBOHYD     48     48       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    341    341       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    481    481       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    562    562       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    667    667       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    799    799       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    879    879       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    898    898       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1006   1006       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1367   1367       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1429   1429       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1751   1751       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1944   1944       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1993   1993       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1996   1996       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2208   2208       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2292   2292       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2331   2331       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2467   2467       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2734   2734       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3000   3000       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3201   3201       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3449   3449       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3618   3618       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3741   3741       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3926   3926       N-linked (GlcNAc...) (Potential).
FT   DISULFID   3798   3809       By similarity.
FT   DISULFID   3803   3821       By similarity.
FT   DISULFID   3823   3831       By similarity.
FT   DISULFID   3984   4017       By similarity.
FT   DISULFID   4024   4035       By similarity.
FT   DISULFID   4029   4045       By similarity.
FT   DISULFID   4047   4056       By similarity.
FT   DISULFID   4063   4074       By similarity.
FT   DISULFID   4068   4083       By similarity.
FT   DISULFID   4085   4094       By similarity.
FT   DISULFID   4101   4112       By similarity.
FT   DISULFID   4106   4121       By similarity.
FT   DISULFID   4123   4132       By similarity.
FT   VAR_SEQ       1   3806       Missing (in isoform 3).
FT                                /FTId=VSP_032329.
FT   VAR_SEQ    1538   1591       RDQEFPYRRNLARVIVNVEDANDHSPYFTNPLYEASVFESA
FT                                ALGSVVLQVTALD -> GPDLGFCSPGRTVNQPRHIPQEAR
FT                                AFKFYRPSFCTARLHAVLPLYFNEEVTVLR (in
FT                                isoform 2).
FT                                /FTId=VSP_032330.
FT   VAR_SEQ    1592   4555       Missing (in isoform 2).
FT                                /FTId=VSP_032331.
FT   VAR_SEQ    4043   4121       YQCSCLSQFTGTNCESEITACFPNPCRNGGSCDPIGNTFVC
FT                                SCKAGLTGVTCEDDVDECEREECENGGSCVNLFGSFFC ->
FT                                ECTSVQARGGSAPEVCPLHSQPLPPSPGPSQKGWSFGYNFT
FT                                SAFMGWRSGPAMVGRELRGRGLWSTLEKRGEGTWGNLN
FT                                (in isoform 3).
FT                                /FTId=VSP_032332.
FT   VAR_SEQ    4122   4555       Missing (in isoform 3).
FT                                /FTId=VSP_032333.
SQ   SEQUENCE   4555 AA;  502011 MW;  4E23122CCAC98DDD CRC64;
     MSVTMGHCMG TKPPSCIILL LLKLFATVSQ GLPGTGPLGF HFTHSTYNAT VYENSAARTY
     VNSQSRMGIT LIDLSWDIKY RIVSGDEEGF FKAEEVIIAD FCFLRIRTKG GNSAILNREI
     QDNYLLIIKG SVRGEDLEAW TKVNIQVLDM NDLRPLFSPT TYSVTIAEST PLRTSVAQVT
     ATDADIGSNG EFYYYFKNKV DLFSVHPTSG VISLSGRLNY DEKNRYDLEI LAVDRGMKLY
     GNNGVSSTAK LYVHIERINE HAPIIHVVSH TPFSLDKEPT YAVVTVDDLD EGANGEIESL
     SIVDGDPLEQ FFLAKEGKWL NEYKVKERRQ VDWESFSYGY NLTIQAKDKG SPQKFSELKT
     VHIANPRRDN TPVRFEKDVY EVSISEFSPP GVLVAIVKVS PEPLDVEYKL LPGKDSDYFK
     INPRSGLIVT AQPLNTVKKE VYKLEVSDKE GDAKAQVTIG IEDANDHTPE FQEALYETFV
     NESVRVGTNV LTVSASDKDK GENGYITYSI ASLNLLPFAI NQFTGVISTT EELDFESSPE
     TYRFIVRASD WGSPYRHESE VNVTIRVGNV NDNSPLFEKV ACQGVISYDF PVGGHITAIS
     AIDIDELELV KYKIISGNEL GFFYLNPDSG VLQLKKSLMN SGIKNGNFAL RITATDGENF
     ADPMAINISV LHGKVSSKSF SCRETRVAQK LAEKLLIKAK ANGKLNLEDG FLDFYSINRQ
     GPHFDKSFPS DVAVKEDMLV GTNILKIKAY DADSGFNGKV LFTISDGNTD SCFNIDMETG
     QLKVLMPMDR EHTDLYVLNI TIYDLGKPQK SSWRLLTVNV EDANDNNPVF LQDSYSVSIL
     ESSSIGTEII QVEARDKDLG SNGEVMYSVL TDTHQFIINS STGIVYIADQ LDRESKANYS
     LKIEARDKAE SGQQLFSVVT LKIFLDDVND CSPAFIPSSY SVKVLEDLPV GTVIAWLETQ
     DPDLGLGGQV RYSLVNDYNG RFEVDKASGA IRLSKELDYE KQQFYNLTVR AKDKGRPVSL
     SSVSFVEVEV VDVNENLHTP YFPDFAVVGS VKENSRIGTS VLQVTAHDED SGRDGEIQYS
     IRDGSGLGRF NIDDESGVIT AADSLDRETT ASYWLTVYAT DRGVVPLYST IEVYIEVEDV
     NDNAPLTSEP IYYPVVMENS PKDVSVIQIQ AEDPDSGSNE KLTYRITSGN PQNFFAINIK
     TGLITTTSRK LDREQQAEHF LEVTVTDGGS SPKQSTIWVV VQVLDENDNR PQFPEKVYQI
     KLPERDRKKR GEPIYRAFAF DKDEGPNAEI SYSIVDGNDD GKFFIDPKTG MVSSRKQFTA
     GSYDILTIKA VDNGRPQKSS TARLHIEWIK KPPPSPIPLT FDEPFYNFTV MESDKVTEIV
     GVVSVQPANT PLWFDIVGGN FDSSFDAEKG VGTIVIAKPL DAEQRSVYNM SVEVTDGTNI
     AVTQVFIKVL DNNDNGPEFS QPHYDVTISE DVLPDTEILQ IEATDRDEKH KLSYTIHSSI
     DAVSMRKFRM DPSTGVLYTA ERLDHEAQDK HILNIMVRDQ EFPYRRNLAR VIVNVEDAND
     HSPYFTNPLY EASVFESAAL GSVVLQVTAL DKDKGENAEL IYSIEAGNTG NTFKIEPVLG
     IITISKEPDM AAMGQFVLSV KVTDQGSPPM SATAIVRISI SMSDNSHPKF THKDYQAEVN
     ENVDIGTSVI LISAISQSTL IYEVKDGNIN GVFTINPYSG VITTRRALDY EHTSSYQLII
     QATNMAGMAS NATISVQIVD ENDNPPVFLF SQYSGSLSEA APINSIVRSL DNSPLVIRAT
     DADSNQNALL VYQIVESTAK KFFTVDSSTG AIRTIANLDH EAIAHFHFHV HVRDSGNPQL
     TAESPVEVNI EVTDVNDNPP VFTQAVFETV LLLPTYIGVE VLKVSATDPD SEVPPELTYS
     LMEGSVDNFL MDPNTGVLTI KNNNLSKDHY MLIVRVSDGK FYSTAMVTVM VKEAMDSGLH
     FTQSFYSTSI SENSTNITKV AIVNAVGNRL NEPLKYSILN PGNKFKIKST SGVIQTTGVP
     FDREEQELYE LVVEASRELD HLRVARVVVR VNIEDVNDNS PVFVGLPYYA AVQVDAEPGT
     LIYRVTAIDK DKGANGEVTY VLQDDYGHFE INPNSGNVIL REAFNSDLSN IDYGVTILAK
     DGGNPSLSTF VELPITIVNK AMPVFDKPFY TASINEDITM NTPILSINAT SPEGQGIIYL
     IIDGDPFQQF NIDFDTGVLK VISPLDYEVT SVYKLTVRAS DALTGARAEV TVDLLVDDIN
     DNPPVFDQPT YNTTLSESSL IGTPVLQLVS TDADSGNNKL VRYQIVQDTY NSTDYFHIDS
     SSGLILTARM LDHELVQHCT LKVTATDNGF PSLSSEVLVQ IYISDVNDNP PVFNQLIYES
     YVSELAPRGH FVTCVQASDA DSSDLDRLEY SILSGNDRAS FLMDSKSGVL TLSSHRKQRM
     EPLYSLNVSV SDGLFTSTAQ VHIRVLGANL YSPAFSQSTY VAEVRENAAS GTKVIHVRAT
     DGDPGTYGQV SYSIINDFAK DRFLIDSNGQ IITTERLDRE NPLEGDISIY LRALDGGGRT
     TFCTVRVIVV DENDNAPQFM TVEYRASVRA DVGRGHLVTQ VQALDPDDGA NSRITYSLYS
     EASVSVADLL EIDPDNGWMV TKGNFNQLRN TVLSFFVKAV DGGIPVRHSL IPVYIHVLPP
     ETFLPSFTQS QYSFTITEDT SIGSTVDTLR ILPNQSVRFS MVNGERPENN KEGVFIIEQE
     TGAIKLDKRL DHEVSPAFHF KVAATIPLDK VDIVFTVDVD VKVLDLNDNK PVFETSTYET
     IIMEGMPVGT KLAQVRAIDM DWGANGQVTY SLHSDSHLEK VIEAFNIDSN TGWISTLKDL
     DHETDPAFSF FVVASDLGEA FSLSSMALVS VKVTDINDNA PVFAHEVYRG NVKESDPPGE
     VVAVLSTLDK DTSNINRQVS YHITGGNPRG QFALGMVQSE WKVYVKRPLD REEQDIYFLN
     ITASDGLFVT QAMVEVTVSD VNDNSPVCDQ VAYSASLPED IPSNKIILKV SAKDADIGSN
     GDIRYSLYGS GNNEFFLDPE SGELKTLAVL DRERVPVYNL IARATDGGGR FCSSSVLLLL
     EDVNDNPPVF SSNHYTACVY ENTATKALLT RVQAMDPDVG INRKVVYSLE DSASGVFSID
     SSSGVIVLEQ PLDREQQSSY NISVRATDQS PGQSLSSLAS VTITVLDIND NPPVFERRDY
     LVTVPEDTSL GTQVLSVFAT SKDIGTNAEI TYLIRSGNEQ GKFSINPKTG GISVLEALDY
     ETCRRFYLVV EAKDGGTPAL STAATVSIDL TDVNDNPPRF SQDVYSAVIS EDALEGDSVI
     LLIAEDVDSK PNGQIRFSIV GGDRDNEFAV DPILGLVKVK KKLDRERVSG YSLLIQAVDS
     GIPAMSSTTT VNIDISDVND NSPVFTPANY TAVIQENKPV GTSILQLVVT DRDSFHNGPP
     FSFSILSGNE DEEFMLDSHG ILRSAVVFRH MESPEYLLCI QAKDSGKPQQ VSHTYIRVRV
     IEESTHKPTA IPLEIFIVTM EDDFPGGVIG KIHATDQDMY DVLTFALKSE QKSLFKVNSH
     DGKIIALGGL DSGKYVLNVS VSDGRFQVPI DVVVHVEQLV HEMLQNTVTI RFEDVSPEDF
     VGLHMHGFRR ILRNAVLTQK QDSLRIISIQ PVVGTNQLDM LFAVEMHSSE FYKPAYLIQK
     LSNARRHLEN VMHIAAILEK NCSGLDCQEQ HCEQGLSLDS HALMTYSTAR ISFVCPRFYR
     NVRCTCNGGV CPGSNDPCVE KPCPEDMQCV GYEASRRPFL CQCPPGKLGE CSGHTSLSFA
     GNSYIKYRLS ENSKEEDFKL ALRLRTLQSN GIIMYTRANP CMILKIVEGK LWFQLDCGSG
     PGILGISSRA VNDGSWHSVF LELNRNFTSL ALDDSYVERR RAPLYFQTLS TDSAIFFGAL
     VQADNVRSLT DTRVTQVLGG FQGCLDSVVL NHYELPLQNK RSSFAEVVGL TELKLGCVLY
     PDACQRSPCL HGGSCSSLPS GGYQCSCLSQ FTGTNCESEI TACFPNPCRN GGSCDPIGNT
     FVCSCKAGLT GVTCEDDVDE CEREECENGG SCVNLFGSFF CNCTPGYVGQ YCGLRPVVVP
     NIQAGHSYVG KEELIGIAVV LFVIFTLIVL FIVFRKKVFR KNYSRNNITL VQDPATAALL
     HKSNGIPFRS LRAGDGRNVY QEVGPPQVPV RPMAYTPCFQ SDSRSNLDKG LDVLGGEPQE
     MSTFHPESPR ILTARRGVVV CSVAPNLPAV SPCRSDCDSI RKNGWDTGSE NKGTEDTGEV
     TCFTNSNKGS NSEVQSLSSF QSDSGDDNAY HWDTSDWMPG ARLSDIEEMP NYESQDGGAA
     HQGSTRELES DYYLGGYDID SEYPPPHEEE FLSRDQLPPP LPEDFPDQYE ALPPSQPTSL
     TSTMSPDCRR RPRFHPSQYL PPHPLPGETD LGGPSSSCDF STFAVNMNQG TEVMAPTDSV
     SLSLHNSRGT SSSEMSARCG FDDSEVAMSD YESAGELSLT NLHIPFVETQ QQTQV
//
ID   Q8BNF7_MOUSE            Unreviewed;      1203 AA.
AC   Q8BNF7;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 2.
DT   08-FEB-2011, entry version 48.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Herc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK083823; BAC39029.2; -; mRNA.
DR   IPI; IPI00553400; -.
DR   UniGene; Mm.244179; -.
DR   STRING; Q8BNF7; -.
DR   PRIDE; Q8BNF7; -.
DR   Ensembl; ENSMUST00000042824; ENSMUSP00000044801; ENSMUSG00000038664.
DR   Ensembl; ENSMUST00000043618; ENSMUSP00000043920; ENSMUSG00000038664.
DR   Ensembl; ENSMUST00000098618; ENSMUSP00000096218; ENSMUSG00000038664.
DR   UCSC; uc009qep.1; mouse.
DR   MGI; MGI:2384589; Herc1.
DR   GeneTree; ENSGT00590000082801; -.
DR   HOGENOM; HBG445368; -.
DR   InParanoid; Q8BNF7; -.
DR   PhylomeDB; Q8BNF7; -.
DR   ArrayExpress; Q8BNF7; -.
DR   Bgee; Q8BNF7; -.
DR   Genevestigator; Q8BNF7; -.
DR   InterPro; IPR000408; Reg_chr_condens.
DR   InterPro; IPR009091; Reg_csome_cond/b-lactamase_inh.
DR   Gene3D; G3DSA:2.130.10.30; Reg_csome_cond/b-lactamase_inh; 1.
DR   Pfam; PF00415; RCC1; 6.
DR   PRINTS; PR00633; RCCNDNSATION.
DR   SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR   PROSITE; PS00626; RCC1_2; 2.
DR   PROSITE; PS50012; RCC1_3; 7.
PE   2: Evidence at transcript level;
KW   Repeat.
FT   NON_TER    1203   1203
SQ   SEQUENCE   1203 AA;  130775 MW;  6B2FA2EEEF45EB3A CRC64;
     MATMVPPVKL KWLEHLNSSW ITEDSESIAT REGVTVLYSK LISNKEVVPL PQQVLCLKGP
     QLPDFERESL SSDEQDHYLD ALLSSQLALA KMVCSDSPFA GAIRKRLLVL QRVFYALSNK
     YHDKGKVKQQ QHSPESSSGS ADVHSVSERP RSSTDALIEM GVRTGLSLLF ALLRQSWMMP
     VSGPGLSLCN DVIHTAIEVV SSLPPLSLAN ESKIPPMGLD CLSQVTTFLK GVTIPNSGAD
     TLGRRLASEL LLGLPAQRGS LRYLLEWIEM ALGASPVVYT MEKNKLLSSQ EGMISFDCFM
     AILMQMRRSL GSSADRSQWR EPTRTSEGLC SLYEAALCLF EEVCRMASDY SRTCASPDSI
     QTGDAPIVSE TCEVYVWGSN SSHQLVEGTQ EKILQPKLAP SFSDAQTIEA GQYCTFVIST
     DGSVRACGKG SYGRLGLGDS NNQSTLKKLT FEPHRSIKKV SSSKGSDGHT LAFTTEGEVF
     SWGDGDYGKL GHGNSSTQKY PKLIQGPLQG KVVVCVSAGY RHSAAVTEDG ELYTWGEGDF
     GRLGHGDSNS RNIPTLVKDI SNVGEVSCGS SHTIALSKDG RTVWSFGGGD NGKLGHGDTN
     RVYKPKVIEA LQGMFIRKVC AGSQSSLALT STGQVYAWGC GACLGCGSSE ATALRPKLIE
     ELAATRIVDI SIGDSHCLSL SHDNEVYAWG NNSMGQCGQG NSTGPITKPK KVSGLDGIAI
     QQISAGTSHS LAWTALPRDR QVVAWHRPYC VDLEESTFSH LRSFLERYCD KINSEIPPLP
     FPSSREHHNF LKLCLKLLSN HLALALAGGV ATSILGRQAG PLRNLLFRLM DSTVPDEIQE
     VVIETLSVGA TMLLPPLRER MELLHSLLPQ GPDRWESLSK GQRMQLDIIL TSLQDHTHVA
     SLLGYSSPSD AADLSTVCMG YGNLSDQPYG SQICHPDTHL AEILMKTLLR NLGFYTDQAF
     GELEKNSDKY LLGTSSSENS QPAHLHELLC SLQKQLLAFC HINNVTENSS SVALLHKHLQ
     LLLPHATDIY SRSANLLKES PWNGSVGEKL RDVIYVSAAG SMLCQIVNSL LLLPVSVARP
     LLSYLLDLLP PLDCLNRLLP AAALLEDQEL QWPLHGGPEV IDPAGVPLPQ PAQSWVWLVD
     LERTIALLIG RCLGGMLQGS PVSPEEQDTA YWMKTPLFSD GVEMDTPQLD KCMSCLLEVA
     LSG
//
ID   Q8BNI6_MOUSE            Unreviewed;       611 AA.
AC   Q8BNI6;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   SubName: Full=Translocase of outer mitochondrial membrane 70 homolog A (Yeast);
GN   Name=Tomm70a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body, and Bone marrow;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body, and Bone marrow;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body, and Bone marrow;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body, and Bone marrow;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body, and Bone marrow;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body, and Bone marrow;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body, and Bone marrow;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [12]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Whole body;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC057096; AAH57096.1; -; mRNA.
DR   EMBL; BC139420; AAI39421.1; -; mRNA.
DR   EMBL; BC139421; AAI39422.1; -; mRNA.
DR   EMBL; AK083586; BAC38960.1; -; mRNA.
DR   EMBL; AK145458; BAE26448.1; -; mRNA.
DR   EMBL; AK150429; BAE29552.1; -; mRNA.
DR   IPI; IPI00751137; -.
DR   RefSeq; NP_613065.2; NM_138599.5.
DR   UniGene; Mm.213292; -.
DR   HSSP; P31948; 1ELW.
DR   ProteinModelPortal; Q8BNI6; -.
DR   SMR; Q8BNI6; 115-602.
DR   STRING; Q8BNI6; -.
DR   PRIDE; Q8BNI6; -.
DR   Ensembl; ENSMUST00000023433; ENSMUSP00000023433; ENSMUSG00000022752.
DR   GeneID; 28185; -.
DR   KEGG; mmu:28185; -.
DR   UCSC; uc007zmz.1; mouse.
DR   CTD; 28185; -.
DR   MGI; MGI:106295; Tomm70a.
DR   HOVERGEN; HBG062335; -.
DR   InParanoid; Q8BNI6; -.
DR   OMA; CDAAYAQ; -.
DR   NextBio; 306774; -.
DR   ArrayExpress; Q8BNI6; -.
DR   Bgee; Q8BNI6; -.
DR   Genevestigator; Q8BNI6; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR001440; TPR-1.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 4.
DR   Pfam; PF00515; TPR_1; 2.
DR   SMART; SM00028; TPR; 10.
DR   PROSITE; PS50005; TPR; 7.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Repeat; TPR repeat.
SQ   SEQUENCE   611 AA;  67590 MW;  5103C658D8BF9C53 CRC64;
     MAASKPIEAA MAAAAAPGSG NGVGGGGGTA GPGSGAGTLP RWHVALAIGA PLLLGAGAMY
     LWSRRRRRRE AGGRGDASGL KRNSERKTPE GRASPALGSG HHDGSGDSLE MSSLDRAQAA
     KNKGNKYFKA GKYEQAIQCY TEAISLCPTE KNVDLSTFYQ NRAAAFEQLQ KWKEVAQDCT
     KAVELNPKYV KALFRRAKAH EKLDNKKECL EDVTAVCILE GFQNEQSMLL ADKVLKLLGK
     ENAKEKYKNR EPLMPSPQFI KSYFSSFTDD IISQPMLKGE KSDEDKDKEG EALEVKENSG
     YLKAKQYMEE ENYDKIISEC SKEIDAQGKY MAEALLLRAT FYLLIGSANA AKPDLDKVIS
     LKEANVKLRA NALIKRGTMC MQQQQPMLST QDFNMAAEID PMNSDVYHHR GQLKILLDLV
     EEAVADFDAC IRLRPKFALA QAQKCFALYR QAYTANNSSQ VQAAMKGFEE IIKKFPRCAE
     GYALYAQALT DQQQFGKADE MYDKCIDLEP DNATTYVHKG LLQLQWKQDL DKGLELISKA
     IEIDNKCDFA YETMGTIEVQ RGNMEKAIDM FNKAINLAKS EMEMAHLYSL CDAAHAQTEV
     AKKYGLKPPT L
//
ID   NETO2_MOUSE             Reviewed;         525 AA.
AC   Q8BNJ6; B2RX93; Q5VM49; Q8C4Q8;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Neuropilin and tolloid-like protein 2;
DE   AltName: Full=Brain-specific transmembrane protein containing 2 CUB and 1 LDL-receptor class A domains protein 2;
DE   Flags: Precursor;
GN   Name=Neto2; Synonyms=Btcl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), MEMBRANE TOPOLOGY, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15464227; DOI=10.1016/j.devbrainres.2004.06.012;
RA   Michishita M., Ikeda T., Nakashiba T., Ogawa M., Tashiro K., Honjo T.,
RA   Doi K., Itohara S., Endo S.;
RT   "Expression of Btcl2, a novel member of Btcl gene family, during
RT   development of the central nervous system.";
RL   Brain Res. Dev. Brain Res. 153:135-142(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=19217376; DOI=10.1016/j.neuron.2008.12.014;
RA   Zhang W., St-Gelais F., Grabner C.P., Trinidad J.C., Sumioka A.,
RA   Morimoto-Tomita M., Kim K.S., Straub C., Burlingame A.L., Howe J.R.,
RA   Tomita S.;
RT   "A transmembrane accessory subunit that modulates kainate-type
RT   glutamate receptors.";
RL   Neuron 61:385-396(2009).
CC   -!- FUNCTION: Accessory subunit of neuronal kainate-sensitive
CC       glutamate receptors, GRIK2 and GRIK3. Increases kainate-receptor
CC       channel activity, slowing the decay kinetics of the receptors,
CC       without affecting their expression at the cell surface, and
CC       increasing the open probability of the receptor channels.
CC       Modulates the agonist sensitivity of kainate receptors. Slows the
CC       decay of kainate receptor-mediated excitatory postsynaptic
CC       currents (EPSCs), thus directly influencing synaptic transmission
CC       (By similarity).
CC   -!- SUBUNIT: Interacts with GRIK2 and GRIK3, but neither with AMPA-nor
CC       with NMDA-sensitive glutamate receptors (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
CC       membrane protein (Potential).
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane; Multi-pass
CC       membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BNJ6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BNJ6-2; Sequence=VSP_012858, VSP_012859;
CC   -!- TISSUE SPECIFICITY: Expressed in brain tissues, including
CC       cerebellar granule cells (at protein level).
CC   -!- DEVELOPMENTAL STAGE: Observed restrictively in brain throughout
CC       embryonic (E) and postnatal stages (P). Expression pattern in
CC       brain slightly changes from E13 to P21.
CC   -!- PTM: N-glycosylated (By similarity).
CC   -!- SIMILARITY: Contains 2 CUB domains.
CC   -!- SIMILARITY: Contains 1 LDL-receptor class A domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC38225.1; Type=Erroneous initiation;
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DR   EMBL; AY138991; AAN38319.1; -; mRNA.
DR   EMBL; AK081462; BAC38225.1; ALT_INIT; mRNA.
DR   EMBL; AK083512; BAC38938.1; -; mRNA.
DR   EMBL; BC151050; AAI51051.1; -; mRNA.
DR   IPI; IPI00223269; -.
DR   IPI; IPI00553243; -.
DR   RefSeq; NP_001074793.1; NM_001081324.1.
DR   UniGene; Mm.126079; -.
DR   ProteinModelPortal; Q8BNJ6; -.
DR   SMR; Q8BNJ6; 43-336.
DR   STRING; Q8BNJ6; -.
DR   PhosphoSite; Q8BNJ6; -.
DR   Ensembl; ENSMUST00000047344; ENSMUSP00000047263; ENSMUSG00000036902.
DR   Ensembl; ENSMUST00000109686; ENSMUSP00000105308; ENSMUSG00000036902.
DR   GeneID; 74513; -.
DR   KEGG; mmu:74513; -.
DR   NMPDR; fig|10090.3.peg.18922; -.
DR   UCSC; uc009mqc.1; mouse.
DR   UCSC; uc009mqd.1; mouse.
DR   CTD; 74513; -.
DR   MGI; MGI:1921763; Neto2.
DR   eggNOG; roNOG14256; -.
DR   GeneTree; ENSGT00600000084035; -.
DR   HOVERGEN; HBG052600; -.
DR   OMA; CGVKSPP; -.
DR   OrthoDB; EOG4CJVGW; -.
DR   ArrayExpress; Q8BNJ6; -.
DR   Bgee; Q8BNJ6; -.
DR   CleanEx; MM_NETO2; -.
DR   Genevestigator; Q8BNJ6; -.
DR   GermOnline; ENSMUSG00000036902; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000859; CUB.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   Gene3D; G3DSA:2.60.120.290; CUB; 2.
DR   Gene3D; G3DSA:4.10.400.10; LDL_rcpt_classA_cys-rich; 1.
DR   Pfam; PF00431; CUB; 2.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00192; LDLa; 1.
DR   SUPFAM; SSF49854; CUB; 2.
DR   SUPFAM; SSF57424; LDL_rcpt_classA_cys-rich; 1.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW   Membrane; Receptor; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     22       By similarity.
FT   CHAIN        23    525       Neuropilin and tolloid-like protein 2.
FT                                /FTId=PRO_0000021802.
FT   TOPO_DOM     23    347       Extracellular (Potential).
FT   TRANSMEM    348    368       Helical; (Potential).
FT   TOPO_DOM    369    525       Cytoplasmic (Potential).
FT   DOMAIN       45    159       CUB 1.
FT   DOMAIN      177    292       CUB 2.
FT   DOMAIN      296    332       LDL-receptor class A.
FT   CARBOHYD    311    311       N-linked (GlcNAc...) (Potential).
FT   DISULFID     45     72       By similarity.
FT   DISULFID    100    122       By similarity.
FT   DISULFID    177    207       By similarity.
FT   DISULFID    234    256       By similarity.
FT   DISULFID    297    309       By similarity.
FT   DISULFID    304    322       By similarity.
FT   DISULFID    316    331       By similarity.
FT   VAR_SEQ       1     11       MALEQLCAVLK -> MGTNAVTHSQTLGRAWGILWKNKDGM
FT                                SQNDQGHHKKTYRINLPGPI (in isoform 2).
FT                                /FTId=VSP_012858.
FT   VAR_SEQ     169    175       Missing (in isoform 2).
FT                                /FTId=VSP_012859.
SQ   SEQUENCE   525 AA;  59368 MW;  3E02308F311EC5CE CRC64;
     MALEQLCAVL KVLLITVLVV EGIAVAQKTQ DGQNIGIKHI PATQCGIWVR TSNGGHFASP
     NYPDSYPPNK ECIYILEAAP RQRIELTFDE RYYIEPSFEC RFDHLEIRDG PFGFSPLIDR
     YCGMKSPALI RSTGRFMWIK FSSDEELEGL GFRAKYSFIP DPDFTYLGGI LNPIPDCQFE
     LSGADGIVRS SQVEQEEKTK PGQAVDCIWT IKATPKAKIY LRFLDYQMEH SNECKRNFVA
     VYDGSSAIEN LKAKFCSTVA NDVMLKTGVG VIRMWADEGS RLSRFRMLFT SFVEPPCTSS
     TFFCHSNMCI NNSLVCNGVQ NCAYPWDENH CKEKKKAGLF EQITKTHGTI IGITSGIVLV
     LLIISILVQV KQPRKKVMAC KTAFNKTGFQ EVFDPPHYEL FSLREKEISA DLADLSEELD
     NYQKLRRSST ASRCIHDHHC GSQASSVKQS RTNLSSMELP FRNDFAQPQP MKTFNSTFKK
     SSYTFKQAHE CPEQALEDRV MEEIPCEIYV RGRDDSAQAS ISIDF
//
ID   SPA2L_MOUSE             Reviewed;         426 AA.
AC   Q8BNN1; Q3UTL5; Q5DTL7;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Spermatogenesis-associated protein 2-like protein;
DE            Short=SPATA2-like protein;
GN   Name=Spata2L; Synonyms=Kiaa4138;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Brain cortex, Corpus striatum, and Dendritic cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BNN1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BNN1-2; Sequence=VSP_027334, VSP_027335;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the SPATA2 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90513.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK081234; BAC38172.1; -; mRNA.
DR   EMBL; AK139339; BAE23965.1; -; mRNA.
DR   EMBL; AK170267; BAE41672.1; -; mRNA.
DR   EMBL; AK220503; BAD90513.1; ALT_INIT; mRNA.
DR   IPI; IPI00223290; -.
DR   IPI; IPI00652084; -.
DR   RefSeq; NP_084452.2; NM_030176.2.
DR   UniGene; Mm.41459; -.
DR   ProteinModelPortal; Q8BNN1; -.
DR   PhosphoSite; Q8BNN1; -.
DR   PRIDE; Q8BNN1; -.
DR   Ensembl; ENSMUST00000098327; ENSMUSP00000095932; ENSMUSG00000033594.
DR   Ensembl; ENSMUST00000098328; ENSMUSP00000095933; ENSMUSG00000033594.
DR   GeneID; 78779; -.
DR   KEGG; mmu:78779; -.
DR   UCSC; uc009nup.1; mouse.
DR   CTD; 78779; -.
DR   MGI; MGI:1926029; Spata2L.
DR   eggNOG; roNOG05311; -.
DR   GeneTree; ENSGT00530000063956; -.
DR   HOGENOM; HBG127009; -.
DR   HOVERGEN; HBG102025; -.
DR   InParanoid; Q8BNN1; -.
DR   OMA; ALRLECE; -.
DR   OrthoDB; EOG4PG61B; -.
DR   PhylomeDB; Q8BNN1; -.
DR   NextBio; 349478; -.
DR   ArrayExpress; Q8BNN1; -.
DR   Bgee; Q8BNN1; -.
DR   CleanEx; MM_SPATA2L; -.
DR   Genevestigator; Q8BNN1; -.
PE   2: Evidence at transcript level;
KW   Alternative splicing.
FT   CHAIN         1    426       Spermatogenesis-associated protein 2-like
FT                                protein.
FT                                /FTId=PRO_0000297671.
FT   VAR_SEQ     102    154       TFSGGYVHVLKGVLSEELLTRSFQKMGYVRRDNHRLMVTTP
FT                                PPACQLVQVALG -> LYNQVDLVDLGSAREEGLMGQQLCQ
FT                                DAADSPVEAADLHLATNQHTREEAGKWP (in isoform
FT                                2).
FT                                /FTId=VSP_027334.
FT   VAR_SEQ     155    426       Missing (in isoform 2).
FT                                /FTId=VSP_027335.
FT   CONFLICT    331    331       G -> R (in Ref. 2; BAD90513).
SQ   SEQUENCE   426 AA;  46772 MW;  048152D184FC50CE CRC64;
     MGSSSLSEDY RQCLERELRR GRAGVCGDPS LRAVLWQILV EDFDLHGALQ DDALALFTDG
     LWGRADLAPA LQDLARAFEL LELAAVHLYL LPWRKEFTTI KTFSGGYVHV LKGVLSEELL
     TRSFQKMGYV RRDNHRLMVT TPPPACQLVQ VALGCFALRL ECEILSEVLT QLGTSVLPAE
     ELLRARRASG DVASCVAWLQ QRLAQDEEPP PLPPRGTPAT YGAPVDLYQD LQEDESSEAS
     LYGEPSPGLD SPPVELAYRP PLWEQSAKLW GSGGQPWEPP ADDMHRASSP PYGALEEELE
     PEPSAFSFLS LRRELSRSGD LAPPESPSSP GQASPRHRQA EAAASSAYGP AVEPLSYQAH
     SCLSPGNLPT LCCDTCRQLH ATHCTALSAC RPTHSLRILL GDNQRRLWLQ RAQVDNLLYD
     SPGAHP
//
ID   KBTBB_MOUSE             Reviewed;         633 AA.
AC   Q8BNW9;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Kelch repeat and BTB domain-containing protein 11;
GN   Name=Kbtbd11; Synonyms=Kiaa0711;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC   -!- SIMILARITY: Contains 4 Kelch repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98007.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK129197; BAC98007.1; ALT_INIT; mRNA.
DR   EMBL; AK080001; BAC37803.1; -; mRNA.
DR   IPI; IPI00672611; -.
DR   UniGene; Mm.46675; -.
DR   ProteinModelPortal; Q8BNW9; -.
DR   SMR; Q8BNW9; 124-268, 330-589.
DR   PRIDE; Q8BNW9; -.
DR   Ensembl; ENSMUST00000069399; ENSMUSP00000068321; ENSMUSG00000055675.
DR   UCSC; uc009kzk.1; mouse.
DR   MGI; MGI:1922151; Kbtbd11.
DR   GeneTree; ENSGT00560000077013; -.
DR   HOGENOM; HBG403048; -.
DR   HOVERGEN; HBG081849; -.
DR   InParanoid; Q8BNW9; -.
DR   OrthoDB; EOG4QZ7KT; -.
DR   NextBio; 341767; -.
DR   ArrayExpress; Q8BNW9; -.
DR   Bgee; Q8BNW9; -.
DR   CleanEx; MM_KBTBD11; -.
DR   Genevestigator; Q8BNW9; -.
DR   GermOnline; ENSMUSG00000055675; Mus musculus.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR013069; BTB_POZ.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Gene3D; G3DSA:2.120.10.80; Kelch-typ_b-propeller; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF01344; Kelch_1; 3.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00612; Kelch; 3.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   1: Evidence at protein level;
KW   Kelch repeat; Phosphoprotein; Repeat.
FT   CHAIN         1    633       Kelch repeat and BTB domain-containing
FT                                protein 11.
FT                                /FTId=PRO_0000119091.
FT   DOMAIN      146    206       BTB.
FT   REPEAT      317    365       Kelch 1.
FT   REPEAT      366    418       Kelch 2.
FT   REPEAT      419    463       Kelch 3.
FT   REPEAT      465    506       Kelch 4.
FT   MOD_RES      70     70       Phosphoserine.
FT   MOD_RES     113    113       Phosphoserine (By similarity).
FT   MOD_RES     243    243       Phosphotyrosine (By similarity).
FT   CONFLICT    173    173       A -> S (in Ref. 2; BAC37803).
FT   CONFLICT    369    369       V -> L (in Ref. 2; BAC37803).
SQ   SEQUENCE   633 AA;  67932 MW;  2A6459C680B08C73 CRC64;
     MENSVAPFVL YSGTEPRTPG EDSLPLPAEE EGAASTAQTP CSLSASLCFS SGDDSPPQSR
     ASAAEGSEAS PPSLRSDLRV VETQWDVSSA ASPESPEECA RPEEPASPED PPSRHEHARP
     VELESLDELG EPVPVPPGVG SVHGEPDLVI EVAGRRLRAH KAVLAARSDY FRARASRDVL
     RVQGVSFTAL RLLLADAYSG RMAGVRPDNV AEVVAGARRL QLPGAAQRAT EAMAPQLSLD
     NCYEVLSAGK RQRLTELRDA AYRFMSDHYL EVLREPAVFG RLSGAERDLL LRRRLCTGRA
     CLLAAALGTT GERSGSRPQS PSGDAESRGD AAVYCYQAEA GEWRELTRLP EGAPARGCGL
     CVLFNYLFVA GGVAPAGPDG RARPSDQVYC YNPVTDSWST VRPLRQARSQ VQLLALDGHL
     YAVGGECLLS VERYDPRADR WTAVAPLPRG AFAVAHEAAT CNGEIYVSGG SLFYRLLKYD
     PRRDEWQECP CSSSRERSAD MVALDGFLYR FDLCGSRGEA QAAVGSGGGV SVFRYHCLAK
     QWSQCAVHLR PPGAPAGLQP FRCVALDGTI YCVSRAGTWR FVPSQDTEAG SDMGPGGSFE
     PEPLGSPLDV RGVLFPFVLN LPEKPDRGEQ GAV
//
ID   CJ078_MOUSE             Reviewed;         319 AA.
AC   Q8BP27; Q3UIQ6; Q8R3W0; Q9CRT7; Q9D0D7; Q9D116; Q9D4W4;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   08-FEB-2011, entry version 63.
DE   RecName: Full=Uncharacterized protein C10orf78 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Amnion, Forelimb, Head, Medulla oblongata, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-103, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-103, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-103, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99 AND SER-103, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB23154.1; Type=Frameshift; Positions=290;
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DR   EMBL; AK004073; BAB23154.1; ALT_FRAME; mRNA.
DR   EMBL; AK011531; BAB27680.1; -; mRNA.
DR   EMBL; AK014266; BAB29232.1; -; mRNA.
DR   EMBL; AK016079; BAB30105.1; -; mRNA.
DR   EMBL; AK077875; BAC37045.1; -; mRNA.
DR   EMBL; AK078147; BAC37148.1; -; mRNA.
DR   EMBL; AK146810; BAE27450.1; -; mRNA.
DR   EMBL; BC024403; AAH24403.1; -; mRNA.
DR   IPI; IPI00458153; -.
DR   RefSeq; NP_080653.2; NM_026377.2.
DR   UniGene; Mm.181610; -.
DR   ProteinModelPortal; Q8BP27; -.
DR   PhosphoSite; Q8BP27; -.
DR   PRIDE; Q8BP27; -.
DR   Ensembl; ENSMUST00000099353; ENSMUSP00000096954; ENSMUSG00000025066.
DR   GeneID; 67788; -.
DR   KEGG; mmu:67788; -.
DR   UCSC; uc008hvk.1; mouse.
DR   MGI; MGI:1915038; 6330577E15Rik.
DR   GeneTree; ENSGT00390000018550; -.
DR   HOVERGEN; HBG056268; -.
DR   InParanoid; Q8BP27; -.
DR   OMA; IKKWRSC; -.
DR   PhylomeDB; Q8BP27; -.
DR   NextBio; 325563; -.
DR   ArrayExpress; Q8BP27; -.
DR   Bgee; Q8BP27; -.
DR   CleanEx; MM_6330577E15RIK; -.
DR   Genevestigator; Q8BP27; -.
DR   GermOnline; ENSMUSG00000025066; Mus musculus.
DR   InterPro; IPR018468; Ds-recomb_repair_prot_Mei5.
DR   Pfam; PF10376; Mei5; 2.
PE   1: Evidence at protein level;
KW   Coiled coil; Phosphoprotein.
FT   CHAIN         1    319       Uncharacterized protein C10orf78 homolog.
FT                                /FTId=PRO_0000089806.
FT   COILED      220    270       Potential.
FT   COMPBIAS     24    116       Pro-rich.
FT   MOD_RES      99     99       Phosphoserine.
FT   MOD_RES     103    103       Phosphoserine.
FT   MOD_RES     115    115       Phosphoserine.
FT   MOD_RES     140    140       Phosphoserine (By similarity).
FT   MOD_RES     163    163       Phosphoserine.
FT   CONFLICT     47     62       Missing (in Ref. 2).
FT   CONFLICT    137    137       A -> S (in Ref. 2; BAC37045).
FT   CONFLICT    290    290       K -> R (in Ref. 1; BAB27680).
SQ   SEQUENCE   319 AA;  35183 MW;  14F1B9FCF269455B CRC64;
     MAEEGNQEFT SKMENSSDSA STSPDAPQPS ENPPSPPTSP AAPQTSENPP SPPTSPAVPQ
     TRENPPSPPT SPAAPQPREN PPSPPTSPAA PQPRENPPSP PTSPAAPQPR ENPPSPHSNS
     SGKQPLSGTP KERLKKARSS SHSFCSVVKR MKVENDENNE TLSEPGESSK EENCSKAQES
     LKNKDSEPGE KSSEEKNTCE SKSSDTGSSN ALPKESENAI IREKLKQEKI RLIRQVEEKE
     DLLRRLKLVK MYRIKNDVTE LENLIKKWRK CGQRLLCELQ SIMSEDEDEK LTLTELIDFY
     GIDDNLLHYN RSEEEFTGV
//
ID   CA216_MOUSE             Reviewed;         230 AA.
AC   Q8BP99; A2A7K4;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=UPF0500 protein C1orf216 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SIMILARITY: Belongs to the UPF0500 family.
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DR   EMBL; AK077438; BAC36801.1; -; mRNA.
DR   EMBL; AL606935; CAM17434.1; -; Genomic_DNA.
DR   IPI; IPI00223440; -.
DR   RefSeq; NP_001013777.2; NM_001013755.3.
DR   RefSeq; NP_001139422.1; NM_001145950.1.
DR   UniGene; Mm.296838; -.
DR   ProteinModelPortal; Q8BP99; -.
DR   PRIDE; Q8BP99; -.
DR   Ensembl; ENSMUST00000097886; ENSMUSP00000095496; ENSMUSG00000073755.
DR   GeneID; 230757; -.
DR   KEGG; mmu:230757; -.
DR   NMPDR; fig|10090.3.peg.10377; -.
DR   UCSC; uc008utp.1; mouse.
DR   MGI; MGI:3609248; 5730409E04Rik.
DR   eggNOG; roNOG08395; -.
DR   GeneTree; ENSGT00390000001867; -.
DR   HOGENOM; HBG279034; -.
DR   HOVERGEN; HBG107568; -.
DR   InParanoid; Q8BP99; -.
DR   OMA; AKDANEN; -.
DR   OrthoDB; EOG418BPD; -.
DR   NextBio; 380115; -.
DR   ArrayExpress; Q8BP99; -.
DR   Bgee; Q8BP99; -.
DR   CleanEx; MM_5730409E04RIK; -.
DR   Genevestigator; Q8BP99; -.
PE   2: Evidence at transcript level;
FT   CHAIN         1    230       UPF0500 protein C1orf216 homolog.
FT                                /FTId=PRO_0000309179.
FT   CONFLICT    215    215       R -> H (in Ref. 1; BAC36801).
SQ   SEQUENCE   230 AA;  25232 MW;  0E3E5F46FE7BE904 CRC64;
     MFAAIQPGLA EGAQYPGSLP PGVCQPDLQP DNNSNFVESA KDANKNWHGV PGKVDPILIR
     SSSESPSDNQ VFQATRLPEA GVRSPPEGAE IPGAEPEKLS GASSVCSPLE DIGYASSSLS
     IDSFSSSPEP VCDTPRGPSP LDPLLPSVAQ AVQQLQAQER YKEQEKEKHH AHLVMYRRLA
     LLQWIRALQH QLVDQQARLQ ESFDTILDNR KELIRCLQQR EAPCRHQDQG
//
ID   MOL1A_MOUSE             Reviewed;         216 AA.
AC   Q8BPB0;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-FEB-2011, entry version 59.
DE   RecName: Full=Mps one binder kinase activator-like 1A;
DE   AltName: Full=Mob1 homolog 1A;
GN   Name=Mobkl1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pituitary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-35, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Activator of LATS1/2 in the Hippo signaling pathway
CC       which plays a pivotal role in organ size control and tumor
CC       suppression by restricting proliferation and promoting apoptosis.
CC       The core of this pathway is composed of a kinase cascade wherein
CC       MST1/MST2, in complex with its regulatory protein SAV1,
CC       phosphorylates and activates LATS1/2 in complex with its
CC       regulatory protein MOB1, which in turn phosphorylates and
CC       inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of
CC       YAP1 by LATS1/2 inhibits its translocation into the nucleus to
CC       regulate cellular genes important for cell proliferation, cell
CC       death, and cell migration. Stimulates the kinase activity of
CC       STK38L (By similarity).
CC   -!- SUBUNIT: Binds STK38L. Interacts with LATS1 and LATS2 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the MOB1/phocein family.
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DR   EMBL; AK077320; BAC36748.1; -; mRNA.
DR   IPI; IPI00223454; -.
DR   RefSeq; NP_081011.1; NM_026735.2.
DR   UniGene; Mm.35764; -.
DR   UniGene; Mm.392493; -.
DR   ProteinModelPortal; Q8BPB0; -.
DR   SMR; Q8BPB0; 33-216.
DR   STRING; Q8BPB0; -.
DR   PhosphoSite; Q8BPB0; -.
DR   PRIDE; Q8BPB0; -.
DR   Ensembl; ENSMUST00000006424; ENSMUSP00000006424; ENSMUSG00000006262.
DR   GeneID; 68473; -.
DR   KEGG; mmu:68473; -.
DR   UCSC; uc008yaf.1; mouse.
DR   CTD; 68473; -.
DR   MGI; MGI:1915723; Mobkl1a.
DR   GeneTree; ENSGT00550000074456; -.
DR   HOVERGEN; HBG052489; -.
DR   PhylomeDB; Q8BPB0; -.
DR   NextBio; 327240; -.
DR   ArrayExpress; Q8BPB0; -.
DR   Bgee; Q8BPB0; -.
DR   Genevestigator; Q8BPB0; -.
DR   GermOnline; ENSMUSG00000006262; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0019209; F:kinase activator activity; ISS:UniProtKB.
DR   GO; GO:0019900; F:kinase binding; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR   InterPro; IPR005301; Mob1_phocein.
DR   Gene3D; G3DSA:1.20.140.30; Mob1_phocein; 1.
DR   PANTHER; PTHR22599; Mob1_phocein; 1.
DR   Pfam; PF03637; Mob1_phocein; 1.
DR   SUPFAM; SSF101152; Mob1_phocein; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein; Zinc.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    216       Mps one binder kinase activator-like 1A.
FT                                /FTId=PRO_0000193565.
FT   METAL        79     79       Zinc (By similarity).
FT   METAL        84     84       Zinc (By similarity).
FT   METAL       161    161       Zinc (By similarity).
FT   METAL       166    166       Zinc (By similarity).
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES      35     35       Phosphothreonine.
SQ   SEQUENCE   216 AA;  25091 MW;  29EBA287B0CDAF90 CRC64;
     MSFLFGSRSS KTFKPKKNIP EGSHQYELLK HAEATLGSGN LRMAVMLPEG EDLNEWVAVN
     TVDFFNQINM LYGTITDFCT EESCPVMSAG PKYEYHWADG TNIKKPIKCS APKYIDYLMT
     WVQDQLDDET LFPSKIGVPF PKNFMSVAKT ILKRLFRVYA HIYHQHFDPV IQLQEEAHLN
     TSFKHFIFFV QEFNLIDRRE LAPLQELIEK LTSKDR
//
ID   DAAM1_MOUSE             Reviewed;        1077 AA.
AC   Q8BPM0; Q3UHB4; Q6TAB8; Q80Y68; Q9CQQ2;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 3.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Disheveled-associated activator of morphogenesis 1;
GN   Name=Daam1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   PubMed=15533824; DOI=10.1016/j.modgep.2004.06.001;
RA   Nakaya M.-A., Habas R., Biris K., Dunty W.C. Jr., Kato Y., He X.,
RA   Yamaguchi T.P.;
RT   "Identification and comparative expression analyses of Daam genes in
RT   mouse and Xenopus.";
RL   Gene Expr. Patterns 5:97-105(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Eye, Placenta, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 592-1077 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=15464228; DOI=10.1016/j.devbrainres.2004.07.014;
RA   Kida Y., Shiraishi T., Ogura T.;
RT   "Identification of chick and mouse Daam1 and Daam2 genes and their
RT   expression patterns in the central nervous system.";
RL   Brain Res. Dev. Brain Res. 153:143-150(2004).
CC   -!- FUNCTION: Binds to disheveled (Dvl) and Rho, and mediates Wnt-
CC       induced Dvl-Rho complex formation. May play a role as a
CC       scaffolding protein to recruit Rho-GDP and Rho-GEF, thereby
CC       enhancing Rho-GTP formation. Can direct nucleation and elongation
CC       of new actin filaments (By similarity).
CC   -!- SUBUNIT: Interacts with CIP4, FNBP1 and FNBP1L. Interacts with the
CC       SH3 domains of Abl, BTK, endophilin, spectrin and SRC. Binds
CC       specifically to GTP-bound CDC42 and RHOA (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=Perinuclear
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BPM0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BPM0-2; Sequence=VSP_027771;
CC       Name=3;
CC         IsoId=Q8BPM0-3; Sequence=VSP_027772, VSP_027773;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: In early embryogenesis, expressed in embryonic
CC       and extraembryonic ectoderm. In later stages of gastrulation,
CC       expressed also in somites and ribs and posterior vertebrae of
CC       developing skeletal system. During organogenesis, expressed in
CC       CNS, PNS, stomach, liver and limb bud.
CC   -!- DOMAIN: The C-terminal DAD domain may participate in
CC       intramolecular interactions with the N-terminus.
CC   -!- SIMILARITY: Belongs to the formin homology family.
CC   -!- SIMILARITY: Contains 1 DAD (diaphanous autoregulatory) domain.
CC   -!- SIMILARITY: Contains 1 FH1 (formin homology 1) domain.
CC   -!- SIMILARITY: Contains 1 FH2 (formin homology 2) domain.
CC   -!- SIMILARITY: Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology
CC       3) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH48856.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY426535; AAR05118.1; -; mRNA.
DR   EMBL; AK006902; BAB24785.1; -; mRNA.
DR   EMBL; AK018919; BAB31482.1; -; mRNA.
DR   EMBL; AK018950; BAB31491.1; -; mRNA.
DR   EMBL; AK053785; BAC35522.1; -; mRNA.
DR   EMBL; AK147480; BAE27943.1; -; mRNA.
DR   EMBL; BC032287; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC048856; AAH48856.1; ALT_INIT; mRNA.
DR   IPI; IPI00223511; -.
DR   IPI; IPI00621301; -.
DR   IPI; IPI00857742; -.
DR   RefSeq; NP_080378.2; NM_026102.2.
DR   UniGene; Mm.474935; -.
DR   UniGene; Mm.87417; -.
DR   ProteinModelPortal; Q8BPM0; -.
DR   SMR; Q8BPM0; 53-424, 595-1047.
DR   STRING; Q8BPM0; -.
DR   PhosphoSite; Q8BPM0; -.
DR   PRIDE; Q8BPM0; -.
DR   Ensembl; ENSMUST00000045448; ENSMUSP00000036187; ENSMUSG00000034574.
DR   Ensembl; ENSMUST00000085299; ENSMUSP00000082406; ENSMUSG00000034574.
DR   Ensembl; ENSMUST00000095639; ENSMUSP00000093299; ENSMUSG00000034574.
DR   GeneID; 208846; -.
DR   KEGG; mmu:208846; -.
DR   CTD; 208846; -.
DR   MGI; MGI:1914596; Daam1.
DR   eggNOG; roNOG12638; -.
DR   HOVERGEN; HBG101333; -.
DR   InParanoid; Q8BPM0; -.
DR   OrthoDB; EOG4RBQHV; -.
DR   ArrayExpress; Q8BPM0; -.
DR   Bgee; Q8BPM0; -.
DR   Genevestigator; Q8BPM0; -.
DR   GermOnline; ENSMUSG00000034574; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   InterPro; IPR003104; Actin-bd_FH2/DRF_autoreg.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR014767; Diaphanous_autoregulatory.
DR   InterPro; IPR010472; Drf_FH3.
DR   InterPro; IPR010473; Drf_GTPase-bd.
DR   InterPro; IPR015425; FH2_actin-bd.
DR   InterPro; IPR014768; GTPase-bd/formin_homology_3.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF06367; Drf_FH3; 1.
DR   Pfam; PF06371; Drf_GBD; 1.
DR   Pfam; PF02181; FH2; 1.
DR   SMART; SM00498; FH2; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF101447; FH2_actin_bd; 1.
DR   PROSITE; PS51231; DAD; 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Alternative splicing; Coiled coil; Cytoplasm.
FT   CHAIN         1   1077       Disheveled-associated activator of
FT                                morphogenesis 1.
FT                                /FTId=PRO_0000194908.
FT   DOMAIN       45    420       GBD/FH3.
FT   DOMAIN      528    599       FH1.
FT   DOMAIN      600   1008       FH2.
FT   DOMAIN     1026   1057       DAD.
FT   REGION      693    702       Actin-binding (By similarity).
FT   COILED      437    526       Potential.
FT   COMPBIAS    528    593       Pro-rich.
FT   VAR_SEQ     657    665       Missing (in isoform 2).
FT                                /FTId=VSP_027771.
FT   VAR_SEQ     657    659       EFF -> VTT (in isoform 3).
FT                                /FTId=VSP_027772.
FT   VAR_SEQ     660   1077       Missing (in isoform 3).
FT                                /FTId=VSP_027773.
FT   CONFLICT     36     36       L -> F (in Ref. 2; BAC35522/BAE27943).
FT   CONFLICT    571    571       P -> A (in Ref. 2; BAC35522).
FT   CONFLICT    894    894       E -> G (in Ref. 2; BAE27943).
SQ   SEQUENCE   1077 AA;  123336 MW;  E16A24B3756EB675 CRC64;
     MAPRKRGGRG ISFIFCCFRN NDHPEITYRL RNDSNLALQT MEPALPMPPV EELDVMFSEL
     VDELDLTDKH REAMFALPAE KKWQIYCSKK KDQEENKGAT SWPEFYIDQL NSMAARKSLL
     ALEKEEEEER SKTIESLKTA LRTKPMRFVT RFIDLDGLSC ILNFLKTMDY ETSESRIHTS
     LIGCIKALMN NSQGRAHVLA HSESINVIAQ SLSTENIKTK VAVLEILGAV CLVPGGHKKV
     LQAMLHYQKY ASERTRFQTL INDLDKSTGR YRDEVSLKTA IMSFINAVLS QGAGVESLDF
     RLHLRYEFLM LGIQPVIDKL REHENSTLDR HLDFFEMLRN EDELEFAKRF ELVHIDTKSA
     TQMFELTRRR LTHSEAYPHF MSILHHCLQM PYKRSGNTVQ YWLLLDRIIQ QIVIQNDKGQ
     DPDSTPLENF NIKNVVRMLV NENEVKQWKE QAEKMRKEHN ELQQKLEKKE RECDAKTQEK
     EEMMQTLNKM KEKLEKETTE HKQVKQQVAD LTAQLHELNR RAVCAAVPGG PSPGAPGGPF
     PSSGLGSLLP PPPPPLLSGG ALPPPPPPLP PGGPPPPPGP PPLGGVLPPP GAPVSLTLKK
     KNIPQPTNAL KSFNWSKLPE NKLDGTVWTE IDDTKVFKIL DLEDLERTFS AYQRQQEFFV
     NNSKQKEADA IDDTLSSKLK VKELSVIDGR RAQNCNILLS RLKLSNDEIK RAILTMDEQE
     DLPKDMLEQL LKFVPEKSDI DLLEEHKHEL DRMAKADRFL FEMSRINHYQ QRLQSLYFKK
     KFAERVAEVK PKVEAIRSGS EEVFRSRALK QLLEVVLAFG NYMNKGQRGN AYGFKISSLN
     KIADTKSSID KNITLLHYLI TIVENKYPKV LNLSEELRDI PQAAKVNMTE LDKEISTLRS
     GLKAVETELE YQKSQPPQPG DKFVSVVSQF ITLASFSFSD VEDLLAEAKE LFTKAVKHFG
     EEAGKIQPDE FFGIFDQFLQ AVAEAKQENE NMRKRKEEEE RRARLEAQLK EQRERERKVR
     KAKESSEESG EFDDLVSALR SGEVFDKDLS KLKRNRKRIS NQVTDSSRER PITKLNF
//
ID   M4K5_MOUSE              Reviewed;         847 AA.
AC   Q8BPM2; Q6PEQ2; Q8C3U5; Q8CGF3; Q99LM7; Q9CX73;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-APR-2003, sequence version 2.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Mitogen-activated protein kinase kinase kinase kinase 5;
DE            EC=2.7.11.1;
DE   AltName: Full=MAPK/ERK kinase kinase kinase 5;
DE            Short=MEK kinase kinase 5;
DE            Short=MEKKK 5;
GN   Name=Map4k5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Fetal eye, Fetal liver, and Fetal lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in the response to environmental stress.
CC       Appears to act upstream of the JUN N-terminal pathway (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SUBUNIT: Interacts with both SH3 domains of the adapter proteins
CC       CRK and CRKL (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BPM2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BPM2-2; Sequence=VSP_050478;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC   -!- SIMILARITY: Contains 1 CNH domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK019468; BAB31739.1; -; mRNA.
DR   EMBL; AK053775; BAC35517.1; -; mRNA.
DR   EMBL; AK084891; BAC39305.1; -; mRNA.
DR   EMBL; BC002309; AAH02309.1; -; mRNA.
DR   EMBL; BC040381; AAH40381.2; -; mRNA.
DR   EMBL; BC057930; AAH57930.1; -; mRNA.
DR   IPI; IPI00225230; -.
DR   IPI; IPI00276646; -.
DR   RefSeq; NP_958927.2; NM_201519.2.
DR   UniGene; Mm.291936; -.
DR   ProteinModelPortal; Q8BPM2; -.
DR   SMR; Q8BPM2; 7-292.
DR   PhosphoSite; Q8BPM2; -.
DR   PRIDE; Q8BPM2; -.
DR   Ensembl; ENSMUST00000110570; ENSMUSP00000106199; ENSMUSG00000034761.
DR   GeneID; 399510; -.
DR   KEGG; mmu:399510; -.
DR   UCSC; uc007nsu.1; mouse.
DR   CTD; 399510; -.
DR   MGI; MGI:1925503; Map4k5.
DR   HOGENOM; HBG315791; -.
DR   HOVERGEN; HBG036702; -.
DR   InParanoid; Q8BPM2; -.
DR   OMA; THTFVAQ; -.
DR   OrthoDB; EOG483D3W; -.
DR   PhylomeDB; Q8BPM2; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 406008; -.
DR   ArrayExpress; Q8BPM2; -.
DR   Bgee; Q8BPM2; -.
DR   Genevestigator; Q8BPM2; -.
DR   GermOnline; ENSMUSG00000034761; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0005083; F:small GTPase regulator activity; IEA:InterPro.
DR   GO; GO:0007243; P:intracellular protein kinase cascade; ISS:UniProtKB.
DR   GO; GO:0006950; P:response to stress; ISS:UniProtKB.
DR   InterPro; IPR001180; Citron.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR021160; MAPKKKK.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF038172; MAPKKKK; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN         1    847       Mitogen-activated protein kinase kinase
FT                                kinase kinase 5.
FT                                /FTId=PRO_0000086283.
FT   DOMAIN       20    277       Protein kinase.
FT   DOMAIN      507    820       CNH.
FT   NP_BIND      26     34       ATP (By similarity).
FT   ACT_SITE    140    140       Proton acceptor (By similarity).
FT   BINDING      49     49       ATP (By similarity).
FT   MOD_RES      31     31       Phosphotyrosine (By similarity).
FT   MOD_RES     335    335       Phosphoserine (By similarity).
FT   MOD_RES     401    401       Phosphotyrosine (By similarity).
FT   VAR_SEQ     294    312       Missing (in isoform 2).
FT                                /FTId=VSP_050478.
FT   CONFLICT     79     79       A -> P (in Ref. 1; BAC35517).
FT   CONFLICT    103    103       Q -> H (in Ref. 1; BAC35517).
FT   CONFLICT    118    118       A -> P (in Ref. 1; BAC35517).
FT   CONFLICT    441    441       A -> V (in Ref. 2; AAH40381).
FT   CONFLICT    727    727       L -> Q (in Ref. 1; BAB31739).
SQ   SEQUENCE   847 AA;  95045 MW;  377F0EFFC6EECFA3 CRC64;
     MEAPLRPAAD ILRRNPQHDY ELVQRVGSGT YGDVYKARNV HTGELAAVKI IKLEPGDDFS
     LIQQEIFMVK ECKHCNIVAY FGSYLSREKL WICMEYCGGG SLQDIYHVTG PLSEMQIAYV
     CRETLQGLAY LHTKGKMHRD IKGANILLTD HGDVKLADFG VAAKITATIA KRKSFIGTPY
     WMAPEVAAVE KNGGYNQLCD IWAVGITAIE LGELQPPMFD LHPMRALFLM SKSNFQPPKL
     KDKTKWSSTF HNFVKIALTK NPKKRPTAER LLTHTFVGQP GLSRALAVEL LDKVSNPDNH
     APYSEGDEDD LEPHAIIRHT IRSTNRNSRA ERTASEINFD KLQFEPPLRK ETEARDEMGL
     SSEPNFILHW NPFVDGANTG RSTSKRAIPP PLPPKPRVNT YPEDSLPDEE KSSTIKRCPD
     LEARAPQVLR RQSSPSCVPV AETSSSIGNG DGISKLISEN TEGSAQAPQL PRKKDKRDFP
     KPTINGLPPT PKVLMGACFS KVFDGCPLKI NCATSWIHPD TKDQYIIFGT EDGIYTLNLN
     ELHEATMEQL FPRKCTWLYV INNTLMSLSE GKTFQLYSHN LIALFEQAKK PGLAAHIQTH
     RFPDRILPRK FALTTKIPDT KGCHKCCIVR NPYTGHKYLC GALQSGIVLL QWYEPMQKFM
     LIKHFDFPLP SPLNVFEMLV IPEQEYPMVC VAISKGSDSS QVVQFETINL NSASSWFTEI
     GAGSQQLDSI HVTQLERDTV LVCLDKFVKI VNLQGKLKSS KKLASELSFD FRIESVVCLQ
     DSVLAFWKHG MQGKSFKSDE VTQEISDETR VFRLLGSDRV VVLESRPTEN PAAHSNLYIL
     AGHENSY
//
ID   DMXL2_MOUSE             Reviewed;        3032 AA.
AC   Q8BPN8; B0V2P4; Q3TNY5; Q69ZX5; Q8CCU3;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 3.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=DmX-like protein 2;
DE   AltName: Full=Rabconnectin-3;
GN   Name=Dmxl2; Synonyms=Kiaa0856;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-1485 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Eye, Head, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1224-2891 (ISOFORM 2).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-721, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1288; SER-1399 AND
RP   SER-1856, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423; SER-451; SER-1141;
RP   SER-1144 AND SER-2394, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May serve as a scaffold protein for MADD and RAB3GA on
CC       synaptic vesicles (By similarity).
CC   -!- SUBUNIT: Interacts with MADD and RAB3GAP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane; Peripheral membrane protein (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BPN8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BPN8-2; Sequence=VSP_026596, VSP_026597;
CC       Name=3;
CC         IsoId=Q8BPN8-3; Sequence=VSP_026594, VSP_026595;
CC   -!- SIMILARITY: Contains 16 WD repeats.
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DR   EMBL; AK032099; BAC27698.1; -; mRNA.
DR   EMBL; AK053672; BAC35468.2; -; mRNA.
DR   EMBL; AK164884; BAE37952.1; -; mRNA.
DR   EMBL; CT010507; CAQ12128.1; -; Genomic_DNA.
DR   EMBL; AC161589; CAQ12128.1; JOINED; Genomic_DNA.
DR   EMBL; AK173043; BAD32321.1; -; Transcribed_RNA.
DR   IPI; IPI00853917; -.
DR   IPI; IPI00853932; -.
DR   IPI; IPI00896744; -.
DR   UniGene; Mm.477414; -.
DR   UniGene; Mm.93636; -.
DR   ProteinModelPortal; Q8BPN8; -.
DR   SMR; Q8BPN8; 111-197, 610-668, 1170-1195, 1249-1274, 2764-2831, 2896-3015.
DR   STRING; Q8BPN8; -.
DR   PhosphoSite; Q8BPN8; -.
DR   PRIDE; Q8BPN8; -.
DR   Ensembl; ENSMUST00000047765; ENSMUSP00000041830; ENSMUSG00000041268.
DR   Ensembl; ENSMUST00000118600; ENSMUSP00000113693; ENSMUSG00000041268.
DR   UCSC; uc009pra.1; mouse.
DR   MGI; MGI:2444630; Dmxl2.
DR   eggNOG; roNOG04652; -.
DR   GeneTree; ENSGT00390000000096; -.
DR   HOVERGEN; HBG079593; -.
DR   OrthoDB; EOG4KWJRW; -.
DR   ArrayExpress; Q8BPN8; -.
DR   Bgee; Q8BPN8; -.
DR   CleanEx; MM_DMXL2; -.
DR   Genevestigator; Q8BPN8; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR022033; Rav1p_C.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
DR   Pfam; PF12234; Rav1p_C; 1.
DR   Pfam; PF00400; WD40; 6.
DR   SMART; SM00320; WD40; 13.
DR   SUPFAM; SSF50978; WD40_like; 2.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Coiled coil; Cytoplasmic vesicle;
KW   Membrane; Phosphoprotein; Repeat; Synapse; WD repeat.
FT   CHAIN         1   3032       DmX-like protein 2.
FT                                /FTId=PRO_0000223325.
FT   REPEAT      108    145       WD 1.
FT   REPEAT      167    207       WD 2.
FT   REPEAT      230    278       WD 3.
FT   REPEAT      492    532       WD 4.
FT   REPEAT      594    633       WD 5.
FT   REPEAT      750    802       WD 6.
FT   REPEAT      879    921       WD 7.
FT   REPEAT     1001   1038       WD 8.
FT   REPEAT     1164   1205       WD 9.
FT   REPEAT     1245   1285       WD 10.
FT   REPEAT     2757   2796       WD 11.
FT   REPEAT     2800   2839       WD 12.
FT   REPEAT     2846   2888       WD 13.
FT   REPEAT     2894   2933       WD 14.
FT   REPEAT     2936   2975       WD 15.
FT   REPEAT     2988   3026       WD 16.
FT   COILED     2117   2146       Potential.
FT   MOD_RES     423    423       Phosphoserine.
FT   MOD_RES     451    451       Phosphoserine.
FT   MOD_RES     721    721       Phosphotyrosine.
FT   MOD_RES    1141   1141       Phosphoserine.
FT   MOD_RES    1144   1144       Phosphoserine.
FT   MOD_RES    1288   1288       Phosphoserine.
FT   MOD_RES    1399   1399       Phosphoserine.
FT   MOD_RES    1403   1403       Phosphoserine (By similarity).
FT   MOD_RES    1856   1856       Phosphoserine.
FT   MOD_RES    2394   2394       Phosphoserine.
FT   VAR_SEQ     923    933       AKAAEGISSDS -> GKKLYCYFIQR (in isoform
FT                                3).
FT                                /FTId=VSP_026594.
FT   VAR_SEQ     934   3032       Missing (in isoform 3).
FT                                /FTId=VSP_026595.
FT   VAR_SEQ    2272   2272       Y -> YS (in isoform 2).
FT                                /FTId=VSP_026596.
FT   VAR_SEQ    2488   2498       Missing (in isoform 2).
FT                                /FTId=VSP_026597.
FT   CONFLICT    655    655       L -> P (in Ref. 1; BAC35468).
SQ   SEQUENCE   3032 AA;  338209 MW;  2FB99AE184E56207 CRC64;
     MHLHQVLTGA VNPGDNCYSV GSVGDVPFTA YGSGCDIVIL ASDFECVQII PGAKHGNIQV
     SCVECSNQHG RVAASYGNAV CIFEPLGVNS HKRNSQLKCQ WLKTGQFFLS SVTYNLAWDP
     QDNRLLTATD SIQLWAPPGG DILEEEEDVD NRAPPVLNDW KCIWQCKTSV SVHLMEWSPD
     GEYFATAGKD DCLLKVWYPM TGWKSSIIPQ DPHEVKRRRA STQFSFVYLA HPRAVTGFSW
     RKTSKYMPRG SVCNVLLTSC HDGVCRLWAE TLLPEDCLLG EQICETTTSS VASNLSSAGK
     HKDRIQHALE TIHHLKNLRK GQRRSSVLVT HAELMPDKTA THEVHRHISH HANALCHFHI
     AASINPTTDI PNVLVGTAFN IDDINGGFVV HWLNNKEFHF TSSTEIFMHQ LRKLSEKQLD
     HESDDADRED EERSQDERER GLRMKLDHEL SLDRESEAGT GSSEHEDGER EGSPRTHPRP
     SISMPLPTVL LDRKIETLLT EWNKNPDMLF TIHPVDGTFL VWHVKYLDEY NPGIFRQVQV
     SFSSRIPVAF PSGDANSLSK NIMMYACVNA TKDSYNPSQQ EMMSVDSPHG SQLHSPSHST
     DMNILAPTVM MVSKHIDGSL NQWAVTFADK SAFTTVLTVS HKFRYCGHRF HLNDLACHSV
     LPLLLTSSHH NALLTPESDC QWDSDSKVNR LIDPVKHTKA SSKQPLRNAA TRTFHDPNAI
     YSELILWRVD PIGPLSYTGG VSELARINSL HTSAFSNVAW LPTLIPSYCL GTYCNSASAC
     FVASDGKNLR LYQAVVDARK LLDELSDPEA SKLIGEVFNI VSQQSTARPG CIIELDAITD
     QCGSNTQLLH VFQEDFIIGY KPHKEDMEKK EKESEIFFQP SQGYRPPPFS EKFFLVVIEK
     DGNNNSILHM WHLHLKSVQA CLAKAAEGIS SDSLLSVPGQ KNLDSSPETS SSMSSVPHSS
     SIANLQTASK LILSSRLVYS QPLDLPEAVE VIRATPSAGH LSSSSIYPVC LAPYLVVTTC
     SDNKVRFWKC CMETNSLGNT SDESETYHWR RWPLMNDEGE DNSSTVSIVG RPVAVSCSYT
     GRLAVAYKQP IHHNGFISKE FSMHVCIFEC ESTGGSEWVL EQTIHLDDLV KVGSVLDSRV
     SVDSNLFVYS KSDAFLSKDR YLIPNIKHLV HLDWVSKEDG SHILTVGVGA NIFMYGRLSG
     IVSDQTNSKD GVAVITLPLG GSIKQGVKSR WVLLRSIDLV SSVDGTPSLP VSLSWVRDGI
     LVVGMDCEMH VYAQWKHSVK FGNVDADSPV EETIQDHSAL KSSMLARKSI VEGAAIPDDV
     FCSPTVVQDG GLFEAAHALS PTLPQYHPTQ LLELMDLGKV RRAKAILSHL VKCIAGEVAI
     VRDPDAGEGT KRHLSRTISV SGSTAKDTVT IGKDGTRDYT EIDSIPPLPL HALLAADQDT
     SYRISEDSTK KPQSYEDHIE SQSEDQYSEL FQVQEITTDD IDLEPEKREN KSKVINLSQY
     GPACFGQEHA RVLSSHLMHS SLPGLTRLEQ MFLVALADTV ATTSTELDEN RDKNYSGRDT
     LDECGLRYLL AMRLHTCLLT SLPPLYRVQL LHQGVSTCHF AWAFHSEAEE ELINMIPAIQ
     RGDPQWSELR AMGIGWWVRN VNTLRRCIEK VAKAAFQRNN EALDAALFYL SMKKKAVVWG
     LFRSQHDEKM TTFFSHNFNE DRWRKAALKN AFSLLGKQRF EQSAAFFLLA GSLKDAIEVC
     LEKMEDIQLA MVIARLFESE FETSSTYISI LNQKILGCQK DGTGFDCKRL HPDPFLRSLA
     YWVVKDYTRA LDTLLEQTPK EDDEQQVIIK SCNPVVFSFY NYLRTHPLLI RRNLASPEGT
     LATLGLKTEK NIADKINLIE RKLFFTTANA HFKVGCPVLA LEVLSKIPKV TKISSLTAKK
     DQLDSVSGRM ENGPSESKPV SRSDGGSGAD WSAVTSSQFD WSQPMVTVDE EPLRLDWGDD
     HDGALEEDDG GGLVMKTTDA KKAGQEQSAS DPRALLTPQD EECADGDTEV DVIAEQLKFR
     ACLKILMTEL RTLATGYEVD GGKLRFQLYN WLEKEIAALH EICNHESVIK EYSSKAHSTV
     ETERLDQEEM VDKPDIGSYE RHQIERRRLQ AKREHAERRK LWLQKNQDLL RVFLSYCSLH
     GAQGGGLASV RMELKFLLQE SQQETTVKQL QSPLPLPTTL PLLSASIAST KTVIANPVLY
     LNNHIHDILY TIVQMKTPPH PSVEDVKVHT LHSLAASLSA SIYQALCDSH SYSQSEGNQF
     TGMAYQGLLL SDRRRLRTES IEEHATPNSA PAQWPGVSSL INLLSSAQDE DQPKLNVLLC
     EAVVAVYLSL LIHALATNSS NELFRLAAHP LNNRMWAAVF GGGVKLVVKP RRQSESIAAP
     PVASEDMDKH RRRFNMRMLV PGRPVKDATP PPVPAERPSY KEKFIPPELS MWDYFVAKPF
     LPLSDSGVIY DSDESVHSDD EEDDAFFSDT QIQEHQDPNS YSWALLHLTM VKLALHNIKN
     FFPIAGLEFS ELPVTSPLGI AVIKNLENWE QILQEKMDHF EGPPPNYVNT YPTDLSVGAG
     PAILRNKAML EPENTPFKSR DSSALPVKRL WHFLVKQEVL QETFIRYIFT KKRKQSEVEA
     DLGYPGGKAK VIHKESDMIM AFSINKANCN EIVLASTHDV QELDVTSLLA CQSYIWIGEE
     YDRESKSSDD IDYRGSTTTL YQPGAASHSS SQPHPPPSLP WLGSGQTSTG ATVLMKRNLH
     NVKRMTSHPV HQYYLTGAQD GSVRMFEWTR PQQLVCFRQA GNARVTRLYF NSQGNKCGVA
     DGEGFLSIWQ VNQTASNPKP YMSWQCHSKA TSDFAFITSS SLVATSGHSN DNRNVCLWDT
     LISPGNSLIH GFTCHDHGAT VLQYAPKQQL LISGGRKGYI CIFDIRQRQL IHTFQAHDSA
     IKALALDSCE EYFTTGSAEG NIKVWRLTGH GLIHSFKSEH AKQSIFRNIG AGVMQIAISQ
     DNRLFSCGAD GTLKTRVLPS AFNIPNRILD IL
//
ID   ELMO1_MOUSE             Reviewed;         727 AA.
AC   Q8BPU7; Q8BSY9; Q8K2C5; Q91ZU3;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2003, sequence version 2.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Engulfment and cell motility protein 1;
DE   AltName: Full=Protein ced-12 homolog;
GN   Name=Elmo1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6;
RX   MEDLINE=21479119; PubMed=11595183; DOI=10.1016/S0092-8674(01)00520-7;
RA   Gumienny T.L., Brugnera E., Tosello-Trampont A.-C., Kinchen J.M.,
RA   Haney L.B., Nishiwaki K., Walk S.F., Nemergut M.E., Macara I.G.,
RA   Francis R., Schedl T., Qin Y., Van Aelst L., Hengartner M.O.,
RA   Ravichandran K.S.;
RT   "CED-12/ELMO, a novel member of the CrkII/Dock180/Rac pathway, is
RT   required for phagocytosis and cell migration.";
RL   Cell 107:27-41(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 309-727 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Eye, Mammary tumor, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH BAI1 AND DOCK1.
RX   PubMed=17960134; DOI=10.1038/nature06329;
RA   Park D., Tosello-Trampont A.-C., Elliott M.R., Lu M., Haney L.B.,
RA   Ma Z., Klibanov A.L., Mandell J.W., Ravichandran K.S.;
RT   "BAI1 is an engulfment receptor for apoptotic cells upstream of the
RT   ELMO/Dock180/Rac module.";
RL   Nature 450:430-434(2007).
CC   -!- FUNCTION: Involved in cytoskeletal rearrangements required for
CC       phagocytosis of apoptotic cells and cell motility. Acts in
CC       assocation with DOCK1 and CRK. Was initially proposed to be
CC       required in complex with DOCK1 to activate Rac Rho small GTPases.
CC       May enhance the guanine nucleotide exchange factor (GEF) activity
CC       of DOCK1 (By similarity).
CC   -!- SUBUNIT: Interacts directly with the SH3-domain of DOCK1 via its
CC       SH3-binding site. Probably forms a heterotrimeric complex with
CC       DOCK1 and RAC1 (By similarity). Interacts with PLEKHG6 (By
CC       similarity). Interacts with BAI1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane (By
CC       similarity). Note=Translocation to plasma membrane seems to be
CC       mediated by DOCK1 and CRK (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8BPU7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BPU7-2; Sequence=VSP_007481;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8BPU7-3; Sequence=VSP_007482, VSP_007483;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q8BPU7-4; Sequence=VSP_007481, VSP_007484, VSP_007485;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated by HCK (By similarity).
CC   -!- SIMILARITY: Contains 1 ELMO domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
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DR   EMBL; AF398883; AAL14464.1; -; mRNA.
DR   EMBL; AK028389; BAC25925.1; -; mRNA.
DR   EMBL; AK053306; BAC35336.1; -; mRNA.
DR   EMBL; BC024727; AAH24727.1; -; mRNA.
DR   EMBL; BC031782; AAH31782.1; -; mRNA.
DR   IPI; IPI00131428; -.
DR   IPI; IPI00310489; -.
DR   IPI; IPI00310490; -.
DR   IPI; IPI00310491; -.
DR   RefSeq; NP_525027.1; NM_080288.1.
DR   RefSeq; NP_932761.1; NM_198093.2.
DR   UniGene; Mm.342392; -.
DR   ProteinModelPortal; Q8BPU7; -.
DR   SMR; Q8BPU7; 530-727.
DR   IntAct; Q8BPU7; 30.
DR   MINT; MINT-219471; -.
DR   STRING; Q8BPU7; -.
DR   PhosphoSite; Q8BPU7; -.
DR   PRIDE; Q8BPU7; -.
DR   Ensembl; ENSMUST00000072519; ENSMUSP00000072334; ENSMUSG00000041112.
DR   Ensembl; ENSMUST00000110493; ENSMUSP00000106119; ENSMUSG00000041112.
DR   GeneID; 140580; -.
DR   KEGG; mmu:140580; -.
DR   UCSC; uc007ppn.1; mouse.
DR   UCSC; uc007ppo.1; mouse.
DR   UCSC; uc007ppq.1; mouse.
DR   UCSC; uc007ppr.1; mouse.
DR   CTD; 140580; -.
DR   MGI; MGI:2153044; Elmo1.
DR   GeneTree; ENSGT00390000014155; -.
DR   HOVERGEN; HBG051463; -.
DR   InParanoid; Q8BPU7; -.
DR   OMA; RDITFAQ; -.
DR   OrthoDB; EOG42RD6S; -.
DR   PhylomeDB; Q8BPU7; -.
DR   NextBio; 369899; -.
DR   ArrayExpress; Q8BPU7; -.
DR   Bgee; Q8BPU7; -.
DR   Genevestigator; Q8BPU7; -.
DR   GermOnline; ENSMUSG00000041112; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0006928; P:cellular component movement; ISS:UniProtKB.
DR   GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
DR   GO; GO:0016601; P:Rac protein signal transduction; ISS:UniProtKB.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR006816; Engulfment_cell_motility_ELMO.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF04727; ELMO_CED12; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS51335; ELMO; 1.
DR   PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Apoptosis; Cell membrane;
KW   Cytoplasm; Membrane; Phagocytosis; Phosphoprotein; SH3-binding.
FT   CHAIN         1    727       Engulfment and cell motility protein 1.
FT                                /FTId=PRO_0000153713.
FT   DOMAIN      319    492       ELMO.
FT   DOMAIN      555    676       PH.
FT   MOTIF       707    714       SH3-binding.
FT   MOD_RES     100    100       N6-acetyllysine (By similarity).
FT   MOD_RES     105    105       N6-acetyllysine (By similarity).
FT   MOD_RES     344    344       Phosphoserine (By similarity).
FT   VAR_SEQ       1    480       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_007481.
FT   VAR_SEQ     398    420       IVLENSSREDKHECPFGRSSIEL -> VSMLASLRYCQCRM
FT                                EFCFPTYAQ (in isoform 3).
FT                                /FTId=VSP_007482.
FT   VAR_SEQ     421    727       Missing (in isoform 3).
FT                                /FTId=VSP_007483.
FT   VAR_SEQ     636    642       EVLELAF -> VWFSKSL (in isoform 4).
FT                                /FTId=VSP_007484.
FT   VAR_SEQ     643    727       Missing (in isoform 4).
FT                                /FTId=VSP_007485.
FT   CONFLICT      9      9       K -> E (in Ref. 2; BAC25925).
FT   CONFLICT    315    315       P -> H (in Ref. 2; BAC25925).
SQ   SEQUENCE   727 AA;  83936 MW;  21B1BB9195504D28 CRC64;
     MPPPSDIVKV AIEWPGAYPK LMEIDQKKPL SAIIKEVCDG WSLANHEYFA LQHADSSNFY
     ITEKNRNEIK NGTILRLTTS PAQNAQQLHE RIQSSSMDAK LEALKDLASL SRDVTFAQEF
     INLDGISLLT QMVESGTERY QKLQKIMKPC FGDMLSFTLT AFVELMDHGI VSWDTFSVAF
     IKKIASFVNK SAIDISILQR SLAILESMVL NSHDLYQKVA QEITIGQLIP HLQGTDQEIQ
     TYTIAVINAL FLKAPDERRQ EMANILAQKQ LRYIILTHVI RAQRAINNEM AHQLYVLQVL
     TFNLLEDRMM TKMDPQDQAQ RDIIFELRRI AFDAESEPNN SSGSMEKRKS MYTRDYKKLG
     FINHVNPAMD FTQTPPGMLA LDNMLYFAKH HQDAYIRIVL ENSSREDKHE CPFGRSSIEL
     TKMLCEILKV GELPSETCND FHPMFFTHDR SFEEFFCICI QLLNKTWKEM RATSEDFNKV
     MQVVKEQVMR ALTTKPSSLD QFKSKLQNLS YTEILKIRQS ERMNQEDFQS RPILELKEKI
     QPEILELIKQ QRLNRLVEGT CFRKLNARRR QDKFWYCRLS PNHKVLHYGD LEESPQGEVP
     HDSLQDKLPV ADIKAVVTGK DCPHMKEKGA LKQNKEVLEL AFSILYDSNC QLNFIAPDKH
     EYCIWTDGLN ALLGKDMMSD LTRNDLDTLL SMEIKLRLLD LENIQIPDAP PPIPKEPSNY
     DFVYDCN
//
ID   PHTNS_MOUSE             Reviewed;         594 AA.
AC   Q8BQ30; B8JJ63; B8JJ64; Q3UDS6; Q8CEY9; Q8R3D8;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 61.
DE   RecName: Full=Phostensin;
DE   AltName: Full=Protein phosphatase 1 F-actin cytoskeleton-targeting subunit;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Spinal ganglion, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134 AND SER-510, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May target protein phosphatase 1 to F-actin cytoskeleton
CC       (By similarity).
CC   -!- SUBUNIT: Interacts with Protein phosphatase 1 (PP1) (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BQ30-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BQ30-2; Sequence=VSP_014260;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH25573.1; Type=Erroneous initiation;
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DR   EMBL; AK009340; BAC25252.1; -; mRNA.
DR   EMBL; AK051656; BAC34706.1; -; mRNA.
DR   EMBL; AK149943; BAE29185.1; -; mRNA.
DR   EMBL; CR974451; CAX15752.1; -; Genomic_DNA.
DR   EMBL; CR974451; CAX15753.1; -; Genomic_DNA.
DR   EMBL; BC025573; AAH25573.1; ALT_INIT; mRNA.
DR   IPI; IPI00336929; -.
DR   IPI; IPI00607928; -.
DR   RefSeq; NP_001140182.1; NM_001146710.1.
DR   RefSeq; NP_001140183.1; NM_001146711.1.
DR   RefSeq; NP_780451.1; NM_175242.1.
DR   UniGene; Mm.359982; -.
DR   UniGene; Mm.421125; -.
DR   ProteinModelPortal; Q8BQ30; -.
DR   IntAct; Q8BQ30; 1.
DR   PhosphoSite; Q8BQ30; -.
DR   PRIDE; Q8BQ30; -.
DR   Ensembl; ENSMUST00000038030; ENSMUSP00000049443; ENSMUSG00000034595.
DR   Ensembl; ENSMUST00000113814; ENSMUSP00000109445; ENSMUSG00000034595.
DR   GeneID; 76448; -.
DR   KEGG; mmu:76448; -.
DR   UCSC; uc008cit.1; mouse.
DR   UCSC; uc008ciu.1; mouse.
DR   MGI; MGI:1923698; 2310014H01Rik.
DR   GeneTree; ENSGT00530000064035; -.
DR   HOVERGEN; HBG080180; -.
DR   OMA; WTPRDTE; -.
DR   NextBio; 345174; -.
DR   ArrayExpress; Q8BQ30; -.
DR   Bgee; Q8BQ30; -.
DR   CleanEx; MM_2310014H01RIK; -.
DR   Genevestigator; Q8BQ30; -.
DR   GermOnline; ENSMUSG00000034595; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW   Phosphoprotein.
FT   CHAIN         1    594       Phostensin.
FT                                /FTId=PRO_0000050809.
FT   COMPBIAS     96    105       Poly-Gln.
FT   MOD_RES     126    126       Phosphoserine (By similarity).
FT   MOD_RES     134    134       Phosphoserine.
FT   MOD_RES     146    146       Phosphoserine (By similarity).
FT   MOD_RES     174    174       Phosphoserine (By similarity).
FT   MOD_RES     194    194       Phosphoserine (By similarity).
FT   MOD_RES     198    198       Phosphothreonine (By similarity).
FT   MOD_RES     224    224       Phosphoserine (By similarity).
FT   MOD_RES     265    265       Phosphoserine (By similarity).
FT   MOD_RES     412    412       Phosphoserine (By similarity).
FT   MOD_RES     510    510       Phosphoserine.
FT   VAR_SEQ     589    594       DESCRR -> GKRLRPGWRRAPPGVCGVVVL (in
FT                                isoform 2).
FT                                /FTId=VSP_014260.
FT   CONFLICT    278    278       R -> I (in Ref. 3; AAH25573).
SQ   SEQUENCE   594 AA;  65630 MW;  6B7B10B39C5B44BA CRC64;
     MTAIPDWKLQ LLARRRQEEA AVRGREKAER DRLSQMPAWK RGILERRRAK LGLPPGEGSP
     VPGNAEAGPP DPDESAVLLE AIGPVHQNRF IQQERQRQQQ QQQQQRNEVL GDRKAGPLEV
     LERRSSPGNL RDQSPKGRES REERLSPRES RDRRLVIGGA QESSSRSLRD WRQSPAEARD
     LSSRPAEAQK WRLSPGETPE ESLRLAGSGD DSPKRKEVLE SILSPGEPGD QKASPTDVHK
     WNLDSREPQK QSLIQLEATE WRLKSGEERK DYLEGCGREE EKLSSGIVPV TKEVQDITSS
     EVETAEQRPT ESWKWTLNSG KARERTTWDI DTQTQKPDPP ASSEKHPGPS GMEAEEEAEK
     EEAEAQSRPL RAQQNLCSGP SPLPPEHSGT EGSRQQEEEA AEPRPPTPAP LSPPPSAPTA
     PQPSGDPLMS RLFYGVKPGP GVGAPRRSGH TFTVNPRRCA PPASPAPPVN PATADAAGSG
     SGKKRYPTAE EILVLGGYLR LSRSCLVKGS PERHHKQLKI SFSETALETT YQYPSESSVL
     EDLGPEPETP IAPLATQPDE EEEEEEEEEE LLLQPGLQGG LRTKALIVDE SCRR
//
ID   Q8BQD7_MOUSE            Unreviewed;       749 AA.
AC   Q8BQD7;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   30-NOV-2010, entry version 51.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Recql5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK050965; BAC34479.1; -; mRNA.
DR   IPI; IPI00129287; -.
DR   UniGene; Mm.379351; -.
DR   HSSP; P15043; 1OYY.
DR   ProteinModelPortal; Q8BQD7; -.
DR   STRING; Q8BQD7; -.
DR   Ensembl; ENSMUST00000021097; ENSMUSP00000021097; ENSMUSG00000020752.
DR   MGI; MGI:2156841; Recql5.
DR   HOVERGEN; HBG057065; -.
DR   InParanoid; Q8BQD7; -.
DR   ArrayExpress; Q8BQD7; -.
DR   Bgee; Q8BQD7; -.
DR   Genevestigator; Q8BQD7; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR010716; RecQ_helicase-like_5.
DR   PANTHER; PTHR13710; RecQ; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF06959; RecQ5; 1.
DR   ProDom; PD120154; RecQ_helicase-like_5; 1.
DR   SMART; SM00490; HELICc; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   749 AA;  82409 MW;  85B797B979536922 CRC64;
     LIPDVYGNLR DFCLKALGQK AENGSSSGCG IVYCRTREAC EQLAIELSSR GVNAKAYHAG
     LKASDRTQVQ NEWMEEKVPV IVATISFGMG VDKANVRFVA HWNIAKSMAG YYQESGRAGR
     DGKPSWCRLY YSRNDRDQVS FLIRKELAKL QEKRGNKPSD KATLLAFDAL VTFCEEVGCR
     HAAIAKYFGD APPACAKGCD YCQNPAAITK KLDALERSSS WSKTCIGPSQ GNGFDPELYE
     GGRRGYGGFS RYDEGSGGSG DEGRDEAHKR EWNLFYQKQM SLRKGKEPKI EEFTPPDEDC
     PLREASSRKI PKLTVKAREH CLRLLEEALI SNHQAAGSTH GADLQAKAVE LEHETFRNAK
     MVNLYKASVL KKVAEIHKAS KDGQLYDMEC GTKSCGAAAE FSEPSDYDIP PTSHVYSLKP
     KRVGAGFSKG PCSFQTATEL LGKSHSQKQA PEAMLEGGQE PPGWVCDLQD EDRSKPHPGY
     QEKALGSSVN CGDPSPEKKT KGSSQGSAKA RASKKQQLLA TAARKDSQNI TRFLCQRTES
     PPLPASVPRS EDASPSCGDV PGKCTQEVGA QGHLVAVFQT EGPRERPSTC SLRDQSFPEG
     QPSPLKETQA EKRPRPQQGN PERRAQKRLR PSTKSSILAE AKDSTLASDR STENKVAQEP
     CQLSASGTSL REAADIVVRH LTPFYKEGRF ISKDLFKGFA RHLSHLLAQQ LSPGRSVKEE
     AQSLIKQFFH NRARCESEAD WHSLRGPQR
//
ID   Q8BQK8_MOUSE            Unreviewed;        99 AA.
AC   Q8BQK8;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 47.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Purb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; AK049443; BAC33753.1; -; mRNA.
DR   IPI; IPI00128867; -.
DR   UniGene; Mm.296150; -.
DR   UniGene; Mm.390332; -.
DR   UniGene; Mm.474493; -.
DR   STRING; Q8BQK8; -.
DR   Ensembl; ENSMUST00000059507; ENSMUSP00000055596; ENSMUSG00000049647.
DR   MGI; MGI:1338779; Purb.
DR   GeneTree; ENSGT00390000015406; -.
DR   InParanoid; Q8BQK8; -.
DR   ArrayExpress; Q8BQK8; -.
DR   Bgee; Q8BQK8; -.
DR   Genevestigator; Q8BQK8; -.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0046332; F:SMAD binding; IDA:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:MGI.
DR   InterPro; IPR006628; PUR_DNA_RNA-bd.
DR   PANTHER; PTHR12611; PUR_DNA_RNA_bd; 1.
DR   Pfam; PF04845; PurA; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   99 AA;  11117 MW;  D50A315C894A719B CRC64;
     GLYGELPEGT SITVDSKRFF FDVGCNKYGV FLRVSEVKPS YRNAITVPFK AWGKFGGAFC
     RYADEMKEIQ ERQRDKLYER RGGGSGGGDE SEGEEVDED
//
ID   R7BP_MOUSE              Reviewed;         257 AA.
AC   Q8BQP9; Q0VF69; Q3UVC4; Q8CBD6; Q9CTP1;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Regulator of G-protein signaling 7-binding protein;
DE   AltName: Full=R7 family-binding protein;
GN   Name=Rgs7bp; Synonyms=D13Bwg1146e, R7bp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, INTERACTION WITH RGS6; RGS7; RGS9 AND RGS11,
RP   PALMITOYLATION AT CYS-252 AND CYS-253, AND MUTAGENESIS OF CYS-252 AND
RP   CYS-253.
RC   STRAIN=C57BL/6J;
RX   PubMed=15897264; DOI=10.1083/jcb.200502007;
RA   Drenan R.M., Doupnik C.A., Boyle M.P., Muglia L.J., Huettner J.E.,
RA   Linder M.E., Blumer K.J.;
RT   "Palmitoylation regulates plasma membrane-nuclear shuttling of R7BP, a
RT   novel membrane anchor for the RGS7 family.";
RL   J. Cell Biol. 169:623-633(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex, Cerebellum, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY, AND INTERACTION WITH RGS6; RGS7; RGS9 AND RGS11.
RX   PubMed=15632198; DOI=10.1074/jbc.C400596200;
RA   Martemyanov K.A., Yoo P.J., Skiba N.P., Arshavsky V.Y.;
RT   "R7BP, a novel neuronal protein interacting with RGS proteins of the
RT   R7 family.";
RL   J. Biol. Chem. 280:5133-5136(2005).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL,
RP   PALMITOYLATION AT CYS-252 AND CYS-253, AND MUTAGENESIS OF ARG-243;
RP   ARG-246 AND 252-CYS-CYS-253.
RX   PubMed=16574655; DOI=10.1074/jbc.M600749200;
RA   Song J.H., Waataja J.J., Martemyanov K.A.;
RT   "Subcellular targeting of RGS9-2 is controlled by multiple molecular
RT   determinants on its membrane anchor, R7BP.";
RL   J. Biol. Chem. 281:15361-15369(2006).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL DOMAIN,
RP   AND MUTAGENESIS OF 242-ARG--ARG-247.
RX   PubMed=16867977; DOI=10.1074/jbc.M604428200;
RA   Drenan R.M., Doupnik C.A., Jayaraman M., Buchwalter A.L.,
RA   Kaltenbronn K.M., Huettner J.E., Linder M.E., Blumer K.J.;
RT   "R7BP augments the function of RGS7*Gbeta5 complexes by a plasma
RT   membrane-targeting mechanism.";
RL   J. Biol. Chem. 281:28222-28231(2006).
RN   [7]
RP   FUNCTION.
RX   PubMed=17158100; DOI=10.1074/jbc.M610518200;
RA   Anderson G.R., Semenov A., Song J.H., Martemyanov K.A.;
RT   "The membrane anchor R7BP controls the proteolytic stability of the
RT   striatal specific RGS protein, RGS9-2.";
RL   J. Biol. Chem. 282:4772-4781(2007).
CC   -!- FUNCTION: Regulator of G protein-coupled receptor (GPCR)
CC       signaling. Regulatory subunit of the R7-Gbeta5 complexes that acts
CC       by controlling the subcellular location of the R7-Gbeta5
CC       complexes. When palmitoylated, it targets the R7-Gbeta5 complexes
CC       to the plasma membrane, leading to inhibit G protein alpha
CC       subunits. When it is unpalmitoylated, the R7-Gbeta5 complexes
CC       undergo a nuclear/cypolasmic shuttling. May also act by
CC       controlling the proteolytic stability of R7 proteins, probably by
CC       protecting them from degradation.
CC   -!- SUBUNIT: Interacts with 'R7' family proteins RGS6, RGS7, RGS9 and
CC       RGS11. Component of some R7-Gbeta5 complex composed of some R7
CC       protein (RGS6, RGS7, RGS9 or RGS11), Gbeta5 (GNB5) and RGS7BP.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cell membrane; Lipid-
CC       anchor. Note=Shuttling between the plasma membrane, the cytoplasm
CC       and the nucleus is regulated by palmitoylation.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in the central nervous
CC       system including the retina but not in other non-neuronal tissues
CC       (at protein level).
CC   -!- DOMAIN: The nuclear localization signal is both required for
CC       nuclear localization and palmitoylation.
CC   -!- PTM: Palmitoylation regulates the cell membrane and nuclear
CC       shuttling and the regulation of GPCR signaling. Upon
CC       depalmitoylation, it is targeted into the nucleus.
CC   -!- SIMILARITY: Belongs to the RGS7BP/RGS9BP family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC29358.1; Type=Frameshift; Positions=36, 217;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; DQ104214; AAZ09201.1; -; mRNA.
DR   EMBL; AK020910; BAB32250.1; -; mRNA.
DR   EMBL; AK036240; BAC29358.1; ALT_FRAME; mRNA.
DR   EMBL; AK046733; BAC32849.1; -; mRNA.
DR   EMBL; AK137417; BAE23346.1; -; mRNA.
DR   EMBL; BC118957; AAI18958.1; -; mRNA.
DR   IPI; IPI00817008; -.
DR   RefSeq; NP_084155.2; NM_029879.2.
DR   UniGene; Mm.100348; -.
DR   ProteinModelPortal; Q8BQP9; -.
DR   STRING; Q8BQP9; -.
DR   PRIDE; Q8BQP9; -.
DR   Ensembl; ENSMUST00000063551; ENSMUSP00000066614; ENSMUSG00000021719.
DR   GeneID; 52882; -.
DR   KEGG; mmu:52882; -.
DR   UCSC; uc007rtp.1; mouse.
DR   CTD; 52882; -.
DR   MGI; MGI:106334; Rgs7bp.
DR   eggNOG; roNOG13712; -.
DR   GeneTree; ENSGT00390000006968; -.
DR   HOGENOM; HBG713507; -.
DR   HOVERGEN; HBG104928; -.
DR   InParanoid; Q8BQP9; -.
DR   OMA; PILEDTS; -.
DR   OrthoDB; EOG4QRH4T; -.
DR   NextBio; 309673; -.
DR   ArrayExpress; Q8BQP9; -.
DR   Bgee; Q8BQP9; -.
DR   Genevestigator; Q8BQP9; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; IDA:MGI.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; Lipoprotein; Membrane; Nucleus; Palmitate;
KW   Signal transduction inhibitor.
FT   CHAIN         1    257       Regulator of G-protein signaling 7-
FT                                binding protein.
FT                                /FTId=PRO_0000287596.
FT   MOTIF       242    247       Nuclear localization signal.
FT   LIPID       252    252       S-palmitoyl cysteine (Probable).
FT   LIPID       253    253       S-palmitoyl cysteine (Probable).
FT   MUTAGEN     242    247       Missing: Abolishes nuclear localization
FT                                and palmitoylation.
FT   MUTAGEN     243    243       R->E: Abolishes nuclear localization;
FT                                when associated with E-246.
FT   MUTAGEN     246    246       R->E: Abolishes nuclear localization;
FT                                when associated with E-243.
FT   MUTAGEN     252    253       CC->AA: Abolishes palmitoylation.
FT   MUTAGEN     252    252       C->S: Strongly reduces palmitoylation and
FT                                its ability to regulate GPCR signaling.
FT                                Abolishes palmitoylation ant its ability
FT                                to regulate GPCR signaling; when
FT                                associated with S-253.
FT   MUTAGEN     253    253       C->S: Strongly reduces palmitoylation and
FT                                its ability to regulate GPCR signaling.
FT                                Abolishes palmitoylation ant its ability
FT                                to regulate GPCR signaling; when
FT                                associated with S-252.
FT   CONFLICT     15     15       S -> A (in Ref. 2; BAB32250).
FT   CONFLICT     47     47       Q -> R (in Ref. 2; BAB32250).
FT   CONFLICT     73     73       S -> F (in Ref. 2; BAB32250).
FT   CONFLICT    138    138       E -> Q (in Ref. 2; BAE23346).
FT   CONFLICT    146    146       L -> V (in Ref. 2; BAB32250).
FT   CONFLICT    188    188       S -> G (in Ref. 3; AAI18958).
SQ   SEQUENCE   257 AA;  29023 MW;  1825969A5E64D544 CRC64;
     MSSAPNGRKK RPSRSTRSSI FQISKPPLQS GDWERRGSGS ESAHKTQRAL DDCKMLVQEF
     NTQVALYREL VISIGDVSVS CPSLRAEMHK TRTKGCEMAR QAHQKLAAIS GPEDGEIHPE
     ICRLYIQLQC CLEMYTTEML KSICLLGSLQ FHRKGKEASG GAKNLDSKIE ENAETPALED
     SLSSPLESQQ QCWQVATDIE NTERDMREMK NLLSKLRETM PLPLKNQDDS SLLNLTPYPM
     VRRRKRRFFG LCCLVSS
//
ID   ZDH14_MOUSE             Reviewed;         489 AA.
AC   Q8BQQ1; Q8BNR2; Q8CFN0;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Probable palmitoyltransferase ZDHHC14;
DE            EC=2.3.1.-;
DE   AltName: Full=NEW1 domain-containing protein;
DE            Short=NEW1CP;
DE   AltName: Full=Zinc finger DHHC domain-containing protein 14;
DE            Short=DHHC-14;
GN   Name=Zdhhc14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=BALB/c; TISSUE=Adipose tissue;
RA   Guo J.H., Chen L., Yu L.;
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex, and Corpora quadrigemina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: Palmitoyl-CoA + protein-cysteine = S-palmitoyl
CC       protein + CoA.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BQQ1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BQQ1-2; Sequence=VSP_016272;
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase
CC       activity (By similarity).
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       ERF2/ZDHHC9 subfamily.
CC   -!- SIMILARITY: Contains 1 DHHC-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC38040.1; Type=Frameshift; Positions=7;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF542387; AAN47141.1; -; mRNA.
DR   EMBL; AK046719; BAC32845.1; -; mRNA.
DR   EMBL; AK080845; BAC38040.1; ALT_FRAME; mRNA.
DR   EMBL; BC059814; AAH59814.1; -; mRNA.
DR   IPI; IPI00403708; -.
DR   IPI; IPI00656220; -.
DR   RefSeq; NP_666185.3; NM_146073.3.
DR   UniGene; Mm.311028; -.
DR   UniGene; Mm.478308; -.
DR   PhosphoSite; Q8BQQ1; -.
DR   PRIDE; Q8BQQ1; -.
DR   Ensembl; ENSMUST00000089185; ENSMUSP00000086589; ENSMUSG00000034265.
DR   GeneID; 224454; -.
DR   KEGG; mmu:224454; -.
DR   UCSC; uc008aff.1; mouse.
DR   CTD; 224454; -.
DR   MGI; MGI:2653229; Zdhhc14.
DR   eggNOG; roNOG07030; -.
DR   HOGENOM; HBG744542; -.
DR   HOVERGEN; HBG056239; -.
DR   InParanoid; Q8BQQ1; -.
DR   OMA; RQIDVAN; -.
DR   OrthoDB; EOG4G7BZ7; -.
DR   PhylomeDB; Q8BQQ1; -.
DR   NextBio; 377190; -.
DR   ArrayExpress; Q8BQQ1; -.
DR   Bgee; Q8BQQ1; -.
DR   CleanEx; MM_ZDHHC14; -.
DR   Genevestigator; Q8BQQ1; -.
DR   GermOnline; ENSMUSG00000034265; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008415; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001594; Znf_DHHC_palmitoyltrfase.
DR   Pfam; PF01529; zf-DHHC; 1.
DR   PROSITE; PS50216; ZF_DHHC; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Alternative splicing; Membrane; Metal-binding;
KW   Phosphoprotein; Transferase; Transmembrane; Transmembrane helix; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    489       Probable palmitoyltransferase ZDHHC14.
FT                                /FTId=PRO_0000212892.
FT   TRANSMEM     61     81       Helical; (Potential).
FT   TRANSMEM     90    110       Helical; (Potential).
FT   TRANSMEM    209    229       Helical; (Potential).
FT   TRANSMEM    256    276       Helical; (Potential).
FT   ZN_FING     165    215       DHHC-type.
FT   ACT_SITE    195    195       S-palmitoyl cysteine intermediate (By
FT                                similarity).
FT   MOD_RES     456    456       Phosphoserine (By similarity).
FT   VAR_SEQ       1    105       Missing (in isoform 2).
FT                                /FTId=VSP_016272.
FT   CONFLICT    274    274       Y -> C (in Ref. 1; AAN47141).
SQ   SEQUENCE   489 AA;  53659 MW;  EFF96E948FA45A03 CRC64;
     MPPGGGGPMK DCEYSQISTH SSSPMESPHK KKKIAARRKW EVFPGRNKFF CNGRIMMARQ
     TGVFYLTLIL ILVTSGLFFA FDCRYLAEKI TPAIPVVGGI LFFFVMGTLL RTSFSDPGVL
     PRATPDEAAD LERQIDIANG TSSGGYRPPP RTKEVVINGQ TVKLKYCFTC KIFRPPRASH
     CSLCDNCVEQ FDHHCPWVGN CVGKRNYRFF YMFILSLSFL TVFIFAFVIT HVIHRSQQKG
     FLDALKDSPA SVLEAVICFF SVWSIIGLSG FHTYLISSNQ TTNEDIKGSW SNKRGKENYN
     PYSYGNIFTN CCVALCGPIS PSLIDRRGYV QPDTPQPAAP SNGITMYGAT QSQSDMCDQD
     QCIQSTKFVL QAAATPLLQS EPSLTSEELH MPGKPGLGTP CASLTLGQPT PPSSMPNLAT
     EATLSDIMPL KDEHGGHQFL TPDEAPSPPR MLGAGSPLAH SRTMHMLGLA SQDSLHEDSV
     RGLVKLSSV
//
ID   Q8BQQ4_MOUSE            Unreviewed;       556 AA.
AC   Q8BQQ4;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   11-JAN-2011, entry version 64.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Ptpn4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Adipose;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Adipose;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Adipose;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Adipose;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Adipose;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Adipose;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Adipose;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Adipose;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 FERM domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK046683; BAC32836.1; -; mRNA.
DR   IPI; IPI00123776; -.
DR   RefSeq; NP_064317.2; NM_019933.2.
DR   UniGene; Mm.458796; -.
DR   HSSP; P11171; 1GG3.
DR   ProteinModelPortal; Q8BQQ4; -.
DR   SMR; Q8BQQ4; 28-368, 510-552.
DR   STRING; Q8BQQ4; -.
DR   Ensembl; ENSMUST00000064091; ENSMUSP00000067614; ENSMUSG00000026384.
DR   GeneID; 19258; -.
DR   KEGG; mmu:19258; -.
DR   CTD; 19258; -.
DR   MGI; MGI:1099792; Ptpn4.
DR   HOVERGEN; HBG098079; -.
DR   InParanoid; Q8BQQ4; -.
DR   NextBio; 296108; -.
DR   ArrayExpress; Q8BQQ4; -.
DR   Bgee; Q8BQQ4; -.
DR   Genevestigator; Q8BQQ4; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0019898; C:extrinsic to membrane; IEA:InterPro.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR   GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IDA:MGI.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR000798; Ez/rad/moesin.
DR   InterPro; IPR014847; FERM-adjacent.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011993; PH_type.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   556 AA;  63649 MW;  EA22106B95F6D006 CRC64;
     MTARFRLPAG RTYNVRASEL ARDRQHTEVV CNILLLDNTV QAFRVNKHDQ GQVLLDIVFK
     HLDLTERDYF GLQLADDSTD NPRWLDPNKP IRKQLKRGSP YNLNFRVKFF VSDPNKLQEE
     YTRYQYFLQI KQDILTGRLS CPCNTAALLA SFAVQSELGD YNQSENLAGY LSDYSFIPNQ
     PQDFEKEIAK LHQQHVGLSP AEAEFNYLNA ARTLELYGVE FHYARDQSNN EILIGVMSGG
     ILIYKNRVRM NTFLWLKIVK ISFKCKQFFI QLRKELHESR ETLLGFNMVN YRACKTLWKA
     CVEHHTFFRL DRPLPPQKNF FAHYFTLGSK FRYCGRTEVQ SVQYGKEKAN KDRVFARSPS
     KPLARKLMDW EVVSRNSLSD DRLETQSLPS RSPPGTPNHR NSSFTQEATR VRPSSVGHLV
     DHVVHMSPSE DFVSQRCPSS TQANSIVLES SPSQETPEDG QPPALPPKQS KKNSWNQIHF
     SNSQQDLVTH TNESFDVPSS PEKSTPNGGI PHDNLVLIKM KPDENGRFGF NVKGGYDQKM
     PVIVSRVAPG TPLSEL
//
ID   CXG2_MOUSE              Reviewed;         440 AA.
AC   Q8BQU6; Q6TLV2; Q8BQS2; Q9EPM1;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 2.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Gap junction gamma-2 protein;
DE   AltName: Full=Connexin-47;
DE            Short=Cx47;
DE   AltName: Full=Gap junction alpha-12 protein;
GN   Name=Gjc2; Synonyms=Gja12;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=129/SvJ;
RX   MEDLINE=21114075; PubMed=11160382;
RA   Teubner B., Odermatt B., Gueldenagel M., Soehl G., Degen J.,
RA   Bukauskas F.F., Kronengold J., Verselis V.K., Jung Y.T., Kozak C.A.,
RA   Schilling K., Willecke K.;
RT   "Functional expression of the new gap junction gene connexin47
RT   transcribed in mouse brain and spinal cord neurons.";
RL   J. Neurosci. 21:1117-1126(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Corpora quadrigemina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-79.
RC   STRAIN=Swiss Webster;
RX   PubMed=15676282; DOI=10.1016/j.ygeno.2004.11.007;
RA   Anderson C.L., Zundel M.A., Werner R.;
RT   "Variable promoter usage and alternative splicing in five mouse
RT   connexin genes.";
RL   Genomics 85:238-244(2005).
RN   [4]
RP   DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=12805295;
RA   Odermatt B., Wellershaus K., Wallraff A., Seifert G., Degen J.,
RA   Euwens C., Fuss B., Buessow H., Schilling K., Steinhaeuser C.,
RA   Willecke K.;
RT   "Connexin 47 (Cx47)-deficient mice with enhanced green fluorescent
RT   protein reporter gene reveal predominant oligodendrocytic expression
RT   of Cx47 and display vacuolized myelin in the CNS.";
RL   J. Neurosci. 23:4549-4559(2003).
RN   [5]
RP   DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=12843301;
RA   Menichella D.M., Goodenough D.A., Sirkowski E., Scherer S.S.,
RA   Paul D.L.;
RT   "Connexins are critical for normal myelination in the CNS.";
RL   J. Neurosci. 23:5963-5973(2003).
RN   [6]
RP   INTERACTION WITH TJP1, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=15183511; DOI=10.1016/j.neuroscience.2004.03.063;
RA   Li X., Ionescu A.V., Lynn B.D., Lu S., Kamasawa N., Morita M.,
RA   Davidson K.G.V., Yasumura T., Rash J.E., Nagy J.I.;
RT   "Connexin47, connexin29 and connexin32 co-expression in
RT   oligodendrocytes and Cx47 association with zonula occludens-1 (ZO-1)
RT   in mouse brain.";
RL   Neuroscience 126:611-630(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
CC   -!- FUNCTION: One gap junction consists of a cluster of closely packed
CC       pairs of transmembrane channels, the connexons, through which
CC       materials of low MW diffuse from one cell to a neighboring cell.
CC       May play a role in myelination in central and peripheral nervous
CC       systems.
CC   -!- SUBUNIT: A connexon is composed of a hexamer of connexins.
CC       Interacts with TJP1.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Cell junction, gap junction.
CC   -!- TISSUE SPECIFICITY: Mainly expressed by oligodendrocytes in the
CC       central nervous system (at protein level).
CC   -!- DEVELOPMENTAL STAGE: Expression starts after birth in the central
CC       nervous system and parallels myelination process.
CC   -!- DISRUPTION PHENOTYPE: Mice display myelination abnormalities
CC       characterized by extracellular vacuolation along nerve fibers.
CC       Mice lacking both Gja12 and Gjb1 display a more severe
CC       demyelination phenotype associated with oligodendrocyte death.
CC       These mice develop action tremors, tonic seizures, sporadic
CC       convulsions and loss of consciousness preceding death in the sixth
CC       week after birth.
CC   -!- SIMILARITY: Belongs to the connexin family. Gamma-type subfamily.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC32806.1; Type=Erroneous initiation;
CC       Sequence=CAC19434.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ276435; CAC19434.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AK046421; BAC32722.1; -; mRNA.
DR   EMBL; AK046609; BAC32806.1; ALT_INIT; mRNA.
DR   EMBL; AY394498; AAR05823.1; -; mRNA.
DR   EMBL; AY394499; AAR05824.1; -; mRNA.
DR   EMBL; AY394500; AAR05825.1; -; mRNA.
DR   IPI; IPI00224027; -.
DR   RefSeq; NP_536702.3; NM_080454.4.
DR   RefSeq; NP_780661.2; NM_175452.4.
DR   UniGene; Mm.40016; -.
DR   ProteinModelPortal; Q8BQU6; -.
DR   SMR; Q8BQU6; 5-291.
DR   MINT; MINT-1891911; -.
DR   STRING; Q8BQU6; -.
DR   TCDB; 1.A.24.2.1; gap junction-forming connexin family.
DR   PhosphoSite; Q8BQU6; -.
DR   PRIDE; Q8BQU6; -.
DR   Ensembl; ENSMUST00000108790; ENSMUSP00000104418; ENSMUSG00000043448.
DR   Ensembl; ENSMUST00000108793; ENSMUSP00000104421; ENSMUSG00000043448.
DR   GeneID; 118454; -.
DR   KEGG; mmu:118454; -.
DR   UCSC; uc007jde.1; mouse.
DR   CTD; 118454; -.
DR   MGI; MGI:2153060; Gjc2.
DR   GeneTree; ENSGT00560000076845; -.
DR   HOGENOM; HBG717760; -.
DR   HOVERGEN; HBG009576; -.
DR   InParanoid; Q8BQU6; -.
DR   OMA; DGKTTVW; -.
DR   OrthoDB; EOG45HRXR; -.
DR   PhylomeDB; Q8BQU6; -.
DR   NextBio; 369746; -.
DR   ArrayExpress; Q8BQU6; -.
DR   Bgee; Q8BQU6; -.
DR   CleanEx; MM_GJC2; -.
DR   Genevestigator; Q8BQU6; -.
DR   GermOnline; ENSMUSG00000043448; Mus musculus.
DR   GO; GO:0005922; C:connexon complex; IEA:InterPro.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005243; F:gap junction channel activity; IDA:MGI.
DR   GO; GO:0007267; P:cell-cell signaling; IDA:MGI.
DR   InterPro; IPR000500; Connexin.
DR   InterPro; IPR019570; Connexin_CCC.
DR   InterPro; IPR017990; Connexin_CS.
DR   InterPro; IPR013092; Connexin_N.
DR   PANTHER; PTHR11984; Connexin; 1.
DR   Pfam; PF00029; Connexin; 1.
DR   Pfam; PF10582; Connexin_CCC; 1.
DR   PRINTS; PR00206; CONNEXIN.
DR   SMART; SM00037; CNX; 1.
DR   PROSITE; PS00407; CONNEXINS_1; 1.
DR   PROSITE; PS00408; CONNEXINS_2; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Gap junction; Membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    440       Gap junction gamma-2 protein.
FT                                /FTId=PRO_0000057843.
FT   TOPO_DOM      1     21       Cytoplasmic (Potential).
FT   TRANSMEM     22     42       Helical; (Potential).
FT   TOPO_DOM     43     78       Extracellular (Potential).
FT   TRANSMEM     79     99       Helical; (Potential).
FT   TOPO_DOM    100    223       Cytoplasmic (Potential).
FT   TRANSMEM    224    244       Helical; (Potential).
FT   TOPO_DOM    245    264       Extracellular (Potential).
FT   TRANSMEM    265    285       Helical; (Potential).
FT   TOPO_DOM    286    440       Cytoplasmic (Potential).
FT   MOD_RES     372    372       Phosphoserine.
FT   CONFLICT    216    216       L -> V (in Ref. 2; BAC32722).
FT   CONFLICT    388    388       V -> A (in Ref. 1; CAC19434).
FT   CONFLICT    408    408       S -> G (in Ref. 1; CAC19434).
SQ   SEQUENCE   440 AA;  47008 MW;  2D11040FE28ADB1E CRC64;
     MTNMSWSFLT RLLEEIHNHS TFVGKVWLTV LVVFRIVLTA VGGESIYSDE QSKFTCNTRQ
     PGCDNVCYDA FAPLSHVRFW VFQIVVISTP SVMYLGYAVH RLARASEQER RRALRRRPGT
     RRLPRAQLPP PPPGWPDTTD LGEAEPILAL EEDEDEEPGA PEGPGEDTEE ERAEDVAAKG
     GGGDGKTVVT PGPAGQHDGR RRIQREGLMR VYVAQLVVRA AFEVAFLVGQ YLLYGFEVPP
     FFACSRQPCP HVVDCFVSRP TEKTVFLLVM YVVSCLCLLL NLCEMAHLGL GSAQDAVRGR
     RGASAAGPGP TPRPPPCAFP AAAAGLACPP DYSLVVRAAE RARAHDQNLA NLALQALRDG
     AAVAAVSADR DSPPCAGLNA TSRGAPRVGG LASGTGSATS GGTVGEQSRP GAQEQLATKP
     RAGSEKGSTG SRDGKATVWI
//
ID   TMM74_MOUSE             Reviewed;         305 AA.
AC   Q8BQU7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=Transmembrane protein 74;
GN   Name=Tmem74;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Plays an essential role in autophagy. TMEM74-induced
CC       autophagy may involve PI3K signal transduction (By similarity).
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane; Multi-pass membrane
CC       protein. Cytoplasmic vesicle, autophagosome membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK046420; BAC32721.1; -; mRNA.
DR   EMBL; BC117021; AAI17022.1; -; mRNA.
DR   EMBL; BC117025; AAI17026.1; -; mRNA.
DR   IPI; IPI00224031; -.
DR   RefSeq; NP_780711.1; NM_175502.3.
DR   UniGene; Mm.41219; -.
DR   UniGene; Mm.461451; -.
DR   ProteinModelPortal; Q8BQU7; -.
DR   PRIDE; Q8BQU7; -.
DR   Ensembl; ENSMUST00000067469; ENSMUSP00000070748; ENSMUSG00000054409.
DR   GeneID; 239408; -.
DR   KEGG; mmu:239408; -.
DR   UCSC; uc007vpn.1; mouse.
DR   CTD; 239408; -.
DR   MGI; MGI:2443417; Tmem74.
DR   eggNOG; roNOG08065; -.
DR   GeneTree; ENSGT00530000063880; -.
DR   HOGENOM; HBG279387; -.
DR   HOVERGEN; HBG094072; -.
DR   InParanoid; Q8BQU7; -.
DR   OMA; NEWSHEA; -.
DR   OrthoDB; EOG498V1G; -.
DR   PhylomeDB; Q8BQU7; -.
DR   NextBio; 384109; -.
DR   ArrayExpress; Q8BQU7; -.
DR   Bgee; Q8BQU7; -.
DR   CleanEx; MM_TMEM74; -.
DR   Genevestigator; Q8BQU7; -.
DR   GermOnline; ENSMUSG00000054409; Mus musculus.
DR   GO; GO:0000421; C:autophagic vacuole membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Autophagy; Cytoplasmic vesicle; Lysosome; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    305       Transmembrane protein 74.
FT                                /FTId=PRO_0000259601.
FT   TRANSMEM    178    198       Helical; (Potential).
FT   TRANSMEM    232    252       Helical; (Potential).
FT   COMPBIAS    159    162       Poly-Asp.
SQ   SEQUENCE   305 AA;  33416 MW;  F53CB0F09DEBEAA9 CRC64;
     MELHSLSKRN SPVDPCNALE WSSGETSGDH IEEATIRDAF CYQKNLVSTP RADVVEVCRL
     STSPASPTSL LQDSAIQTSF SLSGPPDSGN NQVMADRKVC NCCSQELETS FTYVDENVNL
     EQRSQRSPSA KGSNHPVDLG WGNPNEWSHE TAMSLMSEDD DDTSSEATSS GKSVDYGFIS
     AILFLVTGIL LVIISYIVPR EVTVDPNTVA AREMERLEKE SAMLGAHLDR CVIAGLCLLT
     LGGVVLSCLL MMSMWKGELY RRNRFASSKE SAKLYGSFNF RMKTSTNEDT LELSLVEEDA
     LAVQS
//
ID   RLGPB_MOUSE             Reviewed;        1484 AA.
AC   Q8BQZ4; Q80TH5; Q8BQN1;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 2.
DT   08-FEB-2011, entry version 57.
DE   RecName: Full=Ral GTPase-activating protein subunit beta;
DE   AltName: Full=p170;
GN   Name=Ralgapb; Synonyms=Kiaa1219;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1225-1484 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Corpus striatum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 313-1484 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   INTERACTION WITH RALGAPA2, AND TISSUE SPECIFICITY.
RX   PubMed=16490346; DOI=10.1016/j.cellsig.2006.01.002;
RA   Gridley S., Chavez J.A., Lane W.S., Lienhard G.E.;
RT   "Adipocytes contain a novel complex similar to the tuberous sclerosis
RT   complex.";
RL   Cell. Signal. 18:1626-1632(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-710, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Non-catalytic subunit of the heterodimeric RalGAP1 and
CC       RalGAP2 complexes which act as GTPase activators for the Ras-like
CC       small GTPases RALA and RALB (By similarity).
CC   -!- SUBUNIT: Component of the heterodimeric RalGAP1 complex with
CC       RALGAPA1 and of the heterodimeric RalGAP2 complex with RALGAPA2.
CC       Heterodimerization is required for activity (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BQZ4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BQZ4-2; Sequence=VSP_009697, VSP_009698;
CC         Note=May be due to intron retention. No experimental
CC         confirmation available;
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in testis, pancreas,
CC       lung, thymus, brown fat, and white fat. Expressed at lower levels
CC       in the brain.
CC   -!- SIMILARITY: Contains 1 Rap-GAP domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC33137.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK046067; BAC32589.1; -; mRNA.
DR   EMBL; AK047718; BAC33137.1; ALT_INIT; mRNA.
DR   EMBL; AK122470; BAC65752.1; -; mRNA.
DR   IPI; IPI00663802; -.
DR   IPI; IPI00875478; -.
DR   RefSeq; NP_808326.2; NM_177658.3.
DR   UniGene; Mm.398185; -.
DR   ProteinModelPortal; Q8BQZ4; -.
DR   STRING; Q8BQZ4; -.
DR   PhosphoSite; Q8BQZ4; -.
DR   PRIDE; Q8BQZ4; -.
DR   Ensembl; ENSMUST00000046274; ENSMUSP00000048430; ENSMUSG00000027652.
DR   GeneID; 228850; -.
DR   KEGG; mmu:228850; -.
DR   UCSC; uc008nqg.1; mouse.
DR   UCSC; uc008nqh.1; mouse.
DR   CTD; 228850; -.
DR   MGI; MGI:2444531; Ralgapb.
DR   GeneTree; ENSGT00390000008398; -.
DR   HOVERGEN; HBG052199; -.
DR   NextBio; 379202; -.
DR   ArrayExpress; Q8BQZ4; -.
DR   Bgee; Q8BQZ4; -.
DR   CleanEx; MM_B230339M05RIK; -.
DR   Genevestigator; Q8BQZ4; -.
DR   GermOnline; ENSMUSG00000027652; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0017123; F:Ral GTPase activator activity; ISS:UniProtKB.
DR   GO; GO:0032859; P:activation of Ral GTPase activity; ISS:UniProtKB.
DR   InterPro; IPR000331; Rap_GAP.
DR   PROSITE; PS50085; RAPGAP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; GTPase activation; Phosphoprotein.
FT   CHAIN         1   1484       Ral GTPase-activating protein subunit
FT                                beta.
FT                                /FTId=PRO_0000056757.
FT   DOMAIN     1138   1382       Rap-GAP.
FT   MOD_RES     417    417       Phosphoserine (By similarity).
FT   MOD_RES     421    421       Phosphoserine (By similarity).
FT   MOD_RES     710    710       Phosphoserine.
FT   MOD_RES     724    724       Phosphothreonine (By similarity).
FT   VAR_SEQ     473    490       ASFIQILLSYKSSIATQA -> GKYAQKHVVIIPFLFLSF
FT                                (in isoform 2).
FT                                /FTId=VSP_009697.
FT   VAR_SEQ     491   1484       Missing (in isoform 2).
FT                                /FTId=VSP_009698.
FT   CONFLICT   1477   1477       V -> A (in Ref. 1; BAC33137).
SQ   SEQUENCE   1484 AA;  165200 MW;  24CD07B42542920C CRC64;
     MYSEWRSLHL VIQSDQGHTS VLHSYPESVG REVANAVVRP LGQALGTSSV AGSESLLKTD
     KEVKWTMEVI CYGLTLPLDG ETVKYCVDVY TDWIMALVLP KDSIPLPIIK EPNLYVQSIL
     KHLQNLFVPR QEQGSSQIRL CLQVLRAIQK LARESSIMAR ETWEVLLLFL LQINDILLAP
     PTVQGGIAEN LAEKLIGVLF EVWLLACTRC FPTPPYWKTA KEMVANWRHH PAVVEQWSKV
     ICALTSRLLR FTYGPSFPPF KVPDEDANLI PPEMDNECIA QTWFRFLHML SNPVDLSNPA
     VISSTPKFQE QFLNVSGMPQ ELSQYPCLKH LPQIFFRAMR GISCLVDAFL GISRPRSDSA
     PPTPVNRLSM PQSAAVNTTP PHNRRHRAVT VNKATMKTST VTTAHTSKVQ HQASSTSPLS
     SPNQTSSEPR PLPAPRRPKV NSILNLFGSW LFDAAFVHCK LHNGINRDNS MTASFIQILL
     SYKSSIATQA SMEFRRKGSQ MSTDTMVSNP VFDASEFPDN YEAGRAEACG TLCRIFCSKK
     TGEEILPAYL SSVILNSPPL FCCDLKGIDV VVPYFISALE TILPDRELSK FKSYVNPTEL
     RRSSINILLS LLPLPHHFGT VRSEVVLEGK FSNDDSSSYD KPITFLSLKL RLVNILIGAL
     QTETDPNNTQ MILGAMLNIV QDSALLEAIG CQMEMGGGEN NLKSHSRTNS GISSASGGST
     EPTTPDSERP AQALLRDYGS TDSAAGLLIR SIHLVTQRLN SQWRQDMSIS LAALELLSGL
     AKVKVMVDSG DRKRAISSVC SYIVYQCSRP APLHSRDLHS MIVAAFQCLC VWLTEHPDML
     DEKDCLKEVL EIVELGISGS KSKNSEQEVK YKGDKEPNPA SMRVKDAAEA TLTCIMQLLG
     AFPSPSGPAS PCSLVNETTL IKYSRLPTIN KHSFRYFVLD NSVILAMLEQ PLGNEQNDFF
     PSVTVLVRGM SGRLAWAQQL CLLPRGAKAN QKLFVPEPRP VPKNDVGFKY SVKHRPFPEE
     VDKIPFVKAD LSIPDLHEIV TEELEERHEK LRSGMAQQIA YEMHLEQQSE GELQKRSFPD
     PVTDCKPPPP AQEFQTARLF LSHFGFLSLE ALKEPANSRL PPHLIALDST IPGFFDDIGY
     LDLLPCRPFD TVFIFYMKPG QKTNQEILKN VESSRNVQPH FLEFLLSLGW SVDVGKHPGW
     TGHVSTSWSI NSCDDGEGSE PDEITSSEDV GASIFNGQKK VLYYADALTE IAFVVPSPVE
     SLTDSLESNI SDQDSDSNMD LMPGILKQPP LTLELVPNHT DSLNSSQRLS PSSRMKKLPQ
     GRPVPPLGPE TRVSVVWVER YDDIENFPLS DLMTEISTGV ETTANSSTSL RSTTLEKEVP
     VIFIHPLNTG LFRIKIQGAT GKFNMVIPLV DGMIVSRRAL GFLVRQTVIN ICRRKRLESD
     SYSPPHVRRK QKITDIVNKY RNKQLEPEFY TALFQEVGLK NCSS
//
ID   Q8BR46_MOUSE            Unreviewed;       173 AA.
AC   Q8BR46;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 42.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Tmem44;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK045675; BAC32454.1; -; mRNA.
DR   IPI; IPI00876228; -.
DR   UniGene; Mm.241459; -.
DR   Ensembl; ENSMUST00000023188; ENSMUSP00000023188; ENSMUSG00000022537.
DR   MGI; MGI:1924489; Tmem44.
DR   eggNOG; roNOG13760; -.
DR   GeneTree; ENSGT00390000018718; -.
DR   HOVERGEN; HBG064860; -.
DR   ArrayExpress; Q8BR46; -.
DR   Bgee; Q8BR46; -.
DR   Genevestigator; Q8BR46; -.
PE   1: Evidence at protein level;
SQ   SEQUENCE   173 AA;  19222 MW;  BB7D4412AF5BE616 CRC64;
     MSRAFRFATA EARESADTQA LLTCAEKEEE NQEARTEDKN SDWVPLTSLS HCKPLRTMTA
     ISRYMELTIE PAQQAGCSAT RLPGDGQTST RDAASQEPPS YPPIQVIQAR VSSSSSSEVS
     SINSDLEQKY WEALNSEQWD PEDVNLERKK DGELLRVQVR RASLSPVDLA SDD
//
ID   Q8BR49_MOUSE            Unreviewed;       999 AA.
AC   Q8BR49;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Herc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK045649; BAC32444.1; -; mRNA.
DR   IPI; IPI00676574; -.
DR   UniGene; Mm.244179; -.
DR   ProteinModelPortal; Q8BR49; -.
DR   STRING; Q8BR49; -.
DR   PRIDE; Q8BR49; -.
DR   Ensembl; ENSMUST00000042824; ENSMUSP00000044801; ENSMUSG00000038664.
DR   Ensembl; ENSMUST00000098618; ENSMUSP00000096218; ENSMUSG00000038664.
DR   MGI; MGI:2384589; Herc1.
DR   InParanoid; Q8BR49; -.
DR   ArrayExpress; Q8BR49; -.
DR   Bgee; Q8BR49; -.
DR   Genevestigator; Q8BR49; -.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00320; WD40; 2.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Repeat; WD repeat.
FT   NON_TER     999    999
SQ   SEQUENCE   999 AA;  108008 MW;  FF8CFF8E5588A283 CRC64;
     MSSSLEDTTT ATTPVTDTET VPASESPGVM PLSLLRQMFS SYPTTTVLPT RRAQTPPISS
     LPASPSDEVG RRQSLTSPDS QSTRPANRTA LSDPSSRLST SPPPPAIAVP LLEMGFSLRQ
     IAKAMEATGA RGEADAQSIT VLAMWMIEHP GHEDEEEPQP SSTADSRHGA TVLGSGGKSN
     DPCYLQSPGD IPSADAAEME EGFSESPDNL DHTENAASGS GPPTRGRSTV TRRHKFDLAA
     RTLLARAAGL YRSVQAHRNQ SRREGISLQQ DPGALYDFNL DEELEIDLDD EAMEAMFGQD
     LTSDNDILGM WIPEVLDWPT WHVCESEDRE EVVVCELCEC NVVSFNQHMK RNHPGCGRSA
     NRQGYRSNGS YVDGWFGGEC GSGNPYYLLC GSCREKYLAL KTKTKTTNSE RYKGQAPDLI
     GKQDSVYEED WDMLDVDEDE KLTGEEEFEL LAGPLGLNDR RIVPEPVQFP DSDPLGASVA
     MVTATNSMEE TLMQIGCHGS VEKSSSGRVT LGEQAAALAN PHDRVVALRR VTAAAQVLLA
     RTMVMRALSL LSVSGSSCSL AAGLESLGLT DIRTLVRLMC LAAAGRAGLS TSPSAIASTS
     ERSRGGHSKA SKPISCLAYL STAVGCLASN TPSAAKLLVQ LCTQNLISAA TGVNLTTVDD
     PIQRKFLPSF LRGIAEENKL VTSPNFVVTQ ALVALLADKG AKLRPNYDKT EIEKKGPLEL
     ANALAACCLS SRLSSQHRQW AAQQLVRTLA AHDRDNQTAP QTLADMGGDL RKCSFIKLEA
     HQNRVMTCVW CNKKGLLATS GNDGTIRVWN VTKKQYSLQQ TCVFNRLEGD AEESLGSPSD
     PSFSPVSWSI SGKYLAGALE KMVNIWQVNG GKGLVDIQPH WVSALAWPEE GPATTWSGES
     PELLLVGRMD GSLGLIEVVD VSTMHRRELE HCYRKDVSVT CIAWFSEDRP FAVGYFDGKL
     LMGTKEPLEK GGIVLIDAHK ETLVSMKWDP TGHILMTCA
//
ID   F177A_MOUSE             Reviewed;         207 AA.
AC   Q8BR63; Q9D9M7;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Protein FAM177A1;
GN   Name=Fam177a1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the FAM177 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB24712.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK006713; BAB24712.1; ALT_INIT; mRNA.
DR   EMBL; AK045530; BAC32408.1; -; mRNA.
DR   EMBL; BC048158; AAH48158.1; -; mRNA.
DR   EMBL; BC049669; AAH49669.1; -; mRNA.
DR   IPI; IPI00224068; -.
DR   RefSeq; NP_001093586.1; NM_001100116.1.
DR   RefSeq; NP_082803.1; NM_028527.1.
DR   UniGene; Mm.439875; -.
DR   ProteinModelPortal; Q8BR63; -.
DR   PhosphoSite; Q8BR63; -.
DR   PRIDE; Q8BR63; -.
DR   Ensembl; ENSMUST00000038355; ENSMUSP00000037916; ENSMUSG00000034953.
DR   Ensembl; ENSMUST00000101415; ENSMUSP00000098960; ENSMUSG00000073083.
DR   GeneID; 100101807; -.
DR   GeneID; 73385; -.
DR   KEGG; mmu:100101807; -.
DR   KEGG; mmu:73385; -.
DR   UCSC; uc007nog.1; mouse.
DR   CTD; 100101807; -.
DR   CTD; 73385; -.
DR   MGI; MGI:1920635; 1700047I17Rik1.
DR   GeneTree; ENSGT00390000016736; -.
DR   HOGENOM; HBG444589; -.
DR   HOVERGEN; HBG051003; -.
DR   InParanoid; Q8BR63; -.
DR   OMA; MESKQNP; -.
DR   OrthoDB; EOG4FJ8BG; -.
DR   PhylomeDB; Q8BR63; -.
DR   NextBio; 462652; -.
DR   CleanEx; MM_1700047I17RIK1; -.
DR   Genevestigator; Q8BR63; -.
DR   GermOnline; ENSMUSG00000034953; Mus musculus.
DR   GermOnline; ENSMUSG00000073083; Mus musculus.
PE   2: Evidence at transcript level;
KW   Coiled coil; Phosphoprotein.
FT   CHAIN         1    207       Protein FAM177A1.
FT                                /FTId=PRO_0000089886.
FT   COILED      131    170       Potential.
FT   MOD_RES      65     65       Phosphoserine (By similarity).
FT   MOD_RES      66     66       Phosphothreonine (By similarity).
SQ   SEQUENCE   207 AA;  23578 MW;  61CEA19A6B58FBCD CRC64;
     MERESGCAAA GETEAAAATA FRDATRQISN ERGFENVELG VMGKKKKVPR RVIHFVSGET
     MEEYSTDEDE VDGLDKKDVL PTVDPTKLTW GPYLWFYMLR AATSTLSVCD FLGEKIASVL
     GISTPKYQYA IDEYYRMKKE EEEEEEENRM SEEAERQYQQ NKLQADSIVQ TDQPETVSSS
     FVNINFEMEE DCEAIKENKQ RPVSVPP
//
ID   SDS3_MOUSE              Reviewed;         328 AA.
AC   Q8BR65; Q3UC92; Q6P6K1; Q7TNT0; Q8BRR7; Q8K5B4;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Sin3 histone deacetylase corepressor complex component SDS3;
DE   AltName: Full=Suppressor of defective silencing 3 protein homolog;
GN   Name=Suds3; Synonyms=Sds3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, INTERACTION WITH SIN3A
RP   AND SIN3B, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6;
RX   MEDLINE=21907235; PubMed=11909966;
RX   DOI=10.1128/MCB.22.8.2743-2750.2002;
RA   Alland L., David G., Shen-Li H., Potes J., Muhle R., Lee H.-C.,
RA   Hou H. Jr., Chen K., DePinho R.A.;
RT   "Identification of mammalian Sds3 as an integral component of the
RT   Sin3/histone deacetylase corepressor complex.";
RL   Mol. Cell. Biol. 22:2743-2750(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Aorta, Bone marrow macrophage, Brain cortex,
RC   Corpora quadrigemina, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; THR-49 AND THR-244,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Regulatory protein which represses transcription and
CC       augments histone deacetylase activity of HDAC1. May have a
CC       potential role in tumor suppressor pathways. May function in the
CC       assembly and/or enzymatic activity of the mSin3A corepressor
CC       complex or in mediating interactions between the complex and other
CC       regulatory complexes (By similarity).
CC   -!- SUBUNIT: Interacts with HCFC1 (By similarity). Homodimer.
CC       Component of the SIN3 histone deacetylase (HDAC) corepressor
CC       complex. Interacts with SIN3A. Interaction with SIN3B enhances the
CC       interaction between SIN3B and HDAC1 to form a complex. Component
CC       of a mSin3A corepressor complex that contains SIN3A, SAP130,
CC       SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2 (By similarity).
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-591431, EBI-591431;
CC       Q60520:Sin3a; NbExp=4; IntAct=EBI-591431, EBI-349034;
CC       Q62141:Sin3b; NbExp=5; IntAct=EBI-591431, EBI-591450;
CC   -!- TISSUE SPECIFICITY: Expressed in all newborn tissues tested,
CC       including brain, kidney and liver.
CC   -!- DOMAIN: The C-terminus is involved in transcriptional repression
CC       by HDAC-independent mechanisms (By similarity).
CC   -!- SIMILARITY: Belongs to the SDS3 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF469109; AAM22676.1; -; mRNA.
DR   EMBL; AK043652; BAC31608.1; -; mRNA.
DR   EMBL; AK045475; BAC32387.1; -; mRNA.
DR   EMBL; AK138947; BAE23831.1; -; mRNA.
DR   EMBL; AK150633; BAE29722.1; -; mRNA.
DR   EMBL; BC055764; AAH55764.2; -; mRNA.
DR   EMBL; BC062176; AAH62176.1; -; mRNA.
DR   IPI; IPI00408803; -.
DR   RefSeq; NP_001116138.1; NM_001122666.1.
DR   RefSeq; NP_848737.3; NM_178622.4.
DR   UniGene; Mm.34456; -.
DR   IntAct; Q8BR65; 12.
DR   STRING; Q8BR65; -.
DR   PhosphoSite; Q8BR65; -.
DR   PRIDE; Q8BR65; -.
DR   Ensembl; ENSMUST00000086471; ENSMUSP00000083662; ENSMUSG00000066900.
DR   GeneID; 71954; -.
DR   KEGG; mmu:71954; -.
DR   UCSC; uc008zff.1; mouse.
DR   CTD; 71954; -.
DR   MGI; MGI:1919204; Suds3.
DR   eggNOG; roNOG10493; -.
DR   GeneTree; ENSGT00530000063177; -.
DR   HOGENOM; HBG446382; -.
DR   HOVERGEN; HBG108465; -.
DR   InParanoid; Q8BR65; -.
DR   OMA; VEMKEQM; -.
DR   OrthoDB; EOG4N8R5F; -.
DR   NextBio; 335040; -.
DR   ArrayExpress; Q8BR65; -.
DR   Bgee; Q8BR65; -.
DR   Genevestigator; Q8BR65; -.
DR   GermOnline; ENSMUSG00000066900; Mus musculus.
DR   GO; GO:0016580; C:Sin3 complex; IDA:UniProtKB.
DR   GO; GO:0042826; F:histone deacetylase binding; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0016481; P:negative regulation of transcription; IDA:UniProtKB.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR013907; Sds3.
DR   Pfam; PF08598; Sds3; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Coiled coil; Phosphoprotein; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    328       Sin3 histone deacetylase corepressor
FT                                complex component SDS3.
FT                                /FTId=PRO_0000097653.
FT   REGION      188    226       Sin3 interaction domain (SID).
FT   COILED       66    171       Potential.
FT   MOD_RES      45     45       Phosphoserine.
FT   MOD_RES      49     49       Phosphothreonine.
FT   MOD_RES      53     53       Phosphoserine (By similarity).
FT   MOD_RES      55     55       Phosphothreonine (By similarity).
FT   MOD_RES     234    234       Phosphoserine (By similarity).
FT   MOD_RES     236    236       Phosphoserine (By similarity).
FT   MOD_RES     237    237       Phosphoserine (By similarity).
FT   MOD_RES     244    244       Phosphothreonine.
FT   CONFLICT    142    142       K -> N (in Ref. 2; BAC31608).
FT   CONFLICT    186    186       R -> W (in Ref. 1; AAM22676).
FT   CONFLICT    326    328       SAA -> KFLTYRD (in Ref. 3; AAH62176).
SQ   SEQUENCE   328 AA;  38107 MW;  05C22EA578C318E8 CRC64;
     MSAAGLLAPA PAPAAAPAAP EYYPEDEEEL ESAEDDERSC RGRESDEDTE DASETDLAKH
     DEEDYVEMKE QMYQDKLASL KRQLQQLQEG TLQEYQKRMK KLDQQYRERI RNAELFLQLE
     TEQVERNYIK EKKAAVKEFE DKKVELKENL IAELEEKKKM IENEKLTMEL TGDSMEVKPI
     MTRKLRRRPN DPVPIPDKRR KPAPAQLNYL LTDEQIMEDL RTLNKLKSPK RPASPSSPEH
     LPATPAESPA QRFEARIEDG KLYYDKRWYH KSQAIYLESK DNQKLSCVIS SVGANEIWVR
     KTSDSTKMRI YVGQLQRGLF VIRRRSAA
//
ID   PALM2_MOUSE             Reviewed;         376 AA.
AC   Q8BR92;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 53.
DE   RecName: Full=Paralemmin-2;
DE   Flags: Precursor;
GN   Name=Palm2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315 AND SER-355, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (By similarity).
CC   -!- SIMILARITY: Belongs to the paralemmin family.
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DR   EMBL; AK045344; BAC32319.1; -; mRNA.
DR   EMBL; BC113156; AAI13157.1; -; mRNA.
DR   IPI; IPI00648755; -.
DR   RefSeq; NP_766456.1; NM_172868.3.
DR   UniGene; Mm.331630; -.
DR   STRING; Q8BR92; -.
DR   PhosphoSite; Q8BR92; -.
DR   PRIDE; Q8BR92; -.
DR   Ensembl; ENSMUST00000102904; ENSMUSP00000099968; ENSMUSG00000090053.
DR   Ensembl; ENSMUST00000102905; ENSMUSP00000099969; ENSMUSG00000090053.
DR   GeneID; 242481; -.
DR   KEGG; mmu:242481; -.
DR   UCSC; uc008syg.1; mouse.
DR   CTD; 242481; -.
DR   MGI; MGI:1934601; Palm2.
DR   GeneTree; ENSGT00530000063206; -.
DR   HOVERGEN; HBG007431; -.
DR   NextBio; 385357; -.
DR   ArrayExpress; Q8BR92; -.
DR   Bgee; Q8BR92; -.
DR   CleanEx; MM_PALM2; -.
DR   Genevestigator; Q8BR92; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:InterPro.
DR   InterPro; IPR004965; Paralemmin.
DR   Pfam; PF03285; Paralemmin; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Coiled coil; Lipoprotein; Membrane; Methylation;
KW   Palmitate; Phosphoprotein; Prenylation.
FT   CHAIN         1    373       Paralemmin-2.
FT                                /FTId=PRO_0000273447.
FT   PROPEP      374    376       Removed in mature form (Potential).
FT                                /FTId=PRO_0000396694.
FT   COILED        1     34       Potential.
FT   COILED       67    108       Potential.
FT   MOD_RES     315    315       Phosphoserine.
FT   MOD_RES     355    355       Phosphoserine.
FT   MOD_RES     373    373       Cysteine methyl ester (Potential).
FT   LIPID       370    370       S-palmitoyl cysteine (Potential).
FT   LIPID       372    372       S-palmitoyl cysteine (Potential).
FT   LIPID       373    373       S-farnesyl cysteine (Potential).
SQ   SEQUENCE   376 AA;  42095 MW;  8ACC5973898D28F4 CRC64;
     MAEAELHKER LQAIAEKRKR QTEIEGKRRQ LDEQVLLLQH SKSKVLREKW LLQGVPAGTA
     EEEEARRRQS EEDEFKVKQL EDNIQRLEQE IQALESEESQ ISAKEQIILE KLKETEKSFK
     DLQKSFSTAD GAIYAMEINV EKDKQTGETK ILSASTIGPE GVHQRGVKVY DDGTKVVYEV
     HSGGTVVENG VHKLSAKDVE ELIQKAGQSS FRRHMSERTV VADGSLGHPK EHMLCKEAKL
     EMVQKSRKDQ SSGNPGQQAQ PPITEEPGAN LDQPVTMIFM GYQNIEDEEE TKKVLGYDET
     IKAELVLIDE DDEKSLREKT VTDVSTIDGN AAELVSGRPL SDTTEPSSPE GKEESLATDP
     APGTQKKKRC QCCVVM
//
ID   SCFD1_MOUSE             Reviewed;         639 AA.
AC   Q8BRF7; Q8BRZ2; Q8K179; Q9CXR8;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Sec1 family domain-containing protein 1;
DE   AltName: Full=Syntaxin-binding protein 1-like 2;
GN   Name=Scfd1; Synonyms=Stxbp1l2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Aorta, Embryo, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-597 (ISOFORM 3).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Plays a role in SNARE-pin assembly and Golgi-to-ER
CC       retrograde transport via its interaction with COG4. Involved in
CC       vesicular transport between the endoplasmic reticulum and the
CC       Golgi (By similarity).
CC   -!- SUBUNIT: Binds STX5A. Interacts with the COG complex via COG4 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Endoplasmic
CC       reticulum membrane; Peripheral membrane protein (By similarity).
CC       Golgi apparatus, Golgi stack membrane; Peripheral membrane protein
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BRF7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BRF7-2; Sequence=VSP_011310, VSP_011311;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8BRF7-3; Sequence=VSP_011312, VSP_011313;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH27793.1; Type=Erroneous initiation;
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DR   EMBL; AK014070; BAB29141.1; -; mRNA.
DR   EMBL; AK041028; BAC30788.1; -; mRNA.
DR   EMBL; AK044943; BAC32152.1; -; mRNA.
DR   EMBL; BC027793; AAH27793.1; ALT_INIT; mRNA.
DR   IPI; IPI00224219; -.
DR   IPI; IPI00457667; -.
DR   IPI; IPI00457668; -.
DR   RefSeq; NP_084101.1; NM_029825.2.
DR   UniGene; Mm.216511; -.
DR   ProteinModelPortal; Q8BRF7; -.
DR   SMR; Q8BRF7; 10-149.
DR   STRING; Q8BRF7; -.
DR   PhosphoSite; Q8BRF7; -.
DR   PRIDE; Q8BRF7; -.
DR   Ensembl; ENSMUST00000021335; ENSMUSP00000021335; ENSMUSG00000020952.
DR   Ensembl; ENSMUST00000085415; ENSMUSP00000082536; ENSMUSG00000020952.
DR   Ensembl; ENSMUST00000110735; ENSMUSP00000106363; ENSMUSG00000020952.
DR   GeneID; 76983; -.
DR   KEGG; mmu:76983; -.
DR   UCSC; uc007nmp.1; mouse.
DR   UCSC; uc007nmq.1; mouse.
DR   CTD; 76983; -.
DR   MGI; MGI:1924233; Scfd1.
DR   GeneTree; ENSGT00550000074845; -.
DR   HOGENOM; HBG435256; -.
DR   HOVERGEN; HBG061536; -.
DR   InParanoid; Q8BRF7; -.
DR   OMA; TTKPMGL; -.
DR   OrthoDB; EOG4BP1B8; -.
DR   PhylomeDB; Q8BRF7; -.
DR   NextBio; 346238; -.
DR   ArrayExpress; Q8BRF7; -.
DR   Bgee; Q8BRF7; -.
DR   CleanEx; MM_SCFD1; -.
DR   Genevestigator; Q8BRF7; -.
DR   GermOnline; ENSMUSG00000020952; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; IEA:InterPro.
DR   InterPro; IPR001619; Sec1-like.
DR   PANTHER; PTHR11679; Sec1-like; 1.
DR   Pfam; PF00995; Sec1; 1.
DR   SUPFAM; SSF56815; Sec1-like; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Endoplasmic reticulum;
KW   ER-Golgi transport; Golgi apparatus; Membrane; Phosphoprotein;
KW   Protein transport; Transport.
FT   CHAIN         1    639       Sec1 family domain-containing protein 1.
FT                                /FTId=PRO_0000206288.
FT   MOD_RES      54     54       Phosphoserine (By similarity).
FT   MOD_RES     300    300       Phosphoserine (By similarity).
FT   MOD_RES     525    525       Phosphoserine (By similarity).
FT   VAR_SEQ     385    390       SLPELL -> ALMSVH (in isoform 2).
FT                                /FTId=VSP_011310.
FT   VAR_SEQ     391    639       Missing (in isoform 2).
FT                                /FTId=VSP_011311.
FT   VAR_SEQ     578    597       VPRNKSPFQEAIVFVVGGGN -> FLYKTEEPPASQEGGPG
FT                                IPS (in isoform 3).
FT                                /FTId=VSP_011312.
FT   VAR_SEQ     598    639       Missing (in isoform 3).
FT                                /FTId=VSP_011313.
FT   CONFLICT    328    328       G -> E (in Ref. 1; BAB29141).
SQ   SEQUENCE   639 AA;  72323 MW;  D7058563F8549322 CRC64;
     MVGSKMAATA SIRERQTVAL KRMLNFNVPH VKNSTGEPVW KVLIYDRFGQ DIISPLLSVK
     ELRDMGITLH LLLHSDRDPI PDVPAVYFVM PTEENIDRLC QDLRNQLYES YYLNFISAIS
     RSKLEDIANA ALAASAVTQV AKVFDQYLNF ITLEDDMFVL CNQNKELVSY RAINRPDITD
     TEMETVMDTI VDSLFCFFVT LGAVPIIRCS RGTAAEMVAV KLDKKLRENL RDARNSLFTG
     DPLGTGQFSF QRPLLVLVDR NIDLATPLHH TWTYQALVHD VLDFHLNRVN LEESTGVENS
     PAGARPKRKN KKSYDLTPVD KFWQKHKGSP FPEVAESVQQ ELESYRAQED EVKRLKSIMG
     LEGEDEGAIS MLSDNTAKLT SAVSSLPELL EKKRLIDLHT NVATAVLEHI KARKLDVYFE
     YEEKIMSKTT LDKSLLDVIS DPDAGTPEDK MRLFLIYYIS AQQAPSEVDL EQYKKALTDA
     GCNLSPLQYI KQWKAFAKMA STPASYGNTT TKPMGLLSRV MNTGSQFVME GVKNLVLKQQ
     NLPVTRILDN LMEMKSNPET DDYRYFDPKM LRSNDSSVPR NKSPFQEAIV FVVGGGNYIE
     YQNLVDYIKA KQGKHILYGC SEIFNATQFI KQLSQLGQK
//
ID   Q8BRI0_MOUSE            Unreviewed;       682 AA.
AC   Q8BRI0;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 45.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Gm15800; Synonyms=AU042671;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK044167; BAC31803.1; -; mRNA.
DR   IPI; IPI00918533; -.
DR   UniGene; Mm.184589; -.
DR   UniGene; Mm.481359; -.
DR   ProteinModelPortal; Q8BRI0; -.
DR   PRIDE; Q8BRI0; -.
DR   Ensembl; ENSMUST00000055859; ENSMUSP00000050662; ENSMUSG00000042744.
DR   Ensembl; ENSMUST00000119892; ENSMUSP00000112647; ENSMUSG00000042744.
DR   MGI; MGI:3647820; Gm15800.
DR   GeneTree; ENSGT00600000084546; -.
DR   InParanoid; Q8BRI0; -.
DR   ArrayExpress; Q8BRI0; -.
DR   Bgee; Q8BRI0; -.
DR   Genevestigator; Q8BRI0; -.
PE   2: Evidence at transcript level;
FT   NON_TER     682    682
SQ   SEQUENCE   682 AA;  73476 MW;  BFB92077FB31F7D5 CRC64;
     MSVEDCGNVE LPPWSYSVPS LNSEQEDPSD PASKIASLLL AKLADYVVPG CQTVLSPTAS
     EPDTTLTKTS PKNSLKGDKD PGEESEAVDG KLSIFIHKRE DQSSHEVLQP LLSSSEGRPF
     RLGTGANMEK VVKMDRDMTK GGCCEVITEE ASAALRKATK WAQSGLIVSV GPPVESINPE
     TVSGLSTGDK KKTAQTSICR ERNSELARTD PVRPFISGHV ANSMAAEVIA LLHSLLMAPE
     SNAAQIWTTT AEKVLSRALM YIPQLGKYAE SILENGSSSG RKLAKLQRIA RQAVAALCAL
     GGFKETIKIG SEVQVLGRGI SGSIGVVASI NEQEGIATVR FPPVDCRRTS QAADTLTIPL
     SRLCVPRSEA LPLHKLSITE KVVQAVQSML LPQEGSLSIH TSLPATGDGS APVMAVVRLL
     AEIRTRACLV MAQLLEDSLF CEEFIQQCPA AVEVLNLVAQ ECSAGERLAV VEMQCERLRM
     LYRDCARPPP PPLQADRRQP KEITWSPSRV FPPVRACMFS SHLTSVTFLA DPSAGGGLPR
     GTFIYATSPL PVQAPSFYWE IEIVSYGDTD DDTGPIVSFG FATEAEKRDG AWTNPVGTCL
     FHNNGRAVHY NGSSLLQWKS VRLDVTLSPG DVAGIGWERT EGTPPPPGQP AKGRVYFTYC
     GQRLTPYLED VSGGMWPVVH IQ
//
ID   RELL2_MOUSE             Reviewed;         303 AA.
AC   Q8BRJ3;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=RELT-like protein 2;
GN   Name=Rell2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBUNIT: Interacts with RELT, RELL1 and OXSR1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the RELT family.
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DR   EMBL; AK044097; BAC31774.1; -; mRNA.
DR   IPI; IPI00224269; -.
DR   RefSeq; NP_722488.2; NM_153793.2.
DR   UniGene; Mm.233516; -.
DR   UniGene; Mm.285060; -.
DR   ProteinModelPortal; Q8BRJ3; -.
DR   PRIDE; Q8BRJ3; -.
DR   Ensembl; ENSMUST00000070709; ENSMUSP00000070280; ENSMUSG00000044024.
DR   GeneID; 225392; -.
DR   KEGG; mmu:225392; -.
DR   UCSC; uc008ern.1; mouse.
DR   CTD; 225392; -.
DR   MGI; MGI:1918044; Rell2.
DR   GeneTree; ENSGT00530000063385; -.
DR   HOGENOM; HBG125709; -.
DR   HOVERGEN; HBG055726; -.
DR   InParanoid; Q8BRJ3; -.
DR   OMA; HGLYMLF; -.
DR   OrthoDB; EOG4DNF52; -.
DR   PhylomeDB; Q8BRJ3; -.
DR   ArrayExpress; Q8BRJ3; -.
DR   Bgee; Q8BRJ3; -.
DR   CleanEx; MM_RELL2; -.
DR   Genevestigator; Q8BRJ3; -.
DR   GermOnline; ENSMUSG00000044024; Mus musculus.
DR   GO; GO:0005604; C:basement membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005518; F:collagen binding; IDA:MGI.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IDA:MGI.
DR   InterPro; IPR022248; TNF_rcpt_RELT.
DR   Pfam; PF12606; RELT; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    303       RELT-like protein 2.
FT                                /FTId=PRO_0000249846.
FT   TRANSMEM     15     35       Helical; (Potential).
SQ   SEQUENCE   303 AA;  32326 MW;  06287A05AA64793B CRC64;
     MSEPQPDLEP PQHGLYMLFL LVLVFFLMGL VGFMICHVLK KKGYRCRTSR GSEPDDAQLQ
     PPEDDDVNED TVERIVRCII QNEANAEALK EMLGDSEGEG TVQLSSVDAT SSLQDGAPSH
     HHTVHLGSAA PCIHCSRSKR PPLVRQGRSK EGKSRPRPGE TTVFSVGRFR VTHIEKRYGL
     HEHRDGSPTD RSWGSGGGQE PGGSQAAGGG QPRTGTAAIE RLLPEPPPSQ AAATHSVQNG
     RLQDASLVPC TLEGTPGTSA ELNLGPRGRD PSPGLSSQEA NGQPTKLDTS GQQESLPPEA
     GGM
//
ID   PPR3E_MOUSE             Reviewed;         279 AA.
AC   Q8BRJ4;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   08-MAR-2011, entry version 38.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 3E;
GN   Name=Ppp1r3e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], MOTIF, AND FUNCTION.
RX   PubMed=15752363; DOI=10.1111/j.1742-4658.2005.04585.x;
RA   Munro S., Ceulemans H., Bollen M., Diplexcito J., Cohen P.T.W.;
RT   "A novel glycogen-targeting subunit of protein phosphatase 1 that is
RT   regulated by insulin and shows differential tissue distribution in
RT   humans and rodents.";
RL   FEBS J. 272:1478-1489(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 199-279.
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Acts as a glycogen-targeting subunit for PP1. PP1 is
CC       involved in glycogen metabolism and contributes to the activation
CC       of glycogen synthase leading to an increase in glycogen synthesis.
CC   -!- DOMAIN: The CBM21 domain is known to be involved in the
CC       localization to glycogen and is characteristic of some regulatory
CC       subunit of phosphatase complexes.
CC   -!- SIMILARITY: Contains 1 CBM21 (carbohydrate binding type-21)
CC       domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC31772.1; Type=Erroneous translation; Note=Wrong choice of frame;
CC   -----------------------------------------------------------------------
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DR   EMBL; AC116591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK044095; BAC31772.1; ALT_SEQ; mRNA.
DR   IPI; IPI00404450; -.
DR   UniGene; Mm.297365; -.
DR   UniGene; Mm.420485; -.
DR   ProteinModelPortal; Q8BRJ4; -.
DR   SMR; Q8BRJ4; 141-273.
DR   PhosphoSite; Q8BRJ4; -.
DR   PRIDE; Q8BRJ4; -.
DR   MGI; MGI:2145790; Ppp1r3e.
DR   HOVERGEN; HBG108282; -.
DR   Genevestigator; Q8BRJ4; -.
DR   GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005036; CBM_21.
DR   Pfam; PF03370; CBM_21; 1.
DR   PROSITE; PS51159; CBM21; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Glycogen metabolism.
FT   CHAIN         1    279       Protein phosphatase 1 regulatory subunit
FT                                3E.
FT                                /FTId=PRO_0000338639.
FT   DOMAIN      154    259       CBM21.
FT   REGION      176    198       Glycogen-binding motif (By similarity).
FT   REGION      248    256       Substrate-binding motif (By similarity).
FT   MOTIF        87     90       PP1-binding motif.
FT   CONFLICT      3      3       P -> H (in Ref. 2; AC116591).
SQ   SEQUENCE   279 AA;  30575 MW;  47954E88D6EB2CC0 CRC64;
     MSPERPPRTD IPRNLSFIAA LTERAYYRSQ RPSLEEESEE EPGEGGTRPG ARSRAHVPGR
     GRRARSAPAG GGGARTARSR SPDTRKRVRF ADALGLELAV VRRFRPGEPP RVPRHVQVQL
     QRDALRHFAP CPPRARGLQE ARVALEPALE PGFAARLQAQ RICLERADAG PLGVAGSARV
     LDLAYEKRVS VRWSADGWRS LRESPASYAG PAPSPPRADR FAFRLPAPPV GGTLLFALRY
     RVTGREFWDN NGGRDYALLG PEHPAGAGAA EPQGWIHFI
//
ID   Q8BRJ6_MOUSE            Unreviewed;       535 AA.
AC   Q8BRJ6;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 52.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Cpne9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 2 C2 domains.
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DR   EMBL; AK044080; BAC31765.1; -; mRNA.
DR   IPI; IPI00313899; -.
DR   UniGene; Mm.65597; -.
DR   HSSP; P21707; 1RSY.
DR   ProteinModelPortal; Q8BRJ6; -.
DR   SMR; Q8BRJ6; 4-258.
DR   PhosphoSite; Q8BRJ6; -.
DR   PRIDE; Q8BRJ6; -.
DR   Ensembl; ENSMUST00000041203; ENSMUSP00000044416; ENSMUSG00000030270.
DR   MGI; MGI:2443052; Cpne9.
DR   GeneTree; ENSGT00550000074189; -.
DR   HOVERGEN; HBG066841; -.
DR   InParanoid; Q8BRJ6; -.
DR   ArrayExpress; Q8BRJ6; -.
DR   Bgee; Q8BRJ6; -.
DR   Genevestigator; Q8BRJ6; -.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR010734; Copine.
DR   InterPro; IPR002035; VWF_A.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF07002; Copine; 1.
DR   SMART; SM00239; C2; 2.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS50234; VWFA; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   535 AA;  60054 MW;  C9F85FD1B4F2EE8C CRC64;
     MLFSRNLLDL DTFSKSDPMV VLHTQSRASQ EWREFGRTEV IDNTLNPDFV RKFVLDYFFE
     EKQNLRFDVY NVDSKANISK PKDFLGQAFL ALGEVIGGQG SRVERPLTGV PGKKCGTILL
     TAEELSNCRD IATMQLCANK LDKKDFFGKS DPFLVFYRSN EDGTFTICHK TEVVKNTLNP
     VWQPFSIPVR ALCNGDYDRT VKIDVYDWDR DGSHDFIGEF TTSYRELSKA QNQFTVYEVL
     NPRKKCKKKK YTNSGTVTLL SFSVDSEFTF VDYIKGGTQL NFTVAIDFTA SNGNPLQPTS
     LHYMSPYQLS AYAMALKAVG EIIQDYDSDK LFPAYGFGAK LPPEGRISHQ FPLNNNDEDP
     NCAGIEGVLE SYFQSLRTVQ LYGPTYFAPV INQVARAAAK ISDGSQYYVL LIITDGVISD
     MTQTKEAIVS ASSLPMSIII VGVGPAMFEA MEELDGDDVR VSSRGRYAER DIVQFVPFRD
     YVDRSGNQVL SMARLAKDVL AEIPEQLLSY MRTRDIQPRP PPPASPNPTP APEQP
//
ID   AAPK2_MOUSE             Reviewed;         552 AA.
AC   Q8BRK8; Q3UYM4;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=5'-AMP-activated protein kinase catalytic subunit alpha-2;
DE            Short=AMPK subunit alpha-2;
DE            EC=2.7.11.1;
GN   Name=Prkaa2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-552.
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15331533;
RA   Villena J.A., Viollet B., Andreelli F., Kahn A., Vaulont S., Sul H.S.;
RT   "Induced adiposity and adipocyte hypertrophy in mice lacking the AMP-
RT   activated protein kinase-alpha2 subunit.";
RL   Diabetes 53:2242-2249(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-500, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Responsible for the regulation of fatty acid synthesis
CC       by phosphorylation of acetyl-CoA carboxylase. It also regulates
CC       cholesterol synthesis via phosphorylation and inactivation of
CC       hormone-sensitive lipase and hydroxymethylglutaryl-CoA reductase.
CC       Appears to act as a metabolic stress-sensing protein kinase
CC       switching off biosynthetic pathways when cellular ATP levels are
CC       depleted and when 5'-AMP rises in response to fuel limitation
CC       and/or hypoxia. This is a catalytic subunit.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Binding of AMP results in allosteric
CC       activation, inducing phosphorylation on Thr-172 by STK11 in
CC       complex with STE20-related adapter-alpha (STRAD alpha) pseudo
CC       kinase and CAB39. Also activated by phosphorylation by CAMKK2
CC       triggered by a rise in intracellular calcium ions, without
CC       detectable changes in the AMP/ATP ratio (By similarity).
CC   -!- SUBUNIT: Heterotrimer of a catalytic subunit, a beta and a gamma
CC       non-catalytic subunits (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice develop obesity when animals are fed a
CC       high-fat diet, as a result of an enhanced lipid accumulation in
CC       pre-existing adipocytes but not in other tissues.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. SNF1 subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL627307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK044030; BAC31746.1; -; mRNA.
DR   EMBL; AK134573; BAE22188.1; -; mRNA.
DR   IPI; IPI00123445; -.
DR   UniGene; Mm.48638; -.
DR   HSSP; P06782; 2EUE.
DR   ProteinModelPortal; Q8BRK8; -.
DR   SMR; Q8BRK8; 10-335, 353-552.
DR   STRING; Q8BRK8; -.
DR   PhosphoSite; Q8BRK8; -.
DR   PRIDE; Q8BRK8; -.
DR   Ensembl; ENSMUST00000030243; ENSMUSP00000030243; ENSMUSG00000028518.
DR   UCSC; uc008tyd.1; mouse.
DR   MGI; MGI:1336173; Prkaa2.
DR   eggNOG; roNOG12508; -.
DR   GeneTree; ENSGT00600000084026; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG050432; -.
DR   InParanoid; Q8BRK8; -.
DR   OrthoDB; EOG4XSKPM; -.
DR   PhylomeDB; Q8BRK8; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 360016; -.
DR   ArrayExpress; Q8BRK8; -.
DR   Bgee; Q8BRK8; -.
DR   Genevestigator; Q8BRK8; -.
DR   GermOnline; ENSMUSG00000028518; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0004679; F:AMP-activated protein kinase activity; TAS:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006950; P:response to stress; TAS:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cholesterol biosynthesis;
KW   Fatty acid biosynthesis; Kinase; Lipid synthesis; Magnesium;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Steroid biosynthesis;
KW   Sterol biosynthesis; Transferase.
FT   CHAIN         1    552       5'-AMP-activated protein kinase catalytic
FT                                subunit alpha-2.
FT                                /FTId=PRO_0000262957.
FT   DOMAIN       16    268       Protein kinase.
FT   NP_BIND      22     30       ATP (By similarity).
FT   ACT_SITE    139    139       Proton acceptor (By similarity).
FT   BINDING      45     45       ATP (By similarity).
FT   MOD_RES      69     69       N6-acetyllysine (By similarity).
FT   MOD_RES     172    172       Phosphothreonine; by STK11 (By
FT                                similarity).
FT   MOD_RES     173    173       Phosphoserine.
FT   MOD_RES     176    176       Phosphoserine (By similarity).
FT   MOD_RES     377    377       Phosphoserine (By similarity).
FT   MOD_RES     500    500       Phosphoserine.
FT   CONFLICT     15     15       H -> D (in Ref. 2; BAE22188).
FT   CONFLICT    289    289       V -> D (in Ref. 2; BAE22188).
FT   CONFLICT    380    380       A -> E (in Ref. 2; BAE22188).
FT   CONFLICT    502    502       F -> Y (in Ref. 2; BAE22188).
FT   CONFLICT    506    506       T -> K (in Ref. 2; BAE22188).
SQ   SEQUENCE   552 AA;  62006 MW;  593911EAB3BBFE3F CRC64;
     MAEKQKHDGR VKIGHYVLGD TLGVGTFGKV KIGEHQLTGH KVAVKILNRQ KIRSLDVVGK
     IKREIQNLKL FRHPHIIKLY QVISTPTDFF MVMEYVSGGE LFDYICKHGR VEEVEARRLF
     QQILSAVDYC HRHMVVHRDL KPENVLLDAQ MNAKIADFGL SNMMSDGEFL RTSCGSPNYA
     APEVISGRLY AGPEVDIWSC GVILYALLCG TLPFDDEHVP TLFKKIRGGV FYIPDYLNRS
     VATLLMHMLQ VDPLKRATIK DIREHEWFKQ DLPSYLFPED PSYDANVIVD EAVKEVCEKF
     ECTESEVMNS LYSGDPQDQL AVAYHLIIDN RRIMNQASEF YLASSPPSGS FMDDSAMHIP
     PGLKPHPERM PPLIADSPKA RCPLDALNTT KPKSLAVKKA KWHLGIRSQS KACDIMAEVY
     RAMKQLGFEW KVVNAYHLRV RRKNPVTGNY VKMSLQLYLV DSRSYLLDFK SIDDEVVEQR
     SGSSTPQRSC SAAGLHRARS SFDSSTAENH SLSGSLTGSL TGSTLSSASP RLGSHTMDFF
     EMCASLITAL AR
//
ID   C2D1B_MOUSE             Reviewed;         848 AA.
AC   Q8BRN9; B2RQ40; Q3UJ60; Q69Z95;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Coiled-coil and C2 domain-containing protein 1B;
GN   Name=Cc2d1b; Synonyms=Kiaa1836;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 147-848.
RC   TISSUE=Spleen;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SIMILARITY: Belongs to the CC2D1 family.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK043839; BAC31675.1; -; mRNA.
DR   EMBL; AK146601; BAE27295.1; -; mRNA.
DR   EMBL; AL626783; CAM23502.1; -; Genomic_DNA.
DR   EMBL; BC125517; AAI25518.1; -; mRNA.
DR   EMBL; BC137743; AAI37744.1; -; mRNA.
DR   EMBL; AK173271; BAD32549.1; -; mRNA.
DR   IPI; IPI00649691; -.
DR   RefSeq; NP_796019.1; NM_177045.3.
DR   UniGene; Mm.151129; -.
DR   ProteinModelPortal; Q8BRN9; -.
DR   SMR; Q8BRN9; 681-816.
DR   PhosphoSite; Q8BRN9; -.
DR   PRIDE; Q8BRN9; -.
DR   Ensembl; ENSMUST00000030320; ENSMUSP00000030320; ENSMUSG00000028582.
DR   GeneID; 319965; -.
DR   KEGG; mmu:319965; -.
DR   UCSC; uc008ubl.1; mouse.
DR   CTD; 319965; -.
DR   MGI; MGI:2443076; Cc2d1b.
DR   GeneTree; ENSGT00390000009595; -.
DR   HOGENOM; HBG713884; -.
DR   HOVERGEN; HBG100866; -.
DR   InParanoid; Q8BRN9; -.
DR   OMA; ELMRIGK; -.
DR   OrthoDB; EOG41JZBS; -.
DR   PhylomeDB; Q8BRN9; -.
DR   NextBio; 395747; -.
DR   ArrayExpress; Q8BRN9; -.
DR   Bgee; Q8BRN9; -.
DR   CleanEx; MM_CC2D1B; -.
DR   Genevestigator; Q8BRN9; -.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR006608; DM14.
DR   Pfam; PF00168; C2; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00685; DM14; 4.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   PROSITE; PS50004; C2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Coiled coil; Phosphoprotein.
FT   CHAIN         1    848       Coiled-coil and C2 domain-containing
FT                                protein 1B.
FT                                /FTId=PRO_0000288427.
FT   DOMAIN      676    789       C2.
FT   COILED      165    193       Potential.
FT   COILED      600    626       Potential.
FT   COMPBIAS     90     96       Poly-Glu.
FT   MOD_RES     455    455       Phosphoserine.
FT   CONFLICT     25     25       L -> F (in Ref. 1; BAE27295).
FT   CONFLICT    388    388       Q -> L (in Ref. 1; BAE27295).
SQ   SEQUENCE   848 AA;  93091 MW;  32F781AF50CA8297 CRC64;
     MPGPRPRKGP KTSGQGAETA KQLGLFVEFN PEDMLLGVDE TEDDGDLEAE LLALTGETAS
     RSRKPAPKGQ APLPMAHIEK LAADCMRDVE EDEEEEGLED DADLLTELQE VLGEDEEAGL
     LDGSEAASPD LCEEKTWDNT ELPVEQAACQ QAVPAAAQAG GPRGLQALLE ERIRNYREAA
     ASAKEAGEAA KARRCERGLK TLQSQLATVR KGGKICEDEI PPPVALGKRP PAPQERAIKN
     PEIDSPGPCA MEPGNLSQPE SSLPAIAPLP DSDPDPQALL LARQREYKAA ALDAKRAGDL
     DRARELMRIG KRFGTVLEAL EKGQPVDLSG MPPAPADLKA LPQASKASSA TQGLSPAVEQ
     MQPVMASDLP ATPVAPAEPT TVLDALQQRL NKYREAGIQA RANGDERKAR MHDRIAKQYQ
     DAVRAHQAGQ KVDFAELPVP PGFPPIPGLE PRKGSEQDSV AATLATAQKL ASEDAALVDD
     DEESDTPAQA PLAKKPAQTL VSPSHLLTEP KASSSKESLS PSVREQVTLL EARKLQYQRA
     ALQAKRRQDL EQAKSHLRVA KSLEAQIIQA RAGQPIDLSK VPSPLTDEEG DFILIHHEDL
     RLSQKAEEVY AQLQKMLQEQ QAKCLLFSKQ YMHQGNVAET TRFERLAEDR KKQLEILQLA
     QAQGLDPPSH HFELKTFQTV RIFSELNSTE MHLIIVRGMN LPAPPGVTPD DLDAFVRFEF
     HYPNSDQAQK SKTAVVKNTN SPEFEQVFKL NINRNHRGFR RVIQSKGIKF EIFHKGSFFR
     SDKLVGTAHL KLERLEKECE IREIMEVLDG RKPTGGKLEV KVRLREPLSS QDVQTVTENW
     LVLEPRGL
//
ID   Q8BRR9_MOUSE            Unreviewed;       545 AA.
AC   Q8BRR9;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   SubName: Full=Phosphodiesterase 1A, calmodulin-dependent;
DE   SubName: Full=Phosphodiesterase 1A, calmodulin-dependent, isoform CRA_a;
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Pde1a; ORFNames=RP23-326J18.1-002, mCG_141901;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cortex;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RA   Sycamore N.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RA   Almeida-King J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [12]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [13]
RP   NUCLEOTIDE SEQUENCE.
RA   Lawlor S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [14]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC090628; AAH90628.1; -; mRNA.
DR   EMBL; AK043647; BAC31606.1; -; mRNA.
DR   EMBL; AL844577; CAM14508.1; -; Genomic_DNA.
DR   EMBL; AL928607; CAM14508.1; JOINED; Genomic_DNA.
DR   EMBL; AL928811; CAM14508.1; JOINED; Genomic_DNA.
DR   EMBL; AL928607; CAM20942.1; -; Genomic_DNA.
DR   EMBL; AL844577; CAM20942.1; JOINED; Genomic_DNA.
DR   EMBL; AL928811; CAM20942.1; JOINED; Genomic_DNA.
DR   EMBL; AL928811; CAM26821.1; -; Genomic_DNA.
DR   EMBL; AL844577; CAM26821.1; JOINED; Genomic_DNA.
DR   EMBL; AL928607; CAM26821.1; JOINED; Genomic_DNA.
DR   EMBL; CH466519; EDL27255.1; -; Genomic_DNA.
DR   EMBL; CH466519; EDL27257.1; -; Genomic_DNA.
DR   IPI; IPI00874497; -.
DR   RefSeq; NP_001153054.1; NM_001159582.1.
DR   RefSeq; NP_058024.2; NM_016744.4.
DR   UniGene; Mm.40678; -.
DR   HSSP; Q08499; 1OYN.
DR   ProteinModelPortal; Q8BRR9; -.
DR   SMR; Q8BRR9; 142-520.
DR   STRING; Q8BRR9; -.
DR   PRIDE; Q8BRR9; -.
DR   Ensembl; ENSMUST00000102653; ENSMUSP00000099713; ENSMUSG00000059173.
DR   Ensembl; ENSMUST00000102655; ENSMUSP00000099715; ENSMUSG00000059173.
DR   GeneID; 18573; -.
DR   KEGG; mmu:18573; -.
DR   UCSC; uc008khc.1; mouse.
DR   CTD; 18573; -.
DR   MGI; MGI:1201792; Pde1a.
DR   GeneTree; ENSGT00550000074309; -.
DR   HOVERGEN; HBG056120; -.
DR   InParanoid; Q8BRR9; -.
DR   OMA; IIIPLIE; -.
DR   NextBio; 294416; -.
DR   ArrayExpress; Q8BRR9; -.
DR   Bgee; Q8BRR9; -.
DR   Genevestigator; Q8BRR9; -.
DR   GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR003607; Metal-dep_PHydrolase_HD_dom.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR023174; PDEase_CS.
DR   InterPro; IPR013706; PDEase_N.
DR   Gene3D; G3DSA:1.10.1300.10; PDEase_catalytic_dom; 2.
DR   Pfam; PF00233; PDEase_I; 1.
DR   Pfam; PF08499; PDEase_I_N; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00471; HDc; 1.
DR   PROSITE; PS00126; PDEASE_I; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding.
SQ   SEQUENCE   545 AA;  62347 MW;  5B794C8DE8456917 CRC64;
     MGSTDTDIEE LENATYKYLI GEQTEKMWQR LKGILRCLVK QLEKGDVNVV DLKKNIEYAA
     SVLEAVYIDE TRRLLDTEDE LSDIQTDSVP SEVRDWLAST FTRKMGMMKK KPEEKPKFRS
     IVHAVQAGIF VERMYRKNYH MVGLTYPAAV IVTLKEVDKW SFDVFALNEA SGEHSLKFMI
     YELFTRYDLI NRFKIPVSCL IAFAEALEVG YSKHKNPYHN LVHAADVTQT VHYIMLHTGI
     MHWLTELEIL AMVFAAAIHD YEHTGTTNNF HIQTRSDVAI LYNDRSVLEN HHVSAAYRLM
     QEEEMNILVN LSKDDWRDLR NLVIEMVLAT DMSGHFQQIK NIRNSLQQPE GIDRAKTMSL
     ILHAADISHP AKTWKLHYRW TMALMEEFFL QGDKEAELGL PFSPLCDRKS TMVAQSQIGF
     IDFIVEPTFS LLTDSTEKIV IPLIEEASKS QSSNYGASSS STMIGFHVAD SLRRSNTKGS
     VCDGSYAPDY SLSAVDLKSF KNNLVDIIQQ NKERWKELAA QGELDLHKNS EELGNTEEKH
     ADTRP
//
ID   K1671_MOUSE             Reviewed;         308 AA.
AC   Q8BRV5; B2RVT5; Q5DTV9;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Uncharacterized protein KIAA1671;
GN   Name=Kiaa1671;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Aorta, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 118-308.
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK041243; BAC30876.1; -; mRNA.
DR   EMBL; AK154484; BAE32619.1; -; mRNA.
DR   EMBL; AK171617; BAE42566.1; -; mRNA.
DR   EMBL; BC147338; AAI47339.1; -; mRNA.
DR   EMBL; BC147339; AAI47340.1; -; mRNA.
DR   EMBL; AK220411; BAD90261.1; -; mRNA.
DR   IPI; IPI00224491; -.
DR   RefSeq; NP_766472.1; NM_172884.3.
DR   UniGene; Mm.160131; -.
DR   PhosphoSite; Q8BRV5; -.
DR   PRIDE; Q8BRV5; -.
DR   Ensembl; ENSMUST00000050125; ENSMUSP00000058789; ENSMUSG00000051339.
DR   GeneID; 243219; -.
DR   KEGG; mmu:243219; -.
DR   UCSC; uc008yua.1; mouse.
DR   MGI; MGI:1920194; 2900026A02Rik.
DR   eggNOG; roNOG17809; -.
DR   GeneTree; ENSGT00530000064083; -.
DR   HOGENOM; HBG446999; -.
DR   HOVERGEN; HBG100622; -.
DR   InParanoid; Q8BRV5; -.
DR   OMA; MDPSALK; -.
DR   OrthoDB; EOG4HMJ8D; -.
DR   NextBio; 385675; -.
DR   ArrayExpress; Q8BRV5; -.
DR   Bgee; Q8BRV5; -.
DR   CleanEx; MM_2900026A02RIK; -.
DR   Genevestigator; Q8BRV5; -.
PE   2: Evidence at transcript level;
KW   Phosphoprotein.
FT   CHAIN         1    308       Uncharacterized protein KIAA1671.
FT                                /FTId=PRO_0000287146.
FT   MOD_RES      83     83       Phosphoserine (By similarity).
FT   MOD_RES     205    205       Phosphoserine (By similarity).
FT   MOD_RES     259    259       Phosphoserine (By similarity).
FT   MOD_RES     262    262       Phosphoserine (By similarity).
FT   MOD_RES     288    288       Phosphoserine (By similarity).
SQ   SEQUENCE   308 AA;  34668 MW;  0E1DEEDC376C4135 CRC64;
     MDYYYCPSLL KLLRYLWNQL KQCFSRRAPE AKDTDTLVQE ADSQYGTWAD QHQNGGSFGP
     ESPSPDSSAA SVGKQPPGSH LSSYTESTSV EQRDSSRDRR SSSVDRSSSE LESTDGPEGP
     PPSDVCPAQE DDFSFIHQTS VLDSSALKTR VQLSKRSRRR APISHSLRRS QFSESESRSP
     LEEESHSTWM FKDSTEEKSP RRDESDEEPP RVERTPVSHP QRMPVFPGMD PAVLKAQLPK
     RSEVDSPGDS LSWTPQPKSP KSPFHPGVLG SRVLPPSTEK EERSEECSPQ WLKELKSKKR
     QSLYENQA
//
ID   TYW3_MOUSE              Reviewed;         257 AA.
AC   Q8BSA9; Q8BSX2;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=tRNA wybutosine-synthesizing protein 3 homolog;
DE            EC=2.1.1.-;
DE   AltName: Full=tRNA-yW-synthesizing protein 3;
GN   Name=Tyw3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, Eye, and Xiphoid cartilage;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Probable S-adenosyl-L-methionine-dependent
CC       methyltransferase that acts as a component of the wybutosine
CC       biosynthesis pathway. Wybutosine is a hyper modified guanosine
CC       with a tricyclic base found at the 3'-position adjacent to the
CC       anticodon of eukaryotic phenylalanine tRNA (By similarity).
CC   -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC   -!- SIMILARITY: Belongs to the TYW3 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC26913.1; Type=Erroneous initiation;
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DR   EMBL; AK030344; BAC26913.1; ALT_INIT; mRNA.
DR   EMBL; AK034820; BAC28842.1; -; mRNA.
DR   EMBL; BC086686; AAH86686.1; -; mRNA.
DR   EMBL; BC087879; AAH87879.1; -; mRNA.
DR   IPI; IPI00224872; -.
DR   RefSeq; NP_766062.1; NM_172474.5.
DR   UniGene; Mm.347513; -.
DR   ProteinModelPortal; Q8BSA9; -.
DR   SMR; Q8BSA9; 1-195.
DR   STRING; Q8BSA9; -.
DR   PhosphoSite; Q8BSA9; -.
DR   PRIDE; Q8BSA9; -.
DR   Ensembl; ENSMUST00000052774; ENSMUSP00000057828; ENSMUSG00000047583.
DR   GeneID; 209584; -.
DR   KEGG; mmu:209584; -.
DR   NMPDR; fig|10090.3.peg.9181; -.
DR   UCSC; uc008ruo.1; mouse.
DR   CTD; 209584; -.
DR   MGI; MGI:2445040; Tyw3.
DR   eggNOG; roNOG14860; -.
DR   GeneTree; ENSGT00390000018149; -.
DR   HOGENOM; HBG717229; -.
DR   HOVERGEN; HBG106708; -.
DR   InParanoid; Q8BSA9; -.
DR   OMA; AEFGRWK; -.
DR   OrthoDB; EOG4F4SC6; -.
DR   PhylomeDB; Q8BSA9; -.
DR   NextBio; 372726; -.
DR   ArrayExpress; Q8BSA9; -.
DR   Bgee; Q8BSA9; -.
DR   Genevestigator; Q8BSA9; -.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR003827; tRNA_yW-synthesising.
DR   Pfam; PF02676; TYW3; 1.
DR   SUPFAM; SSF111278; DUF207; 1.
PE   1: Evidence at protein level;
KW   Methyltransferase; Phosphoprotein; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN         1    257       tRNA wybutosine-synthesizing protein 3
FT                                homolog.
FT                                /FTId=PRO_0000281843.
FT   MOD_RES      25     25       Phosphoserine.
SQ   SEQUENCE   257 AA;  28575 MW;  03A9EEC6296F19D3 CRC64;
     MDRSAEFGRW KAQSLSKADL SRKGSVDEDA VEVVELLNSR EEFFTTSSCA GRILLLDGST
     EGSGVQKQHC CWLLVTHKPC ARDDVMAALK GATSEAVLKF EPFILHVQCR TLQDAQTLHS
     VAIDSGFRNS GITVGKRGKT MLAVRGTHGL EVPLTHKGKL MVTEEYIEFL LTIANQKMEE
     NKRRIGRFYN YLQHALKRET ISNSHSKIKE RNNPLCTHKN RRSQGKAQGP STTEDNGREL
     EDGDGLEISA ALFLGDD
//
ID   RMD2_MOUSE              Reviewed;         410 AA.
AC   Q8BSE0; A9UN02; Q8CIF1;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Regulator of microtubule dynamics protein 2;
DE            Short=RMD-2;
DE            Short=mRMD-2;
DE   AltName: Full=Protein FAM82A1;
GN   Name=Fam82a1; Synonyms=Fam82a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION.
RX   PubMed=18070910; DOI=10.1083/jcb.200705108;
RA   Oishi K., Okano H., Sawa H.;
RT   "RMD-1, a novel microtubule-associated protein, functions in
RT   chromosome segregation in Caenorhabditis elegans.";
RL   J. Cell Biol. 179:1149-1162(2007).
CC   -!- SUBUNIT: Interacts with microtubules (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential). Cytoplasm. Cytoplasm, cytoskeleton, spindle (By
CC       similarity). Cytoplasm, cytoskeleton, spindle pole (By
CC       similarity). Note=In interphase localizes in the cytoplasm, and
CC       during mitosis localizes to the spindle microtubules and spindle
CC       poles. Also detected as large dots in the perinuclear region (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the FAM82/RMD family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH24059.1; Type=Erroneous initiation;
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DR   EMBL; AK034617; BAC28771.1; -; mRNA.
DR   EMBL; AK139382; BAE23985.1; -; mRNA.
DR   EMBL; BC024059; AAH24059.1; ALT_INIT; mRNA.
DR   EMBL; BR000694; FAA00419.1; -; mRNA.
DR   IPI; IPI00399725; -.
DR   RefSeq; NP_958749.1; NM_201361.2.
DR   UniGene; Mm.293063; -.
DR   UniGene; Mm.449995; -.
DR   ProteinModelPortal; Q8BSE0; -.
DR   SMR; Q8BSE0; 211-263, 337-390.
DR   PhosphoSite; Q8BSE0; -.
DR   PRIDE; Q8BSE0; -.
DR   Ensembl; ENSMUST00000040368; ENSMUSP00000044543; ENSMUSG00000036368.
DR   Ensembl; ENSMUST00000112443; ENSMUSP00000108062; ENSMUSG00000036368.
DR   GeneID; 381110; -.
DR   KEGG; mmu:381110; -.
DR   NMPDR; fig|10090.3.peg.3415; -.
DR   UCSC; uc008dpy.1; mouse.
DR   CTD; 381110; -.
DR   MGI; MGI:2147043; Fam82a1.
DR   eggNOG; roNOG14844; -.
DR   GeneTree; ENSGT00530000063162; -.
DR   HOGENOM; HBG755399; -.
DR   HOVERGEN; HBG072518; -.
DR   InParanoid; Q8BSE0; -.
DR   OMA; GYITANT; -.
DR   OrthoDB; EOG408N8M; -.
DR   PhylomeDB; Q8BSE0; -.
DR   NextBio; 401612; -.
DR   ArrayExpress; Q8BSE0; -.
DR   Bgee; Q8BSE0; -.
DR   CleanEx; MM_AW061290; -.
DR   Genevestigator; Q8BSE0; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR011990; TPR-like_helical.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Membrane; Microtubule;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    410       Regulator of microtubule dynamics protein
FT                                2.
FT                                /FTId=PRO_0000287506.
FT   TRANSMEM      9     28       Helical; (Potential).
FT   COILED       69    110       Potential.
FT   CONFLICT     40     40       P -> S (in Ref. 2; AAH24059).
FT   CONFLICT    289    289       Missing (in Ref. 2; AAH24059).
SQ   SEQUENCE   410 AA;  47016 MW;  170C39E02C052B08 CRC64;
     MPHSTNKELI LGIMAGTAGI SLLAFWYHKV LKPRTTMNFP KLLSLGKKFG SLTLPEESHS
     AQGASVVFQR RQLQILEKLN ELLTNMEELK EEIRFLKETI PKLEECIQDE FGGKVTVHKI
     SPQHRARKKK GTTVQRSATS NSSEEAESEG GYITANTDTE EQNFPFPKAL NTHIEELKLD
     VLLQKADHLR TNESHKMESF ELLCDHKEKF SEETEFLWRL ARAYGDMYDL STSTQEKKHY
     ANIGKTLGER AITRAPMNGH CHLWYAVLCG YVSEFEGLQN KINCGHLFKK HLEIAIQLLP
     EEPLLYYLKG RYCYTVSRLS WIEKKMAATL FGEIPYSTVH EALHNFLKTE ELQPGYSMSN
     YMYTAKCYVE LGEPQEACKF CNLALLLPVV TKEDKDAHKE VKKMISSLKR
//
ID   Q8BSE7_MOUSE            Unreviewed;       400 AA.
AC   Q8BSE7;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 56.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Clasp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryonic body between diaphragm region and neck;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryonic body between diaphragm region and neck;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryonic body between diaphragm region and neck;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryonic body between diaphragm region and neck;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryonic body between diaphragm region and neck;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryonic body between diaphragm region and neck;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryonic body between diaphragm region and neck;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryonic body between diaphragm region and neck;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
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DR   EMBL; AK034560; BAC28754.1; -; mRNA.
DR   IPI; IPI00119157; -.
DR   UniGene; Mm.222272; -.
DR   ProteinModelPortal; Q8BSE7; -.
DR   STRING; Q8BSE7; -.
DR   PRIDE; Q8BSE7; -.
DR   Ensembl; ENSMUST00000035088; ENSMUSP00000035088; ENSMUSG00000033392.
DR   UCSC; uc009rwq.1; mouse.
DR   MGI; MGI:1923749; Clasp2.
DR   GeneTree; ENSGT00390000001762; -.
DR   ArrayExpress; Q8BSE7; -.
DR   Bgee; Q8BSE7; -.
DR   Genevestigator; Q8BSE7; -.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IDA:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR   GO; GO:0016477; P:cell migration; IMP:MGI.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:MGI.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:MGI.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000357; HEAT.
DR   InterPro; IPR021133; HEAT_type_2.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 2.
DR   Pfam; PF02985; HEAT; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
PE   1: Evidence at protein level;
SQ   SEQUENCE   400 AA;  44014 MW;  C89E859496681E26 CRC64;
     MEPRGAEYFC AQVLQKDVSG RLQAGEELLL CLGTPGAIPD LEDDPSRLAK TVDALTRWVG
     SSNYRVSLLG LEILSAFVDR LSTRFKSYVT MVTTALIDRM GDVKDKVREE AQNLTLKLMD
     EVAPPMYIWE QLASGFKHKN FRSREGVCLC LIETLNIFGT QPLVISKLVP HLCVLFGDSN
     SQVRNAALSA VVEIYRHVGE KLRIDLCKRD IPPARLEMVL AKFDEVQNSG GMILSVCKDK
     SFDDEESVDG NRPSSAASAF KVPAPKTPGN PVSSARKPGS AGGPKVGGPS KEGGAGAVDE
     DDFIKAFTDV PSVQIYSSRE LEETLNKIRE ILSDDKHDWD QRANACMSCS LVASEVERAL
     AWPLWSHLAT YQHHCHCTLS HEDLPEKRLT SPVSSAFVQH
//
ID   LAT3_MOUSE              Reviewed;         564 AA.
AC   Q8BSM7; A2ATS3; Q9D0H7;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Large neutral amino acids transporter small subunit 3;
DE   AltName: Full=L-type amino acid transporter 3;
DE   AltName: Full=Solute carrier family 43 member 1;
GN   Name=Slc43a1; Synonyms=Lat3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RA   Babu E., Kanai Y., Chairoungdua A., Li Y., Anzai N., Endou H.;
RT   "Identification and characterization of mouse LAT3 system L amino acid
RT   transporter.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Forelimb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-57, AND MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Sodium-independent, high affinity transport of large
CC       neutral amino acids. Has narrower substrate selectivity compared
CC       to SLC7A5 and SLC7A8 and mainly transports branched-chain amino
CC       acids and phenylalanine (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Probable).
CC   -!- SIMILARITY: Belongs to the SLC43A transporter (TC 2.A.1.44)
CC       family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC27305.1; Type=Frameshift; Positions=11;
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DR   EMBL; AB103034; BAD10947.1; -; mRNA.
DR   EMBL; AK011417; BAB27605.1; ALT_FRAME; mRNA.
DR   EMBL; AK031215; BAC27305.1; ALT_FRAME; mRNA.
DR   EMBL; AL928914; CAM23317.2; -; Genomic_DNA.
DR   EMBL; BC053747; AAH53747.1; -; mRNA.
DR   IPI; IPI00662681; -.
DR   RefSeq; NP_001077278.1; NM_001083809.1.
DR   RefSeq; NP_078773.1; NM_024497.1.
DR   UniGene; Mm.22716; -.
DR   ProteinModelPortal; Q8BSM7; -.
DR   SMR; Q8BSM7; 6-44.
DR   STRING; Q8BSM7; -.
DR   PhosphoSite; Q8BSM7; -.
DR   PRIDE; Q8BSM7; -.
DR   Ensembl; ENSMUST00000028469; ENSMUSP00000028469; ENSMUSG00000027075.
DR   Ensembl; ENSMUST00000111624; ENSMUSP00000107251; ENSMUSG00000027075.
DR   Ensembl; ENSMUST00000111625; ENSMUSP00000107252; ENSMUSG00000027075.
DR   Ensembl; ENSMUST00000121114; ENSMUSP00000112642; ENSMUSG00000027075.
DR   GeneID; 72401; -.
DR   KEGG; mmu:72401; -.
DR   UCSC; uc008kji.1; mouse.
DR   CTD; 72401; -.
DR   MGI; MGI:1931352; Slc43a1.
DR   GeneTree; ENSGT00530000063043; -.
DR   HOGENOM; HBG444314; -.
DR   HOVERGEN; HBG072879; -.
DR   InParanoid; Q8BSM7; -.
DR   OrthoDB; EOG42FSHN; -.
DR   PhylomeDB; Q8BSM7; -.
DR   NextBio; 336198; -.
DR   ArrayExpress; Q8BSM7; -.
DR   Bgee; Q8BSM7; -.
DR   CleanEx; MM_SLC43A1; -.
DR   Genevestigator; Q8BSM7; -.
DR   GermOnline; ENSMUSG00000027075; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; ISS:UniProtKB.
DR   InterPro; IPR011701; MFS_1.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Glycoprotein; Membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    564       Large neutral amino acids transporter
FT                                small subunit 3.
FT                                /FTId=PRO_0000218641.
FT   TRANSMEM     20     40       Helical; (Potential).
FT   TRANSMEM     78     98       Helical; (Potential).
FT   TRANSMEM    105    124       Helical; (Potential).
FT   TRANSMEM    131    151       Helical; (Potential).
FT   TRANSMEM    165    185       Helical; (Potential).
FT   TRANSMEM    191    211       Helical; (Potential).
FT   TRANSMEM    303    323       Helical; (Potential).
FT   TRANSMEM    357    377       Helical; (Potential).
FT   TRANSMEM    424    444       Helical; (Potential).
FT   TRANSMEM    451    471       Helical; (Potential).
FT   TRANSMEM    490    510       Helical; (Potential).
FT   TRANSMEM    515    535       Helical; (Potential).
FT   MOD_RES     265    265       Phosphoserine.
FT   CARBOHYD     54     54       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     57     57       N-linked (GlcNAc...).
FT   CARBOHYD    396    396       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    558    558       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   564 AA;  62644 MW;  AEC14BF1F3438BB8 CRC64;
     MAPTLKQAYR RRWWMACTAV VENLFFSAVL LGWASLLIML KKEGFYSSLC PAENRTNTTQ
     DEQHQWTSCD QQEKMLNLGF TIGSFLLSAT TLPLGILMDR FGPRPLRLVG SACFAASCTL
     MALASRDTEV LSPLIFLALS LNGFAGICLT FTSLTLPNMF GNLRSTFMAL MIGSYASSAI
     TFPGIKLIYD AGVPFTVIMF TWSGLACLIF LNCALNWPAE AFPAPEEVDY TKKIKLIGLA
     LDHKVTGDRF YTHVTIVGQR LSQKSPSLEE GADAFISSPD IPGTSEETPE KSVPFRKSLC
     SPIFLWSLVT MGMTQLRVIF YMGAMNKILE FIVTGGKERE TNEQRQKVEE TVEFYSSIFG
     VMQLLCLLTC PLIGYIMDWR IKDCVDAPTE GTLNENASFG DARDGASTKF TRPRYRKVQK
     LTNAINAFTL TNILLVGFGI ACLIKNLHLQ LLAFVLHTIV RGFFHSACGG LYAAVFPSNH
     FGTLTGLQSL ISAVFALLQQ LLFMAMVGPL HGDPFWVNLG LLLLSFLGFL LPSYLYYYRS
     RLQREYATNL VDPQKVLNTS KVAT
//
ID   PB1_MOUSE               Reviewed;        1634 AA.
AC   Q8BSQ9; Q05C64; Q05CL6; Q7TMP1; Q7TNU2; Q9CV51;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 3.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Protein polybromo-1;
DE   AltName: Full=BRG1-associated factor 180;
DE            Short=BAF180;
GN   Name=Pbrm1; Synonyms=Baf180, Pb1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, Czech II, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-919 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 205-512 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PHF10, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=17640523; DOI=10.1016/j.neuron.2007.06.019;
RA   Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T.,
RA   Wu H., Aebersold R., Graef I.A., Crabtree G.R.;
RT   "An essential switch in subunit composition of a chromatin remodeling
RT   complex during neural development.";
RL   Neuron 55:201-215(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353 AND SER-355, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   STRUCTURE BY NMR OF 646-762.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the fifth bromodomain from mouse polybromo-1.";
RL   Submitted (OCT-2007) to the PDB data bank.
CC   -!- FUNCTION: Involved in transcriptional activation and repression of
CC       select genes by chromatin remodeling (alteration of DNA-nucleosome
CC       topology) (By similarity). Act as a negative regulator of cell
CC       proliferation (By similarity).
CC   -!- SUBUNIT: Component of the SWI/SNF-B (PBAF) chromatin-remodeling
CC       complex, which contains at least SMARCA4/BRG1,
CC       SMARCB1/SNF5/INI1/BAF47, ACTL6A/BAF53A or ACTL6B/BAF53B,
CC       SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps
CC       SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PB1/BAF180,
CC       ARID2/BAF200, ARID1A/BAF250A or ARID1B/BAF250B and actin (By
CC       similarity). Interacts with PHF10/BAF45A.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BSQ9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BSQ9-2; Sequence=VSP_035471;
CC   -!- DEVELOPMENTAL STAGE: Expressed ubiquitously throughout the
CC       developing spinal cord, brain and other embryonic tissues at
CC       E10.5-E16.5.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 2 BAH domains.
CC   -!- SIMILARITY: Contains 6 bromo domains.
CC   -!- SIMILARITY: Contains 1 HMG box DNA-binding domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH29037.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAH55456.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence;
CC       Sequence=AAH55708.1; Type=Erroneous initiation;
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DR   EMBL; BC023452; AAH23452.1; -; mRNA.
DR   EMBL; BC029037; AAH29037.1; ALT_TERM; mRNA.
DR   EMBL; BC055456; AAH55456.1; ALT_TERM; mRNA.
DR   EMBL; BC055708; AAH55708.1; ALT_INIT; mRNA.
DR   EMBL; BF451491; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; CN530699; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK009582; BAB26374.2; -; mRNA.
DR   EMBL; AK030781; BAC27136.2; -; mRNA.
DR   EMBL; AK030252; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK166588; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00856358; -.
DR   IPI; IPI00857632; -.
DR   UniGene; Mm.27913; -.
DR   PDB; 2YQD; NMR; -; A=650-762.
DR   PDBsum; 2YQD; -.
DR   ProteinModelPortal; Q8BSQ9; -.
DR   SMR; Q8BSQ9; 27-292, 388-494, 518-766, 773-914, 957-1102, 1157-1304, 1376-1434.
DR   DIP; DIP-48885N; -.
DR   STRING; Q8BSQ9; -.
DR   PhosphoSite; Q8BSQ9; -.
DR   Ensembl; ENSMUST00000112095; ENSMUSP00000107724; ENSMUSG00000042323.
DR   UCSC; uc007swl.1; mouse.
DR   MGI; MGI:1923998; Pbrm1.
DR   eggNOG; roNOG10051; -.
DR   GeneTree; ENSGT00390000003017; -.
DR   HOVERGEN; HBG079860; -.
DR   OrthoDB; EOG41NTK5; -.
DR   ArrayExpress; Q8BSQ9; -.
DR   Bgee; Q8BSQ9; -.
DR   Genevestigator; Q8BSQ9; -.
DR   GO; GO:0000776; C:kinetochore; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IC:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0001890; P:placenta development; IMP:MGI.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR001025; BAH_dom.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR000910; HMG_HMG1/HMG2.
DR   InterPro; IPR009071; HMG_superfamily.
DR   Gene3D; G3DSA:1.20.920.10; Bromodomain; 6.
DR   Gene3D; G3DSA:1.10.30.10; HMG-box; 1.
DR   Pfam; PF01426; BAH; 2.
DR   Pfam; PF00439; Bromodomain; 6.
DR   Pfam; PF00505; HMG_box; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00439; BAH; 2.
DR   SMART; SM00297; BROMO; 6.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47370; Bromodomain; 6.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   PROSITE; PS51038; BAH; 2.
DR   PROSITE; PS00633; BROMODOMAIN_1; 5.
DR   PROSITE; PS50014; BROMODOMAIN_2; 6.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Bromodomain; Chromatin regulator;
KW   DNA-binding; Nucleus; Phosphoprotein; Repeat; Transcription;
KW   Transcription regulation; Tumor suppressor.
FT   CHAIN         1   1634       Protein polybromo-1.
FT                                /FTId=PRO_0000351134.
FT   DOMAIN       64    134       Bromo 1.
FT   DOMAIN      200    270       Bromo 2.
FT   DOMAIN      400    470       Bromo 3.
FT   DOMAIN      538    608       Bromo 4.
FT   DOMAIN      676    746       Bromo 5.
FT   DOMAIN      792    862       Bromo 6.
FT   DOMAIN      956   1074       BAH 1.
FT   DOMAIN     1156   1272       BAH 2.
FT   DNA_BIND   1379   1447       HMG box.
FT   COMPBIAS    630    633       Poly-Asp.
FT   COMPBIAS   1468   1599       Pro-rich.
FT   MOD_RES      10     10       Phosphoserine (By similarity).
FT   MOD_RES      39     39       Phosphoserine (By similarity).
FT   MOD_RES      54     54       Phosphotyrosine (By similarity).
FT   MOD_RES     131    131       Phosphoserine (By similarity).
FT   MOD_RES     178    178       Phosphoserine (By similarity).
FT   MOD_RES     301    301       Phosphothreonine (By similarity).
FT   MOD_RES     314    314       Phosphoserine (By similarity).
FT   MOD_RES     319    319       Phosphoserine (By similarity).
FT   MOD_RES     353    353       Phosphoserine.
FT   MOD_RES     355    355       Phosphoserine.
FT   MOD_RES     371    371       Phosphoserine (By similarity).
FT   MOD_RES     375    375       Phosphoserine (By similarity).
FT   MOD_RES     498    498       Phosphoserine (By similarity).
FT   MOD_RES     636    636       Phosphoserine (By similarity).
FT   MOD_RES     948    948       Phosphoserine (By similarity).
FT   MOD_RES    1405   1405       Phosphoserine (By similarity).
FT   VAR_SEQ     300    332       RTASNLAAARLTGPSHNKSSLGEERNPTSKYYR -> S
FT                                (in isoform 2).
FT                                /FTId=VSP_035471.
FT   CONFLICT    417    417       Y -> K (in Ref. 1; AAH23452).
FT   CONFLICT    695    695       D -> E (in Ref. 2; BAC27136).
FT   HELIX       659    671
FT   STRAND      679    681
FT   HELIX       682    684
FT   TURN        690    692
FT   HELIX       694    699
FT   HELIX       706    714
FT   HELIX       721    738
FT   HELIX       744    759
SQ   SEQUENCE   1634 AA;  187218 MW;  35B5153F22ECD274 CRC64;
     MGSKRRRATS PSSSVSGDFD DGHHSVPTPG PSRKRRRLSN LPTVDPIAVC HELYNTIRDY
     KDEQGRLLCE LFIRAPKRRN QPDYYEVVSQ PIDLMKIQQK LKMEEYDDVN LLTADFQLLF
     NNAKAYYKPD SPEYKAACKL WDLYLRTRNE FVQKGEADDE DDDEDGQDNQ GTLADGSSPG
     YLKEILEQLL EAIVVATNPS GRLISELFQK LPSKVQYPDY YAIIKEPIDL KTIAQRIQNG
     SYKSIHAMAK DIDLLAKNAK TYNEPGSQVF KDANSIKKIF YMKKAEIEHH EMTKSSLRIR
     TASNLAAARL TGPSHNKSSL GEERNPTSKY YRNKRAVQGG RLSAITMALQ YGSESEEDAA
     LAAARYEEGE SEAESITSFM DVSNPFHQLY DTVRSCRNHQ GQLIAEPFFH LPSKKKYPDY
     YQQIKMPISL QQIRTKLKNQ EYETLDHLEC DLNLMFENAK RYNVPNSAIY KRVLKLQQVM
     QAKKKELARR DDIEDGDSMI SSATSDTGSA KRKSKKNIRK QRMKILFNVV LEAREPGSGR
     RLCDLFMVKP SKKDYPDYYK IILEPMDLKI IEHNIRNDKY AGEEGMMEDM KLMFRNARHY
     NEEGSQVYND AHILEKLLKD KRKELGPLPD DDDMASPKLK LSRKSGVSPK KSKYMTPMQQ
     KLNEVYEAVK NYTDKRGRRL SAIFLRLPSR SELPDYYLTI KKPMDMEKIR SHMMANKYQD
     IDSMVEDFVM MFNNACTYNE PESLIYKDAL VLHKVLLETR RDLEGDEDSH VPNVTLLIQE
     LIHNLFVSVM SHQDDEGRCY SDSLAEIPAV DPNSPNKPPL TFDIIRKNVE SNRYRRLDLF
     QEHMFEVLER ARRMNRTDSE IYEDAVELQQ FFIRIRDELC KNGEILLSPA LSYTTKHLHN
     DVEKEKKEKL PKEIEEDKLK REEEKREAEK SEDSSGTTGL SGLHRTYSQD CSFKNSMYHV
     GDYVYVEPAE ANLQPHIVCI ERLWEDSAGE KWLYGCWFYR PNETFHLATR KFLEKEVFKS
     DYYNKVPVSK ILGKCVVMFV KEYFKLCPEN FRDEDVFVCE SRYSAKTKSF KKIKLWTMPI
     SSVRFVPRDV PLPVVRVASE FANADKGDDE KNTDNSDDNR AEDNFNLEKE KEDVPVEMSN
     GEPGCHYFEQ LRYNDMWLKV GDCVFIKSHG LVRPRVGRIE KVWVRDGAAY FYGPIFIHPE
     ETEHEPTKMF YKKEVFLSNL EETCPMSCIL GKCAVLSFKD FLSCRPTEIP ENDILLCESR
     YNESDKQMKK FKGLKRFSLS AKVVDDEIYY FRKPIIPQKE PSPLLEKKIQ LLEAKFAELE
     GGDDDIEEMG EEDSEVIEAP SLPQLQTPLA NELDLMPYTP PQSTPKSAKG SAKKESSKRK
     INMSGYILFS SEMRAVIKAQ HPDYSFGELS RLVGTEWRNL ETAKKAEYEG MMGGYPPGLP
     PLQGPVDGLV SMGSMQPLHP GGPPPHHLPP GVPGLPGIPP PGVMNQGVAP MVGTPAPGGS
     PYGQQVGVLG PPGQQAPPPY PGPHPAGPPV IQQPTTPMFV APPPKTQRLL HSEAYLKYIE
     GLSAESNSIS KWDQTLAARR RDVHLSKEQE SRLPSHWLKS KGAHTTMADA LWRLRDLMLR
     DTLNIRQAYN LENV
//
ID   LIPA2_MOUSE             Reviewed;        1257 AA.
AC   Q8BSS9; Q6P1D2; Q8BN73;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Liprin-alpha-2;
DE   AltName: Full=Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-2;
DE            Short=PTPRF-interacting protein alpha-2;
GN   Name=Ppfia2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-215 AND 1019-1257.
RC   STRAIN=C57BL/6J; TISSUE=Eye, and Pituitary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538 AND SER-689, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Alters PTPRF cellular localization and induces PTPRF
CC       clustering. May regulate the disassembly of focal adhesions. May
CC       localize receptor-like tyrosine phosphatases type 2A at specific
CC       sites on the plasma membrane, possibly regulating their
CC       interaction with the extracellular environment and their
CC       association with substrates (By similarity).
CC   -!- SUBUNIT: Forms homodimers and heterodimers with liprins-alpha and
CC       liprins-beta. Interacts with the second PTPase domain of PTPRD,
CC       PTPRF and PTPRS (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell surface (By
CC       similarity). Note=Colocalizes with PTPRF at the cell surface (By
CC       similarity).
CC   -!- DOMAIN: The N-terminal coiled coil regions mediate
CC       homodimerization preferentially and heterodimerization type
CC       alpha/alpha. The C-terminal, non-coiled coil regions mediate
CC       heterodimerization type alpha/beta and interaction with PTPRD,
CC       PTPRF and PTPRS (By similarity).
CC   -!- SIMILARITY: Belongs to the liprin family. Liprin-alpha subfamily.
CC   -!- SIMILARITY: Contains 3 SAM (sterile alpha motif) domains.
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DR   EMBL; AC111014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC065133; AAH65133.1; -; mRNA.
DR   EMBL; AK030621; BAC27051.1; -; mRNA.
DR   EMBL; AK087448; BAC39878.1; -; mRNA.
DR   IPI; IPI00224775; -.
DR   RefSeq; NP_796347.2; NM_177373.3.
DR   UniGene; Mm.391424; -.
DR   ProteinModelPortal; Q8BSS9; -.
DR   SMR; Q8BSS9; 892-959, 1017-1084.
DR   PhosphoSite; Q8BSS9; -.
DR   PRIDE; Q8BSS9; -.
DR   Ensembl; ENSMUST00000029404; ENSMUSP00000029404; ENSMUSG00000053825.
DR   GeneID; 327814; -.
DR   KEGG; mmu:327814; -.
DR   CTD; 327814; -.
DR   MGI; MGI:2443834; Ppfia2.
DR   GeneTree; ENSGT00550000074230; -.
DR   HOVERGEN; HBG052330; -.
DR   InParanoid; Q8BSS9; -.
DR   OrthoDB; EOG4PC9RB; -.
DR   PhylomeDB; Q8BSS9; -.
DR   NextBio; 397970; -.
DR   ArrayExpress; Q8BSS9; -.
DR   Bgee; Q8BSS9; -.
DR   Genevestigator; Q8BSS9; -.
DR   GermOnline; ENSMUSG00000053825; Mus musculus.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR011510; SAM_2.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 3.
DR   Pfam; PF00536; SAM_1; 2.
DR   Pfam; PF07647; SAM_2; 1.
DR   SMART; SM00454; SAM; 3.
DR   SUPFAM; SSF47769; SAM_homology; 3.
DR   PROSITE; PS50105; SAM_DOMAIN; 3.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Phosphoprotein; Repeat.
FT   CHAIN         1   1257       Liprin-alpha-2.
FT                                /FTId=PRO_0000191028.
FT   DOMAIN      898    964       SAM 1.
FT   DOMAIN     1020   1084       SAM 2.
FT   DOMAIN     1108   1177       SAM 3.
FT   COILED       29    154       Potential.
FT   COILED      185    235       Potential.
FT   COILED      264    541       Potential.
FT   COILED      643    695       Potential.
FT   COILED     1081   1107       Potential.
FT   COMPBIAS    115    528       Glu-rich.
FT   COMPBIAS    622    627       Poly-Asp.
FT   MOD_RES     538    538       Phosphoserine.
FT   MOD_RES     689    689       Phosphoserine.
FT   MOD_RES     774    774       Phosphoserine.
FT   CONFLICT    516    517       VS -> ER (in Ref. 2; AAH65133).
FT   CONFLICT    798    798       Missing (in Ref. 2; AAH65133).
SQ   SEQUENCE   1257 AA;  143234 MW;  2EC6B680B46EA4B2 CRC64;
     MMCEVMPTIN EDTPMSQRGS QSSGSDSDSH FEQLMVNMLD ERDRLLDTLR ETQESLSLAQ
     QRLQDVIYDR DSLQRQLNSA LPQDIESLTG GLTGSKGADP PEFAALTKEL NACREQLLEK
     EEEISELKAE RNNTRLLLEH LECLVSRHER SLRMTVVKRQ AQSPSGVSSE VEVLKALKSL
     FEHHKALDEK VRERLRVSLE RVSALEEELA AANQEIVALR EQNVHIQRKM VSSEGSTESE
     HLEGMEAGQK VHEKRLSNGS IDSTDDTSQI VELQELLEKQ NYEMAQMKER LTALSSRVGE
     VEQEAETARK DLIKTEEMNT KYQRDIREAM AQKEDMEERI TTLEKRYLSA QRESTSIHDM
     NDKLENELAN KEAILRQMEE KNRQLQERLE LAEQKLQQTM RKAETLPEVE AELAQRIAAL
     TKAEERHGNI EERMRHLEGQ LEEKNQELQR ARQREKMNEE HNKRLSDTVD RLLTESNERL
     QLHLKERMAA LEEKNVLIQE SENFRKNLEE SLHDKVSLAE EIEKLRSELD QMKMRTGSLI
     EPTISRTHID TSTELRYSVG SLVDSQSDYR TTKVIRRPRR GRMGVRRDEP KVKSLGDHEW
     NRTQQIGVLG SHPFESDTEM SDIDDDDRET IFSSMDLLSP SGHSDAQTLA MMLQEQLDAI
     NKEIRLIQEE KESTELRAEE IENRVASVSL EGLNLARVHP GTSITASVTA SSLASSSPPS
     GHSTPKLTPR SPAREMDRMG VMTLPSDLRK HRRKIAVVEE DGREDKATIK CETSPPPTPR
     AVRMTHTLPS SYHNDARSSL SASLEPDSLG LGSANSSQDS LHKAPKKKGI KSSIGRLFGK
     KEKARLGQLR GFMETEAAAQ ESLGLGKLGT QAEKDRRLKK KHELLEEARR KGLPFAQWDG
     PTVVAWLELW LGMPAWYVAA CRANVKSGAI MSALSDTEIQ REIGISNPLH RLKLRLAIQE
     MVSLTSPSAP PTSRTPSGNV WVTHEEMENL TAPAKTKESE EGSWAQCPVF LQTLAYGDMN
     HEWIGNEWLP SLGLPQYRSY FMECLVDARM LDHLTKKDLR VHLKMVDSFH RTSLQYGIMC
     LKRLNYDRKE LERRREASQH EIKDVLVWSN DRVIRWIQAI GLREYANNIL ESGVHGSLIA
     LDENFDYSSL ALLLQIPTQN TQARQILERE YNNLLALGTE RRLDESDDKN FRRGSTWRRQ
     FPPREVHGIS MMPGSSETLP AGFRLTTTSG QSRKMTTDVA SSRLQRLDNS TVRTYSC
//
ID   ASPH_MOUSE              Reviewed;         741 AA.
AC   Q8BSY0; Q9EPA6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Aspartyl/asparaginyl beta-hydroxylase;
DE            EC=1.14.11.16;
DE   AltName: Full=Aspartate beta-hydroxylase;
DE            Short=ASP beta-hydroxylase;
DE   AltName: Full=Peptide-aspartate beta-dioxygenase;
GN   Name=Asph;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=20564328; PubMed=10956665; DOI=10.1074/jbc.M006753200;
RA   Dinchuk J.E., Henderson N.L., Burn T.C., Huber R., Ho S.P., Link J.,
RA   O'Neil K.T., Focht R.J., Scully M.S., Hollis J.M., Hollis G.F.,
RA   Friedman P.A.;
RT   "Aspartyl beta -hydroxylase (Asph) and an evolutionarily conserved
RT   isoform of Asph missing the catalytic domain share exons with
RT   junctin.";
RL   J. Biol. Chem. 275:39543-39554(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Specifically hydroxylates an Asp or Asn residue in
CC       certain epidermal growth factor-like (EGF) domains of a number of
CC       proteins.
CC   -!- CATALYTIC ACTIVITY: Peptide L-aspartate + 2-oxoglutarate + O(2) =
CC       peptide 3-hydroxy-L-aspartate + succinate + CO(2).
CC   -!- COFACTOR: Iron (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       type II membrane protein (By similarity).
CC   -!- PTM: Might be processed to the 56 kDa (AA 274-757) or 52 kDa (AA
CC       315-757) forms in the lumen of the endoplasmic reticulum (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the aspartyl/asparaginyl beta-hydroxylase
CC       family.
CC   -!- SIMILARITY: Contains 2 TPR repeats.
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DR   EMBL; AF289486; AAG40808.1; -; mRNA.
DR   EMBL; AF289487; AAG40809.1; -; mRNA.
DR   EMBL; AK030293; BAC26882.1; -; mRNA.
DR   IPI; IPI00624896; -.
DR   RefSeq; NP_001171321.1; NM_001177850.1.
DR   RefSeq; NP_001171323.1; NM_001177852.1.
DR   RefSeq; NP_001171324.1; NM_001177853.1.
DR   RefSeq; NP_001171325.1; NM_001177854.1.
DR   RefSeq; NP_001171326.1; NM_001177855.1.
DR   RefSeq; NP_075553.2; NM_023066.3.
DR   UniGene; Mm.222206; -.
DR   UniGene; Mm.412008; -.
DR   ProteinModelPortal; Q8BSY0; -.
DR   SMR; Q8BSY0; 359-537.
DR   STRING; Q8BSY0; -.
DR   PhosphoSite; Q8BSY0; -.
DR   PRIDE; Q8BSY0; -.
DR   Ensembl; ENSMUST00000078139; ENSMUSP00000077273; ENSMUSG00000028207.
DR   GeneID; 65973; -.
DR   KEGG; mmu:65973; -.
DR   UCSC; uc008ryf.1; mouse.
DR   CTD; 65973; -.
DR   MGI; MGI:1914186; Asph.
DR   HOGENOM; HBG716318; -.
DR   HOVERGEN; HBG004290; -.
DR   InParanoid; Q8BSY0; -.
DR   OMA; QGRRNEN; -.
DR   OrthoDB; EOG42FSK2; -.
DR   PhylomeDB; Q8BSY0; -.
DR   BRENDA; 1.14.11.16; 244.
DR   NextBio; 320434; -.
DR   ArrayExpress; Q8BSY0; -.
DR   Bgee; Q8BSY0; -.
DR   CleanEx; MM_ASPH; -.
DR   Genevestigator; Q8BSY0; -.
DR   GermOnline; ENSMUSG00000028207; Mus musculus.
DR   GO; GO:0030176; C:integral to endoplasmic reticulum membrane; IEA:InterPro.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IEA:UniProtKB-KW.
DR   GO; GO:0004597; F:peptide-aspartate beta-dioxygenase activity; IEA:EC.
DR   GO; GO:0060325; P:face morphogenesis; IMP:MGI.
DR   GO; GO:0035108; P:limb morphogenesis; IMP:MGI.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IGI:MGI.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0060021; P:palate development; IMP:MGI.
DR   GO; GO:0007389; P:pattern specification process; IMP:MGI.
DR   GO; GO:0042264; P:peptidyl-aspartic acid hydroxylation; IDA:MGI.
DR   InterPro; IPR007943; Asp-B-hydro/Triadin_dom.
DR   InterPro; IPR007803; Asp_Arg_b-Hydrxlase.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
DR   Pfam; PF05279; Asp-B-Hydro_N; 1.
DR   Pfam; PF05118; Asp_Arg_Hydrox; 1.
DR   PROSITE; PS50005; TPR; 2.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   2: Evidence at transcript level;
KW   Dioxygenase; Endoplasmic reticulum; Glycoprotein; Iron; Membrane;
KW   Oxidoreductase; Phosphoprotein; Repeat; Signal-anchor; TPR repeat;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    741       Aspartyl/asparaginyl beta-hydroxylase.
FT                                /FTId=PRO_0000254161.
FT   TOPO_DOM      1     62       Cytoplasmic (Potential).
FT   TRANSMEM     63     83       Helical; Signal-anchor for type II
FT                                membrane protein; (Potential).
FT   TOPO_DOM     84    741       Lumenal (Potential).
FT   REPEAT      324    357       TPR 1.
FT   REPEAT      365    398       TPR 2.
FT   REPEAT      437    470       TPR 3.
FT   REPEAT      472    504       TPR 4.
FT   REPEAT      508    540       TPR 5.
FT   COMPBIAS      9     61       Gly-rich.
FT   COMPBIAS     14     38       Ser-rich.
FT   COMPBIAS    310    315       Poly-Lys.
FT   MOD_RES      38     38       Phosphoserine (By similarity).
FT   CARBOHYD    453    453       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    689    689       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    131    132       Missing (in Ref. 1; AAG40808/AAG40809).
FT   CONFLICT    279    279       A -> E (in Ref. 1; AAG40808/AAG40809).
SQ   SEQUENCE   741 AA;  83042 MW;  0660A6A5E34418C8 CRC64;
     MAPRKNAKGG GGNSSSSGSG SGSGSGSPST GSSGSSSSPG ARREAKHGGH KNGRRGGISG
     GSFFTWFMVI ALLGVWTSVA VVWFDLVDYE EVLGKLGVYD ADGDGDFDVD DAKVLLGLKE
     RSPSERTFPP EEEAETHAEL EEQAPEGADI QNVEDEVKEQ IQSLLQESVH TDHDLEADGL
     AGEPQPEVED FLTVTDSDDR FEDLEPGTVH EEIEDTYHVE DTASQNHPND MEEMTNEQEN
     SDPSEAVTDA GVLLPHAEEV RHQDYDEPVY EPSEHEGVAI SDNTIDDSSI ISEEINVASV
     EEQQDTPPVK KKKPKLLNKF DKTIKAELDA AEKLRKRGKI EEAVNAFEEL VRKYPQSPRA
     RYGKAQCEDD LAEKQRSNEV LRRAIETYQE AADLPDAPTD LVKLSLKRRS ERQQFLGHMR
     GSLLTLQRLV QLFPSDTTLK NDLGVGYLLL GDNDSAKKVY EEVLNVTPND GFAKVHYGFI
     LKAQNKISES IPYLKEGIES GDPGTDDGRF YFHLGDAMQR VGNKEAYKWY ELGHKRGHFA
     SVWQRSLYNV NGLKAQPWWT PRETGYTELV KSLERNWKLI RDEGLMVMDK AKGLFLPEDE
     NLREKGDWSQ FTLWQQGRKN ENACKGAPKT CALLEKFSET TGCRRGQIKY SIMHPGTHVW
     PHTGPTNCRL RMHLGLVIPK EGCKIRCANE TRTWEEGKVL IFDDSFEHEV WQDASSFRLI
     FIVDVWHPEL TPQQRRSLPA I
//
ID   CNOT4_MOUSE             Reviewed;         575 AA.
AC   Q8BT14; Q8CCR4; Q9CV74; Q9Z1D0;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=CCR4-NOT transcription complex subunit 4;
DE            EC=6.3.2.-;
DE   AltName: Full=CCR4-associated factor 4;
DE   AltName: Full=E3 ubiquitin-protein ligase CNOT4;
DE   AltName: Full=Potential transcriptional repressor NOT4Hp;
GN   Name=Cnot4; Synonyms=Not4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Chiang P.-W.;
RT   "Isolation and characterization of human and murine homologues of
RT   yeast NOT4 gene.";
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [5]
RP   STRUCTURE BY NMR OF 101-198.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the RNA recognition motif of CNOT4.";
RL   Submitted (NOV-2005) to the PDB data bank.
CC   -!- FUNCTION: Has E3 ubiquitin ligase activity. The CCR4-NOT complex
CC       functions as general transcription regulation complex (By
CC       similarity).
CC   -!- SUBUNIT: Subunit of the CCR4-NOT core complex that contains
CC       CHAF1A, CHAF1B, CNOT1, CNOT2, CNOT3, CNOT4, CNOT6 and CNOT8. Binds
CC       CNOT1 via its C-terminus. Binds E2 ubiquitin ligases via its RING
CC       domain. Interacts (via RING domain) with UBE2D2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). Nucleus (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BT14-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BT14-2; Sequence=VSP_009930;
CC       Name=3;
CC         IsoId=Q8BT14-3; Sequence=VSP_009931;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Autoubiquitinated (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Contains 1 C3H1-type zinc finger.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; U71269; AAD00181.1; -; mRNA.
DR   EMBL; AK009234; BAB26155.1; -; mRNA.
DR   EMBL; AK028190; BAC25801.1; -; mRNA.
DR   EMBL; AK032248; BAC27779.1; -; mRNA.
DR   EMBL; BC058778; AAH58778.1; -; mRNA.
DR   IPI; IPI00130086; -.
DR   IPI; IPI00410929; -.
DR   IPI; IPI00410930; -.
DR   RefSeq; NP_001157883.1; NM_001164411.1.
DR   RefSeq; NP_001157885.1; NM_001164413.1.
DR   RefSeq; NP_058573.3; NM_016877.4.
DR   UniGene; Mm.214525; -.
DR   UniGene; Mm.398182; -.
DR   PDB; 2CPI; NMR; -; A=101-198.
DR   PDBsum; 2CPI; -.
DR   ProteinModelPortal; Q8BT14; -.
DR   SMR; Q8BT14; 1-78, 103-229.
DR   STRING; Q8BT14; -.
DR   PhosphoSite; Q8BT14; -.
DR   PRIDE; Q8BT14; -.
DR   Ensembl; ENSMUST00000044163; ENSMUSP00000044137; ENSMUSG00000038784.
DR   Ensembl; ENSMUST00000114993; ENSMUSP00000110645; ENSMUSG00000038784.
DR   GeneID; 53621; -.
DR   KEGG; mmu:53621; -.
DR   UCSC; uc009bid.1; mouse.
DR   UCSC; uc009big.1; mouse.
DR   UCSC; uc009bih.1; mouse.
DR   CTD; 53621; -.
DR   MGI; MGI:1859026; Cnot4.
DR   GeneTree; ENSGT00390000000068; -.
DR   HOVERGEN; HBG051043; -.
DR   OMA; RICPTLF; -.
DR   NextBio; 310353; -.
DR   ArrayExpress; Q8BT14; -.
DR   Bgee; Q8BT14; -.
DR   CleanEx; MM_CNOT4; -.
DR   Genevestigator; Q8BT14; -.
DR   GermOnline; ENSMUSG00000038784; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50103; ZF_C3H1; 1.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Ligase;
KW   Metal-binding; Nucleus; Phosphoprotein; RNA-binding; Transcription;
KW   Transcription regulation; Ubl conjugation; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    575       CCR4-NOT transcription complex subunit 4.
FT                                /FTId=PRO_0000081680.
FT   DOMAIN      109    189       RRM.
FT   ZN_FING      14     57       RING-type; degenerate.
FT   ZN_FING     190    217       C3H1-type.
FT   COILED       68    104       Potential.
FT   MOD_RES      71     71       Phosphoserine.
FT   MOD_RES     324    324       Phosphoserine (By similarity).
FT   MOD_RES     432    432       Phosphoserine (By similarity).
FT   VAR_SEQ     271    274       RYDT -> S (in isoform 2).
FT                                /FTId=VSP_009930.
FT   VAR_SEQ     543    575       GEEEVKVSTMPLSASSHSLQQGQQPTSLHTTVA -> DNNS
FT                                SVESLNMKEWQDGLRALLPNININFGGLPNSSSPSNANHSA
FT                                PTSNTATTDSVSWDSPGSWTDPAIITGIPASSGNTLDSIQD
FT                                DNPPHWLKSLQALTEMDGPSAASSQPHHSAPFSTQIPLHRA
FT                                SWNPYPPPSNPSSFHSPPPGFQTAFRPPSKTPTDLLQSSTL
FT                                DRH (in isoform 3).
FT                                /FTId=VSP_009931.
FT   CONFLICT    167    167       E -> Q (in Ref. 2; BAC25801).
FT   CONFLICT    177    177       N -> H (in Ref. 2; BAC25801).
FT   CONFLICT    207    207       K -> Q (in Ref. 2; BAC25801).
FT   CONFLICT    417    417       D -> Y (in Ref. 2; BAC27779).
FT   STRAND      111    116
FT   TURN        118    120
FT   HELIX       123    127
FT   TURN        129    135
FT   STRAND      138    144
FT   STRAND      151    153
FT   STRAND      157    165
FT   HELIX       166    176
FT   STRAND      179    181
FT   STRAND      184    190
SQ   SEQUENCE   575 AA;  63474 MW;  E0B763C8262D03CA CRC64;
     MSRSPDAKED PVECPLCMEP LEIDDINFFP CTCGYQICRF CWHRIRTDEN GLCPACRKPY
     PEDPAVYKPL SQEELQRIKN EKKQKQNERK QKISENRKHL ASVRVVQKNL VFVVGLSQRL
     ADPEVLKRPE YFGKFGKIHK VVINNSTSYA GSQGPSASAY VTYIRSEDAL RAIQCVNNVV
     VDGRTLKASL GTTKYCSYFL KNMQCPKPDC MYLHELGDEA ASFTKEEMQA GKHQEYEQKL
     LQELYKLNPN FLQLSTGSVD KNKNKVTPLQ RYDTPIDKPS DSLSIGNGDN SQQISNSDTP
     SPPPGLSKSN PVIPISSSNH SARSPFEGAV TESQSLFSDN FRHPNPIPSG LPPFPSSPQT
     PSDWPTAPEP QSLFTSETIP VSSSTDWQAA FGFGSSKQPE DDLGFDPFDV TRKALADLIE
     KELSVQDQPS LSPTSLQNAS SHTTTAKGPG SGFLHSAAPT NANSLNSTFS VLPQRFPQFQ
     QHRAVYNSFG FPGQAARYPW MAFPRNSIMH LNHTANPTSN SNFLDLNLPP QHNTGLGGIP
     IAGEEEVKVS TMPLSASSHS LQQGQQPTSL HTTVA
//
ID   CN037_MOUSE             Reviewed;         775 AA.
AC   Q8BT18; Q8BFQ7; Q8R1Q5; Q9D6C5;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Uncharacterized protein C14orf37 homolog;
DE   Flags: Precursor;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, Embryo, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK014402; BAB29326.1; -; mRNA.
DR   EMBL; AK028180; BAC25793.1; -; mRNA.
DR   EMBL; AK032093; BAC27694.1; -; mRNA.
DR   EMBL; AK049427; BAC33748.1; -; mRNA.
DR   EMBL; BC023359; AAH23359.1; -; mRNA.
DR   IPI; IPI00108650; -.
DR   RefSeq; NP_080418.2; NM_026142.4.
DR   UniGene; Mm.318710; -.
DR   PRIDE; Q8BT18; -.
DR   Ensembl; ENSMUST00000036972; ENSMUSP00000036220; ENSMUSG00000036242.
DR   GeneID; 67419; -.
DR   KEGG; mmu:67419; -.
DR   UCSC; uc007tkj.1; mouse.
DR   MGI; MGI:1914669; 3632451O06Rik.
DR   eggNOG; roNOG07656; -.
DR   GeneTree; ENSGT00390000012816; -.
DR   HOGENOM; HBG505580; -.
DR   HOVERGEN; HBG081262; -.
DR   InParanoid; Q8BT18; -.
DR   OMA; DEWDDTK; -.
DR   OrthoDB; EOG418BMV; -.
DR   PhylomeDB; Q8BT18; -.
DR   NextBio; 324514; -.
DR   ArrayExpress; Q8BT18; -.
DR   Bgee; Q8BT18; -.
DR   CleanEx; MM_3632451O06RIK; -.
DR   Genevestigator; Q8BT18; -.
DR   GermOnline; ENSMUSG00000036242; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     47       Potential.
FT   CHAIN        48    775       Uncharacterized protein C14orf37 homolog.
FT                                /FTId=PRO_0000252153.
FT   TOPO_DOM     48    715       Extracellular (Potential).
FT   TRANSMEM    716    736       Helical; (Potential).
FT   TOPO_DOM    737    775       Cytoplasmic (Potential).
FT   COMPBIAS    604    640       Glu-rich.
FT   CARBOHYD     76     76       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    476    476       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    102    102       E -> G (in Ref. 1; BAB29326).
FT   CONFLICT    106    106       I -> H (in Ref. 2; AAH23359).
FT   CONFLICT    137    137       V -> A (in Ref. 2; AAH23359).
FT   CONFLICT    140    140       A -> P (in Ref. 2; AAH23359).
FT   CONFLICT    162    162       V -> A (in Ref. 2; AAH23359).
FT   CONFLICT    183    183       N -> D (in Ref. 1; BAB29326).
FT   CONFLICT    206    208       DNQ -> NNH (in Ref. 2; AAH23359).
FT   CONFLICT    228    228       I -> V (in Ref. 1; BAB29326).
FT   CONFLICT    247    247       V -> F (in Ref. 2; AAH23359).
FT   CONFLICT    256    256       M -> T (in Ref. 2; AAH23359).
FT   CONFLICT    266    266       M -> N (in Ref. 2; AAH23359).
FT   CONFLICT    286    286       F -> V (in Ref. 2; AAH23359).
FT   CONFLICT    351    351       G -> A (in Ref. 2; AAH23359).
FT   CONFLICT    468    468       R -> I (in Ref. 2; AAH23359).
FT   CONFLICT    479    479       S -> F (in Ref. 2; AAH23359).
FT   CONFLICT    522    522       G -> W (in Ref. 2; AAH23359).
FT   CONFLICT    544    544       M -> V (in Ref. 2; AAH23359).
FT   CONFLICT    583    583       P -> L (in Ref. 2; AAH23359).
FT   CONFLICT    591    591       S -> C (in Ref. 1; BAC25793).
FT   CONFLICT    621    621       Missing (in Ref. 2; AAH23359).
FT   CONFLICT    671    671       S -> P (in Ref. 2; AAH23359).
FT   CONFLICT    754    754       Missing (in Ref. 1; BAC25793).
FT   CONFLICT    771    771       S -> F (in Ref. 2; AAH23359).
SQ   SEQUENCE   775 AA;  83774 MW;  FC7D04D0EFE12693 CRC64;
     MLQDSITGIV NSFNLFFPST MSRPTLMPTC VAFCSILFLT LATGCQAFPK VERRETAQEY
     AEKEQSQKMN TDDQENISFA PKYMLQQMSS EAPMVLSEGP SEIPLIKVFS VNKESHLPGA
     GLLHPTSPGV YSSSEPVVSA SEQEPGPSLL ERMSSEHSLS KVMLTVAVSS PASLNPDQEG
     PYNSLSTQPI VAAVTDVTHG SLDYLDNQLF AAKSQEAVSL GNSPSSSINT KEPEIIKADA
     AMGTTVVPGV DSTGDMEPDR ERPSEMAADD GQSTTTKYLV TIPNNFLTTE PTAGSILGDA
     KVTVSVSTAG PVSSIFNEEW DDTKFESISR GRPPEPGDNA ETQMRTKPPH GTYESFEGTE
     ESPSSTAVLK VAPGHLGGEP ALGTALVTAL GDERSPVLTH QISFTPMSLA EDPEVSTMKL
     FPSAGGFRAS TQGDRTQLSS ETAFSTSQYE SVPQQEAGNV LKDITQERKM ATQAMNTTSP
     VVTQEHMATI EVPRGSGEPE EGMPSLSPVP AEVADAELSR RGESLATPAS TTVVPLSLKL
     TSSMEDLMDT ITGPSEEFIP VLGSPMAPPA MTVEAPTISS ALPSEGRTSP SISRPNTAAS
     YGLEQLESEE VEDDEDEEDE EDEEEEEEDE EDEEDEEDKE TDSLYKDFDG DTEPPGFTLP
     GITSQEPDIR SGSMDLLEVA TYQVPETIEW EQQNQGLVRS WMEKLKDKAG YMSGMLVPVG
     VGIAGALFIL GALYSIKVMN RRRRNGFKRH KRKQREFNSM QDRVMLLADS SEDEF
//
ID   CF057_MOUSE             Reviewed;         104 AA.
AC   Q8BTE0; Q9CQN5; Q9D537;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=UPF0369 protein C6orf57 homolog;
DE   Flags: Precursor;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pancreas, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Secreted (Potential).
CC   -!- SIMILARITY: Belongs to the UPF0369 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK003789; BAC25055.1; -; mRNA.
DR   EMBL; AK004301; BAB23255.1; -; mRNA.
DR   EMBL; AK007909; BAB25342.1; -; mRNA.
DR   EMBL; AK015824; BAB29991.1; -; mRNA.
DR   EMBL; BC028981; AAH28981.1; -; mRNA.
DR   IPI; IPI00315560; -.
DR   RefSeq; NP_080779.2; NM_026503.3.
DR   UniGene; Mm.250424; -.
DR   ProteinModelPortal; Q8BTE0; -.
DR   SMR; Q8BTE0; 60-104.
DR   STRING; Q8BTE0; -.
DR   PRIDE; Q8BTE0; -.
DR   Ensembl; ENSMUST00000027338; ENSMUSP00000027338; ENSMUSG00000026154.
DR   GeneID; 68002; -.
DR   KEGG; mmu:68002; -.
DR   UCSC; uc007amj.1; mouse.
DR   MGI; MGI:1915252; 1110058L19Rik.
DR   eggNOG; roNOG16943; -.
DR   GeneTree; ENSGT00390000009155; -.
DR   HOGENOM; HBG745911; -.
DR   HOVERGEN; HBG059140; -.
DR   InParanoid; Q8BTE0; -.
DR   OMA; PLTKFPD; -.
DR   OrthoDB; EOG46Q6V8; -.
DR   PhylomeDB; Q8BTE0; -.
DR   NextBio; 326184; -.
DR   ArrayExpress; Q8BTE0; -.
DR   Bgee; Q8BTE0; -.
DR   CleanEx; MM_1110058L19RIK; -.
DR   Genevestigator; Q8BTE0; -.
DR   GermOnline; ENSMUSG00000026154; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   InterPro; IPR012875; DUF1674.
DR   Pfam; PF07896; DUF1674; 1.
PE   2: Evidence at transcript level;
KW   Secreted; Signal.
FT   SIGNAL        1     23       Potential.
FT   CHAIN        24    104       UPF0369 protein C6orf57 homolog.
FT                                /FTId=PRO_0000244341.
FT   CONFLICT     17     17       A -> E (in Ref. 1; BAB29991).
SQ   SEQUENCE   104 AA;  11889 MW;  70ACA3B549C1B916 CRC64;
     MVSTTLSVSR MTFVWRAARP SLLNHSLRKM SYQEGKPEPA KQALKKSKLP LGRFDSLEDS
     PEEREPLQKF PDDVNPVTKE KGGPKGPEPT RYGDWERKGR CIDF
//
ID   NDRG4_MOUSE             Reviewed;         352 AA.
AC   Q8BTG7; Q6ZPW3; Q923D7;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Protein NDRG4;
DE   AltName: Full=Protein Ndr4;
GN   Name=Ndrg4; Synonyms=Kiaa1180, Ndr4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: May play a role in the early postnatal development and
CC       function of neuronal cells (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BTG7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BTG7-2; Sequence=VSP_022959;
CC       Name=3;
CC         IsoId=Q8BTG7-3; Sequence=VSP_022958;
CC   -!- SIMILARITY: Belongs to the NDRG family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98115.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK090374; BAC41189.1; -; mRNA.
DR   EMBL; AK168873; BAE40691.1; -; mRNA.
DR   EMBL; AK129305; BAC98115.1; ALT_INIT; mRNA.
DR   EMBL; BC006595; AAH06595.1; -; mRNA.
DR   IPI; IPI00124154; -.
DR   IPI; IPI00225031; -.
DR   IPI; IPI00620325; -.
DR   RefSeq; NP_001181935.1; NM_001195006.1.
DR   RefSeq; NP_663577.1; NM_145602.3.
DR   UniGene; Mm.29846; -.
DR   ProteinModelPortal; Q8BTG7; -.
DR   SMR; Q8BTG7; 9-285.
DR   STRING; Q8BTG7; -.
DR   PhosphoSite; Q8BTG7; -.
DR   PRIDE; Q8BTG7; -.
DR   Ensembl; ENSMUST00000041318; ENSMUSP00000036226; ENSMUSG00000036564.
DR   Ensembl; ENSMUST00000073139; ENSMUSP00000072883; ENSMUSG00000036564.
DR   Ensembl; ENSMUST00000080666; ENSMUSP00000079495; ENSMUSG00000036564.
DR   GeneID; 234593; -.
DR   KEGG; mmu:234593; -.
DR   UCSC; uc009myu.1; mouse.
DR   CTD; 234593; -.
DR   MGI; MGI:2384590; Ndrg4.
DR   eggNOG; roNOG06584; -.
DR   GeneTree; ENSGT00390000001874; -.
DR   HOVERGEN; HBG052591; -.
DR   OMA; VDTDWKE; -.
DR   OrthoDB; EOG4Q84XP; -.
DR   ArrayExpress; Q8BTG7; -.
DR   Bgee; Q8BTG7; -.
DR   CleanEx; MM_NDRG4; -.
DR   Genevestigator; Q8BTG7; -.
DR   GermOnline; ENSMUSG00000036564; Mus musculus.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   InterPro; IPR004142; Ndr.
DR   PANTHER; PTHR11034; Ndr; 1.
DR   Pfam; PF03096; Ndr; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Developmental protein; Phosphoprotein.
FT   CHAIN         1    352       Protein NDRG4.
FT                                /FTId=PRO_0000159580.
FT   COMPBIAS    253    256       Poly-Thr.
FT   MOD_RES     298    298       Phosphoserine.
FT   VAR_SEQ       1      7       MPECWDG -> MKVLGHRLQLLTGLLLHDVTMAGLQELRFP
FT                                EEKPLLRGQDATEMDNPDAFLSIVDTDWK (in isoform
FT                                3).
FT                                /FTId=VSP_022958.
FT   VAR_SEQ     289    302       IAHLKDRRLSGGAV -> M (in isoform 2).
FT                                /FTId=VSP_022959.
SQ   SEQUENCE   352 AA;  38509 MW;  3ED388148DC852CD CRC64;
     MPECWDGEHD IETPYGLLHV VIRGSPKGNR PAILTYHDVG LNHKLCFNTF FNFEDMQEIT
     KHFVVCHVDA PGQQVGASQF PQGYQFPSME QLAAMLPSVV QHFGFKYVIG IGVGAGAYVL
     AKFALIFPDL VEGLVLMNID PNGKGWIDWA ATKLSGLTST LPDTVLSHLF SQEELVNNTE
     LVQSYRQQIS NVVNQANLQL FWNMYNSRRD LDINRPGTVP NAKTLRCPVM LVVGDNAPAE
     EGVVECNSKL DPTTTTFLKM ADSGGLPQVT QPGKLTEAFK YFLQGMGYIA HLKDRRLSGG
     AVPSASMTRL ARSRTASLTS ASSVDGSRPQ PCAHSDSSEG MGQVNHTMEV SC
//
ID   KC1G1_MOUSE             Reviewed;         459 AA.
AC   Q8BTH8;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Casein kinase I isoform gamma-1;
DE            Short=CKI-gamma 1;
DE            EC=2.7.11.1;
GN   Name=Csnk1g1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Casein kinases are operationally defined by their
CC       preferential utilization of acidic proteins such as caseins as
CC       substrates. It can phosphorylate a large number of proteins.
CC       Participates in Wnt signaling (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- PTM: Autophosphorylated (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC       protein kinase family. Casein kinase I subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AK090262; BAC41152.1; -; mRNA.
DR   IPI; IPI00225049; -.
DR   RefSeq; NP_775277.2; NM_173185.2.
DR   UniGene; Mm.325816; -.
DR   ProteinModelPortal; Q8BTH8; -.
DR   SMR; Q8BTH8; 45-339.
DR   STRING; Q8BTH8; -.
DR   PhosphoSite; Q8BTH8; -.
DR   PRIDE; Q8BTH8; -.
DR   Ensembl; ENSMUST00000034949; ENSMUSP00000034949; ENSMUSG00000032384.
DR   GeneID; 214897; -.
DR   KEGG; mmu:214897; -.
DR   UCSC; uc009qeg.1; mouse.
DR   CTD; 214897; -.
DR   MGI; MGI:2660884; Csnk1g1.
DR   GeneTree; ENSGT00560000076651; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG000176; -.
DR   InParanoid; Q8BTH8; -.
DR   OrthoDB; EOG4GHZP4; -.
DR   PhylomeDB; Q8BTH8; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 374497; -.
DR   ArrayExpress; Q8BTH8; -.
DR   Bgee; Q8BTH8; -.
DR   CleanEx; MM_CSNK1G1; -.
DR   Genevestigator; Q8BTH8; -.
DR   GermOnline; ENSMUSG00000032384; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR022247; Casein_kinase-1_gamma_C.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   Pfam; PF12605; CK1gamma_C; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.
FT   CHAIN         1    459       Casein kinase I isoform gamma-1.
FT                                /FTId=PRO_0000192840.
FT   DOMAIN       44    315       Protein kinase.
FT   NP_BIND      50     58       ATP (By similarity).
FT   ACT_SITE    164    164       Proton acceptor (By similarity).
FT   BINDING      73     73       ATP (By similarity).
FT   MOD_RES     344    344       Phosphoserine (By similarity).
FT   MOD_RES     361    361       Phosphoserine (By similarity).
SQ   SEQUENCE   459 AA;  52768 MW;  2996B013DECA3DEC CRC64;
     MDHSNREKDD RQRTTKTMAQ RNTHCSRPSG TSTSSGVHMV GPNFRVGKKI GCGNFGELRL
     GKNLYTNEYV AIKLEPIKSR APQLHLEYRF YKQLGSAGEG LPQVYYFGPC GKYNAMVLEL
     LGPSLEDLFD LCDRTFTLKT VLMIAIQLLS RMEYVHSKNL IYRDVKPENF LIGRQGNKKE
     HVIHIIDFGL AKEYVDPETK KHIPYREHKS LTGTARYMSI NTHLGKEQSR RDDLEALGHM
     FMYFLRGSLP WQGLKADTLK ERYQKIGDTK RNTPIEALCE NFPEEMATYL RYVRRLDFFE
     KPDYEYLRTL FTDLFERKGY TFDYAYDWVG RPIPTPVGSV HVDSGASAIT RESHTHRDRP
     SQQQPLRNQT TSSERRGEWE IQPSRQTNTS YLTSHLAADR HGGSVQVVSS TNGELNVDDP
     TGAHSNAPIT AHAEVEVVEE AKCCCFFKRK RKKTAQRHK
//
ID   SRRM2_MOUSE             Reviewed;        2703 AA.
AC   Q8BTI8; Q3TBY5; Q569P9; Q80U37; Q8K383;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Serine/arginine repetitive matrix protein 2;
GN   Name=Srrm2; Synonyms=Kiaa0324;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-745 (ISOFORM 1).
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-191 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2060-2703 (ISOFORM 3).
RC   STRAIN=FVB/N, and NMRI; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 944-968; 1338-1349 AND 1924-1932, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 950-2703 (ISOFORMS 1/2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1360, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-898; THR-1448; SER-1798;
RP   THR-1800 AND SER-1963, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433; SER-434; SER-435;
RP   SER-438; SER-944; SER-945; SER-946; SER-1334; SER-1339; SER-1340;
RP   SER-1343; SER-1376; SER-1377; SER-1378; SER-1380; SER-1572; THR-1574;
RP   SER-1576; SER-1577; SER-2019; SER-2023; SER-2644; SER-2646; TYR-2647
RP   AND SER-2648, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-823; THR-973 AND
RP   SER-1068, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402; SER-406; SER-433;
RP   SER-434; SER-435; SER-821; THR-823; THR-973; SER-1068; SER-1338;
RP   SER-1339; SER-1359; SER-1380; SER-1414; SER-1576; SER-1577; SER-2052;
RP   SER-2054; THR-2056 AND SER-2073, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1209 AND SER-1216, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349; SER-351; SER-1216;
RP   SER-1305; SER-1996; SER-1998; THR-2537; SER-2646 AND SER-2648, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349; SER-351; SER-433;
RP   SER-470; SER-472; SER-531; SER-622; THR-624; SER-626; SER-773;
RP   SER-775; SER-778; SER-924; SER-926; SER-928; SER-1151; SER-1216;
RP   SER-1278; SER-1338; SER-1343; SER-1380; SER-1434; SER-1438; SER-1439;
RP   SER-1453; SER-1458; SER-1508; SER-1513; SER-1515; SER-1533; SER-1535;
RP   SER-1537; SER-1538; SER-1545; SER-1548; SER-1552; SER-1631; THR-1654;
RP   SER-1718; SER-1720; SER-1747; SER-1749; SER-1813; SER-1822; SER-1844;
RP   SER-1846; SER-1849; SER-1864; SER-1866; SER-1869; SER-1910; SER-1912;
RP   THR-1914; SER-1958; SER-1960; THR-1962; SER-1963; SER-1982; SER-1984;
RP   THR-1986; SER-1994; SER-1996; SER-1998; SER-2019; THR-2021; SER-2023;
RP   THR-2056; SER-2360; THR-2362; SER-2381; THR-2537; SER-2618; SER-2638;
RP   SER-2642; SER-2646; SER-2648 AND SER-2656, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433; SER-434; SER-435;
RP   SER-531; SER-533; SER-1151; SER-1338; SER-1339; SER-1343; SER-1360;
RP   SER-1572; SER-1576; SER-1577; SER-1982; SER-1984; THR-1986; SER-2019;
RP   THR-2021; SER-2023; SER-2052; SER-2054; THR-2056; SER-2224; SER-2335;
RP   SER-2351; SER-2404; SER-2646; SER-2648; SER-2656 AND SER-2660, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Involved in pre-mRNA splicing. May function at or prior
CC       to the first catalytic step of splicing at the catalytic center of
CC       the spliceosome. May do so by stabilizing the catalytic center or
CC       the position of the RNA substrate. Binds to RNA (By similarity).
CC   -!- SUBUNIT: Component of the active spliceosome. Found in a pre-mRNA
CC       splicing complex with SFRS4, SFRS5, SNRP70, SNRPA1, SRRM1 and
CC       SRRM2. Identified in the spliceosome C complex, at least composed
CC       of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41,
CC       DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1,
CC       HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK, HNRPM,
CC       HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1,
CC       PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B,
CC       PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2,
CC       SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2,
CC       SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2,
CC       SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BTI8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BTI8-2; Sequence=VSP_020188;
CC       Name=3;
CC         IsoId=Q8BTI8-3; Sequence=VSP_020189;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Belongs to the CWC21 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH27781.1; Type=Erroneous initiation;
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DR   EMBL; AK090123; BAC41104.1; -; mRNA.
DR   EMBL; AK171001; BAE42172.1; -; mRNA.
DR   EMBL; BC027781; AAH27781.1; ALT_INIT; mRNA.
DR   EMBL; BC092355; AAH92355.1; -; mRNA.
DR   EMBL; AK122248; BAC65530.1; -; mRNA.
DR   IPI; IPI00225062; -.
DR   IPI; IPI00785240; -.
DR   IPI; IPI00785384; -.
DR   RefSeq; NP_780438.2; NM_175229.3.
DR   UniGene; Mm.436876; -.
DR   UniGene; Mm.5222; -.
DR   ProteinModelPortal; Q8BTI8; -.
DR   SMR; Q8BTI8; 63-101.
DR   STRING; Q8BTI8; -.
DR   PhosphoSite; Q8BTI8; -.
DR   REPRODUCTION-2DPAGE; IPI00225062; -.
DR   REPRODUCTION-2DPAGE; IPI00785240; -.
DR   PRIDE; Q8BTI8; -.
DR   Ensembl; ENSMUST00000073292; ENSMUSP00000073018; ENSMUSG00000039218.
DR   Ensembl; ENSMUST00000088621; ENSMUSP00000085993; ENSMUSG00000039218.
DR   GeneID; 75956; -.
DR   KEGG; mmu:75956; -.
DR   UCSC; uc008atn.1; mouse.
DR   UCSC; uc008ato.1; mouse.
DR   CTD; 75956; -.
DR   MGI; MGI:1923206; Srrm2.
DR   GeneTree; ENSGT00580000081375; -.
DR   HOGENOM; HBG282546; -.
DR   HOVERGEN; HBG093999; -.
DR   InParanoid; Q8BTI8; -.
DR   OrthoDB; EOG476K1K; -.
DR   NextBio; 344335; -.
DR   ArrayExpress; Q8BTI8; -.
DR   Bgee; Q8BTI8; -.
DR   CleanEx; MM_SRRM2; -.
DR   Genevestigator; Q8BTI8; -.
DR   GermOnline; ENSMUSG00000039218; Mus musculus.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR013170; mRNA_splic_Cwf21.
DR   Pfam; PF08312; cwf21; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil;
KW   Direct protein sequencing; mRNA processing; mRNA splicing; Nucleus;
KW   Phosphoprotein; Spliceosome.
FT   CHAIN         1   2703       Serine/arginine repetitive matrix protein
FT                                2.
FT                                /FTId=PRO_0000248155.
FT   REGION      197    259       Sufficient for RNA-binding (By
FT                                similarity).
FT   COILED       60     92       Potential.
FT   COMPBIAS    186    246       Lys-rich.
FT   COMPBIAS    200   2702       Ser-rich.
FT   COMPBIAS    348    445       Pro-rich.
FT   COMPBIAS    478    772       Arg-rich.
FT   COMPBIAS   1622   2041       Arg-rich.
FT   COMPBIAS   2134   2260       Ala-rich.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      37     37       N6-acetyllysine (By similarity).
FT   MOD_RES     142    142       Phosphoserine (By similarity).
FT   MOD_RES     145    145       Phosphotyrosine (By similarity).
FT   MOD_RES     169    169       N6-acetyllysine (By similarity).
FT   MOD_RES     250    250       Phosphoserine (By similarity).
FT   MOD_RES     252    252       Phosphothreonine (By similarity).
FT   MOD_RES     274    274       Phosphothreonine (By similarity).
FT   MOD_RES     295    295       Phosphoserine (By similarity).
FT   MOD_RES     322    322       Phosphoserine (By similarity).
FT   MOD_RES     323    323       Phosphoserine (By similarity).
FT   MOD_RES     349    349       Phosphoserine.
FT   MOD_RES     351    351       Phosphoserine.
FT   MOD_RES     356    356       Phosphoserine (By similarity).
FT   MOD_RES     357    357       Phosphothreonine (By similarity).
FT   MOD_RES     365    365       Phosphothreonine (By similarity).
FT   MOD_RES     375    375       Phosphoserine (By similarity).
FT   MOD_RES     385    385       Phosphoserine (By similarity).
FT   MOD_RES     393    393       Phosphoserine (By similarity).
FT   MOD_RES     396    396       Phosphoserine (By similarity).
FT   MOD_RES     398    398       Phosphothreonine (By similarity).
FT   MOD_RES     402    402       Phosphoserine.
FT   MOD_RES     406    406       Phosphoserine.
FT   MOD_RES     413    413       Phosphoserine (By similarity).
FT   MOD_RES     416    416       Phosphoserine (By similarity).
FT   MOD_RES     422    422       Phosphoserine (By similarity).
FT   MOD_RES     426    426       Phosphothreonine (By similarity).
FT   MOD_RES     433    433       Phosphoserine.
FT   MOD_RES     434    434       Phosphoserine.
FT   MOD_RES     435    435       Phosphoserine.
FT   MOD_RES     438    438       Phosphoserine.
FT   MOD_RES     470    470       Phosphoserine.
FT   MOD_RES     472    472       Phosphoserine.
FT   MOD_RES     531    531       Phosphoserine.
FT   MOD_RES     533    533       Phosphoserine.
FT   MOD_RES     622    622       Phosphoserine.
FT   MOD_RES     624    624       Phosphothreonine.
FT   MOD_RES     626    626       Phosphoserine.
FT   MOD_RES     753    753       Phosphoserine (By similarity).
FT   MOD_RES     757    757       Phosphoserine (By similarity).
FT   MOD_RES     759    759       Phosphoserine (By similarity).
FT   MOD_RES     761    761       Phosphoserine (By similarity).
FT   MOD_RES     762    762       Phosphoserine (By similarity).
FT   MOD_RES     769    769       Phosphoserine (By similarity).
FT   MOD_RES     773    773       Phosphoserine.
FT   MOD_RES     775    775       Phosphoserine.
FT   MOD_RES     778    778       Phosphoserine.
FT   MOD_RES     821    821       Phosphoserine (By similarity).
FT   MOD_RES     823    823       Phosphothreonine.
FT   MOD_RES     841    841       Phosphothreonine (By similarity).
FT   MOD_RES     846    846       Phosphoserine (By similarity).
FT   MOD_RES     850    850       Phosphoserine (By similarity).
FT   MOD_RES     851    851       Phosphoserine (By similarity).
FT   MOD_RES     858    858       Phosphoserine (By similarity).
FT   MOD_RES     860    860       Phosphothreonine (By similarity).
FT   MOD_RES     865    865       Phosphoserine (By similarity).
FT   MOD_RES     869    869       Phosphoserine (By similarity).
FT   MOD_RES     870    870       Phosphoserine (By similarity).
FT   MOD_RES     875    875       Phosphoserine (By similarity).
FT   MOD_RES     877    877       Phosphothreonine (By similarity).
FT   MOD_RES     882    882       Phosphoserine (By similarity).
FT   MOD_RES     888    888       Phosphoserine (By similarity).
FT   MOD_RES     898    898       Phosphoserine.
FT   MOD_RES     924    924       Phosphoserine.
FT   MOD_RES     926    926       Phosphoserine.
FT   MOD_RES     928    928       Phosphoserine.
FT   MOD_RES     944    944       Phosphoserine.
FT   MOD_RES     945    945       Phosphoserine.
FT   MOD_RES     946    946       Phosphoserine.
FT   MOD_RES     955    955       Phosphothreonine (By similarity).
FT   MOD_RES     962    962       Phosphoserine (By similarity).
FT   MOD_RES     964    964       Phosphoserine (By similarity).
FT   MOD_RES     966    966       Phosphotyrosine (By similarity).
FT   MOD_RES     973    973       Phosphothreonine.
FT   MOD_RES     984    984       Phosphoserine (By similarity).
FT   MOD_RES    1032   1032       Phosphothreonine (By similarity).
FT   MOD_RES    1037   1037       Phosphoserine (By similarity).
FT   MOD_RES    1038   1038       Phosphoserine (By similarity).
FT   MOD_RES    1048   1048       Phosphoserine (By similarity).
FT   MOD_RES    1068   1068       Phosphoserine.
FT   MOD_RES    1097   1097       Phosphoserine (By similarity).
FT   MOD_RES    1115   1115       Phosphoserine (By similarity).
FT   MOD_RES    1117   1117       Phosphoserine (By similarity).
FT   MOD_RES    1149   1149       N6-acetyllysine (By similarity).
FT   MOD_RES    1151   1151       Phosphoserine.
FT   MOD_RES    1175   1175       Phosphoserine (By similarity).
FT   MOD_RES    1209   1209       Phosphoserine.
FT   MOD_RES    1216   1216       Phosphoserine.
FT   MOD_RES    1229   1229       Phosphoserine (By similarity).
FT   MOD_RES    1230   1230       Phosphoserine (By similarity).
FT   MOD_RES    1276   1276       Phosphoserine (By similarity).
FT   MOD_RES    1278   1278       Phosphoserine.
FT   MOD_RES    1284   1284       Phosphoserine (By similarity).
FT   MOD_RES    1287   1287       Phosphoserine (By similarity).
FT   MOD_RES    1305   1305       Phosphoserine.
FT   MOD_RES    1334   1334       Phosphoserine.
FT   MOD_RES    1338   1338       Phosphoserine.
FT   MOD_RES    1339   1339       Phosphoserine.
FT   MOD_RES    1340   1340       Phosphoserine.
FT   MOD_RES    1343   1343       Phosphoserine.
FT   MOD_RES    1359   1359       Phosphoserine.
FT   MOD_RES    1360   1360       Phosphoserine.
FT   MOD_RES    1376   1376       Phosphoserine.
FT   MOD_RES    1377   1377       Phosphoserine.
FT   MOD_RES    1378   1378       Phosphoserine.
FT   MOD_RES    1380   1380       Phosphoserine.
FT   MOD_RES    1397   1397       Phosphoserine (By similarity).
FT   MOD_RES    1399   1399       Phosphoserine (By similarity).
FT   MOD_RES    1400   1400       Phosphoserine (By similarity).
FT   MOD_RES    1409   1409       Phosphothreonine (By similarity).
FT   MOD_RES    1414   1414       Phosphoserine.
FT   MOD_RES    1423   1423       N6-acetyllysine (By similarity).
FT   MOD_RES    1434   1434       Phosphoserine.
FT   MOD_RES    1438   1438       Phosphoserine.
FT   MOD_RES    1439   1439       Phosphoserine.
FT   MOD_RES    1448   1448       Phosphothreonine.
FT   MOD_RES    1453   1453       Phosphoserine.
FT   MOD_RES    1455   1455       Phosphoserine (By similarity).
FT   MOD_RES    1457   1457       Phosphoserine (By similarity).
FT   MOD_RES    1458   1458       Phosphoserine.
FT   MOD_RES    1467   1467       Phosphothreonine (By similarity).
FT   MOD_RES    1473   1473       Phosphoserine (By similarity).
FT   MOD_RES    1475   1475       Phosphoserine (By similarity).
FT   MOD_RES    1478   1478       Phosphoserine (By similarity).
FT   MOD_RES    1487   1487       Phosphothreonine (By similarity).
FT   MOD_RES    1497   1497       Phosphoserine (By similarity).
FT   MOD_RES    1508   1508       Phosphoserine.
FT   MOD_RES    1513   1513       Phosphoserine.
FT   MOD_RES    1515   1515       Phosphoserine.
FT   MOD_RES    1533   1533       Phosphoserine.
FT   MOD_RES    1535   1535       Phosphoserine.
FT   MOD_RES    1537   1537       Phosphoserine.
FT   MOD_RES    1538   1538       Phosphoserine.
FT   MOD_RES    1545   1545       Phosphoserine.
FT   MOD_RES    1548   1548       Phosphoserine.
FT   MOD_RES    1552   1552       Phosphoserine.
FT   MOD_RES    1556   1556       Phosphoserine (By similarity).
FT   MOD_RES    1557   1557       Phosphoserine (By similarity).
FT   MOD_RES    1572   1572       Phosphoserine.
FT   MOD_RES    1574   1574       Phosphothreonine.
FT   MOD_RES    1576   1576       Phosphoserine.
FT   MOD_RES    1577   1577       Phosphoserine.
FT   MOD_RES    1631   1631       Phosphoserine.
FT   MOD_RES    1654   1654       Phosphothreonine.
FT   MOD_RES    1683   1683       Phosphoserine (By similarity).
FT   MOD_RES    1687   1687       Phosphoserine (By similarity).
FT   MOD_RES    1718   1718       Phosphoserine.
FT   MOD_RES    1720   1720       Phosphoserine.
FT   MOD_RES    1747   1747       Phosphoserine.
FT   MOD_RES    1749   1749       Phosphoserine.
FT   MOD_RES    1798   1798       Phosphoserine.
FT   MOD_RES    1800   1800       Phosphothreonine.
FT   MOD_RES    1813   1813       Phosphoserine.
FT   MOD_RES    1822   1822       Phosphoserine.
FT   MOD_RES    1834   1834       Phosphoserine (By similarity).
FT   MOD_RES    1836   1836       Phosphothreonine (By similarity).
FT   MOD_RES    1844   1844       Phosphoserine.
FT   MOD_RES    1846   1846       Phosphoserine.
FT   MOD_RES    1849   1849       Phosphoserine.
FT   MOD_RES    1864   1864       Phosphoserine.
FT   MOD_RES    1866   1866       Phosphoserine.
FT   MOD_RES    1869   1869       Phosphoserine.
FT   MOD_RES    1910   1910       Phosphoserine.
FT   MOD_RES    1912   1912       Phosphoserine.
FT   MOD_RES    1914   1914       Phosphothreonine.
FT   MOD_RES    1927   1927       Phosphoserine (By similarity).
FT   MOD_RES    1958   1958       Phosphoserine.
FT   MOD_RES    1960   1960       Phosphoserine.
FT   MOD_RES    1962   1962       Phosphothreonine.
FT   MOD_RES    1963   1963       Phosphoserine.
FT   MOD_RES    1982   1982       Phosphoserine.
FT   MOD_RES    1984   1984       Phosphoserine.
FT   MOD_RES    1986   1986       Phosphothreonine.
FT   MOD_RES    1994   1994       Phosphoserine.
FT   MOD_RES    1996   1996       Phosphoserine.
FT   MOD_RES    1998   1998       Phosphoserine.
FT   MOD_RES    2019   2019       Phosphoserine.
FT   MOD_RES    2021   2021       Phosphothreonine.
FT   MOD_RES    2023   2023       Phosphoserine.
FT   MOD_RES    2052   2052       Phosphoserine.
FT   MOD_RES    2054   2054       Phosphoserine.
FT   MOD_RES    2056   2056       Phosphothreonine.
FT   MOD_RES    2073   2073       Phosphoserine.
FT   MOD_RES    2075   2075       Phosphoserine (By similarity).
FT   MOD_RES    2077   2077       Phosphothreonine (By similarity).
FT   MOD_RES    2084   2084       Phosphoserine (By similarity).
FT   MOD_RES    2096   2096       Phosphothreonine (By similarity).
FT   MOD_RES    2224   2224       Phosphoserine.
FT   MOD_RES    2241   2241       Phosphothreonine (By similarity).
FT   MOD_RES    2268   2268       Phosphothreonine (By similarity).
FT   MOD_RES    2281   2281       Phosphothreonine (By similarity).
FT   MOD_RES    2335   2335       Phosphoserine.
FT   MOD_RES    2347   2347       Phosphoserine (By similarity).
FT   MOD_RES    2350   2350       Phosphothreonine (By similarity).
FT   MOD_RES    2351   2351       Phosphoserine.
FT   MOD_RES    2360   2360       Phosphoserine.
FT   MOD_RES    2362   2362       Phosphothreonine.
FT   MOD_RES    2365   2365       Phosphoserine (By similarity).
FT   MOD_RES    2381   2381       Phosphoserine.
FT   MOD_RES    2391   2391       Phosphoserine (By similarity).
FT   MOD_RES    2404   2404       Phosphoserine.
FT   MOD_RES    2408   2408       Phosphoserine (By similarity).
FT   MOD_RES    2537   2537       Phosphothreonine.
FT   MOD_RES    2553   2553       Phosphothreonine (By similarity).
FT   MOD_RES    2618   2618       Phosphoserine.
FT   MOD_RES    2629   2629       Phosphoserine (By similarity).
FT   MOD_RES    2631   2631       Phosphoserine (By similarity).
FT   MOD_RES    2638   2638       Phosphoserine.
FT   MOD_RES    2642   2642       Phosphoserine.
FT   MOD_RES    2644   2644       Phosphoserine.
FT   MOD_RES    2646   2646       Phosphoserine.
FT   MOD_RES    2647   2647       Phosphotyrosine.
FT   MOD_RES    2648   2648       Phosphoserine.
FT   MOD_RES    2656   2656       Phosphoserine.
FT   MOD_RES    2660   2660       Phosphoserine.
FT   MOD_RES    2689   2689       Phosphothreonine (By similarity).
FT   MOD_RES    2691   2691       Phosphoserine (By similarity).
FT   VAR_SEQ       1     96       Missing (in isoform 2).
FT                                /FTId=VSP_020188.
FT   VAR_SEQ    2486   2585       Missing (in isoform 3).
FT                                /FTId=VSP_020189.
FT   CONFLICT   1255   1255       G -> E (in Ref. 4; BAC65530).
FT   CONFLICT   1835   1835       I -> R (in Ref. 4; BAC65530).
FT   CONFLICT   2628   2628       G -> R (in Ref. 2; AAH27781 and 4;
FT                                BAC65530).
SQ   SEQUENCE   2703 AA;  294675 MW;  3EAF49A0BE950214 CRC64;
     MYNGIGLPTP RGSGTNGYVQ RNLSLVRGRR GERPDYKGEE ELRHLEAALV KRPNPDILDH
     ERKRRVELRC LELEEMMEEQ GYEEQQIQEK VATFRLMLLE KDVNPGAKEE TPGQRPVVTE
     THQLAELNEK KNERLRAAFG ISDSYVDGSS FDPQRRAREA KQIAPEPPKP YSLVRETSSS
     RSPTPKQKKK KKKKDRGRRS ESSSPRRERK KSSKKKKHRS ESESKKRKHR SPTPKSKRKS
     KDKKRKRSRS TTPAPKSRRA HRSTSADSAS SSDTSRSRSR SAAAKIHTTA LTGQSPPLAS
     GHQGEGDAPS VEPGATNIQQ PSSPAPSTKQ SSSPYEDKDK KEKSAVRPSP SPERSSTGPE
     LPAPTPLLVE QHDDSPRPLA AIPSSQEPVN PSSEASPTRG CSPPKSPEKP PQSTSSESCP
     PSPQPTKVSR HASSSPESLK PTPAPGSRRE ISSSPTSKNR SHGRAKRDKS HSHTPSHRAG
     RSRSPATKRG RSRSRTPTKR GHSRSRSPQW RRSRSAQRWG KSRSPQRRGR SRSPQRPGWS
     RSRNTQRRGR SRSARRGRSH SRSPATRGRS RSRTPARRGR SRSRTPARRR SRSRTPARRR
     SRSRTPARRG RSRSRTPTRR RSRTRSPVRR RSRSRSQARR SGRSRSRTPA RRSGRSRSRT
     PARRGRSRSR TPARRSARSR SRTPARRGRS RSRTPARRRS RSRSLVRRGR SHSRTPQRRG
     RSGSSSERKN KSRTSQRRSR SNSSPEMKKS HVSSRRSRSL SSPRSKAKSL RRSLSGSSPC
     PKQKSQTPTR RSRSGSSPPK QKSKTPPRQS RSNSPQPKVK SGTPPRPGSV TNMQADECTA
     TPQRQSHSES SPDGEVKSRT PSRQSCSGSS PRVKSSTPPR QSPSRSSSPQ PKVKTVISPR
     GRSHSSSSSP SPSRVTSRTP QRKSRSVSPC PKVDSRLRHS RSRSSSPDSK MELGTPLRHS
     GSTSPYPKSM LQTPPDQNLS GSKSPCPQKS RDSPTGSSGS FHLCPGVTPS SIVPGESCFS
     ASFVQQKGHT QTWPDTSSPE VMQTQVESPL LQSKSQTSPK GSLSRSSSPV TELTARSPVK
     QDKSEISTDP KLKSGMSPEQ SKTKPDSSIY PLVDSKSFLV QSRLEPSELK ERLGLIQEDV
     ASSCIPRDKF SPTQDRPESS TVLKVTPRVL LKERSGAGSP PGKRDQKSLL PNSSQDELME
     VEKSEQPLSQ VLPSLSPEHK EMPGSNIESS PEVEERPAVL SALDQSQSQP SKAAGTPAVA
     SCWSGPQVSP EHKELSHSPP RENSFESSLE FKNSGPVSEV NTGFSPEVKE ELNGSFLNQT
     EADPSVDMKE QSRSSRRSSS ELSPEVVEKV GLFSSQKVSS PVLETVQQRT PSRERSSSAS
     PELKDGLPRT PSRRSRSGSS PGLRDGSGTP SRHSLSGSSP GMKDTPQTPS RGRSECDSSP
     EPKALPQTPR ARSHSPSSPE RNNKSVTPQR ERSGSESSVE QKNLARTSPG QRSRSGSSQE
     LDGKPSASPQ ERSESDSSPD SKPKTRTPLR QRSHSGSSPE VDSKSRHSPR LSRSGSSPEM
     KDKPRVLQRA QSGTDSSPEH KIPAPRALPR HSRSGSSSKE RGPSPEGSSS SESSPEHAPK
     SRTARRGSRS SIEPKTKSRT PPRRRSSRSS PELTRKARVS RRSRSASSSP EIRSRTPPRR
     RRSPSVSSPE PTEKSRSSRR RRSVSSPRTK TTSRRGRSPS PKPRGLQRSR SRSRREKTRT
     TRRRDRSGSS QSTSRRRQRS RSRSRVTRRR RGGSGYHSRS PTRQESSRTS SRRRRGRSRT
     PLTSRKRSRS RTSPAPWKRS RSRASPATHR RSRSITPLIS RRRSRSRTSP VSRRRSRSVN
     RRRSRSRASP VSRRRSRSRT PPVTRRRSRS RTPTRRRSRS RTPPVTRRRS RSRTPPVTRR
     RSRSRTSPVT RRRSRSRTSP VTRRRSRSRT SPVTRRRSRS RTSPVTRRRS RSRTPPAIRR
     RSRSRTPLLP RKRSRSRSPL AIRRRSRSRT PRAARGKRSL TRSPPAIRRR SASGSSSDRS
     RSATPPATRN HSGSRTPPVA LSSSRMSCFS RPSMSPTPLD RCRSPGMLEP LGSARTPMSV
     LQQTGGSMMD GPGPRIPDHP RSSVPENHAQ SRIALALTAI SLGTARPPPS MSAAGLAARM
     SQVPAPVPLM SLRTAPAANL ASRIPAASAA AMNLASARTS AIPASVNLAD SRTPAAAAAM
     NLASPRTAVA PSAVNLADPR TPAASAVNLA GARTPAALAA LSLTGSGTPP TAANYPSSSR
     TPQAPTPANL VVGPRSAHGT APVNIAGSRT PAGLAPTNLS SSRMAPALSG ANLTSPRVPL
     SAYDRVSGRT SPLMLDRARS RTPPSAPSQS RMTSERERAP SPASRMVQAS SQSLLPPAQD
     RPRSPVPSAF SDQSRSVAQT TPVAGSQSLS SGTVAKSTSS ASDHNGMLSG PAPGISHAEG
     GEPPASTGAQ QPSTLAALQP AKERRSSSSS SSSSSSSSSS SSSSSSSSSS GSSSSDSEGS
     SLPAQPEVAL KRVPSPTPVP KEAIREGRPQ EPTPAKRKRR SSSSSSSSSS SSSSSSSSSS
     SSSSSSSSSS SSSSSSSSSS SSPSPAKPGP QALPKPASPK KPPPGERGSR SPRKPIDSLR
     DSRSLSYSPV ERRQPSPQPS PRDLQSSERV SWRGQRGDSH SPGHKRKETP SPRSNRHRSS
     RSP
//
ID   CPSF7_MOUSE             Reviewed;         471 AA.
AC   Q8BTV2; Q3TNF1; Q8BKE7; Q8CFS8;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 2.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Cleavage and polyadenylation specificity factor subunit 7;
GN   Name=Cpsf7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Eye, Spleen, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Probable component of the cleavage factor Im complex
CC       (CFIm) that plays a key role in pre-mRNA 3' processing. Binds to
CC       cleavage and polyadenylation RNA substrates (By similarity).
CC   -!- SUBUNIT: Probable component of the cleavage factor Im (CFIm)
CC       complex, composed at least of NUDT21/CPSF5 and CPSF6 or CPSF7 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BTV2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BTV2-2; Sequence=VSP_017196;
CC       Name=3;
CC         IsoId=Q8BTV2-3; Sequence=VSP_017195;
CC   -!- SIMILARITY: Belongs to the RRM CPSF6/7 family.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK053375; BAC35368.1; -; mRNA.
DR   EMBL; AK165330; BAE38138.1; -; mRNA.
DR   EMBL; AK088603; BAC40447.1; -; mRNA.
DR   EMBL; BC038812; AAH38812.1; -; mRNA.
DR   IPI; IPI00225249; -.
DR   IPI; IPI00720126; -.
DR   IPI; IPI00720208; -.
DR   RefSeq; NP_001157744.1; NM_001164272.1.
DR   RefSeq; NP_758506.3; NM_172302.3.
DR   UniGene; Mm.31236; -.
DR   ProteinModelPortal; Q8BTV2; -.
DR   SMR; Q8BTV2; 82-177.
DR   STRING; Q8BTV2; -.
DR   PhosphoSite; Q8BTV2; -.
DR   PRIDE; Q8BTV2; -.
DR   Ensembl; ENSMUST00000038379; ENSMUSP00000038958; ENSMUSG00000034820.
DR   GeneID; 269061; -.
DR   KEGG; mmu:269061; -.
DR   UCSC; uc008gpw.1; mouse.
DR   UCSC; uc008gpz.1; mouse.
DR   UCSC; uc008gqa.1; mouse.
DR   CTD; 269061; -.
DR   MGI; MGI:1917826; Cpsf7.
DR   eggNOG; roNOG09253; -.
DR   GeneTree; ENSGT00600000084083; -.
DR   HOGENOM; HBG505348; -.
DR   HOVERGEN; HBG056699; -.
DR   InParanoid; Q8BTV2; -.
DR   OMA; MKASTPY; -.
DR   OrthoDB; EOG44BB2Q; -.
DR   PhylomeDB; Q8BTV2; -.
DR   NextBio; 392668; -.
DR   PMAP-CutDB; Q8BTV2; -.
DR   ArrayExpress; Q8BTV2; -.
DR   Bgee; Q8BTV2; -.
DR   CleanEx; MM_5730453I16RIK; -.
DR   Genevestigator; Q8BTV2; -.
DR   GermOnline; ENSMUSG00000034820; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; mRNA processing; Nucleus; Phosphoprotein;
KW   RNA-binding.
FT   CHAIN         1    471       Cleavage and polyadenylation specificity
FT                                factor subunit 7.
FT                                /FTId=PRO_0000081528.
FT   DOMAIN       82    162       RRM.
FT   COMPBIAS     51     54       Poly-Pro.
FT   COMPBIAS    218    329       Pro-rich.
FT   COMPBIAS    418    469       Arg-rich.
FT   MOD_RES      48     48       Phosphoserine (By similarity).
FT   MOD_RES      72     72       Phosphotyrosine (By similarity).
FT   MOD_RES      73     73       Phosphothreonine (By similarity).
FT   MOD_RES     197    197       Phosphoserine (By similarity).
FT   MOD_RES     203    203       Phosphothreonine.
FT   MOD_RES     413    413       Phosphoserine (By similarity).
FT   MOD_RES     423    423       Phosphoserine (By similarity).
FT   MOD_RES     429    429       Phosphoserine (By similarity).
FT   VAR_SEQ       1    234       Missing (in isoform 3).
FT                                /FTId=VSP_017195.
FT   VAR_SEQ     176    184       Missing (in isoform 2).
FT                                /FTId=VSP_017196.
FT   CONFLICT    262    262       H -> Q (in Ref. 1; BAC40447).
SQ   SEQUENCE   471 AA;  52011 MW;  3ACC0F1FF7224109 CRC64;
     MSEGVDLIDI YADEEFNQDS EFNNTDQIDL YDDVLTAASQ PSDDRSSSTE PPPPVRQEPA
     PKPNNKTPAI LYTYSGLRSR RAAVYVGSFS WWTTDQQLIQ VIRSIGVYDV VELKFAENRA
     NGQSKGYAEV VVASENSVHK LLELLPGKVL NGEKVDVRPA TRQNLSQFEA QARKRECVRV
     PRGGIPPRAH SRDSSDSADG RATPSENLVP SSARVDKPPS VLPYFNRPPS ALPLMGLPPP
     PIPPPPPLSS SFGVPPPPPG IHYQHLMPPP PRLPPHLAVP PPGAIPPALH LNPAFFPPPN
     ATVGPPPDTY MKASTPYNHH GSRDSGPPPS TVSEAEFEEI MKRNRAISSS AISKAVSGAS
     AGDYSDAIET LLTAIAVIKQ SRVANDERCR VLISSLKDCL HGIEAKSYSV GASGSSSRKR
     HRSRERSPSR SRESSRRHRD LLHNEDRHDD YFQERNREHE RHRDRERDRH H
//
ID   PAK4_MOUSE              Reviewed;         593 AA.
AC   Q8BTW9; Q6ZPX0; Q80Z97; Q9CS71;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Serine/threonine-protein kinase PAK 4;
DE            EC=2.7.11.1;
DE   AltName: Full=p21-activated kinase 4;
DE            Short=PAK-4;
GN   Name=Pak4; Synonyms=Kiaa1142;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH FGFR2 AND GRB2, AND
RP   PHOSPHORYLATION AT TYROSINE RESIDUES.
RC   STRAIN=BALB/c;
RX   MEDLINE=22526742; PubMed=12529371; DOI=10.1074/jbc.M205875200;
RA   Lu Y., Pan Z.-Z., Devaux Y., Ray P.;
RT   "p21-activated protein kinase 4 (PAK4) interacts with the keratinocyte
RT   growth factor receptor and participates in keratinocyte growth factor-
RT   mediated inhibition of oxidant-induced cell death.";
RL   J. Biol. Chem. 278:10374-10380(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Embryo, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Activates the JNK pathway. Plays a role in the
CC       reorganization of the actin cytoskeleton and in the formation of
CC       filopodia. Phosphorylates and inactivates the protein phosphatase
CC       SSH1, leading to increased inhibitory phosphorylation of the actin
CC       binding/depolymerizing factor cofilin. Decreased cofilin activity
CC       may lead to stabilization of actin filaments. Phosphorylates
CC       ARHGEF2 (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts tightly with GTP-bound but not GDP-bound
CC       CDC42/p21 and weakly with RAC1. Interacts with its substrate
CC       ARHGEF2 (By similarity). Interacts with FGFR2 and GRB2.
CC   -!- PTM: Autophosphorylated on serine residues when activated by
CC       CDC42/p21 (By similarity).
CC   -!- PTM: Phosphorylated on tyrosine residues upon stimulation of
CC       FGFR2.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC   -!- SIMILARITY: Contains 1 CRIB domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98108.2; Type=Erroneous initiation;
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DR   EMBL; AY217016; AAO61496.1; -; mRNA.
DR   EMBL; AK129298; BAC98108.2; ALT_INIT; mRNA.
DR   EMBL; AK017713; BAB30889.1; -; mRNA.
DR   EMBL; AK088512; BAC40396.1; -; mRNA.
DR   EMBL; BC048238; AAH48238.1; -; mRNA.
DR   IPI; IPI00467379; -.
DR   RefSeq; NP_081746.1; NM_027470.3.
DR   UniGene; Mm.21876; -.
DR   ProteinModelPortal; Q8BTW9; -.
DR   SMR; Q8BTW9; 10-44, 302-591.
DR   STRING; Q8BTW9; -.
DR   PhosphoSite; Q8BTW9; -.
DR   PRIDE; Q8BTW9; -.
DR   Ensembl; ENSMUST00000032823; ENSMUSP00000032823; ENSMUSG00000030602.
DR   Ensembl; ENSMUST00000108283; ENSMUSP00000103918; ENSMUSG00000030602.
DR   GeneID; 70584; -.
DR   KEGG; mmu:70584; -.
DR   UCSC; uc009fzh.1; mouse.
DR   CTD; 70584; -.
DR   MGI; MGI:1917834; Pak4.
DR   eggNOG; maNOG18163; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108518; -.
DR   InParanoid; Q8BTW9; -.
DR   OMA; VDPACIT; -.
DR   OrthoDB; EOG4RNB7X; -.
DR   PhylomeDB; Q8BTW9; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 331922; -.
DR   ArrayExpress; Q8BTW9; -.
DR   Bgee; Q8BTW9; -.
DR   CleanEx; MM_PAK4; -.
DR   Genevestigator; Q8BTW9; -.
DR   GermOnline; ENSMUSG00000030602; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000095; PAK_box_Rho-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00786; PBD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00285; PBD; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    593       Serine/threonine-protein kinase PAK 4.
FT                                /FTId=PRO_0000086475.
FT   DOMAIN       11     24       CRIB.
FT   DOMAIN      323    574       Protein kinase.
FT   NP_BIND     329    337       ATP (By similarity).
FT   REGION       25    322       Linker.
FT   ACT_SITE    442    442       Proton acceptor (By similarity).
FT   BINDING     352    352       ATP (By similarity).
FT   MOD_RES      41     41       Phosphoserine (By similarity).
FT   MOD_RES      99     99       Phosphoserine (By similarity).
FT   MOD_RES     104    104       Phosphoserine (By similarity).
FT   MOD_RES     142    142       Phosphoserine (By similarity).
FT   MOD_RES     148    148       Phosphoserine (By similarity).
FT   MOD_RES     181    181       Phosphoserine.
FT   MOD_RES     187    187       Phosphothreonine (By similarity).
FT   MOD_RES     195    195       Phosphoserine (By similarity).
FT   MOD_RES     207    207       Phosphothreonine (By similarity).
FT   MOD_RES     257    257       Phosphoserine (By similarity).
FT   MOD_RES     266    266       Phosphoserine (By similarity).
FT   MOD_RES     293    293       Phosphoserine (By similarity).
FT   MOD_RES     476    476       Phosphoserine; by autocatalysis.
FT   CONFLICT      5      5       K -> R (in Ref. 1; AAO61496).
FT   CONFLICT    248    248       P -> L (in Ref. 1; AAO61496).
FT   CONFLICT    564    564       T -> P (in Ref. 4; BAB30889).
SQ   SEQUENCE   593 AA;  64623 MW;  4AFA91DD73D4C6D5 CRC64;
     MFGKKKKRVE ISAPSNFEHR VHTGFDQHEQ KFTGLPRQWQ SLIEESARRP KPLIDPACIT
     SIQPGAPKTI VRGSKGAKDG ALTLLLDEFE NMSVTRSNSL RRESPPPPAR AHQENGMLEE
     RAAPARMAPD KAGSRARATG HSEAGSGSGD RRRVGPEKRP KSSRDGPGGP QEASRDKRPL
     SGPDVSTPQP GSLTSGTKLA AGRPFNTYPR ADTDHPPRGA QGEPHTMAPN GPSATGLAAP
     QSSSSSRPPT RARGAPSPGV LGPHASEPQL APPARALAAP AVPPAPGPPG PRSPQREPQR
     VSHEQFRAAL QLVVDPGDPR SYLDNFIKIG EGSTGIVCIA TVRSSGKLVA VKKMDLRKQQ
     RRELLFNEVV IMRDYRHENV VEMYNSYLVG DELWVVMEFL EGGALTDIVT HTRMNEEQIA
     AVCLAVLQAL AVLHAQGVIH RDIKSDSILL THDGRVKLSD FGFCAQVSKE VPRRKSLVGT
     PYWMAPELIS RLPYGPEVDI WSLGVMVIEM VDGEPPYFNE PPLKAMKMIR DNLPPRLKNL
     HKASPSLKGF LDRLLVRDPA QRATAAELLK HPFLTKAGPP ASIVPLMRQH RTR
//
ID   S4A7_MOUSE              Reviewed;        1034 AA.
AC   Q8BTY2; Q3U5H7;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 2.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Sodium bicarbonate cotransporter 3;
DE   AltName: Full=Solute carrier family 4 member 7;
GN   Name=Slc4a7; Synonyms=Nbc3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-932 (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 826-1034 (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH CFTR AND SLC9A3R1.
RX   PubMed=12403779; DOI=10.1074/jbc.M201862200;
RA   Park M., Ko S.B.H., Choi J.Y., Muallem G., Thomas P.J., Pushkin A.,
RA   Lee M.-S., Kim J.Y., Lee M.G., Muallem S., Kurtz I.;
RT   "The cystic fibrosis transmembrane conductance regulator interacts
RT   with and regulates the activity of the HCO3- salvage transporter human
RT   Na+-HCO3-cotransport isoform 3.";
RL   J. Biol. Chem. 277:50503-50509(2002).
RN   [4]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=12808454; DOI=10.1038/ng1176;
RA   Bok D., Galbraith G., Lopez I., Woodruff M., Nusinowitz S.,
RA   BeltrandelRio H., Huang W., Zhao S., Geske R., Montgomery C.,
RA   van Sligtenhorst I., Friddle C., Platt K., Sparks M.J., Pushkin A.,
RA   Abuladze N., Ishiyama A., Dukkipati R., Liu W., Kurtz I.;
RT   "Blindness and auditory impairment caused by loss of the sodium
RT   bicarbonate cotransporter NBC3.";
RL   Nat. Genet. 34:313-319(2003).
RN   [5]
RP   INTERACTION WITH USH1C, AND TISSUE SPECIFICITY.
RX   PubMed=16301216; DOI=10.1093/hmg/ddi417;
RA   Reiners J., van Wijk E., Maerker T., Zimmermann U., Juergens K.,
RA   te Brinke H., Overlack N., Roepman R., Knipper M., Kremer H.,
RA   Wolfrum U.;
RT   "Scaffold protein harmonin (USH1C) provides molecular links between
RT   Usher syndrome type 1 and type 2.";
RL   Hum. Mol. Genet. 14:3933-3943(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238; SER-247; THR-951;
RP   SER-960 AND SER-1033, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-960, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-654 AND ASN-664, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Electroneutral sodium- and bicarbonate-dependent
CC       cotransporter with a Na(+):HCO3(-) 1:1 stoichiometry. Regulates
CC       intracellular pH and may play a role in bicarbonate salvage in
CC       secretory epithelia. May also have an associated sodium channel
CC       activity.
CC   -!- ENZYME REGULATION: Transporter activity is regulated by
CC       CA2/carbonic anhydrase 2, cAMP and PKA. Insensitive to stilbene
CC       derivatives. May be inhibited by 5-(N-ethyl-N-isopropyl)-amiloride
CC       (EIPA) (By similarity).
CC   -!- SUBUNIT: Forms a complex with ATP6V1B1 and SLC9A3R1/EBP50.
CC       Interacts in a pH dependent-manner with CA2/carbonic anhydrase 2
CC       (By similarity). Interacts with CFTR through SLC9A3R1/EBP50.
CC       Interacts with USH1C.
CC   -!- SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass
CC       membrane protein. Apical cell membrane; Multi-pass membrane
CC       protein (By similarity). Cell projection, stereocilium (By
CC       similarity). Note=Also described at the apical cell membrane.
CC       Localizes to the stereocilia of cochlear outer hair cells and to
CC       the lateral membrane of cochlear inner hair cells (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BTY2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BTY2-2; Sequence=VSP_017166, VSP_017167, VSP_017168;
CC   -!- TISSUE SPECIFICITY: Expressed in the spiral ligament throughout
CC       the cochlea and in photoreceptors of the outer plexiform layer of
CC       the retina (at protein level).
CC   -!- DOMAIN: The PDZ-binding motif mediates interaction with the CFTR,
CC       SLC9A3R1/EBP50 complex and probably with USH1C (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Deafness and blindness due to degeneration
CC       of sensory receptors in internal ear and retina.
CC   -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
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DR   EMBL; AK088400; BAC40330.1; -; mRNA.
DR   EMBL; AK152233; BAE31059.1; -; mRNA.
DR   EMBL; AK153567; BAE32101.1; -; mRNA.
DR   EMBL; CN532915; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00225306; -.
DR   IPI; IPI00664442; -.
DR   UniGene; Mm.258893; -.
DR   ProteinModelPortal; Q8BTY2; -.
DR   SMR; Q8BTY2; 115-419, 460-501, 836-868.
DR   STRING; Q8BTY2; -.
DR   PhosphoSite; Q8BTY2; -.
DR   PRIDE; Q8BTY2; -.
DR   Ensembl; ENSMUST00000057015; ENSMUSP00000058313; ENSMUSG00000021733.
DR   Ensembl; ENSMUST00000090583; ENSMUSP00000088071; ENSMUSG00000021733.
DR   UCSC; uc007sgn.1; mouse.
DR   UCSC; uc007sgo.1; mouse.
DR   MGI; MGI:2443878; Slc4a7.
DR   eggNOG; maNOG22473; -.
DR   GeneTree; ENSGT00560000076851; -.
DR   HOVERGEN; HBG004326; -.
DR   OrthoDB; EOG40GCQ3; -.
DR   PhylomeDB; Q8BTY2; -.
DR   ArrayExpress; Q8BTY2; -.
DR   Bgee; Q8BTY2; -.
DR   Genevestigator; Q8BTY2; -.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0032420; C:stereocilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR011531; HCO3_transpt_C.
DR   InterPro; IPR013769; HCO3_transpt_cyt.
DR   InterPro; IPR003020; HCO3_transpt_euk.
DR   InterPro; IPR003024; Na/HCO3_transpt.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   Gene3D; G3DSA:3.40.1100.10; HCO3_transpt_cyt; 1.
DR   PANTHER; PTHR11453; HCO3_transpt_euk; 1.
DR   Pfam; PF07565; Band_3_cyto; 1.
DR   Pfam; PF00955; HCO3_cotransp; 1.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   PRINTS; PR01232; NAHCO3TRSPRT.
DR   SUPFAM; SSF55804; PTrfase/Anion_transptr; 1.
DR   TIGRFAMs; TIGR00834; ae; 1.
DR   PROSITE; PS00219; ANION_EXCHANGER_1; FALSE_NEG.
DR   PROSITE; PS00220; ANION_EXCHANGER_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cell projection; Glycoprotein;
KW   Ion transport; Membrane; Phosphoprotein; Sodium; Sodium transport;
KW   Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1   1034       Sodium bicarbonate cotransporter 3.
FT                                /FTId=PRO_0000079234.
FT   TOPO_DOM      1    476       Extracellular (Potential).
FT   TRANSMEM    477    497       Helical; (Potential).
FT   TOPO_DOM    498    505       Cytoplasmic (Potential).
FT   TRANSMEM    506    526       Helical; (Potential).
FT   TOPO_DOM    527    563       Extracellular (Potential).
FT   TRANSMEM    564    584       Helical; (Potential).
FT   TOPO_DOM    585    593       Cytoplasmic (Potential).
FT   TRANSMEM    594    614       Helical; (Potential).
FT   TOPO_DOM    615    685       Extracellular (Potential).
FT   TRANSMEM    686    706       Helical; (Potential).
FT   TOPO_DOM    707    729       Cytoplasmic (Potential).
FT   TRANSMEM    730    750       Helical; (Potential).
FT   TOPO_DOM    751    776       Extracellular (Potential).
FT   TRANSMEM    777    797       Helical; (Potential).
FT   TOPO_DOM    798    812       Cytoplasmic (Potential).
FT   TRANSMEM    813    833       Helical; (Potential).
FT   TOPO_DOM    834    876       Extracellular (Potential).
FT   TRANSMEM    877    897       Helical; (Potential).
FT   TOPO_DOM    898   1034       Cytoplasmic (Potential).
FT   REGION      918    920       CA2-binding (By similarity).
FT   MOTIF      1031   1034       PDZ-binding (By similarity).
FT   MOD_RES     238    238       Phosphoserine.
FT   MOD_RES     247    247       Phosphoserine.
FT   MOD_RES     250    250       Phosphoserine (By similarity).
FT   MOD_RES     271    271       Phosphoserine (By similarity).
FT   MOD_RES     275    275       Phosphoserine.
FT   MOD_RES     951    951       Phosphothreonine.
FT   MOD_RES     960    960       Phosphoserine.
FT   MOD_RES    1008   1008       Phosphoserine (By similarity).
FT   MOD_RES    1014   1014       Phosphoserine (By similarity).
FT   MOD_RES    1033   1033       Phosphoserine.
FT   CARBOHYD    176    176       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    274    274       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    644    644       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    654    654       N-linked (GlcNAc...).
FT   CARBOHYD    664    664       N-linked (GlcNAc...).
FT   VAR_SEQ     243    243       G -> GKKHSDPHLLERNG (in isoform 2).
FT                                /FTId=VSP_017166.
FT   VAR_SEQ     815    815       F -> KGAGYHLDLLMVGVMLGVCSIMGLPWFVAATVLSIS
FT                                HVNSLKVESECSAPGEQPKFLGIREQRVTGLMIFILMGLSV
FT                                FMTSVLKVKPLWQCSTILFTLTFILSCKEIKH (in
FT                                isoform 2).
FT                                /FTId=VSP_017167.
FT   VAR_SEQ     816   1034       Missing (in isoform 2).
FT                                /FTId=VSP_017168.
FT   CONFLICT    430    430       G -> D (in Ref. 1; BAC40330).
FT   CONFLICT    717    717       G -> R (in Ref. 1; BAC40330).
SQ   SEQUENCE   1034 AA;  116514 MW;  92B080274D206097 CRC64;
     MEADGAGEQM RPLLTRGPDE EAVVDLGKTS STVNTKFEKE ELESHRAVYV GVHVPFSKES
     RRRHKHRGHK HHHRRRKDKD SDKEDGRESP SYDTPSQRVQ FILGTEDDDE EHIPHDLFTE
     MDELCYRDGE EYEWKETARW LKFEEDVEDG GDRWSKPYVA TLSLHSLFEL RSCILNGTVM
     LDMRASTLDE IADMVLDNMI ASGQLDDSIR ENVREALLKR HHHQNEKRFT SRIPLVRSFA
     DIGILASPQS APGNLDNSKS GEMKGNGSGG SRENSTVDFS KVDMNFMRKI PTGAEASNVL
     VGEVDFLERP IIAFVRLAPA VLLSGLTEVP VPTRFLFLLL GPAGKAPQYH EIGRSIATLM
     TDEIFHDVAY KAKDRNDLLS GIDEFLDQVT VLPPGEWDPS IRIEPPKSVP SQEKRKIPVF
     PNGSAAMSVG PPKEDDHHAG PELQRTGRLF GGLILDIKRK APFFLSDFKD ALSLQCLASI
     LFLYCACMSP VITFGGLLGE ATEGRISAIE SLFGASLTGI AYSLFAGQPL TILGSTGPVL
     VFEKILFKFC RDYHLSYLSL RTSIGLWTSF LCIVLVATDA SSLVCYITRF TEEAFAALIC
     IIFIYEALEK LFHLGEIYAF NMHNNLDELT SYTCVCAEPS NPSNETLELW KRKNITAYSV
     SWGNLTVSEC KTFHGMFVGS ACGPHGPYVP DVLFWCVVLF FTTFFLSSFL KQFKTKGYFP
     TKVRSTISDF AVFLTIVIMV AIDYLVGIPS PKLHVPEKFE PTDPSRGWII SPLGDNPWWT
     LLIAAVPALL CTILIFMDQQ ITAVIINRKE HKLKFIPMPV LYGVFLYMGV SSLKGIQFFD
     RIKLFGMPAK HQPDLIYLRY VPLWKVHVFT VVQLTCLVLL WVIKASAAAV VFPMMVLALV
     FVRKLMDLCF TKRELSWLDD LMPESKKKKE DDKKKKEKEE AERMLQDDED TVHLPFERGS
     LLQIPVKTLK YSIDPSVVNI SDEMAKTAQW KALSMNTENA KVTRPNTSPE KPVSVTINFE
     DEPSKKYMDA ETSL
//
ID   SEC62_MOUSE             Reviewed;         398 AA.
AC   Q8BU14; Q6NX81;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Translocation protein SEC62;
DE   AltName: Full=Translocation protein 1;
DE            Short=TP-1;
GN   Name=Sec62; Synonyms=Tloc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-375, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; THR-158; SER-309;
RP   SER-313; SER-335; THR-343 AND SER-345, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-158 AND THR-375, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-158, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-375, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Required for preprotein translocation (By similarity).
CC   -!- SUBUNIT: Part of a complex that contains SEC61, SEC62 and SEC63
CC       Interacts with SEC61B (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the SEC62 family.
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DR   EMBL; AK088093; BAC40140.1; -; mRNA.
DR   EMBL; BC067202; AAH67202.1; -; mRNA.
DR   IPI; IPI00134398; -.
DR   RefSeq; NP_081292.1; NM_027016.2.
DR   UniGene; Mm.26017; -.
DR   ProteinModelPortal; Q8BU14; -.
DR   STRING; Q8BU14; -.
DR   PhosphoSite; Q8BU14; -.
DR   PRIDE; Q8BU14; -.
DR   Ensembl; ENSMUST00000029256; ENSMUSP00000029256; ENSMUSG00000027706.
DR   GeneID; 69276; -.
DR   KEGG; mmu:69276; -.
DR   UCSC; uc008ovh.1; mouse.
DR   CTD; 69276; -.
DR   MGI; MGI:1916526; Sec62.
DR   HOGENOM; HBG379410; -.
DR   HOVERGEN; HBG055550; -.
DR   InParanoid; Q8BU14; -.
DR   OMA; FEMITRE; -.
DR   OrthoDB; EOG43R3NC; -.
DR   PhylomeDB; Q8BU14; -.
DR   NextBio; 329013; -.
DR   ArrayExpress; Q8BU14; -.
DR   Bgee; Q8BU14; -.
DR   Genevestigator; Q8BU14; -.
DR   GermOnline; ENSMUSG00000027706; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR   GO; GO:0055085; P:transmembrane transport; IEA:UniProtKB-KW.
DR   InterPro; IPR004728; Sec62.
DR   PANTHER; PTHR12443; Sec62; 1.
DR   Pfam; PF03839; Sec62; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Membrane; Phosphoprotein; Protein transport;
KW   Translocation; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    398       Translocation protein SEC62.
FT                                /FTId=PRO_0000206617.
FT   TOPO_DOM      1    196       Cytoplasmic (Potential).
FT   TRANSMEM    197    217       Helical; (Potential).
FT   TOPO_DOM    218    234       Lumenal (Potential).
FT   TRANSMEM    235    255       Helical; (Potential).
FT   TOPO_DOM    256    398       Cytoplasmic (Potential).
FT   MOD_RES     117    117       Phosphoserine.
FT   MOD_RES     158    158       Phosphothreonine.
FT   MOD_RES     309    309       Phosphoserine.
FT   MOD_RES     313    313       Phosphoserine.
FT   MOD_RES     335    335       Phosphoserine.
FT   MOD_RES     343    343       Phosphothreonine.
FT   MOD_RES     345    345       Phosphoserine.
FT   MOD_RES     353    353       Phosphoserine.
FT   MOD_RES     375    375       Phosphothreonine.
FT   CONFLICT     85     85       L -> F (in Ref. 2; AAH67202).
SQ   SEQUENCE   398 AA;  45581 MW;  F91B3E90336FFC9F CRC64;
     MAERRRHKKR IQEVGEPSKE EKAVAKYLRF NCPTKSTNMM GHRVDYFIAS KAVECLLDSK
     WAKAKKGEDA LFTTRESVVD YCNRLLKKQF FHRALKVMKM KYDKDVKKEK DKGKSESGKE
     DDKKSKKESV KEEKTKKEKE KKKDGEKEDS KKEETPGTPK KKETKKKFKL EPHDDQVFLD
     GNEVFVWIYD PVHIKTFVMG LILVIAVIAA TLFPLWPAEM RVGVYYLSVG AGCFVASILL
     LAIARCILFL IIWLITGGRH HFWFLPNLTA DVGFIDSFRP LYTHEYKGPK ADLKKDEKSE
     TKKQQKSDSE EKSDSEKKED EEGKGAPADH GPEGSGGERH SDTDSDRRED DRSQHSSGNG
     NDFEMITKEE LEQQTDGDCD EEDDDKDGEV PKSAHEKS
//
ID   RAP2C_MOUSE             Reviewed;         183 AA.
AC   Q8BU31; Q504Q0; Q6P1Y7; Q810J4; Q8R2P4;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Ras-related protein Rap-2c;
DE   Flags: Precursor;
GN   Name=Rap2c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Embryonic heart, Embryonic liver, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, C57BL/6J, and FVB/N;
RC   TISSUE=Embryo, Eye, Limb, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, PALMITOYLATION, AND MUTAGENESIS OF
RP   CYS-176; CYS-177 AND CYS-180.
RX   PubMed=19061864; DOI=10.1016/j.bbrc.2008.11.107;
RA   Uechi Y., Bayarjargal M., Umikawa M., Oshiro M., Takei K.,
RA   Yamashiro Y., Asato T., Endo S., Misaki R., Taguchi T., Kariya K.;
RT   "Rap2 function requires palmitoylation and recycling endosome
RT   localization.";
RL   Biochem. Biophys. Res. Commun. 378:732-737(2009).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Small GTP-binding protein which cycles between a GDP-
CC       bound inactive and a GTP-bound active form. May play a role in
CC       cytoskeletal rearrangements and regulate cell spreading through
CC       activation of the effector TNIK. May play a role in SRE-mediated
CC       gene transcription.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Recycling
CC       endosome membrane; Lipid-anchor; Cytoplasmic side.
CC   -!- PTM: Palmitoylated. Palmitoylation is required for association
CC       with recycling endosome membranes and activation of TNIK.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK087971; BAC40066.1; -; mRNA.
DR   EMBL; AK146057; BAE26866.1; -; mRNA.
DR   EMBL; AK146956; BAE27564.1; -; mRNA.
DR   EMBL; AK147015; BAE27609.1; -; mRNA.
DR   EMBL; BC027363; AAH27363.3; -; mRNA.
DR   EMBL; BC050056; AAH50056.2; -; mRNA.
DR   EMBL; BC064814; AAH64814.2; -; mRNA.
DR   EMBL; BC094890; AAH94890.1; -; mRNA.
DR   IPI; IPI00466588; -.
DR   RefSeq; NP_766001.1; NM_172413.2.
DR   UniGene; Mm.43152; -.
DR   ProteinModelPortal; Q8BU31; -.
DR   SMR; Q8BU31; 1-167.
DR   PRIDE; Q8BU31; -.
DR   Ensembl; ENSMUST00000053593; ENSMUSP00000058391; ENSMUSG00000050029.
DR   GeneID; 72065; -.
DR   KEGG; mmu:72065; -.
DR   UCSC; uc009tds.1; mouse.
DR   CTD; 72065; -.
DR   MGI; MGI:1919315; Rap2c.
DR   GeneTree; ENSGT00560000076632; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; Q8BU31; -.
DR   OMA; CCTTCIV; -.
DR   OrthoDB; EOG4P2Q3G; -.
DR   PhylomeDB; Q8BU31; -.
DR   NextBio; 460989; -.
DR   ArrayExpress; Q8BU31; -.
DR   Bgee; Q8BU31; -.
DR   CleanEx; MM_RAP2C; -.
DR   Genevestigator; Q8BU31; -.
DR   GermOnline; ENSMUSG00000050029; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0030336; P:negative regulation of cell migration; IDA:MGI.
DR   GO; GO:0031954; P:positive regulation of protein autophosphorylation; IDA:MGI.
DR   GO; GO:0032486; P:Rap protein signal transduction; IDA:UniProtKB.
DR   GO; GO:0061097; P:regulation of protein tyrosine kinase activity; IDA:UniProtKB.
DR   InterPro; IPR003577; GTPase_Ras.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR020849; Ras_small_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00173; RAS; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Endosome; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Palmitate; Phosphoprotein; Prenylation.
FT   CHAIN         1    180       Ras-related protein Rap-2c.
FT                                /FTId=PRO_0000030223.
FT   PROPEP      181    183       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000030224.
FT   NP_BIND      10     17       GTP (By similarity).
FT   NP_BIND      57     61       GTP (By similarity).
FT   NP_BIND     116    119       GTP (By similarity).
FT   MOTIF        32     40       Effector region (Probable).
FT   MOD_RES      66     66       Phosphoserine.
FT   MOD_RES     180    180       Cysteine methyl ester (By similarity).
FT   LIPID       180    180       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   MUTAGEN     176    176       C->G: Loss of association with the
FT                                recycling endosome membranes and loss of
FT                                TNIK activation; when associated with C-
FT                                177.
FT   MUTAGEN     177    177       C->G: Loss of association with the
FT                                recycling endosome membranes and loss of
FT                                TNIK activation; when associated with C-
FT                                176.
FT   MUTAGEN     180    180       C->A: Loss of association with membranes.
FT   CONFLICT     83     83       S -> N (in Ref. 2; AAH27363).
SQ   SEQUENCE   183 AA;  20745 MW;  6763385F76638324 CRC64;
     MREYKVVVLG SGGVGKSALT VQFVTGTFIE KYDPTIEDFY RKEIEVDSSP SVLEILDTAG
     TEQFASMRDL YIKNGQGFIL VYSLVNQQSF QDIKPMRDQI VRVKRYEKVP LILVGNKVDL
     EPEREVMSSE GRALAQEWGC PFMETSAKSK SMVDELFAEI VRQMNYSSLP EKQDQCCTTC
     VVQ
//
ID   Q8BU95_MOUSE            Unreviewed;       153 AA.
AC   Q8BU95;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 47.
DE   SubName: Full=Enoyl Coenzyme A hydratase, short chain, 1, mitochondrial, isoform CRA_c;
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Echs1; ORFNames=mCG_21632;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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DR   EMBL; AK086762; BAC39739.1; -; mRNA.
DR   EMBL; CH466531; EDL17911.1; -; Genomic_DNA.
DR   IPI; IPI00459020; -.
DR   UniGene; Mm.24452; -.
DR   HSSP; P14604; 1MJ3.
DR   ProteinModelPortal; Q8BU95; -.
DR   SMR; Q8BU95; 31-139.
DR   STRING; Q8BU95; -.
DR   PRIDE; Q8BU95; -.
DR   Ensembl; ENSMUST00000026538; ENSMUSP00000026538; ENSMUSG00000025465.
DR   UCSC; uc009kgy.1; mouse.
DR   MGI; MGI:2136460; Echs1.
DR   GeneTree; ENSGT00580000081296; -.
DR   InParanoid; Q8BU95; -.
DR   ArrayExpress; Q8BU95; -.
DR   Bgee; Q8BU95; -.
DR   Genevestigator; Q8BU95; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   InterPro; IPR001753; Crotonase_core.
DR   Pfam; PF00378; ECH; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   153 AA;  16494 MW;  A0EF8B82F566D090 CRC64;
     MAALRALLPR ACSSLLSSVR CPELRRFASG ANFQYIITEK KGKNSSVGLI QLNRPKALNA
     LCNGLIEELN QALETFEQDP AVGAIVLTGG DKAFAAGADI KEMQNRTFQD CYSSKFLSHW
     DHITRVKKPV IAAVNGYAVS DSSPGASCAF KSQ
//
ID   HOOK3_MOUSE             Reviewed;         718 AA.
AC   Q8BUK6; Q540A0; Q8BV48; Q8BW57; Q8BY41;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   02-FEB-2004, sequence version 2.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Protein Hook homolog 3;
DE            Short=mHK3;
GN   Name=Hook3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], INTERACTION WITH IIGP1, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=15075236; DOI=10.1242/jcs.01039;
RA   Kaiser F., Kaufmann S.H.E., Zerrahn J.;
RT   "IIGP, a member of the IFN inducible and microbial defense mediating
RT   47 kDa GTPase family, interacts with the microtubule binding protein
RT   hook3.";
RL   J. Cell Sci. 117:1747-1756(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart, Mammary gland, Ovary, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=21135884; PubMed=11238449; DOI=10.1083/jcb.152.5.923;
RA   Walenta J.H., Didier A.J., Liu X., Kraemer H.;
RT   "The Golgi-associated hook3 protein is a member of a novel family of
RT   microtubule-binding proteins.";
RL   J. Cell Biol. 152:923-934(2001).
RN   [5]
RP   INTERACTION WITH SPIC.
RX   PubMed=12950921; DOI=10.1046/j.1365-2958.2003.03668.x;
RA   Shotland Y., Kraemer H., Groisman E.A.;
RT   "The Salmonella SpiC protein targets the mammalian Hook3 protein
RT   function to alter cellular trafficking.";
RL   Mol. Microbiol. 49:1565-1576(2003).
RN   [6]
RP   INTERACTION WITH MSR1.
RX   PubMed=17237231; DOI=10.1074/jbc.M611537200;
RA   Sano H., Ishino M., Kraemer H., Shimizu T., Mitsuzawa H.,
RA   Nishitani C., Kuroki Y.;
RT   "The microtubule-binding protein Hook3 interacts with a cytoplasmic
RT   domain of scavenger receptor A.";
RL   J. Biol. Chem. 282:7973-7981(2007).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=17140400; DOI=10.1111/j.1600-0854.2006.00511.x;
RA   Szebenyi G., Hall B., Yu R., Hashim A.I., Kraemer H.;
RT   "Hook2 localizes to the centrosome, binds directly to
RT   centriolin/CEP110 and contributes to centrosomal function.";
RL   Traffic 8:32-46(2007).
CC   -!- FUNCTION: Component of the FTS/Hook/FHIP complex (FHF complex).
CC       The FHF complex may function to promote vesicle trafficking and/or
CC       fusion via the homotypic vesicular protein sorting complex (the
CC       HOPS complex). May regulate clearance of endocytosed receptors
CC       such as MSR1. Participates in defining the architecture and
CC       localization of the Golgi complex (By similarity). Serves as a
CC       target for the spiC protein from Salmonella typhimurium, which
CC       inactivates it, leading to a strong alteration in cellular
CC       trafficking.
CC   -!- SUBUNIT: Self-associates. Component of the FTS/Hook/FHIP complex
CC       (FHF complex), composed of AKTIP/FTS, FAM160A2, and one or more
CC       members of the Hook family of proteins HOOK1, HOOK2, and HOOK3.
CC       May interact directly with AKTIP/FTS, HOOK1 and HOOK2. Associates
CC       with several subunits of the homotypic vesicular sorting complex
CC       (the HOPS complex) including VPS16 and VPS41; these interactions
CC       may be indirect. Interacts with microtubules (By similarity).
CC       Interacts with MSR1, and this association is stimulated by ligand
CC       binding to MSR1. Interacts with IIGP1. Interacts with Salmonella
CC       typhimurium spiC.
CC   -!- INTERACTION:
CC       P30204:Msr1; NbExp=1; IntAct=EBI-1777179, EBI-1777188;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Golgi apparatus.
CC       Note=Enriched at the cis-face of the Golgi complex (By
CC       similarity). Localizes to microtubule asters in prophase (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in brain, cerebellum, heart,
CC       intestine, kidney, liver, lung, skeletal muscle, spleen and
CC       stomach (at protein level).
CC   -!- SIMILARITY: Belongs to the hook family.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AY223806; AAO43109.1; -; mRNA.
DR   EMBL; AK042180; BAC31191.1; -; mRNA.
DR   EMBL; AK054263; BAC35709.1; -; mRNA.
DR   EMBL; AK080377; BAC37897.1; -; mRNA.
DR   EMBL; AK084594; BAC39222.1; -; mRNA.
DR   EMBL; AK145149; BAE26261.1; -; mRNA.
DR   EMBL; CH466580; EDL32811.1; -; Genomic_DNA.
DR   IPI; IPI00353927; -.
DR   RefSeq; NP_997542.1; NM_207659.3.
DR   UniGene; Mm.334464; -.
DR   UniGene; Mm.458186; -.
DR   ProteinModelPortal; Q8BUK6; -.
DR   SMR; Q8BUK6; 12-166.
DR   IntAct; Q8BUK6; 1.
DR   STRING; Q8BUK6; -.
DR   PhosphoSite; Q8BUK6; -.
DR   PRIDE; Q8BUK6; -.
DR   Ensembl; ENSMUST00000037182; ENSMUSP00000046788; ENSMUSG00000037234.
DR   GeneID; 320191; -.
DR   KEGG; mmu:320191; -.
DR   UCSC; uc009lhj.1; mouse.
DR   CTD; 320191; -.
DR   MGI; MGI:2443554; Hook3.
DR   GeneTree; ENSGT00570000078853; -.
DR   HOVERGEN; HBG051920; -.
DR   InParanoid; Q8BUK6; -.
DR   OMA; EYIQTIM; -.
DR   OrthoDB; EOG418BN0; -.
DR   PhylomeDB; Q8BUK6; -.
DR   NextBio; 396213; -.
DR   ArrayExpress; Q8BUK6; -.
DR   Bgee; Q8BUK6; -.
DR   CleanEx; MM_HOOK3; -.
DR   Genevestigator; Q8BUK6; -.
DR   GermOnline; ENSMUSG00000037234; Mus musculus.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0000242; C:pericentriolar material; IDA:BHF-UCL.
DR   GO; GO:0045022; P:early endosome to late endosome transport; ISS:UniProtKB.
DR   GO; GO:0007032; P:endosome organization; ISS:UniProtKB.
DR   GO; GO:0008333; P:endosome to lysosome transport; ISS:UniProtKB.
DR   GO; GO:0022027; P:interkinetic nuclear migration; IMP:BHF-UCL.
DR   GO; GO:0007040; P:lysosome organization; ISS:UniProtKB.
DR   GO; GO:0034453; P:microtubule anchoring; IMP:BHF-UCL.
DR   GO; GO:0050768; P:negative regulation of neurogenesis; IMP:BHF-UCL.
DR   GO; GO:0071539; P:protein localization to centrosome; IMP:BHF-UCL.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008636; HOOK.
DR   Pfam; PF05622; HOOK; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Golgi apparatus; Microtubule;
KW   Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1    718       Protein Hook homolog 3.
FT                                /FTId=PRO_0000219198.
FT   REGION        1    164       Sufficient for interaction with
FT                                microtubules (By similarity).
FT   REGION      450    671       Sufficient for interaction with IIGP1.
FT   REGION      553    718       Required for association with Golgi (By
FT                                similarity).
FT   COILED      168    433       Potential.
FT   COILED      462    663       Potential.
FT   MOD_RES     238    238       Phosphoserine (By similarity).
FT   MOD_RES     708    708       Phosphotyrosine (By similarity).
FT   CONFLICT     94     94       Q -> H (in Ref. 2; BAC37897).
SQ   SEQUENCE   718 AA;  83218 MW;  72577D065F118172 CRC64;
     MFNVESVERV ELCESLLTWI QTFNVDAPCQ TAEDLTNGVV MSQVLQKIDP VYFDDNWLNR
     IKTEVGDNWR LKISNLKKIL KGILDYNHEI LGQQINDFTL PDVNLIGEHS DAAELGRMLQ
     LILGCAVNCE QKQEYIQAIM MMEESVQHVV MTAIQELMSK ESPVSAGHDA YVDLDRQLKK
     TTEELNEALS AKEEIAQRCH ELDMQVAALQ EEKSSLLAEN QILMERLNQS DSIEDPNSPA
     GRRHLQLQTQ LEQLQEETFR LEAAKDDYRI RCEELEKEIS ELRQQNDELT TLADEAQSLK
     DEIDVLRHSS DKVSKLEGQV ESYKKKLEDL GDLRRQVKLL EEKNTMYMQN TVSLEEELRK
     ANAARGQLET YKRQVVELQN RLSDESKKAD KLDFEYKRLK EKVDGLQKEK DRLRTERDSL
     KETIEELRCV QAQEGQLTTQ GLMPLGSQES SDSLAAEIVT PEIREKLIRL QHENKMLKLN
     QEDSDNEKIA LLQSLLDDAN LRKNELETEN RLVNQRLLEV QSQVEELQKS LQDQGSKAED
     SVLLKKKLEE HLEKLHEANN ELQKKRAIIE DLEPRFNNSS LRIEELQEAL RKKEEEMKQM
     EERYKKYLEK AKSVIRTLDP KQNQGAAPEI QALKNQLQER DRLFHSLEKE YEKTKSQRDM
     EEKYIVSAWY NMGMTLHKKA AEDRLASTGS GQSFLARQRQ ATSTRRSYPG HVQPATAR
//
ID   PKHA1_MOUSE             Reviewed;         383 AA.
AC   Q8BUL6; Q8BK96; Q8BXU1; Q8VE13;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Pleckstrin homology domain-containing family A member 1;
DE            Short=PH domain-containing family A member 1;
DE   AltName: Full=Tandem PH domain-containing protein 1;
DE            Short=TAPP-1;
GN   Name=Plekha1; Synonyms=Tapp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Binds specifically to phosphatidylinositol-3,4-
CC       diphosphate (PtdIns3,4P2), but not to other phosphoinositides. May
CC       recruit other proteins to the plasma membrane (By similarity).
CC   -!- SUBUNIT: Interacts with MPDZ and PTPN13 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane;
CC       Peripheral membrane protein (By similarity). Nucleus (By
CC       similarity). Note=Locates to the plasma membrane after treatments
CC       that stimulate the production of PtdIns3,4P2 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BUL6-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q8BUL6-2; Sequence=VSP_009764, VSP_009767;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: Binds to membranes enriched in PtdIns3,4P2 via the C-
CC       terminal PH domain.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK083340; BAC38874.1; -; mRNA.
DR   EMBL; BC020017; AAH20017.1; -; mRNA.
DR   IPI; IPI00123693; -.
DR   IPI; IPI00225502; -.
DR   RefSeq; NP_598703.1; NM_133942.2.
DR   UniGene; Mm.323554; -.
DR   ProteinModelPortal; Q8BUL6; -.
DR   SMR; Q8BUL6; 1-112, 190-292.
DR   STRING; Q8BUL6; -.
DR   PhosphoSite; Q8BUL6; -.
DR   PRIDE; Q8BUL6; -.
DR   Ensembl; ENSMUST00000075181; ENSMUSP00000074675; ENSMUSG00000040268.
DR   Ensembl; ENSMUST00000106198; ENSMUSP00000101804; ENSMUSG00000040268.
DR   GeneID; 101476; -.
DR   KEGG; mmu:101476; -.
DR   UCSC; uc009kar.1; mouse.
DR   UCSC; uc009kat.1; mouse.
DR   CTD; 101476; -.
DR   MGI; MGI:2442213; Plekha1.
DR   eggNOG; roNOG04920; -.
DR   GeneTree; ENSGT00440000037398; -.
DR   HOGENOM; HBG443806; -.
DR   HOVERGEN; HBG053612; -.
DR   InParanoid; Q8BUL6; -.
DR   OMA; RRLSNPC; -.
DR   OrthoDB; EOG4MPHQF; -.
DR   PhylomeDB; Q8BUL6; -.
DR   ArrayExpress; Q8BUL6; -.
DR   Bgee; Q8BUL6; -.
DR   Genevestigator; Q8BUL6; -.
DR   GermOnline; ENSMUSG00000040268; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008209; P:androgen metabolic process; IMP:MGI.
DR   GO; GO:0008210; P:estrogen metabolic process; IGI:MGI.
DR   GO; GO:0060325; P:face morphogenesis; IMP:MGI.
DR   GO; GO:0033327; P:Leydig cell differentiation; IMP:MGI.
DR   GO; GO:0001553; P:luteinization; IGI:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR   GO; GO:0060021; P:palate development; IMP:MGI.
DR   GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Pfam; PF00169; PH; 2.
DR   SMART; SM00233; PH; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasm; Lipid-binding;
KW   Membrane; Nucleus; Phosphoprotein; Repeat.
FT   CHAIN         1    383       Pleckstrin homology domain-containing
FT                                family A member 1.
FT                                /FTId=PRO_0000053874.
FT   DOMAIN        7    112       PH 1.
FT   DOMAIN      191    289       PH 2.
FT   MOD_RES     308    308       Phosphoserine.
FT   VAR_SEQ      68    115       Missing (in isoform 2).
FT                                /FTId=VSP_009764.
FT   VAR_SEQ     301    383       MRQARRLSNPCIQRSIPAGLQNPNSLSVLPGPQPPPHIPQP
FT                                LAATLWSQAVPWRSEEFTNLLPRSSQGTSRSRLSLQESQLP
FT                                K -> EHSGWPSEPKFTVRPAGAAATASHSPASRSHSLVSG
FT                                CAMEKRGVYQSLAKVKPGNFKVQTVSPREPASKVTEQALLR
FT                                PQSKNGPQGEDGEPVDLDDASLPVSDV (in isoform
FT                                2).
FT                                /FTId=VSP_009767.
SQ   SEQUENCE   383 AA;  43371 MW;  6020E5A2F3184C19 CRC64;
     MPYVDRQNRI CGFLDIEENE NSGKFLRRYF ILDTREDSFV WYMDNPQNLP SGSSRVGAIK
     LTYISKVSDA TKLRPKAEFC FVMNAGMRKY FLQANDQQDL VEWVNVLNKA IKITVPKQSD
     SQPASDSLSR QGDCGKKQVS YRTDIVGGVP IITPTQKEEV NECGESLDRN NLKRSQSHLP
     YFAPKPPSDS AVIKAGYCVK QGAVMKNWKR RYFQLDENTI GYFKSELEKE PLRVIPLKEV
     HKVQECKQSD IMMRDNLFEI VTTSRTFYVQ ADSPEEMHSW IKAVSGAIVA QRGPGRSSSS
     MRQARRLSNP CIQRSIPAGL QNPNSLSVLP GPQPPPHIPQ PLAATLWSQA VPWRSEEFTN
     LLPRSSQGTS RSRLSLQESQ LPK
//
ID   F163B_MOUSE             Reviewed;         167 AA.
AC   Q8BUM6;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Protein FAM163B;
GN   Name=Fam163b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, and Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-78, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the FAM163 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK083284; BAC38843.1; -; mRNA.
DR   EMBL; AK162827; BAE37071.1; -; mRNA.
DR   IPI; IPI00225518; -.
DR   RefSeq; NP_780636.1; NM_175427.4.
DR   UniGene; Mm.314080; -.
DR   PhosphoSite; Q8BUM6; -.
DR   PRIDE; Q8BUM6; -.
DR   Ensembl; ENSMUST00000009360; ENSMUSP00000009360; ENSMUSG00000089805.
DR   GeneID; 109349; -.
DR   KEGG; mmu:109349; -.
DR   UCSC; uc008ixc.1; mouse.
DR   CTD; 109349; -.
DR   MGI; MGI:1926106; Fam163b.
DR   GeneTree; ENSGT00390000002397; -.
DR   HOGENOM; HBG445382; -.
DR   HOVERGEN; HBG100700; -.
DR   InParanoid; Q8BUM6; -.
DR   OMA; FFLQEPE; -.
DR   OrthoDB; EOG45QHFD; -.
DR   PhylomeDB; Q8BUM6; -.
DR   NextBio; 361955; -.
DR   ArrayExpress; Q8BUM6; -.
DR   Bgee; Q8BUM6; -.
DR   Genevestigator; Q8BUM6; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    167       Protein FAM163B.
FT                                /FTId=PRO_0000280259.
FT   TRANSMEM      6     26       Helical; (Potential).
FT   MOD_RES      78     78       Phosphothreonine.
SQ   SEQUENCE   167 AA;  18306 MW;  6F5158F78CA65B97 CRC64;
     MTAGTVVITG GILATVILLC IIAVLCYCRL QYYCCKKDES EEDEEEPDFA VHSHLPPLHS
     NRNLVLTNGP ALYPAATTSF SQKSPQARAL CRSCSHYEPP TFFLQEPEDE DFEGVRNGGG
     RVAYKSISQE DVELPSASFG GLQALNPNRL SAMREAFSRS RSVSTDV
//
ID   UBP43_MOUSE             Reviewed;        1132 AA.
AC   Q8BUM9; Q8VDP5;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 43;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 43;
DE   AltName: Full=Ubiquitin thiolesterase 43;
DE   AltName: Full=Ubiquitin-specific-processing protease 43;
GN   Name=Usp43;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-1132 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 207-1132 (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May recognize and hydrolyze the peptide bond at the C-
CC       terminal Gly of ubiquitin. Involved in the processing of poly-
CC       ubiquitin precursors as well as that of ubiquinated proteins (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BUM9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BUM9-2; Sequence=VSP_020469, VSP_020470;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH21474.1; Type=Erroneous initiation;
CC       Sequence=BAC38837.1; Type=Erroneous initiation;
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DR   EMBL; AL732570; CAI52000.2; -; Genomic_DNA.
DR   EMBL; AK083271; BAC38837.1; ALT_INIT; mRNA.
DR   EMBL; BC021474; AAH21474.1; ALT_INIT; mRNA.
DR   IPI; IPI00225521; -.
DR   IPI; IPI00788336; -.
DR   RefSeq; NP_776115.2; NM_173754.4.
DR   UniGene; Mm.158885; -.
DR   HSSP; P40818; 2GFO.
DR   ProteinModelPortal; Q8BUM9; -.
DR   MEROPS; C19.979; -.
DR   PhosphoSite; Q8BUM9; -.
DR   PRIDE; Q8BUM9; -.
DR   Ensembl; ENSMUST00000021288; ENSMUSP00000021288; ENSMUSG00000020905.
DR   GeneID; 216835; -.
DR   KEGG; mmu:216835; -.
DR   UCSC; uc007jne.1; mouse.
DR   CTD; 216835; -.
DR   MGI; MGI:2444541; Usp43.
DR   eggNOG; roNOG10587; -.
DR   HOGENOM; HBG446590; -.
DR   HOVERGEN; HBG094126; -.
DR   InParanoid; Q8BUM9; -.
DR   OMA; QFYTKEE; -.
DR   OrthoDB; EOG4DR9BH; -.
DR   PhylomeDB; Q8BUM9; -.
DR   BRENDA; 3.1.2.15; 244.
DR   NextBio; 375380; -.
DR   ArrayExpress; Q8BUM9; -.
DR   Bgee; Q8BUM9; -.
DR   CleanEx; MM_USP43; -.
DR   Genevestigator; Q8BUM9; -.
DR   GermOnline; ENSMUSG00000020905; Mus musculus.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:EC.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19.
DR   Pfam; PF00443; UCH; 1.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; 1.
DR   PROSITE; PS50235; UCH_2_3; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Hydrolase; Phosphoprotein; Protease;
KW   Thiol protease; Ubl conjugation pathway.
FT   CHAIN         1   1132       Ubiquitin carboxyl-terminal hydrolase 43.
FT                                /FTId=PRO_0000249522.
FT   ACT_SITE    110    110       Nucleophile (By similarity).
FT   ACT_SITE    668    668       Proton acceptor (By similarity).
FT   MOD_RES     835    835       Phosphotyrosine (By similarity).
FT   VAR_SEQ    1047   1047       Missing (in isoform 2).
FT                                /FTId=VSP_020469.
FT   VAR_SEQ    1052   1052       Q -> QARGSSP (in isoform 2).
FT                                /FTId=VSP_020470.
FT   CONFLICT    760    760       M -> V (in Ref. 3; AAH21474).
FT   CONFLICT    982    982       S -> N (in Ref. 3; AAH21474).
FT   CONFLICT   1002   1002       D -> G (in Ref. 3; AAH21474).
SQ   SEQUENCE   1132 AA;  123874 MW;  3E9E9E46B75E67FA CRC64;
     MDPGVGNALG EGPPAPRPRR RRSLRRLLNR FLLALGSRSR SGDSPPRPPA QPSPYDGDGE
     GGFACAPGPA PASAGSPGPD RPPGSQPQIS SGDGARPPGA QGLKNHGNTC FMNAVVQCLS
     NTDLLAEFLA LGRYRAAPGR AEVTEQLAAL VRALWTREYT PQLSAEFKNA VSKYGSQFQG
     NSQHDALEFL LWLLDRVHED LEGSAHGLVS EQLPPEVSKI SEDLRPSAAP TSLGPSFVQS
     HFQAQYRSSL TCPHCLKQSN TFDPFLCVSL PIPLRQTRFL SVTLVFPSKS QRFLRVGLAV
     PILSTVAALR KMVAEEGGVP AEEVILVELY PNGFQRSFFD EEDLNTIAEG DNVYAFQVPP
     SPGLGTLSAH PSGLSVSPRL PVRDSQRFSG PLHSENRVVF LFCNLVGSGQ QASRFGPPFL
     IREDRTISWA QLQQCILSKV RCLMRSEVSA QDLGTLFSIR VVGLSLACSY LSPKDNRPLC
     HWAVDRALHL RRPGGPPHVK LAVEWDSSVT ERLFGSLQEE RVQDADSVWR QQQAHQQPSC
     TLDECFQSYT KEEQLAQDDA WKCPHCQVLQ QGVVKLSLWT LPDILIIHLK RFCQVGERRN
     KLSTLVKFPL SGLNMAPHVA RRSTNSKAGP GPWSSWKQPI CLPTTYPLDF LYDLYAVCNH
     HGSLQGGHYT AYCRNSLDGQ WYSYDDSTVE ALREDEVNTR GAYILFYQKR NSIPPWSASS
     SMRGSTSSSL SDHWLMRLGS LNNSTRGSLL SWSSAPCPSM ARVPDSPVFT NGVCHQDKGG
     VETRPLVRGV GGRSISMKAS PASRSRHGPF KTMPLRWSFG HREKRPGASV ELVEYLESRR
     RPRSTSQSIV PLLTRAAGGE ETSASPRSDG TLPAKSEDSG RAIGQGTTGV PLSSCHLNHH
     PALGSLDDSL HTARTRTGNV SQDIRLPKKF DLPLTVMPSV GDEKPARPEG QKMTPWKGSS
     QVGSQSSPPS PSTGLLRNFK DSGPGTLPKM KSKAAMEERA PDKDRGQGTF TLLKSVFWKK
     EHKRTVRTES SPPAPPISLG SDRLSPAAMN EQALRIRESP AKGLGNHMER DIRSAPSSLH
     LPRKASRPPR ASTAGTSQRT IPGEQISYGT LQRVKYHTLS LGRKKSLPES SF
//
ID   DOCK1_MOUSE             Reviewed;        1865 AA.
AC   Q8BUR4; Q3URT8; Q3UY80; Q4QQL8; Q6PD14; Q8BVC9; Q91Z55; Q922V1;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Dedicator of cytokinesis protein 1;
DE   AltName: Full=180 kDa protein downstream of CRK;
DE            Short=DOCK180;
GN   Name=Dock1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-289 AND 1763-1865 (ISOFORM
RP   1), AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1171-1865 (ISOFORM
RP   2).
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 902-1865 (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain, Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION.
RX   MEDLINE=98406090; PubMed=9733740; DOI=10.1074/jbc.273.38.24479;
RA   Kiyokawa E., Hashimoto Y., Kurata T., Sugimura H., Matsuda M.;
RT   "Evidence that DOCK180 up-regulates signals from the CrkII-p130(Cas)
RT   complex.";
RL   J. Biol. Chem. 273:24479-24484(1998).
RN   [5]
RP   INTERACTION WITH BAI1 AND DOCK1.
RX   PubMed=17960134; DOI=10.1038/nature06329;
RA   Park D., Tosello-Trampont A.-C., Elliott M.R., Lu M., Haney L.B.,
RA   Ma Z., Klibanov A.L., Mandell J.W., Ravichandran K.S.;
RT   "BAI1 is an engulfment receptor for apoptotic cells upstream of the
RT   ELMO/Dock180/Rac module.";
RL   Nature 450:430-434(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1756, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Involved in cytoskeletal rearrangements required for
CC       phagocytosis of apoptotic cells and cell motility. Functions as a
CC       guanine nucleotide exchange factor (GEF), which activates Rac Rho
CC       small GTPases by exchanging bound GDP for free GTP. Its GEF
CC       activity may be enhanced by ELMO1 (By similarity).
CC   -!- SUBUNIT: Interacts with the SH3 domains of CRK and NCK2 via
CC       multiple sites. Interacts with nucleotide-free RAC1 via its DHR-2
CC       domain. Interacts with ELMO1, ELMO2 and probably ELMO3 via its SH3
CC       domain. Interacts with RAC1 (By similarity). Interacts with ELMO1
CC       and BAI1.
CC   -!- INTERACTION:
CC       Q8BPU7-1:Elmo1; NbExp=2; IntAct=EBI-646023, EBI-644162;
CC       Q8BYZ7:Elmo3; NbExp=2; IntAct=EBI-646023, EBI-646035;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane (By
CC       similarity). Note=Recruited to membranes via its interaction with
CC       phosphatidylinositol 3,4,5-triphosphate (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BUR4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BUR4-2; Sequence=VSP_022205, VSP_022206;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The DHR-2 domain is necessary and sufficient for the GEF
CC       activity.
CC   -!- SIMILARITY: Belongs to the DOCK family.
CC   -!- SIMILARITY: Contains 1 DHR-1 (CZH-1) domain.
CC   -!- SIMILARITY: Contains 1 DHR-2 (CZH-2) domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; AC100208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC127574; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC129300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC136515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC136641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK078899; BAC37448.1; -; mRNA.
DR   EMBL; AK082835; BAC38645.1; -; mRNA.
DR   EMBL; AK134905; BAE22333.1; -; mRNA.
DR   EMBL; AK141224; BAE24599.1; -; mRNA.
DR   EMBL; BC006755; AAH06755.1; -; mRNA.
DR   EMBL; BC009668; AAH09668.1; -; mRNA.
DR   EMBL; BC058998; AAH58998.1; -; mRNA.
DR   EMBL; BC098214; AAH98214.1; -; mRNA.
DR   IPI; IPI00755697; -.
DR   IPI; IPI00816910; -.
DR   RefSeq; NP_001028592.1; NM_001033420.2.
DR   UniGene; Mm.436572; -.
DR   ProteinModelPortal; Q8BUR4; -.
DR   SMR; Q8BUR4; 10-168, 425-611.
DR   IntAct; Q8BUR4; 23.
DR   STRING; Q8BUR4; -.
DR   PhosphoSite; Q8BUR4; -.
DR   PRIDE; Q8BUR4; -.
DR   Ensembl; ENSMUST00000084488; ENSMUSP00000081531; ENSMUSG00000058325.
DR   GeneID; 330662; -.
DR   KEGG; mmu:330662; -.
DR   UCSC; uc009kdv.1; mouse.
DR   CTD; 330662; -.
DR   MGI; MGI:2429765; Dock1.
DR   eggNOG; maNOG08129; -.
DR   GeneTree; ENSGT00590000083047; -.
DR   HOVERGEN; HBG051389; -.
DR   InParanoid; Q8BUR4; -.
DR   OMA; FTDRYLQ; -.
DR   OrthoDB; EOG473PQD; -.
DR   NextBio; 399497; -.
DR   ArrayExpress; Q8BUR4; -.
DR   Bgee; Q8BUR4; -.
DR   CleanEx; MM_DOCK1; -.
DR   Genevestigator; Q8BUR4; -.
DR   GermOnline; ENSMUSG00000058325; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0051020; F:GTPase binding; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0016477; P:cell migration; IDA:MGI.
DR   GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR   InterPro; IPR010703; DOCK.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF06920; Ded_cyto; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Cytoplasm;
KW   Guanine-nucleotide releasing factor; Membrane; Phagocytosis;
KW   Phosphoprotein; SH3 domain; SH3-binding.
FT   CHAIN         1   1865       Dedicator of cytokinesis protein 1.
FT                                /FTId=PRO_0000189985.
FT   DOMAIN        9     70       SH3.
FT   DOMAIN      422    664       DHR-1.
FT   DOMAIN     1111   1616       DHR-2.
FT   REGION     1687   1695       Phosphoinositide-binding (Potential).
FT   REGION     1793   1819       Interaction with NCK2 second and third
FT                                SH3 domain (minor) (By similarity).
FT   REGION     1820   1836       Interaction with NCK2 third SH3 domain
FT                                (major) (By similarity).
FT   REGION     1837   1852       Interaction with NCK2 (minor) (By
FT                                similarity).
FT   MOTIF      1799   1805       SH3-binding; interaction with CRK
FT                                (Potential).
FT   MOTIF      1838   1843       SH3-binding; interaction with CRK
FT                                (Potential).
FT   MOD_RES    1756   1756       Phosphoserine.
FT   MOD_RES    1811   1811       Phosphotyrosine (By similarity).
FT   MOD_RES    1858   1858       Phosphoserine (By similarity).
FT   VAR_SEQ    1572   1572       I -> V (in isoform 2).
FT                                /FTId=VSP_022205.
FT   VAR_SEQ    1573   1865       Missing (in isoform 2).
FT                                /FTId=VSP_022206.
FT   CONFLICT   1358   1358       I -> V (in Ref. 1; BAE22333).
SQ   SEQUENCE   1865 AA;  215085 MW;  4FFEAA4CBED8DE62 CRC64;
     MTRWVPTKRE EKYGVAFYNY DARGADELSL QIGDTVHILE TYEGWYRGYT LRKKSKKGIF
     PASYIHLKEA IVEGKGQHET VIPGDLPLIQ EVTTTLREWS TIWRQLYVQD NREMFRSVRH
     MIYDLIEWRS QILSGTLPQD ELKELKKKVT AKIDYGNRIL DLDLVVRDED GNILDPELTS
     TISLFRAHEV ASKQVEERLQ EEKSQKQNMD INRQAKFAAT PSLALFVNLK NVVCKIGEDA
     EVLMSLYDPM ESKFISENYL VRWSSSGLPK DIDRLHNLRA VFTDLGSKDL KREKISFVCQ
     IVRVGRMELR DSNTRKLTSG LRRPFGVAVM DVTDIINGKV DDEDKQHFIP FQAVAGENDF
     LQTVINKVIA AKEVNHKGQG LWVTLKLLPG DIHQIRKEFP HLVDRTTAVA RKTGFPEIIM
     PGDVRNDIYV TLVQGDFDKG SKTTAKNVEV TVSVYDEDGK RLEHVIFPGA GDEAISEYKS
     VIYYQVKQPR WFETLKVAIP IEDVNRSHLR FTFRHRSSQD SKDKSEKIFA LAFVKLMRYD
     GTTLRDGEHD LIVYKAEAKK LEDAATYLSL PSTKGELEEK GHSATGKGMQ SLGSCTISKD
     SFQISTLVCS TKLTQNVDLL GLLKWRSNTN LLQQNLRQLM KVDGGEVVKF LQDTLDALFN
     IMMENSESET FDTLVFDALV FIIGLIADRK FQHFNPVLET YIKKHFSATL AYTKLTKVLR
     TYVASAEKPG VNEQLYKAIK ALEYIFKFIV RSRVLFNQLY ENKGEADFVE SLLQLFRSIN
     DMMSSLSELT VRVKGAALKY LPTIVNDVKL VFDPKELSKM FTEFILNVPA GLLTVQKLSC
     LIEIVHSDLF TQHDCREILL PMMTDQLKYH LERQEELEAC CQLLSNILEV LYRKDVGPTQ
     RHVQIIMETL LRTVNRTVIS MGRDSELIGN FVACMTAILR QMEDYHYAHL IKTFGKMRTD
     VVDFLMETFI MFKNLIGKNV YPFDWVIMNT MQNKVFLRAI NQYADMLNKR FLDQANFELQ
     LWNNYFHLAV AFLTQESLQL ENFSSAKRAK ILNKYGDMRR QIGFEIRDMW YNLGQHKIKF
     IPEMVGPILE MTLIPETELR KATLPIFFDM MQCEFHSTRS FQMFENEIIT KLDHEVEGGR
     GDEQYKVLFD KILLEHCRKH KYLAKTGETF VKLVVRLMER LLDYRTIMHD ENKDNRMSCT
     VNVLNFYKEI EREEMYIRYL YKLCDLHKEC DNYTEAAYTL LLHAKLLKWS EDVCAAHLTQ
     RDGFQATTQG QLKEQLYQEI IHYFDKGKMW EEAIALGKEL AEQYETEMFD YEQLSELLKK
     QAQFYENIVK VIRPKPDYFA VGYYGQGFPS FLRGKVFIYR GKEYERREDF EARLLTQFPN
     AEKMKTTSPP GDDIKTSPGQ YIQCFTVKPK LDLPPRFHRP VSEQIVSFYR VNEVQRFEYS
     RPIRKGEKNP DNEFANMWIE RTIYTTAYKL PGILRWFEVK SVFMVEISPL ENAIETMQLT
     NDKISSMVQQ HLDDPGLPIN PLSMLLNGIV DPAVMGGFAN YEKAFFTDRY LQEHPEAHGQ
     IEKLKDLIAW QIPFLAEGIR IHGDKVTEAL RPFHERMEAC FKQLKEKVEK QYGVRTMPSG
     LDDRRGSRPR SMVRSFTMPS SSRPLSVASV SSFSSDSTPS RPGSDGFALE PLLPKKMHSR
     SQDKLDKDDP DKEKKDKKKE KRNSKHQEIF DKEFKPADSS LQQSEAVILS ETISPLRPQR
     PKSQVINVIG NERRFSVSPA SPSSQQTPPP VTPRAKLSFS IQPSLELNGM MGMDVADVPP
     PLPLKGNMAD YGNLMENQDM MVSPTSPPPP PPQRQQPPPL PSKTPPPPPP KTTRKQTSVD
     SGIVQ
//
ID   GEPH_MOUSE              Reviewed;         769 AA.
AC   Q8BUV3;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Gephyrin;
DE   Includes:
DE     RecName: Full=Molybdopterin adenylyltransferase;
DE              Short=MPT adenylyltransferase;
DE              EC=2.7.7.n5;
DE     AltName: Full=Domain G;
DE   Includes:
DE     RecName: Full=Molybdopterin molybdenumtransferase;
DE              Short=MPT Mo-transferase;
DE              EC=2.-.-.-;
DE     AltName: Full=Domain E;
GN   Name=Gphn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-194, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-194, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Microtubule-associated protein involved in membrane
CC       protein-cytoskeleton interactions. It is thought to anchor the
CC       inhibitory glycine receptor (GLYR) to subsynaptic microtubules (By
CC       similarity). Catalyzes two steps in the biosynthesis of the
CC       molybdenum cofactor. In the first step, molybdopterin is
CC       adenylated. Subsequently, molybdate is inserted into adenylated
CC       molybdopterin and AMP is released.
CC   -!- CATALYTIC ACTIVITY: Molybdopterin + ATP = adenylyl-molybdopterin +
CC       diphosphate.
CC   -!- CATALYTIC ACTIVITY: Adenylyl-molybdopterin + molybdate =
CC       molybdenum-cofactor + adenylate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Inhibited by copper and tungsten (By
CC       similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC   -!- SUBUNIT: Homotrimer, homodimer and homooligomer. Interacts with
CC       GLRB and GABARAP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse. Cell junction,
CC       synapse, postsynaptic cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity). Cytoplasm, cytoskeleton (By
CC       similarity). Note=Cytoplasmic face of glycinergic postsynaptic
CC       membranes (By similarity).
CC   -!- SIMILARITY: In the N-terminal section; belongs to the moaB/mog
CC       family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the moeA family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK082353; BAC38476.1; -; mRNA.
DR   IPI; IPI00225670; -.
DR   RefSeq; NP_766540.2; NM_172952.3.
DR   UniGene; Mm.341742; -.
DR   UniGene; Mm.363753; -.
DR   UniGene; Mm.453131; -.
DR   HSSP; Q03555; 2FTS.
DR   ProteinModelPortal; Q8BUV3; -.
DR   SMR; Q8BUV3; 13-181, 351-769.
DR   MINT; MINT-1869852; -.
DR   STRING; Q8BUV3; -.
DR   PhosphoSite; Q8BUV3; -.
DR   PRIDE; Q8BUV3; -.
DR   Ensembl; ENSMUST00000052472; ENSMUSP00000054064; ENSMUSG00000047454.
DR   GeneID; 268566; -.
DR   KEGG; mmu:268566; -.
DR   UCSC; uc007nzc.1; mouse.
DR   CTD; 268566; -.
DR   MGI; MGI:109602; Gphn.
DR   GeneTree; ENSGT00390000016577; -.
DR   HOVERGEN; HBG005828; -.
DR   OrthoDB; EOG4N30NB; -.
DR   PhylomeDB; Q8BUV3; -.
DR   NextBio; 392389; -.
DR   ArrayExpress; Q8BUV3; -.
DR   Bgee; Q8BUV3; -.
DR   CleanEx; MM_GPHN; -.
DR   Genevestigator; Q8BUV3; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0019897; C:extrinsic to plasma membrane; TAS:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008092; F:cytoskeletal protein binding; TAS:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:EC.
DR   GO; GO:0007529; P:establishment of synaptic specificity at neuromuscular junction; IMP:MGI.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR020817; Mo_cofactor_synthesis.
DR   InterPro; IPR008284; MoCF_biosynth_CS.
DR   InterPro; IPR005111; MoeA_C_domain_IV.
DR   InterPro; IPR005110; MoeA_linker/N.
DR   InterPro; IPR001453; Mopterin-bd.
DR   Gene3D; G3DSA:2.40.340.10; G3DSA:2.40.340.10; 1.
DR   Gene3D; G3DSA:3.40.980.10; MPT_bd; 2.
DR   Pfam; PF00994; MoCF_biosynth; 2.
DR   Pfam; PF03454; MoeA_C; 1.
DR   Pfam; PF03453; MoeA_N; 1.
DR   SMART; SM00852; MoCF_biosynth; 2.
DR   SUPFAM; SSF53218; MoCF_biosynth; 2.
DR   SUPFAM; SSF63867; MoeA_C; 1.
DR   SUPFAM; SSF63882; MoeA_N; 1.
DR   TIGRFAMs; TIGR00177; molyb_syn; 2.
DR   PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1.
DR   PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell junction; Cell membrane; Cytoplasm; Cytoskeleton;
KW   Magnesium; Membrane; Metal-binding; Molybdenum;
KW   Molybdenum cofactor biosynthesis; Multifunctional enzyme;
KW   Nucleotide-binding; Phosphoprotein; Postsynaptic cell membrane;
KW   Synapse; Transferase.
FT   CHAIN         1    769       Gephyrin.
FT                                /FTId=PRO_0000269039.
FT   REGION       14    153       MPT Mo-transferase.
FT   REGION      140    349       Interaction with GABARAP (By similarity).
FT   REGION      327    769       MPT adenylyltransferase.
FT   COMPBIAS    187    192       Poly-Pro.
FT   COMPBIAS    213    218       Glu-rich (acidic).
FT   MOD_RES     188    188       Phosphoserine.
FT   MOD_RES     194    194       Phosphoserine.
FT   MOD_RES     266    266       Phosphothreonine (By similarity).
FT   MOD_RES     270    270       Phosphoserine (By similarity).
FT   MOD_RES     286    286       Phosphothreonine (By similarity).
FT   MOD_RES     338    338       Phosphoserine.
SQ   SEQUENCE   769 AA;  83282 MW;  D0EC2009B3E9C1AE CRC64;
     MATEGMILTN HDHQIRVGVL TVSDSCFRNL AEDRSGINLK DLVQDPSLLG GTISAYKIVP
     DEIEEIKETL IDWCDEKELN LILTTGGTGF APRDVTPEAT KEVIEREAPG MALAMLMGSL
     NVTPLGMLSR PVCGIRGKTL IINLPGSKKG SQECFQFILP ALPHAIDLLR DAIVKVKEVH
     DELEDLPSPP PPLSPPPTTS PHKQTEDKGV QCEEEEEEKK DSGVASTEDS SSSHITAAAL
     AAKIPDSIIS RGVQVLPRDT ATLSTTPSES PRAQATSRLS TASCPTPKQI RRPDESKGVA
     SRVGSLKARL PSCSSTYSVS EVQSRCSSKE NILRASHSAV DITKVARRHR MSPFPLTSMD
     KAFITVLEMT PVLGTEIINY RDGMGRVLAQ DVYAKDNLPP FPASVKDGYA VRAADGPGDR
     FIIGESQAGE QPTQTVMPGQ VMRVTTGAPI PCGADAVVQV EDSELIRESD DGTEELEVRI
     LVQARPGQDI RPIGHDIKRG ECVLAKGTHM GPSEIGLLAT VGVTEVEVNK FPVVAVMSTG
     NELLNPEDDL LPGKIRDSNR STLLATIQEH GYPTINLGIV GDNPDDLLNA LNEGISRADV
     IITSGGVSMG EKDYLKQVLD IDLHAQIHFG RVFMKPGLPT TFATLDIDGV RKIIFALPGN
     PVSAVVTCNL FVVPALRKMQ GILDPRPTII KARLSCDVKL DPRPEYHRCI LTWHHQEPLP
     WAQSTGNQMS SRLMSMRSAN GLLMLPPKTE QYVELHKGEV VDVMVIGRL
//
ID   LSM11_MOUSE             Reviewed;         361 AA.
AC   Q8BUV6;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=U7 snRNA-associated Sm-like protein LSm11;
GN   Name=Lsm11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION IN THE U7 SNRNP
RP   COMPLEX, AND INTERACTION WITH ZNF473.
RX   MEDLINE=22855639; PubMed=12975319; DOI=10.1101/gad.274403;
RA   Pillai R.S., Grimmler M., Meister G., Will C.L., Luehrmann R.,
RA   Fischer U., Schuemperli D.;
RT   "Unique Sm core structure of U7 snRNPs: assembly by a specialized SMN
RT   complex and the role of a new component, Lsm11, in histone RNA
RT   processing.";
RL   Genes Dev. 17:2321-2333(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   INTERACTION WITH CLNS1A; PRMT5 AND WDR77, AND ABSENCE OF METHYLATION.
RX   PubMed=16087681; DOI=10.1074/jbc.M505077200;
RA   Azzouz T.N., Pillai R.S., Dapp C., Chari A., Meister G., Kambach C.,
RA   Fischer U., Schuemperli D.;
RT   "Toward an assembly line for U7 snRNPs: interactions of U7-specific
RT   Lsm proteins with PRMT5 and SMN complexes.";
RL   J. Biol. Chem. 280:34435-34440(2005).
RN   [4]
RP   FUNCTION, MUTAGENESIS OF 33-PRO--LEU-35; 59-THY--SER-61;
RP   108-PRO--ARG-110 AND 149-MET--LEU-151, AND INTERACTION WITH ZNF473.
RX   PubMed=15824063; DOI=10.1093/nar/gki516;
RA   Azzouz T.N., Gruber A., Schuemperli D.;
RT   "U7 snRNP-specific Lsm11 protein: dual binding contacts with the 100
RT   kDa zinc finger processing factor (ZFP100) and a ZFP100-independent
RT   function in histone RNA 3'-end processing.";
RL   Nucleic Acids Res. 33:2106-2117(2005).
RN   [5]
RP   FUNCTION.
RX   PubMed=16914750; DOI=10.1128/MCB.00391-06;
RA   Wagner E.J., Marzluff W.F.;
RT   "ZFP100, a component of the active U7 snRNP limiting for histone pre-
RT   mRNA processing, is required for entry into S phase.";
RL   Mol. Cell. Biol. 26:6702-6712(2006).
RN   [6]
RP   IDENTIFICATION IN A HISTONE PRE-MRNA COMPLEX, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RX   PubMed=19470752; DOI=10.1128/MCB.00296-09;
RA   Yang X.-C., Torres M.P., Marzluff W.F., Dominski Z.;
RT   "Three proteins of the U7-specific Sm ring function as the molecular
RT   ruler to determine the site of 3'-end processing in mammalian histone
RT   pre-mRNA.";
RL   Mol. Cell. Biol. 29:4045-4056(2009).
CC   -!- FUNCTION: Component of the U7 snRNP complex that is involved in
CC       the histone 3'-end pre-mRNA processing. Increases U7 snRNA levels
CC       but not histone 3'-end pre-mRNA processing activity, when
CC       overexpressed. Required for cell cycle progression from G1 to S
CC       phases. Binds specifically to the Sm-binding site of U7 snRNA.
CC   -!- SUBUNIT: Identified in a histone pre-mRNA complex, at least
CC       composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1. Interacts
CC       (via the Sm domains) with CLNS1A. Interacts with PRMT5, SMN,
CC       ZNF473 and WDR77. Component of the heptameric ring U7 snRNP
CC       complex, or U7 Sm protein core complex, at least composed of
CC       LSM10, LSM11, SNRPB, SNRPD3, SNRPE, SNRPF, SNRPG and U7 snRNA (By
CC       similarity). Formation of the U7 snRNP is an ATP-dependent process
CC       mediated by a specialized SMN complex containing at least the Sm
CC       protein core complex and additionally, the U7-specific LSM10 and
CC       LSM11 proteins (By similarity). Interacts with LSM10 and SNRPB (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- DOMAIN: The C-terminal SM 1 domain is both necessary for the
CC       binding to the Sm-binding site of U7 snRNA and U7 snRNP assembly.
CC       The N-terminal domain is essential for histone pre-mRNA cleavage
CC       (By similarity). Amino acids 63-82 are sufficient to interact with
CC       ZNF473 (By similarity).
CC   -!- PTM: Not methylated.
CC   -!- SIMILARITY: Belongs to the snRNP Sm proteins family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF514309; AAQ08118.1; -; mRNA.
DR   EMBL; AK082292; BAC38456.1; -; mRNA.
DR   IPI; IPI00225677; -.
DR   RefSeq; NP_082461.1; NM_028185.2.
DR   UniGene; Mm.249827; -.
DR   ProteinModelPortal; Q8BUV6; -.
DR   SMR; Q8BUV6; 155-207.
DR   STRING; Q8BUV6; -.
DR   PhosphoSite; Q8BUV6; -.
DR   PRIDE; Q8BUV6; -.
DR   Ensembl; ENSMUST00000062458; ENSMUSP00000057343; ENSMUSG00000044847.
DR   GeneID; 72290; -.
DR   KEGG; mmu:72290; -.
DR   UCSC; uc007ins.1; mouse.
DR   CTD; 72290; -.
DR   MGI; MGI:1919540; Lsm11.
DR   HOGENOM; HBG714770; -.
DR   HOVERGEN; HBG052367; -.
DR   InParanoid; Q8BUV6; -.
DR   OMA; LPPIPYP; -.
DR   PhylomeDB; Q8BUV6; -.
DR   NextBio; 335924; -.
DR   ArrayExpress; Q8BUV6; -.
DR   Bgee; Q8BUV6; -.
DR   CleanEx; MM_LSM11; -.
DR   Genevestigator; Q8BUV6; -.
DR   GermOnline; ENSMUSG00000044847; Mus musculus.
DR   GO; GO:0071204; C:histone pre-mRNA 3'end processing complex; IDA:UniProtKB.
DR   GO; GO:0005683; C:U7 snRNP; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0071209; F:U7 snRNA binding; ISS:UniProtKB.
DR   GO; GO:0006398; P:histone mRNA 3'-end processing; IDA:UniProtKB.
DR   GO; GO:0000084; P:S phase of mitotic cell cycle; ISS:UniProtKB.
DR   InterPro; IPR010920; LSM-related_domain.
DR   InterPro; IPR001163; LSM_domain.
DR   Pfam; PF01423; LSM; 1.
DR   SUPFAM; SSF50182; Sm_like_riboprot; 2.
PE   1: Evidence at protein level;
KW   mRNA processing; Nucleus; Phosphoprotein; Repeat; Ribonucleoprotein;
KW   RNA-binding.
FT   CHAIN         1    361       U7 snRNA-associated Sm-like protein
FT                                LSm11.
FT                                /FTId=PRO_0000125588.
FT   REGION      172    205       SM 1.
FT   REGION      344    357       SM 2.
FT   MOD_RES      10     10       Phosphoserine (By similarity).
FT   MOD_RES      21     21       Phosphoserine (By similarity).
FT   MUTAGEN      33     35       PLL->AAA: Does not inhibit interaction
FT                                with ZNF473. Reduces strongly histone 3'
FT                                end processing.
FT   MUTAGEN      59     61       YES->AAA: Does not inhibit interaction
FT                                with ZNF473 and histone 3'-end
FT                                processing.
FT   MUTAGEN     108    110       PER->AAA: Does not inhibit interaction
FT                                with ZNF473. Reduces weakly histone 3'
FT                                end processing.
FT   MUTAGEN     149    151       MPL->AAA: Does not inhibit interaction
FT                                with ZNF473. Reduces weakly histone 3'
FT                                end processing.
SQ   SEQUENCE   361 AA;  39907 MW;  68777427AC37E10E CRC64;
     MEEREWGARS ARAGSPASPP SPRLDVSSYS FDPLLALYAP RLPPIPYPNA PCFNNVAEYE
     SFLKGGRTGR GRARGTGEPA SAGTSTGTST GAGSSSRARR RAAPTPDPER IQRLRRLMVV
     KEDTDGTAGA RRQGPGRSKK APRNVLTRMP LHEGSPLGEL HRCIREGVKV NVHIRTFKGL
     RGVCTGFLVA FDKFWNMALT DVDETYRKPV LGKAYERDSS LTLTRLFDRL KLQDSSKKEA
     DSKSAVEDST LSRYSQTSTW KVASVWGRGD TDRSSHRRSR SVPSSLQASA REESRSELSG
     RTTRTEGSSV GGTFSRATTL SRGQSRKKKR KPKVDYQQVF TRHINQIFIR GENVLLVHLA
     Q
//
ID   Q8BV99_MOUSE            Unreviewed;        48 AA.
AC   Q8BV99;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 44.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Map4k3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK079249; BAC37588.1; -; mRNA.
DR   IPI; IPI00669851; -.
DR   UniGene; Mm.458168; -.
DR   STRING; Q8BV99; -.
DR   Ensembl; ENSMUST00000025089; ENSMUSP00000025089; ENSMUSG00000024242.
DR   Ensembl; ENSMUST00000112389; ENSMUSP00000108008; ENSMUSG00000024242.
DR   MGI; MGI:2154405; Map4k3.
DR   eggNOG; roNOG11421; -.
DR   GeneTree; ENSGT00600000084124; -.
DR   InParanoid; Q8BV99; -.
DR   OrthoDB; EOG4MGS6R; -.
DR   ArrayExpress; Q8BV99; -.
DR   Bgee; Q8BV99; -.
DR   Genevestigator; Q8BV99; -.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   48 AA;  5406 MW;  51E70DAE22978D3A CRC64;
     EVTQEISDNT RIFRLLGSDR VVVLESRPTD NPTANSNLYI LAGHENSY
//
ID   TM222_MOUSE             Reviewed;         208 AA.
AC   Q8BVA2; A2AE96; Q8CI41; Q9CYN3;
DT   22-AUG-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Transmembrane protein 222;
GN   Name=Tmem222; Synonyms=D4Ertd196e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB30776.1; Type=Frameshift; Positions=50;
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DR   EMBL; AK017503; BAB30776.1; ALT_FRAME; mRNA.
DR   EMBL; AK079189; BAC37573.1; -; mRNA.
DR   EMBL; AL671882; CAM21070.1; -; Genomic_DNA.
DR   EMBL; BC037609; AAH37609.2; -; mRNA.
DR   IPI; IPI00111733; -.
DR   RefSeq; NP_079943.2; NM_025667.3.
DR   UniGene; Mm.244748; -.
DR   PRIDE; Q8BVA2; -.
DR   Ensembl; ENSMUST00000105907; ENSMUSP00000101527; ENSMUSG00000028857.
DR   GeneID; 52174; -.
DR   KEGG; mmu:52174; -.
DR   UCSC; uc008vcp.1; mouse.
DR   CTD; 52174; -.
DR   MGI; MGI:1098568; Tmem222.
DR   GeneTree; ENSGT00390000007371; -.
DR   HOVERGEN; HBG055708; -.
DR   OrthoDB; EOG4JM7QQ; -.
DR   NextBio; 308598; -.
DR   ArrayExpress; Q8BVA2; -.
DR   Bgee; Q8BVA2; -.
DR   Genevestigator; Q8BVA2; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR008496; DUF778.
DR   PANTHER; PTHR20921; DUF778; 1.
DR   Pfam; PF05608; DUF778; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    208       Transmembrane protein 222.
FT                                /FTId=PRO_0000247964.
FT   TOPO_DOM      1     55       Extracellular (Potential).
FT   TRANSMEM     56     76       Helical; (Potential).
FT   TOPO_DOM     77    164       Cytoplasmic (Potential).
FT   TRANSMEM    165    185       Helical; (Potential).
FT   TOPO_DOM    186    186       Extracellular (Potential).
FT   TRANSMEM    187    207       Helical; (Potential).
FT   TOPO_DOM    208    208       Cytoplasmic (Potential).
SQ   SEQUENCE   208 AA;  23180 MW;  FAF4B73BA2C0F965 CRC64;
     MAEAEGSSPL LLQPPPPPPR MAEVETPTGA ETDMKQYHGS GGVVMDVERS RFPYCVVWTP
     IPVLTWFFPI IGHMGICTSA GVIRDFAGPY FVSEDNMAFG KPAKFWKLDP GQVYASGPNA
     WDTAVHDASE EYKHRMHNLC CDNCHSHVAL ALNLMRYNNS TNWNMVTLCC FCLIYGKYVS
     VGAFVKTWLP FVLLLGIILT VSLVFNLR
//
ID   Q8BVB3_MOUSE            Unreviewed;       266 AA.
AC   Q8BVB3;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   30-NOV-2010, entry version 38.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Ttc15;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK079067; BAC37521.1; -; mRNA.
DR   IPI; IPI00655237; -.
DR   UniGene; Mm.132006; -.
DR   UniGene; Mm.341316; -.
DR   PRIDE; Q8BVB3; -.
DR   Ensembl; ENSMUST00000020954; ENSMUSP00000020954; ENSMUSG00000020628.
DR   MGI; MGI:2445089; Ttc15.
DR   HOVERGEN; HBG068042; -.
DR   InParanoid; Q8BVB3; -.
DR   ArrayExpress; Q8BVB3; -.
DR   Bgee; Q8BVB3; -.
DR   Genevestigator; Q8BVB3; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   266 AA;  28734 MW;  DDAEDAC892F69A6F CRC64;
     METAKDGEQS PSEASPLAQA GPENIPEPMS REEESQPLCH EETIDLGGDE FASEENEPTS
     EGSHNFGDKL NEHMMESVLI SDSPNNSEGD VGDLGCLQDV GEPPRGATDH RLPSSTDKEV
     VDTLSNGSET DGDDTPRDIS DMTPDSRASL KEDSTQEDVT SMPALENAAT EEVGPKDSLA
     PREEQTSEVS SNQSSSKXEP LPVCTIFSQA NATPSKPHLF LQDGFESQMV KSPSFSSTSE
     TSAKTPPPMV QPSSQPQYIF WRYNEL
//
ID   VATH_MOUSE              Reviewed;         483 AA.
AC   Q8BVE3; Q921X8;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=V-type proton ATPase subunit H;
DE            Short=V-ATPase subunit H;
DE   AltName: Full=Vacuolar proton pump subunit H;
GN   Name=Atp6v1h;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 76-86; 108-116; 263-278; 284-290; 342-360; 397-419
RP   AND 450-458, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase.
CC       Subunit H activates the ATPase activity of the enzyme and couples
CC       ATPase activity to proton flow. Vacuolar ATPase is responsible for
CC       acidifying a variety of intracellular compartments in eukaryotic
CC       cells, thus providing most of the energy required for transport
CC       processes in the vacuolar system. Involved in the endocytosis
CC       mediated by clathrin-coated pits, required for the formation of
CC       endosomes (By similarity).
CC   -!- SUBUNIT: V-ATPase is an heteromultimeric enzyme composed of a
CC       peripheral catalytic V1 complex (components A to H) attached to an
CC       integral membrane V0 proton pore complex (components: a, c, c',
CC       c'' and d). Interacts with AP2M1 (By similarity).
CC   -!- SIMILARITY: Belongs to the V-ATPase H subunit family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK078767; BAC37382.1; -; mRNA.
DR   EMBL; BC009154; AAH09154.1; -; mRNA.
DR   IPI; IPI00311461; -.
DR   RefSeq; NP_598587.2; NM_133826.4.
DR   UniGene; Mm.27082; -.
DR   ProteinModelPortal; Q8BVE3; -.
DR   STRING; Q8BVE3; -.
DR   PhosphoSite; Q8BVE3; -.
DR   PRIDE; Q8BVE3; -.
DR   Ensembl; ENSMUST00000044369; ENSMUSP00000040756; ENSMUSG00000033793.
DR   GeneID; 108664; -.
DR   KEGG; mmu:108664; -.
DR   UCSC; uc007afn.1; mouse.
DR   CTD; 108664; -.
DR   MGI; MGI:1914864; Atp6v1h.
DR   GeneTree; ENSGT00390000003289; -.
DR   HOGENOM; HBG387727; -.
DR   HOVERGEN; HBG000459; -.
DR   InParanoid; Q8BVE3; -.
DR   OMA; PNVRYEA; -.
DR   OrthoDB; EOG4K9BC0; -.
DR   PhylomeDB; Q8BVE3; -.
DR   BRENDA; 3.6.3.14; 244.
DR   NextBio; 361187; -.
DR   ArrayExpress; Q8BVE3; -.
DR   Bgee; Q8BVE3; -.
DR   CleanEx; MM_ATP6V1H; -.
DR   Genevestigator; Q8BVE3; -.
DR   GermOnline; ENSMUSG00000033793; Mus musculus.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR004908; ATPase_V1-cplx_hsu.
DR   InterPro; IPR011987; ATPase_V1-cplx_hsu_C.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Gene3D; G3DSA:1.25.40.150; ATPase_V1_H_C; 1.
DR   PANTHER; PTHR10698; ATPase_V1_H; 1.
DR   Pfam; PF03224; V-ATPase_H; 1.
DR   Pfam; PF11698; V-ATPase_H_C; 1.
DR   PIRSF; PIRSF032184; ATPase_V1_H; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrogen ion transport; Ion transport;
KW   Phosphoprotein; Transport.
FT   CHAIN         1    483       V-type proton ATPase subunit H.
FT                                /FTId=PRO_0000124194.
FT   MOD_RES     483    483       Phosphoserine (By similarity).
FT   CONFLICT    247    247       I -> V (in Ref. 2; AAH09154).
SQ   SEQUENCE   483 AA;  55855 MW;  A976B7DC889B84CD CRC64;
     MTKMDIRGAV DAAVPTNIIA AKAAEVRANK VNWQSYLQGQ MISAEDCEFI QRFEMKRSSE
     DKQEMLQTEG SQCAKTFINL MTHISKEQTV QYILTMVDDM LQENHQRVSI FFDYAKRSKS
     TAWPYFLPML NRQDPFTVHM AARIIAKLAA WGKELMEGSD LNYYFNWIKT QLSSQKLRGS
     GVAVETGTIS SSDSSQYVQC VAGCLQLMLR VNEYRFAWVE ADGVNCIMGV LSNKCGFQLQ
     YQMIFSIWLL AFSPQMCEHL RRYNIIPVLS DILQESVKEK VTRIILAAFR NFLEKSTERE
     TRQEYALAMI QCKVLKQLEN LEQQKYDDED ISEDIKFLLE KLGESVQDLS SFDEYSSELK
     SGRLEWSPVH KSEKFWRENA VRLNEKNYEL LKILTKLLEV SDDPQVLAVA AHDVGEYVRH
     YPRGKRVIEQ LGGKQLVMNH MHHEDQQVRY NALLAVQKLM VHNWEYLGKQ LQSEQPQTAA
     ARS
//
ID   PDCL3_MOUSE             Reviewed;         240 AA.
AC   Q8BVF2; Q3TH06; Q99JX2; Q9D0W3;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Phosducin-like protein 3;
DE   AltName: Full=Viral IAP-associated factor 1;
DE            Short=VIAF-1;
GN   Name=Pdcl3; Synonyms=Viaf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15371430; DOI=10.1074/jbc.M409623200;
RA   Wilkinson J.C., Richter B.W.M., Wilkinson A.S., Burstein E.,
RA   Rumble J.M., Balliu B., Duckett C.S.;
RT   "VIAF, a conserved inhibitor of apoptosis (IAP)-interacting factor
RT   that modulates caspase activation.";
RL   J. Biol. Chem. 279:51091-51099(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-237, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
CC   -!- FUNCTION: Modulates the activation of caspases during apoptosis
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the phosducin family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF110512; AAG21888.1; -; mRNA.
DR   EMBL; AK004334; BAB23267.1; -; mRNA.
DR   EMBL; AK078372; BAC37242.1; -; mRNA.
DR   EMBL; AK168509; BAE40392.1; -; mRNA.
DR   EMBL; BC005601; AAH05601.1; -; mRNA.
DR   IPI; IPI00311476; -.
DR   RefSeq; NP_081126.2; NM_026850.4.
DR   UniGene; Mm.28121; -.
DR   ProteinModelPortal; Q8BVF2; -.
DR   SMR; Q8BVF2; 16-208.
DR   PhosphoSite; Q8BVF2; -.
DR   PRIDE; Q8BVF2; -.
DR   Ensembl; ENSMUST00000027247; ENSMUSP00000027247; ENSMUSG00000026078.
DR   GeneID; 68833; -.
DR   KEGG; mmu:68833; -.
DR   UCSC; uc007atc.1; mouse.
DR   CTD; 68833; -.
DR   MGI; MGI:1916083; Pdcl3.
DR   eggNOG; roNOG07260; -.
DR   GeneTree; ENSGT00530000062970; -.
DR   HOGENOM; HBG316414; -.
DR   HOVERGEN; HBG108238; -.
DR   InParanoid; Q8BVF2; -.
DR   OMA; EISGQDY; -.
DR   OrthoDB; EOG4ZCT5P; -.
DR   PhylomeDB; Q8BVF2; -.
DR   NextBio; 328015; -.
DR   ArrayExpress; Q8BVF2; -.
DR   Bgee; Q8BVF2; -.
DR   CleanEx; MM_PDCL3; -.
DR   Genevestigator; Q8BVF2; -.
DR   GermOnline; ENSMUSG00000026078; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Cytoplasm; Phosphoprotein.
FT   CHAIN         1    240       Phosducin-like protein 3.
FT                                /FTId=PRO_0000163759.
FT   COMPBIAS     24     73       Glu-rich.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      44     44       Phosphoserine (By similarity).
FT   MOD_RES     235    235       Phosphoserine.
FT   MOD_RES     237    237       Phosphoserine.
FT   CONFLICT     59     59       Missing (in Ref. 2; BAB23267).
FT   CONFLICT    216    216       P -> L (in Ref. 3; AAH05601).
SQ   SEQUENCE   240 AA;  27581 MW;  446AB65099164E09 CRC64;
     MQDPNADTEW NDILRKKGIL PPKESLKELE EEEAEKEEQL LQQSVVKTYE DMTLEELEEN
     EDEFSEEDER AIEMYRQQRL AEWKATQLKN KFGEVLEISG KDYVQEVTKA GEGLWVILHL
     YKQGIPLCSL INHHLSGLAR KFPDVKFIKA ISTTCIPNYP DRNLPTVFVY REGDIKAQFI
     GPLVFGGMNL TIDELEWKLS ESGAIKTALE ENPKKPIQDL LLSSVRGPVP MRRDSDSEDD
//
ID   DPP9_MOUSE              Reviewed;         862 AA.
AC   Q8BVG4; Q6KAM9; Q8BWT9;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Dipeptidyl peptidase 9;
DE            Short=DP9;
DE            EC=3.4.14.5;
DE   AltName: Full=Dipeptidyl peptidase IX;
DE            Short=DPP IX;
DE   AltName: Full=Dipeptidyl peptidase-like protein 9;
DE            Short=DPLP9;
GN   Name=Dpp9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Liver, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Thymus;
RX   PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of FLJ genes:
RT   the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:127-135(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Dipeptidyl peptidase that cleaves off N-terminal
CC       dipeptides from proteins having a Pro or Ala residue at position 2
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal dipeptide, Xaa-Yaa-|-
CC       Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided
CC       Zaa is neither Pro nor hydroxyproline.
CC   -!- ENZYME REGULATION: Inhibited by the serine proteinase inhibitor 4-
CC       (2-aminoethyl)benzenesulphonyl fluoride (AEBSF), and by di-
CC       isopropylfuorophosphate (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BVG4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BVG4-2; Sequence=VSP_013870, VSP_013871, VSP_013872;
CC   -!- SIMILARITY: Belongs to the peptidase S9B family. DPPIV subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD21428.1; Type=Frameshift; Positions=745;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK050021; BAC34034.1; -; mRNA.
DR   EMBL; AK078301; BAC37211.1; -; mRNA.
DR   EMBL; AK131178; BAD21428.1; ALT_SEQ; mRNA.
DR   EMBL; BC057631; AAH57631.1; -; mRNA.
DR   IPI; IPI00462461; -.
DR   IPI; IPI00606731; -.
DR   RefSeq; NP_766212.2; NM_172624.3.
DR   UniGene; Mm.205535; -.
DR   UniGene; Mm.478753; -.
DR   ProteinModelPortal; Q8BVG4; -.
DR   SMR; Q8BVG4; 46-862.
DR   STRING; Q8BVG4; -.
DR   MEROPS; S09.019; -.
DR   PhosphoSite; Q8BVG4; -.
DR   PRIDE; Q8BVG4; -.
DR   Ensembl; ENSMUST00000038794; ENSMUSP00000046604; ENSMUSG00000001229.
DR   Ensembl; ENSMUST00000113056; ENSMUSP00000108679; ENSMUSG00000001229.
DR   GeneID; 224897; -.
DR   KEGG; mmu:224897; -.
DR   UCSC; uc008dbh.1; mouse.
DR   CTD; 224897; -.
DR   MGI; MGI:2443967; Dpp9.
DR   eggNOG; roNOG11966; -.
DR   GeneTree; ENSGT00530000062751; -.
DR   HOGENOM; HBG356013; -.
DR   HOVERGEN; HBG061620; -.
DR   InParanoid; Q8BVG4; -.
DR   OMA; RHGSKIW; -.
DR   OrthoDB; EOG4BVRSX; -.
DR   BRENDA; 3.4.14.5; 244.
DR   NextBio; 377440; -.
DR   ArrayExpress; Q8BVG4; -.
DR   Bgee; Q8BVG4; -.
DR   CleanEx; MM_DPP9; -.
DR   Genevestigator; Q8BVG4; -.
DR   GermOnline; ENSMUSG00000001229; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002469; Peptidase_S9B.
DR   Pfam; PF00930; DPPIV_N; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Aminopeptidase; Cytoplasm;
KW   Hydrolase; Protease; Serine protease.
FT   CHAIN         1    862       Dipeptidyl peptidase 9.
FT                                /FTId=PRO_0000122416.
FT   ACT_SITE    729    729       Charge relay system (By similarity).
FT   ACT_SITE    807    807       Charge relay system (By similarity).
FT   ACT_SITE    839    839       Charge relay system (By similarity).
FT   MOD_RES      50     50       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1     75       Missing (in isoform 2).
FT                                /FTId=VSP_013870.
FT   VAR_SEQ     748    787       VAIAGAPVTVWMAYDTGYTERYMDVPENNQQGYEAGSVAL
FT                                -> PPHEAESPSSLPATTDPRMASASSSMWEAKPGTPASEG
FT                                QR (in isoform 2).
FT                                /FTId=VSP_013871.
FT   VAR_SEQ     788    862       Missing (in isoform 2).
FT                                /FTId=VSP_013872.
FT   CONFLICT    369    369       D -> Y (in Ref. 1; BAC37211).
FT   CONFLICT    546    546       S -> F (in Ref. 2; BAD21428).
FT   CONFLICT    777    777       Q -> K (in Ref. 1; BAC37211).
SQ   SEQUENCE   862 AA;  98001 MW;  B1D566E824A834E8 CRC64;
     MCSGVSPVEQ VAAGDMDDTA ARFCVQKHSW DGLRSIIHGS RKSSGLIVSK APHDFQFVQK
     PDESGPHSHR LYYLGMPYGS RENSLLYSEI PKKVRKEALL LLSWKQMLDH FQATPHHGVY
     SREEELLRER KRLGVFGITS YDFHSESGLF LFQASNSLFH CRDGGKNGFM VSPMKPLEIK
     TQCSGPRMDP KICPADPAFF SFINNSDLWV ANIETGEERR LTFCHQGSAG VLDNPKSAGV
     ATFVIQEEFD RFTGCWWCPT ASWEGSEGLK TLRILYEEVD ESEVEVIHVP SPALEERKTD
     SYRYPRTGSK NPKIALKLAE LQTDHQGKIV SSCEKELVQP FSSLFPKVEY IARAGWTRDG
     KYAWAMFLDR PQQRLQLVLL PPALFIPAVE SEAQRQAAAR AVPKNVQPFV IYEEVTNVWI
     NVHDIFHPFP QAEGQQDFCF LRANECKTGF CHLYRVTVEL KTKDYDWTEP LSPTEDEFKC
     PIKEEVALTS GEWEVLSRHG SKIWVNEQTK LVYFQGTKDT PLEHHLYVVS YESAGEIVRL
     TTLGFSHSCS MSQSFDMFVS HYSSVSTPPC VHVYKLSGPD DDPLHKQPRF WASMMEAANC
     PPDYVPPEIF HFHTRADVQL YGMIYKPHTL QPGRKHPTVL FVYGGPQVQL VNNSFKGIKY
     LRLNTLASLG YAVVVIDGRG SCQRGLHFEG ALKNQMGQVE IEDQVEGLQY VAEKYGFIDL
     SRVAIHGWSY GGFLSLMGLI HKPQVFKVAI AGAPVTVWMA YDTGYTERYM DVPENNQQGY
     EAGSVALHVE KLPNEPNRLL ILHGFLDENV HFFHTNFLVS QLIRAGKPYQ LQIYPNERHS
     IRCRESGEHY EVTLLHFLQE HL
//
ID   SNX17_MOUSE             Reviewed;         470 AA.
AC   Q8BVL3; Q8R0N8;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Sorting nexin-17;
GN   Name=Snx17;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH LDLR; VLDLR; LRP1 AND LRP8, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=12169628; DOI=10.1093/emboj/cdf435;
RA   Stockinger W., Sailler B., Strasser V., Recheis B., Fasching D.,
RA   Kahr L., Schneider W.J., Nimpf J.;
RT   "The PX-domain protein SNX17 interacts with members of the LDL
RT   receptor family and modulates endocytosis of the LDL receptor.";
RL   EMBO J. 21:4259-4267(2002).
RN   [4]
RP   INTERACTION WITH LRP1, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=16052210; DOI=10.1038/sj.emboj.7600756;
RA   van Kerkhof P., Lee J., McCormick L., Tetrault E., Lu W.,
RA   Schoenfish M., Oorschot V., Strous G.J., Klumperman J., Bu G.;
RT   "Sorting nexin 17 facilitates LRP recycling in the early endosome.";
RL   EMBO J. 24:2851-2861(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-334, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437 AND SER-440, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409; SER-421 AND
RP   SER-440, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May be involved in protein trafficking.
CC   -!- SUBUNIT: Interacts with the C-termini of P-selectin, PTC, LDLR,
CC       VLDLR, LRP1 and LRP8.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Early endosome. Note=Associated
CC       with early endosomes.
CC   -!- TISSUE SPECIFICITY: Broadly expressed, with highest levels in
CC       brain and placenta, and lowest levels in colon, intestine and
CC       liver.
CC   -!- DOMAIN: The PX domain is required for association with endosomes
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the sorting nexin family.
CC   -!- SIMILARITY: Contains 1 PX (phox homology) domain.
CC   -!- SIMILARITY: Contains 1 Ras-associating domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK077650; BAC36927.1; -; mRNA.
DR   EMBL; AK077780; BAC37004.1; -; mRNA.
DR   EMBL; AK156299; BAE33663.1; -; mRNA.
DR   EMBL; BC026571; AAH26571.1; -; mRNA.
DR   EMBL; BC023732; AAH23732.1; -; mRNA.
DR   IPI; IPI00230486; -.
DR   RefSeq; NP_710147.1; NM_153680.2.
DR   UniGene; Mm.6118; -.
DR   ProteinModelPortal; Q8BVL3; -.
DR   SMR; Q8BVL3; 1-109.
DR   STRING; Q8BVL3; -.
DR   PhosphoSite; Q8BVL3; -.
DR   PRIDE; Q8BVL3; -.
DR   Ensembl; ENSMUST00000031029; ENSMUSP00000031029; ENSMUSG00000029146.
DR   GeneID; 266781; -.
DR   KEGG; mmu:266781; -.
DR   NMPDR; fig|10090.3.peg.11392; -.
DR   UCSC; uc008wxm.1; mouse.
DR   CTD; 266781; -.
DR   MGI; MGI:2387801; Snx17.
DR   eggNOG; roNOG13762; -.
DR   GeneTree; ENSGT00530000063147; -.
DR   HOGENOM; HBG713823; -.
DR   HOVERGEN; HBG061207; -.
DR   InParanoid; Q8BVL3; -.
DR   OMA; DIEHGWI; -.
DR   OrthoDB; EOG49KFQH; -.
DR   PhylomeDB; Q8BVL3; -.
DR   NextBio; 392194; -.
DR   ArrayExpress; Q8BVL3; -.
DR   Bgee; Q8BVL3; -.
DR   CleanEx; MM_SNX17; -.
DR   Genevestigator; Q8BVL3; -.
DR   GermOnline; ENSMUSG00000029146; Mus musculus.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; IDA:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR001683; Phox.
DR   InterPro; IPR000159; Ras-assoc.
DR   Gene3D; G3DSA:3.30.1520.10; PX; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; PX; 1.
DR   PROSITE; PS50195; PX; 1.
DR   PROSITE; PS50200; RA; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Endosome; Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1    470       Sorting nexin-17.
FT                                /FTId=PRO_0000236205.
FT   DOMAIN        1    109       PX.
FT   DOMAIN      115    206       Ras-associating.
FT   MOD_RES     334    334       Phosphothreonine.
FT   MOD_RES     407    407       Phosphoserine (By similarity).
FT   MOD_RES     409    409       Phosphoserine.
FT   MOD_RES     415    415       Phosphoserine (By similarity).
FT   MOD_RES     421    421       Phosphoserine.
FT   MOD_RES     437    437       Phosphoserine.
FT   MOD_RES     440    440       Phosphoserine.
FT   CONFLICT    198    198       K -> E (in Ref. 1; BAC37004).
SQ   SEQUENCE   470 AA;  52797 MW;  3023B5FAEF38BB42 CRC64;
     MHFSIPETES RSGDSGGSAY VAYNIHVNGV LHCRVRYSQL LGLHEQLRKE YGANVVPAFP
     PKKLFSLTPA EVEQRREQLE KYMQAVRQDP LLGSSETFNS FLRRAQQETQ QVPTEEVSLE
     VLLSNGQKVL VTVLTSDQTE DVLEAVAAKL DLPDDLIGYF SLFLVREKED GAFSFVRKLQ
     EFELPYVSVT SLRSQEYKIV LRKSYWDSAY DDDVMENRVG LNLLYAQTVS DIEHGWILVT
     KEQHRQLKSL QEKVSKKEFL RLAQTLRHYG YLRFDACVAD FPEKDCPVVV SAGNSELSLQ
     LRLPGQQLRE GSFRVTRMRC WRVTSSVPLP SGGTSSPSRG RGEVRLELAF EYLMSKDRLQ
     WVTITSPQAI MMSICLQSMV DELMVKKSGG SIRKMLRRRV GGTLRRSDSQ QAVKSPPLLE
     SPDASRESMV KLSSKLSAVS LRGIGSPSTD ASASAVHGNF AFEGIGDEDL
//
ID   JKIP1_MOUSE             Reviewed;         626 AA.
AC   Q8BVL9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Janus kinase and microtubule-interacting protein 1;
DE   AltName: Full=GABA-B receptor-binding protein;
DE   AltName: Full=Multiple alpha-helices and RNA-linker protein 1;
DE            Short=Marlin-1;
GN   Name=Jakmip1; Synonyms=Gababrbp, Marlin1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   INTERACTION WITH GABBR1.
RX   PubMed=14718537; DOI=10.1074/jbc.M311737200;
RA   Couve A., Restituito S., Brandon J.M., Charles K.J., Bawagan H.,
RA   Freeman K.B., Pangalos M.N., Calver A.R., Moss S.J.;
RT   "Marlin-1, a novel RNA-binding protein associates with GABA
RT   receptors.";
RL   J. Biol. Chem. 279:13934-13943(2004).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH KIF5B.
RX   PubMed=17532644; DOI=10.1016/j.mcn.2007.04.008;
RA   Vidal R.L., Ramirez O.A., Sandoval L., Koenig-Robert R., Haertel S.,
RA   Couve A.;
RT   "Marlin-1 and conventional kinesin link GABAB receptors to the
RT   cytoskeleton and regulate receptor transport.";
RL   Mol. Cell. Neurosci. 35:501-512(2007).
CC   -!- FUNCTION: Associates with microtubules and may play a role in the
CC       microtubule-dependent transport of the GABA-B receptor. May play a
CC       role in JAK1 signaling and regulate microtubule cytoskeleton
CC       rearrangements.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with JAK1 and TYK2
CC       (By similarity). Forms a complex with GABBR1 and KIF5B/kinesin-1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Membrane; Peripheral membrane protein (By similarity).
CC       Note=Colocalizes with the microtubule network. Localizes to the
CC       cell body and neurites of hippocampal neurons where it accumulates
CC       in granules. Localizes to the tail and to a lower extent to the
CC       head of sperm cells (By similarity).
CC   -!- PTM: Phosphorylated (By similarity).
CC   -!- SIMILARITY: Belongs to the JAKMIP family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK077298; BAC36736.1; -; mRNA.
DR   IPI; IPI00880630; -.
DR   RefSeq; NP_848481.2; NM_178394.4.
DR   UniGene; Mm.85280; -.
DR   HSSP; P17676; 1GU4.
DR   ProteinModelPortal; Q8BVL9; -.
DR   STRING; Q8BVL9; -.
DR   PhosphoSite; Q8BVL9; -.
DR   PRIDE; Q8BVL9; -.
DR   Ensembl; ENSMUST00000043794; ENSMUSP00000038504; ENSMUSG00000063646.
DR   GeneID; 76071; -.
DR   KEGG; mmu:76071; -.
DR   UCSC; uc008xfj.1; mouse.
DR   CTD; 76071; -.
DR   MGI; MGI:1923321; Jakmip1.
DR   eggNOG; roNOG06752; -.
DR   GeneTree; ENSGT00390000002812; -.
DR   HOVERGEN; HBG054249; -.
DR   OrthoDB; EOG4BVRT5; -.
DR   NextBio; 344541; -.
DR   ArrayExpress; Q8BVL9; -.
DR   Bgee; Q8BVL9; -.
DR   Genevestigator; Q8BVL9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0019894; F:kinesin binding; IPI:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Membrane; Microtubule;
KW   Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1    626       Janus kinase and microtubule-interacting
FT                                protein 1.
FT                                /FTId=PRO_0000323009.
FT   REGION        1    365       Mediates association with microtubules
FT                                (By similarity).
FT   REGION      365    626       Mediates interaction with TYK2 and GABBR1
FT                                (By similarity).
FT   COILED       13    255       Potential.
FT   COILED      284    413       Potential.
FT   COILED      490    604       Potential.
FT   MOD_RES     382    382       Phosphoserine (By similarity).
FT   MOD_RES     470    470       Phosphothreonine (By similarity).
SQ   SEQUENCE   626 AA;  73040 MW;  B3562FC99FDD9013 CRC64;
     MSKKGRSKGD KPEAETDSVQ MANEELRAKL TNIQIEFQQE KSKVGKLRER LQEAKLEREQ
     EQRRHTAYIS ELKAKLHEEK TKELQALREA LIRQHEQEAA RTAKIKEGEL QRLQATLNVL
     RDGAADKVKT ALLADAREEA RRTFDGERQR LQQEILELKA ARKQAEEALS NCMQADKAKA
     ADLRAAYQAH QDEVHRIKRE CERDIRGLMD EIKGKERVIL ALEKELGVQT GQTQRLLLQK
     EALDEQLVQV KEAERHHSSP KRELPPGIGD MAELMGGQDQ HMDERDVRRF QLKIAELNSV
     IRKLEDRNTL LADERNELLK RSRETEVQLK PLVEKNKRMN KKNEELLHSI QRMEEKLKSL
     TRENVEMKEK LSAQASLKRH TSLNDLSLTR DEQEIEFLRL QVLEQQHVID DLSLERERLL
     RSKRHRGKSL KPPKKHVVET FFGFDEESVD SETLSETSYN TDRTDRTPAT PEEDLDETTT
     REEADLRFCQ LTREYQALQR AYALLQEQVG GTLDAEREAR TREQLQADLL RCQAKIEDLE
     KLLVEKGQDA AWVEEKQVLM RTNQDLLEKI YRLEMEENQL KSEMQDAKDQ NELLEFRVLE
     LEVRDSICCK LSNGADILFE PKLKFM
//
ID   KC1G2_MOUSE             Reviewed;         415 AA.
AC   Q8BVP5;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 68.
DE   RecName: Full=Casein kinase I isoform gamma-2;
DE            Short=CKI-gamma 2;
DE            EC=2.7.11.1;
GN   Name=Csnk1g2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Casein kinases are operationally defined by their
CC       preferential utilization of acidic proteins such as caseins as
CC       substrates. It can phosphorylate a large number of proteins.
CC       Participates in Wnt signaling (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- PTM: Autophosphorylated (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC       protein kinase family. Casein kinase I subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK077076; BAC36596.1; -; mRNA.
DR   EMBL; AK132871; BAE21399.1; -; mRNA.
DR   IPI; IPI00405343; -.
DR   RefSeq; NP_001153063.1; NM_001159591.1.
DR   RefSeq; NP_598763.1; NM_134002.2.
DR   UniGene; Mm.29873; -.
DR   ProteinModelPortal; Q8BVP5; -.
DR   SMR; Q8BVP5; 44-338.
DR   STRING; Q8BVP5; -.
DR   PhosphoSite; Q8BVP5; -.
DR   Ensembl; ENSMUST00000085435; ENSMUSP00000082560; ENSMUSG00000003345.
DR   GeneID; 103236; -.
DR   KEGG; mmu:103236; -.
DR   UCSC; uc007geb.1; mouse.
DR   CTD; 103236; -.
DR   MGI; MGI:1920014; Csnk1g2.
DR   eggNOG; roNOG05724; -.
DR   GeneTree; ENSGT00560000076651; -.
DR   HOVERGEN; HBG000176; -.
DR   PhylomeDB; Q8BVP5; -.
DR   BRENDA; 2.7.11.1; 244.
DR   ArrayExpress; Q8BVP5; -.
DR   Bgee; Q8BVP5; -.
DR   CleanEx; MM_CSNK1G2; -.
DR   Genevestigator; Q8BVP5; -.
DR   GermOnline; ENSMUSG00000003345; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR022247; Casein_kinase-1_gamma_C.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   Pfam; PF12605; CK1gamma_C; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.
FT   CHAIN         1    415       Casein kinase I isoform gamma-2.
FT                                /FTId=PRO_0000192843.
FT   DOMAIN       46    316       Protein kinase.
FT   NP_BIND      52     60       ATP (By similarity).
FT   ACT_SITE    165    165       Proton acceptor (By similarity).
FT   BINDING      75     75       ATP (By similarity).
FT   MOD_RES     366    366       Phosphoserine (By similarity).
FT   MOD_RES     367    367       Phosphothreonine (By similarity).
SQ   SEQUENCE   415 AA;  47582 MW;  C5EE5AFCF2F44677 CRC64;
     MDFDKKGGKG ELEEGRRMSK TGTSRSNHGV RSSGTSSGVL MVGPNFRVGK KIGCGNFGEL
     RLGKNLYTNE YVAIKLEPIK SRAPQLHLEY RFYKQLSTTE GVPQVYYFGP CGKYNAMVLE
     LLGPSLEDLF DLCDRTFTLK TVLMIAIQLI TRMEYVHTKS LIYRDVKPEN FLVGRPGSKR
     QHSIHIIDFG LAKEYIDPET KKHIPYREHK SLTGTARYMS INTHLGKEQS RRDDLEALGH
     MFMYFLRGSL PWQGLKADTL KERYQKIGDT KRATPIEVLC ESFPEEMATY LRYVRRLDFF
     EKPDYDYLRK LFTDLFDRSG YVFDYEYDWA GKPLPTPIGT VHPDVPSQPP HRDKAQLHTK
     NQALNSTNGE LNTDDPTAGH SNAPIAAPAE VEVADETKCC CFFKRRKRKS LQRHK
//
ID   PPME1_MOUSE             Reviewed;         386 AA.
AC   Q8BVQ5; Q3U392; Q3UJX8; Q3UKE0; Q8K311; Q91YR8; Q9CSP7;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 5.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Protein phosphatase methylesterase 1;
DE            Short=PME-1;
DE            EC=3.1.1.-;
GN   Name=Ppme1; Synonyms=Pme1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, Embryo, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE, AND TISSUE SPECIFICITY.
RX   MEDLINE=99254004; PubMed=10318862; DOI=10.1074/jbc.274.20.14382;
RA   Ogris E., Du X., Nelson K.C., Mak E.K., Yu X.X., Lane W.S.,
RA   Pallas D.C.;
RT   "A protein phosphatase methylesterase (PME-1) is one of several novel
RT   proteins stably associating with two inactive mutants of protein
RT   phosphatase 2A.";
RL   J. Biol. Chem. 274:14382-14391(1999).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: Demethylates proteins that have been reversibly
CC       carboxymethylated. Demethylates PPP2CB (in vitro) (By similarity).
CC   -!- SUBUNIT: Binds PPP2CB (By similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in testis and
CC       brain.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE32896.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK012256; BAB28122.1; -; mRNA.
DR   EMBL; AK146051; BAE26861.1; -; mRNA.
DR   EMBL; AK146268; BAE27027.1; -; mRNA.
DR   EMBL; AK154876; BAE32896.1; ALT_INIT; mRNA.
DR   EMBL; BC014867; AAH14867.1; -; mRNA.
DR   EMBL; BC029064; AAH29064.1; -; mRNA.
DR   IPI; IPI00415908; -.
DR   RefSeq; NP_082568.1; NM_028292.2.
DR   UniGene; Mm.177502; -.
DR   ProteinModelPortal; Q8BVQ5; -.
DR   SMR; Q8BVQ5; 39-376.
DR   DIP; DIP-46211N; -.
DR   STRING; Q8BVQ5; -.
DR   MEROPS; S33.984; -.
DR   PhosphoSite; Q8BVQ5; -.
DR   PRIDE; Q8BVQ5; -.
DR   Ensembl; ENSMUST00000032963; ENSMUSP00000032963; ENSMUSG00000030718.
DR   GeneID; 72590; -.
DR   KEGG; mmu:72590; -.
DR   UCSC; uc009imu.1; mouse.
DR   CTD; 72590; -.
DR   MGI; MGI:1919840; Ppme1.
DR   eggNOG; roNOG08701; -.
DR   GeneTree; ENSGT00390000004396; -.
DR   HOVERGEN; HBG053622; -.
DR   InParanoid; Q8BVQ5; -.
DR   OMA; SMQSFLR; -.
DR   OrthoDB; EOG4N8R52; -.
DR   PhylomeDB; Q8BVQ5; -.
DR   NextBio; 336561; -.
DR   ArrayExpress; Q8BVQ5; -.
DR   Bgee; Q8BVQ5; -.
DR   CleanEx; MM_PPME1; -.
DR   Genevestigator; Q8BVQ5; -.
DR   GermOnline; ENSMUSG00000030718; Mus musculus.
DR   GO; GO:0051722; F:protein C-terminal methylesterase activity; ISS:HGNC.
DR   GO; GO:0051721; F:protein phosphatase 2A binding; ISS:HGNC.
DR   GO; GO:0006482; P:protein demethylation; ISS:HGNC.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   InterPro; IPR016812; PPase_methylesterase_euk.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PIRSF; PIRSF022950; PPase_methylesterase_euk; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   PROSITE; PS00120; LIPASE_SER; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Hydrolase; Phosphoprotein;
KW   Serine esterase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    386       Protein phosphatase methylesterase 1.
FT                                /FTId=PRO_0000090391.
FT   COMPBIAS    256    263       Poly-Glu.
FT   ACT_SITE    156    156       Potential.
FT   MOD_RES       6      6       N6-acetyllysine (By similarity).
FT   MOD_RES      15     15       Phosphoserine (By similarity).
FT   MOD_RES      27     27       Phosphoserine.
FT   MOD_RES     243    243       Phosphoserine (By similarity).
FT   CONFLICT     17     17       P -> T (in Ref. 1; BAE27027).
FT   CONFLICT     86     86       G -> D (in Ref. 2; AAH29064).
FT   CONFLICT    370    370       H -> R (in Ref. 1; BAE27027).
SQ   SEQUENCE   386 AA;  42256 MW;  2BD07B588299DB6D CRC64;
     MSALEKSMHL GRLPSRPPLP GSGGSQSGAK MRMGPGRKRD FTPVPWSQYF ESMEDVEVEN
     ETGKDTFRVY KSGSEGPVLL LLHGGGHSAL SWAVFTAAII SRVQCRIVAL DLRGHGETKV
     KNSEDLSAET MAKDVGNVVE AMYGDLPPPV MLIGHSMGGA IAVHTAAANL VPSLLGLCMI
     DVVEGTAMDA LNSMQNFLRG RPKTFKSLEN AIEWSVKSGQ IRNLESARVS MVGQVKQCEG
     ITSPEGSKSI VEGIIEEEEE DEEGSESVNK RKKEDDMETK KDHPYTWRIE LAKTEKYWDG
     WFRGLSNLFL SCPIPKLLLL AGVDRLDKDL TIGQMQGKFQ MQVLPQCGHA VHEDAPDKVA
     EAVATFLIRH RFAEPIGGFQ CVFPGC
//
ID   RSPRY_MOUSE             Reviewed;         576 AA.
AC   Q8BVR6; Q3T9F1; Q3TM35; Q3U802; Q3UKF9; Q3UYN5; Q8BMH0; Q8C039;
AC   Q9CZ54;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=RING finger and SPRY domain-containing protein 1;
DE   Flags: Precursor;
GN   Name=Rspry1; Synonyms=Kiaa1972;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Thymus;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Amnion, Embryo, Mammary gland, Medulla oblongata,
RC   Olfactory bulb, Spinal cord, Spleen, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Embryo, and Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Secreted (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BVR6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BVR6-2; Sequence=VSP_023385, VSP_023386;
CC       Name=3;
CC         IsoId=Q8BVR6-3; Sequence=VSP_023384;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 B30.2/SPRY domain.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE22177.1; Type=Frameshift; Positions=541;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK173313; BAD32591.1; -; mRNA.
DR   EMBL; AK013003; BAB28589.1; -; mRNA.
DR   EMBL; AK031153; BAC27283.1; -; mRNA.
DR   EMBL; AK032416; BAC27858.1; -; mRNA.
DR   EMBL; AK076799; BAC36485.1; -; mRNA.
DR   EMBL; AK134544; BAE22177.1; ALT_FRAME; mRNA.
DR   EMBL; AK141443; BAE24686.1; -; mRNA.
DR   EMBL; AK146028; BAE26842.1; -; mRNA.
DR   EMBL; AK150941; BAE29976.1; -; mRNA.
DR   EMBL; AK152435; BAE31217.1; -; mRNA.
DR   EMBL; AK166167; BAE38607.1; -; mRNA.
DR   EMBL; AK172567; BAE43070.1; -; mRNA.
DR   EMBL; BC010833; AAH10833.2; -; mRNA.
DR   EMBL; BC054121; AAH54121.1; -; mRNA.
DR   IPI; IPI00223590; -.
DR   IPI; IPI00654218; -.
DR   IPI; IPI00828718; -.
DR   RefSeq; NP_080550.3; NM_026274.4.
DR   UniGene; Mm.109074; -.
DR   ProteinModelPortal; Q8BVR6; -.
DR   SMR; Q8BVR6; 523-570.
DR   PRIDE; Q8BVR6; -.
DR   Ensembl; ENSMUST00000060389; ENSMUSP00000057275; ENSMUSG00000050079.
DR   GeneID; 67610; -.
DR   KEGG; mmu:67610; -.
DR   UCSC; uc009mwq.1; mouse.
DR   CTD; 67610; -.
DR   MGI; MGI:1914860; Rspry1.
DR   eggNOG; roNOG11119; -.
DR   GeneTree; ENSGT00530000063442; -.
DR   HOVERGEN; HBG057205; -.
DR   InParanoid; Q8BVR6; -.
DR   OMA; GHPAKHR; -.
DR   OrthoDB; EOG4QFWCZ; -.
DR   PhylomeDB; Q8BVR6; -.
DR   NextBio; 325045; -.
DR   ArrayExpress; Q8BVR6; -.
DR   Bgee; Q8BVR6; -.
DR   CleanEx; MM_RSPRY1; -.
DR   Genevestigator; Q8BVR6; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001870; B302/SPRY.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR018355; SPla/RYanodine_receptor_sg.
DR   InterPro; IPR003877; SPRY_rcpt.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Metal-binding; Secreted; Signal;
KW   Zinc; Zinc-finger.
FT   SIGNAL        1     16       Potential.
FT   CHAIN        17    576       RING finger and SPRY domain-containing
FT                                protein 1.
FT                                /FTId=PRO_0000278788.
FT   DOMAIN      300    483       B30.2/SPRY.
FT   ZN_FING     527    562       RING-type.
FT   CARBOHYD     65     65       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1    124       Missing (in isoform 3).
FT                                /FTId=VSP_023384.
FT   VAR_SEQ     117    117       N -> K (in isoform 2).
FT                                /FTId=VSP_023385.
FT   VAR_SEQ     118    576       Missing (in isoform 2).
FT                                /FTId=VSP_023386.
FT   CONFLICT     54     54       D -> N (in Ref. 2; BAE43070).
FT   CONFLICT     67     67       T -> A (in Ref. 2; BAE38607).
FT   CONFLICT    250    250       L -> M (in Ref. 2; BAC27858).
FT   CONFLICT    527    527       C -> Y (in Ref. 2; BAE22177).
SQ   SEQUENCE   576 AA;  64322 MW;  823C3532FCE18387 CRC64;
     MIVFGWAVFL ASRSLGQGLL LTLEEHIAHL LGTTGATATM GNSCICRDDS GAEDNVDTHQ
     QQAENSTVPT ADSRSQPRDP VRPPRRGRGP HEPRRKKQNV DGLVLDTLAV IRTLVDNDQE
     PPYSMITLHE MAETDEGWLD VVQSLIRVIP LEDPLGPAVI TLLLDECPLP TKDALQKLTE
     ILNLNGEVAC QDSGHPAKHR NTSAVLGCLA EKLAGPASIG LLSPGILEYL LQCLKLQSHP
     TVMLFALIAL EKFAQTSENK LTISESSISD RLVTLELWAD DPDYLKRQVG FCAQWSLDNL
     FLKEGRQLTY EKVDLNNIRA MLNSNDVSEY LKISPHGLEA RCDASSFESV RCTFCVDTGV
     WYYEVTVVTS GVMQIGWATR DSKFLNHEGY GIGDDEYSCA YDGCRQLIWY NARSKPHVHP
     CWKEGDTVGF LLDLNEKQMI FFLNGNQLPP EKQVFSSTVS GFFAAASFMS YQQCEFNFGA
     RPFKYPPSMK FSTFNDYAFL TAEEKIILPR HRRLALLKQV SIRENCCSLC CDEVADTQLK
     PCGHSDLCMD CALQLETCPL CRKEIVSRIR QISHIS
//
ID   LRCH3_MOUSE             Reviewed;         778 AA.
AC   Q8BVU0; Q3U222; Q3UZ74;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Leucine-rich repeat and calponin homology domain-containing protein 3;
DE   Flags: Precursor;
GN   Name=Lrch3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Head, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Secreted (Potential).
CC   -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC   -!- SIMILARITY: Contains 9 LRR (leucine-rich) repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE21984.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAE33320.1; Type=Frameshift; Positions=37;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK134026; BAE21984.1; ALT_INIT; mRNA.
DR   EMBL; AK155550; BAE33320.1; ALT_FRAME; mRNA.
DR   EMBL; AK076529; BAC36380.1; -; mRNA.
DR   IPI; IPI00343346; -.
DR   UniGene; Mm.227918; -.
DR   ProteinModelPortal; Q8BVU0; -.
DR   SMR; Q8BVU0; 12-286, 650-761.
DR   PhosphoSite; Q8BVU0; -.
DR   PRIDE; Q8BVU0; -.
DR   Ensembl; ENSMUST00000023491; ENSMUSP00000023491; ENSMUSG00000022801.
DR   UCSC; uc007yzs.1; mouse.
DR   MGI; MGI:1917394; Lrch3.
DR   eggNOG; roNOG08117; -.
DR   GeneTree; ENSGT00590000082932; -.
DR   HOGENOM; HBG717214; -.
DR   HOVERGEN; HBG052350; -.
DR   InParanoid; Q8BVU0; -.
DR   OrthoDB; EOG4K3KVS; -.
DR   ArrayExpress; Q8BVU0; -.
DR   Bgee; Q8BVU0; -.
DR   Genevestigator; Q8BVU0; -.
DR   GermOnline; ENSMUSG00000022801; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF00560; LRR_1; 2.
DR   SMART; SM00033; CH; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS50021; CH; 1.
PE   2: Evidence at transcript level;
KW   Leucine-rich repeat; Phosphoprotein; Repeat; Secreted; Signal.
FT   SIGNAL        1     22       Potential.
FT   CHAIN        23    778       Leucine-rich repeat and calponin homology
FT                                domain-containing protein 3.
FT                                /FTId=PRO_0000253485.
FT   REPEAT       56     79       LRR 1.
FT   REPEAT       81    104       LRR 2.
FT   REPEAT      105    127       LRR 3.
FT   REPEAT      128    150       LRR 4.
FT   REPEAT      152    172       LRR 5.
FT   REPEAT      173    195       LRR 6.
FT   REPEAT      197    218       LRR 7.
FT   REPEAT      220    239       LRR 8.
FT   REPEAT      240    264       LRR 9.
FT   DOMAIN      645    758       CH.
FT   COMPBIAS    384    387       Poly-Glu.
FT   COMPBIAS    766    774       Poly-Gln.
FT   MOD_RES     324    324       Phosphoserine (By similarity).
FT   MOD_RES     415    415       Phosphoserine (By similarity).
FT   MOD_RES     419    419       Phosphoserine (By similarity).
FT   CONFLICT     92     92       N -> D (in Ref. 1; BAC36380).
FT   CONFLICT    168    168       E -> K (in Ref. 1; BAC36380).
FT   CONFLICT    177    177       K -> E (in Ref. 1; BAC36380).
FT   CONFLICT    206    206       N -> I (in Ref. 1; BAC36380).
SQ   SEQUENCE   778 AA;  86340 MW;  2AB1546A4CCF2F2B CRC64;
     MAAAGLVAVV AAAEYSGPVA SGGNLSGATC GPSPGLGPGP GPGSWSRSVD RALEEAAVTG
     VLSLSGRKLR EFPRGAANHD LTDTTRADLS RNRLSEIPME ACHFVSLESL NLYQNCIRYI
     PEAVLNLQAL TFLNISRNQL STLPVHLCNL PLKVLIASNN KLVSLPEEIG HLRHLTKLDV
     SCNEIQTVPS QIGNLEALRD FNVRRNHLLR LPEELAEVPL IRLDFSCNKI TVIPVCYRNL
     RHLQVITLDN NPLQSPPAQI CIKGKIHIFK YLNIQACKIA PDLPDYERRP LGFGSCHEEL
     YSGRPYGALD SGFNSVDSGD KRWSGNEPTD EFSDLPLRVA EITKEQRLRR ESQYQENRSS
     VAVTNGGVEH DLDQIDYIDS CTTEEEENDV KQPKSLDTNS LSSQFMAYIE QRRISHEVSP
     VKPIAVREFQ KTEDMKRYSH QNRVPVEPSL VLSMPPSHNQ LSHSDLELHQ RREQSIECTR
     REAQLAALQY EEEKIRTKQI QRDAVLDFVK QKASHNPQRQ QPPGNGECSF PSRRSQHTDD
     SALLVSLSGL DGVSCVATRP HSSAFTPLKS ENRVDVTSSF PMTETVHHSP AYSFPAATQR
     NQPQRPESFL FRAAVRAEAN KGRASPLLLS SAPATDPTDA ITRQREEELK LIDQLRKHIE
     YRLKVSLPCD LGAALTDGVV LCHLANHVRP RSVPSIHVPS PAVPKLTMAK CRRNVENFLD
     ACRKIGVPQE QLCLPLHILE EKGLGQVAVT VQALLELAPP KQPPPQQPQQ QQPQLSAV
//
ID   ARG33_MOUSE             Reviewed;         850 AA.
AC   Q8BW86;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 3.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Rho guanine nucleotide exchange factor 33;
GN   Name=Arhgef33; Synonyms=Gm941;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-460 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Oviduct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BW86-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BW86-2; Sequence=VSP_039455;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC132910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC161447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK053944; BAC35600.2; -; mRNA.
DR   IPI; IPI00378268; -.
DR   IPI; IPI00968923; -.
DR   RefSeq; NP_001138924.1; NM_001145452.1.
DR   UniGene; Mm.360004; -.
DR   UniGene; Mm.434583; -.
DR   ProteinModelPortal; Q8BW86; -.
DR   PhosphoSite; Q8BW86; -.
DR   PRIDE; Q8BW86; -.
DR   Ensembl; ENSMUST00000068175; ENSMUSP00000063284; ENSMUSG00000054901.
DR   GeneID; 381112; -.
DR   KEGG; mmu:381112; -.
DR   UCSC; uc008drf.1; mouse.
DR   CTD; 381112; -.
DR   MGI; MGI:2685787; Arhgef33.
DR   eggNOG; maNOG11898; -.
DR   GeneTree; ENSGT00390000006230; -.
DR   HOGENOM; HBG280883; -.
DR   HOVERGEN; HBG098090; -.
DR   InParanoid; Q8BW86; -.
DR   OrthoDB; EOG4J3WGC; -.
DR   ArrayExpress; Q8BW86; -.
DR   Bgee; Q8BW86; -.
DR   Genevestigator; Q8BW86; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000219; DH-domain.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   PROSITE; PS00741; DH_1; FALSE_NEG.
DR   PROSITE; PS50010; DH_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil;
KW   Guanine-nucleotide releasing factor.
FT   CHAIN         1    850       Rho guanine nucleotide exchange factor
FT                                33.
FT                                /FTId=PRO_0000342344.
FT   DOMAIN      273    448       DH.
FT   COILED       54    128       Potential.
FT   COMPBIAS    511    515       Poly-Ser.
FT   COMPBIAS    530    533       Poly-Gln.
FT   COMPBIAS    759    764       Poly-Ala.
FT   VAR_SEQ       1     86       Missing (in isoform 2).
FT                                /FTId=VSP_039455.
FT   CONFLICT    165    165       F -> L (in Ref. 2; BAC35600).
SQ   SEQUENCE   850 AA;  94758 MW;  B18975B3390B2C0B CRC64;
     MEKSKAKQGE NEHMPVNNPS TQIYQLQALA SELKTGFTEA MQELTRIQHG EYALEEKVKS
     CRCSMEEKVT EMKNSLNYFK EELSNAMSMI QAITSKQEEM QQKIEQLQQE KRRESRKVKA
     KKAQKEEHGA QAGPASAPAP GSAPTQGSPF RSINVPEAGL PSDDFTNMLP SQNYEKAQES
     RSVHVGDSNV KGMMGPGVNP TTPESDENLK PSLSAEIQSK GHHTPGLWRQ PKEGKEWGEE
     YVTKDHPDKL KDAGQGRHSS LENVLCETSL AAKRQTVALE LLESERKYVI NISLILKIKA
     TFQGSDGKRN PKERSLFPGS LRYLVQQHLD LLHALQERVL KWPRQGVLGD LFLKLTNDEN
     NFLDYYVAYL RDLPECISLV HVVVLKEGDE EIKSDIYTLF FHIVQRIPEY LIHLQNVLKF
     TEQEHPDYYL LLVCVQRLRV FISHYTLLFQ CNEDLLIQKR KKLKKSSMAK LYKGLASQCA
     NAGQDASPNA GQEAVHDSGV HSEEMLQPYP SSSSSAPAVS HLMAPAKKGQ QQQSLMESMQ
     PGKPGDWELE GRKHERPESL LAPAQFCAAE QDVKALAGPL QAIPEMDFEP SSAEPLGNVE
     RSLRGPPELL PDARGFVPAG YEEFEYGGEI FALPAPYDEE PFQAPALFDN CSPASSESSL
     DICFLRPVSF AMEAERPEHA LQPLPKSATS PASSSGAYKL EAAQAQAHGK AKPLSRSLKE
     FPRTPPAEGV APRLYSTRSS SGGRAPLKVE RAPAPHGPAA AAAASRGAPR TFFPQQRSQS
     EKQTYLEEMH LEDATRFCPK EERESEQTSF SDQNPRQDQK GGFRSSFRKL FKKKNGNSTG
     EDFCGPWGWW
//
ID   DYH3_MOUSE              Reviewed;        4083 AA.
AC   Q8BW94; O08829; Q7TT83;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=Dynein heavy chain 3, axonemal;
DE   AltName: Full=Axonemal beta dynein heavy chain 3;
DE   AltName: Full=Ciliary dynein heavy chain 3;
GN   Name=Dnah3; Synonyms=Dnahc3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1381-1584 (ISOFORM 1).
RC   STRAIN=NMRI; TISSUE=Testis;
RX   MEDLINE=98038992; PubMed=9373155; DOI=10.1016/S0378-1119(97)00417-4;
RA   Neesen J., Koehler M.R., Kirschner R., Steinlein C., Kreutzberger J.,
RA   Engel W., Schmid M.;
RT   "Identification of dynein heavy chain genes expressed in human and
RT   mouse testis: chromosomal localization of an axonemal dynein gene.";
RL   Gene 200:193-202(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2388-4083 (ISOFORM 3).
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2980-4083 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3581 AND SER-3584, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
CC   -!- FUNCTION: Force generating protein of respiratory cilia. Produces
CC       force towards the minus ends of microtubules. Dynein has ATPase
CC       activity; the force-producing power stroke is thought to occur on
CC       release of ADP. Involved in sperm motility; implicated in sperm
CC       flagellar assembly (By similarity).
CC   -!- SUBUNIT: Consists of at least two heavy chains and a number of
CC       intermediate and light chains.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BW94-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BW94-2; Sequence=VSP_031929, VSP_031930;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8BW94-3; Sequence=VSP_031926, VSP_031927, VSP_031928;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: Dynein heavy chains probably consist of an N-terminal stem
CC       (which binds cargo and interacts with other dynein components),
CC       and the head or motor domain. The motor contains six tandemly-
CC       linked AAA domains in the head, which form a ring. A stalk-like
CC       structure (formed by two of the coiled coil domains) protrudes
CC       between AAA 4 and AAA 5 and terminates in a microtubule-binding
CC       site. A seventh domain may also contribute to this ring; it is not
CC       clear whether the N-terminus or the C-terminus forms this extra
CC       domain. There are four well-conserved and two non-conserved ATPase
CC       sites, one per AAA domain. Probably only one of these (within AAA
CC       1) actually hydrolyzes ATP, the others may serve a regulatory
CC       function (By similarity).
CC   -!- SIMILARITY: Belongs to the dynein heavy chain family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC35298.1; Type=Erroneous initiation;
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DR   EMBL; AC122853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC131702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z83816; CAB06070.1; -; mRNA.
DR   EMBL; BC051401; AAH51401.1; -; mRNA.
DR   EMBL; AK053178; BAC35298.1; ALT_INIT; mRNA.
DR   IPI; IPI00406571; -.
DR   IPI; IPI00880351; -.
DR   IPI; IPI00885678; -.
DR   UniGene; Mm.291751; -.
DR   ProteinModelPortal; Q8BW94; -.
DR   SMR; Q8BW94; 1393-1459, 1670-1695, 2025-2059, 2674-2896.
DR   STRING; Q8BW94; -.
DR   PhosphoSite; Q8BW94; -.
DR   Ensembl; ENSMUST00000046993; ENSMUSP00000042857; ENSMUSG00000052273.
DR   UCSC; uc009jme.1; mouse.
DR   MGI; MGI:2683040; Dnahc3.
DR   eggNOG; roNOG09557; -.
DR   GeneTree; ENSGT00560000076867; -.
DR   HOGENOM; HBG357826; -.
DR   HOVERGEN; HBG107830; -.
DR   InParanoid; Q8BW94; -.
DR   OrthoDB; EOG4GTKFS; -.
DR   ArrayExpress; Q8BW94; -.
DR   CleanEx; MM_DNAHC3; -.
DR   Genevestigator; Q8BW94; -.
DR   GO; GO:0035085; C:cilium axoneme; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR011704; ATPase_AAA-5.
DR   InterPro; IPR004273; Dynein_heavy.
DR   InterPro; IPR013602; Dynein_heavy_N-2.
DR   Pfam; PF07728; AAA_5; 1.
DR   Pfam; PF08393; DHC_N2; 1.
DR   Pfam; PF03028; Dynein_heavy; 1.
DR   SMART; SM00382; AAA; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell projection; Cilium;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Dynein; Microtubule;
KW   Motor protein; Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1   4083       Dynein heavy chain 3, axonemal.
FT                                /FTId=PRO_0000322545.
FT   NP_BIND    1396   1403       ATP (Potential).
FT   NP_BIND    1677   1684       ATP (Potential).
FT   NP_BIND    2041   2048       ATP (Potential).
FT   NP_BIND    2401   2408       ATP (Potential).
FT   REGION        1   1357       Stem (By similarity).
FT   REGION     1358   1579       AAA 1 (By similarity).
FT   REGION     1639   1870       AAA 2 (By similarity).
FT   REGION     2003   2251       AAA 3 (By similarity).
FT   REGION     2362   2613       AAA 4 (By similarity).
FT   REGION     2628   2927       Stalk (By similarity).
FT   REGION     3012   3242       AAA 5 (By similarity).
FT   REGION     3455   3679       AAA 6 (By similarity).
FT   COILED     1026   1052       Potential.
FT   COILED     1108   1133       Potential.
FT   COILED     2651   2714       Potential.
FT   MOD_RES    3581   3581       Phosphoserine.
FT   MOD_RES    3584   3584       Phosphoserine.
FT   VAR_SEQ    2523   2530       GTNRAYFS -> VRKNLHIV (in isoform 3).
FT                                /FTId=VSP_031926.
FT   VAR_SEQ    2720   2737       KNECEGDLAEAMPALEAA -> KVCDQARGAQGANTAKRM
FT                                (in isoform 3).
FT                                /FTId=VSP_031927.
FT   VAR_SEQ    2738   4083       Missing (in isoform 3).
FT                                /FTId=VSP_031928.
FT   VAR_SEQ    3921   3957       EWIDKGPPVVFWISGFYFTQSFLTGVSQNYARKYTIP ->
FT                                VPGNLGNWIPGSSLRWRRHCGVAEQKLGTRVGSCVAS (in
FT                                isoform 2).
FT                                /FTId=VSP_031929.
FT   VAR_SEQ    3958   4083       Missing (in isoform 2).
FT                                /FTId=VSP_031930.
FT   CONFLICT   1506   1509       AELP -> SDLQ (in Ref. 2; CAB06070).
FT   CONFLICT   1514   1514       A -> P (in Ref. 2; CAB06070).
FT   CONFLICT   1520   1520       A -> P (in Ref. 2; CAB06070).
FT   CONFLICT   1570   1571       MR -> IS (in Ref. 2; CAB06070).
FT   CONFLICT   3182   3182       P -> T (in Ref. 4; BAC35298).
SQ   SEQUENCE   4083 AA;  467777 MW;  4E72F4B2EFF4A3CB CRC64;
     MSDTNCSAQK LDKSDSVHHM SHSQARPELP PLPVSANEEP SELYKTVMSH SFYPPLMQRT
     SWTLAVPFKE QDHHRGPSDS IGNNYSLTAR DMKLKDLLKV YQPVTISIPR DKTSQGLPLG
     TSSKTSTEPS KKKMKFNLKA KDDVTGMPFV CKFSSSLSIK NTTDSSVTHP ESRPMSPEQQ
     MDVMLQQEME IESKEQKPSE LDLERYYYYL TNGIRKDMIA PENEEVMMRI YKLIPKTLLT
     TPALEPLQVS LRSEKESDYY YSLMKSIVDY ILMDPMEKKR LFIKSIPRLF PHRVIRAPVP
     WHNIYQSTKK WNEEHLHTVN PMMYKLKELW FAEFQNLRFV RTADLLAGKL PLLPHEYKEV
     VQKHCREARH ILLTKWIPTC AQLFVTQKEH WVHFAPKNDY DSSRNIEEYF ASVASFMSLQ
     LRDLVIKSLR DLVSFFMIHK DGNDFKEPYQ EMDFFIPQLI MIKLEVRDPI IVFNPTFDDC
     WQLIKNSFLE IIKNSDGIPK VYLCWKPLAS YICVSPHLRM TSVLQVESIL FPDLKGYNMI
     LGTVNPEESL VSDFLDQTLE VFKKNQVGPY KYLNVYKKYD DLLDNMAEKG ISEFLKEKHE
     IEDFVTSINS IKKRKNEIAS MHITVPLAMF CLDAVFLNYD LCERAQNLKD NLILYQVDVN
     RETNTSICNQ YSTIADKVSE IPANTAELVA LIEYLKKSSD VTVFKLRRQL RDASERLEFL
     MDYADLPSES IEDVFESSRN LLMSKRDQAE MDLIKRCSEF ESRLEGYSKE LEMFRKREVM
     TTEEMKNNVE KLHDLSKNLD LALTEFELIN KEEELLEKEK SSFPLLQTLM INKIPYEQLW
     VTAYEFSTKS EEWMNGPLYL MNAEQIAEEI GNMWRTTYKL TKTLIDVPAP KRLAENVKLK
     IEKFKQHIPI LNIACNPGMK DRHWQQISDI VGYEIKPTET TCLANMLEYG FGKFVDKLEP
     IGAAASKEYS LEKNLEKMKA DWVNMCFSFV KYRDTDTSIL CAVDDIQLIL DDHVIKTQTM
     CGSVFIKPIE AECRKWEEKL VRVQENLDAW LKCQVTWLYL EPIFSSEDII AQMPEEGKKF
     TTVDTYWKSL MAQAVNDTRV MVAADQPRMT EKLQEANVLL EDIQRGLNDY LEKKRLFFPR
     FFFLSNDELL EILSETKDPL RVQPHLKKCF EGIAKLEFTD NLEIKGMISS EKETVPFIQT
     IYPVKAKGMV EKWLQQVEQV MLASMRQVIE NGIEAYVQVP RNAWVLEWPG QVVICVSSIF
     WTREVSEALV EDTLTDFLKK SNDQIAQIVE LVRGKLSSGA RLTLGALTVI DVHARDVVAK
     LRHDHINSLN DFQWISQLRY YWTEKNVHVQ MITTEALYGY EYLGNSPRLV ITPLTDRCYR
     TLMGALKLNL GGAPEGPAGT GKTETTKDLA KALAKQCVVF NCSDGLDYKA MGKFFKGLAQ
     AGAWACFDEF NRIEVEVLSV VAQQILSIQQ AIIRKLKRFI FEGTELSLNP TCAVFITMNP
     GYAGRAELPD NLKALFRTVA MMVPDYALIG EISLYSMGFL DSRSLAQKIV ATYRLCSEQL
     SSQHHYDYGM RAVKSVLTAA GNLKLKYPEE NESVLLLRAL LDVNLAKFLA QDVPLFQGII
     SDLFPGVVLP KPDYEVFLEA LNNNIRKMKL QPVPWFIGKI IQIYEMMLVR HGYMIVGDPM
     GGKTSAYKVL AAALGDLHAA NQMEEFAVEF KIINPKAITM GQLYGCFDAV SHEWTDGVLA
     NAFREQASSI TDDRKWIIFD GPVDAVWIEN MNTVLDDNKK LCLMSGEIIQ MSSKMSLIFE
     PADLEQASPA TVSRCGMIYM EAHQLGWKPL KDSYMDTLPR CLTKEHTELV EDMFTWLVQP
     CLDFSRLHCK FVVQTSPIHL AFSMMRLYSS LLDEIRDIQE EEMEIYEGLS SQQIFLWLQG
     LFLFSLVWTL AGTINAESRK KFDVFFRNLI MGMDDRNPRP KSVKLTKNNI FPERGSIYDF
     YFLKQGGGHW NAWTEYITKE EETIPANAKV SDLIIPTMET ARQSFFLKTY LDHEIPILFV
     GPTGTGKSAI TNDFLLHLPK NVYQPNFINF SARTSANQTQ DIIMSKLDRR RKGLFGPPIG
     KKAVVFVDDL NMPAKEVYGA QPPIELLRQW IDHGYWFDKK DTNRLDIVDV LLVTAMGPPG
     GGRNDITGRF TRHLNIISIN AFEDEILTKI FSSIADWHFG KGFDVMFLRY GKMLVQATQT
     IYRAAVENFL PTPSKSHYVF NLRDFSRVIQ GVLLCPHTHL QDLEKFIRLW IHEVYRVFYD
     RLIDNDDRQT FFNLVKETTS NCFKQTMEKV LIHLSPTGKI TDDNIRSLFF GDYLKPESDQ
     KIYDEIIDLR GLTVVMEYYL DEFNSVSKAP MSLVMFKFAI EHISRICRVL KQKKGHLLLV
     GIGGSGRQSA TKLSTFMNSY ELYQIEITKN YTNSDWREDL KKIMLQSGVA TKSTVFLFSD
     NQIKHESFVE DINMLLNTGD VPNIFPADEK ADLVEKMQTA ARTEGEKVEA TPLSMYNFFI
     ERGTNRAYFS LAMSPIGDAF RTRLRMFPSL INCCTIDWFQ SWPTDALELV ANKFLEDVEL
     DDNIRAEVVS MCKYFQESVK KLSVDYYNTL LRHNYVTPTS YLELILTFKT LLNSKRQEVD
     TIRNRYLAGL QKLEFASSQV AVMQVELTAL QPQLIQTSED TAMMMVKIEL ETKEADAKKL
     LVQADEKEAN AAAAISQAIK NECEGDLAEA MPALEAALAA LDTLNPSDIT LVKSMQNPPG
     PVKLVMESIC VMKGLKPERK PDPSGSGKMI EDYWGVSRKI LGDLKFLESL KTYDKDNIPS
     VIMKRIRERF IDHPDFQPAV IKNVSSACEG LCKWVRAMEV YDRVAKVVAP KRERLREAEG
     KLEIQMQKLN QKRAELKLVE DRLQDLNDEF ELMNRKKNSL EKNIEICSQK LVRAEKLISG
     LGGEKDRWTE AARQLGIRYD NLTGDVLLAS GTVAYLGAFT VDYRAQCQNE WLVSCKDKVI
     PGSVDFSLSN TLGDPIKIRA WQIAGLPVDS FSVDNGIIVS NSRRWPLMID PQGQANKWVK
     NMEKTNKLSV IKFSDTNYVR TLENALQFGT PVLLENVGEE LDAFIEPILL KATFKQQGVE
     YMRLGENIIE YSREFKFYIT TRLRNPHYLP EVAVKVCLLN FMITPLGLQD QLLGIVAAKE
     KPELEEKKNK LILESAQNKK QLKEIEDKIL EVLSLCEGNI LEDETAIKIL SSSKVLSEEI
     SEKQEIASVT ETQIDETRMG YKPVAVHSAA IFFCISDLAH IEPMYQYSLT WFINLYVQSL
     ANSNKSDELD LRIEYIIEHF TLSIYNNVCR SLFEKDKLLF SLLLTVGLLK ERKAIDEEVW
     YFLLTGGVAL DNPFPNPAPE WLSEKSWGEI VRASSLQKLK GLMEDVMQNI KVWKDIYDSA
     WPHEESLPSP WFFLQTLEKI AILRCLRPDK IVPAIQNFIC ETMGKIFIEA PTFDLQGSYG
     DSSCCVPLIF ILSPGADPMA GLLKFADDVS MGGTKTQTIS LGQGQGPIAA NMINKAIHEG
     TWVVLQNCHL ATSWMPALEK ICEEVIVPEN TNSEFRLWLT SYPSEKFPVS ILQNGIKMTN
     EPPKGLRANL LRSYLNDPIS DPLFFQSCTK PVIWQKLLFG LCFFHAIVQE RRNYGALGWN
     IPYEFNESDL RISMRQIQMF LNDYEEVPFE ALTYLTGECN YGGRVTDDKD RRLLLSLLSM
     FYCKEIETDN YHIAPGDAYV IPPYGSYQSY IEYLRTLPIT AHPEVFGLHE NADITKDNQE
     TNQLFQGVLL TLPRQSGGSG KSPQEVVEEL AQDILSKLPN DFNLEEVMKK YPVVYKESMN
     TVLRQELIRF NRLTKVVRRS LIDLGRAIKG QVLMSSELEE VFNSMLVGKV PAMWAAKSYP
     SLKPLGGYVA DLLARLTFFQ EWIDKGPPVV FWISGFYFTQ SFLTGVSQNY ARKYTIPIDH
     IGFEFEVTPK ETTMENIPED GAYIKGLFLE GARWDRSTSQ IGESLPKILY DPLPIIWLKP
     GESASFLHQD IYVCPVYKTS ARRGILSTTG HSTNYVLSIE LPTDMPQKHW INRGVASLCQ
     LDN
//
ID   KCC1D_MOUSE             Reviewed;         385 AA.
AC   Q8BW96; Q3U450; Q80W64; Q8BWI7;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Calcium/calmodulin-dependent protein kinase type 1D;
DE            EC=2.7.11.17;
DE   AltName: Full=CaM kinase I delta;
DE            Short=CaM-KI delta;
DE            Short=CaMKI delta;
DE   AltName: Full=CaM kinase ID;
DE   AltName: Full=CaMKI-like protein kinase;
DE            Short=CKLiK;
DE            Short=mCKLiK;
GN   Name=Camk1d;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=14980499; DOI=10.1016/j.yexcr.2003.10.023;
RA   Yamada T., Suzuki M., Satoh H., Kihara-Negishi F., Nakano H.,
RA   Oikawa T.;
RT   "Effects of PU.1-induced mouse calcium-calmodulin-dependent kinase I-
RT   like kinase (CKLiK) on apoptosis of murine erythroleukemia cells.";
RL   Exp. Cell Res. 294:39-50(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND INDUCTION.
RC   STRAIN=C57BL/6; TISSUE=Liver;
RX   MEDLINE=22996184; PubMed=12897189; DOI=10.1194/jlr.M300203-JLR200;
RA   Maxwell K.N., Soccio R.E., Duncan E.M., Sehayek E., Breslow J.L.;
RT   "Novel putative SREBP and LXR target genes identified by microarray
RT   analysis in liver of cholesterol-fed mice.";
RL   J. Lipid Res. 44:2109-2119(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Brain, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Calcium/calmodulin-dependent protein kinase belonging to
CC       a proposed calcium-triggered signaling cascade. May regulate
CC       calcium-mediated granulocyte function. May play a role in
CC       apoptosis of erythroleukemia cells. Activates MAP kinase MAPK3 (By
CC       similarity). In vitro, phosphorylates transcription factor CREM
CC       isoform Beta and probably CREB1 (By similarity). Isoform 1 but not
CC       isoform 2 activates CREB1.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Activated by Ca(2+)/calmodulin. Binding of
CC       calmodulin is thought to result in a conformational change and can
CC       lead to subsequent activation through phosphorylation by CAMKK1
CC       and CAMKK2. At least in part, also activated by CAMKK1 in a
CC       calcium-independent manner (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Predominantly cytoplasmic (By similarity).
CC       Nuclear upon activation (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Alpha;
CC         IsoId=Q8BW96-1; Sequence=Displayed;
CC       Name=2; Synonyms=Beta;
CC         IsoId=Q8BW96-2; Sequence=VSP_012137;
CC         Note=Inactive. Does not activate CREB1;
CC       Name=3;
CC         IsoId=Q8BW96-3; Sequence=VSP_012136;
CC   -!- TISSUE SPECIFICITY: Expressed ubiquitously with high levels in
CC       brain and low levels in kidney. Isoform 2 is highly expressed in
CC       brain compared to other tissues. In hematopoietic cell lines
CC       predominant expression was detected in T and EC cells.
CC   -!- INDUCTION: Down-regulated upon cholesterol-rich diet.
CC   -!- DOMAIN: The autoinhibitory domain overlaps with the calmodulin
CC       binding region and interacts in the inactive folded state with the
CC       catalytic domain as a pseudosubstrate (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. CaMK subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY273822; AAP31673.1; -; mRNA.
DR   EMBL; AK052401; BAC34975.1; -; mRNA.
DR   EMBL; AK053173; BAC35295.1; -; mRNA.
DR   EMBL; AK147616; BAE28027.1; -; mRNA.
DR   EMBL; AK154434; BAE32584.1; -; mRNA.
DR   EMBL; AK170777; BAE42022.1; -; mRNA.
DR   IPI; IPI00226188; -.
DR   IPI; IPI00403595; -.
DR   IPI; IPI00480395; -.
DR   RefSeq; NP_796317.2; NM_177343.3.
DR   UniGene; Mm.191949; -.
DR   ProteinModelPortal; Q8BW96; -.
DR   SMR; Q8BW96; 11-313.
DR   STRING; Q8BW96; -.
DR   PhosphoSite; Q8BW96; -.
DR   PRIDE; Q8BW96; -.
DR   Ensembl; ENSMUST00000044009; ENSMUSP00000037028; ENSMUSG00000039145.
DR   Ensembl; ENSMUST00000114987; ENSMUSP00000110638; ENSMUSG00000039145.
DR   GeneID; 227541; -.
DR   KEGG; mmu:227541; -.
DR   NMPDR; fig|10090.3.peg.5372; -.
DR   UCSC; uc008ifp.1; mouse.
DR   UCSC; uc008ifr.1; mouse.
DR   CTD; 227541; -.
DR   MGI; MGI:2442190; Camk1d.
DR   GeneTree; ENSGT00600000084207; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108055; -.
DR   InParanoid; Q8BW96; -.
DR   OMA; CSFMSSS; -.
DR   PhylomeDB; Q8BW96; -.
DR   BRENDA; 2.7.11.17; 244.
DR   NextBio; 378629; -.
DR   ArrayExpress; Q8BW96; -.
DR   Bgee; Q8BW96; -.
DR   CleanEx; MM_CAMK1D; -.
DR   Genevestigator; Q8BW96; -.
DR   GermOnline; ENSMUSG00000039145; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:EC.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0042981; P:regulation of apoptosis; IDA:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   Allosteric enzyme; Alternative splicing; ATP-binding; Calcium;
KW   Calmodulin-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    385       Calcium/calmodulin-dependent protein
FT                                kinase type 1D.
FT                                /FTId=PRO_0000086083.
FT   DOMAIN       23    279       Protein kinase.
FT   NP_BIND      29     37       ATP (By similarity).
FT   REGION      279    319       Autoinhibitory domain (By similarity).
FT   REGION      299    320       Calmodulin-binding (By similarity).
FT   MOTIF       318    324       Nuclear export signal (By similarity).
FT   ACT_SITE    144    144       Proton acceptor (By similarity).
FT   BINDING      52     52       ATP (By similarity).
FT   MOD_RES     122    122       Phosphoserine (By similarity).
FT   MOD_RES     180    180       Phosphothreonine; by CaMKK1, CaMKK2 and
FT                                autocatalysis (By similarity).
FT   VAR_SEQ       1     31       MARENGESSSSWKKQAEDIKKIFEFKETLGT -> MAEFVS
FT                                WSCLNFRWSWIKGSRNS (in isoform 3).
FT                                /FTId=VSP_012136.
FT   VAR_SEQ     333    385       ASVSSNLSLASQKDCLAPSTLCSFLSSSSGVAGVGAERRPR
FT                                PTTVTTGHTGSK -> VWHLPRSVVSFLLRRGSQESELRGD
FT                                PQPPL (in isoform 2).
FT                                /FTId=VSP_012137.
FT   CONFLICT     30     30       G -> Q (in Ref. 3; BAC35295).
FT   CONFLICT    327    327       S -> N (in Ref. 3; BAC35295).
SQ   SEQUENCE   385 AA;  42919 MW;  320EB0D3D5670055 CRC64;
     MARENGESSS SWKKQAEDIK KIFEFKETLG TGAFSEVVLA EEKATGKLFA VKCIPKKALK
     GKESSIENEI AVLRKIKHEN IVALEDIYES PNHLYLVMQL VSGGELFDRI VEKGFYTEKD
     ASTLIRQVLD AVYYLHRMGI VHRDLKPENL LYYSQDEESK IMISDFGLSK MEGKGDVMST
     ACGTPGYVAP EVLAQKPYSK AVDCWSIGVI AYILLCGYPP FYDENDSKLF EQILKAEYEF
     DSPYWDDISD SAKDFIRNLM EKDPNKRYTC EQAARHPWIA GDTALSKNIH ESVSAQIRKN
     FAKSKWRQAF NATAVVRHMR RLQLGSSLDS SNASVSSNLS LASQKDCLAP STLCSFLSSS
     SGVAGVGAER RPRPTTVTTG HTGSK
//
ID   Q8BWA4_MOUSE            Unreviewed;       334 AA.
AC   Q8BWA4;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Tcfap4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 basic helix-loop-helix (bHLH) domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK053091; BAC35263.1; -; mRNA.
DR   IPI; IPI00121217; -.
DR   UniGene; Mm.273210; -.
DR   HSSP; P22415; 1AN4.
DR   ProteinModelPortal; Q8BWA4; -.
DR   SMR; Q8BWA4; 41-117.
DR   STRING; Q8BWA4; -.
DR   Ensembl; ENSMUST00000005862; ENSMUSP00000005862; ENSMUSG00000005718.
DR   UCSC; uc007xzv.1; mouse.
DR   MGI; MGI:103239; Tcfap4.
DR   eggNOG; roNOG16556; -.
DR   HOVERGEN; HBG061473; -.
DR   InParanoid; Q8BWA4; -.
DR   OrthoDB; EOG4ZCT55; -.
DR   PhylomeDB; Q8BWA4; -.
DR   ArrayExpress; Q8BWA4; -.
DR   Bgee; Q8BWA4; -.
DR   Genevestigator; Q8BWA4; -.
DR   InterPro; IPR011598; HLH_DNA-bd.
DR   InterPro; IPR001092; HLH_DNA-bd_dom.
DR   Gene3D; G3DSA:4.10.280.10; HLH_DNA_bd; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; HLH_basic; 1.
DR   PROSITE; PS50888; HLH; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   334 AA;  38156 MW;  57872B0F6A586061 CRC64;
     MVPTQKVPSL QHFRKTEKEV IGGLCSLANI PLTPETQRDQ ERRIRREIAN SNERRRMQSI
     NAGFQSLKTL IPHTDGEKLS KAAILQQTAE YIFSLEQEKT RLLQQNTQLK RFIQELSGSS
     PKRRRAEDKD EGIGSPDIWE DEKAEDLRRE MIELRQQLDK ERSVRMMLEE QVRSLEAHMY
     PEKLKVIAQQ VQLQQQQEQV RLLHQEKLER EQQHLRTQLL PPPAPTHHPT VIVPAPAPPS
     SHHINVVTMG PSSVINSVST SRQNLDTIVQ AIQHIEGTQD KQELEEEQRR AVIVKSVRSC
     PDAHTSDTAS DSEASDSDAM DQSREEPLGD GELP
//
ID   SYP2L_MOUSE             Reviewed;         975 AA.
AC   Q8BWB1;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Synaptopodin 2-like protein;
GN   Name=Synpo2l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Actin-associated protein that may play a role in
CC       modulating actin-based shape (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC   -!- SIMILARITY: Belongs to the synaptopodin family.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK053054; BAC35251.1; -; mRNA.
DR   IPI; IPI00226219; -.
DR   RefSeq; NP_780341.1; NM_175132.3.
DR   UniGene; Mm.35789; -.
DR   ProteinModelPortal; Q8BWB1; -.
DR   SMR; Q8BWB1; 3-85.
DR   PhosphoSite; Q8BWB1; -.
DR   PRIDE; Q8BWB1; -.
DR   Ensembl; ENSMUST00000057090; ENSMUSP00000053176; ENSMUSG00000039376.
DR   GeneID; 68760; -.
DR   KEGG; mmu:68760; -.
DR   UCSC; uc007skf.1; mouse.
DR   CTD; 68760; -.
DR   MGI; MGI:1916010; Synpo2l.
DR   eggNOG; maNOG15091; -.
DR   GeneTree; ENSGT00530000063754; -.
DR   HOVERGEN; HBG060706; -.
DR   OMA; EGPVRSP; -.
DR   OrthoDB; EOG479F6S; -.
DR   PhylomeDB; Q8BWB1; -.
DR   NextBio; 327862; -.
DR   ArrayExpress; Q8BWB1; -.
DR   Bgee; Q8BWB1; -.
DR   CleanEx; MM_SYNPO2L; -.
DR   Genevestigator; Q8BWB1; -.
DR   GermOnline; ENSMUSG00000039376; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Cytoplasm; Cytoskeleton.
FT   CHAIN         1    975       Synaptopodin 2-like protein.
FT                                /FTId=PRO_0000187676.
FT   DOMAIN        6     85       PDZ.
FT   COMPBIAS     93    238       Pro-rich.
FT   COMPBIAS    419    821       Pro-rich.
SQ   SEQUENCE   975 AA;  102953 MW;  9B65C37D10895228 CRC64;
     MGAEEEVQVT LAGGAPWGFR LQGGTEQRKP LQIRRRSQAG RAGLRERDQL LAINGVSCTN
     FSHASAMTLI DASGRQLVLT VRRVTDEGSV RSPSPGELQV LSPLSPLSPE PPGAPVSQAL
     QPTSLRSPPD SEAYYGETDS DVDGPATQEK PRRTRRRGPA RPSLPGAPPD EVYLSDSPAE
     PAPVKTGSPS QGDSRVSSPS WEEGAALQPP PAEALLLPHG PLRPGPHLIP MVGPVPHPVA
     EDLTTTYTQK AKQAKLQRAE SLQEKSVKEA RTKCRTIASL LTAAPNPHSK GVLMFKKRRQ
     RAKKYTLVSF GAAAGTGTEE EDGIPPTSES ELDEETFSDA RSLTNQSDWD SPYLDMELAR
     AGLGTAESQN SGLGGQLSEV SGRGVQLFEQ QRQRVASSSQ ELAQVGPAAM LNGQSLQSPP
     RAQSAPPEAA VLPLSPLSVP AVSPTPFFPD GGAPIPAPSI FNRSARPFTP GLQGQRSGTT
     SVIFRPLAPK KVNEGLGSTS PAPSPFAAPP QGPTPLPSFT TVVPSHTPVS GASSSTQRSS
     GPVTATSSLY IPAPSRPVTP GGAPEPPTPP SAAAMTSTAS IFLSTPLRNS ARPEAPGPAV
     PEPASVREQR ISVPAARTGI LQEARRRGTR KQMFRPGKEE TKNSPNPELL SLVQNLDEKP
     RAGGAESGPE EDALSLGAEA CNFMQPLGGR SYKTLPQVSP KTPPPMAPKT PPPTTPKTPP
     PVAPKPGSRG LLDGLVNGST PMVGIPEPPR LQGRGGELFA KRQSRADRYV VEATSGSSLN
     PGLRPRSPSP TPSLPPSWKY SPNIRAPPPI AYNPLLSPFF PQAARTLPNK AQSQGPRVTP
     KQGIKALDFM RHQPYQLKTA MFCFDEGSST PGPTSGPPKT ARVQEIRRFS TPAPQPTAEP
     LAPTVLVPRA ATTLDEPIWR AELASTPVPN PDHQESLRSF AAAPSSCGFQ VARPRFSATR
     TGLQAHVWRP GAGHQ
//
ID   STEA2_MOUSE             Reviewed;         489 AA.
AC   Q8BWB6; Q3TS12;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Metalloreductase STEAP2;
DE            EC=1.16.1.-;
DE   AltName: Full=Six-transmembrane epithelial antigen of prostate 2;
GN   Name=Steap2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Epididymis, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   FUNCTION, ENZYME ACTIVITY, AND SUBCELLULAR LOCATION.
RX   PubMed=16609065; DOI=10.1182/blood-2006-02-003681;
RA   Ohgami R.S., Campagna D.R., McDonald A., Fleming M.D.;
RT   "The Steap proteins are metalloreductases.";
RL   Blood 108:1388-1394(2006).
CC   -!- FUNCTION: Metalloreductase that has the ability to reduce both
CC       Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+). Uses NAD(+) as acceptor.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity). Endosome membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the STEAP family.
CC   -!- SIMILARITY: Contains 1 ferric oxidoreductase domain.
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DR   EMBL; AK052981; BAC35230.1; -; mRNA.
DR   EMBL; AK162343; BAE36864.1; -; mRNA.
DR   IPI; IPI00226224; -.
DR   RefSeq; NP_001096626.1; NM_001103156.1.
DR   RefSeq; NP_001096627.1; NM_001103157.1.
DR   RefSeq; NP_083010.2; NM_028734.4.
DR   UniGene; Mm.274956; -.
DR   UniGene; Mm.477119; -.
DR   ProteinModelPortal; Q8BWB6; -.
DR   SMR; Q8BWB6; 30-207.
DR   STRING; Q8BWB6; -.
DR   PhosphoSite; Q8BWB6; -.
DR   PRIDE; Q8BWB6; -.
DR   Ensembl; ENSMUST00000015797; ENSMUSP00000015797; ENSMUSG00000015653.
DR   Ensembl; ENSMUST00000115424; ENSMUSP00000111084; ENSMUSG00000015653.
DR   Ensembl; ENSMUST00000115425; ENSMUSP00000111085; ENSMUSG00000015653.
DR   Ensembl; ENSMUST00000115426; ENSMUSP00000111086; ENSMUSG00000015653.
DR   GeneID; 74051; -.
DR   KEGG; mmu:74051; -.
DR   UCSC; uc008wiw.2; mouse.
DR   CTD; 74051; -.
DR   MGI; MGI:1921301; Steap2.
DR   eggNOG; roNOG04258; -.
DR   GeneTree; ENSGT00390000008042; -.
DR   HOGENOM; HBG447106; -.
DR   HOVERGEN; HBG054379; -.
DR   InParanoid; Q8BWB6; -.
DR   OMA; QVYICSN; -.
DR   OrthoDB; EOG4W9J3V; -.
DR   PhylomeDB; Q8BWB6; -.
DR   NextBio; 339632; -.
DR   ArrayExpress; Q8BWB6; -.
DR   Bgee; Q8BWB6; -.
DR   Genevestigator; Q8BWB6; -.
DR   GermOnline; ENSMUSG00000015653; Mus musculus.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030173; C:integral to Golgi membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0030140; C:trans-Golgi network transport vesicle; ISS:UniProtKB.
DR   GO; GO:0042598; C:vesicular fraction; ISS:UniProtKB.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005215; F:transporter activity; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR   GO; GO:0006893; P:Golgi to plasma membrane transport; ISS:UniProtKB.
DR   GO; GO:0006826; P:iron ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0045055; P:regulated secretory pathway; ISS:UniProtKB.
DR   GO; GO:0009725; P:response to hormone stimulus; ISS:UniProtKB.
DR   InterPro; IPR013130; Flavoprotein_TM.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR004455; NADP_OxRdtase_F420.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF03807; F420_oxidored; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Copper; Electron transport; Endosome; FAD;
KW   Flavoprotein; Ion transport; Iron; Iron transport; Membrane;
KW   Metal-binding; NAD; Oxidoreductase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    489       Metalloreductase STEAP2.
FT                                /FTId=PRO_0000191698.
FT   TRANSMEM    207    227       Helical; (Potential).
FT   TRANSMEM    258    278       Helical; (Potential).
FT   TRANSMEM    304    324       Helical; (Potential).
FT   TRANSMEM    358    378       Helical; (Potential).
FT   TRANSMEM    392    412       Helical; (Potential).
FT   TRANSMEM    431    451       Helical; (Potential).
FT   DOMAIN      258    406       Ferric oxidoreductase.
FT   METAL       315    315       Iron (heme axial ligand) (By similarity).
FT   METAL       408    408       Iron (heme axial ligand) (By similarity).
SQ   SEQUENCE   489 AA;  55760 MW;  98CD63D59DDDF24C CRC64;
     MESISMMGSP KSLETFLPNG INGIKDARQV TVGVIGSGDF AKSLTIRLIR CGYHVVIGSR
     NPKFASEFFP HVVDVTHHED ALTKTNIIFV AIHREHYTSL WDLRHLLVGK ILIDVSNNMR
     VNQYPESNAE YLASLFPDSL IVKGFNVISA WALQLGPKDA SRQVYICSNN IQARQQVIEL
     ARQLNFIPVD LGSLSSAKEI ENLPLRLFTL WRGPVVVAIS LATFFFLYSF VRDVIHPYAR
     NQQSDFYKIP IEIVNKTLPI VAITLLSLVY LAGLLAAAYQ LYYGTKYRRF PPWLDTWLQC
     RKQLGLLSFF FAVVHVAYSL CLPMRRSERY LFLNMAYQQV HANIENAWNE EEVWRIEMYI
     SFGIMSLGLL SLLAVTSIPS VSNALNWREF SFIQSTLGYV ALLITTFHVL IYGWKRAFAE
     EYYRFYTPPN FVLALVLPSI VILGKMILLL PCISRKLKRI KKGWEKSQFL DEGMGGAVPH
     LSPERVTVM
//
ID   SSDH_MOUSE              Reviewed;         523 AA.
AC   Q8BWF0; Q5SZW1;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Succinate-semialdehyde dehydrogenase, mitochondrial;
DE            EC=1.2.1.24;
DE   AltName: Full=Aldehyde dehydrogenase family 5 member A1;
DE   AltName: Full=NAD(+)-dependent succinic semialdehyde dehydrogenase;
DE   Flags: Precursor;
GN   Name=Aldh5a1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   PROTEIN SEQUENCE OF 57-87; 115-123; 129-160; 162-172; 181-201;
RP   254-289; 291-320; 323-333; 339-347; 358-375; 401-436; 469-496 AND
RP   507-516, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Catalyzes one step in the degradation of the inhibitory
CC       neurotransmitter gamma-aminobutyric acid (GABA) (By similarity).
CC   -!- CATALYTIC ACTIVITY: Succinate semialdehyde + NAD(+) + H(2)O =
CC       succinate + NADH.
CC   -!- ENZYME REGULATION: Redox-regulated. Inhibited under oxydizing
CC       conditions (By similarity).
CC   -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
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DR   EMBL; AK052703; BAC35105.1; -; mRNA.
DR   EMBL; AK144030; BAE25663.1; -; mRNA.
DR   EMBL; AL589699; CAI26086.1; -; Genomic_DNA.
DR   IPI; IPI00273164; -.
DR   RefSeq; NP_766120.1; NM_172532.3.
DR   UniGene; Mm.393311; -.
DR   ProteinModelPortal; Q8BWF0; -.
DR   SMR; Q8BWF0; 44-523.
DR   STRING; Q8BWF0; -.
DR   PhosphoSite; Q8BWF0; -.
DR   PRIDE; Q8BWF0; -.
DR   Ensembl; ENSMUST00000037615; ENSMUSP00000040591; ENSMUSG00000035936.
DR   GeneID; 214579; -.
DR   KEGG; mmu:214579; -.
DR   NMPDR; fig|10090.3.peg.27594; -.
DR   UCSC; uc007pwq.1; mouse.
DR   CTD; 214579; -.
DR   MGI; MGI:2441982; Aldh5a1.
DR   eggNOG; roNOG15833; -.
DR   GeneTree; ENSGT00550000075018; -.
DR   HOGENOM; HBG752218; -.
DR   HOVERGEN; HBG108515; -.
DR   InParanoid; Q8BWF0; -.
DR   OMA; MIQNKDD; -.
DR   OrthoDB; EOG4255SZ; -.
DR   PhylomeDB; Q8BWF0; -.
DR   BRENDA; 1.2.1.24; 244.
DR   NextBio; 374368; -.
DR   ArrayExpress; Q8BWF0; -.
DR   Bgee; Q8BWF0; -.
DR   CleanEx; MM_ALDH5A1; -.
DR   Genevestigator; Q8BWF0; -.
DR   GermOnline; ENSMUSG00000035936; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0004777; F:succinate-semialdehyde dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0006083; P:acetate metabolic process; IMP:MGI.
DR   GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
DR   GO; GO:0006681; P:galactosylceramide metabolic process; IMP:MGI.
DR   GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; ISS:UniProtKB.
DR   GO; GO:0006006; P:glucose metabolic process; IMP:MGI.
DR   GO; GO:0006678; P:glucosylceramide metabolic process; IMP:MGI.
DR   GO; GO:0006536; P:glutamate metabolic process; IMP:MGI.
DR   GO; GO:0006541; P:glutamine metabolic process; IMP:MGI.
DR   GO; GO:0006749; P:glutathione metabolic process; IMP:MGI.
DR   GO; GO:0006650; P:glycerophospholipid metabolic process; IMP:MGI.
DR   GO; GO:0042135; P:neurotransmitter catabolic process; IMP:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0022904; P:respiratory electron transport chain; IMP:MGI.
DR   GO; GO:0046459; P:short-chain fatty acid metabolic process; IMP:MGI.
DR   GO; GO:0006105; P:succinate metabolic process; IMP:MGI.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR010102; Succ_semiAld_DH.
DR   Gene3D; G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 1.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   PANTHER; PTHR11699; Aldehyde_dehyd; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; Aldehyde_DH/Histidinol_DH; 1.
DR   TIGRFAMs; TIGR01780; SSADH; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Disulfide bond; Mitochondrion;
KW   NAD; Oxidoreductase; Phosphoprotein; Transit peptide.
FT   TRANSIT       1     35       Mitochondrion (By similarity).
FT   CHAIN        36    523       Succinate-semialdehyde dehydrogenase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000007185.
FT   NP_BIND     216    219       NAD (By similarity).
FT   NP_BIND     272    277       NAD (By similarity).
FT   ACT_SITE    294    294       Proton acceptor (By similarity).
FT   ACT_SITE    328    328       Nucleophile (By similarity).
FT   BINDING     201    201       NAD (By similarity).
FT   BINDING     201    201       Substrate (By similarity).
FT   BINDING     322    322       Substrate (By similarity).
FT   BINDING     486    486       Substrate (By similarity).
FT   SITE        193    193       Transition state stabilizer (By
FT                                similarity).
FT   MOD_RES      67     67       Phosphotyrosine.
FT   MOD_RES     114    114       N6-acetyllysine (By similarity).
FT   DISULFID    328    330       In inhibited form (By similarity).
SQ   SEQUENCE   523 AA;  55968 MW;  E0CF82E4F4FAE9D0 CRC64;
     MATCFLLRSF WAARPALPPP GRFRPEPAGT PRRSYASGPG GLHADLLRGD SFVGGRWLPA
     PATFPVYDPA SGAKLGTVAD CGVPEARAAV RAAYDAFNSW KGVSVKERSL LLRKWYDLMI
     QNKDDLAKII TAESGKPLKE AQGEILYSAL FLEWFSEEAR RIYGDIIYTS AKDKRGLVLK
     QPVGVAAIIT PWNFPSAMIT RKVGAALAAG CTVVVKPAED TPYSALALAQ LANQAGIPAG
     VYNVIPCSRN KAKEVGEVLC TDPLVSKISF TGSTATGKIL LHHAANSVKR VSMELGGLAP
     FIVFDSANVD QAVAGAMASK FRNAGQTCVC SNRFLVQRGI HDSFVTKFAE AMKKSLRVGN
     GFEEGTTQGP LINEKAVEKV EKQVNDAVAK GATVVTGGKR HQSGGNFFEP TLLSNVTRDM
     LCITEETFGP LAPVIKFDKE EEAVAIANAA EVGLAGYFYS QDPAQIWRVA EQLEVGMVGV
     NEGLISSVEC PFGGVKQSGL GREGSKYGID EYLEVKYVCY GGL
//
ID   ARRB1_MOUSE             Reviewed;         418 AA.
AC   Q8BWG8; Q3UH95; Q8BTJ5;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Beta-arrestin-1;
DE   AltName: Full=Arrestin beta-1;
GN   Name=Arrb1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1A AND 1B).
RC   STRAIN=C57BL/6J; TISSUE=Colon, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1B).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION IN AKT1 SIGNALING.
RX   PubMed=14534298; DOI=10.1074/jbc.M309968200;
RA   Povsic T.J., Kohout T.A., Lefkowitz R.J.;
RT   "Beta-arrestin1 mediates insulin-like growth factor 1 (IGF-1)
RT   activation of phosphatidylinositol 3-kinase (PI3K) and anti-
RT   apoptosis.";
RL   J. Biol. Chem. 278:51334-51339(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-47, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [5]
RP   FUNCTION IN BETA-ADRENERGIC RECEPTOR REGULATION.
RX   PubMed=18337459; DOI=10.1096/fj.07-102459;
RA   Deshpande D.A., Theriot B.S., Penn R.B., Walker J.K.;
RT   "Beta-arrestins specifically constrain beta2-adrenergic receptor
RT   signaling and function in airway smooth muscle.";
RL   FASEB J. 22:2134-2141(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Functions in regulating agonist-mediated G-protein
CC       coupled receptor (GPCR) signaling by mediating both receptor
CC       desensitization and resensitization processes. During homologous
CC       desensitization, beta-arrestins bind to the GPRK-phosphorylated
CC       receptor and sterically preclude its coupling to the cognate G-
CC       protein; the binding appears to require additional receptor
CC       determinants exposed only in the active receptor conformation. The
CC       beta-arrestins target many receptors for internalization by acting
CC       as endocytic adapters (CLASPs, clathrin-associated sorting
CC       proteins) and recruiting the GPRCs to the adapter protein 2
CC       complex 2 (AP-2) in clathrin-coated pits (CCPs). However, the
CC       extent of beta-arrestin involvement appears to vary significantly
CC       depending on the receptor, agonist and cell type. Internalized
CC       arrestin-receptor complexes traffic to intracellular endosomes,
CC       where they remain uncoupled from G-proteins. Two different modes
CC       of arrestin-mediated internalization occur. Class A receptors,
CC       like ADRB2, OPRM1, ENDRA, D1AR and ADRA1B dissociate from beta-
CC       arrestin at or near the plasma membrane and undergo rapid
CC       recycling. Class B receptors, like AVPR2, AGTR1, NTSR1, TRHR and
CC       TACR1 internalize as a complex with arrestin and traffic with it
CC       to endosomal vesicles, presumably as desensitized receptors, for
CC       extended periods of time. Receptor resensitization then requires
CC       that receptor-bound arrestin is removed so that the receptor can
CC       be dephosphorylated and returned to the plasma membrane. Involved
CC       in internalization of P2RY4 and UTP-stimulated internalization of
CC       P2RY2. Involved in phopshorylation-dependent internalization of
CC       OPRD1 ands subsequent recycling. Involved in the degradation of
CC       cAMP by recruiting cAMP phosphodiesterases to ligand-activated
CC       receptors. Beta-arrestins function as multivalent adapter proteins
CC       that can switch the GPCR from a G-protein signaling mode that
CC       transmits short-lived signals from the plasma membrane via small
CC       molecule second messengers and ion channels to a beta-arrestin
CC       signaling mode that transmits a distinct set of signals that are
CC       initiated as the receptor internalizes and transits the
CC       intracellular compartment. Acts as signaling scaffold for MAPK
CC       pathways such as MAPK1/3 (ERK1/2). ERK1/2 activated by the beta-
CC       arrestin scaffold is largely excluded from the nucleus and
CC       confined to cytoplasmic locations such as endocytic vesicles, also
CC       called beta-arrestin signalosomes. Recruits c-Src/SRC to ADRB2
CC       resulting in ERK activation. GPCRs for which the beta-arrestin-
CC       mediated signaling relies on both ARRB1 and ARRB2 (codependent
CC       regulation) include ADRB2, F2RL1 and PTH1R. For some GPCRs the
CC       beta-arrestin-mediated signaling relies on either ARRB1 or ARRB2
CC       and is inhibited by the other respective beta-arrestin form
CC       (reciprocal regulation). Inhibits ERK1/2 signaling in AGTR1- and
CC       AVPR2-mediated activation (reciprocal regulation). Is required for
CC       SP-stimulated endocytosis of NK1R and recruits c-Src/SRC to
CC       internalized NK1R resulting in ERK1/2 activation, which is
CC       required for the antiapoptotic effects of SP. Is involved in
CC       proteinase-activated F2RL1-mediated ERK activity. Acts as
CC       signaling scaffold for the AKT1 pathway. Is involved in alpha-
CC       thrombin-stimulated AKT1 signaling. Is involved in IGF1-stimulated
CC       AKT1 signaling leading to increased protection from apoptosis.
CC       Involved in activation of the p38 MAPK signaling pathway and in
CC       actin bundle formation. Involved in F2RL1-mediated cytoskeletal
CC       rearrangement and chemotaxis. Involved in AGTR1-mediated stress
CC       fiber formation by acting together with GNAQ to activate RHOA.
CC       Appears to function as signaling scaffold involved in regulation
CC       of MIP-1-beta-stimulated CCR5-dependent chemotaxis. Involved in
CC       attenuation of NF-kappa-B-dependent transcription in response to
CC       GPCR or cytokine stimulation by interacting with and stabilizing
CC       CHUK. May serve as nuclear messenger for GPCRs. Involved in OPRD1-
CC       stimulated transcriptional regulation by translocating to CDKN1B
CC       and FOS promoter regions and recruiting EP300 resulting in
CC       acetylation of histone H4. Involved in regulation of LEF1
CC       transcriptional activity via interaction with DVL1 and/or DVL2
CC       Also involved in regulation of receptors others than GPCRs.
CC       Involved in Toll-like receptor and IL-1 receptor signaling through
CC       the interaction with TRAF6 which prevents TRAF6 autoubiquitination
CC       and oligomerization required for activation of NF-kappa-B and JUN.
CC       Binds phosphoinositides. Binds inositolhexakisphosphate (InsP6)
CC       (By similarity).
CC   -!- SUBUNIT: Monomer. Homodimer. Homooligomer; the self-association is
CC       mediated by InsP6-binding. Heterooligomer with ARRB2; the
CC       association is mediated by InsP6-binding. Interacts with ADRB2
CC       (phosphorylated). Interacts with CHRM2 (phosphorylated). Interacts
CC       with LHCGR. Interacts with CYTH2 and CASR. Interacts with AP2B1
CC       (dephosphorylated); phosphorylation of AP2B1 disrupts the
CC       interaction. Interacts (dephosphorylated at Ser-412) with CLTC.
CC       Interacts with CCR2 and ADRBK1. Interacts with CRR5. Interacts
CC       with PTAFR (phosphorylated on serine residues). Interacts with
CC       CLTC and MAP2K3. Interacts with CREB1. Interacts with TRAF6.
CC       Interacts with IGF1R and MDM2. Interacts with C5AR1. Interacts
CC       with PDE4D. Interacts with SRC (via the SH3 domain and the protein
CC       kinase domain); the interaction is independent of the
CC       phosphorylation state of SRC C-terminus. Interacts with TACR1.
CC       Interacts with RAF1. Interacts with DVL1; the interaction is
CC       enhanced by phosphorylation of DVL1. Interacts with DVL2; the
CC       interaction is enhanced by phosphorylation of DVL2. Interacts with
CC       IGF1R. Interacts with CHUK, IKBKB and MAP3K14. Associates with MAP
CC       kinase p38. Part of a MAPK signaling complex consisting of TACR1,
CC       ARRB1, SRC, MAPK1 (activated) and MAPK3 (activated). Part of a
CC       MAPK signaling complex consisting of F2RL1, ARRB1, RAF1, MAPK1
CC       (activated) and MAPK3 (activated). Interacts with GPR143 (By
CC       similarity).
CC   -!- INTERACTION:
CC       O54946:Dnajb6; NbExp=2; IntAct=EBI-641778, EBI-642500;
CC       O35387:Hax1; NbExp=3; IntAct=EBI-641778, EBI-642449;
CC       P23804:Mdm2; NbExp=2; IntAct=EBI-641778, EBI-641788;
CC       Q9ES97:Rtn3; NbExp=2; IntAct=EBI-641778, EBI-643369;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Cell membrane (By similarity). Membrane, clathrin-
CC       coated pit (Probable). Cell projection, pseudopodium (By
CC       similarity). Cytoplasmic vesicle (By similarity).
CC       Note=Translocates to the plasma membrane and colocalizes with
CC       antagonist-stimulated GPCRs. The monomeric form is predominantly
CC       located in the nucleus. The oligomeric form is located in the
CC       cytoplasm. Translocates to the nucleus upon stimulation of OPRD1
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1A;
CC         IsoId=Q8BWG8-1; Sequence=Displayed;
CC       Name=1B;
CC         IsoId=Q8BWG8-2; Sequence=VSP_019545;
CC   -!- DOMAIN: The [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif mediates
CC       interaction the AP-2 complex subunit AP2B1. Binding to
CC       phosphorylated GPCRs induces a conformationanl change that exposes
CC       the motif to the surface (By similarity).
CC   -!- DOMAIN: The N-terminus binds InsP6 with low affinity (By
CC       similarity).
CC   -!- DOMAIN: The C-terminus binds InsP6 with high affinity (By
CC       similarity).
CC   -!- PTM: Constitutively phosphorylated at in the cytoplasm. At the
CC       plasma membrane, is rapidly dephosphorylated, a process that is
CC       required for clathrin binding and ADRB2 endocytosis but not for
CC       ADRB2 binding and desensitization. Once internalized, is
CC       rephosphorylated (By similarity).
CC   -!- PTM: The ubiquitination status appears to regulate the formation
CC       and trafficking of beta-arrestin-GPCR complexes and signaling.
CC       Ubiquitination appears to occur GPCR-specific. Ubiquitinated by
CC       MDM2; the ubiquitination is required for rapid internalization of
CC       ADRB2. Deubiquitinated by USP33; the deubiquitination leads to a
CC       dissociation of the beta-arrestin-GPCR complex. Stimulation of a
CC       class A GPCR, such as ADRB2, induces transient ubiquitination and
CC       subsequently promotes association with USP33 (By similarity).
CC   -!- SIMILARITY: Belongs to the arrestin family.
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DR   EMBL; AK052588; BAC35050.1; -; mRNA.
DR   EMBL; AK090090; BAC41087.1; -; mRNA.
DR   EMBL; AK144054; BAE25673.1; -; mRNA.
DR   EMBL; AK147508; BAE27962.1; -; mRNA.
DR   EMBL; AK165514; BAE38230.1; -; mRNA.
DR   EMBL; BC108969; AAI08970.1; -; mRNA.
DR   EMBL; BC108970; AAI08971.1; -; mRNA.
DR   IPI; IPI00274186; -.
DR   IPI; IPI00761566; -.
DR   RefSeq; NP_796205.1; NM_177231.2.
DR   RefSeq; NP_835738.1; NM_178220.3.
DR   UniGene; Mm.260193; -.
DR   ProteinModelPortal; Q8BWG8; -.
DR   SMR; Q8BWG8; 5-393.
DR   IntAct; Q8BWG8; 30.
DR   STRING; Q8BWG8; -.
DR   PhosphoSite; Q8BWG8; -.
DR   PRIDE; Q8BWG8; -.
DR   Ensembl; ENSMUST00000032995; ENSMUSP00000032995; ENSMUSG00000018909.
DR   Ensembl; ENSMUST00000098266; ENSMUSP00000095866; ENSMUSG00000018909.
DR   GeneID; 109689; -.
DR   KEGG; mmu:109689; -.
DR   UCSC; uc009ilu.1; mouse.
DR   UCSC; uc009ilv.1; mouse.
DR   CTD; 109689; -.
DR   MGI; MGI:99473; Arrb1.
DR   GeneTree; ENSGT00390000013152; -.
DR   HOGENOM; HBG315972; -.
DR   HOVERGEN; HBG002399; -.
DR   InParanoid; Q8BWG8; -.
DR   OMA; FVDHIDL; -.
DR   OrthoDB; EOG4MCX0K; -.
DR   NextBio; 362583; -.
DR   ArrayExpress; Q8BWG8; -.
DR   Bgee; Q8BWG8; -.
DR   CleanEx; MM_ARRB1; -.
DR   Genevestigator; Q8BWG8; -.
DR   GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031143; C:pseudopodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0007602; P:phototransduction; IMP:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007600; P:sensory perception; IEA:InterPro.
DR   InterPro; IPR000698; Arrestin.
DR   InterPro; IPR011022; Arrestin-like_C.
DR   InterPro; IPR011021; Arrestin-like_N.
DR   InterPro; IPR014752; Arrestin_C.
DR   InterPro; IPR017864; Arrestin_CS.
DR   InterPro; IPR014753; Arrestin_N.
DR   InterPro; IPR014756; Ig_E-set.
DR   Gene3D; G3DSA:2.60.40.640; Arrestin_C; 1.
DR   Gene3D; G3DSA:2.60.40.840; Arrestin_N; 1.
DR   PANTHER; PTHR11792; Arrestin; 1.
DR   Pfam; PF02752; Arrestin_C; 1.
DR   Pfam; PF00339; Arrestin_N; 1.
DR   PRINTS; PR00309; ARRESTIN.
DR   SUPFAM; SSF81296; Ig_E-set; 2.
DR   PROSITE; PS00295; ARRESTINS; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cell projection; Coated pit;
KW   Cytoplasm; Cytoplasmic vesicle; Membrane; Nucleus; Phosphoprotein;
KW   Protein transport; Signal transduction inhibitor; Transcription;
KW   Transcription regulation; Transport; Ubl conjugation.
FT   CHAIN         1    418       Beta-arrestin-1.
FT                                /FTId=PRO_0000205195.
FT   REGION        1    163       Interaction with SRC (By similarity).
FT   REGION       45     86       Interaction with CHRM2 (By similarity).
FT   REGION      318    418       Interaction with TRAF6 (By similarity).
FT   BINDING     250    250       Inositol hexakisphosphate (By
FT                                similarity).
FT   BINDING     255    255       Inositol hexakisphosphate (By
FT                                similarity).
FT   BINDING     324    324       Inositol hexakisphosphate (By
FT                                similarity).
FT   BINDING     326    326       Inositol hexakisphosphate (By
FT                                similarity).
FT   MOD_RES      47     47       Phosphotyrosine.
FT   MOD_RES     410    410       Phosphothreonine (By similarity).
FT   MOD_RES     412    412       Phosphoserine.
FT   VAR_SEQ     334    341       Missing (in isoform 1B).
FT                                /FTId=VSP_019545.
SQ   SEQUENCE   418 AA;  46973 MW;  389C24F8CDA06E64 CRC64;
     MGDKGTRVFK KASPNGKLTV YLGKRDFVDH IDLVDPVDGV VLVDPEYLKE RRVYVTLTCA
     FRYGREDLDV LGLTFRKDLF VANVQSFPPA PEDKKPLTRL QERLIKKLGE HACPFTFEIP
     PNLPCSVTLQ PGPEDTGKAC GVDYEVKAFC AENLEEKIHK RNSVRLVIRK VQYAPERPGP
     QPTAETTRQF LMSDKPLHLE ASLDKEIYYH GEPISVNVHV TNNTNKTVKK IKISVRQYAD
     ICLFNTAQYK CPVAMEEADD NVAPSSTFCK VYTLTPFLAN NREKRGLALD GKLKHEDTNL
     ASSTLLREGA NREILGIIVS YKVKVKLVVS RGGLLGDLAS SDVAVELPFT LMHPKPKEEP
     PHREVPESET PVDTNLIELD TNDDDIVFED FARQRLKGMK DDKDEEDDGT GSPHLNNR
//
ID   CRCM1_MOUSE             Reviewed;         304 AA.
AC   Q8BWG9; Q8BUD4; Q8R586;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Calcium release-activated calcium channel protein 1;
DE   AltName: Full=Protein orai-1;
DE   AltName: Full=Transmembrane protein 142A;
GN   Name=Orai1; Synonyms=Cracm1, Tmem142a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-304.
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Ca(2+) release-activated Ca(2+) (CRAC) channel subunit
CC       which mediates Ca(2+) influx following depletion of intracellular
CC       Ca(2+) stores and channel activation by the Ca(2+) sensor, STIM1.
CC       CRAC channels are the main pathway for Ca(2+) influx in T-cells
CC       and promote the immune response to pathogens by activating the
CC       transcription factor NFAT (By similarity).
CC   -!- SUBUNIT: Interacts with STIM1 and STIM2. Interacts with
CC       EFCAB4B/CRACR2A; the interaction is direct and takes place in
CC       absence of Ca(2+). Forms a complex with EFCAB4B/CRACR2A and STIM1
CC       at low concentration of Ca(2+), the complex dissociates at
CC       elevated Ca(2+) concentrations (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the Orai family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH23149.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK052573; BAC35045.1; -; mRNA.
DR   EMBL; AK085755; BAC39533.1; -; mRNA.
DR   EMBL; BC023149; AAH23149.1; ALT_INIT; mRNA.
DR   IPI; IPI00226276; -.
DR   RefSeq; NP_780632.1; NM_175423.3.
DR   UniGene; Mm.218582; -.
DR   STRING; Q8BWG9; -.
DR   PhosphoSite; Q8BWG9; -.
DR   PRIDE; Q8BWG9; -.
DR   Ensembl; ENSMUST00000051016; ENSMUSP00000058169; ENSMUSG00000049686.
DR   Ensembl; ENSMUST00000121652; ENSMUSP00000113097; ENSMUSG00000049686.
DR   GeneID; 109305; -.
DR   KEGG; mmu:109305; -.
DR   UCSC; uc008zmy.1; mouse.
DR   CTD; 109305; -.
DR   MGI; MGI:1925542; Orai1.
DR   GeneTree; ENSGT00390000015354; -.
DR   HOGENOM; HBG715505; -.
DR   HOVERGEN; HBG081343; -.
DR   InParanoid; Q8BWG9; -.
DR   OMA; GDHPLTP; -.
DR   OrthoDB; EOG4WH8MR; -.
DR   PhylomeDB; Q8BWG9; -.
DR   NextBio; 361899; -.
DR   ArrayExpress; Q8BWG9; -.
DR   Bgee; Q8BWG9; -.
DR   Genevestigator; Q8BWG9; -.
DR   GermOnline; ENSMUSG00000049686; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; ISS:UniProtKB.
DR   GO; GO:0015279; F:store-operated calcium channel activity; ISS:UniProtKB.
DR   GO; GO:0051928; P:positive regulation of calcium ion transport; ISS:UniProtKB.
DR   InterPro; IPR012446; DUF1650.
DR   Pfam; PF07856; DUF1650; 1.
PE   2: Evidence at transcript level;
KW   Adaptive immunity; Calcium; Calcium channel; Calcium transport;
KW   Cell membrane; Glycoprotein; Immunity; Ion transport; Ionic channel;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    304       Calcium release-activated calcium channel
FT                                protein 1.
FT                                /FTId=PRO_0000234382.
FT   TOPO_DOM      1     89       Cytoplasmic (Potential).
FT   TRANSMEM     90    107       Helical; (Potential).
FT   TOPO_DOM    108    121       Extracellular (Potential).
FT   TRANSMEM    122    142       Helical; (Potential).
FT   TOPO_DOM    143    175       Cytoplasmic (Potential).
FT   TRANSMEM    176    196       Helical; (Potential).
FT   TOPO_DOM    197    237       Extracellular (Potential).
FT   TRANSMEM    238    258       Helical; (Potential).
FT   TOPO_DOM    259    304       Cytoplasmic (Potential).
FT   COMPBIAS     43     50       Poly-Pro.
FT   MOD_RES     298    298       Phosphothreonine (By similarity).
FT   CARBOHYD    225    225       N-linked (GlcNAc...) (Potential).
FT   CONFLICT     16     16       L -> F (in Ref. 2; AAH23149).
SQ   SEQUENCE   304 AA;  33062 MW;  9743395B63D2E41F CRC64;
     MHPEPAPPPS HSNPELPVSG GSSTSGSRRS RRRSGDGEPS GAPPLPPPPP AVSYPDWIGQ
     SYSEVMSLNE HSMQALSWRK LYLSRAKLKA SSRTSALLSG FAMVAMVEVQ LDTDHDYPPG
     LLIVFSACTT VLVAVHLFAL MISTCILPNI EAVSNVHNLN SVKESPHERM HRHIELAWAF
     STVIGTLLFL AEVVLLCWVK FLPLKRQAGQ PSPTKPPAES VIVANHSDSS GITPGEAAAI
     ASTAIMVPCG LVFIVFAVHF YRSLVSHKTD RQFQELNELA EFARLQDQLD HRGDHSLTPG
     THYA
//
ID   S38A7_MOUSE             Reviewed;         463 AA.
AC   Q8BWH0; Q3TBN9; Q8K2B1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Putative sodium-coupled neutral amino acid transporter 7;
GN   Name=Slc38a7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Putative sodium-dependent amino acid/proton antiporter
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2
CC       family.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK052548; BAC35035.1; -; mRNA.
DR   EMBL; AK171137; BAE42270.1; -; mRNA.
DR   EMBL; BC031853; AAH31853.1; -; mRNA.
DR   IPI; IPI00395204; -.
DR   RefSeq; NP_766346.1; NM_172758.4.
DR   UniGene; Mm.29267; -.
DR   UniGene; Mm.476852; -.
DR   UniGene; Mm.477198; -.
DR   ProteinModelPortal; Q8BWH0; -.
DR   PhosphoSite; Q8BWH0; -.
DR   Ensembl; ENSMUST00000040481; ENSMUSP00000037023; ENSMUSG00000036534.
DR   GeneID; 234595; -.
DR   KEGG; mmu:234595; -.
DR   UCSC; uc009mzg.1; mouse.
DR   CTD; 234595; -.
DR   MGI; MGI:2679005; Slc38a7.
DR   eggNOG; roNOG04695; -.
DR   GeneTree; ENSGT00590000083116; -.
DR   HOGENOM; HBG444764; -.
DR   HOVERGEN; HBG055999; -.
DR   InParanoid; Q8BWH0; -.
DR   OMA; MGTGICG; -.
DR   OrthoDB; EOG46143X; -.
DR   PhylomeDB; Q8BWH0; -.
DR   NextBio; 382240; -.
DR   ArrayExpress; Q8BWH0; -.
DR   Bgee; Q8BWH0; -.
DR   CleanEx; MM_SLC38A7; -.
DR   Genevestigator; Q8BWH0; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR013057; AA_transpt_TM.
DR   Pfam; PF01490; Aa_trans; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Ion transport; Membrane; Phosphoprotein; Sodium;
KW   Sodium transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    463       Putative sodium-coupled neutral amino
FT                                acid transporter 7.
FT                                /FTId=PRO_0000319598.
FT   TRANSMEM     56     76       Helical; (Potential).
FT   TRANSMEM     82    102       Helical; (Potential).
FT   TRANSMEM    130    150       Helical; (Potential).
FT   TRANSMEM    179    199       Helical; (Potential).
FT   TRANSMEM    206    226       Helical; (Potential).
FT   TRANSMEM    240    260       Helical; (Potential).
FT   TRANSMEM    283    303       Helical; (Potential).
FT   TRANSMEM    320    340       Helical; (Potential).
FT   TRANSMEM    372    392       Helical; (Potential).
FT   TRANSMEM    396    416       Helical; (Potential).
FT   TRANSMEM    429    449       Helical; (Potential).
FT   MOD_RES      28     28       Phosphoserine.
FT   CONFLICT     11     11       S -> SG (in Ref. 2; AAH31853).
FT   CONFLICT     30     30       C -> R (in Ref. 1; BAE42270).
FT   CONFLICT    159    159       A -> V (in Ref. 2; AAH31853).
SQ   SEQUENCE   463 AA;  49913 MW;  3DF98B8EAE2E12E3 CRC64;
     MAQVSINSDY SEWASSTDAG ERARLLQSPC VDVVPKSEGE ASPGDPDSGT TSTLGAVFIV
     VNACLGAGLL NFPAAFSTAG GVAAGIALQM GMLVFIISGL VILAYCSQAS NERTYQEVVW
     AVCGKLTGVL CEVAIAVYTF GTCIAFLIII GDQQDKIIAV MSKEPDGASG SPWYTDRKFT
     ISLTAFLFIL PLSIPKEIGF QKYASFLSVV GTWYVTAIII IKYIWPDKEM RPGDILTRPA
     SWMAVFNAMP TICFGFQCHV SSVPVFNSMR QPEVKTWGGV VTAAMVIALA VYMGTGICGF
     LTFGAAVDPD VLRSYPSEDV AVAVARAFII LSVLTSYPIL HFCGRAVVEG LWLRYKGMPV
     EEDVGRERRR RVLQTLVWFL LTLLLALFIP DIGKVISVIG GLAACFIFIF PGLCLIQAKL
     SEMEEVKPAS WWALVSYGVL LVTLGAFIFG QTTANAIFVD LLA
//
ID   PGES2_MOUSE             Reviewed;         384 AA.
AC   Q8BWM0; Q99J30;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Prostaglandin E synthase 2;
DE            EC=5.3.99.3;
DE   AltName: Full=GATE-binding factor 1;
DE            Short=GBF-1;
DE   AltName: Full=Microsomal prostaglandin E synthase 2;
DE            Short=mPGES-2;
DE   Contains:
DE     RecName: Full=Prostaglandin E synthase 2 truncated form;
GN   Name=Ptges2; Synonyms=Gbf1, Pges2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], POSSIBLE FUNCTION, POSSIBLE SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Kidney;
RX   PubMed=12050152; DOI=10.1074/jbc.M202679200;
RA   Hu J., Meng Q., Roy S.K., Raha A., Hu J., Zhang J., Hashimoto K.,
RA   Kalvakolanu D.V.;
RT   "A novel transactivating factor that regulates interferon-gamma-
RT   dependent gene expression.";
RL   J. Biol. Chem. 277:30253-30263(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=12835322; DOI=10.1074/jbc.M305108200;
RA   Murakami M., Nakashima K., Kamei D., Masuda S., Ishikawa Y., Ishii T.,
RA   Ohmiya Y., Watanabe K., Kudo I.;
RT   "Cellular prostaglandin E2 production by membrane-bound prostaglandin
RT   E synthase-2 via both cyclooxygenases-1 and -2.";
RL   J. Biol. Chem. 278:37937-37947(2003).
RN   [5]
RP   INDUCTION.
RX   PubMed=15584915; DOI=10.1111/j.1471-4159.2004.02829.x;
RA   Bosetti F., Langenbach R., Weerasinghe G.R.;
RT   "Prostaglandin E2 and microsomal prostaglandin E synthase-2 expression
RT   are decreased in the cyclooxygenase-2-deficient mouse brain despite
RT   compensatory induction of cyclooxygenase-1 and Ca2+-dependent
RT   phospholipase A2.";
RL   J. Neurochem. 91:1389-1397(2004).
RN   [6]
RP   INTERACTION WITH CEBPB.
RX   PubMed=15879117; DOI=174/10/6203;
RA   Meng Q., Raha A., Roy S., Hu J., Kalvakolanu D.V.;
RT   "IFN-gamma-stimulated transcriptional activation by IFN-gamma-
RT   activated transcriptional element-binding factor 1 occurs via an
RT   inducible interaction with CAAAT/enhancer-binding protein-beta.";
RL   J. Immunol. 174:6203-6211(2005).
CC   -!- FUNCTION: Isomerase that catalyzes the conversion of unstable
CC       intermediate of prostaglandin E2 H2 (PGH2) into the more stable
CC       prostaglandin E2 (PGE2) form (By similarity). May also have
CC       transactivation activity toward IFN-gamma (IFNG), possibly via an
CC       interaction with CEBPB; however, the relevance of transcription
CC       activation activity remains unclear.
CC   -!- CATALYTIC ACTIVITY: (5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15-
CC       hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-11-alpha,15-
CC       dihydroxy-9-oxoprosta-5,13-dienoate.
CC   -!- COFACTOR: Dihydrolipoic acid (By similarity).
CC   -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC   -!- SUBUNIT: Homodimer (By similarity). May interact with CEBPB.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass
CC       membrane protein. Nucleus. Note=According to PubMed:12050152, some
CC       fraction may be nuclear.
CC   -!- SUBCELLULAR LOCATION: Prostaglandin E synthase 2 truncated form:
CC       Cytoplasm. Note=Synthetized as a Golgi membrane-bound protein,
CC       which is further cleaved into the predominant soluble truncated
CC       form.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed in brain, heart,
CC       liver, colon and lung.
CC   -!- INDUCTION: Constitutively expressed. Not induced during tissue
CC       inflammation. Down-regulated in the absence of Ptges.
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC   -!- SIMILARITY: Contains 1 glutaredoxin domain.
CC   -!- SIMILARITY: Contains 1 GST C-terminal domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK050616; BAC34345.1; -; mRNA.
DR   EMBL; BC004846; AAH04846.1; -; mRNA.
DR   IPI; IPI00312174; -.
DR   RefSeq; NP_598544.2; NM_133783.2.
DR   UniGene; Mm.28048; -.
DR   ProteinModelPortal; Q8BWM0; -.
DR   SMR; Q8BWM0; 99-372.
DR   STRING; Q8BWM0; -.
DR   PhosphoSite; Q8BWM0; -.
DR   PRIDE; Q8BWM0; -.
DR   Ensembl; ENSMUST00000028162; ENSMUSP00000028162; ENSMUSG00000026820.
DR   GeneID; 96979; -.
DR   KEGG; mmu:96979; -.
DR   UCSC; uc008jfm.1; mouse.
DR   CTD; 96979; -.
DR   MGI; MGI:1917592; Ptges2.
DR   GeneTree; ENSGT00390000000224; -.
DR   HOGENOM; HBG608835; -.
DR   HOVERGEN; HBG069136; -.
DR   InParanoid; Q8BWM0; -.
DR   OrthoDB; EOG4R7VB3; -.
DR   BRENDA; 5.3.99.3; 244.
DR   NextBio; 352423; -.
DR   ArrayExpress; Q8BWM0; -.
DR   Bgee; Q8BWM0; -.
DR   CleanEx; MM_PTGES2; -.
DR   Genevestigator; Q8BWM0; -.
DR   GermOnline; ENSMUSG00000026820; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050220; F:prostaglandin-E synthase activity; IEA:EC.
DR   GO; GO:0015035; F:protein disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0016563; F:transcription activator activity; IDA:MGI.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0001516; P:prostaglandin biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0046903; P:secretion; IDA:MGI.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:1.20.1050.10; GST_C_like; 1.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   SUPFAM; SSF47616; GST_C_like; 1.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 1.
DR   PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR   PROSITE; PS50405; GST_CTER; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Cytoplasm; Fatty acid biosynthesis; Golgi apparatus; Isomerase;
KW   Lipid synthesis; Membrane; Nucleus; Phosphoprotein;
KW   Prostaglandin biosynthesis; Transmembrane; Transmembrane helix.
FT   CHAIN         1    384       Prostaglandin E synthase 2.
FT                                /FTId=PRO_0000013131.
FT   CHAIN        87    384       Prostaglandin E synthase 2 truncated form
FT                                (By similarity).
FT                                /FTId=PRO_0000013132.
FT   TOPO_DOM      1     56       Lumenal (Potential).
FT   TRANSMEM     57     73       Helical; (Potential).
FT   TOPO_DOM     74    384       Cytoplasmic (Potential).
FT   DOMAIN       89    192       Glutaredoxin.
FT   DOMAIN      262    376       GST C-terminal.
FT   REGION      163    164       Glutathione binding (By similarity).
FT   BINDING     147    147       Glutathione; via amide nitrogen and
FT                                carbonyl oxygen (By similarity).
FT   SITE         86     87       Cleavage (By similarity).
FT   MOD_RES     289    289       Phosphoserine (By similarity).
FT   CONFLICT    210    210       P -> L (in Ref. 2; BAC34345).
SQ   SEQUENCE   384 AA;  43308 MW;  733A261413258D44 CRC64;
     MAQAARLSWV LVSSRCALTE GLLTRPWQPL SAQSRAGFTR VAAGSRGAAV RKGSPRLLGA
     AALALGGALG LYHTVRWHQR SQDLRAERSA AQLPLSNSLQ LTLYQYKTCP FCSKVRAFLD
     FHSLPYQVVE VNPVRRTEIK FSSYRKVPIL VAQEGDSLQQ LNDSSVIISA LKTYLVSGQP
     LEEVITYYPP MKAMNDQGKE VTEFCNKYWP MLDEKEAQQM YGGKEARTEE MKWRQWADDW
     LVHLISPNVY RTPAEALASF DYIVREGKFG AVEAAMAKYV GAAAMYLISK RLKSRHHLQD
     DVRVDLYEAA NKWVTAVGKD RPFMGGQKPN LADLAVYGVL RVMEGLEAFD DLMRHSHIQP
     WYLRMERAIE EAPSVHHVNP SCKD
//
ID   DCLK3_MOUSE             Reviewed;         619 AA.
AC   Q8BWQ5; Q1A748;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Serine/threonine-protein kinase DCLK3;
DE            EC=2.7.11.1;
DE   AltName: Full=CLICK-I and II-related;
DE            Short=CLr;
DE   AltName: Full=Doublecortin-like and CAM kinase-like 3;
DE   AltName: Full=Doublecortin-like kinase 3;
GN   Name=Dclk3; Synonyms=Dcamkl3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=16684769; DOI=10.1074/jbc.M513212200;
RA   Ohmae S., Takemoto-Kimura S., Okamura M., Adachi-Morishima A.,
RA   Nonaka M., Fuse T., Kida S., Tanji M., Furuyashiki T., Arakawa Y.,
RA   Narumiya S., Okuno H., Bito H.;
RT   "Molecular identification and characterization of a family of kinases
RT   with homology to Ca2+/calmodulin-dependent protein kinases I/IV.";
RL   J. Biol. Chem. 281:20427-20439(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BWQ5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BWQ5-2; Sequence=VSP_020887;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and to a lower
CC       extent in liver and kidney.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. CaMK subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; DQ286388; ABB89470.1; -; mRNA.
DR   EMBL; AK050312; BAC34182.1; -; mRNA.
DR   EMBL; BC056929; AAH56929.1; -; mRNA.
DR   IPI; IPI00226375; -.
DR   IPI; IPI00756117; -.
DR   RefSeq; NP_766516.2; NM_172928.5.
DR   UniGene; Mm.26361; -.
DR   HSSP; P49137; 1NY3.
DR   ProteinModelPortal; Q8BWQ5; -.
DR   SMR; Q8BWQ5; 337-602.
DR   PhosphoSite; Q8BWQ5; -.
DR   PRIDE; Q8BWQ5; -.
DR   Ensembl; ENSMUST00000035081; ENSMUSP00000035081; ENSMUSG00000032500.
DR   Ensembl; ENSMUST00000111879; ENSMUSP00000107510; ENSMUSG00000032500.
DR   GeneID; 245038; -.
DR   KEGG; mmu:245038; -.
DR   UCSC; uc009rvv.1; mouse.
DR   CTD; 245038; -.
DR   MGI; MGI:3039580; Dclk3.
DR   eggNOG; roNOG08261; -.
DR   GeneTree; ENSGT00600000084006; -.
DR   HOGENOM; HBG283500; -.
DR   HOVERGEN; HBG101914; -.
DR   InParanoid; Q8BWQ5; -.
DR   OMA; EEGWKGD; -.
DR   OrthoDB; EOG43R3M5; -.
DR   PhylomeDB; Q8BWQ5; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 386538; -.
DR   ArrayExpress; Q8BWQ5; -.
DR   Bgee; Q8BWQ5; -.
DR   CleanEx; MM_DCLK3; -.
DR   Genevestigator; Q8BWQ5; -.
DR   GermOnline; ENSMUSG00000032500; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Kinase;
KW   Nucleotide-binding; Nucleus; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN         1    619       Serine/threonine-protein kinase DCLK3.
FT                                /FTId=PRO_0000252255.
FT   DOMAIN      343    600       Protein kinase.
FT   NP_BIND     349    357       ATP (By similarity).
FT   ACT_SITE    464    464       Proton acceptor (By similarity).
FT   BINDING     372    372       ATP (By similarity).
FT   VAR_SEQ       1      1       M -> MPAAPVLRPPPPPATPAPPAPSRPAPPIPGHRGPCD
FT                                HSLKCLSSKISERKLPGPWLPAGRGPLEKPVLGPRGAVMPL
FT                                FSPQSSLHSVRAEHSPLKPRVVTVVKLGGQPLRKATLLLNR
FT                                RSVQTFEQLLSDISEALGFPRWKNDRVRKLFTLKGREVKSV
FT                                SDFFREGDAFIAM (in isoform 2).
FT                                /FTId=VSP_020887.
SQ   SEQUENCE   619 AA;  69634 MW;  FB5367F1DBA1E907 CRC64;
     MGKEPLTLKS IQLAMEELYP KNRALALAPH SRVPSPRLRS RLPSKLLKGS HRCGEAGSYS
     AEMESKAVSR HQGKTSTVLA PEDKARAQKW VRGKQESEPG GPPSPGAATQ EETHASGEKH
     LGVEIEKTSG EIVRCEKCKR ERELQLGLQR EPCPLGTSEL DLGRAQKRDS EKLVRTKSCR
     RPSEAKSTDG EEGWKGDSHR GSPRDPPQEL RRPNSNSDKK EIRGSESQDS HPQGAPKAQK
     DLVEGPPAVE EGPIDMRRED RHTCRSKHAA WLRREQQAEP PQLPRTRGEE KQAEHEKKPG
     GLGERRAPEK ESKRKLEEKR PERPSGRKPR PKGIISADVE KHYDIGGVIG DGNFATVKEC
     RHRETKQAYA MKMIDKSQLK GKEDIVDSEI LIIQSLSHPN IVKLHEVYET EAEIYLIMEY
     VQGGDLFDAI VENVKFPEPE AAVMITDLCK ALVHMHDKNI VHRDVKPENL LVQRNEDKSI
     TLKLADFGLA KYVVRPIFTV CGTPTYVAPE ILSEKGYGLE VDMWAAGVIL YILLCGFPPF
     RSPERDQDEL FNIIQVGQFE FLSPYWDNIS DAAKDLVRNL LEVDPKKRYT AEQVLQHPWI
     EMVGHTNTGN SQKEESPNS
//
ID   GRIN3_MOUSE             Reviewed;         763 AA.
AC   Q8BWS5; Q69Z30;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=G protein-regulated inducer of neurite outgrowth 3;
DE            Short=GRIN3;
GN   Name=Gprin3; Synonyms=Kiaa2027;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [4]
RP   IDENTIFICATION.
RX   PubMed=15488195; DOI=10.1016/S0076-6879(04)90029-8;
RA   Iida N., Kozasa T.;
RT   "Identification and biochemical analysis of GRIN1 and GRIN2.";
RL   Methods Enzymol. 390:475-483(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-326, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May be involved in neurite outgrowth (By similarity).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32614.1; Type=Erroneous initiation;
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DR   EMBL; AK173336; BAD32614.1; ALT_INIT; mRNA.
DR   EMBL; AK050148; BAC34093.1; -; mRNA.
DR   IPI; IPI00226416; -.
DR   RefSeq; NP_899006.1; NM_183183.2.
DR   UniGene; Mm.138080; -.
DR   UniGene; Mm.481808; -.
DR   ProteinModelPortal; Q8BWS5; -.
DR   STRING; Q8BWS5; -.
DR   PhosphoSite; Q8BWS5; -.
DR   PRIDE; Q8BWS5; -.
DR   Ensembl; ENSMUST00000051065; ENSMUSP00000051805; ENSMUSG00000045441.
DR   GeneID; 243385; -.
DR   KEGG; mmu:243385; -.
DR   UCSC; uc009cdk.1; mouse.
DR   CTD; 243385; -.
DR   MGI; MGI:1924785; Gprin3.
DR   eggNOG; roNOG06733; -.
DR   GeneTree; ENSGT00570000079168; -.
DR   HOGENOM; HBG126705; -.
DR   HOVERGEN; HBG079421; -.
DR   InParanoid; Q8BWS5; -.
DR   OMA; TPSRSVK; -.
DR   OrthoDB; EOG45HRWV; -.
DR   PhylomeDB; Q8BWS5; -.
DR   NextBio; 385769; -.
DR   ArrayExpress; Q8BWS5; -.
DR   Bgee; Q8BWS5; -.
DR   CleanEx; MM_GPRIN3; -.
DR   Genevestigator; Q8BWS5; -.
DR   GermOnline; ENSMUSG00000045441; Mus musculus.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    763       G protein-regulated inducer of neurite
FT                                outgrowth 3.
FT                                /FTId=PRO_0000251951.
FT   MOD_RES     326    326       Phosphothreonine.
FT   MOD_RES     327    327       Phosphoserine.
FT   MOD_RES     359    359       Phosphoserine.
SQ   SEQUENCE   763 AA;  80485 MW;  34972AE1BF6CA09B CRC64;
     MGTVPDPLRV TKASIVAASG KEESRGESQS VSPQPAQPDN NASGIGNVPA ELSLQLSAAA
     QALMQACVSE SSQQDMASPG VFSEGEPVSP KQKTPDDFLL HGSKESAAPG LNATAQKELI
     SAPCLISVVQ HTHHAIQRDA PNTSTCAVPE GSLVKSEANS NGENPEKPGC PARVTCCSSK
     NQEGLCDFPS PENSQGILQT PDIASPSADR PEGEGQKVIN NITAVSSEPP VREGCSENKQ
     PSATALNTTA ERSENPPPSH LTSKGATCSS EARQALLPAQ YPVSRFKEAS TMTCQAESGA
     KEVSGRAWQD AEVQAVASVE SRSVSTSPSI LPAYLKENPA PELENGQEQL RVICHGKGSG
     NHLLELSNSM VDSQESRQCP SIVPQVHIQA ATATPAAFKG GCKPANQPAE GLKSPLIHVT
     SSQNTETEED LRLSASKEAT SRQPEGTNPD FQKANAIGQI SLPAGSQAEI NQGLWNSGPR
     EPEIVVKTAK DHKAESSCKP SNSGGGANKD YPPESLDPTD KKGAKDKKPA SPLIVKDHAP
     GATSTLDAKT LLLNPKSQVK EGEGPEVSPA PSPGRKSQQN TLEELRQPKT VMSLSLPSDG
     TGDSSPGSGK RTPSLSVKAS PRRGSRVSEF LKELSVTAAA AQVGLTPGEK KKQLGADSKL
     HLKQSKRVRD VVWDDQGMTW EVYGASLDPE SLGVAIQNHL QRQIREHEKI VKTQSGQTRR
     SISSDSSSSK KLKGRQHGVL QSMLQNFRRP NCCVRPAPSS VLD
//
ID   LARP4_MOUSE             Reviewed;         719 AA.
AC   Q8BWW4; Q3UR69;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=La-related protein 4;
DE   AltName: Full=La ribonucleoprotein domain family member 4;
GN   Name=Larp4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Embryonic spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-717, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SIMILARITY: Contains 1 HTH La-type RNA-binding domain.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK049756; BAC33905.2; -; mRNA.
DR   EMBL; AK141743; BAE24819.1; -; mRNA.
DR   IPI; IPI00828620; -.
DR   RefSeq; NP_001019697.2; NM_001024526.2.
DR   UniGene; Mm.28811; -.
DR   UniGene; Mm.476896; -.
DR   ProteinModelPortal; Q8BWW4; -.
DR   SMR; Q8BWW4; 109-268.
DR   PhosphoSite; Q8BWW4; -.
DR   PRIDE; Q8BWW4; -.
DR   Ensembl; ENSMUST00000100206; ENSMUSP00000097780; ENSMUSG00000023025.
DR   GeneID; 207214; -.
DR   KEGG; mmu:207214; -.
DR   CTD; 207214; -.
DR   MGI; MGI:2443114; Larp4.
DR   eggNOG; maNOG06226; -.
DR   GeneTree; ENSGT00530000063417; -.
DR   HOGENOM; HBG445519; -.
DR   HOVERGEN; HBG055137; -.
DR   InParanoid; Q8BWW4; -.
DR   OrthoDB; EOG44MXRZ; -.
DR   NextBio; 371897; -.
DR   ArrayExpress; Q8BWW4; -.
DR   Bgee; Q8BWW4; -.
DR   CleanEx; MM_LARP4; -.
DR   Genevestigator; Q8BWW4; -.
DR   GermOnline; ENSMUSG00000023025; Mus musculus.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR006630; Lupus_La_RNA-bd.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF05383; La; 1.
DR   SMART; SM00715; LA; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50961; HTH_LA; 1.
DR   PROSITE; PS50102; RRM; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein; RNA-binding.
FT   CHAIN         1    719       La-related protein 4.
FT                                /FTId=PRO_0000207612.
FT   DOMAIN      109    198       HTH La-type RNA-binding.
FT   DOMAIN      199    277       RRM.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     387    387       Phosphoserine (By similarity).
FT   MOD_RES     578    578       Phosphoserine (By similarity).
FT   MOD_RES     590    590       Phosphothreonine (By similarity).
FT   MOD_RES     592    592       Phosphoserine (By similarity).
FT   MOD_RES     638    638       Phosphoserine (By similarity).
FT   MOD_RES     642    642       Phosphoserine (By similarity).
FT   MOD_RES     644    644       Phosphothreonine (By similarity).
FT   MOD_RES     717    717       Phosphoserine.
SQ   SEQUENCE   719 AA;  79763 MW;  B699A5FC5642023B CRC64;
     MLLFVEVTSK GTGLNPNAKV WQEIPSGNPD GTPVTEPSWH ETAATSGSHP EGHTELSEDM
     CKEYEVMYSP SCETTRNTAD VEESADGMIL GPEDLSYQLY DVSGESSSAI STEDLKECLK
     KQLEFCFSRE NLSKDLYLIS QMDSDQFVPI WTVANMEEIK KLTTNTDLIL EVLRSSPMVQ
     VDEKGEKVRP SHKRCIVILR EIPETTPVEE VKALFKNENC PKVISCEFAH NSNWYITFQS
     DTDAQQAFKY LREEVKTFQG KPIMARIKAI NTFFAKNGYR LMDSSMYTQP IQTPTQYPSP
     VFMQPVYNPQ QYSVYSLVPQ SWSPSPAPYF ETPLAPFPNG SFVDGFSSPG SYKTNAAAMN
     MGRPFPKNRV KPHFRSSSGS EHSTEGSVSL GDGPLSRSSS RIFLSERHNP TVTGQQEQTY
     LPKEAPILQM EQNGDFGRGR RTLFRGRRRR DDDRIPRPQP AATEAKAPTP KFDLLATNFP
     PLPGSSSRVP DELGLENRMS DVVKGVCREK DSEDVRVSCP VPAEDGQTDC TSAPLSISPS
     PPCTAEPPVL STTQQEQDQM EDSAVPKDTL NPVAVPVSSP TATKPSPANT ASPCTSNINP
     PRAVALQEPR KLSYAEVCQK PPKEPSPVLV QPLRELRSNA VSPTRNEENG APEKPVEKPH
     EKPETRASKD HSGFRGNTIP RGAAGKIREQ RRQFSHRATP QGVTRRNGKE QYVPPRSPK
//
ID   NAA25_MOUSE             Reviewed;         972 AA.
AC   Q8BWZ3; A1A4B7; Q3KQI7; Q3TJC6; Q7TMM2;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=N-alpha-acetyltransferase 25, NatB auxiliary subunit;
DE   AltName: Full=Mitochondrial distribution and morphology protein 20;
DE   AltName: Full=N-terminal acetyltransferase B complex subunit MDM20;
DE            Short=NatB complex subunit MDM20;
DE   AltName: Full=N-terminal acetyltransferase B complex subunit NAA25;
GN   Name=Naa25; Synonyms=Mdm20;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow, Embryonic stem cell, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=FVB/N; TISSUE=Brain, Embryo, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Non-catalytic subunit of the NatB complex which
CC       catalyzes acetylation of the N-terminal methionine residues of
CC       peptides beginning with Met-Asp-Glu (By similarity). May play a
CC       role in normal cell-cycle progression (By similarity).
CC   -!- SUBUNIT: Component of the N-terminal acetyltransferase B (NatB)
CC       complex which is composed of NAA20 and NAA25 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BWZ3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BWZ3-2; Sequence=VSP_026631;
CC   -!- SIMILARITY: Belongs to the MDM20/NAA25 family.
CC   -!- SIMILARITY: Contains 4 TPR repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK049325; BAC33684.1; -; mRNA.
DR   EMBL; AK149758; BAE29066.1; -; mRNA.
DR   EMBL; AK167405; BAE39494.1; -; mRNA.
DR   EMBL; AK167491; BAE39569.1; -; mRNA.
DR   EMBL; BC028868; AAH28868.1; -; mRNA.
DR   EMBL; BC055480; AAH55480.1; -; mRNA.
DR   EMBL; BC106182; AAI06183.1; -; mRNA.
DR   EMBL; BC132172; AAI32173.1; -; mRNA.
DR   IPI; IPI00226576; -.
DR   IPI; IPI00853658; -.
DR   RefSeq; NP_766310.2; NM_172722.3.
DR   UniGene; Mm.33919; -.
DR   ProteinModelPortal; Q8BWZ3; -.
DR   SMR; Q8BWZ3; 21-146, 488-531.
DR   PRIDE; Q8BWZ3; -.
DR   Ensembl; ENSMUST00000042163; ENSMUSP00000038977; ENSMUSG00000042719.
DR   GeneID; 231713; -.
DR   KEGG; mmu:231713; -.
DR   UCSC; uc008zjc.1; mouse.
DR   CTD; 231713; -.
DR   MGI; MGI:2442563; Naa25.
DR   InParanoid; Q8BWZ3; -.
DR   OMA; KTELQFS; -.
DR   OrthoDB; EOG45DWNP; -.
DR   PhylomeDB; Q8BWZ3; -.
DR   NextBio; 380719; -.
DR   ArrayExpress; Q8BWZ3; -.
DR   Bgee; Q8BWZ3; -.
DR   CleanEx; MM_C330023M02RIK; -.
DR   Genevestigator; Q8BWZ3; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR019183; N-acetylTrfase_B_cplx_non-cat.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 3.
DR   Pfam; PF09797; NatB_MDM20; 1.
DR   PROSITE; PS50005; TPR; FALSE_NEG.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Phosphoprotein; Repeat; TPR repeat.
FT   CHAIN         1    972       N-alpha-acetyltransferase 25, NatB
FT                                auxiliary subunit.
FT                                /FTId=PRO_0000294338.
FT   REPEAT       11     44       TPR 1.
FT   REPEAT       45     78       TPR 2.
FT   REPEAT       79    112       TPR 3.
FT   REPEAT      114    146       TPR 4.
FT   COMPBIAS    871    877       Poly-Lys.
FT   MOD_RES     691    691       Phosphoserine.
FT   VAR_SEQ       1     48       MATRGHVQDPNDRRLRPIYDYLDNGNNKMAIQQADKLLKKH
FT                                KDLHCAK -> MCRTLTTGASGPFT (in isoform 2).
FT                                /FTId=VSP_026631.
FT   CONFLICT    424    424       L -> I (in Ref. 1; BAE39569/BAE39494).
SQ   SEQUENCE   972 AA;  111708 MW;  1393A5B38DE26D54 CRC64;
     MATRGHVQDP NDRRLRPIYD YLDNGNNKMA IQQADKLLKK HKDLHCAKVL KAIGLQRTGK
     QEEAFTLAQE VAALEPTDDN SLQALTILYR EMHRPELVTK LYEAAVKKVP NSEEYHSHLF
     MAYARVGEYK KMQQAGMALY KIVPKNPYYF WSVMSLIMQS ISARDENLSK TMFLPLAERM
     VEKMVKEDKI EAEAEVELYY MILERLGKYQ EALDVIRGKL GEKLTSEIQS RENKCMAMYK
     KLSKWPECNA LSRRLLLKNS DDWQFYLTYF DSVFRLIEEA WTPPAEGEHS LEGEVHCSAE
     DAVKFIEDRI TEASQSSRHV RGPHLAKLEL IRRLRSQGCN DEYKLGDPEE LMFQYFKKFG
     DKPCCFTDLK VFVDLLPAAQ CTQFINQLLG VVPLSTPTED KLALPADIRG LQQHLCVVQL
     TRLLGLYHSM DKSQKLDVVK ELMLRYQHGL EFGRSCLKTE LQFSDYYCLL AVHVLIDVWR
     EAGEETAVWQ ALTLLEEGLT HSPSNAQFKL LLVRIYCVLG AFEPVVDLYS SLDAKHIQHD
     TIGYLLTRYA ASLGQYAAAS QSCNFALRFF HSNQKDTSEY IIQAYKYGAF EKIPEFIAFR
     NRLNNSLHFA QVRTERMLLD LLLEANISIS LAESIKSMNL RPEEDDVPWE DLRDNRDLDV
     FFSWDPKDRN VSEEHKKLSL EEETMWLRIR SLTLRLISGL PSLTHPVEPK NSEKMSENGV
     SSRIDILRLL LQQLEVAVET GKRFIEKEIQ YPFLGPVPTR MGRFFSSGCC QCQVQSFHLV
     SDMYELDTSG LEGTVDIQER IENSLASLLE LLKGVFSTCK GDLLEVTDGN VKTQPAVLEN
     LVFFVETISV ILWVSSYCES VLRPYKLNIQ KKKKKKKETS IIMPPIFTSF QDYVTGLQTV
     ISNAVDHIKG LEAHLIALRL EELTLEETSI STEERKFSKT VQGKVQSSYL HSLLETGELL
     RKRLETTKKL KI
//
ID   PGAM5_MOUSE             Reviewed;         288 AA.
AC   Q8BX10; B2RSM6; Q3UK19; Q80VY8; Q8BM78; Q9CZU2;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Serine/threonine-protein phosphatase PGAM5, mitochondrial;
DE            EC=3.1.3.16;
DE   AltName: Full=Phosphoglycerate mutase family member 5;
GN   Name=Pgam5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, DBA/2, and NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 7-288 (ISOFORM 1).
RC   TISSUE=Brain, and Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Displays phosphatase activity for serine/threonine
CC       residues, and, dephosphorylates and activates MAP3K5 kinase. Has
CC       apparently no phosphoglycerate mutase activity. May be regulator
CC       of mitochondrial dynamics. Substrate for a KEAP1-dependent
CC       ubiquitin ligase complex. Contributes to the repression of NFE2L2-
CC       dependent gene expression (By similarity).
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- SUBUNIT: Dimer. Forms a ternary complex with NFE2L2 and KEAP1.
CC       Interacts with BCL2L1 and MAP3K5 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion outer membrane.
CC       Membrane; Single-pass membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BX10-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BX10-2; Sequence=VSP_025762;
CC   -!- DOMAIN: According to PubMed:18387606, may contain a non-cleaved N-
CC       terminal mitochondrial targeting sequence that targets PGAM5 to
CC       the cytosolic side of the outer mitochondrial membrane, instead of
CC       a N-terminal transmembrane (By similarity).
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB28067.1; Type=Frameshift; Positions=52, 66;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK012159; BAB28067.1; ALT_FRAME; mRNA.
DR   EMBL; AK034588; BAC28763.1; -; mRNA.
DR   EMBL; AK049246; BAC33634.1; -; mRNA.
DR   EMBL; AK146216; BAE26984.1; -; mRNA.
DR   EMBL; AK169643; BAE41272.1; -; mRNA.
DR   EMBL; BC052179; AAH52179.1; -; mRNA.
DR   EMBL; BC138924; AAI38925.1; -; mRNA.
DR   EMBL; BC138925; AAI38926.1; -; mRNA.
DR   IPI; IPI00226387; -.
DR   IPI; IPI00848970; -.
DR   RefSeq; NP_001157010.1; NM_001163538.1.
DR   RefSeq; NP_082549.2; NM_028273.3.
DR   UniGene; Mm.61682; -.
DR   ProteinModelPortal; Q8BX10; -.
DR   SMR; Q8BX10; 88-288.
DR   PhosphoSite; Q8BX10; -.
DR   PRIDE; Q8BX10; -.
DR   Ensembl; ENSMUST00000059229; ENSMUSP00000057760; ENSMUSG00000029500.
DR   Ensembl; ENSMUST00000112505; ENSMUSP00000108124; ENSMUSG00000029500.
DR   GeneID; 72542; -.
DR   KEGG; mmu:72542; -.
DR   CTD; 72542; -.
DR   MGI; MGI:1919792; Pgam5.
DR   GeneTree; ENSGT00390000004796; -.
DR   HOVERGEN; HBG105576; -.
DR   InParanoid; Q8BX10; -.
DR   OMA; KHLPGVC; -.
DR   OrthoDB; EOG4T4CW2; -.
DR   NextBio; 336451; -.
DR   ArrayExpress; Q8BX10; -.
DR   Bgee; Q8BX10; -.
DR   CleanEx; MM_PGAM5; -.
DR   Genevestigator; Q8BX10; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:EC.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   Pfam; PF00300; PGAM; 1.
DR   SMART; SM00855; PGAM; 1.
DR   PROSITE; PS00175; PG_MUTASE; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Hydrolase; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    288       Serine/threonine-protein phosphatase
FT                                PGAM5, mitochondrial.
FT                                /FTId=PRO_0000288783.
FT   TRANSMEM      7     29       Helical; (Potential).
FT   REGION       76     81       Interaction with KEAP1 (By similarity).
FT   MOD_RES     115    115       N6-acetyllysine (By similarity).
FT   MOD_RES     143    143       N6-acetyllysine (By similarity).
FT   MOD_RES     190    190       N6-acetyllysine (By similarity).
FT   VAR_SEQ     195    195       Missing (in isoform 2).
FT                                /FTId=VSP_025762.
FT   CONFLICT     46     46       A -> V (in Ref. 1; BAE26984).
FT   CONFLICT    102    102       I -> M (in Ref. 1; BAC28763).
FT   CONFLICT    144    144       I -> V (in Ref. 1; BAB28067).
SQ   SEQUENCE   288 AA;  31994 MW;  B704CDF4E640F888 CRC64;
     MAFRQALQLA ACGLAGGSAA VLFSAVAVGK PRGGGDADTR ATEPPAWTGA RAGRGVWDTN
     WDRREPLSLI NLKKRNVESG EDELTSRLDH YKAKATRHIF LIRHSQYHVD GSLEKDRTLT
     PLGREQAELT GLRLASLGLK FNKIVHSSMT RAVETTDIIS KHLPGVSRVS TDLLREGAPI
     EPDPPVSHWK PEAVQYYEDG ARIEAAFRNY IHRADARQEE DSYEIFICHA NVIRYIVCRA
     LQFPPEGWLR LSLNNGSITH LVIRPNGRVA LRTLGDTGFM PPDKITRS
//
ID   UB2CB_MOUSE             Reviewed;         368 AA.
AC   Q8BX13;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2C-binding protein;
DE            EC=6.3.2.-;
DE   AltName: Full=UbcH10-binding protein with a HECT-like domain;
GN   Name=Ube2cbp; Synonyms=H10bh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from
CC       specific E2 ubiquitin-conjugating enzymes, and transfers it to
CC       substrates, generally promoting their degradation by the
CC       proteasome (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with UBE2C/UbcH10 (E2 ubiquitin-conjugating
CC       enzyme) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- DOMAIN: The C-terminal half (AA 167-368) is able to bind cyclin B
CC       and shows a self-ubiquitinylation activity (mono-, poly, or multi-
CC       ubiquitinylation) in a HECT-like sequence dependent manner (By
CC       similarity).
CC   -!- PTM: Ubiquitinated by UBCH10 (E2 ubiquitin-conjugating enzyme) (By
CC       similarity).
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK049229; BAC33623.1; -; mRNA.
DR   EMBL; BC115686; AAI15687.1; -; mRNA.
DR   EMBL; BC115687; AAI15688.1; -; mRNA.
DR   IPI; IPI00312263; -.
DR   RefSeq; NP_081670.1; NM_027394.2.
DR   UniGene; Mm.53469; -.
DR   PRIDE; Q8BX13; -.
DR   Ensembl; ENSMUST00000034986; ENSMUSP00000034986; ENSMUSG00000032415.
DR   GeneID; 70348; -.
DR   KEGG; mmu:70348; -.
DR   NMPDR; fig|10090.3.peg.20596; -.
DR   UCSC; uc009qxc.1; mouse.
DR   CTD; 70348; -.
DR   MGI; MGI:1917598; Ube2cbp.
DR   HOVERGEN; HBG056762; -.
DR   OMA; FANKPLH; -.
DR   OrthoDB; EOG4T4CVH; -.
DR   PhylomeDB; Q8BX13; -.
DR   NextBio; 331410; -.
DR   ArrayExpress; Q8BX13; -.
DR   Bgee; Q8BX13; -.
DR   CleanEx; MM_UBE2CBP; -.
DR   Genevestigator; Q8BX13; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR019193; UBQ-conj_enz_E2-bd_prot.
DR   Pfam; PF09814; DUF2351; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Ligase; Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN         1    368       Ubiquitin-conjugating enzyme E2C-binding
FT                                protein.
FT                                /FTId=PRO_0000311191.
FT   REGION      214    236       Interaction with UBE2C (By similarity).
FT   REGION      332    368       HECT-like (By similarity).
SQ   SEQUENCE   368 AA;  40753 MW;  5AE96DD625A7277D CRC64;
     MAVAAAETRV FLEVRRRLQS ALLILGGPDE GGMHLDISIT PTSLLVRTPD GCTEIRLPAG
     VRLVPSSCGG LQYISGDGLH LRLRVQAESS PQPISVFNQS LQAQECCTFY CQSCGEVTIK
     DRKLLRVLPL PSENWSALVG EWCCHPDPFA NRPLHPREND CFIGDSFFLV NLKSDLEQEP
     KANTKVICKR CKVTLGETMS SETTKFYMTE VIIRPSEGSF PNIPRSQFLQ SIIAQCLVEL
     SSARSTFRFT IQGQDGKVYI LLWVLNSDSL VIEPLRSSSC SRKFPLLESS LEAGSGSAWN
     AIKVLYQPCI KSRNKELASS WEGDISVHPL TLPSATCLEL LLILSRNNAS LPLSLRQMNS
     FQVAFLKM
//
ID   TR19L_MOUSE             Reviewed;         436 AA.
AC   Q8BX43; Q8BTV0;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Tumor necrosis factor receptor superfamily member 19L;
DE   Flags: Precursor;
GN   Name=Relt; Synonyms=Tnfrsf19l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Mediates activation of NF-kappa-B. May play a role in T-
CC       cell activation (By similarity).
CC   -!- SUBUNIT: Associates with TRAF1. Interacts with RELL1, RELL2 and
CC       OXSR1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the RELT family.
CC   -!- SIMILARITY: Contains 1 TNFR-Cys repeat.
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DR   EMBL; AK049073; BAC33534.1; -; mRNA.
DR   EMBL; AK088621; BAC40459.1; -; mRNA.
DR   IPI; IPI00310661; -.
DR   RefSeq; NP_796047.2; NM_177073.6.
DR   UniGene; Mm.40336; -.
DR   ProteinModelPortal; Q8BX43; -.
DR   SMR; Q8BX43; 33-118.
DR   STRING; Q8BX43; -.
DR   PhosphoSite; Q8BX43; -.
DR   PRIDE; Q8BX43; -.
DR   Ensembl; ENSMUST00000008462; ENSMUSP00000008462; ENSMUSG00000008318.
DR   GeneID; 320100; -.
DR   KEGG; mmu:320100; -.
DR   CTD; 320100; -.
DR   MGI; MGI:2443373; Relt.
DR   GeneTree; ENSGT00530000063385; -.
DR   HOGENOM; HBG444824; -.
DR   HOVERGEN; HBG062274; -.
DR   InParanoid; Q8BX43; -.
DR   OrthoDB; EOG4Z8XWH; -.
DR   ArrayExpress; Q8BX43; -.
DR   Bgee; Q8BX43; -.
DR   CleanEx; MM_RELT; -.
DR   Genevestigator; Q8BX43; -.
DR   GermOnline; ENSMUSG00000008318; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR022248; TNF_rcpt_RELT.
DR   InterPro; IPR022333; TNFR_19-like.
DR   InterPro; IPR001368; TNFR_Cys_rich_reg.
DR   Pfam; PF12606; RELT; 1.
DR   PRINTS; PR01970; TNFACTORR19L.
DR   SMART; SM00208; TNFR; 1.
DR   PROSITE; PS00652; TNFR_NGFR_1; FALSE_NEG.
DR   PROSITE; PS50050; TNFR_NGFR_2; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cytoplasm; Disulfide bond; Glycoprotein; Membrane;
KW   Receptor; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     31       By similarity.
FT   CHAIN        32    436       Tumor necrosis factor receptor
FT                                superfamily member 19L.
FT                                /FTId=PRO_0000034601.
FT   TOPO_DOM     32    169       Extracellular (Potential).
FT   TRANSMEM    170    190       Helical; (Potential).
FT   TOPO_DOM    191    436       Cytoplasmic (Potential).
FT   REPEAT       57     97       TNFR-Cys.
FT   CARBOHYD    156    156       N-linked (GlcNAc...) (Potential).
FT   DISULFID     58     72       By similarity.
FT   DISULFID     78     97       By similarity.
FT   CONFLICT     39     39       G -> C (in Ref. 1; BAC40459).
SQ   SEQUENCE   436 AA;  46472 MW;  1F96C5E021945DF9 CRC64;
     MSLQGLMMKR TLLCWPLSCL FVLLPWPLAT PTPITPWLGP PGKEPDPDPG QGTLCRTCPP
     GTFSASWNSY PCQPHYRCSL QKRLEAQAGT ATHDTMCGDC QHGWFGPQGV PHVPCQPCSK
     APPSTGGCDE SGRRGRRGVE VAAGTSSNGE PRQPGNGTRA GGPEETAAQY AVIAIVPVFC
     LMGLLGILVC NLLKRKGYHC TAQKEVGPSP GGGGSGINPA YRTEDANEDT IGVLVRLITE
     KKENAAALEE LLKEYHSKQL VQTSHRPVPR LLPASPSIPH ICPHHHHLHT VQGLASLSGP
     CCSRCSQKWP EVLLSPEAAA ATTPAPTLLP TASRAPKASA KPGRQGEITI LSVGRFRVAR
     IPEQRTSSLL SEVKTITEAG PSEGDLPDSP QPGLPPEQRA LLGSGGSHTK WLKPPAENKA
     EENRYVVRLS ESNLVI
//
ID   VP13C_MOUSE             Reviewed;        3748 AA.
AC   Q8BX70; Q3V3W5; Q6ZPE1; Q8BLB1; Q8BQI7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Vacuolar protein sorting-associated protein 13C;
GN   Name=Vps13c; Synonyms=Kiaa3021;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-924 (ISOFORM 3),
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1444-2010, AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 3040-3748 (ISOFORMS 1/3).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Corpora quadrigemina, Embryo, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2868-3623 (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1435, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1968 AND SER-1974, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BX70-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BX70-2; Sequence=VSP_052247, VSP_052248;
CC       Name=3;
CC         IsoId=Q8BX70-3; Sequence=VSP_052246;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the VPS13 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC33451.1; Type=Frameshift; Positions=763;
CC       Sequence=BAC33809.1; Type=Erroneous initiation;
CC       Sequence=BAE20465.1; Type=Erroneous initiation;
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DR   EMBL; AC156799; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK030931; BAE20465.1; ALT_INIT; mRNA.
DR   EMBL; AK045749; BAC32479.2; -; mRNA.
DR   EMBL; AK048766; BAC33451.1; ALT_FRAME; mRNA.
DR   EMBL; AK049557; BAC33809.1; ALT_INIT; mRNA.
DR   EMBL; AK129486; BAC98296.1; -; mRNA.
DR   IPI; IPI00551411; -.
DR   IPI; IPI00661059; -.
DR   IPI; IPI00761666; -.
DR   RefSeq; NP_796158.2; NM_177184.3.
DR   UniGene; Mm.241454; -.
DR   PhosphoSite; Q8BX70; -.
DR   PRIDE; Q8BX70; -.
DR   Ensembl; ENSMUST00000057972; ENSMUSP00000062856; ENSMUSG00000035284.
DR   Ensembl; ENSMUST00000077879; ENSMUSP00000077040; ENSMUSG00000035284.
DR   Ensembl; ENSMUST00000098601; ENSMUSP00000096201; ENSMUSG00000035284.
DR   GeneID; 320528; -.
DR   KEGG; mmu:320528; -.
DR   UCSC; uc009qms.1; mouse.
DR   CTD; 320528; -.
DR   MGI; MGI:2444207; Vps13c.
DR   GeneTree; ENSGT00410000025397; -.
DR   HOGENOM; HBG402793; -.
DR   HOVERGEN; HBG079736; -.
DR   InParanoid; Q8BX70; -.
DR   OMA; QPCSLFM; -.
DR   OrthoDB; EOG4NKBTN; -.
DR   PhylomeDB; Q8BX70; -.
DR   NextBio; 396907; -.
DR   ArrayExpress; Q8BX70; -.
DR   Bgee; Q8BX70; -.
DR   CleanEx; MM_VPS13C; -.
DR   Genevestigator; Q8BX70; -.
DR   GermOnline; ENSMUSG00000035284; Mus musculus.
DR   GO; GO:0008104; P:protein localization; IEA:InterPro.
DR   InterPro; IPR015412; Autophagy-rel_C.
DR   InterPro; IPR009543; VPSAP.
DR   Pfam; PF09333; ATG_C; 1.
DR   Pfam; PF06650; DUF1162; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Isopeptide bond; Phosphoprotein;
KW   Ubl conjugation.
FT   CHAIN         1   3748       Vacuolar protein sorting-associated
FT                                protein 13C.
FT                                /FTId=PRO_0000262950.
FT   COMPBIAS    145    179       Lys-rich.
FT   MOD_RES     188    188       Phosphothreonine (By similarity).
FT   MOD_RES     613    613       Phosphothreonine (By similarity).
FT   MOD_RES     618    618       Phosphoserine (By similarity).
FT   MOD_RES     623    623       Phosphothreonine (By similarity).
FT   MOD_RES     736    736       Phosphoserine (By similarity).
FT   MOD_RES    1435   1435       Phosphothreonine.
FT   MOD_RES    1968   1968       Phosphothreonine.
FT   MOD_RES    1974   1974       Phosphoserine.
FT   MOD_RES    3533   3533       N6-acetyllysine (By similarity).
FT   CROSSLNK   2352   2352       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   VAR_SEQ     763    802       Missing (in isoform 3).
FT                                /FTId=VSP_052246.
FT   VAR_SEQ    3617   3623       NHIKKLE -> QEMGTQE (in isoform 2).
FT                                /FTId=VSP_052247.
FT   VAR_SEQ    3624   3748       Missing (in isoform 2).
FT                                /FTId=VSP_052248.
FT   CONFLICT   1759   1759       A -> S (in Ref. 2; BAC33809).
FT   CONFLICT   2868   2868       T -> P (in Ref. 3; BAC98296).
FT   CONFLICT   2916   2916       R -> G (in Ref. 3; BAC98296).
SQ   SEQUENCE   3748 AA;  420089 MW;  57F0943B89B7A087 CRC64;
     MVLESVVADL LNRFLGDYVE NLNKSQLKLG IWGGNVALDN LQIKENALSE LDVPFKVKAG
     QIDKLTLKIP WKNLYGEAVV ATLEGLYLLV VPGASIKYDA EKEEKSLQDI KQKELCRIEE
     ALQKAAEKGA HSGEFMYGLE NLLYKDVKPG RKRKKHKKHF KKRFKGLDRS KDKPKEAKKD
     TFLEKLATQV IKNVQVKITD IHIKYEDDIT DPERPLSFGV TLREFSLLTT NEHWTPCILN
     EAEKIIYKLV KLDSLSAYWN VGCCMSYRGS REHILEQLKR EILTSTNIPP DHQYIFQPIS
     ASAKLYMNPG AESELKTPKL DGNVEVQNIA IELTKPQYLS MIDFLESLDY MVRNAPYRKY
     KPCLPLHTNC RQWWKYAIDS VLEVHIRRYT QPWSWSNIKN HRQLLKSYKM AYKTKLTQAK
     VSEEIQKQIQ DLEKSLDVFN IILVRQQAQV EVIHSGQKLR KKSAEAGEKR GWFSGFWGKK
     ESKKRDEESS VPETIDDLMT PEEKDKLFTA IGYSENAYNL ALPKQYVAHI LTLKLVSTSI
     IIRENRNVPE ILRVQIIGLG TQVSQRPGAQ ALKIEAKLEH WYVTGLRQQD IVPSLVASIG
     DTTSSLLKIE FETNPENSPA DQTLIVQSQP VEVIYDAKTI NAVVEFFQSN KGLDLEQITS
     ATLMKLEEIK ERTATGLTHI IETRKVLDLR INLKPSYLII PQTGFHHEKS NLLILDFGTF
     QLNSKDQGAQ KTANASLEEI IDKAYDKFDV EIRSVQLLFA KAEENWKKCR FQHPSTMHIL
     QPMDIHVELA KAMVEKDVRM AKFKVSGGLP LMHVRISDQK IKDALCLINS IPLPQKSSTP
     SPERQVASIP VLSGGTKALL GTSLLLDGVE SESDEEFFDA EDGDSQAART VKASELKKAA
     EVPNEELVSL LLKFEIKEVV LELTKQQKEE ETILVFNVTQ LGTEATMRTF DLTAVSYLRK
     ISLDYHDIKG SRKKPIHLIS SSDRPGLDLL KVEYIKVDRN GPSFQTTFEK TEQTVKVAFS
     SLNLLLQTQA LLSSLNYLTT VIPSDSQNTG VAKEVQAMPE KQKNSPLQKV MVPSRDSDVI
     GFRLFAKLNA FCVTVCDEKS NIAEIKIQGL DSSLSLQSKK QSLFARLENI IVTDVDPKTI
     HKKAVSIVGN EVFRFNLDLY PDATEGDSYT DMSTVDGVVA LHVGCIQIVY LHKFLMSLLS
     FLNNFQVAKE ALSAATAQAA EKAATSVKDL AQRSFRVSVD IDLKAPVIVI PQSSLSTNAV
     VVDLGLIRVH NRFSLVSGED TANPPVIDKM EVQLTKLKLS RTAIQPGTSH PDIQLLHPIN
     LEFFVSRNLA ANWYHKVPVV EIKGRLDSMN VSLNQEDLNL LFRILAENLG EATEDLDKGK
     PRIQERGETK ACREVSTPQD VHTTQGVPAA RVEETRPVDI INVLLNFEIK EVVVTLMKKA
     ERKGSPFHEL KILHLGMEAK VKAHDMTAAA YLRNISMRCF HFPDSKGEPL RIVNTSDVSD
     GILLKLLFIK ADSDGPDFKT IHDNTKQKLK VSFSSLDLVL HLEALLSLMD FLSSAIPSSD
     SSSSEKEPEL KPLVGESRSL AIRAVPSSYE GDAFDLKITA ELNAFNIFIC DQKSNIAEIK
     IHGMDASISV KPKQTDVFAR LKNIIVMNVD SLSIHKKAVS ILGDEVFRFQ MSLYPDATEG
     ENYGDMSKVD GRLSLKVGCI QIVYVHKFFM SLLSFLNNFQ AAKEALSTAT VQAAERAASS
     VKDLAQKSFR LLMDIDLKAP VITIPQSSVS PNVVIADLGL IRVENKFSLV SVEQLALPPV
     ADEMSIQLTQ LKLARTVLQA DSPQHDVEIL KPVNMLLCIQ RNLSAAWYTQ IPGMEIKGEL
     KPMQVALSQD DLTVLMKILL ENLGEASSQP SPTQYAQEAA RVKRDTRSGP DYLKEQELAD
     PKPPGDQTVT LQFDFHFDSL SIILYNSDSS QEPRLSFHND SFRLGELTLH LMASAGKMFK
     DGSMNVSLKL KTCTLDDLRE GIERATSRMI DKKNDQDNNS SMIDISYSQD KNGSQVDAVL
     DKLYVCASVE FLMTVADFFI KAMPQSPENI AKEIQIPSRQ TAAGRVKMEK DDSVRPNMTL
     KAMITDPEVV FVASLTKADA PALTASFQCN LSLSTSKLEQ MMEASVRDLK VLACPFLRER
     RGKSITTVLQ PCSLFMEKCT WASGKQNINI VVKEFVIKIS PIILNTVMTI MAAMSPKTKE
     DEWKDTPKET DNLWAVKSIT DYNSWFLGVD MATEVTENFR DSEHPSIEEN CVVAVESVQV
     TLECGLGHRT VPLLLAESKF SGNIKNWTSL MAAAADMTLE VHYYNETHAV WEPLIERVEG
     NKPWSLKLNV KKNPIQDKSL MPGDDFIPEP QTAVHISSGA TMNITISKSC LNVFSNLAKG
     FSEGAASTFD YSLKDRAPFT VKNALGVPMK VQPNRNLKVM GSPEKSDIYD VGAGQHLELD
     YASLEPSRQG KLSILSRQES SLFTLTFVPY GYTEVASVPV ARPGRRLYNV RNPSASHSDS
     VLVQIDATEG NKVVTLRSPL QIKNHFSIAF IIYKFVKNVK LLERIGIARP EEEFHVPLDS
     YRCQLYVQPA GGLEQQYTHS STYISWKEEL HRSREVRCML QCPAVEVSFL PLIVNTVALP
     DELSYIGAHG EDWDPAYVIH LYPPLTLRNL LPYSLRYLLE GTAETHELAE GSSADVLHSR
     ISGEIIELVL VKYLGKNWNG HFRICDTLPE FFLVCFSSDT AEVMTVDLSV HVRRIGCRME
     LSVFSPYWLI NKTSRVLQYR SEEIHVKHPA DFRDIILFSF KKKNIFSKNK VQLKISTSAW
     SNGFSLDTVG SYGCVKCPAT NMEYLVGVSI KMSSFNLSRV VTLTPFCTVA NKSSLDLEVG
     EIASDGSIPT NKWHYVASSE CIPFWPENLS GKLCVRVVGY EGSSKPFFYN RQDNGTLLSL
     EDLNGGILVD INTAEHSTVI TFSDYHEGSA PALIMNHTQW DVLTYKQSGS QEELVLLPGE
     TRLFAWADPT GIRKLTWNYA ANFGEHDLLK DECGQFPYDA NIQIHWVSFL DGRQRVLLFT
     DDVALVSKAL QAEEMEQADH EVALSLHSLG LSLVNNENKQ EVSYVGITSS GVVWEMKPKQ
     KWKPFSQKQI MSLEQAYSKR LASQDRGWVK LDSNFEVNFD KVPMEMRLPI RCPIKRDFLS
     GIQVEFKQSP HQRSLRARLY WLQVDNQLPG TMFPVVFHPV APPKSIALDS EPKPFIDVSV
     ITRFNEYSKV LQFKYFMVLI QEMALKVDQG FLGAVISLFT PTTDPEAERK RTKLIQQDID
     ALNTELMESS MTDMSILSFF EHFHISPVKL HLSLSLGSGG EESDKEKQEM IAIHSVNLLL
     KSIGATLTDV DDLIFKLAYY EIRYQFYKRD QLMWSVVRHY SEQFLKQMYV LVLGLDVLGN
     PFGLIRGLSE GVEALFYEPF QGAVQGPEEF AEGLVIGVRS LVGHTVGGAA GVVSRITGSV
     GKGLAAITMD KEYQQKRREE MGRQPKDFGD SLARGGKGFL RGVVGGVTGI ITKPVEGAKK
     EGAAGFFKGI GKGLVGAVAR PTGGIIDMAS STFQGIQRVA ESTEEVSSLR PPRLIHEDGI
     IRPYDRQESE GSDLLENHIK KLEGEAYQFH CAVPGNKRAV LMITNRRALF IKEVEILGHM
     SVDWQCLFED FVCPPEVSEN LLKISVKEQG LFHKKDSANI GHLRKIYLKD PITAKRAFDA
     IESAQSARQQ QKLMRQSSVK LLRPQGPS
//
ID   FND3A_MOUSE             Reviewed;        1198 AA.
AC   Q8BX90; Q2VEY7; Q3T9K5; Q6ZQ15; Q811D3; Q8BME4; Q8BTM3;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 3.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Fibronectin type-III domain-containing protein 3A;
GN   Name=Fndc3a; Synonyms=D14Ertd453e, Fndc3, Kiaa0970;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6;
RX   PubMed=16904100; DOI=10.1016/j.ydbio.2006.06.054;
RA   Obholz K.L., Akopyan A., Waymire K.G., MacGregor G.R.;
RT   "FNDC3A is required for adhesion between spermatids and Sertoli
RT   cells.";
RL   Dev. Biol. 298:498-513(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1053.
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Fetal head, Spleen, and Wolffian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 577-1198.
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 638-1198.
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Mediates spermatid-Sertoli adhesion during
CC       spermatogenesis.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass
CC       membrane protein (Potential).
CC   -!- TISSUE SPECIFICITY: Testis. Localizes to the acrosome of
CC       spermatids, as well as to Leydig cells. Can be detected on the
CC       acrosome beginning at steps 2-3 and continuing until step 12 of
CC       spermiogenesis.
CC   -!- SIMILARITY: Belongs to the FNDC3 family.
CC   -!- SIMILARITY: Contains 9 fibronectin type-III domains.
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DR   EMBL; DQ192036; ABA82149.1; -; mRNA.
DR   EMBL; AK032733; BAC28002.2; -; mRNA.
DR   EMBL; AK048586; BAC33381.1; -; mRNA.
DR   EMBL; AK172458; BAE43015.1; -; mRNA.
DR   EMBL; AK129250; BAC98060.1; -; mRNA.
DR   EMBL; BC047066; AAH47066.1; -; mRNA.
DR   IPI; IPI00356888; -.
DR   RefSeq; NP_997519.2; NM_207636.2.
DR   UniGene; Mm.205421; -.
DR   UniGene; Mm.413549; -.
DR   UniGene; Mm.450820; -.
DR   ProteinModelPortal; Q8BX90; -.
DR   SMR; Q8BX90; 256-1146.
DR   STRING; Q8BX90; -.
DR   PhosphoSite; Q8BX90; -.
DR   PRIDE; Q8BX90; -.
DR   Ensembl; ENSMUST00000089017; ENSMUSP00000086411; ENSMUSG00000033487.
DR   GeneID; 319448; -.
DR   KEGG; mmu:319448; -.
DR   UCSC; uc007upf.1; mouse.
DR   CTD; 319448; -.
DR   MGI; MGI:1196463; Fndc3a.
DR   eggNOG; roNOG12043; -.
DR   HOVERGEN; HBG100680; -.
DR   InParanoid; Q8BX90; -.
DR   OMA; CDHGSEI; -.
DR   OrthoDB; EOG4K3KVG; -.
DR   NextBio; 394750; -.
DR   ArrayExpress; Q8BX90; -.
DR   Bgee; Q8BX90; -.
DR   CleanEx; MM_FNDC3A; -.
DR   Genevestigator; Q8BX90; -.
DR   GermOnline; ENSMUSG00000033487; Mus musculus.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0012506; C:vesicle membrane; IDA:MGI.
DR   GO; GO:0042598; C:vesicular fraction; IDA:MGI.
DR   GO; GO:0016337; P:cell-cell adhesion; IMP:MGI.
DR   GO; GO:0009566; P:fertilization; IMP:MGI.
DR   GO; GO:0060009; P:Sertoli cell development; IMP:MGI.
DR   GO; GO:0007286; P:spermatid development; IMP:MGI.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 9.
DR   Pfam; PF00041; fn3; 8.
DR   SMART; SM00060; FN3; 9.
DR   SUPFAM; SSF49265; FN_III-like; 9.
DR   PROSITE; PS50853; FN3; 9.
PE   1: Evidence at protein level;
KW   Acetylation; Golgi apparatus; Membrane; Phosphoprotein; Repeat;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1   1198       Fibronectin type-III domain-containing
FT                                protein 3A.
FT                                /FTId=PRO_0000087322.
FT   TRANSMEM   1177   1197       Helical; (Potential).
FT   DOMAIN      265    365       Fibronectin type-III 1.
FT   DOMAIN      371    462       Fibronectin type-III 2.
FT   DOMAIN      467    558       Fibronectin type-III 3.
FT   DOMAIN      564    657       Fibronectin type-III 4.
FT   DOMAIN      661    754       Fibronectin type-III 5.
FT   DOMAIN      758    848       Fibronectin type-III 6.
FT   DOMAIN      849    947       Fibronectin type-III 7.
FT   DOMAIN      951   1042       Fibronectin type-III 8.
FT   DOMAIN     1047   1143       Fibronectin type-III 9.
FT   COMPBIAS     68    133       Pro-rich.
FT   MOD_RES     203    203       Phosphoserine (By similarity).
FT   MOD_RES     207    207       Phosphoserine.
FT   MOD_RES     213    213       Phosphoserine (By similarity).
FT   MOD_RES     259    259       Phosphothreonine (By similarity).
FT   MOD_RES     384    384       N6-acetyllysine (By similarity).
FT   CONFLICT    249    249       D -> E (in Ref. 2; BAE43015).
FT   CONFLICT    620    620       T -> A (in Ref. 2; BAC28002).
FT   CONFLICT    788    788       D -> G (in Ref. 2; BAC33381).
FT   CONFLICT   1165   1165       R -> Q (in Ref. 4; AAH47066).
SQ   SEQUENCE   1198 AA;  131958 MW;  700E545ED3D4A8F3 CRC64;
     MAEHPPLLDT AQILSSDISL LSAPIVSADG TQQVILVQVN PGEAFTIRRE DGQFQCITGP
     AQVPMMSPNG SVPPIYVPPG YAPQVIEDNG VRRVVVVPQS PEFHPGGHTV IHRSPHPPLP
     GFIPVPTMMP PPPRHMYSPV TGAGDMATQY MPQYQSSQVY ADVDAHSTHG RSNFRDERSS
     KTYERLQKKL KDRQGTQKDK MSSPPPSPQK CPSPISEHNG LIKGQNASGG NTGSARNRSG
     RGRSCTQVDP EMEEKDEETK AFEAFLSNIV KPVASDIQAR TVLLTWSPPS SFINGEVNET
     AVPELFNYEV LVSSTGKEGK YRSVYIGEET SVTLNDLKPA TDYHAKVQAE SNSIKGIPSE
     AESFTTLSCE PDPPNAPRIA NRTKNSLTLQ WKAPSDNGSK IQSFILEWDE GKGNGEFCQC
     YMGSQKQFKI TKLSPAMGCK FRLSAKNDYG VSDFSEEVLY YTSGCAPSVP ASPVLTKAGV
     TWLSLQWTKP SGTPSDEGIS YILEMEEETS GYGFKPKYDG EDLAYTVKNL RRSTKYKFKV
     IAYNSEGKSN PSEVVEFSTC PDKPGVPVKP SVKGKIHSHG FKITWDPPKD NGGAPINKYV
     VEMAEGSNGN KWDMIYSGTT REHLCDRLTP GCYYRLRVYC ISDGGQSAVS ESLLVQTPAV
     PPGPCLPPRL QGRPKAKEIQ LRWGPPQVDG GSPISCYAVE MTPADKDEPR DVYQGSEVEC
     TVGSLLPGKT YSFRLRAANR IGFGPFSEKY DITTAPGPPD QCRPPQVTCR SATCAQVNWE
     IPLSNGTDVT EYRLEWGGVE GSMQMCYCGP GLSCELKGLS PATTYYCRVQ AMSVVGAGPF
     SEVVACVTPP SVPAIVTCLQ EISDDDIEYP HYSPSTCLAI SWKEPYDHGS EILAYSIDLG
     DKQPLTVGKM TSYIIDSLQP DTTYRIRIQA LNSLGAGPFS HTIKLKTKPL PPDPPRLECV
     AFNHQNLKLK WGEGTPKTLS TDAVQYHLQM EDRNGRFVSL YRGPCHTYKV QRLSESTSYK
     FCIQACNEAG EGPLSQEYVF TTPKSLPAAL KAPKIEKIND HICEITWEYL QPMKGDPVIY
     NLQVMVGKDS EFKQIYKGPD TSFRYSSLQL NCEYRFRVCA IRQCQDPTGH QDLVGPYSTT
     VFFISQRTEP PASSNKDSVD SARTRRTLSD EQCAAVILVV FAFFSILIAF IIQYFVIK
//
ID   PHLP2_MOUSE             Reviewed;        1320 AA.
AC   Q8BXA7; Q8BX96;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=PH domain leucine-rich repeat-containing protein phosphatase 2;
DE            EC=3.1.3.16;
DE   AltName: Full=PH domain leucine-rich repeat-containing protein phosphatase-like;
DE            Short=PHLPP-like;
GN   Name=Phlpp2; Synonyms=Phlppl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1259.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Protein phosphatase that mediates dephosphorylation of
CC       'Ser-473' of AKT1, 'Ser-660' of PRKCB and 'Ser-657' of PRKCA. AKT1
CC       regulates the balance between cell survival and apoptosis through
CC       a cascade that primarily alters the function of transcription
CC       factors that regulate pro- and antiapoptotic genes.
CC       Dephosphorylation of 'Ser-473' of AKT1 triggers apoptosis and
CC       decreases cell proliferation. Also controls the phosphorylation of
CC       AKT3. Dephosphorylation of PRKCA and PRKCB leads to their
CC       destabilization and degradation. Inhibits cancer cell
CC       proliferation and may act as a tumor suppressor (By similarity).
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- COFACTOR: Binds 2 manganese ions per subunit (By similarity).
CC   -!- SUBUNIT: Interacts with AKT1, AKT3 and PRKCB (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC       protein. Nucleus (By similarity).
CC   -!- SIMILARITY: Contains 21 LRR (leucine-rich) repeats.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 PP2C-like domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC33347.2; Type=Erroneous initiation;
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CC   -----------------------------------------------------------------------
DR   EMBL; AC122807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK048260; BAC33288.1; -; mRNA.
DR   EMBL; AK048472; BAC33347.2; ALT_INIT; mRNA.
DR   IPI; IPI00890064; -.
DR   RefSeq; NP_001116066.2; NM_001122594.2.
DR   UniGene; Mm.23494; -.
DR   ProteinModelPortal; Q8BXA7; -.
DR   SMR; Q8BXA7; 233-772, 780-1031.
DR   STRING; Q8BXA7; -.
DR   PRIDE; Q8BXA7; -.
DR   Ensembl; ENSMUST00000034175; ENSMUSP00000034175; ENSMUSG00000031732.
DR   GeneID; 244650; -.
DR   KEGG; mmu:244650; -.
DR   CTD; 244650; -.
DR   MGI; MGI:2444928; Phlpp2.
DR   GeneTree; ENSGT00440000037833; -.
DR   InParanoid; Q8BXA7; -.
DR   OrthoDB; EOG48PMJB; -.
DR   BRENDA; 3.1.3.16; 244.
DR   ArrayExpress; Q8BXA7; -.
DR   Bgee; Q8BXA7; -.
DR   Genevestigator; Q8BXA7; -.
DR   GermOnline; ENSMUSG00000031732; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001932; PP2C-like.
DR   InterPro; IPR014045; PP2C_N.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:3.60.40.10; PP2C-related; 1.
DR   Pfam; PF00560; LRR_1; 5.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00369; LRR_TYP; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-related; 1.
DR   PROSITE; PS51450; LRR; 17.
DR   PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Leucine-rich repeat; Manganese; Membrane;
KW   Metal-binding; Nucleus; Protein phosphatase; Repeat; Tumor suppressor.
FT   CHAIN         1   1320       PH domain leucine-rich repeat-containing
FT                                protein phosphatase 2.
FT                                /FTId=PRO_0000057785.
FT   DOMAIN      147    245       PH.
FT   REPEAT      246    268       LRR 1.
FT   REPEAT      270    291       LRR 2.
FT   REPEAT      295    318       LRR 3.
FT   REPEAT      319    341       LRR 4.
FT   REPEAT      342    364       LRR 5.
FT   REPEAT      366    387       LRR 6.
FT   REPEAT      389    410       LRR 7.
FT   REPEAT      411    434       LRR 8.
FT   REPEAT      435    456       LRR 9.
FT   REPEAT      457    479       LRR 10.
FT   REPEAT      497    521       LRR 11.
FT   REPEAT      522    544       LRR 12.
FT   REPEAT      546    566       LRR 13.
FT   REPEAT      567    589       LRR 14.
FT   REPEAT      591    613       LRR 15.
FT   REPEAT      616    639       LRR 16.
FT   REPEAT      640    663       LRR 17.
FT   REPEAT      664    687       LRR 18.
FT   REPEAT      689    709       LRR 19.
FT   REPEAT      710    734       LRR 20.
FT   REPEAT      756    771       LRR 21.
FT   DOMAIN      772   1028       PP2C-like.
FT   COMPBIAS     40     47       Poly-Thr.
FT   COMPBIAS     48     57       Poly-Ser.
FT   COMPBIAS   1068   1071       Poly-Ser.
FT   METAL       817    817       Manganese 1 (By similarity).
FT   METAL       817    817       Manganese 2 (By similarity).
FT   METAL       818    818       Manganese 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       982    982       Manganese 2 (By similarity).
FT   METAL      1021   1021       Manganese 2 (By similarity).
FT   CONFLICT     67     67       Q -> E (in Ref. 2; BAC33347).
SQ   SEQUENCE   1320 AA;  145946 MW;  AF1C22B064E347A7 CRC64;
     MKHNGSRTCL NRRSRFGSRE RDWLREDVKR GCVYLYGADT TTATTTTSSS SSSSSSSDLH
     LVLCTVQTPA SEICAGEGRE SLYLQLHGDL VRRLEPSERP LQIVYDYLSR LGFEDPVRIQ
     EEATNPDLSC MIRFYGEKPC QMDHLDRILL SGIYNVRKGK TQLHKWAERL VVLCGTCLIV
     SSVKDCQTGK MHILPLVGGK IEEVKRRQHS LAFSSAGAQA QTYHVSFETL AEYQRWQRQA
     SKVVSQRMST VDLSCYSLEE VPEHLFYSQD ITYLNLRHNF MQLERPGGLD TLHKFSQLKG
     LNLSHNKLGL FPVLLCEIST LTELSLSCNG FHDLPSQIGK LLNLQTLSLD GNGLTALPDE
     LGNLRQLTSL GISFNDFRHI PEVLEKLTML DKVAMAGNRL EVLNLGALTR MSQVKHVDLR
     MNHLKTVITE NMEGNKHITH MDLRDNQLTD LDLSSLCSLE QLHCERNQLR ELTLSGFSLR
     TLYASWNRLT AVNVYPVPSL LTSLELSQNL LECVPDWACE AKKLEILDIS HNLLTEVPMR
     ILSSLSLRKL MVGHNHIHVL PALVEHIPLE VLDIQHNTLS RLPDTLFSKA LNLRYLNASA
     NSLESLPSAC AGEESLSVLQ LLYLTSNLLT DQCIPVLVGH PHLRVLHLAN NQLQTFPASK
     LNKLEQLEEL NLSGNKLTAI PTTIANCKRL HTLVAHANNI SIFPEILQLP QIQFVDLSCN
     DLTEILIPEA LPATLQDLDL TGNTNLVLEH KTLDMFSHIT ALKIDQKPLP ATDSAVTSTF
     WSHGLAEMAG QRNKLCVSAL AMDNFAEGVG AVYGMFDGDR NEELPRLLQC TMADVLLEEV
     QHSTNDTVFM TNTFLVSHRK LGMAGQKLGS SALLCYIRPD TADPTSSFSL TVANVGMCQA
     VLCRGGKPVP LSKVFSLEHD PEEAQRVKDQ KAIITEDNKV NGVTCCTRLL GCTYLYPWIL
     PKPHIASTPL TIQDELLILG NKALWEHLSY LEAVNAVRHV QDPLAAAKKL CTLAQSYGCQ
     DNVGAMVVYL NIGEEGCTCE MNGLTLPGPV GFASTAALKD TPKPTTPSSS SGIASEFSSE
     MSTSEVSSEV GSTASDEHNT VGLEASLLPR PERRCSLHPA SSAGVFQRQP SCATFSSNQS
     DNGLDSDDDQ PVEGVITNGS RVEVEVDIHC CRGREPESSP PLPKNSSNAC SEERARGAGF
     GIRRQNSVNS GILLPANRDK MELQKSPSTS CLYGKKLSNG SIVPLEDSLN LIEVATEAPK
     RKTGYFAAPT QLEPEDQFVV PRDLEEEVKE QMKQHQEGRP EPEPRGEERT EPLEEFDTAL
//
ID   Z385B_MOUSE             Reviewed;         482 AA.
AC   Q8BXJ8; Q8BWQ7;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Zinc finger protein 385B;
DE   AltName: Full=Zinc finger protein 533;
GN   Name=Znf385b; Synonyms=Zfp385b, Zfp533, Znf533;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Liver, Medulla oblongata, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BXJ8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BXJ8-2; Sequence=VSP_015981;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 4 matrin-type zinc fingers.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK046798; BAC32874.1; -; mRNA.
DR   EMBL; AK050293; BAC34170.1; -; mRNA.
DR   EMBL; AK149352; BAE28828.1; -; mRNA.
DR   IPI; IPI00226712; -.
DR   IPI; IPI00655184; -.
DR   RefSeq; NP_001106870.1; NM_001113399.1.
DR   RefSeq; NP_001106871.1; NM_001113400.1.
DR   RefSeq; NP_848838.2; NM_178723.6.
DR   UniGene; Mm.126649; -.
DR   UniGene; Mm.447554; -.
DR   UniGene; Mm.453232; -.
DR   ProteinModelPortal; Q8BXJ8; -.
DR   SMR; Q8BXJ8; 169-201, 292-391.
DR   PRIDE; Q8BXJ8; -.
DR   Ensembl; ENSMUST00000090766; ENSMUSP00000088271; ENSMUSG00000027016.
DR   Ensembl; ENSMUST00000111830; ENSMUSP00000107461; ENSMUSG00000027016.
DR   Ensembl; ENSMUST00000111831; ENSMUSP00000107462; ENSMUSG00000027016.
DR   GeneID; 241494; -.
DR   KEGG; mmu:241494; -.
DR   UCSC; uc008kfy.1; mouse.
DR   UCSC; uc008kfz.1; mouse.
DR   CTD; 241494; -.
DR   MGI; MGI:2444734; Zfp385b.
DR   GeneTree; ENSGT00390000002371; -.
DR   HOGENOM; HBG447157; -.
DR   HOVERGEN; HBG054524; -.
DR   InParanoid; Q8BXJ8; -.
DR   OMA; KLAFQKD; -.
DR   OrthoDB; EOG4SN1P1; -.
DR   PhylomeDB; Q8BXJ8; -.
DR   NextBio; 460397; -.
DR   ArrayExpress; Q8BXJ8; -.
DR   Bgee; Q8BXJ8; -.
DR   CleanEx; MM_ZFP385B; -.
DR   Genevestigator; Q8BXJ8; -.
DR   GermOnline; ENSMUSG00000027016; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR022755; Znf_C2H2_jaz.
DR   InterPro; IPR003604; Znf_U1.
DR   Pfam; PF12171; zf-C2H2_jaz; 3.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   SMART; SM00451; ZnF_U1; 4.
DR   PROSITE; PS50171; ZF_MATRIN; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Metal-binding; Nucleus; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    482       Zinc finger protein 385B.
FT                                /FTId=PRO_0000191813.
FT   ZN_FING      34     64       Matrin-type 1.
FT   ZN_FING     169    199       Matrin-type 2.
FT   ZN_FING     294    328       Matrin-type 3.
FT   ZN_FING     360    390       Matrin-type 4.
FT   VAR_SEQ       1    114       Missing (in isoform 2).
FT                                /FTId=VSP_015981.
SQ   SEQUENCE   482 AA;  51356 MW;  C9F234F5E18E1B71 CRC64;
     MNMATFLRGF EEKGLKNDRP GDQFSKEKKK ILFSFCEVCN IQLNSAAQAQ VHYDGKSHRK
     RVKQLSDGQP PPPVQGSVPL LAGPCPCPGP GPNTSTGSAC HTTTLPALVR TPTLMMQPSL
     DIKPFMSFPV DSSSAVGLFP NFNTMDPVQK AVINHTFGVS IPPKKKQVIS CNVCQLRFNS
     DSQAEAHYKG SKHAKKVKAL EATKNKPKMV PSKDSAKANP SCSIRPGTGD SSDKSEDKGK
     IKATSSSQPS GSEGGSFLLK SGTTPLPLGA IASPSKSTNG APGSVAESEE EKAKKLLYCS
     LCKVAVNSLS QLEAHNTGSK HKTMVEARNG AGPIKSYPRP GSRLKVQNGS KGSGLQNKMF
     HCEICDVHVN SEIQLKQHIS SRRHKDRVAG KPLKPKYSPY NKLQRSPSIL AAKLAFQKDL
     MKPLAPTFLS SPLAAAAVSS ALSLPPRPSA SLFQAAAIPP ALLRPGHGPI RATPASILFA
     PY
//
ID   AGAP1_MOUSE             Reviewed;         857 AA.
AC   Q8BXK8; Q3UHA0; Q6ZPX9; Q8BZG0;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 79.
DE   RecName: Full=Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1;
DE            Short=AGAP-1;
DE   AltName: Full=Centaurin-gamma-2;
DE            Short=Cnt-g2;
GN   Name=Agap1; Synonyms=Centg2, Kiaa1099;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Adrenal gland, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   DEVELOPMENTAL STAGE.
RX   MEDLINE=22527266; PubMed=12640130;
RX   DOI=10.1128/MCB.23.7.2476-2488.2003;
RA   Xia C., Ma W., Stafford L.J., Liu C., Gong L., Martin J.F., Liu M.;
RT   "GGAPs, a new family of bifunctional GTP-binding and GTPase-activating
RT   proteins.";
RL   Mol. Cell. Biol. 23:2476-2488(2003).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=15381706; DOI=10.1074/jbc.M410565200;
RA   Meurer S., Pioch S., Wagner K., Mueller-Esterl W., Gross S.;
RT   "AGAP1, a novel binding partner of nitric oxide-sensitive guanylyl
RT   cyclase.";
RL   J. Biol. Chem. 279:49346-49354(2004).
CC   -!- FUNCTION: GTPase-activating protein for ARF1 and, to a lesser
CC       extent, ARF5. Directly and specifically regulates the adapter
CC       protein 3 (AP-3)-dependent trafficking of proteins in the
CC       endosomal-lysosomal system (By similarity).
CC   -!- ENZYME REGULATION: GAP activity stimulated by phosphatidylinositol
CC       3,4,5-trisphosphate (PIP3) and, to a lesser extent, by
CC       phosphatidylinositol 4,5-bisphosphate (PIP2). Phosphatidic acid
CC       potentiates PIP2 stimulation (By similarity).
CC   -!- SUBUNIT: Homodimer. Interacts with several subunits of the AP-3
CC       protein complex: AP3M1, AP3S1 and AP3S2. Interacts with GUCY1A3
CC       and GUCY1B3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=Associates
CC       with the endocytic compartment (By similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in brain
CC       and kidney.
CC   -!- DEVELOPMENTAL STAGE: At 12.5 dpc, expression is restricted to
CC       neural tube, forebrain and midbrain.
CC   -!- DOMAIN: The PH domain mediates AP-3 binding.
CC   -!- PTM: Phosphorylated on tyrosines (By similarity).
CC   -!- SIMILARITY: Belongs to the centaurin gamma-like family.
CC   -!- SIMILARITY: Contains 2 ANK repeats.
CC   -!- SIMILARITY: Contains 1 Arf-GAP domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98099.2; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK035494; BAC29078.1; -; mRNA.
DR   EMBL; AK046523; BAC32770.1; -; mRNA.
DR   EMBL; AK147503; BAE27957.1; -; mRNA.
DR   EMBL; AK129289; BAC98099.2; ALT_INIT; mRNA.
DR   IPI; IPI00226729; -.
DR   RefSeq; NP_001032213.1; NM_001037136.1.
DR   RefSeq; NP_835220.1; NM_178119.3.
DR   UniGene; Mm.291135; -.
DR   ProteinModelPortal; Q8BXK8; -.
DR   SMR; Q8BXK8; 70-233, 344-592, 610-829.
DR   STRING; Q8BXK8; -.
DR   PhosphoSite; Q8BXK8; -.
DR   PRIDE; Q8BXK8; -.
DR   Ensembl; ENSMUST00000027521; ENSMUSP00000027521; ENSMUSG00000055013.
DR   GeneID; 347722; -.
DR   KEGG; mmu:347722; -.
DR   UCSC; uc007byw.1; mouse.
DR   CTD; 347722; -.
DR   MGI; MGI:2653690; Agap1.
DR   GeneTree; ENSGT00600000084361; -.
DR   HOGENOM; HBG505242; -.
DR   HOVERGEN; HBG054045; -.
DR   InParanoid; Q8BXK8; -.
DR   OMA; ERDEWIQ; -.
DR   NextBio; 400243; -.
DR   ArrayExpress; Q8BXK8; -.
DR   Bgee; Q8BXK8; -.
DR   Genevestigator; Q8BXK8; -.
DR   GermOnline; ENSMUSG00000055013; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR001164; ArfGAP.
DR   InterPro; IPR013684; MIRO-like.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF08477; Miro; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF57863; ArfGAP; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   2: Evidence at transcript level;
KW   ANK repeat; Cytoplasm; GTP-binding; GTPase activation; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Protein transport; Repeat;
KW   Transport; Zinc; Zinc-finger.
FT   CHAIN         1    857       Arf-GAP with GTPase, ANK repeat and PH
FT                                domain-containing protein 1.
FT                                /FTId=PRO_0000074219.
FT   DOMAIN      346    588       PH.
FT   DOMAIN      609    729       Arf-GAP.
FT   REPEAT      768    797       ANK 1.
FT   REPEAT      801    830       ANK 2.
FT   NP_BIND      78     85       GTP (Potential).
FT   NP_BIND     122    126       GTP (Potential).
FT   NP_BIND     178    181       GTP (Potential).
FT   ZN_FING     624    647       C4-type.
FT   REGION       66    276       Small GTPase-like.
FT   MOD_RES     315    315       Phosphoserine (By similarity).
FT   MOD_RES     836    836       Phosphothreonine (By similarity).
FT   CONFLICT    424    424       K -> R (in Ref. 2; BAC98099).
FT   CONFLICT    668    668       D -> Y (in Ref. 1; BAC29078).
FT   CONFLICT    700    700       S -> P (in Ref. 1; BAE27957).
FT   CONFLICT    811    811       Q -> H (in Ref. 1; BAC29078).
SQ   SEQUENCE   857 AA;  94411 MW;  A88AF73A4BB50815 CRC64;
     MNYQQQLANS AAIRAEIQRF ESVHPNIYSI YELLERVEEP VLQNQIREHV IAIEDAFVNS
     QEWTLSRSVP ELKVGIVGNL ASGKSALVHR YLTGTYVQEE SPEGGRFKKE IVVDGQSYLL
     LIRDEGGPPE AQFAMWVDAV IFVFSLEDEI SFQTVYHYYS RMANYRNTSE IPLVLVGTQD
     AISSTNPRVI DDVRARKLSN DLKRCTYYET CATYGLNVER VFQDVAQKIV ATRKKQQLSI
     GPCKSLPNSP SHSSVCSAQV SAVHISQTSN GGGSLSDYSS SVPSTPSTSQ KELRIDVPPT
     ANTPTPVRKQ SKRRSNLFTS RKGSDPDKEK KGLESRADSI GSGRAIPIKQ GMLLKRSGKS
     LNKEWKKKYV TLCDNGVLTY HPSLHDYMQN VHGKEIDLLR TTVKVPGKRP PRATSACAPI
     SSPKTNGLAK DMSSLHISPN SGNVTSASGS QMASGISLVS FNSRPDGMHQ RSYSVSSADQ
     WSDATVIANS AISSDTGLGD SVCSSPSISS STSPKLDPPP SPHANRKKHR RKKSTSNFKA
     DGLSGTAEEQ EENLEFIIVS LTGQTWHFEA TTYEERDAWV QAIESQILAS LQSCESSKNK
     SRLTSQSEAM ALQSIRNMRG NSHCVDCDTQ NPNWASLNLG ALMCIECSGI HRNLGTHLSR
     VRSLDLDDWP MELIKVMSSI GNELANSVWE EGSQGRTKPS LDSTREEKER WIRAKYEQKL
     FLAPLPCTEF SLGQQLLRAT AEEDLRTVIL LLAHGSRDEV NETCGEGDGR TALHLACRKG
     NVVLAQLLIW YGVDVMARDA HGNTALAYAR QASSQECIDV LLQYGCPDER FVLMATPNLS
     RKSNSRNNSS GRAPSVI
//
ID   PPM1K_MOUSE             Reviewed;         372 AA.
AC   Q8BXN7;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Protein phosphatase 1K, mitochondrial;
DE            EC=3.1.3.16;
DE   AltName: Full=Protein phosphatase 2C isoform kappa;
DE            Short=PP2C-kappa;
DE   Flags: Precursor;
GN   Name=Ppm1k; Synonyms=Pp2cm;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=17374715; DOI=10.1101/gad.1499107;
RA   Lu G., Ren S., Korge P., Choi J., Dong Y., Weiss J., Koehler C.,
RA   Chen J.-N., Wang Y.;
RT   "A novel mitochondrial matrix serine/threonine protein phosphatase
RT   regulates the mitochondria permeability transition pore and is
RT   essential for cellular survival and development.";
RL   Genes Dev. 21:784-796(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Head;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=17336929; DOI=10.1016/j.bbrc.2007.02.108;
RA   Joshi M.A., Jeoung N.H., Popov K.M., Harris R.A.;
RT   "Identification of a novel PP2C-type mitochondrial phosphatase.";
RL   Biochem. Biophys. Res. Commun. 356:38-44(2007).
CC   -!- FUNCTION: Regulates the mitochondrial permeability transition pore
CC       and is essential for cellular survival and development.
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the heart, kidney, brain
CC       and liver and to a lesser extent in testis, lung, spleen and
CC       adipose tissue. Very low amount in muscle (at protein level). Also
CC       expressed in the thymus (at protein level) and the diaphragm.
CC       Significantly reduced in hypertrophied hearts.
CC   -!- SIMILARITY: Belongs to the PP2C family.
CC   -!- SIMILARITY: Contains 1 PP2C-like domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK044610; BAC32001.1; -; mRNA.
DR   EMBL; BC092238; AAH92238.1; -; mRNA.
DR   IPI; IPI00226766; -.
DR   RefSeq; NP_780732.1; NM_175523.4.
DR   UniGene; Mm.396893; -.
DR   UniGene; Mm.440035; -.
DR   HSSP; P35813; 1A6Q.
DR   ProteinModelPortal; Q8BXN7; -.
DR   SMR; Q8BXN7; 90-349.
DR   STRING; Q8BXN7; -.
DR   PhosphoSite; Q8BXN7; -.
DR   PRIDE; Q8BXN7; -.
DR   Ensembl; ENSMUST00000042766; ENSMUSP00000041395; ENSMUSG00000037826.
DR   GeneID; 243382; -.
DR   KEGG; mmu:243382; -.
DR   UCSC; uc009cch.1; mouse.
DR   CTD; 243382; -.
DR   MGI; MGI:2442111; Ppm1k.
DR   eggNOG; roNOG12792; -.
DR   GeneTree; ENSGT00540000070009; -.
DR   HOGENOM; HBG445575; -.
DR   HOVERGEN; HBG096199; -.
DR   InParanoid; Q8BXN7; -.
DR   OMA; NEDRFGF; -.
DR   OrthoDB; EOG4MCX0J; -.
DR   PhylomeDB; Q8BXN7; -.
DR   BRENDA; 3.1.3.16; 244.
DR   NextBio; 385765; -.
DR   ArrayExpress; Q8BXN7; -.
DR   Bgee; Q8BXN7; -.
DR   CleanEx; MM_PPM1K; -.
DR   Genevestigator; Q8BXN7; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0008287; C:protein serine/threonine phosphatase complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   InterPro; IPR001932; PP2C-like.
DR   InterPro; IPR000222; PP2C_Mn2_Asp60_BS.
DR   InterPro; IPR014045; PP2C_N.
DR   InterPro; IPR015655; Protein_Pase_2C.
DR   Gene3D; G3DSA:3.60.40.10; PP2C-related; 1.
DR   PANTHER; PTHR13832; PP2C; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-related; 1.
DR   PROSITE; PS01032; PP2C; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW   Protein phosphatase; Transit peptide.
FT   TRANSIT       1     29       Mitochondrion.
FT   CHAIN        30    372       Protein phosphatase 1K, mitochondrial.
FT                                /FTId=PRO_0000278209.
FT   DOMAIN       93    346       PP2C-like.
FT   METAL       127    127       Magnesium (By similarity).
FT   METAL       128    128       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       337    337       Magnesium (By similarity).
SQ   SEQUENCE   372 AA;  40918 MW;  3749BEB94F211E7A CRC64;
     MLSAAFITLL RSGGNQVKKR VLLSSILLQD HRQATPACYF STSEARCSRF DPDGSGQPAT
     WDNFGIWDNR IDEPILLPPS IKYGKPIPKI SLENVGCASL IGKRKENEDR FGFAQLTEEV
     LYFAVYDGHG GPAAADFCHT HMEKCVMDLL PREKDLETVL TLAFLEIDKA FASYAHLSAD
     ASLLTSGTTA TVALLRDGVE LVVASVGDSR ALLCRKGKPM KLTTDHTPER KDEKERIKKF
     GGFVAWNSLG QPHVNGRLAM TRSIGDLDLK ASGVIAEPET TRIKLYHADD SFLVLTTDGI
     NFMVNSQEIC DFVNQCHDPK EAAHSVTEQA IQYGTEDNST AVVVPFGAWG KYKNSEITFS
     FSRSFASSGR WA
//
ID   TM87A_MOUSE             Reviewed;         555 AA.
AC   Q8BXN9; Q8BTV9; Q8BU98; Q8R2P9; Q8R3S7;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Transmembrane protein 87A;
DE   Flags: Precursor;
GN   Name=Tmem87a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Head, Retina, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 328-555 (ISOFORM 1).
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-157 AND ASN-160, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BXN9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BXN9-2; Sequence=VSP_022210;
CC       Name=3;
CC         IsoId=Q8BXN9-3; Sequence=VSP_022210, VSP_022211, VSP_022212;
CC   -!- SIMILARITY: Belongs to the LU7TM family. TMEM87 subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH24676.1; Type=Erroneous initiation;
CC       Sequence=BAC39731.1; Type=Erroneous initiation;
CC       Sequence=BAC40424.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK044591; BAC31991.1; -; mRNA.
DR   EMBL; AK086738; BAC39731.1; ALT_INIT; mRNA.
DR   EMBL; AK088559; BAC40424.1; ALT_INIT; mRNA.
DR   EMBL; BC024676; AAH24676.1; ALT_INIT; mRNA.
DR   EMBL; BC027354; AAH27354.1; -; mRNA.
DR   IPI; IPI00279051; -.
DR   IPI; IPI00625262; -.
DR   IPI; IPI00626341; -.
DR   RefSeq; NP_001103966.1; NM_001110496.1.
DR   RefSeq; NP_001103967.1; NM_001110497.1.
DR   RefSeq; NP_776095.2; NM_173734.3.
DR   UniGene; Mm.260712; -.
DR   UniGene; Mm.411810; -.
DR   PhosphoSite; Q8BXN9; -.
DR   PRIDE; Q8BXN9; -.
DR   Ensembl; ENSMUST00000043847; ENSMUSP00000042237; ENSMUSG00000033808.
DR   Ensembl; ENSMUST00000090042; ENSMUSP00000087496; ENSMUSG00000033808.
DR   Ensembl; ENSMUST00000090046; ENSMUSP00000087500; ENSMUSG00000033808.
DR   GeneID; 211499; -.
DR   KEGG; mmu:211499; -.
DR   UCSC; uc008lvm.1; mouse.
DR   CTD; 211499; -.
DR   MGI; MGI:2441844; Tmem87a.
DR   GeneTree; ENSGT00390000015417; -.
DR   HOVERGEN; HBG068138; -.
DR   OrthoDB; EOG4QNMW3; -.
DR   PhylomeDB; Q8BXN9; -.
DR   NextBio; 373270; -.
DR   ArrayExpress; Q8BXN9; -.
DR   Bgee; Q8BXN9; -.
DR   CleanEx; MM_TMEM87A; -.
DR   Genevestigator; Q8BXN9; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR009637; TM_rcpt_euk.
DR   PANTHER; PTHR21229; Lung7_TM_rcpt; 1.
DR   Pfam; PF06814; Lung_7-TM_R; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Glycoprotein; Membrane; Phosphoprotein; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     21       Potential.
FT   CHAIN        22    555       Transmembrane protein 87A.
FT                                /FTId=PRO_0000270752.
FT   TRANSMEM    226    246       Helical; (Potential).
FT   TRANSMEM    258    278       Helical; (Potential).
FT   TRANSMEM    326    346       Helical; (Potential).
FT   TRANSMEM    362    382       Helical; (Potential).
FT   TRANSMEM    404    424       Helical; (Potential).
FT   TRANSMEM    438    458       Helical; (Potential).
FT   MOD_RES     540    540       Phosphoserine.
FT   CARBOHYD     79     79       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    157    157       N-linked (GlcNAc...).
FT   CARBOHYD    160    160       N-linked (GlcNAc...).
FT   VAR_SEQ     355    376       AQTDLASLAFIPLAFLDTALCW -> YFSYSLALIVSLALS
FT                                AIDACIIL (in isoform 2 and isoform 3).
FT                                /FTId=VSP_022210.
FT   VAR_SEQ     469    483       FAFSPLSEEDEEDEQ -> RNENEKYQAGTKWD (in
FT                                isoform 3).
FT                                /FTId=VSP_022211.
FT   VAR_SEQ     484    555       Missing (in isoform 3).
FT                                /FTId=VSP_022212.
FT   CONFLICT    116    116       G -> W (in Ref. 1; BAC40424).
FT   CONFLICT    141    141       F -> L (in Ref. 1; BAC40424).
FT   CONFLICT    491    491       S -> G (in Ref. 1; BAC39731).
FT   CONFLICT    514    514       Missing (in Ref. 1; BAC39731).
SQ   SEQUENCE   555 AA;  63380 MW;  4BC075BF0491A826 CRC64;
     MAVAAWLQVS PVIFLLLGAQ PFPLSFLGAG PAPVFAADRS KWHIPMPSGK GYFNFGKILF
     RNTTILLKFD GEPCDQSLNI TWFLKSADCY NEIYNFKADE IESYLENLKG KKGLSGRYQT
     SSRLFQNCSE LYKAQSFSGD FTHRLPLLGE KQEAKENATN VTFTGDKIAM HEPLQTWQDA
     PYIFIVHVGI SSSKESPKEN ALSNLFTMTV EVKGPYEYLT LEDYPLMIFF MVMCIVYVLF
     GVLWLAWSAC YWRDLLRIQF WIGAVIFLGM FEKAVFYAEF QNIRYKGESV QNALVLAELL
     SAVKRSLART LVIIVSLGYG IVKPRLGVTL HKVVVAGALY LLFSGMEGVL RVTGAQTDLA
     SLAFIPLAFL DTALCWWIFI SLTQTMKLLK LRRNIVKLSL YRHFTNTLIL AVAASIVFII
     WTTMKFRIVT CQSDWRELWV DDAIWRLLFS MILFVIMILW RPSANNQRFA FSPLSEEDEE
     DEQKEPMLKE SFEGMKMRST KQEPNGTSKV NKAQEDDLKW VEENVPSSVT DVALPALLDS
     DEERMITHFE RSKME
//
ID   FA53C_MOUSE             Reviewed;         393 AA.
AC   Q8BXQ8; Q3U4J2;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=Protein FAM53C;
GN   Name=Fam53c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SIMILARITY: Belongs to the FAM53 family.
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DR   EMBL; BC057111; AAH57111.1; -; mRNA.
DR   EMBL; AK044469; BAC31938.1; -; mRNA.
DR   EMBL; AK154214; BAE32439.1; -; mRNA.
DR   IPI; IPI00226801; -.
DR   RefSeq; NP_780313.1; NM_175104.4.
DR   UniGene; Mm.29424; -.
DR   ProteinModelPortal; Q8BXQ8; -.
DR   PhosphoSite; Q8BXQ8; -.
DR   PRIDE; Q8BXQ8; -.
DR   Ensembl; ENSMUST00000049281; ENSMUSP00000037034; ENSMUSG00000034300.
DR   Ensembl; ENSMUST00000097622; ENSMUSP00000095226; ENSMUSG00000034300.
DR   GeneID; 66306; -.
DR   KEGG; mmu:66306; -.
DR   UCSC; uc008eli.1; mouse.
DR   CTD; 66306; -.
DR   MGI; MGI:1913556; Fam53c.
DR   eggNOG; roNOG08907; -.
DR   GeneTree; ENSGT00530000063371; -.
DR   HOGENOM; HBG714254; -.
DR   HOVERGEN; HBG051537; -.
DR   InParanoid; Q8BXQ8; -.
DR   OMA; FMACSPP; -.
DR   OrthoDB; EOG4Z62NW; -.
DR   PhylomeDB; Q8BXQ8; -.
DR   NextBio; 321261; -.
DR   ArrayExpress; Q8BXQ8; -.
DR   Bgee; Q8BXQ8; -.
DR   CleanEx; MM_2810012G03RIK; -.
DR   Genevestigator; Q8BXQ8; -.
DR   GermOnline; ENSMUSG00000034300; Mus musculus.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    393       Protein FAM53C.
FT                                /FTId=PRO_0000189547.
FT   MOD_RES       6      6       Phosphothreonine (By similarity).
FT   MOD_RES      13     13       Phosphothreonine (By similarity).
FT   MOD_RES     122    122       Phosphoserine (By similarity).
FT   MOD_RES     232    232       Phosphoserine.
FT   MOD_RES     234    234       Phosphoserine (By similarity).
FT   MOD_RES     251    251       Phosphoserine (By similarity).
FT   MOD_RES     254    254       Phosphoserine (By similarity).
FT   MOD_RES     255    255       Phosphoserine (By similarity).
SQ   SEQUENCE   393 AA;  43261 MW;  059D5BF355BCDD7F CRC64;
     MITLITEQLQ KQTLDELKCT RFSVSLPLPD HADIPNCGDP FQLVSEGASW RGLPHCSCAE
     FQDSLNFSYH PSGLSLHLRP PSRGNSPKEP PLSQVLSPEP PDPEKLPVPP APPSKRHCRS
     LSVPVDLSRW QPVWRPAPSK LWTPIKHRGN AGGGGPQVPQ QSPPKRVSSL RFLQAPSASS
     QCAPAHRPYS PPFFSLALAQ DSAQPCATSP QSGSWESDAE SLSPCPPQRR FSLSPSLGPQ
     ASRFLPSARS SPASSPELPW RPRGLRNLPR SRSQPCDLDA RKTGVKRRHE EDCRRLRPSL
     DFDKMNQKPY SGGLCLQETA REEGSNVSPP WFMACSPPPL SASCSPVEGS SQVLSESEEE
     EEGSVRWERQ ALSKRTLCQQ DFGDLDLNLI EEN
//
ID   S7A14_MOUSE             Reviewed;         771 AA.
AC   Q8BXR1; Q69ZE9;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Probable cationic amino acid transporter;
DE   AltName: Full=Solute carrier family 7 member 14;
GN   Name=Slc7a14; Synonyms=Kiaa1613;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32495.1; Type=Erroneous initiation;
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DR   EMBL; AK173217; BAD32495.1; ALT_INIT; mRNA.
DR   EMBL; AK044448; BAC31925.1; -; mRNA.
DR   EMBL; BC061928; AAH61928.1; -; mRNA.
DR   IPI; IPI00226807; -.
DR   RefSeq; NP_766449.1; NM_172861.3.
DR   UniGene; Mm.285366; -.
DR   UniGene; Mm.477224; -.
DR   ProteinModelPortal; Q8BXR1; -.
DR   PhosphoSite; Q8BXR1; -.
DR   PRIDE; Q8BXR1; -.
DR   Ensembl; ENSMUST00000091259; ENSMUSP00000088803; ENSMUSG00000069072.
DR   GeneID; 241919; -.
DR   KEGG; mmu:241919; -.
DR   UCSC; uc008ovx.1; mouse.
DR   CTD; 241919; -.
DR   MGI; MGI:3040688; Slc7a14.
DR   eggNOG; roNOG08228; -.
DR   GeneTree; ENSGT00560000076611; -.
DR   HOGENOM; HBG727793; -.
DR   HOVERGEN; HBG000280; -.
DR   InParanoid; Q8BXR1; -.
DR   OMA; WMVDSVG; -.
DR   OrthoDB; EOG4WH8KD; -.
DR   NextBio; 385178; -.
DR   ArrayExpress; Q8BXR1; -.
DR   Bgee; Q8BXR1; -.
DR   Genevestigator; Q8BXR1; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015171; F:amino acid transmembrane transporter activity; IEA:InterPro.
DR   InterPro; IPR004841; AA-permease_dom.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   InterPro; IPR015606; Cat-AATrans.
DR   PANTHER; PTHR11785; AA/rel_permease1; 1.
DR   PANTHER; PTHR11785:SF53; Cat-AATrans; 1.
DR   Pfam; PF00324; AA_permease; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid transport; Glycoprotein; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    771       Probable cationic amino acid transporter.
FT                                /FTId=PRO_0000307361.
FT   TRANSMEM     58     78       Helical; (Potential).
FT   TRANSMEM     83    103       Helical; (Potential).
FT   TRANSMEM    119    141       Helical; (Potential).
FT   TRANSMEM    187    207       Helical; (Potential).
FT   TRANSMEM    216    236       Helical; (Potential).
FT   TRANSMEM    251    271       Helical; (Potential).
FT   TRANSMEM    291    311       Helical; (Potential).
FT   TRANSMEM    336    356       Helical; (Potential).
FT   TRANSMEM    384    404       Helical; (Potential).
FT   TRANSMEM    407    427       Helical; (Potential).
FT   TRANSMEM    565    585       Helical; (Potential).
FT   TRANSMEM    596    616       Helical; (Potential).
FT   TRANSMEM    628    648       Helical; (Potential).
FT   TRANSMEM    655    675       Helical; (Potential).
FT   CARBOHYD    282    282       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    676    676       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   771 AA;  83984 MW;  52381841C32BC848 CRC64;
     MSGFLASLDP RRVQWGAAWY AMHSRILRTK PVESMLEGTG TTSAHGTKLA QVLTTVDLIS
     LGVGSCVGTG MYVVSGLVAK EMAGPGVIVS FIIAAVASIL SGVCYAEFGV RVPKTTGSAY
     TYSYVTVGEF VAFFIGWNLI LEYLIGTAAG ASALSSMFDS LANHSISRWM VDTVGTLNGL
     GKGEESYPDL LALVIAVIVT IIVALGVKNS VGFNNVLNVL NLAVWVFIMI AGLFFINGKY
     WAEGQFLPHG WSGVLQGAAT CFYAFIGFDI IATTGEEAKN PNTSIPYAIT ASLVICLTAY
     VSVSMILTLM VPYYAIDTES PLMEMFVAHG FYAAKFVVAI GSVAGLTVSL LGSLFPMPRV
     IYAMAGDGLL FRFLAHVSSY TETPVVACIV SGFLAALLSL LVSLRDLIEM MSIGTLLAYT
     LVSVCVLLLR YQPESDIDGF VKFLSEEHTK KKEGILADCE KETCSPVSEG EEFSSPATNT
     CGAKNLPSLG DNEMLIGKSD KSAYNVNHPN YGTVDMTTGI EADESENIYL IKLKKLIGPR
     YYTMRIRLGL PGKMDRPTAA TGHTVTICVL LLFILMFIFC SFIIFGSEYI SGQSWWAILL
     VVLMMLLISV LVFVILQQPE NPKKLPYMAP CLPFVPAFAM LVNIYLMLKL STITWIRFAV
     WCFVGMLIYF GYGIWNSTLE ISAREQALHQ STYQRYDVDD PFSVEEGFSY ATEGESQEDW
     GGPAEDKGFY YQQMSDAKAN SRTSSKAKSK SKHKQNSEAL IANDELDCSP E
//
ID   NALCN_MOUSE             Reviewed;        1738 AA.
AC   Q8BXR5; Q8BYM2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Sodium leak channel non-selective protein;
DE   AltName: Full=Voltage gated channel-like protein 1;
GN   Name=Nalcn; Synonyms=Vgcnl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1229-1738 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=17448995; DOI=10.1016/j.cell.2007.02.041;
RA   Lu B., Su Y., Das S., Liu J., Xia J., Ren D.;
RT   "The neuronal channel NALCN contributes resting sodium permeability
RT   and is required for normal respiratory rhythm.";
RL   Cell 129:371-383(2007).
RN   [4]
RP   FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH UNC79 AND UNC80.
RX   PubMed=19092807; DOI=10.1038/nature07579;
RA   Lu B., Su Y., Das S., Wang H., Wang Y., Liu J., Ren D.;
RT   "Peptide neurotransmitters activate a cation channel complex of NALCN
RT   and UNC-80.";
RL   Nature 457:741-744(2009).
CC   -!- FUNCTION: Voltage-independent, cation-nonselective channel which
CC       is permeable to sodium, potassium and calcium ions. Responsible
CC       for the background sodium ion leak current in neurons and controls
CC       neuronal excitability. Activated either by neuropeptides substance
CC       P or neurotensin. Required for normal respiratory rhythm and
CC       neonatal survival.
CC   -!- SUBUNIT: Interacts with UNC79/KIAA1409 and UNC80.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BXR5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BXR5-2; Sequence=VSP_030192;
CC   -!- TISSUE SPECIFICITY: Widely expressed in the brain and spinal cord
CC       neurons.
CC   -!- DOMAIN: Each of the four internal repeats contains five
CC       hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one
CC       positively charged transmembrane segment (S4). S4 segments
CC       probably represent the voltage-sensor and are characterized by a
CC       series of positively charged amino acids at every third position.
CC   -!- PTM: Phosphorylated on tyrosine residues.
CC   -!- SIMILARITY: Belongs to the cation-nonselective channel family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC31915.1; Type=Frameshift; Positions=1257;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK039034; BAC30213.1; -; mRNA.
DR   EMBL; AK044431; BAC31915.1; ALT_FRAME; mRNA.
DR   EMBL; AC102783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC124818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00660906; -.
DR   IPI; IPI00742341; -.
DR   RefSeq; NP_796367.3; NM_177393.4.
DR   UniGene; Mm.255348; -.
DR   ProteinModelPortal; Q8BXR5; -.
DR   PhosphoSite; Q8BXR5; -.
DR   PRIDE; Q8BXR5; -.
DR   Ensembl; ENSMUST00000000201; ENSMUSP00000000201; ENSMUSG00000000197.
DR   Ensembl; ENSMUST00000072254; ENSMUSP00000072105; ENSMUSG00000000197.
DR   GeneID; 338370; -.
DR   KEGG; mmu:338370; -.
DR   CTD; 338370; -.
DR   MGI; MGI:2444306; Nalcn.
DR   eggNOG; roNOG06448; -.
DR   GeneTree; ENSGT00450000040277; -.
DR   HOGENOM; HBG355985; -.
DR   HOVERGEN; HBG063081; -.
DR   InParanoid; Q8BXR5; -.
DR   OrthoDB; EOG4R501V; -.
DR   NextBio; 400179; -.
DR   ArrayExpress; Q8BXR5; -.
DR   Bgee; Q8BXR5; -.
DR   CleanEx; MM_NALCN; -.
DR   Genevestigator; Q8BXR5; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005272; F:sodium channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR   InterPro; IPR005821; Ion_trans.
DR   Pfam; PF00520; Ion_trans; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Ion transport; Ionic channel;
KW   Membrane; Phosphoprotein; Repeat; Sodium; Sodium channel;
KW   Sodium transport; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN         1   1738       Sodium leak channel non-selective
FT                                protein.
FT                                /FTId=PRO_0000314011.
FT   TOPO_DOM      1     40       Cytoplasmic (Potential).
FT   TRANSMEM     41     61       Helical; Name=S1 of repeat I;
FT                                (Potential).
FT   TOPO_DOM     62     66       Extracellular (Potential).
FT   TRANSMEM     67     87       Helical; Name=S2 of repeat I;
FT                                (Potential).
FT   TOPO_DOM     88    106       Cytoplasmic (Potential).
FT   TRANSMEM    107    127       Helical; Name=S3 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    128    138       Extracellular (Potential).
FT   TRANSMEM    139    158       Helical; Voltage-sensor; Name=S4 of
FT                                repeat I; (Potential).
FT   TOPO_DOM    159    182       Cytoplasmic (Potential).
FT   TRANSMEM    183    203       Helical; Name=S5 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    204    301       Extracellular (Potential).
FT   TRANSMEM    302    322       Helical; Name=S6 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    323    382       Cytoplasmic (Potential).
FT   TRANSMEM    383    403       Helical; Name=S1 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    404    422       Extracellular (Potential).
FT   TRANSMEM    423    443       Helical; Name=S2 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    444    448       Cytoplasmic (Potential).
FT   TRANSMEM    449    468       Helical; Name=S3 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    469    476       Extracellular (Potential).
FT   TRANSMEM    477    500       Helical; Voltage-sensor; Name=S4 of
FT                                repeat II; (Potential).
FT   TOPO_DOM    501    509       Cytoplasmic (Potential).
FT   TRANSMEM    510    530       Helical; Name=S5 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    531    578       Extracellular (Potential).
FT   TRANSMEM    579    599       Helical; Name=S6 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    600    880       Cytoplasmic (Potential).
FT   TRANSMEM    881    901       Helical; Name=S1 of repeat III;
FT                                (Potential).
FT   TOPO_DOM    902    923       Extracellular (Potential).
FT   TRANSMEM    924    944       Helical; Name=S2 of repeat III;
FT                                (Potential).
FT   TOPO_DOM    945    952       Cytoplasmic (Potential).
FT   TRANSMEM    953    973       Helical; Name=S3 of repeat III;
FT                                (Potential).
FT   TOPO_DOM    974    979       Extracellular (Potential).
FT   TRANSMEM    980    997       Helical; Voltage-sensor; Name=S4 of
FT                                repeat III; (Potential).
FT   TOPO_DOM    998   1015       Cytoplasmic (Potential).
FT   TRANSMEM   1016   1036       Helical; Name=S5 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1037   1135       Extracellular (Potential).
FT   TRANSMEM   1136   1156       Helical; Name=S6 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1157   1209       Cytoplasmic (Potential).
FT   TRANSMEM   1210   1227       Helical; Name=S1 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1228   1235       Extracellular (Potential).
FT   TRANSMEM   1236   1256       Helical; Name=S2 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1257   1277       Cytoplasmic (Potential).
FT   TRANSMEM   1278   1298       Helical; Name=S3 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1299   1299       Extracellular (Potential).
FT   TRANSMEM   1300   1316       Helical; Voltage-sensor; Name=S4 of
FT                                repeat IV; (Potential).
FT   TOPO_DOM   1317   1335       Cytoplasmic (Potential).
FT   TRANSMEM   1336   1356       Helical; Name=S5 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1357   1426       Extracellular (Potential).
FT   TRANSMEM   1427   1447       Helical; Name=S6 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1448   1738       Cytoplasmic (Potential).
FT   COILED      795    830       Potential.
FT   MOD_RES     497    497       Phosphotyrosine (By similarity).
FT   VAR_SEQ     216   1738       Missing (in isoform 2).
FT                                /FTId=VSP_030192.
FT   CONFLICT   1229   1229       V -> F (in Ref. 1; BAC31915).
FT   CONFLICT   1607   1607       R -> RL (in Ref. 1; BAC31915).
SQ   SEQUENCE   1738 AA;  200441 MW;  C35A414B4B694299 CRC64;
     MLKRKQSSRV EAQPVTDFGP DESLSDNADI LWINKPWVHS LLRICAIISV ISVCMNTPMT
     FEHYPPLQYV TFTLDTLLMF LYTAEMIAKM HIRGIVKGDS SYVKDRWCVF DGFMVFCLWV
     SLVLQVFEIA DIVDQMSPWG MLRIPRPLIM IRAFRIYFRF ELPRTRITNI LKRSGEQIWS
     VSIFLLFFLL LYGILGVQMF GTFTYHCVVN DTKPGNVTWN SLAIPDTHCS PELEEGYQCP
     PGFKCMDLED LGLSRQELGY SGFNEIGTSI FTVYEASSQE GWVFLMYRAI DSFPRWRSYF
     YFITLIFFLA WLVKNVFIAV IIETFAEIRV QFQQMWGTRS STTSTATTQM FHEDAAGGWQ
     LVAVDVNKPQ GRAPACLQKM MRSSVFHMFI LSMVTVDVIV AASNYYKGEN FRRQYDEFYL
     AEVAFTVLFD LEALLKIWCL GFTGYISSSL HKFELLLVIG TTLHVYPDLY HSQFTYFQVL
     RVVRLIKISP ALEDFVYKIF GPGKKLGSLV VFTASLLIVM SAISLQMFCF VEELDRFTTF
     PRAFMSMFQI LTQEGWVDVM DQTLNAVGHM WAPLVAIYFI LYHLFATLIL LSLFVAVILD
     NLELDEDLKK LKQLKQSEAN ADTKEKLPLR LRIFEKFPNR PQMVKISKLP SDFTVPKIRE
     SFMKQFIDRQ QQDTCCLFRI LPSTSSSSCD NPKKPTAEDN KYIDQKLRKS VFSIRARNLL
     EKETAVTKIL RACTRQRMLS GSFEGQPAKE RSILSVQHHI RQERRSLRHG SNSQRISRGK
     SLETLTQDHS NTVRYRNAQR EDSEIKMIQE KKEQAEMKRK VQEEELRENH PYFDKPLFIV
     GREHRFRNFC RVVVRARFNA SKTDPVTGAV KNTKYHQLYD LLGLVTYLDW VMITVTICSC
     ISMMFESPFR RVMHAPTLQI AEYVFVIFMS IELNLKIMAD GLFFTPTAVI RDFGGVMDIF
     IYLVSLIFLC WMPQNVPAES GAQLLMVLRC LRPLRIFKLV PQMRKVVREL FSGFKEIFLV
     SILLLTLMLV FASFGVQLFA GKLAKCNDPN IIRREDCNGI FRINVSVSKN LNLKLRPGEK
     KPGFWVPRVW ANPRNFNFDN VGNAMLALFE VLSLKGWVEV RDVIIHRVGP IHGIYIHVFV
     FLGCMIGLTL FVGVVIANFN ENKGTALLTV DQRRWEDLKS RLKIAQPLHL PPRPDNDGFR
     AKMYDITQHP FFKRTIALLV LAQSVLLSVK WDVDDPVTVP LATMSVVFTF IFVLEVTMKI
     IAMSPAGFWQ SRRNRYDLLV TSLGVVWVVL HFALLNAYTY MMGACVIVFR FFSICGKHVT
     LKMLLLTVVV SMYKSFFIIV GMFLLLLCYA FAGVVLFGTV KYGENINRHA NFSSAGKAIT
     VLFRIVTGED WNKIMHDCMV QPPFCTPDEF TYWATDCGNY AGALMYFCSF YVIIAYIMLN
     LLVAIIVENF SLFYSTEEDQ LLSYNDLRHF QIIWNMVDDK REGVIPTFRV KFLLRLLRGR
     LEVDLDKDKL LFKHMCYEME RLHNGGDVTF HDVLSMLSYR SVDIRKSLQL EELLAREQLE
     YTIEEEVAKQ TIRMWLKKCL KRIRAKQQQS CSIIHSLRES QEQERSRFLN PPSIETTQPS
     EDSNANSQDH SMQPETSSQQ QLLSPTLSDR GGSRQDAADT GKPQRKIGQW RLPSAPKPIS
     HSVSSVNLRF GGRTTMKTVV CKMNPMPDTA SCGSEVKKWW TRQLTVESDE SGDDLLDI
//
ID   OSBL6_MOUSE             Reviewed;         959 AA.
AC   Q8BXR9; Q8BYW2;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Oxysterol-binding protein-related protein 6;
DE            Short=ORP-6;
DE            Short=OSBP-related protein 6;
GN   Name=Osbpl6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Retina, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BXR9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BXR9-2; Sequence=VSP_010012;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the OSBP family.
CC   -!- SIMILARITY: Contains 1 PH domain.
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DR   EMBL; AK037703; BAC29854.1; -; mRNA.
DR   EMBL; AK044411; BAC31907.1; -; mRNA.
DR   IPI; IPI00226821; -.
DR   IPI; IPI00411121; -.
DR   RefSeq; NP_663500.2; NM_145525.2.
DR   UniGene; Mm.240435; -.
DR   ProteinModelPortal; Q8BXR9; -.
DR   SMR; Q8BXR9; 85-182.
DR   STRING; Q8BXR9; -.
DR   PhosphoSite; Q8BXR9; -.
DR   PRIDE; Q8BXR9; -.
DR   Ensembl; ENSMUST00000090784; ENSMUSP00000088290; ENSMUSG00000042359.
DR   Ensembl; ENSMUST00000111929; ENSMUSP00000107560; ENSMUSG00000042359.
DR   Ensembl; ENSMUST00000111930; ENSMUSP00000107561; ENSMUSG00000042359.
DR   GeneID; 99031; -.
DR   KEGG; mmu:99031; -.
DR   UCSC; uc008kfb.1; mouse.
DR   UCSC; uc008kfc.1; mouse.
DR   CTD; 99031; -.
DR   MGI; MGI:2139014; Osbpl6.
DR   GeneTree; ENSGT00550000074251; -.
DR   HOVERGEN; HBG058934; -.
DR   OrthoDB; EOG49S65P; -.
DR   PhylomeDB; Q8BXR9; -.
DR   NextBio; 353761; -.
DR   ArrayExpress; Q8BXR9; -.
DR   Bgee; Q8BXR9; -.
DR   CleanEx; MM_OSBPL6; -.
DR   Genevestigator; Q8BXR9; -.
DR   GermOnline; ENSMUSG00000042359; Mus musculus.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0008202; P:steroid metabolic process; IEA:InterPro.
DR   InterPro; IPR000648; Oxysterol-bd.
DR   InterPro; IPR018494; Oxysterol-bd_CS.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   PANTHER; PTHR10972; Oxysterol_bd; 1.
DR   Pfam; PF01237; Oxysterol_BP; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS01013; OSBP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Lipid transport; Lipid-binding; Phosphoprotein;
KW   Transport.
FT   CHAIN         1    959       Oxysterol-binding protein-related protein
FT                                6.
FT                                /FTId=PRO_0000100376.
FT   DOMAIN       86    181       PH.
FT   MOD_RES       2      2       Phosphoserine (By similarity).
FT   MOD_RES      44     44       Phosphoserine (By similarity).
FT   MOD_RES     229    229       Phosphoserine (By similarity).
FT   MOD_RES     368    368       Phosphoserine (By similarity).
FT   MOD_RES     453    453       Phosphoserine (By similarity).
FT   VAR_SEQ     299    329       Missing (in isoform 2).
FT                                /FTId=VSP_010012.
FT   CONFLICT    796    796       W -> L (in Ref. 1; BAC29854).
SQ   SEQUENCE   959 AA;  108920 MW;  5D50B27C0065C361 CRC64;
     MSSDEKGISP AHKTSTPTHR SASSSTSSQR ESRQSIHVLE RTASSSTEPS VSRQLLEPEP
     IPLSKEADSW EIIEGLKIGQ TNVQKPDRHE GFMLKKRKWP LKGWHKRFFV LDNGMLKYSK
     APLDIQKGKV HGSIDVGLSV MSIKKKARRI DLDTEEHIYH LKVKSQDWFD AWVSKLRHHR
     LYRQNEIVRS PRDASFHIFP ATSTAESSPA ANVSVVDGKM QPNSFPWQSP LPCSNSLPAT
     CTTGQSKVAA WLQDSEEMDR CAEDLAHCQS NLVELSKLLQ NLEILQRTQS APNFTDMQAN
     CVDISKKDKR VTRRWRTKSV SKDTKIQLQE GPPAKGQFNT TRRRQRLAAA VATTVPFSAT
     MSPVRLHSSN PNLCADIEFQ TPPSHLTDPL ESSTDYTKLQ EEFCLIAQKV HSLLKSAFNS
     IAIEKEKLKQ VVSEQDHNKG HSTQMARLRQ SLSQALNQNA ELRSRLNRIH SESTICDHVV
     SVNIIPSPDE PGEQIHVSLP LSQQVANESR LSMSESVSEF FDAQEVLLSA SSSENEASDD
     ESYISDVSDN ISEDNTSVAD NISRQILNGE LTGGAFRNGR RTCLPAPCPD TSNINLWNIL
     RNNIGKDLSK VSMPVELNEP LNTLQHLCEE MEYSELLDKA SETDDPYERM VLVAAFAVSG
     YCSTYFRAGS KPFNPVLGET YECIREDKGF RFFSEQVSHH PPISACHCES KNFVFWQDIR
     WKNKFWGKSM EILPVGTLNV TLPKYGDYYV WNKVTTCIHN ILSGRRWIEH YGEVTLRNTK
     SSVCICKLTF VKVNYWNSNV NEVQGVVIDQ EGKVVHRLFG KWHEGLYCGV APSAKCIWRP
     GSLPTNYELY YGFTRFAVEL NELDPVLKDL LPPTDARFRP DQRFLEEGNL EAAAAEKQRV
     EELQRSRRRY MEENNLEHIP KFFKKVIDAN QREAWVSNDT YWELRKDPGF SKVDSPVLW
//
ID   RGS8_MOUSE              Reviewed;         180 AA.
AC   Q8BXT1; Q505F2;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Regulator of G-protein signaling 8;
DE            Short=RGS8;
GN   Name=Rgs8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Inhibits signal transduction by increasing the GTPase
CC       activity of G protein alpha subunits thereby driving them into
CC       their inactive GDP-bound form. Preferentially binds to G(o)-alpha
CC       and G(i)-alpha-3 (By similarity).
CC   -!- SIMILARITY: Contains 1 RGS domain.
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DR   EMBL; AK044337; BAC31874.1; -; mRNA.
DR   EMBL; AK142301; BAE25020.1; -; mRNA.
DR   EMBL; BC065056; AAH65056.1; -; mRNA.
DR   EMBL; BC094577; AAH94577.1; -; mRNA.
DR   IPI; IPI00399848; -.
DR   RefSeq; NP_080656.2; NM_026380.3.
DR   UniGene; Mm.379143; -.
DR   ProteinModelPortal; Q8BXT1; -.
DR   SMR; Q8BXT1; 56-171.
DR   STRING; Q8BXT1; -.
DR   PhosphoSite; Q8BXT1; -.
DR   PRIDE; Q8BXT1; -.
DR   Ensembl; ENSMUST00000041776; ENSMUSP00000045715; ENSMUSG00000042671.
DR   Ensembl; ENSMUST00000111810; ENSMUSP00000107441; ENSMUSG00000042671.
DR   Ensembl; ENSMUST00000111812; ENSMUSP00000107443; ENSMUSG00000042671.
DR   GeneID; 67792; -.
DR   KEGG; mmu:67792; -.
DR   UCSC; uc007dad.1; mouse.
DR   CTD; 67792; -.
DR   MGI; MGI:108408; Rgs8.
DR   eggNOG; roNOG16741; -.
DR   GeneTree; ENSGT00600000084096; -.
DR   HOGENOM; HBG713967; -.
DR   HOVERGEN; HBG013233; -.
DR   InParanoid; Q8BXT1; -.
DR   OMA; SCFDQAQ; -.
DR   OrthoDB; EOG4RV2SM; -.
DR   PhylomeDB; Q8BXT1; -.
DR   NextBio; 325577; -.
DR   ArrayExpress; Q8BXT1; -.
DR   Bgee; Q8BXT1; -.
DR   CleanEx; MM_RGS8; -.
DR   Genevestigator; Q8BXT1; -.
DR   GermOnline; ENSMUSG00000042671; Mus musculus.
DR   GO; GO:0005096; F:GTPase activator activity; TAS:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; TAS:MGI.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000342; Regulat_G_prot_signal.
DR   InterPro; IPR016137; Regulat_G_prot_signal_superfam.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48097; Regulat_G_prot_signal_superfam; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   2: Evidence at transcript level;
KW   Signal transduction inhibitor.
FT   CHAIN         1    180       Regulator of G-protein signaling 8.
FT                                /FTId=PRO_0000204200.
FT   DOMAIN       56    171       RGS.
SQ   SEQUENCE   180 AA;  20963 MW;  00FC35E572785856 CRC64;
     MAALLMPRRN KGMRTRLGCL SHKSDSCSDF TAILPDKPNR ALKRLSTEEA TRWAESFDVL
     LSHKYGVAAF RAFLKTEFSE ENLEFWLACE EFKKTRSTAK LVTKAHRIFE EFVDVQAPRE
     VNIDFQTREA TRKNMQEPSL TCFDQAQGKV HSLMEKDSYP RFLRSKMYLD LLSQSQRRLS
//
ID   Q8BXW8_MOUSE            Unreviewed;       698 AA.
AC   Q8BXW8;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   30-NOV-2010, entry version 49.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Uvrag; Synonyms=Uvrag1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK043084; BAC31454.1; -; mRNA.
DR   IPI; IPI00453656; -.
DR   UniGene; Mm.323072; -.
DR   ProteinModelPortal; Q8BXW8; -.
DR   STRING; Q8BXW8; -.
DR   Ensembl; ENSMUST00000037968; ENSMUSP00000045297; ENSMUSG00000035354.
DR   MGI; MGI:1925860; Uvrag.
DR   HOVERGEN; HBG059846; -.
DR   InParanoid; Q8BXW8; -.
DR   ArrayExpress; Q8BXW8; -.
DR   Bgee; Q8BXW8; -.
DR   Genevestigator; Q8BXW8; -.
DR   GO; GO:0043234; C:protein complex; IDA:MGI.
DR   GO; GO:0017124; F:SH3 domain binding; IPI:MGI.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   Pfam; PF00168; C2; 1.
DR   SMART; SM00239; C2; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   698 AA;  77483 MW;  424D82DFEE3DAC24 CRC64;
     MSSCASLGGP GPLPPPGPSA ALTSGAPARA LHVELPSQQR RLRHLRNIAA RNIVNRNGHQ
     LLDTYFTLHL CDNEKIFKEF YRSEVIKNSL NPTWRSLDFG IMPDRLDTSV SCFVVKIWGG
     KEEAFQLLIE WKVYLDGLKY LGQQIHARNQ NEIIFGLNDG YYGAPCEHKG HPNAQKNLLQ
     VDQNCVRNSY DVFSLLRLHR AQCAIKQTQV TVQRLGKEIE EKLRLTSTSN ELKKESECLR
     LKILVLRNEL ERQKKALGRE VAFLHKQQMA LQDKGSAFST EHGKLQLQKD SLSELRKECT
     AKRELFLKTN AQLTIRCRQL LSELSYIYPI DLNENKDYFV CGVKLPNSED FQAKDDGSIA
     VALGYTAHLV SMISFFLQVP LRYPIIHKGS RSTIKDNIND KLTEKEREFP LYPKGGEKLQ
     FDYGVYLLNK NIAQLRYQHG LGTPDLRQTL PNLKNFMEHG LMVRCDRHHI SNAIPVPKRQ
     SSTFGGADGG FSAGIPSPDK VHRKRASSEN ERLQYKTPPP SYNSALTQPG VAMPTSGDSE
     RKVAPLSSSL DTSLDFSKEN KKAGVDLGSS VSGDHGNSDS GQEQGEALPG HLAAVNGTAL
     PSEQAGPAGT LLPGSCHPAP SAELCCAVEQ AEEIIGLEAT GFTSGDQLEA LSCIPVDSAV
     AVECDEQVLG EFEEFSRRIY ALSENVSSFR RPRRSSDK
//
ID   TMX3_MOUSE              Reviewed;         456 AA.
AC   Q8BXZ1; Q3US84; Q6PGA1; Q6ZPH5; Q8BZB8;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 2.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Protein disulfide-isomerase TMX3;
DE            EC=5.3.4.1;
DE   AltName: Full=Thioredoxin domain-containing protein 10;
DE   AltName: Full=Thioredoxin-related transmembrane protein 3;
DE   Flags: Precursor;
GN   Name=Tmx3; Synonyms=Kiaa1830, Txndc10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Corpus striatum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 132-150 AND 368-375, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Probable disulfide isomerase, which participates in the
CC       folding of proteins containing disulfide bonds. May act as a
CC       dithiol oxidase (By similarity).
CC   -!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
CC       proteins.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       membrane protein (By similarity).
CC   -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum
CC       localization for type I membrane proteins (By similarity).
CC   -!- PTM: N-glycosylated (By similarity).
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98261.1; Type=Erroneous initiation;
CC       Sequence=BC057139; Type=Frameshift; Positions=176;
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DR   EMBL; AK129451; BAC98261.1; ALT_INIT; mRNA.
DR   EMBL; AK035946; BAC29254.1; -; mRNA.
DR   EMBL; AK042787; BAC31366.2; -; mRNA.
DR   EMBL; AK140709; BAE24450.1; -; mRNA.
DR   EMBL; BC057139; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00453798; -.
DR   RefSeq; NP_938037.2; NM_198295.2.
DR   UniGene; Mm.268041; -.
DR   ProteinModelPortal; Q8BXZ1; -.
DR   SMR; Q8BXZ1; 28-230.
DR   STRING; Q8BXZ1; -.
DR   PhosphoSite; Q8BXZ1; -.
DR   PRIDE; Q8BXZ1; -.
DR   Ensembl; ENSMUST00000025515; ENSMUSP00000025515; ENSMUSG00000024614.
DR   GeneID; 67988; -.
DR   KEGG; mmu:67988; -.
DR   UCSC; uc008fvv.1; mouse.
DR   CTD; 67988; -.
DR   MGI; MGI:2442418; Tmx3.
DR   eggNOG; roNOG10254; -.
DR   GeneTree; ENSGT00590000082864; -.
DR   InParanoid; Q8BXZ1; -.
DR   OMA; CYGICTA; -.
DR   OrthoDB; EOG444KKF; -.
DR   BRENDA; 5.3.4.1; 244.
DR   NextBio; 326146; -.
DR   ArrayExpress; Q8BXZ1; -.
DR   Bgee; Q8BXZ1; -.
DR   CleanEx; MM_TXNDC10; -.
DR   Genevestigator; Q8BXZ1; -.
DR   GermOnline; ENSMUSG00000024614; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR017936; Thioredoxin-like.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 2.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW   Glycoprotein; Isomerase; Membrane; Phosphoprotein;
KW   Redox-active center; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     29       Potential.
FT   CHAIN        30    456       Protein disulfide-isomerase TMX3.
FT                                /FTId=PRO_0000034186.
FT   TOPO_DOM     30    378       Lumenal (Potential).
FT   TRANSMEM    379    399       Helical; (Potential).
FT   TOPO_DOM    400    456       Cytoplasmic (Potential).
FT   DOMAIN       30    131       Thioredoxin.
FT   MOTIF       453    456       Di-lysine motif.
FT   MOD_RES     271    271       Phosphoserine (By similarity).
FT   CARBOHYD     35     35       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    261    261       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    316    316       N-linked (GlcNAc...) (Potential).
FT   DISULFID     56     59       Redox-active (By similarity).
SQ   SEQUENCE   456 AA;  51848 MW;  7813FC587B35B88F CRC64;
     MANAVGRRSW AALRLCAAVI LLDLAVCKGF VEDLNESFKD NRKDDIWLVD FYAPWCGHCK
     KLEPIWNEVG LEMKSIGSPV KVGKMDATSY SSIASEFGVR GYPTIKLLKG DLAYNYRGPR
     TKDDIIEFAH RVSGALIRPL PSQQMFDHVR KRHRVFFVYI GGESPLKEKY IDAASELIVY
     TYFFSASEDV VPEYVTLKEM PAVLVFKDDT YFVYDEYEDG DLSSWISRER FQNYLTMDGF
     LLYELGDTGK LVAIAVIDEK NTSLEHTRLK SIIQEVARDF RDHFHRDFQF GHMDGNDYIN
     TLLMDELTVP TIVVLNTSNQ QYFLLDRHIK DASDMVQFIN SILDGTVPAQ GGDSIFQRLK
     RIVFDAKSTI VSIFKSSPLM GCFLFGLPLG VISIMCYGIY TADTDGGYIE ERYEVSKSEM
     ENQEQIEESK EQESSSGGSL APTVQEPKDV LEKKKD
//
ID   UBP47_MOUSE             Reviewed;        1376 AA.
AC   Q8BY87; Q5EBP2; Q6KAR9; Q80V06; Q8BHU1; Q8BI15; Q8BI16; Q8BUW4;
AC   Q91X25;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 2.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 47;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 47;
DE   AltName: Full=Ubiquitin thiolesterase 47;
DE   AltName: Full=Ubiquitin-specific-processing protease 47;
GN   Name=Usp47;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-379 (ISOFORM 1),
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-591 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 637-1376 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 395-1376.
RC   TISSUE=Brain;
RX   PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of FLJ genes:
RT   the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:127-135(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 679-1376.
RC   STRAIN=Czech II; TISSUE=Brain, Liver, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-911, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1016, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   FUNCTION.
RX   PubMed=19966869; DOI=10.1038/onc.2009.430;
RA   Peschiaroli A., Skaar J.R., Pagano M., Melino G.;
RT   "The ubiquitin-specific protease USP47 is a novel beta-TRCP interactor
RT   regulating cell survival.";
RL   Oncogene 29:1384-1393(2010).
CC   -!- FUNCTION: Putative ubiquitin-specific-processing protease that
CC       regulates cell growth and survival. Probably regulates CDC25A
CC       expression at a transcriptional level. May be catalytically
CC       inactive although it seems to have kept all necessary active site
CC       residues.
CC   -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- SUBUNIT: Interacts with BTRC and FBXW11 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BY87-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BY87-2; Sequence=VSP_014416;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC27179.1; Type=Erroneous initiation;
CC       Sequence=BAC27195.1; Type=Erroneous initiation;
CC       Sequence=BAC38411.1; Type=Frameshift; Positions=109;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK030909; BAC27179.1; ALT_INIT; mRNA.
DR   EMBL; AK030963; BAC27195.1; ALT_INIT; mRNA.
DR   EMBL; AK041541; BAC30979.1; -; mRNA.
DR   EMBL; AK082114; BAC38411.1; ALT_FRAME; mRNA.
DR   EMBL; AK087981; BAC40073.1; -; mRNA.
DR   EMBL; AK131138; BAD21388.1; -; mRNA.
DR   EMBL; BC012722; AAH12722.1; -; mRNA.
DR   EMBL; BC024117; AAH24117.1; -; mRNA.
DR   EMBL; BC089364; AAH89364.1; -; mRNA.
DR   IPI; IPI00420143; -.
DR   IPI; IPI00608091; -.
DR   RefSeq; NP_598519.2; NM_133758.3.
DR   RefSeq; NP_796223.2; NM_177249.3.
DR   UniGene; Mm.16974; -.
DR   ProteinModelPortal; Q8BY87; -.
DR   SMR; Q8BY87; 182-565.
DR   MEROPS; C19.055; -.
DR   PRIDE; Q8BY87; -.
DR   Ensembl; ENSMUST00000084708; ENSMUSP00000081757; ENSMUSG00000059263.
DR   Ensembl; ENSMUST00000106653; ENSMUSP00000102264; ENSMUSG00000059263.
DR   GeneID; 74996; -.
DR   KEGG; mmu:74996; -.
DR   UCSC; uc009jgg.1; mouse.
DR   UCSC; uc009jgh.1; mouse.
DR   CTD; 74996; -.
DR   MGI; MGI:1922246; Usp47.
DR   GeneTree; ENSGT00600000084170; -.
DR   HOVERGEN; HBG058854; -.
DR   InParanoid; Q8BY87; -.
DR   OMA; FQSYKPG; -.
DR   OrthoDB; EOG4BRWJW; -.
DR   PhylomeDB; Q8BY87; -.
DR   BRENDA; 3.1.2.15; 244.
DR   NextBio; 341978; -.
DR   ArrayExpress; Q8BY87; -.
DR   Bgee; Q8BY87; -.
DR   CleanEx; MM_USP47; -.
DR   Genevestigator; Q8BY87; -.
DR   GermOnline; ENSMUSG00000059263; Mus musculus.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016566; F:specific transcriptional repressor activity; ISS:UniProtKB.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:EC.
DR   GO; GO:0034644; P:cellular response to UV; IMP:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptosis; IMP:UniProtKB.
DR   GO; GO:0043154; P:negative regulation of caspase activity; ISS:UniProtKB.
DR   GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0032582; P:negative regulation of gene-specific transcription; ISS:UniProtKB.
DR   GO; GO:0030307; P:positive regulation of cell growth; ISS:UniProtKB.
DR   GO; GO:0042493; P:response to drug; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19.
DR   Pfam; PF00443; UCH; 1.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; 1.
DR   PROSITE; PS50235; UCH_2_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Hydrolase; Phosphoprotein;
KW   Protease; Thiol protease; Ubl conjugation pathway.
FT   CHAIN         1   1376       Ubiquitin carboxyl-terminal hydrolase 47.
FT                                /FTId=PRO_0000080677.
FT   ACT_SITE    197    197       Nucleophile (By similarity).
FT   ACT_SITE    503    503       Proton acceptor (By similarity).
FT   MOD_RES     122    122       N6-acetyllysine (By similarity).
FT   MOD_RES     832    832       Phosphoserine (By similarity).
FT   MOD_RES     836    836       Phosphotyrosine (By similarity).
FT   MOD_RES     911    911       Phosphoserine.
FT   MOD_RES    1016   1016       Phosphothreonine.
FT   MOD_RES    1354   1354       Phosphoserine (By similarity).
FT   VAR_SEQ      14     33       Missing (in isoform 2).
FT                                /FTId=VSP_014416.
FT   CONFLICT    341    341       A -> G (in Ref. 1; BAC38411).
FT   CONFLICT    376    379       GLRF -> VRDL (in Ref. 1; BAC38411).
FT   CONFLICT   1178   1178       R -> H (in Ref. 1; BAC27195).
FT   CONFLICT   1200   1203       DINI -> IYNF (in Ref. 1; BAC40073).
FT   CONFLICT   1257   1257       R -> Q (in Ref. 1; BAC27195).
FT   CONFLICT   1299   1301       VST -> TRP (in Ref. 3; AAH12722).
SQ   SEQUENCE   1376 AA;  157455 MW;  09729C3B691C3709 CRC64;
     MVPGEENQLV PKEDVFWRCR QNIFDEMKKK FLQIENAAEE PRVLCIIQDT TNSKTVSERI
     TLNLPASTPV RKLFEDVANK VGYINGTFDL TRENGVTTAD MAPLDHTSDK SLLDANFEPG
     KKNFLHLTDK DGEPPQMLLE DSNNVDDSVH DRFIGPLPRE GSVASTNDYV SQNYSYSSIL
     NKSETGYVGL VNQAMTCYLN SLLQTLFMTP EFRNALYKWE FEDSEEDPVT SIPYQLQRLF
     VLLQTSKKRA IETTDVTRSF GWDSSEAWQQ HDVQELCRVM FDALEQKWKQ TEQADLINEL
     YQGKLKDYVR CLECGYEGWR IDTYLDIPLV IRPYGSSQAF ASVEEALHAF IQPEILDGPN
     QYFCERCKKK CDARKGLRFL HFPYLLTLQL KRFDFDYTTM HRIKLNDRMS FPEELDMSTF
     IDIEDEKSPQ TESCTDSGAE NEGSCHSDQM SNDFSTDDAV DEGICLESSS GSEKISKPGL
     EKNSLMYELF SVMVHSGSAA GGHYYACIKS FSDDQWYSFN DQHVSRITQE DIKKTHGGSS
     GSRGYYSSAF ASSTNAYMLI YRLKDPTRNA KFLEVDEYPE HIKNLVQKER ELEEQEKRQR
     EIERNTCKIK LFCLHPVKQV MMENKLEVHK DKTLKEAVEM AYKMMDLEDV IPLDCCRLVK
     YDEFHDYLER SYEGEEDTPM GLLLGGVKST YMFDLLLETR KPDQIFQSYK PGEVMVKVHV
     VDLKAETVAA PVTVRAYLNQ TVTEFKQLIS KATHLPADSM RIVLERCYND LRLLSMPSKT
     LKAEGFFRSN KVFVESSETV DHQAAFTDSH LWKLLDRHAN TIRLFVLLPE QSPGSYSKRT
     AYQKAGGDSG NVDDDCERVK GPAGNLKSVD AILEESTEKL KSLSLQQQQQ DGDNGDSSKS
     TETSDFENIE SPLNERGSST SVDNRELEQH IQTSDPENFQ SEERSDSDVN NDRSTSSVDS
     DILSSSHSSD TLCNADSAQI PLANGLDSHS ITSSRRTKAN EGKKETWDTA EEDSGTDSEY
     DESGKSRGDM QYMYFKADPY TADEGSGEGH KWLMVHVDKR ITLAAFKQHL EPFVGVLSSH
     FKVFRVYTSN QEFETVRLNE TLSSFSDDNK ITIRLGRALK KGEYRVKVCQ LLVNEQEPCK
     FLLDAVFAKG MTVRQSKEEL IPQLREQCGL DLSIDRFRLR KKTWKNPGTV FLDYHIYEED
     INISSNWEVF LEVLDGVEKM KSMSQLAILT RRWRPAEMKL DPFQELVLES NSVDELREKL
     SEISGIPLED IEFAKGRGTF PCDISVLDIH QDLDWNPKVS TLNVWPLYIC DDGAVIFYRD
     RTEEVMELTD EQRNELMKKE SSRLQKTGHR VTYSPRKEKA LKIYLDGAPN KDVAQD
//
ID   TAOK3_MOUSE             Reviewed;         898 AA.
AC   Q8BYC6; Q3V3B3;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 2.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Serine/threonine-protein kinase TAO3;
DE            EC=2.7.11.1;
DE   AltName: Full=Thousand and one amino acid protein 3;
GN   Name=Taok3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-561 AND 766-898.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 556-757.
RA   Ida H., Boylan S., Weigel A., Smit-McBride Z., Chao A., Gao J.,
RA   Buchoff P., Wistow G., Hjelmeland L.;
RT   "Expressed sequence tag analysis of mouse RPE/choroid.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 766-898.
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346 AND SER-349, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Inhibits the basal activity of Jun kinase. Negatively
CC       regulated by epidermal growth factor (EGF). When overexpressed,
CC       may activate ERK1/ERK2 and JNK/SAPK (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Self-associates (By similarity). Interacts with ERN1 and
CC       TRAF2. Interaction with TRAF2 is facilitated under ER stress
CC       conditions, such as treatment with tunicamycin, and may promote
CC       TRAF2 phosphorylation (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- PTM: Autophosphorylated. Phosphorylated upon DNA damage, probably
CC       by ATM or ATR (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AK040531; BAC30618.1; -; mRNA.
DR   EMBL; AK042181; BAE20625.1; -; mRNA.
DR   EMBL; CJ197745; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; CK625948; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; CO813561; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00227043; -.
DR   RefSeq; NP_001074777.1; NM_001081308.2.
DR   RefSeq; NP_001186614.1; NM_001199685.1.
DR   RefSeq; NP_899129.2; NM_183306.2.
DR   UniGene; Mm.24343; -.
DR   UniGene; Mm.248296; -.
DR   ProteinModelPortal; Q8BYC6; -.
DR   SMR; Q8BYC6; 8-315.
DR   STRING; Q8BYC6; -.
DR   PhosphoSite; Q8BYC6; -.
DR   PRIDE; Q8BYC6; -.
DR   Ensembl; ENSMUST00000092889; ENSMUSP00000090565; ENSMUSG00000061288.
DR   Ensembl; ENSMUST00000111978; ENSMUSP00000107609; ENSMUSG00000061288.
DR   GeneID; 330177; -.
DR   KEGG; mmu:330177; -.
DR   UCSC; uc008zfj.1; mouse.
DR   CTD; 330177; -.
DR   MGI; MGI:3041177; Taok3.
DR   GeneTree; ENSGT00600000084021; -.
DR   HOGENOM; HBG382294; -.
DR   HOVERGEN; HBG088996; -.
DR   InParanoid; Q8BYC6; -.
DR   OMA; NGPLNES; -.
DR   OrthoDB; EOG4THVSD; -.
DR   PhylomeDB; Q8BYC6; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 399217; -.
DR   ArrayExpress; Q8BYC6; -.
DR   Bgee; Q8BYC6; -.
DR   CleanEx; MM_TAOK3; -.
DR   Genevestigator; Q8BYC6; -.
DR   GermOnline; ENSMUSG00000061288; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Coiled coil; Cytoplasm; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    898       Serine/threonine-protein kinase TAO3.
FT                                /FTId=PRO_0000086738.
FT   DOMAIN       24    277       Protein kinase.
FT   NP_BIND      30     38       ATP (By similarity).
FT   COILED      452    502       Potential.
FT   COILED      548    649       Potential.
FT   COILED      754    871       Potential.
FT   COMPBIAS    326    329       Poly-Glu.
FT   ACT_SITE    147    147       Proton acceptor (By similarity).
FT   BINDING      53     53       ATP (By similarity).
FT   MOD_RES     316    316       Phosphothreonine (By similarity).
FT   MOD_RES     324    324       Phosphoserine.
FT   MOD_RES     346    346       Phosphoserine.
FT   MOD_RES     349    349       Phosphoserine.
FT   MOD_RES     442    442       Phosphoserine (By similarity).
SQ   SEQUENCE   898 AA;  105336 MW;  2A68F2D48906EC05 CRC64;
     MRKGALKDPE IADLFFKDDP EELFIDLHEI GHGSFGAVYF ATNAHTNEVV AVKKMSYSGK
     QTHEKWQDIL KEVKFLQQLK HPNTIEYKGC YLKEHTAWLV MEYCLGSASD LLEVHKKPLQ
     EVEIAAITHG ALQGLAYLHF HSLIHRDIKA GNILLTEPGQ VKLADFGSAS MASPANSFVG
     TPYWMAPEVI LAMDEGQYDG KVDIWSLGIT CIELAERKPP LFNMNAMSAL YHIAQNDSPT
     LQSREWTDSF RRFVDYCLHK IPQERPAAVE LLRHDFIRRE RPPKVLIDLI QRTKDAVREL
     DNLQYRKMKK ILFQETRNGP LNESQEEEED GEQGSNLNRE VDSLGSIHSI PSTSVSTGSR
     SSSVNSMQEV MDESSSELVM MQEDEGTANS SASTVHKKDH VFVRDEAGHG DPRPEPRPTQ
     SVQSRALHYR NRERFATIKS ASLVTRQIHE HEQENELREQ MSGYKRMRRQ HQKQLIALEN
     KLKAEMDEHR LKLQKEVETH ANNSSIELEK LAKKQVATIE KEAKVAAADE KKFQQQILAQ
     QKKDLTTFLE SQKKQYKICK EKIKEEMNED HSTPKKEKQE RISKHKENLQ HTQAEEEAHL
     LTQQRLYYDR NCRFFKRKIM IKRHEVEQQN IREELNKKRT QKEMEHAMLI RHDESTRELE
     YRQLHTLQKL RMDLIRLQHQ TELENQLEYN KRRERELHRK HVMELRQQPK NLKAMEMQIK
     KQFQDTCKVQ TKQYKALKNH QLEVTPKNEH KAILKTLKDE QTRKLAILAE QYEQSINEMM
     ASQALRLDEA QEAECQALRL QLQQEMELLN AYQSKIKMQT EAQHERELQK LEQRVSLRRA
     HLEQKIEEEL AALQKERSER IKTLLERQER ETETFDMESL RMGFGNLVTL DFPKEDYR
//
ID   CHD9_MOUSE              Reviewed;        2885 AA.
AC   Q8BYH8; Q7TMV5; Q8BJG8; Q8BZJ2; Q8CHG8;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Chromodomain-helicase-DNA-binding protein 9;
DE            Short=CHD-9;
DE            EC=3.6.4.12;
DE   AltName: Full=ATP-dependent helicase CHD9;
DE   AltName: Full=PPAR-alpha-interacting complex protein 320 kDa;
DE   AltName: Full=Peroxisomal proliferator-activated receptor A-interacting complex 320 kDa protein;
GN   Name=Chd9; Synonyms=Kiaa0308, Pric320;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=16554032; DOI=10.1016/j.bbrc.2006.02.160;
RA   Surapureddi S., Viswakarma N., Yu S., Guo D., Rao M.S., Reddy J.K.;
RT   "PRIC320, a transcription coactivator, isolated from peroxisome
RT   proliferator-binding protein complex.";
RL   Biochem. Biophys. Res. Commun. 343:535-543(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1104 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Diencephalon, Spinal cord, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 980-2885 (ISOFORM 2).
RC   TISSUE=Pancreatic islet;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [4]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2207-2885 (ISOFORM 1).
RC   STRAIN=C3H/He; TISSUE=Mesenchymal stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=16419031; DOI=10.1002/jcp.20586;
RA   Shur I., Socher R., Benayahu D.;
RT   "In vivo association of CReMM/CHD9 with promoters in osteogenic
RT   cells.";
RL   J. Cell. Physiol. 207:374-378(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-644, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: Acts as a transcriptional coactivator for PPARA and
CC       possibly other nuclear receptors. Proposed to be a ATP-dependent
CC       chromatin remodeling protein. Has DNA-dependent ATPase activity
CC       and binds to A/T-rich DNA (By similarity). Associates with A/T-
CC       rich regulatory regions in promoters of genes that participate in
CC       the differentiation of progenitors during osteogenesis.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Interacts with PPARA. Probably interacts with ESR1 and
CC       NR1I3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BYH8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BYH8-2; Sequence=VSP_018087;
CC   -!- TISSUE SPECIFICITY: Expressed in osteoprogenitor cells during
CC       development and in mature bone (at protein level).
CC   -!- DEVELOPMENTAL STAGE: Expressed from embryonic day 16.5 dpc in
CC       mesenchymal cartilage surrounding bone cartilage and newly formed
CC       bone trabecular spicules. Detected in bone sections of 4-day-old
CC       newborn and 3-week-old mice.
CC   -!- PTM: Phosphorylated on serine and tyrosine residues (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC   -!- SIMILARITY: Contains 2 chromo domains.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH52896.1; Type=Erroneous initiation;
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DR   EMBL; DQ127229; AAZ73184.2; -; mRNA.
DR   EMBL; AK034446; BAC28711.1; -; mRNA.
DR   EMBL; AK039562; BAC30385.1; -; mRNA.
DR   EMBL; AK084000; BAC39090.1; -; mRNA.
DR   EMBL; AB093226; BAC41410.3; -; mRNA.
DR   EMBL; BC052896; AAH52896.1; ALT_INIT; mRNA.
DR   IPI; IPI00229650; -.
DR   IPI; IPI00758139; -.
DR   RefSeq; NP_796198.1; NM_177224.2.
DR   UniGene; Mm.100615; -.
DR   ProteinModelPortal; Q8BYH8; -.
DR   SMR; Q8BYH8; 688-1403, 1673-1705, 2472-2520, 2535-2616.
DR   STRING; Q8BYH8; -.
DR   PhosphoSite; Q8BYH8; -.
DR   PRIDE; Q8BYH8; -.
DR   Ensembl; ENSMUST00000048665; ENSMUSP00000046356; ENSMUSG00000056608.
DR   Ensembl; ENSMUST00000109614; ENSMUSP00000105243; ENSMUSG00000056608.
DR   GeneID; 109151; -.
DR   KEGG; mmu:109151; -.
DR   UCSC; uc009msf.1; mouse.
DR   CTD; 109151; -.
DR   MGI; MGI:1924001; Chd9.
DR   GeneTree; ENSGT00560000077077; -.
DR   HOGENOM; HBG446013; -.
DR   HOVERGEN; HBG081150; -.
DR   InParanoid; Q8BYH8; -.
DR   OMA; TECFRVE; -.
DR   OrthoDB; EOG4548XQ; -.
DR   PhylomeDB; Q8BYH8; -.
DR   NextBio; 361700; -.
DR   ArrayExpress; Q8BYH8; -.
DR   Bgee; Q8BYH8; -.
DR   CleanEx; MM_CHD9; -.
DR   Genevestigator; Q8BYH8; -.
DR   GO; GO:0000785; C:chromatin; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006333; P:chromatin assembly or disassembly; IEA:InterPro.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR006576; BRK_domain.
DR   InterPro; IPR000953; Chromodomain.
DR   InterPro; IPR016197; Chromodomain-like.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF07533; BRK; 2.
DR   Pfam; PF00385; Chromo; 2.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00592; BRK; 2.
DR   SMART; SM00298; CHROMO; 2.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF54160; Chromodomain-like; 1.
DR   PROSITE; PS00598; CHROMO_1; FALSE_NEG.
DR   PROSITE; PS50013; CHROMO_2; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Chromatin regulator;
KW   Cytoplasm; DNA-binding; Helicase; Hydrolase; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Repeat; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   2885       Chromodomain-helicase-DNA-binding protein
FT                                9.
FT                                /FTId=PRO_0000233173.
FT   DOMAIN      689    760       Chromo 1.
FT   DOMAIN      772    838       Chromo 2.
FT   DOMAIN      871   1045       Helicase ATP-binding.
FT   DOMAIN     1185   1336       Helicase C-terminal.
FT   NP_BIND     884    891       ATP (Potential).
FT   REGION     2331   2471       Binds A/T-rich DNA (By similarity).
FT   REGION     2428   2435       A.T hook-like.
FT   MOTIF       867    871       LXXLL motif 1.
FT   MOTIF       996    999       DEAH box.
FT   MOTIF      1035   1039       LXXLL motif 2.
FT   MOTIF      2030   2034       LXXLL motif 3.
FT   MOTIF      2710   2714       LXXLL motif 4.
FT   MOTIF      2782   2787       LXXLL motif 5.
FT   MOD_RES     498    498       N6-acetyllysine (By similarity).
FT   MOD_RES     549    549       Phosphoserine (By similarity).
FT   MOD_RES     610    610       Phosphoserine (By similarity).
FT   MOD_RES     611    611       Phosphoserine (By similarity).
FT   MOD_RES     615    615       Phosphoserine (By similarity).
FT   MOD_RES     624    624       Phosphothreonine (By similarity).
FT   MOD_RES     644    644       Phosphotyrosine.
FT   MOD_RES    1467   1467       Phosphoserine (By similarity).
FT   MOD_RES    1471   1471       Phosphoserine (By similarity).
FT   MOD_RES    2025   2025       Phosphoserine (By similarity).
FT   MOD_RES    2057   2057       Phosphoserine (By similarity).
FT   MOD_RES    2058   2058       Phosphoserine (By similarity).
FT   MOD_RES    2074   2074       Phosphoserine (By similarity).
FT   MOD_RES    2078   2078       Phosphoserine (By similarity).
FT   MOD_RES    2867   2867       Phosphoserine (By similarity).
FT   MOD_RES    2871   2871       Phosphoserine (By similarity).
FT   MOD_RES    2879   2879       Phosphoserine (By similarity).
FT   VAR_SEQ    2335   2350       Missing (in isoform 2).
FT                                /FTId=VSP_018087.
FT   CONFLICT    101    101       N -> I (in Ref. 2; BAC39090).
FT   CONFLICT    584    584       Y -> D (in Ref. 2; BAC28711).
SQ   SEQUENCE   2885 AA;  323860 MW;  B820BE8EA9CC2915 CRC64;
     MTDPMMDFFD DANLFGETLE GLSDDTFVQP GPVSLVDELN LGAEFEPLHI DSLNHVQGTP
     THQKMADFEQ LSQFDSMKFH PVNQSFGSPV EHVLSPHSQF NCSPIHPPNQ PNGLFQDVAD
     GSPMWGHQTA TGLANQNGSP FHQPGHSHSL HQNKSFVAHP DFALFQASEH QTQCSSLHSQ
     QSRSNLNPGQ NSLGQAKNFL DANVSGAHRV NVNHLATAPS SQQTLPVQFS PTANPPAHFL
     KCSSHQEGNY NRPSPSMTSC SVSNSQQFPS HYSFSSGHVS PSSLLQSSAG LAPGHTNQAL
     SDFAGSNSFS PHRGMKQEPT QHLLNPTPSL NSNNFQILHS SHPQGNYSNS KLSPVHMNFP
     DPVDAGPPVG HFNDHAETNG FSSLEENLLH HVDSHAEPFA GLDPEDLLQE GLLPQFDESP
     FGQDNSNHVL DHDLDRQFTS HLVSRPSDMA QTQLQYQARG WPSPLSTNHQ HLHSRNHLCL
     QRQPPSSKKS DGSGTYTKLQ NTQVRVMSEK KPRKRVESES KQEKANRIIS EAIARAKERG
     ERNIPRVMSP ENFPSASVEG KEEKRGRRMK SKPKDRDNKK PKTYSKLKEK TKIGKLIITL
     GKKHKRRNES SDELSDAEQR SQHTFKEQHS QKRRSNRQIK RKKYAEDAEG KQSEEEVKGS
     LRVKRNSAPP PGEQPLQLFV ENPSEEDAAI VDKILACRTV KKEVSPGVML DIEEFFVKYK
     NYSYLHCEWA TEQQLLKDKR IQQKIKRFKL RQAQRAHFLA DMEEEPFNPD YVEVDRILEV
     SFCEDKDTGE SVIYYLVKWC SLPYEDSTWE LKEDVDLAKI EEFEQLQASR PDTRHLDRPP
     SNIWKKIEQS REYKNGNQLR EYQLEGLNWL LFNWYNRRNC ILADEMGLGK TIQSITFLYE
     ILLTGIRGPF LIIAPLSTIA NWEREFRTWT DINVVVYHGS LISRQMIQQY EMYFRDSQGR
     IIRGAYRFQA IITTFEMILG GCGELNAIDW RCVIIDEAHR LKNKNCKLLE GLKLMNLEHK
     VLLTGTPLQN TVEELFSLLH FLEPLRFPSE STFMQEFGDL KTEEQVQKLQ AILKPMMLRR
     LKEDVEKKLA PKEETIIEVE LTNIQKKYYR AILEKNFSFL SKGAGQTNVP NLVNTMMELR
     KCCNHPYLIK GAEEKILGEF RDTYNPSASD FHLQAMIQSA GKLVLIDKLL PKMKAGGHKV
     LIFSQMVRCL DILEDYLIHK RYLYERIDGR VRGNLRQAAI DRFSKPDSDR FVFLLCTRAG
     GLGINLTAAD TCIIFDSDWN PQNDLQAQAR CHRIGQNKAV KVYRLVTRNS YEREMFDRAS
     LKLGLDKAVL QSMSGRDSNV SGIQQLSKKE IEDLLRRGAY GAIMEEEDEG SKFCEEDIDQ
     ILLRRTKTIT IESEGRGSTF AKASFVASGN RTDISLDDPN FWQKWAKKAE LDIDTISGRN
     SLVIDTPRIR KQTRPFSATK DELAELSEAE SEGEEKPKLR RPCDRSGGYG RTECFRVEKN
     LLVYGWGRWR EILSHGRFKR QLNEHDVEVI CRALLAYCLI HYRGDEKIKG FIWDLITPTE
     DGQTRELQNH LGLSAPVPRG RKGKKVKTQT SSFDIQKAEW LRKYNPEQLL QDEGYKKHVK
     HHCNKVLLRV RMLYYLKQEV IGNESQKVFD GVDASDIDVW VPEPDHSEVP AAWWDFDADK
     SLLIGVFKHG YEKYNTIRAD PALCFLERVG KPDDKAVAAE QRANDYMDGD VEDPEYKPAP
     AIFKDDIEDD VSSPGDLVIA DGEGQLMEGD KVYWPTPSAL TTRLRRLITA YQRTNKNRHI
     QQMQPTFSLP ANAMQPLYEE ATLNPKMAAK IERQQRWTRR EEADFYRVVS TFGVVFDPDR
     GQFDWTKFRA LARLHKKTDN SLEKYLCAFM SMCRRVCRLP SKEELVDPNI FIQPITEERA
     SRTLYRIELL RKVREQALRH PQLFERLKLC HPNPDLPIWW ECGSHDRDLL IGAAKHGVSR
     TDYHILRDPE LSFMAAQRNY NQSKAAHSRT SAPLLQQYQV ALSASPLTSL PRLLGAKGTL
     LEDMKVKSES LTEEPQSSEE ESMSSMETRT RVKSEPVSPK NGVLSQATGD QKSGGKSETD
     RRMVAARTEP LTPNPASKKP RVHKRGSQSS SDSDSDSARS SCSSRSSSSS SSSSSCSHSR
     SGSSSSSSSS CSSASSSSSS SSSSSSSSSS SSSEESDSEE DVQKREGTPH RKAYDEESVA
     SLSTTQDETQ DSFQANNGTP ESAYLLQGGY MLAASYWPKD RVMINRLDSI CQTVLKGKWP
     SARRHYDANT VASFYTTKLL DSPGAATERG EPSVPTPPAV AVREEHEQSA QMSKVKKHVR
     EKEFTVKIKD EGGLKLTFQK QGLAQKRPFD GEDGALGQQQ YLTRLRELQS TSETSLVNLP
     KAVPASGTSI QPTLGANGAI LDSQPIVKKR RGRRRNVEGA DILFLNRNKP PNHIPTGMNP
     ALSYPQPQRI PDTESPVPVI NLKDGTRLAG DDAPKRKDLD RWLKEHPGYV EDLGAFIPRV
     QLHEGRPKQK RHRCRNPNKL DINSLTGEER VQLINRRNAR KVGGAFAPPL KDLCRFLKEN
     SEYGVAPEWG DVVKQSGFLP ESMFERILTG PVVREEVSRR GRRPKSGIAK ATTAAAVPAG
     SVPGNPLLAN GLLPGVDLTA LQALQQNLQN LQSLQVTAGL MGMPAGLSSG GETKNMAAMF
     PMLFSGMAGL PNLLGMGGLL SKTAESGAEE KRGNDSKELE GKKERTESQS PENGGERCVP
     GSPSTSSTAA LSSAAAAKPI ALNPLLLSNI LYPGMLLTPG LNLHLPTLSQ SNAFDVQKNK
     SDDLDSSKSV EIKEENSRVR DQEEKGGTEP SPLNENSTDE GSERASSGSD SSSSSSEDSD
     SSNED
//
ID   K1467_MOUSE             Reviewed;         624 AA.
AC   Q8BYI8; Q3TE07; Q5DTX5; Q8BYJ4; Q9CXB0;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Uncharacterized protein KIAA1467;
GN   Name=Kiaa1467;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Lung, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 92-624.
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BYI8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BYI8-2; Sequence=VSP_025825;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the ITFG3 family.
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DR   EMBL; AK018428; BAB31206.1; -; mRNA.
DR   EMBL; AK039348; BAC30325.1; -; mRNA.
DR   EMBL; AK039401; BAC30340.1; -; mRNA.
DR   EMBL; AK169892; BAE41441.1; -; mRNA.
DR   EMBL; AK220395; BAD90448.1; -; mRNA.
DR   IPI; IPI00466999; -.
DR   IPI; IPI00851005; -.
DR   RefSeq; NP_083258.2; NM_028982.4.
DR   UniGene; Mm.34182; -.
DR   ProteinModelPortal; Q8BYI8; -.
DR   PhosphoSite; Q8BYI8; -.
DR   PRIDE; Q8BYI8; -.
DR   Ensembl; ENSMUST00000087740; ENSMUSP00000085033; ENSMUSG00000030207.
DR   Ensembl; ENSMUST00000111915; ENSMUSP00000107546; ENSMUSG00000030207.
DR   GeneID; 74525; -.
DR   KEGG; mmu:74525; -.
DR   UCSC; uc009eli.1; mouse.
DR   MGI; MGI:1921775; 8430419L09Rik.
DR   eggNOG; roNOG05273; -.
DR   GeneTree; ENSGT00530000063694; -.
DR   HOVERGEN; HBG101158; -.
DR   OMA; PGKKSPD; -.
DR   OrthoDB; EOG451DQT; -.
DR   NextBio; 341016; -.
DR   ArrayExpress; Q8BYI8; -.
DR   Bgee; Q8BYI8; -.
DR   CleanEx; MM_8430419L09RIK; -.
DR   Genevestigator; Q8BYI8; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR011047; Quino_AlcDH-like.
DR   Gene3D; G3DSA:2.140.10.10; Quinoprotein_alc_DH-like; 2.
DR   SUPFAM; SSF50998; Quin_alc_DH_like; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    624       Uncharacterized protein KIAA1467.
FT                                /FTId=PRO_0000288914.
FT   TRANSMEM    107    127       Helical; (Potential).
FT   MOD_RES      16     16       Phosphoserine (By similarity).
FT   MOD_RES      22     22       Phosphotyrosine (By similarity).
FT   MOD_RES      30     30       Phosphoserine (By similarity).
FT   MOD_RES      33     33       Phosphoserine (By similarity).
FT   MOD_RES      63     63       Phosphoserine (By similarity).
FT   VAR_SEQ     624    624       I -> AGEMAQCVLAKPGYLNLIPWPHMLEGGNGVLHTVL
FT                                (in isoform 2).
FT                                /FTId=VSP_025825.
FT   CONFLICT    250    250       N -> D (in Ref. 2; BAD90448).
FT   CONFLICT    419    419       T -> M (in Ref. 2; BAD90448).
FT   CONFLICT    544    544       I -> V (in Ref. 1; BAB31206).
SQ   SEQUENCE   624 AA;  67031 MW;  2C377FE4B3A2F17E CRC64;
     MATVLSRALK LPGKKSPDLG EYDPLTQADS DESEDDLVLN LQQKNGGVKN GKSALGDLPE
     PDSDADVAGA AKPHLSEVTP EGFPSEPLGG LEQKATSPLV SYVRTSVFLL TLVISMVLVL
     LCAFLIPCPP RDLHSAWSRR LGSQGGGDLS PLELADVNRD GLRDVLLTFV TTRNGTEGGV
     GSQPTADLVC LSGMNGSTLW SSPLPEEAQD VTCLDLIPGS VAKTICLVTG TRKMLSAFNA
     TSGKVLWTLN PNHLSNGTLA APVVVLPDLD EDGVRDLVVL AIGELQPDLC FLLVSGRTGS
     PVGRPVKYNI VGVGNLIGPQ VYITASGAVY ILFGFGNIQA VALRDIFVQA QNRDSSPPSL
     QIEEPEWEKH RSVNLSELID VYSDGVELLQ LVKAPDSNSS SLLITTRQGL VLLRGQDLTP
     HWKLNLQGLR SQPTPGYFTD DQTLDFLLQT QDGDGMKKMT VVDGGSGSIV WSYSIPCHMK
     ETPTTSAITS DQKSVFLFWA EALTAASLSS DDSSGAEPPG LYHLYLLHPA FPSILLDLSN
     TTGIVTASEV GINDIWKDAF YVTRTTGMSP EGHPTSLVVS KLSLRWALME GQMVQLKETT
     PKIGRGELRR FLSRIKFVDS PYQI
//
ID   TENR_MOUSE              Reviewed;        1358 AA.
AC   Q8BYI9; O88717;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Tenascin-R;
DE            Short=TN-R;
DE   AltName: Full=Janusin;
DE   AltName: Full=Neural recognition molecule J1-160/180;
DE   AltName: Full=Restrictin;
DE   Flags: Precursor;
GN   Name=Tnr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-24.
RC   TISSUE=Brain;
RX   MEDLINE=99274730; PubMed=10341229;
RA   Weber P., Bartsch U., Rasband M.N., Czaniera R., Lang Y.,
RA   Bluethmann H., Margolis R.U., Levinson S.R., Shrager P., Montag D.;
RT   "Mice deficient for tenascin-r display alterations of the
RT   extracellular matrix and decreased axonal conduction velocities in the
RT   CNS.";
RL   J. Neurosci. 19:4245-4262(1999).
RN   [3]
RP   TISSUE SPECIFICITY, ALTERNATIVE SPLICING, AND DEVELOPMENTAL STAGE.
RX   PubMed=2477380; DOI=10.1083/jcb.109.4.1765;
RA   Pesheva P., Spiess E., Schachner M.;
RT   "J1-160 and J1-180 are oligodendrocyte-secreted nonpermissive
RT   substrates for cell adhesion.";
RL   J. Cell Biol. 109:1765-1778(1989).
RN   [4]
RP   INTERACTION WITH CNTN1, AND FUNCTION.
RX   MEDLINE=93152173; PubMed=7678967; DOI=10.1016/0896-6273(93)90243-K;
RA   Pesheva P., Gennarini G., Goridis C., Schachner M.;
RT   "The F3/11 cell adhesion molecule mediates the repulsion of neurons by
RT   the extracellular matrix glycoprotein J1-160/180.";
RL   Neuron 10:69-82(1993).
RN   [5]
RP   FUNCTION, AND BINDING TO MEMBRANE SURFACE SULFATIDES OF
RP   OLIGODENDROCYTES.
RX   PubMed=9169525;
RA   Pesheva P., Gloor S., Schachner M., Probstmeier R.;
RT   "Tenascin-R is an intrinsic autocrine factor for oligodendrocyte
RT   differentiation and promotes cell adhesion by a sulfatide-mediated
RT   mechanism.";
RL   J. Neurosci. 17:4642-4651(1997).
RN   [6]
RP   FUNCTION, AND BINDING TO MEMBRANE SURFACE GANGLIOSIDES OF
RP   OLIGODENDROCYTES.
RX   PubMed=10383637; DOI=10.1046/j.1460-9568.1999.00670.x;
RA   Probstmeier R., Michels M., Franz T., Chan B.M.C., Pesheva P.;
RT   "Tenascin-R interferes with integrin-dependent oligodendrocyte
RT   precursor cell adhesion by a ganglioside-mediated signalling
RT   mechanism.";
RL   Eur. J. Neurosci. 11:2474-2488(1999).
RN   [7]
RP   GLYCOSYLATION.
RX   PubMed=10406848; DOI=10.1093/glycob/9.8.823;
RA   Zamze S., Harvey D.J., Pesheva P., Mattu T.S., Schachner M.,
RA   Dwek R.A., Wing D.R.;
RT   "Glycosylation of a CNS-specific extracellular matrix glycoprotein,
RT   tenascin-R, is dominated by O-linked sialylated glycans and 'brain-
RT   type' neutral N-glycans.";
RL   Glycobiology 9:823-831(1999).
RN   [8]
RP   GLYCOSYLATION, INTERACTION WITH FN1 AND TNC, AND FUNCTION.
RX   PubMed=10773191; DOI=10.1016/S0006-8993(00)02075-8;
RA   Probstmeier R., Braunewell K.-H., Pesheva P.;
RT   "Involvement of chondroitin sulfates on brain-derived tenascin-R in
RT   carbohydrate-dependent interactions with fibronectin and tenascin-C.";
RL   Brain Res. 863:42-51(2000).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-724, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Neural extracellular matrix (ECM) protein involved in
CC       interactions with different cells and matrix components. Theses
CC       interactions can influence cellular behavior by either evoking a
CC       stable adhesion and differentiation, or repulsion and inhibition
CC       of neurite growth. Binding to cell surface gangliosides inhibits
CC       RGD-dependent integrin-mediated cell adhesion and results in an
CC       inhibition of PTK2 (FAK) phosphorylation and cell detachment.
CC       Binding to membrane surface sulfatides results in a
CC       oligodendrocyte adhesion and differentiation. Interaction with
CC       CNTN1 induces a repulsion of neurons and an inhibition of neurite
CC       outgrowth. Interacts with SCN2B may play a crucial role in
CC       clustering and regulation of activity of sodium channels at nodes
CC       of Ranvier. TNR-linked chondroitin sulfate glycosaminoglycans are
CC       involved in the interaction with FN1 and mediates inhibition of
CC       cell adhesion and neurite outgrowth. The highly regulated addition
CC       of sulfated carbohydrate structure may modulate the adhesive
CC       properties of TNR over the course of development and during
CC       synapse maintenance (By similarity).
CC   -!- SUBUNIT: Interacts with BCAN and AGC1 in a calcium-dependent
CC       manner. Interacts with SCN2B, PTPRZ1, and CSPG3 (By similarity).
CC       Forms oligomers. Isoforms 1 and 2 form respectively trimeric
CC       (tribrachion) and dimeric kink-armed rodlike structures, which are
CC       linked by disulfide bridges. Interacts with CNTN1, TNC and FN1.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=J1-180, TN-R 180;
CC         IsoId=Q8BYI9-1; Sequence=Displayed;
CC       Name=2; Synonyms=J1-160, TN-R 160;
CC         IsoId=Q8BYI9-2; Sequence=VSP_012994;
CC   -!- TISSUE SPECIFICITY: Brain-specific.
CC   -!- DEVELOPMENTAL STAGE: Isoform 1 is barely detectable at E17 embryo
CC       and increases in intensity until postnatal day 15, when it reaches
CC       adult levels. Isoform 2 is detectable from postnatal day 5 and
CC       reaches adult levels also at postnatal day 15.
CC   -!- DOMAIN: The EGF-like domains mediate interaction with CNTN1. The
CC       fibronectin type-III domains 3-5 mediate interaction with BCAN.
CC       The fibronectin type-III domains 1-2 and 7-9 mediate interaction
CC       with SCN2B (By similarity).
CC   -!- PTM: Contains N-linked oligosaccharides with a sulfated
CC       carbohydrate structures (By similarity). Contains N-linked
CC       oligosaccharides, O-linked sialylated structures and O-linked
CC       chondroitin sulfate glycosaminoglycans.
CC   -!- MISCELLANEOUS: Knockout mice display alterations of the
CC       extracellular matrix, and decreased axonal conduction velocities
CC       in the CNS.
CC   -!- SIMILARITY: Belongs to the tenascin family.
CC   -!- SIMILARITY: Contains 5 EGF-like domains.
CC   -!- SIMILARITY: Contains 1 fibrinogen C-terminal domain.
CC   -!- SIMILARITY: Contains 9 fibronectin type-III domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK039390; BAC30335.1; -; mRNA.
DR   EMBL; AJ005844; CAA06739.1; -; mRNA.
DR   IPI; IPI00227126; -.
DR   IPI; IPI00553593; -.
DR   RefSeq; NP_071707.2; NM_022312.3.
DR   UniGene; Mm.444966; -.
DR   UniGene; Mm.44701; -.
DR   ProteinModelPortal; Q8BYI9; -.
DR   SMR; Q8BYI9; 171-1343.
DR   STRING; Q8BYI9; -.
DR   PhosphoSite; Q8BYI9; -.
DR   PRIDE; Q8BYI9; -.
DR   Ensembl; ENSMUST00000040797; ENSMUSP00000039253; ENSMUSG00000015829.
DR   Ensembl; ENSMUST00000111669; ENSMUSP00000107298; ENSMUSG00000015829.
DR   GeneID; 21960; -.
DR   KEGG; mmu:21960; -.
DR   UCSC; uc007dea.1; mouse.
DR   CTD; 21960; -.
DR   MGI; MGI:99516; Tnr.
DR   GeneTree; ENSGT00580000081396; -.
DR   HOGENOM; HBG714000; -.
DR   HOVERGEN; HBG008949; -.
DR   InParanoid; Q8BYI9; -.
DR   OrthoDB; EOG42FSGP; -.
DR   NextBio; 301652; -.
DR   ArrayExpress; Q8BYI9; -.
DR   Bgee; Q8BYI9; -.
DR   CleanEx; MM_TNR; -.
DR   Genevestigator; Q8BYI9; -.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0045121; C:membrane raft; IDA:MGI.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:MGI.
DR   GO; GO:0005102; F:receptor binding; IEA:InterPro.
DR   GO; GO:0046625; F:sphingolipid binding; TAS:MGI.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR002181; Fibrinogen_a/b/g_C.
DR   InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR   InterPro; IPR014715; Fibrinogen_a/b/g_C_2.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Gene3D; G3DSA:3.90.215.10; Fibrinogen_a/b/g_C_1; 1.
DR   Gene3D; G3DSA:4.10.530.10; Fibrinogen_a/b/g_C_2; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 9.
DR   Pfam; PF07974; EGF_2; 4.
DR   Pfam; PF00147; Fibrinogen_C; 1.
DR   Pfam; PF00041; fn3; 9.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00186; FBG; 1.
DR   SMART; SM00060; FN3; 9.
DR   SUPFAM; SSF56496; Fibrinogen_a/b/g_C; 1.
DR   SUPFAM; SSF49265; FN_III-like; 9.
DR   PROSITE; PS00022; EGF_1; 5.
DR   PROSITE; PS01186; EGF_2; 4.
DR   PROSITE; PS50026; EGF_3; FALSE_NEG.
DR   PROSITE; PS00514; FIBRINOGEN_C_1; FALSE_NEG.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR   PROSITE; PS50853; FN3; 9.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Coiled coil; Disulfide bond;
KW   EGF-like domain; Extracellular matrix; Glycoprotein; Phosphoprotein;
KW   Proteoglycan; Repeat; Secreted; Sialic acid; Signal.
FT   SIGNAL        1     31       Potential.
FT   CHAIN        32   1358       Tenascin-R.
FT                                /FTId=PRO_0000007748.
FT   DOMAIN      188    199       EGF-like 1.
FT   DOMAIN      219    230       EGF-like 2.
FT   DOMAIN      250    261       EGF-like 3.
FT   DOMAIN      281    292       EGF-like 4.
FT   DOMAIN      312    323       EGF-like 5.
FT   DOMAIN      325    413       Fibronectin type-III 1.
FT   DOMAIN      414    502       Fibronectin type-III 2.
FT   DOMAIN      503    592       Fibronectin type-III 3.
FT   DOMAIN      593    684       Fibronectin type-III 4.
FT   DOMAIN      685    772       Fibronectin type-III 5.
FT   DOMAIN      773    862       Fibronectin type-III 6.
FT   DOMAIN      863    951       Fibronectin type-III 7.
FT   DOMAIN      952   1039       Fibronectin type-III 8.
FT   DOMAIN     1040   1127       Fibronectin type-III 9.
FT   DOMAIN     1129   1344       Fibrinogen C-terminal.
FT   COILED      127    157       Potential.
FT   COMPBIAS    155    314       Cys-rich.
FT   MOD_RES     724    724       Phosphoserine.
FT   CARBOHYD     55     55       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    180    180       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    198    198       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    278    278       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    392    392       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    470    470       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    581    581       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    791    791       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    869    869       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    874    874       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1036   1036       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1046   1046       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1261   1261       N-linked (GlcNAc...) (Potential).
FT   DISULFID    297    307       By similarity.
FT   DISULFID    314    323       By similarity.
FT   VAR_SEQ     773    862       Missing (in isoform 2).
FT                                /FTId=VSP_012994.
SQ   SEQUENCE   1358 AA;  149563 MW;  C0EA4AC5AEE4433B CRC64;
     MGIDGETVVL KNMLIGVNLI LLGSMLKPSE CRLEVTTERA QRQTVEEEGG ASSHNTSSKE
     QPMVFNHVYN INVPLESLCS SGLEASAEQD MSAEDDTLAE YIGQTSDHES QVTFTHKINL
     PKKACPCASS SQVLQELLSR IEMLEREVSL LRDQCNTNCC QESAATGQLD YVPHCSGHGN
     FSFESCGCIC NEGWFGKNCS EPYCPLGCSS RGVCVDGQCI CDSEYSGDDC SELRCPTDCS
     SRGLCVDGEC VCEEPYTGED CRELRCPGDC SGKGQCANGT CLCQEGYAGE DCSQRRCLNA
     CSGRGHCQEG LCICEEGYQG PDCSAVAPPE DLRVAGISDR SIELEWDGPM AVTEYVISYQ
     PTALGGLQLQ QRVPGDWSGV TIMELEPGLT YNISVYAVIS NILSLPITAK VATHLSTPQG
     LQFKTITETT VEVQWEPFSF SFDGWEISFI PKNNEGGVIA QLPSDVTSFN QTGLKPGEEY
     IVNVVALKEQ ARSPPTSASV STVIDGPTQI LVRDVSDTVA FVEWTPPRAK VDFILLKYGL
     VGGEGGKTTF RLQPPLSQYS VQALRPGSRY EVSISAVRGT NESEASSTQF TTEIDAPKNL
     RVGSRTATSL DLEWDNSEAE AQEYKVVYST LAGEQYHEVL VPKGIGPTTK TTLTDLVPGT
     EYGVGISAVM NSKQSIPATM NARTELDSPR DLMVTASSET SISLIWTKAS GPIDHYRITF
     TPSSGISSEV TVPRDRTSYT LTDLEPGAEY IISITAERGR QQSLESTVDA FTGFRPISHL
     HFSHVTSSSV NITWSDPSPP ADRLILNYSP RDKEEDMLEV LLDATKRHAV LMGLQPATEY
     IVNLVAVHGT VTSEPIVGSI TTGIDPPKNI TISNVTKDSL TVSWSSPVAP FDYYRVSYRP
     TQVGRLDSSV VPNTVTEFAI TRLYPATEYE ISLNSVRGRE ESERICTLVH TAMDSPMDLI
     ATNITPTEAL LQWKAPMGEV ENYVIVLTHF AIAGETILVD GVSEEFQLVD LLPSTHYTVT
     MYATSGPLMS GTIATNFSTL LDPPDNLTAS EVTRQSALIS WQPPRAAIEN YVLTYKSTDG
     SRKELIVDAE DTWIRLEGLS ENTDYTVLLQ AAQEATRSSL TSTVFTTGGR VFSHPQDCAQ
     HLMNGDTLSG VYTIFLNGEL SHKLQVYCDM TTDGGGWIVF QRRQNGQTDF FRKWADYRVG
     FGNLEDEFWL GLDNIHRITA QGRYELRVDM RDGQEAVFAY YDKFAVEDSR SLYKIRIGSY
     NGTAGDSLSY HQGRPFSTED RDNDVAVTNC AMSYKGAWWY KNCHRTNLNG KYGESRHSQG
     INWYHWKGHE FSIPFVEMKM RPYIHRLTAG RKRRALKF
//
ID   TBCD4_MOUSE             Reviewed;        1307 AA.
AC   Q8BYJ6; Q149C0; Q149C1; Q3T9E8; Q3TAQ5; Q5DU23; Q66JU2; Q6P2M2;
AC   Q8BMH6; Q8BXM2;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=TBC1 domain family member 4;
DE   AltName: Full=Akt substrate of 160 kDa;
DE            Short=AS160;
GN   Name=Tbc1d4; Synonyms=As160, Kiaa0603;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-840 (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Forelimb, Retina, Spinal cord, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-844 (ISOFORM 2).
RC   STRAIN=NMRI; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 289-1307 (ISOFORM 2).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PHOSPHORYLATION AT SER-595 AND THR-649, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RX   MEDLINE=22063368; PubMed=11994271; DOI=10.1074/jbc.C200198200;
RA   Kane S., Sano H., Liu S.C.H., Asara J.M., Lane W.S., Garner C.C.,
RA   Lienhard G.E.;
RT   "A method to identify serine kinase substrates. Akt phosphorylates a
RT   novel adipocyte protein with a Rab GTPase-activating protein (GAP)
RT   domain.";
RL   J. Biol. Chem. 277:22115-22118(2002).
RN   [5]
RP   PHOSPHORYLATION AT SER-324; SER-348; SER-577; SER-595; THR-649 AND
RP   SER-758.
RX   MEDLINE=22590501; PubMed=12637568; DOI=10.1074/jbc.C300063200;
RA   Sano H., Kane S., Sano E., Miinea C.P., Asara J.M., Lane W.S.,
RA   Garner C.W., Lienhard G.E.;
RT   "Insulin-stimulated phosphorylation of a Rab GTPase-activating protein
RT   regulates GLUT4 translocation.";
RL   J. Biol. Chem. 278:14599-14602(2003).
RN   [6]
RP   EFFECT ON GLUT4 TRANSLOCATION.
RX   PubMed=15254270; DOI=10.1091/mbc.E04-04-0333;
RA   Zeigerer A., McBrayer M.K., McGraw T.E.;
RT   "Insulin stimulation of GLUT4 exocytosis, but not its inhibition of
RT   endocytosis, is dependent on RabGAP AS160.";
RL   Mol. Biol. Cell 15:4406-4415(2004).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=18276765; DOI=10.2337/db07-1469;
RA   Bouzakri K., Ribaux P., Tomas A., Parnaud G., Rickenbach K.,
RA   Halban P.A.;
RT   "Rab GTPase-activating protein AS160 is a major downstream effector of
RT   protein kinase B/Akt signaling in pancreatic beta-cells.";
RL   Diabetes 57:1195-1204(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May act as a GTPase-activating protein for RAB2A, RAB8A,
CC       RAB10 and RAB14. Promotes insulin-induced glucose transporter
CC       SLC2A4/GLUT4 translocation at the plasma membrane, thus increasing
CC       glucose uptake (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Cytoplasmic perinuclear (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q8BYJ6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BYJ6-2; Sequence=VSP_013891, VSP_036876, VSP_036878;
CC       Name=3;
CC         IsoId=Q8BYJ6-3; Sequence=VSP_036874, VSP_036876, VSP_036878;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q8BYJ6-4; Sequence=VSP_036873, VSP_013891, VSP_036876,
CC                                  VSP_036878;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q8BYJ6-5; Sequence=VSP_036872, VSP_036875, VSP_036877;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Widely expressed, including in pancreatic beta
CC       cells.
CC   -!- PTM: Phosphorylated by AKT1; insulin-induced.
CC   -!- PTM: Insulin-stimulated phosphorylation is required for GLUT4
CC       translocation. Has no effect on GLUT4 internalization.
CC   -!- SIMILARITY: Contains 2 PID domains.
CC   -!- SIMILARITY: Contains 1 Rab-GAP TBC domain.
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DR   EMBL; AK039337; BAC30322.2; -; mRNA.
DR   EMBL; AK044719; BAC32048.1; -; mRNA.
DR   EMBL; AK031120; BAC27263.1; -; mRNA.
DR   EMBL; AK171689; BAE42613.1; -; mRNA.
DR   EMBL; AK172575; BAE43074.1; -; mRNA.
DR   EMBL; BC064433; AAH64433.1; -; mRNA.
DR   EMBL; BC080762; AAH80762.1; -; mRNA.
DR   EMBL; BC117869; AAI17870.1; -; mRNA.
DR   EMBL; BC117870; AAI17871.1; -; mRNA.
DR   EMBL; AK220347; BAD90243.1; -; mRNA.
DR   IPI; IPI00675197; -.
DR   IPI; IPI00761281; -.
DR   IPI; IPI00874756; -.
DR   IPI; IPI00928118; -.
DR   IPI; IPI00928545; -.
DR   RefSeq; NP_001074747.2; NM_001081278.2.
DR   UniGene; Mm.320639; -.
DR   ProteinModelPortal; Q8BYJ6; -.
DR   SMR; Q8BYJ6; 367-445, 900-1191.
DR   STRING; Q8BYJ6; -.
DR   PhosphoSite; Q8BYJ6; -.
DR   PRIDE; Q8BYJ6; -.
DR   Ensembl; ENSMUST00000110795; ENSMUSP00000106422; ENSMUSG00000033083.
DR   Ensembl; ENSMUST00000110796; ENSMUSP00000106423; ENSMUSG00000033083.
DR   GeneID; 210789; -.
DR   KEGG; mmu:210789; -.
DR   UCSC; uc007uvm.1; mouse.
DR   CTD; 210789; -.
DR   MGI; MGI:2429660; Tbc1d4.
DR   eggNOG; roNOG04059; -.
DR   GeneTree; ENSGT00550000074196; -.
DR   HOVERGEN; HBG059376; -.
DR   OrthoDB; EOG498V01; -.
DR   PhylomeDB; Q8BYJ6; -.
DR   NextBio; 373057; -.
DR   ArrayExpress; Q8BYJ6; -.
DR   Bgee; Q8BYJ6; -.
DR   CleanEx; MM_TBC1D4; -.
DR   Genevestigator; Q8BYJ6; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005097; F:Rab GTPase activator activity; IEA:InterPro.
DR   GO; GO:0032313; P:regulation of Rab GTPase activity; IEA:InterPro.
DR   InterPro; IPR021785; DUF3350.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   InterPro; IPR000195; RabGAP/TBC_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Pfam; PF11830; DUF3350; 1.
DR   Pfam; PF00640; PID; 2.
DR   Pfam; PF00566; TBC; 1.
DR   SMART; SM00462; PTB; 2.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; RabGAP_TBC; 2.
DR   PROSITE; PS01179; PID; 1.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; GTPase activation;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1   1307       TBC1 domain family member 4.
FT                                /FTId=PRO_0000208027.
FT   DOMAIN       53    209       PID 1.
FT   DOMAIN      319    475       PID 2.
FT   DOMAIN      927   1121       Rab-GAP TBC.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     324    324       Phosphoserine; by PKB/AKT1.
FT   MOD_RES     348    348       Phosphoserine; by PKB/AKT1.
FT   MOD_RES     351    351       Phosphoserine (By similarity).
FT   MOD_RES     484    484       N6-acetyllysine (By similarity).
FT   MOD_RES     573    573       Phosphoserine (By similarity).
FT   MOD_RES     575    575       Phosphothreonine (By similarity).
FT   MOD_RES     577    577       Phosphoserine; by PKB/AKT1.
FT   MOD_RES     595    595       Phosphoserine; by PKB/AKT1.
FT   MOD_RES     598    598       Phosphoserine (By similarity).
FT   MOD_RES     649    649       Phosphothreonine; by PKB/AKT1.
FT   MOD_RES     673    673       Phosphoserine (By similarity).
FT   MOD_RES     756    756       Phosphothreonine (By similarity).
FT   MOD_RES     758    758       Phosphoserine; by PKB/AKT1.
FT   MOD_RES     759    759       Phosphothreonine (By similarity).
FT   MOD_RES     764    764       Phosphoserine (By similarity).
FT   MOD_RES     773    773       Phosphothreonine (By similarity).
FT   VAR_SEQ       1    793       Missing (in isoform 5).
FT                                /FTId=VSP_036872.
FT   VAR_SEQ     508    508       Missing (in isoform 4).
FT                                /FTId=VSP_036873.
FT   VAR_SEQ     685    747       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_013891.
FT   VAR_SEQ     685    739       Missing (in isoform 3).
FT                                /FTId=VSP_036874.
FT   VAR_SEQ     794    802       SPSAMQQQK -> MPLTVFFSA (in isoform 5).
FT                                /FTId=VSP_036875.
FT   VAR_SEQ     873    873       E -> G (in isoform 2, isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_036876.
FT   VAR_SEQ     873    873       Missing (in isoform 5).
FT                                /FTId=VSP_036877.
FT   VAR_SEQ     874   1307       Missing (in isoform 2, isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_036878.
FT   CONFLICT    171    171       I -> V (in Ref. 1; BAC30322).
FT   CONFLICT    631    631       H -> Y (in Ref. 1; BAC30322).
FT   CONFLICT    840    840       E -> A (in Ref. 1; BAC30322).
FT   CONFLICT    840    840       E -> K (in Ref. 2; AAH64433).
FT   CONFLICT    844    844       S -> K (in Ref. 2; AAH80762).
FT   CONFLICT    880    880       Q -> L (in Ref. 1; BAE42613).
FT   CONFLICT    914    914       R -> K (in Ref. 1; BAE42613).
FT   CONFLICT    974    974       A -> T (in Ref. 1; BAE42613).
SQ   SEQUENCE   1307 AA;  147451 MW;  60B37CC6ED1D2F55 CRC64;
     MESPSCIQDE PFPHPLEPEP SAPAQPGATK PGDKRFRLWY VGGSCLDRRT TLPMLPWLMA
     EIRRRSQKPD AGGCGAPAAR EVILVLSAPF LRCVPAPGAG VGGGAGSGAV QPNTGVFIFE
     HKAQHISRFI HNSHDLTYFA YLIKAQPDDP ESQMACHVFR ATDPNQVPDV ISSIRQLSKA
     AMKEDSKPSK DNEDAFYNSQ KFEVLYCGRV IVTHKKAPSS LIDDCKDKFS LHEQQRLKLQ
     GERGGDPGDE MGVLEVESPV SPDDSLPEKA DGTVNSPRAL PSLASLPALA SQPALASSRV
     CFPERILEDC GFDEQQEFRS RCSSVTGVMQ KKVHENNQKT QPRRRHASAP SHVQPSDSEK
     NRTMLFQVGR FEINLISPDT KSVVLEKNFK DISSCSQGIK HVDHFGFICR ESPEPGLSQY
     ICYVFQCANE SLVDEVMLTL KQAFSTAAAL QSAKTQIKLC ETCPMHSLHK LCERIEGLYP
     PRAKLVIQRH LSSLTDNEQA DIFERVQKMK PISDQEENEL VILHLRQLCE AKQRTHVHIG
     EGPAIISNST IPENVTSGGR FKLDVLKNKA KRSLTSSLEN IFSRGANRMR GRLGSMDSFE
     RANSLASEKD FSPGDSPPGT PPASPLSSAW HAFPEEDSDS PQFRRRAHTF SHPPSSSRRK
     LNLQDGKAHG LRSPLLRQSS SEQCSIVPSA RRMYKESNSS CSLPSLHTSF SAPSFTAPSF
     LKSFYQNSGR LSPQYENEIR QDTASESSDG EGRKRTSSTC SNESLNAGGT PVTPRRVSWR
     QRIFLRVASP VNKSPSAMQQ QKDGLDRTEL LPLSPLSPTM EEEPLIIFLS GDEDTEKVEE
     KKKSKELKSL WKKAIHQQIL LLRMEKENQK LEEARRDELQ SRKVKLDYEE VGTCQKEILI
     AWDKKLLNCR TKIRCDMEDI HTSLKEGVPK SRRGEIWQFL ALQYRLRHRL PNKHQPPDTS
     YKELLKQLTA QQHAILVDLG RTFPTHPYFS VQLGAGQLSL FNLLKAYSLL DKEVGYCQGI
     SFVAGVLLLH MSEEQAFEML KFLMYDLGFR KQYRPDMMSL QIQMYQLSRL LHDYHRELYN
     HLEENEISPS LYAAPWFLTL FASQFPLGFV ARVFDIIFLQ GTEVIFKVAL SLLSSQEALI
     MECENFENIV EFLKSTLPDM NTTEMEKIIT QVFEMDISKQ LHAYEVEYHV LQDELLESSY
     ACEDNESLEK LERANNQLKR QNMDLLEKLQ VAHAKIQALE SNLETLLTRE TKMKALIRTL
     EQDKMAYQKT VEQIRKLLPA DALANCELLL KDLTHPTNDK AKAGNKP
//
ID   PHAR3_MOUSE             Reviewed;         558 AA.
AC   Q8BYK5; Q8BYS8; Q8C058; Q9DB87;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2003, sequence version 2.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Phosphatase and actin regulator 3;
DE   AltName: Full=Scaffold-associated PP1-inhibiting protein;
DE            Short=Scapinin;
GN   Name=Phactr3; Synonyms=Scapin1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH PPP1CA
RP   AND ACTIN.
RC   STRAIN=C57BL/6;
RX   PubMed=15107502; DOI=10.1073/pnas.0401673101;
RA   Allen P.B., Greenfield A.T., Svenningsson P., Haspeslagh D.C.,
RA   Greengard P.;
RT   "Phactrs 1-4: a family of protein phosphatase 1 and actin regulatory
RT   proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7187-7192(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Hypothalamus, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBUNIT: Binds PPP1CA and actin; thus inhibiting the protein
CC       phosphatase 1 (PP1) activity (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus matrix (By similarity).
CC       Note=Localized to the nuclear matrix-intermediate filament
CC       scaffold (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8BYK5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BYK5-2; Sequence=VSP_009093;
CC       Name=3;
CC         IsoId=Q8BYK5-3; Sequence=VSP_009094;
CC       Name=4;
CC         IsoId=Q8BYK5-4; Sequence=VSP_009095;
CC   -!- SIMILARITY: Belongs to the phosphatase and actin regulator family.
CC   -!- SIMILARITY: Contains 4 RPEL repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; AY501387; AAS86433.1; -; mRNA.
DR   EMBL; AK005136; BAB23834.1; -; mRNA.
DR   EMBL; AK032242; BAC27776.1; -; mRNA.
DR   EMBL; AK038449; BAC30003.1; -; mRNA.
DR   EMBL; AK039213; BAC30278.1; -; mRNA.
DR   EMBL; BC058621; AAH58621.1; -; mRNA.
DR   EMBL; BC059869; AAH59869.1; -; mRNA.
DR   IPI; IPI00338087; -.
DR   IPI; IPI00395154; -.
DR   IPI; IPI00395155; -.
DR   IPI; IPI00395156; -.
DR   RefSeq; NP_001007155.1; NM_001007154.3.
DR   RefSeq; NP_001171260.1; NM_001177789.1.
DR   RefSeq; NP_001171261.1; NM_001177790.1.
DR   RefSeq; NP_001171262.1; NM_001177791.1.
DR   RefSeq; NP_083082.1; NM_028806.2.
DR   UniGene; Mm.44413; -.
DR   STRING; Q8BYK5; -.
DR   PRIDE; Q8BYK5; -.
DR   Ensembl; ENSMUST00000029031; ENSMUSP00000029031; ENSMUSG00000027525.
DR   Ensembl; ENSMUST00000103066; ENSMUSP00000099355; ENSMUSG00000027525.
DR   Ensembl; ENSMUST00000108914; ENSMUSP00000104542; ENSMUSG00000027525.
DR   GeneID; 74189; -.
DR   KEGG; mmu:74189; -.
DR   UCSC; uc008ohj.1; mouse.
DR   UCSC; uc008ohk.1; mouse.
DR   UCSC; uc008ohl.1; mouse.
DR   CTD; 74189; -.
DR   MGI; MGI:1921439; Phactr3.
DR   GeneTree; ENSGT00390000004420; -.
DR   HOVERGEN; HBG057352; -.
DR   OMA; GASENKW; -.
DR   NextBio; 340044; -.
DR   ArrayExpress; Q8BYK5; -.
DR   Bgee; Q8BYK5; -.
DR   CleanEx; MM_PHACTR3; -.
DR   Genevestigator; Q8BYK5; -.
DR   GermOnline; ENSMUSG00000027525; Mus musculus.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004018; RPEL_repeat.
DR   Pfam; PF02755; RPEL; 2.
DR   SMART; SM00707; RPEL; 4.
DR   PROSITE; PS51073; RPEL; 4.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Coiled coil; Nucleus;
KW   Phosphoprotein; Protein phosphatase inhibitor; Repeat.
FT   CHAIN         1    558       Phosphatase and actin regulator 3.
FT                                /FTId=PRO_0000126639.
FT   REPEAT       92    117       RPEL 1.
FT   REPEAT      400    425       RPEL 2.
FT   REPEAT      438    463       RPEL 3.
FT   REPEAT      476    501       RPEL 4.
FT   COILED      449    485       Potential.
FT   COMPBIAS    216    238       Pro-rich.
FT   MOD_RES      69     69       Phosphothreonine (By similarity).
FT   VAR_SEQ       1     40       Missing (in isoform 4).
FT                                /FTId=VSP_009095.
FT   VAR_SEQ       1     38       MAASEDGSSCLVSRGRSQSDPSFLSDSSATSTDAGENP ->
FT                                MQTANQMLSLNFRRMKSGTAAVRTRARHRPPGSGPSRCG
FT                                (in isoform 2).
FT                                /FTId=VSP_009093.
FT   VAR_SEQ       1     38       MAASEDGSSCLVSRGRSQSDPSFLSDSSATSTDAGENP ->
FT                                MRGQGRGHARWPAPLRSLLRAFGPQDTTTGGLEQ (in
FT                                isoform 3).
FT                                /FTId=VSP_009094.
SQ   SEQUENCE   558 AA;  62652 MW;  8D7D1D5F5BEE37A9 CRC64;
     MAASEDGSSC LVSRGRSQSD PSFLSDSSAT STDAGENPDE MDQTPPARSE PLVSGIRTPP
     VRRNSKLATL GRIFKPWKWR KKKNEKLKQT TSALEKKMAG RQGREELIKQ GLLEMMEQDS
     ENKACSPKEG SQPVQSEPPA GEQETLTSEG AQPGSPSASG TDQVSQDELL SSDAHLDDTA
     NIPSASTAEE ADAGSLLPTT DEPSQALAGS DSLDSPPRSL ERSVSQLPSP PLLPTPPPKA
     SSKATKNVTG QAALFQGPSM KNNEPALRGQ LATPTGSPHV TTVHRPLPPS RVMEELHRAL
     ATKHRQDSFQ GRECRGSPKK RMDVRLSRTS SMERGKERDE AWSFDGASEN KWTATKDSEE
     NKENLMLSSE LKDDMLLYQD EEALNDSIIS GTLPRKCKKE LLAVKLRNRP SKQELEDRNI
     FPRRTDEERQ EIRQQIEMKL SKRLSQRPAV EELERRNILK QRNDQTEQEE RREIKQRLTR
     KLNQRPTVDE LRDRKILIRF SDYVEVARAQ DYDRRADKPW TRLSAADKAA IRKELNEYKS
     NEMEVHASSK HLTRFHRP
//
ID   ZC3H6_MOUSE             Reviewed;        1177 AA.
AC   Q8BYK8; A2AP87; Q80UK3; Q8C1H1; Q9D604;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Zinc finger CCCH domain-containing protein 6;
GN   Name=Zc3h6; Synonyms=Zc3hdc6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 215-1177 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BYK8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BYK8-2; Sequence=VSP_010212, VSP_010213;
CC   -!- SIMILARITY: Contains 3 C3H1-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH43311.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK014766; BAB29540.1; -; mRNA.
DR   EMBL; AK039171; BAC30264.1; -; mRNA.
DR   EMBL; AL833780; CAM18661.1; -; Genomic_DNA.
DR   EMBL; BC043311; AAH43311.1; ALT_INIT; mRNA.
DR   EMBL; BC058173; AAH58173.1; -; mRNA.
DR   IPI; IPI00108263; -.
DR   IPI; IPI00761322; -.
DR   UniGene; Mm.26377; -.
DR   ProteinModelPortal; Q8BYK8; -.
DR   SMR; Q8BYK8; 267-385.
DR   PhosphoSite; Q8BYK8; -.
DR   PRIDE; Q8BYK8; -.
DR   Ensembl; ENSMUST00000110319; ENSMUSP00000105948; ENSMUSG00000042851.
DR   Ensembl; ENSMUST00000110320; ENSMUSP00000105949; ENSMUSG00000042851.
DR   UCSC; uc008mha.2; mouse.
DR   UCSC; uc008mhc.2; mouse.
DR   MGI; MGI:1926001; Zc3h6.
DR   GeneTree; ENSGT00530000063288; -.
DR   HOGENOM; HBG446706; -.
DR   HOVERGEN; HBG063914; -.
DR   InParanoid; Q8BYK8; -.
DR   OrthoDB; EOG4CG081; -.
DR   ArrayExpress; Q8BYK8; -.
DR   Bgee; Q8BYK8; -.
DR   CleanEx; MM_ZC3H6; -.
DR   Genevestigator; Q8BYK8; -.
DR   GermOnline; ENSMUSG00000042851; Mus musculus.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR000571; Znf_CCCH.
DR   Pfam; PF00642; zf-CCCH; 2.
DR   SMART; SM00356; ZnF_C3H1; 3.
DR   PROSITE; PS50103; ZF_C3H1; 3.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Metal-binding; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1177       Zinc finger CCCH domain-containing
FT                                protein 6.
FT                                /FTId=PRO_0000213902.
FT   ZN_FING     271    297       C3H1-type 1.
FT   ZN_FING     299    326       C3H1-type 2.
FT   ZN_FING     327    350       C3H1-type 3.
FT   COILED       27     73       Potential.
FT   COILED      347    383       Potential.
FT   COMPBIAS    386    518       Pro-rich.
FT   VAR_SEQ     113    151       HRRISGSYMTSKKSQHNKKTNSKEYAESSFYSDDYFGNY
FT                                -> NSAITVVHLQNLIHLTQKFCTSEADLLRSPLTAVLTFC
FT                                L (in isoform 2).
FT                                /FTId=VSP_010212.
FT   VAR_SEQ     152   1177       Missing (in isoform 2).
FT                                /FTId=VSP_010213.
FT   CONFLICT    469    469       R -> H (in Ref. 3; AAH43311).
FT   CONFLICT    482    482       K -> N (in Ref. 3; AAH43311).
FT   CONFLICT    556    556       V -> M (in Ref. 3; AAH43311).
FT   CONFLICT    629    629       R -> H (in Ref. 3; AAH43311).
SQ   SEQUENCE   1177 AA;  131250 MW;  6476FBE426823394 CRC64;
     MTDSEHAGHD REDGELEDGE IDDAGFEETQ DQEAKENEKQ KNEKAYRKSR KKHKKEREKK
     KSKRRKHEKH KHNSPSGDDS SDYSLDSDVE RMQSSRKKRT SSYRDYDVPF SQHRRISGSY
     MTSKKSQHNK KTNSKEYAES SFYSDDYFGN YSDDNFGNYS NQEGEEDFSS QLKYYRQSQE
     SSGSSFSKES GKKLRSKGSP PGTEYRIKSF DVSHGHLLPK KIRRKEHCGA RVIKGPYVFS
     GMDDFQEYSK PGKKWKVMTQ EFINQHTVEH KGKQICKYFL EGRCIKGDHC KFNHDAELEK
     KKEVCKYYLQ GYCTKGENCI YMHSEFPCKF YHSGAKCYQG DKCKFSHDDL TKETRKLLDK
     VLNADEELVN EDERELEELR KRGITPLPKP PPGVGLLPTP SEHFPFSDPE DDFETDLSDD
     MKKIPSLFEI VVKPTVDLAH KIGKKPPAFY NSTSPPGPQF EESSHCPQRM YSSESSPGPG
     SKVPQGCESP VRHPGSPGHH PCVGPPGPPM QENPSLLPSS SEIVGPHSQA GGLVQLDTLP
     SMGGAYHSPG FPGHSVKVPR ESHSSPASLY QQMPSEMQRS ADSESMQGSA EFYDDYYPQH
     AAHNFQPPDN SADEMWHEEF AQQQPPIARD TAHLGSGPNS SSRMTSHCPL SASGLPPAVQ
     RALFIPLTQR YQEDEEPAGT QPHRASSKEE DDTANWYSSS EEEEGSGVKS ILRTLQKQTG
     TLRNQQLPPT ELSVPTDPRL AKEKRKRNQV VDPRLRTVPR QDIKKPHESV PVDLRLVWDP
     KKLRGNGGAP GGSSARGAEF DLRHTNAGAN HKSKRREDDD EDSERELREK AFLIPLDSSP
     GIVLQDPRSQ LRQFSHIKMD IILNKPNFAK HIVWAPEDLL PVPLPKPDPV SSINLPLPPL
     IADQRLNRLW NTKSDHQGAL SLDPTSAAKA KLSLTHREGC LEQSGDLHSS GGKLGDPRLQ
     KNFDPRLHRL PNTESHQVTA KDSHSSRSAL PLARWNPALS QPSTAAPINV ASVTPPLYAP
     KLSSEGLPPG TSSSVLSGIS LYDPRDKGSL SATELSTISS GENTESQKKS GLKNSDKNQP
     SPGEVTVPQN TTADMEVPVD GPVDMQTDIL RSADKVQVPA VHSLPIQALT GLLRPPYSDP
     RQAREPGQAS PTPDEETDDK PLKEVFKTFD PTASPFC
//
ID   Q8BYL0_MOUSE            Unreviewed;       554 AA.
AC   Q8BYL0;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 2.
DT   30-NOV-2010, entry version 52.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Arap2; Synonyms=Centd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK039153; BAC30258.2; -; mRNA.
DR   IPI; IPI00606178; -.
DR   UniGene; Mm.244403; -.
DR   ProteinModelPortal; Q8BYL0; -.
DR   STRING; Q8BYL0; -.
DR   Ensembl; ENSMUST00000076623; ENSMUSP00000075924; ENSMUSG00000037999.
DR   MGI; MGI:2684416; Arap2.
DR   InParanoid; Q8BYL0; -.
DR   ArrayExpress; Q8BYL0; -.
DR   Bgee; Q8BYL0; -.
DR   Genevestigator; Q8BYL0; -.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   2: Evidence at transcript level;
FT   NON_TER     554    554
SQ   SEQUENCE   554 AA;  62149 MW;  B43A386186CAC1EF CRC64;
     MSSVSEVNAD IRDFLMSINL EQYLLHFREF GFYTVRDCTS INDSVLHQIG ISPTGHRRRI
     LKQLQMIFSK MQDFPIYANV HKAKNGSTTK EQQHSDPSSS THTGIECSDS ITVHRPGPAP
     SEMVTTSTLS EGNCQSPKSH DKLCLSSHDL LCPEEELHQN VDSSKDSLFG GVNVKIDPLI
     TKRAVEYTAG EEHTEKGNLT SEDSSKALST NTECLPSGDC PTSGTHSGNG TNGVLESFPP
     TPFFQFQGEM VVNELYVPSS PVHGPMRSRS KLVSRPSRSF LLRHRPVPEI PGSTKSIPGS
     YFRDRRSNTT SAGKSLTLKN SNEDNSTSIF PYGETFLFQR LESSKKRSIK NEFWPHENTV
     KEEAATTRNS ILTQSSIYDN RKEKVSEDKV EDIWIPREDK NNLAQDSASE SEYSTVEECF
     QSLRRKNSKA SKSRTQKAFY LDPFNRHSYP LSSTSGNTEP SSTISNAISP YACFYGSSAA
     KEKCGWLDKL SPQGKRMFQK RWVKFDGLSI SYYNNDREMY SKGIIPLTAI STVRAQGDNK
     FEIVTTQRTF VFRV
//
ID   NLGN3_MOUSE             Reviewed;         825 AA.
AC   Q8BYM5; Q8BXR4;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Neuroligin-3;
DE   AltName: Full=Gliotactin homolog;
DE   Flags: Precursor;
GN   Name=Nlgn3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=21226491; PubMed=11329178; DOI=10.1002/glia.1050;
RA   Gilbert M., Smith J., Roskams A.J., Auld V.J.;
RT   "Neuroligin 3 is a vertebrate gliotactin expressed in the olfactory
RT   ensheathing glia, a growth-promoting class of macroglia.";
RL   Glia 34:151-164(2001).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-769, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Neuronal cell surface protein thought to be involved in
CC       cell-cell-interactions by forming intercellular junctions through
CC       binding to beta-neurexins. May play a role in formation or
CC       maintenance of synaptic junctions. May also play a role in glia-
CC       glia or glia-neuron interactions in the developing peripheral
CC       nervous system.
CC   -!- SUBUNIT: Interacts with neurexin 1-beta, neurexin 2-beta and
CC       neurexin 3-beta, and probably through its C-terminus with
CC       DLG4/PSD-95 third PDZ domain (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- TISSUE SPECIFICITY: Expressed in olfactory bulb and olfactory
CC       epithelium. Found in olfactory ensheathing glia but not in
CC       olfactory neurons, and in developing peripheral glia.
CC   -!- DEVELOPMENTAL STAGE: Detected at embryonic day E17 and postnatal
CC       day P1 in retinal astrocytes, spinal chord astrocytes and Schwann
CC       cells of the dorsal root ganglion.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
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DR   EMBL; AK039018; BAC30207.1; -; mRNA.
DR   EMBL; AK044438; BAC31918.1; -; mRNA.
DR   IPI; IPI00227168; -.
DR   RefSeq; NP_766520.2; NM_172932.3.
DR   UniGene; Mm.121508; -.
DR   UniGene; Mm.479388; -.
DR   ProteinModelPortal; Q8BYM5; -.
DR   SMR; Q8BYM5; 36-608.
DR   STRING; Q8BYM5; -.
DR   MEROPS; S09.987; -.
DR   PhosphoSite; Q8BYM5; -.
DR   PRIDE; Q8BYM5; -.
DR   Ensembl; ENSMUST00000065858; ENSMUSP00000066304; ENSMUSG00000031302.
DR   GeneID; 245537; -.
DR   KEGG; mmu:245537; -.
DR   UCSC; uc009txj.1; mouse.
DR   CTD; 245537; -.
DR   MGI; MGI:2444609; Nlgn3.
DR   HOVERGEN; HBG008839; -.
DR   OrthoDB; EOG4CZBF6; -.
DR   NextBio; 386794; -.
DR   ArrayExpress; Q8BYM5; -.
DR   Bgee; Q8BYM5; -.
DR   CleanEx; MM_NLGN3; -.
DR   Genevestigator; Q8BYM5; -.
DR   GermOnline; ENSMUSG00000031302; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0060080; P:regulation of inhibitory postsynaptic membrane potential; IMP:MGI.
DR   GO; GO:0002087; P:regulation of respiratory gaseous exchange by neurological system process; IGI:MGI.
DR   GO; GO:0050804; P:regulation of synaptic transmission; IGI:MGI.
DR   GO; GO:0035176; P:social behavior; IMP:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   InterPro; IPR000460; Neuroligin.
DR   PANTHER; PTHR11559; CarbesteraseB; 1.
DR   Pfam; PF00135; COesterase; 1.
DR   PRINTS; PR01090; NEUROLIGIN.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     34       Potential.
FT   CHAIN        35    825       Neuroligin-3.
FT                                /FTId=PRO_0000008646.
FT   TOPO_DOM     35    686       Extracellular (Potential).
FT   TRANSMEM    687    707       Helical; (Potential).
FT   TOPO_DOM    708    825       Cytoplasmic (Potential).
FT   MOD_RES     769    769       Phosphotyrosine.
FT   CARBOHYD     95     95       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    522    522       N-linked (GlcNAc...) (Potential).
FT   DISULFID    103    138       By similarity.
FT   DISULFID    317    328       By similarity.
FT   DISULFID    487    521       By similarity.
FT   CONFLICT    459    459       Q -> K (in Ref. 1; BAC31918).
SQ   SEQUENCE   825 AA;  91176 MW;  3BF17F889B0A44CE CRC64;
     MWLQPSLSLS PTPTVGRSLC LTLGFLSLVL RASTQAPAPT VNTHFGKLRG ARVPLPSEIL
     GPVEQYLGVP YAAPPIGEKR FLPPEPPPSW SGIRNATHFP PVCPQNIHTA VPEVMLPVWF
     TANLDIVATY IQEPNEDCLY LNVYVPTEDG SGAKKQGEDL ADNDGDEDED IRDSGAKPVM
     VYIHGGSYME GTGNMIDGSV LASYGNVIVI TLNYRVGVLG FLSTGDQAAK GNYGLLDQIQ
     ALRWVSENIA FFGGDPRRIT VFGSGIGASC VSLLTLSHHS EGLFQRAIIQ SGSALSSWAV
     NYQPVKYTSL LADKVGCNVL DTVDMVDCLR QKSAKELVEQ DIQPARYHVA FGPVIDGDVI
     PDDPEILMEQ GEFLNYDIML GVNQGEGLKF VEGVVDPEDG VSGTDFDYSV SNFVDNLYGY
     PEGKDTLRET IKFMYTDWAD RDNPETRRKT LVALFTDHQW VEPSVVTADL HARYGSPTYF
     YAFYHHCQSL MKPAWSDAAH GDEVPYVFGV PMVGPTDLFP CNFSKNDVML SAVVMTYWTN
     FAKTGDPNKP VPQDTKFIHT KANRFEEVAW SKYNPRDQLY LHIGLKPRVR DHYRATKVAF
     WKHLVPHLYN LHDMFHYTST TTKVPPPDTT HSSHITRRPN GKTWSTKRPA ISPAYSNENA
     PGSWNGDQDA GPLLVENPRD YSTELSVTIA VGASLLFLNV LAFAALYYRK DKRRQEPLRQ
     PSPQRGTGAP ELGTAPEEEL AALQLGPTHH ECEAGPPHDT LRLTALPDYT LTLRRSPDDI
     PLMTPNTITM IPNSLVGLQT LHPYNTFAAG FNSTGLPHSH STTRV
//
ID   RHG25_MOUSE             Reviewed;         648 AA.
AC   Q8BYW1; B2RS69; Q2VPR2; Q3TE04; Q3TVX0; Q3UVB7; Q6A0E0; Q8BX98;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Rho GTPase-activating protein 25;
DE   AltName: Full=Rho-type GTPase-activating protein 25;
GN   Name=Arhgap25; Synonyms=Kiaa0053;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone, Dendritic cell, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 117-648 (ISOFORMS 1/2/3).
RC   TISSUE=Jaw, Limb, and Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 100-648 (ISOFORMS 1/2/3).
RC   TISSUE=Thymus;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-363, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting
CC       them to an inactive GDP-bound state (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BYW1-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q8BYW1-2; Sequence=VSP_019233;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8BYW1-3; Sequence=VSP_019234;
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC29857.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK037710; BAC29857.1; ALT_INIT; mRNA.
DR   EMBL; AK137444; BAE23353.1; -; mRNA.
DR   EMBL; AK159941; BAE35498.1; -; mRNA.
DR   EMBL; AK159598; BAE35218.1; -; mRNA.
DR   EMBL; AK169897; BAE41444.1; -; mRNA.
DR   EMBL; BC108400; AAI08401.1; -; mRNA.
DR   EMBL; BC138751; AAI38752.1; -; mRNA.
DR   EMBL; AK172878; BAD32156.1; -; mRNA.
DR   IPI; IPI00353418; -.
DR   IPI; IPI00663705; -.
DR   IPI; IPI00760043; -.
DR   RefSeq; NP_001032816.1; NM_001037727.1.
DR   RefSeq; NP_780685.2; NM_175476.3.
DR   UniGene; Mm.119564; -.
DR   ProteinModelPortal; Q8BYW1; -.
DR   SMR; Q8BYW1; 47-152, 156-356.
DR   STRING; Q8BYW1; -.
DR   PhosphoSite; Q8BYW1; -.
DR   PRIDE; Q8BYW1; -.
DR   Ensembl; ENSMUST00000101197; ENSMUSP00000098758; ENSMUSG00000030047.
DR   Ensembl; ENSMUST00000113637; ENSMUSP00000109267; ENSMUSG00000030047.
DR   GeneID; 232201; -.
DR   KEGG; mmu:232201; -.
DR   UCSC; uc009ctl.1; mouse.
DR   UCSC; uc009ctm.1; mouse.
DR   UCSC; uc009ctn.1; mouse.
DR   CTD; 232201; -.
DR   MGI; MGI:2443687; Arhgap25.
DR   eggNOG; roNOG12906; -.
DR   GeneTree; ENSGT00590000083061; -.
DR   HOVERGEN; HBG058875; -.
DR   InParanoid; Q8BYW1; -.
DR   OMA; IFKNEFW; -.
DR   OrthoDB; EOG40CHGT; -.
DR   PhylomeDB; Q8BYW1; -.
DR   NextBio; 380982; -.
DR   ArrayExpress; Q8BYW1; -.
DR   Bgee; Q8BYW1; -.
DR   CleanEx; MM_ARHGAP25; -.
DR   Genevestigator; Q8BYW1; -.
DR   GermOnline; ENSMUSG00000030047; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; GTPase activation; Phosphoprotein.
FT   CHAIN         1    648       Rho GTPase-activating protein 25.
FT                                /FTId=PRO_0000056717.
FT   DOMAIN       46    151       PH.
FT   DOMAIN      160    354       Rho-GAP.
FT   COILED      540    641       Potential.
FT   MOD_RES     363    363       Phosphoserine.
FT   MOD_RES     396    396       Phosphoserine (By similarity).
FT   MOD_RES     408    408       Phosphoserine.
FT   VAR_SEQ       1     89       Missing (in isoform 2).
FT                                /FTId=VSP_019233.
FT   VAR_SEQ       1     26       Missing (in isoform 3).
FT                                /FTId=VSP_019234.
FT   CONFLICT    144    144       K -> N (in Ref. 2; AAI08401).
FT   CONFLICT    333    333       M -> T (in Ref. 1; BAE41444).
SQ   SEQUENCE   648 AA;  73383 MW;  CBDFE75515BB2C51 CRC64;
     MSLKLPRNWD FNLKAEASKI ARSRSVMTGE QMAAFHPPTT PNPLERPIKV GWLKKQRSIV
     KNWQQRYFVL RAQQLYYYKD EEDSKPQGCM YLPGSTVKEI ATNPEEAGKF VFEVIPASSD
     QNRIGQDSYV LMASSQVEME EWVKFLRRVA GTPSGAVFGQ RLDETVAYEQ KFGPHLVPIL
     VEKCAEFILE HGVSEEGIFR LPGQDNLVKQ LRDAFDAGER PSFDRDTDVH TVASLLKLYL
     RDLPEPVVPW SQYEGFLLCG QLMNADEAKA QQELVKQLST LPRDNYNLLS YICRFLHEIQ
     LNCAVNKMSV DNLATVIGVN LIRSKVEDPA VIMRGTPQIQ RVMTMMIRDH EVLFPKSKDA
     PISPPAQKND AKKAPVPRSS VGWDATEDPP LSRTDSFSNT ASSPDATSPT GPLPSDQHQE
     DSGKAPRENP GDWKMQSRKR TQTLPNRKCF LTSAFQGTTS SKLEIFKNEF WSPSSEAKAG
     EGHRRTMSQD LRHLSNDQRT STYDNVPTSP QSQGNPAGAL SPPASDSKRD ALVSTDSEME
     AGSKNSGEDD LDSLQRTVQS LQKEIETQKQ VYEEQIKNLE KENYDVWAKV VRLNEELERE
     RKKFAALEIS LRNVERSRED VEKRNRVLEE EVKEFVKSME KPKTKTDP
//
ID   ABI3_MOUSE              Reviewed;         367 AA.
AC   Q8BYZ1; Q6PE63; Q9D7S4;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=ABI gene family member 3;
DE   AltName: Full=New molecule including SH3;
DE            Short=Nesh;
GN   Name=Abi3; Synonyms=Nesh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Skin, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION.
RX   PubMed=11956071;
RA   Ichigotani Y., Yokozaki S., Fukuda Y., Hamaguchi M., Matsuda S.;
RT   "Forced expression of NESH suppresses motility and metastatic
RT   dissemination of malignant cells.";
RL   Cancer Res. 62:2215-2219(2002).
CC   -!- FUNCTION: Inhibits ectopic tumor cell metastasis of SRD cells. In
CC       vitro, reduces cell motility.
CC   -!- SUBUNIT: May interact with PAK1 and PAK2. Probably interacts with
CC       TARSH (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BYZ1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BYZ1-2; Sequence=VSP_010773;
CC   -!- SIMILARITY: Belongs to the ABI family.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK008928; BAB25972.1; -; mRNA.
DR   EMBL; AK037144; BAC29720.1; -; mRNA.
DR   EMBL; BC058260; AAH58260.1; -; mRNA.
DR   IPI; IPI00454197; -.
DR   IPI; IPI00653923; -.
DR   RefSeq; NP_001156936.1; NM_001163464.1.
DR   RefSeq; NP_079935.1; NM_025659.4.
DR   UniGene; Mm.479272; -.
DR   ProteinModelPortal; Q8BYZ1; -.
DR   SMR; Q8BYZ1; 3-157, 302-364.
DR   STRING; Q8BYZ1; -.
DR   PRIDE; Q8BYZ1; -.
DR   Ensembl; ENSMUST00000059026; ENSMUSP00000061893; ENSMUSG00000018381.
DR   GeneID; 66610; -.
DR   KEGG; mmu:66610; -.
DR   CTD; 66610; -.
DR   MGI; MGI:1913860; Abi3.
DR   GeneTree; ENSGT00390000003756; -.
DR   HOGENOM; HBG125191; -.
DR   HOVERGEN; HBG050446; -.
DR   InParanoid; Q8BYZ1; -.
DR   OrthoDB; EOG4CRM0Q; -.
DR   ArrayExpress; Q8BYZ1; -.
DR   Bgee; Q8BYZ1; -.
DR   CleanEx; MM_ABI3; -.
DR   Genevestigator; Q8BYZ1; -.
DR   GermOnline; ENSMUSG00000018381; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR012849; Abl-interactor_HHR_dom.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF07815; Abi_HHR; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Cytoplasm; SH3 domain.
FT   CHAIN         1    367       ABI gene family member 3.
FT                                /FTId=PRO_0000191793.
FT   DOMAIN      309    367       SH3.
FT   COILED       36     64       Potential.
FT   COMPBIAS    235    307       Pro-rich.
FT   VAR_SEQ       1     53       Missing (in isoform 2).
FT                                /FTId=VSP_010773.
FT   CONFLICT    339    339       I -> T (in Ref. 1; BAB25972/BAC29720).
SQ   SEQUENCE   367 AA;  39119 MW;  0CEC0279E88BAFF7 CRC64;
     MAELQQLQQL QEFDIPTGRE ALRGNHSALL RVANYCEDNY LQATDKRKAL EETMAFTTQA
     LASVAYQVGN LAGHTLRMLD LQGAALRQVE AKMSTLGQMV NMHMEKVARR EIGTLATVVR
     LPSNQKVIPP ESLPSLTPYH RKPLNFACLD DIGHGVKDLS TQLSRTGTLS RKSIKAPATP
     VSATLGRPPR IPEPVQLPAV PDGKLSAASS ASSLASAGSA EGASGIPQSK GQVAPATPPP
     PPVAPVTPPP PPLSAEVFLP PPPLEVSQPP LEAELPLPPP PALEGDELGL LPPPPPGFGP
     DEPSWVPASY LEKVVTLYPY TRQKDNELSF SEGTVICVIR RYSDGWCEGV SSEGTGFFPG
     NYVEPSC
//
ID   KPCD2_MOUSE             Reviewed;         875 AA.
AC   Q8BZ03; Q3TCE5; Q3TDF0; Q3U4V4;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Serine/threonine-protein kinase D2;
DE            EC=2.7.11.13;
DE   AltName: Full=nPKC-D2;
GN   Name=Prkd2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Thymus, and Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200; SER-211; SER-212
RP   AND SER-214, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Converts transient diacylglycerol (DAG) signals into
CC       prolonged physiological effects, downstream of PKC. Involved in
CC       resistance to oxidative stress (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activated by DAG and phorbol esters. Phorbol-
CC       ester/DAG-type domains bind DAG, mediating translocation to
CC       membranes. Autophosphorylation of Ser-711 and phosphorylation of
CC       Ser-707 by PKC relieves auto-inhibition by the PH domain (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane (By
CC       similarity). Note=Translocation to the cell membrane is required
CC       for kinase activation (By similarity).
CC   -!- PTM: Phosphorylation of Ser-873 correlates with the activation
CC       status of the kinase (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. PKD subfamily.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 2 phorbol-ester/DAG-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AK037030; BAC29677.1; -; mRNA.
DR   EMBL; AK154029; BAE32326.1; -; mRNA.
DR   EMBL; AK170236; BAE41652.1; -; mRNA.
DR   EMBL; AK170761; BAE42012.1; -; mRNA.
DR   EMBL; BC095949; AAH95949.1; -; mRNA.
DR   EMBL; BC096444; AAH96444.1; -; mRNA.
DR   IPI; IPI00227209; -.
DR   RefSeq; NP_849231.1; NM_178900.4.
DR   UniGene; Mm.1881; -.
DR   HSSP; Q9BZL6; 2COA.
DR   ProteinModelPortal; Q8BZ03; -.
DR   SMR; Q8BZ03; 135-189, 261-317, 396-510, 544-812.
DR   PhosphoSite; Q8BZ03; -.
DR   PRIDE; Q8BZ03; -.
DR   Ensembl; ENSMUST00000086104; ENSMUSP00000083273; ENSMUSG00000041187.
DR   GeneID; 101540; -.
DR   KEGG; mmu:101540; -.
DR   UCSC; uc009fig.1; mouse.
DR   CTD; 101540; -.
DR   MGI; MGI:2141917; Prkd2.
DR   eggNOG; roNOG09017; -.
DR   GeneTree; ENSGT00600000084006; -.
DR   HOGENOM; HBG314865; -.
DR   HOVERGEN; HBG003564; -.
DR   InParanoid; Q8BZ03; -.
DR   OMA; PASPWSH; -.
DR   OrthoDB; EOG4548XW; -.
DR   BRENDA; 2.7.11.13; 244.
DR   NextBio; 355000; -.
DR   ArrayExpress; Q8BZ03; -.
DR   Bgee; Q8BZ03; -.
DR   CleanEx; MM_PRKD2; -.
DR   Genevestigator; Q8BZ03; -.
DR   GermOnline; ENSMUSG00000041187; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004697; F:protein kinase C activity; IEA:EC.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR015727; Protein_Kinase_C_mu-related.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   PANTHER; PTHR22968; PKC_mu_like; 1.
DR   Pfam; PF00130; C1_1; 2.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Kinase; Magnesium; Membrane; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Repeat;
KW   Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    875       Serine/threonine-protein kinase D2.
FT                                /FTId=PRO_0000260436.
FT   DOMAIN      398    510       PH.
FT   DOMAIN      552    808       Protein kinase.
FT   ZN_FING     138    188       Phorbol-ester/DAG-type 1.
FT   ZN_FING     265    315       Phorbol-ester/DAG-type 2.
FT   NP_BIND     558    566       ATP (By similarity).
FT   ACT_SITE    675    675       Proton acceptor (By similarity).
FT   BINDING     581    581       ATP (By similarity).
FT   MOD_RES     189    189       Phosphoserine (By similarity).
FT   MOD_RES     197    197       Phosphoserine (By similarity).
FT   MOD_RES     198    198       Phosphoserine (By similarity).
FT   MOD_RES     199    199       Phosphothreonine (By similarity).
FT   MOD_RES     200    200       Phosphoserine.
FT   MOD_RES     203    203       Phosphoserine (By similarity).
FT   MOD_RES     206    206       Phosphoserine (By similarity).
FT   MOD_RES     211    211       Phosphoserine.
FT   MOD_RES     212    212       Phosphoserine.
FT   MOD_RES     214    214       Phosphoserine.
FT   MOD_RES     225    225       Phosphoserine (By similarity).
FT   MOD_RES     227    227       Phosphothreonine (By similarity).
FT   MOD_RES     236    236       Phosphoserine (By similarity).
FT   MOD_RES     237    237       Phosphoserine (By similarity).
FT   MOD_RES     238    238       Phosphoserine (By similarity).
FT   MOD_RES     339    339       Phosphoserine (By similarity).
FT   MOD_RES     354    354       Phosphoserine (By similarity).
FT   MOD_RES     356    356       Phosphoserine (By similarity).
FT   MOD_RES     363    363       Phosphoserine (By similarity).
FT   MOD_RES     375    375       Phosphoserine (By similarity).
FT   MOD_RES     376    376       Phosphoserine (By similarity).
FT   MOD_RES     397    397       Phosphoserine (By similarity).
FT   MOD_RES     519    519       Phosphoserine (By similarity).
FT   MOD_RES     707    707       Phosphoserine; by PKC (By similarity).
FT   MOD_RES     711    711       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     718    718       Phosphotyrosine (By similarity).
FT   MOD_RES     873    873       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   CONFLICT    213    213       E -> G (in Ref. 1; BAE42012).
FT   CONFLICT    220    220       E -> G (in Ref. 1; BAE41652).
FT   CONFLICT    310    310       R -> H (in Ref. 1; BAE32326/BAE41652).
FT   CONFLICT    630    630       K -> N (in Ref. 1; BAE42012).
SQ   SEQUENCE   875 AA;  96542 MW;  C7173546FA1E6DB1 CRC64;
     MAAAPSHPAG LPGSPGPGSP PPPGGLDLQS PPPLLPQIPA PGSGVSFHIQ IGLTREFVLL
     PAASELAHVK QLACSIVDQK FPECGFYGLY DKILLFKHDP TSANLLQLVR SAADIQEGDL
     VEVVLSASAT FEDFQIRPHA LTVHSYRAPA FCDHCGEMLF GLVRQGLKCD GCGLNYHKRC
     AFSIPNNCSG ARKRRLSSTS LASGHSVRLG SSESLPCTAE ELSRSTTDLL PRRPPSSSSS
     SSSSSFYTGR PIELDKMLMS KVKVPHTFLI HSYTRPTVCQ ACKKLLKGLF RQGLQCKDCK
     FNCHKRCATR VPNDCLGEAL INGDVPMEEA ADYSEADKSS ISDELEDSGV IPGSHSESAL
     HASEEEEGEG HKAQSSLGYI PLMRVVQSVR HTTRKSSTTL REGWVVHYSN KDTLRKRHYW
     RLDCKCITLF QNNTTNRYYK EIPLSEILAV EPAQNFSLVP PGTNPHCFEI ITANVTYFVG
     ETPGGAPGGP SGQGTEAVRG WETAIRQALM PVILQDAPSA PGHTPHRQAS LSISVSNSQI
     QENVDIATVY QIFPDEVLGS GQFGVVYGGK HRKTGRDVAV KVIDKLRFPT KQESQLRNEV
     AILQSLRHPG IVNLECMFET PEKVFVVMEK LHGDMLEMIL SSEKGRLPER LTKFLITQIL
     VALRHLHFKN IVHCDLKPEN VLLASADPFP QVKLCDFGFA RIIGEKSFRR SVVGTPAYLA
     PEVLLNQGYN RSLDMWSVGV IMYVSLSGTF PFNEDEDIND QIQNAAFMYP ASPWSHISSG
     AIDLINNLLQ VKMRKRYSVD KSLSHPWLQE YQTWLDLREL EGKMGERYIT HESDDARWDQ
     FVAERHGTPA EGDLGGACLP QDHEMQGLAE RISIL
//
ID   MYST3_MOUSE             Reviewed;        2003 AA.
AC   Q8BZ21; Q8BW52; Q8BYH1; Q8C1F3;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 2.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Histone acetyltransferase MYST3;
DE            Short=MYST-3;
DE            EC=2.3.1.48;
DE   AltName: Full=MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3;
DE   AltName: Full=Monocytic leukemia zinc finger homolog;
DE   AltName: Full=Monocytic leukemia zinc finger protein;
GN   Name=Myst3; Synonyms=Moz;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1010.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Ovary, Spinal cord, and Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   INTERACTION WITH RUNX1, FUNCTION, AND MASS SPECTROMETRY.
RX   PubMed=11742995; DOI=10.1093/emboj/20.24.7184;
RA   Kitabayashi I., Aikawa Y., Nguyen L.A., Yokoyama A., Ohki M.;
RT   "Activation of AML1-mediated transcription by MOZ and inhibition by
RT   the MOZ-CBP fusion protein.";
RL   EMBO J. 20:7184-7196(2001).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1115, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Histone acetyltransferase that acetylates lysine
CC       residues in histone H3 and histone H4 (in vitro). Component of the
CC       MOZ/MORF complex which has a histone H3 acetyltransferase
CC       activity. May act as a transcriptional coactivator for RUNX1 and
CC       RUNX2 (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + [histone] = CoA + acetyl-
CC       [histone].
CC   -!- SUBUNIT: Component of the MOZ/MORF complex composed at least of
CC       ING5, MYST3/MOZ, MYST4/MORF, MEAF6 and one of BRPF1, BRD1/BRPF2
CC       and BRPF3 (By similarity). Interacts with RUNX2 (By similarity).
CC       Interacts with RUNX1; phosphorylation of RUNX1 enhances the
CC       interaction.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- DOMAIN: The N-terminus is involved in transcriptional activation
CC       while the C-terminus is involved in transcriptional repression (By
CC       similarity).
CC   -!- PTM: Autoacetylated (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC   -!- SIMILARITY: Contains 1 C2HC-type zinc finger.
CC   -!- SIMILARITY: Contains 1 H15 (linker histone H1/H5 globular) domain.
CC   -!- SIMILARITY: Contains 2 PHD-type zinc fingers.
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DR   EMBL; AC115361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK028058; BAC25728.1; -; mRNA.
DR   EMBL; AK036885; BAC29621.1; -; mRNA.
DR   EMBL; AK039615; BAC30401.1; -; mRNA.
DR   EMBL; AK054322; BAC35729.1; -; mRNA.
DR   IPI; IPI00380122; -.
DR   UniGene; Mm.182776; -.
DR   ProteinModelPortal; Q8BZ21; -.
DR   SMR; Q8BZ21; 98-163, 207-313, 506-778.
DR   STRING; Q8BZ21; -.
DR   PhosphoSite; Q8BZ21; -.
DR   PRIDE; Q8BZ21; -.
DR   Ensembl; ENSMUST00000044331; ENSMUSP00000038181; ENSMUSG00000031540.
DR   Ensembl; ENSMUST00000110696; ENSMUSP00000106324; ENSMUSG00000031540.
DR   UCSC; uc009lec.1; mouse.
DR   MGI; MGI:2442415; Myst3.
DR   HOGENOM; HBG446384; -.
DR   HOVERGEN; HBG052563; -.
DR   InParanoid; Q8BZ21; -.
DR   OrthoDB; EOG48KR9D; -.
DR   PhylomeDB; Q8BZ21; -.
DR   BRENDA; 2.3.1.48; 244.
DR   ArrayExpress; Q8BZ21; -.
DR   Bgee; Q8BZ21; -.
DR   Genevestigator; Q8BZ21; -.
DR   GermOnline; ENSMUSG00000031540; Mus musculus.
DR   GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0004402; F:histone acetyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0016563; F:transcription activator activity; ISS:UniProtKB.
DR   GO; GO:0008134; F:transcription factor binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0035162; P:embryonic hemopoiesis; IMP:MGI.
DR   GO; GO:0043966; P:histone H3 acetylation; ISS:UniProtKB.
DR   GO; GO:0030099; P:myeloid cell differentiation; ISS:UniProtKB.
DR   GO; GO:0016481; P:negative regulation of transcription; ISS:UniProtKB.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   GO; GO:0035019; P:somatic stem cell maintenance; IMP:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR005818; Histone_H1/H5.
DR   InterPro; IPR002717; MOZ_SAS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.40.630.30; Acyl_CoA_acyltransferase; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 2.
DR   Pfam; PF01853; MOZ_SAS; 1.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00526; H15; 1.
DR   SMART; SM00249; PHD; 2.
DR   SMART; SM00184; RING; 2.
DR   SUPFAM; SSF55729; Acyl_CoA_acyltransferase; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 2.
DR   PROSITE; PS51504; H15; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Acyltransferase; Chromatin regulator;
KW   Metal-binding; Nucleus; Phosphoprotein; Repeat; Repressor;
KW   Transcription; Transcription regulation; Transferase; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   2003       Histone acetyltransferase MYST3.
FT                                /FTId=PRO_0000051573.
FT   DOMAIN       95    171       H15.
FT   ZN_FING     206    265       PHD-type 1.
FT   ZN_FING     262    313       PHD-type 2.
FT   ZN_FING     537    559       C2HC-type.
FT   REGION        1    144       Required for activation of RUNX1-1 (By
FT                                similarity).
FT   REGION       52    166       Required for nuclear localization (By
FT                                similarity).
FT   REGION      312    663       Interaction with RUNX1-1 (By similarity).
FT   REGION      487    777       Catalytic (By similarity).
FT   REGION      506    809       Mediates interaction with BRPF1, required
FT                                for histone H3 acetyltransferase activity
FT                                (By similarity).
FT   REGION      644    648       Acetyl-CoA binding (By similarity).
FT   REGION      653    659       Acetyl-CoA binding (By similarity).
FT   REGION     1511   1636       Interaction with RUNX1-2 (By similarity).
FT   REGION     1912   1947       Required for activation of RUNX1-2 (By
FT                                similarity).
FT   COMPBIAS    989    995       Poly-Glu.
FT   COMPBIAS   1019   1026       Poly-Arg.
FT   COMPBIAS   1066   1079       Poly-Glu.
FT   COMPBIAS   1107   1114       Poly-Glu.
FT   COMPBIAS   1149   1176       Lys-rich.
FT   COMPBIAS   1232   1238       Poly-Glu.
FT   COMPBIAS   1405   1408       Poly-Glu.
FT   COMPBIAS   1471   1591       Ser-rich.
FT   COMPBIAS   1601   1703       Gln-rich.
FT   COMPBIAS   1896   1976       Met-rich.
FT   ACT_SITE    645    645       Nucleophile (By similarity).
FT   BINDING     683    683       Acetyl-CoA (By similarity).
FT   MOD_RES     350    350       N6-acetyllysine (By similarity).
FT   MOD_RES     355    355       N6-acetyllysine (By similarity).
FT   MOD_RES     417    417       Phosphothreonine (By similarity).
FT   MOD_RES     419    419       Phosphoserine (By similarity).
FT   MOD_RES     448    448       Phosphothreonine (By similarity).
FT   MOD_RES     472    472       Phosphoserine (By similarity).
FT   MOD_RES     603    603       N6-acetyllysine (By similarity).
FT   MOD_RES     816    816       N6-acetyllysine (By similarity).
FT   MOD_RES     941    941       Phosphoserine (By similarity).
FT   MOD_RES    1007   1007       N6-acetyllysine (By similarity).
FT   MOD_RES    1115   1115       Phosphoserine.
SQ   SEQUENCE   2003 AA;  224919 MW;  93D0D687A1621B31 CRC64;
     MVKLANPLYT EWILEAIKKV KKQKQRPSEE RICNAVSSSH GLDRRTVLEQ LELSVKDGTI
     LKVSNKGLNS YKDPDNPGRI ALPKPRNHGK LDTKQSVDWN KLLKRAFEGL AETGGSTLKS
     IERFLKSQKD VSAACGGSAA PGFHQQLRLA IKRAVGHGRL LKDGPLYRLN TKAASAEGKE
     GCESLSCLPP VSLLPHEKDK PVAEPIPICS FCLGTKEQNR EKQPEELVSC ADCGNSGHPS
     CLKFSPELTV RVKALRWQCI ECKTCSSCRD QGKNADNMLF CDSCDRGFHM ECCDPPLTRM
     PKGMWICQIC RPRKKGRKLL QKKAAQIKRR YANPIGRPKN RLKKQNTVSK GPFSKVRTGP
     GRGRKRKITV SSQSASSSEE GYLERIDGLD FCRDSNAPLK FNKKTKGLID GLTKFFTPSP
     DGRKARGEVV DYSEQYRIRK KGNRKSSTSD WPTDNQDGWE SKQENEERLF GSQEIMTERD
     MELFRDIQEQ ALQKVGVTGP PDPQVRCPSV IEFGKYEIHT WYSSPYPQEY SRLPKLYLCE
     FCLKYMKSRT ILQQHMKKCG WFHPPANEIY RKNNISVFEV DGNVSTIYCQ NLCLLAKLFL
     DHKTLYYDVE PFLFYVLTQN DVKGCHLVGY FSKEKHCQQK YNVSCIMILP QYQRKGYGRF
     LIDFSYLLSK REGQAGSPEK PLSDLGRLSY MAYWKSVILE CLYHQNDKQI SIKKLSKLTG
     VCPQDITSTL HHLRMLDFRS DQFVIIRREK LIQDHMAKLQ LNLRPVDVDP ECLRWTPVIV
     SNSVVSEDED EEADEGEKEE PQGQERELET RVKVGKSVSR EKKDQESSSL IETDKKPEVK
     ELASSSRLSK QALPRDSLPA NSQPPRRGRC GRKNRKTQER FGDKDSKMLV DETLSASQEQ
     YGDCEEKSET SQERFTEMEE QLAAPQVQAD GKPDIPKGRF SESVELWRGQ LKKSPETLKC
     RLPEGNDRLP CCYTDGDRAF FRGFSESSEE EEEPESPRSN SPPILTKPTL KRKKPILHRR
     RRVRKRKHHN SSVVTETISE TTEVLDEPFE DSDSERPMPR LEPTFEMEEE EEEEEEESEL
     FPRGYFHCLS SQDILRCQSS SKRPSKEEEE EEEESDDADD TPVLKPVSLL RKCDVNSASL
     EPDTSTPMKK KKGWPKGKSR KPIHWKKRPG RKPGFKLNQE IIAASAQECI VEPVVPIKPG
     RKPRTQENEE IVEVKEDLLE ERKEEMHTEP DEEAEEEEDT TSSDIRAMSP LDSSNSPEAE
     PKEPEPEEED EKPSDDQRQS EEEPQELEEQ EQEEEDEVTT EANQNEDHDA DDEDEGHLDS
     LKTKEPEEQP AREDDKEEPG IQGSFLAANM QDSRENTKDK DEAEPDSEED QPSHEASVVS
     ETMPGSEEDH EEDSNTKEEL IELKEEEEIP HSELDLETVQ AVQSLTQEES SEHEGAYQDC
     EETLAACQTL QSYTHTDEDP QMSMVEDCHA SEHNSPISSI PSHPSQSVRS VNSPSMPALE
     SGYTQISPEQ GSLSAPSMQN METSPMMDVP SVSDHSQQVV DSGFSDLGSI ESTTENYENP
     SSYDSTMGSS ICGNNSSQSS CSYGGLSSSS SLTQNSCVVT QQMANMGNSC SMLQQNTVQP
     AANCNIKSPQ TCVVERPPSN QQPPPPPPPP PPPQQPQPPP QQQAAPQPPP PQPQQQQQQQ
     QQPPPPQQQP QPPPPQQQPP LSQCSMNNSF TAAPMIMEIP ESGSTGNISI YERIPGDFGA
     GSYSQPSATF SLAKLQQLTN TIMDPHAMPY SHSPAVTSYA TSVSLSNTGL AQLAPSHPLA
     GTPQAQATMT PPPNLASTTM NLTSPLLQCN MSATNIGIPH TQRLQGQMPV KGHISIRSKS
     APLPSATAHQ QQLYGRSPPA VAMQAGPRAL AVQRGMNMGV NLMPTPAYNV NSMNMNTLNA
     MNSYRMTQPM MNSSYHSNPA YMNQTAQYPM QMQMGMMGSQ AYTQQPMQPN PHGNMMYTGP
     SHHSYMNAAG VPKQSLNGPY MRR
//
ID   ASXL2_MOUSE             Reviewed;        1370 AA.
AC   Q8BZ32; Q3TRU9; Q80TA5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 51.
DE   RecName: Full=Putative Polycomb group protein ASXL2;
DE   AltName: Full=Additional sex combs-like protein 2;
GN   Name=Asxl2; Synonyms=Kiaa1685;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 311-1370.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
CC   -!- FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins act
CC       by forming multiprotein complexes, which are required to maintain
CC       the transcriptionally repressive state of homeotic genes
CC       throughout development. PcG proteins are not required to initiate
CC       repression, but to maintain it during later stages of development.
CC       They probably act via methylation of histones, rendering chromatin
CC       heritably changed in its expressibility (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- DOMAIN: Contains one Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif, which may
CC       be required for an association with nuclear receptors (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the Asx family.
CC   -!- SIMILARITY: Contains 1 PHD-type zinc finger.
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DR   EMBL; AK036839; BAC29602.1; -; mRNA.
DR   EMBL; AK162455; BAE36927.1; -; mRNA.
DR   EMBL; AK122540; BAC65822.1; -; mRNA.
DR   IPI; IPI00331397; -.
DR   RefSeq; NP_766009.2; NM_172421.3.
DR   UniGene; Mm.120475; -.
DR   STRING; Q8BZ32; -.
DR   PhosphoSite; Q8BZ32; -.
DR   PRIDE; Q8BZ32; -.
DR   Ensembl; ENSMUST00000049021; ENSMUSP00000036720; ENSMUSG00000037486.
DR   GeneID; 75302; -.
DR   KEGG; mmu:75302; -.
DR   UCSC; uc007mwq.1; mouse.
DR   CTD; 75302; -.
DR   MGI; MGI:1922552; Asxl2.
DR   GeneTree; ENSGT00520000055578; -.
DR   HOGENOM; HBG713010; -.
DR   HOVERGEN; HBG106941; -.
DR   InParanoid; Q8BZ32; -.
DR   ArrayExpress; Q8BZ32; -.
DR   Bgee; Q8BZ32; -.
DR   CleanEx; MM_ASXL2; -.
DR   Genevestigator; Q8BZ32; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   PROSITE; PS01359; ZF_PHD_1; FALSE_NEG.
DR   PROSITE; PS50016; ZF_PHD_2; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Metal-binding; Nucleus; Phosphoprotein; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1   1370       Putative Polycomb group protein ASXL2.
FT                                /FTId=PRO_0000313827.
FT   ZN_FING    1332   1369       PHD-type; atypical.
FT   MOTIF       178    182       Nuclear localization signal (Potential).
FT   MOTIF       258    262       LXXLL motif.
FT   COMPBIAS     95    166       Ser-rich.
FT   COMPBIAS    176    179       Poly-Gln.
FT   COMPBIAS    258    262       Poly-Leu.
FT   COMPBIAS    607    637       Ala-rich.
FT   COMPBIAS    640    692       Gly-rich.
FT   MOD_RES     136    136       Phosphoserine (By similarity).
FT   MOD_RES     143    143       Phosphoserine (By similarity).
FT   MOD_RES     146    146       Phosphoserine (By similarity).
FT   MOD_RES     150    150       Phosphoserine (By similarity).
FT   MOD_RES     782    782       Phosphoserine (By similarity).
FT   MOD_RES     793    793       Phosphoserine (By similarity).
FT   CONFLICT    564    564       V -> S (in Ref. 1; BAE36927).
FT   CONFLICT    621    621       E -> K (in Ref. 1; BAE36927 and 2;
FT                                BAC65822).
FT   CONFLICT    627    627       A -> P (in Ref. 1; BAE36927).
FT   CONFLICT    646    646       P -> L (in Ref. 2; BAC65822).
FT   CONFLICT    686    686       G -> V (in Ref. 1; BAE36927).
SQ   SEQUENCE   1370 AA;  147107 MW;  5E93DCF61F64861B CRC64;
     MREKGRRKKG RTWAEAAKTV LEKYPNTPMS HKEILQVIQR EGLKEIRSGT SPLACLNAML
     HTNSRGEEGI FYKVPGRMGV YTLKKDVPDG VKELSECSEE SSDGQSDSHS SDNSSSSDGG
     SNKEGRKSRW KRKVSSRLSH PPSPPSGCPS PTIPASKVIS PSQKHSKKAL KQALKQQQQK
     KKQQQCRPSM SISNQHLSLK TVKAASDSVP AKPGQMKRTK CADIDVETPD SILVNTNLRA
     LINKHTFSVL PGDCQQRLLL LLPEVDRQVG PDGLMKLNGS ALNNEFFTSA AQGWKERLSE
     GEFTPEMQVR IRQEIEKEKK VELWKEQFFE NYYGQSSGLS LEDSQKLTAS SSDPKAKKTP
     AEQPKSILPS EASPVRIVPV VPQSECKEEA VQIPSPSQKE ENQDEARPDS KSPEPVLASA
     SNTNELITMK PIKSPKDEGL LEQKPVACAE QESEKENHVT TTSRNNKSEN QEALAISPSK
     SKNAGLQKPI IKPVAEASPL NPDMKMPPAT VTDQIQESLK RKSSLTDEEA TSSWEKRPRI
     TENRQHQQPF QVSPQPFLNR GDRVQVRKVP PLKIPVSRIS PMLFSTSQVS PRARFPISIT
     SPYRTGARTL ADIKAKAQLV EAQKAAAAAA AAAAAAASVG GTIPGPGPGG GQSPREGGER
     KIAGGGSAGS DPVSTNGKGP TLELAGTGSR GGTRELLPCG PQPETNMPGQ AQPPGISGAQ
     LQQTSSVPTG LASSGACTSV PLPAHIEISN SEKPNLHKAT ATAASPCHLQ DPRSCRLEKA
     LSPTGPPLIS GASTVYFVAD GTVEPKAGSN KNAPKPSALA KTTAPAPLDM TSSPVTTASL
     EKLPVPQISG TATSTGSAPS SSTLPAASSL KTPGTSANMN GPISRTSSSI PANNPLVTQL
     LQGKDVPLEQ ILPKPLTKIE MKTVPLTTKE EKGIGIFPGI SVMESSSREE VNGRQAHLAI
     PQLGKPLQSK QLSQVPRPVF TAKDRKDPCI DTHQYREGLS KTTQDQLFQT LIQRAQRQSV
     LSFVPPSQFN FAHSGFHLED ISTSQKFMLG FAGRRTSKPA MAGHYLLNIS TYGRGTENIK
     RTHSVNPDDR FCLSSPTEAL RMGHADYKNT TGEISSKEDE SDEDRVGDEQ EPISVKEEPW
     ASQSSGRHPH HGEASSTNDC LASKNGKTEA PVSEQTTLGQ ENYIFSRGQA SDEKSLPRDF
     IPAAHKQMTH AVRGKTVCSS PELFNSTALS LPADSPTHQP LLLPPLQTPK LYGSPTQIGP
     SYRGMINVST SSDMDHNSAI PGSQVSSNVG DVMSFSVTVT TIPASQAMNP SSHGQTIPVQ
     TFPDDNSIED TPSKCYCRLK AMIMCKGCGA FCHDDCIGPS KLCVSCLVVR
//
ID   ZN609_MOUSE             Reviewed;        1413 AA.
AC   Q8BZ47; Q05DD7; Q6PD47; Q6ZQE3;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Zinc finger protein 609;
GN   Name=Znf609; Synonyms=Kiaa0295, Zfp609;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1136.
RC   TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-1413.
RC   STRAIN=C57BL/6J; TISSUE=Bone;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 610-1413.
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-575 AND SER-577, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SIMILARITY: Contains 1 C2H2-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC29549.1; Type=Erroneous initiation;
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DR   EMBL; AC151906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC121979; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC016271; AAH16271.1; -; mRNA.
DR   EMBL; BC058943; AAH58943.1; ALT_SEQ; mRNA.
DR   EMBL; AK036715; BAC29549.1; ALT_INIT; mRNA.
DR   EMBL; AK129111; BAC97921.1; -; mRNA.
DR   IPI; IPI00227314; -.
DR   RefSeq; NP_766124.2; NM_172536.3.
DR   UniGene; Mm.139231; -.
DR   UniGene; Mm.477320; -.
DR   PhosphoSite; Q8BZ47; -.
DR   PRIDE; Q8BZ47; -.
DR   Ensembl; ENSMUST00000113785; ENSMUSP00000109415; ENSMUSG00000040524.
DR   GeneID; 214812; -.
DR   KEGG; mmu:214812; -.
DR   UCSC; uc009qdw.1; mouse.
DR   CTD; 214812; -.
DR   MGI; MGI:2674092; Zfp609.
DR   eggNOG; roNOG11793; -.
DR   GeneTree; ENSGT00390000008748; -.
DR   HOGENOM; HBG717404; -.
DR   HOVERGEN; HBG054557; -.
DR   InParanoid; Q8BZ47; -.
DR   OMA; MGEPFTV; -.
DR   OrthoDB; EOG490784; -.
DR   NextBio; 374482; -.
DR   ArrayExpress; Q8BZ47; -.
DR   Bgee; Q8BZ47; -.
DR   CleanEx; MM_ZFP609; -.
DR   Genevestigator; Q8BZ47; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   SMART; SM00355; ZnF_C2H2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Phosphoprotein; Zinc; Zinc-finger.
FT   CHAIN         1   1413       Zinc finger protein 609.
FT                                /FTId=PRO_0000280423.
FT   ZN_FING     495    520       C2H2-type.
FT   COMPBIAS    378    460       Ser-rich.
FT   COMPBIAS    724    734       Poly-Lys.
FT   COMPBIAS    955   1020       Gln-rich.
FT   COMPBIAS   1335   1338       Poly-Gly.
FT   COMPBIAS   1368   1373       Poly-His.
FT   MOD_RES     358    358       Phosphoserine (By similarity).
FT   MOD_RES     381    381       Phosphothreonine (By similarity).
FT   MOD_RES     467    467       Phosphoserine (By similarity).
FT   MOD_RES     470    470       Phosphoserine (By similarity).
FT   MOD_RES     559    559       Phosphoserine (By similarity).
FT   MOD_RES     565    565       Phosphothreonine (By similarity).
FT   MOD_RES     575    575       Phosphoserine.
FT   MOD_RES     577    577       Phosphoserine.
FT   MOD_RES     745    745       Phosphothreonine (By similarity).
FT   MOD_RES     803    803       Phosphoserine (By similarity).
FT   MOD_RES     841    841       Phosphoserine (By similarity).
FT   MOD_RES     844    844       Phosphotyrosine (By similarity).
FT   MOD_RES     845    845       Phosphoserine (By similarity).
FT   MOD_RES     848    848       Phosphoserine (By similarity).
FT   MOD_RES    1057   1057       Phosphoserine (By similarity).
FT   CONFLICT    697    697       S -> G (in Ref. 3; BAC29549).
FT   CONFLICT    735    735       D -> K (in Ref. 2; AAH16271).
FT   CONFLICT    914    914       S -> N (in Ref. 4; BAC97921).
SQ   SEQUENCE   1413 AA;  151117 MW;  6BC74B23591605FF CRC64;
     MSLSSGACGG KGVDANPVET YDSGDEWDIG VGNLIIDLDA DLEKDQQKLE MSGSKEVGIP
     APNAVATLPD NIKFVTPVPG PQGKEGKSKS KRSKSGKDAS KPTPGTSLFS PSEGAASKKE
     VQGRAGDGAS AGGLVAAVAP KGSEKAAKAS RSVAGSKKEK ENSSSKGKKE RSEGVGTCSE
     KDPGVLQPVP LGGRGSQYDG SAGMDTGTVE PLGSIAIEPG AALNPLGTKP EPEEGENECR
     PLKKVKSEKM ESPVSTPAVL PLHLLVPVVN NDISSPCEQI MVRTRSVGVN TCDVALATEP
     ECLGPCEPGT SVNLEGIVWQ ETEDGMLVVN VTWRNKTYVG TLLDCTRHDW APPRFCDSPT
     SDLEMRNGRG RGKRMRPSSN TPVSEAAAAS DSKGTSSSSK TRAGANSKGR RGSQNSSEHR
     PPASSTSEDV KASPSSANKR KSKPLSDMEL NSSSEDSKGS KRVRTNSMGS ATGPLPGTKV
     EPTLVDRNCP SPVLIDCPHP NCNKKYKHIN GLKYHQAHAH TDDDSKPEAD GDSEYGEEPA
     LHADLSCNGA PVPQKGSLSP ARSATPKVRL VEPHSPSPSS KFSTKGLCKK KLSGEGDTDP
     GALSNDGSDD GPSVMDETSN DAFDSLERKC MEKEKCKKPS SLKSEKIPSK SLKSARPIAP
     AIPPQQIYTF QTATFTAASP GSSSGLTTTV VQAMPNSPQL KPIQPKPTVM GEPFTVNPAL
     TPAKDKKKKD KKKKDSSKEL ESPLTPGKVC RAEEGKSPFR DAAGDGIKVE SLLNGSSESH
     QSRLASIKAE ADKIYSFTDN APSPSIGGSS RLDSTTPTQP LTPLHVVTQN GAEASSVKTN
     SPAYSDISDA GEDGEGKVDS AKSKDPEQLV KEGAKKTLFP PQPQSKDSPY YQGFESYYSP
     GYAQSSPGTL TSSSQAGMEG QPLKTKKDEE PESVEGKVKN DVCEEKKPEL SNSSQQPSVI
     QQRPNMYMQS LYYNQYAYVP PYGYSDQSYH SHLLSTNTAY RQQYEEQQKR QSLEQQQQQQ
     RGLDKKTEMG LKEREASLKE EWKQKPSIPP TLTKAPSLTD LVKSGPGKAK EPGTDPAKSV
     IIPKLDDSSK LPSQPPEGLK GKLGEASHLG KEASEAKTGT ECGRQAEVDP ILWYRQETES
     RMWTYVYPAK YSDIKSEDDR WKEERDRKLK EDRSRSKDSV PKEDGKESTS SDCKLPPSEE
     SRLGSKEPRP SVHVPVSSPL TQHQSYIPYM HGYSYSQSYD PNHPSYRGMP AVMMQNYPGS
     YLPSSYSFSP YGSKVSGGED ADKARASPSV SCKASSESKA LDILQQHASH YKSKSPTISD
     KNSQERDRGG CGVVGGGGSC GSVAGAGGTD RSADRPRTSP SQRLMSTHHH HHHLGYSLLP
     AQYNLPYAAG LSSTAIVASQ QGSTPSLYPP PRR
//
ID   PRDM8_MOUSE             Reviewed;         687 AA.
AC   Q8BZ97;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=PR domain zinc finger protein 8;
DE   AltName: Full=PR domain-containing protein 8;
GN   Name=Prdm8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains 2 C2H2-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 SET domain.
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DR   EMBL; AK036202; BAC29345.1; -; mRNA.
DR   IPI; IPI00227431; -.
DR   RefSeq; NP_084223.2; NM_029947.2.
DR   UniGene; Mm.332511; -.
DR   ProteinModelPortal; Q8BZ97; -.
DR   SMR; Q8BZ97; 16-139, 149-191, 622-647.
DR   STRING; Q8BZ97; -.
DR   PRIDE; Q8BZ97; -.
DR   Ensembl; ENSMUST00000112959; ENSMUSP00000108583; ENSMUSG00000035456.
DR   GeneID; 77630; -.
DR   KEGG; mmu:77630; -.
DR   CTD; 77630; -.
DR   MGI; MGI:1924880; Prdm8.
DR   eggNOG; roNOG09673; -.
DR   GeneTree; ENSGT00520000055673; -.
DR   HOVERGEN; HBG053674; -.
DR   InParanoid; Q8BZ97; -.
DR   OrthoDB; EOG4BG8VX; -.
DR   NextBio; 347264; -.
DR   ArrayExpress; Q8BZ97; -.
DR   Bgee; Q8BZ97; -.
DR   Genevestigator; Q8BZ97; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0022008; P:neurogenesis; IDA:MGI.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 1.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   PROSITE; PS50280; SET; FALSE_NEG.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    687       PR domain zinc finger protein 8.
FT                                /FTId=PRO_0000047765.
FT   DOMAIN        8    135       SET.
FT   ZN_FING     154    182       C2H2-type 1; atypical.
FT   ZN_FING     624    647       C2H2-type 2.
FT   COMPBIAS    202    207       Poly-Gly.
FT   COMPBIAS    210    219       Poly-Gln.
FT   COMPBIAS    284    488       Gly-rich.
FT   COMPBIAS    539    597       Ala-rich.
SQ   SEQUENCE   687 AA;  70886 MW;  B33B2DEBC3512B3E CRC64;
     MEDSGIQRGI WDGDAKAVQQ CLTDIFTSVY TTCDIPENAI FGPCVLSHTS LYDSIAFVAL
     KSTDKRTVPY IFRVDTSAAN GSSEGLMWLR LVQSARDKEE QNLEAYIKNG QLFYRSLRRI
     AKDEELLVWY GKELTELLLL CPSRAHKMNG SSPYTCLECS QRFQFEFPYV AHLRFRCPKR
     LHSTDANPQD EQGGGLGTKD HGGGGGGKEQ QQQQQQQQQE APLIPGPKFC KAGPIHHYPA
     SSPEASNPPG SAGASSAKPS TDFHNLAREL ENSRGNSSCV AAPGVGSGGS GHQEAELSPD
     GVATGGCKGK RRFPEEAAAE GGGAGLAGGR ARFSERPLAT SKEELVCTPQ QYRAAGSYFG
     LEENGRLFAP PSPETGEAKR SAFVEVKKAG RAVGLQEEAA ATDGAGGTAE DPDAGGGVAG
     GGSNGSSTPA AGSPGAPEKL LAPRPGGSLP GRLEGGSPAR GSAFTSVSQL GGGGGAGTAG
     TAGGSGGGQT AASDERKSAF SQPARSFSQL SPLVLGQKLG ALEPCHPGDG VGPTRLYPAA
     ADPLAVKLQG AADLNGACGP LASGGGGGLP KQSPFLYATA FWPKSSAAAA AAAAAAAGPL
     QLQLPSALTL LPPSFTSLCL PAQNWCAKCN ASFRMTSDLV YHMRSHHKKE YAMEPLVKAA
     AGGETQVPHL QRVLQGASPP VPAHDLA
//
ID   DYN3_MOUSE              Reviewed;         863 AA.
AC   Q8BZ98; B2RUH0; Q3UGY9; Q80TR2; Q8BWW6;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Dynamin-3;
DE            EC=3.6.5.5;
GN   Name=Dnm3; Synonyms=Kiaa0820;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, Cerebellum, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 394-863 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-763, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Microtubule-associated force-producing protein involved
CC       in producing microtubule bundles and able to bind and hydrolyze
CC       GTP. Most probably involved in vesicular trafficking processes, in
CC       particular endocytosis (By similarity).
CC   -!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity). Note=Microtubule-associated (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BZ98-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BZ98-2; Sequence=VSP_031548;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the dynamin family.
CC   -!- SIMILARITY: Contains 1 GED domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
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DR   EMBL; AK036199; BAC29343.1; -; mRNA.
DR   EMBL; AK049724; BAC33895.1; -; mRNA.
DR   EMBL; AK147678; BAE28068.1; -; mRNA.
DR   EMBL; BC141143; AAI41144.1; -; mRNA.
DR   EMBL; BC141144; AAI41145.1; -; mRNA.
DR   EMBL; AK122379; BAC65661.1; -; Transcribed_RNA.
DR   IPI; IPI00227432; -.
DR   IPI; IPI00625738; -.
DR   RefSeq; NP_001033708.1; NM_001038619.1.
DR   RefSeq; NP_766234.1; NM_172646.2.
DR   UniGene; Mm.441620; -.
DR   HSSP; P21575; 2AKA.
DR   ProteinModelPortal; Q8BZ98; -.
DR   SMR; Q8BZ98; 6-344, 516-624.
DR   STRING; Q8BZ98; -.
DR   PhosphoSite; Q8BZ98; -.
DR   PRIDE; Q8BZ98; -.
DR   Ensembl; ENSMUST00000070330; ENSMUSP00000064538; ENSMUSG00000040265.
DR   Ensembl; ENSMUST00000086074; ENSMUSP00000083241; ENSMUSG00000040265.
DR   GeneID; 103967; -.
DR   KEGG; mmu:103967; -.
DR   UCSC; uc007dga.1; mouse.
DR   CTD; 103967; -.
DR   MGI; MGI:1341299; Dnm3.
DR   GeneTree; ENSGT00600000084144; -.
DR   HOGENOM; HBG434086; -.
DR   HOVERGEN; HBG107833; -.
DR   InParanoid; Q8BZ98; -.
DR   OrthoDB; EOG49GKG1; -.
DR   BRENDA; 3.6.5.5; 244.
DR   NextBio; 356261; -.
DR   ArrayExpress; Q8BZ98; -.
DR   Bgee; Q8BZ98; -.
DR   CleanEx; MM_DNM3; -.
DR   Genevestigator; Q8BZ98; -.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003774; F:motor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   InterPro; IPR022812; Dynamin.
DR   InterPro; IPR000375; Dynamin_central.
DR   InterPro; IPR001401; Dynamin_GTPase.
DR   InterPro; IPR019762; Dynamin_GTPase_CS.
DR   InterPro; IPR003130; GED.
DR   InterPro; IPR020850; GTPase_effector_domain_GED.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Pfam; PF01031; Dynamin_M; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   Pfam; PF02212; GED; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00195; DYNAMIN.
DR   SMART; SM00053; DYNc; 1.
DR   SMART; SM00302; GED; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS00410; DYNAMIN; 1.
DR   PROSITE; PS51388; GED; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton;
KW   Endocytosis; GTP-binding; Hydrolase; Microtubule; Motor protein;
KW   Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1    863       Dynamin-3.
FT                                /FTId=PRO_0000319951.
FT   DOMAIN      515    621       PH.
FT   DOMAIN      653    744       GED.
FT   NP_BIND      38     45       GTP (By similarity).
FT   NP_BIND     136    140       GTP (By similarity).
FT   NP_BIND     205    208       GTP (By similarity).
FT   MOD_RES     594    594       N6-acetyllysine (By similarity).
FT   MOD_RES     763    763       Phosphoserine.
FT   VAR_SEQ     628    631       Missing (in isoform 2).
FT                                /FTId=VSP_031548.
FT   CONFLICT    139    139       G -> A (in Ref. 1; BAE28068).
FT   CONFLICT    532    549       Missing (in Ref. 3; BAC65661).
SQ   SEQUENCE   863 AA;  97190 MW;  8BDBB091CB10D264 CRC64;
     MGNREMEELI PLVNRLQDAF SALGQSCLLE LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG
     SGIVTRRPLV LQLVTSKAEY AEFLHCKGKK FTDFDEVRHE IEAETDRVTG MNKGISSIPI
     NLRVYSPHVL NLTLIDLPGI TKVPVGDQPP DIEYQIRDMI MQFITRENCL ILAVTPANTD
     LANSDALKLA KEVDPQGLRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YVGVVNRSQK
     DIDGKKDIKA AMLAERKFFL SHPAYRHIAD RMGTPHLQKV LNQQLTNHIR DTLPNFRNKL
     QGQLLSIEHE VEAFKNFKPE DPTRKTKALL QMVQQFAVDF EKRIEGSGDQ VDTLELSGGA
     KINRIFHERF PFEIVKMEFN EKELRREISY AIKNIHGIRT GLFTPDMAFE AIVKKQIVKL
     KGPSLKSVDL VMQELINTVK KCTKRLANFP RLCEETERIV ANHIREREGK TKDQVLLLID
     IQVSYINTNH EDFIGFANAQ QRSSQVHKKS TIGNQVIRKG WLTVSNIGIM KGGSKGYWFV
     LTAESLSWYK DDEEKEKKYM LPLDNLKVRD VEKGFMSSKH VFALFNTEQR NVYKDYRFLE
     LACDSQEDVD SWKASLLRAG VYPDKSVGSN KTENDENGQA ENFSMDPQLE RQVETIRNLV
     DSYMSIINKC IRDLIPKTIM HLMINNVKDF INSELLAQLY SSEDQNTLME ESAEQAQRRD
     EMLRMYQALK EALAIIGDIN TATVSTPAPP PVDDSWLQHS RRSPPPSPTT QRRLTISAPL
     PRPTSGRGPA PAIPSPGPHS GAPPVPFRPG PLPPFPNSSD SFGAPPQVPS RPTRAPPSVP
     SRRPPPSPTR PTIIRPLESS LLD
//
ID   CO027_MOUSE             Reviewed;         538 AA.
AC   Q8BZB3; B1B1B3; Q6NVG3;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Transmembrane protein C15orf27 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Embryonic brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BZB3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BZB3-2; Sequence=VSP_022109, VSP_022110, VSP_019514,
CC                                  VSP_019515;
CC         Note=No experimental confirmation available;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK036040; BAC29283.1; -; mRNA.
DR   EMBL; CT025532; CAO77737.1; -; Genomic_DNA.
DR   EMBL; BC068128; AAH68128.1; -; mRNA.
DR   IPI; IPI00227460; -.
DR   IPI; IPI00462880; -.
DR   RefSeq; NP_766511.1; NM_172923.3.
DR   UniGene; Mm.24361; -.
DR   ProteinModelPortal; Q8BZB3; -.
DR   PhosphoSite; Q8BZB3; -.
DR   PRIDE; Q8BZB3; -.
DR   Ensembl; ENSMUST00000034862; ENSMUSP00000034862; ENSMUSG00000032313.
DR   Ensembl; ENSMUST00000085754; ENSMUSP00000082906; ENSMUSG00000032313.
DR   GeneID; 244886; -.
DR   KEGG; mmu:244886; -.
DR   UCSC; uc009psj.1; mouse.
DR   UCSC; uc009psk.1; mouse.
DR   MGI; MGI:2142980; AI118078.
DR   eggNOG; roNOG11572; -.
DR   GeneTree; ENSGT00530000063670; -.
DR   HOGENOM; HBG445805; -.
DR   HOVERGEN; HBG079803; -.
DR   InParanoid; Q8BZB3; -.
DR   OMA; QREGSNW; -.
DR   OrthoDB; EOG4B5P5J; -.
DR   PhylomeDB; Q8BZB3; -.
DR   NextBio; 386472; -.
DR   ArrayExpress; Q8BZB3; -.
DR   Bgee; Q8BZB3; -.
DR   CleanEx; MM_AI118078; -.
DR   Genevestigator; Q8BZB3; -.
DR   GermOnline; ENSMUSG00000032313; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Glycoprotein; Membrane;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    538       Transmembrane protein C15orf27 homolog.
FT                                /FTId=PRO_0000244096.
FT   TRANSMEM    103    123       Helical; (Potential).
FT   TRANSMEM    131    151       Helical; (Potential).
FT   TRANSMEM    170    190       Helical; (Potential).
FT   COILED      232    278       Potential.
FT   CARBOHYD    380    380       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1     65       Missing (in isoform 2).
FT                                /FTId=VSP_022109.
FT   VAR_SEQ      66     76       SNLDEEYQREG -> MMLFQPHRAFR (in isoform
FT                                2).
FT                                /FTId=VSP_022110.
FT   VAR_SEQ     341    363       DSGAPEPAVCVVTTAAIDIHQPN -> GKSGLGLFACTMQP
FT                                QDTCDPSKP (in isoform 2).
FT                                /FTId=VSP_019514.
FT   VAR_SEQ     364    538       Missing (in isoform 2).
FT                                /FTId=VSP_019515.
SQ   SEQUENCE   538 AA;  58897 MW;  D3F14858BD140C65 CRC64;
     MALVTSFNMA NPQPAIEGGI SEVEIISQQV DEETKSIAPV QLVNFAYRDL PLAAVDLSTG
     GSQLLSNLDE EYQREGSDWL KPCCGKRAAV WQVFLLSASL NSFLVACVIL VVILLTLELL
     IDTKLLQFSN AFQFAGVIHW ISLVILSVFF SETVLRIVVL GIWDYIENKI EVFDGAVIIL
     SLAPMVASTV ANGPRSPWDA ISLIIMFRIW RVKRVIDAYV LPVKLEMEMV TQQYEKAKAI
     QDEQLERLTQ ICQEQGFEIR QLRAHLAQQD LDLAAEREAA LQAPHVLSQP RSRYKVVEAG
     TWAEETAAES IVEELRPSQE ATVKDDMNSY ISQYYNGPSS DSGAPEPAVC VVTTAAIDIH
     QPNVPSDLFS VDLPLKLSGN STCASATSET TSHSTCGSVT RAQSASSQTL GSSTDCSTPR
     EELLPSKPRS SPLPLLLPPQ QLVAEATVQD LMSSLSKDPC PSHKALDPAP LAQPTPLGSV
     QTSPELEHRV SLFNQKNQEA LPVLQINPVI HLQPTAGLEE KFRSLESKEP KLHTVPEA
//
ID   POGZ_MOUSE              Reviewed;        1409 AA.
AC   Q8BZH4; Q4VA94; Q80TZ8; Q8C0K1; Q8K294;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Pogo transposable element with ZNF domain;
GN   Name=Pogz; Synonyms=Kiaa0461;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C3H/He; TISSUE=Mammary tumor, and Mesenchymal stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 557-1409.
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421 AND SER-422, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Plays a role in mitotic cell cycle progression and is
CC       involved in kinetochore assembly and mitotic sister chromatid
CC       cohesion. Probably through its association with CBX5 plays a role
CC       in mitotic chromosome segregation by regulating aurora kinase
CC       B/AURKB activation and AURKB and CBX5 dissociation from chromosome
CC       arms (By similarity).
CC   -!- SUBUNIT: Interacts with CBX1, CBX3, MAD2L2 and ZNF828. Interacts
CC       with CBX5; POGZ competes with PXVXL motif-containing proteins such
CC       as INCENP and TRIM28 for interaction with CBX5. Interacts with
CC       PSIP1 isoform 1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Chromosome (By
CC       similarity). Cytoplasm (By similarity). Note=Recruited to
CC       trimethylated 'Lys-9' of histone H3 (H3K9me3) (By similarity).
CC   -!- SIMILARITY: Contains 9 C2H2-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 DDE domain.
CC   -!- SIMILARITY: Contains 1 HTH CENPB-type DNA-binding domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK030880; BAC27169.1; -; mRNA.
DR   EMBL; AK035255; BAC29003.1; -; mRNA.
DR   EMBL; BC032176; AAH32176.1; -; mRNA.
DR   EMBL; BC096492; AAH96492.1; -; mRNA.
DR   EMBL; AK122288; BAC65570.1; -; mRNA.
DR   IPI; IPI00227539; -.
DR   RefSeq; NP_766271.2; NM_172683.3.
DR   UniGene; Mm.274787; -.
DR   ProteinModelPortal; Q8BZH4; -.
DR   SMR; Q8BZH4; 371-402, 443-670, 767-836, 967-1076.
DR   PhosphoSite; Q8BZH4; -.
DR   PRIDE; Q8BZH4; -.
DR   Ensembl; ENSMUST00000107270; ENSMUSP00000102891; ENSMUSG00000038902.
DR   GeneID; 229584; -.
DR   KEGG; mmu:229584; -.
DR   UCSC; uc008qhc.1; mouse.
DR   CTD; 229584; -.
DR   MGI; MGI:2442117; Pogz.
DR   GeneTree; ENSGT00530000063300; -.
DR   HOGENOM; HBG444509; -.
DR   HOVERGEN; HBG049435; -.
DR   InParanoid; Q8BZH4; -.
DR   OMA; YPPVQRN; -.
DR   OrthoDB; EOG4SXNBN; -.
DR   PhylomeDB; Q8BZH4; -.
DR   NextBio; 379525; -.
DR   ArrayExpress; Q8BZH4; -.
DR   Bgee; Q8BZH4; -.
DR   CleanEx; MM_POGZ; -.
DR   Genevestigator; Q8BZH4; -.
DR   GermOnline; ENSMUSG00000038902; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0000790; C:nuclear chromatin; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051382; P:kinetochore assembly; ISS:UniProtKB.
DR   GO; GO:0007064; P:mitotic sister chromatid cohesion; ISS:UniProtKB.
DR   GO; GO:0045449; P:regulation of transcription; IEA:InterPro.
DR   InterPro; IPR004875; DDE_SF_endonuclease_CENPB-like.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR006600; Pogo/CenpB/PDC2_DNA-bd_HTH.
DR   InterPro; IPR004906; Pogo/CenpB/PDC2_subgr_DNA-bd.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Pfam; PF03184; DDE; 1.
DR   Pfam; PF03221; Transposase_Tc5; 1.
DR   SMART; SM00674; CENPB; 1.
DR   SMART; SM00355; ZnF_C2H2; 8.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
DR   PROSITE; PS51253; HTH_CENPB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Cell cycle; Cell division; Chromosome; Coiled coil;
KW   Cytoplasm; Metal-binding; Nucleus; Phosphoprotein; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1409       Pogo transposable element with ZNF
FT                                domain.
FT                                /FTId=PRO_0000047225.
FT   DOMAIN     1011   1081       HTH CENPB-type.
FT   DOMAIN     1113   1319       DDE.
FT   ZN_FING     372    394       C2H2-type 1; atypical.
FT   ZN_FING     491    513       C2H2-type 2.
FT   ZN_FING     527    550       C2H2-type 3.
FT   ZN_FING     557    580       C2H2-type 4.
FT   ZN_FING     587    610       C2H2-type 5.
FT   ZN_FING     616    638       C2H2-type 6.
FT   ZN_FING     644    667       C2H2-type 7.
FT   ZN_FING     767    790       C2H2-type 8.
FT   ZN_FING     811    836       C2H2-type 9.
FT   REGION      806    846       Required for interaction with CBX5 (By
FT                                similarity).
FT   COILED     1336   1364       Potential.
FT   COMPBIAS    872    927       Pro-rich.
FT   MOD_RES     251    251       Phosphoserine (By similarity).
FT   MOD_RES     258    258       Phosphothreonine (By similarity).
FT   MOD_RES     333    333       Phosphoserine (By similarity).
FT   MOD_RES     416    416       Phosphoserine (By similarity).
FT   MOD_RES     421    421       Phosphoserine.
FT   MOD_RES     422    422       Phosphoserine.
FT   MOD_RES     436    436       Phosphothreonine (By similarity).
FT   MOD_RES     442    442       Phosphoserine (By similarity).
FT   MOD_RES     445    445       Phosphothreonine (By similarity).
FT   MOD_RES     797    797       N6-acetyllysine (By similarity).
FT   MOD_RES    1334   1334       Phosphoserine (By similarity).
FT   MOD_RES    1360   1360       Phosphoserine (By similarity).
FT   CONFLICT    513    515       HVE -> TRP (in Ref. 2; AAH32176).
FT   CONFLICT   1342   1342       Q -> E (in Ref. 1; BAC29003).
SQ   SEQUENCE   1409 AA;  154910 MW;  ED08A5E2C1E719A5 CRC64;
     MADTDLFMEC EEEELEPWQK ISDVIEDSVV EDYNSVDKTT SVSVSQQPVS APVPIAAHAS
     VAGHLSTSTT VSNSGAQNSD STKKTLVTLI ANNNAGNTLV QQGGQPLILT QNPAPGLGTM
     VTQPVLRPVQ VMQNANHVTS SPVASQPIFI TTQGFPVRNV RPVQNAMNQV GIVLNVQQGQ
     TVRPITLVPA PGTQFVKPTV GVPQVFSQMT PVRPGSTMPV RPTTNTFTTV IPATLTIRST
     VPQSQSQQTK STPSTSTTPT ATQPTSLGQL AGQPPGQSNQ TSNPKLAPSF PSPPAVSIAS
     FVTVKRPGVT GENSNEVAKL VNTLNTVPSL GQSPGPVVVS NNSSAQRTSG PESSVKVTSS
     IPVFDLQDGG RKICPRCNAQ FRVTEALRGH MCYCCPEMVE YQKKGKSLDA EPSVPSAAKP
     SSPEKTAPVT STPSSTPIPA LSPPTKVPEP NENAGDAVQT KLIMLVDDFY YGRDGGKAAQ
     LTSFPKVATS FRCPHCTKRL KNNIRFMNHM KHHVELDQQN GEVDGHTICQ HCYRQFSTPF
     QLQCHLENVH SPYESTTKCK ICEWAFESEP LFLQHMKDTH KPGEMPYVCQ VCQYRSSLYS
     EVDVHFRMIH EDTRHLLCPY CLKVFKNGNA FQQHYMRHQK RNVYHCNKCR LQFLFAKDKI
     EHKLQHHKTF RKPKQLEGLK PGTKVTIRAS RGQPRTVPVS SNDAPSGTLQ EAAALTSTDP
     LPVFLYPPVQ RNIQKRAVRK MSVMGRQTCL ECSFEIPDFP NHFPTYVHCS LCRYSTCCSR
     AYANHMINNH VPRKSPKYLA LFKNSVSGIK LACTSCTFAT SVGDAMAKHL VFNPSHRSSN
     ILPRGLSWMS HLRPGQASER VFDWSMKNTY LPPPLVPNKA ATVKPVGVTP AEPQELAGPV
     LQALPSPAST ATPPATPTHP QPSALPPSAT EGTECLNVSE QEEGSPVTQD PEPASGGGGG
     SGVGKKEQLS VKKLRVVLFA LCCNTEQAAE HFRNPQRRIR RWLRRFQASQ GENLEGKYLS
     FEAEEKLAEW VLIQREQQLP VNEETLFQKA TKIGRSLEGG FKISYEWAVR FMLRHHLTPH
     ARRAVAHTLP KHVAENAGLF IEFVQRQIHN QDLPLSMIVA IDEISLFLDT EVLSSDDRKE
     NALQTVGTGE PWCDVVLAIL ADGTVLPTLV FFRGQANRFA NVPDSILLEA KDSGYSDDEI
     MELWSTRVWK KHTACQHSKS MLVMDCHRTH LSEEVLALLS ASSTLPAVVP AGCSSKIQPL
     DVCIKRTVKN FLHKKWKEQA REMADAACDS DVLLQLVLVW LGEVLGVIGD SPELVQRSFL
     VASVLPGPDG NVNSPTRNAD MQEELIASLE EQLKLNGEQS EEHSASAPRP RSSPEETVEP
     ESLHQLFEGE SETESFYGFE EADLDLMEI
//
ID   AF1L1_MOUSE             Reviewed;         768 AA.
AC   Q8BZI0; Q8BKB8;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Actin filament-associated protein 1-like 1;
DE            Short=AFAP1-like protein 1;
GN   Name=Afap1l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343 AND SER-351, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343; SER-353 AND
RP   SER-359, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BZI0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BZI0-2; Sequence=VSP_026860, VSP_026861;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK035227; BAC28988.1; -; mRNA.
DR   EMBL; AK053714; BAC35486.1; -; mRNA.
DR   IPI; IPI00227546; -.
DR   IPI; IPI00457681; -.
DR   RefSeq; NP_849259.2; NM_178928.4.
DR   UniGene; Mm.26632; -.
DR   HSSP; Q8N4X5; 2COF.
DR   ProteinModelPortal; Q8BZI0; -.
DR   SMR; Q8BZI0; 224-316, 414-518.
DR   PhosphoSite; Q8BZI0; -.
DR   PRIDE; Q8BZI0; -.
DR   Ensembl; ENSMUST00000120472; ENSMUSP00000113286; ENSMUSG00000033032.
DR   GeneID; 106877; -.
DR   KEGG; mmu:106877; -.
DR   NMPDR; fig|10090.3.peg.4079; -.
DR   UCSC; uc008fcq.1; mouse.
DR   CTD; 106877; -.
DR   MGI; MGI:2147199; Afap1l1.
DR   eggNOG; roNOG04817; -.
DR   GeneTree; ENSGT00390000003998; -.
DR   HOGENOM; HBG443857; -.
DR   HOVERGEN; HBG106875; -.
DR   InParanoid; Q8BZI0; -.
DR   OrthoDB; EOG4HDST7; -.
DR   NextBio; 358446; -.
DR   ArrayExpress; Q8BZI0; -.
DR   Bgee; Q8BZI0; -.
DR   CleanEx; MM_AFAP1L1; -.
DR   Genevestigator; Q8BZI0; -.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Pfam; PF00169; PH; 2.
DR   SMART; SM00233; PH; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Phosphoprotein; Repeat.
FT   CHAIN         1    768       Actin filament-associated protein 1-like
FT                                1.
FT                                /FTId=PRO_0000295240.
FT   DOMAIN      220    316       PH 1.
FT   DOMAIN      418    512       PH 2.
FT   COILED      611    701       Potential.
FT   COMPBIAS    194    199       Poly-Glu.
FT   MOD_RES     343    343       Phosphoserine.
FT   MOD_RES     351    351       Phosphoserine.
FT   MOD_RES     353    353       Phosphoserine.
FT   MOD_RES     359    359       Phosphoserine.
FT   VAR_SEQ     373    458       KGKKNSLAELKGSMSRAAGRKITRIISFSKKKALSEDLQTF
FT                                SSEDEVPCCGYLNVLVNQGWKERWCRLRCNTLYFHKDRTDL
FT                                HTHV -> RSYHELPLVHAGECQRWEGLCYRSTVTEQITGT
FT                                RVRPLGLSYLVITGRLQGLLGRPEVGRSGTVASFPIPVSPL
FT                                LWCQAKGRRTAWLSLRAP (in isoform 2).
FT                                /FTId=VSP_026860.
FT   VAR_SEQ     459    768       Missing (in isoform 2).
FT                                /FTId=VSP_026861.
SQ   SEQUENCE   768 AA;  86638 MW;  5913993426EBCFB2 CRC64;
     MDRSRVLEQL IPELTGLLSL LDHEYLSDST LEKKMAVASL LQSLQPLPAK EVSFLYVNTA
     DLHSGPSFVE SLFEEFDCDL GDLRDMSDDG EPSKGASPEP TKSPSLRSAA ADVPPPLPNK
     PPPEDYYEEA LPLGPGKSPE YISSHNGCSP AQSIVDGYYE DADNSYPTTR MNGELKNSYN
     DSDAMSSSYE SYDEEEEEEK GRQPKHQWPS EEASMHLVRD CRICAFLLRK KRFGQWAKQL
     TVIKEEQLLC YKSSKDRQPH LRLALDVCTV IYVPKDSRHK RHELRFSQGA TEVLVLALQS
     REQAEEWLKV IREVSRPIVG AEGLEVPRSP VILCKADQDK RLSQEKQNSD SDSLGMNDSG
     STLGRREACE HGKGKKNSLA ELKGSMSRAA GRKITRIISF SKKKALSEDL QTFSSEDEVP
     CCGYLNVLVN QGWKERWCRL RCNTLYFHKD RTDLHTHVNS IALRGCEVAP GFGPRHPFAF
     RILRNRQEVA ILEASCSEDM GRWLGLLLVE MGSKVTPEAL HYDYVDVETL TSIVSAGRNS
     FLYAQSCQDQ WPEPRIYDEV PYEKVQDEEP QRPTGAQVKR HASSCSEKSH RADPQVKVKR
     HASSANQYKY GKNRAEEDAR RYLVEKERLE KEKETIRTEL TALRQEKKEL KEAIRNNPGA
     KSKALEEAVA TLEAQCRAKE EQRIDLELKL VAVKERLQQS LAGGPALGLS VSNKNKSQDT
     TNKPQSNAPE QSLPVNCVSE LRKRSPSIVT SNQGRVLQKA KEWEMKKT
//
ID   CH034_MOUSE             Reviewed;         459 AA.
AC   Q8BZJ8; Q3UVZ9; Q8BJN6; Q8BUZ5;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Uncharacterized protein C8orf34 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 105-459 (ISOFORM 4).
RC   STRAIN=C57BL/6J; TISSUE=Corpus striatum, Diencephalon, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8BZJ8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BZJ8-2; Sequence=VSP_033018, VSP_033020;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8BZJ8-3; Sequence=VSP_033016, VSP_033017;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q8BZJ8-4; Sequence=VSP_033019, VSP_033021;
CC         Note=No experimental confirmation available;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK034391; BAC28694.1; -; mRNA.
DR   EMBL; AK081222; BAC38170.1; -; mRNA.
DR   EMBL; AK081622; BAC38273.1; -; mRNA.
DR   EMBL; AK136763; BAE23120.1; -; mRNA.
DR   IPI; IPI00227568; -.
DR   IPI; IPI00890841; -.
DR   IPI; IPI00890942; -.
DR   IPI; IPI00890948; -.
DR   RefSeq; NP_001153841.1; NM_001160369.2.
DR   RefSeq; NP_001153842.1; NM_001160370.2.
DR   RefSeq; NP_001153843.1; NM_001160371.2.
DR   RefSeq; NP_796147.2; NM_177173.6.
DR   UniGene; Mm.52021; -.
DR   PRIDE; Q8BZJ8; -.
DR   Ensembl; ENSMUST00000048613; ENSMUSP00000043857; ENSMUSG00000057715.
DR   GeneID; 320492; -.
DR   KEGG; mmu:320492; -.
DR   UCSC; uc007ahx.1; mouse.
DR   MGI; MGI:2444149; A830018L16Rik.
DR   eggNOG; roNOG07797; -.
DR   GeneTree; ENSGT00390000005870; -.
DR   HOVERGEN; HBG107671; -.
DR   InParanoid; Q8BZJ8; -.
DR   OMA; FNQGRAT; -.
DR   OrthoDB; EOG48SGSV; -.
DR   NextBio; 396839; -.
DR   Bgee; Q8BZJ8; -.
DR   Genevestigator; Q8BZJ8; -.
DR   GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR   SUPFAM; SSF47391; cAMP-dep_prot_kin_reg_I/II_a/b; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    459       Uncharacterized protein C8orf34 homolog.
FT                                /FTId=PRO_0000330040.
FT   COMPBIAS    239    243       Poly-Gln.
FT   MOD_RES     111    111       Phosphoserine (By similarity).
FT   VAR_SEQ     227    227       S -> R (in isoform 3).
FT                                /FTId=VSP_033016.
FT   VAR_SEQ     228    459       Missing (in isoform 3).
FT                                /FTId=VSP_033017.
FT   VAR_SEQ     283    287       ENLDD -> GNFKN (in isoform 2).
FT                                /FTId=VSP_033018.
FT   VAR_SEQ     284    288       NLDDL -> QIFSV (in isoform 4).
FT                                /FTId=VSP_033019.
FT   VAR_SEQ     288    459       Missing (in isoform 2).
FT                                /FTId=VSP_033020.
FT   VAR_SEQ     289    459       Missing (in isoform 4).
FT                                /FTId=VSP_033021.
SQ   SEQUENCE   459 AA;  51086 MW;  42997A310FC93146 CRC64;
     MASRQQTRIQ AYLEKNKIGP LFEELMTKLI TETPDQPIPF LIDHLQSKQG NQGQLQRALS
     GSAALWAESE SSEPKGTRRD FRSYDKPWQM NAKKPKKSKS DLAVSNISPP SPDSKSLPRS
     VDHLKWNWRT KPQSRDFDEL NHILQESKKL GKALENLSRS IAISDELDKE TLAFNSSLLR
     PRVIGEWIGR AENDADPLAA EMLQPPVPRS KNDSWESEDS SSSPAGSLKM EPKTKGLKQQ
     QQQHKKLLAA MLSQDSFESI HSPTPSVIEE DIDNEDDAME LLENLDDLRM EGVTTLVLSG
     SKFNQGRPTH PAEPQAKVTL NICSRLQGDN LMERTEDTLQ ILHTPDEIIP DSLDSLPGTE
     ETLMEEGEDF EKTSNLTEPG EASSGAHSLK SYMEEDESLK QLQVVHQPWL LPSDTESEGI
     EAEQDKRSAD LLCVPCSSCP TLIYSGLSVK PAKEVASGP
//
ID   DOC10_MOUSE             Reviewed;        2150 AA.
AC   Q8BZN6;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Dedicator of cytokinesis protein 10;
DE   AltName: Full=Zizimin-3;
GN   Name=Dock10; Synonyms=Kiaa0694, Ziz3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 348-2150 (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1690-2150 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=15710388; DOI=10.1016/j.febslet.2005.01.006;
RA   Nishikimi A., Meller N., Uekawa N., Isobe K., Schwartz M.A.,
RA   Maruyama M.;
RT   "Zizimin2: a novel, DOCK180-related Cdc42 guanine nucleotide exchange
RT   factor expressed predominantly in lymphocytes.";
RL   FEBS Lett. 579:1039-1046(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376; SER-1292; SER-1295
RP   AND THR-1440, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Potential guanine nucleotide exchange factor (GEF). GEF
CC       proteins activate some small GTPases by exchanging bound GDP for
CC       free GTP.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BZN6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BZN6-2; Sequence=VSP_007718, VSP_022288;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8BZN6-3; Sequence=VSP_007718, VSP_022227;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, lung, spleen and thymus.
CC   -!- DOMAIN: The DHR-2 domain may mediate some GEF activity (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the DOCK family.
CC   -!- SIMILARITY: Contains 1 DHR-1 (CZH-1) domain.
CC   -!- SIMILARITY: Contains 1 DHR-2 (CZH-2) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC28567.1; Type=Erroneous initiation;
CC       Sequence=BAC65629.1; Type=Erroneous initiation;
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DR   EMBL; AC124672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC132387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK122347; BAC65629.1; ALT_INIT; mRNA.
DR   EMBL; AK034064; BAC28567.1; ALT_INIT; mRNA.
DR   IPI; IPI00337028; -.
DR   IPI; IPI00661259; -.
DR   IPI; IPI00816904; -.
DR   UniGene; Mm.133473; -.
DR   ProteinModelPortal; Q8BZN6; -.
DR   SMR; Q8BZN6; 173-308, 1694-2150.
DR   STRING; Q8BZN6; -.
DR   PhosphoSite; Q8BZN6; -.
DR   PRIDE; Q8BZN6; -.
DR   Ensembl; ENSMUST00000077946; ENSMUSP00000077099; ENSMUSG00000038608.
DR   Ensembl; ENSMUST00000097681; ENSMUSP00000095286; ENSMUSG00000038608.
DR   MGI; MGI:2146320; Dock10.
DR   GeneTree; ENSGT00560000076710; -.
DR   HOVERGEN; HBG107819; -.
DR   OrthoDB; EOG461432; -.
DR   ArrayExpress; Q8BZN6; -.
DR   Bgee; Q8BZN6; -.
DR   CleanEx; MM_DOCK10; -.
DR   Genevestigator; Q8BZN6; -.
DR   GermOnline; ENSMUSG00000038608; Mus musculus.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0017048; F:Rho GTPase binding; IPI:MGI.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IDA:MGI.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR010703; DOCK.
DR   InterPro; IPR021816; DUF3398.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF06920; Ded_cyto; 1.
DR   Pfam; PF11878; DUF3398; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing;
KW   Guanine-nucleotide releasing factor; Phosphoprotein.
FT   CHAIN         1   2150       Dedicator of cytokinesis protein 10.
FT                                /FTId=PRO_0000190003.
FT   DOMAIN      181    290       PH.
FT   DOMAIN      673    913       DHR-1.
FT   DOMAIN     1591   2141       DHR-2.
FT   MOD_RES     200    200       Phosphothreonine (By similarity).
FT   MOD_RES     376    376       Phosphoserine.
FT   MOD_RES     834    834       N6-acetyllysine (By similarity).
FT   MOD_RES    1292   1292       Phosphoserine.
FT   MOD_RES    1295   1295       Phosphoserine.
FT   MOD_RES    1318   1318       Phosphoserine (By similarity).
FT   MOD_RES    1440   1440       Phosphothreonine.
FT   MOD_RES    1593   1593       N6-acetyllysine (By similarity).
FT   VAR_SEQ    1739   1771       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_007718.
FT   VAR_SEQ    2150   2150       Q -> LCRGPCLYSFCASVSSISLSTVSKSDYGQGRPSKVR
FT                                SGATLHHTCNQGDRGCTCGLHLIQCGGLRGTLEHPMHLSEN
FT                                SLNVLQLISGKKKIDLIYLKFLQCSCLPC (in isoform
FT                                2).
FT                                /FTId=VSP_022288.
FT   VAR_SEQ    2150   2150       Q -> LCRGPCLYSFCASVSSISLSTVSKSGTSFSLYVYPV
FT                                LQPPVHPPLLITSPVPQSALVAQLLLRLHCHLKTRHVDSLA
FT                                FKKKTHAPSSPKCIFELFQFFKTKTQNVFMILQNIKEKHRP
FT                                GVEEERNRKWLFYKGNL (in isoform 3).
FT                                /FTId=VSP_022227.
SQ   SEQUENCE   2150 AA;  245758 MW;  D7CDA1FE6476AB0E CRC64;
     MAGERTRRFT RSLLRPGQAA ELRHSAASAA AVAVSSRQQQ RQEKPRLLDP LDYETVIEEL
     EKTYRDDPLQ DLLFFPSDDF STATVSWDIR TLYSTVPEEA EHRAESLLVK EACKFYSSQW
     YVVNYKYEQY SGDIRQLPRA EHKPEKLPSH SFEVDHEDAD KDEDTTSHSS SKGGGGAGGT
     GVFKSGWLYK GNFNSTVNNT VTVRSFKKRY FQLTQLPDNS YIMNFYKDEK ISKEPKGCIF
     LDSCTGVVQN NRLRKYAFEL KMNDLTYFVL AAETESDMDE WIHTLNRILQ ISPEGPLQGR
     KSAELAELGL DPLDNCVTCE CTLEETDSSE NSLHPDFAKY LTETEDTVKT TRNMGRLNLF
     SLDPDIDTLK LQKRDSFENE LMIKPFEEKA AKRIMIICRA LNFNLQGCVT ENEYDPVTNI
     EPFFVSVALY DLRDNRKISA DFHVDLNHPA VRQMLSGTPP ALENGNIDTG TPRQSEEPHI
     KGLPEEWLKF PKQAVFSVSD PHSEIVLVAK VEKVLMGNIG SGAEPYIKNP DSNKFAQKIL
     KSNRQFCSKL GKYRMPFAWA VRSVFKDNQG NVDRDSRFSP LYRQESSKMS SEDLLKLVSD
     YRRADRISKM QSIPGSLDIA VDNIPLEHPN CVTSSFIPVK PFNVSAQSEP TVEVEEFIYD
     STKYCRPYRV YKNQIYVYPK HLKYDSQKCF NKARNITVCI EFKNSDDDGA KPMKCIYGKP
     GGPLFTSSAY TAVLHHSQNP DFSDEVKIEL PTQLHGKHHL LFSFYHITCD INAKANAKKK
     EALETSVGYA WLPLMKHDQI ASQEYNIPIA TTLPPNYLSI QDPTSAKHGG SDIKWVDGGK
     PLFKVSTFVV STVNTQDPHV NAFFRQCQKR EKDMSQSPTS SFVRACKNLL NVDKIHSIMS
     FLPIILNQLF KILVQNEEDE ITATVTRVLA DIVAKCHEEQ LDHSVQSYIK FVFKTKSYKE
     RTIHEELAKN LSDLLKSNDS TIVKHVLEHS WFFFAIILKS MAQHLIDTNK IQLPRAQRFP
     ESYQSELDNL VMGLCDHVIW KCKEAPEETK RANHSVARFL KRCFTFMDRG FVFKMVNNYI
     SMFSSGEFKT LCQYKFDFLQ EVCQHEHFIP LCLPIRSANI PDPLTPSESI RELHASDMPE
     YSVTNEFCRK HFLIGILLRE VGFALQEDQD IRHLALAVLK NLMAKHSFDD RYREPRKQAQ
     IASLYMPLYG MLLDNMPRIY LKDLYPFTVN TSNQGSRDDL STNGGFQTQT SMKHATSVDT
     SFSKDVLNSI AAFSSIAIST VNHADSRASL ASLDSNPSTT EKSSEKTDNC EKIPRPLSLI
     GSTLRFDKLD QAETRSLLMC FLHIMKTISD ETLIAYWQRA PSPEVSDFFS ILDVCLQNFR
     YLGKRNIIRK IAAAFKFVQS TQNNGTLKGS NPSCQTSGLL SQWMHTTSGH EGHKQHRSQT
     LPIIRGKNAL SNPKLLQMLD NSMNSNSNEI DIVHHVDTEA NIATEVCLTI LDLLSLFTQV
     HQRQLQQSDC QNSLMKRVFD TYMLFFQVNQ SASALKHVFA SLRLFVCKFP SAFFQGPADL
     CGSFCYEVLK CCNHRSRLTQ MEASALLYFF MRKNFEFNKQ KSIVRSHLQL IKAVSQLIAD
     AGIGGSRFQH SLAITNNFAN GDKQMKNSNF PAEVKDLTKR IRTVLMATAQ MKEHEKDPEM
     LVDLQYSLAN SYASTPELRR TWLESMAKIH ARNGDLSEAA MCYIHIAALI AEYLKRKGYW
     KMEKICTPPL LPEDTQPCDS NLLLTTPGGG SMFSMGWPAF LSITPNIKEE GAMKEDSGMQ
     DTPYNENILV EQLYMCVEFL WKSERYELIA DVNKPIIAVF EKQRDFKKLS DLYYDIHRSY
     LKVAEVVNSE KRLFGRYYRV AFYGQAVGFF EEEEGKEYIY KEPKLTGLSE ISQRLLKLYA
     DKFGADNVKI IQDSNKVNPK DLDPKYAYIQ VTYVTPFFEE KEIEDRKTDF EMHHNINRFV
     FETPFTLSGK KHGGVAEQCK RRTVLTTSHL FPYVKKRIQV ISQSSTELNP IEVAIDEMSR
     KVSELNQLCT TEEVDMIRLQ LKLQGSVSVK VNAGPMAYAR AFLEETNAKK YPDNQVKLLK
     EIFRQFADAC GQALDVNERL IKEDQLEYQE ELRSHYKDML SELSAIMNEQ
//
ID   ANC2_MOUSE              Reviewed;         837 AA.
AC   Q8BZQ7; Q8R2Q1;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Anaphase-promoting complex subunit 2;
DE            Short=APC2;
DE   AltName: Full=Cyclosome subunit 2;
GN   Name=Anapc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Epididymis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-837.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-825, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
CC   -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC       (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls
CC       progression through mitosis and the G1 phase of the cell cycle.
CC       The APC/C complex acts by mediating ubiquitination and subsequent
CC       degradation of target proteins: it mainly mediates the formation
CC       of 'Lys-11'-linked polyubiquitin chains and, to a lower extent,
CC       the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin
CC       chains (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: The APC/C is composed of at least 12 subunits (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the cullin family.
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DR   EMBL; AK033784; BAC28472.1; -; mRNA.
DR   EMBL; BC027351; AAH27351.1; -; mRNA.
DR   IPI; IPI00227654; -.
DR   RefSeq; NP_780509.2; NM_175300.4.
DR   UniGene; Mm.291624; -.
DR   ProteinModelPortal; Q8BZQ7; -.
DR   SMR; Q8BZQ7; 762-833.
DR   STRING; Q8BZQ7; -.
DR   PhosphoSite; Q8BZQ7; -.
DR   PRIDE; Q8BZQ7; -.
DR   Ensembl; ENSMUST00000028341; ENSMUSP00000028341; ENSMUSG00000026965.
DR   GeneID; 99152; -.
DR   KEGG; mmu:99152; -.
DR   UCSC; uc008ird.1; mouse.
DR   CTD; 99152; -.
DR   MGI; MGI:2139135; Anapc2.
DR   GeneTree; ENSGT00390000016127; -.
DR   HOVERGEN; HBG045327; -.
DR   InParanoid; Q8BZQ7; -.
DR   OrthoDB; EOG4T1HM4; -.
DR   PhylomeDB; Q8BZQ7; -.
DR   NextBio; 353811; -.
DR   ArrayExpress; Q8BZQ7; -.
DR   Bgee; Q8BZQ7; -.
DR   CleanEx; MM_ANAPC2; -.
DR   Genevestigator; Q8BZQ7; -.
DR   GermOnline; ENSMUSG00000026965; Mus musculus.
DR   GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR   GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR014786; APC2.
DR   InterPro; IPR016158; Cullin_homology.
DR   InterPro; IPR001373; Cullin_N.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF08672; APC2; 1.
DR   Pfam; PF00888; Cullin; 1.
DR   SMART; SM00182; CULLIN; 1.
DR   SUPFAM; SSF75632; Cullin_homology; 1.
DR   PROSITE; PS50069; CULLIN_2; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Mitosis; Phosphoprotein;
KW   Ubl conjugation pathway.
FT   CHAIN         1    837       Anaphase-promoting complex subunit 2.
FT                                /FTId=PRO_0000119812.
FT   MOD_RES     233    233       Phosphoserine (By similarity).
FT   MOD_RES     329    329       Phosphoserine (By similarity).
FT   MOD_RES     485    485       Phosphoserine (By similarity).
FT   MOD_RES     549    549       Phosphoserine (By similarity).
FT   MOD_RES     825    825       Phosphotyrosine.
FT   CONFLICT    680    680       L -> V (in Ref. 2; AAH27351).
SQ   SEQUENCE   837 AA;  95321 MW;  6FADCB86334ADE59 CRC64;
     MEAEGVAVAA AAAAAAAAAT IIASDDCDSR PGQELLVAWN TVSTGLVPPA ALGLASSRTS
     GAVPPKEEEL RAAVEVLRGH GLHSVLEEWF VEVLQNDLQG NIATEFWNAI ALRENSVDEP
     QCLGLLLDAF GLLESRLDPY LHSLELLEKW TRLGLLMGAG AQGLREKVHT MLRGVLFFST
     PRTFQEMVQR LYGRFLRVYM QSKRKGEGGT DPELEGELDS RYARRRYYRL LQSPLCAGCG
     SDKQQCWCRQ ALEQFNQLSQ VLHRLSLLER VCAEAVTTTL HQVTRERMED RCRGEYERSF
     LREFHKWIER VVGWLGKVFL QDNPTRPTSP EAGNTLRRWR CHVQRFFYRI YATLRIEELF
     SIIRDFPDSR PAIEDLKYCL ERTDQRQQLL VSLKVALETR LLHPGVNTCD IITLYISAIK
     ALRVLDPSMV ILEVACEPIR RYLRTREDTV RQIVAGLTGD SDGTGDLAVE LSKTDPACLE
     TGQDSEDDSG EPEDWVPDPV DADPVKSSSK RRSSDIISLL VSIYGSKDLF INEYRSLLAD
     RLLHQFSFSP EREIRNVELL KLRFGEAPMH FCEVMLKDMA DSRRINANIR EEDEKRPVEE
     QPPFGVYAVI LSSEFWPPFK DEKLEVPEDI RAALDVYCKK YEKLKAMRTL SWKHTLGLVT
     MDVELADRTL SVAVTPVQAL VLLYFQNQAS WTLEELSKVV KMPVALLRRR MSVWLQQGVL
     REEPPGTFSV IEEERPQDRD NMVLIDSDDE SDSGMASQAD QKEEELLLFW AYIQAMLTNL
     ESLSLERIYS MLRMFVMTGP ALAEIDLQEL QGYLQKKVRD QQLIYSAGVY RLPKNSN
//
ID   CQ085_MOUSE             Reviewed;         615 AA.
AC   Q8BZR9; Q3TNF4; Q3TQ96; Q4G0C3; Q8BMB1; Q9CRM6; Q9CS93; Q9D0G9;
AC   Q9DBT0;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Uncharacterized protein C17orf85 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow, Cecum, Head, Lung, Spleen, and Wolffian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Trophoblast stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8BZR9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BZR9-2; Sequence=VSP_029001, VSP_029002;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8BZR9-3; Sequence=VSP_029000, VSP_029003;
CC         Note=No experimental confirmation available;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB27625.1; Type=Erroneous initiation;
CC       Sequence=BAC28111.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK004766; BAB23546.2; -; mRNA.
DR   EMBL; AK011450; BAB27625.1; ALT_INIT; mRNA.
DR   EMBL; AK033682; BAC28428.1; -; mRNA.
DR   EMBL; AK017496; BAB30775.2; -; mRNA.
DR   EMBL; AK020130; BAB32004.1; -; mRNA.
DR   EMBL; AK032983; BAC28111.1; ALT_INIT; mRNA.
DR   EMBL; AK163780; BAE37488.1; -; mRNA.
DR   EMBL; AK153152; BAE31762.1; -; mRNA.
DR   EMBL; AK153241; BAE31833.1; -; mRNA.
DR   EMBL; AK165317; BAE38135.1; -; mRNA.
DR   EMBL; AL670399; CAI24786.1; -; Genomic_DNA.
DR   EMBL; BC098495; AAH98495.1; -; mRNA.
DR   EMBL; BC118943; AAI18944.1; -; mRNA.
DR   IPI; IPI00278062; -.
DR   IPI; IPI00869379; -.
DR   IPI; IPI00869441; -.
DR   RefSeq; NP_080094.3; NM_025818.3.
DR   UniGene; Mm.41903; -.
DR   ProteinModelPortal; Q8BZR9; -.
DR   PhosphoSite; Q8BZR9; -.
DR   PRIDE; Q8BZR9; -.
DR   Ensembl; ENSMUST00000021135; ENSMUSP00000021135; ENSMUSG00000020783.
DR   GeneID; 66874; -.
DR   KEGG; mmu:66874; -.
DR   UCSC; uc007jzv.1; mouse.
DR   MGI; MGI:1914124; 1200014J11Rik.
DR   eggNOG; roNOG05700; -.
DR   GeneTree; ENSGT00390000005712; -.
DR   HOVERGEN; HBG059983; -.
DR   InParanoid; Q8BZR9; -.
DR   OMA; QDIFSYF; -.
DR   OrthoDB; EOG4NGGMG; -.
DR   PhylomeDB; Q8BZR9; -.
DR   NextBio; 322897; -.
DR   ArrayExpress; Q8BZR9; -.
DR   Bgee; Q8BZR9; -.
DR   CleanEx; MM_1200014J11RIK; -.
DR   Genevestigator; Q8BZR9; -.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   InterPro; IPR019416; DUF2414.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF10309; DUF2414; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    615       Uncharacterized protein C17orf85 homolog.
FT                                /FTId=PRO_0000308583.
FT   COMPBIAS    340    371       Glu-rich.
FT   MOD_RES      25     25       Phosphoserine (By similarity).
FT   MOD_RES     209    209       Phosphoserine (By similarity).
FT   MOD_RES     210    210       Phosphoserine (By similarity).
FT   MOD_RES     226    226       Phosphoserine (By similarity).
FT   MOD_RES     387    387       Phosphoserine (By similarity).
FT   MOD_RES     388    388       Phosphoserine (By similarity).
FT   MOD_RES     390    390       Phosphoserine (By similarity).
FT   MOD_RES     391    391       Phosphoserine (By similarity).
FT   MOD_RES     392    392       Phosphoserine (By similarity).
FT   MOD_RES     394    394       Phosphoserine (By similarity).
FT   MOD_RES     407    407       Phosphoserine (By similarity).
FT   MOD_RES     408    408       Phosphothreonine (By similarity).
FT   MOD_RES     410    410       Phosphoserine (By similarity).
FT   MOD_RES     495    495       Phosphoserine (By similarity).
FT   MOD_RES     563    563       Phosphoserine.
FT   VAR_SEQ     119    161       AIPKVRLETIYICGVDEMSTQDIFSYFKEYPPAHIEWLDDT
FT                                SC -> GTVCLGEIFHPGSRVTFPAVVSRSFWLCPVCPVVI
FT                                QIPKRKGF (in isoform 3).
FT                                /FTId=VSP_029000.
FT   VAR_SEQ     119    121       AIP -> VVS (in isoform 2).
FT                                /FTId=VSP_029001.
FT   VAR_SEQ     122    615       Missing (in isoform 2).
FT                                /FTId=VSP_029002.
FT   VAR_SEQ     162    615       Missing (in isoform 3).
FT                                /FTId=VSP_029003.
FT   CONFLICT     73     73       S -> I (in Ref. 1; BAB30775).
FT   CONFLICT    202    202       K -> E (in Ref. 3; AAH98495).
FT   CONFLICT    247    247       R -> S (in Ref. 1; BAB27625).
FT   CONFLICT    251    251       K -> Q (in Ref. 1; BAB23546).
FT   CONFLICT    268    268       K -> Q (in Ref. 1; BAB23546).
FT   CONFLICT    382    382       S -> R (in Ref. 1; BAB27625).
FT   CONFLICT    508    508       R -> K (in Ref. 1; BAB27625).
SQ   SEQUENCE   615 AA;  70043 MW;  67033DB16255889F CRC64;
     MAAVRGLRVS VKAEAPAGPA LGLPSPEVES GLERGEPEPM EVEEGELEIV PVRRSLKELL
     PDTSRRYENK AGSFITGIDV TSKEAIEKKE QRAKRFHFRA EVNLAQRNVA LDRDMMKKAI
     PKVRLETIYI CGVDEMSTQD IFSYFKEYPP AHIEWLDDTS CNVVWLDEMT ATRALINMSS
     LPAQDKMRSR DASEDKSSEK NKKDKQEDSS DDDETEEGEV EDENSSDVEL DTLSQVEEES
     LLRNDLRPAN KLAKGNRLFM RFATKDDKKE LGAARRSQYY MKYGNPNYGG MKGILSNSWK
     RRYHSRRIQR DVIKKRALIG DDVGLTSYKH RHSGLVNVPE EPIEEEEEEE EEEEDQDMDA
     DDRVVVEYHE ELPGLKQPRE RSLSRRSSAS SSDSDEMDYD LELKMISTPS PKKSMKMTMY
     ADEVESQLKS IRNPMRADSI STSNIKNRIG NKLPPEKFAD VRHLLDEKRQ HSCPRPAVSS
     TKPDIRQRLG KRPYSPEKAF SSNQVVRREP SSDVHSRLGV PRQDVKGLYS DTRERKSGGL
     WTRLGSTPKT KEKNTKKVDH RASGAEEDDS ELQRAWGALI KEKEESRQKK SRLDSLPSLQ
     IEVSRESSSG SEAES
//
ID   SH3R2_MOUSE             Reviewed;         735 AA.
AC   Q8BZT2; B2RQJ2; Q80VJ1; Q8C122; Q8C1E3;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Putative E3 ubiquitin-protein ligase SH3RF2;
DE            EC=6.3.2.-;
DE   AltName: Full=SH3 domain-containing RING finger protein 2;
GN   Name=Sh3rf2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Cecum, Head, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N-3; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   STRUCTURE BY NMR OF 385-441.
RG   RIKEN structural genomics initiative (RSGI);
RT   "solution structure of the SH3 domain of the mouse hypothetical
RT   protein SH3RF2.";
RL   Submitted (NOV-2005) to the PDB data bank.
CC   -!- FUNCTION: May be a E3 ubiquitin-protein ligase (Potential). May
CC       play a role in cardiac function (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with FASLG and PPP1CA (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BZT2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BZT2-2; Sequence=VSP_022060;
CC   -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC       ubiquitin-conjugating enzyme (By similarity).
CC   -!- SIMILARITY: Belongs to the SH3RF family.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SIMILARITY: Contains 3 SH3 domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK028153; BAC25780.1; -; mRNA.
DR   EMBL; AK029168; BAC26334.1; -; mRNA.
DR   EMBL; AK033601; BAC28382.1; -; mRNA.
DR   EMBL; BC048400; AAH48400.1; -; mRNA.
DR   EMBL; BC137955; AAI37956.1; -; mRNA.
DR   EMBL; BC145060; AAI45061.1; -; mRNA.
DR   IPI; IPI00223967; -.
DR   IPI; IPI00227686; -.
DR   RefSeq; NP_001139771.1; NM_001146299.1.
DR   RefSeq; NP_766554.2; NM_172966.3.
DR   UniGene; Mm.45472; -.
DR   PDB; 2CUC; NMR; -; A=385-441.
DR   PDB; 2DJQ; NMR; -; A=128-182.
DR   PDBsum; 2CUC; -.
DR   PDBsum; 2DJQ; -.
DR   ProteinModelPortal; Q8BZT2; -.
DR   SMR; Q8BZT2; 10-56, 128-182, 188-251, 383-441.
DR   PhosphoSite; Q8BZT2; -.
DR   PRIDE; Q8BZT2; -.
DR   Ensembl; ENSMUST00000072008; ENSMUSP00000071896; ENSMUSG00000057719.
DR   GeneID; 269016; -.
DR   KEGG; mmu:269016; -.
DR   NMPDR; fig|10090.3.peg.3905; -.
DR   UCSC; uc008etk.1; mouse.
DR   UCSC; uc008etl.1; mouse.
DR   CTD; 269016; -.
DR   MGI; MGI:2444628; Sh3rf2.
DR   eggNOG; roNOG05183; -.
DR   GeneTree; ENSGT00550000074287; -.
DR   HOGENOM; HBG278072; -.
DR   HOVERGEN; HBG082418; -.
DR   InParanoid; Q8BZT2; -.
DR   OMA; HSYSAHG; -.
DR   OrthoDB; EOG48WC1H; -.
DR   PhylomeDB; Q8BZT2; -.
DR   NextBio; 392640; -.
DR   ArrayExpress; Q8BZT2; -.
DR   Bgee; Q8BZT2; -.
DR   CleanEx; MM_SH3RF2; -.
DR   Genevestigator; Q8BZT2; -.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008157; F:protein phosphatase 1 binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00018; SH3_1; 2.
DR   Pfam; PF07653; SH3_2; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00326; SH3; 3.
DR   SUPFAM; SSF50044; SH3; 3.
DR   PROSITE; PS50002; SH3; 3.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Ligase; Metal-binding; Repeat;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    735       Putative E3 ubiquitin-protein ligase
FT                                SH3RF2.
FT                                /FTId=PRO_0000269513.
FT   DOMAIN      125    184       SH3 1.
FT   DOMAIN      187    252       SH3 2.
FT   DOMAIN      382    443       SH3 3.
FT   ZN_FING      12     53       RING-type.
FT   REGION      647    652       Interaction with PPP1CA (By similarity).
FT   VAR_SEQ     217    248       Missing (in isoform 2).
FT                                /FTId=VSP_022060.
FT   CONFLICT    127    127       V -> G (in Ref. 1; BAC26334).
FT   CONFLICT    258    258       E -> Q (in Ref. 1; BAC25780).
FT   CONFLICT    662    662       S -> C (in Ref. 1; BAC28382).
FT   STRAND      408    416
FT   STRAND      419    424
FT   TURN        425    427
FT   STRAND      430    434
FT   HELIX       435    437
SQ   SEQUENCE   735 AA;  80066 MW;  FAE1D97780289FCC CRC64;
     MDDLTLLDLL ECPVCFEKLD VTAKVLPCQH TFCKPCLQRI FKAHKELRCP ECRTLVFCSI
     EALPANLLLV RLLDGVRSGQ SSWKGGSFRR PRILTLQDNR KAKSSPRSLQ ASPFRLVPSV
     RIHMDGVPRA KALCNYRGKN PGDLKFNKGD VILLRRQLDE NWYQGEINGV SGIFPASSVE
     VIKQLPQPPP LCRALYNFDL RDKDKSENQD CLTFLKDDVI TVISRVDENW AEGKLGDKVG
     IFPILFVEPN VSARHLLENK GHQLSRTRHL SLMSSPSRGK ATNTSSLRKS PGSRRKGSGQ
     FSMTTALNTL NRTVHSPEGH QMVEISTPML ISSNSPSVLT QHGDKADFPT SSTGQVSSSQ
     PAPASPGHST AMVSVPSSQQ HLSNNMFVAL HTYSAHRPEE LDLQKGEGIR VLGKYQDGWL
     KGLSLLTGRT GIFPSDYVIP VFSSTARKTS SFPDSRSPTV CTTWALSTSS VSSQGSFAEG
     DPRQSGPFKS VFVPTAVVNP SRSTPGPGSS GQGSLRKVRS SMRKNGSLQR PVQSGIPTFM
     VGSLRCSPTM VIRPQRFQFY PPQGMTPSPT PIMVEMGSKS IYTGEPALTC INRGSKTRIH
     SAGNSIIMEG KETPIKSEPP PKPPASAPPS ILVKPENSKN GTEKQVKTVR FQNYSPPPTK
     HSASSPTSGK HDHPATLKGS QHEAVSSGGE MTILFAHRSG CHSGQQTDLR RKSAFGKTMP
     LLSTASATQT LFPSK
//
ID   ANR56_MOUSE             Reviewed;         760 AA.
AC   Q8BZW2; Q8BZS7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Ankyrin repeat domain-containing protein 56;
GN   Name=Ankrd56;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cecum, Cerebellum, and Colon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SIMILARITY: Contains 2 ANK repeats.
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DR   EMBL; AK033423; BAC28281.1; -; mRNA.
DR   EMBL; AK033641; BAC28403.1; -; mRNA.
DR   EMBL; AK137429; BAE23349.1; -; mRNA.
DR   IPI; IPI00227725; -.
DR   RefSeq; NP_780479.1; NM_175270.4.
DR   UniGene; Mm.245085; -.
DR   UniGene; Mm.477202; -.
DR   ProteinModelPortal; Q8BZW2; -.
DR   SMR; Q8BZW2; 564-692.
DR   PhosphoSite; Q8BZW2; -.
DR   PRIDE; Q8BZW2; -.
DR   Ensembl; ENSMUST00000061328; ENSMUSP00000055267; ENSMUSG00000045314.
DR   GeneID; 78088; -.
DR   KEGG; mmu:78088; -.
DR   UCSC; uc008ydw.1; mouse.
DR   CTD; 78088; -.
DR   MGI; MGI:1925338; Ankrd56.
DR   GeneTree; ENSGT00530000063547; -.
DR   HOGENOM; HBG126596; -.
DR   HOVERGEN; HBG094934; -.
DR   InParanoid; Q8BZW2; -.
DR   OMA; RTREWVA; -.
DR   OrthoDB; EOG408N97; -.
DR   PhylomeDB; Q8BZW2; -.
DR   NextBio; 348182; -.
DR   ArrayExpress; Q8BZW2; -.
DR   Bgee; Q8BZW2; -.
DR   CleanEx; MM_ANKRD56; -.
DR   Genevestigator; Q8BZW2; -.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 1.
DR   SMART; SM00248; ANK; 2.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
PE   2: Evidence at transcript level;
KW   ANK repeat; Repeat.
FT   CHAIN         1    760       Ankyrin repeat domain-containing protein
FT                                56.
FT                                /FTId=PRO_0000317241.
FT   REPEAT      597    626       ANK 1.
FT   REPEAT      636    666       ANK 2.
SQ   SEQUENCE   760 AA;  83542 MW;  9E4386D1FD33679E CRC64;
     MAGELSQEAL LDFLCQAGGR VRNAELLSHF KSFLRDPHVS PGQLQERRER FKGFVNSVAA
     VRQDPDGTKY VVLKRRYRDL LGEEGLQRPG PVDGKPRGHR RRDPEPQKPP AGAGTQVDVG
     GSAQKVAGPD PSPEDSPNQR TPEPEAAQAR GRCAAVGTRG RCCWECQQNG WGQSTGQPLP
     EDLGDPAVAC EKPERAAPAR DDLGAPGWLR EGEAAEHAPG SVPPVWPPTA VEAAGSPTSP
     PALPPHPAPS REPLELFTAG SPNHSTQQLQ QQHQRTQEWV ARYLQVPEPE IQAPTRAWSV
     LPDNFLQLPS ETAFGVSETS SALPEPALSF HSLLPVVLDE SSESWPGNAP STVFRSIRCQ
     LSLQDLNDFV EQESHGSEES SSGPKESPGT PEEGLQPVLR TSSWGELRDP VEDLFLPPND
     SPCLIRRDLG YRGNAPSFRK VPTVAKSLGD HPQEPFPALK FRRSVRRSSR TGRTKSPSSS
     DEEHPDEDLW KRSRRPPRSR KPSKAGALPS PRVDAVLVQK LADANAVASQ PHSSWIPSRD
     GSAALIPHRP SEHRSPLVPL DTREHEWIVR LASGSWLHVL TLFWEDPQLA LHRDFLTGYT
     ALHWIAKHGD LCALQDLVSG AQKAGIALDV NVRSSCGYTP LHLAAIHGHQ GVIKLLVQRL
     ASRVNIRDCS GKKPWQYLNS NVSGETWQLL GAPRGKPIFP VYSLVQSSSP ARKVKSREVS
     RNVTRKTSLA ALLKTQHNKW KLASQYEKIH TSKEREEYSD
//
ID   WWP1_MOUSE              Reviewed;         918 AA.
AC   Q8BZZ3; Q8BIV9; Q8VDP8;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2003, sequence version 2.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=NEDD4-like E3 ubiquitin-protein ligase WWP1;
DE            EC=6.3.2.-;
DE   AltName: Full=WW domain-containing protein 1;
GN   Name=Wwp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 639-918.
RC   STRAIN=FVB/N; TISSUE=Colon, and Mammary cancer;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH KLF2.
RX   MEDLINE=21369920; PubMed=11375995; DOI=10.1074/jbc.M103670200;
RA   Conkright M.D., Wani M.A., Lingrel J.B.;
RT   "Lung Krueppel-like factor contains an autoinhibitory domain that
RT   regulates its transcriptional activation by binding WWP1, an E3
RT   ubiquitin ligase.";
RL   J. Biol. Chem. 276:29299-29306(2001).
RN   [4]
RP   FUNCTION IN UBIQUITINATION OF KLF2, AND MUTAGENESIS OF CYS-886.
RX   PubMed=15003522; DOI=10.1016/j.bbrc.2004.02.033;
RA   Zhang X., Srinivasan S.V., Lingrel J.B.;
RT   "WWP1-dependent ubiquitination and degradation of the lung Kruppel-
RT   like factor, KLF2.";
RL   Biochem. Biophys. Res. Commun. 316:139-148(2004).
RN   [5]
RP   FUNCTION IN UBIQUITINATION OF KLF5, INTERACTION WITH KLF5, SUBCELLULAR
RP   LOCATION, AND MUTAGENESIS OF CYS-886.
RX   PubMed=15735697; DOI=10.1038/sj.onc.1208497;
RA   Chen C., Sun X., Ran Q., Wilkinson K.D., Murphy T.J., Simons J.W.,
RA   Dong J.T.;
RT   "Ubiquitin-proteasome degradation of KLF5 transcription factor in
RT   cancer and untransformed epithelial cells.";
RL   Oncogene 24:3319-3327(2005).
RN   [6]
RP   INTERACTION WITH HIVEP3.
RX   PubMed=16728642; DOI=10.1126/science.1126313;
RA   Jones D.C., Wein M.N., Oukka M., Hofstaetter J.G., Glimcher M.J.,
RA   Glimcher L.H.;
RT   "Regulation of adult bone mass by the zinc finger adapter protein
RT   Schnurri-3.";
RL   Science 312:1223-1227(2006).
RN   [7]
RP   FUNCTION IN UBIQUITINATION OF TP63, AND INTERACTION WITH TP63.
RX   PubMed=18806757; DOI=10.1038/cdd.2008.134;
RA   Li Y., Zhou Z., Chen C.;
RT   "WW domain-containing E3 ubiquitin protein ligase 1 targets p63
RT   transcription factor for ubiquitin-mediated proteasomal degradation
RT   and regulates apoptosis.";
RL   Cell Death Differ. 15:1941-1951(2008).
RN   [8]
RP   FUNCTION IN UBIQUITINATION OF RNF11, INTERACTION WITH RNF11,
RP   UBIQUITINATION, AND MUTAGENESIS OF CYS-886.
RX   PubMed=18724389; DOI=10.1038/onc.2008.288;
RA   Chen C., Zhou Z., Liu R., Li Y., Azmi P.B., Seth A.K.;
RT   "The WW domain containing E3 ubiquitin protein ligase 1 upregulates
RT   ErbB2 and EGFR through RING finger protein 11.";
RL   Oncogene 27:6845-6855(2008).
RN   [9]
RP   FUNCTION IN UBIQUITINATION OF ERBB4, AND INTERACTION WITH ERBB4.
RX   PubMed=19561640; DOI=10.1038/onc.2009.162;
RA   Li Y., Zhou Z., Alimandi M., Chen C.;
RT   "WW domain containing E3 ubiquitin protein ligase 1 targets the full-
RT   length ErbB4 for ubiquitin-mediated degradation in breast cancer.";
RL   Oncogene 28:2948-2958(2009).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from
CC       an E2 ubiquitin-conjugating enzyme in the form of a thioester and
CC       then directly transfers the ubiquitin to targeted substrates.
CC       Ubiquitinates ERBB4 isoforms JM-A CYT-1 and JM-B CYT-1, KLF2, KLF5
CC       and TP63 and promotes their proteasomal degradation. Ubiquitinates
CC       RNF11 without targeting it for degradation. Ubiquitinates and
CC       promotes degradation of TGFBR1; the ubiquitination is enhanced by
CC       SMAD7. Ubiquitinates SMAD6 and SMAD7.
CC   -!- ENZYME REGULATION: Activated by NDFIP1- and NDFIP2-binding (By
CC       similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Binds SCNN1A, SCNN1B, SCNN1G, WBP1, WBP2, DRPLA and
CC       adenovirus type 2 PIII (By similarity). Binds KLF2 AND HIVEP3.
CC       Interacts with RNF11. Interacts with SPG20. Interacts with NDFIP1
CC       and NDFIP2; this interaction activates the E3 ubiquitin-protein
CC       ligase (By similarity). Interacts with ERBB4 isoforms JM-B CYT-1
CC       and JM-A CYT-1. Does not interact with ERB4 isoform JMA-A CYT-2.
CC       Interacts with SMAD1, SMAD2, SMAD3, SMAD5, SMAD6, SMAD7, TGFBR1
CC       AND TGFBR2. Associates with the TGFBR1:TGFBR2 receptor complex in
CC       presence of SMAD7. Interacts with SKIL isoform 1. Interacts with
CC       TP63 isoform 1 and isoform 2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral
CC       membrane protein. Nucleus.
CC   -!- PTM: Auto-ubiquitinated and ubiquitinated by RNF11 (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 HECT (E6AP-type E3 ubiquitin-protein
CC       ligase) domain.
CC   -!- SIMILARITY: Contains 4 WW domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH21470.1; Type=Erroneous initiation;
CC       Sequence=BAC38473.1; Type=Miscellaneous discrepancy; Note=Chimera. The second part of the clone maps to another chromosome;
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DR   EMBL; AK033138; BAC28168.1; -; mRNA.
DR   EMBL; AK082346; BAC38473.1; ALT_SEQ; mRNA.
DR   EMBL; BC021470; AAH21470.1; ALT_INIT; mRNA.
DR   EMBL; BC051405; AAH51405.1; -; mRNA.
DR   IPI; IPI00227759; -.
DR   RefSeq; NP_796301.2; NM_177327.3.
DR   UniGene; Mm.78312; -.
DR   ProteinModelPortal; Q8BZZ3; -.
DR   SMR; Q8BZZ3; 15-145, 341-528, 543-913.
DR   STRING; Q8BZZ3; -.
DR   PhosphoSite; Q8BZZ3; -.
DR   PRIDE; Q8BZZ3; -.
DR   Ensembl; ENSMUST00000035982; ENSMUSP00000041627; ENSMUSG00000041058.
DR   Ensembl; ENSMUST00000108246; ENSMUSP00000103881; ENSMUSG00000041058.
DR   GeneID; 107568; -.
DR   KEGG; mmu:107568; -.
DR   UCSC; uc008scc.1; mouse.
DR   CTD; 107568; -.
DR   MGI; MGI:1861728; Wwp1.
DR   GeneTree; ENSGT00570000078756; -.
DR   HOGENOM; HBG607874; -.
DR   HOVERGEN; HBG004134; -.
DR   InParanoid; Q8BZZ3; -.
DR   OMA; EFRVWSH; -.
DR   OrthoDB; EOG473PQM; -.
DR   PhylomeDB; Q8BZZ3; -.
DR   NextBio; 359054; -.
DR   ArrayExpress; Q8BZZ3; -.
DR   Bgee; Q8BZZ3; -.
DR   Genevestigator; Q8BZZ3; -.
DR   GermOnline; ENSMUSG00000041058; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
DR   GO; GO:0030324; P:lung development; TAS:UniProtKB.
DR   GO; GO:0016481; P:negative regulation of transcription; IDA:UniProtKB.
DR   GO; GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR   GO; GO:0030217; P:T cell differentiation; TAS:UniProtKB.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR000569; HECT.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00397; WW; 4.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00456; WW; 4.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF56204; HECT; 1.
DR   SUPFAM; SSF51045; WW_Rsp5_WWP; 4.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 4.
DR   PROSITE; PS50020; WW_DOMAIN_2; 4.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; Ligase; Membrane; Nucleus; Phosphoprotein;
KW   Repeat; Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN         1    918       NEDD4-like E3 ubiquitin-protein ligase
FT                                WWP1.
FT                                /FTId=PRO_0000120337.
FT   DOMAIN        5     98       C2.
FT   DOMAIN      345    378       WW 1.
FT   DOMAIN      377    410       WW 2.
FT   DOMAIN      452    485       WW 3.
FT   DOMAIN      492    525       WW 4.
FT   DOMAIN      584    918       HECT.
FT   REGION      345    525       Interaction with ERBB4.
FT   ACT_SITE    886    886       Glycyl thioester intermediate (By
FT                                similarity).
FT   SITE        886    886       Required for ubiquitin-thioester
FT                                formation.
FT   MOD_RES     818    818       Phosphothreonine (By similarity).
FT   MUTAGEN     886    886       C->S: Loss of catalytic activity. No
FT                                effect on RNF11-binding. No effect on
FT                                KLF2 ubiquitination. Abolishes
FT                                ubiquitination of KLF5.
FT   CONFLICT    302    302       V -> L (in Ref. 1; BAC28168).
SQ   SEQUENCE   918 AA;  104694 MW;  01478A3C1CFFDAA9 CRC64;
     MATASPRSDT SDIHSGRLQL KVTVSSAKLK RKKNWFGTAI YTEVIVDGEV KKTAKSSSSS
     NPKWDEQLIV NVTPQTTLEF RVWSHHTLKA DALLGKATVD LKQVLLTHNR KLEKVKEQLK
     LSLENKNGIV QTGELTVVLD GLVIEQEPVT NRSSSPPIEI QQNGDALHEN GDPATRTTPR
     LPVEGTIGID NHVSTNTVVP NSCCSHVVNG ENTPSSPSQV AARPKNAPAP KPVTSAPTSD
     TVNGESSSVL ADNTSTMGTL LPSEDTTSTS NCTSTTTQEP PVQEPPASSE HSECIPSASA
     EVGPEARSLI DPDSDSRNNS VFDKVRQPEG CVEPLRPQSG NTNTEALPSG WEQRKDPHGR
     TYYVDHNTRT TTWERPQPLP PGWERRVDDR GRVYYVDHNT RTTTWQRPTM ESVRNFEQWQ
     SQRNQLQGAM QQFNQRYLYS ASMLAAENDP YGPLPPGWEK RVDSTDRVYF VNHNTKTTQW
     EDPRTQGLPN EEPLPEGWEI RYTREGVRYF VDHNTRTTTF KDPRNGKSSV TKGGPQIAYE
     RSFRWKLAHF RYLCQSNALP SHVKINVSRQ TLFEDSFQQI MALKPYDLRR RLYVIFRGEE
     GLDYGGLARE WFFLLSHEVL NPMYCLFEYA GKNNYCLQIN PASTINPDHL SYFCFIGRFI
     AMALFHGKFI DTGFSLPFYK RMLSKKLTIK DLESIDTEFY NSLIWIRDNN IEECGLEMYF
     SVDMEILGKV TSHDLKLGGS NILVTEENKD EYIGLMTEWR FSRGVQEQTK AFLDGFNEVV
     PLQWLQYFDE KELEVMLCGM QEVDLADWQR NTVYRHYTRN SKQIIWFWQF VKETDNEVRM
     RLLQFVTGTC RLPLGGFAEL MGSNGPQKFC IEKVGKDTWL PRSHTCFNRL DLPPYKSYEQ
     LKEKLLFAIE ETEGFGQE
//
ID   CT012_MOUSE             Reviewed;         778 AA.
AC   Q8C008; A2AN93; Q8C060;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Ankyrin repeat-containing protein C20orf12 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   PROTEIN SEQUENCE OF 212-223, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-768, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
CC   -!- SIMILARITY: Contains 2 ANK repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC27747.1; Type=Frameshift; Positions=7;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK032182; BAC27747.1; ALT_FRAME; mRNA.
DR   EMBL; AK032632; BAC27960.1; ALT_TERM; mRNA.
DR   EMBL; AL808119; CAM26704.1; -; Genomic_DNA.
DR   IPI; IPI00223634; -.
DR   RefSeq; NP_766447.2; NM_172859.2.
DR   UniGene; Mm.442156; -.
DR   ProteinModelPortal; Q8C008; -.
DR   SMR; Q8C008; 635-758.
DR   PhosphoSite; Q8C008; -.
DR   PRIDE; Q8C008; -.
DR   Ensembl; ENSMUST00000081982; ENSMUSP00000080643; ENSMUSG00000037259.
DR   GeneID; 241688; -.
DR   KEGG; mmu:241688; -.
DR   UCSC; uc008mrd.1; mouse.
DR   MGI; MGI:2139080; 6330439K17Rik.
DR   GeneTree; ENSGT00390000000549; -.
DR   HOVERGEN; HBG063313; -.
DR   InParanoid; Q8C008; -.
DR   OMA; ITVAVMN; -.
DR   OrthoDB; EOG483D45; -.
DR   NextBio; 385118; -.
DR   ArrayExpress; Q8C008; -.
DR   Bgee; Q8C008; -.
DR   CleanEx; MM_6330439K17RIK; -.
DR   Genevestigator; Q8C008; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00547; ZnF_RBZ; 3.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; FALSE_NEG.
PE   1: Evidence at protein level;
KW   ANK repeat; Direct protein sequencing; Phosphoprotein; Repeat.
FT   CHAIN         1    778       Ankyrin repeat-containing protein
FT                                C20orf12 homolog.
FT                                /FTId=PRO_0000235912.
FT   REPEAT      631    662       ANK 1.
FT   REPEAT      666    695       ANK 2.
FT   MOD_RES     768    768       Phosphoserine.
FT   CONFLICT    202    202       P -> H (in Ref. 1; BAC27960).
FT   CONFLICT    693    693       I -> N (in Ref. 1; BAC27747).
FT   CONFLICT    710    710       L -> Q (in Ref. 1; BAC27747).
SQ   SEQUENCE   778 AA;  85025 MW;  1A3EDB966EC74AED CRC64;
     MTAGSVCAPQ IIPLRVPQPG KANHEIDTNT LLEMKSDTPD VNIYYTLDGS KPDFLKKVGS
     GENNTFKYVK PITLPDGKIQ VKAVAVSKDC RQSGIVTKVF QVDYEPPKMV SSEDNVEDAL
     KGFSKQELKN GFVGPKLRKK YKNAENKSTW NVNLRRLADL KVGERADPKT LKDLRFAESP
     LEIPAYHEGA SARLPTHQAQ SPGFAHITGQ KSLTSTEIMR IQRETDFLKC AHCLASRPSD
     PFARFCHECG APVPPIFGYR LPPPEGAQMG LCAECGSMVP MNTPICVVCE APLAPQLRPQ
     ASLYLKERVI CRTCGTGNPA HLRYCVTCEG PLPPTQEQWL CNGDEVPHPP ARNGETISCS
     RCGCQNLWEA SFCDWCGAML GISASHSVCP KCGASNHLTA RFCGSCGIYV KSITRFRMHN
     SLAIVAGAPR PFPEPRSAWQ SLNVPLPTSA SGSKKDTGTQ TSGLFYPSGK LLAKKELEAA
     SHRQRQEKMS DHRPVLTAVS PGRGYWRKQL DHISAHLRSY AQNNPEFRAL IAEPRMGKLI
     SATVHEDGYE VSIRLNYIQV SNKSLYFNKS VNLSDHFLSS VTEGGNGLYD SRSSLVSAYS
     QSVSDTPESI KKMKNLKAKS FLVNPEPLTP ENKLLLEEVG SSGKGRLSVL EQLLDEGADP
     NCCDSQGRPA VIVAVVNKHY EAIPVLAQRG ADIDQQWGPF RNTALHEATL LGLEGRESIA
     TLLGCNANAQ KKNTRGQTAY DIALEMGDDL TSSLFAAKFT QGLEDQLSPP GNRILGDS
//
ID   PAK7_MOUSE              Reviewed;         719 AA.
AC   Q8C015; Q3TQJ7; Q6RWS7;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Serine/threonine-protein kinase PAK 7;
DE            EC=2.7.11.1;
DE   AltName: Full=p21-activated kinase 5;
DE            Short=PAK-5;
DE   AltName: Full=p21-activated kinase 7;
DE            Short=PAK-7;
GN   Name=Pak7; Synonyms=Pak5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND DISRUPTION PHENOTYPE.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=22879895; PubMed=14517284;
RX   DOI=10.1128/MCB.23.20.7134-7142.2003;
RA   Li X., Minden A.;
RT   "Targeted disruption of the gene for the PAK5 kinase in mice.";
RL   Mol. Cell. Biol. 23:7134-7142(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104 AND THR-107, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
CC   -!- FUNCTION: The activated kinase acts on a variety of targets (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts tightly with GTP-bound but not GDP-bound
CC       CDC42/p21 and RAC1 (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and eye. Also
CC       expressed in adrenal gland, pancreas, prostate and testes. Within
CC       the brain, expression is restricted to neurons. Present in brain
CC       but not in kidney, lung and spleen (at protein level).
CC   -!- DEVELOPMENTAL STAGE: Expressed in fetal brain.
CC   -!- PTM: Autophosphorylated when activated by CDC42/p21 (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice are viable and fertile, and show normal
CC       development of brain, eye, pancreas and adrenal gland.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC   -!- SIMILARITY: Contains 1 CRIB domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY487425; AAR37415.1; -; mRNA.
DR   EMBL; AK032593; BAC27939.1; -; mRNA.
DR   EMBL; AK163530; BAE37385.1; -; mRNA.
DR   IPI; IPI00225805; -.
DR   RefSeq; NP_766446.2; NM_172858.2.
DR   UniGene; Mm.131572; -.
DR   ProteinModelPortal; Q8C015; -.
DR   SMR; Q8C015; 10-93, 422-718.
DR   STRING; Q8C015; -.
DR   PRIDE; Q8C015; -.
DR   Ensembl; ENSMUST00000035264; ENSMUSP00000047285; ENSMUSG00000039913.
DR   Ensembl; ENSMUST00000077200; ENSMUSP00000076440; ENSMUSG00000039913.
DR   GeneID; 241656; -.
DR   KEGG; mmu:241656; -.
DR   UCSC; uc008moh.1; mouse.
DR   CTD; 241656; -.
DR   MGI; MGI:1920334; Pak7.
DR   eggNOG; roNOG04742; -.
DR   GeneTree; ENSGT00580000081260; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108518; -.
DR   InParanoid; Q8C015; -.
DR   OMA; LQEPMMP; -.
DR   OrthoDB; EOG4RNB7X; -.
DR   PhylomeDB; Q8C015; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 385114; -.
DR   ArrayExpress; Q8C015; -.
DR   Bgee; Q8C015; -.
DR   CleanEx; MM_PAK7; -.
DR   Genevestigator; Q8C015; -.
DR   GermOnline; ENSMUSG00000039913; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
DR   GO; GO:0006916; P:anti-apoptosis; IDA:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000095; PAK_box_Rho-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00786; PBD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00285; PBD; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    719       Serine/threonine-protein kinase PAK 7.
FT                                /FTId=PRO_0000086478.
FT   DOMAIN       11     24       CRIB.
FT   DOMAIN      449    700       Protein kinase.
FT   NP_BIND     455    463       ATP (By similarity).
FT   REGION       25    448       Linker.
FT   ACT_SITE    568    568       Proton acceptor (By similarity).
FT   BINDING     478    478       ATP (By similarity).
FT   MOD_RES     104    104       Phosphoserine.
FT   MOD_RES     107    107       Phosphothreonine.
FT   CONFLICT    315    315       S -> F (in Ref. 1; AAR37415).
FT   CONFLICT    320    320       R -> G (in Ref. 1; AAR37415).
FT   CONFLICT    454    454       K -> R (in Ref. 1; AAR37415).
FT   CONFLICT    522    522       V -> A (in Ref. 1; AAR37415).
FT   CONFLICT    664    664       K -> E (in Ref. 1; AAR37415).
FT   CONFLICT    687    687       Q -> R (in Ref. 1; AAR37415).
SQ   SEQUENCE   719 AA;  80948 MW;  5E16D2318C238C8D CRC64;
     MFGKKKKKIE ISGPSNFEHR VHTGFDPQEQ KFTGLPQQWH SLLADTANRP KPMVDPSCIT
     PIQLAPMKTI VRGNKSCKET SINGLLEDFD NISVTRSNSL RKESPPTPDQ GAASRIQGHS
     EENGFITFSQ YSSESDTTAD YTTEKYRDRS LYGDDLDLYY KSSHAAKQNG HAMKMKHGDA
     YYPEMKSLKT DLAGFPVDYH THLDSLRKSS EYGDLRWDYQ RASSSSPLDY SFQLTPSRTA
     GTSRCSKESL AYSESDWGPS LDDYDRRPKS SYLHQTSPQP AMRQRSKSGS GLQEPMMPFG
     ASAFKTHPQG HSYNSYTYPR LSEPTMCIPK VDYDRAQMVF SPPLSGSDTY PRGPTKLPQS
     QSKAGYSSGS HQYPSGYHKA SLYHHPSLQT SSQYISTASY LSSLSISSST YPPPSWGSSS
     DQQPSRVSHE QFRAALQLVV SPGDPREYLD NFIKIGEGST GIVCIATEKH TGKQVAVKKM
     DLRKQQRREL LFNEVVIMRD YHHDNVVDMY NSYLVGDELW VVMEFLEGGA LTDIVTHTRM
     NEEQIATVCL SVLKALSYLH NQGVIHRDIK SDSILLTSDG RIKLSDFGFC AQVSKEVPKR
     KSLVGTPYWM APEVISRLPY GTEVDIWSLG IMVIEMIDGE PPYFNEPPLQ AMRRIRDSLP
     PRVKDLHKVS SMLRGFLDLM LVREPSQRAT AQELLGHPFL KLAGPPSCIV PLMRQYRHH
//
ID   LRC4C_MOUSE             Reviewed;         640 AA.
AC   Q8C031; Q505E5; Q8BGH8;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Leucine-rich repeat-containing protein 4C;
DE   AltName: Full=Netrin-G1 ligand;
DE            Short=NGL-1;
DE   Flags: Precursor;
GN   Name=Lrrc4c; Synonyms=Ngl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=14595443; DOI=10.1038/nn1148;
RA   Lin J.C., Ho W.-H., Gurney A.L., Rosenthal A.;
RT   "The netrin-G1 ligand NGL-1 promotes the outgrowth of thalamocortical
RT   axons.";
RL   Nat. Neurosci. 6:1270-1276(2003).
RN   [4]
RP   INTERACTION WITH WHRN.
RX   PubMed=15590698; DOI=10.1093/hmg/ddi036;
RA   Delprat B., Michel V., Goodyear R., Yamasaki Y., Michalski N.,
RA   El-Amraoui A., Perfettini I., Legrain P., Richardson G.,
RA   Hardelin J.-P., Petit C.;
RT   "Myosin XVa and whirlin, two deafness gene products required for hair
RT   bundle growth, are located at the stereocilia tips and interact
RT   directly.";
RL   Hum. Mol. Genet. 14:401-410(2005).
CC   -!- FUNCTION: May promote neurite outgrowth of developing thalamic
CC       neurons.
CC   -!- SUBUNIT: Interacts with NTNG1 and WHRN.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in the developing cerebral
CC       cortex and striatum at 14 dpc.
CC   -!- DOMAIN: The LRR region is both necessary and sufficient for the
CC       interaction with NTNG1 (By similarity).
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 9 LRR (leucine-rich) repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK032467; BAC27884.1; -; mRNA.
DR   EMBL; AK034276; BAC28656.1; -; mRNA.
DR   EMBL; AK048322; BAC33302.1; -; mRNA.
DR   EMBL; BC094588; AAH94588.1; -; mRNA.
DR   IPI; IPI00309419; -.
DR   RefSeq; NP_848840.3; NM_178725.5.
DR   UniGene; Mm.241682; -.
DR   ProteinModelPortal; Q8C031; -.
DR   SMR; Q8C031; 45-487.
DR   DIP; DIP-42049N; -.
DR   MINT; MINT-1895606; -.
DR   STRING; Q8C031; -.
DR   PRIDE; Q8C031; -.
DR   Ensembl; ENSMUST00000162807; ENSMUSP00000125218; ENSMUSG00000090091.
DR   GeneID; 241568; -.
DR   KEGG; mmu:241568; -.
DR   CTD; 241568; -.
DR   MGI; MGI:2442636; Lrrc4c.
DR   GeneTree; ENSGT00600000084155; -.
DR   HOGENOM; HBG444724; -.
DR   HOVERGEN; HBG052359; -.
DR   InParanoid; Q8C031; -.
DR   OMA; WITPNGS; -.
DR   OrthoDB; EOG4XKV6K; -.
DR   PhylomeDB; Q8C031; -.
DR   NextBio; 385057; -.
DR   ArrayExpress; Q8C031; -.
DR   Bgee; Q8C031; -.
DR   CleanEx; MM_LRRC4C; -.
DR   Genevestigator; Q8C031; -.
DR   GermOnline; ENSMUSG00000050587; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0050770; P:regulation of axonogenesis; ISS:UniProtKB.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR000372; LRR-contain_N.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00560; LRR_1; 4.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00369; LRR_TYP; 4.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00013; LRRNT; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51450; LRR; 7.
PE   1: Evidence at protein level;
KW   Disulfide bond; Immunoglobulin domain; Leucine-rich repeat; Membrane;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     44       Potential.
FT   CHAIN        45    640       Leucine-rich repeat-containing protein
FT                                4C.
FT                                /FTId=PRO_0000015109.
FT   TRANSMEM    528    548       Helical; (Potential).
FT   REPEAT       75     98       LRR 1.
FT   REPEAT       99    122       LRR 2.
FT   REPEAT      123    146       LRR 3.
FT   REPEAT      148    170       LRR 4.
FT   REPEAT      172    195       LRR 5.
FT   REPEAT      196    217       LRR 6.
FT   REPEAT      218    241       LRR 7.
FT   REPEAT      243    265       LRR 8.
FT   REPEAT      266    289       LRR 9.
FT   DOMAIN      354    442       Ig-like C2-type.
FT   DISULFID    375    426       By similarity.
FT   CONFLICT    581    581       M -> V (in Ref. 1; BAC27884).
SQ   SEQUENCE   640 AA;  71992 MW;  9810515A995CAB6B CRC64;
     MLNKMTLHPQ QIMIGPRFNR ALFDPLLVVL LALQLLVVAG LVRAQTCPSV CSCSNQFSKV
     ICVRKNLREV PDGISTNTRL LNLHENQIQI IKVNSFKHLR HLEILQLSRN HIRTIEIGAF
     NGLANLNTLE LFDNRLTTIP NGAFVYLSKL KELWLRNNPI ESIPSYAFNR IPSLRRLDLG
     ELKRLSYISE GAFEGLSNLR YLNLAMCNLR EIPNLTPLIK LDELDLSGNH LSAIRPGSFQ
     GLMHLQKLWM IQSQIQVIER NAFDNLQSLV EINLAHNNLT LLPHDLFTPL HHLERIHLHH
     NPWNCNCDIL WLSWWIRDMA PSNTACCARC NTPPNLKGRY IGELDQNYFT CYAPVIVEPP
     ADLNVTEGMA AELKCRASTS LTSVSWITPN GTVMTHGAYK VRIAVLSDGT LNFTNVTVQD
     TGMYTCMVSN SVGNTTASAT LNVTAATTTP FSYFSTVTVE TMEPSQDEAR TTDNNVGPTP
     VIDWETTNVT TSLTPQSTRS TEKTFTIPVT DINSGIPGID EVMKTTKIII GCFVAITLMA
     AVMLVIFYKM RKQHHRQNHH APTRTVEIIN VDDEITGDTP MESHLPMPAI EHEHLNHYNS
     YKSPFNHTTT VNTINSIHSS VHEPLLIRMN SKDNVQETQI
//
ID   ARHGA_MOUSE             Reviewed;        1345 AA.
AC   Q8C033; Q5DU38; Q80VH8; Q8BW76; Q922S7;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Rho guanine nucleotide exchange factor 10;
GN   Name=Arhgef10; Synonyms=Kiaa0294;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Oviduct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND ALTERNATIVE
RP   SPLICING.
RX   MEDLINE=22870321; PubMed=14508709; DOI=10.1086/378159;
RA   Verhoeven K., De Jonghe P., Van de Putte T., Nelis E., Zwijsen A.,
RA   Verpoorten N., De Vriendt E., Jacobs A., Van Gerwen V., Francis A.,
RA   Ceuterick C., Huylebroeck D., Timmerman V.;
RT   "Slowed conduction and thin myelination of peripheral nerves
RT   associated with mutant rho Guanine-nucleotide exchange factor 10.";
RL   Am. J. Hum. Genet. 73:926-932(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May play a role in developmental myelination of
CC       peripheral nerves.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1;
CC         IsoId=Q8C033-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C033-2; Sequence=VSP_010707;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- DEVELOPMENTAL STAGE: Found in the neuroepithelium of the meninges
CC       at E8.5, and in the roof plate of the rhombencephalon at E9.5. In
CC       E12.5 embryos, it is ubiquitously expressed, with a pronounced
CC       expression in the neuroepithelium of brain vesicles, the neural
CC       tube, the ganglia and the neural layer of the retina.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH59212.1; Type=Erroneous initiation;
CC       Sequence=AAH66074.1; Type=Erroneous initiation;
CC       Sequence=BAC27875.1; Type=Erroneous initiation;
CC       Sequence=BAD90400.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK032452; BAC27875.1; ALT_INIT; mRNA.
DR   EMBL; AK054038; BAC35629.2; -; mRNA.
DR   EMBL; AK220332; BAD90400.1; ALT_INIT; mRNA.
DR   EMBL; BC006842; AAH06842.1; -; mRNA.
DR   EMBL; BC047430; AAH47430.1; -; mRNA.
DR   EMBL; BC059212; AAH59212.1; ALT_INIT; mRNA.
DR   EMBL; BC066074; AAH66074.1; ALT_INIT; mRNA.
DR   IPI; IPI00223579; -.
DR   IPI; IPI00474255; -.
DR   RefSeq; NP_001032825.1; NM_001037736.1.
DR   RefSeq; NP_766339.2; NM_172751.2.
DR   UniGene; Mm.240298; -.
DR   ProteinModelPortal; Q8C033; -.
DR   SMR; Q8C033; 389-685.
DR   STRING; Q8C033; -.
DR   PhosphoSite; Q8C033; -.
DR   PRIDE; Q8C033; -.
DR   Ensembl; ENSMUST00000084207; ENSMUSP00000081225; ENSMUSG00000071176.
DR   Ensembl; ENSMUST00000110800; ENSMUSP00000106424; ENSMUSG00000071176.
DR   GeneID; 234094; -.
DR   KEGG; mmu:234094; -.
DR   NMPDR; fig|10090.3.peg.18217; -.
DR   UCSC; uc009kzg.1; mouse.
DR   UCSC; uc009kzh.1; mouse.
DR   CTD; 234094; -.
DR   MGI; MGI:2444453; Arhgef10.
DR   GeneTree; ENSGT00600000084097; -.
DR   HOGENOM; HBG402923; -.
DR   HOVERGEN; HBG050570; -.
DR   InParanoid; Q8C033; -.
DR   OMA; ILKKTCA; -.
DR   OrthoDB; EOG4FR0QW; -.
DR   NextBio; 382014; -.
DR   ArrayExpress; Q8C033; -.
DR   Bgee; Q8C033; -.
DR   CleanEx; MM_ARHGEF10; -.
DR   Genevestigator; Q8C033; -.
DR   GermOnline; ENSMUSG00000071176; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00741; DH_1; FALSE_NEG.
DR   PROSITE; PS50010; DH_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil;
KW   Guanine-nucleotide releasing factor; Phosphoprotein.
FT   CHAIN         1   1345       Rho guanine nucleotide exchange factor
FT                                10.
FT                                /FTId=PRO_0000080927.
FT   DOMAIN      397    584       DH.
FT   COILED      307    335       Potential.
FT   MOD_RES     355    355       Phosphoserine.
FT   MOD_RES    1259   1259       Phosphoserine (By similarity).
FT   MOD_RES    1262   1262       Phosphoserine (By similarity).
FT   VAR_SEQ     283    321       Missing (in isoform 2).
FT                                /FTId=VSP_010707.
FT   CONFLICT    184    184       Missing (in Ref. 1; BAC35629).
FT   CONFLICT    196    196       R -> Q (in Ref. 1; BAC27875).
FT   CONFLICT    207    207       M -> I (in Ref. 2; BAD90400).
FT   CONFLICT    348    348       G -> R (in Ref. 2; BAD90400).
FT   CONFLICT    528    528       D -> Y (in Ref. 1; BAC27875).
FT   CONFLICT    581    581       L -> R (in Ref. 1; BAC35629).
FT   CONFLICT   1332   1332       V -> F (in Ref. 3; AAH06842).
SQ   SEQUENCE   1345 AA;  147946 MW;  8583299B5A4C5835 CRC64;
     MEQGEASPPV PAEHEAKCDT SNNEEEGELF DFDSGDEVPE ADRQVPSADD RTRGAEAGGA
     DENTCPAGNG TGAEPAPEAE PAKLVVPTKV NPYSVIDITP LQEDQPSSPD ANTEEEGVGL
     RVPSGYSVPV PCGYAVPSNL PLLLPAYSSP VIIRAESVEE EEAAETVGDG QCNSLSSEDL
     PHSSEQGSQE GSALARWAAD PANTAWMENP EEAIYDDVPR ENSDSEPDEM IYDDVENGEE
     GGNSSPEYGW SSSEFESYEE PSDSEGKNGI PRSFLRSSHK KQLSHDLTRF KAHCEEKMRG
     LVASTVGAME IQQAKQRQER KMQKLMKAAK EGTKDGLEKT KAAVKRGGSF IRTRSLVSQD
     HRCYFEEEQN LFIDVDCKHP EAVLTPMPEG LSQQQVVRRY ILGSIVESEK NYVDALRRIL
     EQYEKPLSEM EPRLLSDRKL RMVFYRVKEI LQCHSMFQIA LASRVSEWDV VETIGDVFVA
     SFSKSMVLDA YSEYVNNFST AVAVLKKTCA TKPAFLEFLK LSQDSSPDRV TLHSLMMRPI
     QRFPQFILLL QDMLKNTAKG HPDRLPLQMA LTELETLAEK LNERKRDADQ RCEIKQIAKA
     INERYLNKLL SSGNRYLVRS DDVIETVYND RGEIVKTKQR RIFMLNDVLM CATASSRNSH
     ESHAVMSQRY LLKWSVPLGH VDVIQYNGGS GAGEHCRHHA AHSPESLAVV ANAKPHKVYM
     GPGQLYQDLQ NLLHDLNVVG QISQLIGNLR GSYQNLNQSV AHDWTSGLQR LILRKEDAIR
     AADRCRIQLQ LPGKQDKSGR PTFFTAVFNT LTPAIKESWV SSLQMAKLAL EEENHMGWFC
     VDDDGNLAKK ETHPLLVGHM PVMVAKQPEF KIECAAYNPE PYLSNESQPA SPSTARGFLW
     IGSCSNQMGQ VAIVSFQGSN PKVIECFNVE SRILCMVYIP AEESKPQETT ETKDPEATAS
     RAPHVPTICL GTEEGSISIY KSSQGCKKVR LQHFYAPDKS TVMSLACSPQ GLYAGLVNGS
     VASYTKAPDG SWNSEPQQVI KLGVLPVRSL LLVEGALWAA SGGQVFMASV ETHTIENQLE
     AHQDEGMVIS HMAVAGVGIW IAFTSGSTLR LFHTETLKHL QDVNIDAPVH SMLPGHQRLS
     VTSLLVCHGL LMVGTSLGVV VALPVPRLQG IPKVTGRGMV SYHAHNGPVK FIVSATAFQN
     KDRARDSPRS GSELQDEDPK DLLCSEEGPS CPGQPDTYTS VWLGDSLGLP TQKNDLSSSS
     GSLNLSHGSS SLEHRSVDSS LCDLLRDPSA SPRSRPQGSR RARASSALVV CGGQGHRRVH
     RKARQPSQED LVSSVMVWQI PLLGM
//
ID   KKCC2_MOUSE             Reviewed;         588 AA.
AC   Q8C078; Q80TS0; Q8BXM8; Q8C0G3; Q8CH42; Q8QZT7;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 2.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Calcium/calmodulin-dependent protein kinase kinase 2;
DE            Short=CaM-KK 2;
DE            Short=CaM-kinase kinase 2;
DE            Short=CaMKK 2;
DE            EC=2.7.11.17;
DE   AltName: Full=Calcium/calmodulin-dependent protein kinase kinase beta;
DE            Short=CaM-KK beta;
DE            Short=CaM-kinase kinase beta;
DE            Short=CaMKK beta;
GN   Name=Camkk2; Synonyms=Kiaa0787;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   PubMed=12654522; DOI=10.1016/S0169-328X(02)00698-8;
RA   Vinet J., Carra S., Blom J.M.C., Harvey M., Brunello N., Barden N.,
RA   Tascedda F.;
RT   "Cloning of mouse Ca2+/calmodulin-dependent protein kinase kinase beta
RT   (CaMKKbeta) and characterization of CaMKKbeta and CaMKKalpha
RT   distribution in the adult mouse brain.";
RL   Brain Res. Mol. Brain Res. 111:216-221(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata, Retina, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 207-588 (ISOFORM 5).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=14586002;
RA   Peters M., Mizuno K., Ris L., Angelo M., Godaux E., Giese K.P.;
RT   "Loss of Ca2+/calmodulin kinase kinase beta affects the formation of
RT   some, but not all, types of hippocampus-dependent long-term memory.";
RL   J. Neurosci. 23:9752-9760(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-495, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129 AND SER-133, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Calcium/calmodulin-dependent protein kinase belonging to
CC       a proposed calcium-triggered signaling cascade involved in a
CC       number of cellular processes. Phosphorylates CAMK1, CAMK4 and
CC       CAMK1D (By similarity). Seems to be involved in hippocampal
CC       activation of CREB1.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Activated by Ca(2+)/calmodulin. Binding of
CC       calmodulin may releave intrasteric autoinhibition.
CC       Autophosphorylation does not alter activity or regulation by
CC       Ca(2+)/calmodulin. In part, activity is independent on
CC       Ca(2+)/calmodulin (By similarity).
CC   -!- SUBUNIT: Interacts with calmodulin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q8C078-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C078-2; Sequence=VSP_012155;
CC         Note=Phosphorylated on Ser-522 (By similarity);
CC       Name=3;
CC         IsoId=Q8C078-3; Sequence=VSP_012151, VSP_012152, VSP_012154;
CC       Name=4;
CC         IsoId=Q8C078-4; Sequence=VSP_012150, VSP_012153;
CC       Name=5;
CC         IsoId=Q8C078-5; Sequence=VSP_012156;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues tested. A
CC       differential expression pattern compared to CAMKK1 is observed in
CC       the brain.
CC   -!- DOMAIN: The autoinhibitory domain overlaps with the calmodulin
CC       binding region and may be involved in intrasteric autoinhibition.
CC   -!- DOMAIN: The RP domain (arginine/proline-rich) is involved in the
CC       recognition of CAMKI and CAMK4 as substrates (By similarity).
CC   -!- PTM: Autophosphorylated (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice are unable to form spatial long-term
CC       memory.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AF453383; AAN75696.1; -; mRNA.
DR   EMBL; AK031399; BAC27387.1; -; mRNA.
DR   EMBL; AK032070; BAC27681.1; -; mRNA.
DR   EMBL; AK044660; BAC32023.1; -; mRNA.
DR   EMBL; BC023103; AAH23103.1; -; mRNA.
DR   EMBL; AK122370; BAC65652.1; -; mRNA.
DR   IPI; IPI00404152; -.
DR   IPI; IPI00404236; -.
DR   IPI; IPI00457626; -.
DR   IPI; IPI00480226; -.
DR   IPI; IPI00480493; -.
DR   RefSeq; NP_001186605.1; NM_001199676.1.
DR   RefSeq; NP_663333.1; NM_145358.2.
DR   UniGene; Mm.289237; -.
DR   UniGene; Mm.394637; -.
DR   UniGene; Mm.474852; -.
DR   ProteinModelPortal; Q8C078; -.
DR   SMR; Q8C078; 160-448.
DR   STRING; Q8C078; -.
DR   PhosphoSite; Q8C078; -.
DR   PRIDE; Q8C078; -.
DR   Ensembl; ENSMUST00000047365; ENSMUSP00000048135; ENSMUSG00000029471.
DR   Ensembl; ENSMUST00000086224; ENSMUSP00000083401; ENSMUSG00000029471.
DR   Ensembl; ENSMUST00000111667; ENSMUSP00000107296; ENSMUSG00000029471.
DR   Ensembl; ENSMUST00000111668; ENSMUSP00000107297; ENSMUSG00000029471.
DR   GeneID; 207565; -.
DR   KEGG; mmu:207565; -.
DR   NMPDR; fig|10090.3.peg.12398; -.
DR   UCSC; uc008zly.1; mouse.
DR   UCSC; uc008zlz.1; mouse.
DR   UCSC; uc008zmc.1; mouse.
DR   CTD; 207565; -.
DR   MGI; MGI:2444812; Camkk2.
DR   GeneTree; ENSGT00530000063214; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG052262; -.
DR   InParanoid; Q8C078; -.
DR   OMA; CICPSLP; -.
DR   OrthoDB; EOG4C5CJQ; -.
DR   PhylomeDB; Q8C078; -.
DR   BRENDA; 2.7.11.17; 244.
DR   NextBio; 371961; -.
DR   ArrayExpress; Q8C078; -.
DR   Bgee; Q8C078; -.
DR   Genevestigator; Q8C078; -.
DR   GermOnline; ENSMUSG00000029471; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:EC.
DR   GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Calmodulin-binding; Cytoplasm;
KW   Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    588       Calcium/calmodulin-dependent protein
FT                                kinase kinase 2.
FT                                /FTId=PRO_0000086145.
FT   DOMAIN      165    446       Protein kinase.
FT   NP_BIND     171    179       ATP (By similarity).
FT   REGION      204    226       RP domain.
FT   REGION      472    477       Autoinhibitory domain (By similarity).
FT   REGION      475    500       Calmodulin-binding (By similarity).
FT   COMPBIAS    549    552       Poly-Gly.
FT   ACT_SITE    312    312       Proton acceptor (By similarity).
FT   BINDING     194    194       ATP (By similarity).
FT   MOD_RES      99     99       Phosphoserine (By similarity).
FT   MOD_RES     129    129       Phosphoserine.
FT   MOD_RES     133    133       Phosphoserine.
FT   MOD_RES     495    495       Phosphoserine.
FT   MOD_RES     511    511       Phosphoserine (By similarity).
FT   VAR_SEQ     485    503       ILVKTMIRKRSFGNPFEGS -> VRRAGPLTKNKNRESPRQ
FT                                G (in isoform 4).
FT                                /FTId=VSP_012150.
FT   VAR_SEQ     498    498       N -> T (in isoform 3).
FT                                /FTId=VSP_012151.
FT   VAR_SEQ     499    507       Missing (in isoform 3).
FT                                /FTId=VSP_012152.
FT   VAR_SEQ     504    588       Missing (in isoform 4).
FT                                /FTId=VSP_012153.
FT   VAR_SEQ     508    588       RSLSAPGNLLTKKPTREWEPLSEPKEARQRRQPPGPRAGPC
FT                                GGGGSALVKGGPCVESWGAPAPGSPPRMPPLQPEEVMEPE
FT                                -> RSKVAAGRNVPCQRLETCSRSKAAKTAPGAQSRPLWGR
FT                                RKCSCERWSLRGKLGGSGPWLPTTHASTAARGGDGAGVAAW
FT                                TT (in isoform 3).
FT                                /FTId=VSP_012154.
FT   VAR_SEQ     520    541       KPTREWEPLSEPKEARQRRQPP -> QGSEDSPRGPEPAPV
FT                                GEEEVLL (in isoform 2).
FT                                /FTId=VSP_012155.
FT   VAR_SEQ     533    588       EARQRRQPPGPRAGPCGGGGSALVKGGPCVESWGAPAPGSP
FT                                PRMPPLQPEEVMEPE -> VNACLPACAIASPPLGPGGGQL
FT                                QSKHVGISSRQDVPSAGAAVPGSLRASGFPARGIQGLGSHG
FT                                VSCMRAGLRCMALHPECLRTYPGSSGPLDG (in
FT                                isoform 5).
FT                                /FTId=VSP_012156.
FT   CONFLICT    176    176       Y -> F (in Ref. 2; BAC32023).
FT   CONFLICT    290    290       R -> H (in Ref. 2; BAC27681).
FT   CONFLICT    396    398       MCL -> IWR (in Ref. 1).
FT   CONFLICT    401    401       K -> R (in Ref. 1).
SQ   SEQUENCE   588 AA;  64618 MW;  AED7433ADB3477A5 CRC64;
     MSSCVSSQPT SDRVAPQDEL GSGGGSREGQ KPCEALRGLS SLSIHLGMES FIVVTECEPG
     RGVDLNLARD QPPEADGQEL PLEASDPESR SPLSGRKMSL QEPSQGGPAS SSNSLDMNGR
     CICPSLSYSP ASSPQSSPRM PRRPTVESHH VSITGLQDCV QLNQYTLKDE IGKGSYGVVK
     LAYNENDNTY YAMKVLSKKK LIRQAGFPRR PPPRGARPAP GGCIQPRGPI EQVYQEIAIL
     KKLDHPNVVK LVEVLDDPNE DHLYMVFELV NQGPVMEVPT LKPLSEDQAR FYFQDLIKGI
     EYLHYQKIIH RDIKPSNLLV GEDGHIKIAD FGVSNEFKGS DALLSNTVGT PAFMAPESLS
     ETRKIFSGKA LDVWAMGVTL YCFVFGQCPF MDERIMCLHS KIKSQALEFP DQPDIAEDLK
     DLITRMLDKN PESRIVVPEI KLHPWVTRHG AEPLPSEDEN CTLVEVTEEE VENSVKHIPS
     LATVILVKTM IRKRSFGNPF EGSRREERSL SAPGNLLTKK PTREWEPLSE PKEARQRRQP
     PGPRAGPCGG GGSALVKGGP CVESWGAPAP GSPPRMPPLQ PEEVMEPE
//
ID   FA40A_MOUSE             Reviewed;         837 AA.
AC   Q8C079; Q80T92; Q8BZC6; Q8CIF7;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Protein FAM40A;
GN   Name=Fam40a; Synonyms=Kiaa1761;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-837 (ISOFORM 3).
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 AND SER-831, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8C079-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C079-2; Sequence=VSP_014865;
CC         Note=No experimental confirmation available. Ref.1 (BAC29206)
CC         sequence differs from that shown due to several frameshifts;
CC       Name=3;
CC         IsoId=Q8C079-3; Sequence=VSP_014866;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q8C079-4; Sequence=VSP_014863;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the FAM40 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK032065; BAC27678.1; -; mRNA.
DR   EMBL; AK035833; BAC29206.1; ALT_FRAME; mRNA.
DR   EMBL; BC023952; AAH23952.1; -; mRNA.
DR   EMBL; AK122553; BAC65835.1; -; Unassigned_RNA.
DR   IPI; IPI00223670; -.
DR   IPI; IPI00403187; -.
DR   IPI; IPI00406150; -.
DR   IPI; IPI00607972; -.
DR   RefSeq; NP_705791.2; NM_153563.2.
DR   UniGene; Mm.278643; -.
DR   PhosphoSite; Q8C079; -.
DR   PRIDE; Q8C079; -.
DR   Ensembl; ENSMUST00000064759; ENSMUSP00000068587; ENSMUSG00000014601.
DR   Ensembl; ENSMUST00000106707; ENSMUSP00000102318; ENSMUSG00000014601.
DR   GeneID; 229707; -.
DR   KEGG; mmu:229707; -.
DR   NMPDR; fig|10090.3.peg.8788; -.
DR   UCSC; uc008qxg.1; mouse.
DR   CTD; 229707; -.
DR   MGI; MGI:2443884; Fam40a.
DR   GeneTree; ENSGT00400000022095; -.
DR   HOGENOM; HBG356504; -.
DR   HOVERGEN; HBG081506; -.
DR   InParanoid; Q8C079; -.
DR   OMA; QFEYMAQ; -.
DR   OrthoDB; EOG49GKG0; -.
DR   PhylomeDB; Q8C079; -.
DR   NextBio; 379627; -.
DR   ArrayExpress; Q8C079; -.
DR   Bgee; Q8C079; -.
DR   Genevestigator; Q8C079; -.
DR   GermOnline; ENSMUSG00000014601; Mus musculus.
DR   InterPro; IPR021819; DUF3402.
DR   InterPro; IPR012486; N1221.
DR   Pfam; PF11882; DUF3402; 1.
DR   Pfam; PF07923; N1221; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Phosphoprotein.
FT   CHAIN         1    837       Protein FAM40A.
FT                                /FTId=PRO_0000187019.
FT   COMPBIAS      3     36       Pro-rich.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      59     59       Phosphoserine.
FT   MOD_RES     335    335       Phosphoserine.
FT   MOD_RES     560    560       Phosphoserine.
FT   MOD_RES     831    831       Phosphoserine.
FT   VAR_SEQ       1    126       Missing (in isoform 4).
FT                                /FTId=VSP_014863.
FT   VAR_SEQ     430    837       Missing (in isoform 2).
FT                                /FTId=VSP_014865.
FT   VAR_SEQ     555    629       Missing (in isoform 3).
FT                                /FTId=VSP_014866.
FT   CONFLICT    104    104       D -> A (in Ref. 1; BAC27678).
FT   CONFLICT    347    347       Q -> H (in Ref. 1; BAC27678).
SQ   SEQUENCE   837 AA;  95585 MW;  BD984594F049D3F4 CRC64;
     MEPAAAGPGP LIVNNKQPQP PPPPPPATAQ PPPGAPRAAG GLLPGGKARE FNRNQRKDSE
     GYSESPDLEF EYADTDKWAA ELAELYSYTE GPEFLMNRKC FEEDFRIHVS DKKWTELDTN
     QHRTHAMRLL DGLEVTAREK RLKVARAILY VAQGTFGECS SEAEVQFWMR YNIFLLLEVG
     TFNALVELLN MEIDNSAACS SAVRKPAISL ADSTDLRVLL NIMYLIVETV HQDCDGDKAE
     WRTMRQTFRA ELGSPLYNNE PFAIMLFGMV TKFCSGHAPH FPMKKVLLLL WKTVLCTLGG
     FEELQSMKAE KRTLLGLPPL PEDSIKVIRN MRAASPPASA SDLIEQQQKR GRREHKALIK
     QDNLDAFNER DPYKADDSRE EEEENDDDSS LEGEAFPLER DEVMPPPLQH PQTDRLTCPK
     GLPWAPKVRE KDIEMFLESS RSKFIGYTLG SDTNTVVGLP RPIHESIKTL KQHKYTSIAE
     VQAQMEEEYL RSPLSGGEEE VEQVPAETLY QGLLPSLPQY MIALLKILLA AAPTSKAKTD
     SINILADVLP EEMPTTVLQS MKLGVDVNRH KEVIVKAISA VLLLLLKHFK LNHIYQFEYM
     AQHLVFANCI PLILKFFNQN IMSYITAKNS ISVLDYPHCV VNELPELTAE SLEAGDNNQF
     CWRNLFSCIN LLRILNKLTK WKHSRTMMLV VFKSAPILKR ALKVKQAMMQ LYVLKLLKVQ
     TKYLGRQWRK SNMKTMSAIY QKVRHRLNDD WAYGNDLDAR PWDFQAEECA LRANIERFNA
     RRYDRTHSNP DFLPVDNCLQ SVLGQRVDLP EDFQMNYDLW LEREVFSKPI SWEELLQ
//
ID   F190A_MOUSE             Reviewed;         895 AA.
AC   Q8C0C4; Q3KN97; Q69ZD5; Q8C822;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Protein FAM190A;
GN   Name=Fam190a; Synonyms=Kiaa1680;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 513-895 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 321-895 (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493; SER-494 AND
RP   SER-495, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8C0C4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C0C4-2; Sequence=VSP_035320, VSP_035321;
CC       Name=3;
CC         IsoId=Q8C0C4-3; Sequence=VSP_035322, VSP_035323;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the FAM190 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32509.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK031754; BAC27537.1; -; mRNA.
DR   EMBL; AK048645; BAC33408.1; -; mRNA.
DR   EMBL; AC122505; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC103630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC113320; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC122524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC125119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC137119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC168089; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC174640; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC174778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC107398; AAI07399.1; -; mRNA.
DR   EMBL; BC107399; AAI07400.1; -; mRNA.
DR   EMBL; BC117738; AAI17739.1; -; mRNA.
DR   EMBL; AK173231; BAD32509.1; ALT_INIT; mRNA.
DR   IPI; IPI00405752; -.
DR   IPI; IPI00875700; -.
DR   IPI; IPI00903408; -.
DR   RefSeq; NP_001157788.1; NM_001164316.1.
DR   RefSeq; NP_899133.2; NM_183310.2.
DR   UniGene; Mm.150324; -.
DR   UniGene; Mm.376946; -.
DR   PhosphoSite; Q8C0C4; -.
DR   PRIDE; Q8C0C4; -.
DR   Ensembl; ENSMUST00000045522; ENSMUSP00000040251; ENSMUSG00000039578.
DR   GeneID; 232035; -.
DR   KEGG; mmu:232035; -.
DR   CTD; 232035; -.
DR   MGI; MGI:3045354; Fam190a.
DR   eggNOG; roNOG06999; -.
DR   GeneTree; ENSGT00510000048616; -.
DR   HOGENOM; HBG713497; -.
DR   InParanoid; Q8C0C4; -.
DR   OMA; CSTESSS; -.
DR   OrthoDB; EOG43TZV2; -.
DR   ArrayExpress; Q8C0C4; -.
DR   Bgee; Q8C0C4; -.
DR   Genevestigator; Q8C0C4; -.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Phosphoprotein.
FT   CHAIN         1    895       Protein FAM190A.
FT                                /FTId=PRO_0000349293.
FT   COILED      675    705       Potential.
FT   COMPBIAS     28    202       Ser-rich.
FT   MOD_RES     493    493       Phosphoserine.
FT   MOD_RES     494    494       Phosphoserine.
FT   MOD_RES     495    495       Phosphoserine.
FT   VAR_SEQ     440    485       VLASSLSPYREGRYIERRLRSSSEGTAGSSRMVLKPKDGHV
FT                                EASSL -> GMQIFLVQKLCTLIFILFEQLFLRHIVNERHV
FT                                SFVFIISVKSLLWF (in isoform 2).
FT                                /FTId=VSP_035320.
FT   VAR_SEQ     486    895       Missing (in isoform 2).
FT                                /FTId=VSP_035321.
FT   VAR_SEQ     721    743       GLSLKRLEAVQGGRETTHRNRTM -> TNLKHLGAFRRIIP
FT                                GINGIPNSY (in isoform 3).
FT                                /FTId=VSP_035322.
FT   VAR_SEQ     744    895       Missing (in isoform 3).
FT                                /FTId=VSP_035323.
FT   CONFLICT    432    432       G -> R (in Ref. 1; BAC27537).
SQ   SEQUENCE   895 AA;  98217 MW;  F630C3EB4233E4A9 CRC64;
     MGDSGSRRCT LVSRLPIFRK SINRRHDSLP SSPSSSNTAG VHSSSPSSTN SSSGSTGKRR
     SIFRAPSISF HHKKGSEPKP EPTEQNLSIS NGAQPSHSNM QKLSLEEHVK TRGRHSVGFS
     SSRSKKITRS LTEDFEREKE PSTNKNVFIN CLSSGRSEGD DSGFTEEQSR RSIKQSTKKL
     LPKSFSSHYK FCKSVPQSQS TSLIQQPEFS LAIAQYQEQE AALGRPSPSC SVDVTERAGS
     SLQSPLLSAD LTTAQTPSEF LALTEDSLSE ADAFPKSGST ASHCDNFGHN DATSQPTSSL
     TAVSKTKMEF VGTAPCVMSP GRYRLEGRCS TELHSSPETP AGNRREVSLQ STELSVGNGS
     DPETHLPAHH QRGESPLAHA GEPALRTGSP RTLGSYDQHK ALAERFKGVH PVSDSRVIPS
     SGDHVFNKTS YGYEASAAKV LASSLSPYRE GRYIERRLRS SSEGTAGSSR MVLKPKDGHV
     EASSLRKHRT GSSSSKMNSL DVLNHLGSCE LDEDDLMLDL EFLEEQNLQP PVCREDSCHS
     VMSCTAVLLS PVDPGKEVNM LEEPKCPEPS KQNLSLRITK DTDQEARCSH VSCMPNSPSA
     DWPQQGVEEN GGIDSLPFRL MLQECTAVKT LLLKMKRVLQ ESDVSPSSST TSLPISPLTE
     EPLPFKDITR DECSMLRLQL KDRDELISQL QAELEKVQHL QKAFASRVDK STQTELLGCD
     GLSLKRLEAV QGGRETTHRN RTMSQSHSTR DRKAIHTPTE DRFRYSTADQ TSPYKNICQL
     PGLCLSNFLK DKELGGVMKH TRGNHEAVTS EMTQNSRTTM GQSFLKAAAK PEGLPMFSEK
     PKDPAALSRQ HSTFTGRFGQ PPRGPISLHT YSRKNVFLHH NLHTTEFQTL GQQDG
//
ID   RHG12_MOUSE             Reviewed;         838 AA.
AC   Q8C0D4; Q8BVP8;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Rho GTPase-activating protein 12;
DE   AltName: Full=Rho-type GTPase-activating protein 12;
GN   Name=Arhgap12;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-584, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238 AND TYR-241, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-229; SER-238 AND
RP   TYR-241, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-513, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-204; THR-229
RP   AND SER-238, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting
CC       them to an inactive GDP-bound state (By similarity).
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SIMILARITY: Contains 2 WW domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK031648; BAC27494.1; -; mRNA.
DR   EMBL; AK077063; BAC36587.1; -; mRNA.
DR   IPI; IPI00223751; -.
DR   RefSeq; NP_001034781.1; NM_001039692.1.
DR   RefSeq; NP_083553.2; NM_029277.2.
DR   UniGene; Mm.239675; -.
DR   ProteinModelPortal; Q8C0D4; -.
DR   SMR; Q8C0D4; 27-71, 457-567, 629-837.
DR   STRING; Q8C0D4; -.
DR   PhosphoSite; Q8C0D4; -.
DR   PRIDE; Q8C0D4; -.
DR   Ensembl; ENSMUST00000062584; ENSMUSP00000054209; ENSMUSG00000041225.
DR   GeneID; 75415; -.
DR   KEGG; mmu:75415; -.
DR   UCSC; uc008dzc.1; mouse.
DR   CTD; 75415; -.
DR   MGI; MGI:1922665; Arhgap12.
DR   eggNOG; roNOG08302; -.
DR   HOGENOM; HBG505851; -.
DR   HOVERGEN; HBG005328; -.
DR   InParanoid; Q8C0D4; -.
DR   OMA; QVYIEVE; -.
DR   PhylomeDB; Q8C0D4; -.
DR   NextBio; 342942; -.
DR   ArrayExpress; Q8C0D4; -.
DR   Bgee; Q8C0D4; -.
DR   CleanEx; MM_ARHGAP12; -.
DR   Genevestigator; Q8C0D4; -.
DR   GermOnline; ENSMUSG00000041225; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR015767; Rho_GTPase_activating.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   PANTHER; PTHR23181; Rho_GTPase_activating; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   SUPFAM; SSF51045; WW_Rsp5_WWP; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; FALSE_NEG.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   1: Evidence at protein level;
KW   GTPase activation; Phosphoprotein; Repeat; SH3 domain.
FT   CHAIN         1    838       Rho GTPase-activating protein 12.
FT                                /FTId=PRO_0000056715.
FT   DOMAIN       10     72       SH3.
FT   DOMAIN      263    296       WW 1.
FT   DOMAIN      355    388       WW 2.
FT   DOMAIN      466    567       PH.
FT   DOMAIN      648    836       Rho-GAP.
FT   MOD_RES     199    199       Phosphoserine.
FT   MOD_RES     204    204       Phosphoserine.
FT   MOD_RES     211    211       Phosphoserine (By similarity).
FT   MOD_RES     213    213       Phosphoserine (By similarity).
FT   MOD_RES     228    228       Phosphothreonine (By similarity).
FT   MOD_RES     229    229       Phosphothreonine.
FT   MOD_RES     238    238       Phosphoserine.
FT   MOD_RES     241    241       Phosphotyrosine.
FT   MOD_RES     513    513       Phosphothreonine.
FT   MOD_RES     584    584       Phosphoserine.
FT   CONFLICT     42     42       K -> N (in Ref. 1; BAC27494).
FT   CONFLICT     86     86       P -> A (in Ref. 1; BAC36587).
FT   CONFLICT    483    483       A -> P (in Ref. 1; BAC36587).
FT   CONFLICT    530    530       S -> T (in Ref. 1; BAC36587).
FT   CONFLICT    698    698       A -> T (in Ref. 1; BAC36587).
SQ   SEQUENCE   838 AA;  95352 MW;  C8660927694567AB CRC64;
     MAERSGKITA GQAYIEVEYD YEYDAKDRKI VIRQGERYLL VKKTNDDWWQ VRPDENSKAF
     YVPAQYVKEV TRKALMPPVK QATGLPNNSM KTIQSMHLQR STENVNKMPE LSSFGKPSSS
     VQGTGLIRDA NQNFGSNYNS GQTLNLSLDL THNNGKFNSD SHSPKVSSQN RTRLFGHFPG
     PEFLDIEKTS FSQEQSCDSA GEGSERIQQD SESGDELSSS STEQMRATTP PNQGRPDSPV
     YANLQELKIS QSALPPLPGS PAIQVNGEWE THKDSSGRCY YYNRTTQERT WKPPRWARDV
     STSRDFQSPG EQEPLSSEEN YHSSCFSQSD SQCGSPPRGW SEELDERGHT LYTSDYTKEK
     WLKHVDDQGR QYYYSADGSR SEWELPKYNA SSQQQREIIK SRSLDRRLQE PIVLTKWRHS
     TIVLDSNDKD SPTTTKLCLP ENESPPTSSK HQDPGQEKYG LLNVTKITEN GKKVRKNWLS
     SWAVLQGSSL LFTKTQGSST SWFGSNQSKP EFTVDLKGAV IEMASKDKSS KKNVFELKTR
     QGTELLIQSD NDAVINDWFK VLSSTINNQV AEADEAAEEE TPDSPGVEKH DKEKDQKELK
     KLRSMKGSSM DSSEQKKTKK NLKKFLTRRP TLQAVREKGY IKDQVFGSNL ANLCQRENGT
     VPKFVKLCIE HVEEHGLDVD GIYRVSGNLA VIQKLRFAVN HDEKLDLNDS KWEDIHVITG
     ALKMFFRELP EPLFTFNHFN DFVNAIKQEP RQRVTAVKDL IRQLPKPNQD TMQILFRHLK
     RVIENGEKNR MTYQSIAIVF GPTLLKPERE TGNIAVHTVY QNQIVELILL ELSTVFGR
//
ID   ETUD1_MOUSE             Reviewed;        1127 AA.
AC   Q8C0D5; Q80W46; Q8C198; Q8K0B8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Elongation factor Tu GTP-binding domain-containing protein 1;
GN   Name=Eftud1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skin, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon, and Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
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DR   EMBL; AK028676; BAC26061.1; -; mRNA.
DR   EMBL; AK031647; BAC27493.1; -; mRNA.
DR   EMBL; BC031852; AAH31852.1; -; mRNA.
DR   EMBL; BC045616; AAH45616.1; -; mRNA.
DR   IPI; IPI00453532; -.
DR   RefSeq; NP_001153144.1; NM_001159672.1.
DR   RefSeq; NP_780526.2; NM_175317.3.
DR   UniGene; Mm.238020; -.
DR   HSSP; O26359; 1G7S.
DR   ProteinModelPortal; Q8C0D5; -.
DR   SMR; Q8C0D5; 17-154.
DR   STRING; Q8C0D5; -.
DR   PhosphoSite; Q8C0D5; -.
DR   PRIDE; Q8C0D5; -.
DR   Ensembl; ENSMUST00000039881; ENSMUSP00000046046; ENSMUSG00000038563.
DR   Ensembl; ENSMUST00000107296; ENSMUSP00000102917; ENSMUSG00000038563.
DR   GeneID; 101592; -.
DR   KEGG; mmu:101592; -.
DR   CTD; 101592; -.
DR   MGI; MGI:2141969; Eftud1.
DR   eggNOG; roNOG12237; -.
DR   GeneTree; ENSGT00550000074806; -.
DR   HOGENOM; HBG737692; -.
DR   HOVERGEN; HBG101597; -.
DR   InParanoid; Q8C0D5; -.
DR   OMA; EDFQNSV; -.
DR   OrthoDB; EOG4JHCF0; -.
DR   PhylomeDB; Q8C0D5; -.
DR   NextBio; 355030; -.
DR   ArrayExpress; Q8C0D5; -.
DR   Bgee; Q8C0D5; -.
DR   Genevestigator; Q8C0D5; -.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR009022; Elongation_fac_G/III/V.
DR   InterPro; IPR000795; ProtSyn_GTP-bd.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR000640; Transl_elong_EFG/EF2_C.
DR   InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR   InterPro; IPR009000; Transl_elong_init/rib_B-barrel.
DR   Gene3D; G3DSA:3.30.230.10; Ribosomal_S5_D2-type_fold; 2.
DR   Gene3D; G3DSA:3.30.70.240; Transl_elong_EFG/EF2_C; 1.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SUPFAM; SSF54980; EFG_III_V; 2.
DR   SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR   SUPFAM; SSF50447; Translat_factor; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; EFACTOR_GTP; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Acetylation; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN         1   1127       Elongation factor Tu GTP-binding domain-
FT                                containing protein 1.
FT                                /FTId=PRO_0000313806.
FT   NP_BIND      26     33       GTP (By similarity).
FT   NP_BIND      92     96       GTP (By similarity).
FT   NP_BIND     146    149       GTP (By similarity).
FT   MOD_RES     528    528       N6-acetyllysine (By similarity).
FT   CONFLICT    249    249       A -> P (in Ref. 2; AAH45616).
FT   CONFLICT    452    452       K -> N (in Ref. 1; BAC26061).
SQ   SEQUENCE   1127 AA;  125777 MW;  333623236F83E4E6 CRC64;
     MVLSGVDKMI RLQKNTANIR NICVLAHVDH GKTTLADCLI SSNGIISSRL AGKLRYMDSR
     EDEQVRGITM KSSAISLHYA EGHEEYLINL IDSPGHVDFS SEVSTAVRIC DGCIIVVDAV
     EGVCPQTQAV LRQAWLENIR PVLVINKIDR LIVELKFTPQ EAYSHLKNIL EQINALTGTL
     FTSKVLEERA ERETESQAKP HSEQGEQVYD WSAGLEDVDD SQLYFSPEQG NVVFTSAIDG
     WGFGIEHFAR IYSQKIGIKK EVLLKTLWGD YYINMKAKKI MKVDQAKGKK PLFVQLILEN
     IWSLYDAVLK KDKEKIDKIV TSLGLKIGAR EARHSDPKVQ INAICSQWLP ISHAVLAMVC
     HKLPSPLDMT SERVEKLLCT GSQTFESLPP ETQALKAAFM KCGSEDTAPV IIFVSKMFAV
     DVKALPQNKP RPLTQEEMAQ RRERARQRHA EKLAAAQGQT SQGPTQDGGA LETSPHEDEP
     RGDEPDVASV SRQPVSQEES SQEAFIAFAR VFSGIARRGK KIFVLGPKYS PVDFLQRVPL
     GFSAPLEDLP PVPHMACCTL ENLYLLMGRE LEDLEEVPPG NVLGIGGLQD FVLKSATLCS
     LPSCPPFIPL NFEATPIVRV AVEPKHPSEM PQLVKGMKLL NQADPCVQVL IQETGEHVLV
     TAGEVHLQRC LDDLRERFAK IHISVSEPII PFRETITKPP KVDMVNEEIG RQQKVAVIHQ
     TKEEQSKIPE GIHVDSDGLI TIPTPNKLAT LSVRAIPLPE EVTRILEENS DLIRSMELLT
     SSLNEGRNTQ AIHQKTQEKI WEFKGKLEKH LTGRKWRNTV DQIWSFGPRK CGPNILVSRS
     EDFQNSVWSG PAGRESKEAS RFRDFGNSIV SGFQLATLSG PMCEEPLMGV CFVLEKWELN
     KCAEQGASDK QHQGQCDLAG EGQGGGKTCH VGDENQEQQD VCSEPFEETS QKGDSPVIDC
     YGPFSGQLIA TMKEACRYAL QVKPQRLMAA MYTCDIMATS DVLGRVYAVL SKREGRVLQE
     EMKEGTDMFI IKAVLPVAES FGFADEIRKR TSGLASPQLV FSHWEVIPSD PFWVPTTEEE
     YLHFGEKADS ENQARKYMNA VRKRKGLYVE EKIVEHAEKQ RTLSKNK
//
ID   CEP68_MOUSE             Reviewed;         733 AA.
AC   Q8C0D9; Q3US49; Q5SW85; Q8R2V0;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Centrosomal protein of 68 kDa;
DE            Short=Cep68;
GN   Name=Cep68;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=129; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8C0D9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C0D9-2; Sequence=VSP_013477;
CC         Note=No experimental confirmation available;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK031622; BAC27484.1; -; mRNA.
DR   EMBL; AK140820; BAE24488.1; -; mRNA.
DR   EMBL; AL606522; CAI24452.1; -; Genomic_DNA.
DR   EMBL; AL606522; CAI24453.1; -; Genomic_DNA.
DR   EMBL; BC027174; AAH27174.1; -; mRNA.
DR   IPI; IPI00309536; -.
DR   IPI; IPI00556751; -.
DR   RefSeq; NP_758464.2; NM_172260.3.
DR   UniGene; Mm.260314; -.
DR   ProteinModelPortal; Q8C0D9; -.
DR   PhosphoSite; Q8C0D9; -.
DR   PRIDE; Q8C0D9; -.
DR   Ensembl; ENSMUST00000050611; ENSMUSP00000054943; ENSMUSG00000044066.
DR   Ensembl; ENSMUST00000116392; ENSMUSP00000112093; ENSMUSG00000044066.
DR   GeneID; 216543; -.
DR   KEGG; mmu:216543; -.
DR   NMPDR; fig|10090.3.peg.23318; -.
DR   UCSC; uc007icw.1; mouse.
DR   UCSC; uc007icx.1; mouse.
DR   CTD; 216543; -.
DR   MGI; MGI:2667663; Cep68.
DR   GeneTree; ENSGT00390000000556; -.
DR   HOGENOM; HBG125065; -.
DR   HOVERGEN; HBG050898; -.
DR   InParanoid; Q8C0D9; -.
DR   OMA; ADTEDDP; -.
DR   OrthoDB; EOG4VX24N; -.
DR   NextBio; 375198; -.
DR   ArrayExpress; Q8C0D9; -.
DR   Bgee; Q8C0D9; -.
DR   CleanEx; MM_CEP68; -.
DR   Genevestigator; Q8C0D9; -.
DR   GermOnline; ENSMUSG00000044066; Mus musculus.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0051297; P:centrosome organization; ISS:UniProtKB.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   SMART; SM00150; SPEC; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Cytoskeleton; Phosphoprotein.
FT   CHAIN         1    733       Centrosomal protein of 68 kDa.
FT                                /FTId=PRO_0000089495.
FT   MOD_RES     459    459       Phosphoserine (By similarity).
FT   VAR_SEQ     647    733       QFKKDVDEHQSLTESVLEKGEILLQCLLDNTPVLKDVLERI
FT                                AKQSGELESRADHLYDSILASLDMLAGCTLIPDNRPTAAEH
FT                                PHEGL -> VICSPGLFIHGDGS (in isoform 2).
FT                                /FTId=VSP_013477.
FT   CONFLICT    228    228       P -> Q (in Ref. 1; BAC27484).
SQ   SEQUENCE   733 AA;  78749 MW;  15D93FCECDDC92A9 CRC64;
     MALSEDEAEA EVSVNTKVPS CGRWNSGKLL PSGLEPDQPL HLGVEGGPLW RAEADPGCIS
     GVFLSRVHTA SKEPVADRSK PPLRGPLPSA SVGTGEVLHS MGSQMEEDRL PASQDLLPAL
     QVFGTITVCS GQEADSEDFQ ATLDPSQVLG LSQQPHTSGL PLPPQWKSTV SPGAPQLSSR
     SISASSVGSS LQDHQEKAGP QRASFANVSS PELTVPQAAH SVVGAGPPLQ GSAQPLTSGS
     DATGLGKRHL SFQAEYWACA LPNSLPPSPN RHSALWDPNK EYEDLLDYTY PLRPGPQLPK
     QPESHVLTEP VLQDSGVDLD SLSVSPASTL KSPTNVSHNC SSAEVPTLPF SGARESCLKR
     WPLGIFQKQG GTSLSSWNQL ASTPRAPGTE DASWENREAA LRGTAEDCLP IGEDLRMGSP
     QLKTKEKEPP FPRQKRGRQH VSCPACVTPG WPSEEEVGSD EEYLALPTRL TQVSSLVSYS
     GARPSFVNLH TGAAEEHSSL QVSDSDKPAS PTLDSSHRKH PSGTSFQGPV GQNPCFRHSI
     QPQDSRGKSS LMSNQTLGVS SKPLKTQPAS KAMTDRRLFS ELVAGETLPR TTDEQEKASL
     VQCVQTFCCR LEELICWLYN VTDVADLSAP PRTSLTGLKS SLQLYRQFKK DVDEHQSLTE
     SVLEKGEILL QCLLDNTPVL KDVLERIAKQ SGELESRADH LYDSILASLD MLAGCTLIPD
     NRPTAAEHPH EGL
//
ID   VP26B_MOUSE             Reviewed;         336 AA.
AC   Q8C0E2; Q3TN45; Q8K2V3;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Vacuolar protein sorting-associated protein 26B;
DE   AltName: Full=Vesicle protein sorting 26B;
GN   Name=Vps26b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, and FVB/N;
RC   TISSUE=Brain, Mammary tumor, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH VPS35.
RX   PubMed=16190980; DOI=10.1111/j.1600-0854.2005.00328.x;
RA   Kerr M.C., Bennetts J.S., Simpson F., Thomas E.C., Flegg C.,
RA   Gleeson P.A., Wicking C., Teasdale R.D.;
RT   "A novel mammalian retromer component, Vps26B.";
RL   Traffic 6:991-1001(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302 AND SER-304, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Probable component of the retromer complex, a complex
CC       required to retrieve lysosomal enzyme receptors (IGF2R and M6PR)
CC       from endosomes to the trans-Golgi network.
CC   -!- SUBUNIT: Probable component of the retromer complex composed of
CC       VPS26 (VPS26A or VPS26B), VPS29, VPS35, SNX1 and SNX2. Interacts
CC       directly with VPS35.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC       protein. Note=Does not localize to endosomes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8C0E2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C0E2-2; Sequence=VSP_019927;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed in developing embryo
CC       and adult.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the VPS26 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK031589; BAC27465.1; -; mRNA.
DR   EMBL; AK150929; BAE29967.1; -; mRNA.
DR   EMBL; AK155578; BAE33333.1; -; mRNA.
DR   EMBL; AK165539; BAE38244.1; -; mRNA.
DR   EMBL; AK171154; BAE42279.1; -; mRNA.
DR   EMBL; BC029758; AAH29758.1; -; mRNA.
DR   EMBL; BC049180; AAH49180.1; -; mRNA.
DR   EMBL; BC052721; AAH52721.1; -; mRNA.
DR   EMBL; BC062972; AAH62972.1; -; mRNA.
DR   IPI; IPI00223759; -.
DR   IPI; IPI00775828; -.
DR   RefSeq; NP_821170.1; NM_178027.4.
DR   UniGene; Mm.218717; -.
DR   UniGene; Mm.440390; -.
DR   PDB; 2R51; X-ray; 2.10 A; A=7-336.
DR   PDB; 3LH8; X-ray; 2.60 A; A/B=7-336.
DR   PDB; 3LH9; X-ray; 2.40 A; A/B=7-336.
DR   PDB; 3LHA; X-ray; 2.80 A; A/B=7-336.
DR   PDBsum; 2R51; -.
DR   PDBsum; 3LH8; -.
DR   PDBsum; 3LH9; -.
DR   PDBsum; 3LHA; -.
DR   ProteinModelPortal; Q8C0E2; -.
DR   SMR; Q8C0E2; 9-296.
DR   STRING; Q8C0E2; -.
DR   PhosphoSite; Q8C0E2; -.
DR   PRIDE; Q8C0E2; -.
DR   Ensembl; ENSMUST00000034470; ENSMUSP00000034470; ENSMUSG00000031988.
DR   GeneID; 69091; -.
DR   KEGG; mmu:69091; -.
DR   UCSC; uc009oqe.1; mouse.
DR   UCSC; uc009oqf.1; mouse.
DR   CTD; 69091; -.
DR   MGI; MGI:1917656; Vps26b.
DR   eggNOG; roNOG12742; -.
DR   GeneTree; ENSGT00390000002588; -.
DR   HOGENOM; HBG525567; -.
DR   HOVERGEN; HBG082914; -.
DR   InParanoid; Q8C0E2; -.
DR   OMA; VVRKSMS; -.
DR   OrthoDB; EOG4X6C8P; -.
DR   PhylomeDB; Q8C0E2; -.
DR   NextBio; 328584; -.
DR   ArrayExpress; Q8C0E2; -.
DR   Bgee; Q8C0E2; -.
DR   CleanEx; MM_VPS26B; -.
DR   Genevestigator; Q8C0E2; -.
DR   GermOnline; ENSMUSG00000031988; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030904; C:retromer complex; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007034; P:vacuolar transport; IEA:InterPro.
DR   InterPro; IPR005377; VPS26.
DR   Pfam; PF03643; Vps26; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Membrane;
KW   Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1    336       Vacuolar protein sorting-associated
FT                                protein 26B.
FT                                /FTId=PRO_0000247090.
FT   MOD_RES     302    302       Phosphoserine.
FT   MOD_RES     304    304       Phosphoserine.
FT   MOD_RES     311    311       Phosphoserine (By similarity).
FT   MOD_RES     319    319       Phosphoserine (By similarity).
FT   MOD_RES     330    330       Phosphoserine (By similarity).
FT   VAR_SEQ     243    336       SIPIRLFLAGYELTPTMRDINKKFSVRYYLNLVLIDEEERR
FT                                YFKQQEVVLWRKGDIVRKSMSHQAAIASQRFEGTTSLGEVR
FT                                TPGQLSDNNSRQ -> PPGLGPLSLCSQTTCSVSALGKGSN
FT                                FEVKSLFYFIYLFIF (in isoform 2).
FT                                /FTId=VSP_019927.
FT   STRAND       10     14
FT   TURN         17     21
FT   STRAND       24     28
FT   STRAND       34     41
FT   STRAND       50     56
FT   STRAND       67     71
FT   STRAND       73     76
FT   HELIX        77     79
FT   STRAND       89     92
FT   STRAND      103    105
FT   STRAND      124    134
FT   STRAND      141    150
FT   STRAND      162    166
FT   TURN        169    171
FT   STRAND      172    179
FT   STRAND      181    184
FT   STRAND      193    198
FT   STRAND      202    215
FT   STRAND      222    234
FT   STRAND      259    262
FT   TURN        263    265
FT   STRAND      266    278
FT   STRAND      283    293
SQ   SEQUENCE   336 AA;  39125 MW;  AD5395AF30900018 CRC64;
     MSFFGFGQSV EVEILLNDAE SRKRAEHKTE DGKKEKYFLF YDGETVSGKV SLSLKNPNKR
     LEHQGIKIEF IGQIELYYDR GNHHEFVSLV KDLARPGEIT QSQAFDFEFT HVEKPYESYT
     GQNVKLRYFL RATISRRLND VVKEMDIVVH TLSTYPELNS SIKMEVGIED CLHIEFEYNK
     SKYHLKDVIV GKIYFLLVRI KIKHMEIDII KRETTGTGPN VYHENDTIAK YEIMDGAPVR
     GESIPIRLFL AGYELTPTMR DINKKFSVRY YLNLVLIDEE ERRYFKQQEV VLWRKGDIVR
     KSMSHQAAIA SQRFEGTTSL GEVRTPGQLS DNNSRQ
//
ID   Q8C0E9_MOUSE            Unreviewed;       390 AA.
AC   Q8C0E9;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   SubName: Full=Psd3 protein;
GN   Name=Psd3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC131913; AAI31914.1; -; mRNA.
DR   EMBL; BC145641; AAI45642.1; -; mRNA.
DR   EMBL; AK031477; BAC27421.1; -; mRNA.
DR   IPI; IPI00761957; -.
DR   UniGene; Mm.32525; -.
DR   HSSP; Q62261; 1BTN.
DR   ProteinModelPortal; Q8C0E9; -.
DR   PhosphoSite; Q8C0E9; -.
DR   PRIDE; Q8C0E9; -.
DR   Ensembl; ENSMUST00000059374; ENSMUSP00000060306; ENSMUSG00000030465.
DR   UCSC; uc009lwb.1; mouse.
DR   MGI; MGI:1918215; Psd3.
DR   eggNOG; roNOG10383; -.
DR   GeneTree; ENSGT00570000079011; -.
DR   HOVERGEN; HBG069382; -.
DR   ArrayExpress; Q8C0E9; -.
DR   Bgee; Q8C0E9; -.
DR   Genevestigator; Q8C0E9; -.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IDA:MGI.
DR   GO; GO:0032011; P:ARF protein signal transduction; IC:MGI.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001605; Spectrin_PH.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00683; SPECTRINPH.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   390 AA;  43761 MW;  D66E57CA1637E2B8 CRC64;
     MIGVNSVQSA SKVRVRTSGS VKYSREDSIR RQSHRSKSMK ISNSSEFSAK ESKALYNSIK
     NEKLEWAVDD EEKKKSPSEG TDEKANGTHP KTISRIGSTT NPFLDIPHDP NAAVYKSGFL
     ARKIHADMDG KKTPRGKRGW KTFYAVLKGT VLYLQKDEYK PEKSLSDEDL KNAVSVHHAL
     ASKATDYEKK PNVFKLKTAD WRVLLFQTQS PEEMQGWINK INCVAAVFSA PPFPAAIGSQ
     KKFSRPLLPA TTTKLSQEEQ LKSHESKLKQ ITTELAEHRS YPPDKKVKAK DVDEYKLKDH
     YLEFESLGQN QHSGGNELPS ERKHLLFCTR LLLGDISALL SIAHRHALQE GTAERRLGSF
     ILNDMNASVV RREADIQTQA ESLIPGAPFI
//
ID   ADAS_MOUSE              Reviewed;         645 AA.
AC   Q8C0I1;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Alkyldihydroxyacetonephosphate synthase, peroxisomal;
DE            Short=Alkyl-DHAP synthase;
DE            EC=2.5.1.26;
DE   AltName: Full=Alkylglycerone-phosphate synthase;
DE   Flags: Precursor;
GN   Name=Agps;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-57, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- CATALYTIC ACTIVITY: 1-acyl-glycerone 3-phosphate + a long-chain
CC       alcohol = an alkyl-glycerone 3-phosphate + a long-chain acid
CC       anion.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- PATHWAY: Glycerolipid metabolism; ether lipid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Peroxisome (By similarity).
CC   -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase
CC       type 4 family.
CC   -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK031049; BAC27229.1; -; mRNA.
DR   EMBL; BC063086; AAH63086.1; -; mRNA.
DR   IPI; IPI00756601; -.
DR   RefSeq; NP_766254.2; NM_172666.3.
DR   UniGene; Mm.31227; -.
DR   ProteinModelPortal; Q8C0I1; -.
DR   SMR; Q8C0I1; 69-644.
DR   STRING; Q8C0I1; -.
DR   PhosphoSite; Q8C0I1; -.
DR   PRIDE; Q8C0I1; -.
DR   Ensembl; ENSMUST00000047232; ENSMUSP00000041967; ENSMUSG00000042410.
DR   Ensembl; ENSMUST00000111951; ENSMUSP00000107582; ENSMUSG00000042410.
DR   GeneID; 228061; -.
DR   KEGG; mmu:228061; -.
DR   UCSC; uc008ket.1; mouse.
DR   CTD; 228061; -.
DR   MGI; MGI:2443065; Agps.
DR   GeneTree; ENSGT00530000063515; -.
DR   HOVERGEN; HBG004179; -.
DR   InParanoid; Q8C0I1; -.
DR   OrthoDB; EOG44XJGD; -.
DR   PhylomeDB; Q8C0I1; -.
DR   BRENDA; 2.5.1.26; 244.
DR   NextBio; 378913; -.
DR   ArrayExpress; Q8C0I1; -.
DR   Bgee; Q8C0I1; -.
DR   CleanEx; MM_AGPS; -.
DR   Genevestigator; Q8C0I1; -.
DR   GermOnline; ENSMUSG00000042410; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0008609; F:alkylglycerone-phosphate synthase activity; IEA:EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR016166; FAD-bd_2.
DR   InterPro; IPR016167; FAD-bd_2_sub1.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR016168; FAD-linked_Oxase_FAD-bd_sub2.
DR   InterPro; IPR004113; FAD-linked_oxidase_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   Gene3D; G3DSA:3.30.43.10; FAD-binding_2_sub1; 1.
DR   Gene3D; G3DSA:3.30.465.20; FAD-linked_oxidase_FAD-bd_sub2; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF55103; FAD-binding_2; 1.
DR   SUPFAM; SSF56176; FAD-binding_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; FAD; Flavoprotein; Lipid synthesis; Peroxisome;
KW   Phosphoprotein; Transferase; Transit peptide.
FT   TRANSIT       1     45       Peroxisome (By similarity).
FT   CHAIN        46    645       Alkyldihydroxyacetonephosphate synthase,
FT                                peroxisomal.
FT                                /FTId=PRO_0000231676.
FT   DOMAIN      189    371       FAD-binding PCMH-type.
FT   ACT_SITE    565    565       By similarity.
FT   MOD_RES      52     52       Phosphoserine.
FT   MOD_RES      57     57       Phosphoserine.
FT   MOD_RES      89     89       N6-acetyllysine (By similarity).
FT   MOD_RES     156    156       N6-acetyllysine (By similarity).
FT   MOD_RES     334    334       N6-acetyllysine (By similarity).
SQ   SEQUENCE   645 AA;  71684 MW;  EED5030FB7BA4A8B CRC64;
     MAEAAAGEAG ASERDPDAGR ARRRLRVLSG HLLGRPQEAP STNECKARRA ASAAGASPAA
     TPAAPESGTI PKKRQEVMKW NGWGYNDSKF LLNKKGQVEL TGKRYPLSGL VLPTLRDWIQ
     NTLGVSLEHK TTSKTSINPS EAPPSIVNED FLQELKEARI SYSQEADDRV FRAHGHCLHE
     IFLLREGMFE RIPDIVVWPT CHDDVVKIVN LACKYNLCII PIGGGTSVSY GLMCPADETR
     TIISLDTSQM NRILWVDENN LTAHVEAGIT GQDLERQLKE SGYCTGHEPD SLEFSTVGGW
     ISTRASGMKK NIYGNIEDLV VHMKMVTPRG VIEKSSQGPR MSTGPDIHHF IMGSEGTLGV
     ITEATIKIRP TPEYQKYGSV AFPNFEQGVA CLREIAKQRC APASIRLMDN QQFQFGHALK
     PQVSSIFTSF LDGLKKFYIT KFKGFDPNQI SVATLLFEGD REKVLQHEKQ VYDIAAKFGG
     LAAGEDNGQR GYLLTYVIAY IRDLGLEYYV IGESFETSAP WDRVIDLCRN VKERIRRECK
     ERGVQFAPLS TCRVTQTYDA GACIYFYFAF NYRGISDPLT VFEHTEAAAR EEILANGGSL
     SHHHGVGKIR KQWLKESISD VGFGMLKSVK EYVDPSNIFG NRNLL
//
ID   EPC2_MOUSE              Reviewed;         808 AA.
AC   Q8C0I4; A2AQU9; Q3URX9; Q80Y70; Q8BXC5;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 2.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Enhancer of polycomb homolog 2;
DE   AltName: Full=EPC-like;
GN   Name=Epc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 82-808.
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in transcription or DNA repair (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the enhancer of polycomb family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC33197.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK031025; BAC27218.1; -; mRNA.
DR   EMBL; AK047947; BAC33197.1; ALT_INIT; mRNA.
DR   EMBL; AK141073; BAE24558.1; -; mRNA.
DR   EMBL; AL845163; CAM19640.1; -; Genomic_DNA.
DR   EMBL; BC048785; AAH48785.1; -; mRNA.
DR   IPI; IPI00223821; -.
DR   RefSeq; NP_766251.3; NM_172663.4.
DR   UniGene; Mm.29167; -.
DR   STRING; Q8C0I4; -.
DR   PhosphoSite; Q8C0I4; -.
DR   PRIDE; Q8C0I4; -.
DR   Ensembl; ENSMUST00000092123; ENSMUSP00000089758; ENSMUSG00000069495.
DR   GeneID; 227867; -.
DR   KEGG; mmu:227867; -.
DR   NMPDR; fig|10090.3.peg.5956; -.
DR   UCSC; uc008jpw.2; mouse.
DR   CTD; 227867; -.
DR   MGI; MGI:1278321; Epc2.
DR   GeneTree; ENSGT00390000013262; -.
DR   HOGENOM; HBG355238; -.
DR   HOVERGEN; HBG051489; -.
DR   InParanoid; Q8C0I4; -.
DR   OMA; PEMLNSF; -.
DR   OrthoDB; EOG44XJG9; -.
DR   NextBio; 378848; -.
DR   ArrayExpress; Q8C0I4; -.
DR   Bgee; Q8C0I4; -.
DR   CleanEx; MM_EPC2; -.
DR   Genevestigator; Q8C0I4; -.
DR   GermOnline; ENSMUSG00000069495; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR009607; E_Pc_C.
DR   InterPro; IPR019542; Enhancer_of_polycomb-like_N.
DR   Pfam; PF06752; E_Pc_C; 1.
DR   Pfam; PF10513; EPL1; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; DNA damage; DNA repair; Nucleus; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    808       Enhancer of polycomb homolog 2.
FT                                /FTId=PRO_0000239296.
FT   COMPBIAS    486    489       Poly-Ser.
FT   COMPBIAS    583    620       Gln-rich.
FT   CONFLICT      5      5       S -> A (in Ref. 1; BAC33197).
FT   CONFLICT    260    260       E -> K (in Ref. 1; BAE24558).
FT   CONFLICT    382    382       L -> P (in Ref. 3; AAH48785).
FT   CONFLICT    451    451       A -> V (in Ref. 1; BAC27218).
SQ   SEQUENCE   808 AA;  90960 MW;  F1DAAC73786B349B CRC64;
     MSKLSFRARA LDAAKPLPIY RGKDMPDLND CVSINRAVPQ MPTGMEKEEE SEHHLQRAIS
     AQQVFREKKE SMVIPVPEAE SNVNYYNRLY KGEFKQPKQF IHIQPFNLDN EQPDYDMDSE
     DETLLNRLNR KMEIKPLQFE IMIDRLEKAS SNQLVTLQEA KLLLNEDDYL IKAVYDYWVR
     KRKNCRGPSL IPQIKQEKRD GSTNNDPYVA FRRRTEKMQT RKNRKNDEAS YEKMLKLRRE
     FSRAITILEM IKRREKTKRE LLHLTLEVVE KRYHLGDYGG EILNEVKVNR SEKELYASPA
     TLHNGNHHKV QECKTKHPHH LSLKEEASDV VRQKKKYPKK PKAEAGIAPQ QPTPETLPVI
     NKSDIKQYDF QSSDEDEFPQ VLSPASEAEE ENDPDGSCAF RRRAGCQYYA PRLDQANNHM
     CENSELADLD KLRYKHCLTT LTVPRRCIGF ARRRIGRGGR VIMDRISTEH DPVLKQIDPE
     MLNGFSSSSQ TIDFSSNFSR TNASSKPCEN RLSLSEILSN IRSCRLQCFQ PRLLNVQDID
     SEECTSRKPG QTVSSKRVSA ASVALLNTSK NGISVTGGIT EEQFQTHQQQ LVQMQRQQLA
     QLHQKQQSQH SSQQTHPKAQ GSSTSDCMSK TLDSASAHFA ASAVVSAPVP SRSEGSKEQN
     TGHNNMNGVV QPSGPSKTLY STNMALSSSP GISAVQLVRT VGHTTTNHLI PALCTSSPQT
     LPMNNSCLTN AVHLNNVSVV SPVNVHINTR TSAPSPTALK LATVAASMDR VPKVTPSSAI
     SSIARENHEP ERLGLNGLAE TTVAMEVT
//
ID   ANR57_MOUSE             Reviewed;         512 AA.
AC   Q8C0J6; Q8BWN1;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Ankyrin repeat domain-containing protein 57;
GN   Name=Ankrd57;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pancreas, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SIMILARITY: Contains 2 ANK repeats.
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DR   EMBL; AK030944; BAC27191.1; -; mRNA.
DR   EMBL; AK050497; BAC34291.1; -; mRNA.
DR   IPI; IPI00223838; -.
DR   RefSeq; NP_766527.3; NM_172939.3.
DR   UniGene; Mm.3036; -.
DR   ProteinModelPortal; Q8C0J6; -.
DR   SMR; Q8C0J6; 254-446.
DR   PhosphoSite; Q8C0J6; -.
DR   PRIDE; Q8C0J6; -.
DR   Ensembl; ENSMUST00000095658; ENSMUSP00000093319; ENSMUSG00000071286.
DR   GeneID; 268301; -.
DR   KEGG; mmu:268301; -.
DR   CTD; 268301; -.
DR   MGI; MGI:3606051; Ankrd57.
DR   eggNOG; roNOG08979; -.
DR   GeneTree; ENSGT00530000063547; -.
DR   HOGENOM; HBG715074; -.
DR   HOVERGEN; HBG079715; -.
DR   InParanoid; Q8C0J6; -.
DR   OMA; MGSSPQL; -.
DR   OrthoDB; EOG41C6WC; -.
DR   PhylomeDB; Q8C0J6; -.
DR   NextBio; 392235; -.
DR   ArrayExpress; Q8C0J6; -.
DR   Bgee; Q8C0J6; -.
DR   CleanEx; MM_ANKRD57; -.
DR   Genevestigator; Q8C0J6; -.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 1.
DR   SMART; SM00248; ANK; 2.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
PE   2: Evidence at transcript level;
KW   ANK repeat; Phosphoprotein; Repeat.
FT   CHAIN         1    512       Ankyrin repeat domain-containing protein
FT                                57.
FT                                /FTId=PRO_0000274341.
FT   REPEAT      288    317       ANK 1.
FT   REPEAT      327    357       ANK 2.
FT   COMPBIAS    481    492       Poly-Glu.
FT   MOD_RES     205    205       Phosphoserine (By similarity).
FT   MOD_RES     500    500       Phosphoserine (By similarity).
FT   CONFLICT     55     60       NAVATV -> MPWPPL (in Ref. 1; BAC34291).
FT   CONFLICT    119    119       E -> Q (in Ref. 1; BAC34291).
FT   CONFLICT    123    123       Q -> K (in Ref. 1; BAC34291).
FT   CONFLICT    167    167       S -> T (in Ref. 1; BAC34291).
FT   CONFLICT    330    330       T -> S (in Ref. 1; BAC27191).
SQ   SEQUENCE   512 AA;  54938 MW;  AA4B1D706B1607F8 CRC64;
     MEGSLELSSE AILRFLAERG GRAGHSELVQ HFRDVLGGQR EQRTRARERF KELVNAVATV
     RTDPADGTKY VHLKKRFCTG DSPPLEAKLP REPPRIEVTE EPQVPDLAAE PCEGSQLQEA
     NPQLSLGLGG EVSDQEPPAP AQGGAQGKDS PPQEVEAVSW ASGPGSSENL KLPPQGEAEG
     GSSPSGPNTP RSARQNFRDL VLGSSPQLKR SVGPGDGNAG GRSRGGGDSD TASLASSSAE
     EESSVGASVT LDPLDHAWML SASEGKWDSL EGLLTCEPGL LSKRDFITGF TCLHWAAKHG
     RQELLAMLVN FATKHQLPVN INAKSSGGYT ALHLAAMHGH VEVVKLLVGA YDADVDIRDY
     SGRKASQYLS ESIAEEIKNL VGALDEDDGD SPAARGGGRW RLSKVLPSHI THKLSPVVED
     GAELHHHVPE GWTGGSKAKD SGRKASGSSS GRMKPRLNKI RFRTQIIHTT PSFRDAKPTL
     EEGEEEEEEE EERSLRGYSS SFKLRPKSNV FG
//
ID   TMX4_MOUSE              Reviewed;         335 AA.
AC   Q8C0L0; Q3UHC6; Q6ZPW7; Q80X49;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 2.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Thioredoxin-related transmembrane protein 4;
DE   AltName: Full=Thioredoxin domain-containing protein 13;
DE   Flags: Precursor;
GN   Name=Tmx4; Synonyms=D2Bwg1356e, Kiaa1162, Txndc13;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247 AND SER-255, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH50918.1; Type=Erroneous initiation;
CC       Sequence=BAC98111.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK030696; BAC27085.1; -; mRNA.
DR   EMBL; AK129301; BAC98111.1; ALT_INIT; mRNA.
DR   EMBL; AK147465; BAE27931.1; -; mRNA.
DR   EMBL; BC050918; AAH50918.1; ALT_INIT; mRNA.
DR   IPI; IPI00453829; -.
DR   RefSeq; NP_083424.1; NM_029148.1.
DR   UniGene; Mm.264096; -.
DR   ProteinModelPortal; Q8C0L0; -.
DR   SMR; Q8C0L0; 30-150.
DR   PhosphoSite; Q8C0L0; -.
DR   PRIDE; Q8C0L0; -.
DR   Ensembl; ENSMUST00000038228; ENSMUSP00000045154; ENSMUSG00000034723.
DR   GeneID; 52837; -.
DR   KEGG; mmu:52837; -.
DR   UCSC; uc008mnt.1; mouse.
DR   CTD; 52837; -.
DR   MGI; MGI:106558; Tmx4.
DR   GeneTree; ENSGT00390000011580; -.
DR   HOGENOM; HBG126019; -.
DR   InParanoid; Q8C0L0; -.
DR   OMA; GIYEDLQ; -.
DR   OrthoDB; EOG48KRC3; -.
DR   NextBio; 309603; -.
DR   ArrayExpress; Q8C0L0; -.
DR   Bgee; Q8C0L0; -.
DR   CleanEx; MM_TXNDC13; -.
DR   Genevestigator; Q8C0L0; -.
DR   GermOnline; ENSMUSG00000034723; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR017936; Thioredoxin-like.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Electron transport; Membrane; Phosphoprotein;
KW   Redox-active center; Signal; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21    335       Thioredoxin-related transmembrane protein
FT                                4.
FT                                /FTId=PRO_0000034192.
FT   TRANSMEM    186    206       Helical; (Potential).
FT   DOMAIN       26    133       Thioredoxin.
FT   COMPBIAS    220    288       Glu-rich.
FT   MOD_RES     247    247       Phosphoserine.
FT   MOD_RES     255    255       Phosphoserine.
FT   DISULFID     60     63       Redox-active (Potential).
FT   CONFLICT     22     22       G -> S (in Ref. 1; BAC27085).
SQ   SEQUENCE   335 AA;  37131 MW;  526E4E6F894737D2 CRC64;
     MTGGFCVPVL LAAWLAAAAA EGLEQAALPA EESRVQPMTA SNWTLVMEGE WMLKFYAPWC
     PSCQQTDSEW ETFAKNGETL QISVGKVDVI QEPGLSGRFF VTTLPAFFHA KDGIFRRYRG
     PGIYEDLQNY ILEKKWQSVE PLTGWKSPAS LTMSGMAGLF SISGKIWHLH NYFTVTLGIP
     AWCSYVFFVI ATLVFGLFMG LILVVISECF CVPLPRASSE RCEQEQSTGE AQGAEQLQDA
     EEEKDDSNEE ENKDSLVDDE EEKEDIGDED EGEEDEEEDN LAGIMAEERS DTNERAVVKE
     GSVSPKEDGA HPADTQDVVE DALRQRKSQN ANKGS
//
ID   GPCP1_MOUSE             Reviewed;         675 AA.
AC   Q8C0L9; A2AMD5; Q3TLV6; Q80TD5; Q8BKJ7; Q8BKW7; Q8CFW2; Q9D759;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Putative glycerophosphocholine phosphodiesterase GPCPD1;
DE            EC=3.1.-.-;
DE   AltName: Full=Glycerophosphodiester phosphodiesterase 5;
DE   AltName: Full=Preimplantation protein 4;
GN   Name=Gpcpd1; Synonyms=Gde5, Kiaa1434, Prei4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryo, Embryonic spinal ganglion, Head, Mammary gland, and
RC   Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-611, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8C0L9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C0L9-2; Sequence=VSP_020820;
CC       Name=3;
CC         IsoId=Q8C0L9-3; Sequence=VSP_020819;
CC   -!- SIMILARITY: Belongs to the glycerophosphoryl diester
CC       phosphodiesterase family.
CC   -!- SIMILARITY: Contains 1 CBM20 (carbohydrate binding type-20)
CC       domain.
CC   -!- SIMILARITY: Contains 1 GDPD domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB26361.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC       Sequence=BAC33775.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAC34739.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAC65792.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK122510; BAC65792.1; ALT_INIT; mRNA.
DR   EMBL; AK009563; BAB26361.2; ALT_INIT; mRNA.
DR   EMBL; AK030645; BAC27063.1; -; mRNA.
DR   EMBL; AK049491; BAC33775.1; ALT_INIT; mRNA.
DR   EMBL; AK051728; BAC34739.1; ALT_INIT; mRNA.
DR   EMBL; AK166293; BAE38686.1; -; mRNA.
DR   EMBL; AL807386; CAM17016.1; -; Genomic_DNA.
DR   EMBL; BC033408; AAH33408.1; -; mRNA.
DR   IPI; IPI00177225; -.
DR   IPI; IPI00223864; -.
DR   IPI; IPI00752034; -.
DR   RefSeq; NP_001036136.1; NM_001042671.1.
DR   RefSeq; NP_083078.3; NM_028802.2.
DR   UniGene; Mm.211211; -.
DR   UniGene; Mm.448334; -.
DR   ProteinModelPortal; Q8C0L9; -.
DR   SMR; Q8C0L9; 3-115, 319-619.
DR   CAZy; CBM20; Carbohydrate-Binding Module Family 20.
DR   PhosphoSite; Q8C0L9; -.
DR   PRIDE; Q8C0L9; -.
DR   Ensembl; ENSMUST00000060955; ENSMUSP00000062221; ENSMUSG00000027346.
DR   Ensembl; ENSMUST00000110142; ENSMUSP00000105769; ENSMUSG00000027346.
DR   GeneID; 74182; -.
DR   KEGG; mmu:74182; -.
DR   UCSC; uc008mmv.1; mouse.
DR   UCSC; uc008mmx.1; mouse.
DR   CTD; 74182; -.
DR   MGI; MGI:104898; Gpcpd1.
DR   GeneTree; ENSGT00440000033970; -.
DR   HOVERGEN; HBG080384; -.
DR   InParanoid; Q8C0L9; -.
DR   OMA; KQNKYPV; -.
DR   OrthoDB; EOG47H5PP; -.
DR   PhylomeDB; Q8C0L9; -.
DR   NextBio; 340014; -.
DR   ArrayExpress; Q8C0L9; -.
DR   Bgee; Q8C0L9; -.
DR   CleanEx; MM_PREI4; -.
DR   Genevestigator; Q8C0L9; -.
DR   GermOnline; ENSMUSG00000027346; Mus musculus.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IEA:InterPro.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR004129; GlyceroP-diester-Pdiesterase.
DR   InterPro; IPR002044; Glyco_hydro_carb-bd.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Gene3D; G3DSA:3.20.20.190; PLC-like_Pdiesterase_TIM-brl; 1.
DR   Pfam; PF00686; CBM_20; 1.
DR   Pfam; PF03009; GDPD; 1.
DR   SUPFAM; SSF49452; CBD_4; 1.
DR   SUPFAM; SSF51695; PLC-like_Pdiesterase_TIM-brl; 1.
DR   PROSITE; PS51166; CBM20; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; Phosphoprotein.
FT   CHAIN         1    675       Putative glycerophosphocholine
FT                                phosphodiesterase GPCPD1.
FT                                /FTId=PRO_0000251947.
FT   DOMAIN        1    115       CBM20.
FT   DOMAIN      326    616       GDPD.
FT   REGION       88     89       Substrate binding (Potential).
FT   COMPBIAS    169    175       Poly-Asp.
FT   BINDING      70     70       Substrate (Potential).
FT   MOD_RES     611    611       Phosphotyrosine.
FT   VAR_SEQ       1    445       Missing (in isoform 3).
FT                                /FTId=VSP_020819.
FT   VAR_SEQ       1    184       Missing (in isoform 2).
FT                                /FTId=VSP_020820.
FT   CONFLICT    289    289       G -> D (in Ref. 2; BAE38686).
FT   CONFLICT    460    460       E -> Q (in Ref. 2; BAC33775).
FT   CONFLICT    494    495       LE -> SQ (in Ref. 2; BAC33775).
FT   CONFLICT    499    499       K -> N (in Ref. 2; BAC33775).
FT   CONFLICT    559    559       L -> S (in Ref. 2; BAB26361).
FT   CONFLICT    602    602       K -> E (in Ref. 2; BAB26361).
SQ   SEQUENCE   675 AA;  76579 MW;  7ABF9EE48CF39B47 CRC64;
     MTPSQVTFEI RGTLLPGEVF AICGSCDALG NWNPQNAVAL INENETGDSV LWKAVIALNR
     GVSVKYRYFR GCFLEPKTIG GPCQVIVHKW ETHLQPRSIT PLESEIIIDD GQFGIHNGVE
     TLDSGWLTCQ TEIRLRLHFS EKPPVSISKK KFKKSRFRVK LTLEGLEEDE DDDDDKVSPT
     VLHKMSNSLE ISLISDNEFK CRHSQPECGY GLQPDRWTEY SIQTMEPDNL ELIFDFFEED
     LSEHVVQGDV LPGHVGTACL LSSTIAESGR SAGILTLPIM SRNSRKTIGK VRVDFIIIKP
     LPGYSCSMQS SFSKYWKPRI PLDVGHRGAG NSTTTAKLAK VQENTIASLR NAASHGAAFV
     EFDVHLSKDF VPVVYHDLTC CLTMKRKYEA DPVELFEIPV KELTFDQLQL LKLSHVTALK
     TKDRKQSLYE EENFFSENQP FPSLKMVLES LPENVGFNIE IKWICQHRDG VWDGNLSTYF
     DMNVFLDIIL KTVLENSGKR RIVFSSFDAD ICTMVRQKQN KYPILFLTQG KSDIYPELMD
     LRSRTTPIAM SFAQFENILG INAHTEDLLR NPSYVQEAKA KGLVIFCWGD DTNDPENRRK
     LKEFGVNGLI YDRIYDWMPE QPNIFQVEQL ERLKQELPEL KNCLCPTVSH FIPSSFCVEP
     DIHVDANGID SVENA
//
ID   WDR59_MOUSE             Reviewed;         992 AA.
AC   Q8C0M0; Q3TC49; Q3UWJ3; Q69Z65; Q6NZK7; Q8BLZ2; Q8BWK9;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=WD repeat-containing protein 59;
DE   AltName: Full=CUL4- and DDB1-associated WDR protein 12;
GN   Name=Wdr59; Synonyms=Cdw12, Kiaa1923;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH CUL4.
RX   PubMed=17041588; DOI=10.1038/ncb1490;
RA   Higa L.A., Wu M., Ye T., Kobayashi R., Sun H., Zhang H.;
RT   "CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat
RT   proteins and regulates histone methylation.";
RL   Nat. Cell Biol. 8:1277-1283(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Aorta, Head, Heart, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-839, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBUNIT: Interacts with DDB1-CUL4A/B E3 ligase complexes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8C0M0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C0M0-2; Sequence=VSP_023886;
CC       Name=3;
CC         IsoId=Q8C0M0-3; Sequence=VSP_023885, VSP_023886;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 RWD domain.
CC   -!- SIMILARITY: Contains 8 WD repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC30708.1; Type=Erroneous initiation;
CC       Sequence=BAD32579.1; Type=Erroneous initiation;
CC       Sequence=BAE42108.1; Type=Erroneous termination; Positions=241; Note=Translated as Arg;
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CC   -----------------------------------------------------------------------
DR   EMBL; EF011622; ABK41112.1; -; mRNA.
DR   EMBL; AK173301; BAD32579.1; ALT_INIT; mRNA.
DR   EMBL; AK030644; BAC27062.1; -; mRNA.
DR   EMBL; AK040807; BAC30708.1; ALT_INIT; mRNA.
DR   EMBL; AK052262; BAC34902.1; -; mRNA.
DR   EMBL; AK136303; BAE22922.1; -; mRNA.
DR   EMBL; AK170910; BAE42108.1; ALT_SEQ; mRNA.
DR   EMBL; BC066082; AAH66082.1; -; mRNA.
DR   IPI; IPI00263940; -.
DR   IPI; IPI00469939; -.
DR   IPI; IPI00955111; -.
DR   RefSeq; NP_001164213.1; NM_001170742.1.
DR   RefSeq; NP_001164214.1; NM_001170743.1.
DR   RefSeq; NP_795897.2; NM_176923.4.
DR   UniGene; Mm.247294; -.
DR   ProteinModelPortal; Q8C0M0; -.
DR   SMR; Q8C0M0; 49-319, 940-986.
DR   PhosphoSite; Q8C0M0; -.
DR   PRIDE; Q8C0M0; -.
DR   Ensembl; ENSMUST00000038193; ENSMUSP00000043671; ENSMUSG00000031959.
DR   Ensembl; ENSMUST00000109151; ENSMUSP00000104779; ENSMUSG00000031959.
DR   GeneID; 319481; -.
DR   KEGG; mmu:319481; -.
DR   UCSC; uc009nmh.1; mouse.
DR   CTD; 319481; -.
DR   MGI; MGI:2442115; Wdr59.
DR   eggNOG; roNOG13821; -.
DR   GeneTree; ENSGT00600000084510; -.
DR   HOVERGEN; HBG092820; -.
DR   OMA; QGHTRVI; -.
DR   PhylomeDB; Q8C0M0; -.
DR   NextBio; 394820; -.
DR   ArrayExpress; Q8C0M0; -.
DR   Bgee; Q8C0M0; -.
DR   CleanEx; MM_WDR59; -.
DR   Genevestigator; Q8C0M0; -.
DR   InterPro; IPR006575; RWD-domain.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM00591; RWD; 1.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS50908; RWD; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein; Repeat; WD repeat.
FT   CHAIN         1    992       WD repeat-containing protein 59.
FT                                /FTId=PRO_0000280722.
FT   REPEAT       57     98       WD 1.
FT   REPEAT      103    143       WD 2.
FT   REPEAT      146    185       WD 3.
FT   REPEAT      189    229       WD 4.
FT   REPEAT      232    276       WD 5.
FT   REPEAT      278    318       WD 6.
FT   REPEAT      319    362       WD 7.
FT   DOMAIN      393    494       RWD.
FT   REPEAT      660    706       WD 8.
FT   MOD_RES     564    564       Phosphoserine (By similarity).
FT   MOD_RES     839    839       Phosphoserine.
FT   MOD_RES     840    840       Phosphoserine (By similarity).
FT   MOD_RES     848    848       Phosphoserine (By similarity).
FT   VAR_SEQ     622    622       R -> RMSPRSARRRWSIQAINDFP (in isoform 3).
FT                                /FTId=VSP_023885.
FT   VAR_SEQ     733    750       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_023886.
FT   CONFLICT    154    154       V -> A (in Ref. 3; BAC27062).
FT   CONFLICT    355    355       D -> G (in Ref. 3; BAC27062).
FT   CONFLICT    499    499       D -> E (in Ref. 3; BAE22922).
FT   CONFLICT    825    825       Missing (in Ref. 3; BAC27062).
FT   CONFLICT    961    961       H -> L (in Ref. 3; BAC34902).
SQ   SEQUENCE   992 AA;  111726 MW;  FA85E469CE518AFA CRC64;
     MAARWSSENV VVEFRDSQAT AMSVDCLGQH AVLSGRRFLY IVNLDAPFEG HRKISRQSKW
     DIGAVQWNPH DSFAHYFAAS SNQRVDLYKW KDGSGEVGTT LQGHTRVISD LDWAVFEPDL
     LVTSSVDTYI YIWDIKDTRK PTVALSAVAG ASQVKWNKKN ANYLATSHDG DVRIWDKRKP
     STAVEYLAAH LSKIHGLDWH PDSEHIFATS SQDNSVKFWD YRQPRKYLNI LPCQVPVWKA
     RYTPFSNGLV TVMVPQLRRE NSLLLWNASD LNAPVHTFVG HDDVVLEFQW RRQKEGSKDY
     QLVTWSRDQT LRMWRVDYQM QRLCANDILD GVDEFIESIS LLPEPEKTPH PQDIDHQPSL
     SHGEEDAIKE DPPSSLLEEK RSDQLGLPQT LQQEFSLINV QIRNVNVEMD AADRSCTVSV
     HCSNHRVKML VTFPAQYPNN AAPSFQFINP TTITSAVKAK LLKILKDTSL QKVKRNQSCL
     EPCLRQLVSC LESFVNQEDS ASSNPFALQN SVTPPLPTFA RVTTAYGSYQ DANIPFPRTS
     GARFCGAGYL VYFTRPMTMH RAVSPTEPTP RSLSALSAYH TGLIAPMKIR TEAPGNLRLY
     SGSPTRSEKE QVSISSFYYK ERKSRRWKSK REGSDSGNRP IKAAGKVIIQ DVSCLLPVHK
     SLGELYILNV NDTQETCQKN ATSAMLVGRK DLVQVWSLAT VATDLCLGPK SDPDLETPWA
     RHPFGRQLLE SLWGDRESTR VCGPPLSGAR LAHYCQLRDV QTLAMLCSVF EAQSRPQGLP
     NPFGPFPNRS SNLVVSHSRY PSFTSSGSCS SMSDPGFNTG GWNIAGRETE HISSPWGESS
     PEELRFGSLT YSDPRERERD QHDKNKRLLD PANTQQFDDF KKCYGEILYR WGLREKRAEV
     LKFVSCPPDP HKGIEFGVYC SHCRSEVRGT QCAICKGFTF QCAICHVAVR GSSNFCLTCG
     HGGHTSHMME WFRTQEVCPT GCGCHCLLES TF
//
ID   GPAT3_MOUSE             Reviewed;         438 AA.
AC   Q8C0N2; A6H5X0;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase 3;
DE            Short=GPAT-3;
DE            EC=2.3.1.15;
DE   AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 9;
DE            Short=1-AGP acyltransferase 9;
DE            Short=1-AGPAT 9;
DE   AltName: Full=Acyl-CoA:glycerol-3-phosphate acyltransferase 3;
DE            Short=mGPAT3;
DE   AltName: Full=Lysophosphatidic acid acyltransferase theta;
DE            Short=LPAAT-theta;
GN   Name=Agpat9; Synonyms=Gpat3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CD-1; TISSUE=Brain, Neural stem cell, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=17170135; DOI=10.1073/pnas.0609140103;
RA   Cao J., Li J.-L., Li D., Tobin J.F., Gimeno R.E.;
RT   "Molecular identification of microsomal acyl-CoA:glycerol-3-phosphate
RT   acyltransferase, a key enzyme in de novo triacylglycerol synthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:19695-19700(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position
CC       of glycerol-3-phosphate, an essential step in glycerolipid
CC       biosynthesis.
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-
CC       acyl-sn-glycerol 3-phosphate.
CC   -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CC       CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
CC   -!- TISSUE SPECIFICITY: Most abundant in epididymal fat, followed by
CC       small intestine, brown adipose tissue, kidney, heart and colon.
CC   -!- INDUCTION: During adipocyte differentiation.
CC   -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity
CC       and may constitute the binding site for the phosphate moiety of
CC       the glycerol-3-phosphate (By similarity).
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family.
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DR   EMBL; AK030171; BAC26820.1; -; mRNA.
DR   EMBL; AK160261; BAE35719.1; -; mRNA.
DR   EMBL; AK138410; BAE23647.1; -; mRNA.
DR   EMBL; BC096769; AAH96769.1; -; mRNA.
DR   EMBL; BC138228; AAI38229.1; -; mRNA.
DR   EMBL; BC145669; AAI45670.1; -; mRNA.
DR   IPI; IPI00223880; -.
DR   RefSeq; NP_766303.1; NM_172715.3.
DR   UniGene; Mm.271911; -.
DR   ProteinModelPortal; Q8C0N2; -.
DR   STRING; Q8C0N2; -.
DR   PhosphoSite; Q8C0N2; -.
DR   PRIDE; Q8C0N2; -.
DR   Ensembl; ENSMUST00000031255; ENSMUSP00000031255; ENSMUSG00000029314.
DR   Ensembl; ENSMUST00000092990; ENSMUSP00000090667; ENSMUSG00000029314.
DR   Ensembl; ENSMUST00000112887; ENSMUSP00000108508; ENSMUSG00000029314.
DR   GeneID; 231510; -.
DR   KEGG; mmu:231510; -.
DR   UCSC; uc008yih.1; mouse.
DR   CTD; 231510; -.
DR   MGI; MGI:3603816; Agpat9.
DR   eggNOG; roNOG12959; -.
DR   GeneTree; ENSGT00390000000536; -.
DR   HOGENOM; HBG408354; -.
DR   InParanoid; Q8C0N2; -.
DR   OMA; KPQKGGI; -.
DR   OrthoDB; EOG4Z62NH; -.
DR   PhylomeDB; Q8C0N2; -.
DR   BRENDA; 2.3.1.51; 244.
DR   NextBio; 380592; -.
DR   ArrayExpress; Q8C0N2; -.
DR   Bgee; Q8C0N2; -.
DR   CleanEx; MM_AGPAT9; -.
DR   Genevestigator; Q8C0N2; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; IDA:UniProtKB.
DR   InterPro; IPR002123; Acyltransferase.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Endoplasmic reticulum; Membrane;
KW   Phospholipid biosynthesis; Phosphoprotein; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    438       Glycerol-3-phosphate acyltransferase 3.
FT                                /FTId=PRO_0000291571.
FT   TRANSMEM     14     34       Helical; (Potential).
FT   TRANSMEM    137    157       Helical; (Potential).
FT   TRANSMEM    161    181       Helical; (Potential).
FT   MOTIF       229    234       HXXXXD motif.
FT   MOD_RES      68     68       Phosphoserine.
FT   MOD_RES      77     77       Phosphoserine (By similarity).
SQ   SEQUENCE   438 AA;  49000 MW;  29B4ED7405DCC8BD CRC64;
     MEGADLAVKL LSTWLTLVGG LILLPSAFGL SLGISEIYMK ILVKTLEWAT LRIQKGAPKE
     SALKNSASVG IIQRDESPME KGLSGLRGRD FELSDVFYFS KKGLEAIVED EVTQRFSSEE
     LVSWNLLTRT NVNFQYISPR LTMVWVLGVL VRYCFLLPLR VTLAFIGISL LIIGTTLVGQ
     LPDSSLKNWL SELVHLTCCR ICVRSLSGTI HYHNKQYRPQ KGGICVANHT SPIDVLILAT
     DGCYAMVGQV HGGLMGIIQR AMVKACPHVW FERSEIKDRH LVTKRLKEHI ADKKKLPILI
     FPEGTCINNT SVMMFKKGSF EIGGTIYPVA IKYNPQFGDA FWNSSKYNLV SYLLRIMTSW
     AIVCDVWYMP PMTREEGEDA VQFANRVKSA IAVQGGLTEL PWDGGLKRAK VKDTFKEEQQ
     KNYSKMIVGN GSPNLARD
//
ID   SI1L1_MOUSE             Reviewed;        1782 AA.
AC   Q8C0T5; Q6PDI8; Q80U02; Q8C026;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Signal-induced proliferation-associated 1-like protein 1;
DE            Short=SIPA1-like protein 1;
GN   Name=Sipa1l1; Synonyms=Kiaa0440;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 18-28; 1379-1408 AND 1468-1482, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 273-1782 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1528, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1528, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1528 AND SER-1547, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1507, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1507, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1528, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Stimulates the GTPase activity of RAP2A. Promotes
CC       reorganization of the actin cytoskeleton and recruits DLG4 to F-
CC       actin. Contributes to the regulation of dendritic spine
CC       morphogenesis (By similarity).
CC   -!- SUBUNIT: Interacts with DLG4, PDLIM5, PDLIM7 and PROSAPIP1.
CC       Interacts with the actin cytoskeleton (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Cell junction, synapse, postsynaptic cell membrane, postsynaptic
CC       density (By similarity). Cell junction, synapse, synaptosome (By
CC       similarity). Note=Associated with the actin cytoskeleton. Detected
CC       at synapses and dendritic spines of cultured hippocampal neurons
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=E6TP1 alpha;
CC         IsoId=Q8C0T5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C0T5-2; Sequence=VSP_010918, VSP_010919;
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 Rap-GAP domain.
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DR   EMBL; AK029889; BAC26660.1; -; mRNA.
DR   EMBL; AK032493; BAC27896.1; -; mRNA.
DR   EMBL; BC058681; AAH58681.1; -; mRNA.
DR   EMBL; AK122284; BAC65566.1; -; mRNA.
DR   IPI; IPI00453688; -.
DR   IPI; IPI00453689; -.
DR   RefSeq; NP_001161455.1; NM_001167983.1.
DR   RefSeq; NP_766167.2; NM_172579.3.
DR   UniGene; Mm.261333; -.
DR   ProteinModelPortal; Q8C0T5; -.
DR   SMR; Q8C0T5; 479-824, 957-1027.
DR   PhosphoSite; Q8C0T5; -.
DR   PRIDE; Q8C0T5; -.
DR   Ensembl; ENSMUST00000047967; ENSMUSP00000037886; ENSMUSG00000042700.
DR   Ensembl; ENSMUST00000053969; ENSMUSP00000061014; ENSMUSG00000042700.
DR   Ensembl; ENSMUST00000110321; ENSMUSP00000105950; ENSMUSG00000042700.
DR   GeneID; 217692; -.
DR   KEGG; mmu:217692; -.
DR   UCSC; uc007ocu.1; mouse.
DR   UCSC; uc007ocw.1; mouse.
DR   CTD; 217692; -.
DR   MGI; MGI:2443679; Sipa1l1.
DR   GeneTree; ENSGT00550000074284; -.
DR   HOGENOM; HBG445166; -.
DR   HOVERGEN; HBG056135; -.
DR   InParanoid; Q8C0T5; -.
DR   OMA; IETSSCL; -.
DR   OrthoDB; EOG4XGZZ6; -.
DR   PhylomeDB; Q8C0T5; -.
DR   NextBio; 375960; -.
DR   ArrayExpress; Q8C0T5; -.
DR   Bgee; Q8C0T5; -.
DR   CleanEx; MM_SIPA1L1; -.
DR   Genevestigator; Q8C0T5; -.
DR   GermOnline; ENSMUSG00000042700; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR   GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019717; C:synaptosome; ISS:UniProtKB.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR   GO; GO:0032861; P:activation of Rap GTPase activity; ISS:UniProtKB.
DR   GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR   InterPro; IPR021818; DUF3401.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR000331; Rap_GAP.
DR   Pfam; PF11881; DUF3401; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF02145; Rap_GAP; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50085; RAPGAP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; GTPase activation;
KW   Membrane; Phosphoprotein; Postsynaptic cell membrane; Synapse;
KW   Synaptosome.
FT   CHAIN         1   1782       Signal-induced proliferation-associated
FT                                1-like protein 1.
FT                                /FTId=PRO_0000056747.
FT   DOMAIN      599    816       Rap-GAP.
FT   DOMAIN      953   1031       PDZ.
FT   COILED     1713   1773       Potential.
FT   COMPBIAS     93    129       Ser-rich.
FT   COMPBIAS   1114   1447       Ser-rich.
FT   COMPBIAS   1438   1447       Poly-Ser.
FT   MOD_RES     161    161       Phosphoserine (By similarity).
FT   MOD_RES     162    162       Phosphoserine (By similarity).
FT   MOD_RES     288    288       Phosphoserine (By similarity).
FT   MOD_RES    1234   1234       Phosphoserine (By similarity).
FT   MOD_RES    1236   1236       Phosphoserine (By similarity).
FT   MOD_RES    1249   1249       Phosphoserine (By similarity).
FT   MOD_RES    1412   1412       Phosphoserine (By similarity).
FT   MOD_RES    1507   1507       Phosphoserine.
FT   MOD_RES    1528   1528       Phosphoserine.
FT   MOD_RES    1530   1530       Phosphothreonine (By similarity).
FT   MOD_RES    1547   1547       Phosphoserine.
FT   MOD_RES    1562   1562       Phosphothreonine (By similarity).
FT   MOD_RES    1564   1564       Phosphoserine (By similarity).
FT   MOD_RES    1626   1626       Phosphoserine (By similarity).
FT   MOD_RES    1629   1629       Phosphoserine (By similarity).
FT   MOD_RES    1706   1706       Phosphotyrosine (By similarity).
FT   MOD_RES    1708   1708       Phosphoserine (By similarity).
FT   VAR_SEQ    1736   1751       EKEDKAQLQAEVEHLR -> VNALRKRRQGPAAGGS (in
FT                                isoform 2).
FT                                /FTId=VSP_010918.
FT   VAR_SEQ    1752   1782       Missing (in isoform 2).
FT                                /FTId=VSP_010919.
FT   CONFLICT    855    855       S -> N (in Ref. 1; BAC26660).
FT   CONFLICT   1204   1204       W -> C (in Ref. 1; BAC65566).
SQ   SEQUENCE   1782 AA;  197031 MW;  A5BBD8CD69A481FC CRC64;
     MTSLKRSQTE RPVTADRASV VSTDGAPKVH TDDFYMRRFR SQNGSLGSSV MAAVGPPRSE
     GPHHITSTPG VPKMGVRARI ADWPPRKENV KESSRSSQEI ETSSCLESLS SKGSPVSQGS
     SVSLNSNDSA MLKSIQNTLK NKTGPAESMD SRFLMPEAYP SSPRKALRRI RQRSNSDITI
     SELDVDSFDE CISPTYKSGP SLHREYGSTS SIDKQGTSGD SFFDLLKGYK DDRSDRGPTP
     TKLSDFLITG GGKGSGFSLD VIDGPISQRE NLRLFKEREK PLKRRSKSET GDSSIFRKLR
     NAKGEELGKS SDLEDNRSED SVRPWTCPKC FAHYDVQSIL FDLNEAIMNR HNVIKRRNTT
     TGASAAAVAS LVSGPLSHSA SFSSPMGSTE DLNSKGSLGM DQGDDKSNEL VMSCPYFRNE
     IGGEGERKIS LSKSNSGSFS GCESTSFESA LSSHCTNAGV AVLEVPKESL MLHLDRVKRY
     TVEHVDLGAY YYRKFFYQKE HWNYFGADEN LGPVAVSIRR EKPEDMKENG SPYNYRIIFR
     TSELMTLRGS VLEDAIPSTA KHSTARGLPL KEVLEHVIPE LNVQCLRLAF NTPKVTEQLM
     KLDEQGLNYQ QKVGIMYCKA GQSTEEEMYN NESAGPAFEE FLQLLGERVR LKGFEKYRAQ
     LDTKTDSTGT HSLYTTYKDY EIMFHVSTML PYTPNNKQQL LRKRHIGNDI VTIVFQEPGA
     QPFSPKNIRS HFQHVFVIVR AHNPCTESVC YSVAVTRSRD VPSFGPPIPK GVTFPKSNVF
     RDFLLAKVIN AENAAHKSEK FRAMATRTRQ EYLKDLAEKN VTNTPIDPSG KFPFISLASK
     KKEKSKPYPG AELSSMGAIV WAVRAKDYNK AMEFDCLLGI SSEFIVLIEQ ETKSVAFNCS
     CRDVIGWTSS DTSLKIFYER GECVSVESFI SGEDIKEIVR RLQFVSKGCE SVEMTLRRNG
     LGQLGFHVNY EGIVADVEPY GYAWQAGLRQ GSRLVEICKV AVATLSHEQM IDLLRTSVTV
     KVVIIPPHDD CTPRRSCSET YRMPVMEYQM NEGISYEFKF PFRNNNKWQR NASKGAHSPQ
     VPSQLQSPMT SRLNAGKGDG KMPPPERAAN IPRSISSDGR PLERRLSPGS DIYVTVSSMA
     LARSQCRNSP SNLSSSSETG SGGGTYRQKS MPEGFGVSRR SPASIDRQNT QSDISGSGKS
     TPSWQRSEDS LADQMEPTCH LPAVSKVLPA FRESPSGRLM RQDPVVHLSP NKQGHSDSHY
     SSHSSSNTLS SNASSAHSDE KWYDGDRTES DLNSYNYLQG TSADSGIDTA SYGPSHGSTA
     SLGASTSSPR SGPGKEKVAP LWHSSSEVLS LADRTLETEG HGMDRKAESS LSLDIHSKSQ
     GGSSPLSREN STFSINDAAS HTSTMSSRHS ASPVVFSSAR SSPKEELHPT ASSQLAPSFS
     SSSSSSSGPR TFYPRQGATS KYLIGWKKPE GTINSVGFMD TRKRHQSDGN EIAHTRLRAS
     TRDLQASPKP TSKSTIEEDL KKLIDLESPT PESQKNFKFH ALSSPQSPFP TTPTSRRALH
     RTLSDESIYS SQREHFFTSR ASLLDQALPN DVLFSSTYPS LPKSLPLRRP SYTLGMKSLH
     GEFSASDSSL TDIQETRRQP IPDPGLMPLP DAASDLDWSN LVDAAKAYEV QRASFFAASD
     ENHRPLSAAS NSDQLEEQAL VQMKSYSSKD PSPTLASKVD QLEGMLKMLR EDLKKEKEDK
     AQLQAEVEHL REDNLRLQEE SQNASDKLKK FTEWVFNTID MS
//
ID   FRMD6_MOUSE             Reviewed;         622 AA.
AC   Q8C0V9; Q8BW34;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-AUG-2003, sequence version 2.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=FERM domain-containing protein 6;
GN   Name=Frmd6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Ovary, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522 AND SER-525, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450; SER-542 AND
RP   SER-544, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane;
CC       Peripheral membrane protein; Cytoplasmic side (By similarity).
CC       Note=Can colocalize with actin (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8C0V9-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q8C0V9-2; Sequence=VSP_008024, VSP_008025, VSP_008026;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8C0V9-3; Sequence=VSP_008026, VSP_008027, VSP_008028;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 FERM domain.
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DR   EMBL; AK029709; BAC26574.1; -; mRNA.
DR   EMBL; AK054457; BAC35785.1; -; mRNA.
DR   EMBL; BC053929; AAH53929.1; -; mRNA.
DR   IPI; IPI00338635; -.
DR   IPI; IPI00338636; -.
DR   IPI; IPI00338637; -.
DR   RefSeq; NP_082403.2; NM_028127.3.
DR   UniGene; Mm.2962; -.
DR   ProteinModelPortal; Q8C0V9; -.
DR   PhosphoSite; Q8C0V9; -.
DR   PRIDE; Q8C0V9; -.
DR   Ensembl; ENSMUST00000057859; ENSMUSP00000052202; ENSMUSG00000048285.
DR   Ensembl; ENSMUST00000061386; ENSMUSP00000106139; ENSMUSG00000048285.
DR   GeneID; 319710; -.
DR   KEGG; mmu:319710; -.
DR   UCSC; uc007ntv.1; mouse.
DR   UCSC; uc007ntw.1; mouse.
DR   UCSC; uc007ntx.1; mouse.
DR   CTD; 319710; -.
DR   MGI; MGI:2442579; Frmd6.
DR   eggNOG; roNOG06487; -.
DR   GeneTree; ENSGT00600000084312; -.
DR   HOGENOM; HBG444071; -.
DR   HOVERGEN; HBG081539; -.
DR   InParanoid; Q8C0V9; -.
DR   OMA; CLAQQCV; -.
DR   OrthoDB; EOG4S1T6S; -.
DR   PhylomeDB; Q8C0V9; -.
DR   NextBio; 395244; -.
DR   ArrayExpress; Q8C0V9; -.
DR   Bgee; Q8C0V9; -.
DR   CleanEx; MM_FRMD6; -.
DR   Genevestigator; Q8C0V9; -.
DR   GermOnline; ENSMUSG00000048285; Mus musculus.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH_type.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   SMART; SM00295; B41; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   PROSITE; PS00660; FERM_1; FALSE_NEG.
DR   PROSITE; PS00661; FERM_2; FALSE_NEG.
DR   PROSITE; PS50057; FERM_3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasm; Membrane;
KW   Phosphoprotein.
FT   CHAIN         1    622       FERM domain-containing protein 6.
FT                                /FTId=PRO_0000219449.
FT   DOMAIN       16    328       FERM.
FT   COMPBIAS    130    133       Poly-Tyr.
FT   COMPBIAS    506    512       Poly-Ser.
FT   MOD_RES     450    450       Phosphoserine.
FT   MOD_RES     522    522       Phosphoserine.
FT   MOD_RES     525    525       Phosphoserine.
FT   MOD_RES     542    542       Phosphoserine.
FT   MOD_RES     544    544       Phosphoserine.
FT   VAR_SEQ       1     22       Missing (in isoform 2).
FT                                /FTId=VSP_008024.
FT   VAR_SEQ      23     33       PNDKSVSIIIN -> MCRIPRHCCLR (in isoform
FT                                2).
FT                                /FTId=VSP_008025.
FT   VAR_SEQ      91     98       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_008026.
FT   VAR_SEQ     499    571       LIVKEIGSSTSSSSETVVRLRGQSTDSLPQTICRKPKTSTD
FT                                RHSLSLDDIRLYQKDFLRIAGLCQDTAQSYTF -> ELLGQ
FT                                AVACRSPQAGTSKNRTVVGTLNPPGRRATAGGLIPGQVPSV
FT                                EEMGEGTRVVSMFCSARFSEASSVGLI (in isoform
FT                                3).
FT                                /FTId=VSP_008027.
FT   VAR_SEQ     572    622       Missing (in isoform 3).
FT                                /FTId=VSP_008028.
FT   CONFLICT    321    321       H -> Q (in Ref. 1; BAC26574).
FT   CONFLICT    431    431       G -> S (in Ref. 1; BAC35785).
SQ   SEQUENCE   622 AA;  71652 MW;  EDDC8490CD84305C CRC64;
     MNKLTFHNNK AMQDRRRVCI FLPNDKSVSI IINVKILCHQ LLVQVCDLLR LKDSHLFGLS
     VIQNNEHVYM ELSQKLYKYC PKEWKKEASK VRQYEVTWGI DQFGPPMIIH FRVQYYVENG
     KLISDRIARY YYYWHLRKQV LHSQCVLREE AYFLLAAFAL QADLGNFKRK LHHGDYFEPE
     AYFPAWVVSK RGKDYILKHI PNMHKDQFAL TASEAYLKYI KEAVRLDDVA IHYYRLYKDK
     REAEGSLTLG LTMRGIQIFQ NLEEEKQLLY DFPWTNVGKL VFVGKKFEIL PDGLPSARKL
     VYYTGCPTRS RHLLQLLSNS HRLYMNLQPV LRHLRKQEEN EEKKQYRESY ISDNLDLDMD
     PLEKRSRASG SSAGSVKHKR LSRHSTASHS SSHTSGIEAD TKPRDPGPED SCSGSAMHRK
     LKTCSSMTSH GSSHTSGVES GGKDRLEEDS QDEEIEMLVD DPRDLEPMPE ESLEVSPEMC
     IYITEDMLLS RKLNGHSGLI VKEIGSSTSS SSETVVRLRG QSTDSLPQTI CRKPKTSTDR
     HSLSLDDIRL YQKDFLRIAG LCQDTAQSYT FGCGHELDES GLYCNSCLAQ QCVNIQDAFP
     VKRASKYFSL DLTHDEVPEF VV
//
ID   PP4R4_MOUSE             Reviewed;         875 AA.
AC   Q8C0Y0; Q14CI7; Q14DT1; Q69ZE5; Q9CRR0;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit 4;
GN   Name=Ppp4r4; Synonyms=Kiaa1622, Pp4r4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Pancreatic islet;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-698 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Lung, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Putative regulatory subunit of serine/threonine-protein
CC       phosphatase 4 (By similarity).
CC   -!- SUBUNIT: Serine/threonine-protein phosphatase 4 (PP4) occurs in
CC       different assemblies of the catalytic and one or more regulatory
CC       subunits. Component of the PP4 complex PPP4C-PPP4R4 (By
CC       similarity).
CC   -!- INTERACTION:
CC       P97470:Ppp4c; NbExp=1; IntAct=EBI-2476041, EBI-2476073;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8C0Y0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C0Y0-2; Sequence=VSP_029619, VSP_029620;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8C0Y0-3; Sequence=VSP_029618;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 2 HEAT repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32499.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK173221; BAD32499.1; ALT_INIT; Transcribed_RNA.
DR   EMBL; AK018414; BAB31199.1; -; mRNA.
DR   EMBL; AK029499; BAC26478.1; -; mRNA.
DR   EMBL; BC111887; AAI11888.1; -; mRNA.
DR   EMBL; BC113754; AAI13755.1; -; mRNA.
DR   IPI; IPI00224111; -.
DR   IPI; IPI00877267; -.
DR   IPI; IPI00877280; -.
DR   RefSeq; NP_083256.2; NM_028980.3.
DR   UniGene; Mm.248619; -.
DR   ProteinModelPortal; Q8C0Y0; -.
DR   SMR; Q8C0Y0; 95-121, 216-280, 401-459, 608-635.
DR   IntAct; Q8C0Y0; 1.
DR   PRIDE; Q8C0Y0; -.
DR   Ensembl; ENSMUST00000021631; ENSMUSP00000021631; ENSMUSG00000021209.
DR   GeneID; 74521; -.
DR   KEGG; mmu:74521; -.
DR   UCSC; uc007ovw.1; mouse.
DR   CTD; 74521; -.
DR   MGI; MGI:1921771; Ppp4r4.
DR   eggNOG; roNOG06782; -.
DR   GeneTree; ENSGT00510000047895; -.
DR   HOGENOM; HBG713728; -.
DR   HOVERGEN; HBG098096; -.
DR   InParanoid; Q8C0Y0; -.
DR   OrthoDB; EOG4WSW95; -.
DR   NextBio; 341008; -.
DR   ArrayExpress; Q8C0Y0; -.
DR   Bgee; Q8C0Y0; -.
DR   Genevestigator; Q8C0Y0; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0008287; C:protein serine/threonine phosphatase complex; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000357; HEAT.
DR   InterPro; IPR021133; HEAT_type_2.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF02985; HEAT; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Repeat.
FT   CHAIN         1    875       Serine/threonine-protein phosphatase 4
FT                                regulatory subunit 4.
FT                                /FTId=PRO_0000311851.
FT   REPEAT      215    253       HEAT 1.
FT   REPEAT      254    292       HEAT 2.
FT   COILED      686    730       Potential.
FT   VAR_SEQ       1    109       Missing (in isoform 3).
FT                                /FTId=VSP_029618.
FT   VAR_SEQ     764    790       SKEIKKSKLTRSQSFNNQAFHAKYGTL -> REKSPSASQN
FT                                SGSLFSLHEIPESVLVP (in isoform 2).
FT                                /FTId=VSP_029619.
FT   VAR_SEQ     791    875       Missing (in isoform 2).
FT                                /FTId=VSP_029620.
FT   CONFLICT    624    631       RMKLCYLL -> SCLLM (in Ref. 1; BAD32499).
FT   CONFLICT    792    792       Q -> K (in Ref. 3; AAI11888 and 1;
FT                                BAD32499).
FT   CONFLICT    811    811       R -> G (in Ref. 3; AAI11888).
SQ   SEQUENCE   875 AA;  99481 MW;  12434A80AE936B1B CRC64;
     MHPPPPDAGV AMDFGQNSLF GYMEDLQELT IIERPVRRSL KTPEEIERLT VDEDLSDIDR
     AVYLLSAGQD VQGASVIANL PFLMRQNPTE TLRRVLPKVR EVLHVASVEM QLTAAVSFLT
     ILQEESMSVH TCAHSFLQVI LLHLEHRDTG VSNAWLETLL SAVELLPKET LRHEILNPLV
     SKAQLSQTVQ SRLVSCKILG KITNKFDAHS IKREILPLVK SLCQDVEYEV RSCMCRQLEN
     IAQGIGAELT KNVVLPELIE LSRDESGSVR LAAFETLVNM LDMFDTDDRS QTILPLVKSF
     CEKSFKADES ILISLSFHLG KLCHGLYGIF TPDQHLRFLE FYKKLCTLGL QQENGHNESQ
     IPSQIVEQEK KYTSVRKNCA YNFPAMIVFV DPKNFHMELY STFFCLCHDP EVPVRHTIAI
     CFYEVSKLLN SGVHLIHKEL ITLLQDESLE VLDALINHLP EILELMSTGG ENSVQENKFS
     SVPDLIPALT AAEQRAAASL KWRTHEKLLQ KYTCLPHIIS SDQIYYRFLQ RMFTIMMTNN
     VLPVQRAAAR TLCIFLRYNR KQEQRHEVIQ KLIEQLGQGK SYWNRLRFLD TCEFIIEIFS
     RSFFCKYFFL PVIELTHDPV ANVRMKLCYL LPKVKSALKI PADMHLLQQL EMCVRKLLCQ
     EKDKDVLAIV KKTVLELDRM EMSMDMFQKK NYEKDLLDQE KEREELLFLE MEQLEKEKHQ
     SDGRLASDKS FEKKRRDSRT STQSLSKNLP ISVPGPSSST ASTSKEIKKS KLTRSQSFNN
     QAFHAKYGTL DQCASKSSTL AHTSSVSGLV RTAMLSLTDD SFRTRNASSV PASFSPNPVM
     PSTSRGPGNT ADPKSSGSKD AQPRKATLKS RKSNP
//
ID   S39A6_MOUSE             Reviewed;         765 AA.
AC   Q8C145; Q7TPP9; Q7TQE0; Q8R518;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Zinc transporter ZIP6;
DE   AltName: Full=Endoplasmic reticulum membrane-linked protein;
DE            Short=Ermelin;
DE   AltName: Full=Solute carrier family 39 member 6;
DE   AltName: Full=Zrt- and Irt-like protein 6;
DE            Short=ZIP-6;
DE   Flags: Precursor;
GN   Name=Slc39a6; Synonyms=Zip6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 21-765, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RX   MEDLINE=21888618; PubMed=11891044; DOI=10.1016/S0378-1119(01)00885-X;
RA   Suzuki A., Endo T.;
RT   "Ermelin, an endoplasmic reticulum transmembrane protein, contains the
RT   novel HELP domain conserved in eukaryotes.";
RL   Gene 284:31-40(2002).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-68 AND ASN-275, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: May act as a zinc-influx transporter (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity). Note=Found in the endoplasmic reticulum when
CC       overexpressed.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the brain and testis. In
CC       the brain strongly expressed in the CA1 and CA3 regions, Purkinje
CC       cells in cerebellum and dentate gyrus in hippocampus. In testis
CC       found in spermatids or mature sperms in the central areas of
CC       seminiferous tubules.
CC   -!- INDUCTION: Induced during neuronal differentiation neuroblastoma
CC       cells line but down-regulated during myogenic differentiation of
CC       skeletal muscle cells line.
CC   -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH54780.2; Type=Erroneous initiation;
CC       Sequence=BAB86300.1; Type=Frameshift; Positions=226;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK028976; BAC26223.1; -; mRNA.
DR   EMBL; BC054780; AAH54780.2; ALT_INIT; mRNA.
DR   EMBL; BC055012; AAH55012.1; -; mRNA.
DR   EMBL; AB071697; BAB86300.1; ALT_SEQ; mRNA.
DR   IPI; IPI00469000; -.
DR   RefSeq; NP_631882.2; NM_139143.3.
DR   UniGene; Mm.21688; -.
DR   ProteinModelPortal; Q8C145; -.
DR   PhosphoSite; Q8C145; -.
DR   PRIDE; Q8C145; -.
DR   Ensembl; ENSMUST00000070726; ENSMUSP00000064667; ENSMUSG00000024270.
DR   GeneID; 106957; -.
DR   KEGG; mmu:106957; -.
DR   UCSC; uc008egv.1; mouse.
DR   CTD; 106957; -.
DR   MGI; MGI:2147279; Slc39a6.
DR   eggNOG; roNOG14965; -.
DR   GeneTree; ENSGT00550000074174; -.
DR   HOGENOM; HBG443965; -.
DR   HOVERGEN; HBG055748; -.
DR   InParanoid; Q8C145; -.
DR   OMA; VSEGTHF; -.
DR   OrthoDB; EOG4WDDBC; -.
DR   PhylomeDB; Q8C145; -.
DR   NextBio; 358490; -.
DR   ArrayExpress; Q8C145; -.
DR   Bgee; Q8C145; -.
DR   Genevestigator; Q8C145; -.
DR   GermOnline; ENSMUSG00000024270; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046873; F:metal ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0006829; P:zinc ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR003689; ZIP.
DR   Pfam; PF02535; Zip; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Coiled coil; Glycoprotein; Ion transport; Membrane;
KW   Phosphoprotein; Signal; Transmembrane; Transmembrane helix; Transport;
KW   Zinc; Zinc transport.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21    765       Zinc transporter ZIP6.
FT                                /FTId=PRO_0000041651.
FT   TOPO_DOM     21    335       Extracellular (Potential).
FT   TRANSMEM    336    356       Helical; Name=1; (Potential).
FT   TOPO_DOM    357    365       Cytoplasmic (Potential).
FT   TRANSMEM    366    386       Helical; Name=2; (Potential).
FT   TOPO_DOM    387    433       Extracellular (Potential).
FT   TRANSMEM    434    454       Helical; Name=3; (Potential).
FT   TOPO_DOM    455    667       Cytoplasmic (Potential).
FT   TRANSMEM    668    688       Helical; Name=4; (Potential).
FT   TOPO_DOM    689    696       Extracellular (Potential).
FT   TRANSMEM    697    717       Helical; Name=5; (Potential).
FT   TOPO_DOM    718    734       Cytoplasmic (Potential).
FT   TRANSMEM    735    755       Helical; Name=6; (Potential).
FT   TOPO_DOM    756    765       Extracellular (Potential).
FT   COILED      475    495       Potential.
FT   COMPBIAS     92    141       His-rich.
FT   COMPBIAS    458    463       Poly-Lys.
FT   COMPBIAS    523    526       Poly-Glu.
FT   COMPBIAS    551    588       His-rich.
FT   MOD_RES     488    488       Phosphoserine (By similarity).
FT   CARBOHYD     68     68       N-linked (GlcNAc...).
FT   CARBOHYD    250    250       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    275    275       N-linked (GlcNAc...).
FT   CARBOHYD    292    292       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    694    694       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    102    107       Missing (in Ref. 3; BAB86300).
FT   CONFLICT    201    201       A -> V (in Ref. 2; AAH55012).
SQ   SEQUENCE   765 AA;  86380 MW;  C8938B9C3371377B CRC64;
     MATDLSVIMI LTFALWVTSP LHELQSTAAF SQTTEKINSN WEPGVNVDLA VTMQRHHLQQ
     LFYRYGENDS LSVEGFRKLL QNIGIDKIKR VHIHHDHEHH ADHEHHSDHE HHSDHEHHSD
     HEHHSDHEHH SDHEHHSHRS HTVAGKNNRK AFCPDLDSDN SGKNPRTSLG KGSRPAEHMN
     GRRNIKESAS SSEVTSAVYN AVSEGTRFVE TIETPKPGRR TKDVNPSTPP SITEKSRVGR
     LSRLARKKSN ESVSEPRKSF MYSRNTNDNI QECFNTTKLL TSHGMSIQAL LNATEFNYLC
     PAIINQIDAR ACLIHTASEK KAEIPPKTYS LQIAWLGGFI AISIISFLSL LGVILVPLMN
     RVFFKFLLSF LVALAVGTLS GDALLHLLPH SHASHQHSHS HEEPAMEMKR GPLFSHLSAQ
     NIEESSYFDS TWKGLTALGG LYFMFLVEHV LTLIKQFKDK KKKNQKKPEN DEDVESKKQL
     SKYDSQLSSN EEKVDPGERP ESYLRADSQE PSPFDSQQPT MLEEEEVMIA HAHPQEVYNE
     YVPRGCKNKC HSHFHDTLGQ SDDLIHHHHD YHHILHHHHH QNHHPHSHSQ RYSREELKDA
     GIATLAWMVI MGDGLHNFSD GLAIGAAFTE GLSSGLSTSV AVFCHELPHE LGDFAVLLKA
     GMTVKQAVLY NALSAMLAYL GMATGIFIGH YAENVSMWIF ALTAGLFMYV ALVDMVPEML
     HNDASDHGCS RWGYFFLQNA GILLGFGIML LISIFEHKIV FRINF
//
ID   CPNE1_MOUSE             Reviewed;         536 AA.
AC   Q8C166; Q925K4; Q925K5;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Copine-1;
DE   AltName: Full=Copine I;
GN   Name=Cpne1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-454.
RC   STRAIN=ILS, and ISS;
RX   MEDLINE=21363810; PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-525, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: May function in membrane trafficking. Exhibits calcium-
CC       dependent phospholipid binding properties.
CC   -!- SIMILARITY: Belongs to the copine family.
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -!- SIMILARITY: Contains 1 VWFA domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK028882; BAC26170.1; -; mRNA.
DR   EMBL; BC057554; AAH57554.1; -; mRNA.
DR   EMBL; AF332057; AAK56086.1; -; mRNA.
DR   EMBL; AF332058; AAK56087.1; -; mRNA.
DR   IPI; IPI00224075; -.
DR   RefSeq; NP_733467.1; NM_170588.3.
DR   RefSeq; NP_733469.1; NM_170590.3.
DR   UniGene; Mm.27660; -.
DR   ProteinModelPortal; Q8C166; -.
DR   SMR; Q8C166; 5-281.
DR   PhosphoSite; Q8C166; -.
DR   REPRODUCTION-2DPAGE; Q8C166; -.
DR   PRIDE; Q8C166; -.
DR   Ensembl; ENSMUST00000109607; ENSMUSP00000105236; ENSMUSG00000074643.
DR   Ensembl; ENSMUST00000109608; ENSMUSP00000105237; ENSMUSG00000074643.
DR   GeneID; 266692; -.
DR   KEGG; mmu:266692; -.
DR   UCSC; uc008nmf.1; mouse.
DR   CTD; 266692; -.
DR   MGI; MGI:2386621; Cpne1.
DR   GeneTree; ENSGT00550000074189; -.
DR   HOGENOM; HBG464786; -.
DR   HOVERGEN; HBG066841; -.
DR   InParanoid; Q8C166; -.
DR   OMA; LQHFCGG; -.
DR   NextBio; 392184; -.
DR   ArrayExpress; Q8C166; -.
DR   Bgee; Q8C166; -.
DR   Genevestigator; Q8C166; -.
DR   GermOnline; ENSMUSG00000074643; Mus musculus.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR010734; Copine.
DR   InterPro; IPR002035; VWF_A.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF07002; Copine; 1.
DR   SMART; SM00239; C2; 2.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50234; VWFA; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein; Repeat.
FT   CHAIN         1    536       Copine-1.
FT                                /FTId=PRO_0000144835.
FT   DOMAIN        1     97       C2 1.
FT   DOMAIN      143    227       C2 2.
FT   DOMAIN      284    504       VWFA.
FT   MOD_RES     170    170       N6-acetyllysine (By similarity).
FT   MOD_RES     525    525       Phosphothreonine.
FT   CONFLICT     43     43       L -> P (in Ref. 2; AAH57554).
FT   CONFLICT    452    454       ADF -> GHS (in Ref. 3; AAK56087).
SQ   SEQUENCE   536 AA;  58887 MW;  DF603A71A1A74F7B CRC64;
     MAHCVTLVQL SVSCEHLIDK DIGSKSDPLC VLLQDVGGAW AELCRTERVR NCSSPEFSKT
     LQIEYHFETV QKLRFGIYDI DNKTPELGDD DFLGGAECSL GQIVSSQTLT LPLMLKPGKP
     AGRGTITVSA QELKDSRVVT MEVEARNLDK KDFLGKSDPF LEFFRQGDGK WQLAYRTEVV
     KNNLNPTWKR FSVSLQHFCG GDLSTPIQVR CSDYDSDGSH DLIGTFHTTL AQLQAVPAEF
     ECVHPEKQQR KKNYRNSGTV RVKTCRVETE YSFLDYVMGG CQINFTVGVD FTGSNGDPSS
     PDSLHYLSPT GVNEYLTALW SVGSVVQDYD SDKLFPAFGF GAQVPPDWQV SHEFALNFNP
     SNPYCAGIQG IVDAYRQALP QVRLYGPTNF APIINHVARF AAQAAQQRSA SQYFVLLLLT
     DGAVTDVEAT CKAVVDASKL PMSVIIVGVG GADFEVMEQL DADGGPLRTR SGEAAARDIV
     QFVPYRRFQN APRETLAQTV LAEVPTQMVS YFRAQGWAPL KAPPTPGKGP AQAPQA
//
ID   PPCEL_MOUSE             Reviewed;         725 AA.
AC   Q8C167; Q3TR35; Q6ZQB4; Q8BUP5; Q99KJ9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Prolyl endopeptidase-like;
DE            EC=3.4.21.-;
DE   AltName: Full=Prolylendopeptidase-like;
GN   Name=Prepl; Synonyms=Kiaa0436;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Aorta, Skin, Spinal cord, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Probable serine peptidase whose precise substrate
CC       specificity remains unclear. Does not cleave peptides after a
CC       arginine or lysine residue (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8C167-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C167-2; Sequence=VSP_030405;
CC       Name=3;
CC         IsoId=Q8C167-3; Sequence=VSP_030404;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q8C167-4; Sequence=VSP_030406, VSP_030407;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the peptidase S9A family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97952.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK129142; BAC97952.1; ALT_INIT; mRNA.
DR   EMBL; AK028877; BAC26168.1; -; mRNA.
DR   EMBL; AK083070; BAC38751.1; -; mRNA.
DR   EMBL; AK163108; BAE37195.1; -; mRNA.
DR   EMBL; BC004612; AAH04612.1; -; mRNA.
DR   IPI; IPI00224078; -.
DR   IPI; IPI00652834; -.
DR   IPI; IPI00875132; -.
DR   IPI; IPI00881277; -.
DR   RefSeq; NP_001157094.1; NM_001163622.1.
DR   RefSeq; NP_001157095.1; NM_001163623.1.
DR   RefSeq; NP_001157096.1; NM_001163624.1.
DR   RefSeq; NP_666096.3; NM_145984.3.
DR   UniGene; Mm.259035; -.
DR   UniGene; Mm.437393; -.
DR   UniGene; Mm.461481; -.
DR   ProteinModelPortal; Q8C167; -.
DR   SMR; Q8C167; 458-583.
DR   STRING; Q8C167; -.
DR   MEROPS; S09.015; -.
DR   PhosphoSite; Q8C167; -.
DR   PRIDE; Q8C167; -.
DR   Ensembl; ENSMUST00000064592; ENSMUSP00000063373; ENSMUSG00000024127.
DR   Ensembl; ENSMUST00000072406; ENSMUSP00000072239; ENSMUSG00000024127.
DR   GeneID; 213760; -.
DR   KEGG; mmu:213760; -.
DR   UCSC; uc008dto.1; mouse.
DR   CTD; 213760; -.
DR   MGI; MGI:2441932; Prepl.
DR   GeneTree; ENSGT00530000063426; -.
DR   HOGENOM; HBG443962; -.
DR   HOVERGEN; HBG108279; -.
DR   InParanoid; Q8C167; -.
DR   OMA; LTINIMN; -.
DR   OrthoDB; EOG4GHZNS; -.
DR   PhylomeDB; Q8C167; -.
DR   NextBio; 374089; -.
DR   ArrayExpress; Q8C167; -.
DR   Bgee; Q8C167; -.
DR   CleanEx; MM_PREPL; -.
DR   Genevestigator; Q8C167; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002470; Peptidase_S9A.
DR   InterPro; IPR004106; Peptidase_S9A_B_C_N.
DR   PANTHER; PTHR11757; Peptidase_S9A; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   Pfam; PF02897; Peptidase_S9_N; 1.
DR   PRINTS; PR00862; PROLIGOPTASE.
DR   SUPFAM; SSF50993; Peptidase_S9A_N; 1.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Hydrolase; Protease; Serine protease.
FT   CHAIN         1    725       Prolyl endopeptidase-like.
FT                                /FTId=PRO_0000314862.
FT   ACT_SITE    557    557       Charge relay system (By similarity).
FT   ACT_SITE    643    643       Charge relay system (By similarity).
FT   ACT_SITE    688    688       Charge relay system (By similarity).
FT   VAR_SEQ       1    267       Missing (in isoform 3).
FT                                /FTId=VSP_030404.
FT   VAR_SEQ       1     87       Missing (in isoform 2).
FT                                /FTId=VSP_030405.
FT   VAR_SEQ     249    261       SYFVFLYLTKDSR -> RCQRAALTALQALTIQ (in
FT                                isoform 4).
FT                                /FTId=VSP_030406.
FT   VAR_SEQ     262    725       Missing (in isoform 4).
FT                                /FTId=VSP_030407.
SQ   SEQUENCE   725 AA;  83194 MW;  111579DFA45CE68B CRC64;
     MLQTAKFSLR ALKHSIPHLG NCMQKQSYRN VAGPYYSRVR LKKYHLTKCL QNKPRIAGLA
     RNIPSRSFSC KDLLPIKPES EKPISENMDA FEKVRTRLET QPQEEYEVVN AEIKHGGFVY
     YQEGCCLVRS KDEEADSDNY EVLFNLEELK LDQPFIDCIR VAPDEKYVAA KIRTEDSETS
     TLVVVKLSDQ PVMEASFPNV SSFEWVKDEE DEDVLFYTFQ RNLRCHDVYR ATFGDNKRNE
     RFYTEKDPSY FVFLYLTKDS RFLTLNIMNK TTSEVWLIDG LSPWDPPVLI QKRIHGMLYY
     VEHRDDELYI LTNVGEPTEF KLMRTAADAP AIMNWDLFFT MKRNTKVVDL DMFKDHCVLF
     LKHSNLLYVN VIGLADDSVR SLKLPPWACG FIMDTNSDPK NCPFQLCSPI RPPKYYTYKF
     AEGKLFEETG HEDPITKTSR VLRIEAKSKD GKLVPMTVFH KTDSEDLQRK PLLVHVYGAY
     GMDLKMNFRP EKRVLVDDGW ILAYCHVRGG GELGLQWHAD GRLTKKLNGL ADLVACIKTL
     HSQGFSQPSL TTLSAFSAGG VLVGALCNSK PELLRAVTLE APFLDVLNTM LDTTLPLTLE
     ELEEWGNPSS DEKHKNYIKR YCPCQNIKPQ HYPSVHITAY ENDERVPLKG IVNYTEKLKE
     AVAEHTKGAG EGYQPPNIIL DIQPGGNHVI EDSHKKITTQ MKFLYEELGL DSTDAFEALK
     KYLKF
//
ID   MYO9A_MOUSE             Reviewed;        2542 AA.
AC   Q8C170; Q3TRT5; Q4VBD3; Q80Y92; Q8C0U0;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Myosin-IXa;
DE   AltName: Full=Unconventional myosin-9a;
GN   Name=Myo9a; Synonyms=Myr7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1848-2542 (ISOFORM 1/2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Skin, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2144-2542 (ISOFORM 1/2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=99339979; PubMed=10409426; DOI=10.1006/geno.1999.5867;
RA   Gorman S.W., Haider N.B., Grieshammer U., Swiderski R.E., Kim E.,
RA   Welch J.W., Searby C., Leng S., Carmi R., Sheffield V.C., Duhl D.M.;
RT   "The cloning and developmental expression of unconventional myosin IXA
RT   (MYO9A) a gene in the Bardet-Biedl syndrome (BBS4) region at
RT   chromosome 15q22-q23.";
RL   Genomics 59:150-160(1999).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1259 AND SER-1832, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-770, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Myosins are actin-based motor molecules with ATPase
CC       activity. Unconventional myosins serve in intracellular movements.
CC       Regulates Rho activity in neurons, has a role in the regulation of
CC       neuronal morphology and function (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8C170-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C170-2; Sequence=VSP_035161;
CC   -!- TISSUE SPECIFICITY: Expressed in the eye, lung, liver, brain,
CC       heart, kidney, skeletal muscle and spleen. No detection was found
CC       in liver.
CC   -!- DEVELOPMENTAL STAGE: Detected in whole embryos from E7, E11, E15,
CC       and E17. Also present in limb buds from E13.5. At E16.5, it is
CC       expressed throughout the developing nervous system, eye, inner
CC       ear, kidney, thyroid gland and teeth.
CC   -!- SIMILARITY: Contains 5 IQ domains.
CC   -!- SIMILARITY: Contains 2 myosin head-like domains.
CC   -!- SIMILARITY: Contains 2 phorbol-ester/DAG-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 Ras-associating domain.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC26164.1; Type=Erroneous initiation;
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DR   EMBL; AC156795; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC131749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK028873; BAC26164.1; ALT_INIT; mRNA.
DR   EMBL; AK029836; BAC26639.1; -; mRNA.
DR   EMBL; AK162486; BAE36942.1; -; mRNA.
DR   EMBL; BC046526; AAH46526.1; -; mRNA.
DR   EMBL; BC096035; AAH96035.1; -; mRNA.
DR   IPI; IPI00675346; -.
DR   IPI; IPI00882076; -.
DR   UniGene; Mm.249545; -.
DR   HSSP; P27986; 1PBW.
DR   ProteinModelPortal; Q8C170; -.
DR   SMR; Q8C170; 14-111, 144-1163, 1996-2249.
DR   PhosphoSite; Q8C170; -.
DR   Ensembl; ENSMUST00000085572; ENSMUSP00000082709; ENSMUSG00000039585.
DR   MGI; MGI:107735; Myo9a.
DR   eggNOG; roNOG10129; -.
DR   GeneTree; ENSGT00600000084203; -.
DR   HOGENOM; HBG446005; -.
DR   HOVERGEN; HBG108165; -.
DR   InParanoid; Q8C170; -.
DR   Bgee; Q8C170; -.
DR   Genevestigator; Q8C170; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:motor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000159; Ras-assoc.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF00612; IQ; 4.
DR   Pfam; PF00063; Myosin_head; 2.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00015; IQ; 5.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00314; RA; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50096; IQ; 4.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; ATP-binding; Coiled coil;
KW   GTPase activation; Membrane; Metal-binding; Motor protein; Myosin;
KW   Nucleotide-binding; Phosphoprotein; Repeat; Transmembrane;
KW   Transmembrane helix; Zinc; Zinc-finger.
FT   CHAIN         1   2542       Myosin-IXa.
FT                                /FTId=PRO_0000348441.
FT   TRANSMEM    175    195       Helical; (Potential).
FT   DOMAIN       14    112       Ras-associating.
FT   DOMAIN      148    690       Myosin head-like 1.
FT   DOMAIN      884   1005       Myosin head-like 2.
FT   DOMAIN     1021   1041       IQ 1.
FT   DOMAIN     1043   1072       IQ 2.
FT   DOMAIN     1075   1104       IQ 3.
FT   DOMAIN     1116   1145       IQ 4.
FT   DOMAIN     1139   1168       IQ 5.
FT   DOMAIN     2065   2253       Rho-GAP.
FT   NP_BIND     239    246       ATP (Potential).
FT   ZN_FING    2001   2050       Phorbol-ester/DAG-type 1.
FT   ZN_FING    2068   2119       Phorbol-ester/DAG-type 2.
FT   REGION      908    919       Actin-binding (By similarity).
FT   REGION     1022   1163       Neck or regulatory domain (By
FT                                similarity).
FT   REGION     1164   2505       Tail (By similarity).
FT   COILED     1265   1292       Potential.
FT   COILED     1492   1539       Potential.
FT   COILED     2324   2360       Potential.
FT   COMPBIAS   2371   2438       Ser-rich.
FT   MOD_RES     770    770       Phosphothreonine.
FT   MOD_RES    1259   1259       Phosphoserine.
FT   MOD_RES    1832   1832       Phosphoserine.
FT   VAR_SEQ    1717   1717       E -> EVARPAHKKKARMARTRSDFLTRGTFAEGEGDTEED
FT                                DYDDIIEPLLSLDQASHSELGPVSSLGQASHSDSEM (in
FT                                isoform 2).
FT                                /FTId=VSP_035161.
FT   CONFLICT   2434   2434       N -> Y (in Ref. 3; AAH96035).
SQ   SEQUENCE   2542 AA;  292119 MW;  9371996D5B3D72E0 CRC64;
     MNVSDGGRRR FEDNEHTLRI YPGTISEGTI YCPIPARKNS TAAEVIDSLI NRLHLDKTKC
     YVLAEVKEFG GEEWILNPTD CPVQRMMLWP RMALENRLSG EDYRFLLREK NLDGSIHYGS
     LQSWLRVTEE RRRMMERGFL PQPQQKDFDD LCSLPDLNEK TLLENLRNRF KHEKIYTYVG
     SILIAINPFK FLPIYNPKYV KMYDNHQLGK LEPHIYAVAD VAYHAMLQRK KNQCIVISGE
     SGSGKTQSTN FLIHHLTALS QKGFASGVEQ IILGAGPVLE AFGNAKTAHN NNSSRFGKFI
     QVNYQETGTV LGAYVEKYLL EKSRLVYQEH NERNYHVFYY LLAGASEEER LAFHLKQPEE
     YHFLNQITKK PLRQSWDDYC YDSEPDCFTV EGEDLRHDFE RLQLAMEMVG FLPKTRRQIF
     SLLSAILHLG NISYKKKTYR DDSIDICNPE VLPIVSELLE VKEEMLFEAL VTRKTVTVGE
     KLILPYKLAE AVTVRNSMAK SLYSALFDWI VFRINHALLN SKDLEQDTKT LSIGVLDIFG
     FEDYENNSFE QFCINFANER LQHYFNQHIF KLEQEEYRTE GISWHNIDYI DNTCCINLIS
     KKPTGLLHLL DEESNFPQAT NQTLLDKFKH QHEENSYIEF PAVMEPAFII KHYAGKVKYG
     VKDFREKNTD HMRPDIVALL RSSRNAFVSG MTGIDPVAVF RWAVLRAFFR AVVAFREAGK
     RHIQRKSGHD DTTPCAILKS MDSFSFLQHP VHQRSLEILQ RCKEEKYSIT RKNPRTPLSD
     LQGMNTLNEK NQHDTFDIAW NVRTGIRQSR LPASNTSLLD KDGIFAHSAS SKLLERAHGI
     LTRNKNFRSK PVLPKHLLEV NSLKHLTRLT LQDRITKSLL HLHKKKKPPS ISAQFQASLS
     KLMETLGQAE PYFVKCIRSN AEKLPLRFSD ALVLRQLRYT GMLETVRIRQ SGYSSKYSFQ
     DFVSHFHVLL PQHIIPSKFN IQDFFRKINI NSDNYQVGKT MVFLKEHERQ HLQDLLHQEV
     LRRIVLLQRW FRVLLSRQQF LHLRQASIII QRFWRNYLNQ KQVRNAAVEK DAFIMASAAS
     LLQASWRAHL ERQRYLELRA AAVIIQQRWR ELYRCRHKAA TCIQSRWRGY RQRKKYKEQR
     NKIILLQSIY RGFRARQRCN ALKEEKLREA KLEHGLVHVK ACGPLEIQGS DPSEWEDRSF
     DNRVKAIEEC KYVIESNRIS RESSMDFSKE SPDKQQERGR RQSGTDLQED VIVRQRPKSL
     EDLHQKKVGR AKRESRRMRE LEQAIFSLEL LKVRSLGGMS PSEERRWSTE LMPEGLQSPH
     GTPDSESSQG SLELLTCDEN QKSKPESLIL DEGELKISSP NTFTNPKSQD NALSASSETS
     STLAGKGASS DSEHLKNGTA KEKLVCSSEP ITCKPQLRDS FVSSSLPTFF YIPHQEALKT
     SSHLDTSIQR NKLPEREAIL KTTLTQDINR EARKCQFSGD QMTPLNTDSS CTVLKKLEKL
     NIEKEKRQKQ LQQQNEKEMM EQIRQQTDIL EKERKAFKTI EQSRTEASVL APSFYQPRQK
     VERPCSLYIQ NTPSKGEAGV LGSPSAVTKR DAALATKDSP SIHLPPKDRP VTLFFEKKGS
     PCQSRTVKEL PKTERTGTQH DAAYKLSNNR STERDHFKST HFYSHRSDDP SREGSSRAIF
     FTPKDNITPL VHSGNPQAHK QDESAWKPKL AGPGQQETSQ RFSSVDEQAK LHKAMSQGEI
     TKLAVRQKAS DLDIRPQRAK MRFWAKGKQG EKKTTRVKPA SQSEISSFFP GPDVTPAHPF
     SDELTQYHPT PPLSPELPGS CRKEFKENKE PSPKAKRKRG VKISSVALDS MHWQNDSVQI
     IASASDLKSM DEFLLKKMND LDNEDSKKDT LVDVVFKKAL KEFRQNIFSS YSSALAMDDG
     KSIRYKDLYA LFEQILEKTM RLEQRDWNES PVRVWVNTFK VFLDEYMNEF KTLDSTAPKV
     LKTERKKRRK KETDLVEEHN GHIFKATQYS IPTYCEYCSS LIWIMDRASV CKLCKYACHK
     KCCLKTTAKC SKKYDPELSS RQFGVELSRL TSEDRAVPLV VEKLINYIEM HGLYTEGIYR
     KSGSTNKIKE LRQGLDTDAE SVNLDDYNIH VIASVFKQWL RDLPNPLMTF ELYEEFLRAM
     GLQERKETIR GVYSVIDQLS RTHLNTLERL IFHLVRIALQ EDTNRMSANA LAIVFAPCIL
     RCPDTTDPLQ SVQDISKTTT CVELIVVEQM NKYKARLKDI SSLEFAENKA KTRLSLIRRS
     MGKGRIHRGN YPSPSSPVIV RLPSMSDVPE ETLSSETAME TDLTDQQQAA MQQEEKVLTE
     QIENLQKEKE ELTFEMLVLE PRASDDETLE SEASIGTADS SENLNMDSEE RSLALSSLKA
     AGKSEPSSKS RKQLRKQPDS LDSVSSSVSS CLSNTTSSHG TRKRFQIYSK SPFYRAASAC
     EAQGTEGPLG QAKSLEDRPQ FISRGTFNPE KGKQKLKNVK NSPQKTKETP EGTVTSGRKK
     TVDSDCSSTQ QLPLFGNNEF MV
//
ID   Q8C173_MOUSE            Unreviewed;       238 AA.
AC   Q8C173;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 46.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Auts2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK028848; BAC26152.1; -; mRNA.
DR   IPI; IPI00970099; -.
DR   UniGene; Mm.389695; -.
DR   UniGene; Mm.409595; -.
DR   STRING; Q8C173; -.
DR   PRIDE; Q8C173; -.
DR   Ensembl; ENSMUST00000061007; ENSMUSP00000062515; ENSMUSG00000029673.
DR   Ensembl; ENSMUST00000160071; ENSMUSP00000125349; ENSMUSG00000029673.
DR   Ensembl; ENSMUST00000161374; ENSMUSP00000124730; ENSMUSG00000029673.
DR   Ensembl; ENSMUST00000161804; ENSMUSP00000124027; ENSMUSG00000029673.
DR   MGI; MGI:1919847; Auts2.
DR   GeneTree; ENSGT00390000001466; -.
DR   HOVERGEN; HBG069435; -.
DR   InParanoid; Q8C173; -.
DR   ArrayExpress; Q8C173; -.
DR   Bgee; Q8C173; -.
DR   Genevestigator; Q8C173; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   238 AA;  27212 MW;  B6FB0AAA1B56EE49 CRC64;
     MPMTVGVTGI HAMNSIGSLD RTRMVTPFMG LSPIPGGERF PYPSFHWDPM RDPLRDPYRD
     LDMHRRDPLG RDFLLRNDPL HRLSTPRLYE ADRSFRDREP HDYSHHHHHH HHPLAVDPRR
     EHERGGHLDE RERLHVLRED YEHPRLHPVH PASLDGHLPH PSLLTPGLPS MHYPRISPTA
     GHQNGLLNKT PPTAALSAPP PLISTLGGRP GSPRRTTPLS AEIRERPPSH TLKDIEAR
//
ID   FRS2_MOUSE              Reviewed;         508 AA.
AC   Q8C180;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Fibroblast growth factor receptor substrate 2;
DE            Short=FGFR substrate 2;
DE   AltName: Full=FGFR-signaling adaptor SNT;
DE   AltName: Full=FRS2-alpha;
DE   AltName: Full=Suc1-associated neurotrophic factor target 1;
DE            Short=SNT-1;
GN   Name=Frs2; Synonyms=Frs2a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 251-260; 305-320; 344-361 AND 468-480, FUNCTION,
RP   INTERACTION WITH GRB2, IDENTIFICATION IN A COMPLEX WITH GRB2 AND SOS1,
RP   MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2; TYR-196; TYR-306;
RP   TYR-349 AND TYR-392, PHOSPHORYLATION AT TYROSINE RESIDUES, AND TISSUE
RP   SPECIFICITY.
RX   MEDLINE=97325745; PubMed=9182757; DOI=10.1016/S0092-8674(00)80252-4;
RA   Kouhara H., Hadari Y.R., Spivak-Kroizman T., Schilling J.,
RA   Bar-Sagi D., Lax I., Schlessinger J.;
RT   "A lipid-anchored Grb2-binding protein that links FGF-receptor
RT   activation to the Ras/MAPK signaling pathway.";
RL   Cell 89:693-702(1997).
RN   [4]
RP   INTERACTION WITH SUC1 AND GRB2, PHOSPHORYLATION AT TYROSINE RESIDUES,
RP   AND SUBCELLULAR LOCATION.
RX   MEDLINE=96374436; PubMed=8780727; DOI=10.1006/bbrc.1996.1288;
RA   Ong S.-H., Goh K.C., Lim Y.P., Low B.C., Klint P., Claesson-Welsh L.,
RA   Cao X., Tan Y.H., Guy G.R.;
RT   "Suc1-associated neurotrophic factor target (SNT) protein is a major
RT   FGF-stimulated tyrosine phosphorylated 90-kDa protein which binds to
RT   the SH2 domain of GRB2.";
RL   Biochem. Biophys. Res. Commun. 225:1021-1026(1996).
RN   [5]
RP   INTERACTION WITH PTPN11, AND MUTAGENESIS OF TYR-436.
RX   PubMed=9632781;
RA   Hadari Y.R., Kouhara H., Lax I., Schlessinger J.;
RT   "Binding of Shp2 tyrosine phosphatase to FRS2 is essential for
RT   fibroblast growth factor-induced PC12 cell differentiation.";
RL   Mol. Cell. Biol. 18:3966-3973(1998).
RN   [6]
RP   INTERACTION WITH FGFR1 AND NTRK1.
RX   MEDLINE=20094977; PubMed=10629055; DOI=10.1128/MCB.20.3.979-989.2000;
RA   Ong S.-H., Guy G.R., Hadari Y.R., Laks S., Gotoh N., Schlessinger J.,
RA   Lax I.;
RT   "FRS2 proteins recruit intracellular signaling pathways by binding to
RT   diverse targets on fibroblast growth factor and nerve growth factor
RT   receptors.";
RL   Mol. Cell. Biol. 20:979-989(2000).
RN   [7]
RP   FUNCTION, INTERACTION WITH RET, AND PHOSPHORYLATION AT TYROSINE
RP   RESIDUES.
RX   PubMed=11390647; DOI=10.1128/MCB.21.13.4177-4187.2001;
RA   Melillo R.M., Santoro M., Ong S.-H., Billaud M., Fusco A.,
RA   Hadari Y.R., Schlessinger J., Lax I.;
RT   "Docking protein FRS2 links the protein tyrosine kinase RET and its
RT   oncogenic forms with the mitogen-activated protein kinase signaling
RT   cascade.";
RL   Mol. Cell. Biol. 21:4177-4187(2001).
RN   [8]
RP   IDENTIFICATION IN A COMPLEX WITH GRB2 AND CBL, AND UBIQUITINATION.
RX   PubMed=11997436; DOI=10.1073/pnas.052138899;
RA   Wong A., Lamothe B., Lee A., Schlessinger J., Lax I.;
RT   "FRS2 alpha attenuates FGF receptor signaling by Grb2-mediated
RT   recruitment of the ubiquitin ligase Cbl.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:6684-6689(2002).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-288, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-172 AND
RP   SER-211, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-349, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Adapter protein that links FGR and NGF receptors to
CC       downstream signaling pathways. Involved in the activation of MAP
CC       kinases. Modulates signaling via SHC1 by competing for a common
CC       binding site on NTRK1.
CC   -!- SUBUNIT: Binds NTRK2 and NTRK3. Part of a complex containing GRB2
CC       and CBL (By similarity). Binds FGFR1, SUC1, RET and phosphorylated
CC       NTRK1. The tyrosine-phosphorylated protein binds the SH2 domains
CC       of GRB2 and PTPN11. Part of a complex containing FRS2, GRB2 and
CC       SOS1.
CC   -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Expression is highest in brain,
CC       kidney, lung and testis.
CC   -!- PTM: Phosphorylated on tyrosine residues upon stimulation by BFGF
CC       or NGFB.
CC   -!- PTM: Ubiquitinated when tyrosine phosphorylated and in a complex
CC       with GRB2. The unphosphorylated form is not subject to
CC       ubiquitination.
CC   -!- SIMILARITY: Contains 1 IRS-type PTB domain.
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DR   EMBL; AK028813; BAC26132.1; -; mRNA.
DR   EMBL; BC043109; AAH43109.1; -; mRNA.
DR   EMBL; BC055334; AAH55334.1; -; mRNA.
DR   IPI; IPI00224112; -.
DR   RefSeq; NP_808466.1; NM_177798.3.
DR   UniGene; Mm.135965; -.
DR   ProteinModelPortal; Q8C180; -.
DR   SMR; Q8C180; 11-136.
DR   STRING; Q8C180; -.
DR   PhosphoSite; Q8C180; -.
DR   PRIDE; Q8C180; -.
DR   Ensembl; ENSMUST00000020381; ENSMUSP00000020381; ENSMUSG00000020170.
DR   GeneID; 327826; -.
DR   KEGG; mmu:327826; -.
DR   UCSC; uc007hct.1; mouse.
DR   CTD; 327826; -.
DR   MGI; MGI:1100860; Frs2.
DR   eggNOG; roNOG11010; -.
DR   GeneTree; ENSGT00510000046707; -.
DR   HOGENOM; HBG446324; -.
DR   HOVERGEN; HBG062705; -.
DR   InParanoid; Q8C180; -.
DR   OMA; NVNNSAQ; -.
DR   OrthoDB; EOG4M398C; -.
DR   PhylomeDB; Q8C180; -.
DR   NextBio; 397981; -.
DR   ArrayExpress; Q8C180; -.
DR   Bgee; Q8C180; -.
DR   CleanEx; MM_FRS2; -.
DR   Genevestigator; Q8C180; -.
DR   GermOnline; ENSMUSG00000020170; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005158; F:insulin receptor binding; IEA:InterPro.
DR   GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; IDA:MGI.
DR   GO; GO:0000187; P:activation of MAPK activity; IMP:MGI.
DR   GO; GO:0008595; P:anterior/posterior axis specification, embryo; IMP:MGI.
DR   GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IGI:MGI.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
DR   GO; GO:0007405; P:neuroblast proliferation; IGI:MGI.
DR   GO; GO:0046619; P:optic placode formation involved in camera-type eye formation; IMP:MGI.
DR   GO; GO:0001759; P:organ induction; IMP:MGI.
DR   GO; GO:0060527; P:prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis; IMP:MGI.
DR   GO; GO:0050678; P:regulation of epithelial cell proliferation; IMP:MGI.
DR   GO; GO:0003281; P:ventricular septum development; IMP:MGI.
DR   InterPro; IPR002404; Insln_rcpt_S1.
DR   InterPro; IPR011993; PH_type.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF02174; IRS; 1.
DR   SMART; SM00310; PTBI; 1.
DR   PROSITE; PS51064; IRS_PTB; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Lipoprotein; Membrane; Myristate;
KW   Phosphoprotein; Ubl conjugation.
FT   INIT_MET      1      1       Removed (Potential).
FT   CHAIN         2    508       Fibroblast growth factor receptor
FT                                substrate 2.
FT                                /FTId=PRO_0000087345.
FT   DOMAIN       13    115       IRS-type PTB.
FT   MOD_RES     169    169       Phosphoserine.
FT   MOD_RES     172    172       Phosphoserine.
FT   MOD_RES     211    211       Phosphoserine.
FT   MOD_RES     288    288       Phosphothreonine.
FT   MOD_RES     349    349       Phosphotyrosine.
FT   LIPID         2      2       N-myristoyl glycine.
FT   MUTAGEN       2      2       G->A: Abolishes myristoylation and
FT                                membrane association.
FT   MUTAGEN     196    196       Y->F: Abolishes tyrosine phosphorylation
FT                                and interactions with GRB2 and PTPN11;
FT                                when associated with F-306; F-349; F-392
FT                                and F-436.
FT   MUTAGEN     306    306       Y->F: Abolishes tyrosine phosphorylation
FT                                and interactions with GRB2 and PTPN11;
FT                                when associated with F-196; F-349; F-392
FT                                and F-436.
FT   MUTAGEN     349    349       Y->F: Abolishes tyrosine phosphorylation
FT                                and interactions with GRB2 and PTPN11;
FT                                when associated with F-196; F-306; F-392
FT                                and F-436.
FT   MUTAGEN     392    392       Y->F: Abolishes tyrosine phosphorylation
FT                                and interactions with GRB2 and PTPN11;
FT                                when associated with F-196; F-306; F-349
FT                                and F-436.
FT   MUTAGEN     436    436       Y->F: Abolishes tyrosine phosphorylation
FT                                and interactions with GRB2 and PTPN11;
FT                                when associated with F-196; F-306; F-349
FT                                and F-392.
SQ   SEQUENCE   508 AA;  56794 MW;  DFFE8A818BFF8631 CRC64;
     MGSCCSCPDK DTVPDNHRNK FKVINVDDDG NELGSGVMEL TDTELILYTR KRDSVKWHYL
     CLRRYGYDSN LFSFESGRRC QTGQGIFAFK CARAEELFNM LQEIMQNNSI NVVEEPVVER
     SSHQTELEVP RTPRTPTTPG LGAQNLPNGY PRYPSFGDAS SHPSSRHPSV GSARLPSVGE
     ESTHPLLVAE EQVHTYVNTT GVQEERKNRA SVHVPPEARV SNAESNTPKE EPSNPEDRDP
     QVLLKPEGVR FVLGPTPVQK QLMEKEKLEQ LGKDPVSGSG AGNTEWDTGY DSDERRDVPP
     VNKLVYENIN GLSIPSASGV RRGRLTSTST SDTQNINNSA QRRPALLNYE NLPSLPPVWE
     ARKLSRDEDD NLGPKTPSLN GYHNNLDPMH NYVNTENVTV PASAHKIDYS KRRDCTPTVF
     NFDIRRPSLE HRQLNYIQVD LEGGSDSDNP QTPKTPTTPL PQTPTRRTEL YAVIDIERTA
     AMSNLQKALP RDDGTSRKTR HNSTDLPM
//
ID   CAMP2_MOUSE             Reviewed;        1461 AA.
AC   Q8C1B1; B7ZNI4; Q80TK8; Q8C4J5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 3.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Calmodulin-regulated spectrin-associated protein 2;
DE   AltName: Full=Calmodulin-regulated spectrin-associated protein 1-like protein 1;
GN   Name=Camsap1l1; Synonyms=Camsap2, Kiaa1078;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1185 (ISOFORMS 1/2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1223-1461 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 658-1461 (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1222, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1291, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8C1B1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C1B1-2; Sequence=VSP_030807;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The CKK domain binds microtubules (By similarity).
CC   -!- SIMILARITY: Belongs to the CAMSAP1 family.
CC   -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC   -!- SIMILARITY: Contains 1 CKK domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC145258; AAI45259.1; -; mRNA.
DR   EMBL; AK028542; BAC25999.2; -; mRNA.
DR   EMBL; AK081975; BAC38384.1; -; mRNA.
DR   EMBL; AK122436; BAC65718.1; -; mRNA.
DR   IPI; IPI00831089; -.
DR   IPI; IPI00885543; -.
DR   UniGene; Mm.144143; -.
DR   ProteinModelPortal; Q8C1B1; -.
DR   SMR; Q8C1B1; 1320-1449.
DR   STRING; Q8C1B1; -.
DR   Ensembl; ENSMUST00000048309; ENSMUSP00000041920; ENSMUSG00000041570.
DR   UCSC; uc007cur.1; mouse.
DR   MGI; MGI:1922434; Camsap1l1.
DR   eggNOG; roNOG06953; -.
DR   GeneTree; ENSGT00390000010026; -.
DR   InParanoid; Q8C1B1; -.
DR   OrthoDB; EOG402WR9; -.
DR   PhylomeDB; Q8C1B1; -.
DR   ArrayExpress; Q8C1B1; -.
DR   Bgee; Q8C1B1; -.
DR   Genevestigator; Q8C1B1; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   InterPro; IPR014797; CAMSAP_C.
DR   InterPro; IPR022613; CAMSAP_CH.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR011033; PRC_barrell-like.
DR   Pfam; PF11971; CAMSAP_CH; 1.
DR   Pfam; PF08683; DUF1781; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   SUPFAM; SSF50346; PRCH_cytoplasmic; 1.
DR   PROSITE; PS50021; CH; FALSE_NEG.
DR   PROSITE; PS51508; CKK; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Cytoskeleton; Microtubule;
KW   Phosphoprotein.
FT   CHAIN         1   1461       Calmodulin-regulated spectrin-associated
FT                                protein 2.
FT                                /FTId=PRO_0000316833.
FT   DOMAIN      175    321       CH.
FT   DOMAIN     1321   1455       CKK.
FT   MOD_RES     439    439       Phosphoserine (By similarity).
FT   MOD_RES     572    572       Phosphoserine (By similarity).
FT   MOD_RES     573    573       Phosphoserine.
FT   MOD_RES     647    647       Phosphoserine (By similarity).
FT   MOD_RES     874    874       Phosphoserine (By similarity).
FT   MOD_RES     905    905       Phosphoserine (By similarity).
FT   MOD_RES     910    910       Phosphoserine (By similarity).
FT   MOD_RES     961    961       Phosphothreonine (By similarity).
FT   MOD_RES     970    970       Phosphothreonine (By similarity).
FT   MOD_RES     975    975       Phosphothreonine (By similarity).
FT   MOD_RES     977    977       Phosphothreonine (By similarity).
FT   MOD_RES     981    981       Phosphoserine (By similarity).
FT   MOD_RES    1002   1002       Phosphoserine (By similarity).
FT   MOD_RES    1222   1222       Phosphothreonine.
FT   MOD_RES    1285   1285       Phosphoserine (By similarity).
FT   MOD_RES    1291   1291       Phosphoserine.
FT   VAR_SEQ    1257   1257       P -> PGSRISRVFS (in isoform 2).
FT                                /FTId=VSP_030807.
FT   CONFLICT     30     30       A -> T (in Ref. 1; AAI45259).
FT   CONFLICT    802    802       R -> Q (in Ref. 1; AAI45259).
SQ   SEQUENCE   1461 AA;  164333 MW;  24308DADC498788A CRC64;
     MGDAADPREM RRTFIVPAIK PFDHYDFSRA KIACNLAWLV AKAFGTENVP EELGDPFYTD
     QYDQEHIKPP VVNLLLSAEL YCRAGSLILK SDAAKPLLGH DAVIQALAQK GLYVTDQEKL
     VTERDLHKKP IQMSAHLAMI DTLMMAYTVE MISIEKVIAC AQQYSAFFQA TDLPYDIEDA
     VMYWMNKVNE HLKDIMEQEQ KSKEHHPAEA PGGQKARYRK EQTLLKQLPC IPLVENLLKD
     GTDGCALAAL IHFYCPAVVR LEDICLKETM SLADSLYNLQ LIQEFCQEYL NHCCHFSLED
     MLYAASSIKS NYLVFMAELF WWFEVVKPSF VQPRVVRPQG AEPAKDVPSV PVLNAAKRNI
     RDSSSSSDFS SRYTRPQTHS SASGGIRRSS SMSYVDGFIG TWPKEKRTSV HGVSFDISFD
     KEDSAQSSTP NRGIIRSVSN EGLTLNNSRA SKHIRKNLSF KPVNGEEEES IEEELHVDPH
     GDLQSPMPLN TNELNSNEST HYKLPNGALQ NRVLLDEFGN QIETPSIEEA LQIIHDTERP
     PHTPRPDQIA NGFFLHGQDL SILNSNIKLN QSSPDNLTDT KGALSPITDT TEVDTGIHVP
     SEDIPETMDE DSSLRDYTVS LDSDMDDASK LLQDYDLRAS NPREALSPCP STISTKSQPG
     SSASSSSGVK MTSFAEQKFR KLNHTDGKSS GSSSQKTTPE GSELNIPHVV SWAQIPEEAG
     VAPGRDTTQL LASEMVHLRM RLEEKRRAIE AQKKKMEAAF TKQRQKMGRT AFLTVVKKKG
     EGISPLREEA AGAEDEKVYT DRAKERESQK MDGQRSKSLA DIKESMETPP GRWLKSPTTP
     VDPERQWNLT SPSEETLNEG EILEYTKSIE KLNSSLHFLQ QEMQRLSLQQ EMLMQMREQQ
     AWVISPPQPS PQKQIRDFKP RQAGLSSAAA PFSSDSPRPT HPSPQSSTRK SASFSVKNQR
     TPRPNELKIT PLNRTLTPPR SVDSLPRLRR FSPSQVPIQT RSFVCFGDDG EPQKEPKQKE
     EIKKEPSECK GTLGPCDHNP GEKEIKPVES TVSEVLSQPI TETVCVTPNE DQLSQPTEPP
     PKPVFPPTAP KNVNLIEVSL SDLKPPEKAD VSVEKLDGES DKEQFDDDQK VCCGFFFKDD
     QKAENDMAMK RAALLEKRLR REKETQLRKQ QLEAEMEHKK EETRRKTEEE RQKKEDERAR
     REFIRQEYMR RKQLKLMEDM DTVIKPRPQA AKQKKQRPKS IHRDHIESPK TPIKGPPVSS
     LSLASLNTGD SESVHSGKRT PRSESVEGFL SPSRCGSRNG EKDWENASTT SSVASGTEYT
     GPKLYKEPSA KSNKHIIQNA LAHCCLAGKV NEGQKKKILE EMEKSDANNF LILFRDSGCQ
     FRSLYTYCPE TEEINKLTGI GPKSITKKMI EGLYKYNSDR KQFSHIPAKT LSASVDAITI
     HSHLWQTKRP VTPKKLLPTK A
//
ID   SEP11_MOUSE             Reviewed;         431 AA.
AC   Q8C1B7; Q3TBA0; Q3TC24; Q5D0F0; Q6P2K5; Q6P6I0;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Septin-11;
GN   Name=Sept11; Synonyms=D5Ertd606e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Mammary gland, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 15-79; 84-93; 96-110; 138-146; 163-170; 176-184;
RP   280-286; 293-298; 309-336; 387-397 AND 399-418, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17546647; DOI=10.1002/humu.20554;
RA   Sudo K., Ito H., Iwamoto I., Morishita R., Asano T., Nagata K.;
RT   "SEPT9 sequence alternations causing hereditary neuralgic amyotrophy
RT   are associated with altered interactions with SEPT4/SEPT11 and
RT   resistance to Rho/Rhotekin-signaling.";
RL   Hum. Mutat. 28:1005-1013(2007).
CC   -!- FUNCTION: Filament-forming cytoskeletal GTPase. May play a role in
CC       cytokinesis (Potential). May play a role in the cytoarchitecture
CC       of neurons, including dendritic arborization and dendritic spines,
CC       and in GABAergic synaptic connectivity (By similarity).
CC   -!- SUBUNIT: Septins polymerize into heterooligomeric protein
CC       complexes that form filaments, and can associate with cellular
CC       membranes, actin filaments and microtubules. GTPase acitivity is
CC       required for filament formation. Interacts with SEPT7, SEPT9 and
CC       SEPT12. Forms homooligomers (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cell
CC       junction, synapse. Cell projection, dendritic spine. Cell
CC       projection, axon (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8C1B7-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q8C1B7-2; Sequence=VSP_011041;
CC       Name=3;
CC         IsoId=Q8C1B7-3; Sequence=VSP_011042;
CC   -!- SIMILARITY: Belongs to the septin family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK028475; BAC25969.1; -; mRNA.
DR   EMBL; AK166517; BAE38822.1; -; mRNA.
DR   EMBL; AK170945; BAE42133.1; -; mRNA.
DR   EMBL; AK171368; BAE42414.1; -; mRNA.
DR   EMBL; BC031456; AAH31456.1; -; mRNA.
DR   EMBL; BC062206; AAH62206.1; -; mRNA.
DR   EMBL; BC064466; AAH64466.1; -; mRNA.
DR   IPI; IPI00420385; -.
DR   IPI; IPI00454142; -.
DR   IPI; IPI00454143; -.
DR   RefSeq; NP_001009818.1; NM_001009818.1.
DR   UniGene; Mm.428571; -.
DR   ProteinModelPortal; Q8C1B7; -.
DR   SMR; Q8C1B7; 18-306.
DR   STRING; Q8C1B7; -.
DR   PRIDE; Q8C1B7; -.
DR   Ensembl; ENSMUST00000074733; ENSMUSP00000074293; ENSMUSG00000058013.
DR   GeneID; 52398; -.
DR   KEGG; mmu:52398; -.
DR   UCSC; uc008ydx.1; mouse.
DR   UCSC; uc008yea.1; mouse.
DR   CTD; 52398; -.
DR   MGI; MGI:1277214; Sept11.
DR   eggNOG; roNOG13245; -.
DR   GeneTree; ENSGT00590000082767; -.
DR   HOGENOM; HBG715249; -.
DR   HOVERGEN; HBG065093; -.
DR   InParanoid; Q8C1B7; -.
DR   OMA; KDLHEKF; -.
DR   OrthoDB; EOG4320Z8; -.
DR   PhylomeDB; Q8C1B7; -.
DR   NextBio; 308900; -.
DR   ArrayExpress; Q8C1B7; -.
DR   Bgee; Q8C1B7; -.
DR   CleanEx; MM_SEPT11; -.
DR   Genevestigator; Q8C1B7; -.
DR   GermOnline; ENSMUSG00000058013; Mus musculus.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0031105; C:septin complex; IEA:InterPro.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   InterPro; IPR000038; Cell_Div_GTP-bd.
DR   InterPro; IPR016491; Septin.
DR   PANTHER; PTHR18884; Cell_Div_GTP_bd; 1.
DR   Pfam; PF00735; Septin; 1.
DR   PIRSF; PIRSF006698; Septin; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell cycle; Cell division;
KW   Cell junction; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; GTP-binding; Nucleotide-binding; Synapse.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    431       Septin-11.
FT                                /FTId=PRO_0000173543.
FT   NP_BIND      48     55       GTP (By similarity).
FT   NP_BIND     184    192       GTP (By similarity).
FT   COILED      320    413       Potential.
FT   BINDING     103    103       GTP; via amide nitrogen (By similarity).
FT   BINDING     238    238       GTP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     253    253       GTP (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   VAR_SEQ     426    431       PWLCTE -> ASFA (in isoform 2).
FT                                /FTId=VSP_011041.
FT   VAR_SEQ     426    431       Missing (in isoform 3).
FT                                /FTId=VSP_011042.
FT   CONFLICT    171    171       K -> N (in Ref. 1; BAC25969).
FT   CONFLICT    418    418       K -> T (in Ref. 1; BAE42414).
FT   CONFLICT    425    425       N -> K (in Ref. 1; BAE42414).
SQ   SEQUENCE   431 AA;  49695 MW;  CC838B791729B511 CRC64;
     MAVAVGRPSN EELRNLSLSG HVGFDSLPDQ LVNKSTSQGF CFNILCVGET GIGKSTLMDT
     LFNTKFESDP ATHNEPGVRL KARSYELQES NVRLKLTIVD TVGFGDQINK DDSYKPIVEY
     IDAQFEAYLQ EELKIKRSLF NYHDTRIHAC LYFIAPTGHS LKSLDLVTMK KLDSKVNIIP
     IIAKADTIAK NELHKFKSKI MSELVSNGVQ IYQFPTDEET VAEINATMSV HLPFAVVGST
     EEVKIGNKMA KARQYPWGVV QVENENHCDF VKLREMLIRV NMEDLREQTH TRHYELYRRC
     KLEEMGFKDT DPDSKPFSLQ ETYEAKRNEF LGELQKKEEE MRQMFVMRVK EKEAELKEAE
     KELHEKFDLL KRTHQEEKKK VEDKKKELEE EVSNFQKKKA AAQLLQSQAQ QSGAQQTKKD
     KDKKNPWLCT E
//
ID   Q8C1W2_MOUSE            Unreviewed;       530 AA.
AC   Q8C1W2;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Pick1; Synonyms=Prkcabp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
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DR   EMBL; AK090155; BAC41117.1; -; mRNA.
DR   IPI; IPI00404576; -.
DR   UniGene; Mm.259464; -.
DR   HSSP; Q86UL8; 1UEQ.
DR   ProteinModelPortal; Q8C1W2; -.
DR   SMR; Q8C1W2; 18-104, 152-327, 393-529.
DR   STRING; Q8C1W2; -.
DR   PRIDE; Q8C1W2; -.
DR   Ensembl; ENSMUST00000053926; ENSMUSP00000061125; ENSMUSG00000068206.
DR   MGI; MGI:894645; Pick1.
DR   GeneTree; ENSGT00440000033690; -.
DR   InParanoid; Q8C1W2; -.
DR   OrthoDB; EOG4GQQ55; -.
DR   ArrayExpress; Q8C1W2; -.
DR   Bgee; Q8C1W2; -.
DR   Genevestigator; Q8C1W2; -.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
DR   GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
DR   GO; GO:0008022; F:protein C-terminus binding; ISS:UniProtKB.
DR   GO; GO:0005529; F:sugar binding; IEA:UniProtKB-KW.
DR   GO; GO:0007205; P:activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway; ISS:UniProtKB.
DR   GO; GO:0015844; P:monoamine transport; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0006605; P:protein targeting; IDA:MGI.
DR   InterPro; IPR010504; Arfaptin.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   InterPro; IPR001079; Galectin_CRD.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Gene3D; G3DSA:1.20.1270.60; Arfaptin; 1.
DR   Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 1.
DR   Pfam; PF06456; Arfaptin; 1.
DR   Pfam; PF00337; Gal-bind_lectin; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00908; Gal-bind_lectin; 1.
DR   SMART; SM00276; GLECT; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50870; AH; 1.
DR   PROSITE; PS51304; GALECTIN; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   530 AA;  58972 MW;  779B4AEE1C83BF0D CRC64;
     MFADLDYDIE EDKLGIPTVP GKVTLQKDAQ NLIGISIGGG AQYCPCLYIV QVFDNTPAAL
     DGTVAAGDEI TGVNGKSIKG KTKVEVAKMI QEVKGEVTIH YNKLQADPKQ GMSLDIVLKK
     VKHRLVENMS SGTADALGLS RAILCNDGLV KRLEELERTA ELYKGMTEHT KNLLRAFYEL
     SQTHRAFGDV FSVIGVREPQ PAASEAFVKF ADAHRSIEKF GIRLLKTIKP MLTDLNTYLN
     KAIPDTRLTI KKYLDVKFEY LSYCLKVKEM DDEEYSCIAL GEPLYRVSTG NYEYRLILRC
     RQEARARFSQ MRKDVLEKME LLDQKHGLRQ CQPGHESLPM CTHGLRPTPA LTAGTWRGSV
     ADSDTVVKLD DGHLNNSLGS PVQADVYFPR MIVPFCGHIK GDRRPDKKAL VMGILDLTPE
     SFAVGLTSGD PEDPPAHVAI ELEAVFTDLQ LLRNSCISGE RGGRAVSSRA VPYFSFIPDQ
     PFRAEILCQH PQFRVFVDGH QLFDFYHCIQ TVSATDTIKI NGDLQITKLG
//
ID   CCZ1_MOUSE              Reviewed;         480 AA.
AC   Q8C1Y8; Q3U891;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Vacuolar fusion protein CCZ1 homolog;
GN   Name=Ccz1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and C57BL/6J; TISSUE=Bone marrow, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane (By similarity).
CC   -!- SIMILARITY: Belongs to the CCZ1 family.
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DR   EMBL; AK090008; BAC41041.1; -; mRNA.
DR   EMBL; AK150793; BAE29856.1; -; mRNA.
DR   EMBL; AK152328; BAE31127.1; -; mRNA.
DR   EMBL; AK152576; BAE31327.1; -; mRNA.
DR   EMBL; AK153160; BAE31770.1; -; mRNA.
DR   EMBL; BC048077; AAH48077.1; -; mRNA.
DR   RefSeq; NP_808350.1; NM_177682.3.
DR   UniGene; Mm.320432; -.
DR   ProteinModelPortal; Q8C1Y8; -.
DR   PhosphoSite; Q8C1Y8; -.
DR   PRIDE; Q8C1Y8; -.
DR   Ensembl; ENSMUST00000031621; ENSMUSP00000031621; ENSMUSG00000029617.
DR   GeneID; 231874; -.
DR   KEGG; mmu:231874; -.
DR   UCSC; uc009ale.1; mouse.
DR   MGI; MGI:2141070; AU022870.
DR   eggNOG; roNOG13025; -.
DR   GeneTree; ENSGT00390000004713; -.
DR   HOGENOM; HBG315865; -.
DR   HOVERGEN; HBG053322; -.
DR   InParanoid; Q8C1Y8; -.
DR   OMA; RMSGSEK; -.
DR   OrthoDB; EOG4G1MG7; -.
DR   PhylomeDB; Q8C1Y8; -.
DR   NextBio; 380837; -.
DR   ArrayExpress; Q8C1Y8; -.
DR   Bgee; Q8C1Y8; -.
DR   CleanEx; MM_AU022870; -.
DR   Genevestigator; Q8C1Y8; -.
DR   GermOnline; ENSMUSG00000029617; Mus musculus.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR013176; DUF1712_fun.
DR   Pfam; PF08217; DUF1712; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Lysosome; Membrane; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    480       Vacuolar fusion protein CCZ1 homolog.
FT                                /FTId=PRO_0000089585.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     168    168       N6-acetyllysine (By similarity).
FT   MOD_RES     264    264       Phosphoserine.
SQ   SEQUENCE   480 AA;  55505 MW;  B6ABFCE751942389 CRC64;
     MAAAAAGPGA WAAQEKQFPP ALLSFFIYNP RFGPREGEEE NKILFYHPNE VEKNEKIRNV
     GLCEAIVQFT RTFSPSKPAK SLHTQKNRQF FNEPEENFWM VMVVRNPIIE KQSKDGKAVV
     EYQEEELLDK VYSSVLQQCY SMYKLFNGTF LKAMEDGGVK LLKERLEKFF HRYLQTLHLQ
     SCDLLDIFGG ISFFPLDKMT YLKIQSFINR MEESLSVVKY TAFLYNDQLI WSGLEQDDMR
     ILYKYLTTSL FPRHIEPELA GRDSPVRAEM PGNLQHYGRF LTGPLNLNDP EAKCRFPKIF
     VNTDDTYEEL HLIVYKAMSA AVCFMIDAST PLTLDFCRRL DSIVGPQLTV LASDICEQFN
     INKRISGSEK EPQFKFIYFN HMNLAEKSTI HMRKTPSVSL TSVHPDLMKI LGDINSDFTR
     ADEDEEIIVK AMSDYWVVGK KSDQRELYVI LSQKNANLIE VNEEVKKLCA TQFNNIFFLD
//
ID   RBM14_MOUSE             Reviewed;         669 AA.
AC   Q8C2Q3; Q3TJB6; Q91Z21; Q9DBI6;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=RNA-binding protein 14;
DE   AltName: Full=RNA-binding motif protein 14;
GN   Name=Rbm14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Liver, Placenta, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=129; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-629 AND SER-632, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-206, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256 AND SER-520, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582 AND SER-618, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-206 AND SER-582, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May function as a nuclear receptor coactivator,
CC       enhancing transcription through other coactivators such as NCOA6
CC       and CITED1 (By similarity).
CC   -!- SUBUNIT: Interacts with NCOA6, CITED1 and XRCC5/KU86. Interacts
CC       with SS18 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8C2Q3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C2Q3-2; Sequence=VSP_015080;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK004928; BAB23678.1; -; mRNA.
DR   EMBL; AK088201; BAC40206.1; -; mRNA.
DR   EMBL; AK167503; BAE39579.1; -; mRNA.
DR   EMBL; BC010294; AAH10294.1; -; mRNA.
DR   IPI; IPI00404707; -.
DR   IPI; IPI00649362; -.
DR   RefSeq; NP_063922.2; NM_019869.2.
DR   UniGene; Mm.276338; -.
DR   UniGene; Mm.441002; -.
DR   ProteinModelPortal; Q8C2Q3; -.
DR   SMR; Q8C2Q3; 2-156.
DR   STRING; Q8C2Q3; -.
DR   PhosphoSite; Q8C2Q3; -.
DR   PRIDE; Q8C2Q3; -.
DR   Ensembl; ENSMUST00000006625; ENSMUSP00000006625; ENSMUSG00000006456.
DR   Ensembl; ENSMUST00000113793; ENSMUSP00000109424; ENSMUSG00000006456.
DR   GeneID; 56275; -.
DR   KEGG; mmu:56275; -.
DR   UCSC; uc008gaz.1; mouse.
DR   CTD; 56275; -.
DR   MGI; MGI:1929092; Rbm14.
DR   eggNOG; roNOG04888; -.
DR   GeneTree; ENSGT00390000020883; -.
DR   HOGENOM; HBG280703; -.
DR   HOVERGEN; HBG053180; -.
DR   InParanoid; Q8C2Q3; -.
DR   OMA; GPGLAIQ; -.
DR   OrthoDB; EOG45X7XS; -.
DR   PhylomeDB; Q8C2Q3; -.
DR   NextBio; 312164; -.
DR   ArrayExpress; Q8C2Q3; -.
DR   Bgee; Q8C2Q3; -.
DR   CleanEx; MM_RBM14; -.
DR   Genevestigator; Q8C2Q3; -.
DR   GermOnline; ENSMUSG00000006456; Mus musculus.
DR   GO; GO:0005667; C:transcription factor complex; ISS:UniProtKB.
DR   GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; ISS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016575; P:histone deacetylation; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Nucleus; Phosphoprotein; Repeat; RNA-binding;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    669       RNA-binding protein 14.
FT                                /FTId=PRO_0000081775.
FT   DOMAIN        1     73       RRM 1.
FT   DOMAIN       79    149       RRM 2.
FT   REGION      307    354       TRBP-interacting domain (By similarity).
FT   COMPBIAS    224    538       Ala-rich.
FT   MOD_RES     161    161       Phosphoserine (By similarity).
FT   MOD_RES     206    206       Phosphothreonine.
FT   MOD_RES     215    215       Phosphoserine (By similarity).
FT   MOD_RES     220    220       Phosphoserine (By similarity).
FT   MOD_RES     256    256       Phosphoserine.
FT   MOD_RES     280    280       Phosphoserine (By similarity).
FT   MOD_RES     520    520       Phosphoserine.
FT   MOD_RES     562    562       Phosphoserine (By similarity).
FT   MOD_RES     571    571       Phosphoserine (By similarity).
FT   MOD_RES     572    572       Phosphothreonine (By similarity).
FT   MOD_RES     582    582       Phosphoserine.
FT   MOD_RES     618    618       Phosphoserine.
FT   MOD_RES     629    629       Phosphothreonine.
FT   MOD_RES     632    632       Phosphoserine.
FT   MOD_RES     649    649       Phosphoserine (By similarity).
FT   VAR_SEQ     603    669       GSDRRLAELSDYRRLSESQLSFRRSPTKSSLDYRRLPDAHS
FT                                DYARYSGSYNDYLRAAQMHSGYQRRM -> CMPPRLSPQLG
FT                                LRARG (in isoform 2).
FT                                /FTId=VSP_015080.
FT   CONFLICT    124    124       D -> Y (in Ref. 1; BAB23678).
FT   CONFLICT    136    136       E -> G (in Ref. 1; BAB23678).
FT   CONFLICT    182    182       S -> F (in Ref. 1; BAB23678).
SQ   SEQUENCE   669 AA;  69449 MW;  5B913852B06C87FA CRC64;
     MKIFVGNVDG ADTTPEELAA LFAPYGTVMS CAVMKQFAFV HMRENAGAVR AIEALHGHEL
     RPGRALVVEM SRPRPLNTWK IFVGNVSAAC TSQELRSLFE RRGRVIECDV VKDYAFVHME
     KEADAKAAIA QLNGKEVKGK RINVELSTKG QKKGPALAIQ SGDKTKKPGA GDTAFPGTGG
     FSATFDYQQA FGNSTGGFDG QARQPTPPFF GRDRSPLRRS PPRASYVAPL TAQPATYRAQ
     PSVSLGAAYR AQPSASLGVG YRTQPMAAQA ASYRAQPSVS LGAPYRGQLA SPSSQSAAAS
     SLGPYGGVQP SASALSTYGG QAAAASSLNS YGAQGSSLAS YGNQPSSYGA QAASSYGVRA
     AASSYNTQGA ASSLGSYGAQ AASYGAQSAA SSLAYGAQAA SYSAQPSASY SAQSAPYAAQ
     QAASYSSQPA AYVAQPATAA AYASQPAAYA AQATTPMAGS YGAQPVVQTQ LNSYGAQASI
     GLSGSYGAQS AAAATGSYGA AAAYGAQPSA TLAAPYRTQS SASLAASYAA QQHPQAAASY
     RGQPGSAYDG TGQPSAAYLS MSQGAVANAN STPPPYERTR LSPPRASYDD PYKKAVAMSK
     RYGSDRRLAE LSDYRRLSES QLSFRRSPTK SSLDYRRLPD AHSDYARYSG SYNDYLRAAQ
     MHSGYQRRM
//
ID   Q8C318_MOUSE            Unreviewed;       590 AA.
AC   Q8C318;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   30-NOV-2010, entry version 44.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Uhrf1bp1l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK087280; BAC39836.1; -; mRNA.
DR   IPI; IPI00762371; -.
DR   UniGene; Mm.268922; -.
DR   UniGene; Mm.446134; -.
DR   ProteinModelPortal; Q8C318; -.
DR   PRIDE; Q8C318; -.
DR   Ensembl; ENSMUST00000020112; ENSMUSP00000020112; ENSMUSG00000019951.
DR   MGI; MGI:2442888; Uhrf1bp1l.
DR   eggNOG; roNOG08645; -.
DR   InParanoid; Q8C318; -.
DR   ArrayExpress; Q8C318; -.
DR   Bgee; Q8C318; -.
DR   Genevestigator; Q8C318; -.
PE   2: Evidence at transcript level;
FT   NON_TER     590    590
SQ   SEQUENCE   590 AA;  66799 MW;  85C9AA66AF0CE1A3 CRC64;
     MEMSTCEEPR APNGPSPIAT ASGQSEYGFA EKVVEGITVS VNSIVIRIGA KAFNASFELS
     QLRIYSVNAQ WEHGDLRFTR IQDPQRGEVL TFKEINWQMI RIEADATQSS HLEIMCAPVR
     LITNQSKIRV TLKRRLKDCN VIATKLVLIL DDLLWVLTDS QLKAMVQYAK SLSEAIEKST
     EQRKSMAPEP TQSSTVTSSA QHVKTPQAAN APDLSDAIVK LFNDFDVKET SHHLVISHLD
     LHICDDIHAK EKESNRRVSG GAMQLSFTQL TIDYYPYHKA GDSCSHWMYF SDATKTKNGW
     ANELLHEFEC NVEMLKQAMK DRNLGSPPKS PTHASPQHTQ TEKDSTLKGT PKTPSVLPQP
     SKAKLMSSSV VVRLADFNIY QVSTAEQCRS SPKSMISCNK KSLYLPQEMS AIYIEFTEYY
     YPDGKDFPIP SPNLYSQLNA LQFTVDERSI LWLNQFLLDL KQSLNQFMAV YKLNDSSKSD
     EHVDIRVDGL MLKFVIPSEV KAGCHQDQPH TVSIQSSEMI ATNTRHCPNC RHSDLEALCQ
     DFKECDFFSK TYTRFPKSCD SFNLLHPIFQ RHAHEQDTKM HEVYKGNIIP
//
ID   OSPT_MOUSE              Reviewed;        1250 AA.
AC   Q8C341; Q3TAG8; Q3V3T1; Q8CE34;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 3.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Protein osteopotentia;
DE   Flags: Precursor;
GN   Name=Opt;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Cecum, Lung, Skin, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   FUNCTION, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RX   PubMed=20440000; DOI=10.1083/jcb.201003006;
RA   Sohaskey M.L., Jiang Y., Zhao J.J., Mohr A., Roemer F., Harland R.M.;
RT   "Osteopotentia regulates osteoblast maturation, bone formation, and
RT   skeletal integrity in mice.";
RL   J. Cell Biol. 189:511-525(2010).
CC   -!- FUNCTION: Required for bone modeling during late embryogenesis.
CC       Regulates type I collagen synthesis in osteoblasts during their
CC       postnatal maturation.
CC   -!- SUBCELLULAR LOCATION: Rough endoplasmic reticulum membrane;
CC       Single-pass type I membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8C341-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C341-2; Sequence=VSP_027924;
CC   -!- TISSUE SPECIFICITY: Present in chondrocytes, osteoblasts,
CC       osteoclasts and osteocytes (at protein level).
CC   -!- DEVELOPMENTAL STAGE: Expressed at E9.5 and E13.5.
CC   -!- PTM: N-glycosylated.
CC   -!- DISRUPTION PHENOTYPE: Most mice die neonatally from respiratory
CC       distress (50% on a mixed C57BL6/CD1 background and 100% on an
CC       inbred C57BL6/129Ola background). Surviving mice fail to thrive
CC       and show significantly reduced body weight, skeletal deformities
CC       and spontaneous fractures. More than 80% die by postnatal day 10,
CC       and none survives to weaning.
CC   -!- SIMILARITY: Contains 1 SUN domain.
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DR   EMBL; AK029097; BAC26295.1; -; mRNA.
DR   EMBL; AK033720; BAE43286.1; -; mRNA.
DR   EMBL; AK087029; BAC39786.2; -; mRNA.
DR   EMBL; AK171856; BAE42700.1; -; mRNA.
DR   EMBL; AC164414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00856553; -.
DR   IPI; IPI00944095; -.
DR   UniGene; Mm.170002; -.
DR   UniGene; Mm.425067; -.
DR   ProteinModelPortal; Q8C341; -.
DR   PhosphoSite; Q8C341; -.
DR   PRIDE; Q8C341; -.
DR   Ensembl; ENSMUST00000097505; ENSMUSP00000095112; ENSMUSG00000040297.
DR   MGI; MGI:2138346; AI848100.
DR   eggNOG; roNOG07452; -.
DR   GeneTree; ENSGT00390000013502; -.
DR   HOVERGEN; HBG107549; -.
DR   InParanoid; Q8C341; -.
DR   OrthoDB; EOG4ZS92P; -.
DR   ArrayExpress; Q8C341; -.
DR   Bgee; Q8C341; -.
DR   CleanEx; MM_AI848100; -.
DR   Genevestigator; Q8C341; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030867; C:rough endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR012919; Sad1_UNC_C.
DR   Pfam; PF07738; Sad1_UNC; 1.
DR   SUPFAM; SSF49785; Gal_bind_like; 1.
DR   PROSITE; PS51469; SUN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Developmental protein;
KW   Endoplasmic reticulum; Glycoprotein; Membrane; Osteogenesis; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     19       Potential.
FT   CHAIN        20   1250       Protein osteopotentia.
FT                                /FTId=PRO_0000302718.
FT   TRANSMEM   1007   1027       Helical; (Potential).
FT   DOMAIN      283    452       SUN.
FT   COILED      905   1005       Potential.
FT   CARBOHYD    201    201       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    235    235       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    523    523       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    924    924       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    951    951       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     285    285       S -> SLSTG (in isoform 2).
FT                                /FTId=VSP_027924.
FT   CONFLICT      4      4       Y -> N (in Ref. 1; BAE42700).
FT   CONFLICT    299    299       T -> K (in Ref. 1; BAC26295).
SQ   SEQUENCE   1250 AA;  139169 MW;  8713115267891629 CRC64;
     MKKYRRALAL VSCLSLCSLV WLPSWHVCCK ESSSASTSYY SQDDNCAIGS EDTQFQKKNE
     REEPSNAELS GKSNSYLTIS PEGNKIKDDY TVDVQDLETT KLSLPVVEAL PTVDLHEESS
     SVVVGSETIE NSSSSSTSER TPVSELDEVE KSGTLSIAKP GEVEQPEADC DAGEAPDADA
     PVEQPAFVSP PESLVGQHIE NVSSSHGKEK VTKSEFESKV SVSEQDGGDP KSALNTSDTL
     KNESSDYTKP GETDPTSVTS PKDPEDIPTF DEWKKKVMEV EKEKSQSLHP SSNGGPHATK
     KVQKNRNNYA SVECGAKILA ANPEAKSTSA ILIENMDLYM LNPCSTKIWF VIELCEPIQV
     KQFDIANYEL FSSTPKDFLV SISDRYPTNK WIKLGTFHGR DERNVQSFPL DEQMYAKYVK
     MFIKYIKVEL LSHFGSEHFC PLSLIRVFGT SMVEEYEEIA DSQYQSERQE LFDEDYDYPL
     DYNTVEDKSS KNLLGSATNA ILNMVNIAAN ILGAKTEDLT EGNKSISENA TATTEPKMTE
     STRVSTPVPS PEYVIKEVHT HDREPSTSDP PKESPIVQLV QEEEEEASPS TVTLLGSGEQ
     EDESSSWFES ETHILCSELT SICCISSFSE YIYKWCSVRI ALYRQRSRTV SKGKDFVPPQ
     PSLLLPVESV EVSVPQPPSG DVDSENMERE AETVDLDDLS SVHQGHLINH TVDTIELEPS
     YPQTLSQSLL LDVTPEMNSL SKVEGSESVK SEGGYIPSQL MTQESSVEFD DKTEKKTESF
     SSAEKLSVIY ETSKVNEVMD NTVKEDILST EVVTKFPETV VPPPMNTATV PEGESVETKP
     SIADTLKHTV TPVMDPSLPE VKEDEQSPED ALLRGLQRTA TDFYAELQNS TDLGYGNGNL
     VHGSNQKESV FMRLNNRIKA LEVNMSLSGR YLEELSQRYR KQMEEMQKAF NKTIVKLQNT
     SRIAEEQDQR QTEAIHLLQA QLTNMTQLVS NLSATVAELK REVSDRQSYL VMSLVLCVVL
     GLMLCMQRCR TTSQFDGDYI SKLPKSNQYP SPKRCFSSYD DMNLKRRTSF PLIRSKSLQF
     TGKEVDPNDL YIVEPLKFSP EKKKKRCKYK TEKIETIKPA DPLHPIANGD IKGRKPFTNQ
     RDFSNMGEVY HSSYKGPPSE GSSETSSQSE ESYFCGISAC TSLCNGQTQK TKTEKRALKR
     RRSKVQDQGK LIKALIQTKS GSLPSLHDII KGNKEITVGA FGVTAVSGHI
//
ID   LAYN_MOUSE              Reviewed;         381 AA.
AC   Q8C351; Q3TMU7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 3.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Layilin;
DE   Flags: Precursor;
GN   Name=Layn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-212 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Lung, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   INTERACTION WITH NF2 AND RDX.
RX   PubMed=15913605; DOI=10.1016/j.yexcr.2005.04.017;
RA   Bono P., Cordero E., Johnson K., Borowsky M., Ramesh V., Jacks T.,
RA   Hynes R.O.;
RT   "Layilin, a cell surface hyaluronan receptor, interacts with merlin
RT   and radixin.";
RL   Exp. Cell Res. 308:177-187(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-286 AND SER-299, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Receptor for hyaluronate (By similarity).
CC   -!- SUBUNIT: Interacts with TLN1 (By similarity). Interacts with NF2
CC       and RDX.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential). Note=Colocalizes with TLN1 at the membrane
CC       ruffles (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8C351-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C351-2; Sequence=VSP_021782, VSP_021783;
CC   -!- DOMAIN: The C-terminal domain interacts with the N-terminal domain
CC       of RDX.
CC   -!- SIMILARITY: Contains 1 C-type lectin domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK086930; BAC39765.2; -; mRNA.
DR   EMBL; AK165695; BAE38343.1; -; mRNA.
DR   EMBL; AC119831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00352139; -.
DR   IPI; IPI00808123; -.
DR   UniGene; Mm.335152; -.
DR   PDB; 2K00; NMR; -; B=367-381.
DR   PDBsum; 2K00; -.
DR   ProteinModelPortal; Q8C351; -.
DR   SMR; Q8C351; 37-186.
DR   STRING; Q8C351; -.
DR   PhosphoSite; Q8C351; -.
DR   PRIDE; Q8C351; -.
DR   Ensembl; ENSMUST00000073452; ENSMUSP00000073157; ENSMUSG00000060594.
DR   Ensembl; ENSMUST00000098782; ENSMUSP00000096379; ENSMUSG00000060594.
DR   UCSC; uc009plb.1; mouse.
DR   MGI; MGI:2685357; Layn.
DR   GeneTree; ENSGT00390000001844; -.
DR   HOGENOM; HBG715864; -.
DR   HOVERGEN; HBG050945; -.
DR   InParanoid; Q8C351; -.
DR   OrthoDB; EOG4FN4JN; -.
DR   ArrayExpress; Q8C351; -.
DR   Bgee; Q8C351; -.
DR   CleanEx; MM_LAYN; -.
DR   Genevestigator; Q8C351; -.
DR   GermOnline; ENSMUSG00000060594; Mus musculus.
DR   GO; GO:0009986; C:cell surface; ISS:HGNC.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0001726; C:ruffle; ISS:HGNC.
DR   GO; GO:0005540; F:hyaluronic acid binding; ISS:HGNC.
DR   GO; GO:0005529; F:sugar binding; IEA:UniProtKB-KW.
DR   InterPro; IPR001304; C-type_lectin.
DR   InterPro; IPR016186; C-type_lectin-like.
DR   InterPro; IPR016187; C-type_lectin_fold.
DR   Gene3D; G3DSA:3.10.100.10; C-type_lectin-like; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; C-type_lectin_fold; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; FALSE_NEG.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Disulfide bond; Glycoprotein;
KW   Lectin; Membrane; Phosphoprotein; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25    381       Layilin.
FT                                /FTId=PRO_0000262509.
FT   TOPO_DOM     25    235       Extracellular (Potential).
FT   TRANSMEM    236    256       Helical; (Potential).
FT   TOPO_DOM    257    381       Cytoplasmic (Potential).
FT   DOMAIN       45    185       C-type lectin.
FT   REPEAT      340    344       1-1.
FT   REPEAT      350    354       1-2.
FT   REPEAT      356    359       2-1.
FT   REPEAT      371    375       1-3.
FT   REPEAT      377    380       2-2.
FT   REGION      330    374       Interaction with NF2.
FT   REGION      337    381       Interaction with TLN1 (By similarity).
FT   REGION      340    375       3 X 5 AA repeats of E-S-G-X-V.
FT   REGION      356    380       2 X 4 AA repeats of N-X-I-Y.
FT   MOD_RES     286    286       Phosphoserine.
FT   MOD_RES     299    299       Phosphoserine.
FT   CARBOHYD    117    117       N-linked (GlcNAc...) (Potential).
FT   DISULFID     71    184       By similarity.
FT   DISULFID    150    176       By similarity.
FT   VAR_SEQ     136    137       RN -> SG (in isoform 2).
FT                                /FTId=VSP_021782.
FT   VAR_SEQ     138    381       Missing (in isoform 2).
FT                                /FTId=VSP_021783.
SQ   SEQUENCE   381 AA;  43200 MW;  C2207AF77B422A37 CRC64;
     MQPGAALQAM LLAVLLAKPR DSKGRLLSAS DLDPRGGQLV CRGGTRRPCY KVIYFHDAFQ
     RLNFEEAKET CMEDGGQLVS IETEDEQRLI EKFIENLLAS DGDFWIGLKR LEEKQSNNTA
     CQDLYAWTDG STSQFRNWYV DEPSCGSEVC VVMYHQPSAP PGIGGSYMFQ WNDDRCNMKN
     NFICKYHDDK PSTTPSIWPG GEATEPATPL LPEETQKEDT KETFKESEAA LNLAYILIPS
     IPLFLLLVVT SAVCWVWICR RRKREQTDPS TKEQHTIWPT PRQENSPNLD VYNVIRKQSE
     ADLAEPRPDL KNISFRVCSG EAMPDDMSCD YENIAVNPSE SGFVTLASME SGFVTNDIYE
     FSPDRMGRSK ESGWVENEIY Y
//
ID   DOCK2_MOUSE             Reviewed;        1828 AA.
AC   Q8C3J5; Q99M79;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   03-JUL-2003, sequence version 2.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Dedicator of cytokinesis protein 2;
DE   AltName: Full=Protein Hch;
GN   Name=Dock2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   MEDLINE=21410164; PubMed=11518968; DOI=10.1038/35090591;
RA   Fukui Y., Hashimoto O., Sanui T., Oono T., Koga H., Abe M.,
RA   Inayoshi A., Noda M., Oike M., Shirai T., Sasazuki T.;
RT   "Haematopoietic cell-specific CDM family protein DOCK2 is essential
RT   for lymphocyte migration.";
RL   Nature 412:826-831(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1501-1828.
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1704, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Involved in cytoskeletal rearrangements required for
CC       lymphocyte migration in response of chemokines. Activates RAC1 and
CC       RAC2 small GTPases, probably by functioning as a guanine
CC       nucleotide exchange factor (GEF), which exchanges bound GDP for
CC       free GTP. May participate in IL2 transcriptional activation via
CC       the activation of RAC2.
CC   -!- SUBUNIT: Interacts with RAC1 and RAC2. Interacts with CRKL and
CC       VAV. Interacts with CD3Z (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane
CC       protein (By similarity). Cytoplasm, cytoskeleton (By similarity).
CC       Note=Colocalizes with F-actin (By similarity).
CC   -!- TISSUE SPECIFICITY: Specifically expressed in hematopoietic cells.
CC   -!- DOMAIN: The DHR-2 domain probably mediates the GEF activity (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the DOCK family.
CC   -!- SIMILARITY: Contains 1 DHR-1 (CZH-1) domain.
CC   -!- SIMILARITY: Contains 1 DHR-2 (CZH-2) domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; AY027438; AAK13045.1; -; mRNA.
DR   EMBL; AK085708; BAC39514.2; -; mRNA.
DR   IPI; IPI00117274; -.
DR   RefSeq; NP_203538.2; NM_033374.2.
DR   UniGene; Mm.380679; -.
DR   ProteinModelPortal; Q8C3J5; -.
DR   SMR; Q8C3J5; 1-167, 423-609.
DR   IntAct; Q8C3J5; 3.
DR   STRING; Q8C3J5; -.
DR   PhosphoSite; Q8C3J5; -.
DR   PRIDE; Q8C3J5; -.
DR   Ensembl; ENSMUST00000093193; ENSMUSP00000090884; ENSMUSG00000020143.
DR   GeneID; 94176; -.
DR   KEGG; mmu:94176; -.
DR   CTD; 94176; -.
DR   MGI; MGI:2149010; Dock2.
DR   GeneTree; ENSGT00590000083047; -.
DR   HOGENOM; HBG356771; -.
DR   HOVERGEN; HBG051389; -.
DR   InParanoid; Q8C3J5; -.
DR   OrthoDB; EOG4MW855; -.
DR   NextBio; 352121; -.
DR   ArrayExpress; Q8C3J5; -.
DR   Bgee; Q8C3J5; -.
DR   CleanEx; MM_DOCK2; -.
DR   Genevestigator; Q8C3J5; -.
DR   GermOnline; ENSMUSG00000020143; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0051020; F:GTPase binding; IEA:InterPro.
DR   GO; GO:0030675; F:Rac GTPase activator activity; IMP:MGI.
DR   GO; GO:0030676; F:Rac guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0042608; F:T cell receptor binding; ISS:UniProtKB.
DR   GO; GO:0046633; P:alpha-beta T cell proliferation; IMP:MGI.
DR   GO; GO:0006935; P:chemotaxis; IMP:MGI.
DR   GO; GO:0007010; P:cytoskeleton organization; IDA:MGI.
DR   GO; GO:0001768; P:establishment of T cell polarity; IMP:MGI.
DR   GO; GO:0001771; P:immunological synapse formation; IMP:MGI.
DR   GO; GO:0001766; P:membrane raft polarization; IMP:MGI.
DR   GO; GO:0045060; P:negative thymic T cell selection; IMP:MGI.
DR   GO; GO:0035022; P:positive regulation of Rac protein signal transduction; IC:MGI.
DR   GO; GO:0045059; P:positive thymic T cell selection; IMP:MGI.
DR   InterPro; IPR010703; DOCK.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF06920; Ded_cyto; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Cytoskeleton;
KW   Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW   SH3 domain.
FT   CHAIN         1   1828       Dedicator of cytokinesis protein 2.
FT                                /FTId=PRO_0000189987.
FT   DOMAIN        8     69       SH3.
FT   DOMAIN      420    662       DHR-1.
FT   DOMAIN     1114   1620       DHR-2.
FT   MOD_RES      67     67       N6-acetyllysine (By similarity).
FT   MOD_RES     209    209       Phosphotyrosine (By similarity).
FT   MOD_RES     212    212       Phosphotyrosine (By similarity).
FT   MOD_RES     304    304       N6-acetyllysine (By similarity).
FT   MOD_RES     588    588       Phosphoserine (By similarity).
FT   MOD_RES     593    593       Phosphoserine (By similarity).
FT   MOD_RES     738    738       N6-acetyllysine (By similarity).
FT   MOD_RES    1057   1057       N6-acetyllysine (By similarity).
FT   MOD_RES    1683   1683       Phosphoserine (By similarity).
FT   MOD_RES    1704   1704       Phosphoserine.
FT   MOD_RES    1729   1729       Phosphoserine (By similarity).
FT   CONFLICT   1722   1722       S -> F (in Ref. 2; BAC39514).
SQ   SEQUENCE   1828 AA;  211734 MW;  A1C4720290BEB1DD CRC64;
     MAPWRKTDKE RHGVAIYNFQ GSEAQHLTLQ IGDVVRIQET CGDWYRGYLI KHKLSQGIFP
     TSFIHLKEVT VEKRRNIENI IPAEIPLAQE VTTTLWEWGS IWKQLYVASK KERFLQVQSM
     MYDLMEWRSQ LLSGTLPKDE LKELKQKVTS KIDYGNKILE LDLIVRDEDG NILDPDKTSV
     ISLFHAHEEA TYKITERIKE EMSKDQPDYG VYSRISSSPT HSLYVFVRNF VCRIGEDAEL
     FMSLYDPHKQ TVISENYLVR WGSKGFPKEI EMLNNLKVVF TDLGNKDLNR DKIFLICQIV
     RIGKMDLKDI NAKKCTQGLR RPFGVAVMDI TDIIKGKAES DEEKQHFIPF HPVSAENDFL
     HSLLGKVIAS KGDSGGQGLW VTMKMLVGDI IQIRKDYPHL VDRTTVVARK LGFPEIIMPG
     DVRNDIYITL LQGDFDKYTK TTQRNVEVIM CVCTEDGKVL PNAICVGAGD KAMNEYHSVV
     YYQVKQPRWM ETVKVAVPIE DMQRIHLRFM FRHRSSLESK DKGEKNFAMS YVKLMKEDGT
     TLHDGYHELV VLKGDSKKME DASAYLTLPS YRHPVENKGA TLSRSSSSVG GLSVSSRDVF
     SISTLVCSTK LTQNVGLLGL LKWRMKPQLL QENLEKLKIV DGEEVVKFLQ DTLDALFNIM
     MEHSQSNEYD ILVFDALIYI IGLIADRKFQ HFNTVLEAYI QQHFSATLAY KKLMTVLKTY
     LDTSSRGEQC EPILRTLKAL EYVFKFIVRS RTLFSQLYEG KEQMEFEESM RRLFESINNL
     MKSQYKTTIL LQVAALKYIP SVLHDVETVF DAKLLSQLLY EFYTCIPPVK LQKQKVQSMN
     EIVQSNLFKK QECRDILLPV ITKELKELLE QRDDGQHQAE KKHCVELLNS ILEVLSCQDA
     AFTYDHIQEI MVQLLRTVNR TVITMGRDHA LISHFEACMT AILDQMGDQH YSFYIETFQT
     SSDLVDFLME TFIMFKDLIG KNVYPGDWMA MSMVQNRVFL RAINKFAETM NQKFLEHTSF
     EFQLWNNYFH LAVAFITQDS LQLEQFTHAK YNKILNKYGD MRRLIGFSIR DMWYKLGQNK
     ICFIPGMVGP ILEMTLIPEA ELRKATIPIF FDMMLCEYQR TGAFKKFENE IILKLDHEVE
     GGRGDEQYMQ LLESILMECT AEHPTIAKSV ENFVSLVKGL LEKLLDYRGV MTDESKDNRM
     SCTVNLLNFY KDNNREEMYI RYLYKLRDLH LDCENYTEAA YTLLLHTWLL KWSDEQCASQ
     VMQTGQQHPQ THRQLKETLY ETIIGYFDKG KMWEEAISLC KELAEQYEME IFDYELLSQN
     LTQQAKFYEN IMKILRTKPD YFAVGYYGQG FPSFLRNKVF IYRGKEYERR EDFQMQLLSQ
     FPNAEKMNTT SAPGDDVRNA PGQYIQCFTV QPVLDEHPRF KNKPVPDQII NFYKSNYVQK
     FHYSRPVRRG KVDPENEFAS MWIERTSFLT AYKLPGILRW FEVVHMSQTT ISPLENAIET
     MSTVNEKILM MINQYQSDES LPINPLSMLL NGIVDPAVMG GFAKYEKAFF TEEYSREHPE
     DQDKLSHLKD LIAWQIPFLG AGIKIHEKRV SDNLRPFHDR MEECFKNLKM KVEKEYGVRE
     MPDFEDRRVG RPRSMLRSYR QMSVISLASM HSDCSTPSKV PAESFDLESA PPKTPKVEEE
     PISPGSTLPE VKLRRSKKRT KRSSVVFADE KAATESDLKR LSRKQEFMSD TNLSEHAAIP
     ARVSILSQMS FASQSMPTIP ALTLSVAGVP GLDEANTSPR LSQTFFQVSD GDKKTLKKKK
     VNQFFKTMLA SKSSEESKQI PDFLSTNM
//
ID   SHSA7_MOUSE             Reviewed;         558 AA.
AC   Q8C3Q5; Q3UMB3;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 3.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Protein shisa-7;
DE   AltName: Full=Protein shisa-6-like;
DE   Flags: Precursor;
GN   Name=Shisa7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-558 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 184-558 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Lung, and Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-532, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-354, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8C3Q5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C3Q5-2; Sequence=VSP_034790;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the shisa family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC39371.1; Type=Erroneous initiation;
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DR   EMBL; AC162034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK085127; BAC39371.1; ALT_INIT; mRNA.
DR   EMBL; AK145016; BAE26185.1; -; mRNA.
DR   IPI; IPI00225153; -.
DR   IPI; IPI00880347; -.
DR   RefSeq; NP_766325.3; NM_172737.4.
DR   UniGene; Mm.44666; -.
DR   PhosphoSite; Q8C3Q5; -.
DR   Ensembl; ENSMUST00000066041; ENSMUSP00000064886; ENSMUSG00000053550.
DR   GeneID; 232813; -.
DR   KEGG; mmu:232813; -.
DR   UCSC; uc009eyu.1; mouse.
DR   CTD; 232813; -.
DR   MGI; MGI:3605641; Shisa7.
DR   eggNOG; maNOG18954; -.
DR   GeneTree; ENSGT00510000047247; -.
DR   HOGENOM; HBG444407; -.
DR   HOVERGEN; HBG108632; -.
DR   InParanoid; Q8C3Q5; -.
DR   NextBio; 381250; -.
DR   ArrayExpress; Q8C3Q5; -.
DR   Bgee; Q8C3Q5; -.
DR   Genevestigator; Q8C3Q5; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Alternative splicing; Glycoprotein; Membrane; Phosphoprotein; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     22       Potential.
FT   CHAIN        23    558       Protein shisa-7.
FT                                /FTId=PRO_0000344473.
FT   TOPO_DOM     23    189       Extracellular (Potential).
FT   TRANSMEM    190    210       Helical; (Potential).
FT   TOPO_DOM    211    558       Cytoplasmic (Potential).
FT   COMPBIAS    148    186       Gly-rich.
FT   MOD_RES     354    354       Phosphotyrosine.
FT   MOD_RES     532    532       Phosphothreonine.
FT   CARBOHYD     26     26       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     280    296       Missing (in isoform 2).
FT                                /FTId=VSP_034790.
FT   CONFLICT    202    202       V -> M (in Ref. 1; BAC39371).
SQ   SEQUENCE   558 AA;  58334 MW;  BEDD9B53CE4C8D71 CRC64;
     MPALLLLGTV ALLASAAGPA GARPSNDTSS VAPGPLPALL AHLRRLTGAL AGGGSAAGTS
     ANATKTSPAS GTGAAARAPP PAELCHGYYD VMGQYDATFN CSTGSYRFCC GTCHYRFCCE
     HRHMRLAQAS CSNYDTPRWA TTPPPLAGGA GGAGGAGGGP GPGQAGWLEG GRAGGAGGRG
     GEGPGGSTAY VVCGVISFAL AVGVGAKVAF SKASRAPRAH REINVPRALV DILRHQAGPA
     TRPDRARSSS LTPGLGGPDS MAPRTPKNLY NTMKPSNLDN LHYNVNSPKH HAATLDWRAM
     PPPSPSLHYS TLSCSRSFHN LSHLPPSYEA AVKSELNRYS SLKRLAEKDL DEAYLKRRQL
     EMPRGTLPLH ALRRPGTGGG YRMDGWGGPE ELGLAPAPNP RRVMSQEHLL GDGSRASRYE
     FTLPRARLVS QEHLLLSSPE ALRQSREHLL SPPRSPALPP DPTTRASLAA SHSNLLLGPG
     GPPTPLHGLP PSGLHAHHHH ALHGSPQPAW MSDAGGGGGT LARRPPFQRQ GTLEQLQFIP
     GHHLPQHLRT ASKNEVTV
//
ID   CA198_MOUSE             Reviewed;         322 AA.
AC   Q8C3W1; Q3TCS2; Q3U2K7; Q3U3E1; Q6PDM3;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Uncharacterized protein C1orf198 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
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DR   EMBL; AK084773; BAC39275.1; -; mRNA.
DR   EMBL; AK154813; BAE32847.1; -; mRNA.
DR   EMBL; AK155222; BAE33133.1; -; mRNA.
DR   EMBL; AK170562; BAE41883.1; -; mRNA.
DR   EMBL; BC058626; AAH58626.1; -; mRNA.
DR   IPI; IPI00225267; -.
DR   RefSeq; NP_780358.3; NM_175149.4.
DR   UniGene; Mm.261920; -.
DR   ProteinModelPortal; Q8C3W1; -.
DR   PhosphoSite; Q8C3W1; -.
DR   PRIDE; Q8C3W1; -.
DR   Ensembl; ENSMUST00000034464; ENSMUSP00000034464; ENSMUSG00000031983.
DR   GeneID; 69551; -.
DR   KEGG; mmu:69551; -.
DR   UCSC; uc009nxg.1; mouse.
DR   MGI; MGI:1916801; 2310022B05Rik.
DR   eggNOG; roNOG09125; -.
DR   GeneTree; ENSGT00390000018361; -.
DR   HOGENOM; HBG713749; -.
DR   HOVERGEN; HBG080980; -.
DR   InParanoid; Q8C3W1; -.
DR   OMA; PPAQQDE; -.
DR   OrthoDB; EOG40ZQZ5; -.
DR   PhylomeDB; Q8C3W1; -.
DR   NextBio; 329760; -.
DR   ArrayExpress; Q8C3W1; -.
DR   Bgee; Q8C3W1; -.
DR   CleanEx; MM_2310022B05RIK; -.
DR   Genevestigator; Q8C3W1; -.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    322       Uncharacterized protein C1orf198 homolog.
FT                                /FTId=PRO_0000280343.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      37     37       Phosphoserine (By similarity).
FT   MOD_RES     278    278       Phosphoserine.
FT   CONFLICT     52     52       E -> D (in Ref. 2; AAH58626).
FT   CONFLICT     78     78       R -> H (in Ref. 1; BAE33133).
FT   CONFLICT     85     85       D -> E (in Ref. 1; BAE32847).
SQ   SEQUENCE   322 AA;  35316 MW;  2C0D2A472BE73284 CRC64;
     MASMAAAIAA SRSAVMSGNR PLDDRERKRF TYFSSLSPMA RKIMQDKEKI REKYGPEWAR
     LPPAQQDEII DRCLVGPRAP AAAADAGDVR DPARFPGLRG PTGQKLVRFG DEDITWQDEH
     SAPFSWETRS QMEFSISSLS IQEPSAATVT SDARSLAKAP QGTQGSKPAQ SSRSSSLDAL
     GPARKEEEAP FWKINAERSR EGPEAEFQSL TPSQIKSMEK GEKVLPACYR QEPTTKDREA
     KPVPQEQQTL PSVSAEQEVP QPVQAPASLL PKATPTESPE KPPPPAVQRD EDDDALFSEP
     ALAQISSSNV LLKTGFDFLD NW
//
ID   GP158_MOUSE             Reviewed;        1200 AA.
AC   Q8C419; Q8CHB0;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Probable G-protein coupled receptor 158;
DE   Flags: Precursor;
GN   Name=Gpr158; Synonyms=Kiaa1136;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-724.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 70-1200.
RC   TISSUE=Brain;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-904 AND SER-976, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Orphan receptor.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
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DR   EMBL; AK083234; BAC38819.1; -; mRNA.
DR   EMBL; AB093287; BAC41471.1; -; mRNA.
DR   IPI; IPI00465871; -.
DR   RefSeq; NP_001004761.1; NM_001004761.1.
DR   UniGene; Mm.166647; -.
DR   ProteinModelPortal; Q8C419; -.
DR   STRING; Q8C419; -.
DR   PhosphoSite; Q8C419; -.
DR   PRIDE; Q8C419; -.
DR   Ensembl; ENSMUST00000055946; ENSMUSP00000049708; ENSMUSG00000045967.
DR   GeneID; 241263; -.
DR   KEGG; mmu:241263; -.
DR   UCSC; uc008inf.1; mouse.
DR   CTD; 241263; -.
DR   MGI; MGI:2441697; Gpr158.
DR   GeneTree; ENSGT00390000010934; -.
DR   HOGENOM; HBG445867; -.
DR   HOVERGEN; HBG080352; -.
DR   InParanoid; Q8C419; -.
DR   OMA; TYDHVRD; -.
DR   OrthoDB; EOG4SBDX6; -.
DR   PhylomeDB; Q8C419; -.
DR   NextBio; 384949; -.
DR   ArrayExpress; Q8C419; -.
DR   Bgee; Q8C419; -.
DR   CleanEx; MM_GPR158; -.
DR   Genevestigator; Q8C419; -.
DR   GermOnline; ENSMUSG00000045967; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR017978; GPCR_3_C.
DR   Pfam; PF00003; 7tm_3; 1.
DR   PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; FALSE_NEG.
DR   PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; FALSE_NEG.
DR   PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; FALSE_NEG.
DR   PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein;
KW   Isopeptide bond; Membrane; Phosphoprotein; Receptor; Signal;
KW   Transducer; Transmembrane; Transmembrane helix; Ubl conjugation.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25   1200       Probable G-protein coupled receptor 158.
FT                                /FTId=PRO_0000012970.
FT   TOPO_DOM     25    417       Extracellular (Potential).
FT   TRANSMEM    418    438       Helical; Name=1; (Potential).
FT   TOPO_DOM    439    451       Cytoplasmic (Potential).
FT   TRANSMEM    452    472       Helical; Name=2; (Potential).
FT   TOPO_DOM    473    483       Extracellular (Potential).
FT   TRANSMEM    484    506       Helical; Name=3; (Potential).
FT   TOPO_DOM    507    528       Cytoplasmic (Potential).
FT   TRANSMEM    529    549       Helical; Name=4; (Potential).
FT   TOPO_DOM    550    579       Extracellular (Potential).
FT   TRANSMEM    580    600       Helical; Name=5; (Potential).
FT   TOPO_DOM    601    613       Cytoplasmic (Potential).
FT   TRANSMEM    614    634       Helical; Name=6; (Potential).
FT   TOPO_DOM    635    643       Extracellular (Potential).
FT   TRANSMEM    644    664       Helical; Name=7; (Potential).
FT   TOPO_DOM    665   1200       Cytoplasmic (Potential).
FT   MOD_RES     904    904       Phosphoserine.
FT   MOD_RES     976    976       Phosphoserine.
FT   CARBOHYD     98     98       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    143    143       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    215    215       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    274    274       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    333    333       N-linked (GlcNAc...) (Potential).
FT   CROSSLNK    774    774       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
SQ   SEQUENCE   1200 AA;  134426 MW;  2FCEF8283DE964B4 CRC64;
     MGAMAYSLLF CLLLAHLGLG EVGASLDPPG RPDSPRERTP RGKQHGQQLP RASAPDPSIP
     WSRSTDGTIL AQKLAEEVPV DVASYLYTGD FHQLKRANCS GRYELAGLPG KSPSLASSHP
     SLHGALDTLT HATNFLNMML QSNKSREQTV QDDLQWYQAL VRSLLEGEPS ISRAAITFST
     ESLSTPAPQV FLQATREESR ILLQDLSSSA HHLANATLET EWFHGLRRKW RPHLHRRGSN
     QGPRGLGHSW RRRDGLGGDR SHVKWSPPYL ECENGSYKPG WLVTLSAAFY GLQPNLVPEF
     RGVMKVDISL QKVDIDQCSS DGWFSGTHKC HLNNSECMPI KGLGFVLGAY QCICKAGFYH
     PRVFSVNNFQ RRGPDHHFSG STKDVSEETH VCLPCREGCP FCADDRPCFV QEDKYLRLAI
     ISFQALCMLL DFVSMLVVYH FRKAKSIRAS GLILLETILF GSLLLYFPVV ILYFEPSTFR
     CILLRWARLL GFATVYGTVT LKLHRVLKVF LSRTAQRIPY MTGGRVMRML AVIVLVVFWF
     LVGWTSSMCQ NLERDILLVG QGQTSDHLTF NMCLIDRWDY MTAVAEFLFL LWGIYLCYAV
     RTVPSAFHEP RYMAVAVHNE LIITAIFHTI RFVLASRLQP DWMLMLYFAH AHLTVTVTIG
     LLLIPKFSHS SNNPRDDIAT EAYEDELDMG RSGSYLNSSI NSAWSEHSLD PEDIRDELKK
     LYAQLEIYKR KKMITNNPHL QKKRCSKKGL GRSIMRRITE IPETVSRQCS KEDKEGTDHS
     AAKGTGLVRK NPTESSGNTG RPKEESLKNR VFSLKKSHST YDHVRDQTVE SSSLPMESQE
     EEATENSTLE SLSSKKLTQK LKEDSEAEST ESVPLVCKSA SAHNLSSEKK PGHPRTSMLQ
     KSLSVIASAK EKTLGLAGKT QTLVMEDRAK SQKPKDRETI RKYSNSDNVE TIPNSGHMEE
     PRKPQKSGIM KQQRVSLPTA NPDVSSGITQ IKDNFDIGEV CPWEVYDLTP GPMPSEPKAQ
     KHVSIAASEV EQNPASFLKE KSYHKSKATE GLYQANHKSI DKTEVCPWEI HSQSLLEDEN
     RLISKTPVLP GRAREENGSQ LYTTNMCAGQ YEELPHKVVA PKVENENLNQ MGDQEKQTSS
     SVDIIPGSCN SSNNSHQPLT SRAEVCPWEF EPLEQPNAER SVTLPASSAL SANKIPGPQK
//
ID   PEX5R_MOUSE             Reviewed;         567 AA.
AC   Q8C437; Q8CA31; Q9DAA1; Q9JMB9;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=PEX5-related protein;
DE   AltName: Full=PEX2-related protein;
DE   AltName: Full=PEX5-like protein;
DE   AltName: Full=Peroxin-5-related protein;
DE            Short=Pex5Rp;
GN   Name=Pex5l; Synonyms=Pex2, Pex5r, Pxr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RA   Sano H., Snider J., Ohta M.;
RT   "A novel peroxisomal targeting signal 1 receptor-like gene, PXR2,
RT   preferentially expressed in brain.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SUBUNIT: Interacts with RAB8B (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane;
CC       Peripheral membrane protein (By similarity). Note=Some fraction is
CC       membrane associated via its interaction with RAB8B (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8C437-1; Sequence=Displayed;
CC       Name=3;
CC         IsoId=Q8C437-3; Sequence=VSP_010439;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q8C437-4; Sequence=VSP_010437;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the peroxisomal targeting signal receptor
CC       family.
CC   -!- SIMILARITY: Contains 5 TPR repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC38781.1; Type=Erroneous initiation;
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DR   EMBL; AB032591; BAA92877.1; -; mRNA.
DR   EMBL; AK006035; BAB24376.1; -; mRNA.
DR   EMBL; AK083141; BAC38781.1; ALT_INIT; mRNA.
DR   IPI; IPI00125412; -.
DR   IPI; IPI00282186; -.
DR   IPI; IPI00416130; -.
DR   RefSeq; NP_001156988.1; NM_001163516.1.
DR   RefSeq; NP_001156989.1; NM_001163517.1.
DR   UniGene; Mm.151332; -.
DR   ProteinModelPortal; Q8C437; -.
DR   SMR; Q8C437; 193-566.
DR   STRING; Q8C437; -.
DR   PhosphoSite; Q8C437; -.
DR   PRIDE; Q8C437; -.
DR   Ensembl; ENSMUST00000078226; ENSMUSP00000077353; ENSMUSG00000027674.
DR   Ensembl; ENSMUST00000108225; ENSMUSP00000103860; ENSMUSG00000027674.
DR   Ensembl; ENSMUST00000108226; ENSMUSP00000103861; ENSMUSG00000027674.
DR   GeneID; 58869; -.
DR   KEGG; mmu:58869; -.
DR   UCSC; uc008owt.1; mouse.
DR   UCSC; uc008owu.1; mouse.
DR   UCSC; uc008owv.1; mouse.
DR   CTD; 58869; -.
DR   MGI; MGI:1916672; Pex5l.
DR   eggNOG; roNOG08834; -.
DR   GeneTree; ENSGT00390000013941; -.
DR   HOVERGEN; HBG053575; -.
DR   OrthoDB; EOG4ZW59S; -.
DR   PhylomeDB; Q8C437; -.
DR   NextBio; 314436; -.
DR   ArrayExpress; Q8C437; -.
DR   Bgee; Q8C437; -.
DR   CleanEx; MM_PEX2; -.
DR   CleanEx; MM_PEX5L; -.
DR   Genevestigator; Q8C437; -.
DR   GermOnline; ENSMUSG00000027674; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045185; P:maintenance of protein location; IDA:MGI.
DR   GO; GO:0043949; P:regulation of cAMP-mediated signaling; ISS:UniProtKB.
DR   GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
DR   InterPro; IPR001440; TPR-1.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 2.
DR   Pfam; PF00515; TPR_1; 1.
DR   SMART; SM00028; TPR; 4.
DR   PROSITE; PS50005; TPR; 5.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Membrane; Phosphoprotein; Repeat;
KW   TPR repeat.
FT   CHAIN         1    567       PEX5-related protein.
FT                                /FTId=PRO_0000106318.
FT   REPEAT      301    334       TPR 1.
FT   REPEAT      336    368       TPR 2.
FT   REPEAT      415    448       TPR 3.
FT   REPEAT      450    482       TPR 4.
FT   REPEAT      484    516       TPR 5.
FT   MOD_RES     202    202       Phosphoserine.
FT   MOD_RES     388    388       Phosphoserine.
FT   VAR_SEQ       1    223       Missing (in isoform 4).
FT                                /FTId=VSP_010437.
FT   VAR_SEQ       1      6       MYQGHM -> MSDSEMDGRTHIPSLLNALLSRNRVMQMSYL
FT                                KSKEQGYGKLSSDEDLEIIVDQK (in isoform 3).
FT                                /FTId=VSP_010439.
FT   CONFLICT     62     62       P -> T (in Ref. 2).
FT   CONFLICT    564    564       N -> K (in Ref. 2; BAB24376).
SQ   SEQUENCE   567 AA;  63135 MW;  4955363C5A70FB28 CRC64;
     MYQGHMQLVN EQQESRPLLS PSIDDFLCET KSEAIAKPVT SNTAVLTTGL DLLDLSEPVS
     QPQTKAKKSE PSSKSSSLKK KADGSDLISA DAEQRAQALR GPETSSLDLD IQTQLEKWDD
     VKFHGDRTSK GHLMAERKSC SSRTGSKELL WSAEHRSQPE LSTGKSALNS ESASELELVA
     PAQARLTKEH RWGSALLSRN HSLEEEFERA KAAVESDTEF WDKMQAEWEE MARRNWISEN
     QEAQNQVTVS ASEKGYYFHT ENPFKDWPGA FEEGLKRLKE GDLPVTILFM EAAILQDPGD
     AEAWQFLGIT QAENENEQAA IVALQRCLEL QPNNLKALMA LAVSYTNTSH QQDACEALKN
     WIKQNPKYKY LVKNKKGSPG LTRRMSKSPV DSSVLEGVKE LYLEAAHQNG DMIDPDLQTG
     LGVLFHLSGE FNRAIDAFNA ALTVRPEDYS LWNRLGATLA NGDRSEEAVE AYTRALEIQP
     GFIRSRYNLG ISCINLGAYR EAVSNFLTAL SLQRKSRNQQ QVPHPAISGN IWAALRIALS
     LMDQPELFQA ANLGDLDVLL RAFNLDP
//
ID   AIDA_MOUSE              Reviewed;         305 AA.
AC   Q8C4Q6; Q3U6V0; Q3UP85; Q6NXY2; Q6PG77; Q78W09; Q99K80;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Axin interactor, dorsalization-associated protein;
DE   AltName: Full=Axin interaction partner and dorsalization antagonist;
GN   Name=Aida;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Embryo, Head, Inner ear, Placenta, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and Czech II;
RC   TISSUE=Brain, Embryonic germ cell, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   STRUCTURE BY NMR OF 1-115.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of four helical up-and-down bundle domain of the
RT   hypothetical protein 2610208m17RIK similar to the protein FLJ12806.";
RL   Submitted (AUG-2004) to the PDB data bank.
RN   [4]
RP   FUNCTION, AND INTERACTION WITH AXIN.
RX   PubMed=17681137; DOI=10.1016/j.devcel.2007.07.006;
RA   Rui Y., Xu Z., Xiong B., Cao Y., Lin S., Zhang M., Chan S.-C., Luo W.,
RA   Han Y., Lu Z., Ye Z., Zhou H.-M., Han J., Meng A., Lin S.-C.;
RT   "A beta-catenin-independent dorsalization pathway activated by
RT   Axin/JNK signaling and antagonized by aida.";
RL   Dev. Cell 13:268-282(2007).
CC   -!- FUNCTION: Acts as a ventralizing factor during embryogenesis (By
CC       similarity). Inhibits axin-mediated JNK activation by binding axin
CC       and disrupting axin homodimerization. This in turn antagonizes a
CC       Wnt/beta-catenin-independent dorsalization pathway activated by
CC       AXIN/JNK-signaling.
CC   -!- SUBUNIT: Interacts with AXIN1.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8C4Q6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C4Q6-2; Sequence=VSP_028323;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the AIDA family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK027971; BAC25682.1; -; mRNA.
DR   EMBL; AK081494; BAC38234.1; -; mRNA.
DR   EMBL; AK143716; BAE25512.1; -; mRNA.
DR   EMBL; AK149788; BAE29085.1; -; mRNA.
DR   EMBL; AK150639; BAE29727.1; -; mRNA.
DR   EMBL; AK150702; BAE29781.1; -; mRNA.
DR   EMBL; AK152961; BAE31624.1; -; mRNA.
DR   EMBL; AK153448; BAE32003.1; -; mRNA.
DR   EMBL; AK159318; BAE34985.1; -; mRNA.
DR   EMBL; AK167520; BAE39592.1; -; mRNA.
DR   EMBL; AK172451; BAE43012.1; -; mRNA.
DR   EMBL; AK158103; BAE34358.1; -; mRNA.
DR   EMBL; BC057183; AAH57183.1; -; mRNA.
DR   EMBL; BC066829; AAH66829.1; -; mRNA.
DR   EMBL; BC086763; AAH86763.1; -; mRNA.
DR   IPI; IPI00311123; -.
DR   IPI; IPI00664676; -.
DR   RefSeq; NP_859421.1; NM_181732.4.
DR   UniGene; Mm.290502; -.
DR   PDB; 1UG7; NMR; -; A=1-115.
DR   PDB; 2QZ5; X-ray; 2.60 A; A/B=151-305.
DR   PDBsum; 1UG7; -.
DR   PDBsum; 2QZ5; -.
DR   ProteinModelPortal; Q8C4Q6; -.
DR   SMR; Q8C4Q6; 3-115, 151-304.
DR   STRING; Q8C4Q6; -.
DR   PhosphoSite; Q8C4Q6; -.
DR   REPRODUCTION-2DPAGE; Q8C4Q6; -.
DR   PRIDE; Q8C4Q6; -.
DR   Ensembl; ENSMUST00000052053; ENSMUSP00000104794; ENSMUSG00000042901.
DR   Ensembl; ENSMUST00000109166; ENSMUSP00000104795; ENSMUSG00000042901.
DR   GeneID; 108909; -.
DR   KEGG; mmu:108909; -.
DR   CTD; 108909; -.
DR   MGI; MGI:1919737; Aida.
DR   eggNOG; roNOG06305; -.
DR   GeneTree; ENSGT00390000016465; -.
DR   HOVERGEN; HBG057354; -.
DR   InParanoid; Q8C4Q6; -.
DR   OMA; DVEIQRH; -.
DR   OrthoDB; EOG4640CJ; -.
DR   NextBio; 361453; -.
DR   Bgee; Q8C4Q6; -.
DR   Genevestigator; Q8C4Q6; -.
DR   GO; GO:0044444; C:cytoplasmic part; IDA:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; ISS:UniProtKB.
DR   GO; GO:0046329; P:negative regulation of JNK cascade; IMP:UniProtKB.
DR   GO; GO:0043508; P:negative regulation of JUN kinase activity; IDA:MGI.
DR   GO; GO:0043496; P:regulation of protein homodimerization activity; IMP:UniProtKB.
DR   InterPro; IPR015006; AIDA.
DR   InterPro; IPR023421; AIDA_N.
DR   Gene3D; G3DSA:1.20.120.360; G3DSA:1.20.120.360; 1.
DR   Pfam; PF08910; DUF1855; 1.
DR   SUPFAM; SSF109779; SSF109779; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil;
KW   Developmental protein.
FT   CHAIN         1    305       Axin interactor, dorsalization-associated
FT                                protein.
FT                                /FTId=PRO_0000305279.
FT   REGION      153    220       Axin-binding.
FT   COILED       27     62       Potential.
FT   VAR_SEQ     153    234       Missing (in isoform 2).
FT                                /FTId=VSP_028323.
FT   CONFLICT    138    138       G -> V (in Ref. 2; AAH66829).
FT   CONFLICT    171    171       R -> K (in Ref. 1; BAE31624).
FT   CONFLICT    231    231       R -> K (in Ref. 1; BAE34358).
FT   HELIX         4     25
FT   HELIX        28     46
FT   STRAND       49     51
FT   HELIX        57     78
FT   HELIX        89     92
FT   HELIX        94     99
FT   TURN        100    103
SQ   SEQUENCE   305 AA;  34888 MW;  A285C564AF5333D0 CRC64;
     MSEVTRSLLQ RWGASLRRGA DFDSWGQLVE AIDEYQILAR HLQKEAQAQH NNSEFTEEQK
     KTIGKIATCL ELRSAALQST QSQEEFKLED LKKLEPILKN ILTYNKEFPF DVQPIPLRRI
     LAPGEEENLE FEEDEEGGAG AGPPDSFSAR VPGTLLPRLP SEPGMTLLTI RIEKIGLKDA
     GQCIDPYITV SVKDLNGIDL TPVQDTPVAS RKEDTYVHFN VDIELQKHVE RLTKGAAIFF
     EFKHYKPKKR FTSTKCFAFM EMDEIKPGPI VIELYKKPTD FKRKKLQLLT KKPLYLHLHQ
     SLHKE
//
ID   DEN2A_MOUSE             Reviewed;        1000 AA.
AC   Q8C4S8; Q3TJU2; Q3TUG3; Q3UXA3;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=DENN domain-containing protein 2A;
GN   Name=Dennd2a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 210-217, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435 AND SER-441, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SIMILARITY: Contains 1 dDENN domain.
CC   -!- SIMILARITY: Contains 1 DENN domain.
CC   -!- SIMILARITY: Contains 1 uDENN domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE22660.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK081176; BAC38157.1; -; mRNA.
DR   EMBL; AK135781; BAE22660.1; ALT_INIT; mRNA.
DR   EMBL; AK160784; BAE36008.1; -; mRNA.
DR   EMBL; AK167298; BAE39403.1; -; mRNA.
DR   IPI; IPI00225616; -.
DR   RefSeq; NP_766065.1; NM_172477.4.
DR   UniGene; Mm.440021; -.
DR   ProteinModelPortal; Q8C4S8; -.
DR   PhosphoSite; Q8C4S8; -.
DR   PRIDE; Q8C4S8; -.
DR   Ensembl; ENSMUST00000036877; ENSMUSP00000045367; ENSMUSG00000038456.
DR   GeneID; 209773; -.
DR   KEGG; mmu:209773; -.
DR   UCSC; uc009blx.1; mouse.
DR   CTD; 209773; -.
DR   MGI; MGI:2444961; Dennd2a.
DR   eggNOG; roNOG13372; -.
DR   GeneTree; ENSGT00550000074339; -.
DR   HOGENOM; HBG715710; -.
DR   HOVERGEN; HBG079980; -.
DR   InParanoid; Q8C4S8; -.
DR   OMA; RFLRQME; -.
DR   OrthoDB; EOG4HT8RG; -.
DR   PhylomeDB; Q8C4S8; -.
DR   NextBio; 372792; -.
DR   ArrayExpress; Q8C4S8; -.
DR   Bgee; Q8C4S8; -.
DR   CleanEx; MM_DENND2A; -.
DR   Genevestigator; Q8C4S8; -.
DR   GermOnline; ENSMUSG00000038456; Mus musculus.
DR   InterPro; IPR005112; dDENN.
DR   InterPro; IPR001194; DENN.
DR   InterPro; IPR005113; uDENN.
DR   Pfam; PF03455; dDENN; 1.
DR   Pfam; PF02141; DENN; 1.
DR   Pfam; PF03456; uDENN; 1.
DR   SMART; SM00801; dDENN; 1.
DR   SMART; SM00799; DENN; 1.
DR   SMART; SM00800; uDENN; 1.
DR   PROSITE; PS50947; DDENN; 1.
DR   PROSITE; PS50211; DENN; 1.
DR   PROSITE; PS50946; UDENN; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Phosphoprotein.
FT   CHAIN         1   1000       DENN domain-containing protein 2A.
FT                                /FTId=PRO_0000242683.
FT   DOMAIN      570    646       UDENN.
FT   DOMAIN      653    837       DENN.
FT   DOMAIN      888    953       dDENN.
FT   COMPBIAS    249    306       Pro-rich.
FT   MOD_RES     435    435       Phosphoserine.
FT   MOD_RES     441    441       Phosphoserine.
FT   CONFLICT     67     67       K -> E (in Ref. 1; BAE36008).
FT   CONFLICT    122    122       Q -> L (in Ref. 1; BAE39403).
FT   CONFLICT    523    523       K -> E (in Ref. 1; BAE39403).
FT   CONFLICT    612    612       A -> V (in Ref. 1; BAE22660).
FT   CONFLICT    620    620       E -> G (in Ref. 1; BAE39403).
FT   CONFLICT    698    698       A -> P (in Ref. 1; BAE22660).
SQ   SEQUENCE   1000 AA;  113094 MW;  8866696B3B25303B CRC64;
     MLEARVDMLS SNMIISGPAA DLGAKEASRP WKKQLNSVPN SGPSARARAQ PQPLSIKDKI
     SKWEGKKEPP ASDPARQTDG QEDHLPSCKV ERRGSELTRT KNGMRLETER LQNDSRARTV
     CQDTEQLPGP RPIDGQPELS QHRGRELKPS DLRFQSDHLS VLRQVKRLEK ALKDGSAGLD
     PQMPGTCYSP HCLPDKTEED LPSLESHEKG GVLAAGRRAH HLEVREPGPE ISEDWKGQES
     VYRGSRWYPP KPFINPVPKP RRTFKHAGEG DKDVSPGISF KKEKRNLPPL PSLPPPPPPL
     PSSPPPTSVN RRLWTGRQRP SADHRKSYEF EDLLQSSSEN SRVDWYAQTK LGLTRTLSEE
     NVYEDILDPP MKENPYEDVE LHGRCLGKKC VLTFPASPTS SIPDTSTKQS LSKSAFFRQN
     SERRNLKLLD TRKLSRDGAG SPLRTSPPST PSSPDDTFFN LGDLQNGRKK KKIPRLVLRI
     NAIYEARRGK KRVKRLSQST ESNSGKVTDE NSESDSDTEE KLKAHSQRLV NVKSRLKQAP
     RYSSLDRDLI EYQERQLFEY FVVVSLHKKQ AGAAYVPELT QQFPLKLEKS FKFMREAEDQ
     LKAIPQFCFP DAKDWAPVQE FTSETFSFVL TGEDGSRRFG YCRRLLPGGK GKRLPEVYCI
     VSRLGCFSLF SKILDEVEKR RGISPALVQP LMRSVMEAPF PALGKTIIVK NFLPGSGTEV
     IELCRPLDSR LEHVDFESLF SSLSVRHLVS VFASLLLERR VIFIADKLST LSKCCHAMVA
     LIYPFSWQHT YIPVLPPAMI DIVCSPTPFL IGLLSSSLPL LRELPLEEVL VVDLINDRFL
     RQMEDEDSIL PRKLQVALEH ILEQRNDLAC DQDGGPLDCV HGPESSSLSE VVSEAFVRFF
     VEIVGHYPLF LTSGEERSLQ REAFRKAVSS KSLRRFLEVF METQTFRGFI QERELRRQDA
     KGLFEVRAQE YLETLPSGEH SGVNKFLKGL GNKMKFLHKK
//
ID   TM145_MOUSE             Reviewed;         746 AA.
AC   Q8C4U2;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 48.
DE   RecName: Full=Transmembrane protein 145;
GN   Name=Tmem145;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK081054; BAC38124.1; -; mRNA.
DR   IPI; IPI00225646; -.
DR   RefSeq; NP_899134.2; NM_183311.2.
DR   UniGene; Mm.260740; -.
DR   PhosphoSite; Q8C4U2; -.
DR   PRIDE; Q8C4U2; -.
DR   Ensembl; ENSMUST00000058863; ENSMUSP00000059231; ENSMUSG00000043843.
DR   GeneID; 330485; -.
DR   KEGG; mmu:330485; -.
DR   CTD; 330485; -.
DR   MGI; MGI:3607779; Tmem145.
DR   eggNOG; roNOG07942; -.
DR   GeneTree; ENSGT00510000048317; -.
DR   HOGENOM; HBG506002; -.
DR   HOVERGEN; HBG094058; -.
DR   InParanoid; Q8C4U2; -.
DR   NextBio; 399407; -.
DR   ArrayExpress; Q8C4U2; -.
DR   Bgee; Q8C4U2; -.
DR   CleanEx; MM_TMEM145; -.
DR   Genevestigator; Q8C4U2; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR019336; Rhodopsin-like_GPCR_TM_domain.
DR   Pfam; PF10192; GpcrRhopsn4; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    746       Transmembrane protein 145.
FT                                /FTId=PRO_0000280356.
FT   TRANSMEM      9     29       Helical; (Potential).
FT   TRANSMEM    189    209       Helical; (Potential).
FT   TRANSMEM    221    241       Helical; (Potential).
FT   TRANSMEM    255    275       Helical; (Potential).
FT   TRANSMEM    296    316       Helical; (Potential).
FT   TRANSMEM    332    352       Helical; (Potential).
FT   TRANSMEM    363    383       Helical; (Potential).
FT   TRANSMEM    395    415       Helical; (Potential).
FT   MOD_RES     511    511       Phosphoserine.
FT   CARBOHYD     35     35       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    250    250       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    458    458       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   746 AA;  82473 MW;  E4BF8600F35CF733 CRC64;
     MEPSRAPVLG RLLPPLLLLL LPLYPRTRAK YVRGNLSSKE DWVFLTRFCF LSDYGRLDFR
     FRYPEAKCCQ NILLYFDDPS QWPAVYKARD KDCLAKESVI RPENNQVINL TTQYAWSGCQ
     VVSEEGTRYL SCSSGRSFRS VRERWWYIAL SKCGGDGLQL EYEMVLTNGK SFWTRHFSAD
     EFGILETDVT FLLIFTLIFV LSCYFGYLLK GRQLLHTTYK MFMAAAGVEV LSLLFFCIYW
     GQYATDGIGN GSVKILAKLL FSSSFLIFLL TLILLGKGFT VTRGRISHSG SVKLSVYMTL
     YTLTHVVLLI YEAEFFDPGQ VLYTYESPAG YGLIGLQVAA YVWFCYAVLV SLRHYPEKQP
     FYVPFFAAYT LWFFAVPVMA LIANFGIPKW AREKIVNGIQ LGIHLYAHGV FLIMTRPSAA
     NKNFPYHVRT SQIASAGVPG PGGSQSADKA FPQHVYGNVT FISDSVPNFT ELFSIPPPTS
     SAGKQVEETA VAAAVAPRGR VVTMAEPGAA SPPPPARFSK AVHSGWDGPT PSYQPLVPPE
     QRRGKPASPN TSACTQPGAL HPRSEHPFPA SAPRAAHRAP AGLRNPVSLP AQGLGHARHP
     APLPHPAPTL DALRPAPFPL VPNGPAGAVL RVPSLSPCPE WLRNLDSRCS VISAPLTPFE
     TSDPAGLRNT RDDRLDPARP SRTLRPSSHC LETDIVKLVS TLKPSLGFVT SDLCFVRPSE
     CQGPSHGLWQ KDVFSSCQNK EDSLSF
//
ID   KC1G3_MOUSE             Reviewed;         424 AA.
AC   Q8C4X2; Q8BM57; Q8C001; Q8K079;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Casein kinase I isoform gamma-3;
DE            Short=CKI-gamma 3;
DE            EC=2.7.11.1;
GN   Name=Csnk1g3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-210 AND 238-424.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryoid bodies;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-210.
RC   TISSUE=Melanocyte;
RX   PubMed=15782199; DOI=10.1038/nmeth719;
RA   Watahiki A., Waki K., Hayatsu N., Shiraki T., Kondo S., Nakamura M.,
RA   Sasaki D., Arakawa T., Kawai J., Harbers M., Hayashizaki Y.,
RA   Carninci P.;
RT   "Libraries enriched for alternatively spliced exons reveal splicing
RT   patterns in melanocytes and melanomas.";
RL   Nat. Methods 1:233-239(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-424.
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Casein kinases are operationally defined by their
CC       preferential utilization of acidic proteins such as caseins as
CC       substrates. It can phosphorylate a large number of proteins.
CC       Participates in Wnt signaling (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- PTM: Autophosphorylated (By similarity).
CC   -!- MISCELLANEOUS: Triazolodiamine 1 is a commercial name for 5-amino-
CC       3-([4-(aminosulfonyl)phenyl]amino)-N-(2,6-difluorophenyl)-1H-
CC       1,2,4-triazole-1-carbothioamide.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC       protein kinase family. Casein kinase I subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AC115124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC127368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK032675; BAC27983.1; -; mRNA.
DR   EMBL; AK034842; BAC28850.1; -; mRNA.
DR   EMBL; AK080491; BAC37932.1; -; mRNA.
DR   EMBL; AK218008; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC033601; AAH33601.2; -; mRNA.
DR   IPI; IPI00169513; -.
DR   RefSeq; NP_690022.2; NM_152809.2.
DR   UniGene; Mm.368668; -.
DR   HSSP; Q9Y6M4; 2CHL.
DR   ProteinModelPortal; Q8C4X2; -.
DR   SMR; Q8C4X2; 36-335.
DR   PhosphoSite; Q8C4X2; -.
DR   PRIDE; Q8C4X2; -.
DR   Ensembl; ENSMUST00000069597; ENSMUSP00000070259; ENSMUSG00000073563.
DR   GeneID; 70425; -.
DR   KEGG; mmu:70425; -.
DR   CTD; 70425; -.
DR   MGI; MGI:1917675; Csnk1g3.
DR   eggNOG; maNOG10143; -.
DR   GeneTree; ENSGT00560000076651; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG000176; -.
DR   InParanoid; Q8C4X2; -.
DR   OMA; NREAHPH; -.
DR   OrthoDB; EOG4GHZP4; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 460950; -.
DR   ArrayExpress; Q8C4X2; -.
DR   Bgee; Q8C4X2; -.
DR   CleanEx; MM_CSNK1G3; -.
DR   Genevestigator; Q8C4X2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR022247; Casein_kinase-1_gamma_C.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   Pfam; PF12605; CK1gamma_C; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.
FT   CHAIN         1    424       Casein kinase I isoform gamma-3.
FT                                /FTId=PRO_0000305924.
FT   DOMAIN       43    313       Protein kinase.
FT   NP_BIND      49     57       ATP (By similarity).
FT   COMPBIAS     31     34       Poly-Ser.
FT   ACT_SITE    162    162       Proton acceptor (By similarity).
FT   BINDING      72     72       ATP (By similarity).
FT   BINDING     117    117       Inhibitor triazolodiamine 1; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING     119    119       Inhibitor triazolodiamine 1; via amide
FT                                nitrogen and carbonyl oxygen (By
FT                                similarity).
FT   MOD_RES      29     29       Phosphothreonine (By similarity).
FT   MOD_RES      32     32       Phosphoserine (By similarity).
FT   MOD_RES     256    256       Phosphothreonine (By similarity).
FT   MOD_RES     345    345       Phosphoserine (By similarity).
FT   MOD_RES     366    366       Phosphoserine (By similarity).
FT   MOD_RES     367    367       Phosphoserine (By similarity).
FT   MOD_RES     368    368       Phosphothreonine (By similarity).
FT   MOD_RES     382    382       Phosphoserine (By similarity).
FT   CONFLICT     62     84       NLYTNEYVAIKLEPMKSRAPQLH -> IVLFIPLCEEQFKN
FT                                EYTCKRVFL (in Ref. 2; BAC37932).
FT   CONFLICT    119    119       L -> V (in Ref. 2).
FT   CONFLICT    138    138       T -> A (in Ref. 2; AK218008).
FT   CONFLICT    167    167       N -> K (in Ref. 2; AK218008).
SQ   SEQUENCE   424 AA;  48938 MW;  A0A0789CE718F3C0 CRC64;
     MDNKKKDKDK SDDRMARPSG RSGHSTRGTG SSSSGVLMVG PNFRVGKKIG CGNFGELRLG
     KNLYTNEYVA IKLEPMKSRA PQLHLEYRFY KQLGSGDGIP QVYYFGPCGK YNAMVLELLG
     PSLEDLFDLC DRTFSLKTVL MIAIQLISRM EYVHSKNLIY RDVKPENFLI GRPGNKAQQV
     IHIIDFGLAK EYIDPETKKH IPYREHKSLT GTARYMSINT HLGKEQSRRD DLEALGHMFM
     YFLRGSLPWQ GLKADTLKER YQKIGDTKRA TPIEVLCENF PEEMATYLRY VRRLDFFEKP
     DYDYLRKLFT DLFDRKGYMF DYEYDWIGKQ LPTPVGAVQQ DPALSSNREA HQHRDKIQQS
     KNQVVSSTNG ELNTDDPTAG RSNAPITAPT EVEVMDETNC QKVLNMWCCC FFKRRKRKTI
     QRHK
//
ID   K102L_MOUSE             Reviewed;         151 AA.
AC   Q8C4X7; Q6DI98;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 3.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=UPF0258 protein KIAA1024-like homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the UPF0258 family.
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DR   EMBL; AK080452; BAC37921.1; -; mRNA.
DR   EMBL; BC075669; AAH75669.1; -; mRNA.
DR   IPI; IPI00463661; -.
DR   UniGene; Mm.209711; -.
DR   PhosphoSite; Q8C4X7; -.
DR   PRIDE; Q8C4X7; -.
DR   Ensembl; ENSMUST00000058633; ENSMUSP00000056379; ENSMUSG00000050875.
DR   Ensembl; ENSMUST00000117064; ENSMUSP00000113487; ENSMUSG00000050875.
DR   Ensembl; ENSMUST00000118510; ENSMUSP00000113023; ENSMUSG00000050875.
DR   UCSC; uc008ezt.1; mouse.
DR   MGI; MGI:2442934; A730017C20Rik.
DR   eggNOG; roNOG17082; -.
DR   GeneTree; ENSGT00530000063851; -.
DR   HOGENOM; HBG446462; -.
DR   HOVERGEN; HBG092676; -.
DR   InParanoid; Q8C4X7; -.
DR   OrthoDB; EOG4RNB9Z; -.
DR   NextBio; 377708; -.
DR   ArrayExpress; Q8C4X7; -.
DR   Bgee; Q8C4X7; -.
DR   CleanEx; MM_A730017C20RIK; -.
DR   Genevestigator; Q8C4X7; -.
DR   GermOnline; ENSMUSG00000050875; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR009626; UPF0258.
DR   Pfam; PF06789; UPF0258; 1.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    151       UPF0258 protein KIAA1024-like homolog.
FT                                /FTId=PRO_0000157136.
FT   TRANSMEM    130    150       Helical; (Potential).
FT   MOD_RES      40     40       Phosphoserine.
FT   CONFLICT    116    116       E -> K (in Ref. 2; AAH75669).
SQ   SEQUENCE   151 AA;  17168 MW;  797E3B5B16B2263E CRC64;
     MPAYQEDREE DTCTIGEREK TIATQRIKGF GVENPVLPES PPASMSSVMK NNPLYGDITL
     EEAMEERKKS PSWTIEEYDK HSVHTNLSGH LKENPNDLRF WLGDTYTPGF DTLLKEKKKR
     NKRSKLCHMG LILLLVASIL VTIVTLSTIF S
//
ID   CC059_MOUSE             Reviewed;         428 AA.
AC   Q8C525; Q5U4H4;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 42.
DE   RecName: Full=Uncharacterized protein C3orf59 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=B5/EGFP; TISSUE=Trophoblast stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
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DR   EMBL; AK079722; BAC37732.1; -; mRNA.
DR   EMBL; BC085092; AAH85092.1; -; mRNA.
DR   IPI; IPI00762238; -.
DR   UniGene; Mm.155887; -.
DR   ProteinModelPortal; Q8C525; -.
DR   PhosphoSite; Q8C525; -.
DR   PRIDE; Q8C525; -.
DR   Ensembl; ENSMUST00000058376; ENSMUSP00000053260; ENSMUSG00000051065.
DR   MGI; MGI:1917028; 1600021P15Rik.
DR   eggNOG; roNOG10683; -.
DR   GeneTree; ENSGT00530000063769; -.
DR   HOVERGEN; HBG081021; -.
DR   PhylomeDB; Q8C525; -.
DR   ArrayExpress; Q8C525; -.
DR   Bgee; Q8C525; -.
DR   CleanEx; MM_1600021P15RIK; -.
DR   Genevestigator; Q8C525; -.
DR   GermOnline; ENSMUSG00000051065; Mus musculus.
DR   InterPro; IPR020950; Mab-21-like.
DR   Pfam; PF03281; Mab-21; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    428       Uncharacterized protein C3orf59 homolog.
FT                                /FTId=PRO_0000239304.
FT   MOD_RES     242    242       Phosphoserine (By similarity).
FT   MOD_RES     373    373       Phosphoserine.
FT   MOD_RES     376    376       Phosphoserine.
FT   CONFLICT      1      7       MLQTPMT -> ML (in Ref. 2; AAH85092).
FT   CONFLICT    332    332       L -> P (in Ref. 2; AAH85092).
SQ   SEQUENCE   428 AA;  48477 MW;  8480716109117DB8 CRC64;
     MLQTPMTGMV QKLDQKLPVA NEYLLLSGGV REGVVDLDLD ELNVYARGTD YDMDFTLLVP
     ALKLHDRNQP VTLDMRHSAL CHSWLSLRLF DEGTISKWKG CCTIADHING ATNYFFSPTK
     VADWFYDSIS IVLSEIQKKP QRGMPKVEKV EKNGTIISII LGVGSSRMLY DIVPVVSFKG
     WPAVAQSWLM ENHFWDGKIT EEEVISGFYL VPACSYKGKK DNEWRLSFAR SEVQLKKCIS
     GSLMQAYQAC KAIIIKLLSR PKAISPYHLR SMMLWACDRL PASYLAQEDY AAHFLLGLID
     DLQHCLVNKM CPNYFIPQCN MLEHLSEETV MLHARKLSSV RSDPAEHLRT AIEHVKAANR
     LTLKLQRRGS TTSIPSPQSD GGDPNQPDDR LAKKLQQLVT ENPGKSISVF INPDDVTRPH
     FRIDDKFF
//
ID   CE033_MOUSE             Reviewed;         452 AA.
AC   Q8C5H8; Q3TRP5; Q3UEY1; Q9CTE4;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=UPF0465 protein C5orf33 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 63-452 (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 63-452 (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 61-452 (ISOFORM 4).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Adipose tissue, Cerebellum, Embryo, Olfactory bulb, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8C5H8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C5H8-2; Sequence=VSP_027195, VSP_027196;
CC       Name=3;
CC         IsoId=Q8C5H8-3; Sequence=VSP_027195;
CC       Name=4;
CC         IsoId=Q8C5H8-4; Sequence=VSP_027194, VSP_027195;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the UPF0465 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB23041.1; Type=Frameshift; Positions=80;
CC       Sequence=BAE28780.1; Type=Erroneous initiation;
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DR   EMBL; AK003858; BAB23041.1; ALT_FRAME; mRNA.
DR   EMBL; AK046666; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK078318; BAC37218.1; -; mRNA.
DR   EMBL; AK149267; BAE28780.1; ALT_INIT; mRNA.
DR   EMBL; AK162601; BAE36982.1; -; mRNA.
DR   IPI; IPI00651954; -.
DR   IPI; IPI00652978; -.
DR   IPI; IPI00662342; -.
DR   IPI; IPI00855212; -.
DR   RefSeq; NP_001035485.2; NM_001040395.3.
DR   RefSeq; NP_001078879.1; NM_001085410.1.
DR   UniGene; Mm.244226; -.
DR   UniGene; Mm.468219; -.
DR   ProteinModelPortal; Q8C5H8; -.
DR   SMR; Q8C5H8; 111-209.
DR   PhosphoSite; Q8C5H8; -.
DR   REPRODUCTION-2DPAGE; Q8C5H8; -.
DR   REPRODUCTION-2DPAGE; Q9CTE4; -.
DR   PRIDE; Q8C5H8; -.
DR   Ensembl; ENSMUST00000067760; ENSMUSP00000068318; ENSMUSG00000022253.
DR   Ensembl; ENSMUST00000100789; ENSMUSP00000098353; ENSMUSG00000022253.
DR   GeneID; 68646; -.
DR   KEGG; mmu:68646; -.
DR   NMPDR; fig|10090.3.peg.29672; -.
DR   MGI; MGI:1915896; 1110020G09Rik.
DR   GeneTree; ENSGT00390000006320; -.
DR   HOGENOM; HBG384403; -.
DR   HOVERGEN; HBG106388; -.
DR   InParanoid; Q8C5H8; -.
DR   OMA; IEVRLVK; -.
DR   OrthoDB; EOG41ZF9X; -.
DR   PhylomeDB; Q8C5H8; -.
DR   NextBio; 327622; -.
DR   ArrayExpress; Q8C5H8; -.
DR   Bgee; Q8C5H8; -.
DR   CleanEx; MM_1110020G09RIK; -.
DR   Genevestigator; Q8C5H8; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR   InterPro; IPR012355; ATP-NAD-like_euk.
DR   InterPro; IPR016064; ATP-NAD_kinase_PpnK-typ.
DR   InterPro; IPR017438; ATP-NAD_kinase_PpnK-typ_a/b.
DR   InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_all-b.
DR   InterPro; IPR002504; polyP/ATP_NADK_prd.
DR   Gene3D; G3DSA:2.60.200.30; ATP-NAD_kinase_PpnK-typ; 2.
DR   Gene3D; G3DSA:3.40.50.10330; ATP-NAD_kinase_PpnK-typ_a/b; 2.
DR   Pfam; PF01513; NAD_kinase; 1.
DR   PIRSF; PIRSF017565; Kin_ATP-NAD_euk; 1.
DR   SUPFAM; SSF111331; ATP-NAD_kinase_PpnK-typ; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    452       UPF0465 protein C5orf33 homolog.
FT                                /FTId=PRO_0000296293.
FT   MOD_RES     176    176       Phosphoserine.
FT   VAR_SEQ     175    202       Missing (in isoform 4).
FT                                /FTId=VSP_027194.
FT   VAR_SEQ     276    297       Missing (in isoform 2, isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_027195.
FT   VAR_SEQ     408    452       Missing (in isoform 2).
FT                                /FTId=VSP_027196.
FT   CONFLICT     62     62       V -> G (in Ref. 1; BAB23041).
FT   CONFLICT     81     81       S -> P (in Ref. 1; BAB23041).
FT   CONFLICT    207    207       R -> S (in Ref. 1; BAB23041).
SQ   SEQUENCE   452 AA;  50859 MW;  C0FC67A5BA762D1B CRC64;
     MTCYRGFLLG SCRRVAGGRA ALRGSGSGAD GRRHLGHGQP RELAGGGSPA DGGFRPSRVV
     VVAKTTRYEF EQQRYRYAEL SEEDLKQLLA LKGSSYSGLL ERHHIHTKNV EHIIDSLRDE
     GIEVRLVKRR EYDEETVRWA DAVIAAGGDG TMLLAASKVL DRLKPVIGVN TDPERSEGHL
     CLPVRYTHSF PEALRRFSRG EFRWLWRQRI RLYLEGTGIN PTPVDLHEQQ LSLNQHSRAF
     NIERAHDERS EASGPQLLPV RALNEVFIGE SLSSRMPYCW AVAVDNLRRD IPNLKGLASY
     YEISVDDGPW EKQKSSGLNL CTGTGSKAWS FNINRVAAQA VEDVLHIARR QGNLTLPLNK
     DLVEKVTNEY NESLLYSPEE PKILFSIREP IANRVFSSSR QRCFSSKVCV RSRCWDACMV
     VDGGTSFEFN DGAIASMMIN KEDELRTVIL EQ
//
ID   CNOT2_MOUSE             Reviewed;         540 AA.
AC   Q8C5L3; Q3UE39; Q80YA5; Q9D0P1;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=CCR4-NOT transcription complex subunit 2;
DE   AltName: Full=CCR4-associated factor 2;
GN   Name=Cnot2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: The CCR4-NOT complex functions as general transcription
CC       regulation complex (By similarity).
CC   -!- SUBUNIT: Subunit of the CCR4-NOT core complex that contains
CC       CHAF1A, CHAF1B, CNOT1, CNOT2, CNOT3, CNOT4, CNOT6 and CNOT8 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). Nucleus (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8C5L3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C5L3-2; Sequence=VSP_009918;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8C5L3-3; Sequence=VSP_009917;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the CNOT2/3/5 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH43133.1; Type=Frameshift; Positions=1;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK011231; BAB27481.1; -; mRNA.
DR   EMBL; AK078121; BAC37134.1; -; mRNA.
DR   EMBL; AK149767; BAE29072.1; -; mRNA.
DR   EMBL; BC043133; AAH43133.1; ALT_FRAME; mRNA.
DR   EMBL; BC063105; AAH63105.1; -; mRNA.
DR   EMBL; BC065171; AAH65171.1; -; mRNA.
DR   IPI; IPI00132821; -.
DR   IPI; IPI00410747; -.
DR   IPI; IPI00410748; -.
DR   RefSeq; NP_001032935.2; NM_001037846.3.
DR   RefSeq; NP_001032936.2; NM_001037847.2.
DR   RefSeq; NP_001032937.1; NM_001037848.3.
DR   RefSeq; NP_082358.2; NM_028082.2.
DR   UniGene; Mm.351553; -.
DR   STRING; Q8C5L3; -.
DR   PhosphoSite; Q8C5L3; -.
DR   PRIDE; Q8C5L3; -.
DR   Ensembl; ENSMUST00000064218; ENSMUSP00000066310; ENSMUSG00000020166.
DR   Ensembl; ENSMUST00000105265; ENSMUSP00000100900; ENSMUSG00000020166.
DR   Ensembl; ENSMUST00000105266; ENSMUSP00000100901; ENSMUSG00000020166.
DR   Ensembl; ENSMUST00000105267; ENSMUSP00000100902; ENSMUSG00000020166.
DR   GeneID; 72068; -.
DR   KEGG; mmu:72068; -.
DR   UCSC; uc007hca.1; mouse.
DR   UCSC; uc007hcb.1; mouse.
DR   UCSC; uc007hce.1; mouse.
DR   CTD; 72068; -.
DR   MGI; MGI:1919318; Cnot2.
DR   GeneTree; ENSGT00390000001285; -.
DR   HOGENOM; HBG445797; -.
DR   HOVERGEN; HBG051041; -.
DR   InParanoid; Q8C5L3; -.
DR   OMA; MFGARKK; -.
DR   OrthoDB; EOG44MXRV; -.
DR   PhylomeDB; Q8C5L3; -.
DR   NextBio; 335352; -.
DR   ArrayExpress; Q8C5L3; -.
DR   Bgee; Q8C5L3; -.
DR   CleanEx; MM_CNOT2; -.
DR   Genevestigator; Q8C5L3; -.
DR   GermOnline; ENSMUSG00000020166; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030528; F:transcription regulator activity; IEA:InterPro.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR007282; NOT.
DR   Pfam; PF04153; NOT2_3_5; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    540       CCR4-NOT transcription complex subunit 2.
FT                                /FTId=PRO_0000198332.
FT   MOD_RES      93     93       Phosphothreonine (By similarity).
FT   MOD_RES     101    101       Phosphoserine (By similarity).
FT   MOD_RES     126    126       Phosphoserine (By similarity).
FT   MOD_RES     165    165       Phosphoserine (By similarity).
FT   VAR_SEQ       1     85       Missing (in isoform 3).
FT                                /FTId=VSP_009917.
FT   VAR_SEQ       1     15       MVRTDGHTLSEKRNY -> MLKEVA (in isoform 2).
FT                                /FTId=VSP_009918.
FT   CONFLICT    148    148       G -> S (in Ref. 1; BAC37134).
FT   CONFLICT    426    426       H -> Y (in Ref. 2; AAH43133).
SQ   SEQUENCE   540 AA;  59711 MW;  C5185262B5E3C78C CRC64;
     MVRTDGHTLS EKRNYQVTNS MFGASRKKFV EGVDSDYHDE NMYYSQSSMF PHRSEKDMLA
     SPSTSGQLSQ FGASLYGQQS ALGLPMRGMS NNTPQLNRSL SQGTQLPSHV TPTTGVPTMS
     LHTPPSPSRG ILPMNPRNMM NHSQVGQGIG IPSRTNSMSS SGLGSPNRSS PSIICMPKQQ
     PSRQPFTVNS MSGFGMNRNQ AFGMNNSLSS NIFNGTDGSE NVTGLDLSDF PALADRNRRE
     GSGNPTPLIN PLAGRAPYVG MVTKPANEQS QDFSIHNEDF PALPGSSYKD PTSSNDDSKS
     NLSTSGKTTS STDGPKFPGD KSSTTQNNNQ QKKGIQVLPD GRVTNIPQGM VTDQFGMIGL
     LTFIRAAETD PGMVHLALGS DLTTLGLNLN SPENLYPKFA SPWASSPCRP QDIDFHVPSE
     YLTNIHIRDK LAAIKLGRYG EDLLFYLYYM NGGDVLQLLA AVELFNRDWR YHKEERVWIT
     RAPGMEPTMK TNTYERGTYY FFDCLNWRKV AKEFHLEYDK LEERPHLPST FNYNPAQQAF
//
ID   CLMN_MOUSE              Reviewed;        1052 AA.
AC   Q8C5W0; Q91V71; Q91XT7; Q91XT8; Q91XU9;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2003, sequence version 2.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Calmin;
DE   AltName: Full=Calponin-like transmembrane domain protein;
GN   Name=Clmn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=ICR; TISSUE=Brain, and Testis;
RX   MEDLINE=21280911; PubMed=11386753; DOI=10.1006/geno.2001.6544;
RA   Ishisaki Z., Takaishi M., Furuta I., Huh N.-H.;
RT   "Calmin, a protein with calponin homology and transmembrane domains
RT   expressed in maturing spermatogenic cells.";
RL   Genomics 74:172-179(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 98-1052 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=22557181; PubMed=12670712; DOI=10.1016/S0169-328X(03)00061-5;
RA   Takaishi M., Ishisaki Z., Yoshida T., Takata Y., Huh N.-H.;
RT   "Expression of calmin, a novel developmentally regulated brain protein
RT   with calponin-homology domains.";
RL   Brain Res. Mol. Brain Res. 112:146-152(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317 AND SER-724, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-395 AND SER-537, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Membrane; Single-pass type IV
CC       membrane protein (Potential). Note=Shows a reticular pattern in
CC       the cytoplasm.
CC   -!- SUBCELLULAR LOCATION: Isoform 4: Membrane; Single-pass type IV
CC       membrane protein (Potential). Note=Shows a reticular pattern in
CC       the cytoplasm.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.
CC   -!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=Beta;
CC         IsoId=Q8C5W0-1; Sequence=Displayed;
CC       Name=2; Synonyms=Delta;
CC         IsoId=Q8C5W0-2; Sequence=VSP_007766, VSP_007767;
CC         Note=Lacks the transmembrane domain;
CC       Name=3; Synonyms=Gamma;
CC         IsoId=Q8C5W0-3; Sequence=VSP_007768, VSP_007769;
CC         Note=Lacks the transmembrane domain;
CC       Name=4; Synonyms=Alpha;
CC         IsoId=Q8C5W0-4; Sequence=VSP_007770;
CC   -!- TISSUE SPECIFICITY: Expressed in testis. Expressed during testis
CC       maturation process and in maturing spermatids. In brain, it is
CC       expressed in neurons of the hippocampus, cerebral cortex, and
CC       thalamus, Purkinje cells, and also in the choroid plexus and
CC       ependymal cells. Expressed predominantly in dendrites and cell
CC       bodies of the neurons, but not in axons. The level of expression
CC       increases during the period of maturation of the mouse brain after
CC       birth.
CC   -!- SIMILARITY: Contains 1 actin-binding domain.
CC   -!- SIMILARITY: Contains 2 CH (calponin-homology) domains.
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DR   EMBL; AB047978; BAB59009.1; -; mRNA.
DR   EMBL; AB059643; BAB59120.1; -; mRNA.
DR   EMBL; AB059644; BAB59121.1; -; mRNA.
DR   EMBL; AB059645; BAB59122.1; -; mRNA.
DR   EMBL; AB059646; BAB59123.1; -; mRNA.
DR   EMBL; AB059647; BAB59124.1; -; mRNA.
DR   EMBL; AB059648; BAB59125.1; -; mRNA.
DR   EMBL; AK077023; BAC36573.1; -; mRNA.
DR   IPI; IPI00331290; -.
DR   IPI; IPI00336416; -.
DR   IPI; IPI00469735; -.
DR   IPI; IPI00755695; -.
DR   RefSeq; NP_001035772.1; NM_001040682.1.
DR   RefSeq; NP_444385.2; NM_053155.2.
DR   UniGene; Mm.244078; -.
DR   ProteinModelPortal; Q8C5W0; -.
DR   SMR; Q8C5W0; 22-296.
DR   STRING; Q8C5W0; -.
DR   PhosphoSite; Q8C5W0; -.
DR   PRIDE; Q8C5W0; -.
DR   Ensembl; ENSMUST00000077761; ENSMUSP00000076939; ENSMUSG00000021097.
DR   Ensembl; ENSMUST00000109936; ENSMUSP00000105562; ENSMUSG00000021097.
DR   Ensembl; ENSMUST00000109937; ENSMUSP00000105563; ENSMUSG00000021097.
DR   GeneID; 94040; -.
DR   KEGG; mmu:94040; -.
DR   UCSC; uc007oxl.1; mouse.
DR   CTD; 94040; -.
DR   MGI; MGI:2136957; Clmn.
DR   GeneTree; ENSGT00600000084318; -.
DR   HOGENOM; HBG282295; -.
DR   HOVERGEN; HBG039395; -.
DR   InParanoid; Q8C5W0; -.
DR   OMA; DHFSYVQ; -.
DR   OrthoDB; EOG4RFKTK; -.
DR   NextBio; 351985; -.
DR   ArrayExpress; Q8C5W0; -.
DR   Bgee; Q8C5W0; -.
DR   CleanEx; MM_CLMN; -.
DR   Genevestigator; Q8C5W0; -.
DR   GermOnline; ENSMUSG00000021097; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 2.
DR   Pfam; PF00307; CH; 2.
DR   SMART; SM00033; CH; 2.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Cytoplasm; Membrane;
KW   Phosphoprotein; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN         1   1052       Calmin.
FT                                /FTId=PRO_0000089855.
FT   TRANSMEM   1027   1047       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   DOMAIN        1    288       Actin-binding.
FT   DOMAIN        1    139       CH 1.
FT   DOMAIN      187    288       CH 2.
FT   MOD_RES     317    317       Phosphoserine.
FT   MOD_RES     395    395       Phosphothreonine.
FT   MOD_RES     537    537       Phosphoserine.
FT   MOD_RES     724    724       Phosphoserine.
FT   VAR_SEQ     922    927       NSHSDS -> TVIPFL (in isoform 2).
FT                                /FTId=VSP_007766.
FT   VAR_SEQ     928   1052       Missing (in isoform 2).
FT                                /FTId=VSP_007767.
FT   VAR_SEQ     942    946       DHFSY -> SFHLY (in isoform 3).
FT                                /FTId=VSP_007768.
FT   VAR_SEQ     947   1052       Missing (in isoform 3).
FT                                /FTId=VSP_007769.
FT   VAR_SEQ     966    996       Missing (in isoform 4).
FT                                /FTId=VSP_007770.
FT   CONFLICT    170    170       Missing (in Ref. 2; BAC36573).
FT   CONFLICT   1012   1012       S -> R (in Ref. 2; BAC36573).
SQ   SEQUENCE   1052 AA;  117227 MW;  A5AD7D3FF99A6EB6 CRC64;
     MAAQEWDWFQ REELIGQISD IRVQNLQVER ENVQKRTFTR WINLHLEKCD PPLEVTDLFV
     DIQDGKILMA LLEVLSGRNL LHEYKSSSHR IFRLNNIAKA LKFLEDSNVK LVSIDAAEIA
     DGNPSLVLGL IWNIILFFQI KELTGNLSRS SPSSSLSPGS GGTDSDSSYP PTPTTERSVA
     VAVKDQRKAI KTLLSWVQRK TRKYGVAVQD FAGSWRSGLA FLAVIKAIDP SLVDMKQALE
     DSTRDNLEKA FSIAHDSLHI PRLLEPEDIM VDMPDEQSIV TYVAQFLERF PELEPEDFVN
     PDKEAPIEST FVRIKESPSE QGSRVLLLSE NGERAYTVNQ ETSYPPPDKV FVCDQLESPT
     GFCLDSAPSH KLSDSSTEFM HEIIDQVLQG STGKTGSIAE PTPESSILST RKDGRRSNSL
     PVKKTVHFEA DLHKDASCSK DPFYSSDFRF EGSPKATKEL SKQDGHVSLA EVSKEKKKSE
     QEARLVLEAA SDKVPESTVD GLDAVPQDAQ PSQDSSFCNG TVESPSSQGE KGPPPSSPGD
     HTLLANSTEL KVQLLTVEPM DKEDYFECIP LKASKFNRDL VDFASTSQAF GEDPSSHEKT
     RGEEEGSENH AEKPGKRKSK SPRAETEAAE SRLEPKKLEP PPKDPEQEDQ GHALPPETPA
     DKKPKVYEKA KRKSTRHHSE EEGEAESGFS AVCEEEIPSA PPSTSVSLET LRSHSEEGLD
     FKPSPPLSKI SVIPHDLFYY PHYEVPLAAV LEAYAEGGED LKSEDTDLEH PEDSYLQDSR
     EEEADEDEEE AQSSQSSCSF SLPVDNSYPS VSEHVSHVDG SSEGPTSALG PGSPPSHEDH
     QPKETKENGP VESQQSQEPP NPELPTKPLE EKLTEASTSS KKKEKRKHMD HVESSLFIAP
     GTVRSSDDLE ENSSEHKVPS RNSHSDSSIY IRRHTNRSLE LDHFSYVQLR NAADLDDRRN
     RVLNRYNSQK LTELILQFYG IRADMKREYK HARLSMTGTN SSGEAVPLGN QSPPNDSLTQ
     FVQQPDVIYF ILFLWLLVYC LLLFPQLDVS RL
//
ID   TBCEL_MOUSE             Reviewed;         424 AA.
AC   Q8C5W3; B9EID8; Q8C7A5;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Tubulin-specific chaperone cofactor E-like protein;
DE   AltName: Full=Leucine-rich repeat-containing protein 35;
GN   Name=Tbcel; Synonyms=Lrrc35;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Acts as a regulator of tubulin stability (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8C5W3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C5W3-2; Sequence=VSP_019253;
CC   -!- SIMILARITY: Contains 6 LRR (leucine-rich) repeats.
CC   -!- SIMILARITY: Contains 1 ubiquitin-like domain.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK052261; BAC34901.1; -; mRNA.
DR   EMBL; AK077017; BAC36568.1; -; mRNA.
DR   EMBL; BC139386; AAI39387.1; -; mRNA.
DR   EMBL; BC139387; AAI39388.1; -; mRNA.
DR   IPI; IPI00226110; -.
DR   IPI; IPI00226608; -.
DR   RefSeq; NP_766626.1; NM_173038.3.
DR   UniGene; Mm.34483; -.
DR   ProteinModelPortal; Q8C5W3; -.
DR   SMR; Q8C5W3; 44-303, 343-422.
DR   PhosphoSite; Q8C5W3; -.
DR   PRIDE; Q8C5W3; -.
DR   Ensembl; ENSMUST00000066148; ENSMUSP00000067882; ENSMUSG00000037287.
DR   Ensembl; ENSMUST00000066179; ENSMUSP00000065125; ENSMUSG00000037287.
DR   GeneID; 272589; -.
DR   KEGG; mmu:272589; -.
DR   UCSC; uc009paw.1; mouse.
DR   UCSC; uc009pax.1; mouse.
DR   CTD; 272589; -.
DR   MGI; MGI:1925543; Tbcel.
DR   eggNOG; roNOG12667; -.
DR   GeneTree; ENSGT00530000063405; -.
DR   HOGENOM; HBG446509; -.
DR   HOVERGEN; HBG082881; -.
DR   InParanoid; Q8C5W3; -.
DR   OMA; CAGDERE; -.
DR   OrthoDB; EOG476K06; -.
DR   PhylomeDB; Q8C5W3; -.
DR   Reactome; REACT_24972; Circadian Clock (mouse).
DR   NextBio; 393606; -.
DR   ArrayExpress; Q8C5W3; -.
DR   Bgee; Q8C5W3; -.
DR   CleanEx; MM_TBCEL; -.
DR   Genevestigator; Q8C5W3; -.
DR   GermOnline; ENSMUSG00000037287; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   PROSITE; PS00299; UBIQUITIN_1; FALSE_NEG.
DR   PROSITE; PS50053; UBIQUITIN_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Leucine-rich repeat; Phosphoprotein; Repeat.
FT   CHAIN         1    424       Tubulin-specific chaperone cofactor E-
FT                                like protein.
FT                                /FTId=PRO_0000239669.
FT   REPEAT       73     98       LRR 1.
FT   REPEAT       99    123       LRR 2.
FT   REPEAT      150    172       LRR 3.
FT   REPEAT      173    197       LRR 4.
FT   REPEAT      199    224       LRR 5.
FT   REPEAT      226    250       LRR 6.
FT   DOMAIN      334    424       Ubiquitin-like.
FT   COILED      349    375       Potential.
FT   MOD_RES      41     41       Phosphoserine.
FT   VAR_SEQ       1      1       M -> MASEVNASSPALNFSEKKM (in isoform 2).
FT                                /FTId=VSP_019253.
FT   CONFLICT    275    275       K -> R (in Ref. 1; BAC34901).
SQ   SEQUENCE   424 AA;  48032 MW;  3C1AD31DF4C7B27A CRC64;
     MDQPSGRSFM QVLCEKYSPE NFPYRRGPGV GVHVPATPQG SPMKDRLNLP SVLVLNSCGI
     TCAGDEREIA AFCAHVSELD LSDNKLQDWH EVSKIVSNVP QLEFLNLSSN PLSLSVLERT
     CAGSFSGVRK LVLNNSKASW ETVHTILQEL PELEELFLCL NDYETVSCPS VCCHSLKLLH
     ITDNNLQDWT EIRKLGVMFP SLDTLVLANN HLNAIEEPAD SLARLFPNLR SISLHKSGLQ
     SWEDIDKLNS FPKLEEVRLL GIPLLQPYTT EERRKLVVAR LPSVSKLNGS VVTDGEREDS
     ERFFIRYYVD VPQEEVPFRY HELITKYGKL EPLAEVDLRP QSSAKVEVHF NDQVEEMSIR
     LDQTVAELKK QLKTLVQLPT SSMLLYYFDH EAPFGPEEMK YSSRALHSFG IRDGDKIFVE
     SKTK
//
ID   RTKN_MOUSE              Reviewed;         564 AA.
AC   Q8C6B2; Q61192; Q8VIG7;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Rhotekin;
GN   Name=Rtkn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH RHOA; RHOB
RP   AND RHOC, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=96278781; PubMed=8662891; DOI=10.1074/jbc.271.23.13556;
RA   Reid T., Furuyashiki T., Ishizaki T., Watanabe G., Watanabe N.,
RA   Fujisawa K., Morii N., Madaule P., Narumiya S.;
RT   "Rhotekin, a new putative target for Rho bearing homology to a
RT   serine/threonine kinase, PKN, and rhophilin in the rho-binding
RT   domain.";
RL   J. Biol. Chem. 271:13556-13560(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-520, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Mediates Rho signaling to activate NF-kappa-B and may
CC       confer increased resistance to apoptosis to cells in gastric
CC       tumorigenesis. May play a novel role in the organization of septin
CC       structures (By similarity).
CC   -!- SUBUNIT: Interacts via its C-terminal region with the TAX1BP3 PDZ
CC       domain. This interaction facilitates Rho-mediated activation of
CC       the c-Fos serum response element (SRE). Interacts with SEPT9 (By
CC       similarity). Specifically binds to GTP-bound RHOA, RHOB and RHOC
CC       and inhibits their GTPase activity.
CC   -!- INTERACTION:
CC       Q9DBG9:Tax1bp3; NbExp=1; IntAct=EBI-1162441, EBI-1161647;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8C6B2-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q8C6B2-2; Sequence=VSP_052006;
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in brain and kidney.
CC       Weakly expressed in lung, testis, skeletal muscle, heart and
CC       thymus.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 REM (Hr1) repeat.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U54638; AAC52605.1; -; mRNA.
DR   EMBL; AK076155; BAC36222.1; -; mRNA.
DR   EMBL; BC013820; AAH13820.1; -; mRNA.
DR   IPI; IPI00226220; -.
DR   IPI; IPI00278604; -.
DR   RefSeq; NP_001129699.1; NM_001136227.1.
DR   RefSeq; NP_033132.2; NM_009106.2.
DR   RefSeq; NP_598396.2; NM_133641.2.
DR   UniGene; Mm.4139; -.
DR   ProteinModelPortal; Q8C6B2; -.
DR   SMR; Q8C6B2; 310-415.
DR   DIP; DIP-29983N; -.
DR   IntAct; Q8C6B2; 3.
DR   MINT; MINT-1791510; -.
DR   STRING; Q8C6B2; -.
DR   PhosphoSite; Q8C6B2; -.
DR   PRIDE; Q8C6B2; -.
DR   Ensembl; ENSMUST00000065512; ENSMUSP00000065571; ENSMUSG00000034930.
DR   Ensembl; ENSMUST00000087938; ENSMUSP00000085249; ENSMUSG00000034930.
DR   GeneID; 20166; -.
DR   KEGG; mmu:20166; -.
DR   UCSC; uc009cms.1; mouse.
DR   UCSC; uc009cmt.1; mouse.
DR   CTD; 20166; -.
DR   MGI; MGI:107371; Rtkn.
DR   eggNOG; roNOG11996; -.
DR   GeneTree; ENSGT00390000000104; -.
DR   HOGENOM; HBG715547; -.
DR   HOVERGEN; HBG059480; -.
DR   InParanoid; Q8C6B2; -.
DR   OrthoDB; EOG46143R; -.
DR   NextBio; 297673; -.
DR   ArrayExpress; Q8C6B2; -.
DR   Bgee; Q8C6B2; -.
DR   CleanEx; MM_RTKN; -.
DR   Genevestigator; Q8C6B2; -.
DR   GermOnline; ENSMUSG00000034930; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017049; F:GTP-Rho binding; IDA:UniProtKB.
DR   GO; GO:0005095; F:GTPase inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0045767; P:regulation of anti-apoptosis; ISS:UniProtKB.
DR   GO; GO:0007266; P:Rho protein signal transduction; ISS:UniProtKB.
DR   InterPro; IPR011072; HR1_rho-bd.
DR   InterPro; IPR000861; HR1_rpt_rho-bd.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF02185; HR1; 1.
DR   SMART; SM00742; Hr1; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; GTP-binding; Nucleotide-binding;
KW   Phosphoprotein.
FT   CHAIN         1    564       Rhotekin.
FT                                /FTId=PRO_0000233941.
FT   REPEAT       36     99       REM.
FT   DOMAIN      309    416       PH.
FT   COMPBIAS    479    545       Pro-rich.
FT   MOD_RES     106    106       Phosphoserine.
FT   MOD_RES     232    232       Phosphoserine (By similarity).
FT   MOD_RES     520    520       Phosphoserine.
FT   MOD_RES     544    544       Phosphoserine (By similarity).
FT   VAR_SEQ       1     36       MFSRNHRSRITVARGSALEMEFKRGRFRLSFFSESP -> M
FT                                QDRLRILEDLNMLYIRQMALSL (in isoform 2).
FT                                /FTId=VSP_052006.
FT   CONFLICT     67     67       Q -> L (in Ref. 2; BAC36222).
FT   CONFLICT    365    365       R -> G (in Ref. 1 and 2).
FT   CONFLICT    444    444       V -> A (in Ref. 2; BAC36222).
SQ   SEQUENCE   564 AA;  63041 MW;  0124F9BF09B13D3E CRC64;
     MFSRNHRSRI TVARGSALEM EFKRGRFRLS FFSESPEDTE LQRKLDHEIR MRDGACKLLA
     ACSQREQALE ATKSLLVCNS RILSYMGELQ RRKEAQVLEK TGRRPSDSVQ PAQHSPCRGR
     VCISDLRIPL MWKDTEYFKN KGDLHRWAVF LLLQIGEQIQ DTEMVLVDRT LTDISFQNNV
     LFAEAEPDFE LRLELYGACV EEEGALAGAP KRLATKLSSS LGRSSGKRVR ASLDSAGASG
     NSPVLLPTPA VGGPRFHLLA HTTLTLEEVQ DGFRTHDLTL TSHEENPAWL PLYGSVCCRL
     AAQPLCMIQP TASGALRVQQ AGELQNGTLV HGVLKGTNLF CYWRSEDADT GQEPLFTIVI
     NKETRVRAGE LEQAPEWPFT LSISNKYGDD EVTNTLQLES REALQNWMEA LWQLFFDMSQ
     WRHCCDEVMK IETPAPRKPP QALVKQGSLY HEMAIEPLDD IAAVTDILAQ REGTRLEPSP
     PWLAMFTDQP ALPSSCSPAS VAPVPTWMQP LPWGRPRTFS LDAAPADHSL GPSRSVAPLP
     PQRSPKSRGF YSKSQLGPWL QSPV
//
ID   Q8C6E9_MOUSE            Unreviewed;       321 AA.
AC   Q8C6E9;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 48.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Pura;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK075821; BAC35987.1; -; mRNA.
DR   IPI; IPI00118447; -.
DR   UniGene; Mm.231802; -.
DR   STRING; Q8C6E9; -.
DR   Ensembl; ENSMUST00000051301; ENSMUSP00000059404; ENSMUSG00000043991.
DR   MGI; MGI:103079; Pura.
DR   GeneTree; ENSGT00390000015406; -.
DR   HOVERGEN; HBG006888; -.
DR   InParanoid; Q8C6E9; -.
DR   ArrayExpress; Q8C6E9; -.
DR   Bgee; Q8C6E9; -.
DR   Genevestigator; Q8C6E9; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0005662; C:DNA replication factor A complex; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR   GO; GO:0046332; F:SMAD binding; IDA:MGI.
DR   GO; GO:0008134; F:transcription factor binding; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:MGI.
DR   GO; GO:0007399; P:nervous system development; IMP:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
DR   InterPro; IPR006628; PUR_DNA_RNA-bd.
DR   PANTHER; PTHR12611; PUR_DNA_RNA_bd; 1.
DR   Pfam; PF04845; PurA; 1.
DR   SMART; SM00712; PUR; 3.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   321 AA;  34980 MW;  A6529C1A3FBC717E CRC64;
     MADRDSGSEQ GGAALGSGGS LGHPGSGSGS GGGGGGGGGG CGSGGCGGAP GGLQHETQEL
     ASKRVDIQNK RFYLDVKHNA KGLFLKIAEV GAGGNKSRLT LSMSVAVEFR DYLGDFIEHY
     AQLGPSQPPD LAQAQXEPRR ALKSEFLVRE NRKYYMNLKE NQRGRFLRIR QTVNRGPGLG
     STQGQTIALP AQGLIEFRDA LAKLIDDYGV EEEPAELPEG TSLTVDNKRF FFDVGSNKYG
     VFMRVSEVKP TYRNSITVPY KVWAKFGHTF CKYSEEMKKI QEKQREKRAD CEQLHQQQQQ
     QQEETTAATL LLQGEEEGEK D
//
ID   WDR26_MOUSE             Reviewed;         641 AA.
AC   Q8C6G8; Q3TK81; Q8C4F3; Q8VDZ6;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=WD repeat-containing protein 26;
GN   Name=Wdr26;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and Czech II; TISSUE=Mammary gland, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-641.
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: May be involved in MAPK pathways (By similarity).
CC   -!- SUBUNIT: Interacts with DDB1-CUL4A/B E3 ligase complexes (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Contains 1 CTLH domain.
CC   -!- SIMILARITY: Contains 1 LisH domain.
CC   -!- SIMILARITY: Contains 6 WD repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC35923.1; Type=Erroneous initiation;
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DR   EMBL; BF136897; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC020044; AAH20044.2; -; mRNA.
DR   EMBL; BC058601; AAH58601.1; -; mRNA.
DR   EMBL; AK075743; BAC35923.1; ALT_INIT; mRNA.
DR   EMBL; AK167116; BAE39264.1; -; mRNA.
DR   EMBL; AK167017; BAE39191.1; -; mRNA.
DR   IPI; IPI00226275; -.
DR   RefSeq; NP_663489.4; NM_145514.5.
DR   UniGene; Mm.289082; -.
DR   ProteinModelPortal; Q8C6G8; -.
DR   SMR; Q8C6G8; 324-626.
DR   PhosphoSite; Q8C6G8; -.
DR   PRIDE; Q8C6G8; -.
DR   Ensembl; ENSMUST00000036329; ENSMUSP00000045177; ENSMUSG00000038733.
DR   GeneID; 226757; -.
DR   KEGG; mmu:226757; -.
DR   UCSC; uc007dxf.1; mouse.
DR   CTD; 226757; -.
DR   MGI; MGI:1923825; Wdr26.
DR   eggNOG; roNOG09870; -.
DR   GeneTree; ENSGT00530000063585; -.
DR   HOGENOM; HBG443712; -.
DR   HOVERGEN; HBG083958; -.
DR   InParanoid; Q8C6G8; -.
DR   OrthoDB; EOG4GHZNV; -.
DR   PhylomeDB; Q8C6G8; -.
DR   NextBio; 378339; -.
DR   ArrayExpress; Q8C6G8; -.
DR   Bgee; Q8C6G8; -.
DR   CleanEx; MM_WDR26; -.
DR   Genevestigator; Q8C6G8; -.
DR   GermOnline; ENSMUSG00000038733; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR006595; CTLH_C.
DR   InterPro; IPR006594; LisH_dimerisation.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 5.
DR   SMART; SM00668; CTLH; 1.
DR   SMART; SM00667; LisH; 1.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS50897; CTLH; 1.
DR   PROSITE; PS50896; LISH; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; Repeat; WD repeat.
FT   CHAIN         1    641       WD repeat-containing protein 26.
FT                                /FTId=PRO_0000051374.
FT   DOMAIN      103    135       LisH.
FT   DOMAIN      136    211       CTLH.
FT   REPEAT      333    372       WD 1.
FT   REPEAT      379    418       WD 2.
FT   REPEAT      424    464       WD 3.
FT   REPEAT      504    543       WD 4.
FT   REPEAT      546    588       WD 5.
FT   REPEAT      591    631       WD 6.
FT   MOD_RES     101    101       Phosphoserine.
SQ   SEQUENCE   641 AA;  70600 MW;  0135875562F236CF CRC64;
     MQANGAGGGG GGGGGARAQT PELACLSAQN GESSPSATSA GDLAHANGLL PAAPSAAGNN
     SNSLSVNNGV PGGAAAASAT AAAAQATPEL GSSLKKKKRL SQSDEDVIRL IGQHLNGLGL
     NQTVDLLMQE SGCRLEHPSA TKFRNHVMEG DWDKAENDLN ELKPLVHSPH AIVVRGALEI
     SQTLLGIIVR MKFLLLQQKY LEYLEDGKVL EALQVLRCEL TPLKYNTERI HVLSGYLMCS
     HAEDLRAKAE WEGKGTASRS KLLDKLQTYL PPSVMLPPRR LQTLLRQAVE LQRDRCLYHN
     TKLDNNLDSV SLLIDHVCSR RQFPCYTQQI LTEHCNEVWF CKFSNDGTKL ATGSKDTTVI
     IWQVDPDTHL LKLLKTLEGH AYGVSYIAWS PDDSYLVACG PDDCSELWLW NVQTGELRTK
     MSQSHEDSLT SVAWNPDGKR FVTGGQRGQF YQCDLDGNLL DSWEGVRVQC LWCLSDGKTV
     LASDTHQRVR GYNFEDLTDR NIVQEDHPIM SFTISKNGRL ALLNVATQGV HLWDLQDRVL
     VRKYQGVTQG FYTIHSCFGG HNEDFIASGS EDHKVYIWHK RSELPIAELT GHTRTVNCVS
     WNPQIPSMMA SASDDGTVRI WGPAPFIDHQ NIEEECSSMD S
//
ID   UBP20_MOUSE             Reviewed;         916 AA.
AC   Q8C6M1; Q69ZT5; Q8CJ72;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 20;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 20;
DE   AltName: Full=Ubiquitin thiolesterase 20;
DE   AltName: Full=Ubiquitin-specific-processing protease 20;
DE   AltName: Full=VHL-interacting deubiquitinating enzyme 2;
GN   Name=Usp20; Synonyms=Kiaa1003, Vdu2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12056827; DOI=10.1016/S0006-291X(02)00534-X;
RA   Li Z., Wang D., Na X., Schoen S.R., Messing E.M., Wu G.;
RT   "Identification of a deubiquitinating enzyme subfamily as substrates
RT   of the von Hippel-Lindau tumor suppressor.";
RL   Biochem. Biophys. Res. Commun. 294:700-709(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata, and Ovary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-378 AND SER-415, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Deubiquitinating enzyme involved in beta-2 adrenergic
CC       receptor (ADRB2) recycling. Acts as a regulator of G-protein
CC       coupled receptor (GPCR) signaling by mediating the
CC       deubiquitination beta-2 adrenergic receptor (ADRB2). Plays a
CC       central role in ADRB2 recycling and resensitization after
CC       prolonged agonist stimulation by constitutively binding ADRB2,
CC       mediating deubiquitination of ADRB2 and inhibiting lysosomal
CC       trafficking of ADRB2. Upon dissociation, it is probably
CC       transferred to the translocated beta-arrestins, possibly leading
CC       to beta-arrestins deubiquitination and disengagement from ADRB2.
CC       This suggests the existence of a dynamic exchange between the
CC       ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating
CC       thyroid hormone regulation. Deubiquitinates HIF1A, leading to
CC       stabilize HIF1A and enhance HIF1A-mediated activity. Mediates
CC       deubiquitination of both 'Lys-48'- and 'Lys-63'-linked
CC       polyubiquitin chains (By similarity).
CC   -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- SUBUNIT: Interacts with VHL, leading to its ubiquitination and
CC       subsequent degradation. Interacts with DIO2 and HIF1A.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region (By
CC       similarity).
CC   -!- DOMAIN: The UBP-type zinc finger binds 3 zinc ions. However, it
CC       does not bind ubiquitin, probably because the conserved Arg in
CC       position 55 is replaced by a Glu residue (By similarity).
CC   -!- PTM: Ubiquitinated via a VHL-dependent pathway for proteasomal
CC       degradation (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. USP20/USP33
CC       subfamily.
CC   -!- SIMILARITY: Contains 2 DUSP domains.
CC   -!- SIMILARITY: Contains 1 UBP-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32361.1; Type=Erroneous initiation;
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DR   EMBL; AF449715; AAN15803.1; -; mRNA.
DR   EMBL; AK173083; BAD32361.1; ALT_INIT; mRNA.
DR   EMBL; AK054279; BAC35715.1; -; mRNA.
DR   EMBL; AK163663; BAE37447.1; -; mRNA.
DR   EMBL; AL844546; CAM18433.1; -; Genomic_DNA.
DR   EMBL; CH466542; EDL08500.1; -; Genomic_DNA.
DR   EMBL; BC079674; AAH79674.1; -; mRNA.
DR   IPI; IPI00469997; -.
DR   RefSeq; NP_083122.1; NM_028846.5.
DR   UniGene; Mm.346654; -.
DR   HSSP; Q93009; 1NB8.
DR   ProteinModelPortal; Q8C6M1; -.
DR   SMR; Q8C6M1; 5-99, 142-688, 815-889.
DR   MEROPS; C19.025; -.
DR   PhosphoSite; Q8C6M1; -.
DR   PRIDE; Q8C6M1; -.
DR   Ensembl; ENSMUST00000061544; ENSMUSP00000060167; ENSMUSG00000026854.
DR   Ensembl; ENSMUST00000102849; ENSMUSP00000099913; ENSMUSG00000026854.
DR   GeneID; 74270; -.
DR   KEGG; mmu:74270; -.
DR   UCSC; uc008jdf.1; mouse.
DR   CTD; 74270; -.
DR   MGI; MGI:1921520; Usp20.
DR   HOVERGEN; HBG054196; -.
DR   InParanoid; Q8C6M1; -.
DR   OMA; MYSFKIN; -.
DR   OrthoDB; EOG4D52WZ; -.
DR   NextBio; 340299; -.
DR   ArrayExpress; Q8C6M1; -.
DR   Bgee; Q8C6M1; -.
DR   Genevestigator; Q8C6M1; -.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:0008277; P:regulation of G-protein coupled receptor protein signaling pathway; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR006615; Pept_C19_DUSP.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF06337; DUF1055; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SMART; SM00695; DUSP; 2.
DR   PROSITE; PS51283; DUSP; 2.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; 1.
DR   PROSITE; PS50235; UCH_2_3; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Endocytosis; Hydrolase; Metal-binding; Phosphoprotein;
KW   Protease; Repeat; Thiol protease; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    916       Ubiquitin carboxyl-terminal hydrolase 20.
FT                                /FTId=PRO_0000390418.
FT   DOMAIN      689    782       DUSP 1.
FT   DOMAIN      791    894       DUSP 2.
FT   ZN_FING      28     92       UBP-type.
FT   ACT_SITE    154    154       Nucleophile (By similarity).
FT   ACT_SITE    645    645       Proton acceptor (By similarity).
FT   MOD_RES     132    132       Phosphoserine (By similarity).
FT   MOD_RES     134    134       Phosphoserine (By similarity).
FT   MOD_RES     259    259       Phosphothreonine (By similarity).
FT   MOD_RES     264    264       Phosphoserine (By similarity).
FT   MOD_RES     374    374       Phosphoserine (By similarity).
FT   MOD_RES     378    378       Phosphothreonine.
FT   MOD_RES     408    408       Phosphoserine (By similarity).
FT   MOD_RES     409    409       Phosphoserine (By similarity).
FT   MOD_RES     415    415       Phosphoserine.
FT   CONFLICT    117    117       H -> T (in Ref. 1; AAN15803).
FT   CONFLICT    380    380       E -> D (in Ref. 1; AAN15803).
SQ   SEQUENCE   916 AA;  102140 MW;  E104BD489E7ED49F CRC64;
     MGDARDLCPH LDCIGEVTKE DLLLKSKGTC QSCGVAGPNL WACLQVTCPY VGCGESFADH
     SSIHAQVKKH NLTVNLTTFR VWCYACEREV FLEQRLAVHL ASSSARLSEQ DSPPPSHPLK
     AVPIAVADEG ESESEDDDLK PRGLTGMKNL GNSCYMNAAL QALSNCPPLT QFFLECGGLV
     RTDKKPALCK SYQKLISEVW HKKRPSYVVP TSLSHGIKLV NPMFRGYAQQ DTQEFLRCLM
     DQLHEELKEP MVAAVAALTD ARDSDSSDTD ERRDGDRSPS EDEFLSCDSS SDRGEGDGQG
     RGGGSSKAEM ELLISDEAGR AISEKERMKD RKFSWGQQRT NSEQVDEDAD VDTAMASLDE
     QSREAQPPSP RSTSPCQTPE PDNEAHIRSS SRPCSPVHHH HEGHSKLSSS PPRASPVRMG
     PSYVLKKAQV PSTGGRRRKE QSYRSVISDV FNGSVLSLVQ CLTCDRVSTT VETFQDLSLP
     IPGKEDLAKL HSAIYQNVPA KPGACGDSYS SQGWLAFIVE YIRRFVVSCT PSWFWGPVVT
     LEDCLAAFFA ADELKGDNMY SCERCKKLRN GVKYCKVLCL PEILCVHLKR FRHEVMYSFK
     VSSHVSFPLE GLDLRPFLAK ECTSQVTTYD LLSVICHHGT AGSGHYIAYC QNVINGQWYE
     FDDQYVTEVH ETVVQNVEAY VLFYRKSSEE AMRERQQVVS LAAMREPSLL RFYVSREWLN
     KFNTFAEPGP ITNHTFLCSH GGIPPNKYHY IDDLVVILPQ SVWEHLYSRF GGGPAVNHLY
     VCSICQVEIE ALAKRRRVEI DTFIKLNKAF QAEESPAVIY CISMHWFREW EAFVKGKDSE
     PPGPIDNSRI AQVKGSGHIQ LKQGADCGQI SEETWTYLSS LYGGGPEIAI RQSVAQLPDP
     ESLHGEQKIE AETRAL
//
ID   CL055_MOUSE             Reviewed;         816 AA.
AC   Q8C6S9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   05-OCT-2010, entry version 37.
DE   RecName: Full=Uncharacterized protein C12orf55 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-370.
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
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DR   EMBL; AC122326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK053219; BAC35315.1; -; mRNA.
DR   IPI; IPI00808401; -.
DR   UniGene; Mm.228429; -.
DR   UCSC; uc007gui.1; mouse.
DR   MGI; MGI:1922208; 4930485B16Rik.
DR   eggNOG; roNOG09419; -.
DR   HOVERGEN; HBG107708; -.
DR   CleanEx; MM_4930485B16RIK; -.
DR   Genevestigator; Q8C6S9; -.
PE   2: Evidence at transcript level;
FT   CHAIN         1    816       Uncharacterized protein C12orf55 homolog.
FT                                /FTId=PRO_0000324607.
FT   COMPBIAS      3     48       Ser-rich.
SQ   SEQUENCE   816 AA;  92719 MW;  3F4713A026686BE5 CRC64;
     MASSRSSSSS SEEFPDSETS VSPVHLPPTP PPTSTAVLKS PSESKSSSTD PPQCTHSEDS
     LPSAAFYGPL DSKNPLLASC EKEIRELLGF MKKRKALATS MEQKYEFHRR CATTLFNIWT
     KYAPRLPSNY YNEKLLKVGD SLCQIKEYKL ALLQCYGRYL QEFIADFDEH KEDVNHFKTV
     FFPKGFGDET ARLTFHALSG KNICNYQLVC ESDANLQNEE SVRQCLHILS SFRLIMQVAL
     PQEHLCWIIF NGTLYIYTIC RKLMVIGQSS KALEFLLWAS MCMESSVPLL SIRYLTWRAT
     LYTAVCQCHY DCQDGIHGEA FARRALAKID ELRQLELMSS SSSLETSRKY YREATIKMAV
     MIFKRGVFES RRKNKNVLRP KLRLNLKEAQ SLPWPRTVTE RLLDELLDST SSRFLAVLEA
     LSDSNRRILQ TGPLVTDEME LRDVVSELFM AGKELLILSN VRSNGKLDFP QTSLLEHVVE
     KRNALSVGAS VRFAKLAFTY EEWGLFESLA GQLIHFLQKQ DNPQSKKAEK DLILLLAVEP
     LINVKRNRGL IFPLETDKET QSIENYLKHI ACHESCMRTT FTEDTFSLAA ILHFCVCVGE
     QGVLPDKDIV VDIIGLLWQR CKLGIQRLNI PKNDFAKYSH KISTNKWVYL LWQISEVIHC
     YKLEDLDIVM VAEITLRLSE ILESLGSPKR KFKKSADLSA KKGPDELPGT SKGVPEILPI
     LKRAPVEQLF YAYELLDKAI IGMSWKCMLT TLSDGSSVID HCYVKDSQDV DGDTYKPIAS
     NSYTMDLHLE LIQAQHRIAV VLLDQLEGSF ILFSSD
//
ID   F126B_MOUSE             Reviewed;         530 AA.
AC   Q8C729; Q3UMY7; Q6NV64;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 53.
DE   RecName: Full=Protein FAM126B;
GN   Name=Fam126b; Synonyms=D1Ertd53e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Amnion, Kidney, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-306 AND SER-442, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8C729-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C729-2; Sequence=VSP_035078;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the FAM126 family.
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DR   EMBL; AK052638; BAC35073.1; -; mRNA.
DR   EMBL; AK144602; BAE25961.1; -; mRNA.
DR   EMBL; AK168372; BAE40304.1; -; mRNA.
DR   EMBL; BC068302; AAH68302.1; -; mRNA.
DR   IPI; IPI00226426; -.
DR   IPI; IPI00653706; -.
DR   RefSeq; NP_766101.3; NM_172513.3.
DR   UniGene; Mm.26272; -.
DR   ProteinModelPortal; Q8C729; -.
DR   PhosphoSite; Q8C729; -.
DR   PRIDE; Q8C729; -.
DR   Ensembl; ENSMUST00000038372; ENSMUSP00000038718; ENSMUSG00000038174.
DR   GeneID; 213056; -.
DR   KEGG; mmu:213056; -.
DR   UCSC; uc007bch.1; mouse.
DR   CTD; 213056; -.
DR   MGI; MGI:1098784; Fam126b.
DR   eggNOG; roNOG12267; -.
DR   GeneTree; ENSGT00390000011295; -.
DR   HOVERGEN; HBG057270; -.
DR   OMA; HRWRRED; -.
DR   PhylomeDB; Q8C729; -.
DR   NextBio; 373843; -.
DR   ArrayExpress; Q8C729; -.
DR   Bgee; Q8C729; -.
DR   Genevestigator; Q8C729; -.
DR   InterPro; IPR018619; Hyccin.
DR   Pfam; PF09790; Hyccin; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    530       Protein FAM126B.
FT                                /FTId=PRO_0000278095.
FT   MOD_RES     306    306       Phosphothreonine.
FT   MOD_RES     442    442       Phosphoserine.
FT   MOD_RES     491    491       Phosphoserine (By similarity).
FT   VAR_SEQ     330    330       E -> EDGFDFSNEADSSIPGSPIQHGSTDLGIKRVQEGEV
FT                                LVRRTPEHGSPEPTSAAATTE (in isoform 2).
FT                                /FTId=VSP_035078.
FT   CONFLICT    239    239       Q -> R (in Ref. 2; AAH68302).
SQ   SEQUENCE   530 AA;  58587 MW;  7C57D7C10D047FD7 CRC64;
     MLGSERAVVE EWLSEFKALP DTQITSYAAT LHRKKALVPA LYKVIQDSNN ELLEPVCHQL
     FELYRSSEVR LKRFTLQFLP ELIWVYLRLT VSRDRQSNGC IEALLLGIYN LEIADKDGNN
     KVLSFTIPSL SKPSIYHEPS TIGSMALTEG ALCQHDLIRV VYSDLHPQRE TFTAQNRFEV
     LSFLMLCYNS AIVYMPASSY QSLCRMGSRV CVSGFPRQHE KQWKELCGRI VLDPEFMVQL
     LTGVYYAMYN GQWDLGQEVL DDIIYRAQLE LFSQPLLVAN AMKNSLPFDA PDSSQEGQKV
     LKVEVTPTVP RISRTAITTA SIRRHRWRRE GAEGLNGGEE SLNMNDADEG FSSGASLSSQ
     PHGTKPPSSS QRGSLRKVAT GRSAKDKETA LAIKSNESPR DSVVGKQFVQ QQADLSIDSV
     ELTPMKKHLS LPAGQVVPKT NSLSLIRTAS ASSSKSFDYV NGGQASTSIG VGTEGVTNLA
     ATNANRYSTI SLQEDRLGHA GEGKELLSPG APLTKQSRSP SFNMQLISQV
//
ID   F110B_MOUSE             Reviewed;         366 AA.
AC   Q8C739; Q3UKH0;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Protein FAM110B;
GN   Name=Fam110b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney, Placenta, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton,
CC       centrosome (By similarity).
CC   -!- SIMILARITY: Belongs to the FAM110 family.
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DR   EMBL; AK052596; BAC35053.1; -; mRNA.
DR   EMBL; AK146011; BAE26831.1; -; mRNA.
DR   EMBL; AK159054; BAE34787.1; -; mRNA.
DR   EMBL; AL732614; CAM20807.1; -; Genomic_DNA.
DR   EMBL; BC055683; AAH55683.1; -; mRNA.
DR   IPI; IPI00226450; -.
DR   RefSeq; NP_775602.1; NM_173426.2.
DR   UniGene; Mm.331470; -.
DR   UniGene; Mm.458843; -.
DR   ProteinModelPortal; Q8C739; -.
DR   PhosphoSite; Q8C739; -.
DR   PRIDE; Q8C739; -.
DR   Ensembl; ENSMUST00000054857; ENSMUSP00000062734; ENSMUSG00000049119.
DR   Ensembl; ENSMUST00000108380; ENSMUSP00000104017; ENSMUSG00000049119.
DR   GeneID; 242297; -.
DR   KEGG; mmu:242297; -.
DR   UCSC; uc008rxe.1; mouse.
DR   CTD; 242297; -.
DR   MGI; MGI:1916593; Fam110b.
DR   eggNOG; roNOG10486; -.
DR   GeneTree; ENSGT00530000063395; -.
DR   HOGENOM; HBG716517; -.
DR   HOVERGEN; HBG051171; -.
DR   InParanoid; Q8C739; -.
DR   OMA; YGISAVE; -.
DR   OrthoDB; EOG4907B1; -.
DR   PhylomeDB; Q8C739; -.
DR   NextBio; 385296; -.
DR   ArrayExpress; Q8C739; -.
DR   Bgee; Q8C739; -.
DR   Genevestigator; Q8C739; -.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Phosphoprotein.
FT   CHAIN         1    366       Protein FAM110B.
FT                                /FTId=PRO_0000285652.
FT   MOD_RES     297    297       Phosphoserine (By similarity).
FT   CONFLICT    271    271       E -> D (in Ref. 1; BAE26831).
SQ   SEQUENCE   366 AA;  40360 MW;  B5DE416119777BBA CRC64;
     MPTETLQTGS MVKPVSPAGT FTSAVPLRIL NKGPDYFRRQ AEPNPKRLSA VERLEADKAK
     YVKSQEVINA KQEPVKPAVL AKPPVCPGTK RALGSPTLKV FGNHAKTESG VQRETLKLEI
     LKNIINSSEG SSSGSGHKHS SRNWPPHRDT TDLHRHSFAE SLKVYPTPGH GSPQESSSHV
     SRRLLEQSAE TFLHVSHSSS DIRKVTSVKP LKAIPCSSSA PPLPPKPKVA AMKSPEADQV
     EPACGVSRRP SLQRSKSDLS DRYFRVDADV ERFFNYCGLD PEELENLGME NFARANSDII
     SLNFRSASMI SSDCEQSQDS NSDLRNDDSA NDRVPYGISA IERNARIIKW LYSIKQARES
     QKVSHV
//
ID   Q8C7C3_MOUSE            Unreviewed;       248 AA.
AC   Q8C7C3;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 52.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Tpm3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the tropomyosin family.
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DR   EMBL; AK050665; BAC34370.1; -; mRNA.
DR   IPI; IPI00459570; -.
DR   UniGene; Mm.240839; -.
DR   UniGene; Mm.474711; -.
DR   HSSP; P42639; 1C1G.
DR   ProteinModelPortal; Q8C7C3; -.
DR   SMR; Q8C7C3; 9-248.
DR   STRING; Q8C7C3; -.
DR   PRIDE; Q8C7C3; -.
DR   Ensembl; ENSMUST00000118566; ENSMUSP00000113056; ENSMUSG00000027940.
DR   UCSC; uc008qbi.1; mouse.
DR   MGI; MGI:1890149; Tpm3.
DR   GeneTree; ENSGT00550000074494; -.
DR   HOVERGEN; HBG107404; -.
DR   ArrayExpress; Q8C7C3; -.
DR   Bgee; Q8C7C3; -.
DR   Genevestigator; Q8C7C3; -.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR   GO; GO:0030426; C:growth cone; IDA:MGI.
DR   GO; GO:0002102; C:podosome; IDA:MGI.
DR   InterPro; IPR000533; Tropomyosin.
DR   Pfam; PF00261; Tropomyosin; 1.
DR   PRINTS; PR00194; TROPOMYOSIN.
DR   PROSITE; PS00326; TROPOMYOSIN; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil.
SQ   SEQUENCE   248 AA;  28896 MW;  98D7F0688D6CB012 CRC64;
     MAGTTTIEAV KRKIQVLQQQ ADDAEERAER LQREVEGERR AREQAEAEVA SLNRRIQLVE
     EELDRAQERL ATALQKLEEA EKAADESERG MKVIENRALK DEEKMELQEI QLKEAKHIAE
     EADRKYEEVA RKLVIIEGDL ERTEERAELA ESRCREMDEQ IRLMDQNLKC LSAAEEKYSQ
     KEDKYEEEIK ILTDKLKEAE TRAEFAERSV AKLEKTIDDL EDELYAQKLK YKAISDELDH
     ALNDMTSI
//
ID   CRBN_MOUSE              Reviewed;         445 AA.
AC   Q8C7D2; Q3TVC2; Q5RJV6; Q6IS49; Q80XJ1; Q8BP45; Q8C6B7; Q9JKR4;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Protein cereblon;
DE            Short=Protein PiL;
GN   Name=Crbn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 6-445 (ISOFORM 1).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-445.
RA   Rose J.B., van Driel I.R., Tan S.;
RT   "A novel gene mutated in R197 insertional mutant mice.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=20131966; DOI=10.3109/01677060903567849;
RA   Higgins J.J., Tal A.L., Sun X., Hauck S.C., Hao J., Kosofosky B.E.,
RA   Rajadhyaksha A.M.;
RT   "Temporal and spatial mouse brain expression of cereblon, an ionic
RT   channel regulator involved in human intelligence.";
RL   J. Neurogenet. 24:18-26(2010).
CC   -!- FUNCTION: Component of some DCX (DDB1-CUL4-X-box) E3 protein
CC       ligase complex, a complex that mediates the ubiquitination and
CC       subsequent proteasomal degradation of target proteins and is
CC       required for limb outgrowth and expression of the fibroblast
CC       growth factor FGF8. In the complex, may act as a substrate
CC       receptor. Regulates the assembly and neuronal surface expression
CC       of large-conductance calcium-activated potassium channels in brain
CC       regions involved in memory and learning via its interaction with
CC       KCNT1 (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Component of a DCX (DDB1-CUL4-X-box) protein ligase
CC       complex, at least composed of CRBN, CUL4A, DDB1 and RBX1.
CC       Interacts with KCNT1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Membrane; Peripheral membrane protein (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8C7D2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C7D2-2; Sequence=VSP_015210;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8C7D2-3; Sequence=VSP_039063;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain.
CC   -!- DEVELOPMENTAL STAGE: In brain, expression is abundant in the
CC       cerebellum, with less expression in the neocortical, hippocampus
CC       and striatum in adult. Neocortical expression increases from
CC       embryonic stages to adulthood.
CC   -!- PTM: Ubiquitinated, ubiquitination is mediated by its own DCX
CC       protein ligase complex (By similarity).
CC   -!- SIMILARITY: Belongs to the CRBN family.
CC   -!- SIMILARITY: Contains 1 Lon domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF35895.1; Type=Frameshift; Positions=27;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK050557; BAC34322.1; -; mRNA.
DR   EMBL; AK076144; BAC36214.1; -; mRNA.
DR   EMBL; AK077707; BAC36970.1; -; mRNA.
DR   EMBL; AK160219; BAE35697.1; -; mRNA.
DR   EMBL; BC046967; AAH46967.1; -; mRNA.
DR   EMBL; BC069905; AAH69905.1; -; mRNA.
DR   EMBL; BC086488; AAH86488.1; -; mRNA.
DR   EMBL; AF229032; AAF35895.1; ALT_FRAME; mRNA.
DR   IPI; IPI00123335; -.
DR   IPI; IPI00387238; -.
DR   IPI; IPI00956787; -.
DR   RefSeq; NP_067424.2; NM_021449.2.
DR   RefSeq; NP_780566.1; NM_175357.2.
DR   UniGene; Mm.290085; -.
DR   ProteinModelPortal; Q8C7D2; -.
DR   STRING; Q8C7D2; -.
DR   PRIDE; Q8C7D2; -.
DR   Ensembl; ENSMUST00000013882; ENSMUSP00000013882; ENSMUSG00000005362.
DR   Ensembl; ENSMUST00000049675; ENSMUSP00000061604; ENSMUSG00000005362.
DR   Ensembl; ENSMUST00000113239; ENSMUSP00000108865; ENSMUSG00000005362.
DR   GeneID; 58799; -.
DR   KEGG; mmu:58799; -.
DR   UCSC; uc009dda.1; mouse.
DR   UCSC; uc009ddb.1; mouse.
DR   CTD; 58799; -.
DR   MGI; MGI:1913277; Crbn.
DR   GeneTree; ENSGT00390000016404; -.
DR   HOVERGEN; HBG054571; -.
DR   InParanoid; Q8C7D2; -.
DR   OMA; HEWDENL; -.
DR   OrthoDB; EOG44XJGR; -.
DR   PhylomeDB; Q8C7D2; -.
DR   NextBio; 314364; -.
DR   ArrayExpress; Q8C7D2; -.
DR   Bgee; Q8C7D2; -.
DR   CleanEx; MM_CRBN; -.
DR   Genevestigator; Q8C7D2; -.
DR   GermOnline; ENSMUSG00000005362; Mus musculus.
DR   GO; GO:0031464; C:Cul4A-RING ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR   GO; GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   InterPro; IPR003111; Pept_S16_N.
DR   InterPro; IPR015947; PUA-like.
DR   Pfam; PF02190; LON; 1.
DR   SMART; SM00464; LON; 1.
DR   SUPFAM; SSF88697; PUA-like; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Membrane; Nucleus; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   CHAIN         1    445       Protein cereblon.
FT                                /FTId=PRO_0000076161.
FT   DOMAIN       83    320       Lon.
FT   VAR_SEQ       1     23       MAGEGDQQDAAHNMGNHLPLLPA -> MGNHLPLLP (in
FT                                isoform 2).
FT                                /FTId=VSP_015210.
FT   VAR_SEQ      23     23       Missing (in isoform 3).
FT                                /FTId=VSP_039063.
FT   CONFLICT     10     10       A -> R (in Ref. 3; AAF35895).
FT   CONFLICT     48     48       N -> D (in Ref. 3; AAF35895).
FT   CONFLICT     71     71       H -> P (in Ref. 1; BAC36214).
FT   CONFLICT     82     82       Q -> R (in Ref. 3; AAF35895).
FT   CONFLICT    127    127       A -> G (in Ref. 3; AAF35895).
FT   CONFLICT    202    202       L -> V (in Ref. 2; AAH86488).
FT   CONFLICT    310    310       R -> A (in Ref. 3; AAF35895).
FT   CONFLICT    317    317       I -> V (in Ref. 1; BAC36970).
FT   CONFLICT    439    439       D -> N (in Ref. 1; BAE35697).
SQ   SEQUENCE   445 AA;  50880 MW;  D66C2C3D50366E27 CRC64;
     MAGEGDQQDA AHNMGNHLPL LPADSEDEDD EIEMEVEDQD SKEARKPNII NFDTSLPTSH
     TYLGADMEEF HGRTLHDDDS CQVIPVLPEV LMILIPGQTL PLQLSHPQEV SMVRNLIQKD
     RTFAVLAYSN VQEREAQFGT TAEIYAYREE QEFGIEVVKV KAIGRQRFKV LELRTQSDGI
     QQAKVQILPE CVLPSTMSAV QLESLNKCQV FPSKPISWED QYSCKWWQKY QKRKFHCANL
     TSWPRWLYSL YDAETLMDRI KKQLREWDEN LKDDSLPENP IDFSYRVAAC LPIDDVLRIQ
     LLKIGSAIQR LRCELDIMNK CTSLCCKQCQ ETEITTKNEI FSLSLCGPMA AYVNPHGYVH
     ETLTVYKASN LNLIGRPSTV HSWFPGYAWT IAQCKICASH IGWKFTATKK DMSPQKFWGL
     TRSALLPTIP ETEDEISPDK VILCL
//
ID   PCYXL_MOUSE             Reviewed;         495 AA.
AC   Q8C7K6;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Prenylcysteine oxidase-like;
DE            EC=1.8.3.-;
DE   Flags: Precursor;
GN   Name=Pcyox1l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Probable oxidoreductase (By similarity).
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- SIMILARITY: Belongs to the prenylcysteine oxidase family.
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DR   EMBL; AK050006; BAC34029.1; -; mRNA.
DR   EMBL; BC060677; AAH60677.1; -; mRNA.
DR   IPI; IPI00226726; -.
DR   RefSeq; NP_766420.1; NM_172832.4.
DR   UniGene; Mm.234457; -.
DR   ProteinModelPortal; Q8C7K6; -.
DR   SMR; Q8C7K6; 27-100.
DR   PRIDE; Q8C7K6; -.
DR   Ensembl; ENSMUST00000025472; ENSMUSP00000025472; ENSMUSG00000024579.
DR   GeneID; 240334; -.
DR   KEGG; mmu:240334; -.
DR   UCSC; uc008fcm.1; mouse.
DR   CTD; 240334; -.
DR   MGI; MGI:3606062; Pcyox1l.
DR   eggNOG; roNOG13972; -.
DR   GeneTree; ENSGT00390000011206; -.
DR   HOGENOM; HBG447064; -.
DR   HOVERGEN; HBG053532; -.
DR   InParanoid; Q8C7K6; -.
DR   OMA; DWYLLNL; -.
DR   OrthoDB; EOG4TQM90; -.
DR   PhylomeDB; Q8C7K6; -.
DR   NextBio; 384562; -.
DR   ArrayExpress; Q8C7K6; -.
DR   Bgee; Q8C7K6; -.
DR   CleanEx; MM_PCYOX1L; -.
DR   Genevestigator; Q8C7K6; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016670; F:oxidoreductase activity, acting on a sulfur group of donors, oxygen as acceptor; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0030328; P:prenylcysteine catabolic process; IEA:InterPro.
DR   InterPro; IPR010795; Prenylcys_lyase.
DR   InterPro; IPR017046; Prenylcysteine_Oxase.
DR   Pfam; PF07156; Prenylcys_lyase; 1.
DR   PIRSF; PIRSF036292; Prenylcysteine_oxidase; 1.
PE   2: Evidence at transcript level;
KW   FAD; Glycoprotein; Oxidoreductase; Secreted; Signal.
FT   SIGNAL        1     22       By similarity.
FT   CHAIN        23    495       Prenylcysteine oxidase-like.
FT                                /FTId=PRO_0000280287.
FT   CARBOHYD    185    185       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    343    343       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   495 AA;  54875 MW;  DA86F56E6B108198 CRC64;
     MARAAPLLAV LATVLTTAAA GGDAPPGKIA VIGAGIGGSA VAHFLQQHFG PRVQIVVYEK
     GTVGGRLATI SVNKQNYESG AASFHSLSLH MQDFVKLLGL RQRREVVGRS AIFGGEHFVL
     EETDWYLLNL FRLWWYYGIS FLRLQMWVEE VMEKFMRIYK YQAHGYAFSG VEELLYSLGE
     ATFVNMTQRS VAESLLQVGV TQRFIDDVVS AVLRASYGQS ASMPAFAGAM SLAGAQGNLW
     SVEGGNKLVC SGLLKLAKAT VIHATVTSVT LHSTEGKALY QVAYESDKGN SSDFYDIVVI
     ATPLHLDNSS NNNITFEGFT PPIEDIQGSF QPTVVSLVHG YLNSSYFGFP DPKLFPFANI
     LTTDFPSFFC TLDNICPVNI SASFRRKQPQ EAAVWRVQSP KPLFRTELKT LFRSYYSVQT
     AEWQAHPLYG SRRTLPRFAL HDQLFYLNAL EWAASSVEVT AVAAKNVALL AYNRWYQDLD
     KIDQKDLIHK VKTEL
//
ID   TRIM9_MOUSE             Reviewed;         817 AA.
AC   Q8C7M3; Q6ZQE5; Q80WT6; Q8C7Z4; Q8CC32; Q8CEG2; Q99PQ3;
DT   04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   04-AUG-2003, sequence version 2.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=E3 ubiquitin-protein ligase TRIM9;
DE            EC=6.3.2.-;
DE   AltName: Full=Tripartite motif-containing protein 9;
GN   Name=Trim9; Synonyms=Kiaa0282;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Diencephalon, Head, and Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 317-679 (ISOFORM 5).
RX   MEDLINE=21231161; PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA   Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA   Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A.,
RA   Minucci S., Pelicci P.G., Ballabio A.;
RT   "The tripartite motif family identifies cell compartments.";
RL   EMBO J. 20:2140-2151(2001).
RN   [5]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=21959294; PubMed=11960705; DOI=10.1016/S0925-4773(02)00013-8;
RA   Berti C., Messali S., Ballabio A., Reymond A., Meroni G.;
RT   "TRIM9 is specifically expressed in the embryonic and adult nervous
RT   system.";
RL   Mech. Dev. 113:159-162(2002).
RN   [6]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=20085810; DOI=10.1016/j.nbd.2010.01.007;
RA   Tanji K., Kamitani T., Mori F., Kakita A., Takahashi H.,
RA   Wakabayashi K.;
RT   "TRIM9, a novel brain-specific E3 ubiquitin ligase, is repressed in
RT   the brain of Parkinson's disease and dementia with Lewy bodies.";
RL   Neurobiol. Dis. 38:210-218(2010).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which ubiquitinates itself
CC       in cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a
CC       targeting signal for proteasomal degradation. May play a role in
CC       regulation of neuronal functions. May act as a regulator of
CC       synaptic vesicle exocytosis by controlling the availability of
CC       SNAP25 for the SNARE complex formation (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with SNAP25 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell projection, dendrite.
CC       Cytoplasmic vesicle, secretory vesicle, synaptic vesicle (By
CC       similarity). Cell junction, synapse (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity). Note=Enriched at synaptic terminals
CC       where it exists in a soluble form and a synaptic vesicle-
CC       associated form. Associated with the cytoskeleton (By similarity).
CC       Found in proximal dendrites of pyramidal neurons in the cerebral
CC       cortex and hippocampus, and Purkinje cells in the cerebellum.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1;
CC         IsoId=Q8C7M3-1; Sequence=Displayed;
CC         Note=May be due to an intron retention;
CC       Name=2;
CC         IsoId=Q8C7M3-2; Sequence=VSP_007930, VSP_007935;
CC         Note=May be due to a competing acceptor splice site and to an
CC         exon skipping;
CC       Name=3;
CC         IsoId=Q8C7M3-3; Sequence=VSP_007931, VSP_007935, VSP_007936;
CC         Note=May be due to a competing donnor splice site and ?;
CC       Name=4;
CC         IsoId=Q8C7M3-4; Sequence=VSP_007937, VSP_007938;
CC         Note=May be due to an intron retention;
CC       Name=5;
CC         IsoId=Q8C7M3-5; Sequence=VSP_007932;
CC         Note=May be due to exon skipping;
CC       Name=6;
CC         IsoId=Q8C7M3-6; Sequence=VSP_007933, VSP_007934;
CC         Note=May be due to an exon inclusion;
CC   -!- TISSUE SPECIFICITY: Brain. Expression is higher in the cerebral
CC       cortex and hippocampus (at protein level). Its expression is
CC       mainly confined to the central nervous system. The developing
CC       neocortex, the dorsal thalamus, the midbrain, the basal area of
CC       the hindbrain and spinal cord show high level of expression during
CC       embryogenesis. In adult brain, it is detected in the Purkinje
CC       cells of the cerebellum, in the hippocampus, and in the cortex.
CC   -!- DEVELOPMENTAL STAGE: First seen at E9.5. From E9.5 to E11.5, it
CC       remains uniformly present in the ventral part of the entire
CC       neuroepithelium and in the dorsal root ganglia. A more restricted
CC       central nervous system (CNS) expression is observed at E13.5 and
CC       E15.5 when it is present in specific regions of the forebrain,
CC       midbrain, hindbrain and spinal cord.
CC   -!- DOMAIN: The coiled coil domain mediates the interaction with the
CC       N-terminal t-SNARE domain of SNAP25 (By similarity).
CC   -!- PTM: Auto-ubiquitinated (By similarity).
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC   -!- SIMILARITY: Contains 2 B box-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 B30.2/SPRY domain.
CC   -!- SIMILARITY: Contains 1 COS domain.
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97919.1; Type=Erroneous initiation;
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DR   EMBL; AK049907; BAC33982.1; -; mRNA.
DR   EMBL; AK034029; BAC28552.1; -; mRNA.
DR   EMBL; AK028280; BAC25854.1; -; mRNA.
DR   EMBL; AK048875; BAC33479.1; -; mRNA.
DR   EMBL; AK129109; BAC97919.1; ALT_INIT; mRNA.
DR   EMBL; BC052034; AAH52034.1; -; mRNA.
DR   EMBL; AF220039; AAG53493.1; -; mRNA.
DR   IPI; IPI00337062; -.
DR   IPI; IPI00337064; -.
DR   IPI; IPI00337066; -.
DR   IPI; IPI00354319; -.
DR   IPI; IPI00408580; -.
DR   IPI; IPI00470115; -.
DR   RefSeq; NP_001103672.1; NM_001110202.1.
DR   RefSeq; NP_001103673.1; NM_001110203.1.
DR   RefSeq; NP_444397.2; NM_053167.3.
DR   UniGene; Mm.184012; -.
DR   ProteinModelPortal; Q8C7M3; -.
DR   SMR; Q8C7M3; 2-36, 160-268, 436-537.
DR   STRING; Q8C7M3; -.
DR   PhosphoSite; Q8C7M3; -.
DR   PRIDE; Q8C7M3; -.
DR   Ensembl; ENSMUST00000081485; ENSMUSP00000080204; ENSMUSG00000021071.
DR   Ensembl; ENSMUST00000110520; ENSMUSP00000106149; ENSMUSG00000021071.
DR   Ensembl; ENSMUST00000110522; ENSMUSP00000106151; ENSMUSG00000021071.
DR   GeneID; 94090; -.
DR   KEGG; mmu:94090; -.
DR   UCSC; uc007ntp.1; mouse.
DR   UCSC; uc007nts.1; mouse.
DR   CTD; 94090; -.
DR   MGI; MGI:2137354; Trim9.
DR   GeneTree; ENSGT00560000076722; -.
DR   HOVERGEN; HBG062305; -.
DR   InParanoid; Q8C7M3; -.
DR   OrthoDB; EOG46HG97; -.
DR   PhylomeDB; Q8C7M3; -.
DR   NextBio; 352073; -.
DR   ArrayExpress; Q8C7M3; -.
DR   Bgee; Q8C7M3; -.
DR   CleanEx; MM_TRIM9; -.
DR   Genevestigator; Q8C7M3; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR   GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   InterPro; IPR001870; B302/SPRY.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR017903; COS_domain.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003877; SPRY_rcpt.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 2.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 2.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
DR   SUPFAM; SSF49265; FN_III-like; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS51262; COS; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50119; ZF_BBOX; 2.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell projection; Coiled coil;
KW   Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Ligase; Metal-binding;
KW   Phosphoprotein; Repeat; Synapse; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    817       E3 ubiquitin-protein ligase TRIM9.
FT                                /FTId=PRO_0000056209.
FT   DOMAIN      374    432       COS.
FT   DOMAIN      439    532       Fibronectin type-III.
FT   DOMAIN      613    794       B30.2/SPRY.
FT   ZN_FING      10     50       RING-type.
FT   ZN_FING     163    212       B box-type 1.
FT   ZN_FING     224    266       B box-type 2.
FT   COILED      273    340       Potential.
FT   MOD_RES      46     46       Phosphoserine (By similarity).
FT   VAR_SEQ     535    630       Missing (in isoform 5).
FT                                /FTId=VSP_007932.
FT   VAR_SEQ     535    608       Missing (in isoform 3).
FT                                /FTId=VSP_007931.
FT   VAR_SEQ     535    536       AA -> GR (in isoform 6).
FT                                /FTId=VSP_007933.
FT   VAR_SEQ     535    535       Missing (in isoform 2).
FT                                /FTId=VSP_007930.
FT   VAR_SEQ     537    817       Missing (in isoform 6).
FT                                /FTId=VSP_007934.
FT   VAR_SEQ     546    565       DTDSEEQTLPFPVPSERLPL -> GMCGWRQSILRLLGIVL
FT                                LVD (in isoform 4).
FT                                /FTId=VSP_007937.
FT   VAR_SEQ     566    817       Missing (in isoform 4).
FT                                /FTId=VSP_007938.
FT   VAR_SEQ     714    732       MYVDNNRSWFMHNNSHTNR -> I (in isoform 2
FT                                and isoform 3).
FT                                /FTId=VSP_007935.
FT   VAR_SEQ     788    817       SLWAPGLRACSGCYFKVCPGAVKSPQAPAP -> TLHTGLP
FT                                VPDFYSSRASIA (in isoform 3).
FT                                /FTId=VSP_007936.
FT   CONFLICT     27     27       H -> D (in Ref. 1; BAC28552).
FT   CONFLICT    251    251       Q -> H (in Ref. 1; BAC33982).
FT   CONFLICT    254    254       E -> Q (in Ref. 1; BAC33982).
FT   CONFLICT    319    319       Q -> R (in Ref. 4; AAG53493).
SQ   SEQUENCE   817 AA;  90870 MW;  F23A355F6FF5762D CRC64;
     MEEMEEELKC PVCGSFYREP IILPCSHNLC QACARNILVQ TPESESPQSR RASGSGVSDY
     DYLDLDKMSL YSEADSGYGS YGGFASAPTT PCQKSPNGVR VFPPAMPPPP THLSPALAPV
     PRNSCITCPQ CHRSLILDDR GLRGFPKNRV LEGVIDRYQQ SKAAALKCQL CEKAPKEATV
     MCEQCDVFYC DPCRLRCHPP RGPLAKHRLV PPAQGRVSRR LSPRKVSTCT DHELENHSMY
     CVQCKMPVCY QCLEEGKHSS HEVKALGAMW KLHKSQLSQA LNGLSDRAKE AKEFLVQLRT
     MVQQIQENSV EFEACLVAQC DALIDALNRR KAQLLARVNK EHEHKLKVVR DQISHCTVKL
     RQTTGLMEYC LEVIKENDPS GFLQISDALI RRVHLTEDQW GKGTLTPRMT TDFDLSLDNS
     PLLQSIHQLD FVQVKASSPV PATPILQLEE CCTHNNSATL SWKQPPLSTV AADGYILELD
     DGSGGQFREV YVGKETMCTV DGLHFNSTYN ARVKAFNKTG VSPYSKTLVL QTSEAAGAHE
     TKPMKDTDSE EQTLPFPVPS ERLPLRRMSP FSSTLNLQPS FPGRSYFDFR SSPHQLSLHS
     SLQSLNAPGC NFETQSASYS QLVDIKKLLA VAWFAFDPGS AHSDIIFSND NLTVTCSSYD
     DRVVLGKTGF SKGVHYWELT IDRYDNHPDP AFGVARIDVM KDMMLGKDDK AWAMYVDNNR
     SWFMHNNSHT NRTEGGITKG ATIGVLLDLN RKTLTFFVNN EQQGPIAFEN VEGLFFPAVS
     LNRNVQVSLW APGLRACSGC YFKVCPGAVK SPQAPAP
//
ID   K0090_MOUSE             Reviewed;         997 AA.
AC   Q8C7X2; B2RTJ5; Q3TCG4; Q6ZQJ4; Q8K3W8;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Uncharacterized protein KIAA0090;
DE   Flags: Precursor;
GN   Name=Kiaa0090;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   STRAIN=BALB/c; TISSUE=Heart;
RA   Chen X.G., Li Y.;
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-896 (ISOFORM 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-997 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-917, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8C7X2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C7X2-2; Sequence=VSP_020331;
CC       Name=3;
CC         IsoId=Q8C7X2-3; Sequence=VSP_020330;
CC   -!- SIMILARITY: Contains 1 DUF1620 domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF525925; AAM88856.1; -; mRNA.
DR   EMBL; AK049061; BAC33530.1; -; mRNA.
DR   EMBL; AK170739; BAE41992.1; -; mRNA.
DR   EMBL; BC139366; AAI39367.1; -; mRNA.
DR   EMBL; AK129052; BAC97862.1; -; mRNA.
DR   IPI; IPI00226932; -.
DR   IPI; IPI00720171; -.
DR   IPI; IPI00785382; -.
DR   RefSeq; NP_001034289.1; NM_001039200.1.
DR   RefSeq; NP_666269.2; NM_146157.3.
DR   UniGene; Mm.271956; -.
DR   ProteinModelPortal; Q8C7X2; -.
DR   SMR; Q8C7X2; 51-123.
DR   STRING; Q8C7X2; -.
DR   PRIDE; Q8C7X2; -.
DR   Ensembl; ENSMUST00000042096; ENSMUSP00000049034; ENSMUSG00000078517.
DR   Ensembl; ENSMUST00000082262; ENSMUSP00000080888; ENSMUSG00000078517.
DR   GeneID; 230866; -.
DR   KEGG; mmu:230866; -.
DR   UCSC; uc008vmg.1; mouse.
DR   UCSC; uc008vmh.1; mouse.
DR   MGI; MGI:2443696; C230096C10Rik.
DR   GeneTree; ENSGT00390000002461; -.
DR   HOGENOM; HBG355887; -.
DR   HOVERGEN; HBG057156; -.
DR   InParanoid; Q8C7X2; -.
DR   OMA; FYDARKP; -.
DR   OrthoDB; EOG4NKBTT; -.
DR   NextBio; 380232; -.
DR   ArrayExpress; Q8C7X2; -.
DR   Bgee; Q8C7X2; -.
DR   CleanEx; MM_C230096C10RIK; -.
DR   Genevestigator; Q8C7X2; -.
DR   GermOnline; ENSMUSG00000066036; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR011678; DUF1620.
DR   InterPro; IPR011047; Quino_AlcDH-like.
DR   Gene3D; G3DSA:2.140.10.10; Quinoprotein_alc_DH-like; 1.
DR   Pfam; PF07774; DUF1620; 1.
DR   SUPFAM; SSF50998; Quin_alc_DH_like; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Glycoprotein; Membrane; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     22       Potential.
FT   CHAIN        23    997       Uncharacterized protein KIAA0090.
FT                                /FTId=PRO_0000248598.
FT   TOPO_DOM     23    962       Extracellular (Potential).
FT   TRANSMEM    963    983       Helical; (Potential).
FT   TOPO_DOM    984    997       Cytoplasmic (Potential).
FT   DOMAIN      723    996       DUF1620.
FT   CARBOHYD    917    917       N-linked (GlcNAc...).
FT   VAR_SEQ       1    635       Missing (in isoform 3).
FT                                /FTId=VSP_020330.
FT   VAR_SEQ     479    481       Missing (in isoform 2).
FT                                /FTId=VSP_020331.
FT   CONFLICT     20     20       A -> V (in Ref. 4; BAC97862).
SQ   SEQUENCE   997 AA;  111605 MW;  0EBB28811D94B39F CRC64;
     MAVAVASGFW IWAAVLLVPA AAVYEDQVGK FDWRQQYVGK IKFASLEFSP GSKKLVVATE
     KNVIAALNSR TGEILWRHVD KGTAEGAVDA MLVHGQDAIT VSNGGRLMRS WETNIGGLNW
     EITLDTGSFQ ALGLVGLQES VRYIAVLKKT TLTLHHLSSG HLKWVEHLPE SDSILYQMVY
     SYGSGVVWAL GIVPFSHVNI VKFNVEDGEI VQQVRVWTPW LQHLTGACGV VDEAVLVCPD
     PSSHSLHTLA LETEWELRQI PLQSPDLEFG SGFQPQVLPT QPSPVAPSRA QFFLQLSPSH
     YALLHYHHGA VTLLKNFPQA TLVSFATTGE KTVAAVMTCR TEVQKPVSAG DGSVASFPET
     SGAQDSLACF NQTYTINLYL VETGRRLLDT SISFSLEQKG TRPEQLYIQV FLKKDDSVGY
     RALVQTQDHL QLFLQQLAGK VVLWSREESL AEVVCLEMVD LPLTGAQAEL EGEFGKKAAI
     QDGLLGMFLK RLSSQLILLQ AWTSHLWKMF YDARKPRSQI KNEINIDTLA RDEFNLQKMM
     VTVTASGKLF GIESSSGTIL WKQYLPNVKP DSSFKLMVQR TTAHFPHPPQ CTLLVKDKET
     GMSSLFVFNP IFGKWSQVAP PVLKRPILQS LLLPVMDQDY AKVLLLVDDE YKVTAFPATR
     NVLRQLHELA PSIFFYLVDA EQGRLSGYQL RKDLTTELSW ELTIPPEVQR VVKVKGKRSS
     EHVHSQGRVM GDRSVLYKSL NPNLLAVVTE STDVHHERTF IGIFLIDGVT GRIIHSSVQK
     KARGPVHLVH SENWVVYQYW NSKARRNELT ALELYEGTEQ YNATAFSSLD RPQLPQVLQQ
     SYIFPSSISA MEATITERGI TSRHLLIGLP SGAILSLPKA LLDPRRPEIP TEQSREENLI
     PYSPDVQVHA ERFINYNQTV SRMRGIYTAP SGLESTCLVV AYGLDIYQTR VYPSKQFDVL
     KDDYDYVLIS SVLFGLVFAT MITKRLAQVK LLNRAWR
//
ID   SPICE_MOUSE             Reviewed;         860 AA.
AC   Q8C804; Q8K3I7;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Spindle and centriole-associated protein 1;
DE   AltName: Full=Coiled-coil domain-containing protein 52;
GN   Name=Spice1; Synonyms=Ccdc52, D16Ertd480e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RA   Guo J.H.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH CEP120.
RX   PubMed=20360068; DOI=10.1126/science.1181348;
RA   Hutchins J.R., Toyoda Y., Hegemann B., Poser I., Heriche J.K.,
RA   Sykora M.M., Augsburg M., Hudecz O., Buschhorn B.A., Bulkescher J.,
RA   Conrad C., Comartin D., Schleiffer A., Sarov M., Pozniakovsky A.,
RA   Slabicki M.M., Schloissnig S., Steinmacher I., Leuschner M.,
RA   Ssykor A., Lawo S., Pelletier L., Stark H., Nasmyth K., Ellenberg J.,
RA   Durbin R., Buchholz F., Mechtler K., Hyman A.A., Peters J.M.;
RT   "Systematic analysis of human protein complexes identifies chromosome
RT   segregation proteins.";
RL   Science 328:593-599(2010).
CC   -!- FUNCTION: Regulator required for centriole duplication, for proper
CC       bipolar spindle formation and chromosome congression in mitosis
CC       (By similarity).
CC   -!- SUBUNIT: Interacts with CEP120.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome,
CC       centriole (By similarity). Cytoplasm, cytoskeleton, spindle (By
CC       similarity).
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK048789; BAC33458.1; -; mRNA.
DR   EMBL; AY099108; AAM34496.1; -; mRNA.
DR   EMBL; BC052381; AAH52381.1; -; mRNA.
DR   EMBL; BC056960; AAH56960.1; -; mRNA.
DR   IPI; IPI00170090; -.
DR   RefSeq; NP_653133.3; NM_144550.4.
DR   UniGene; Mm.24035; -.
DR   IntAct; Q8C804; 2.
DR   PhosphoSite; Q8C804; -.
DR   PRIDE; Q8C804; -.
DR   Ensembl; ENSMUST00000050897; ENSMUSP00000058832; ENSMUSG00000043065.
DR   GeneID; 212514; -.
DR   KEGG; mmu:212514; -.
DR   CTD; 212514; -.
DR   MGI; MGI:1196252; Ccdc52.
DR   GeneTree; ENSGT00390000006207; -.
DR   HOGENOM; HBG282506; -.
DR   HOVERGEN; HBG102011; -.
DR   InParanoid; Q8C804; -.
DR   OMA; RWRVSHM; -.
DR   OrthoDB; EOG4G7BXW; -.
DR   NextBio; 373598; -.
DR   ArrayExpress; Q8C804; -.
DR   Bgee; Q8C804; -.
DR   CleanEx; MM_CCDC52; -.
DR   Genevestigator; Q8C804; -.
DR   GO; GO:0005814; C:centriole; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Mitosis; Phosphoprotein.
FT   CHAIN         1    860       Spindle and centriole-associated protein
FT                                1.
FT                                /FTId=PRO_0000282414.
FT   COILED      383    439       Potential.
FT   COILED      729    757       Potential.
FT   MOD_RES     236    236       Phosphothreonine (By similarity).
FT   MOD_RES     648    648       Phosphoserine (By similarity).
FT   MOD_RES     765    765       Phosphoserine (By similarity).
FT   MOD_RES     769    769       Phosphoserine (By similarity).
FT   CONFLICT    482    482       E -> G (in Ref. 1; BAC33458).
SQ   SEQUENCE   860 AA;  95645 MW;  DC919B72DCE5D621 CRC64;
     MSLIRVNRFG PRGGGRKTLK VKKKAAVRQE WDNTVNDLTV HRATPEDLVR RHEMHKSKNR
     ALVHWELQEK ALKRKWKKQK PETSSLEKRK LSIMKEILSD QYLTQDVLEK SDHLMAAAKG
     LFADVPRKRT GFPNVTRAPD SSQSHTGINQ DPVTQSILNE SIIEPQALNE VDDAGEQSTA
     HSQSEDSENE LPNSLSQHSN RSTERFLHQL KEENSELINQ LWTDIQQKIA TQSQRTPPGS
     PSSELSAEDQ KAALNATDAV KRIQAGPQPE EAAEPVDFSS SYLGQVLNTR KQKPLLAKVK
     RKQDMHAASK QKTNMLSSST ASADRPSSTG SSLDVLKHVI HEVEHEMEEY ERCTGREVTG
     LQGGQGLTGF TLSLVSSLCR LVRYLKESEI QLRKEVETRQ QLEQMLGDHR ELIDALTAEI
     LSLREENSTM QARLQQYMVT TDEQLISLTH AIKNCPVINN SRQESQAPER AAMGRRLVDN
     VEGPVISSNG SMPLMFRGEE VVEFPQEELP VKLSQGPTPT ENLNLANNFP THIFEPAVML
     TPPRQKSNSE FSPLQDVLRR TVQTRPAPRI PPTVEVIEKE QNWEKKALPI DPDIQNSSEE
     NRLFTQRWRV SHMGEDLENK GQPAFVSLSQ PPCSSLPSTQ QPRNPVLSEE PTVLGDGQQL
     RTSEALVQRK DIMARIAELT LQNSAIKAHL NNITSSGGEQ GDGLREPRKQ GSASEVSTNF
     PAVQSLTPSS MEERIAELNR QSMEARSKLL QLIEQQKLVG LNLSSSPVSP VESPLRAWAE
     EGKRTIEVSV PGMEASESSK CNTVSPVSGN SSRRSSGAIS NSCSPLNATS GSGKFTPVNP
     RTKTEKKNEE GWFALSAHIP
//
ID   T200A_MOUSE             Reviewed;         491 AA.
AC   Q8C817; Q69Z67; Q8CCL5;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Transmembrane protein 200A;
GN   Name=Tmem200a; Synonyms=Kiaa1913;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the TMEM200 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32577.1; Type=Erroneous initiation;
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DR   EMBL; AK173299; BAD32577.1; ALT_INIT; mRNA.
DR   EMBL; AK032569; BAC27929.1; -; mRNA.
DR   EMBL; AK048673; BAC33418.1; -; mRNA.
DR   IPI; IPI00405747; -.
DR   RefSeq; NP_084157.2; NM_029881.3.
DR   UniGene; Mm.266260; -.
DR   ProteinModelPortal; Q8C817; -.
DR   PhosphoSite; Q8C817; -.
DR   PRIDE; Q8C817; -.
DR   Ensembl; ENSMUST00000066049; ENSMUSP00000064080; ENSMUSG00000049420.
DR   GeneID; 77220; -.
DR   KEGG; mmu:77220; -.
DR   UCSC; uc007erw.1; mouse.
DR   CTD; 77220; -.
DR   MGI; MGI:1924470; Tmem200a.
DR   eggNOG; maNOG06500; -.
DR   GeneTree; ENSGT00530000063698; -.
DR   HOGENOM; HBG713843; -.
DR   HOVERGEN; HBG102357; -.
DR   InParanoid; Q8C817; -.
DR   OMA; KRQDSAR; -.
DR   OrthoDB; EOG48GW3V; -.
DR   NextBio; 346612; -.
DR   ArrayExpress; Q8C817; -.
DR   Bgee; Q8C817; -.
DR   Genevestigator; Q8C817; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR018787; DUF2371_TMEM200.
DR   Pfam; PF10177; DUF2371; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    491       Transmembrane protein 200A.
FT                                /FTId=PRO_0000294341.
FT   TOPO_DOM      1     61       Cytoplasmic (Potential).
FT   TRANSMEM     62     82       Helical; (Potential).
FT   TOPO_DOM     83    126       Extracellular (Potential).
FT   TRANSMEM    127    147       Helical; (Potential).
FT   TOPO_DOM    148    491       Cytoplasmic (Potential).
FT   MOD_RES     225    225       Phosphoserine.
FT   CARBOHYD    100    100       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    194    194       V -> E (in Ref. 2; BAC27929).
SQ   SEQUENCE   491 AA;  54008 MW;  A06DCE2D0CCC9E3B CRC64;
     MIATGGVITG LAALKRQDSA RSQQHINLSP LPATQDQKPV RRRPRADVVV VRGKIRLYSP
     SGFFLILGVL VSIIGIAMAV LGYWPQKEHF IDAETTLSTN ETQVVRNQGG VVVRFFEQHL
     HSDKMKMLGP FTMGIGIFIF ICANAILHEN RDKETKIIHM RDIYSTVIDI HTLRLKEQKQ
     ANGLYAGLLG DTEVKQNGSP CASRLAATTL ASFSGMRNSF RVDSSVEEDE LMLTESKSLG
     HLMPPLLSDS AVSVFGLYPP PAKATDDKAS SSKKCDTKSI VSSSISAFTL PVIKLNNCVI
     DEPSIDSITE VADNLKTRSR NLSMDSLVVP LPSSGESFQP AVTLLPRNNS VGESLSSQYK
     SSVALGPGTG QLLSPGAARR QFGSNTSLHL LSSHSKSLDL DRGPSTLTVH AEQRKHPSWP
     RLDRSNSKGY MRLENKEDPM DRLLVPQTAI KKDFTNKEKL LMISRSHNNL SFEHDEFLSN
     NLKRGTSETR F
//
ID   UBA3_MOUSE              Reviewed;         462 AA.
AC   Q8C878; O88598; Q9D6B7;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=NEDD8-activating enzyme E1 catalytic subunit;
DE            EC=6.3.2.-;
DE   AltName: Full=NEDD8-activating enzyme E1C;
DE   AltName: Full=Ubiquitin-activating enzyme E1C;
DE   AltName: Full=Ubiquitin-like modifier-activating enzyme 3;
DE            Short=Ubiquitin-activating enzyme 3;
GN   Name=Uba3; Synonyms=Ube1c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic head, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-462 (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 9-462 (ISOFORM 1).
RC   TISSUE=Liver;
RX   MEDLINE=99223531; PubMed=10207026; DOI=10.1074/jbc.274.17.12036;
RA   Gong L., Yeh E.T.H.;
RT   "Identification of the activating and conjugating enzymes of the NEDD8
RT   conjugation pathway.";
RL   J. Biol. Chem. 274:12036-12042(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 9-462 (ISOFORM 1), AND FUNCTION.
RC   STRAIN=C57BL/6;
RX   MEDLINE=21562688; PubMed=11696557; DOI=10.1083/jcb.200104035;
RA   Tateishi K., Omata M., Tanaka K., Chiba T.;
RT   "The NEDD8 system is essential for cell cycle progression and
RT   morphogenetic pathway in mice.";
RL   J. Cell Biol. 155:571-580(2001).
CC   -!- FUNCTION: Catalytic subunit of the dimeric UBA3-NAE1 E1 enzyme. E1
CC       activates NEDD8 by first adenylating its C-terminal glycine
CC       residue with ATP, thereafter linking this residue to the side
CC       chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester
CC       and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine
CC       of UBE2M. Down-regulates steroid receptor activity. Necessary for
CC       cell cycle progression.
CC   -!- ENZYME REGULATION: Binding of TP53BP2 to the regulatory subunit
CC       NAE1 decreases activity (By similarity).
CC   -!- PATHWAY: Protein modification; protein neddylation.
CC   -!- SUBUNIT: Heterodimer of UBA3 and NAE1. Interacts with NEDD8, UBE2F
CC       and UBE2M. Binds ESR1 and ESR2 with bound steroid ligand (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8C878-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C878-2; Sequence=VSP_010787;
CC   -!- DISEASE: Note=Defects in Uba3 are a cause of embryonic lethality.
CC       Mouse embryos deficient in Uba3 die at the preimplantation stage.
CC   -!- MISCELLANEOUS: Arg-211 acts as a selectivity gate, preventing
CC       misactivation of ubiquitin by this NEDD8-specific E1 complex (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA3
CC       subfamily.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK014433; BAB29346.1; -; mRNA.
DR   EMBL; AK032514; BAC27905.1; -; mRNA.
DR   EMBL; AK048148; BAC33258.1; -; mRNA.
DR   EMBL; BC002002; AAH02002.1; -; mRNA.
DR   EMBL; AF077330; AAC27323.1; -; mRNA.
DR   EMBL; AY029181; AAK33015.1; -; mRNA.
DR   IPI; IPI00226943; -.
DR   IPI; IPI00453622; -.
DR   UniGene; Mm.277626; -.
DR   ProteinModelPortal; Q8C878; -.
DR   SMR; Q8C878; 33-462.
DR   STRING; Q8C878; -.
DR   PRIDE; Q8C878; -.
DR   Ensembl; ENSMUST00000089287; ENSMUSP00000086701; ENSMUSG00000030061.
DR   UCSC; uc009daq.1; mouse.
DR   MGI; MGI:1341217; Uba3.
DR   eggNOG; roNOG10492; -.
DR   GeneTree; ENSGT00550000074831; -.
DR   HOGENOM; HBG521753; -.
DR   HOVERGEN; HBG082736; -.
DR   InParanoid; Q8C878; -.
DR   PhylomeDB; Q8C878; -.
DR   ArrayExpress; Q8C878; -.
DR   Bgee; Q8C878; -.
DR   CleanEx; MM_UBA3; -.
DR   Genevestigator; Q8C878; -.
DR   GermOnline; ENSMUSG00000030061; Mus musculus.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019781; F:NEDD8 activating enzyme activity; TAS:MGI.
DR   GO; GO:0007113; P:endomitotic cell cycle; IMP:MGI.
DR   GO; GO:0045116; P:protein neddylation; IEA:InterPro.
DR   GO; GO:0051726; P:regulation of cell cycle; IMP:MGI.
DR   InterPro; IPR014929; E2_binding.
DR   InterPro; IPR009036; Molybdenum_cofac_synth_MoeB.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR023318; Ub_act_enz_dom_a.
DR   InterPro; IPR000127; UBact_repeat.
DR   InterPro; IPR019572; Ubiquitin-activating_enzyme.
DR   InterPro; IPR018074; UBQ-activ_enz_E1_AS.
DR   Gene3D; G3DSA:1.10.10.520; G3DSA:1.10.10.520; 1.
DR   Gene3D; G3DSA:3.10.20.260; G3DSA:3.10.20.260; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 2.
DR   Pfam; PF08825; E2_bind; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   Pfam; PF10585; UBA_e1_thiolCys; 1.
DR   Pfam; PF02134; UBACT; 1.
DR   SUPFAM; SSF69572; MoeB; 1.
DR   PROSITE; PS00536; UBIQUITIN_ACTIVAT_1; FALSE_NEG.
DR   PROSITE; PS00865; UBIQUITIN_ACTIVAT_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cell cycle; Ligase;
KW   Nucleotide-binding; Ubl conjugation pathway.
FT   CHAIN         1    462       NEDD8-activating enzyme E1 catalytic
FT                                subunit.
FT                                /FTId=PRO_0000194942.
FT   NP_BIND     100    124       ATP (By similarity).
FT   NP_BIND     148    171       ATP (By similarity).
FT   REGION       53     70       Interaction with UBE2M N-terminus (By
FT                                similarity).
FT   REGION      157    161       Interaction with UBE2M N-terminus (By
FT                                similarity).
FT   REGION      192    217       Interaction with UBE2M N-terminus (By
FT                                similarity).
FT   REGION      227    229       Interaction with NEDD8 (By similarity).
FT   REGION      242    248       Interaction with NAE1 (By similarity).
FT   REGION      292    295       Interaction with NAE1 (By similarity).
FT   REGION      331    338       Interaction with UBE2M N-terminus (By
FT                                similarity).
FT   REGION      352    357       Interaction with NEDD8 (By similarity).
FT   REGION      368    462       Interaction with UBE2M core domain (By
FT                                similarity).
FT   ACT_SITE    237    237       Glycyl thioester intermediate (By
FT                                similarity).
FT   SITE        211    211       Determines specificity for NEDD8 (By
FT                                similarity).
FT   VAR_SEQ     396    462       Missing (in isoform 2).
FT                                /FTId=VSP_010787.
FT   CONFLICT    147    147       K -> E (in Ref. 1; BAB29346).
FT   CONFLICT    334    334       S -> G (in Ref. 1; BAB29346).
FT   CONFLICT    397    397       I -> M (in Ref. 3; BAC27905/AAH02002/
FT                                AAC27323/AAK33015).
SQ   SEQUENCE   462 AA;  51719 MW;  403208F9E02F614E CRC64;
     MADGEEPEKK RRRIEELLAE KMAVDGGCGD TGDWEGRWNH VKKFLERSGP FTHPDFEPST
     ESLQFLLDTC KVLVIGAGGL GCELLKNLAL SGFRQIHVID MDTIDVSNLN RQFLFRPKDV
     GRPKAEVAAE FLNDRVPNCN VVPHFNKIQD FNDTFYRQFH IIVCGLDSII ARRWINGMLI
     SLLNYEDGVL DPSSIVPLID GGTEGFKGNA RVILPGMTAC IECTLELYPP QVNFPMCTIA
     SMPRLPEHCI EYVRMLQWPK EQPFGDGVPL DGDDPEHIQW IFQKSIERAS QYNIRGVTYR
     LTQGVVKRII PAVASTNAVI AAVCATEVFK IATSAYIPLN NYLVFNDVDG LYTYTFEAER
     KENCPACSQL PQNIQFSPSA KLQEVLDYLT NSASLQIKSP AITATLEGKN RTLYLQSVTS
     IEERTRPNLS KTLKELGLVD GQELAVADVT TPQTVLFKLH FT
//
ID   Q8C8C0_MOUSE            Unreviewed;       694 AA.
AC   Q8C8C0;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Mctp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 3 C2 domains.
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DR   EMBL; AK047562; BAC33087.1; -; mRNA.
DR   IPI; IPI00405518; -.
DR   RefSeq; NP_084450.2; NM_030174.2.
DR   UniGene; Mm.316249; -.
DR   HSSP; Q9JKS6; 1RH8.
DR   ProteinModelPortal; Q8C8C0; -.
DR   SMR; Q8C8C0; 3-441.
DR   PhosphoSite; Q8C8C0; -.
DR   Ensembl; ENSMUST00000046098; ENSMUSP00000039169; ENSMUSG00000021596.
DR   Ensembl; ENSMUST00000109583; ENSMUSP00000105212; ENSMUSG00000021596.
DR   Ensembl; ENSMUST00000125209; ENSMUSP00000118958; ENSMUSG00000021596.
DR   GeneID; 78771; -.
DR   KEGG; mmu:78771; -.
DR   UCSC; uc007rgn.1; mouse.
DR   CTD; 78771; -.
DR   MGI; MGI:1926021; Mctp1.
DR   GeneTree; ENSGT00550000074417; -.
DR   HOVERGEN; HBG055341; -.
DR   OrthoDB; EOG4PRSQ2; -.
DR   NextBio; 349460; -.
DR   ArrayExpress; Q8C8C0; -.
DR   Bgee; Q8C8C0; -.
DR   Genevestigator; Q8C8C0; -.
DR   GO; GO:0016021; C:integral to membrane; ISS:HGNC.
DR   GO; GO:0005509; F:calcium ion binding; ISS:HGNC.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   InterPro; IPR013583; PRibTrfase_C.
DR   Pfam; PF00168; C2; 3.
DR   Pfam; PF08372; PRT_C; 1.
DR   PRINTS; PR00360; C2DOMAIN.
DR   SMART; SM00239; C2; 3.
DR   SUPFAM; SSF49562; C2_CaLB; 3.
DR   PROSITE; PS50004; C2; 3.
PE   2: Evidence at transcript level;
KW   Repeat.
SQ   SEQUENCE   694 AA;  80539 MW;  3E5D7A34A7185256 CRC64;
     MYQLDITLRR GQSLAARDRG GTSDPYVKFK IGRKEVFRSK IIHKNLNPVW EEKACVLIDH
     LREPLYIKVF DYDFGLQDDF MGSAFLDLTQ LELNRSTDVT LTLKDPHYPD HDLGIILLSV
     ILTPKEGEHR DVTMLMRKSW KRSSKFQTQS LRLSDQHRKS HLWRGIVSIT LIEGRDLKAM
     DSNGLSDPYV KFRLGHQKYK SKIMPKTLNP QWREQFDFHL YEERGGIMDI TAWDKDAGKR
     DDFIGRCQVD LSSLSREQTH KLELHLEEGE GHLVLLVTLT ASATVCISDL SVNSMEDQKE
     REEILKRYSP LRIFNNLKDV GFLQVKVIRA EGLMAADVTG KSDPFCVVEL NNDRLLTHTV
     YKNLNPEWNK VFTFNIKDIH SVLEVTVYDE DRDRSADFLG RVAIPLLSIQ NGEQKAYVLK
     NKQLTGPTKG VIYLEIDVIF NAVKASLRTL IPKERKYIEE ENRLSKQLLL RNFIRTKRCV
     IVLVNAAYYV NSCFDWDSPP RSLAAFVLFL LIVWNFELYM IPLLLLLLLT WNYFLIISGK
     DNRQRDTVVE DMLEDEEEED DRDDKDGEKK GFINKIYAIQ EVCVSVQNIL DEVASLGERI
     KNTFNWTVPF LSWLAIVALC VFTAILYFIP LTYIVLVWGI NKFTKKLRSP YAIDNNELLD
     FLSRVPSDVQ VVQYQELKPD HSHSPYKRKK NNLG
//
ID   SCAI_MOUSE              Reviewed;         606 AA.
AC   Q8C8N2; A2RTF5; A3KGQ2; Q8C409; Q8C8K2;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Protein SCAI;
DE   AltName: Full=Suppressor of cancer cell invasion protein;
GN   Name=Scai;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Hippocampus, Medulla oblongata, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-64, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [6]
RP   FUNCTION, INTERACTION WITH DIAPH1; MKL1 AND SRF, SUBCELLULAR LOCATION,
RP   AND TISSUE SPECIFICITY.
RX   PubMed=19350017; DOI=10.1038/ncb1862;
RA   Brandt D.T., Baarlink C., Kitzing T.M., Kremmer E., Ivaska J.,
RA   Nollau P., Grosse R.;
RT   "SCAI acts as a suppressor of cancer cell invasion through the
RT   transcriptional control of beta1-integrin.";
RL   Nat. Cell Biol. 11:557-568(2009).
CC   -!- FUNCTION: Tumor suppressor which functions to suppress MKL1-
CC       induced SRF transcriptional activity. May function in the RHOA-
CC       DIAPH1 signal transduction pathway and regulate cell migration
CC       through transcriptional regulation of ITGB1.
CC   -!- SUBUNIT: Interacts with DIAPH1. Forms a nuclear ternary complex
CC       with MKL1 and SRF.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential). Nucleus. Cytoplasm. Note=Nuclear localization is
CC       required for inhibition of MKL1.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8C8N2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C8N2-2; Sequence=VSP_015121, VSP_015122;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in most tissues tested with higher
CC       expression levels in brain, spleen and thymus.
CC   -!- SIMILARITY: Belongs to the SCAI family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC32904.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK044772; BAC32081.1; -; mRNA.
DR   EMBL; AK046875; BAC32904.1; ALT_INIT; mRNA.
DR   EMBL; AK083280; BAC38841.1; -; mRNA.
DR   EMBL; AL844588; CAM46058.2; -; Genomic_DNA.
DR   EMBL; AL845350; CAM46058.2; JOINED; Genomic_DNA.
DR   EMBL; AL928639; CAM46058.2; JOINED; Genomic_DNA.
DR   EMBL; AL928639; CAO77724.2; -; Genomic_DNA.
DR   EMBL; AL844588; CAO77724.2; JOINED; Genomic_DNA.
DR   EMBL; AL845350; CAO77724.2; JOINED; Genomic_DNA.
DR   EMBL; AL845350; CAQ11836.1; -; Genomic_DNA.
DR   EMBL; AL844588; CAQ11836.1; JOINED; Genomic_DNA.
DR   EMBL; AL928639; CAQ11836.1; JOINED; Genomic_DNA.
DR   EMBL; CH466519; EDL26843.1; -; Genomic_DNA.
DR   EMBL; BC132485; AAI32486.1; -; mRNA.
DR   IPI; IPI00313539; -.
DR   IPI; IPI00648639; -.
DR   RefSeq; NP_848893.2; NM_178778.3.
DR   UniGene; Mm.204836; -.
DR   PhosphoSite; Q8C8N2; -.
DR   PRIDE; Q8C8N2; -.
DR   Ensembl; ENSMUST00000038874; ENSMUSP00000037194; ENSMUSG00000035236.
DR   GeneID; 320271; -.
DR   KEGG; mmu:320271; -.
DR   NMPDR; fig|10090.3.peg.5933; -.
DR   UCSC; uc008jof.1; mouse.
DR   UCSC; uc008joh.1; mouse.
DR   CTD; 320271; -.
DR   MGI; MGI:2443716; Scai.
DR   GeneTree; ENSGT00390000009566; -.
DR   HOGENOM; HBG717216; -.
DR   InParanoid; Q8C8N2; -.
DR   OMA; RGARQPQ; -.
DR   OrthoDB; EOG41NTKR; -.
DR   PhylomeDB; Q8C8N2; -.
DR   NextBio; 396403; -.
DR   ArrayExpress; Q8C8N2; -.
DR   Bgee; Q8C8N2; -.
DR   CleanEx; MM_A930041I02RIK; -.
DR   Genevestigator; Q8C8N2; -.
DR   GermOnline; ENSMUSG00000035236; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR   GO; GO:0030336; P:negative regulation of cell migration; IGI:UniProtKB.
DR   GO; GO:0035024; P:negative regulation of Rho protein signal transduction; IDA:UniProtKB.
DR   InterPro; IPR022709; DUF3550.
DR   InterPro; IPR016607; UCP013022.
DR   Pfam; PF12070; DUF3550; 1.
DR   PIRSF; PIRSF013022; UCP013022; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Membrane; Nucleus; Phosphoprotein;
KW   Repressor; Signal transduction inhibitor; Transcription;
KW   Transcription regulation; Transmembrane; Transmembrane helix.
FT   CHAIN         1    606       Protein SCAI.
FT                                /FTId=PRO_0000089736.
FT   TRANSMEM    472    492       Helical; (Potential).
FT   REGION        1    212       Necessary to inhibit MKL1-induced SRF
FT                                transcriptional activity.
FT   REGION       71    173       Required for interaction with MKL1.
FT   MOD_RES      64     64       Phosphotyrosine.
FT   VAR_SEQ     322    325       EPAD -> VIIA (in isoform 2).
FT                                /FTId=VSP_015121.
FT   VAR_SEQ     326    606       Missing (in isoform 2).
FT                                /FTId=VSP_015122.
FT   CONFLICT     58     58       T -> A (in Ref. 1; BAC32081).
SQ   SEQUENCE   606 AA;  70275 MW;  09CBEDC06FDC573F CRC64;
     MVRGARQSQQ PRSRLAPRLS GTVEKPPRKR KSRTEFTLKE TMSSGGAEDD IPQGERKTVT
     DFCYLLDKSK QLFNGLRDLP QYGQKQWQSY FGRTFDVYTK LWKFQQQHRQ VLDNRYGLKR
     WQIGEIASKI GQLYYHYYLR TSETSYLNEA FSFYSAIRQR SYYSQVNKED RPELVVKKLR
     YYARFIVVCL LLNKMDVVKD LVKELSDEIE DYTHRFNTED QVEWNLVLQE VAAFIEADPV
     MVLNDDNTIV ITSNRLAETG APLLEQGMIV GQLSLADALI IGNCNNQVKF SELTVDMFRM
     LQALEREPMN LASQMNKPGI QEPADKPTRR ENPHKYLLYK PTFSQLYTFL AASFKELPAN
     SVLLIYLSAT GVFPTGRSDG EGPYDFGGVL TNSNRDIING DAIHKRNQSH KEMHCLHPGD
     LYPFTRKPLF IVVDSSNSVA YKNFTNLFGQ PLVCLLSPTA YPKALQDQSQ RGSLFTLFLN
     NPLMAFLFVS GLSSMRRGLW EKCQEYLRKI NRDIAQLLTH SRSIDQAFLQ FFGDEFLRLL
     LTRFVFCSAT MRMHKAFRET RNYPESYPQL PRDETVENPH LQKHILELAS ILDVRNIFFE
     NSMDDY
//
ID   ANK2_MOUSE              Reviewed;        3898 AA.
AC   Q8C8R3; Q3TM62; Q3V2X0; Q6PCN2; Q80ZZ7; Q8BNC1; Q8C445; Q8CCV0;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   30-NOV-2010, entry version 60.
DE   RecName: Full=Ankyrin-2;
DE            Short=ANK-2;
DE   AltName: Full=Brain ankyrin;
GN   Name=Ank2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 6; 7 AND 8),
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1674 (ISOFORM 5),
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1190 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3402-3897 (ISOFORM 4).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Hippocampus, Lung, Medulla oblongata, Retina, and
RC   Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 2922-3898 (ISOFORM 4).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=94075409; PubMed=8253844; DOI=10.1083/jcb.123.6.1463;
RA   Chan W., Kordeli E., Bennett V.;
RT   "440-kD ankyrinB: structure of the major developmentally regulated
RT   domain and selective localization in unmyelinated axons.";
RL   J. Cell Biol. 123:1463-1473(1993).
RN   [5]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=15262991; DOI=10.1074/jbc.M406018200;
RA   Mohler P.J., Yoon W., Bennett V.;
RT   "Ankyrin-B targets beta2-spectrin to an intracellular compartment in
RT   neonatal cardiomyocytes.";
RL   J. Biol. Chem. 279:40185-40193(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3717, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-34; SER-3315;
RP   SER-3343 AND SER-3362, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-34; SER-1428;
RP   THR-3050; SER-3226; SER-3362; TYR-3363; SER-3686; SER-3692; SER-3744;
RP   THR-3745; SER-3764 AND THR-3785, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [9]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=17940615; DOI=10.1371/journal.pone.0001051;
RA   Mohler P.J., Healy J.A., Xue H., Puca A.A., Kline C.F.,
RA   Allingham R.R., Kranias E.G., Rockman H.A., Bennett V.;
RT   "Ankyrin-B syndrome: enhanced cardiac function balanced by risk of
RT   cardiac death and premature senescence.";
RL   PLoS ONE 2:E1051-E1051(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-378; TYR-531 AND
RP   TYR-1349, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-34; SER-846 AND
RP   SER-898, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 (ISOFORM 7),
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [12]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=19007774; DOI=10.1016/j.exer.2008.09.022;
RA   Kizhatil K., Sandhu N.K., Peachey N.S., Bennett V.;
RT   "Ankyrin-B is required for coordinated expression of beta-2-spectrin,
RT   the Na/K-ATPase and the Na/Ca exchanger in the inner segment of rod
RT   photoreceptors.";
RL   Exp. Eye Res. 88:57-64(2009).
CC   -!- FUNCTION: Attaches integral membrane proteins to cytoskeletal
CC       elements. Also binds to cytoskeletal proteins. Required for
CC       coordinate assembly of Na/Ca exchanger, Na/K ATPase and InsP3
CC       receptor at sarcoplasmic reticulum sites in cardiomyocytes (By
CC       similarity). Required for the coordinated expression of the Na/K
CC       ATPase, Na/Ca exchanger and beta-2-spectrin (SPTBN1) in the inner
CC       segment of rod photoreceptors. Required for expression and
CC       targeting of SPTBN1 in neonatal cardiomyocytes and for the
CC       regulation of neonatal cardiomyocyte contraction rate.
CC   -!- SUBUNIT: Interacts with RHBG and SPTBN1 (By similarity).
CC       Colocalizes with Na/K ATPase, Na/Ca exchanger and SPTBN1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Membrane. Cytoplasm, myofibril, sarcomere, M-band. Apical cell
CC       membrane. Cell membrane. Note=Expressed at the apical membrane of
CC       airway lung epithelial cells. Localized to the plasma membrane of
CC       the inner segments of photoreceptors in retina. Colocalizes with
CC       SPTBN1 in a distict intracellular compartment of neonatal
CC       cardiomyocytes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC       Name=1;
CC         IsoId=Q8C8R3-1; Sequence=Displayed;
CC         Note=Gene prediction based on similarity to human ortholog;
CC       Name=2;
CC         IsoId=Q8C8R3-2; Sequence=VSP_053011, VSP_053023, VSP_053025;
CC         Note=Incomplete sequence. Acetylated on Ala-2. Phosphorylated on
CC         Ser-3;
CC       Name=3;
CC         IsoId=Q8C8R3-3; Sequence=VSP_053010, VSP_053027, VSP_053029;
CC         Note=Ref.1 (BAC27676) sequence is in conflict in position:
CC         1014:V->A;
CC       Name=4;
CC         IsoId=Q8C8R3-4; Sequence=VSP_053029;
CC       Name=5;
CC         IsoId=Q8C8R3-5; Sequence=VSP_053013, VSP_053021;
CC         Note=No experimental confirmation available;
CC       Name=6;
CC         IsoId=Q8C8R3-6; Sequence=VSP_053012, VSP_053016, VSP_053019,
CC                                  VSP_053020;
CC         Note=No experimental confirmation available;
CC       Name=7;
CC         IsoId=Q8C8R3-7; Sequence=VSP_053014, VSP_053017, VSP_053018;
CC         Note=Acetylated on Ala-2. Phosphorylated on Ser-7;
CC       Name=8;
CC         IsoId=Q8C8R3-8; Sequence=VSP_053015, VSP_053017, VSP_053018;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Present in skeletal muscle, kidney, lung,
CC       testes, spleen and lung. In the pancreas, highly expressed in
CC       islets and concentrated in beta cells. Expressed in Purkinje
CC       neurons in cerebellum. Expression in the central nerve tracts in
CC       forebrain and cerebellum is elevated in the myelinate-deficient
CC       strain Shiverer. Expressed in the inner segments of rod
CC       photoreceptors in retina.
CC   -!- DEVELOPMENTAL STAGE: Expressed in neonatal developing ventricular
CC       cardiomyocytes as well as adult cardiomyocytes.
CC   -!- PTM: Phosphorylated at multiple sites by different protein kinases
CC       and each phosphorylation event regulates the protein's structure
CC       and function (Potential).
CC   -!- SIMILARITY: Contains 24 ANK repeats.
CC   -!- SIMILARITY: Contains 1 death domain.
CC   -!- SIMILARITY: Contains 1 ZU5 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AK036018; Type=Frameshift; Positions=1002;
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DR   EMBL; AK032060; BAC27676.1; -; mRNA.
DR   EMBL; AK036018; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK044634; BAC32012.1; -; mRNA.
DR   EMBL; AK083111; BAC38764.1; -; mRNA.
DR   EMBL; AK083826; BAE43385.1; -; mRNA.
DR   EMBL; AK084070; BAC39111.1; -; mRNA.
DR   EMBL; AK166115; BAE38580.1; -; mRNA.
DR   EMBL; AC102480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC102591; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC131744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC043123; AAH43123.1; -; mRNA.
DR   EMBL; BC059251; AAH59251.1; -; mRNA.
DR   IPI; IPI00225231; -.
DR   IPI; IPI00227235; -.
DR   IPI; IPI00228697; -.
DR   IPI; IPI00404055; -.
DR   IPI; IPI00652331; -.
DR   IPI; IPI00921617; -.
DR   IPI; IPI00921642; -.
DR   IPI; IPI00921659; -.
DR   RefSeq; NP_001029340.1; NM_001034168.1.
DR   RefSeq; NP_848770.2; NM_178655.3.
DR   UniGene; Mm.220242; -.
DR   UniGene; Mm.461850; -.
DR   HSSP; P16157; 1N11.
DR   ProteinModelPortal; Q8C8R3; -.
DR   SMR; Q8C8R3; 32-841, 966-1123.
DR   STRING; Q8C8R3; -.
DR   PhosphoSite; Q8C8R3; -.
DR   GeneID; 109676; -.
DR   KEGG; mmu:109676; -.
DR   UCSC; uc008rgx.1; mouse.
DR   CTD; 109676; -.
DR   MGI; MGI:88025; Ank2.
DR   eggNOG; roNOG05180; -.
DR   HOVERGEN; HBG100442; -.
DR   InParanoid; Q8C8R3; -.
DR   OMA; RDRMERK; -.
DR   Genevestigator; Q8C8R3; -.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral to plasma membrane; IDA:UniProtKB.
DR   GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0060048; P:cardiac muscle contraction; IMP:MGI.
DR   GO; GO:0034394; P:protein localization at cell surface; IMP:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR000488; Death.
DR   InterPro; IPR011029; DEATH-like.
DR   InterPro; IPR000906; ZU5.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 3.
DR   Gene3D; G3DSA:1.10.533.10; DEATH_like; 1.
DR   Pfam; PF00023; Ank; 19.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF00791; ZU5; 1.
DR   SMART; SM00248; ANK; 23.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00218; ZU5; 1.
DR   SUPFAM; SSF48403; ANK; 2.
DR   SUPFAM; SSF47986; DEATH_like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 20.
DR   PROSITE; PS50017; DEATH_DOMAIN; 1.
DR   PROSITE; PS51145; ZU5; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ANK repeat; Cell membrane;
KW   Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein; Repeat.
FT   CHAIN         1   3898       Ankyrin-2.
FT                                /FTId=PRO_0000364087.
FT   REPEAT       30     62       ANK 1.
FT   REPEAT       63     92       ANK 2.
FT   REPEAT       96    125       ANK 3.
FT   REPEAT      129    158       ANK 4.
FT   REPEAT      162    191       ANK 5.
FT   REPEAT      193    220       ANK 6.
FT   REPEAT      232    261       ANK 7.
FT   REPEAT      265    294       ANK 8.
FT   REPEAT      298    327       ANK 9.
FT   REPEAT      331    360       ANK 10.
FT   REPEAT      364    393       ANK 11.
FT   REPEAT      397    426       ANK 12.
FT   REPEAT      430    459       ANK 13.
FT   REPEAT      463    492       ANK 14.
FT   REPEAT      496    525       ANK 15.
FT   REPEAT      529    558       ANK 16.
FT   REPEAT      562    591       ANK 17.
FT   REPEAT      595    624       ANK 18.
FT   REPEAT      628    657       ANK 19.
FT   REPEAT      661    690       ANK 20.
FT   REPEAT      694    723       ANK 21.
FT   REPEAT      727    756       ANK 22.
FT   REPEAT      760    789       ANK 23.
FT   REPEAT      793    822       ANK 24.
FT   DOMAIN      966   1073       ZU5.
FT   DOMAIN     3522   3606       Death.
FT   REGION      966   1125       Interaction with SPTBN1 (By similarity).
FT   COMPBIAS   1777   1855       Ser-rich.
FT   COMPBIAS   2620   2626       Poly-Ser.
FT   MOD_RES      31     31       Phosphoserine.
FT   MOD_RES      34     34       Phosphoserine.
FT   MOD_RES     378    378       Phosphotyrosine.
FT   MOD_RES     531    531       Phosphotyrosine.
FT   MOD_RES     846    846       Phosphoserine.
FT   MOD_RES     898    898       Phosphoserine.
FT   MOD_RES     911    911       Phosphoserine (By similarity).
FT   MOD_RES    1349   1349       Phosphotyrosine.
FT   MOD_RES    1428   1428       Phosphoserine.
FT   MOD_RES    1475   1475       Phosphoserine (By similarity).
FT   MOD_RES    1490   1490       Phosphothreonine (By similarity).
FT   MOD_RES    2542   2542       Phosphothreonine (By similarity).
FT   MOD_RES    3050   3050       Phosphothreonine.
FT   MOD_RES    3226   3226       Phosphoserine.
FT   MOD_RES    3315   3315       Phosphoserine.
FT   MOD_RES    3343   3343       Phosphoserine.
FT   MOD_RES    3362   3362       Phosphoserine.
FT   MOD_RES    3363   3363       Phosphotyrosine.
FT   MOD_RES    3686   3686       Phosphoserine.
FT   MOD_RES    3692   3692       Phosphoserine.
FT   MOD_RES    3718   3718       Phosphothreonine.
FT   MOD_RES    3735   3735       Phosphoserine (By similarity).
FT   MOD_RES    3739   3739       Phosphothreonine (By similarity).
FT   MOD_RES    3744   3744       Phosphoserine.
FT   MOD_RES    3745   3745       Phosphothreonine.
FT   MOD_RES    3764   3764       Phosphoserine.
FT   MOD_RES    3785   3785       Phosphothreonine.
FT   VAR_SEQ       1    838       Missing (in isoform 3).
FT                                /FTId=VSP_053010.
FT   VAR_SEQ       1     28       MMNEDAAQKSDSGEKFNGSSQRRKRPKK -> MASPTSPGP
FT                                EGGACTPQNPPRIRQ (in isoform 2).
FT                                /FTId=VSP_053011.
FT   VAR_SEQ       1     28       MMNEDAAQKSDSGEKFNGSSQRRKRPKK -> MTTMLQKSQ
FT                                NKCESQTTCNEVTQSSCIQRKDPNGVHPDDQ (in
FT                                isoform 6).
FT                                /FTId=VSP_053012.
FT   VAR_SEQ       1     27       MMNEDAAQKSDSGEKFNGSSQRRKRPK -> MTTMLQ (in
FT                                isoform 5).
FT                                /FTId=VSP_053013.
FT   VAR_SEQ       1     27       MMNEDAAQKSDSGEKFNGSSQRRKRPK -> MAHAAASIKK
FT                                VREAELDEKEKNLDRERKKQRKIPRDRMERKR (in
FT                                isoform 7).
FT                                /FTId=VSP_053014.
FT   VAR_SEQ       1     27       MMNEDAAQKSDSGEKFNGSSQRRKRPK -> MATMLQ (in
FT                                isoform 8).
FT                                /FTId=VSP_053015.
FT   VAR_SEQ     224    231       Missing (in isoform 6).
FT                                /FTId=VSP_053016.
FT   VAR_SEQ     397    439       NGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHV
FT                                AA -> VNLAQSTFTQCSKTTLLGQRHLHQCKSMDLWLITA
FT                                KLFPPLNH (in isoform 7 and isoform 8).
FT                                /FTId=VSP_053017.
FT   VAR_SEQ     440   3898       Missing (in isoform 7 and isoform 8).
FT                                /FTId=VSP_053018.
FT   VAR_SEQ     463    477       RGETALHMAARAGQV -> MQPKWESMSLSAEPV (in
FT                                isoform 6).
FT                                /FTId=VSP_053019.
FT   VAR_SEQ     478   3898       Missing (in isoform 6).
FT                                /FTId=VSP_053020.
FT   VAR_SEQ     597    629       Missing (in isoform 5).
FT                                /FTId=VSP_053021.
FT   VAR_SEQ     899    902       LRSF -> TIP (in isoform 2).
FT                                /FTId=VSP_053023.
FT   VAR_SEQ    1042   1042       G -> GKLHLPTAPPPLNEGESLVSRILQLGPPGTKFLG
FT                                (in isoform 2).
FT                                /FTId=VSP_053025.
FT   VAR_SEQ    1444   3514       Missing (in isoform 3).
FT                                /FTId=VSP_053027.
FT   VAR_SEQ    3894   3894       E -> EVTLSEPSVLSSTSQFQAEPVEGRRVSKVVKTTMVH
FT                                GERMEKSLGDSSLATDLPSAKDDFEE (in isoform 3
FT                                and isoform 4).
FT                                /FTId=VSP_053029.
FT   CONFLICT   1026   1026       L -> Q (in Ref. 1; BAC27676).
FT   CONFLICT   1112   1112       R -> H (in Ref. 1; BAC27676).
FT   CONFLICT   3649   3649       E -> K (in Ref. 1; BAC27676).
FT   CONFLICT   3731   3731       A -> T (in Ref. 3; AAH43123).
SQ   SEQUENCE   3898 AA;  426261 MW;  A779A20AA489DB34 CRC64;
     MMNEDAAQKS DSGEKFNGSS QRRKRPKKSD SNASFLRAAR AGNLDKVVEY LKGGIDINTC
     NQNGLNALHL AAKEGHVGLV QELLGRGSSV DSATKKGNTA LHIASLAGQA EVVKVLVKEG
     ANINAQSQNG FTPLYMAAQE NHIDVVKYLL ENGANQSTAT EDGFTPLAVA LQQGHNQAVA
     ILLENDTKGK VRLPALHIAA RKDDTKSAAL LLQNDHNADV QSKMMVNRTT ESGFTPLHIA
     AHYGNVNVAT LLLNRGAAVD FTARNGITPL HVASKRGNTN MVKLLLDRGG QIDAKTRDGL
     TPLHCAARSG HDQVVELLLE RKAPLLARTK NGLSPLHMAA QGDHVECVKH LLQYKAPVDD
     VTLDYLTALH VAAHCGHYRV TKLLLDKRAN PNARALNGFT PLHIACKKNR IKVMELLVKY
     GASIQAITES GLTPIHVAAF MGHLNIVLLL LQNGASPDVT NIRGETALHM AARAGQVEVV
     RCLLRNGALV DARAREEQTP LHIASRLGKT EIVQLLLQHM AHPDAATTNG YTPLHISARE
     GQVDVASVLL EAGAAHSLAT KKGFTPLHVA AKYGSLDVAK LLLQRRAAAD SAGKNGLTPL
     HVAAHYDNQK VALLLLEKGA SPHATAKNGY TPLHIAAKKN QMQIASTLLN YGAETNTVTK
     QGVTPLHLAS QEGHTDMVTL LLDKGANIHM STKSGLTSLH LAAQEDKVNV ADILTKHGAD
     RDAYTKLGYT PLIVACHYGN VKMVNFLLKQ GANVNAKTKN GYTPLHQAAQ QGHTHIINVL
     LQHGAKPNAT TANGNTALAI AKRLGYISVV DTLKVVTEEV TTTTTTITEK HKLNVPETMT
     EVLDVSDEEG DDTVTGDGGE YLRPEDLKEL GDDSLPSSQF LDGMNYLRYS LEGGRSDSLR
     SFSSDRSHTL SHASYLRDSA MIDDTVVIPS HQVSALAKEA ERNSYRLSWG TENLDNVALS
     SSPIHSGFLV SFMVDARGGA MRGCRHNGLR IIIPPRKCTA PTRVTCRLVK RHRLATMPPM
     VEGEGLASRL IEVGPSGAQF LGPVIVEIPH FAALRGKERE LVVLRSENGD SWKEHFCDYT
     EDELNEILNG MDEVLDSPED LEKKRICRII TRDFPQYFAV VSRIKQDSNL IGPEGGVLSS
     TVVSQVQAVF PEGALTKRIR VGLQAQPMHS ELVKKILGNK ATFSPIVTLE PRRRKFHKPI
     TMTIPVPKAS SDVMLNGFGG DAPTLRLLCS ITGGTTPAQW EDITGTTPLT FVNECVSFTT
     NVSARFWLID CRQIQESVAF ASQVYREIIC VPYMAKFVVF AKSHDPIEAR LRCFCMTDDK
     VDKTLEQQEN FSEVARSRDV EVLEGKPIYV DCFGNLVPLT KSGQHHIFSF FAFKENRLPL
     FVKVRDTTQE PCGRLSFMKE PKSTRGLVHQ AICNLNITLP IYAKESESDQ EPEEEIGMTS
     EKNDETESTE TSVLKSHLVN EVPVLASPDL LSEVSEMKQD LIKMTAILTT DVSDKAGSLK
     VKELAKAGEE EPGEPFEIVE RVKEDLEKVN AILRSGTCMR DEGRARSSQS ERELEEEWVI
     VSDEEIQEAK QHAPVEIDEH PCIEVRVDRE TKAKVEKDST GLVNYLTDDL NSYTSPHEKK
     PHTAPEKSGE TSQASAVGKS SESNKGKATS AEEKQSAQKQ LKPGLAIKKP VRRKLKEKQK
     QKEESSQSSE EKTELKKGSS EESVDEDRGL VPEPLPTAKA TSPLIEETPI GSIKDKVKAL
     QKRVEDEQKG RSKLPVRVKG KEDVPKRTTP RTHPAVSPSS KSSTSSKAER HSSLSSSAKP
     ERHTPVSPSS KNEKLSPVSP SAKTERHSPV FSGKPEKHSP GSPSTKNERH SPVSSLKTER
     HTPGSPSGKT DKRPPVPSSG RTEKHPPVSP GKTEKHLPGS PSIRTPEKPA PGSATGKHEK
     HLPVSPGKTE KQPPISPTSK TERIEETMSV RELMKAFQSG QDPSKHKTGL FEHKSAKQKQ
     PQDKSKSRVE KEKGHTVTQR EVTQRETQRI ESQTAKRGQR FQVSAATESR RFRSTTITVG
     LRMEDPVRER FERTPIIKTP EVVPSVAAEE SHRGSEKIVD EQGDMDFQIS PDRKTSTDFS
     EVIKQELEDN DKYQQFRLTE DTEKAQVHLD QVITSPFNTA FPLDYMKDEF LPALSLQSGA
     LGGSSESLKQ EVIAGSPCSS LMEGTPQISS EESYKHEGLA ETPETSPESL SFSPKKSEEQ
     IGEAKETTKV GTPTDIHSEK ELPITNDITD SSQKQGAGVT RGSEPSTEHS QKEVTQDPHK
     DVCSKQDGCP ESQSVSLASE VFTEKGSCGE SQLPLVSSAF KTQSESETQE SLTPSEVTKP
     FPPSDASVKT AEGTEPKPQG AIRSPQGLEL PLPNRDSEVL SPMADESLAV SHKDSLEASP
     VLEDNSSHKT PDSLEPSPLK ESPCRDSLES SPVEPKMKAG ILPSHFPLPA AIAKTDLVAE
     VASMRSRLLR DPDGSAEDDS LEQTSLMESS GKSPLSPDTP SSEEVSYEVT PKPSDSSTPK
     PAVIHECAEE DDSENGEKKR FTPEEEMFKM VTKIKTFDEL EQEAKQKRDY KKEPRQDGSS
     SASDPDADYS AEVNDEKQMA GTEGEGEVPV LVTSENRKVS SSSSESEPEL TQLSKGADSG
     LLTEPVIRVQ PPSPLPSSID SNSSPEEATQ FQPIVPKQYT FKMNEEIQEE PATSEDKDCK
     SHLAEDSQTH SADAADGSDG DLNRETTQPE TCDGHGCETV SPSNSATPVS LGVQSPEHKD
     VDKPLAIDKD SLAHQDTCEN DREEREFDPS GVESTQADLP NESSSLSSRC AIPEGNESAK
     EIASPSSPVK VEVTITDQAL ESMPEDCPIQ DSSTTMQTER FAMDVPVSEL AETDENSDPQ
     IISPYENVPS SSFFSAEPSK IQTDTCHSTV VHSPEVYSVI IRSSPEDVVV TNSSNRTVSG
     EESHCESHDL ETESEQKSAL WAAQSDAPPL AVAPTASDAA SVTGEQASKV IITKTDADAD
     SWSEIREDDA AFEARVKEEE QKIFGLMVDR QSQGTTPDTT PARTPTEEGT PTSEQNPFLF
     QEGKLFEMTR SGAIDMTKRP YADESLHFFQ IGQESNEEAI SEDLKEGATG AEPPQTETTS
     ESLELSEPKE AMDDEGELLP DDVSEEIEDL PASDANIDSQ VIISASTETP TKEAVSTAVE
     EPPTTQRSDS LSTVKQTPRP AVPGPVGQLD FSPVTRSVYS GQDDESPESS PEEQKSVIEI
     PTAPVDNVPS AESKPQIPIR TLPTLVPAPP SAEDESAFSD DFPSSLDEDS KEGGAKPKSK
     IPVKAPTQRT EWQPSPTDIP LQKTAVPQGQ ETLSRAPDGR SKSESDASSL DAKTKCPVKA
     RSYIETETES RERAEGFESE SEDGATKPKL FASRLPVKSR STSSSGRPGT SPTRESREHF
     FDLYRNSIEF FEEISDEASK LVDRLTQSER EQEPPSDDES SSALEVSVIE SLPPVDIEHS
     APEDIFDTRP IWDESIETMI ERIPDENGHD RAEDPQDEQE RMEERLAYIA DHLGFSWTEL
     ARELDFTEEQ IHQIRIENPN SLQDQSHALL KYWLERDGKH ATDTILIECL TKINRMDIVH
     LLETNTEPLQ ERMGRSYAEI EQTITLDHSE GFSVLPDELC AAKEKKEQEA SKESESSDHP
     PMVSEEDISV GYSTFQDCLP KTEGDSPAAA LSPQMHQEPV QQDFSGKTQD QQEYYVTTPG
     AEVEDPQKAT AVPDSLCKTP EDISTPPEGT KPCLQTPVTS ERGSPIVQEP EEASEPKEES
     SPRKTSLVIV ESTDDQSQVF ERLDGDAAFQ KGDDMPDIPP ETVTEEEYVD ENGHTVVKKV
     TRKIIRRYVS SDGTEKEEVT MQGMPQEPVN IEDGDNYSKV IKRVVLKSDT QQSEDNNE
//
ID   Q8C8S5_MOUSE            Unreviewed;       676 AA.
AC   Q8C8S5;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Plec; Synonyms=Plec1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK044559; BAC31980.1; -; mRNA.
DR   IPI; IPI00230061; -.
DR   UniGene; Mm.234912; -.
DR   HSSP; Q15149; 1MB8.
DR   ProteinModelPortal; Q8C8S5; -.
DR   STRING; Q8C8S5; -.
DR   PRIDE; Q8C8S5; -.
DR   Ensembl; ENSMUST00000089610; ENSMUSP00000087037; ENSMUSG00000022565.
DR   UCSC; uc007wje.1; mouse.
DR   MGI; MGI:1277961; Plec.
DR   ArrayExpress; Q8C8S5; -.
DR   Bgee; Q8C8S5; -.
DR   Genevestigator; Q8C8S5; -.
DR   GO; GO:0043292; C:contractile fiber; IDA:MGI.
DR   GO; GO:0005626; C:insoluble fraction; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 2.
DR   Pfam; PF00307; CH; 2.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00150; SPEC; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
PE   2: Evidence at transcript level;
KW   Actin-binding; Repeat.
FT   NON_TER     676    676
SQ   SEQUENCE   676 AA;  77580 MW;  6DA7D8815CAE6C70 CRC64;
     MSGEDSEVRP VAVAEGSSNG SSGSPSPGDT LPWNLGKTQR SRRSGGGSVG NGSVLDPAER
     AVIRIADERD RVQKKTFTKW VNKHLIKHWR AEAQRHISDL YEDLRDGHNL ISLLEVLSGD
     SLPRERDVIR SVRLPREKGR MRFHKLQNVQ IALDYLRHRQ VKLVNIRNDD IADGNPKLTL
     GLIWTIILHF QISDIQVSGQ SEDMTAKEKL LLWSQRMVEG YQGLRCDNFT TSWRDGRLFN
     AIIHRHKPML IDMNKVYRQT NLENLDQAFS VAERDLGVTR LLDPEDVDVP QPDEKSIITY
     VSSLYDAMPR VPGAQDGVRA NELQLRWQEY RELVLLLLQW IRHHTAAFEE RKFPSSFEEI
     EILWCQFLKF KETELPAKEA DKNQSKVIYQ SLEGAVQAGQ LKIPPGYHPL DVEKEWGKLH
     VAILEREKQL RSEFERLECL QRIVSKLQME AGLCEEQLNQ ADALLQSDIR LLASGKVAQR
     AGEVERDLDK ADGMIRLLFN DVQTLKDGRH PQGEQMYRRV YRLHERLVAI RTEYNLRLKA
     GVGAPVTQVT LQSTQRRPEL EDSTLRYLQD LLAWVEENQR RIDSAEWGVD LPSVEAQLGS
     HRGMHQSIEE FRAKIERARN DESQLSPATR GAYRDCLGRL DLQYAKLLNS SKARLRSLES
     LHGFVAAATK ELMWLN
//
ID   ELFN1_MOUSE             Reviewed;         828 AA.
AC   Q8C8T7;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Extracellular leucine-rich repeat and fibronectin type-III domain-containing protein 1;
DE   Flags: Precursor;
GN   Name=Elfn1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC   -!- SIMILARITY: Contains 5 LRR (leucine-rich) repeats.
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DR   EMBL; AK044511; BAC31957.1; -; mRNA.
DR   EMBL; BC059029; AAH59029.1; -; mRNA.
DR   IPI; IPI00227288; -.
DR   RefSeq; NP_780731.1; NM_175522.3.
DR   UniGene; Mm.237102; -.
DR   HSSP; P24014; 1W8A.
DR   ProteinModelPortal; Q8C8T7; -.
DR   SMR; Q8C8T7; 41-241.
DR   PhosphoSite; Q8C8T7; -.
DR   PRIDE; Q8C8T7; -.
DR   Ensembl; ENSMUST00000050519; ENSMUSP00000053869; ENSMUSG00000048988.
DR   Ensembl; ENSMUST00000110830; ENSMUSP00000106454; ENSMUSG00000048988.
DR   GeneID; 243312; -.
DR   KEGG; mmu:243312; -.
DR   UCSC; uc009ahi.1; mouse.
DR   CTD; 243312; -.
DR   MGI; MGI:2442479; Elfn1.
DR   GeneTree; ENSGT00550000074348; -.
DR   HOGENOM; HBG446203; -.
DR   HOVERGEN; HBG056941; -.
DR   InParanoid; Q8C8T7; -.
DR   OMA; PSTATHY; -.
DR   OrthoDB; EOG4SXNC1; -.
DR   PhylomeDB; Q8C8T7; -.
DR   NextBio; 385717; -.
DR   ArrayExpress; Q8C8T7; -.
DR   Bgee; Q8C8T7; -.
DR   Genevestigator; Q8C8T7; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   SMART; SM00082; LRRCT; 1.
DR   PROSITE; PS50853; FN3; FALSE_NEG.
DR   PROSITE; PS51450; LRR; 5.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Leucine-rich repeat; Membrane; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     25       Potential.
FT   CHAIN        26    828       Extracellular leucine-rich repeat and
FT                                fibronectin type-III domain-containing
FT                                protein 1.
FT                                /FTId=PRO_0000343739.
FT   TOPO_DOM     26    418       Extracellular (Potential).
FT   TRANSMEM    419    439       Helical; (Potential).
FT   TOPO_DOM    440    828       Cytoplasmic (Potential).
FT   REPEAT       59     82       LRR 1.
FT   REPEAT       83    106       LRR 2.
FT   REPEAT      107    130       LRR 3.
FT   REPEAT      132    154       LRR 4.
FT   REPEAT      155    178       LRR 5.
FT   DOMAIN      312    399       Fibronectin type-III.
FT   COMPBIAS    263    288       Pro-rich.
FT   COMPBIAS    709    724       Pro-rich.
FT   CARBOHYD     85     85       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     90     90       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    122    122       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    210    210       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    376    376       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   828 AA;  90815 MW;  D07E6734C156E03D CRC64;
     MAGHGWGTAW VLVAAATLLH AGGLAQGDCW LIEGDKGFVW LAICSQNQPP YEAIPQQINN
     TIVDLRLNEN RIRSVQYASL SRFGNLTYLN LTKNEIGYIE DGAFSGQFNL QVLQLGYNRL
     RNLTEGMLRG LSKLEYLYLQ ANLIEVVMAS AFWECPNIVN IDLSMNRIQQ LGSGTFAGLT
     KLSVCEIYSN PFYCSCELLG FLRWLAAFTN ATQTHDRVQC ESPPVYAGYF LLGQGRHGHQ
     RSILSKLQSV CTEGSYTAEV LGPPRPVPGR SQPGHSPPPP PPEPSDMPCA DDECFSGDGT
     TPLVILTTLV PQTEARPSMK VKQLTQNSAT IMVQLPSPFN RMYTLEQYNN SKSFTVSKLT
     QPQEEIRLTN LYTLTNYTYC VVSTSSGTHH NHTCLTICLP KPPSPPGPVP SPSTATHYIM
     TILGCLFGMV LVLGAVYYCL RKRRRQEEKH KKAVAAAAGS LKKTIIELKY GPEIEAPGLA
     PLTQGPLLGP EAVTRIPYLP AATSDVEQYK LVESSETPKA TKGNYIEVRT GEPQERRGCE
     LSRPGEPQSS VAEISTIAKE VDRVNQIINN CIDALKSEST SFQGAKSGAV SAAEPQLVLL
     SEPLASKHSF LSPVYKDAFG HGGLQRHHSV EAAPGPPRAS TSSSGSARSP RTFRAEATGT
     HKAPATETKY IEKSSPVPET ILTVTPAATV LRAEADKSRQ YGEHRHSYPG SHPAEPPAPP
     PPPPTHEGLG GRKASILEPL TRPRPRDLVY SQLSPQYHNL SYSSSPEYTC RASPSIWERL
     RLSRRRHKDD AEFMAAGHAL RKKVQFAKDE DLHDILDYWK GVSAQHKS
//
ID   Q8C8Y6_MOUSE            Unreviewed;       309 AA.
AC   Q8C8Y6;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Kcnj6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
CC       family.
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DR   EMBL; AK044218; BAC31823.1; -; mRNA.
DR   IPI; IPI00606708; -.
DR   RefSeq; NP_034736.2; NM_010606.2.
DR   UniGene; Mm.328720; -.
DR   HSSP; P35562; 1N9P.
DR   ProteinModelPortal; Q8C8Y6; -.
DR   SMR; Q8C8Y6; 38-304.
DR   STRING; Q8C8Y6; -.
DR   Ensembl; ENSMUST00000056268; ENSMUSP00000052888; ENSMUSG00000043301.
DR   Ensembl; ENSMUST00000095873; ENSMUSP00000093558; ENSMUSG00000043301.
DR   Ensembl; ENSMUST00000099508; ENSMUSP00000097108; ENSMUSG00000043301.
DR   GeneID; 16522; -.
DR   KEGG; mmu:16522; -.
DR   UCSC; uc008abn.1; mouse.
DR   CTD; 16522; -.
DR   MGI; MGI:104781; Kcnj6.
DR   GeneTree; ENSGT00590000082771; -.
DR   HOGENOM; HBG716702; -.
DR   HOVERGEN; HBG006178; -.
DR   InParanoid; Q8C8Y6; -.
DR   NextBio; 289901; -.
DR   ArrayExpress; Q8C8Y6; -.
DR   Bgee; Q8C8Y6; -.
DR   Genevestigator; Q8C8Y6; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015467; F:G-protein activated inward rectifier potassium channel activity; IDA:MGI.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR016449; K_chnl_inward-rec_Kir.
DR   InterPro; IPR001838; K_chnl_inward-rec_Kir-like.
DR   InterPro; IPR003275; K_chnl_inward-rec_Kir3.2.
DR   InterPro; IPR013521; K_chnl_inward-rec_Kir_Cr2.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   Gene3D; G3DSA:2.60.40.1400; IR_K+channel_cytopl; 1.
DR   PANTHER; PTHR11767; K+channel_IR; 1.
DR   PANTHER; PTHR11767:SF19; KIR32_channel; 1.
DR   Pfam; PF01007; IRK; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01328; KIR32CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; Ig_E-set; 1.
PE   2: Evidence at transcript level;
KW   Ion transport; Ionic channel; Membrane; Potassium;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
SQ   SEQUENCE   309 AA;  35483 MW;  2F4FBCC3DBFD3A3C CRC64;
     MDQDVESPVA IHQPKLPKQA RDDLPRHISR DRTKRKIQRY VRKDGKCNVH HGNVRETYRY
     LTDIFTTLVD LKWRFNLLIF VMVYTVTWLF FGMIWWLIAY IRGDMDHIED PSWTPCVTNL
     NGFVSAFLFS IETETTIGYG YRVITDKCPE GIILLLIQSV LGSIVNAFMV GCMFVKISQP
     KKRAETLVFS THAVISMRDG KLCLMFRVGD LRNSHIVEAS IRAKLIKSKQ TSEGEFIPLN
     QTDINVGYYT GDDRLFLVSP LIISHEINQQ SPFWEISKAQ LPKEELEIVV ILEGMVEATG
     KMGFALGFL
//
ID   TM163_MOUSE             Reviewed;         288 AA.
AC   Q8C996; Q8C8I2; Q9D0E0;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Transmembrane protein 163;
GN   Name=Tmem163;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK011522; BAB27676.1; -; mRNA.
DR   EMBL; AK042650; BAC31320.1; -; mRNA.
DR   EMBL; AK047006; BAC32940.1; -; mRNA.
DR   EMBL; BC046234; AAH46234.1; -; mRNA.
DR   EMBL; BC059048; AAH59048.1; -; mRNA.
DR   IPI; IPI00459759; -.
DR   RefSeq; NP_082411.1; NM_028135.2.
DR   UniGene; Mm.281287; -.
DR   ProteinModelPortal; Q8C996; -.
DR   STRING; Q8C996; -.
DR   PhosphoSite; Q8C996; -.
DR   PRIDE; Q8C996; -.
DR   Ensembl; ENSMUST00000027585; ENSMUSP00000027585; ENSMUSG00000026347.
DR   GeneID; 72160; -.
DR   KEGG; mmu:72160; -.
DR   UCSC; uc007cku.1; mouse.
DR   CTD; 72160; -.
DR   MGI; MGI:1919410; Tmem163.
DR   eggNOG; roNOG07032; -.
DR   GeneTree; ENSGT00390000001170; -.
DR   HOGENOM; HBG447087; -.
DR   HOVERGEN; HBG094063; -.
DR   InParanoid; Q8C996; -.
DR   OMA; SVWYLDG; -.
DR   OrthoDB; EOG4VX261; -.
DR   PhylomeDB; Q8C996; -.
DR   NextBio; 335593; -.
DR   ArrayExpress; Q8C996; -.
DR   Bgee; Q8C996; -.
DR   CleanEx; MM_TMEM163; -.
DR   Genevestigator; Q8C996; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    288       Transmembrane protein 163.
FT                                /FTId=PRO_0000278540.
FT   TRANSMEM     88    108       Helical; (Potential).
FT   TRANSMEM    116    136       Helical; (Potential).
FT   TRANSMEM    150    170       Helical; (Potential).
FT   TRANSMEM    187    207       Helical; (Potential).
FT   TRANSMEM    217    237       Helical; (Potential).
FT   TRANSMEM    255    275       Helical; (Potential).
FT   COMPBIAS     12     38       Pro-rich.
FT   MOD_RES      60     60       Phosphoserine.
FT   CONFLICT     21     21       P -> S (in Ref. 1; BAC32940).
FT   CONFLICT    288    288       E -> K (in Ref. 1; BAB27676).
SQ   SEQUENCE   288 AA;  31193 MW;  39552DEE746C4221 CRC64;
     MEPALGSERR SPPGPGVPRP PPRGHAPSTA APAPSPAPMS SSVQSDEERQ PRISESGQFS
     DGLEDRGLLE SSTRLKPHEA QNYRKKALWV SWLSIIVTLA LAVAAFTVSV MRYSASAFGF
     AFDAILDVLS SAIVLWRYSN AAAVHSANRE YIACVILGVI FLLSSICIVV KAIHDLSTRL
     LPEVDDFLFS VSILSGILCS VLAVLKFMLG KVLTSRALIT DGFNSLVGGV MGFSILLSAE
     VFKHNAAVWY LDGSIGVLIG LTIFAYGVKL LIDMVPRVRQ TRHYEMFE
//
ID   DIDO1_MOUSE             Reviewed;        2256 AA.
AC   Q8C9B9; A2AJ47; A2AJ48; B2RS46; Q05C59; Q3ZTP5; Q3ZTP6; Q4V9W1;
AC   Q6ZQD7; Q80V34; Q8BMD0; Q8BRG2; Q8CHR5; Q9WV00;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 4.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Death-inducer obliterator 1;
DE            Short=DIO-1;
DE   AltName: Full=Death-associated transcription factor 1;
DE            Short=DATF-1;
GN   Name=Dido1; Synonyms=Datf1, Dio1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND CHARACTERIZATION.
RC   TISSUE=Pre-B cell;
RX   MEDLINE=99324176; PubMed=10393935; DOI=10.1073/pnas.96.14.7992;
RA   Garcia-Domingo D., Leonardo E., Grandien A., Martinez P., Albar J.P.,
RA   Izpisua-Belmonte J.-C., Martinez-A C.;
RT   "DIO-1 is a novel gene involved in onset of apoptosis in vitro, whose
RT   misexpression disrupts limb development.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:7992-7997(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RX   PubMed=16127461; DOI=10.1172/JCI24177;
RA   Futterer A., Campanero M.R., Leonardo E., Criado L.M., Flores J.M.,
RA   Hernandez J.M., San Miguel J.F., Martinez-A C.;
RT   "Dido gene expression alterations are implicated in the induction of
RT   hematological myeloid neoplasms.";
RL   J. Clin. Invest. 115:2351-2362(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1484-2256 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Thymus, and Wolffian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J, and FVB/N;
RC   TISSUE=Brain, Mammary gland, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 540-548 AND 699-705, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-802, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; THR-148; SER-802 AND
RP   SER-1256, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [10]
RP   STRUCTURE BY NMR OF 257-319.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of PHD domain in death inducer-obliterator 1(DIO-
RT   1).";
RL   Submitted (NOV-2004) to the PDB data bank.
CC   -!- FUNCTION: Putative transcription factor, weakly pro-apoptotic when
CC       overexpressed.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocates to the
CC       nucleus after pro-apoptotic stimuli.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Dido3;
CC         IsoId=Q8C9B9-1; Sequence=Displayed;
CC       Name=2; Synonyms=Dido1;
CC         IsoId=Q8C9B9-2; Sequence=VSP_012363, VSP_012364;
CC       Name=3; Synonyms=Dido2;
CC         IsoId=Q8C9B9-3; Sequence=VSP_026606, VSP_026607;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at intermediate levels.
CC   -!- INDUCTION: Up-regulated during apoptosis.
CC   -!- SIMILARITY: Contains 1 PHD-type zinc finger.
CC   -!- SIMILARITY: Contains 1 TFIIS central domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH44755.1; Type=Erroneous initiation;
CC       Sequence=BAC28053.1; Type=Erroneous initiation;
CC       Sequence=BAC97927.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AJ238332; CAB48401.1; -; mRNA.
DR   EMBL; AY425951; AAR84049.1; -; mRNA.
DR   EMBL; AY425952; AAR84050.1; -; mRNA.
DR   EMBL; AK129117; BAC97927.1; ALT_INIT; mRNA.
DR   EMBL; AK032843; BAC28053.1; ALT_INIT; mRNA.
DR   EMBL; AK042474; BAC31270.1; -; mRNA.
DR   EMBL; AK044919; BAC32141.1; -; mRNA.
DR   EMBL; AL732560; CAM27684.1; -; Genomic_DNA.
DR   EMBL; AL732560; CAM27685.1; -; Genomic_DNA.
DR   EMBL; AL732560; CAM27686.1; -; Genomic_DNA.
DR   EMBL; AL732560; CAM27687.1; -; Genomic_DNA.
DR   EMBL; BC029110; AAH29110.1; -; mRNA.
DR   EMBL; BC044755; AAH44755.1; ALT_INIT; mRNA.
DR   EMBL; BC096662; AAH96662.1; -; mRNA.
DR   EMBL; BC138712; AAI38713.1; -; mRNA.
DR   EMBL; BC138713; AAI38714.1; -; mRNA.
DR   IPI; IPI00227469; -.
DR   IPI; IPI00453851; -.
DR   IPI; IPI00828403; -.
DR   RefSeq; NP_035935.2; NM_011805.2.
DR   RefSeq; NP_780760.2; NM_175551.3.
DR   RefSeq; NP_808520.2; NM_177852.3.
DR   UniGene; Mm.253836; -.
DR   UniGene; Mm.481681; -.
DR   PDB; 1WEM; NMR; -; A=257-319.
DR   PDBsum; 1WEM; -.
DR   ProteinModelPortal; Q8C9B9; -.
DR   SMR; Q8C9B9; 257-319, 665-771.
DR   STRING; Q8C9B9; -.
DR   PhosphoSite; Q8C9B9; -.
DR   PRIDE; Q8C9B9; -.
DR   Ensembl; ENSMUST00000087517; ENSMUSP00000084794; ENSMUSG00000038914.
DR   Ensembl; ENSMUST00000103056; ENSMUSP00000099345; ENSMUSG00000038914.
DR   GeneID; 23856; -.
DR   KEGG; mmu:23856; -.
DR   UCSC; uc008oju.1; mouse.
DR   CTD; 23856; -.
DR   MGI; MGI:1344352; Dido1.
DR   eggNOG; roNOG06980; -.
DR   GeneTree; ENSGT00530000063844; -.
DR   HOVERGEN; HBG060199; -.
DR   InParanoid; Q8C9B9; -.
DR   OMA; GPPPGHF; -.
DR   NextBio; 303557; -.
DR   ArrayExpress; Q8C9B9; -.
DR   Bgee; Q8C9B9; -.
DR   CleanEx; MM_DIDO1; -.
DR   CleanEx; MM_DIO1; -.
DR   Genevestigator; Q8C9B9; -.
DR   GO; GO:0005737; C:cytoplasm; TAS:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IDA:MGI.
DR   GO; GO:0006350; P:transcription; IEA:InterPro.
DR   InterPro; IPR012921; SPOC_C.
DR   InterPro; IPR003618; TFIIS_cen_dom.
DR   InterPro; IPR017890; TFS2M.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:1.10.472.30; TFIIS_centre; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF07744; SPOC; 1.
DR   Pfam; PF07500; TFIIS_M; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00510; TFS2M; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   SUPFAM; SSF46942; TFIIS_centre; 1.
DR   PROSITE; PS51321; TFIIS_CENTRAL; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Apoptosis; Cytoplasm;
KW   Direct protein sequencing; Metal-binding; Nucleus; Phosphoprotein;
KW   Zinc; Zinc-finger.
FT   CHAIN         1   2256       Death-inducer obliterator 1.
FT                                /FTId=PRO_0000059325.
FT   DOMAIN      667    787       TFIIS central.
FT   ZN_FING     265    319       PHD-type.
FT   MOTIF       162    170       Nuclear localization signal (Potential).
FT   MOTIF       182    190       Nuclear localization signal (Potential).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES       8      8       Phosphoserine.
FT   MOD_RES     148    148       Phosphothreonine.
FT   MOD_RES     149    149       Phosphoserine (By similarity).
FT   MOD_RES     151    151       Phosphoserine (By similarity).
FT   MOD_RES     522    522       Phosphoserine (By similarity).
FT   MOD_RES     647    647       Phosphoserine (By similarity).
FT   MOD_RES     674    674       Phosphoserine (By similarity).
FT   MOD_RES     802    802       Phosphoserine.
FT   MOD_RES     806    806       Phosphoserine (By similarity).
FT   MOD_RES    1016   1016       Phosphoserine (By similarity).
FT   MOD_RES    1027   1027       Phosphoserine (By similarity).
FT   MOD_RES    1035   1035       Phosphoserine (By similarity).
FT   MOD_RES    1243   1243       Phosphoserine (By similarity).
FT   MOD_RES    1256   1256       Phosphoserine.
FT   MOD_RES    1305   1305       Phosphothreonine (By similarity).
FT   MOD_RES    1307   1307       Phosphoserine (By similarity).
FT   MOD_RES    1463   1463       Phosphoserine (By similarity).
FT   MOD_RES    1726   1726       Phosphoserine (By similarity).
FT   VAR_SEQ     529    614       SMKDDRRVEDRTMAAVTIPKKALPSASLVGRQTSPRNLVPK
FT                                KLPPYSNMAGAKPAIKKLPSGFKGTIPKRPWPSATLSGTSA
FT                                RQAG -> CTYHPKAGFPGPSHHLGGCLGLSRTRVLGVLVL
FT                                IVASSSLPARSRYQDASGPQVFLPSLWSLSGWFLKSCVGLM
FT                                LEAISYFSFRPW (in isoform 2).
FT                                /FTId=VSP_012363.
FT   VAR_SEQ     615   2256       Missing (in isoform 2).
FT                                /FTId=VSP_012364.
FT   VAR_SEQ    1177   1183       LESPRPN -> KHPVSGR (in isoform 3).
FT                                /FTId=VSP_026606.
FT   VAR_SEQ    1184   2256       Missing (in isoform 3).
FT                                /FTId=VSP_026607.
FT   CONFLICT     45     45       V -> A (in Ref. 1; CAB48401).
FT   CONFLICT    331    331       D -> N (in Ref. 1; CAB48401).
FT   CONFLICT    353    353       V -> I (in Ref. 4; BAC31270).
FT   CONFLICT    436    436       P -> K (in Ref. 6; AAH29110).
FT   CONFLICT    688    688       D -> Y (in Ref. 2; AAR84049/AAR84050).
FT   CONFLICT    718    718       Y -> F (in Ref. 2; AAR84049/AAR84050).
FT   CONFLICT   1739   1739       P -> L (in Ref. 2; AAR84050).
FT   CONFLICT   2046   2046       Q -> H (in Ref. 2; AAR84050).
FT   CONFLICT   2049   2049       K -> T (in Ref. 2; AAR84050).
FT   CONFLICT   2054   2054       E -> K (in Ref. 2; AAR84050).
FT   CONFLICT   2058   2058       A -> P (in Ref. 2; AAR84050).
FT   CONFLICT   2118   2118       Q -> L (in Ref. 4; BAC28053).
FT   STRAND      279    281
FT   STRAND      283    285
FT   STRAND      288    290
FT   HELIX       291    294
FT   HELIX       298    307
SQ   SEQUENCE   2256 AA;  247176 MW;  CB4F6F6D3FE53747 CRC64;
     MDDKGHLSNE EAPKAIKPTS KEFRKTWGFR RTTIAKREGA GDTEVDPSEQ QPQQHNLSLR
     RSGRQPKRTE RVEEFLTTVR RRGKKNVPVS LEDSSEPTSS TVTDVETASE GSVESSSEIR
     SGPVSDSLGK EHPASSEKAK GGEEEEDTSD SDSDGLTLKE LQNRLRRKRE QEPVERSLRG
     SQNRLRKKRR EEDSAETGSV QIGSAEQDRP LCKQEPEASQ GPVSQSETDD IENQLEGKAT
     QGNTEENPRE AGKPKPECEV YDPNALYCIC RQPHNNRFMI CCDRCEEWFH GDCVGISEAR
     GRLLERNGED YICPNCTILQ VQDETNGSAT DEQDSGCRSV GADGTDCTSI GTVEQKSGED
     QGIKGRIEKA ANPSGKKKLK IFQPVVEAPG APKCIGPGCS SVAQPDSVYC SNDCILKHAA
     ATMRFLSSGK EQKTKPKEKV KTKPEKFSLP KCSVQVGIKI SSVHKRLASE KRENPVKKVM
     LASRSETSGK EAACESSTPS WASDHNYNAV KPEKPEKPTA LSPTLLSKSM KDDRRVEDRT
     MAAVTIPKKA LPSASLVGRQ TSPRNLVPKK LPPYSNMAGA KPAIKKLPSG FKGTIPKRPW
     PSATLSGTSA RQAGPTPMTA ASKKLPGSAA VVGVTRKPMS ANVPAASPAP GRLGPVSPAP
     SQPNSQIRQN IRRSLKEILW KRVNDSDDLI MTENEVGKIA LHIEKEMFNL FQVTDNRYKS
     KYRSIMFNLK DPKNQGLFHR VLREEISLAK LVRMKPEELV SKELSMWTEK PTKSVIESRT
     KLLNESKKNT TKPETIPDME DSPPVSDSEE QQESVRAAPE KSAAPLLDVF SSMLKDTTSQ
     HRAHLFDLNC KICTGQVPSS EDEPAPKKQK LSASSKKEDF KPRHDSSPPN AVPNTADEGI
     ADTLPENASE PDPESTSSLN QERKCFPESP GDSHPEPSSL GGLSPSSASG GSGVVTTVTM
     SGRDPRTALS GSCTVTASMA AHLDNSQASE TKLDMIKPAL TSAVVPKSIL AKPSSSPDPR
     YLSVPPSPSI SESRSPPEGD TTLFLSRLNT IWKGFINMQS VAKFVTKAYP VSGCLDYLSE
     DLPDTIHIGG RIAPKTVWDY VGKLKSSVSK ELCLIRFHPA TEEEEVAYIS LYSYFSSRGR
     FGVVANNNRH VKDLYLIPLS AKDPVPSKLL PFEGPGLESP RPNIILGLVI CQKVKRPSSA
     GELDKTDEKR TRLQQEELET SVYPKVTAAL PSEKKPPKYS VHSIDTAATS TTPPGSPPPP
     PPLPEPPVLK ILSSLKPGST STVTAPTTAA ITTTASPVTA ATSKTASPLE HILQTLFGKK
     KSFEPSGKES VGSTLSPHQD SKAKGEDTMS AAPLLDPIVQ QFGQFSKDKA LEEEEEDDRP
     YDPEEEYNPD RAFHTLLAEP GRPHDVQSVS ETAEREEVAY DPEDETILEE AKVTIDDLPN
     RMCMKVSATE RPADFTTDAS SASLVEQQKM LEELNKQIEE QKRQLEEQEE ALRQQRAAVG
     VSMAHFSVSD ALMSPPPKSS LGKTELFSQE QQAPDPSQGA PNTNHNLDSR QSRDPRQARR
     LAAENTENES LPRAPTGSTP GPQGTLPARE TPAGTAVVQG PGLAAEAKES MAVPWAPGEN
     AVLRPEHDIQ KCEHPGNPVS LPLDTSHLPT AGDGAARPAP PRRVLLPTPP STTFPPSFPL
     QPKAQNFSSG SREPFSGPTF MSQETSLGSS QYEDPRGAQS AGKNDSPVAD MEDSREPQPR
     PGESTTSFPQ PGQRGGGPQP QFPGQREPAP RTFGMSGHHG PSFPGPRGPV PPYSEENLVP
     NSDGPRGPPP ARFGAQKPPI PSLFSGQHGP PPYGDNRGLS PSYLGGPRGG APAQFEDRKD
     PHGEKREFQD TPYNEMTGAP AQCEGPDQAQ FMGNRAPFQF GGQRRPLLTQ MKGPRGGPPP
     SQFGAQRGPP PGHFVGPRGP HPSQFENSRG THPGQFEGAR GQAPGFMPGP RGIQPQQFEE
     QRVNSPPRFA GQRASAPLPY GGPRGPAPFP EKNEQPPSRF HFQGPSSQPV KPPPRPLLEL
     PSHPPQHRKD RWDEAGPATA LPSSAGPGQG HEADGQWATS EFREGKGHEY RSPAFEGRQR
     ERFEAGSKEK PLDEPEAQGL ESRQGRAFED RRRERERGRN WSRERDWERS RDWDRHREWD
     KGRDRSSNRD RERDNDRAKE WDRSRERSRN RDRDRERRRD RDRSRSRDRD RDRERARDRD
     RDRGRDRKDR SKSRESPRDQ KPEARTSEGG PAAAQA
//
ID   FA40B_MOUSE             Reviewed;         844 AA.
AC   Q8C9H6; Q3TQB7; Q80TI6; Q8C7A2;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Protein FAM40B;
GN   Name=Fam40b; Synonyms=Kiaa1170;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 46-844 (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8C9H6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8C9H6-4; Sequence=VSP_019001, VSP_019002;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8C9H6-3; Sequence=VSP_014870;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the FAM40 family.
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DR   EMBL; AK042073; BAC31154.1; -; mRNA.
DR   EMBL; AK163706; BAE37467.1; -; mRNA.
DR   EMBL; AK122459; BAC65741.1; -; mRNA.
DR   IPI; IPI00465770; -.
DR   IPI; IPI00607991; -.
DR   IPI; IPI00759974; -.
DR   RefSeq; NP_001032829.1; NM_001037740.1.
DR   RefSeq; NP_796178.2; NM_177204.3.
DR   UniGene; Mm.56097; -.
DR   PhosphoSite; Q8C9H6; -.
DR   PRIDE; Q8C9H6; -.
DR   Ensembl; ENSMUST00000046028; ENSMUSP00000036477; ENSMUSG00000039629.
DR   Ensembl; ENSMUST00000115224; ENSMUSP00000110879; ENSMUSG00000039629.
DR   GeneID; 320609; -.
DR   KEGG; mmu:320609; -.
DR   UCSC; uc009bem.1; mouse.
DR   UCSC; uc009ben.1; mouse.
DR   UCSC; uc009beo.1; mouse.
DR   CTD; 320609; -.
DR   MGI; MGI:2444363; Fam40b.
DR   eggNOG; roNOG15190; -.
DR   GeneTree; ENSGT00400000022095; -.
DR   HOGENOM; HBG356504; -.
DR   HOVERGEN; HBG081506; -.
DR   InParanoid; Q8C9H6; -.
DR   OMA; FKTQVQG; -.
DR   OrthoDB; EOG49ZXNQ; -.
DR   PhylomeDB; Q8C9H6; -.
DR   NextBio; 397061; -.
DR   ArrayExpress; Q8C9H6; -.
DR   Bgee; Q8C9H6; -.
DR   Genevestigator; Q8C9H6; -.
DR   GermOnline; ENSMUSG00000039629; Mus musculus.
DR   InterPro; IPR021819; DUF3402.
DR   InterPro; IPR012486; N1221.
DR   Pfam; PF11882; DUF3402; 1.
DR   Pfam; PF07923; N1221; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing.
FT   CHAIN         1    844       Protein FAM40B.
FT                                /FTId=PRO_0000187023.
FT   VAR_SEQ     659    662       EAGD -> GLSV (in isoform 2).
FT                                /FTId=VSP_019001.
FT   VAR_SEQ     663    844       Missing (in isoform 2).
FT                                /FTId=VSP_019002.
FT   VAR_SEQ     694    721       Missing (in isoform 3).
FT                                /FTId=VSP_014870.
FT   CONFLICT     47     47       Q -> L (in Ref. 2; BAC65741).
SQ   SEQUENCE   844 AA;  96294 MW;  78E4D64476A7B097 CRC64;
     MDDPAAPGPA GSPANDNGNG NGNGNGNGNG GKGKPAVPKG RETFRNQRRE SEGSVDCPTL
     EFEYGDSDGH AAELSELYSY TENLEFTTNR KCFEEDFRTQ VQDTKEWLEL EEDAQKTYVM
     GLLDRLEVVS REKRLKVARA VLYLAQGTFG ECDSEVDVLH WSRYNCFLLY QMGTFSAFLE
     LLHMEIDNSQ ASSSALRKPA VSIADSTELR VLLSVMYLMV ENIRLEREID PCGWRTARET
     FRTELSFSTH NEEPFALLLF SMVTKFCSGL APHFPIKKVL LLLWKVVMFT LGGFEHLQAL
     KIQKRAELGL PPLAEDSIQV VKSMRAASPP SYTLDLGESQ LAPPPSKLRG RRGSRRQLLT
     KQDSLDIYNE RDLFKTEEPA TEEEEESAAD GERTLDGELD LLEQDPLVPP PPSQTPLSTD
     RVAFPKGLPW APKVRQKDIE HFLEMSRNKF IGFTLGQDTD TLVGLPRPIH ESVKTLKQHK
     YISIADIQIK NEEELEKCPL SLGEEVVPET PSEILYQGML YSLPQYMIAL LKILLAAAPT
     SKAKTDSINI LADVLPEEMP VTVLQSMKLG IDVNRHKEII VKSISALLLL LLKHFKLNHI
     YQFEYVSQHL VFANCIPLIL KFFNQNILSY ITAKNSISVL DYPCCTIQDL PELTTESLEA
     GDNSQFCWRN LFSCINLLRL LNKLTKWKHS RTMMLVVFKS APILKRALKV KQAMLQLYVL
     KLLKIQTKYL GRQWRKSNMK TMSAIYQKVR HRMNDDWAYG NDIDARPWDF QAEECTLRAN
     IEAFNSRRYD KPQDSEFSPV DNCLQSVLGQ RLDLPEDFHY SYELWLEREV FSQPICWEEL
     LQNH
//
ID   CJ118_MOUSE             Reviewed;         917 AA.
AC   Q8C9S4; Q6P3D6; Q8CJC0;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Uncharacterized protein C10orf118 homolog;
DE   AltName: Full=Oocyte-testis gene 1 protein;
GN   Name=Otg1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Varani S., Racie L., Matzuk M.M.;
RT   "Expression and genomic characterization of Otg1, a novel gene
RT   expressed in postnatal germ cells in the mouse.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-362.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-234.
RC   STRAIN=Czech II; TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- TISSUE SPECIFICITY: Expressed in postnatal germ cells.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-19 is the initiator.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH64039.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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DR   EMBL; AF349751; AAN61566.1; -; mRNA.
DR   EMBL; AK041398; BAC30931.1; -; mRNA.
DR   EMBL; BC064039; AAH64039.1; ALT_SEQ; mRNA.
DR   IPI; IPI00229968; -.
DR   RefSeq; NP_739563.1; NM_170757.1.
DR   UniGene; Mm.131555; -.
DR   ProteinModelPortal; Q8C9S4; -.
DR   PhosphoSite; Q8C9S4; -.
DR   PRIDE; Q8C9S4; -.
DR   Ensembl; ENSMUST00000076085; ENSMUSP00000075454; ENSMUSG00000035173.
DR   Ensembl; ENSMUST00000118592; ENSMUSP00000113457; ENSMUSG00000035173.
DR   GeneID; 213993; -.
DR   KEGG; mmu:213993; -.
DR   UCSC; uc008hzg.1; mouse.
DR   MGI; MGI:2445022; A630007B06Rik.
DR   eggNOG; roNOG10505; -.
DR   GeneTree; ENSGT00390000010528; -.
DR   HOGENOM; HBG443854; -.
DR   HOVERGEN; HBG081202; -.
DR   InParanoid; Q8C9S4; -.
DR   OMA; KGEHALV; -.
DR   OrthoDB; EOG4P8FHJ; -.
DR   NextBio; 374162; -.
DR   ArrayExpress; Q8C9S4; -.
DR   Bgee; Q8C9S4; -.
DR   CleanEx; MM_A630007B06RIK; -.
DR   Genevestigator; Q8C9S4; -.
DR   GermOnline; ENSMUSG00000035173; Mus musculus.
PE   2: Evidence at transcript level;
KW   Coiled coil.
FT   CHAIN         1    917       Uncharacterized protein C10orf118
FT                                homolog.
FT                                /FTId=PRO_0000089824.
FT   COILED      220    736       Potential.
FT   COILED      778    822       Potential.
FT   COILED      874    913       Potential.
FT   COMPBIAS    737    766       Ser-rich.
SQ   SEQUENCE   917 AA;  104901 MW;  3409DE3409A8E1D6 CRC64;
     MKIRSRFEEM QSELVPVSMS ETEHIASISS DATTEKTSEL RDDSCISVSG DESSRLETGA
     ELLSLDSDRI LCQTNEHCSQ IEVQESHIPD CGSGENSCAN TDTCPEDSGQ IDDFPGGDFT
     EQVSKTKEPE QTVTQILAEL KSSAPAEAAN PKTASASLYD TDCTRKLISE MKTVSASDDL
     LGEIESELLS AEFAEGHQVP NGLNKGEQAL ALFEKCVHSR YLQQELTVKQ LIKENKNHQE
     LILNICSEKD SLREELRKRT ETEKQHMNTI KQLELRIEEL NKEIKASKDQ LVAQDVTAKN
     AIQQIHKEMA QRMDQANKKC EEARQEKEAM VMKYVRGEKE ALDLRKEKET LERKLRDASK
     ELEKNTNKIK QLSQEKGRLQ QLYESKEGET TRLIREIEKL KEEMNSQVIK VKWAQNKLKA
     EMDSHKETKD KLKETTTKLT QAKEEAEQIR QNCQDMIKTY QESEEIKSNE LDAKLRVTKG
     ELEKQMQEKS DQLEMHHAKI KELEDLKRTF KEGMDELRTL RTKAKCLEDE RLRTEDELSK
     YREIINRQKS EIQNLLDKVK ITDQLHEQLQ SGKQEIEHLK EEMESLNSLI NDLQKDIEGS
     RKRESELLLF TEKLTSKNAQ LQSESSALQS QVDNLSCTES QLQSQCQQMG QANRNLESKL
     LKEEELRKEE VQTLQAELSA AQTEVKALST QVEELKDELV TQRRKHASNV KDLSKQLQQA
     RRKLEQTENG NHDKDISSMG SRSSSSGSLN ARISAEDRSP ENTSSSVAVD NFPEVDKAML
     IERIVRLQKA HARKNEKIEF MEDHIKQLVE EIRKKTKIIQ SYVLREESGT LSSEASDFNK
     VHLSRRGGIM ASLYTSHPAD SGLTLELSLE INRKLQAVLE DTLLKNITLK ENLQTLGTEI
     ERLIKHQHEL EQRTKKA
//
ID   PDE10_MOUSE             Reviewed;         790 AA.
AC   Q8CA95; Q3TLU6; Q3TRG6; Q69C21; Q9WVI1;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   08-FEB-2011, entry version 57.
DE   RecName: Full=cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A;
DE            EC=3.1.4.17;
DE            EC=3.1.4.35;
GN   Name=Pde10a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   MEDLINE=99289599; PubMed=10359840; DOI=10.1073/pnas.96.12.7071;
RA   Soderling S.H., Bayuga S.J., Beavo J.A.;
RT   "Isolation and characterization of a dual-substrate phosphodiesterase
RT   gene family: PDE10A.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:7071-7076(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INDUCTION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=C57BL/6 X CBA; TISSUE=Corpus striatum;
RX   PubMed=14751289; DOI=10.1016/j.neuroscience.2003.11.009;
RA   Hebb A.L., Robertson H.A., Denovan-Wright E.M.;
RT   "Striatal phosphodiesterase mRNA and protein levels are reduced in
RT   Huntington's disease transgenic mice prior to the onset of motor
RT   symptoms.";
RL   Neuroscience 123:967-981(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland, Spinal cord, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Plays a role in signal transduction by regulating the
CC       intracellular concentration of cyclic nucleotides. Can hydrolyze
CC       both cAMP and cGMP, but has higher affinity for cAMP and is more
CC       efficient with cAMP as substrate. May play a critical role in
CC       regulating cAMP and cGMP levels in the striatum, a region of the
CC       brain that contributes to the control of movement and cognition.
CC   -!- CATALYTIC ACTIVITY: Nucleoside 3',5'-cyclic phosphate + H(2)O =
CC       nucleoside 5'-phosphate.
CC   -!- CATALYTIC ACTIVITY: Guanosine 3',5'-cyclic phosphate + H(2)O =
CC       guanosine 5'-phosphate.
CC   -!- COFACTOR: Binds 2 divalent metal cations per subunit. Site 1 may
CC       preferentially bind zinc ions, while site 2 has a preference for
CC       magnesium and/or manganese ions (By similarity).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.05 uM for cAMP;
CC         KM=3 uM for cGMP;
CC   -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC       3',5'-cyclic AMP: step 1/1.
CC   -!- PATHWAY: Purine metabolism; 3',5'-cyclic GMP degradation; GMP from
CC       3',5'-cyclic GMP: step 1/1.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8CA95-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CA95-2; Sequence=VSP_035917;
CC       Name=3;
CC         IsoId=Q8CA95-3; Sequence=VSP_035916;
CC       Name=4;
CC         IsoId=Q8CA95-4; Sequence=VSP_035915, VSP_035918;
CC   -!- TISSUE SPECIFICITY: Detected in striatum (at protein level).
CC       Detected in testis and brain.
CC   -!- INDUCTION: Down-regulated by the expression of a huntingtin (HD)
CC       gene with an expanded polyglutamine repeat prior to the onset of
CC       neurological symptoms related to Huntington disease.
CC   -!- DOMAIN: The tandem GAF domains bind cAMP, and regulate enzyme
CC       activity. The binding of cAMP stimulates enzyme activity (By
CC       similarity).
CC   -!- DOMAIN: Composed of a C-terminal catalytic domain containing two
CC       divalent metal sites and an N-terminal regulatory domain which
CC       contains one cyclic nucleotide-binding region (By similarity).
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
CC       family.
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DR   EMBL; AF110507; AAD31544.1; -; mRNA.
DR   EMBL; AY360383; AAR12579.1; -; mRNA.
DR   EMBL; AK039249; BAC30292.1; -; mRNA.
DR   EMBL; AK162804; BAE37063.1; -; mRNA.
DR   EMBL; AK166310; BAE38696.1; -; mRNA.
DR   EMBL; CH466619; EDL02097.1; -; Genomic_DNA.
DR   EMBL; CH466619; EDL02099.1; -; Genomic_DNA.
DR   EMBL; BC113201; AAI13202.1; -; mRNA.
DR   IPI; IPI00468960; -.
DR   IPI; IPI00621783; -.
DR   IPI; IPI00830614; -.
DR   IPI; IPI00831191; -.
DR   RefSeq; NP_035996.2; NM_011866.2.
DR   UniGene; Mm.87161; -.
DR   HSSP; O76074; 1UDT.
DR   ProteinModelPortal; Q8CA95; -.
DR   SMR; Q8CA95; 74-761.
DR   STRING; Q8CA95; -.
DR   PhosphoSite; Q8CA95; -.
DR   PRIDE; Q8CA95; -.
DR   Ensembl; ENSMUST00000115724; ENSMUSP00000111389; ENSMUSG00000023868.
DR   GeneID; 23984; -.
DR   KEGG; mmu:23984; -.
DR   CTD; 23984; -.
DR   MGI; MGI:1345143; Pde10a.
DR   GeneTree; ENSGT00590000082915; -.
DR   HOVERGEN; HBG082113; -.
DR   NextBio; 303873; -.
DR   ArrayExpress; Q8CA95; -.
DR   Bgee; Q8CA95; -.
DR   Genevestigator; Q8CA95; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:EC.
DR   GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR003607; Metal-dep_PHydrolase_HD_dom.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR023174; PDEase_CS.
DR   Gene3D; G3DSA:1.10.1300.10; PDEase_catalytic_dom; 1.
DR   Pfam; PF01590; GAF; 2.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00065; GAF; 2.
DR   SMART; SM00471; HDc; 1.
DR   PROSITE; PS00126; PDEASE_I; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; Alternative splicing; cAMP; cAMP-binding; cGMP;
KW   cGMP-binding; Cytoplasm; Hydrolase; Metal-binding; Nucleotide-binding;
KW   Repeat.
FT   CHAIN         1    790       cAMP and cAMP-inhibited cGMP 3',5'-cyclic
FT                                phosphodiesterase 10A.
FT                                /FTId=PRO_0000355558.
FT   REGION      290    291       Allosteric effector binding (By
FT                                similarity).
FT   REGION      334    335       Allosteric effector binding (By
FT                                similarity).
FT   ACT_SITE    519    519       Proton donor (By similarity).
FT   METAL       523    523       Divalent metal cation 1 (By similarity).
FT   METAL       557    557       Divalent metal cation 1 (By similarity).
FT   METAL       558    558       Divalent metal cation 1 (By similarity).
FT   METAL       558    558       Divalent metal cation 2 (By similarity).
FT   METAL       668    668       Divalent metal cation 1 (By similarity).
FT   BINDING     368    368       Allosteric effector (By similarity).
FT   BINDING     387    387       Allosteric effector (By similarity).
FT   BINDING     519    519       Substrate (By similarity).
FT   BINDING     720    720       Substrate (By similarity).
FT   VAR_SEQ       1     60       Missing (in isoform 4).
FT                                /FTId=VSP_035915.
FT   VAR_SEQ       1     17       MSNDSTEGTVGSCNATG -> MEDGPSNNASCFRRLTECFL
FT                                SPS (in isoform 3).
FT                                /FTId=VSP_035916.
FT   VAR_SEQ       1     16       MSNDSTEGTVGSCNAT -> MEKLY (in isoform 2).
FT                                /FTId=VSP_035917.
FT   VAR_SEQ      61     69       EPSPKEVSR -> MPGPGQ (in isoform 4).
FT                                /FTId=VSP_035918.
FT   CONFLICT    774    774       P -> Q (in Ref. 3; BAC30292).
SQ   SEQUENCE   790 AA;  89408 MW;  1B1D8111A5AD7B92 CRC64;
     MSNDSTEGTV GSCNATGLTD EKVKAYLSLH PQVLDEFVSE SVSAETVEKW LKRKTNKAKD
     EPSPKEVSRY QDTNMQGVVY ELNSYIEQRL DTGGDNHLLL YELSSIIRIA TKADGFALYF
     LGECNNSLCV FIPPGMKEGQ PRLIPAGPIT QGTTISAYVA KSRKTLLVED ILGDERFPRG
     TGLESGTRIQ SVLCLPIVTA IGDLIGILEL YRHWGKEAFC LSHQEVATAN LAWASVAIHQ
     VQVCRGLAKQ TELNDFLLDV SKTYFDNIVA IDSLLEHIMI YAKNLVNADR CALFQVDHKN
     KELYSDLFDI GEEKEGKPIF KKTKEIRFSI EKGIAGQVAR TGEVLNIPDA YADPRFNREV
     DLYTGYTTRN ILCMPIVSRG SVIGVVQMVN KISGSAFSKT DENNFKMFAV FCALALHCAN
     MYHRIRHSEC IYRVTMEKLS YHSICTSEEW QGLMRFNLPA RICRDIELFH FDIGPFENMW
     PGIFVYMIHR SCGTSCFELE KLCRFIMSVK KNYRRVPYHN WKHAVTVAHC MYAILQNNNG
     LFTDLERKGL LIACLCHDLD HRGFSNSYLQ KFDHPLAALY STSTMEQHHF SQTVSILQLE
     GHNIFSTLSS SEYEQVLEII RKAIIATDLA LYFGNRKQLE EMYQTGSLNL HNQSHRDRVI
     GLMMTACDLC SVTKLWPVTK LTANDIYAEF WAEGDEMKKL GIQPIPMMDR DKRDEVPQGQ
     LGFYNAVAIP CYTTLTQILP PTEPLLKACR DNLNQWEKVI RGEETAMWIS GPGPAPSKST
     PEKLNVKVED
//
ID   F163A_MOUSE             Reviewed;         168 AA.
AC   Q8CAA5;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Protein FAM163A;
GN   Name=Fam163a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the FAM163 family.
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DR   EMBL; AK039197; BAC30275.1; -; mRNA.
DR   EMBL; BC116972; AAI16973.1; -; mRNA.
DR   EMBL; BC116974; AAI16975.1; -; mRNA.
DR   IPI; IPI00228058; -.
DR   RefSeq; NP_808506.1; NM_177838.2.
DR   UniGene; Mm.150857; -.
DR   PRIDE; Q8CAA5; -.
DR   Ensembl; ENSMUST00000015628; ENSMUSP00000015628; ENSMUSG00000015484.
DR   GeneID; 329274; -.
DR   KEGG; mmu:329274; -.
DR   UCSC; uc007dce.1; mouse.
DR   CTD; 329274; -.
DR   MGI; MGI:3618859; Fam163a.
DR   GeneTree; ENSGT00390000002397; -.
DR   HOGENOM; HBG445382; -.
DR   HOVERGEN; HBG100700; -.
DR   InParanoid; Q8CAA5; -.
DR   OMA; SPFYIRT; -.
DR   OrthoDB; EOG4S1T8B; -.
DR   PhylomeDB; Q8CAA5; -.
DR   NextBio; 398663; -.
DR   ArrayExpress; Q8CAA5; -.
DR   Bgee; Q8CAA5; -.
DR   Genevestigator; Q8CAA5; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    168       Protein FAM163A.
FT                                /FTId=PRO_0000280257.
FT   TRANSMEM      6     26       Helical; (Potential).
SQ   SEQUENCE   168 AA;  17839 MW;  414769B3494D3CC5 CRC64;
     MTAGTVVITG GILATVILLC IIAVLCYCRL QYYCCKKGTD GEDAEEEEEE EEHGLSIHPR
     VPACNACSSH VLDGRGGLAP LTSESCSQPC GVASHCTTCS PYRTPFYIRT ADMVPNGGGG
     ERLSFAPTHY KEGGTPSLKL AAPQNYPVTW PSSGHEAFTN PRAISTDV
//
ID   PGM2L_MOUSE             Reviewed;         621 AA.
AC   Q8CAA7;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Glucose 1,6-bisphosphate synthase;
DE            EC=2.7.1.106;
DE   AltName: Full=Phosphoglucomutase-2-like 1;
GN   Name=Pgm2l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 142-150 AND 600-613, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=17804405; DOI=10.1074/jbc.M706818200;
RA   Maliekal P., Sokolova T., Vertommen D., Veiga-da-Cunha M.,
RA   Van Schaftingen E.;
RT   "Molecular identification of mammalian phosphopentomutase and glucose-
RT   1,6-bisphosphate synthase, two members of the alpha-D-
RT   phosphohexomutase family.";
RL   J. Biol. Chem. 282:31844-31851(2007).
CC   -!- FUNCTION: Glucose 1,6-bisphosphate synthase using 1,3-
CC       bisphosphoglycerate as a phosphate donor and a series of 1-
CC       phosphate sugars as acceptors, including glucose 1-phosphate,
CC       mannose 1-phosphate, ribose 1-phosphate and deoxyribose 1-
CC       phosphate. 5 or 6-phosphosugars are bad substrates, with the
CC       exception of glucose 6-phosphate. Also synthesizes ribose 1,5-
CC       bisphosphate. Has only low phosphopentomutase and
CC       phosphoglucomutase activities (By similarity).
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glyceroyl phosphate + alpha-D-
CC       glucose 1-phosphate = 3-phospho-D-glycerate + alpha-D-glucose 1,6-
CC       bisphosphate.
CC   -!- TISSUE SPECIFICITY: Expressed at highest levels in the brain and
CC       testis, at intermediate levels in thymus, spleen, lung and
CC       skeletal muscle, and at lowest levels in kidney, liver and heart.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK039189; BAC30270.1; -; mRNA.
DR   EMBL; BC076571; AAH76571.1; -; mRNA.
DR   IPI; IPI00228059; -.
DR   RefSeq; NP_081905.1; NM_027629.3.
DR   UniGene; Mm.440524; -.
DR   ProteinModelPortal; Q8CAA7; -.
DR   SMR; Q8CAA7; 557-605.
DR   STRING; Q8CAA7; -.
DR   PhosphoSite; Q8CAA7; -.
DR   PRIDE; Q8CAA7; -.
DR   Ensembl; ENSMUST00000054436; ENSMUSP00000054782; ENSMUSG00000030729.
DR   Ensembl; ENSMUST00000084935; ENSMUSP00000081998; ENSMUSG00000030729.
DR   GeneID; 70974; -.
DR   KEGG; mmu:70974; -.
DR   UCSC; uc009imq.1; mouse.
DR   CTD; 70974; -.
DR   MGI; MGI:1918224; Pgm2l1.
DR   eggNOG; roNOG10554; -.
DR   GeneTree; ENSGT00390000017247; -.
DR   HOGENOM; HBG571743; -.
DR   HOVERGEN; HBG056917; -.
DR   InParanoid; Q8CAA7; -.
DR   OMA; HIIGQEV; -.
DR   OrthoDB; EOG4BRWKK; -.
DR   PhylomeDB; Q8CAA7; -.
DR   BRENDA; 2.7.1.106; 244.
DR   NextBio; 332727; -.
DR   ArrayExpress; Q8CAA7; -.
DR   Bgee; Q8CAA7; -.
DR   CleanEx; MM_PGM2L1; -.
DR   Genevestigator; Q8CAA7; -.
DR   GermOnline; ENSMUSG00000030729; Mus musculus.
DR   GO; GO:0047933; F:glucose-1,6-bisphosphate synthase activity; IEA:EC.
DR   GO; GO:0016868; F:intramolecular transferase activity, phosphotransferases; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR   InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR   InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR   InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR   InterPro; IPR005843; A-D-PHexomutase_C.
DR   Gene3D; G3DSA:3.40.120.10; A-D-PHexomutase_a/b/a-I/II/III; 3.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   Pfam; PF00408; PGM_PMM_IV; 1.
DR   SUPFAM; SSF53738; A-D-PHexomutase_a/b/a-I/II/III; 3.
DR   PROSITE; PS00710; PGM_PMM; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing;
KW   Glucose metabolism; Isomerase; Phosphoprotein; Transferase.
FT   CHAIN         1    621       Glucose 1,6-bisphosphate synthase.
FT                                /FTId=PRO_0000147785.
FT   ACT_SITE    175    175       Phosphoserine intermediate (By
FT                                similarity).
FT   MOD_RES     175    175       Phosphoserine (By similarity).
SQ   SEQUENCE   621 AA;  70279 MW;  976F86C1FECD52CA CRC64;
     MAENADDDLN SNLLHAPYLT GDPQLDTAIG QWLRWDKNPK TKEQIENLLR NGMNKELRDR
     LCCRMTFGTA GLRSAMGAGF CYINDLTVIQ STQGMYKYLE RCFSDFKQRG FVVGYDTRGQ
     VTSSCSSQRL AKLTAAVLLA KDIPVYLFSR YVPTPFVPYA VQELKAVAGV MITASHNRKE
     DNGYKVYWET GAQITSPHDK EILKCIEECV EPWNDSWNDN LVDTSPLKKD PLQDICKKYM
     EDLKKICFYR DLNSKTTLKF VHTSFHGVGH DYVQLAFQVF GFKPPIPVPE QKDPDPDFST
     VKCPNPEEGE SVLELSLRLA EKENARIVLA TDPDADRLAV AELQENGRWK VFTGNELAAL
     FGWWMFDCWK KNKPNADVKN VYMLATTVSS KILKAIALKE GFHFEETLPG FKWIGSRIKD
     LLGNGKEVLF AFEESIGFLC GTSVLDKDGV SAAAVVAEMA SFLDTRKVTL MEQLTKVYEI
     YGYHMSKTSY FLCYDPPTIK TIFERIRNFE SPKEYPKFCG AFAILHVRDI TTGYDSSQPN
     KKSVLPVSKN SQMITFTFQN GCVATLRTSG TEPKIKYYAE MCASPGQSDT TFLEEELKKL
     IDALIENFLE PSKNALVWRS V
//
ID   PDXL2_MOUSE             Reviewed;         603 AA.
AC   Q8CAE9; Q8CFW3;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Podocalyxin-like protein 2;
DE   AltName: Full=Endoglycan;
DE   Flags: Precursor;
GN   Name=Podxl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
CC   -!- FUNCTION: Acts as a ligand for vascular selectins. Mediates rapid
CC       rolling of leukocytes over vascular surfaces through high affinity
CC       divalent cation-dependent interactions with E-, P- and L-selectins
CC       (By similarity).
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with SELL, SELE
CC       and SELP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8CAE9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CAE9-2; Sequence=VSP_020878, VSP_020879;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8CAE9-3; Sequence=VSP_020877;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Glycosylated; contains chondroitin sulfate. Displays
CC       sialylated O-linked oligosaccharides (By similarity).
CC   -!- PTM: Sulfation is necessary for interaction with SELL. Sialylated
CC       O-linked oligosaccharides are necessary for interaction with SELL,
CC       SELE and SELP (By similarity).
CC   -!- SIMILARITY: Belongs to the podocalyxin family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK038943; BAC30176.1; -; mRNA.
DR   EMBL; AC153923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC033384; AAH33384.1; -; mRNA.
DR   IPI; IPI00229420; -.
DR   IPI; IPI00406801; -.
DR   IPI; IPI00788451; -.
DR   RefSeq; NP_795947.3; NM_176973.4.
DR   UniGene; Mm.302613; -.
DR   UniGene; Mm.442704; -.
DR   STRING; Q8CAE9; -.
DR   PhosphoSite; Q8CAE9; -.
DR   PRIDE; Q8CAE9; -.
DR   Ensembl; ENSMUST00000038409; ENSMUSP00000040417; ENSMUSG00000033152.
DR   Ensembl; ENSMUST00000089447; ENSMUSP00000086870; ENSMUSG00000033152.
DR   GeneID; 319655; -.
DR   KEGG; mmu:319655; -.
DR   UCSC; uc009cvu.1; mouse.
DR   UCSC; uc009cvw.1; mouse.
DR   CTD; 319655; -.
DR   MGI; MGI:2442488; Podxl2.
DR   eggNOG; roNOG11616; -.
DR   GeneTree; ENSGT00570000079197; -.
DR   HOGENOM; HBG283265; -.
DR   HOVERGEN; HBG082114; -.
DR   InParanoid; Q8CAE9; -.
DR   OrthoDB; EOG4TMR1Z; -.
DR   NextBio; 395162; -.
DR   ArrayExpress; Q8CAE9; -.
DR   Bgee; Q8CAE9; -.
DR   CleanEx; MM_PODXL2; -.
DR   Genevestigator; Q8CAE9; -.
DR   GermOnline; ENSMUSG00000033152; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050901; P:leukocyte tethering or rolling; ISS:UniProtKB.
DR   InterPro; IPR013836; CD34/Podocalyxin.
DR   Pfam; PF06365; CD34_antigen; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Disulfide bond; Glycoprotein;
KW   Membrane; Phosphoprotein; Sialic acid; Signal; Sulfation;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     28       Potential.
FT   CHAIN        29    603       Podocalyxin-like protein 2.
FT                                /FTId=PRO_0000252130.
FT   TOPO_DOM     29    499       Extracellular (Potential).
FT   TRANSMEM    500    520       Helical; (Potential).
FT   TOPO_DOM    521    603       Cytoplasmic (Potential).
FT   COMPBIAS    157    186       Glu-rich.
FT   MOD_RES      93     93       Sulfotyrosine (By similarity).
FT   MOD_RES     113    113       Sulfotyrosine (By similarity).
FT   MOD_RES     594    594       Phosphoserine.
FT   CARBOHYD    101    101       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    260    260       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    394    394       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1     64       Missing (in isoform 3).
FT                                /FTId=VSP_020877.
FT   VAR_SEQ     112    131       DYVFPDLTEKVASMEDPGQA -> GSSAHLPLHRISGVIHG
FT                                EGP (in isoform 2).
FT                                /FTId=VSP_020878.
FT   VAR_SEQ     132    603       Missing (in isoform 2).
FT                                /FTId=VSP_020879.
SQ   SEQUENCE   603 AA;  64973 MW;  1FF3CF9472E1BCE3 CRC64;
     MARPLRAARL PPPLLLLLAA GASLGAYAVG VDEPGPEGLT STSLLDLLLP TDFEPLDSEE
     PSEAMGLDAG LAPGSGFPSE DSEESRLLQP PQYFWEEEEL NGSSLDLGPT ADYVFPDLTE
     KVASMEDPGQ APDLPNLPSI LPKMDLAEPP WHMPLQEEEE EEEEEEEERE EEEREKEAEE
     EEEEEELLPV SGSPGATAQA HAPSPSTSSS TSSQSPGATR HRQEDSGDQA TSGMEVESSV
     KPTLSVPSVT PSTVAPGVQN YSQESGGTEW PTGGLGVQSE VPQGAGEGAT VGAADFDGQQ
     GALPSSSLPQ TVPPSGTEVP SEGPLYPRIP DSLPPGPQDT ESTPSSATWG QEGLSEQPLE
     GQAAEAHSLT PWDSTQVICK DWSNLAGKSY IILNMTQNID CEVFRRHRGL RLLALVEEVL
     PRHRSGHRGD WHISLSKPSE KEQHLLMTLV GEQGVVPTQD VLSMLSGIRR SLEEIGIQNY
     STTSSCQARA TQVRSDYGTL FVVLVIIGVI CFIIIVLGLL YNCWQRRMPK LKHVSHGEEL
     RFVENGCHDN PTLDVASDSQ SEMQEKQPSL NGGAINGPSS WSALMGSKRD PEDSDVFEED
     THL
//
ID   NHSL1_MOUSE             Reviewed;        1587 AA.
AC   Q8CAF4; Q5DTY4; Q6P6Y7; Q8C8Z7; Q8K0R2; Q91YY6; Q9CYM2;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 3.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=NHS-like protein 1;
GN   Name=Nhsl1; Synonyms=Kiaa1357;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-526 (ISOFORM 3), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1259-1587 (ISOFORM 1).
RC   STRAIN=Czech II, and FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-446 AND 1140-1587 (ISOFORM
RP   1).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Hypothalamus, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1107-1587 (ISOFORM 1).
RC   TISSUE=Kidney;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1373; SER-1375 AND
RP   THR-1379, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CAF4-1; Sequence=Displayed;
CC       Name=3;
CC         IsoId=Q8CAF4-3; Sequence=VSP_034261, VSP_034263;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the NHS family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH13565.2; Type=Erroneous initiation;
CC       Sequence=AAH30842.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part;
CC       Sequence=AAH61949.1; Type=Erroneous initiation;
CC       Sequence=BAB30793.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC       Sequence=BAC31551.1; Type=Erroneous initiation;
CC       Sequence=BAE22306.1; Type=Erroneous initiation;
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DR   EMBL; AC153560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC153561; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC013565; AAH13565.2; ALT_INIT; mRNA.
DR   EMBL; BC030842; AAH30842.1; ALT_SEQ; mRNA.
DR   EMBL; BC061949; AAH61949.1; ALT_INIT; mRNA.
DR   EMBL; AK038892; BAC30160.2; -; mRNA.
DR   EMBL; AK017530; BAB30793.1; ALT_SEQ; mRNA.
DR   EMBL; AK043447; BAC31551.1; ALT_INIT; mRNA.
DR   EMBL; AK134837; BAE22306.1; ALT_INIT; mRNA.
DR   EMBL; AK220386; BAD90251.1; -; mRNA.
DR   IPI; IPI00169614; -.
DR   IPI; IPI00378754; -.
DR   RefSeq; NP_001157064.1; NM_001163592.1.
DR   RefSeq; NP_775566.3; NM_173390.3.
DR   UniGene; Mm.297971; -.
DR   STRING; Q8CAF4; -.
DR   PhosphoSite; Q8CAF4; -.
DR   PRIDE; Q8CAF4; -.
DR   Ensembl; ENSMUST00000037341; ENSMUSP00000040799; ENSMUSG00000039835.
DR   Ensembl; ENSMUST00000100054; ENSMUSP00000097631; ENSMUSG00000039835.
DR   GeneID; 215819; -.
DR   KEGG; mmu:215819; -.
DR   CTD; 215819; -.
DR   MGI; MGI:106390; Nhsl1.
DR   eggNOG; roNOG10205; -.
DR   GeneTree; ENSGT00530000063248; -.
DR   HOVERGEN; HBG108185; -.
DR   InParanoid; Q8CAF4; -.
DR   OMA; SSEACDF; -.
DR   OrthoDB; EOG444KJF; -.
DR   NextBio; 374861; -.
DR   ArrayExpress; Q8CAF4; -.
DR   Bgee; Q8CAF4; -.
DR   Genevestigator; Q8CAF4; -.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1   1587       NHS-like protein 1.
FT                                /FTId=PRO_0000341354.
FT   COMPBIAS    884    908       Ser-rich.
FT   COMPBIAS    924   1022       Pro-rich.
FT   MOD_RES    1175   1175       Phosphoserine (By similarity).
FT   MOD_RES    1176   1176       Phosphoserine (By similarity).
FT   MOD_RES    1178   1178       Phosphoserine (By similarity).
FT   MOD_RES    1218   1218       Phosphoserine (By similarity).
FT   MOD_RES    1263   1263       Phosphoserine (By similarity).
FT   MOD_RES    1265   1265       Phosphoserine (By similarity).
FT   MOD_RES    1373   1373       Phosphoserine.
FT   MOD_RES    1375   1375       Phosphoserine.
FT   MOD_RES    1379   1379       Phosphothreonine.
FT   MOD_RES    1459   1459       Phosphoserine (By similarity).
FT   VAR_SEQ       1     68       MKKDGSSGSFGIKASPGSLSRAVSWINFSSLSRQTKRLFRS
FT                                DGELSVCGHQVEADDENWIYRTQPRKA -> MVVFINAKIK
FT                                SFFKLFKKKT (in isoform 3).
FT                                /FTId=VSP_034261.
FT   VAR_SEQ     224    224       T -> TGENFDRQASLRRSLIYTDTLVRRPKKVKRRKTISG
FT                                IPDIIQKEL (in isoform 3).
FT                                /FTId=VSP_034263.
FT   CONFLICT    125    125       Q -> R (in Ref. 3; AAH30842).
FT   CONFLICT   1555   1555       S -> G (in Ref. 3; AAH61949 and 4;
FT                                BAD90251).
SQ   SEQUENCE   1587 AA;  169419 MW;  5E63EA1AEAAE412F CRC64;
     MKKDGSSGSF GIKASPGSLS RAVSWINFSS LSRQTKRLFR SDGELSVCGH QVEADDENWI
     YRTQPRKAVS NLDEESRWTV HYTAPWHQQE NVFLPATRPP CVEDLHRQAK LNLKSVLREC
     DKLRQDGCRS SQYYSQGPTF AAGSSPCDDY QDEDTEADRK CSLSSSEEER FIGIRRPKTP
     TSGDFSDLHT QTNWTKSLPL PTPEEKTRQQ AQTVQADVVP INITASATGQ DDDGSAHSLY
     VPDHYSTLGR LDSYRSTGQC LETRDTSCQT EDVKVIPPSM RRIRAHKGVG VAAQMSHLSG
     SSGNMSVLSD SAGVVFPSRL SNDTGFHSLP RTGPRASTYS LEGRMGALGS TEDTDDTSPY
     QGGSLQGHEN FAHLGGASST GMLSRPKSQQ LRFLESPACV VSPHAAYSTS VIPNATLLSS
     SEVIVIHTAQ SAGQLDSRTP GSSSYSKIKP RDRPTPRCSV KDDHQSPRHH WNEGHLIHSR
     ALASSVPGAT TLLSLHDSEV SLNAPANREN GSQAILYHCR NNPSFPDHPS DVDGKSECSY
     SGDRGCGSSE PWEYKTSSNG RASPLKPHLA TPGCSTPTSN VSSCSLDQTS LKGDTRSLCS
     EDHDGYYTTT HEAGNLYTLS DGLGNPRHSM VNVFDGRAQR SQGDQAAHQD KILSRNISLK
     KAKKPPLPPS RTDSLRRIPK KNNQTNGQVL NESLIASLQH SLQLSLPGKG GSSPSQSPCS
     DFEEPWLPRS RSQSIVSEGS SLTSTTTPNV YSLCGVTPSQ SDTSSVKSEY TDPWGYYIDY
     TSLQEDPGNP TGGCSANTEA ATGNGPVRHI QEGSRVPVPQ VPGCSVRPKI ASPEKSQRVT
     SPSSGYSSQS NTPTALTPVP VFLKSMSPAN GKGKAKPKVP ERKSSLISSM SISSSSTSLS
     SNTSTEGSGT MKKLDTTLAS ALAPPPPPLP PLPSPCLADK SPFLPPPPPL ADCSEGSPLP
     PSPMFPPPPP EALVPFCSPT DGCLSPSPTA VSPSLPRSLP PVPAPPPFLP SSEPPPAPPL
     DPKLMKENRP FFKNSSQSES SREALRRPAN KEEGCRPPMP LITTEALQMV QLRPVRKNSG
     AGAVLFSEPS AQEQRTPTAP QYHLKPSAFL KSRNSINEME SESQAASVTS SLPMPAKSQS
     QGDHDSAVER GGLPSCSDGA PGPGPSLRTT LLPDSSPSRK PPPISKKPKL FLVVPPPQRD
     FTAEPTENGS EAFPGVPSPT RAEGEAVRSQ EEKSSPASRA GSHATAPTPG SPALEPGTAG
     SLSSSIVEAN VPMVQPNTSP GPTQEESGEN SVDGERNAKS CLSQQGREAG LLEPNTAASS
     SDPVDVSKEE GSDEVLTPTK PRTTEDLFAA IHRSKRKVLG RKDSEDDHTR NHSPSPPVTP
     TSAAPNLASP KQVGSIQRSI KKSTTSSDNF KALLLKKGSR SDTSARMSAA EMLKSTDPRF
     QRSRSEPSAD SPDSPSSCSP NKNRRAQEEW AKNEGLMPRS LSFSGPRYSR SRTPPSAASS
     RYSMRNRIQS SPMTVISEGE GEPAEPADNK ARRALDATRV CSLDRLTGQE MDQASLLCSE
     EPASVDGIGR AEGNGPSEQC GGTEQKS
//
ID   IMMT_MOUSE              Reviewed;         757 AA.
AC   Q8CAQ8; Q66JS4; Q7TNE2; Q8C7V1; Q8CCI0; Q8CDA8; Q9D9F6;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Mitochondrial inner membrane protein;
DE   AltName: Full=Mitofilin;
GN   Name=Immt;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 503-757 (ISOFORM 5).
RC   STRAIN=C57BL/6J; TISSUE=Testis, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 353-365; 395-409; 581-599 AND 672-688, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 475-757.
RC   STRAIN=Czech II, and FVB/N; TISSUE=Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-505, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-506, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q8CAQ8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CAQ8-2; Sequence=VSP_007003;
CC       Name=3;
CC         IsoId=Q8CAQ8-3; Sequence=VSP_007003, VSP_007004, VSP_007005;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q8CAQ8-4; Sequence=VSP_007003, VSP_013222, VSP_013223;
CC         Note=May be due to intron retention. No experimental
CC         confirmation available;
CC       Name=5;
CC         IsoId=Q8CAQ8-5; Sequence=VSP_013224;
CC         Note=No experimental confirmation available;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB24817.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAB24817.1; Type=Frameshift; Positions=754;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK006977; BAB24817.1; ALT_SEQ; mRNA.
DR   EMBL; AK030841; BAC27154.1; -; mRNA.
DR   EMBL; AK033126; BAC28163.1; -; mRNA.
DR   EMBL; AK038129; BAC29936.1; -; mRNA.
DR   EMBL; AK049189; BAC33599.1; -; mRNA.
DR   EMBL; BC055840; AAH55840.1; -; mRNA.
DR   EMBL; BC080790; AAH80790.1; -; mRNA.
DR   IPI; IPI00228150; -.
DR   IPI; IPI00381412; -.
DR   IPI; IPI00554845; -.
DR   IPI; IPI00555088; -.
DR   IPI; IPI00875638; -.
DR   RefSeq; NP_083949.2; NM_029673.2.
DR   UniGene; Mm.235123; -.
DR   ProteinModelPortal; Q8CAQ8; -.
DR   STRING; Q8CAQ8; -.
DR   PhosphoSite; Q8CAQ8; -.
DR   REPRODUCTION-2DPAGE; Q8CAQ8; -.
DR   PRIDE; Q8CAQ8; -.
DR   Ensembl; ENSMUST00000064062; ENSMUSP00000066181; ENSMUSG00000052337.
DR   Ensembl; ENSMUST00000101301; ENSMUSP00000098859; ENSMUSG00000052337.
DR   Ensembl; ENSMUST00000114151; ENSMUSP00000109788; ENSMUSG00000052337.
DR   Ensembl; ENSMUST00000114156; ENSMUSP00000109793; ENSMUSG00000052337.
DR   GeneID; 76614; -.
DR   KEGG; mmu:76614; -.
DR   UCSC; uc009che.1; mouse.
DR   UCSC; uc009chh.1; mouse.
DR   UCSC; uc009chi.1; mouse.
DR   UCSC; uc009chm.1; mouse.
DR   CTD; 76614; -.
DR   MGI; MGI:1923864; Immt.
DR   GeneTree; ENSGT00390000002313; -.
DR   HOVERGEN; HBG039233; -.
DR   InParanoid; Q8CAQ8; -.
DR   OrthoDB; EOG4WWRJ6; -.
DR   NextBio; 345458; -.
DR   ArrayExpress; Q8CAQ8; -.
DR   Bgee; Q8CAQ8; -.
DR   CleanEx; MM_IMMT; -.
DR   Genevestigator; Q8CAQ8; -.
DR   GermOnline; ENSMUSG00000052337; Mus musculus.
DR   GO; GO:0031305; C:integral to mitochondrial inner membrane; IEA:InterPro.
DR   InterPro; IPR019133; Mt-IM_prot_Mitofilin.
DR   Pfam; PF09731; Mitofilin; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Direct protein sequencing;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    757       Mitochondrial inner membrane protein.
FT                                /FTId=PRO_0000084185.
FT   TOPO_DOM      1     40       Mitochondrial matrix (Potential).
FT   TRANSMEM     41     63       Helical; (Potential).
FT   TOPO_DOM     64    757       Mitochondrial intermembrane (Potential).
FT   MOD_RES     210    210       N6-acetyllysine (By similarity).
FT   MOD_RES     221    221       N6-acetyllysine (By similarity).
FT   MOD_RES     450    450       N6-acetyllysine (By similarity).
FT   MOD_RES     505    505       N6-acetyllysine.
FT   MOD_RES     506    506       Phosphotyrosine.
FT   VAR_SEQ     141    151       Missing (in isoform 2, isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_007003.
FT   VAR_SEQ     186    218       EEAFSSSVRERPPEEVAARLAQQEKQEQVEMES -> A
FT                                (in isoform 3).
FT                                /FTId=VSP_007004.
FT   VAR_SEQ     186    194       EEAFSSSVR -> GSLIIYIML (in isoform 4).
FT                                /FTId=VSP_013222.
FT   VAR_SEQ     195    757       Missing (in isoform 4).
FT                                /FTId=VSP_013223.
FT   VAR_SEQ     387    392       SISDLA -> T (in isoform 3).
FT                                /FTId=VSP_007005.
FT   VAR_SEQ     757    757       E -> FWIKAVFKSQMSNPTSFKVTRLNSVQKNRSSPLI
FT                                (in isoform 5).
FT                                /FTId=VSP_013224.
FT   CONFLICT    532    532       D -> E (in Ref. 1; BAB24817).
FT   CONFLICT    658    658       F -> L (in Ref. 1; BAB24817).
SQ   SEQUENCE   757 AA;  83900 MW;  5EB37BCA054BD7A6 CRC64;
     MLRACQLSGV TVAAQSCLCG KFVLRPLRPC RRYSTSSSSG LTAGKIAGAG LLFVGGGIGG
     TILYAKWDSH FRESVEKTIP YSDKLFGMVL GSAPYTVPLP KKPVQSGPLK ISSVSEVMKD
     SKLPVAQSQK TKGDTPASAA STGAAQIISA AGDTLSVPAP AVQHEDTIKT ECPNTNEGKS
     TSETTEEAFS SSVRERPPEE VAARLAQQEK QEQVEMESLA KSLEDALNRT SSVTLQTITA
     QNAAVQAVKA HSNILKTAMD NSEIAGEKKS AQWRTVEGAL KERRKAVDEA ADALLKAKEE
     LEKMKTIIED AKKREIAGAT PHITAAEGRL HNMIVDLDNV VKKVQAAQSE AKVVSQYHEL
     VVQARDDFRK ELDSITPDIT PGWKGMSISD LAGKLSTDDL NSLIAHAHRR IDQLNRELAQ
     QKATEKQHIE LALEKHKLEE KRTFDSAVAK ALEHHRSEIQ AEQDRKVEEV RDAMENEMRT
     QLRRQAAAHT DHLRDVLKVQ EQELKYEFEQ GLSEKLSEQE LEFRRRSQEQ MDSFTLDINT
     AYARLRGIEQ AVQSHAVAEE EARKAHQLWL SVEALKYSMK TSSAEMPTIP LGSAVEAIRV
     NCSDNEFTQA LTAAIPPESL TRGVYSEETL RARFYAVQKL ARRVAMIDET RNSLYQYFLS
     YLQSLLLFPP KQLKPPAELY PEDINTFKLL SYASYCIEHG DLELAAKFVN QLKGESRRVA
     QDWLKEARMT LETKQIVEIL TAYASAVGIG TTQVQQE
//
ID   PHTF2_MOUSE             Reviewed;         747 AA.
AC   Q8CB19; Q7TPX6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   08-MAR-2011, entry version 47.
DE   RecName: Full=Putative homeodomain transcription factor 2;
GN   Name=Phtf2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in transcription regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- SIMILARITY: Contains 1 basic helix-loop-helix (bHLH) domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK037021; BAC29673.1; -; mRNA.
DR   EMBL; BC052841; AAH52841.1; -; mRNA.
DR   IPI; IPI00228168; -.
DR   RefSeq; NP_766580.3; NM_172992.3.
DR   UniGene; Mm.86410; -.
DR   STRING; Q8CB19; -.
DR   PRIDE; Q8CB19; -.
DR   Ensembl; ENSMUST00000118174; ENSMUSP00000114087; ENSMUSG00000039987.
DR   GeneID; 68770; -.
DR   KEGG; mmu:68770; -.
DR   UCSC; uc008wnz.1; mouse.
DR   CTD; 68770; -.
DR   MGI; MGI:1916020; Phtf2.
DR   GeneTree; ENSGT00390000011648; -.
DR   HOGENOM; HBG443697; -.
DR   HOVERGEN; HBG061164; -.
DR   InParanoid; Q8CB19; -.
DR   OrthoDB; EOG4001HW; -.
DR   ArrayExpress; Q8CB19; -.
DR   Bgee; Q8CB19; -.
DR   CleanEx; MM_PHTF2; -.
DR   Genevestigator; Q8CB19; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR021980; TF_homeodomain_male.
DR   Pfam; PF12129; Phtf-FEM1B_bdg; 1.
DR   PROSITE; PS50888; HLH; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   DNA-binding; Nucleus; Transcription; Transcription regulation.
FT   CHAIN         1    747       Putative homeodomain transcription factor
FT                                2.
FT                                /FTId=PRO_0000318510.
FT   DOMAIN      702    735       Helix-loop-helix motif.
FT   DNA_BIND    683    701       Basic motif.
FT   CONFLICT    197    197       Y -> H (in Ref. 1; BAC29673).
FT   CONFLICT    260    260       L -> P (in Ref. 1; BAC29673).
FT   CONFLICT    366    366       G -> D (in Ref. 1; BAC29673).
FT   CONFLICT    628    628       C -> Y (in Ref. 1; BAC29673).
SQ   SEQUENCE   747 AA;  84105 MW;  0994F8C14D29A889 CRC64;
     MASRVTDAIV WYQKKIGAYD QQIWEKSVEQ REIKGLRNKP KKTAHVKPDL IDVDLVRGSA
     FAKAKPESPW TSLTRKGIVR VVFFPFFSRW WLQVTSRVIF SWLLVLYLLQ VAAIVLFCSA
     PSPHSIPLTE VIGPIWLMLL LGTVHCQIVS TRTPKPPLGT GGKRRRKLRK AAHLEVHREG
     DGSSTTDNTQ EGAVQSYGAG APYSVGTVFR DLWLAAFFLS GSKKAKNSID KSTETDNGYV
     SLDGKRTVKS SEDGAQYHEL QCETVGPEDA AWATRTPRSV PAKDTQRKIT NVSDEVSSEE
     GPETGYPLRG HVDRTSESGL RNRKPHHYKK HYANEDAPKS GTSCSSRCSS SRQDSESTRP
     ESETEGVLWE DLLHCAECRS SCTSETDVGN PQINPCGKKE YRDDPFHQSH LPWLHSSHPG
     LEKISAIVWE GNDCKKADMS VLEISGMIMN RVNNHVPGIG YQVFGNAISL ILGLTPFVFR
     LSQATDLEQL TAHSASELYV IAFGSNEDVM VLSMVLISFV VRVSLVWIFF FLLCVAERTY
     KQRLLFAKLF GHLTSARRAR KSEVPHFRLK KVQNIKMWLS LRSYLKRRGP QRSVDVIVSS
     AFLLTISVVF ICCAQLLHVH EIFLDCHCNW ELVIWCISLT LFLLRFVTLG SETSKKYSNT
     SILLTEQINL YLKMEKKPNK KEELTLVNNV LKLATKLLKE LDSPFRLYGL TMNPLLYNIT
     QVVILSAVSG VISDLLGFNL KLWKIKS
//
ID   GRAM4_MOUSE             Reviewed;         633 AA.
AC   Q8CB44; B2RTC1; Q6ZQ52; Q8VDL6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=GRAM domain-containing protein 4;
DE   AltName: Full=Death-inducing protein;
GN   Name=Gramd4; Synonyms=Dip, Kiaa0767;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 57-633.
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Plays a role as a mediator of E2F1-induced apoptosis in
CC       the absence of p53/TP53 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane
CC       protein (By similarity). Note=Colocalizes with COX4I1 (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 GRAM domain.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-52 is the initiator.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH21523.1; Type=Erroneous initiation;
CC       Sequence=BAC98019.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK036832; BAC29597.1; -; mRNA.
DR   EMBL; AK129209; BAC98019.1; ALT_SEQ; Transcribed_RNA.
DR   EMBL; BC021523; AAH21523.1; ALT_INIT; mRNA.
DR   EMBL; BC139228; AAI39229.1; -; mRNA.
DR   EMBL; BC139229; AAI39230.1; -; mRNA.
DR   IPI; IPI00228202; -.
DR   RefSeq; NP_766199.1; NM_172611.3.
DR   UniGene; Mm.24442; -.
DR   ProteinModelPortal; Q8CB44; -.
DR   PhosphoSite; Q8CB44; -.
DR   PRIDE; Q8CB44; -.
DR   Ensembl; ENSMUST00000088931; ENSMUSP00000086321; ENSMUSG00000035900.
DR   GeneID; 223752; -.
DR   KEGG; mmu:223752; -.
DR   UCSC; uc007xdv.1; mouse.
DR   CTD; 223752; -.
DR   MGI; MGI:2676308; Gramd4.
DR   GeneTree; ENSGT00390000010968; -.
DR   HOVERGEN; HBG098114; -.
DR   OrthoDB; EOG4P5K8T; -.
DR   NextBio; 376870; -.
DR   ArrayExpress; Q8CB44; -.
DR   Bgee; Q8CB44; -.
DR   Genevestigator; Q8CB44; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   InterPro; IPR004182; GRAM.
DR   InterPro; IPR013583; PRibTrfase_C.
DR   Pfam; PF02893; GRAM; 1.
DR   Pfam; PF08372; PRT_C; 1.
DR   SMART; SM00568; GRAM; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Coiled coil; Membrane; Mitochondrion; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    633       GRAM domain-containing protein 4.
FT                                /FTId=PRO_0000328743.
FT   TRANSMEM    295    315       Helical; (Potential).
FT   TRANSMEM    389    409       Helical; (Potential).
FT   TRANSMEM    411    431       Helical; (Potential).
FT   DOMAIN      500    578       GRAM.
FT   COILED      134    190       Potential.
FT   MOD_RES      75     75       Phosphoserine (By similarity).
FT   MOD_RES      79     79       Phosphoserine (By similarity).
FT   MOD_RES     214    214       Phosphoserine (By similarity).
FT   MOD_RES     219    219       Phosphoserine (By similarity).
SQ   SEQUENCE   633 AA;  72264 MW;  C961FEE9749B3AD3 CRC64;
     MGIASHSAFR ERESSPTGAS LDASPRPWDK GLSGREPPRH VQVRPRSAVL NMLRRLDRIR
     FRGHKREDLL DLAESPNASD TECGDEIPLK TPRPSPRDSE ELRDPAGPGT LIMAAGVQDF
     NRTEFDRLNE IKGHLEIALL EKHFLQEELR KLREETNSEM LRQELDRERQ RRIELEQKMQ
     EVLKARSEEQ PAQPQQPPKG QSQASNGTGT ERRSQGLASR VQKWFYERFG EYIEDFRFQP
     EENTVETEEP LSARRLTENM RRLKRGAKPV TNFVKNLSAL SDWYSIYTSA IAFTVYMNAV
     WHGWAIPMFL FLAILRLSLN YLIARGWRIQ WSIVPEVSEA VEPAKEDLTV SEKFQLVLDV
     AQKAQNLFGK MADILEKIKN LFMWVQPETT QKLYVALWAA FLASCFFPYR LVGLAVGLYA
     GIKFFLIDFI FKRCPRLRAK YDTPYIIWRS LPTDPQLKER AGATVSRRLQ TASSRSYVSS
     APAGLSKDED AGRFHSTKKG NFHEIFNLTE NERPLAVCEN GWRCCLINRD RKMPTDYIRN
     GVLYVTENYL CFESSKSGSS KRNKVIKLMD ITDIQKYKVL SVLPGSGMGI AVSTPSTQKP
     LVFGAMVHRD EAFETIFSQY VKITSAAASG GDS
//
ID   CNST_MOUSE              Reviewed;         711 AA.
AC   Q8CBC4; Q8BFS5; Q8K053;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Consortin;
GN   Name=Cnst;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Amnion, Aorta, Cerebellum, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION OF ISOFORM 3, INTERACTION WITH GGA1; GGA2; GJA1; GJB1;
RP   GJB2; GJB3; GJB6 AND GJC1, AND MUTAGENESIS OF 558-562.
RX   PubMed=19864490; DOI=10.1093/hmg/ddp490;
RA   del Castillo F.J., Cohen-Salmon M., Charollais A., Caille D.,
RA   Lampe P.D., Chavrier P., Meda P., Petit C.;
RT   "Consortin, a trans-Golgi network cargo receptor for the plasma
RT   membrane targeting and recycling of connexins.";
RL   Hum. Mol. Genet. 19:262-275(2010).
CC   -!- FUNCTION: Required for targeting of connexins to the plasma
CC       membrane (By similarity).
CC   -!- SUBUNIT: Interacts with connexins GJA1/CX43, GJB1/CX32, GJB2/CX26,
CC       GJB3/CX31, GJB6/CX30 and GJC1/CX45. Also interacts with GGA1 and
CC       GGA2. Does not interact with PANX1.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein
CC       (By similarity). Golgi apparatus, trans-Golgi network membrane;
CC       Single-pass membrane protein (By similarity). Cytoplasmic vesicle,
CC       secretory vesicle (By similarity). Note=Located predominantly in
CC       the trans-Golgi network. Probably trafficks between the trans-
CC       Golgi network and the cell membrane via the secretory pathway (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8CBC4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CBC4-2; Sequence=VSP_025821, VSP_025822;
CC       Name=3;
CC         IsoId=Q8CBC4-3; Sequence=VSP_038657;
CC   -!- SIMILARITY: Belongs to the CNST family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK036332; BAC29388.1; -; mRNA.
DR   EMBL; AK040666; BAC30660.1; -; mRNA.
DR   EMBL; AK040899; BAC30736.1; -; mRNA.
DR   EMBL; AK146681; BAE27356.1; -; mRNA.
DR   EMBL; BC034107; AAH34107.1; -; mRNA.
DR   EMBL; BC054802; AAH54802.1; -; mRNA.
DR   IPI; IPI00228289; -.
DR   IPI; IPI00475239; -.
DR   IPI; IPI00955089; -.
DR   RefSeq; NP_666217.2; NM_146105.3.
DR   UniGene; Mm.87662; -.
DR   ProteinModelPortal; Q8CBC4; -.
DR   IntAct; Q8CBC4; 26.
DR   PRIDE; Q8CBC4; -.
DR   Ensembl; ENSMUST00000040706; ENSMUSP00000048205; ENSMUSG00000038949.
DR   GeneID; 226744; -.
DR   KEGG; mmu:226744; -.
DR   UCSC; uc007dvo.1; mouse.
DR   CTD; 226744; -.
DR   MGI; MGI:2445141; Cnst.
DR   eggNOG; roNOG04588; -.
DR   GeneTree; ENSGT00390000005861; -.
DR   HOGENOM; HBG279672; -.
DR   HOVERGEN; HBG098332; -.
DR   InParanoid; Q8CBC4; -.
DR   OMA; SYSLQEN; -.
DR   OrthoDB; EOG4B8JCH; -.
DR   PhylomeDB; Q8CBC4; -.
DR   NextBio; 378309; -.
DR   ArrayExpress; Q8CBC4; -.
DR   Bgee; Q8CBC4; -.
DR   CleanEx; MM_9630058J23RIK; -.
DR   Genevestigator; Q8CBC4; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR   GO; GO:0030133; C:transport vesicle; ISS:UniProtKB.
DR   GO; GO:0071253; F:connexin binding; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0042998; P:positive regulation of Golgi to plasma membrane protein transport; ISS:UniProtKB.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasmic vesicle;
KW   Glycoprotein; Golgi apparatus; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    711       Consortin.
FT                                /FTId=PRO_0000288907.
FT   TRANSMEM    651    671       Helical; (Potential).
FT   CARBOHYD    137    137       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    218    218       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1    289       Missing (in isoform 3).
FT                                /FTId=VSP_038657.
FT   VAR_SEQ     128    197       DAVPVMQTQNATSQAAGEEEAAGVNANDPPKAPALQPLFSL
FT                                IRGEVAQMDSRALPLFLHQVAETYFQEED -> EAFRLSLL
FT                                SFNKNKHFFWCCSAAAPVAPLCGSCIPFVPAVTVYREITTC
FT                                LVCFLYRPHHGVLTLPSLRHGGFAL (in isoform 2).
FT                                /FTId=VSP_025821.
FT   VAR_SEQ     198    711       Missing (in isoform 2).
FT                                /FTId=VSP_025822.
FT   MUTAGEN     558    562       DSDLL->NSDAA: Does not affect binding to
FT                                connexins but results in their
FT                                intracellular accumulation.
SQ   SEQUENCE   711 AA;  76866 MW;  B117F1FA8648E8EC CRC64;
     MDDSDPPTYS LQIEPQDGCH PGDSVERRVT RLPSVSDENE NQLAGDGPAG LTTSEGAMGR
     ATVSEQDSLN NNESFPSSCE AAPTENAENT PSEGPKDDPP SLGQDQKLPA KRSPRAKKSS
     PKSAPPGDAV PVMQTQNATS QAAGEEEAAG VNANDPPKAP ALQPLFSLIR GEVAQMDSRA
     LPLFLHQVAE TYFQEEDYEK AMKFIQLERL YHEQLLANLS AIQEQWETKW KAVQPRTVTP
     LRNSEKGFNG EDFEQLAKIC TTHQDPLLSK LKTAPVEPSP ERKSLARAIM SEEAVGTEAA
     AKEPEIETCP STDPSGDRHE EEPQESSPGC HQMEWQTASP ELPGTAGKDH TEELPSSTNA
     TLDLHTQSLE TAGSRSGPAA ASNACKDSSC VPAPPTEDHC GVARDPKVAP PSESVAEQKL
     STGDDGALPG LISEGKYSQA HRKELCLPLQ DAFEALPRDQ PHSSEVAEPR QPDVTASDGK
     SAQSQAGLET GPESALCGDR KACDVSTLCL EVCMAPEERR DSEDRVSKET EDYLHSLLER
     CLKDAEDSLS YEDIQDDDSD LLQDLSPEEA SYSLQEDLPP DESTLSLDDL AKKIEIAEAI
     PAEGLVSILK KRNDTVGSHP AQMQQKPAKR RVRFQEIDDN LEQDEVGGGS CILLILLCIA
     TVFLSVGGTA LYCTLGNIES PVCTDFADNV DFYYTKLLQG VAGLKHWVYL S
//
ID   WDR37_MOUSE             Reviewed;         496 AA.
AC   Q8CBE3; Q80Y96; Q8CCL2;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=WD repeat-containing protein 37;
GN   Name=Wdr37; Synonyms=Kiaa0982;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 7 WD repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98064.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK129254; BAC98064.1; ALT_INIT; mRNA.
DR   EMBL; AK032582; BAC27934.1; -; mRNA.
DR   EMBL; AK036203; BAC29346.1; -; mRNA.
DR   EMBL; BC046236; AAH46236.1; -; mRNA.
DR   IPI; IPI00387421; -.
DR   RefSeq; NP_001034477.1; NM_001039388.1.
DR   RefSeq; NP_766033.1; NM_172445.2.
DR   UniGene; Mm.284654; -.
DR   ProteinModelPortal; Q8CBE3; -.
DR   SMR; Q8CBE3; 109-493.
DR   PhosphoSite; Q8CBE3; -.
DR   PRIDE; Q8CBE3; -.
DR   Ensembl; ENSMUST00000021572; ENSMUSP00000021572; ENSMUSG00000021147.
DR   Ensembl; ENSMUST00000054251; ENSMUSP00000062174; ENSMUSG00000021147.
DR   GeneID; 207615; -.
DR   KEGG; mmu:207615; -.
DR   UCSC; uc007pki.1; mouse.
DR   CTD; 207615; -.
DR   MGI; MGI:1920393; Wdr37.
DR   GeneTree; ENSGT00600000084420; -.
DR   HOGENOM; HBG315433; -.
DR   HOVERGEN; HBG057072; -.
DR   InParanoid; Q8CBE3; -.
DR   OMA; SIETGRC; -.
DR   OrthoDB; EOG4DZ1V5; -.
DR   PhylomeDB; Q8CBE3; -.
DR   NextBio; 371979; -.
DR   ArrayExpress; Q8CBE3; -.
DR   Bgee; Q8CBE3; -.
DR   CleanEx; MM_WDR37; -.
DR   Genevestigator; Q8CBE3; -.
DR   GermOnline; ENSMUSG00000021147; Mus musculus.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 6.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Repeat; WD repeat.
FT   CHAIN         1    496       WD repeat-containing protein 37.
FT                                /FTId=PRO_0000051388.
FT   REPEAT      154    194       WD 1.
FT   REPEAT      197    236       WD 2.
FT   REPEAT      281    320       WD 3.
FT   REPEAT      323    362       WD 4.
FT   REPEAT      367    405       WD 5.
FT   REPEAT      408    447       WD 6.
FT   REPEAT      454    495       WD 7.
FT   CONFLICT     69     69       F -> L (in Ref. 2; BAC27934).
FT   CONFLICT    139    139       T -> I (in Ref. 3; AAH46236).
FT   CONFLICT    224    224       H -> N (in Ref. 2; BAC27934).
SQ   SEQUENCE   496 AA;  55046 MW;  D647D239E5F6EA08 CRC64;
     MPTESGSCST ARQAKQKRKS HSLSIRRTNS SEQERTGLPR EMLEGQDSKL PSSVRSTLLE
     LFGQIEREFE NLYIENLELR REIDTLNERL AGEGQAIDGA ELSKGQLKTK ASHSTSQLSQ
     KLKTTYKAST SKIVSSFKTT TSRAICQLVK EYIGHRDGIW DVSVTRTQPI VLGTASADHT
     ALLWSIETGK CLVKYAGHVG SVNSIKFHPS EQLALTASGD QTAHIWRYVV QLPTPQPVAD
     TSQQISGEDE IECSDKDEPD IDGDVSSDCP TVRVPLTSLK SHQGVVIAAD WLVGGKQVVT
     ASWDRTANLY DVETSELVHS LTGHDQELTH CCTHPTQRLV VTSSRDTTFR LWDFRDPSIH
     SVNVFQGHTD TVTSAVFTVG DNVVSGSDDR TVKVWDLKNM RSPIATIRTD SAINRINVCV
     GQKIIALPHD NRQVRLFDMS GVRLARLPRS SRQGHRRMVC CSAWSEDHPI CNLFTCGFDR
     QAIGWNINIP ALLQEK
//
ID   EPHB1_MOUSE             Reviewed;         984 AA.
AC   Q8CBF3; B1B1C2; Q3UY27; Q6PG23; Q8CBE2;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Ephrin type-B receptor 1;
DE            EC=2.7.10.1;
DE   Flags: Precursor;
GN   Name=Ephb1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Receptor for members of the ephrin-B family. Binds to
CC       ephrin-B1, -B2 and -B3. May be involved in cell-cell interactions
CC       in the nervous system (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBUNIT: The ligand-activated form interacts with GRB2, GRB10 and
CC       NCK through their respective SH2 domains. The GRB10 SH2 domain
CC       binds EPHB1 through Tyr-928, while GRB2 binds residues within the
CC       catalytic domain. The NCK SH2 domain binds EPHB1 through Tyr-594.
CC       Interacts with EPHB6 and PRKCABP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CBF3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CBF3-2; Sequence=VSP_021595;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Ephrin receptor subfamily.
CC   -!- SIMILARITY: Contains 2 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
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DR   EMBL; AK036148; BAC29320.1; -; mRNA.
DR   EMBL; AK036211; BAC29348.1; -; mRNA.
DR   EMBL; AK135018; BAE22386.1; -; mRNA.
DR   EMBL; CT025594; CAM23741.1; -; Genomic_DNA.
DR   EMBL; AC109247; CAM23741.1; JOINED; Genomic_DNA.
DR   EMBL; AC132684; CAM23741.1; JOINED; Genomic_DNA.
DR   EMBL; AC156635; CAM23741.1; JOINED; Genomic_DNA.
DR   EMBL; BC057301; AAH57301.1; -; mRNA.
DR   IPI; IPI00228309; -.
DR   IPI; IPI00808241; -.
DR   RefSeq; NP_001161768.1; NM_001168296.1.
DR   RefSeq; NP_775623.3; NM_173447.3.
DR   UniGene; Mm.22897; -.
DR   HSSP; P54763; 1JPA.
DR   ProteinModelPortal; Q8CBF3; -.
DR   SMR; Q8CBF3; 18-528, 612-892, 900-984.
DR   STRING; Q8CBF3; -.
DR   PhosphoSite; Q8CBF3; -.
DR   PRIDE; Q8CBF3; -.
DR   Ensembl; ENSMUST00000035129; ENSMUSP00000035129; ENSMUSG00000032537.
DR   Ensembl; ENSMUST00000085169; ENSMUSP00000082261; ENSMUSG00000032537.
DR   GeneID; 270190; -.
DR   KEGG; mmu:270190; -.
DR   UCSC; uc009rfn.1; mouse.
DR   CTD; 270190; -.
DR   MGI; MGI:1096337; Ephb1.
DR   eggNOG; roNOG09683; -.
DR   GeneTree; ENSGT00570000078802; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG062180; -.
DR   InParanoid; Q8CBF3; -.
DR   OMA; NSVACKA; -.
DR   OrthoDB; EOG4W9J35; -.
DR   PhylomeDB; Q8CBF3; -.
DR   BRENDA; 2.7.10.1; 244.
DR   NextBio; 393293; -.
DR   ArrayExpress; Q8CBF3; -.
DR   Bgee; Q8CBF3; -.
DR   CleanEx; MM_EPHB1; -.
DR   Genevestigator; Q8CBF3; -.
DR   GermOnline; ENSMUSG00000032537; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:MGI.
DR   GO; GO:0045121; C:membrane raft; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008046; F:axon guidance receptor activity; IDA:MGI.
DR   GO; GO:0005005; F:transmembrane-ephrin receptor activity; TAS:MGI.
DR   GO; GO:0048593; P:camera-type eye morphogenesis; IMP:MGI.
DR   GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IDA:MGI.
DR   GO; GO:0021631; P:optic nerve morphogenesis; IMP:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0031290; P:retinal ganglion cell axon guidance; IDA:MGI.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR   InterPro; IPR001090; Ephrin_rcpt_lig-bd.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR009030; Growth_fac_rcpt.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   InterPro; IPR016257; Tyr_prot_kinase_ephrin_rcpt.
DR   InterPro; IPR001426; Tyr_prot_kinase_rcpt_V_CS.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF01404; Ephrin_lbd; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00615; EPH_lbd; 1.
DR   SMART; SM00060; FN3; 2.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF49265; FN_III-like; 2.
DR   SUPFAM; SSF49785; Gal_bind_like; 1.
DR   SUPFAM; SSF57184; Grow_fac_recept; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS01186; EGF_2; UNKNOWN_1.
DR   PROSITE; PS50853; FN3; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
DR   PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Glycoprotein; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Receptor; Repeat; Signal;
KW   Transferase; Transmembrane; Transmembrane helix;
KW   Tyrosine-protein kinase.
FT   SIGNAL        1     17       Potential.
FT   CHAIN        18    984       Ephrin type-B receptor 1.
FT                                /FTId=PRO_0000260317.
FT   TOPO_DOM     18    540       Extracellular (Potential).
FT   TRANSMEM    541    563       Helical; (Potential).
FT   TOPO_DOM    564    984       Cytoplasmic (Potential).
FT   DOMAIN      323    424       Fibronectin type-III 1.
FT   DOMAIN      430    525       Fibronectin type-III 2.
FT   DOMAIN      619    882       Protein kinase.
FT   DOMAIN      911    975       SAM.
FT   NP_BIND     625    633       ATP (By similarity).
FT   MOTIF       982    984       PDZ-binding (Potential).
FT   COMPBIAS    183    319       Cys-rich.
FT   ACT_SITE    744    744       Proton acceptor (By similarity).
FT   BINDING     651    651       ATP (By similarity).
FT   MOD_RES     928    928       Phosphotyrosine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     968    968       Phosphoserine (By similarity).
FT   CARBOHYD    334    334       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    426    426       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    480    480       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     588    628       Missing (in isoform 2).
FT                                /FTId=VSP_021595.
FT   CONFLICT     72     72       L -> Q (in Ref. 1; BAE22386).
FT   CONFLICT    187    187       L -> P (in Ref. 1; BAE22386).
FT   CONFLICT    194    194       K -> I (in Ref. 3; AAH57301).
FT   CONFLICT    641    641       P -> Q (in Ref. 1; BAC29348).
FT   CONFLICT    678    678       P -> R (in Ref. 3; AAH57301).
SQ   SEQUENCE   984 AA;  109881 MW;  E967019C82AA400A CRC64;
     MALDCLLLFL LASAVAAMEE TLMDTRTATA ELGWTANPAS GWEEVSGYDE NLNTIRTYQV
     CNVFEPNQNN WLLTTFINRR GAHRIYTEMR FTVRDCSSLP NVPGSCKETF NLYYYETDSV
     IATKKSAFWS EAPYLKVDTI AADESFSQVD FGGRLMKVNT EVRSFGPLTR NGFYLAFQDY
     GACMSLLSVR VFFKKCPSIV QNFAVFPETM TGAESTSLVI ARGTCIPNAE EVDVPIKLYC
     NGDGEWMVPI GRCTCKPGYE PENSVACKAC PAGTFKASQE AEGCSHCPSN SRSPSEASPI
     CTCRTGYYRA DFDPPEVACT SVPSGPRNVI SIVNETSIIL EWHPPRETGG RDDVTYNIIC
     KKCRADRRSC SRCDDNVEFV PRQLGLTECR VSISSLWAHT PYTFDIQAIN GVSSKSPFPP
     QHVSVNITTN QAAPSTVPIM HQVSATMRSI TLSWPQPEQP NGIILDYEIR YYEKEHNEFN
     SSMARSQTNT ARIDGLRPGM VYVVQVRART VAGYGKFSGK MCFQTLTDDD YKSELREQLP
     LIAGSAAAGV VFVVSLVAIS IVCSRKRAYS KEAAYSDKLQ HYSTGRGSPG MKIYIDPFTY
     EDPNEAVREF AKEIDVSFVK IEEVIGAGEF GEVYKGRLKL PGKREIYVAI KTLKAGYSEK
     QRRDFLSEAS IMGQFDHPNI IRLEGVVTKS RPVMIITEFM ENGALDSFLR QNDGQFTVIQ
     LVGMLRGIAA GMKYLSEMNY VHRDLAARNI LVNSNLVCKV SDFGLSRYLQ DDTSDPTYTS
     SLGGKIPVRW TAPEAIAYRK FTSASDVWSY GIVMWEVMSF GERPYWDMSN QDVINAIEQD
     YRLPPPMDCP AALHQLMLDC WQKDRNSRPR FAEIVNTLDK MIRNPASLKT VATITAVPSQ
     PLLDRSIPDF TAFTTVDDWL SAIKMVQYRD SFLTAGFTSL QLVTQMTSED LLRIGVTLAG
     HQKKILSSIH SMRVQMNQSP SVMA
//
ID   Q8CBF8_MOUSE            Unreviewed;       654 AA.
AC   Q8CBF8;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   SubName: Full=Potassium voltage-gated channel, shaker-related subfamily, member 4;
GN   Name=Kcna4; ORFNames=RP23-417K1.1-001, mCG_15708;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RA   Wood J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [11]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC109014; AAI09015.1; -; mRNA.
DR   EMBL; AK036112; BAC29309.1; -; mRNA.
DR   EMBL; BX293548; CAM23761.1; -; Genomic_DNA.
DR   EMBL; CH466519; EDL27774.1; -; Genomic_DNA.
DR   IPI; IPI00317376; -.
DR   RefSeq; NP_067250.2; NM_021275.4.
DR   UniGene; Mm.142718; -.
DR   HSSP; P15385; 1KN7.
DR   ProteinModelPortal; Q8CBF8; -.
DR   SMR; Q8CBF8; 1-75, 177-572.
DR   STRING; Q8CBF8; -.
DR   PRIDE; Q8CBF8; -.
DR   Ensembl; ENSMUST00000037012; ENSMUSP00000037958; ENSMUSG00000042604.
DR   Ensembl; ENSMUST00000111060; ENSMUSP00000106689; ENSMUSG00000042604.
DR   GeneID; 16492; -.
DR   KEGG; mmu:16492; -.
DR   NMPDR; fig|10090.3.peg.6522; -.
DR   UCSC; uc008llu.1; mouse.
DR   CTD; 16492; -.
DR   MGI; MGI:96661; Kcna4.
DR   GeneTree; ENSGT00560000076957; -.
DR   HOVERGEN; HBG052230; -.
DR   InParanoid; Q8CBF8; -.
DR   OMA; HHRQSSF; -.
DR   PhylomeDB; Q8CBF8; -.
DR   NextBio; 289795; -.
DR   ArrayExpress; Q8CBF8; -.
DR   Bgee; Q8CBF8; -.
DR   Genevestigator; Q8CBF8; -.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003972; K_chnl_volt-dep_Kv1.
DR   InterPro; IPR020467; K_chnl_volt-dep_Kv1.4.
DR   InterPro; IPR012897; K_chnl_volt-dep_Kv1.4_TID.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Gene3D; G3DSA:1.20.5.600; K_channel_TID; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF07941; K_channel_TID; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01511; KV14CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01496; SHAKERCHANEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
PE   2: Evidence at transcript level;
KW   Ion transport; Ionic channel; Membrane; Potassium; Potassium channel;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
SQ   SEQUENCE   654 AA;  73470 MW;  9322A3DC9CBA2AC4 CRC64;
     MEVAMVSAES SGCNSHMPYG YAAQARARER ERLAHSRAAA AAAVAAATAA VEGTGGSGGG
     PHHHHQTRGA YSSHDPQGSR GSRRRRRQRT EKKKLHHRQS SFPHCSDLMP SGSEEKILRE
     LSEEEEDEEE EEEEEEEGRF YYSEEDHGDG CSYTDLLPQD DGGGGGYSSV RYSDCCERVV
     INVSGLRFET QMKTLAQFPE TLLGDPEKRT QYFDPLRNEY FFDRNRPSFD AILYYYQSGG
     RLKRPVNVPF DIFTEEVKFY QLGEEALLKF REDEGFVREE EDRALPENEF KKQIWLLFEY
     PESSSPARGI AIVSVLVILI SIVIFCLETL PEFRDDRDLI MALSAGGHSR LLNDTSAPHL
     ENSGHTIFND PFFIVETVCI VWFSFEFVVR CFACPSQALF FKNIMNIIDI VSILPYFITL
     GTDLAQQQGG GNGQQQQAMS FAILRIIRLV RVFRIFKLSR HSKGLQILGH TLRASMRELG
     LLIFFLFIGV ILFSSAVYFA EADEPTTHFQ SIPDAFWWAV VTMTTVGYGD MKPITVGGKI
     VGSLCAIAGV LTIALPVPVI VSNFNYFYHR ETENEEQTQL TQNAVSCPYL PSNLLKKFRS
     STSSSLGDKS EYLEMEEGVK ESLCGKEEKC QGKGDESETD KNNCSNAKAV ETDV
//
ID   MARHB_MOUSE             Reviewed;         400 AA.
AC   Q8CBH7; B9EIG0;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=E3 ubiquitin-protein ligase MARCH11;
DE            EC=6.3.2.-;
DE   AltName: Full=Membrane-associated RING finger protein 11;
DE   AltName: Full=Membrane-associated RING-CH protein XI;
DE            Short=MARCH-XI;
GN   Name=March11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that mediates
CC       polyubiquitination of CD4. E3 ubiquitin ligases accept ubiquitin
CC       from an E2 ubiquitin-conjugating enzyme in the form of a thioester
CC       and then directly transfer the ubiquitin to targeted substrates.
CC       May play a role in ubuquitin-dependent protein sorting in
CC       develomenting spermatids (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts (YXXL motif) with AP1M1. Interacts (via PDZ-
CC       binding motif) with LIN7A. Interacts with unidentified fucose
CC       glycoproteins (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CBH7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CBH7-2; Sequence=VSP_034148, VSP_034149;
CC   -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3
CC       ligase activity (By similarity).
CC   -!- SIMILARITY: Contains 1 RING-CH-type zinc finger.
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DR   EMBL; AK035990; BAC29270.1; -; mRNA.
DR   EMBL; AC102845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC139422; AAI39423.1; -; mRNA.
DR   EMBL; BC139423; AAI39424.1; -; mRNA.
DR   IPI; IPI00228326; -.
DR   IPI; IPI00896037; -.
DR   RefSeq; NP_808265.2; NM_177597.5.
DR   UniGene; Mm.54257; -.
DR   ProteinModelPortal; Q8CBH7; -.
DR   SMR; Q8CBH7; 160-228.
DR   PhosphoSite; Q8CBH7; -.
DR   Ensembl; ENSMUST00000049988; ENSMUSP00000050659; ENSMUSG00000022269.
DR   GeneID; 211147; -.
DR   KEGG; mmu:211147; -.
DR   UCSC; uc007vjl.1; mouse.
DR   CTD; 211147; -.
DR   MGI; MGI:3608327; March11.
DR   eggNOG; maNOG19911; -.
DR   GeneTree; ENSGT00570000078779; -.
DR   HOVERGEN; HBG052412; -.
DR   InParanoid; Q8CBH7; -.
DR   OMA; RYHVTAI; -.
DR   OrthoDB; EOG42V8GN; -.
DR   NextBio; 373152; -.
DR   ArrayExpress; Q8CBH7; -.
DR   Bgee; Q8CBH7; -.
DR   Genevestigator; Q8CBH7; -.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR011016; Znf_RING-CH.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00744; RINGv; 1.
DR   PROSITE; PS51292; ZF_RING_CH; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasmic vesicle; Ligase; Membrane;
KW   Metal-binding; Transmembrane; Transmembrane helix;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    400       E3 ubiquitin-protein ligase MARCH11.
FT                                /FTId=PRO_0000339345.
FT   TRANSMEM    243    263       Helical; (Potential).
FT   TRANSMEM    276    296       Helical; (Potential).
FT   ZN_FING     160    220       RING-CH-type.
FT   MOTIF       369    372       YXXL motif.
FT   MOTIF       397    400       PDZ-binding.
FT   COMPBIAS     19     83       Pro-rich.
FT   COMPBIAS    143    149       Poly-Ser.
FT   VAR_SEQ     230    252       WQSISITLVEKVQMIAVILGSLF -> VDTMFTLPGIILLT
FT                                RVHLNFVLA (in isoform 2).
FT                                /FTId=VSP_034148.
FT   VAR_SEQ     253    400       Missing (in isoform 2).
FT                                /FTId=VSP_034149.
SQ   SEQUENCE   400 AA;  44223 MW;  A3C5DB5378B3CDC3 CRC64;
     MSDEGKKRSS RADSLEAEPP LPPPPPPPPP GESVLVPTSP RYRPPLPAPL ERIVGSGEPP
     VELAPRRKGA GEPLPPLPPS LLPGDQEVTA AGDSCEGPRR LPEVKLPEAA TGKGSPGEPE
     AGACREGERR GTGDQPETRS VCSSRSSSSG GGSDQRSGHQ HQHHQPICKI CFQGAEQGEL
     LNPCRCDGSV RYTHQLCLLK WISERGSWTC ELCCYRYHVT AIKMKQPCQW QSISITLVEK
     VQMIAVILGS LFLIASVTWL LWSAFSPYAV WQRKDILFQI CYGMYGFMDL VCIGLIVHEG
     AAVYRVFKRW RAVNLHWDVL NYDKATDIEE SSRGESSTSR TLWLPLSALR NRNLVHPTQL
     TSPRFQCGYV LLHLFNRMRA HEDVSEDNGS GEVVMRVTSV
//
ID   Q8CBI8_MOUSE            Unreviewed;       726 AA.
AC   Q8CBI8;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 45.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Dennd4a; Synonyms=AI115600;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
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DR   EMBL; AK035923; BAC29245.1; -; mRNA.
DR   IPI; IPI00938460; -.
DR   UniGene; Mm.222473; -.
DR   IntAct; Q8CBI8; 1.
DR   PhosphoSite; Q8CBI8; -.
DR   Ensembl; ENSMUST00000038890; ENSMUSP00000037915; ENSMUSG00000035492.
DR   UCSC; uc009qcj.1; mouse.
DR   MGI; MGI:2142979; Dennd4a.
DR   GeneTree; ENSGT00550000074509; -.
DR   HOGENOM; HBG446853; -.
DR   HOVERGEN; HBG106307; -.
DR   InParanoid; Q8CBI8; -.
DR   ArrayExpress; Q8CBI8; -.
DR   Bgee; Q8CBI8; -.
DR   Genevestigator; Q8CBI8; -.
PE   1: Evidence at protein level;
FT   NON_TER       1      1
SQ   SEQUENCE   726 AA;  81213 MW;  7DA609C80558B08E CRC64;
     KRLQRRNSSF SVKPSEKTDV VTGFDPLSLL VAETEQQQKV EEEEDEDDNK SVSTPSARRN
     LAEEIEMYMN NMSSPLTSRT PSIDLQRACD DKLTNKKSPT LVKACRRSSL PPNSPRPVRL
     TKSKSYTKSE ERPRDRLWSS PVFSPTCPFR EGSQETLAHS SPSFNLDTLL VPKLDVLRHS
     VFTAGKGVAE KASKWYSRFT MYTTSSKDQS SDRTSLSSVG AQDSESTSLT DEDVCHELEG
     ATSSQESSAA SGTKGIDVSR ASLGSSASLE GSLSKFALPG KSETASSLNT SNANIFQNYA
     MEVLISSCSR CRTCDCLVHD EEIMAGWTAD DSNLNTTCPF CGNLFLPFLN VEIRDLRRPG
     RYFLKSSSST ETMHFASRTR QSCISASASG LDTSSLSVQG NFDLNNKSKL QENPCARSIQ
     IPAHRSKTVV SKCPLFPMAR SISTCGPLDK DDPGGQKLIP TGSLPATLQG HTDSLGLEWH
     LPSPDPVTVP YLSPLVVWKE LESLLENEGD HAITVADFVD HHPIVFWNLV WYFRRLDLPS
     NLPGLILSSE HCNKYSKIPR HCMSEDSKYV LIQMLWDNMK LHQDPGQPLY ILWNAHSQNR
     TLLFETQKYP MVHLLQKGDD SFNQELLKSM VKSIKMNDVY GPMSQILETL NKCPHFKRQR
     SLYREILFLS LVALGRENID IDAFDKEYKM AYDRLTPSQV KSTHNCDRPP STGVMECRKT
     FGEPYL
//
ID   Q8CBK2_MOUSE            Unreviewed;       147 AA.
AC   Q8CBK2;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Pde4d;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
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DR   EMBL; AK035860; BAC29216.1; -; mRNA.
DR   IPI; IPI00228346; -.
DR   RefSeq; XP_003084992.1; XM_003084944.1.
DR   UniGene; Mm.434429; -.
DR   PRIDE; Q8CBK2; -.
DR   Ensembl; ENSMUST00000105096; ENSMUSP00000100723; ENSMUSG00000021699.
DR   Ensembl; ENSMUST00000120671; ENSMUSP00000112991; ENSMUSG00000021699.
DR   GeneID; 100504580; -.
DR   KEGG; mmu:100504580; -.
DR   MGI; MGI:99555; Pde4d.
DR   GeneTree; ENSGT00550000074309; -.
DR   HOVERGEN; HBG070662; -.
DR   InParanoid; Q8CBK2; -.
DR   OMA; CRAMDRA; -.
DR   NextBio; 450124; -.
DR   ArrayExpress; Q8CBK2; -.
DR   Bgee; Q8CBK2; -.
DR   Genevestigator; Q8CBK2; -.
DR   GO; GO:0006198; P:cAMP catabolic process; IMP:MGI.
DR   GO; GO:0006939; P:smooth muscle contraction; IMP:MGI.
PE   1: Evidence at protein level;
SQ   SEQUENCE   147 AA;  16396 MW;  CF651F18828751C8 CRC64;
     MEAEGSSVPA RAVSEEGNDS AGGAALKAPK HLWRHEQHHQ YPLRQPQFRL LHPHHHLPPP
     PPPSPQPQLQ PPPPPPLPPP PPPPGATRGR YASSGASRVR HRGYSDTERY LYCRAMDRTS
     YAVETGHRPG LKKSRMSWPS SFQGLRR
//
ID   CHIC1_MOUSE             Reviewed;         227 AA.
AC   Q8CBW7; O08904; Q8K3S5;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=Cysteine-rich hydrophobic domain 1 protein;
DE   AltName: Full=Brain X-linked protein;
GN   Name=Chic1; Synonyms=Brx;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=97468275; PubMed=9321471; DOI=10.1007/s003359900561;
RA   Simmler M.-C., Heard E., Rougeulle C., Cruaud C., Weissenbach J.,
RA   Avner P.;
RT   "Localization and expression analysis of a novel conserved brain
RT   expressed transcript, Brx/BRX, lying within the Xic/XIC candidate
RT   region.";
RL   Mamm. Genome 8:760-766(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=22040331; PubMed=12045143; DOI=10.1101/gr.152902;
RA   Chureau C., Prissette M., Bourdet A., Barbe V., Cattolico L.,
RA   Jones L., Eggen A., Avner P., Duret L.;
RT   "Comparative sequence analysis of the X-inactivation center region in
RT   mouse, human and bovine.";
RL   Genome Res. 12:894-908(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Cell membrane (By similarity). Cytoplasmic
CC       vesicle (By similarity). Note=Also present at a Golgi-like
CC       vesicular compartment and at scattered vesicles (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed moderately in the brain.
CC   -!- DEVELOPMENTAL STAGE: Detected in the 7, 11, 15, or 19 dpc.
CC   -!- PTM: Palmitoylated (By similarity).
CC   -!- SIMILARITY: Belongs to the CHIC family.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-8 is the initiator.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC28706.1; Type=Frameshift; Positions=6;
CC       Sequence=CAA72638.1; Type=Frameshift; Positions=204;
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DR   EMBL; Y11896; CAA72638.1; ALT_SEQ; mRNA.
DR   EMBL; AJ421479; CAD33951.1; -; Genomic_DNA.
DR   EMBL; AK034427; BAC28706.1; ALT_FRAME; mRNA.
DR   IPI; IPI00890025; -.
DR   RefSeq; NP_033897.1; NM_009767.2.
DR   UniGene; Mm.42223; -.
DR   STRING; Q8CBW7; -.
DR   PRIDE; Q8CBW7; -.
DR   Ensembl; ENSMUST00000116547; ENSMUSP00000112246; ENSMUSG00000031327.
DR   GeneID; 12212; -.
DR   KEGG; mmu:12212; -.
DR   UCSC; uc009tzl.1; mouse.
DR   CTD; 12212; -.
DR   MGI; MGI:1344694; Chic1.
DR   eggNOG; roNOG16275; -.
DR   GeneTree; ENSGT00390000003601; -.
DR   HOVERGEN; HBG050942; -.
DR   OrthoDB; EOG47SSG2; -.
DR   PhylomeDB; Q8CBW7; -.
DR   NextBio; 280609; -.
DR   ArrayExpress; Q8CBW7; -.
DR   Bgee; Q8CBW7; -.
DR   CleanEx; MM_CHIC1; -.
DR   Genevestigator; Q8CBW7; -.
DR   GermOnline; ENSMUSG00000031327; Mus musculus.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR019383; Golgin_A_7/ERF4.
DR   Pfam; PF10256; Erf4; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Coiled coil; Cytoplasmic vesicle; Lipoprotein;
KW   Membrane; Palmitate.
FT   CHAIN         1    227       Cysteine-rich hydrophobic domain 1
FT                                protein.
FT                                /FTId=PRO_0000189555.
FT   COILED       46     73       Potential.
FT   COMPBIAS     16     22       Poly-Glu.
FT   COMPBIAS     26     43       Ser-rich.
FT   COMPBIAS     47     71       Poly-Glu.
FT   COMPBIAS    150    168       Cys-rich.
FT   CONFLICT    193    193       A -> V (in Ref. 1; CAA72638).
SQ   SEQUENCE   227 AA;  25791 MW;  10C866CE9126AD97 CRC64;
     MSILLPNMAE FDTISELEEE EEAATSSSSP SSSPSSSSSS SVSGPDEDEE DEEEEEEEDE
     EEEDEEEEEE EVPPPPRVVS EEHLRRYAPD PVLVRGAGHI TVFGLSNKFD TEFPSVLTGK
     VAPEEFKTSI GRVNSCLKKA LPVNVKWLLC GCLCCCCTLG CSLWPVICLN KRTRRSIQKL
     LEWENNRLYH KLALHWKLTK RKCETSNMME YVILIEFLPK YPIFRPD
//
ID   TM63C_MOUSE             Reviewed;         802 AA.
AC   Q8CBX0;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Transmembrane protein 63C;
GN   Name=Tmem63c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the SPO75/TMEM63 family.
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DR   EMBL; AK034410; BAC28698.1; -; mRNA.
DR   EMBL; BC056936; AAH56936.1; -; mRNA.
DR   EMBL; BC057088; AAH57088.1; -; mRNA.
DR   IPI; IPI00228467; -.
DR   RefSeq; NP_766171.1; NM_172583.2.
DR   UniGene; Mm.110032; -.
DR   ProteinModelPortal; Q8CBX0; -.
DR   PRIDE; Q8CBX0; -.
DR   Ensembl; ENSMUST00000110187; ENSMUSP00000105816; ENSMUSG00000034145.
DR   GeneID; 217733; -.
DR   KEGG; mmu:217733; -.
DR   UCSC; uc007oig.1; mouse.
DR   CTD; 217733; -.
DR   MGI; MGI:2444386; Tmem63c.
DR   eggNOG; roNOG14333; -.
DR   GeneTree; ENSGT00390000011855; -.
DR   HOGENOM; HBG716737; -.
DR   HOVERGEN; HBG056752; -.
DR   InParanoid; Q8CBX0; -.
DR   OMA; ITIFICY; -.
DR   OrthoDB; EOG41G33G; -.
DR   PhylomeDB; Q8CBX0; -.
DR   NextBio; 376008; -.
DR   ArrayExpress; Q8CBX0; -.
DR   Bgee; Q8CBX0; -.
DR   CleanEx; MM_TMEM63C; -.
DR   Genevestigator; Q8CBX0; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR003864; DUF221.
DR   Pfam; PF02714; DUF221; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    802       Transmembrane protein 63C.
FT                                /FTId=PRO_0000280731.
FT   TRANSMEM     33     53       Helical; (Potential).
FT   TRANSMEM    135    155       Helical; (Potential).
FT   TRANSMEM    182    202       Helical; (Potential).
FT   TRANSMEM    409    429       Helical; (Potential).
FT   TRANSMEM    455    475       Helical; (Potential).
FT   TRANSMEM    494    514       Helical; (Potential).
FT   TRANSMEM    540    560       Helical; (Potential).
FT   TRANSMEM    604    624       Helical; (Potential).
FT   TRANSMEM    655    675       Helical; (Potential).
FT   TRANSMEM    685    705       Helical; (Potential).
FT   CARBOHYD     73     73       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   802 AA;  93011 MW;  861020EE3B05EA5A CRC64;
     MSAFPDSMDQ KFHNMTVNEC FQSRSTVLQG QPFGGIPTVL VLNIILWVFV VLLYSFLRKA
     AWDYGRLALL IHNDSLTSLI YGEQSEKSSP SEVSLEAERR DRGFSSWFFN SLTMRDRDLI
     NKCGDDARIY ITFQYHLIIF VLILCIPSLG IILPVNYIGT VLDWNSHFGR TTIVNVSTES
     KFLWLHSLFA FLYFLINLAF MGHHCLGFVP KKSLHFTRTL MITYVPTEIQ DPEIISKHFH
     EAYPGCVVTR VHFCYDVRNL IDLDDQRRHA MRGRLYYTAK AKKTGKVMIK THPCSRLCFC
     KCWTCFKEVD AEQYYSELEE QLTDEFNAEL NRVQLKRLDL IFVTFQDART VRRIYDDYKY
     IHCGRHPKQS SVTTIVKNYH WRVAHAPHPK DIIWKHLSIR RFSWWTRFIA INTFLFFLFF
     FLTTPAIIIN TIDIYNVTRP IEKLQSPIVT QFFPSVLLWA FTVTMPLLVY LSAFLEAHWT
     RSSQNLIIVH KCYIFLVFMV VILPSMGLTS LHVFLRWLFD IYYLEHATIR FQCVFLPDNG
     AFFINYVITA ALLGTGMELM RLGSLCTYCT RLFLSKSEPE RVHIRKNQAT DFQFGREYAW
     MLNVFSVVMA YSITCPIIVP FGLLYLCMKH ITDRYNMYYS YAPTKLNAQI HMAAVYQAIF
     APLLGLFWML FFSILRVGSL HSITLFSMSS LIISVVIAFS GVFLGKLRIA QRYEQPEEET
     ETVFDVEPSS TTSTPTSLLY VATVLQEPEL NLTPASSPAR HTYGTINSQP EEGEEESGLR
     GFARELDSAQ FQEGLEMEGQ SH
//
ID   SMAG1_MOUSE             Reviewed;         711 AA.
AC   Q8CBY1; A6H6C5; Q2VA55; Q3TQA5; Q3TTN7; Q3UZ00; Q9D3T3;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Protein Smaug homolog 1;
DE            Short=Smaug 1;
DE            Short=mSmaug 1;
DE   AltName: Full=Sterile alpha motif domain-containing protein 4A;
GN   Name=Samd4a; Synonyms=Samd4, Smaug1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Embryo;
RX   PubMed=16221671; DOI=10.1074/jbc.M508374200;
RA   Baez M.V., Boccaccio G.L.;
RT   "Mammalian Smaug is a translational repressor that forms cytoplasmic
RT   foci similar to stress granules.";
RL   J. Biol. Chem. 280:43131-43140(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Corpus striatum, Diencephalon, Forelimb, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC   TISSUE=Brain, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Acts as a translational repressor of SRE-containing
CC       messengers (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell projection, dendrite. Cell
CC       junction, synapse, synaptosome. Note=Colocalizes throughout the
CC       cytoplasm in granules with polyadenylated RNAs, PABPC1 and STAU1.
CC       Also frequently colocalizes in cytoplasmic stress granule-like
CC       foci with ELAVL1, TIA1 and TIAL1. Shuttles between the nucleus and
CC       the cytoplasm in a CRM1-dependent manner (By similarity). Enriched
CC       in synaptoneurosomes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8CBY1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CBY1-2; Sequence=VSP_037782;
CC       Name=3;
CC         IsoId=Q8CBY1-3; Sequence=VSP_037783;
CC       Name=4;
CC         IsoId=Q8CBY1-4; Sequence=VSP_037781;
CC   -!- TISSUE SPECIFICITY: Expressed in brain (at protein level).
CC   -!- SIMILARITY: Belongs to the SMAUG family.
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABB83932.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; DQ278487; ABB83932.1; ALT_SEQ; mRNA.
DR   EMBL; AK017081; BAB30585.1; -; mRNA.
DR   EMBL; AK034323; BAC28674.1; -; mRNA.
DR   EMBL; AK134243; BAE22061.1; -; mRNA.
DR   EMBL; AK161277; BAE36288.1; -; mRNA.
DR   EMBL; AK163751; BAE37479.1; -; mRNA.
DR   EMBL; AC131586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC159006; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466605; EDL20734.1; -; Genomic_DNA.
DR   EMBL; BC049740; AAH49740.1; -; mRNA.
DR   EMBL; BC145827; AAI45828.1; -; mRNA.
DR   EMBL; BC145829; AAI45830.1; -; mRNA.
DR   IPI; IPI00228483; -.
DR   IPI; IPI00654261; -.
DR   IPI; IPI00856457; -.
DR   IPI; IPI00856907; -.
DR   RefSeq; NP_001032298.1; NM_001037221.2.
DR   RefSeq; NP_001156905.1; NM_001163433.1.
DR   RefSeq; NP_083242.1; NM_028966.3.
DR   UniGene; Mm.214454; -.
DR   ProteinModelPortal; Q8CBY1; -.
DR   SMR; Q8CBY1; 314-545.
DR   STRING; Q8CBY1; -.
DR   PhosphoSite; Q8CBY1; -.
DR   PRIDE; Q8CBY1; -.
DR   Ensembl; ENSMUST00000100672; ENSMUSP00000098237; ENSMUSG00000021838.
DR   GeneID; 74480; -.
DR   KEGG; mmu:74480; -.
DR   UCSC; uc007tho.1; mouse.
DR   CTD; 74480; -.
DR   MGI; MGI:1921730; Samd4.
DR   GeneTree; ENSGT00390000015877; -.
DR   OMA; LMFQQPE; -.
DR   OrthoDB; EOG402WRN; -.
DR   PhylomeDB; Q8CBY1; -.
DR   NextBio; 340900; -.
DR   ArrayExpress; Q8CBY1; -.
DR   Bgee; Q8CBY1; -.
DR   CleanEx; MM_SAMD4; -.
DR   Genevestigator; Q8CBY1; -.
DR   GermOnline; ENSMUSG00000021838; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR015327; Smaug_PHAT.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Gene3D; G3DSA:1.25.40.170; Smaug_PHAT; 2.
DR   Pfam; PF00536; SAM_1; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell projection; Cytoplasm;
KW   Phosphoprotein; Repressor; Synapse; Synaptosome;
KW   Translation regulation.
FT   CHAIN         1    711       Protein Smaug homolog 1.
FT                                /FTId=PRO_0000097572.
FT   DOMAIN      323    396       SAM.
FT   MOD_RES     418    418       Phosphotyrosine (By similarity).
FT   MOD_RES     420    420       Phosphoserine (By similarity).
FT   MOD_RES     422    422       Phosphoserine (By similarity).
FT   MOD_RES     424    424       Phosphothreonine (By similarity).
FT   MOD_RES     573    573       Phosphoserine (By similarity).
FT   VAR_SEQ       1    409       Missing (in isoform 4).
FT                                /FTId=VSP_037781.
FT   VAR_SEQ       1    101       Missing (in isoform 2).
FT                                /FTId=VSP_037782.
FT   VAR_SEQ     239    327       ILSGQAHHSPLKRSVSLTPPMNVPNQPLGHGWMSHEDLRAR
FT                                GPQCLPSDHAPLSPQSSVASSGSGGSEHLEDQTTARNTFQE
FT                                EGSGMKD -> N (in isoform 3).
FT                                /FTId=VSP_037783.
FT   CONFLICT     99     99       A -> V (in Ref. 2; BAE22061).
SQ   SEQUENCE   711 AA;  78359 MW;  B4A6811D9107415B CRC64;
     MMFRDQVGVL AGWFKGWNEC EQTVALLSLL KRVSQTQARF LQLCLEHSLA DCAELHVLEG
     EANSPGIINQ WQQESKDKVI SLLLTHLPLL KPGNLDAKAE YMKLLPKILA HSIEHNQHIE
     ESRQLLSYAL IHPATSLEDR SALAMWLNHL EDRTSTSFGS QNRGRSDSVD YGQTHYYHQR
     QNSDDKLNGW QNSRDSGICI SASNWQDKSL GCENGHVPLY SSSSVPATIN TIGTGASTIL
     SGQAHHSPLK RSVSLTPPMN VPNQPLGHGW MSHEDLRARG PQCLPSDHAP LSPQSSVASS
     GSGGSEHLED QTTARNTFQE EGSGMKDVPA WLKSLRLHKY AALFSQMTYE EMMALTECQL
     EAQNVTKGAR HKIVISIQKL KERQNLLKSL ERDIIEGGSL RTPLQELHQM ILTPIKAYSS
     PSTTPEVRCR EPSLMESPSP DCKDSAAAVT SATASASAGA SGGLQPPQLS SCDGELAVAP
     LPEGDLPGQF TRVMGKVCTQ LLVSRPDEEN ISSYLQLLDK CLVHEAFTET QKKRLLSWKQ
     QVQKLFRSFP RKTLLDISGY RQQRNRGFGQ SNSLPTASSV GSGMGRRNPR QYQIASRNVP
     SARLGLLGTS GFVSSNQRHT AANPTIMKQG RQNLWFANPG GSNSMPSRTH SSVQKTRSLP
     VHTSPQNMLM FQQPEFQLPV TEPDINNRLE SLCLSMTEHA LGDGVDRTST I
//
ID   CACB2_MOUSE             Reviewed;         655 AA.
AC   Q8CC27; A2ASJ8; Q8C5J5; Q9CTQ6;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit beta-2;
DE            Short=CAB2;
DE   AltName: Full=Calcium channel voltage-dependent subunit beta 2;
GN   Name=Cacnb2; Synonyms=Cacnlb2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 3), AND FUNCTION.
RC   TISSUE=Heart;
RX   PubMed=14674701; DOI=10.1023/A:1027316017156;
RA   Murakami M., Aoyama M., Suzuki T., Sasano H., Nakayama S., Iijima T.;
RT   "Genetic characterization of a new splice variant of the beta2 subunit
RT   of the voltage-dependent calcium channel.";
RL   Mol. Cell. Biochem. 254:217-225(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon, Olfactory bulb, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- FUNCTION: The beta subunit of voltage-dependent calcium channels
CC       contributes to the function of the calcium channel by increasing
CC       peak calcium current, shifting the voltage dependencies of
CC       activation and inactivation, modulating G protein inhibition and
CC       controlling the alpha-1 subunit membrane targeting (By
CC       similarity).
CC   -!- SUBUNIT: The L-type calcium channel is composed of four subunits:
CC       alpha-1, alpha-2, beta and gamma. Interacts with RRAD. Interaction
CC       with RRAD regulates the trafficking of CACNA1C to the cell
CC       membrane (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Peripheral
CC       membrane protein; Cytoplasmic side (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8CC27-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CC27-2; Sequence=VSP_010730;
CC         Note=No experimental confirmation available;
CC       Name=3; Synonyms=Beta-2g;
CC         IsoId=Q8CC27-3; Sequence=VSP_010731;
CC       Name=4;
CC         IsoId=Q8CC27-4; Sequence=VSP_010731, VSP_010732;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the calcium channel beta subunit family.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB109465; BAD01474.1; -; Genomic_DNA.
DR   EMBL; AK020806; BAB32216.1; -; mRNA.
DR   EMBL; AK034054; BAC28562.1; -; mRNA.
DR   EMBL; AK078220; BAC37179.1; -; mRNA.
DR   EMBL; AL928632; CAM20242.1; -; Genomic_DNA.
DR   IPI; IPI00228423; -.
DR   IPI; IPI00420994; -.
DR   IPI; IPI00420995; -.
DR   IPI; IPI00420996; -.
DR   RefSeq; NP_075605.1; NM_023116.3.
DR   UniGene; Mm.313930; -.
DR   ProteinModelPortal; Q8CC27; -.
DR   SMR; Q8CC27; 84-467.
DR   STRING; Q8CC27; -.
DR   PhosphoSite; Q8CC27; -.
DR   PRIDE; Q8CC27; -.
DR   Ensembl; ENSMUST00000065126; ENSMUSP00000070063; ENSMUSG00000057914.
DR   Ensembl; ENSMUST00000114720; ENSMUSP00000110368; ENSMUSG00000057914.
DR   Ensembl; ENSMUST00000114723; ENSMUSP00000110371; ENSMUSG00000057914.
DR   GeneID; 12296; -.
DR   KEGG; mmu:12296; -.
DR   UCSC; uc008ikm.1; mouse.
DR   UCSC; uc008iks.1; mouse.
DR   CTD; 12296; -.
DR   MGI; MGI:894644; Cacnb2.
DR   GeneTree; ENSGT00390000002740; -.
DR   HOGENOM; HBG445475; -.
DR   HOVERGEN; HBG050765; -.
DR   InParanoid; Q8CC27; -.
DR   OMA; RHKSKDR; -.
DR   OrthoDB; EOG4WQ12J; -.
DR   PhylomeDB; Q8CC27; -.
DR   NextBio; 280802; -.
DR   ArrayExpress; Q8CC27; -.
DR   Bgee; Q8CC27; -.
DR   Genevestigator; Q8CC27; -.
DR   GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:MGI.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; TAS:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007268; P:synaptic transmission; IMP:MGI.
DR   GO; GO:0007601; P:visual perception; IMP:MGI.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR005444; VDCC_L_b2su.
DR   InterPro; IPR000584; VDCC_L_bsu.
DR   PANTHER; PTHR11824; Ca_channel_B; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF12052; VGCC_beta4Aa_N; 1.
DR   PRINTS; PR01626; LCACHANNELB.
DR   PRINTS; PR01628; LCACHANNELB2.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW   Cell membrane; Ion transport; Ionic channel; Membrane; Phosphoprotein;
KW   SH3 domain; Transport; Voltage-gated channel.
FT   CHAIN         1    655       Voltage-dependent L-type calcium channel
FT                                subunit beta-2.
FT                                /FTId=PRO_0000144052.
FT   DOMAIN      110    179       SH3.
FT   VAR_SEQ       1     67       MVQSDTSKSPPVAAVAQESQMELLESAAPAGALGAQSYGKG
FT                                ARRKNRFKGSDGSTSSDTTSNSFVRQ -> MQCCGLVHRRR
FT                                VRVSY (in isoform 2).
FT                                /FTId=VSP_010730.
FT   VAR_SEQ       1     67       MVQSDTSKSPPVAAVAQESQMELLESAAPAGALGAQSYGKG
FT                                ARRKNRFKGSDGSTSSDTTSNSFVRQ -> MKATWIRLLKR
FT                                AKGGRLKSSDIC (in isoform 3 and isoform
FT                                4).
FT                                /FTId=VSP_010731.
FT   VAR_SEQ     221    264       IDIDATGLDAEENDIPANHRSPKPSANSVTSPHSKEKRMPF
FT                                FKK -> KQKQKS (in isoform 4).
FT                                /FTId=VSP_010732.
FT   CONFLICT    124    124       A -> R (in Ref. 1; BAD01474).
SQ   SEQUENCE   655 AA;  73149 MW;  77841E9C2613843D CRC64;
     MVQSDTSKSP PVAAVAQESQ MELLESAAPA GALGAQSYGK GARRKNRFKG SDGSTSSDTT
     SNSFVRQGSA DSYTSRPSDS DVSLEEDREA VRREAERQAQ AQLEKAKTKP VAFAVRTNVR
     YSAAQEDDVP VPGMAISFEA KDFLHVKEKF NNDWWIGRLV KEGCEIGFIP SPVKLENMRL
     QHEQRAKQGK FYSSKSGGNS SSSLGDIVPS SRKSTPPSSA IDIDATGLDA EENDIPANHR
     SPKPSANSVT SPHSKEKRMP FFKKTEHTPP YDVVPSMRPV VLVGPSLKGY EVTDMMQKAL
     FDFLKHRFEG RISITRVTAD ISLAKRSVLN NPSKHAIIER SNTRSSLAEV QSEIERIFEL
     ARTLQLVVLD ADTINHPAQL SKTSLAPIIV YVKISSPKVL QRLIKSRGKS QAKHLNVQMV
     AADKLAQCPP QESFDVILDE NQLEDACEHL ADYLEAYWKA THPPSGNLPN PLLSRTLASS
     TLPLSPTLAS NSQGSQGDQR PDRSAPRSAS QAEEEPCLEP VKKSQHRSSS ATHQNHRSGT
     GRGLSRQETF DSETQESRDS AYVEPKEDYS HEHVDRYVPH REHNHREETH SSNGHRHRES
     RHRSRDMGRD QDHNECIKQR SRHKSKDRYC DKEGEVISKR RNEAGEWNRD VYIRQ
//
ID   SYNPO_MOUSE             Reviewed;         929 AA.
AC   Q8CC35; Q99JI0;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Synaptopodin;
GN   Name=Synpo; Synonyms=Kiaa1029;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-203 (ISOFORM 1).
RC   TISSUE=Brain;
RG   The MGC Project Team;
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 392-404; 567-586 AND 751-760, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 863-929 (ISOFORMS 1/3).
RC   TISSUE=Skeletal muscle;
RA   Ievolella C., Zara I., Millino C., Faulkner G., Lanfranchi G.;
RT   "Full-length sequencing of some human and murine muscular transcripts
RT   (Telethon Italy project B41).";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 921-929 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   INTERACTION WITH ACTIN, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   MEDLINE=97461576; PubMed=9314539; DOI=10.1083/jcb.139.1.193;
RA   Mundel P., Heid H.W., Mundel T.M., Krueger M., Reiser J., Kriz W.;
RT   "Synaptopodin: an actin-associated protein in telencephalic dendrites
RT   and renal podocytes.";
RL   J. Cell Biol. 139:193-204(1997).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=12357430; DOI=10.1002/cne.10362;
RA   Deller T., Haas C.A., Deissenrieder K., Del Turco D., Coulin C.,
RA   Gebhardt C., Drakew A., Schwarz K., Mundel P., Frotscher M.;
RT   "Laminar distribution of synaptopodin in normal and reeler mouse brain
RT   depends on the position of spine-bearing neurons.";
RL   J. Comp. Neurol. 453:33-44(2002).
RN   [8]
RP   FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=12928494; DOI=10.1073/pnas.1832384100;
RA   Deller T., Korte M., Chabanis S., Drakew A., Schwegler H.,
RA   Stefani G.G., Zuniga A., Schwarz K., Bonhoeffer T., Zeller R.,
RA   Frotscher M., Mundel P.;
RT   "Synaptopodin-deficient mice lack a spine apparatus and show deficits
RT   in synaptic plasticity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:10494-10499(2003).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-535; SER-672
RP   AND SER-740, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [10]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452088; DOI=10.1074/mcp.T500040-MCP200;
RA   Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G.,
RA   Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F.,
RA   Maltby D.A., Schoepfer R., Burlingame A.L.;
RT   "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT   preparations using lectin weak affinity chromatography and mass
RT   spectrometry.";
RL   Mol. Cell. Proteomics 5:923-934(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-672; SER-740;
RP   SER-833; SER-882 AND THR-884, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856 (ISOFORM 2), AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672 AND SER-833, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Actin-associated protein that may play a role in
CC       modulating actin-based shape and motility of dendritic spines and
CC       renal podocyte foot processes. Seems to be essential for the
CC       formation of spine apparatuses in spines of telencephalic neurons,
CC       which is involved in synaptic plasticity.
CC   -!- SUBUNIT: Interacts with BAIAP1. Interacts with actin. Interacts
CC       (via PPxY motifs) with WWC1 (via WW domains) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction,
CC       tight junction. Perikaryon. Cell projection, dendritic spine. Cell
CC       junction, synapse, postsynaptic cell membrane, postsynaptic
CC       density. Cell junction, synapse. Note=Localized at the tight
CC       junction of cells. In brain, localized to the postsynaptic
CC       densities and in the perikarya. Asssociated with dendritic spines
CC       of a subset of synapses.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8CC35-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q8CC35-2; Sequence=VSP_010478, VSP_010479;
CC         Note=Phosphorylated on Ser-856. Phosphorylated on Ser-824,
CC         ser-838 and Ser-869 (By similarity);
CC       Name=3;
CC         IsoId=Q8CC35-3; Sequence=VSP_010478;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, namely in the olfactory
CC       bulb, cerebral cortex, striatum, and hippocampus, but not in the
CC       cerebellum. Also expressed in the podocytes of kidney glomeruli.
CC       In the hippocampus, mainly expressed in the principal cell layer
CC       of the dentate gyrus and Ammon's horn.
CC   -!- PTM: O-glycosylated.
CC   -!- PTM: Isoform 2 is phosphorylated on Ser-824, ser-838 and Ser-869
CC       (By similarity). Isoform 2 is phosphorylated on Ser-856.
CC   -!- MISCELLANEOUS: Synpo deficient mice develop normally, but they
CC       lack the spine apparatuses. Adult mice have an impairment of
CC       spatial learning in the radial arm maze test.
CC   -!- SIMILARITY: Belongs to the synaptopodin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC28546.1; Type=Erroneous initiation;
CC       Sequence=BAC98077.1; Type=Erroneous initiation;
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DR   EMBL; AK129267; BAC98077.1; ALT_INIT; mRNA.
DR   EMBL; CF539371; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AJ278123; CAC34581.1; -; mRNA.
DR   EMBL; AK034012; BAC28546.1; ALT_INIT; mRNA.
DR   IPI; IPI00415558; -.
DR   IPI; IPI00662157; -.
DR   IPI; IPI00850112; -.
DR   UniGene; Mm.252321; -.
DR   UniGene; Mm.440740; -.
DR   ProteinModelPortal; Q8CC35; -.
DR   STRING; Q8CC35; -.
DR   PhosphoSite; Q8CC35; -.
DR   PRIDE; Q8CC35; -.
DR   Ensembl; ENSMUST00000031639; ENSMUSP00000031639; ENSMUSG00000043079.
DR   Ensembl; ENSMUST00000097566; ENSMUSP00000095174; ENSMUSG00000043079.
DR   Ensembl; ENSMUST00000115318; ENSMUSP00000110973; ENSMUSG00000043079.
DR   UCSC; uc008fap.1; mouse.
DR   UCSC; uc008far.1; mouse.
DR   MGI; MGI:1099446; Synpo.
DR   GeneTree; ENSGT00530000063754; -.
DR   HOGENOM; HBG125726; -.
DR   HOVERGEN; HBG056954; -.
DR   InParanoid; Q8CC35; -.
DR   OMA; KLYSEVH; -.
DR   OrthoDB; EOG4933H7; -.
DR   PhylomeDB; Q8CC35; -.
DR   ArrayExpress; Q8CC35; -.
DR   Bgee; Q8CC35; -.
DR   CleanEx; MM_SYNPO; -.
DR   Genevestigator; Q8CC35; -.
DR   GermOnline; ENSMUSG00000043079; Mus musculus.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0043197; C:dendritic spine; NAS:UniProtKB.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0001725; C:stress fiber; IDA:UniProtKB.
DR   GO; GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IDA:MGI.
DR   GO; GO:0030865; P:cortical cytoskeleton organization; NAS:UniProtKB.
DR   GO; GO:0032233; P:positive regulation of actin filament bundle assembly; IDA:UniProtKB.
DR   GO; GO:0051492; P:regulation of stress fiber assembly; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Cell junction; Cell membrane;
KW   Cell projection; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Glycoprotein; Membrane; Phosphoprotein; Postsynaptic cell membrane;
KW   Synapse; Tight junction.
FT   CHAIN         1    929       Synaptopodin.
FT                                /FTId=PRO_0000187671.
FT   MOTIF       549    552       PPxY motif.
FT   MOTIF       568    571       PPxY motif.
FT   COMPBIAS    766    929       Pro-rich.
FT   MOD_RES     258    258       Phosphoserine.
FT   MOD_RES     454    454       Phosphotyrosine (By similarity).
FT   MOD_RES     488    488       Phosphoserine.
FT   MOD_RES     512    512       Phosphoserine (By similarity).
FT   MOD_RES     535    535       Phosphoserine.
FT   MOD_RES     567    567       Phosphoserine (By similarity).
FT   MOD_RES     672    672       Phosphoserine.
FT   MOD_RES     689    689       Phosphoserine (By similarity).
FT   MOD_RES     740    740       Phosphoserine.
FT   MOD_RES     744    744       Phosphoserine (By similarity).
FT   MOD_RES     833    833       Phosphoserine.
FT   MOD_RES     882    882       Phosphoserine.
FT   MOD_RES     884    884       Phosphothreonine.
FT   VAR_SEQ       1    239       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_010478.
FT   VAR_SEQ     921    929       VWKPSFCFK -> DRPESLPTSPPWTPAASRPPSSLDGWVS
FT                                PGPWEPGRGSSMSSPPPLPPPPPMSPSWSERSVSPLRSETE
FT                                ARPPSRQLQALLARNIINAARRKSASPRPAPAETLRPFSPP
FT                                QGPPPPPARMRSPQPASPARNFRGAAFSPIPRSPLPIGPSS
FT                                CASPRSPQAAPSRPFPYRRSPTDSDVSLDSEDSGLKSPGIL
FT                                GYNICPRGWNGSLRLKRGSLPTEASCTT (in isoform
FT                                2).
FT                                /FTId=VSP_010479.
FT   CONFLICT    189    189       K -> M (in Ref. 2).
SQ   SEQUENCE   929 AA;  99552 MW;  979CFEE4F9E061A2 CRC64;
     MLGAHFPPPP LGASEGRAAP CTFQIPDGSY RCLALEAEES SSEDGLQGEV RLVDLEEEGT
     SQSRANHGTP PLSRAPAIIQ PSSCHREARG GFQRSDRPSH DWDVVQARKV MTASGSSSPV
     PRVAQKPALG RSTSFTENDL KEAKARSQQI AAQLTTPPSS NSRGVQLFNR RRQRVNEFTL
     ESRGQRSPKL NQEALQTGRP LSPIGHAPGP SVKPTSPSKP GSPKHPSPQS PSRGVAGHIM
     EGYSEEASLL RHLEKVASEE EEVPLVVYLK ENAALLTANG LHLSQSRETQ QSSPNPPDTE
     VPSPAADINQ NPSSPNATLT TLASSSHHSQ PTADINQNPP AAITPVPQNS SQAQCSPNGT
     LDSKPGTLCA DDGQSPVPAE EVRSSILLID KVSAPPSAAS TFSREATPLS SSGPPAADLM
     SSSLLIDMQP STLVAPAEQE VPGHVAVTTP TKVYSEVHLT LAKPASVVNR TARPFGIQSP
     GTSQIEQSPM MGRRQFGEKA WAPPASSMAD RSPQPQRHIM SRSPMVERRL LGQRSPVLER
     RPLGNFTPPP TYAETLSTAP VASRVRSPPS YSTLYPSSDP KPSHLKGQVA PANKTGILEE
     SMARRGSRKS MFTFVEKPKV TPNPDLLDLV QTADEKRRQR DHGEVGMEEE PFALGAEASN
     FQQEPIARDR ASPAAAEEAV PEWASCLKSP RIQAKPKPKP NQNLSEASGK GAELYARRQS
     RMEKYVIESS GHAELARCPS PTMSLPSSWK YTTNAPGGFR VASLSPARTP PASLYHGYLP
     ENGVLRPEPT KQQPYQMRPS LYALSPVKEP AKASSRATSS RTPSRTVSPR AASPAKPSSL
     DLVPNLPRAG LPPSPALPRP SRSSPGLYTA PVQDSLQPTA VSPTYSSDIS PVSPSRAWSP
     RAKQAPRPSF STRNAGIEAQ VWKPSFCFK
//
ID   CF222_MOUSE             Reviewed;         669 AA.
AC   Q8CC96; B2KF61; Q148X2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Uncharacterized protein C6orf222 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cecum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK033585; BAC28374.1; -; mRNA.
DR   EMBL; CT025867; CAQ52047.1; -; Genomic_DNA.
DR   EMBL; AC140278; CAQ52047.1; JOINED; Genomic_DNA.
DR   EMBL; BC117930; AAI17931.1; -; mRNA.
DR   IPI; IPI00228504; -.
DR   RefSeq; NP_766038.1; NM_172450.3.
DR   UniGene; Mm.248931; -.
DR   ProteinModelPortal; Q8CC96; -.
DR   PhosphoSite; Q8CC96; -.
DR   PRIDE; Q8CC96; -.
DR   Ensembl; ENSMUST00000062357; ENSMUSP00000050646; ENSMUSG00000048905.
DR   GeneID; 207819; -.
DR   KEGG; mmu:207819; -.
DR   UCSC; uc008bru.1; mouse.
DR   MGI; MGI:1925441; 4930539E08Rik.
DR   eggNOG; roNOG13047; -.
DR   GeneTree; ENSGT00390000001176; -.
DR   HOVERGEN; HBG101051; -.
DR   InParanoid; Q8CC96; -.
DR   OMA; ESRPPKR; -.
DR   OrthoDB; EOG4N30P6; -.
DR   PhylomeDB; Q8CC96; -.
DR   NextBio; 372067; -.
DR   ArrayExpress; Q8CC96; -.
DR   Bgee; Q8CC96; -.
DR   CleanEx; MM_4930539E08RIK; -.
DR   Genevestigator; Q8CC96; -.
PE   2: Evidence at transcript level;
FT   CHAIN         1    669       Uncharacterized protein C6orf222 homolog.
FT                                /FTId=PRO_0000317188.
FT   CONFLICT     63     63       A -> V (in Ref. 3; AAI17931).
SQ   SEQUENCE   669 AA;  72970 MW;  1E30636A45FEB39B CRC64;
     MPRSRNPSQG MPRDSSDSCG LSPVETPKGK KRARSLDRQV PRKKDPESSN TRCPSSATCR
     RTASDGARSS ESPSHFAEAQ GATAAALPPG EGRGFLPSEQ GPPEDTKKER LPREAQQSWL
     RLVLNILLMR IEEPREKASR ASKGKGDLPE AAEEPALRKK SHEKRTSRKK HSHRKPIAEE
     PPGPQTAEAQ GREDVPPSLA ASSAPHEIAL GLICRGGPDS DLPQALPTEG DHAETPDSFG
     QASGPPLEED PRKPDQDDVI WQIVELLKKA GDQLEEEQVQ IPQPEAVPPR KPTPLPRKKS
     QEKKSSLKRV LSLKKPASEE PKRVGTATTL GPETRPKRPS FLPLCVSSQR ASTSSSLDLE
     APEFQEVPSV DGGGSHPSEL HTPAAIFQGP EEKPLLDRAS ESREFRRKIL VLLQSAEDER
     GEQEAQAQEA EKAGENPTPA GKVKSQVKKS NLRRAFSLRK HSSKDSKKTE ASGTPGSGSL
     EARPPKKHGF LPMCVSGHRA SISSSPESLE FQKTEAAGGA PAGSPGAPFQ ARSHTPDEGP
     SPERAWESKE FMIQKLVASL QEVDRDLGRQ IRKYPSFKRF FNEFSDASLR KLVATLERQK
     ASLSEEGRSL ANRPPPCAFG TLNKFAATRS CTICTLMQSR GEYKGHSYAH FLSRKAEQDI
     TNLDSQSPD
//
ID   VPS53_MOUSE             Reviewed;         832 AA.
AC   Q8CCB4; Q8C7U0; Q8CIA1; Q9CX82; Q9D6T7;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Vacuolar protein sorting-associated protein 53 homolog;
GN   Name=Vps53;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Colon, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in retrograde transport of early and
CC       late endosomes to the late Golgi (By similarity).
CC   -!- SUBUNIT: Component of the Golgi-associated retrograde protein
CC       (GARP) complex, also called VFT (VPS fifty-three) complex,
CC       composed of VPS52, VPS53 and VPS54 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC       membrane; Peripheral membrane protein (By similarity). Endosome
CC       membrane; Peripheral membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CCB4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CCB4-2; Sequence=VSP_016239;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the VPS53 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB26620.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK009970; BAB26620.1; ALT_INIT; mRNA.
DR   EMBL; AK019408; BAB31707.1; -; mRNA.
DR   EMBL; AK033495; BAC28318.1; -; mRNA.
DR   EMBL; AK049259; BAC33641.1; -; mRNA.
DR   EMBL; AL591129; CAI35098.1; -; Genomic_DNA.
DR   EMBL; BC034371; AAH34371.1; -; mRNA.
DR   IPI; IPI00229808; -.
DR   IPI; IPI00387427; -.
DR   RefSeq; NP_080940.2; NM_026664.3.
DR   UniGene; Mm.46397; -.
DR   ProteinModelPortal; Q8CCB4; -.
DR   STRING; Q8CCB4; -.
DR   PhosphoSite; Q8CCB4; -.
DR   PRIDE; Q8CCB4; -.
DR   Ensembl; ENSMUST00000056601; ENSMUSP00000061317; ENSMUSG00000017288.
DR   Ensembl; ENSMUST00000108419; ENSMUSP00000104057; ENSMUSG00000017288.
DR   GeneID; 68299; -.
DR   KEGG; mmu:68299; -.
DR   UCSC; uc007kfa.1; mouse.
DR   CTD; 68299; -.
DR   MGI; MGI:1915549; Vps53.
DR   GeneTree; ENSGT00390000015165; -.
DR   HOGENOM; HBG315692; -.
DR   HOVERGEN; HBG092351; -.
DR   InParanoid; Q8CCB4; -.
DR   OMA; YMTERIA; -.
DR   OrthoDB; EOG4894KW; -.
DR   PhylomeDB; Q8CCB4; -.
DR   NextBio; 326953; -.
DR   ArrayExpress; Q8CCB4; -.
DR   Bgee; Q8CCB4; -.
DR   CleanEx; MM_VPS53; -.
DR   Genevestigator; Q8CCB4; -.
DR   GermOnline; ENSMUSG00000017288; Mus musculus.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR007234; Vps53_N.
DR   Pfam; PF04100; Vps53_N; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Coiled coil; Endosome;
KW   Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW   Transport.
FT   CHAIN         1    832       Vacuolar protein sorting-associated
FT                                protein 53 homolog.
FT                                /FTId=PRO_0000215190.
FT   COILED       55    142       Potential.
FT   MOD_RES     110    110       N6-acetyllysine (By similarity).
FT   MOD_RES     360    360       N6-acetyllysine (By similarity).
FT   MOD_RES     377    377       Phosphoserine (By similarity).
FT   MOD_RES     391    391       Phosphothreonine (By similarity).
FT   VAR_SEQ     230    406       Missing (in isoform 2).
FT                                /FTId=VSP_016239.
FT   CONFLICT     85     85       G -> V (in Ref. 1; BAB31707).
FT   CONFLICT    524    524       S -> G (in Ref. 1; BAB26620).
FT   CONFLICT    614    614       D -> E (in Ref. 1; BAB26620).
SQ   SEQUENCE   832 AA;  94423 MW;  7B9C9FFA702EE88E CRC64;
     MMEEEELEFV EELEAVLQLT PEVQLAIEQV FPSQDPLDQA DFNAVEYINT LFPTEQSLAN
     IDDVVNKIRL KIRRLDDNIR TVVRGQTNVG QDGRQALEEA QKAIQQLFGK IKDIKDKAEK
     SEQMVKEITR DIKQLDHAKR HLTTSITTLN HLHMLAGGVD SLEAMTRRRQ YGEVANLLQG
     VMNVLEHFHK YMGIPQIRQL SERVKAAQTE LGQQILADFE EAFPSQGTKR PGGPSNVLRD
     ACLVANILDP RIKQEIIKKF IKQHLSEYLV LFQENQDVAW LDKIDRRYAW VKRQLVDYEE
     KYGRMFPREW CMTERISVEF CHVTRAELSK IMRARAKEIE VKLLLFAIQR TTNFEGFLAK
     RFSGCTLTDG TLKKLESPPP STNPFLEDET TPEMEELALE KGELEQPKKP KAPDNPFHGI
     VSKCFEPHLY VYIESQDKNL SELIDRFVAD FKAQGPPKPN TDEGGAVLPS CADLFVYYKK
     CMVQCSQLST GEPMIALTTI FQKYLREYAW KILSGNLPKT SSSSGGLTIS SLLKEKEGSE
     VARFTLEELC LICSILSTAE YCLATTQQLE EKLKEKVDVS LTERINLTGE MDTFSTVISS
     SIQLLVQDLD AACDPALIAM SKMPWQNVEH VGDQSPYVTS VILHIKQNVP IIRDNLASTR
     KYFTQFCIKF ANSFIPKFIT HLFKCKPISM VGAEQLLLDT HSLKMVLLDL PSIGSQVVRK
     APASYTKIVV KGMTRAEMIL KVVMAPHEPL VVFVDNYIKL LTDCNSETFQ KILDMKGLKR
     SEQSSMLELL RQRLPAPPSG TEGSSTLSLI APTPEQESSR IRKLEKLIKK RL
//
ID   F123A_MOUSE             Reviewed;         672 AA.
AC   Q8CCJ4; Q7TNC5; Q8K0U9; Q9D0Q2;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Protein FAM123A;
GN   Name=Fam123a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 32-672 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-672 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-672 (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 599-608, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356 AND SER-359, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-282, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CCJ4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CCJ4-2; Sequence=VSP_024090;
CC   -!- SIMILARITY: Belongs to the FAM123 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH30356.1; Type=Erroneous initiation;
CC       Sequence=AAH56350.1; Type=Erroneous initiation;
CC       Sequence=BAB27452.1; Type=Erroneous initiation;
CC       Sequence=BAC27972.1; Type=Erroneous initiation;
CC       Sequence=BAE23912.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC103355; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK032651; BAC27972.1; ALT_INIT; mRNA.
DR   EMBL; AK011185; BAB27452.1; ALT_INIT; mRNA.
DR   EMBL; AK139177; BAE23912.1; ALT_INIT; mRNA.
DR   EMBL; BC030356; AAH30356.1; ALT_INIT; mRNA.
DR   EMBL; BC056350; AAH56350.1; ALT_INIT; mRNA.
DR   IPI; IPI00228580; -.
DR   IPI; IPI00844740; -.
DR   RefSeq; NP_001158177.1; NM_001164705.1.
DR   RefSeq; NP_082389.1; NM_028113.3.
DR   UniGene; Mm.275499; -.
DR   IntAct; Q8CCJ4; 1.
DR   MINT; MINT-218421; -.
DR   PhosphoSite; Q8CCJ4; -.
DR   PRIDE; Q8CCJ4; -.
DR   Ensembl; ENSMUST00000022561; ENSMUSP00000022561; ENSMUSG00000021986.
DR   GeneID; 72125; -.
DR   KEGG; mmu:72125; -.
DR   CTD; 72125; -.
DR   MGI; MGI:1919375; Fam123a.
DR   eggNOG; roNOG05734; -.
DR   GeneTree; ENSGT00530000063529; -.
DR   HOGENOM; HBG445656; -.
DR   HOVERGEN; HBG107862; -.
DR   InParanoid; Q8CCJ4; -.
DR   OrthoDB; EOG4GB766; -.
DR   NextBio; 335506; -.
DR   ArrayExpress; Q8CCJ4; -.
DR   Bgee; Q8CCJ4; -.
DR   Genevestigator; Q8CCJ4; -.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR019003; Uncharacterised_FAM123.
DR   Pfam; PF09422; WTX; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing; Phosphoprotein.
FT   CHAIN         1    672       Protein FAM123A.
FT                                /FTId=PRO_0000281886.
FT   COMPBIAS    204    207       Poly-Glu.
FT   MOD_RES     244    244       Phosphoserine.
FT   MOD_RES     282    282       Phosphothreonine.
FT   MOD_RES     356    356       Phosphoserine.
FT   MOD_RES     359    359       Phosphoserine.
FT   VAR_SEQ     255    380       Missing (in isoform 2).
FT                                /FTId=VSP_024090.
SQ   SEQUENCE   672 AA;  69933 MW;  5CE3FFDF4FFE1348 CRC64;
     METGRSRGGG AAVSERGGGA RAGVCGRQEQ AGALAADMDS HCECAAETPA AEPPSGKINK
     AAFKLFKKRK SGGTMPSIFG VKNKGDGKSS GPTGMVRSRT HDGLAEVLVL EGSKKEEPPG
     GSDHSGARPI PGPPKPSGPG LGSLASSSVA KSHSFFSLLK KNGRSETGKG DHAEASKAGG
     KQKRGLKGIF SSMRWHRRDK RGKEEEEKAV RAAGPGNLVL PGSLTASLEC VKEEPPRAAR
     RPDSPGQDAS RHAAGEPAGG EQAPASAESA PERICLEAGS PTGSGDQSSR GEDAEGHRRE
     EKPGAALESG AGEVQAAEDA SKTGDVPIKT VPLVDSEGGS GRASAVPDPS SVDPPSDPSA
     DRICLMFSDV TSLKSFDSLT GCGDIIADPE EEAGPSCDKH VPGPGKPVLS KKNASVVAYQ
     GGGEEMASPD QVDDTYLPEF WDMLSQTEDQ GQGTQEGAAK AATASDIKLA PETSSDTRCG
     EAAKDMSSVK RRRLHRIPIE SQQKEEPKHP EKEHQEGVPN SDEGYWDSTT PGPEEESISN
     SSSSKKVVIP RDSDSGDALC DLYVEPEASP ATLPATEDPP CLSRLKPVSP GTITCPLRTP
     GSLLKDSKIP ISIKHLSNLP SSHPVVHQQP ARSEVPRTKI PVSKVLVRRV SNRGLAGTTI
     RAAACHDSAK KL
//
ID   BCAS3_MOUSE             Reviewed;         928 AA.
AC   Q8CCN5; Q8CC16; Q9EPX3;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2003, sequence version 2.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Breast carcinoma-amplified sequence 3 homolog;
DE   AltName: Full=K20D4;
GN   Name=Bcas3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-477 (ISOFORM 1).
RA   Inamdar M.S.;
RT   "A gene trap clone K20D4 is expressed during vascular development.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480 AND SER-869, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CCN5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CCN5-2; Sequence=VSP_007861, VSP_007862;
CC         Note=Due to an intron retention;
CC   -!- SIMILARITY: Belongs to the WD repeat BCAS3 family.
CC   -!- SIMILARITY: Contains 3 WD repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG34697.1; Type=Erroneous termination; Positions=388; Note=Translated as Ser;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK032423; BAC27862.1; -; mRNA.
DR   EMBL; AK034117; BAC28592.1; -; mRNA.
DR   EMBL; AF313800; AAG34697.1; ALT_SEQ; mRNA.
DR   IPI; IPI00336713; -.
DR   IPI; IPI00336714; -.
DR   RefSeq; NP_001160114.1; NM_001166642.1.
DR   RefSeq; NP_619622.3; NM_138681.4.
DR   UniGene; Mm.287663; -.
DR   ProteinModelPortal; Q8CCN5; -.
DR   SMR; Q8CCN5; 91-131, 167-220, 347-373, 407-435.
DR   STRING; Q8CCN5; -.
DR   PhosphoSite; Q8CCN5; -.
DR   PRIDE; Q8CCN5; -.
DR   Ensembl; ENSMUST00000074875; ENSMUSP00000074416; ENSMUSG00000059439.
DR   GeneID; 192197; -.
DR   KEGG; mmu:192197; -.
DR   UCSC; uc007krn.1; mouse.
DR   UCSC; uc007krp.1; mouse.
DR   CTD; 192197; -.
DR   MGI; MGI:2385848; Bcas3.
DR   GeneTree; ENSGT00390000006454; -.
DR   HOVERGEN; HBG050676; -.
DR   NextBio; 371234; -.
DR   ArrayExpress; Q8CCN5; -.
DR   Bgee; Q8CCN5; -.
DR   CleanEx; MM_BCAS3; -.
DR   Genevestigator; Q8CCN5; -.
DR   GermOnline; ENSMUSG00000059439; Mus musculus.
DR   GO; GO:0071944; C:cell periphery; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR022175; BCAS3.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
DR   Pfam; PF12490; BCAS3; 1.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00320; WD40; 2.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR   PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Nucleus; Phosphoprotein; Repeat; WD repeat.
FT   CHAIN         1    928       Breast carcinoma-amplified sequence 3
FT                                homolog.
FT                                /FTId=PRO_0000050884.
FT   REPEAT       74    114       WD 1.
FT   REPEAT      349    389       WD 2.
FT   REPEAT      403    447       WD 3.
FT   MOD_RES     480    480       Phosphoserine.
FT   MOD_RES     488    488       Phosphoserine (By similarity).
FT   MOD_RES     869    869       Phosphoserine.
FT   MOD_RES     886    886       Phosphoserine.
FT   VAR_SEQ     498    527       LTSQDSYNNFTNNNPGNPRLSPLPSLMVVT -> HFPLMLL
FT                                SSRFLLYHLGSDANFYSVCAEHS (in isoform 2).
FT                                /FTId=VSP_007861.
FT   VAR_SEQ     528    928       Missing (in isoform 2).
FT                                /FTId=VSP_007862.
FT   CONFLICT     75     75       R -> Q (in Ref. 1; BAC27862).
FT   CONFLICT    472    472       T -> D (in Ref. 2).
SQ   SEQUENCE   928 AA;  101021 MW;  EF8FE46CF7011A7B CRC64;
     MNETMATDSP RRPSRCTGGV VVRPQAVTEQ SYMESVVTFL QDVVPQAYSG SPLTEEKEKI
     VWVRFENADL NDTSRNLEFH ELHSTGNEPP LLVMIGYSDG MQVWGIPISG EAQELFSVRH
     GPVRAARILP APQLGAQKCD NFAEKRPLLG VCKSIGSSGT TPPYCCVDLY SLRTGEMVKS
     IQFKTPIYDL HCNKRILVVV LQEKIAAFDS CTFTKKFFVT SCYPCPGPNM NPIALGSRWL
     AYAENKLIRC HQSRGGACGD NIQSYTATVL SAAKTLKSGL TMVGKVVTQL TGTLPSGVTE
     DDVALHCNSR RSPLVPGIIT VIDTETVGEG QVLVSEDSDS DGIVAHFPAH EKPVCCMAFN
     TSGMLLVTTD TLGHDFHVFQ ILTHPWSSSQ CAVHHLYTLH RGETEAKVQD ICFSHDCRWV
     VVSTLRGTSH VFPINPYGGQ PCVRTHMSPR VVNRMSRFQK SAGLEEIEQE LTSKQGGRCS
     PVPGLSSSPS GSPLHGKLTS QDSYNNFTNN NPGNPRLSPL PSLMVVTPLA QIKQPMTLGT
     ITKRTGPYLF GAGCFSIKAP CKVKSPPQIS PSKSMGGEFC VAAVFGTSRS WFANNAGLKR
     EKDQSKQVVV ESLYIISCYG TLVEHMIEPR PISTAPKISD DTPLEIMTSP RASWTLVRTP
     QWNELQPPFN ANHPLLLAAE AVQYYQLLLA GSLPPGSPGP ITRHGSYDSL ASDHSGQEDE
     EWLSQVEIVT HTGPHRRLWM GPQFHFKTIQ TSGQTTVIST SSSVLQSHGP SDTPQPLLDF
     DTDDLDLNSL RIQPVRSDPV SMPGSSRAVS DRRGVSTVTD AASGTFDRSV TLLEVCGSWP
     EGFGLRHMSS MEHSEEGLRE RLADAMAESP SRDVVGSGTE LQREGSIETL SNSSGSTSGS
     IPRNFDGYRS PLPTNESQPL SLFPTGFP
//
ID   SDCG1_MOUSE             Reviewed;        1064 AA.
AC   Q8CCP0; Q66JX6; Q8C9R6; Q8CA65; Q8JZT9; Q8R072; Q9CW30; Q9CYB8;
AC   Q9D4A9;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Serologically defined colon cancer antigen 1 homolog;
GN   Name=Sdccag1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Embryo, Olfactory bulb, Spinal cord, Testis, and
RC   Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 687-1064 (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-443 AND 855-1064 (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NMRI; TISSUE=Embryo, Mammary tumor, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-737 AND SER-738, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8CCP0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CCP0-2; Sequence=VSP_008397, VSP_008398;
CC         Note=Due to intron retention. No experimental confirmation
CC         available;
CC       Name=3;
CC         IsoId=Q8CCP0-3; Sequence=VSP_010465, VSP_010466;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q8CCP0-4; Sequence=VSP_010463, VSP_010464;
CC   -!- SIMILARITY: Belongs to the SDCCAG1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH27272.1; Type=Erroneous initiation;
CC       Sequence=AAH53488.2; Type=Erroneous initiation;
CC       Sequence=BAB30366.1; Type=Erroneous initiation;
CC       Sequence=BAC27849.1; Type=Erroneous initiation;
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DR   EMBL; AK005212; BAB23886.1; -; mRNA.
DR   EMBL; AK016662; BAB30366.1; ALT_INIT; mRNA.
DR   EMBL; AK017826; BAB30959.1; -; mRNA.
DR   EMBL; AK032388; BAC27849.1; ALT_INIT; mRNA.
DR   EMBL; AK039497; BAC30369.1; -; mRNA.
DR   EMBL; AK041458; BAC30950.1; -; mRNA.
DR   EMBL; AK089000; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC027272; AAH27272.1; ALT_INIT; mRNA.
DR   EMBL; BC037106; AAH37106.2; -; mRNA.
DR   EMBL; BC053488; AAH53488.2; ALT_INIT; mRNA.
DR   EMBL; BC080716; AAH80716.1; -; mRNA.
DR   IPI; IPI00227669; -.
DR   IPI; IPI00277549; -.
DR   IPI; IPI00380816; -.
DR   IPI; IPI00416572; -.
DR   RefSeq; NP_079717.2; NM_025441.2.
DR   UniGene; Mm.234368; -.
DR   UniGene; Mm.46705; -.
DR   ProteinModelPortal; Q8CCP0; -.
DR   STRING; Q8CCP0; -.
DR   PhosphoSite; Q8CCP0; -.
DR   PRIDE; Q8CCP0; -.
DR   Ensembl; ENSMUST00000021368; ENSMUSP00000021368; ENSMUSG00000020982.
DR   GeneID; 66244; -.
DR   KEGG; mmu:66244; -.
DR   UCSC; uc007nse.1; mouse.
DR   UCSC; uc007nsg.1; mouse.
DR   UCSC; uc007nsh.1; mouse.
DR   CTD; 66244; -.
DR   MGI; MGI:1918305; Sdccag1.
DR   GeneTree; ENSGT00390000018516; -.
DR   HOVERGEN; HBG079170; -.
DR   InParanoid; Q8CCP0; -.
DR   OMA; TTIQKAR; -.
DR   OrthoDB; EOG4JDH63; -.
DR   PhylomeDB; Q8CCP0; -.
DR   NextBio; 321071; -.
DR   ArrayExpress; Q8CCP0; -.
DR   Bgee; Q8CCP0; -.
DR   CleanEx; MM_SDCCAG1; -.
DR   Genevestigator; Q8CCP0; -.
DR   GermOnline; ENSMUSG00000020982; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR021846; DUF3441.
DR   InterPro; IPR008532; DUF814.
DR   InterPro; IPR008616; Fibro-bd_N.
DR   Pfam; PF11923; DUF3441; 1.
DR   Pfam; PF05670; DUF814; 1.
DR   Pfam; PF05833; FbpA; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Nucleus; Phosphoprotein.
FT   CHAIN         1   1064       Serologically defined colon cancer
FT                                antigen 1 homolog.
FT                                /FTId=PRO_0000097643.
FT   MOD_RES     417    417       Phosphoserine (By similarity).
FT   MOD_RES     702    702       Phosphoserine (By similarity).
FT   MOD_RES     737    737       Phosphoserine.
FT   MOD_RES     738    738       Phosphoserine.
FT   VAR_SEQ     412    415       NPYL -> GGRW (in isoform 4).
FT                                /FTId=VSP_010463.
FT   VAR_SEQ     416   1064       Missing (in isoform 4).
FT                                /FTId=VSP_010464.
FT   VAR_SEQ     638    641       KKNF -> NSLT (in isoform 3).
FT                                /FTId=VSP_010465.
FT   VAR_SEQ     642   1064       Missing (in isoform 3).
FT                                /FTId=VSP_010466.
FT   VAR_SEQ     889    892       SAGS -> VSII (in isoform 2).
FT                                /FTId=VSP_008397.
FT   VAR_SEQ     893   1064       Missing (in isoform 2).
FT                                /FTId=VSP_008398.
FT   CONFLICT    295    295       A -> P (in Ref. 1; BAB23886).
FT   CONFLICT    405    405       H -> Q (in Ref. 1; BAB30959).
FT   CONFLICT    416    416       L -> S (in Ref. 1; BAB23886).
FT   CONFLICT    443    443       Q -> K (in Ref. 2; AAH80716).
FT   CONFLICT    873    873       K -> R (in Ref. 2; AAH53488).
FT   CONFLICT   1023   1023       H -> Y (in Ref. 2; AAH53488).
SQ   SEQUENCE   1064 AA;  121188 MW;  F74F6ED7552AB183 CRC64;
     MKSRFSTVDL RAVLAELNAS LLGMRVNNVY DVDNKTYLIR LQKPDFKATL LLESGIRIHT
     TEFEWPKNMM PSSFAMKCRK HLKSRRLVSA KQLGVDRIVD FQFGSDEAAY HLIIELYDRG
     NIVLTDYEYL ILNILRFRTD EADDVKFAVR ERYPIDHARA AEPLLTLERL TEVIAAAPKG
     EVLKRVLNPL LPYGPALIEH CLIESGFSGN AKVDEKLESK DIEKILVCVQ RAEDYLRKTS
     NFNGKGYIIQ KREAKPSLDA DKPAEDILTY EEFHPFLFSQ HLQCPYIEFE SFDKAVDEFY
     SKIEGQKIDL KALQQEKQAL KKLDNVRKDH ENRLEALQQA QEIDKLKGEL IEMNLQIVDR
     AIQVVRSALA NQIDWTEIGV IVKEAQAQGD PVACAIKELK LQTNHVTMLL RNPYLLSEEE
     DGDGDASIEN SDAEAPKGKK KKQKNKQLQK PQKNKPLLVD VDLSLSAYAN AKKYYDHKRY
     AAKKTQRTVE AAEKAFKSAE KKTKQTLKEV QTVTSIQKAR KVYWFEKFLW FISSENYLII
     GGRDQQQNEI IVKRYLTPGD IYVHADLHGA TSCVIKNPTG EPIPPRTLTE AGTMALCYSA
     AWDARVITSA WWVYHHQVSK TAPTGEYLTT GSFMIRGKKN FLPPSYLMMG FSFLFKVDES
     CVWRHRGERK VRVQDEDMET LTSCTSELMA EEMEQLEGGD SSEEETEELH GMPGDVELMT
     QVDQEDIAVH SGRDELSSED GEAKAVTKDQ EPIGEMKEEE EDTFEYPDTT IDLSHLQSQR
     PLQKLAPREE SLNSNDSKSQ GRRHLSAKER REMKKKKLPC ESGDLEVIEE KDKERESAVH
     TEAYQNTSKN VAAGQPMKRG QKSKMKKMKE KYKDQDDEDR ELIMKLLASA GSNKEEKGKK
     GKKGKPKDEP VKKPPQKPRG GQRVLDVVKE PPSLQVLAHD LQDLAVDDPH DDKEEHDLDQ
     QGNEENLFDS LTGQPHPEDV LMFAIPICAP YTIMTNYKYK VKLTPGVQKK GKAAKTALNS
     FMHSKEATAR EKDLFRSVKD TDLSRNIPGK VKVSAPNLLH VKRK
//
ID   TCAL5_MOUSE             Reviewed;         200 AA.
AC   Q8CCT4; Q497R6;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Transcription elongation factor A protein-like 5;
DE            Short=TCEA-like protein 5;
DE   AltName: Full=Transcription elongation factor S-II protein-like 5;
GN   Name=Tceal5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- SIMILARITY: Belongs to the TFS-II family. TFA subfamily.
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DR   EMBL; AK032140; BAC27722.1; -; mRNA.
DR   EMBL; BC100415; AAI00416.1; -; mRNA.
DR   IPI; IPI00228674; -.
DR   RefSeq; NP_808587.1; NM_177919.2.
DR   UniGene; Mm.41605; -.
DR   ProteinModelPortal; Q8CCT4; -.
DR   STRING; Q8CCT4; -.
DR   PhosphoSite; Q8CCT4; -.
DR   UCD-2DPAGE; Q8CCT4; -.
DR   PRIDE; Q8CCT4; -.
DR   Ensembl; ENSMUST00000066819; ENSMUSP00000065397; ENSMUSG00000054034.
DR   GeneID; 331532; -.
DR   KEGG; mmu:331532; -.
DR   UCSC; uc009uif.1; mouse.
DR   CTD; 331532; -.
DR   MGI; MGI:3036236; Tceal5.
DR   GeneTree; ENSGT00510000046867; -.
DR   HOGENOM; HBG127442; -.
DR   HOVERGEN; HBG055896; -.
DR   InParanoid; Q8CCT4; -.
DR   OMA; KADEDKS; -.
DR   OrthoDB; EOG4VQ9QH; -.
DR   PhylomeDB; Q8CCT4; -.
DR   NextBio; 399821; -.
DR   ArrayExpress; Q8CCT4; -.
DR   Bgee; Q8CCT4; -.
DR   CleanEx; MM_TCEAL5; -.
DR   Genevestigator; Q8CCT4; -.
DR   GermOnline; ENSMUSG00000054034; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR021156; TF_A-like/BEX-like.
DR   InterPro; IPR010370; TFA.
DR   PANTHER; PTHR14754; TFA; 1.
DR   Pfam; PF04538; BEX; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Transcription; Transcription regulation.
FT   CHAIN         1    200       Transcription elongation factor A
FT                                protein-like 5.
FT                                /FTId=PRO_0000239212.
FT   COMPBIAS      2     74       Glu-rich.
FT   CONFLICT     75     75       G -> A (in Ref. 2; AAI00416).
SQ   SEQUENCE   200 AA;  22038 MW;  A843465710CE11F7 CRC64;
     MEKFYKENEG KPENKGRAED EGSTEEGGKA DEDKSDAEGK PARQGKLEVE GGPGEQAQQK
     GEGKPEKQGK SDGEGKRQGE SKPDSQAKSA SEARAAEKRP AEDYVPRKAK RKTDRGTDDS
     PKNSQEDLQD RHVSSEEMMR ECADMTRAQE ELRKRQKMGG FHWVPRDAQD ALVPRGQRGV
     RGVRGGGGRG QKDLEDAPFV
//
ID   Q8CD65_MOUSE            Unreviewed;       347 AA.
AC   Q8CD65;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 49.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Kcnab1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK031362; BAC27367.1; -; mRNA.
DR   IPI; IPI00969849; -.
DR   UniGene; Mm.316402; -.
DR   HSSP; Q46933; 1LQA.
DR   ProteinModelPortal; Q8CD65; -.
DR   SMR; Q8CD65; 73-343.
DR   STRING; Q8CD65; -.
DR   Ensembl; ENSMUST00000159525; ENSMUSP00000124311; ENSMUSG00000027827.
DR   MGI; MGI:109155; Kcnab1.
DR   GeneTree; ENSGT00550000074567; -.
DR   HOVERGEN; HBG052216; -.
DR   InParanoid; Q8CD65; -.
DR   ArrayExpress; Q8CD65; -.
DR   Bgee; Q8CD65; -.
DR   Genevestigator; Q8CD65; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:InterPro.
DR   InterPro; IPR001395; Aldo/ket_red.
DR   InterPro; IPR005983; K_chnl_volt-dep_bsu_KCNAB.
DR   InterPro; IPR005399; K_chnl_volt-dep_bsu_KCNAB-rel.
DR   InterPro; IPR005400; K_chnl_volt-dep_bsu_KCNAB1.
DR   InterPro; IPR023210; NADP_OxRdtase_dom.
DR   Gene3D; G3DSA:3.20.20.100; Aldo/ket_red; 1.
DR   PANTHER; PTHR11732; Aldo/ket_red; 1.
DR   PANTHER; PTHR11732:SF14; KCNAB_channel; 1.
DR   Pfam; PF00248; Aldo_ket_red; 1.
DR   PRINTS; PR01578; KCNAB1CHANEL.
DR   PRINTS; PR01577; KCNABCHANNEL.
DR   SUPFAM; SSF51430; Aldo/ket_red; 1.
DR   TIGRFAMs; TIGR01293; Kv_beta; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   347 AA;  38558 MW;  A3C2C8C23827C1B1 CRC64;
     MQVSIACTEH NLKSRNGEDR LLSKQSSNAP NVVNAARAKF RTVAIIARSL GTFTPQHHIS
     LKESTAKQTG MKYRNLGKSG LRVSCLGLGT WVTFGGQISD EVAERLMTIA YESGVNLFDT
     AEVYAAGKAE VILGSIIKKK GWRRSSLVIT TKLYWGGKAE TERGLSRKHI IEGLKGSLQR
     LQLEYVDVVF ANRPDSNTPM EEIVRAMTHV INQGMAMYWG TSRWSAMEIM EAYSVARQFN
     MIPPVCEQAE YHLFQREKVE VQLPELYHKI GVGAMTWSPL ACGIISGKYG NGVPESSRAS
     LKCYQWLKER IVSEEGRKQQ NKLKDLSPIA ERLGCTLPQL AVGSSPC
//
ID   SAC2_MOUSE              Reviewed;        1132 AA.
AC   Q8CDA1; Q3UCS0; Q6NX83; Q6ZQ16; Q8C8G7; Q8CBW2;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Phosphatidylinositide phosphatase SAC2;
DE            EC=3.1.3.-;
DE   AltName: Full=Inositol polyphosphate 5-phosphatase F;
DE   AltName: Full=Sac domain-containing inositol phosphatase 2;
DE   AltName: Full=Sac domain-containing phosphoinositide 5-phosphatase 2;
GN   Name=Inpp5f; Synonyms=Kiaa0966, Sac2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow, Cerebellum, Diencephalon, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-829; SER-906 AND
RP   SER-910, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=17322895; DOI=10.1038/nm1552;
RA   Trivedi C.M., Luo Y., Yin Z., Zhang M., Zhu W., Wang T., Floss T.,
RA   Goettlicher M., Noppinger P.R., Wurst W., Ferrari V.A., Abrams C.S.,
RA   Gruber P.J., Epstein J.A.;
RT   "Hdac2 regulates the cardiac hypertrophic response by modulating Gsk3
RT   beta activity.";
RL   Nat. Med. 13:324-331(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-943 AND SER-946, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Inositol 5-phosphatase which acts on
CC       phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol
CC       3,4,5-triphosphate. Hydrolyzes phosphatidylinositol 4,5-
CC       bisphosphate most effectively. Modulates AKT/GSK3B pathway by
CC       decreasing AKT and GSK3B phosphorylation (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8CDA1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CDA1-2; Sequence=VSP_033271, VSP_033274;
CC       Name=3;
CC         IsoId=Q8CDA1-3; Sequence=VSP_033270;
CC       Name=4;
CC         IsoId=Q8CDA1-4; Sequence=VSP_033272, VSP_033273;
CC   -!- INDUCTION: Up-regulated in the absence of histone deacetylase
CC       2/HDAC2 in the heart from HDAC2-null mice.
CC   -!- SIMILARITY: Contains 1 SAC domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC28723.1; Type=Frameshift; Positions=692;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK129249; BAC98059.1; -; mRNA.
DR   EMBL; AK030870; BAC27166.1; -; mRNA.
DR   EMBL; AK034482; BAC28723.1; ALT_FRAME; mRNA.
DR   EMBL; AK047166; BAC32978.1; -; mRNA.
DR   EMBL; AK150418; BAE29542.1; -; mRNA.
DR   EMBL; BC067200; AAH67200.1; -; mRNA.
DR   EMBL; BC125437; AAI25438.1; -; mRNA.
DR   IPI; IPI00420542; -.
DR   IPI; IPI00654237; -.
DR   IPI; IPI00876396; -.
DR   IPI; IPI00890940; -.
DR   RefSeq; NP_848756.2; NM_178641.5.
DR   UniGene; Mm.464029; -.
DR   ProteinModelPortal; Q8CDA1; -.
DR   SMR; Q8CDA1; 5-520.
DR   STRING; Q8CDA1; -.
DR   PhosphoSite; Q8CDA1; -.
DR   PRIDE; Q8CDA1; -.
DR   Ensembl; ENSMUST00000043138; ENSMUSP00000045910; ENSMUSG00000042105.
DR   Ensembl; ENSMUST00000098007; ENSMUSP00000095616; ENSMUSG00000042105.
DR   GeneID; 101490; -.
DR   KEGG; mmu:101490; -.
DR   UCSC; uc009jzc.1; mouse.
DR   CTD; 101490; -.
DR   MGI; MGI:2141867; Inpp5f.
DR   GeneTree; ENSGT00530000063393; -.
DR   HOGENOM; HBG714173; -.
DR   HOVERGEN; HBG095361; -.
DR   InParanoid; Q8CDA1; -.
DR   OMA; KFHGGWA; -.
DR   OrthoDB; EOG4640B6; -.
DR   PhylomeDB; Q8CDA1; -.
DR   NextBio; 354962; -.
DR   ArrayExpress; Q8CDA1; -.
DR   Bgee; Q8CDA1; -.
DR   Genevestigator; Q8CDA1; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR022158; hSac2.
DR   InterPro; IPR002013; Syja_N.
DR   Pfam; PF12456; hSac2; 1.
DR   Pfam; PF02383; Syja_N; 1.
DR   PROSITE; PS50275; SAC; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Hydrolase; Phosphoprotein.
FT   CHAIN         1   1132       Phosphatidylinositide phosphatase SAC2.
FT                                /FTId=PRO_0000331622.
FT   DOMAIN      167    518       SAC.
FT   MOD_RES     829    829       Phosphoserine.
FT   MOD_RES     906    906       Phosphoserine.
FT   MOD_RES     910    910       Phosphoserine.
FT   MOD_RES     943    943       Phosphoserine.
FT   MOD_RES     946    946       Phosphoserine.
FT   MOD_RES    1069   1069       Phosphoserine (By similarity).
FT   VAR_SEQ       1    691       Missing (in isoform 3).
FT                                /FTId=VSP_033270.
FT   VAR_SEQ       1    627       Missing (in isoform 2).
FT                                /FTId=VSP_033271.
FT   VAR_SEQ     373    414       VIVNLVDQAGREKIIGDAYLKQVLLFNNPKLTYVSFDFHEH
FT                                C -> RIWVWSQHPLTQREEKRREEKRREEKRREEKRREEK
FT                                RREEVT (in isoform 4).
FT                                /FTId=VSP_033272.
FT   VAR_SEQ     415   1132       Missing (in isoform 4).
FT                                /FTId=VSP_033273.
FT   VAR_SEQ     628    629       PS -> MH (in isoform 2).
FT                                /FTId=VSP_033274.
FT   CONFLICT    728    728       E -> D (in Ref. 3; AAH67200).
SQ   SEQUENCE   1132 AA;  127608 MW;  4EDEA936E95D486C CRC64;
     MELFQAKDHY ILQQGERALW CSRRDGGLQL RPATDLLLAW NPICLGLVEG VIGKIQLHSD
     LPWWLILIRQ KALVGKLPGD HEVCKVTKIA VLSLSEMEPQ ELELELCKKH HFGINKPEKI
     IPSPDDSKFL LKTFTNIKSN VSAPNKKKVK ESKEKEKLER RLLEELLKMF MDSESFYYSL
     TYDLTNSVQR QSTGERDGRP LWQKVDDRFF WNKYMIQALT EIGTPDVDFW IIPIIQGFVQ
     IEELVVNYNE SSDDDKSSPE TPPQDSTCVD DIHPRFLVAL ISRRSRHRAG MRYKRRGVDK
     NGNVANYVET EQLIHVHHHT LSFIQTRGSV PVFWSQVGYR YNPRPRLDKS EKETVDCFCA
     HFEEQLKIYK KQVIVNLVDQ AGREKIIGDA YLKQVLLFNN PKLTYVSFDF HEHCRGMKFE
     NVQTLTDAIH DIIIDMKWCW VDQAGVICKQ EGIFRVNCMD CLDRTNVVQA AIARVVMEQQ
     LKKLGVMPPE QPLPVKCNRT YQIMWANNGD SISRQYAGTA ALKGDFTRTG ERKLAGVMKD
     GVNSANRYYL SRFKDAYRQA VIDLMQGVPV TEDLYSIFTK EKEHEALHKE SQRSHQELIS
     QLLQSYMQLL LPGDEKFHGG WALVDCDPSL TDAAHRDVEV LLLLSNAAYY VAYYDDEVDK
     VNQYQRLGLE DLERIEIGPE PTLFGKPKFS CMRLHYRCKE AGGYFHTLRA VPRSPEEDGK
     DTLQCIAEML QITKQAMGLD VPIIEKKLER KSSKPHEDII GIRSQNQGSL AQGKSFLMSK
     FSSLNQKVKQ TKSNVNIGNL RKLGNFTKPE MKVNFLKPNL KVNLWKSDSS LETMENPGVM
     GNKVQGESDG DISSDNDSYH SDEFLTNSKS EEDKQLANSL ESVGPIDYIL PSCGIIVSAP
     RLGSRSQSAS SIDVSTHAPS EAAAGPGSEL GKGLESPLKK SPSADSIHTR TGFTKPMDVY
     CQRFVQDAQN KMNDLSEIRS VAQKSEEGSH KTNRVSNEET QSEPMGQTPP RPSQLNVSCS
     VAGPPFLSVE PVHSVLSQKT PSSGSSLLEL EAGLCVTPSS ESSSSRAVSP FAKIRSSMVQ
     VANITQAGLT HGINLAVAKV QKSPAEPEAV NEIQQNELKN MFTQCQTRII QI
//
ID   VCIP1_MOUSE             Reviewed;        1220 AA.
AC   Q8CDG3; Q7TMU9; Q8BP90;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Deubiquitinating protein VCIP135;
DE            EC=3.4.22.-;
DE   AltName: Full=Valosin-containing protein p97/p47 complex-interacting protein 1;
DE   AltName: Full=Valosin-containing protein p97/p47 complex-interacting protein p135;
GN   Name=Vcpip1; Synonyms=Vcip135;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hematopoietic;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Acts as a deubiquitinating enzyme. Necessary for VCP-
CC       mediated reassembly of Golgi stacks after mitosis. May play a role
CC       in VCP-mediated formation of transitional endoplasmic reticulum
CC       (tER). Mediates dissociation of the ternary complex containing
CC       STX5A, NSFL1C and VCP (By similarity).
CC   -!- SUBUNIT: Binds VCP and the ternary complex containing STX5A,
CC       NSFL1C and VCP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum (By similarity). Golgi
CC       apparatus, Golgi stack (By similarity). Note=Associated with Golgi
CC       stacks and endoplasmic reticulum (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CDG3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CDG3-2; Sequence=VSP_009376, VSP_009377;
CC         Note=May be due to an intron retention. No experimental
CC         confirmation available;
CC   -!- SIMILARITY: Contains 1 OTU domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH52908.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK030104; BAC26787.1; -; mRNA.
DR   EMBL; AK077494; BAC36830.1; -; mRNA.
DR   EMBL; BC052908; AAH52908.1; ALT_INIT; mRNA.
DR   EMBL; BC059209; AAH59209.1; -; mRNA.
DR   IPI; IPI00377609; -.
DR   IPI; IPI00466186; -.
DR   RefSeq; NP_775619.2; NM_173443.2.
DR   UniGene; Mm.274493; -.
DR   UniGene; Mm.440951; -.
DR   ProteinModelPortal; Q8CDG3; -.
DR   SMR; Q8CDG3; 157-392.
DR   IntAct; Q8CDG3; 1.
DR   STRING; Q8CDG3; -.
DR   PhosphoSite; Q8CDG3; -.
DR   PRIDE; Q8CDG3; -.
DR   Ensembl; ENSMUST00000057438; ENSMUSP00000051248; ENSMUSG00000045210.
DR   GeneID; 70675; -.
DR   KEGG; mmu:70675; -.
DR   UCSC; uc007ags.1; mouse.
DR   CTD; 70675; -.
DR   MGI; MGI:1917925; Vcpip1.
DR   GeneTree; ENSGT00390000002854; -.
DR   HOVERGEN; HBG059748; -.
DR   InParanoid; Q8CDG3; -.
DR   OrthoDB; EOG4RBQHR; -.
DR   NextBio; 332059; -.
DR   ArrayExpress; Q8CDG3; -.
DR   Bgee; Q8CDG3; -.
DR   Genevestigator; Q8CDG3; -.
DR   GermOnline; ENSMUSG00000045210; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR   GO; GO:0004843; F:ubiquitin-specific protease activity; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR   InterPro; IPR003323; OTU.
DR   Pfam; PF02338; OTU; 1.
DR   PROSITE; PS50802; OTU; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Endoplasmic reticulum;
KW   Golgi apparatus; Hydrolase; Isopeptide bond; Phosphoprotein; Protease;
KW   Thiol protease; Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN         1   1220       Deubiquitinating protein VCIP135.
FT                                /FTId=PRO_0000065770.
FT   DOMAIN      207    360       OTU.
FT   COMPBIAS      4     20       Pro-rich.
FT   MOD_RES     407    407       N6-acetyllysine (By similarity).
FT   MOD_RES     746    746       Phosphoserine (By similarity).
FT   MOD_RES     756    756       Phosphoserine (By similarity).
FT   MOD_RES     760    760       Phosphothreonine (By similarity).
FT   MOD_RES     762    762       Phosphothreonine (By similarity).
FT   MOD_RES     766    766       Phosphotyrosine (By similarity).
FT   MOD_RES     769    769       Phosphothreonine (By similarity).
FT   MOD_RES     993    993       Phosphoserine (By similarity).
FT   MOD_RES     997    997       Phosphoserine (By similarity).
FT   MOD_RES    1196   1196       Phosphoserine (By similarity).
FT   CROSSLNK    869    869       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   VAR_SEQ     904    906       EDV -> KSN (in isoform 2).
FT                                /FTId=VSP_009376.
FT   VAR_SEQ     907   1220       Missing (in isoform 2).
FT                                /FTId=VSP_009377.
FT   CONFLICT    471    471       Y -> C (in Ref. 2; AAH59209).
SQ   SEQUENCE   1220 AA;  134503 MW;  8062E3C17DCD2E3B CRC64;
     MSQPPPPPPL PPPPPPPEAP QTSSSLAAAA SPGGLSKRRD RRILSGSCPD PKCQARLFFP
     ASGSVSIECT ECGQRHEQQQ LLGVEEVTDP DVVLHNLLRN ALLGVTGAPK KNTELVKVMG
     LSNYHCKLLS PILARYGMDK QTGRAKLLRD MNQGELFDCA LLGDRAFLIE PEHVNTVGYG
     KDRSGSLLYL HDTLEDIKRA NKSQECLIPV HVDGDGHCLV HAVSRALVGR ELFWHALREN
     LKQHFQQHLA RYQALFHDFI DAAEWEDIIN ECDPLFVPPE GVPLGLRNIH IFGLANVLHR
     PIILLDSLSG MRSSGDYSAT FLPGLIPAEK CTGRDGHLNK PICIAWSSSG RNHYIPLVGI
     KGAALPKLPM NLLPKAWGVP QDLIKKYIKL EEDGGCVIGG DRSLQDKYLL RLVAAMEEVF
     MDKHGIHPSL VADVHQYFYR RTGVIGVQPE EVTAAAKKAV MDNRLHKCLL YGALSELHVP
     SEWLAPGGKL YNLAKSTHGQ LRPDKNYSFP LNNLVCSYDP VKDVLLPDYG LSNLTACNWC
     HGSSVRRVRG DGSIVYLDGD RTNSRSTGGK CGCGFKHFWE GKEYDNLPEA FPITLEWGGR
     VVRETVYWFQ YESDPSLNSN VYDVAMKLVT KHFPGEFGSE ILVQKVVHTI LHQTAKKNPD
     DYTPVNIDGA HAQRVGDVQG QELESQLPTK IILTGQKTKT LHKEELNMSK TERTIQQNIT
     EQASVMQKRK TEKLKQEQKG QPRTVSPSTI RDGPSSAPAT PTKAPYSPTT SKEKKIRITT
     NDGRQSMVTL KPSTTFFELQ ESIAREFNIP PYLQCIRYGF PPKELMPPQA GMEKEPVPLQ
     HGDRITIEIL KGRAEGGPST AAHSAHTVKQ EEIAVTGKLS SKELQEQADK EMYSLCLLAT
     LMGEDVWSYA KGLPHMFQQG GVFYNIMKKT MGMADGKHCT FPHLPGKTFV YNASEDRLEL
     CVDAAGHFPI GPDVEDLVKE AVSQVRAEAT TRSRESSPSH GLLKLGSGGV VKKKSEQLHN
     VTAFQGKGHS LGTASSHPHI DPRARETLAV RKHNTGTDFS NSSIKTEPPV FTAASSNSEL
     IRIAPGVVTM RDGRQIDPDV VEAQRKKLQE MVSSIQASMD KHLRDQSAEQ APSDLSQRKV
     EVVSSVRPVN LQTGLPEPFS LTGGTENLNT ETTDSHVADV LGAAFATRSK AQKENSMEEP
     EEMDSQDAET TNTTEPMDHS
//
ID   TXNL1_MOUSE             Reviewed;         289 AA.
AC   Q8CDN6; O70379; Q3TI92;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Thioredoxin-like protein 1;
DE   AltName: Full=32 kDa thioredoxin-related protein;
GN   Name=Txnl1; Synonyms=Trp32, Txnl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98334653; PubMed=9668102; DOI=10.1074/jbc.273.30.19160;
RA   Lee K.-K., Murakawa M., Takahashi S., Tsubuki S., Kawashima S.,
RA   Sakamaki K., Yonehara S.;
RT   "Purification, molecular cloning, and characterization of TRP32, a
RT   novel thioredoxin-related mammalian protein of 32 kDa.";
RL   J. Biol. Chem. 273:19160-19166(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2; TISSUE=Amnion, Bone marrow, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
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DR   EMBL; AF052660; AAC40183.1; -; mRNA.
DR   EMBL; AK029807; BAC26626.1; -; mRNA.
DR   EMBL; AK150326; BAE29469.1; -; mRNA.
DR   EMBL; AK167954; BAE39954.1; -; mRNA.
DR   EMBL; AK168712; BAE40554.1; -; mRNA.
DR   EMBL; BC061123; AAH61123.1; -; mRNA.
DR   IPI; IPI00266281; -.
DR   RefSeq; NP_058072.2; NM_016792.4.
DR   UniGene; Mm.19169; -.
DR   ProteinModelPortal; Q8CDN6; -.
DR   SMR; Q8CDN6; 2-108, 123-279.
DR   STRING; Q8CDN6; -.
DR   PhosphoSite; Q8CDN6; -.
DR   REPRODUCTION-2DPAGE; Q8CDN6; -.
DR   PRIDE; Q8CDN6; -.
DR   Ensembl; ENSMUST00000025476; ENSMUSP00000025476; ENSMUSG00000024583.
DR   GeneID; 53382; -.
DR   KEGG; mmu:53382; -.
DR   UCSC; uc008fdx.1; mouse.
DR   CTD; 53382; -.
DR   MGI; MGI:1860078; Txnl1.
DR   eggNOG; roNOG06692; -.
DR   GeneTree; ENSGT00530000063008; -.
DR   HOVERGEN; HBG055982; -.
DR   InParanoid; Q8CDN6; -.
DR   OMA; VNSVTLF; -.
DR   OrthoDB; EOG4KD6MH; -.
DR   PhylomeDB; Q8CDN6; -.
DR   NextBio; 310213; -.
DR   ArrayExpress; Q8CDN6; -.
DR   Bgee; Q8CDN6; -.
DR   CleanEx; MM_TXNL1; -.
DR   Genevestigator; Q8CDN6; -.
DR   GermOnline; ENSMUSG00000024583; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR010400; Proteasome-int_thioredoxin_C.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:2.60.120.470; G3DSA:2.60.120.470; 1.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   PANTHER; PTHR10438; Trx; 1.
DR   Pfam; PF06201; DUF1000; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF49785; Gal_bind_like; 1.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Cytoplasm; Disulfide bond; Electron transport; Phosphoprotein;
KW   Redox-active center; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    289       Thioredoxin-like protein 1.
FT                                /FTId=PRO_0000120017.
FT   DOMAIN        2    109       Thioredoxin.
FT   MOD_RES     113    113       Phosphoserine.
FT   DISULFID     34     37       Redox-active (By similarity).
FT   CONFLICT    251    251       N -> K (in Ref. 1; AAC40183).
SQ   SEQUENCE   289 AA;  32237 MW;  4BE29C6C1D1DFA0A CRC64;
     MVGVKPVGSD PDFQPELSGA GSRLAVVKFT MRGCGPCLRI APAFSSMSNK YPQAVFLEVD
     VHQCQGTAAT NNISATPTFL FFRNKVRIDQ YQGADAVGLE EKIKQHLEND PGSNEDADIP
     KGYMDLMPFI NKAGCECLNE SDEHGFDNCL RKDMSFLESD CDEQLLITVA FNQPVKLYSM
     KFQGPDNGQG PKYVKIFINL PRSMDFEEAE RSEPTQALEL TEDDIKEDGI VPLRYVKFQN
     VNSVTLFVQS NQGEEETTRI SYFTFIGTPV QATNMNDFKR VVGKKGESH
//
ID   HECD2_MOUSE             Reviewed;         774 AA.
AC   Q8CDU6; Q8CBQ9;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Probable E3 ubiquitin-protein ligase HECTD2;
DE            EC=6.3.2.-;
DE   AltName: Full=HECT domain-containing protein 2;
GN   Name=Hectd2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Probable E3 ubiquitin-protein ligase which accepts
CC       ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a
CC       thioester and then directly transfers the ubiquitin to targeted
CC       substrates (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SIMILARITY: Contains 1 HECT (E6AP-type E3 ubiquitin-protein
CC       ligase) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC29085.1; Type=Erroneous initiation;
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK029549; BAC26510.1; -; mRNA.
DR   EMBL; AK035511; BAC29085.1; ALT_INIT; mRNA.
DR   IPI; IPI00944168; -.
DR   RefSeq; NP_001156943.1; NM_001163471.1.
DR   RefSeq; NP_766225.2; NM_172637.3.
DR   UniGene; Mm.61107; -.
DR   ProteinModelPortal; Q8CDU6; -.
DR   SMR; Q8CDU6; 367-768.
DR   PhosphoSite; Q8CDU6; -.
DR   PRIDE; Q8CDU6; -.
DR   Ensembl; ENSMUST00000047247; ENSMUSP00000042646; ENSMUSG00000041180.
DR   GeneID; 226098; -.
DR   KEGG; mmu:226098; -.
DR   UCSC; uc008hho.1; mouse.
DR   CTD; 226098; -.
DR   MGI; MGI:2442663; Hectd2.
DR   GeneTree; ENSGT00550000074324; -.
DR   HOVERGEN; HBG081596; -.
DR   InParanoid; Q8CDU6; -.
DR   OrthoDB; EOG4B8JCJ; -.
DR   PhylomeDB; Q8CDU6; -.
DR   NextBio; 377980; -.
DR   ArrayExpress; Q8CDU6; -.
DR   Bgee; Q8CDU6; -.
DR   CleanEx; MM_HECTD2; -.
DR   Genevestigator; Q8CDU6; -.
DR   GermOnline; ENSMUSG00000041180; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0006464; P:protein modification process; IEA:InterPro.
DR   InterPro; IPR000569; HECT.
DR   Pfam; PF00632; HECT; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SUPFAM; SSF56204; HECT; 1.
DR   PROSITE; PS50237; HECT; 1.
PE   2: Evidence at transcript level;
KW   Ligase; Ubl conjugation pathway.
FT   CHAIN         1    774       Probable E3 ubiquitin-protein ligase
FT                                HECTD2.
FT                                /FTId=PRO_0000240852.
FT   DOMAIN      435    774       HECT.
FT   ACT_SITE    742    742       Glycyl thioester intermediate (By
FT                                similarity).
FT   CONFLICT    754    754       R -> K (in Ref. 1; BAC29085).
SQ   SEQUENCE   774 AA;  87787 MW;  3CFF1F4815AA15D5 CRC64;
     MSEAARDLSP GAPPAVAAAA PEERKGKEPE REKLPPIVTA GAAAGLDRGS KGQISTFSSF
     VSTVTQKKEA AENRSSPTHL ALPNIRNVRD LPPICLDVRQ KQRMSVEALP SEVKVPPLPE
     PSLPSQPKTV KDFEEDLEKA EATGNWKTVH AFYITAFDSF TELNTAFKKD ATASFNTIED
     SGLNANLVNA VFDALLNTPQ DIQKSVLKGI INSLLQEWKG PRTKDDLRAY FILLQNPQFN
     ITSTYVIYAH LLRQIATLVE ADHHFLVHWL KKLSQKKFKQ LVERLLQFVS LRLFPAKPEE
     FPPLTKCTWW IPSAGKVLAL LNTANNLVHP PLVPYTDFYN STLDHIDLME EYHTWQSFGN
     SHRFSFCQYP FVISIAAKKI IIQRDSEQQM ISIARQSLVD KVSRRQRPDM NMLFLNMKVR
     RTHLVSDSLD ELTRKRADLK KKLKVTFVGE AGLDMGGLTK EWFLLLIRQI FHPDYGMFTY
     HKDSHCHWFS SFKCDNYSEF RLVGILMGLA VYNSITLDIR FPPCCYKKLL SPPVVPSDQS
     TPVGICSVTI DDLCQVMPEL AHGLKELLSY EGNVEEDFYS TFQVFQEEFG VIKSYNLKPG
     GDKIPVTNQN RREYVQLYTD FLLNKSIYKQ FAAFYCGFHS VCASNALMLL RPEEVEILVC
     GSPELDMHAL QRSTQYDGYA KTDLTIRYFW DVVLGFPLEL QKKLLHFTTG SDRVPVGGMA
     DLNFKISKNE TSTNWLPVAH TCFNQLCLPP YKSRKDLKQK LIIGISNSEG FGLE
//
ID   SNX30_MOUSE             Reviewed;         437 AA.
AC   Q8CE50; Q3UHE6;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Sorting nexin-30;
GN   Name=Snx30;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, C57BL/6J, and NOD;
RC   TISSUE=Brain, Dendritic cell, Skin, and Submandibular gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in several stages of intracellular
CC       trafficking (By similarity).
CC   -!- SIMILARITY: Belongs to the sorting nexin family.
CC   -!- SIMILARITY: Contains 1 PX (phox homology) domain.
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DR   EMBL; AK029012; BAC26242.1; -; mRNA.
DR   EMBL; AK147437; BAE27911.1; -; mRNA.
DR   EMBL; AK165619; BAE38299.1; -; mRNA.
DR   EMBL; AK170774; BAE42020.1; -; mRNA.
DR   EMBL; AK170999; BAE42170.1; -; mRNA.
DR   EMBL; AL831738; CAM24713.1; -; Genomic_DNA.
DR   EMBL; BC099674; AAH99674.1; -; mRNA.
DR   IPI; IPI00228948; -.
DR   RefSeq; NP_766056.1; NM_172468.2.
DR   UniGene; Mm.259705; -.
DR   HSSP; Q9UMY4; 2CSK.
DR   ProteinModelPortal; Q8CE50; -.
DR   SMR; Q8CE50; 87-206.
DR   STRING; Q8CE50; -.
DR   PhosphoSite; Q8CE50; -.
DR   PRIDE; Q8CE50; -.
DR   Ensembl; ENSMUST00000030080; ENSMUSP00000030080; ENSMUSG00000028385.
DR   GeneID; 209131; -.
DR   KEGG; mmu:209131; -.
DR   UCSC; uc008tae.1; mouse.
DR   CTD; 209131; -.
DR   MGI; MGI:2443882; Snx30.
DR   eggNOG; roNOG06249; -.
DR   GeneTree; ENSGT00530000063144; -.
DR   HOGENOM; HBG506074; -.
DR   HOVERGEN; HBG009723; -.
DR   InParanoid; Q8CE50; -.
DR   OMA; TRPLEFA; -.
DR   OrthoDB; EOG4K6G46; -.
DR   PhylomeDB; Q8CE50; -.
DR   NextBio; 372561; -.
DR   ArrayExpress; Q8CE50; -.
DR   Bgee; Q8CE50; -.
DR   CleanEx; MM_SNX30; -.
DR   Genevestigator; Q8CE50; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR004148; BAR.
DR   InterPro; IPR001683; Phox.
DR   Gene3D; G3DSA:3.30.1520.10; PX; 1.
DR   Pfam; PF03114; BAR; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; PX; 1.
DR   PROSITE; PS50195; PX; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1    437       Sorting nexin-30.
FT                                /FTId=PRO_0000284534.
FT   DOMAIN       89    210       PX.
FT   MOD_RES      40     40       Phosphoserine (By similarity).
FT   CONFLICT     19     19       D -> G (in Ref. 1; BAE27911).
SQ   SEQUENCE   437 AA;  49520 MW;  52805380D0E0D158 CRC64;
     MAGGPPKALP STGPQSLRDM PHPLAGSSSE EAVGGDSTPS PDLLMARSFG DKDLILPNGG
     TPAGTASPAS SSSLLNRLQL DDDIDGEARD LFVTVDDPKK HVCTMETYIT YRITTKSTRV
     EFDLPEYSVR RRYQDFDWLR NKLEESQPTH LIPPLPEKFV VKGVVDRFSE EFVETRRKAL
     DKFLKRITDH PVLSFNEHFN VFLTAKDLNA YKKQGIALLS RVGESVKHVT GGYKLRSRPL
     EFAAISDYLD TFALKLGTID RIAQRIIKEE IEYLVELREY GPVYSTWSAL EGELAEPLEG
     VSACIGNCST ALEELTDDIT EEFLPVLREY VLYSDSMKGV LKKRDQVQAE YEAKLEAVAL
     RKEERPKVPA DVEKCQDRME CFNADLKADM ERWQSNKRHD FRQLLVGLAD KNIQYYEKCL
     MAWESIIPLL QEKQETK
//
ID   TRM6_MOUSE              Reviewed;         497 AA.
AC   Q8CE96; Q3TJZ8; Q3TME7; Q6ZPW8; Q80Y59; Q8CEU0;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=tRNA (adenine-N(1)-)-methyltransferase non-catalytic subunit TRM6;
DE   AltName: Full=tRNA(m1A58)-methyltransferase subunit TRM6;
DE            Short=tRNA(m1A58)MTase subunit TRM6;
GN   Name=Trmt6; Synonyms=Kiaa1153, Trm6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryo;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Blastocyst;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-108, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
CC   -!- FUNCTION: Substrate-binding subunit of tRNA (adenine-N(1)-)-
CC       methyltransferase, which catalyzes the formation of N(1)-
CC       methyladenine at position 58 (m1A58) in initiator methionyl-tRNA
CC       (By similarity).
CC   -!- SUBUNIT: tRNA (adenine-N(1)-)-methyltransferase is a heterodimer
CC       of TRM6 and TRM61 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8CE96-1; Sequence=Displayed;
CC       Name=3;
CC         IsoId=Q8CE96-3; Sequence=VSP_018026;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q8CE96-4; Sequence=VSP_018026, VSP_018027, VSP_018028;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Belongs to the TRM6/GCD10 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98110.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC       Sequence=BAC98110.1; Type=Frameshift; Positions=490;
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DR   EMBL; AK129300; BAC98110.1; ALT_SEQ; mRNA.
DR   EMBL; AK014359; BAC25432.1; -; mRNA.
DR   EMBL; AK165976; BAE38495.1; -; mRNA.
DR   EMBL; AK167222; BAE39347.1; -; mRNA.
DR   EMBL; AK028755; BAC26100.1; -; mRNA.
DR   EMBL; BC049083; AAH49083.1; -; mRNA.
DR   EMBL; BC052648; AAH52648.1; -; mRNA.
DR   IPI; IPI00453830; -.
DR   IPI; IPI00458059; -.
DR   IPI; IPI00752927; -.
DR   RefSeq; NP_780322.2; NM_175113.3.
DR   UniGene; Mm.34199; -.
DR   ProteinModelPortal; Q8CE96; -.
DR   PhosphoSite; Q8CE96; -.
DR   PRIDE; Q8CE96; -.
DR   Ensembl; ENSMUST00000039554; ENSMUSP00000044687; ENSMUSG00000037376.
DR   Ensembl; ENSMUST00000110126; ENSMUSP00000105753; ENSMUSG00000037376.
DR   GeneID; 66926; -.
DR   KEGG; mmu:66926; -.
DR   NMPDR; fig|10090.3.peg.6972; -.
DR   UCSC; uc008mng.1; mouse.
DR   UCSC; uc008mnh.1; mouse.
DR   CTD; 66926; -.
DR   MGI; MGI:1914176; Trmt6.
DR   GeneTree; ENSGT00390000008327; -.
DR   HOVERGEN; HBG061231; -.
DR   OrthoDB; EOG4P2Q2K; -.
DR   PhylomeDB; Q8CE96; -.
DR   NextBio; 323037; -.
DR   ArrayExpress; Q8CE96; -.
DR   Bgee; Q8CE96; -.
DR   CleanEx; MM_TRMT6; -.
DR   Genevestigator; Q8CE96; -.
DR   GermOnline; ENSMUSG00000037376; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:InterPro.
DR   GO; GO:0006446; P:regulation of translational initiation; IEA:InterPro.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR007316; EIF3_gamma.
DR   InterPro; IPR017423; tRNA_m1A_mtfrase.
DR   PANTHER; PTHR12945; EIF3_gamma; 1.
DR   Pfam; PF04189; Gcd10p; 1.
DR   PIRSF; PIRSF038170; tRNA_m1A_mtfrase; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Nucleus; Phosphoprotein;
KW   tRNA processing.
FT   CHAIN         1    497       tRNA (adenine-N(1)-)-methyltransferase
FT                                non-catalytic subunit TRM6.
FT                                /FTId=PRO_0000233099.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     108    108       Phosphothreonine.
FT   VAR_SEQ       1    183       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_018026.
FT   VAR_SEQ     343    358       IQEKQRRQEEQRKRHL -> VSMSRVIILVIASEPR (in
FT                                isoform 4).
FT                                /FTId=VSP_018027.
FT   VAR_SEQ     359    497       Missing (in isoform 4).
FT                                /FTId=VSP_018028.
FT   CONFLICT      9      9       P -> Q (in Ref. 2; BAE38495).
FT   CONFLICT     86     86       S -> P (in Ref. 2; BAE38495).
FT   CONFLICT    159    159       V -> I (in Ref. 2; BAE38495).
FT   CONFLICT    283    283       S -> N (in Ref. 2; BAE38495).
FT   CONFLICT    377    377       R -> H (in Ref. 2; BAE39347).
SQ   SEQUENCE   497 AA;  55518 MW;  F6F16FE689DB514B CRC64;
     MEASAAEQPS SPPPPLGDHC IHDGDFVVLK REDVFKAVQV QRRKKVTFEK QWFYLDNAIG
     HSYGSAFDVS SGGSLQLRKK LEEPASETKE AGTDNRNIVD DGKSQKLTQD DIKALKDKGI
     KGEEIVQQLI ENSTTFRDKT EFAQDKYIKK KKKKYEAIVT ILKPSTRILS IMYYAREPGK
     INHMRYDTLA QMLTLGNIRA GNKMIVMETC SGLVLGAMME RMGGFGSIIQ LYPGDGPVRA
     ATACFGFPKS FLSGLYEFPL NKVNSLLNGT FSAEMLSSEP KDSTPVEESN GELEEKEIAE
     QADEDNIVDA AENNSGEQRP MEIVPGDPEN KEPKEKRSKR DYIQEKQRRQ EEQRKRHLEA
     AALLGERNAD GLIVASRFHP TPLLLSLLDF VAPSRPFVVY CQYKEPLLEC YTKLRERGGV
     INLRLSETWL RNYQVLPDRS HPKLLMSGGG GYLLSGFTVV SDSLRADPSL KSCTGALDPH
     KAEEPAAKKQ KCMESAS
//
ID   RDH13_MOUSE             Reviewed;         334 AA.
AC   Q8CEE7; Q8CC07;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Retinol dehydrogenase 13;
DE            EC=1.1.1.-;
GN   Name=Rdh13;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Does not exhibit retinol dehydrogenase (RDH) activity in
CC       vitro (By similarity).
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
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DR   EMBL; AK028434; BAC25950.1; -; mRNA.
DR   EMBL; AK034180; BAC28618.1; -; mRNA.
DR   EMBL; BC082583; AAH82583.1; -; mRNA.
DR   IPI; IPI00229040; -.
DR   RefSeq; NP_780581.1; NM_175372.4.
DR   UniGene; Mm.413106; -.
DR   ProteinModelPortal; Q8CEE7; -.
DR   SMR; Q8CEE7; 35-288.
DR   STRING; Q8CEE7; -.
DR   PRIDE; Q8CEE7; -.
DR   Ensembl; ENSMUST00000008579; ENSMUSP00000008579; ENSMUSG00000008435.
DR   GeneID; 108841; -.
DR   KEGG; mmu:108841; -.
DR   UCSC; uc009exm.1; mouse.
DR   CTD; 108841; -.
DR   MGI; MGI:1918732; Rdh13.
DR   eggNOG; roNOG08071; -.
DR   GeneTree; ENSGT00570000078988; -.
DR   HOGENOM; HBG750976; -.
DR   HOVERGEN; HBG078800; -.
DR   InParanoid; Q8CEE7; -.
DR   OMA; GPIFWLL; -.
DR   OrthoDB; EOG43R3N9; -.
DR   PhylomeDB; Q8CEE7; -.
DR   NextBio; 361381; -.
DR   ArrayExpress; Q8CEE7; -.
DR   Bgee; Q8CEE7; -.
DR   CleanEx; MM_RDH13; -.
DR   Genevestigator; Q8CEE7; -.
DR   GermOnline; ENSMUSG00000008435; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   PROSITE; PS00061; ADH_SHORT; 1.
PE   2: Evidence at transcript level;
KW   NADP; Oxidoreductase.
FT   CHAIN         1    334       Retinol dehydrogenase 13.
FT                                /FTId=PRO_0000054769.
FT   NP_BIND      45     51       NAD or NADP (By similarity).
FT   ACT_SITE    200    200       Proton acceptor (By similarity).
FT   BINDING     174    174       Substrate (By similarity).
FT   CONFLICT    114    148       Missing (in Ref. 1; BAC28618).
SQ   SEQUENCE   334 AA;  36464 MW;  4EBBCE1643C1FECE CRC64;
     MSRFLLPVSV VGTVIGGTVL LKDYVAGGAC PSKATIPGKT VIVTGANTGI GKQTALELAK
     RGGNVILACR DMEKCEVAAK DIRGETLNPR VRAERLDLAS LKSIREFARK VIKEEERVDI
     LVNNAAVMRC PHWTTEDGFE MQFGVNYLGH FLLTNLLLDK LKASAPSRII NLSSLAHVAG
     HIDFEDLNWQ MKKYDTKAAY CQSKLAVVLF TKELSHRLQG SGVTVNALHP GVARTELGRH
     TGMHNSAFSG FMLGPFFWLL FKSPQLAAQP STYLAVAEEL ENVSGKYFDG LREKAPSPEA
     EDEEVARRLW TESARLVGLA MAHGSPGRGH AIPR
//
ID   CC28B_MOUSE             Reviewed;         200 AA.
AC   Q8CEG5; Q8K132;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Coiled-coil domain-containing protein 28B;
GN   Name=Ccdc28b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; AK028262; BAC25848.1; -; mRNA.
DR   EMBL; AK158016; BAE34319.1; -; mRNA.
DR   EMBL; BC028873; AAH28873.1; -; mRNA.
DR   IPI; IPI00318620; -.
DR   RefSeq; NP_079731.2; NM_025455.2.
DR   UniGene; Mm.383215; -.
DR   STRING; Q8CEG5; -.
DR   PRIDE; Q8CEG5; -.
DR   Ensembl; ENSMUST00000030586; ENSMUSP00000030586; ENSMUSG00000028795.
DR   GeneID; 66264; -.
DR   KEGG; mmu:66264; -.
DR   UCSC; uc008uxu.1; mouse.
DR   CTD; 66264; -.
DR   MGI; MGI:1913514; Ccdc28b.
DR   GeneTree; ENSGT00500000044870; -.
DR   HOVERGEN; HBG061498; -.
DR   OrthoDB; EOG44TP94; -.
DR   NextBio; 321139; -.
DR   ArrayExpress; Q8CEG5; -.
DR   Bgee; Q8CEG5; -.
DR   CleanEx; MM_CCDC28B; -.
DR   Genevestigator; Q8CEG5; -.
DR   GermOnline; ENSMUSG00000028795; Mus musculus.
PE   2: Evidence at transcript level;
KW   Coiled coil; Phosphoprotein.
FT   CHAIN         1    200       Coiled-coil domain-containing protein
FT                                28B.
FT                                /FTId=PRO_0000234095.
FT   COILED      158    189       Potential.
FT   MOD_RES      46     46       Phosphoserine (By similarity).
FT   CONFLICT     17     17       Q -> P (in Ref. 1; BAC25848).
SQ   SEQUENCE   200 AA;  22064 MW;  BC057791B8FC280A CRC64;
     MEDKKKKRSP KPCLTQQAQA PGTLRRVPVP TSHSGSLALG LPHLPSPKQR AKFKRAGKEK
     CRPVLAGGGG GSAGTPLQHS FLTEVTDVYE MEGGLLNLLN DFHSGRLQAF GKECSFEQLE
     HVREMQEKLA RLHFSLDVCG EEEDEEEEED GVTEGLPEEQ KKTMADRNLD QLLSNLEDLS
     NSIQKLHLAE NAEPEDQPAA
//
ID   Q8CEQ9_MOUSE            Unreviewed;       752 AA.
AC   Q8CEQ9;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 49.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=4932414N04Rik;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RA   Adachi J., Aizawa K., Akahira S., Akimura T., Arai A., Aono H.,
RA   Arakawa T., Bono H., Carninci P., Fukuda S., Fukunishi Y., Furuno M.,
RA   Hanagaki T., Hara A., Hayatsu N., Hiramoto K., Hiraoka T., Hori F.,
RA   Imotani K., Ishii Y., Itoh M., Izawa M., Kasukawa T., Kato H.,
RA   Kawai J., Kojima Y., Konno H., Kouda M., Koya S., Kurihara C.,
RA   Matsuyama T., Miyazaki A., Nishi K., Nomura K., Numazaki R., Ohno M.,
RA   Okazaki Y., Okido T., Owa C., Saito H., Saito R., Sakai C., Sakai K.,
RA   Sano H., Sasaki D., Shibata K., Shibata Y., Shinagawa A., Shiraki T.,
RA   Sogabe Y., Suzuki H., Tagami M., Tagawa A., Takahashi F., Tanaka T.,
RA   Tejima Y., Toya T., Yamamura T., Yasunishi A., Yoshida K., Yoshino M.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
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DR   EMBL; AK016523; BAC25486.1; -; mRNA.
DR   IPI; IPI00281164; -.
DR   RefSeq; NP_898936.1; NM_183113.3.
DR   UniGene; Mm.65456; -.
DR   PRIDE; Q8CEQ9; -.
DR   Ensembl; ENSMUST00000055930; ENSMUSP00000059809; ENSMUSG00000048204.
DR   GeneID; 75721; -.
DR   KEGG; mmu:75721; -.
DR   UCSC; uc008jxr.1; mouse.
DR   MGI; MGI:1922971; 4932414N04Rik.
DR   eggNOG; maNOG08689; -.
DR   GeneTree; ENSGT00520000060168; -.
DR   InParanoid; Q8CEQ9; -.
DR   OMA; LELRIQH; -.
DR   OrthoDB; EOG44QT2Q; -.
DR   NextBio; 343776; -.
DR   ArrayExpress; Q8CEQ9; -.
DR   Bgee; Q8CEQ9; -.
DR   Genevestigator; Q8CEQ9; -.
PE   1: Evidence at protein level;
SQ   SEQUENCE   752 AA;  87255 MW;  AE558764BB1796E8 CRC64;
     MLTKKTSSEK NKALKYADAM DDHQLSESLS EDYDLPDYDN ILMIVDQLQM NYKDSGKPLE
     IQDAVHSYKM IVERNQNHSE LLIEKSKNKR NQGHRVMKKP GETEKAKLQL RCRREEQQLD
     LLDVGSPEKQ DMQQRNPDGW YEEMKKELTE KDPQHGREKQ QLELRLRAQD MELQHLRNDI
     NKLQEAQHPE TEAGHGDSMT KGHLQKVEHE VFKLVETIKK QSETIEQLER KLANEDKILT
     GTGHLTQAGR DFFNAFREMY TTSVMSQLEL RIQHLEREFS EMKTRTWENG VVLENYVKLH
     QSHKLMETES KMKEVMSQFA MLTQHNTALL NLLSSVFASE CPCKGRSKSL FTQENMLTST
     SGPQPANQSI IAHLDAPADD NEDFNKALTK SILSPQSELH QKKEKCLESA EEKTLRKKRF
     KPTKTSTVCE NGEHSFFEVS NTRQFEKNTP VDEPQHEIIR EDQETLDNIP GNHNTLIISP
     WEYRCTDLES EHSEERTHHA FCKAEPEQYK DPCLEWVPIT RSPSQGQLRS KDRQDGPIRK
     NFNKMEAYTS TSNACMMSSG PEFGSGQLYN SLGYSRNFLQ REPLMTTSRP QTFENSLSFP
     NRVREENQQT SYDKVGHHNA SRIKPQKATL STLQSKHPEV THQASCKAEP KRYEEPHPER
     IQMTSPLTYD QLKSKDRQDE SVRRNFVKME AYSSVLNTYT TTSPAPGFGS GQCCNSLEHS
     RSFTPPISRP WRFVESVDSY LCRTWQQLHY HY
//
ID   Q8CF63_MOUSE            Unreviewed;       301 AA.
AC   Q8CF63;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Nisch;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RA   Adachi J., Aizawa K., Akahira S., Akimura T., Arai A., Aono H.,
RA   Arakawa T., Bono H., Carninci P., Fukuda S., Fukunishi Y., Furuno M.,
RA   Hanagaki T., Hara A., Hayatsu N., Hiramoto K., Hiraoka T., Hori F.,
RA   Imotani K., Ishii Y., Itoh M., Izawa M., Kasukawa T., Kato H.,
RA   Kawai J., Kojima Y., Konno H., Kouda M., Koya S., Kurihara C.,
RA   Matsuyama T., Miyazaki A., Nishi K., Nomura K., Numazaki R., Ohno M.,
RA   Okazaki Y., Okido T., Owa C., Saito H., Saito R., Sakai C., Sakai K.,
RA   Sano H., Sasaki D., Shibata K., Shibata Y., Shinagawa A., Shiraki T.,
RA   Sogabe Y., Suzuki H., Tagami M., Tagawa A., Takahashi F., Tanaka T.,
RA   Tejima Y., Toya T., Yamamura T., Yasunishi A., Yoshida K., Yoshino M.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK004628; BAC25092.1; -; mRNA.
DR   IPI; IPI00110435; -.
DR   UniGene; Mm.298728; -.
DR   HSSP; P07359; 1M0Z.
DR   ProteinModelPortal; Q8CF63; -.
DR   SMR; Q8CF63; 69-213.
DR   STRING; Q8CF63; -.
DR   Ensembl; ENSMUST00000022469; ENSMUSP00000022469; ENSMUSG00000021910.
DR   MGI; MGI:1928323; Nisch.
DR   GeneTree; ENSGT00530000063625; -.
DR   HOVERGEN; HBG071006; -.
DR   InParanoid; Q8CF63; -.
DR   ArrayExpress; Q8CF63; -.
DR   Bgee; Q8CF63; -.
DR   Genevestigator; Q8CF63; -.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005178; F:integrin binding; IDA:MGI.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IDA:MGI.
DR   GO; GO:0030336; P:negative regulation of cell migration; IDA:MGI.
DR   GO; GO:0016601; P:Rac protein signal transduction; IDA:MGI.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   Pfam; PF00560; LRR_1; 3.
DR   PROSITE; PS51450; LRR; 6.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   301 AA;  33126 MW;  45E40222FC7A467B CRC64;
     MFKSLHHVER DHRDTQHIRG LVTSKPTLAT MSVRFSATSM KEVLAPEASE FDEWEPEGTA
     TLGGPVTAII PTWQALTTLD LSHNSICEID ESVKLIPKIE YLDLSHNGLR VVDNLQHLYN
     LVHLDLSYNK LSSLEGVHTK LGNVKTLNLA GNFLESLSGL HKLYSLVNVD LRDNRIEQLD
     EVKSIGSLPC LERLTLLNNP LSIIPDYRTK VLSQFGERAS EICLDDVATT EKELDTVEVL
     KAIQKAKDVK SKLSNTEKKA GEDFRLPPAP CIRPGGSPPA APASASLPQP ILSNQGILGD
     E
//
ID   TAB1_MOUSE              Reviewed;         502 AA.
AC   Q8CF89; Q7TQJ5; Q80V65; Q8R0D1;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 2.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=TGF-beta-activated kinase 1 and MAP3K7-binding protein 1;
DE   AltName: Full=Mitogen-activated protein kinase kinase kinase 7-interacting protein 1;
DE   AltName: Full=TGF-beta-activated kinase 1-binding protein 1;
DE            Short=TAK1-binding protein 1;
GN   Name=Tab1; Synonyms=Map3k7ip1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=22352456; PubMed=12464436; DOI=10.1016/S0925-4773(02)00391-X;
RA   Komatsu Y., Shibuya H., Takeda N., Ninomiya-Tsuji J., Yasui T.,
RA   Miyado K., Sekimoto T., Ueno N., Matsumoto K., Yamada G.;
RT   "Targeted disruption of the Tab1 gene causes embryonic lethality and
RT   defects in cardiovascular and lung morphogenesis.";
RL   Mech. Dev. 119:239-249(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Eye, Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be an important signaling intermediate between TGFB
CC       receptors and MAP3K7/TAK1. May play an important role in mammalian
CC       embryogenesis.
CC   -!- SUBUNIT: Interacts with XIAP and BIRC7. Interacts with TRAF6 and
CC       MAP3K7; during IL-1 signaling. Identified in the TRIKA2 complex
CC       composed of MAP3K7, TAB1 and TAB2 (By similarity).
CC   -!- INTERACTION:
CC       Q91YI4:Arrb2; NbExp=1; IntAct=EBI-1778503, EBI-994161;
CC       Q62073:Map3k7; NbExp=1; IntAct=EBI-1778503, EBI-1775345;
CC       Q86Y07-1:VRK2 (xeno); NbExp=1; IntAct=EBI-1778503, EBI-1207633;
CC   -!- PTM: Monoubiquitinated (By similarity).
CC   -!- SIMILARITY: Contains 1 PP2C-like domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AB088136; BAC43729.1; -; mRNA.
DR   EMBL; BC027054; AAH27054.1; -; mRNA.
DR   EMBL; BC041110; AAH41110.1; -; mRNA.
DR   EMBL; BC054369; AAH54369.1; -; mRNA.
DR   IPI; IPI00380503; -.
DR   RefSeq; NP_079885.2; NM_025609.2.
DR   UniGene; Mm.288245; -.
DR   ProteinModelPortal; Q8CF89; -.
DR   SMR; Q8CF89; 16-370, 466-494.
DR   IntAct; Q8CF89; 7.
DR   STRING; Q8CF89; -.
DR   PhosphoSite; Q8CF89; -.
DR   PRIDE; Q8CF89; -.
DR   Ensembl; ENSMUST00000023050; ENSMUSP00000023050; ENSMUSG00000022414.
DR   GeneID; 66513; -.
DR   KEGG; mmu:66513; -.
DR   UCSC; uc007wve.1; mouse.
DR   CTD; 66513; -.
DR   MGI; MGI:1913763; Tab1.
DR   HOGENOM; HBG714303; -.
DR   HOVERGEN; HBG007302; -.
DR   InParanoid; Q8CF89; -.
DR   OMA; AEHTEAD; -.
DR   OrthoDB; EOG4R7V9G; -.
DR   PhylomeDB; Q8CF89; -.
DR   NextBio; 321908; -.
DR   ArrayExpress; Q8CF89; -.
DR   Bgee; Q8CF89; -.
DR   Genevestigator; Q8CF89; -.
DR   GermOnline; ENSMUSG00000022414; Mus musculus.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0019209; F:kinase activator activity; IMP:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0000185; P:activation of MAPKKK activity; IMP:MGI.
DR   GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0030324; P:lung development; IMP:MGI.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:MGI.
DR   InterPro; IPR001932; PP2C-like.
DR   InterPro; IPR014045; PP2C_N.
DR   InterPro; IPR015655; Protein_Pase_2C.
DR   Gene3D; G3DSA:3.60.40.10; PP2C-related; 1.
DR   PANTHER; PTHR13832; PP2C; 1.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-related; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Ubl conjugation.
FT   CHAIN         1    502       TGF-beta-activated kinase 1 and MAP3K7-
FT                                binding protein 1.
FT                                /FTId=PRO_0000057798.
FT   DOMAIN       64    368       PP2C-like.
FT   COMPBIAS    450    455       Poly-Ser.
FT   MOD_RES       7      7       Phosphoserine (By similarity).
FT   MOD_RES     436    436       Phosphoserine (By similarity).
FT   CONFLICT    199    199       Q -> H (in Ref. 1; BAC43729).
FT   CONFLICT    210    212       ENE -> DND (in Ref. 1; BAC43729).
FT   CONFLICT    323    323       L -> P (in Ref. 1; BAC43729).
SQ   SEQUENCE   502 AA;  54616 MW;  F7529D2E3CF30696 CRC64;
     MAAQRRSLLQ SEQQPSWTDD LPLCHLSGVG SASNRSYSAD GKGTESHPPE DNWLKFRSEN
     NCFLYGVFNG YDGNRVTNFV AQRLSAELLL GQLNTEHTEA DVRRVLLQAF DVVERSFLES
     IDDALAEKAS LQSQLPEGVP QHQLPPQYQK ILERLKALER EISGGAMAVV AVLLNSKLYV
     ANVGTNRALL CKSTVDGLQV TQLNMDHTTE NEDELFRLSQ LGLDAGKIKQ MGVICGQEST
     RRIGDYKVKY GYTDIDLLSA AKSKPIIAEP EIHGAQPLDG VTGFLVLMSE GLYKALEAAH
     GPGQANQEIA AMIDTEFAKQ TSLDAVAQAV VDRVKRIHSD TFASGGERAK FCPRHEDMTL
     LVRNFGYPLG EMSQPTPTPA PGGRVYPVSV PYSSAQSTSK TSVTLSLVMP SQGQMVNGSH
     SASTLDEATP TLTNQSPTLT LQSTNTHTQS SSSSSDGGLF RSRPAHSLPP GEDGRVEPYV
     DFAEFYRLWS VDHGEQSVMT AP
//
ID   Q8CF95_MOUSE            Unreviewed;       518 AA.
AC   Q8CF95;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 52.
DE   SubName: Full=Synaptotagmin VIIgamma;
GN   Name=Syt7; Synonyms=syt VIIgamma;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=22067076; PubMed=12071850; DOI=10.1042/BJ20011877;
RA   Fukuda M., Ogata Y., Saegusa C., Kanno E., Mikoshiba K.;
RT   "Alternative splicing isoforms of synaptotagmin VII in the mouse, rat
RT   and human.";
RL   Biochem. J. 365:173-180(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c; TISSUE=Brain;
RA   Mitsunori F.;
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 2 C2 domains.
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DR   EMBL; AB075901; BAC44833.1; -; mRNA.
DR   IPI; IPI00229256; -.
DR   UniGene; Mm.182654; -.
DR   HSSP; P21707; 1RSY.
DR   ProteinModelPortal; Q8CF95; -.
DR   SMR; Q8CF95; 248-517.
DR   STRING; Q8CF95; -.
DR   PhosphoSite; Q8CF95; -.
DR   PRIDE; Q8CF95; -.
DR   Ensembl; ENSMUST00000025652; ENSMUSP00000025652; ENSMUSG00000024743.
DR   UCSC; uc008gpo.1; mouse.
DR   MGI; MGI:1859545; Syt7.
DR   GeneTree; ENSGT00600000084008; -.
DR   HOGENOM; HBG716633; -.
DR   HOVERGEN; HBG005010; -.
DR   InParanoid; Q8CF95; -.
DR   ArrayExpress; Q8CF95; -.
DR   Bgee; Q8CF95; -.
DR   Genevestigator; Q8CF95; -.
DR   GO; GO:0005764; C:lysosome; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0008021; C:synaptic vesicle; IEA:InterPro.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   GO; GO:0001778; P:plasma membrane repair; IDA:MGI.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   InterPro; IPR001565; Synaptotagmin.
DR   InterPro; IPR015427; Synaptotagmin7.
DR   PANTHER; PTHR10024:SF29; Synaptotagmin7; 1.
DR   Pfam; PF00168; C2; 2.
DR   PRINTS; PR00360; C2DOMAIN.
DR   PRINTS; PR00399; SYNAPTOTAGMN.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 2.
PE   2: Evidence at transcript level;
KW   Repeat.
SQ   SEQUENCE   518 AA;  58260 MW;  98E550CE940B10FA CRC64;
     MYRDPEAASP GAPTRDVLLV SAIITVSLSV TIVLCGLCHW CQRKLGKRYK NSLETVGTPD
     SGRGRGEKKA INFEDSTLST ATTLESIPSS AGEPKCQRPR TLMRQQSLQQ PLSQNQRGRQ
     PSQPTTSWDH VVGQIRNRGL DMKSFLEGRM VVLSLVLGLS EQDDFANIPD LQNPGTQQNQ
     NAQGDKRLPA GGKAVNTAPV PGQTPHDESD RRTETRSSVS DLVNSLTSEM LMLSPGSEED
     EAHEGCSREN LGRIQFSVGY NFQESTLTVK VMKAQELPAK DFSGTSDPFV KIYLLPDKKH
     KLETKVKRKN LNPHWNETFL FEGFPYEKVV QRVLYLQVLD YDRFSRNDPI GEVSIPLNKV
     DLTQMQTFWK DLKPCSDGSG SRGELLLSLC YNPSANSIIV NIIKARNLKA MDIGGTSDPY
     VKVWLMYKDK RVEKKKTVTK KRNLNPIFNE SFAFDIPTEK LRETTIIITV MDKDKLSRND
     VIGKIYLSWK SGPGEVKHWK DMIARPRQPV AQWHQLKA
//
ID   Q8CF96_MOUSE            Unreviewed;       447 AA.
AC   Q8CF96;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 58.
DE   SubName: Full=Synaptotagmin VIIbeta;
GN   Name=Syt7; Synonyms=syt VIIbeta;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=22067076; PubMed=12071850; DOI=10.1042/BJ20011877;
RA   Fukuda M., Ogata Y., Saegusa C., Kanno E., Mikoshiba K.;
RT   "Alternative splicing isoforms of synaptotagmin VII in the mouse, rat
RT   and human.";
RL   Biochem. J. 365:173-180(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c; TISSUE=Brain;
RA   Mitsunori F.;
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB075900; BAC44832.1; -; mRNA.
DR   IPI; IPI00400053; -.
DR   RefSeq; NP_775090.1; NM_173067.3.
DR   UniGene; Mm.182654; -.
DR   HSSP; P21707; 1RSY.
DR   ProteinModelPortal; Q8CF96; -.
DR   SMR; Q8CF96; 177-446.
DR   STRING; Q8CF96; -.
DR   PRIDE; Q8CF96; -.
DR   Ensembl; ENSMUST00000076968; ENSMUSP00000076234; ENSMUSG00000024743.
DR   GeneID; 54525; -.
DR   KEGG; mmu:54525; -.
DR   UCSC; uc008gpp.1; mouse.
DR   CTD; 54525; -.
DR   MGI; MGI:1859545; Syt7.
DR   GeneTree; ENSGT00600000084008; -.
DR   HOVERGEN; HBG005010; -.
DR   OMA; RIQFSIG; -.
DR   NextBio; 311364; -.
DR   ArrayExpress; Q8CF96; -.
DR   Bgee; Q8CF96; -.
DR   Genevestigator; Q8CF96; -.
DR   GO; GO:0005764; C:lysosome; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0008021; C:synaptic vesicle; IEA:InterPro.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   GO; GO:0001778; P:plasma membrane repair; IDA:MGI.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   InterPro; IPR001565; Synaptotagmin.
DR   InterPro; IPR015427; Synaptotagmin7.
DR   PANTHER; PTHR10024:SF29; Synaptotagmin7; 1.
DR   Pfam; PF00168; C2; 2.
DR   PRINTS; PR00360; C2DOMAIN.
DR   PRINTS; PR00399; SYNAPTOTAGMN.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 2.
PE   2: Evidence at transcript level;
KW   Repeat.
SQ   SEQUENCE   447 AA;  50671 MW;  C1968D5EAAEF07B7 CRC64;
     MYRDPEAASP GAPTRDVLLV SAIITVSLSV TIVLCGLCHW CQRKLGKRYK NSLETVGTPD
     SGRGRGEKKA INDLDRDFWN NNESTVQQKW SSYPPKEFIL NISPYAPYGD PRLSLKLPAG
     GKAVNTAPVP GQTPHDESDR RTETRSSVSD LVNSLTSEML MLSPGSEEDE AHEGCSRENL
     GRIQFSVGYN FQESTLTVKV MKAQELPAKD FSGTSDPFVK IYLLPDKKHK LETKVKRKNL
     NPHWNETFLF EGFPYEKVVQ RVLYLQVLDY DRFSRNDPIG EVSIPLNKVD LTQMQTFWKD
     LKPCSDGSGS RGELLLSLCY NPSANSIIVN IIKARNLKAM DIGGTSDPYV KVWLMYKDKR
     VEKKKTVTKK RNLNPIFNES FAFDIPTEKL RETTIIITVM DKDKLSRNDV IGKIYLSWKS
     GPGEVKHWKD MIARPRQPVA QWHQLKA
//
ID   SNX8_MOUSE              Reviewed;         459 AA.
AC   Q8CFD4; Q8BLI6; Q8BUQ7;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Sorting nexin-8;
GN   Name=Snx8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-459.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: May be involved in several stages of intracellular
CC       trafficking. May play a role in intracellular protein transport
CC       from early endosomes to the trans-Golgi network (By similarity).
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane
CC       protein; Cytoplasmic side (By similarity). Note=Colocalizes with
CC       retromer components (By similarity).
CC   -!- SIMILARITY: Belongs to the sorting nexin family.
CC   -!- SIMILARITY: Contains 1 PX (phox homology) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC32202.1; Type=Erroneous initiation;
CC       Sequence=BAE28549.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; BC037599; AAH37599.1; -; mRNA.
DR   EMBL; AK045061; BAC32202.1; ALT_INIT; mRNA.
DR   EMBL; AK082871; BAC38662.1; -; mRNA.
DR   EMBL; AK148429; BAE28549.1; ALT_INIT; mRNA.
DR   IPI; IPI00319079; -.
DR   RefSeq; NP_758481.1; NM_172277.2.
DR   UniGene; Mm.27098; -.
DR   ProteinModelPortal; Q8CFD4; -.
DR   SMR; Q8CFD4; 77-173.
DR   PhosphoSite; Q8CFD4; -.
DR   PRIDE; Q8CFD4; -.
DR   Ensembl; ENSMUST00000031539; ENSMUSP00000031539; ENSMUSG00000029560.
DR   GeneID; 231834; -.
DR   KEGG; mmu:231834; -.
DR   UCSC; uc009ahq.1; mouse.
DR   CTD; 231834; -.
DR   MGI; MGI:2443816; Snx8.
DR   GeneTree; ENSGT00460000041594; -.
DR   HOGENOM; HBG314330; -.
DR   HOVERGEN; HBG017827; -.
DR   InParanoid; Q8CFD4; -.
DR   OMA; LYCLHQE; -.
DR   OrthoDB; EOG42JNRD; -.
DR   NextBio; 380783; -.
DR   ArrayExpress; Q8CFD4; -.
DR   Bgee; Q8CFD4; -.
DR   CleanEx; MM_SNX8; -.
DR   Genevestigator; Q8CFD4; -.
DR   GermOnline; ENSMUSG00000029560; Mus musculus.
DR   GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR   GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   GO; GO:0034498; P:early endosome to Golgi transport; ISS:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR   InterPro; IPR001683; Phox.
DR   Gene3D; G3DSA:3.30.1520.10; PX; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; PX; 1.
DR   PROSITE; PS50195; PX; 1.
PE   2: Evidence at transcript level;
KW   Endosome; Lipid-binding; Membrane; Phosphoprotein; Protein transport;
KW   Transport.
FT   CHAIN         1    459       Sorting nexin-8.
FT                                /FTId=PRO_0000236199.
FT   DOMAIN       68    176       PX.
FT   BINDING     104    104       Phosphatidylinositol 3-phosphate (By
FT                                similarity).
FT   BINDING     130    130       Phosphatidylinositol 3-phosphate (By
FT                                similarity).
FT   BINDING     143    143       Phosphatidylinositol 3-phosphate (By
FT                                similarity).
FT   MOD_RES     446    446       Phosphothreonine (By similarity).
FT   MOD_RES     450    450       Phosphoserine (By similarity).
FT   CONFLICT    222    222       N -> Y (in Ref. 2; BAC38662).
FT   CONFLICT    366    366       L -> V (in Ref. 2; BAC38662).
SQ   SEQUENCE   459 AA;  52059 MW;  5E0BE9C1AB054454 CRC64;
     MTGRAMDPLP SPAVAAAAEA EADEEADPPA TGPRTSQVTE WRALDPGRMQ MPQGNPLLLS
     YTLQELLAKD TVQVELIPEK KGLFLKHVEY EVSSQRFKSS VYRRYNDFVV FHEVLLHKFP
     YRMVPALPPK RVLGADREFI EGRRRALKRF INLVARHPPF SEDVLLKLFL SFSGSDVQHK
     LKEAAQCVGD EFMNCKLAAR AKDFLPADIQ TQFAMSRELI RNVYNSFYKL RDRAERIASR
     AIDNAADLLI FGKELSALGS DTTPLPSWAA LHLSTWGSLK QALKGLSVEF ALLADRAAQQ
     GKKEENDVVE KLNLFLDLLQ SYKDLCERHE KGVLHKHQRA LHKYGLMKRQ MMSAAHGREP
     ESVEQLESRI VEQENVIQTM ELRNYFSLYC LHQETQLVHV YLPLTSHILG AFVNSQIQGH
     KEMSKVWNDL KPKLSCLFAG PHSVLTPPRS PQEDGVCPH
//
ID   SCYL2_MOUSE             Reviewed;         930 AA.
AC   Q8CFE4; Q3UT57; Q3UWU9; Q8K0M4;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=SCY1-like protein 2;
DE   AltName: Full=Coated vesicle-associated kinase of 104 kDa;
GN   Name=Scyl2; Synonyms=Cvak104, D10Ertd802e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 664-930 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 817-930 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=16914521; DOI=10.1091/mbc.E06-05-0390;
RA   Duewel M., Ungewickell E.J.;
RT   "Clathrin-dependent association of CVAK104 with endosomes and the
RT   trans-Golgi network.";
RL   Mol. Biol. Cell 17:4513-4525(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Component of AP2-containing clathrin coated structures
CC       at the plasma membrane or of endocytic coated vesicles. May be a
CC       serine/threonine-protein kinase. May regulate clathrin-dependent
CC       trafficking between the TGN and/or the endosomal system (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with clathrin and AP2B1; the interaction
CC       mediates the association with the AP-2 complex (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region (By
CC       similarity). Cytoplasmic vesicle, clathrin-coated vesicle (By
CC       similarity). Golgi apparatus, trans-Golgi network membrane (By
CC       similarity). Endosome membrane (By similarity). Note=Plasma
CC       membrane-associated in clathrin-coated vesicles. Colocalizes to
CC       the trans-Golgi network (TGN) and to endosomal membranes with
CC       clathrin, transferrin and plasma membrane adapter AP1 and AP3
CC       complexes (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CFE4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CFE4-2; Sequence=VSP_020980, VSP_020981, VSP_020982;
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC   -!- SIMILARITY: Contains 1 HEAT repeat.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AK136092; BAE22815.1; -; mRNA.
DR   EMBL; AK139747; BAE24123.1; -; mRNA.
DR   EMBL; BC030932; AAH30932.1; -; mRNA.
DR   EMBL; BC042443; AAH42443.1; -; mRNA.
DR   IPI; IPI00229287; -.
DR   IPI; IPI00798571; -.
DR   RefSeq; NP_932138.1; NM_198021.2.
DR   UniGene; Mm.27651; -.
DR   ProteinModelPortal; Q8CFE4; -.
DR   SMR; Q8CFE4; 29-329.
DR   STRING; Q8CFE4; -.
DR   PhosphoSite; Q8CFE4; -.
DR   PRIDE; Q8CFE4; -.
DR   Ensembl; ENSMUST00000092227; ENSMUSP00000089874; ENSMUSG00000069539.
DR   Ensembl; ENSMUST00000105294; ENSMUSP00000100931; ENSMUSG00000069539.
DR   GeneID; 213326; -.
DR   KEGG; mmu:213326; -.
DR   UCSC; uc007gsl.1; mouse.
DR   UCSC; uc007gsm.1; mouse.
DR   CTD; 213326; -.
DR   MGI; MGI:1289172; Scyl2.
DR   eggNOG; roNOG06000; -.
DR   GeneTree; ENSGT00500000044907; -.
DR   HOGENOM; HBG446307; -.
DR   HOVERGEN; HBG055627; -.
DR   InParanoid; Q8CFE4; -.
DR   OMA; PDADQMT; -.
DR   OrthoDB; EOG4XWFX5; -.
DR   PhylomeDB; Q8CFE4; -.
DR   NextBio; 373916; -.
DR   ArrayExpress; Q8CFE4; -.
DR   Bgee; Q8CFE4; -.
DR   CleanEx; MM_SCYL2; -.
DR   Genevestigator; Q8CFE4; -.
DR   GermOnline; ENSMUSG00000069539; Mus musculus.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Cytoplasmic vesicle; Endosome;
KW   Golgi apparatus; Membrane; Phosphoprotein.
FT   CHAIN         1    930       SCY1-like protein 2.
FT                                /FTId=PRO_0000252447.
FT   DOMAIN       32    327       Protein kinase.
FT   REPEAT      443    479       HEAT.
FT   MOD_RES     350    350       Phosphoserine (By similarity).
FT   MOD_RES     438    438       Phosphothreonine (By similarity).
FT   MOD_RES     440    440       Phosphothreonine (By similarity).
FT   MOD_RES     677    677       Phosphoserine.
FT   VAR_SEQ       1    423       Missing (in isoform 2).
FT                                /FTId=VSP_020980.
FT   VAR_SEQ     424    424       Q -> M (in isoform 2).
FT                                /FTId=VSP_020981.
FT   VAR_SEQ     643    643       Missing (in isoform 2).
FT                                /FTId=VSP_020982.
SQ   SEQUENCE   930 AA;  103317 MW;  1771D113D098189E CRC64;
     MESMLNKLKS TVTKVTADVT SAVMGNPVTR EFDVGRHIAS GGNGLAWKIF NGTKKSTKQE
     VAVFVFDKKL IDKYQKFEKD QIIDSLKRGV QQLTRLRHPR LLTVQHPLEE SRDCLAFCTE
     PVFASLANVL GNWENLPSSI SPDIKDYKLY DVETKYGLLQ VSEGLSFLHS SVKMVHGNVT
     PENVILNKSG AWKIMGFDFC VSSSNPSEQE PKFPCKEWDP NLPSLCLPNP EYLAPEYILS
     VSCETASDMY SLGAVMYAVF NQGRPIFEVN KQDIYKSFSR QLDQLSRLGS SSLTSIPEEV
     REHVKLLLNV TPTVRPDADQ MTKIPFFDDV GAVTLQYFDT LFQRDNLQKS QFFKGLPKVL
     PKLPKRVIVQ RILPCLTSEF VNPDMVPFVL PNVLLIAEEC TKEEYIKLIL PELGPVFKQQ
     EPIQILLIFL QKMDLLLTKT PPDEIKNSVL PMVYRALEAP SIQIQELCLN IIPTFANLID
     YPSMKNALIP RIKNACLQTS SLAVRVNSLV CLGKILEYLD KWFVLDDILP FLQQIPSKEP
     AVLMGILGIY KCTFTHKKLG ITKEQLAGKV LPHLIPLSIE NNLNLNQFSS FIAVIKEMLS
     RLESEHRTKL EQLHVMQEQQ RSLDIGNQMS TSEETKVAHS GSQQIDKVFN NIGADLLSGS
     ESENREDGMQ GKQKRGSLTL EEKQKLAKEQ EQAQKLKSQQ PLKPQVHTPI APIKQTKDLT
     DTLMENMSSL TSLSVSTPKI SASSTFTPVP STGLGMMFST PIDNTKRNLT NGLNANMGFQ
     TSGFSMPVNP NQNFFSGTGT AGVTTMSLGA PPTMSNFSPL TIPPASVKQP QQRPTDMSAL
     NNLFGPQKPK VSMNQLSQQK PNQWLNQFAP PQGSPVMGSA AMGTQGNVMG QAAFGMQGNP
     FFNPQNFAQP PPTTMTSSSS ASNDLKDLFG
//
ID   NED4L_MOUSE             Reviewed;        1004 AA.
AC   Q8CFI0; Q8BRT9; Q8BS42; Q99PK2;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=E3 ubiquitin-protein ligase NEDD4-like;
DE            EC=6.3.2.-;
DE   AltName: Full=NEDD4.2;
DE   AltName: Full=Nedd4-2;
GN   Name=Nedd4l; Synonyms=Kiaa0439, Nedd4b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, FUNCTION,
RP   AND MUTAGENESIS OF CYS-971.
RC   STRAIN=C57BL/6;
RX   MEDLINE=21067027; PubMed=11149908; DOI=10.1096/fj.00-0191com;
RA   Kamynina E., Debonneville C., Bens M., Vandewalle A., Staub O.;
RT   "A novel mouse Nedd4 protein suppresses the activity of the epithelial
RT   Na+ channel.";
RL   FASEB J. 15:204-214(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), INTERACTION WITH
RP   SCNN1A; SCNN1B AND SCNN1G, AND FUNCTION.
RC   TISSUE=Brain;
RX   PubMed=12424229; DOI=10.1096/fj.02-0497fje;
RA   Fotia A.B., Dinudom A., Shearwin K.E., Koch J.-P., Korbmacher C.,
RA   Cook D.I., Kumar S.;
RT   "The role of individual Nedd4-2 (KIAA0439) WW domains in binding and
RT   regulating epithelial sodium channels.";
RL   FASEB J. 17:70-72(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Kidney, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 44-1004 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   FUNCTION, INTERACTION WITH SCNN1A; SCNN1B AND SCNN1G, PHOSPHORYLATION
RP   AT SER-371 AND SER-477, AND MUTAGENESIS OF SER-371 AND SER-477.
RX   PubMed=11742982; DOI=10.1093/emboj/20.24.7052;
RA   Debonneville C., Flores S.Y., Kamynina E., Plant P.J., Tauxe C.,
RA   Thomas M.A., Muenster C., Chraiebi A., Pratt J.H., Horisberger J.-D.,
RA   Pearce D., Loffing J., Staub O.;
RT   "Phosphorylation of Nedd4-2 by Sgk1 regulates epithelial Na(+) channel
RT   cell surface expression.";
RL   EMBO J. 20:7052-7059(2001).
RN   [6]
RP   FUNCTION, INTERACTION WITH SCNN1A; SCNN1B AND SCNN1G, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=11244092; DOI=10.1074/jbc.C000906200;
RA   Harvey K.F., Dinudom A., Cook D.I., Kumar S.;
RT   "The Nedd4-like protein KIAA0439 is a potential regulator of the
RT   epithelial sodium channel.";
RL   J. Biol. Chem. 276:8597-8601(2001).
RN   [7]
RP   INTERACTION WITH NDFIP2, AND SUBCELLULAR LOCATION.
RX   PubMed=12050153; DOI=10.1074/jbc.M203018200;
RA   Konstas A.-A., Shearwin-Whyatt L.M., Fotia A.B., Degger B.,
RA   Riccardi D., Cook D.I., Korbmacher C., Kumar S.;
RT   "Regulation of the epithelial sodium channel by N4WBP5A, a novel
RT   Nedd4/Nedd4-2-interacting protein.";
RL   J. Biol. Chem. 277:29406-29416(2002).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH SCN1A; SCN2A; SCN3A; SCN5A; SCN8A;
RP   SCN9A; SCN10A; SCNN1A; SCNN1B AND SCNN1G.
RX   PubMed=15123669; DOI=10.1074/jbc.M402820200;
RA   Fotia A.B., Ekberg J., Adams D.J., Cook D.I., Poronnik P., Kumar S.;
RT   "Regulation of neuronal voltage-gated sodium channels by the
RT   ubiquitin-protein ligases Nedd4 and Nedd4-2.";
RL   J. Biol. Chem. 279:28930-28935(2004).
RN   [9]
RP   INTERACTION WITH UBE2E3.
RX   PubMed=14993279; DOI=10.1128/MCB.24.6.2397-2409.2004;
RA   Debonneville C., Staub O.;
RT   "Participation of the ubiquitin-conjugating enzyme UBE2E3 in Nedd4-2-
RT   dependent regulation of the epithelial Na+ channel.";
RL   Mol. Cell. Biol. 24:2397-2409(2004).
RN   [10]
RP   PHOSPHORYLATION AT SER-477.
RX   PubMed=15958725; DOI=10.1681/ASN.2004100828;
RA   Flores S.Y., Loffing-Cueni D., Kamynina E., Daidie D., Gerbex C.,
RA   Chabanel S., Dudler J., Loffing J., Staub O.;
RT   "Aldosterone-induced serum and glucocorticoid-induced kinase 1
RT   expression is accompanied by nedd4-2 phosphorylation and increased na+
RT   transport in cortical collecting duct cells.";
RL   J. Am. Soc. Nephrol. 16:2279-2287(2005).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-331; SER-477; SER-508
RP   AND SER-512, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [13]
RP   STRUCTURE BY NMR OF 221-254; 414-447 AND 525-560.
RA   Kowalski K., Merkel A.L., Booker G.W.;
RT   "Solution structures of WW domains of NEDD4-2.";
RL   Submitted (OCT-2005) to the PDB data bank.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from
CC       an E2 ubiquitin-conjugating enzyme in the form of a thioester and
CC       then directly transfers the ubiquitin to targeted substrates.
CC       Inhibits TGF-beta signaling by triggering SMAD2 and TGFR1
CC       ubiquitination and proteasome-dependent degradation. Promotes
CC       ubiquitination and internalization of various plasma membrane
CC       channels such as ENaC, Nav1.2, Nav1.3, Nav1.5, Nav1.7, Nav1.8,
CC       Kv1.3, EAAT1 or CLC5. Promotes ubiquitination and degradation of
CC       SGK.
CC   -!- ENZYME REGULATION: Activated by NDFIP1- and NDFIP2-binding (By
CC       similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with SMAD2, SMAD3, SMAD6 and SMAD7. Interacts
CC       with CLCN5. The phosphorylated form interacts with 14-3-3
CC       proteins. Interacts with NDIF1P in vitro (By similarity).
CC       Interacts via its WW domains with SCNN1A, SCNN1B, SCNN1G, SCN1A,
CC       SCN2A, SCN3A, SCN5A, SCN8A, SCN9A and SCN10A. Interacts with
CC       UBE2E3. Interacts with NDFIP1 and NDFIP2; this interaction
CC       activates the E3 ubiquitin-protein ligase (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8CFI0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CFI0-2; Sequence=VSP_015450;
CC       Name=3;
CC         IsoId=Q8CFI0-3; Sequence=VSP_015453;
CC   -!- TISSUE SPECIFICITY: Highly expressed in liver and kidney. Also
CC       expressed in heart, brain and lung. Isoform 1 is expressed in
CC       kidney, lung and gut. Isoform 3 is ubiquitously expressed.
CC   -!- PTM: Phosphorylated; which impairs interaction with SCNN.
CC       Interaction with YWHAH inhibits dephosphorylation (By similarity).
CC       Aldosterone induces Ser-477 phosphorylation by SGK.
CC   -!- PTM: Auto-ubiquitinated (By similarity).
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 HECT (E6AP-type E3 ubiquitin-protein
CC       ligase) domain.
CC   -!- SIMILARITY: Contains 4 WW domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC31307.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF277232; AAK00809.1; -; mRNA.
DR   EMBL; BC039746; AAH39746.1; -; mRNA.
DR   EMBL; BC071210; AAH71210.1; -; mRNA.
DR   EMBL; AK042621; BAC31307.1; ALT_INIT; mRNA.
DR   IPI; IPI00404545; -.
DR   IPI; IPI00469332; -.
DR   IPI; IPI00649115; -.
DR   UniGene; Mm.98668; -.
DR   PDB; 1WR3; NMR; -; A=221-254.
DR   PDB; 1WR4; NMR; -; A=414-447.
DR   PDB; 1WR7; NMR; -; A=525-560.
DR   PDBsum; 1WR3; -.
DR   PDBsum; 1WR4; -.
DR   PDBsum; 1WR7; -.
DR   ProteinModelPortal; Q8CFI0; -.
DR   SMR; Q8CFI0; 40-182, 221-254, 413-447, 523-617, 625-999.
DR   STRING; Q8CFI0; -.
DR   TCDB; 8.A.30.1.1; Nedd4-family interacting protein-2 (Nedd4) family.
DR   PhosphoSite; Q8CFI0; -.
DR   PRIDE; Q8CFI0; -.
DR   Ensembl; ENSMUST00000025485; ENSMUSP00000025485; ENSMUSG00000024589.
DR   Ensembl; ENSMUST00000080418; ENSMUSP00000079280; ENSMUSG00000024589.
DR   UCSC; uc008fer.1; mouse.
DR   MGI; MGI:1933754; Nedd4l.
DR   GeneTree; ENSGT00570000078756; -.
DR   HOGENOM; HBG607874; -.
DR   HOVERGEN; HBG004134; -.
DR   InParanoid; Q8CFI0; -.
DR   OMA; PSLMDVS; -.
DR   OrthoDB; EOG4QRH3C; -.
DR   PhylomeDB; Q8CFI0; -.
DR   ArrayExpress; Q8CFI0; -.
DR   Bgee; Q8CFI0; -.
DR   Genevestigator; Q8CFI0; -.
DR   GermOnline; ENSMUSG00000024589; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IDA:MGI.
DR   GO; GO:0010766; P:negative regulation of sodium ion transport; IDA:MGI.
DR   GO; GO:0006464; P:protein modification process; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   InterPro; IPR000569; HECT.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00397; WW; 4.
DR   PRINTS; PR00360; C2DOMAIN.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00456; WW; 4.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF56204; HECT; 1.
DR   SUPFAM; SSF51045; WW_Rsp5_WWP; 4.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 4.
DR   PROSITE; PS50020; WW_DOMAIN_2; 4.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Ligase; Phosphoprotein;
KW   Repeat; Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN         1   1004       E3 ubiquitin-protein ligase NEDD4-like.
FT                                /FTId=PRO_0000120324.
FT   DOMAIN       35    137       C2.
FT   DOMAIN      221    254       WW 1.
FT   DOMAIN      414    447       WW 2.
FT   DOMAIN      526    559       WW 3.
FT   DOMAIN      577    610       WW 4.
FT   DOMAIN      669   1003       HECT.
FT   COMPBIAS    321    324       Poly-Pro.
FT   ACT_SITE    971    971       Glycyl thioester intermediate.
FT   MOD_RES     331    331       Phosphothreonine.
FT   MOD_RES     332    332       Phosphoserine (By similarity).
FT   MOD_RES     347    347       Phosphothreonine (By similarity).
FT   MOD_RES     371    371       Phosphoserine.
FT   MOD_RES     396    396       Phosphothreonine (By similarity).
FT   MOD_RES     475    475       Phosphoserine.
FT   MOD_RES     477    477       Phosphoserine; by SGK.
FT   MOD_RES     478    478       Phosphoserine (By similarity).
FT   MOD_RES     493    493       Phosphoserine (By similarity).
FT   MOD_RES     508    508       Phosphoserine.
FT   MOD_RES     512    512       Phosphoserine.
FT   MOD_RES     516    516       Phosphoserine (By similarity).
FT   VAR_SEQ       1    149       Missing (in isoform 2).
FT                                /FTId=VSP_015450.
FT   VAR_SEQ     385    404       Missing (in isoform 3).
FT                                /FTId=VSP_015453.
FT   MUTAGEN     371    371       S->A: Weakly reduces phosphorylation by
FT                                SGK.
FT   MUTAGEN     477    477       S->A: Strongly reduces phosphorylation by
FT                                SGK.
FT   MUTAGEN     971    971       C->S: Abolishes catalytic activity.
FT   CONFLICT    179    179       A -> G (in Ref. 1; AAK00809).
FT   CONFLICT    390    390       R -> G (in Ref. 1; AAK00809).
FT   CONFLICT    403    403       P -> S (in Ref. 1; AAK00809).
FT   CONFLICT    585    585       E -> G (in Ref. 1; AAK00809).
FT   CONFLICT    832    832       N -> T (in Ref. 1; AAK00809).
FT   CONFLICT    847    847       N -> D (in Ref. 1; AAK00809).
FT   CONFLICT    949    949       N -> K (in Ref. 4; BAC31307).
FT   STRAND      227    231
FT   STRAND      233    235
FT   STRAND      237    241
FT   TURN        242    244
FT   STRAND      247    250
FT   STRAND      532    536
FT   STRAND      542    546
FT   TURN        547    550
FT   STRAND      551    555
FT   HELIX       557    559
SQ   SEQUENCE   1004 AA;  115419 MW;  50CBB3436052AA60 CRC64;
     MSLCEAPVHV GDKELKYFQI PQMLSQLSLL ASHHSRGLEF SGGQGESRIL RVKVVSGIDL
     AKKDIFGASD PYVKLSLYVA DENRELALVQ TKTIKKTLNP KWNEEFYFRV NPSNHRLLFE
     VFDENRLTRD DFLGQVDVPL SHLPTEDPTM ERPYTFKDFL LRPRSHKSRV KGFLRLKMAY
     MPKNGGQDEE NSEQRDDMEH GWEVVDSNDS ASQHQEELPP PPLPPGWEEK VDNLGRTYYV
     NHNNRSTQWH RPSLMDVSSE SDNNIRQINQ EAAHRRFRSR RHISEDLEPE ASEGGGEGPE
     PWETISEEMN MAGDSLSLAL PPPPASPVSR TSPQELSEEV SRRLQITPDS NGEQFSSLIQ
     REPSSRLRSC SVTDTVAEQA HLPPPSTPTR RARSSTVTGG EEPTPSVAYV HTTPGLPSGW
     EERKDAKGRT YYVNHNNRTT TWTRPIMQLA EDGASGSATN SNNHLVEPQI RRPRSLSSPT
     VTLSAPLEGA KDSPIRRAVK DTLSNPQSPQ PSPYNSPKPQ HKVTQSFLPP GWEMRIAPNG
     RPFFIDHNTK TTTWEDPRLK FPVHMRSKAS LNPNDLGPLP PGWEERIHLD GRTFYIDHNS
     KITQWEDPRL QNPAITGPAV PYSREFKQKY DYFRKKLKKP ADIPNRFEMK LHRNNIFEES
     YRRIMSVKRP DVLKARLWIE FESEKGLDYG GVAREWFFLL SKEMFNPYYG LFEYSATDNY
     TLQINPNSGL CNEDHLSYFT FIGRVAGLAV FHGKLLDGFF IRPFYKMMLG KQITLNDMES
     VDSEYYNSLK WILENDPTEL DLMFCIDEEN FGQTYQVDLK PNGSEIMVTN ENKREYIDLV
     IQWRFVNRVQ KQMNAFLEGF TELLPIDLIK IFDENELELL MCGLGDVDVN DWRQHSIYKN
     GYCPNHPVIQ WFWKAVLLMD AEKRIRLLQF VTGTSRVPMN GFAELYGSNG PQLFTIEQWG
     SPEKLPRAHT CFNRLDLPPY ETFEDLREKL LMAVENAQGF EGVD
//
ID   WDR24_MOUSE             Reviewed;         790 AA.
AC   Q8CFJ9;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=WD repeat-containing protein 24;
GN   Name=Wdr24;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the WD repeat WDR24 family.
CC   -!- SIMILARITY: Contains 6 WD repeats.
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DR   EMBL; BC037651; AAH37651.1; -; mRNA.
DR   IPI; IPI00229321; -.
DR   RefSeq; NP_776102.1; NM_173741.3.
DR   UniGene; Mm.95512; -.
DR   ProteinModelPortal; Q8CFJ9; -.
DR   SMR; Q8CFJ9; 26-350, 740-786.
DR   PhosphoSite; Q8CFJ9; -.
DR   PRIDE; Q8CFJ9; -.
DR   Ensembl; ENSMUST00000026833; ENSMUSP00000026833; ENSMUSG00000025737.
DR   GeneID; 268933; -.
DR   KEGG; mmu:268933; -.
DR   UCSC; uc008bcd.1; mouse.
DR   CTD; 268933; -.
DR   MGI; MGI:2446285; Wdr24.
DR   eggNOG; roNOG04664; -.
DR   GeneTree; ENSGT00600000084542; -.
DR   HOGENOM; HBG315730; -.
DR   HOVERGEN; HBG080644; -.
DR   InParanoid; Q8CFJ9; -.
DR   OMA; SWFVDTA; -.
DR   OrthoDB; EOG48WC1D; -.
DR   PhylomeDB; Q8CFJ9; -.
DR   NextBio; 392587; -.
DR   ArrayExpress; Q8CFJ9; -.
DR   Bgee; Q8CFJ9; -.
DR   CleanEx; MM_WDR24; -.
DR   Genevestigator; Q8CFJ9; -.
DR   GermOnline; ENSMUSG00000025737; Mus musculus.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 4.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 3.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Repeat; WD repeat.
FT   CHAIN         1    790       WD repeat-containing protein 24.
FT                                /FTId=PRO_0000051376.
FT   REPEAT       72    112       WD 1.
FT   REPEAT      118    158       WD 2.
FT   REPEAT      161    201       WD 3.
FT   REPEAT      205    245       WD 4.
FT   REPEAT      249    291       WD 5.
FT   REPEAT      295    338       WD 6.
FT   MOD_RES     594    594       Phosphoserine (By similarity).
SQ   SEQUENCE   790 AA;  88184 MW;  AF4A5E490357D57D CRC64;
     MEKMSRVSTA LSGSALTGRT MHCHLDAPAN AISVCRDAAQ VVVAGRSIFK IYAIEEEQFV
     EKLNLRVGRK PSLNLSCADV VWHQMDENLL ATAATNGVVV TWNLGRPSRN KQDQLFTEHK
     RTVNKVCFHP TEAHVLLSGS QDGFMKCFDL RRKDSVSTFS GQSESVRDVQ FSIRDYFTFA
     STFENGNVQL WDIRRPDRCE RMFTAHNGPV FCCDWHPEDR GWLATGGRDK MVKVWDMTTH
     RAKEIHCVQT IASVARVKWR PECRHHLATC SMMVDHNIYV WDVRRPFVPA AMFEEHRDVT
     TGIAWRHPHD PSFLLSGSKD STLCQHLFRD ASQPVERANP EGLCYGLFGD LAFAVKESLV
     AAESGRKPYA GDRRHPIFFK RKLDPAEPFS GLASSALSVF ETESSGGSMS WFVDTAERYV
     LAGRPLAELC DHNAKVAREL GRNQVAQTWT MLRIIYCSPG LVSSANLNHS VGKGSSCGLP
     LMNSFNLKDM GPGLGSETRL DRSKGDTRSD AALLDSSATL VTNEDNEETE GSDVPADYLL
     GDVEGEDDEL YPLDTEHVHS EEPEYVLPQE AFPLRHEIVD TPSGPEHLQD KADSPHVSGN
     EADTASLAPV DSSSSLLSVS HALYDSRLPP DFFSVLVRDM LRFYAEQGDV QMAVSVLIVL
     GERVRKDIDE QTQEHWYTSY IDLLQRFCLW NVSNEVVKLS TSRAVSCLNQ ASTTLHVNCS
     HCKRPMSSRG WVCDRCHRCA SMCAVCHHVV KGLFVWCQGC SHGGHLQHIM KWLEGSSHCP
     AGCGHLCEYS
//
ID   MEF2C_MOUSE             Reviewed;         474 AA.
AC   Q8CFN5; Q8R0H1; Q9D7L0; Q9QW20;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Myocyte-specific enhancer factor 2C;
GN   Name=Mef2c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX   MEDLINE=93281742; PubMed=8506376; DOI=10.1073/pnas.90.11.5282;
RA   Martin J.F., Schwarz J.J., Olson E.N.;
RT   "Myocyte enhancer factor (MEF) 2C: a tissue-restricted member of the
RT   MEF-2 family of transcription factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:5282-5286(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=97165895; PubMed=9013788; DOI=10.1016/S0169-328X(96)00135-0;
RA   Lin X., Shah S., Bulleit R.F.;
RT   "The expression of MEF2 genes is implicated in CNS neuronal
RT   differentiation.";
RL   Brain Res. Mol. Brain Res. 42:307-316(1996).
RN   [5]
RP   PHOSPHORYLATION AT SER-59, AND MUTAGENESIS OF SER-59.
RX   PubMed=8663403; DOI=10.1074/jbc.271.29.17199;
RA   Molkentin J.D., Li L., Olson E.N.;
RT   "Phosphorylation of the MADS-Box transcription factor MEF2C enhances
RT   its DNA binding activity.";
RL   J. Biol. Chem. 271:17199-17204(1996).
RN   [6]
RP   FUNCTION.
RX   PubMed=9162005; DOI=10.1126/science.276.5317.1404;
RA   Lin Q., Schwarz J., Bucana C., Olson E.N.;
RT   "Control of mouse cardiac morphogenesis and myogenesis by
RT   transcription factor MEF2C.";
RL   Science 276:1404-1407(1997).
RN   [7]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=9778514;
RA   Lin Q., Lu J., Yanagisawa H., Webb R., Lyons G.E., Richardson J.A.,
RA   Olson E.N.;
RT   "Requirement of the MADS-box transcription factor MEF2C for vascular
RT   development.";
RL   Development 125:4565-4574(1998).
RN   [8]
RP   INTERACTION WITH HDAC7.
RX   MEDLINE=21264450; PubMed=11279209; DOI=10.1074/jbc.M101508200;
RA   Dressel U., Bailey P.J., Wang S.-C.M., Downes M., Evans R.M.,
RA   Muscat G.E.O.;
RT   "A dynamic role for HDAC7 in MEF2-mediated muscle differentiation.";
RL   J. Biol. Chem. 276:17007-17013(2001).
RN   [9]
RP   INTERACTION WITH CARM1.
RX   PubMed=11713257; DOI=10.1074/jbc.M109835200;
RA   Chen S.L., Loffler K.A., Chen D., Stallcup M.R., Muscat G.E.;
RT   "The coactivator-associated arginine methyltransferase is necessary
RT   for muscle differentiation: CARM1 coactivates myocyte enhancer factor-
RT   2.";
RL   J. Biol. Chem. 277:4324-4333(2002).
RN   [10]
RP   TISSUE SPECIFICITY OF ISOFORMS.
RX   PubMed=15340086; DOI=10.1128/MCB.24.18.8264-8275.2004;
RA   Zhu B., Gulick T.;
RT   "Phosphorylation and alternative pre-mRNA splicing converge to
RT   regulate myocyte enhancer factor 2C activity.";
RL   Mol. Cell. Biol. 24:8264-8275(2004).
RN   [11]
RP   TISSUE SPECIFICITY OF ISOFORMS.
RX   PubMed=15834131; DOI=10.1074/jbc.M502491200;
RA   Zhu B., Ramachandran B., Gulick T.;
RT   "Alternative pre-mRNA splicing governs expression of a conserved
RT   acidic transactivation domain in myocyte enhancer factor 2 factors of
RT   striated muscle and brain.";
RL   J. Biol. Chem. 280:28749-28760(2005).
RN   [12]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=18438409; DOI=10.1038/ni.1609;
RA   Wilker P.R., Kohyama M., Sandau M.M., Albring J.C., Nakagawa O.,
RA   Schwarz J.J., Murphy K.M.;
RT   "Transcription factor Mef2c is required for B cell proliferation and
RT   survival after antigen receptor stimulation.";
RL   Nat. Immunol. 9:603-612(2008).
RN   [13]
RP   ACETYLATION AT LYS-4, DNA-BINDING, MASS SPECTROMETRY, FUNCTION, AND
RP   MUTAGENESIS OF ARG-3 AND LYS-4.
RX   PubMed=18086704; DOI=10.1093/nar/gkm1114;
RA   Angelelli C., Magli A., Ferrari D., Ganassi M., Matafora V.,
RA   Parise F., Razzini G., Bachi A., Ferrari S., Molinari S.;
RT   "Differentiation-dependent lysine 4 acetylation enhances MEF2C binding
RT   to DNA in skeletal muscle cells.";
RL   Nucleic Acids Res. 36:915-928(2008).
RN   [14]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=18599438; DOI=10.1073/pnas.0802679105;
RA   Barbosa A.C., Kim M.S., Ertunc M., Adachi M., Nelson E.D.,
RA   McAnally J., Richardson J.A., Kavalali E.T., Monteggia L.M.,
RA   Bassel-Duby R., Olson E.N.;
RT   "MEF2C, a transcription factor that facilitates learning and memory by
RT   negative regulation of synapse numbers and function.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:9391-9396(2008).
RN   [15]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18599437; DOI=10.1073/pnas.0802876105;
RA   Li H., Radford J.C., Ragusa M.J., Shea K.L., McKercher S.R.,
RA   Zaremba J.D., Soussou W., Nie Z., Kang Y.J., Nakanishi N., Okamoto S.,
RA   Roberts A.J., Schwarz J.J., Lipton S.A.;
RT   "Transcription factor MEF2C influences neural stem/progenitor cell
RT   differentiation and maturation in vivo.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:9397-9402(2008).
RN   [16]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19211936; DOI=10.1182/blood-2008-07-167577;
RA   Gekas C., Rhodes K.E., Gereige L.M., Helgadottir H., Ferrari R.,
RA   Kurdistani S.K., Montecino-Rodriguez E., Bassel-Duby R., Olson E.,
RA   Krivtsov A.V., Armstrong S., Orkin S.H., Pellegrini M., Mikkola H.K.;
RT   "Mef2C is a lineage-restricted target of Scl/Tal1 and regulates
RT   megakaryopoiesis and B-cell homeostasis.";
RL   Blood 113:3461-3471(2009).
RN   [17]
RP   INTERACTION WITH LIPN1.
RX   PubMed=19753306; DOI=10.1371/journal.pone.0007031;
RA   Liu G.H., Gerace L.;
RT   "Sumoylation regulates nuclear localization of lipin-1alpha in
RT   neuronal cells.";
RL   PLoS ONE 4:E7031-E7031(2009).
CC   -!- FUNCTION: Transcription activator which binds specifically to the
CC       MEF2 element present in the regulatory regions of many muscle-
CC       specific genes. Controls cardiac morphogenesis and myogenesis, and
CC       is also involved in vascular development. May also be involved in
CC       neurogenesis and in the development of cortical architecture.
CC       Isoform 3 and isoform 4, which lack the repressor domain, are more
CC       active than isoform 1, isoform 2 and isoform 5 (By similarity).
CC       Plays an essential role in hippocampal-dependent learning and
CC       memory by suppressing the number of excitatory synapses and thus
CC       regulating basal and evoked synaptic transmission. Crucial for
CC       normal neuronal development, distribution, and electrical activity
CC       in the neocortex. Necessary for proper development of
CC       megakaryocytes and platelets and for bone marrow B lymphopoiesis.
CC       Required for B-cell survival and proliferation in response to BCR
CC       stimulation, efficient IgG1 antibody responses to T-cell-dependent
CC       antigens and for normal induction of germinal center B cells.
CC   -!- SUBUNIT: Forms a complex with class II HDACs in undifferentiating
CC       cells. On myogenic differentiation, HDACs are released into the
CC       cytoplasm allowing MEF2s to interact with other proteins for
CC       activation. Interacts with EP300 in differentiating cells; the
CC       interaction acetylates MEF2C leading to increased DNA binding and
CC       activation. Interacts with HDAC7 and CARM1 (By similarity).
CC       Interacts with HDAC4, HDAC7 AND HDAC9; the interaction WITH HDACs
CC       represses transcriptional activity. Interacts with LPIN1.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1;
CC         IsoId=Q8CFN5-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q8CFN5-2; Sequence=VSP_012504;
CC       Name=3;
CC         IsoId=Q8CFN5-3; Sequence=VSP_012505;
CC       Name=4;
CC         IsoId=Q8CFN5-4; Sequence=VSP_012501, VSP_012502, VSP_012503,
CC                                  VSP_012504, VSP_012505;
CC       Name=5;
CC         IsoId=Q8CFN5-5; Sequence=VSP_012501, VSP_012502, VSP_012503;
CC   -!- TISSUE SPECIFICITY: Widely expressed though mainly restricted to
CC       skeletal and cardiac muscle, brain, neurons and lymphocytes. Beta
CC       beta domain-lacking isoforms are the most predominantly expressed
CC       in all tissues including skeletal and cardiac muscle and brain.
CC       Only brain expresses all isoforms. Expression occurs primarily in
CC       the internal granule cell layer of the olfactory bulb, cortex,
CC       thalamus, hippocampus and cerebellum. Low levels in the cerebellum
CC       and hindbrain. Expressed throughout the cortex, including the
CC       frontal and entorhinal cortex, dentate gyrus, and basolateral
CC       amygdala. Selectively expressed in B-cells but not in T-cells, and
CC       its expression increases as B-cells mature.
CC   -!- DEVELOPMENTAL STAGE: Expressed in developing endothelial cells and
CC       smooth muscle cells, as well as in surrounding mesenchyme, during
CC       embryogenesis. Up-regulated during myogenesis.
CC   -!- DOMAIN: The beta domain, missing in a number of isoforms, is
CC       required for enhancement of transcriptional activity (By
CC       similarity).
CC   -!- PTM: Phosphorylation on Ser-59 enhances DNA binding activity (By
CC       similarity). Phosphorylation on Ser-396 is required for Lys-391
CC       sumoylation and inhibits transcriptional activity.
CC   -!- PTM: Acetylated by p300 on several sites in diffentiating myocytes
CC       (By similarity). Acetylation on Lys-4 increases DNA binding and
CC       transactivation.
CC   -!- PTM: Sumoylated on Lys-391 by SUMO2 but not by SUMO1 represses
CC       transcriptional activity (By similarity).
CC   -!- PTM: Proteolytically cleaved in cerebellar granule neurons,
CC       probably by caspase 7, following neurotoxicity. Preferentially
CC       cleaves the CDK5-mediated hyperphosphorylated form which leads to
CC       neuron apoptosis and transcriptional inactivation (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice show impairment in hippocampal-
CC       dependent learning and also increase in the number of excitatory
CC       synapses and potentiation of basal and evoked synaptic
CC       transmission. Mice surviving to adulthood manifest smaller,
CC       apparently less mature neurons and smaller whole brain size, with
CC       resultant aberrant electrophysiology and behavior. Mice exhibit
CC       thrombocytopenia and a defect in B-lymphopoiesis.
CC   -!- SIMILARITY: Belongs to the MEF2 family.
CC   -!- SIMILARITY: Contains 1 MADS-box domain.
CC   -!- SIMILARITY: Contains 1 Mef2-type DNA-binding domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK009139; BAB26099.1; -; mRNA.
DR   EMBL; BC026841; AAH26841.1; -; mRNA.
DR   EMBL; BC037731; AAH37731.1; -; mRNA.
DR   EMBL; BC057650; AAH57650.1; -; mRNA.
DR   IPI; IPI00153197; -.
DR   IPI; IPI00318314; -.
DR   IPI; IPI00408591; -.
DR   IPI; IPI00515347; -.
DR   IPI; IPI00515421; -.
DR   RefSeq; NP_079558.1; NM_025282.3.
DR   UniGene; Mm.24001; -.
DR   UniGene; Mm.451574; -.
DR   ProteinModelPortal; Q8CFN5; -.
DR   SMR; Q8CFN5; 2-73.
DR   IntAct; Q8CFN5; 16.
DR   PhosphoSite; Q8CFN5; -.
DR   PRIDE; Q8CFN5; -.
DR   Ensembl; ENSMUST00000005722; ENSMUSP00000005722; ENSMUSG00000005583.
DR   Ensembl; ENSMUST00000109560; ENSMUSP00000105188; ENSMUSG00000005583.
DR   GeneID; 17260; -.
DR   KEGG; mmu:17260; -.
DR   UCSC; uc007rie.1; mouse.
DR   UCSC; uc007rih.1; mouse.
DR   UCSC; uc007rii.1; mouse.
DR   UCSC; uc007rik.1; mouse.
DR   CTD; 17260; -.
DR   MGI; MGI:99458; Mef2c.
DR   GeneTree; ENSGT00390000011828; -.
DR   HOVERGEN; HBG053944; -.
DR   OMA; SLHIKSE; -.
DR   OrthoDB; EOG4DFPNH; -.
DR   NextBio; 291752; -.
DR   Bgee; Q8CFN5; -.
DR   CleanEx; MM_MEF2C; -.
DR   Genevestigator; Q8CFN5; -.
DR   GO; GO:0005634; C:nucleus; IC:MGI.
DR   GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
DR   GO; GO:0010843; F:promoter binding; IDA:BHF-UCL.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0016563; F:transcription activator activity; IDA:MGI.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0042100; P:B cell proliferation; IMP:UniProtKB.
DR   GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR   GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
DR   GO; GO:0035051; P:cardiac cell differentiation; IGI:MGI.
DR   GO; GO:0003211; P:cardiac ventricle formation; IGI:MGI.
DR   GO; GO:0002062; P:chondrocyte differentiation; IGI:MGI.
DR   GO; GO:0001958; P:endochondral ossification; IGI:MGI.
DR   GO; GO:0007611; P:learning or memory; IMP:UniProtKB.
DR   GO; GO:0007521; P:muscle cell fate determination; IMP:MGI.
DR   GO; GO:0048666; P:neuron development; IMP:UniProtKB.
DR   GO; GO:0001649; P:osteoblast differentiation; IGI:MGI.
DR   GO; GO:0003151; P:outflow tract morphogenesis; IGI:MGI.
DR   GO; GO:0090073; P:positive regulation of protein homodimerization activity; IDA:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0002634; P:regulation of germinal center formation; IMP:UniProtKB.
DR   GO; GO:0045652; P:regulation of megakaryocyte differentiation; IMP:UniProtKB.
DR   GO; GO:0060025; P:regulation of synaptic activity; IMP:UniProtKB.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IMP:MGI.
DR   GO; GO:0051145; P:smooth muscle cell differentiation; IMP:MGI.
DR   InterPro; IPR022102; HJURP_C.
DR   InterPro; IPR002100; TF_MADSbox.
DR   Pfam; PF12347; HJURP_C; 1.
DR   Pfam; PF00319; SRF-TF; 1.
DR   PRINTS; PR00404; MADSDOMAIN.
DR   SMART; SM00432; MADS; 1.
DR   SUPFAM; SSF55455; TF_MADSbox; 1.
DR   PROSITE; PS00350; MADS_BOX_1; 1.
DR   PROSITE; PS50066; MADS_BOX_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Alternative splicing; Apoptosis;
KW   Developmental protein; Differentiation; DNA-binding; Isopeptide bond;
KW   Neurogenesis; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN         1    474       Myocyte-specific enhancer factor 2C.
FT                                /FTId=PRO_0000199434.
FT   DOMAIN        3     57       MADS-box.
FT   DNA_BIND     58     86       Mef2-type (Potential).
FT   REGION      271    278       Beta domain (By similarity).
FT   REGION      368    399       Transcription repressor (By similarity).
FT   COMPBIAS      4     31       Lys-rich (basic).
FT   COMPBIAS    146    183       Ser-rich.
FT   SITE        433    434       Cleavage (Probable).
FT   MOD_RES       4      4       N6-acetyllysine.
FT   MOD_RES      59     59       Phosphoserine; by CK2.
FT   MOD_RES     116    116       N6-acetyllysine (By similarity).
FT   MOD_RES     119    119       N6-acetyllysine (By similarity).
FT   MOD_RES     234    234       N6-acetyllysine (By similarity).
FT   MOD_RES     239    239       N6-acetyllysine (By similarity).
FT   MOD_RES     252    252       N6-acetyllysine (By similarity).
FT   MOD_RES     264    264       N6-acetyllysine (By similarity).
FT   MOD_RES     293    293       Phosphothreonine; by MAPK14 (By
FT                                similarity).
FT   MOD_RES     300    300       Phosphothreonine; by MAPK14 (By
FT                                similarity).
FT   MOD_RES     396    396       Phosphoserine; by CDK5 (By similarity).
FT   MOD_RES     420    420       Phosphoserine; by MAPK7.
FT   CROSSLNK    391    391       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   VAR_SEQ      87     97       TLRKKGLNGCD -> ALNKKENKGSE (in isoform 4
FT                                and isoform 5).
FT                                /FTId=VSP_012501.
FT   VAR_SEQ     103    118       ADDSVGHSPESEDKYR -> SSYALTPRTEEKYK (in
FT                                isoform 4 and isoform 5).
FT                                /FTId=VSP_012502.
FT   VAR_SEQ     123    134       DIDLMISRQRLC -> EFDNMIKSHKIP (in isoform
FT                                4 and isoform 5).
FT                                /FTId=VSP_012503.
FT   VAR_SEQ     271    278       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_012504.
FT   VAR_SEQ     368    399       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_012505.
FT   MUTAGEN       3      3       R->T: Increased mobility in
FT                                differentiating cells. Greatly reduced
FT                                DNA binding.
FT   MUTAGEN       4      4       K->Q: 7-fold increase in DNA binding.
FT   MUTAGEN       4      4       K->R: Reduced acetylation by 30%. Some
FT                                loss of DNA binding and transactivation
FT                                activity.
FT   MUTAGEN      59     60       ST->CR: Reduced DNA binding activity.
FT   MUTAGEN      59     60       ST->DD: Enhanced DNA binding activity.
FT   MUTAGEN      59     59       S->A: Reduced DNA binding activity.
FT   MUTAGEN      59     59       S->D: Enhanced DNA binding activity.
FT   CONFLICT    141    141       F -> L (in Ref. 3; AAH37731).
FT   CONFLICT    211    211       S -> P (in Ref. 1).
FT   CONFLICT    428    428       C -> S (in Ref. 1).
SQ   SEQUENCE   474 AA;  51278 MW;  CEFC2DB21E89632A CRC64;
     MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS TNKLFQYAST
     DMDKVLLKYT EYNEPHESRT NSDIVETLRK KGLNGCDSPD PDADDSVGHS PESEDKYRKI
     NEDIDLMISR QRLCAVPPPS FEMPVTIPVS SHNSLVYSNP VSTLGNPNLL PLAHPSLQRN
     SMSPGVTHRP PSAGNTGGLM GGDLTSGAGT SAGNGYGNPR NSPGLLVSPG NLNKNIQAKS
     PPPMNLGMNN RKPDLRVLIP PGSKNTMPSV SEDVDLLLNQ RINNSQSAQS LATPVVSVAT
     PTLPGQGMGG YPSAISTTYG TEYSLSSADL SSLSGFNTAS ALHLGSVTGW QQQHLHNMPP
     SALSQLGACT STHLSQSSNL SLPSTQSLSI KSEPVSPPRD RTTTPSRYPQ HTTRHEAGRS
     PVDSLSSCSS SYDGSDREDH RNEFHSPIGL TRPSPDERES PSVKRMRLSE GWAT
//
ID   SHF_MOUSE               Reviewed;         238 AA.
AC   Q8CG80; A2AQ90; A2AQ91;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=SH2 domain-containing adapter protein F;
GN   Name=Shf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-64, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Adapter protein which may play a role in the regulation
CC       of apoptosis in response to PDGF (By similarity).
CC   -!- SUBUNIT: Interacts with phosphorylated 'Tyr-720' of PDGFRA via its
CC       SH2 domain (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1;
CC         IsoId=Q8CG80-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q8CG80-2; Sequence=VSP_052700;
CC         Note=No experimental confirmation available;
CC   -!- PTM: May become phosphorylated upon binding to PDGFRA (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 SH2 domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL844566; CAM16329.1; -; Genomic_DNA.
DR   EMBL; AL844566; CAM16330.1; -; Genomic_DNA.
DR   EMBL; BC042839; AAH42839.1; -; mRNA.
DR   IPI; IPI00756557; -.
DR   IPI; IPI00776284; -.
DR   RefSeq; NP_001013851.2; NM_001013829.2.
DR   UniGene; Mm.458215; -.
DR   HSSP; P16333; 2CI8.
DR   ProteinModelPortal; Q8CG80; -.
DR   SMR; Q8CG80; 135-233.
DR   STRING; Q8CG80; -.
DR   PhosphoSite; Q8CG80; -.
DR   Ensembl; ENSMUST00000048635; ENSMUSP00000045135; ENSMUSG00000033256.
DR   Ensembl; ENSMUST00000110530; ENSMUSP00000106159; ENSMUSG00000033256.
DR   GeneID; 435684; -.
DR   KEGG; mmu:435684; -.
DR   UCSC; uc008mar.1; mouse.
DR   CTD; 435684; -.
DR   MGI; MGI:3613669; Shf.
DR   GeneTree; ENSGT00390000015203; -.
DR   HOVERGEN; HBG066172; -.
DR   OrthoDB; EOG4RR6JD; -.
DR   PhylomeDB; Q8CG80; -.
DR   NextBio; 410234; -.
DR   ArrayExpress; Q8CG80; -.
DR   Bgee; Q8CG80; -.
DR   CleanEx; MM_SHF; -.
DR   Genevestigator; Q8CG80; -.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   InterPro; IPR000980; SH2.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   SMART; SM00252; SH2; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Phosphoprotein; SH2 domain.
FT   CHAIN         1    238       SH2 domain-containing adapter protein F.
FT                                /FTId=PRO_0000322559.
FT   DOMAIN      138    233       SH2.
FT   MOD_RES      64     64       Phosphotyrosine.
FT   VAR_SEQ       1     11       MEPYEAQKMMA -> MQKHR (in isoform 2).
FT                                /FTId=VSP_052700.
FT   CONFLICT     87     87       E -> EK (in Ref. 2; AAH42839).
SQ   SEQUENCE   238 AA;  26893 MW;  9484D44D689C9ECB CRC64;
     MEPYEAQKMM AEIRGSKETA AQPLPLYDTP YEPEDEGASP EGEGTPWPRE SRLPEDDERP
     PEEYDQPWEW KKERISKAFA AQFEGSENCL SPGREEKGRL PPRLSAGNPK SAKPLGMEPS
     SPLGEWTDPA LPLENQVWYH GAISRTDAEN LLRLCKEASY LVRNSETSKN DFSLSLKSSQ
     GFMHMKLSRT KEHKYVLGQN SPPFSSVPEI VHHYASRKLP IKGAEHMSLL YPVAIRTL
//
ID   LAT4_MOUSE              Reviewed;         568 AA.
AC   Q8CGA3; Q5CD76;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Large neutral amino acids transporter small subunit 4;
DE   AltName: Full=L-type amino acid transporter 4;
DE   AltName: Full=Solute carrier family 43 member 2;
GN   Name=Slc43a2; Synonyms=Lat4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP   GLYCOSYLATION, AND FUNCTION.
RC   STRAIN=FVB/N;
RX   PubMed=15659399; DOI=10.1074/jbc.M408638200;
RA   Bodoy S., Martin L., Zorzano A., Palacin M., Estevez R., Bertran J.;
RT   "Identification of LAT4, a novel amino acid transporter with system L
RT   activity.";
RL   J. Biol. Chem. 280:12002-12011(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RA   Chairoungdua A., Kanai Y., Babu E., Iribe Y., Kim D., Tangtrongsup S.,
RA   Jutabha P., Li Y., Anzai N., Endou H.;
RT   "Identification of a novel epithelial type neutral amino acid
RT   transporter with the properties of system L2.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Sodium-, chloride, pH-independent, high affinity
CC       transport of large neutral amino acids.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in intestine, kidney, brain and
CC       adipose tissue, heart and testis. In the kidney is detected in
CC       epithelial cells of the distal tubule and collecting duct. In the
CC       intestine is expressed mainly in crypt cells of the intestinal
CC       microvilli ans epithelial cells in the base of the villus.
CC   -!- PTM: Glycosylated.
CC   -!- SIMILARITY: Belongs to the SLC43A transporter (TC 2.A.1.44)
CC       family.
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DR   EMBL; BK005643; DAA05677.1; -; mRNA.
DR   EMBL; AB120363; BAD91090.1; -; mRNA.
DR   EMBL; AK143773; BAE25533.1; -; mRNA.
DR   EMBL; AK159144; BAE34852.1; -; mRNA.
DR   EMBL; AL591440; CAI24094.1; -; Genomic_DNA.
DR   EMBL; AL591496; CAI24094.1; JOINED; Genomic_DNA.
DR   EMBL; AL591496; CAI35390.1; -; Genomic_DNA.
DR   EMBL; AL591440; CAI35390.1; JOINED; Genomic_DNA.
DR   EMBL; BC042513; AAH42513.1; -; mRNA.
DR   IPI; IPI00229457; -.
DR   RefSeq; NP_001186212.1; NM_001199283.1.
DR   RefSeq; NP_001186213.1; NM_001199284.1.
DR   RefSeq; NP_775564.1; NM_173388.2.
DR   UniGene; Mm.11186; -.
DR   ProteinModelPortal; Q8CGA3; -.
DR   STRING; Q8CGA3; -.
DR   PhosphoSite; Q8CGA3; -.
DR   PRIDE; Q8CGA3; -.
DR   Ensembl; ENSMUST00000042561; ENSMUSP00000046074; ENSMUSG00000038178.
DR   Ensembl; ENSMUST00000100839; ENSMUSP00000098400; ENSMUSG00000038178.
DR   Ensembl; ENSMUST00000108433; ENSMUSP00000104071; ENSMUSG00000038178.
DR   GeneID; 215113; -.
DR   KEGG; mmu:215113; -.
DR   UCSC; uc007keb.1; mouse.
DR   CTD; 215113; -.
DR   MGI; MGI:2442746; Slc43a2.
DR   GeneTree; ENSGT00530000063043; -.
DR   HOGENOM; HBG444314; -.
DR   HOVERGEN; HBG072879; -.
DR   InParanoid; Q8CGA3; -.
DR   OMA; STQFGSL; -.
DR   OrthoDB; EOG40CHGR; -.
DR   PhylomeDB; Q8CGA3; -.
DR   NextBio; 374612; -.
DR   ArrayExpress; Q8CGA3; -.
DR   Bgee; Q8CGA3; -.
DR   CleanEx; MM_SLC43A2; -.
DR   Genevestigator; Q8CGA3; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IDA:MGI.
DR   InterPro; IPR011701; MFS_1.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
DR   PROSITE; PS50850; MFS; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    568       Large neutral amino acids transporter
FT                                small subunit 4.
FT                                /FTId=PRO_0000307273.
FT   TRANSMEM     20     40       Helical; (Potential).
FT   TRANSMEM     90    110       Helical; (Potential).
FT   TRANSMEM    120    140       Helical; (Potential).
FT   TRANSMEM    143    163       Helical; (Potential).
FT   TRANSMEM    177    197       Helical; (Potential).
FT   TRANSMEM    207    227       Helical; (Potential).
FT   TRANSMEM    319    341       Helical; (Potential).
FT   TRANSMEM    365    385       Helical; (Potential).
FT   TRANSMEM    434    454       Helical; (Potential).
FT   TRANSMEM    461    481       Helical; (Potential).
FT   TRANSMEM    489    509       Helical; (Potential).
FT   TRANSMEM    515    535       Helical; (Potential).
FT   MOD_RES     274    274       Phosphoserine.
FT   MOD_RES     278    278       Phosphoserine (By similarity).
FT   CARBOHYD     55     55       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    237    237       P -> S (in Ref. 2; BAD91090).
FT   CONFLICT    402    402       K -> E (in Ref. 2; BAD91090).
SQ   SEQUENCE   568 AA;  62430 MW;  02F076C32FE5988E CRC64;
     MAPTLATAHR RRWWMACTAV LENLLFSAVL LGWGSLLIML KSEGFYSYLC TKPENVTNST
     VGGSAEPEPE ELSLVNGWLS CKAQDEILNL AFTVGSFLLS AITLPLGIIM DKYGPRKLRL
     LGSACFAVSC LLIAYGASNP DSLSVLIFIA LALNGFGGMC MTFTSLTLPN MFGDLRSTFI
     ALMIGSYASS AVTFPGIKLI YDAGASFIGI LVVWAGCSGL VFFNCFFNWP LEPFPGPEDM
     DYSVKIKFSW LGFDHKITGK QFYKQVTTVG RRLSVGSSMR TAKEQAALQE GHKLCLSTVD
     LEVKCQPDAA AAPSFMHSVF SPLLVLSLVT MCVTQLRLIF YMGAMNSILE FLVRGDQKTV
     ALYTSIFGAL QLLCLLTAPV IGYIMDWKLK ECEDTSEEPE EKEGTQGEKK QKRDRQIQKV
     TNAMRAFAFT NVLLVGFGVT CLIPNLPLQI FSFVLHTIVR GFIHSAVGGL YAAVYPSTQF
     GSLTGLQSLV SALFALLQQP LYLAMMGPLG GDPLWVNVGL LAMSMLGFCL PLYLICYRRQ
     LERQLQQKRE DSKLFLKING SSNREAFV
//
ID   TENC1_MOUSE             Reviewed;        1400 AA.
AC   Q8CGB6; Q3TZ93; Q3UGR8; Q8CJ95; Q8R122;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Tensin-like C1 domain-containing phosphatase;
DE            EC=3.1.3.-;
DE   AltName: Full=C1 domain-containing phosphatase and tensin homolog;
DE            Short=C1-TEN;
DE   AltName: Full=Tensin-2;
GN   Name=Tenc1; Synonyms=Tns2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Lo S.H.;
RT   "Molecular cloning and characterization of mouse tensin 2.";
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 753-1400 (ISOFORM 3).
RC   STRAIN=FVB/N; TISSUE=Liver, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-935 (ISOFORM 4), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-875 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Inner ear, and Melanocyte;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-483, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455; SER-466; SER-481;
RP   TYR-483; SER-832; SER-835 AND THR-913, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-483 AND SER-1087, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Regulates cell motility and proliferation. May have
CC       phosphatase activity. Reduces AKT1 phosphorylation. Lowers AKT1
CC       kinase activity and interferes with AKT1 signaling (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with AXL (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell
CC       membrane; Peripheral membrane protein; Cytoplasmic side.
CC       Note=Detected at the end of actin stress fibers (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8CGB6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CGB6-2; Sequence=VSP_026462;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8CGB6-3; Sequence=VSP_026464;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q8CGB6-4; Sequence=VSP_026463;
CC   -!- SIMILARITY: Contains 1 C2 tensin-type domain.
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC   -!- SIMILARITY: Contains 1 phosphatase tensin-type domain.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE34316.1; Type=Frameshift; Positions=66;
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DR   EMBL; AF424789; AAN32753.1; -; mRNA.
DR   EMBL; BC025818; AAH25818.1; -; mRNA.
DR   EMBL; BC042190; AAH42190.1; -; mRNA.
DR   EMBL; AK147789; BAE28139.1; -; mRNA.
DR   EMBL; AK158009; BAE34316.1; ALT_FRAME; mRNA.
DR   IPI; IPI00762785; -.
DR   IPI; IPI00816969; -.
DR   IPI; IPI00848476; -.
DR   IPI; IPI00848939; -.
DR   RefSeq; NP_705761.2; NM_153533.2.
DR   UniGene; Mm.29389; -.
DR   HSSP; Q04205; 1WVH.
DR   ProteinModelPortal; Q8CGB6; -.
DR   SMR; Q8CGB6; 29-81, 123-461, 1125-1400.
DR   STRING; Q8CGB6; -.
DR   PhosphoSite; Q8CGB6; -.
DR   PRIDE; Q8CGB6; -.
DR   Ensembl; ENSMUST00000046144; ENSMUSP00000041087; ENSMUSG00000037003.
DR   GeneID; 209039; -.
DR   KEGG; mmu:209039; -.
DR   UCSC; uc007xuo.1; mouse.
DR   CTD; 209039; -.
DR   MGI; MGI:2387586; Tenc1.
DR   eggNOG; roNOG12828; -.
DR   GeneTree; ENSGT00550000074191; -.
DR   HOGENOM; HBG715389; -.
DR   HOVERGEN; HBG108559; -.
DR   InParanoid; Q8CGB6; -.
DR   OMA; QDTRSPT; -.
DR   OrthoDB; EOG4MW858; -.
DR   PhylomeDB; Q8CGB6; -.
DR   NextBio; 372540; -.
DR   ArrayExpress; Q8CGB6; -.
DR   Bgee; Q8CGB6; -.
DR   CleanEx; MM_TENC1; -.
DR   Genevestigator; Q8CGB6; -.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   GO; GO:0019725; P:cellular homeostasis; IMP:MGI.
DR   GO; GO:0032963; P:collagen metabolic process; IMP:MGI.
DR   GO; GO:0001822; P:kidney development; IMP:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR   GO; GO:0048871; P:multicellular organismal homeostasis; IMP:MGI.
DR   GO; GO:0014850; P:response to muscle activity; IMP:MGI.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR014019; Phosphatase_tensin-typ.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR013625; PTB.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR014020; Tensin_phosphatase_C2-dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF08416; PTB; 1.
DR   Pfam; PF10409; PTEN_C2; 1.
DR   Pfam; PF00017; SH2; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM00252; SH2; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   PROSITE; PS51182; C2_TENSIN; 1.
DR   PROSITE; PS51181; PPASE_TENSIN; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Hydrolase;
KW   Membrane; Metal-binding; Phosphoprotein; Protein phosphatase;
KW   SH2 domain; Zinc; Zinc-finger.
FT   CHAIN         1   1400       Tensin-like C1 domain-containing
FT                                phosphatase.
FT                                /FTId=PRO_0000292988.
FT   DOMAIN      122    294       Phosphatase tensin-type.
FT   DOMAIN      299    425       C2 tensin-type.
FT   DOMAIN     1131   1238       SH2.
FT   ZN_FING      31     79       Phorbol-ester/DAG-type.
FT   COMPBIAS    502    505       Poly-Pro.
FT   COMPBIAS    966   1113       Pro-rich.
FT   ACT_SITE    231    231       Phosphocysteine intermediate (By
FT                                similarity).
FT   MOD_RES     455    455       Phosphoserine.
FT   MOD_RES     466    466       Phosphoserine.
FT   MOD_RES     481    481       Phosphoserine.
FT   MOD_RES     483    483       Phosphotyrosine.
FT   MOD_RES     770    770       Phosphotyrosine (By similarity).
FT   MOD_RES     832    832       Phosphoserine.
FT   MOD_RES     835    835       Phosphoserine.
FT   MOD_RES     913    913       Phosphothreonine.
FT   MOD_RES    1003   1003       Phosphoserine (By similarity).
FT   MOD_RES    1087   1087       Phosphoserine.
FT   VAR_SEQ       1     25       MKSSGPVERLLRALGRRDSSRATSR -> MK (in
FT                                isoform 2).
FT                                /FTId=VSP_026462.
FT   VAR_SEQ       1     25       MKSSGPVERLLRALGRRDSSRATSR -> MGWSGGAPCCCP
FT                                SSPRPRPSGRPPQ (in isoform 4).
FT                                /FTId=VSP_026463.
FT   VAR_SEQ     872    872       T -> TELFPPVS (in isoform 3).
FT                                /FTId=VSP_026464.
FT   CONFLICT     54     54       D -> N (in Ref. 3; BAE28139).
FT   CONFLICT    195    195       F -> L (in Ref. 3; BAE28139).
FT   CONFLICT    204    204       P -> H (in Ref. 3; BAE28139).
FT   CONFLICT   1112   1114       HPL -> NPFVVQE (in Ref. 1; AAN32753).
SQ   SEQUENCE   1400 AA;  152013 MW;  72CB109A17BB021C CRC64;
     MKSSGPVERL LRALGRRDSS RATSRPRKAE PHSFREKVFR KKTPVCAVCK VTIDGTGVSC
     RVCKVATHRK CEAKVTSSCQ ALPPAELRRS TAPVRRIEHL GSTKSLNHSK QRSTLPRSFS
     LDPLMERRWD LDLTYVTERI LAAAFPARPD EQRHRGHLRE LAHVLQSKHR DKYLLFNLSE
     KRHDLTRLNP KVQDFGWPEL HAPPLDKLCS ICKAMETWLS ADPQHVVVLY CKGSKGKLGV
     IVSAYMHYSK ISAGADQALA TLTMRKFCED KVATELQPSQ RRYVSYFSGL LSGSIRMNSS
     PLFLHYVFVP VLPAFEPNTG FQPFLKIYQS MQLVYTSGVY RIAGPGPQQL CISLEPALLL
     KGDVMVTCYH KGGQGTDRTL VFRVQFHTCT IHGSRLTFPK DQLDEAWADE RFPFQASVEF
     VFSSSPEKVK GNTPRNDPSV SVDYNTTEPA VRWDSYENFN QHHEDSVDGA LAHTRGPLDG
     SPYAQVQRVP RQTPPAPSPE LPPPPMLSVS SDSGHSSTLT TEHTAESPGR PPPTAAERQE
     LDRLLGGCGV ASAGRGAGRE TAILDDEEQP SVGGGLHLGM YSGHRPGLSR RCSCRQGFRE
     PCGVPNGSYY RPEGTLERRR PPYGGYEGHP QGYAEASVEK RRLCRSLSEG PYPYAPELGK
     PANGDFGYRP AGYREVVILE DPGVPALCSC PACEEKLALP TAALYGLRLE REAAEGWSSE
     VGKPLLHPVR PGHPLPLLVP ACGHHHAPMP DYGCLKPPKV GEEGHEGCSY AVCSEGRYGH
     SGYPALVTYG YGGAVPSYCP AYGRAPHSCG SPSEGRGYPS PGAHSPRAGS VSPGSPPYLQ
     PRKLGYEISA EDGRDKYPLS GHLASTGPLA STESPEPSWR DGSSGHSTLP RSPRDPQCSA
     SSELSGPSTP LHTSSPVQGK ESNRRQDTTR SPSLAPTQRL SPGEALPSVV QGVAEKTPEL
     LTSSRPEQLD PSPFSQTSAP GSPNGWPQER SPGGHTNSAS PRSPVPTTLP GLRHAPWQGP
     RGTSDSPDGS PLTPVPTQMP WLVGSPEPPQ SSPTPAFPLA TSYDANGPIQ PPLPEKRHLP
     GSGQQPSPPA RSTNQHVTFA SPLPDVTQPP EHPLQENQSN VKFVQDTSKF WYKPHLSRDQ
     AIALLKDKDP GAFLIRDSHS FQGAYGLALK VATPPPSAQP WKGDPSEQLV RHFLIETGPK
     GVKIKGCPTE PYFGSLSALV SQHSISPISL PCCLRIPSKD PLEETPEAPV PTNMSTAADL
     LRQGAACSVL YLTSVETESL TGPQAVAKAS SAALSCSPVP VPAIVHFKVS AQGITLTDNQ
     RKLFFRRHYP VNSITFSSTD PQDRRWTNPD GATSKIFGFV AKKPGSPWEN VCHLFAELDP
     DQPASAIVTF ITKVLLGQRK
//
ID   Q8CGE9_MOUSE            Unreviewed;      1381 AA.
AC   Q8CGE9;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   SubName: Full=Regulator of G-protein signaling 12;
GN   Name=Rgs12;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N;
RC   TISSUE=Mammary tumor. Metallothionien-TGF alpha model. 10 month old
RC   virgin mouse. Taken by biopsy.;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 RGS domain.
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DR   EMBL; BC040396; AAH40396.1; -; mRNA.
DR   IPI; IPI00229481; -.
DR   UniGene; Mm.196208; -.
DR   HSSP; O08773; 1KJY.
DR   ProteinModelPortal; Q8CGE9; -.
DR   SMR; Q8CGE9; 11-111, 705-852, 1019-1121, 1186-1220.
DR   MINT; MINT-4115792; -.
DR   STRING; Q8CGE9; -.
DR   PhosphoSite; Q8CGE9; -.
DR   PRIDE; Q8CGE9; -.
DR   Ensembl; ENSMUST00000030984; ENSMUSP00000030984; ENSMUSG00000029101.
DR   UCSC; uc008xdg.1; mouse.
DR   MGI; MGI:1918979; Rgs12.
DR   GeneTree; ENSGT00540000071162; -.
DR   HOVERGEN; HBG063299; -.
DR   NextBio; 334351; -.
DR   ArrayExpress; Q8CGE9; -.
DR   Bgee; Q8CGE9; -.
DR   Genevestigator; Q8CGE9; -.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0005057; F:receptor signaling protein activity; IEA:InterPro.
DR   InterPro; IPR003109; GoLoco_motif.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   InterPro; IPR003116; Raf-like_ras-bd.
DR   InterPro; IPR000342; Regulat_G_prot_signal.
DR   InterPro; IPR016137; Regulat_G_prot_signal_superfam.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF02188; GoLoco; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF02196; RBD; 2.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00390; GoLoco; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM00455; RBD; 2.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF48097; Regulat_G_prot_signal_superfam; 1.
DR   PROSITE; PS50877; GOLOCO; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS01179; PID; 1.
DR   PROSITE; PS50898; RBD; 2.
DR   PROSITE; PS50132; RGS; 1.
PE   1: Evidence at protein level;
SQ   SEQUENCE   1381 AA;  149583 MW;  D18D725B73999085 CRC64;
     MYRAGEPGKR QPGPAPPRVR SVEVARGRAG YGFTLSGQAP CVLSCVMRGS PADFVGLRAG
     DQILAINEIN VKKASHEDVV KLIGKCSGVL HMVIAEGTSH VESCSSDEEG GLYEGKGWLR
     PKLDSKALGI NRAERVVEEV QSGGIFNMIF ESSSLCASGP EPLKLKQRSL SESAALRLDA
     GQAGLCAPHP SMLSKEDISK VINDDSVFTV GLDSHDDFGL DASILNVAMV VGYLGSIELP
     STSSNLEHDS LQAIRGCMRR LRAEQKIHSL VTMKVMHDCV QLVTDRAGVV AEYPAEKLAF
     SAVCPDDRRF FGLVTMQTND DGGLAQEDEG ALRTSCHVFM VDPDLFHHKI HQGIARRFGF
     ACTADPDTSG CLEFPASSLP VLQFISVLYR DMGELIEGVR ARAFLDGDAD AHQNNSTSSN
     SDSGIGNFNQ EEKSNRVLVV DLGGGSSRHG QGSSPGWESG GGRGSQPWSA PWNGAFCHDS
     EAGSPLETSP NTDRFWDLTK HSGPVSHMEV PPATLRSSIP PSKRGAAGSS CGFNQKWLPV
     HVLQEWQCGH ASDQESYTDS TDGWSSVNCG TLPPPMSKIP ADRYRVEGSF AQAPLSTQKR
     DWSRKAFGMQ NLFGPHRNVR KTKEDKKSSK LGRGVALAQT SQRTSARRSF GRSRRFSITR
     SLDDLESATV SDGELTGADL KDCISNNSLS SNASLPSVQS CRRLRERRVA SWAVSFERLL
     QDPVGVRYFS DFLRKEFSEE NILFWQACEC FSHVPAHDKK ELSYRAREIF SKFLCSKATT
     PVNIDSQAQL ADDILNAPHP DMFKEQQLQI FNLMKFDSYT RFLKSQLYQE CVLAEVEGRT
     LPDSQQVPSS PASKHSISSD HSNVSTPKKL SGKSKSGRSL NEDVGEEDSE KKRRGAFFSW
     SRSRSTGRSQ KKKDHGDHAH DAPHANGGLC RRESQGSVSS AGSLDLSEAC RTSALEKDKA
     AKHCCVHLPD GTSCVVAVKS GFSIKEILSG LCERHGINGA AVDLFLVGGD KPLVLHQDSS
     ILATRDLRLE KRTLFRLDLV PINRSVGLKA KPTKPVTEVL RPVVAKYGLD LGSLLVRLSG
     EKEPLDLGAP ISSLDGQRVI LEERDPSRGK VSTDKQKGAP VKQNSAVNSS PRNHSAMGEE
     RTLGKSNSIK IRGENGKSAR DPRLSKREES IAKIGKKKYQ KINLDEAEEF FELISKAQSN
     RADDQRGLLR KEDLVLPEFL RLPAGSSELA LSSPPPVKGY SKRAVTGHGQ EGAAQTEESY
     SDSPATSPAS AQSPCSAYSP GSAHSPGSAH STPGPPGTTQ PGEKPTKPSC VSMVQEGTTQ
     AWRRLSPEME AGGIQTVEDE QVADLTLMGE GDISSPNSTL LPPPPTPQDT PGPPRPGTSR
     F
//
ID   F193A_MOUSE             Reviewed;        1231 AA.
AC   Q8CGI1; Q499G1;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   08-FEB-2011, entry version 48.
DE   RecName: Full=Protein FAM193A;
GN   Name=Fam193a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N-3; TISSUE=Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-648, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SIMILARITY: Belongs to the FAM193 family.
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DR   EMBL; BC037112; AAH37112.1; -; mRNA.
DR   EMBL; BC099925; AAH99925.1; -; mRNA.
DR   IPI; IPI00752794; -.
DR   RefSeq; NP_001025477.1; NM_001030306.1.
DR   UniGene; Mm.286885; -.
DR   ProteinModelPortal; Q8CGI1; -.
DR   PhosphoSite; Q8CGI1; -.
DR   PRIDE; Q8CGI1; -.
DR   Ensembl; ENSMUST00000094867; ENSMUSP00000092463; ENSMUSG00000037210.
DR   GeneID; 231128; -.
DR   KEGG; mmu:231128; -.
DR   UCSC; uc008xch.1; mouse.
DR   CTD; 231128; -.
DR   MGI; MGI:2447768; Fam193a.
DR   GeneTree; ENSGT00390000000973; -.
DR   HOGENOM; HBG714437; -.
DR   HOVERGEN; HBG081059; -.
DR   InParanoid; Q8CGI1; -.
DR   OMA; MHHHKEG; -.
DR   NextBio; 380417; -.
DR   ArrayExpress; Q8CGI1; -.
DR   Bgee; Q8CGI1; -.
DR   CleanEx; MM_BC037112; -.
DR   Genevestigator; Q8CGI1; -.
DR   GermOnline; ENSMUSG00000037210; Mus musculus.
PE   1: Evidence at protein level;
KW   Coiled coil; Phosphoprotein.
FT   CHAIN         1   1231       Protein FAM193A.
FT                                /FTId=PRO_0000089431.
FT   COILED      106    142       Potential.
FT   COILED      877    973       Potential.
FT   COMPBIAS    570    573       Poly-Pro.
FT   COMPBIAS    634    637       Poly-Ser.
FT   COMPBIAS    884    926       Glu-rich.
FT   COMPBIAS    940    944       Poly-Lys.
FT   COMPBIAS   1110   1115       Poly-Asn.
FT   COMPBIAS   1155   1165       Poly-Lys.
FT   MOD_RES     293    293       Phosphoserine (By similarity).
FT   MOD_RES     648    648       Phosphoserine.
FT   MOD_RES     683    683       Phosphoserine (By similarity).
FT   MOD_RES    1151   1151       Phosphoserine (By similarity).
SQ   SEQUENCE   1231 AA;  136714 MW;  451534B775BE862E CRC64;
     MKVRLLRQLS AAAKAKAPSG LQGPPQAHHF VSLLLEEYAA LCQAARSIST FLGTLENEHL
     KKFQVTWELH NKHLFENLVF SEPLLQSNLP ALVSQIRLGT TTHDTCTEDM YSTLLQRYQR
     SEEELRKVAE EWLECQKRID AYVDEQMTMK TKQRMLTEDW EIFKQRRLIE EQLTNKKVVT
     GENNFTDTRR HMLSSRLSMP DCPNCNYRRR CACDDCSLSH ILTCGIMDTP VTDDIHIHQL
     PLQVDSAPDY LSEMRPPSVS SASSGSGSSS PITIQQHPRL ILTDNGSAPT FCSDDEDVAP
     LSAKFADIYP LTNYDDTNVV ANMNGIHSEL NGGGENMALK DESPQVSSTS RSSSEADDED
     ADGESSGEPP GAPKQEEAIG NGNPKTEESN VNTPPPSYPA QQAEQTPNTC ECHVCKQEAS
     GLPASAMTAG ALPPGHQFLS PEKPTHPALH LYPHIHGHVP LHTVPHLPRP LIHPTLYPAP
     PFTHSKALPP APVQSHTNKP QAFNASLQDH IYPSCFGNTP DWNSSKFISL WESEMMNDKN
     WNPGTFLPDT ISGNDILGPV LSETRPEALP PPPSNEAPAV SDIKEKKNAA KKKCLYNFQD
     AFMEANEVAM ANTVAMATSS ATSSVSCTAT TVQSSSSQFK VSSRRPPSIG DVFHGLNKED
     HRHSAPAAPR NSPTGLAPLP ALSPSALSPA STPHLPNLAA PSFPKTATTA PGFVDTRKSF
     CPTPVAPPPS TTDGSISAPP SVCSDPDCEG HRCENGVYDP QQDDGDESAD EDSCSEHSSS
     TSTSTNQKEG KYCDCCYCEF FGHGGPPAAP TSRNYAEMRE KLRLRLTKRK EEQPKKMEQI
     SEREGVVDHR RVEDLLQFIN SSEAKPVSSS RAAKRARHKQ RKLEEKARLE AEARAREHLH
     HQEEQKQREE EEDEEEEDEE QHFKEEFQRL QELQKLRAAK KKKKDRPSKD CSKLDMLARN
     FQAATESISN SENIHNGSLE QTEEPETSSH SPSRHMNHSE PRPGPGANGD ATDPVDPRDP
     SKLLLPKEVN GKQHEPLAFL LDMMHHHKEG NSKQKLKQTS KTSNEPARKP TEPPKTTEVQ
     LKPRAQPELK PKVVDLALLT EQKREERKTN SNNNNKKQLS HIKEEKLSTV TPEPPSPSQL
     LQNGRLILAS SPQPKGKNKK NKKKKGDRTS SSLDDVFLPK DIDLDSVDMD ETEREVEYFK
     RFCLDSARQN RQRLSINWSN FSLKKATFAA H
//
ID   GNAL_MOUSE              Reviewed;         381 AA.
AC   Q8CGK7; Q61020; Q61589;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-FEB-2011, entry version 70.
DE   RecName: Full=Guanine nucleotide-binding protein G(olf) subunit alpha;
DE   AltName: Full=Adenylate cyclase-stimulating G alpha protein, olfactory type;
GN   Name=Gnal;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RA   Von Dannecker L.E.C., Malnic B.;
RT   "The mouse G protein Golf alpha subunit full length coding sequence.";
RL   Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 45-55, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 209-373.
RC   STRAIN=CF-1 / Harlan; TISSUE=Brain;
RX   MEDLINE=97011591; PubMed=8858601;
RX   DOI=10.1002/(SICI)1098-2795(199607)44:3<315::AID-MRD5>3.3.CO;2-V;
RA   Williams C.J., Schultz R.M., Kopf G.S.;
RT   "G protein gene expression during mouse oocyte growth and maturation,
RT   and preimplantation embryo development.";
RL   Mol. Reprod. Dev. 44:315-323(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 216-276.
RC   TISSUE=Brain;
RX   MEDLINE=90017488; PubMed=2508088; DOI=10.1073/pnas.86.19.7407;
RA   Strathmann M., Wilkie T.M., Simon M.I.;
RT   "Diversity of the G-protein family: sequences from five additional
RT   alpha subunits in the mouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:7407-7409(1989).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC       involved as modulators or transducers in various transmembrane
CC       signaling systems. G(olf) alpha mediates signal transduction
CC       within the olfactory neuroepithelium and the basal ganglia. May be
CC       involved in some aspect of visual transduction, and in mediating
CC       the effect of one or more hormones/neurotransmitters (By
CC       similarity).
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and
CC       gamma. The alpha chain contains the guanine nucleotide binding
CC       site.
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(s) subfamily.
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DR   EMBL; AY179169; AAO03564.1; -; mRNA.
DR   EMBL; U38503; AAB01734.1; -; mRNA.
DR   EMBL; M57635; AAA63300.1; -; mRNA.
DR   IPI; IPI00229525; -.
DR   PIR; A33833; A33833.
DR   RefSeq; NP_034437.1; NM_010307.2.
DR   UniGene; Mm.440746; -.
DR   ProteinModelPortal; Q8CGK7; -.
DR   SMR; Q8CGK7; 39-378.
DR   STRING; Q8CGK7; -.
DR   PhosphoSite; Q8CGK7; -.
DR   PRIDE; Q8CGK7; -.
DR   Ensembl; ENSMUST00000076605; ENSMUSP00000075908; ENSMUSG00000024524.
DR   GeneID; 14680; -.
DR   KEGG; mmu:14680; -.
DR   UCSC; uc008flt.1; mouse.
DR   CTD; 14680; -.
DR   MGI; MGI:95774; Gnal.
DR   GeneTree; ENSGT00560000077005; -.
DR   HOVERGEN; HBG063184; -.
DR   OMA; DYSQEFF; -.
DR   PhylomeDB; Q8CGK7; -.
DR   NextBio; 286586; -.
DR   ArrayExpress; Q8CGK7; -.
DR   Bgee; Q8CGK7; -.
DR   Genevestigator; Q8CGK7; -.
DR   GermOnline; ENSMUSG00000024524; Mus musculus.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0007191; P:activation of adenylate cyclase activity by dopamine receptor signaling pathway; IGI:MGI.
DR   GO; GO:0001975; P:response to amphetamine; IMP:MGI.
DR   GO; GO:0031000; P:response to caffeine; IMP:MGI.
DR   GO; GO:0007608; P:sensory perception of smell; IMP:MGI.
DR   InterPro; IPR000367; Gprotein_alpha_S.
DR   InterPro; IPR001019; Gprotein_alpha_su.
DR   InterPro; IPR011025; GproteinA_insert.
DR   Gene3D; G3DSA:1.10.400.10; GproteinA_insert; 1.
DR   PANTHER; PTHR10218; Gprotein_alph_bd; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00443; GPROTEINAS.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF47895; Transducn_insert; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; GTP-binding; Lipoprotein;
KW   Nucleotide-binding; Palmitate; Transducer.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    381       Guanine nucleotide-binding protein G(olf)
FT                                subunit alpha.
FT                                /FTId=PRO_0000203733.
FT   NP_BIND      49     56       GTP (By similarity).
FT   NP_BIND     210    214       GTP (By similarity).
FT   NP_BIND     279    282       GTP (By similarity).
FT   LIPID         2      2       N-palmitoyl glycine (By similarity).
FT   LIPID         3      3       S-palmitoyl cysteine (By similarity).
SQ   SEQUENCE   381 AA;  44308 MW;  F707E668EC279033 CRC64;
     MGCLGNSSKT AEDQGVDEKE RREANKKIEK QLQKERLAYK ATHRLLLLGA GESGKSTIVK
     QMRILHVNGF NPEEKKQKIL DIRKNVKDAI VTIVSAMSTI IPPVPLANPE NQFRSDYIKS
     IAPITDFEYS QEFFDHVKKL WDDEGVKACF ERSNEYQLID CAQYFLERID SVSLVDYTPT
     DQDLLRCRVL TSGIFETRFQ VDKVNFHMFD VGGQRDERRK WIQCFNDVTA IIYVAACSSY
     NMVIREDNNT NRLRESLDLF ESIWNNRWLR TISIILFLNK QDMLAEKVLA GKSKIEDYFP
     EYANYTVPED ATPDAGEDPK VTRAKFFIRD LFLRISTATG DGKHYCYPHF TCAVDTENIR
     RVFNDCRDII QRMHLKQYEL L
//
ID   BAI2_MOUSE              Reviewed;        1561 AA.
AC   Q8CGM1; B1ASB7; B1ASB8; B2FDE3; Q3TYC8; Q3UN11; Q3UNE2; Q6PGN0;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Brain-specific angiogenesis inhibitor 2;
DE   Flags: Precursor;
GN   Name=Bai2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND FUNCTION.
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=22206655; PubMed=12218411;
RX   DOI=10.1097/00004647-200209000-00003;
RA   Kee H.J., Koh J.T., Kim M.Y., Ahn K.Y., Kim J.K., Bae C.S., Park S.S.,
RA   Kim K.K.;
RT   "Expression of brain-specific angiogenesis inhibitor 2 (BAI2) in
RT   normal and ischemic brain: involvement of BAI2 in the ischemia-induced
RT   brain angiogenesis.";
RL   J. Cereb. Blood Flow Metab. 22:1054-1067(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH GABPB2.
RX   PubMed=16412436; DOI=10.1016/j.febslet.2005.12.086;
RA   Jeong B.C., Kim M.Y., Lee J.H., Kee H.J., Kho D.H., Han K.E.,
RA   Qian Y.R., Kim J.K., Kim K.K.;
RT   "Brain-specific angiogenesis inhibitor 2 regulates VEGF through GABP
RT   that acts as a transcriptional repressor.";
RL   FEBS Lett. 580:669-676(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1345, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Might be involved in angiogenesis inhibition.
CC   -!- SUBUNIT: Interacts with GABPB2.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8CGM1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CGM1-2; Sequence=VSP_019762;
CC       Name=3;
CC         IsoId=Q8CGM1-3; Sequence=VSP_019763;
CC   -!- TISSUE SPECIFICITY: Specifically expressed in the brain. The peak
CC       level in the brain is observed 10 days after birth.
CC   -!- DEVELOPMENTAL STAGE: Ubiquitous in embryonic tissues, but
CC       expression is acutely down-regulated after birth, except in the
CC       brain, to a level that is maintained throughout adulthood.
CC   -!- INDUCTION: Down-regulated after hypoxia.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       LN-TM7 subfamily.
CC   -!- SIMILARITY: Contains 1 GPS domain.
CC   -!- SIMILARITY: Contains 4 TSP type-1 domains.
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DR   EMBL; AY168407; AAN86965.1; -; mRNA.
DR   EMBL; AK144268; BAE25805.1; -; mRNA.
DR   EMBL; AK144559; BAE25937.1; -; mRNA.
DR   EMBL; AK158735; BAE34635.1; -; mRNA.
DR   EMBL; AL626774; CAM17272.1; -; Genomic_DNA.
DR   EMBL; AL626774; CAM17273.1; -; Genomic_DNA.
DR   EMBL; AL626774; CAQ52064.1; -; Genomic_DNA.
DR   EMBL; BC056926; AAH56926.1; -; mRNA.
DR   IPI; IPI00319528; -.
DR   IPI; IPI00623397; -.
DR   IPI; IPI00648090; -.
DR   RefSeq; NP_001186625.1; NM_001199696.1.
DR   RefSeq; NP_775094.2; NM_173071.3.
DR   UniGene; Mm.262241; -.
DR   ProteinModelPortal; Q8CGM1; -.
DR   SMR; Q8CGM1; 217-407, 410-562.
DR   MINT; MINT-1504097; -.
DR   STRING; Q8CGM1; -.
DR   MEROPS; S63.032; -.
DR   PhosphoSite; Q8CGM1; -.
DR   PRIDE; Q8CGM1; -.
DR   Ensembl; ENSMUST00000030571; ENSMUSP00000030571; ENSMUSG00000028782.
DR   Ensembl; ENSMUST00000097868; ENSMUSP00000095480; ENSMUSG00000028782.
DR   Ensembl; ENSMUST00000106015; ENSMUSP00000101636; ENSMUSG00000028782.
DR   Ensembl; ENSMUST00000106018; ENSMUSP00000101639; ENSMUSG00000028782.
DR   GeneID; 230775; -.
DR   KEGG; mmu:230775; -.
DR   UCSC; uc008uym.1; mouse.
DR   UCSC; uc008uyn.1; mouse.
DR   UCSC; uc008uyp.1; mouse.
DR   CTD; 230775; -.
DR   MGI; MGI:2451244; Bai2.
DR   eggNOG; roNOG11853; -.
DR   GeneTree; ENSGT00600000084332; -.
DR   HOGENOM; HBG714232; -.
DR   HOVERGEN; HBG004813; -.
DR   InParanoid; Q8CGM1; -.
DR   OMA; ARNAMAS; -.
DR   OrthoDB; EOG4MSCXB; -.
DR   PhylomeDB; Q8CGM1; -.
DR   NextBio; 380140; -.
DR   ArrayExpress; Q8CGM1; -.
DR   Bgee; Q8CGM1; -.
DR   CleanEx; MM_BAI2; -.
DR   Genevestigator; Q8CGM1; -.
DR   GermOnline; ENSMUSG00000028782; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:InterPro.
DR   InterPro; IPR022624; DUF3497.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR008077; GPCR_2_brain-spec_angio_inhib.
DR   InterPro; IPR001879; GPCR_2_extracellular_dom.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR000203; GPS_dom.
DR   InterPro; IPR000884; Thrombospondin_1_rpt.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF12003; DUF3497; 1.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF00090; TSP_1; 4.
DR   PRINTS; PR01694; BAIPRECURSOR.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   SMART; SM00303; GPS; 1.
DR   SMART; SM00008; HormR; 1.
DR   SMART; SM00209; TSP1; 4.
DR   SUPFAM; SSF82895; TSP1; 4.
DR   PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG.
DR   PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; FALSE_NEG.
DR   PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
DR   PROSITE; PS50092; TSP1; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW   Receptor; Repeat; Signal; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21   1561       Brain-specific angiogenesis inhibitor 2.
FT                                /FTId=PRO_0000245613.
FT   TOPO_DOM     21    930       Extracellular (Potential).
FT   TRANSMEM    931    951       Helical; Name=1; (Potential).
FT   TOPO_DOM    952    959       Cytoplasmic (Potential).
FT   TRANSMEM    960    980       Helical; Name=2; (Potential).
FT   TOPO_DOM    981    988       Extracellular (Potential).
FT   TRANSMEM    989   1009       Helical; Name=3; (Potential).
FT   TOPO_DOM   1010   1030       Cytoplasmic (Potential).
FT   TRANSMEM   1031   1051       Helical; Name=4; (Potential).
FT   TOPO_DOM   1052   1072       Extracellular (Potential).
FT   TRANSMEM   1073   1093       Helical; Name=5; (Potential).
FT   TOPO_DOM   1094   1115       Cytoplasmic (Potential).
FT   TRANSMEM   1116   1136       Helical; Name=6; (Potential).
FT   TOPO_DOM   1137   1147       Extracellular (Potential).
FT   TRANSMEM   1148   1168       Helical; Name=7; (Potential).
FT   TOPO_DOM   1169   1561       Cytoplasmic (Potential).
FT   DOMAIN      300    353       TSP type-1 1.
FT   DOMAIN      355    408       TSP type-1 2.
FT   DOMAIN      410    463       TSP type-1 3.
FT   DOMAIN      466    519       TSP type-1 4.
FT   DOMAIN      865    917       GPS.
FT   COMPBIAS    117    122       Poly-Glu.
FT   COMPBIAS    123    127       Poly-Ala.
FT   COMPBIAS    180    183       Poly-Asn.
FT   COMPBIAS   1309   1312       Poly-Pro.
FT   COMPBIAS   1358   1361       Poly-Gly.
FT   COMPBIAS   1419   1424       Poly-Pro.
FT   MOD_RES    1345   1345       Phosphotyrosine.
FT   CARBOHYD     94     94       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    182    182       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    183    183       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    347    347       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    428    428       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    551    551       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    636    636       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    861    861       N-linked (GlcNAc...) (Potential).
FT   DISULFID    312    346       By similarity.
FT   DISULFID    316    352       By similarity.
FT   DISULFID    327    336       By similarity.
FT   DISULFID    367    402       By similarity.
FT   DISULFID    371    407       By similarity.
FT   DISULFID    382    392       By similarity.
FT   DISULFID    422    457       By similarity.
FT   DISULFID    426    462       By similarity.
FT   DISULFID    437    447       By similarity.
FT   DISULFID    478    513       By similarity.
FT   DISULFID    482    518       By similarity.
FT   DISULFID    493    503       By similarity.
FT   VAR_SEQ     299    353       Missing (in isoform 2).
FT                                /FTId=VSP_019762.
FT   VAR_SEQ    1113   1145       SERCPWASLLLPCSACGAVPSPLLSSASARNAM -> RLSW
FT                                NLWGYGSQLCLFPKLPR (in isoform 3).
FT                                /FTId=VSP_019763.
FT   CONFLICT    116    116       P -> L (in Ref. 1; AAN86965).
FT   CONFLICT    122    122       Missing (in Ref. 1; AAN86965).
FT   CONFLICT    386    386       Q -> K (in Ref. 1; AAN86965).
FT   CONFLICT    526    526       R -> G (in Ref. 2; BAE34635).
FT   CONFLICT    674    674       D -> G (in Ref. 2; BAE34635).
FT   CONFLICT   1179   1179       A -> V (in Ref. 2; BAE34635).
FT   CONFLICT   1316   1316       N -> D (in Ref. 2; BAE25937).
FT   CONFLICT   1467   1467       Missing (in Ref. 2; BAE25937/BAE25805).
FT   CONFLICT   1550   1550       T -> P (in Ref. 1; AAN86965).
SQ   SEQUENCE   1561 AA;  169863 MW;  3B3EB731F619CBA3 CRC64;
     MTPACPLLLS VILSLRLATA FDPAPSACSA LASGVLYGAF SLQDLFPTIA SGCSWTLENP
     DPTKYSLYLR FNRQEQVCTH FAPRLLPLDH YLVNFTCLRP GPEEATARAE SEVGRPEEEE
     EEAAAAASGL ELCGGSGPFT FLHFDKNFVQ LCLSAEPSEA PRLLAPAALA FRFVEVLLIN
     NNNSSQFTCG VLCRWSEECG RAAGRACGFA QPGCSCPGEA GANPATTTSP GPPVAHTLSN
     ALVPGGPAPP AEADLHSGSS NDLFTTEMRY GEEPEEEPKV KTQWPRSADE PGLYMAQTGD
     PAAEEWSPWS VCSLTCGQGL QVRTRSCVSS PYGTLCSGPL RETRPCNNSA TCPVHGVWEE
     WGSWSLCSRS CGRGSRSRMR TCVPPQHGGK ACEGPELQTK LCSMAACPVE GQWLEWGPWG
     PCSSSCANGT QQRSRKCSVA GPAWATCAGA LTDTRECSNL DCPATDGKWG PWNAWSLCSK
     TCDTGWQRRF RMCQASGTQG YPCEGTGEEV KPCSEKRCPA FHEMCRDEYV MLMTWKRAAA
     GEIIYNKCPP NASGSASRRC LLSAQGVAYW GLPSFARCIS HEYRYLYLSL REHLAKGQRM
     LAGEGMSQVV RSLQELLARR TYYSGDLLFS VDILRNVTDT FKRATYVPSA DDVQRFFQVV
     SFMVDSENKD KWDDAQQVSP GSVHLLRVVE DFIHLVGDAL KAFQSSLIVT DNLVISIQRE
     PISAVSSDIT FPMRGRRGMK DWVRHSEDRL FLPKEVLSLS SPGKPATPGA ATAGSPGRGR
     GPGTVPPGPG HAHQRLLPAD PEESSSYFVI GAVLYRTLGL ILPPPRPPLA VTSRVMTVTV
     RPPTQPPAEP LITVELSYII NGTTDPHCAS WDYSRADTNS GDWNTESCQT LETQAAHTRC
     QCQHLSTFAV LAQPPKDLTL ELAGAPSVPL VIGCAVSCMA LLTLLAIYAA FWRFIKSERS
     IILLNFCLSI LASNILILVG QSRVLSKGVC TMTAAFLHFF FLSSFCWVLT EAWQSYLAVI
     GRMRTRLVRK RFLCLGWGLP ALVVAVSVGF TRTKGYGTSS YCWLSLEGGL LYAFVGPAAV
     IVLVNMLIGI IVFNKLMARD GVSDKSKKQR AGSERCPWAS LLLPCSACGA VPSPLLSSAS
     ARNAMASLWS SCVVLPLLAL TWMSAVLAMT DRRSVLFQAL FAVFNSAQGF VITAVHCFLR
     REVQDVVKCQ MGVCRADESE DSPDSCKNGQ LQILSDFEKD VDLACQTVLF KEVNTCNPST
     ITGTLSRLSL DEDEEPKSCL VGPEGGLSFS PLPGNILVPM AASPGLGEPP PPQETNPVYM
     CGEGGLRQLD LTWIRQSEPG SEGDYMVLPR RTLSLQPGGG GTAGEEAPRA RPEGTPRRAA
     KTVAHTEGYP SFLSVEHSGL GLGPAYGSLQ NPYGMTFQPP PPTPSARQVP EPGERSRTMP
     RTVPGSTMKL GSLERKKLRY SDLDFEKVMH TRKRHSELYH ELNQKFHTFD RYRSQSSAKE
     KPSPPGGRPG LSQHRRHQSW STFKSMTLGS LPPKPRERLA LHRTAAWEPT EPPDGDFQTE
     V
//
ID   BCOR_MOUSE              Reviewed;        1759 AA.
AC   Q8CGN4; B1AXK3; B1AXK4; B1AXK5; B1AXK6; Q6PDK5; Q6ZPM3; Q8BKF5;
AC   Q8CGN1; Q8CGN2; Q8CGN3;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=BCL-6 corepressor;
DE            Short=BCoR;
GN   Name=Bcor; Synonyms=Kiaa1575;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION,
RP   INTERACTION WITH MLLT3, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=Swiss Webster / NIH;
RX   MEDLINE=22660632; PubMed=12776190; DOI=10.1038/sj.onc.1206361;
RA   Srinivasan R.S., de Erkenez A.C., Hemenway C.S.;
RT   "The mixed lineage leukemia fusion partner AF9 binds specific isoforms
RT   of the BCL-6 corepressor.";
RL   Oncogene 22:3395-3406(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-945.
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1146, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Transcriptional corepressor. May specifically inhibit
CC       gene expression when recruited to promoter regions by sequence
CC       specific DNA-binding proteins such as BCL6 and MLLT3. This
CC       repression may be mediated at least in part by histone deacetylase
CC       activities which can associate with this corepressor. Involved in
CC       the repression of TFAP2A; impairs binding of BCL6 and KDM2B to
CC       TFAP2A promoter regions. Via repression of TFAP2A acts as a
CC       negative regulator of osteo-dentiogenic capacity in adult stem
CC       cells; the function implies inhibition of methylation on histone
CC       H3 'Lys-4' (H3K4me3) and 'Lys-36' (H3K36me2) (By similarity).
CC   -!- SUBUNIT: Interacts with BCL6. Can interact with HDAC1, HDAC3 and
CC       HDAC5. Interacts with PCGF1; the interaction is direct. Interacts
CC       with KDM2B. Component of an approximative 800 kDa repressive BCOR
CC       complex at least composed of BCOR, RYBP, PCGF1, RING1, RNF2/RING2,
CC       KDM2B and SKP1 (By similarity). Isoform 1 and isoform 2 can
CC       interact with MLLT3/AF9.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=A;
CC         IsoId=Q8CGN4-1; Sequence=Displayed;
CC       Name=2; Synonyms=B;
CC         IsoId=Q8CGN4-2; Sequence=VSP_012558;
CC       Name=3; Synonyms=C;
CC         IsoId=Q8CGN4-3; Sequence=VSP_012559;
CC       Name=4; Synonyms=D;
CC         IsoId=Q8CGN4-4; Sequence=VSP_012558, VSP_012559;
CC   -!- TISSUE SPECIFICITY: Expressed in heart, liver, lung, skeletal
CC       muscle, spleen and testis.
CC   -!- SIMILARITY: Belongs to the BCOR family.
CC   -!- SIMILARITY: Contains 3 ANK repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98208.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY161170; AAN85318.1; -; mRNA.
DR   EMBL; AY161171; AAN85319.1; -; mRNA.
DR   EMBL; AY161172; AAN85320.1; -; mRNA.
DR   EMBL; AY161173; AAN85321.1; -; mRNA.
DR   EMBL; AK129398; BAC98208.1; ALT_INIT; mRNA.
DR   EMBL; AL808012; CAM24722.1; -; Genomic_DNA.
DR   EMBL; AL808012; CAM24723.1; -; Genomic_DNA.
DR   EMBL; AL808012; CAM24724.1; -; Genomic_DNA.
DR   EMBL; AL808012; CAM24725.1; -; Genomic_DNA.
DR   EMBL; BC058656; AAH58656.1; -; mRNA.
DR   EMBL; AK053309; BAC35338.1; -; mRNA.
DR   IPI; IPI00229530; -.
DR   IPI; IPI00400070; -.
DR   IPI; IPI00400071; -.
DR   IPI; IPI00467347; -.
DR   RefSeq; NP_001161793.1; NM_001168321.1.
DR   RefSeq; NP_083786.2; NM_029510.3.
DR   RefSeq; NP_778209.2; NM_175044.3.
DR   RefSeq; NP_778210.2; NM_175045.3.
DR   RefSeq; NP_778211.2; NM_175046.3.
DR   UniGene; Mm.196328; -.
DR   ProteinModelPortal; Q8CGN4; -.
DR   SMR; Q8CGN4; 1465-1590.
DR   DIP; DIP-29852N; -.
DR   STRING; Q8CGN4; -.
DR   PhosphoSite; Q8CGN4; -.
DR   PRIDE; Q8CGN4; -.
DR   Ensembl; ENSMUST00000043441; ENSMUSP00000048024; ENSMUSG00000040363.
DR   Ensembl; ENSMUST00000065143; ENSMUSP00000068618; ENSMUSG00000040363.
DR   Ensembl; ENSMUST00000115512; ENSMUSP00000111174; ENSMUSG00000040363.
DR   Ensembl; ENSMUST00000115513; ENSMUSP00000111175; ENSMUSG00000040363.
DR   GeneID; 71458; -.
DR   KEGG; mmu:71458; -.
DR   UCSC; uc009sqq.1; mouse.
DR   UCSC; uc009sqr.1; mouse.
DR   UCSC; uc009sqs.1; mouse.
DR   UCSC; uc009sqt.1; mouse.
DR   CTD; 71458; -.
DR   MGI; MGI:1918708; Bcor.
DR   GeneTree; ENSGT00530000064000; -.
DR   HOVERGEN; HBG050682; -.
DR   InParanoid; Q8CGN4; -.
DR   OMA; SSSCPRM; -.
DR   OrthoDB; EOG4KPT9C; -.
DR   PhylomeDB; Q8CGN4; -.
DR   NextBio; 333823; -.
DR   ArrayExpress; Q8CGN4; -.
DR   Bgee; Q8CGN4; -.
DR   CleanEx; MM_BCOR; -.
DR   Genevestigator; Q8CGN4; -.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; IPI:MGI.
DR   GO; GO:0016564; F:transcription repressor activity; IDA:MGI.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0010553; P:negative regulation of gene-specific transcription from RNA polymerase II promoter; IDA:MGI.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 2.
DR   SMART; SM00248; ANK; 3.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ANK repeat; Chromatin regulator;
KW   Nucleus; Phosphoprotein; Repeat; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   1759       BCL-6 corepressor.
FT                                /FTId=PRO_0000066979.
FT   REPEAT     1466   1499       ANK 1.
FT   REPEAT     1500   1529       ANK 2.
FT   REPEAT     1533   1562       ANK 3.
FT   REGION      498    514       Interaction with BCL6 (By similarity).
FT   MOD_RES     392    392       N6-acetyllysine (By similarity).
FT   MOD_RES     423    423       Phosphoserine (By similarity).
FT   MOD_RES     469    469       Phosphoserine (By similarity).
FT   MOD_RES     473    473       Phosphoserine (By similarity).
FT   MOD_RES     480    480       Phosphoserine (By similarity).
FT   MOD_RES    1146   1146       Phosphoserine.
FT   MOD_RES    1293   1293       Phosphoserine (By similarity).
FT   MOD_RES    1413   1413       Phosphoserine (By similarity).
FT   VAR_SEQ    1005   1022       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_012558.
FT   VAR_SEQ    1171   1204       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_012559.
FT   CONFLICT    161    161       A -> V (in Ref. 1; AAN85318/AAN85319/
FT                                AAN85320/AAN85321).
FT   CONFLICT    167    167       G -> S (in Ref. 1; AAN85318/AAN85319/
FT                                AAN85320/AAN85321).
FT   CONFLICT    731    731       I -> V (in Ref. 1; AAN85318/AAN85319/
FT                                AAN85320/AAN85321).
FT   CONFLICT    852    852       E -> D (in Ref. 5; BAC35338).
FT   CONFLICT   1424   1424       D -> G (in Ref. 1; AAN85318/AAN85319/
FT                                AAN85320/AAN85321).
SQ   SEQUENCE   1759 AA;  192631 MW;  C7FF21CFB3C60D49 CRC64;
     MLSATPLYGN VHSWMNSERV RMCGTSEDRK IPVNDGDASK ARLELREETP LSHSVVDTSG
     AHRIDGLAAL SMDRTGLIRE GLRVPGNIVY SGLCGLGSEK GREATPSSLS GLGFSSERNP
     EMQFKPNTPE TVEASAVSGK PPNGFSAIYK TPPGIQKSAV ATAESLGLDR PASDKQSPLN
     INGASYLRLP WVNPYMEGAT PAIYPFLDSP NKYSLNMYKA LLPQQSYGLA QPLYSPVCTS
     GERFLYLPPP HYVNPHIPSS LASPMRLSTP SASAAIPPLV HCSDKSLPWK MGVNPGNPVD
     SHSYPHIQNS KQPRVTSAKA VNSGLPGDTA LLLPPSPRPS ARVHLPTQPA AETYSEFHKH
     YPRISTSPSV TLTKPYMTAN SEFSTSRLSN GKYPKALDGG DCAQSMPGHT RKTTVQDRKD
     GGSPPLLEKQ TVTKDVTDKP LDLSSKVVDA DASKGDHMKK MAPTVLVHSR AASGLVLSGS
     EIPKETLSPP GNGCSIYRSE IISTAPSSWV VPGPSPNEEN NGKSLSLKNK ALDWAIPQQR
     SSSCPRMGGT DAVVTNVSGS VSSSGRPASA SPAPNANANA DGTKTSRSSV DTTPSVIQHV
     GQPSSTPAKH GGSTSSKGAK ANPEPSFKAS ENGLPPTSIF LSPNEAFRSP AIPYPRSYLP
     YAAPEGIALS PLSLHGKGPV YPHPVLLPNG SLFPGHLAPK PGLPYGLHTS RPEFVTYQDA
     LGLGMVHPML IPHTPIEITK EEKPERRSRS HERARYEDPT LRSRFSEMLE ASSTKLHPEV
     PTDKNLKPNS SWNQGKTGVK SDKLVYVDLL REEADTKTDA GAPKAGLVAE NVGQDTEATK
     PSADPVIQQR REFISLREEL GRITDFHESF TFKQASSQPV FSLGKDSGAA GTNKENLGVQ
     VATPFLETAL GSEGPAVTFG KTQEDPKPFC VGGAPPNMDV TPAYTKEGTD EAESNDGKVL
     KPKPSKLAKR IANSAGYVGD RFKCVTTELY ADSSQLSREQ RALQMEGLQE DSILCLPAAY
     CERAMMRFSE LEMKEREGSH PATKDSEVCK FSPADWERLK GNQEKKPKSV TLEEAIADQN
     DSERCEYSTG NKHDLFEAPE DKDLPVEKYF LERPPVSEPP SDQGVVDTPH SPTLRLDRKR
     KLSGDSTHTE TAVEELAEDP LKAKRRRISK DDWPEREMTN SSSNHLEDPH CNELTNLKVC
     IELTGLHPKK QRHLLHLRER WEQQVSAAES KPGRQSRKEV AQAVQPEVTS QGTNITEEKP
     GRKKAEAKGN RGWSEESLKS CDNEQGLPVL SGSPPMKSLS STNASGKKQT QPSCTPASRL
     PAKQQKIKES QKTDVLCTGE DEDCQAASPL QKYTDNIEKP SGKRLCKTKH LIPQESRRSL
     QITGDYYVEN TDTKMTVRRF RKRPEPSSDY DLSPPAKQEP KPFDRLQQLL PATQATQLPR
     SNSPQETTQS RPMPPEARRL IVNKNAGETL LQRAARLGYE EVVLYCLENK VCDVNHRDNA
     GYCALHEACA RGWLNIVRHL LEYGADVNCS AQDGTRPLHD AVENDHLEIV RLLLSYGADP
     TLATYSGRTI MKMTHSELME KFLTDYLNDL QGRSEDDTSG AWEFYGSSVC EPDDESGYDV
     LANPPGPEDP DEEEDTYSDL FEFEFAESSL LPCYNIQVSV AQGPRNWLLL SDVLKKLKMS
     SRIFRSNFPN LEIVTIAEAE FYRQVSTSLL FSCPKDLEAF NPESKELLDL VEFTNELQTL
     LGSSVEWLHP SDTGHENYW
//
ID   NCKX4_MOUSE             Reviewed;         605 AA.
AC   Q8CGQ8; Q8BLL5; Q8BLL7;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Sodium/potassium/calcium exchanger 4;
DE   AltName: Full=Na(+)/K(+)/Ca(2+)-exchange protein 4;
DE   Flags: Precursor;
GN   Name=Slc24a4; Synonyms=Nckx4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   MEDLINE=22359087; PubMed=12379639; DOI=10.1074/jbc.M210011200;
RA   Li X.-F., Kraev A.S., Lytton J.;
RT   "Molecular cloning of a fourth member of the potassium-dependent
RT   sodium-calcium exchanger gene family, NCKX4.";
RL   J. Biol. Chem. 277:48410-48417(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-240 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CGQ8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CGQ8-2; Sequence=VSP_008375, VSP_008376, VSP_008377,
CC                                  VSP_008378;
CC   -!- TISSUE SPECIFICITY: Widely expressed in most regions of the brain,
CC       including hippocampus, neocortex, thalamus, striatum and olfactory
CC       bulb.
CC   -!- SIMILARITY: Belongs to the sodium/potassium/calcium exchanger
CC       family. SLC24A subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC31887.1; Type=Erroneous initiation;
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DR   EMBL; AY156046; AAN37415.1; -; mRNA.
DR   EMBL; AK044239; BAC31835.1; -; mRNA.
DR   EMBL; AK044368; BAC31887.1; ALT_INIT; mRNA.
DR   IPI; IPI00229553; -.
DR   IPI; IPI00355842; -.
DR   RefSeq; NP_742164.1; NM_172152.2.
DR   UniGene; Mm.312448; -.
DR   ProteinModelPortal; Q8CGQ8; -.
DR   STRING; Q8CGQ8; -.
DR   PRIDE; Q8CGQ8; -.
DR   Ensembl; ENSMUST00000079020; ENSMUSP00000078030; ENSMUSG00000041771.
DR   GeneID; 238384; -.
DR   KEGG; mmu:238384; -.
DR   UCSC; uc007oty.1; mouse.
DR   UCSC; uc007otz.1; mouse.
DR   CTD; 238384; -.
DR   MGI; MGI:2447362; Slc24a4.
DR   eggNOG; roNOG04590; -.
DR   GeneTree; ENSGT00560000076876; -.
DR   HOGENOM; HBG444187; -.
DR   HOVERGEN; HBG054881; -.
DR   InParanoid; Q8CGQ8; -.
DR   OMA; DRKLGIY; -.
DR   OrthoDB; EOG4W6NVW; -.
DR   PhylomeDB; Q8CGQ8; -.
DR   NextBio; 383757; -.
DR   ArrayExpress; Q8CGQ8; -.
DR   Bgee; Q8CGQ8; -.
DR   Genevestigator; Q8CGQ8; -.
DR   GO; GO:0005887; C:integral to plasma membrane; IC:MGI.
DR   GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0006816; P:calcium ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR004481; K-dep_Na/Ca-exchanger-like.
DR   InterPro; IPR004837; NaCa_Exmemb.
DR   Pfam; PF01699; Na_Ca_ex; 2.
DR   TIGRFAMs; TIGR00367; K_NaCaexchng; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Antiport; Calcium; Calcium transport;
KW   Glycoprotein; Ion transport; Membrane; Potassium; Potassium transport;
KW   Repeat; Signal; Sodium; Sodium transport; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     21       Potential.
FT   CHAIN        22    605       Sodium/potassium/calcium exchanger 4.
FT                                /FTId=PRO_0000019374.
FT   TOPO_DOM     22     80       Extracellular (Potential).
FT   TRANSMEM     81    101       Helical; (Potential).
FT   TOPO_DOM    102    155       Cytoplasmic (Potential).
FT   TRANSMEM    156    176       Helical; (Potential).
FT   TOPO_DOM    177    183       Extracellular (Potential).
FT   TRANSMEM    184    204       Helical; (Potential).
FT   TOPO_DOM    205    207       Cytoplasmic (Potential).
FT   TRANSMEM    208    228       Helical; (Potential).
FT   TOPO_DOM    229    407       Extracellular (Potential).
FT   TRANSMEM    408    428       Helical; (Potential).
FT   TOPO_DOM    429    440       Cytoplasmic (Potential).
FT   TRANSMEM    441    461       Helical; (Potential).
FT   TOPO_DOM    462    462       Extracellular (Potential).
FT   TRANSMEM    463    483       Helical; (Potential).
FT   TOPO_DOM    484    509       Cytoplasmic (Potential).
FT   TRANSMEM    510    530       Helical; (Potential).
FT   TOPO_DOM    531    540       Extracellular (Potential).
FT   TRANSMEM    541    561       Helical; (Potential).
FT   TOPO_DOM    562    569       Cytoplasmic (Potential).
FT   TRANSMEM    570    590       Helical; (Potential).
FT   TOPO_DOM    591    605       Extracellular (Potential).
FT   REPEAT      122    162       Alpha-1.
FT   REPEAT      478    509       Alpha-2.
FT   COMPBIAS    378    387       Poly-Pro.
FT   CARBOHYD     52     52       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     59     59       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1     47       Missing (in isoform 2).
FT                                /FTId=VSP_008375.
FT   VAR_SEQ     258    276       Missing (in isoform 2).
FT                                /FTId=VSP_008376.
FT   VAR_SEQ     557    566       LGIHLNKWRL -> SFCHFQTGAP (in isoform 2).
FT                                /FTId=VSP_008377.
FT   VAR_SEQ     567    605       Missing (in isoform 2).
FT                                /FTId=VSP_008378.
FT   CONFLICT    413    413       T -> M (in Ref. 2; BAC31835).
SQ   SEQUENCE   605 AA;  66866 MW;  A32D256278FB0686 CRC64;
     MLPQQVGFVC AVLALVCCAS GLFGSLGHKT ASAGKHVLLD TWRNRKLMAP INGTPLAKNC
     TDPAIHEFPT DLFSNKERQH GAVLLHILGA LYMFYALAIV CDDFFVPSLE KICEKLHLSE
     DVAGATFMAA GSSTPELFAS VIGVFITHGD VGVGTIVGSA VFNILCIIGV CGLFAGQVVR
     LTWWAVCRDS VYYTLSVIVL IAFIYDEEIV WWEGLVLIIL YVFYILIMKY NMKMQTFFTT
     KQKSIANGNP VSNELEDGND LYDGSYDDPS VPLLGQVKEK PPYGKTPVVM VDEILSSSPP
     KFTFPEAGLR IMITNKFGPR TRLRMASRII INERQRLINS ANGVNSKPLQ NGRHENMENG
     NVPVENPEDP QQGQEQQPPP QPPPPEPESV ETVFLSPFSM PEAKGDKAKW VFTWPLIFLL
     CVTIPNCSKP RWEKFFMVTF ITATLWIAVF SYLMVWLVTI IGYTLGIPDV IMGITFLAAG
     TSVPDCMASL IVARQGLGDM AVSNTIGSNV FDILVGLGIP WGLQTMVINY GSTVKINSRG
     LVYSVVLLLG SVALTVLGIH LNKWRLDRKL GIYVLVLYAV FLCFSIMIEF NVFTFVNLPM
     CREDD
//
ID   CACO1_MOUSE             Reviewed;         691 AA.
AC   Q8CGU1; Q5DTX0; Q9D935;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Calcium-binding and coiled-coil domain-containing protein 1;
DE   AltName: Full=Coiled-coil coactivator protein;
GN   Name=Calcoco1; Synonyms=CocoA, Kiaa1536;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH GRIP1, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=14690606; DOI=10.1016/S1097-2765(03)00450-7;
RA   Kim J.H., Li H., Stallcup M.R.;
RT   "CoCoA, a nuclear receptor coactivator which acts through an N-
RT   terminal activation domain of p160 coactivators.";
RL   Mol. Cell 12:1537-1549(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pancreas, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=15522220; DOI=10.1016/j.bbrc.2004.10.021;
RA   Takahashi K., Inuzuka M., Ingi T.;
RT   "Cellular signaling mediated by calphoglin-induced activation of IPP
RT   and PGM.";
RL   Biochem. Biophys. Res. Commun. 325:203-214(2004).
RN   [6]
RP   INTERACTION WITH AHR AND ARNT.
RX   PubMed=15383530; DOI=10.1074/jbc.M408535200;
RA   Kim J.H., Stallcup M.R.;
RT   "Role of the coiled-coil coactivator (CoCoA) in aryl hydrocarbon
RT   receptor-mediated transcription.";
RL   J. Biol. Chem. 279:49842-49848(2004).
RN   [7]
RP   INTERACTION WITH CTNNB; GRIP1 AND P300.
RX   PubMed=16344550; DOI=10.1074/jbc.M510403200;
RA   Yang C.K., Kim J.H., Li H., Stallcup M.R.;
RT   "Differential use of functional domains by coiled-coil coactivator in
RT   its synergistic coactivator function with beta-catenin or GRIP1.";
RL   J. Biol. Chem. 281:3389-3397(2006).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CTNNB, AND
RP   MUTAGENESIS OF PHE-17 AND VAL-20.
RX   PubMed=16931570; DOI=10.1210/me.2006-0200;
RA   Yang C.K., Kim J.H., Stallcup M.R.;
RT   "Role of the N-terminal activation domain of the coiled-coil
RT   coactivator in mediating transcriptional activation by beta-catenin.";
RL   Mol. Endocrinol. 20:3251-3262(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Functions as a coactivator for aryl hydrocarbon and
CC       nuclear receptors (NR). Recruited to promoters through its contact
CC       with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS)
CC       domain of transcription factors or coactivators, such as NCOA2.
CC       During ER-activation acts synergistically in combination with
CC       other NCOA2-binding proteins, such as EP300, CREBBP and CARM1.
CC       Involved in the transcriptional activation of target genes in the
CC       Wnt/CTNNB1 pathway. Functions as a secondary coactivator in LEF1-
CC       mediated transcriptional activation via its interaction with
CC       CTNNB1. Coactivator function for nuclear receptors and LEF1/CTNNB1
CC       involves differential utilization of two different activation
CC       regions.
CC   -!- SUBUNIT: Part of a calphoglin complex consisting of CALCOCO1, PPA1
CC       and PGM (By similarity). Interacts with the bHLH-PAS domains of
CC       GRIP1, AHR and ARNT. Interacts with CTNNB1 via both its N- and C-
CC       terminal regions. Interacts with EP300.
CC   -!- INTERACTION:
CC       O42486:chBcat (xeno); NbExp=2; IntAct=EBI-972374, EBI-972394;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between
CC       nucleus and cytoplasm.
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined except
CC       spleen, with high levels of expression in the heart and kidney.
CC   -!- DOMAIN: The C-terminal activation region (AD) is used for
CC       downstream signaling. Seems to be essential for coactivator
CC       function with nuclear receptors and with the aryl hydrocarbon
CC       receptor.
CC   -!- DOMAIN: The N-terminal activation region (AD) is necessary and
CC       sufficient for synergistic activation of LEF1-mediated
CC       transcription by CTNNB1. Contains a EP3000 binding region which is
CC       important for synergistic cooperation.
CC   -!- DOMAIN: Recruitment by nuclear receptors is accomplished by the
CC       interaction of the coiled-coiled domain with p160 coactivators.
CC   -!- SIMILARITY: Belongs to the CALCOCO family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90452.1; Type=Erroneous initiation;
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DR   EMBL; AY131329; AAN10148.1; -; mRNA.
DR   EMBL; AK007393; BAB25009.1; -; mRNA.
DR   EMBL; AK035598; BAC29119.1; -; mRNA.
DR   EMBL; AK220400; BAD90452.1; ALT_INIT; mRNA.
DR   EMBL; BC054783; AAH54783.1; -; mRNA.
DR   IPI; IPI00461826; -.
DR   RefSeq; NP_080468.1; NM_026192.3.
DR   UniGene; Mm.71682; -.
DR   ProteinModelPortal; Q8CGU1; -.
DR   IntAct; Q8CGU1; 5.
DR   STRING; Q8CGU1; -.
DR   PhosphoSite; Q8CGU1; -.
DR   PRIDE; Q8CGU1; -.
DR   Ensembl; ENSMUST00000023818; ENSMUSP00000023818; ENSMUSG00000023055.
DR   GeneID; 67488; -.
DR   KEGG; mmu:67488; -.
DR   CTD; 67488; -.
DR   MGI; MGI:1914738; Calcoco1.
DR   eggNOG; roNOG10167; -.
DR   GeneTree; ENSGT00530000063216; -.
DR   HOGENOM; HBG713292; -.
DR   HOVERGEN; HBG107573; -.
DR   InParanoid; Q8CGU1; -.
DR   OMA; ELLEYMR; -.
DR   OrthoDB; EOG4NZTTD; -.
DR   PhylomeDB; Q8CGU1; -.
DR   NextBio; 324722; -.
DR   ArrayExpress; Q8CGU1; -.
DR   Bgee; Q8CGU1; -.
DR   CleanEx; MM_CALCOCO1; -.
DR   Genevestigator; Q8CGU1; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000790; C:nuclear chromatin; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
DR   GO; GO:0030518; P:steroid hormone receptor signaling pathway; IDA:HGNC.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR012852; CoCoA.
DR   Pfam; PF07888; CALCOCO1; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Nucleus; Phosphoprotein;
KW   Wnt signaling pathway.
FT   CHAIN         1    691       Calcium-binding and coiled-coil domain-
FT                                containing protein 1.
FT                                /FTId=PRO_0000308900.
FT   REGION        1    190       N-terminal AD (CTNNB1 binding site).
FT   REGION        1     30       p300 KIX-binding.
FT   REGION      501    691       C-terminal AD (CTNNB1 binding site).
FT   COILED      145    205       Potential.
FT   COILED      232    339       Potential.
FT   COILED      417    514       Potential.
FT   MOD_RES     563    563       Phosphoserine.
FT   MUTAGEN      17     17       F->A: Loss of interaction with p300 KIX
FT                                domain; eliminated the autonomous
FT                                transactivation function.
FT   MUTAGEN      20     20       V->A: Reduced binding to p300 KIX domain;
FT                                severe reduction in the autonomous
FT                                transactivation function.
FT   MUTAGEN      20     20       V->P: Reduced binding to p300 KIX domain;
FT                                severe reduction in the autonomous
FT                                transactivation function.
FT   CONFLICT    301    301       E -> Q (in Ref. 1; AAN10148 and 3;
FT                                BAD90452).
SQ   SEQUENCE   691 AA;  77280 MW;  4759E5478839D9B7 CRC64;
     MEESSLSRAP SRGGVNFLNV ARTYIPNTKV ECHYTLPPGT MPSASDWIGI FKVEAACVRD
     YHTFVWSSVP ESTTDGSPTH ASVQFQASYL PKPGAQLYQF RYVNRQGRVC GQSPPFQFRE
     PRPMDELVTL EEADGGSDIL LVVPKATVLQ NQLDESQQER NDLMQLKLQL EDQVTELRSR
     VQELEAALAT ARQEHSELTE QYKGLSRSHG ELSEERDILS QQQGDHVARI LELEDDIQTM
     SDKVLMKEVE LDRVRDTVKA LTREQEKLLR QLKEFQADKE QSEAELQTVR EENCCLNTEL
     EEAKSRQEEQ GAQVQRLKDK LAHMKDTLGQ AQQKVAELEP LKEQLRGVQE LAASSQQKAA
     LLGEELASAA GARDRTIAEL HRSRLEVAEV NGRLAELSLH MKEEKCQWSK ERTGLLQSME
     AEKDKILKLS AEILRLEKTV QEERTQSHVF KTELAREKDS SLVQLSESKR ELTELRSALR
     VLQKEKEQLQ TEKQELLEYM RKLEARLEKV ADEKWTEDAA TEDEEATAGL SCPASLTDSE
     DESPEDMRLP SYGLCESGNT SSSPPGPREP SSLVVINQPA PIAPQFSGPG EASSSDSEAE
     DEKSVLMAAV QSGGEEASLL LPELGSAFYD VASAFTVSSL SEASPGVPAN PPWKECPICK
     ERFPAESDKD ALEGHMDGHF FFSTQDPFTF E
//
ID   TPH2_MOUSE              Reviewed;         488 AA.
AC   Q8CGV2;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Tryptophan 5-hydroxylase 2;
DE            EC=1.14.16.4;
DE   AltName: Full=Neuronal tryptophan hydroxylase;
DE   AltName: Full=Tryptophan 5-monooxygenase 2;
GN   Name=Tph2; Synonyms=Ntph;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=22400097; PubMed=12511643; DOI=10.1126/science.1078197;
RA   Walther D.J., Peter J.-U., Bashammakh S., Hortnagl H., Voits M.,
RA   Fink H., Bader M.;
RT   "Synthesis of serotonin by a second tryptophan hydroxylase isoform.";
RL   Science 299:76-76(2003).
CC   -!- CATALYTIC ACTIVITY: L-tryptophan + tetrahydrobiopterin + O(2) = 5-
CC       hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin.
CC   -!- COFACTOR: Fe(2+) ion (By similarity).
CC   -!- PATHWAY: Aromatic compound metabolism; serotonin biosynthesis;
CC       serotonin from L-tryptophan: step 1/2.
CC   -!- TISSUE SPECIFICITY: Brain specific.
CC   -!- SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid
CC       hydroxylase family.
CC   -!- SIMILARITY: Contains 1 ACT domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY090565; AAM08923.1; -; mRNA.
DR   IPI; IPI00229583; -.
DR   UniGene; Mm.31597; -.
DR   ProteinModelPortal; Q8CGV2; -.
DR   SMR; Q8CGV2; 53-482.
DR   STRING; Q8CGV2; -.
DR   PhosphoSite; Q8CGV2; -.
DR   PRIDE; Q8CGV2; -.
DR   Ensembl; ENSMUST00000006949; ENSMUSP00000006949; ENSMUSG00000006764.
DR   MGI; MGI:2651811; Tph2.
DR   GeneTree; ENSGT00390000010268; -.
DR   HOGENOM; HBG484724; -.
DR   HOVERGEN; HBG006841; -.
DR   InParanoid; Q8CGV2; -.
DR   OrthoDB; EOG4S7JPZ; -.
DR   BRENDA; 1.14.16.4; 244.
DR   ArrayExpress; Q8CGV2; -.
DR   Bgee; Q8CGV2; -.
DR   CleanEx; MM_TPH2; -.
DR   Genevestigator; Q8CGV2; -.
DR   GermOnline; ENSMUSG00000006764; Mus musculus.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004510; F:tryptophan 5-monooxygenase activity; IDA:MGI.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0006587; P:serotonin biosynthetic process from tryptophan; IC:MGI.
DR   InterPro; IPR002912; ACT-bd.
DR   InterPro; IPR001273; ArAA_hydroxylase.
DR   InterPro; IPR018301; ArAA_hydroxylase_Fe/CU_BS.
DR   InterPro; IPR019774; Aromatic-AA_hydroxylase_C.
DR   InterPro; IPR005963; Trp_5_mOase.
DR   InterPro; IPR019773; Tyrosine_3-monooxygenase-like.
DR   Gene3D; G3DSA:1.10.800.10; Aaa_hydroxylase; 1.
DR   PANTHER; PTHR11473; Aaa_hydroxylase; 1.
DR   Pfam; PF01842; ACT; 1.
DR   Pfam; PF00351; Biopterin_H; 1.
DR   PIRSF; PIRSF000336; TH; 1.
DR   PRINTS; PR00372; FYWHYDRXLASE.
DR   SUPFAM; SSF56534; Aaa_hydroxylase; 1.
DR   TIGRFAMs; TIGR01270; Trp_5_monoox; 1.
DR   PROSITE; PS00367; BH4_AAA_HYDROXYL_1; 1.
DR   PROSITE; PS51410; BH4_AAA_HYDROXYL_2; 1.
PE   2: Evidence at transcript level;
KW   Iron; Metal-binding; Monooxygenase; Oxidoreductase; Phosphoprotein;
KW   Serotonin biosynthesis.
FT   CHAIN         1    488       Tryptophan 5-hydroxylase 2.
FT                                /FTId=PRO_0000205575.
FT   DOMAIN       62    134       ACT.
FT   METAL       316    316       Iron (By similarity).
FT   METAL       321    321       Iron (By similarity).
FT   METAL       361    361       Iron (By similarity).
FT   MOD_RES     380    380       Phosphoserine (By similarity).
FT   MOD_RES     390    390       Phosphoserine (By similarity).
SQ   SEQUENCE   488 AA;  55918 MW;  8769FB4DAEE80E4A CRC64;
     MQPAMMMFSS KYWARRGLSL DSAVPEDHQL LGSLTQNKAI KSEDKKSGKE PGKGDTTESS
     KTAVVFSLKN EVGGLVKALR LFQEKHVNML HIESRRSRRR SSEVEIFVDC ECGKTEFNEL
     IQLLKFQTTI VTLNPPESIW TEEEDLEDVP WFPRKISELD RCSHRVLMYG TELDADHPGF
     KDNVYRQRRK YFVDVAMGYK YGQPIPRVEY TEEETKTWGV VFRELSKLYP THACREYLKN
     LPLLTKYCGY REDNVPQLED VSMFLKERSG FTVRPVAGYL SPRDFLAGLA YRVFHCTQYV
     RHGSDPLYTP EPDTCHELLG HVPLLADPKF AQFSQEIGLA SLGASDEDVQ KLATCYFFTI
     EFGLCKQEGQ LRAYGAGLLS SIGELKHALS DKACVKSFDP KTTCLQECLI TTFQDAYFVS
     DSFEEAKEKM RDFAKSITRP FSVYFNRYTQ SIEILKDTRS IENVVQDLRS DLNTVCDALN
     KMNQYLGI
//
ID   CHERP_MOUSE             Reviewed;         936 AA.
AC   Q8CGZ0; Q8K291; Q8VCD2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Calcium homeostasis endoplasmic reticulum protein;
DE   AltName: Full=SR-related CTD-associated factor 6;
GN   Name=Cherp; Synonyms=Scaf6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Sampson N.D., Hewitt J.E.;
RT   "Functional characterization of the novel SR-related CTD associated
RT   factor, SCAF6.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-723, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-822, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826 AND THR-828, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Involved in calcium homeostasis, growth and
CC       proliferation (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       perinuclear region (By similarity). Endoplasmic reticulum (By
CC       similarity). Note=Distributed throughout the cytoplasm and also
CC       localizes to the perinuclear region. Colocalizes with ITPR1 (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 CID domain.
CC   -!- SIMILARITY: Contains 1 G-patch domain.
CC   -!- SIMILARITY: Contains 1 SURP motif repeat.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF536541; AAN77182.1; -; mRNA.
DR   EMBL; BC020488; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00229604; -.
DR   RefSeq; NP_613051.3; NM_138585.3.
DR   UniGene; Mm.30136; -.
DR   HSSP; Q8CH02; 1UG0.
DR   ProteinModelPortal; Q8CGZ0; -.
DR   SMR; Q8CGZ0; 5-67.
DR   IntAct; Q8CGZ0; 1.
DR   PhosphoSite; Q8CGZ0; -.
DR   PRIDE; Q8CGZ0; -.
DR   Ensembl; ENSMUST00000079510; ENSMUSP00000078469; ENSMUSG00000052488.
DR   GeneID; 27967; -.
DR   KEGG; mmu:27967; -.
DR   UCSC; uc009mgb.1; mouse.
DR   CTD; 27967; -.
DR   MGI; MGI:106417; Cherp.
DR   eggNOG; roNOG15209; -.
DR   GeneTree; ENSGT00600000084415; -.
DR   HOGENOM; HBG445457; -.
DR   HOVERGEN; HBG052716; -.
DR   InParanoid; Q8CGZ0; -.
DR   OrthoDB; EOG4BCDMG; -.
DR   NextBio; 306460; -.
DR   ArrayExpress; Q8CGZ0; -.
DR   Bgee; Q8CGZ0; -.
DR   CleanEx; MM_CHERP; -.
DR   Genevestigator; Q8CGZ0; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   InterPro; IPR006903; DUF618.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR000467; G_patch.
DR   InterPro; IPR006569; RNA_polymerase_II_lsu_CTD.
DR   InterPro; IPR000061; Surp.
DR   Gene3D; G3DSA:1.25.40.90; ENTH_VHS; 1.
DR   Pfam; PF04818; DUF618; 1.
DR   Pfam; PF01585; G-patch; 1.
DR   Pfam; PF01805; Surp; 1.
DR   SMART; SM00443; G_patch; 1.
DR   SMART; SM00582; RPR; 1.
DR   SMART; SM00648; SWAP; 1.
DR   SUPFAM; SSF48464; ENTH_VHS; 1.
DR   PROSITE; PS51391; CID; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
DR   PROSITE; PS50128; SURP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Endoplasmic reticulum; Phosphoprotein.
FT   CHAIN         1    936       Calcium homeostasis endoplasmic reticulum
FT                                protein.
FT                                /FTId=PRO_0000299493.
FT   REPEAT       15     57       SURP motif.
FT   DOMAIN      149    289       CID.
FT   DOMAIN      850    900       G-patch.
FT   COMPBIAS    279    355       Gln-rich.
FT   COMPBIAS    343    691       Pro-rich.
FT   COMPBIAS    727    825       Arg-rich.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      18     18       N6-acetyllysine (By similarity).
FT   MOD_RES     723    723       Phosphotyrosine.
FT   MOD_RES     822    822       Phosphoserine.
FT   MOD_RES     824    824       Phosphoserine (By similarity).
FT   MOD_RES     826    826       Phosphoserine.
FT   MOD_RES     828    828       Phosphothreonine.
FT   MOD_RES     831    831       Phosphoserine (By similarity).
FT   MOD_RES     837    837       Phosphoserine (By similarity).
FT   MOD_RES     839    839       Phosphoserine (By similarity).
FT   MOD_RES     888    888       N6-acetyllysine (By similarity).
FT   MOD_RES     910    910       N6-acetyllysine (By similarity).
FT   MOD_RES     913    913       Phosphoserine (By similarity).
FT   CONFLICT    348    349       Missing (in Ref. 2; BC020488).
SQ   SEQUENCE   936 AA;  106169 MW;  8C29DF0822CA9EB3 CRC64;
     MEMPMPPDDQ ELRNVIDKLA QFVARNGPEF EKMTMEKQKD NPKFSFLFGG EFYSYYKCKL
     ALEQQQLICK QQAPELEPTS AMPPLPQPPL APTASLTPAQ GTPSMDELIQ QSQWSLQQQE
     QHLLALRQEQ VTTAVAHAVE QQMQKLLEET QLDMSEFDNL LQPIIDTCTK DAISAGKNWM
     FSNAKSPPHC ELMAGHLRNR ITADGAHFEL RLHLIYLIND VLHHCQRKQA RELLAALQKV
     VVPIYCTSFL AVEEDKQQKI ARLLQLWEKN GYFDDSIIQQ LQSPALGLGQ YQATLINEYS
     SVVQPVQLAF QQQIQSLKTQ HEEFVSSLAQ QQQQQQQQQQ QQPQPQPQPQ IQLPQMEADV
     KATPPPPAPP PASAPAPTIP PTTQPDDNKP PIQMPGSSEY DTSAGVQDPA AAGPRGPGPH
     EQIPPNKPPW FDQPHPVAPW GQQQPPEQPP YPHHQGGPPH CPPWNNSHEG MWGEQRGDPG
     WNGQRDAPWN NQPDPNWNNQ FEGPWNNQHE PPPWGGAQRE PPFRMQRPPH FRGPFPPHQQ
     HPQFNQPPHP HNFNRFPPRF MQDDFPPRHP FERPPYPHRF DYPQGDFPAD MGPPHHHPGH
     RMPHPGINEH PPWAGPQHPD FGPPPHGFNG QPPHMRRQGP PHINHDDPSL VPNVPYFDLP
     AGLMAPLVKL EDHEYKPLDP KDIRLPPPMP PSERLLAAVE AFYSPPSHDR PRNSEGWEQN
     GLYEFFRAKM RARRRKGQEK RNSGPSRSRS RSKSRGRSSS RSSSRSSKSS RSSSRSHSRS
     RSRSSSRSRS RSRSRSRSSR SRSRSRSRSR SKSYSPGRRR RSRSRSPTPP SAAGLGSNSA
     PPIPDSRLGE ENKGHQMLVK MGWSGSGGLG AKEQGIQDPI KGGDVRDKWD QYKGVGVALD
     DPYENYRRNK SYSFIARMKA RDEFSTFGTR KEEKED
//
ID   SUGP2_MOUSE             Reviewed;        1067 AA.
AC   Q8CH09; Q6PG19; Q80UY8; Q8BY32; Q8CFM0;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=SURP and G-patch domain-containing protein 2;
DE   AltName: Full=Arginine/serine-rich-splicing factor 14;
DE   AltName: Full=Splicing factor, arginine/serine-rich 14;
GN   Name=Sugp2; Synonyms=Sfrs14, Srsf14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RX   MEDLINE=22482436; PubMed=12594045; DOI=10.1016/S0378-1119(02)01230-1;
RA   Sampson N.D., Hewitt J.E.;
RT   "SF4 and SFRS14, two related putative splicing factors on human
RT   chromosome 19p13.11.";
RL   Gene 305:91-100(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-666.
RC   STRAIN=C57BL/6, and FVB/N;
RC   TISSUE=Brain, Mammary gland, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in mRNA splicing (Potential).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 G-patch domain.
CC   -!- SIMILARITY: Contains 2 SURP motif repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH57305.1; Type=Frameshift; Positions=679;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF518875; AAN77118.1; -; mRNA.
DR   EMBL; AK042293; BAC31218.1; -; mRNA.
DR   EMBL; BC023276; AAH23276.1; -; mRNA.
DR   EMBL; BC042763; AAH42763.1; -; mRNA.
DR   EMBL; BC057305; AAH57305.1; ALT_FRAME; mRNA.
DR   IPI; IPI00405760; -.
DR   RefSeq; NP_001161762.1; NM_001168290.1.
DR   RefSeq; NP_766343.3; NM_172755.3.
DR   UniGene; Mm.284505; -.
DR   ProteinModelPortal; Q8CH09; -.
DR   SMR; Q8CH09; 572-622, 759-825.
DR   PhosphoSite; Q8CH09; -.
DR   PRIDE; Q8CH09; -.
DR   Ensembl; ENSMUST00000093458; ENSMUSP00000091167; ENSMUSG00000036054.
DR   GeneID; 234373; -.
DR   KEGG; mmu:234373; -.
DR   NMPDR; fig|10090.3.peg.18656; -.
DR   UCSC; uc009lzl.1; mouse.
DR   CTD; 234373; -.
DR   MGI; MGI:2678085; Sugp2.
DR   eggNOG; roNOG15117; -.
DR   GeneTree; ENSGT00410000025695; -.
DR   HOGENOM; HBG402969; -.
DR   HOVERGEN; HBG079176; -.
DR   InParanoid; Q8CH09; -.
DR   OMA; QTFSLAS; -.
DR   OrthoDB; EOG4QFWCG; -.
DR   PhylomeDB; Q8CH09; -.
DR   NextBio; 382135; -.
DR   ArrayExpress; Q8CH09; -.
DR   Bgee; Q8CH09; -.
DR   CleanEx; MM_SFRS14; -.
DR   Genevestigator; Q8CH09; -.
DR   GermOnline; ENSMUSG00000036054; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR000467; G_patch.
DR   InterPro; IPR000061; Surp.
DR   Pfam; PF01585; G-patch; 1.
DR   Pfam; PF01805; Surp; 1.
DR   SMART; SM00443; G_patch; 1.
DR   SMART; SM00648; SWAP; 2.
DR   PROSITE; PS50174; G_PATCH; 1.
DR   PROSITE; PS50128; SURP; 1.
PE   2: Evidence at transcript level;
KW   mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism;
KW   Repeat.
FT   CHAIN         1   1067       SURP and G-patch domain-containing
FT                                protein 2.
FT                                /FTId=PRO_0000097709.
FT   REPEAT      573    616       SURP motif 1.
FT   REPEAT      770    813       SURP motif 2.
FT   DOMAIN      996   1042       G-patch.
FT   MOTIF       980    985       Nuclear localization signal (Potential).
FT   COMPBIAS    844    884       Glu-rich.
FT   MOD_RES     265    265       Phosphothreonine (By similarity).
FT   MOD_RES     267    267       Phosphoserine (By similarity).
FT   MOD_RES     756    756       Phosphoserine (By similarity).
FT   MOD_RES     925    925       Phosphoserine (By similarity).
FT   VARIANT     666    666       I -> L (in strain: FVB/N).
FT   CONFLICT    923    923       G -> A (in Ref. 1; AAN77118).
FT   CONFLICT    949    949       P -> T (in Ref. 2; BAC31218).
SQ   SEQUENCE   1067 AA;  118103 MW;  8A191DC7C71C4949 CRC64;
     MAARRMAQES LDSVLQEKSK RYGDSEAVGE ALHLKAQDLL RTGSRARADV YEDIHGDSRY
     SASGSGVYSL DMGREGLRGD MFVGPSFRSS NQSVGEDSYL RKECGRDLEP AHTDSRDQSF
     GHRNLGHFPS QDWKLALRGS WEQDLGHSVS QESSWSQEYG FGPSLLGDLA SSRRMEKESR
     DYDLDHPGEV DSVSRSSGQV LTRGRSLNIA DQEGTLLGKG DTQGLLGAKG VGKLITLKSM
     TTKKIPVASR ITSKPQGTNQ IQKPTPSPDV TIGTSPVLDE IQFAALKIPL GLDLRTLGLP
     RRKMGFDAID KADVFSRFGI EIIKWAGFHT IKDDLKFSQL FQTLFELETE TCAKMLASFK
     CSLKPEHRDF CFFTIKFLKH SALKTPRVDN EFLNMLLDKG AVKTKNCFFE IIKPFDKSIM
     RLQDRLLKGV TPLLMACNAY ELSVKMKTLT SPLDLAMALE TTNSLCRKSL ALLGQTFSLA
     SSFRQEKILE AVGLQDIAPS PAYFPNFEDS TLFGREYIDH LKAWLMASGY PLQLKRAVPP
     ESREQKTTAQ TWASSTLSQA VPQRADHRVV DTIDQLVMRV IQGRLSPRER TLLLQDPAYW
     FLSDESSLEY KYYKLKLAES QRLNHSWPIV ERRPTPAQCA VRAMLYAQAV RSLKRRLLPW
     QRRRLIRSQG PRGLKAKKAT TAQQTSLSSG TRQKHHGRQA SGSLRVKPPP RDSSDAAQDC
     LSEPAKPCPQ PSSPGALGPS PRPTGADDSE ALPASSRCPS ANMDAKTMET AEKLARFVAQ
     VGPEIEQFSI ENSTDNPDLW FLHDQSSSAF KFYREKVLEL CPSISFQSTG EAGDSVQSPT
     AGKEGKGEPQ EGHPEQEASL EGTEVLPEEE EEDEEESEDE GGEETSTLRP QAGAAKCPGS
     EGSSPTDSIP GEGSREDQAS TPGLSQASSG SCFPRKRISS KSLKVGMIPA PKRVCLIQES
     KVHEPVRIAY DRPRGRPIAK KKKPKDMEFS QQKLTDKNVG FQMLQKMGWK EGHGLGSLGK
     GIREPVSVGA LSEGEGLGAD GPEQKEDTFD VFRQRMMQMY RHKRASK
//
ID   SLTM_MOUSE              Reviewed;        1031 AA.
AC   Q8CH25; Q3UYE5; Q8BP76; Q8BR40; Q8VCF4; Q9CS57;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=SAFB-like transcription modulator;
DE   AltName: Full=Modulator of estrogen-induced transcription;
DE   AltName: Full=SAF-like transcription modulator;
GN   Name=Sltm; Synonyms=Met;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=17630952; DOI=10.1042/BJ20070170;
RA   Chan C.W., Lee Y.-B., Uney J., Flynn A., Tobias J.H., Norman M.;
RT   "A novel member of the SAF (scaffold attachment factor)-box protein
RT   family inhibits gene expression and induces apoptosis.";
RL   Biochem. J. 407:355-362(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-582 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 425-1031 (ISOFORM 1/2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Corpora quadrigemina, Embryo, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 528-1031 (ISOFORM 1/2).
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-552, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289 AND SER-552, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289 AND SER-552, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-999, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: When overexpressed, acts as a general inhibitor of
CC       transcription that eventually leads to apoptosis.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Detected in punctate
CC       structures.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CH25-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CH25-2; Sequence=VSP_028834;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -!- SIMILARITY: Contains 1 SAP domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH19992.1; Type=Erroneous initiation;
CC       Sequence=BAC32471.1; Type=Erroneous initiation;
CC       Sequence=BAE22267.1; Type=Erroneous initiation;
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DR   EMBL; AF462146; AAO15605.1; -; mRNA.
DR   EMBL; AK017839; BAB30967.1; -; mRNA.
DR   EMBL; AK045723; BAC32471.1; ALT_INIT; mRNA.
DR   EMBL; AK077578; BAC36873.1; -; mRNA.
DR   EMBL; AK134756; BAE22267.1; ALT_INIT; mRNA.
DR   EMBL; BC019992; AAH19992.1; ALT_INIT; mRNA.
DR   IPI; IPI00229571; -.
DR   IPI; IPI00556695; -.
DR   RefSeq; NP_079966.2; NM_025690.3.
DR   RefSeq; NP_080613.1; NM_026337.1.
DR   UniGene; Mm.22379; -.
DR   HSSP; Q9UH33; 2CQ3.
DR   ProteinModelPortal; Q8CH25; -.
DR   SMR; Q8CH25; 22-61.
DR   STRING; Q8CH25; -.
DR   PhosphoSite; Q8CH25; -.
DR   PRIDE; Q8CH25; -.
DR   Ensembl; ENSMUST00000049263; ENSMUSP00000049112; ENSMUSG00000032212.
DR   GeneID; 66660; -.
DR   KEGG; mmu:66660; -.
DR   UCSC; uc009qok.1; mouse.
DR   CTD; 66660; -.
DR   MGI; MGI:1913910; Sltm.
DR   GeneTree; ENSGT00590000082875; -.
DR   HOGENOM; HBG715703; -.
DR   HOVERGEN; HBG096731; -.
DR   InParanoid; Q8CH25; -.
DR   OMA; NGSSGQT; -.
DR   OrthoDB; EOG4DNF4Q; -.
DR   PhylomeDB; Q8CH25; -.
DR   NextBio; 322303; -.
DR   ArrayExpress; Q8CH25; -.
DR   Bgee; Q8CH25; -.
DR   CleanEx; MM_MET; -.
DR   CleanEx; MM_SLTM; -.
DR   Genevestigator; Q8CH25; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR003034; SAP_DNA-bd.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF02037; SAP; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00513; SAP; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS50800; SAP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Apoptosis; Coiled coil; Nucleus;
KW   Phosphoprotein; Repressor; RNA-binding; Transcription;
KW   Transcription regulation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1031       SAFB-like transcription modulator.
FT                                /FTId=PRO_0000307799.
FT   DOMAIN       22     56       SAP.
FT   DOMAIN      384    462       RRM.
FT   COILED      107    182       Potential.
FT   COILED      608    727       Potential.
FT   COMPBIAS    108    239       Glu-rich.
FT   COMPBIAS    568    903       Arg/Glu-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      74     74       Phosphothreonine (By similarity).
FT   MOD_RES      93     93       Phosphoserine (By similarity).
FT   MOD_RES      97     97       Phosphoserine (By similarity).
FT   MOD_RES     139    139       Phosphoserine.
FT   MOD_RES     244    244       Phosphoserine (By similarity).
FT   MOD_RES     289    289       Phosphoserine.
FT   MOD_RES     401    401       N6-acetyllysine (By similarity).
FT   MOD_RES     406    406       N6-acetyllysine (By similarity).
FT   MOD_RES     421    421       Phosphoserine (By similarity).
FT   MOD_RES     549    549       Phosphoserine (By similarity).
FT   MOD_RES     550    550       Phosphoserine (By similarity).
FT   MOD_RES     552    552       Phosphoserine.
FT   MOD_RES     589    589       Phosphoserine (By similarity).
FT   MOD_RES     747    747       Phosphoserine (By similarity).
FT   MOD_RES     999    999       Phosphoserine.
FT   MOD_RES    1011   1011       Phosphoserine (By similarity).
FT   MOD_RES    1021   1021       N6-acetyllysine (By similarity).
FT   VAR_SEQ     197    214       Missing (in isoform 2).
FT                                /FTId=VSP_028834.
FT   CONFLICT      4      4       A -> R (in Ref. 2; BAB30967).
FT   CONFLICT    985    985       R -> Q (in Ref. 2; BAE22267).
SQ   SEQUENCE   1031 AA;  116919 MW;  DBD3F617F816C79C CRC64;
     MAAAAGAVVA SAASGPAEGK KITELRVIDL RSELKRRNLD INGVKTVLVS RLKQAIEEEG
     GDPDNIELTV STDTPNKKPT KGKGKKQEAD ELSGDASVED DSFVKDCELE NQETHDQDGN
     EELKDLEEFG ENEEEIVHSQ ELLSTEENKT TQEFVEAEAI EDREKEDIES QETEAQEGED
     DTFLTAQDGE EEENEKDIAG SGDGTQEVSK PLPSEGSLAE ADHTAHEEME ANATGKEAED
     DNISVTIQAE DAITLDFDGD DLLETGKNVK ITDSEASKPK DVQDAIAQSP EKEAKDYEMN
     PNHKDGKKED SVKGEPVEKE ARESAKKAES GDKEKDTLKK GPSSTGASGQ AKSSSKESKD
     SKTSSKDDKG STGSAGGSSG SSTKNIWVSG LSSNTKAADL KNLFGKYGKV LSAKVVTNAR
     SPGAKCYGIV TMSSSTEVSR CVAHLHRTEL HGQLISVEKV KGDPSKKEMK KENDEKSSSR
     SAGDKKNASD RSAKTQASIK KEEKRSSEKS EKKESKDTKK IEKDEKNDDG PSGQTSESLK
     KSEEKKRISS KSPGHMVILN QTKGDHCRPS RRGRYEKGHG RSKEKERASL DKKRDKDYRR
     KEILPFEKMK EQRLREHLVR FERLKQAVEF RRRKEIAERE RRERERIRII REREERERLQ
     RERERLEIER QKLERERMER ERLERERIRI EQERRREAER IAREREELRR QQQQLRYEQE
     KRNSLKRPRD VDHRRDDPYW SENKKLSLDT EARFGHGSDY RQQSRFLDFS HRERARFPDT
     ASVQSSFERR ERFVGQSEGK KPRPAARREE PSFERYPKNF SDSRRNEPPP PRNELRETDR
     REVRGERDER RTVILHDRPE VAHPRHPRET VPNPSRPTSW KSEANMSTEK RESRVERPER
     SGREVSGHTV RGAPPGNRSS ASGYGTREGE RGVIADRGSG TQHYPEERHV VERHGRDTSG
     PRKEWHGPPS QGPSYHDTRR MGDGRAGAGM ITQHSSTASP VNRIVQMSGN SLPRGSSSGF
     KPFKSGPPRR F
//
ID   TRI32_MOUSE             Reviewed;         655 AA.
AC   Q8CH72; Q8K055;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=E3 ubiquitin-protein ligase TRIM32;
DE            EC=6.3.2.-;
DE   AltName: Full=Tripartite motif-containing protein 32;
GN   Name=Trim32;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   UBIQUITINATION.
RC   TISSUE=Testis;
RX   PubMed=14578165; DOI=10.1093/carcin/bgh003;
RA   Horn E.J., Albor A., Liu Y., El-Hizawi S., Vanderbeek G.E.,
RA   Babcock M., Bowden G.T., Hennings H., Lozano G., Weinberg W.C.,
RA   Kulesz-Martin M.;
RT   "RING protein Trim32 associated with skin carcinogenesis has anti-
RT   apoptotic and E3-ubiquitin ligase properties.";
RL   Carcinogenesis 25:157-167(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PIAS4.
RX   PubMed=16816390; DOI=10.1074/jbc.M601655200;
RA   Albor A., El-Hizawi S., Horn E.J., Laederich M., Frosk P.,
RA   Wrogemann K., Kulesz-Martin M.;
RT   "The interaction of Piasy with Trim32, an E3-ubiquitin ligase mutated
RT   in limb-girdle muscular dystrophy type 2H, promotes Piasy degradation
RT   and regulates UVB-induced keratinocyte apoptosis through NFkappaB.";
RL   J. Biol. Chem. 281:25850-25866(2006).
CC   -!- FUNCTION: Has an E3 ubiquitin ligase activity. Ubiquitinates
CC       DTNBP1 (dysbindin) (By similarity). Ubiquitinates PIAS4/PIASY and
CC       promotes its degradation in keratinocytes treated with UVB and
CC       TNF-alpha.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with DTNBP1 (By similarity). It self-associates
CC       (By similarity). Interacts with PIAS4/PIASY upon treatement with
CC       UVB and TNF-alpha.
CC   -!- INTERACTION:
CC       Q9UL18:EIF2C1 (xeno); NbExp=1; IntAct=EBI-773837, EBI-527363;
CC       Q8CJG1:Eif2c1; NbExp=1; IntAct=EBI-773837, EBI-2291996;
CC       P01108:Myc; NbExp=1; IntAct=EBI-773837, EBI-1183114;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Localized in cytoplasmic
CC       bodies, usually concentrated around the nucleus.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. High expression in brain.
CC   -!- INDUCTION: By interferon alpha/UVB treatment.
CC   -!- PTM: Ubiquitinated.
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC   -!- SIMILARITY: Contains 1 B box-type zinc finger.
CC   -!- SIMILARITY: Contains 5 NHL repeats.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
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DR   EMBL; AF347694; AAO13297.1; -; mRNA.
DR   EMBL; AL691456; CAD62276.1; -; Genomic_DNA.
DR   EMBL; BC034104; AAH34104.1; -; mRNA.
DR   IPI; IPI00321005; -.
DR   RefSeq; NP_001155254.1; NM_001161782.1.
DR   RefSeq; NP_444314.2; NM_053084.2.
DR   UniGene; Mm.22786; -.
DR   ProteinModelPortal; Q8CH72; -.
DR   SMR; Q8CH72; 4-91, 352-649.
DR   IntAct; Q8CH72; 6.
DR   STRING; Q8CH72; -.
DR   PhosphoSite; Q8CH72; -.
DR   PRIDE; Q8CH72; -.
DR   Ensembl; ENSMUST00000050850; ENSMUSP00000062277; ENSMUSG00000051675.
DR   Ensembl; ENSMUST00000107366; ENSMUSP00000102989; ENSMUSG00000051675.
DR   GeneID; 69807; -.
DR   KEGG; mmu:69807; -.
DR   UCSC; uc008thr.1; mouse.
DR   CTD; 69807; -.
DR   MGI; MGI:1917057; Trim32.
DR   HOGENOM; HBG447330; -.
DR   HOVERGEN; HBG060344; -.
DR   InParanoid; Q8CH72; -.
DR   OMA; EHHLEGG; -.
DR   OrthoDB; EOG4QZ7KF; -.
DR   PhylomeDB; Q8CH72; -.
DR   NextBio; 330382; -.
DR   ArrayExpress; Q8CH72; -.
DR   Bgee; Q8CH72; -.
DR   Genevestigator; Q8CH72; -.
DR   GermOnline; ENSMUSG00000051675; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0017022; F:myosin binding; IPI:MGI.
DR   GO; GO:0031369; F:translation initiation factor binding; IPI:MGI.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045444; P:fat cell differentiation; IEP:BHF-UCL.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:MGI.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR001258; NHL_repeat.
DR   InterPro; IPR013017; NHL_repeat_subgr.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Gene3D; G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF01436; NHL; 2.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS51125; NHL; 5.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Cytoplasm; Ligase; Metal-binding;
KW   Phosphoprotein; Repeat; Ubl conjugation; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    655       E3 ubiquitin-protein ligase TRIM32.
FT                                /FTId=PRO_0000056247.
FT   REPEAT      360    403       NHL 1.
FT   REPEAT      417    460       NHL 2.
FT   REPEAT      461    501       NHL 3.
FT   REPEAT      564    607       NHL 4.
FT   REPEAT      608    648       NHL 5.
FT   ZN_FING      21     66       RING-type.
FT   ZN_FING      96    139       B box-type; atypical.
FT   COILED      139    198       Potential.
FT   COMPBIAS      2      7       Poly-Ala.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     330    330       Phosphoserine (By similarity).
FT   MOD_RES     337    337       Phosphoserine (By similarity).
FT   MOD_RES     341    341       Phosphoserine (By similarity).
FT   CONFLICT    169    169       A -> V (in Ref. 1; AAO13297).
SQ   SEQUENCE   655 AA;  72057 MW;  32C01387DA7E9224 CRC64;
     MAAAAAASHL NLDALREVLE CPICMESFTE EQLRPKLLHC GHTICRQCLE KLLASSINGV
     RCPFCSKITR ITSLTQLTDN LTVLKIIDTA GLSEAVGLLM CRGCGRRLPR QFCRSCGVVL
     CEPCREADHQ PPGHCTLPVK EAAEERRRDF GEKLTRLREL TGELQRRKAA LEGVSRDLQA
     RYKAVLQEYG HEERRIQEEL ARSRKFFTGS LAEVEKSNSQ VVEEQSYLLN IAEVQAVSRC
     DYFLAKIKQA DVALLEETAD EEEPELTASL PRELTLQDVE LLKVGHVGPL QIGQAVKKPR
     TVNMEDSWAG EEGAASSASA SVTFREMDMS PEEVAPSPRA SPAKQRSSEA ASGIQQCLFL
     KKMGAKGSTP GMFNLPVSLY VTSQSEVLVA DRGNYRIQVF NRKGFLKEIR RSPSGIDSFV
     LSFLGADLPN LTPLSVAMNC HGLIGVTDSY DNSLKVYTMD GHCVACHRSQ LSKPWGITAL
     PSGQFVVTDV EGGKLWCFTV DRGAGVVKYS CLCSAVRPKF VTCDAEGTVY FTQGLGLNVE
     NRQNEHHLEG GFSIGSVGPD GQLGRQISHF FSENEDFRCI AGMCVDARGD LIVADSSRKE
     ILHFPKGGGY SVLIREGLTC PVGIALTPKG QLLVLDCWDH CVKIYSYHLR RYSTP
//
ID   NAV1_MOUSE              Reviewed;        1875 AA.
AC   Q8CH77; Q3U5B6; Q68EE8; Q6PB78; Q80TI7; Q8BKG2; Q8BUT5;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Neuron navigator 1;
DE   AltName: Full=Pore membrane and/or filament-interacting-like protein 3;
GN   Name=Nav1; Synonyms=Kiaa1151, Pomfil3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, TISSUE
RP   SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INTERACTION
RP   WITH TUBULIN, AND FUNCTION.
RC   STRAIN=ICR; TISSUE=Brain;
RX   PubMed=15797708; DOI=10.1016/j.mcn.2004.09.016;
RA   Martinez-Lopez M.J., Alcantara S., Mascaro C., Perez-Branguli F.,
RA   Ruiz-Lozano P., Maes T., Soriano E., Buesa C.;
RT   "Mouse neuron navigator 1, a novel microtubule-associated protein
RT   involved in neuronal migration.";
RL   Mol. Cell. Neurosci. 28:599-612(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1216-1875 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Eye, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1299-1875 (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=12062803; DOI=10.1016/S0378-1119(02)00567-X;
RA   Coy J.F., Wiemann S., Bechmann I., Baechner D., Nitsch R., Kretz O.,
RA   Christiansen H., Poustka A.;
RT   "Pore membrane and/or filament interacting like protein 1 (POMFIL1) is
RT   predominantly expressed in the nervous system and encodes different
RT   protein isoforms.";
RL   Gene 290:73-94(2002).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145 AND SER-810, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May be involved in neuronal migration.
CC   -!- SUBUNIT: Interacts with tubulin.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Associates
CC       with a subset of microtubule plus ends. Enriched in neuronal
CC       growth cones.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8CH77-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CH77-2; Sequence=VSP_025262, VSP_025263;
CC       Name=3;
CC         IsoId=Q8CH77-3; Sequence=VSP_025263, VSP_025266, VSP_025267;
CC       Name=4;
CC         IsoId=Q8CH77-4; Sequence=VSP_025260, VSP_025261, VSP_025264,
CC                                  VSP_025265;
CC   -!- TISSUE SPECIFICITY: Expressed in heart and brain. Present in brain
CC       (at protein level). In adult brain, found almost exclusively in
CC       areas of secondary neurogenesis from the hippocampus and the
CC       subventricular zone.
CC   -!- DEVELOPMENTAL STAGE: Expressed in neural structures at E10. At E13
CC       and E15, highly expressed in neural tube, somites, heart and
CC       dispersed cells in tongue and face. At P5, widely expressed
CC       through the central nervous system in post-mitotic post-migratory
CC       zones. Brain expression decreases rapidly from P5 to P21 (at
CC       protein level).
CC   -!- SIMILARITY: Belongs to the Nav/unc-53 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65740.1; Type=Erroneous initiation;
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DR   EMBL; AF307453; AAO13290.1; -; mRNA.
DR   EMBL; AK122458; BAC65740.1; ALT_INIT; mRNA.
DR   EMBL; AK053255; BAC35323.1; -; mRNA.
DR   EMBL; AK082667; BAC38568.1; -; mRNA.
DR   EMBL; AK153742; BAE32163.1; -; mRNA.
DR   EMBL; BC059840; AAH59840.1; -; mRNA.
DR   EMBL; BC080292; AAH80292.1; -; mRNA.
DR   IPI; IPI00229599; -.
DR   IPI; IPI00399498; -.
DR   IPI; IPI00845619; -.
DR   IPI; IPI00845683; -.
DR   RefSeq; NP_775613.2; NM_173437.2.
DR   UniGene; Mm.34977; -.
DR   ProteinModelPortal; Q8CH77; -.
DR   SMR; Q8CH77; 1548-1644.
DR   STRING; Q8CH77; -.
DR   PhosphoSite; Q8CH77; -.
DR   PRIDE; Q8CH77; -.
DR   Ensembl; ENSMUST00000040599; ENSMUSP00000043803; ENSMUSG00000009418.
DR   Ensembl; ENSMUST00000067414; ENSMUSP00000067241; ENSMUSG00000009418.
DR   GeneID; 215690; -.
DR   KEGG; mmu:215690; -.
DR   UCSC; uc007cth.1; mouse.
DR   CTD; 215690; -.
DR   MGI; MGI:2183683; Nav1.
DR   eggNOG; roNOG04741; -.
DR   GeneTree; ENSGT00530000063334; -.
DR   HOVERGEN; HBG058814; -.
DR   OrthoDB; EOG4GHZNB; -.
DR   NextBio; 374799; -.
DR   ArrayExpress; Q8CH77; -.
DR   Bgee; Q8CH77; -.
DR   CleanEx; MM_NAV1; -.
DR   Genevestigator; Q8CH77; -.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0001578; P:microtubule bundle formation; IDA:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   SMART; SM00382; AAA; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Developmental protein; Differentiation; Microtubule; Neurogenesis;
KW   Phosphoprotein.
FT   CHAIN         1   1875       Neuron navigator 1.
FT                                /FTId=PRO_0000286975.
FT   COILED      258    283       Potential.
FT   COILED      733    758       Potential.
FT   COILED     1070   1161       Potential.
FT   COILED     1301   1360       Potential.
FT   COMPBIAS   1204   1209       Poly-Lys.
FT   MOD_RES      21     21       Phosphoserine.
FT   MOD_RES     145    145       Phosphoserine.
FT   MOD_RES     162    162       Phosphothreonine (By similarity).
FT   MOD_RES     202    202       Phosphoserine (By similarity).
FT   MOD_RES     299    299       Phosphoserine (By similarity).
FT   MOD_RES     311    311       Phosphoserine.
FT   MOD_RES     314    314       Phosphoserine (By similarity).
FT   MOD_RES     394    394       Phosphoserine (By similarity).
FT   MOD_RES     455    455       Phosphoserine (By similarity).
FT   MOD_RES     537    537       Phosphothreonine (By similarity).
FT   MOD_RES     544    544       Phosphoserine (By similarity).
FT   MOD_RES     575    575       Phosphothreonine (By similarity).
FT   MOD_RES     752    752       Phosphoserine (By similarity).
FT   MOD_RES     762    762       Phosphoserine (By similarity).
FT   MOD_RES     810    810       Phosphoserine.
FT   MOD_RES     998    998       Phosphoserine (By similarity).
FT   MOD_RES    1000   1000       Phosphothreonine (By similarity).
FT   MOD_RES    1168   1168       Phosphothreonine (By similarity).
FT   MOD_RES    1179   1179       Phosphoserine (By similarity).
FT   MOD_RES    1251   1251       Phosphoserine (By similarity).
FT   MOD_RES    1380   1380       Phosphoserine (By similarity).
FT   VAR_SEQ       1    392       Missing (in isoform 4).
FT                                /FTId=VSP_025260.
FT   VAR_SEQ     393    412       MSDSDLMGKTMTEDDDITTG -> MLHLPLPRSGRTANFPR
FT                                S (in isoform 4).
FT                                /FTId=VSP_025261.
FT   VAR_SEQ     997   1053       Missing (in isoform 2).
FT                                /FTId=VSP_025262.
FT   VAR_SEQ    1212   1214       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_025263.
FT   VAR_SEQ    1213   1221       YELRSSFNK -> CKGLGIGLC (in isoform 4).
FT                                /FTId=VSP_025264.
FT   VAR_SEQ    1222   1875       Missing (in isoform 4).
FT                                /FTId=VSP_025265.
FT   VAR_SEQ    1225   1225       I -> L (in isoform 3).
FT                                /FTId=VSP_025266.
FT   VAR_SEQ    1226   1875       Missing (in isoform 3).
FT                                /FTId=VSP_025267.
FT   CONFLICT    132    132       G -> D (in Ref. 1; AAO13290).
FT   CONFLICT    310    310       L -> F (in Ref. 2; BAC65740).
FT   CONFLICT    386    386       V -> G (in Ref. 1; AAO13290).
FT   CONFLICT    437    437       A -> G (in Ref. 1; AAO13290).
FT   CONFLICT    899    899       F -> Y (in Ref. 3; BAC38568).
FT   CONFLICT    933    933       Missing (in Ref. 4; AAH59840).
FT   CONFLICT    954    954       E -> D (in Ref. 4; AAH59840).
FT   CONFLICT    960    960       R -> G (in Ref. 1; AAO13290).
FT   CONFLICT    975    975       A -> E (in Ref. 1; AAO13290).
FT   CONFLICT    981    981       P -> L (in Ref. 1; AAO13290).
FT   CONFLICT   1361   1361       P -> S (in Ref. 4; AAH80292).
FT   CONFLICT   1686   1686       G -> V (in Ref. 2; BAC65740).
SQ   SEQUENCE   1875 AA;  202368 MW;  6EDEF58B6953DBB7 CRC64;
     MLGSSVKSVQ PEVELSGGSG SGGDEGADES RGASRKAAAA DGRGMLPKRA KAAGGSGSMA
     KASAAELKVF KSGSVDSRVP GGLPTSNLRK QKSLTNLSFL TDSEKKLQLY EPEWSDDMAK
     APKGLGKLGP KGRETPLMSK TLSKSEHSLF QPKGGSTGGA KTPLAPLAPS LGKPSRIPRG
     PYAEVKPLSK APEAAVSDDG KSDDELLSSK AKAQKGSGTV PSAKGQEERA FLKVDPELVV
     TVLGDLEQLL FSQMLDPESQ RKRTVQNVLD LRQNLEETMS SLRGSQVTHS SLEMPCYDSD
     DANPRSVSSL SNRSSPLSWR YGQSSPRLQA GDAPSVGGSC RSEGPPAWYM HGERAHYSHT
     MPMRSPSKLS HISRLELVES LDSDEVDLKS GYMSDSDLMG KTMTEDDDIT TGWDESSSIS
     SGLSDASDNL SSEEFNASSS LNSLPTTPTA SRRSSTIVLR TDSEKRSLAE SGLNWFSESE
     EKTPKKLEYD SGSLKMEPGT SKWRRERPES CDDASKGGEL KKPISLGHPG SLKKGKTPPV
     AVTSPITHTA QSALKVAGKP EGKATDKGKL AVKNTGLQRS SSDAGRDRLS DAKKPPSGIA
     RPSTSGSFGY KKPPPATGTA TVMQTGSSAT LSKIQKSSGI PVKPVNGRKT SLDVSNSVEP
     GFLAPGARSN IQYRSLPRPA KSSSMSVTGR GGPRPVSSSI DPSLLSTKQG GLTPSRLKEP
     SKVASGRSTP APVNQTDREK EKAKAKAVAL DSDNISLKSI GSPESTPKNQ ASHPPATKLA
     ELPPTPLRAT AKSFVKPPSL ANLDKVNSNS LDLPSSSDTH ASKVPDLHAP SSSTGGPLPS
     CFTPSPAPIL NINSASFSQG LELMSGFSVP KETRMYPKLS GLHRSMESLQ MPMSLPSAFP
     SSAPIPTPPT APSEEDTEEL PWSGSPRAGQ LDSSQRDRNT LPKKGLRYQL QSQEETKERR
     HSHTAGGLPE SDDQAELPSP PALSMSLSAK GQLTNIVSPT AATTPRITRS NSIPTHEAAF
     ELYSGSQMGS TLSLAERPKG MIRSGSFRDP TDDVHGSVLS LASSASSTYS SAEERMQSEQ
     IRKLRRELES SQEKVATLTS QLSANANLVA AFEQSLVNMT SRLRHLAETA EEKDTELLDL
     RETIDFLKKK NSEAQAVIQG ALNASEATPK ELRIKRQNSS DSISSLNSIT SHSSIGSSKD
     ADAKKKKKKS WVYELRSSFN KAFSIKKGPK SASSYSDIEE IATPDSSAPS SPKLQHGSTE
     TASPSIKSST SSSVGTEVTE TPAHSVPHTR LFQANEEEEP EKKEVSELRS ELWEKEMKLT
     DIRLEALNSA HQLDQLRETM HNMQLEVDLL KAENDRLKVA PGPSSGCTPG QVPGSSALSS
     PRRSLGLALS HPFSPSLTDT DLSPMDGIST CGSKEEVTLR VVVRMPPQHI IKGDLKQQEF
     FLGCSKVSGK VDWKMLDEAV FQVFKDYISK MDPASTLGLS TESIHGYSLS HVKRVLDAEP
     PEMPPCRRGV NNISVALKGL KEKCVDSLVF ETLIPKPMMQ HYISLLLKHR RLVLSGPSGT
     GKTYLTNRLA EYLVERSGRE VTDGIVSTFN MHQQSCKDLQ LYLSNLANQI DRETGIGDVP
     LVILLDDLSE AGSISELVNG ALTCKYHKCP YIIGTTNQPV KMTPNHGLHL SFRMLTFSNN
     VEPANGFLVR YLRRKLVESD SDVNANKEEL LRVLDWVPKL WYHLHTFLEK HSTSDFLIGP
     CFFLSCPIGI EDFRTWFIDL WNNSIIPYLQ EGAKDGIKVH GQKAAWEDPV EWVRDTLPWP
     SAQQDQSKLY HLPPPSVGPH STASPPEDRT VKDSTPNSLD SDPLMAMLLK LQEAANYIES
     PDRETILDPN LQATL
//
ID   K0317_MOUSE             Reviewed;         823 AA.
AC   Q8CHG5; Q6P9Q1; Q80YC4; Q8C5W5;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Protein KIAA0317;
GN   Name=Kiaa0317;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Contains 1 filamin repeat.
CC   -!- SIMILARITY: Contains 1 HECT (E6AP-type E3 ubiquitin-protein
CC       ligase) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC41414.1; Type=Erroneous initiation;
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DR   EMBL; AB093230; BAC41414.1; ALT_INIT; mRNA.
DR   EMBL; AK077015; BAC36566.1; -; mRNA.
DR   EMBL; BC049900; AAH49900.1; -; mRNA.
DR   EMBL; BC060658; AAH60658.1; -; mRNA.
DR   IPI; IPI00229648; -.
DR   RefSeq; NP_835166.3; NM_178065.4.
DR   UniGene; Mm.24446; -.
DR   ProteinModelPortal; Q8CHG5; -.
DR   SMR; Q8CHG5; 56-155, 433-814.
DR   STRING; Q8CHG5; -.
DR   PhosphoSite; Q8CHG5; -.
DR   PRIDE; Q8CHG5; -.
DR   Ensembl; ENSMUST00000043169; ENSMUSP00000048780; ENSMUSG00000042350.
DR   GeneID; 68497; -.
DR   KEGG; mmu:68497; -.
DR   UCSC; uc007ofy.1; mouse.
DR   MGI; MGI:1915747; 1110018G07Rik.
DR   GeneTree; ENSGT00570000078981; -.
DR   HOGENOM; HBG358350; -.
DR   HOVERGEN; HBG052181; -.
DR   InParanoid; Q8CHG5; -.
DR   OMA; CQVFLRL; -.
DR   OrthoDB; EOG4VMFDQ; -.
DR   PhylomeDB; Q8CHG5; -.
DR   NextBio; 327296; -.
DR   ArrayExpress; Q8CHG5; -.
DR   Bgee; Q8CHG5; -.
DR   CleanEx; MM_1110018G07RIK; -.
DR   Genevestigator; Q8CHG5; -.
DR   GermOnline; ENSMUSG00000042350; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0006464; P:protein modification process; IEA:InterPro.
DR   InterPro; IPR001298; Filamin.
DR   InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR   InterPro; IPR000569; HECT.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF00630; Filamin; 1.
DR   Pfam; PF00632; HECT; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00557; IG_FLMN; 1.
DR   SUPFAM; SSF56204; HECT; 1.
DR   SUPFAM; SSF81296; Ig_E-set; 1.
DR   PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR   PROSITE; PS50237; HECT; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix; Ubl conjugation pathway.
FT   CHAIN         1    823       Protein KIAA0317.
FT                                /FTId=PRO_0000120350.
FT   TRANSMEM      2     22       Helical; (Potential).
FT   REPEAT       64    158       Filamin.
FT   DOMAIN      483    823       HECT.
FT   CONFLICT    424    424       T -> I (in Ref. 3; AAH60658).
SQ   SEQUENCE   823 AA;  94199 MW;  E74AAE76555A20D4 CRC64;
     MFYVIGGIIV SVVAFFFTIK FLFELAARVV SFLQNEDRER RGDRTIYDYV RGNYLDPRSC
     KVSWDWKDPY EVGHSMAFRV HLFYKNGQPF PAHRPVGLRV HISHVELAVD IPVTQEVLQE
     PNSNVVKVAF TVRKAGRYEI TVKLGGLNVA YSPYYKIFQP GMVVPSKTKI VCHFSTLVLT
     CGQPHTLQIV PRDEYDNPTN NSMSLRDEHS YSLAIHELGP QEEENNEVSF EKSVTSNRQT
     CQVFLRLTLH SRGCFHACIS YQNQPINNGE FDIIVLSENE KNIVERNVST SGVSIYFEAY
     LYNANNCTST PWHLPPMHMS SSQRRPSTAI EEDDEDSPSE CHTPEKVKKP KKVYCYVSPK
     QFSVKEFYLK IIPWRLYTFR VCPGTKFSYL GPDPVHKLLT LVVDDGIQPP VELSCKERNI
     LAATFIRSLH KNIGGSETFQ DKVNFFQREL RQVHMKRPHS KVTLKVSRHA LLESSLKATR
     NFSISDWSKN FEVVFQDEEA LDWGGPRREW FELICKALFD TTSQLFARFT DSNQALVHPN
     PNRPAHLRLK MYEFAGRLVG KCLYESSLGG AYKQLVRARF TRSFLAQIIG LRMHYKYFET
     DDPEFYKSKV CFILNNDMSE MELVFAEEKY NKSGQLDKIV ELMTGGAQTP VTNANKIFYL
     NLLAQYRLAS QVKEEVEHFL KGLNELVPEN LLAIFDENEL ELLMCGTGDI NVSDFKAHAV
     VVGGSWHFRE KVMRWFWAVV SSLTQEELAR LLQFTTGSSQ LPPGGFAALC PSFQIIAAPT
     HSTLPTAHTC FNQLCLPTYD SYEEVHRMLQ LAISEGCEGF GML
//
ID   RPGF2_MOUSE             Reviewed;        1138 AA.
AC   Q8CHG7;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Rap guanine nucleotide exchange factor 2;
DE   AltName: Full=Neural RAP guanine nucleotide exchange protein;
DE            Short=nRap GEP;
DE   AltName: Full=PDZ domain-containing guanine nucleotide exchange factor 1;
DE            Short=PDZ-GEF1;
DE   Flags: Fragment;
GN   Name=Rapgef2; Synonyms=Kiaa0313, Pdzgef1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-62, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Guanine nucleotide exchange factor (GEF) for Rap1, Rap1B
CC       and Rap2 GTPases (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane (By similarity).
CC       Note=Associated with the synaptic plasma membrane (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 Ras-associating domain.
CC   -!- SIMILARITY: Contains 1 Ras-GEF domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB093228; BAC41412.1; -; mRNA.
DR   IPI; IPI00853823; -.
DR   UniGene; Mm.31220; -.
DR   ProteinModelPortal; Q8CHG7; -.
DR   SMR; Q8CHG7; 21-107, 245-645.
DR   STRING; Q8CHG7; -.
DR   PRIDE; Q8CHG7; -.
DR   Ensembl; ENSMUST00000118100; ENSMUSP00000114119; ENSMUSG00000062232.
DR   Ensembl; ENSMUST00000118340; ENSMUSP00000113778; ENSMUSG00000062232.
DR   MGI; MGI:2659071; Rapgef2.
DR   GeneTree; ENSGT00560000076949; -.
DR   HOVERGEN; HBG056658; -.
DR   InParanoid; Q8CHG7; -.
DR   OrthoDB; EOG4XPQF2; -.
DR   ArrayExpress; Q8CHG7; -.
DR   Bgee; Q8CHG7; -.
DR   CleanEx; MM_RAPGEF2; -.
DR   Genevestigator; Q8CHG7; -.
DR   GermOnline; ENSMUSG00000062232; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0017034; F:Rap guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR000159; Ras-assoc.
DR   InterPro; IPR008937; Ras_GEF.
DR   InterPro; IPR001895; RasGRF_CDC25.
DR   Gene3D; G3DSA:1.10.840.10; RasGRF_CDC25; 1.
DR   PANTHER; PTHR23113; Ras_GEF; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00314; RA; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Guanine-nucleotide releasing factor; Membrane;
KW   Phosphoprotein.
FT   CHAIN        <1   1138       Rap guanine nucleotide exchange factor 2.
FT                                /FTId=PRO_0000068866.
FT   DOMAIN       27    112       PDZ.
FT   DOMAIN      248    334       Ras-associating.
FT   DOMAIN      359    586       Ras-GEF.
FT   COMPBIAS    749    807       Ser-rich.
FT   COMPBIAS   1040   1121       Pro-rich.
FT   MOD_RES      60     60       Phosphoserine.
FT   MOD_RES      62     62       Phosphoserine.
FT   MOD_RES     577    577       Phosphoserine (By similarity).
FT   MOD_RES     664    664       Phosphoserine.
FT   MOD_RES     757    757       Phosphoserine (By similarity).
FT   MOD_RES     760    760       Phosphothreonine (By similarity).
FT   NON_TER       1      1
SQ   SEQUENCE   1138 AA;  126099 MW;  548D4D6EBF364CE1 CRC64;
     NNLEREKMGG HLRLLNIACA AKAKRRLMTL TKPSREAPLP FILLGGSEKG FGIFVDSVDS
     CSKATEAGLK RGDQILEVNG QNFENIQLSK AMEILRNNTH LSITVKTNLF VFKELLTRLS
     EEKRNGAPHL PKIGDIKKAS RYSIPDLAVD VEQVIGLEKV NKKSKANTVG GRNKLKKILD
     KTRISILPQK PYNDIGIGQS QDDSIVGLRQ TKHIPAALPV SGTLSSSNPD LLQSHHRILD
     FSTTPDLPDQ VLRVFKADQQ SRYIMISKDT TAKEVVIQAI REFAVTATPE QYSLCEVSVT
     PEGVIKQRRL PDQLSKLADR IQLSGRYYLK NNMETETLCS DEDAQELLRE SQISLLQLST
     VEVATQLSMR NFELFRNIEP TEYIDDLFKL KSKTSCANLK KFEEVINQET FWVASEILRE
     TNQLKRMKII KHFIKIALHC RECKNFNSMF AIISGLNLAP VARLRTTWEK LPNKYEKLFQ
     DLQDLFDPSR NMAKYRNVLS GQNLQPPVIP LFPVIKKDLT FLHEGNDSKV DGLVNFEKLR
     MIAKEIRHVG RMASVNMDPA LMFRTRKKKW RSLGSLSQGS ANATVLDVAQ TGGHKKRVRR
     SSFLNAKKLY EDAQMARKVK QYLSNLELEM DEESLQTLSL QCEPATSTLP KNPGDKKPVK
     SETSPVAPRA GPQQKVQPQQ PLAQPQPPHK VSQGLQVPAV SLYPSRKKVP VKDLPPFGIN
     SPQALKKILS LSEEGSLERH RKQAEDTISN ASSQLSSPPT SPQSSPRKGY ALALSGTVDN
     FSDSGHSEIS SRSSIVSNSS FDSVPVSLHD ERRQRHSVSI VESNLGVGRM ERRTLMEPDQ
     YSLGSYAPVS ESRGLYAAAT VISSPSTEEL SHDQGDRASL DAADSGRGSW TSCSSGSHDN
     IQTIQHQRSW ETLPFGHTHF DYSGDAASIW ASGGHMDQMM FSDHSTKYNR QNQSRESLEQ
     AQSRASWASS TGYWGEDSEG DTGTIKRRGG KDVSAEAESS SMVPVTTEEA KPVPMPAHIA
     VTPSTTKGLI ARKEGRYREP PPTPPGYVGI PIADFPEGPC HPARKPPDYN VALQRSRMVA
     RPTEAPAPGQ TPPAAAASRP GSKPQWHKPS DADPRLAPFQ PQGFAGAEED EDEQVSAV
//
ID   EP400_MOUSE             Reviewed;        3072 AA.
AC   Q8CHI8; Q3TPY1; Q5RKN8; Q80TC8; Q8BXI5; Q8BYW3; Q8C0P6; Q8CHI7;
AC   Q8VDF4; Q9DA54;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=E1A-binding protein p400;
DE            EC=3.6.4.-;
DE   AltName: Full=Domino homolog;
DE            Short=mDomino;
DE   AltName: Full=p400 kDa SWI2/SNF2-related protein;
GN   Name=Ep400; Synonyms=Kiaa1498;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND INTERACTION WITH
RP   ZNF42.
RX   MEDLINE=22541380; PubMed=12653961;
RX   DOI=10.1046/j.1365-2443.2003.00636.x;
RA   Ogawa H., Ueda T., Aoyama T., Aronheim A., Nagata S., Fukunaga R.;
RT   "A SWI2/SNF2-type ATPase/helicase protein, mDomino, interacts with
RT   myeloid zinc finger protein 2A (MZF-2A) to regulate its
RT   transcriptional activity.";
RL   Genes Cells 8:325-339(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-896 (ISOFORM 3),
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-894 (ISOFORM 2),
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-677 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 992-2359.
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Corpora quadrigemina, Embryo, Testis, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1415-3072 (ISOFORM 5).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1881-3072 (ISOFORM 4), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2429-3072 (ISOFORMS 1/2/3).
RC   STRAIN=C57BL/6, and FVB/N-3; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 2443-2450, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-754, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   INTERACTION WITH PHF5A.
RX   PubMed=18758164; DOI=10.1159/000138890;
RA   Rzymski T., Grzmil P., Meinhardt A., Wolf S., Burfeind P.;
RT   "PHF5A represents a bridge protein between splicing proteins and ATP-
RT   dependent helicases and is differentially expressed during mouse
RT   spermatogenesis.";
RL   Cytogenet. Genome Res. 121:232-244(2008).
CC   -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex
CC       which is involved in transcriptional activation of select genes
CC       principally by acetylation of nucleosomal histones H4 and H2A.
CC       This modification may both alter nucleosome - DNA interactions and
CC       promote interaction of the modified histones with other proteins
CC       which positively regulate transcription. May be required for
CC       transcriptional activation of E2F1 and MYC target genes during
CC       cellular proliferation. The NuA4 complex ATPase and helicase
CC       activities seem to be, at least in part, contributed by the
CC       association of RUVBL1 and RUVBL2 with EP400 (By similarity).
CC       Regulates transcriptional activity of ZNF42.
CC   -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex
CC       which contains the catalytic subunit KAT5/TIP60 and the subunits
CC       EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49,
CC       RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX,
CC       MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. May also participate in
CC       the formation of NuA4 related complexes which lack the KAT5/TIP60
CC       catalytic subunit, but which include the SWI/SNF related protein
CC       SRCAP. The NuA4 complex interacts with MYC. EP400 interacts with
CC       TRRAP, RUVBL1 and RUVBL2 (By similarity). Interacts with ZNF42.
CC       Interacts with PHF5A.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q8CHI8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CHI8-2; Sequence=VSP_011996;
CC       Name=3;
CC         IsoId=Q8CHI8-3; Sequence=VSP_011996, VSP_011997;
CC       Name=4;
CC         IsoId=Q8CHI8-4; Sequence=VSP_011998;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q8CHI8-5; Sequence=VSP_017127, VSP_011998;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, thymus, lung, liver,
CC       spleen, kidney, colon and bone marrow.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 HSA domain.
CC   -!- SIMILARITY: Contains 1 Myb-like domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB24439.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC       Sequence=BAC26781.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC       Sequence=BAC32913.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; AB092694; BAC45253.1; -; mRNA.
DR   EMBL; AB092695; BAC45254.1; -; mRNA.
DR   EMBL; AK006168; BAB24439.1; ALT_SEQ; mRNA.
DR   EMBL; AK030095; BAC26781.1; ALT_SEQ; mRNA.
DR   EMBL; AK037693; BAC29849.2; -; mRNA.
DR   EMBL; AK046892; BAC32913.2; ALT_INIT; mRNA.
DR   EMBL; AK163566; BAE37399.1; -; mRNA.
DR   EMBL; AK164049; BAE37604.1; -; mRNA.
DR   EMBL; AK122517; BAC65799.2; -; Transcribed_RNA.
DR   EMBL; BC022153; AAH22153.1; -; mRNA.
DR   EMBL; BC085511; AAH85511.1; -; mRNA.
DR   IPI; IPI00229659; -.
DR   IPI; IPI00404291; -.
DR   IPI; IPI00474628; -.
DR   IPI; IPI00480329; -.
DR   IPI; IPI00720144; -.
DR   UniGene; Mm.270487; -.
DR   ProteinModelPortal; Q8CHI8; -.
DR   SMR; Q8CHI8; 1815-1950.
DR   STRING; Q8CHI8; -.
DR   PhosphoSite; Q8CHI8; -.
DR   PRIDE; Q8CHI8; -.
DR   Ensembl; ENSMUST00000041558; ENSMUSP00000049038; ENSMUSG00000029505.
DR   Ensembl; ENSMUST00000086645; ENSMUSP00000083845; ENSMUSG00000029505.
DR   Ensembl; ENSMUST00000112435; ENSMUSP00000108054; ENSMUSG00000029505.
DR   Ensembl; ENSMUST00000112436; ENSMUSP00000108055; ENSMUSG00000029505.
DR   UCSC; uc008yrg.1; mouse.
DR   UCSC; uc008yrh.1; mouse.
DR   MGI; MGI:1276124; Ep400.
DR   eggNOG; roNOG09820; -.
DR   GeneTree; ENSGT00530000063427; -.
DR   HOVERGEN; HBG051488; -.
DR   InParanoid; Q8CHI8; -.
DR   OrthoDB; EOG4RBQHQ; -.
DR   ArrayExpress; Q8CHI8; -.
DR   Bgee; Q8CHI8; -.
DR   CleanEx; MM_EP400; -.
DR   Genevestigator; Q8CHI8; -.
DR   GermOnline; ENSMUSG00000029505; Mus musculus.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
DR   GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR013999; HAS_subgroup.
DR   InterPro; IPR014012; Helicase/SANT-assoc_DNA-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR006562; HSA.
DR   InterPro; IPR017877; MYB-like.
DR   InterPro; IPR001005; SANT_DNA-bd.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07529; HSA; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00573; HSA; 1.
DR   SMART; SM00717; SANT; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51204; HSA; 1.
DR   PROSITE; PS50090; MYB_LIKE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Chromatin regulator;
KW   Direct protein sequencing; DNA-binding; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein.
FT   CHAIN         1   3072       E1A-binding protein p400.
FT                                /FTId=PRO_0000074313.
FT   DOMAIN      798    870       HSA.
FT   DOMAIN     1102   1267       Helicase ATP-binding.
FT   DOMAIN     1815   1972       Helicase C-terminal.
FT   DOMAIN     2276   2345       Myb-like.
FT   NP_BIND    1115   1122       ATP (Potential).
FT   REGION      950   1364       Interactions with RUVBL1 and RUVBL2 (By
FT                                similarity).
FT   REGION     2440   2699       Interaction with ZNF42.
FT   MOTIF      1218   1221       DEAD box-like.
FT   COMPBIAS    277    281       Poly-Gln.
FT   COMPBIAS    316    319       Poly-Pro.
FT   COMPBIAS    426    436       Poly-Glu.
FT   COMPBIAS    699    704       Poly-Ser.
FT   COMPBIAS    956    959       Poly-Glu.
FT   COMPBIAS   2462   2479       Poly-Gln.
FT   COMPBIAS   2480   2484       Poly-Pro.
FT   COMPBIAS   2487   2494       Poly-Pro.
FT   COMPBIAS   2685   2698       Poly-Gln.
FT   COMPBIAS   2739   2745       Poly-Pro.
FT   COMPBIAS   2767   2770       Poly-Gln.
FT   MOD_RES     314    314       Phosphothreonine (By similarity).
FT   MOD_RES     315    315       Phosphoserine (By similarity).
FT   MOD_RES     320    320       Phosphothreonine (By similarity).
FT   MOD_RES     321    321       Phosphoserine (By similarity).
FT   MOD_RES     735    735       Phosphoserine (By similarity).
FT   MOD_RES     754    754       Phosphoserine.
FT   MOD_RES     940    940       Phosphoserine (By similarity).
FT   MOD_RES     942    942       Phosphoserine (By similarity).
FT   MOD_RES     944    944       Phosphothreonine (By similarity).
FT   MOD_RES    1471   1471       N6-acetyllysine (By similarity).
FT   MOD_RES    1552   1552       N6-acetyllysine (By similarity).
FT   MOD_RES    1646   1646       Phosphoserine (By similarity).
FT   MOD_RES    1650   1650       Phosphoserine (By similarity).
FT   MOD_RES    2265   2265       N6-acetyllysine (By similarity).
FT   MOD_RES    2272   2272       N6-acetyllysine (By similarity).
FT   VAR_SEQ     446    482       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_011996.
FT   VAR_SEQ     513    548       Missing (in isoform 3).
FT                                /FTId=VSP_011997.
FT   VAR_SEQ    1764   1919       Missing (in isoform 5).
FT                                /FTId=VSP_017127.
FT   VAR_SEQ    2800   2806       Missing (in isoform 4 and isoform 5).
FT                                /FTId=VSP_011998.
FT   CONFLICT    102    102       G -> S (in Ref. 2; BAC26781).
FT   CONFLICT    107    107       A -> D (in Ref. 2; BAC29849).
FT   CONFLICT    163    163       N -> S (in Ref. 1; BAC45253/BAC45254).
FT   CONFLICT    678    686       TVASTRPPL -> VLCGHWLFY (in Ref. 2;
FT                                BAB24439/BAC26781).
FT   CONFLICT    896    896       E -> G (in Ref. 2; BAC29849).
FT   CONFLICT   2249   2249       K -> N (in Ref. 2; BAC32913).
FT   CONFLICT   2353   2359       SKNNRPL -> LICEANP (in Ref. 2; BAC32913).
FT   CONFLICT   2518   2518       A -> T (in Ref. 5; AAH85511).
FT   CONFLICT   2539   2539       A -> V (in Ref. 1; BAC45253/BAC45254).
SQ   SEQUENCE   3072 AA;  337150 MW;  02990D622EACB19E CRC64;
     MHHGSGPQNV QHQLQRSRSF TGSEEEQPAH PNLPPSPAAP FAPSASPSAP QSPGYQIQQL
     MSRSPVAGQN VNITLQNVGP VVGGNQQITL APLPLPNPTS PGFQFGAQQR RFEHGSPSYI
     QVTSPMSQQV QTQSPTQPSP GPGQTLQNVR AGAPGPGLGI CSNSPTGGFV DASVLVRQIS
     LSPSSGGHFV FQEAPGLTQM AQGAQVQLQH SGAPITVRER RLSQPHAQSG GTIHHLGPQS
     PAAAGGTGLQ PLASPNHITT ASLPPQISSI IQGQLIQQQQ QVLQGQPMNR SLGFERTPGV
     LLPGVGGPSA FGMTSPPPPT SPSRTTMPPG LSSVPLTSMG SSGMKKVPKK LEEIPPASQE
     MAQMRKQCLD YHYKEMEALK EVFKEYLIEL FFLQHLQGNM MDFLAFKKKH YAPLQAYLRQ
     NDLDIEEEEE EEEEEEGKSE VINDEVKVVT GKDGQTGTPV AIATQLPPNV SAAFSSQQQP
     FQHQSLTGSL VVGPGSATEA DPFKRQQVMP PTEQSKRPRL EVGHPGVVFQ HPGVNAGVPL
     QQLMPTVQGG MPPTPQATQL TGQKQSQQQY DPSTGPPVQN AASLHTPPPQ LPARLPPASV
     PATALPSTLQ FSQQSQMVEA STQLQIPVKT QQLNAPIPAP LPSQLPAPSS QPAQPALHVP
     MPGKAQMQTS QLSSQTQTVA STRPPLDSAQ PCQRSLPTSS SSSSLVPVSG SGPGPSPARS
     SPVNRPSSAT NKALSPITSR SPGVAVSAPP KPQSPAQNAA SSQDGSQDKL AEQITLENQI
     HQRIADLRKE GLWSLRRLPK LQEAPRPKSH WDYLLEEMQW MATDFAQERR WKLAAAKKLV
     RTVARHHEEK KLREERGKKE EQSRLRRIAA TTAREIEYFW SNIEQVVEIK LQVELEEKRK
     KALNLQKVSR RGKESRLKGF DTSPEHSLDL GISGRKRKAS TSLTDDEVED EEETIEEEEA
     HEGLVDHHTE LTNLAKEAEL PLIDLMKLYE GAFLPNFQWP QPEPDHEESS GEEDVEDCPS
     DRESRRDSVL IDSLFIMDQF KAAERMSIGK SNTKDITEVT AVAEAILPKG SARVTTAVKF
     SAPSLLYGAL RDYQKIGLDW LAKLYRKNLN GILADEAGLG KTVQIIAFFA HLACNEGNWG
     PHLVVMRSCN ILKWELELKR WCPGLKTLSY VGSHRELKAK RQEWTEPNNF HICITSYKQF
     FRGYTAFSRV HWKCLVVDEM QRVKGMTERH WEAIFKLQSQ QRLLLIDVPL HNTFLELWTM
     VHFLIPGISR PYLSFPLKAP NEENQDYYHK MVIRLHRVTQ PFILRRTKRD VEKQLTRKYE
     HVLKCRLSSR QKALYEDVIL QPRTQEALKS GHFVSVLSVL TRLQRICNHP GLVEPRVPGS
     SFAAGSLQYK SASLILRVLE REFWKETDLS IFDLIGLENK ITRHEAELLC KKKVTRKLME
     EVFASPPPSA RPAAVKLKAS RLFQPVQYGQ KPEGRTVAFP STHPPRMANT NTSTATPQGQ
     VRGRPPIATF SANPDTKGGE VVKIAQLASI AGPQSRVAQP ETPVTLQFQG NKFTLSHSQL
     RQLTAGQPLQ LQGSVLQIVS APGQPYLRAP GPVVMQTVSQ AGAVHSTLGS KPPTSGPSPA
     PLTPQVGVPG RVAVSAMAVG EPGLASKPAS PAAGPTQEEK SRLLKERLDQ IHFINERRCS
     QAPVYGRDLL RICSLPGRRK RPLCWSLDSN FGKGPKGVNY DMSLSKSEGD LILTLSQESL
     QDVLGRVACV IPPVVATPPS LWVARPPSLY SSRLRALRQC LREHTGPYHR QLQQLTALRS
     LQFPELRLVQ FDSGKLEALA ILLQKLKSEG RRVLILSQMV LMLDILEMFL NFHYLTYVRI
     DENANSEQRQ ELMRSFNRDR RIFCALLSTH SRATGINLVE ADTVVFYDND LNPVMDAKAQ
     EWCDRIGRCK DIHIYRLVSG NSIEEKLLKN GTKDLIREVA AQGNDYSMAF LTQRTIQELF
     EVYSPMDDTG FPVKAEEFVV LSQEPSVSET IAPKIARPFI EALKSIECLE EDAQRSTEEA
     VPGSSSVAVS SDSDGSRYDE EPSQLEELAD FMEQLTPIEK YALNYLELFH TTTEQEKERI
     SEDLVMASMK DWETRNARAL QEREARLQLE QEEAELLTYT REDAYTMEYV YEDADGQTEV
     MPLWTPPTPP QDDNDIYIDS VMCLMYETTP IPEAKLPPVY VRKERKRHKT DPSAAGRKKK
     QRHGEAVVPP RSLFDRATPG MLKIRREGKE QKKNLLLKQQ TPFAKPLPTY VKSSGEPAQD
     SPDWLIGEDW ALLQAVKQLL ELPLNLTIVS PAHTPNWDLV SDVVNSCSRI YRSSKQCRNR
     YENVIIPREE GKSKNNRPLR TSQIYAQDEN ATHTQLYTSH FELMKMTAGK RSPPIKPLLG
     MNPFQKNPKH ASVLAESGIN YDKPLPPIQV ASLRAERIAK EKKALADQQK AQQPPVTQPP
     PQQQQQQQQQ QQQQQQQQQP PPPPQQPPPP VPQPQAASSQ TPAGQPAVQP QPQPQVQAQP
     QPVQPQSKGQ PTMTTVGSAA VLAGTIKTSV TGTSIPTGTV SGNVIVNTIA GVPAATFQSI
     NKRLASPVAP GTLTTSGGSA PAQVVHTQQR AVGSPATATT DLVSMTTTQG VRAVTSVTAS
     AVVTTNLTPV QTPTRSLVTQ VSQATGVQLP GKTITPAAHF QLLRQQQQQQ QQQQQQQQTS
     QVQVPQLQSQ AQSPAQIKAV SKLGPEHIIK MQKQKMQLPP QPPPPQAQPG PPQQPAQVQV
     QTPQPPQQQQ SPQLTTVTAP RPGALLTGTT VTNLQVARLT RVPTSQLQAQ GQMQTQTPQP
     AQVALAKPPV VSVPAAVVSS PGVTTLPMNV AGISVAIGQP QKTAGQTVVA QPVNVQQLLK
     YKQQTAVQQQ KAIQPQVAQG QAAVQQKLTT QQITTQGPQQ KVAYAAQPAL KTQFLTTPIS
     QAQKLAGTQQ VQTQIQVAKL PQVVQQQTPV ASIQQVASAS QQASPQTVTL TQATAAGQQV
     QMIPTVTATA QLVQQKLIQQ QVVTTASASL QTPGGPSPAQ LPASSDSPSQ QPKLQMRVPA
     VRLKTPTKPP CQ
//
ID   KAT5_MOUSE              Reviewed;         513 AA.
AC   Q8CHK4; A1L394; Q8CGZ3; Q8CGZ4; Q8VIH0;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2003, sequence version 2.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Histone acetyltransferase KAT5;
DE            EC=2.3.1.48;
DE   AltName: Full=60 kDa Tat-interactive protein;
DE            Short=Tip60;
DE   AltName: Full=Histone acetyltransferase HTATIP;
DE   AltName: Full=Lysine acetyltransferase 5;
GN   Name=Kat5; Synonyms=Htatip, Tip60;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), SUBCELLULAR LOCATION,
RP   AND TISSUE SPECIFICITY.
RC   STRAIN=129/SvJ;
RX   PubMed=12036595; DOI=10.1016/S0378-1119(02)00546-2;
RA   McAllister D., Merlo X., Lough J.W.;
RT   "Characterization and expression of the mouse tat interactive protein
RT   60 kD (TIP60) gene.";
RL   Gene 289:169-176(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 3).
RX   PubMed=12801643; DOI=10.1016/S0378-1119(03)00547-X;
RA   Legube G., Trouche D.;
RT   "Identification of a larger form of the histone acetyl transferase
RT   Tip60.";
RL   Gene 310:161-168(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6;
RA   Szendro P.I., Cadenas C., Eichele G.;
RT   "Cloning of mouse Tip60.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC   STRAIN=W/Wv;
RA   Daigo Y., Takayama I., Fujino M.A.;
RT   "Isolation and characterization of novel human and mouse genes, which
RT   are expressed in the digestive tract.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Catalytic subunit of the NuA4 histone acetyltransferase
CC       complex which is involved in transcriptional activation of select
CC       genes principally by acetylation of nucleosomal histones H4 and
CC       H2A. This modification may both alter nucleosome - DNA
CC       interactions and promote interaction of the modified histones with
CC       other proteins which positively regulate transcription. This
CC       complex may be required for the activation of transcriptional
CC       programs associated with oncogene and proto-oncogene mediated
CC       growth induction, tumor suppressor mediated growth arrest and
CC       replicative senescence, apoptosis, and DNA repair. The NuA4
CC       complex ATPase and helicase activities seem to be, at least in
CC       part, contributed by the association of RUVBL1 and RUVBL2 with
CC       EP400. NuA4 may also play a direct role in DNA repair when
CC       recruited to sites of DNA damage. Directly acetylates and
CC       activates ATM (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + [histone] = CoA + acetyl-
CC       [histone].
CC   -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex
CC       which contains the catalytic subunit KAT5/TIP60 and the subunits
CC       EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49,
CC       RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX,
CC       MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6 (By similarity).
CC       HTATTIP/TIP60, EPC1, and ING3 together constitute a minimal HAT
CC       complex termed Piccolo NuA4 (By similarity). The NuA4 complex
CC       interacts with MYC (By similarity). Interacts with ATM (By
CC       similarity). Interacts with PHF17 (By similarity). Interacts with
CC       PLA2G4A/CPLA2, EDNRA and HDAC7 (By similarity). Interacts with the
CC       cytoplasmic tail of APP and APBB1/FE65 (By similarity). Interacts
CC       with TRIM24 and TRIM68 (By similarity). Forms a complex with SENP6
CC       and UBE2I in response to UV irradiation (By similarity).
CC   -!- INTERACTION:
CC       P54254:Atxn1; NbExp=1; IntAct=EBI-1169948, EBI-1169713;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm, perinuclear
CC       region (By similarity). Note=Upon stimulation with EDN1, it is
CC       exported from the nucleus to the perinuclear region (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8CHK4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CHK4-2; Sequence=VSP_009107;
CC       Name=3;
CC         IsoId=Q8CHK4-3; Sequence=VSP_009106;
CC       Name=4;
CC         IsoId=Q8CHK4-4; Sequence=VSP_009105;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in testis, heart, brain, kidney and
CC       liver. Weakly expressed in lung.
CC   -!- PTM: Sumoylated by UBE2I at Lys-430 and Lys-451, leading to
CC       increase of its histone acetyltransferase activity in UV-induced
CC       DNA damage response, as well as its translocation to nuclear
CC       bodies (By similarity).
CC   -!- PTM: Phosphorylated on Ser-86 and Ser-90; enhanced during G2/M
CC       phase. Phosphorylated form has a higher activity (By similarity).
CC   -!- PTM: Ubiquitinated by MDM2, leading to its proteasome-dependent
CC       degradation (By similarity).
CC   -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
CC   -!- SIMILARITY: Contains 1 C2HC-type zinc finger.
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DR   EMBL; AY061983; AAL34981.1; -; Genomic_DNA.
DR   EMBL; AF528194; AAN77140.1; -; mRNA.
DR   EMBL; AF528195; AAN77141.1; -; mRNA.
DR   EMBL; AF528196; AAN77142.1; -; mRNA.
DR   EMBL; AB055409; BAC53807.1; -; mRNA.
DR   EMBL; BC129968; AAI29969.1; -; mRNA.
DR   IPI; IPI00129354; -.
DR   IPI; IPI00229606; -.
DR   IPI; IPI00395035; -.
DR   IPI; IPI00395036; -.
DR   RefSeq; NP_001186176.1; NM_001199247.1.
DR   RefSeq; NP_848752.1; NM_178637.2.
DR   UniGene; Mm.228930; -.
DR   ProteinModelPortal; Q8CHK4; -.
DR   SMR; Q8CHK4; 11-79, 230-504.
DR   IntAct; Q8CHK4; 29.
DR   MINT; MINT-4302182; -.
DR   STRING; Q8CHK4; -.
DR   PhosphoSite; Q8CHK4; -.
DR   PRIDE; Q8CHK4; -.
DR   Ensembl; ENSMUST00000025865; ENSMUSP00000025865; ENSMUSG00000024926.
DR   Ensembl; ENSMUST00000113640; ENSMUSP00000109270; ENSMUSG00000024926.
DR   Ensembl; ENSMUST00000113641; ENSMUSP00000109271; ENSMUSG00000024926.
DR   GeneID; 81601; -.
DR   KEGG; mmu:81601; -.
DR   UCSC; uc008gdy.1; mouse.
DR   UCSC; uc008gdz.1; mouse.
DR   UCSC; uc008geb.1; mouse.
DR   CTD; 81601; -.
DR   MGI; MGI:1932051; Kat5.
DR   GeneTree; ENSGT00550000074503; -.
DR   OrthoDB; EOG4JHCFH; -.
DR   PhylomeDB; Q8CHK4; -.
DR   BRENDA; 2.3.1.48; 244.
DR   NextBio; 350414; -.
DR   ArrayExpress; Q8CHK4; -.
DR   Bgee; Q8CHK4; -.
DR   Genevestigator; Q8CHK4; -.
DR   GermOnline; ENSMUSG00000024926; Mus musculus.
DR   GO; GO:0000785; C:chromatin; IEA:InterPro.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0005667; C:transcription factor complex; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR   GO; GO:0006333; P:chromatin assembly or disassembly; IEA:InterPro.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000953; Chromodomain.
DR   InterPro; IPR016197; Chromodomain-like.
DR   InterPro; IPR002717; MOZ_SAS.
DR   Gene3D; G3DSA:3.40.630.30; Acyl_CoA_acyltransferase; 1.
DR   Pfam; PF01853; MOZ_SAS; 1.
DR   SMART; SM00298; CHROMO; 1.
DR   SUPFAM; SSF55729; Acyl_CoA_acyltransferase; 1.
DR   SUPFAM; SSF54160; Chromodomain-like; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Acyltransferase; Alternative splicing;
KW   Chromatin regulator; Cytoplasm; Growth regulation; Isopeptide bond;
KW   Metal-binding; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation; Transferase; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    513       Histone acetyltransferase KAT5.
FT                                /FTId=PRO_0000051581.
FT   ZN_FING     261    283       C2HC-type.
FT   REGION      377    383       Acetyl-CoA binding (By similarity).
FT   ACT_SITE    369    369       Nucleophile (By similarity).
FT   BINDING     372    372       Acetyl-CoA (By similarity).
FT   BINDING     407    407       Acetyl-CoA (By similarity).
FT   MOD_RES      52     52       N6-acetyllysine (By similarity).
FT   MOD_RES      86     86       Phosphoserine (By similarity).
FT   MOD_RES      90     90       Phosphoserine; by CDK1 (By similarity).
FT   CROSSLNK    430    430       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    451    451       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   VAR_SEQ       1    211       Missing (in isoform 4).
FT                                /FTId=VSP_009105.
FT   VAR_SEQ       4      4       V -> VVSPVPGAGRREPGEVGRARGPPVADPGVALSPQ
FT                                (in isoform 3).
FT                                /FTId=VSP_009106.
FT   VAR_SEQ      96    147       Missing (in isoform 2).
FT                                /FTId=VSP_009107.
SQ   SEQUENCE   513 AA;  58598 MW;  EACEE4D544C0DB60 CRC64;
     MAEVGEIIEG CRLPVLRRNQ DNEDEWPLAE ILSVKDISGR KLFYVHYIDF NKRLDEWVTH
     ERLDLKKIQF PKKEAKTPTK NGLPGSRPGS PEREVPASAQ ASGKTLPIPV QITLRFNLPK
     EREAIPGGEP DQPLSSSSCL QPNHRSTKRK VEVVSPATPV PSETAPASVF PQNGSARRAV
     AAQPGRKRKS NCLGTDEDSQ DSSDGIPSAP RMTGSLVSDR SHDDIVTRMK NIECIELGRH
     RLKPWYFSPY PQELTTLPVL YLCEFCLKYG RSLKCLQRHL TKCDLRHPPG NEIYRKGTIS
     FFEIDGRKNK SYSQNLCLLA KCFLDHKTLY YDTDPFLFYV MTEYDCKGFH IVGYFSKEKE
     STEDYNVACI LTLPPYQRRG YGKLLIEFSY ELSKVEGKTG TPEKPLSDLG LLSYRSYWSQ
     TILEILMGLK SESGERPQIT INEISEITSI KKEDVISTLQ YLNLINYYKG QYILTLSEDI
     VDGHERAMLK RLLRIDSKCL HFTPKDWSKR GKW
//
ID   PGP_MOUSE               Reviewed;         321 AA.
AC   Q8CHP8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Phosphoglycolate phosphatase;
DE            Short=PGP;
DE            Short=PGPase;
DE            EC=3.1.3.18;
GN   Name=Pgp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: 2-phosphoglycolate + H(2)O = glycolate +
CC       phosphate.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       CbbY/CbbZ/Gph/YieH family.
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DR   EMBL; BC040100; AAH40100.1; -; mRNA.
DR   IPI; IPI00380195; -.
DR   RefSeq; NP_080230.2; NM_025954.3.
DR   UniGene; Mm.28541; -.
DR   HSSP; O59622; 1ZJJ.
DR   ProteinModelPortal; Q8CHP8; -.
DR   SMR; Q8CHP8; 11-319.
DR   STRING; Q8CHP8; -.
DR   REPRODUCTION-2DPAGE; IPI00380195; -.
DR   REPRODUCTION-2DPAGE; Q8CHP8; -.
DR   PRIDE; Q8CHP8; -.
DR   Ensembl; ENSMUST00000053024; ENSMUSP00000052866; ENSMUSG00000043445.
DR   GeneID; 67078; -.
DR   KEGG; mmu:67078; -.
DR   UCSC; uc008awe.1; mouse.
DR   CTD; 67078; -.
DR   MGI; MGI:1914328; Pgp.
DR   HOGENOM; HBG646794; -.
DR   HOVERGEN; HBG049429; -.
DR   InParanoid; Q8CHP8; -.
DR   OMA; SKTRAAY; -.
DR   OrthoDB; EOG4V9TR6; -.
DR   PhylomeDB; Q8CHP8; -.
DR   BRENDA; 3.1.3.18; 244.
DR   NextBio; 323510; -.
DR   ArrayExpress; Q8CHP8; -.
DR   Bgee; Q8CHP8; -.
DR   Genevestigator; Q8CHP8; -.
DR   GO; GO:0008967; F:phosphoglycolate phosphatase activity; IEA:EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   InterPro; IPR006357; HAD-SF_hydro_IIA.
DR   InterPro; IPR023215; NPhePase-like_dom.
DR   InterPro; IPR006349; PGP_euk.
DR   Gene3D; G3DSA:3.40.50.1000; HAD-like_dom; 2.
DR   Gene3D; G3DSA:3.40.50.10410; NPhePase-like_dom; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01460; HAD-SF-IIA; 1.
DR   TIGRFAMs; TIGR01452; PGP_euk; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Hydrolase.
FT   CHAIN         1    321       Phosphoglycolate phosphatase.
FT                                /FTId=PRO_0000316889.
FT   ACT_SITE     29     29       Nucleophile (By similarity).
SQ   SEQUENCE   321 AA;  34541 MW;  F083ED0432327A83 CRC64;
     MAEAEAGGDE ARCVRLSAER AKLLLAEVDT LLFDCDGVLW RGETAVPGAP ETLRALRARG
     KRLGFITNNS SKTRTAYAEK LRRLGFGGPV GPEAGLEVFG TAYCSALYLR QRLAGVPDPK
     AYVLGSPALA AELEAVGVTS VGVGPDVLHG DGPSDWLAVP LEPDVRAVVV GFDPHFSYMK
     LTKAVRYLQQ PDCLLVGTNM DNRLPLENGR FIAGTGCLVR AVEMAAQRQA DIIGKPSRFI
     FDCVSQEYGI NPERTVMVGD RLDTDILLGS TCSLKTILTL TGVSSLEDVK SNQESDCMFK
     KKMVPDFYVD SIADLLPALQ G
//
ID   NGEF_MOUSE              Reviewed;         710 AA.
AC   Q8CHT1; Q8R204; Q923H2; Q9JHT9;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Ephexin-1;
DE   AltName: Full=Eph-interacting exchange protein;
DE   AltName: Full=Neuronal guanine nucleotide exchange factor;
GN   Name=Ngef;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Brain;
RX   MEDLINE=20241931; PubMed=10777665; DOI=10.1006/geno.2000.6138;
RA   Rodrigues N.R., Theodosiou A.M., Nesbit M.A., Campbell L.,
RA   Tandle A.T., Saranath D., Davies K.E.;
RT   "Characterization of Ngef, a novel member of the Dbl family of genes
RT   expressed predominantly in the caudate nucleus.";
RL   Genomics 65:53-61(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND INTERACTION WITH
RP   EPHA4.
RC   STRAIN=C57BL/6;
RX   MEDLINE=21234975; PubMed=11336673; DOI=10.1016/S0092-8674(01)00314-2;
RA   Shamah S.M., Lin M.Z., Goldberg J.L., Estrach S., Sahin M., Hu L.,
RA   Bazalakova M., Neve R.L., Corfas G., Debant A., Greenberg M.E.;
RT   "EphA receptors regulate growth cone dynamics through the novel
RT   guanine nucleotide exchange factor ephexin.";
RL   Cell 105:233-244(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=15142957; DOI=10.1093/cercor/bhh063;
RA   Funatsu N., Inoue T., Nakamura S.;
RT   "Gene expression analysis of the late embryonic mouse cerebral cortex
RT   using DNA microarray: identification of several region- and layer-
RT   specific genes.";
RL   Cereb. Cortex 14:1031-1044(2004).
RN   [5]
RP   PHOSPHORYLATION BY SRC FAMILY KINASES.
RX   PubMed=15254079; DOI=10.1523/JNEUROSCI.0985-04.2004;
RA   Knoell B., Drescher U.;
RT   "Src family kinases are involved in EphA receptor-mediated retinal
RT   axon guidance.";
RL   J. Neurosci. 24:6248-6257(2004).
RN   [6]
RP   FUNCTION, AND MUTAGENESIS OF TYR-177.
RX   PubMed=15848799; DOI=10.1016/j.neuron.2005.01.030;
RA   Sahin M., Greer P.L., Lin M.Z., Poucher H., Eberhart J., Schmidt S.,
RA   Wright T.M., Shamah S.M., O'connell S., Cowan C.W., Hu L.,
RA   Goldberg J.L., Debant A., Corfas G., Krull C.E., Greenberg M.E.;
RT   "Eph-dependent tyrosine phosphorylation of ephexin1 modulates growth
RT   cone collapse.";
RL   Neuron 46:191-204(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-606, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-606, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Acts as a guanine nucleotide exchange factor (GEF) which
CC       differentially activates the GTPases RHOA, RAC1 and CDC42. Plays a
CC       role in axon guidance regulating ephrin-induced growth cone
CC       collapse. Upon activation by ephrin through EPHA4, the GEF
CC       activity switches toward RHOA resulting in its activation.
CC       Activated RHOA promotes cone retraction at the expense of RAC1-
CC       and CDC42-stimulated growth cone extension.
CC   -!- SUBUNIT: Interacts with EPHA4.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane (By
CC       similarity). Cell projection, growth cone (By similarity).
CC       Note=Associated with membranes. Localizes to axonal growth cones
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CHT1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CHT1-2; Sequence=VSP_020262, VSP_020263;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and to a lower
CC       extent in eye.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in E7 and to a lower extent
CC       in E11, E15 and E17 embryos. Expressed at E16.5 in the lateral
CC       regions of the cortex.
CC   -!- DOMAIN: The DH domain and the PH domain are both required to
CC       mediate interaction with EPHA4.
CC   -!- PTM: Src-dependent phosphorylation at Tyr-177 upon EPHA4
CC       activation increases the guanine exchange factor activity toward
CC       RHOA.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH22680.1; Type=Erroneous initiation;
CC       Sequence=CAC00698.1; Type=Frameshift; Positions=154;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AJ238898; CAC00698.1; ALT_FRAME; mRNA.
DR   EMBL; AY038025; AAK71494.1; -; mRNA.
DR   EMBL; BC022680; AAH22680.1; ALT_INIT; mRNA.
DR   EMBL; BC039279; AAH39279.1; -; mRNA.
DR   IPI; IPI00229725; -.
DR   IPI; IPI00405459; -.
DR   RefSeq; NP_001104784.1; NM_001111314.1.
DR   RefSeq; NP_063920.2; NM_019867.2.
DR   UniGene; Mm.435439; -.
DR   HSSP; Q5VV41; 1X6B.
DR   ProteinModelPortal; Q8CHT1; -.
DR   SMR; Q8CHT1; 265-598, 609-675.
DR   STRING; Q8CHT1; -.
DR   PhosphoSite; Q8CHT1; -.
DR   PRIDE; Q8CHT1; -.
DR   Ensembl; ENSMUST00000068681; ENSMUSP00000066894; ENSMUSG00000026259.
DR   GeneID; 53972; -.
DR   KEGG; mmu:53972; -.
DR   UCSC; uc007bwx.1; mouse.
DR   UCSC; uc007bwy.1; mouse.
DR   CTD; 53972; -.
DR   MGI; MGI:1858414; Ngef.
DR   eggNOG; roNOG11811; -.
DR   GeneTree; ENSGT00550000074493; -.
DR   HOGENOM; HBG755322; -.
DR   HOVERGEN; HBG058673; -.
DR   InParanoid; Q8CHT1; -.
DR   OrthoDB; EOG428213; -.
DR   NextBio; 310857; -.
DR   ArrayExpress; Q8CHT1; -.
DR   Bgee; Q8CHT1; -.
DR   CleanEx; MM_NGEF; -.
DR   Genevestigator; Q8CHT1; -.
DR   GermOnline; ENSMUSG00000026259; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00741; DH_1; FALSE_NEG.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell projection; Cytoplasm;
KW   Developmental protein; Differentiation;
KW   Guanine-nucleotide releasing factor; Membrane; Neurogenesis;
KW   Phosphoprotein; SH3 domain.
FT   CHAIN         1    710       Ephexin-1.
FT                                /FTId=PRO_0000248389.
FT   DOMAIN      273    457       DH.
FT   DOMAIN      489    601       PH.
FT   DOMAIN      612    673       SH3.
FT   REGION        1    272       Regulatory region; modulates activity
FT                                toward RHOA, RAC1 and CDC42.
FT   COMPBIAS    214    226       Poly-Glu.
FT   MOD_RES     177    177       Phosphotyrosine (By similarity).
FT   MOD_RES     606    606       Phosphoserine.
FT   VAR_SEQ       1     90       Missing (in isoform 2).
FT                                /FTId=VSP_020262.
FT   VAR_SEQ      91    125       KMGKSVNERSAFNLPQGRLSPWRTPAQRDTGAQEA -> ME
FT                                LLAAAFSAACAVDHDSSTSESDTRDSAAGHLPG (in
FT                                isoform 2).
FT                                /FTId=VSP_020263.
FT   MUTAGEN     177    177       Y->F: Loss of ephrin-mediated growth cone
FT                                collapse. No effect on interaction with
FT                                EPHA4.
FT   CONFLICT    530    530       R -> W (in Ref. 2; AAK71494).
SQ   SEQUENCE   710 AA;  82199 MW;  F255DE351E02A586 CRC64;
     METKNSEDWG KPQRKSESSS RKSNHGPAEM RPALPPENRE APETGEETQN EEPRRLIPIQ
     RHSLFNRAVR HRHKARSTSE RRASDQADLP KMGKSVNERS AFNLPQGRLS PWRTPAQRDT
     GAQEASESSS TPGNGTTPEE CPALTDSPTT LTEALQMIHP IPADSWRNLI EQIGLLYQEY
     RDKSTLQEIE TRRQQDAEIQ GNSDGSQVGE DAGEEEEEEE EGEEEELASP PERRALPQIC
     LLSNPHSRFN LWQDLPEIQS SGVLDILQPE EIRLQEAMFE LVTSEASYYK SLNLLVSHFM
     ENERLKKILH PSEAHILFSN VLDVMAVSER FLLELEHRME ENIVISDVCD IVYRYAADHF
     SVYITYVSNQ TYQERTYKQL LQEKAAFREL IAQLELDPKC KGLPFSSFLI LPFQRITRLK
     LLVQNILKRV EERSEREGTA LDAHKELEMV VKACNEGVRK MSRTEQMISI QKKMEFKIKS
     VPIISHSRWL LKQGELQQMS GPKTSRTLRT KKLFREIYLF LFNDLLVICR QIPGDKYQVF
     DSAPRGLLRV EELEDQGQTL ANVFILRLLE NADDREATYM LKASSQSEMK RWMTSLAPNR
     RTKFVSFTSR LLDCPQVQCV HPYVAQQPDE LTLELADILN ILEKTEDGWI FGERLHDQER
     GWFPSSMTEE ILNPKIRSQN LKECFRVHKM EDPQRSQNKD RRKLGSRNRQ
//
ID   EPN2_MOUSE              Reviewed;         595 AA.
AC   Q8CHU3; O70447; Q5NCM4; Q8BZ85;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Epsin-2;
DE   AltName: Full=EPS-15-interacting protein 2;
DE   AltName: Full=Intersectin-EH-binding protein 2;
DE            Short=Ibp2;
GN   Name=Epn2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 75-595 (ISOFORM 2), AND INTERACTION WITH
RP   ITSN1.
RX   MEDLINE=99030416; PubMed=9813051; DOI=10.1074/jbc.273.47.31401;
RA   Yamabhai M., Hoffman N.G., Hardison N.L., McPherson P.S.,
RA   Castagnoli L., Cesareni G., Kay B.K.;
RT   "Intersectin, a novel adaptor protein with two eps15 homology and five
RT   src homology 3 domains.";
RL   J. Biol. Chem. 273:31401-31407(1998).
RN   [5]
RP   PROTEIN SEQUENCE OF 77-86, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173 AND SER-182, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; THR-442 AND
RP   SER-449, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; SER-195 AND
RP   SER-443, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Plays a role in the formation of clathrin-coated
CC       invaginations and endocytosis (By similarity).
CC   -!- SUBUNIT: Binds EPS15, AP-2 and clathrin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=In punctate
CC       structures throughout the cell and particularly concentrated in
CC       the region of the Golgi complex (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CHU3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CHU3-2; Sequence=VSP_009157;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The NPF repeat domain is involved in EPS15 binding.
CC   -!- DOMAIN: The DPW repeat domain is involved in AP-2 and clathrin
CC       binding.
CC   -!- PTM: Ubiquitinated (By similarity).
CC   -!- SIMILARITY: Belongs to the epsin family.
CC   -!- SIMILARITY: Contains 1 ENTH (epsin N-terminal homology) domain.
CC   -!- SIMILARITY: Contains 2 UIM (ubiquitin-interacting motif) repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC97476.1; Type=Erroneous initiation;
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK036331; BAC29387.1; -; mRNA.
DR   EMBL; AL604029; CAI24192.1; -; Genomic_DNA.
DR   EMBL; BC039138; AAH39138.1; -; mRNA.
DR   EMBL; AF057286; AAC97476.1; ALT_INIT; mRNA.
DR   IPI; IPI00336844; -.
DR   IPI; IPI00400174; -.
DR   RefSeq; NP_034278.1; NM_010148.2.
DR   UniGene; Mm.139695; -.
DR   UniGene; Mm.436466; -.
DR   ProteinModelPortal; Q8CHU3; -.
DR   SMR; Q8CHU3; 1-144.
DR   MINT; MINT-93098; -.
DR   STRING; Q8CHU3; -.
DR   PhosphoSite; Q8CHU3; -.
DR   PRIDE; Q8CHU3; -.
DR   Ensembl; ENSMUST00000001063; ENSMUSP00000001063; ENSMUSG00000001036.
DR   Ensembl; ENSMUST00000116368; ENSMUSP00000112069; ENSMUSG00000001036.
DR   GeneID; 13855; -.
DR   KEGG; mmu:13855; -.
DR   UCSC; uc007jhv.1; mouse.
DR   UCSC; uc007jhy.1; mouse.
DR   CTD; 13855; -.
DR   MGI; MGI:1333766; Epn2.
DR   eggNOG; roNOG14097; -.
DR   GeneTree; ENSGT00550000074611; -.
DR   HOVERGEN; HBG006690; -.
DR   OrthoDB; EOG4HMJ9P; -.
DR   PhylomeDB; Q8CHU3; -.
DR   NextBio; 284722; -.
DR   ArrayExpress; Q8CHU3; -.
DR   Bgee; Q8CHU3; -.
DR   CleanEx; MM_EPN2; -.
DR   Genevestigator; Q8CHU3; -.
DR   GermOnline; ENSMUSG00000001036; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR013809; Epsin-like_N.
DR   InterPro; IPR001026; Epsin_dom_N.
DR   InterPro; IPR003903; Ubiquitin-int_motif.
DR   Gene3D; G3DSA:1.25.40.90; ENTH_VHS; 1.
DR   Pfam; PF01417; ENTH; 1.
DR   SMART; SM00273; ENTH; 1.
DR   SMART; SM00726; UIM; 2.
DR   SUPFAM; SSF48464; ENTH_VHS; 1.
DR   PROSITE; PS50942; ENTH; 1.
DR   PROSITE; PS50330; UIM; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Direct protein sequencing;
KW   Endocytosis; Lipid-binding; Phosphoprotein; Repeat; Ubl conjugation.
FT   CHAIN         1    595       Epsin-2.
FT                                /FTId=PRO_0000074517.
FT   DOMAIN       12    144       ENTH.
FT   REPEAT      218    237       UIM 1.
FT   REPEAT      255    274       UIM 2.
FT   REPEAT      313    315       1.
FT   REPEAT      325    327       2.
FT   REPEAT      338    340       3.
FT   REPEAT      352    354       4.
FT   REPEAT      370    372       5.
FT   REPEAT      387    389       6.
FT   REPEAT      494    496       1.
FT   REPEAT      508    510       2.
FT   REPEAT      591    593       3.
FT   REGION      313    389       6 X 3 AA repeats of [DE]-P-W.
FT   REGION      494    593       3 X 3 AA repeats of N-P-F.
FT   BINDING       8      8       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   BINDING      11     11       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   BINDING      25     25       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   BINDING      30     30       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   BINDING      63     63       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   BINDING      73     73       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   MOD_RES     173    173       Phosphoserine.
FT   MOD_RES     182    182       Phosphoserine.
FT   MOD_RES     192    192       Phosphoserine.
FT   MOD_RES     195    195       Phosphoserine.
FT   MOD_RES     442    442       Phosphothreonine.
FT   MOD_RES     443    443       Phosphoserine.
FT   MOD_RES     449    449       Phosphoserine.
FT   VAR_SEQ     237    248       Missing (in isoform 2).
FT                                /FTId=VSP_009157.
FT   CONFLICT     75     75       Y -> S (in Ref. 4; AAC97476).
SQ   SEQUENCE   595 AA;  63472 MW;  255DC7BC7E1B2D13 CRC64;
     MTTSSIRRQM KNIVNNYSEA EIKVREATSN DPWGPSSSLM TEIADLTYNV VAFSEIMSMV
     WKRLNDHGKN WRHVYKALTL LDYLIKTGSE RVAQQCRENI FAIQTLKDFQ YIDRDGKDQG
     INVREKSKQL VALLKDEERL KVERVQALKT KERMAQVATG VGSNQITFGR GSSQPNLSTS
     YSEQEYGKAG GSPASYHGST SPRVSSELEQ ARPQTSGEEE LQLQLALAMS REVAEQSSES
     VQTARGSKEE RLRRGDDLRL QMALEESRRD TVKVPKKKEA KACCKPGSHS QQTTLLDLMD
     ALPSSGPVTQ KTEPWSAGAS ANQTNPWGGT VAPSNITDPW PSFGTKPAAS VDPWGVPTTA
     STQSVPKNSD PWAASQQPAS NAGKTTDAWG AAKPSSASGS FELFSNFNGT VKDDFSEFDN
     LRTSKKPAES GASVPPQDSR TTSPDLFESQ SLTSASSKPS SARKTPESFL GPNAALVNLD
     SLVTKPAPPA QSLNPFLAPG AAAPAPVNPF QVNQPQPLTL NQLRGSPVLG SSASFGSGPG
     VETVAPMTSV APHSSVGASG SSLTPLGPTA MNMVGSVGIP PSAAQSTGTT NPFLL
//
ID   EI2BE_MOUSE             Reviewed;         717 AA.
AC   Q8CHW4; Q3TU39;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Translation initiation factor eIF-2B subunit epsilon;
DE   AltName: Full=eIF-2B GDP-GTP exchange factor subunit epsilon;
GN   Name=Eif2b5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713 AND SER-714, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Catalyzes the exchange of eukaryotic initiation factor
CC       2-bound GDP for GTP (By similarity).
CC   -!- SUBUNIT: Complex of five different subunits; alpha, beta, gamma,
CC       delta and epsilon (By similarity).
CC   -!- SIMILARITY: Belongs to the eIF-2B gamma/epsilon subunits family.
CC   -!- SIMILARITY: Contains 1 W2 domain.
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DR   EMBL; AK160985; BAE36132.1; -; mRNA.
DR   EMBL; BC038620; AAH38620.1; -; mRNA.
DR   EMBL; BC085255; AAH85255.1; -; mRNA.
DR   IPI; IPI00261239; -.
DR   RefSeq; NP_758469.1; NM_172265.2.
DR   UniGene; Mm.233855; -.
DR   ProteinModelPortal; Q8CHW4; -.
DR   SMR; Q8CHW4; 354-450, 543-711.
DR   STRING; Q8CHW4; -.
DR   PhosphoSite; Q8CHW4; -.
DR   PRIDE; Q8CHW4; -.
DR   Ensembl; ENSMUST00000003320; ENSMUSP00000003320; ENSMUSG00000003235.
DR   GeneID; 224045; -.
DR   KEGG; mmu:224045; -.
DR   UCSC; uc007ypu.1; mouse.
DR   CTD; 224045; -.
DR   MGI; MGI:2446176; Eif2b5.
DR   eggNOG; roNOG09172; -.
DR   GeneTree; ENSGT00510000047568; -.
DR   HOGENOM; HBG445046; -.
DR   HOVERGEN; HBG051460; -.
DR   InParanoid; Q8CHW4; -.
DR   OMA; SRANKRS; -.
DR   OrthoDB; EOG4THVSP; -.
DR   PhylomeDB; Q8CHW4; -.
DR   NextBio; 377029; -.
DR   ArrayExpress; Q8CHW4; -.
DR   Bgee; Q8CHW4; -.
DR   Genevestigator; Q8CHW4; -.
DR   GermOnline; ENSMUSG00000003235; Mus musculus.
DR   GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0014002; P:astrocyte development; ISS:UniProtKB.
DR   GO; GO:0042552; P:myelination; ISS:UniProtKB.
DR   GO; GO:0014003; P:oligodendrocyte development; ISS:UniProtKB.
DR   GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR   GO; GO:0045948; P:positive regulation of translational initiation; ISS:UniProtKB.
DR   GO; GO:0009749; P:response to glucose stimulus; ISS:UniProtKB.
DR   GO; GO:0009408; P:response to heat; ISS:UniProtKB.
DR   GO; GO:0043434; P:response to peptide hormone stimulus; ISS:UniProtKB.
DR   GO; GO:0016070; P:RNA metabolic process; IEA:InterPro.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003307; eIF5C.
DR   InterPro; IPR016021; MIF4-like_typ_1/2/3.
DR   InterPro; IPR011004; Trimer_LpxA-like.
DR   Gene3D; G3DSA:1.25.40.180; MIF4-like_typ_1/2/3; 1.
DR   Pfam; PF02020; W2; 1.
DR   SMART; SM00515; eIF5C; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF51161; Trimer_LpxA_like; 1.
DR   PROSITE; PS51363; W2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Initiation factor; Phosphoprotein; Protein biosynthesis.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    717       Translation initiation factor eIF-2B
FT                                subunit epsilon.
FT                                /FTId=PRO_0000239429.
FT   DOMAIN      539    716       W2.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     521    521       Phosphoserine (By similarity).
FT   MOD_RES     525    525       Phosphoserine (By similarity).
FT   MOD_RES     528    528       Phosphoserine (By similarity).
FT   MOD_RES     536    536       Phosphoserine (By similarity).
FT   MOD_RES     540    540       Phosphoserine.
FT   MOD_RES     713    713       Phosphoserine.
FT   MOD_RES     714    714       Phosphoserine.
FT   CONFLICT     54     54       P -> H (in Ref. 1; BAE36132).
SQ   SEQUENCE   717 AA;  80086 MW;  61455A437B7D513B CRC64;
     MAATAAVPGA AAGRASKRGG GGSGGGGTQG AEEEPPPPLQ AVLVADSFNR RFFPISKDQP
     RVLLPLANVA LIDYTLEFLT ATGVQETFVF CCWKAAQIKE HLQKSKWCHP TSPNVVRIIT
     SELYRSLGDV LRDVDAKALV RSDFLLIYGD VISNINICRA LEEHRLRRKL EKNVSVMTMV
     FKESSPSHPT RCHEDNVVMA VDSATNRVLH FQKTQGLRRF SFPLSLFQGS GDGVEIRYDL
     LDCHISICSP QVAQLFTDNF DYQTRDDFVR GILMNEEVLG NQIHLHVTTR EYGARVSNLH
     MYSAVCADVI RRWVYPLTPE VNFTDSTTQS YTHSRHNIYR GPEVSLGHGS VLEENVLLGA
     GTVIGSNCSI TNSVIGPNCH IGDNVVLDQA YLWQGVRVAA GAQIHQSLLC DRAEVKERVK
     LKPYCVLTSQ VVVGPDITLP EGSVISLHPP DAEEDEDDGQ FSDDSGADQE KEKVKLKGYN
     PAEVGLEGQG YLWKAEGVNS KEDEELRQSL WGLMIKTEEE SETESEGSVD PEELDSRAGS
     PQLDDIRVFQ NEVLGTLQRG REENISCENL VLEINSLKHA YNISLKEVMQ VLTLVVLEFP
     LQQVDGLLDP NRYCALLLPL LKAWSPVLRN YIKRAADHLE ALAAIEDFFL EHETLVTSMA
     KVLMAFYQLE ILAEETILSW FSQRDTTDEG QQLRKNQQLQ RFIQWLREAE EESSEDD
//
ID   RFTN2_MOUSE             Reviewed;         500 AA.
AC   Q8CHX7; Q8R306; Q9CXJ5;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Raftlin-2;
DE   AltName: Full=Raft-linking protein 2;
GN   Name=Rftn2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CHX7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CHX7-2; Sequence=VSP_015324, VSP_015325;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the raftlin family.
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DR   EMBL; AK014318; BAB29269.1; ALT_TERM; mRNA.
DR   EMBL; BC026871; AAH26871.1; -; mRNA.
DR   EMBL; BC038341; AAH38341.1; -; mRNA.
DR   IPI; IPI00229775; -.
DR   IPI; IPI00648355; -.
DR   RefSeq; NP_082989.1; NM_028713.1.
DR   UniGene; Mm.292050; -.
DR   ProteinModelPortal; Q8CHX7; -.
DR   PhosphoSite; Q8CHX7; -.
DR   PRIDE; Q8CHX7; -.
DR   Ensembl; ENSMUST00000027121; ENSMUSP00000027121; ENSMUSG00000025978.
DR   Ensembl; ENSMUST00000114428; ENSMUSP00000110071; ENSMUSG00000025978.
DR   GeneID; 74013; -.
DR   KEGG; mmu:74013; -.
DR   UCSC; uc007bag.1; mouse.
DR   CTD; 74013; -.
DR   MGI; MGI:1921263; Rftn2.
DR   eggNOG; roNOG08734; -.
DR   GeneTree; ENSGT00530000063609; -.
DR   HOGENOM; HBG714975; -.
DR   HOVERGEN; HBG054056; -.
DR   InParanoid; Q8CHX7; -.
DR   OMA; QTPERKG; -.
DR   OrthoDB; EOG4X0MSQ; -.
DR   PhylomeDB; Q8CHX7; -.
DR   NextBio; 339532; -.
DR   ArrayExpress; Q8CHX7; -.
DR   Bgee; Q8CHX7; -.
DR   CleanEx; MM_RFTN2; -.
DR   Genevestigator; Q8CHX7; -.
DR   GermOnline; ENSMUSG00000025978; Mus musculus.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Lipoprotein; Membrane; Myristate;
KW   Palmitate.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    500       Raftlin-2.
FT                                /FTId=PRO_0000089339.
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
FT   LIPID         3      3       S-palmitoyl cysteine (By similarity).
FT   VAR_SEQ     309    344       GDQLPKSLEGFFIYEEEGSGVPGSNRRGNDAIVVEQ -> V
FT                                AKLEAFQLSVSDKLPKGKQKYSFQSLSGIPASGLA (in
FT                                isoform 2).
FT                                /FTId=VSP_015324.
FT   VAR_SEQ     345    500       Missing (in isoform 2).
FT                                /FTId=VSP_015325.
SQ   SEQUENCE   500 AA;  54972 MW;  1D5DC3727517C68A CRC64;
     MGCGLRKLED PDESSPGKIF STLKRPQVET KTEFAYEYAL LDFTLQASTN PDVIKINSVL
     DIVAKVEDYY LKGYVVGAIH PVIQPVGQRK HLPASHLYRA VLSRLKLSPK HSAAGGQRRA
     RLVMEECPLT CEAQANDAAK ELMDKINAAA KRGMKFVGLV SQCYLPSMHC NGASHDGVAE
     SGLHVRQDSQ DNCKGWNEGA LGGHLSESGV EEEPQHESGQ HQTERNSSPS YANPKRGEAP
     DGKLYMVFNA FEEDAASWAY QEGVLSMKVT RKGAVISALD ANWLELTTFY YKQGFSLIDS
     FVCWETPKGD QLPKSLEGFF IYEEEGSGVP GSNRRGNDAI VVEQWTVIEG CEIKTDYGPL
     LHTLAEFGWL LTSVLPTPIL RHDSEGNLAT KQVVFLQRPV TWNSAAQTPE RKGSRLLKGE
     DRNKVSSRSL GLDTNASQAA GGRAPLEEGS LSPSRECWTK EERPAQSDSF SGFSSSDSVL
     RELDDGQFDQ EEGVTQVTCM
//
ID   P66A_MOUSE              Reviewed;         629 AA.
AC   Q8CHY6; Q8BTQ2; Q8VEC9;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Transcriptional repressor p66 alpha;
DE   AltName: Full=GATA zinc finger domain-containing protein 2A;
GN   Name=Gatad2a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N, and FVB/N-3; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-103 AND SER-110,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-103 AND SER-105,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Transcriptional repressor (By similarity).
CC   -!- SUBUNIT: Binds MBD2 and MBD3. Part of a complex containing MBD2,
CC       HDAC1 and/or HDAC2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle (By similarity).
CC   -!- SIMILARITY: Contains 1 GATA-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH19178.1; Type=Erroneous initiation;
CC       Sequence=AAH31407.1; Type=Erroneous initiation;
CC       Sequence=BAC40736.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK089074; BAC40736.1; ALT_INIT; mRNA.
DR   EMBL; BC019178; AAH19178.1; ALT_INIT; mRNA.
DR   EMBL; BC031407; AAH31407.1; ALT_INIT; mRNA.
DR   EMBL; BC038221; AAH38221.2; -; mRNA.
DR   IPI; IPI00229784; -.
DR   RefSeq; NP_001106816.1; NM_001113345.1.
DR   RefSeq; NP_001106817.1; NM_001113346.1.
DR   UniGene; Mm.270044; -.
DR   STRING; Q8CHY6; -.
DR   PhosphoSite; Q8CHY6; -.
DR   PRIDE; Q8CHY6; -.
DR   Ensembl; ENSMUST00000065169; ENSMUSP00000070229; ENSMUSG00000036180.
DR   Ensembl; ENSMUST00000116463; ENSMUSP00000112164; ENSMUSG00000036180.
DR   GeneID; 234366; -.
DR   KEGG; mmu:234366; -.
DR   UCSC; uc009lyf.1; mouse.
DR   CTD; 234366; -.
DR   MGI; MGI:2384585; Gatad2a.
DR   eggNOG; roNOG15630; -.
DR   GeneTree; ENSGT00390000004097; -.
DR   HOGENOM; HBG717465; -.
DR   HOVERGEN; HBG053401; -.
DR   InParanoid; Q8CHY6; -.
DR   OrthoDB; EOG4320XZ; -.
DR   PhylomeDB; Q8CHY6; -.
DR   NextBio; 460466; -.
DR   ArrayExpress; Q8CHY6; -.
DR   Bgee; Q8CHY6; -.
DR   CleanEx; MM_GATAD2A; -.
DR   Genevestigator; Q8CHY6; -.
DR   GermOnline; ENSMUSG00000036180; Mus musculus.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0016581; C:NuRD complex; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030674; F:protein binding, bridging; ISS:UniProtKB.
DR   GO; GO:0016564; F:transcription repressor activity; ISS:UniProtKB.
DR   GO; GO:0021506; P:anterior neuropore closure; IMP:MGI.
DR   GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR   GO; GO:0010172; P:embryonic body morphogenesis; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; ISS:UniProtKB.
DR   GO; GO:0001842; P:neural fold formation; IMP:MGI.
DR   GO; GO:0012501; P:programmed cell death; IMP:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   PROSITE; PS00344; GATA_ZN_FINGER_1; FALSE_NEG.
DR   PROSITE; PS50114; GATA_ZN_FINGER_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Coiled coil; Metal-binding; Nucleus; Phosphoprotein; Repressor;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    629       Transcriptional repressor p66 alpha.
FT                                /FTId=PRO_0000083501.
FT   ZN_FING     410    462       GATA-type.
FT   COILED      135    170       Potential.
FT   COMPBIAS    402    407       Poly-Ala.
FT   MOD_RES      96     96       Phosphoserine.
FT   MOD_RES     103    103       Phosphoserine.
FT   MOD_RES     105    105       Phosphoserine.
FT   MOD_RES     109    109       Phosphoserine (By similarity).
FT   MOD_RES     110    110       Phosphoserine.
FT   MOD_RES     185    185       Phosphothreonine (By similarity).
FT   MOD_RES     335    335       Phosphoserine (By similarity).
FT   MOD_RES     543    543       Phosphoserine (By similarity).
FT   MOD_RES     545    545       Phosphoserine (By similarity).
FT   MOD_RES     594    594       Phosphoserine (By similarity).
FT   CONFLICT    248    248       Q -> QQ (in Ref. 1; BAC40736).
SQ   SEQUENCE   629 AA;  67334 MW;  5EA79CC71C9E29A4 CRC64;
     MSEEACRTRS QKRTLEPDLT EDDVENKKMK MEKGSSELTV DGDSRVMPEP SAGSAQGLLR
     TTEAMGTGSG EGLLGDGPVD MRTSHSDMKS EKRPPSPDVI VLSDSEQPSS PRVNGLTTVA
     LKDTSTEALL KSSPEERERM IKQLKEELRL EEAKLVLLKK LRQSQIQKEA TAQKPTASSG
     STVTTPPPLV RGTQNIPAGK TSLQTSSTRI PGSIIPPPLV RGGQQVSAKL GPQASSQVVM
     PPLVRGAQIH NIRQHSSTGP PPLLLAPRAS VPSMQIQGQR IIQQGLIRVA NVPNTSLLVN
     IPQPTAASMK GTAVASAQAN STPTSVASVV ASAESPASRQ AAAKLALRKQ LEKTLLEIPP
     PKPPAPEMNF LPSAANNEFI YLVGLEEVVQ NLLETQAGRI SATAAAAVLS REPYMCVQCK
     TDFTCRWREK GGAVMCENCM TSNQKKALKV EHTSRLKAAF VKALQQEQEM EQRLLQQGVG
     TASIKAEPAA PHPTLKQVIK PRRKLAFRSG EARVWNNGSS LQASSQLSRG SATAPRGVLH
     TFSQSPKLQN AASATALVSR TGRHSERVVG TGKGTASNWK KTPLSTGGTL AFVSPSLAVH
     KTSSAVDRQR EYLLDMIPPR SIPQSATWK
//
ID   FWCH1_MOUSE             Reviewed;         673 AA.
AC   Q8CI03; Q3TH83; Q6ZPN0; Q8C792;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=FLYWCH-type zinc finger-containing protein 1;
GN   Name=Flywch1; Synonyms=Kiaa1552;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-666 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 193-673 (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8CI03-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CI03-2; Sequence=VSP_030283;
CC       Name=3;
CC         IsoId=Q8CI03-3; Sequence=VSP_030282;
CC   -!- SIMILARITY: Contains 5 FLYWCH-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE40315.1; Type=Frameshift; Positions=174, 197, 213;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK052314; BAC34932.1; -; mRNA.
DR   EMBL; AK168389; BAE40315.1; ALT_FRAME; mRNA.
DR   EMBL; BC038031; AAH38031.1; -; mRNA.
DR   EMBL; AK129391; BAC98201.1; -; mRNA.
DR   IPI; IPI00229692; -.
DR   IPI; IPI00761768; -.
DR   IPI; IPI00880339; -.
DR   RefSeq; NP_722486.2; NM_153791.2.
DR   UniGene; Mm.328835; -.
DR   PhosphoSite; Q8CI03; -.
DR   PRIDE; Q8CI03; -.
DR   Ensembl; ENSMUST00000045517; ENSMUSP00000040022; ENSMUSG00000040097.
DR   Ensembl; ENSMUST00000086325; ENSMUSP00000083505; ENSMUSG00000040097.
DR   GeneID; 224613; -.
DR   KEGG; mmu:224613; -.
DR   UCSC; uc008ath.1; mouse.
DR   CTD; 224613; -.
DR   MGI; MGI:2442638; Flywch1.
DR   GeneTree; ENSGT00530000064166; -.
DR   HOVERGEN; HBG098123; -.
DR   OrthoDB; EOG49GKG6; -.
DR   NextBio; 377247; -.
DR   ArrayExpress; Q8CI03; -.
DR   Bgee; Q8CI03; -.
DR   CleanEx; MM_FLYWCH1; -.
DR   Genevestigator; Q8CI03; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR007588; Znf_FLYWCH.
DR   Pfam; PF04500; FLYWCH; 5.
PE   2: Evidence at transcript level;
KW   Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW   Phosphoprotein; Repeat; Zinc; Zinc-finger.
FT   CHAIN         1    673       FLYWCH-type zinc finger-containing
FT                                protein 1.
FT                                /FTId=PRO_0000314461.
FT   ZN_FING      92    150       FLYWCH-type 1.
FT   ZN_FING     235    293       FLYWCH-type 2.
FT   ZN_FING     402    460       FLYWCH-type 3.
FT   ZN_FING     490    548       FLYWCH-type 4.
FT   ZN_FING     581    639       FLYWCH-type 5.
FT   COMPBIAS    660    670       Lys-rich.
FT   MOD_RES      21     21       Phosphoserine (By similarity).
FT   VAR_SEQ       1    287       Missing (in isoform 3).
FT                                /FTId=VSP_030282.
FT   VAR_SEQ     672    673       IH -> KSKSKN (in isoform 2).
FT                                /FTId=VSP_030283.
FT   CONFLICT    260    260       S -> G (in Ref. 1; BAE40315).
SQ   SEQUENCE   673 AA;  77114 MW;  DEEC50AE676F551E CRC64;
     MPLPEPSEQD CESLRAGQEP SVGARKPQES SNLVPARDKE RPKPTDVASQ ETSSTATLPN
     NTLQVAPVKK QGRIIHRKRS RVDAVPPQPL EFLKTPFGGR LLVHKSFLYK QEKAVGDKVY
     WKCRQHSELS CRGRAITRGF RVTEMRDHCH PPEKEGLDRK KRHRGRPPSS ALPEGAEVQE
     DEVSLWLYPV EPEPTPQPST ETPEEEQGYR SLALQSLPPK KRPTPGVVRY RPLEFLKTCY
     GGTFLVHQSF LYKREKTVGS KVYWTCREHA VHGCRSRAIT QGQRVTVMRS HCHSPDIEGL
     QARRQQEKTI KKIQARRIGA GDLEDCDDIE DSLLQGVDSL FYRRGQGTLT LSRSKSKSKS
     KSRSKSKSKS RSRSRKRAKK QQESSQEPPE EDQDVDPRGP EFLKTPLGGN FLVYESFLYR
     REKVAGEKVY WTCRDQARMG CRSRAITQGR QVTVMRSHCH PPDLLGLETL RQREKRPGPS
     QWDGPEGPEF LKTPLGGSFL VYESFLYRRE KATGDKVYWT CRDQARMGCR SRAITQGQRV
     MVMRRHCHPP DMGGLEALRQ RENFPNLTHW EGPEPLQPLE FLRTSLGGRF LVYESFLYRK
     EKAAGEKVYW MCRDQARLGC RSRAITQGRR VMVMRSHCHP PDLAGLEALR QREKAPSAAK
     KKKKKKKKKK GIH
//
ID   SLAI2_MOUSE             Reviewed;         581 AA.
AC   Q8CI08; Q05DK1; Q3UJI9; Q6ZPQ5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=SLAIN motif-containing protein 2;
GN   Name=Slain2; Synonyms=Kiaa1458;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=DBA/2;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-406 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 182-581 (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-324, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87 AND SER-392, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CI08-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CI08-2; Sequence=VSP_030834;
CC   -!- SIMILARITY: Belongs to the SLAIN motif-containing family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH10836.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAH10836.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential vector sequence;
CC       Sequence=AAH38019.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAC98175.1; Type=Erroneous initiation;
CC       Sequence=BAE27166.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK129365; BAC98175.1; ALT_INIT; mRNA.
DR   EMBL; AK146432; BAE27166.1; ALT_INIT; mRNA.
DR   EMBL; BC010836; AAH10836.1; ALT_SEQ; mRNA.
DR   EMBL; BC038019; AAH38019.1; ALT_SEQ; mRNA.
DR   IPI; IPI00229697; -.
DR   IPI; IPI00757214; -.
DR   RefSeq; NP_001106894.1; NM_001113423.1.
DR   RefSeq; NP_705795.2; NM_153567.2.
DR   UniGene; Mm.403691; -.
DR   UniGene; Mm.478300; -.
DR   PhosphoSite; Q8CI08; -.
DR   Ensembl; ENSMUST00000086498; ENSMUSP00000083684; ENSMUSG00000036087.
DR   GeneID; 75991; -.
DR   KEGG; mmu:75991; -.
DR   UCSC; uc008xsj.1; mouse.
DR   CTD; 75991; -.
DR   MGI; MGI:1923241; Slain2.
DR   eggNOG; roNOG13200; -.
DR   GeneTree; ENSGT00390000017860; -.
DR   HOGENOM; HBG506689; -.
DR   HOVERGEN; HBG072961; -.
DR   InParanoid; Q8CI08; -.
DR   OrthoDB; EOG4HX51B; -.
DR   NextBio; 344391; -.
DR   ArrayExpress; Q8CI08; -.
DR   Bgee; Q8CI08; -.
DR   CleanEx; MM_SLAIN2; -.
DR   Genevestigator; Q8CI08; -.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Phosphoprotein.
FT   CHAIN         1    581       SLAIN motif-containing protein 2.
FT                                /FTId=PRO_0000316967.
FT   COILED        4     39       Potential.
FT   COMPBIAS    124    128       Poly-Glu.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      48     48       Phosphoserine (By similarity).
FT   MOD_RES      55     55       Phosphoserine (By similarity).
FT   MOD_RES      63     63       Phosphoserine (By similarity).
FT   MOD_RES      87     87       Phosphoserine.
FT   MOD_RES     147    147       Phosphoserine (By similarity).
FT   MOD_RES     160    160       Phosphoserine (By similarity).
FT   MOD_RES     179    179       Phosphoserine (By similarity).
FT   MOD_RES     234    234       Phosphoserine (By similarity).
FT   MOD_RES     248    248       Phosphoserine (By similarity).
FT   MOD_RES     251    251       Phosphoserine (By similarity).
FT   MOD_RES     252    252       Phosphoserine (By similarity).
FT   MOD_RES     255    255       Phosphoserine (By similarity).
FT   MOD_RES     258    258       Phosphoserine (By similarity).
FT   MOD_RES     316    316       Phosphoserine (By similarity).
FT   MOD_RES     324    324       Phosphoserine.
FT   MOD_RES     378    378       Phosphoserine (By similarity).
FT   MOD_RES     392    392       Phosphoserine.
FT   MOD_RES     414    414       Phosphoserine (By similarity).
FT   MOD_RES     419    419       Phosphoserine (By similarity).
FT   MOD_RES     434    434       Phosphoserine (By similarity).
FT   MOD_RES     457    457       Phosphoserine (By similarity).
FT   MOD_RES     463    463       Phosphoserine (By similarity).
FT   MOD_RES     468    468       Phosphoserine (By similarity).
FT   VAR_SEQ     454    455       AI -> ATSQRLKSLPRTSLKAKQLLPTSSTKRV (in
FT                                isoform 2).
FT                                /FTId=VSP_030834.
FT   CONFLICT    462    462       R -> H (in Ref. 2; BAE27166).
SQ   SEQUENCE   581 AA;  62378 MW;  1C412715B6E313DC CRC64;
     MEDVNSNVNA DQEVRKLQEL VKKLEKQNEQ LRSRSGAVQG AGLLGPGSPA RVGVSTPSSG
     AASPRGFPLG LGAKASGGAG SGPRRTSSED LRDATSLLAA GEGGLLDEVE PLRPDELERL
     SGWEEEEESW LYSSPKKKLT PMQKSVSPLV WCRQVLDYPS PDVECAKKSL IHKLDQTMSA
     LKRQNLYNNP FNSVSYSNSY SPNASSPYSS GFNSPSSTPV RPPIVKQLIL PGNSGNFKSS
     SDRNPPLSPQ SSIDSELSAS ELDEDSIGSN YKLNDVTDVQ ILARMQEESL RQEYAASTSR
     RSSGSSCNST RRGTFSDQEL DAQSLDDEDD SLQHAVHPAL NRFSPSPRNS PRPSPKQSPR
     NSPRSRSPAR GIEYSRASPQ PMISRLQQPR LSLQGHPTDL QTSNVKNEEK LRRSLPNLSR
     TSSTQVDSVK SSRSDSNFQV PNGGIPRMQP QASAIPSPGK FRSPAAPSPL ALRQPVKAFS
     NHGSGSGSQE TTQFTQTTSS PGPPVVQNSA PANPSSNINS ATLTRPAGTT AMRSGLPRPS
     APSAGGIPVP RSKLVQPVRR SLPAPKSYGS MKDDSWKDGC Y
//
ID   GNL3_MOUSE              Reviewed;         538 AA.
AC   Q8CI11; Q811R9; Q811S8; Q8BK21;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Guanine nucleotide-binding protein-like 3;
DE   AltName: Full=Nucleolar GTP-binding protein 3;
DE   AltName: Full=Nucleostemin;
GN   Name=Gnl3; Synonyms=Ns;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), DEVELOPMENTAL STAGE,
RP   AND TISSUE SPECIFICITY.
RC   STRAIN=129/SvJ;
RX   MEDLINE=22352080; PubMed=12464630; DOI=10.1101/gad.55671;
RA   Tsai R.Y.L., McKay R.D.G.;
RT   "A nucleolar mechanism controlling cell proliferation in stem and
RT   cancer cells.";
RL   Genes Dev. 16:2991-3003(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May be required to maintain the proliferative capacity
CC       of stem cells (By similarity).
CC   -!- SUBUNIT: May interact with p53/TP53 via its basic domain (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Nucleus, nucleolus
CC       (By similarity). Note=Shuttles between the nucleus and nucleolus
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Long;
CC         IsoId=Q8CI11-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short;
CC         IsoId=Q8CI11-2; Sequence=VSP_013412;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in the adult bone marrow population
CC       that is enriched in hematopoietic stem cells.
CC   -!- DEVELOPMENTAL STAGE: Expressed at E8.5 and E10.5 in the cerebral
CC       cortex; expression declines rapidly from this point.
CC   -!- DOMAIN: The basic domain (B) allows nucleolar localization in the
CC       absence of GTP. The intermediate domain (I) inhibits nucleolar
CC       localization by the B domain and is required for exit from the
CC       nucleolus. Exit from the nucleolus to the nucleoplasm requires
CC       both the I and the acidic (A) domains, and may be triggered by GTP
CC       hydrolysis (By similarity).
CC   -!- DOMAIN: In contrast to other GTP-binding proteins, this family is
CC       characterized by a circular permutation of the GTPase motifs
CC       described by a G4-G1-G3 pattern.
CC   -!- SIMILARITY: Belongs to the MMR1/HSR1 GTP-binding protein family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AY181025; AAO19472.1; -; mRNA.
DR   EMBL; AY185498; AAO19473.1; -; mRNA.
DR   EMBL; AK077523; BAC36844.1; -; mRNA.
DR   EMBL; BC037996; AAH37996.2; -; mRNA.
DR   IPI; IPI00222461; -.
DR   IPI; IPI00399477; -.
DR   RefSeq; NP_705775.2; NM_153547.5.
DR   UniGene; Mm.88512; -.
DR   ProteinModelPortal; Q8CI11; -.
DR   SMR; Q8CI11; 127-399.
DR   STRING; Q8CI11; -.
DR   PhosphoSite; Q8CI11; -.
DR   PRIDE; Q8CI11; -.
DR   Ensembl; ENSMUST00000037739; ENSMUSP00000047119; ENSMUSG00000042354.
DR   GeneID; 30877; -.
DR   KEGG; mmu:30877; -.
DR   NMPDR; fig|10090.3.peg.28757; -.
DR   UCSC; uc007swi.1; mouse.
DR   CTD; 30877; -.
DR   MGI; MGI:1353651; Gnl3.
DR   GeneTree; ENSGT00550000074731; -.
DR   HOGENOM; HBG397932; -.
DR   HOVERGEN; HBG051747; -.
DR   InParanoid; Q8CI11; -.
DR   OMA; CQELKKV; -.
DR   OrthoDB; EOG4D26Q4; -.
DR   PhylomeDB; Q8CI11; -.
DR   NextBio; 307286; -.
DR   ArrayExpress; Q8CI11; -.
DR   Bgee; Q8CI11; -.
DR   Genevestigator; Q8CI11; -.
DR   GermOnline; ENSMUSG00000042354; Mus musculus.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0042127; P:regulation of cell proliferation; ISS:UniProtKB.
DR   InterPro; IPR014813; GN3L_Grn1.
DR   InterPro; IPR023179; GTP-bd_ortho_bundle.
DR   Gene3D; G3DSA:1.10.1580.10; GTP-bd_ortho_bundle; 1.
DR   Pfam; PF08701; GN3L_Grn1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; GTP-binding;
KW   Nucleotide-binding; Nucleus; Phosphoprotein.
FT   CHAIN         1    538       Guanine nucleotide-binding protein-like
FT                                3.
FT                                /FTId=PRO_0000122445.
FT   NP_BIND     176    179       GTP (Potential).
FT   NP_BIND     256    263       GTP (Potential).
FT   NP_BIND     300    303       GTP (Potential).
FT   REGION        2     46       Basic (By similarity).
FT   REGION      277    451       Intermediate (By similarity).
FT   REGION      460    532       Acidic (By similarity).
FT   COILED       54     95       Potential.
FT   MOD_RES      79     79       N6-acetyllysine (By similarity).
FT   MOD_RES     505    505       Phosphoserine.
FT   MOD_RES     518    518       Phosphoserine (By similarity).
FT   VAR_SEQ     465    497       Missing (in isoform 2).
FT                                /FTId=VSP_013412.
FT   CONFLICT    470    470       R -> S (in Ref. 1; AAO19472).
FT   CONFLICT    475    475       K -> Q (in Ref. 1; AAO19472).
SQ   SEQUENCE   538 AA;  60786 MW;  C092AD5305E5D69F CRC64;
     MKRPKLKKAS KRMTCHKRYK IQKKVREHHR KLRKEAKKRG HKKPRKDPGV PNSAPFKEAL
     LREAELRKQQ LEELKQQQKL DRQKEQERKR KLEVSPGDEQ SNVETREESD EPKRKKAKAG
     KQNPKKLHCQ ELKKVIEASD IVLEVLDARD PLGCRCPQIE EAVIQSGSKK LILVLNKSDL
     VPKENLENWL NYLNKELPTV VFKASTNLKN RKTFKIKKKK VVPFQSKICC GKEALWKLLG
     DFQQSCGKDI QVGVIGFPNV GKSSVINSLK QEWICNVGIS MGLTRSMQIV PLDKQITIID
     SPCLIISPCN SPTALALRSP ASIEELRPLE AASAILSQAD NEQVVLKYTV PEYKDSLHFF
     TKLAQRRGLH QKGGSPNVES AAKLVWSEWT GASLGYYCHP PASWNHSLHF NENIAAVMKK
     GFNLEELEKN NAHSIQVLKG PHLTNRILFR SSGLTNGILD EKDIVEESPR QTEDKQDADD
     QENGSGERNA EISDVAPVEE TRELSPEQST AGKPSDGSSA LDRASQEDET YDFTTDYI
//
ID   BAG5_MOUSE              Reviewed;         447 AA.
AC   Q8CI32; Q3TVA8; Q8K175; Q9DAU0;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=BAG family molecular chaperone regulator 5;
DE            Short=BAG-5;
DE   AltName: Full=Bcl-2-associated athanogene 5;
GN   Name=Bag5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Placenta, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   STRUCTURE BY NMR OF 1-86.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the first murine BAG domain of BCL2-associated
RT   athanogene 5.";
RL   Submitted (AUG-2004) to the PDB data bank.
CC   -!- FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by
CC       promoting substrate release. Inhibits both auto-ubiquitination of
CC       PARK2 and ubiquitination of target proteins by PARK2 (By
CC       similarity).
CC   -!- SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones. Binds
CC       PARK2 (By similarity).
CC   -!- SIMILARITY: Contains 4 BAG domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH27827.1; Type=Erroneous initiation;
CC       Sequence=BAB24105.1; Type=Frameshift; Positions=5, 8, 16, 34, 40, 42, 44, 54, 56, 64;
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DR   EMBL; AK005534; BAB24105.1; ALT_FRAME; mRNA.
DR   EMBL; AK160246; BAE35711.1; -; mRNA.
DR   EMBL; BC027827; AAH27827.1; ALT_INIT; mRNA.
DR   EMBL; BC037642; AAH37642.1; -; mRNA.
DR   IPI; IPI00229727; -.
DR   RefSeq; NP_081680.1; NM_027404.2.
DR   UniGene; Mm.44239; -.
DR   PDB; 1UGO; NMR; -; A=1-86.
DR   PDBsum; 1UGO; -.
DR   ProteinModelPortal; Q8CI32; -.
DR   SMR; Q8CI32; 1-89, 177-259, 276-447.
DR   STRING; Q8CI32; -.
DR   PhosphoSite; Q8CI32; -.
DR   PRIDE; Q8CI32; -.
DR   Ensembl; ENSMUST00000054636; ENSMUSP00000051049; ENSMUSG00000049792.
DR   GeneID; 70369; -.
DR   KEGG; mmu:70369; -.
DR   UCSC; uc007pdr.1; mouse.
DR   CTD; 70369; -.
DR   MGI; MGI:1917619; Bag5.
DR   eggNOG; maNOG04232; -.
DR   GeneTree; ENSGT00530000063256; -.
DR   HOGENOM; HBG713028; -.
DR   HOVERGEN; HBG004810; -.
DR   InParanoid; Q8CI32; -.
DR   OMA; YIRLEEL; -.
DR   OrthoDB; EOG46T31D; -.
DR   PhylomeDB; Q8CI32; -.
DR   NextBio; 331467; -.
DR   ArrayExpress; Q8CI32; -.
DR   Bgee; Q8CI32; -.
DR   CleanEx; MM_BAG5; -.
DR   Genevestigator; Q8CI32; -.
DR   GermOnline; ENSMUSG00000049792; Mus musculus.
DR   GO; GO:0016234; C:inclusion body; ISS:BHF-UCL.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:BHF-UCL.
DR   GO; GO:0051087; F:chaperone binding; ISS:BHF-UCL.
DR   GO; GO:0006915; P:apoptosis; IEA:InterPro.
DR   GO; GO:0061084; P:negative regulation of protein refolding; ISS:BHF-UCL.
DR   GO; GO:0051444; P:negative regulation of ubiquitin-protein ligase activity; ISS:BHF-UCL.
DR   GO; GO:0070997; P:neuron death; ISS:BHF-UCL.
DR   GO; GO:0090083; P:regulation of inclusion body assembly; ISS:BHF-UCL.
DR   InterPro; IPR003103; Apoptosis_reg_Bcl-2_prot_BAG.
DR   Pfam; PF02179; BAG; 4.
DR   SMART; SM00264; BAG; 4.
DR   PROSITE; PS51035; BAG; 4.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Chaperone; Repeat.
FT   CHAIN         1    447       BAG family molecular chaperone regulator
FT                                5.
FT                                /FTId=PRO_0000088873.
FT   DOMAIN        9     86       BAG 1.
FT   DOMAIN      182    260       BAG 2.
FT   DOMAIN      275    350       BAG 3.
FT   DOMAIN      365    442       BAG 4.
FT   MOD_RES     278    278       N6-acetyllysine (By similarity).
FT   CONFLICT      6      6       Q -> H (in Ref. 1; BAB24105).
FT   CONFLICT     23     23       I -> K (in Ref. 1; BAB24105).
FT   CONFLICT     36     36       D -> E (in Ref. 1; BAB24105).
FT   CONFLICT     52     52       E -> G (in Ref. 1; BAB24105).
FT   CONFLICT    142    142       K -> E (in Ref. 1; BAB24105).
FT   CONFLICT    148    148       A -> S (in Ref. 1; BAB24105).
FT   CONFLICT    341    341       I -> T (in Ref. 2; AAH27827).
FT   HELIX        10     22
FT   HELIX        24     28
FT   HELIX        38     55
SQ   SEQUENCE   447 AA;  50943 MW;  72E2C5472DA95416 CRC64;
     MDMGNQHPSI SRLQEIQREV KAIEPQVVGF SGLSDDKNYK RLERILTKQL FEIDSVDTEG
     KGDIQQARKR AAQETERLLK ELEQNANHPH RIEIQNIFKE AQALVKDKIV PFYSGGNCVT
     DEFEEGIQDI ILRLTHVKTG GKVSLRKARY RTLTKICAVQ EVIEDCMKKQ PSLPLSEDVH
     PSVAKINSVM CEVNKARGTL IALLMGVDSS ETCRHLSCVL SGLIADLDAL DVCGRTEIRN
     YRREVVEDIN KLLKYLDLEE EADSTHAFDL GQNHSIIKIE NVLKRMREIK NELLQAQSPP
     ELYLRAKTEL QGLIGQLDEV SLEKNPCIRE ARRRAVIEVQ ILITYLDLKE ALEKRKLFPC
     EEHPPHKAVW EILGNLSEIL GEVLSFGGNR TDKNYIRLEE LLTKQLLALD AVDPQGEEKC
     KAARKQAVKL AQNILSYLDM KSDEWEY
//
ID   STEA3_MOUSE             Reviewed;         488 AA.
AC   Q8CI59; Q3TKE4; Q80ZF3; Q8C5F0; Q924Z1;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Metalloreductase STEAP3;
DE            EC=1.16.1.-;
DE   AltName: Full=Dudulin-2;
DE   AltName: Full=Protein nm1054;
DE   AltName: Full=Six-transmembrane epithelial antigen of prostate 3;
DE   AltName: Full=Tumor suppressor-activated pathway protein 6;
GN   Name=Steap3; Synonyms=Tsap6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX   MEDLINE=22506415; PubMed=12606722; DOI=10.1073/pnas.0530298100;
RA   Passer B.J., Nancy-Portebois V., Amzallag N., Prieur S., Cans C.,
RA   Roborel de Climens A., Fiucci G., Bouvard V., Tuynder M., Susini L.,
RA   Morchoisne S., Crible V., Lespagnol A., Dausset J., Oren M., Amson R.,
RA   Telerman A.;
RT   "The p53-inducible TSAP6 gene product regulates apoptosis and the cell
RT   cycle and interacts with Nix and the Myt1 kinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:2284-2289(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Serru V., Lamblin D., Lenoir C., Manivet P., Vaubourdolle M.,
RA   Kellermann O., Loric S.;
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP   HEME-BINDING, COFACTOR, TISSUE SPECIFICITY, AND MUTAGENESIS OF HIS-316
RP   AND HIS-409.
RX   PubMed=16227996; DOI=10.1038/ng1658;
RA   Ohgami R.S., Campagna D.R., Greer E.L., Antiochos B., McDonald A.,
RA   Chen J., Sharp J.J., Fujiwara Y., Barker J.E., Fleming M.D.;
RT   "Identification of a ferrireductase required for efficient
RT   transferrin-dependent iron uptake in erythroid cells.";
RL   Nat. Genet. 37:1264-1269(2005).
RN   [6]
RP   FUNCTION.
RX   PubMed=16609065; DOI=10.1182/blood-2006-02-003681;
RA   Ohgami R.S., Campagna D.R., McDonald A., Fleming M.D.;
RT   "The Steap proteins are metalloreductases.";
RL   Blood 108:1388-1394(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-20, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-20, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Endosomal ferrireductase required for efficient
CC       transferrin-dependent iron uptake in erythroid cells. Participates
CC       in erythroid iron homeostasis by reducing Fe(3+) to Fe(2+). Also
CC       mediates reduction of Cu(2+) to Cu(1+), suggesting that it
CC       participates in copper homeostasis. Uses NAD(+) as acceptor. May
CC       play a role downstream of p53/TP53 to interface apoptosis and cell
CC       cycle progression. Indirectly involved in exosome secretion by
CC       facilitating the secretion of proteins such as TCTP.
CC   -!- COFACTOR: FAD (Probable).
CC   -!- SUBUNIT: Interacts with BNIP3L, MYT1 and TCTP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endosome membrane; Multi-pass membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CI59-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CI59-2; Sequence=VSP_024832;
CC   -!- TISSUE SPECIFICITY: Highly expressed in fetal liver (the site of
CC       midgestational hematopoiesis).
CC   -!- DISRUPTION PHENOTYPE: Mice display iron deficiency anemia, due to
CC       a defect in iron release through the transferrin cycle.
CC   -!- SIMILARITY: Belongs to the STEAP family.
CC   -!- SIMILARITY: Contains 1 ferric oxidoreductase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK50539.1; Type=Frameshift; Positions=171, 173, 479;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY214462; AAO38239.1; -; mRNA.
DR   EMBL; AY029586; AAK50539.1; ALT_FRAME; mRNA.
DR   EMBL; AK078769; BAC37383.1; -; mRNA.
DR   EMBL; AK167028; BAE39201.1; -; mRNA.
DR   EMBL; AK171237; BAE42333.1; -; mRNA.
DR   EMBL; BC037435; AAH37435.1; -; mRNA.
DR   IPI; IPI00126245; -.
DR   IPI; IPI00330941; -.
DR   RefSeq; NP_001078878.1; NM_001085409.1.
DR   RefSeq; NP_573449.2; NM_133186.3.
DR   UniGene; Mm.181033; -.
DR   ProteinModelPortal; Q8CI59; -.
DR   SMR; Q8CI59; 29-209.
DR   STRING; Q8CI59; -.
DR   PhosphoSite; Q8CI59; -.
DR   PRIDE; Q8CI59; -.
DR   Ensembl; ENSMUST00000051660; ENSMUSP00000056248; ENSMUSG00000026389.
DR   Ensembl; ENSMUST00000112639; ENSMUSP00000108258; ENSMUSG00000026389.
DR   Ensembl; ENSMUST00000112640; ENSMUSP00000108259; ENSMUSG00000026389.
DR   Ensembl; ENSMUST00000112641; ENSMUSP00000108260; ENSMUSG00000026389.
DR   Ensembl; ENSMUST00000112643; ENSMUSP00000108262; ENSMUSG00000026389.
DR   GeneID; 68428; -.
DR   KEGG; mmu:68428; -.
DR   CTD; 68428; -.
DR   MGI; MGI:1915678; Steap3.
DR   eggNOG; roNOG10887; -.
DR   GeneTree; ENSGT00390000008042; -.
DR   HOGENOM; HBG447106; -.
DR   HOVERGEN; HBG054379; -.
DR   InParanoid; Q8CI59; -.
DR   OrthoDB; EOG412M5Q; -.
DR   NextBio; 327158; -.
DR   ArrayExpress; Q8CI59; -.
DR   Bgee; Q8CI59; -.
DR   CleanEx; MM_STEAP3; -.
DR   Genevestigator; Q8CI59; -.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0000293; F:ferric-chelate reductase activity; IDA:MGI.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006826; P:iron ion transport; IMP:MGI.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR013130; Flavoprotein_TM.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR004455; NADP_OxRdtase_F420.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF03807; F420_oxidored; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Cell cycle; Copper; Endosome; FAD;
KW   Flavoprotein; Glycoprotein; Ion transport; Iron; Iron transport;
KW   Membrane; Metal-binding; NAD; Oxidoreductase; Phosphoprotein;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    488       Metalloreductase STEAP3.
FT                                /FTId=PRO_0000285172.
FT   TOPO_DOM      1    207       Cytoplasmic (Potential).
FT   TRANSMEM    208    228       Helical; (Potential).
FT   TOPO_DOM    229    258       Vesicular (Potential).
FT   TRANSMEM    259    279       Helical; (Potential).
FT   TOPO_DOM    280    304       Cytoplasmic (Potential).
FT   TRANSMEM    305    325       Helical; (Potential).
FT   TOPO_DOM    326    358       Vesicular (Potential).
FT   TRANSMEM    359    379       Helical; (Potential).
FT   TOPO_DOM    380    390       Cytoplasmic (Potential).
FT   TRANSMEM    391    411       Helical; (Potential).
FT   TOPO_DOM    412    433       Vesicular (Potential).
FT   TRANSMEM    434    454       Helical; (Potential).
FT   TOPO_DOM    455    488       Cytoplasmic (Potential).
FT   DOMAIN      259    407       Ferric oxidoreductase.
FT   METAL       316    316       Iron (heme axial ligand) (Probable).
FT   METAL       409    409       Iron (heme axial ligand) (Probable).
FT   MOD_RES      17     17       Phosphoserine.
FT   MOD_RES      20     20       Phosphoserine.
FT   CARBOHYD    256    256       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1      1       M -> MAAEAHRQQGSCPTIPSEGCGKSPEKKGSAADSRPG
FT                                TAM (in isoform 2).
FT                                /FTId=VSP_024832.
FT   MUTAGEN     316    316       H->L: Loss of function.
FT   MUTAGEN     409    409       H->L: Loss of function.
FT   CONFLICT     81     81       V -> M (in Ref. 3; BAC37383).
FT   CONFLICT    157    157       G -> V (in Ref. 2; AAK50539).
FT   CONFLICT    169    172       SDQP -> GNQQ (in Ref. 2; AAK50539).
FT   CONFLICT    176    179       RTIS -> QRVM (in Ref. 2; AAK50539).
FT   CONFLICT    212    212       W -> G (in Ref. 2; AAK50539).
FT   CONFLICT    350    350       V -> A (in Ref. 3; BAC37383/BAE39201).
FT   CONFLICT    455    455       S -> N (in Ref. 3; BAC37383/BAE39201).
SQ   SEQUENCE   488 AA;  54749 MW;  9A08D99C90CF83F4 CRC64;
     MSGEMDKPLI SRRLVDSDGS LAEVPKEAPK VGILGSGDFA RSLATRLVGS GFSVVVGSRN
     PKRTAGLFPS LAQVTFQEEA VSSPEVIFVA VFREHYSSLC SLADQLAGKI LVDVSNPTEK
     EHLQHRQSNA EYLASLFPAC TVVKAFNVIS AWALQAGPRD GNRQVLICSD QPEAKRTISE
     MARAMGFTPL DMGSLASARE VEAIPLRLLP SWKVPTLLAL GLFVCFYTYN FIRDVLQPYI
     RKDENKFYKM PLSVVNTTLP CVAYVLLSLV YLPGVLAAAL QLRRGTKYQR FPDWLDHWLQ
     HRKQIGLLSF FFAMLHALYS FCLPLRRSHR YDLVNLAVKQ VLANKSRLWV EEEVWRMEIY
     LSLGVLALGM LSLLAVTSLP SIANSLNWKE FSFVQSTLGF VALILSTMHT LTYGWTRAFE
     ENHYKFYLPP TFTLTLLLPC VIILAKGLFL LPCLSRRLTK IRRGWEKDGA VKFMLPGDHT
     QGEKTSHV
//
ID   CC132_MOUSE             Reviewed;         964 AA.
AC   Q8CI71; Q6ZPG9; Q7TSR5; Q80XR1; Q8C6D0; Q8C9I6; Q99LN1;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 2.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Coiled-coil domain-containing protein 132;
DE   AltName: Full=Bcl2-like protein blm;
GN   Name=Ccdc132; Synonyms=Kiaa1861;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RA   Huang H.-Y., Chen S.-Y., Tseng Y.-H., Huang P.-H., Hsu S.-M.;
RT   "Identification and characterization of novel members of the bcl-2
RT   family -- blm, expressed specifically in developing embryos.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Thymus, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, Czech II, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559; SER-561 AND
RP   SER-595, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8CI71-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CI71-2; Sequence=VSP_028661, VSP_028662;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8CI71-3; Sequence=VSP_028660, VSP_028663;
CC         Note=No experimental confirmation available;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH02304.1; Type=Erroneous initiation;
CC       Sequence=BAC98268.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AY254697; AAO84056.1; -; mRNA.
DR   EMBL; AK129458; BAC98268.1; ALT_INIT; mRNA.
DR   EMBL; AK042031; BAC31137.1; -; mRNA.
DR   EMBL; AK075898; BAC36038.1; -; mRNA.
DR   EMBL; BC002304; AAH02304.1; ALT_INIT; mRNA.
DR   EMBL; BC036294; AAH36294.2; -; mRNA.
DR   EMBL; BC043092; AAH43092.1; -; mRNA.
DR   IPI; IPI00621085; -.
DR   IPI; IPI00869359; -.
DR   IPI; IPI00869473; -.
DR   RefSeq; NP_001161222.1; NM_001167750.1.
DR   RefSeq; NP_001161223.1; NM_001167751.1.
DR   RefSeq; NP_077222.4; NM_024260.5.
DR   UniGene; Mm.45539; -.
DR   PhosphoSite; Q8CI71; -.
DR   PRIDE; Q8CI71; -.
DR   Ensembl; ENSMUST00000001412; ENSMUSP00000001412; ENSMUSG00000001376.
DR   GeneID; 73288; -.
DR   KEGG; mmu:73288; -.
DR   UCSC; uc009avc.1; mouse.
DR   CTD; 73288; -.
DR   MGI; MGI:1920538; Ccdc132.
DR   HOVERGEN; HBG075377; -.
DR   InParanoid; Q8CI71; -.
DR   OMA; HDNEDTT; -.
DR   OrthoDB; EOG444KJM; -.
DR   PhylomeDB; Q8CI71; -.
DR   NextBio; 337857; -.
DR   ArrayExpress; Q8CI71; -.
DR   Bgee; Q8CI71; -.
DR   CleanEx; MM_CCDC132; -.
DR   Genevestigator; Q8CI71; -.
DR   InterPro; IPR019514; DUF2451_C.
DR   InterPro; IPR019515; Vacuolar_sorting-assoc_54.
DR   Pfam; PF10475; DUF2450; 1.
DR   Pfam; PF10474; DUF2451; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Phosphoprotein.
FT   CHAIN         1    964       Coiled-coil domain-containing protein
FT                                132.
FT                                /FTId=PRO_0000307266.
FT   COILED       81    107       Potential.
FT   COILED      216    244       Potential.
FT   MOD_RES      15     15       Phosphoserine (By similarity).
FT   MOD_RES     492    492       Phosphoserine (By similarity).
FT   MOD_RES     494    494       Phosphoserine (By similarity).
FT   MOD_RES     496    496       Phosphoserine (By similarity).
FT   MOD_RES     498    498       Phosphoserine (By similarity).
FT   MOD_RES     546    546       Phosphoserine (By similarity).
FT   MOD_RES     557    557       Phosphotyrosine (By similarity).
FT   MOD_RES     559    559       Phosphoserine.
FT   MOD_RES     561    561       Phosphoserine.
FT   MOD_RES     595    595       Phosphoserine.
FT   VAR_SEQ     926    938       EYSTKQLTNLVNV -> VRTRVGVLILSGV (in
FT                                isoform 3).
FT                                /FTId=VSP_028660.
FT   VAR_SEQ     926    929       EYST -> IFSV (in isoform 2).
FT                                /FTId=VSP_028661.
FT   VAR_SEQ     930    964       Missing (in isoform 2).
FT                                /FTId=VSP_028662.
FT   VAR_SEQ     939    964       Missing (in isoform 3).
FT                                /FTId=VSP_028663.
FT   CONFLICT     77     78       LP -> PS (in Ref. 3; BAC31137).
FT   CONFLICT     89     96       YRDKLKQQ -> SRYQFKQH (in Ref. 3;
FT                                BAC31137).
FT   CONFLICT    160    160       N -> Y (in Ref. 3; BAC31137).
FT   CONFLICT    429    429       F -> S (in Ref. 3; BAC36038).
FT   CONFLICT    511    511       V -> M (in Ref. 4; AAH02304).
SQ   SEQUENCE   964 AA;  111174 MW;  F88C364742914D0E CRC64;
     MQKIKSLMTR QGLKSPPESL NDLGAFESLR VPGKEEFREL REQPSDPQAE QELINSIEQV
     YFSADPFDIV KYELEKLPPV LNLQELEEYR DKLKQQQSAV SKKVADLILE KQPAYVKELE
     RVTSLQTGLQ LAAVICTNGR RHLNIAKEGF TQASLGLLAN QRKRQLLIGL LKSLRTIKTL
     QRTDIRLSEM LEEEDYPGAI QLCLECQKAA STFKHYSCIS ELNSKLQDTL EQIEEQLDVA
     LSKICKNFDI NHYTKVQQAY RLLGKTQTAM DQLHMHFTQA IHNTVFQVVL GYVELCAGNT
     DTKFQKLQYK DLCTHVTPDS YIPCLADLCK ALWEVMLSYY RTMEWHEKHD NEETAAAAEG
     SNVMSTEEAT FDRGYVKKKL EHGLTRIWQD VQLKVKTYLL GTDLSIFKYD DFIFVLDIVS
     RLMQVGEEFC GSKSEVLQES IRKQSVNYFK NHHRIRLDEL RMFLENETWE LCPVKSNFSI
     LQLHEFKFLE QSRSPSVSPS KQPSATSSKP VTLFEQYCSG GNPFEIQADH KDEETEDVLA
     SNGYESDEQE KSAYQDYDSD SDVPEELKRD YVDEQTGDVP VKSVSRETLK SRKKSDYSLN
     KVNAPILTNT TLNVIRLVGK YMQMMNILKP IAFDVIHFMS QLFDYYLYAI YTFFGRNDSL
     ESTGLGLSSS RLKTTLNRIQ ESLIDLEGSA DPTATLTAAE ERKEKVPSPH LNQLVILTSG
     DTLYGLAERV VATESLVFLA EQFEFLQPHL DAVMPAVKKP FLQQFYSQTV STASELRKPI
     YWIVAGKAID YEQMLLLMMN VKWDVKEIMS QHNIYVDALL KEFEQFNKRL NEVSKRVRIP
     LPVSNILWEH CIRLANRTIV EGYANVKKCS NEGRALMQLD FQQFLMKLEK LTDIRPIPDK
     EFVETYIKAY YLTENDMERW IKEHREYSTK QLTNLVNVCL GSHINKKARQ KLLAAIDEID
     RPKR
//
ID   DI3L2_MOUSE             Reviewed;         870 AA.
AC   Q8CI75; Q8BMG9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=DIS3-like exonuclease 2;
DE            EC=3.1.13.-;
GN   Name=Dis3l2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Forelimb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-864, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Probable exonuclease (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CI75-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CI75-2; Sequence=VSP_030379;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the ribonuclease II (RNB) family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC27292.1; Type=Frameshift; Positions=53;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK031180; BAC27292.1; ALT_FRAME; mRNA.
DR   EMBL; BC036177; AAH36177.1; -; mRNA.
DR   IPI; IPI00229771; -.
DR   IPI; IPI00881442; -.
DR   RefSeq; NP_001165628.1; NM_001172157.1.
DR   RefSeq; NP_705758.1; NM_153530.2.
DR   UniGene; Mm.389152; -.
DR   ProteinModelPortal; Q8CI75; -.
DR   SMR; Q8CI75; 45-855.
DR   STRING; Q8CI75; -.
DR   PhosphoSite; Q8CI75; -.
DR   PRIDE; Q8CI75; -.
DR   Ensembl; ENSMUST00000065694; ENSMUSP00000070506; ENSMUSG00000053333.
DR   GeneID; 208718; -.
DR   KEGG; mmu:208718; -.
DR   UCSC; uc007bvu.1; mouse.
DR   CTD; 208718; -.
DR   MGI; MGI:2442555; Dis3l2.
DR   GeneTree; ENSGT00530000063106; -.
DR   HOGENOM; HBG382785; -.
DR   HOVERGEN; HBG107810; -.
DR   InParanoid; Q8CI75; -.
DR   OMA; KECIFTI; -.
DR   OrthoDB; EOG415GCR; -.
DR   PhylomeDB; Q8CI75; -.
DR   NextBio; 372395; -.
DR   ArrayExpress; Q8CI75; -.
DR   Bgee; Q8CI75; -.
DR   Genevestigator; Q8CI75; -.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR001900; RNase_II/R.
DR   InterPro; IPR022966; RNase_II/R_CS.
DR   Pfam; PF00773; RNB; 1.
DR   SMART; SM00955; RNB; 1.
DR   PROSITE; PS01175; RIBONUCLEASE_II; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Exonuclease; Hydrolase; Nuclease;
KW   Phosphoprotein; RNA-binding.
FT   CHAIN         1    870       DIS3-like exonuclease 2.
FT                                /FTId=PRO_0000314818.
FT   MOD_RES     192    192       Phosphoserine.
FT   MOD_RES     250    250       N6-acetyllysine (By similarity).
FT   MOD_RES     660    660       Phosphothreonine (By similarity).
FT   MOD_RES     864    864       Phosphoserine.
FT   VAR_SEQ     122    122       K -> KPRITLSLPGVLGLQ (in isoform 2).
FT                                /FTId=VSP_030379.
SQ   SEQUENCE   870 AA;  97775 MW;  E54474450DCD363F CRC64;
     MNHPDYKLNL RSPGTPRGVS SVVGPSAVGA SPGDKKSKNK SMRGKKKSIF ETYMSKEDVS
     EGLKRGTLIQ GVLRINPKKF HEAFIPSPDG DRDIFIDGVV ARNRALNGDL VVVKLLPEDQ
     WKAVKPESND KEIEATYEAD IPEEGCGHHP LQQSRKGWSG PDVIIEAQFD DSDSEDRHGN
     TSGLVDGVKK LSISTPDRGK EDSSTPVMKD ENTPIPQDTR GLSEKSLQKS AKVVYILEKK
     HSRAATGILK LLADKNSDLF KKYALFSPSD HRVPRIYVPL KDCPQDFMTR PKDFANTLFI
     CRIIDWKEDC NFALGQLAKS LGQAGEIEPE TEGILTEYGV DFSDFSSEVL ECLPQSLPWT
     IPPDEVGKRR DLRKDCIFTI DPSTARDLDD ALACRRLTDG TFEVGVHIAD VSYFVPEGSS
     LDKVAAERAT SVYLVQKVVP MLPRLLCEEL CSLNPMTDKL TFSVIWKLTP EGKILEEWFG
     RTIIRSCTKL SYDHAQSMIE NPTEKIPEEE LPPISPEHSV EEVHQAVLNL HSIAKQLRRQ
     RFVDGALRLD QLKLAFTLDH ETGLPQGCHI YEYRDSNKLV EEFMLLANMA VAHKIFRTFP
     EQALLRRHPP PQTKMLSDLV EFCDQMGLPM DVSSAGALNK SLTKTFGDDK YSLARKEVLT
     NMYSRPMQMA LYFCSGMLQD QEQFRHYALN VPLYTHFTSP IRRFADVIVH RLLAAALGYS
     EQPDVEPDTL QKQADHCNDR RMASKRVQEL SIGLFFAVLV KESGPLESEA MVMGVLNQAF
     DVLVLRFGVQ KRIYCNALAL RSYSFQKVGK KPELTLVWEP DDLEEEPTQQ VITIFSLVDV
     VLQAEATALK YSAILKRPGL EKASDEEPED
//
ID   PYGB_MOUSE              Reviewed;         843 AA.
AC   Q8CI94; Q8K283;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Glycogen phosphorylase, brain form;
DE            EC=2.4.1.1;
GN   Name=Pygb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-197 AND TYR-473, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Phosphorylase is an important allosteric enzyme in
CC       carbohydrate metabolism. Enzymes from different sources differ in
CC       their regulatory mechanisms and in their natural substrates.
CC       However, all known phosphorylases share catalytic and structural
CC       properties (By similarity).
CC   -!- CATALYTIC ACTIVITY: (1,4-alpha-D-glucosyl)(n) + phosphate = (1,4-
CC       alpha-D-glucosyl)(n-1) + alpha-D-glucose 1-phosphate.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- ENZYME REGULATION: Activity of phosphorylase is controlled both by
CC       allosteric means (through the noncovalent binding of metabolites)
CC       and by covalent modification. Thus AMP allosterically activates,
CC       whereas ATP, ADP, and glucose-6-phosphate allosterically inhibit,
CC       phosphorylase B (By similarity).
CC   -!- SUBUNIT: Homodimer. Dimers associate into a tetramer to form the
CC       enzymatically active phosphorylase A (By similarity).
CC   -!- PTM: Phosphorylation of Ser-15 converts phosphorylase B
CC       (unphosphorylated) to phosphorylase A (By similarity).
CC   -!- SIMILARITY: Belongs to the glycogen phosphorylase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH32209.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC032209; AAH32209.1; ALT_INIT; mRNA.
DR   EMBL; BC035283; AAH35283.1; -; mRNA.
DR   IPI; IPI00229796; -.
DR   RefSeq; NP_722476.1; NM_153781.1.
DR   UniGene; Mm.222584; -.
DR   ProteinModelPortal; Q8CI94; -.
DR   SMR; Q8CI94; 14-839.
DR   STRING; Q8CI94; -.
DR   CAZy; GT35; Glycosyltransferase Family 35.
DR   PhosphoSite; Q8CI94; -.
DR   PRIDE; Q8CI94; -.
DR   Ensembl; ENSMUST00000045441; ENSMUSP00000035743; ENSMUSG00000033059.
DR   GeneID; 110078; -.
DR   KEGG; mmu:110078; -.
DR   NMPDR; fig|10090.3.peg.7118; -.
DR   UCSC; uc008mul.1; mouse.
DR   CTD; 110078; -.
DR   MGI; MGI:97828; Pygb.
DR   GeneTree; ENSGT00390000016886; -.
DR   HOGENOM; HBG444050; -.
DR   HOVERGEN; HBG006848; -.
DR   InParanoid; Q8CI94; -.
DR   OMA; ETWPVEM; -.
DR   OrthoDB; EOG4S1T6F; -.
DR   PhylomeDB; Q8CI94; -.
DR   BRENDA; 2.4.1.1; 244.
DR   NextBio; 363279; -.
DR   ArrayExpress; Q8CI94; -.
DR   Bgee; Q8CI94; -.
DR   CleanEx; MM_PYGB; -.
DR   Genevestigator; Q8CI94; -.
DR   GermOnline; ENSMUSG00000033059; Mus musculus.
DR   GO; GO:0004645; F:phosphorylase activity; IEA:EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   InterPro; IPR011833; Glycg_phsphrylas.
DR   InterPro; IPR000811; Glyco_trans_35.
DR   PANTHER; PTHR11468; Glyco_trans_35; 1.
DR   Pfam; PF00343; Phosphorylase; 1.
DR   PIRSF; PIRSF000460; Pprylas_GlgP; 1.
DR   TIGRFAMs; TIGR02093; P_ylase; 1.
DR   PROSITE; PS00102; PHOSPHORYLASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Allosteric enzyme; Carbohydrate metabolism;
KW   Glycogen metabolism; Glycosyltransferase; Phosphoprotein;
KW   Pyridoxal phosphate; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    843       Glycogen phosphorylase, brain form.
FT                                /FTId=PRO_0000188536.
FT   BINDING      76     76       AMP (By similarity).
FT   SITE        109    109       Involved in the association of subunits
FT                                (By similarity).
FT   SITE        143    143       Involved in the association of subunits
FT                                (By similarity).
FT   SITE        156    156       May be involved in allosteric control (By
FT                                similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      15     15       Phosphoserine; by PHK; in form
FT                                phosphorylase A (By similarity).
FT   MOD_RES      76     76       Phosphotyrosine (By similarity).
FT   MOD_RES     197    197       Phosphotyrosine.
FT   MOD_RES     473    473       Phosphotyrosine.
FT   MOD_RES     681    681       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   843 AA;  96730 MW;  AF9F499FBB5B8B0C CRC64;
     MAKPLTDSER QKQISVRGIA GLGDVAEVRK SFNRHLHFTL VKDRNVATPR DYFFALAHTV
     RDHLVGRWIR TQQHYYERDP KRIYYLSLEF YMGRTLQNTM VNLGLQTACD EATYQLGLDL
     EELEEIEEDA GLGNGGLGRL AACFLDSMAT LGLAAYGYGI RYEFGIFNQK IVNGWQVEEA
     DDWLRYGNPW EKARPEYMLP VHFYGRVEHT PDGVLWLDTQ VVLAMPYDTP VPGYKNNTVN
     TMRLWSAKAP NDFKLKDFNV GDYIEAVLDR NLAENISRVL YPNDNFFEGK ELRLKQEYFV
     VAATLQDIIR RFKSSRFGCR DPVRTCFETF PDKVAIQLND THPALSIPEL MRILVDVEKV
     DWDKAWEITK KTCAYTNHTV LPEALERWPV SMFEKLLPRH LEIIYAINQR HLDHVAALFP
     GDVDRLRRMS VIEEGDCKRI NMAHLCVIGS HAVNGVARIH SEIVKQSVFK DFYELEPEKF
     QNKTNGITPR RWLLLCNPGL AEIIVERIGE GFLTDLSQLK KLLSLVDDEA FIRDVAKVKQ
     ENKLKFSAQL EKEYKVKINP ASMFDVHVKR IHEYKRQLLN CLHIITLYNR IKKDPAKAFV
     PRTVMIGGKA APGYHMAKMI IKLVTSIGDV VNHDPVVGDR LRVIFLENYR VSLAEKVIPA
     ADLSQQISTA GTEASGTGNM KFMLNGALTI GTMDGANVEM AEEAGEENLF IFGMRVEDVE
     ALDQKGYNAR EFYERLPELR QAVDQISSGF FSPKDPDCFK DVVNMLMYHD RFKVFADYEA
     YIQCQAQVDR LYRNSKEWTK KVIRNIACSG KFSSDRTITE YAREIWGVEP SDLQIPPPNL
     PKD
//
ID   OSB11_MOUSE             Reviewed;         751 AA.
AC   Q8CI95;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Oxysterol-binding protein-related protein 11;
DE            Short=ORP-11;
DE            Short=OSBP-related protein 11;
GN   Name=Osbpl11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-15; SER-177;
RP   SER-179; SER-182; SER-186; SER-189 AND SER-194, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- SIMILARITY: Belongs to the OSBP family.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH35278.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC035278; AAH35278.1; ALT_INIT; mRNA.
DR   IPI; IPI00918049; -.
DR   UniGene; Mm.26564; -.
DR   ProteinModelPortal; Q8CI95; -.
DR   SMR; Q8CI95; 64-170, 376-732.
DR   PhosphoSite; Q8CI95; -.
DR   PRIDE; Q8CI95; -.
DR   Ensembl; ENSMUST00000039733; ENSMUSP00000039632; ENSMUSG00000022807.
DR   UCSC; uc007yzy.1; mouse.
DR   MGI; MGI:2146553; Osbpl11.
DR   eggNOG; roNOG08845; -.
DR   GeneTree; ENSGT00550000074515; -.
DR   HOGENOM; HBG444510; -.
DR   HOVERGEN; HBG053376; -.
DR   InParanoid; Q8CI95; -.
DR   OrthoDB; EOG4TQM8K; -.
DR   PhylomeDB; Q8CI95; -.
DR   NextBio; 358145; -.
DR   ArrayExpress; Q8CI95; -.
DR   Bgee; Q8CI95; -.
DR   CleanEx; MM_OSBPL11; -.
DR   Genevestigator; Q8CI95; -.
DR   GermOnline; ENSMUSG00000022807; Mus musculus.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0008202; P:steroid metabolic process; IEA:InterPro.
DR   InterPro; IPR000648; Oxysterol-bd.
DR   InterPro; IPR018494; Oxysterol-bd_CS.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   PANTHER; PTHR10972; Oxysterol_bd; 1.
DR   Pfam; PF01237; Oxysterol_BP; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS01013; OSBP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Lipid transport; Lipid-binding; Phosphoprotein;
KW   Transport.
FT   CHAIN         1    751       Oxysterol-binding protein-related protein
FT                                11.
FT                                /FTId=PRO_0000100382.
FT   DOMAIN       63    160       PH.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      13     13       Phosphoserine.
FT   MOD_RES      15     15       Phosphoserine.
FT   MOD_RES      27     27       Phosphothreonine (By similarity).
FT   MOD_RES     177    177       Phosphoserine.
FT   MOD_RES     179    179       Phosphoserine.
FT   MOD_RES     182    182       Phosphoserine.
FT   MOD_RES     186    186       Phosphoserine.
FT   MOD_RES     189    189       Phosphoserine.
FT   MOD_RES     194    194       Phosphoserine.
SQ   SEQUENCE   751 AA;  83629 MW;  70E5817835DC5B87 CRC64;
     MQGGEPASVM KVSESEGKLE GLATAVTPNK NSGNSSCGGA ISSSSSNSSR GGSAKGWQYS
     DHMESVNGYL MKYTNLVTGW QYRFFVLNNE AGLLEYFVNE QSRNQKPRGT LQLAGAVISP
     SDEDSHTFTV NAASGEQYKL RATDAKERQH WVSRLQICTQ HHTEAIGKNN PPLKSRSFSL
     ASSGNSPISQ RRPSQNAMSF FNVGHSKLQS VNKRAHLHPD HLVEVREMMS HAEGQQRDLI
     RRIECLPASG LLSSLDQDLL MLKATSMATM NCLNDCFHIL QLQHASHQKG ALPSGTTIEW
     LEPKIPLSNH YKNGAEQPFA TEPNKPMGAP EAQCVAESGV LAREPEDISA DDEVEDTCDN
     KEDDLGAVEE QRSVILHLLS QLKLGMDLTR VVLPTFILEK RSLLEMYADF MSHPDLFIGI
     TNGATPEDRM IRFVEYYLTS FHEGRKGAIA KKPYNPIIGE TFHCSWRMPK SEVASGVSSS
     SSTPAITDHA PLPEEAPTQS VSDCYTVRFV AEQVSHHPPV SGFYAECAER KMCVNAHVWT
     KSKFLGMSIG VTMVGEGVLC LLEHGEEYTF SLPCAYARSI LTVPWVELGG KVSVNCAKTG
     YSASITFHTK PFYGGKLHRV TAEVKYNLTN TVVCRVQGEW NSVLEFTYSN GETKFVDLAK
     LAVTKKRVRP LEKQDPFESR RLWKNVTDSL RESEIDKATE HKRSLEERQR TEERLRTETG
     TPWKTKYFIK EGDGWVYHKP LWKGIPSQPA E
//
ID   Q8CIA7_MOUSE            Unreviewed;       853 AA.
AC   Q8CIA7;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   05-OCT-2010, entry version 36.
DE   SubName: Full=Plekha5 protein;
GN   Name=Plekha5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor. C3;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC033481; AAH33481.1; -; mRNA.
DR   IPI; IPI00460678; -.
DR   UniGene; Mm.247670; -.
DR   STRING; Q8CIA7; -.
DR   PhosphoSite; Q8CIA7; -.
DR   PRIDE; Q8CIA7; -.
DR   Ensembl; ENSMUST00000032358; ENSMUSP00000032358; ENSMUSG00000030231.
DR   UCSC; uc009eod.1; mouse.
DR   MGI; MGI:1923802; Plekha5.
DR   HOVERGEN; HBG053615; -.
DR   ArrayExpress; Q8CIA7; -.
DR   Bgee; Q8CIA7; -.
DR   Genevestigator; Q8CIA7; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   853 AA;  96338 MW;  796AD44214C45ACC CRC64;
     MELWMKAMLD AALVQTEPVK RVDKITTDNA STKETNNIPN HRVLIRPEVQ NHQKNKEISK
     IEEKRALEAE RYGFQKDGQD RPLTKINSVK LNSLPSEYES GPDCPPQNVH YRPINVNSSD
     GKAVNVSLAD VRGGSHPNAG PLATEADRVI QRTNSMQQLE QWIKVQKGRG LEEEPRGVIS
     YQTLPRNMPS HRAQILARCP EGYRTLPRNS KTRPESICSV TPSGHEKTGP GAEEKRRSMR
     DDTMWQLYEW QQRQFYHKQS TLPRHGCLSS PKAMVQVSDQ TMHSIPTSPS HGSAAAYQGF
     SPQRTYRSEV TSPIQRGDVT IDRRHRPHHP KHVYVADRRS MPAGLTLQAV SPQSLQGRTL
     SQDECRGTLY KYRPEEAGID AKLSRLCEQD KVVRALEEKL QQLHKEKYTL EQALLSASQE
     IEMNADNPAA IQTVVLQRDD LQNGLLSTCR ELSRATAELE RAWREYDKLE YDVTVTRDQM
     QGQLDRLGEV QSESAGIQRA QIQKELWRIQ DVMEGLSKHK QQRGSSETVG LAGSKPFSSV
     KYKSEGPDYR LYKSEPELTT VAEVDESNGE EKSEPVSETE APVVKGSHFP VGVPLRTKSP
     TPESSTIASY VTLRKTKKMV ELRTERPRSA VEQLCLAESA RPRMTVEEQL ERIRRHQQAC
     LREKKKGLSV LGASDPSDVR DSPLRLTQTL RRDDNVKELD TVHRENDVKP DYETPAAQYA
     HLEDAEPQNA DIGRKLKRSE SIFYEMLYTP EPNGMASEEV TEKERQKEQV HADGSCSPQE
     ETAMTEHQME GPPEEAESLH EEEETLASCE PAPEIPRENQ TTVRSLSPSP DSSTAADPPT
     PPQLREGSHF MCV
//
ID   CT030_MOUSE             Reviewed;         120 AA.
AC   Q8CIB6; Q9CYF7;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=UPF0414 transmembrane protein C20orf30 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-25, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the UPF0414 family.
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DR   EMBL; AK170062; BAE41540.1; -; mRNA.
DR   EMBL; AK017729; BAB30900.1; -; mRNA.
DR   EMBL; BC033429; AAH33429.1; -; mRNA.
DR   IPI; IPI00111462; -.
DR   RefSeq; NP_001135443.1; NM_001141971.1.
DR   RefSeq; NP_081754.2; NM_027478.3.
DR   UniGene; Mm.30116; -.
DR   STRING; Q8CIB6; -.
DR   PhosphoSite; Q8CIB6; -.
DR   PRIDE; Q8CIB6; -.
DR   Ensembl; ENSMUST00000028816; ENSMUSP00000028816; ENSMUSG00000027341.
DR   Ensembl; ENSMUST00000110163; ENSMUSP00000105792; ENSMUSG00000027341.
DR   Ensembl; ENSMUST00000110164; ENSMUSP00000105793; ENSMUSG00000027341.
DR   GeneID; 70612; -.
DR   KEGG; mmu:70612; -.
DR   UCSC; uc008mmk.1; mouse.
DR   MGI; MGI:1917862; 5730494N06Rik.
DR   GeneTree; ENSGT00390000008694; -.
DR   HOGENOM; HBG715461; -.
DR   HOVERGEN; HBG054972; -.
DR   InParanoid; Q8CIB6; -.
DR   OMA; CQRVMMP; -.
DR   OrthoDB; EOG4R23WB; -.
DR   PhylomeDB; Q8CIB6; -.
DR   NextBio; 331976; -.
DR   ArrayExpress; Q8CIB6; -.
DR   Bgee; Q8CIB6; -.
DR   CleanEx; MM_5730494N06RIK; -.
DR   Genevestigator; Q8CIB6; -.
DR   GermOnline; ENSMUSG00000027341; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR008590; DUF872_TM.
DR   Pfam; PF05915; DUF872; 1.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    120       UPF0414 transmembrane protein C20orf30
FT                                homolog.
FT                                /FTId=PRO_0000233893.
FT   TRANSMEM     46     66       Helical; (Potential).
FT   TRANSMEM     79     99       Helical; (Potential).
FT   MOD_RES      24     24       Phosphoserine.
FT   MOD_RES      25     25       Phosphothreonine.
FT   CONFLICT     86     86       G -> R (in Ref. 1; BAB30900).
SQ   SEQUENCE   120 AA;  13188 MW;  5F612C2B15D31E34 CRC64;
     MMPSRTNLAT GLPSSKVKYS RLASTDDGYI DLQFKKSPPK IPYKAIALAT VLFLIGTFLI
     IIGSLLLSGY ISKGGADRAV PVLIIGILVF LPGFYHLRIA YYASKGYRGY SYDDIPDFDD
//
ID   COPA_MOUSE              Reviewed;        1224 AA.
AC   Q8CIE6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Coatomer subunit alpha;
DE   AltName: Full=Alpha-coat protein;
DE            Short=Alpha-COP;
DE   Contains:
DE     RecName: Full=Xenin;
DE     AltName: Full=Xenopsin-related peptide;
DE   Contains:
DE     RecName: Full=Proxenin;
GN   Name=Copa;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1035, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: The coatomer is a cytosolic protein complex that binds
CC       to dilysine motifs and reversibly associates with Golgi non-
CC       clathrin-coated vesicles, which further mediate biosynthetic
CC       protein transport from the ER, via the Golgi up to the trans Golgi
CC       network. Coatomer complex is required for budding from Golgi
CC       membranes, and is essential for the retrograde Golgi-to-ER
CC       transport of dilysine-tagged proteins. In mammals, the coatomer
CC       can only be recruited by membranes associated to ADP-ribosylation
CC       factors (ARFs), which are small GTP-binding proteins; the complex
CC       also influences the Golgi structural integrity, as well as the
CC       processing, activity, and endocytic recycling of LDL receptors (By
CC       similarity).
CC   -!- FUNCTION: Xenin stimulates exocrine pancreatic secretion. It
CC       inhibits pentagastrin-stimulated secretion of acid, to induce
CC       exocrine pancreatic secretion and to affect small and large
CC       intestinal motility. In the gut, xenin interacts with the
CC       neurotensin receptor (By similarity).
CC   -!- SUBUNIT: Oligomeric complex that consists of at least the alpha,
CC       beta, beta', gamma, delta, epsilon and zeta subunits. Probably
CC       interacts with PEX11A. Interacts with SCYL1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus
CC       membrane; Peripheral membrane protein; Cytoplasmic side (By
CC       similarity). Cytoplasmic vesicle, COPI-coated vesicle membrane;
CC       Peripheral membrane protein; Cytoplasmic side (By similarity).
CC       Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic
CC       side of the Golgi, as well as on the vesicles/buds originating
CC       from it (By similarity).
CC   -!- SUBCELLULAR LOCATION: Xenin: Secreted (By similarity).
CC   -!- SIMILARITY: Contains 6 WD repeats.
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DR   EMBL; BC024070; AAH24070.1; -; mRNA.
DR   EMBL; BC047429; AAH47429.1; -; mRNA.
DR   IPI; IPI00229834; -.
DR   UniGene; Mm.30041; -.
DR   HSSP; P63005; 1VYH.
DR   ProteinModelPortal; Q8CIE6; -.
DR   SMR; Q8CIE6; 1-812, 905-1224.
DR   IntAct; Q8CIE6; 14.
DR   STRING; Q8CIE6; -.
DR   PRIDE; Q8CIE6; -.
DR   Ensembl; ENSMUST00000027833; ENSMUSP00000027833; ENSMUSG00000026553.
DR   UCSC; uc007dpn.1; mouse.
DR   MGI; MGI:1334462; Copa.
DR   HOGENOM; HBG328393; -.
DR   HOVERGEN; HBG005379; -.
DR   InParanoid; Q8CIE6; -.
DR   PhylomeDB; Q8CIE6; -.
DR   ArrayExpress; Q8CIE6; -.
DR   Bgee; Q8CIE6; -.
DR   Genevestigator; Q8CIE6; -.
DR   GO; GO:0030126; C:COPI vesicle coat; IEA:InterPro.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   InterPro; IPR016391; Coatomer_alpha_subunit.
DR   InterPro; IPR010714; Coatomer_asu_C.
DR   InterPro; IPR006692; Coatomer_WD-assoc_reg.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF04053; Coatomer_WDAD; 1.
DR   Pfam; PF06957; COPI_C; 1.
DR   Pfam; PF00400; WD40; 6.
DR   PIRSF; PIRSF003354; Coatomer_alpha_subunit; 1.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 6.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport; Golgi apparatus;
KW   Hormone; Membrane; Phosphoprotein; Protein transport; Repeat;
KW   Secreted; Transport; WD repeat.
FT   CHAIN         1   1224       Coatomer subunit alpha.
FT                                /FTId=PRO_0000327496.
FT   PEPTIDE       1     35       Proxenin.
FT                                /FTId=PRO_0000327497.
FT   PEPTIDE       1     25       Xenin.
FT                                /FTId=PRO_0000327498.
FT   REPEAT        7     37       WD 1.
FT   REPEAT       49     79       WD 2.
FT   REPEAT       91    121       WD 3.
FT   REPEAT      133    163       WD 4.
FT   REPEAT      203    233       WD 5.
FT   REPEAT      247    277       WD 6.
FT   MOD_RES     173    173       Phosphoserine (By similarity).
FT   MOD_RES     249    249       Phosphotyrosine (By similarity).
FT   MOD_RES     402    402       Phosphoserine (By similarity).
FT   MOD_RES    1035   1035       Phosphoserine.
SQ   SEQUENCE   1224 AA;  138446 MW;  82DED0F2BC4AD71F CRC64;
     MLTKFETKSA RVKGLSFHPK RPWILTSLHN GVIQLWDYRM CTLIDKFDEH DGPVRGIDFH
     KQQPLFVSGG DDYKIKVWNY KLRRCLFTLL GHLDYIRTTF FHHEYPWILS ASDDQTIRVW
     NWQSRTCVCV LTGHNHYVMC AQFHPSEDLV VSASLDQTVR VWDISGLRKK NLSPGAVESD
     VRGITGVDLF GTTDAVVKHV LEGHDRGVNW AAFHPTMPLI VSGADDRQVK IWRMNESKAW
     EVDTCRGHYN NVSCAVFHPR QELILSNSED KSIRVWDMSK RTGVQTFRRD HDRFWVLAAH
     PNLNLFAAGH DGGMIVFKLE RERPAYAVHG NMLHYVKDRF LRQLDFNSSK DVAVMQLRSG
     SKFPVFNMSY NPAENAVLLC TRASNLENST YDLYTIPKDA DSQNPDAPEG KRSSGLTAVW
     VARNRFAVLD RMHSLLIKNL KNEITKKIQV PNCDEIFYAG TGNLLLRDAD SITLFDVQQK
     RTLASVKISK VKYVIWSADM SHVALLAKHA IVICNRKLDA LCNIHENIRV KSGAWDESGV
     FIYTTSNHIK YAVTTGDHGI IRTLDLPIYV TRVKGNNVYC LDRECRPRVL TIDPTEFKFK
     LALINRKYDE VLHMVRNAKL VGQSIIAYLQ KKGYPEVALH FVKDEKTRFS LALECGNIEI
     ALEAAKALDD KNCWEKLGEV ALLQGNHQIV EMCYQRTKNF DKLSFLYLIT GNLEKLRKMM
     KIAEIRKDMS GHYQNALYLG DVSERVRILK NCGQKSLAYL TAATHGLDEE AESLKETFDP
     EKETIPDIDP NAKLLQPPAP IMPLDTNWPL LTVSKGFFEG SIASKGKGGA LAADIDIDTV
     GTEGWGEDAE LQLDEDGFVE APEGLGEDVL GKGQEEGGGW DVEEDLELPP ELDVPSGVSG
     SAEDGFFVPP TKGTSPTQIW CNNSQLPVDH ILAGSFETAM RLLHDQVGVI QFGPYKQLFL
     QTYARGRTTY QALPCLPSMY SYPNRNWKDA GLKNGVPAVG LKLNDLIQRL QLCYQLTTVG
     KFEEAVEKFR SILLSVPLLV VDNKQEIAEA QQLITICREY IVGLCMEIER KKLPKETLDQ
     QKRICEMAAY FTHSNLQPVH MILVLRTALN LFFKLKNFKT AATFARRLLE LGPKPEVAQQ
     TRKILSACEK NPTDACQLNY DMHNPFDICA ASYRPIYRGK PVEKCPLSGA CYSPEFKGQI
     CRVTTVTEIG KDVIGLRISP LQFR
//
ID   CA131_MOUSE             Reviewed;         281 AA.
AC   Q8CIL4; Q3UNZ3; Q9CZF4;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=Uncharacterized protein C1orf131 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
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DR   EMBL; AK012675; BAB28401.1; -; mRNA.
DR   EMBL; AK143919; BAE25604.1; -; mRNA.
DR   EMBL; BC023675; AAH23675.1; -; mRNA.
DR   IPI; IPI00136186; -.
DR   RefSeq; NP_079891.2; NM_025615.2.
DR   UniGene; Mm.261321; -.
DR   UniGene; Mm.436864; -.
DR   ProteinModelPortal; Q8CIL4; -.
DR   PhosphoSite; Q8CIL4; -.
DR   PRIDE; Q8CIL4; -.
DR   Ensembl; ENSMUST00000034465; ENSMUSP00000034465; ENSMUSG00000031984.
DR   GeneID; 66523; -.
DR   KEGG; mmu:66523; -.
DR   UCSC; uc009nxs.1; mouse.
DR   MGI; MGI:1913773; 2810004N23Rik.
DR   HOGENOM; HBG506134; -.
DR   HOVERGEN; HBG058578; -.
DR   InParanoid; Q8CIL4; -.
DR   OMA; LREELHC; -.
DR   OrthoDB; EOG40P47X; -.
DR   PhylomeDB; Q8CIL4; -.
DR   NextBio; 321932; -.
DR   ArrayExpress; Q8CIL4; -.
DR   Bgee; Q8CIL4; -.
DR   CleanEx; MM_2810004N23RIK; -.
DR   Genevestigator; Q8CIL4; -.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein.
FT   CHAIN         1    281       Uncharacterized protein C1orf131 homolog.
FT                                /FTId=PRO_0000285030.
FT   COMPBIAS    123    242       Lys-rich.
FT   MOD_RES      67     67       Phosphoserine.
FT   MOD_RES      75     75       Phosphoserine (By similarity).
FT   MOD_RES     172    172       N6-acetyllysine (By similarity).
FT   MOD_RES     267    267       Phosphoserine (By similarity).
FT   CONFLICT      5      5       H -> T (in Ref. 1; BAB28401).
FT   CONFLICT    119    119       E -> G (in Ref. 1; BAE25604).
FT   CONFLICT    182    182       R -> Q (in Ref. 1; BAB28401).
FT   CONFLICT    251    251       G -> V (in Ref. 1; BAB28401).
SQ   SEQUENCE   281 AA;  31344 MW;  9EFAC62B06FD6FD8 CRC64;
     MAAEHDSDSV EPPGSEALLD AVLRTLYDLG ETEGETEQKR IRKKKAKKRD SETIEDVAVE
     PLPLPGSPVR GQKKSASSFF QKLREELQSA PAAPSEVPVT TAVSLSPPKN GSKLVEVVEF
     QSKSKKRKLK SDEDEPAKNK TKVVKKDVDI QEFNLEKARL EVHRFGITGY GKGKERVLER
     ERAIMLGAKP PKNTYVNYKV LQKQIKEKKI AVEEEKRAAR ETDIFKKKKK KGRGQEDRRS
     KKSAPSILSS GQVGQVGKFR NGTLILSPTD IKKINSSRVA K
//
ID   PAK2_MOUSE              Reviewed;         524 AA.
AC   Q8CIN4;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Serine/threonine-protein kinase PAK 2;
DE            EC=2.7.11.1;
DE   AltName: Full=Gamma-PAK;
DE   AltName: Full=p21-activated kinase 2;
DE            Short=PAK-2;
DE   Contains:
DE     RecName: Full=PAK-2p27;
DE   Contains:
DE     RecName: Full=PAK-2p34;
GN   Name=Pak2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=14749374; DOI=10.1128/MCB.24.4.1582-1594.2004;
RA   Huang Z., Traugh J.A., Bishop J.M.;
RT   "Negative control of the Myc protein by the stress-responsive kinase
RT   Pak2.";
RL   Mol. Cell. Biol. 24:1582-1594(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   SUBCELLULAR LOCATION, AND CLEAVAGE.
RX   PubMed=12853446; DOI=10.1074/jbc.M306494200;
RA   Jakobi R., McCarthy C.C., Koeppel M.A., Stringer D.K.;
RT   "Caspase-activated PAK-2 is regulated by subcellular targeting and
RT   proteasomal degradation.";
RL   J. Biol. Chem. 278:38675-38685(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141 AND THR-143, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   INTERACTION WITH SCRIB.
RX   PubMed=18716323; DOI=10.1093/hmg/ddn248;
RA   Nola S., Sebbagh M., Marchetto S., Osmani N., Nourry C., Audebert S.,
RA   Navarro C., Rachel R., Montcouquiol M., Sans N.,
RA   Etienne-Manneville S., Borg J.-P., Santoni M.-J.;
RT   "Scrib regulates PAK activity during the cell migration process.";
RL   Hum. Mol. Genet. 17:3552-3565(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: The activated kinase acts on a variety of targets. Full
CC       length PAK 2 stimulates cell survival and cell growth. The process
CC       is, at least in part, mediated by phosphorylation and inhibition
CC       of pro-apoptotic BAD. Caspase-activated PAK-2p34 is involved in
CC       cell death response, probably involving the JNK signaling pathway
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Activated by binding small G proteins. Binding
CC       of GTP-bound CDC42 or RAC1 to the autoregulatory region releases
CC       monomers from the autoinhibited dimer, enables phosphorylation of
CC       Thr-402 and allows the kinase domain to adopt an active structure.
CC       Following caspase cleavage, autophosphorylted PAK-2p34 is
CC       constitutively active (By similarity).
CC   -!- SUBUNIT: Interacts tightly with GTP-bound but not GDP-bound
CC       CDC42/p21 and RAC1. Interacts with SH3MD4. PAK-2p34 interacts with
CC       ARHGAP10 (By similarity). Interacts with SCRIB.
CC   -!- INTERACTION:
CC       Q01112:cdc42 (xeno); NbExp=1; IntAct=EBI-1559317, EBI-767502;
CC   -!- SUBCELLULAR LOCATION: Serine/threonine-protein kinase PAK 2:
CC       Cytoplasm.
CC   -!- SUBCELLULAR LOCATION: PAK-2p34: Nucleus (By similarity).
CC       Cytoplasm, perinuclear region (By similarity). Membrane; Lipid-
CC       anchor (By similarity). Note=Interaction with ARHGAP10 probably
CC       changes PAK-2p34 location to cytoplasmic perinuclear region (By
CC       similarity).
CC   -!- PTM: Full length PAK2 is autophosphorylated when activated by
CC       CDC42/p21. Following cleavage, both peptides, PAK-2p27 and PAK-
CC       2p34, become highly autophosphorylated. Autophosphorylation of
CC       PAK-2p27 can occur in the absence of any effectors and is
CC       dependent on phosphorylation of Thr-402, because PAK-2p27 is
CC       acting as an exogenous substrate (By similarity).
CC   -!- PTM: During apoptosis proteolytically cleaved by caspase-3 or
CC       caspase-3-like proteases to yield active PAK-2p34 (By similarity).
CC   -!- PTM: Ubiquitinated, leading to its proteosomal degradation (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC   -!- SIMILARITY: Contains 1 CRIB domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AY167030; AAN65624.1; -; mRNA.
DR   EMBL; BC086650; AAH86650.1; -; mRNA.
DR   IPI; IPI00229884; -.
DR   RefSeq; NP_796300.1; NM_177326.2.
DR   UniGene; Mm.234204; -.
DR   ProteinModelPortal; Q8CIN4; -.
DR   SMR; Q8CIN4; 69-143, 228-519.
DR   IntAct; Q8CIN4; 1.
DR   MINT; MINT-268891; -.
DR   STRING; Q8CIN4; -.
DR   PhosphoSite; Q8CIN4; -.
DR   PRIDE; Q8CIN4; -.
DR   Ensembl; ENSMUST00000023467; ENSMUSP00000023467; ENSMUSG00000022781.
DR   GeneID; 224105; -.
DR   KEGG; mmu:224105; -.
DR   UCSC; uc007yyd.1; mouse.
DR   CTD; 224105; -.
DR   MGI; MGI:1339984; Pak2.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108518; -.
DR   InParanoid; Q8CIN4; -.
DR   OMA; LANANMP; -.
DR   OrthoDB; EOG4M3988; -.
DR   PhylomeDB; Q8CIN4; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 377081; -.
DR   ArrayExpress; Q8CIN4; -.
DR   Bgee; Q8CIN4; -.
DR   CleanEx; MM_PAK2; -.
DR   Genevestigator; Q8CIN4; -.
DR   GermOnline; ENSMUSG00000022781; Mus musculus.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000095; PAK_box_Rho-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00786; PBD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00285; PBD; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Allosteric enzyme; Apoptosis; ATP-binding; Cytoplasm;
KW   Growth regulation; Kinase; Lipoprotein; Membrane; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Serine/threonine-protein kinase; Transferase;
KW   Ubl conjugation.
FT   CHAIN         1    524       Serine/threonine-protein kinase PAK 2.
FT                                /FTId=PRO_0000086466.
FT   CHAIN         1    212       PAK-2p27 (By similarity).
FT                                /FTId=PRO_0000304924.
FT   CHAIN       213    524       PAK-2p34 (By similarity).
FT                                /FTId=PRO_0000304925.
FT   DOMAIN       74     87       CRIB.
FT   DOMAIN      249    499       Protein kinase.
FT   NP_BIND     255    263       ATP (By similarity).
FT   REGION       69    137       Autoregulatory region (By similarity).
FT   REGION       69    112       GTPase-binding (By similarity).
FT   MOTIF       245    251       Nuclear localization signal (By
FT                                similarity).
FT   ACT_SITE    367    367       Proton acceptor (By similarity).
FT   BINDING     278    278       ATP (By similarity).
FT   SITE        212    213       Cleavage; by caspase-3 or caspase-3-like
FT                                proteases (By similarity).
FT   MOD_RES       2      2       Phosphoserine (By similarity).
FT   MOD_RES      38     38       N6-acetyllysine (By similarity).
FT   MOD_RES      55     55       Phosphoserine (By similarity).
FT   MOD_RES      58     58       Phosphoserine (By similarity).
FT   MOD_RES      60     60       Phosphothreonine (By similarity).
FT   MOD_RES     128    128       N6-acetyllysine (By similarity).
FT   MOD_RES     139    139       Phosphotyrosine (By similarity).
FT   MOD_RES     141    141       Phosphoserine.
FT   MOD_RES     143    143       Phosphothreonine.
FT   MOD_RES     169    169       Phosphothreonine (By similarity).
FT   MOD_RES     197    197       Phosphoserine (By similarity).
FT   MOD_RES     402    402       Phosphothreonine; by autocatalysis (By
FT                                similarity).
SQ   SEQUENCE   524 AA;  57930 MW;  D8BDA7B193D41B1B CRC64;
     MSDNGELEDK PPAPPVRMSS TIFSTGGKDP LSANHSLKPL PSVPEEKKPR NKIISIFSGT
     EKGSKKKEKE RPEISPPSDF EHTIHVGFDA VTGEFTGMPE QWARLLQTSN ITKLEQKKNP
     QAVLDVLKFY DSNTVKQKYL SFTPPEKDGF PSGTPALNTK GSETSAVVTE EDDDDEDAAP
     PVIAPRPDHT KSIYTRSVID PIPAPVGDSN VDSGAKSSDK QKKKAKMTDE EIMEKLRTIV
     SIGDPKKKYT RYEKIGQGAS GTVFTATDVA LGQEVAIKQI NLQKQPKKEL IINEILVMKE
     LKNPNIVNFL DSYLVGDELF VVMEYLAGGS LTDVVTETCM DEAQIAAVCR ECLQALEFLH
     ANQVIHRDIK SDNVLLGMEG SVKLTDFGFC AQITPEQSKR STMVGTPYWM APEVVTRKAY
     GPKVDIWSLG IMAIEMVEGE PPYLNENPLR ALYLIATNGT PELQNPEKLS PIFRDFLNRC
     LEMDVEKRGS AKELLQHPFL KLAKPLSSLT PLILAAKEAM KSNR
//
ID   MARK4_MOUSE             Reviewed;         752 AA.
AC   Q8CIP4; Q80T81;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=MAP/microtubule affinity-regulating kinase 4;
DE            EC=2.7.11.1;
GN   Name=Mark4; Synonyms=Kiaa1860;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster;
RA   Beghini A., Moroni R.F., Larizza L.;
RT   "Identification of a novel mouse gene MARK4 homologous to human
RT   MARKL1.";
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 119-752.
RC   TISSUE=Pancreatic islet;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 299-308, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- PTM: Ubiquitinated with 'Lys-29'- and 'Lys-33'-linked
CC       polyubiquitins which appear to impede LKB1-mediated
CC       phosphorylation. Deubiquitinated by USP9X (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. MARK subfamily.
CC   -!- SIMILARITY: Contains 1 KA1 (kinase-associated) domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 UBA domain.
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DR   EMBL; AY151083; AAN60072.1; -; mRNA.
DR   EMBL; AK122565; BAC65847.2; -; mRNA.
DR   IPI; IPI00229893; -.
DR   RefSeq; NP_758483.1; NM_172279.1.
DR   UniGene; Mm.260504; -.
DR   ProteinModelPortal; Q8CIP4; -.
DR   SMR; Q8CIP4; 53-369, 647-752.
DR   STRING; Q8CIP4; -.
DR   PhosphoSite; Q8CIP4; -.
DR   PRIDE; Q8CIP4; -.
DR   Ensembl; ENSMUST00000085715; ENSMUSP00000082862; ENSMUSG00000030397.
DR   GeneID; 232944; -.
DR   KEGG; mmu:232944; -.
DR   UCSC; uc009fly.1; mouse.
DR   CTD; 232944; -.
DR   MGI; MGI:1920955; Mark4.
DR   eggNOG; roNOG09909; -.
DR   GeneTree; ENSGT00600000084258; -.
DR   HOGENOM; HBG315019; -.
DR   HOVERGEN; HBG052453; -.
DR   InParanoid; Q8CIP4; -.
DR   OMA; TERPGSE; -.
DR   OrthoDB; EOG4TB49R; -.
DR   PhylomeDB; Q8CIP4; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 381357; -.
DR   ArrayExpress; Q8CIP4; -.
DR   Bgee; Q8CIP4; -.
DR   CleanEx; MM_MARK4; -.
DR   Genevestigator; Q8CIP4; -.
DR   GermOnline; ENSMUSG00000030397; Mus musculus.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043015; F:gamma-tubulin binding; ISS:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0050321; F:tau-protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR001772; Kinase-assoc_KA1.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   InterPro; IPR000449; UBA/transl_elong_EF1B_N.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   Gene3D; G3DSA:3.30.310.80; Kinase-assoc_KA1; 1.
DR   Pfam; PF02149; KA1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00627; UBA; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF103243; Kinase-assoc_KA1; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50032; KA1; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase;
KW   Ubl conjugation.
FT   CHAIN         1    752       MAP/microtubule affinity-regulating
FT                                kinase 4.
FT                                /FTId=PRO_0000086308.
FT   DOMAIN       59    310       Protein kinase.
FT   DOMAIN      324    368       UBA.
FT   DOMAIN      703    752       KA1.
FT   NP_BIND      65     73       ATP (By similarity).
FT   ACT_SITE    181    181       Proton acceptor (By similarity).
FT   BINDING      88     88       ATP (By similarity).
FT   MOD_RES       2      2       Phosphoserine (By similarity).
FT   MOD_RES      17     17       Phosphothreonine (By similarity).
FT   MOD_RES      23     23       Phosphoserine (By similarity).
FT   MOD_RES      26     26       Phosphoserine (By similarity).
FT   MOD_RES     214    214       Phosphothreonine (By similarity).
FT   MOD_RES     423    423       Phosphoserine (By similarity).
FT   MOD_RES     438    438       Phosphoserine (By similarity).
FT   MOD_RES     545    545       Phosphoserine (By similarity).
SQ   SEQUENCE   752 AA;  82644 MW;  185FDAE3F0D627DD CRC64;
     MSSRTALAPG NDRNSDTHGT LGSGRSSDKG PSWSSRSLGA RCRNSIASCP EEQPHVGNYR
     LLRTIGKGNF AKVKLARHIL TGREVAIKII DKTQLNPSSL QKLFREVRIM KGLNHPNIVK
     LFEVIETEKT LYLVMEYASA GEVFDYLVSH GRMKEKEARA KFRQIVSAVH YCHQKNIVHR
     DLKAENLLLD AEANIKIADF GFSNEFTLGS KLDTFCGSPP YAAPELFQGK KYDGPEVDIW
     SLGVILYTLV SGSLPFDGHN LKELRERVLR GKYRVPFYMS TDCESILRRF LVLNPAKRCT
     LEQIMKDKWI NIGYEGEELK PYTEPEEDFG DTKRIEVMVG MGYTREEIKE ALTNQKYNEV
     TATYLLLGRK TEEGGDRGAP GLALARVRAP SDTTNGTSSS KGSSHNKGQR ASSSTYHRQR
     RHSDFCGPSP APLHPKRSPT STGDTELKEE RMPGRKASCS AVGSGSRGLP PSSPMVSSAH
     NPNKAEIPER RKDSTSTPNN LPPSMMTRRN TYVCTERPGS ERPSLLPNGK ENSSGTSRVP
     PASPSSHSLA PPSGERSRLA RGSTIRSTFH GGQVRDRRAG SGSGGGVQNG PPASPTLAHE
     AAPLPSGRPR PTTNLFTKLT SKLTRRVTDE PERIGGPEVT SCHLPWDKTE TAPRLLRFPW
     SVKLTSSRPP EALMAALRQA TAAARCRCRQ PQPFLLACLH GGAGGPEPLS HFEVEVCQLP
     RPGLRGVLFR RVAGTALAFR TLVTRISNDL EL
//
ID   DISP2_MOUSE             Reviewed;        1345 AA.
AC   Q8CIP5; Q148A2; Q80T98; Q8CBA3;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 47.
DE   RecName: Full=Protein dispatched homolog 2;
GN   Name=Disp2; Synonyms=Kiaa1742;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=129; TISSUE=Lung;
RX   MEDLINE=22259598; PubMed=12372301; DOI=10.1016/S0092-8674(02)00977-7;
RA   Ma Y., Erkner A., Gong R., Yao S., Taipale J., Basler K., Beachy P.A.;
RT   "Hedgehog-mediated patterning of the mammalian embryo requires
RT   transporter-like function of dispatched.";
RL   Cell 111:63-75(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Bone;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 378-1345 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CIP5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CIP5-2; Sequence=VSP_029324, VSP_029325;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the dispatched family.
CC   -!- SIMILARITY: Contains 1 SSD (sterol-sensing) domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY150699; AAN52162.1; -; mRNA.
DR   EMBL; AK036480; BAC29446.1; -; mRNA.
DR   EMBL; AL772255; CAM45999.1; -; Genomic_DNA.
DR   EMBL; AL772255; CAM46000.1; -; Genomic_DNA.
DR   EMBL; BC118526; AAI18527.1; -; mRNA.
DR   EMBL; AK122547; BAC65829.1; -; mRNA.
DR   IPI; IPI00229895; -.
DR   IPI; IPI00406957; -.
DR   RefSeq; NP_733481.1; NM_170593.3.
DR   UniGene; Mm.221499; -.
DR   ProteinModelPortal; Q8CIP5; -.
DR   SMR; Q8CIP5; 880-1071.
DR   PhosphoSite; Q8CIP5; -.
DR   PRIDE; Q8CIP5; -.
DR   Ensembl; ENSMUST00000037547; ENSMUSP00000037136; ENSMUSG00000040035.
DR   GeneID; 214240; -.
DR   KEGG; mmu:214240; -.
DR   UCSC; uc008lsr.1; mouse.
DR   CTD; 214240; -.
DR   MGI; MGI:2388733; Disp2.
DR   GeneTree; ENSGT00530000063208; -.
DR   HOGENOM; HBG713127; -.
DR   HOVERGEN; HBG094891; -.
DR   InParanoid; Q8CIP5; -.
DR   OMA; FQRLLPC; -.
DR   OrthoDB; EOG4HQDHN; -.
DR   PhylomeDB; Q8CIP5; -.
DR   NextBio; 374236; -.
DR   ArrayExpress; Q8CIP5; -.
DR   Bgee; Q8CIP5; -.
DR   CleanEx; MM_DISP2; -.
DR   Genevestigator; Q8CIP5; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR000731; SSD.
DR   PROSITE; PS50156; SSD; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   1345       Protein dispatched homolog 2.
FT                                /FTId=PRO_0000310697.
FT   TRANSMEM    125    145       Helical; (Potential).
FT   TRANSMEM    440    460       Helical; (Potential).
FT   TRANSMEM    465    485       Helical; (Potential).
FT   TRANSMEM    497    517       Helical; (Potential).
FT   TRANSMEM    544    564       Helical; (Potential).
FT   TRANSMEM    572    592       Helical; (Potential).
FT   TRANSMEM    659    679       Helical; (Potential).
FT   TRANSMEM    919    939       Helical; (Potential).
FT   TRANSMEM    945    965       Helical; (Potential).
FT   TRANSMEM    974    994       Helical; (Potential).
FT   TRANSMEM   1019   1039       Helical; (Potential).
FT   TRANSMEM   1043   1063       Helical; (Potential).
FT   DOMAIN      429    598       SSD.
FT   CARBOHYD    304    304       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    420    420       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    776    776       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     271    302       IRSHISFGALCQRSAANECCPSWSLGNYLAVL -> EGSVR
FT                                VPVVSAMWEAEAGGLLEPRRPSTAWTT (in isoform
FT                                2).
FT                                /FTId=VSP_029324.
FT   VAR_SEQ     303   1345       Missing (in isoform 2).
FT                                /FTId=VSP_029325.
FT   CONFLICT   1066   1066       C -> S (in Ref. 5; BAC65829).
FT   CONFLICT   1219   1219       S -> P (in Ref. 4; AAI18527 and 5;
FT                                BAC65829).
SQ   SEQUENCE   1345 AA;  147944 MW;  931738C26FD3A57F CRC64;
     MAPEASPERS CSLHTCPLED PTGAPVPPPT VSTLQAIDPT SPLTAGHFAF PRAPQDYQEG
     SSLLGLGDQA SLCAHVSNLS TSIDTSQHDG VWKQPSVQRH VVSVRQERTF RMPKSYSHMI
     ADWPVAVIVG CLAFIFLCTL AGLLGSPPLD FSEPLLGFEP RDTEIGRRLE VWKAMQALTG
     PKNLLSLSPD PEMNSSSLLS TLSPAAWGRA EESVVRTKRM VGPVEVKEEE NFFCGRPEKS
     HAKLVFVSTS GGSLWNLQAI HSMCRIEQEQ IRSHISFGAL CQRSAANECC PSWSLGNYLA
     VLSNRSSCQD TTQADTDRTL ALLRFCATFY HRGVLVPACV GSSQDKPPFC AQVPAKCTGS
     NVVYEFLHYL LDRDFLSPQT ADYQVPSLKF ALLFLPIIKT SSLLDIYLDG LGDPIKVSDN
     YTSISGMDLG LKPRLLKYYL AEDTMYPLIA LVVIFFGMSL YLRSLFITFM SLLGVLGSLM
     VAYFLYHVAF RMAYFPFVNL AALLLLSGVC VNYTLIFLDM WRLSRGQVPS GGMPHRVGRT
     MHHFGYLLLV SGLTTSAAFY GSYLSRLPAV RCFALFMGTA VLVHMGLTLL WLPATVVLHE
     RYLAHGCVAQ AHGQRGGSDP LRLLLALHRR IRIFRKIISI LSRLLFQRLL PCGVIKFRYI
     WICWFAALAA GGAYIGGVSP RLQLPILLPL GGQFFRSSHP FERFDAEYRQ QFLFEDLPPN
     EGGNLPVVLV WGILPVDTSD PLDPRTNSSV VSDPDFSPSS PEAQEWLLAL CHGAQNQSFF
     GDQPEGWPTL CLVEALQQWM ESPSCGRLGP DLCCGQSEFP WAPQLYLHCL KMMALEQSPD
     GTRDLGLRFD THGNLAALVL KFQTNLPYST EYGPVHHFYT EISRWLSTEM SKAPPGLNQG
     WFTSNLELYS LQHSLSTEPA VVLGLALALA FATLLLSTWN VPLSLFSVAA VAGTVLLTVG
     LLVLLEWQLN TAEALFLSAS VGLSVDLTIN YCISYHLCPH PDRLSRVAFS LRQISRATAM
     TTGVLFASGV IMLPSTILLY RKLGIIVMMV KFLGCGFASF FFQSLCCFFG PEKNCGQILW
     PCAHLPWDAG TEDPDEKGRA GPPGFSEHYE LQPLARRRSP SFDTSTATSK LSHRPSILSE
     DLQIHDGSCC LQHAQAPVSP RDLLLDHQTV FSQCPALQTS SPYKQAGPTP QTWIRQDSQG
     QKTEPLQALP EGPAHCPKSK VEELPDGLCS SASTLEGLSV SDDTCASEHS VRVPDSVGTS
     PEVMNGTGHP ILERGQLNGK RDTLWLALKE TIYDPNMPNS HHSSLSWKGR GGPGDISPVM
     LPNSQPDLPD VWLRRPSTYT SGYSS
//
ID   DOCK3_MOUSE             Reviewed;        2027 AA.
AC   Q8CIQ7;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Dedicator of cytokinesis protein 3;
DE   AltName: Full=Modifier of cell adhesion;
DE   AltName: Full=Presenilin-binding protein;
DE            Short=PBP;
GN   Name=Dock3; Synonyms=Moca;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND INTERACTION WITH PSEN1 AND CRK.
RC   TISSUE=Brain;
RX   MEDLINE=20312861; PubMed=10854253;
RX   DOI=10.1046/j.1471-4159.2000.0750109.x;
RA   Kashiwa A., Yoshida H., Lee S., Paladino T., Liu Y., Chen Q.,
RA   Dargusch R., Schubert D., Kimura H.;
RT   "Isolation and characterization of novel presenilin binding protein.";
RL   J. Neurochem. 75:109-116(2000).
RN   [2]
RP   FUNCTION, AND INTERACTION WITH PSEN2.
RX   MEDLINE=22100008; PubMed=12093789; DOI=10.1083/jcb.200110151;
RA   Chen Q., Kimura H., Schubert D.;
RT   "A novel mechanism for the regulation of amyloid precursor protein
RT   metabolism.";
RL   J. Cell Biol. 158:79-89(2002).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2010, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
CC   -!- FUNCTION: Potential guanine nucleotide exchange factor (GEF). GEF
CC       proteins activate some small GTPases by exchanging bound GDP for
CC       free GTP. Its interaction with presenilin proteins as well as its
CC       ability to stimulate Tau/MAPT phosphorylation suggest that it may
CC       be involved in Alzheimer disease. Ectopic expression in nerve
CC       cells decreases the secretion of beta-amyloid APBA1 protein and
CC       lowers the rate of cell-substratum adhesion, suggesting that it
CC       may affect the function of some small GTPase involved in the
CC       regulation of actin cytoskeleton or cell adhesion receptors.
CC   -!- SUBUNIT: Interacts with presenilin proteins PSEN1 and PSEN2.
CC       Interacts with CRK.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Expressed in brain. Not expressed in heart,
CC       liver, kidney, spleen and lung. In brain, it is highly expressed
CC       in the cerebral cortex and hippocampus, while it is absent in
CC       other tissues, except in spinal cord. In the cerebral cortex, it
CC       is found within the intermediate (III and IV) and deep (V and VI)
CC       layers, whereas it is weakly expressed in superficial layer I. It
CC       is also abundant in the piriform cortex. Within the hippocampus,
CC       it is expressed in the pyramidal neurons of the CA1, CA2, and CA3
CC       regions and the dentate gyrus.
CC   -!- DOMAIN: The DHR-2 domain may mediate some GEF activity (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the DOCK family.
CC   -!- SIMILARITY: Contains 1 DHR-1 (CZH-1) domain.
CC   -!- SIMILARITY: Contains 1 DHR-2 (CZH-2) domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY145302; AAN12300.1; -; mRNA.
DR   IPI; IPI00284521; -.
DR   UniGene; Mm.150259; -.
DR   ProteinModelPortal; Q8CIQ7; -.
DR   SMR; Q8CIQ7; 1-165, 421-600, 1230-1630.
DR   IntAct; Q8CIQ7; 2.
DR   STRING; Q8CIQ7; -.
DR   PRIDE; Q8CIQ7; -.
DR   Ensembl; ENSMUST00000044532; ENSMUSP00000047652; ENSMUSG00000039716.
DR   UCSC; uc009rkv.1; mouse.
DR   MGI; MGI:2429763; Dock3.
DR   GeneTree; ENSGT00590000083100; -.
DR   HOGENOM; HBG356771; -.
DR   HOVERGEN; HBG051389; -.
DR   InParanoid; Q8CIQ7; -.
DR   OrthoDB; EOG4NS39M; -.
DR   ArrayExpress; Q8CIQ7; -.
DR   Bgee; Q8CIQ7; -.
DR   CleanEx; MM_DOCK3; -.
DR   Genevestigator; Q8CIQ7; -.
DR   GermOnline; ENSMUSG00000039716; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005625; C:soluble fraction; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0051020; F:GTPase binding; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR010703; DOCK.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF06920; Ded_cyto; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Guanine-nucleotide releasing factor; Phosphoprotein;
KW   SH3 domain; SH3-binding.
FT   CHAIN         1   2027       Dedicator of cytokinesis protein 3.
FT                                /FTId=PRO_0000189989.
FT   DOMAIN        6     67       SH3.
FT   DOMAIN      418    653       DHR-1.
FT   DOMAIN     1119   1627       DHR-2.
FT   MOTIF      1967   1973       SH3-binding (Potential).
FT   COMPBIAS   1728   1765       Ser-rich.
FT   MOD_RES    2010   2010       Phosphoserine.
SQ   SEQUENCE   2027 AA;  232910 MW;  006DCE0B4583A1CC CRC64;
     MWTPTEEEKY GVVICSFRGS VPQGLVLEIG ETVQILEKCE GWYRGVSTKK PNVKGLFPAN
     YIHLKKAIVS NRGQYETVVP LEDSIVTEVT TTLQEWASLW KQLYVKHKVD LFYKLRHVMN
     ELIDLRRQLL SGHLTQDQVR EVKRHITVRL DWGNEHLGLD LVPRKDFEVV DSDQISVSDL
     YKMHLSSRQS VQQSTSQVDT MRPRHGETCR MPVPYHFFFS LKSFTYNTIG EDSDVFFSLY
     DMREGKQISE RFLVRLNKNG GPRNPEKIER MCALFTDLSS KDMKRDLYIV AHVIRIGRML
     LNDSKKGPAH LHYRRPYGCA VLSILDVLQS LTELKEEKDF VLKVYTCNNE SEWTQIHENI
     IRKSSTKYSA PSASHGLIIS LQLFRGDMEQ IRRENPMIFN RGLAITRKLG FPDVIMPGDI
     RNDLYLTLEK GDFERGGKSV QKNIEVTMYV LYADGEILKD CISLGSGEPN RSSYHSFVLY
     HSNSPRWGEI IKLPIPIDRF RGSHLRFEFR HCSTKDKGEK KLFGFAFSPL MRDDGTTLSD
     DIHELYVYKC DENSTFNNHA LYLGLPCCKE DYNGCPNIPS SLIFQRSKES FFISTQLSST
     KLTQNVDLLA LLKWKAFPDR IMDILGRLRH VSGEEIVKFL QDILDTLFVI LDDNTEKYGL
     LVFQSLVFII NLLRDIKYFH FRPVMDTYIQ KHFAGALAYK ELIRCLKWYM DCSAELIRQD
     HIQEAMRALE YLFKFIVQSR ILYSRATCGM EEEQFRSSIQ ELFQSIRFVL SLDSRNSETL
     LFTQAALLNS FPTIFDELLQ MFTVQEVAEF VRGTLGSMPS TVHIGQSMDV VKLQSIARTV
     DSRLFSFSES RRILLPVVLH HIHLHLRQQK ELLICSGILG SIFSIVKTSS LEADVMEEVE
     MMVESLLDVL LQTLLTIMSK SHAQEAVRGH CPVTAEITGE YVSCLLSLLR QMCDTHFQHL
     LDNFQSKDEL KEFLLKIFCV FRNLMKMSVF PRDWMVMRLL TSNIIVTTVQ YLSSALHKNF
     TETDFDFKVW NSYFSLAVLF INQPSLQLEI ITSAKRKKIL DKYGDMRVMM AYELFSMWQN
     LGEHKIHFIP GMIGPFLGVT LVPQPEVRNI MIPIFHDMMD WEQRKNGNFK QVEAELIDKL
     DSMVSEGKGD ESYRELFGLL TQLFGPYPSL LEKVEQETWR ETGISFVTSV TRLMERLLDY
     RDCMKGEETE NKKVGCTVNL MNFYKSEINK EEMYIRYIHK LCDMHLQAEN YTEAAFTLLL
     YCELLQWEDR PLREFLHYPS QTEWQRKEGL CRKIIHYFNK GKSWEFGIPL CRELACQYES
     LYDYQSLSWI RKMEASYYDN IIEQQRLEPE FFRVGFYGRK FPFFLRNKEY VCRGHDYERL
     EAFQQRMLSE FPQAVAMQHP NHPDDAILQC DAQYLQIYAV TPIPDYVDVL QMDRVPDRVK
     SFYRVNNVRK FRYDRPFHKG PKDKDNEFKS LWIERTTLTL THSLPGISRW FEVERRELVE
     VSPLENAIQV VENKNQELRA LISQYQHKQV HGNINLLSMC LNGVIDAAVN GGIARYQEAF
     FDKDYITKHP GDAEKISQLK ELMQEQVHVL GVGLAVHEKF VHPEMRPLHK KLIDQFQMMR
     ASLYHEFPGL DKLSPACSGT STPRGNVLAS HSPMSPENIK MTHRHSPMNL MGTGRHSSSS
     LSSHASSEAG NMMMMGDNSM GEAPEDLYHH MQLAYHNPRY QGSVTNVSVL SSSQASPSSS
     SLSSTHSAPS QMITSAPSST RGSPSLPDKY RHAREMMLLL PTHRDRPSSA MYPAAILENG
     QPPNFQRALF QQVVGACKPC SDPNLSMAEK GHYSLHFDAF HHPLGDTPPA LPARTLRKSP
     LHPIPASPTS PQSGLDGSNS TLSGSASSGV SSLSESNFGH SSEAPPRTDT MDSMPSQAWN
     GDEGLEPPYL PVHYSLSESA VLDAIKSQPC RSHSAPGCVL PQDPMDPPAL PPKPYHPRLP
     ALEHDEGMLL REEAERPRGL HRKASLPPGS VKEEQARLAW EHGRGEQ
//
ID   MBRL_MOUSE              Reviewed;         574 AA.
AC   Q8CIV2; Q68EE1; Q6KAN7; Q7TS84; Q8CIV1; Q99K29;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Membralin;
GN   Name=ORF61;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain;
RX   MEDLINE=22525561; PubMed=12638133; DOI=10.1016/S1567-133X(02)00019-4;
RA   Andersson O., von Euler G.;
RT   "Characterization and expression of the gene encoding membralin, an
RT   evolutionary conserved protein expressed in the central nervous
RT   system.";
RL   Gene Expr. Patterns 1:205-212(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 91-574 (ISOFORM 1).
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 374-574.
RC   TISSUE=Embryonic tail;
RX   PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of FLJ genes:
RT   the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:127-135(2004).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-180, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Membralin-1;
CC         IsoId=Q8CIV2-1; Sequence=Displayed;
CC       Name=2; Synonyms=Membralin-2;
CC         IsoId=Q8CIV2-2; Sequence=VSP_014379;
CC         Note=No experimental confirmation;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH52787.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AY096037; AAM34493.1; -; mRNA.
DR   EMBL; AY096036; AAM34492.1; -; mRNA.
DR   EMBL; BC005494; AAH05494.1; -; mRNA.
DR   EMBL; BC052787; AAH52787.1; ALT_INIT; mRNA.
DR   EMBL; AK131170; BAD21420.1; -; mRNA.
DR   IPI; IPI00229925; -.
DR   IPI; IPI00462465; -.
DR   RefSeq; NP_001003949.2; NM_001003949.3.
DR   UniGene; Mm.29442; -.
DR   ProteinModelPortal; Q8CIV2; -.
DR   STRING; Q8CIV2; -.
DR   PRIDE; Q8CIV2; -.
DR   Ensembl; ENSMUST00000052885; ENSMUSP00000056792; ENSMUSG00000013858.
DR   Ensembl; ENSMUST00000105375; ENSMUSP00000101014; ENSMUSG00000013858.
DR   GeneID; 216157; -.
DR   KEGG; mmu:216157; -.
DR   UCSC; uc007gax.1; mouse.
DR   UCSC; uc007gay.1; mouse.
DR   CTD; 216157; -.
DR   MGI; MGI:2177957; ORF61.
DR   GeneTree; ENSGT00390000013329; -.
DR   HOVERGEN; HBG053033; -.
DR   OMA; AYIHIAF; -.
DR   OrthoDB; EOG4FBHT1; -.
DR   PhylomeDB; Q8CIV2; -.
DR   NextBio; 375028; -.
DR   ArrayExpress; Q8CIV2; -.
DR   Bgee; Q8CIV2; -.
DR   CleanEx; MM_ORF61; -.
DR   Genevestigator; Q8CIV2; -.
DR   GermOnline; ENSMUSG00000013858; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR019144; Membralin.
DR   Pfam; PF09746; Membralin; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Glycoprotein; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    574       Membralin.
FT                                /FTId=PRO_0000096274.
FT   TRANSMEM     69     89       Helical; (Potential).
FT   TRANSMEM    122    142       Helical; (Potential).
FT   TRANSMEM    293    313       Helical; (Potential).
FT   TRANSMEM    337    357       Helical; (Potential).
FT   TRANSMEM    394    411       Helical; (Potential).
FT   TRANSMEM    417    437       Helical; (Potential).
FT   TRANSMEM    520    540       Helical; (Potential).
FT   COMPBIAS     14     19       Poly-Gly.
FT   COMPBIAS    143    148       Poly-Glu.
FT   CARBOHYD    180    180       N-linked (GlcNAc...).
FT   VAR_SEQ     324    324       I -> IGESQPAGGGVGSPQALMGGRPVPA (in
FT                                isoform 2).
FT                                /FTId=VSP_014379.
FT   CONFLICT     83     83       A -> V (in Ref. 1; AAM34493).
FT   CONFLICT     95     95       N -> D (in Ref. 1; AAM34492).
FT   CONFLICT    198    198       D -> V (in Ref. 1; AAM34492).
FT   CONFLICT    224    224       P -> S (in Ref. 1; AAM34493).
FT   CONFLICT    281    281       E -> G (in Ref. 1; AAM34493).
FT   CONFLICT    301    301       I -> F (in Ref. 1; AAM34493).
FT   CONFLICT    339    339       F -> S (in Ref. 1; AAM34492).
FT   CONFLICT    354    354       M -> V (in Ref. 1; AAM34493).
FT   CONFLICT    374    396       TVWLADQYDAICCHTNTSKRHWL -> GASWAPGWDREGPV
FT                                WQGSFSRPH (in Ref. 3).
FT   CONFLICT    423    423       V -> D (in Ref. 1; AAM34493).
FT   CONFLICT    540    540       S -> N (in Ref. 1; AAM34493).
SQ   SEQUENCE   574 AA;  63561 MW;  898C0EBDF9B25FD1 CRC64;
     MSEHAAAPGP GPNGGGGGGA APVRGPRGPN LNPNPLINVR DRLFHALFFK MAVTYSRLFP
     PAFRRLFEFF VLLKALFVLF VLAYIHIVFS RSPINCLEHV RDRWPREGVL RVEVRHNSSR
     APVILQFCDG GLGGLELEPG GLELEEEELT VEMFTNSSIK FELDIEPKVF KPQSGADALN
     DSQDFPFPET PAKVWPQDEY IVEYSLEYGF LRLSQATRQR LSIPVMVVTL DPTRDQCFGD
     RFSRLLLDEF LGYDDILMSS VKGLAENEEN KGFLRNVVSG EHYRFVSMWM ARTSYLAAFV
     IMVIFTLSVS MLLRYSHHQI FVFIVDLLQM LEMNMAIAFP AAPLLTVILA LVGMEAIMSE
     FFNDTTTAFY IILTVWLADQ YDAICCHTNT SKRHWLRFFY LYHFAFYAYH YRFNGQYSSL
     ALVTSWLFIQ HSMIYFFHHY ELPAILQQIR IQEMLLQTPP LGPGTPTALP DDLNNNSGSP
     ATPDPSPPLA LGPSSSPAPT GGASGPGSLG AGASVSGSDL GWVAETAAII SDASFLSGLS
     ASLLERRPTA PSTPDSSRPD PGVPLEDAPA PAGS
//
ID   MICA3_MOUSE             Reviewed;        1993 AA.
AC   Q8CJ19; Q3UGQ8; Q69ZY5; Q80TE8; Q8BXB1;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Protein MICAL-3;
GN   Name=Mical3; Synonyms=Kiaa0819, Kiaa1364;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   TISSUE=Testis;
RA   Korenbaum E., Hust H., Munck M., Noegel A.A.;
RT   "Flavoprotein oxidoreductase MICAL-3 is associated with spermatid
RT   development.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1526-1993 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-695 (ISOFORMS 1/2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1740 (ISOFORM 4).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1153; SER-1187 AND
RP   SER-1216, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-977 AND SER-1307, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Associated with spermatid development.
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- SUBUNIT: Interacts with RAB1B (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8CJ19-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CJ19-2; Sequence=VSP_039491, VSP_039492;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8CJ19-3; Sequence=VSP_039493, VSP_039494;
CC       Name=4;
CC         IsoId=Q8CJ19-4; Sequence=VSP_039490, VSP_039495;
CC   -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC   -!- SIMILARITY: Contains 1 LIM zinc-binding domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65779.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AF536756; AAN06715.1; -; mRNA.
DR   EMBL; AK173033; BAD32311.1; -; mRNA.
DR   EMBL; AK122497; BAC65779.1; ALT_INIT; mRNA.
DR   EMBL; AC079443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC083894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK147803; BAE28149.1; -; mRNA.
DR   EMBL; AK048201; BAC33271.1; -; mRNA.
DR   IPI; IPI00229906; -.
DR   IPI; IPI00890125; -.
DR   IPI; IPI00956923; -.
DR   IPI; IPI00968905; -.
DR   RefSeq; NP_700445.2; NM_153396.2.
DR   UniGene; Mm.122399; -.
DR   ProteinModelPortal; Q8CJ19; -.
DR   SMR; Q8CJ19; 9-494, 515-630, 759-822.
DR   STRING; Q8CJ19; -.
DR   PhosphoSite; Q8CJ19; -.
DR   PRIDE; Q8CJ19; -.
DR   Ensembl; ENSMUST00000077159; ENSMUSP00000076402; ENSMUSG00000003178.
DR   GeneID; 194401; -.
DR   KEGG; mmu:194401; -.
DR   UCSC; uc009dnz.1; mouse.
DR   UCSC; uc009doa.1; mouse.
DR   CTD; 194401; -.
DR   MGI; MGI:2442733; Mical3.
DR   eggNOG; roNOG08139; -.
DR   GeneTree; ENSGT00600000084263; -.
DR   HOVERGEN; HBG052474; -.
DR   InParanoid; Q8CJ19; -.
DR   OrthoDB; EOG4TXBR4; -.
DR   Bgee; Q8CJ19; -.
DR   Genevestigator; Q8CJ19; -.
DR   GermOnline; ENSMUSG00000003178; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:InterPro.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR022735; DUF3585.
DR   InterPro; IPR002938; mOase_FAD-bd.
DR   InterPro; IPR003042; Rng_hydrolase-like.
DR   InterPro; IPR001781; Znf_LIM.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 1.
DR   Gene3D; G3DSA:2.10.110.10; Znf_LIM; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF12130; DUF3585; 1.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   Pfam; PF00412; LIM; 1.
DR   PRINTS; PR00420; RNGMNOXGNASE.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00132; LIM; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; FAD;
KW   Flavoprotein; LIM domain; Metal-binding; Phosphoprotein; Zinc.
FT   CHAIN         1   1993       Protein MICAL-3.
FT                                /FTId=PRO_0000075847.
FT   DOMAIN      518    621       CH.
FT   DOMAIN      762    824       LIM zinc-binding.
FT   NP_BIND      88    117       FAD (Potential).
FT   COILED     1817   1983       Potential.
FT   COMPBIAS    688    691       Poly-Glu.
FT   MOD_RES     649    649       Phosphoserine (By similarity).
FT   MOD_RES     977    977       Phosphoserine.
FT   MOD_RES    1153   1153       Phosphoserine.
FT   MOD_RES    1154   1154       Phosphoserine (By similarity).
FT   MOD_RES    1187   1187       Phosphoserine.
FT   MOD_RES    1216   1216       Phosphoserine.
FT   MOD_RES    1307   1307       Phosphoserine.
FT   MOD_RES    1335   1335       Phosphoserine (By similarity).
FT   MOD_RES    1339   1339       Phosphothreonine (By similarity).
FT   MOD_RES    1365   1365       Phosphoserine (By similarity).
FT   MOD_RES    1369   1369       Phosphoserine (By similarity).
FT   MOD_RES    1382   1382       Phosphoserine (By similarity).
FT   MOD_RES    1452   1452       Phosphothreonine (By similarity).
FT   MOD_RES    1695   1695       Phosphoserine (By similarity).
FT   MOD_RES    1783   1783       Phosphoserine (By similarity).
FT   MOD_RES    1785   1785       Phosphoserine (By similarity).
FT   MOD_RES    1788   1788       Phosphoserine (By similarity).
FT   MOD_RES    1791   1791       Phosphoserine (By similarity).
FT   MOD_RES    1792   1792       Phosphoserine (By similarity).
FT   VAR_SEQ       1    871       Missing (in isoform 4).
FT                                /FTId=VSP_039490.
FT   VAR_SEQ     748    774       GSIKKEFPQNLGGSDTCYFCQKRVYVM -> VSPKLSSRMT
FT                                TWYRKEGLHAAISQALV (in isoform 2).
FT                                /FTId=VSP_039491.
FT   VAR_SEQ     775   1993       Missing (in isoform 2).
FT                                /FTId=VSP_039492.
FT   VAR_SEQ     810    864       GKFYCKPHYCYRLSGYAQRKRPAVAPLSGKEVKGALQDGPT
FT                                ADANGLASVAASSA -> EFSPNFWTSASYHVPVALPATVM
FT                                PMCLLYHPSQVLVCLEGGPAFMSPVLFNDTNS (in
FT                                isoform 3).
FT                                /FTId=VSP_039493.
FT   VAR_SEQ     865   1993       Missing (in isoform 3).
FT                                /FTId=VSP_039494.
FT   VAR_SEQ    1016   1061       Missing (in isoform 4).
FT                                /FTId=VSP_039495.
FT   CONFLICT    281    281       A -> T (in Ref. 1; AAN06715).
FT   CONFLICT   1249   1249       P -> H (in Ref. 4; BAE28149).
SQ   SEQUENCE   1993 AA;  223721 MW;  5059DCB5EF4DB091 CRC64;
     MEERKQETTN QAHVLFDRFV QATTCKGTLR AFQELCDHLE LKPKDYRSFY HKLKSKLNYW
     KAKALWAKLD KRGSHKDYKK GKACTNTKCL IIGAGPCGLR TAIDLSLLGA KVVVIEKRDA
     FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGAIDHISIR QLQLILLKVA LILGIEIHVN
     VEFQGLVQPP EDQENERIGW RALVHPKTHP VSEYEFEVII GGDGRRNTLE GFRRKEFRGK
     LAIAITANFI NRNTTAEAKV EEISGVAFIF NQKFFQELRE ATGIDLENIV YYKDDTHYFV
     MTAKKQSLLD KGVILHDYTD TELLLSRENV DQEALLNYAR EAADFSTQQQ LPSLDFAINH
     YGQPDVAMFD FTCMYASENA ALVREQNGHQ LLVALVGDSL LEPFWPMGTG IARGFLAAMD
     SAWMVRSWSL GTSPLEVLAE RESIYRLLPQ TTPENVSKNF SQYSIDPVTR YPNININFLR
     PSQVRHLYDS GETKDIHLEM ENMVNPRTTP KLTRNESVAR SSKLLGWCQR QTEGYSGVNV
     TDLTMSWKSG LALCAIIHRY RPDLIDFDSL DEQNVEKNNQ LAFDIAEKEL GISPIMTGKE
     MASVGEPDKL SMVMYLTQFY EMFKDSLSSS DTLDLNAEEK AVLIASTKSP ISFLSKLGQT
     ISRKRSPKDK KEKDSDGAGK RRKTSQSEEE EPPRSYKGER PTLVSTLTDR RMDAAVGNQN
     KVKYMATQLL AKFEENAPAQ STGVRRQGSI KKEFPQNLGG SDTCYFCQKR VYVMERLSAE
     GKFFHRSCFK CEYCATTLRL SAYAYDIEDG KFYCKPHYCY RLSGYAQRKR PAVAPLSGKE
     VKGALQDGPT ADANGLASVA ASSAERSPGT SMNGLEEPSI AKRLRGTPER IELENYRRSV
     RQVEELEEVP EETQAEHNLS SVLDKGTEED VASSSSESEM EEEEEEDDED DHLPTSDLGG
     VPWKEAVRIH ALLKGRSEEE LEASKNFEPE EEEEEEEYEE EDEEYEEEEE EESSEAGNKR
     LQQIITAADP LAIQADVHWT HIREREAEER MLPTSESSTS RAPLDEDDLE EDADSEPAET
     EGEAAEDGDP GDTGAELDDQ HWSDDIPSDA EAEHRLQSQA KVKAELELRV SENEEEKPSD
     APKQEERGTS QVSSPSQPPE KQVGVFSPAR SPGTEEAKSP LATKVKSPEE PLFPTPLLLR
     EKPKAEVPEE QKAVLSPIRS QPVALPEARS PTSPTSLQPE SLLAPPTPPT PPPTQLPICS
     QPQPSSDASI PSPTKSPIRF QPVPAKTSTP LTPLPVKSQG DPKDRLSGPL AVEEVLKRSD
     LVEEFWMKSA EIRRSLGLTP VDRSKGSEPS LPSPASKPIS LKSYSVDKSP QDEGLCLLKP
     PSVPKRLGLP KSAGDQPPLL TPKSPSDKEL RSSQEERRDL SSSSGLGLHD SSSNMKTLGS
     QSFNTSDSTM LTPPSSPPPP PPPNEEPATL RRKPHQTFER REASIIPPPT PASFMRPPRE
     PAQPPREEVR KSFVESVDEI PFADDVEDTY DDKTEDSSLQ EKFFTPPSCW SRSEKLQAKE
     NGRLPPLEQD VPPQKRGLPL VSAEAKELAE ERMRAREKSV KSQALRDAMA KQLSRMQAME
     MVSSRSHTAQ SQGKELGSES TRHPSLRGTQ EPTLKHEATS EEILSPPSDS GGPDGSVTSS
     EGSSGKSKKR SSLFSPRRNK KEKKTKGEAR PPEKPSPGLP EDVVAKPKSL WKSVFSGYKK
     DKKKKSDEKS CSSTPSSGAT VDSGQRRASP MVRAELQLRR QLSFSEDSDL SSDDILERSS
     QKSKREPRTY TEEELSAKLT RRVQKAARRQ AKQEELKRLH RAQIIQRQLE QVEEKQRQLE
     ERGVAVEKAL RGEAGMGKKD DPKLMQEWFK LVQEKNAMVR YESELMIFAR ELELEDRQSR
     LQQELRERMA VEDHLKTEGE LSEEKKILNE MLEVVEQRDS LVALLEEQRL REKEEDKDLE
     AAMLCKGFSL DWS
//
ID   CROCC_MOUSE             Reviewed;        2009 AA.
AC   Q8CJ40; Q7TQL2; Q80U01; Q8R0B9;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   30-NOV-2010, entry version 49.
DE   RecName: Full=Rootletin;
DE   AltName: Full=Ciliary rootlet coiled-coil protein;
GN   Name=Crocc; Synonyms=Kiaa0445;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH KLC3.
RC   STRAIN=C57BL/6;
RX   MEDLINE=22315152; PubMed=12427867; DOI=10.1083/jcb.200207153;
RA   Yang J., Liu X., Yue G., Adamian M., Bulgakov O., Li T.;
RT   "Rootletin, a novel coiled-coil protein, is a structural component of
RT   the ciliary rootlet.";
RL   J. Cell Biol. 159:431-440(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Colon, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 391-2009 (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   PROTEIN SEQUENCE OF 1261-1274, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=15870283; DOI=10.1128/MCB.25.10.4129-4137.2005;
RA   Yang J., Gao J., Adamian M., Wen X.-H., Pawlyk B., Zhang L.,
RA   Sanderson M.J., Zuo J., Makino C.L., Li T.;
RT   "The ciliary rootlet maintains long-term stability of sensory cilia.";
RL   Mol. Cell. Biol. 25:4129-4137(2005).
RN   [6]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH CEP250.
RX   PubMed=16339073; DOI=10.1091/mbc.E05-10-0943;
RA   Yang J., Adamian M., Li T.;
RT   "Rootletin interacts with C-Nap1 and may function as a physical linker
RT   between the pair of centrioles/basal bodies in cells.";
RL   Mol. Biol. Cell 17:1033-1040(2006).
CC   -!- FUNCTION: Major structural component of the ciliary rootlet, a
CC       cytoskeletal-like structure in ciliated cells which originates
CC       from the basal body at the proximal end of a cilium and extends
CC       proximally toward the cell nucleus. Contributes to centrosome
CC       cohesion before mitosis.
CC   -!- SUBUNIT: Homopolymer. Interacts with KLC3, NEK2 and the N-terminus
CC       of CEP250.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome,
CC       centriole. Note=In ciliated cells, associated with ciliary
CC       rootlets. In non-ciliated cells, localized between, around and at
CC       the proximal ends of the centrioles. Dissociates from the
CC       centrioles at the onset of mitosis and reassociates with them at
CC       anaphase.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8CJ40-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CJ40-2; Sequence=VSP_052066, VSP_052067;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8CJ40-3; Sequence=VSP_052068;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highest expression detected in photoreceptor
CC       cells of retina. Expressed at lower levels in brain, trachea and
CC       kidney. Detected in all major ciliated epithelia. During embryonic
CC       development, enriched along the apical domains of neuroepithelium
CC       in brain ventricular zone, in primordia of retinal pigment
CC       epithelia and in neural retina.
CC   -!- PTM: Phosphorylated by NEK2 which may regulate its association
CC       with centrosomes. Phosphorylated upon DNA damage, probably by ATM
CC       or ATR (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice have no ciliary rootlets in ciliated
CC       cells.
CC   -!- SIMILARITY: Belongs to the rootletin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH27090.1; Type=Erroneous initiation;
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DR   EMBL; AF527975; AAN73044.1; -; mRNA.
DR   EMBL; BC027090; AAH27090.1; ALT_INIT; mRNA.
DR   EMBL; BC054054; AAH54054.1; -; mRNA.
DR   EMBL; AK122285; BAC65567.3; -; Transcribed_RNA.
DR   IPI; IPI00229917; -.
DR   IPI; IPI00649734; -.
DR   IPI; IPI00760082; -.
DR   RefSeq; NP_001139430.1; NM_001145958.1.
DR   RefSeq; NP_742120.2; NM_172122.2.
DR   UniGene; Mm.80685; -.
DR   ProteinModelPortal; Q8CJ40; -.
DR   IntAct; Q8CJ40; 1.
DR   STRING; Q8CJ40; -.
DR   PhosphoSite; Q8CJ40; -.
DR   PRIDE; Q8CJ40; -.
DR   Ensembl; ENSMUST00000040222; ENSMUSP00000037679; ENSMUSG00000040860.
DR   Ensembl; ENSMUST00000102491; ENSMUSP00000099549; ENSMUSG00000040860.
DR   GeneID; 230872; -.
DR   KEGG; mmu:230872; -.
DR   UCSC; uc008vns.1; mouse.
DR   UCSC; uc008vnt.1; mouse.
DR   CTD; 230872; -.
DR   MGI; MGI:3529431; Crocc.
DR   HOGENOM; HBG283046; -.
DR   HOVERGEN; HBG080162; -.
DR   InParanoid; Q8CJ40; -.
DR   NextBio; 380242; -.
DR   ArrayExpress; Q8CJ40; -.
DR   Bgee; Q8CJ40; -.
DR   CleanEx; MM_CROCC; -.
DR   Genevestigator; Q8CJ40; -.
DR   GermOnline; ENSMUSG00000040860; Mus musculus.
DR   GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR   GO; GO:0035253; C:ciliary rootlet; IDA:MGI.
DR   GO; GO:0019894; F:kinesin binding; IPI:MGI.
DR   GO; GO:0005198; F:structural molecule activity; IDA:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR   GO; GO:0051297; P:centrosome organization; ISS:UniProtKB.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Cilium biogenesis/degradation;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Phosphoprotein.
FT   CHAIN         1   2009       Rootletin.
FT                                /FTId=PRO_0000239944.
FT   COILED       74    265       Potential.
FT   COILED      346    438       Potential.
FT   COILED      550   1058       Potential.
FT   COILED     1091   1439       Potential.
FT   COILED     1498   1697       Potential.
FT   COILED     1744   1998       Potential.
FT   MOD_RES    1612   1612       Phosphoserine (By similarity).
FT   VAR_SEQ       1     74       Missing (in isoform 2).
FT                                /FTId=VSP_052066.
FT   VAR_SEQ     120    209       Missing (in isoform 2).
FT                                /FTId=VSP_052067.
FT   VAR_SEQ    1136   1156       Missing (in isoform 3).
FT                                /FTId=VSP_052068.
FT   CONFLICT    360    360       E -> G (in Ref. 2; AAH54054).
FT   CONFLICT    811    811       V -> M (in Ref. 2; AAH54054).
FT   CONFLICT   1041   1041       K -> E (in Ref. 2; AAH54054).
FT   CONFLICT   1346   1346       L -> V (in Ref. 3; BAC65567).
FT   CONFLICT   1864   1864       F -> L (in Ref. 2; AAH54054).
SQ   SEQUENCE   2009 AA;  226914 MW;  EA9F8A4FF5ED5C35 CRC64;
     MSLGLAGSLQ AQLALEIVIQ SLENCVLGPN QEKSLSVQNR VQDFQGASLL VCAREVIASN
     LSRPETPAPL QVPEMASLLS LQEENQLLQQ ELSRVEDLLA QSRAERDELA IKYNAVNERL
     EQAVRLETGE LEAQEPRGLV RQSVELRRQL QEEQSSYRRK LQAYQEGQQR QAQLVQRLQA
     KILQYKKQCS ELEKQLMDRS TELEQQRLRD TEHSQDLDSA LLRLEEEQQR SASLAQVNAM
     LREQLDQANL ANQALSEDIR KVTSDWTRSC KELEQREAVW RREEESFNAY FSSEHSRLLR
     LWRQVMGLRR QASEVKMGTE RDLLQLGGEL VRTSRAVQEL GLGLSASLHR AESKAEAALE
     KQKLLQAQLE EQLQAKLLRE KDLAQLQVQS DLDKADLSAR VTELALSVEH LQNQNSEKDQ
     VNRTLSDKLE ALESLRLQEQ TTLDTEDGEG LQQTLRDLAQ AALSDTESGV QLSSSERTAD
     TSDGSLRGFS GQRTPTPPRH SPGRGRSPRR GLSPACSDSS TLTLIHSALH KRQLQVQDMR
     GRYEASQELL GSVRKQLSDS EGERRGLEEQ LQRLRDQTAA SAQAQEDAQR EAQRLRSANE
     LLSREKGNLT HSLQVTQQQA KELRQELEKL QAAQEELKRQ HNQLEDAQED SVQEGARARR
     ELERSHRQLE QLEVKRSGLT KELVEVREAL SCAILQRDVL QTEKAEVAEA LTKAEAGRAQ
     LELSLTKLRA EEASLRDSLS KMSALNESLA QDKLELNRLI AQLEEEKVAL LGRQQQAEHA
     TTMAVEKQEL LEQLRLEQEV ERQGLQGSLC VAEQAREALE QQILVLRSER SHLQEQLAQL
     SRQLSGRDQE LEQALRESQR QVEALERAAR EKEAMAKERA GLAVKLAAAE REGRTLSEEA
     IRLRLEKEAL ESSLFDVQRQ LAQLEARREQ LEADSQALLL AKETLTGELA GLRQQVTSTE
     EKAALDKELM TQKLVQAERE AQASLREQRA AHEEDLQRLQ HEKEAAWREL QAERAQLQGQ
     LQQEREELLA RMEAEKEELS KEIAALQQER DEGLLLAESE KQQALSLKES EKTALSEKLM
     GTRHSLAAIS LEMERQKRDA QSRQEQDRNT LNALTSELRD LRAQLEEATA AHAQTVKELE
     ERTGNLGRQR EACMREAEEL RTQLRVLEDT RDGLRRELLE AQRKGRDSQD SSEAHRQEAS
     ELRRSLSEGA KEREALRRSN EELRSAVKKA ESERISLKLA NEDKEQKLAL LEEARVSVAK
     EAGELRASLQ EVERSRLEAR RELQELRRQM KTLDSDNGRL GRELADLQGR LALGERTEKE
     SRREALGLRQ RLLKGESSLE ALKQELQGSQ RKLQEQEAEF RARERGLLGS LEEARGAEKR
     LLDSARSLEL RLEAVRAETS ELGLRLSAAE GRAQGLEVEL ARVEAQRRVA EAQLGGLRSA
     LRRGLGLGRV SSSPAREAPA GGSGDGLSSP SPLEYSPRSQ PPSPGLIASP APPDLDPEAV
     RDALRDFLQE LRSAQRERDE LKVQTSTLSQ QLVEMEAERD HAASRAKQLQ KAVAESEEAW
     RSADRRLSGA QAELALQEES VRRSKRECRA TLDQMAVLER SLQATESELR ASQEKVSKMK
     ATEAKLESDK RRLKEVLDAS ESRSIKLELQ RRALEGELQR SRLGLGDREA HAQALQDRVD
     SLQRQVADSE VKAGTLQLTV ERLSGALAKV EESEGNLRSK VQSLTDALTQ SSASLSSTQD
     KNLHLQKALS TCEHDRQVLQ ERLDAARQAL SEARRQSSSL GEQVQTLRGE LASLELQRGD
     AEGQLQQLQQ ALRQRQEGEA MALRSVQKLQ EERRLLQERL GSLQRALAQL EAEKRDLERS
     ALQFDKDRVA LRKTLDKVER EKLRSHEDTL RLNAERGRLD RTLTGAELDL AEAQQQIQHL
     EAQVDVALEG NHNPVQPEAG EQQLELQQEV ERLRSAQVQT ERTLEARERA HRQRVSGLEE
     QVSTLKAQLH QELRRSSASV SLPPGTPEK
//
ID   CIP4_MOUSE              Reviewed;         603 AA.
AC   Q8CJ53; Q8BTR8; Q8R433; Q99LI0;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Cdc42-interacting protein 4;
DE   AltName: Full=Thyroid receptor-interacting protein 10;
DE            Short=TR-interacting protein 10;
DE            Short=TRIP-10;
GN   Name=Trip10; Synonyms=Cip4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Heart;
RX   MEDLINE=22050151; PubMed=12054674; DOI=10.1016/S0006-291X(02)00398-4;
RA   Wang L., Rudert W.A., Grishin A., Dombrosky-Ferlan P., Sullivan K.,
RA   Deng X., Whitcomb D., Corey S.J.;
RT   "Identification and genetic analysis of human and mouse activated
RT   Cdc42 interacting protein-4 isoforms.";
RL   Biochem. Biophys. Res. Commun. 293:1426-1430(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
RP   CDC42 AND RHOQ, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ILE-454.
RC   TISSUE=Adipocyte;
RX   MEDLINE=22247726; PubMed=12242347; DOI=10.1073/pnas.202495599;
RA   Chang L., Adams R.D., Saltiel A.R.;
RT   "The TC10-interacting protein CIP4/2 is required for insulin-
RT   stimulated Glut4 translocation in 3T3L1 adipocytes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12835-12840(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 98-104, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16735024; DOI=10.1016/j.bbrc.2006.05.073;
RA   Archila S., King M.A., Carlson G.M., Rice N.A.;
RT   "The cytoskeletal organizing protein Cdc42-interacting protein 4
RT   associates with phosphorylase kinase in skeletal muscle.";
RL   Biochem. Biophys. Res. Commun. 345:1592-1599(2006).
RN   [7]
RP   FUNCTION, INTERACTION WITH DNM2 AND WASL, AND SUBCELLULAR LOCATION.
RX   PubMed=16418535; DOI=10.1083/jcb.200508091;
RA   Tsujita K., Suetsugu S., Sasaki N., Furutani M., Oikawa T.,
RA   Takenawa T.;
RT   "Coordination between the actin cytoskeleton and membrane deformation
RT   by a novel membrane tubulation domain of PCH proteins is involved in
RT   endocytosis.";
RL   J. Cell Biol. 172:269-279(2006).
RN   [8]
RP   INTERACTION WITH GAPVD1.
RX   PubMed=17189207; DOI=10.1016/j.cmet.2006.12.006;
RA   Lodhi I.J., Chiang S.-H., Chang L., Vollenweider D., Watson R.T.,
RA   Inoue M., Pessin J.E., Saltiel A.R.;
RT   "Gapex-5, a Rab31 guanine nucleotide exchange factor that regulates
RT   Glut4 trafficking in adipocytes.";
RL   Cell Metab. 5:59-72(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Required to coordinate membrane tubulation with
CC       reorganization of the actin cytoskeleton during endocytosis. Binds
CC       to lipids such as phosphatidylinositol 4,5-bisphosphate and
CC       phosphatidylserine and promotes membrane invagination and the
CC       formation of tubules. Also promotes CDC42-induced actin
CC       polymerization by recruiting WASL/N-WASP which in turn activates
CC       the Arp2/3 complex. Actin polymerization may promote the fission
CC       of membrane tubules to form endocytic vesicles. Required for the
CC       formation of podosomes, actin-rich adhesion structures specific to
CC       monocyte-derived cells. May be required for the lysosomal
CC       retention of FASLG/FASL (By similarity). Required for
CC       translocation of GLUT4 to the plasma membrane in response to
CC       insulin signaling.
CC   -!- SUBUNIT: Interacts with AKAP9, ARHGAP17, DAAM1, DIAPH1, DIAPH2,
CC       DNM1, FASLG/FASL, GAPVD1, LYN, microtubules, PDE6G, SRC and
CC       WAS/WASP. Interacts with the ligand binding domain of the thyroid
CC       receptor (TR) in the presence of thyroid hormone. May interact
CC       with CTNNB1 and HD/HTT (By similarity). Interacts specifically
CC       with GTP-bound CDC42 and RHOQ. Interacts with DNM2 and WASL.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell
CC       cortex. Lysosome. Golgi apparatus (By similarity). Cell membrane.
CC       Cell projection, phagocytic cup (By similarity). Note=Localizes to
CC       cortical regions coincident with F-actin, to lysosomes and to
CC       sites of phagocytosis in macrophages. Also localizes to the Golgi,
CC       and this requires AKAP9 (By similarity). Translocates to the
CC       plasma membrane in response to insulin stimulation, and this may
CC       require active RHOQ.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=Cip4/2;
CC         IsoId=Q8CJ53-1; Sequence=Displayed;
CC       Name=2; Synonyms=H;
CC         IsoId=Q8CJ53-2; Sequence=VSP_021723;
CC       Name=3;
CC         IsoId=Q8CJ53-3; Sequence=VSP_021722;
CC       Name=4;
CC         IsoId=Q8CJ53-4; Sequence=VSP_021722, VSP_021723;
CC   -!- PTM: Tyrosine phosphorylated. Also phosphorylated by PKA (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the FNBP1 family.
CC   -!- SIMILARITY: Contains 1 FCH domain.
CC   -!- SIMILARITY: Contains 1 REM (Hr1) repeat.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AY081142; AAL89589.1; -; mRNA.
DR   EMBL; AF502565; AAN38709.1; -; mRNA.
DR   EMBL; AK088909; BAC40648.1; -; mRNA.
DR   EMBL; AK149902; BAE29155.1; -; mRNA.
DR   EMBL; BC003249; AAH03249.1; -; mRNA.
DR   IPI; IPI00116923; -.
DR   IPI; IPI00229927; -.
DR   IPI; IPI00807747; -.
DR   IPI; IPI00808628; -.
DR   RefSeq; NP_598886.1; NM_134125.3.
DR   UniGene; Mm.37368; -.
DR   HSSP; Q15642; 2CT4.
DR   ProteinModelPortal; Q8CJ53; -.
DR   SMR; Q8CJ53; 10-288, 546-601.
DR   STRING; Q8CJ53; -.
DR   PhosphoSite; Q8CJ53; -.
DR   PRIDE; Q8CJ53; -.
DR   Ensembl; ENSMUST00000019631; ENSMUSP00000019631; ENSMUSG00000019487.
DR   Ensembl; ENSMUST00000077277; ENSMUSP00000076509; ENSMUSG00000019487.
DR   GeneID; 106628; -.
DR   KEGG; mmu:106628; -.
DR   UCSC; uc008dej.1; mouse.
DR   UCSC; uc008dek.1; mouse.
DR   UCSC; uc008del.1; mouse.
DR   UCSC; uc008dem.1; mouse.
DR   CTD; 106628; -.
DR   MGI; MGI:2146901; Trip10.
DR   eggNOG; roNOG13092; -.
DR   GeneTree; ENSGT00510000046403; -.
DR   HOGENOM; HBG446221; -.
DR   HOVERGEN; HBG002489; -.
DR   InParanoid; Q8CJ53; -.
DR   OMA; QEMKQER; -.
DR   OrthoDB; EOG4RBQJD; -.
DR   PhylomeDB; Q8CJ53; -.
DR   ArrayExpress; Q8CJ53; -.
DR   Bgee; Q8CJ53; -.
DR   CleanEx; MM_TRIP10; -.
DR   Genevestigator; Q8CJ53; -.
DR   GermOnline; ENSMUSG00000019487; Mus musculus.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; TAS:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   InterPro; IPR001060; FCH.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50133; FCH; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cell projection; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; Endocytosis;
KW   Golgi apparatus; Lipid-binding; Lysosome; Membrane; Phosphoprotein;
KW   SH3 domain.
FT   CHAIN         1    603       Cdc42-interacting protein 4.
FT                                /FTId=PRO_0000261439.
FT   DOMAIN        1     65       FCH.
FT   REPEAT      405    481       REM.
FT   DOMAIN      542    603       SH3.
FT   REGION        1    284       Induction of membrane tubulation (By
FT                                similarity).
FT   REGION        1    117       Required for podosome formation and
FT                                interaction with AKAP9 and microtubules
FT                                (By similarity).
FT   REGION        1    117       Required for translocation to the plasma
FT                                membrane in response to insulin.
FT   REGION      293    603       Interaction with PDE6G (By similarity).
FT   REGION      293    539       Interaction with CDC42 (By similarity).
FT   REGION      471    603       Required for interaction with FASLG and
FT                                localization to lysosomes (By
FT                                similarity).
FT   REGION      487    543       Interaction with DNM2 and WASL.
FT   REGION      532    603       Interaction with DNM1 and WASL (By
FT                                similarity).
FT   REGION      540    603       Required for podosome formation (By
FT                                similarity).
FT   REGION      546    603       Interaction with WAS (By similarity).
FT   REGION      548    603       Interaction with ARHGAP17, DAAM1, DIAPH1
FT                                and DIAPH2 (By similarity).
FT   COILED      107    200       Potential.
FT   MOD_RES     296    296       Phosphoserine.
FT   MOD_RES     299    299       Phosphoserine (By similarity).
FT   MOD_RES     335    335       Phosphoserine (By similarity).
FT   MOD_RES     351    351       Phosphoserine (By similarity).
FT   VAR_SEQ     329    384       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_021722.
FT   VAR_SEQ     515    515       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_021723.
FT   MUTAGEN     454    454       I->S: Impairs interaction with CDC42 and
FT                                RHOQ and reduces insulin-stimulated
FT                                translocation to the plasma membrane.
FT   CONFLICT    321    321       W -> C (in Ref. 2; AAN38709).
SQ   SEQUENCE   603 AA;  68489 MW;  DDA6271D5FD515AC CRC64;
     MDWGTELWDQ FEVLERHTQW GLDLLDKYVK FVKERAEVEQ AYAKQLRSLV KKYLPKRPTK
     DDPEVKFSQQ QSFVQLLQEV NDFAGQRELV AESLGIRVCL ELAKYSQEMK QERKMHFQEG
     RRAQQQLENG FKQLENSKRK FERDCREAEK AAHTAERLDQ DINATKADVE KAKQQAHLRN
     HMAEESKNEY AAQLQRFNRD QAHFYFSQMP QIFDKLQDMD ERRATRLGAG YGLLSEAELQ
     VVPIIGKCLE GMKVAAESVD AKNDSQVLIE LHKSGFARPG DLEFEDFSQV INRVPSDSSL
     GTPDGRPELR AASSRSRAKR WPFGKKNKPR PPSLSLLGGH LPSTLSDGPS SPRSGRDPLA
     ILSEISKSVK PRLASFRSFR GGRGTVATED FSHLPPEQQR KRLQQQLEER NRELQKEEDQ
     REALKKMKDV YEKTPQMGDP ASLEPRIAET LGNIERLKLE VQKYEAWLAE AESRVLSNRG
     DSLSRHARPP DPPTTAPPDS SSSSTNSGSQ DNKESSSEEP PSEGQDTPIY TEFDEDFEEP
     ASPIGQCVAI YHFEGSSEGT VSMSEGEDLS LMEEDKGDGW TRVRRKQGAE GYVPTSYLRV
     TLN
//
ID   ELYS_MOUSE              Reviewed;        2243 AA.
AC   Q8CJF7; B2RRC8; Q8BVJ5; Q8VD55;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Protein ELYS;
DE   AltName: Full=Embryonic large molecule derived from yolk sac;
DE   AltName: Full=Protein MEL-28;
DE   AltName: Full=Putative AT-hook-containing transcription factor 1;
GN   Name=Ahctf1; Synonyms=Elys;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC   STRAIN=C57BL/6; TISSUE=Yolk sac;
RX   MEDLINE=21950467; PubMed=11952839;
RX   DOI=10.1046/j.1365-2443.2002.00529.x;
RA   Kimura N., Takizawa M., Okita K., Natori O., Igarashi K., Ueno M.,
RA   Nakashima K., Nobuhisa I., Taga T.;
RT   "Identification of a novel transcription factor, ELYS, expressed
RT   predominantly in mouse foetal haematopoietic tissues.";
RL   Genes Cells 7:435-446(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C57BL/6; TISSUE=Liver;
RX   MEDLINE=22630158; PubMed=12745078; DOI=10.1016/S0006-291X(03)00772-1;
RA   Okita K., Takizawa M., Ueno M., Kimura N., Nobuhisa I., Taga T.;
RT   "Genomic organization and characterization of the mouse ELYS gene.";
RL   Biochem. Biophys. Res. Commun. 305:327-332(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2082-2243.
RC   STRAIN=C57BL/6J; TISSUE=Fetal head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=15507119; DOI=10.1111/j.1365-2443.2004.00791.x;
RA   Okita K., Kiyonari H., Nobuhisa I., Kimura N., Aizawa S., Taga T.;
RT   "Targeted disruption of the mouse ELYS gene results in embryonic death
RT   at peri-implantation development.";
RL   Genes Cells 9:1083-1091(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1381, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Required for the assembly of a functional nuclear pore
CC       complex (NPC) on the surface of chromosomes as nuclei form at the
CC       end of mitosis. May initiate NPC assembly by binding to chromatin
CC       and recruiting the Nup107-160 subcomplex of the NPC. Also required
CC       for the localization of the Nup107-160 subcomplex of the NPC to
CC       the kinetochore during mitosis and for the completion of
CC       cytokinesis (By similarity). Has also been proposed to function as
CC       a transcription factor which may play a specific role in
CC       hematopoietic tissues (PubMed:11952839).
CC   -!- SUBUNIT: Associates with the Nup107-160 subcomplex of the NPC (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore (By
CC       similarity). Nucleus, nucleoplasm (By similarity). Nucleus,
CC       nuclear pore complex (By similarity). Nucleus matrix. Cytoplasm.
CC       Note=Localizes to the nuclear pore complex (NPC) throughout
CC       interphase. Localizes to the kinetochore from prophase, and this
CC       appears to require the Nup107-160 subcomplex of the NPC. Localizes
CC       to the periphery of chromatin from late anaphase (By similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed with higher expression in
CC       testis, lung and kidney. Expressed in T-cells, B-cells and
CC       granulocytes in bone marrow.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout the embryo at E3.5 and
CC       E6.5. Higher expression is detected at 10.5 dpc nad then
CC       progressively decreases. Highly expressed in fetal hematopoietic
CC       tissues including liver, spleen and thymus. Expressed in the
CC       endothelium lining the dorsal aorta of 11.5 dpc embryos (at
CC       protein level).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Embryonic lethality before E7.5. Impaired
CC       proliferation of the inner cells of the blastocyst due at least in
CC       part to increased apoptosis.
CC   -!- SIMILARITY: Belongs to the ELYS family.
CC   -!- SIMILARITY: Contains 1 A.T hook DNA-binding domain.
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DR   EMBL; AB059278; BAB78517.1; -; mRNA.
DR   EMBL; AB081498; BAC22610.1; -; Genomic_DNA.
DR   EMBL; BC138343; AAI38344.1; -; mRNA.
DR   EMBL; BC138344; AAI38345.1; -; mRNA.
DR   EMBL; AK078022; BAC37101.2; ALT_SEQ; mRNA.
DR   IPI; IPI00122594; -.
DR   RefSeq; NP_080651.2; NM_026375.2.
DR   UniGene; Mm.128165; -.
DR   ProteinModelPortal; Q8CJF7; -.
DR   STRING; Q8CJF7; -.
DR   PhosphoSite; Q8CJF7; -.
DR   PRIDE; Q8CJF7; -.
DR   Ensembl; ENSMUST00000027768; ENSMUSP00000027768; ENSMUSG00000026491.
DR   GeneID; 226747; -.
DR   KEGG; mmu:226747; -.
DR   UCSC; uc007dvr.1; mouse.
DR   CTD; 226747; -.
DR   MGI; MGI:1915033; Ahctf1.
DR   eggNOG; roNOG13485; -.
DR   GeneTree; ENSGT00390000018900; -.
DR   HOGENOM; HBG506138; -.
DR   InParanoid; Q8CJF7; -.
DR   OMA; LLDIMYS; -.
DR   OrthoDB; EOG4FR0QQ; -.
DR   PhylomeDB; Q8CJF7; -.
DR   NextBio; 378313; -.
DR   ArrayExpress; Q8CJF7; -.
DR   Bgee; Q8CJF7; -.
DR   CleanEx; MM_AHCTF1; -.
DR   Genevestigator; Q8CJF7; -.
DR   GermOnline; ENSMUSG00000026491; Mus musculus.
DR   GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0016363; C:nuclear matrix; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IMP:MGI.
DR   GO; GO:0000910; P:cytokinesis; ISS:UniProtKB.
DR   GO; GO:0030097; P:hemopoiesis; TAS:UniProtKB.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0051292; P:nuclear pore complex assembly; ISS:UniProtKB.
DR   GO; GO:0045941; P:positive regulation of transcription; TAS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:UniProtKB-KW.
DR   InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 3.
DR   SMART; SM00384; AT_hook; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell cycle; Cell division; Centromere; Chromosome;
KW   Cytoplasm; Developmental protein; DNA-binding; Kinetochore; Mitosis;
KW   mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW   Protein transport; Transcription; Translocation; Transport.
FT   CHAIN         1   2243       Protein ELYS.
FT                                /FTId=PRO_0000246320.
FT   DNA_BIND   1955   1967       A.T hook.
FT   REGION        1    981       Necessary for cytoplasmic localization.
FT   REGION     1149   2243       Necessary for nuclear localization.
FT   REGION     1447   1694       Mediates transcriptional activity.
FT   MOD_RES     528    528       Phosphoserine (By similarity).
FT   MOD_RES    1017   1017       N6-acetyllysine (By similarity).
FT   MOD_RES    1087   1087       Phosphoserine (By similarity).
FT   MOD_RES    1142   1142       Phosphoserine (By similarity).
FT   MOD_RES    1150   1150       Phosphoserine (By similarity).
FT   MOD_RES    1155   1155       Phosphoserine (By similarity).
FT   MOD_RES    1175   1175       Phosphothreonine (By similarity).
FT   MOD_RES    1216   1216       Phosphoserine (By similarity).
FT   MOD_RES    1218   1218       Phosphoserine (By similarity).
FT   MOD_RES    1222   1222       Phosphoserine (By similarity).
FT   MOD_RES    1235   1235       Phosphoserine (By similarity).
FT   MOD_RES    1305   1305       Phosphoserine (By similarity).
FT   MOD_RES    1381   1381       Phosphoserine.
FT   MOD_RES    1511   1511       Phosphoserine (By similarity).
FT   MOD_RES    1541   1541       Phosphoserine (By similarity).
FT   MOD_RES    1725   1725       Phosphoserine (By similarity).
FT   MOD_RES    1733   1733       Phosphoserine (By similarity).
FT   MOD_RES    1758   1758       Phosphothreonine (By similarity).
FT   MOD_RES    1864   1864       Phosphoserine (By similarity).
FT   MOD_RES    1870   1870       Phosphoserine (By similarity).
FT   MOD_RES    1884   1884       Phosphoserine (By similarity).
FT   MOD_RES    1928   1928       Phosphoserine (By similarity).
FT   MOD_RES    2099   2099       Phosphoserine (By similarity).
FT   MOD_RES    2132   2132       Phosphoserine (By similarity).
FT   MOD_RES    2188   2188       Phosphoserine (By similarity).
FT   MOD_RES    2198   2198       Phosphoserine (By similarity).
FT   MOD_RES    2202   2202       Phosphoserine (By similarity).
FT   MOD_RES    2215   2215       Phosphothreonine (By similarity).
FT   MOD_RES    2231   2231       Phosphoserine (By similarity).
FT   CONFLICT   1207   1207       F -> L (in Ref. 1; BAB78517).
FT   CONFLICT   1379   1379       A -> T (in Ref. 1; BAB78517).
FT   CONFLICT   1414   1414       A -> G (in Ref. 1; BAB78517).
FT   CONFLICT   1718   1718       H -> R (in Ref. 1; BAB78517).
FT   CONFLICT   2084   2084       T -> A (in Ref. 4; BAC37101).
SQ   SEQUENCE   2243 AA;  247646 MW;  EEEA09B70F2B5691 CRC64;
     MQDLTAQVTS DLLHFPEVTI EALGEDEITL ESVLRGKFAA GKNGLACLAC GPQLEVVNSL
     TGERLSAYRF SGVNEQPPVV LAVKEFSWHK RTGLLIGLEE ADGSVLCLYD LGISRVVKAV
     VLPGRVTAIE PIINHGGASA STQHLHPSLR WLFGVAAVVT DVGQILLIDL CLDDLSCSQN
     EVEASDLEVI TGIPAEVPHI RERVMREGRH LCFQLVSPLG VAISTLSYIN RTNQLAVGFS
     DGYLALWNMK SMKREYYTQL EGGRVPVHAV AFQEPENDPR NCCYLWAVQS TQDSEGDVLS
     LHLLQLAFGD RKCLASGQIL YEGLEYCEER YTLDLAGGTF PLRGQTSNTK LLGCQSIERF
     PSHGDREESM REALSPDTSV SVFTWQVNIY GQGKPSVYLG LFDINRWYHA QMPDSLRSGE
     SLHNCSYFAL WSLDSVVSRT SPHHILDILV HERSLNRGVP PSYPPPEQFF NPSTFNFDAT
     CLLDSGVIHV TCAGFQKETL TFLKKSGPTL NEVIPDSYNR CLVAGLLSPR LIDIQPSSLS
     QEEQLEAILS AAIQTSSLGL LTGYIRTWII EEQPNSAANL RFVLEWTWNK VVLTKEEFDR
     LCVPLFDGSC RFIDPQTIQS IQQCHLLLSN LSTVLSCFAM EAQGITERGL VDLSNKHMVT
     QLLCQYAHMV LWFCHSGLLP EGLDDALQLS RLRYNYPVIQ NYYTSRRQKS ERSPRGKWNH
     DCLMIDGLVS QLGDEVEKLW KRDEGGTGRY PPASIHALLD IYLLDNITEA SKHAITIYLL
     LDIMYSFPNK TDTPIESFPT AFAISWGQVK LVQGFWLLDH NDYENGLDLL FHPVTAKPAS
     WQHSKIIEAF MSQGEHKQAL RYLQTMKPTV SSSNEVILHL TVLLFNRCMV EAWNLLRQNS
     NRVNIEELLK HAYEVCQEMG LMEDLLKLPF TNTEQECLVK FLQSSTSVEN HEFLLVHHLQ
     RANYISALKL NQILKNNLMS DRDPRLRERS VTRNSILDQY GKILPRVQRK LAVERAKPYH
     LSTSSVFHEV SRPKPLSAFP KKAITGTVLT RSTFISNVLS KIGEVWASHE PRNGVSLFNS
     PKTEQPSPVV HSFPHPELPE AFVGTPISNT SQRISRLLDL VVHPVPQPSQ CLEFIQQSPT
     RSPLCLLSSS LPLSSQFKRP HQNTSRPSEL LLLETPLIVK KAKSLALSAT SSGFAEFTPP
     SILRSGFRTT PLASPSLSPG RSLTPPFRVK ETRISFMEEG MNTHWTDRAT DDRNTKAFVS
     TSFHKCGLPA ETEWMKTSDK NTYFPLDVPA KGPQKVVAES LATHSGRLEK LDVSKEDSTA
     STRSDQTSLE YHDAPSPEDL EGAVFVSPKP ASSSTELTTN STLQTERDND KDAFKSEGAP
     SPVKKQIGTG DAAVEAFSEL SRLDPVERAE ASFAVSSVCE GETSTSNSKT SVLDGIVPIE
     SRTSILTADH KESVANTVAD VESSGSTSSK CPVTSERSLG QKLTLNLKED EIEAHVPKEN
     VGLPEESPRI SAAPSDTHEI HLIGCENLEV QNSEEEAKNL SFDELYPLGA EKLEYNLSTI
     EQQFCDLPDD KDSAECDAAE VDGELFVAQS NFTLILEGEE GEAEASDSAA PNMLPKATKE
     KPVCHREPHN QERVTDLPSA VTADQESHKV ETLPYVPEPV KVAIAENLLD VIKDTRSKEA
     TPVAAGEAGD EDGAVIVSKA AHSSRLTNST PKTVKEPHAE TVNTSQNDDM VSSRTLTRRQ
     HALSLNVTSE QEPSAVATPK KRTRKIKETP ESSERTCSDL KVAPENQLTA QSPPAPRRGK
     KKDVSQGTLP SSGAVEPEPE PQGTPGRLRL RTQPPEPAAE ETPSRTKVRL SSVRKGTPRR
     LKKSVENGQS TEILDDLKGS EAASHDGTVT ELRNANLEDT QNMEYKQDEH SDQQLPLKRK
     RVREREVSVS SVTEEPKLDS SQLPLQTGLD VPATPRKRGR PRKVVPLEAD GGTTGKEQTS
     PQKKDVPVVR RSTRNTPARN VSTLEKSVLV PNKEAALVVT SKRRPTKKSA EESSKDPSAA
     VSDLAGGAAH TESADRRDGL LAAAALTPSA QGTRTRSRRT MLLTDISEPK TEPLFPPPSV
     KVPKKKSKAE NMEAAAQLKE LVSDLSSQFV VSPPALRTRQ KSISNTSKLL GELESDPKPL
     EIIEQKPKRS RTVKTRASRN TGKGSSWSPP PVEIKLVSPL ASPVDEIKTG KPRKTAEIAG
     KTLGRGRKKP SSFPKQILRR KML
//
ID   AGO2_MOUSE              Reviewed;         860 AA.
AC   Q8CJG0; Q4VAB3; Q571J6;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Protein argonaute-2;
DE            Short=Argonaute2;
DE            Short=mAgo2;
DE            EC=3.1.26.n2;
DE   AltName: Full=Eukaryotic translation initiation factor 2C 2;
DE            Short=eIF-2C 2;
DE            Short=eIF2C 2;
DE   AltName: Full=Piwi/argonaute family protein meIF2C2;
DE   AltName: Full=Protein slicer;
GN   Name=Eif2c2; Synonyms=Ago2, Kiaa4215;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12526743; DOI=10.1016/S0960-9822(02)01394-5;
RA   Doi N., Zenno S., Ueda R., Ohki-Hamazaki H., Ui-Tei K., Saigo K.;
RT   "Short-interfering-RNA-mediated gene silencing in mammalian cells
RT   requires Dicer and eIF2C translation initiation factors.";
RL   Curr. Biol. 13:41-46(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=B5/EGFP; TISSUE=Trophoblast stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 158-860.
RC   TISSUE=Embryonic tail;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=15284456; DOI=10.1126/science.1102513;
RA   Liu J., Carmell M.A., Rivas F.V., Marsden C.G., Thomson J.M.,
RA   Song J.-J., Hammond S.M., Joshua-Tor L., Hannon G.J.;
RT   "Argonaute2 is the catalytic engine of mammalian RNAi.";
RL   Science 305:1437-1441(2004).
RN   [5]
RP   INTERACTION WITH DICER1 AND TARBP2.
RX   PubMed=16357216; DOI=10.1101/gad.1384005;
RA   Maniataki E., Mourelatos Z.;
RT   "A human, ATP-independent, RISC assembly machine fueled by pre-
RT   miRNA.";
RL   Genes Dev. 19:2979-2990(2005).
RN   [6]
RP   NITRATION [LARGE SCALE ANALYSIS] AT TYR-2, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16800626; DOI=10.1021/bi060474w;
RA   Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
RA   Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
RA   Squier T.C., Bigelow D.J.;
RT   "Endogenously nitrated proteins in mouse brain: links to
RT   neurodegenerative disease.";
RL   Biochemistry 45:8009-8022(2006).
RN   [7]
RP   FUNCTION.
RX   PubMed=17626790; DOI=10.1101/gad.1565607;
RA   O'Carroll D., Mecklenbrauker I., Das P.P., Santana A., Koenig U.,
RA   Enright A.J., Miska E.A., Tarakhovsky A.;
RT   "A Slicer-independent role for Argonaute 2 in hematopoiesis and the
RT   microRNA pathway.";
RL   Genes Dev. 21:1999-2004(2007).
RN   [8]
RP   FUNCTION.
RX   PubMed=19174539; DOI=10.1101/gad.1749809;
RA   Su H., Trombly M.I., Chen J., Wang X.;
RT   "Essential and overlapping functions for mammalian Argonautes in
RT   microRNA silencing.";
RL   Genes Dev. 23:304-317(2009).
CC   -!- FUNCTION: Required for RNA-mediated gene silencing (RNAi) by the
CC       RNA-induced silencing complex (RISC). The 'minimal RISC' appears
CC       to include EIF2C2/AGO2 bound to a short guide RNA such as a
CC       microRNA (miRNA) or short interfering RNA (siRNA). These guide
CC       RNAs direct RISC to complementary mRNAs that are targets for RISC-
CC       mediated gene silencing. The precise mechanism of gene silencing
CC       depends on the degree of complementarity between the miRNA or
CC       siRNA and its target. Binding of RISC to a perfectly complementary
CC       mRNA generally results in silencing due to endonucleolytic
CC       cleavage of the mRNA specifically by EIF2C2/AGO2. Binding of RISC
CC       to a partially complementary mRNA results in silencing through
CC       inhibition of translation, and this is independent of endonuclease
CC       activity. May inhibit translation initiation by binding to the 7-
CC       methylguanosine cap, thereby preventing the recruitment of the
CC       translation initiation factor eIF4-E. May also inhibit translation
CC       initiation via interaction with EIF6, which itself binds to the
CC       60S ribosomal subunit and prevents its association with the 40S
CC       ribosomal subunit. The inhibition of translational initiation
CC       leads to the accumulation of the affected mRNA in cytoplasmic
CC       processing bodies (P-bodies), where mRNA degradation may
CC       subsequently occur. In some cases RISC-mediated translational
CC       repression is also observed for miRNAs that perfectly match the 3'
CC       untranslated region (3'-UTR). May also upregulate the translation
CC       of specific mRNAs under certain growth conditions. Binds to the AU
CC       element of the 3'-UTR of the TNF (TNF-alpha) mRNA and upregulates
CC       translation under conditions of serum starvation. May also be
CC       required for transcriptional gene silencing (TGS), in which short
CC       RNAs known as antigene RNAs or agRNAs direct the transcriptional
CC       repression of complementary promoter regions. Regulates lymphoid
CC       and erythroid development and function, and this is independent of
CC       endonuclease activity.
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
CC       phosphomonoester.
CC   -!- SUBUNIT: Interacts with EIF2C1/AGO1. Also interacts with DDB1,
CC       DDX6, DDX20, DDX47, DHX9, DHX36, EIF6, FXR1, GEMIN4, ILF3, MOV10,
CC       PRMT5, P4HA1, P4HB, SART3, TNRC6A, TNRC6B and UPF1. Interacts with
CC       the P-body components DCP1A and XRN1 (By similarity). Interacts
CC       with DICER1 through its Piwi domain and with TARBP2 during
CC       assembly of the RNA-induced silencing complex (RISC). Together,
CC       DICER1, EIF2C2/AGO2 and TARBP2 constitute the trimeric RISC
CC       loading complex (RLC), or micro-RNA (miRNA) loading complex
CC       (miRLC). Within the RLC/miRLC, DICER1 and TARBP2 are required to
CC       process precursor miRNAs (pre-miRNAs) to mature miRNAs and then
CC       load them onto EIF2C2/AGO2. EIF2C2/AGO2 bound to the mature miRNA
CC       constitutes the minimal RISC and may subsequently dissociate from
CC       DICER1 and TARBP2. Note however that the term RISC has also been
CC       used to describe the trimeric RLC/miRLC. The formation of RISC
CC       complexes containing siRNAs rather than miRNAs appears to occur
CC       independently of DICER1.
CC   -!- INTERACTION:
CC       Q9UPY3:DICER1 (xeno); NbExp=2; IntAct=EBI-528299, EBI-395506;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body (By similarity). Nucleus
CC       (By similarity). Note=Translational repression of mRNAs results in
CC       their recruitment to P-bodies. Translocation to the nucleus
CC       requires IMP8 (By similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitous expression in 9.5 day embryos with
CC       highest levels in forebrain, heart, limb buds, and branchial
CC       arches.
CC   -!- DOMAIN: The Piwi domain may perform RNA cleavage by a mechanism
CC       similar to that of RNase H. However while RNase H utilizes a triad
CC       of Asp-Asp-Glu (DDE) for metal ion coordination, this protein
CC       appears to utilize a triad of Asp-Asp-His (DDH) (By similarity).
CC   -!- PTM: Hydroxylated. 4-hydroxylation appears to enhance protein
CC       stability but is not required for miRNA-binding or endonuclease
CC       activity (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Embryonic death with a strong defect in
CC       neural tube closure and apparent cardiac failure.
CC   -!- SIMILARITY: Belongs to the argonaute family. Ago subfamily.
CC   -!- SIMILARITY: Contains 1 PAZ domain.
CC   -!- SIMILARITY: Contains 1 Piwi domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH96465.1; Type=Erroneous initiation;
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DR   EMBL; AB081472; BAC15767.1; -; mRNA.
DR   EMBL; BC096465; AAH96465.1; ALT_INIT; mRNA.
DR   EMBL; AK220193; BAD90378.1; -; mRNA.
DR   IPI; IPI00229988; -.
DR   RefSeq; NP_694818.3; NM_153178.4.
DR   UniGene; Mm.274482; -.
DR   ProteinModelPortal; Q8CJG0; -.
DR   SMR; Q8CJG0; 223-390, 441-575.
DR   DIP; DIP-35014N; -.
DR   IntAct; Q8CJG0; 3.
DR   STRING; Q8CJG0; -.
DR   PhosphoSite; Q8CJG0; -.
DR   PRIDE; Q8CJG0; -.
DR   Ensembl; ENSMUST00000044113; ENSMUSP00000042207; ENSMUSG00000036698.
DR   GeneID; 239528; -.
DR   KEGG; mmu:239528; -.
DR   CTD; 239528; -.
DR   MGI; MGI:2446632; Eif2c2.
DR   HOGENOM; HBG717005; -.
DR   InParanoid; Q8CJG0; -.
DR   OrthoDB; EOG4229J0; -.
DR   NextBio; 384151; -.
DR   ArrayExpress; Q8CJG0; -.
DR   Bgee; Q8CJG0; -.
DR   CleanEx; MM_EIF2C2; -.
DR   Genevestigator; Q8CJG0; -.
DR   GermOnline; ENSMUSG00000036698; Mus musculus.
DR   GO; GO:0000932; C:cytoplasmic mRNA processing body; IEA:UniProtKB-SubCell.
DR   GO; GO:0035068; C:micro-ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0005845; C:mRNA cap binding complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016442; C:RNA-induced silencing complex; ISS:UniProtKB.
DR   GO; GO:0070551; F:endoribonuclease activity, cleaving siRNA-paired mRNA; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0000340; F:RNA 7-methylguanosine cap binding; ISS:UniProtKB.
DR   GO; GO:0035197; F:siRNA binding; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0035279; P:mRNA cleavage involved in gene silencing by miRNA; ISS:UniProtKB.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0035278; P:negative regulation of translation involved in gene silencing by miRNA; ISS:UniProtKB.
DR   GO; GO:0045947; P:negative regulation of translational initiation; ISS:UniProtKB.
DR   GO; GO:0031054; P:pre-microRNA processing; ISS:UniProtKB.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR014811; DUF1785.
DR   InterPro; IPR003100; PAZ.
DR   InterPro; IPR003165; Piwi.
DR   InterPro; IPR012337; RNaseH-like.
DR   Pfam; PF08699; DUF1785; 1.
DR   Pfam; PF02170; PAZ; 1.
DR   Pfam; PF02171; Piwi; 1.
DR   SMART; SM00949; PAZ; 1.
DR   SMART; SM00950; Piwi; 1.
DR   SUPFAM; SSF101690; PAZ; 1.
DR   SUPFAM; SSF53098; RNaseH_fold; 1.
DR   PROSITE; PS50821; PAZ; 1.
DR   PROSITE; PS50822; PIWI; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Developmental protein; Differentiation; Endonuclease;
KW   Hydrolase; Hydroxylation; Metal-binding; Nitration; Nuclease; Nucleus;
KW   Repressor; Ribonucleoprotein; RNA-binding;
KW   RNA-mediated gene silencing; Transcription; Transcription regulation;
KW   Translation regulation.
FT   CHAIN         1    860       Protein argonaute-2.
FT                                /FTId=PRO_0000194058.
FT   DOMAIN      236    349       PAZ.
FT   DOMAIN      518    819       Piwi.
FT   METAL       598    598       Divalent metal cation (By similarity).
FT   METAL       670    670       Divalent metal cation (By similarity).
FT   METAL       808    808       Divalent metal cation (By similarity).
FT   MOD_RES       2      2       Nitrated tyrosine.
FT   MOD_RES     701    701       4-hydroxyproline (By similarity).
FT   CONFLICT     65     65       E -> G (in Ref. 2; AAH96465).
FT   CONFLICT     67     67       R -> C (in Ref. 2; AAH96465).
FT   CONFLICT    129    129       L -> F (in Ref. 2; AAH96465).
FT   CONFLICT    360    360       N -> D (in Ref. 1; BAC15767).
FT   CONFLICT    563    563       N -> D (in Ref. 2; AAH96465).
FT   CONFLICT    711    711       R -> P (in Ref. 2; AAH96465).
FT   CONFLICT    761    761       S -> G (in Ref. 1; BAC15767).
SQ   SEQUENCE   860 AA;  97323 MW;  8E73A345E9E3DD9D CRC64;
     MYSGAGPVLA SPAPTTSPIP GYAFKPPPRP DFGTTGRTIK LQANFFEMDI PKIDIYHYEL
     DIKPEKRPRR VNREIVEHMV QHFKTQIFGD RKPVFDGRKN LYTAMPLPIG RDKVELEVTL
     PGEGKDRILK VSIKWVSCVS LQALHDALSG RLPSVPFETI QALDVVMRHL PSMRYTPVGR
     SFFTASEGCS NPLGGGREVW FGFHQSVRPS LWKMMLNIDV SATAFYKAQP VIEFVCEVLD
     FKSIEEQQKP LTDSQRVKFT KEIKGLKVEI THCGQMKRKY RVCNVTRRPA SHQTFPLQQE
     SGQTVECTVA QYFKDRHKLV LRYPHLPCLQ VGQEQKHTYL PLEVCNIVAG QRCIKKLTDN
     QTSTMIRATA RSAPDRQEEI SKLMRSASFN TDPYVREFGI MVKDEMTDVT GRVLQPPSIL
     YGGRNKAIAT PVQGVWDMRN KQFHTGIEIK VWAIACFAPQ RQCTEVHLKS FTEQLRKISR
     DAGMPIQGQP CFCKYAQGAD SVEPMFRHLK NTYAGLQLVV VILPGKTPVY AEVKRVGDTV
     LGMATQCVQM KNVQRTTPQT LSNLCLKINV KLGGVNNILL PQGRPPVFQQ PVIFLGADVT
     HPPAGDGKKP SIAAVVGSMD AHPNRYCATV RVQQHRQEII QDLAAMVREL LIQFYKSTRF
     KPTRIIFYRD GVSEGQFQQV LHHELLAIRE ACIKLEKDYQ PGITFIVVQK RHHTRLFCTD
     KNERVGKSGN IPAGTTVDTK ITHPTEFDFY LCSHAGIQGT SRPSHYHVLW DDNRFSSDEL
     QILTYQLCHT YVRCTRSVSI PAPAYYAHLV AFRARYHLVD KEHDSAEGSH TSGQSNGRDH
     QALAKAVQVH QDTLRTMYFA
//
ID   PLXB1_MOUSE             Reviewed;        2119 AA.
AC   Q8CJH3; Q6ZQC3; Q80ZZ1;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Plexin-B1;
DE   Flags: Precursor;
GN   Name=Plxnb1; Synonyms=Kiaa0407;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH
RP   PLXNA1.
RC   TISSUE=Brain;
RX   PubMed=12559962; DOI=10.1016/S0006-291X(02)02966-2;
RA   Usui H., Taniguchi M., Yokomizo T., Shimizu T.;
RT   "Plexin-A1 and plexin-B1 specifically interact at their cytoplasmic
RT   domains.";
RL   Biochem. Biophys. Res. Commun. 300:927-931(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 913-2119.
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1885-2119.
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-543 AND ASN-1251, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Receptor for SEMA4D. Plays a role in RHOA activation and
CC       subsequent changes of the actin cytoskeleton. Plays a role in axon
CC       guidance, invasive growth and cell migration (By similarity).
CC   -!- SUBUNIT: Monomer, and heterodimer with PLXNB2 after proteolytic
CC       processing. Binds RAC1 that has been activated by GTP binding.
CC       Interaction with SEMA4D promotes binding of cytoplasmic ligands.
CC       Interacts with RRAS, ARHGEF11, ARHGEF12, ERBB2, MET, MST1R, RND1,
CC       RHOD, NRP1 and NRP2 (By similarity). Binds PLXNA1.
CC   -!- INTERACTION:
CC       Q04912:MST1R (xeno); NbExp=1; IntAct=EBI-2637650, EBI-2637518;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Detected in brain, heart, lung, liver, kidney,
CC       stomach, testis, uterus and placenta.
CC   -!- PTM: Phosphorylated on tyrosine residues by ERBB2 and MET upon
CC       SEMA4D binding (By similarity).
CC   -!- PTM: Proteolytic processing favors heterodimerization with PLXNB2
CC       and SEMA4D binding (By similarity).
CC   -!- SIMILARITY: Belongs to the plexin family.
CC   -!- SIMILARITY: Contains 3 IPT/TIG domains.
CC   -!- SIMILARITY: Contains 1 Sema domain.
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DR   EMBL; AB072381; BAC22660.1; -; mRNA.
DR   EMBL; AK129133; BAC97943.1; -; mRNA.
DR   EMBL; BC043322; AAH43322.1; -; mRNA.
DR   IPI; IPI00229992; -.
DR   RefSeq; NP_766363.2; NM_172775.2.
DR   UniGene; Mm.53862; -.
DR   ProteinModelPortal; Q8CJH3; -.
DR   SMR; Q8CJH3; 25-669, 1013-1250, 1498-2115.
DR   IntAct; Q8CJH3; 1.
DR   MINT; MINT-1791147; -.
DR   STRING; Q8CJH3; -.
DR   PhosphoSite; Q8CJH3; -.
DR   PRIDE; Q8CJH3; -.
DR   Ensembl; ENSMUST00000072093; ENSMUSP00000071966; ENSMUSG00000053646.
DR   GeneID; 235611; -.
DR   KEGG; mmu:235611; -.
DR   UCSC; uc009rrz.1; mouse.
DR   CTD; 235611; -.
DR   MGI; MGI:2154238; Plxnb1.
DR   eggNOG; roNOG05992; -.
DR   GeneTree; ENSGT00600000084313; -.
DR   HOGENOM; HBG716170; -.
DR   HOVERGEN; HBG053404; -.
DR   InParanoid; Q8CJH3; -.
DR   OrthoDB; EOG40K7XZ; -.
DR   NextBio; 382789; -.
DR   ArrayExpress; Q8CJH3; -.
DR   Bgee; Q8CJH3; -.
DR   CleanEx; MM_PLXNB1; -.
DR   Genevestigator; Q8CJH3; -.
DR   GermOnline; ENSMUSG00000053646; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0002116; C:semaphorin receptor complex; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0017154; F:semaphorin receptor activity; ISS:UniProtKB.
DR   GO; GO:0050772; P:positive regulation of axonogenesis; IGI:MGI.
DR   GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR   GO; GO:0051493; P:regulation of cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISS:UniProtKB.
DR   InterPro; IPR015716; CD2_adhesion_molc.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002909; IPT_TIG_rcpt.
DR   InterPro; IPR003659; Plexin-like.
DR   InterPro; IPR016201; Plexin-like_fold.
DR   InterPro; IPR013548; Plexin_cytoplasmic_RasGAP_dom.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR001936; RasGAP.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR001627; Semaphorin/CD100_Ag.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 4.
DR   Gene3D; G3DSA:1.10.506.10; RasGAP; 1.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   PANTHER; PTHR22625:SF10; Plxnb1; 1.
DR   Pfam; PF08337; Plexin_cytopl; 1.
DR   Pfam; PF01437; PSI; 1.
DR   Pfam; PF01403; Sema; 1.
DR   Pfam; PF01833; TIG; 3.
DR   SMART; SM00429; IPT; 3.
DR   SMART; SM00423; PSI; 3.
DR   SMART; SM00630; Sema; 1.
DR   SUPFAM; SSF81296; Ig_E-set; 3.
DR   SUPFAM; SSF103575; Plexin-like_fold; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   SUPFAM; SSF101912; Sema; 1.
DR   PROSITE; PS51004; SEMA; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Glycoprotein; Membrane; Phosphoprotein; Receptor; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     19       Potential.
FT   CHAIN        20   2119       Plexin-B1.
FT                                /FTId=PRO_0000024672.
FT   TOPO_DOM     20   1474       Extracellular (Potential).
FT   TRANSMEM   1475   1495       Helical; (Potential).
FT   TOPO_DOM   1496   2119       Cytoplasmic (Potential).
FT   DOMAIN       20    479       Sema.
FT   DOMAIN     1068   1158       IPT/TIG 1.
FT   DOMAIN     1160   1247       IPT/TIG 2.
FT   DOMAIN     1250   1359       IPT/TIG 3.
FT   COILED     1492   1523       Potential.
FT   COMPBIAS    678    835       Pro-rich.
FT   SITE       1799   1799       Important for interaction with RAC1 and
FT                                RND1 (By similarity).
FT   CARBOHYD     31     31       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     74     74       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    334    334       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    349    349       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    543    543       N-linked (GlcNAc...).
FT   CARBOHYD   1251   1251       N-linked (GlcNAc...).
FT   CARBOHYD   1314   1314       N-linked (GlcNAc...) (Potential).
FT   CONFLICT   1777   1777       P -> L (in Ref. 2; BAC97943).
SQ   SEQUENCE   2119 AA;  231361 MW;  08FAFDE425B455AD CRC64;
     MSVLGPVLLQ VFWAGCVVTL RSPLPAAFTA NGTHLLHLAR DPTTGTLYVG ATNFLFQLSP
     GLQLEAVVST GPVNDSRDCL PPVIPDECPQ AQPTNNPNQL LLVSPEALVV CGSVHQGICE
     LRSLGQIRQL LLRPERPGDT QYVAANDPAV STVGLVAQGL VGEPLLFVGR GYTSRGVGGG
     IPPITTRALR PPDPQAAFSY EETAKLAVGR LSEYSHHFVS AFVRGASAYF LFLRRDLKAP
     SRAFRAYVSR VCLQDQHYYS YVELPLACQG GRYGLIQAAA VATSKEVARG DVLFAAFSSV
     APPTVDWPLS ASTGASGTSV LCAFPLDEVD QLANYTRDAC YTREGRAENG TKVADIAYDV
     LSDCAQLPVD TPDAFPCGSD HTPSPMVSCV PLEATPILEL PGVQLTAVAV TMEDGHTIAF
     LGDSQGQLHR VYLGPGRSAA PYSKQSIQPG SPVNRDLTFD GTFEHLYVAT QTTLVKVPVA
     PCAQHLDCDS CLAHRDPYCG WCVLLGRCSR RSECSRDQGP EQWLWSFQPE LGCLRVVAVS
     PANISREERR EVFLSVPGLP SLWPGESYFC YFGDQQSPAL LTSSGVMCPS PDPSEAPVLQ
     RGADHISVNV ELRFGAVVIA STSLSFYDCV AVTASSPSAP CRACVSSRWG CNWCVWQQLC
     THKASCDAGP MVASQQSPLL PLIPPARDEL TPFPPTVPQT TVTPTPNSFP IEPRAPSTAS
     DVLPGAKPSR LSLWGPWAGP GPILSPTSTE SPLHEKPLPP DPPTIPGTTV PAPTGLGPST
     TPEDLLASYP FPSDAAAVSP AEPGPEALPS MVALDQPPGT VPDTTFPGAP GSMKPVLDWL
     TKGGGELPEA DEWMGGDTPA FSTSTLLSGD GDSAEHEGPP APLILLSSLD YQYDTPGLWE
     LGEVNQRVSS CPCVETVQGS LLIPVHVERE VQLRGRNLWL FQDGPRSSEC VLELGSREVA
     VEAQVECAPP PDVWCHIKCQ QHQFSYEALK PELQVGLFLR WAGGLRVDSA DGLHVVLYDC
     SVGHGDCSRC QTAMPQYDCV WCEGERPRCV AREACNEAET VATQCPAPLI HSVDPLTGPI
     DGGTRVTIRG SNLGQHVQDV LDMVRVAGVP CAVDAGEYDV SSSLVCITGA SGEEVTGTVA
     VEVPGRGHGV SEFSFAYQDP KVHSIFPARG PRAGGTRLTL HGSKLLTGRL EDIRVVVGDQ
     PCHLLLEQQS EQLHCETGPY PVPAELPVTV LFGATERRLQ HGQFKYTSDP NVTSVGPSKS
     FFSGGREIWV RGQDLDVVQR PRIRVTVVPR QHGQGLAQKQ HVVPEKFEEP CLVNSSHLLM
     CRTPALPGPP WDSGVQVEFI LDNMVFDFAA LSPTPFSYEA DPTLRSLNPE DPSTPFRHKP
     GSVFSVEGEN LDLAMSKEEV VAMIGDGPCV VKTLTRNHLY CEPPVEQPLP HPHALREAPD
     ALPEFTVQMG NLRFSLGHVQ YDGESPVAFP VAAQVGLGVG TSLLALGVII IVLIYRRKSK
     QALRDYKKVQ IQLENLESSV RDRCKKEFTD LMTEMTDLTS DLLGSGIPFL DYKVYAERVF
     FPGYRESPLH RDLGVPDSRR PTVEQGLGQL SNLLNSKLFL TKFIHTLESQ RTFSARDRAY
     VASLLTVALH GKLEYFTDIL RTLLSDLVAQ YVAKNPKLML RRTETVVEKL LTNWMSICLY
     TFVRDSVGEP LYMLFRGIKH QVDKGPVDSV TGKAKYTLND NRLLREDVEY RPLTLNALLA
     VGPGAGEAQC VPVKVLDCDT ISQAKEKMLD QLYKGVPLAQ RPDSCTLDVE WRSGVAGHLI
     LSDEDVTSEL QGLWRRLNTL QHYKVPDGAT VALVPCLTKH ILRENQDYVP GERTPMLEDV
     DEGGIRPWHL VKPSDEPEPP RPRRGSLRGG ERERAKAIPE IYLTRLLSMK GTLQKFVDDL
     FQVILSTSRP VPLAVKYFFD LLDEQAQQHG ISDQDTIHIW KTNSLPLRFW INIIKNPQFV
     FDVQTSDNMD AVLLVIAQTF MDACTLADHK LGRDSPINKL LYARDIPRYK QMVERYYADI
     RQTVPASDQE MNSVLAELSR NCSADLGARV ALHELYKYIN KYYDQIITAL EEDGTAQKMQ
     LGYRLQQIAA AVENKVTDL
//
ID   DNER_MOUSE              Reviewed;         737 AA.
AC   Q8JZM4; Q3U697; Q8R226; Q8R4T6; Q8VD97;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Delta and Notch-like epidermal growth factor-related receptor;
DE   AltName: Full=Brain EGF repeat-containing transmembrane protein;
DE   Flags: Precursor;
GN   Name=Dner; Synonyms=Bet, Bret;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-677, AND INTERACTION WITH
RP   AP1G1.
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=22095525; PubMed=11950833; DOI=10.1074/jbc.M110793200;
RA   Eiraku M., Hirata Y., Takeshima H., Hirano T., Kengaku M.;
RT   "Delta/notch-like epidermal growth factor (EGF)-related receptor, a
RT   novel EGF-like repeat-containing protein targeted to dendrites of
RT   developing and adult central nervous system neurons.";
RL   J. Biol. Chem. 277:25400-25407(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   MEDLINE=21993226; PubMed=11997712;
RX   DOI=10.1097/00001756-200205070-00035;
RA   Nishizumi H., Komiyama T., Miyabayashi T., Sakano S., Sakano H.;
RT   "BET, a novel neuronal transmembrane protein with multiple EGF-like
RT   motifs.";
RL   NeuroReport 13:909-915(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH NOTCH1, AND FUNCTION.
RX   PubMed=15965470; DOI=10.1038/nn1492;
RA   Eiraku M., Tohgo A., Ono K., Kaneko M., Fujishima K., Hirano T.,
RA   Kengaku M.;
RT   "DNER acts as a neuron-specific Notch ligand during Bergmann glial
RT   development.";
RL   Nat. Neurosci. 8:873-880(2005).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16298139; DOI=10.1016/j.mcn.2005.10.003;
RA   Tohgo A., Eiraku M., Miyazaki T., Miura E., Kawaguchi S.Y., Nishi M.,
RA   Watanabe M., Hirano T., Kengaku M., Takeshima H.;
RT   "Impaired cerebellar functions in mutant mice lacking DNER.";
RL   Mol. Cell. Neurosci. 31:326-333(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-711; TYR-718 AND
RP   TYR-721, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Mediates neuron-glia interaction during
CC       astrocytogenesis. May promote differentiation of Bergmann glia
CC       during cerebellar development by activating DELTEX-dependent
CC       NOTCH1 signaling.
CC   -!- SUBUNIT: Interacts with AP1G1. Interacts with NOTCH1.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Note=Present on the membrane of dendrites and cell bodies
CC       but excluded from axonal membrane. Also found in early endosomes
CC       in the somatodendritic region.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in brain neurons (at
CC       protein level).
CC   -!- DEVELOPMENTAL STAGE: Expression in the central nervous system
CC       starts at E11, peaks during postnatal development and declines in
CC       the adult brain. At P7 and P20, present in several types of post-
CC       mitotic neurons, including cortical and hippocampal pyramidal
CC       neurons, cerebellar granule cells and Purkinje cells. Absent from
CC       mitotic neuroblasts in the ventricular zones.
CC   -!- PTM: N-glycosylated.
CC   -!- DISRUPTION PHENOTYPE: Mice show no obvious abnormality and no
CC       apparent survival disadvantage. However they have delayed
CC       cerebellar histogenesis and exhibit motor discoordination at adult
CC       stages.
CC   -!- SIMILARITY: Contains 10 EGF-like domains.
CC   -!- SIMILARITY: Contains 1 follistatin-like domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE31470.1; Type=Frameshift; Positions=631;
CC       Sequence=BAE31828.1; Type=Frameshift; Positions=631;
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DR   EMBL; AY032924; AAK50342.1; -; mRNA.
DR   EMBL; AF370126; AAM14419.1; -; mRNA.
DR   EMBL; AB067650; BAB72175.1; -; mRNA.
DR   EMBL; AK044597; BAC31995.1; -; mRNA.
DR   EMBL; AK152755; BAE31470.1; ALT_FRAME; mRNA.
DR   EMBL; AK153235; BAE31828.1; ALT_FRAME; mRNA.
DR   EMBL; BC022636; AAH22636.1; -; mRNA.
DR   EMBL; BC034634; AAH34634.1; -; mRNA.
DR   IPI; IPI00170342; -.
DR   RefSeq; NP_690879.1; NM_152915.1.
DR   UniGene; Mm.292560; -.
DR   HSSP; P00740; 1EDM.
DR   ProteinModelPortal; Q8JZM4; -.
DR   SMR; Q8JZM4; 45-171, 314-622.
DR   STRING; Q8JZM4; -.
DR   PhosphoSite; Q8JZM4; -.
DR   PRIDE; Q8JZM4; -.
DR   Ensembl; ENSMUST00000049126; ENSMUSP00000042927; ENSMUSG00000036766.
DR   GeneID; 227325; -.
DR   KEGG; mmu:227325; -.
DR   UCSC; uc007bsw.1; mouse.
DR   CTD; 227325; -.
DR   MGI; MGI:2152889; Dner.
DR   eggNOG; roNOG04449; -.
DR   GeneTree; ENSGT00600000084071; -.
DR   HOGENOM; HBG280485; -.
DR   HOVERGEN; HBG060866; -.
DR   InParanoid; Q8JZM4; -.
DR   OMA; KWDQVEV; -.
DR   OrthoDB; EOG4M65H0; -.
DR   PhylomeDB; Q8JZM4; -.
DR   NextBio; 378548; -.
DR   ArrayExpress; Q8JZM4; -.
DR   Bgee; Q8JZM4; -.
DR   CleanEx; MM_DNER; -.
DR   Genevestigator; Q8JZM4; -.
DR   GermOnline; ENSMUSG00000036766; Mus musculus.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005112; F:Notch binding; IPI:MGI.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0010001; P:glial cell differentiation; IDA:MGI.
DR   GO; GO:0007220; P:Notch receptor processing; IDA:MGI.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0048741; P:skeletal muscle fiber development; IDA:MGI.
DR   InterPro; IPR006209; EGF.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR001881; EGF_Ca-bd.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR013111; EGF_extracell.
DR   Pfam; PF00008; EGF; 7.
DR   Pfam; PF07974; EGF_2; 2.
DR   SMART; SM00181; EGF; 7.
DR   SMART; SM00179; EGF_CA; 3.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS00022; EGF_1; 10.
DR   PROSITE; PS01186; EGF_2; 7.
DR   PROSITE; PS50026; EGF_3; 10.
DR   PROSITE; PS01187; EGF_CA; 2.
PE   1: Evidence at protein level;
KW   Activator; Calcium; Cell membrane; Developmental protein;
KW   Differentiation; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Membrane; Notch signaling pathway; Phosphoprotein; Receptor; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     25       Potential.
FT   CHAIN        26    737       Delta and Notch-like epidermal growth
FT                                factor-related receptor.
FT                                /FTId=PRO_0000253558.
FT   TOPO_DOM     26    640       Extracellular (Potential).
FT   TRANSMEM    641    661       Helical; (Potential).
FT   TOPO_DOM    662    737       Cytoplasmic (Potential).
FT   DOMAIN       44     92       EGF-like 1.
FT   DOMAIN       94    133       EGF-like 2.
FT   DOMAIN      309    348       EGF-like 3.
FT   DOMAIN      349    390       EGF-like 4.
FT   DOMAIN      392    428       EGF-like 5.
FT   DOMAIN      430    466       EGF-like 6.
FT   DOMAIN      468    503       EGF-like 7.
FT   DOMAIN      505    541       EGF-like 8; calcium-binding (Potential).
FT   DOMAIN      543    579       EGF-like 9.
FT   DOMAIN      581    617       EGF-like 10; calcium-binding (Potential).
FT   REGION       44    133       Interaction with NOTCH1.
FT   REGION      677    680       Interaction with AP1G1 and
FT                                somatodendritic targeting.
FT   MOD_RES     711    711       Phosphotyrosine.
FT   MOD_RES     718    718       Phosphotyrosine.
FT   MOD_RES     721    721       Phosphotyrosine.
FT   CARBOHYD    204    204       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    564    564       N-linked (GlcNAc...) (Potential).
FT   DISULFID     48     59       By similarity.
FT   DISULFID     53     80       By similarity.
FT   DISULFID     82     91       By similarity.
FT   DISULFID     98    108       By similarity.
FT   DISULFID    103    121       By similarity.
FT   DISULFID    123    132       By similarity.
FT   DISULFID    319    336       By similarity.
FT   DISULFID    338    347       By similarity.
FT   DISULFID    353    364       By similarity.
FT   DISULFID    358    378       By similarity.
FT   DISULFID    380    389       By similarity.
FT   DISULFID    396    407       By similarity.
FT   DISULFID    401    416       By similarity.
FT   DISULFID    418    427       By similarity.
FT   DISULFID    434    445       By similarity.
FT   DISULFID    439    454       By similarity.
FT   DISULFID    456    465       By similarity.
FT   DISULFID    472    482       By similarity.
FT   DISULFID    477    491       By similarity.
FT   DISULFID    493    502       By similarity.
FT   DISULFID    509    520       By similarity.
FT   DISULFID    514    529       By similarity.
FT   DISULFID    531    540       By similarity.
FT   DISULFID    547    558       By similarity.
FT   DISULFID    552    567       By similarity.
FT   DISULFID    569    578       By similarity.
FT   DISULFID    585    596       By similarity.
FT   DISULFID    590    605       By similarity.
FT   DISULFID    607    616       By similarity.
FT   MUTAGEN     677    677       Y->A: Fails to be restricted to the
FT                                somatodendritic compartment.
FT   CONFLICT    424    424       G -> A (in Ref. 2; BAB72175).
FT   CONFLICT    509    510       CL -> SV (in Ref. 1; AAM14419).
SQ   SEQUENCE   737 AA;  78747 MW;  8C85694EB7420756 CRC64;
     MPPRRAQAPG APLLPVLALL PLLLGAGPQS GCLASPVSAA PLPAPGPCAS QPCRNGGVCT
     PRSVTDQEHP AADAEPRYSC TCPAGVSGTY CQFVADPCAS NPCHHGNCSS SSSSSSDSYL
     CICNDGYEGL NCEQPLPSIP TSGWTESTAP RQLQPVPATQ EPDIILPRSQ ATVTLPTWQP
     KTGQKVVEMK WDQVEVVPDV ACGNASSNNS AGGRLVSFEV PQNTSVKIRQ DANSLLILLW
     KVTATGFQQC SLIDGRSVTP LQAPGGLVLL EEMLALGPNH FIGFVNDSVA KSIVALRLTL
     VVKASNCVPG DSHSNDLECS GKGKCATKPS EATFSCTCQD QYIGTFCEEF DACQRKPCQN
     EASCIDANEK QDGSNFTCLC LPGYTGELCQ SKIDYCVLDP CRNGATCVSS LSGFTCQCLE
     GYFGSACEEK VDPCMSSPCQ NNGTCYVDGV HFTCSCSPGF TGPTCAQLVD FCALSPCAHG
     MCRSVGTSYK CLCDPGYHGL YCEEEYNECL SAPCLNAATC RDLINGYECV CLAEYKGTHC
     ELYKDPCANI SCLNGGTCDS EGLNGTCICA PGFTGEECDI DINECDSNPC HHAGTCLDQP
     NGYTCHCPHG WVGANCEIHL QWKSGHMAES LTNMPRHSLY IIIGALCVAF ILMLIILIVG
     ICRISRIEYQ GSSRPAYEEF YNCRSIDSEF SNAIASIRHA RFGKKSRPAM YDVTPIAYED
     YSPDDKPLVT LIKTKDL
//
ID   SYN3_MOUSE              Reviewed;         579 AA.
AC   Q8JZP2;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Synapsin-3;
DE   AltName: Full=Synapsin III;
GN   Name=Syn3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ILS, and ISS;
RX   MEDLINE=21363810; PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-461 AND SER-469, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: May be involved in the regulation of neurotransmitter
CC       release and synaptogenesis. Binds ATP with high affinity and ADP
CC       with a lower affinity. This is consistent with a catalytic role of
CC       the C-domain in which ADP would be dissociated by cellular ATP
CC       after bound ATP was hydrolyzed (By similarity).
CC   -!- SUBUNIT: Interacts with CAPON (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity). Note=Peripheral membrane protein
CC       localized to the cytoplasmic surface of synaptic vesicles (By
CC       similarity).
CC   -!- MISCELLANEOUS: Regulated by calcium. Calcium inhibits ATP binding
CC       to the C-domain (By similarity).
CC   -!- SIMILARITY: Belongs to the synapsin family.
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DR   EMBL; AF498252; AAM22969.1; -; mRNA.
DR   EMBL; AF498253; AAM22970.1; -; mRNA.
DR   IPI; IPI00463761; -.
DR   UniGene; Mm.394931; -.
DR   UniGene; Mm.441038; -.
DR   UniGene; Mm.444790; -.
DR   ProteinModelPortal; Q8JZP2; -.
DR   SMR; Q8JZP2; 90-395.
DR   STRING; Q8JZP2; -.
DR   PRIDE; Q8JZP2; -.
DR   Ensembl; ENSMUST00000077267; ENSMUSP00000076499; ENSMUSG00000059602.
DR   Ensembl; ENSMUST00000120638; ENSMUSP00000113720; ENSMUSG00000059602.
DR   UCSC; uc007gno.1; mouse.
DR   MGI; MGI:1351334; Syn3.
DR   HOGENOM; HBG445598; -.
DR   HOVERGEN; HBG016354; -.
DR   InParanoid; Q8JZP2; -.
DR   OrthoDB; EOG4KPTB4; -.
DR   ArrayExpress; Q8JZP2; -.
DR   Bgee; Q8JZP2; -.
DR   CleanEx; MM_SYN3; -.
DR   Genevestigator; Q8JZP2; -.
DR   GermOnline; ENSMUSG00000059602; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0007269; P:neurotransmitter secretion; IEA:InterPro.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR013817; Pre-ATP_grasp.
DR   InterPro; IPR016185; PreATP-grasp-like.
DR   InterPro; IPR001359; Synapsin.
DR   InterPro; IPR020898; Synapsin_ATP-bd_dom.
DR   InterPro; IPR019735; Synapsin_CS.
DR   InterPro; IPR019736; Synapsin_P_site.
DR   InterPro; IPR020897; Synapsin_pre-ATP-grasp_dom.
DR   Gene3D; G3DSA:3.30.1490.20; ATP_grasp_subdomain_1; 1.
DR   Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 2.
DR   Gene3D; G3DSA:3.40.50.20; Pre-ATP_grasp; 1.
DR   Pfam; PF02078; Synapsin; 1.
DR   Pfam; PF02750; Synapsin_C; 1.
DR   Pfam; PF10581; Synapsin_N; 1.
DR   PRINTS; PR01368; SYNAPSIN.
DR   SUPFAM; SSF52440; PreATP-grasp-like; 1.
DR   PROSITE; PS00415; SYNAPSIN_1; 1.
DR   PROSITE; PS00416; SYNAPSIN_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Calcium; Cell junction; Cytoplasmic vesicle; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Synapse.
FT   CHAIN         1    579       Synapsin-3.
FT                                /FTId=PRO_0000183025.
FT   REGION        1     28       A.
FT   REGION       28     90       B; linker.
FT   REGION       91    398       C; actin-binding and synaptic-vesicle
FT                                binding.
FT   REGION      399    530       J; Pro-rich linker.
FT   REGION      531    579       E.
FT   MOD_RES     461    461       Phosphoserine.
FT   MOD_RES     469    469       Phosphoserine.
FT   MOD_RES     483    483       Phosphoserine.
SQ   SEQUENCE   579 AA;  63345 MW;  2B84E6B283A3D50F CRC64;
     MNFLRRRLSD SSFVANLPNG YMPDLQRPES SSSSPASPAT ERRHPQPLAA SFSSPGSSLF
     SSFSSAMKQT PQAPSGLMEP PTPVTPVVQR PRILLVIDDA HTDWSKYFHG KKVNGDIEIR
     VEQAEFSELN LAAYVTGGCM VDMQVVRNGT KIVRSFKPDF ILVRQHAYSM ALAEDYRSLV
     IGLQYGGLPA VNSLYSVYNF CSKPWVFSQL IKIFHSLGPE KFPLVEQTFF PNHKPMLTAP
     NFPVVIKLGH AHAGMGKIKV ENQHDYQDIT SVVAMAKTYA TTEAFIDSKY DIRIQKIGSN
     YKAYMRTSIS GNWKANTGSA MLEQVAMTER YRLWVDSCSE MFGGLDICAV KAVHSKDGRD
     YIIEVMDSSM PLIGEHVEED KQLMADLVVS KMSQLLVPGA TVPSPLRPWG PQTKPAKSPG
     QGQLGPLLGQ PQPRPPPQGG PRQAQSPQPP RSRSPSQQRL SPQGQQPVSP QSGSPQQQRS
     PGSPQLSRAS GGSSPNQASK PSASLSSHNR PPVQGRSTSQ QGEEPQKSAS PHPHLNKSQS
     LTNSLSTSDT SHRGTPSEDE AKAETIRNLR KSFASLFSD
//
ID   GA2L1_MOUSE             Reviewed;         678 AA.
AC   Q8JZP9; Q5SVG0; Q8K573;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=GAS2-like protein 1;
DE   AltName: Full=Growth arrest-specific protein 2-like 1;
GN   Name=Gas2l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=22472147; PubMed=12584248; DOI=10.1242/jcs.00272;
RA   Goriounov D., Leung C.L., Liem R.K.;
RT   "Protein products of human Gas2-related genes on chromosomes 17 and 22
RT   (hGAR17 and hGAR22) associate with both microfilaments and
RT   microtubules.";
RL   J. Cell Sci. 116:1045-1058(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Seems to be involved in the cross-linking of
CC       microtubules and microfilaments (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Beta;
CC         IsoId=Q8JZP9-1; Sequence=Displayed;
CC       Name=2; Synonyms=Alpha;
CC         IsoId=Q8JZP9-2; Sequence=VSP_015496;
CC   -!- SIMILARITY: Belongs to the GAS2 family.
CC   -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC   -!- SIMILARITY: Contains 1 GAR domain.
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DR   EMBL; AF508323; AAM34262.1; -; mRNA.
DR   EMBL; AF508324; AAM34263.1; -; mRNA.
DR   EMBL; AL645522; CAI25940.1; -; Genomic_DNA.
DR   EMBL; AL645522; CAI25941.1; -; Genomic_DNA.
DR   EMBL; BC031785; AAH31785.1; -; mRNA.
DR   IPI; IPI00134843; -.
DR   IPI; IPI00338961; -.
DR   RefSeq; NP_001177337.1; NM_001190408.1.
DR   RefSeq; NP_653146.1; NM_144560.3.
DR   UniGene; Mm.374836; -.
DR   UniGene; Mm.44591; -.
DR   ProteinModelPortal; Q8JZP9; -.
DR   SMR; Q8JZP9; 20-157, 202-281.
DR   STRING; Q8JZP9; -.
DR   PhosphoSite; Q8JZP9; -.
DR   PRIDE; Q8JZP9; -.
DR   Ensembl; ENSMUST00000037146; ENSMUSP00000043709; ENSMUSG00000034201.
DR   Ensembl; ENSMUST00000056649; ENSMUSP00000050275; ENSMUSG00000034201.
DR   Ensembl; ENSMUST00000109895; ENSMUSP00000105521; ENSMUSG00000034201.
DR   GeneID; 78926; -.
DR   KEGG; mmu:78926; -.
DR   UCSC; uc007hvt.1; mouse.
DR   UCSC; uc007hvu.1; mouse.
DR   CTD; 78926; -.
DR   MGI; MGI:1926176; Gas2l1.
DR   eggNOG; maNOG18544; -.
DR   GeneTree; ENSGT00390000002205; -.
DR   HOGENOM; HBG713558; -.
DR   HOVERGEN; HBG079404; -.
DR   InParanoid; Q8JZP9; -.
DR   OMA; WVPRGRG; -.
DR   OrthoDB; EOG4C2H9T; -.
DR   PhylomeDB; Q8JZP9; -.
DR   NextBio; 349776; -.
DR   ArrayExpress; Q8JZP9; -.
DR   Bgee; Q8JZP9; -.
DR   CleanEx; MM_GAS2L1; -.
DR   Genevestigator; Q8JZP9; -.
DR   GermOnline; ENSMUSG00000034201; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0007050; P:cell cycle arrest; IEA:InterPro.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR003108; GAS2_dom.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 1.
DR   Gene3D; G3DSA:3.30.920.20; GAS2_dom; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF02187; GAS2; 1.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00243; GAS2; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS51460; GAR; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Cytoskeleton; Phosphoprotein.
FT   CHAIN         1    678       GAS2-like protein 1.
FT                                /FTId=PRO_0000190443.
FT   DOMAIN       27    147       CH.
FT   DOMAIN      203    275       GAR.
FT   COMPBIAS    379    462       Arg-rich.
FT   MOD_RES     297    297       Phosphoserine (By similarity).
FT   MOD_RES     306    306       Phosphoserine (By similarity).
FT   MOD_RES     352    352       Phosphoserine (By similarity).
FT   MOD_RES     384    384       Phosphoserine (By similarity).
FT   MOD_RES     394    394       Phosphoserine (By similarity).
FT   MOD_RES     436    436       Phosphoserine (By similarity).
FT   MOD_RES     438    438       Phosphoserine (By similarity).
FT   MOD_RES     493    493       Phosphoserine (By similarity).
FT   MOD_RES     501    501       Phosphothreonine (By similarity).
FT   VAR_SEQ     338    678       Missing (in isoform 2).
FT                                /FTId=VSP_015496.
SQ   SEQUENCE   678 AA;  72411 MW;  067DCB47F5F1A3A7 CRC64;
     MANPVAGIAG SAAKSVRPFR SSEAYVEAMK EDLADWLNAL YSLGLPGSGD GFLTGLATGT
     TLCQHANAVT EAARALAAAR PTRGVAFQAH SVAPGSFMAR DNVASFIGWC RAELGVPEVL
     MFETEDLVLR KNEKSVVLCL LEVARRGARL GLLAPRLVQF EQEIERELRA TPQVSSVPAA
     EEDVTEIATV PGVPTRTPRM TPNDLRNLDE LVREILGRCT CPDQFPMIKV SEGKYRVGDS
     SLLIFVRVLR SHVMVRVGGG WDTLEHYLDK HDPCRCSSST HRLPQQRTGT FSPQRGSPTP
     SPRPGSPVPG SERRSSRPEV TPISLRGTKE GPETPLRPRD QLPPLPRSRR YSGDSDSSAS
     SAQSGPMGAR SDDSATGSRR ERPSHRPTSC LPASPRRPTA PRSQSRDRLD RGRPRVAPGG
     RGAQLSTSSP ARRTRSQSRE EQAVLMVRRD RDGQHSWVAR GRGGGGSGGS GRSTPQTPRA
     LSPAAPRPSR GPSPGPELAA TPASIFRTPL QLDPQQEQQL FRRLEEEFLA NARALEAAAS
     HTPMGSAPDP PAPDSAYCSS SSSSSSLSVL GGKCGQPGES GRTANGLPGP RSQALSSSSD
     EGSPYLAVGG ALDATRSSLA GPEPSLTWAR GRMDTQPDRK PSRIPTPRGP RRPSGPIELG
     AWHAQHSVTP RTEPDSSM
//
ID   AFG32_MOUSE             Reviewed;         802 AA.
AC   Q8JZQ2;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=AFG3-like protein 2;
DE            EC=3.4.24.-;
GN   Name=Afg3l2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 173-181; 283-296 AND 632-650, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [3]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-307 AND LYS-542, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
RN   [4]
RP   FUNCTION, AND VARIANT PAR GLY-389.
RX   PubMed=18337413; DOI=10.1523/JNEUROSCI.4677-07.2008;
RA   Maltecca F., Aghaie A., Schroeder D.G., Cassina L., Taylor B.A.,
RA   Phillips S.J., Malaguti M., Previtali S., Guenet J.L., Quattrini A.,
RA   Cox G.A., Casari G.;
RT   "The mitochondrial protease AFG3L2 is essential for axonal
RT   development.";
RL   J. Neurosci. 28:2827-2836(2008).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=20208537; DOI=10.1038/ng.544;
RA   Di Bella D., Lazzaro F., Brusco A., Plumari M., Battaglia G.,
RA   Pastore A., Finardi A., Cagnoli C., Tempia F., Frontali M.,
RA   Veneziano L., Sacco T., Boda E., Brussino A., Bonn F., Castellotti B.,
RA   Baratta S., Mariotti C., Gellera C., Fracasso V., Magri S., Langer T.,
RA   Plevani P., Di Donato S., Muzi-Falconi M., Taroni F.;
RT   "Mutations in the mitochondrial protease gene AFG3L2 cause dominant
RT   hereditary ataxia SCA28.";
RL   Nat. Genet. 42:313-321(2010).
CC   -!- FUNCTION: ATP-dependent protease which is essential for axonal
CC       development.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (Potential).
CC   -!- SUBUNIT: Homooligomer.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane
CC       protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in the cerebellar Purkinje
CC       cells.
CC   -!- DISEASE: Note=Defects in Afg3l2 are the cause of the paralyze
CC       (par) phenotype, a spontaneous mutant strain. Par mice have a
CC       normal appearance and fertility but are significantly smaller than
CC       their littermates at 1 week of age and display a rapidly
CC       progressive loss of motor function in all limbs by 12-14 days. As
CC       the disease progresses, they lose the ability to support their own
CC       weight or turn themselves over when placed on their back and
CC       exhibit a typical posture with over extension of all limbs and
CC       uncoordinated movements. They rarely survive beyond 16 days of
CC       age, when they are completely paralyzed.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC       family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidase
CC       M41 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; BC036999; AAH36999.1; -; mRNA.
DR   EMBL; BC043056; AAH43056.1; -; mRNA.
DR   IPI; IPI00170357; -.
DR   RefSeq; NP_081406.1; NM_027130.1.
DR   UniGene; Mm.426052; -.
DR   ProteinModelPortal; Q8JZQ2; -.
DR   SMR; Q8JZQ2; 294-752.
DR   STRING; Q8JZQ2; -.
DR   MEROPS; M41.007; -.
DR   PhosphoSite; Q8JZQ2; -.
DR   PRIDE; Q8JZQ2; -.
DR   Ensembl; ENSMUST00000025408; ENSMUSP00000025408; ENSMUSG00000024527.
DR   GeneID; 69597; -.
DR   KEGG; mmu:69597; -.
DR   UCSC; uc008fmf.1; mouse.
DR   CTD; 69597; -.
DR   MGI; MGI:1916847; Afg3l2.
DR   HOGENOM; HBG724153; -.
DR   HOVERGEN; HBG050184; -.
DR   InParanoid; Q8JZQ2; -.
DR   OMA; QIPVLYK; -.
DR   OrthoDB; EOG4SBDXC; -.
DR   PhylomeDB; Q8JZQ2; -.
DR   NextBio; 329880; -.
DR   ArrayExpress; Q8JZQ2; -.
DR   Bgee; Q8JZQ2; -.
DR   CleanEx; MM_AFG3L2; -.
DR   Genevestigator; Q8JZQ2; -.
DR   GermOnline; ENSMUSG00000024527; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR   GO; GO:0016265; P:death; IMP:MGI.
DR   GO; GO:0042552; P:myelination; IMP:MGI.
DR   GO; GO:0021675; P:nerve development; IMP:MGI.
DR   GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
DR   GO; GO:0030163; P:protein catabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
DR   GO; GO:0060013; P:righting reflex; IMP:MGI.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR005936; Pept_M41_FtsH.
DR   InterPro; IPR011546; Pept_M41_FtsH_extracell.
DR   InterPro; IPR000642; Peptidase_M41.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF06480; FtsH_ext; 1.
DR   Pfam; PF01434; Peptidase_M41; 1.
DR   SMART; SM00382; AAA; 1.
DR   TIGRFAMs; TIGR01241; FtsH_fam; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Direct protein sequencing; Disease mutation;
KW   Hydrolase; Membrane; Metal-binding; Metalloprotease; Mitochondrion;
KW   Nucleotide-binding; Protease; Transmembrane; Transmembrane helix;
KW   Zinc.
FT   CHAIN         1    802       AFG3-like protein 2.
FT                                /FTId=PRO_0000084674.
FT   TRANSMEM    142    162       Helical; (Potential).
FT   TRANSMEM    250    270       Helical; (Potential).
FT   NP_BIND     347    354       ATP (Potential).
FT   ACT_SITE    574    574       By similarity.
FT   METAL       573    573       Zinc; catalytic (By similarity).
FT   METAL       577    577       Zinc; catalytic (By similarity).
FT   METAL       648    648       Zinc; catalytic (By similarity).
FT   MOD_RES     305    305       N6-acetyllysine (By similarity).
FT   MOD_RES     307    307       N6-acetyllysine.
FT   MOD_RES     542    542       N6-acetyllysine.
FT   VARIANT     389    389       R -> G (in par).
SQ   SEQUENCE   802 AA;  89519 MW;  E7300BD686532D2D CRC64;
     MAHRCLLLWS RGGCRRGLPP LLVPRGCLGP DRRPCLRTLY QYATVQTASS RRSLLRDVIA
     AYQRFCSRPP KGFEKYFPNG KNGKKASEPK EAVGEKKEPQ PSGPQPSGGA GGGGGKRRGK
     KEDSHWWSRF QKGDFPWDDK DFRMYFLWTA LFWGGVMIYF VFKSSGREIT WKDFVNNYLS
     KGVVDRLEVV NKRFVRVTFT PGKTPVDGQY VWFNIGSVDT FERNLETLQQ ELGIEGENRV
     PVVYIAESDG SFLLSMLPTV LIIAFLLYTI RRGPAGIGRT GRGMGGLFSV GETTAKVLKD
     EIDVKFKDVA GCEEAKLEIM EFVNFLKNPK QYQDLGAKIP KGAILTGPPG TGKTLLAKAT
     AGEANVPFIT VSGSEFLEMF VGVGPARVRD LFALARKNAP CILFIDEIDA VGRKRGRGNF
     GGQSEQENTL NQLLVEMDGF NTTTNVVILA GTNRPDILDP ALLRPGRFDR QIFIGPPDIK
     GRASIFKVHL RPLKLDSALE KDKLARKLAS LTPGFSGADV ANVCNEAALI AARHLSDAIN
     EKHFEQAIER VIGGLEKKTQ VLQPEEKKTV AYHEAGHAVA GWYLEHADPL LKVSIIPRGK
     GLGYAQYLPK EQYLYTKEQL LDRMCMTLGG RVSEEIFFGR ITTGAQDDLR KVTQSAYAQI
     VQFGMNEKVG QISFDLPRQG DMVLEKPYSE ATARMIDDEV RILISDAYRR TVALLTEKKA
     DVEKVALLLL EKEVLDKNDM VQLLGPRPFT EKSTYEEFVE GTGSLDEDTS LPEGLQDWNK
     EREKEEKKEK EKEEPLNEKV VS
//
ID   EIF3B_MOUSE             Reviewed;         803 AA.
AC   Q8JZQ9; Q922K2;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit B;
DE            Short=eIF3b;
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 9;
DE   AltName: Full=eIF-3-eta;
DE   AltName: Full=eIF3 p116;
GN   Name=Eif3b; Synonyms=Eif3s9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Embryonic stem cell;
RX   MEDLINE=22035555; PubMed=12038979;
RA   Koyanagi-Katsuta R., Akimitsu N., Hamamoto H., Arimitsu N., Hatano T.,
RA   Sekimizu K.;
RT   "Embryonic lethality of mutant mice deficient in the p116 gene.";
RL   J. Biochem. 131:833-837(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Cecum, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   INTERACTION WITH EIF3A; EIF3F; EIF3J; EIF4A1; EIF4B; EIF4E; EIF4G1 AND
RP   RPS6.
RX   PubMed=16541103; DOI=10.1038/sj.emboj.7601047;
RA   Harris T.E., Chi A., Shabanowitz J., Hunt D.F., Rhoads R.E.,
RA   Lawrence J.C. Jr.;
RT   "mTOR-dependent stimulation of the association of eIF4G and eIF3 by
RT   insulin.";
RL   EMBO J. 25:1659-1668(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   CHARACTERIZATION OF THE EIF-3 COMPLEX, IDENTIFICATION IN THE EIF-3
RP   COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17581632; DOI=10.1038/sj.emboj.7601765;
RA   Masutani M., Sonenberg N., Yokoyama S., Imataka H.;
RT   "Reconstitution reveals the functional core of mammalian eIF3.";
RL   EMBO J. 26:3373-3383(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-440, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-123, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; THR-74; SER-75;
RP   SER-79; SER-90; SER-120 AND SER-123, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-120 AND SER-123,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-123, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-79, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74; SER-75; SER-79;
RP   SER-120 AND SER-123, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Component of the eukaryotic translation initiation
CC       factor 3 (eIF-3) complex, which is required for several steps in
CC       the initiation of protein synthesis. The eIF-3 complex associates
CC       with the 40S ribosome and facilitates the recruitment of eIF-1,
CC       eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S
CC       preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA
CC       recruitment to the 43S PIC and scanning of the mRNA for AUG
CC       recognition. The eIF-3 complex is also required for disassembly
CC       and recycling of posttermination ribosomal complexes and
CC       subsequently prevents premature joining of the 40S and 60S
CC       ribosomal subunits prior to initiation.
CC   -!- SUBUNIT: Interacts with UPF2 (By similarity). Component of the
CC       eukaryotic translation initiation factor 3 (eIF-3) complex, which
CC       is composed of 13 subunits: EIF3A, EIF3B, EIF3C, EIF3D, EIF3E,
CC       EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K, EIF3L and EIF3M. The
CC       eIF-3 complex appears to include 3 stable modules: module A is
CC       composed of EIF3A, EIF3B, EIF3G and EIF3I; module B is composed of
CC       EIF3F, EIF3H, and EIF3M; and module C is composed of EIF3C, EIF3D,
CC       EIF3E, EIF3K and EIF3L. EIF3C of module C binds EIF3B of module A
CC       and EIF3H of module B, thereby linking the three modules. EIF3J is
CC       a labile subunit that binds to the eIF-3 complex via EIF3B. The
CC       eIF-3 complex may also interact with RPS6KB1 under conditions of
CC       nutrient depletion. Mitogenic stimulation may lead to binding and
CC       activation of a complex composed of MTOR and RPTOR, leading to
CC       phosphorylation and release of RPS6KB1 and binding of EIF4B to
CC       eIF-3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- DOMAIN: The RRM domain mediates interaction with EIF3J (By
CC       similarity).
CC   -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
CC       stimulation (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Embryonic death.
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit B family.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -!- SIMILARITY: Contains 5 WD repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK033722; BAC28445.1; -; mRNA.
DR   EMBL; AK167618; BAE39671.1; -; mRNA.
DR   EMBL; AK170938; BAE42128.1; -; mRNA.
DR   EMBL; BC007175; AAH07175.1; -; mRNA.
DR   EMBL; BC031704; AAH31704.1; -; mRNA.
DR   IPI; IPI00229859; -.
DR   PIR; JC7862; JC7862.
DR   RefSeq; NP_598677.1; NM_133916.2.
DR   UniGene; Mm.21671; -.
DR   ProteinModelPortal; Q8JZQ9; -.
DR   SMR; Q8JZQ9; 159-263, 327-428, 454-494, 621-659.
DR   MINT; MINT-1899500; -.
DR   STRING; Q8JZQ9; -.
DR   PRIDE; Q8JZQ9; -.
DR   Ensembl; ENSMUST00000100507; ENSMUSP00000098076; ENSMUSG00000056076.
DR   GeneID; 27979; -.
DR   KEGG; mmu:27979; -.
DR   UCSC; uc009ahr.1; mouse.
DR   CTD; 27979; -.
DR   MGI; MGI:106478; Eif3b.
DR   GeneTree; ENSGT00550000074913; -.
DR   HOVERGEN; HBG006127; -.
DR   NextBio; 306472; -.
DR   ArrayExpress; Q8JZQ9; -.
DR   Bgee; Q8JZQ9; -.
DR   Genevestigator; Q8JZQ9; -.
DR   GermOnline; ENSMUSG00000056076; Mus musculus.
DR   GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR011400; eIF3b.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR013979; TIF2A_beta_prop_like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   Gene3D; G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 1.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   PANTHER; PTHR14068; eIF3b; 1.
DR   Pfam; PF08662; eIF2A; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PIRSF; PIRSF036424; eIF3b; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50102; RRM; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR   PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Initiation factor; Phosphoprotein;
KW   Protein biosynthesis; Repeat; RNA-binding; WD repeat.
FT   CHAIN         1    803       Eukaryotic translation initiation factor
FT                                3 subunit B.
FT                                /FTId=PRO_0000223479.
FT   DOMAIN      174    257       RRM.
FT   REPEAT      321    359       WD 1.
FT   REPEAT      361    406       WD 2.
FT   REPEAT      410    448       WD 3.
FT   REPEAT      549    590       WD 4.
FT   REPEAT      638    683       WD 5.
FT   REGION      113    402       Sufficient for interaction with EIF3E (By
FT                                similarity).
FT   REGION      159    263       Sufficient for interaction with EIF3J (By
FT                                similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      31     31       Phosphothreonine.
FT   MOD_RES      68     68       Phosphoserine.
FT   MOD_RES      74     74       Phosphothreonine.
FT   MOD_RES      75     75       Phosphoserine.
FT   MOD_RES      79     79       Phosphoserine.
FT   MOD_RES      90     90       Phosphoserine.
FT   MOD_RES     120    120       Phosphoserine.
FT   MOD_RES     123    123       Phosphoserine.
FT   MOD_RES     141    141       Phosphoserine (By similarity).
FT   MOD_RES     143    143       Phosphoserine (By similarity).
FT   MOD_RES     153    153       Phosphoserine (By similarity).
FT   MOD_RES     198    198       N6-acetyllysine (By similarity).
FT   MOD_RES     228    228       Phosphoserine (By similarity).
FT   MOD_RES     277    277       N6-acetyllysine (By similarity).
FT   MOD_RES     353    353       N6-acetyllysine (By similarity).
FT   MOD_RES     425    425       N6-acetyllysine (By similarity).
FT   MOD_RES     440    440       Phosphothreonine.
FT   MOD_RES     514    514       Phosphotyrosine (By similarity).
SQ   SEQUENCE   803 AA;  91370 MW;  D770AC70BFE9832F CRC64;
     MQDAENVAVP EAAEERAEPA RQQPASESPP TDEAAGSGGS EVGQTEDAEE DAEAGPEPEV
     RAKPAAQSEE ETATSPAASP TPQSAERSPS QEPSAPGKAE AVGEQARGHP SAGAEEEGGS
     DGSAAEAEPR ALENGEADEP SFSDPEDFVD DVSEEELLGD VLKDRPQEAD GIDSVIVVDN
     VPQVGPDRLE KLKNVIHKIF SKFGKIINDY YPEEDGKTKG YIFLEYASPA HAVDAVKNAD
     GYKLDKQHTF RVNLFTDFDK YMTISDEWDI PEKQPFKDLG NLRYWLEEAE CRDQYSVIFE
     SGDRTSIFWN DVKDPVSIEE RARWTETYVR WSPKGTYLAT FHQRGIALWG GDKFKQIQRF
     SHQGVQLIDF SPCERYLVTF SPLMDTQDDP QAIIIWDILT GHKKRGFHCE SSAHWPIFKW
     SHDGKFFARM TLDTLSIYET PSMGLLDKKS LKISGIKDFS WSPGGNIIAF WVPEDKDIPA
     RVTLMQLPTR QEIRVRNLFN VVDCKLHWQK NGDYLCVKVD RTPKGTQGVV TNFEIFRMRE
     KQVPVDVVEM KETIIAFAWE PNGSKFAVLH GEAPRISVSF YHVKSNGKIE LIKMFDKQQA
     NTIFWSPQGQ FVVLAGLRSM NGALAFVDTS DCTVMNIAEH YMASDVEWDP TGRYVVTSVS
     WWSHKVDNAY WLWTFQGRLL QKNNKDRFCQ LLWRPRPPTL LSQDQIKQIK KDLKKYSKIF
     EQKDRLSQSK ASKELVERRR TMMEDFRQYR KMAQELYMKQ KNERLELRGG VDTDELDSNV
     DDWEEETIEF FVTEEVIPLG SQE
//
ID   S4A8_MOUSE              Reviewed;        1089 AA.
AC   Q8JZR6; Q3TAV7; Q6A004; Q8BYI7; Q9JKV6;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Electroneutral sodium bicarbonate exchanger 1;
DE   AltName: Full=Electroneutral Na+-driven Cl-HCO3 exchanger;
DE   AltName: Full=Solute carrier family 4 member 8;
DE   AltName: Full=k-NBC3;
GN   Name=Slc4a8; Synonyms=Kiaa0739;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP   AND INHIBITION.
RC   TISSUE=Kidney inner medulla;
RX   MEDLINE=21160130; PubMed=11260402;
RX   DOI=10.1046/j.1523-1755.2001.0590041405.x;
RA   Wang Z., Conforti L., Petrovic S., Amlal H., Burnham C.E.,
RA   Soleimani M.;
RT   "Mouse Na+: HCO3- cotransporter isoform NBC-3 (kNBC-3): cloning,
RT   expression, and renal distribution.";
RL   Kidney Int. 59:1405-1414(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Dendritic cell, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Mediates electroneutral sodium- and carbonate-dependent
CC       choride-HCO3(-) exchange with a Na(+):HCO3(-) stoichiometry of
CC       2:1. Plays a major role in pH regulation in neurons. May be
CC       involved in cell pH regulation by transporting HCO3(-) from blood
CC       to cell. Enhanced expression in severe acid stress could be
CC       important for cell survival by mediating the influx of HCO3(-)
CC       into the cells. Also mediates lithium-dependent HCO3(-)
CC       cotransport. May be regulated by osmolarity.
CC   -!- ENZYME REGULATION: Activity is inhibited by 4,4'-Di-
CC       isothiocyanatostilbene-2,2'-disulfonic acid (DIDS - an inhibitor
CC       of several anion channels and transporters).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8JZR6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8JZR6-2; Sequence=VSP_052769;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain with lower levels in
CC       lung, kidney and heart. In the kidney, there is high expression in
CC       the inner medulla, localized to the inner medullary collecting
CC       duct. In the brain, there seems to be three transcripts each
CC       having a different expression pattern. The smaller 3kb transcript
CC       has highest expression levels in the thalamus and the largest
CC       9.5kb transcript has highest levels in the substantia nigra. The
CC       middle transcript of 4.4kb, which is also the main transcript in
CC       kidney, is highly expressed in thalamus. Hence, the highest levels
CC       are observed in the thalamus, amygdala and caudate nucleus and
CC       very low expression was seen in the corpus callosum.
CC   -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32292.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF224508; AAF61705.1; -; mRNA.
DR   EMBL; AK039404; BAC30341.1; -; mRNA.
DR   EMBL; AK171610; BAE42561.1; -; mRNA.
DR   EMBL; AK173014; BAD32292.1; ALT_INIT; mRNA.
DR   EMBL; BC030388; AAH30388.1; -; mRNA.
DR   IPI; IPI00323442; -.
DR   IPI; IPI00890144; -.
DR   RefSeq; NP_067505.2; NM_021530.2.
DR   UniGene; Mm.209856; -.
DR   HSSP; P02730; 1BZK.
DR   ProteinModelPortal; Q8JZR6; -.
DR   SMR; Q8JZR6; 114-426, 460-501, 920-952.
DR   PhosphoSite; Q8JZR6; -.
DR   PRIDE; Q8JZR6; -.
DR   Ensembl; ENSMUST00000023776; ENSMUSP00000023776; ENSMUSG00000023032.
DR   GeneID; 59033; -.
DR   KEGG; mmu:59033; -.
DR   NMPDR; fig|10090.3.peg.30646; -.
DR   UCSC; uc007xse.1; mouse.
DR   CTD; 59033; -.
DR   MGI; MGI:1928745; Slc4a8.
DR   eggNOG; roNOG09504; -.
DR   GeneTree; ENSGT00560000076851; -.
DR   HOGENOM; HBG355640; -.
DR   HOVERGEN; HBG004326; -.
DR   InParanoid; Q8JZR6; -.
DR   OMA; MTAILKF; -.
DR   OrthoDB; EOG45B1DS; -.
DR   NextBio; 314630; -.
DR   ArrayExpress; Q8JZR6; -.
DR   Bgee; Q8JZR6; -.
DR   Genevestigator; Q8JZR6; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR011531; HCO3_transpt_C.
DR   InterPro; IPR013769; HCO3_transpt_cyt.
DR   InterPro; IPR003020; HCO3_transpt_euk.
DR   InterPro; IPR003024; Na/HCO3_transpt.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   Gene3D; G3DSA:3.40.1100.10; HCO3_transpt_cyt; 1.
DR   PANTHER; PTHR11453; HCO3_transpt_euk; 1.
DR   Pfam; PF07565; Band_3_cyto; 1.
DR   Pfam; PF00955; HCO3_cotransp; 1.
DR   PRINTS; PR01231; HCO3TRNSPORT.
DR   PRINTS; PR01232; NAHCO3TRSPRT.
DR   SUPFAM; SSF55804; PTrfase/Anion_transptr; 1.
DR   TIGRFAMs; TIGR00834; ae; 1.
DR   PROSITE; PS00219; ANION_EXCHANGER_1; FALSE_NEG.
DR   PROSITE; PS00220; ANION_EXCHANGER_2; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Anion exchange; Antiport; Ion transport;
KW   Membrane; Phosphoprotein; Sodium; Sodium transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1   1089       Electroneutral sodium bicarbonate
FT                                exchanger 1.
FT                                /FTId=PRO_0000328923.
FT   TOPO_DOM      1    476       Extracellular (Potential).
FT   TRANSMEM    477    497       Helical; (Potential).
FT   TOPO_DOM    498    505       Cytoplasmic (Potential).
FT   TRANSMEM    506    526       Helical; (Potential).
FT   TOPO_DOM    527    563       Extracellular (Potential).
FT   TRANSMEM    564    584       Helical; (Potential).
FT   TOPO_DOM    585    593       Cytoplasmic (Potential).
FT   TRANSMEM    594    614       Helical; (Potential).
FT   TOPO_DOM    615    685       Extracellular (Potential).
FT   TRANSMEM    686    706       Helical; (Potential).
FT   TOPO_DOM    707    729       Cytoplasmic (Potential).
FT   TRANSMEM    730    750       Helical; (Potential).
FT   TOPO_DOM    751    776       Extracellular (Potential).
FT   TRANSMEM    777    797       Helical; (Potential).
FT   TOPO_DOM    798    822       Cytoplasmic (Potential).
FT   TRANSMEM    823    843       Helical; (Potential).
FT   TOPO_DOM    844    879       Extracellular (Potential).
FT   TRANSMEM    880    900       Helical; (Potential).
FT   TOPO_DOM    901    902       Cytoplasmic (Potential).
FT   TRANSMEM    903    923       Helical; (Potential).
FT   TOPO_DOM    924    960       Extracellular (Potential).
FT   TRANSMEM    961    981       Helical; (Potential).
FT   TOPO_DOM    982   1089       Cytoplasmic (Potential).
FT   COMPBIAS   1021   1026       Poly-Glu.
FT   MOD_RES     237    237       Phosphoserine (By similarity).
FT   VAR_SEQ       1     52       Missing (in isoform 2).
FT                                /FTId=VSP_052769.
FT   CONFLICT    219    219       K -> E (in Ref. 2; BAE42561).
FT   CONFLICT    258    258       V -> M (in Ref. 1; AAF61705).
FT   CONFLICT    291    291       K -> R (in Ref. 2; BAE42561).
FT   CONFLICT    644    644       N -> S (in Ref. 2; BAC30341).
FT   CONFLICT    707    707       S -> P (in Ref. 1; AAF61705).
FT   CONFLICT    949    949       K -> E (in Ref. 2; BAE42561).
FT   CONFLICT   1015   1015       D -> G (in Ref. 2; BAC30341).
SQ   SEQUENCE   1089 AA;  122421 MW;  CFAE127D3853DDD8 CRC64;
     MPAGSNEPDG VLSYQRPDEE AVVDQGGTST ILNIHYEKEE LEGHRTLYVG VRMPLGRQSH
     RHHRTHGQKH RRRGGRGKGA SQGEEGLEAL AHDTPSQRVQ FILGTEEDEE HVPHELFTEL
     DEICMKEGED AEWKETARWL KFEEDVEDGG ERWSKPYVAT LSLHSLFELR SCLINGSVLL
     DMRASSIEEI SDLILDQQEL LRDLSDSVRV KVREALLKKH HHQNERRRNN LIPIVRSFAE
     VGKKQSDPHS MDRDGQTVSP QSATNLEVKN GVNCEHSPVD LSKVDLHFMK KIPTGAEASN
     VLVGEVDTLD RPIVAFVRLS PAVLLSGLTE VPIPTRFLFI LLGPVGKGQQ YHEIGRSMAT
     IMTDEIFHDV AYKAKERDDL LAGIDEFLDQ VTVLPPGEWD PSIRIEPPKN VPSQEKRKMP
     GVPNGNVCHI EPEPHGGHSG PELERTGRLF GGLVLDVKRK APWYWSDYRD ALSLQCLASF
     LFLYCACMSP VITFGGLLGE ATEGRISAIE SLFGASMTGI AYSLFAGQPL TILGSTGPVL
     VFEKILFKFC KDYALSYLSL RALIGLWTAF LCIVLVATDA SSLVCYITRF TEEAFASLIC
     IIFIYEAIEK LIHLAETYPI HMHSQLDHLS LYYCRCVLPE NPNNHTLQYW KDHNILAAEV
     NWANLTVSEC QEMHGEFMGS ACGHHGPYTP DVLFWSCILF FATFIVSSTL KTFKTSRYFP
     TRVRSMVSDF AVFLTIFTMV VLDFLIGVPS PKLQVPNVFK PTRDDRGWFI NPIGPNPWWT
     VIAAIIPALL CTILIFMDQQ ITAVIINRKE HKLKKGCGYH LDLLMVAVML GVCSIMGLPW
     FVAATVLSIT HVNSLKLESE CSAPGEQPKF LGIREQRVTG LMIFVLMGCS VFMTAVLKFI
     PMPVLYGVFL YMGVSSLQGI QFFDRLKLFG MPAKHQPDFI YLRHVPLRKV HLFTLVQLTC
     LVLLWVIKAS PAAIVFPMMV LALVFVRKVM DLCFSKRELS WLDDLMPESK KKKLDDAKKK
     EEEEAEKMLD IGGDKFPLES RKLLSSPGKS SSFRCDPSEI NISDEMPKTT VWKALSINSG
     NTKEKSPFN
//
ID   LIN7A_MOUSE             Reviewed;         233 AA.
AC   Q8JZS0;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Protein lin-7 homolog A;
DE            Short=Lin-7A;
DE            Short=mLin-7;
DE   AltName: Full=Mammalian lin-seven protein 1;
DE            Short=MALS-1;
DE   AltName: Full=Vertebrate lin-7 homolog 1;
DE            Short=Veli-1;
GN   Name=Lin7a; Synonyms=Mals1, Veli1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-111.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Aizawa K., Akimura T., Arakawa T., Carninci P., Fukuda S.,
RA   Hirozane T., Imotani K., Ishii Y., Itoh M., Kawai J., Konno H.,
RA   Miyazaki A., Murata M., Nakamura M., Nomura K., Numazaki R., Ohno M.,
RA   Sakai K., Sakazume N., Sasaki D., Sato K., Shibata K., Shiraki T.,
RA   Tagami M., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 23-233.
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH CDH1 AND CTNNB1.
RX   PubMed=10921879; DOI=10.1093/emboj/19.15.3978;
RA   Perego C., Vanoni C., Massari S., Longhi R., Pietrini G.;
RT   "Mammalian LIN-7 PDZ proteins associate with beta-catenin at the cell-
RT   cell junctions of epithelia and neurons.";
RL   EMBO J. 19:3978-3989(2000).
RN   [4]
RP   FUNCTION IN SYNAPTIC VESICLE LOCALIZATION.
RX   PubMed=14622577; DOI=10.1016/S0896-6273(03)00718-9;
RA   Bamji S.X., Shimazu K., Kimes N., Huelsken J., Birchmeier W., Lu B.,
RA   Reichardt L.F.;
RT   "Role of beta-catenin in synaptic vesicle localization and presynaptic
RT   assembly.";
RL   Neuron 40:719-731(2003).
RN   [5]
RP   INTERACTION WITH HTR4.
RX   PubMed=15466885; DOI=10.1242/jcs.01379;
RA   Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W.,
RA   Marin P., Dumuis A., Bockaert J.;
RT   "New sorting nexin (SNX27) and NHERF specifically interact with the 5-
RT   HT4a receptor splice variant: roles in receptor targeting.";
RL   J. Cell Sci. 117:5367-5379(2004).
RN   [6]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15494546; DOI=10.1152/ajprenal.00235.2004;
RA   Olsen O., Wade J.B., Morin N., Bredt D.S., Welling P.A.;
RT   "Differential localization of the Mammalian Lin 7 (MALS/Veli) PDZ
RT   proteins in the kidney.";
RL   Am. J. Physiol. 288:F345-F352(2005).
CC   -!- FUNCTION: Plays a role in establishing and maintaining the
CC       asymmetric distribution of channels and receptors at the plasma
CC       membrane of polarized cells. Forms membrane-associated
CC       multiprotein complexes that may regulate delivery and recycling of
CC       proteins to the correct membrane domains. The tripartite complex
CC       composed of LIN7 (LIN7A, LIN7B or LIN7C), CASK and APBA1 may have
CC       the potential to couple synaptic vesicle exocytosis to cell
CC       adhesion in brain. Ensures the proper localization of GRIN2B
CC       (subunit 2B of the NMDA receptor) to neuronal postsynaptic density
CC       and may function in localizing synaptic vesicles at synapses where
CC       it is recruited by beta-catenin and cadherin. Required to localize
CC       Kir2 channels, GABA transporter (SLC6A12) and EGFR/ERBB1, ERBB2,
CC       ERBB3 and ERBB4 to the basolateral membrane of epithelial cells.
CC   -!- SUBUNIT: Forms two exclusive ternary complexes with CASK and APBA1
CC       or CASKIN1 (By similarity). Can also interact with other modular
CC       proteins containing protein-protein interaction domains like MPP5,
CC       MPP6, MPP7, DLG1, DLG2 and DLG3 through its L27 domain. Interacts
CC       with DLG4, GRIN2B and MARCH11 as well as CDH1 and CTNNB1, the
CC       channels KCNJ12/Kir2.2, KCNJ4/Kir2.3 and probably KCNJ2/Kir2.1 and
CC       SLC6A12/BGT-1 via its PDZ domain. The association of LIN7A with
CC       cadherin and beta-catenin is calcium-dependent, occurs at synaptic
CC       junctions and requires the actin cytoskeleton. Interacts with
CC       EGFR, ERBB2, ERBB3 and ERBB4 with both PDZ and KID domains.
CC       Associates with KIF17 via APBA1. Interacts with HTR4. Forms a
CC       tripartite complex composed of DLG1, MPP7 and LIN7 (LIN7A or
CC       LIN7C) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC       Basolateral cell membrane; Peripheral membrane protein. Cell
CC       junction. Cell junction, synapse, postsynaptic cell membrane,
CC       postsynaptic density; Peripheral membrane protein. Cell junction,
CC       tight junction. Cell junction, synapse, synaptosome. Note=Enriched
CC       in synaptosomes and at epithelial cell-cell junctions. Mainly
CC       basolateral in renal epithelial cells.
CC   -!- TISSUE SPECIFICITY: Expressed in the kidney, along the length of
CC       the nephron.
CC   -!- DOMAIN: The kinase interacting site is required for proper
CC       delivery of ERBB2 to the basolateral membrane (By similarity).
CC   -!- DOMAIN: The PDZ domain regulates endocytosis and recycling of the
CC       receptor at the membrane (By similarity).
CC   -!- DOMAIN: The L27 domain mediates interaction with CASK and is
CC       involved in the formation of multimeric complexes and the
CC       association of LIN7 to membranes (By similarity).
CC   -!- SIMILARITY: Belongs to the lin-7 family.
CC   -!- SIMILARITY: Contains 1 L27 domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; BY123635; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC029721; AAH29721.1; -; mRNA.
DR   IPI; IPI00344142; -.
DR   RefSeq; NP_001034443.1; NM_001039354.1.
DR   UniGene; Mm.268025; -.
DR   ProteinModelPortal; Q8JZS0; -.
DR   SMR; Q8JZS0; 21-79, 108-190.
DR   MINT; MINT-91208; -.
DR   STRING; Q8JZS0; -.
DR   PRIDE; Q8JZS0; -.
DR   Ensembl; ENSMUST00000020057; ENSMUSP00000020057; ENSMUSG00000019906.
DR   GeneID; 108030; -.
DR   KEGG; mmu:108030; -.
DR   UCSC; uc007gyy.1; mouse.
DR   CTD; 108030; -.
DR   MGI; MGI:2135609; Lin7a.
DR   GeneTree; ENSGT00550000074582; -.
DR   HOGENOM; HBG315705; -.
DR   HOVERGEN; HBG052329; -.
DR   InParanoid; Q8JZS0; -.
DR   OMA; AQQNHMS; -.
DR   OrthoDB; EOG4BK556; -.
DR   PhylomeDB; Q8JZS0; -.
DR   NextBio; 359907; -.
DR   ArrayExpress; Q8JZS0; -.
DR   Bgee; Q8JZS0; -.
DR   CleanEx; MM_LIN7A; -.
DR   Genevestigator; Q8JZS0; -.
DR   GermOnline; ENSMUSG00000019906; Mus musculus.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019717; C:synaptosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0007269; P:neurotransmitter secretion; IGI:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0048489; P:synaptic vesicle transport; IMP:MGI.
DR   InterPro; IPR004172; L27.
DR   InterPro; IPR014775; L27_C.
DR   InterPro; IPR017365; Lin-7_homologue.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF02828; L27; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   PIRSF; PIRSF038039; Lin-7_homologue; 1.
DR   SMART; SM00569; L27; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS51022; L27; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Exocytosis; Membrane;
KW   Postsynaptic cell membrane; Protein transport; Synapse; Synaptosome;
KW   Tight junction; Transport.
FT   CHAIN         1    233       Protein lin-7 homolog A.
FT                                /FTId=PRO_0000189624.
FT   DOMAIN       25     80       L27.
FT   DOMAIN      108    190       PDZ.
FT   MOTIF        14     28       Kinase interacting site.
FT   COMPBIAS    210    213       Poly-Gln.
FT   COMPBIAS    217    229       Poly-Gln.
SQ   SEQUENCE   233 AA;  25993 MW;  D8D05EF16A93B8BB CRC64;
     MLKPSVTSAP TADMATLTVV QPLTLDRDVA RAIELLEKLQ ESGEVPVHKL QSLKKVLQSE
     FCTAIREVYQ YMHETITVNG CPEFRARATA KATVAAFAAS EGHSHPRVVE LPKTDEGLGF
     NVMGGKEQNS PIYISRIIPG GVAERHGGLK RGDQLLSVNG VSVEGEHHEK AVELLKAAKD
     SVKLVVRYTP KVLEEMEARF EKLRTARRRQ QQQLLIQQQQ QQQQQQPQQN HMS
//
ID   CPNE5_MOUSE             Reviewed;         593 AA.
AC   Q8JZW4;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Copine-5;
DE   AltName: Full=Copine V;
GN   Name=Cpne5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May function in membrane trafficking. Exhibits calcium-
CC       dependent phospholipid binding properties (By similarity).
CC   -!- SIMILARITY: Belongs to the copine family.
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -!- SIMILARITY: Contains 1 VWFA domain.
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DR   EMBL; AK044042; BAC31750.1; -; mRNA.
DR   EMBL; BC036971; AAH36971.1; -; mRNA.
DR   IPI; IPI00170387; -.
DR   RefSeq; NP_694806.1; NM_153166.2.
DR   UniGene; Mm.39905; -.
DR   ProteinModelPortal; Q8JZW4; -.
DR   SMR; Q8JZW4; 23-291, 427-464.
DR   PhosphoSite; Q8JZW4; -.
DR   PRIDE; Q8JZW4; -.
DR   Ensembl; ENSMUST00000024805; ENSMUSP00000024805; ENSMUSG00000024008.
DR   GeneID; 240058; -.
DR   KEGG; mmu:240058; -.
DR   UCSC; uc008bsk.1; mouse.
DR   CTD; 240058; -.
DR   MGI; MGI:2385908; Cpne5.
DR   GeneTree; ENSGT00550000074189; -.
DR   HOGENOM; HBG464786; -.
DR   HOVERGEN; HBG066841; -.
DR   InParanoid; Q8JZW4; -.
DR   OMA; ILEAYHH; -.
DR   OrthoDB; EOG415GD5; -.
DR   PhylomeDB; Q8JZW4; -.
DR   NextBio; 384405; -.
DR   ArrayExpress; Q8JZW4; -.
DR   Bgee; Q8JZW4; -.
DR   CleanEx; MM_CPNE5; -.
DR   Genevestigator; Q8JZW4; -.
DR   GermOnline; ENSMUSG00000024008; Mus musculus.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR010734; Copine.
DR   InterPro; IPR002035; VWF_A.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF07002; Copine; 1.
DR   SMART; SM00239; C2; 2.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS50234; VWFA; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1    593       Copine-5.
FT                                /FTId=PRO_0000144844.
FT   DOMAIN        9    116       C2 1.
FT   DOMAIN      147    268       C2 2.
FT   DOMAIN      328    554       VWFA.
FT   MOD_RES      11     11       Phosphoserine (By similarity).
FT   MOD_RES      19     19       Phosphoserine (By similarity).
SQ   SEQUENCE   593 AA;  65592 MW;  0B0BF66A852EACC2 CRC64;
     MEQPEDMASL SEFDSLAGSI PATKVEITVS CRNLLDKDMF SKSDPLCVMY TQGMENKQWR
     EFGRTEVIDN TLNPDFVRKF IVDYFFEEKQ NLRFDLYDVD SKSPDLSKHD FLGQAFCTLG
     EIVGSSGSRL EKPLTIGTFS LNSRTGKPMP AVSNGGVPGK KCGTIILSAE ELSNCRDVAT
     MQFCANKLDK KDFFGKSDPF LVFYRSNEDG TFTICHKTEV MKNTLNPVWQ TFSIPVRALC
     NGDYDRTIKV EVYDWDRDGS HDFIGEFTTS YRELARGQSQ FNIYEVINPK KKMKKKKYVN
     SGTVTLLSFA VESESTFLDY IKGGTQINFT VAIDFTASNG NPSQSTSLHY MSPYQLNAYA
     LALTAVGEII QHYDSDKMFP ALGFGAKLPP DGRVSHEFPL NGNQENPSCC GIDGILEAYH
     SSLRTVQLYG PTNFAPVVTH VARNAAAVQD GSQYSVLLII TDGVISDMAQ TKEAIVNAAK
     LPMSIIIVGV GQAEFDAMVE LDGDDVRISS RGKLAERDIV QFVPFRDYVD RTGNHVLSMA
     RLARDVLAEI PDQLVSYMKA QGIRPRPPPA APAQSPPQSP AHSPPGSPVH THI
//
ID   COMDA_MOUSE             Reviewed;         202 AA.
AC   Q8JZY2;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=COMM domain-containing protein 10;
DE   AltName: Full=Down-regulated in W/WV mouse stomach 2;
DE            Short=mDRWMS2;
GN   Name=Commd10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Daigo Y., Takayama I., Fujino M.A.;
RT   "Isolation and characterization of novel human and mouse genes, which
RT   are expressed in the digestive tract.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBUNIT: Interacts (via COMM domain) with COMMD1 (via COMM domain)
CC       (By similarity).
CC   -!- SIMILARITY: Contains 1 COMM domain.
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DR   EMBL; AB052770; BAC53803.1; -; mRNA.
DR   EMBL; BC034879; AAH34879.1; -; mRNA.
DR   IPI; IPI00265354; -.
DR   RefSeq; NP_848464.1; NM_178377.4.
DR   UniGene; Mm.210734; -.
DR   ProteinModelPortal; Q8JZY2; -.
DR   STRING; Q8JZY2; -.
DR   PRIDE; Q8JZY2; -.
DR   Ensembl; ENSMUST00000049388; ENSMUSP00000041650; ENSMUSG00000042705.
DR   GeneID; 69456; -.
DR   KEGG; mmu:69456; -.
DR   UCSC; uc008evz.1; mouse.
DR   CTD; 69456; -.
DR   MGI; MGI:1916706; Commd10.
DR   GeneTree; ENSGT00390000001500; -.
DR   HOGENOM; HBG713315; -.
DR   HOVERGEN; HBG051075; -.
DR   InParanoid; Q8JZY2; -.
DR   OMA; SSMGQET; -.
DR   PhylomeDB; Q8JZY2; -.
DR   NextBio; 329498; -.
DR   ArrayExpress; Q8JZY2; -.
DR   Bgee; Q8JZY2; -.
DR   CleanEx; MM_COMMD10; -.
DR   Genevestigator; Q8JZY2; -.
DR   GermOnline; ENSMUSG00000042705; Mus musculus.
DR   InterPro; IPR017920; COMM.
DR   InterPro; IPR009886; HCaRG.
DR   Pfam; PF07258; HCaRG; 1.
DR   PROSITE; PS51269; COMM; 1.
PE   2: Evidence at transcript level;
FT   CHAIN         1    202       COMM domain-containing protein 10.
FT                                /FTId=PRO_0000077406.
FT   DOMAIN      133    202       COMM.
SQ   SEQUENCE   202 AA;  22812 MW;  51798F2D0F6D8B45 CRC64;
     MAASAALILP ESPSMKKAVP LINAIDTGRF PRLLSRILQK LHLKAESSFS EEEEEKLQAA
     FSLEKQELHL VLETISFVLE QAVYHNVKPA ALQQQLEMIH LRKDKAEAFA SAWSAMGQET
     VEKFRQRILG PHKLETVGWQ LNLQMAHSAQ AKLQSPQAVL QLGVSKEDAK NVEKVLVEFN
     HKELFDFYNK LETIQAQLDS LT
//
ID   LPHN2_MOUSE             Reviewed;         891 AA.
AC   Q8JZZ7; Q8BM90;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 2.
DT   08-FEB-2011, entry version 73.
DE   RecName: Full=Latrophilin-2;
DE   AltName: Full=Calcium-independent alpha-latrotoxin receptor 2;
DE            Short=CIRL-2;
DE   Flags: Fragment;
GN   Name=Lphn2; Synonyms=Kiaa0786;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   PROTEIN SEQUENCE OF 211-218, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 486-891 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 660-891.
RC   TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-206, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Calcium-independent receptor of low affinity for alpha-
CC       latrotoxin, an excitatory neurotoxin present in black widow spider
CC       venom which triggers massive exocytosis from neurons and
CC       neuroendocrine cells. Receptor propably implicated in the
CC       regulation of exocytosis (By similarity).
CC   -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular
CC       region (p120) non-covalently linked to a seven-transmembrane
CC       moiety (p85) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8JZZ7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8JZZ7-2; Sequence=VSP_010110, VSP_010111;
CC   -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular
CC       subunit and a seven-transmembrane subunit (By similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       LN-TM7 subfamily.
CC   -!- SIMILARITY: Contains 1 GPS domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH34660.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK129215; BAC98025.1; -; mRNA.
DR   EMBL; AK034430; BAC28707.1; -; mRNA.
DR   EMBL; BC034660; AAH34660.1; ALT_INIT; mRNA.
DR   IPI; IPI00668099; -.
DR   IPI; IPI00876154; -.
DR   UniGene; Mm.331434; -.
DR   UniGene; Mm.9776; -.
DR   ProteinModelPortal; Q8JZZ7; -.
DR   MEROPS; S63.012; -.
DR   PRIDE; Q8JZZ7; -.
DR   Ensembl; ENSMUST00000037655; ENSMUSP00000042432; ENSMUSG00000028184.
DR   Ensembl; ENSMUST00000106127; ENSMUSP00000101733; ENSMUSG00000028184.
DR   UCSC; uc008rsa.1; mouse.
DR   MGI; MGI:2139714; Lphn2.
DR   GeneTree; ENSGT00600000084303; -.
DR   HOVERGEN; HBG052337; -.
DR   ArrayExpress; Q8JZZ7; -.
DR   Bgee; Q8JZZ7; -.
DR   CleanEx; MM_LPHN2; -.
DR   Genevestigator; Q8JZZ7; -.
DR   GermOnline; ENSMUSG00000028184; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:InterPro.
DR   InterPro; IPR022624; DUF3497.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR003924; GPCR_2_latrophilin.
DR   InterPro; IPR003334; GPCR_2_latrophilin_rcpt_C.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR   InterPro; IPR000203; GPS_dom.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF12003; DUF3497; 1.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF02354; Latrophilin; 2.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   PRINTS; PR01444; LATROPHILIN.
DR   SMART; SM00303; GPS; 1.
DR   PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG.
DR   PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR   PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; FALSE_NEG.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Direct protein sequencing;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW   Receptor; Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN        <1    891       Latrophilin-2.
FT                                /FTId=PRO_0000070343.
FT   TOPO_DOM     <1    326       Extracellular (Potential).
FT   TRANSMEM    327    347       Helical; Name=1; (Potential).
FT   TOPO_DOM    348    355       Cytoplasmic (Potential).
FT   TRANSMEM    356    376       Helical; Name=2; (Potential).
FT   TOPO_DOM    377    382       Extracellular (Potential).
FT   TRANSMEM    383    403       Helical; Name=3; (Potential).
FT   TOPO_DOM    404    426       Cytoplasmic (Potential).
FT   TRANSMEM    427    447       Helical; Name=4; (Potential).
FT   TOPO_DOM    448    465       Extracellular (Potential).
FT   TRANSMEM    466    486       Helical; Name=5; (Potential).
FT   TOPO_DOM    487    512       Cytoplasmic (Potential).
FT   TRANSMEM    513    533       Helical; Name=6; (Potential).
FT   TOPO_DOM    534    537       Extracellular (Potential).
FT   TRANSMEM    538    558       Helical; Name=7; (Potential).
FT   TOPO_DOM    559    891       Cytoplasmic (Potential).
FT   DOMAIN      260    311       GPS.
FT   SITE        299    300       Cleavage (By similarity).
FT   MOD_RES     813    813       Phosphoserine (By similarity).
FT   MOD_RES     819    819       Phosphoserine (By similarity).
FT   CARBOHYD      8      8       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    104    104       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    206    206       N-linked (GlcNAc...).
FT   CARBOHYD    219    219       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    262    262       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    267    267       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    288    288       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     509    509       K -> NNYRVCDGYYNTDLPG (in isoform 2).
FT                                /FTId=VSP_010110.
FT   VAR_SEQ     641    641       G -> GMTGNYLLTNPLLRPHGTNNPYNTLLAETVVCNAPS
FT                                APAFNSPATYRETR (in isoform 2).
FT                                /FTId=VSP_010111.
FT   NON_TER       1      1
SQ   SEQUENCE   891 AA;  99452 MW;  C5008C6438F95389 CRC64;
     PKGPDLSNCT SHWVNQLAQK IRSGENAASL ANELAKHTKG HVFAGDVSSS VRLMEQLVDI
     LDAQLQELKP SEKDSAGRSY NKAIVDTVDN LLRAEALESW KHMNSSEQAH TATMLLDTLE
     EGAFVLADNL LEPTRVSMPT ENIVLEVAVL STEGQVQDFK FPLGLKGLGS SIQLSANTVK
     QNSRNGLAKL VFIIYRSLGQ FLSTENATIK LGADLMGRNS TIAVNSPVIS VSINKESSRV
     YLTDPVLFTL PHIDPDNYFN ANCSFWNYSE RTMMGYWSTQ GCKLVDTNKT RTTCACSHLT
     NFAILMAHRE IAYKDGVHHL LLTVITWVGI VVSLVCLAIC IFTFCFFRGL QSDRNTIHKN
     LCINLFIAEF IFLIGIDKTK YTIACPVFAG LLHFFFLAAF SWMCLEGVQL YLMLVEVFES
     EYSRKKYYYV AGYLFPATVV GVSAAIDYKS YGTVQACWLH VDNYFIWSFI GPVTFIILLN
     IIFLVITLCK MVKHSNTLKP DSSRLENIKS WVLGAFALLC LLGLTWSFGL LFVNEETVVM
     AYLFTAFNAF QGLFIFIFHC ALQKKVRKEY GKCFRHWYCC GGLPTESPHS SVKASTTRTS
     ARYSSGTQSR IRRMWNDTVR KQSESSFISG DINSTSTLNQ GHSLNNARDT SAMDTLPLNG
     NFNNSYSLRK ADYHDGVQVV DCGLSLNDTA FEKMIISELV HNNLRGGNKT HNLELKLPVK
     PVIGGSSSED DAIVADASSL MHGDNPGLEF RHKELEAPLI PQRTHSLLYQ PQKKVKPEAT
     DSYVSQLTAE ADDHLQSPNR DSLYTSMPNL RDSPYPESSP DMAEDLSPSR RSENEDIYYK
     SMPNLGAGRH LHMCYQISRG NSDGYIIPIN KEGCIPEGDV REGQMQLVTS L
//
ID   AL1L2_MOUSE             Reviewed;         923 AA.
AC   Q8K009;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Probable 10-formyltetrahydrofolate dehydrogenase ALDH1L2;
DE            EC=1.5.1.6;
DE   AltName: Full=Aldehyde dehydrogenase family 1 member L2;
GN   Name=Aldh1l2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + NADP(+) + H(2)O =
CC       tetrahydrofolate + CO(2) + NADPH.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the GART family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the aldehyde
CC       dehydrogenase family. ALDH1L subfamily.
CC   -!- SIMILARITY: Contains 1 acyl carrier domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC034531; AAH34531.1; -; mRNA.
DR   IPI; IPI00169472; -.
DR   UniGene; Mm.263138; -.
DR   HSSP; O75891; 2BW0.
DR   ProteinModelPortal; Q8K009; -.
DR   SMR; Q8K009; 23-923.
DR   PhosphoSite; Q8K009; -.
DR   PRIDE; Q8K009; -.
DR   Ensembl; ENSMUST00000020497; ENSMUSP00000020497; ENSMUSG00000020256.
DR   UCSC; uc007gkh.1; mouse.
DR   MGI; MGI:2444680; Aldh1l2.
DR   eggNOG; roNOG06727; -.
DR   GeneTree; ENSGT00550000074289; -.
DR   HOGENOM; HBG315849; -.
DR   HOVERGEN; HBG051668; -.
DR   InParanoid; Q8K009; -.
DR   OrthoDB; EOG45TCMG; -.
DR   PhylomeDB; Q8K009; -.
DR   BRENDA; 1.5.1.6; 244.
DR   NextBio; 375062; -.
DR   ArrayExpress; Q8K009; -.
DR   Bgee; Q8K009; -.
DR   CleanEx; MM_ALDH1L2; -.
DR   Genevestigator; Q8K009; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0000036; F:acyl carrier activity; IEA:InterPro.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0016155; F:formyltetrahydrofolate dehydrogenase activity; IEA:EC.
DR   GO; GO:0016742; F:hydroxymethyl-, formyl- and related transferase activity; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0009258; P:10-formyltetrahydrofolate catabolic process; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR011407; 10_FTHF_DH.
DR   InterPro; IPR009081; Acyl_carrier_prot-like.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR005793; Formyl_trans_C.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR011034; Formyl_transferase_C-like.
DR   InterPro; IPR001555; GART_AS.
DR   InterPro; IPR006163; Phsphopanteth-bd.
DR   InterPro; IPR006162; PPantetheine_attach_site.
DR   Gene3D; G3DSA:1.10.1200.10; ACP_like; 1.
DR   Gene3D; G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 1.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   Gene3D; G3DSA:3.10.25.10; Formyl_trans_C; 1.
DR   Gene3D; G3DSA:3.40.50.170; Formyl_transf_N; 1.
DR   PANTHER; PTHR11699; Aldehyde_dehyd; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   Pfam; PF02911; Formyl_trans_C; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   PIRSF; PIRSF036489; 10-FTHFDH; 1.
DR   SUPFAM; SSF47336; ACP_like; 1.
DR   SUPFAM; SSF53720; Aldehyde_DH/Histidinol_DH; 1.
DR   SUPFAM; SSF50486; FMT_C_like; 1.
DR   SUPFAM; SSF53328; formyl_transf; 1.
DR   PROSITE; PS50075; ACP_DOMAIN; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
DR   PROSITE; PS00373; GART; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; NADP; One-carbon metabolism; Oxidoreductase;
KW   Phosphopantetheine.
FT   CHAIN         1    923       Probable 10-formyltetrahydrofolate
FT                                dehydrogenase ALDH1L2.
FT                                /FTId=PRO_0000316002.
FT   DOMAIN      344    413       Acyl carrier.
FT   REGION       23    225       GART.
FT   REGION      438    923       Aldehyde dehydrogenase.
FT   ACT_SITE    128    128       Proton donor (By similarity).
FT   ACT_SITE    694    694       By similarity.
FT   ACT_SITE    728    728       By similarity.
FT   SITE        164    164       Essential for catalytic activity (By
FT                                similarity).
FT   MOD_RES     375    375       O-(pantetheine 4'-phosphoryl)serine (By
FT                                similarity).
FT   MOD_RES     903    903       N6-acetyllysine (By similarity).
SQ   SEQUENCE   923 AA;  101564 MW;  441D57CAF3D11303 CRC64;
     MLWRGSQALR HFSTSRVYFK NKLKLALIGQ SLFGQEVYSQ LLKEGHRVVG VFTVPDKDGK
     ADPLALAAEK DGTPVFKFPR WRLKGKTIKE VAEAYQSVGA ELNVLPFCTQ FIPMDVIDSP
     KHGSIIYHPS LLPRHRGASA INWTLIMGDK KAGFSVFWAD DGLDTGPILL QRSCDVKPND
     TVDSLYNRFL FPEGIKAMVE AVQLIADGKA PRTPQPEEGA TYEGIQKKEN AEVSWDQPAE
     GLHNWIRGHD KVPGAWAEIN GQMVTFYGSS LLTSSVPSGE PLDIRGAKKP GLVTKNGLVL
     FGNDGKALMV RNLQFEDGKM IPASQYFSAG ETSVVELTAE ELKVAETIKV IWARILSNTP
     VIEDSTDFFK SGASSMDVVR LVEEIRQSCG GLQLQNEDVY MATKFGDFIQ KVVRRLRGED
     EEAEMVVDYV SKEVNGMTVK IPYQCFINGQ FVDAEDGETY ATVNPTDGTT ICRVSHASLA
     DVDRAVAAAK DAFENGEWGR MNARDRGRLM YRLADLMEEN QEELATIEAL DSGAVYTLAL
     KTHIGMSVQT FRYFAGWCDK IQGSTIPINQ ARPNYNLTFT KKEPLGACAI IIPWNYPLMM
     LAWKSAACLA AGNTLVLKPA QVTPLTALKF AELTVKAGFP KGVINIIPGS GGVAGQRLSQ
     HPDIRKLGFT GSTSVGKQIM KSCAVSNLKK VSLELGGKSP LIIFSDCDLE KAVRMGMGAV
     FFNKGENCIA AGRLFVEEAI HDEFVTRVVE EIKKMKIGDP LDRSTDHGPQ NHRAHLEKLL
     QYCETGVQEG ATLVYGGRQV QRPGFFMEPT VFTGVEDHMY LAKEESFGPI MVISKFQNGD
     IDGVLQRANN TEYGLASGVF TRDINKAMYV SDKLEAGTVF INTYNKTDVA APFGGMKQSG
     FGKDLGEEAL NEYLKIKTVT LEY
//
ID   FBP1L_MOUSE             Reviewed;         605 AA.
AC   Q8K012; Q3U901;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Formin-binding protein 1-like;
DE   AltName: Full=Transducer of Cdc42-dependent actin assembly protein 1;
DE            Short=Toca-1;
GN   Name=Fnbp1l; Synonyms=Toca1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-108 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 132-605 (ISOFORM 2).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Required to coordinate membrane tubulation with
CC       reorganization of the actin cytoskeleton during endocytosis. May
CC       bind to lipids such as phosphatidylinositol 4,5-bisphosphate and
CC       phosphatidylserine and promote membrane invagination and the
CC       formation of tubules. Also promotes CDC42-induced actin
CC       polymerization by activating the WASL-WASPIP complex, the
CC       predominant form of WASL/N-WASP in cells. Actin polymerization may
CC       promote the fission of membrane tubules to form endocytic vesicles
CC       (By similarity).
CC   -!- SUBUNIT: Interacts with GTP-bound CDC42. Interacts with DAAM1,
CC       DIAPH1, DIAPH2, DNM1, DNM2 and WASL/N-WASP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity). Cytoplasm, cell cortex (By
CC       similarity). Cytoplasmic vesicle (By similarity). Cell membrane;
CC       Peripheral membrane protein; Cytoplasmic side (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K012-1; Sequence=Displayed;
CC         Note=Gene prediction based on EST data;
CC       Name=2;
CC         IsoId=Q8K012-2; Sequence=VSP_021712, VSP_021713;
CC   -!- SIMILARITY: Belongs to the FNBP1 family.
CC   -!- SIMILARITY: Contains 1 FCH domain.
CC   -!- SIMILARITY: Contains 1 REM (Hr1) repeat.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH34510.1; Type=Erroneous initiation;
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DR   EMBL; AC099584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC138720; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK151930; BAE30806.1; -; mRNA.
DR   EMBL; AK152002; BAE30866.1; -; mRNA.
DR   EMBL; BC034510; AAH34510.1; ALT_INIT; mRNA.
DR   IPI; IPI00169474; -.
DR   IPI; IPI00970419; -.
DR   RefSeq; NP_001108137.1; NM_001114665.1.
DR   RefSeq; NP_694758.2; NM_153118.2.
DR   UniGene; Mm.209491; -.
DR   UniGene; Mm.470230; -.
DR   HSSP; Q15642; 2CT4.
DR   ProteinModelPortal; Q8K012; -.
DR   SMR; Q8K012; 9-287, 542-602.
DR   STRING; Q8K012; -.
DR   PhosphoSite; Q8K012; -.
DR   PRIDE; Q8K012; -.
DR   Ensembl; ENSMUST00000098637; ENSMUSP00000096236; ENSMUSG00000039735.
DR   Ensembl; ENSMUST00000106438; ENSMUSP00000102046; ENSMUSG00000039735.
DR   GeneID; 214459; -.
DR   KEGG; mmu:214459; -.
DR   UCSC; uc008rer.1; mouse.
DR   CTD; 214459; -.
DR   MGI; MGI:1925642; Fnbp1l.
DR   eggNOG; roNOG12731; -.
DR   GeneTree; ENSGT00510000046403; -.
DR   HOGENOM; HBG446221; -.
DR   HOVERGEN; HBG002489; -.
DR   InParanoid; Q8K012; -.
DR   OrthoDB; EOG4SN1NK; -.
DR   NextBio; 374318; -.
DR   ArrayExpress; Q8K012; -.
DR   Bgee; Q8K012; -.
DR   CleanEx; MM_FNBP1L; -.
DR   Genevestigator; Q8K012; -.
DR   GermOnline; ENSMUSG00000039735; Mus musculus.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   InterPro; IPR001060; FCH.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50133; FCH; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW   Cytoplasmic vesicle; Cytoskeleton; Endocytosis; Lipid-binding;
KW   Membrane; Phosphoprotein; SH3 domain.
FT   CHAIN         1    605       Formin-binding protein 1-like.
FT                                /FTId=PRO_0000261435.
FT   DOMAIN        1     65       FCH.
FT   REPEAT      409    484       REM.
FT   DOMAIN      538    599       SH3.
FT   REGION        1    371       Induction of membrane tubulation (By
FT                                similarity).
FT   REGION      245    535       Interaction with CDC42 (By similarity).
FT   REGION      522    605       Interaction with DNM1 (By similarity).
FT   REGION      541    605       Interaction with DAAM1, DIAPH1 and DIAPH2
FT                                (By similarity).
FT   REGION      541    597       Interaction with DNM2 and WASL (By
FT                                similarity).
FT   COILED      130    177       Potential.
FT   MOD_RES     295    295       Phosphoserine (By similarity).
FT   MOD_RES     488    488       Phosphoserine (By similarity).
FT   MOD_RES     501    501       Phosphoserine.
FT   VAR_SEQ     331    389       Missing (in isoform 2).
FT                                /FTId=VSP_021712.
FT   VAR_SEQ     605    605       S -> AVTYI (in isoform 2).
FT                                /FTId=VSP_021713.
SQ   SEQUENCE   605 AA;  69885 MW;  ABFE6744EF4241E1 CRC64;
     MSWGTELWDQ FDSLDKHTQW GIDFLERYAK FVKERIEIEQ NYAKQLRNLV KKYCPKRSSK
     DEEPRFTSCI AFFNILNELN DYAGQREVVA EEMAHRVYGE LMRYAHDLKT ERKMHLQEGR
     KAQQYLDMCW KQMDNSKKKF ERECREAEKA QQSYERLDND TNATKADVEK AKQQLNLRTH
     MADENKNEYA AQLQNFNGEQ HKHFYVVIPQ IYKQLQEMDE RRTIKLSECY RGFADSERKV
     IPIISKCLEG MILAAKSVDE RRDSQMVVDS FKSGFEPPGD FPFEDYSQHI YRTISDGTIS
     AAKQESGKMD SKSTVGKAKG KLWLFGKKPK PQSPPLTPTS LFTSSTPNGS QFLTLSIEPV
     HYCMNEIKTG KPRIPSFRSL KRGVSLIMGP ALEDFSHLPP EQRRKKLQQR IDELNRGLQK
     EADQKEALNK MKDVYEKNPQ MGDPGSLQPK LAETMNNIDR LRMEIHKNEA WLSEVEGKTG
     IRGDRRHSSD INHLVTQGRE SPEGSYTDDA NQEVRGPPQQ HGHHSEFDDE FEDDDPLPAI
     GHCKAIYPFD GHNEGTLAMK EGEVLYIIEE DKGDGWTRAR RQNGEEGYVP TTYIDVTLEK
     SSKGS
//
ID   BCLF1_MOUSE             Reviewed;         919 AA.
AC   Q8K019; Q8BNZ0; Q8C2E9; Q9CSW5;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   08-FEB-2011, entry version 71.
DE   RecName: Full=Bcl-2-associated transcription factor 1;
DE            Short=Btf;
GN   Name=Bclaf1; Synonyms=Btf, Kiaa0164;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-164 (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 499-917 (ISOFORM 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-917 (ISOFORMS 1/2).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284; SER-289 AND
RP   THR-839, AND MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177 AND SER-510, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-383; SER-395
RP   AND THR-400, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284; SER-289; SER-395
RP   AND THR-400, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494 AND SER-656, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; SER-122; SER-125;
RP   SER-177; SER-198; SER-267; SER-296; SER-383; SER-395; SER-494; SER-510
RP   AND SER-658, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-284; SER-286;
RP   SER-395; SER-494; SER-529; SER-646 AND SER-656, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177; SER-510; SER-529
RP   AND SER-656, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Death-promoting transcriptional repressor (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with Bcl-2 related proteins, EMD, with the
CC       adenovirus E1B 19 kDa protein and with DNA (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8K019-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K019-2; Sequence=VSP_010372;
CC       Name=3;
CC         IsoId=Q8K019-3; Sequence=VSP_010372, VSP_010373, VSP_010374;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK011802; BAB27851.1; -; mRNA.
DR   EMBL; AK079110; BAC37542.1; -; mRNA.
DR   EMBL; AK088741; BAC40542.1; -; mRNA.
DR   EMBL; BC034300; AAH34300.1; -; mRNA.
DR   EMBL; AK129071; BAC97881.1; -; mRNA.
DR   IPI; IPI00169477; -.
DR   IPI; IPI00415385; -.
DR   IPI; IPI00762634; -.
DR   RefSeq; NP_001020563.1; NM_001025392.1.
DR   RefSeq; NP_722482.1; NM_153787.2.
DR   UniGene; Mm.294783; -.
DR   STRING; Q8K019; -.
DR   PhosphoSite; Q8K019; -.
DR   PRIDE; Q8K019; -.
DR   Ensembl; ENSMUST00000043881; ENSMUSP00000043583; ENSMUSG00000037608.
DR   Ensembl; ENSMUST00000100045; ENSMUSP00000097622; ENSMUSG00000037608.
DR   GeneID; 72567; -.
DR   KEGG; mmu:72567; -.
DR   UCSC; uc007ent.1; mouse.
DR   UCSC; uc007enu.1; mouse.
DR   CTD; 72567; -.
DR   MGI; MGI:1917580; Bclaf1.
DR   GeneTree; ENSGT00530000063211; -.
DR   HOGENOM; HBG282098; -.
DR   HOVERGEN; HBG050681; -.
DR   InParanoid; Q8K019; -.
DR   OMA; EYSGFAG; -.
DR   PhylomeDB; Q8K019; -.
DR   NextBio; 336507; -.
DR   ArrayExpress; Q8K019; -.
DR   Bgee; Q8K019; -.
DR   CleanEx; MM_BCLAF1; -.
DR   Genevestigator; Q8K019; -.
DR   GermOnline; ENSMUSG00000037608; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; DNA-binding; Nucleus;
KW   Phosphoprotein; Repressor; Transcription; Transcription regulation.
FT   CHAIN         1    919       Bcl-2-associated transcription factor 1.
FT                                /FTId=PRO_0000064889.
FT   COMPBIAS    141    148       Poly-Ser.
FT   COMPBIAS    748    762       Poly-Ser.
FT   MOD_RES     102    102       Phosphoserine (By similarity).
FT   MOD_RES     104    104       Phosphoserine (By similarity).
FT   MOD_RES     119    119       Phosphoserine.
FT   MOD_RES     122    122       Phosphoserine.
FT   MOD_RES     125    125       Phosphoserine.
FT   MOD_RES     148    148       Phosphoserine (By similarity).
FT   MOD_RES     151    151       Phosphoserine (By similarity).
FT   MOD_RES     152    152       N6-acetyllysine (By similarity).
FT   MOD_RES     153    153       Phosphoserine (By similarity).
FT   MOD_RES     161    161       Phosphoserine (By similarity).
FT   MOD_RES     177    177       Phosphoserine.
FT   MOD_RES     181    181       Phosphoserine (By similarity).
FT   MOD_RES     183    183       Phosphoserine (By similarity).
FT   MOD_RES     198    198       Phosphoserine.
FT   MOD_RES     216    216       Phosphoserine (By similarity).
FT   MOD_RES     221    221       Phosphoserine (By similarity).
FT   MOD_RES     263    263       Phosphoserine (By similarity).
FT   MOD_RES     267    267       Phosphoserine.
FT   MOD_RES     275    275       Phosphoserine (By similarity).
FT   MOD_RES     280    280       Phosphoserine (By similarity).
FT   MOD_RES     283    283       Phosphotyrosine (By similarity).
FT   MOD_RES     284    284       Phosphoserine.
FT   MOD_RES     286    286       Phosphoserine.
FT   MOD_RES     289    289       Phosphoserine.
FT   MOD_RES     296    296       Phosphoserine.
FT   MOD_RES     314    314       Phosphoserine (By similarity).
FT   MOD_RES     318    318       Phosphoserine (By similarity).
FT   MOD_RES     319    319       Phosphoserine (By similarity).
FT   MOD_RES     333    333       N6-acetyllysine (By similarity).
FT   MOD_RES     339    339       Phosphothreonine (By similarity).
FT   MOD_RES     383    383       Phosphoserine.
FT   MOD_RES     387    387       Phosphoserine (By similarity).
FT   MOD_RES     395    395       Phosphoserine.
FT   MOD_RES     400    400       Phosphothreonine.
FT   MOD_RES     403    403       Phosphothreonine (By similarity).
FT   MOD_RES     406    406       Phosphotyrosine (By similarity).
FT   MOD_RES     419    419       N6-acetyllysine (By similarity).
FT   MOD_RES     435    435       N6-acetyllysine (By similarity).
FT   MOD_RES     441    441       Phosphoserine (By similarity).
FT   MOD_RES     448    448       Phosphoserine (By similarity).
FT   MOD_RES     487    487       Phosphothreonine (By similarity).
FT   MOD_RES     494    494       Phosphoserine.
FT   MOD_RES     500    500       Phosphoserine (By similarity).
FT   MOD_RES     509    509       Phosphotyrosine (By similarity).
FT   MOD_RES     510    510       Phosphoserine.
FT   MOD_RES     523    523       Phosphoserine (By similarity).
FT   MOD_RES     529    529       Phosphoserine.
FT   MOD_RES     576    576       Phosphoserine (By similarity).
FT   MOD_RES     635    635       N6-acetyllysine (By similarity).
FT   MOD_RES     646    646       Phosphoserine.
FT   MOD_RES     656    656       Phosphoserine.
FT   MOD_RES     658    658       Phosphoserine.
FT   MOD_RES     688    688       Phosphoserine (By similarity).
FT   MOD_RES     709    709       Phosphoserine (By similarity).
FT   MOD_RES     718    718       Phosphoserine (By similarity).
FT   MOD_RES     756    756       Phosphoserine (By similarity).
FT   MOD_RES     759    759       Phosphoserine (By similarity).
FT   MOD_RES     839    839       Phosphothreonine.
FT   VAR_SEQ      35     36       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_010372.
FT   VAR_SEQ     740    750       HKGRERDHSRS -> NVFVFYTAYGG (in isoform
FT                                3).
FT                                /FTId=VSP_010373.
FT   VAR_SEQ     751    919       Missing (in isoform 3).
FT                                /FTId=VSP_010374.
FT   CONFLICT    616    616       E -> K (in Ref. 1; BAC37542).
FT   CONFLICT    667    667       A -> T (in Ref. 1; BAC37542).
SQ   SEQUENCE   919 AA;  106002 MW;  F57E6327B29B8920 CRC64;
     MGRSNSRSHS SRSKSRSQSS SRSRSRSHSR KKRYSSRSRS RTYSRSRSRD RIYSRDYRRD
     YRNNRGMRRP YGYRGRGRGY YQGGGGRYHR GGYRPVWNRR HSRSPRRGRS RSRSPKRRSV
     SSQRSRSRSR RSYRSSRSPR SSSSRSSSPY SKSPVSKRRG SQEKQTKKAE GEPQEESPLK
     SKSQEEPKDT FEHDPSESID EFNKSATSGD IWPGLSAYDN SPRSPHSPSP IATPPSQSSS
     CSDAPMLSTV HSAKNTPSQH SHSIQHSPER SGSGSVGNGS SRYSPSQNSP IHHIPSRRSP
     AKTITPQNAP REESRGRSSF YPEGDQETAK TGKFLKRFTD EESRVFLLDR GNIRDKEAPK
     EKGSEKGRAD GDWDDQEVLD YFSDKESAKQ KFHDSEGDDT EETEDYRQFR KSVLADQGKS
     FATSSHRNTE EEGPKYKSKV SLKGNRESDG FREEKNYKLK ETAYIVERPS TAKDKHKEED
     KGSDRITVKK EVQSPEQVKS EKLKELFDYS PPLHKSLDAR EKSIFREESP LRIKMIASDS
     HRPEVKLKMA PVPLDDSNRP ASLTKDRLLA STLVHSVKKE QEFRSIFDHI KLPQANKSTS
     ESFIQHIVSL VHHVKEQYFK SPAVTLNERF TSYQKATEEH STRQKSPEIH RRIDISPSAL
     RKHTRLAGEE RGFKEEIQKG DKKLRCDSAD LRHDIDRRRK ERSKERGDSK GSRESSGSRK
     QEKTPKDYKE YKPYKDDSKH KGRERDHSRS SSSSASPSSP SSREEKESKK EREEEFKTHH
     EMKDYSGFAG VSRPRGTFFR IRGRGRARGV FAGTNTGPNN SNTTFQKRPK EEEWDPEYTP
     KSKKYFLHDD RDDGVDYWAK RGRGRGTFQR GRGRFNFKKS GSSPKWTHDK YQGDGIVEDD
     EETMENNEEK KDRRKEEKE
//
ID   SCAM1_MOUSE             Reviewed;         338 AA.
AC   Q8K021;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Secretory carrier-associated membrane protein 1;
DE            Short=Secretory carrier membrane protein 1;
GN   Name=Scamp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 91-103 AND 299-334, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: Functions in post-Golgi recycling pathways. Acts as a
CC       recycling carrier to the cell surface (By similarity).
CC   -!- SUBUNIT: Interacts with SYNRG, ITSN1 and SLC9A7 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC       membrane; Multi-pass membrane protein (By similarity). Recycling
CC       endosome membrane; Multi-pass membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the SCAMP family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC034283; AAH34283.1; -; mRNA.
DR   IPI; IPI00278804; -.
DR   RefSeq; NP_083429.1; NM_029153.1.
DR   UniGene; Mm.201455; -.
DR   STRING; Q8K021; -.
DR   PhosphoSite; Q8K021; -.
DR   PRIDE; Q8K021; -.
DR   Ensembl; ENSMUST00000022197; ENSMUSP00000022197; ENSMUSG00000021687.
DR   GeneID; 107767; -.
DR   KEGG; mmu:107767; -.
DR   UCSC; uc007rls.1; mouse.
DR   CTD; 107767; -.
DR   MGI; MGI:1349480; Scamp1.
DR   HOGENOM; HBG444815; -.
DR   HOVERGEN; HBG071938; -.
DR   InParanoid; Q8K021; -.
DR   OMA; RAVDFGL; -.
DR   OrthoDB; EOG4G4GQX; -.
DR   PhylomeDB; Q8K021; -.
DR   NextBio; 359416; -.
DR   ArrayExpress; Q8K021; -.
DR   Bgee; Q8K021; -.
DR   CleanEx; MM_SCAMP1; -.
DR   Genevestigator; Q8K021; -.
DR   GermOnline; ENSMUSG00000021687; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; ISS:UniProtKB.
DR   GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR   GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR   GO; GO:0042589; C:zymogen granule membrane; IDA:MGI.
DR   GO; GO:0006887; P:exocytosis; IMP:MGI.
DR   GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR   InterPro; IPR007273; SCAMP.
DR   PANTHER; PTHR10687; SCAMP; 1.
DR   Pfam; PF04144; SCAMP; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endosome; Golgi apparatus; Membrane;
KW   Protein transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    338       Secretory carrier-associated membrane
FT                                protein 1.
FT                                /FTId=PRO_0000191251.
FT   TOPO_DOM      1    155       Cytoplasmic (Potential).
FT   TRANSMEM    156    176       Helical; (Potential).
FT   TOPO_DOM    177    181       Lumenal (Potential).
FT   TRANSMEM    182    202       Helical; (Potential).
FT   TOPO_DOM    203    218       Cytoplasmic (Potential).
FT   TRANSMEM    219    239       Helical; (Potential).
FT   TOPO_DOM    240    261       Lumenal (Potential).
FT   TRANSMEM    262    282       Helical; (Potential).
FT   TOPO_DOM    283    338       Cytoplasmic (Potential).
SQ   SEQUENCE   338 AA;  38029 MW;  7588A06064B23B9D CRC64;
     MSDFDSNPFA DPDLNNPFKD PSVTQVTRNV PPGLDEYNPF SDSRTPPPGS VKMPNVPNTQ
     PAIMKPTEEH PAYTQITKEH ALAQAELLKR QEELERKAAE LDRREREMQN LSQHGRKNNW
     PPLPSNFPVG PCFYQDFSVD IPVEFQKTVK LMYYLWMFHA VTLFLNIFGC LAWFCVDSSR
     AVDFGLSILW FLLFTPCSFV CWYRPLYGAF RSDSSFRFFV FFFVYICQFA VHVLQAAGFH
     NWGNCGWISS LTGLNKNIPV GIMMIIIAAL FTASAVISLV MFKKVHGLYR TTGASFEKAQ
     QEFATGVMSN KTVQTAAANA ASTAATSAAQ NAFKGNQM
//
ID   SAM14_MOUSE             Reviewed;         417 AA.
AC   Q8K070; Q5SWB7; Q8BHE2; Q8C8N5;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Sterile alpha motif domain-containing protein 14;
DE            Short=SAM domain-containing protein 14;
GN   Name=Samd14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Retina, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Eye, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC32983.1; Type=Frameshift; Positions=116;
CC       Sequence=BAC33903.1; Type=Frameshift; Positions=60, 118;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK044765; BAC32075.1; -; mRNA.
DR   EMBL; AK047184; BAC32983.1; ALT_FRAME; mRNA.
DR   EMBL; AK049753; BAC33903.1; ALT_FRAME; mRNA.
DR   EMBL; AL606480; CAI23966.1; -; Genomic_DNA.
DR   EMBL; BC034054; AAH34054.1; -; mRNA.
DR   EMBL; BC049954; AAH49954.1; -; mRNA.
DR   IPI; IPI00169507; -.
DR   RefSeq; NP_666137.1; NM_146025.2.
DR   UniGene; Mm.297199; -.
DR   ProteinModelPortal; Q8K070; -.
DR   SMR; Q8K070; 322-392.
DR   PhosphoSite; Q8K070; -.
DR   PRIDE; Q8K070; -.
DR   Ensembl; ENSMUST00000055947; ENSMUSP00000062231; ENSMUSG00000047181.
DR   GeneID; 217125; -.
DR   KEGG; mmu:217125; -.
DR   UCSC; uc007kzt.1; mouse.
DR   CTD; 217125; -.
DR   MGI; MGI:2384945; Samd14.
DR   eggNOG; roNOG07317; -.
DR   GeneTree; ENSGT00390000010033; -.
DR   HOGENOM; HBG715345; -.
DR   HOVERGEN; HBG093931; -.
DR   InParanoid; Q8K070; -.
DR   OMA; HPRAEPH; -.
DR   PhylomeDB; Q8K070; -.
DR   NextBio; 375577; -.
DR   ArrayExpress; Q8K070; -.
DR   Bgee; Q8K070; -.
DR   CleanEx; MM_SAMD14; -.
DR   Genevestigator; Q8K070; -.
DR   GermOnline; ENSMUSG00000047181; Mus musculus.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Phosphoprotein.
FT   CHAIN         1    417       Sterile alpha motif domain-containing
FT                                protein 14.
FT                                /FTId=PRO_0000250564.
FT   DOMAIN      326    389       SAM.
FT   COILED      375    416       Potential.
FT   COMPBIAS    203    288       Ser-rich.
FT   MOD_RES     108    108       Phosphoserine.
FT   MOD_RES     173    173       Phosphoserine.
FT   CONFLICT     17     17       D -> H (in Ref. 1; BAC33903).
FT   CONFLICT    113    113       E -> K (in Ref. 1; BAC32075).
SQ   SEQUENCE   417 AA;  45102 MW;  1FB9F3D7390DFA82 CRC64;
     MASSKLREPV DEVFDLDLAV PETTRLDSSL HKARAQLLAK GRRHRPSRSR LRDSASSAED
     GEGSDGPGGK VTDGCGSPLH RLRSPLHSGP GSPASGSFCL EPPGLRRSLD EDEPPPSPLA
     RYRPLHNAAS HEGLAATSGS PPRSAPSSDS SPSFVRRYPR AEPHSEDDSR DASPPEPASP
     TIGLDKKTRR KFLDLGVTLR RASTSRSRKE KGSNRLSMGS RESVEGSGRT GSSPFLPFSW
     FTDSGKGSAS SGSTTSPTCS PKHEGFSPKK SASQESTLSD DSTPPSSSPK IPGGPRQETK
     CSYPYHTLSQ SSDEFLDESL PAVQHWTSQQ VGQWLHSLNL EQYAAEFAAR QVDGPQLLQL
     DGSKLKSLGL SNSHDRALVK RKLKELAAAA EKERKAQEKT AKQREKLRRR ENDAKKS
//
ID   REEP4_MOUSE             Reviewed;         257 AA.
AC   Q8K072;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Receptor expression-enhancing protein 4;
GN   Name=Reep4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15550249; DOI=10.1016/j.cell.2004.11.021;
RA   Saito H., Kubota M., Roberts R.W., Chi Q., Matsunami H.;
RT   "RTP family members induce functional expression of mammalian odorant
RT   receptors.";
RL   Cell 119:679-691(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May enhance the cell surface expression of odorant
CC       receptors (By similarity).
CC   -!- SUBUNIT: Interacts with odorant receptor proteins (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the DP1 family.
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CC   -----------------------------------------------------------------------
DR   EMBL; AY562232; AAT70677.1; -; mRNA.
DR   EMBL; BC033929; AAH33929.1; -; mRNA.
DR   IPI; IPI00169509; -.
DR   RefSeq; NP_850919.1; NM_180588.1.
DR   UniGene; Mm.46742; -.
DR   ProteinModelPortal; Q8K072; -.
DR   PhosphoSite; Q8K072; -.
DR   PRIDE; Q8K072; -.
DR   Ensembl; ENSMUST00000047218; ENSMUSP00000040162; ENSMUSG00000033589.
DR   GeneID; 72549; -.
DR   KEGG; mmu:72549; -.
DR   UCSC; uc007uoi.1; mouse.
DR   CTD; 72549; -.
DR   MGI; MGI:1919799; Reep4.
DR   eggNOG; roNOG15406; -.
DR   GeneTree; ENSGT00550000074535; -.
DR   HOGENOM; HBG716753; -.
DR   HOVERGEN; HBG056861; -.
DR   InParanoid; Q8K072; -.
DR   OMA; RHEKEID; -.
DR   OrthoDB; EOG4HQDK4; -.
DR   PhylomeDB; Q8K072; -.
DR   NextBio; 336467; -.
DR   ArrayExpress; Q8K072; -.
DR   Bgee; Q8K072; -.
DR   CleanEx; MM_REEP4; -.
DR   Genevestigator; Q8K072; -.
DR   GermOnline; ENSMUSG00000033589; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR004345; TB2_DP1_HVA22.
DR   PANTHER; PTHR12300; TB2_DP1_HVA22; 1.
DR   Pfam; PF03134; TB2_DP1_HVA22; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    257       Receptor expression-enhancing protein 4.
FT                                /FTId=PRO_0000101831.
FT   TRANSMEM      1     21       Helical; (Potential).
FT   TRANSMEM     42     62       Helical; (Potential).
FT   MOD_RES     152    152       Phosphoserine (By similarity).
FT   MOD_RES     194    194       Phosphoserine (By similarity).
FT   MOD_RES     196    196       Phosphothreonine (By similarity).
FT   MOD_RES     202    202       Phosphoserine (By similarity).
FT   MOD_RES     253    253       Phosphoserine (By similarity).
SQ   SEQUENCE   257 AA;  29691 MW;  69C3877CC439EF28 CRC64;
     MVSWMICRLV VLIFGMLYPA YASYKAVKSK NIREYVRWMM YWIVFAIFMA AETFTDIFIS
     WFPFYYEFKM AFVLWLLSPY TKGASLLYRK FVHPSLSRHE KEIDACIVQA KERSYETMLS
     FGKRSLNIAA SAAVQAATKS QGALAGRLRS FSMQDLRSIP DTPVPTYQDP LYLEDQVPRR
     RPPIGYRPGG LQGSDTEDEC WSDNEIVPQP PVRPREKPLG RSQSLRVVKR KPLTREGTSR
     SLKVRTRKKA MPSDMDS
//
ID   SO4A1_MOUSE             Reviewed;         723 AA.
AC   Q8K078; Q8BZT4;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2003, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Solute carrier organic anion transporter family member 4A1;
DE   AltName: Full=Organic anion-transporting polypeptide E;
DE            Short=OATP-E;
DE   AltName: Full=Sodium-independent organic anion transporter E;
DE   AltName: Full=Solute carrier family 21 member 12;
GN   Name=Slco4a1; Synonyms=Oatp4a1, Oatpe, Slc21a12;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cecum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-67, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Mediates the Na(+)-independent transport of organic
CC       anions such as the thyroid hormone T3 (triiodo-L-thyronine) and of
CC       taurocholate (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K078-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K078-2; Sequence=VSP_006157, VSP_006158;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60)
CC       family.
CC   -!- SIMILARITY: Contains 1 Kazal-like domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH33602.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK033598; BAC28379.1; -; mRNA.
DR   EMBL; BC030719; AAH30719.1; -; mRNA.
DR   EMBL; BC030720; AAH30720.1; -; mRNA.
DR   EMBL; BC033602; AAH33602.1; ALT_INIT; mRNA.
DR   IPI; IPI00177177; -.
DR   IPI; IPI00473307; -.
DR   RefSeq; NP_683735.1; NM_148933.1.
DR   UniGene; Mm.133687; -.
DR   ProteinModelPortal; Q8K078; -.
DR   SMR; Q8K078; 509-535.
DR   STRING; Q8K078; -.
DR   PhosphoSite; Q8K078; -.
DR   PRIDE; Q8K078; -.
DR   Ensembl; ENSMUST00000038225; ENSMUSP00000045023; ENSMUSG00000038963.
DR   Ensembl; ENSMUST00000038259; ENSMUSP00000046502; ENSMUSG00000038963.
DR   GeneID; 108115; -.
DR   KEGG; mmu:108115; -.
DR   UCSC; uc008ojc.1; mouse.
DR   CTD; 108115; -.
DR   MGI; MGI:1351866; Slco4a1.
DR   GeneTree; ENSGT00560000076724; -.
DR   HOGENOM; HBG717600; -.
DR   HOVERGEN; HBG100565; -.
DR   InParanoid; Q8K078; -.
DR   OMA; TFGPKFF; -.
DR   OrthoDB; EOG41VK2S; -.
DR   PhylomeDB; Q8K078; -.
DR   NextBio; 360096; -.
DR   ArrayExpress; Q8K078; -.
DR   Bgee; Q8K078; -.
DR   Genevestigator; Q8K078; -.
DR   GermOnline; ENSMUSG00000038963; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR020846; Major_facilitator_SF.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   InterPro; IPR004156; OA_transporter.
DR   InterPro; IPR011497; Prot_Inh_Kazal_2.
DR   PANTHER; PTHR11388; OA_transporter; 1.
DR   Pfam; PF07648; Kazal_2; 1.
DR   Pfam; PF03137; OATP; 1.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
DR   TIGRFAMs; TIGR00805; oat; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW   Ion transport; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    723       Solute carrier organic anion transporter
FT                                family member 4A1.
FT                                /FTId=PRO_0000191068.
FT   TOPO_DOM      1    102       Cytoplasmic (Potential).
FT   TRANSMEM    103    123       Helical; Name=1; (Potential).
FT   TOPO_DOM    124    142       Extracellular (Potential).
FT   TRANSMEM    143    163       Helical; Name=2; (Potential).
FT   TOPO_DOM    164    169       Cytoplasmic (Potential).
FT   TRANSMEM    170    194       Helical; Name=3; (Potential).
FT   TOPO_DOM    195    224       Extracellular (Potential).
FT   TRANSMEM    225    255       Helical; Name=4; (Potential).
FT   TOPO_DOM    256    274       Cytoplasmic (Potential).
FT   TRANSMEM    275    295       Helical; Name=5; (Potential).
FT   TOPO_DOM    296    309       Extracellular (Potential).
FT   TRANSMEM    310    334       Helical; Name=6; (Potential).
FT   TOPO_DOM    335    380       Cytoplasmic (Potential).
FT   TRANSMEM    381    402       Helical; Name=7; (Potential).
FT   TOPO_DOM    403    422       Extracellular (Potential).
FT   TRANSMEM    423    446       Helical; Name=8; (Potential).
FT   TOPO_DOM    447    450       Cytoplasmic (Potential).
FT   TRANSMEM    451    473       Helical; Name=9; (Potential).
FT   TOPO_DOM    474    582       Extracellular (Potential).
FT   TRANSMEM    583    605       Helical; Name=10; (Potential).
FT   TOPO_DOM    606    614       Cytoplasmic (Potential).
FT   TRANSMEM    615    640       Helical; Name=11; (Potential).
FT   TOPO_DOM    641    673       Extracellular (Potential).
FT   TRANSMEM    674    691       Helical; Name=12; (Potential).
FT   TOPO_DOM    692    723       Cytoplasmic (Potential).
FT   DOMAIN      500    557       Kazal-like.
FT   MOD_RES      39     39       Phosphoserine (By similarity).
FT   MOD_RES      42     42       Phosphoserine (By similarity).
FT   MOD_RES      45     45       Phosphoserine.
FT   MOD_RES      67     67       Phosphoserine.
FT   CARBOHYD    212    212       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    566    566       N-linked (GlcNAc...) (Potential).
FT   DISULFID    506    532       By similarity.
FT   DISULFID    511    521       By similarity.
FT   DISULFID    512    536       By similarity.
FT   VAR_SEQ     629    632       SIPG -> TAWG (in isoform 2).
FT                                /FTId=VSP_006157.
FT   VAR_SEQ     633    723       Missing (in isoform 2).
FT                                /FTId=VSP_006158.
FT   CONFLICT     28     28       S -> R (in Ref. 1; BAC28379).
SQ   SEQUENCE   723 AA;  77669 MW;  0856B45F02C4EBAC CRC64;
     MPQHAMGDTH FLSLPKHLFT STSSATDSGC DTPPSSRASP ASLRSAHGTL GSSSQPLFEP
     QAEKRSSQTA REVQYVSSGP QNSLCGWQAF TPKCLQVFNT PKGFLFFLCA ASFLQGMTVN
     GFINTVITSI ERRFDLHSYQ SGLIASSYDI AACLCLTFVS YFGGNGHKPR WLGWGVLVLG
     IGSLVFALPH FTAGRYEVEM DEGLGTGTCL TNQSHVECKD SASGLSNYRL IFMLGQLLHG
     VGATPLYTLG VTYLDENVKS SYSPIYIAIF YTAAILGPAA GYLIGGAMLN VYTEVGQRTE
     LTTDSPLWVG AWWIGFLGTG IAAFLIAIPI LGYPRQLPGS QRYVVMRAAE TQQLKDHSRG
     AVSNPAFGKT VRDLPLSIWL LLRNPTFILL CLAGATEATL IAGMSTFGPK FFEAQFSLSA
     SEAATLFGYL VVPAGGGGTL LGGFLVNKFK LRGSGIIRFC LFCTLTSLLA FFVFLMHCPN
     VHMAGVTTGY VGSLLPKGQL DLKAACNAIY CCQPKHYSPL CGSDGTMYYS PCYAGCPADA
     ETDLGGQKVY RGCSCILEKA SSGWGNATAG KCASTCQSKP FLLVLVFVVI IFTFLSSIPA
     LTATLRCVSD RQRSFALGIQ WIVVRTLGSI PGPIAFGWVI DKACLLWQDQ CGHQGSCFVY
     ENEAMSRYML IAGLTFKVLG FLFFVAAYFL YKSPSVSSDG LEASLPSQSS ASDSPTEQLQ
     SNV
//
ID   ZN536_MOUSE             Reviewed;        1302 AA.
AC   Q8K083; Q80U15;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Zinc finger protein 536;
GN   Name=Znf536; Synonyms=Kiaa0390, Zfp536;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon, and Pituitary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC       Recognizes and binds 2 copies of the core DNA sequence 5'-CCCCCA-
CC       3' (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family.
CC   -!- SIMILARITY: Contains 9 C2H2-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65552.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK122270; BAC65552.1; ALT_INIT; mRNA.
DR   EMBL; AK030633; BAC27055.1; -; mRNA.
DR   EMBL; AK034508; BAC28735.1; -; mRNA.
DR   EMBL; BC033594; AAH33594.1; -; mRNA.
DR   IPI; IPI00377726; -.
DR   RefSeq; NP_759017.1; NM_172385.2.
DR   UniGene; Mm.322505; -.
DR   UniGene; Mm.378309; -.
DR   UniGene; Mm.388121; -.
DR   HSSP; P15822; 1BBO.
DR   ProteinModelPortal; Q8K083; -.
DR   SMR; Q8K083; 124-460, 626-810.
DR   PRIDE; Q8K083; -.
DR   Ensembl; ENSMUST00000056338; ENSMUSP00000058468; ENSMUSG00000043456.
DR   GeneID; 243937; -.
DR   KEGG; mmu:243937; -.
DR   UCSC; uc009gkk.1; mouse.
DR   CTD; 243937; -.
DR   MGI; MGI:1926102; Zfp536.
DR   GeneTree; ENSGT00530000063100; -.
DR   HOGENOM; HBG717175; -.
DR   HOVERGEN; HBG080712; -.
DR   InParanoid; Q8K083; -.
DR   OMA; EFRCEVC; -.
DR   PhylomeDB; Q8K083; -.
DR   NextBio; 386046; -.
DR   ArrayExpress; Q8K083; -.
DR   Bgee; Q8K083; -.
DR   CleanEx; MM_ZFP536; -.
DR   Genevestigator; Q8K083; -.
DR   GO; GO:0005634; C:nucleus; IC:MGI.
DR   GO; GO:0044323; F:retinoic acid-responsive element binding; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; IDA:MGI.
DR   GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; IDA:MGI.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 7.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 10.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1   1302       Zinc finger protein 536.
FT                                /FTId=PRO_0000271042.
FT   ZN_FING     130    152       C2H2-type 1.
FT   ZN_FING     158    180       C2H2-type 2.
FT   ZN_FING     274    297       C2H2-type 3.
FT   ZN_FING     300    323       C2H2-type 4.
FT   ZN_FING     345    367       C2H2-type 5.
FT   ZN_FING     373    395       C2H2-type 6.
FT   ZN_FING     631    653       C2H2-type 7.
FT   ZN_FING     753    775       C2H2-type 8.
FT   ZN_FING     781    803       C2H2-type 9.
FT   MOD_RES     828    828       Phosphoserine (By similarity).
FT   MOD_RES     829    829       Phosphoserine (By similarity).
FT   CONFLICT    590    590       N -> Y (in Ref. 1; BAC65552).
FT   CONFLICT    899    899       Y -> F (in Ref. 1; BAC65552).
FT   CONFLICT   1036   1036       T -> A (in Ref. 1; BAC65552).
FT   CONFLICT   1207   1207       G -> S (in Ref. 1; BAC65552).
SQ   SEQUENCE   1302 AA;  141576 MW;  A9AF82D1D9481465 CRC64;
     MEEASLCLGV SSTAPEAEPH LSGPVLNGQY AMSQKLHQIT SQLSHAFPEL HPRPNPEEKT
     PAALEEKAHV PMSGQSMGSQ MALLANQLGR DVDNSLNGRV DLQQFLNGQN LGIMSQMSDI
     EDDARKNRKY PCPLCGKRFR FNSILSLHMR THTGEKPFKC PYCDHRAAQK GNLKIHLRTH
     KLGNLGKGRG RVREENRLLH ELEERAILRD KQMKGSLLQP RSDLKPLAHA QQAPLATCNL
     ALPPNHSVPD VAHPAPSPKP ANLQEDSVTP AAGFRCTFCK GKFKKREELD RHIRILHKPY
     KCTLCDFAAS QEEELISHVE KAHITAESAQ GQGPNGGGEQ SANEFRCEVC GQVFSQAWFL
     KGHMRKHKDS FEHCCQICGR RFKEPWFLKN HMKVHLNKLS VKNKSPTEPE VAVPMGGLSQ
     EAHANLYSRY LSCLQSGFMA PDKASLNEPS QLYGKGELPA KEKEVLGKLL SPISSMAHSV
     PEGDKHSLLG CLNLVPPLKS SCIERLQAAA KAAEMDPVNS YQAWQLMARG MAMEHGFLSK
     EHQLSRNHED PLANTGVLFD KEKREYVLVG ADGSKQKMPA DLVHSTKVGN QRDLPNKLDP
     LEGSREFLSH GLNQTLDYNL QGPGNMKEKP TECPDCGRVF RTYHQVVVHS RVHKRDRKSD
     EDALHVGVGL EERRGSGSDQ ESQSVSRSTT PGSSNVTEES GAGGGLSQTG SAQEDSPHPS
     SPSSSDIGEE AGRAGGVQQQ ALLRDRNLGS AMKDCPYCGK TFRTSHHLKV HLRIHTGEKP
     YKCPHCDYAG TQSASLKYHL ERHHRERQNG AGPLSGQPPN QEHKDETSSK APMFIRPDIL
     RGAFKGLPGI DFRGGPASQQ WTAGMLSSGD HSGQATGMPS ELSSDALKGS DLPSKSSHYS
     EIGRAYQNIV SNGVNFQGSL QAFMDSFVLS SLKKKDTKDK VPSDAHPMKA HTAEGGEEKA
     SMKPSQRKSE KSQYEPLDLS VRPDAPTLPG SSVTVQDSIA WHGCLFCAFT TSSMELMALH
     LQANHLGRAK RKDHPTGVTV NCKEQGREAS KVSVLPSLQS NKEMALPSAV GVLDSAPEKL
     AQGPAKETLG DPKSGQWPNH MDPAFCTFPS DFYKQFGVYP AMVGSGAPGS CLNKNTEGKT
     HPDDDAPILI PETTNKNTTD DLSDIASSED MDSSKGENNE DEELDTEPEM TSKPLSALSK
     DGSSEGGDSL LSPGAPQPIQ GLVSPLAQAA EEQWHSPGLL PAQDPSAGLP KPERGPPGLE
     KPMSMLSVLR AYSADGLAAF NGLASSTANS GCIKRPDLCG KF
//
ID   FAIM2_MOUSE             Reviewed;         317 AA.
AC   Q8K097; Q3TY22; Q8K1F6; Q9D6K4;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Fas apoptotic inhibitory molecule 2;
DE   AltName: Full=Protein lifeguard;
GN   Name=Faim2; Synonyms=Kiaa0950, Lfg;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RA   Sole C., Segura M.F., Bayascas J.R., Comella J.X.;
RT   "Cloning and characterization of the long form of mouse lifeguard
RT   (LFG-L), an anti Fas-apoptotic molecule.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-39, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Protects cells uniquely from Fas-induced apoptosis (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with TNFRSF6 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity). Cell junction, synapse, postsynaptic cell
CC       membrane (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Long, LFG-L;
CC         IsoId=Q8K097-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short, LFG-S;
CC         IsoId=Q8K097-2; Sequence=VSP_008994;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the BI1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98056.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AF468028; AAM46781.1; -; mRNA.
DR   EMBL; AK013476; BAB28874.1; -; mRNA.
DR   EMBL; AK030513; BAC26999.1; -; mRNA.
DR   EMBL; AK129246; BAC98056.1; ALT_INIT; mRNA.
DR   EMBL; AK158960; BAE34742.1; -; mRNA.
DR   EMBL; BC032278; AAH32278.1; -; mRNA.
DR   IPI; IPI00408985; -.
DR   IPI; IPI00467229; -.
DR   RefSeq; NP_001033747.1; NM_001038658.1.
DR   RefSeq; NP_082500.2; NM_028224.3.
DR   UniGene; Mm.39760; -.
DR   STRING; Q8K097; -.
DR   PhosphoSite; Q8K097; -.
DR   PRIDE; Q8K097; -.
DR   Ensembl; ENSMUST00000023750; ENSMUSP00000023750; ENSMUSG00000023011.
DR   GeneID; 72393; -.
DR   KEGG; mmu:72393; -.
DR   UCSC; uc007xpp.1; mouse.
DR   UCSC; uc007xpq.1; mouse.
DR   CTD; 72393; -.
DR   MGI; MGI:1919643; Faim2.
DR   eggNOG; roNOG15373; -.
DR   GeneTree; ENSGT00500000044791; -.
DR   HOGENOM; HBG595196; -.
DR   HOVERGEN; HBG012084; -.
DR   InParanoid; Q8K097; -.
DR   OMA; SCQGVIF; -.
DR   OrthoDB; EOG43R3N3; -.
DR   PhylomeDB; Q8K097; -.
DR   NextBio; 336176; -.
DR   ArrayExpress; Q8K097; -.
DR   Bgee; Q8K097; -.
DR   CleanEx; MM_FAIM2; -.
DR   Genevestigator; Q8K097; -.
DR   GermOnline; ENSMUSG00000023011; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   InterPro; IPR006214; Inhibitor_apoptosis_Bax1.
DR   PANTHER; PTHR23291; UPF0005; 1.
DR   Pfam; PF01027; UPF0005; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Cell junction; Cell membrane;
KW   Glycoprotein; Membrane; Phosphoprotein; Postsynaptic cell membrane;
KW   Synapse; Transmembrane; Transmembrane helix.
FT   CHAIN         1    317       Fas apoptotic inhibitory molecule 2.
FT                                /FTId=PRO_0000179088.
FT   TRANSMEM    107    127       Helical; (Potential).
FT   TRANSMEM    139    159       Helical; (Potential).
FT   TRANSMEM    166    186       Helical; (Potential).
FT   TRANSMEM    195    215       Helical; (Potential).
FT   TRANSMEM    226    246       Helical; (Potential).
FT   TRANSMEM    252    272       Helical; (Potential).
FT   TRANSMEM    291    311       Helical; (Potential).
FT   MOD_RES      39     39       Phosphotyrosine.
FT   CARBOHYD    192    192       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ      72     84       SGSSGYEGGFPAG -> R (in isoform 2).
FT                                /FTId=VSP_008994.
FT   CONFLICT    256    256       A -> T (in Ref. 2; BAC98056).
FT   CONFLICT    312    312       F -> Y (in Ref. 1; AAM46781).
SQ   SEQUENCE   317 AA;  35258 MW;  A62D51BA49BCDB15 CRC64;
     MTQGKLSVAN KAPGTEGQQH QANGEKKDAP AVPSAPPSYE EATSGEGLKA GTFPQGPTAV
     PLHPSWAYVD PSGSSGYEGG FPAGHHEHFT TFSWDDQKVR RLFIRKVYTI LLVQLLVTLA
     VVALFTFCDV VKDYVQANPG WYWASYAVFF ATYLTLACCS GPRRHFPWNL ILLTIFTLSM
     AYLTGMLSSY YNTTSVLLCL VITALVCLSV TIFSFQTKFD FTSCQGVLFV LLMTLFFSGL
     LLAVLLPFQY VPWLHAVYAV LGAGVFTLFL AFDTQLLMGN RRHSLSPEEY IFGALNIYLD
     IIYIFTFFLQ LFGTNRE
//
ID   IPO13_MOUSE             Reviewed;         963 AA.
AC   Q8K0C1; Q6ZQ60;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Importin-13;
DE            Short=Imp13;
GN   Name=Ipo13; Synonyms=Kiaa0724;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryo;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Functions in nuclear protein import as nuclear transport
CC       receptor. Serves as receptor for nuclear localization signals
CC       (NLS) in cargo substrates. Is thought to mediate docking of the
CC       importin/substrate complex to the nuclear pore complex (NPC)
CC       through binding to nucleoporin and the complex is subsequently
CC       translocated through the pore by an energy requiring, Ran-
CC       dependent mechanism. At the nucleoplasmic side of the NPC, Ran
CC       binds to the importin, the importin/substrate complex dissociates
CC       and importin is re-exported from the nucleus to the cytoplasm
CC       where GTP hydrolysis releases Ran. The directionality of nuclear
CC       import is thought to be conferred by an asymmetric distribution of
CC       the GTP- and GDP-bound forms of Ran between the cytoplasm and
CC       nucleus (By similarity). Mediates the nuclear import of UBC9, the
CC       RBM8A/MAGOH complex, PAX6 and probably other members of the paired
CC       homeobox family. Also mediates nuclear export of eIF-1A, and the
CC       cytoplasmic release of eIF-1A is triggered by the loading of
CC       import substrates onto IPO13 (By similarity).
CC   -!- SUBUNIT: Interacts with UBC9, RBM8A, eIF-1A and PAX6 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K0C1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K0C1-2; Sequence=VSP_010936, VSP_010937;
CC   -!- SIMILARITY: Belongs to the importin beta family.
CC   -!- SIMILARITY: Contains 14 HEAT repeats.
CC   -!- SIMILARITY: Contains 1 importin N-terminal domain.
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DR   EMBL; AK129200; BAC98010.2; -; Transcribed_RNA.
DR   EMBL; BC031823; AAH31823.1; -; mRNA.
DR   EMBL; AK052257; BAC34899.1; -; mRNA.
DR   IPI; IPI00169541; -.
DR   IPI; IPI00453577; -.
DR   RefSeq; NP_666264.1; NM_146152.3.
DR   UniGene; Mm.287810; -.
DR   ProteinModelPortal; Q8K0C1; -.
DR   SMR; Q8K0C1; 18-953.
DR   STRING; Q8K0C1; -.
DR   PRIDE; Q8K0C1; -.
DR   Ensembl; ENSMUST00000036156; ENSMUSP00000035989; ENSMUSG00000033365.
DR   Ensembl; ENSMUST00000106417; ENSMUSP00000102025; ENSMUSG00000033365.
DR   GeneID; 230673; -.
DR   KEGG; mmu:230673; -.
DR   UCSC; uc008ujg.1; mouse.
DR   CTD; 230673; -.
DR   MGI; MGI:2385205; Ipo13.
DR   GeneTree; ENSGT00530000063347; -.
DR   HOVERGEN; HBG052141; -.
DR   OMA; VQEDGRM; -.
DR   OrthoDB; EOG4K6G3G; -.
DR   PhylomeDB; Q8K0C1; -.
DR   NextBio; 380039; -.
DR   ArrayExpress; Q8K0C1; -.
DR   Bgee; Q8K0C1; -.
DR   CleanEx; MM_IPO13; -.
DR   Genevestigator; Q8K0C1; -.
DR   GermOnline; ENSMUSG00000033365; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR013598; Exportin-1/Importin-b-like.
DR   InterPro; IPR001494; Importin-beta_N.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 3.
DR   Pfam; PF03810; IBN_N; 1.
DR   Pfam; PF08389; Xpo1; 1.
DR   SMART; SM00913; IBN_N; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
DR   PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Nucleus; Protein transport; Repeat;
KW   Transport.
FT   CHAIN         1    963       Importin-13.
FT                                /FTId=PRO_0000120759.
FT   DOMAIN       45    111       Importin N-terminal.
FT   REPEAT      164    195       HEAT 1.
FT   REPEAT      196    235       HEAT 2.
FT   REPEAT      251    276       HEAT 3.
FT   REPEAT      277    314       HEAT 4.
FT   REPEAT      331    370       HEAT 5.
FT   REPEAT      388    437       HEAT 6.
FT   REPEAT      444    481       HEAT 7.
FT   REPEAT      482    522       HEAT 8.
FT   REPEAT      525    560       HEAT 9.
FT   REPEAT      599    634       HEAT 10.
FT   REPEAT      635    674       HEAT 11.
FT   REPEAT      679    717       HEAT 12.
FT   REPEAT      718    756       HEAT 13.
FT   REPEAT      788    830       HEAT 14.
FT   VAR_SEQ     369    375       Missing (in isoform 2).
FT                                /FTId=VSP_010936.
FT   VAR_SEQ     872    886       AIGGQASRSLMDCFA -> VSWSKWLGVGRPSLLRRLALCC
FT                                G (in isoform 2).
FT                                /FTId=VSP_010937.
SQ   SEQUENCE   963 AA;  108229 MW;  3ABBCE15668B6BCB CRC64;
     MERREEQLGA AGAGAAPALD FTVENVEKAL HQLYYDPNID NKNLAQKWLM QAQVSPQAWH
     FSWQLLQPDK VPEIQYFGAS ALHIKISRYW SDIPTDQYES LKAQLFTQIT RFASGSKIVL
     TRLCVALASL ALSMMPDAWP CAVADMVRLF QAEDSPVDSQ GRCLALLELL TVLPEEFQTS
     RLPQYRKGLV RTSLAVECGT VFPLLEQLLQ QPSSPSCVRQ KVLKCFSSWV QLEVPLQDCE
     ALIQAAFAAL QDSELFDSSV EAIVNAISQP DAQRYVNTLL KLIPLVLGLQ EQLRQAVQNG
     DMETSHGICR IAVALGENHS RALLDQVEHW QSFLALVNMI MFCTGIPGHY PVNETTSSLT
     LTFWYTLQDD ILSFEAEKQA VYQQVYRPVY FQLVDVLLHK AQFPSDEEYG FWSSDEKEQF
     RIYRVDISDT LMYVYEMLGA ELLSNLYDKL GRLLTSSEEP YSWQHTEALL YGFQSIAETI
     DVNYSDVVPG LIGLIPRISI SNVQLADTVM FTIGALSEWL ADHPVMINSV LPLVLHALGN
     PELSVSSVST LKKICRECKY DLPPYAANIV AVSQDVLMKQ IHKTSQCMWL MQALGFLLSA
     LQVEEILKNL HSLISPYIQQ LEKLAEEIPN PSNKLAIVHI LGLLSNLFTT LDVSHHEDDH
     EGPELRKLPV PQGPNPVVVV LQQVFQLIQK VLSKWLNDAQ VVEAVCAIFE KSVKTLLDDF
     APMVPQLCEM LGRMYSTVPQ ASALDLTRQL VHIFAHEPAH FPPIEALFLL VTSVTLSLFQ
     QGPRDHPDIV DSFMQLLAQA LKRKPDLFLC ERLDVKAVFQ CAVLALKFPE APTVKASCGF
     FTELLPRCGE IESVGKVVQE DGRMLLIAVL EAIGGQASRS LMDCFADILF ALNKHCFSLL
     SMWIKEALQP PGFPSARLSP EQKDTFSQQI LRERVNKRRV KEMVKEFTLL CRGLHGTDYT
     ADY
//
ID   CDK17_MOUSE             Reviewed;         523 AA.
AC   Q8K0D0;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Cyclin-dependent kinase 17;
DE            EC=2.7.11.22;
DE   AltName: Full=Cell division protein kinase 17;
DE   AltName: Full=PCTAIRE-motif protein kinase 2;
DE   AltName: Full=Serine/threonine-protein kinase PCTAIRE-2;
GN   Name=Cdk17; Synonyms=Pctk2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Limb, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   IDENTIFICATION IN A COMPLEX WITH CABLES1 AND TDRD7.
RX   PubMed=11527406; DOI=10.1006/bbrc.2001.5493;
RA   Yamochi T., Nishimoto I., Okuda T., Matsuoka M.;
RT   "ik3-1/Cables is associated with Trap and Pctaire2.";
RL   Biochem. Biophys. Res. Commun. 286:1045-1050(2001).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-203, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-146 AND
RP   SER-180, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-137 AND SER-180,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May play a role in terminally differentiated neurons.
CC       Has a Ser/Thr-phosphorylating activity for histone H1 (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Found in a complex containing CABLES1, CDK16 and TDRD7.
CC       Interacts with TDRD7.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K0D0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K0D0-2; Sequence=VSP_010640, VSP_010641;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. CDC2/CDKX subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH31778.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; BC031778; AAH31778.1; ALT_INIT; mRNA.
DR   EMBL; BC064815; AAH64815.1; -; mRNA.
DR   IPI; IPI00132433; -.
DR   IPI; IPI00421065; -.
DR   RefSeq; NP_666351.2; NM_146239.2.
DR   UniGene; Mm.478891; -.
DR   ProteinModelPortal; Q8K0D0; -.
DR   SMR; Q8K0D0; 189-499.
DR   STRING; Q8K0D0; -.
DR   PhosphoSite; Q8K0D0; -.
DR   PRIDE; Q8K0D0; -.
DR   Ensembl; ENSMUST00000069965; ENSMUSP00000070355; ENSMUSG00000020015.
DR   GeneID; 237459; -.
DR   KEGG; mmu:237459; -.
DR   UCSC; uc007gul.1; mouse.
DR   UCSC; uc007gum.1; mouse.
DR   CTD; 237459; -.
DR   MGI; MGI:97517; Cdk17.
DR   GeneTree; ENSGT00600000083998; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG014652; -.
DR   InParanoid; Q8K0D0; -.
DR   OMA; NDEFKNY; -.
DR   OrthoDB; EOG44BB24; -.
DR   PhylomeDB; Q8K0D0; -.
DR   BRENDA; 2.7.11.22; 244.
DR   NextBio; 383378; -.
DR   ArrayExpress; Q8K0D0; -.
DR   Bgee; Q8K0D0; -.
DR   CleanEx; MM_PCTK2; -.
DR   Genevestigator; Q8K0D0; -.
DR   GermOnline; ENSMUSG00000020015; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004693; F:cyclin-dependent protein kinase activity; IEA:EC.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    523       Cyclin-dependent kinase 17.
FT                                /FTId=PRO_0000086488.
FT   DOMAIN      192    473       Protein kinase.
FT   NP_BIND     198    206       ATP (By similarity).
FT   ACT_SITE    313    313       Proton acceptor (By similarity).
FT   BINDING     221    221       ATP (By similarity).
FT   MOD_RES       9      9       Phosphoserine.
FT   MOD_RES      75     75       Phosphoserine (By similarity).
FT   MOD_RES      80     80       Phosphoserine (By similarity).
FT   MOD_RES     105    105       Phosphoserine (By similarity).
FT   MOD_RES     115    115       Phosphothreonine (By similarity).
FT   MOD_RES     116    116       Phosphoserine (By similarity).
FT   MOD_RES     122    122       Phosphoserine (By similarity).
FT   MOD_RES     137    137       Phosphoserine.
FT   MOD_RES     146    146       Phosphoserine.
FT   MOD_RES     165    165       Phosphoserine (By similarity).
FT   MOD_RES     180    180       Phosphoserine.
FT   MOD_RES     202    202       Phosphothreonine (By similarity).
FT   MOD_RES     203    203       Phosphotyrosine.
FT   MOD_RES     205    205       Phosphothreonine (By similarity).
FT   MOD_RES     520    520       Phosphoserine (By similarity).
FT   VAR_SEQ       1     84       Missing (in isoform 2).
FT                                /FTId=VSP_010640.
FT   VAR_SEQ     512    523       GHGKNRRQSMLF -> ALS (in isoform 2).
FT                                /FTId=VSP_010641.
SQ   SEQUENCE   523 AA;  59506 MW;  847B045A3BCE4628 CRC64;
     MKKFKRRLSL TLRGSQTIDE SLSELAEQMT IEESSSKDNE PIVKNGRPPT SHSVHSFLHQ
     YTGSFKKPPL RRPHSVIGGS LGSFMAMPRN GSRLDIVHEN LKMGSDGESD QASGTSSDEV
     QSPTGVCLRN RIHRRISMED LNKRLSLPAD IRIPDGYLEK LQISSPPFDQ PMSRRSRRAS
     LSEIGFGKME TYIKLEKLGE GTYATVYKGR SKLTENLVAL KEIRLEHEEG APCTAIREVS
     LLKDLKHANI VTLHDIVHTD KSLTLVFEYL DKDLKQYMDD CGNIMSMHNV KLFLYQILRG
     LAYCHRRKVL HRDLKPQNLL INERGELKLA DFGLARAKSV PTKTYSNEVV TLWYRPPDVL
     LGSSEYSTQI DMWGVGCIFF EMASGRPLFP GSTVEDELHL IFRLLGTPSQ ETWPGVSSND
     EFKNYNFPKY KPQPLINHAP RLDSEGIELI TKFLQYESKK RVPAEEAMKH VYFRSLGPRI
     HALPESVSIF SLKEIQLQKD PGFRNSSYPE TGHGKNRRQS MLF
//
ID   Q8K0D1_MOUSE            Unreviewed;       857 AA.
AC   Q8K0D1;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   SubName: Full=Potassium voltage gated channel Shab-related subfamily member 1;
DE   SubName: Full=Potassium voltage gated channel, Shab-related subfamily, member 1;
GN   Name=Kcnb1; ORFNames=RP23-19L12.6-001, mCG_14614;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Johnson C.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RA   Almeida-King J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC031776; AAH31776.1; -; mRNA.
DR   EMBL; BC061501; AAH61501.1; -; mRNA.
DR   EMBL; AL591854; CAM13429.1; -; Genomic_DNA.
DR   EMBL; AL591711; CAM13429.1; JOINED; Genomic_DNA.
DR   EMBL; AL591711; CAM17304.1; -; Genomic_DNA.
DR   EMBL; AL591854; CAM17304.1; JOINED; Genomic_DNA.
DR   EMBL; CH466551; EDL06500.1; -; Genomic_DNA.
DR   IPI; IPI00331602; -.
DR   RefSeq; NP_032446.2; NM_008420.3.
DR   UniGene; Mm.387390; -.
DR   HSSP; O76457; 3KVT.
DR   ProteinModelPortal; Q8K0D1; -.
DR   SMR; Q8K0D1; 31-141.
DR   STRING; Q8K0D1; -.
DR   PRIDE; Q8K0D1; -.
DR   Ensembl; ENSMUST00000059826; ENSMUSP00000057981; ENSMUSG00000050556.
DR   GeneID; 16500; -.
DR   KEGG; mmu:16500; -.
DR   NMPDR; fig|10090.3.peg.7463; -.
DR   UCSC; uc008nzh.1; mouse.
DR   CTD; 16500; -.
DR   MGI; MGI:96666; Kcnb1.
DR   GeneTree; ENSGT00560000076807; -.
DR   HOVERGEN; HBG052225; -.
DR   InParanoid; Q8K0D1; -.
DR   OMA; IHQYIDA; -.
DR   PhylomeDB; Q8K0D1; -.
DR   NextBio; 289823; -.
DR   ArrayExpress; Q8K0D1; -.
DR   Bgee; Q8K0D1; -.
DR   Genevestigator; Q8K0D1; -.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003973; K_chnl_volt-dep_Kv2.
DR   InterPro; IPR004350; K_chnl_volt-dep_Kv2.1.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   Pfam; PF03521; Kv2channel; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01514; KV21CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01495; SHABCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
PE   2: Evidence at transcript level;
KW   Ion transport; Ionic channel; Membrane; Potassium; Potassium channel;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
SQ   SEQUENCE   857 AA;  95591 MW;  5FE2D80E58E60710 CRC64;
     MPAGMTKHGS RSTSSLPPEP MEIVRSKACS RRVRLNVGGL AHEVLWRTLD RLPRTRLGKL
     RDCNTHDSLL QVCDDYSLED NEYFFDRHPG AFTSILNFYR TGRLHMMEEM CALSFSQELD
     YWGIDEIYLE SCCQARYHQK KEQMNEELKR EAETLREREG EEFDNTCCAE KRKKLWDLLE
     KPNSSVAAKI LAIISIMFIV LSTIALSLNT LPELQSLDEF GQSTDNPQLA HVEAVCIAWF
     TMEYLLRFLS SPKKWKFFKG PLNAIDLLAI LPYYVTIFLT ESNKSVLQFQ NVRRVVQIFR
     IMRILRILKL ARHSTGLQSL GFTLRRSYNE LGLLILFLAM GIMIFSSLVF FAEKDEDDTK
     FKSIPASFWW ATITMTTVGY GDIYPKTLLG KIVGGLCCIA GVLVIALPIP IIVNNFSEFY
     KEQKRQEKAI KRREALERAK RNGSIVSMNM KDAFARSIEM MDIVVEKNGE GVAKKDKVQD
     NHLSPNKWKW TKRALSETSS SKSFETKEQG SPEKARSSSS PQHLNVQQLQ DMYSKMAKTQ
     SQPILNTKEM APQSQPQEEL EMGSMPSPVA PLPTRTEGVI DMRSMSSIDS FISCATDFPE
     ATRFSHSPLA SLSGKSGGST APEVGWRGAL GASGGRLMET NPIPEASRSG FFVESPRSSM
     KTHNPMKLRA LKVNFLEGDP TPLLPALGLY HDPLRNRGGA AAAVAGLECA SLLDKPVLSP
     ESSIYTTASA RTPPRSPEKH TAIAFNFEAG VHQYIDTDTD DEGQLLYSVD SSPPKSLHGS
     TSPKFSLGAR TEKNHFESSP LPTSPKFLRP NCVYASEGLP GKGPGAQEKC KLENHTSPDV
     HMLPGGGAHG STRDQSI
//
ID   TBC23_MOUSE             Reviewed;         684 AA.
AC   Q8K0F1; Q3TAW9; Q8VE48;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=TBC1 domain family member 23;
GN   Name=Tbc1d23;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II, and FVB/N; TISSUE=Liver, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K0F1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K0F1-2; Sequence=VSP_025520, VSP_025521;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 Rab-GAP TBC domain.
CC   -!- SIMILARITY: Contains 1 rhodanese domain.
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DR   EMBL; AK155142; BAE33073.1; -; mRNA.
DR   EMBL; AK171591; BAE42547.1; -; mRNA.
DR   EMBL; BC019762; AAH19762.1; -; mRNA.
DR   EMBL; BC031706; AAH31706.1; -; mRNA.
DR   IPI; IPI00172147; -.
DR   IPI; IPI00845632; -.
DR   RefSeq; NP_080530.2; NM_026254.2.
DR   UniGene; Mm.257819; -.
DR   ProteinModelPortal; Q8K0F1; -.
DR   PhosphoSite; Q8K0F1; -.
DR   PRIDE; Q8K0F1; -.
DR   Ensembl; ENSMUST00000023431; ENSMUSP00000023431; ENSMUSG00000022749.
DR   GeneID; 67581; -.
DR   KEGG; mmu:67581; -.
DR   UCSC; uc007znb.1; mouse.
DR   CTD; 67581; -.
DR   MGI; MGI:1914831; Tbc1d23.
DR   eggNOG; roNOG12026; -.
DR   GeneTree; ENSGT00390000000191; -.
DR   HOGENOM; HBG506499; -.
DR   HOVERGEN; HBG055636; -.
DR   InParanoid; Q8K0F1; -.
DR   OMA; NMVLAHF; -.
DR   OrthoDB; EOG4F7NJH; -.
DR   PhylomeDB; Q8K0F1; -.
DR   NextBio; 324969; -.
DR   ArrayExpress; Q8K0F1; -.
DR   Bgee; Q8K0F1; -.
DR   CleanEx; MM_TBC1D23; -.
DR   Genevestigator; Q8K0F1; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005097; F:Rab GTPase activator activity; IEA:InterPro.
DR   GO; GO:0032313; P:regulation of Rab GTPase activity; IEA:InterPro.
DR   InterPro; IPR000195; RabGAP/TBC_dom.
DR   InterPro; IPR001763; Rhodanese-like.
DR   Gene3D; G3DSA:3.40.250.10; Rhodanese-like; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF00566; TBC; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; RabGAP_TBC; 1.
DR   SUPFAM; SSF52821; Rhodanese-like; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    684       TBC1 domain family member 23.
FT                                /FTId=PRO_0000287498.
FT   DOMAIN       44    225       Rab-GAP TBC.
FT   DOMAIN      334    446       Rhodanese.
FT   MOD_RES     474    474       Phosphoserine (By similarity).
FT   MOD_RES     507    507       Phosphoserine (By similarity).
FT   MOD_RES     514    514       Phosphothreonine (By similarity).
FT   VAR_SEQ     201    203       LGS -> VIK (in isoform 2).
FT                                /FTId=VSP_025520.
FT   VAR_SEQ     204    684       Missing (in isoform 2).
FT                                /FTId=VSP_025521.
SQ   SEQUENCE   684 AA;  76426 MW;  B1DE9548FFB0A7FE CRC64;
     MAEGEELLPL STSGGDSWEK DLEEALEAGG CDLETLRNII QGRPLPAELR AKVWKIALNV
     AGKGDSLASW DGILDLPEQN TIHKDCLEFI EQLSVPEEKA AELLLDIESV ITFYCKSRSV
     KYSTSLSWIH LLKPLICLQL PRSDLYNCFY AVMNKYIPRD CSLKGRPFHL FRLLIQYHEP
     ELCSFLDTKK ITPDSYALNW LGSLFAHYCS TEVTQAIWDG YLQQADPFFI YFLMLIILVN
     TKEVILAQES DSKEEVIRFL ESTPASLNLE DIEDLFSLAQ YYCSKTPASF RKDNHHLFGS
     TLLGIKDDEA DLSQALCLAV SVSEILQANQ LQGEGVRFFV VDCRPAEQYN AGHLATAFHL
     DSDLMLQNPS EFAQSVKSLL EAQKQSIESG SIAGGEHLCF MGSGREEEDM YMNMVLAHFL
     QKNKEYVSIA SGGFMALQQH LADINVEGPE SGYGHWIAST SGSRGSISSV DGESCNGSND
     RGMKSLVSKM TVALKTKSVT VREKVISFIE NSSTPVDRHV SSSDRVGKPY RGVKPVFSIG
     DEEEYDTDEI DSSSMSDDDR KEVVNIQTWI NKPDIKHHFP CKEVKESGHM FPSHLLVTAT
     HMYCLREILS RKGLAYIQSR QALNSVVKIT SKKKHPELIT FKYGNSSASG IEILAIERYL
     IPNAGDATRA IKQQIMKVLD ALES
//
ID   TSSC1_MOUSE             Reviewed;         386 AA.
AC   Q8K0G5;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Protein TSSC1;
GN   Name=Tssc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SIMILARITY: Contains 5 WD repeats.
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DR   EMBL; BC031458; AAH31458.1; -; mRNA.
DR   IPI; IPI00321310; -.
DR   UniGene; Mm.273724; -.
DR   ProteinModelPortal; Q8K0G5; -.
DR   SMR; Q8K0G5; 175-379.
DR   STRING; Q8K0G5; -.
DR   PRIDE; Q8K0G5; -.
DR   Ensembl; ENSMUST00000035657; ENSMUSP00000038845; ENSMUSG00000036613.
DR   UCSC; uc007ngb.1; mouse.
DR   MGI; MGI:1289332; Tssc1.
DR   eggNOG; roNOG13743; -.
DR   GeneTree; ENSGT00570000079069; -.
DR   HOGENOM; HBG609636; -.
DR   HOVERGEN; HBG052937; -.
DR   InParanoid; Q8K0G5; -.
DR   OrthoDB; EOG4C5CJP; -.
DR   NextBio; 401194; -.
DR   ArrayExpress; Q8K0G5; -.
DR   Bgee; Q8K0G5; -.
DR   CleanEx; MM_TSSC1; -.
DR   Genevestigator; Q8K0G5; -.
DR   GermOnline; ENSMUSG00000036613; Mus musculus.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM00320; WD40; 5.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Repeat; WD repeat.
FT   CHAIN         1    386       Protein TSSC1.
FT                                /FTId=PRO_0000051300.
FT   REPEAT      132    172       WD 1.
FT   REPEAT      182    222       WD 2.
FT   REPEAT      226    266       WD 3.
FT   REPEAT      270    310       WD 4.
FT   REPEAT      344    384       WD 5.
FT   MOD_RES     307    307       Phosphoserine.
FT   MOD_RES     320    320       Phosphoserine (By similarity).
SQ   SEQUENCE   386 AA;  43171 MW;  15991E8D3545C0A6 CRC64;
     MEDDAPVIYG LEFQARALTP QTAETDAIRF LVGTQSLKYD NQIHIIDFDD ENNIINKNVL
     LHQAGEIWHI SASPADKGVL ATCYNKTTDS RVQACAAVWR MPKELESGSH ESPDDPASTA
     QTLELLCHLD NSAQGNVACV VWEPMGDGKK VISLADSHIL LWDLQPSSSQ AVLASSATLE
     GRGQLKFTAG RWSPHHNCTQ VATASDTTLR GWDTRSMSQI YCIENAHGQL VRDLDFNPNK
     QYYLASCGDD CKVKFWDTRN VTEPVKTLEE HSHWVWSVRY NHSHDQLVLT GSSDSRVILS
     NMVSISSEPF GHLVDDDDVS DPEEHHAEKS KEPLQDNVIA TYEEHEDSVY AVDWASADPW
     LFASLSYDGR LVINRVPRAL KYHILL
//
ID   ZBT20_MOUSE             Reviewed;         741 AA.
AC   Q8K0L9; A6X916; Q9DBD4; Q9QZ87;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Zinc finger and BTB domain-containing protein 20;
DE   AltName: Full=BTB/POZ domain zinc finger factor HOF;
DE   AltName: Full=Zinc finger protein 288;
GN   Name=Zbtb20; Synonyms=Zfp288;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING,
RP   SUBCELLULAR LOCATION, HOMODIMERIZATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Oligodendroglioma;
RX   MEDLINE=21850655; PubMed=11744704; DOI=10.1074/jbc.M110023200;
RA   Mitchelmore C., Kjaerulff K.M., Pedersen H.C., Nielsen J.V.,
RA   Rasmussen T.E., Fisker M.F., Finsen B., Pedersen K.M., Jensen N.A.;
RT   "Characterization of two novel nuclear BTB/POZ domain zinc finger
RT   isoforms. Association with differentiation of hippocampal neurons,
RT   cerebellar granule cells, and macroglia.";
RL   J. Biol. Chem. 277:7598-7609(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May be a transcription factor that may be involved in
CC       hematopoiesis, oncogenesis, and immune responses (By similarity).
CC       Binds to DNA.
CC   -!- SUBUNIT: Can homodimerize. Binds to DNA.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=HOF-L;
CC         IsoId=Q8K0L9-1; Sequence=Displayed;
CC       Name=2; Synonyms=HOF-S;
CC         IsoId=Q8K0L9-2; Sequence=VSP_032504;
CC   -!- TISSUE SPECIFICITY: Specifically expressed in early hippocampal
CC       neurons, cerebellar granule cells and gliogenic progenitors as
CC       well as in differentiated glia.
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC   -!- SIMILARITY: Contains 5 C2H2-type zinc fingers.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF194030; AAF06015.1; -; mRNA.
DR   EMBL; AK005028; BAB23755.1; -; mRNA.
DR   EMBL; CT010512; CAO77851.1; -; Genomic_DNA.
DR   EMBL; CT010512; CAO77852.1; -; Genomic_DNA.
DR   EMBL; BC031114; AAH31114.1; -; mRNA.
DR   EMBL; BC056446; AAH56446.1; -; mRNA.
DR   IPI; IPI00137338; -.
DR   IPI; IPI00856879; -.
DR   RefSeq; NP_062752.2; NM_019778.2.
DR   RefSeq; NP_851401.1; NM_181058.1.
DR   UniGene; Mm.136238; -.
DR   UniGene; Mm.440824; -.
DR   UniGene; Mm.441121; -.
DR   UniGene; Mm.441972; -.
DR   UniGene; Mm.460947; -.
DR   HSSP; O43298; 2CSH.
DR   ProteinModelPortal; Q8K0L9; -.
DR   SMR; Q8K0L9; 80-195, 471-737.
DR   PRIDE; Q8K0L9; -.
DR   Ensembl; ENSMUST00000079441; ENSMUSP00000078410; ENSMUSG00000022708.
DR   Ensembl; ENSMUST00000114694; ENSMUSP00000110342; ENSMUSG00000022708.
DR   Ensembl; ENSMUST00000114695; ENSMUSP00000110343; ENSMUSG00000022708.
DR   GeneID; 56490; -.
DR   KEGG; mmu:56490; -.
DR   UCSC; uc007zga.1; mouse.
DR   CTD; 56490; -.
DR   MGI; MGI:1929213; Zbtb20.
DR   HOGENOM; HBG714316; -.
DR   HOVERGEN; HBG060183; -.
DR   InParanoid; Q8K0L9; -.
DR   OMA; MRLHRGE; -.
DR   OrthoDB; EOG4QJRMN; -.
DR   PhylomeDB; Q8K0L9; -.
DR   ArrayExpress; Q8K0L9; -.
DR   Bgee; Q8K0L9; -.
DR   CleanEx; MM_ZBTB20; -.
DR   Genevestigator; Q8K0L9; -.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR013069; BTB_POZ.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 4.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW   Phosphoprotein; Repeat; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    741       Zinc finger and BTB domain-containing
FT                                protein 20.
FT                                /FTId=PRO_0000325961.
FT   DOMAIN      104    167       BTB.
FT   ZN_FING     578    600       C2H2-type 1.
FT   ZN_FING     606    628       C2H2-type 2.
FT   ZN_FING     634    656       C2H2-type 3.
FT   ZN_FING     662    684       C2H2-type 4.
FT   ZN_FING     715    737       C2H2-type 5.
FT   MOD_RES     432    432       Phosphoserine.
FT   VAR_SEQ       1     73       Missing (in isoform 2).
FT                                /FTId=VSP_032504.
FT   CONFLICT     88     88       N -> D (in Ref. 2; BAB23755).
FT   CONFLICT    421    421       A -> D (in Ref. 1; AAF06015).
SQ   SEQUENCE   741 AA;  81034 MW;  04C0744D66BFE418 CRC64;
     MLERKKPKTA ENQKASEENE ITQPGGSSAK PALPCLNFEA VLSPAPALIH STHSLTNSHA
     HTGSSDCDIS CKGMTERIHS INLHNFSNSV LETLNEQRNR GHFCDVTVRI HGSMLRAHRC
     VLAAGSPFFQ DKLLLGYSDI EIPSVVSVQS VQKLIDFMYS GVLRVSQSEA LQILTAASIL
     QIKTVIDECT RIVSQNVGDV FPGIQDSGQD TPRGTPESGT SGQSSDTESG YLQSHPQHSV
     DRIYSALYAC SMQNGSGERS FYSGAVVSHH ETALGLPRDH HMEDPSWITR IHERSQQMER
     YLSTTPETTH CRKQPRPVRI QTLVGNIHIK QEMEDDYDYY GQQRVQILER NESEECTEDT
     DQAEGTESEP KGESFDSGVS SSIGTEPDSV EQQFGAAAPR DGQAEPAQPE QAAEAPAESS
     AQPNQLEPGA SSPERSNESE MDNTVITVSN SSDKGVLQQP SVNTSIGQPL PSTQLYLRQT
     ETLTSNLRMP LTLTSNTQVI GTAGNTYLPA LFTTQPAGSG PKPFLFSLPQ PLTGQQTQFV
     TVSQPGLSTF TAQLPAPQPL ASSAGHSTAS GQGDKKPYEC TLCNKTFTAK QNYVKHMFVH
     TGEKPHQCSI CWRSFSLKDY LIKHMVTHTG VRAYQCSICN KRFTQKSSLN VHMRLHRGEK
     SYECYICKKK FSHKTLLERH VALHSASNGT PPAGTPPGAR AGPPGVVACT EGTTYVCSVC
     PAKFDQIEQF NDHMRMHVSD G
//
ID   PHYIP_MOUSE             Reviewed;         330 AA.
AC   Q8K0S0;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Phytanoyl-CoA hydroxylase-interacting protein;
DE   AltName: Full=Phytanoyl-CoA hydroxylase-associated protein 1;
DE            Short=PAHX-AP1;
DE            Short=PAHXAP1;
GN   Name=Phyhip;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND INTERACTION WITH PHYH.
RX   MEDLINE=20153698; PubMed=10686344; DOI=10.1016/S0169-328X(99)00304-6;
RA   Lee Z.H., Kim H.-H., Ahn K.Y., Seo K.H., Kim J.K., Bae C.S., Kim K.K.;
RT   "Identification of a brain specific protein that associates with a
RT   Refsum disease gene product, phytanoyl-CoA alpha-hydroxylase.";
RL   Brain Res. Mol. Brain Res. 75:237-247(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   OVEREXPRESSION IN HEART.
RX   PubMed=11527414; DOI=10.1006/bbrc.2001.5510;
RA   Koh J.T., Choi H.H., Ahn K.Y., Kim J.U., Kim J.H., Chun J.-Y.,
RA   Baik Y.H., Kim K.K.;
RT   "Cardiac characteristics of transgenic mice overexpressing Refsum
RT   disease gene-associated protein within the heart.";
RL   Biochem. Biophys. Res. Commun. 286:1107-1116(2001).
RN   [5]
RP   INTERACTION WITH BAI1.
RX   MEDLINE=21143048; PubMed=11245925; DOI=10.1016/S0169-328X(01)00004-3;
RA   Koh J.T., Lee Z.H., Ahn K.Y., Kim J.-K., Bae C.S., Kim H.-H.,
RA   Kee H.J., Kim K.K.;
RT   "Characterization of mouse brain-specific angiogenesis inhibitor 1
RT   (BAI1) and phytanoyl-CoA alpha-hydroxylase-associated protein 1, a
RT   novel BAI1-binding protein.";
RL   Brain Res. Mol. Brain Res. 87:223-237(2001).
RN   [6]
RP   OVEREXPRESSION IN HEART.
RX   PubMed=14672712; DOI=10.1016/j.bbrc.2003.11.105;
RA   Koh J.T., Jeong B.C., Kim J.H., Ahn Y.K., Lee H.S., Baik Y.H.,
RA   Kim K.K.;
RT   "Changes underlying arrhythmia in the transgenic heart overexpressing
RT   Refsum disease gene-associated protein.";
RL   Biochem. Biophys. Res. Commun. 313:156-162(2004).
CC   -!- FUNCTION: Its interaction with PHYH suggests a role in the
CC       development of the central system.
CC   -!- SUBUNIT: Interacts with PHYH and BAI1.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the brain.
CC   -!- DEVELOPMENTAL STAGE: At 18 dpc, expressed in most tissues,
CC       particularly in the skin. By neonatal day 1, the expression in
CC       brain and skin is markedly increased, whereas expression in the
CC       heart and skeletal muscles shows steady state levels similar to
CC       those observed in the fetus. At adulthood, very high expression in
CC       brain, little or no expression in other tissues.
CC   -!- MISCELLANEOUS: Overexpression in heart induce atrial tachycardia
CC       and increased susceptibility to aconitine-induced arrhythmia,
CC       possibly due to altered expression of voltage-gated K(1+) channel
CC       and adrenergic beta1-receptor (ADRB1).
CC   -!- SIMILARITY: Belongs to the PHYHIP family.
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH30494.2; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK049900; BAC33979.1; -; mRNA.
DR   EMBL; BC030494; AAH30494.2; ALT_INIT; mRNA.
DR   IPI; IPI00169622; -.
DR   RefSeq; NP_666093.1; NM_145981.3.
DR   UniGene; Mm.192598; -.
DR   STRING; Q8K0S0; -.
DR   PRIDE; Q8K0S0; -.
DR   Ensembl; ENSMUST00000003561; ENSMUSP00000003561; ENSMUSG00000003469.
DR   GeneID; 105653; -.
DR   KEGG; mmu:105653; -.
DR   UCSC; uc007uoa.1; mouse.
DR   CTD; 105653; -.
DR   MGI; MGI:1860417; Phyhip.
DR   eggNOG; roNOG14063; -.
DR   GeneTree; ENSGT00390000014563; -.
DR   HOGENOM; HBG443953; -.
DR   HOVERGEN; HBG053596; -.
DR   InParanoid; Q8K0S0; -.
DR   OMA; WAMENSD; -.
DR   OrthoDB; EOG4ZCT4N; -.
DR   PhylomeDB; Q8K0S0; -.
DR   NextBio; 357814; -.
DR   ArrayExpress; Q8K0S0; -.
DR   Bgee; Q8K0S0; -.
DR   CleanEx; MM_PHYHIP; -.
DR   Genevestigator; Q8K0S0; -.
DR   GermOnline; ENSMUSG00000003469; Mus musculus.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   SMART; SM00060; FN3; 1.
DR   SUPFAM; SSF49265; FN_III-like; 1.
DR   PROSITE; PS50853; FN3; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein.
FT   CHAIN         1    330       Phytanoyl-CoA hydroxylase-interacting
FT                                protein.
FT                                /FTId=PRO_0000058417.
FT   DOMAIN        3    108       Fibronectin type-III.
FT   CARBOHYD     14     14       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    325    325       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   330 AA;  37555 MW;  C87196F5D6BDA7AD CRC64;
     MELLSTPHSI EINNITCDSF RISWAMEDSD LERVTHYFID LNKKENKNSN KFKHRDVPTK
     LVAKAVPLPM TVRGHWFLSP RTEYSVAVQT AVKQSDGEYL VSGWSETVEF CTGDYAKEHL
     AQLQEKAEQI AGRMLRFSVF YRNHHKEYFQ HARTHCGNVL QPYLKDNSGS HGSPTSGMLH
     GVFFSCNTEF NTGQPPQDSP YGRWRFQIPA QRLFNPSTNL YFADFYCMYT AYHYAILVLA
     PKGSLGDRFC RDRLPLLDIA CNKFLTCSVE DGELIFRHAQ DLILEIIYTE PVDLSLGTLG
     EISGHQLMSL STADAKKDPS CKTCNISVGR
//
ID   CH047_MOUSE             Reviewed;         362 AA.
AC   Q8K0S2; Q3TS52; Q3UX98;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   RecName: Full=Uncharacterized protein C8orf47 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, and Oocyte;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-341.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC030476; AAH30476.1; -; mRNA.
DR   EMBL; BC099414; AAH99414.1; -; mRNA.
DR   EMBL; AK135792; BAE22665.1; -; mRNA.
DR   EMBL; AK162262; BAE36823.1; -; mRNA.
DR   IPI; IPI00169624; -.
DR   RefSeq; NP_775597.1; NM_173421.2.
DR   UniGene; Mm.211977; -.
DR   ProteinModelPortal; Q8K0S2; -.
DR   PRIDE; Q8K0S2; -.
DR   Ensembl; ENSMUST00000060894; ENSMUSP00000058182; ENSMUSG00000044726.
DR   GeneID; 239368; -.
DR   KEGG; mmu:239368; -.
DR   UCSC; uc007vls.1; mouse.
DR   MGI; MGI:2447772; BC030476.
DR   eggNOG; roNOG09919; -.
DR   GeneTree; ENSGT00390000010783; -.
DR   HOGENOM; HBG125392; -.
DR   HOVERGEN; HBG096287; -.
DR   InParanoid; Q8K0S2; -.
DR   OMA; QHIEGET; -.
DR   OrthoDB; EOG4VT5XZ; -.
DR   PhylomeDB; Q8K0S2; -.
DR   NextBio; 384095; -.
DR   ArrayExpress; Q8K0S2; -.
DR   Bgee; Q8K0S2; -.
DR   CleanEx; MM_BC030476; -.
DR   Genevestigator; Q8K0S2; -.
PE   2: Evidence at transcript level;
FT   CHAIN         1    362       Uncharacterized protein C8orf47 homolog.
FT                                /FTId=PRO_0000294434.
FT   COMPBIAS    295    348       Glu-rich.
SQ   SEQUENCE   362 AA;  38527 MW;  0F42E85A8388E5C7 CRC64;
     MGCSSSALNK AGDSSRFGSG VTSNENSSTV EHNKFCVDQP KPCTPGGEAA FHGNTQRESH
     PSLERPKASV VPTANGVKSY HQPSLANDET PGKEATDHSR PTKKIEPLVQ GGECEQPQPG
     GKDDMLGTEE VKKDVEARTE VPSLKGDAEI KPLRLSSERD SPGAPQAGTM KFLQTAENIL
     PLETTQELPP KEATGKGAQP QILEAIPKEN SSPEIEGIQS AESSGQQQLV EAPGEAEQPQ
     ALETVLKENE TSQMPGRSQP VPTPVMNKSP CEAPDGLRNA HEPQVTGGNR VQPAETGETA
     AKVEMAREIH PDKEEQHIEG ETGEKVEAEM KNEKESEEAE TKEKETGEAV DLGAAGAGDR
     RA
//
ID   RTN1_MOUSE              Reviewed;         780 AA.
AC   Q8K0T0; Q8K4S4;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Reticulon-1;
DE   AltName: Full=Neuroendocrine-specific protein;
GN   Name=Rtn1; Synonyms=Nsp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ICR; TISSUE=Brain;
RX   PubMed=12036513; DOI=10.1016/S0165-3806(02)00304-8;
RA   Hirata T., Nomura T., Takagi Y., Sato Y., Tomioka N., Fujisawa H.,
RA   Osumi N.;
RT   "Mosaic development of the olfactory cortex with Pax6-dependent and
RT   -independent components.";
RL   Brain Res. Dev. Brain Res. 136:17-26(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 181-190; 238-248; 647-654 AND 759-767, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   IDENTIFICATION.
RX   MEDLINE=22715887; PubMed=12832288; DOI=10.1096/fj.02-1166hyp;
RA   Oertle T., Klinger M., Stuermer C.A.O., Schwab M.E.;
RT   "A reticular rhapsody: phylogenic evolution and nomenclature of the
RT   RTN/Nogo gene family.";
RL   FASEB J. 17:1238-1247(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-350 AND SER-352, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-92; SER-350 AND
RP   SER-352, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: May be involved in neuroendocrine secretion or in
CC       membrane trafficking in neuroendocrine cells (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
CC   -!- DEVELOPMENTAL STAGE: At E12.5-E14.5, strongly expressed in radial
CC       glial fibers, which are a scaffold for migrating neurons (at
CC       protein level).
CC   -!- SIMILARITY: Contains 1 reticulon domain.
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DR   EMBL; AB074899; BAB96551.1; -; mRNA.
DR   EMBL; BC030455; AAH30455.1; -; mRNA.
DR   EMBL; BC053926; AAH53926.1; -; mRNA.
DR   EMBL; BC058579; AAH58579.1; -; mRNA.
DR   EMBL; BK001694; DAA01939.1; -; mRNA.
DR   IPI; IPI00395193; -.
DR   RefSeq; NP_001007597.1; NM_001007596.1.
DR   RefSeq; NP_703187.2; NM_153457.6.
DR   UniGene; Mm.221275; -.
DR   ProteinModelPortal; Q8K0T0; -.
DR   SMR; Q8K0T0; 643-702.
DR   STRING; Q8K0T0; -.
DR   PhosphoSite; Q8K0T0; -.
DR   PRIDE; Q8K0T0; -.
DR   Ensembl; ENSMUST00000078505; ENSMUSP00000077594; ENSMUSG00000021087.
DR   GeneID; 104001; -.
DR   KEGG; mmu:104001; -.
DR   UCSC; uc007nvk.1; mouse.
DR   CTD; 104001; -.
DR   MGI; MGI:1933947; Rtn1.
DR   GeneTree; ENSGT00390000009934; -.
DR   HOGENOM; HBG713123; -.
DR   HOVERGEN; HBG008971; -.
DR   InParanoid; Q8K0T0; -.
DR   OMA; LPFLNKQ; -.
DR   OrthoDB; EOG437RDX; -.
DR   NextBio; 356325; -.
DR   ArrayExpress; Q8K0T0; -.
DR   Bgee; Q8K0T0; -.
DR   CleanEx; MM_RTN1; -.
DR   Genevestigator; Q8K0T0; -.
DR   GermOnline; ENSMUSG00000021087; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR003388; Reticulon.
DR   PANTHER; PTHR10994; Reticulon; 1.
DR   Pfam; PF02453; Reticulon; 1.
DR   PROSITE; PS50845; RETICULON; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Membrane;
KW   Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    780       Reticulon-1.
FT                                /FTId=PRO_0000168159.
FT   TRANSMEM    607    627       Helical; (Potential).
FT   TRANSMEM    709    729       Helical; (Potential).
FT   DOMAIN      593    780       Reticulon.
FT   MOD_RES      70     70       Phosphoserine.
FT   MOD_RES      92     92       Phosphoserine.
FT   MOD_RES     350    350       Phosphoserine.
FT   MOD_RES     352    352       Phosphoserine.
FT   MOD_RES     487    487       Phosphoserine (By similarity).
FT   CONFLICT     71     71       P -> S (in Ref. 1; BAB96551).
FT   CONFLICT    226    226       D -> G (in Ref. 1; BAB96551).
SQ   SEQUENCE   780 AA;  83572 MW;  29B47A58FC2F2027 CRC64;
     MAAPPDLQDE PLSLGSPGSQ WFGGRGDGED EATAVMGARP AQQDGEPAWG SGAGAGVTSS
     RELCSGPARS PPVAMETAST GMAAVPDALD HSPSSTLKDG EGACYTSLIS DVCYPPREDS
     AYFTGILQKE NGHITTSESP EEPETPGPSL PEVPGMEPQG LLSSDSGIEM TPAESTEVNK
     ILADPLDQMK AEAYKYIDIT RPQEAKGQEE QHPGLEDKDL DFKDKDTEVS TKAEGVRAPN
     QPAPVEGKLI KDHLFEESTF APYIDELSDE QHRVSLVTAP VKITLTEIEP PLMTATQETI
     PEKQDLCLKP SPDTVPTVTV SEPEDDSPGS VTPPSSGTEP SAAESQGKGS VSEDELIAAI
     KEAKGLSYET TESPRPVGQV ADKPKTKTRS GLPTIPSPLD QEASSAESGD SEIELVSEDP
     MASEDALPSG YVSFGHVSGP PPSPASPSIQ YSILREEREA ELDSELIIES CDASSASEES
     PKREQDSPPM KPGALDAIRE ETGSRATEER APSHQGPVEP DPMLSFAPAA ALQSRPEPSS
     GDGASVPEPP RSQQQKPEEE AVSSSQSPTA TEIPGPLGSG LMPPLPFFNK QKAIDLLYWR
     DIKQTGIVFG SFLLLLFSLT QFSVVSVVAY LALAALSATI SFRIYKSVLQ AVQKTDEGHP
     FKAYLELEIT LSQEQIQKYT DCLQLYVNST LKELRRLFLV QDLVDSLKFA VLMWLLTYVG
     ALFNGLTLLL MAVVSMFTLP VVYVKHQAQV DQYLGLVRTH INTVVAKIQA KIPGAKRHAE
//
ID   KATL1_MOUSE             Reviewed;         488 AA.
AC   Q8K0T4;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Katanin p60 ATPase-containing subunit A-like 1;
DE            Short=Katanin p60 subunit A-like 1;
DE            EC=3.6.4.3;
DE   AltName: Full=p60 katanin-like 1;
GN   Name=Katnal1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Severs microtubules in vitro in an ATP-dependent manner.
CC       This activity may promote rapid reorganization of cellular
CC       microtubule arrays (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC030434; AAH30434.1; -; mRNA.
DR   IPI; IPI00114980; -.
DR   RefSeq; NP_705800.1; NM_153572.2.
DR   UniGene; Mm.397405; -.
DR   ProteinModelPortal; Q8K0T4; -.
DR   SMR; Q8K0T4; 187-482.
DR   PRIDE; Q8K0T4; -.
DR   Ensembl; ENSMUST00000047257; ENSMUSP00000043210; ENSMUSG00000041298.
DR   Ensembl; ENSMUST00000110509; ENSMUSP00000106136; ENSMUSG00000041298.
DR   GeneID; 231912; -.
DR   KEGG; mmu:231912; -.
DR   UCSC; uc009aow.1; mouse.
DR   CTD; 231912; -.
DR   MGI; MGI:2387638; Katnal1.
DR   eggNOG; roNOG09766; -.
DR   GeneTree; ENSGT00550000074466; -.
DR   HOGENOM; HBG724153; -.
DR   HOVERGEN; HBG057074; -.
DR   InParanoid; Q8K0T4; -.
DR   OMA; LRKEMPG; -.
DR   OrthoDB; EOG4F7NJX; -.
DR   PhylomeDB; Q8K0T4; -.
DR   BRENDA; 3.6.4.3; 244.
DR   NextBio; 380863; -.
DR   Bgee; Q8K0T4; -.
DR   CleanEx; MM_KATNAL1; -.
DR   Genevestigator; Q8K0T4; -.
DR   GermOnline; ENSMUSG00000041298; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008568; F:microtubule-severing ATPase activity; IEA:EC.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR015415; Vps4_C.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF09336; Vps4_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Hydrolase; Microtubule;
KW   Nucleotide-binding.
FT   CHAIN         1    488       Katanin p60 ATPase-containing subunit A-
FT                                like 1.
FT                                /FTId=PRO_0000084602.
FT   NP_BIND     246    253       ATP (Potential).
SQ   SEQUENCE   488 AA;  55165 MW;  A9BFF34DF2F44BAC CRC64;
     MNLAEICENA KKGREYALLG NYDSSMVYYQ GVIQQIQRHC QSLRDPATKA KWQQVRQELL
     EEYEQVKSIV STLESFKMDK PPDFPVSCRD EPFRDPAVWP PPVPAEHRAP PQIRRPNREV
     RPLRKDVGAG ARGLVGRAHQ ISKSDKPASR DKDYRARGRD DKARKNVQDG ASDSEIPKFD
     GAGYDKDLVE ALERDIVSRN PSIHWDDIAD LEEAKKLLRE AVVLPMWMPD FFKGIRRPWK
     GVLMVGPPGT GKTMLAKAVA TECGTTFFNV SSSTLTSKYR GESEKLVRLL FEMARFYAPT
     TIFIDEIDSI CSRRGTSDEH EASRRVKSEL LIQMDGVGGA LENDDPSKMV MVLAATNFPW
     DIDEALRRRL EKRIYIPLPT AKGRAELLKI SLREVELDPD VHLEDIADKT EGYSGADITN
     ICRDASLMAM RRRINGLSPE EIRALSKEEL QMPVTRGDLE LALKKIAKSV SAADLEKYEK
     WMVEFGSA
//
ID   UN13C_MOUSE             Reviewed;        2210 AA.
AC   Q8K0T7;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 3.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Protein unc-13 homolog C;
DE   AltName: Full=Munc13-3;
GN   Name=Unc13c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-30.
RC   TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 700-1430.
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Probably plays a role in vesicle maturation during
CC       exocytosis as a target of the diacylglycerol second messenger
CC       pathway. Probably is involved in neurotransmitter release.
CC   -!- SUBUNIT: Interacts with STX1A and/or STX1B1, VAMP2 and SNAP25 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane;
CC       Peripheral membrane protein (By similarity). Cell junction,
CC       synapse, presynaptic cell membrane; Peripheral membrane protein
CC       (By similarity). Note=Localized to presynaptic structures (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Exclusively expressed in brain.
CC   -!- DOMAIN: The C2 domains are not involved in calcium-dependent
CC       phospholipid binding (By similarity).
CC   -!- SIMILARITY: Belongs to the unc-13 family.
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -!- SIMILARITY: Contains 1 MHD1 (MUNC13 homology domain 1) domain.
CC   -!- SIMILARITY: Contains 1 MHD2 (MUNC13 homology domain 2) domain.
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH30416.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N- terminal and C-terminal parts;
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DR   EMBL; AC112267; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC124451; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC131722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC132267; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC153359; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK005367; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC030416; AAH30416.1; ALT_SEQ; mRNA.
DR   IPI; IPI00831256; -.
DR   RefSeq; NP_001074622.1; NM_001081153.1.
DR   UniGene; Mm.41035; -.
DR   ProteinModelPortal; Q8K0T7; -.
DR   SMR; Q8K0T7; 313-404, 1094-1143, 1214-1346, 2035-2169.
DR   STRING; Q8K0T7; -.
DR   PhosphoSite; Q8K0T7; -.
DR   PRIDE; Q8K0T7; -.
DR   Ensembl; ENSMUST00000075245; ENSMUSP00000074726; ENSMUSG00000062151.
DR   GeneID; 208898; -.
DR   KEGG; mmu:208898; -.
DR   CTD; 208898; -.
DR   MGI; MGI:2149021; Unc13c.
DR   eggNOG; roNOG08136; -.
DR   GeneTree; ENSGT00580000081383; -.
DR   HOGENOM; HBG505645; -.
DR   HOVERGEN; HBG108648; -.
DR   InParanoid; Q8K0T7; -.
DR   OMA; IVRDVAM; -.
DR   OrthoDB; EOG4GTKC1; -.
DR   NextBio; 372451; -.
DR   ArrayExpress; Q8K0T7; -.
DR   Bgee; Q8K0T7; -.
DR   CleanEx; MM_UNC13C; -.
DR   Genevestigator; Q8K0T7; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0001566; F:non-kinase phorbol ester receptor activity; TAS:MGI.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0007268; P:synaptic transmission; IMP:MGI.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   InterPro; IPR010439; Ca-dep_secretion_activator.
DR   InterPro; IPR014770; Munc13_1.
DR   InterPro; IPR014772; Munc13_dom-2.
DR   InterPro; IPR019558; Munc13_subgr_dom-2.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF06292; DUF1041; 1.
DR   Pfam; PF10540; Membr_traf_MHD; 1.
DR   PRINTS; PR00360; C2DOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS51258; MHD1; 1.
DR   PROSITE; PS51259; MHD2; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Coiled coil; Cytoplasm; Exocytosis;
KW   Membrane; Metal-binding; Phosphoprotein; Repeat; Synapse; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   2210       Protein unc-13 homolog C.
FT                                /FTId=PRO_0000188579.
FT   DOMAIN     1203   1309       C2 1.
FT   DOMAIN     1633   1776       MHD1.
FT   DOMAIN     1882   2024       MHD2.
FT   DOMAIN     2044   2149       C2 2.
FT   ZN_FING    1093   1143       Phorbol-ester/DAG-type.
FT   COILED      967    991       Potential.
FT   MOD_RES     433    433       Phosphoserine (By similarity).
SQ   SEQUENCE   2210 AA;  249844 MW;  ED6A02639FC6FA3F CRC64;
     MVASLFKSLI LAYIHKLCKG MFTKKLGNTT KKKENRQQKK DQDFPTAGHT KPPKLSNALK
     STVKKIAKCS STRNFSIEDE EGHKDFSLSP TFSYRVAIAN GLQTAVTNSD EDLLQELSSI
     ESSYSESFNE LRSSTENQVQ STHTMPVRRN RKSSSSLAPS EGSSDGERTL HTLKLGALRK
     LRKWKKSQEC VSSDSELSTV KKTWGIRSKS LDRTARNPKT NVLEPGFSSS GCISQTHDVM
     EMIFKELQGI SQIETELSEL RGHVNALKYS IDEISSSVEV VQSEIEQLRT GFVQARRETR
     DIHDYIKHLG HMGSKVSLRF LNVPEERHEY VESVVYQILI DKMGFSDVPN AIKIEFAQRI
     GQQRDCPNAK PRPILVYFET PQQRDSVLKK SYKLKGTGIG ISTDILTYDI RERKEKGVLP
     SSQTYESMDM KLSTPEPKAK KNAWLSPNDS DRELESDLSR SSYADSPAKG SSSKSSSKSH
     SARSKNKAAN SRTSQKSDYN KRPSQPPASS TPEKQTPHYV EATPPLWHSQ SDFFTLKLSR
     SESDFSKLCQ SYSEDFSESQ FFCRTNGSSL LSSSDRELWQ RKQEGMPALY HRLQDQGLDE
     TIPAVPGQAE IENTETVDSG MSNSMVCASG DRSNYSGSQL SLHEDLSPWK EWNQAGQGTD
     DVGLDSSTQE PFDYDTNSLS DQQLDLSSKD LDDLGKCHSD LQDDSESYDL TQDDNSSPCP
     GLDNEPQGQW VGQYDSYQEA NSNDLYPNQS HPSMMYRSQS ELQSDDSEGA QPKSWHSRLS
     IDLSDKTFKF PKFGSTLQRA KSALEVVWNK STQSLSGCED SGSSLMGRFR TLSQSTANES
     STTLDSDIYT EPYYYKAEEE EDYCEPVADS ETDYVEVMEQ VLAKLENRTS ITEVNEHIKD
     YDHPSYETPY ETPQDEGYDG QADDIISEGE LETLNEPAVE MELAEDENQN LPAESLEVMK
     PKRIRPSFKE AALRAYKKQM AELEEKILAG DSSSMDEKAR IVSGNDLDAS KFSALQVFGG
     AGRGLYGIDS MPDLRRKKTL PIVRDVAMTL AARKSGLSLA MVIRTSLNNE ELKMHVFRKT
     LQALIYPISS TTPHNFEVWT ATTPTYCYEC EGLLWGIARQ GMKCLECGVK CHEKCQDLLN
     ADCLQRAAEK SSKHGAEDKT QTIITAMKER MKIRERNRPE VFEVIQEMFQ ISKEDFVQYT
     KAAKQSVLDG TSKWSAKITI TVVSAQGLQA KDKTGSSDPY VTVQVGKNKR RTKTIFGNLN
     PVWDEKFFFE CHNSTDRIKV RVWDEDDDIK SRVKQHFKKE SDDFLGQTIV EVRTLSGEMD
     VWYNLEKRTD KSAVSGAIRL KINVEIKGEE KVAPYHIQYT CLHENLFHYL TEVKSNGSVK
     IPEVKGDEAW KVFFDDASQE IVDEFAMRYG VESIYQAMTH FSCLSSKYMC PGVPAVMSAL
     LANINAFYAH TTVSTNVQVS ASDRFAATNF GREKFIKLLD QLHNSLRIDL SKYRENFPAS
     NSERLQDLKS TVDLLTSITF FRMKVLELQS PPKASAVVKD CVRACLDSTY KYIFDNCHEL
     YSQLIDPSKK QDVPREDQGP TTKNLDFWPQ LITLMVTIID EDKTAYTPVL NQFPQELNMG
     KISAEIMWSL FALDMKYALE EHEKQRLCKS TDYMNLHFKV KWFYNEYVRE LPAFKDAVPE
     YSLWFEPFVM QWLDENEDVS MEFLHGALGR DKKDGFQQTS DHALFSCSVV DVFAQLNQSF
     EIIKKLECPN PEALSHLMRR FAKTINKVLV QYAAIVSNDF SSYCDKETVP CILMNNIQQL
     RVQLEKMFES MGGKELDPEA STILKELQIK LNGVLDALSI TYGESFQLTI EECIKQMGAE
     LNQMRANGNS TANKNSAAMD AEIVLRPLMD FLDKTLSLSA KICEKTVLKR VLKELWKLVL
     NKIEKQIVLP PLTDQTGPQM IFIAAKDLGQ LSKLKEHMIR EDAKGLTPRQ CAIVEVVLAT
     IKQYFHAGGN GLKKNFLEKS PDLHSLRYAL SLYTQTTDAL IKKFIETQGS QSRSSKDAVG
     QISVHVDVTT TPGTGDHKVT VKVIAINDLN WQTTAMFRPF VEVCMLGPSL GDKKRKQGTK
     TKSNTWSPKY NETFQFILGN ENRPGAYELH LSVKDYCFAR EDRIIGMTVI QLQNIAEKGS
     YGAWYPLLKN LSMDETGLTI LRILSQRTSD DVAKEFVRLK SETRSIEESA
//
ID   HS12A_MOUSE             Reviewed;         675 AA.
AC   Q8K0U4; Q3UQZ8; Q8CHF6;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Heat shock 70 kDa protein 12A;
GN   Name=Hspa12a; Synonyms=Kiaa0417;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 99-109; 165-177; 362-372; 398-414; 504-529;
RP   533-544; 571-585 AND 641-654, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   IDENTIFICATION, AND TISSUE SPECIFICITY.
RX   MEDLINE=22457227; PubMed=12552099; DOI=10.1073/pnas.252764399;
RA   Han Z., Truong Q.A., Park S., Breslow J.L.;
RT   "Two Hsp70 family members expressed in atherosclerotic lesions.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1256-1261(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-631, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- TISSUE SPECIFICITY: Expressed most strongly in brain, kidney and
CC       heart with little or no expression in other tissues. In the aorta,
CC       preferentially expressed in lesions.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC41423.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB093239; BAC41423.1; ALT_INIT; mRNA.
DR   EMBL; AK038491; BAC30016.1; -; mRNA.
DR   EMBL; AK141925; BAE24890.1; -; mRNA.
DR   EMBL; BC030362; AAH30362.1; -; mRNA.
DR   EMBL; AY196789; AAO37638.1; -; mRNA.
DR   IPI; IPI00279443; -.
DR   RefSeq; NP_780408.1; NM_175199.3.
DR   UniGene; Mm.39739; -.
DR   ProteinModelPortal; Q8K0U4; -.
DR   STRING; Q8K0U4; -.
DR   PhosphoSite; Q8K0U4; -.
DR   PRIDE; Q8K0U4; -.
DR   Ensembl; ENSMUST00000066285; ENSMUSP00000066860; ENSMUSG00000025092.
DR   GeneID; 73442; -.
DR   KEGG; mmu:73442; -.
DR   UCSC; uc008iaw.1; mouse.
DR   CTD; 73442; -.
DR   MGI; MGI:1920692; Hspa12a.
DR   eggNOG; roNOG14307; -.
DR   GeneTree; ENSGT00390000014360; -.
DR   HOGENOM; HBG282805; -.
DR   HOVERGEN; HBG051928; -.
DR   InParanoid; Q8K0U4; -.
DR   OMA; EIWSELE; -.
DR   OrthoDB; EOG4HX50H; -.
DR   NextBio; 338277; -.
DR   ArrayExpress; Q8K0U4; -.
DR   Bgee; Q8K0U4; -.
DR   CleanEx; MM_HSPA12A; -.
DR   Genevestigator; Q8K0U4; -.
DR   GermOnline; ENSMUSG00000025092; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   PROSITE; PS00297; HSP70_1; FALSE_NEG.
DR   PROSITE; PS00329; HSP70_2; FALSE_NEG.
DR   PROSITE; PS01036; HSP70_3; FALSE_NEG.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Nucleotide-binding;
KW   Phosphoprotein.
FT   CHAIN         1    675       Heat shock 70 kDa protein 12A.
FT                                /FTId=PRO_0000078293.
FT   MOD_RES      24     24       Phosphoserine.
FT   MOD_RES     631    631       Phosphoserine.
FT   CONFLICT    128    128       S -> N (in Ref. 1; BAC41423).
FT   CONFLICT    607    607       H -> R (in Ref. 1; BAC41423).
SQ   SEQUENCE   675 AA;  74871 MW;  36FD7ADBF58E3653 CRC64;
     MADKEAGGGD AGPRETAPTS TYSSPARSLG DTGITPLSPS HILNDADPVS EQQTFLVVVA
     IDFGTTSSGY AYSFTKEPEC IHVMRRWEGG DPGVSNQKTP TTILLTPERK FHSFGYAARD
     FYHDLDPSEA KQWLYLEKFK MKLHTTGDLT MDTDLTAANG KKVKALEIFA YALQYFKEQA
     LKELSDQAGS DFENSDVRWV ITVPAIWKQP AKQFMREAAY QAGLASPENS EQLIIALEPE
     AASIYCRKLR LHQMIELSSK AVVNGYSASD TVGAGFAQAK EHVRRNRQSR TFLVENVIGE
     IWSELEEGDK YVVVDSGGGT VDLTVHQIRL PEGHLKELYK ATGGPYGSLG VDYEFEKLLC
     KIFGEDFIEQ FKIKRPAAWV DLMIAFESRK RAAAPDRTNP LNITLPFSFI DYYKKFRGHS
     VEHALRKSNV DFVKWSSQGM LRMSPDAMNA LFKPTIDSII EHLRDLFQKP EVSTVKFLFL
     VGGFAEAPLL QQAVQTAFGD KCRIIIPQDV GLTILKGAVL FGLDPAVIKV RRSPLTYGVG
     VLNRYVEGKH PPEKLLVKDG TRWCTDVFDK FISADQSVAL GELVKRSYTP AKPSQLVIII
     NIYSSEHDNV SFITDPGVKK CGTLRLDLTG SGGTAVPARR EIQTIMQFGD TEIKATAVDI
     TTSKSVKVGI DFLNY
//
ID   RN208_MOUSE             Reviewed;         265 AA.
AC   Q8K0W3; A2AI04; B2FDG8; Q8BTC4;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=RING finger protein 208;
GN   Name=Rnf208;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 138-265.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH30073.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL732309; CAM14674.1; -; Genomic_DNA.
DR   EMBL; AL732309; CAQ52063.1; -; Genomic_DNA.
DR   EMBL; CH466542; EDL08218.1; -; Genomic_DNA.
DR   EMBL; BC030073; AAH30073.1; ALT_INIT; mRNA.
DR   EMBL; AK004344; BAC25078.1; -; mRNA.
DR   IPI; IPI00876492; -.
DR   RefSeq; NP_789804.2; NM_176834.2.
DR   UniGene; Mm.24777; -.
DR   UniGene; Mm.481727; -.
DR   HSSP; Q13049; 2CT2.
DR   ProteinModelPortal; Q8K0W3; -.
DR   SMR; Q8K0W3; 141-220.
DR   PRIDE; Q8K0W3; -.
DR   Ensembl; ENSMUST00000060818; ENSMUSP00000057742; ENSMUSG00000044628.
DR   Ensembl; ENSMUST00000114351; ENSMUSP00000109991; ENSMUSG00000044628.
DR   Ensembl; ENSMUST00000114355; ENSMUSP00000109995; ENSMUSG00000044628.
DR   GeneID; 68846; -.
DR   KEGG; mmu:68846; -.
DR   CTD; 68846; -.
DR   MGI; MGI:1916096; Rnf208.
DR   GeneTree; ENSGT00530000063798; -.
DR   HOGENOM; HBG443536; -.
DR   HOVERGEN; HBG080301; -.
DR   InParanoid; Q8K0W3; -.
DR   OMA; NQACGGD; -.
DR   OrthoDB; EOG4X3H24; -.
DR   NextBio; 328051; -.
DR   ArrayExpress; Q8K0W3; -.
DR   Bgee; Q8K0W3; -.
DR   CleanEx; MM_RNF208; -.
DR   Genevestigator; Q8K0W3; -.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Phosphoprotein; Zinc; Zinc-finger.
FT   CHAIN         1    265       RING finger protein 208.
FT                                /FTId=PRO_0000274614.
FT   ZN_FING     147    194       RING-type.
FT   MOD_RES     103    103       Phosphoserine (By similarity).
SQ   SEQUENCE   265 AA;  28390 MW;  75F13A652F6FB8BB CRC64;
     MPADPGPEVG SGWPGLLMSC LKGPHVILKM EAMKIVHPEK FPELPAATPC FPPAPRPTPT
     LAPKRAWPSD TEIIVNQACG GDMPTLEGAS HTPPLPRRPR KGSSELGFPR VAPVDEVIVN
     QYVIRPGPTA SAPSSSGPVI AGEPLECPTC GHTYNVTQRR PRVLSCLHSV CEQCLQILYE
     SCPKYKFISC PTCHRETVLF TDYGLAALAV NTSILSRLPP EALTAPSGGQ WGGESEGSCY
     QTFRQYCGAA CTCHVRNPLS ACSIM
//
ID   FEZ1_MOUSE              Reviewed;         392 AA.
AC   Q8K0X8;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Fasciculation and elongation protein zeta-1;
DE   AltName: Full=Zygin I;
DE   AltName: Full=Zygin-1;
GN   Name=Fez1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May be involved in axonal outgrowth as component of the
CC       network of molecules that regulate cellular morphology and axon
CC       guidance machinery. May participate in the transport of
CC       mitochondria and other cargos along microtubules (By similarity).
CC   -!- SUBUNIT: Homodimer. Interacts with the NH2-terminal variable
CC       region (V1) of PKC zeta and weakly with that of PKC epsilon.
CC       Interacts with UBE4B, SAP30L, and with SCOC (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome (By
CC       similarity). Cell membrane (By similarity). Note=Co-localizes with
CC       both, alpha- and gamma-tubulin. Translocated from the plasma
CC       membrane to the cytoplasm by activation of the PKC zeta (By
CC       similarity).
CC   -!- PTM: Phosphorylated by protein kinase C zeta; which enhances
CC       interaction with UBE4B and polyubiquitination (By similarity).
CC   -!- PTM: Polyubiquitinated in a UBE4B-dependent manner; which does not
CC       lead to proteasomal degradation and may be important for
CC       neurogenic activity. Polyubiquitin linkage seems to be mainly
CC       through Lys-26 (By similarity).
CC   -!- SIMILARITY: Belongs to the zygin family.
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DR   EMBL; BC029629; AAH29629.1; -; mRNA.
DR   IPI; IPI00169689; -.
DR   UniGene; Mm.5264; -.
DR   STRING; Q8K0X8; -.
DR   PhosphoSite; Q8K0X8; -.
DR   PRIDE; Q8K0X8; -.
DR   Ensembl; ENSMUST00000034630; ENSMUSP00000034630; ENSMUSG00000032118.
DR   MGI; MGI:2670976; Fez1.
DR   GeneTree; ENSGT00390000017627; -.
DR   HOGENOM; HBG444514; -.
DR   HOVERGEN; HBG005657; -.
DR   InParanoid; Q8K0X8; -.
DR   OrthoDB; EOG4SF967; -.
DR   ArrayExpress; Q8K0X8; -.
DR   Bgee; Q8K0X8; -.
DR   Genevestigator; Q8K0X8; -.
DR   GermOnline; ENSMUSG00000032118; Mus musculus.
DR   GO; GO:0005813; C:centrosome; IDA:MGI.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043015; F:gamma-tubulin binding; IDA:MGI.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR011680; FEZ.
DR   PANTHER; PTHR12394; FEZ; 1.
DR   Pfam; PF07763; FEZ; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton; Membrane;
KW   Microtubule; Phosphoprotein; Transport; Ubl conjugation.
FT   CHAIN         1    392       Fasciculation and elongation protein
FT                                zeta-1.
FT                                /FTId=PRO_0000189526.
FT   COILED      230    298       Potential.
FT   COMPBIAS     95     98       Poly-Glu.
FT   MOD_RES      58     58       Phosphoserine.
FT   MOD_RES     316    316       Phosphoserine.
SQ   SEQUENCE   392 AA;  45203 MW;  8FBD667303ADDFF5 CRC64;
     MEAPLVSLDE EFEDIRPSCT EEPEEKPQCL YGTSPHHLED PSLSELENFS SEIISFKSME
     DLVNEFDEKL NVCFRNYNAK TESLAPVKIQ LQIQEEEETL RDEEVWDALT DNYIPSLSED
     WRDPNIEALN GNSSDIEIHE KEEEEFNEKS ENDSGINEEP LLTADQVIEE TEEMMQNSPD
     PEEEEEVLEE EDGGEISSQA DSVLLQEMQA LTQTFNDNWS YEGLRHMSGS ELTELLDRVE
     GAIRDFSEEL VHQLARRDEL EFEKEVKNSF ITVLIEVQNK QREQRELMKK RRKEKGLSLQ
     SNRIEKGSQM PLKRFSMEGI SNILQSGIRQ TFGSSGADRQ YLNTVIPYEK KSSPPSVEDL
     QMLTNILFAM KEDNEKVPTL LTDYILKVLC PT
//
ID   GP153_MOUSE             Reviewed;         631 AA.
AC   Q8K0Z9; Q80T37; Q8CFK0;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Probable G-protein coupled receptor 153;
DE   AltName: Full=G-protein coupled receptor PGR1;
GN   Name=Gpr153; Synonyms=Pgr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-84.
RX   MEDLINE=22584407; PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA   Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA   Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA   Bergmann J.E., Gaitanaris G.A.;
RT   "The G protein-coupled receptor repertoires of human and mouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
CC   -!- FUNCTION: Orphan receptor.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC029098; AAH29098.2; -; mRNA.
DR   EMBL; BC037650; AAH37650.1; -; mRNA.
DR   EMBL; AY255610; AAO85122.1; -; mRNA.
DR   IPI; IPI00169712; -.
DR   RefSeq; NP_848493.1; NM_178406.2.
DR   UniGene; Mm.23235; -.
DR   ProteinModelPortal; Q8K0Z9; -.
DR   STRING; Q8K0Z9; -.
DR   PRIDE; Q8K0Z9; -.
DR   Ensembl; ENSMUST00000055754; ENSMUSP00000052742; ENSMUSG00000042804.
DR   Ensembl; ENSMUST00000105651; ENSMUSP00000101276; ENSMUSG00000042804.
DR   GeneID; 100129; -.
DR   KEGG; mmu:100129; -.
DR   UCSC; uc008wab.1; mouse.
DR   CTD; 100129; -.
DR   MGI; MGI:1916157; Gpr153.
DR   GeneTree; ENSGT00390000017213; -.
DR   HOGENOM; HBG716108; -.
DR   HOVERGEN; HBG080132; -.
DR   InParanoid; Q8K0Z9; -.
DR   OMA; SGYATLH; -.
DR   OrthoDB; EOG4FBHSK; -.
DR   PhylomeDB; Q8K0Z9; -.
DR   NextBio; 354279; -.
DR   ArrayExpress; Q8K0Z9; -.
DR   Bgee; Q8K0Z9; -.
DR   CleanEx; MM_GPR153; -.
DR   Genevestigator; Q8K0Z9; -.
DR   GermOnline; ENSMUSG00000042804; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR022335; GPCR_153.
DR   InterPro; IPR022347; GPCR_153/162.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01992; GPR153.
DR   PRINTS; PR01991; GPR153GPR162.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; FALSE_NEG.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; G-protein coupled receptor; Membrane; Receptor;
KW   Transducer; Transmembrane; Transmembrane helix.
FT   CHAIN         1    631       Probable G-protein coupled receptor 153.
FT                                /FTId=PRO_0000069638.
FT   TOPO_DOM      1     11       Extracellular (Potential).
FT   TRANSMEM     12     32       Helical; Name=1; (Potential).
FT   TOPO_DOM     33     41       Cytoplasmic (Potential).
FT   TRANSMEM     42     62       Helical; Name=2; (Potential).
FT   TOPO_DOM     63     84       Extracellular (Potential).
FT   TRANSMEM     85    105       Helical; Name=3; (Potential).
FT   TOPO_DOM    106    126       Cytoplasmic (Potential).
FT   TRANSMEM    127    147       Helical; Name=4; (Potential).
FT   TOPO_DOM    148    162       Extracellular (Potential).
FT   TRANSMEM    163    183       Helical; Name=5; (Potential).
FT   TOPO_DOM    184    243       Cytoplasmic (Potential).
FT   TRANSMEM    244    264       Helical; Name=6; (Potential).
FT   TOPO_DOM    265    276       Extracellular (Potential).
FT   TRANSMEM    277    297       Helical; Name=7; (Potential).
FT   TOPO_DOM    298    631       Cytoplasmic (Potential).
SQ   SEQUENCE   631 AA;  68459 MW;  AC171D496D66A797 CRC64;
     MSDERRLPSS AVGWLACGGL SLLANAWGIL SVGAKQKKWK PLEFLLCTLA ATHMLNVAVP
     IATYAVVQLR RQRPDYEWNE GLCKVFVSTF YTLTLATCFS VTSISYHRMW MVRWPVNYRL
     SNAKKQAVHT VMGIWMVSFI LSALPAVGWH DTSERFYTHG CRFIVAEIGL GFGVCFLLLV
     GGSVAMGMVC TAIALFQTLA TQVGHRADRR TFTVPTIVVE DAQGKRRSSI DGSEPARTSL
     QITGLVATIV VIYDCLMGFP VLVVSFSSLR ADASAPWMAL CVLWCSVTQA LLLPLFLWTC
     DRYRADLKAV WEKCVALMAN DEDSDNETSL EGSISPDMVL ERSLDYSYGG DFVALDRMAK
     YELSALEGGL PQLYPLRPLQ EDRMQYLQGA GRHRCGFPGG QPCFSPAGCS QVPPTRRFSH
     DDADVWAAVP LPTFLPRWSS GEDLAALAHL MLPAGSDRRR GSLLAFAEDA PPFRPRRRSA
     ESLLSLQPSS LDGGPRHAQD SPPGSPRRRP GPGARSASVS LLPDAFALTA FEREPQALRR
     VPAPAQPFPA ARDSAEPAEV PTPPGGRTQR SQGRRAARTH VGPLQSSLSA SWGEPGGLHA
     AGCGSISSFL SSPSESSGYV TLHSDSLGSA S
//
ID   PKHO2_MOUSE             Reviewed;         495 AA.
AC   Q8K124; Q3TCY2; Q3U4R2; Q8C1F2; Q8R140;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-FEB-2011, entry version 49.
DE   RecName: Full=Pleckstrin homology domain-containing family O member 2;
DE            Short=PH domain-containing family O member 2;
DE   AltName: Full=Pleckstrin homology domain-containing family Q member 1;
DE            Short=PH domain-containing family Q member 1;
GN   Name=Plekho2; Synonyms=Plekhq1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-233; SER-236 AND
RP   SER-279, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 PH domain.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK028069; BAC25735.1; -; mRNA.
DR   EMBL; AK154092; BAE32369.1; -; mRNA.
DR   EMBL; AK170479; BAE41823.1; -; mRNA.
DR   EMBL; BC025598; AAH25598.1; -; mRNA.
DR   EMBL; BC028908; AAH28908.1; -; mRNA.
DR   IPI; IPI00403031; -.
DR   RefSeq; NP_694759.1; NM_153119.2.
DR   UniGene; Mm.247303; -.
DR   HSSP; O08967; 1FHW.
DR   ProteinModelPortal; Q8K124; -.
DR   SMR; Q8K124; 18-120.
DR   PhosphoSite; Q8K124; -.
DR   PRIDE; Q8K124; -.
DR   Ensembl; ENSMUST00000068944; ENSMUSP00000063677; ENSMUSG00000050721.
DR   GeneID; 102595; -.
DR   KEGG; mmu:102595; -.
DR   UCSC; uc009qdl.1; mouse.
DR   CTD; 102595; -.
DR   MGI; MGI:2143132; Plekho2.
DR   eggNOG; roNOG07106; -.
DR   GeneTree; ENSGT00530000063760; -.
DR   HOGENOM; HBG268508; -.
DR   HOVERGEN; HBG096634; -.
DR   InParanoid; Q8K124; -.
DR   OMA; QEAPGLQ; -.
DR   PhylomeDB; Q8K124; -.
DR   NextBio; 355548; -.
DR   ArrayExpress; Q8K124; -.
DR   Bgee; Q8K124; -.
DR   Genevestigator; Q8K124; -.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Phosphoprotein.
FT   CHAIN         1    495       Pleckstrin homology domain-containing
FT                                family O member 2.
FT                                /FTId=PRO_0000309484.
FT   DOMAIN       18    120       PH.
FT   COILED      444    469       Potential.
FT   MOD_RES     233    233       Phosphothreonine.
FT   MOD_RES     236    236       Phosphoserine.
FT   MOD_RES     279    279       Phosphoserine.
FT   MOD_RES     395    395       Phosphoserine.
FT   CONFLICT      1      4       MEEE -> VRRWRNWAEQDKTFP (in Ref. 1;
FT                                BAE32369).
FT   CONFLICT    183    183       P -> A (in Ref. 1; BAE41823).
FT   CONFLICT    218    218       A -> P (in Ref. 1; BAE32369).
FT   CONFLICT    330    332       GSS -> TRP (in Ref. 2; AAH25598).
FT   CONFLICT    396    428       LGDLLRESPQHPRLPKEKLYRAQLEVKVASKQT -> HAGG
FT                                VEWGWGLPRLSPCPYDPPFLSFGNKPHFM (in Ref. 1;
FT                                BAC25735).
SQ   SEQUENCE   495 AA;  53872 MW;  2105D71A407498FE CRC64;
     MEEESIKEGS EKPRGARTAD KAGWIKKSSG GLLGLWKDRY LLLCQAQLLV YENEDEQKCV
     ETVELGSYEK CQDLRTLLKR KHHRFILLRS PGNKVSDIKF QAPSGEEKES WIKALNEGIN
     RGKNKAFDEV KVDKTCALEH VTRNRVRGGQ RRRPPTRIHL KEVASAASDG LSRLDLDVPD
     SGPPVFAPLS DISEDQPQEP PRALMPPVKP SPGPETSAVE DSKETPAGER ALTPDSASSG
     ANPESQEDAE TPAKEDSDVK SLPNSTLSEK LKVSWENPSP EKPSAPESAQ LSSSETPEAT
     PRESKKPPAP PPKILSEKMK ACMSGVDASG SSQSSEAPET TSPEPTQVSV NGMDDGPESA
     LQAMGIPGPA PEDAAASPAL PFSDLPSQFH PRSSSLGDLL RESPQHPRLP KEKLYRAQLE
     VKVASKQTEK LLNQVLGSEP PPVCAESLLS QAVEQLRQAT QVLQEMRDLG ELNQETPGLV
     QKRKELVTLY RRSAP
//
ID   K319L_MOUSE             Reviewed;        1048 AA.
AC   Q8K135; A2A790; Q3TTA3; Q8BHR5; Q8BHU7; Q8BHZ3; Q8VBZ9;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Dyslexia-associated protein KIAA0319-like protein;
GN   Name=Kiaa0319l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and NOD;
RC   TISSUE=Brain, Cerebellum, Embryo, Embryonic heart, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Kidney, and Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-973 AND SER-977, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Possible role in axon guidance through interaction with
CC       RTN4R (By similarity).
CC   -!- SUBUNIT: Interacts with RTN4R (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic granule membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K135-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K135-2; Sequence=VSP_032956;
CC         Note=No experimental confirmation available;
CC   -!- PTM: N-glycosylated (By similarity).
CC   -!- SIMILARITY: Contains 1 MANSC domain.
CC   -!- SIMILARITY: Contains 5 PKD domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH22154.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK043006; BAC31432.1; -; mRNA.
DR   EMBL; AK049570; BAC33818.1; -; mRNA.
DR   EMBL; AK084668; BAC39244.1; -; mRNA.
DR   EMBL; AK147569; BAE27999.1; -; mRNA.
DR   EMBL; AK161493; BAE36422.1; -; mRNA.
DR   EMBL; AK170261; BAE41669.1; -; mRNA.
DR   EMBL; AL606908; CAM19269.1; -; Genomic_DNA.
DR   EMBL; AL606908; CAM19270.1; -; Genomic_DNA.
DR   EMBL; BC022154; AAH22154.1; ALT_SEQ; mRNA.
DR   EMBL; BC028869; AAH28869.1; -; mRNA.
DR   IPI; IPI00453492; -.
DR   IPI; IPI00626472; -.
DR   RefSeq; NP_001030602.1; NM_001035525.1.
DR   RefSeq; NP_001030603.1; NM_001035526.1.
DR   RefSeq; NP_598647.1; NM_133886.2.
DR   UniGene; Mm.206206; -.
DR   ProteinModelPortal; Q8K135; -.
DR   SMR; Q8K135; 297-401, 403-594, 599-687, 689-784.
DR   PRIDE; Q8K135; -.
DR   Ensembl; ENSMUST00000047431; ENSMUSP00000037802; ENSMUSG00000028830.
DR   Ensembl; ENSMUST00000102607; ENSMUSP00000099667; ENSMUSG00000028830.
DR   Ensembl; ENSMUST00000102608; ENSMUSP00000099668; ENSMUSG00000028830.
DR   GeneID; 100317; -.
DR   KEGG; mmu:100317; -.
DR   UCSC; uc008utw.1; mouse.
DR   MGI; MGI:2140475; AU040320.
DR   GeneTree; ENSGT00390000006285; -.
DR   HOVERGEN; HBG057130; -.
DR   OrthoDB; EOG4B8JC7; -.
DR   NextBio; 354386; -.
DR   ArrayExpress; Q8K135; -.
DR   Bgee; Q8K135; -.
DR   Genevestigator; Q8K135; -.
DR   GO; GO:0044433; C:cytoplasmic vesicle part; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013980; MANSC.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR002859; PKD/REJ-like.
DR   InterPro; IPR000601; PKD_dom.
DR   Gene3D; G3DSA:2.60.40.670; PKD; 3.
DR   Pfam; PF02010; REJ; 2.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00089; PKD; 5.
DR   SUPFAM; SSF49299; PKD; 4.
DR   PROSITE; PS50986; MANSC; 1.
DR   PROSITE; PS50093; PKD; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Glycoprotein; Membrane; Phosphoprotein; Repeat;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1   1048       Dyslexia-associated protein KIAA0319-like
FT                                protein.
FT                                /FTId=PRO_0000329065.
FT   TOPO_DOM      1     29       Cytoplasmic (Potential).
FT   TRANSMEM     30     50       Helical; (Potential).
FT   TOPO_DOM     51    928       Extracellular (Potential).
FT   TRANSMEM    929    949       Helical; (Potential).
FT   TOPO_DOM    950   1048       Cytoplasmic (Potential).
FT   DOMAIN       49    127       MANSC.
FT   DOMAIN      309    400       PKD 1.
FT   DOMAIN      408    497       PKD 2.
FT   DOMAIN      503    593       PKD 3.
FT   DOMAIN      599    687       PKD 4.
FT   DOMAIN      693    784       PKD 5.
FT   MOD_RES     973    973       Phosphothreonine.
FT   MOD_RES     977    977       Phosphoserine.
FT   CARBOHYD    246    246       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    394    394       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ    1025   1048       YGQNGSVPNGQTPLKSRSAREEIL -> ALHWCRSQSLHHI
FT                                GWWCRAPVCHETSSTNSTPGSDSGFCKGGKNLSSDYRTRTK
FT                                SALVHGK (in isoform 2).
FT                                /FTId=VSP_032956.
FT   CONFLICT      4      4       R -> G (in Ref. 1; BAC39244).
FT   CONFLICT    579    579       Missing (in Ref. 1; BAE36422).
FT   CONFLICT    656    656       G -> V (in Ref. 1; BAC33818).
FT   CONFLICT    684    684       V -> A (in Ref. 1; BAC33818).
SQ   SEQUENCE   1048 AA;  115312 MW;  F4D51DD6DE4C889D CRC64;
     MEKRLGVKPS PASWVLPGYC WQTSVKLPRS LYLLYSFFCF SVLWLSTDAD ESRCQQGKTL
     YGAGLRTEGE NHLRLLAGSL PFHACRAACC RDSACHALWW LEGMCFQADC SKPQSCQPFR
     TDSSNSMLII FQKSQTTDDL GLLPEDDEPH LLRLGWGRTS WRRQSLLGAP LTLSVPSSHH
     QSLLRDRQKR DLSVVPTHGA MQHSKVNHSE EAGALSPTSA EVRKTITVAG SFTSNHTTQT
     PEWPKNVSIH PEPSEHSSPV SGTPQVKSTE HSPTDAPLPV APSYSYATPT PQASSQSTSA
     PHPVVKELVV SAGKSVQITL PKNEVQLNAF VLPEAEPGET YTYDWQLITH PTDYSGEVER
     KHSQSLQLSK LTPGLYEFKV TVDGQNAHGE GYVNVTVKPE PRKNRPPVAV VSPQFQEISL
     PTTSTIIDGS QSTDDDKIVQ YHWEELKGPL REEKISEDTA ILKLSKLVPG NYTFSLTVVD
     SDGATNSTTA SLTVNKAVDY PPVANAGPNQ VITLPQNSIT LFGNQSTDDH GITSYEWSLS
     PSSKGKVVEM QGVRTPALQL SAMQEGDYTY QLTVTDTAGQ QATAQVTVIV QPENNKPPQA
     DAGPDKELTL PVDSTTLDGS KSTDDQRVVS YLWEQSRGPD GVQLENANSS VATVTGLQVG
     TYVFTLTVKD ERNLQSQSSV NVIVKEEINK PPVAKIAGNV VVTLPTSTAE LDGSRSSDDK
     GIVSYLWTRD ETSPAAGEVL NHSDHHPVLF LSNLVEGTYT FHLKVTDAKG ESDTDRTTVE
     VKPDPRKSNL VEIILDVNVS QLTERLKGML IRQIGVLLGV LDSDIIVQKI QPYTEQSTKM
     LFFVQNDPPH QLFKGHEVAA MLKSELQKQK ADFLIFRALE ISTVTCQLNC SDHGHCDSFT
     KRCVCDPFWM ENFIKVQLRD GDSNCEWSVL YVIIASFVIV VALGILSWTT ICCCKRQKGK
     PKRKSRYKIL DATDQESLEL KPTSRAGSKQ KGPTLSSSLM HSESELDSDD AIFTWPDREK
     GKLLYGQNGS VPNGQTPLKS RSAREEIL
//
ID   SCNM1_MOUSE             Reviewed;         229 AA.
AC   Q8K136; Q9CXV5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-FEB-2011, entry version 49.
DE   RecName: Full=Sodium channel modifier 1;
GN   Name=Scnm1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION OF ISOFORMS 2 AND 3, FUNCTION, SUBCELLULAR LOCATION,
RP   AND DISEASE.
RX   PubMed=12920299; DOI=10.1126/science.1086187;
RA   Buchner D.A., Trudeau M., Meisler M.H.;
RT   "SCNM1, a putative RNA splicing factor that modifies disease severity
RT   in mice.";
RL   Science 301:967-969(2003).
CC   -!- FUNCTION: May function as a RNA splicing factor.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8K136-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K136-2; Sequence=VSP_021491;
CC         Note=Only found in strains C57BL/6J, C57BR/cdJ, C57BL/KsJ
CC         C57L/J, C57BL/10J and C58/J;
CC       Name=3;
CC         IsoId=Q8K136-3; Sequence=VSP_021490;
CC   -!- DISEASE: Note=Isoform 2 modifies the severity of the disease
CC       jolting mutant (medjo) caused by defects in Scn8a. It reduces the
CC       abundance of correctly spliced Scn8a transcripts below the
CC       threshold for survival thereby converting a chronic movement
CC       disorder into a lethal neurological disease.
CC   -!- SIMILARITY: Contains 1 matrin-type zinc finger.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK013948; BAB29077.1; -; mRNA.
DR   EMBL; BC028867; AAH28867.1; -; mRNA.
DR   IPI; IPI00110870; -.
DR   IPI; IPI00798505; -.
DR   IPI; IPI00798577; -.
DR   RefSeq; NP_001157045.1; NM_001163573.1.
DR   RefSeq; NP_081289.2; NM_027013.2.
DR   UniGene; Mm.182944; -.
DR   STRING; Q8K136; -.
DR   PhosphoSite; Q8K136; -.
DR   PRIDE; Q8K136; -.
DR   Ensembl; ENSMUST00000005770; ENSMUSP00000005770; ENSMUSG00000005629.
DR   Ensembl; ENSMUST00000107226; ENSMUSP00000102845; ENSMUSG00000005629.
DR   GeneID; 69269; -.
DR   KEGG; mmu:69269; -.
DR   UCSC; uc008qid.1; mouse.
DR   CTD; 69269; -.
DR   MGI; MGI:1341284; Scnm1.
DR   eggNOG; roNOG11702; -.
DR   GeneTree; ENSGT00390000010811; -.
DR   HOGENOM; HBG444480; -.
DR   HOVERGEN; HBG093936; -.
DR   InParanoid; Q8K136; -.
DR   OMA; RWVKDEN; -.
DR   NextBio; 328997; -.
DR   ArrayExpress; Q8K136; -.
DR   Bgee; Q8K136; -.
DR   CleanEx; MM_SCNM1; -.
DR   Genevestigator; Q8K136; -.
DR   GermOnline; ENSMUSG00000005629; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IMP:MGI.
DR   PROSITE; PS50171; ZF_MATRIN; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Metal-binding; mRNA processing; mRNA splicing;
KW   Nucleus; Phosphoprotein; Zinc; Zinc-finger.
FT   CHAIN         1    229       Sodium channel modifier 1.
FT                                /FTId=PRO_0000259636.
FT   ZN_FING      42     74       Matrin-type.
FT   MOTIF         4     20       Bipartite nuclear localization signal
FT                                (Potential).
FT   MOD_RES     182    182       Phosphoserine (By similarity).
FT   MOD_RES     218    218       Phosphoserine (By similarity).
FT   VAR_SEQ     132    196       Missing (in isoform 3).
FT                                /FTId=VSP_021490.
FT   VAR_SEQ     187    229       Missing (in isoform 2).
FT                                /FTId=VSP_021491.
SQ   SEQUENCE   229 AA;  25823 MW;  BFE63B0E8A3361B9 CRC64;
     MSFKREGDDW SQLNVLKKRR VGDLLASYIP EDEALMLRDG RFACAICPHR PVLDTLAMLT
     AHRAGKKHLS SLKLFYGKKQ TGKGTEQNPR QQNELKTESK TEAPLLTQTR IITQNALHRA
     PHYNSCCRRK HRPEAPAPSV SSPPLPTAEV QLQSAEISKE PEPRERSDAK ESAALLASAP
     MSPTKRRVLN HYLTLRSSGW VPDGRGRWIK DENVEFDSDE EEPPDLPLD
//
ID   CP061_MOUSE             Reviewed;          79 AA.
AC   Q8K199; Q8CEV6;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Uncharacterized protein C16orf61 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the CMC1 family.
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DR   EMBL; AK002429; BAC24989.1; -; mRNA.
DR   EMBL; AK013475; BAC25407.1; -; mRNA.
DR   EMBL; BC027549; AAH27549.1; -; mRNA.
DR   IPI; IPI00169713; -.
DR   RefSeq; NP_081120.2; NM_026844.3.
DR   UniGene; Mm.4011; -.
DR   PRIDE; Q8K199; -.
DR   Ensembl; ENSMUST00000078589; ENSMUSP00000077663; ENSMUSG00000014633.
DR   GeneID; 66531; -.
DR   KEGG; mmu:66531; -.
DR   UCSC; uc009nom.1; mouse.
DR   MGI; MGI:1913781; 2310061C15Rik.
DR   eggNOG; roNOG16951; -.
DR   GeneTree; ENSGT00390000016908; -.
DR   HOGENOM; HBG715684; -.
DR   HOVERGEN; HBG045487; -.
DR   InParanoid; Q8K199; -.
DR   OMA; CHKEHNV; -.
DR   NextBio; 321952; -.
DR   ArrayExpress; Q8K199; -.
DR   Bgee; Q8K199; -.
DR   CleanEx; MM_2310061C15RIK; -.
DR   Genevestigator; Q8K199; -.
DR   GermOnline; ENSMUSG00000014633; Mus musculus.
DR   InterPro; IPR013892; Cyt_c_biogenesis_Cmc1-like.
DR   Pfam; PF08583; Cmc1; 1.
PE   2: Evidence at transcript level;
FT   CHAIN         1     79       Uncharacterized protein C16orf61 homolog.
FT                                /FTId=PRO_0000192944.
SQ   SEQUENCE   79 AA;  9419 MW;  27B3EDBAEBB3F54A CRC64;
     MHPDLSPHLH TEECNVLINL LKECHKNHNI LKFFGHCNDL DREMRKCLKN EYSERRTRSR
     EHGAAMRRRL SDPPEEAGR
//
ID   TM41B_MOUSE             Reviewed;         291 AA.
AC   Q8K1A5; Q3TKT0; Q3TLK6; Q8C1X2; Q8CBS5; Q8CBU5;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Transmembrane protein 41B;
GN   Name=Tmem41b; Synonyms=D7Ertd743e, Kiaa0033;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Pancreatic islet;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Blastocyst, Bone marrow, Cerebellum, Colon, Diencephalon, Egg,
RC   Head, Hypothalamus, Mammary gland, Spleen, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Eye, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8K1A5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K1A5-2; Sequence=VSP_026319;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8K1A5-3; Sequence=VSP_026318;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the TMEM41 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK172876; BAD32154.1; -; mRNA.
DR   EMBL; AK029327; BAC26397.1; -; mRNA.
DR   EMBL; AK033997; BAC28541.1; -; mRNA.
DR   EMBL; AK035266; BAC29008.1; -; mRNA.
DR   EMBL; AK035365; BAC29048.1; -; mRNA.
DR   EMBL; AK038953; BAC30179.1; -; mRNA.
DR   EMBL; AK078357; BAC37235.1; -; mRNA.
DR   EMBL; AK090100; BAC41091.1; -; mRNA.
DR   EMBL; AK139961; BAE24197.1; -; mRNA.
DR   EMBL; AK150353; BAE29490.1; -; mRNA.
DR   EMBL; AK153048; BAE31676.1; -; mRNA.
DR   EMBL; AK165226; BAE38087.1; -; mRNA.
DR   EMBL; AK166427; BAE38770.1; -; mRNA.
DR   EMBL; AK166455; BAE38786.1; -; mRNA.
DR   EMBL; AK166845; BAE39064.1; -; mRNA.
DR   EMBL; BC026515; AAH26515.1; -; mRNA.
DR   EMBL; BC027103; AAH27103.1; -; mRNA.
DR   IPI; IPI00309972; -.
DR   IPI; IPI00848962; -.
DR   IPI; IPI00849143; -.
DR   RefSeq; NP_705745.3; NM_153525.5.
DR   UniGene; Mm.43212; -.
DR   ProteinModelPortal; Q8K1A5; -.
DR   PRIDE; Q8K1A5; -.
DR   Ensembl; ENSMUST00000094097; ENSMUSP00000091641; ENSMUSG00000047554.
DR   Ensembl; ENSMUST00000118429; ENSMUSP00000112574; ENSMUSG00000047554.
DR   GeneID; 233724; -.
DR   KEGG; mmu:233724; -.
DR   UCSC; uc009jen.1; mouse.
DR   CTD; 233724; -.
DR   MGI; MGI:1289225; Tmem41b.
DR   eggNOG; roNOG09329; -.
DR   GeneTree; ENSGT00520000055582; -.
DR   HOGENOM; HBG380268; -.
DR   HOVERGEN; HBG108584; -.
DR   InParanoid; Q8K1A5; -.
DR   OMA; AYFATYV; -.
DR   OrthoDB; EOG4XD3RT; -.
DR   PhylomeDB; Q8K1A5; -.
DR   NextBio; 381795; -.
DR   ArrayExpress; Q8K1A5; -.
DR   Bgee; Q8K1A5; -.
DR   CleanEx; MM_TMEM41B; -.
DR   Genevestigator; Q8K1A5; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR015414; SNARE_assoc.
DR   Pfam; PF09335; SNARE_assoc; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    291       Transmembrane protein 41B.
FT                                /FTId=PRO_0000291938.
FT   TRANSMEM     52     72       Helical; (Potential).
FT   TRANSMEM    109    129       Helical; (Potential).
FT   TRANSMEM    147    169       Helical; (Potential).
FT   TRANSMEM    197    217       Helical; (Potential).
FT   TRANSMEM    225    245       Helical; (Potential).
FT   TRANSMEM    262    282       Helical; (Potential).
FT   MOD_RES      18     18       Phosphothreonine (By similarity).
FT   MOD_RES      35     35       Phosphoserine (By similarity).
FT   VAR_SEQ       1     85       Missing (in isoform 3).
FT                                /FTId=VSP_026318.
FT   VAR_SEQ       1     67       Missing (in isoform 2).
FT                                /FTId=VSP_026319.
FT   CONFLICT     34     34       G -> D (in Ref. 2; BAE38770/BAE38786).
FT   CONFLICT    104    104       K -> Q (in Ref. 2; BAC41091).
FT   CONFLICT    109    109       F -> L (in Ref. 2; BAC29048).
FT   CONFLICT    252    252       H -> Y (in Ref. 2; BAE38770/BAE38786).
FT   CONFLICT    262    262       S -> P (in Ref. 2; BAC41091).
FT   CONFLICT    264    264       S -> N (in Ref. 2; BAE38770/BAE38786).
FT   CONFLICT    271    271       V -> I (in Ref. 2; BAE38770/BAE38786).
FT   CONFLICT    285    285       Q -> K (in Ref. 2; BAE38770/BAE38786).
SQ   SEQUENCE   291 AA;  32429 MW;  337B420282D69149 CRC64;
     MAKGRVADRS PTEMLHSTPA GDRAVRTQGS AAPGSKDHLN EKPCAEAGSA RTSLLILVSI
     FSCAAFVMFL VYKNFPQLSE EERVNMKVPR DMDDAKALGK VLSKYKDTFY VQVLVAYFAT
     YIFLQTFAIP GSIFLSILSG FLYPFPLALF LVCLCSGLGA SFCYMLSYLV GRPVVYKYLT
     EKAVKWSQQV ERHREHLINY IIFLRITPFL PNWFINITSP VINVPLKVFF IGTFLGVAPP
     SFVAIKAGTT LHQLTTAGEA VSWSSVFILM VLALLSILPA IFQKQLKQKF E
//
ID   C2D1A_MOUSE             Reviewed;         943 AA.
AC   Q8K1A6; Q2MJB5; Q8R3Z4;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 2.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Coiled-coil and C2 domain-containing protein 1A;
DE   AltName: Full=Five repressor element under dual repression-binding protein 1;
DE            Short=FRE under dual repression-binding protein 1;
DE            Short=Freud-1;
GN   Name=Cc2d1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 301-943, AND FUNCTION.
RC   STRAIN=Swiss Webster;
RX   MEDLINE=22799051; PubMed=12917378;
RA   Ou X.-M., Lemonde S., Jafar-Nejad H., Bown C.D., Goto A., Rogaeva A.,
RA   Albert P.R.;
RT   "Freud-1: a neuronal calcium-regulated repressor of the 5-HT1A
RT   receptor gene.";
RL   J. Neurosci. 23:7415-7425(2003).
RN   [3]
RP   FUNCTION.
RX   PubMed=14756806;
RA   Lemonde S., Rogaeva A., Albert P.R.;
RT   "Cell type-dependent recruitment of trichostatin A-sensitive
RT   repression of the human 5-HT1A receptor gene.";
RL   J. Neurochem. 88:857-868(2004).
RN   [4]
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=16033914; DOI=10.1136/jmg.2005.035709;
RA   Basel-Vanagaite L., Attia R., Yahav M., Ferland R.J., Anteki L.,
RA   Walsh C.A., Olender T., Straussberg R., Magal N., Taub E.,
RA   Drasinover V., Alkelai A., Bercovich D., Rechavi G., Simon A.J.,
RA   Shohat M.;
RT   "The CC2D1A, a member of a new gene family with C2 domains, is
RT   involved in autosomal recessive non-syndromic mental retardation.";
RL   J. Med. Genet. 43:203-210(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Transcription factor that binds specifically to the FRE
CC       (five repressor element) and represses HTR1A gene transcription in
CC       neuronal cells. The combination of calcium and ATP specifically
CC       inactivates the binding with FRE. May play a role in the altered
CC       regulation of HTR1A associated with anxiety and major depression.
CC       Mediates HDAC-independent repression of HTR1A promoter in neuronal
CC       cell.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in brain.
CC   -!- DEVELOPMENTAL STAGE: Expressed at E12 throughout the ventricular
CC       zone and developing cortical plate and ganglionic eminences. At
CC       E16 detected throughout the brain but most strongly in the
CC       cortical plate. At postnatal day 3 expressed widely with strong
CC       expression in cerebral cortex and hippocampus.
CC   -!- DOMAIN: The C2 domain is required for the repression.
CC   -!- SIMILARITY: Belongs to the CC2D1 family.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH16188.1; Type=Erroneous initiation;
CC       Sequence=AAH27028.1; Type=Erroneous initiation;
CC       Sequence=ABC56419.1; Type=Frameshift; Positions=331, 338, 342;
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DR   EMBL; BC016188; AAH16188.1; ALT_INIT; mRNA.
DR   EMBL; BC027028; AAH27028.1; ALT_INIT; mRNA.
DR   EMBL; DQ329239; ABC56419.1; ALT_SEQ; mRNA.
DR   IPI; IPI00321848; -.
DR   RefSeq; NP_666082.2; NM_145970.1.
DR   UniGene; Mm.41424; -.
DR   ProteinModelPortal; Q8K1A6; -.
DR   STRING; Q8K1A6; -.
DR   PhosphoSite; Q8K1A6; -.
DR   PRIDE; Q8K1A6; -.
DR   Ensembl; ENSMUST00000040383; ENSMUSP00000046449; ENSMUSG00000036686.
DR   GeneID; 212139; -.
DR   KEGG; mmu:212139; -.
DR   NMPDR; fig|10090.3.peg.18862; -.
DR   UCSC; uc009mma.1; mouse.
DR   CTD; 212139; -.
DR   MGI; MGI:2384831; Cc2d1a.
DR   eggNOG; roNOG07697; -.
DR   HOGENOM; HBG713884; -.
DR   HOVERGEN; HBG100866; -.
DR   InParanoid; Q8K1A6; -.
DR   OMA; KGDQRKA; -.
DR   OrthoDB; EOG41C6W0; -.
DR   NextBio; 373476; -.
DR   ArrayExpress; Q8K1A6; -.
DR   Bgee; Q8K1A6; -.
DR   CleanEx; MM_CC2D1A; -.
DR   Genevestigator; Q8K1A6; -.
DR   GermOnline; ENSMUSG00000036686; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR006608; DM14.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00685; DM14; 4.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   PROSITE; PS50004; C2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN         1    943       Coiled-coil and C2 domain-containing
FT                                protein 1A.
FT                                /FTId=PRO_0000239610.
FT   DOMAIN      635    748       C2.
FT   COILED      339    385       Potential.
FT   COILED      477    510       Potential.
FT   COMPBIAS    305    338       Pro-rich.
FT   MOD_RES     435    435       Phosphoserine.
FT   CONFLICT    446    446       Q -> H (in Ref. 2; ABC56419).
FT   CONFLICT    863    863       P -> S (in Ref. 2; ABC56419).
SQ   SEQUENCE   943 AA;  103698 MW;  A730FF6E950DFA81 CRC64;
     MHKRNGPQAP PGRGAVTARQ LGLLVDFSPD GLMIPEDGIN EEELEAEFLA LVGGQPQALE
     KLKGQGPLPM EAIEKMARLC MRDLDEDEEG TDEDDVEADE DLLAELNEVL GEEQKAVEPL
     MPVAQPKPSG PNPGVEATLQ ERLTLYQSAL ESARQAGDSA KMRRYDRGLK TLENLLVSAK
     KGNIINEADI PPPVASGKGA AAGHSHTQAT SQLASVSPPA PESSGTLEAP STTTPTSAKP
     QLPPDPCSPL ARLQSLQHEY KLAALRAKHQ DDTATATRHL RIAKSFDPVL EALSRGELVD
     LSRLPPPPDQ LSPEPPLPAA QPLTSASTLT RPEVPQPPRN LLEALEQRME RYHVAAAQAK
     AKGDQRKARM HERIVKQYQD AIRAHKAGRA VDVAELPVPP GFPPMQGLES AEPSQQSLVG
     VLETAMRLAN HDEGSDDEEE ETPKKQNTPA ASTTQLKSSP SKAPPSGPAP AGKAAPKGTS
     NRAQQQLAFL EGRKKQLLQA ALRAKQKNDV EGAKMHLRQA KGLEPMLEAS RNGLPVDIAK
     VPPAPVNKDD FVLVQRPGPG LSQEAVRRYG ELTKLLRQQH EMCLNHSTQF THLGNIAETI
     KFEKLAEDCK RSMDTLKQAF ARSLPTPAAR FEQRTFSVIK VFPDLSNSDM LLFIVKGINL
     PTPTGLSPSD LDAFVRFDFP YPNVEEAQKD KTSVIKNTDS PEFKEQFKLC INRGHRGFRR
     AIQTKGIKFE VVHKGGLFKT DRVLGTAQLK LGTLETACEV HEILEVLDGR RPTGGRLEVM
     VRIREPLTAQ QLETTTERWL VIDHIPAAMP TVTGPKAKAP LIPASSREAG NRSARPLHSL
     SVLAFDQERL ERKILALRQA RRPVPPEVAQ QYQDVVQRSQ WQRAQLEQGG AALRREYASH
     LERQLHFYTE AARRLGYDGS REAAKEALYR RNLVESELQR LRR
//
ID   MOT14_MOUSE             Reviewed;         512 AA.
AC   Q8K1C7; Q9D1K0;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Monocarboxylate transporter 14;
DE            Short=MCT 14;
DE   AltName: Full=Solute carrier family 16 member 14;
GN   Name=Slc16a14; Synonyms=Mct14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Proton-linked monocarboxylate transporter. Catalyzes the
CC       rapid transport across the plasma membrane of many
CC       monocarboxylates (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC       Monocarboxylate porter (TC 2.A.1.13) family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB22782.1; Type=Erroneous initiation;
CC       Sequence=BAC33953.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK003423; BAB22782.1; ALT_INIT; mRNA.
DR   EMBL; AK049846; BAC33953.1; ALT_INIT; mRNA.
DR   EMBL; BC023456; AAH23456.1; -; mRNA.
DR   IPI; IPI00172178; -.
DR   RefSeq; NP_082197.1; NM_027921.1.
DR   UniGene; Mm.158754; -.
DR   ProteinModelPortal; Q8K1C7; -.
DR   PRIDE; Q8K1C7; -.
DR   Ensembl; ENSMUST00000027422; ENSMUSP00000027422; ENSMUSG00000026220.
DR   GeneID; 71781; -.
DR   KEGG; mmu:71781; -.
DR   UCSC; uc007btd.1; mouse.
DR   CTD; 71781; -.
DR   MGI; MGI:1919031; Slc16a14.
DR   eggNOG; roNOG08758; -.
DR   GeneTree; ENSGT00560000076727; -.
DR   HOGENOM; HBG280487; -.
DR   HOVERGEN; HBG094888; -.
DR   InParanoid; Q8K1C7; -.
DR   OMA; CRQTAII; -.
DR   OrthoDB; EOG4C87S4; -.
DR   PhylomeDB; Q8K1C7; -.
DR   NextBio; 334508; -.
DR   ArrayExpress; Q8K1C7; -.
DR   Bgee; Q8K1C7; -.
DR   Genevestigator; Q8K1C7; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   InterPro; IPR020846; Major_facilitator_SF.
DR   InterPro; IPR011701; MFS_1.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Symport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    512       Monocarboxylate transporter 14.
FT                                /FTId=PRO_0000288924.
FT   TOPO_DOM      1     29       Extracellular (Potential).
FT   TRANSMEM     30     50       Helical; (Potential).
FT   TOPO_DOM     51     75       Cytoplasmic (Potential).
FT   TRANSMEM     76     96       Helical; (Potential).
FT   TOPO_DOM     97    104       Extracellular (Potential).
FT   TRANSMEM    105    125       Helical; (Potential).
FT   TOPO_DOM    126    128       Cytoplasmic (Potential).
FT   TRANSMEM    129    149       Helical; (Potential).
FT   TOPO_DOM    150    160       Extracellular (Potential).
FT   TRANSMEM    161    181       Helical; (Potential).
FT   TOPO_DOM    182    192       Cytoplasmic (Potential).
FT   TRANSMEM    193    211       Helical; (Potential).
FT   TOPO_DOM    212    316       Extracellular (Potential).
FT   TRANSMEM    317    337       Helical; (Potential).
FT   TOPO_DOM    338    354       Cytoplasmic (Potential).
FT   TRANSMEM    355    375       Helical; (Potential).
FT   TOPO_DOM    376    380       Extracellular (Potential).
FT   TRANSMEM    381    401       Helical; (Potential).
FT   TOPO_DOM    402    409       Cytoplasmic (Potential).
FT   TRANSMEM    410    430       Helical; (Potential).
FT   TOPO_DOM    431    445       Extracellular (Potential).
FT   TRANSMEM    446    466       Helical; (Potential).
FT   TOPO_DOM    467    475       Cytoplasmic (Potential).
FT   TRANSMEM    476    496       Helical; (Potential).
FT   TOPO_DOM    497    512       Extracellular (Potential).
SQ   SEQUENCE   512 AA;  56476 MW;  347B725EE7103A63 CRC64;
     MYTSHEDIGY DLEDDRKAKN KKTLKPHPDI DGGWAWMMVL SSFFVHILIM GSQMALGVLN
     VEWLEEFHQS RGLTAWVSSL SMGITLIVGP FIGLFINTCG CRQTAIIGGL VNSLGWVLSA
     YAANVQSLFI TFGVAAGLGS GMAYLPAVVM VGRYFQKRRA LAQGLSTTGT GFGTFLMTVL
     LKYLCAEYGW RNAMFIQGAL SLNLCVCGAL MRPLSPEKLE NCPEAEEPCA LPAYSTESVK
     SGGPLGMAEE QDRRPGNEEM VCDLQTQECQ GQTHPRKNVC AFRVLKTVSQ LTVQVRRGFR
     DWHSGYFGTA SLFTNRMFVA FIFWALFAYS SFVIPFIHLP EIVSLYNLSE QNDTFPLTSI
     IAILHIFGKV ILGAVADLPC ISVWNVFLIA NFTLVLSIFL LPLMHTYASL AVICALIGFS
     SGYFSLMPVV TEDLVGTEHL ANAYGIIICA NGISALLGPP FAGWIFDITQ KYDFSFYICG
     LLYMVGILFL LIQPCIQMID QSRRKCIEGA HV
//
ID   LBN_MOUSE               Reviewed;        1220 AA.
AC   Q8K1G2; Q8BRF3;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Limbin;
GN   Name=Evc2; Synonyms=Lbn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Limb bud;
RX   MEDLINE=22155879; PubMed=12136126; DOI=10.1073/pnas.152337899;
RA   Takeda H., Takami M., Oguni T., Tsuji T., Yoneda K., Sato H.,
RA   Ihara N., Itoh T., Kata S.R., Mishina Y., Womack J.E., Moritomo Y.,
RA   Sugimoto Y., Kunieda T.;
RT   "Positional cloning of the gene LIMBIN responsible for bovine
RT   chondrodysplastic dwarfism.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:10549-10554(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-744.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Plays a critical role in bone formation and skeletal
CC       development. May be involved in early embryonic morphogenesis.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- TISSUE SPECIFICITY: Expressed in long and cranial bones, kidney
CC       and heart. Strongly expressed in proliferating chondrocytes,
CC       osteoblasts and osteoclasts.
CC   -!- DEVELOPMENTAL STAGE: Found in the embryo at day E7, E11, E15, and
CC       E17. At the limb bud formation stage E11, it is expressed in fore-
CC       and hindlimb buds, branchial arches, and facial primordia.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC32167.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB083066; BAC06589.1; -; mRNA.
DR   EMBL; BC037473; AAH37473.1; -; mRNA.
DR   EMBL; BC064473; AAH64473.1; -; mRNA.
DR   EMBL; AK044977; BAC32167.1; ALT_INIT; mRNA.
DR   IPI; IPI00467271; -.
DR   RefSeq; NP_666032.1; NM_145920.3.
DR   UniGene; Mm.25506; -.
DR   ProteinModelPortal; Q8K1G2; -.
DR   STRING; Q8K1G2; -.
DR   PRIDE; Q8K1G2; -.
DR   Ensembl; ENSMUST00000056365; ENSMUSP00000055130; ENSMUSG00000050248.
DR   GeneID; 68525; -.
DR   KEGG; mmu:68525; -.
DR   UCSC; uc008xfs.1; mouse.
DR   CTD; 68525; -.
DR   MGI; MGI:1915775; Evc2.
DR   GeneTree; ENSGT00390000014437; -.
DR   HOGENOM; HBG279950; -.
DR   HOVERGEN; HBG045574; -.
DR   InParanoid; Q8K1G2; -.
DR   OMA; RLQNSAM; -.
DR   OrthoDB; EOG4M91QW; -.
DR   PhylomeDB; Q8K1G2; -.
DR   NextBio; 327386; -.
DR   ArrayExpress; Q8K1G2; -.
DR   Bgee; Q8K1G2; -.
DR   CleanEx; MM_EVC2; -.
DR   Genevestigator; Q8K1G2; -.
DR   GermOnline; ENSMUSG00000050248; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR022076; EVC2-like.
DR   Pfam; PF12297; EVC2_like; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Glycoprotein; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   1220       Limbin.
FT                                /FTId=PRO_0000084364.
FT   TRANSMEM    211    231       Helical; (Potential).
FT   COILED      355    404       Potential.
FT   COILED      563    644       Potential.
FT   COILED      854    875       Potential.
FT   COILED      920   1005       Potential.
FT   CARBOHYD    130    130       N-linked (GlcNAc...).
SQ   SEQUENCE   1220 AA;  137639 MW;  E67671714A866B1D CRC64;
     MGATGPTGAG GRATWVLAGN ILAAALVLGS GPRALPPSFP ALGPGSPSRP GPAGPWASSQ
     YSDISREARG PFENGVIFQK CSLVSGQSES QTMHVQLSVN NTRTPTSVNL SNLLVLDEIT
     GLAVKESPGN NTQDGIQTFR KSFLQVGECY SVSYTASLDP TALGTGESLD LPARLIFQSP
     SQNRTQLKAP FTITVEEKIM VLPNHGLHAA GFIAAFLISL LLTVAALFFL ARGRCLQGGM
     LSRCRIQHPE NKLEPSPFTS ANGVSQDLSL NDQVVAILTS EEPGSMLQAL EELEIATLNQ
     ADADLEACRN QISKDIIALL MKNLVSGGHL SPQTERKMAA AFKKQFLLLE NEIQEEYERK
     MLALTAECDL EMRKKTENQY QREMVAMEEA EEVLKRVSER SAAECSSLLR TLHGLEQEDM
     QRSLTLDQAE DFAQAHRQLA VFQRNELHSI VYTQIQSAVS KGELRPEVAK MMLQDYSKTQ
     ESVEELMDFF QATKRYHLSK RFGHREYLVQ RLQAMETRVQ GLLNTAATQL TSLIHKHERA
     GYLDEDQMET LLERAQTETF SIKQKLDNDL KQEKKRLHQR LITRRRRELL QKHKEQQKEQ
     VSLGEASSTA EDAVQYLHQW RSVMAEHTAA LEELQERLDQ AALDDLRVLT VSLSEKATEE
     LRRLQSTAMT QELLKRSAPW LFLQQILEEH SRESAARTTQ LEAEERERGQ ELVQGVRQRL
     QQDALEAYTE EQAELRHWEH LVFMKLCCAA ISLSEEDLLR VRQEAQGCFS QLDRSLALPR
     VRARVLQQQA QMAWREAEFR KLDQALAAPE LQSKARKLRS KGRGKADLLK KNLEDKIRLF
     EERAPVELAD QVRGELLQER VQRLEAQEAH FAESLVALQF QKVARAAETL SVYTALLSIQ
     DLLLGELSES ETLTKSACVQ ILESHRPELQ ELQELERKLE DQLVQQEEAE QQRVLESWQR
     WAADGPGLSE PEEMDPERQV SAILRQALNK GQKLLEQHQQ RVREEWQNGA VLEDSLESIE
     ADTMASLCSQ GLRLVSYLSR MTMVPGSTLL RLLSVVLPAA SQPQLLALLD AVSEKHSDHT
     AENESSGEQA QAEQSKRRKH QVWWKVLDSR FRADLVSQGL ERMLWARQKK ERILKKIYVP
     VQERVMFPGK GSWPHLSLEP IGELAPIPIT GADAMDILNT GEKIFVFRSP REPEISLRVP
     PRRKKNFLNA KKANRALGLD
//
ID   PP1RB_MOUSE             Reviewed;         131 AA.
AC   Q8K1L5; Q9DB02;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 11;
DE   AltName: Full=T-complex testis expressed protein 5;
DE            Short=Tctex-5;
GN   Name=Ppp1r11; Synonyms=Tctex5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=1718647; DOI=10.1002/dvg.1020120409;
RA   Ha H., Howard C.A., Yeom Y.I., Abe K., Uehara H., Artzt K.,
RA   Bennett D.;
RT   "Several testis-expressed genes in the mouse T-complex have expression
RT   differences between wild-type and t-mutant mice.";
RL   Dev. Genet. 12:318-332(1991).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-79; THR-80 AND
RP   SER-82, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Inhibitor of protein phosphatase 1 (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in testis with high level during
CC       spermatogenesis.
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DR   EMBL; AK005379; BAB23986.1; -; mRNA.
DR   EMBL; AK089107; BAC40754.1; -; mRNA.
DR   EMBL; AK170104; BAE41566.1; -; mRNA.
DR   EMBL; BC027737; AAH27737.1; -; mRNA.
DR   IPI; IPI00118923; -.
DR   RefSeq; NP_083908.1; NM_029632.3.
DR   UniGene; Mm.46176; -.
DR   STRING; Q8K1L5; -.
DR   PhosphoSite; Q8K1L5; -.
DR   PRIDE; Q8K1L5; -.
DR   Ensembl; ENSMUST00000040402; ENSMUSP00000047202; ENSMUSG00000036398.
DR   GeneID; 76497; -.
DR   KEGG; mmu:76497; -.
DR   UCSC; uc008cln.1; mouse.
DR   CTD; 76497; -.
DR   MGI; MGI:1923747; Ppp1r11.
DR   GeneTree; ENSGT00390000001153; -.
DR   HOGENOM; HBG125626; -.
DR   HOVERGEN; HBG080560; -.
DR   InParanoid; Q8K1L5; -.
DR   OrthoDB; EOG4VT5ZT; -.
DR   ArrayExpress; Q8K1L5; -.
DR   Bgee; Q8K1L5; -.
DR   Genevestigator; Q8K1L5; -.
DR   GermOnline; ENSMUSG00000036398; Mus musculus.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; IDA:UniProtKB.
DR   InterPro; IPR011107; PPI_Ypi1.
DR   PANTHER; PTHR20835; PPI_Ypi1; 1.
DR   Pfam; PF07491; PPI_Ypi1; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Protein phosphatase inhibitor.
FT   CHAIN         1    131       Protein phosphatase 1 regulatory subunit
FT                                11.
FT                                /FTId=PRO_0000239621.
FT   COMPBIAS    105    128       Pro-rich.
FT   MOD_RES      69     69       Phosphotyrosine (By similarity).
FT   MOD_RES      78     78       Phosphoserine.
FT   MOD_RES      79     79       Phosphoserine.
FT   MOD_RES      80     80       Phosphothreonine.
FT   MOD_RES      82     82       Phosphoserine.
FT   MOD_RES     114    114       Phosphothreonine (By similarity).
FT   CONFLICT     34     34       I -> T (in Ref. 1; BAB23986).
FT   CONFLICT    123    123       Q -> K (in Ref. 1; BAB23986).
SQ   SEQUENCE   131 AA;  14544 MW;  533FCEC7128FA14C CRC64;
     MAETGAGISE TVTETTVTET TVTETTEPEN QSLIMKLRKR KPEKKVEWSS DTVDNEHMGR
     RSSKCCCIYE KPRAFGESST ESDEDEEEGC SHKHCVRGHR KGRRPTTPAP TPTTPPQPPD
     PSQPPPGPMQ H
//
ID   CP074_MOUSE             Reviewed;          64 AA.
AC   Q8K1L6;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=Uncharacterized protein C16orf74 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; AK004494; BAE43181.1; -; mRNA.
DR   EMBL; BC027666; AAH27666.1; -; mRNA.
DR   IPI; IPI00169785; -.
DR   RefSeq; NP_932105.2; NM_197988.1.
DR   UniGene; Mm.473736; -.
DR   PhosphoSite; Q8K1L6; -.
DR   PRIDE; Q8K1L6; -.
DR   Ensembl; ENSMUST00000061208; ENSMUSP00000060254; ENSMUSG00000043687.
DR   GeneID; 68918; -.
DR   KEGG; mmu:68918; -.
DR   UCSC; uc009nre.1; mouse.
DR   MGI; MGI:1916168; 1190005I06Rik.
DR   eggNOG; maNOG21568; -.
DR   GeneTree; ENSGT00390000015933; -.
DR   HOGENOM; HBG505778; -.
DR   HOVERGEN; HBG081317; -.
DR   InParanoid; Q8K1L6; -.
DR   OMA; GSHDEAP; -.
DR   PhylomeDB; Q8K1L6; -.
DR   NextBio; 328179; -.
DR   ArrayExpress; Q8K1L6; -.
DR   Bgee; Q8K1L6; -.
DR   CleanEx; MM_1190005I06RIK; -.
DR   Genevestigator; Q8K1L6; -.
DR   GermOnline; ENSMUSG00000043687; Mus musculus.
PE   2: Evidence at transcript level;
KW   Phosphoprotein.
FT   CHAIN         1     64       Uncharacterized protein C16orf74 homolog.
FT                                /FTId=PRO_0000264622.
FT   MOD_RES      32     32       Phosphothreonine (By similarity).
FT   MOD_RES      34     34       Phosphothreonine (By similarity).
SQ   SEQUENCE   64 AA;  6996 MW;  45C6D7BA6338AE3E CRC64;
     MCVSSSNNNH DEAPVLNDKH LSVPNIIITP PTPTGMGLSR DSNKQVWMDE LGSYQDDGEL
     EPEA
//
ID   Q8K1M3_MOUSE            Unreviewed;       402 AA.
AC   Q8K1M3;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   SubName: Full=Protein kinase, cAMP dependent regulatory, type II alpha;
DE   SubName: Full=Protein kinase, cAMP dependent regulatory, type II alpha, isoform CRA_b;
DE   SubName: Full=Putative uncharacterized protein;
DE   SubName: Full=cAMP-dependent protein kinase type II-alpha regulatory chain;
GN   Name=Prkar2a; ORFNames=mCG_16488;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6; TISSUE=Testis;
RA   Mowen K.A., Collard M.W.;
RT   "Full length testicular cDNAs for mouse cAMP-dependent protein kinase
RT   type II regulatory subunit.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [11]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC075623; AAH75623.1; -; mRNA.
DR   EMBL; BC080276; AAH80276.1; -; mRNA.
DR   EMBL; AF533977; AAM97688.1; -; mRNA.
DR   EMBL; AK132728; BAE21323.1; -; mRNA.
DR   EMBL; CH466560; EDL21312.1; -; Genomic_DNA.
DR   IPI; IPI00169788; -.
DR   RefSeq; NP_032950.1; NM_008924.2.
DR   UniGene; Mm.253102; -.
DR   ProteinModelPortal; Q8K1M3; -.
DR   SMR; Q8K1M3; 1-45, 93-394.
DR   STRING; Q8K1M3; -.
DR   PRIDE; Q8K1M3; -.
DR   Ensembl; ENSMUST00000035220; ENSMUSP00000035220; ENSMUSG00000032601.
DR   GeneID; 19087; -.
DR   KEGG; mmu:19087; -.
DR   UCSC; uc009rqt.1; mouse.
DR   CTD; 19087; -.
DR   MGI; MGI:108025; Prkar2a.
DR   GeneTree; ENSGT00530000062947; -.
DR   HOGENOM; HBG736470; -.
DR   HOVERGEN; HBG002025; -.
DR   InParanoid; Q8K1M3; -.
DR   OMA; DQQRCRL; -.
DR   PhylomeDB; Q8K1M3; -.
DR   NextBio; 295632; -.
DR   ArrayExpress; Q8K1M3; -.
DR   Bgee; Q8K1M3; -.
DR   Genevestigator; Q8K1M3; -.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR002373; cAMP/cGMP_kin.
DR   InterPro; IPR012198; cAMP_dep_PK_reg_su.
DR   InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 2.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF02197; RIIa; 1.
DR   PIRSF; PIRSF000548; PK_regulatory; 1.
DR   PRINTS; PR00103; CAMPKINASE.
DR   SMART; SM00100; cNMP; 2.
DR   SMART; SM00394; RIIa; 1.
DR   SUPFAM; SSF47391; cAMP-dep_prot_kin_reg_I/II_a/b; 1.
DR   SUPFAM; SSF51206; cNMP_binding; 2.
DR   PROSITE; PS00888; CNMP_BINDING_1; 2.
DR   PROSITE; PS00889; CNMP_BINDING_2; 2.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
PE   2: Evidence at transcript level;
KW   Kinase; Transferase.
SQ   SEQUENCE   402 AA;  45589 MW;  505FDD8B35F1BA00 CRC64;
     MSHIQIPAGL TELLQGYTVE VLRQQPPDLV DFAVEYFTRL REARRQESDT FIVSPTTFHT
     QESSAVPVIE EDGESDSDSE DADLEVPVPS KFTRRVSVCA ETFNPDEEEE DNDPRVVHPK
     TDEQRCRLQE ACKDILLFKN LDQEQLSQVL DAMFEKIVKT DEHVIDQGDD GDNFYVIERG
     TYDILVTKDN QTRSVGQYDN RGSFGELALM YNTPRAATII ATSEGSLWGL DRVTFRRIIV
     KNNAKKRKMF ESFIESVPLF KSLEMSERMK IVDVIGEKIY KDGERIIAQG EKADSFYIIE
     SGEVSILIRS KTKSNKNGGN QEVEIAHCHK GQYFGELALV TNKPRAASAY AVGDVKCLVM
     DVQAFERLLG PCMDIMKRNI SHYEEQLVKM FGSNLDLMDP GQ
//
ID   DNM1L_MOUSE             Reviewed;         742 AA.
AC   Q8K1M6; Q8BNQ5; Q8BQ64; Q8CGD0; Q8K1A1;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 2.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Dynamin-1-like protein;
DE            EC=3.6.5.5;
DE   AltName: Full=Dynamin family member proline-rich carboxyl-terminal domain less;
DE            Short=Dymple;
DE   AltName: Full=Dynamin-related protein 1;
GN   Name=Dnm1l; Synonyms=Drp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Osteoclast;
RX   PubMed=14592431; DOI=10.1016/j.bbrc.2003.10.008;
RA   Honda S., Hirose S.;
RT   "Stage-specific enhanced expression of mitochondrial fusion and
RT   fission factors during spermatogenesis in rat testis.";
RL   Biochem. Biophys. Res. Commun. 311:424-432(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC   STRAIN=C57BL/6; TISSUE=Brain, Mammary gland, and Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 448-659 (ISOFORM 1).
RX   PubMed=11544199; DOI=10.1101/gr.185501;
RA   Piao Y., Ko N.T., Lim M.K., Ko M.S.H.;
RT   "Construction of long-transcript enriched cDNA libraries from
RT   submicrogram amounts of total RNAs by a universal PCR amplification
RT   method.";
RL   Genome Res. 11:1553-1558(2001).
RN   [5]
RP   PROTEIN SEQUENCE OF 626-640 AND 725-737, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [6]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=98086281; PubMed=9422767; DOI=10.1074/jbc.273.2.1044;
RA   Kamimoto T., Nagai Y., Onogi H., Muro Y., Wakabayashi T., Hagiwara M.;
RT   "Dymple, a novel dynamin-like high molecular weight GTPase lacking a
RT   proline-rich carboxyl-terminal domain in mammalian cells.";
RL   J. Biol. Chem. 273:1044-1051(1998).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=19578372; DOI=10.1038/ncb1907;
RA   Ishihara N., Nomura M., Jofuku A., Kato H., Suzuki S.O., Masuda K.,
RA   Otera H., Nakanishi Y., Nonaka I., Goto Y., Taguchi N., Morinaga H.,
RA   Maeda M., Takayanagi R., Yokota S., Mihara K.;
RT   "Mitochondrial fission factor Drp1 is essential for embryonic
RT   development and synapse formation in mice.";
RL   Nat. Cell Biol. 11:958-966(2009).
CC   -!- FUNCTION: Functions in mitochondrial and peroxisomal division.
CC       Mediates membrane fission through oligomerization into ring-like
CC       structures which wrap around the scission site to constict and
CC       sever the mitochondrial membrane through a GTP hydrolysis-
CC       dependent mechanism. Required for normal brain development.
CC       Facilitates developmentally-regulated apoptosis during neural tube
CC       development. Required for a normal rate of cytochrome c release
CC       and caspase activation during apoptosis. Also required for
CC       mitochondrial fission during mitosis. May be involved in vesicle
CC       transport (By similarity).
CC   -!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate.
CC   -!- SUBUNIT: Homotetramer; dimerizes through the N-terminal GTP-middle
CC       region of one molecule binding to the GED domain of another DNM1L
CC       molecule (By similarity). Can self-assemble in multimeric ring-
CC       like structures. Interacts with BCL2L1; the interaction stimulates
CC       the GTPase activity of DMN1L in synapses and increases the number
CC       of axonal mitochondria and the size and number of synaptic vesicle
CC       clusters. Interacts with FIS1. Interacts with GSK3B and MARCH5.
CC       Interacts (via the GTPase and B domains) with UBE2I; the
CC       interaction promotes sumoylation of DNM1L, mainly in ite B domain.
CC       Interacts with PPP3CA; the interaction dephosphorylates DNM1L and
CC       regulates its transition to mitochondria (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity). Golgi
CC       apparatus (By similarity). Endomembrane system; Peripheral
CC       membrane protein. Note=Mainly cytosolic. Translocated to the
CC       mitochondrial membrane through interaction with FIS1. Colocalized
CC       with MARCH5 at mitochondrial membrane. Localizes to mitochondria
CC       at sites of division. Associated with peroxisomal membranes,
CC       partly recruited there by PEX11B. May also be associated with
CC       endoplasmic reticulum tubules and cytoplasmic vesicles and found
CC       to be perinuclear. In some cell types, localizes to the Golgi
CC       complex (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q8K1M6-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q8K1M6-2; Sequence=VSP_013695;
CC       Name=3;
CC         IsoId=Q8K1M6-3; Sequence=VSP_013690, VSP_013694;
CC       Name=4;
CC         IsoId=Q8K1M6-4; Sequence=VSP_013689, VSP_013691, VSP_013695;
CC       Name=5;
CC         IsoId=Q8K1M6-5; Sequence=VSP_013690, VSP_013692, VSP_013693;
CC   -!- TISSUE SPECIFICITY: Expressed in the cerebellum and in several
CC       regions of the cerebrum and diencephalon. Strongly expressed in
CC       the cerebellar Purkinje cells and in the pontile giant neurons.
CC   -!- DOMAIN: The GED domain folds back to interact, in cis, with the
CC       GTP-binding domain and middle domain, and interacts, in trans,
CC       with the GED domains of other DNM1L molecules, and is thus
CC       critical for activating GTPase activity and for DNM1L dimerization
CC       (By similarity).
CC   -!- PTM: Phosphorylation/dephosphorylation events on two sites near
CC       the GED domain regulate mitochondrial fission. Phosphorylation on
CC       Ser-643 inhibits mitochondrial fissin probably through preventing
CC       intramolecular interaction. Dephosphorylated on this site by
CC       PPP3CA which promotes mitochondrial fission. Phosphorylation on
CC       Ser-622 also promotes mitochondrial fission (By similarity).
CC   -!- PTM: Sumoylated on various lysine residues within the B domain.
CC       Desumoylated by SENP5 during G2/M transition of mitosis. Appears
CC       to be linked to its catalytic activity (By similarity).
CC   -!- PTM: S-nitrosylation increases DNM1L dimerization, mitochondrial
CC       fission and causes neuronal damage (By similarity).
CC   -!- DISRUPTION PHENOTYPE: In embryonic fibroblasts, mice show defects
CC       in trophoblast giant cells and cardiomyocytes. Extensive
CC       mitochondrial networks are formed, and peroxisomes elongated. In
CC       brain, there are developmental defects in which Purkinje cells
CC       contained few giant mitochondria. In the forebrain, there is a
CC       decreased number of neurites and defective synapse formation.
CC       Embryos undergo developmentally-regulated apoptosis during neural
CC       tube formation. Mice die by around embryonic day 12.
CC   -!- SIMILARITY: Belongs to the dynamin family.
CC   -!- SIMILARITY: Contains 1 GED domain.
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DR   EMBL; AB079133; BAC06576.1; -; mRNA.
DR   EMBL; AK051443; BAC34640.1; -; mRNA.
DR   EMBL; AK080871; BAC38054.1; -; mRNA.
DR   EMBL; BC027538; AAH27538.1; -; mRNA.
DR   EMBL; BC040777; AAH40777.1; -; mRNA.
DR   EMBL; BC079635; AAH79635.1; -; mRNA.
DR   EMBL; CF914619; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00172221; -.
DR   IPI; IPI00471349; -.
DR   IPI; IPI00556723; -.
DR   IPI; IPI00556781; -.
DR   IPI; IPI00556857; -.
DR   RefSeq; NP_001021118.1; NM_001025947.1.
DR   RefSeq; NP_690029.2; NM_152816.2.
DR   UniGene; Mm.218820; -.
DR   ProteinModelPortal; Q8K1M6; -.
DR   SMR; Q8K1M6; 1-354.
DR   IntAct; Q8K1M6; 1.
DR   STRING; Q8K1M6; -.
DR   PhosphoSite; Q8K1M6; -.
DR   PRIDE; Q8K1M6; -.
DR   Ensembl; ENSMUST00000023477; ENSMUSP00000023477; ENSMUSG00000022789.
DR   Ensembl; ENSMUST00000047122; ENSMUSP00000093944; ENSMUSG00000022789.
DR   Ensembl; ENSMUST00000115749; ENSMUSP00000111415; ENSMUSG00000022789.
DR   GeneID; 74006; -.
DR   KEGG; mmu:74006; -.
DR   UCSC; uc007yik.1; mouse.
DR   UCSC; uc007yil.1; mouse.
DR   UCSC; uc007yin.1; mouse.
DR   UCSC; uc007yio.1; mouse.
DR   CTD; 74006; -.
DR   MGI; MGI:1921256; Dnm1l.
DR   GeneTree; ENSGT00600000084466; -.
DR   HOGENOM; HBG434086; -.
DR   HOVERGEN; HBG107833; -.
DR   InParanoid; Q8K1M6; -.
DR   OMA; DPATWKN; -.
DR   OrthoDB; EOG4SN1N7; -.
DR   PhylomeDB; Q8K1M6; -.
DR   BRENDA; 3.6.5.5; 244.
DR   NextBio; 339508; -.
DR   ArrayExpress; Q8K1M6; -.
DR   Bgee; Q8K1M6; -.
DR   CleanEx; MM_DNM1L; -.
DR   Genevestigator; Q8K1M6; -.
DR   GermOnline; ENSMUSG00000022789; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   InterPro; IPR022812; Dynamin.
DR   InterPro; IPR000375; Dynamin_central.
DR   InterPro; IPR001401; Dynamin_GTPase.
DR   InterPro; IPR019762; Dynamin_GTPase_CS.
DR   InterPro; IPR003130; GED.
DR   InterPro; IPR020850; GTPase_effector_domain_GED.
DR   Pfam; PF01031; Dynamin_M; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   Pfam; PF02212; GED; 1.
DR   PRINTS; PR00195; DYNAMIN.
DR   SMART; SM00053; DYNc; 1.
DR   SMART; SM00302; GED; 1.
DR   PROSITE; PS00410; DYNAMIN; 1.
DR   PROSITE; PS51388; GED; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm;
KW   Direct protein sequencing; Golgi apparatus; GTP-binding; Hydrolase;
KW   Isopeptide bond; Membrane; Nucleotide-binding; Phosphoprotein;
KW   S-nitrosylation; Ubl conjugation.
FT   CHAIN         1    742       Dynamin-1-like protein.
FT                                /FTId=PRO_0000206567.
FT   DOMAIN      650    741       GED.
FT   NP_BIND      32     39       GTP (By similarity).
FT   NP_BIND     152    156       GTP (By similarity).
FT   NP_BIND     221    224       GTP (By similarity).
FT   REGION        1    349       GTPase domain (By similarity).
FT   REGION        1    349       N-terminal dimerization domain (By
FT                                similarity).
FT   REGION      350    495       Middle domain (By similarity).
FT   REGION      454    691       Interaction with GSK3B (By similarity).
FT   REGION      454    654       Interaction with GSK3B (By similarity).
FT   REGION      508    575       B domain (By similarity).
FT   REGION      548    742       C-terminal dimerization domain (By
FT                                similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     289    289       N6-acetyllysine (By similarity).
FT   MOD_RES     535    535       Phosphoserine.
FT   MOD_RES     622    622       Phosphoserine; by CDK1 (By similarity).
FT   MOD_RES     643    643       Phosphoserine; by CAMK1 and PKA (By
FT                                similarity).
FT   MOD_RES     650    650       S-nitrosocysteine (By similarity).
FT   CROSSLNK    538    538       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    541    541       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    564    564       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    574    574       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    600    600       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    603    603       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    612    612       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    614    614       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   VAR_SEQ       1    104       Missing (in isoform 4).
FT                                /FTId=VSP_013689.
FT   VAR_SEQ      85     90       Missing (in isoform 3 and isoform 5).
FT                                /FTId=VSP_013690.
FT   VAR_SEQ     105    105       K -> M (in isoform 4).
FT                                /FTId=VSP_013691.
FT   VAR_SEQ     214    227       RRTLAVITKLDLMD -> KGRCLYLMDVDLQW (in
FT                                isoform 5).
FT                                /FTId=VSP_013692.
FT   VAR_SEQ     228    742       Missing (in isoform 5).
FT                                /FTId=VSP_013693.
FT   VAR_SEQ     539    575       Missing (in isoform 3).
FT                                /FTId=VSP_013694.
FT   VAR_SEQ     539    564       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_013695.
FT   CONFLICT    165    165       P -> L (in Ref. 1; BAC06576).
FT   CONFLICT    320    320       Q -> R (in Ref. 1; BAC06576).
FT   CONFLICT    519    519       E -> A (in Ref. 2; BAC34640).
SQ   SEQUENCE   742 AA;  82658 MW;  5A8679B61A444847 CRC64;
     MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL LPRGTGVVTR
     RPLILQLVHV SPEDKRKTTG EENGKFQSWR VEAEEWGKFL HTKNKLYTDF DEIRQEIENE
     TERISGNNKG VSPEPIHLKV FSPNVVNLTL VDLPGMTKVP VGDQPKDIEL QIRELILRFI
     SNPNSIILAV TAANTDMATS EALKISREVD PDGRRTLAVI TKLDLMDAGT DAMDVLMGRV
     IPVKLGIIGV VNRSQLDINN KKSVTDSIRD EYAFLQKKYP SLANRNGTKY LARTLNRLLM
     HHIRDCLPEL KTRINVLAAQ YQSLLNSYGE PVDDKSATLL QLITKFATEY CNTIEGTAKY
     IETSELCGGA RICYIFHETF GRTLESVDPL GGLNTIDILT AIRNATGPRP ALFVPEVSFE
     LLVKRQIKRL EEPSLRCVEL VHEEMQRIIQ HCSNYSTQEL LRFPKLHDAI VEVVTCLLRK
     RLPVTNEMVH NLVAIELAYI NTKHPDFADA CGLMNNNIEE QRRNRLAREL PSAGSRDKSS
     KVPSALAPAS QEPPPAASAE ADGKLIQDNR RETKNVPSAG GGIGDGGQEP TTGNWRGMLK
     TSKAEELLAE EKSKPIPIMP ASPQKGHAVN LLDVPVPVAR KLSAREQRDC EVIERLIKSY
     FLIVRKNIQD SVPKAVMHFL VNHVKDTLQS ELVGQLYKSS LLDDLLTESE DMAQRRKEAA
     DMLKALQGAS QIIAEIRETH LW
//
ID   PLPL8_MOUSE             Reviewed;         776 AA.
AC   Q8K1N1; Q3TH33; Q8VEC0; Q9DC20;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Calcium-independent phospholipase A2-gamma;
DE            EC=3.1.1.5;
DE   AltName: Full=Intracellular membrane-associated calcium-independent phospholipase A2 gamma;
DE            Short=iPLA2-gamma;
DE   AltName: Full=Patatin-like phospholipase domain-containing protein 8;
GN   Name=Pnpla8; Synonyms=Ipla22, Ipla2g;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20294840; PubMed=10833412; DOI=10.1006/bbrc.2000.2776;
RA   Tanaka H., Takeya R., Sumimoto H.;
RT   "A novel intracellular membrane-bound calcium-independent
RT   phospholipase A(2).";
RL   Biochem. Biophys. Res. Commun. 272:320-326(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Egg, Kidney, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Calcium-independent phospholipase A2, which catalyzes
CC       the hydrolysis of the sn-2 position of glycerophospholipids,
CC       PtdSer and to a lower extent PtdCho. Cleaves membrane
CC       phospholipids (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2-lysophosphatidylcholine + H(2)O =
CC       glycerophosphocholine + a carboxylate.
CC   -!- ENZYME REGULATION: Inhibited by E-6-bromomethylene-3-1-
CC       naphthalenyl-2H-tetrahydropyran-2-one (BEL) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       membrane protein (By similarity). Golgi apparatus membrane;
CC       Single-pass membrane protein (By similarity). Cytoplasm,
CC       perinuclear region (By similarity).
CC   -!- SIMILARITY: Contains 1 patatin domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH19364.1; Type=Erroneous initiation;
CC       Sequence=BAB23417.1; Type=Erroneous termination; Positions=777; Note=Translated as stop;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB044139; BAB97200.1; -; mRNA.
DR   EMBL; AK004621; BAB23417.1; ALT_SEQ; mRNA.
DR   EMBL; AK145776; BAE26645.1; -; mRNA.
DR   EMBL; AK163211; BAE37236.1; -; mRNA.
DR   EMBL; AK168475; BAE40365.1; -; mRNA.
DR   EMBL; BC019364; AAH19364.1; ALT_INIT; mRNA.
DR   EMBL; BC127056; AAI27057.1; -; mRNA.
DR   IPI; IPI00120080; -.
DR   RefSeq; NP_080440.2; NM_026164.2.
DR   UniGene; Mm.54126; -.
DR   ProteinModelPortal; Q8K1N1; -.
DR   PhosphoSite; Q8K1N1; -.
DR   PRIDE; Q8K1N1; -.
DR   Ensembl; ENSMUST00000043082; ENSMUSP00000043286; ENSMUSG00000036257.
DR   GeneID; 67452; -.
DR   KEGG; mmu:67452; -.
DR   UCSC; uc007nlq.1; mouse.
DR   CTD; 67452; -.
DR   MGI; MGI:1914702; Pnpla8.
DR   HOGENOM; HBG716186; -.
DR   HOVERGEN; HBG102100; -.
DR   InParanoid; Q8K1N1; -.
DR   OMA; QLEGLKY; -.
DR   BRENDA; 3.1.1.5; 244.
DR   NextBio; 324606; -.
DR   ArrayExpress; Q8K1N1; -.
DR   Bgee; Q8K1N1; -.
DR   CleanEx; MM_PNPLA8; -.
DR   Genevestigator; Q8K1N1; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005778; C:peroxisomal membrane; ISS:UniProtKB.
DR   GO; GO:0047499; F:calcium-independent phospholipase A2 activity; ISS:UniProtKB.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:EC.
DR   GO; GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPlipase.
DR   InterPro; IPR002641; Patatin/PhospholipaseA2-rel.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; Acyl_Trfase/lysoPlipase; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW   Hydrolase; Lipid degradation; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    776       Calcium-independent phospholipase A2-
FT                                gamma.
FT                                /FTId=PRO_0000303215.
FT   TRANSMEM    469    489       Helical; (Potential).
FT   DOMAIN      439    634       Patatin.
FT   MOTIF       475    479       GXSXG (By similarity).
FT   CARBOHYD      4      4       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    157    157       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    438    441       ILTI -> DAWV (in Ref. 3; AAH19364).
FT   CONFLICT    729    729       M -> I (in Ref. 2; BAE40365).
FT   CONFLICT    749    749       E -> Q (in Ref. 2; BAE40365).
SQ   SEQUENCE   776 AA;  87381 MW;  1140CC8358B1E119 CRC64;
     MSINLTLDIY IYFLNNARSL CGKQRSKQLH FVCSKQYWRM NHVNVHREFH TSKKSCKWNR
     SEAHCSKHWH SPSNHGLHFG IVRLSTSAPK GLTKVSIHMS RIKSTLNSVS KAIFGSQNEM
     VTRLAQFKPS SRILRKVSDK GWLKQKNVKQ AVESLKNYSD KSAGKNSLAE QKSYFADKEE
     DSGKHSLFHY TYGITTRFGE SFSVLANHIN SYFKSKGKMS QTKEDKQLQD KPDLEERKSS
     SPGPDTVADR PDSESPLEVK DKLSSPTQMP EAHPVSAKQS IANFLSRPTE GVQALVGGYI
     GGLVPKLKSD PKSPPEEQEV SAKTEQAVNK DKKAEEKKRV LLQQEKIIAR VSIDNRTRAL
     VQALRRTADP KLCITRVEEL TFHLLEFPEG KGVAIKEKII PYLLRLRQVK DETLQAAVRE
     ILALIGYVDP VKGRGIRILT IDGGGTRGVV ALQTLRKLVE LTQKPIHQLF DYICGVSTGA
     ILAFMLGLFH MPLDECEELY RKLGSDVFTQ NVIVGTVKMS WSHAFYDSNT WEKILKDRIG
     SALMIETARN PACPKVAAIS TIVNRGQTPK AFVFRNYGHF PGTNSHYLGG CQYKMWQAIR
     ASSAAPGYFA EYALGSDLHQ DGGLLLNNPS ALALHECKCI WPDTPLECIV SLGTGRYESD
     VRNTSTYTSL KTKLSNVISS ATDTEEVHIM LDGLLPSDTY FRFNPVICEN IPLDESRDEK
     LDQLQLEGMK YIERNDQKMK KVAKILSQEK TTLQKINDWI KLKSDMYEGL PFFSKL
//
ID   UNC5D_MOUSE             Reviewed;         956 AA.
AC   Q8K1S2; B9EHC0;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Netrin receptor UNC5D;
DE   AltName: Full=Protein unc-5 homolog 4;
DE   AltName: Full=Protein unc-5 homolog D;
DE   Flags: Precursor;
GN   Name=Unc5d; Synonyms=Unc5h4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=22239710; PubMed=12351186; DOI=10.1016/S0925-4773(02)00248-4;
RA   Engelkamp D.;
RT   "Cloning of three mouse Unc5 genes and their expression patterns at
RT   mid-gestation.";
RL   Mech. Dev. 118:191-197(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Receptor for netrin involved in cell migration. May be
CC       involved in axon guidance by mediating axon repulsion of neuronal
CC       growth cones in the developing nervous system upon ligand binding.
CC       Axon repulsion in growth cones may be caused by its association
CC       with DCC that may trigger signaling for repulsion. It also acts as
CC       a dependence receptor required for apoptosis induction when not
CC       associated with netrin ligand (By similarity).
CC   -!- SUBUNIT: Interacts with the cytoplasmic part of DCC (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in developing limb and mammary
CC       gland.
CC   -!- PTM: Phosphorylated on cytoplasmic tyrosine residues (By
CC       similarity).
CC   -!- PTM: Proteolytically cleaved by caspases during apoptosis. The
CC       cleavage does not take place when the receptor is associated with
CC       netrin ligand. Its cleavage by caspases is required to induce
CC       apoptosis (By similarity).
CC   -!- SIMILARITY: Belongs to the unc-5 family.
CC   -!- SIMILARITY: Contains 1 death domain.
CC   -!- SIMILARITY: Contains 1 Ig-like (immunoglobulin-like) domain.
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 2 TSP type-1 domains.
CC   -!- SIMILARITY: Contains 1 ZU5 domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ487854; CAD32252.1; -; mRNA.
DR   EMBL; BC137615; AAI37616.1; -; mRNA.
DR   IPI; IPI00470031; -.
DR   RefSeq; NP_694775.1; NM_153135.3.
DR   UniGene; Mm.248433; -.
DR   ProteinModelPortal; Q8K1S2; -.
DR   SMR; Q8K1S2; 52-359, 543-942.
DR   STRING; Q8K1S2; -.
DR   PhosphoSite; Q8K1S2; -.
DR   PRIDE; Q8K1S2; -.
DR   Ensembl; ENSMUST00000078597; ENSMUSP00000077670; ENSMUSG00000063626.
DR   GeneID; 210801; -.
DR   KEGG; mmu:210801; -.
DR   UCSC; uc009liz.1; mouse.
DR   CTD; 210801; -.
DR   MGI; MGI:2389364; Unc5d.
DR   GeneTree; ENSGT00600000084104; -.
DR   HOGENOM; HBG358171; -.
DR   HOVERGEN; HBG056483; -.
DR   InParanoid; Q8K1S2; -.
DR   OMA; TLPHFIE; -.
DR   OrthoDB; EOG4NCMC0; -.
DR   NextBio; 373061; -.
DR   ArrayExpress; Q8K1S2; -.
DR   Bgee; Q8K1S2; -.
DR   CleanEx; MM_UNC5D; -.
DR   Genevestigator; Q8K1S2; -.
DR   GO; GO:0009986; C:cell surface; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   InterPro; IPR000488; Death.
DR   InterPro; IPR011029; DEATH-like.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR000884; Thrombospondin_1_rpt.
DR   InterPro; IPR000906; ZU5.
DR   Gene3D; G3DSA:1.10.533.10; DEATH_like; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00090; TSP_1; 2.
DR   Pfam; PF00791; ZU5; 1.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00209; TSP1; 2.
DR   SUPFAM; SSF47986; DEATH_like; 1.
DR   SUPFAM; SSF82895; TSP1; 2.
DR   PROSITE; PS50017; DEATH_DOMAIN; FALSE_NEG.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS50092; TSP1; 2.
DR   PROSITE; PS51145; ZU5; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Developmental protein; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Phosphoprotein; Receptor; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     30       Potential.
FT   CHAIN        31    956       Netrin receptor UNC5D.
FT                                /FTId=PRO_0000036080.
FT   TOPO_DOM     31    382       Extracellular (Potential).
FT   TRANSMEM    383    403       Helical; (Potential).
FT   TOPO_DOM    404    956       Cytoplasmic (Potential).
FT   DOMAIN       52    149       Ig-like.
FT   DOMAIN      151    242       Ig-like C2-type.
FT   DOMAIN      250    304       TSP type-1 1.
FT   DOMAIN      306    358       TSP type-1 2.
FT   DOMAIN      543    648       ZU5.
FT   DOMAIN      862    939       Death.
FT   REGION      706    724       Interaction with DCC (By similarity).
FT   SITE        419    420       Cleavage; by caspase-3 (By similarity).
FT   MOD_RES     208    208       Phosphothreonine (By similarity).
FT   CARBOHYD    115    115       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    226    226       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    351    351       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    379    379       N-linked (GlcNAc...) (Potential).
FT   DISULFID     73    132       By similarity.
FT   DISULFID    178    229       By similarity.
FT   DISULFID    262    299       By similarity.
FT   DISULFID    266    303       By similarity.
FT   DISULFID    277    289       By similarity.
SQ   SEQUENCE   956 AA;  106352 MW;  DFDF07839C10C68D CRC64;
     MGTGAADGSR GARRWLPWLG LFFWAAGAAA ARGADGSEIL PDSIPSAPGT LPHFIEEPED
     AYIIKSNPIA LRCKARPAMQ IFFKCNGEWV HQNEHVSEES LDESSGLKVR EVFINVTRQQ
     VEDFHGPEDY WCQCVAWSHL GTSKSRKASV RIAYLRKNFE QDPQGREVPI EGMIVLHCRP
     PEGVPAAEVE WLKNEEPIDS EQDENIDTRA DHNLIIRQAR LSDSGNYTCM AANIVAKRRS
     LSATVVVYVN GGWSSWTEWS ACNVRCGRGW QKRSRTCTNP APLNGGAFCE GMSVQKITCT
     ALCPVDGSWE VWSEWSVCSP ECEHLRIREC TAPPPRNGGK FCEGLSQESE NCTDGLCILD
     KKPLHEIKPQ RWSRRGIENA SDIALYSGLG AAVVAVAVLV IGVTLYRRSH SDYGVDVIDS
     SALTGGFQTF NFKTVRQGNS LLLNPAMQPD LTVSRTYSGP ICLQDPLDKE LMTESSLFNP
     LSDIKVKVQS SFMVSLGVSE RAEYHGKNHS GTFPHGNNRG FSTIHPRNKT PYIQNLSSLP
     TRTELRTTGV FGHLGGRLVM PNTGVSLLIP HGAIPEENSW EIYMSINQGE PSLQSDGSEV
     LLSPEVTCGP PDMLVTTPFA LTIPHCADVS SEHWNIHLKK RTQQGKWEEV MSVEDESTSC
     YCLLDPFACH VLLDSFGTYA LTGEPITDCA VKQLKVAVFG CMSCNSLDYN LRVYCVDNTP
     CAFQEVISDE RHQGGQLLEE PKLLHFKGNT FSLQVSVLDI PPFLWRIKPF TACQEVPFSR
     VWSSNRQPLH CAFSLERYTP TTTQLSCKIC IRQLKGHEQI LQVQTSILES ERETITFFAQ
     EDSTFPAQTG PKAFKIPYSI RQRICATFDT PNAKGKDWQM LAQKNSINRN LSYFATQSSP
     SAVILNLWEA RHQQDGDLDS LACALEEIGR THTKLSNITE PQIDDADFNY SRQNGL
//
ID   UNC5A_MOUSE             Reviewed;         898 AA.
AC   Q8K1S4; Q6PEF7; Q80T71;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Netrin receptor UNC5A;
DE   AltName: Full=Protein unc-5 homolog 1;
DE   AltName: Full=Protein unc-5 homolog A;
DE   Flags: Precursor;
GN   Name=Unc5a; Synonyms=Kiaa1976, Unc5h1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   MEDLINE=22239710; PubMed=12351186; DOI=10.1016/S0925-4773(02)00248-4;
RA   Engelkamp D.;
RT   "Cloning of three mouse Unc5 genes and their expression patterns at
RT   mid-gestation.";
RL   Mech. Dev. 118:191-197(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Receptor for netrin required for axon guidance. Mediates
CC       axon repulsion of neuronal growth cones in the developing nervous
CC       system upon ligand binding. Axon repulsion in growth cones may be
CC       caused by its association with DCC that may trigger signaling for
CC       repulsion. It also acts as a dependence receptor required for
CC       apoptosis induction when not associated with netrin ligand (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with the cytoplasmic part of DCC. Interacts
CC       with MAGED1. Interacts with PRKCABP, possibly mediating some
CC       interaction with PKC (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein (By similarity). Note=The interaction with PRKCABP
CC       regulates its surface expression and leads to its removal from
CC       surface of neurons and growth cones (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8K1S4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K1S4-2; Sequence=VSP_011697;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8K1S4-3; Sequence=VSP_011696;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Restricted to central nervous system.
CC   -!- DOMAIN: The ZU5 domain mediates the interaction with MAGED1, which
CC       participates in the induction of apoptosis (By similarity).
CC   -!- PTM: Phosphorylated by PKC in vitro. Phosphorylated on cytoplasmic
CC       tyrosine residues (By similarity).
CC   -!- PTM: Proteolytically cleaved by caspases during apoptosis. The
CC       cleavage does not take place when the receptor is associated with
CC       netrin ligand. Its cleavage by caspases is required to induce
CC       apoptosis (By similarity).
CC   -!- SIMILARITY: Belongs to the unc-5 family.
CC   -!- SIMILARITY: Contains 1 death domain.
CC   -!- SIMILARITY: Contains 1 Ig-like (immunoglobulin-like) domain.
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 2 TSP type-1 domains.
CC   -!- SIMILARITY: Contains 1 ZU5 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65857.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ487852; CAD32250.1; -; mRNA.
DR   EMBL; AK122575; BAC65857.1; ALT_INIT; mRNA.
DR   EMBL; BC058084; AAH58084.1; -; mRNA.
DR   IPI; IPI00169811; -.
DR   IPI; IPI00403172; -.
DR   IPI; IPI00471426; -.
DR   RefSeq; NP_694771.1; NM_153131.3.
DR   UniGene; Mm.23573; -.
DR   ProteinModelPortal; Q8K1S4; -.
DR   SMR; Q8K1S4; 42-240, 242-349, 495-895.
DR   STRING; Q8K1S4; -.
DR   PRIDE; Q8K1S4; -.
DR   Ensembl; ENSMUST00000026994; ENSMUSP00000026994; ENSMUSG00000025876.
DR   Ensembl; ENSMUST00000109994; ENSMUSP00000105621; ENSMUSG00000025876.
DR   GeneID; 107448; -.
DR   KEGG; mmu:107448; -.
DR   UCSC; uc007qpp.1; mouse.
DR   UCSC; uc007qpq.1; mouse.
DR   CTD; 107448; -.
DR   MGI; MGI:894682; Unc5a.
DR   eggNOG; maNOG12483; -.
DR   GeneTree; ENSGT00600000084104; -.
DR   HOGENOM; HBG358171; -.
DR   HOVERGEN; HBG056483; -.
DR   InParanoid; Q8K1S4; -.
DR   OMA; LHHSSPT; -.
DR   OrthoDB; EOG4SJ5D5; -.
DR   PhylomeDB; Q8K1S4; -.
DR   NextBio; 358818; -.
DR   ArrayExpress; Q8K1S4; -.
DR   Bgee; Q8K1S4; -.
DR   CleanEx; MM_UNC5A; -.
DR   Genevestigator; Q8K1S4; -.
DR   GermOnline; ENSMUSG00000025876; Mus musculus.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   InterPro; IPR000488; Death.
DR   InterPro; IPR011029; DEATH-like.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR000884; Thrombospondin_1_rpt.
DR   InterPro; IPR000906; ZU5.
DR   Gene3D; G3DSA:1.10.533.10; DEATH_like; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00090; TSP_1; 2.
DR   Pfam; PF00791; ZU5; 1.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00209; TSP1; 2.
DR   SMART; SM00218; ZU5; 1.
DR   SUPFAM; SSF47986; DEATH_like; 1.
DR   SUPFAM; SSF82895; TSP1; 2.
DR   PROSITE; PS50017; DEATH_DOMAIN; FALSE_NEG.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS50092; TSP1; 2.
DR   PROSITE; PS51145; ZU5; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Apoptosis; Cell membrane; Developmental protein;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane;
KW   Phosphoprotein; Receptor; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     25       Potential.
FT   CHAIN        26    898       Netrin receptor UNC5A.
FT                                /FTId=PRO_0000036069.
FT   TOPO_DOM     26    361       Extracellular (Potential).
FT   TRANSMEM    362    382       Helical; (Potential).
FT   TOPO_DOM    383    898       Cytoplasmic (Potential).
FT   DOMAIN       44    141       Ig-like.
FT   DOMAIN      155    234       Ig-like C2-type.
FT   DOMAIN      242    296       TSP type-1 1.
FT   DOMAIN      298    350       TSP type-1 2.
FT   DOMAIN      495    601       ZU5.
FT   DOMAIN      817    897       Death.
FT   REGION      661    679       Interaction with DCC (By similarity).
FT   SITE        396    397       Cleavage; by caspase-3 (By similarity).
FT   CARBOHYD    107    107       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    218    218       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    343    343       N-linked (GlcNAc...) (Potential).
FT   DISULFID     65    124       By similarity.
FT   DISULFID    170    221       By similarity.
FT   DISULFID    254    291       By similarity.
FT   DISULFID    258    295       By similarity.
FT   DISULFID    269    281       By similarity.
FT   VAR_SEQ       1    790       Missing (in isoform 3).
FT                                /FTId=VSP_011696.
FT   VAR_SEQ     241    296       Missing (in isoform 2).
FT                                /FTId=VSP_011697.
FT   CONFLICT    217    217       A -> P (in Ref. 3; AAH58084).
SQ   SEQUENCE   898 AA;  98857 MW;  59F04BA2E196C1DB CRC64;
     MAVRPGLWPA LLGIVLTAWL RGSGAQQSAT VANPVPGANP DLLPHFLVEP EDVYIVKNKP
     VLLVCKAVPA TQIFFKCNGE WVRQVDHVIE RSTDGSSGLP TMEVRINVSR QQVEKVFGLE
     EYWCQCVAWS SSGTTKSQKA YIRIAYLRKN FEQEPLAKEV SLEQGIVLPC RPPEGIPPAE
     VEWLRNEDLV DPSLDPNVYI TREHSLVVRQ ARLADTANYT CVAKNIVARR RSASAAVIVY
     VNGGWSTWTE WSVCSASCGR GWQKRSRSCT NPAPLNGGAF CEGQNVQKTA CATLCPVDGS
     WSPWSKWSAC GLDCTHWRSR ECSDPAPRNG GEECRGADLD TRNCTSDLCL HTSSGPEDVA
     LYIGLVAVAV CLILLLLVLV LIYCRKKEGL DSDVADSSIL TSGFQPVSIK PSKADNPHLL
     TIQPDLSTTT TTYQGSLCPR QDGPSPKFQL SNGHLLSPLG SGRHTLHHSS PTSEAEDFVS
     RLSTQNYFRS LPRGTSNMAY GTFNFLGGRL MIPNTGISLL IPPDAIPRGK IYEIYLTLHK
     PEDVRLPLAG CQTLLSPIVS CGPPGVLLTR PVILAMDHCG EPSPDSWSLR LKKQSCEGSW
     EDVLHLGEES PSHLYYCQLE AGACYVFTEQ LGRFALVGEA LSVAATKRLR LLLFAPVACT
     SLEYNIRVYC LHDTHDALKE VVQLEKQLGG QLIQEPRVLH FKDSYHNLRL SIHDVPSSLW
     KSKLLVSYQE IPFYHIWNGT QQYLHCTFTL ERVNASTSDL ACKVWVWQVE GDGQSFNINF
     NITKDTRFAE MLALESEGGV PALVGPSAFK IPFLIRQKII TSLDPPCSRG ADWRTLAQKL
     HLDSHLSFFA SKPSPTAMIL NLWEARHFPN GNLGQLAAAV AGLGQPDAGL FTVSEAEC
//
ID   WDR11_MOUSE             Reviewed;        1223 AA.
AC   Q8K1X1; Q69ZL3; Q8C937;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=WD repeat-containing protein 11;
DE   AltName: Full=Bromodomain and WD repeat-containing protein 2;
GN   Name=Wdr11; Synonyms=Brwd2, Kiaa1351;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 260-877.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 766-1223.
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Contains 9 WD repeats.
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DR   EMBL; BC037177; AAH37177.1; -; mRNA.
DR   EMBL; AK043051; BAC31449.2; -; mRNA.
DR   EMBL; AK173155; BAD32433.1; -; mRNA.
DR   IPI; IPI00621735; -.
DR   RefSeq; NP_758459.2; NM_172255.3.
DR   UniGene; Mm.229323; -.
DR   ProteinModelPortal; Q8K1X1; -.
DR   SMR; Q8K1X1; 86-122, 544-616.
DR   STRING; Q8K1X1; -.
DR   PRIDE; Q8K1X1; -.
DR   Ensembl; ENSMUST00000084519; ENSMUSP00000081567; ENSMUSG00000042055.
DR   GeneID; 207425; -.
DR   KEGG; mmu:207425; -.
DR   UCSC; uc009jzo.1; mouse.
DR   CTD; 207425; -.
DR   MGI; MGI:1920230; Wdr11.
DR   GeneTree; ENSGT00390000004068; -.
DR   HOGENOM; HBG357721; -.
DR   HOVERGEN; HBG060317; -.
DR   InParanoid; Q8K1X1; -.
DR   OrthoDB; EOG4Q2DDP; -.
DR   NextBio; 371945; -.
DR   ArrayExpress; Q8K1X1; -.
DR   Bgee; Q8K1X1; -.
DR   CleanEx; MM_BRWD2; -.
DR   Genevestigator; Q8K1X1; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 5.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR   PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Membrane; Phosphoprotein; Repeat; Transmembrane; Transmembrane helix;
KW   WD repeat.
FT   CHAIN         1   1223       WD repeat-containing protein 11.
FT                                /FTId=PRO_0000309846.
FT   TRANSMEM   1126   1146       Helical; (Potential).
FT   REPEAT       59    108       WD 1.
FT   REPEAT      111    154       WD 2.
FT   REPEAT      354    393       WD 3.
FT   REPEAT      470    509       WD 4.
FT   REPEAT      565    604       WD 5.
FT   REPEAT      707    744       WD 6.
FT   REPEAT      746    786       WD 7.
FT   REPEAT      792    830       WD 8.
FT   REPEAT      892    939       WD 9.
FT   COMPBIAS   1003   1006       Poly-Leu.
FT   MOD_RES     401    401       Phosphoserine (By similarity).
FT   MOD_RES     405    405       Phosphoserine (By similarity).
FT   MOD_RES    1085   1085       Phosphotyrosine (By similarity).
FT   CONFLICT    482    482       T -> M (in Ref. 2; BAC31449).
FT   CONFLICT    766    780       IAMYNDGAEVWDTKE -> SRMVKDFIFCQSFLQ (in
FT                                Ref. 3; BAD32433).
SQ   SEQUENCE   1223 AA;  135937 MW;  D8C945901E2C245E CRC64;
     MLPYTVNFKV SARTLTGALN AHNKAAVDWG WQGLIAYGCH SLVVVIDSNT AQTLQVLEKH
     KADIVKVRWA RENYHHNIGS PYCLRLASAD VTGKIIVWDV AAGVAQCEIQ EHVKPIQDVQ
     WLWNQDASRD LLLAIHPPNY IVLWNADTGT KLWKKSYADN ILSFSFDPFD PSHLTLLTSE
     GIVFISDFSP SKPPSGPGKK VYISSPHSSP AHNKLAAATG AKKALNKVKI LITQEKPSAD
     FVALNDCLQL AYLPSKRNHM LLLYPREILI LDLEVNQTVG VIAIERTGVP FLQVIPCSQR
     DGLFCLHENG CITLRVRRSY NSICTTSNDE PDLDPVQELT YDLRSQCDAI RVTKTVRPFS
     MVCCPVNENA AALIVSDGRV MIWELKSAVC SRNARNSSGV SPLYSPVSFC GIPGGVLQNK
     LPDLSLDNMI GQSAIAGEEH PKGSILQEVH LKFLLTGLLS GLPSPQFAIR MCPPLTTKNI
     KTYQPLLAVG TSNGSVLVYH LTSGLLHKEL SVHSCEVKGI EWTSLTSFLS FAASTPNNMG
     LVRNELQLVD LPTGRSTAFR GDRGNDESPI EMIKVSHLKQ YLAVVFKDKP LELWDIRTCT
     LLREMSKSFP AITALEWSPS HNLKSLRKKQ LATREAMARQ TVVSDAELGA VESSVISLLQ
     EAESKAELSQ NISAREHFVF TDNDGQVYHL TVEGNSVKDS ARIPPDGSMG SITCIAWKGD
     TLVLGDMDGN LNFWDLKARV SRGIPTHRSW VRKIRFAPGK GNQKLIAMYN DGAEVWDTKE
     VQMVSSLRSG RNVTFRILDV DWCTSDKVIL ASDDGCIRVL EMSMKSTCFR MDEQELVEPV
     WCPYLLVPRA ALALKAFLLH QPWNGRYSLD ISHIDYPENE EIKTLLQEQL HALSNDIKKL
     LLDPDFSLLQ RCLLVSRLYG DESELHFWTV AAHYLHSLSQ AKSGDTVVTK EGAPKDRLSN
     PLDICYDVLC ENTYFQKFQL ERVNLQEVKR STYDHTRKCT DQLLLLGQTD RAVQLLLETS
     ADNQHYYCDS LKACLVTTVT SSGPSQSTIK LVATNMIANG KLAEGVQLLC LIDKAADACR
     YLQTYGEWNR AAWLAKVRLN SEECADVLKR WVDHLCSPQV NQKSKALLVL LSLGCFVSVA
     ETLHSMRYFD RAALFVEACL KYGAFEVSED TEKLIAAIYA DYARSLKSLG FRQGAVRFAS
     KAGAAGRDLL NELGSTKEEL TES
//
ID   COQ9_MOUSE              Reviewed;         313 AA.
AC   Q8K1Z0; Q9CT61;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Ubiquinone biosynthesis protein COQ9, mitochondrial;
DE   Flags: Precursor;
GN   Name=Coq9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=C57BL/6J;
RX   PubMed=14651853; DOI=10.1016/S0092-8674(03)00926-7;
RA   Mootha V.K., Bunkenborg J., Olsen J.V., Hjerrild M., Wisniewski J.R.,
RA   Stahl E., Bolouri M.S., Ray H.N., Sihag S., Kamal M., Patterson N.,
RA   Lander E.S., Mann M.;
RT   "Integrated analysis of protein composition, tissue diversity, and
RT   gene regulation in mouse mitochondria.";
RL   Cell 115:629-640(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-77, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Involved in the biosynthesis of coenzyme Q (By
CC       similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; ubiquinone biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the COQ9 family.
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DR   EMBL; AK004527; BAB23347.1; -; mRNA.
DR   EMBL; AK154343; BAE32528.1; -; mRNA.
DR   EMBL; AK158979; BAE34754.1; -; mRNA.
DR   EMBL; BC036386; AAH36386.1; -; mRNA.
DR   IPI; IPI00169862; -.
DR   RefSeq; NP_080728.1; NM_026452.2.
DR   UniGene; Mm.169234; -.
DR   ProteinModelPortal; Q8K1Z0; -.
DR   STRING; Q8K1Z0; -.
DR   PhosphoSite; Q8K1Z0; -.
DR   PRIDE; Q8K1Z0; -.
DR   Ensembl; ENSMUST00000034234; ENSMUSP00000034234; ENSMUSG00000031782.
DR   GeneID; 67914; -.
DR   KEGG; mmu:67914; -.
DR   UCSC; uc009mxd.1; mouse.
DR   CTD; 67914; -.
DR   MGI; MGI:1915164; Coq9.
DR   eggNOG; roNOG12069; -.
DR   GeneTree; ENSGT00390000009328; -.
DR   HOGENOM; HBG750909; -.
DR   HOVERGEN; HBG079760; -.
DR   InParanoid; Q8K1Z0; -.
DR   OMA; WYTRRAM; -.
DR   OrthoDB; EOG40P47B; -.
DR   PhylomeDB; Q8K1Z0; -.
DR   NextBio; 325934; -.
DR   ArrayExpress; Q8K1Z0; -.
DR   Bgee; Q8K1Z0; -.
DR   CleanEx; MM_COQ9; -.
DR   Genevestigator; Q8K1Z0; -.
DR   GermOnline; ENSMUSG00000031782; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0006744; P:ubiquinone biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR013718; COQ9.
DR   InterPro; IPR012762; Ubiq_biosynth_COQ9.
DR   PANTHER; PTHR21427; COQ9; 1.
DR   Pfam; PF08511; COQ9; 1.
DR   TIGRFAMs; TIGR02396; diverge_rpsU; 1.
PE   1: Evidence at protein level;
KW   Mitochondrion; Phosphoprotein; Transit peptide;
KW   Ubiquinone biosynthesis.
FT   TRANSIT       1     45       Mitochondrion (Potential).
FT   CHAIN        46    313       Ubiquinone biosynthesis protein COQ9,
FT                                mitochondrial.
FT                                /FTId=PRO_0000228638.
FT   MOD_RES      77     77       Phosphotyrosine.
FT   MOD_RES      81     81       Phosphoserine.
FT   CONFLICT    208    208       I -> N (in Ref. 1; BAB23347).
SQ   SEQUENCE   313 AA;  35083 MW;  9B8D8FED0724F138 CRC64;
     MAATAAVSGV LGRLGWRLLQ LRCLPVARCR PALVPRAFHT AVGFRSSEEQ KQQPPHSSSQ
     QHSETQGPEF SRPPPRYTDQ SGEEEEDYES EEQLQHRILT AALEFVPAHG WTAEAIAEGA
     QSLGLSSAAA SMFGSDGSEL ILHFVTQCNA RLNQVLEEEQ KLVQLGQAEK RKTDQFLRDA
     VETRLRMLIP YIEHWPRALS ILLLPHNIPP SLNLLTSMVD DMWHYAGDQS TDFNWYTRRA
     VLAGIYNTTE LVMMQDSSPD FEDTWRFLEN RINDAMNMGH TAKQVKSTGE ALVQGLMGAA
     VTLKNLTGLN QRR
//
ID   CA021_MOUSE             Reviewed;         121 AA.
AC   Q8K207;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Uncharacterized protein C1orf21 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
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DR   EMBL; BC034723; AAH34723.1; -; mRNA.
DR   EMBL; BC055912; AAH55912.1; -; mRNA.
DR   IPI; IPI00169799; -.
DR   RefSeq; NP_932107.1; NM_197990.3.
DR   UniGene; Mm.278031; -.
DR   PhosphoSite; Q8K207; -.
DR   Ensembl; ENSMUST00000044581; ENSMUSP00000036406; ENSMUSG00000032666.
DR   Ensembl; ENSMUST00000121533; ENSMUSP00000113971; ENSMUSG00000032666.
DR   GeneID; 69399; -.
DR   KEGG; mmu:69399; -.
DR   UCSC; uc007cze.1; mouse.
DR   MGI; MGI:1916649; 1700025G04Rik.
DR   GeneTree; ENSGT00390000014594; -.
DR   HOGENOM; HBG283891; -.
DR   HOVERGEN; HBG060374; -.
DR   InParanoid; Q8K207; -.
DR   OMA; SYQNGDV; -.
DR   OrthoDB; EOG40P487; -.
DR   NextBio; 329357; -.
DR   ArrayExpress; Q8K207; -.
DR   Bgee; Q8K207; -.
DR   CleanEx; MM_1700025G04RIK; -.
DR   Genevestigator; Q8K207; -.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    121       Uncharacterized protein C1orf21 homolog.
FT                                /FTId=PRO_0000089247.
FT   MOD_RES      95     95       Phosphoserine (By similarity).
FT   MOD_RES     115    115       Phosphoserine.
SQ   SEQUENCE   121 AA;  13882 MW;  78520C4326C32AFD CRC64;
     MGCASAKHVA TVQNEEEAQR GKSYQNGDVF GDEYRIKPVE EVKYMKNGAE EEQKIAARNQ
     ENLEKSASSN TRLKTNKEIP GLVHQPRANM HISESQQEFF RMLDEKIEKG RDYCSEEEDI
     T
//
ID   GPR56_MOUSE             Reviewed;         687 AA.
AC   Q8K209; Q3UR17; Q9QZT2;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=G-protein coupled receptor 56;
DE   AltName: Full=Serpentine receptor cyt28;
DE   Flags: Precursor;
GN   Name=Gpr56; Synonyms=Cyt28;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Liver;
RA   Phillips R.L., Ernst R.E., Dosil M., Wesley C.K., Moore K.A.,
RA   Kingsley P.D., Sykes S., Palis J., Lemischka I.R.;
RT   "Identification of novel hematopoietic stem cell regulatory genes.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Lung, Pituitary, Placenta, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Could be involved in cell-cell interactions.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       LN-TM7 subfamily.
CC   -!- SIMILARITY: Contains 1 GPS domain.
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DR   EMBL; AF166382; AAF00617.1; -; mRNA.
DR   EMBL; AK087268; BAC39835.1; -; mRNA.
DR   EMBL; AK133678; BAE21780.1; -; mRNA.
DR   EMBL; AK141886; BAE24871.1; -; mRNA.
DR   EMBL; AK141894; BAE24874.1; -; mRNA.
DR   EMBL; AK167547; BAE39613.1; -; mRNA.
DR   EMBL; BC034678; AAH34678.1; -; mRNA.
DR   IPI; IPI00321919; -.
DR   RefSeq; NP_001185823.1; NM_001198894.1.
DR   RefSeq; NP_061370.2; NM_018882.3.
DR   UniGene; Mm.290834; -.
DR   ProteinModelPortal; Q8K209; -.
DR   STRING; Q8K209; -.
DR   MEROPS; S63.011; -.
DR   PRIDE; Q8K209; -.
DR   Ensembl; ENSMUST00000093271; ENSMUSP00000090959; ENSMUSG00000031785.
DR   GeneID; 14766; -.
DR   KEGG; mmu:14766; -.
DR   UCSC; uc009mxl.1; mouse.
DR   CTD; 14766; -.
DR   MGI; MGI:1340051; Gpr56.
DR   eggNOG; roNOG06731; -.
DR   GeneTree; ENSGT00600000084061; -.
DR   HOGENOM; HBG281662; -.
DR   HOVERGEN; HBG051814; -.
DR   InParanoid; Q8K209; -.
DR   OMA; MVVQILR; -.
DR   OrthoDB; EOG45DWNX; -.
DR   PhylomeDB; Q8K209; -.
DR   NextBio; 286855; -.
DR   ArrayExpress; Q8K209; -.
DR   Bgee; Q8K209; -.
DR   CleanEx; MM_GPR56; -.
DR   Genevestigator; Q8K209; -.
DR   GermOnline; ENSMUSG00000031785; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:InterPro.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR003910; GPCR_2_orphan_rcpt_GPR56.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR000203; GPS_dom.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF01825; GPS; 1.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   PRINTS; PR01422; GPR56ORPHANR.
DR   SMART; SM00303; GPS; 1.
DR   PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; FALSE_NEG.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Receptor; Signal; Transducer; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     25       Potential.
FT   CHAIN        26    687       G-protein coupled receptor 56.
FT                                /FTId=PRO_0000012882.
FT   TOPO_DOM     26    402       Extracellular (Potential).
FT   TRANSMEM    403    423       Helical; Name=1; (Potential).
FT   TOPO_DOM    424    442       Cytoplasmic (Potential).
FT   TRANSMEM    443    463       Helical; Name=2; (Potential).
FT   TOPO_DOM    464    471       Extracellular (Potential).
FT   TRANSMEM    472    492       Helical; Name=3; (Potential).
FT   TOPO_DOM    493    512       Cytoplasmic (Potential).
FT   TRANSMEM    513    533       Helical; Name=4; (Potential).
FT   TOPO_DOM    534    570       Extracellular (Potential).
FT   TRANSMEM    571    591       Helical; Name=5; (Potential).
FT   TOPO_DOM    592    603       Cytoplasmic (Potential).
FT   TRANSMEM    604    624       Helical; Name=6; (Potential).
FT   TOPO_DOM    625    630       Extracellular (Potential).
FT   TRANSMEM    631    651       Helical; Name=7; (Potential).
FT   TOPO_DOM    652    687       Cytoplasmic (Potential).
FT   DOMAIN      343    394       GPS.
FT   CARBOHYD     39     39       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    148    148       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    171    171       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    234    234       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    303    303       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    324    324       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    341    341       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    643    643       F -> Y (in Ref. 1; AAF00617).
SQ   SEQUENCE   687 AA;  77255 MW;  B5315D70B66C9A9A CRC64;
     MAVQVLRQMV YFLLSLFSLV QGAHSGSPRE DFRFCGQRNQ TQQSTLHYDQ SSEPHIFVWN
     TEETLTIRAP FLAAPDIPRF FPEPRGLYHF CLYWSRHTGR LHLRYGKHDY LLSSQASRLL
     CFQKQEQSLK QGAPLIATSV SSWQIPQNTS LPGAPSFIFS FHNAPHKVSH NASVDMCDLK
     KELQQLSRYL QHPQKAAKRP TAAFISQQLQ SLESKLTSVS FLGDTLSFEE DRVNATVWKL
     PPTAGLEDLH IHSQKEEEQS EVQAYSLLLP RAVFQQTRGR RRDDAKRLLV VDFSSQALFQ
     DKNSSQVLGE KVLGIVVQNT KVTNLSDPVV LTFQHQPQPK NVTLQCVFWV EDPASSSTGS
     WSSAGCETVS RDTQTSCLCN HLTYFAVLMV SSTEVEATHK HYLTLLSYVG CVISALACVF
     TIAAYLCSRR KSRDYTIKVH MNLLSAVFLL DVSFLLSEPV ALTGSEAACR TSAMFLHFSL
     LACLSWMGLE GYNLYRLVVE VFGTYVPGYL LKLSIVGWGF PVFLVTLVAL VDVNNYGPII
     LAVRRTPERV TYPSMCWIRD SLVSYVTNLG LFSLVFLFNL AMLATMVVQI LRLRPHSQNW
     PHVLTLLGLS LVLGLPWALV FFSFASGTFQ LVILYLFSII TSFQGFLIFL WYWSMRFQAQ
     GGPSPLKNNS DSAKLPISSG STSSSRI
//
ID   PACS1_MOUSE             Reviewed;         961 AA.
AC   Q8K212; Q6P5H8;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 2.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Phosphofurin acidic cluster sorting protein 1;
DE            Short=PACS-1;
GN   Name=Pacs1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-249, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND THR-427, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Coat protein that is involved in the localization of
CC       trans-Golgi network (TGN) membrane proteins that contain acidic
CC       cluster sorting motifs. Controls the endosome-to-Golgi trafficking
CC       of furin and mannose-6-phosphate receptor by connecting the
CC       acidic-cluster-containing cytoplasmic domain of these molecules
CC       with the adapter-protein complex-1 (AP-1) of endosomal clathrin-
CC       coated membrane pits (By similarity).
CC   -!- SUBUNIT: Associates with AP-1 and AP-3 but not with AP-2
CC       complexes. Forms a ternary complex with furin and AP-1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network (By
CC       similarity). Note=Localizes in the perinuclear region, probably
CC       the TGN (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the PACS family.
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DR   EMBL; BC062886; AAH62886.1; -; mRNA.
DR   EMBL; BC034670; AAH34670.1; -; mRNA.
DR   IPI; IPI00321922; -.
DR   RefSeq; NP_694769.2; NM_153129.2.
DR   UniGene; Mm.234923; -.
DR   ProteinModelPortal; Q8K212; -.
DR   STRING; Q8K212; -.
DR   PhosphoSite; Q8K212; -.
DR   PRIDE; Q8K212; -.
DR   Ensembl; ENSMUST00000025786; ENSMUSP00000025786; ENSMUSG00000024855.
DR   GeneID; 107975; -.
DR   KEGG; mmu:107975; -.
DR   UCSC; uc008gci.1; mouse.
DR   CTD; 107975; -.
DR   MGI; MGI:1277113; Pacs1.
DR   GeneTree; ENSGT00390000003281; -.
DR   HOGENOM; HBG358421; -.
DR   HOVERGEN; HBG053488; -.
DR   InParanoid; Q8K212; -.
DR   OMA; KSTWIKN; -.
DR   OrthoDB; EOG4RV2QT; -.
DR   PhylomeDB; Q8K212; -.
DR   NextBio; 359807; -.
DR   ArrayExpress; Q8K212; -.
DR   Bgee; Q8K212; -.
DR   CleanEx; MM_PACS1; -.
DR   Genevestigator; Q8K212; -.
DR   GermOnline; ENSMUSG00000024855; Mus musculus.
DR   GO; GO:0030137; C:COPI-coated vesicle; IDA:MGI.
DR   GO; GO:0000042; P:protein targeting to Golgi; IDA:MGI.
DR   InterPro; IPR019381; Phosphofurin_acidic_CS-1.
DR   Pfam; PF10254; Pacs-1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Golgi apparatus; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    961       Phosphofurin acidic cluster sorting
FT                                protein 1.
FT                                /FTId=PRO_0000058172.
FT   COILED      351    375       Potential.
FT   COMPBIAS     53     82       Ser-rich.
FT   COMPBIAS     60     63       Poly-Ala.
FT   COMPBIAS    110    113       Poly-Ser.
FT   COMPBIAS    277    281       Poly-Glu.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      28     28       Phosphoserine.
FT   MOD_RES      44     44       Phosphothreonine (By similarity).
FT   MOD_RES     249    249       Phosphotyrosine.
FT   MOD_RES     377    377       Phosphoserine (By similarity).
FT   MOD_RES     379    379       Phosphoserine (By similarity).
FT   MOD_RES     405    405       Phosphoserine (By similarity).
FT   MOD_RES     408    408       Phosphoserine (By similarity).
FT   MOD_RES     427    427       Phosphothreonine.
FT   MOD_RES     428    428       Phosphoserine (By similarity).
FT   MOD_RES     493    493       Phosphoserine (By similarity).
FT   MOD_RES     502    502       Phosphothreonine (By similarity).
FT   MOD_RES     526    526       Phosphoserine (By similarity).
FT   MOD_RES     527    527       Phosphoserine (By similarity).
FT   MOD_RES     532    532       Phosphoserine (By similarity).
FT   CONFLICT    816    816       D -> E (in Ref. 1; AAH34670).
SQ   SEQUENCE   961 AA;  104829 MW;  A57F3D86800D9B83 CRC64;
     MAERGGAGGG PGGSGGGSSQ RGSGVAQSPQ QQPQQQPPQP QQPTPPKLAQ ATSSSSSTSA
     AAASSSSSST STSMAVAVAS GSAPPGGPGP GRTPAPVQMN LYATWEVDRS SSSCVPRLFS
     LTLKKLVMLK EMDKDLNSVV IAVKLQGSKR ILRSNEIILP ASGLVETELQ LTFSLQYPHF
     LKRDANKLQI MLQRRKRYKN RTILGYKTLA VGLINMAEVM QHPNEGALVL GLHSNVKDVS
     VPVAEIKIYS LSSQPIDHEG IKSKLSDRSP DIDNYSEEEE ESFSSEQEGS DDPLHGQDLF
     YEDEDLRKVK KTRRKLTSTS AITRQPNIKQ KFVALLKRFK VSDEVGFGLE HVSREQIREV
     EEDLDELYDS LEMYNPSDSG PEMEETESIL STPKPKLKPF FEGMSQSSSQ TEIGSLNSKG
     SLGKDTTSPM ELAALEKVKS TWIKNQDDSL TETDTLEITD QDMFGDVSTS LVVPEKVKTP
     MKSSKADLQG SASPSKVEGT HTPRQKRSTP LKERQLSKPL SERTNSSDSE RSPDLGHSTQ
     IPRKVVYDQL NQILVSDAAL PENVILVNTT DWQGQYVAEL LQDQRKPVVC TCSTVEVQAV
     LSALLTRIQR YCNCNSSMPR PVKVAAVGSQ SYLSSILRFF VKSLASKTPD WLGYMRFLII
     PLGSHPVAKY LGSVDSRYSS TFLDSAWRDL FSRSEPPVSE PLDVVGRVMQ YVNGATTTHQ
     LPVAEAMLTC RHKFPDEDSY QKFIPFIGVV KVGLVEDSPS TAGDGDDSPV VSLTVPSTSP
     PSSSGLSRDA TATPPSSPSM SSALAIVGSP NSPYGDVIGL QVDYWLGHPG ERRREGDKRD
     ASSKNTLKSV FRSVQVSRLP HAGEAQLSGT MAMTVVTKEK NKKVPTIFLS KKPREKEVDS
     KSQVIEGISR LICSAKQQQT MLRVSIDGVE WSDIKFFQLA AQWPTHVKHF PVGLFSGSKT
     T
//
ID   ARFP2_MOUSE             Reviewed;         341 AA.
AC   Q8K221; Q3U3G6; Q9D7M3;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Arfaptin-2;
DE   AltName: Full=ADP-ribosylation factor-interacting protein 2;
GN   Name=Arfip2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Putative target protein of ADP-ribosylation factor.
CC       Involved in membrane ruffling (By similarity).
CC   -!- SUBUNIT: Interacts with RAC1 by binding directly to it.
CC       Specifically binds to GTP-bound ARF1 and ARF6, but binds to
CC       RAC1.GTP and RAC1.GDP with similar affinities (By similarity).
CC   -!- SIMILARITY: Contains 1 AH domain.
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DR   EMBL; AK009100; BAB26070.1; -; mRNA.
DR   EMBL; AK154772; BAE32820.1; -; mRNA.
DR   EMBL; BC013794; AAH13794.1; -; mRNA.
DR   EMBL; BC022942; AAH22942.1; -; mRNA.
DR   EMBL; BC034520; AAH34520.1; -; mRNA.
DR   IPI; IPI00321942; -.
DR   RefSeq; NP_084078.3; NM_029802.4.
DR   UniGene; Mm.41637; -.
DR   ProteinModelPortal; Q8K221; -.
DR   SMR; Q8K221; 119-319.
DR   IntAct; Q8K221; 1.
DR   STRING; Q8K221; -.
DR   PhosphoSite; Q8K221; -.
DR   PRIDE; Q8K221; -.
DR   Ensembl; ENSMUST00000033171; ENSMUSP00000033171; ENSMUSG00000030881.
DR   Ensembl; ENSMUST00000084782; ENSMUSP00000081840; ENSMUSG00000030881.
DR   GeneID; 76932; -.
DR   KEGG; mmu:76932; -.
DR   UCSC; uc009iyr.1; mouse.
DR   CTD; 76932; -.
DR   MGI; MGI:1924182; Arfip2.
DR   eggNOG; roNOG13187; -.
DR   GeneTree; ENSGT00500000044828; -.
DR   HOGENOM; HBG714438; -.
DR   HOVERGEN; HBG050564; -.
DR   InParanoid; Q8K221; -.
DR   OMA; SISTYKC; -.
DR   OrthoDB; EOG4M398W; -.
DR   PhylomeDB; Q8K221; -.
DR   NextBio; 346109; -.
DR   ArrayExpress; Q8K221; -.
DR   Bgee; Q8K221; -.
DR   CleanEx; MM_ARFIP2; -.
DR   Genevestigator; Q8K221; -.
DR   GermOnline; ENSMUSG00000030881; Mus musculus.
DR   GO; GO:0005625; C:soluble fraction; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR010504; Arfaptin.
DR   Gene3D; G3DSA:1.20.1270.60; Arfaptin; 1.
DR   Pfam; PF06456; Arfaptin; 1.
DR   PROSITE; PS50870; AH; 1.
PE   2: Evidence at transcript level;
FT   CHAIN         1    341       Arfaptin-2.
FT                                /FTId=PRO_0000064668.
FT   DOMAIN      121    321       AH.
FT   CONFLICT    107    107       T -> K (in Ref. 2; AAH34520).
SQ   SEQUENCE   341 AA;  37773 MW;  AA3BE39EF0C75037 CRC64;
     MTDGILGKAA TMEIPIHGNG EAGQLPEDDG LEQDLQQVMV SGPNLNETSI VSGGYGGSGD
     GLIPTGSGRH PSHSTSPSGP GDEVARGIAG EKFDIVKKWG INTYKCTKQL LSERFGRGSR
     TVDLELELQI ELLRETKRKY ESVLQLGRAL TAHLYSLLQT QHALGDAFAD LSQKSPELQE
     EFGYNAETQK LLCKNGETLL GAVNFFVSSI NTLVTKTMED TLMTVKQYEA ARLEYDAYRT
     DLEELSLGPR DAGTRGRLES AQATFQTHRD KYEKLRGDVA IKLKFLEENK IKVMHKQLLL
     FHNAVSAYFA GNQKQLEQTL QQFNIKLRPP GAEKPSWLEE Q
//
ID   ABCF3_MOUSE             Reviewed;         709 AA.
AC   Q8K268; Q9JL49;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=ATP-binding cassette sub-family F member 3;
GN   Name=Abcf3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 589-709.
RC   STRAIN=CD-1;
RX   MEDLINE=20175428; PubMed=10708515; DOI=10.1006/geno.1999.6102;
RA   Schriml L.M., Dean M.;
RT   "Identification of 18 mouse ABC genes and characterization of the ABC
RT   superfamily in Mus musculus.";
RL   Genomics 64:24-31(2000).
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF
CC       family. EF3 subfamily.
CC   -!- SIMILARITY: Contains 2 ABC transporter domains.
CC   -!- CAUTION: Lacks transmembrane domains and is probably not involved
CC       in transport.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF31421.1; Type=Frameshift; Positions=599;
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DR   EMBL; BC032923; AAH32923.1; -; mRNA.
DR   EMBL; AF213381; AAF31421.1; ALT_FRAME; mRNA.
DR   IPI; IPI00169840; -.
DR   RefSeq; NP_038880.1; NM_013852.2.
DR   UniGene; Mm.27135; -.
DR   HSSP; P58301; 1F2T.
DR   ProteinModelPortal; Q8K268; -.
DR   SMR; Q8K268; 178-696.
DR   PhosphoSite; Q8K268; -.
DR   PRIDE; Q8K268; -.
DR   Ensembl; ENSMUST00000003319; ENSMUSP00000003319; ENSMUSG00000003234.
DR   GeneID; 27406; -.
DR   KEGG; mmu:27406; -.
DR   UCSC; uc007ypz.1; mouse.
DR   CTD; 27406; -.
DR   MGI; MGI:1351656; Abcf3.
DR   eggNOG; roNOG15484; -.
DR   GeneTree; ENSGT00550000074722; -.
DR   HOGENOM; HBG758042; -.
DR   HOVERGEN; HBG050440; -.
DR   InParanoid; Q8K268; -.
DR   OMA; DADVWRK; -.
DR   OrthoDB; EOG4PNXGK; -.
DR   PhylomeDB; Q8K268; -.
DR   NextBio; 305414; -.
DR   ArrayExpress; Q8K268; -.
DR   Bgee; Q8K268; -.
DR   Genevestigator; Q8K268; -.
DR   GermOnline; ENSMUSG00000003234; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding; Phosphoprotein; Repeat.
FT   CHAIN         1    709       ATP-binding cassette sub-family F member
FT                                3.
FT                                /FTId=PRO_0000248043.
FT   DOMAIN      178    424       ABC transporter 1.
FT   DOMAIN      492    707       ABC transporter 2.
FT   NP_BIND     210    217       ATP 1 (Potential).
FT   NP_BIND     525    532       ATP 2 (Potential).
FT   MOD_RES     283    283       Phosphoserine (By similarity).
FT   CONFLICT    705    706       RE -> SG (in Ref. 2; AAF31421).
SQ   SEQUENCE   709 AA;  79865 MW;  03CBD4E7FD967B79 CRC64;
     MATCADILRS EFPEIDGQVF DYVTGVLHSG SADFESVDDL VEAVGELLQE VSGDSKDDAG
     IRAVCQRMYN TLRLAEPQNQ GNSQVLLDAP IQLSKIMENY DCDTKLPGLL KREQSSTVNA
     KKLEKAEARL KAKQEKRSEK ETLKTSNPLV LEEASASQAG SRKESRLESS GKNKSYDVRI
     ENFDVSFGDR VLLAGADVNL AWGRRYGLVG RNGLGKTTLL KMLATRSLRV PAHISLLHVE
     QEVAGDDTPA LQSVLESDTV REDLLRQERE LSLRIAAGRA EGSEAAQLAE IYGKLEEIEA
     DKAPARASVI LAGLGFTPKM QQQPTREFSG GWRMRLALAR ALFARPDLLL LDEPTNMLDV
     RAILWLENYL QTWPSTILVV SHDRNFLNAI ATDIIHLHSQ RLDGYRGDFE TFIKSKQERL
     LNQQREYEAQ QQYRQHIQVF IDRFRYNANR ASQVQSKLKM LEKLPELKPV DKESEVVLKF
     PDGFEKFSPP ILQLDEVDFY YDPKHSIFSR LSVSADLESR ICVVGENGAG KSTMLKLLMG
     DLSPVRGIRH AHRNLKIGYF SQHHVEQLDL NVSAVELLAR KFPGLPEEEY RHQLGRYGIS
     GELAMRPVAS LSGGQKSRVA FAQMTMPCPN FYILDEPTNH LDMETIEALG QALNNFRGGV
     ILVSHDERFI RLVCKELWVC ENGSVTRVEG GFDQYRALLQ EQFRREGFL
//
ID   MMGT1_MOUSE             Reviewed;         131 AA.
AC   Q8K273; A7UH87;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Membrane magnesium transporter 1;
DE   AltName: Full=Transmembrane protein 32;
DE   Flags: Precursor;
GN   Name=Mmgt1; Synonyms=Tmem32;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RX   PubMed=18057121; DOI=10.1152/ajpcell.00238.2007;
RA   Goytain A., Quamme G.A.;
RT   "Identification and characterization of a novel family of membrane
RT   magnesium transporters, MMgT1 and MMgT2.";
RL   Am. J. Physiol. 294:C495-C502(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain cortex, Cerebellum, and Embryonic spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Mediates Mg(2+) transport.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       type I membrane protein (By similarity). Golgi apparatus membrane;
CC       Single-pass type I membrane protein. Early endosome membrane;
CC       Single-pass type I membrane protein. Note=Detected in the Golgi
CC       apparatus and in post-Golgi vesicles including early endosomes.
CC   -!- TISSUE SPECIFICITY: Abundant in heart muscle and kidney with lower
CC       levels in liver and brain and very little expression in intestine
CC       or colon. In kidney, highest levels in distal convoluted tubule.
CC   -!- INDUCTION: Up-regulated by low extracellular Mg(2+).
CC   -!- SIMILARITY: Belongs to the membrane magnesium transporter family.
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DR   EMBL; EU069461; ABS87351.1; -; mRNA.
DR   EMBL; AK036253; BAC29362.1; -; mRNA.
DR   EMBL; AK043524; BAC31567.1; -; mRNA.
DR   EMBL; AK049689; BAC33874.1; -; mRNA.
DR   EMBL; BC032271; AAH32271.1; -; mRNA.
DR   IPI; IPI00169845; -.
DR   RefSeq; NP_666346.1; NM_146234.3.
DR   UniGene; Mm.291824; -.
DR   STRING; Q8K273; -.
DR   TCDB; 1.A.67.1.1; membrane Mg2+ transporter (MMgT) family.
DR   PhosphoSite; Q8K273; -.
DR   PRIDE; Q8K273; -.
DR   Ensembl; ENSMUST00000059899; ENSMUSP00000051621; ENSMUSG00000061273.
DR   GeneID; 236792; -.
DR   KEGG; mmu:236792; -.
DR   UCSC; uc009tgj.1; mouse.
DR   CTD; 236792; -.
DR   MGI; MGI:2384305; Mmgt1.
DR   eggNOG; roNOG15658; -.
DR   GeneTree; ENSGT00510000047104; -.
DR   HOGENOM; HBG557500; -.
DR   HOVERGEN; HBG105215; -.
DR   InParanoid; Q8K273; -.
DR   OMA; FKEIRAT; -.
DR   OrthoDB; EOG4MCX1R; -.
DR   PhylomeDB; Q8K273; -.
DR   NextBio; 383082; -.
DR   ArrayExpress; Q8K273; -.
DR   Bgee; Q8K273; -.
DR   Genevestigator; Q8K273; -.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0015087; F:cobalt ion transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0015093; F:ferrous iron transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0006825; P:copper ion transport; IDA:MGI.
DR   InterPro; IPR018937; Magnesium_transport.
DR   Pfam; PF10270; Tmemb_32; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Endosome; Golgi apparatus; Magnesium; Membrane;
KW   Signal; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21    131       Membrane magnesium transporter 1.
FT                                /FTId=PRO_0000286436.
FT   TOPO_DOM     21     44       Lumenal (Potential).
FT   TRANSMEM     45     65       Helical; (Potential).
FT   TOPO_DOM     66    131       Cytoplasmic (Potential).
SQ   SEQUENCE   131 AA;  14677 MW;  DB3841F8CCBD801E CRC64;
     MAPSLWKGLV GVGLFALAHA AFSAAQHRSY MRLTEKEDES LPIDIVLQTL LAFAVTCYGI
     VHIAGEFKDM DATSELKNKT FDTLRNHPSF YVFNHRGRVL FRPSDATNSS NLDALSSNTS
     LKLRKFDSLR R
//
ID   TF3C1_MOUSE             Reviewed;        2101 AA.
AC   Q8K284; Q8CAL9;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 2.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=General transcription factor 3C polypeptide 1;
DE   AltName: Full=TF3C-alpha;
DE   AltName: Full=TFIIIC box B-binding subunit;
DE   AltName: Full=Transcription factor IIIC 220 kDa subunit;
DE            Short=TFIIIC 220 kDa subunit;
DE            Short=TFIIIC220;
DE   AltName: Full=Transcription factor IIIC subunit alpha;
GN   Name=Gtf3c1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Required for RNA polymerase III-mediated transcription.
CC       Component of TFIIIC that initiates transcription complex assembly
CC       on tRNA and is required for transcription of 5S rRNA and other
CC       stable nuclear and cytoplasmic RNAs. Binds to the box B promoter
CC       element (By similarity).
CC   -!- SUBUNIT: Part of the TFIIIC subcomplex TFIIIC2, consisting of six
CC       subunits, GTF3C1, GTF3C2, GTF3C3, GTF3C4, GTF3C5 and GTF3C6 (By
CC       similarity). Interacts with IGHMBP2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8K284-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K284-2; Sequence=VSP_010576;
CC         Note=Incomplete sequence;
CC       Name=3;
CC         IsoId=Q8K284-3; Sequence=VSP_010573, VSP_010574, VSP_010575;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the TFIIIC subunit 1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH32208.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK038537; BAC30032.1; -; mRNA.
DR   EMBL; BC032208; AAH32208.1; ALT_INIT; mRNA.
DR   EMBL; BC067041; AAH67041.1; -; mRNA.
DR   IPI; IPI00403414; -.
DR   IPI; IPI00416203; -.
DR   IPI; IPI00416204; -.
DR   RefSeq; NP_997122.1; NM_207239.1.
DR   UniGene; Mm.294173; -.
DR   STRING; Q8K284; -.
DR   PhosphoSite; Q8K284; -.
DR   PRIDE; Q8K284; -.
DR   Ensembl; ENSMUST00000055506; ENSMUSP00000056719; ENSMUSG00000032777.
DR   Ensembl; ENSMUST00000106423; ENSMUSP00000102031; ENSMUSG00000032777.
DR   GeneID; 233863; -.
DR   KEGG; mmu:233863; -.
DR   UCSC; uc009jqh.1; mouse.
DR   UCSC; uc009jql.1; mouse.
DR   CTD; 233863; -.
DR   MGI; MGI:107887; Gtf3c1.
DR   GeneTree; ENSGT00390000008664; -.
DR   HOGENOM; HBG714289; -.
DR   HOVERGEN; HBG057283; -.
DR   InParanoid; Q8K284; -.
DR   OMA; YIFSVVE; -.
DR   OrthoDB; EOG40CHG3; -.
DR   NextBio; 381879; -.
DR   ArrayExpress; Q8K284; -.
DR   Bgee; Q8K284; -.
DR   CleanEx; MM_GTF3C1; -.
DR   Genevestigator; Q8K284; -.
DR   GermOnline; ENSMUSG00000032777; Mus musculus.
DR   GO; GO:0030529; C:ribonucleoprotein complex; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR007309; TFIIIC_Bblock-bd.
DR   Pfam; PF04182; B-block_TFIIIC; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW   Transcription.
FT   CHAIN         1   2101       General transcription factor 3C
FT                                polypeptide 1.
FT                                /FTId=PRO_0000209711.
FT   COMPBIAS    344    354       Asp/Glu-rich (acidic).
FT   COMPBIAS   1199   1227       Arg/Lys-rich (basic).
FT   COMPBIAS   1607   1617       Asp/Glu-rich (acidic).
FT   MOD_RES     751    751       Phosphoserine (By similarity).
FT   MOD_RES     774    774       Phosphothreonine (By similarity).
FT   MOD_RES    1063   1063       Phosphoserine (By similarity).
FT   MOD_RES    1646   1646       Phosphothreonine (By similarity).
FT   MOD_RES    1854   1854       Phosphoserine (By similarity).
FT   VAR_SEQ       1    156       Missing (in isoform 3).
FT                                /FTId=VSP_010573.
FT   VAR_SEQ     326    375       TDVMVRCLKLLKEFKRKMEDDHDDDDDEEVISKGVPPVDIV
FT                                FERDMLTQT -> KSRTLWPTGSPCCHFLWSHSALKCEDYT
FT                                SFSSLLLSAFYLKRIREVCPEF (in isoform 3).
FT                                /FTId=VSP_010574.
FT   VAR_SEQ     376   2101       Missing (in isoform 3).
FT                                /FTId=VSP_010575.
FT   VAR_SEQ    1503   1598       Missing (in isoform 2).
FT                                /FTId=VSP_010576.
FT   CONFLICT   1599   1599       S -> N (in Ref. 2; AAH32208).
SQ   SEQUENCE   2101 AA;  237476 MW;  182C2EFFD9599AD6 CRC64;
     MDALESLLDE VALEGLDGLC LPALWSRLES RSPAFPLPLE PYTQEFLWRA LATHPGISFY
     EEPRERPDLQ LQDRYEEIDL ETGILESRRD PVTLEDVYPI HMILENKDGI QGSCRYFKER
     KDITSSIRSK CLQPRCTMVE AFSRWGKKLI IVASQDMRYR ALIGLEGDPD LKLPDFSYCI
     LERLGRSRWQ GELQRDLHTT AFKVDAGKLH YHRKILNKNG LITMQSHVIR LPTGAQQHSI
     LLLLNRFHVD RRSKYDILME KLSMMLSTRS NQIETLGKLR EELGLCERTF KRLYQYMLNA
     GLAKVVSLPL QEIHPECGPC KTKKGTDVMV RCLKLLKEFK RKMEDDHDDD DDEEVISKGV
     PPVDIVFERD MLTQTYELIE RRGTKGISQA EIRVAMNVGK LEARMLCRLL QRFKVVKGFM
     EDEGRQRTTK YISCVFAEES DLSRQYAREK ARGELLTTVS LASVQDESLM PEGEEAFLSD
     SESEEESSCS GGKRRGRGSR GHARASGDAG SGSRPHHSTP AKGGWKVLNL HPLKKPKAAA
     EERSRRSSAC RDGLDTSSSS ELNAPFDPHS MDSHSGDIAV IEEVRLDNPK EGGGSQKGGR
     HGSSQDKPHK TYRLLKRRNL IIEAVTNLRL IESLFTIQKM IMDQEKQEGV STKCCKKSII
     RLVRNLSEEG LLRLYRTTVI QDGIKKKVDL VVHPSMDQND PLVRSAIEQV RFRISNSSTA
     NRVKVPPAPA PQEEAEEENQ EPEVPSRSAN SDPNTSSKPE STRVKKTDEK MGITPLKNYK
     PVIVPGLGRS IGFLPKMPRL KAMHLFLWYL VYGHPAGHTG EQPALHSERK TGKQESSRPG
     AQPSSGDDWD TSEAKNNTES SSWESEMELS TEIVYVDEIS WMRYVPPIPI HRDFGFGWAL
     VSDILLCLPL SIFVQLVQVS YKVDNLEDFL NDPLKKHTLI RFLPRHIRQQ LLYKRRYIFS
     VVENLQRLCY MGLLQFGPTE KFQDKDQVFV FLKKNAVIVD TTICDPHYNL AHSSRPFERR
     LYVLDSMQDV ECYWFDLQCI CLNTPLGVVR CPCAQKICPD PGSDPEGSLR KEQESAMDKH
     NLERKCAMLE YTTGSREVVD EGLVPGDGLG AAGLDSSFYA HLKRNWVWTS YIINKARKNN
     TSENGLTGRL QTFLSKRPMP LGSGGSGRLP LWSEGRADAE LCADKEEQFE LDREPTPGRN
     RKVRGGKSQK RKRLKKEPIR KTKRRRRGEH PEAKSKKLRY QDEADQNALR MMTRLRVSWS
     MQEDGLLMLC RIASNVLNTK VKGPFVTWQV VRDILHATFE ESLDKTSHSV GRRARYIVKN
     PQAFMNYKVC LAEVYQDKAL VGDFMSRKGN YEDPKVCAKE FKEFVEKLKE KFSSGLRNPN
     LEIPNTLQEL FAKYRVLAIG DEKDRVRKED ELNSVEDIHF LVLQNLIQST LSLSNSQSNS
     CQSFQIFRLY REFREPVLVR AFMECQKRSL VNRRRVSHSQ GPKKNRAVPF VPMSYQLSQS
     YYKLFTWRFP TTICTESFQF YDRLRTNGML DQPDHFSFKD LDSSDPSNDL VAFSLDSPGG
     HCVTALALFS LGLLSVDVRI PEQIVVVDSS MVESEVMKSL GKDGGLDDDE EEEDLDEGSG
     TKRQGVEVKA HQASHTKYLL MRGYYTVPGM VSTRNLNPND SIVVNSCQVK FRLRNTPAST
     QLGPTGFTAT PLEELQAGLS CLPASFTSLV DPQLRTHCPE EFAHQMAQSG YSPEDVAASL
     EILQAVAAAD CFGIDKEKLS RQFSALEKIA DRRTRTFLDY IQDLLEQEQV MEVGGNTVRL
     VTMASAQPWL LHSMRLRDME VDTKASGDDS QSRLPEGPSI EDHTSEGAAV PPVSSHSTKK
     RPHCPETDAE EATRLPAKKP TLQDVRVAAS PRPGAEEQAE AQAPAQLAAP EDADAGGPRQ
     ENQENVGVSG LEQLGCEFQL PEGSEDPRGL TESNMAQAAW ESGCERVCFV GRPWRGVDGH
     LNMPVCKGML EAVLYHIMSR PGVPESCLLQ YYQGVLQPVA VLELLRGLES LGCIQKRTLR
     KPASVSLFSR PVVEGLGQAS EAEALSCHES TVTFYEPTLD CTIRLGRVFP HDINWNKWIH
     L
//
ID   MTMR3_MOUSE             Reviewed;        1196 AA.
AC   Q8K296; Q5NCA4;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   08-FEB-2011, entry version 69.
DE   RecName: Full=Myotubularin-related protein 3;
DE            EC=3.1.3.48;
GN   Name=Mtmr3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613 AND THR-1179, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Phosphatase that acts on lipids with a phosphoinositol
CC       headgroup. Has phosphatase activity towards phosphatidylinositol-
CC       3-phosphate and phosphatidylinositol-3,5-bisphosphate. May also
CC       dephosphorylate proteins phosphorylated on Ser, Thr, and Tyr
CC       residues (By similarity).
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K296-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K296-2; Sequence=VSP_026027;
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class myotubularin subfamily.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 1 myotubularin phosphatase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI35184.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL645910; CAI35184.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC032166; AAH32166.1; -; mRNA.
DR   IPI; IPI00551495; -.
DR   IPI; IPI00649536; -.
DR   UniGene; Mm.425669; -.
DR   ProteinModelPortal; Q8K296; -.
DR   SMR; Q8K296; 35-579, 1035-1180.
DR   STRING; Q8K296; -.
DR   PhosphoSite; Q8K296; -.
DR   PRIDE; Q8K296; -.
DR   Ensembl; ENSMUST00000093376; ENSMUSP00000091068; ENSMUSG00000034354.
DR   MGI; MGI:1921552; Mtmr3.
DR   eggNOG; roNOG09974; -.
DR   GeneTree; ENSGT00580000081198; -.
DR   HOGENOM; HBG715843; -.
DR   HOVERGEN; HBG052526; -.
DR   InParanoid; Q8K296; -.
DR   OMA; RLESQYL; -.
DR   PhylomeDB; Q8K296; -.
DR   BRENDA; 3.1.3.48; 244.
DR   ArrayExpress; Q8K296; -.
DR   Bgee; Q8K296; -.
DR   CleanEx; MM_MTMR3; -.
DR   Genevestigator; Q8K296; -.
DR   GermOnline; ENSMUSG00000034354; Mus musculus.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR010569; Myotub-related.
DR   InterPro; IPR017906; Myotubularin_phosphatase_dom.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF06602; Myotub-related; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; FALSE_NEG.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Hydrolase; Metal-binding;
KW   Phosphoprotein; Protein phosphatase; Zinc; Zinc-finger.
FT   CHAIN         1   1196       Myotubularin-related protein 3.
FT                                /FTId=PRO_0000094937.
FT   DOMAIN      155    576       Myotubularin phosphatase.
FT   ZN_FING    1117   1177       FYVE-type.
FT   REGION      326    329       Substrate binding (By similarity).
FT   REGION      351    352       Substrate binding (By similarity).
FT   REGION      413    419       Substrate binding (By similarity).
FT   COILED     1027   1060       Potential.
FT   ACT_SITE    413    413       Phosphocysteine intermediate (By
FT                                similarity).
FT   BINDING     459    459       Substrate (By similarity).
FT   MOD_RES     613    613       Phosphoserine.
FT   MOD_RES     633    633       Phosphoserine (By similarity).
FT   MOD_RES     647    647       Phosphoserine (By similarity).
FT   MOD_RES    1179   1179       Phosphothreonine.
FT   VAR_SEQ    1076   1196       Missing (in isoform 2).
FT                                /FTId=VSP_026027.
FT   CONFLICT    782    782       R -> S (in Ref. 2; AAH32166).
FT   CONFLICT   1074   1074       T -> V (in Ref. 2; AAH32166).
SQ   SEQUENCE   1196 AA;  133840 MW;  409D23ABBEABAC7D CRC64;
     MDEEMRHSLE CIQANQIFPR KQLIREDENL QVPFLELHGE STEYVGRAEE AIIALSNYRL
     HIKFKESLVN VPLQLIESVE CRDIFQLHLT CKDCKVIRCQ FPTFEQCQDW LKRLNNAIRP
     PGKIEDLFSF AYHAWCMEVY ASEKEQHGDL CRPGEHVTSR FKNEVERMGF DMNNAWRISN
     INEKYKLCGS YPQELIVPAW ITDKELESVA GFRSWKRIPA VIYRHQSNGA VIARCGQPEV
     SWWGWRNADD EHLVQSVARA CASDSQSSIS KVSTRNSCRD FPNAGDLSDV EFDSSLSNTS
     GAESLALQPQ KLLILDARSY AAAVANRAKG GGCECPEYYP NCEVVFMGMA NIHSIRRSFQ
     SLRLLCTQMP DPGNWLSALE STKWLHHLSV LLKSALLVVH AVDRDQRPVL VHCSDGWDRT
     PQIVALAKLL LDPYYRTIEG FQVLVEMEWL DFGHKFADRC GHGEDSDDLN ERCPVFLQWL
     DCVHQLQRQF PCSFEFNEAF LVKLVQHTYS CLFGTFLCNN AKERGEKQTQ ERTCSVWSLL
     RAGNKAFKNL LYSSQSEAVL YPVCHVRNLM LWSAVYLPCP SPSTPTDDSC APYPVPGTSP
     DEPPLSRLPK TRSFDNLTTT CENMVPLASR RSSDPSLNEK WQEHGRSLEL SSFASAGEEV
     PAMDSLRKPS RLLGGAELSV AAGVAEGQME NILQEATKEE SGVEEPTHRG HTEVPEVKEE
     APLAKESSMA AEGPVVLYQE PQLDDATLRS HQGPSLSLFS QGIPEHQDGH NVLSSSLQAP
     LRGEDSQEVP VEQPQVENIA EDRENVAPAV PVDAKVGLGI SQSSSLLPSQ VPFETRGPHI
     NNSVHMLLED KVKSESGPQL HHRPCPASSG RFSGKDMLPV APEPRSAERP QWDSVLHRTS
     SPGNTLSLLQ APCALPLDKC RQGIVCNGAL ETENKASEQP AGFDTLQKYP TPNGHCANWE
     AGRSKDSLSH QLSATSCSSA HLYSRNLHHK WLNSHSGRPS TTSSPDQPSR SHLDDDGMPV
     YTDTIQQRLR QIESGHQQEV ETLKKQVQEL KSRLESQYLT SSLRFNGDFG DEVTSIPDSE
     SNLDQNCVSR CSTEIFSEAS WEQVDKQDTE MTRWLPDHLA AHCYACDSAF WLASRKHHCR
     NCGNVFCSSC CNQKVPVPSQ QLFEPSRVCK SCYSSLHPTS SSIDLELDKP IAATSN
//
ID   ANLN_MOUSE              Reviewed;        1121 AA.
AC   Q8K298; Q8BL79; Q8BLB3; Q8K2N0; Q9CUY0;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Actin-binding protein anillin;
GN   Name=Anln;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 247-1121.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-510, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Required for cytokinesis. Essential for the structural
CC       integrity of the cleavage furrow and for completion of cleavage
CC       furrow ingression (By similarity).
CC   -!- SUBUNIT: Interacts with F-actin. Interacts with CD2AP. May
CC       interact with RHOA. Interacts with FZR1/CDH1 during mitotic exit
CC       (By similarity).
CC   -!- INTERACTION:
CC       Q9NQW6:ANLN (xeno); NbExp=1; IntAct=EBI-2553580, EBI-2553589;
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity). Cytoplasm, cell cortex (By
CC       similarity). Note=Mainly found in the nucleus during interphase.
CC       Colocalizes with cortical F-actin upon nuclear envelope breakdown
CC       in mitosis and subsequently concentrates in the area of the
CC       prospective contractile ring in anaphase. This pattern persists
CC       until telophase, when the protein becomes concentrated in the
CC       midbody.
CC   -!- PTM: Phosphorylated during mitosis (By similarity).
CC   -!- PTM: Ubiquitinated, and this requires FZR1/CDH1 (By similarity).
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH30489.1; Type=Erroneous initiation;
CC       Sequence=BAC32605.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; BC030489; AAH30489.1; ALT_INIT; mRNA.
DR   EMBL; BC032164; AAH32164.1; -; mRNA.
DR   EMBL; AK013624; BAB28931.3; -; mRNA.
DR   EMBL; AK045703; BAC32464.1; -; mRNA.
DR   EMBL; AK046102; BAC32605.1; ALT_INIT; mRNA.
DR   IPI; IPI00172197; -.
DR   RefSeq; NP_082666.2; NM_028390.3.
DR   UniGene; Mm.282751; -.
DR   UniGene; Mm.453238; -.
DR   ProteinModelPortal; Q8K298; -.
DR   SMR; Q8K298; 978-1104.
DR   IntAct; Q8K298; 1.
DR   STRING; Q8K298; -.
DR   PhosphoSite; Q8K298; -.
DR   PRIDE; Q8K298; -.
DR   Ensembl; ENSMUST00000040912; ENSMUSP00000045873; ENSMUSG00000036777.
DR   GeneID; 68743; -.
DR   KEGG; mmu:68743; -.
DR   NMPDR; fig|10090.3.peg.19782; -.
DR   UCSC; uc009ook.1; mouse.
DR   CTD; 68743; -.
DR   MGI; MGI:1920174; Anln.
DR   GeneTree; ENSGT00390000008749; -.
DR   HOGENOM; HBG444893; -.
DR   HOVERGEN; HBG059477; -.
DR   InParanoid; Q8K298; -.
DR   OMA; SKESPAR; -.
DR   OrthoDB; EOG41ZF92; -.
DR   PhylomeDB; Q8K298; -.
DR   NextBio; 327834; -.
DR   ArrayExpress; Q8K298; -.
DR   Bgee; Q8K298; -.
DR   Genevestigator; Q8K298; -.
DR   GermOnline; ENSMUSG00000036777; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Cell cycle; Cell division; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Mitosis; Nucleus; Phosphoprotein;
KW   Ubl conjugation.
FT   CHAIN         1   1121       Actin-binding protein anillin.
FT                                /FTId=PRO_0000227966.
FT   DOMAIN      980   1104       PH.
FT   REGION        1    228       Nuclear localization (By similarity).
FT   REGION        1    154       Interaction with CD2AP (By similarity).
FT   REGION        1     45       Required for ubiquitination (By
FT                                similarity).
FT   REGION      229    671       Interaction with F-actin (By similarity).
FT   REGION      725   1121       Localization to the cleavage furrow (By
FT                                similarity).
FT   COILED      564    599       Potential.
FT   MOD_RES      73     73       Phosphoserine (By similarity).
FT   MOD_RES      96     96       Phosphoserine (By similarity).
FT   MOD_RES     192    192       Phosphothreonine (By similarity).
FT   MOD_RES     316    316       Phosphothreonine (By similarity).
FT   MOD_RES     318    318       Phosphoserine (By similarity).
FT   MOD_RES     359    359       Phosphothreonine (By similarity).
FT   MOD_RES     366    366       N6-acetyllysine (By similarity).
FT   MOD_RES     392    392       Phosphothreonine (By similarity).
FT   MOD_RES     396    396       Phosphothreonine (By similarity).
FT   MOD_RES     444    444       Phosphoserine (By similarity).
FT   MOD_RES     510    510       Phosphothreonine.
FT   MOD_RES     513    513       Phosphoserine (By similarity).
FT   MOD_RES     548    548       Phosphoserine (By similarity).
FT   MOD_RES     637    637       Phosphoserine.
FT   MOD_RES     653    653       Phosphoserine (By similarity).
FT   MOD_RES     656    656       Phosphoserine (By similarity).
FT   MOD_RES     659    659       Phosphoserine (By similarity).
FT   MOD_RES     787    787       Phosphoserine (By similarity).
FT   MOD_RES     924    924       Phosphoserine (By similarity).
FT   CONFLICT    366    366       K -> N (in Ref. 1; AAH32164).
FT   CONFLICT    613    613       G -> S (in Ref. 2; BAC32464).
SQ   SEQUENCE   1121 AA;  122794 MW;  0D23488D3264E525 CRC64;
     MDPFTEKLLE RTRARRENLQ RKMAERPTAV ARSAPHAKRG REPLSEASNQ QQPLPGGEEK
     SCTKPSPSKK RCSDKIEVGA PDLENTEPID VAKPCSPMPA PRQAKPPAPA AISESVAAPA
     ALLSADRGLN SGSEASATSS VKTRMQRLAE QRRHWDSDLT DDVSESSYFA PVPTEDKAAS
     PSKPPISNAS ATPVGRRGRL ANLAATICSW EDDVSHSSAK QNSVQEQPGT ACLSKSSSAS
     GASASINSSS VQQEATCCSP RDGNASVRKD PSSNAAHGPL LSASVSSSVK ASSPVTAATF
     ITENREAQNP ELLHKTASPL KTEARKPCEK PTLSQGAQPK EEANREVCLQ SQSKDKLATP
     GGRGIKPFLE RFGERCQEHS KESPSYRASH KTPNITPNTK AIQERLFKQN TCSSTTHLAQ
     QLKQEREKEL ACLRGRLDKG NLWSAEKNEK SRSKHLETKQ EVHCQNTPLK KHQTVASTPL
     TSVTDKVAEN EPAVKLSSTE PAGSTESEMT KSSPLKITLF LEEEKSLKVA SDLEVEQNTE
     AVREVEMSVD DEDINSSRVI NDIFSDVLEE GELDVEKSQE EMDQVGAENS EEQEDALNIS
     SMSLLAPLAQ TVGVVSLENV ISSPPSELRD SNLSAASPKP GKFQRTRVPR AESADSLGSE
     DRDLLYSIDA YRSQRFKETE RPSIKQVIVR KEDVTSKLGE KKNVFSGQVN IKQKMQELNN
     DINLQQTVIY QASQALNCCV DEEHGKGSLE EAEAERLLLI ATEKRALLID ELNKLKSEGP
     QRRNKTSVIS QSEFAPSKGS VTLSEICLPL KADFVCSTAQ KTDASNYYYL IMLKAGAEQM
     VATPLASTAN SLSGDALTFP TTFTLHDVSN DFEINIEVYS LVQKKDSLGP DKKKKASKSK
     AITPKRLLTS ITSKSSLHSS VMASPGGLGA VRTSNFTLVG SHTLSLSSVG DTKFALDKVP
     FLSPLEGHIC LKISCQVNSA VEEKGFLTIF EDVSGFGAWH RRWCVLSGNC ISYWTYPDDE
     RRKNPIGRIN LANCISHQIE PANREFCARR NTLELITVRP QREDDRETLV SQCRDTLCVT
     KNWLSADTKE ERDLWMQKLN QVIVDIRLWQ PDACYKPVGK P
//
ID   HACD3_MOUSE             Reviewed;         362 AA.
AC   Q8K2C9; O09003; Q6PGH3; Q8BGM8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=3-hydroxyacyl-CoA dehydratase 3;
DE            Short=HACD3;
DE            EC=4.2.1.-;
DE   AltName: Full=Butyrate-induced protein 1;
DE            Short=B-ind1;
DE   AltName: Full=Protein tyrosine phosphatase-like protein PTPLAD1;
DE   AltName: Full=Protein-tyrosine phosphatase-like A domain-containing protein 1;
GN   Name=ptplad1; Synonyms=hacd3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart, Pancreas, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-190.
RX   MEDLINE=20298798; PubMed=10747961; DOI=10.1074/jbc.M000887200;
RA   Courilleau D., Chastre E., Sabbah M., Redeuilh G., Atfi A., Mester J.;
RT   "B-ind1, a novel mediator of Rac1 signaling cloned from sodium
RT   butyrate-treated fibroblasts.";
RL   J. Biol. Chem. 275:17344-17348(2000).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Responsible for the dehydration step in very long-chain
CC       fatty acids (VLCFAs) synthesis. Involved in Rac1-signaling
CC       pathways leading to the modulation of gene expression.
CC   -!- SUBUNIT: Interact with the condensation enzymes of the ELOVL
CC       family. Interacts with RAC1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the very long-chain fatty acids dehydratase
CC       HACD family.
CC   -!- SIMILARITY: Contains 1 CS domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK051735; BAC34744.1; -; mRNA.
DR   EMBL; AK052865; BAC35179.1; -; mRNA.
DR   EMBL; AK050556; BAE20677.1; -; mRNA.
DR   EMBL; AK159494; BAE35128.1; -; mRNA.
DR   EMBL; BC031755; AAH31755.1; -; mRNA.
DR   EMBL; BC057023; AAH57023.1; -; mRNA.
DR   EMBL; Z97207; CAB10097.2; -; mRNA.
DR   IPI; IPI00322145; -.
DR   RefSeq; NP_067320.2; NM_021345.2.
DR   UniGene; Mm.480367; -.
DR   ProteinModelPortal; Q8K2C9; -.
DR   SMR; Q8K2C9; 12-120.
DR   STRING; Q8K2C9; -.
DR   PhosphoSite; Q8K2C9; -.
DR   PRIDE; Q8K2C9; -.
DR   Ensembl; ENSMUST00000036615; ENSMUSP00000044955; ENSMUSG00000033629.
DR   GeneID; 57874; -.
DR   KEGG; mmu:57874; -.
DR   CTD; 57874; -.
DR   MGI; MGI:1889341; Ptplad1.
DR   eggNOG; roNOG10549; -.
DR   GeneTree; ENSGT00530000062962; -.
DR   HOGENOM; HBG444752; -.
DR   HOVERGEN; HBG108301; -.
DR   InParanoid; Q8K2C9; -.
DR   OMA; HFKAQGH; -.
DR   OrthoDB; EOG4JHCG0; -.
DR   PhylomeDB; Q8K2C9; -.
DR   NextBio; 314029; -.
DR   ArrayExpress; Q8K2C9; -.
DR   Bgee; Q8K2C9; -.
DR   Genevestigator; Q8K2C9; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0007249; P:I-kappaB kinase/NF-kappaB cascade; IDA:MGI.
DR   GO; GO:0007254; P:JNK cascade; IDA:MGI.
DR   GO; GO:0007266; P:Rho protein signal transduction; IDA:MGI.
DR   InterPro; IPR007052; CS-like_domain.
DR   InterPro; IPR017447; CS_domain.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   InterPro; IPR007482; Tyr_Pase-like_PTPLA.
DR   PANTHER; PTHR11035; PTPLA; 1.
DR   Pfam; PF04969; CS; 1.
DR   Pfam; PF04387; PTPLA; 1.
DR   SUPFAM; SSF49764; HSP20_chap; 1.
DR   PROSITE; PS51203; CS; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Endoplasmic reticulum; Fatty acid biosynthesis;
KW   Lipid synthesis; Lyase; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    362       3-hydroxyacyl-CoA dehydratase 3.
FT                                /FTId=PRO_0000313725.
FT   TOPO_DOM      1    149       Cytoplasmic (Potential).
FT   TRANSMEM    150    170       Helical; (Potential).
FT   TOPO_DOM    171    189       Lumenal (Potential).
FT   TRANSMEM    190    210       Helical; (Potential).
FT   TOPO_DOM    211    212       Cytoplasmic (Potential).
FT   TRANSMEM    213    233       Helical; (Potential).
FT   TOPO_DOM    234    242       Lumenal (Potential).
FT   TRANSMEM    243    263       Helical; (Potential).
FT   TOPO_DOM    264    280       Cytoplasmic (Potential).
FT   TRANSMEM    281    301       Helical; (Potential).
FT   TOPO_DOM    302    322       Lumenal (Potential).
FT   TRANSMEM    323    343       Helical; (Potential).
FT   TOPO_DOM    344    362       Cytoplasmic (Potential).
FT   DOMAIN        5     94       CS.
FT   COILED      111    138       Potential.
FT   COMPBIAS    350    353       Poly-Arg.
FT   COMPBIAS    357    360       Poly-Lys.
FT   ACT_SITE    286    286       By similarity.
FT   ACT_SITE    293    293       By similarity.
FT   MOD_RES     114    114       Phosphoserine.
FT   CONFLICT     32     32       A -> P (in Ref. 2; AAH57023).
FT   CONFLICT     63     63       D -> E (in Ref. 2; AAH31755).
FT   CONFLICT    146    146       K -> R (in Ref. 3; CAB10097).
SQ   SEQUENCE   362 AA;  43131 MW;  85716941EF7008F6 CRC64;
     METQVLTPHV YWAQRHRELY LRVELSDVQN PAISITDNVL HFKAQGHGAK GDNVYEFHLE
     FLDLVKPEPA YRLTQRQVNI TVQKKGSHWW ERLTKQEKRP LFLAPDFDRW LDESDAEMEL
     RAKEEERLNK LRLEREGSPE TLTNLKKGYL FMYNLVQLLG FSWIFVNLTV RFFILGKESF
     YDTFHNVADM MYFCQMLALV ETLNAAIGVT STPVLPALIQ FLGRNFILFL VFGTMEEMQN
     KAVVFFVFYS WSAIEIFRYP FYMLSCIDMD WKVLTWLRYT MWIPLYPLGC LSEAVAVIQS
     IPVFNESGRF SFTLPYPVKM KVRFSFFLQV YLVMLFLGLY INFRHLYKQR RRRYGQKKKK
     LH
//
ID   EDC3_MOUSE              Reviewed;         508 AA.
AC   Q8K2D3; Q3THV7;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Enhancer of mRNA-decapping protein 3;
DE   AltName: Full=YjeF domain-containing protein 1;
GN   Name=Edc3; Synonyms=Yjdc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2; TISSUE=Mammary gland, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: In the process of mRNA degradation, may play a role in
CC       mRNA decapping.
CC   -!- SUBUNIT: Forms a complex with DCP1A, DCP2, DDX6 and EDC4/HEDLS,
CC       within this complex directly interacts with DCP1A and DDX6.
CC       Interacts with ZFP36 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body (By similarity).
CC       Note=Processing bodies (PB) (By similarity).
CC   -!- SIMILARITY: Belongs to the EDC3 family.
CC   -!- SIMILARITY: Contains 1 YjeF N-terminal domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK146804; BAE27445.1; -; mRNA.
DR   EMBL; AK166286; BAE38683.1; -; mRNA.
DR   EMBL; AK168118; BAE40089.1; -; mRNA.
DR   EMBL; BC031725; AAH31725.1; -; mRNA.
DR   EMBL; BC033484; AAH33484.1; -; mRNA.
DR   IPI; IPI00169888; -.
DR   RefSeq; NP_722494.1; NM_153799.3.
DR   UniGene; Mm.268104; -.
DR   ProteinModelPortal; Q8K2D3; -.
DR   SMR; Q8K2D3; 4-74, 197-226, 258-507.
DR   STRING; Q8K2D3; -.
DR   PhosphoSite; Q8K2D3; -.
DR   PRIDE; Q8K2D3; -.
DR   Ensembl; ENSMUST00000043990; ENSMUSP00000049146; ENSMUSG00000038957.
DR   GeneID; 353190; -.
DR   KEGG; mmu:353190; -.
DR   UCSC; uc009pvp.1; mouse.
DR   CTD; 353190; -.
DR   MGI; MGI:2142951; Edc3.
DR   GeneTree; ENSGT00390000016435; -.
DR   HOGENOM; HBG713540; -.
DR   HOVERGEN; HBG079428; -.
DR   InParanoid; Q8K2D3; -.
DR   OMA; GFRRRHN; -.
DR   OrthoDB; EOG4W0XCZ; -.
DR   PhylomeDB; Q8K2D3; -.
DR   NextBio; 400339; -.
DR   ArrayExpress; Q8K2D3; -.
DR   Bgee; Q8K2D3; -.
DR   Genevestigator; Q8K2D3; -.
DR   GermOnline; ENSMUSG00000038957; Mus musculus.
DR   GO; GO:0000932; C:cytoplasmic mRNA processing body; IEA:UniProtKB-SubCell.
DR   InterPro; IPR019050; DFDF_motif.
DR   InterPro; IPR021024; Enhancer_mRNA-decap_3_N.
DR   InterPro; IPR004443; YjeF_N.
DR   Gene3D; G3DSA:3.40.50.10260; G3DSA:3.40.50.10260; 1.
DR   Pfam; PF09532; DFDF; 1.
DR   Pfam; PF11562; EDC3_LSm; 1.
DR   Pfam; PF03853; YjeF_N; 1.
DR   SUPFAM; SSF64153; YjeF_N; 1.
DR   PROSITE; PS51385; YJEF_N; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Phosphoprotein.
FT   CHAIN         1    508       Enhancer of mRNA-decapping protein 3.
FT                                /FTId=PRO_0000119056.
FT   DOMAIN      283    487       YjeF N-terminal.
FT   REGION        1     79       Required for P-body targeting and
FT                                interaction with DCP1A (By similarity).
FT   REGION      191    296       Required for interaction with DDX6 (By
FT                                similarity).
FT   MOD_RES     131    131       Phosphoserine (By similarity).
FT   MOD_RES     161    161       Phosphoserine (By similarity).
FT   CONFLICT    237    237       P -> T (in Ref. 1; BAE40089).
FT   CONFLICT    333    333       Q -> R (in Ref. 1; BAE40089).
SQ   SEQUENCE   508 AA;  55957 MW;  DD1F449BEF1341C8 CRC64;
     MAMDWLGSIV SINCGDSLGV YQGRVSAVDQ VSQTISLTRP FHNGVKCLVP EVTFRAGDIT
     ELKILEIPGP GDNQQVGDLH QTELGPSGVG YQMSISQNGT GKVVKKPASS SSAPQSIPKR
     TDVKSQDVAI SPQQQQCSKS YVDRHMESLS QSKSFRRRHN SWSSSSRHPN QATPKKSGLK
     NGQMKNKDDE CFGDDIEELP DTDFDFEGNL ALFDKAAVFE EIDTYERRSG SRSRGVPNER
     PARYRHDENI LESEPIVYRR ITVPHSVSKE FCTDSGLVVP SVSYELHKKL LSVAEKHGLT
     LERRLEMTGV CASQMALTLL GGPNRLNPKN VHQRPTVALL CGPHVKGAQG ISCGRHLANH
     DVQVILFLPN FVKMLESITN ELSLFSKTQG QQVSSLRDLP ASPVDLVINC LDCPENAFLR
     DQPWYKAAVA WANQNRAPVL SIDPPVHEVE QGIDAKWSLA LGLPLPLGEH AGRVYLCDIG
     IPQQVFQEVG INYHSPFGCK FVIPLHSA
//
ID   BRD3_MOUSE              Reviewed;         726 AA.
AC   Q8K2F0; Q8C665; Q8CAX7; Q9JI25;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Bromodomain-containing protein 3;
DE   AltName: Full=Bromodomain-containing FSH-like protein FSRG2;
GN   Name=Brd3; Synonyms=Fsrg2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RA   Shang E., Wolgemuth D.J.;
RT   "Cloning and expression pattern of Fsrg2, a putative murine
RT   bromodomain-containing homolog of the Drosophila gene female sterile
RT   homeotic.";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-494 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K2F0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K2F0-2; Sequence=VSP_010249;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 2 bromo domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF269193; AAF78072.1; -; mRNA.
DR   EMBL; BC031536; AAH31536.1; -; mRNA.
DR   EMBL; AK037435; BAC29806.1; -; mRNA.
DR   EMBL; AK076472; BAC36359.1; -; mRNA.
DR   IPI; IPI00410791; -.
DR   IPI; IPI00410792; -.
DR   RefSeq; NP_001107045.1; NM_001113573.1.
DR   RefSeq; NP_001107046.1; NM_001113574.1.
DR   RefSeq; NP_075825.3; NM_023336.4.
DR   UniGene; Mm.28721; -.
DR   ProteinModelPortal; Q8K2F0; -.
DR   SMR; Q8K2F0; 24-154, 306-415, 572-645.
DR   STRING; Q8K2F0; -.
DR   PhosphoSite; Q8K2F0; -.
DR   PRIDE; Q8K2F0; -.
DR   Ensembl; ENSMUST00000028282; ENSMUSP00000028282; ENSMUSG00000026918.
DR   Ensembl; ENSMUST00000077737; ENSMUSP00000076918; ENSMUSG00000026918.
DR   Ensembl; ENSMUST00000113941; ENSMUSP00000109574; ENSMUSG00000026918.
DR   GeneID; 67382; -.
DR   KEGG; mmu:67382; -.
DR   UCSC; uc008ixl.1; mouse.
DR   UCSC; uc008ixn.1; mouse.
DR   CTD; 67382; -.
DR   MGI; MGI:1914632; Brd3.
DR   GeneTree; ENSGT00550000074306; -.
DR   HOVERGEN; HBG004896; -.
DR   OMA; KMPDEPA; -.
DR   NextBio; 324408; -.
DR   ArrayExpress; Q8K2F0; -.
DR   Bgee; Q8K2F0; -.
DR   CleanEx; MM_BRD3; -.
DR   Genevestigator; Q8K2F0; -.
DR   GermOnline; ENSMUSG00000026918; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   Gene3D; G3DSA:1.20.920.10; Bromodomain; 2.
DR   Pfam; PF00439; Bromodomain; 2.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 2.
DR   SUPFAM; SSF47370; Bromodomain; 2.
DR   PROSITE; PS00633; BROMODOMAIN_1; 2.
DR   PROSITE; PS50014; BROMODOMAIN_2; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Bromodomain; Coiled coil; Nucleus;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1    726       Bromodomain-containing protein 3.
FT                                /FTId=PRO_0000211182.
FT   DOMAIN       50    122       Bromo 1.
FT   DOMAIN      325    397       Bromo 2.
FT   COILED      452    482       Potential.
FT   COILED      646    689       Potential.
FT   COMPBIAS    178    234       Pro-rich.
FT   COMPBIAS    486    556       Lys-rich.
FT   COMPBIAS    565    569       Poly-Glu.
FT   COMPBIAS    691    725       Ser-rich.
FT   MOD_RES     258    258       Phosphoserine (By similarity).
FT   MOD_RES     262    262       Phosphoserine.
FT   MOD_RES     280    280       Phosphoserine (By similarity).
FT   MOD_RES     564    564       Phosphoserine (By similarity).
FT   MOD_RES     682    682       Phosphoserine (By similarity).
FT   VAR_SEQ     468    468       Q -> QTGCGAFQDQLLNVSSVQ (in isoform 2).
FT                                /FTId=VSP_010249.
FT   CONFLICT    174    174       S -> F (in Ref. 3; BAC36359).
FT   CONFLICT    216    216       A -> T (in Ref. 2; AAH31536).
FT   CONFLICT    477    477       A -> D (in Ref. 1; AAF78072).
FT   CONFLICT    659    660       EE -> VV (in Ref. 1; AAF78072).
SQ   SEQUENCE   726 AA;  79762 MW;  D5B2FC0ACA41D8ED CRC64;
     MSTTAAAPTG IPAVPGPVNP PPPEVSNPSK PGRKTNQLQY MQNVVVKTLW KHQFAWPFYQ
     PVDAIKLNLP DYHKIIKNPM DMGTIKKRLE NNYYWSASEC MQDFNTMFTN CYIYNKPTDD
     IVLMAQALEK IFLQKVAQMP QEEVELLPPA PKGKGRKPAA GAQNAGSQQV AAVSSVSPAT
     PFQNIPPTVS QTPVIAATPV PTITANVTSV PVPPPAAPPP PATPIVPVVP PTPPVVKKKG
     VKRKADTTTP TTSAITASRS ESPPPLSEPK QAKVVARRES GGRPIKPPKK DLEDGEVPQH
     AGKKGKLSEH LRHCDSILRE MLSKKHAAYA WPFYKPVDAE ALELHDYHDI IKHPMDLSTV
     KRKMDSREYP DAQGFAADIR LMFSNCYKYN PPDHEVVAMA RKLQDVFEMR FAKMPDEPME
     APALPAPTAP IVSKGAESSR SSEESSSDSG SSDSEEERAT RLAELQEQLK AVHEQLAALS
     QAPVNKPKKK KEKKEKEKKK KDKDKDKEKE KHKAKSEEEK KAKAAPAAKQ AQQKKAPTKK
     ANSTTTASRQ LKKGGKQASA SYDSEEEEEG LPMSYDEKRQ LSLDINRLPG EKLGRVVHII
     QSREPSLRDS NPDEIEIDFE TLKPTTLREL ERYVKSCLQK KQRKPLSTSG KKQAAKSKEE
     LAQEKKKELE KRLQDVSGQL NSKKPTKKEK SGSAPSGGPS RLSSSSSSES ASSSSSGSSS
     DSSDSE
//
ID   LS14A_MOUSE             Reviewed;         462 AA.
AC   Q8K2F8; Q9CTG8;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Protein LSM14 homolog A;
DE   AltName: Full=Protein FAM61A;
DE   AltName: Full=RNA-associated protein 55A;
DE            Short=mRAP55A;
GN   Name=Lsm14a; Synonyms=Fam61a, Rap55a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-462.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [6]
RP   REVIEW.
RX   PubMed=18723115; DOI=10.1016/j.biocel.2008.06.015;
RA   Marnef A., Sommerville J., Ladomery M.R.;
RT   "RAP55: insights into an evolutionarily conserved protein family.";
RL   Int. J. Biochem. Cell Biol. 41:977-981(2009).
CC   -!- FUNCTION: Essential for formation of P-bodies, cytoplasmic
CC       structures that provide storage sites for non-translating mRNAs
CC       (By similarity).
CC   -!- SUBUNIT: Component of a ribonucleoprotein (RNP) complex (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm, P-body
CC       (By similarity). Note=Targeted to stress granules (SGs) in
CC       response to cellular stress (By similarity).
CC   -!- DOMAIN: The LSM14 domain and the RGG repeats are required for
CC       accumulation in P-bodies, and the region containing the FDF motif
CC       is responsible for cytoplasmic retention (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the LSM14 family.
CC   -!- SIMILARITY: Contains 1 FFD-TFG box domain.
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DR   EMBL; BC031521; AAH31521.1; -; mRNA.
DR   EMBL; AK003611; BAB22889.1; -; mRNA.
DR   IPI; IPI00172202; -.
DR   RefSeq; NP_080224.1; NM_025948.2.
DR   UniGene; Mm.276503; -.
DR   ProteinModelPortal; Q8K2F8; -.
DR   SMR; Q8K2F8; 2-83.
DR   STRING; Q8K2F8; -.
DR   PhosphoSite; Q8K2F8; -.
DR   PRIDE; Q8K2F8; -.
DR   Ensembl; ENSMUST00000085585; ENSMUSP00000082723; ENSMUSG00000066568.
DR   GeneID; 67070; -.
DR   KEGG; mmu:67070; -.
DR   NMPDR; fig|10090.3.peg.16225; -.
DR   UCSC; uc009gjd.1; mouse.
DR   CTD; 67070; -.
DR   MGI; MGI:1914320; Lsm14a.
DR   GeneTree; ENSGT00390000004174; -.
DR   HOGENOM; HBG445488; -.
DR   HOVERGEN; HBG054326; -.
DR   InParanoid; Q8K2F8; -.
DR   OMA; DNRERRP; -.
DR   OrthoDB; EOG4NCMD3; -.
DR   PhylomeDB; Q8K2F8; -.
DR   NextBio; 323480; -.
DR   ArrayExpress; Q8K2F8; -.
DR   Bgee; Q8K2F8; -.
DR   CleanEx; MM_LSM14A; -.
DR   Genevestigator; Q8K2F8; -.
DR   GermOnline; ENSMUSG00000066568; Mus musculus.
DR   GO; GO:0000932; C:cytoplasmic mRNA processing body; ISS:UniProtKB.
DR   GO; GO:0010494; C:stress granule; ISS:UniProtKB.
DR   GO; GO:0033962; P:cytoplasmic mRNA processing body assembly; ISS:UniProtKB.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   InterPro; IPR019050; DFDF_motif.
DR   InterPro; IPR019053; FFD/TFG_box_motif.
DR   InterPro; IPR010920; LSM-related_domain.
DR   Pfam; PF09532; DFDF; 1.
DR   Pfam; PF09542; FFD_TFG; 1.
DR   SUPFAM; SSF50182; Sm_like_riboprot; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Developmental protein; Phosphoprotein;
KW   Repressor; Ribonucleoprotein; Translation regulation.
FT   CHAIN         1    462       Protein LSM14 homolog A.
FT                                /FTId=PRO_0000187091.
FT   DOMAIN      360    396       FFD-TFG box.
FT   MOTIF       295    297       FDF.
FT   MOD_RES       2      2       Phosphoserine (By similarity).
FT   MOD_RES       7      7       Phosphotyrosine (By similarity).
FT   MOD_RES     182    182       Phosphoserine (By similarity).
FT   MOD_RES     183    183       Phosphoserine.
FT   MOD_RES     192    192       Phosphoserine (By similarity).
FT   MOD_RES     194    194       Phosphothreonine (By similarity).
FT   MOD_RES     201    201       Phosphothreonine (By similarity).
FT   MOD_RES     203    203       Phosphoserine (By similarity).
FT   MOD_RES     216    216       Phosphoserine.
FT   MOD_RES     227    227       Phosphoserine (By similarity).
FT   MOD_RES     290    290       N6-acetyllysine (By similarity).
SQ   SEQUENCE   462 AA;  50546 MW;  B2554A73B96C473B CRC64;
     MSGGTPYIGS KISLISKAEI RYEGILYTID TENSTVALAK VRSFGTEDRP TDRPIPPRDE
     VFEYIIFRGS DIKDLTVCEP PKPQCSLPQD PAIVQSSLGS SSSSFQSVGS YGPFGRMPAY
     SQFSPSTLVG QQFGAVGVAG NSLTSFGTEA SNSGTLSQSN AVGSAFTQDT RSVKPQLAQG
     RSSPQLDPLR KSPTMEQAVQ TASAHLPAPA PVGRRSPVPA RPLPPTSQKA IDNQEHRRAE
     VHKVPRPENE QLRNDKRQVV PGVPSAPRRG RGGHRGGRGR FGIRRDGPMK FEKDFDFESA
     NAQFNKEEID REFHNKLKLK EDKLEKQEKP VNGEDKGDSG VDTQNSEGNA DEEDPLGPNC
     YYDKTKSFFD NISCDDNRER RPTWAEERRL NAETFGIPLR PNRGRGGYRG RGGLGFRGGR
     GRGSGRGGTF TAPRGFRAGF RGARGGREFA DFEYRKTTAF GP
//
ID   Q8K2H5_MOUSE            Unreviewed;       775 AA.
AC   Q8K2H5;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   08-FEB-2011, entry version 39.
DE   SubName: Full=Melanoma antigen, family D, 1;
GN   Name=Maged1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II;
RC   TISSUE=Mammary tumor metastatized to lung. Tumor arose spontaneously;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC031461; AAH31461.1; -; mRNA.
DR   IPI; IPI00136178; -.
DR   UniGene; Mm.27578; -.
DR   STRING; Q8K2H5; -.
DR   Ensembl; ENSMUST00000026142; ENSMUSP00000026142; ENSMUSG00000025151.
DR   MGI; MGI:1930187; Maged1.
DR   HOVERGEN; HBG003714; -.
DR   InParanoid; Q8K2H5; -.
DR   ArrayExpress; Q8K2H5; -.
DR   Bgee; Q8K2H5; -.
DR   Genevestigator; Q8K2H5; -.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   InterPro; IPR002190; MAGE.
DR   PANTHER; PTHR11736; MAGE; 1.
DR   Pfam; PF01454; MAGE; 1.
DR   PROSITE; PS50838; MAGE; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   775 AA;  85692 MW;  3E433816CAF74F14 CRC64;
     MAQKPDGGAG LRGFQAEASV EDSALLVQTL MEAIQISEAP PTSQATAAAS GPNASPQSSQ
     PPTANEKADT EVSAAAARPK TGFKAQNATT KGPNDYSQAR NAKEMPKNQS KAAFKSQNGT
     PKGSHAASDF SQAAPTGKSA KKSEMAFKGQ NSTKAGPGTT YNFPQSPSAN EMTNNQPKTA
     KAWNDTTKVP GADAQTQNVN QAKMADVGTS AGISEADGAA AQTSADGSQT QNMESRTIIR
     GKRTRKVNNL NVEENNSGDQ RRASLASGNW RSAPVPVTTQ QNPPGAPPNV VWQTPLAWQN
     PSGWQNQTAR QTPPAARQSP PARQTPSAWQ NPVAWQNPVI WPNPVIWQNP VIWPNPIVWP
     GPIVWPNPMA WQSTPGWQSP PSWQAPPSWQ SPQDWQGPPD WQVPPDWSMP PDWSFPSDWP
     FPPDWIPADW PIPPDWQNLR PSPNLRSSSN SRASQNQGPP QPRDVALLQE RANKLVKYLM
     LKDYTKVPIK RSEMLRDIIR EYTDVYPEII ERACFVLEKK FGIQLKEIDK EEHLYILIST
     PESLAGILGT TKDTPKLGLL LVILGIIFMN GNRATEAVLW EALRKMGLRP GVRHPLLGDL
     RKLLTYEFVK QKYLDYRRVP NSNPPEYEFL WGLRSYHETS KMKVLRFIAE VQKRDPRDWT
     AQFMEAADEA LDALDAAAAE AEARAEARNR MGIGDEAVSG PWSWDDIEFE LLTWDEEGDF
     GDPWSRIPFT FWARYHQNAR SRFPQAFTGP IIGPSGTATA NFAANFGAIG FFWVE
//
ID   FNTB_MOUSE              Reviewed;         437 AA.
AC   Q8K2I1;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Protein farnesyltransferase subunit beta;
DE            Short=FTase-beta;
DE            EC=2.5.1.58;
DE   AltName: Full=CAAX farnesyltransferase subunit beta;
DE   AltName: Full=Ras proteins prenyltransferase subunit beta;
GN   Name=Fntb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Catalyzes the transfer of a farnesyl moiety from
CC       farnesyl pyrophosphate to a cysteine at the fourth position from
CC       the C-terminus of several proteins. The beta subunit is
CC       responsible for peptide-binding (By similarity).
CC   -!- CATALYTIC ACTIVITY: Farnesyl diphosphate + protein-cysteine = S-
CC       farnesyl protein + diphosphate.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta
CC       family.
CC   -!- SIMILARITY: Contains 5 PFTB repeats.
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DR   EMBL; BC031417; AAH31417.1; -; mRNA.
DR   IPI; IPI00169914; -.
DR   RefSeq; NP_666039.1; NM_145927.2.
DR   UniGene; Mm.151174; -.
DR   ProteinModelPortal; Q8K2I1; -.
DR   SMR; Q8K2I1; 17-423.
DR   STRING; Q8K2I1; -.
DR   PhosphoSite; Q8K2I1; -.
DR   PRIDE; Q8K2I1; -.
DR   Ensembl; ENSMUST00000041008; ENSMUSP00000035498; ENSMUSG00000033373.
DR   GeneID; 110606; -.
DR   KEGG; mmu:110606; -.
DR   UCSC; uc007nyu.1; mouse.
DR   CTD; 110606; -.
DR   MGI; MGI:1861305; Fntb.
DR   eggNOG; roNOG14622; -.
DR   GeneTree; ENSGT00550000075042; -.
DR   HOGENOM; HBG736019; -.
DR   HOVERGEN; HBG008173; -.
DR   InParanoid; Q8K2I1; -.
DR   OMA; QEYILLC; -.
DR   OrthoDB; EOG4KKZ33; -.
DR   PhylomeDB; Q8K2I1; -.
DR   BRENDA; 2.5.1.58; 244.
DR   NextBio; 364317; -.
DR   ArrayExpress; Q8K2I1; -.
DR   Bgee; Q8K2I1; -.
DR   CleanEx; MM_FNTB; -.
DR   Genevestigator; Q8K2I1; -.
DR   GermOnline; ENSMUSG00000033373; Mus musculus.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004660; F:protein farnesyltransferase activity; IEA:EC.
DR   InterPro; IPR001330; Prenyltrans.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   Pfam; PF00432; Prenyltrans; 5.
DR   SUPFAM; SSF48239; Terp_cyc_toroid; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Phosphoprotein; Prenyltransferase; Repeat; Transferase;
KW   Zinc.
FT   CHAIN         1    437       Protein farnesyltransferase subunit beta.
FT                                /FTId=PRO_0000119762.
FT   REPEAT      123    164       PFTB 1.
FT   REPEAT      174    215       PFTB 2.
FT   REPEAT      222    263       PFTB 3.
FT   REPEAT      270    312       PFTB 4.
FT   REPEAT      332    374       PFTB 5.
FT   METAL       297    297       Zinc (By similarity).
FT   METAL       299    299       Zinc (By similarity).
FT   METAL       362    362       Zinc (By similarity).
FT   MOD_RES     300    300       Phosphotyrosine (By similarity).
SQ   SEQUENCE   437 AA;  48820 MW;  42B780B356136950 CRC64;
     MASSSSFTYY CPPSSSPVWS EPLYSLRPEH VRERLQDDSV ETVTSIEQAK VEEKIQEVFS
     SYKFNHLVPR LILQREKHFH YLKRGLRQLT DAYECLDASR PWLCYWILHS LELLDEPIPQ
     IVATDVCQFL ELCQSPDGGF GGGPGQYPHL APTYAAVNAL CIIGTEEAYN VINREKLLQY
     LYSLKQPDGS FLMHVGGEVD VRSAYCAASV ASLTNIITPD LFEGTAEWIA RCQNWEGGIG
     GVPGMEAHGG YTFCGLAALV ILKKERSLNL KSLLQWVTSR QMRFEGGFQG RCNKLVDGCY
     SFWQAGLLPL LHRALHAQGD PALSMSHWMF HQQALQEYIL MCCQCPAGGL LDKPGKSRDF
     YHTCYCLSGL SIAQHFGSGA MLHDMVMGVP ENVLQPTHPV YNIGPEKVIQ ATTHFLQKPV
     PGFEECEDEV TSDPATD
//
ID   PLCD3_MOUSE             Reviewed;         785 AA.
AC   Q8K2J0; A2AHR0; A2AHR1; Q3UME8; Q69Z55; Q8BL19;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 2.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3;
DE            EC=3.1.4.11;
DE   AltName: Full=Phosphoinositide phospholipase C-delta-3;
DE   AltName: Full=Phospholipase C-delta-3;
DE            Short=PLC-delta-3;
GN   Name=Plcd3; Synonyms=Kiaa1964;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic intestine;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16314520; DOI=10.1128/MCB.25.24.10979-10988.2005;
RA   Nakamura Y., Hamada Y., Fujiwara T., Enomoto H., Hiroe T., Tanaka S.,
RA   Nose M., Nakahara M., Yoshida N., Takenawa T., Fukami K.;
RT   "Phospholipase C-delta1 and -delta3 are essential in the trophoblast
RT   for placental development.";
RL   Mol. Cell. Biol. 25:10979-10988(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-492, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Hydrolyzes the phosphatidylinositol 4,5-bisphosphate
CC       (PIP2) to generate 2 second messenger molecules diacylglycerol
CC       (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the
CC       activation of protein kinase C (PKC), while IP3 releases Ca(2+)
CC       from intracellular stores. Essential for trophoblast and placental
CC       development. May participate in cytokinesis by hydrolyzing PIP2 at
CC       the cleavage furrow.
CC   -!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-
CC       bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate +
CC       diacylglycerol.
CC   -!- COFACTOR: Binds 3 calcium ions per subunit. Two of the calcium
CC       ions are bound to the C2 domain (By similarity).
CC   -!- ENZYME REGULATION: Strongly activated by phosphatidic acid.
CC       Inhibited by phosphatidylethanolamine (PtdEtn),
CC       phosphatidylcholine (PtdCho), sphingomyelin and phosphatidylserine
CC       (PtdSer) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC       similarity). Cytoplasm (By similarity). Cleavage furrow.
CC       Note=Localizes at the cleavage furrow during cytokinesis.
CC   -!- DOMAIN: The C2 domain is a Ca(2+)-dependent membrane-targeting
CC       module (By similarity).
CC   -!- DOMAIN: The PH domain mediates interaction with the surface
CC       membrane by binding to PIP2 (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice lacking Plcd1 and Plcd3 die at
CC       embryonic day 11.5 (E11.5) to E13.5 and exhibit severe disruption
CC       of the normal labyrinth architecture in the placenta and decreased
CC       placental vascularization, as well as abnormal proliferation and
CC       apoptosis of trophoblasts in the labyrinth area. Furthermore,
CC       Plcd1 and Plcd3 double-knockout embryos supplied with a normal
CC       placenta by the tetraploid aggregation method survive beyond
CC       E14.5, clearly indicating that the embryonic lethality is caused
CC       by a defect in trophoblasts.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 3 EF-hand domains.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 PI-PLC X-box domain.
CC   -!- SIMILARITY: Contains 1 PI-PLC Y-box domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC32829.1; Type=Erroneous initiation;
CC       Sequence=BAD32589.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC       Sequence=CAM22088.1; Type=Erroneous gene model prediction;
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DR   EMBL; AK173311; BAD32589.1; ALT_SEQ; Transcribed_RNA.
DR   EMBL; AK046669; BAC32829.1; ALT_INIT; mRNA.
DR   EMBL; AK144950; BAE26150.1; -; mRNA.
DR   EMBL; AL731805; CAM22088.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL731805; CAM22089.1; -; Genomic_DNA.
DR   EMBL; BC031392; AAH31392.1; -; mRNA.
DR   IPI; IPI00331040; -.
DR   RefSeq; NP_690026.2; NM_152813.3.
DR   UniGene; Mm.264743; -.
DR   HSSP; P10688; 1DJX.
DR   ProteinModelPortal; Q8K2J0; -.
DR   SMR; Q8K2J0; 51-785.
DR   STRING; Q8K2J0; -.
DR   PhosphoSite; Q8K2J0; -.
DR   PRIDE; Q8K2J0; -.
DR   Ensembl; ENSMUST00000021320; ENSMUSP00000021320; ENSMUSG00000020937.
DR   Ensembl; ENSMUST00000103077; ENSMUSP00000099366; ENSMUSG00000020937.
DR   GeneID; 72469; -.
DR   KEGG; mmu:72469; -.
DR   CTD; 72469; -.
DR   MGI; MGI:107451; Plcd3.
DR   eggNOG; maNOG13913; -.
DR   GeneTree; ENSGT00570000078720; -.
DR   HOGENOM; HBG527074; -.
DR   HOVERGEN; HBG053610; -.
DR   InParanoid; Q8K2J0; -.
DR   OMA; KECDHSN; -.
DR   OrthoDB; EOG45QHCM; -.
DR   BRENDA; 3.1.4.11; 244.
DR   NextBio; 336294; -.
DR   ArrayExpress; Q8K2J0; -.
DR   Bgee; Q8K2J0; -.
DR   CleanEx; MM_PLCD3; -.
DR   Genevestigator; Q8K2J0; -.
DR   GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:EC.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0001525; P:angiogenesis; IGI:MGI.
DR   GO; GO:0060716; P:labyrinthine layer blood vessel development; IGI:MGI.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0042127; P:regulation of cell proliferation; IGI:MGI.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR015359; Phospholipase_C_EF-hand-like.
DR   InterPro; IPR001711; Phospholipase_C_Pinositol-sp_Y.
DR   InterPro; IPR001192; Pinositol_Phospholipase-C.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:3.20.20.190; PLC-like_Pdiesterase_TIM-brl; 2.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF09279; efhand_like; 1.
DR   Pfam; PF00388; PI-PLC-X; 1.
DR   Pfam; PF00387; PI-PLC-Y; 1.
DR   PRINTS; PR00390; PHPHLIPASEC.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00148; PLCXc; 1.
DR   SMART; SM00149; PLCYc; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF51695; PLC-like_Pdiesterase_TIM-brl; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00018; EF_HAND_1; FALSE_NEG.
DR   PROSITE; PS50222; EF_HAND_2; FALSE_NEG.
DR   PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cytoplasm; Hydrolase; Lipid degradation; Membrane;
KW   Metal-binding; Phosphoprotein; Repeat; Transducer.
FT   CHAIN         1    785       1-phosphatidylinositol-4,5-bisphosphate
FT                                phosphodiesterase delta-3.
FT                                /FTId=PRO_0000306822.
FT   DOMAIN       65    168       PH.
FT   DOMAIN      178    213       EF-hand 1.
FT   DOMAIN      214    249       EF-hand 2.
FT   DOMAIN      246    281       EF-hand 3.
FT   DOMAIN      333    478       PI-PLC X-box.
FT   DOMAIN      524    640       PI-PLC Y-box.
FT   DOMAIN      643    748       C2.
FT   CA_BIND     191    202       1 (Potential).
FT   CA_BIND     227    238       2 (Potential).
FT   REGION       69     97       Substrate binding (By similarity).
FT   ACT_SITE    348    348       By similarity.
FT   ACT_SITE    393    393       By similarity.
FT   METAL       349    349       Calcium 1; catalytic (By similarity).
FT   METAL       378    378       Calcium 1; catalytic (By similarity).
FT   METAL       380    380       Calcium 1; catalytic (By similarity).
FT   METAL       427    427       Calcium 1; catalytic (By similarity).
FT   METAL       679    679       Calcium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       681    681       Calcium 2 (By similarity).
FT   METAL       705    705       Calcium 2 (By similarity).
FT   METAL       734    734       Calcium 3 (By similarity).
FT   METAL       735    735       Calcium 3; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       736    736       Calcium 3 (By similarity).
FT   BINDING     476    476       Substrate (By similarity).
FT   BINDING     478    478       Substrate (By similarity).
FT   BINDING     553    553       Substrate (By similarity).
FT   BINDING     580    580       Substrate (By similarity).
FT   MOD_RES     101    101       Phosphoserine (By similarity).
FT   MOD_RES     492    492       Phosphoserine.
FT   CONFLICT    199    199       S -> N (in Ref. 2; BAE26150).
FT   CONFLICT    301    302       AK -> GE (in Ref. 1; BAD32589).
FT   CONFLICT    378    378       E -> K (in Ref. 2; BAE26150).
FT   CONFLICT    540    540       D -> E (in Ref. 4; AAH31392).
FT   CONFLICT    659    659       A -> T (in Ref. 2; BAE26150).
FT   CONFLICT    660    660       I -> V (in Ref. 2; BAE26150).
SQ   SEQUENCE   785 AA;  88607 MW;  8B3DE84FB7A52238 CRC64;
     MLCGGWKRSR RSPEESRVSA QVAAPLAFPP SPASSDSSTK RPGLRALKKM GLTEDEDVQA
     MLRGSRLLKI RSRTWHKERL YRLQEDGLSV WFQRRIPRAA SKHIFFVQHI EAVREGHQSE
     GLRRFGGAFA PACCLTIAFK GRRKNLDLAA PTAEEAQRWV RGLAKLRARL DAMSQRERLD
     HWIHSYLHRA DSDQDSKMSF KEIKSLLRMV NVDMNDMYAY RLFKECDHSN NERLEGAEIE
     AFLRRLLKRP ELEEIFRRYS GEDRVLSASE LLEFLEDQGE DGATLACAQQ LIQTYELNET
     AKQHELMTLD GFMMYLLSPE GAALNVAHTC VFQDMGQPLA HYFISSSHNT YLTDSQIGGT
     SSTEAYIRAF AQGCRCVELD CWEGPGGEPV IYHGHTLTSK ILFRDVIQAV RDHAFTSSPY
     PVILSLENHC GLEQQAVMAR HLRSILGDML VTQALDSQNP EELPSPEQLK GRILVKGKKL
     PAARSEDGRI LSDREEEEEE EEEAEEALEA AEQRSRAKQI SPELSALAVY CCATRLRTLD
     PSPGPPQSCT VGSLSERKAR KFTREAGTSF VRHNTQQLTR VYPLGLRMNS ANYNPQEMWN
     SGCQLVALNF QTPGYEMDLN TGRFLINGQC GYVLKPAYLR QLNTTFDPEC PGPPRTTLAI
     QVLTAQQLPK LNAEKPSSIV DPLVRVEIHG VPEDCAQKET DYVLNNGFNP CWEQTLQFRL
     RAPELVLVRF VVEDYDTTSP NDFVGQSTLP LSSLKQGYRH IHLLSKDGAS LAPATLFVHI
     RIQNS
//
ID   RELL1_MOUSE             Reviewed;         272 AA.
AC   Q8K2J7; Q3TVW8; Q3UZH6; Q8R3S5;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=RELT-like protein 1;
DE   Flags: Precursor;
GN   Name=Rell1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, Czech II, and FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBUNIT: Interacts with RELT, RELL2 and OXSR1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K2J7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K2J7-2; Sequence=VSP_032026;
CC   -!- SIMILARITY: Belongs to the RELT family.
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DR   EMBL; AK133845; BAE21881.1; -; mRNA.
DR   EMBL; AK140108; BAE24240.1; -; mRNA.
DR   EMBL; AK159944; BAE35500.1; -; mRNA.
DR   EMBL; AK161061; BAE36178.1; -; mRNA.
DR   EMBL; BC024679; AAH24679.1; -; mRNA.
DR   EMBL; BC031198; AAH31198.2; -; mRNA.
DR   EMBL; BC066137; AAH66137.2; -; mRNA.
DR   EMBL; BC066160; AAH66160.2; -; mRNA.
DR   IPI; IPI00169921; -.
DR   IPI; IPI00889254; -.
DR   RefSeq; NP_666035.2; NM_145923.4.
DR   UniGene; Mm.480645; -.
DR   ProteinModelPortal; Q8K2J7; -.
DR   PhosphoSite; Q8K2J7; -.
DR   PRIDE; Q8K2J7; -.
DR   Ensembl; ENSMUST00000087327; ENSMUSP00000084585; ENSMUSG00000047881.
DR   GeneID; 100532; -.
DR   KEGG; mmu:100532; -.
DR   UCSC; uc008xmh.1; mouse.
DR   CTD; 100532; -.
DR   MGI; MGI:2140767; Rell1.
DR   eggNOG; roNOG04833; -.
DR   GeneTree; ENSGT00530000063385; -.
DR   HOGENOM; HBG714820; -.
DR   HOVERGEN; HBG055552; -.
DR   InParanoid; Q8K2J7; -.
DR   OMA; TNKSKEG; -.
DR   OrthoDB; EOG4255TM; -.
DR   NextBio; 354498; -.
DR   ArrayExpress; Q8K2J7; -.
DR   Bgee; Q8K2J7; -.
DR   CleanEx; MM_RELL1; -.
DR   Genevestigator; Q8K2J7; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR022248; TNF_rcpt_RELT.
DR   Pfam; PF12606; RELT; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Membrane; Phosphoprotein; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     23       Potential.
FT   CHAIN        24    272       RELT-like protein 1.
FT                                /FTId=PRO_0000323591.
FT   TOPO_DOM     24     58       Extracellular (Potential).
FT   TRANSMEM     59     79       Helical; (Potential).
FT   TOPO_DOM     80    272       Cytoplasmic (Potential).
FT   COILED       90    114       Potential.
FT   MOD_RES     245    245       Phosphoserine (By similarity).
FT   MOD_RES     248    248       Phosphoserine (By similarity).
FT   VAR_SEQ       1     70       Missing (in isoform 2).
FT                                /FTId=VSP_032026.
SQ   SEQUENCE   272 AA;  29351 MW;  3029F065E2BC3C69 CRC64;
     MALWGLPGSA VLAASVFVGG AVSSPLVAAD NTGSHTLHSR AETTPSSPTN NPGNGHPEYI
     AYVLVPVFFV MGLLGVLICH LLKKKGYRCT TEAEQEVEEE KVEKIELNDS INENSDTVGQ
     IVQYIMKNEA NADILKAMVA DNSVGDIESP VTPSTPGSPP VSPGPLSPGA TPGKHVCGHH
     LHTVGGVVER DVCQRCRHKR WHFIKPTNKT KEGRPRRQGE VTVLSVGRFR VTKVEHKSNQ
     KERRSLMSVS GIESVNGDVP ATPVKRERSD TE
//
ID   AGFG1_MOUSE             Reviewed;         561 AA.
AC   Q8K2K6; O70448; Q8BQL5; Q8CDK9;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 2.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Arf-GAP domain and FG repeats-containing protein 1;
DE   AltName: Full=HIV-1 Rev-binding protein homolog;
DE   AltName: Full=Nucleoporin-like protein RIP;
GN   Name=Agfg1; Synonyms=Hrb, Rip;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH EPS15R.
RX   PubMed=9446614; DOI=10.1074/jbc.273.5.3003;
RA   Coda L., Salcini A.E., Confalonieri S., Pelicci G., Sorkina T.,
RA   Sorkin A., Pelicci P.G., Di Fiore P.P.;
RT   "Eps15R is a tyrosine kinase substrate with characteristics of a
RT   docking protein possibly involved in coated pits-mediated
RT   internalization.";
RL   J. Biol. Chem. 273:3003-3012(1998).
RN   [4]
RP   FUNCTION, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, INTERACTION WITH
RP   EPS15, AND DISRUPTION PHENOTYPE.
RX   PubMed=11711676; DOI=10.1126/science.1063665;
RA   Kang-Decker N., Mantchev G.T., Juneja S.C., McNiven M.A.,
RA   van Deursen J.M.A.;
RT   "Lack of acrosome formation in Hrb-deficient mice.";
RL   Science 294:1531-1533(2001).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177; SER-179 AND
RP   SER-181, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177 AND SER-181, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Required for vesicle docking or fusion during acrosome
CC       biogenesis. May play a role in RNA trafficking or localization.
CC   -!- SUBUNIT: Interacts with EPS15R and EPS15.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasmic vesicle
CC       (By similarity). Note=Associated with the cytosolic surface of
CC       proacrosomic vesicles of early round spermatids.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=4;
CC         IsoId=Q8K2K6-4; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q8K2K6-1; Sequence=VSP_017602;
CC       Name=2;
CC         IsoId=Q8K2K6-2; Sequence=VSP_010664;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8K2K6-3; Sequence=VSP_010665;
CC   -!- DEVELOPMENTAL STAGE: Highly expressed during spermiogenesis.
CC   -!- DOMAIN: Contains FG repeats.
CC   -!- PTM: O-glycosylated (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice have a normal life-span and show no
CC       apparent abnormalities. Females display normal fertility but males
CC       are infertile due to a lack of acrosome in their spermatozoa.
CC   -!- SIMILARITY: Contains 1 Arf-GAP domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK049400; BAC33736.1; -; mRNA.
DR   EMBL; AK029917; BAC26675.1; -; mRNA.
DR   EMBL; AK048326; BAC33303.1; -; mRNA.
DR   EMBL; AF057287; AAC97477.1; -; mRNA.
DR   EMBL; BC031154; AAH31154.1; -; mRNA.
DR   IPI; IPI00230359; -.
DR   IPI; IPI00420170; -.
DR   IPI; IPI00420171; -.
DR   IPI; IPI00420172; -.
DR   RefSeq; NP_034602.1; NM_010472.2.
DR   UniGene; Mm.392569; -.
DR   UniGene; Mm.433409; -.
DR   ProteinModelPortal; Q8K2K6; -.
DR   SMR; Q8K2K6; 14-134, 153-186.
DR   STRING; Q8K2K6; -.
DR   PhosphoSite; Q8K2K6; -.
DR   PRIDE; Q8K2K6; -.
DR   Ensembl; ENSMUST00000063380; ENSMUSP00000070250; ENSMUSG00000026159.
DR   Ensembl; ENSMUST00000113443; ENSMUSP00000109070; ENSMUSG00000026159.
DR   Ensembl; ENSMUST00000113444; ENSMUSP00000109071; ENSMUSG00000026159.
DR   GeneID; 15463; -.
DR   KEGG; mmu:15463; -.
DR   NMPDR; fig|10090.3.peg.648; -.
DR   UCSC; uc007bse.1; mouse.
DR   UCSC; uc007bsf.1; mouse.
DR   UCSC; uc007bsg.1; mouse.
DR   CTD; 15463; -.
DR   MGI; MGI:1333754; Agfg1.
DR   eggNOG; roNOG11753; -.
DR   GeneTree; ENSGT00560000077249; -.
DR   HOGENOM; HBG444331; -.
DR   HOVERGEN; HBG006551; -.
DR   InParanoid; Q8K2K6; -.
DR   OMA; AHFNSHT; -.
DR   OrthoDB; EOG40S0G0; -.
DR   NextBio; 288282; -.
DR   ArrayExpress; Q8K2K6; -.
DR   Bgee; Q8K2K6; -.
DR   Genevestigator; Q8K2K6; -.
DR   GermOnline; ENSMUSG00000026159; Mus musculus.
DR   GO; GO:0042995; C:cell projection; IDA:MGI.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0001675; P:acrosome assembly; IMP:MGI.
DR   GO; GO:0045109; P:intermediate filament organization; IMP:MGI.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR   GO; GO:0007289; P:spermatid nucleus differentiation; IMP:MGI.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001164; ArfGAP.
DR   Pfam; PF01412; ArfGap; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SUPFAM; SSF57863; ArfGAP; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasmic vesicle; Developmental protein;
KW   Differentiation; DNA-binding; Glycoprotein; Metal-binding; Nucleus;
KW   Phosphoprotein; Repeat; Spermatogenesis; Transport; Zinc; Zinc-finger.
FT   CHAIN         1    561       Arf-GAP domain and FG repeats-containing
FT                                protein 1.
FT                                /FTId=PRO_0000204905.
FT   DOMAIN       11    135       Arf-GAP.
FT   ZN_FING      29     52       C4-type.
FT   MOD_RES     177    177       Phosphothreonine.
FT   MOD_RES     179    179       Phosphoserine.
FT   MOD_RES     181    181       Phosphoserine.
FT   CARBOHYD    367    367       O-linked (GlcNAc) (By similarity).
FT   VAR_SEQ     342    362       Missing (in isoform 2).
FT                                /FTId=VSP_010664.
FT   VAR_SEQ     428    458       Missing (in isoform 3).
FT                                /FTId=VSP_010665.
FT   VAR_SEQ     513    514       Missing (in isoform 1).
FT                                /FTId=VSP_017602.
FT   CONFLICT      2      4       AAS -> GGR (in Ref. 1; BAC33736).
FT   CONFLICT      9      9       Q -> P (in Ref. 1; BAC33736).
FT   CONFLICT     34     34       Q -> H (in Ref. 1; BAC33736).
FT   CONFLICT     43     43       T -> R (in Ref. 1; BAC33736).
FT   CONFLICT     57     57       R -> K (in Ref. 1; BAC33736).
SQ   SEQUENCE   561 AA;  58043 MW;  B612D82F0051ECFF CRC64;
     MAASAKRKQE EKHLKMLRDM TGLPHNRKCF DCDQRGPTYV NMTVGSFVCT SCSGSLRGLN
     PPHRVKSISM TTFTQQEIEF LQKHGNEVCK QIWLGLFDDR SSAIPDFRDP QKVKEFLQEK
     YEKKRWYVPP EQAKVVASVH ASISGSSASS TSSTPEVKPL KSLLGESAPA LHLNKGTPSQ
     SPVVGRSQGQ QQEKKQFDLL SDLGSDIFAA PAPQSTATAN FANFAHFNSH AAQNSANADF
     ANFDAFGQSS GSSNFGGFPT ASHSSFQPQT TGGSAGSVNA NFAHFDNFPK SSSADFGTFS
     TSQSHQTAST VSKVSTNKAG LQTADKYAAL ANLDNIFSAG QGGDQGSGFG TTGKAPVGSV
     VSVPSHSSAS SDKYAALAEL DSVFSSAATS SNAYTPTSNA SSSVFGTVPV GASAQTQPAS
     SGPAPFGATP STNPFVAATG PSAASSTNPF QTNARGATAA TFGTASMSMP AGFGTPAQYS
     LPTSFSGSFQ QPAFPAQAAF PQQTAFSQQP NGAGFATFGQ TKPVVTPFGQ VAAAGVSSNP
     FMTGAPTGQL PTGSSSTNPF L
//
ID   TTC15_MOUSE             Reviewed;         797 AA.
AC   Q8K2L8; Q8BX27;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Tetratricopeptide repeat protein 15;
DE            Short=TPR repeat protein 15;
GN   Name=Ttc15;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 224-797.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-128; THR-130
RP   AND SER-234, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SIMILARITY: Contains 4 TPR repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC33585.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC024077; AAH24077.1; -; mRNA.
DR   EMBL; BC030887; AAH30887.1; -; mRNA.
DR   EMBL; AK049172; BAC33585.1; ALT_INIT; mRNA.
DR   IPI; IPI00322302; -.
DR   RefSeq; NP_848926.3; NM_178811.4.
DR   UniGene; Mm.132006; -.
DR   UniGene; Mm.341316; -.
DR   ProteinModelPortal; Q8K2L8; -.
DR   SMR; Q8K2L8; 608-765.
DR   PhosphoSite; Q8K2L8; -.
DR   PRIDE; Q8K2L8; -.
DR   Ensembl; ENSMUST00000020954; ENSMUSP00000020954; ENSMUSG00000020628.
DR   GeneID; 217449; -.
DR   KEGG; mmu:217449; -.
DR   UCSC; uc007nfw.1; mouse.
DR   CTD; 217449; -.
DR   MGI; MGI:2445089; Ttc15.
DR   HOGENOM; HBG444697; -.
DR   HOVERGEN; HBG068968; -.
DR   InParanoid; Q8K2L8; -.
DR   OrthoDB; EOG4B5P4X; -.
DR   NextBio; 375861; -.
DR   ArrayExpress; Q8K2L8; -.
DR   Bgee; Q8K2L8; -.
DR   CleanEx; MM_TTC15; -.
DR   Genevestigator; Q8K2L8; -.
DR   GermOnline; ENSMUSG00000020628; Mus musculus.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR013105; TPR_2.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 2.
DR   Pfam; PF07719; TPR_2; 1.
DR   SMART; SM00028; TPR; 4.
DR   PROSITE; PS50005; TPR; 4.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Repeat; TPR repeat.
FT   CHAIN         1    797       Tetratricopeptide repeat protein 15.
FT                                /FTId=PRO_0000106402.
FT   REPEAT      607    640       TPR 1.
FT   REPEAT      642    675       TPR 2.
FT   REPEAT      682    715       TPR 3.
FT   REPEAT      716    749       TPR 4.
FT   MOD_RES     125    125       Phosphoserine.
FT   MOD_RES     128    128       Phosphoserine.
FT   MOD_RES     130    130       Phosphothreonine.
FT   MOD_RES     232    232       Phosphoserine (By similarity).
FT   MOD_RES     234    234       Phosphoserine.
FT   CONFLICT    241    241       M -> T (in Ref. 2; BAC33585).
FT   CONFLICT    305    305       V -> I (in Ref. 2; BAC33585).
SQ   SEQUENCE   797 AA;  87724 MW;  5DFE960A9EE062D7 CRC64;
     METAKDGEQS PSEASPSAQA GPENIPEPMS REEESQPLYH EETIDLGGDE FASEENEPTS
     EGSHNFGDKL NEHMMESVLI SDSPNNSEGD VGDLGCLQDV GEPPRGATDH RLPSSTDKEV
     VDTLSNGSET DGDDTPRDIS DMTPDSRASL KEDSTQEDVT SMPALENAAT EEVGPKDSLA
     PREEQTSEVS SNQSSSKDEP LPVCTIFSQA TATPSQPHLF LQDGFESQMV KSPSFSSTSE
     MSAKTPPPMV QPSPSLSTFF GDTMSSNSLA SDFFDSFTTS TFISVSNPNA GSPVPEKLSS
     LTAPVGEKSP DSTSPSYSTR MDRSESGVSR APLDVPESPK PFSQIQAVFA GSDDPFATAL
     SMSEMDRRND AWLPSQATRE VLMSVATQQY GTVFIDKENL TMPGLKFDNI QGDAVKDLML
     RFLGEKAAAK RQVLNASSVE QSFVGLKQLI SCRNWRAAVD LCGRLLTAHG QGYGKNGLPT
     SHTTDSLQLW FVRLALLVKL GLFQNAEMEF EPFGNLDQPD LYYEYYPHVY PGRRGSMVPF
     SMRILHAELQ QYLGNPQESL DRLHRVKTVC SKILANLEQG LAEDGGLSSV TQESRQASVQ
     LWRSRLGRVL YSMANCLLLM KDYVLAVDAY LTVIKYYPEQ EPQLLSGIGR ILLQIGDIKT
     AEKYFQDVEK VTQKLDGLQG KIMVLMNRAF LYLGQNNFAE AHKFFTEILR MDPTNAVANN
     NAAVCLLYLG KLKDSLRQLE AMVQQDPRHY LHESVLFNLT TMYELESSRS MQKKQSLLEA
     VASKEGDSFN TQCLKLA
//
ID   S38A1_MOUSE             Reviewed;         485 AA.
AC   Q8K2P7; Q3TNM1; Q3TQ53; Q6NXZ2; Q8BHI3; Q8BXE2; Q99PR1;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Sodium-coupled neutral amino acid transporter 1;
DE   AltName: Full=Amino acid transporter A1;
DE   AltName: Full=MNat2;
DE   AltName: Full=N-system amino acid transporter 2;
DE   AltName: Full=Solute carrier family 38 member 1;
DE   AltName: Full=System A amino acid transporter 1;
DE   AltName: Full=System N amino acid transporter 1;
GN   Name=Slc38a1; Synonyms=Nat2, Snat1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=21316561; PubMed=11325958; DOI=10.1074/jbc.M009003200;
RA   Gu S., Roderick H.L., Camacho P., Jiang J.X.;
RT   "Characterization of an N-system amino acid transporter expressed in
RT   retina and its involvement in glutamine transport.";
RL   J. Biol. Chem. 276:24137-24144(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Diencephalon, Embryo, Embryonic head,
RC   Embryonic stem cell, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=CD-1, and FVB/N-3; TISSUE=Mammary tumor, and Neural stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INDUCTION BY BDNF.
RX   PubMed=17179157; DOI=10.1074/jbc.M608548200;
RA   Burkhalter J., Fiumelli H., Erickson J.D., Martin J.-L.;
RT   "A critical role for system A amino acid transport in the regulation
RT   of dendritic development by brain-derived neurotrophic factor
RT   (BDNF).";
RL   J. Biol. Chem. 282:5152-5159(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-56, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Functions as a sodium-dependent amino acid transporter.
CC       Mediates the saturable, pH-sensitive and electrogenic cotransport
CC       of glutamine and sodium ions with a stoichiometry of 1:1. May also
CC       transport small zwitterionic and aliphatic amino acids with a
CC       lower affinity. May supply glutamatergic and GABAergic neurons
CC       with glutamine which is required for the synthesis of the
CC       neurotransmitters glutamate and GABA.
CC   -!- ENZYME REGULATION: Inhibited by lithium, potassium, choline ions,
CC       N-methyl-D-glucamine and 2-methylamino-isobutyric acid (MeAIB) (By
CC       similarity).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2400 uM for L-glutamine (at pH 7.0);
CC         KM=890 uM for L-glutamine (at pH 7.5);
CC         KM=540 uM for L-glutamine (at pH 8.0);
CC         Note=Decrease in pH from 8.0 to 7.0 results in decreased
CC         affinity for L-glutamine;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity). Note=Restricted to the somatodendritic
CC       compartment of neurons (By similarity). Found in the cellular
CC       processes of neurons in the developing brain (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8K2P7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K2P7-2; Sequence=VSP_029307, VSP_029308;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8K2P7-3; Sequence=VSP_029305, VSP_029306;
CC   -!- TISSUE SPECIFICITY: Specifically expressed in brain and retina (at
CC       protein level). Also detected in spleen, small intestine and lung.
CC   -!- INDUCTION: Up-regulated by BDNF.
CC   -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2
CC       family.
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DR   EMBL; AF184240; AAG43433.2; -; mRNA.
DR   EMBL; AK029189; BAC26341.1; -; mRNA.
DR   EMBL; AK034130; BAC28597.1; -; mRNA.
DR   EMBL; AK035098; BAC28944.1; -; mRNA.
DR   EMBL; AK047459; BAC33064.1; -; mRNA.
DR   EMBL; AK049294; BAC33663.1; -; mRNA.
DR   EMBL; AK050914; BAC34457.1; -; mRNA.
DR   EMBL; AK081724; BAC38310.1; -; mRNA.
DR   EMBL; AK162612; BAE36989.1; -; mRNA.
DR   EMBL; AK163914; BAE37532.1; -; mRNA.
DR   EMBL; AK165188; BAE38067.1; -; mRNA.
DR   EMBL; BC030378; AAH30378.1; -; mRNA.
DR   EMBL; BC066815; AAH66815.1; -; mRNA.
DR   IPI; IPI00459577; -.
DR   IPI; IPI00621987; -.
DR   IPI; IPI00875551; -.
DR   RefSeq; NP_001159928.1; NM_001166456.1.
DR   RefSeq; NP_001159930.1; NM_001166458.1.
DR   RefSeq; NP_598847.2; NM_134086.4.
DR   UniGene; Mm.103568; -.
DR   ProteinModelPortal; Q8K2P7; -.
DR   STRING; Q8K2P7; -.
DR   PhosphoSite; Q8K2P7; -.
DR   PRIDE; Q8K2P7; -.
DR   Ensembl; ENSMUST00000088452; ENSMUSP00000085799; ENSMUSG00000023169.
DR   Ensembl; ENSMUST00000088454; ENSMUSP00000085801; ENSMUSG00000023169.
DR   GeneID; 105727; -.
DR   KEGG; mmu:105727; -.
DR   UCSC; uc007xkg.1; mouse.
DR   CTD; 105727; -.
DR   MGI; MGI:2145895; Slc38a1.
DR   eggNOG; roNOG04774; -.
DR   GeneTree; ENSGT00550000074222; -.
DR   HOVERGEN; HBG059571; -.
DR   InParanoid; Q8K2P7; -.
DR   OMA; RIWAALF; -.
DR   OrthoDB; EOG4CJVH4; -.
DR   NextBio; 357848; -.
DR   ArrayExpress; Q8K2P7; -.
DR   Bgee; Q8K2P7; -.
DR   CleanEx; MM_SLC38A1; -.
DR   Genevestigator; Q8K2P7; -.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0015186; F:L-glutamine transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR013057; AA_transpt_TM.
DR   Pfam; PF01490; Aa_trans; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Amino-acid transport; Cell membrane;
KW   Glycoprotein; Ion transport; Membrane; Phosphoprotein; Sodium;
KW   Sodium transport; Symport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    485       Sodium-coupled neutral amino acid
FT                                transporter 1.
FT                                /FTId=PRO_0000310476.
FT   TOPO_DOM      1     74       Cytoplasmic (Potential).
FT   TRANSMEM     75     97       Helical; (Potential).
FT   TOPO_DOM     98    112       Extracellular (Potential).
FT   TRANSMEM    113    133       Helical; (Potential).
FT   TOPO_DOM    134    148       Cytoplasmic (Potential).
FT   TRANSMEM    149    169       Helical; (Potential).
FT   TOPO_DOM    170    188       Extracellular (Potential).
FT   TRANSMEM    189    211       Helical; (Potential).
FT   TOPO_DOM    212    216       Cytoplasmic (Potential).
FT   TRANSMEM    217    237       Helical; (Potential).
FT   TOPO_DOM    238    273       Extracellular (Potential).
FT   TRANSMEM    274    294       Helical; (Potential).
FT   TOPO_DOM    295    310       Cytoplasmic (Potential).
FT   TRANSMEM    311    331       Helical; (Potential).
FT   TOPO_DOM    332    348       Extracellular (Potential).
FT   TRANSMEM    349    369       Helical; (Potential).
FT   TOPO_DOM    370    391       Cytoplasmic (Potential).
FT   TRANSMEM    392    412       Helical; (Potential).
FT   TOPO_DOM    413    414       Extracellular (Potential).
FT   TRANSMEM    415    435       Helical; (Potential).
FT   TOPO_DOM    436    450       Cytoplasmic (Potential).
FT   TRANSMEM    451    471       Helical; (Potential).
FT   TOPO_DOM    472    485       Extracellular (Potential).
FT   MOD_RES      25     25       Phosphoserine (By similarity).
FT   MOD_RES      28     28       Phosphoserine (By similarity).
FT   MOD_RES      49     49       Phosphoserine (By similarity).
FT   MOD_RES      52     52       Phosphoserine.
FT   MOD_RES      54     54       Phosphothreonine (By similarity).
FT   MOD_RES      56     56       Phosphoserine.
FT   CARBOHYD    251    251       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    257    257       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ      67     72       IPGTTS -> VSIICM (in isoform 3).
FT                                /FTId=VSP_029305.
FT   VAR_SEQ      73    485       Missing (in isoform 3).
FT                                /FTId=VSP_029306.
FT   VAR_SEQ     333    344       EKVQSDLLHKYQ -> GKLLPLAMPICT (in isoform
FT                                2).
FT                                /FTId=VSP_029307.
FT   VAR_SEQ     345    485       Missing (in isoform 2).
FT                                /FTId=VSP_029308.
FT   CONFLICT     48     48       E -> G (in Ref. 2; BAE38067).
FT   CONFLICT    244    244       P -> H (in Ref. 2; BAC33064).
FT   CONFLICT    354    354       V -> A (in Ref. 1; AAG43433).
FT   CONFLICT    360    360       V -> A (in Ref. 1; AAG43433).
SQ   SEQUENCE   485 AA;  53795 MW;  1171E1458818977C CRC64;
     MMHFKSGLEL TELQNMTVPE DDNVSNDSND FTEVENGQIN SKFISDRESR RSLTNSHLEK
     RKCDEYIPGT TSLGMSVFNL SNAIMGSGIL GLAFALANTG ILLFLILLTS VTLLSIYSIN
     LLLICSKETG CMVYEKLGEQ VFGTTGKLVI FGATSLQNTG AMLSYLFIVK NELPSAIKSL
     MGEEDAFSAW YVDGRVLVVM VTFGIILPLC LLKNLGYLGY TSGFSLSCMM FFLIVVIYKK
     FQTPCMSVEQ NSTVSANVTD ACTPKYVTFN SKTVYALPTI AFAFVCHPSV LPIYSELKDR
     SQKKMQMVSN ISFFAMFVMY FLTAIFGYLT FYEKVQSDLL HKYQSTGDIL ILTVRLAVIV
     AVILTVPVLF FTVRSSLFEL AKKTKFHLCR HVLVTIILLI IINLLVIFIP SMKDIFGVVG
     VTSANMLIFI LPSSLYLKIT NQDGDKGTQR IWAALFLGLG VLFSLISIPL VIYDWACSSG
     TDEGH
//
ID   Q8K2T9_MOUSE            Unreviewed;       549 AA.
AC   Q8K2T9;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   08-FEB-2011, entry version 36.
DE   SubName: Full=Tpr protein;
GN   Name=Tpr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N;
RC   TISSUE=Mammary tumor. Metallothionien-TGF alpha model. 10 month old
RC   virgin mouse. Taken by biopsy.;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
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DR   EMBL; BC029834; AAH29834.1; -; mRNA.
DR   IPI; IPI00177059; -.
DR   UniGene; Mm.174256; -.
DR   ProteinModelPortal; Q8K2T9; -.
DR   STRING; Q8K2T9; -.
DR   PRIDE; Q8K2T9; -.
DR   Ensembl; ENSMUST00000151563; ENSMUSP00000116012; ENSMUSG00000006005.
DR   UCSC; uc007cye.1; mouse.
DR   MGI; MGI:1922066; Tpr.
DR   GeneTree; ENSGT00570000079199; -.
DR   InParanoid; Q8K2T9; -.
DR   ArrayExpress; Q8K2T9; -.
DR   Bgee; Q8K2T9; -.
DR   Genevestigator; Q8K2T9; -.
DR   GO; GO:0005635; C:nuclear envelope; IDA:MGI.
PE   1: Evidence at protein level;
SQ   SEQUENCE   549 AA;  60192 MW;  77A29FBCD483AAB8 CRC64;
     METSTQSSGD HQEQHISVQE MQELKDTLSQ SETKTKSLEG QVENLQKTLS EKETEARSLQ
     EQTVQLQSEL SRLRQDLQDK TTEEQLRQQM NEKTWKTLAL AKSKITHLSG VKDQLTKEIE
     ELKQRNGALD QQKDELDVRM TALKSQYEGR ISRLERELRE HQERHLEQRD EPQEPTNKAP
     EQQRQITLKT TPASGERGIA STSDPPTANI KPTPVVSTPS KVTAAAMAGN KSTPRASIRP
     MVTPATVTNP TTTPTATVMP TTQVESQEAM QSEGPVEHVP VFGNASGSVR STSPNVQPSI
     SQPILTVQQQ TQATAFVQPT QQSHPQIEPT NQELSPNIVE VVQSSPVERP STSTAVFGTV
     SATPSSSLPK RTREEEEDST MEAGDQVSED TVEMPLPKKL KMVTPVGTEE EVMAEESTDG
     EAETQAYNQD SQDSIGEGVT QGDYTPMEDS EETSQSLQID LGPLQSDQQT TSSQDGQGKG
     DDVIVIDSDD EDDDEENDGE HEDYEEDEDD DDDEEDDTGM GDEGEDSNEG TGSADGNDGY
     EADDAEVTG
//
ID   RN219_MOUSE             Reviewed;         722 AA.
AC   Q8K2Y0; Q9CYU1; Q9D1Y0;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=RING finger protein 219;
GN   Name=Rnf219;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8K2Y0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K2Y0-2; Sequence=VSP_015335, VSP_015336;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8K2Y0-3; Sequence=VSP_015337, VSP_015338;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH29231.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK013314; BAB28786.1; -; mRNA.
DR   EMBL; AK020974; BAB32265.1; -; mRNA.
DR   EMBL; BC029231; AAH29231.1; ALT_INIT; mRNA.
DR   IPI; IPI00322413; -.
DR   IPI; IPI00473261; -.
DR   IPI; IPI00650028; -.
DR   UniGene; Mm.291811; -.
DR   ProteinModelPortal; Q8K2Y0; -.
DR   SMR; Q8K2Y0; 16-63.
DR   PhosphoSite; Q8K2Y0; -.
DR   PRIDE; Q8K2Y0; -.
DR   Ensembl; ENSMUST00000022716; ENSMUSP00000022716; ENSMUSG00000022120.
DR   UCSC; uc007uxc.1; mouse.
DR   UCSC; uc007uxd.1; mouse.
DR   UCSC; uc007uxe.1; mouse.
DR   MGI; MGI:1919736; Rnf219.
DR   HOGENOM; HBG278550; -.
DR   HOVERGEN; HBG054043; -.
DR   InParanoid; Q8K2Y0; -.
DR   OrthoDB; EOG49CQ8Q; -.
DR   ArrayExpress; Q8K2Y0; -.
DR   Bgee; Q8K2Y0; -.
DR   CleanEx; MM_RNF219; -.
DR   Genevestigator; Q8K2Y0; -.
DR   GermOnline; ENSMUSG00000022120; Mus musculus.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Metal-binding; Phosphoprotein;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    722       RING finger protein 219.
FT                                /FTId=PRO_0000055877.
FT   ZN_FING      18     56       RING-type; degenerate.
FT   COILED       87    129       Potential.
FT   COILED      157    267       Potential.
FT   MOD_RES     414    414       Phosphoserine (By similarity).
FT   MOD_RES     588    588       Phosphoserine (By similarity).
FT   MOD_RES     715    715       Phosphoserine (By similarity).
FT   MOD_RES     717    717       Phosphoserine (By similarity).
FT   VAR_SEQ     213    214       KF -> NL (in isoform 2).
FT                                /FTId=VSP_015335.
FT   VAR_SEQ     214    232       FGRFTVAALQSKVEQYERE -> YVPHTQSEAIATPMGCGS
FT                                L (in isoform 3).
FT                                /FTId=VSP_015337.
FT   VAR_SEQ     215    722       Missing (in isoform 2).
FT                                /FTId=VSP_015336.
FT   VAR_SEQ     233    722       Missing (in isoform 3).
FT                                /FTId=VSP_015338.
SQ   SEQUENCE   722 AA;  79958 MW;  A7120DE6561FEC95 CRC64;
     MAQTVQNVTL SLTLPITCHI CLGKVRQPVV CTNNHVFCSI CIDLWLKNNS QCPACRVPIT
     PENPCKEIIG GTSESEPMLS HTVRKHLRKT RLELLHREYE DEIDCLQKEV EELKSKNLSL
     ESQIKTILDP LALMQGSQNE DKHPLADNPS KMDPDSVVEW KKKLRTANEI YEKVKDDVDK
     LKEANKKLKL ENGGLLRENL RLKAEVDNRS PQKFGRFTVA ALQSKVEQYE RETNRLKKAL
     ERSDKYIEEL ESQVAHLKHS EEAKEDVDAL CQRAPSADSK GPNGSDELGP PKNQSDSARK
     QAGSASASHL ASPSSSRLAD SGSVRQESTS RTEPNCPQNK DRYPKPTEPR LGARETPMDT
     YLEREWGSKP SDCAPYKEDE LYGIPASCTP LSLSCLQLNT PENRENPVIK AGSSKKHANH
     LRKLVFDDFC DSPNACNNNS SEDDRRENEK KSDCFASSKT GFWDCCSTSY AQSLEFDGSE
     GNAIANSVGE IPSKLSEKSG SCLSKRLSCI RSLEMNRTRT SSEASMDAAY LDKISELDSM
     MSESDNSKSP CNNGFKSVEV EGPSKSPQGR EFLEEPDKLQ EGSKLNLSKP ALTADGLESG
     GEWKPSSFFL LSPADHEMSE DFSLHSTSHS GTSEVKPPNC LFQTEFSQGA LLSSSQGLFE
     DQRFGSSLFK ISSEMQSLHS PLQSPWSAAF VPEKRSKNGN QSTKRKIQSS LANASPSKAT
     KS
//
ID   CCM2_MOUSE              Reviewed;         453 AA.
AC   Q8K2Y9; Q5SUA3;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Malcavernin;
DE   AltName: Full=Cerebral cavernous malformations protein 2 homolog;
DE   AltName: Full=Osmosensing scaffold for MEKK3;
GN   Name=Ccm2; Synonyms=Osm;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH MAP3K3; MAP2K3 AND
RP   RAC1.
RC   STRAIN=C57BL/6; TISSUE=T-cell lymphoma;
RX   PubMed=14634666; DOI=10.1038/ncb1071;
RA   Uhlik M.T., Abell A.N., Johnson N.L., Sun W., Cuevas B.D.,
RA   Lobel-Rice K.E., Horne E.A., Dell'Acqua M.L., Johnson G.L.;
RT   "Rac-MEKK3-MKK3 scaffolding for p38 MAPK activation during
RT   hyperosmotic shock.";
RL   Nat. Cell Biol. 5:1104-1110(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=NOD; TISSUE=Dendritic cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
RP   SPLICING (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May function as a scaffold protein for MAP2K3-MAP3K3
CC       signaling. Seems to play a major role in the modulation of MAP3K3-
CC       dependent p38 activation induced by hyperosmotic shock.
CC   -!- SUBUNIT: Part of a complex with MAP2K3, MAP3K3 and RAC1. Binds
CC       RAC1 directly and independently of its nucleotide-bound state.
CC       Interacts with PDCD10 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Treatment with sorbitol
CC       caused relocalization to ruffle-like structures.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K2Y9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K2Y9-2; Sequence=VSP_024404, VSP_024405;
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart, lower expression in
CC       kidney, lung and liver (at protein level).
CC   -!- SIMILARITY: Contains 1 PID domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY442689; AAR29082.1; -; mRNA.
DR   EMBL; AK155145; BAE33075.1; -; mRNA.
DR   EMBL; AL603787; CAI24218.1; -; Genomic_DNA.
DR   EMBL; AL646047; CAI24218.1; JOINED; Genomic_DNA.
DR   EMBL; AL603787; CAI24220.1; -; Genomic_DNA.
DR   EMBL; AL646047; CAI24220.1; JOINED; Genomic_DNA.
DR   EMBL; AL646047; CAI25990.1; -; Genomic_DNA.
DR   EMBL; AL603787; CAI25990.1; JOINED; Genomic_DNA.
DR   EMBL; AL646047; CAI25992.1; -; Genomic_DNA.
DR   EMBL; AL603787; CAI25992.1; JOINED; Genomic_DNA.
DR   EMBL; BC029157; AAH29157.1; -; mRNA.
DR   IPI; IPI00170037; -.
DR   IPI; IPI00649501; -.
DR   RefSeq; NP_666126.1; NM_146014.3.
DR   UniGene; Mm.221271; -.
DR   ProteinModelPortal; Q8K2Y9; -.
DR   STRING; Q8K2Y9; -.
DR   PhosphoSite; Q8K2Y9; -.
DR   PRIDE; Q8K2Y9; -.
DR   Ensembl; ENSMUST00000000388; ENSMUSP00000000388; ENSMUSG00000000378.
DR   GeneID; 216527; -.
DR   KEGG; mmu:216527; -.
DR   UCSC; uc007hyv.1; mouse.
DR   CTD; 216527; -.
DR   MGI; MGI:2384924; Ccm2.
DR   GeneTree; ENSGT00390000016168; -.
DR   HOGENOM; HBG445607; -.
DR   HOVERGEN; HBG054451; -.
DR   InParanoid; Q8K2Y9; -.
DR   OMA; SYIRDDS; -.
DR   OrthoDB; EOG4RFKSP; -.
DR   PhylomeDB; Q8K2Y9; -.
DR   NextBio; 375194; -.
DR   ArrayExpress; Q8K2Y9; -.
DR   Bgee; Q8K2Y9; -.
DR   CleanEx; MM_CCM2; -.
DR   CleanEx; MM_OSM; -.
DR   Genevestigator; Q8K2Y9; -.
DR   GermOnline; ENSMUSG00000000378; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0043234; C:protein complex; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0060837; P:blood vessel endothelial cell differentiation; IMP:MGI.
DR   GO; GO:0045216; P:cell-cell junction organization; IMP:MGI.
DR   GO; GO:0001885; P:endothelial cell development; IGI:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IGI:MGI.
DR   GO; GO:0060039; P:pericardium development; IGI:MGI.
DR   GO; GO:0001570; P:vasculogenesis; IGI:MGI.
DR   GO; GO:0048845; P:venous blood vessel morphogenesis; IGI:MGI.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   PROSITE; PS01179; PID; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Phosphoprotein.
FT   CHAIN         1    453       Malcavernin.
FT                                /FTId=PRO_0000089425.
FT   DOMAIN       59    248       PID.
FT   MOD_RES     393    393       Phosphoserine (By similarity).
FT   VAR_SEQ       1     10       MEEEGKKGKK -> MENE (in isoform 2).
FT                                /FTId=VSP_024404.
FT   VAR_SEQ     279    287       Missing (in isoform 2).
FT                                /FTId=VSP_024405.
SQ   SEQUENCE   453 AA;  49917 MW;  51F165291E52691F CRC64;
     MEEEGKKGKK PGIVSPFKRV FLKGEKSRDK KAHEKVTERR PLHTVVLALP ERVEPDRLLS
     DYIEKEVKYL GQLTSIPGYL NPSSRTEILH FIDKAKRSHQ LPGHLTQEHD AVLSLSAYNV
     KLAWRDGEDI ILRVPIHDIA AVSYVRDDAA HLVVLKTAQD PGISPSQSLC AESSRGLSAG
     SLSESAVGPV EACCLVIMAT ESKVAAEELC SLLSQVFQIV YTESTIDFLD RAIFDGASTP
     THHLSLHSDD SSTKVDMKDS YDADASTFCF PDSGDVGGLP PLPFCMQTSP HSKTVSESEL
     STSATELLQD YMLTLRTKLS SQEIQQFAAL LHEYRNGASI HEFCISLRQL YGDSRKFLLL
     GLRPFIPEKD SQHFENFLET IGVKDGRGII TDSFGRHRRA LSTTSTSTIN GNRTTGSPDD
     RSAPSEGDEW DRMISDISSD IEALGCSMDQ DSA
//
ID   MATR3_MOUSE             Reviewed;         846 AA.
AC   Q8K310;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Matrin-3;
GN   Name=Matr3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 4-12; 20-44; 93-127; 133-146; 193-223; 230-245;
RP   271-304; 399-407; 413-433; 497-515; 525-530; 533-542; 556-562;
RP   719-735; 780-797 AND 804-816, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-598, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-598, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-598, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-598, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [9]
RP   STRUCTURE BY NMR OF 390-576.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of RRM domains in matrin 3.";
RL   Submitted (NOV-2005) to the PDB data bank.
CC   -!- FUNCTION: May play a role in transcription or may interact with
CC       other nuclear matrix proteins to form the internal fibrogranular
CC       network. In association with the SFPQ-NONO heteromer may play a
CC       role in nuclear retention of defective RNAs (By similarity).
CC   -!- SUBUNIT: Part of complex consisting of SFPQ, NONO and MATR3 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus matrix (By similarity).
CC   -!- SIMILARITY: Contains 1 matrin-type zinc finger.
CC   -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK087939; BAC40050.1; -; mRNA.
DR   EMBL; BC029070; AAH29070.1; -; mRNA.
DR   IPI; IPI00453826; -.
DR   RefSeq; NP_034901.2; NM_010771.6.
DR   UniGene; Mm.215034; -.
DR   PDB; 1X4D; NMR; -; A=390-478.
DR   PDB; 1X4F; NMR; -; A=478-576.
DR   PDBsum; 1X4D; -.
DR   PDBsum; 1X4F; -.
DR   ProteinModelPortal; Q8K310; -.
DR   SMR; Q8K310; 390-576.
DR   STRING; Q8K310; -.
DR   PhosphoSite; Q8K310; -.
DR   PRIDE; Q8K310; -.
DR   Ensembl; ENSMUST00000041514; ENSMUSP00000046908; ENSMUSG00000037236.
DR   GeneID; 17184; -.
DR   KEGG; mmu:17184; -.
DR   UCSC; uc008emg.1; mouse.
DR   CTD; 17184; -.
DR   MGI; MGI:1298379; Matr3.
DR   HOVERGEN; HBG057347; -.
DR   InParanoid; Q8K310; -.
DR   OMA; LFYTNED; -.
DR   OrthoDB; EOG4KSPJ4; -.
DR   PhylomeDB; Q8K310; -.
DR   NextBio; 291510; -.
DR   ArrayExpress; Q8K310; -.
DR   Bgee; Q8K310; -.
DR   CleanEx; MM_MATR3; -.
DR   Genevestigator; Q8K310; -.
DR   GermOnline; ENSMUSG00000037236; Mus musculus.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR000690; Znf_C2H2_matrin.
DR   InterPro; IPR003604; Znf_U1.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   SMART; SM00360; RRM; 2.
DR   SMART; SM00355; ZnF_C2H2; 1.
DR   SMART; SM00451; ZnF_U1; 2.
DR   PROSITE; PS50102; RRM; 2.
DR   PROSITE; PS50171; ZF_MATRIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing; Metal-binding;
KW   Nucleus; Phosphoprotein; Repeat; RNA-binding; Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    846       Matrin-3.
FT                                /FTId=PRO_0000081623.
FT   DOMAIN      398    473       RRM 1.
FT   DOMAIN      496    571       RRM 2.
FT   ZN_FING     800    831       Matrin-type.
FT   MOTIF       709    717       Nuclear localization signal (Potential).
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES       3      3       N6-acetyllysine (By similarity).
FT   MOD_RES      22     22       Phosphoserine (By similarity).
FT   MOD_RES     118    118       Phosphoserine (By similarity).
FT   MOD_RES     188    188       Phosphoserine.
FT   MOD_RES     195    195       Phosphoserine (By similarity).
FT   MOD_RES     206    206       Phosphoserine (By similarity).
FT   MOD_RES     208    208       Phosphoserine (By similarity).
FT   MOD_RES     397    397       Phosphoserine (By similarity).
FT   MOD_RES     473    473       N6-acetyllysine (By similarity).
FT   MOD_RES     522    522       N6-acetyllysine (By similarity).
FT   MOD_RES     533    533       Phosphoserine (By similarity).
FT   MOD_RES     571    571       N6-acetyllysine (By similarity).
FT   MOD_RES     596    596       Phosphoserine (By similarity).
FT   MOD_RES     598    598       Phosphoserine.
FT   MOD_RES     604    604       Phosphoserine (By similarity).
FT   MOD_RES     606    606       Phosphoserine (By similarity).
FT   MOD_RES     653    653       Phosphoserine (By similarity).
FT   MOD_RES     670    670       Phosphoserine (By similarity).
FT   MOD_RES     672    672       Phosphoserine (By similarity).
FT   MOD_RES     673    673       Phosphoserine (By similarity).
FT   MOD_RES     695    695       Phosphoserine (By similarity).
FT   MOD_RES     772    772       Phosphotyrosine (By similarity).
FT   MOD_RES     835    835       N6-acetyllysine (By similarity).
FT   STRAND      399    404
FT   STRAND      408    410
FT   HELIX       411    416
FT   TURN        417    419
FT   HELIX       420    422
FT   STRAND      425    430
FT   STRAND      432    435
FT   STRAND      437    443
FT   HELIX       444    456
FT   STRAND      467    471
FT   STRAND      497    502
FT   HELIX       511    514
FT   TURN        515    520
FT   STRAND      524    529
FT   TURN        530    533
FT   STRAND      534    538
FT   HELIX       542    554
FT   STRAND      559    562
FT   STRAND      565    569
SQ   SEQUENCE   846 AA;  94630 MW;  59C30E63D55093AF CRC64;
     MSKSFQQSSL GRDSQGHGRD LSAAGIGLLA AATQSLSMPA SLGRMNQGTA RLASLMNLGM
     SSSLNQQGAH SALSSASTSS HNLQSIFNIG SRGPLPLSSQ HRGDTDQASN ILASFGLSAR
     DLDELSRYPE DKITPENLPQ ILLQLKRRRT EEGPTLSYGR DGRSATREPP YRVPRDDWEE
     KRHFRRDSFD DRGPSLNPVL DYDHGSRSQE SGYYDRMDYE DDRLRDGERC RDDSFFGETS
     HNYHKFDSEY ERMGRGPGPL QERSLFEKKR GAPPSSNIED FHGLLPKGYP HLCSICDLPV
     HSNKEWSQHI NGASHSRRCQ LLLEIYPEWN PDNDTGHTMG DPFMLQQSTN PAPGILGPPP
     PSFHLGGPAV GPRGNLGAGN GNLQGPRHMQ KGRVETSRVV HIMDFQRGKN LRYQLLQLVE
     PFGVISNHLI LNKINEAFIE MATTEDAQAA VDYYTTTPAL VFGKPVRVHL SQKYKRIKKP
     EGKPDQKFDQ KQELGRVIHL SNLPHSGYSD SAVLKLAEPY GKIKNYILMR MKSQAFIEME
     TREDAMAMVD HCLKKALWFQ GRCVKVDLSE KYKKLVLRIP NRGIDLLKKD KSRKRSYSPD
     GKESPSDKKS KTDAQKTESP AEGKEQEEKS GEDGEKDTKD DQTEQEPSML LESEDELLVD
     EEEAAALLES GSSVGDETDL ANLGDVSSDG KKEPSDKAVK KDPSASATSK KKLKKVDKIE
     ELDQENEAAL ENGIKNEENT EPGAESAENA DDPNKDTSEN ADGQNDENKE DYTIPDEYRI
     GPYQPNVPVG IDYVIPKTGF YCKLCSLFYT NEEVAKNTHC SSLPHYQKLK KFLNKLAEER
     RQKKET
//
ID   Q8K314_MOUSE            Unreviewed;       914 AA.
AC   Q8K314;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   SubName: Full=Atp2b1 protein;
DE   Flags: Fragment;
GN   Name=Atp2b1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor. C3, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC029045; AAH29045.1; -; mRNA.
DR   EMBL; BC049262; AAH49262.1; -; mRNA.
DR   IPI; IPI00556827; -.
DR   UniGene; Mm.166944; -.
DR   UniGene; Mm.471912; -.
DR   ProteinModelPortal; Q8K314; -.
DR   STRING; Q8K314; -.
DR   PhosphoSite; Q8K314; -.
DR   PRIDE; Q8K314; -.
DR   Ensembl; ENSMUST00000020107; ENSMUSP00000020107; ENSMUSG00000019943.
DR   NMPDR; fig|10090.3.peg.22785; -.
DR   MGI; MGI:104653; Atp2b1.
DR   GeneTree; ENSGT00510000046331; -.
DR   HOGENOM; HBG456486; -.
DR   HOVERGEN; HBG061286; -.
DR   InParanoid; Q8K314; -.
DR   ArrayExpress; Q8K314; -.
DR   Bgee; Q8K314; -.
DR   Genevestigator; Q8K314; -.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005388; F:calcium-transporting ATPase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   InterPro; IPR022141; ATP_Ca_trans_C.
DR   InterPro; IPR023306; ATPase_cation_domN.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR006408; ATPase_P-typ_Ca-transp_PMCA.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Gene3D; G3DSA:3.40.1110.10; ATPase_P-typ_cyto_domN; 1.
DR   Gene3D; G3DSA:1.20.1110.10; ATPase_P-typ_TM_dom; 1.
DR   Gene3D; G3DSA:3.40.50.1000; HAD-like_dom; 1.
DR   Pfam; PF12424; ATP_Ca_trans_C; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SUPFAM; SSF81660; ATPase_cation_domN; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01517; ATPase-IIB_Ca; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Hydrolase; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Transmembrane; Transmembrane helix; Transport.
FT   NON_TER       1      1
SQ   SEQUENCE   914 AA;  101683 MW;  BB3DD518F5DBF77D CRC64;
     EKKNKKQDGA IENRNKAKAQ DGAAMEMQPL KSEEGGDGDE KDKKKANLPK KEKSVLQGKL
     TKLAVQIGKA GLLMSAITVI ILVLYFVIDT FWVQKRPWLA ECTPIYIQYF VKFFIIGVTV
     LVVAVPEGLP LAVTISLAYS VKKMMKDNNL VRHLDACETM GNATAICSDK TGTLTMNRMT
     VVQAYINEKH YKKVPEPEAI PPNILSYLVT GISVNCAYTS KILPPEKEGG LPRHVGNKTE
     CALLGFLLDL KRDYQDVRNE IPEEALYKVY TFNSVRKSMS TVLKNSDGSF RIFSKGASEI
     ILKKCFKILS ANGEAKVFRP RDRDDIVKTV IEPMASEGLR TICLAFRDFP AGEPEPEWDN
     ENDVVTGLTC IAVVGIEDPV RPEVPEAIKK CQRAGITVRM VTGDNINTAR AIATKCGILH
     PGEDFLCLEG KDFNRRIRNE KGEIEQERID KIWPKLRVLA RSSPTDKHTL VKGIIDSTVS
     EQRQVVAVTG DGTNDGPALK KADVGFAMGI AGTDVAKEAS DIILTDDNFT SIVKAVMWGR
     NVYDSISKFL QFQLTVNVVA VIVAFTGACI TQDSPLKAVQ MLWVNLIMDT LASLALATEP
     PTESLLLRKP YGRNKPLISR TMMKNILGHA FYQLVVVFTL LFAGEKFFDI DSGRNAPLHA
     PPSEHYTIVF NTFVLMQLFN EINARKIHGE RNVFEGIFNN AIFCTIVLGT FVVQIIIVQF
     GGKPFSCSEL SIEQWLWSIF LGMGTLLWGQ LISTIPTSRL KFLKEAGHGT QKEEIPEEEL
     AEDVEEIDHA ERELRRGQIL WFRGLNRIQT QIRVVNAFRS SLYEGLEKPE SRSSIHNFMT
     HPEFRIEDSE PHIPLIDDTD AEDDAPTKRN SSPPPSPNKN NNAVDSGIHL TIEMNKSATS
     SSPGSPLHSL ETSL
//
ID   ZN828_MOUSE             Reviewed;         802 AA.
AC   Q8K327; Q3UZ85; Q6ZPI1;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Zinc finger protein 828;
GN   Name=Znf828; Synonyms=D8Ertd457e, Kiaa1802, Zfp828;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-643, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416 AND SER-532, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-603, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Required for proper alignment of chromosomes at
CC       metaphase and their accurate segregation during mitosis. Involved
CC       in the maintenance of spindle microtubules attachment to the
CC       kinetochore during sister chromatid biorientation. May recruit
CC       CENPE and CENPF to the kinetochore (By similarity).
CC   -!- SUBUNIT: Interacts with MAD2L2. Interacts with POGZ, CBX1, CBX3
CC       and CBX5 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Chromosome (By
CC       similarity). Chromosome, centromere, kinetochore (By similarity).
CC       Cytoplasm, cytoskeleton, spindle (By similarity).
CC   -!- PTM: Phosphorylated by CDK1. Mitotic phosphorylation is required
CC       for the attachment of spindle microtubules to the kinetochore (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 C2H2-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98254.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK129444; BAC98254.1; ALT_INIT; mRNA.
DR   EMBL; AK132164; BAE21006.1; -; mRNA.
DR   EMBL; AK133990; BAE21972.1; -; mRNA.
DR   EMBL; AK170835; BAE42063.1; -; mRNA.
DR   EMBL; BC028991; AAH28991.1; -; mRNA.
DR   IPI; IPI00453800; -.
DR   RefSeq; NP_862902.1; NM_181854.2.
DR   UniGene; Mm.289346; -.
DR   UniGene; Mm.412576; -.
DR   ProteinModelPortal; Q8K327; -.
DR   SMR; Q8K327; 12-39, 56-86, 682-790.
DR   PhosphoSite; Q8K327; -.
DR   PRIDE; Q8K327; -.
DR   Ensembl; ENSMUST00000051870; ENSMUSP00000057270; ENSMUSG00000047710.
DR   GeneID; 101994; -.
DR   KEGG; mmu:101994; -.
DR   UCSC; uc009kyp.1; mouse.
DR   CTD; 101994; -.
DR   MGI; MGI:1196398; Zfp828.
DR   eggNOG; maNOG04222; -.
DR   GeneTree; ENSGT00440000038062; -.
DR   HOGENOM; HBG402875; -.
DR   HOVERGEN; HBG062352; -.
DR   InParanoid; Q8K327; -.
DR   OMA; IFYQKSA; -.
DR   OrthoDB; EOG4SQWW6; -.
DR   PhylomeDB; Q8K327; -.
DR   NextBio; 355222; -.
DR   ArrayExpress; Q8K327; -.
DR   Bgee; Q8K327; -.
DR   CleanEx; MM_ZFP828; -.
DR   Genevestigator; Q8K327; -.
DR   GermOnline; ENSMUSG00000047710; Mus musculus.
DR   GO; GO:0000777; C:condensed chromosome kinetochore; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0051315; P:attachment of spindle microtubules to kinetochore involved in mitotic sister chromatid segregation; ISS:UniProtKB.
DR   GO; GO:0034501; P:protein localization to kinetochore; ISS:UniProtKB.
DR   GO; GO:0035372; P:protein localization to microtubule; ISS:UniProtKB.
DR   GO; GO:0031134; P:sister chromatid biorientation; ISS:UniProtKB.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW   Kinetochore; Metal-binding; Nucleus; Phosphoprotein; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    802       Zinc finger protein 828.
FT                                /FTId=PRO_0000248320.
FT   ZN_FING     728    750       C2H2-type.
FT   REGION      261    479       Mediates interaction with MAD2L2 (By
FT                                similarity).
FT   REGION      440    580       Mediates localization to the spindle and
FT                                the kinetochore and is required for the
FT                                attachment of spindle microtubules to the
FT                                kinetochore (By similarity).
FT   REGION      581    802       Mediates localization to the chromosome
FT                                and the spindle and negatively regulates
FT                                chromosome alignment (By similarity).
FT   COMPBIAS    109    466       Pro-rich.
FT   MOD_RES     108    108       Phosphoserine (By similarity).
FT   MOD_RES     204    204       Phosphoserine (By similarity).
FT   MOD_RES     207    207       Phosphoserine (By similarity).
FT   MOD_RES     265    265       Phosphoserine (By similarity).
FT   MOD_RES     272    272       Phosphoserine (By similarity).
FT   MOD_RES     276    276       Phosphoserine (By similarity).
FT   MOD_RES     298    298       Phosphoserine (By similarity).
FT   MOD_RES     309    309       Phosphoserine.
FT   MOD_RES     365    365       Phosphoserine (By similarity).
FT   MOD_RES     375    375       Phosphoserine (By similarity).
FT   MOD_RES     394    394       Phosphoserine (By similarity).
FT   MOD_RES     405    405       Phosphoserine (By similarity).
FT   MOD_RES     416    416       Phosphoserine.
FT   MOD_RES     421    421       Phosphoserine (By similarity).
FT   MOD_RES     425    425       Phosphoserine (By similarity).
FT   MOD_RES     434    434       Phosphoserine (By similarity).
FT   MOD_RES     441    441       Phosphoserine (By similarity).
FT   MOD_RES     447    447       Phosphothreonine (By similarity).
FT   MOD_RES     448    448       Phosphoserine (By similarity).
FT   MOD_RES     451    451       Phosphoserine (By similarity).
FT   MOD_RES     479    479       N6-acetyllysine (By similarity).
FT   MOD_RES     497    497       Phosphoserine (By similarity).
FT   MOD_RES     532    532       Phosphoserine.
FT   MOD_RES     603    603       Phosphoserine.
FT   MOD_RES     606    606       Phosphoserine (By similarity).
FT   MOD_RES     617    617       Phosphoserine (By similarity).
FT   MOD_RES     622    622       Phosphoserine (By similarity).
FT   MOD_RES     623    623       Phosphoserine (By similarity).
FT   MOD_RES     641    641       Phosphoserine (By similarity).
FT   MOD_RES     642    642       Phosphoserine (By similarity).
FT   MOD_RES     643    643       Phosphoserine.
FT   MOD_RES     726    726       Phosphoserine (By similarity).
FT   CONFLICT    170    170       C -> S (in Ref. 1; BAC98254).
FT   CONFLICT    244    244       P -> T (in Ref. 1; BAC98254).
FT   CONFLICT    335    335       P -> H (in Ref. 2; BAE21972).
FT   CONFLICT    549    549       F -> L (in Ref. 1; BAC98254).
FT   CONFLICT    661    661       M -> K (in Ref. 2; BAE21972).
SQ   SEQUENCE   802 AA;  87561 MW;  D163571FE4492EA8 CRC64;
     MEVCQELRKP ALSLECGHCS FRGTDYENVQ LHMGSIHPEF CDDMDAGGLG KLIFYQKSAK
     LFHCHKCFFT SKLYANVYYH ITARHAASDK WSEQPKEQPS KDTESGKSPS PPERQNPAFD
     PAEARPTPAL PMEAQKTSPS LCPESQASGP PVLEPQGAGP LISPEPQAPC LPAEASKAAP
     VPCPERVDPP CELPELEKPE RGPSPESVKS ALVSSKPPKH SSFADTGAAP SALSPESPVL
     ATSPEPWGPS LSASPESRKP ARTASPEPRK PSPAESPELW KPFPAIASEP RRPTPAVSPG
     SWKPGPPGSP RPWKSSPSAT SGPWKSSKPV QPMSPGPWKP IPSVSPGPWK PAPSMSTASW
     KSSVSSGSWK TPPTSPESWK SGPPELRKTA LPLSPEHWKA VPPVSPELRR PGPPLSPEIR
     SPAGSPELKK PSSSPDLWKV SPDQRKTSPA SLDFPEPQKS SCGSPPDLWK SSFIMESQKP
     NVFSETRKHT ASGSSESPKV ASDIWKPVLS IDAEPRKSTL FPEPTKAVLP ASPEPRKRAL
     FPESRKHVFL PELPKSAVFS DAQKAPELSE EIQLEAVDNA KCDSLAQEGL LATPKKLLDE
     ALSPSSKKLK KDSQENSDAE LSSSEYIRAD LDTLDTKGQE SSSDQEQVDV ESIDFSKENK
     MEMGSTEQAK NVLQFTEEKE AFISEEEIAK YMKRGKGKYY CKICCCRAMK KGAVLHHLVN
     KHNVHSPYKC TICGKAFLLE SLLKNHVAAH GQSLLKCPRC NFESNFPRGF KKHLTHCQSR
     HNEEVNKKLM EALESPLEEQ QI
//
ID   SSH3_MOUSE              Reviewed;         649 AA.
AC   Q8K330; Q3UDX0;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Protein phosphatase Slingshot homolog 3;
DE            EC=3.1.3.16;
DE            EC=3.1.3.48;
DE   AltName: Full=SSH-like protein 3;
DE            Short=SSH-3L;
DE            Short=mSSH-3L;
GN   Name=Ssh3; Synonyms=Ssh3l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP   CYS-410.
RC   TISSUE=Brain;
RX   MEDLINE=22894424; PubMed=14531860;
RX   DOI=10.1046/j.1365-2443.2003.00678.x;
RA   Ohta Y., Kousaka K., Nagata-Ohashi K., Ohashi K., Muramoto A.,
RA   Shima Y., Niwa R., Uemura T., Mizuno K.;
RT   "Differential activities, subcellular distribution and tissue
RT   expression patterns of three members of Slingshot family phosphatases
RT   that dephosphorylate cofilin.";
RL   Genes Cells 8:811-824(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-582 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-38 AND SER-639,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Protein phosphatase which may play a role in the
CC       regulation of actin filament dynamics. Can dephosphorylate and
CC       activate the actin binding/depolymerizing factor cofilin, which
CC       subsequently binds to actin filaments and stimulates their
CC       disassembly.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- SUBUNIT: Does not bind to, or colocalize with, filamentous actin.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K330-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K330-2; Sequence=VSP_016337;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, small intestine and
CC       testis. Also expressed at lower levels in heart, kidney, liver,
CC       spleen and thymus.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the nervous system and
CC       epithelial tissues of the trachea at E14.5.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- MISCELLANEOUS: Tyrosine phosphatase activity has not been
CC       demonstrated for this protein to date.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AB099289; BAC97812.1; -; mRNA.
DR   EMBL; BC028922; AAH28922.1; -; mRNA.
DR   EMBL; AK149880; BAE29141.1; -; mRNA.
DR   IPI; IPI00356992; -.
DR   IPI; IPI00656268; -.
DR   RefSeq; NP_932781.1; NM_198113.2.
DR   UniGene; Mm.248388; -.
DR   ProteinModelPortal; Q8K330; -.
DR   SMR; Q8K330; 325-466.
DR   STRING; Q8K330; -.
DR   PhosphoSite; Q8K330; -.
DR   PRIDE; Q8K330; -.
DR   Ensembl; ENSMUST00000037992; ENSMUSP00000047718; ENSMUSG00000034616.
DR   Ensembl; ENSMUST00000113852; ENSMUSP00000109483; ENSMUSG00000034616.
DR   GeneID; 245857; -.
DR   KEGG; mmu:245857; -.
DR   UCSC; uc008fzo.1; mouse.
DR   CTD; 245857; -.
DR   MGI; MGI:2683546; Ssh3.
DR   eggNOG; roNOG12429; -.
DR   GeneTree; ENSGT00590000082789; -.
DR   HOVERGEN; HBG089321; -.
DR   OMA; VSHILNM; -.
DR   OrthoDB; EOG4WDDBT; -.
DR   PhylomeDB; Q8K330; -.
DR   BRENDA; 3.1.3.16; 244.
DR   BRENDA; 3.1.3.48; 244.
DR   NextBio; 386960; -.
DR   ArrayExpress; Q8K330; -.
DR   Bgee; Q8K330; -.
DR   CleanEx; MM_SSH3; -.
DR   Genevestigator; Q8K330; -.
DR   GermOnline; ENSMUSG00000034616; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   InterPro; IPR014876; DEK_C.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR020422; Dual-sp_phosphatase_subgr_cat.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   Pfam; PF08766; DEK_C; 1.
DR   Pfam; PF00782; DSPc; 1.
DR   SMART; SM00195; DSPc; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Cytoskeleton; Hydrolase; Nucleus;
KW   Phosphoprotein; Protein phosphatase.
FT   CHAIN         1    649       Protein phosphatase Slingshot homolog 3.
FT                                /FTId=PRO_0000094846.
FT   DOMAIN      325    465       Tyrosine-protein phosphatase.
FT   ACT_SITE    410    410       Phosphocysteine intermediate (Probable).
FT   MOD_RES       7      7       Phosphoserine.
FT   MOD_RES       9      9       Phosphoserine.
FT   MOD_RES      38     38       Phosphoserine.
FT   MOD_RES      88     88       Phosphoserine (By similarity).
FT   MOD_RES     639    639       Phosphoserine.
FT   MOD_RES     643    643       Phosphoserine (By similarity).
FT   VAR_SEQ     261    261       Q -> QITTR (in isoform 2).
FT                                /FTId=VSP_016337.
FT   MUTAGEN     410    410       C->S: Abrogates phosphatase activity.
FT   CONFLICT     74     74       Q -> R (in Ref. 3; BAE29141).
SQ   SEQUENCE   649 AA;  72227 MW;  DF8628B5E007E6F0 CRC64;
     MALVTVSRSP PASGHSTPVG PTQDRVVRRR GRLQRRQSFA VLRGAVLGLQ DGGDSNVASE
     ADSEPMEEPS GEEQPTEDQT DKGQGLQSPW KQVQKRHLHL MVELLRPQDD IRLAAQLEAA
     RPPRLRYLLV VSTGEELSEE AILLGVDFPD SSSHSCTLGL VLPLWSDTQV YLDGDGGFSV
     TSGGQSRIFK PVSIQTMWAT LQVLHQACEV ALGSGLVPGG SALAWATYYQ EKLNSDQGCL
     NEWMAMSDLE SFRPPNAEPG QASEQEKMEQ AILAELWQVL DTSDLDSVTS KEIRQALELR
     LGCPLQQYRD FIDNQMLLLM AQQDRASRIF PHLYLGSEWN AANLEELQKN RVSHILNMAR
     EIDNFFPERF TYYNVRVWDE ESAQLLPHWK ETHRFIEDAR AQGTRVLVHC KMGVSRSAAT
     VLAYAMKQYG WDLEQALIHV QELRPIVRPN HGFLRQLRTY QGILTASRQS HVWEQKVGVV
     SPEEPLAPEV STPLPPLPPE PGGSGEVMVM GLEGSQETPK EELGLRPRIN LRGVMRSISL
     LEPSESESTP EAGGLPEVFS SDEEPLHPFS QLSRAKGGQR VRKGPWPALK SRQSVVALHS
     AALVASRTRA FQEQGQGQEQ SEPGMSSTPR LRKVMRQASV DDSREEDKA
//
ID   Q8K337_MOUSE            Unreviewed;       993 AA.
AC   Q8K337;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   SubName: Full=Inositol polyphosphate-5-phosphatase B;
GN   Name=Inpp5b; ORFNames=RP23-168M5.1-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N;
RC   TISSUE=Mammary tumor. Metallothionien-TGF alpha model. 10 month old
RC   virgin mouse. Taken by biopsy.;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Hammond S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC028864; AAH28864.1; -; mRNA.
DR   EMBL; AL606933; CAM16097.1; -; Genomic_DNA.
DR   EMBL; AL606907; CAM16097.1; JOINED; Genomic_DNA.
DR   IPI; IPI00120070; -.
DR   RefSeq; NP_032411.3; NM_008385.3.
DR   UniGene; Mm.296202; -.
DR   PDB; 2KIG; NMR; -; A=1-156.
DR   PDBsum; 2KIG; -.
DR   ProteinModelPortal; Q8K337; -.
DR   SMR; Q8K337; 325-664, 673-992.
DR   STRING; Q8K337; -.
DR   PhosphoSite; Q8K337; -.
DR   Ensembl; ENSMUST00000094782; ENSMUSP00000092375; ENSMUSG00000028894.
DR   GeneID; 16330; -.
DR   KEGG; mmu:16330; -.
DR   UCSC; uc008uqy.1; mouse.
DR   CTD; 16330; -.
DR   MGI; MGI:103257; Inpp5b.
DR   HOVERGEN; HBG000070; -.
DR   NextBio; 289414; -.
DR   ArrayExpress; Q8K337; -.
DR   Bgee; Q8K337; -.
DR   Genevestigator; Q8K337; -.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IDA:MGI.
DR   GO; GO:0004437; F:inositol or phosphatidylinositol phosphatase activity; IEA:InterPro.
DR   GO; GO:0070613; P:regulation of protein processing; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0030317; P:sperm motility; IMP:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   InterPro; IPR000300; IPPc.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00128; IPPc; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF56219; Exo_endo_phos; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
SQ   SEQUENCE   993 AA;  112762 MW;  C15670755B562878 CRC64;
     MDQSVAIQET LVEGEYCVIA VQGVLCKGDS RQSRLLGLVR YRLENDAQEH ALFLYTHRRM
     AITGDDVSLD QIVPLSKDFM LEEVSPDGEL YILGSDVTVQ LNTAELKLVF QLPFGSHTRT
     FLQEVARACP GFDPETRDPE FEWLSRHTCA EPDAESPKPR EWNSDPGTRS GFAPIGGSRH
     QSRNARRGLE DVLPRGPGYI LLWGGAAEEP EFLLAEEMHE GGPVRGRRPL AGRRDEALEE
     ADWEMSAGGG SRERDCAGVS NVDSSRPNGR GPDQPSGARC PEKPENSLTR QNKSKSDMSE
     KVRSATVTVS DKAHILSVQK FGLRDTIVRS HLVQKEENYT YIQNFRFFVG TYNVNGQSPK
     ECLRPWLSHS ALAPDVYCVG FQELDLSKEA FFFHDTPKEE EWFKAVSESL HPDAKYAKVK
     FVRLVGIMLL LYVKQEHAAY ISEVEAETVG TGIMGRMGNK GGVAIRFQLH NTSICVVNSH
     LAAHTEEYER RNQDYRDICS RMQFPQVDPS QPPLTINKHD VILWLGDLNY RIEELDVGKV
     KKLVEEKAFQ TLYAHDQLKI QVAARTIFDG FTEGEITFQP TYKYDTGSDD WDTSEKCRAP
     AWCDRILWKG KNITQLSYQS HMALKTSDHK PVSSVFDIGV RVVNEELYRK TLEEIVRSLD
     KMENANIPSV TLSKREFCFE NVKYMQLQTE SFTIHNSQVP CQFEFINKPD EESYCKQWLT
     ARPSKGFLLP DSHVEIELEL FVNKSTATKL NSGKDTIEDI LVLHLERGKD YFLSVSGNYL
     PSCFGSPIHT LCYMREPILD LPLKTVSDLT LMSVQTADDR SQLENPMEIP KELWMMVDYL
     YRNAVQQEDL FQQPGLRPEF DHIRDCLDTG MIDQLCANNH SVAEALLLFL ESLPEPVICY
     SAYHSCLECS GNYAASKQII LTLPSFHKNV FNYLMAFLQE LLKNSANNHL DENILASIFG
     SLLLRNPARH QKLDMAEKKK AQEFIHQFLC GPL
//
ID   ATAT_MOUSE              Reviewed;         421 AA.
AC   Q8K341; B8JJ75; B8JJ77; Q3UZR9; Q8BM67; Q8C1D1; Q8K2M7;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 44.
DE   RecName: Full=Alpha-tubulin N-acetyltransferase;
DE            Short=Alpha-TAT;
DE            Short=TAT;
DE            EC=2.3.1.108;
DE   AltName: Full=Acetyltransferase MEC-17;
GN   Name=Atat1; Synonyms=Mec17;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4 AND 5).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Embryonic head, and Pituitary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and Czech II;
RC   TISSUE=Mammary gland, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION.
RX   PubMed=20829795; DOI=10.1038/nature09324;
RA   Akella J.S., Wloga D., Kim J., Starostina N.G., Lyons-Abbott S.,
RA   Morrissette N.S., Dougan S.T., Kipreos E.T., Gaertig J.;
RT   "MEC-17 is an alpha-tubulin acetyltransferase.";
RL   Nature 467:218-222(2010).
CC   -!- FUNCTION: Specifically acetylates 'Lys-40' in alpha-tubulin on the
CC       lumenal side of microtubules. May affect microtubule stability and
CC       regulate microtubule dynamics. May be involved in neuron
CC       development.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + [alpha-tubulin]-L-lysine = CoA +
CC       [alpha-tubulin]-N(6)-acetyl-L-lysine.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q8K341-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K341-2; Sequence=VSP_052905;
CC       Name=3;
CC         IsoId=Q8K341-3; Sequence=VSP_052908, VSP_052909;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q8K341-4; Sequence=VSP_052906, VSP_052907;
CC       Name=5;
CC         IsoId=Q8K341-5; Sequence=VSP_052905, VSP_052906, VSP_052907;
CC   -!- SIMILARITY: Belongs to the acetyltransferase ATAT1 family.
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DR   EMBL; AK028297; BAC25866.1; -; mRNA.
DR   EMBL; AK034725; BAC28808.1; -; mRNA.
DR   EMBL; AK133694; BAE21786.1; -; mRNA.
DR   EMBL; CR974451; CAX15764.1; -; Genomic_DNA.
DR   EMBL; CR974451; CAX15766.1; -; Genomic_DNA.
DR   EMBL; BC028847; AAH28847.1; -; mRNA.
DR   EMBL; BC030669; AAH30669.1; -; mRNA.
DR   IPI; IPI00230368; -.
DR   IPI; IPI00263903; -.
DR   IPI; IPI00322313; -.
DR   IPI; IPI00404416; -.
DR   IPI; IPI00903416; -.
DR   RefSeq; NP_001136216.1; NM_001142744.1.
DR   RefSeq; NP_001136217.1; NM_001142745.1.
DR   RefSeq; NP_082752.3; NM_028476.4.
DR   UniGene; Mm.273155; -.
DR   ProteinModelPortal; Q8K341; -.
DR   PRIDE; Q8K341; -.
DR   Ensembl; ENSMUST00000061052; ENSMUSP00000056383; ENSMUSG00000024426.
DR   GeneID; 73242; -.
DR   KEGG; mmu:73242; -.
DR   UCSC; uc008cja.1; mouse.
DR   CTD; 73242; -.
DR   MGI; MGI:1913869; Atat1.
DR   GeneTree; ENSGT00390000008276; -.
DR   HOGENOM; HBG282052; -.
DR   HOVERGEN; HBG055797; -.
DR   InParanoid; Q8K341; -.
DR   OMA; GNSPDRG; -.
DR   OrthoDB; EOG40GCR7; -.
DR   PhylomeDB; Q8K341; -.
DR   ArrayExpress; Q8K341; -.
DR   Bgee; Q8K341; -.
DR   Genevestigator; Q8K341; -.
DR   GO; GO:0019799; F:tubulin N-acetyltransferase activity; IDA:UniProtKB.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR007965; Touch_recpt_neuron_Mec-17.
DR   Gene3D; G3DSA:3.40.630.30; Acyl_CoA_acyltransferase; 1.
DR   PANTHER; PTHR12327; DUF738; 1.
DR   Pfam; PF05301; DUF738; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Transferase.
FT   CHAIN         1    421       Alpha-tubulin N-acetyltransferase.
FT                                /FTId=PRO_0000348067.
FT   MOD_RES     233    233       N6-acetyllysine (By similarity).
FT   VAR_SEQ     195    218       RPPTSSLRATRHSRAAVADPIPAA -> P (in isoform
FT                                2 and isoform 5).
FT                                /FTId=VSP_052905.
FT   VAR_SEQ     323    333       RGTPWGLVAQS -> SSLPRSDESRY (in isoform 4
FT                                and isoform 5).
FT                                /FTId=VSP_052906.
FT   VAR_SEQ     324    353       GTPWGLVAQSCHYSRHGGFNTSFLGTGNQE -> SHTHTTT
FT                                VSLDAWYFHRQPRTEAGGTGSGG (in isoform 3).
FT                                /FTId=VSP_052908.
FT   VAR_SEQ     334    421       Missing (in isoform 4 and isoform 5).
FT                                /FTId=VSP_052907.
FT   VAR_SEQ     354    421       Missing (in isoform 3).
FT                                /FTId=VSP_052909.
FT   CONFLICT     92     92       A -> V (in Ref. 3; AAH30669).
FT   CONFLICT    102    102       K -> E (in Ref. 1; BAC28808).
SQ   SEQUENCE   421 AA;  47164 MW;  E47F1060F183D19C CRC64;
     MEFPFDVDAL FPERITVLDQ HLRPPARRPG TTTPARVDLQ QQIMTIVDEL GKASAKAQHL
     PAPITSALRM QSNRHVIYIL KDTSARPAGK GAIIGFLKVG YKKLFVLDDR EAHNEVEPLC
     ILDFYIHESV QRHGHGRELF QHMLQKERVE PHQLAIDRPS PKLLKFLNKH YNLETTVPQV
     NNFVIFEGFF AHQHRPPTSS LRATRHSRAA VADPIPAAPA RKLPPKRAEG DIKPYSSSDR
     EFLKVAVEPP WPLNRAPRRA TPPAHPPPRS SSLGNSPDRG PLRPFVPEQE LLRSLRLCPP
     HPTARLLLAT DPGGSPAQRR RTRGTPWGLV AQSCHYSRHG GFNTSFLGTG NQERKQGEQE
     AEDRSASEDR VLLLDGSGEE PTQTGAPRAQ APPPQSWTVG GDIMNARVIR NLQERRSTRP
     W
//
ID   DEN1A_MOUSE             Reviewed;        1016 AA.
AC   Q8K382; A0MCI0; A2ALU2;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=DENN domain-containing protein 1A;
DE   AltName: Full=Connecdenn 1;
DE            Short=Connecdenn;
GN   Name=Dennd1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH AP2B1; ITSN1 AND SH3GL2,
RP   AND FUNCTION.
RC   STRAIN=FVB/N;
RX   PubMed=17182770; DOI=10.1523/JNEUROSCI.4608-06.2006;
RA   Allaire P.D., Ritter B., Thomas S., Burman J.L., Denisov A.Y.,
RA   Legendre-Guillemin V., Harper S.Q., Davidson B.L., Gehring K.,
RA   McPherson P.S.;
RT   "Connecdenn, a novel DENN domain-containing protein of neuronal
RT   clathrin-coated vesicles functioning in synaptic vesicle
RT   endocytosis.";
RL   J. Neurosci. 26:13202-13212(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Guanine nucleotide exchange factor (GEF) for RAB35 (By
CC       similarity). May be involved in the clathrin-mediated endocytosis
CC       of synaptic vesicles.
CC   -!- SUBUNIT: Interacts with RAB35 in the absence of nucleotide, but
CC       not in the presence of GTP (By similarity). Interacts with
CC       clathrin heavy chain/CLTC and with AP2A2, but not with AP2B1 (By
CC       similarity). Interacts with AP2B1, ITSN1 AND SH3GL2.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, presynaptic cell
CC       membrane; Peripheral membrane protein. Cytoplasmic vesicle,
CC       clathrin-coated vesicle membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Contains 1 dDENN domain.
CC   -!- SIMILARITY: Contains 1 DENN domain.
CC   -!- SIMILARITY: Contains 1 uDENN domain.
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DR   EMBL; DQ448594; ABD93329.1; -; mRNA.
DR   EMBL; AL805959; CAM22966.1; -; Genomic_DNA.
DR   EMBL; AL928810; CAM22966.1; JOINED; Genomic_DNA.
DR   EMBL; AL929186; CAM22966.1; JOINED; Genomic_DNA.
DR   EMBL; AL929238; CAM22966.1; JOINED; Genomic_DNA.
DR   EMBL; AL929186; CAM23322.1; -; Genomic_DNA.
DR   EMBL; AL805959; CAM23322.1; JOINED; Genomic_DNA.
DR   EMBL; AL928810; CAM23322.1; JOINED; Genomic_DNA.
DR   EMBL; AL929238; CAM23322.1; JOINED; Genomic_DNA.
DR   EMBL; AL929238; CAM25676.1; -; Genomic_DNA.
DR   EMBL; AL805959; CAM25676.1; JOINED; Genomic_DNA.
DR   EMBL; AL928810; CAM25676.1; JOINED; Genomic_DNA.
DR   EMBL; AL929186; CAM25676.1; JOINED; Genomic_DNA.
DR   EMBL; AL928810; CAM26757.1; -; Genomic_DNA.
DR   EMBL; AL805959; CAM26757.1; JOINED; Genomic_DNA.
DR   EMBL; AL929186; CAM26757.1; JOINED; Genomic_DNA.
DR   EMBL; AL929238; CAM26757.1; JOINED; Genomic_DNA.
DR   EMBL; BC027786; AAH27786.1; -; mRNA.
DR   IPI; IPI00322415; -.
DR   RefSeq; NP_666234.3; NM_146122.3.
DR   UniGene; Mm.314245; -.
DR   UniGene; Mm.461078; -.
DR   PhosphoSite; Q8K382; -.
DR   PRIDE; Q8K382; -.
DR   Ensembl; ENSMUST00000102787; ENSMUSP00000099848; ENSMUSG00000035392.
DR   GeneID; 227801; -.
DR   KEGG; mmu:227801; -.
DR   UCSC; uc008jng.1; mouse.
DR   CTD; 227801; -.
DR   MGI; MGI:2442794; Dennd1a.
DR   eggNOG; roNOG13752; -.
DR   GeneTree; ENSGT00550000074339; -.
DR   HOGENOM; HBG506118; -.
DR   HOVERGEN; HBG059210; -.
DR   InParanoid; Q8K382; -.
DR   OMA; STPAGPF; -.
DR   OrthoDB; EOG4NP72W; -.
DR   PhylomeDB; Q8K382; -.
DR   NextBio; 378840; -.
DR   ArrayExpress; Q8K382; -.
DR   Bgee; Q8K382; -.
DR   CleanEx; MM_DENND1A; -.
DR   Genevestigator; Q8K382; -.
DR   GermOnline; ENSMUSG00000035392; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0030665; C:clathrin coated vesicle membrane; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0017124; F:SH3 domain binding; IPI:MGI.
DR   GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:MGI.
DR   InterPro; IPR005112; dDENN.
DR   InterPro; IPR001194; DENN.
DR   InterPro; IPR005113; uDENN.
DR   Pfam; PF03455; dDENN; 1.
DR   Pfam; PF02141; DENN; 1.
DR   Pfam; PF03456; uDENN; 1.
DR   SMART; SM00801; dDENN; 1.
DR   SMART; SM00799; DENN; 1.
DR   SMART; SM00800; uDENN; 1.
DR   PROSITE; PS50947; DDENN; 1.
DR   PROSITE; PS50211; DENN; 1.
DR   PROSITE; PS50946; UDENN; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Cytoplasmic vesicle;
KW   Guanine-nucleotide releasing factor; Membrane; Phosphoprotein;
KW   Synapse.
FT   CHAIN         1   1016       DENN domain-containing protein 1A.
FT                                /FTId=PRO_0000242681.
FT   DOMAIN       24     91       UDENN.
FT   DOMAIN       92    273       DENN.
FT   DOMAIN      304    371       dDENN.
FT   COMPBIAS    649   1000       Pro-rich.
FT   MOD_RES     394    394       Phosphotyrosine (By similarity).
FT   MOD_RES     519    519       Phosphothreonine (By similarity).
FT   MOD_RES     520    520       Phosphoserine (By similarity).
FT   MOD_RES     523    523       Phosphoserine (By similarity).
FT   MOD_RES     536    536       Phosphoserine (By similarity).
FT   MOD_RES     538    538       Phosphoserine (By similarity).
FT   MOD_RES     546    546       Phosphoserine (By similarity).
FT   MOD_RES     592    592       Phosphoserine.
FT   CONFLICT    152    152       H -> Y (in Ref. 1; ABD93329 and 3;
FT                                AAH27786).
SQ   SEQUENCE   1016 AA;  111538 MW;  352A1A6F940D7382 CRC64;
     MGSRIKQNPE TTFEVYVEVA YPRTGGTLSD PEVQRQFPED YSDQEVLQTL TKFCFPFYVD
     SLTVSQVGQN FTFVLTDIDS KQRFGFCRLS SGAKSCFCIL SYLPWFEVFY KLLNILADYT
     TKRQESQWNE LLETLHRLPI PDPGVSVHLS VHSYFTVPDS RELPSIPENR NLTEYFVAVD
     VNNMLHLYAS MLYERRILII CSKLSTLTAC IHGSAAMLYP MYWQHVYIPV LPPHLLDYCC
     APMPYLIGIH LSLMEKVRNM ALDDVVILNV DTNTLETPFD DLQSLPNDVI SSLKNRLKKV
     STTTGDGVAR AFLKAQAAFF GSYRNALKIE PEEPITFSEE AFVSHYRSGA MKQFLQNATQ
     LQLFKQFIDG RLDLLNSGEG FSDVFEEEIN MGEYAGSDKL YHQWLSTVRK GSGAILNTVK
     TKANPAMKTV YKFAKDHAKM GIKEVKNRLK QKDITENGCV SSAEDPLPKT MPSPQAETQD
     PRLREDRRPI TVHFGQVRPP RPHVVRRPKS NITVEGRRTS VSSPEQPQPY RTLKESDSAE
     GDETESPEQL VREPWGPTPA PPDRAASIDL LEDVFSSLDV EAPLQPLGQA KSLEDLRAPK
     DLREQPGSFD YQRLDLCRSE RGLSMAAALK LAHPYTKLWS LGQDDMAIPS KPSITSPEKP
     SALLGTSPAL PLRPQNQEGI LSPSIKEETP IPTPGSITIP RPQGRKTPEL GIVPPPPTAR
     PAKLQAAGGP LGDFSSEPLQ MDRERQAALS PALLSGLLPR AVPQGPTELL QPPSPAPGAA
     GTGSDALLAL LDPLNTAWSG STIPSHPATP SAATPFIPQL SFPPTVTPTP FVQTPLNPFV
     PSVPVVPPSM PLSSTPARPF GTPPASLGPA YAPSILLSSS GFYAPHRSQP NLSALSMPNL
     FGQIPMGAHT SPLQPLGPPA VAPSRIRTLP LARSSARAAE AKQGLALRPG ESPLLPPRPP
     QSLQPTPQPS VPTQARDPFE DLLRKTKQDV SPSPAPALAP ASTSVEQLRR QWETFE
//
ID   PLCL2_MOUSE             Reviewed;        1128 AA.
AC   Q8K394; Q3U4E2; Q80TK5; Q9QYG1;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Inactive phospholipase C-like protein 2;
DE            Short=PLC-L(2);
DE            Short=PLC-L2;
DE            Short=Phospholipase C-L2;
DE   AltName: Full=Phospholipase C-epsilon-2;
DE            Short=PLC-epsilon-2;
GN   Name=Plcl2; Synonyms=Kiaa1092, Plce2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP   AND FUNCTION.
RX   MEDLINE=20050058; PubMed=10581172; DOI=10.1006/bbrc.1999.1784;
RA   Otsuki M., Fukami K., Kohno T., Yokota J., Takenawa T.;
RT   "Identification and characterization of a new phospholipase C-like
RT   protein, PLC-L(2).";
RL   Biochem. Biophys. Res. Commun. 266:97-103(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 240-1128.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1114, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: May play an role in the regulation of Ins(1,4,5)P3
CC       around the endoplasmic reticulum.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Predominantly localized to
CC       perinuclear areas in both myoblast and myotube C2C12 cells.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed, with a strong
CC       expression in skeletal muscle.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 PI-PLC X-box domain.
CC   -!- SIMILARITY: Contains 1 PI-PLC Y-box domain.
CC   -!- CAUTION: The PI-PLC X-box lacks the essential His at position 487
CC       which is replaced by a Thr and is predicted to be inactive.
CC   -----------------------------------------------------------------------
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DR   EMBL; AB033615; BAA89457.1; -; mRNA.
DR   EMBL; AK154288; BAE32490.1; -; mRNA.
DR   EMBL; BC027746; AAH27746.1; -; mRNA.
DR   EMBL; AK122439; BAC65721.1; -; mRNA.
DR   IPI; IPI00322431; -.
DR   RefSeq; NP_038908.2; NM_013880.3.
DR   UniGene; Mm.217362; -.
DR   HSSP; P10688; 1QAS.
DR   ProteinModelPortal; Q8K394; -.
DR   SMR; Q8K394; 137-888.
DR   STRING; Q8K394; -.
DR   PhosphoSite; Q8K394; -.
DR   PRIDE; Q8K394; -.
DR   Ensembl; ENSMUST00000043938; ENSMUSP00000046584; ENSMUSG00000038910.
DR   GeneID; 224860; -.
DR   KEGG; mmu:224860; -.
DR   UCSC; uc008cyx.1; mouse.
DR   CTD; 224860; -.
DR   MGI; MGI:1352756; Plcl2.
DR   eggNOG; roNOG12324; -.
DR   GeneTree; ENSGT00570000078720; -.
DR   HOGENOM; HBG527074; -.
DR   HOVERGEN; HBG108265; -.
DR   InParanoid; Q8K394; -.
DR   OMA; AMEFHEN; -.
DR   OrthoDB; EOG4N8R3Z; -.
DR   PhylomeDB; Q8K394; -.
DR   NextBio; 377425; -.
DR   ArrayExpress; Q8K394; -.
DR   Bgee; Q8K394; -.
DR   CleanEx; MM_PLCL2; -.
DR   Genevestigator; Q8K394; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:InterPro.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR015359; Phospholipase_C_EF-hand-like.
DR   InterPro; IPR001711; Phospholipase_C_Pinositol-sp_Y.
DR   InterPro; IPR001192; Pinositol_Phospholipase-C.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:3.20.20.190; PLC-like_Pdiesterase_TIM-brl; 2.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF09279; efhand_like; 1.
DR   Pfam; PF00388; PI-PLC-X; 1.
DR   Pfam; PF00387; PI-PLC-Y; 1.
DR   PRINTS; PR00390; PHPHLIPASEC.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00148; PLCXc; 1.
DR   SMART; SM00149; PLCYc; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF51695; PLC-like_Pdiesterase_TIM-brl; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Phosphoprotein; Transducer.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1128       Inactive phospholipase C-like protein 2.
FT                                /FTId=PRO_0000288852.
FT   DOMAIN      142    252       PH.
FT   DOMAIN      427    571       PI-PLC X-box.
FT   DOMAIN      619    735       PI-PLC Y-box.
FT   DOMAIN      742    847       C2.
FT   COMPBIAS      5     79       Gly-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      15     15       Phosphothreonine (By similarity).
FT   MOD_RES      16     16       Phosphoserine (By similarity).
FT   MOD_RES      18     18       Phosphoserine.
FT   MOD_RES     585    585       Phosphothreonine (By similarity).
FT   MOD_RES    1114   1114       Phosphoserine.
FT   CONFLICT    142    142       N -> H (in Ref. 1; BAA89457).
FT   CONFLICT    273    273       I -> V (in Ref. 3; AAH27746).
FT   CONFLICT    340    340       C -> R (in Ref. 1; BAA89457).
FT   CONFLICT    449    449       D -> N (in Ref. 2; BAE32490).
FT   CONFLICT    485    485       I -> V (in Ref. 1; BAA89457).
FT   CONFLICT    797    798       EQ -> AD (in Ref. 1; BAA89457).
SQ   SEQUENCE   1128 AA;  125772 MW;  08066A8C023E7935 CRC64;
     MAECGRGAAG GALPTSPSPA LGAKGALKAG AGEGGGGGGG GRLGHGRARY DSGGVSNGDC
     SLGVSGDEAR TSPGRGPLGV ALARTPSPAA GPVPRDSKPG GLPRRSSIIK DGTKQKRERK
     KTVSFSSMPT EKKISSASDC INSMVEGSEL KKVRSNSRIY HRYFLLDADM QSLRWEPSKK
     DSEKAKIDIK SIKEVRTGKN TDIFRSNGIS EQISEDCAFS VIYGENYESL DLVANSADVA
     NIWVTGLRYL ISYGKHTLDM LESSQDNMRT SWISQMFSEI DVDGLGHITL CHAVQCIRNL
     NPGLKTSKIE LKFKELHKSK DKAGTEITKE EFIEVFHELC TRPEIYFLLV QFSSNKEFLD
     TKDLMMFLEA EQGVAHINEE ISLEIIHKYE PSKEGQEKGW LSIDGFTNYL MSPDCYIFDP
     EHKKVCQDMK QPLSHYFINS SHNTYLIEDQ FRGPSDITGY IRALKMGCRS VELDVWDGPD
     NEPVIYTGHT MTSQIVFRSV IDIINKYAFF ASEYPLILCL ENHCSIKQQK VMVQHMKKIL
     GDKLYTTSPN MEESYLPSPD VLKGKILIKA KKLSSNCSGV EGDVTDEDEG AEMSQRMGKE
     NVEQPNHVPV KRFQLCKELS ELVSICKSVQ FKEFQVSFQV QKYWEVCSFN EVLASKYANE
     NPGDFVNYNK RFLARVFPSP MRIDSSNMNP QDFWKCGCQI VAMNFQTPGL MMDLNVGWFR
     QNGNCGYVLR PAIMREEVSF FSANTKDSVP GVSPQLLHIK IISGQNFPKP KGSGAKGDVV
     DPYVYVEIHG IPADCAEQRT KTVNQNGDAP IFDESFEFQI NLPELAMVRF VVLDDDYIGD
     EFIGQYTIPF ECLQTGYRHV PLQSLTGEVL AHASLFVHVA ITNRRGGGKP HKRGLSVRKG
     KKSREYASLR TLWIKTVDEV FKNAQPPIRD ATDLRENMQN AVVSFKELCG LSSVANLMQC
     MLAVSPRFLG PDNNPLVVLN LSEPYPTMEL QAIVPEVLKK IVTTYDMMMQ SLKALIENAD
     AVYEKIVHCQ KAAMEFHEHL HSIGTKEGLK ERKLQKAVES FTWNITILKG QADLLKYAKN
     ETLENLKQIH FAAVSCGLNK PGTENSEAQK PRRSLEAIPE KASDENGD
//
ID   AHI1_MOUSE              Reviewed;        1047 AA.
AC   Q8K3E5; Q7TNV2; Q9CVY1;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Jouberin;
DE   AltName: Full=Abelson helper integration site 1 protein;
DE            Short=AHI-1;
GN   Name=Ahi1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=C3H;
RX   PubMed=12186888; DOI=10.1128/JVI.76.18.9046-9059.2002;
RA   Jiang X., Hanna Z., Kaouass M., Girard L., Jolicoeur P.;
RT   "Ahi-1, a novel gene encoding a modular protein with WD40-repeat and
RT   SH3 domains, is targeted by the Ahi-1 and Mis-2 provirus
RT   integrations.";
RL   J. Virol. 76:9046-9059(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-322.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=15467982; DOI=10.1086/425985;
RA   Dixon-Salazar T., Silhavy J.L., Marsh S.E., Louie C.M., Scott L.C.,
RA   Gururaj A., Al-Gazali L., Al-Tawari A.A., Kayserili H., Sztriha L.,
RA   Gleeson J.G.;
RT   "Mutations in the AHI1 gene, encoding jouberin, cause Joubert syndrome
RT   with cortical polymicrogyria.";
RL   Am. J. Hum. Genet. 75:979-987(2004).
RN   [5]
RP   INTERACTION WITH NPHP1, AND SUBCELLULAR LOCATION.
RX   PubMed=18633336; DOI=10.1038/ki.2008.377;
RA   Eley L., Gabrielides C., Adams M., Johnson C.A., Hildebrandt F.,
RA   Sayer J.A.;
RT   "Jouberin localizes to collecting ducts and interacts with
RT   nephrocystin-1.";
RL   Kidney Int. 74:1139-1149(2008).
CC   -!- SUBUNIT: Interacts with NPHP1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body.
CC       Cell junction, adherens junction (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K3E5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K3E5-2; Sequence=VSP_015357, VSP_015358;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in the brain and testis.
CC       Weakly expressed in the liver. Strongly expressed during periods
CC       of both cortical and cerebellar development.
CC   -!- DEVELOPMENTAL STAGE: First detected at embryonic days 7 (E7) and
CC       is also present at E11, E15 and E17 with the most high level at
CC       E15. Expression in whole brain is detected from E14 to adult.
CC       Expression in cerebellum appears maximal at E18 and postnatal days
CC       5 (P5), whereas expression in cerebral cortex appears maximal at
CC       E16 and E18.
CC   -!- MISCELLANEOUS: Is targeted by provirus integrations. This
CC       deregulation contributes to tumor development.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SIMILARITY: Contains 7 WD repeats.
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DR   EMBL; AY133241; AAM94175.1; -; mRNA.
DR   EMBL; BC055400; AAH55400.1; -; mRNA.
DR   EMBL; AK005991; BAB24355.1; -; mRNA.
DR   IPI; IPI00170079; -.
DR   IPI; IPI00649381; -.
DR   UniGene; Mm.253280; -.
DR   ProteinModelPortal; Q8K3E5; -.
DR   SMR; Q8K3E5; 450-769, 903-958.
DR   STRING; Q8K3E5; -.
DR   PhosphoSite; Q8K3E5; -.
DR   PRIDE; Q8K3E5; -.
DR   Ensembl; ENSMUST00000095801; ENSMUSP00000093480; ENSMUSG00000019986.
DR   Ensembl; ENSMUST00000105525; ENSMUSP00000101164; ENSMUSG00000019986.
DR   UCSC; uc007eod.1; mouse.
DR   MGI; MGI:87971; Ahi1.
DR   GeneTree; ENSGT00530000063479; -.
DR   HOGENOM; HBG713012; -.
DR   HOVERGEN; HBG080824; -.
DR   InParanoid; Q8K3E5; -.
DR   OrthoDB; EOG4548XS; -.
DR   ArrayExpress; Q8K3E5; -.
DR   Bgee; Q8K3E5; -.
DR   CleanEx; MM_AHI1; -.
DR   Genevestigator; Q8K3E5; -.
DR   GermOnline; ENSMUSG00000019986; Mus musculus.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR   GO; GO:0005932; C:microtubule basal body; IEA:UniProtKB-SubCell.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF00400; WD40; 5.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50044; SH3; 1.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell projection; Cilium;
KW   Cytoplasm; Cytoskeleton; Phosphoprotein; Repeat; SH3 domain;
KW   WD repeat.
FT   CHAIN         1   1047       Jouberin.
FT                                /FTId=PRO_0000050839.
FT   REPEAT      457    499       WD 1.
FT   REPEAT      502    541       WD 2.
FT   REPEAT      545    585       WD 3.
FT   REPEAT      592    631       WD 4.
FT   REPEAT      648    687       WD 5.
FT   REPEAT      691    730       WD 6.
FT   REPEAT      735    776       WD 7.
FT   DOMAIN      902    962       SH3.
FT   COMPBIAS     87     94       Poly-Lys.
FT   MOD_RES     974    974       Phosphoserine (By similarity).
FT   VAR_SEQ     994   1005       QSLSKGRPLDPR -> GGHEEETKSQTN (in isoform
FT                                2).
FT                                /FTId=VSP_015357.
FT   VAR_SEQ    1006   1047       Missing (in isoform 2).
FT                                /FTId=VSP_015358.
FT   CONFLICT     48     48       Q -> T (in Ref. 1; AAM94175).
FT   CONFLICT    194    194       V -> L (in Ref. 1; AAM94175).
FT   CONFLICT    227    234       QYVKKDDS -> H (in Ref. 3; BAB24355).
FT   CONFLICT    632    632       T -> H (in Ref. 2; AAH55400).
SQ   SEQUENCE   1047 AA;  119650 MW;  91908C847218D4C0 CRC64;
     MEPETPEKVD SAQEKVRGKT PTADDSDDSR EKTGIEEKGE LTDAYQLQVA EEMAKEIKKK
     IRKKLKEQLT YFPPDTLLHD DKLASEKRKK KKKKVPVPTK PESSPSDVCD SAVEGEQKKE
     GTPEDSQHME GICSREQDVD ATVPENAKPK PKKTKKKTKA VSNDNEDTNG DGVHEITSRD
     SPVHPKCLLD DDLVMGVYIH RTDRLKSDFM ISHPMVKIHV VDEHTGQYVK KDDSERPVSS
     YYEKDNVDYI LPIMTQPYDF KKLKSRLPEW EEQVIFNENF PYLLREFEEC PKVILFFEIL
     DFLSMDEIKN NSEVQNQECG FRKIAWAFLK LLGANGNANI NSKLRLQLYY PPTKPRSQLN
     VVEVFEWWSK CPRNRYPSTL YVTVRGLKVP DCIKPSYRSM MALQEERGTP VYCERHRETS
     SVDTEPGLED SKEEVKWKRL PGQACRIPNK HLFSLNAGER GCFCLDFSHN GRILAAACAS
     RDGYPIILYE IPSGRFMREL CGHLNIIYDL DWSKDDRYLV TSSSDGTARV WKNEINSTST
     FRVLPHPSFV YTAKFHPATR ELVVTGCYDS MIRIWKIDAR EDAAILVRQL DVHKSFVNSI
     CFDDEGHHMY SGDCIGVIVV WDTYVKVNDV QTSVRHWTIN KEIKETEFRG VPISYLEVHP
     NGKRLLIHTK DSTLRIMDLR ILAARKFVGA ANYREKIHST LTPCGTLLFS GSEDGIVYVW
     NPETGEQVAM YSDLPFKSTI RDISYHPLEN MVAFCAFGQS EPILLYIYDF QVAQQEAEML
     KRYSGTLPLP GIHQSEDALC TCPKLPQQGS FQIDEFVNTE NSSSRKIQLV KQRLETVTEV
     IRSCAAKVNK NLSMTSPPPG PAKKPRVKQS FVLTTDEIIH QFGLPQTAFI SIERGPFVRH
     VDPPPMVVAL YDYTASRSDE LTIHRGDIIR VYFKDNEDWW YGSVRKGQEG FFPANHVASE
     TLYRDSPPKV KERSPPLTPK EKTKPEKPLA SQKQSLSKGR PLDPRLGPQP VGHSEKGKDQ
     NVEDRGHKVD METKKSEPVV RKVTLIE
//
ID   KCNQ3_MOUSE             Reviewed;         873 AA.
AC   Q8K3F6;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Potassium voltage-gated channel subfamily KQT member 3;
DE   AltName: Full=KQT-like 3;
DE   AltName: Full=Potassium channel subunit alpha KvLQT3;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv7.3;
GN   Name=Kcnq3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RA   Isbrandt D., Peters H.C., Pongs O.;
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Probably important in the regulation of neuronal
CC       excitability. Associates with KCNQ2 to form a potassium channel
CC       with essentially identical properties to the channel underlying
CC       the native M-current, a slowly activating and deactivating
CC       potassium conductance which plays a critical role in determining
CC       the subthreshold electrical excitability of neurons as well as the
CC       responsiveness to synaptic inputs (By similarity).
CC   -!- SUBUNIT: Heteromultimer with KCNQ2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position (By similarity).
CC   -!- SIMILARITY: Belongs to the potassium channel family. KQT
CC       (TC 1.A.1.15) subfamily. Kv7.3/KCNQ3 sub-subfamily.
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DR   EMBL; AY118171; AAM81579.1; -; mRNA.
DR   IPI; IPI00624504; -.
DR   RefSeq; NP_690887.2; NM_152923.2.
DR   UniGene; Mm.255585; -.
DR   ProteinModelPortal; Q8K3F6; -.
DR   SMR; Q8K3F6; 112-373, 615-644.
DR   STRING; Q8K3F6; -.
DR   PhosphoSite; Q8K3F6; -.
DR   PRIDE; Q8K3F6; -.
DR   Ensembl; ENSMUST00000070256; ENSMUSP00000063380; ENSMUSG00000056258.
DR   GeneID; 110862; -.
DR   KEGG; mmu:110862; -.
DR   UCSC; uc007wab.1; mouse.
DR   CTD; 110862; -.
DR   MGI; MGI:1336181; Kcnq3.
DR   GeneTree; ENSGT00550000074513; -.
DR   HOGENOM; HBG714141; -.
DR   HOVERGEN; HBG059014; -.
DR   InParanoid; Q8K3F6; -.
DR   OrthoDB; EOG4V9TPZ; -.
DR   NextBio; 364809; -.
DR   ArrayExpress; Q8K3F6; -.
DR   Bgee; Q8K3F6; -.
DR   Genevestigator; Q8K3F6; -.
DR   GermOnline; ENSMUSG00000056258; Mus musculus.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR020969; Ankyrin-G_BS.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003937; K_chnl_volt-dep_KCNQ.
DR   InterPro; IPR003948; K_chnl_volt-dep_KCNQ3.
DR   InterPro; IPR013821; K_chnl_volt-dep_KCNQ_C.
DR   PANTHER; PTHR11537:SF5; KCNQ3_channel; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF03520; KCNQ_channel; 1.
DR   Pfam; PF11956; KCNQC3-Ank-G_bd; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01462; KCNQ3CHANNEL.
DR   PRINTS; PR01459; KCNQCHANNEL.
PE   1: Evidence at protein level;
KW   Ion transport; Ionic channel; Membrane; Phosphoprotein; Potassium;
KW   Potassium channel; Potassium transport; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    873       Potassium voltage-gated channel subfamily
FT                                KQT member 3.
FT                                /FTId=PRO_0000054035.
FT   TRANSMEM    123    143       Helical; Name=Segment S1; (Potential).
FT   TRANSMEM    154    174       Helical; Name=Segment S2; (Potential).
FT   TRANSMEM    198    218       Helical; Name=Segment S3; (Potential).
FT   TRANSMEM    227    248       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TRANSMEM    263    283       Helical; Name=Segment S5; (Potential).
FT   INTRAMEM    305    325       Pore-forming; Name=Segment H5;
FT                                (Potential).
FT   TRANSMEM    332    352       Helical; Name=Segment S6; (Potential).
FT   MOTIF       317    322       Selectivity filter (By similarity).
FT   COMPBIAS     13     25       Poly-Gly.
FT   MOD_RES      34     34       Phosphoserine.
FT   MOD_RES     599    599       Phosphoserine.
FT   MOD_RES     747    747       Phosphothreonine (By similarity).
SQ   SEQUENCE   873 AA;  96796 MW;  B216709DA8CCFE9E CRC64;
     MGLKARTAAG AAGGGGGEGG GGGGGAANPA GGDSAVAGDE ERKVGLAPGD VEQVTLALGA
     GADKDGTLLL EGGGREEGQR RTPQGIGLLA KTPLSRPVKR NNAKYRRIQT LIYDALERPR
     GWALLYHALV FLIVLGCLIL AVLTTFKEYE TVSGDWLLLL ETFAIFIFGA EFALRIWAAG
     CCCRYKGWRG RLKFARKPLC MLDIFVLIAS VPVVAVGNQG NVLATSLRSL RFLQILRMLR
     MDRRGGTWKL LGSAICAHSK ELITAWYIGF LTLILSSFLV YLVEKDVPEM DAQGEEMKEE
     FETYADALWW GLITLATIGY GDKTPKTWEG RLIAATFSLI GVSFFALPAG ILGSGLALKV
     QEQHRQKHFE KRRKPAAELI QAAWRYYATN PNRLDLVATW RFYESVVSFP FFRKEQLEAA
     ASQKLGLLDR VRLSNPRGSN TKGKLFTPLN VDAIEESPSK EPKPVGLNNK ERFRTAFRMK
     AYAFWQSSED AGTGDPMAED RGYGNDFLIE DMIPTLKAAI RAVRILQFRL YKKKFKETLR
     PYDVKDVIEQ YSAGHLDMLS RIKYLQTRID MIFTPGPPST PKHKKSQKGS AFTYPSQQSP
     RNEPYVARAA TSETEDQSMM GKFVKVERQV HDMGKKLDFL VDMHMQHMER LQVHVTEYYP
     TKGASSPAEG EKKEDNRYSD LKTIICNYSE TGPPDPPYSF HQVPIDRVGP YGFFAHDPVK
     LTRGGPSSTK AQANLPSSGS TYAERPTVLP ILTLLDSCVS YHSQTELQGP YSDHISPRQR
     RSITRDSDTP LSLMSVNHEE LERSPSGFSI SQDRDDYVFG PSGGSSWMRE KRYLAEGETD
     TDTDPFTPSG SMPMSSTGDG ISDSIWTPSN KPT
//
ID   VRK3_MOUSE              Reviewed;         453 AA.
AC   Q8K3G5; Q921W6;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2003, sequence version 2.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Inactive serine/threonine-protein kinase VRK3;
DE   AltName: Full=Serine/threonine-protein pseudokinase VRK3;
DE   AltName: Full=Vaccinia-related kinase 3;
GN   Name=Vrk3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=22086217; PubMed=11986327; DOI=10.1074/jbc.M202833200;
RA   Angata T., Kerr S.C., Greaves D.R., Varki N.M., Crocker P.R.,
RA   Varki A.;
RT   "Cloning and characterization of human Siglec-11. A recently evolved
RT   signaling molecule that can interact with SHP-1 and SHP-2 and is
RT   expressed by tissue macrophages, including brain microglia.";
RL   J. Biol. Chem. 277:24466-24474(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon, Liver, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=22666552; PubMed=12782311; DOI=10.1016/S0014-5793(03)00501-5;
RA   Vega F.M., Gonzalo P., Gaspar M.L., Lazo P.A.;
RT   "Expression of the VRK (vaccinia-related kinase) gene family of p53
RT   regulators in murine hematopoietic development.";
RL   FEBS Lett. 544:176-180(2003).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND NUCLEAR LOCALIZATION SIGNAL.
RX   PubMed=14645249; DOI=10.1074/jbc.M310813200;
RA   Nichols R.J., Traktman P.;
RT   "Characterization of three paralogous members of the Mammalian
RT   vaccinia related kinase family.";
RL   J. Biol. Chem. 279:7934-7946(2004).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH DUSP3.
RX   PubMed=16845380; DOI=10.1038/ncb1447;
RA   Kang T.H., Kim K.T.;
RT   "Negative regulation of ERK activity by VRK3-mediated activation of
RT   VHR phosphatase.";
RL   Nat. Cell Biol. 8:863-869(2006).
CC   -!- FUNCTION: Inactive kinase that suppresses ERK activity by
CC       promoting phosphatase activity of DUSP3 which specifically
CC       dephosphorylates and inactivates ERK in the nucleus.
CC   -!- SUBUNIT: Interacts with DUSP3.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed in liver, kidney, muscle, thymus,
CC       and bone marrow. Weakly expressed in spleen.
CC   -!- DEVELOPMENTAL STAGE: Weakly expressed in embryo compared to VRK1
CC       and VRK3. Expressed from E10.5 to E13.5 in developing liver and
CC       then decreases. It increases again from E17.5 and remains
CC       thereafter. Highly expressed in hematopoietic embryonic tissues
CC       from E10.5 to E14.5. Strongly expressed in the yolk-sac.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC       protein kinase family. VRK subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- CAUTION: Inactive as a kinase due to its inability to bind ATP.
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DR   EMBL; AY115107; AAM74471.1; -; Genomic_DNA.
DR   EMBL; BC010473; AAH10473.1; -; mRNA.
DR   EMBL; BC024782; AAH24782.1; -; mRNA.
DR   EMBL; BC024839; AAH24839.1; -; mRNA.
DR   EMBL; BC034196; AAH34196.1; -; mRNA.
DR   IPI; IPI00122321; -.
DR   RefSeq; NP_598706.1; NM_133945.1.
DR   UniGene; Mm.28816; -.
DR   ProteinModelPortal; Q8K3G5; -.
DR   SMR; Q8K3G5; 124-451.
DR   STRING; Q8K3G5; -.
DR   PhosphoSite; Q8K3G5; -.
DR   PRIDE; Q8K3G5; -.
DR   Ensembl; ENSMUST00000002275; ENSMUSP00000002275; ENSMUSG00000002205.
DR   GeneID; 101568; -.
DR   KEGG; mmu:101568; -.
DR   UCSC; uc009gqr.1; mouse.
DR   CTD; 101568; -.
DR   MGI; MGI:2182465; Vrk3.
DR   GeneTree; ENSGT00600000084076; -.
DR   HOGENOM; HBG715700; -.
DR   HOVERGEN; HBG047756; -.
DR   InParanoid; Q8K3G5; -.
DR   OMA; YEEKPPY; -.
DR   OrthoDB; EOG48WC2Q; -.
DR   PhylomeDB; Q8K3G5; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 355022; -.
DR   ArrayExpress; Q8K3G5; -.
DR   Bgee; Q8K3G5; -.
DR   CleanEx; MM_VRK3; -.
DR   Genevestigator; Q8K3G5; -.
DR   GermOnline; ENSMUSG00000002205; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0019903; F:protein phosphatase binding; IPI:MGI.
DR   GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IPI:MGI.
DR   GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IPI:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Nucleotide-binding; Nucleus; Phosphoprotein.
FT   CHAIN         1    453       Inactive serine/threonine-protein kinase
FT                                VRK3.
FT                                /FTId=PRO_0000086809.
FT   DOMAIN      125    436       Protein kinase.
FT   MOTIF        49     64       Nuclear localization signal.
FT   MOD_RES      55     55       Phosphoserine (By similarity).
FT   MOD_RES      59     59       Phosphoserine (By similarity).
FT   MOD_RES      82     82       Phosphoserine (By similarity).
FT   MOD_RES      83     83       Phosphoserine (By similarity).
FT   MOD_RES     115    115       Phosphoserine (By similarity).
FT   CONFLICT     44     44       S -> P (in Ref. 1; AAM74471).
FT   CONFLICT    168    168       V -> I (in Ref. 1; AAM74471).
SQ   SEQUENCE   453 AA;  50830 MW;  B882A3F60802C432 CRC64;
     MISFCPVCGK SVKVSFKFCP YCGKALPVEE DGGTQSAVTP HVSSVPGSRR DLNSSFETSP
     KKVKCSHTVT SLPLSRHSDC DSSGSDNTLT SPDRATGTRS RPLTPKGSPL SNRQSPQTLK
     RTRVTTSLQA LATGTELTDQ NGKHWTLGAL QIRDDQGILY EAEPTSAVPS ESRTQKWRFS
     LKLDSKDGRL FNEQNFFQRV AKPLQVNKWK KQFLLPLLAI PTCIGFGIHQ DKYRFLVFPS
     LGRSLQSALD DNPKHVVSER CVLQVACRLL DALEYLHENE YVHGNLTAEN VFVNPEDLSQ
     VTLVGYGFTY RYCPGGKHVA YKEGSRSPHD GDLEFISMDL HKGCGPSRRS DLQTLGYCML
     KWLYGSLPWT NCLPNTEKIT RQKQKYLDSP ERLVGLCGRW NKASETLREY LKVVMALNYE
     EKPPYATLRN SLEALLQDMR VSPYDPLDLQ MVP
//
ID   DP13B_MOUSE             Reviewed;         662 AA.
AC   Q8K3G9; Q99LT7;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=DCC-interacting protein 13-beta;
DE            Short=Dip13-beta;
DE   AltName: Full=Adapter protein containing PH domain, PTB domain and leucine zipper motif 2;
GN   Name=Appl2; Synonyms=Dip13b, Dip3b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Chen Y.Q.;
RT   "Cloning of mouse DIP13 alpha and beta.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Required for the regulation of cell proliferation in
CC       response to extracellular signals mediated by an early endosomal
CC       compartment. Links Rab5 to nuclear signal transduction (By
CC       similarity).
CC   -!- SUBUNIT: Binds RAB5A/Rab5 through an N-terminal domain. This
CC       interaction is essential for its recruitment to endosomal
CC       membranes as well as its role in cell proliferation. Binds
CC       subunits of the NuRD/MeCP1 complex (By similarity).
CC   -!- INTERACTION:
CC       Q91VH1:Adipor1; NbExp=1; IntAct=EBI-647007, EBI-992398;
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane
CC       protein (By similarity). Nucleus (By similarity). Note=Early
CC       endosomal membrane-bound and nuclear. Translocated into the
CC       nucleus upon release from endosomal membranes following
CC       internalization of EGF (By similarity).
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 PID domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AY113706; AAM55532.1; -; mRNA.
DR   EMBL; BC002232; AAH02232.1; -; mRNA.
DR   EMBL; BC048906; AAH48906.1; -; mRNA.
DR   IPI; IPI00170083; -.
DR   RefSeq; NP_660255.1; NM_145220.2.
DR   UniGene; Mm.282985; -.
DR   ProteinModelPortal; Q8K3G9; -.
DR   SMR; Q8K3G9; 4-378, 485-613.
DR   IntAct; Q8K3G9; 2.
DR   STRING; Q8K3G9; -.
DR   PhosphoSite; Q8K3G9; -.
DR   PRIDE; Q8K3G9; -.
DR   Ensembl; ENSMUST00000020500; ENSMUSP00000020500; ENSMUSG00000020263.
DR   GeneID; 216190; -.
DR   KEGG; mmu:216190; -.
DR   UCSC; uc007gkk.1; mouse.
DR   CTD; 216190; -.
DR   MGI; MGI:2384914; Appl2.
DR   GeneTree; ENSGT00390000011534; -.
DR   HOGENOM; HBG447421; -.
DR   HOVERGEN; HBG051394; -.
DR   InParanoid; Q8K3G9; -.
DR   OMA; GLVTTTW; -.
DR   OrthoDB; EOG41G33P; -.
DR   PhylomeDB; Q8K3G9; -.
DR   NextBio; 375066; -.
DR   ArrayExpress; Q8K3G9; -.
DR   Bgee; Q8K3G9; -.
DR   Genevestigator; Q8K3G9; -.
DR   GermOnline; ENSMUSG00000020263; Mus musculus.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0008283; P:cell proliferation; ISS:UniProtKB.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Pfam; PF00640; PID; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS01179; PID; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Endosome; Membrane; Nucleus.
FT   CHAIN         1    662       DCC-interacting protein 13-beta.
FT                                /FTId=PRO_0000079988.
FT   DOMAIN      277    375       PH.
FT   DOMAIN      486    635       PID.
FT   REGION        1    428       Required for RAB5A binding (By
FT                                similarity).
FT   CONFLICT    428    428       V -> D (in Ref. 2; AAH02232).
SQ   SEQUENCE   662 AA;  73854 MW;  8917BDE1CF13FC3B CRC64;
     MPAVDKLLLE EALQDSPQAR SLLSVFEEDA GTLTDYTNQL LQAMQRVYGA QNEMCLATQQ
     LSRQLLAYEK QNFALGKGDE EVISTLHYFS KVMDELNGLH TELAKQLADT MVLPVIQFRE
     KDLTEVSTLK DLFGLASSEH DLSMAKYSRL PKKKENEKAK TEIVKEVAAA RRKQHLSSLQ
     YYCALNALQY RKRAAMMEPL IGFAHGQINF FKRGAEMFSK SMDGFLSSVK DMVQSIQVEL
     EAEADKMRVS QQELLSVSES VYTPDIDVAT AQINRNLIQK TGYLNLRNKT GLVTTTWERL
     YFFTQGGNLM CQPRGAVAGG LIQDLDNCSV MAVDCEDRRY CFQISTPSGK PGIILQAESR
     KEYEEWICAV NNISRQIYLT DNPEAVAIKL NQTALQAVTP ITSFGKKQES SCSSQNIKNS
     DIEDDNIVPK ATASIPETEE LIAPGTPIQF DIVLPATEFL DQNRGGRRTN PFGETEDGSF
     PEAEDSLLQQ MFIVRFLGSM AVKTDSTAEV IYEAMRQVLA ARAIHNIFRM TESHLMVTSQ
     TLRLIDPQTQ VSRACFELTS VTQFAAHQEN KRLVGFVIRV PESTGEESLS TYIFESNSEG
     EKICYAINLG KEIIEVQKDP EALARLMLSV PLTNDGKYVL LNDQADDTGG SPSENRGAES
     EA
//
ID   DP13A_MOUSE             Reviewed;         707 AA.
AC   Q8K3H0; Q3UJP7; Q69ZJ9; Q8BWZ8; Q8VCJ8; Q9CUW4;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=DCC-interacting protein 13-alpha;
DE            Short=Dip13-alpha;
DE   AltName: Full=Adapter protein containing PH domain, PTB domain and leucine zipper motif 1;
GN   Name=Appl1; Synonyms=Dip13a, Kiaa1428;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Chen Y.Q.;
RT   "Cloning of mouse DIP13 alpha and beta.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2;
RC   TISSUE=Cecum, Corpora quadrigemina, Embryonic stem cell, and
RC   Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Limb, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 485-707.
RC   TISSUE=Pancreatic islet;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-401, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   INTERACTION WITH OCRL.
RX   PubMed=20133602; DOI=10.1073/pnas.0914658107;
RA   Swan L.E., Tomasini L., Pirruccello M., Lunardi J., De Camilli P.;
RT   "Two closely related endocytic proteins that share a common OCRL-
RT   binding motif with APPL1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:3511-3516(2010).
CC   -!- FUNCTION: Required for the regulation of cell proliferation in
CC       response to extracellular signals from an early endosomal
CC       compartment. Links Rab5 to nuclear signal transduction (By
CC       similarity).
CC   -!- SUBUNIT: Binds RAB5A/Rab5 through an N-terminal domain. This
CC       interaction is essential for its recruitment to endosomal
CC       membranes as well as its role in cell proliferation. Binds DCC and
CC       the catalytic domain of the inactive form of AKT2 through its PID
CC       domain. Binds PIK3CA and subunits of the NuRD/MeCP1 complex (By
CC       similarity). Interacts with OCRL.
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane
CC       protein (By similarity). Nucleus (By similarity). Note=Early
CC       endosomal membrane-bound and nuclear. Translocated into the
CC       nucleus upon release from endosomal membranes following
CC       internalization of EGF (By similarity).
CC   -!- DOMAIN: Overexpression of an N-terminal domain (residues 1-319) or
CC       a C-terminal region (residues 273-707) has a proapoptotic effect
CC       (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 PID domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH19708.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY113705; AAM55531.1; -; mRNA.
DR   EMBL; AK013715; BAB28966.3; -; mRNA.
DR   EMBL; AK033566; BAC28364.1; -; mRNA.
DR   EMBL; AK045438; BAC32367.1; -; mRNA.
DR   EMBL; AK049307; BAC33672.2; -; mRNA.
DR   EMBL; AK146356; BAE27108.1; -; mRNA.
DR   EMBL; BC019708; AAH19708.1; ALT_INIT; mRNA.
DR   EMBL; BC063751; AAH63751.1; -; mRNA.
DR   EMBL; AK173169; BAD32447.1; -; mRNA.
DR   IPI; IPI00170084; -.
DR   RefSeq; NP_660256.1; NM_145221.2.
DR   UniGene; Mm.202322; -.
DR   ProteinModelPortal; Q8K3H0; -.
DR   SMR; Q8K3H0; 4-378, 498-644.
DR   IntAct; Q8K3H0; 4.
DR   MINT; MINT-136655; -.
DR   STRING; Q8K3H0; -.
DR   PhosphoSite; Q8K3H0; -.
DR   PRIDE; Q8K3H0; -.
DR   Ensembl; ENSMUST00000036570; ENSMUSP00000042875; ENSMUSG00000040760.
DR   GeneID; 72993; -.
DR   KEGG; mmu:72993; -.
DR   UCSC; uc007sth.1; mouse.
DR   CTD; 72993; -.
DR   MGI; MGI:1920243; Appl1.
DR   eggNOG; roNOG06311; -.
DR   GeneTree; ENSGT00390000011534; -.
DR   HOGENOM; HBG447421; -.
DR   HOVERGEN; HBG051394; -.
DR   InParanoid; Q8K3H0; -.
DR   OMA; GTKSETE; -.
DR   OrthoDB; EOG4PVNZ2; -.
DR   PhylomeDB; Q8K3H0; -.
DR   NextBio; 337289; -.
DR   ArrayExpress; Q8K3H0; -.
DR   Bgee; Q8K3H0; -.
DR   Genevestigator; Q8K3H0; -.
DR   GermOnline; ENSMUSG00000040760; Mus musculus.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0008283; P:cell proliferation; ISS:UniProtKB.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Pfam; PF00640; PID; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS01179; PID; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Coiled coil; Endosome; Membrane; Nucleus; Phosphoprotein.
FT   CHAIN         1    707       DCC-interacting protein 13-alpha.
FT                                /FTId=PRO_0000079986.
FT   DOMAIN      277    375       PH.
FT   DOMAIN      495    655       PID.
FT   REGION        1    428       Required for RAB5A binding (By
FT                                similarity).
FT   COILED      234    257       Potential.
FT   COILED      620    670       Potential.
FT   MOD_RES     399    399       Phosphothreonine (By similarity).
FT   MOD_RES     401    401       Phosphoserine.
FT   MOD_RES     689    689       Phosphoserine (By similarity).
FT   CONFLICT     37     37       M -> K (in Ref. 2; BAB28966).
FT   CONFLICT    117    117       Q -> P (in Ref. 2; BAB28966).
FT   CONFLICT    136    136       A -> T (in Ref. 2; BAB28966).
FT   CONFLICT    151    151       S -> P (in Ref. 2; BAB28966).
SQ   SEQUENCE   707 AA;  79328 MW;  7B0F4BF4B6247A7F CRC64;
     MPGIDKLPIE ETLEDSPQTR SLLGVFEEDA TAISNYMNQL YQAMHRIYDA QNELSAATHL
     TSKLLKEYEK QRFPLGGDDE VMSSTLQQFS KVIDELSSCH AVLSTQLADA MMFPISQFKE
     RDLKEILTLK EVFQIASNDH DAAINRYSRL SKKRENDKVK YEVTEDVYTS RKKQHQTMMH
     YFCALNTLQY KKKIALLEPL LGYMQAQISF FKMGSENLNG QLEEFLANIG TSVQNVRREM
     DGDVETMQQT IEDLEVASDP LYLPDPDPTK FPINRNLTRK AGYLNARNKT GLVSSTWDRQ
     FYFTQGGNLM SQARGDVAGG LAMDIDNCSV MAVDCEDRRY CFQITSFDGK KSSILQAESK
     KDHEEWICTI NNISKQIYLS ENPEETAARV NQSALEAVTP SPSFQQRHES LRPGGQSRPP
     TARTSSSGSL GSESTNLAAL SLDSLVAPDT PIQFDIISPV CEDQPGQAKA FGQGGRRTNP
     FGESGGSTKS ETEDSILHQL FIVRFLGSME VKSDDHPDVV YETMRQILAA RAIHNIFRMT
     ESHLLVTCDC LKLIDPQTQV TRLTFPLPCV VLYATHQENK RLFGFVLRTS GGRSESNLSS
     VCYIFESNNE GEKICDSVGL AKQIALHAEL DRRASEKQKE IERVKEKQQK ELSKQKQIEK
     DLEEQSRLIA ASSRPNQAGS EGQLVLSSSQ SEESDLGEEG KKRESEA
//
ID   MYRIP_MOUSE             Reviewed;         856 AA.
AC   Q8K3I4; Q8CFC0; Q8K4H5;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Rab effector MyRIP;
DE   AltName: Full=Exophilin-8;
DE   AltName: Full=Myosin-VIIa- and Rab-interacting protein;
DE   AltName: Full=Slp homolog lacking C2 domains c;
DE            Short=SlaC2-c;
GN   Name=Myrip; Synonyms=Slac2c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Inner ear;
RX   MEDLINE=21987934; PubMed=11964381; DOI=10.1093/embo-reports/kvf090;
RA   El-Amraoui A., Schonn J.-S., Kuessel-Andermann P., Blanchard S.,
RA   Desnos C., Henry J.-P., Wolfrum U., Darchen F., Petit C.;
RT   "MyRIP, a novel Rab effector, enables myosin VIIa recruitment to
RT   retinal melanosomes.";
RL   EMBO Rep. 3:463-470(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=22057839; PubMed=12062444; DOI=10.1016/S0014-5793(02)02634-0;
RA   Nagashima K., Torii S., Yi Z., Igarashi M., Okamoto K., Takeuchi T.,
RA   Izumi T.;
RT   "Melanophilin directly links Rab27a and myosin Va through its distinct
RT   coiled-coil regions.";
RL   FEBS Lett. 517:233-238(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH RAB27A; MYO5A; MYO7A AND
RP   F-ACTIN, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=22302022; PubMed=12221080; DOI=10.1074/jbc.M203862200;
RA   Fukuda M., Kuroda T.S.;
RT   "Slac2-c (synaptotagmin-like protein homologue lacking C2 domains-c),
RT   a novel linker protein that interacts with Rab27, myosin Va/VIIa, and
RT   actin.";
RL   J. Biol. Chem. 277:43096-43103(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, and Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Rab effector protein involved in melanosome transport.
CC       Serves as link between melanosome-bound RAB27A and the motor
CC       proteins MYO5A and MYO7A. May link RAB27A-containing vesicles to
CC       actin filaments.
CC   -!- SUBUNIT: Binds RAB27A that has been activated by GTP-binding via
CC       its N-terminus. Binds MYO5A, MYO7A and F-actin.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Melanosome. Note=In pre- and
CC       post-synaptic areas in photoreceptor cells and in the basal
CC       microvilli of retinal pigment epithelium cells. Associated with
CC       melanosomes. Colocalizes with actin filaments.
CC   -!- TISSUE SPECIFICITY: Detected in brain, skin, heart, lung, adrenal
CC       medulla, pancreas, intestine, liver, kidney, skeletal muscle and
CC       testis. Detected in cochlear and vestibular hair cells in the
CC       inner ear, and in photoreceptor and pigment epithelium cells in
CC       the retina.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 1 RabBD (Rab-binding) domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF396688; AAM43955.1; -; mRNA.
DR   EMBL; AY099470; AAM44403.1; -; mRNA.
DR   EMBL; AB083782; BAC15554.1; -; mRNA.
DR   EMBL; AK038988; BAC30194.1; -; mRNA.
DR   EMBL; AK083225; BAC38816.1; -; mRNA.
DR   IPI; IPI00322509; -.
DR   RefSeq; NP_653140.1; NM_144557.5.
DR   UniGene; Mm.100936; -.
DR   ProteinModelPortal; Q8K3I4; -.
DR   SMR; Q8K3I4; 4-144.
DR   STRING; Q8K3I4; -.
DR   PhosphoSite; Q8K3I4; -.
DR   PRIDE; Q8K3I4; -.
DR   Ensembl; ENSMUST00000048121; ENSMUSP00000046891; ENSMUSG00000041794.
DR   GeneID; 245049; -.
DR   KEGG; mmu:245049; -.
DR   UCSC; uc009scn.1; mouse.
DR   CTD; 245049; -.
DR   MGI; MGI:2384407; Myrip.
DR   GeneTree; ENSGT00390000013933; -.
DR   HOGENOM; HBG445612; -.
DR   HOVERGEN; HBG052562; -.
DR   InParanoid; Q8K3I4; -.
DR   OMA; STNRTKE; -.
DR   OrthoDB; EOG46T30W; -.
DR   PhylomeDB; Q8K3I4; -.
DR   NextBio; 386542; -.
DR   ArrayExpress; Q8K3I4; -.
DR   Bgee; Q8K3I4; -.
DR   CleanEx; MM_MYRIP; -.
DR   Genevestigator; Q8K3I4; -.
DR   GermOnline; ENSMUSG00000041794; Mus musculus.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR   GO; GO:0042470; C:melanosome; IDA:UniProtKB.
DR   GO; GO:0001750; C:photoreceptor outer segment; IDA:UniProtKB.
DR   GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR   GO; GO:0003779; F:actin binding; IDA:MGI.
DR   GO; GO:0017022; F:myosin binding; IDA:MGI.
DR   GO; GO:0017137; F:Rab GTPase binding; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0030050; P:vesicle transport along actin filament; TAS:MGI.
DR   InterPro; IPR006788; Myelin-assoc_OBP.
DR   InterPro; IPR010911; Rab-bd_domain.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF04698; MOBP; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS50916; RABBD; 1.
DR   PROSITE; PS50178; ZF_FYVE; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Actin-binding; Cytoplasm; Metal-binding; Phosphoprotein; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    856       Rab effector MyRIP.
FT                                /FTId=PRO_0000190225.
FT   DOMAIN        4    124       RabBD.
FT   ZN_FING      63    105       FYVE-type.
FT   REGION      143    560       Myosin-binding.
FT   REGION      495    856       Actin-binding.
FT   MOD_RES      48     48       Phosphoserine (By similarity).
FT   MOD_RES      51     51       Phosphoserine (By similarity).
FT   MOD_RES      54     54       Phosphoserine (By similarity).
FT   CONFLICT    400    400       E -> G (in Ref. 1; AAM43955).
FT   CONFLICT    408    408       A -> R (in Ref. 2; BAC15554).
FT   CONFLICT    409    409       L -> F (in Ref. 1; AAM43955).
FT   CONFLICT    593    593       E -> K (in Ref. 1; AAM43955).
SQ   SEQUENCE   856 AA;  94924 MW;  1150ABB83B102C8A CRC64;
     MGRKLDLSGL TDDETEHVLQ VVQRDFNLRK KEEDRLSEMK QRLAEENSKC SILSKHQKFV
     ERCCMRCCSP FTFLVNARRR CGECKFSVCK SCCSYQKHEK LWVCCVCQQA RLLRTQSLEW
     FYNNVKSRFK RFGSAKVLKN LYRKHRLESG ACFDILGGGL FEPNLENEGS ISGSDSTFYR
     QSEGHSMMDT LAVALRVAEE AIEEAISKAE SHGDSLDKQN EASYLRDHKQ ELTEELAGTI
     LQRIIRKQKD KAELRAEEEE PEWPRSQSGS VKARGEGTTA PPGRHKARAT FRRSQSAFSF
     TMEDALKSGS AEAAPRSPKD RAQRLLEEAA LPSWRSMDGL DGTNLAPLLQ SPDGNWMTLK
     DGSRQPPTRL LTKPKSGTFQ ALEVASSVTS AYDEIGSDSE EDFDYSEALS KLCPPSQSRL
     KQPQPQPTQA QSSGQGPLAT SPSNPEAMCS DSETSSTSSS REAGCRAKLS WLQRKAPKNP
     AVEKMPLQGE LDVNFNPQAA GGETSDSSDP EETLRTAERR ARRWRRARVG PEESNRGLPS
     PGAHPRALHT AQVSDNVSET DISNETQNSR SSTDSVEEKL RNRLYELAMK MSEKETSSGE
     DQESESKAEP KNQKGSLSSE ENNQGVQEEL KKKCSAVSLC NISTEVLKVI NATEELIAES
     AGPWEIPPVS TDRENGMFPL GTDQVRLDKQ LTSLEENVYL AAGTVYGLEG QLSELEDAAR
     CIHSSTGETE LADLEDQVAA AAAQVHHAEL QISDIESRIS ALTIAGLNIA PCVRLTRRRD
     QKQRSQVQTI DTSRQQRRKL PAPPVKAEKI EASSVTPIKT FNRNFLLQGS STNRPTASTG
     DTKDLMEPDL ESAVMY
//
ID   GLCI1_MOUSE             Reviewed;         537 AA.
AC   Q8K3I9; Q80YT1; Q8CEA5; Q925C1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=Glucocorticoid-induced transcript 1 protein;
DE   AltName: Full=Glucocorticoid-induced gene 18 protein;
DE   AltName: Full=Testhymin;
DE   AltName: Full=Thymocyte/spermatocyte selection protein 1;
GN   Name=Glcci1; Synonyms=Gig18, Tssn1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Leptich T.D., Flomerfelt F.A., Chapman M.S., Miesfeld R.L.;
RT   "Characterization of a glucocorticoid-regulated gene in immature
RT   thymocytes.";
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Thymus;
RX   PubMed=12557054; DOI=10.1007/s00251-002-0513-1;
RA   Miazek A., Malissen B.;
RT   "Two genes, three messengers: hybrid transcript between a gene
RT   expressed at specific stages of T-cell and sperm maturation and an
RT   unrelated adjacent gene.";
RL   Immunogenetics 54:681-692(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-423 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8K3I9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K3I9-2; Sequence=VSP_021322, VSP_021323;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8K3I9-3; Sequence=VSP_021321;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in thymus and testis,
CC       especially in CD4+CD8+ cells and at specific stages of
CC       spermatogenesis.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF374476; AAK54615.1; -; mRNA.
DR   EMBL; AY098636; AAM33072.1; -; mRNA.
DR   EMBL; BC050802; AAH50802.1; -; mRNA.
DR   EMBL; AK028709; BAC26078.1; -; mRNA.
DR   IPI; IPI00126712; -.
DR   IPI; IPI00170092; -.
DR   IPI; IPI00274737; -.
DR   UniGene; Mm.210787; -.
DR   STRING; Q8K3I9; -.
DR   PhosphoSite; Q8K3I9; -.
DR   PRIDE; Q8K3I9; -.
DR   Ensembl; ENSMUST00000050350; ENSMUSP00000058581; ENSMUSG00000089862.
DR   Ensembl; ENSMUST00000064285; ENSMUSP00000069444; ENSMUSG00000029638.
DR   UCSC; uc009axn.1; mouse.
DR   UCSC; uc009axt.1; mouse.
DR   UCSC; uc009axu.1; mouse.
DR   MGI; MGI:2179717; Glcci1.
DR   eggNOG; roNOG13624; -.
DR   GeneTree; ENSGT00390000005655; -.
DR   HOGENOM; HBG446570; -.
DR   HOVERGEN; HBG079782; -.
DR   InParanoid; Q8K3I9; -.
DR   OrthoDB; EOG44MXSJ; -.
DR   ArrayExpress; Q8K3I9; -.
DR   Bgee; Q8K3I9; -.
DR   CleanEx; MM_GLCCI1; -.
DR   Genevestigator; Q8K3I9; -.
DR   GermOnline; ENSMUSG00000029638; Mus musculus.
DR   PROSITE; PS50901; FTSK; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Phosphoprotein.
FT   CHAIN         1    537       Glucocorticoid-induced transcript 1
FT                                protein.
FT                                /FTId=PRO_0000256129.
FT   COILED      217    244       Potential.
FT   COMPBIAS      5      9       Poly-Ser.
FT   COMPBIAS     74     82       Poly-Ala.
FT   COMPBIAS    515    518       Poly-Gln.
FT   MOD_RES      26     26       Phosphoserine.
FT   MOD_RES      96     96       Phosphoserine (By similarity).
FT   MOD_RES      98     98       Phosphoserine (By similarity).
FT   MOD_RES      99     99       Phosphoserine (By similarity).
FT   MOD_RES     101    101       Phosphothreonine (By similarity).
FT   MOD_RES     122    122       Phosphoserine (By similarity).
FT   MOD_RES     139    139       Phosphoserine (By similarity).
FT   MOD_RES     163    163       Phosphoserine (By similarity).
FT   MOD_RES     166    166       Phosphothreonine (By similarity).
FT   MOD_RES     168    168       Phosphothreonine (By similarity).
FT   MOD_RES     212    212       Phosphoserine (By similarity).
FT   MOD_RES     214    214       Phosphoserine (By similarity).
FT   MOD_RES     293    293       Phosphoserine (By similarity).
FT   MOD_RES     335    335       Phosphoserine (By similarity).
FT   VAR_SEQ       1    187       Missing (in isoform 3).
FT                                /FTId=VSP_021321.
FT   VAR_SEQ       1    107       Missing (in isoform 2).
FT                                /FTId=VSP_021322.
FT   VAR_SEQ     108    143       PAEQAPRAKGRPRRSPESRRRSSSPERRSPGSPVCR -> M
FT                                CPSPWPHMCWRHRAPSATFLTTYSHTMSATTCPDS (in
FT                                isoform 2).
FT                                /FTId=VSP_021323.
FT   CONFLICT    223    223       E -> EQ (in Ref. 3; AAH50802 and 4;
FT                                BAC26078).
SQ   SEQUENCE   537 AA;  57479 MW;  A0B1D63CAC7534EE CRC64;
     MSTASSSSSQ TPHSAPQRMR RSTAGSPPAA AGSGTGPAGS CAPAAGAGRL LQPIRATVPY
     QLLRGSQHSP TRPAAAATAA AALGSLSGPG GARGPSPSSP TPPPAAAPAE QAPRAKGRPR
     RSPESRRRSS SPERRSPGSP VCRVDRPKSQ HIRTSSTIRR TSSLDTITGP YLTGQWPRDP
     HVHYPSCMRD KATQTPSCWA EEGAEKRSHQ RSASWGSADQ LKEIAKLRQQ LQRSKQSSRH
     SKEKDRQSPL HGNHITISHT QAIGSRSVPM PLSNISVPKS SVSRVPCNVE GISPELEKVF
     IKENNGKEEV SKPLDIPDGR RAPLPAHYRS SSTRSIDTQT PSVQERSSSC SSHSPCVSPF
     CPPESQDGSP CSTEDLLYDR DKDSGSSSPL PKYASSPKPN NSYMFKREPP EGCERVKVFE
     EMASRQPISA PLFSCPDKNK VNFIPTGSAF CPVKLLGPLL PASDLMLKNS PNSGQSSALA
     TLTVEQLSSR VSFTSLSDDT STADSLEPSA QQPSQQQQLL QDLQVEEHVS TQNYVMI
//
ID   NDUS8_MOUSE             Reviewed;         212 AA.
AC   Q8K3J1;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 8, mitochondrial;
DE            EC=1.6.5.3;
DE            EC=1.6.99.3;
DE   AltName: Full=Complex I-23kD;
DE            Short=CI-23kD;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 23 kDa subunit;
DE   Flags: Precursor;
GN   Name=Ndufs8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Lucas-Teixeira V.A., Marques S., Belo J.A.;
RT   "Genomic organization of the mouse NDUFS8 gene encoding the NADH
RT   dehydrogenase:ubiquinone Fe-S protein 8.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 19-37; 60-90 AND 118-135, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory
CC       chain NADH dehydrogenase (Complex I) that is believed to belong to
CC       the minimal assembly required for catalysis. Complex I functions
CC       in the transfer of electrons from NADH to the respiratory chain.
CC       The immediate electron acceptor for the enzyme is believed to be
CC       ubiquinone (By similarity).
CC   -!- CATALYTIC ACTIVITY: NADH + ubiquinone = NAD(+) + ubiquinol.
CC   -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor.
CC   -!- COFACTOR: Binds 2 4Fe-4S clusters per subunit (By similarity).
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits This is a
CC       component of the iron-sulfur (IP) fragment of the enzyme (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the complex I 23 kDa subunit family.
CC   -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains.
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DR   EMBL; AY096002; AAM34451.1; -; Genomic_DNA.
DR   IPI; IPI00170093; -.
DR   PIR; PC7079; PC7079.
DR   RefSeq; NP_659119.2; NM_144870.4.
DR   UniGene; Mm.44227; -.
DR   ProteinModelPortal; Q8K3J1; -.
DR   SMR; Q8K3J1; 86-202.
DR   STRING; Q8K3J1; -.
DR   PhosphoSite; Q8K3J1; -.
DR   REPRODUCTION-2DPAGE; Q8K3J1; -.
DR   PRIDE; Q8K3J1; -.
DR   Ensembl; ENSMUST00000075092; ENSMUSP00000074600; ENSMUSG00000059734.
DR   GeneID; 225887; -.
DR   KEGG; mmu:225887; -.
DR   NMPDR; fig|10090.3.peg.4372; -.
DR   UCSC; uc008fxn.1; mouse.
DR   CTD; 225887; -.
DR   MGI; MGI:2385079; Ndufs8.
DR   HOGENOM; HBG724359; -.
DR   HOVERGEN; HBG006547; -.
DR   InParanoid; Q8K3J1; -.
DR   OMA; LQADHLY; -.
DR   OrthoDB; EOG43R3NR; -.
DR   PhylomeDB; Q8K3J1; -.
DR   BRENDA; 1.6.5.3; 244.
DR   BRENDA; 1.6.99.3; 244.
DR   NextBio; 377849; -.
DR   ArrayExpress; Q8K3J1; -.
DR   Bgee; Q8K3J1; -.
DR   CleanEx; MM_NDUFS8; -.
DR   Genevestigator; Q8K3J1; -.
DR   GermOnline; ENSMUSG00000059734; Mus musculus.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:EC.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001450; 4Fe4S-bd_domain.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR   InterPro; IPR012285; Fum_reductase_C.
DR   InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
DR   Gene3D; G3DSA:1.10.1060.10; Fum_reductase_C; 1.
DR   Pfam; PF00037; Fer4; 1.
DR   TIGRFAMs; TIGR01971; NuoI; 1.
DR   PROSITE; PS00198; 4FE4S_FER_1; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
PE   1: Evidence at protein level;
KW   4Fe-4S; Direct protein sequencing; Electron transport; Iron;
KW   Iron-sulfur; Metal-binding; Mitochondrion; NAD; Oxidoreductase;
KW   Repeat; Respiratory chain; Transit peptide; Transport; Ubiquinone.
FT   TRANSIT       1     34       Mitochondrion (By similarity).
FT   CHAIN        35    212       NADH dehydrogenase [ubiquinone] iron-
FT                                sulfur protein 8, mitochondrial.
FT                                /FTId=PRO_0000020014.
FT   DOMAIN      104    133       4Fe-4S ferredoxin-type 1.
FT   DOMAIN      143    172       4Fe-4S ferredoxin-type 2.
FT   METAL       113    113       Iron-sulfur 1 (4Fe-4S) (By similarity).
FT   METAL       116    116       Iron-sulfur 1 (4Fe-4S) (By similarity).
FT   METAL       119    119       Iron-sulfur 1 (4Fe-4S) (By similarity).
FT   METAL       123    123       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       152    152       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       155    155       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       158    158       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       162    162       Iron-sulfur 1 (4Fe-4S) (By similarity).
SQ   SEQUENCE   212 AA;  24038 MW;  1E06E024EA7829CD CRC64;
     MYRLSSSMLP RALAQAMRTG HLNGQSLHSS AVAATYKYVN KKEQESEVDM KSATDNAARI
     LMWTELIRGL GMTLSYLFRE PATINYPFEK GPLSPRFRGE HALRRYPSGE ERCIACKLCE
     AICPAQAITI EAEPRADGSR RTTRYDIDMT KCIYCGFCQE ACPVDAIVEG PNFEFSTETH
     EELLYNKEKL LNNGDKWEAE IAANIQADYL YR
//
ID   CABL2_MOUSE             Reviewed;         481 AA.
AC   Q8K3M5;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   11-JAN-2011, entry version 61.
DE   RecName: Full=CDK5 and ABL1 enzyme substrate 2;
DE   AltName: Full=Interactor with CDK3 2;
DE            Short=Ik3-2;
GN   Name=Cables2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver, and Spleen;
RX   MEDLINE=21952370; PubMed=11955625; DOI=10.1016/S0167-4781(01)00367-0;
RA   Sato H., Nishimoto I., Matsuoka M.;
RT   "Ik3-2, a relative to ik3-1/cables, is associated with cdk3, cdk5, and
RT   c-abl.";
RL   Biochim. Biophys. Acta 1574:157-163(2002).
CC   -!- FUNCTION: Unknown. Probably involved in G1-S cell cycle
CC       transition.
CC   -!- SUBUNIT: Binds to CDK3, CDK5 and ABL1. The C-terminal cyclin-box-
CC       like region binds to CDK5.
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- SIMILARITY: Belongs to the cyclin family.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-6 is the initiator.
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DR   EMBL; AY049712; AAL12171.1; -; mRNA.
DR   IPI; IPI00170106; -.
DR   UniGene; Mm.386884; -.
DR   ProteinModelPortal; Q8K3M5; -.
DR   SMR; Q8K3M5; 351-469.
DR   STRING; Q8K3M5; -.
DR   PhosphoSite; Q8K3M5; -.
DR   PRIDE; Q8K3M5; -.
DR   Ensembl; ENSMUST00000108891; ENSMUSP00000104519; ENSMUSG00000038990.
DR   UCSC; uc008oit.1; mouse.
DR   MGI; MGI:2182335; Cables2.
DR   HOGENOM; HBG445535; -.
DR   HOVERGEN; HBG050759; -.
DR   InParanoid; Q8K3M5; -.
DR   ArrayExpress; Q8K3M5; -.
DR   Bgee; Q8K3M5; -.
DR   CleanEx; MM_CABLES2; -.
DR   Genevestigator; Q8K3M5; -.
DR   GermOnline; ENSMUSG00000038990; Mus musculus.
DR   GO; GO:0016538; F:cyclin-dependent protein kinase regulator activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR   GO; GO:0051302; P:regulation of cell division; IEA:InterPro.
DR   InterPro; IPR012388; Cdk5/c-Abl_linker_prot_cables.
DR   InterPro; IPR006670; Cyclin.
DR   InterPro; IPR011028; Cyclin-like.
DR   InterPro; IPR013763; Cyclin-related.
DR   InterPro; IPR006671; Cyclin_N.
DR   Gene3D; G3DSA:1.10.472.10; Cyclin_related; 1.
DR   Pfam; PF00134; Cyclin_N; 1.
DR   PIRSF; PIRSF025798; Cables; 1.
DR   SMART; SM00385; CYCLIN; 1.
DR   SUPFAM; SSF47954; Cyclin_like; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Cyclin; Phosphoprotein.
FT   CHAIN         1    481       CDK5 and ABL1 enzyme substrate 2.
FT                                /FTId=PRO_0000080513.
FT   COMPBIAS      7     11       Poly-Ala.
FT   COMPBIAS     15    113       Pro-rich.
FT   MOD_RES     108    108       Phosphoserine (By similarity).
FT   MOD_RES     128    128       Phosphothreonine (By similarity).
FT   MOD_RES     129    129       Phosphoserine (By similarity).
FT   MOD_RES     133    133       Phosphoserine (By similarity).
FT   MOD_RES     211    211       Phosphoserine (By similarity).
SQ   SEQUENCE   481 AA;  52711 MW;  00DA1C706578B1B2 CRC64;
     MWHSSMAAAA AGGAPGPAPG PSRPAPAARN PPAVPRRRGD SRRRQAALFF LNNISLDGRP
     PSLGPGGEKP APPPPPPTEA REAPAPPPAP PGGLPGLPAR PAPQGLLSPT TAPAGLGLDG
     QRQRRRVTSQ RCSLEFLEDT VGCASVQRTK HASGSPRHKG LKKTHFIKNM RQYDTKNSRI
     VLICAKRSLC AAFSVLPYGE GLRISDLRVD SQKQRHPSGG VSVSSEMVFE LEGVELGADG
     KVVSYAKFLY PTNALVIHKN DSHGLLPQPR PSIPRAPPGS RHKPVPTKST PAGTELGSDG
     GDAVEYNPNL LDDPQWPCGK HKRVLIFASY MTTVIEYVKP ADLKKDMNET FREKFPHIKL
     TLSKIRSLKR EMRNLSEECS LEPVTVSMAY VYFEKLVLQG KLNKQNRKLC AGACVLLAAK
     ISSDLRKSEV KQLIDKLEER FRFNRKDLIG FEFTVLVALE LALYLPENQV LPHYRRLTQQ
     F
//
ID   K1024_MOUSE             Reviewed;         917 AA.
AC   Q8K3V7; Q69ZS9;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=UPF0258 protein KIAA1024;
DE   AltName: Full=Protein DD1;
GN   Name=Kiaa1024;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6;
RA   Mas C., Meda P.;
RT   "Full length cloning of DD1, a novel gene expressed in brain and in
RT   islets of Langerhans.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K3V7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K3V7-2; Sequence=VSP_013706;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in brain and in islets of
CC       Langerhans.
CC   -!- SIMILARITY: Belongs to the UPF0258 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32367.1; Type=Erroneous initiation;
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DR   EMBL; AF529169; AAM93262.1; -; mRNA.
DR   EMBL; AK035830; BAC29204.1; -; mRNA.
DR   EMBL; AK173089; BAD32367.1; ALT_INIT; Transcribed_RNA.
DR   IPI; IPI00170159; -.
DR   IPI; IPI00556897; -.
DR   RefSeq; NP_705729.1; NM_153509.2.
DR   UniGene; Mm.242899; -.
DR   UniGene; Mm.458520; -.
DR   ProteinModelPortal; Q8K3V7; -.
DR   PRIDE; Q8K3V7; -.
DR   Ensembl; ENSMUST00000044491; ENSMUSP00000046111; ENSMUSG00000039313.
DR   Ensembl; ENSMUST00000113096; ENSMUSP00000108719; ENSMUSG00000039313.
DR   GeneID; 209743; -.
DR   KEGG; mmu:209743; -.
DR   UCSC; uc009qzn.1; mouse.
DR   CTD; 209743; -.
DR   MGI; MGI:2667167; AF529169.
DR   GeneTree; ENSGT00530000063851; -.
DR   HOGENOM; HBG447262; -.
DR   HOVERGEN; HBG052193; -.
DR   InParanoid; Q8K3V7; -.
DR   OMA; QQPEKVS; -.
DR   OrthoDB; EOG437RDG; -.
DR   PhylomeDB; Q8K3V7; -.
DR   NextBio; 372783; -.
DR   ArrayExpress; Q8K3V7; -.
DR   Bgee; Q8K3V7; -.
DR   CleanEx; MM_AF529169; -.
DR   Genevestigator; Q8K3V7; -.
DR   GermOnline; ENSMUSG00000039313; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR009626; UPF0258.
DR   Pfam; PF06789; UPF0258; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    917       UPF0258 protein KIAA1024.
FT                                /FTId=PRO_0000157134.
FT   TRANSMEM    893    913       Helical; (Potential).
FT   CARBOHYD    301    301       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    404    404       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    544    544       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     373    382       Missing (in isoform 2).
FT                                /FTId=VSP_013706.
SQ   SEQUENCE   917 AA;  102792 MW;  065DCB22C917E493 CRC64;
     MEANQEASLF LVKILEELDS KQNTVSYQDL CKSLCAQFDL SQLAKLRSVL FYTACLDPNF
     PATLFKDKMK CSVNNQQSKK IMVAADIVTI FNLIQMNGGT AKEKLPMSCH KVRKKEASFE
     SCRSDTEVCS PTVCEPLNCE LSERPFSRGY PTRQSSKCRK MDCKECPQFV PASEPNFLLG
     VSKEVKNRAA SLDRLQALSP YSVASPQPCE MQRTYFPMNI ENEPMSDQDS LPISQGIKET
     FISSEEPFVV QSCVQKRNIF KEDFHNLMTV SPSLVGTTNK AEEGHGEPQS QKELHKPPFF
     NHSFEMPYHN QYLNPVYSPI PDKRRAKHES LDDLQASTYF GPTPVMGTQD TRRCPGRSSK
     QTPWPAKSWS LNTEEVPDFE RSFFNRNPSE EKLRYPNSGS QTPNFSGPDR HPVYLVPKDQ
     QKVLPAGYAV KPNGLKSKEI SSPVDLEKHE AVKKFKDKSI SCTSGQHSSD TSSVGTQTEQ
     HVLDPPKCKD LCTSGQAKYG DRHAMKQSDD DSEIVSDDIS DIFRFLDDMS ISGSTGVIQS
     SCYNSTGSLS QLHKSDCDSS PEHHLAKITN GVSSGKGDKC NRPENVHHSE EELKSSVCKL
     VLRIGEIERK LESLSGVREE ISQVLGKLNK LDQKIQQPEK VNVQIDLNSL TSEAPSDDSA
     SPRVFRAHSG SHGPKLENSP DWCCSDASGS NSESLRVKAL KKSLFTRPSS RSLTEENSAT
     ESKIASISNS PRDWRTITYT NRMSLNEEEI KDAGPANNKD WHRKSKEADR QYDIPPQHRL
     PKQPKDGFLV EQVFSPHPYP TSLKGHMKSN PLYTDMRLTE LAEVKRGQPS WTIEEYARNS
     GDKGKLTALD LQTQESLNPN NLEYWMEDIY TPGYDSLLKR KEAEFRRAKV CKIAALITAA
     ACTVILVIVV PICTMKS
//
ID   BRE_MOUSE               Reviewed;         383 AA.
AC   Q8K3W0; Q497G6; Q6P8Z2; Q8BKU1; Q8CJ13; Q8JZP0; Q8K3V9; Q8VHN1;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=BRCA1-A complex subunit BRE;
DE   AltName: Full=BRCA1/BRCA2-containing complex subunit 45;
DE   AltName: Full=Brain and reproductive organ-expressed protein;
GN   Name=Bre;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=BALB/c, and C57BL/6 X CBA/N; TISSUE=Heart;
RX   MEDLINE=22927756; PubMed=14565866; DOI=10.1089/10445490360708900;
RA   Ching A.K.K., Li Q., Lim P.L., Chan J.Y.-H., Chui Y.L.;
RT   "Expression of a conserved mouse stress-modulating gene, Bre:
RT   comparison with the human ortholog.";
RL   DNA Cell Biol. 22:497-504(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Embryo, Medulla oblongata, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=Czech II; TISSUE=Kidney, and Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, AND INTERACTION WITH TNFRSF1A.
RX   PubMed=9737713;
RA   Gu C., Castellino A., Chan J.Y.-H., Chao M.V.;
RT   "BRE: a modulator of TNF-alpha action.";
RL   FASEB J. 12:1101-1108(1998).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=21534249; PubMed=11676476; DOI=10.1006/bbrc.2001.5801;
RA   Ching A.K.K., Li P.S., Li Q., Chan B.C.L., Chan J.Y.-H., Lim P.L.,
RA   Pang J.C.S., Chui Y.L.;
RT   "Expression of human BRE in multiple isoforms.";
RL   Biochem. Biophys. Res. Commun. 288:535-545(2001).
CC   -!- FUNCTION: Component of the BRCA1-A complex, a complex that
CC       specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A
CC       and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1
CC       heterodimer to sites of DNA damage at double-strand breaks (DSBs).
CC       The BRCA1-A complex also possesses deubiquitinase activity that
CC       specifically removes 'Lys-63'-linked ubiquitin on histones H2A and
CC       H2AX. In the BRCA1-A complex, it acts as an adapter that bridges
CC       the interaction between MERIT40/NBA1 and the rest of the complex,
CC       thereby being required for the complex integrity and modulating
CC       the E3 ubiquitin ligase activity of the BRCA1-BARD1 heterodimer.
CC       Probably also plays a role as a component of the BRISC complex, a
CC       multiprotein complex that specifically cleaves 'Lys-63'-linked
CC       ubiquitin (By similarity). May regulate TNF-alpha signaling
CC       through its interactions with TNFRSF1A.
CC   -!- SUBUNIT: Component of the BRCA1-A complex, at least composed of
CC       the BRCA1, BARD1, UIMC1/RAP80, FAM175A/Abraxas, BRCC3/BRCC36,
CC       BRE/BRCC45 and MERIT40/NBA1. In the BRCA1-A complex, interacts
CC       directly with FAM175A/Abraxas, BRCC3/BRCC36 and MERIT40/NBA1.
CC       Binds polyubiquitin. Component of the BRISC complex, at least
CC       composed of the FAM175B/ABRO1, BRCC3/BRCC36, BRE/BRCC45 and
CC       MERIT40/NBA1. Component of the BRCA1/BRCA2 containing complex
CC       (BRCC), which also contains BRCA1, BRCA2, BARD1, BRCC3/BRCC36 and
CC       RAD51. BRCC is a ubiquitin E3 ligase complex that enhances
CC       cellular survival following DNA damage. May interact with FAS (By
CC       similarity). Interacts with TNFRSF1A.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Localizes at sites of DNA damage at double-
CC       strand breaks (DSBs) (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC         Comment=Additional isoforms may exist;
CC       Name=2;
CC         IsoId=Q8K3W0-2; Sequence=Displayed;
CC       Name=1; Synonyms=I;
CC         IsoId=Q8K3W0-1; Sequence=VSP_051953;
CC       Name=3; Synonyms=II,II3+;
CC         IsoId=Q8K3W0-4; Sequence=VSP_051952;
CC       Name=4; Synonyms=IV;
CC         IsoId=Q8K3W0-5; Sequence=VSP_037263;
CC       Name=5; Synonyms=III;
CC         IsoId=Q8K3W0-6; Sequence=VSP_037262;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver,
CC       lung, testis, germinal center B-cells and various mouse cell
CC       lines.
CC   -!- DOMAIN: Contains 2 ubiquitin-conjugating enzyme family-like (UEV-
CC       like) regions. These regions lack the critical Cys residues
CC       required for ubiquitination but retain the ability to bind
CC       ubiquitin (By similarity).
CC   -!- SIMILARITY: Belongs to the BRE family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC34385.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
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DR   EMBL; AF440752; AAL40809.1; -; mRNA.
DR   EMBL; AF527952; AAM92774.1; -; mRNA.
DR   EMBL; AF527953; AAM92775.1; -; mRNA.
DR   EMBL; AF527954; AAM92776.1; -; mRNA.
DR   EMBL; AF527955; AAM92777.1; -; mRNA.
DR   EMBL; AF538925; AAN15148.1; -; mRNA.
DR   EMBL; AK050695; BAC34385.1; ALT_SEQ; mRNA.
DR   EMBL; AK080991; BAC38108.1; -; mRNA.
DR   EMBL; AK156929; BAE33900.1; -; mRNA.
DR   EMBL; BC061000; AAH61000.1; -; mRNA.
DR   EMBL; BC100565; AAI00566.1; -; mRNA.
DR   IPI; IPI00128466; -.
DR   IPI; IPI00170162; -.
DR   IPI; IPI00400095; -.
DR   IPI; IPI00400287; -.
DR   IPI; IPI00400376; -.
DR   RefSeq; NP_653124.1; NM_144541.1.
DR   RefSeq; NP_851796.1; NM_181279.1.
DR   RefSeq; NP_851797.1; NM_181280.1.
DR   RefSeq; NP_851798.1; NM_181281.1.
DR   RefSeq; NP_851799.1; NM_181282.1.
DR   UniGene; Mm.120763; -.
DR   STRING; Q8K3W0; -.
DR   PhosphoSite; Q8K3W0; -.
DR   PRIDE; Q8K3W0; -.
DR   Ensembl; ENSMUST00000078891; ENSMUSP00000077929; ENSMUSG00000052139.
DR   Ensembl; ENSMUST00000080598; ENSMUSP00000079434; ENSMUSG00000052139.
DR   Ensembl; ENSMUST00000114507; ENSMUSP00000110152; ENSMUSG00000089895.
DR   GeneID; 107976; -.
DR   KEGG; mmu:107976; -.
DR   UCSC; uc008wza.1; mouse.
DR   UCSC; uc008wzb.1; mouse.
DR   UCSC; uc008wzd.1; mouse.
DR   UCSC; uc008wzf.1; mouse.
DR   CTD; 107976; -.
DR   MGI; MGI:1333875; Bre.
DR   eggNOG; roNOG07019; -.
DR   GeneTree; ENSGT00390000004208; -.
DR   HOVERGEN; HBG071492; -.
DR   InParanoid; Q8K3W0; -.
DR   OrthoDB; EOG4G7BZD; -.
DR   NextBio; 359811; -.
DR   ArrayExpress; Q8K3W0; -.
DR   Bgee; Q8K3W0; -.
DR   CleanEx; MM_BRE; -.
DR   Genevestigator; Q8K3W0; -.
DR   GermOnline; ENSMUSG00000052139; Mus musculus.
DR   GO; GO:0070531; C:BRCA1-A complex; ISS:UniProtKB.
DR   GO; GO:0070552; C:BRISC complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0000152; C:nuclear ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0031593; F:polyubiquitin binding; ISS:UniProtKB.
DR   GO; GO:0005164; F:tumor necrosis factor receptor binding; IDA:UniProtKB.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR   GO; GO:0031572; P:G2/M transition DNA damage checkpoint; ISS:UniProtKB.
DR   GO; GO:0045768; P:positive regulation of anti-apoptosis; ISS:UniProtKB.
DR   GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR   GO; GO:0010212; P:response to ionizing radiation; ISS:UniProtKB.
DR   InterPro; IPR010358; Brain/reproduct-express_prot.
DR   Pfam; PF06113; BRE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Apoptosis; Chromatin regulator;
KW   Cytoplasm; DNA damage; DNA repair; Nucleus; Repeat.
FT   CHAIN         1    383       BRCA1-A complex subunit BRE.
FT                                /FTId=PRO_0000224190.
FT   REGION       30    147       UEV-like 1.
FT   REGION      275    364       UEV-like 2.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     270    270       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1    138       Missing (in isoform 3).
FT                                /FTId=VSP_051952.
FT   VAR_SEQ       1     69       MSPEIALNRISPMLSPFISSVVRNGKVGLDATNCLRITDLK
FT                                SGCTSLTPGPNCDRFKLHIPYAGETLKW -> MCACR (in
FT                                isoform 5).
FT                                /FTId=VSP_037262.
FT   VAR_SEQ       1     43       MSPEIALNRISPMLSPFISSVVRNGKVGLDATNCLRITDLK
FT                                SG -> MCACNEWYGVPDLEKASYLWRKKENHLPLEKGQN
FT                                (in isoform 4).
FT                                /FTId=VSP_037263.
FT   VAR_SEQ      27     43       VGLDATNCLRITDLKSG -> IHEKGPSQKLSFKSCSYHLP
FT                                MCACNEWYGVPDLEKASYLWRKKENHLPLEKGQN (in
FT                                isoform 1).
FT                                /FTId=VSP_051953.
FT   CONFLICT    105    105       W -> R (in Ref. 3; AAH61000).
SQ   SEQUENCE   383 AA;  43545 MW;  7BABA837A8AF82E6 CRC64;
     MSPEIALNRI SPMLSPFISS VVRNGKVGLD ATNCLRITDL KSGCTSLTPG PNCDRFKLHI
     PYAGETLKWD IIFNAQYPEL PPDFIFGEDA EFLPDPSALH NLASWNPSNP ECLLLVVKEL
     VQQYHQFQCG RLRESSRLMF EYQTLLEEPQ YGENMEIYAG KKNNWTGEFS ARFLLKLPVD
     FSNIPTYLLK DVNEDPGEDV ALLSVSFEDT EATQVYPKLY LSPRIEHALG GSSALHIPAF
     PGGGCLIDYV PQVCHLLTNK VQYVIQGYHK RREYIAAFLS HFGTGVVEYD AEGFTKLTLL
     LMWKDFCFLV HIDLPLFFPR DQPTLTFQSV YHFTNSGQLY SQAQKNYPYS PRWDGNEMAK
     RAKAYFKTFV PQFQEAAFAN GKL
//
ID   CASC3_MOUSE             Reviewed;         698 AA.
AC   Q8K3W3; A3KFP7; Q3UT99; Q8K219; Q99NF0;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 3.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Protein CASC3;
DE   AltName: Full=Cancer susceptibility candidate gene 3 protein homolog;
DE   AltName: Full=Metastatic lymph node gene 51 protein homolog;
DE            Short=MLN 51 homolog;
DE   AltName: Full=Protein barentsz;
DE            Short=Btz;
DE            Short=mBtz;
GN   Name=Casc3; Synonyms=Mln51;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=22075525; PubMed=12080473; DOI=10.1038/sj.onc.1205611;
RA   Degot S.F., Regnier C.H., Wendling C., Chenard M.-P., Rio M.-C.,
RA   Tomasetto C.L.;
RT   "Metastatic lymph node 51, a novel nucleo-cytoplasmic protein
RT   overexpressed in breast cancer.";
RL   Oncogene 21:4422-4434(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH STAU1, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF LEU-464.
RC   STRAIN=BALB/c;
RX   PubMed=12843282;
RA   Macchi P., Kroening S., Palacios I.M., Baldassa S., Grunewald B.,
RA   Ambrosino C., Goetze B., Lupas A., St Johnston D., Kiebler M.;
RT   "Barentsz, a new component of the Staufen-containing ribonucleoprotein
RT   particles in mammalian cells, interacts with Staufen in an RNA-
RT   dependent manner.";
RL   J. Neurosci. 23:5778-5788(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 40-697.
RC   STRAIN=Czech II, and FVB/N; TISSUE=Brain, Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Component of a splicing-dependent multiprotein exon
CC       junction complex (EJC) deposited at splice junction on mRNAs. The
CC       EJC is a dynamic structure consisting of a few core proteins and
CC       several more peripheral nuclear and cytoplasmic associated factors
CC       that join the complex only transiently either during EJC assembly
CC       or during subsequent mRNA metabolism. Core components of the EJC,
CC       that remains bound to spliced mRNAs throughout all stages of mRNA
CC       metabolism, functions to mark the position of the exon-exon
CC       junction in the mature mRNA and thereby influences downstream
CC       processes of gene expression including mRNA splicing, nuclear mRNA
CC       export, subcellular mRNA localization, translation efficiency and
CC       nonsense-mediated mRNA decay (NMD). Stimulates the ATPase and RNA-
CC       helicase activities of EIF4A3. Plays a role in the stress response
CC       by participating in cytoplasmic stress granules assembly and by
CC       favouring cell recovery following stress. Binds spliced mRNA in
CC       sequence-independent manner, 20-24 nucleotides upstream of mRNA
CC       exon-exon junctions. Binds poly(G) and poly(U) RNA homopolymer.
CC       Component of the dendritic ribonucleoprotein particles (RNPs) in
CC       hippocampal neurons. May play a role in mRNA transport (By
CC       similarity).
CC   -!- SUBUNIT: Forms homooligomers. Part of the EJC core complex that
CC       contains CASC3, EIF4A3, MAGOH and RBM8A. Found in a mRNA splicing-
CC       dependent exon junction complex (EJC), at least composed of ACIN1,
CC       CASC3, EIF4A3, MAGOH, PNN, RBM8A, RNPS1, SAP18 and THOC4.
CC       Interacts with EIF4A3, MAGOH, NXF1 and RBM8A (By similarity).
CC       Interacts with STAU1 in an RNA-dependent manner.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Nucleus.
CC       Nucleus speckle (By similarity). Note=Travels to the cytoplasm as
CC       part of the exon junction complex (EJC) bound to mRNA. Shuttles
CC       between the cytoplasm and the stress granules. More specifically
CC       found in nuclear intrachromatin granules clusters (IGC), also
CC       called nuclear speckles, which are storage compartments for
CC       nuclear proteins involved in mRNA processing. Colocalizes in
CC       nuclear speckles with MAGOH. Under stress condition, colocalizes
CC       with FMR1 and TIA1, but not MAGOH and RBM8A EJC core factors, in
CC       cytoplasmic stress granules, which contain stored mRNAs whose
CC       translation is stopped in response to stress (By similarity).
CC       Predominantly found in the perinuclear region. Shuttles between
CC       the nucleus and the cytoplasm in a CRM1-dependent manner.
CC   -!- TISSUE SPECIFICITY: High levels in heart, brain, including
CC       hippocampus and cerebellum, liver, kidney and testis; lower levels
CC       in muscle, lung and spleen.
CC   -!- DOMAIN: The coiled coil domain may be involved in oligomerization
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the CASC3 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH60672.1; Type=Erroneous initiation;
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DR   EMBL; AF526276; AAM88396.1; -; mRNA.
DR   EMBL; AJ292072; CAC27775.1; -; mRNA.
DR   EMBL; AK139608; BAE24081.1; -; mRNA.
DR   EMBL; AL590963; CAM46181.1; -; Genomic_DNA.
DR   EMBL; CH466556; EDL16170.1; -; Genomic_DNA.
DR   EMBL; BC034533; AAH34533.1; -; mRNA.
DR   EMBL; BC060672; AAH60672.1; ALT_INIT; mRNA.
DR   EMBL; BC141296; AAI41297.1; -; mRNA.
DR   IPI; IPI00877339; -.
DR   RefSeq; NP_619601.2; NM_138660.2.
DR   UniGene; Mm.40120; -.
DR   ProteinModelPortal; Q8K3W3; -.
DR   SMR; Q8K3W3; 165-245.
DR   STRING; Q8K3W3; -.
DR   PhosphoSite; Q8K3W3; -.
DR   PRIDE; Q8K3W3; -.
DR   Ensembl; ENSMUST00000017384; ENSMUSP00000017384; ENSMUSG00000078676.
DR   GeneID; 192160; -.
DR   KEGG; mmu:192160; -.
DR   UCSC; uc007lhp.1; mouse.
DR   CTD; 192160; -.
DR   MGI; MGI:2179723; Casc3.
DR   GeneTree; ENSGT00390000006930; -.
DR   HOGENOM; HBG715340; -.
DR   HOVERGEN; HBG050799; -.
DR   InParanoid; Q8K3W3; -.
DR   OMA; RSGGFKE; -.
DR   OrthoDB; EOG4P5K9B; -.
DR   ArrayExpress; Q8K3W3; -.
DR   Bgee; Q8K3W3; -.
DR   CleanEx; MM_CASC3; -.
DR   Genevestigator; Q8K3W3; -.
DR   GermOnline; ENSMUSG00000052915; Mus musculus.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030529; C:ribonucleoprotein complex; IDA:MGI.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008298; P:intracellular mRNA localization; IDA:MGI.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR018545; CASC3/Barentsz_eIF4AIII-bd.
DR   Pfam; PF09405; Btz; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; mRNA processing; mRNA splicing;
KW   mRNA transport; Nonsense-mediated mRNA decay; Nucleus; Phosphoprotein;
KW   RNA-binding; Stress response; Translation regulation; Transport.
FT   CHAIN         1    698       Protein CASC3.
FT                                /FTId=PRO_0000089325.
FT   REGION      134    280       Necessary for RNA-binding, interaction
FT                                with MAGOH and localization in nucleus
FT                                speckles (By similarity).
FT   REGION      134    280       Sufficient to form the EJC (By
FT                                similarity).
FT   REGION      374    698       Necessary for localization in cytoplasmic
FT                                stress granules (By similarity).
FT   COILED       98    127       Potential.
FT   MOTIF       201    207       Nuclear localization signal 1
FT                                (Potential).
FT   MOTIF       251    259       Nuclear localization signal 2
FT                                (Potential).
FT   MOTIF       457    466       Nuclear export signal.
FT   COMPBIAS     40     45       Poly-Gly.
FT   COMPBIAS    638    642       Poly-Pro.
FT   COMPBIAS    686    689       Poly-Pro.
FT   MOD_RES      36     36       Phosphoserine (By similarity).
FT   MOD_RES      44     44       Phosphoserine (By similarity).
FT   MOD_RES     145    145       Phosphoserine.
FT   MOD_RES     263    263       Phosphoserine.
FT   MOD_RES     360    360       Phosphoserine.
FT   MOD_RES     370    370       Phosphoserine (By similarity).
FT   MOD_RES     472    472       Phosphoserine (By similarity).
FT   MUTAGEN     464    464       L->A: Accumulation in the nucleus.
FT   CONFLICT    297    297       N -> D (in Ref. 3; BAE24081).
FT   CONFLICT    474    474       S -> G (in Ref. 6; AAH34533).
FT   CONFLICT    589    589       L -> V (in Ref. 3; BAE24081).
FT   CONFLICT    638    638       Missing (in Ref. 2; CAC27775 and 6;
FT                                AAH60672).
SQ   SEQUENCE   698 AA;  75770 MW;  3B718FC297A5E0F3 CRC64;
     MADRRRQRAS QDTEDEESGA SGSDSGSPAR GGGSCSGSVG GGGSGSLPSQ RGGRGGGLHL
     RRVESGGAKS AEESECESED GMEGDAVLSD YESAEDSEGE EDYSEEENSK VELKSEANDA
     ADSSAKEKGE EKPESKGTVT GERQSGDGQE STEPVENKVG KKGPKHLDDD EDRKNPAYIP
     RKGLFFEHDL RGQTQEEEVR PKGRQRKLWK DEGRWEHDKF REDEQAPKSR QELIALYGYD
     IRSAHNPDDI KPRRIRKPRF GSSPQRDPNW IGDRSSKSHR HQGPGGNLPP RTFINRNTAG
     TGRMSASRNY SRSGGFKDGR TSFRPVEVAG QHGGRSAETL KHEASYRSRR LEQTPVRDPS
     PEPDAPLLGS PEKEEVASET PAAVPDITPP APDRPIEKKS YSRARRTRTK VGDAVKAAEE
     VPPPSEGLAS TATVPETTPA AKTGNWEAPV DSTTGGLEQD VAQLNIAEQS WSPSQPSFLQ
     PRELRGVPNH IHMGAGPPPQ FNRMEEMGVQ SGRAKRYSSQ RQRPVPEPPA PPVHISIMEG
     HYYDPLQFQG PIYTHGDSPA PLPPQGMIVQ PEMHLPHPGL HPHQSPGPLP NPGLYPPPVS
     MSPGQPPPQQ LLAPTYFSAP GVMNFGNPNY PYAPGALPPP PPPHLYPNTQ APPQVYGGVT
     YYNPAQQQVQ PKPSPPRRTP QPVSIKPPPP EVVSRGSS
//
ID   EAP1_MOUSE              Reviewed;         775 AA.
AC   Q8K3X4; Q3TBU9; Q3U483; Q3USE5; Q69Z84; Q8BUS1; Q8C011;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Enhanced at puberty protein 1;
GN   Name=Eap1; Synonyms=Kiaa1865;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Heart;
RA   Chen X.G., Li Y.;
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Dendritic cell, Eye, Medulla oblongata, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-636; SER-637;
RP   SER-638 AND SER-641, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195 AND SER-526, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May contribute to the control of female reproductive
CC       function. May play a role in gene transcription by transactivating
CC       GNRH1 promoter and repressing PENK promoter (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the IRF2BP family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32560.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF525300; AAM82165.1; -; mRNA.
DR   EMBL; AK173282; BAD32560.1; ALT_INIT; mRNA.
DR   EMBL; AK032366; BAC27837.1; -; mRNA.
DR   EMBL; AK032622; BAC27955.1; -; mRNA.
DR   EMBL; AK082791; BAC38621.1; -; mRNA.
DR   EMBL; AK140441; BAE24388.1; -; mRNA.
DR   EMBL; AK154383; BAE32550.1; -; mRNA.
DR   EMBL; AK155373; BAE33226.1; -; mRNA.
DR   EMBL; AK171043; BAE42208.1; -; mRNA.
DR   EMBL; BC057128; AAH57128.1; -; mRNA.
DR   EMBL; BC063253; AAH63253.1; -; mRNA.
DR   IPI; IPI00469941; -.
DR   RefSeq; NP_665835.1; NM_145836.2.
DR   UniGene; Mm.248358; -.
DR   ProteinModelPortal; Q8K3X4; -.
DR   SMR; Q8K3X4; 685-765.
DR   STRING; Q8K3X4; -.
DR   PhosphoSite; Q8K3X4; -.
DR   PRIDE; Q8K3X4; -.
DR   Ensembl; ENSMUST00000038422; ENSMUSP00000041070; ENSMUSG00000034168.
DR   GeneID; 238330; -.
DR   KEGG; mmu:238330; -.
DR   UCSC; uc007oia.1; mouse.
DR   MGI; MGI:2442463; 6430527G18Rik.
DR   eggNOG; maNOG14379; -.
DR   GeneTree; ENSGT00390000005089; -.
DR   HOVERGEN; HBG108364; -.
DR   InParanoid; Q8K3X4; -.
DR   OMA; SGVAKQM; -.
DR   OrthoDB; EOG4H9XMB; -.
DR   PhylomeDB; Q8K3X4; -.
DR   NextBio; 383739; -.
DR   PMAP-CutDB; Q8K3X4; -.
DR   ArrayExpress; Q8K3X4; -.
DR   Bgee; Q8K3X4; -.
DR   CleanEx; MM_6430527G18RIK; -.
DR   Genevestigator; Q8K3X4; -.
DR   GermOnline; ENSMUSG00000034168; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR022750; Interferon_reg_fac2-bd1_2.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF11261; IRF-2BP1_2; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Nucleus; Phosphoprotein.
FT   CHAIN         1    775       Enhanced at puberty protein 1.
FT                                /FTId=PRO_0000056412.
FT   REGION      694    746       Cys-rich.
FT   COILED       83    113       Potential.
FT   COILED      314    350       Potential.
FT   COMPBIAS     88     95       Poly-Ala.
FT   COMPBIAS     96    108       Poly-Gln.
FT   COMPBIAS    134    144       Poly-Ala.
FT   COMPBIAS    154    282       Pro-rich.
FT   COMPBIAS    575    602       Pro-rich.
FT   MOD_RES      69     69       Phosphoserine (By similarity).
FT   MOD_RES     195    195       Phosphoserine.
FT   MOD_RES     207    207       Phosphoserine.
FT   MOD_RES     526    526       Phosphoserine.
FT   MOD_RES     636    636       Phosphoserine.
FT   MOD_RES     637    637       Phosphoserine.
FT   MOD_RES     638    638       Phosphoserine.
FT   MOD_RES     641    641       Phosphoserine.
FT   MOD_RES     644    644       Phosphoserine (By similarity).
FT   CONFLICT    226    226       G -> E (in Ref. 3; BAC38621).
FT   CONFLICT    227    227       G -> E (in Ref. 3; BAE32550).
FT   CONFLICT    330    330       A -> P (in Ref. 3; BAC27955).
FT   CONFLICT    442    442       E -> G (in Ref. 3; BAC27955).
FT   CONFLICT    619    619       P -> S (in Ref. 3; BAE33226/BAE42208).
SQ   SEQUENCE   775 AA;  80565 MW;  ECB11652F2F7C2AB CRC64;
     MSAAQVSSSR RQSCYLCDLP RMPWAMIWDF SEPVCRGCVN YEGADRIEFV IETARQLKRA
     HGCFQDGRSP GPPPPVGVKT VALSAKEAAA AAAAAQQQQQ QQQQQQQQLN HVDGSTKPAV
     LAAPSGLERY GLSAAAAAAA AAAAVEQRSR FEYPPPPVSL GSSSHAARLP NGLGGPNGFP
     KPAPEEGPPE LNRQSPNSSS AATSVASRRG THSGLVTGLP NPGGGGGPQL TVPPNLLPQT
     LLNGPASAAV LPPPHGLGGS RGPPTPAPPG APGGPACLGG PPGVSATVSS APSSTSSTVA
     EVGVGAAGKR PGSVSSTDQE RELKEKQRNA EALAELSESL RNRAEEWANK PKMVRDTLLT
     LAGCTPYEVR FKKDHSLLGR VFAFDAVSKP GMDYELKLFI EYPTGSGNVY SSASGVAKQM
     YQDCMKDFGR GLSSGFKYLE YEKKHGSGDW RLLGDLLPEA VRFFKEGVPG ADMLPQPYLD
     ASCPMLPTAL VSLSRAPSAP PGTGALPPAA PTGRGAASSL RKRKASPEPP DSAESALKLG
     EEQQRQQWMA NQSEALKLTM SAGGFAAPGH SAGGPPPPPP PLGPHSNRTT PPESAPQNGP
     SPMAALMSVA DTLGTAHSPK DGSSVHSTTA SARRNSSSPV SPASVPGQRR LASRNGDLNL
     QVAPPPPSAH PGMDQVHPQN IPDSPMANSG PLCCTICHER LEDTHFVQCP SVPSHKFCFP
     CSRESIKAQG ATGEVYCPSG EKCPLVGSNV PWAFMQGEIA TILAGDVKVK KERDP
//
ID   PO121_MOUSE             Reviewed;        1200 AA.
AC   Q8K3Z9; Q7TSH5;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   08-FEB-2011, entry version 66.
DE   RecName: Full=Nuclear envelope pore membrane protein POM 121;
DE   AltName: Full=Nucleoporin Nup121;
DE   AltName: Full=Pore membrane protein of 121 kDa;
GN   Name=Pom121; Synonyms=Nup121;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Tassabehji M., Cunliffe P.;
RT   "Identification of mouse genes mapping to the Williams syndrome
RT   critical region.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319; SER-322; SER-325
RP   AND SER-409, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Essential component of the nuclear pore complex (NPC).
CC       The repeat-containing domain may be involved in anchoring
CC       components of the pore complex to the pore membrane. When
CC       overexpressed in cells induces the formation of cytoplasmic
CC       annulate lamellae (AL) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex (By
CC       similarity). Nucleus membrane; Single-pass membrane protein (By
CC       similarity). Endoplasmic reticulum membrane; Single-pass membrane
CC       protein (By similarity). Note=Stably associated with the NPC
CC       throughout interphase and the endoplasmic reticulum during
CC       metaphase (By similarity).
CC   -!- DOMAIN: Contains F-X-F-G repeats.
CC   -!- PTM: Proteolytically cleaved by caspase-3 during apoptosis (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the POM121 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF516680; AAM64199.1; -; mRNA.
DR   EMBL; BC053101; AAH53101.1; -; mRNA.
DR   IPI; IPI00380737; -.
DR   RefSeq; NP_683734.2; NM_148932.2.
DR   UniGene; Mm.28399; -.
DR   ProteinModelPortal; Q8K3Z9; -.
DR   STRING; Q8K3Z9; -.
DR   PhosphoSite; Q8K3Z9; -.
DR   PRIDE; Q8K3Z9; -.
DR   Ensembl; ENSMUST00000111171; ENSMUSP00000106801; ENSMUSG00000053293.
DR   GeneID; 107939; -.
DR   KEGG; mmu:107939; -.
DR   UCSC; uc008zyi.1; mouse.
DR   CTD; 107939; -.
DR   MGI; MGI:2137624; Pom121.
DR   GeneTree; ENSGT00550000074606; -.
DR   HOGENOM; HBG506844; -.
DR   HOVERGEN; HBG053628; -.
DR   InParanoid; Q8K3Z9; -.
DR   OMA; ATFGSSA; -.
DR   PhylomeDB; Q8K3Z9; -.
DR   NextBio; 359749; -.
DR   ArrayExpress; Q8K3Z9; -.
DR   Bgee; Q8K3Z9; -.
DR   CleanEx; MM_POM121; -.
DR   Genevestigator; Q8K3Z9; -.
DR   GermOnline; ENSMUSG00000053293; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Membrane; mRNA transport; Nuclear pore complex;
KW   Nucleus; Phosphoprotein; Protein transport; Repeat; Translocation;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1   1200       Nuclear envelope pore membrane protein
FT                                POM 121.
FT                                /FTId=PRO_0000204907.
FT   TRANSMEM     57     77       Helical; (Potential).
FT   REGION        1     56       Cisternal side (Potential).
FT   REGION       76   1200       Pore side (Potential).
FT   COMPBIAS      4      8       Poly-Ala.
FT   COMPBIAS     53     58       Poly-Ala.
FT   COMPBIAS    438    441       Poly-Ser.
FT   COMPBIAS    497    500       Poly-Pro.
FT   COMPBIAS    685    688       Poly-Ser.
FT   COMPBIAS    719    722       Poly-Ser.
FT   COMPBIAS   1035   1040       Poly-Ser.
FT   SITE        531    532       Cleavage; by caspase-3 (By similarity).
FT   MOD_RES     319    319       Phosphoserine.
FT   MOD_RES     322    322       Phosphoserine.
FT   MOD_RES     325    325       Phosphoserine.
FT   MOD_RES     355    355       Phosphoserine.
FT   MOD_RES     363    363       Phosphoserine (By similarity).
FT   MOD_RES     366    366       Phosphoserine (By similarity).
FT   MOD_RES     367    367       Phosphoserine (By similarity).
FT   MOD_RES     370    370       Phosphoserine (By similarity).
FT   MOD_RES     409    409       Phosphoserine.
FT   CONFLICT    500    500       Missing (in Ref. 1; AAM64199).
SQ   SEQUENCE   1200 AA;  121022 MW;  C15B5D6C204D445E CRC64;
     MSPAAAAADG GERRRPPLGG REGRSRARGY GGPAGAAALG LALLGLALYL VPAAAALAWL
     AVGASAAWWG LSREPRGPRA LSSFVRDARR HPRPALTASP PPAKSPVNGS LCEPRSPLGG
     PDPAELLLMG SYLGKPGPPE PALRQDPRER PGRRPPARSP PPASAVQRVH HVYPALPTPL
     LRPSRRPPHR DCGPLSSRFV ITPRRRYPIQ QAQYSLLGAL PTVCWNGGHK KAVLSPRNSR
     MVCSPVTVRI APPDSKLFRS SMSEQILDTT LSSPSSNAPD PCAKETVLNA LKEKKKRTVA
     EEDQLHLDGQ ENKRRRHDSG GSGHSAFEPL VANGVPAAFV PKPGSLKRSL ASQSSDDHLN
     KRSRTSSVSS LASACTGGIP SSSRNAITSS YSSTRGISQL WKRSGPTSSP FSSPASSRSQ
     TPERPAKKTR EEEPCQQSSS SPPLVTDKES PGEKVTDTTT GKQQSSWTSP PTPGSSGQRK
     RKIQLLPSRR GDQLTLPPPP ELGYSITAED LDMERKASLQ WFNKVLEDKP DDASASATDG
     PPSTSPPFTF TLPAVGPAAS PASLPAPSSN PLLESLKKMQ ESPAPSSSEP AEAATVAAPS
     PPKTPSLLAP LVSPLAGPLA STSSDSKPAA TFLGLASASS ITPLTDSKSS GVSQAEQSVS
     TPASTASSPT PKPSMLFGML SPPASSSSLA TPAPACASPM FKPIFPATPK SESDSPLPSS
     SSAATTASSS TAPPTAASTT PTFKPIFDKM EPFTAMPLST PFSLKQTTAT ATTTATSAPL
     FTGLGTATST VASGTAASAS KPVFGFGVTT AASTASSTMT STSQSVLFGG APPVTTSSSA
     PALASIFQFG KPLAPAASAA GTSFSQPLAS STQTAASNSG FSGFGSTLTT STSAPATTSQ
     PTLTFSNTVT PTFNIPFSSS AKPALPTYPG ANSQPTFGAT DGATKPALAP SFGSSFTFGN
     SVASAPSAAP APATFGSAAQ PAFGGLKAAA STFGAPASTQ PAFGSTTSVF SFGSATTSGF
     GAAATAATTT QTTNSGSSSS LFGSSAPSPF TFGGSAAPAG SGGFGLSATP GTSSTSGTFS
     FGSGQSGTPG TTTSFGSLSQ NTLGAPSQGS PFAFSVGSTP ESKPVFGGTS TPTFGQSAPA
     PGVGTTGSSL SFGASSTPAQ GFVGVGPFGS AAPSFSIGAG SKTPGARQRL QARRQHTRKK
//
ID   STXB5_MOUSE             Reviewed;        1152 AA.
AC   Q8K400; Q80TM5; Q8K401; Q9D2F3;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Syntaxin-binding protein 5;
DE   AltName: Full=Lethal(2) giant larvae protein homolog 3;
DE   AltName: Full=Tomosyn-1;
GN   Name=Stxbp5; Synonyms=Kiaa4253, Llgl3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
RP   STX1A AND STX4A, IDENTIFICATION IN A COMPLEX WITH STX4A AND SNAP23,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=Swiss albino; TISSUE=Adipocyte;
RX   MEDLINE=22841120; PubMed=12832401; DOI=10.1074/jbc.M304261200;
RA   Widberg C.H., Bryant N.J., Girotti M., Rea S., James D.E.;
RT   "Tomosyn interacts with the t-SNAREs syntaxin4 and SNAP23 and plays a
RT   role in insulin-stimulated GLUT4 translocation.";
RL   J. Biol. Chem. 278:35093-35101(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 892-1152.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
RX   PubMed=15659226; DOI=10.1111/j.1471-4159.2004.02890.x;
RA   Groffen A.J.A., Jacobsen L., Schut D., Verhage M.;
RT   "Two distinct genes drive expression of seven tomosyn isoforms in the
RT   mammalian brain, sharing a conserved structure with a unique variable
RT   domain.";
RL   J. Neurochem. 92:554-568(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1059, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783 AND SER-786, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Plays a regulatory role in calcium-dependent exocytosis
CC       and neurotransmitter release (By similarity). Inhibits membrane
CC       fusion between transport vesicles and the plasma membrane. May
CC       modulate the assembly of trans-SNARE complexes between transport
CC       vesicles and the plasma membrane. Competes with STXBP1 for STX1
CC       binding. Inhibits translocation of GLUT4 from intracellular
CC       vesicles to the plasma membrane.
CC   -!- SUBUNIT: Part of a complex that contains STX1, STXBP5, SNAP25 and
CC       SYT1 (By similarity). Interacts with STX1A and STX4A via its v-
CC       SNARE homology domain. Part of a complex that contains STXBP5,
CC       STX4A and SNAP23.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral
CC       membrane protein. Membrane; Peripheral membrane protein.
CC       Note=Cytoplasmic, and associated with vesicular membranes and the
CC       plasma membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K400-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K400-2; Sequence=VSP_016206;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Detected in heart, spleen, lung, skeletal
CC       muscle, liver and kidney (at protein level). Detected in brain,
CC       particularly in the olfactory bulb and in hippocampus. Detected in
CC       the tenia tecta and in the piriform layer of the brain cortex.
CC   -!- SIMILARITY: Belongs to the WD repeat L(2)GL family.
CC   -!- SIMILARITY: Contains 1 v-SNARE coiled-coil homology domain.
CC   -!- SIMILARITY: Contains 14 WD repeats.
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DR   EMBL; AF516607; AAM61881.1; -; mRNA.
DR   EMBL; AF516608; AAM61882.1; -; mRNA.
DR   EMBL; AK019788; BAB31853.1; -; mRNA.
DR   EMBL; AK122417; BAC65699.1; -; mRNA.
DR   IPI; IPI00656317; -.
DR   IPI; IPI00674768; -.
DR   UniGene; Mm.331751; -.
DR   ProteinModelPortal; Q8K400; -.
DR   SMR; Q8K400; 194-271, 505-532, 1088-1144.
DR   MINT; MINT-269206; -.
DR   STRING; Q8K400; -.
DR   PhosphoSite; Q8K400; -.
DR   PRIDE; Q8K400; -.
DR   Ensembl; ENSMUST00000038213; ENSMUSP00000044535; ENSMUSG00000019790.
DR   UCSC; uc007eiy.1; mouse.
DR   UCSC; uc007eiz.1; mouse.
DR   MGI; MGI:1926058; Stxbp5.
DR   eggNOG; roNOG14128; -.
DR   GeneTree; ENSGT00390000000018; -.
DR   HOVERGEN; HBG083064; -.
DR   OrthoDB; EOG4JHCDX; -.
DR   PhylomeDB; Q8K400; -.
DR   ArrayExpress; Q8K400; -.
DR   Bgee; Q8K400; -.
DR   CleanEx; MM_STXBP5; -.
DR   Genevestigator; Q8K400; -.
DR   GermOnline; ENSMUSG00000019790; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005892; C:nicotinic acetylcholine-gated receptor-channel complex; IDA:MGI.
DR   GO; GO:0017075; F:syntaxin-1 binding; IPI:MGI.
DR   GO; GO:0006887; P:exocytosis; IDA:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000664; Lethal2_giant.
DR   InterPro; IPR013905; Lgl_C.
DR   InterPro; IPR013577; LLGL2.
DR   InterPro; IPR001388; Synaptobrevin.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 3.
DR   Pfam; PF08596; Lgl_C; 1.
DR   Pfam; PF08366; LLGL; 1.
DR   Pfam; PF00400; WD40; 2.
DR   PRINTS; PR00962; LETHAL2GIANT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40_like; 2.
DR   PROSITE; PS50892; V_SNARE; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW   Exocytosis; Membrane; Phosphoprotein; Protein transport; Repeat;
KW   Transport; WD repeat.
FT   CHAIN         1   1152       Syntaxin-binding protein 5.
FT                                /FTId=PRO_0000051245.
FT   REPEAT       62     95       WD 1.
FT   REPEAT      102    141       WD 2.
FT   REPEAT      146    182       WD 3.
FT   REPEAT      201    235       WD 4.
FT   REPEAT      241    273       WD 5.
FT   REPEAT      295    337       WD 6.
FT   REPEAT      345    379       WD 7.
FT   REPEAT      401    478       WD 8.
FT   REPEAT      506    620       WD 9.
FT   REPEAT      634    696       WD 10.
FT   REPEAT      795    852       WD 11.
FT   REPEAT      861    935       WD 12.
FT   REPEAT      940    984       WD 13.
FT   REPEAT      998   1021       WD 14.
FT   DOMAIN     1087   1147       v-SNARE coiled-coil homology.
FT   COMPBIAS     22     28       Poly-Gln.
FT   COMPBIAS    585    591       Poly-Ser.
FT   MOD_RES     724    724       Phosphoserine; by PKA (By similarity).
FT   MOD_RES     760    760       Phosphoserine (By similarity).
FT   MOD_RES     763    763       Phosphothreonine (By similarity).
FT   MOD_RES     783    783       Phosphoserine.
FT   MOD_RES     785    785       Phosphothreonine (By similarity).
FT   MOD_RES     786    786       Phosphoserine.
FT   MOD_RES    1059   1059       Phosphoserine.
FT   VAR_SEQ       1    754       Missing (in isoform 2).
FT                                /FTId=VSP_016206.
FT   CONFLICT    225    225       D -> E (in Ref. 1; AAM61882).
FT   CONFLICT    238    238       D -> G (in Ref. 1; AAM61881).
FT   CONFLICT    247    247       H -> Y (in Ref. 1; AAM61881).
FT   CONFLICT    271    271       A -> T (in Ref. 1; AAM61881).
FT   CONFLICT    301    301       F -> L (in Ref. 1; AAM61882).
FT   CONFLICT    811    811       S -> F (in Ref. 2).
SQ   SEQUENCE   1152 AA;  127656 MW;  986C066058C630BD CRC64;
     MRKFNIRKVL DGLTAGSSSA SQQQQQQQHP PGNREPEIQE TLQSEHFQLC KTVRHGFPYQ
     PSALAFDPVQ KILAVGTQTG ALRLFGRPGA ECYCQHDSGA AVIQLQFLIN EGALVSALAD
     DTLHLWNLRQ KRPAVLHSLK FCRERVTFCH LPFQSKWLYV GTERGNIHIV NVESFTLSGY
     VIMWNKAIEL SSKSHPGPVV HISDNPMDEG KLPIGFESGT VVLWDLKSKK ADYRYTYDEA
     IHSVAWHHEG KQFICSHSDG TLTIWNVRSP AKPVQTITPH GKQLKDGKKP EPCKPILKVE
     FKTTRSGEPF IILSGGLSYD TVGRRPCLTV MHGKSTAVLE MDYSIVDFLT LCETPYPNDF
     QEPYAVVVLL EKDLVLIDLA QNGYPIFENP YPLSIHESPV TCCEYFADCP VDLIPALYSV
     GARQKRQGYS KKEWPINGGN WGLGAQSYPE IIITGHADGS VKFWDASAIT LQVLYKLKTS
     KVFEKSRNKD DRQNTDIVDE DPYAIQIISW CPESRMLCIA GVSAHVIIYR FSKQEVLTEV
     IPMLEVRLLY EINDVDTPEG EQPPPLSTPV GSSNPQPIPP QSHPSTSSSS SDGLRDNVPC
     LKVKNSPLKQ SPGYQTELVI QLVWVGGEPP QQITSLALNS SYGLVVFGNC NGIAMVDYLQ
     KAVLLNLSTI ELYGSNDPYR REPRSPRKSR QPSGAGLCDI TEGTVVPEDR CKSPTSGSSS
     PHNSDDEQKV NNFIEKVKTQ SRKFSKMVAN DLAKMSRKLS LPTDLKPDLD VKDNSFSRSR
     SSSVTSIDKE SRETISALHF CETLTRKADS SPSPCLWVGT TVGTAFVITL NLPPGPEQRL
     LQPVIVSPSG TILRLKGAIL RMAFLDATGC LMSPAYEPWK EHNVAEEKDE KEKLKKRRPV
     SVSPSSSQEI SENQYAVICS EKQAKVMSLP TQSCAYKQNI TETSFVLRGD IVALSNSVCL
     ACFCANGHIM TFSLPSLRPL LDVYYLPLTN MRIARTFCFA NNGQALYLVS PTEIQRLTYS
     QETCENLQEM LGELFTPVET PEAPNRGFFK GLFGGGAQSL DREELFGESS SGKASRSLAQ
     HIPGPGGIEG VKGAASGVVG ELARARLALD ERGQKLSDLE ERTAAMMSSA DSFSKHAHEM
     MLKYKDKKWY QF
//
ID   ADA32_MOUSE             Reviewed;         750 AA.
AC   Q8K410; Q6P901; Q8BJ80;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 2.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 32;
DE            Short=ADAM 32;
DE   Flags: Precursor;
GN   Name=Adam32;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=ICR; TISSUE=Testis;
RX   MEDLINE=22456603; PubMed=12568724; DOI=10.1016/S0378-1119(02)01202-7;
RA   Choi I., Woo J.-M., Hong S., Jung Y.-K., Kim D.H., Cho C.;
RT   "Identification and characterization of ADAM32 with testis-predominant
RT   gene expression.";
RL   Gene 304:151-162(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in sperm development and fertilization
CC       This is a non-catalytic metalloprotease-like protein.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K410-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K410-2; Sequence=VSP_012051, VSP_012052;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in the testis and weakly
CC       expressed in the epididymis, brain and heart.
CC   -!- DEVELOPMENTAL STAGE: First detected in the testis at day 16 and
CC       was reached to the adult level by day 30 after birth.
CC   -!- SIMILARITY: Contains 1 disintegrin domain.
CC   -!- SIMILARITY: Contains 1 EGF-like domain.
CC   -!- SIMILARITY: Contains 1 peptidase M12B domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF513715; AAN03858.1; -; mRNA.
DR   EMBL; AK005759; BAC25124.1; -; mRNA.
DR   EMBL; BC060983; AAH60983.1; -; mRNA.
DR   IPI; IPI00271489; -.
DR   IPI; IPI00403257; -.
DR   RefSeq; NP_700446.2; NM_153397.2.
DR   UniGene; Mm.269223; -.
DR   ProteinModelPortal; Q8K410; -.
DR   SMR; Q8K410; 174-619, 626-658.
DR   MEROPS; M12.960; -.
DR   PhosphoSite; Q8K410; -.
DR   PRIDE; Q8K410; -.
DR   Ensembl; ENSMUST00000041257; ENSMUSP00000046737; ENSMUSG00000037437.
DR   Ensembl; ENSMUST00000110649; ENSMUSP00000106279; ENSMUSG00000037437.
DR   Ensembl; ENSMUST00000121438; ENSMUSP00000113627; ENSMUSG00000037437.
DR   GeneID; 353188; -.
DR   KEGG; mmu:353188; -.
DR   UCSC; uc009lfh.1; mouse.
DR   UCSC; uc009lfi.1; mouse.
DR   CTD; 353188; -.
DR   MGI; MGI:2653822; Adam32.
DR   eggNOG; maNOG15391; -.
DR   GeneTree; ENSGT00590000082741; -.
DR   HOGENOM; HBG507118; -.
DR   HOVERGEN; HBG103628; -.
DR   InParanoid; Q8K410; -.
DR   OMA; SYDDPKK; -.
DR   OrthoDB; EOG49CQ78; -.
DR   NextBio; 400335; -.
DR   ArrayExpress; Q8K410; -.
DR   Bgee; Q8K410; -.
DR   CleanEx; MM_ADAM32; -.
DR   Genevestigator; Q8K410; -.
DR   GermOnline; ENSMUSG00000037437; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR001762; Blood-coag_inhib_Disintegrin.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   Gene3D; G3DSA:4.10.70.10; Blood-coag_inhib_Disintegrin; 1.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SMART; SM00181; EGF; 1.
DR   SUPFAM; SSF57552; Disintegrin; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; FALSE_NEG.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS00022; EGF_1; FALSE_NEG.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cleavage on pair of basic residues;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW   Phosphoprotein; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     18       Potential.
FT   PROPEP       19    172       Potential.
FT                                /FTId=PRO_0000029140.
FT   CHAIN       173    750       Disintegrin and metalloproteinase domain-
FT                                containing protein 32.
FT                                /FTId=PRO_0000029141.
FT   TOPO_DOM    173    685       Extracellular (Potential).
FT   TRANSMEM    686    706       Helical; (Potential).
FT   TOPO_DOM    707    750       Cytoplasmic (Potential).
FT   DOMAIN      183    380       Peptidase M12B.
FT   DOMAIN      387    479       Disintegrin.
FT   DOMAIN      624    656       EGF-like.
FT   COMPBIAS    480    502       Cys-rich.
FT   MOD_RES      19     19       Phosphoserine (By similarity).
FT   CARBOHYD    122    122       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    358    358       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    465    465       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    566    566       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    567    567       N-linked (GlcNAc...) (Potential).
FT   DISULFID    292    375       By similarity.
FT   DISULFID    334    359       By similarity.
FT   DISULFID    336    341       By similarity.
FT   DISULFID    450    471       By similarity.
FT   DISULFID    628    638       By similarity.
FT   DISULFID    632    644       By similarity.
FT   DISULFID    646    655       By similarity.
FT   VAR_SEQ       1      1       M -> MLGAM (in isoform 2).
FT                                /FTId=VSP_012051.
FT   VAR_SEQ     637    750       VCNSHGVCHCNAGYSPPNCQYPTTKRSASLWSGKHDLPMER
FT                                ASKNQEKKWLLSLYIVLIILASVFLIGTGWKGLKQCGSKEE
FT                                ESMSSESKSEDSTYTYVSRSTSETSSMTSTSS -> KQIRR
FT                                QHLHVCQQVSSLKDGVKRHVENEHHNFQPINF (in
FT                                isoform 2).
FT                                /FTId=VSP_012052.
FT   CONFLICT    357    357       S -> I (in Ref. 1; AAN03858).
FT   CONFLICT    724    724       E -> K (in Ref. 3; AAH60983).
SQ   SEQUENCE   750 AA;  83612 MW;  2844626CE3C4B24D CRC64;
     MLHTLLLLLL AELGALLASG PESQSSFLEI IFPEKIEDKT HSEEQISYII PINKKQYTVH
     LQKRYFLTNR FMVYMYNQGS TSFHSPNIPA QCYYQGHIKG YPNSVATLST CSGLRGFLQF
     ENVSYGIEPL QSAFTSQHIV YKLGNKEKEL IFNKNSRNIE MPTNYGILIN KKPKSPFKNL
     FPLYLEMSIV VDKALYDYLG SDSNIVTNKI IEIISLINSV FAQLKVTIVL SSLELWSDKN
     KIPTVGEADE LLHKFLEWKQ AYLTLRPHDV AYLFIYNEYP NYMGATYPGK MCTAHYSAGI
     TMYPKDMTLE AFSVILTQML GLSLGISYDE PEKCYCSESI CIMNPRAMQY GGVKSFSNCS
     LNDFEHFKSN EGAKCLQNKP QMQRTAAAVC GNGKVEGDEI CDCGSEAECG PDSCCEPNRC
     VLKAGRACDS KSPSSTCCKN CQFLPEKHQC RPEKHLYCDI PEVCNGSSGN CPPDVTINNG
     HVCKESGTIC YNGDCPDLDR VCESIYGAGS VNAPFACYEE IQGQNDRFGN CGKDNRNRYV
     FCGWRNLICG RLICTYPTRM PYNPPNNSTA SVIYAFVRDK VCITVDFGSS VKEDPLRVAN
     GATCDLDRIC LNGVCVESRF LRDQSKTCSS KCHGNGVCNS HGVCHCNAGY SPPNCQYPTT
     KRSASLWSGK HDLPMERASK NQEKKWLLSL YIVLIILASV FLIGTGWKGL KQCGSKEEES
     MSSESKSEDS TYTYVSRSTS ETSSMTSTSS
//
ID   ABC8B_MOUSE             Reviewed;        1620 AA.
AC   Q8K440; A2AM55; Q69ZY4; Q8BRQ1; Q9JL38;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=ATP-binding cassette sub-family A member 8-B;
GN   Name=Abca8b; Synonyms=Abca8, Kiaa0822;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=BALB/c;
RX   MEDLINE=22419899; PubMed=12532264; DOI=10.1007/s00335-002-2229-9;
RA   Annilo T., Chen Z.-Q., Shulenin S., Dean M.;
RT   "Evolutionary analysis of a cluster of ATP-binding cassette (ABC)
RT   genes.";
RL   Mamm. Genome 14:7-20(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Pancreatic islet;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1415-1620 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1433-1620 (ISOFORMS 1/2).
RX   MEDLINE=20175428; PubMed=10708515; DOI=10.1006/geno.1999.6102;
RA   Schriml L.M., Dean M.;
RT   "Identification of 18 mouse ABC genes and characterization of the ABC
RT   superfamily in Mus musculus.";
RL   Genomics 64:24-31(2000).
RN   [6]
RP   INDUCTION.
RX   PubMed=16445568; DOI=10.1111/j.1440-1681.2005.04301.x;
RA   Wakaumi M., Ishibashi K., Ando H., Kasanuki H., Tsuruoka S.;
RT   "Acute digoxin loading reduces ABCA8A mRNA expression in the mouse
RT   liver.";
RL   Clin. Exp. Pharmacol. Physiol. 32:1034-1041(2005).
CC   -!- FUNCTION: ATP-dependent lipophilic drug transporter (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K440-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K440-2; Sequence=VSP_020704;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in heart, brain, lung, liver and
CC       skeletal muscle.
CC   -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis.
CC   -!- INDUCTION: Down-regulated by digoxin.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA
CC       family.
CC   -!- SIMILARITY: Contains 2 ABC transporter domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32312.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF498362; AAM90908.1; -; mRNA.
DR   EMBL; AK173034; BAD32312.1; ALT_INIT; mRNA.
DR   EMBL; AL807245; CAM13339.1; -; Genomic_DNA.
DR   EMBL; AK043744; BAC31640.1; -; mRNA.
DR   EMBL; AF213393; AAF31432.1; -; mRNA.
DR   IPI; IPI00170145; -.
DR   IPI; IPI00788403; -.
DR   RefSeq; NP_038879.2; NM_013851.2.
DR   UniGene; Mm.341004; -.
DR   ProteinModelPortal; Q8K440; -.
DR   SMR; Q8K440; 479-704, 1277-1511.
DR   STRING; Q8K440; -.
DR   PRIDE; Q8K440; -.
DR   Ensembl; ENSMUST00000020948; ENSMUSP00000020948; ENSMUSG00000020620.
DR   Ensembl; ENSMUST00000106669; ENSMUSP00000102280; ENSMUSG00000020620.
DR   GeneID; 27404; -.
DR   KEGG; mmu:27404; -.
DR   NMPDR; fig|10090.3.peg.25544; -.
DR   UCSC; uc007mdb.1; mouse.
DR   UCSC; uc007mdc.1; mouse.
DR   CTD; 27404; -.
DR   MGI; MGI:1351668; Abca8b.
DR   GeneTree; ENSGT00600000084012; -.
DR   HOGENOM; HBG358021; -.
DR   HOVERGEN; HBG079884; -.
DR   InParanoid; Q8K440; -.
DR   OMA; KESIRIR; -.
DR   OrthoDB; EOG40P45W; -.
DR   PhylomeDB; Q8K440; -.
DR   NextBio; 305406; -.
DR   ArrayExpress; Q8K440; -.
DR   Bgee; Q8K440; -.
DR   Genevestigator; Q8K440; -.
DR   GermOnline; ENSMUSG00000020620; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cell membrane; Glycoprotein;
KW   Membrane; Nucleotide-binding; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1   1620       ATP-binding cassette sub-family A member
FT                                8-B.
FT                                /FTId=PRO_0000250679.
FT   TRANSMEM     30     50       Helical; (Potential).
FT   TRANSMEM    223    243       Helical; (Potential).
FT   TRANSMEM    267    287       Helical; (Potential).
FT   TRANSMEM    298    318       Helical; (Potential).
FT   TRANSMEM    326    346       Helical; (Potential).
FT   TRANSMEM    352    372       Helical; (Potential).
FT   TRANSMEM    396    416       Helical; (Potential).
FT   TRANSMEM    860    880       Helical; (Potential).
FT   TRANSMEM    979    999       Helical; (Potential).
FT   TRANSMEM   1023   1043       Helical; (Potential).
FT   TRANSMEM   1069   1089       Helical; (Potential).
FT   TRANSMEM   1105   1125       Helical; (Potential).
FT   TRANSMEM   1135   1155       Helical; (Potential).
FT   TRANSMEM   1164   1184       Helical; (Potential).
FT   TRANSMEM   1194   1214       Helical; (Potential).
FT   DOMAIN      479    714       ABC transporter 1.
FT   DOMAIN     1283   1516       ABC transporter 2.
FT   NP_BIND     515    522       ATP 1 (Potential).
FT   NP_BIND    1321   1328       ATP 2 (Potential).
FT   CARBOHYD    723    723       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     313    374       Missing (in isoform 2).
FT                                /FTId=VSP_020704.
FT   CONFLICT    985    985       D -> G (in Ref. 1; AAM90908).
FT   CONFLICT   1447   1447       D -> V (in Ref. 5; AAF31432).
SQ   SEQUENCE   1620 AA;  183039 MW;  4330378E6D820B62 CRC64;
     MIKREISVRQ QTCALLQKNL LKKWRLKRES LMEWVSSLLL LLFLYWYPHG HGATDLSSVP
     TKDLGRVDSF RQSGFMIGYT PVTSMTQQIM EKVAATPFMA DKKVLGLLDE ENIKELTESH
     AEIIRVIFSD TFSYHLKFQF DQRIPTSREL RDHNAHCDGL YEDVNCLIAI FWKEGFVALQ
     AAINAAIIET TTNHSVMEEL LSVSGKFMKI HPFVRQEGIL TDFFIFTCII SFSPITYYVS
     INVARERKRM KGLMMMMGLR DPAFWLSWGL LYAGFVFIMA LSLALVIKSV QFFILTSFMV
     VFSLFLLYGL SMITLAFLMS ALVRKSVLTG LSVFLLTIFW GSLGFTSLYR YLPAPVEWTL
     SLFSPFAFTL GMAQLLRVDY DLNSNAPPDP ASGSNLIIAT NFMLVFDAFL YLALMMYFEK
     VLPNEYGHQH SPLFFLKSSF WLQTRKPAHV ILEDGIDPVP SSGDSFEPVS PEFHGKESIR
     IRNISKEYKG KPNKIEALKD LTLDIYEGQI TAVLGHSGAG KSTLLNILSG LSVPTKGSVT
     IYNNNLSEMA DLENILRIAG VCPQANVQFD FLTVRENLRL FAKIRGIPPQ DVEKEVQRVL
     LELEMKNIQN ILAQNLSGGQ KRKLTFGIAI LGDSQIFLLD EPTAGLDPFS RHRVWNLLKE
     RRADRVVLFS TQFMDEADIL ADRKVFISNG RLKCAGSSLF LKKKWGVGYH LSLQLKEVCV
     PENITSLVKQ HIPAAKLSAE GEGKLLYTLP LETTYRFPEL CQSLDSCPGL GIENYGVSMT
     TLNEVFLKLE GKASIDEPEV DIVGEGQTER SGDTERLMEM EQTLSSLRET EKTDGMALWR
     QQTCAIAKVR LLKLKHERKT LLSVLLILVV GICPFLFENI STKIRQSSYT WELSPHDYFL
     APGQQPQGML TQLLIINKTE ASIDDFIHSV ERQNIALEVD ASGTRDGTDD PSYNGALIVS
     GNEKNHSFSF ACNTKRLNCF PVLMDILSNG LLGMVKPSAR IQTDRSTYLM DETIHPLEDL
     WKTAFWLILT SACPPYIAMS SVTDYKNRAW FQLRVSGLFP SAYWVGQAMV DIPLYCFVFL
     FMSLMDYLFR FPDTMFSIIS HVIQIPCSVG YAISLIFLTY VISFISRKGK KNSGIWSLSF
     YIITVFSVAV ILLAFDVDGT QYYIIFLIPP STLVGCLILS LHLFIGQIFE EGQVIEPFLV
     FLIPFLHVFI FIFTLRCLEW KFGKKTMRKD PIFRISPRNN DVYQNPEEPE DEDEDVQMER
     MRTANALVST SFDEKPVIIA SCLRKEYAGK QKHCLSKKKA KIATRNVSFC VRKGEILGLL
     GHNGAGKSTS LKMISGDTKV TAGQVLLKGS REGDTPGFLG YCPQENALWP NLTVKEHLEI
     FAAVRGLRKS HAAVAITRLA DALKLQDQLK SPVKTLSEGV KRKLCFVLSI LGNPSILLLD
     EPSTGLDPEG QQQIWQAIRA IIKNTDRGAL LTTHYMAEAE ALCDRVAILV SGRLRCIGSI
     QHLKSKFGKD YLLEMKVKTL EQVEPLNTEI LRLFPQASRQ ERYSSLMAYK LPVEAVQPLS
     QAFFKLEKVK QTFDLEEYSL SQSTLEQVFL ELSKEQELDG LELEELDSSI KWKLLPQEEA
//
ID   ABCA5_MOUSE             Reviewed;        1642 AA.
AC   Q8K448; Q3TE17; Q3UUB4; Q6P1Y0; Q6ZPG4; Q810C7; Q8BM46; Q8BXG7;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=ATP-binding cassette sub-family A member 5;
GN   Name=Abca5; Synonyms=Kiaa1888;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=22419899; PubMed=12532264; DOI=10.1007/s00335-002-2229-9;
RA   Annilo T., Chen Z.-Q., Shulenin S., Dean M.;
RT   "Evolutionary analysis of a cluster of ATP-binding cassette (ABC)
RT   genes.";
RL   Mamm. Genome 14:7-20(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, GLYCOSYLATION, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC   TISSUE=Brain;
RX   PubMed=15870284; DOI=10.1128/MCB.25.10.4138-4149.2005;
RA   Kubo Y., Sekiya S., Ohigashi M., Takenaka C., Tamura K., Nada S.,
RA   Nishi T., Yamamoto A., Yamaguchi A.;
RT   "ABCA5 resides in lysosomes, and ABCA5 knockout mice develop lysosomal
RT   disease-like symptoms.";
RL   Mol. Cell. Biol. 25:4138-4149(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1589.
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Dendritic cell, Embryo, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1480.
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1034-1642.
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [6]
RP   INDUCTION.
RX   PubMed=16445568; DOI=10.1111/j.1440-1681.2005.04301.x;
RA   Wakaumi M., Ishibashi K., Ando H., Kasanuki H., Tsuruoka S.;
RT   "Acute digoxin loading reduces ABCA8A mRNA expression in the mouse
RT   liver.";
RL   Clin. Exp. Pharmacol. Physiol. 32:1034-1041(2005).
CC   -!- FUNCTION: May play a role in the processing of autolysosomes.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass
CC       membrane protein (By similarity). Lysosome membrane; Multi-pass
CC       membrane protein. Late endosome membrane; Multi-pass membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Expressed in cardiomyocytes, oligodendrocytes
CC       and astrocytes in brain, alveolar type 2 cells in lung and
CC       follicular cells in the thyroid gland (at protein level). Detected
CC       in brain, testis, lung, heart, liver, kidney, skeletal muscle and
CC       placenta.
CC   -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis.
CC   -!- INDUCTION: Down-regulated by digoxin.
CC   -!- PTM: N-glycosylated.
CC   -!- DISRUPTION PHENOTYPE: Mice display hypothyroidism and lethal heart
CC       abnormalities that may be due to altered autolysosomes processing.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA
CC       family.
CC   -!- SIMILARITY: Contains 2 ABC transporter domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC28896.2; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF491842; AAM90895.1; -; mRNA.
DR   EMBL; AB097675; BAC66658.1; -; mRNA.
DR   EMBL; AK034961; BAC28896.2; ALT_INIT; mRNA.
DR   EMBL; AK047188; BAC32984.1; -; mRNA.
DR   EMBL; AK138604; BAE23713.1; -; mRNA.
DR   EMBL; AK169879; BAE41431.1; -; mRNA.
DR   EMBL; BC064823; AAH64823.1; ALT_SEQ; mRNA.
DR   EMBL; AK129463; BAC98273.1; -; mRNA.
DR   IPI; IPI00329848; -.
DR   RefSeq; NP_671752.2; NM_147219.2.
DR   UniGene; Mm.41942; -.
DR   ProteinModelPortal; Q8K448; -.
DR   SMR; Q8K448; 477-704, 1288-1527.
DR   STRING; Q8K448; -.
DR   PhosphoSite; Q8K448; -.
DR   PRIDE; Q8K448; -.
DR   Ensembl; ENSMUST00000043961; ENSMUSP00000047927; ENSMUSG00000018800.
DR   GeneID; 217265; -.
DR   KEGG; mmu:217265; -.
DR   UCSC; uc007mdm.1; mouse.
DR   CTD; 217265; -.
DR   MGI; MGI:2386607; Abca5.
DR   GeneTree; ENSGT00600000084012; -.
DR   HOVERGEN; HBG079884; -.
DR   InParanoid; Q8K448; -.
DR   OMA; PSYWSKS; -.
DR   OrthoDB; EOG40ZQWQ; -.
DR   PhylomeDB; Q8K448; -.
DR   NextBio; 375715; -.
DR   ArrayExpress; Q8K448; -.
DR   Bgee; Q8K448; -.
DR   Genevestigator; Q8K448; -.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0033344; P:cholesterol efflux; IMP:BHF-UCL.
DR   GO; GO:0034375; P:high-density lipoprotein particle remodeling; IMP:BHF-UCL.
DR   GO; GO:0010745; P:negative regulation of macrophage derived foam cell differentiation; IMP:BHF-UCL.
DR   GO; GO:0043691; P:reverse cholesterol transport; IC:BHF-UCL.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Endosome; Glycoprotein; Golgi apparatus; Lysosome;
KW   Membrane; Nucleotide-binding; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1   1642       ATP-binding cassette sub-family A member
FT                                5.
FT                                /FTId=PRO_0000250670.
FT   TRANSMEM     32     52       Helical; (Potential).
FT   TRANSMEM    220    240       Helical; (Potential).
FT   TRANSMEM    264    284       Helical; (Potential).
FT   TRANSMEM    297    317       Helical; (Potential).
FT   TRANSMEM    328    348       Helical; (Potential).
FT   TRANSMEM    355    375       Helical; (Potential).
FT   TRANSMEM    396    416       Helical; (Potential).
FT   TRANSMEM    864    884       Helical; (Potential).
FT   TRANSMEM    967    987       Helical; (Potential).
FT   TRANSMEM   1021   1041       Helical; (Potential).
FT   TRANSMEM   1071   1091       Helical; (Potential).
FT   TRANSMEM   1102   1122       Helical; (Potential).
FT   TRANSMEM   1138   1158       Helical; (Potential).
FT   TRANSMEM   1164   1184       Helical; (Potential).
FT   TRANSMEM   1207   1227       Helical; (Potential).
FT   DOMAIN      478    713       ABC transporter 1.
FT   DOMAIN     1290   1533       ABC transporter 2.
FT   NP_BIND     514    521       ATP 1 (Potential).
FT   NP_BIND    1333   1340       ATP 2 (Potential).
FT   CARBOHYD     86     86       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    388    388       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    458    458       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    919    919       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    996    996       N-linked (GlcNAc...) (Potential).
FT   CONFLICT     96     96       S -> C (in Ref. 3; BAC32984).
FT   CONFLICT    113    113       K -> E (in Ref. 3; BAE41431).
FT   CONFLICT    132    132       K -> E (in Ref. 3; BAC32984).
FT   CONFLICT    188    188       K -> E (in Ref. 1; AAM90895).
FT   CONFLICT    303    303       F -> V (in Ref. 1; AAM90895).
FT   CONFLICT    384    384       A -> P (in Ref. 3; BAC32984).
FT   CONFLICT    530    530       L -> P (in Ref. 1; AAM90895).
FT   CONFLICT    551    551       M -> I (in Ref. 1; AAM90895).
FT   CONFLICT    809    809       E -> G (in Ref. 1; AAM90895).
FT   CONFLICT    839    839       L -> P (in Ref. 1; AAM90895).
FT   CONFLICT    856    856       K -> N (in Ref. 1; AAM90895).
FT   CONFLICT    880    880       F -> V (in Ref. 1; AAM90895).
FT   CONFLICT   1231   1231       I -> K (in Ref. 4; AAH64823).
FT   CONFLICT   1503   1503       V -> G (in Ref. 1; AAM90895).
SQ   SEQUENCE   1642 AA;  185895 MW;  177A5FC0B075DFC5 CRC64;
     MATAIRDVGV WRQTRTLLLK NYLIKCRTKK SSVQEILFPL FFLFWLILVS MMHPNKKYEE
     VSDIELSPMD KFSLSNVILG YTPVTNITSS IMQRVSTDHL PKVIVTEEYA NEKELVAASL
     SKSSNFVGVV FKDTMSYELR FFPEMIPVSS IYMNSREGCS KTCDAAQYWS LGFTVLQASI
     DAAIIQLKTN VSVWSELEST KAVIMGEAAV VEIDTFPRGV ILIYLVIAFS PFGYFLAIHI
     VAEKEKKLKE FLKIMGLHDT AFWLSWVLLY ASLIFLMSLL MAVIATASSL FPQSSSIVIF
     LLFFLYGLSS VFFALMLTPL FKKSKHVGVV EFFVTVVFGF VGLLIVLIES FPRSLVWLFS
     PLCQCAFLIG IAQVMHLEDF NEGALFSNLT EGPYPLIITI IMLALDSVFY VLLAVYLDQV
     IPGEFGLRRS SLYFLKPSYW SKNKRNYKEL SEGNINGNIS LNEIVEPVSS EFIGKEAIRI
     SGIQKSYRKK TENVEALRNL SFDIYEGQIT ALLGHSGTGK STLMNILCGL CPPSDGFASI
     YGHRVSEIDE MFEARKMIGI CPQSDINFDV LTVEENLSIL ASIKGIPANN IIQEVQKVLL
     DLDMQAIKDN QAKKLSGGQK RKLSVGIAVL GNPKILLLDE PTAGMDPCSR HIVWNLLKYR
     KANRVTVFST HFMDEADILA DRKAVISQGM LKCVGSSIFL KSKWGIGYRL SMYIDRYCAT
     ESLSSLVRQH IPAAALLQQN DQQLVYSLPF KDMDKFSGLF SALDIHSNLG VISYGVSMTT
     LEDVFLKLEV EAEIDQADYS VFTQQPREEE TDSKSFDEME QSLLILSETK ASSVSTMSLW
     KQQVSTIAKF HFLSLKRESK SVRAVLLLLL IFFAVQIFMF FLHHSFKNAV VPIKLVPDLY
     FLKPGDKPHK YKTSLLLQNS TDSDINGLIE FFAHQNIMVA MFNDSDYVSA APHSAALNVV
     RSEKDYVFSA VFNSTMVYCL PVMMNIISNY YLYHLNVTEA IQTWSTPFIQ EITDIVFKIE
     LYFQAALLGI IVTAMPPYFA MENAENHKIK AYTQLKLSGL LPSAYWVGQA VVDIPLFFVV
     LILMLGSLFA FHHGLYFYPA KFLAVVFCLI AYVPSVILFT YIASFTFKKI LNTKEFWSFI
     YSVTALACVA ITETTFFLQY AVTAVFHYTF CIAIPIYPLL GCLISFIKGS WKNMPKNENT
     YNPWDRLLVA VIMPYLQCIL WIFLLQHYEK IHGGRSIRKD PFFRALSQKA KNKKFPEPPI
     NEDEDEDVKA ERLKVKELMG CQCCEEKPAI MVCNLHKEYD DKKDFLHSRK TTKVATKYIS
     FCVKKGEILG LLGPNGAGKS TVINTLVGDV EPTSGKIFLG DYGSHSSEDD ESIKCMGYCP
     QTNPLWPDLT LQEHFEIYGA VKGMSPGDMK EVISRITKAL DLKEHLQKTV KKLPAGIKRK
     LCFALSMLGN PQVTLLDEPS TGMDPRAKQH MWRAIRTAFK NKKRAALLTT HYMEEAEAVC
     DRVAIMVSGQ LRCIGTVQHL KSKFGKGYFL EIKLKDWIEN LEIDRLQREI QYIFPNASRQ
     ESFSSILAFK IPKEDVQSLS QSFAKLEEAK RTFAIEEYSF SQATLEQVFV ELTKEQEEED
     NSCGTLASTL WWERTQEDRV VF
//
ID   TMIE_MOUSE              Reviewed;         153 AA.
AC   Q8K467;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Transmembrane inner ear expressed protein;
DE   Flags: Precursor;
GN   Name=Tmie;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INVOLVEMENT IN
RP   SPINNER MUTANT STRAIN PHENOTYPE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=22135658; PubMed=12140191; DOI=10.1093/hmg/11.16.1887;
RA   Mitchem K.L., Hibbard E., Beyer L.A., Bosom K., Dootz G.A.,
RA   Dolan D.F., Johnson K.R., Raphael Y., Kohrman D.C.;
RT   "Mutation of the novel gene Tmie results in sensory cell defects in
RT   the inner ear of spinner, a mouse model of human hearing loss DFNB6.";
RL   Hum. Mol. Genet. 11:1887-1898(2002).
CC   -!- FUNCTION: Unknown. The protein may play some role in a cellular
CC       membrane location. May reside within an internal membrane
CC       compartment and function in pathways such as those involved in
CC       protein and/or vesicle trafficking. Alternatively, the mature
CC       protein may be localized in the plasma membrane and serve as a
CC       site of interaction for other molecules through its highly charged
CC       C-terminal domain.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- TISSUE SPECIFICITY: Expressed in brain, kidney, liver, lung and
CC       cochlea.
CC   -!- DEVELOPMENTAL STAGE: Required for normal postnatal maturation of
CC       sensory hair cells in the cochlea, including correct development
CC       of stereocilia bundles.
CC   -!- DISEASE: Note=Defects in Tmie are the cause of the spinner mutant
CC       strain phenotype (sr). This disorder results in hearing loss and
CC       vestibular dysfunction due to neuroepithelial defects in the inner
CC       ear. It is recognized by behavioral dysfunction, including
CC       bidirectional circling and head shaking. Auditory function in
CC       spinner mice is found to be reduced, based upon the lack of a
CC       startle reflex to sound at any age. Breeding experiments indicated
CC       that these defects are inherited in an autosomal recessive
CC       fashion. The postnatal defects present in the cochleae of sr/sr
CC       mice suggest a requirement for Tmie during maturation of sensory
CC       cells, including the normal development or maintenance of
CC       stereocilia bundles.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF481143; AAM89222.1; -; mRNA.
DR   IPI; IPI00170169; -.
DR   RefSeq; NP_666372.1; NM_146260.2.
DR   UniGene; Mm.390229; -.
DR   STRING; Q8K467; -.
DR   PRIDE; Q8K467; -.
DR   Ensembl; ENSMUST00000050958; ENSMUSP00000060148; ENSMUSG00000049555.
DR   GeneID; 20776; -.
DR   KEGG; mmu:20776; -.
DR   UCSC; uc009rvb.1; mouse.
DR   CTD; 20776; -.
DR   MGI; MGI:2159400; Tmie.
DR   eggNOG; roNOG16648; -.
DR   GeneTree; ENSGT00390000005082; -.
DR   HOGENOM; HBG713880; -.
DR   HOVERGEN; HBG079268; -.
DR   InParanoid; Q8K467; -.
DR   OMA; TELTEVP; -.
DR   OrthoDB; EOG4QFWFQ; -.
DR   PhylomeDB; Q8K467; -.
DR   NextBio; 299495; -.
DR   ArrayExpress; Q8K467; -.
DR   Bgee; Q8K467; -.
DR   CleanEx; MM_TMIE; -.
DR   Genevestigator; Q8K467; -.
DR   GermOnline; ENSMUSG00000049555; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042472; P:inner ear morphogenesis; IMP:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
PE   2: Evidence at transcript level;
KW   Deafness; Membrane; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     28       Potential.
FT   CHAIN        29    153       Transmembrane inner ear expressed
FT                                protein.
FT                                /FTId=PRO_0000022556.
FT   TOPO_DOM     29     58       Extracellular (Potential).
FT   TRANSMEM     59     79       Helical; (Potential).
FT   TOPO_DOM     80    153       Cytoplasmic (Potential).
FT   COMPBIAS    124    153       Lys-rich.
SQ   SEQUENCE   153 AA;  17027 MW;  2B22474B275CBBD8 CRC64;
     MAGRQHGSGR LWALGGAALG ACLAGVATQL VEPSTAPPKP KPPPLTKETV VFWDMRLWHV
     VGIFSLFVLS IIITLCCVFN CRVPRTRKEI EARYLQRKAA KMYTDKLETV PPLNELTEIP
     GEDKKKKKKD SVDTVAIKVE EDEKNEAKKK GEK
//
ID   KCD11_MOUSE             Reviewed;         232 AA.
AC   Q8K485;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=BTB/POZ domain-containing protein KCTD11;
GN   Name=Kctd11; Synonyms=Ren;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=Swiss Webster;
RX   MEDLINE=22174637; PubMed=12186855; DOI=10.1083/jcb.200202024;
RA   Gallo R., Zazzeroni F., Alesse E., Mincione C., Borello U., Buanne P.,
RA   D'Eugenio R., Mackay A.R., Argenti B., Gradini R., Russo M.A.,
RA   Maroder M., Cossu G., Frati L., Screpanti I., Gulino A.;
RT   "REN: a novel, developmentally regulated gene that promotes neural
RT   cell differentiation.";
RL   J. Cell Biol. 158:731-740(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Head, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and Czech II; TISSUE=Brain, and Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   MISCELLANEOUS.
RX   PubMed=15249678; DOI=10.1073/pnas.0400690101;
RA   Di Marcotullio L., Ferretti E., De Smaele E., Argenti B., Mincione C.,
RA   Zazzeroni F., Gallo R., Masuelli L., Napolitano M., Maroder M.,
RA   Modesti A., Giangaspero F., Screpanti I., Alesse E., Gulino A.;
RT   "REN(KCTD11) is a suppressor of Hedgehog signaling and is deleted in
RT   human medulloblastoma.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:10833-10838(2004).
RN   [5]
RP   FUNCTION, TISSUE SPECIFICITY, AND CHARACTERIZATION OF BTB DOMAIN.
RX   PubMed=16148242; DOI=10.1523/JNEUROSCI.2438-05.2005;
RA   Argenti B., Gallo R., Di Marcotullio L., Ferretti E., Napolitano M.,
RA   Canterini S., De Smaele E., Greco A., Fiorenza M.T., Maroder M.,
RA   Screpanti I., Alesse E., Gulino A.;
RT   "Hedgehog antagonist REN(KCTD11) regulates proliferation and apoptosis
RT   of developing granule cell progenitors.";
RL   J. Neurosci. 25:8338-8346(2005).
CC   -!- FUNCTION: Play a role as a marker and a regulator of neuronal
CC       differentiation; Up-regulated by a variety of neurogenic signals,
CC       such as retinoic acid, epidermal growth factor/EGF and NGFB/nerve
CC       growth factor. Induces apoptosis, growth arrest and the expression
CC       of cyclin-dependent kinase inhibitor CDKN1B. Plays a role as a
CC       tumor repressor and inhibits cell growth and tumorigenicity of
CC       medulloblastoma (MDB). Functions as antagonist of the Hedgehog
CC       pathway on cell proliferation and differentiation by affecting the
CC       nuclear transfer of transcrition factor GLI1, thus maintaining
CC       cerebellar granule cells in undifferentiated state. When knock-
CC       down, Hedgehog antagonism is impaired and proliferation of granule
CC       cells is sustained. Activates the caspase cascade.
CC   -!- TISSUE SPECIFICITY: Weakly expressed in lung. In the cerebellum,
CC       higher expression in non proliferating external granule cells
CC       layer than in highly proliferating ones.
CC   -!- DEVELOPMENTAL STAGE: Detected at E7.5 in neuroectodermal cells,
CC       and later in neural crest, in ventral region of the spinal cord
CC       and in ventricular epithelium of the neural tube.
CC   -!- DOMAIN: The BTB domain is required for growth-suppressing
CC       properties.
CC   -!- MISCELLANEOUS: Overexpression of Kctd11 by lentiviral vector
CC       injection inhibits xenograft tumor growth in athymic nude mice.
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF465352; AAM95915.1; -; mRNA.
DR   EMBL; AK039558; BAC30382.1; -; mRNA.
DR   EMBL; AK161602; BAE36486.1; -; mRNA.
DR   EMBL; AK170258; BAE41666.1; -; mRNA.
DR   EMBL; BC052502; AAH52502.1; -; mRNA.
DR   EMBL; BC052734; AAH52734.1; -; mRNA.
DR   IPI; IPI00170182; -.
DR   RefSeq; NP_694783.1; NM_153143.4.
DR   UniGene; Mm.239498; -.
DR   HSSP; Q9UK17; 1S1G.
DR   ProteinModelPortal; Q8K485; -.
DR   SMR; Q8K485; 19-70.
DR   PRIDE; Q8K485; -.
DR   Ensembl; ENSMUST00000050555; ENSMUSP00000059107; ENSMUSG00000046731.
DR   GeneID; 216858; -.
DR   KEGG; mmu:216858; -.
DR   UCSC; uc007jsd.1; mouse.
DR   CTD; 216858; -.
DR   MGI; MGI:2448712; Kctd11.
DR   GeneTree; ENSGT00600000084079; -.
DR   HOGENOM; HBG716696; -.
DR   HOVERGEN; HBG080457; -.
DR   InParanoid; Q8K485; -.
DR   OMA; RAEGGPH; -.
DR   OrthoDB; EOG4PZJ7D; -.
DR   PhylomeDB; Q8K485; -.
DR   NextBio; 375404; -.
DR   ArrayExpress; Q8K485; -.
DR   Bgee; Q8K485; -.
DR   Genevestigator; Q8K485; -.
DR   GermOnline; ENSMUSG00000046731; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IC:MGI.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IDA:MGI.
DR   GO; GO:0007399; P:nervous system development; IDA:MGI.
DR   GO; GO:0042127; P:regulation of cell proliferation; IDA:MGI.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   PROSITE; PS50097; BTB; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Cell cycle; Developmental protein; Growth regulation;
KW   Tumor suppressor.
FT   CHAIN         1    232       BTB/POZ domain-containing protein KCTD11.
FT                                /FTId=PRO_0000248592.
FT   DOMAIN        1     49       BTB.
SQ   SEQUENCE   232 AA;  26300 MW;  993C1FFDE8D52943 CRC64;
     MLGAMFRADT LMPANLNPQG DGHYFIDRDG KAFRHILNFL RLGRLDLPRG YGETALLKAE
     ADFYQIRPLL DALRELEASR GTPASTAALL HADVDVSPRQ VHFSARRGPH HYELSSVQVD
     TFRANLFCTD PECLAAMRNR FGVAIGDRAE GGPHFRLEWA SRPQELPEVE YQRLGLQPLW
     TGGPEDRREV ANTPTFLEEV LRVALEHGFR LDSVFPDPED LLNSRSLRFV RH
//
ID   MTA1_MOUSE              Reviewed;         715 AA.
AC   Q8K4B0; Q80UI1; Q8K4D4; Q924K9;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Metastasis-associated protein MTA1;
GN   Name=Mta1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=22269978; PubMed=12370427; DOI=10.1073/pnas.212392399;
RA   Zhou J., Ashouian N., Delepine M., Matsuda F., Chevillard C.,
RA   Riblet R., Schildkraut C.L., Birshtein B.K.;
RT   "The origin of a developmentally regulated Igh replicon is located
RT   near the border of regulatory domains for Igh replication and
RT   expression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13693-13698(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=129/Sv;
RX   MEDLINE=21376123; PubMed=11483358; DOI=10.1016/S0378-1119(01)00563-7;
RA   Simpson A., Uitto J., Rodeck U., Mahoney M.G.;
RT   "Differential expression and subcellular distribution of the mouse
RT   metastasis-associated proteins Mta1 and Mta3.";
RL   Gene 273:29-39(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ; TISSUE=Liver;
RA   Takiguchi S.;
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-449, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May be involved in the regulation of gene expression by
CC       covalent modification of histone proteins.
CC   -!- SUBUNIT: Component of the nucleosome-remodeling and histone-
CC       deacetylase multiprotein complex (NuRD). Interacts with HDAC1 and
CC       ITGB3BP/CENPR (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Widely expressed but not in skeletal muscle.
CC   -!- SIMILARITY: Contains 1 BAH domain.
CC   -!- SIMILARITY: Contains 1 ELM2 domain.
CC   -!- SIMILARITY: Contains 1 GATA-type zinc finger.
CC   -!- SIMILARITY: Contains 1 SANT domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC57413.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF463504; AAM97588.1; -; mRNA.
DR   EMBL; AF450245; AAM97587.1; -; Genomic_DNA.
DR   EMBL; AF288137; AAK83044.1; -; mRNA.
DR   EMBL; AB039744; BAC57413.1; ALT_INIT; Genomic_DNA.
DR   IPI; IPI00853911; -.
DR   UniGene; Mm.212577; -.
DR   ProteinModelPortal; Q8K4B0; -.
DR   SMR; Q8K4B0; 5-162, 285-341.
DR   DIP; DIP-38226N; -.
DR   MINT; MINT-1350646; -.
DR   STRING; Q8K4B0; -.
DR   PhosphoSite; Q8K4B0; -.
DR   PRIDE; Q8K4B0; -.
DR   Ensembl; ENSMUST00000009099; ENSMUSP00000009099; ENSMUSG00000021144.
DR   Ensembl; ENSMUST00000109727; ENSMUSP00000105349; ENSMUSG00000021144.
DR   UCSC; uc007pfv.1; mouse.
DR   MGI; MGI:2150037; Mta1.
DR   eggNOG; roNOG14717; -.
DR   GeneTree; ENSGT00580000081398; -.
DR   HOGENOM; HBG403019; -.
DR   HOVERGEN; HBG002598; -.
DR   InParanoid; Q8K4B0; -.
DR   OMA; SAPVINN; -.
DR   OrthoDB; EOG4HT8RP; -.
DR   PhylomeDB; Q8K4B0; -.
DR   ArrayExpress; Q8K4B0; -.
DR   Bgee; Q8K4B0; -.
DR   CleanEx; MM_MTA1; -.
DR   Genevestigator; Q8K4B0; -.
DR   GermOnline; ENSMUSG00000021144; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0016581; C:NuRD complex; IPI:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR001025; BAH_dom.
DR   InterPro; IPR000949; ELM2_dom.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR001005; SANT_DNA-bd.
DR   InterPro; IPR017884; SANT_eukarya.
DR   InterPro; IPR000679; Znf_GATA.
DR   Pfam; PF01426; BAH; 1.
DR   Pfam; PF01448; ELM2; 1.
DR   Pfam; PF00320; GATA; 1.
DR   SMART; SM00439; BAH; 1.
DR   SMART; SM00717; SANT; 1.
DR   SMART; SM00401; ZnF_GATA; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
DR   PROSITE; PS51038; BAH; 1.
DR   PROSITE; PS51156; ELM2; 1.
DR   PROSITE; PS00344; GATA_ZN_FINGER_1; FALSE_NEG.
DR   PROSITE; PS50114; GATA_ZN_FINGER_2; FALSE_NEG.
DR   PROSITE; PS51293; SANT; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    715       Metastasis-associated protein MTA1.
FT                                /FTId=PRO_0000083494.
FT   DOMAIN        1    164       BAH.
FT   DOMAIN      165    276       ELM2.
FT   DOMAIN      283    335       SANT.
FT   ZN_FING     393    420       GATA-type; atypical.
FT   MOTIF       545    552       SH3-binding (Potential).
FT   MOTIF       696    705       SH3-binding (Potential).
FT   COMPBIAS    700    705       Poly-Pro.
FT   MOD_RES     386    386       Phosphoserine (By similarity).
FT   MOD_RES     449    449       Phosphoserine.
FT   MOD_RES     467    467       Phosphothreonine (By similarity).
FT   MOD_RES     520    520       Phosphoserine (By similarity).
FT   MOD_RES     522    522       Phosphoserine (By similarity).
FT   MOD_RES     564    564       Phosphothreonine (By similarity).
FT   MOD_RES     576    576       Phosphoserine.
FT   MOD_RES     578    578       Phosphothreonine (By similarity).
FT   CONFLICT     64     64       T -> R (in Ref. 2).
FT   CONFLICT     65     81       Missing (in Ref. 2).
FT   CONFLICT    420    420       C -> W (in Ref. 2; AAK83044).
SQ   SEQUENCE   715 AA;  80798 MW;  135152CD3554278D CRC64;
     MAANMYRVGD YVYFENSSSN PYLIRRIEEL NKTANGNVEA KVVCFYRRRD ISSSLIALAD
     KHATLSVCYR AGPGADTGEE GEVEEEVENP EMVDLPEKLK HQLRHRELFL SRQLESLPAT
     HIRGKCSVTL LNETESLKSY LEREDFFFYS LVYDPQQKTL LADKGEIRVG NRYQADITDL
     LKEGEEDGRD QSKLETKVWE AHNPLVDKQI DQFLVVARSV GTFARALDCS SSVRQPSLHM
     SAAAASRDIT LFHAMDTLHK NIYDISKAIS ALVPQGGPVL CRDEMEEWSA SEANLFEEAL
     EKYGKDFTDI QQDFLPWKSL TSIIEYYYMW KTTDRYVQQK RLKAAEAESK LKQVYIPNYN
     KPNPNQISAS SVKATVVNGT GTPGQSPGAG RACESCYTTQ SYQWYSWGPP NMQCRLCASC
     WTYWKKYGGL KMPTRLDGER PGPNRNNMSP HGIPARSSGS PKFAMKTRQA FYLHTTKLTR
     IARRLCREIL RPWHAARHPY MPINSAAIKA ECTARLPEAS QSPLVLKQVV RKPLEAVLRY
     LETHPRPPKP DPVKSSSSVL SSLTPAKSAP VINNGSPTIL GKRSYEQHNG VDGNMKKRLL
     MPSRGLANHG QTRHMGPSRN LLLNGKSYPT KVRLIRGGSL PPVKRRRMNW IDAPDDVFYM
     ATEETRKIRK LLSSSETKRA ARRPYKPIAL RQSQALPLRP PPPAPVNDEP IVIED
//
ID   ALMS1_MOUSE             Reviewed;        3251 AA.
AC   Q8K4E0; Q6A084; Q8C9N9;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Alstrom syndrome protein 1 homolog;
GN   Name=Alms1; Synonyms=Kiaa0328;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   MEDLINE=21980192; PubMed=11941369; DOI=10.1038/ng867;
RA   Collin G.B., Marshall J.D., Ikeda A., So W.V., Russell-Eggitt I.,
RA   Maffei P., Beck S., Boerkoel C., Sicolo N., Martin M., Nishina P.M.,
RA   Naggert J.K.;
RT   "Mutations in ALMS1 cause obesity, type 2 diabetes and neurosensory
RT   degeneration in Alstrom syndrome.";
RL   Nat. Genet. 31:74-78(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryonic tail;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2974-3251 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=16000322; DOI=10.1093/hmg/ddi235;
RA   Collin G.B., Cyr E., Bronson R., Marshall J.D., Gifford E.J.,
RA   Hicks W., Murray S.A., Zheng Q.Y., Smith R.S., Nishina P.M.,
RA   Naggert J.K.;
RT   "Alms1-disrupted mice recapitulate human Alstrom syndrome.";
RL   Hum. Mol. Genet. 14:2323-2333(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2531, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: Possible role in intracellular trafficking.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytoskeleton, centrosome (By similarity). Cytoplasm, cytoskeleton,
CC       cilium basal body (By similarity). Cytoplasm, cytoskeleton,
CC       spindle pole (By similarity). Note=Associated with centrosomes and
CC       basal body at the base of primary cilia. During mitosis localizes
CC       to both spindle poles (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K4E0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K4E0-2; Sequence=VSP_017350;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- DEVELOPMENTAL STAGE: Expressed at E7.5. At E8.0 expression is
CC       found in mesodermal- and ectodermal-derived layers. At E10.5
CC       mainly detected in midbrain, hindbrain, forelimb and hindlimb.
CC       Also expressed at E15.5 and E18.5.
CC   -!- DISRUPTION PHENOTYPE: Mice display obesity, hypogonadism,
CC       hyperinsulinemia, retinal dysfunction and hearing loss.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32212.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF425257; AAM62320.1; -; mRNA.
DR   EMBL; AK172934; BAD32212.1; ALT_INIT; mRNA.
DR   EMBL; AK041679; BAC31030.1; -; mRNA.
DR   IPI; IPI00170205; -.
DR   IPI; IPI00742378; -.
DR   RefSeq; NP_660258.2; NM_145223.2.
DR   UniGene; Mm.246967; -.
DR   UniGene; Mm.422971; -.
DR   STRING; Q8K4E0; -.
DR   PhosphoSite; Q8K4E0; -.
DR   PRIDE; Q8K4E0; -.
DR   Ensembl; ENSMUST00000072018; ENSMUSP00000071904; ENSMUSG00000063810.
DR   GeneID; 236266; -.
DR   KEGG; mmu:236266; -.
DR   UCSC; uc009cpz.1; mouse.
DR   UCSC; uc009cqe.1; mouse.
DR   CTD; 236266; -.
DR   MGI; MGI:1934606; Alms1.
DR   eggNOG; roNOG07240; -.
DR   GeneTree; ENSGT00550000074751; -.
DR   HOGENOM; HBG126725; -.
DR   HOVERGEN; HBG080834; -.
DR   InParanoid; Q8K4E0; -.
DR   OrthoDB; EOG4WH8JV; -.
DR   NextBio; 382932; -.
DR   ArrayExpress; Q8K4E0; -.
DR   Bgee; Q8K4E0; -.
DR   CleanEx; MM_ALMS1; -.
DR   Genevestigator; Q8K4E0; -.
DR   GermOnline; ENSMUSG00000063810; Mus musculus.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-KW.
DR   GO; GO:0005932; C:microtubule basal body; IEA:UniProtKB-SubCell.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0006915; P:apoptosis; IMP:MGI.
DR   GO; GO:0019722; P:calcium-mediated signaling; IMP:MGI.
DR   GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
DR   GO; GO:0042384; P:cilium assembly; IMP:MGI.
DR   GO; GO:0048589; P:developmental growth; IMP:MGI.
DR   GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR   GO; GO:0045444; P:fat cell differentiation; IMP:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0045598; P:regulation of fat cell differentiation; IMP:MGI.
DR   GO; GO:0046548; P:retinal rod cell development; IMP:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR   GO; GO:0007286; P:spermatid development; IMP:MGI.
DR   GO; GO:0006641; P:triglyceride metabolic process; IMP:MGI.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell projection; Cilium; Cytoplasm;
KW   Cytoskeleton; Phosphoprotein; Repeat.
FT   CHAIN         1   3251       Alstrom syndrome protein 1 homolog.
FT                                /FTId=PRO_0000225593.
FT   REPEAT      440    485       1.
FT   REPEAT      486    534       2.
FT   REPEAT      540    587       3.
FT   REPEAT      588    638       4.
FT   REPEAT      639    684       5.
FT   REPEAT      685    731       6.
FT   REPEAT      732    777       7.
FT   REPEAT      778    824       8.
FT   REPEAT      825    871       9.
FT   REPEAT      872    917       10.
FT   REPEAT      918    959       11.
FT   REPEAT      960   1005       12.
FT   REPEAT     1006   1048       13.
FT   REPEAT     1115   1163       14.
FT   REPEAT     1164   1208       15.
FT   REPEAT     1269   1314       16.
FT   REPEAT     1315   1362       17.
FT   REGION      440   1362       17 X 47 AA approximate tandem repeat.
FT   COMPBIAS      2     80       Glu-rich.
FT   COMPBIAS     90    113       Pro-rich.
FT   COMPBIAS   2582   2618       His-rich.
FT   MOD_RES    2531   2531       Phosphoserine.
FT   VAR_SEQ       1   2947       Missing (in isoform 2).
FT                                /FTId=VSP_017350.
FT   CONFLICT   3017   3017       D -> G (in Ref. 2; BAD32212).
FT   CONFLICT   3060   3060       S -> N (in Ref. 2; BAD32212).
FT   CONFLICT   3077   3077       V -> G (in Ref. 2; BAD32212).
FT   CONFLICT   3229   3229       W -> R (in Ref. 2; BAD32212).
SQ   SEQUENCE   3251 AA;  360238 MW;  2054C92F8755E136 CRC64;
     MEPEDLPWPD ELEEEEEEEE EEGEEYEGKK EVENASAAAT EEALTSEESG RLEEFEEAGP
     DLDFNYESQR QESSDEEEDE LAKAWLQAHP DRPGSAFSLP PPTPPPPPPP LSPRLRYTPV
     EHLGKTEVVP LTCRVWQQSS YQDNSRAQFS NSSTMLLETG VRWGSEEDQR TESWHCLPQE
     RDSSQTLAMS QTEIGRVEGT EVPDLPSQEG GLPAQSQCPG KKPKLNVLCS PLLVIQDNFA
     APDLPLLTCL IQDQEEVEPD SLFQQSELEF APLRGIPDKS EDSEWLARPS EVSEALIQAT
     SETSSDLANS CFSISQHPLT EGLQGKAESG VLTRCGDAKY SSLYENLGAQ SERIAVLQRE
     VGCSNLGISQ ASPSSLPSFV PQEPTSEPEY HSSNLRMLRV SPDTLLTTHT HSAGSADQKI
     GAAVVSSAYS QEIKPGSFHQ EELPDRHLNE EIRKVSPALR TAGQKPEMLP VQSSSYSKGM
     KSIFYQHPVS HGHQGKEPLS VSAVCGSAGN KAFHQLSTLS DSLLTEETWP VSVIPGLGNQ
     KTPLPSEFSL SYSHRGKNLP EDVVKVSTDS GSAHKKADIL TASSRTYQHK MKPANIYHQE
     LPDSRVPIGT RKVAFESGPA GQKSGVSHPY GEMPSVFYQQ GLPDRHSAKS PTKTFIPGPA
     DQKTDLSPVP PTSSSHAEKP VSPYQLTLPG SHLPEDVFKA SSVCKSSDEL SGITALTSAS
     YSYKGRPNSS YQQKFPDSHL NEEAQKILGT TGTVDQKTVT PTMSSSFLQK EKPSIFYQQT
     LPDGGLSEED LQVSAVPWPA DQNIAIPTVT SAAFSQREKP RIFYQQTLSV DRLPGEPLNV
     LGTSGPPDQN TGAPTVTPSS YFPGEESIIF YQAGFPGNTL SAMSFKVPRI SGSTEQTNVT
     TGSSSSYSVG EKSIIFYHQA LPDGRLPQEA SPAPADLNTG EPPMYLASCS VGVKPIIFYQ
     QPMSDSQRTK GHKESDVPGP TDQKTGIATV HSTSQSYIGR RTVSYQKEFP DLSEKALKVL
     GDVGSTEQKT QIPVVSSALL HKEGPSAYQE DLPDLTEEPL QILGVSEEVS SSSYQRKLPD
     HIEVFLKSVG SGSADRKTGA QIVSSSREKS SGFHQQELPN TGGDAVDAFH PEPVVQEVRK
     VQTPGAPAGP SSSHFHKEKL SDYQKASPHR DLTESSLKAS TVPGLSDQKK KPAVSSGFCL
     HKEKHEISAS ALLNCQTAEL LTVTQRSCLH REDPAISTVI KPDDQKIPLP TTFHGSSDQK
     VKPVIFVQKQ LRDRDQSEDI PKISTVSEPT VVNTVLPVLL PGSYSHREKS DSFYPQELPD
     GHLTEVDLKV SSGLGQADQI SGLPTGIPGT YSHSEKHQLI SEHVQELMDN LNSSESSCLS
     VDSMPLNSQI DDGVIICKPE SLGFANAGCE EMQNIDRGSK TLKEIQTLLM EAENMALKRC
     NFSVPLVPFR DVNDVSFIRS KKVVCFKESS TTDVCTQRES FVEEVPHIEY VQKDIGTQTN
     LKYQRGVGNW EFISSATFRS PLQEAEGTAR MAYDETFRQY KAARSVMRSE PEGCSTGIGN
     KMIIPMMTII KSDSSSDVSD GCCSWDNNLP ESLESVSDVF LNFFPYTSPK TSITDSREEE
     WLSESEDGYG STDSLAAHVK YLLQCETSLN QAKQILKNAE EEEYRVRTQA WNLKFNLGRD
     RGYSISELNE DDRRKVEEIK AKLFGHGRAT HMSEGLRSPQ GIGCLPEAVC SRIIIESHEK
     GCFRTLTAEQ PRPDSCHCAF RSVEPSDLIR GHRSPSSWRG RHINLSRSIE QSNPCFKVGS
     SFQLQSHPPF QKLLPDDIKI SKGVGMPVHA YMDPQPSELV EPTCVPAKEM DFPSSSQILP
     PEPKKQFTTA ITFSSHEHSE CISDSSGCKV GVTADSQCSG PSLGVFKPHI PEEQISPRDL
     KQKTSFQSSL ERHGSTPVTI LADGSRQRQK LPVDFEHSHQ KEKLLQRLGF KVSHSEPNVS
     TNVSNFKGVQ FSGKDTIVSQ DKLTSTVEVK EKNVTVTPDL PSCIFLEQPE LFEESHTPHT
     DLQMRKYPSP SCPEIASRIF LEQPKLSEQS KAPHVDREIR EDHSFFPKCQ DYIVADPSPD
     FPDQQQCKPP DVVGHTRKQN SLLSEGQDYE LEEVQHIPQS YFSNMVNVEA KVSDAISQSA
     PDHCTAASTP PSNRKALSCV RITLCPKTSS KLDSGTLGER FHSLDPASKT RINSEFNSDL
     RIISSRSLEP TSKLLTCKPV AQDQESLVFL GPKSPLDLQV AQSSLPDSKT IFQDLKTKPP
     QNSQIVTSRQ TQVNISHLEG YSKPEGTPVS ADGSQEQSKV SFTTSFGKLS SDAITQITTE
     SPEKTTFSSE IFIHADDRGQ GILDPMAQKP SRFASSSSVQ QIPASHGKDA QPVLLPYKPS
     GSSKMYYVPL LKRVPSYLDS KSDTTVESSH SGSNDAIAPD FPPQMLGTRD DDLSNTVNIK
     HKEGIYSKRA ATKGKNPSQK GDAAAPVQMP ITWDENVLDE NQEEVISRGV VIKMAGPEEM
     SSLEKDLAGP SDITVQDRKT ENLPDTKSIK QKEGSLEIES ECHSAFENTA HSVFRSAKFY
     FHHPVHLPHE QDFCHESLGR SVFMQHSWKD FFHHHSGHSC LPPPGPSSDK LDKTKMDYTR
     IKSLSINLNL GEHEKIHTIK NQARDPKGKR QANEQKKDQK VTPELTTECP VSLNELWNRY
     QERQKQQSPC GACDTKELSL VERLDRLAKL LQNPITHSLR ASESAQDDSR GGHRAREWTG
     RRQQKQKGKQ HRKWSKSLER GQSTGDFRKS KVFSPHQGGK SSQFKIEQIK LDKYILRKEP
     GFNNVSNTSL DSRPSEESVS LTDSPNIFSS TDSPVDSDVL TPTDRDMPLN ERSSSISTID
     TVRLIQAFGQ DRLSLSPRRI KLYSTVTSQR RRYLEQPCKH NRKALNTACP QMTSEHSRRR
     HIQVANHMTS SDSVSSPGSL LSLDSALSNE ETVRMVSKGV QAGNLEIVAG VKKYTQDVGV
     TFPTPSSSEA RLEEDSDVTS SSEEKAKEKK FLSNYLQTKN LRKNKPNPCA GVSWFVPVES
     GQSGSKKENL PKIYRPVISW FEPVTKTKPW REPLREQNWQ AQCMNSRGSL GGPGRDSGQV
     SLRPFVRATL QESLQLHRPD FISHSGERIK RLKLLVQERK LQSLFQSERE ALFHSARPLP
     RRVLLAVQKN KPIGKKEMIQ RTRRIYEQLP EVKKKREEEK RKSEYKSYWL RAQHYKMKVT
     NHLLGRKVPW D
//
ID   ARHG6_MOUSE             Reviewed;         771 AA.
AC   Q8K4I3; Q8C9V4;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Rho guanine nucleotide exchange factor 6;
DE   AltName: Full=Rac/Cdc42 guanine nucleotide exchange factor 6;
GN   Name=Arhgef6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=22057597; PubMed=12063400;
RA   Kutsche K., Gal A.;
RT   "The mouse Arhgef6 gene: cDNA sequence, expression analysis, and
RT   chromosome assignment.";
RL   Cytogenet. Cell Genet. 95:196-201(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-622.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND THR-649, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-639 AND SER-679, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487 AND SER-679, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   STRUCTURE BY NMR OF 429-547.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the pleckstrin homology domain of alpha-PIX.";
RL   Submitted (MAY-2004) to the PDB data bank.
CC   -!- FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF)
CC       (By similarity).
CC   -!- SUBUNIT: Interacts with PAK kinases through the SH3 domain.
CC       Interacts with GIT1. Component of cytoplasmic complexes, which
CC       also contain PXN, GIT1 and PAK1 (By similarity).
CC   -!- TISSUE SPECIFICITY: Detected in adult heart, spleen, lung,
CC       skeletal muscle, kidney and testis. Detected throughout
CC       embryogenesis.
CC   -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF393831; AAM94903.1; -; mRNA.
DR   EMBL; AK040468; BAC30599.1; -; mRNA.
DR   IPI; IPI00874444; -.
DR   RefSeq; NP_690014.2; NM_152801.2.
DR   UniGene; Mm.261443; -.
DR   PDB; 1V61; NMR; -; A=429-547.
DR   PDBsum; 1V61; -.
DR   ProteinModelPortal; Q8K4I3; -.
DR   SMR; Q8K4I3; 4-111, 154-551, 706-757.
DR   MINT; MINT-4117855; -.
DR   STRING; Q8K4I3; -.
DR   PhosphoSite; Q8K4I3; -.
DR   PRIDE; Q8K4I3; -.
DR   Ensembl; ENSMUST00000114736; ENSMUSP00000110384; ENSMUSG00000031133.
DR   GeneID; 73341; -.
DR   KEGG; mmu:73341; -.
DR   UCSC; uc009thd.1; mouse.
DR   CTD; 73341; -.
DR   MGI; MGI:1920591; Arhgef6.
DR   GeneTree; ENSGT00600000084055; -.
DR   HOVERGEN; HBG050569; -.
DR   NextBio; 338019; -.
DR   ArrayExpress; Q8K4I3; -.
DR   Bgee; Q8K4I3; -.
DR   Genevestigator; Q8K4I3; -.
DR   GermOnline; ENSMUSG00000031133; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR003096; SM22_calponin.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR00888; SM22CALPONIN.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Guanine-nucleotide releasing factor;
KW   Phosphoprotein; SH3 domain.
FT   CHAIN         1    771       Rho guanine nucleotide exchange factor 6.
FT                                /FTId=PRO_0000080918.
FT   DOMAIN        1    110       CH.
FT   DOMAIN      159    218       SH3.
FT   DOMAIN      240    420       DH.
FT   DOMAIN      442    547       PH.
FT   MOD_RES     122    122       Phosphoserine.
FT   MOD_RES     126    126       Phosphoserine (By similarity).
FT   MOD_RES     187    187       Phosphotyrosine (By similarity).
FT   MOD_RES     224    224       Phosphoserine (By similarity).
FT   MOD_RES     487    487       Phosphoserine.
FT   MOD_RES     639    639       Phosphoserine.
FT   MOD_RES     649    649       Phosphothreonine.
FT   MOD_RES     679    679       Phosphoserine.
FT   MOD_RES     746    746       N6-acetyllysine (By similarity).
FT   TURN        430    432
FT   STRAND      452    457
FT   STRAND      467    472
FT   STRAND      477    481
FT   STRAND      483    485
FT   STRAND      515    518
FT   STRAND      525    527
FT   HELIX       533    546
SQ   SEQUENCE   771 AA;  87051 MW;  3A408B7D0D6FCEAE CRC64;
     MNPEERLVTW LISLGVLESP KKTVCDPEEF LKSSLKNGVV LCKLINRLLP GSVEKYCLEP
     QTEADCIDNI NDFLKGCATL QVEVFEPDDL YSGANFSKVL NTLLAVNKAT EDQLSERPCG
     RSSSLSAATS SQTNPQVAVP STAPEQHSEE KAEMTENGSH QLIVKARFNF KQTNEDELSV
     CKGDIIYVTR VEEGGWWEGT LNGRTGWFPS NYVREIKPSE RPLSPKAIKG FDTAPLTKNY
     YTVVLQNILD TEKEYAKELQ SLLVTYLRPL QSNNNLSTVE FTCLLGNFEE VCTFQQTLCQ
     ALEECSKFPE NQHKVGGCLL NLMPHFKSMY LAYCANHPSA VNVLTQHSDD LERFMENQGA
     SSPGILILTT SLSKPFMRLE KYVTLLQELE RHMEDTHPDH QDILKAIIAF KTLMGQCQDL
     RKRKQLELQI LSEPIQAWEG DDIKTLGNVI FMSQVVMQHG ACEEKEERYF LLFSSVLIML
     SASPRMSGFM YQGKIPIAGM VVNRLDEIEG SDCMFEITGS TVERIVVHCN NNQDFQEWME
     QLNRLTKGPT SCGSLSKTSS SSCSTHSSFS STGQPRGPLE PPQIIKPWSL SCLRPAPPLR
     PSAALGYKER MSYILKESSK SPKTMKKFLH KRKTERKASE EEYVIRKSTA ALEEDAQILK
     VIEAYCTSAS FQQGTRKDSV PQVLLPEEEK LIIEETRSNG QTIIEEKSLV DTVYALKDEV
     KELKQENKKM KQCLEEELKS RKDLEKLVRK LLKQTDECIR SESSSKTSIL Q
//
ID   MKL1_MOUSE              Reviewed;         964 AA.
AC   Q8K4J6; Q642U1;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2003, sequence version 2.
DT   08-FEB-2011, entry version 83.
DE   RecName: Full=MKL/myocardin-like protein 1;
DE   AltName: Full=Basic SAP coiled-coil transcription activator;
DE   AltName: Full=Megakaryoblastic leukemia 1 protein homolog;
DE   AltName: Full=Myocardin-related transcription factor A;
DE            Short=MRTF-A;
GN   Name=Mkl1; Synonyms=Bsac;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Spleen;
RX   MEDLINE=22151065; PubMed=12019265; DOI=10.1074/jbc.M203190200;
RA   Sasazuki T., Sawada Y., Sakon S., Kitamura T., Kishi T., Okazaki T.,
RA   Katano M., Tanaka M., Watanabe M., Yagita H., Okumura K., Nakano H.;
RT   "Identification of a novel transcriptional activator, BSAC, by a
RT   functional cloning to inhibit tumor necrosis factor-induced cell
RT   death.";
RL   J. Biol. Chem. 277:28853-28860(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6;
RX   MEDLINE=22317395; PubMed=12397177; DOI=10.1073/pnas.222561499;
RA   Wang D.-Z., Li S., Hockemeyer D., Sutherland L., Wang Z., Schratt G.,
RA   Richardson J.A., Nordheim A., Olson E.N.;
RT   "Potentiation of serum response factor activity by a family of
RT   myocardin-related transcription factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14855-14860(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, INTERACTION WITH ACTB; SCAI AND SRF, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=19350017; DOI=10.1038/ncb1862;
RA   Brandt D.T., Baarlink C., Kitzing T.M., Kremmer E., Ivaska J.,
RA   Nollau P., Grosse R.;
RT   "SCAI acts as a suppressor of cancer cell invasion through the
RT   transcriptional control of beta1-integrin.";
RL   Nat. Cell Biol. 11:557-568(2009).
CC   -!- FUNCTION: Transcriptional coactivator of serum response factor
CC       (SRF) with the potential to modulate SRF target genes. Suppresses
CC       TNF-induced cell death by inhibiting activation of caspases; its
CC       transcriptional activity is indispensable for the antiapoptotic
CC       function. It may up-regulate antiapoptotic molecules, which in
CC       turn inhibit caspase activation.
CC   -!- SUBUNIT: Forms with SCAI and SRF a nuclear ternary complex which
CC       binds the CArG consensus motif (CArG box) on DNA via SRF. Some
CC       authors (PubMed:12019265) have found contradictory results, they
CC       could not demonstrate that it forms a complex with the CArG boxes,
CC       even in the presence of SRF. Interacts with ACTB; interaction with
CC       ACTB prevents interaction with SCAI. Interacts with MKL2.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K4J6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K4J6-2; Sequence=VSP_007652;
CC   -!- TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung,
CC       liver, muscle, kidney and testis.
CC   -!- DEVELOPMENTAL STAGE: Detected throughout the embryo at 10.5 dpc;
CC       higher expression is found at 13.5 dpc in neural mesenchymal
CC       cells, skeletal muscle of the tongue, and epithelial cells of the
CC       colon and small intestine; at 15.5 dpc, expression in epithelial
CC       cells of lung, kidney, bladder, and colon is also detected.
CC   -!- DOMAIN: The N-terminal region is required for nuclear localization
CC       and the C-terminal region mediates transcriptional activity.
CC   -!- SIMILARITY: Contains 3 RPEL repeats.
CC   -!- SIMILARITY: Contains 1 SAP domain.
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DR   EMBL; AF385582; AAM94258.1; -; mRNA.
DR   EMBL; AF532597; AAN33041.1; -; mRNA.
DR   EMBL; AK044188; BAC31809.1; -; mRNA.
DR   EMBL; AK089416; BAC40873.1; -; mRNA.
DR   EMBL; BC050941; AAH50941.1; -; mRNA.
DR   IPI; IPI00276393; -.
DR   IPI; IPI00331708; -.
DR   RefSeq; NP_001076005.1; NM_001082536.1.
DR   RefSeq; NP_694629.2; NM_153049.2.
DR   UniGene; Mm.439814; -.
DR   PDB; 2V51; X-ray; 2.35 A; E/F=16-41.
DR   PDB; 2V52; X-ray; 1.45 A; M=54-85.
DR   PDBsum; 2V51; -.
DR   PDBsum; 2V52; -.
DR   ProteinModelPortal; Q8K4J6; -.
DR   SMR; Q8K4J6; 14-40, 54-83.
DR   STRING; Q8K4J6; -.
DR   PhosphoSite; Q8K4J6; -.
DR   PRIDE; Q8K4J6; -.
DR   Ensembl; ENSMUST00000109579; ENSMUSP00000105207; ENSMUSG00000042292.
DR   GeneID; 223701; -.
DR   KEGG; mmu:223701; -.
DR   UCSC; uc007wwc.1; mouse.
DR   UCSC; uc007wwd.1; mouse.
DR   CTD; 223701; -.
DR   MGI; MGI:2384495; Mkl1.
DR   GeneTree; ENSGT00530000063195; -.
DR   HOGENOM; HBG443837; -.
DR   HOVERGEN; HBG036493; -.
DR   InParanoid; Q8K4J6; -.
DR   OMA; SADFKEP; -.
DR   PhylomeDB; Q8K4J6; -.
DR   NextBio; 376834; -.
DR   ArrayExpress; Q8K4J6; -.
DR   Bgee; Q8K4J6; -.
DR   CleanEx; MM_MKL1; -.
DR   Genevestigator; Q8K4J6; -.
DR   GermOnline; ENSMUSG00000042292; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003785; F:actin monomer binding; IDA:UniProtKB.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0016563; F:transcription activator activity; IDA:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR   GO; GO:0006916; P:anti-apoptosis; IDA:MGI.
DR   InterPro; IPR004018; RPEL_repeat.
DR   InterPro; IPR003034; SAP_DNA-bd.
DR   Pfam; PF02755; RPEL; 3.
DR   Pfam; PF02037; SAP; 1.
DR   SMART; SM00707; RPEL; 3.
DR   SMART; SM00513; SAP; 1.
DR   PROSITE; PS51073; RPEL; 3.
DR   PROSITE; PS50800; SAP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil; Nucleus;
KW   Phosphoprotein; Repeat; Transcription; Transcription regulation.
FT   CHAIN         1    964       MKL/myocardin-like protein 1.
FT                                /FTId=PRO_0000126626.
FT   REPEAT       15     40       RPEL 1.
FT   REPEAT       59     84       RPEL 2.
FT   REPEAT      103    128       RPEL 3.
FT   DOMAIN      385    419       SAP.
FT   REGION        1    291       Mediates interaction with SCAI and ACTB.
FT   COILED      552    600       Potential.
FT   COMPBIAS    299    325       Gln-rich.
FT   COMPBIAS    712    844       Pro-rich.
FT   MOD_RES      41     41       Phosphoserine (By similarity).
FT   MOD_RES     488    488       Phosphothreonine (By similarity).
FT   MOD_RES     492    492       Phosphoserine (By similarity).
FT   VAR_SEQ       1     35       Missing (in isoform 2).
FT                                /FTId=VSP_007652.
FT   CONFLICT     53     53       E -> Q (in Ref. 3; BAC31809).
FT   CONFLICT    724    724       S -> D (in Ref. 3; BAC40873).
FT   CONFLICT    728    728       S -> F (in Ref. 1; AAM94258).
FT   HELIX        59     66
FT   HELIX        71     76
SQ   SEQUENCE   964 AA;  102546 MW;  AFAEA328A1860CE5 CRC64;
     MTLLEPEMLM MAVQSVLQLK LQQRRTREEL VSQGIMPPLK SPAAFHEQRR SLERARTEDY
     LKRKIRSRPE RAELVRMHIL EETSAEPSLQ AKQLKLKRAR LADDLNEKIA QRPGPMELVE
     KNILPVESSL KEAIIVGQVN YPKVADSSSF DEDSSDALSP EQPASHESQG SVPSPLESRV
     SDPLPSATSI SPTQVLSQLP MAPDPGETLF LAEQPPLPPA PLLPPSLANG SIVPTAKPAP
     TLIKQSQPKS ASEKSQRSKK AKELKPKVKK LKYHQYIPPD QKQDKGAPAM DSSYAKILQQ
     QQLFLQLQIL NQQQQQQQQQ HYNYQAILPA PPKPSAETPG SSAPTPSRSL STSSSPSSGT
     PGPSGLARQS STALAAKPGA LPANLDDMKV AELKQELKLR SLPVSGTKTE LIERLRAYQD
     QVSPAPGAPK APATTSVLSK AGEVVVAFPA ALLSTGSALV TAGLAPAEMV VATVTSNGMV
     KFGSTGSTPP VSPTPSERSL LSTGDENSTP GDAFGEMVTS PLTQLTLQAS PLQIVKEEGA
     RAASCCLSPG ARAELEGLDK DQMLQEKDKQ IEELTRMLQQ KQQLVELLRL QLEQQKRAQQ
     PAPASSPVKR ESGFSSCQLS CQPQGSAHAF GSGLVVPTTN HGDTQAPAPE SPPVVVKQEA
     GPPEPDLAPS SQLLLGSQGT SFLKRVSPPT LVTDSTGTHL ILTVTNKSAD GPGLPAGSPQ
     QPLSQPGSPA PGPPAQMDLE HPPQPPFATP TSLLKKEPPG YEETVTQQPK QQENGSSSQH
     MDDLFDILIQ SGEISADFKE PPSLPGKEKS PPAAAAYGPP LTPQPSPLSE LPQAAPPPGS
     PTLPGRLEDF LESSTGLPLL TSGHEGPEPL SLIDDLHSQM LSSSAILDHP PSPMDTSELH
     FAPEPSSGMG LDLAVGHLDS MDWLELSSGG PVLSLAPLST AAPSLFSMDF LDGHDLQLHW
     DSCL
//
ID   Q8K4P0_MOUSE            Unreviewed;      1330 AA.
AC   Q8K4P0;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   SubName: Full=Putative WDC146;
GN   Name=Wdr33; Synonyms=wdc146;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21092660; PubMed=11162572; DOI=10.1006/bbrc.2000.4163;
RA   Ito S., Sakai A., Nomura T., Miki Y., Ouchida M., Sasaki J.,
RA   Shimizu K.;
RT   "A novel WD40 repeat protein, WDC146, highly expressed during
RT   spermatogenesis in a stage-specific manner.";
RL   Biochem. Biophys. Res. Commun. 280:656-663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Sakai A., Ito S., Nomura T., Miki Y., Takai S., Ouchida M., Sasaki J.,
RA   Shimizu K.;
RT   "a novel human WD-repeat protein containing a collagen-like domain
RT   shows highly expression in testis.";
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AB086191; BAC00776.1; -; mRNA.
DR   IPI; IPI00170242; -.
DR   RefSeq; NP_083142.2; NM_028866.3.
DR   UniGene; Mm.277705; -.
DR   HSSP; P16649; 1ERJ.
DR   ProteinModelPortal; Q8K4P0; -.
DR   SMR; Q8K4P0; 120-403.
DR   STRING; Q8K4P0; -.
DR   PhosphoSite; Q8K4P0; -.
DR   PRIDE; Q8K4P0; -.
DR   Ensembl; ENSMUST00000025264; ENSMUSP00000025264; ENSMUSG00000024400.
DR   GeneID; 74320; -.
DR   KEGG; mmu:74320; -.
DR   UCSC; uc008eis.1; mouse.
DR   CTD; 74320; -.
DR   MGI; MGI:1921570; Wdr33.
DR   HOGENOM; HBG125697; -.
DR   HOVERGEN; HBG054623; -.
DR   InParanoid; Q8K4P0; -.
DR   OMA; GGPQGFM; -.
DR   PhylomeDB; Q8K4P0; -.
DR   NextBio; 340445; -.
DR   ArrayExpress; Q8K4P0; -.
DR   Bgee; Q8K4P0; -.
DR   Genevestigator; Q8K4P0; -.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF01391; Collagen; 1.
DR   Pfam; PF00400; WD40; 6.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 6.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Repeat; WD repeat.
SQ   SEQUENCE   1330 AA;  145267 MW;  5175B5DEB49F9A03 CRC64;
     MATEIGSPPR FFHMPRFQHQ APRQLFYKRP DFAQQQAMQQ LTFDGKRMRK AVNRKTIDYN
     PSVIKYLENR IWQRDQRDMR AIQPDAGYYN DLVPPIGMLN NPMNAVTTKF VRTSTNKVKC
     PVFVVRWTPE GRRLVTGASS GEFTLWNGLT FNFETILQAH DSPVRAMTWS HNDMWMLTAD
     HGGYVKYWQS NMNNVKMFQA HKEAIREASF SPTDNKFATC SDDGTVRIWD FLRCHEERIL
     RGHGADVKCV DWHPTKGLVV SGSKDSQQPI KFWDPKTGQS LATLHAHKNT VMEVKLNLNG
     NWLLTASRDH LCKLFDIRNL KEELQVFRGH KKEATAVAWH PVHEGLFASG GSDGSLLFWH
     VGVEKEVGGM EMAHEGMIWS LAWHPLGHIL CSGSNDHTSK FWTRNRPGDK MRDRYNLNLL
     PGMSEDGVEY DDLEPNSLAV IPGMGIPEQL KLAMEQEQMG KDESSEIEMT IPGLDWGMEE
     VMQKDQKKVP QKKVPYAKPI PAQFQQAWMQ NKVPIPAPNE VLNDRKEDIK LEEKKKTQAE
     IEQEMATLQY TNPQLLEQLK IERLAQKQAD QIQPPPSSGT PLLGPQPFSG QGPISQIPQG
     FQQPHPSQQM PLVPQMGPPG PQGQFRAPGP QGQMGPQGPP MHQGGGGPQG FMGPQGPQGP
     PQGLPRPQDM HGPQGMQRHP GPHGPLGPQG PPGPQGSSGP QGHMGPQGPP GPQGHIGPQG
     PPASQGHMGP QGPPGTQGMQ GPPGPRGMQG PPHPHGIQGG PASQGIQGPL MGLNPRGMQG
     PPGPRENQGP APQGLMIGHP PQEMRGPHPP SGLLGHGPQE MRGPQEMRGM QGPPPQGSML
     GPPQELRGPS GSQGQQGPPQ GSLGPPPQGG MQGPPGPQGQ QNPARGPHPS QGPIPFQQQK
     APLLGDGPRA PFNQEGQSTG PPPLIPGLGQ QGAQGRIPPL NPGQGPGPNK GDTRGPPNHH
     LGPMSERRHE QSGGPEHGPD RGPFRGGQDC RGPPDRRGSH PDFPDDFRPD DFHPDKRFGH
     RLREFEGRGG PLPQEEKWRR GGPGPPFPPD HREFNEGDGR GAARGPPGAW EGRRPGDDRF
     PRDPDDPRFR GRREESFRRG APPRHEGRAP PRGRDNFPGP DDFGPEEGFD ASDEAARGRD
     LRGRGRGTPR GGSRKCLLPT PDEFPRFEGG RKPDSWDGNR EPGPGHEHFR DAPRPDHPPH
     DGHSPASRER SSSLQGMDMA SLPPRKRPWH DGSGTSEHRE MEAQGGPSED RGSKGRGGPG
     PSQRVPKSGR SSSLDGDHHD GYHRDEPFGG PPGSSSSSRG ARSGSNWGRG SNMNSGPPRR
     GTSRGSGRGR
//
ID   HECW1_MOUSE             Reviewed;        1604 AA.
AC   Q8K4P8; Q6A086; Q8BIA6; Q8BKC2; Q8BKL3; Q8BKZ8;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=E3 ubiquitin-protein ligase HECW1;
DE            EC=6.3.2.-;
DE   AltName: Full=HECT, C2 and WW domain-containing protein 1;
DE   AltName: Full=NEDD4-like E3 ubiquitin-protein ligase 1;
DE            Short=mNEDL1;
GN   Name=Hecw1; Synonyms=Kiaa0322, Nedl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1212-1604 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Corpus striatum, Diencephalon, and Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 22-1604 (ISOFORM 1), FUNCTION, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=14684739; DOI=10.1074/jbc.M312389200;
RA   Miyazaki K., Fujita T., Ozaki T., Kato C., Kurose Y., Sakamoto M.,
RA   Kato S., Goto T., Itoyama Y., Aoki M., Nakagawara A.;
RT   "NEDL1, a novel ubiquitin-protein isopeptide ligase for dishevelled-1,
RT   targets mutant superoxide dismutase-1.";
RL   J. Biol. Chem. 279:11327-11335(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 414-1604 (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination
CC       and subsequent degradation of DVL1 (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with DVL1 and SSR3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8K4P8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K4P8-2; Sequence=VSP_023076;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8K4P8-3; Sequence=VSP_023074, VSP_023075;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q8K4P8-4; Sequence=VSP_023075;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in neurons of the
CC       spinal cord.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 HECT (E6AP-type E3 ubiquitin-protein
CC       ligase) domain.
CC   -!- SIMILARITY: Contains 2 WW domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC28516.1; Type=Erroneous initiation;
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DR   EMBL; AK033922; BAC28516.1; ALT_INIT; mRNA.
DR   EMBL; AK047678; BAC33122.1; -; mRNA.
DR   EMBL; AK051569; BAC34677.1; -; mRNA.
DR   EMBL; AK053694; BAC35477.1; -; mRNA.
DR   EMBL; AC154615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC154511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB083710; BAB97389.1; -; mRNA.
DR   EMBL; AK172932; BAD32210.1; -; mRNA.
DR   IPI; IPI00403957; -.
DR   IPI; IPI00461506; -.
DR   IPI; IPI00666236; -.
DR   IPI; IPI00875875; -.
DR   RefSeq; NP_001074817.3; NM_001081348.3.
DR   UniGene; Mm.125298; -.
DR   HSSP; Q8CFI0; 1WR4.
DR   ProteinModelPortal; Q8K4P8; -.
DR   SMR; Q8K4P8; 207-341, 828-858, 946-1054, 1224-1599.
DR   STRING; Q8K4P8; -.
DR   PRIDE; Q8K4P8; -.
DR   Ensembl; ENSMUST00000039097; ENSMUSP00000048972; ENSMUSG00000021301.
DR   GeneID; 94253; -.
DR   KEGG; mmu:94253; -.
DR   UCSC; uc007pnd.1; mouse.
DR   CTD; 94253; -.
DR   MGI; MGI:2444115; Hecw1.
DR   eggNOG; roNOG04768; -.
DR   GeneTree; ENSGT00570000078981; -.
DR   HOGENOM; HBG445632; -.
DR   HOVERGEN; HBG057414; -.
DR   InParanoid; Q8K4P8; -.
DR   PhylomeDB; Q8K4P8; -.
DR   NextBio; 352271; -.
DR   ArrayExpress; Q8K4P8; -.
DR   Bgee; Q8K4P8; -.
DR   Genevestigator; Q8K4P8; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0006464; P:protein modification process; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR000569; HECT.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00397; WW; 2.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF56204; HECT; 1.
DR   SUPFAM; SSF51045; WW_Rsp5_WWP; 2.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 2.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Ligase; Repeat;
KW   Ubl conjugation pathway.
FT   CHAIN         1   1604       E3 ubiquitin-protein ligase HECW1.
FT                                /FTId=PRO_0000277666.
FT   DOMAIN      192    302       C2.
FT   DOMAIN      826    859       WW 1.
FT   DOMAIN     1016   1049       WW 2.
FT   DOMAIN     1269   1604       HECT.
FT   COILED      871    898       Potential.
FT   COMPBIAS    407    524       Glu-rich.
FT   COMPBIAS    671    703       Cys-rich.
FT   ACT_SITE   1572   1572       Glycyl thioester intermediate (By
FT                                similarity).
FT   VAR_SEQ       1      8       MLLHLCSV -> MICAQLEAA (in isoform 3).
FT                                /FTId=VSP_023074.
FT   VAR_SEQ     316   1604       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_023075.
FT   VAR_SEQ     782    795       Missing (in isoform 2).
FT                                /FTId=VSP_023076.
FT   CONFLICT    154    154       C -> S (in Ref. 1; BAC33122/BAC34677/
FT                                BAC35477 and 3; BAB97389).
FT   CONFLICT    167    167       S -> R (in Ref. 3; BAB97389).
FT   CONFLICT    241    241       F -> Y (in Ref. 1; BAC34677).
FT   CONFLICT    823    823       T -> A (in Ref. 3; BAB97389).
FT   CONFLICT   1036   1036       D -> G (in Ref. 3; BAB97389).
FT   CONFLICT   1248   1248       V -> I (in Ref. 1; BAC28516 and 3;
FT                                BAD32210).
FT   CONFLICT   1356   1356       L -> P (in Ref. 3; BAB97389).
FT   CONFLICT   1538   1538       V -> M (in Ref. 3; BAB97389).
SQ   SEQUENCE   1604 AA;  179469 MW;  5C9E9B5C5FC5D1E2 CRC64;
     MLLHLCSVKN LYQNRFLGLA AMASPSRNSQ SRRRCKEPLR YSYNPDQFHN IDIRNGAHDA
     ITIPRSTSDT DLVTSDSRST LMVSSSYYSI GHSQDLVIHW DIKEEVDAGD WIGMYLIGEV
     SSENFLDYKN RGVNGSHRGQ IIWKIDASSY FVECETKICF KYYHGVSGAL RATTPSVTVK
     NSAAPIFKGI GSEETAQSQG SRRLISFSLS DFQAMGLKKG MFFNPDPYLK ISIQPGKHSI
     FPALPHHGQE RRSTIIGNTV NPIWQAEHFS FVSLPTDVLE IEVKDKFAKS RPIIKRFLGK
     LSMPVQRLLE RHAIGDRVVS YTLGRRLPTD HVSGQLQFRF EITSSIHADD EEISLSAEPE
     SSAETQDSIM NSMVGNSNGE PSGDATEFCK DAKPESPSEG NGVNSSENQN QEHAGPVEEA
     AGAMEARDGS NVSEAPEEPG ELQDPEQHDT QPTLSAEEVA EGLPLDEDSP SSLLPEENTA
     LGSKVEEETV PENGAREEEM QKGKDEEEEE EDVSTLEQGE PGLELRVSVR KKSRPCSLPV
     SELETVIASA CGDAETPRTH YIRIHTLLHS MPSAQRGSTT EEEDGLEEES TLKESSEKDG
     LSEVDTIAAD PQSMEDGESD GATLCMAPSD CSGGHFSSLS KGIGAGQDGE AHPSTGSESD
     SSPQQGADHS CEGCDASCCS PSCYSTSCYS SSCYSSSCYS SSCYNGNNRF ASHTRFSSVD
     SAKISESTVF SSQEDEEEEN SAFESVPDSV QSPELDPEST NGAGPWQDEL AAPGGNAARS
     TEGLESPMAG PSNRREGECP ILHNSQPISQ LPSLRPEHHH YPTIDEPLPP NWEARIDSHG
     RVFYVDHINR TTTWQRPSMA PTPDGMIRSG SVHQMEQLNR RYQNIQRTMA TERAEEDSGN
     QNSEQIPDGG GGGGGGSDSE AESSQSSLDL RREGSLSPVN SQKVTLLLQS PAVKFITNPE
     FFTVLHANYS AYRVFTSSTC LKHMILKVRR DARNFERYQH NRDLVNFINM FADTRLELPR
     GWEIKTDHQG KSFFVDHNSR ATTFIDPRIP LQNGRLPNHL THRQHLQRLR SYSAGEASEV
     SRNRGASLLA RPGHSLIAAI RSQHQHESLP LAYNDKIVAF LRQPNIFEML QERQPSLARN
     HTLREKIHYI RTEGNHGLDK LSCDADLVIL LSLFEEEIMS YVPLQSAFHP GYSFSPRCSP
     CSSPQNSPGL QRASARAPSP YRRDFEAKLR NFYRKLEAKG FGQGPGKVKL IIRRDHLLEG
     TFNQVMAYSR KELQRNKLYI TFVGEEGLDY SGPSREFFFL LSQELFNPYY GLFEYSANDT
     YTVQISPMSA FVENYLEWFR FSGRILGLAL IHQYLLDAFF TRPFYKGLLK LPCDLSDLEY
     LDEEFHQSLQ WMKDNNITDI LDLTFTVNEE VFGQVTEREL KSGGANTQVT EKNKKEYIER
     MVKWRVERGV VQQTEALLRG FYEVVDSRLV SVFDARELEL VIAGTAEIDL NDWRNNTEYR
     GGYHDGHLVI RWFWAAVERF NNEQRLRLLQ FVTGTSSVPY EGFAALRGSN GLRRFCIEKW
     GKITSLPRAH TCFNRLDLPP YPSYSMLYEK LLTAVEETST FGLE
//
ID   RPTOR_MOUSE             Reviewed;        1335 AA.
AC   Q8K4Q0; Q8C9W9; Q8CBY4; Q8CDY8; Q9D4H3;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Regulatory-associated protein of mTOR;
DE            Short=Raptor;
DE   AltName: Full=p150 target of rapamycin (TOR)-scaffold protein;
GN   Name=Rptor; Synonyms=Raptor;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=22145924; PubMed=12150926; DOI=10.1016/S0092-8674(02)00833-4;
RA   Hara K., Maruki Y., Long X., Yoshino K., Oshiro N., Hidayat S.,
RA   Tokunaga C., Avruch J., Yonezawa K.;
RT   "Raptor, a binding partner of target of rapamycin (TOR), mediates TOR
RT   action.";
RL   Cell 110:177-189(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 5).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon, Head, Testis, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-857 AND SER-863, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-877, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859 AND SER-863, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Involved in the control of the mammalian target of
CC       rapamycin complex 1 (mTORC1) activity which regulates cell growth
CC       and survival, and autophagy in response to nutrient and hormonal
CC       signals; functions as a scaffold for recruiting mTORC1 substrates.
CC       mTORC1 is activated in response to growth factors or amino-acids.
CC       Growth factor-stimulated mTORC1 activation involves a AKT1-
CC       mediated phosphorylation of TSC1-TSC2, which leads to the
CC       activation of the RHEB GTPase that potently activates the protein
CC       kinase activity of mTORC1. Amino-acid-signaling to mTORC1 requires
CC       its relocalization to the lysosomes mediated by the Ragulator
CC       complex and the Rag GTPases. Activated mTORC1 up-regulates protein
CC       synthesis by phosphorylating key regulators of mRNA translation
CC       and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and
CC       releases it from inhibiting the elongation initiation factor 4E
CC       (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389',
CC       which then promotes protein synthesis by phosphorylating PDCD4 and
CC       targeting it for degradation (By similarity).
CC   -!- SUBUNIT: Part of the mammalian target of rapamycin complex 1
CC       (mTORC1) which contains MTOR, MLST8, RPTOR and AKT1S1. mTORC1
CC       binds to and is inhibited by FKBP12-rapamycin. Binds directly
CC       4EBP1 and RPS6KB1 independently of its association with MTOR.
CC       Binds preferentially to poorly or non-phosphorylated form of
CC       EIF4EBP1, and this binding is critical to the ability of MTOR to
CC       catalyze phosphorylation. Forms a complex with MTOR under both
CC       leucine-rich and -poor conditions (By similarity). Interacts with
CC       ULK1 in a nutrient-dependent manner; the interaction is reduced
CC       during starvation (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Lysosome (By
CC       similarity). Note=Targeting to lysosomes depends on amino acid
CC       availability (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q8K4Q0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8K4Q0-2; Sequence=VSP_010175, VSP_010181, VSP_010182;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8K4Q0-3; Sequence=VSP_010177, VSP_010179, VSP_010180;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q8K4Q0-4; Sequence=VSP_010176, VSP_010183, VSP_010184;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q8K4Q0-5; Sequence=VSP_010178;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the WD repeat RAPTOR family.
CC   -!- SIMILARITY: Contains 7 WD repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AK029341; Type=Frameshift; Positions=22;
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DR   EMBL; AB082952; BAC06491.1; -; mRNA.
DR   EMBL; AK016530; BAB30288.1; -; mRNA.
DR   EMBL; AK029341; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK034306; BAC28669.1; -; mRNA.
DR   EMBL; AK040288; BAC30561.1; -; mRNA.
DR   IPI; IPI00170249; -.
DR   IPI; IPI00407061; -.
DR   IPI; IPI00411051; -.
DR   IPI; IPI00411053; -.
DR   IPI; IPI00411054; -.
DR   UniGene; Mm.209933; -.
DR   ProteinModelPortal; Q8K4Q0; -.
DR   SMR; Q8K4Q0; 474-670, 1017-1097, 1202-1332.
DR   DIP; DIP-46324N; -.
DR   STRING; Q8K4Q0; -.
DR   PhosphoSite; Q8K4Q0; -.
DR   PRIDE; Q8K4Q0; -.
DR   Ensembl; ENSMUST00000026671; ENSMUSP00000026671; ENSMUSG00000025583.
DR   UCSC; uc007mqw.1; mouse.
DR   UCSC; uc007mqz.1; mouse.
DR   MGI; MGI:1921620; Rptor.
DR   GeneTree; ENSGT00390000005679; -.
DR   HOGENOM; HBG737108; -.
DR   HOVERGEN; HBG059496; -.
DR   InParanoid; Q8K4Q0; -.
DR   OrthoDB; EOG46Q6RQ; -.
DR   PhylomeDB; Q8K4Q0; -.
DR   ArrayExpress; Q8K4Q0; -.
DR   Bgee; Q8K4Q0; -.
DR   CleanEx; MM_4932417H02RIK; -.
DR   Genevestigator; Q8K4Q0; -.
DR   GermOnline; ENSMUSG00000025583; Mus musculus.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0031931; C:TORC1 complex; ISS:UniProtKB.
DR   GO; GO:0016049; P:cell growth; ISS:UniProtKB.
DR   GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR   GO; GO:0031929; P:TOR signaling cascade; ISS:UniProtKB.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000357; HEAT.
DR   InterPro; IPR004083; Raptor.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 2.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   PANTHER; PTHR12848; Raptor; 1.
DR   Pfam; PF02985; HEAT; 1.
DR   Pfam; PF00400; WD40; 3.
DR   PRINTS; PR01547; YEAST176DUF.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Lysosome; Phosphoprotein; Repeat;
KW   WD repeat.
FT   CHAIN         1   1335       Regulatory-associated protein of mTOR.
FT                                /FTId=PRO_0000051201.
FT   REPEAT     1020   1061       WD 1.
FT   REPEAT     1065   1106       WD 2.
FT   REPEAT     1121   1160       WD 3.
FT   REPEAT     1164   1203       WD 4.
FT   REPEAT     1209   1249       WD 5.
FT   REPEAT     1251   1291       WD 6.
FT   REPEAT     1299   1335       WD 7.
FT   MOD_RES     719    719       Phosphoserine (By similarity).
FT   MOD_RES     721    721       Phosphoserine (By similarity).
FT   MOD_RES     722    722       Phosphoserine (By similarity).
FT   MOD_RES     857    857       Phosphothreonine.
FT   MOD_RES     859    859       Phosphoserine.
FT   MOD_RES     863    863       Phosphoserine.
FT   MOD_RES     865    865       Phosphothreonine (By similarity).
FT   MOD_RES     877    877       Phosphoserine.
FT   VAR_SEQ       1    954       Missing (in isoform 4).
FT                                /FTId=VSP_010176.
FT   VAR_SEQ       1    421       Missing (in isoform 3).
FT                                /FTId=VSP_010177.
FT   VAR_SEQ       1    185       Missing (in isoform 2).
FT                                /FTId=VSP_010175.
FT   VAR_SEQ     298   1335       Missing (in isoform 5).
FT                                /FTId=VSP_010178.
FT   VAR_SEQ     701    728       EGGSLTPVRDSPCTPRLRSVSSYGNIRA -> GTGVAGSLG
FT                                PPSGPSPGQSVAWVQPGQV (in isoform 3).
FT                                /FTId=VSP_010179.
FT   VAR_SEQ     729   1335       Missing (in isoform 3).
FT                                /FTId=VSP_010180.
FT   VAR_SEQ     841    843       ATV -> VCI (in isoform 2).
FT                                /FTId=VSP_010181.
FT   VAR_SEQ     844   1335       Missing (in isoform 2).
FT                                /FTId=VSP_010182.
FT   VAR_SEQ    1202   1202       C -> W (in isoform 4).
FT                                /FTId=VSP_010183.
FT   VAR_SEQ    1203   1335       Missing (in isoform 4).
FT                                /FTId=VSP_010184.
FT   CONFLICT    630    630       S -> F (in Ref. 2; AK029341/BAB30288).
FT   CONFLICT    970    970       A -> P (in Ref. 2; BAC30561).
SQ   SEQUENCE   1335 AA;  149471 MW;  26702199FF7C8136 CRC64;
     MESEMLQSPL MGLGEEDEAD LTDWNLPLAF MKKRHCEKIE GSKSLAQSWR MKDRMKTVSV
     ALVLCLNVGV DPPDVVKTTP CARLECWIDP LSMGPQKALE TIGANLQKQY ENWQPRARYK
     QSLDPTVDEV KKLCTSLRRN AKEERVLFHY NGHGVPRPTV NGEVWVFNKN YTQYIPLSIY
     DLQTWMGSPS IFVYDCSNAG LIVKSFKQFA LQREQELEVA AINPNHPLAQ MPLPPSMKNC
     IQLAACEAHE LLPMIPDLPA DLFTSCLTTP IKIALRWFCM QKCVSLVPGV TLDLIEKIPG
     RLNDRRTPLG ELNWIFTAIT DTIAWNVLPR DLFQKLFRQD LLVASLFRNF LLAERIMRSY
     NCTPVSSPRL PPTYMHAMWQ AWDLAVDICL SQLPTIIEEG TAFRHSPFFA EQLTAFQVWL
     TMGVENRSPP EQLPIVLQVL LSQVHRLRAL DLLGRFLDLG PWAVSLALSV GIFPYVLKLL
     QSSARELRPL LVFIWAKILA VDSSCQADLV KDNGHKYFLS VLADPYMPAE HRTMTAFILA
     VIVNSYTTGQ EACLQGNLIA ICLEQLSDPH PLLRQWVAIC LGRIWQNFDS ARWCGVRDSA
     HEKLYSLLSD PIPEVRCAAV FALGTFVGNS AERTDHSTTI DHNVAMMLAQ LINDGSPMVR
     KELVVALSHL VVQYESNFCT VALQFMEEEK NYPLPSPAAT EGGSLTPVRD SPCTPRLRSV
     SSYGNIRAVT TARNLNKSLQ NLSLTEESGS SVAFSPGNLS TSSSASSTLG SPENEEYILS
     FETIDKMRRV SSYSALNSLI GVSFNSVYTQ IWRVLLHLAA DPYPDVSDLA MKVLNSIAYK
     ATVNARPQRI LDTSSLTQSA PASPTNKGMH MHQVGGSPPA SSTSSCSLTN DVAKQTVSRD
     LPSSRPGTAG PTGAQYTPHS HQFPRTRKMF DKGPDQTTDD ADDAAGHKSF ICASMQTGFC
     DWSARYFAQA VMKIPEEHDL ESQIRKEREW RFLRNTRVRK QAQQVIQKGI TRLDDQIFLN
     RNPGVPSVVK FHPFTPCIAV ADKDSICFWD WEKGEKLDYF HNGNPRYTRV TAMEYLNGQD
     CSLLLTATDD GAIRVWKNFA DLEKNPEMVT AWQGLSDMLP TTRGAGMVVD WEQETGLLMS
     SGDVRIVRIW DTDRETKVQD IPTGADSCVT SLSCDSHRSL IVAGLGDGSI RVYDRRMALS
     ECRVMTYREH TAWVVKAYLQ KHPEGHIVSV SVNGDVRFFD PRMPESVNVM QIVKGLTALD
     IHPQANLIAC GSMNQFTAIY NGNGELINNI KYYDGFMGQR VGAISCLAFH PHWPHLAVGS
     NDYYISVYSV EKRVR
//
ID   PITC1_MOUSE             Reviewed;         332 AA.
AC   Q8K4R4; A2A650; A2A651; Q3TBB3; Q3U5F5; Q8K4R5;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=Cytoplasmic phosphatidylinositol transfer protein 1;
DE   AltName: Full=Mammalian rdgB homolog beta;
DE            Short=M-rdgB beta;
DE            Short=MrdgBbeta;
DE            Short=mM-rdgBbeta;
DE   AltName: Full=Retinal degeneration B homolog beta;
DE            Short=RdgBbeta;
GN   Name=Pitpnc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=12562526; DOI=10.1046/j.1471-4159.2003.01591.x;
RA   Takano N., Owada Y., Suzuki R., Sakagami H., Shimosegawa T., Kondo H.;
RT   "Cloning and characterization of a novel variant (mM-rdgBbeta1) of
RT   mouse M-rdgBs, mammalian homologs of Drosophila retinal degeneration B
RT   gene proteins, and its mRNA localization in mouse brain in comparison
RT   with other M-rdgBs.";
RL   J. Neurochem. 84:829-839(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
CC   -!- FUNCTION: Phosphatidylinositol transfer proteins mediate the
CC       monomeric transport of lipids by shielding a lipid from the
CC       aqueous environment and binding the lipid in a hydrophobic cavity.
CC       Able to transfer phosphatidylinositol in vitro. Isoform 2
CC       specifically binds to phosphatidylinositol but not to other
CC       phospholipids and may play a role in the phosphoinositide-mediated
CC       signaling in the neural development.
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=mM-rdgBbeta;
CC         IsoId=Q8K4R4-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2; Synonyms=mM-rdgBbeta1;
CC         IsoId=Q8K4R4-2; Sequence=VSP_025549, VSP_025551;
CC       Name=3;
CC         IsoId=Q8K4R4-3; Sequence=VSP_025548, VSP_025550;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q8K4R4-4; Sequence=VSP_025546, VSP_025547;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is widely expressed. Isoform 2 is
CC       weakly expressed. In brain, isoform 2 is weakly expressed and is
CC       rather confined to the embryonic stage. In contrast, isoform 1 is
CC       widely expressed in brain, with expression in the gray matters of
CC       pre- and postnatal brains.
CC   -!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI
CC       transfer class IIB subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM17314.1; Type=Erroneous gene model prediction;
CC       Sequence=CAM17315.1; Type=Erroneous gene model prediction;
CC       Sequence=CAM20627.1; Type=Erroneous gene model prediction;
CC       Sequence=CAM25441.1; Type=Erroneous gene model prediction;
CC       Sequence=CAM25442.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AB077281; BAC02913.1; -; mRNA.
DR   EMBL; AB077282; BAC02914.1; -; mRNA.
DR   EMBL; AK153625; BAE32124.1; -; mRNA.
DR   EMBL; AK171340; BAE42401.1; -; mRNA.
DR   EMBL; AL596116; CAM20633.1; -; Genomic_DNA.
DR   EMBL; AL645687; CAM20633.1; JOINED; Genomic_DNA.
DR   EMBL; AL645905; CAM20633.1; JOINED; Genomic_DNA.
DR   EMBL; AL596116; CAM20627.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL645687; CAM20627.1; JOINED; Genomic_DNA.
DR   EMBL; AL645905; CAM20627.1; JOINED; Genomic_DNA.
DR   EMBL; AL596116; CAM20628.1; -; Genomic_DNA.
DR   EMBL; AL645687; CAM20628.1; JOINED; Genomic_DNA.
DR   EMBL; AL645905; CAM20628.1; JOINED; Genomic_DNA.
DR   EMBL; AL645687; CAM25441.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL596116; CAM25441.1; JOINED; Genomic_DNA.
DR   EMBL; AL645905; CAM25441.1; JOINED; Genomic_DNA.
DR   EMBL; AL645687; CAM25442.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL596116; CAM25442.1; JOINED; Genomic_DNA.
DR   EMBL; AL645905; CAM25442.1; JOINED; Genomic_DNA.
DR   EMBL; AL645687; CAM25443.1; -; Genomic_DNA.
DR   EMBL; AL596116; CAM25443.1; JOINED; Genomic_DNA.
DR   EMBL; AL645905; CAM25443.1; JOINED; Genomic_DNA.
DR   EMBL; AL645905; CAM17314.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL596116; CAM17314.1; JOINED; Genomic_DNA.
DR   EMBL; AL645687; CAM17314.1; JOINED; Genomic_DNA.
DR   EMBL; AL645905; CAM17315.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL596116; CAM17315.1; JOINED; Genomic_DNA.
DR   EMBL; AL645687; CAM17315.1; JOINED; Genomic_DNA.
DR   EMBL; AL645905; CAM17317.1; -; Genomic_DNA.
DR   EMBL; AL596116; CAM17317.1; JOINED; Genomic_DNA.
DR   EMBL; AL645687; CAM17317.1; JOINED; Genomic_DNA.
DR   EMBL; BC108351; AAI08352.1; -; mRNA.
DR   IPI; IPI00463203; -.
DR   IPI; IPI00473215; -.
DR   IPI; IPI00648419; -.
DR   IPI; IPI00845562; -.
DR   RefSeq; NP_665822.1; NM_145823.2.
DR   UniGene; Mm.397413; -.
DR   UniGene; Mm.476186; -.
DR   HSSP; P53812; 2A1L.
DR   ProteinModelPortal; Q8K4R4; -.
DR   SMR; Q8K4R4; 1-255.
DR   STRING; Q8K4R4; -.
DR   PRIDE; Q8K4R4; -.
DR   Ensembl; ENSMUST00000103064; ENSMUSP00000099353; ENSMUSG00000040430.
DR   GeneID; 71795; -.
DR   KEGG; mmu:71795; -.
DR   UCSC; uc007mam.1; mouse.
DR   CTD; 71795; -.
DR   MGI; MGI:1919045; Pitpnc1.
DR   eggNOG; roNOG09685; -.
DR   GeneTree; ENSGT00550000074351; -.
DR   HOVERGEN; HBG058915; -.
DR   InParanoid; Q8K4R4; -.
DR   OMA; DMTMDDV; -.
DR   OrthoDB; EOG4TQM9G; -.
DR   NextBio; 334538; -.
DR   ArrayExpress; Q8K4R4; -.
DR   Bgee; Q8K4R4; -.
DR   Genevestigator; Q8K4R4; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0008526; F:phosphatidylinositol transporter activity; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR   InterPro; IPR001666; PI_transfer.
DR   PANTHER; PTHR10658; PI_transfer; 1.
DR   Pfam; PF02121; IP_trans; 1.
DR   PRINTS; PR00391; PITRANSFER.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Lipid transport; Lipid-binding;
KW   Nucleus; Phosphoprotein; Transport.
FT   CHAIN         1    332       Cytoplasmic phosphatidylinositol transfer
FT                                protein 1.
FT                                /FTId=PRO_0000287531.
FT   MOD_RES     274    274       Phosphoserine.
FT   VAR_SEQ     208    209       VR -> GC (in isoform 4).
FT                                /FTId=VSP_025546.
FT   VAR_SEQ     210    332       Missing (in isoform 4).
FT                                /FTId=VSP_025547.
FT   VAR_SEQ     228    234       DMTMDEV -> GKSDGPK (in isoform 3).
FT                                /FTId=VSP_025548.
FT   VAR_SEQ     233    268       EVREFERATQEATNKKIGVFPPAISISSIALLPSSV -> D
FT                                VREYEKNMHEQTNIKVCNQHSSTVDDIESHAQTST (in
FT                                isoform 2).
FT                                /FTId=VSP_025549.
FT   VAR_SEQ     235    332       Missing (in isoform 3).
FT                                /FTId=VSP_025550.
FT   VAR_SEQ     269    332       Missing (in isoform 2).
FT                                /FTId=VSP_025551.
SQ   SEQUENCE   332 AA;  38384 MW;  A20BF9EEAB80E178 CRC64;
     MLLKEYRICM PLTVDEYKIG QLYMISKHSH EQSDRGEGVE VVQNEPFEDP HHGNGQFTEK
     RVYLNSKLPS WARAVVPKIF YVTEKAWNYY PYTITEYTCS FLPKFSIHIE TKYEDNKGSN
     DSIFDSEAKD LEREVCFIDI ACDEIPERYY KESEDPKHFK SEKTGRGQLR EGWRDNHQPI
     MCSYKLVTVK FEVWGLQTRV EQFVHKVVRD ILLIGHRQAF AWVDEWYDMT MDEVREFERA
     TQEATNKKIG VFPPAISISS IALLPSSVRS APSSAPSTPL STDAPEFLSI PKDRPRKKSA
     PETLTLPDPE KKATLNLPGV YTSEKPCRPK SE
//
ID   AIBP_MOUSE              Reviewed;         282 AA.
AC   Q8K4Z3;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Apolipoprotein A-I-binding protein;
DE            Short=AI-BP;
DE   Flags: Precursor;
GN   Name=Apoa1bp; Synonyms=Aibp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster;
RX   MEDLINE=21988047; PubMed=11991719; DOI=10.1006/geno.2002.6761;
RA   Ritter M., Buechler C., Boettcher A., Barlage S., Schmitz-Madry A.,
RA   Orso E., Bared S.M., Schmiedeknecht G., Baehr C.H., Fricker G.,
RA   Schmitz G.;
RT   "Cloning and characterization of a novel apolipoprotein A-I-binding
RT   protein, AI-BP, secreted by cells of the kidney proximal tubules in
RT   response to HDL or ApoA-I.";
RL   Genomics 79:693-702(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF
RP   25-282, SUBUNIT, AND PHOSPHORYLATION AT SER-43.
RC   STRAIN=BALB/c; TISSUE=Testis;
RX   PubMed=18202122; DOI=10.1210/en.2007-0582;
RA   Jha K.N., Shumilin I.A., Digilio L.C., Chertihin O., Zheng H.,
RA   Schmitz G., Visconti P.E., Flickinger C.J., Minor W., Herr J.C.;
RT   "Biochemical and structural characterization of apolipoprotein A-I
RT   binding protein, a novel phosphoprotein with a potential role in sperm
RT   capacitation.";
RL   Endocrinology 149:2108-2120(2008).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SUBUNIT: Interacts with APOA1 and APOA2 (By similarity).
CC       Homodimer.
CC   -!- SUBCELLULAR LOCATION: Secreted (By similarity).
CC   -!- SIMILARITY: Contains 1 YjeF N-terminal domain.
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DR   EMBL; AJ344092; CAC86966.1; -; mRNA.
DR   EMBL; AY566271; AAT70236.1; -; mRNA.
DR   EMBL; AK159846; BAE35424.1; -; mRNA.
DR   EMBL; BC058362; AAH58362.1; -; mRNA.
DR   IPI; IPI00170307; -.
DR   RefSeq; NP_659146.1; NM_144897.3.
DR   UniGene; Mm.205996; -.
DR   PDB; 2DG2; X-ray; 2.45 A; A/B/C/D/E/F=25-282.
DR   PDB; 2O8N; X-ray; 2.00 A; A=25-282.
DR   PDBsum; 2DG2; -.
DR   PDBsum; 2O8N; -.
DR   ProteinModelPortal; Q8K4Z3; -.
DR   SMR; Q8K4Z3; 50-282.
DR   STRING; Q8K4Z3; -.
DR   PhosphoSite; Q8K4Z3; -.
DR   REPRODUCTION-2DPAGE; Q8K4Z3; -.
DR   PRIDE; Q8K4Z3; -.
DR   Ensembl; ENSMUST00000029708; ENSMUSP00000029708; ENSMUSG00000028070.
DR   GeneID; 246703; -.
DR   KEGG; mmu:246703; -.
DR   UCSC; uc008ptu.1; mouse.
DR   CTD; 246703; -.
DR   MGI; MGI:2180167; Apoa1bp.
DR   eggNOG; maNOG16986; -.
DR   GeneTree; ENSGT00390000007227; -.
DR   HOGENOM; HBG608485; -.
DR   HOVERGEN; HBG058276; -.
DR   InParanoid; Q8K4Z3; -.
DR   OMA; GWDVENG; -.
DR   OrthoDB; EOG4P5K9V; -.
DR   PhylomeDB; Q8K4Z3; -.
DR   NextBio; 387247; -.
DR   ArrayExpress; Q8K4Z3; -.
DR   Bgee; Q8K4Z3; -.
DR   CleanEx; MM_APOA1BP; -.
DR   Genevestigator; Q8K4Z3; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   InterPro; IPR004443; YjeF_N.
DR   Gene3D; G3DSA:3.40.50.10260; G3DSA:3.40.50.10260; 1.
DR   Pfam; PF03853; YjeF_N; 1.
DR   SUPFAM; SSF64153; YjeF_N; 1.
DR   TIGRFAMs; TIGR00197; yjeF_nterm; 1.
DR   PROSITE; PS51385; YJEF_N; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Phosphoprotein; Secreted; Signal.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25    282       Apolipoprotein A-I-binding protein.
FT                                /FTId=PRO_0000292423.
FT   DOMAIN       59    269       YjeF N-terminal.
FT   MOD_RES      43     43       Phosphoserine; by PKA.
FT   HELIX        56     68
FT   HELIX        74     92
FT   HELIX        95     97
FT   STRAND       98    102
FT   STRAND      104    109
FT   HELIX       113    127
FT   STRAND      131    135
FT   HELIX       143    154
FT   HELIX       167    173
FT   STRAND      175    181
FT   HELIX       194    201
FT   STRAND      208    211
FT   TURN        219    221
FT   STRAND      230    237
FT   HELIX       240    244
FT   STRAND      247    253
FT   HELIX       259    264
SQ   SEQUENCE   282 AA;  30973 MW;  DFD95155755D8D96 CRC64;
     MSGLRTLLGL GLLVAGSRLP RVISQQSVCR ARPIWWGTQR RGSETMAGAA VKYLSQEEAQ
     AVDQELFNEY QFSVDQLMEL AGLSCATAIA KAYPPTSMSK SPPTVLVICG PGNNGGDGLV
     CARHLKLFGY QPTIYYPKRP NKPLFTGLVT QCQKMDIPFL GEMPPEPMMV DELYELVVDA
     IFGFSFKGDV REPFHSILSV LSGLTVPIAS IDIPSGWDVE KGNPSGIQPD LLISLTAPKK
     SATHFTGRYH YLGGRFVPPA LEKKYQLNLP SYPDTECVYR LQ
//
ID   MCFD2_MOUSE             Reviewed;         145 AA.
AC   Q8K5B2; Q3U9G5;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Multiple coagulation factor deficiency protein 2 homolog;
DE   AltName: Full=Neural stem cell-derived neuronal survival protein;
DE   Flags: Precursor;
GN   Name=Mcfd2; Synonyms=Sdnsf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Toda H., Tashiro K., Takahashi J., Hashimoto N., Nakano I., Kobuke K.,
RA   Tsuji M., Honjo T.;
RT   "Isolation and characterization of SDNSF, a novel secretory molecule
RT   with neuronal survival effect, from adult rat hippocampal stem
RT   cells.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow, Hippocampus, Pancreas, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: The MCFD2-LMAN1 complex forms a specific cargo receptor
CC       for the ER-to-Golgi transport of selected proteins (By
CC       similarity).
CC   -!- SUBUNIT: Interacts in a calcium-dependent manner with LMAN1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC       compartment (By similarity). Endoplasmic reticulum (By
CC       similarity). Golgi apparatus (By similarity).
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
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DR   EMBL; AF475283; AAM28464.1; -; mRNA.
DR   EMBL; AK033139; BAC28169.1; -; mRNA.
DR   EMBL; AK075781; BAC35955.1; -; mRNA.
DR   EMBL; AK077139; BAC36638.1; -; mRNA.
DR   EMBL; AK077631; BAC36914.1; -; mRNA.
DR   EMBL; AK141599; BAE24757.1; -; mRNA.
DR   EMBL; AK151803; BAE30702.1; -; mRNA.
DR   IPI; IPI00170316; -.
DR   RefSeq; NP_647456.1; NM_139295.3.
DR   RefSeq; NP_789778.1; NM_176808.5.
DR   UniGene; Mm.30251; -.
DR   ProteinModelPortal; Q8K5B2; -.
DR   SMR; Q8K5B2; 66-145.
DR   STRING; Q8K5B2; -.
DR   PhosphoSite; Q8K5B2; -.
DR   PRIDE; Q8K5B2; -.
DR   Ensembl; ENSMUST00000024963; ENSMUSP00000024963; ENSMUSG00000024150.
DR   GeneID; 193813; -.
DR   KEGG; mmu:193813; -.
DR   UCSC; uc008dur.1; mouse.
DR   CTD; 193813; -.
DR   MGI; MGI:2183439; Mcfd2.
DR   eggNOG; roNOG16339; -.
DR   HOGENOM; HBG717834; -.
DR   HOVERGEN; HBG060762; -.
DR   InParanoid; Q8K5B2; -.
DR   OMA; QDKDHIM; -.
DR   OrthoDB; EOG4640DK; -.
DR   PhylomeDB; Q8K5B2; -.
DR   NextBio; 371520; -.
DR   ArrayExpress; Q8K5B2; -.
DR   Bgee; Q8K5B2; -.
DR   CleanEx; MM_MCFD2; -.
DR   Genevestigator; Q8K5B2; -.
DR   GermOnline; ENSMUSG00000024150; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005793; C:ER-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   2: Evidence at transcript level;
KW   Calcium; Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus;
KW   Protein transport; Repeat; Signal; Transport.
FT   SIGNAL        1     26       Potential.
FT   CHAIN        27    145       Multiple coagulation factor deficiency
FT                                protein 2 homolog.
FT                                /FTId=PRO_0000004160.
FT   DOMAIN       67    102       EF-hand 1.
FT   DOMAIN      115    145       EF-hand 2.
FT   CA_BIND      80     91       1 (By similarity).
FT   CA_BIND     128    139       2 (By similarity).
SQ   SEQUENCE   145 AA;  16168 MW;  EB654BA9B76E0269 CRC64;
     MATLQLLRAP LLCVLLWVFC APGARAHDHG ADVHHGSVGL DKSTVHDQEH IMEHLEGVID
     QPEAEMSPQE LQLHYFKMHD YDGNSLLDGL ELSIAITHVH KEEGSEQAPV MSEDELVSII
     DGVLRDDDKN NDGYIDYAEF AKSLQ
//
ID   FLCN_MOUSE              Reviewed;         579 AA.
AC   Q8QZS3; Q3U4U8; Q3UFZ1; Q5SWZ2; Q5SX01; Q5SX02; Q8CAC0;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Folliculin;
GN   Name=Flcn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Adipose tissue, Egg, Hypothalamus, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May be a tumor suppressor. May be involved in energy
CC       and/or nutrient sensing through the AMPK and mTOR signaling
CC       pathways (By similarity).
CC   -!- SUBUNIT: Interacts (via C-terminus) with FNIP1 and FNIP2. This
CC       mediates indirect interaction with the PRKAA1, PRKAB1 and PRKAG1
CC       subunits of 5'-AMP-activated protein kinase (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the folliculin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC30240.1; Type=Frameshift; Positions=42;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK039106; BAC30240.1; ALT_FRAME; mRNA.
DR   EMBL; AK080933; BAC38084.1; -; mRNA.
DR   EMBL; AK136071; BAE22806.1; -; mRNA.
DR   EMBL; AK148216; BAE28418.1; -; mRNA.
DR   EMBL; AK154040; BAE32332.1; -; mRNA.
DR   EMBL; AL596204; CAI24295.1; -; Genomic_DNA.
DR   EMBL; AL596204; CAI24297.1; -; Genomic_DNA.
DR   EMBL; BC025820; AAH25820.1; -; mRNA.
DR   IPI; IPI00323161; -.
DR   RefSeq; NP_666130.1; NM_146018.1.
DR   UniGene; Mm.339640; -.
DR   STRING; Q8QZS3; -.
DR   PhosphoSite; Q8QZS3; -.
DR   PRIDE; Q8QZS3; -.
DR   Ensembl; ENSMUST00000091246; ENSMUSP00000091696; ENSMUSG00000032633.
DR   Ensembl; ENSMUST00000102697; ENSMUSP00000099758; ENSMUSG00000032633.
DR   GeneID; 216805; -.
DR   KEGG; mmu:216805; -.
DR   UCSC; uc007jew.1; mouse.
DR   CTD; 216805; -.
DR   MGI; MGI:2442184; Flcn.
DR   eggNOG; roNOG05748; -.
DR   GeneTree; ENSGT00390000009864; -.
DR   HOVERGEN; HBG081531; -.
DR   InParanoid; Q8QZS3; -.
DR   OMA; LLKFWMT; -.
DR   OrthoDB; EOG4P8FHW; -.
DR   PhylomeDB; Q8QZS3; -.
DR   NextBio; 375332; -.
DR   ArrayExpress; Q8QZS3; -.
DR   Bgee; Q8QZS3; -.
DR   CleanEx; MM_FLCN; -.
DR   Genevestigator; Q8QZS3; -.
DR   GermOnline; ENSMUSG00000032633; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR021713; Folliculin.
DR   Pfam; PF11704; Folliculin; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Phosphoprotein; Tumor suppressor.
FT   CHAIN         1    579       Folliculin.
FT                                /FTId=PRO_0000223941.
FT   COILED      287    310       Potential.
FT   MOD_RES      62     62       Phosphoserine.
FT   MOD_RES      73     73       Phosphoserine (By similarity).
FT   MOD_RES     302    302       Phosphoserine (By similarity).
FT   CONFLICT     29     29       L -> M (in Ref. 1; BAE28418).
FT   CONFLICT    240    240       S -> Y (in Ref. 1; BAE28418).
FT   CONFLICT    328    328       E -> G (in Ref. 1; BAE32332).
FT   CONFLICT    377    377       K -> R (in Ref. 1; BAC30240).
SQ   SEQUENCE   579 AA;  64327 MW;  DD20DB9F7AFAC81C CRC64;
     MNAIVALCHF CELHGPRTLF CTEVLHAPLP QGAGSGDSPD QVEQAEEEEG GIQMSSRVRA
     HSPAEGASSE SSSPGPKKSD MCEGCRSLAV GHPGYISHDK ETSIKYVSHQ HPNHPQLFSI
     VRQACVRSLS CEVCPGREGP IFFGDEQHGF VFSHTFFIKD SLARGFQRWY SIIAIMMDRI
     YLINSWPFLL GRIRGIISEL QAKAFKVFEA EQFGCPQRAQ RMNTAFTPFL HQRNGNAARS
     LTSLTSDDNL WACLHTSFAW LLKACGSRLT EKLLEGAPTE DTLVQMEKLA DLEEESESWD
     NSEAEEEEKA PVTPEGAEGR ELTSCPTESS FLSACGSWQP PKLTGFKSLR HMRQVLGAPS
     FRMLAWHVLM GNQVIWKSRD VNLVHSAFEV LRTMLPVGCV RIIPYSSQYE EAYRCNFLGL
     SPPVPIPAHV LASEFVVVVE VHTATRSNLH PAGCEDDQSL SKYEFVVTSG SPVAADRVGP
     TILNKIEAAL TNQNLSVDVV DQCLICLKEE WMNKVKVLFK FTKVDSRPKE DTQKLLSVLG
     ASEEDNVKLL KFWMTGLSKT YKSHLMSTVR SPTATESRS
//
ID   CA096_MOUSE             Reviewed;         252 AA.
AC   Q8QZT2; Q8C3E1;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Uncharacterized protein C1orf96 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC39624.1; Type=Frameshift; Positions=185;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK086180; BAC39624.1; ALT_FRAME; mRNA.
DR   EMBL; BC024705; AAH24705.1; -; mRNA.
DR   EMBL; BC036300; AAH36300.1; -; mRNA.
DR   IPI; IPI00187478; -.
DR   RefSeq; NP_082812.1; NM_028536.1.
DR   UniGene; Mm.157746; -.
DR   ProteinModelPortal; Q8QZT2; -.
DR   PhosphoSite; Q8QZT2; -.
DR   PRIDE; Q8QZT2; -.
DR   Ensembl; ENSMUST00000034452; ENSMUSP00000034452; ENSMUSG00000031971.
DR   Ensembl; ENSMUST00000122421; ENSMUSP00000113319; ENSMUSG00000031971.
DR   GeneID; 73420; -.
DR   KEGG; mmu:73420; -.
DR   UCSC; uc009nwp.1; mouse.
DR   MGI; MGI:1920670; 1700054N08Rik.
DR   eggNOG; roNOG15803; -.
DR   GeneTree; ENSGT00390000003512; -.
DR   HOGENOM; HBG715674; -.
DR   HOVERGEN; HBG100745; -.
DR   InParanoid; Q8QZT2; -.
DR   OMA; YGPCYRE; -.
DR   OrthoDB; EOG44J2K3; -.
DR   PhylomeDB; Q8QZT2; -.
DR   NextBio; 338220; -.
DR   ArrayExpress; Q8QZT2; -.
DR   Bgee; Q8QZT2; -.
DR   CleanEx; MM_1700054N08RIK; -.
DR   Genevestigator; Q8QZT2; -.
PE   2: Evidence at transcript level;
FT   CHAIN         1    252       Uncharacterized protein C1orf96 homolog.
FT                                /FTId=PRO_0000284644.
FT   CONFLICT    129    129       S -> I (in Ref. 1; BAC39624).
FT   CONFLICT    175    175       Q -> K (in Ref. 1; BAC39624).
SQ   SEQUENCE   252 AA;  28379 MW;  0392B8050ECFBE6C CRC64;
     MSPGSGVKSE YMKRYREPRW DEYAPCYREL LRYRLGRRLL EQAHAPWLWD AWGPDSPSDS
     SASPSPAPRG ALGEPSAPSA REEEQPVGER GAELRDAEEQ DTVLPAPPKK DTEEKPEEHK
     TKETDGAPSG PGPRQQPSAL CARGSKKATR SPQRSTSKIK ENKHPFALYG WGERQMDMGS
     QKTHNVCASA SVHEIHESAL RAKNRRQVEK RKLAAQRQRA HSVDVEKNQR VKPASAENPW
     LTEYMRCYSA RA
//
ID   ST32C_MOUSE             Reviewed;         488 AA.
AC   Q8QZV4; Q9JJG4;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Serine/threonine-protein kinase 32C;
DE            EC=2.7.11.1;
GN   Name=Stk32c; Synonyms=Pkek; ORFNames=MNCb-1563;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S.,
RA   Hashimoto K.;
RT   "Isolation of full-length cDNA clones from mouse brain cDNA library
RT   made by oligo-capping method.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB041542; BAA95027.1; -; mRNA.
DR   EMBL; AK046439; BAC32730.1; -; mRNA.
DR   EMBL; BC026457; AAH26457.1; -; mRNA.
DR   IPI; IPI00323182; -.
DR   RefSeq; NP_001156012.1; NM_001162540.1.
DR   RefSeq; NP_067277.2; NM_021302.3.
DR   UniGene; Mm.478434; -.
DR   ProteinModelPortal; Q8QZV4; -.
DR   SMR; Q8QZV4; 86-376.
DR   PhosphoSite; Q8QZV4; -.
DR   PRIDE; Q8QZV4; -.
DR   Ensembl; ENSMUST00000016125; ENSMUSP00000016125; ENSMUSG00000015981.
DR   GeneID; 57740; -.
DR   KEGG; mmu:57740; -.
DR   UCSC; uc009kfl.1; mouse.
DR   CTD; 57740; -.
DR   MGI; MGI:2385336; Stk32c.
DR   eggNOG; roNOG15179; -.
DR   GeneTree; ENSGT00600000084135; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG106458; -.
DR   InParanoid; Q8QZV4; -.
DR   OMA; EKRVEPG; -.
DR   OrthoDB; EOG4DV5MD; -.
DR   PhylomeDB; Q8QZV4; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 313863; -.
DR   ArrayExpress; Q8QZV4; -.
DR   Bgee; Q8QZV4; -.
DR   CleanEx; MM_STK32C; -.
DR   Genevestigator; Q8QZV4; -.
DR   GermOnline; ENSMUSG00000015981; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    488       Serine/threonine-protein kinase 32C.
FT                                /FTId=PRO_0000232416.
FT   DOMAIN       94    354       Protein kinase.
FT   NP_BIND     100    108       ATP (By similarity).
FT   COMPBIAS    398    401       Poly-Lys.
FT   ACT_SITE    217    217       Proton acceptor (By similarity).
FT   BINDING     123    123       ATP (By similarity).
FT   MOD_RES      11     11       Phosphoserine (By similarity).
FT   MOD_RES      18     18       Phosphoserine (By similarity).
FT   CONFLICT     30     30       D -> E (in Ref. 1; BAA95027).
SQ   SEQUENCE   488 AA;  55263 MW;  2B6A927BE6B78EF2 CRC64;
     MRSGAERRGS SAAAPPSSPP PGRARPAGSD VSPALPPPAA SQPRARDAGD ARAQPRPLFQ
     WSKWKKRMSM SSISSGSARR PVFDDKEDVN FDHFQILRAI GKGSFGKVCI VQKRDTEKMY
     AMKYMNKQQC IERDEVRNVF RELEILQEIE HVFLVNLWYS FQDEEDMFMV VDLLLGGDLR
     YHLQQNVQFS EDTVRLYICE MALALDYLRS QHIIHRDVKP DNILLDEQGH AHLTDFNIAT
     IIKDGERATA LAGTKPYMAP EIFHSFVNGG TGYSFEVDWW SVGVMAYELL RGWRPYDIHS
     SNAVESLVQL FSTVSVQYVP TWSKEMVALL RKLLTVNPEH RFSSLQDMQT APSLAHVLWD
     DLSEKKVEPG FVPNKGRLHC DPTFELEEMI LESRPLHKKK KRLAKNKSRD SSRDSSQSEN
     DYLQDCLDAI QQDFVIFNRE KLKRSQELMS EPPPGPETSD MTDSTADSEA EPTALPMCGS
     ICPSSGSS
//
ID   Q8QZV8_MOUSE            Unreviewed;      2429 AA.
AC   Q8QZV8;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   SubName: Full=CREB-binding protein;
DE   Flags: Fragment;
GN   Name=Crebbp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ILS, and ISS;
RX   MEDLINE=21363810; PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ILS, and ISS;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AY079443; AAL87531.1; -; Genomic_DNA.
DR   EMBL; AY079444; AAL87532.1; -; Genomic_DNA.
DR   IPI; IPI00463549; -.
DR   UniGene; Mm.132238; -.
DR   UniGene; Mm.392384; -.
DR   HSSP; P45481; 1L8C.
DR   ProteinModelPortal; Q8QZV8; -.
DR   STRING; Q8QZV8; -.
DR   PRIDE; Q8QZV8; -.
DR   Ensembl; ENSMUST00000023165; ENSMUSP00000023165; ENSMUSG00000022521.
DR   UCSC; uc007xzl.1; mouse.
DR   MGI; MGI:1098280; Crebbp.
DR   GeneTree; ENSGT00550000074306; -.
DR   HOGENOM; HBG402903; -.
DR   HOVERGEN; HBG000185; -.
DR   InParanoid; Q8QZV8; -.
DR   ArrayExpress; Q8QZV8; -.
DR   Bgee; Q8QZV8; -.
DR   Genevestigator; Q8QZV8; -.
DR   GO; GO:0000940; C:condensed chromosome outer kinetochore; IDA:MGI.
DR   GO; GO:0000123; C:histone acetyltransferase complex; IDA:MGI.
DR   GO; GO:0005667; C:transcription factor complex; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030718; P:germ-line stem cell maintenance; IMP:MGI.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR010303; DUF902_CREBbp.
DR   InterPro; IPR013178; Histone_H3-K56_AcTrfase_RTT109.
DR   InterPro; IPR003101; KIX.
DR   InterPro; IPR009110; Nuc_rcpt_coact.
DR   InterPro; IPR014744; Nuc_rcpt_coact_CREBbp.
DR   InterPro; IPR000197; Znf_TAZ.
DR   InterPro; IPR000433; Znf_ZZ.
DR   Gene3D; G3DSA:1.20.920.10; Bromodomain; 1.
DR   Gene3D; G3DSA:1.10.246.20; KIX; 1.
DR   Gene3D; G3DSA:1.10.1630.10; Nuc_rcpt_coact_CREBbp; 1.
DR   Gene3D; G3DSA:1.20.1020.10; Znf_TAZ; 2.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF09030; Creb_binding; 1.
DR   Pfam; PF06001; DUF902; 1.
DR   Pfam; PF08214; KAT11; 1.
DR   Pfam; PF02172; KIX; 1.
DR   Pfam; PF02135; zf-TAZ; 2.
DR   Pfam; PF00569; ZZ; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00551; ZnF_TAZ; 2.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF47040; KIX; 1.
DR   SUPFAM; SSF69125; Nuc_recept_coact; 1.
DR   SUPFAM; SSF57933; TAZ_finger; 2.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS50952; KIX; 1.
DR   PROSITE; PS50134; ZF_TAZ; 2.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   2: Evidence at transcript level;
KW   Bromodomain.
FT   NON_TER       1      1
FT   NON_TER    2429   2429
SQ   SEQUENCE   2429 AA;  264222 MW;  F1D2D84C23B51835 CRC64;
     DGPPNPKRAK LSSPGFSAND NTDFGSLFDL ENDLPDELIP NGELSLLNSG NLVPDAASKH
     KQLSELLRGG SGSSINPGIG NVSASSPVQQ GLGGQAQGQP NSTNMASLGA MGKSPLNQGD
     SSTPNLPKQA ASTSGPTPPA SQALNPQAQK QVGLVTSSPA TSQTGPGICM NANFNQTHPG
     LLNSNSGHSL MNQAQQGQAQ VMNGSLGAAG RGRGAGMPYP APAMQGATSS VLAETLTQVS
     PQMAGHAGLN TAQAGGMTKM GMTGTTSPFG QPFSQTGGQQ MGATGVNPQL ASKQSMVNSL
     PAFPTDIKNT SVTTVPNMSQ LQTSVGIVPT QAIATGPTAD PEKRKLIQQQ LVLLLHAHKC
     QRREQANGEV RACSLPHCRT MKNVLNHMTH CQAGKACQVA HCASSRQIIS HWKNCTRHDC
     PVCLPLKNAS DKRNQQTILG SPASGIQNTI GSVGAGQQNA TSLSNPNPID PSSMQRAYAA
     LGLPYMNQPQ TQLQPQVPGQ QPAQPPAHQQ MRTLNALGNN PMSIPAGGIT TDQQPPNLIS
     ESALPTSLGA TNPLMNDGSN SGNIGSLSTI PTAAPPSSTG VRKGWHEHVT QDLRSHLVHK
     LVQAIFPTPD PAALKDRRME NLVAYAKKVE GDMYESANSR DEYYHLLAEK IYKIQKELEE
     KRRSRLHKQG ILGNQPALPA SGAQPPVIPP AQSVRPPNGP LPLPVNRMQV SQGMNSFNPM
     SLGNVQLPQA PMGPRAASPM NHSVQMNSMA SVPGMAISPS RMPQPPNMMG THANNIMAQA
     PTQNQFLPQN QFPSSSGAMS VNSVGMGQPA AQAGVSQGQV PGAALPNPLN MLAPQASQLP
     CPPVTQSPLH PTPPPASTAA GMPSLQHPTA PGMTPPQPAA PTQPSTPVSS GQTPTPTPGS
     VPSAAQTQST PTVQAAAQAQ VTPQPQTPVQ PPSVATPQSS QQQPTPVHTQ PPGTPLSQAA
     ASIDNRVPTP SSVTSAETSS QQPGPDVPML EMKTEVQTDD AEPEPTESKG EPRSEMMEED
     LQGSSQVKEE TDTTEQKSEP MEVEEKKPEV KVEAKEEEEN SSNDTASQST SPSQPRKKIF
     KPEELRQALM PTLEALYRQD PESLPFRQPV DPQLLGIPDY FDIVKNPMDL STIKRKLDTG
     QYQEPWQYVD DVWLMFNNAW LYNRKTSRVY KFCSKLAEVF EQEIDPVMQS LGYCCGRKYE
     FSPQTLCCYG KQLCTIPRDA AYYSYQNRYH FCEKCFTEIQ GENVTLGDDP SQPQTTISKD
     QFEKKKNDTL DPEPFVDCKE CGRKMHQICV LHYDIIWPSG FVCDNCLKKT GRPRKENKFS
     AKRLQTTRLG NHLEDRVNKF LRRQNHPEAG EVFVRVVASS DKTVEVKPGM KSRFVDSGEM
     SESFPYRTKA LFAFEEIDGV DVCFFGMHVQ EYGSDCPPPN TRRVYISYLD SIHFFRPRCL
     RTAVYHEILI GYLEYVKKLG YVTGHIWACP PSEGDDYIFH CHPPDQKIPK PKRLQEWYKK
     MLDKAFAERI INDYKDIFKQ ANEDRLTSAK ELPYFEGDFW PNVLEESIKE LEQEEEERKK
     EESTAASETP EGSQGDSKNA KKKNNKKTNK NKSSISRANK KKPSMPNVSN DLSQKLYATM
     EKHKEVFFVI HLHAGPVIST QPPIVDPDPL LSCDLMDGRD AFLTLARDKH WEFSSLRRSK
     WSTLCMLVEL HTQGQDRFVY TCNECKHHVE TRWHCTVCED YDLCINCYNT KSHTHKMVKW
     GLGLDDEGSS QGEPQSKSPQ ESRRLSIQRC IQSLVHACQC RNANCSLPSC QKMKRVVQHT
     KGCKRKTNGG CPVCKQLIAL CCYHAKHCQE NKCPVPFCLN IKHKLRQQQI QHRLQQAQLM
     RRRMATMNTR NVPQQSLPSP TSAPPGTPTQ QPSTPQTPQP PAQPQPSPVN MSPAGFPNVA
     RTQPPTIVSA GKPTNQVPAP PPPAQPPPAA VEAARQIERE AQQQQHLYRA NINNGMPPGR
     AGMGTPGSQM TPVGLNVPRP NQVSGPVMSS MPPGQWQQAP IPQQQPMPGM PRPVMSMQAQ
     AAVAGPRMPN VQPPRSISPS ALQDLLRTLK SPSSPQQQQQ VLNILKSNPQ LMAAFIKQRT
     AKYVANQPGM QPQPGLQSQP GMQPQPGMHQ QPSLQNLNAM QAGVPRPGVP PPQPAMGGLN
     PQGQALNIMN PGHNPNMTNM NPQYREMVRR QLLQHQQQQQ QQQQQQQQQQ NSASLAGGMA
     GHSQFQQPQG PGGYAPAMQQ QRMQQHLPIQ GSSMGQMAAP MGQLGQMGQP GLGADSTPNI
     QQALQQRILQ QQQMKQQIGS PGQPNPMSPQ QHMLSGQPQA SHLPGQQIAT SLSNQVRSPA
     PVQSPRPQSQ PPHSSPSPRI QPQPSPHHVS PQTGSPHPGL AVTMASSMDQ GHLGNPEQSA
     MLPQLNTPNR SALSSELSLV GDTTGDTLE
//
ID   MARE2_MOUSE             Reviewed;         326 AA.
AC   Q8R001; Q3UF61; Q8BLZ6; Q8BYR6; Q8C177; Q8K109;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Microtubule-associated protein RP/EB family member 2;
DE   AltName: Full=APC-binding protein EB2;
DE   AltName: Full=End-binding protein 2;
DE            Short=EB2;
GN   Name=Mapre2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Aorta, Corpora quadrigemina, Hypothalamus, Skin,
RC   Sympathetic ganglion, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Eye, and Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-166, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
CC   -!- FUNCTION: May be involved in microtubule polymerization, and
CC       spindle function by stabilizing microtubules and anchoring them at
CC       centrosomes. May play a role in cell migration (By similarity).
CC   -!- SUBUNIT: Interacts with DCTN1. Binds to the C-terminal domain of
CC       APC. Binds monomeric and polymerized tubulin (By similarity).
CC   -!- INTERACTION:
CC       Q9QWI6-2:Srcin1; NbExp=1; IntAct=EBI-774541, EBI-775607;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity). Note=Associated with the microtubule
CC       network. Accumulates at the plus end of microtubules (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R001-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R001-2; Sequence=VSP_012946;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: Composed of two functionally independent domains. The N-
CC       terminal domain forms an hydrophobic cleft involved in microtubule
CC       binding and the C-terminal is involved in the formation of
CC       mutually exclusive complexes with APC and DCTN1 (By similarity).
CC   -!- SIMILARITY: Belongs to the MAPRE family.
CC   -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC   -!- SIMILARITY: Contains 1 EB1 C-terminal domain.
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DR   EMBL; AK028823; BAC26138.1; -; mRNA.
DR   EMBL; AK038562; BAC30045.1; -; mRNA.
DR   EMBL; AK040767; BAC30700.1; -; mRNA.
DR   EMBL; AK045493; BAC32393.1; -; mRNA.
DR   EMBL; AK045904; BAE43326.1; -; mRNA.
DR   EMBL; AK046221; BAC32643.1; -; mRNA.
DR   EMBL; AK148954; BAE28700.1; -; mRNA.
DR   EMBL; BC025804; AAH25804.1; -; mRNA.
DR   EMBL; BC027056; AAH27056.1; -; mRNA.
DR   EMBL; BC028987; AAH28987.1; -; mRNA.
DR   EMBL; BC035254; AAH35254.1; -; mRNA.
DR   IPI; IPI00403682; -.
DR   IPI; IPI00474073; -.
DR   RefSeq; NP_001156413.1; NM_001162941.1.
DR   RefSeq; NP_001156414.1; NM_001162942.1.
DR   RefSeq; NP_694698.3; NM_153058.4.
DR   UniGene; Mm.132237; -.
DR   ProteinModelPortal; Q8R001; -.
DR   SMR; Q8R001; 43-172, 245-301.
DR   IntAct; Q8R001; 2.
DR   STRING; Q8R001; -.
DR   PhosphoSite; Q8R001; -.
DR   PRIDE; Q8R001; -.
DR   Ensembl; ENSMUST00000025127; ENSMUSP00000025127; ENSMUSG00000024277.
DR   GeneID; 212307; -.
DR   KEGG; mmu:212307; -.
DR   UCSC; uc008ege.1; mouse.
DR   UCSC; uc008egf.1; mouse.
DR   CTD; 212307; -.
DR   MGI; MGI:106271; Mapre2.
DR   GeneTree; ENSGT00490000043329; -.
DR   HOGENOM; HBG622485; -.
DR   HOVERGEN; HBG052410; -.
DR   InParanoid; Q8R001; -.
DR   OMA; REVELLC; -.
DR   OrthoDB; EOG4ZGPCX; -.
DR   PhylomeDB; Q8R001; -.
DR   NextBio; 373531; -.
DR   ArrayExpress; Q8R001; -.
DR   Bgee; Q8R001; -.
DR   Genevestigator; Q8R001; -.
DR   GermOnline; ENSMUSG00000024277; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR004953; EB1_C.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF03271; EB1; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS51230; EB1_C; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell cycle; Cell division;
KW   Cytoplasm; Cytoskeleton; Microtubule; Mitosis; Phosphoprotein.
FT   CHAIN         1    326       Microtubule-associated protein RP/EB
FT                                family member 2.
FT                                /FTId=PRO_0000213425.
FT   DOMAIN       56    158       CH.
FT   DOMAIN      235    305       EB1 C-terminal.
FT   REGION      186    326       DCTN1-binding (By similarity).
FT   REGION      258    301       APC-binding (By similarity).
FT   MOD_RES       9      9       Phosphoserine (By similarity).
FT   MOD_RES     166    166       Phosphotyrosine.
FT   MOD_RES     199    199       Phosphoserine (By similarity).
FT   MOD_RES     207    207       Phosphoserine (By similarity).
FT   MOD_RES     218    218       Phosphoserine (By similarity).
FT   MOD_RES     222    222       Phosphoserine (By similarity).
FT   MOD_RES     270    270       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1     40       MPGPTQTLSPNGENNNDIIQDNGTIIPFRKHTVRGERSYS
FT                                -> MKQIRDQRVIRKGPQKHHSLQQPGRVPGCSN (in
FT                                isoform 2).
FT                                /FTId=VSP_012946.
FT   CONFLICT    103    103       V -> E (in Ref. 1; BAC30045).
FT   CONFLICT    251    251       H -> Y (in Ref. 2; AAH35254/AAH28987).
FT   CONFLICT    319    319       Q -> H (in Ref. 1; BAC30700).
SQ   SEQUENCE   326 AA;  36946 MW;  51C0916F37075651 CRC64;
     MPGPTQTLSP NGENNNDIIQ DNGTIIPFRK HTVRGERSYS WGMAVNVYST SITQETMSRH
     DIIAWVNDIV SLNYTKVEQL CSGAAYCQFM DMLFPGCISL KKVKFQAKLE HEYIHNFKLL
     QASFKRMNVD KVIPVEKLVK GRFQDNLDFI QWFKKFYDAN YDGKEYDPVE ARQGQDAIPP
     PDPGEQIFNL PKKSHHANSP TAGAAKSSPA SKPGSTPSRP SSAKRASSSG SASRSDKDLE
     TQVIQLNEQV HSLKLALEGV EKERDFYFGK LREIELLCQE HGQENDDLVQ RLMEVLYASD
     EQEGQTEEPE AEEQAHDQQP QQQEEY
//
ID   IP3KA_MOUSE             Reviewed;         459 AA.
AC   Q8R071; A2AQ20;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Inositol-trisphosphate 3-kinase A;
DE            EC=2.7.1.127;
DE   AltName: Full=Inositol 1,4,5-trisphosphate 3-kinase A;
DE            Short=IP3 3-kinase A;
DE            Short=IP3K A;
DE            Short=InsP 3-kinase A;
GN   Name=Itpka;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 1,4,5-trisphosphate =
CC       ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate.
CC   -!- ENZYME REGULATION: IP3K is activated by calmodulin (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the inositol phosphokinase (IPK) family.
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DR   EMBL; AL844536; CAM18079.1; -; Genomic_DNA.
DR   EMBL; BC027291; AAH27291.1; -; mRNA.
DR   IPI; IPI00153136; -.
DR   RefSeq; NP_666237.1; NM_146125.2.
DR   UniGene; Mm.65337; -.
DR   ProteinModelPortal; Q8R071; -.
DR   SMR; Q8R071; 171-459.
DR   STRING; Q8R071; -.
DR   PhosphoSite; Q8R071; -.
DR   PRIDE; Q8R071; -.
DR   Ensembl; ENSMUST00000028758; ENSMUSP00000028758; ENSMUSG00000027296.
DR   GeneID; 228550; -.
DR   KEGG; mmu:228550; -.
DR   UCSC; uc008luf.1; mouse.
DR   CTD; 228550; -.
DR   MGI; MGI:1333822; Itpka.
DR   GeneTree; ENSGT00390000017438; -.
DR   HOGENOM; HBG314443; -.
DR   HOVERGEN; HBG052138; -.
DR   InParanoid; Q8R071; -.
DR   OMA; PCSPGLE; -.
DR   OrthoDB; EOG40S0FV; -.
DR   PhylomeDB; Q8R071; -.
DR   BRENDA; 2.7.1.127; 244.
DR   NextBio; 379032; -.
DR   ArrayExpress; Q8R071; -.
DR   Bgee; Q8R071; -.
DR   CleanEx; MM_ITPKA; -.
DR   Genevestigator; Q8R071; -.
DR   GermOnline; ENSMUSG00000027296; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0008440; F:inositol trisphosphate 3-kinase activity; IEA:EC.
DR   GO; GO:0006020; P:inositol metabolic process; IMP:MGI.
DR   InterPro; IPR005522; IPK.
DR   PANTHER; PTHR12400; IPK; 1.
DR   Pfam; PF03770; IPK; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Calmodulin-binding; Kinase; Nucleotide-binding;
KW   Transferase.
FT   CHAIN         1    459       Inositol-trisphosphate 3-kinase A.
FT                                /FTId=PRO_0000066866.
FT   NP_BIND     247    249       ATP (By similarity).
FT   REGION      285    293       Calmodulin-binding (By similarity).
FT   REGION      310    317       Substrate binding (By similarity).
FT   BINDING     195    195       ATP (By similarity).
FT   BINDING     207    207       ATP (By similarity).
FT   BINDING     260    260       ATP (By similarity).
FT   BINDING     262    262       Substrate (By similarity).
FT   BINDING     283    283       Substrate (By similarity).
FT   BINDING     334    334       ATP (By similarity).
FT   BINDING     414    414       ATP (By similarity).
FT   BINDING     417    417       Substrate (By similarity).
SQ   SEQUENCE   459 AA;  50935 MW;  3CDA79DD267A1A5D CRC64;
     MTLPGRPTGM ARPRGAGPCS PGLERAPRRS VGELRLLFEA RCAAVAAAAA AGEPRARGAK
     RRGGQVPNGL PRAAPAPVIP QLTVTSEEDV TPASPGPPDQ EGNWLPAAGS HLQQPRRLST
     SSLSSTGSSS LLEDSEDDLL SDSESRSRGN VQLETSEDVG QKSHWQKIRT MVNLPVMSPF
     RKRYSWVQLA GHTGSFKAAG TSGLILKRSS EPEHYCLVRL MADVLRGCVP AFHGIVERDG
     ESYLQLQDLL DGFDGPCVLD CKMGVRTYLE EELTKARERP KLRKDMYKKM LAVDPEAPTE
     EEHAQRAVTK PRYMQWREGI SSSTTLGFRI EGIKKADGSC STDFKTTRSR EQVTRVFEEF
     MQGDAEVLRR YLNRLQQIRD TLEISDFFRR HEVIGSSLLF VHDHCHRAGV WLIDFGKTTP
     LPDGQILDHR RPWEEGNRED GYLLGLDNLI GILASLAER
//
ID   HNRPL_MOUSE             Reviewed;         586 AA.
AC   Q8R081; O54789; Q499X2; Q8K0S7;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Heterogeneous nuclear ribonucleoprotein L;
DE            Short=hnRNP L;
GN   Name=Hnrnpl; Synonyms=Hnrpl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 388-586.
RA   Sakai N., Saitou Y., Toyota T.;
RT   "Mouse ribonucleoprotein.";
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 396-408 AND 566-576.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
CC   -!- FUNCTION: This protein is a component of the heterogeneous nuclear
CC       ribonucleoprotein (hnRNP) complexes which provide the substrate
CC       for the processing events that pre-mRNAs undergo before becoming
CC       functional, translatable mRNAs in the cytoplasm. L is associated
CC       with most nascent transcripts including those of the landmark
CC       giant loops of amphibian lampbrush chromosomes. Associates,
CC       together with APEX1, to the negative calcium responsive element
CC       (nCaRE) B2 of the APEX2 promoter (By similarity).
CC   -!- SUBUNIT: Identified in a mRNP granule complex, at least composed
CC       of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD,
CC       HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1,
CC       NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8,
CC       RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with
CC       HNRPLL. Interacts with APEX1; the interaction is DNA-dependent (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm (By similarity).
CC       Cytoplasm (By similarity). Note=Localized in cytoplasmic mRNP
CC       granules containing untranslated mRNAs.
CC   -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH27206.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC   -----------------------------------------------------------------------
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DR   EMBL; BC027206; AAH27206.1; ALT_INIT; mRNA.
DR   EMBL; BC030461; AAH30461.1; -; mRNA.
DR   EMBL; BC099683; AAH99683.1; -; mRNA.
DR   EMBL; AB009392; BAA24237.1; -; mRNA.
DR   IPI; IPI00620362; -.
DR   RefSeq; NP_796275.3; NM_177301.5.
DR   UniGene; Mm.9043; -.
DR   ProteinModelPortal; Q8R081; -.
DR   SMR; Q8R081; 93-287, 375-583.
DR   IntAct; Q8R081; 2.
DR   STRING; Q8R081; -.
DR   PhosphoSite; Q8R081; -.
DR   REPRODUCTION-2DPAGE; Q8R081; -.
DR   PRIDE; Q8R081; -.
DR   Ensembl; ENSMUST00000038572; ENSMUSP00000049407; ENSMUSG00000015165.
DR   GeneID; 15388; -.
DR   KEGG; mmu:15388; -.
DR   UCSC; uc009fzz.1; mouse.
DR   CTD; 15388; -.
DR   MGI; MGI:104816; Hnrnpl.
DR   eggNOG; roNOG05038; -.
DR   HOVERGEN; HBG105786; -.
DR   OrthoDB; EOG4RFKSD; -.
DR   ArrayExpress; Q8R081; -.
DR   Bgee; Q8R081; -.
DR   CleanEx; MM_HNRNPL; -.
DR   Genevestigator; Q8R081; -.
DR   GermOnline; ENSMUSG00000015165; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045120; C:pronucleus; IDA:MGI.
DR   GO; GO:0030529; C:ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0010843; F:promoter binding; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR   InterPro; IPR006536; HnRNP-L_PTB.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 4.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 3.
DR   TIGRFAMs; TIGR01649; hnRNP-L_PTB; 1.
DR   PROSITE; PS50102; RRM; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Nucleus;
KW   Phosphoprotein; Repeat; Ribonucleoprotein; RNA-binding.
FT   CHAIN         1    586       Heterogeneous nuclear ribonucleoprotein
FT                                L.
FT                                /FTId=PRO_0000081863.
FT   DOMAIN       99    173       RRM 1.
FT   DOMAIN      190    267       RRM 2.
FT   DOMAIN      379    453       RRM 3.
FT   COMPBIAS     39     86       Gly-rich.
FT   COMPBIAS    332    379       Pro-rich.
FT   MOD_RES     266    266       N6-acetyllysine (By similarity).
FT   MOD_RES     295    295       Phosphoserine (By similarity).
FT   MOD_RES     472    472       N6-acetyllysine (By similarity).
FT   MOD_RES     549    549       N6-acetyllysine (By similarity).
FT   CONFLICT    388    388       Q -> E (in Ref. 2; BAA24237).
SQ   SEQUENCE   586 AA;  63964 MW;  BB56D3D6A8553F7E CRC64;
     MSRRLLPRAE KRRRRLEQRQ QPDEQLRRAG AMVKMAAAGG GGGGGRYYGG GNEGGRAPKR
     LKTENAGDQH GGGGGGGSGA AGGGGGENYD DPHKTPASPV VHIRGLIDGV VEADLVEALQ
     EFGPISYVVV MPKKRQALVE FEDVLGACNA VNYAADNQIY IAGHPAFVNY STSQKISRPG
     DSDDSRSVNS VLLFTILNPI YSITTDVLYT ICNPCGPVQR IVIFRKNGVQ AMVEFDSVQS
     AQRAKASLNG ADIYSGCCTL KIEYAKPTRL NVFKNDQDTW DYTNPNLSGQ GDPGSNPNKR
     QRQPPLLGDH PAEYGGPHGG YHSHYHDEGY GPPPPHYEGR RMGPPVGGHR RGPSRYGPQY
     GHPPPPPPPP DYGPHADSPV LMVYGLDQSK MNCDRVFNVF CLYGNVEKVK FMKSKPGAAM
     VEMADGYAVD RAITHLNNNF MFGQKMNVCV SKQPAIMPGQ SYGLEDGSCS YKDFSESRNN
     RFSTPEQAAK NRIQHPSNVL HFFNAPLEVT EENFFEICDE LGVKRPTSVK VFSGKSERSS
     SGLLEWDSKS DALETLGFLN HYQMKNPNGP YPYTLKLCFS TAQHAS
//
ID   ZBT44_MOUSE             Reviewed;         453 AA.
AC   Q8R0A2; Q8CB31;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Zinc finger and BTB domain-containing protein 44;
DE   AltName: Full=BTB/POZ domain-containing protein 15;
GN   Name=Zbtb44; Synonyms=Btbd15;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 287-453 (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND SER-194, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R0A2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R0A2-2; Sequence=VSP_022838;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC   -!- SIMILARITY: Contains 2 C2H2-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC29628.1; Type=Erroneous termination; Positions=348; Note=Translated as Glu;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK036895; BAC29628.1; ALT_SEQ; mRNA.
DR   EMBL; CT025653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BG243783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00467660; -.
DR   IPI; IPI00828437; -.
DR   RefSeq; NP_001108602.1; NM_001115130.1.
DR   RefSeq; NP_766353.2; NM_172765.3.
DR   UniGene; Mm.239355; -.
DR   UniGene; Mm.393131; -.
DR   HSSP; P41182; 1R29.
DR   ProteinModelPortal; Q8R0A2; -.
DR   SMR; Q8R0A2; 7-125, 341-450.
DR   PhosphoSite; Q8R0A2; -.
DR   PRIDE; Q8R0A2; -.
DR   Ensembl; ENSMUST00000061588; ENSMUSP00000062681; ENSMUSG00000047412.
DR   Ensembl; ENSMUST00000115222; ENSMUSP00000110877; ENSMUSG00000047412.
DR   GeneID; 235132; -.
DR   KEGG; mmu:235132; -.
DR   CTD; 235132; -.
DR   MGI; MGI:1925123; Zbtb44.
DR   eggNOG; roNOG11828; -.
DR   GeneTree; ENSGT00600000084004; -.
DR   HOGENOM; HBG446409; -.
DR   HOVERGEN; HBG061797; -.
DR   InParanoid; Q8R0A2; -.
DR   OrthoDB; EOG47SSDJ; -.
DR   PhylomeDB; Q8R0A2; -.
DR   NextBio; 382520; -.
DR   ArrayExpress; Q8R0A2; -.
DR   Bgee; Q8R0A2; -.
DR   CleanEx; MM_ZBTB44; -.
DR   Genevestigator; Q8R0A2; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR013069; BTB_POZ.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 2.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW   Phosphoprotein; Repeat; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    453       Zinc finger and BTB domain-containing
FT                                protein 44.
FT                                /FTId=PRO_0000274609.
FT   DOMAIN       31     98       BTB.
FT   ZN_FING     399    421       C2H2-type 1.
FT   ZN_FING     427    449       C2H2-type 2.
FT   COMPBIAS      9     14       Poly-Ser.
FT   COMPBIAS    364    367       Poly-Asp.
FT   MOD_RES     135    135       Phosphoserine (By similarity).
FT   MOD_RES     161    161       Phosphoserine (By similarity).
FT   MOD_RES     191    191       Phosphoserine.
FT   MOD_RES     194    194       Phosphoserine.
FT   VAR_SEQ     368    385       Missing (in isoform 2).
FT                                /FTId=VSP_022838.
SQ   SEQUENCE   453 AA;  50175 MW;  314AEAFFD1F9AC9C CRC64;
     MGVKTFTHSS SSHSQEMLGK LNMLRNDGHF CDITIRVQDK IFRAHKVVLA ACSDFFRTKL
     VGQTEDENKN VLDLHHVTVT GFIPLLEYAY TATLSINTEN IIDVLAAASY MQMFSVASTC
     SEFMKSSILW NTPNSQPEKS LDAGQENSSN CNFTSRDGSI SPVSSECSAV ERTIPVCRES
     RRKRKSYIVM SPESPVKCST QTSSPQVLNS SASYAENRSQ PVDSSLAFPW TFPFGIDRRI
     QPEKAKQAEN TRTLELPGPS EAGRRVADYV TCESTKPTLP LGTEEDVRVK VERLSDEEVH
     EEVSQPVSAS QSSLSDQQTV PGSEPVQEDL LISPQSSSIG SVDEGVTEGL PTLQSTSSTN
     AHADDDDRLE NVQYPYQLYI APSTSSTERP SPNGPDRPFQ CPTCGVRFTR IQNLKQHMLI
     HSGIKPFQCD CCGKKFTRAY SLKMHRLKHE VIS
//
ID   TCAL3_MOUSE             Reviewed;         200 AA.
AC   Q8R0A5; A2AEC3; Q9CYK5; Q9D1S4;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Transcription elongation factor A protein-like 3;
DE            Short=TCEA-like protein 3;
DE   AltName: Full=Transcription elongation factor S-II protein-like 3;
GN   Name=Tceal3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- SIMILARITY: Belongs to the TFS-II family. TFA subfamily.
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DR   EMBL; AK003156; BAB22610.1; -; mRNA.
DR   EMBL; AK017585; BAB30822.1; -; mRNA.
DR   EMBL; AK158996; BAE34762.1; -; mRNA.
DR   EMBL; AL671887; CAM17212.1; -; Genomic_DNA.
DR   EMBL; BC027131; AAH27131.1; -; mRNA.
DR   IPI; IPI00757153; -.
DR   RefSeq; NP_001025149.2; NM_001029978.2.
DR   UniGene; Mm.260515; -.
DR   ProteinModelPortal; Q8R0A5; -.
DR   PhosphoSite; Q8R0A5; -.
DR   PRIDE; Q8R0A5; -.
DR   Ensembl; ENSMUST00000060904; ENSMUSP00000059401; ENSMUSG00000044550.
DR   Ensembl; ENSMUST00000113100; ENSMUSP00000108724; ENSMUSG00000044550.
DR   GeneID; 594844; -.
DR   KEGG; mmu:594844; -.
DR   UCSC; uc009uir.1; mouse.
DR   CTD; 594844; -.
DR   MGI; MGI:1913354; Tceal3.
DR   GeneTree; ENSGT00510000046867; -.
DR   HOGENOM; HBG127442; -.
DR   HOVERGEN; HBG055896; -.
DR   InParanoid; Q8R0A5; -.
DR   OrthoDB; EOG4VQ9QH; -.
DR   PhylomeDB; Q8R0A5; -.
DR   NextBio; 414439; -.
DR   Bgee; Q8R0A5; -.
DR   CleanEx; MM_TCEAL3; -.
DR   Genevestigator; Q8R0A5; -.
DR   GermOnline; ENSMUSG00000044550; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR021156; TF_A-like/BEX-like.
DR   InterPro; IPR010370; TFA.
DR   PANTHER; PTHR14754; TFA; 1.
DR   Pfam; PF04538; BEX; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein.
FT   CHAIN         1    200       Transcription elongation factor A
FT                                protein-like 3.
FT                                /FTId=PRO_0000239208.
FT   COMPBIAS      2     66       Glu-rich.
FT   MOD_RES      30     30       Phosphoserine.
FT   MOD_RES     120    120       Phosphoserine (By similarity).
FT   CONFLICT    170    170       D -> Y (in Ref. 1; BAB22610).
FT   CONFLICT    200    200       L -> P (in Ref. 3; AAH27131).
SQ   SEQUENCE   200 AA;  22468 MW;  559365DA0F66A9A1 CRC64;
     MEEVRGENEG KLEKEGKPED EVEPEDEEKS DEDEKPDKKA KPAPRQGKPE EEAKPDEQGQ
     DEGKPEKQGK SDGEGKRQGE SKPDSQAKSA SEARAAEKRP AEDYVPRKAK RKTDRGTDDS
     PKNSQEDLQD RHVSSEEMMR ECADMTRAQE ELRKRQKMGG FHWVPRDAQD ALVPRGPRGV
     RGVRGGGGRS QRGLHDIPYL
//
ID   K0513_MOUSE             Reviewed;         407 AA.
AC   Q8R0A7; Q80TY8; Q8BQV3; Q8C8N9; Q8CCN0;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Uncharacterized protein KIAA0513;
GN   Name=Kiaa0513;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Corpora quadrigemina, Olfactory bulb, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65581.1; Type=Erroneous initiation;
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DR   EMBL; AK122299; BAC65581.1; ALT_INIT; mRNA.
DR   EMBL; AK032447; BAC27873.1; -; mRNA.
DR   EMBL; AK044754; BAC32067.1; -; mRNA.
DR   EMBL; AK046401; BAC32707.1; -; mRNA.
DR   EMBL; BC027126; AAH27126.1; -; mRNA.
DR   IPI; IPI00377731; -.
DR   RefSeq; NP_001157232.1; NM_001163760.1.
DR   RefSeq; NP_001157233.1; NM_001163761.1.
DR   RefSeq; NP_758490.3; NM_172286.4.
DR   UniGene; Mm.101958; -.
DR   ProteinModelPortal; Q8R0A7; -.
DR   STRING; Q8R0A7; -.
DR   PhosphoSite; Q8R0A7; -.
DR   PRIDE; Q8R0A7; -.
DR   Ensembl; ENSMUST00000034281; ENSMUSP00000034281; ENSMUSG00000031824.
DR   Ensembl; ENSMUST00000108950; ENSMUSP00000104578; ENSMUSG00000031824.
DR   GeneID; 234797; -.
DR   KEGG; mmu:234797; -.
DR   UCSC; uc009nqu.1; mouse.
DR   MGI; MGI:2443793; 6430548M08Rik.
DR   eggNOG; maNOG10039; -.
DR   GeneTree; ENSGT00390000009535; -.
DR   HOGENOM; HBG717415; -.
DR   HOVERGEN; HBG052186; -.
DR   InParanoid; Q8R0A7; -.
DR   OMA; SENDMGE; -.
DR   OrthoDB; EOG46Q6SP; -.
DR   PhylomeDB; Q8R0A7; -.
DR   NextBio; 382367; -.
DR   ArrayExpress; Q8R0A7; -.
DR   Bgee; Q8R0A7; -.
DR   CleanEx; MM_6430548M08RIK; -.
DR   Genevestigator; Q8R0A7; -.
DR   GermOnline; ENSMUSG00000031824; Mus musculus.
DR   InterPro; IPR022096; SBF2.
DR   Pfam; PF12335; SBF2; 1.
PE   2: Evidence at transcript level;
FT   CHAIN         1    407       Uncharacterized protein KIAA0513.
FT                                /FTId=PRO_0000050758.
FT   CONFLICT     78     78       F -> I (in Ref. 2; BAC27873).
FT   CONFLICT    155    155       F -> L (in Ref. 2; BAC32067).
FT   CONFLICT    198    198       P -> T (in Ref. 2; BAC32707).
SQ   SEQUENCE   407 AA;  46318 MW;  56DFB1DD3E6C933F CRC64;
     MEAPEVPVGS LIDFETEPPT SPPLEAAPST LQDPDGSLGD GASESETTES ADSENDMGES
     PSHPSWDQDR RSSSNESFSS NQSADSAPDE ETLALREFMR SYVEKIFSGG EDLDQEEKAK
     FGEYCSGEDG KGREWFARFV SAQRCKSKCV SEPTFYRLVQ SFAVVLFECH QMDDFGPAKN
     LMTMCFTYYH LGKPQLPPTE PREKPAGSID SYLKSANSWL AEKKDIAERL LKNTENMKGF
     FGGLETKLKG PLVRKNEEDE NKPKDRQTKT VTMISPEDEQ KGEKVYLYTH LRQQPIWHTL
     RFWNAAFFDA VHCERRKRSP TTRGDAGEQE EKREKWCHMT QEERDDSLRF NENITFGQLG
     TFTHNMLAFG LNKKLCSDFL KKQAVIGNLD EEQYKLLSDH IEQMATE
//
ID   RBMX2_MOUSE             Reviewed;         326 AA.
AC   Q8R0F5; A2AF74; Q3TI42;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=RNA-binding motif protein, X-linked 2;
GN   Name=Rbmx2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-140 AND SER-149, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SIMILARITY: Belongs to the IST3 family.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR   EMBL; AK076115; BAC36195.1; -; mRNA.
DR   EMBL; AK168018; BAE40004.1; -; mRNA.
DR   EMBL; AL672042; CAM27334.1; -; Genomic_DNA.
DR   EMBL; BC026976; AAH26976.1; -; mRNA.
DR   IPI; IPI00261255; -.
DR   RefSeq; NP_775552.1; NM_173376.3.
DR   UniGene; Mm.32561; -.
DR   ProteinModelPortal; Q8R0F5; -.
DR   SMR; Q8R0F5; 6-117.
DR   STRING; Q8R0F5; -.
DR   PhosphoSite; Q8R0F5; -.
DR   PRIDE; Q8R0F5; -.
DR   Ensembl; ENSMUST00000033433; ENSMUSP00000033433; ENSMUSG00000031107.
DR   GeneID; 209003; -.
DR   KEGG; mmu:209003; -.
DR   NMPDR; fig|10090.3.peg.21508; -.
DR   UCSC; uc009tct.1; mouse.
DR   CTD; 209003; -.
DR   MGI; MGI:1919414; Rbmx2.
DR   GeneTree; ENSGT00600000084414; -.
DR   HOGENOM; HBG127482; -.
DR   HOVERGEN; HBG056427; -.
DR   InParanoid; Q8R0F5; -.
DR   OrthoDB; EOG4FJ8B4; -.
DR   PhylomeDB; Q8R0F5; -.
DR   NextBio; 372506; -.
DR   ArrayExpress; Q8R0F5; -.
DR   Bgee; Q8R0F5; -.
DR   CleanEx; MM_RBMX2; -.
DR   Genevestigator; Q8R0F5; -.
DR   GermOnline; ENSMUSG00000031107; Mus musculus.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; RNA-binding.
FT   CHAIN         1    326       RNA-binding motif protein, X-linked 2.
FT                                /FTId=PRO_0000081898.
FT   DOMAIN       36    114       RRM.
FT   COMPBIAS    155    174       Lys-rich.
FT   COMPBIAS    259    324       Arg-rich.
FT   MOD_RES     140    140       Phosphothreonine.
FT   MOD_RES     149    149       Phosphoserine.
FT   MOD_RES     185    185       Phosphoserine (By similarity).
SQ   SEQUENCE   326 AA;  37536 MW;  EC702B0E79404CD5 CRC64;
     MNPLTKVKLI NELNEREVQL GVAEKVSWHS EYKHSAWIFV GGLPYELTEG DIICVFSQYG
     EIVNINLVRD KKTGKSKGFC FLCYEDQRST VLAVDNFNGI KIKGRTIRVD HVSNYRAPQE
     SEDVDDVTRE LQEKGCGVKT PPSSPPEVSE DEDAKLTKKH KKDKKEKKKR KKEKTEGQAQ
     AEQPSCSRSA TVKEKKDERA SRKHSSKTSE RAQKSEHRES KKSHSGSPDG RSSYHARAED
     PECKARKEKP KHEHKSASRR EAEEKSRERE RGRSSGTHSG RHRGHSDGRS HRSRSRSRSP
     DKSHRHKKYR HSRERDSYHG SDRRHH
//
ID   ABHD8_MOUSE             Reviewed;         439 AA.
AC   Q8R0P8; Q9DC79; Q9JMF5;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Abhydrolase domain-containing protein 8;
DE            EC=3.-.-.-;
GN   Name=Abhd8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=20145471; PubMed=10679242; DOI=10.1006/bbrc.2000.2170;
RA   Inoue S., Sano H., Ohta M.;
RT   "Growth suppression of Escherichia coli by induction of expression of
RT   mammalian genes with transmembrane or ATPase domains.";
RL   Biochem. Biophys. Res. Commun. 268:553-561(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-7 is the initiator.
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DR   EMBL; AB030191; BAA92755.1; -; mRNA.
DR   EMBL; AK003090; BAB22558.1; -; mRNA.
DR   EMBL; AK155503; BAE33297.1; -; mRNA.
DR   EMBL; BC026540; AAH26540.1; -; mRNA.
DR   IPI; IPI00312614; -.
DR   RefSeq; NP_071864.2; NM_022419.3.
DR   UniGene; Mm.276383; -.
DR   ProteinModelPortal; Q8R0P8; -.
DR   SMR; Q8R0P8; 151-409.
DR   IntAct; Q8R0P8; 1.
DR   MEROPS; S33.011; -.
DR   PhosphoSite; Q8R0P8; -.
DR   PRIDE; Q8R0P8; -.
DR   Ensembl; ENSMUST00000008094; ENSMUSP00000008094; ENSMUSG00000007950.
DR   GeneID; 64296; -.
DR   KEGG; mmu:64296; -.
DR   NMPDR; fig|10090.3.peg.18708; -.
DR   UCSC; uc009mdf.1; mouse.
DR   CTD; 64296; -.
DR   MGI; MGI:1918946; Abhd8.
DR   eggNOG; roNOG11995; -.
DR   GeneTree; ENSGT00390000007336; -.
DR   HOGENOM; HBG713949; -.
DR   HOVERGEN; HBG080814; -.
DR   InParanoid; Q8R0P8; -.
DR   OMA; QRRITVY; -.
DR   OrthoDB; EOG4X0MSH; -.
DR   PhylomeDB; Q8R0P8; -.
DR   NextBio; 320017; -.
DR   ArrayExpress; Q8R0P8; -.
DR   Bgee; Q8R0P8; -.
DR   CleanEx; MM_ABHD8; -.
DR   Genevestigator; Q8R0P8; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00412; EPOXHYDRLASE.
PE   2: Evidence at transcript level;
KW   Hydrolase.
FT   CHAIN         1    439       Abhydrolase domain-containing protein 8.
FT                                /FTId=PRO_0000281384.
FT   ACT_SITE    244    244       Charge relay system (By similarity).
FT   ACT_SITE    362    362       Charge relay system (By similarity).
FT   ACT_SITE    390    390       Charge relay system (By similarity).
FT   CONFLICT     84     84       R -> P (in Ref. 2; BAB22558).
FT   CONFLICT    248    248       S -> F (in Ref. 1; BAA92755).
SQ   SEQUENCE   439 AA;  48229 MW;  A3FDE2A1174C2481 CRC64;
     MTSEHTMLTG VTDGFFCCLL GTPPNAVRPL ESVESSDGYT FVEVKPGRVL RVKHAGPAPI
     PTPPPPPPED DPGVKTGLVR CQRRITVYRN GRLVVENLGR APRADLQGRS GSGDPPAALE
     VELAEPAGGD TRANPGSGRR RRPRRPKRTI HIDCEQRITS CKGAQADVVL FFIHGVGGSL
     AIWKEQLDFF VRLGYEVVAP DLAGHGASSA PQVAAAYTFY ALAEDMRAIF TRYAKKRNVL
     IGHSYGVSFC TFLAHEYPDL VHKVIMINGG GPTALEPSLC SIFNMPTCVL HCLSPCLAWS
     FLKAGFARQG AKEKQLLKEG NAFNVSSFVL RAMMSGQYWP EGDEVYHAEL TVPVLLVHGM
     HDKFVPVEED QRMAEILLLA FLKLIEEGSH MVMLECPETV NTLLHEFLLW EPEPEAEPKL
     EPKPKPQLLQ PEPAPGEEK
//
ID   IQEC1_MOUSE             Reviewed;         961 AA.
AC   Q8R0S2; Q3TZC3; Q5DU15;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=IQ motif and SEC7 domain-containing protein 1;
GN   Name=Iqsec1; Synonyms=Kiaa0763;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-217 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 414-961.
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 432-961.
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179 AND SER-513, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-510, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-510, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: In addition to accelerate GTP gamma S binding by ARFs of
CC       all three classes, it appears to function preferentially as a
CC       guanine nucleotide exchange protein for ARF6, mediating
CC       internalisation of beta-1 integrin (By similarity).
CC   -!- SUBUNIT: Interacts with ARF6 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R0S2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R0S2-2; Sequence=VSP_019759;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the BRAG family.
CC   -!- SIMILARITY: Contains 1 IQ domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 SEC7 domain.
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DR   EMBL; AC121954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK157963; BAE34286.1; -; mRNA.
DR   EMBL; BC026481; AAH26481.1; -; mRNA.
DR   EMBL; AK220355; BAD90418.1; -; mRNA.
DR   IPI; IPI00761443; -.
DR   IPI; IPI00762507; -.
DR   RefSeq; NP_001127855.1; NM_001134383.1.
DR   UniGene; Mm.196943; -.
DR   UniGene; Mm.473438; -.
DR   ProteinModelPortal; Q8R0S2; -.
DR   SMR; Q8R0S2; 518-864.
DR   PhosphoSite; Q8R0S2; -.
DR   PRIDE; Q8R0S2; -.
DR   Ensembl; ENSMUST00000043863; ENSMUSP00000042960; ENSMUSG00000034312.
DR   Ensembl; ENSMUST00000101153; ENSMUSP00000098712; ENSMUSG00000034312.
DR   GeneID; 232227; -.
DR   KEGG; mmu:232227; -.
DR   CTD; 232227; -.
DR   MGI; MGI:1196356; Iqsec1.
DR   GeneTree; ENSGT00590000083058; -.
DR   HOVERGEN; HBG056324; -.
DR   OMA; KKPEKGV; -.
DR   OrthoDB; EOG48GW2K; -.
DR   NextBio; 381000; -.
DR   ArrayExpress; Q8R0S2; -.
DR   Bgee; Q8R0S2; -.
DR   CleanEx; MM_IQSEC1; -.
DR   Genevestigator; Q8R0S2; -.
DR   GermOnline; ENSMUSG00000034312; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000904; Sec7.
DR   InterPro; IPR023394; SEC7_alpha_orthog.
DR   Gene3D; G3DSA:1.10.1000.11; G3DSA:1.10.1000.11; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF01369; Sec7; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00222; Sec7; 1.
DR   SUPFAM; SSF48425; Sec7; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
DR   PROSITE; PS50190; SEC7; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil;
KW   Guanine-nucleotide releasing factor; Phosphoprotein.
FT   CHAIN         1    961       IQ motif and SEC7 domain-containing
FT                                protein 1.
FT                                /FTId=PRO_0000245607.
FT   DOMAIN      133    162       IQ.
FT   DOMAIN      515    708       SEC7.
FT   DOMAIN      772    864       PH.
FT   COILED      846    877       Potential.
FT   MOD_RES     106    106       Phosphoserine.
FT   MOD_RES     179    179       Phosphoserine.
FT   MOD_RES     360    360       Phosphothreonine (By similarity).
FT   MOD_RES     510    510       Phosphoserine.
FT   MOD_RES     513    513       Phosphoserine.
FT   VAR_SEQ       1     22       MWCLHCNSERTQSLLELELDSG -> MKGDGGAVWGLMWKY
FT                                CISVRTLS (in isoform 2).
FT                                /FTId=VSP_019759.
FT   CONFLICT    759    759       E -> Q (in Ref. 3; BAD90418).
SQ   SEQUENCE   961 AA;  108015 MW;  44E9B61CE2445325 CRC64;
     MWCLHCNSER TQSLLELELD SGVEGEAPSS ETGTSLDSPS AYHQGPLVPG SSLSPDHYEH
     TSVGAYGLYA GPGPQQRTRR PRLQHSTSVL RKQAEEEAIK RSRSLSESYE LSSDLQDKQV
     EMLERKYGGR LVTRHAARTI QTAFRQYQMN KNFERLRSSM SENRMSRRIV LSNMRMQFSF
     EGPEKVHSSY FEGKQVSVTN DGSQLGALVP SECGDLSDPA LKSPAPSSDF ADAITELEDA
     FSRQVKSLAE SIDDALNCRS LHSEEVPASD TARARDTEPK PGLHGMDHRK LDEMTASYSD
     VTLYIDEEEL SPPLPLSQAG DRPSSTESDL RLRSGGAAQD YWALAHKEDK ADTDTSCRST
     PSLERPEPRL RVEHLPLLTI EPPSDSSVEL SDRSDRSSLK RQSAYERSLG GQQGSPKHGP
     HGGPPKGLPR EEPELRPRPP RPLESHLAIN GSANRQSKSE SDYSDGDNDS INSTSNSNDT
     INCSSESSSR DSLREQTLSK QTYHKETRNS WDSPAFSNDV IRKRHYRIGL NLFNKKPEKG
     IQYLIERGFV PDTPVGVAHF LLQRKGLSRQ MIGEFLGNRQ KQFNRDVLDC VVDEMDFSAM
     ELDEALRKFQ AHIRVQGEAQ KVERLIEAFS QRYCVCNPGV VRQFRNPDTI FILAFAIILL
     NTDMYSPNVK PERKMKLEDF VKNLRGVDDG EDIPRETLIG IYERIRKREL KTNEDHVSQV
     QKVEKLIVGK KPIGSLHHGL GCVLSLPHRR LVCYCRLFEV PDPNKPQKLG LHQREIFLFN
     DLLVVTKIFQ KKKNSVTYSF RQSFSLYGMQ VLLFENQYYP NGIRLTSAVP GADIKVLINF
     NAPNPQDRKK FTDDLRESVA EVQEMEKHRI ESELEKQKGV VRPSMSQCSS LKKESGNGTL
     SRACLDDSYA SGEGLKRSAL SSSLRDLSEA GKRGRRSSAG SLESNVEFQP FQPPQPPVLC
     S
//
ID   CACB4_MOUSE             Reviewed;         519 AA.
AC   Q8R0S4; Q3UHK2; Q8BRN6; Q8CAJ9;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit beta-4;
DE            Short=CAB4;
DE   AltName: Full=Calcium channel voltage-dependent subunit beta 4;
GN   Name=Cacnb4; Synonyms=Cacnlb4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 1).
RX   PubMed=14500989; DOI=10.1385/JMN:21:1:13;
RA   Murakami M., Miyoshi I., Suzuki T., Sasano H., Iijima T.;
RT   "Structures of the murine genes for the beta1- and beta4-Subunits of
RT   the voltage-dependent calcium channel.";
RL   J. Mol. Neurosci. 21:13-22(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex, Hypothalamus, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404 AND THR-410, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND SER-405, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: The beta subunit of voltage-dependent calcium channels
CC       contributes to the function of the calcium channel by increasing
CC       peak calcium current, shifting the voltage dependencies of
CC       activation and inactivation, modulating G protein inhibition and
CC       controlling the alpha-1 subunit membrane targeting (By
CC       similarity).
CC   -!- SUBUNIT: The L-type calcium channel is composed of four subunits:
CC       alpha-1, alpha-2, beta and gamma. Interacts with FASLG (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=3;
CC         IsoId=Q8R0S4-3; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q8R0S4-1; Sequence=VSP_022599;
CC       Name=2;
CC         IsoId=Q8R0S4-2; Sequence=VSP_010737;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the calcium channel beta subunit family.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB100402; BAC80139.1; -; Genomic_DNA.
DR   EMBL; AK038633; BAC30073.1; -; mRNA.
DR   EMBL; AK043850; BAC31681.1; -; mRNA.
DR   EMBL; AK079616; BAC37703.1; -; mRNA.
DR   EMBL; AK147338; BAE27855.1; -; mRNA.
DR   EMBL; BC026479; AAH26479.1; -; mRNA.
DR   IPI; IPI00131720; -.
DR   IPI; IPI00473235; -.
DR   IPI; IPI00626660; -.
DR   RefSeq; NP_001032176.1; NM_001037099.1.
DR   RefSeq; NP_666235.1; NM_146123.2.
DR   UniGene; Mm.330223; -.
DR   UniGene; Mm.472778; -.
DR   PDB; 1VYV; X-ray; 3.00 A; A=49-407.
DR   PDBsum; 1VYV; -.
DR   ProteinModelPortal; Q8R0S4; -.
DR   SMR; Q8R0S4; 49-402.
DR   STRING; Q8R0S4; -.
DR   PhosphoSite; Q8R0S4; -.
DR   PRIDE; Q8R0S4; -.
DR   Ensembl; ENSMUST00000078324; ENSMUSP00000077438; ENSMUSG00000017412.
DR   Ensembl; ENSMUST00000102760; ENSMUSP00000099821; ENSMUSG00000017412.
DR   GeneID; 12298; -.
DR   KEGG; mmu:12298; -.
DR   UCSC; uc008jra.1; mouse.
DR   UCSC; uc008jrb.1; mouse.
DR   UCSC; uc008jrd.1; mouse.
DR   CTD; 12298; -.
DR   MGI; MGI:103301; Cacnb4.
DR   GeneTree; ENSGT00390000002740; -.
DR   HOGENOM; HBG445475; -.
DR   HOVERGEN; HBG050765; -.
DR   InParanoid; Q8R0S4; -.
DR   OMA; PLVEEEY; -.
DR   OrthoDB; EOG4GQQ4X; -.
DR   NextBio; 280812; -.
DR   ArrayExpress; Q8R0S4; -.
DR   Bgee; Q8R0S4; -.
DR   Genevestigator; Q8R0S4; -.
DR   GermOnline; ENSMUSG00000017412; Mus musculus.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:MGI.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; TAS:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0046058; P:cAMP metabolic process; IMP:MGI.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
DR   GO; GO:0014051; P:gamma-aminobutyric acid secretion; IMP:MGI.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IMP:MGI.
DR   GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
DR   GO; GO:0019227; P:neuronal action potential propagation; IMP:MGI.
DR   GO; GO:0048541; P:Peyer's patch development; IMP:MGI.
DR   GO; GO:0042391; P:regulation of membrane potential; IMP:MGI.
DR   GO; GO:0048536; P:spleen development; IMP:MGI.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR   GO; GO:0050852; P:T cell receptor signaling pathway; IMP:MGI.
DR   GO; GO:0048538; P:thymus development; IMP:MGI.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR000584; VDCC_L_bsu.
DR   PANTHER; PTHR11824; Ca_channel_B; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF12052; VGCC_beta4Aa_N; 1.
DR   PRINTS; PR01626; LCACHANNELB.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Calcium channel;
KW   Calcium transport; Ion transport; Ionic channel; Phosphoprotein;
KW   SH3 domain; Transport; Voltage-gated channel.
FT   CHAIN         1    519       Voltage-dependent L-type calcium channel
FT                                subunit beta-4.
FT                                /FTId=PRO_0000144061.
FT   DOMAIN       98    160       SH3.
FT   MOD_RES      38     38       Phosphoserine.
FT   MOD_RES     404    404       Phosphoserine.
FT   MOD_RES     405    405       Phosphoserine.
FT   MOD_RES     410    410       Phosphothreonine.
FT   MOD_RES     507    507       Phosphoserine.
FT   VAR_SEQ       1     48       MSSSYGKNGAADGPHSPSSQVARGTTTRRSRLKRSDGSTTS
FT                                TSFILRQ -> MYDNLYLHGVEDSEA (in isoform
FT                                1).
FT                                /FTId=VSP_022599.
FT   VAR_SEQ       1     48       MSSSYGKNGAADGPHSPSSQVARGTTTRRSRLKRSDGSTTS
FT                                TSFILRQ -> MA (in isoform 2).
FT                                /FTId=VSP_010737.
FT   CONFLICT    492    492       P -> A (in Ref. 2; BAC31681).
FT   HELIX        72     88
FT   STRAND       94    100
FT   STRAND      124    132
FT   STRAND      135    142
FT   STRAND      148    151
FT   HELIX       153    161
FT   TURN        162    164
FT   STRAND      211    215
FT   STRAND      221    224
FT   HELIX       232    248
FT   TURN        249    251
FT   STRAND      252    258
FT   HELIX       262    264
FT   HELIX       288    302
FT   STRAND      307    312
FT   HELIX       318    321
FT   STRAND      329    333
FT   HELIX       338    346
FT   HELIX       350    353
FT   HELIX       356    367
FT   HELIX       371    373
FT   STRAND      375    378
FT   STRAND      380    382
FT   HELIX       383    401
SQ   SEQUENCE   519 AA;  57950 MW;  663A88C7BCF7E90C CRC64;
     MSSSYGKNGA ADGPHSPSSQ VARGTTTRRS RLKRSDGSTT STSFILRQGS ADSYTSRPSD
     SDVSLEEDRE AIRQEREQQA AIQLERAKSK PVAFAVKTNV SYCGALDEDV PVPSTAISFD
     AKDFLHIKEK YNNDWWIGRL VKEGCEIGFI PSPLRLENIR IQQEQKRGRF HGGKSSGNSS
     SSLGEMVSGT FRATPTTTAK QKQKVTEHIP PYDVVPSMRP VVLVGPSLKG YEVTDMMQKA
     LFDFLKHRFD GRISITRVTA DISLAKRSVL NNPSKRAIIE RSNTRSSLAE VQSEIERIFE
     LARSLQLVVL DADTINHPAQ LIKTSLAPII VHVKVSSPKV LQRLIKSRGK SQSKHLNVQL
     VAADKLAQCP PEMFDVILDE NQLEDACEHL GEYLEAYWRA THTSSSTPMT PLLGRNVGST
     ALSPYPTAIS GLQSQRMRHS NHSTENSPIE RRSLMTSDEN YHNERARKSR NRLSSSSQHS
     RDHYPLVEED YPDSYQDTYK PHRNRGSPGG CSHDSRHRL
//
ID   FTHFD_MOUSE             Reviewed;         902 AA.
AC   Q8R0Y6;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=10-formyltetrahydrofolate dehydrogenase;
DE            Short=10-FTHFDH;
DE            EC=1.5.1.6;
DE   AltName: Full=Aldehyde dehydrogenase family 1 member L1;
GN   Name=Aldh1l1; Synonyms=Fthfd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + NADP(+) + H(2)O =
CC       tetrahydrofolate + CO(2) + NADPH.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the GART family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the aldehyde
CC       dehydrogenase family. ALDH1L subfamily.
CC   -!- SIMILARITY: Contains 1 acyl carrier domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC025939; AAH25939.1; -; mRNA.
DR   EMBL; BC028817; AAH28817.1; -; mRNA.
DR   EMBL; BC030722; AAH30722.1; -; mRNA.
DR   EMBL; BC030723; AAH30723.1; -; mRNA.
DR   EMBL; BC030727; AAH30727.1; -; mRNA.
DR   EMBL; BC030730; AAH30730.1; -; mRNA.
DR   IPI; IPI00153317; -.
DR   RefSeq; NP_081682.1; NM_027406.1.
DR   UniGene; Mm.30035; -.
DR   ProteinModelPortal; Q8R0Y6; -.
DR   SMR; Q8R0Y6; 1-402, 405-902.
DR   STRING; Q8R0Y6; -.
DR   PhosphoSite; Q8R0Y6; -.
DR   PRIDE; Q8R0Y6; -.
DR   Ensembl; ENSMUST00000032175; ENSMUSP00000032175; ENSMUSG00000030088.
DR   GeneID; 107747; -.
DR   KEGG; mmu:107747; -.
DR   UCSC; uc009cxl.1; mouse.
DR   CTD; 107747; -.
DR   MGI; MGI:1340024; Aldh1l1.
DR   HOGENOM; HBG315849; -.
DR   HOVERGEN; HBG051668; -.
DR   InParanoid; Q8R0Y6; -.
DR   OMA; EDSIHDQ; -.
DR   PhylomeDB; Q8R0Y6; -.
DR   BRENDA; 1.5.1.6; 244.
DR   NextBio; 359368; -.
DR   ArrayExpress; Q8R0Y6; -.
DR   Bgee; Q8R0Y6; -.
DR   CleanEx; MM_ALDH1L1; -.
DR   Genevestigator; Q8R0Y6; -.
DR   GermOnline; ENSMUSG00000030088; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0000036; F:acyl carrier activity; IEA:InterPro.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0016155; F:formyltetrahydrofolate dehydrogenase activity; IEA:EC.
DR   GO; GO:0016742; F:hydroxymethyl-, formyl- and related transferase activity; IEA:InterPro.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:InterPro.
DR   GO; GO:0009258; P:10-formyltetrahydrofolate catabolic process; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR011407; 10_FTHF_DH.
DR   InterPro; IPR009081; Acyl_carrier_prot-like.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR005793; Formyl_trans_C.
DR   InterPro; IPR002376; Formyl_transf_N.
DR   InterPro; IPR011034; Formyl_transferase_C-like.
DR   InterPro; IPR001555; GART_AS.
DR   InterPro; IPR006163; Phsphopanteth-bd.
DR   Gene3D; G3DSA:1.10.1200.10; ACP_like; 1.
DR   Gene3D; G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 1.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   Gene3D; G3DSA:3.10.25.10; Formyl_trans_C; 1.
DR   Gene3D; G3DSA:3.40.50.170; Formyl_transf_N; 1.
DR   PANTHER; PTHR11699; Aldehyde_dehyd; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   Pfam; PF02911; Formyl_trans_C; 1.
DR   Pfam; PF00551; Formyl_trans_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   PIRSF; PIRSF036489; 10-FTHFDH; 1.
DR   SUPFAM; SSF47336; ACP_like; 1.
DR   SUPFAM; SSF53720; Aldehyde_DH/Histidinol_DH; 1.
DR   SUPFAM; SSF50486; FMT_C_like; 1.
DR   SUPFAM; SSF53328; formyl_transf; 1.
DR   PROSITE; PS50075; ACP_DOMAIN; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
DR   PROSITE; PS00373; GART; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Cytoplasm; NADP; One-carbon metabolism; Oxidoreductase;
KW   Phosphopantetheine; Phosphoprotein.
FT   CHAIN         1    902       10-formyltetrahydrofolate dehydrogenase.
FT                                /FTId=PRO_0000199420.
FT   DOMAIN      323    392       Acyl carrier.
FT   REGION        1    203       GART.
FT   REGION      417    902       Aldehyde dehydrogenase.
FT   ACT_SITE    106    106       Proton donor (By similarity).
FT   ACT_SITE    673    673       By similarity.
FT   ACT_SITE    707    707       By similarity.
FT   SITE        142    142       Essential for catalytic activity (By
FT                                similarity).
FT   MOD_RES     354    354       O-(pantetheine 4'-phosphoryl)serine (By
FT                                similarity).
FT   MOD_RES     613    613       Phosphothreonine (By similarity).
SQ   SEQUENCE   902 AA;  98709 MW;  9B5526A7FB41909E CRC64;
     MKIAVIGQSL FGQEVYCQLR KEGHEVVGVF TIPDKDGKAD PLGLEAEKDG VPVFKFPRWR
     ARGQALPEVV AKYQALGAEL NVLPFCSQFI PMEVINAPRH GSIIYHPSLL PRHRGASAIN
     WTLIHGDKKG GFTIFWADDG LDTGDLLLQK ECDVLPDDTV STLYNRFLFP EGIKGMVQAV
     RLIAEGTAPR RPQPEEGATY EGIQKKETAM INWDQPAEAI HNWIRGNDKV PGAWTEACGQ
     KLTFFNSTLN TSGLVAQGEA LPIPGAHRPG LVTKAGLILF GNDDRMLLVK NIQLEDGKMM
     PASQFFKGSA SSALELTEEE LATAEAVRSS WMRILPNVPE VEDSTDFFKS GAASVDVVRL
     VEEVKELCDG LELENEDVYM ATTFGDFIQL LVRKLRGEDG ESECVINYVE KAVKKLTLQM
     PYQLFIGGEF VDAEGAKTYS TINPTDGSVI CQVSLAQVSD VDKAVAAAKE AFENGLWGKI
     NARDRGRLLY RLADLMEQHQ EELATIEALD AGAVYTLALK THVGMSIQTF RYFAGWCDKI
     QGATIPINQA RPNRNLTLTK KEPVGVCGIV IPWNYPLMML SWKTAACLAA GNTVVIKPAQ
     VTPLTALKFA ELTLKAGIPK GVVNILPGSG SLVGQRLSDH PDVRKIGFTG STEVGKHIMK
     SCALSNVKKV SLELGGKSPL IIFADCDLNK AVQMGMSSVF FNKGENCIAA GRLFVEDSIH
     DQFVQKVVEE VGKMKIGNPL DRDTNHGPQN HEAHLRKLVE YCQRGVKEGA TLVCGGNQVP
     RPGFFFQPTV FTDVEDHMYI AKEESFGPIM IISRFADGDV DAVLSRANAT EFGLASGVFT
     RDINKALYVS DKLQAGTVFV NTYNKTDVAA PFGGFKQSGF GKDLGEAALN EYLRIKTVTF
     EY
//
ID   VP37C_MOUSE             Reviewed;         352 AA.
AC   Q8R105; Q3TY76;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Vacuolar protein sorting-associated protein 37C;
DE   AltName: Full=ESCRT-I complex subunit VPS37C;
GN   Name=Vps37c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Component of the ESCRT-I complex, a regulator of
CC       vesicular trafficking process. Required for the sorting of
CC       endocytic ubiquitinated cargos into multivesicular bodies. May be
CC       involved in cell growth and differentiation (By similarity).
CC   -!- SUBUNIT: Component of the ESCRT-I complex (endosomal sorting
CC       complex required for transport I) which consists of TSG101, VPS28,
CC       a VPS37 protein (VPS37A to -D) and a FAM125/MVB12 protein (FAM125A
CC       or -B) in a 1:1:1:1 stoechiometry. Interacts with TSG101, VPS28,
CC       FAM125A and FAM125B. Interacts with HGS and STAM2. Interacts with
CC       CEP55 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane; Peripheral membrane
CC       protein (By similarity). Note=Probably associates with membranes
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R105-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R105-2; Sequence=VSP_029730;
CC   -!- SIMILARITY: Belongs to the VPS37 family.
CC   -!- SIMILARITY: Contains 1 VPS37 C-terminal domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK158833; BAE34687.1; -; mRNA.
DR   EMBL; AK159309; BAE34977.1; -; mRNA.
DR   EMBL; BC025865; AAH25865.1; -; mRNA.
DR   IPI; IPI00153241; -.
DR   IPI; IPI00877200; -.
DR   RefSeq; NP_852068.1; NM_181403.2.
DR   UniGene; Mm.19091; -.
DR   ProteinModelPortal; Q8R105; -.
DR   IntAct; Q8R105; 1.
DR   STRING; Q8R105; -.
DR   PhosphoSite; Q8R105; -.
DR   PRIDE; Q8R105; -.
DR   Ensembl; ENSMUST00000087951; ENSMUSP00000085264; ENSMUSG00000048832.
DR   GeneID; 107305; -.
DR   KEGG; mmu:107305; -.
DR   UCSC; uc008gqs.1; mouse.
DR   CTD; 107305; -.
DR   MGI; MGI:2147661; Vps37c.
DR   eggNOG; roNOG11516; -.
DR   GeneTree; ENSGT00530000063123; -.
DR   HOGENOM; HBG281316; -.
DR   HOVERGEN; HBG073355; -.
DR   InParanoid; Q8R105; -.
DR   OMA; SWSPQRS; -.
DR   OrthoDB; EOG4B2SZG; -.
DR   PhylomeDB; Q8R105; -.
DR   NextBio; 358674; -.
DR   ArrayExpress; Q8R105; -.
DR   Bgee; Q8R105; -.
DR   CleanEx; MM_VPS37C; -.
DR   Genevestigator; Q8R105; -.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR009851; Mod_r.
DR   Pfam; PF07200; Mod_r; 1.
DR   PROSITE; PS51314; VPS37_C; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Endosome; Membrane; Protein transport;
KW   Transport.
FT   CHAIN         1    352       Vacuolar protein sorting-associated
FT                                protein 37C.
FT                                /FTId=PRO_0000312199.
FT   DOMAIN       78    167       VPS37 C-terminal.
FT   COMPBIAS    160    350       Pro-rich.
FT   VAR_SEQ       1    108       Missing (in isoform 2).
FT                                /FTId=VSP_029730.
SQ   SEQUENCE   352 AA;  38453 MW;  CA3F793154A6BB95 CRC64;
     MEGLKDKTLQ ELEEMQNDPE AIARLALESP EVQDLQLERE MALATNRSLA EQNLEFQGPL
     EISRSNLSDK YQELRKLVER CQEQKAKLEK FSSALQPGTL LDLLQIEGMK IEEESEAMAE
     KFLEGEVPLE TFLESFSSMR TLLHLRRVRV EKLQDVVRRP RALPELAGDV PPKRPPPPRP
     VPQATPPETE EQPPQPSVVT PYPLPYSPSP GLPVGPTAQG ALQPAPFPVV AQPSSYGGPL
     GPYPSPHPGP RAMVGYSWSP QRSGPPQPGY PTAPTSTSGP GYPLVGGRTP GPGYPQQSPY
     LPSGNKPPYP TQPQLPGFPG QPQPPVPPQP PYPPGTTPSY GFHPPGPAWP RY
//
ID   FAD1_MOUSE              Reviewed;         492 AA.
AC   Q8R123; Q3TSN6; Q8BXQ1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=FAD synthase;
DE            EC=2.7.7.2;
DE   AltName: Full=FAD pyrophosphorylase;
DE   AltName: Full=FMN adenylyltransferase;
DE   AltName: Full=Flavin adenine dinucleotide synthase;
DE   Includes:
DE     RecName: Full=Molybdenum cofactor biosynthesis protein-like region;
DE   Includes:
DE     RecName: Full=FAD synthase region;
GN   Name=Flad1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, Liver, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 230-237, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the adenylation of flavin mononucleotide (FMN)
CC       to form flavin adenine dinucleotide (FAD) coenzyme (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + FMN = diphosphate + FAD.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN:
CC       step 1/1.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R123-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R123-2; Sequence=VSP_027955;
CC   -!- DOMAIN: The molybdenum cofactor biosynthesis protein-like region
CC       may not be functional.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the moaB/mog
CC       family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the PAPS
CC       reductase family. FAD1 subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK044501; BAC31952.1; -; mRNA.
DR   EMBL; AK161929; BAE36639.1; -; mRNA.
DR   EMBL; BC009152; AAH09152.2; -; mRNA.
DR   EMBL; BC025817; AAH25817.1; -; mRNA.
DR   EMBL; BC046769; AAH46769.1; -; mRNA.
DR   IPI; IPI00226787; -.
DR   IPI; IPI00831326; -.
DR   RefSeq; NP_796015.2; NM_177041.3.
DR   UniGene; Mm.258142; -.
DR   ProteinModelPortal; Q8R123; -.
DR   SMR; Q8R123; 15-177, 276-492.
DR   STRING; Q8R123; -.
DR   PhosphoSite; Q8R123; -.
DR   PRIDE; Q8R123; -.
DR   Ensembl; ENSMUST00000050398; ENSMUSP00000051366; ENSMUSG00000042642.
DR   Ensembl; ENSMUST00000107426; ENSMUSP00000103049; ENSMUSG00000042642.
DR   Ensembl; ENSMUST00000107429; ENSMUSP00000103052; ENSMUSG00000042642.
DR   GeneID; 319945; -.
DR   KEGG; mmu:319945; -.
DR   UCSC; uc008pzi.1; mouse.
DR   CTD; 319945; -.
DR   MGI; MGI:2443030; Flad1.
DR   GeneTree; ENSGT00390000007266; -.
DR   HOVERGEN; HBG058211; -.
DR   OMA; SFMRINP; -.
DR   OrthoDB; EOG4P2Q27; -.
DR   PhylomeDB; Q8R123; -.
DR   BRENDA; 2.7.7.2; 244.
DR   NextBio; 395713; -.
DR   ArrayExpress; Q8R123; -.
DR   Bgee; Q8R123; -.
DR   Genevestigator; Q8R123; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003919; F:FMN adenylyltransferase activity; IEA:EC.
DR   GO; GO:0006747; P:FAD biosynthetic process; IEA:InterPro.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:InterPro.
DR   InterPro; IPR012183; FAD_synth_Mopterin-bd.
DR   InterPro; IPR001453; Mopterin-bd.
DR   InterPro; IPR002500; PAPS_reduct.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.980.10; MPT_bd; 1.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   Pfam; PF00994; MoCF_biosynth; 1.
DR   Pfam; PF01507; PAPS_reduct; 1.
DR   PIRSF; PIRSF036620; MPTbdFAD; 1.
DR   SMART; SM00852; MoCF_biosynth; 1.
DR   SUPFAM; SSF53218; MoCF_biosynth; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Direct protein sequencing; FAD;
KW   FMN; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
KW   Transferase.
FT   CHAIN         1    492       FAD synthase.
FT                                /FTId=PRO_0000302738.
FT   REGION       19    110       Molybdenum cofactor biosynthesis protein-
FT                                like.
FT   REGION      303    460       FAD synthase.
FT   MOD_RES     468    468       Phosphoserine (By similarity).
FT   VAR_SEQ     492    492       M -> IPKTPGASWPSPRMGHKELKKEPRTLL (in
FT                                isoform 2).
FT                                /FTId=VSP_027955.
FT   CONFLICT     73     73       R -> S (in Ref. 1; BAE36639).
FT   CONFLICT    390    390       L -> Q (in Ref. 1; BAE36639).
SQ   SEQUENCE   492 AA;  54766 MW;  75008DD249A7F43E CRC64;
     MASRASELPP GSGRSVTAGI IIVGDEILKG HTQDTNTYFL CRTLRSLGVQ VCRVSVVPDE
     VATIASEVNS FSRRFTHVLT AGGIGPTHDD VTFEAVAQAF GEELKPHPEL QAAIKTLGGE
     GWEKLSMVPS SARLHYGTDP RTGHPFRFPL VSVRNVYLFP GIPELLRRVL EGLKGLFQNT
     AVQFHLKELY VAASEGSIAP ILSEAQAHFG RRLSLGSYPD WSSNYFQVKL ILDSEEKEPL
     EECLAYLTAR LPQGSLVPYQ PDAVEKAGEA VYKLAESGSC LGKKVAGALQ TIETALAQYH
     LSQLCVGFNG GKDCTALLHL FHAAVQRKFP DVPKPLQILY IRSISPFPEL EQFLQDTIKR
     YNLQVLEAEG NMKQALGELQ EKHPQLEAVL MGTRRTDPYS CSLSHFSPTD PGWPSFMRIN
     PLLDWTYRNI WEFLRQLFVP YCILYDRGYT SLGSRENTTQ NPALKCLSPG GHPVYRPAYL
     LENEDEERNS RM
//
ID   SCPDH_MOUSE             Reviewed;         429 AA.
AC   Q8R127; Q3TMB9;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Probable saccharopine dehydrogenase;
DE            EC=1.5.1.9;
GN   Name=Sccpdh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Corpora quadrigemina, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NAD(+)
CC       + H(2)O = L-glutamate + 2-aminoadipate 6-semialdehyde + NADH.
CC   -!- PATHWAY: Amino-acid degradation; L-lysine degradation via
CC       saccharopine pathway; glutaryl-CoA from L-lysine: step 2/6.
CC   -!- SIMILARITY: Belongs to the saccharopine dehydrogenase family.
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DR   EMBL; AK042919; BAC31405.1; -; mRNA.
DR   EMBL; AK046033; BAC32578.1; -; mRNA.
DR   EMBL; AK077695; BAC36962.1; -; mRNA.
DR   EMBL; AK082803; BAC38628.1; -; mRNA.
DR   EMBL; AK166018; BAE38523.1; -; mRNA.
DR   EMBL; BC025803; AAH25803.1; -; mRNA.
DR   IPI; IPI00153266; -.
DR   RefSeq; NP_848768.1; NM_178653.3.
DR   UniGene; Mm.136458; -.
DR   ProteinModelPortal; Q8R127; -.
DR   SMR; Q8R127; 10-103.
DR   PhosphoSite; Q8R127; -.
DR   PRIDE; Q8R127; -.
DR   Ensembl; ENSMUST00000040538; ENSMUSP00000040956; ENSMUSG00000038936.
DR   GeneID; 109232; -.
DR   KEGG; mmu:109232; -.
DR   UCSC; uc007dvp.1; mouse.
DR   CTD; 109232; -.
DR   MGI; MGI:1924486; Sccpdh.
DR   eggNOG; roNOG13655; -.
DR   GeneTree; ENSGT00390000004799; -.
DR   HOGENOM; HBG527018; -.
DR   HOVERGEN; HBG057028; -.
DR   InParanoid; Q8R127; -.
DR   OMA; GTSCIDI; -.
DR   OrthoDB; EOG4C5CJK; -.
DR   PhylomeDB; Q8R127; -.
DR   BRENDA; 1.5.1.9; 244.
DR   NextBio; 361807; -.
DR   ArrayExpress; Q8R127; -.
DR   Bgee; Q8R127; -.
DR   CleanEx; MM_SCCPDH; -.
DR   Genevestigator; Q8R127; -.
DR   GermOnline; ENSMUSG00000038936; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0047131; F:saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR005097; Saccharopine_DH/HSpermid_syn.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF03435; Saccharop_dh; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; NAD; Oxidoreductase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    429       Probable saccharopine dehydrogenase.
FT                                /FTId=PRO_0000212841.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
SQ   SEQUENCE   429 AA;  47129 MW;  FCC63118BFCEE7E4 CRC64;
     MATEQRPFHL VVFGASGFTG QFVTEEVARE QIASEQSSRL PWAVAGRSKE KLQQVLEKAA
     QKLGRPSLSS EVGVIICDIS NPASLDEMAK QAKLVLNCVG PYRFYGEPVV KACIENGTSC
     IDICGEPQFL ELMHAKYHEK AAEKGVYIIG SSGFDSIPAD LGVLYTRNQM NGTLTAVESF
     LTINTGPEGL CIHDGTWKSA IYGFGDKGSL RKLRSVSCLK PVPIVGTKLK RRWPVSYCRE
     LNSYSIPFLG SDISVVKRTQ RYLHENLEDS PVQYAAYVTV GGITSVIKLM FAGLFFLFFV
     KFSIGRQLLI KFPWLFSFGY FSKQGPTQKQ MDETSFTMTF FGQGYSHGTC VEKNKPNIRI
     CTQVKGPEAG YVATPIAMVQ AAMTFLSDAS DLPKGGGVFT PGAAFSRTKL IDRLNKHGIE
     FSVISSSEV
//
ID   TM119_MOUSE             Reviewed;         280 AA.
AC   Q8R138; Q8BP14;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Transmembrane protein 119;
DE   Flags: Precursor;
GN   Name=Tmem119;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Muellerian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
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DR   EMBL; AK078473; BAC37292.1; -; mRNA.
DR   EMBL; AK170712; BAE41970.1; -; mRNA.
DR   EMBL; BC025600; AAH25600.1; -; mRNA.
DR   IPI; IPI00395051; -.
DR   RefSeq; NP_666274.1; NM_146162.2.
DR   UniGene; Mm.41681; -.
DR   ProteinModelPortal; Q8R138; -.
DR   PRIDE; Q8R138; -.
DR   Ensembl; ENSMUST00000067853; ENSMUSP00000070551; ENSMUSG00000054675.
DR   GeneID; 231633; -.
DR   KEGG; mmu:231633; -.
DR   UCSC; uc008yyq.1; mouse.
DR   CTD; 231633; -.
DR   MGI; MGI:2385228; Tmem119.
DR   eggNOG; maNOG19713; -.
DR   GeneTree; ENSGT00390000017134; -.
DR   HOGENOM; HBG268743; -.
DR   HOVERGEN; HBG080787; -.
DR   InParanoid; Q8R138; -.
DR   OMA; MFIVCAA; -.
DR   OrthoDB; EOG4SF96W; -.
DR   PhylomeDB; Q8R138; -.
DR   NextBio; 380669; -.
DR   ArrayExpress; Q8R138; -.
DR   Bgee; Q8R138; -.
DR   CleanEx; MM_TMEM119; -.
DR   Genevestigator; Q8R138; -.
DR   GermOnline; ENSMUSG00000054675; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Membrane; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21    280       Transmembrane protein 119.
FT                                /FTId=PRO_0000251221.
FT   TOPO_DOM     21     91       Extracellular (Potential).
FT   TRANSMEM     92    112       Helical; (Potential).
FT   TOPO_DOM    113    280       Cytoplasmic (Potential).
FT   CONFLICT     78     78       L -> H (in Ref. 1; BAC37292).
SQ   SEQUENCE   280 AA;  29401 MW;  CBC0F96107F75C29 CRC64;
     MVPWFLLSLL LLARPVPGVA YSVSLPASFL EDVAGSGEAE GSSASSPSLP PPGTPAFSPT
     PERPQPTALD GPVPPTNLLE GIMDFFRQYV MLIAVVGSLT FLIMFIVCAA LITRQKHKAT
     AYYPSSFPEK KYVDQRDRAG GPRTFSEVPD RAPDSRHEEG LDTSHQLQAD ILAATQNLRS
     PARALPGNGE GAKPVKGGSE EEEEEVLSGQ EEAQEAPVCG VTEEKLGVPE ESVSAEAEGV
     PATSEGQGEA EGSFSLAQES QGATGPPESP CACNRVSPSV
//
ID   S29A4_MOUSE             Reviewed;         528 AA.
AC   Q8R139;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Equilibrative nucleoside transporter 4;
DE   AltName: Full=Solute carrier family 29 member 4;
GN   Name=Slc29a4; Synonyms=Ent4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   FUNCTION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT ASN-521.
RX   PubMed=16873718; DOI=10.1161/01.RES.0000238359.18495.42;
RA   Barnes K., Dobrzynski H., Foppolo S., Beal P.R., Ismat F.,
RA   Scullion E.R., Sun L., Tellez J., Ritzel M.W., Claycomb W.C.,
RA   Cass C.E., Young J.D., Billeter-Clark R., Boyett M.R., Baldwin S.A.;
RT   "Distribution and functional characterization of equilibrative
RT   nucleoside transporter-4, a novel cardiac adenosine transporter
RT   activated at acidic pH.";
RL   Circ. Res. 99:510-519(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-220, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: Functions as a polyspecific organic cation transporter,
CC       efficiently transporting many organic cations such as monoamine
CC       neurotransmitters 1-methyl-4-phenylpyridinium and biogenic amines
CC       including serotonin, dopamine, norepinephrine and epinephrine. May
CC       play a role in regulating central nervous system homeostasis of
CC       monoamine neurotransmitters. May be involved in luminal transport
CC       of organic cations in the kidney and seems to use luminal proton
CC       gradient to drive organic cation reabsorptprev reabsorption. Does
CC       not seem to transport nucleoside and nucleoside analogs such as
CC       uridine, cytidine, thymidine, adenosine, inosine, guanosine, and
CC       azidothymidine. In (PubMed:16873718) adenosine is efficiently
CC       transported but in a fashion highly sensitive to extracellular pH,
CC       with maximal activity in the pH range 5.5 to 6.5. Glu-206 is
CC       essential for the cation selectivity and may function as the
CC       charge sensor for cationic substrates. Transport is chloride and
CC       sodium-independent but appears to be sensitive to changes in
CC       membrane potential. Weakly inhibited by the classical inhibitors
CC       of equilibrative nucleoside transport, dipyridamole, dilazep, and
CC       nitrobenzylthioinosine. May play a role in the regulation of
CC       extracellular adenosine concentrations in cardiac tissues, in
CC       particular during ischemia (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Potential). Apical cell membrane; Multi-pass membrane protein (By
CC       similarity). Note=Located to the plasma membranes of ventricular
CC       myocytes and vascular endothelial cells. Targeted to the apical
CC       membranes of differentiated kidney epithelial cells (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in heart.
CC   -!- PTM: N-glycosylated.
CC   -!- SIMILARITY: Belongs to the SLC29A transporter family.
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DR   EMBL; BC025599; AAH25599.1; -; mRNA.
DR   IPI; IPI00153278; -.
DR   RefSeq; NP_666369.1; NM_146257.2.
DR   UniGene; Mm.125942; -.
DR   ProteinModelPortal; Q8R139; -.
DR   STRING; Q8R139; -.
DR   PhosphoSite; Q8R139; -.
DR   PRIDE; Q8R139; -.
DR   Ensembl; ENSMUST00000058418; ENSMUSP00000059896; ENSMUSG00000050822.
DR   GeneID; 243328; -.
DR   KEGG; mmu:243328; -.
DR   UCSC; uc009aiz.1; mouse.
DR   CTD; 243328; -.
DR   MGI; MGI:2385330; Slc29a4.
DR   eggNOG; roNOG07138; -.
DR   GeneTree; ENSGT00390000002232; -.
DR   HOGENOM; HBG445133; -.
DR   HOVERGEN; HBG095787; -.
DR   InParanoid; Q8R139; -.
DR   OMA; TTRPRDS; -.
DR   OrthoDB; EOG43FGWW; -.
DR   NextBio; 385721; -.
DR   ArrayExpress; Q8R139; -.
DR   Bgee; Q8R139; -.
DR   Genevestigator; Q8R139; -.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005337; F:nucleoside transmembrane transporter activity; IEA:InterPro.
DR   InterPro; IPR002259; DER/eqnu_transpt.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   PANTHER; PTHR10332; DER/eqnu_transpt; 1.
DR   Pfam; PF01733; Nucleoside_tran; 1.
DR   PRINTS; PR01130; DERENTRNSPRT.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    528       Equilibrative nucleoside transporter 4.
FT                                /FTId=PRO_0000326252.
FT   TOPO_DOM      1     68       Extracellular (Potential).
FT   TRANSMEM     69     89       Helical; (Potential).
FT   TOPO_DOM     90    101       Cytoplasmic (Potential).
FT   TRANSMEM    102    122       Helical; (Potential).
FT   TOPO_DOM    123    139       Extracellular (Potential).
FT   TRANSMEM    140    160       Helical; (Potential).
FT   TOPO_DOM    161    166       Cytoplasmic (Potential).
FT   TRANSMEM    167    187       Helical; (Potential).
FT   TOPO_DOM    188    231       Extracellular (Potential).
FT   TRANSMEM    232    252       Helical; (Potential).
FT   TOPO_DOM    253    346       Cytoplasmic (Potential).
FT   TRANSMEM    347    367       Helical; (Potential).
FT   TOPO_DOM    368    376       Extracellular (Potential).
FT   TRANSMEM    377    397       Helical; (Potential).
FT   TOPO_DOM    398    411       Cytoplasmic (Potential).
FT   TRANSMEM    412    432       Helical; (Potential).
FT   TOPO_DOM    433    445       Extracellular (Potential).
FT   TRANSMEM    446    466       Helical; (Potential).
FT   TOPO_DOM    467    481       Cytoplasmic (Potential).
FT   TRANSMEM    482    504       Helical; (Potential).
FT   TOPO_DOM    505    528       Extracellular (Potential).
FT   COMPBIAS    515    520       Poly-Ala.
FT   MOD_RES     220    220       Phosphothreonine.
FT   CARBOHYD    521    521       N-linked (GlcNAc...).
SQ   SEQUENCE   528 AA;  58099 MW;  96379B4FBB2AD2ED CRC64;
     MGSIGSQRLK EPCVAATSDQ SVVTSFSFDN FQLETTAEGA QDPGIRVRGV PTFTDSAVEE
     PVPDDRYHAI YFAMLLAGVG FLLPYNSFIT DVDYLHHKYP GTSIVFDMSL TYILVALAAV
     LLNNVVVERL NLHTRITTGY LLALGPLLFI SICDVWLQLF SHDQAYAINL AAVGTVAFGC
     TVQQSSFYGY TGLLPKRYTQ GVMTGESTAG VMISLSRILT KLLLPDERAS TIIFFLVSAG
     LELLCFLLHL LVRRSRFVLY YTTRPRDSRP VQAGYRVHHD VASGDIHFEH QTPALSSSRS
     PKESPAHEVT HSNSGVYMRF DVPRPRVKRS WPTFRALLLH RYVVARVIWA DMLSIAVTYF
     ITLCLFPGLE SEIRHCVLGE WLPILVMAVF NLSDFVGKIL AALPVEWRGT HLLACSCLRV
     VFIPLFILCV YPSGMPALRH PAWPCVFSLL MGISNGYFGS VPMILAAGKV SPKQRELAGN
     TMTVSYMSGL TLGSAVAYCT YSLTRDAHGS CFQTATAAAA NDSIPVGP
//
ID   APEH_MOUSE              Reviewed;         732 AA.
AC   Q8R146; Q8K029; Q8R0M9;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   07-NOV-2003, sequence version 2.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Acylamino-acid-releasing enzyme;
DE            Short=AARE;
DE            EC=3.4.19.1;
DE   AltName: Full=Acyl-peptide hydrolase;
DE            Short=APH;
DE   AltName: Full=Acylaminoacyl-peptidase;
GN   Name=Apeh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Colon, Kidney, and Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: This enzyme catalyzes the hydrolysis of the N-terminal
CC       peptide bond of an N-acetylated peptide to generate an N-
CC       acetylated amino acid and a peptide with a free N-terminus. It
CC       preferentially cleaves off Ac-Ala, Ac-Met and Ac-Ser (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Cleavage of an N-acetyl or N-formyl amino acid
CC       from the N-terminus of a polypeptide.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R146-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R146-2; Sequence=VSP_008866;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the peptidase S9C family.
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DR   EMBL; BC025494; AAH25494.1; -; mRNA.
DR   EMBL; BC026594; AAH26594.1; -; mRNA.
DR   EMBL; BC034199; AAH34199.1; -; mRNA.
DR   IPI; IPI00279218; -.
DR   IPI; IPI00387245; -.
DR   UniGene; Mm.219639; -.
DR   ProteinModelPortal; Q8R146; -.
DR   SMR; Q8R146; 222-317, 478-613.
DR   STRING; Q8R146; -.
DR   MEROPS; S09.004; -.
DR   PhosphoSite; Q8R146; -.
DR   PRIDE; Q8R146; -.
DR   Ensembl; ENSMUST00000081309; ENSMUSP00000080058; ENSMUSG00000032590.
DR   UCSC; uc009ros.1; mouse.
DR   UCSC; uc009rot.1; mouse.
DR   MGI; MGI:88041; Apeh.
DR   eggNOG; roNOG04047; -.
DR   GeneTree; ENSGT00390000013172; -.
DR   HOGENOM; HBG446946; -.
DR   HOVERGEN; HBG000869; -.
DR   InParanoid; Q8R146; -.
DR   OrthoDB; EOG495ZR6; -.
DR   BRENDA; 3.4.19.1; 244.
DR   NextBio; 382781; -.
DR   ArrayExpress; Q8R146; -.
DR   Bgee; Q8R146; -.
DR   CleanEx; MM_APEH; -.
DR   Genevestigator; Q8R146; -.
DR   GermOnline; ENSMUSG00000032590; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR004106; Peptidase_S9A_B_C_N.
DR   Gene3D; G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 2.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF50993; Peptidase_S9A_N; 1.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Cytoplasm; Hydrolase.
FT   CHAIN         1    732       Acylamino-acid-releasing enzyme.
FT                                /FTId=PRO_0000122431.
FT   ACT_SITE    587    587       Charge relay system (By similarity).
FT   ACT_SITE    675    675       Charge relay system (By similarity).
FT   ACT_SITE    707    707       Charge relay system (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   VAR_SEQ     508    522       Missing (in isoform 2).
FT                                /FTId=VSP_008866.
SQ   SEQUENCE   732 AA;  81522 MW;  D393E9F600BB2CC4 CRC64;
     MERQVLLSEP QEAAALYRGL SRQPSLSAAC LGPEVTTQYG GLYRTVHTEW TQRDLDRMEN
     IRFCRQYLVF HDGDSVVFAG PAGNSVETPG ELLSRESPSG TMKAVLRKAG GAVSGEEKQF
     LEVWEKNRKL KSFNLSALEK HGPVYEDDCF GCLSWSHSET HLLYVAEKKR PKAESFFQTK
     ALDVSASDEE MARPKKPDQA IKGDQFVFYE DWGETMVSKS IPVLCVLDIE SGNISVLEGV
     PENVSPGQAF WAPGDTGVVF VGWWHEPFRL GIRYCTNRRS ALYYVDLSGG KCELLSDESL
     AVCSPRLSPD QCRVVYLQYP SLAPHHQCSQ LFLYDWYTKV TSLVVDIVPR QLGESFSGIY
     CSLLPLGCWS ADSQRVVFDS VQRSRQDLFA VDTQTGSVTS LTAGGSAGSW KLLTIDRDLM
     VAQFSTPNLP PSLKVGFLPP AGKEQSVSWV SLEEAEPIPD IHWGIRVLHP PPDQENVQYA
     DLDFEAILLQ PSNSPDKSQV PMVVMPHGGP HSSFVTAWML FPAMLCKMGF AVLLVNYRGS
     TGFGQDSILS LPGNVGHQDV KDVQFAVQQV LQEEHFDARR VALMGGSHGG FLSCHLIGQY
     PETYSACIAR NPVINIVSMM GTTDIPDWCM VETGFPYSND YLPDLNVLEE MLDKSPIKYI
     PQVKTPVLLM LGQEDRRVPF KQGLEYYHAL KARNVPVRLL LYPKSTHALS EVEVESDSFM
     NTVLWLHTHL GS
//
ID   BUD13_MOUSE             Reviewed;         637 AA.
AC   Q8R149; Q8BQC0; Q8CB03;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=BUD13 homolog;
GN   Name=Bud13;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Thymus, and Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341; SER-344; SER-371;
RP   SER-373 AND SER-376, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-157; THR-170; SER-174;
RP   THR-209; SER-213; THR-222 AND SER-226, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R149-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R149-2; Sequence=VSP_025591;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the CWC26 family.
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DR   EMBL; AK037134; BAC29716.1; -; mRNA.
DR   EMBL; AK038126; BAE20531.1; -; mRNA.
DR   EMBL; AK051047; BAC34509.1; -; mRNA.
DR   EMBL; BC025490; AAH25490.1; -; mRNA.
DR   IPI; IPI00153284; -.
DR   IPI; IPI00845543; -.
DR   RefSeq; NP_666112.1; NM_146000.2.
DR   UniGene; Mm.32648; -.
DR   ProteinModelPortal; Q8R149; -.
DR   PhosphoSite; Q8R149; -.
DR   PRIDE; Q8R149; -.
DR   Ensembl; ENSMUST00000074957; ENSMUSP00000074490; ENSMUSG00000032077.
DR   GeneID; 215051; -.
DR   KEGG; mmu:215051; -.
DR   UCSC; uc009phj.1; mouse.
DR   CTD; 215051; -.
DR   MGI; MGI:2443443; Bud13.
DR   eggNOG; roNOG11564; -.
DR   GeneTree; ENSGT00390000014500; -.
DR   HOGENOM; HBG610339; -.
DR   HOVERGEN; HBG059757; -.
DR   InParanoid; Q8R149; -.
DR   OMA; RRVRHDT; -.
DR   OrthoDB; EOG40ZQZ9; -.
DR   PhylomeDB; Q8R149; -.
DR   NextBio; 374592; -.
DR   ArrayExpress; Q8R149; -.
DR   Bgee; Q8R149; -.
DR   CleanEx; MM_BUD13; -.
DR   Genevestigator; Q8R149; -.
DR   InterPro; IPR018609; Bud13.
DR   Pfam; PF09736; DUF2050; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Phosphoprotein.
FT   CHAIN         1    637       BUD13 homolog.
FT                                /FTId=PRO_0000287689.
FT   COILED      490    538       Potential.
FT   COMPBIAS    123    228       Pro-rich.
FT   MOD_RES     144    144       Phosphothreonine (By similarity).
FT   MOD_RES     148    148       Phosphoserine (By similarity).
FT   MOD_RES     157    157       Phosphothreonine.
FT   MOD_RES     161    161       Phosphoserine (By similarity).
FT   MOD_RES     170    170       Phosphothreonine.
FT   MOD_RES     174    174       Phosphoserine.
FT   MOD_RES     209    209       Phosphothreonine.
FT   MOD_RES     213    213       Phosphoserine.
FT   MOD_RES     222    222       Phosphothreonine.
FT   MOD_RES     226    226       Phosphoserine.
FT   MOD_RES     238    238       Phosphoserine (By similarity).
FT   MOD_RES     272    272       Phosphoserine (By similarity).
FT   MOD_RES     281    281       Phosphothreonine (By similarity).
FT   MOD_RES     297    297       Phosphoserine (By similarity).
FT   MOD_RES     341    341       Phosphoserine.
FT   MOD_RES     344    344       Phosphoserine.
FT   MOD_RES     371    371       Phosphoserine.
FT   MOD_RES     373    373       Phosphoserine.
FT   MOD_RES     376    376       Phosphoserine.
FT   MOD_RES     512    512       Phosphotyrosine (By similarity).
FT   VAR_SEQ     608    637       Missing (in isoform 2).
FT                                /FTId=VSP_025591.
FT   CONFLICT    174    174       S -> Y (in Ref. 1; BAC34509).
FT   CONFLICT    189    189       P -> H (in Ref. 1; BAC34509).
SQ   SEQUENCE   637 AA;  72139 MW;  CA381776034D1A89 CRC64;
     MAAAPPLTKA EYLKRYLSGT DAGLEGGPEA GRKRRKKRPK PGGAGGKGMR IVDDDVGWAA
     ISTAKPEKEE EEDGDLPVVA EFVDERPEEV KQMEAFRSSA KWKLLGGHGE DGHFHHDDQD
     SSPPRRVRHD TPDTSPPRKA RHDTPDPSPP RKARHDTPDT SPPRKARHDT PDPSPPRKAR
     HDTPDPSPPR RVRHDTPDLS PPRRVRHDTP DLSPPRRVRH DTPDPSPPRR VRHDLDASPP
     RKSHRNSSAV SPRRGHHGSL GTSSPRQTHN HSPTAAQHRR TLDSSGTQHL RRAHHESPDL
     ELHKAKSSKA AERAPSKAAS QSGLGPSHPS LSTNSKYEHD SDLSPPRKRQ AKAHFEAKKQ
     LDSKGVYQKA SDSDLSPPRK KKNSGHQDSD SDLSPPRNRP RRQSSDSDLS PPRRRQRTKS
     SDSDLSPPRR SPRPGKKTAH MYSGAKTGLV TDVQREHQEL KKQDQDTTDL GAQFEFTETV
     FRDKSGRKRN LKLERLEQRR KAEKDSERDE LYAQWGKGLA QSRQQQQNVE DAMKEMQKPL
     ARYIDDEDLD RMLREQEREG DPMANFIKKN KAKENKNKKV KPRYSGPAPP PNRFNIWPGY
     RWDGVDRSNG FEQKRFARLA SKKAVEELAY KWSVEDM
//
ID   ERO1A_MOUSE             Reviewed;         464 AA.
AC   Q8R180; Q9CV47; Q9QY03;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=ERO1-like protein alpha;
DE            Short=ERO1-L;
DE            Short=ERO1-L-alpha;
DE            EC=1.8.4.-;
DE   AltName: Full=Endoplasmic oxidoreductin-1-like protein;
DE   AltName: Full=Oxidoreductin-1-L-alpha;
DE   Flags: Precursor;
GN   Name=Ero1l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20138221; PubMed=10671517; DOI=10.1074/jbc.275.7.4827;
RA   Cabibbo A., Pagani M., Fabbri M., Rocchi M., Farmery M.R.,
RA   Bulleid N.J., Sitia R.;
RT   "ERO1-L, a human protein that favors disulfide bond formation in the
RT   endoplasmic reticulum.";
RL   J. Biol. Chem. 275:4827-4833(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 232-464.
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   INDUCTION.
RX   PubMed=12752442; DOI=10.1046/j.1432-1033.2003.03590.x;
RA   Gess B., Hofbauer K.H., Wenger R.H., Lohaus C., Meyer H.E., Kurtz A.;
RT   "The cellular oxygen tension regulates expression of the endoplasmic
RT   oxidoreductase ERO1-Lalpha.";
RL   Eur. J. Biochem. 270:2228-2235(2003).
CC   -!- FUNCTION: Essential oxidoreductase that oxidizes proteins in the
CC       endoplasmic reticulum to produce disulfide bonds. Acts by
CC       oxidizing directly P4HB/PDI isomerase through a direct disulfide
CC       exchange. Does not act as a direct oxidant of folding substrate,
CC       but relies on P4HB/PDI to transfer oxidizing equivalent.
CC       Associates with ERP44 but not with GRP54, demonstrating that it
CC       does not oxidize all PDI related proteins and can discriminate
CC       between PDI and related proteins. Its reoxidation probably
CC       involves electron transfer to molecular oxygen via FAD. Acts
CC       independently of glutathione. May be responsible for a significant
CC       proportion of reactive oxygen species (ROS) in the cell, thereby
CC       being a source of oxidative stress. Required for the folding of
CC       immunoglobulin proteins (By similarity).
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- ENZYME REGULATION: Enzyme activity is tighly regulated to prevent
CC       the accumulation of reactive oxygen species in the endoplasmic
CC       reticulum. Reversibly down-regulated by the formation of disulfide
CC       bonds between the active site Cys-94 and Cys-130, and between Cys-
CC       99 and Cys-104. Glutathione may be required to regulate its
CC       activity in the endoplasmic reticulum (By similarity).
CC   -!- SUBUNIT: Predominantly monomer. May function both as a monomer and
CC       a homodimer. Interacts with PDILT (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein; Lumenal side (By similarity). Note=The
CC       association with ERP44 is essential for its retention in the
CC       endoplasmic reticulum (By similarity).
CC   -!- INDUCTION: Stimulated by hypoxia; suggesting that it is regulated
CC       via the HIF-pathway.
CC   -!- PTM: N-glycosylated (By similarity).
CC   -!- PTM: The Cys-94/Cys-99 and Cys-390/Cys-393 disulfide bonds
CC       constitute the redox-active center. The Cys-94/Cys-99 disulfide
CC       bond may accept electron from P4HB and funnel them to the active
CC       site disulfide Cys-390/Cys-393 (By similarity).
CC   -!- SIMILARITY: Belongs to the EROs family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF144695; AAF20364.1; -; mRNA.
DR   EMBL; BC025102; AAH25102.1; -; mRNA.
DR   EMBL; AK009667; BAB26428.1; -; mRNA.
DR   IPI; IPI00754386; -.
DR   RefSeq; NP_056589.1; NM_015774.2.
DR   UniGene; Mm.387108; -.
DR   ProteinModelPortal; Q8R180; -.
DR   SMR; Q8R180; 49-463.
DR   STRING; Q8R180; -.
DR   PhosphoSite; Q8R180; -.
DR   PRIDE; Q8R180; -.
DR   Ensembl; ENSMUST00000022378; ENSMUSP00000022378; ENSMUSG00000021831.
DR   GeneID; 50527; -.
DR   KEGG; mmu:50527; -.
DR   CTD; 50527; -.
DR   MGI; MGI:1354385; Ero1l.
DR   GeneTree; ENSGT00390000007753; -.
DR   HOGENOM; HBG521237; -.
DR   HOVERGEN; HBG051507; -.
DR   InParanoid; Q8R180; -.
DR   OMA; DDIQSPD; -.
DR   OrthoDB; EOG4T7833; -.
DR   NextBio; 307530; -.
DR   ArrayExpress; Q8R180; -.
DR   Bgee; Q8R180; -.
DR   CleanEx; MM_ERO1L; -.
DR   Genevestigator; Q8R180; -.
DR   GermOnline; ENSMUSG00000021831; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IEA:InterPro.
DR   GO; GO:0050873; P:brown fat cell differentiation; IDA:MGI.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IDA:MGI.
DR   GO; GO:0006467; P:protein thiol-disulfide exchange; IEA:InterPro.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR007266; ER_oxidoreductin-1.
DR   PANTHER; PTHR12613; ERO1; 1.
DR   Pfam; PF04137; ERO1; 1.
DR   PIRSF; PIRSF017205; ERO1; 1.
DR   SUPFAM; SSF110019; ERO1; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Electron transport; Endoplasmic reticulum; FAD;
KW   Flavoprotein; Glycoprotein; Membrane; Oxidoreductase;
KW   Redox-active center; Signal; Transport.
FT   SIGNAL        1     23       Potential.
FT   CHAIN        24    464       ERO1-like protein alpha.
FT                                /FTId=PRO_0000008416.
FT   BINDING     186    186       FAD (By similarity).
FT   BINDING     188    188       FAD (By similarity).
FT   BINDING     199    199       FAD (By similarity).
FT   BINDING     248    248       FAD (By similarity).
FT   BINDING     251    251       FAD (By similarity).
FT   BINDING     283    283       FAD (By similarity).
FT   CARBOHYD    276    276       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    380    380       N-linked (GlcNAc...) (Potential).
FT   DISULFID     35     46       Or C-35 with C-48 (By similarity).
FT   DISULFID     37     48       Or C-35 with C-46 (By similarity).
FT   DISULFID     85    387       By similarity.
FT   DISULFID     94    130       Alternate.
FT   DISULFID     94     99       Redox-active (By similarity).
FT   DISULFID     99    104       Alternate (By similarity).
FT   DISULFID    207    237       By similarity.
FT   DISULFID    390    393       Redox-active (By similarity).
FT   CONFLICT    130    130       C -> G (in Ref. 2; AAH25102).
SQ   SEQUENCE   464 AA;  54084 MW;  FED19B00E1FBD2A1 CRC64;
     MGRAWGLLVG LLGVVWLLRL GHGEERRPET AAQRCFCQVS GYLDDCTCDV ETIDKFNNYR
     LFPRLQKLLE SDYFRYYKVN LKKPCPFWND INQCGRRDCA VKPCHSDEVP DGIKSASYKY
     SEEANRIEEC EQAERLGAVD ESLSEETQKA VLQWTKHDDS SDSFCEIDDI QSPDAEYVDL
     LLNPERYTGY KGPDAWRIWS VIYEENCFKP QTIQRPLASG RGKSKENTFY NWLEGLCVEK
     RAFYRLISGL HASINVHLSA RYLLQDTWLE KKWGHNVTEF QQRFDGILTE GEGPRRLRNL
     YFLYLIELRA LSKVLPFFER PDFQLFTGNK VQDAENKALL LEILHEIKSF PLHFDENSFF
     AGDKNEAHKL KEDFRLHFRN ISRIMDCVGC FKCRLWGKLQ TQGLGTALKI LFSEKLIANM
     PESGPSYEFQ LTRQEIVSLF NAFGRISTSV RELENFRHLL QNVH
//
ID   SNG3_MOUSE              Reviewed;         229 AA.
AC   Q8R191; Q9WVG8;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Synaptogyrin-3;
GN   Name=Syngr3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99315823; PubMed=10383386; DOI=10.1074/jbc.274.27.18893;
RA   Sugita S., Janz R., Suedhof T.C.;
RT   "Synaptogyrins regulate Ca2+-dependent exocytosis in PC12 cells.";
RL   J. Biol. Chem. 274:18893-18901(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 11-22; 92-99 AND 133-147, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=14755516; DOI=10.1002/cne.20008;
RA   Belizaire R., Komanduri C., Wooten K., Chen M., Thaller C., Janz R.;
RT   "Characterization of synaptogyrin 3 as a new synaptic vesicle
RT   protein.";
RL   J. Comp. Neurol. 470:266-281(2004).
RN   [6]
RP   FUNCTION, INTERACTION WITH SLC6A3, TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=19357284; DOI=10.1523/JNEUROSCI.4559-08.2009;
RA   Egana L.A., Cuevas R.A., Baust T.B., Parra L.A., Leak R.K.,
RA   Hochendoner S., Pena K., Quiroz M., Hong W.C., Dorostkar M.M.,
RA   Janz R., Sitte H.H., Torres G.E.;
RT   "Physical and functional interaction between the dopamine transporter
RT   and the synaptic vesicle protein synaptogyrin-3.";
RL   J. Neurosci. 29:4592-4604(2009).
CC   -!- FUNCTION: Involved in the positive regulation of dopamine
CC       transporter activity. Probably facilitates the physical and
CC       functional interactions of the transporter with the dopamine
CC       vesicular storage system, allowing a more efficient loading of the
CC       vesicles with extracellular dopamine after release.
CC   -!- SUBUNIT: Interacts (via N-terminus) with SLC6A3 (via N-terminus).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC       Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. Cell
CC       junction, synapse. Note=Found at the neuromuscular synapses.
CC   -!- TISSUE SPECIFICITY: Found in the brain across the dorsal and
CC       ventral corpus striatum as well as in the cortex.
CC   -!- SIMILARITY: Belongs to the synaptogyrin family.
CC   -!- SIMILARITY: Contains 1 MARVEL domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF117207; AAD28556.1; -; mRNA.
DR   EMBL; AK048753; BAC33444.1; -; mRNA.
DR   EMBL; AK081164; BAC38151.1; -; mRNA.
DR   EMBL; AK082167; BAC38430.1; -; mRNA.
DR   EMBL; BC025022; AAH25022.1; -; mRNA.
DR   IPI; IPI00331579; -.
DR   RefSeq; NP_035652.2; NM_011522.3.
DR   UniGene; Mm.26032; -.
DR   ProteinModelPortal; Q8R191; -.
DR   STRING; Q8R191; -.
DR   PhosphoSite; Q8R191; -.
DR   PRIDE; Q8R191; -.
DR   Ensembl; ENSMUST00000007236; ENSMUSP00000007236; ENSMUSG00000007021.
DR   GeneID; 20974; -.
DR   KEGG; mmu:20974; -.
DR   UCSC; uc008axq.1; mouse.
DR   CTD; 20974; -.
DR   MGI; MGI:1341881; Syngr3.
DR   eggNOG; roNOG04160; -.
DR   GeneTree; ENSGT00510000046450; -.
DR   HOGENOM; HBG446580; -.
DR   HOVERGEN; HBG000896; -.
DR   InParanoid; Q8R191; -.
DR   OMA; SILSWVA; -.
DR   OrthoDB; EOG43JC5R; -.
DR   PhylomeDB; Q8R191; -.
DR   NextBio; 299952; -.
DR   ArrayExpress; Q8R191; -.
DR   Bgee; Q8R191; -.
DR   CleanEx; MM_SYNGR3; -.
DR   Genevestigator; Q8R191; -.
DR   GermOnline; ENSMUSG00000007021; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:UniProtKB.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
DR   GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR   GO; GO:0042169; F:SH2 domain binding; IDA:MGI.
DR   GO; GO:0032411; P:positive regulation of transporter activity; IMP:UniProtKB.
DR   InterPro; IPR008253; Marvel.
DR   InterPro; IPR021128; MARVEL-like_dom.
DR   InterPro; IPR016579; Synaptogyrin.
DR   Pfam; PF01284; MARVEL; 1.
DR   PIRSF; PIRSF011282; Synaptogyrin; 1.
DR   PROSITE; PS51225; MARVEL; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cytoplasmic vesicle; Direct protein sequencing;
KW   Membrane; Synapse; Transmembrane; Transmembrane helix.
FT   CHAIN         1    229       Synaptogyrin-3.
FT                                /FTId=PRO_0000183997.
FT   TRANSMEM     30     50       Helical; (Potential).
FT   TRANSMEM     70     90       Helical; (Potential).
FT   TRANSMEM    105    125       Helical; (Potential).
FT   TRANSMEM    148    168       Helical; (Potential).
FT   DOMAIN       20    172       MARVEL.
FT   CONFLICT    171    171       F -> L (in Ref. 1; AAD28556).
SQ   SEQUENCE   229 AA;  24561 MW;  E04C00555B8A3C08 CRC64;
     MEGASFGAGR AGAAFDPVSF ARRPQTLLRV VSWVFSIAVF GPIVNEGYVN SDSGPELRCV
     FNGNAGACRF GVVLGLGAFI ACVAFLLLDV RFQQISSVRD RRRAVLLDLG FSGVWSFLWF
     VGFCFLTNQW QRTTPGPGTA QAGDAARAAI AFSFFSILSW VALTVKALQR FRLGTDMSLF
     ATDQLGTGAA QAYPGYPVGS GVEGTETYQS PPFTETLDTS SKGYQVPAY
//
ID   DOCK7_MOUSE             Reviewed;        2130 AA.
AC   Q8R1A4; Q45V78; Q5PRE6; Q6PJ17; Q9CSB6; Q9CXM7;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Dedicator of cytokinesis protein 7;
GN   Name=Dock7; Synonyms=Gm430, Kiaa1771;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 109-587.
RC   STRAIN=BALB/c;
RA   Yamauchi J., Miyamoto Y., Takashima S., Tanoue A.;
RT   "Characterization of a novel GEF Dock7.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 811-2130 (ISOFORM 2).
RC   STRAIN=C57BL/6, FVB/N, and NMRI; TISSUE=Head, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1404-2130 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1856-2130 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Embryonic head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-900; SER-963; THR-965
RP   AND SER-1422, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439 AND SER-440, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1422 AND SER-1428, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Functions as a guanine nucleotide exchange factor (GEF),
CC       which activates Rac1 and Rac3 Rho small GTPases by exchanging
CC       bound GDP for free GTP. Does not have a GEF activity for CDC42.
CC       Required for STMN1 'Ser-15' phosphorylation during axon formation
CC       and consequently for neuronal polarization (By similarity).
CC   -!- SUBUNIT: Interacts with TSC1. Interacts with nucleotide-free RAC1
CC       and RAC3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell projection, axon (By similarity).
CC       Note=Enriched in the developing axons of hippocampal neurons (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R1A4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R1A4-2; Sequence=VSP_007708;
CC   -!- DOMAIN: The DHR-2 domain mediates GEF activity (By similarity).
CC   -!- SIMILARITY: Belongs to the DOCK family.
CC   -!- SIMILARITY: Contains 1 DHR-1 (CZH-1) domain.
CC   -!- SIMILARITY: Contains 1 DHR-2 (CZH-2) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH24823.2; Type=Erroneous initiation;
CC       Sequence=AAH86672.1; Type=Erroneous initiation;
CC       Sequence=BAB28798.3; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AL627349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL935325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DQ109674; AAZ17650.1; -; mRNA.
DR   EMBL; BC024823; AAH24823.2; ALT_INIT; mRNA.
DR   EMBL; BC024917; AAH24917.3; -; mRNA.
DR   EMBL; BC086672; AAH86672.1; ALT_INIT; mRNA.
DR   EMBL; AK122554; BAC65836.1; -; mRNA.
DR   EMBL; AK013336; BAB28798.3; ALT_INIT; mRNA.
DR   EMBL; AK014226; BAB29215.1; -; mRNA.
DR   IPI; IPI00339428; -.
DR   IPI; IPI00816914; -.
DR   RefSeq; NP_080358.3; NM_026082.4.
DR   UniGene; Mm.260623; -.
DR   ProteinModelPortal; Q8R1A4; -.
DR   SMR; Q8R1A4; 561-729, 1672-2103.
DR   PhosphoSite; Q8R1A4; -.
DR   PRIDE; Q8R1A4; -.
DR   Ensembl; ENSMUST00000030286; ENSMUSP00000030286; ENSMUSG00000028556.
DR   Ensembl; ENSMUST00000107015; ENSMUSP00000102629; ENSMUSG00000028556.
DR   GeneID; 67299; -.
DR   KEGG; mmu:67299; -.
DR   UCSC; uc008tup.1; mouse.
DR   UCSC; uc008tuq.1; mouse.
DR   CTD; 67299; -.
DR   MGI; MGI:1914549; Dock7.
DR   GeneTree; ENSGT00560000076710; -.
DR   HOGENOM; HBG446229; -.
DR   HOVERGEN; HBG051390; -.
DR   InParanoid; Q8R1A4; -.
DR   OrthoDB; EOG4Q2DDM; -.
DR   NextBio; 324164; -.
DR   ArrayExpress; Q8R1A4; -.
DR   Bgee; Q8R1A4; -.
DR   CleanEx; MM_DOCK7; -.
DR   Genevestigator; Q8R1A4; -.
DR   GermOnline; ENSMUSG00000028556; Mus musculus.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0048365; F:Rac GTPase binding; IDA:BHF-UCL.
DR   GO; GO:0043473; P:pigmentation; IMP:MGI.
DR   InterPro; IPR010703; DOCK.
DR   InterPro; IPR021816; DUF3398.
DR   Pfam; PF06920; Ded_cyto; 1.
DR   Pfam; PF11878; DUF3398; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell projection; Coiled coil;
KW   Developmental protein; Differentiation;
KW   Guanine-nucleotide releasing factor; Neurogenesis; Phosphoprotein.
FT   CHAIN         1   2130       Dedicator of cytokinesis protein 7.
FT                                /FTId=PRO_0000189996.
FT   DOMAIN      561    799       DHR-1.
FT   DOMAIN     1570   2093       DHR-2.
FT   COILED      365    395       Potential.
FT   COILED     2076   2102       Potential.
FT   MOD_RES      28     28       Phosphoserine (By similarity).
FT   MOD_RES      30     30       Phosphoserine (By similarity).
FT   MOD_RES     180    180       Phosphoserine (By similarity).
FT   MOD_RES     182    182       Phosphoserine (By similarity).
FT   MOD_RES     439    439       Phosphoserine.
FT   MOD_RES     440    440       Phosphoserine.
FT   MOD_RES     882    882       Phosphoserine (By similarity).
FT   MOD_RES     888    888       Phosphoserine (By similarity).
FT   MOD_RES     894    894       Phosphoserine (By similarity).
FT   MOD_RES     896    896       Phosphoserine (By similarity).
FT   MOD_RES     898    898       Phosphoserine (By similarity).
FT   MOD_RES     900    900       Phosphoserine.
FT   MOD_RES     905    905       Phosphoserine (By similarity).
FT   MOD_RES     907    907       Phosphothreonine (By similarity).
FT   MOD_RES     909    909       Phosphothreonine (By similarity).
FT   MOD_RES     910    910       Phosphoserine (By similarity).
FT   MOD_RES     929    929       Phosphoserine (By similarity).
FT   MOD_RES     963    963       Phosphoserine.
FT   MOD_RES     965    965       Phosphothreonine.
FT   MOD_RES    1382   1382       Phosphoserine (By similarity).
FT   MOD_RES    1384   1384       Phosphothreonine (By similarity).
FT   MOD_RES    1420   1420       Phosphoserine (By similarity).
FT   MOD_RES    1422   1422       Phosphoserine.
FT   MOD_RES    1428   1428       Phosphoserine.
FT   MOD_RES    1952   1952       N6-acetyllysine (By similarity).
FT   VAR_SEQ    1822   1826       STGWE -> DGK (in isoform 2).
FT                                /FTId=VSP_007708.
SQ   SEQUENCE   2130 AA;  241438 MW;  936B564638C1FC1D CRC64;
     MAERRAFAQK ISRTVAAEVR KQISGQYSGS PQLLKNLNIV GNISHHTTVP LTEAVDPVDL
     EDYLVTHPLS GDSGPLRDLV EFPPDDIEVV YSPRDCRTLV SAVPEESEMD PHVRDCIRSY
     TEDWAVVVRK YHKLGTGFNP NTLDKQKERQ KGLPRQVFES DEAPDGSSYQ DEQDDLKRRS
     MSIDDTPRGS WACSIFDLKN SLPDALLPNL LDRTPNEEID HQNDDQRKSN RHKELFALHP
     SPDEEEPIER LSVPDVPKEH FGQRLLVKCL SLKFEIEIEP IFASLALYDV KEKKKISENF
     YFDLNSEQMK GLLRPHVPPA AITTLARSAI FSITYPSQDV FLVIKLEKVL QQGDIGECAE
     PYMIFKEADA TKNKEKLEKL KSQADQFCQR LGKYRMPFAW TAIHLMNIVS SAGSLERDST
     EVEISTGERK GSWSERRNSS LVGRRSLERT TSGDDACNLT SFRPATLTVA NFFKQEGDRL
     SDEDLYKFLA DMRRPSSVLR RLRPITAQLK IDISPAPENP HYCLTPELLQ VKLYPDSRVR
     PTREILEFPA RDVYVPNTTY RNLLYIYPQS LNFANRQGSA RNITVKVQFM YGEDPSNAMP
     VIFGKSSCSE FSKEAYTAVV YHNRSPDFHE EIKVKLPATL TDHHHLLFTF YHVSCQQKQN
     TPLETPVGYT WIPMLQNGRL KTGQFCLPVS LEKPPQAYSV LSPEVPLPGM KWVDNHKGVF
     NVEVVAVSSI HTQDPYLDKF FALVNALDEH MFPVRIGDMR IMENNLESEL KSSISALNSS
     QLEPVVRFLH LLLDKLILLV VRPPVIAGQI VNLGQASFEA MASIINRLHK NLEGNHDQHG
     RNNLLASYIY YVFRLPNTYP NSPSPGPGGL GGSVHYATMA RSAVRPASLN LNRSRSLSNS
     NPDISGTPTS PDDEVRSIIG SKGLDRSNSW VNTGPKAAPW GSNPSPSAES TQAMDRSCNR
     MSSHTETSSF LQTLTGRLPT KKLFHEELAL QWVVCSGSVR ESALQQAWFF FELMVKSMVH
     HLYFNDKLDA PRESRFPERF MDDIAALVST IAGDVVSRFQ KDTEMVERLN TSLAFFLNDL
     LSVMDRGFVF SLIKSCYKQV SAKLYSLPNP SVLVSLRLDF LRIICSHEHY VTLNLPCSLL
     TPPASPSPSV SSATSQSSGF STSVQDQKIA NMFELSLPFR QQHYLAGLVL TELALILDPD
     AEGLFGLHKK VINMVHNLLS THDSDPRYSD PQIKARVAML YLPLIGIIME TVPQLYDFTE
     SHNQRGRPIC IAPDDYDSES GSMISQTVAM AIAGTSVPQL TRPGSFLLTS TSGRQHTTFS
     AESSRSLLIC LLWVLKNADE TVLQKWFTDL SVLQLNRLLD LLYLCVSCFE YKGKKVFERM
     NSLTFKKSKD MRAKLEEAIL GSIGARQEMV RRSRGQLERS PSGSAFGSQE NLRWRKDMTH
     WRQNSEKLDK SRAEIEHEAL IDGNLATEAN LIILDTLEII VQTVSVTESK ESILGGVLKV
     LLQSMACNQS AVYLQHCFAT QRALVSKFPE LLFEEETEQC ADLCLRLLRH CSSSISTIRS
     HASASLYLLM RQNFEIGNNF ARVKMQVTMS LSSLVGTSQN FNEEFLRRSL KTILTYAEED
     LELRETTFPD QVQDLVFNLH MILSDTVKMK EHQEDPEMLI DLMYRIAKGY QTSPDLRLTW
     LQNMAGKHSE RSNHAEAAQC LVHSAALVAE YLSMLEDRKY LPVGCVTFQN ISSNVLEESA
     VSDDVVSPDE EGICSGKYFT ESGLVGLLEQ AAASFSMAGM YEAVNEVYKV LIPIHEANRD
     AKKLSTIHGK LQEAFSKIVH QSTGWERMFG TYFRVGFYGT KFGDLDEQEF VYKEPAITKL
     AEISHRLEGF YGERFGEDVL EVIKDSNPVD KCKLDPNKAY IQITYVEPFF DTYEMKDRIT
     YFDKNYNLRR FMYCTPFTLD GRAHGELHEQ FKRKTILTTS HAFPYIKTRV NVTHKEEIIL
     TPIEVAIEDM QKKTQELAFA THQDPADPKM LQMVLQGSVG TTVNQGPLEV AQVFLSEIPG
     DPKLFRHHNK LRLCFKDFTK RCEDALRKNK SLIGPDQKEY QRELERNYHR LKEALQPLIN
     RKIPQLYKAV LPVTCHRDSF SRMSLRKMEL
//
ID   STAC2_MOUSE             Reviewed;         408 AA.
AC   Q8R1B0; Q8BV93; Q8K2U4;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=SH3 and cysteine-rich domain-containing protein 2;
DE   AltName: Full=24b2/STAC2;
DE   AltName: Full=Src homology 3 and cysteine-rich domain-containing protein 2;
GN   Name=Stac2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Rossner M., Faucheron N., Wuerz R., von Ahsen O., Kammandel B.,
RA   Schwaninger M., Schneider A.;
RT   "Cloning of 24b2/STAC2, a novel STAC-homologous gene up-regulated in
RT   cerebral ischemia in mice.";
RL   Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain cortex, Cerebellum, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- MISCELLANEOUS: Up-regulated in cerebral ischemia.
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; AJ608761; CAE75538.1; -; mRNA.
DR   EMBL; AK078132; BAC37142.1; -; mRNA.
DR   EMBL; AK079357; BAC37621.1; -; mRNA.
DR   EMBL; AK144433; BAE25886.1; -; mRNA.
DR   EMBL; BC024864; AAH24864.1; -; mRNA.
DR   EMBL; BC029794; AAH29794.1; -; mRNA.
DR   IPI; IPI00153337; -.
DR   RefSeq; NP_666140.1; NM_146028.4.
DR   UniGene; Mm.181008; -.
DR   HSSP; P43603; 1OOT.
DR   ProteinModelPortal; Q8R1B0; -.
DR   SMR; Q8R1B0; 106-165, 293-346, 353-408.
DR   PRIDE; Q8R1B0; -.
DR   Ensembl; ENSMUST00000017544; ENSMUSP00000017544; ENSMUSG00000017400.
DR   GeneID; 217154; -.
DR   KEGG; mmu:217154; -.
DR   UCSC; uc007lfl.1; mouse.
DR   CTD; 217154; -.
DR   MGI; MGI:2144518; Stac2.
DR   GeneTree; ENSGT00390000008822; -.
DR   HOGENOM; HBG716103; -.
DR   HOVERGEN; HBG017859; -.
DR   InParanoid; Q8R1B0; -.
DR   OMA; NQICVGV; -.
DR   OrthoDB; EOG4RR6HZ; -.
DR   PhylomeDB; Q8R1B0; -.
DR   NextBio; 375613; -.
DR   ArrayExpress; Q8R1B0; -.
DR   Bgee; Q8R1B0; -.
DR   CleanEx; MM_STAC2; -.
DR   Genevestigator; Q8R1B0; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR000108; p67phox.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR00499; P67PHOX.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; SH3 domain; Zinc; Zinc-finger.
FT   CHAIN         1    408       SH3 and cysteine-rich domain-containing
FT                                protein 2.
FT                                /FTId=PRO_0000274414.
FT   DOMAIN      289    348       SH3.
FT   ZN_FING     110    161       Phorbol-ester/DAG-type.
FT   COMPBIAS     70    107       Pro-rich.
FT   CONFLICT     93     93       P -> S (in Ref. 1; BAC37621).
FT   CONFLICT    181    181       A -> E (in Ref. 2; AAH29794).
SQ   SEQUENCE   408 AA;  44793 MW;  58D275A654EE4CCA CRC64;
     MTEMSEKENE PDDAATHTPP GTVSTLQETK LQRFKRSLSL KTILRSKSVE NFFLRSGSEL
     KCPTEVLLTP PTPLPPPSPP PASTDRGLPT PTPSPCPVPR PLAPLKPVRL HSFQEHVFKR
     ASPCELCHQL IVGNSKQGLR CKTCKVSVHL WCSEEISHQQ CPGKTSTSFR RNFSSPLLVH
     APPPACAMNK ESPPTGTSGK VDPVYETLRY GTSLALMNRS SFSSTSESPT RSLSERDELT
     EDGEGSIRSS EEGPGDSVFT APAESEGSGP EEKSPGQQPP KLPLRKDVGP MYSYVALYKF
     LPQENNDLAL QPGDRIMLVD DSNEDWWKGK IGDRVGFFPA NFVQRVRPGE NVWRCCQPFS
     GNKEQGYMSL KENQICVGVS RSKDSDGFIR VSSGKKRGLV PADSLAEI
//
ID   EIF3C_MOUSE             Reviewed;         911 AA.
AC   Q8R1B4; Q8R3M7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit C;
DE            Short=eIF3c;
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 8;
DE   AltName: Full=eIF3 p110;
GN   Name=Eif3c; Synonyms=Eif3s8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   CHARACTERIZATION OF THE EIF-3 COMPLEX, IDENTIFICATION IN THE EIF-3
RP   COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17581632; DOI=10.1038/sj.emboj.7601765;
RA   Masutani M., Sonenberg N., Yokoyama S., Imataka H.;
RT   "Reconstitution reveals the functional core of mammalian eIF3.";
RL   EMBO J. 26:3373-3383(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178; SER-181 AND
RP   SER-182, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Component of the eukaryotic translation initiation
CC       factor 3 (eIF-3) complex, which is required for several steps in
CC       the initiation of protein synthesis. The eIF-3 complex associates
CC       with the 40S ribosome and facilitates the recruitment of eIF-1,
CC       eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S
CC       preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA
CC       recruitment to the 43S PIC and scanning of the mRNA for AUG
CC       recognition. The eIF-3 complex is also required for disassembly
CC       and recycling of posttermination ribosomal complexes and
CC       subsequently prevents premature joining of the 40S and 60S
CC       ribosomal subunits prior to initiation.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor
CC       3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B,
CC       EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K,
CC       EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable
CC       modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I;
CC       module B is composed of EIF3F, EIF3H, and EIF3M; and module C is
CC       composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module
CC       C binds EIF3B of module A and EIF3H of module B, thereby linking
CC       the three modules. EIF3J is a labile subunit that binds to the
CC       eIF-3 complex via EIF3B. The eIF-3 complex may interact with
CC       RPS6KB1 under conditions of nutrient depletion. Mitogenic
CC       stimulation may lead to binding and activation of a complex
CC       composed of MTOR and RPTOR, leading to phosphorylation and release
CC       of RPS6KB1 and binding of EIF4B to eIF-3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
CC       stimulation (By similarity).
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit C family.
CC   -!- SIMILARITY: Contains 1 PCI domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK160078; BAE35610.1; -; mRNA.
DR   EMBL; BC024855; AAH24855.1; -; mRNA.
DR   EMBL; BC025032; AAH25032.1; -; mRNA.
DR   IPI; IPI00321647; -.
DR   RefSeq; NP_666312.1; NM_146200.1.
DR   UniGene; Mm.22776; -.
DR   ProteinModelPortal; Q8R1B4; -.
DR   SMR; Q8R1B4; 774-847.
DR   MINT; MINT-4608642; -.
DR   STRING; Q8R1B4; -.
DR   PhosphoSite; Q8R1B4; -.
DR   PRIDE; Q8R1B4; -.
DR   Ensembl; ENSMUST00000032992; ENSMUSP00000032992; ENSMUSG00000030738.
DR   GeneID; 56347; -.
DR   KEGG; mmu:56347; -.
DR   NMPDR; fig|10090.3.peg.17626; -.
DR   UCSC; uc009jrw.1; mouse.
DR   CTD; 56347; -.
DR   MGI; MGI:1926966; Eif3c.
DR   HOGENOM; HBG608917; -.
DR   HOVERGEN; HBG035174; -.
DR   InParanoid; Q8R1B4; -.
DR   OMA; TEEICRI; -.
DR   OrthoDB; EOG4NVZJQ; -.
DR   PhylomeDB; Q8R1B4; -.
DR   NextBio; 312336; -.
DR   ArrayExpress; Q8R1B4; -.
DR   Bgee; Q8R1B4; -.
DR   Genevestigator; Q8R1B4; -.
DR   GermOnline; ENSMUSG00000030738; Mus musculus.
DR   GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
DR   GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB.
DR   InterPro; IPR008905; eIF3c_N.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF05470; eIF-3c_N; 2.
DR   Pfam; PF01399; PCI; 1.
DR   SMART; SM00088; PINT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Initiation factor; Phosphoprotein;
KW   Protein biosynthesis.
FT   CHAIN         1    911       Eukaryotic translation initiation factor
FT                                3 subunit C.
FT                                /FTId=PRO_0000259425.
FT   DOMAIN      710    844       PCI.
FT   COMPBIAS    164    189       Asp/Glu-rich (acidic).
FT   COMPBIAS    241    244       Poly-Glu.
FT   COMPBIAS    289    292       Poly-Glu.
FT   MOD_RES       6      6       Phosphothreonine (By similarity).
FT   MOD_RES       9      9       Phosphoserine (By similarity).
FT   MOD_RES      11     11       Phosphoserine (By similarity).
FT   MOD_RES      13     13       Phosphoserine (By similarity).
FT   MOD_RES      15     15       Phosphoserine (By similarity).
FT   MOD_RES      16     16       Phosphoserine (By similarity).
FT   MOD_RES      18     18       Phosphoserine (By similarity).
FT   MOD_RES      39     39       Phosphoserine.
FT   MOD_RES      95     95       Phosphoserine (By similarity).
FT   MOD_RES     166    166       Phosphoserine.
FT   MOD_RES     178    178       Phosphoserine.
FT   MOD_RES     181    181       Phosphoserine.
FT   MOD_RES     182    182       Phosphoserine.
FT   MOD_RES     522    522       Phosphothreonine (By similarity).
FT   MOD_RES     556    556       N6-acetyllysine (By similarity).
FT   MOD_RES     907    907       Phosphoserine (By similarity).
FT   CONFLICT    111    111       A -> T (in Ref. 2; AAH25032).
FT   CONFLICT    894    894       E -> L (in Ref. 2; AAH25032).
SQ   SEQUENCE   911 AA;  105531 MW;  A88282C5B4C55AEB CRC64;
     MSRFFTTGSD SESESSLSGE ELVTKPVSGN YGKQPLLLSE DEEDTKRVVR SAKDKRFEEL
     TNLIRTIRNA MKIRDVTKCL EEFELLGKAY GKAKSIVDKE GVPRFYIRIL ADLEDYLNEL
     WEDKEGKKKM NKNNAKALST LRQKIRKYNR DFESHITNYK QNPEQSADED AEKNEEDSEG
     SSDEDEDEDG VGNTTFLKKK QESSGESRKF HKKMEDDDED SEDSEDEEWD TSSTSSDSDS
     EEEEGKQTVL ASKFLKKAPT TEEDKKAAEK KREDKAKKKH DRKSKRLDEE EEDNEGGEWE
     RVRGGVPLVK EKPKMFAKGT EITHAVVIKK LNEILQVRGK KGTDRATQIE LLQLLVQIAA
     ENNLGVGVIV KIKFNIIASL YDYNPNLATY MKPEMWQMCL DCINELMDTL VAHSNIFVGE
     NILEESENLH NFDQPLRVRG CILTLVERMD EEFTKIMQNT DPHSQEYVEH LKDEAQVCAI
     IERVQRYLEE KGTTEEICQI YLRRILHTYY KFDYKAHQRQ LTPPEGSSKS EQDQAENEGE
     DSAVLMERLC KYIYAKDRTD RIRTCAILCH IYHHALHSRW YQARDLMLMS HLQDNIQHAD
     PPVQILYNRT MVQLGICAFR QGLTKDAHNA LLDIQSSGRA KELLGQGLLL RSLQERNQEQ
     EKVERRRQVP FHLHINLELL ECVYLVSAML LEIPYMAAHE SDARRRMISK QFHHQLRVGE
     RQPLLGPPES MREHVVAASK AMKMGDWKTC HSFIINEKMN GKVWDLFPEA DKVRTMLVRK
     IQEESLRTYL FTYSSVYDSI SMETLSDMFE LDLPTVHSII SKMIINEELM ASLDQPTQTV
     VMHRTEPTAQ QNLALQLAEK LGSLVENNER VFDHKQGTYG GYFRDQKDGY RKNEGYMRRG
     GYRQQQSQTA Y
//
ID   KCNC4_MOUSE             Reviewed;         628 AA.
AC   Q8R1C0;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Potassium voltage-gated channel subfamily C member 4;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv3.4;
GN   Name=Kcnc4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: This protein mediates the voltage-dependent potassium
CC       ion permeability of excitable membranes. Assuming opened or closed
CC       conformations in response to the voltage difference across the
CC       membrane, the protein forms a potassium-selective channel through
CC       which potassium ions may pass in accordance with their
CC       electrochemical gradient (By similarity).
CC   -!- SUBUNIT: Homotetramer (Probable). Heterotetramer of potassium
CC       channel proteins (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position (By similarity).
CC   -!- DOMAIN: The tail may be important in modulation of channel
CC       activity and/or targeting of the channel to specific subcellular
CC       compartments (By similarity).
CC   -!- PTM: Phosphorylation of serine residues in the inactivation gate
CC       inhibits rapid channel closure (By similarity).
CC   -!- SIMILARITY: Belongs to the potassium channel family. C (Shaw)
CC       (TC 1.A.1.2) subfamily. Kv3.4/KCNC4 sub-subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC024837; AAH24837.1; -; mRNA.
DR   IPI; IPI00153343; -.
DR   RefSeq; NP_666034.1; NM_145922.2.
DR   UniGene; Mm.101976; -.
DR   ProteinModelPortal; Q8R1C0; -.
DR   SMR; Q8R1C0; 1-30, 32-484.
DR   STRING; Q8R1C0; -.
DR   PhosphoSite; Q8R1C0; -.
DR   PRIDE; Q8R1C0; -.
DR   Ensembl; ENSMUST00000009617; ENSMUSP00000009617; ENSMUSG00000027895.
DR   GeneID; 99738; -.
DR   KEGG; mmu:99738; -.
DR   UCSC; uc008qxa.1; mouse.
DR   CTD; 99738; -.
DR   MGI; MGI:96670; Kcnc4.
DR   GeneTree; ENSGT00580000081499; -.
DR   HOGENOM; HBG445693; -.
DR   HOVERGEN; HBG105862; -.
DR   InParanoid; Q8R1C0; -.
DR   OMA; GCEFFFD; -.
DR   OrthoDB; EOG4HMJ92; -.
DR   PhylomeDB; Q8R1C0; -.
DR   NextBio; 354099; -.
DR   ArrayExpress; Q8R1C0; -.
DR   Bgee; Q8R1C0; -.
DR   Genevestigator; Q8R1C0; -.
DR   GermOnline; ENSMUSG00000027895; Mus musculus.
DR   GO; GO:0043679; C:axon terminus; IDA:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0046928; P:regulation of neurotransmitter secretion; IMP:MGI.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003974; K_chnl_volt-dep_Kv3.
DR   InterPro; IPR005405; K_chnl_volt-dep_Kv3.4.
DR   InterPro; IPR021105; K_chnl_volt-dep_Kv3_ID.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   Pfam; PF11404; Potassium_chann; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01583; KV34CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01498; SHAWCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Ion transport; Ionic channel; Membrane; Phosphoprotein;
KW   Potassium; Potassium channel; Potassium transport; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    628       Potassium voltage-gated channel subfamily
FT                                C member 4.
FT                                /FTId=PRO_0000054059.
FT   TOPO_DOM      1    230       Cytoplasmic (Potential).
FT   TRANSMEM    231    251       Helical; Name=Segment S1; (Potential).
FT   TRANSMEM    282    302       Helical; Name=Segment S2; (Potential).
FT   TOPO_DOM    303    316       Cytoplasmic (Potential).
FT   TRANSMEM    317    337       Helical; Name=Segment S3; (Potential).
FT   TRANSMEM    349    368       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TOPO_DOM    369    384       Cytoplasmic (Potential).
FT   TRANSMEM    385    405       Helical; Name=Segment S5; (Potential).
FT   TRANSMEM    456    476       Helical; Name=Segment S6; (Potential).
FT   TOPO_DOM    477    628       Cytoplasmic (Potential).
FT   REGION        1     28       Inactivation gate.
FT   MOTIF       440    445       Selectivity filter (By similarity).
FT   MOD_RES       8      8       Phosphoserine (By similarity).
FT   MOD_RES       9      9       Phosphoserine (By similarity).
FT   MOD_RES      15     15       Phosphoserine (By similarity).
FT   MOD_RES      21     21       Phosphoserine (By similarity).
FT   CARBOHYD    260    260       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    269    269       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   628 AA;  68655 MW;  E9D7B3EC6A03EBF8 CRC64;
     MISSVCVSSY RGRKSGNKPP SKTCLKEEMA KGEASEKIII NVGGTRHETY RSTLRTLPGT
     RLAWLADPDG GGRPESDGGG AGSSGSSGGG GGGGGCEFFF DRHPGVFAYV LNYYRTGKLH
     CPADVCGPLF EEELTFWGID ETDVEPCCWM TYRQHRDAEE ALDIFESPDG GGGGAGPGDE
     AGDDERELAL QRLGPHEGGS GPGAGSGGCR GWQPRMWALF EDPYSSRAAR VVAFASLFFI
     LVSITTFCLE THEAFNIDRN VTEIHRVGNI TSVRFRREVE TEPILTYIEG VCVMWFTLEF
     LVRIVCCPDT LDFVKNLLNI IDFVAILPFY LEVGLSGLSS KAARDVLGFL RVVRFVRILR
     IFKLTRHFVG LRVLGHTLRA STNEFLLLII FLALGVLIFA TMIYYAERIG ARPSDPRGND
     HTDFKNIPIG FWWAVVTMTT LGYGDMYPKT WSGMLVGALC ALAGVLTIAM PVPVIVNNFG
     MYYSLAMAKQ KLPKKRKKHV PRPPQLESPI YCKSEETSPR DSTYSDTSPP AREEGVVERK
     RADSKQNGDA NAVLSDEEGA GLTQPLALAP TPEERRALRR SGTRDRNKKA AACFLLSAGD
     YACADGSVRK EGNVEPKACV PVSHTCAL
//
ID   CQ028_MOUSE             Reviewed;         788 AA.
AC   Q8R1F6; A2A6S8; Q8C8V6;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=UPF0663 transmembrane protein C17orf28 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Kikkawa Y., Shitara H., Kohara Y., Takada T., Okamoto M., Taya C.,
RA   Wakana S., Kamiya K., Yoshikawa Y., Tokano H., Kitamura K.,
RA   Shimizu K., Shiroishi T., Wakabayashi Y., Kominami R., Yonekawa H.;
RT   "Mutations in a new protein containing ankyrin repeats and SAM domain
RT   cause deafness in Jackson shaker mice, a model for Usher syndrome type
RT   IG.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-591, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R1F6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R1F6-2; Sequence=VSP_014474;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the UPF0663 family.
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DR   EMBL; AB087506; BAC67686.1; -; mRNA.
DR   EMBL; AK044395; BAC31902.1; -; mRNA.
DR   EMBL; AL603828; CAM13806.1; -; Genomic_DNA.
DR   EMBL; BC024617; AAH24617.1; -; mRNA.
DR   IPI; IPI00153369; -.
DR   IPI; IPI00607902; -.
DR   RefSeq; NP_780663.1; NM_175454.2.
DR   UniGene; Mm.205707; -.
DR   ProteinModelPortal; Q8R1F6; -.
DR   PhosphoSite; Q8R1F6; -.
DR   PRIDE; Q8R1F6; -.
DR   Ensembl; ENSMUST00000106542; ENSMUSP00000102152; ENSMUSG00000034586.
DR   GeneID; 217310; -.
DR   KEGG; mmu:217310; -.
DR   UCSC; uc007mhg.1; mouse.
DR   UCSC; uc007mhh.1; mouse.
DR   MGI; MGI:2445087; C630004H02Rik.
DR   GeneTree; ENSGT00390000003070; -.
DR   HOGENOM; HBG358137; -.
DR   HOVERGEN; HBG061276; -.
DR   InParanoid; Q8R1F6; -.
DR   OMA; LSMVTAN; -.
DR   OrthoDB; EOG4ZKJKP; -.
DR   PhylomeDB; Q8R1F6; -.
DR   NextBio; 375745; -.
DR   ArrayExpress; Q8R1F6; -.
DR   Bgee; Q8R1F6; -.
DR   CleanEx; MM_C630004H02RIK; -.
DR   Genevestigator; Q8R1F6; -.
DR   GermOnline; ENSMUSG00000034586; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR019142; Dymeclin.
DR   Pfam; PF09742; Dymeclin; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    788       UPF0663 transmembrane protein C17orf28
FT                                homolog.
FT                                /FTId=PRO_0000079297.
FT   TRANSMEM    385    405       Helical; (Potential).
FT   TRANSMEM    416    436       Helical; (Potential).
FT   MOD_RES     591    591       Phosphothreonine.
FT   VAR_SEQ     130    130       Missing (in isoform 2).
FT                                /FTId=VSP_014474.
FT   CONFLICT    332    332       I -> F (in Ref. 2; BAC31902).
SQ   SEQUENCE   788 AA;  88779 MW;  1C9212C1CD7DDCAA CRC64;
     MGSADSKLNF RKAVIQLTTK TQPVEATDNA FWDQFWADTA TSVQDVFALV PAAEIRAVRE
     ESPSNLATLC YKAVEKLVQG AEGGCHSEKE KQVVLNCSRL LTRVLPYIFE DPDWRGFFWS
     TVPGAGRGGQ GEEEDENARP LAESLLLAIA DLLFCPDFTV QNHRRNDVDS AEDVHSLDSC
     EYIWEAGVGF AHSPQPNYIH DMNRMELLKL LLTCFSEAMY LPPSPESGST NPWVQFFCST
     ENRHALPLFT SLLNTVCAYD PVGYGIPYNH LLFSDYREPL VEEAAQVLIV TLDHDSATST
     SPTVDGTTTG TAMDDADPPG PENLFVNYLS RIHREEDFQF ILKGIARLLS NPLLQTYLPN
     STKKIQFHQE LLVLFWKLCD FNKKFLFFVL KSSDVLDILV PILYFLNDAR ADQSRVGLMH
     IGVFILLLLS GERNFGVRLN KPYSVRVPMD IPVFTGTHAD LLIVVFHKII TSGHQRLQPL
     FDCLLTIVVN VSPYLKSLSM VTANKLLHLL EAFSTTWFLF SASQNHHLVF FLLEVFNNII
     QYQFDGNSNL VYAIIRKRAV FHQLANLPTD PPSIHKALQR RRRTPEPLSR TGSQEGTSME
     GSRPAAPAEP GTLKTSLVAT PGIDKLTEKS QVSEDGTLRS LEPESQQSSA ENSPSDGESS
     QTWREQRRLS NASASGQWSP TSDWILSWKS KLPLQTIMRL LQVLVPQVEK ICIDKGLTDE
     SEILRFLQHG TLVGLLPVPH PILIRKYQAN SGTAMWFRTY MWGVIYLRNV DPPIWYDTDV
     KLFEIQRV
//
ID   PDLI2_MOUSE             Reviewed;         349 AA.
AC   Q8R1G6;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=PDZ and LIM domain protein 2;
DE   AltName: Full=PDZ-LIM protein mystique;
GN   Name=Pdlim2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=15659642; DOI=10.1091/mbc.E04-12-1052;
RA   Loughran G., Healy N., Kiely P.A., Huigsloot M., Kedersha N.L.,
RA   O'connor R.;
RT   "Mystique is a new IGF-I regulated PDZ-LIM domain protein that
RT   promotes cell attachment and migration and suppresses anchorage
RT   independent growth.";
RL   Mol. Biol. Cell 16:1811-1822(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199 AND SER-205, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [5]
RP   STRUCTURE BY NMR OF 3-83.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the PDZ domain of PDZ and LIM domain 2.";
RL   Submitted (FEB-2004) to the PDB data bank.
CC   -!- FUNCTION: Probable adapter protein located at the actin
CC       cytoskeleton that promotes cell attachment. Necessary for the
CC       migratory capacity of epithelial cells. Overexpression enhances
CC       cell adhesion to collagen and fibronectin and suppresses anchorage
CC       independent growth. May contribute to tumor cell migratory
CC       capacity (By similarity).
CC   -!- SUBUNIT: Interacts with alpha-actinins ACTN1 and ACTN4, FLNA and
CC       MYH9 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
CC       Note=Localizes at the cytoskeleton. Colocalizes with beta-1
CC       integrin (ITGB1) and alpha-actinin but not with paxillin (PXN) (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced;
CC       Name=1;
CC         IsoId=Q8R1G6-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Highly expressed in lung. Expressed at
CC       intermediate level in kidney, testis and spleen. Weakly expressed
CC       in heart and brain.
CC   -!- INDUCTION: Regulated by IGF-1.
CC   -!- SIMILARITY: Contains 1 LIM zinc-binding domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC024556; AAH24556.1; -; mRNA.
DR   IPI; IPI00153375; -.
DR   RefSeq; NP_666090.1; NM_145978.1.
DR   UniGene; Mm.283968; -.
DR   PDB; 1VB7; NMR; -; A=3-83.
DR   PDBsum; 1VB7; -.
DR   ProteinModelPortal; Q8R1G6; -.
DR   SMR; Q8R1G6; 2-89, 274-344.
DR   STRING; Q8R1G6; -.
DR   PhosphoSite; Q8R1G6; -.
DR   PRIDE; Q8R1G6; -.
DR   Ensembl; ENSMUST00000022681; ENSMUSP00000022681; ENSMUSG00000022090.
DR   GeneID; 213019; -.
DR   KEGG; mmu:213019; -.
DR   UCSC; uc007uni.1; mouse.
DR   CTD; 213019; -.
DR   MGI; MGI:2384850; Pdlim2.
DR   GeneTree; ENSGT00590000082980; -.
DR   HOGENOM; HBG444171; -.
DR   HOVERGEN; HBG061371; -.
DR   InParanoid; Q8R1G6; -.
DR   OMA; QGSVRTY; -.
DR   PhylomeDB; Q8R1G6; -.
DR   NextBio; 373818; -.
DR   ArrayExpress; Q8R1G6; -.
DR   Bgee; Q8R1G6; -.
DR   CleanEx; MM_PDLIM2; -.
DR   Genevestigator; Q8R1G6; -.
DR   GermOnline; ENSMUSG00000022090; Mus musculus.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR001781; Znf_LIM.
DR   Gene3D; G3DSA:2.10.110.10; Znf_LIM; 1.
DR   Pfam; PF00412; LIM; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00132; LIM; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton;
KW   LIM domain; Metal-binding; Phosphoprotein; Zinc.
FT   CHAIN         1    349       PDZ and LIM domain protein 2.
FT                                /FTId=PRO_0000075864.
FT   DOMAIN        1     84       PDZ.
FT   DOMAIN      281    341       LIM zinc-binding.
FT   MOD_RES     129    129       Phosphoserine (By similarity).
FT   MOD_RES     134    134       Phosphoserine (By similarity).
FT   MOD_RES     199    199       Phosphoserine.
FT   MOD_RES     205    205       Phosphoserine.
FT   MOD_RES     263    263       Phosphoserine (By similarity).
FT   STRAND        3      7
FT   STRAND        9     11
FT   STRAND       18     20
FT   TURN         21     24
FT   STRAND       25     28
FT   HELIX        38     41
FT   STRAND       48     52
FT   HELIX        62     70
FT   STRAND       74     81
SQ   SEQUENCE   349 AA;  37703 MW;  9809D7F1AF2BD907 CRC64;
     MALTVDVAGP APWGFRISGG RDFHTPIIVT KVTERGKAEA ADLRPGDIIV AINGQSAENM
     LHAEAQSKIR QSASPLRLQL DRSQTASPGQ TNGEGSLEVL ATRFQGSLRT HRDSQSSQRS
     ACFSPVSLSP RPCSPFSTPP PTSPVALSKE DMIGCSFQSL THSPGLAAAH HLTYPGHPTS
     QQAGHSSPSD SAVRVLLHSP GRPSSPRFSS LDLEEDSEVF KMLQENRQGR AAPRQSSSFR
     LLQEALEAEE RGGTPAFVPS SLSSQASLPT SRALATPPKL HTCEKCSVNI SNQAVRIQEG
     RYRHPGCYTC ADCGLNLKMR GHFWVGNELY CEKHARQRYS MPGTLNSRA
//
ID   UBAC2_MOUSE             Reviewed;         345 AA.
AC   Q8R1K1; Q3TWC0;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Ubiquitin-associated domain-containing protein 2;
DE            Short=UBA domain-containing protein 2;
DE   AltName: Full=Phosphoglycerate dehydrogenase-like protein 1;
DE   Flags: Precursor;
GN   Name=Ubac2; Synonyms=Phgdhl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Contains 1 UBA domain.
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DR   EMBL; AK049109; BAC33546.1; -; mRNA.
DR   EMBL; AK158177; BAE34394.1; -; mRNA.
DR   EMBL; AK159755; BAE35346.1; -; mRNA.
DR   EMBL; BC024467; AAH24467.1; -; mRNA.
DR   IPI; IPI00153390; -.
DR   RefSeq; NP_081137.2; NM_026861.2.
DR   UniGene; Mm.441151; -.
DR   HSSP; Q10256; 1Z96.
DR   ProteinModelPortal; Q8R1K1; -.
DR   SMR; Q8R1K1; 308-343.
DR   PRIDE; Q8R1K1; -.
DR   Ensembl; ENSMUST00000039803; ENSMUSP00000043245; ENSMUSG00000041765.
DR   GeneID; 68889; -.
DR   KEGG; mmu:68889; -.
DR   NMPDR; fig|10090.3.peg.29595; -.
DR   UCSC; uc007vao.1; mouse.
DR   CTD; 68889; -.
DR   MGI; MGI:1916139; Ubac2.
DR   eggNOG; roNOG10579; -.
DR   HOGENOM; HBG402879; -.
DR   HOVERGEN; HBG106192; -.
DR   InParanoid; Q8R1K1; -.
DR   OMA; LVEAMQY; -.
DR   OrthoDB; EOG4W9J4B; -.
DR   PhylomeDB; Q8R1K1; -.
DR   NextBio; 328121; -.
DR   ArrayExpress; Q8R1K1; -.
DR   Bgee; Q8R1K1; -.
DR   CleanEx; MM_UBAC2; -.
DR   Genevestigator; Q8R1K1; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR009060; UBA-like.
DR   InterPro; IPR000449; UBA/transl_elong_EF1B_N.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   Pfam; PF00627; UBA; 1.
DR   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF46934; UBA_like; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     39       Potential.
FT   CHAIN        40    345       Ubiquitin-associated domain-containing
FT                                protein 2.
FT                                /FTId=PRO_0000280756.
FT   TOPO_DOM     40     91       Extracellular (Potential).
FT   TRANSMEM     92    112       Helical; (Potential).
FT   TOPO_DOM    113    125       Cytoplasmic (Potential).
FT   TRANSMEM    126    146       Helical; (Potential).
FT   TOPO_DOM    147    163       Extracellular (Potential).
FT   TRANSMEM    164    184       Helical; (Potential).
FT   TOPO_DOM    185    345       Cytoplasmic (Potential).
FT   DOMAIN      305    345       UBA.
FT   CARBOHYD    161    161       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   345 AA;  39057 MW;  5C41C1BB4272247C CRC64;
     MFTSTGSSGL YKAPLSKSLL LVPSALSLLL TLLLPHCQKF FVYDLHAVKH DLQIWRLICG
     RIICLDLKDA FCSGLLIYNF RIFERRYGSR KFASFLLGSW VLSALFDFIL VEAVQYSLGV
     TVASNLPSGF LAPVFALFVP FHCSIPRVQV AQILGPLSIT NKTLIYILGL QLFTSGSYIW
     IVAMSGLISG MCYDRKVLQV HQVLRIPGRM AEFFSWALEP IFSSSEPTSE ARVGMGATVD
     IQRQQRMEQL DRQLMLSQFA QVRRQRQQQG GMINWNRLFP PLRQRRNINY QDGPRSEQRA
     SPPLEVSEEQ VARLMEMGFS RGDALEALRA SNNDLNVATN FLLQH
//
ID   ZN830_MOUSE             Reviewed;         363 AA.
AC   Q8R1N0; Q3TR52; Q9CWV9; Q9CYI6;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Zinc finger protein 830;
DE   AltName: Full=Coiled-coil domain-containing protein 16;
DE   AltName: Full=Ovus mutant candidate gene 1 protein;
GN   Name=Znf830; Synonyms=Ccdc16, Omcg1, Zfp830;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney, Liver, Skin, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=15988037; DOI=10.1128/MCB.25.14.6289-6302.2005;
RA   Artus J., Vandormael-Pournin S., Froedin M., Nacerddine K.,
RA   Babinet C., Cohen-Tannoudji M.;
RT   "Impaired mitotic progression and preimplantation lethality in mice
RT   lacking OMCG1, a new evolutionarily conserved nuclear protein.";
RL   Mol. Cell. Biol. 25:6289-6302(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342 AND SER-353, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Acts as an important regulator of the cell cycle in the
CC       preimplantation embryo by controlling different aspects of M
CC       phase.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Excluded from
CC       nucleolus. In metaphase II oocytes and in mitotic blastomeres, it
CC       is detected in cytoplasm, suggesting that it is not associated
CC       with chromosomes during mitosis.
CC   -!- TISSUE SPECIFICITY: Widely expressed at low level.
CC   -!- DEVELOPMENTAL STAGE: Expressed in preimplantation embryos.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- DISRUPTION PHENOTYPE: Mice die by the end of preimplantation
CC       development and exhibit a dramatic reduction in the total cell
CC       number, a high mitotic index, and the presence of abnormal mitotic
CC       figures.
CC   -!- SIMILARITY: Contains 1 C2H2-type zinc finger.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK050043; BAC34045.1; -; mRNA.
DR   EMBL; AK010353; BAB26873.1; -; mRNA.
DR   EMBL; AK017640; BAB30851.1; -; mRNA.
DR   EMBL; AK132497; BAE21204.1; -; mRNA.
DR   EMBL; AK148058; BAE28318.1; -; mRNA.
DR   EMBL; AK163064; BAE37178.1; -; mRNA.
DR   EMBL; AK167656; BAE39707.1; -; mRNA.
DR   EMBL; AK168417; BAE40331.1; -; mRNA.
DR   EMBL; AL645594; CAI25093.1; -; Genomic_DNA.
DR   EMBL; BC024340; AAH24340.1; -; mRNA.
DR   IPI; IPI00320645; -.
DR   RefSeq; NP_080160.2; NM_025884.4.
DR   UniGene; Mm.29622; -.
DR   ProteinModelPortal; Q8R1N0; -.
DR   STRING; Q8R1N0; -.
DR   PhosphoSite; Q8R1N0; -.
DR   PRIDE; Q8R1N0; -.
DR   Ensembl; ENSMUST00000056677; ENSMUSP00000056154; ENSMUSG00000046010.
DR   GeneID; 66983; -.
DR   KEGG; mmu:66983; -.
DR   UCSC; uc007kmy.1; mouse.
DR   CTD; 66983; -.
DR   MGI; MGI:1914233; Zfp830.
DR   eggNOG; roNOG15199; -.
DR   GeneTree; ENSGT00390000012151; -.
DR   HOGENOM; HBG713871; -.
DR   HOVERGEN; HBG105347; -.
DR   InParanoid; Q8R1N0; -.
DR   OMA; ESPFAKY; -.
DR   OrthoDB; EOG4QFWFC; -.
DR   PhylomeDB; Q8R1N0; -.
DR   NextBio; 323216; -.
DR   ArrayExpress; Q8R1N0; -.
DR   Bgee; Q8R1N0; -.
DR   CleanEx; MM_ZFP830; -.
DR   Genevestigator; Q8R1N0; -.
DR   GermOnline; ENSMUSG00000046010; Mus musculus.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0001832; P:blastocyst growth; IMP:MGI.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; Cell cycle; Cell division; Chromosome; Coiled coil;
KW   Developmental protein; Metal-binding; Mitosis; Nucleus;
KW   Phosphoprotein; Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    363       Zinc finger protein 830.
FT                                /FTId=PRO_0000076194.
FT   ZN_FING      53     75       C2H2-type.
FT   COILED       16     40       Potential.
FT   COILED      303    331       Potential.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     342    342       Phosphoserine.
FT   MOD_RES     353    353       Phosphoserine.
FT   CONFLICT     81     82       EL -> DV (in Ref. 1; BAB30851).
FT   CONFLICT    111    111       Q -> L (in Ref. 1; BAB26873).
FT   CONFLICT    305    305       C -> G (in Ref. 1; BAE37178).
FT   CONFLICT    309    309       V -> G (in Ref. 1; BAE37178).
SQ   SEQUENCE   363 AA;  40658 MW;  1247580A0D8B6E60 CRC64;
     MASSTSTRTP AGKRVVNQEE LRRLMREKQR LSTNRKRIES PFAKYNRLGQ LSCALCNTPV
     KSELLWQTHV LGKQHRERVA ELKGAKGATQ GPSTGTVPQA TKRRATDVES QDAKKAKASA
     GPQVQPSTSA SSANLDAARA APSKPGLGLL PDYDDEEEEE EEGGGEERRD SSKHLPDAQG
     KEHSLASPRE TTSNVLPNDP FNTNPPKAPL VPHSGSIEKA EIHEKVVERR ENTAEALPEG
     FFDDPEVDAK VRKVDAPKDQ MDKEWDEFQK AMRQVNTISE AIVAEEDEEG RLDRQIGEID
     EQIECYRRVE KLRNRQDEIK NKLKEVLTIK ELQKKEEENV DSDDEGELQD LLSQDWRVKG
     ALL
//
ID   DC1L1_MOUSE             Reviewed;         523 AA.
AC   Q8R1Q8;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Cytoplasmic dynein 1 light intermediate chain 1;
DE   AltName: Full=Dynein light chain A;
DE            Short=DLC-A;
DE   AltName: Full=Dynein light intermediate chain 1, cytosolic;
GN   Name=Dync1li1; Synonyms=Dncli1, Dnclic1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 134-142, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; THR-513 AND
RP   SER-516, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-405, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-510; THR-515
RP   AND THR-518, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-510; THR-513; THR-515
RP   AND SER-516, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-510 AND SER-516, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Acts as one of several non-catalytic accessory
CC       components of the cytoplasmic dynein 1 complex that are thought to
CC       be involved in linking dynein to cargos and to adapter proteins
CC       that regulate dynein function. Cytoplasmic dynein 1 acts as a
CC       motor for the intracellular retrograde motility of vesicles and
CC       organelles along microtubules. May play a role in binding dynein
CC       to membranous organelles or chromosomes. Probably involved in the
CC       microtubule-dependent transport of pericentrin. Is required for
CC       progress throuh the spindle assembly checkpoint. The
CC       phosphorylated form appears to be involved in the selective
CC       removal of MAD1L1 and MAD1L2 but not BUB1B from kinetochores (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer (By similarity). The cytoplasmic dynein 1
CC       complex consists of two catalytic heavy chains (HCs) and a number
CC       of non-catalytic subunits presented by intermediate chains (ICs),
CC       light intermediate chains (LICs) and light chains (LCs); the
CC       composition seems to vary in respect to the IC, LIC and LC
CC       composition. The heavy chain homodimer serves as a scaffold for
CC       the probable homodimeric assembly of the respective non-catalytic
CC       subunits. The ICs and LICs bind directly to the HC dimer and the
CC       LCs assemble on the IC dimer. Self-associates. Interacts with
CC       DYNC1H1; DYNC1LI1 and DYNC1LI2 bind mutually exclusive to DYNC1H1.
CC       Interacts with PCNT (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Chromosome,
CC       centromere, kinetochore (By similarity). Cytoplasm, cytoskeleton,
CC       spindle pole (By similarity).
CC   -!- PTM: Phosphorylated during mitosis but not in interphase (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the dynein light intermediate chain family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC023347; AAH23347.1; -; mRNA.
DR   IPI; IPI00153421; -.
DR   RefSeq; NP_666341.1; NM_146229.2.
DR   UniGene; Mm.128627; -.
DR   ProteinModelPortal; Q8R1Q8; -.
DR   SMR; Q8R1Q8; 236-304.
DR   STRING; Q8R1Q8; -.
DR   PhosphoSite; Q8R1Q8; -.
DR   PRIDE; Q8R1Q8; -.
DR   Ensembl; ENSMUST00000047404; ENSMUSP00000035366; ENSMUSG00000032435.
DR   GeneID; 235661; -.
DR   KEGG; mmu:235661; -.
DR   UCSC; uc009rxy.1; mouse.
DR   CTD; 235661; -.
DR   MGI; MGI:2135610; Dync1li1.
DR   GeneTree; ENSGT00390000008295; -.
DR   HOGENOM; HBG314876; -.
DR   HOVERGEN; HBG005546; -.
DR   InParanoid; Q8R1Q8; -.
DR   OMA; SVVREHI; -.
DR   OrthoDB; EOG4W3SN1; -.
DR   PhylomeDB; Q8R1Q8; -.
DR   NextBio; 382833; -.
DR   ArrayExpress; Q8R1Q8; -.
DR   Bgee; Q8R1Q8; -.
DR   CleanEx; MM_DYNC1LI1; -.
DR   Genevestigator; Q8R1Q8; -.
DR   GermOnline; ENSMUSG00000032435; Mus musculus.
DR   GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
DR   GO; GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:motor activity; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; ISS:UniProtKB.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008467; Dynein1_light_intermed_chain.
DR   InterPro; IPR022780; Dynein_light_int_chain.
DR   PANTHER; PTHR12688; DLIC; 1.
DR   Pfam; PF05783; DLIC; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; Dynein;
KW   Kinetochore; Microtubule; Mitosis; Motor protein; Nucleotide-binding;
KW   Phosphoprotein; Transport.
FT   CHAIN         1    523       Cytoplasmic dynein 1 light intermediate
FT                                chain 1.
FT                                /FTId=PRO_0000114667.
FT   NP_BIND      74     81       ATP (Potential).
FT   MOD_RES     207    207       Phosphoserine.
FT   MOD_RES     398    398       Phosphoserine (By similarity).
FT   MOD_RES     405    405       Phosphoserine.
FT   MOD_RES     408    408       Phosphothreonine (By similarity).
FT   MOD_RES     412    412       Phosphoserine (By similarity).
FT   MOD_RES     414    414       Phosphoserine (By similarity).
FT   MOD_RES     419    419       Phosphoserine (By similarity).
FT   MOD_RES     421    421       Phosphoserine (By similarity).
FT   MOD_RES     450    450       Phosphoserine (By similarity).
FT   MOD_RES     486    486       Phosphoserine (By similarity).
FT   MOD_RES     510    510       Phosphoserine.
FT   MOD_RES     512    512       Phosphothreonine (By similarity).
FT   MOD_RES     513    513       Phosphothreonine.
FT   MOD_RES     515    515       Phosphothreonine.
FT   MOD_RES     516    516       Phosphoserine.
FT   MOD_RES     518    518       Phosphothreonine.
SQ   SEQUENCE   523 AA;  56614 MW;  F080D6865A399498 CRC64;
     MAAVGRVGSF GSSPPGLAST YASGPLANEL ASGSGGPAAG DDEDGQNLWS CILSEVSTRS
     RSKLPTGKNV LLLGEDGAGK TSLIRRIQGI EEYKKGRGLE YLYLNVHDED RDDQTRCNVW
     ILDGDLYHKG LLKFSLDALS LRDTLVMLVV DMSKPWTALD SLQKWASVVR EHVDKLKIPP
     EEMKEMEQKL IRDFQEYVEP GEDFPASPQR RTTGAQEDRG DSVVLPLGAD TLTHNLGLPV
     LVVCTKCDAI SVLEKEHDYR DEHFDFIQSH IRKFCLQYGA ALIYTSVKEN KNIDLVYKYI
     VQKLYGFPYK IPAVVVEKDA VFIPAGWDND KKIGILHENF QTLKVEDNFE DIITKPPVRK
     FVHEKEIMAE DDQVFLMKLQ SLLAKQPPTA AGRPVDASPR VPGGSPRTPN RSVSSNVASV
     SPIPAGSKKI DPNMKAGATS EGVLANFFNS LLSKKTGSPG GPGVGGSPGG GAAGASPSLP
     PSAKKSGQKP VLSDVHAELD RITRKPASVS PTTPTSPTEG EAS
//
ID   CHMP7_MOUSE             Reviewed;         451 AA.
AC   Q8R1T1; Q8CFW4;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Charged multivesicular body protein 7;
DE   AltName: Full=Chromatin-modifying protein 7;
GN   Name=Chmp7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=FVB/N; TISSUE=Eye, and Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
CC   -!- FUNCTION: Plays a role in the endosomal sorting pathway (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with CHMP4B, but not with VPS25 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Diffused localization, with
CC       some punctate distribution, especially in the perinuclear area (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R1T1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R1T1-2; Sequence=VSP_015343, VSP_015344;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the SNF7 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC024115; AAH24115.1; -; mRNA.
DR   EMBL; BC033365; AAH33365.1; -; mRNA.
DR   IPI; IPI00153445; -.
DR   IPI; IPI00461712; -.
DR   RefSeq; NP_598839.2; NM_134078.4.
DR   UniGene; Mm.159637; -.
DR   ProteinModelPortal; Q8R1T1; -.
DR   STRING; Q8R1T1; -.
DR   PhosphoSite; Q8R1T1; -.
DR   PRIDE; Q8R1T1; -.
DR   Ensembl; ENSMUST00000036381; ENSMUSP00000047700; ENSMUSG00000034190.
DR   GeneID; 105513; -.
DR   KEGG; mmu:105513; -.
DR   UCSC; uc007ums.1; mouse.
DR   CTD; 105513; -.
DR   MGI; MGI:1913922; Chmp7.
DR   eggNOG; roNOG13739; -.
DR   GeneTree; ENSGT00530000063571; -.
DR   HOGENOM; HBG713369; -.
DR   HOVERGEN; HBG081151; -.
DR   InParanoid; Q8R1T1; -.
DR   OMA; ERCKEDA; -.
DR   OrthoDB; EOG4HHP33; -.
DR   PhylomeDB; Q8R1T1; -.
DR   NextBio; 357748; -.
DR   ArrayExpress; Q8R1T1; -.
DR   Bgee; Q8R1T1; -.
DR   CleanEx; MM_CHMP7; -.
DR   Genevestigator; Q8R1T1; -.
DR   GermOnline; ENSMUSG00000034190; Mus musculus.
DR   GO; GO:0000815; C:ESCRT III complex; ISS:UniProtKB.
DR   GO; GO:0008565; F:protein transporter activity; ISS:UniProtKB.
DR   GO; GO:0045324; P:late endosome to vacuole transport; ISS:UniProtKB.
DR   InterPro; IPR005024; Snf7.
DR   Pfam; PF03357; Snf7; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Phosphoprotein;
KW   Protein transport; Transport.
FT   CHAIN         1    451       Charged multivesicular body protein 7.
FT                                /FTId=PRO_0000211517.
FT   COILED      248    312       Potential.
FT   MOD_RES     232    232       Phosphoserine.
FT   VAR_SEQ     322    370       FNAYQAGVGALKLSMKDVTVEKAESLVDQIQELCDTQDEVS
FT                                QTLAGGVT -> ATPLRALWSQSPTLQLPPLWSAVSGNPGF
FT                                FQRVAGFSFLLGSLTSLGVR (in isoform 2).
FT                                /FTId=VSP_015343.
FT   VAR_SEQ     371    451       Missing (in isoform 2).
FT                                /FTId=VSP_015344.
SQ   SEQUENCE   451 AA;  50633 MW;  F52C0B3F72CBA827 CRC64;
     MWSPEREAQA PTGGDPAGLL PPEWEEDEER MSFLFSAFKR SREVNSTDWD SKMGFWAPLV
     LSHSRRQGVV RLRLRDLQEA FQRKGSVPLG LATVLQDLLR RGELQRESDF MASVDSSWIS
     WGVGVFLLKP LKWTLSNMLG DHKVPAEEVL VAVELLKEKA EEVYRLYQNS PLSSHPVVAL
     SELSALCANS CPDERTFYLV LLQLQKEKRV TVLEQNGEKI VKFARGPHAK VSPVNDVDVG
     VYQLMQSEQL LSRKVESLSQ ESERCKEEAR RACRAGKKQL ALRSLKAKQR TEKRIEALHA
     KLDTVQGILD RIYASQTDQM VFNAYQAGVG ALKLSMKDVT VEKAESLVDQ IQELCDTQDE
     VSQTLAGGVT NGLDFDSEEL EKELDILLQD TTTEPLSLLE TPQETTLYTN SVPKPRILDA
     ELEAELEKLS LSEGGLIPSS KSPKRQLEPT L
//
ID   RRF2M_MOUSE             Reviewed;         779 AA.
AC   Q8R2Q4; B2RR55; Q8BXS5;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Ribosome-releasing factor 2, mitochondrial;
DE            Short=RRF2mt;
DE   AltName: Full=Elongation factor G 2, mitochondrial;
DE            Short=EF-G2mt;
DE            Short=mEF-G 2;
DE   Flags: Precursor;
GN   Name=Gfm2; Synonyms=Efg2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Mitochondrial GTPase that mediates the disassembly of
CC       ribosomes from messenger RNA at the termination of mitochondrial
CC       protein biosynthesis. Acts in collaboration with MRRF. GTP
CC       hydrolysis follows the ribosome disassembly and probably occurs on
CC       the ribosome large subunit. Not involved in the GTP-dependent
CC       ribosomal translocation step during translation elongation (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8R2Q4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R2Q4-2; Sequence=VSP_038195;
CC       Name=3;
CC         IsoId=Q8R2Q4-3; Sequence=VSP_038196;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC       EF-G/EF-2 subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK044371; BAC31889.1; -; mRNA.
DR   EMBL; BC027341; AAH27341.1; -; mRNA.
DR   EMBL; BC138233; AAI38234.1; -; mRNA.
DR   EMBL; BC145208; AAI45209.1; -; mRNA.
DR   IPI; IPI00269240; -.
DR   IPI; IPI00338876; -.
DR   IPI; IPI00928146; -.
DR   RefSeq; NP_796240.3; NM_177266.4.
DR   UniGene; Mm.219675; -.
DR   ProteinModelPortal; Q8R2Q4; -.
DR   SMR; Q8R2Q4; 63-770.
DR   STRING; Q8R2Q4; -.
DR   PRIDE; Q8R2Q4; -.
DR   Ensembl; ENSMUST00000022170; ENSMUSP00000022170; ENSMUSG00000021666.
DR   Ensembl; ENSMUST00000109434; ENSMUSP00000105060; ENSMUSG00000021666.
DR   GeneID; 320806; -.
DR   KEGG; mmu:320806; -.
DR   UCSC; uc007rnu.1; mouse.
DR   CTD; 320806; -.
DR   MGI; MGI:2444783; Gfm2.
DR   GeneTree; ENSGT00550000074890; -.
DR   InParanoid; Q8R2Q4; -.
DR   OMA; KCLQRED; -.
DR   OrthoDB; EOG4NKBV3; -.
DR   PhylomeDB; Q8R2Q4; -.
DR   NextBio; 397475; -.
DR   ArrayExpress; Q8R2Q4; -.
DR   Bgee; Q8R2Q4; -.
DR   CleanEx; MM_GFM2; -.
DR   Genevestigator; Q8R2Q4; -.
DR   GermOnline; ENSMUSG00000021666; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0032543; P:mitochondrial translation; ISS:UniProtKB.
DR   GO; GO:0032790; P:ribosome disassembly; ISS:UniProtKB.
DR   InterPro; IPR009022; Elongation_fac_G/III/V.
DR   InterPro; IPR000795; ProtSyn_GTP-bd.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR000640; Transl_elong_EFG/EF2_C.
DR   InterPro; IPR005517; Transl_elong_EFG/EF2_IV.
DR   InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR   InterPro; IPR009000; Transl_elong_init/rib_B-barrel.
DR   Gene3D; G3DSA:3.30.230.10; Ribosomal_S5_D2-type_fold; 1.
DR   Gene3D; G3DSA:3.30.70.240; Transl_elong_EFG/EF2_C; 1.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF03764; EFG_IV; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SMART; SM00889; EFG_IV; 1.
DR   SUPFAM; SSF54980; EFG_III_V; 2.
DR   SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
DR   SUPFAM; SSF50447; Translat_factor; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS00301; EFACTOR_GTP; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; GTP-binding; Mitochondrion; Nucleotide-binding;
KW   Protein biosynthesis; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    779       Ribosome-releasing factor 2,
FT                                mitochondrial.
FT                                /FTId=PRO_0000007451.
FT   NP_BIND      77     84       GTP (By similarity).
FT   NP_BIND     141    145       GTP (By similarity).
FT   NP_BIND     195    198       GTP (By similarity).
FT   VAR_SEQ      50     51       Missing (in isoform 2).
FT                                /FTId=VSP_038195.
FT   VAR_SEQ     284    310       Missing (in isoform 3).
FT                                /FTId=VSP_038196.
FT   CONFLICT    245    245       L -> V (in Ref. 2; AAH27341).
FT   CONFLICT    680    680       K -> T (in Ref. 2; AAH27341).
FT   CONFLICT    777    777       H -> R (in Ref. 2; AAH27341).
SQ   SEQUENCE   779 AA;  86109 MW;  D9AA1D5775027207 CRC64;
     MFTKWRIFAV NHQRTFSVHL NTMCYCKIKA NLKRLKTQLP LTRNYSSAPG IAGSDVKSLH
     SVINPPVAKI RNIGIMAHID AGKTTTTERI LYYSGYTRSL GDVDDGDTVT DFMAQERERG
     ITIQSAAVTL DWKGYRVNLI DTPGHVDFTL EVERCLRVLD GAVAVFDASA GVEAQTLTVW
     RQADKHKIPR ICFLNKMDKT GASFNYAVES IREKLKAKPL ILQLPIGEAR TFQGVVDVVN
     KEKLLWNSNS DDGKDFERMP LSEASDRELL KETIEARNSL IEQVADLDDE FADLVLGEFS
     ENFDLVPAEK LQAAVHRVTL AQAAVPVLCG SALKNKGVQP LLDAVTTYLP SPEEREDRFL
     QWYEGDLCAL AFKVLHDKQR GPLVFLRIYS GTLTPQLAVH NINRNCTERM SRLLLPFADQ
     HVEIPSLTAG NIALTVGLKQ TATGDTIVSS KSSALAAARR AGRGEREHGK KREAESLLLA
     GVEVPEPVFF CTIEPPSVAK QPDLDHALER LQREDPSLKV KLDPDSGQTV LCGMGELHIE
     IIHDRIKREY GLETYLGPLQ VAYRETILNS VRATDTLDRV LGDKRHLVSA ELEVRPAEEP
     CAVAKIEYAD CVGEDLLQAS REAIESAVHS ACLQGPLLGS PVQDVAMTLH SLMIHPGTST
     TMVTACISRC MQKALKKADK QVLEPLMSLE VTVSREYLSP VLADLAQRRG NIQEIQTRQD
     NRVVLGFVPL AEIMGYSTVL RTLTSGSATF ALELSTYQAM SPQDQSALLN QRSGLAHVL
//
ID   AAGAB_MOUSE             Reviewed;         316 AA.
AC   Q8R2R3; Q9CV78;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 39.
DE   RecName: Full=Alpha- and gamma-adaptin-binding protein p34;
GN   Name=Aagab;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 209-316.
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: May play a role in membrane traffic (By similarity).
CC   -!- SUBUNIT: Interacts with AP1G1 and AP2A1 (By similarity).
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DR   EMBL; BC027311; AAH27311.1; -; mRNA.
DR   EMBL; AK009203; BAB26137.1; -; mRNA.
DR   IPI; IPI00336915; -.
DR   UniGene; Mm.34338; -.
DR   ProteinModelPortal; Q8R2R3; -.
DR   PhosphoSite; Q8R2R3; -.
DR   PRIDE; Q8R2R3; -.
DR   Ensembl; ENSMUST00000041551; ENSMUSP00000048595; ENSMUSG00000037257.
DR   MGI; MGI:1914189; Aagab.
DR   GeneTree; ENSGT00390000007218; -.
DR   HOGENOM; HBG713687; -.
DR   InParanoid; Q8R2R3; -.
DR   OrthoDB; EOG4QFWDP; -.
DR   ArrayExpress; Q8R2R3; -.
DR   Bgee; Q8R2R3; -.
DR   CleanEx; MM_2310007F21RIK; -.
DR   Genevestigator; Q8R2R3; -.
DR   GermOnline; ENSMUSG00000037257; Mus musculus.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR019341; Alpha/Gamma-adaptin-bd_p34.
DR   Pfam; PF10199; Adaptin_binding; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1    316       Alpha- and gamma-adaptin-binding protein
FT                                p34.
FT                                /FTId=PRO_0000058135.
FT   MOD_RES     311    311       Phosphoserine (By similarity).
FT   MOD_RES     312    312       Phosphoserine (By similarity).
SQ   SEQUENCE   316 AA;  34510 MW;  A868E07CC409286D CRC64;
     MAAGVPCALV TSCSATFTGD RLVQHILGTE DAVVEATSSD AVRFYPWTID NKYYSAEINL
     CVVPSKFLVT AEIAESVQAF VVYFDSTQKS GLDSVSSWLP LAEAWLAEVM ILVCDRVCDD
     GINRQQAQEW CIKHGFELVE LNPEELPEED NDFPESTGVK RIVQALNANV WSNVVMKSDR
     SQGFSLLNSL AGANRRVASA ESCHSEQQEP SPTAERTESL PGHHSGACGS AGAQVDSIVD
     PMLDLDIQEL ASLTTGGGDL ENFERLFSKL KEMKDKAATL PHEQRKLHAE KVAKAFWMAI
     GGDRDEIEGL SSDDEH
//
ID   Q8R2T7_MOUSE            Unreviewed;       591 AA.
AC   Q8R2T7;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Oxysterol-binding protein;
GN   Name=Osbpl10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129; TISSUE=Mammary tumor. Brca1-/fl;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the OSBP family.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC027256; AAH27256.1; -; mRNA.
DR   IPI; IPI00271388; -.
DR   RefSeq; NP_683761.1; NM_148958.2.
DR   UniGene; Mm.458474; -.
DR   ProteinModelPortal; Q8R2T7; -.
DR   SMR; Q8R2T7; 228-576.
DR   PRIDE; Q8R2T7; -.
DR   Ensembl; ENSMUST00000046627; ENSMUSP00000038013; ENSMUSG00000040875.
DR   GeneID; 74486; -.
DR   KEGG; mmu:74486; -.
DR   UCSC; uc009ryl.1; mouse.
DR   CTD; 74486; -.
DR   MGI; MGI:1921736; Osbpl10.
DR   eggNOG; roNOG04466; -.
DR   GeneTree; ENSGT00550000074515; -.
DR   HOGENOM; HBG444510; -.
DR   HOVERGEN; HBG053376; -.
DR   InParanoid; Q8R2T7; -.
DR   OMA; HKPGASE; -.
DR   OrthoDB; EOG4MGS76; -.
DR   PhylomeDB; Q8R2T7; -.
DR   NextBio; 340924; -.
DR   ArrayExpress; Q8R2T7; -.
DR   Bgee; Q8R2T7; -.
DR   Genevestigator; Q8R2T7; -.
DR   GO; GO:0008202; P:steroid metabolic process; IEA:InterPro.
DR   InterPro; IPR000648; Oxysterol-bd.
DR   InterPro; IPR018494; Oxysterol-bd_CS.
DR   PANTHER; PTHR10972; Oxysterol_bd; 1.
DR   Pfam; PF01237; Oxysterol_BP; 1.
DR   PROSITE; PS01013; OSBP; 1.
PE   2: Evidence at transcript level;
KW   Lipid transport; Transport.
SQ   SEQUENCE   591 AA;  65801 MW;  7AF0CE7EBFDF1D81 CRC64;
     MEMSSKTTPG SRSRSLTLLP HGTPSSASPC SQRHLSTGAP GVVSVTRHKS PAAARRAKSQ
     YSGQLHEVRE MMNQVEGQQK NLVHAIESLP GSGPLTALDQ DLLLLKATSA ATLSCLGECL
     SLLQQSVRQA APPSHKPGAS ETILGWHGPT SHSTDQLKNG TLGSLPSASA NITWAILPNS
     AEEEHNSQPE PEPDSGPELV LSEEEQSDNE DKGEVEPGAM EDQRSVILHL ISQLKLGMDL
     TKVVLPTFIL EKRSLLEMYA DFMAHPDLLL AITAGATPEE RVISFVEYYL TAFHEGRKGT
     LAKKPYNPII GETFHCSWEV PKDRVKSKWT SPHPPISAHE HPMADDPSKS YKLRFVAEQV
     SHHPPISCFY CECKEKRLCV NTHVWTKSKF MGMSVGVSMI GEGVLRLLDH GEEYVFTLPS
     AYARSILTVP WVELGGKVNI SCAKTGYSAT VTFHTKPFYG GKVHRVTAEV KHNPTNTIVC
     KAHGEWNGTL EFTYSNGETK VIDTTTLPVY PKKLRPLEKQ GPMESRNLWQ EVTHYLRLGD
     IDAATEQKRR LEERQRVEER KRETLRTPWR PKYFIPEGDG WVYFNPLWKT H
//
ID   ABHD6_MOUSE             Reviewed;         336 AA.
AC   Q8R2Y0; Q3TGD2; Q9DCD4;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Monoacylglycerol lipase ABHD6;
DE            EC=3.1.1.23;
DE   AltName: Full=2-arachidonoylglycerol hydrolase;
DE   AltName: Full=Abhydrolase domain-containing protein 6;
GN   Name=Abhd6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Amnion, Embryo, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18096503; DOI=10.1016/j.chembiol.2007.11.006;
RA   Blankman J.L., Simon G.M., Cravatt B.F.;
RT   "A comprehensive profile of brain enzymes that hydrolyze the
RT   endocannabinoid 2-arachidonoylglycerol.";
RL   Chem. Biol. 14:1347-1356(2007).
CC   -!- FUNCTION: Has 2-arachidonoylglycerol hydrolase activity. May be a
CC       regulator of endocannabinoid signaling pathways.
CC   -!- CATALYTIC ACTIVITY: Hydrolyzes glycerol monoesters of long-chain
CC       fatty acids.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R2Y0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R2Y0-2; Sequence=VSP_024012;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE40616.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK002883; BAB22430.1; -; mRNA.
DR   EMBL; AK076105; BAC36186.1; -; mRNA.
DR   EMBL; AK090076; BAC41081.1; -; mRNA.
DR   EMBL; AK168782; BAE40616.1; ALT_INIT; mRNA.
DR   EMBL; BC027011; AAH27011.1; -; mRNA.
DR   IPI; IPI00321386; -.
DR   IPI; IPI00830283; -.
DR   RefSeq; NP_079617.2; NM_025341.3.
DR   UniGene; Mm.181473; -.
DR   ProteinModelPortal; Q8R2Y0; -.
DR   SMR; Q8R2Y0; 48-326.
DR   STRING; Q8R2Y0; -.
DR   MEROPS; S33.977; -.
DR   PRIDE; Q8R2Y0; -.
DR   Ensembl; ENSMUST00000026313; ENSMUSP00000026313; ENSMUSG00000025277.
DR   GeneID; 66082; -.
DR   KEGG; mmu:66082; -.
DR   NMPDR; fig|10090.3.peg.28535; -.
DR   UCSC; uc007sen.1; mouse.
DR   CTD; 66082; -.
DR   MGI; MGI:1913332; Abhd6.
DR   eggNOG; roNOG09273; -.
DR   HOGENOM; HBG445497; -.
DR   HOVERGEN; HBG059524; -.
DR   InParanoid; Q8R2Y0; -.
DR   OMA; CSLSLVC; -.
DR   OrthoDB; EOG4MSCZH; -.
DR   PhylomeDB; Q8R2Y0; -.
DR   NextBio; 320572; -.
DR   ArrayExpress; Q8R2Y0; -.
DR   Bgee; Q8R2Y0; -.
DR   CleanEx; MM_ABHD6; -.
DR   Genevestigator; Q8R2Y0; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0047372; F:acylglycerol lipase activity; IEA:EC.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00412; EPOXHYDRLASE.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Hydrolase; Membrane; Signal-anchor;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    336       Monoacylglycerol lipase ABHD6.
FT                                /FTId=PRO_0000281576.
FT   TOPO_DOM      1      8       Extracellular (Potential).
FT   TRANSMEM      9     29       Helical; Signal-anchor for type II
FT                                membrane protein; (Potential).
FT   TOPO_DOM     30    336       Cytoplasmic (Potential).
FT   ACT_SITE    148    148       Charge relay system (By similarity).
FT   ACT_SITE    278    278       Charge relay system (By similarity).
FT   ACT_SITE    306    306       Charge relay system (By similarity).
FT   VAR_SEQ       1     47       Missing (in isoform 2).
FT                                /FTId=VSP_024012.
FT   CONFLICT     85     85       D -> G (in Ref. 1; BAB22430).
FT   CONFLICT    173    173       P -> A (in Ref. 1; BAB22430).
SQ   SEQUENCE   336 AA;  38205 MW;  4C207C66DBE41FE4 CRC64;
     MDLDVVNMFV IAGGTLAIPI LAFVASFLLW PSALIRIYYW YWRRTLGMQV RYAHHEDYQF
     CYSFRGRPGH KPSILMLHGF SAHKDMWLSV VKFLPKNLHL VCVDMPGHEG TTRSSLDDLS
     IVGQVKRIHQ FVECLKLNKK PFHLIGTSMG GHVAGVYAAY YPSDVCSLSL VCPAGLQYST
     DNPFVQRLKE LEESAAIQKI PLIPSTPEEM SEMLQLCSYV RFKVPQQILQ GLVDVRIPHN
     SFYRKLFLEI VNEKSRYSLH ENMDKIKVPT QIIWGKQDQV LDVSGADILA KSISNSQVEV
     LENCGHSVVM ERPRKTAKLI VDFLASVHNT DNKKLN
//
ID   TMCC3_MOUSE             Reviewed;         477 AA.
AC   Q8R310; Q501N6;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Transmembrane and coiled-coil domains protein 3;
GN   Name=Tmcc3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=129, Czech II, and NMRI; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-48, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R310-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R310-2; Sequence=VSP_025999;
CC   -!- SIMILARITY: Belongs to the TEX28 family.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK132545; BAE21229.1; -; mRNA.
DR   EMBL; BC026867; AAH26867.1; -; mRNA.
DR   EMBL; BC057202; AAH57202.1; -; mRNA.
DR   EMBL; BC095951; AAH95951.1; -; mRNA.
DR   IPI; IPI00225221; -.
DR   IPI; IPI00762409; -.
DR   RefSeq; NP_001162155.1; NM_001168684.1.
DR   RefSeq; NP_742048.2; NM_172051.3.
DR   RefSeq; NP_796000.1; NM_177026.1.
DR   UniGene; Mm.23047; -.
DR   ProteinModelPortal; Q8R310; -.
DR   PhosphoSite; Q8R310; -.
DR   PRIDE; Q8R310; -.
DR   Ensembl; ENSMUST00000065060; ENSMUSP00000063264; ENSMUSG00000020023.
DR   GeneID; 319880; -.
DR   KEGG; mmu:319880; -.
DR   UCSC; uc007gvt.1; mouse.
DR   CTD; 319880; -.
DR   MGI; MGI:2442900; Tmcc3.
DR   eggNOG; roNOG12583; -.
DR   GeneTree; ENSGT00390000007639; -.
DR   HOGENOM; HBG443696; -.
DR   HOVERGEN; HBG057342; -.
DR   InParanoid; Q8R310; -.
DR   OMA; NAPIELA; -.
DR   OrthoDB; EOG4WWRJH; -.
DR   PhylomeDB; Q8R310; -.
DR   NextBio; 395575; -.
DR   ArrayExpress; Q8R310; -.
DR   Bgee; Q8R310; -.
DR   CleanEx; MM_TMCC3; -.
DR   Genevestigator; Q8R310; -.
DR   GermOnline; ENSMUSG00000020023; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR019394; Predicted_TM_coiled-coil_2.
DR   Pfam; PF10267; Tmemb_cc2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    477       Transmembrane and coiled-coil domains
FT                                protein 3.
FT                                /FTId=PRO_0000184600.
FT   TRANSMEM    409    429       Helical; (Potential).
FT   COILED       63     83       Potential.
FT   COILED      112    149       Potential.
FT   COILED      284    398       Potential.
FT   MOD_RES      48     48       Phosphothreonine.
FT   MOD_RES     216    216       Phosphoserine.
FT   VAR_SEQ       1     31       Missing (in isoform 2).
FT                                /FTId=VSP_025999.
SQ   SEQUENCE   477 AA;  53722 MW;  8848410F6E74A217 CRC64;
     MPGSDTALTV DRTYSDPGRH HRCKSRVDRH DMNTLSLPLN IRRGGSDTNL NFDVPDGILD
     FHKVKLNADS LRQKILKVTE QIKIEQTSRD GNVAEYLKLV SSADKQQAGR IKQVFEKKNQ
     KSAHSIAQLQ KKLEQYHRKL REIEQNGVTR SSKDISKDSL KEIHHSLKDA HVKSRTAPHC
     LESSKSSMPG VSLTPPVFVF NKSREFANLI RNKFGSADNI AHLKNSLEEF RPEASPRAYG
     GSATIVNKPK YGSDDECSSG TSGSADSNGN QSFGAGGTST LDSQGKIAKI MEELREIKVT
     QTQLAEDIEA LKVQFKREYG FISQTLQEER YRYERLEDQL HDLTELHQHE TANLKQELAS
     AEEKVAYQAY ERSRDIQEAL ESCQTRISKL ELHQQEQQTL QTDAVNAKVL LGKCINVVLA
     FMTVILVCVS TLAKFVSPMM KSRSHILGTF FAVTLLAIFC KNWDHILCAI ERIIIPR
//
ID   CTGE5_MOUSE             Reviewed;         779 AA.
AC   Q8R311; Q8CIE3;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-FEB-2011, entry version 58.
DE   RecName: Full=Cutaneous T-cell lymphoma-associated antigen 5 homolog;
DE            Short=Protein cTAGE-5;
DE   AltName: Full=Meningioma-expressed antigen 6;
GN   Name=Ctage5; Synonyms=Mea6, Mgea6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-623, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-561, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514 AND SER-654, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514 AND SER-526, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the cTAGE family.
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DR   EMBL; BC024076; AAH24076.1; -; mRNA.
DR   EMBL; BC026864; AAH26864.1; -; mRNA.
DR   IPI; IPI00153633; -.
DR   UniGene; Mm.244118; -.
DR   UniGene; Mm.438038; -.
DR   ProteinModelPortal; Q8R311; -.
DR   SMR; Q8R311; 47-173, 447-472.
DR   PhosphoSite; Q8R311; -.
DR   PRIDE; Q8R311; -.
DR   Ensembl; ENSMUST00000043421; ENSMUSP00000047061; ENSMUSG00000021000.
DR   UCSC; uc007nqf.1; mouse.
DR   MGI; MGI:1346056; Ctage5.
DR   GeneTree; ENSGT00530000063635; -.
DR   HOGENOM; HBG505569; -.
DR   HOVERGEN; HBG051216; -.
DR   InParanoid; Q8R311; -.
DR   NextBio; 375923; -.
DR   ArrayExpress; Q8R311; -.
DR   Bgee; Q8R311; -.
DR   CleanEx; MM_CTAGE5; -.
DR   Genevestigator; Q8R311; -.
DR   GermOnline; ENSMUSG00000021000; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Coiled coil; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    779       Cutaneous T-cell lymphoma-associated
FT                                antigen 5 homolog.
FT                                /FTId=PRO_0000189542.
FT   TRANSMEM     10     30       Helical; (Potential).
FT   COILED       62    250       Potential.
FT   COILED      297    470       Potential.
FT   COMPBIAS    531    536       Poly-Gly.
FT   COMPBIAS    652    774       Pro-rich.
FT   MOD_RES     115    115       Phosphoserine (By similarity).
FT   MOD_RES     495    495       Phosphoserine (By similarity).
FT   MOD_RES     500    500       Phosphoserine (By similarity).
FT   MOD_RES     514    514       Phosphoserine.
FT   MOD_RES     526    526       Phosphoserine.
FT   MOD_RES     561    561       Phosphoserine.
FT   MOD_RES     611    611       Phosphoserine (By similarity).
FT   MOD_RES     623    623       Phosphoserine.
FT   MOD_RES     654    654       Phosphoserine.
SQ   SEQUENCE   779 AA;  87718 MW;  77F6FC898BA833D8 CRC64;
     MRADFNPSGF SLELAVCVLS VGLLAVVLFL WRGFRSIRSR FYVGREKKLA LELSALIEEK
     CKLLDKVSIV QKEYEGLESS LKEASFEKES TEAQSLEFVE GSQISEATYE NLEQSKSKLE
     DEILLLEEKL EEERAKHSEQ DELMADISKR IQSLEDESKS LKSQVAEAKT TFRIFEINEE
     RLKGAIKDAL NENSQLQESQ KQLLQETEMM KEQVNDLDKQ KVALEESRAQ AEQALSEKES
     QIETLVTSLL KMKDWAAVLG EDIADDGNLD LDMKSGLENT AALDNQPKGA LKKLIYAAKL
     NASLKALEGE RNQVYTQLSE VDQVKEDLTE HIKSLESKQA SLQSEKTEFE SESQKLQQKL
     KVITELYQEN EMKLHRKLTV EENYRLEKEE KLSKVDEKIS HATEELETCR QRAKDLEEEL
     ERTIHSYQGQ VISHEKKAHD NWLAARTLER NLNDLRKENA HNRQKLTETE FKFELLEKDP
     YALDVPNTAF GREHSPYGPS PLGRPPSETR AFLSPPTLLE GPLRLSPLLP GGGGRGSRGP
     ENLLDHQMNT ERGESSYDRL SDAPRAPSDR SLSPPWEQDR RMTAHPPPGQ PYSDPALQRQ
     DRFYPNSGRL SGPAELRSYN MPSLDKVDGP VPSEMESSGN GTKDNLGNSN VPDSPIPAEC
     EAAGRGFFPP PFPPVRDPLF PVDPRSQFMR RGPSFPPPPP GSIYAAPRDY FPPRDFPGPP
     LPPFPGRTVY APRGFPPYLP PRAGFFPPPP HPESRSELPP DLIPPSKEPA ADPPETQEA
//
ID   EXOC6_MOUSE             Reviewed;         802 AA.
AC   Q8R313;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2002, sequence version 2.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Exocyst complex component 6;
DE   AltName: Full=Exocyst complex component Sec15A;
DE   AltName: Full=SEC15-like protein 1;
GN   Name=Exoc6; Synonyms=Sec15a, Sec15l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Component of the exocyst complex involved in the docking
CC       of exocystic vesicles with fusion sites on the plasma membrane (By
CC       similarity).
CC   -!- SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3,
CC       EXOC4, EXOC5, EXOC6, EXOC7 and EXOC8 (By similarity). Interacts
CC       with CEP110 (By similarity).
CC   -!- SIMILARITY: Belongs to the SEC15 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH26859.1; Type=Erroneous initiation;
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DR   EMBL; BC026859; AAH26859.1; ALT_INIT; mRNA.
DR   IPI; IPI00753681; -.
DR   UniGene; Mm.24865; -.
DR   ProteinModelPortal; Q8R313; -.
DR   SMR; Q8R313; 409-729.
DR   STRING; Q8R313; -.
DR   PRIDE; Q8R313; -.
DR   Ensembl; ENSMUST00000066439; ENSMUSP00000064332; ENSMUSG00000053799.
DR   MGI; MGI:1351611; Exoc6.
DR   GeneTree; ENSGT00390000005739; -.
DR   HOVERGEN; HBG057543; -.
DR   InParanoid; Q8R313; -.
DR   OrthoDB; EOG4DNF3S; -.
DR   PhylomeDB; Q8R313; -.
DR   ArrayExpress; Q8R313; -.
DR   Bgee; Q8R313; -.
DR   CleanEx; MM_EXOC6; -.
DR   Genevestigator; Q8R313; -.
DR   GermOnline; ENSMUSG00000053799; Mus musculus.
DR   GO; GO:0000145; C:exocyst; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; IEA:InterPro.
DR   InterPro; IPR007225; Sec15.
DR   PANTHER; PTHR12702; Sec15; 1.
DR   Pfam; PF04091; Sec15; 1.
DR   PIRSF; PIRSF025007; Sec15; 1.
PE   2: Evidence at transcript level;
KW   Exocytosis; Protein transport; Transport.
FT   CHAIN         1    802       Exocyst complex component 6.
FT                                /FTId=PRO_0000118952.
SQ   SEQUENCE   802 AA;  93077 MW;  7AA82DCADBCD8E8B CRC64;
     MAESCEALGT VPEHERILQE IESTDTACVG PTLRSVYDDQ PNAHKKFMEK LDACIRNHDK
     EIEKMCNFHH QGFVDAITEL LKVRADAEKL KVTDTNRRFQ DAGKEVIIQT EDIIRCRIQQ
     RNITTVVEKL QLCLPVLEMY SKLKEQMSMK RYYSALKTME QLENVYFPRV SQYRFCQLMM
     ETLPKLREDM MNYCMSDLTY GLESIRKHSD KIGEAAMKQA QQQKSFSVAL QKQNNMRFGK
     NMHVNNDRIL EEKSDVIPKH ALEEEAENDE EVLTVQDLVD FSPVYRCLHI YSALGDEETF
     ENYYRKQRKK QARLVLQPQS SVHETVDGYR RYFTQIVGFF VVEDHILHVT QGLVTRVYTE
     ELWNMALSKI IAVLRAHSSY CTDPDLVLEL KNLIVIFADT LQGYGFPVNR LFDLLFEIRD
     QYNETLLKKW AGIFRDIFEE DNYSPIPIGS EEEYKVVISR FPFQDPDLEK QSFPKKFPMS
     QSVPLIYIQV KEFIYASLKF SESLHRSSTE IDDMLRKSTN LLLTRILSSC LLNLIRKPHI
     GLTELVQIII NTTHLEQACK YLEDFITNIT NISQETVHTT RLYGLSTFKD ARHAAEGEIY
     TKLNQKIDEF VQLADYDWTM AESDGRASGY LMDLINFLRS IFQVFTHLPG KVAQTACMSA
     CQHLSTSLMQ MLLDSELKQI SMGAVQQFNL DVIQCELFAS SEPVPGFQGD TLQLAFIDLR
     QLLDLFMVWD WSTYLADYGQ PASKYLRVNP HAALTLLEKM KDTSKKNNIF AQFRKNDRDR
     QKLIETVVRQ LRGLVTGMSQ HT
//
ID   PSPC1_MOUSE             Reviewed;         523 AA.
AC   Q8R326; Q3TUK2; Q9CYH1; Q9D0M8;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Paraspeckle component 1;
DE   AltName: Full=Paraspeckle protein 1;
DE            Short=mPSP1;
GN   Name=Pspc1; Synonyms=Psp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH NONO AND SFPQ, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=15140795; DOI=10.1095/biolreprod.104.028159;
RA   Myojin R., Kuwahara S., Yasaki T., Matsunaga T., Sakurai T.,
RA   Kimura M., Uesugi S., Kurihara Y.;
RT   "Expression and functional significance of mouse paraspeckle protein 1
RT   on spermatogenesis.";
RL   Biol. Reprod. 71:926-932(2004).
RN   [4]
RP   IDENTIFICATION IN A RNP COMPLEX WITH CTN-RNA.
RX   PubMed=16239143; DOI=10.1016/j.cell.2005.08.033;
RA   Prasanth K.V., Prasanth S.G., Xuan Z., Hearn S., Freier S.M.,
RA   Bennett C.F., Zhang M.Q., Spector D.L.;
RT   "Regulating gene expression through RNA nuclear retention.";
RL   Cell 123:249-263(2005).
RN   [5]
RP   FUNCTION, INTERACTION WITH NONO AND SFPQ, MUTAGENESIS OF PHE-118;
RP   PHE-120; LYS-197 AND PHE-199, MASS SPECTROMETRY, SUBCELLULAR LOCATION,
RP   AND TISSUE SPECIFICITY.
RX   PubMed=16641145; DOI=10.1095/biolreprod.106.051136;
RA   Kuwahara S., Ikei A., Taguchi Y., Tabuchi Y., Fujimoto N., Obinata M.,
RA   Uesugi S., Kurihara Y.;
RT   "PSPC1, NONO, and SFPQ are expressed in mouse Sertoli cells and may
RT   function as coregulators of androgen receptor-mediated
RT   transcription.";
RL   Biol. Reprod. 75:352-359(2006).
CC   -!- FUNCTION: Regulates, cooperatively with NONO and SFPQ, androgen
CC       receptor-mediated gene transcription activity in Sertoli cell
CC       line. Binds to poly(A), poly(G) and poly(U) RNA homopolymers.
CC   -!- SUBUNIT: Forms heterodimers with NONO (By similarity). Interaction
CC       with NONO is required for its targeting to paraspeckles and
CC       perinucleolar caps (By similarity). Found in a RNP complex with
CC       CAT2 transcribed nuclear RNA (CTN-RNA). Interacts with NONO and
CC       SFPQ.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity). Note=In
CC       punctate subnuclear structures localized adjacent to nuclear
CC       splicing speckles, called paraspeckles (By similarity).
CC       Colocalizes with NONO and SFPQ in paraspeckles and perinucleolar
CC       caps in a RNA-dependent manner (By similarity). May cycles between
CC       paraspeckles and nucleolus (By similarity). In telophase, when
CC       daughter nuclei form, localizes to perinucleolar caps (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Nucleus matrix. Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=PSP1-alpha;
CC         IsoId=Q8R326-1; Sequence=Displayed;
CC       Name=2; Synonyms=PSP1-beta;
CC         IsoId=Q8R326-2; Sequence=VSP_027276, VSP_027277;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is strongly expressed in testis
CC       (leptoten spermatocytes, round spematids and Sertoli cells) and
CC       moderately in cerebrum, cerebellum, lung, spleen and ovary (at
CC       protein level). Isoform 2 is strongly expressed in kidney and
CC       moderately in salivary gland (at protein level).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the PSPC family.
CC   -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
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DR   EMBL; AK011272; BAB27509.2; -; mRNA.
DR   EMBL; AK017689; BAB30876.2; -; mRNA.
DR   EMBL; AK150823; BAE29885.1; -; mRNA.
DR   EMBL; AK160722; BAE35969.1; -; mRNA.
DR   EMBL; BC026772; AAH26772.1; -; mRNA.
DR   IPI; IPI00321266; -.
DR   IPI; IPI00857897; -.
DR   RefSeq; NP_079958.3; NM_025682.3.
DR   UniGene; Mm.20129; -.
DR   HSSP; Q99K48; 2CPJ.
DR   ProteinModelPortal; Q8R326; -.
DR   SMR; Q8R326; 74-277.
DR   IntAct; Q8R326; 1.
DR   MINT; MINT-218330; -.
DR   STRING; Q8R326; -.
DR   PhosphoSite; Q8R326; -.
DR   PRIDE; Q8R326; -.
DR   Ensembl; ENSMUST00000022507; ENSMUSP00000022507; ENSMUSG00000021938.
DR   GeneID; 66645; -.
DR   KEGG; mmu:66645; -.
DR   NMPDR; fig|10090.3.peg.29164; -.
DR   UCSC; uc007ucj.1; mouse.
DR   CTD; 66645; -.
DR   MGI; MGI:1913895; Pspc1.
DR   eggNOG; roNOG07542; -.
DR   GeneTree; ENSGT00390000005004; -.
DR   HOGENOM; HBG715412; -.
DR   HOVERGEN; HBG009801; -.
DR   InParanoid; Q8R326; -.
DR   OMA; DNREQEM; -.
DR   OrthoDB; EOG444KKN; -.
DR   PhylomeDB; Q8R326; -.
DR   NextBio; 322261; -.
DR   ArrayExpress; Q8R326; -.
DR   Bgee; Q8R326; -.
DR   CleanEx; MM_PSPC1; -.
DR   Genevestigator; Q8R326; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042382; C:paraspeckles; IDA:MGI.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR012975; NOPS.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   Pfam; PF08075; NOPS; 1.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Alternative splicing; Coiled coil; Cytoplasm;
KW   Nucleus; Phosphoprotein; Repeat; RNA-binding; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    523       Paraspeckle component 1.
FT                                /FTId=PRO_0000297541.
FT   DOMAIN       81    153       RRM 1.
FT   DOMAIN      155    236       RRM 2.
FT   REGION      124    357       Sufficient for paraspeckles localization
FT                                (By similarity).
FT   REGION      230    357       Sufficient for perinucleolar caps
FT                                localization and interaction with NONO
FT                                (By similarity).
FT   COILED      282    376       Potential.
FT   COMPBIAS    394    516       Gly-rich.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     205    205       N6-acetyllysine (By similarity).
FT   MOD_RES     473    473       Phosphoserine (By similarity).
FT   MOD_RES     477    477       Phosphoserine (By similarity).
FT   MOD_RES     509    509       Phosphoserine (By similarity).
FT   VAR_SEQ     463    466       HNDR -> VMYH (in isoform 2).
FT                                /FTId=VSP_027276.
FT   VAR_SEQ     467    523       Missing (in isoform 2).
FT                                /FTId=VSP_027277.
FT   MUTAGEN     118    118       F->A: Abolishes RNA-binding activity but
FT                                not AR-mediated transcription
FT                                coactivation; when associated with A-120;
FT                                A-197 and A-199.
FT   MUTAGEN     120    120       F->A: Abolishes RNA-binding activity but
FT                                not AR-mediated transcription
FT                                coactivation; when associated with A-118;
FT                                A-197 and A-199.
FT   MUTAGEN     197    197       K->A: Abolishes RNA-binding activity but
FT                                not AR-mediated transcription
FT                                coactivation; when associated with A-118;
FT                                A-120 and A-199.
FT   MUTAGEN     199    199       F->A: Abolishes RNA-binding activity but
FT                                not AR-mediated transcription
FT                                coactivation; when associated with A-118;
FT                                A-120 and A-197.
FT   CONFLICT    349    349       L -> Q (in Ref. 1; BAB30876).
SQ   SEQUENCE   523 AA;  58758 MW;  1F6804934C98432B CRC64;
     MMLRGNLKQV RIEKNPARLR ALESAAGESE PVAAAAMALT LAGEQAPPPA PSEEHPDEEL
     GFTIDIKSFL KPGEKTYTQR CRLFVGNLPT DITEEDFKRL FERYGEPSEV FINRDRGFGF
     IRLESRTLAE IAKAELDGTI LKSRPLRIRF ATHGAALTVK NLSPVVSNEL LEQAFSQFGP
     VEKAVVVVDD RGRATGKGFV EFAAKPPARK ALERCGDGAF LLTTTPRPVI VEPMEQFDDE
     DGLPEKLMQK TQQYHKEREQ PPRFAQPGTF EFEYASRWKA LDEMEKQQRE QVDRNIREAK
     EKLEAEMEAA RHEHQLMLMR QDLMRRQEEL RRLEELRNQE LQKRKQIQLR HEEEHRRREE
     EMIRHREQEE LRRQQEGGFK PNYMENREQE MRMGDMGPRG AINMGDAFSP APAGTQGPPP
     MMGMNMNNRG TIPGPPMGPG PAMGPEGAAN MGTPMIPDNG AVHNDRFPQG PPSQMGSPMG
     NRTGSETPQA PMSGVGPVSG GPGGFGRGSQ GGNFEGPNKR RRY
//
ID   CCD12_MOUSE             Reviewed;         166 AA.
AC   Q8R344; Q9CZH5;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Coiled-coil domain-containing protein 12;
GN   Name=Ccdc12;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-157, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
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DR   EMBL; AK012610; BAB28353.1; -; mRNA.
DR   EMBL; BC026668; AAH26668.1; -; mRNA.
DR   IPI; IPI00319221; -.
DR   RefSeq; NP_082588.2; NM_028312.3.
DR   UniGene; Mm.249115; -.
DR   ProteinModelPortal; Q8R344; -.
DR   PhosphoSite; Q8R344; -.
DR   PRIDE; Q8R344; -.
DR   Ensembl; ENSMUST00000019803; ENSMUSP00000019803; ENSMUSG00000019659.
DR   GeneID; 72654; -.
DR   KEGG; mmu:72654; -.
DR   UCSC; uc009rum.1; mouse.
DR   CTD; 72654; -.
DR   MGI; MGI:1919904; Ccdc12.
DR   eggNOG; roNOG07318; -.
DR   GeneTree; ENSGT00390000011619; -.
DR   HOGENOM; HBG716021; -.
DR   HOVERGEN; HBG059850; -.
DR   InParanoid; Q8R344; -.
DR   OMA; KGQEDNL; -.
DR   OrthoDB; EOG4PNXJD; -.
DR   PhylomeDB; Q8R344; -.
DR   NextBio; 336657; -.
DR   ArrayExpress; Q8R344; -.
DR   Bgee; Q8R344; -.
DR   CleanEx; MM_CCDC12; -.
DR   Genevestigator; Q8R344; -.
DR   GermOnline; ENSMUSG00000019659; Mus musculus.
DR   InterPro; IPR013169; mRNA_splic_Cwf18.
DR   Pfam; PF08315; cwf18; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Phosphoprotein.
FT   CHAIN         1    166       Coiled-coil domain-containing protein 12.
FT                                /FTId=PRO_0000076192.
FT   COILED        8     28       Potential.
FT   COILED      115    144       Potential.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     157    157       Phosphothreonine.
FT   MOD_RES     165    165       Phosphoserine (By similarity).
FT   CONFLICT    119    119       D -> N (in Ref. 1; BAB28353).
FT   CONFLICT    151    151       A -> P (in Ref. 2; AAH26668).
SQ   SEQUENCE   166 AA;  18891 MW;  D40AF91AED281D12 CRC64;
     MAAAPAGVGR LEEEALRRKE RLKALREKTG RKDREDGEPQ TKQLREEGEE VGKHRGLRLR
     NYVPEDEDLK RRRVPQAKPV AVEEKVKEQL EAAKPEPVIE EVDLANLAPR KPDWDLKRDV
     AKKLEKLEKR TQRAIAELIR ERLKGQEDSL ASAVDATTGQ EACDSD
//
ID   CDC16_MOUSE             Reviewed;         620 AA.
AC   Q8R349; Q9CYX9;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Cell division cycle protein 16 homolog;
DE   AltName: Full=Anaphase-promoting complex subunit 6;
DE            Short=APC6;
DE   AltName: Full=Cyclosome subunit 6;
GN   Name=Cdc16; Synonyms=Anapc6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 325-620.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC       (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls
CC       progression through mitosis and the G1 phase of the cell cycle.
CC       The APC/C complex acts by mediating ubiquitination and subsequent
CC       degradation of target proteins: it mainly mediates the formation
CC       of 'Lys-11'-linked polyubiquitin chains and, to a lower extent,
CC       the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin
CC       chains (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: The APC/C is composed of at least 12 subunits. Interacts
CC       with PPP5C and CDC20 (By similarity).
CC   -!- PTM: Phosphorylated. Phosphorylation on Ser-560 occurs
CC       specifically during mitosis (By similarity).
CC   -!- SIMILARITY: Belongs to the APC6/CDC16 family.
CC   -!- SIMILARITY: Contains 7 TPR repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB28717.1; Type=Miscellaneous discrepancy; Note=Intron retention;
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DR   EMBL; BC026606; AAH26606.1; -; mRNA.
DR   EMBL; AK013213; BAB28717.1; ALT_SEQ; mRNA.
DR   IPI; IPI00221621; -.
DR   RefSeq; NP_081552.2; NM_027276.2.
DR   UniGene; Mm.182412; -.
DR   ProteinModelPortal; Q8R349; -.
DR   SMR; Q8R349; 5-98, 228-529.
DR   STRING; Q8R349; -.
DR   PhosphoSite; Q8R349; -.
DR   PRIDE; Q8R349; -.
DR   Ensembl; ENSMUST00000043962; ENSMUSP00000047950; ENSMUSG00000038416.
DR   GeneID; 69957; -.
DR   KEGG; mmu:69957; -.
DR   UCSC; uc009kyi.1; mouse.
DR   CTD; 69957; -.
DR   MGI; MGI:1917207; Cdc16.
DR   HOGENOM; HBG559313; -.
DR   HOVERGEN; HBG050857; -.
DR   InParanoid; Q8R349; -.
DR   OMA; HFLFENK; -.
DR   OrthoDB; EOG4DBTD7; -.
DR   PhylomeDB; Q8R349; -.
DR   NextBio; 330683; -.
DR   ArrayExpress; Q8R349; -.
DR   Bgee; Q8R349; -.
DR   Genevestigator; Q8R349; -.
DR   GermOnline; ENSMUSG00000038416; Mus musculus.
DR   GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR   InterPro; IPR001440; TPR-1.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 2.
DR   Pfam; PF00515; TPR_1; 2.
DR   SMART; SM00028; TPR; 4.
DR   PROSITE; PS50005; TPR; 5.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Mitosis; Phosphoprotein; Repeat;
KW   TPR repeat; Ubl conjugation pathway.
FT   CHAIN         1    620       Cell division cycle protein 16 homolog.
FT                                /FTId=PRO_0000106268.
FT   REPEAT      130    163       TPR 1.
FT   REPEAT      299    333       TPR 2.
FT   REPEAT      334    367       TPR 3.
FT   REPEAT      369    401       TPR 4.
FT   REPEAT      403    435       TPR 5.
FT   REPEAT      445    478       TPR 6.
FT   REPEAT      479    512       TPR 7.
FT   MOD_RES     490    490       Phosphoserine (By similarity).
FT   MOD_RES     560    560       Phosphoserine (By similarity).
FT   MOD_RES     599    599       Phosphothreonine (By similarity).
SQ   SEQUENCE   620 AA;  71460 MW;  A0E47748506CC14E CRC64;
     MNLEPLRKRV RQYLDQQQYQ SALFWADKVA SLSHEEPQDV YWLAQCLYLT AQYHRAAHAL
     RSRKLDKLYE ACRYLAARCH YAAKEHQQAL DILDMEEPIN RRLFEKYLKD DNGSRDPSSD
     WEMSQSSIKS SICLLRGKIY DALDNRTLAT YSYKEALKLD VYCFEAFDLL TSHHMLTAQE
     EKELLDSLPL NKLCAEEQEL LRFVFENKLK KYNKPSETVI PESVDGLQEN LDVVVSLAER
     HYYNCDFKMC YKLTSTVMEK DPFHANCLPV HIGTLVELNK ANELFYLSHK LVDLYPSNPV
     SWFAVGCYYL MVGHKNEHAR RYLSKATTLE KTYGPAWIAY GHSFAVESEH DQAMAAYFTA
     AQLMKGCHLP MLYIGLEYGL TNNSKLAERF FGQALSIAPE DPFVIHEVGV VAFQNGEWKT
     AEKWFLDALE KIKAIGNEVT VDKWEPLLNN LGHVCRKLKK YAEALDYHRQ ALVLIPQNAS
     TYSAIGYIHS LMGNFENAVD YFHTALGLRR DDTFSVTMLG HCIEMYIGDS EAYIGADIKD
     KLKCYDFDVH TMKTLKNIIS PPWDFRDFEV EKQNTEEAGL APLQNSTKAP ESRPNLEETF
     EIEMNESDMM LETSMSDHST
//
ID   RFIP5_MOUSE             Reviewed;         645 AA.
AC   Q8R361; C4IXU4;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2003, sequence version 2.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Rab11 family-interacting protein 5;
DE            Short=Rab11-FIP5;
DE   AltName: Full=Rab11-interacting protein Rip11;
GN   Name=Rab11fip5; Synonyms=D6Ertd32e, Rip11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 382-389, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-306, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Rab effector involved in protein trafficking from apical
CC       recycling endosomes to the apical plasma membrane (By similarity).
CC   -!- SUBUNIT: Forms an heterooligomeric complex with RAB11FIP4. Binds
CC       NAPG and TROVE2. Binds RAB11A that has been activated by GTP
CC       binding (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Recycling
CC       endosome membrane; Peripheral membrane protein (By similarity).
CC       Mitochondrion membrane; Peripheral membrane protein (By
CC       similarity).
CC   -!- DOMAIN: Binds to vesicles enriched in neutral phospholipids via
CC       its C2 domain. The interaction is favored by Mg(2+) rather than
CC       Ca(2+) (By similarity).
CC   -!- PTM: Phosphorylated on serine and threonine residues (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 FIP-RBD domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AC153605; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC155728; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC026473; AAH26473.1; -; mRNA.
DR   EMBL; BC044833; AAH44833.2; -; mRNA.
DR   EMBL; BC051063; AAH51063.3; -; mRNA.
DR   EMBL; BC141380; AAI41381.1; -; mRNA.
DR   IPI; IPI00230238; -.
DR   RefSeq; NP_001003955.1; NM_001003955.2.
DR   RefSeq; NP_803417.3; NM_177466.4.
DR   UniGene; Mm.220334; -.
DR   ProteinModelPortal; Q8R361; -.
DR   SMR; Q8R361; 20-150, 588-644.
DR   STRING; Q8R361; -.
DR   PhosphoSite; Q8R361; -.
DR   PRIDE; Q8R361; -.
DR   Ensembl; ENSMUST00000060837; ENSMUSP00000058305; ENSMUSG00000051343.
DR   GeneID; 52055; -.
DR   KEGG; mmu:52055; -.
DR   UCSC; uc009cpo.1; mouse.
DR   CTD; 52055; -.
DR   MGI; MGI:1098586; Rab11fip5.
DR   GeneTree; ENSGT00530000063203; -.
DR   HOVERGEN; HBG079127; -.
DR   NextBio; 308438; -.
DR   ArrayExpress; Q8R361; -.
DR   Bgee; Q8R361; -.
DR   CleanEx; MM_RAB11FIP5; -.
DR   Genevestigator; Q8R361; -.
DR   GermOnline; ENSMUSG00000051343; Mus musculus.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043015; F:gamma-tubulin binding; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR019018; Rab11-bd_FIP_dom_C.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF09457; RBD-FIP; 1.
DR   SMART; SM00239; C2; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS51511; FIP_RBD; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Endosome; Membrane;
KW   Mitochondrion; Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1    645       Rab11 family-interacting protein 5.
FT                                /FTId=PRO_0000097308.
FT   DOMAIN        6    128       C2.
FT   DOMAIN      578    640       FIP-RBD.
FT   COMPBIAS    243    397       Ser-rich.
FT   MOD_RES     174    174       Phosphoserine (By similarity).
FT   MOD_RES     188    188       Phosphoserine (By similarity).
FT   MOD_RES     306    306       Phosphotyrosine.
FT   MOD_RES     307    307       Phosphoserine.
FT   MOD_RES     359    359       Phosphoserine (By similarity).
FT   MOD_RES     530    530       Phosphoserine (By similarity).
FT   MOD_RES     545    545       Phosphoserine (By similarity).
SQ   SEQUENCE   645 AA;  69553 MW;  CBA713E9E68A042A CRC64;
     MALVRDPEPA AGSSRWLPTH VQVTVLRASG LRGKSSGAGS TSDAYTVIQV GREKYSTSVV
     EKTQGCPEWC EECSFELPPG ALDGLLRAQE ADAGPAPWAS GPNAACELVL TTMHRSLIGV
     DKFLGRATVA LDEVFRAGRA QHTQWYRLHS KPGKKEKERG EIQVTIQFTR NNLSASMFDL
     SMKDKPRSPF SKLKDRVKGK KKYDLESASA ILPSSALEDP ELGSLGKMGK AKGFFLRNKL
     RKSSLTQSNT SLGSDSTLSS TSGSLVYQGP GAELLTRSPS HSSWLSTEGG RDSIQSPKLL
     THKRTYSDEA SQLRAAPPRA LLELQGHLDG ASRSSLCVNG SHVYNEEPQP PLRHRSSISG
     PFPPSSSLHS VPPRSSEEGS RSSDDSWGRG SHGTSSSEAV PGQEELSKQA KGASCSGEEE
     GARLPEGKPV QVATPMVASS EAVAAEKDRK PRMGLFHHHH HQGLSRSEQG RRGSVGEKGS
     PSLGASPHHS STGEEKAKSS WFGLRESKEP TQKPSPHPVK PLTAAPVEAS PDRKQPRTSL
     STALSSGLER LKTVTSGGIQ SVLPASQLGS SVDTKRPKDS AVLDQSAKYY HLTHDELIGL
     LLQRERELSQ RDEHVQELES YIDRLLVRIM ETSPTLLQIS PGPPK
//
ID   PLCD1_MOUSE             Reviewed;         756 AA.
AC   Q8R3B1;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-1;
DE            EC=3.1.4.11;
DE   AltName: Full=Phosphoinositide phospholipase C-delta-1;
DE   AltName: Full=Phospholipase C-delta-1;
DE            Short=PLC-delta-1;
GN   Name=Plcd1; Synonyms=Plcd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16314520; DOI=10.1128/MCB.25.24.10979-10988.2005;
RA   Nakamura Y., Hamada Y., Fujiwara T., Enomoto H., Hiroe T., Tanaka S.,
RA   Nose M., Nakahara M., Yoshida N., Takenawa T., Fukami K.;
RT   "Phospholipase C-delta1 and -delta3 are essential in the trophoblast
RT   for placental development.";
RL   Mol. Cell. Biol. 25:10979-10988(2005).
CC   -!- FUNCTION: The production of the second messenger molecules
CC       diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is
CC       mediated by activated phosphatidylinositol-specific phospholipase
CC       C enzymes. Essential for trophoblast and placental development.
CC   -!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-
CC       bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate +
CC       diacylglycerol.
CC   -!- COFACTOR: Binds 3 calcium ions per subunit. Two of the calcium
CC       ions are bound to the C2 domain (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice lacking Plcd1 and Plcd3 die at
CC       embryonic day 11.5 (E11.5) to E13.5 and exhibit severe disruption
CC       of the normal labyrinth architecture in the placenta and decreased
CC       placental vascularization, as well as abnormal proliferation and
CC       apoptosis of trophoblasts in the labyrinth area. Furthermore,
CC       Plcd1 and Plcd3 double-knockout embryos supplied with a normal
CC       placenta by the tetraploid aggregation method survive beyond
CC       E14.5, clearly indicating that the embryonic lethality is caused
CC       by a defect in trophoblasts.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 PI-PLC X-box domain.
CC   -!- SIMILARITY: Contains 1 PI-PLC Y-box domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC025798; AAH25798.1; -; mRNA.
DR   IPI; IPI00321515; -.
DR   UniGene; Mm.23963; -.
DR   ProteinModelPortal; Q8R3B1; -.
DR   SMR; Q8R3B1; 12-129, 158-756.
DR   STRING; Q8R3B1; -.
DR   PhosphoSite; Q8R3B1; -.
DR   PRIDE; Q8R3B1; -.
DR   Ensembl; ENSMUST00000010804; ENSMUSP00000010804; ENSMUSG00000010660.
DR   MGI; MGI:97614; Plcd1.
DR   HOGENOM; HBG527074; -.
DR   HOVERGEN; HBG053610; -.
DR   InParanoid; Q8R3B1; -.
DR   OrthoDB; EOG4H19V6; -.
DR   PhylomeDB; Q8R3B1; -.
DR   BRENDA; 3.1.4.11; 244.
DR   ArrayExpress; Q8R3B1; -.
DR   Bgee; Q8R3B1; -.
DR   CleanEx; MM_PLCD1; -.
DR   Genevestigator; Q8R3B1; -.
DR   GermOnline; ENSMUSG00000010660; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:EC.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0001525; P:angiogenesis; IGI:MGI.
DR   GO; GO:0060716; P:labyrinthine layer blood vessel development; IGI:MGI.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0042127; P:regulation of cell proliferation; IGI:MGI.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR015359; Phospholipase_C_EF-hand-like.
DR   InterPro; IPR001711; Phospholipase_C_Pinositol-sp_Y.
DR   InterPro; IPR001192; Pinositol_Phospholipase-C.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:3.20.20.190; PLC-like_Pdiesterase_TIM-brl; 2.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF09279; efhand_like; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00388; PI-PLC-X; 1.
DR   Pfam; PF00387; PI-PLC-Y; 1.
DR   PRINTS; PR00390; PHPHLIPASEC.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00148; PLCXc; 1.
DR   SMART; SM00149; PLCYc; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF51695; PLC-like_Pdiesterase_TIM-brl; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Hydrolase; Lipid degradation; Metal-binding; Repeat;
KW   Transducer.
FT   CHAIN         1    756       1-phosphatidylinositol-4,5-bisphosphate
FT                                phosphodiesterase delta-1.
FT                                /FTId=PRO_0000088505.
FT   DOMAIN       21    130       PH.
FT   DOMAIN      140    175       EF-hand 1.
FT   DOMAIN      176    211       EF-hand 2.
FT   DOMAIN      296    440       PI-PLC X-box.
FT   DOMAIN      492    609       PI-PLC Y-box.
FT   DOMAIN      630    720       C2.
FT   CA_BIND     153    164       1 (Potential).
FT   CA_BIND     189    200       2 (Potential).
FT   REGION       30     57       Substrate binding (By similarity).
FT   ACT_SITE    311    311       By similarity.
FT   ACT_SITE    356    356       By similarity.
FT   METAL       312    312       Calcium 1; catalytic (By similarity).
FT   METAL       341    341       Calcium 1; catalytic (By similarity).
FT   METAL       343    343       Calcium 1; catalytic (By similarity).
FT   METAL       390    390       Calcium 1; catalytic (By similarity).
FT   METAL       651    651       Calcium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       653    653       Calcium 2 (By similarity).
FT   METAL       677    677       Calcium 2 (By similarity).
FT   METAL       706    706       Calcium 3 (By similarity).
FT   METAL       707    707       Calcium 3; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       708    708       Calcium 3 (By similarity).
FT   BINDING     438    438       Substrate (By similarity).
FT   BINDING     440    440       Substrate (By similarity).
FT   BINDING     522    522       Substrate (By similarity).
FT   BINDING     549    549       Substrate (By similarity).
SQ   SEQUENCE   756 AA;  85901 MW;  74AB0C33E1A0B938 CRC64;
     MDSGRDFLTL HGLQDDPDLQ ALLKGSQLLK VKSSSWRRER FYKLQEDCKT IWQESRKVMR
     SPESQLFSIE DIQEVRMGHR TEGLEKFARD IPEDRCFSIV FKDQRNTLDL IAPSPADVQH
     WVQGLRKIID RSGSMDQRQK LQHWIHSCLR KADKNKDNKM NFKEVKDFLK ELNVQVDDSY
     ARKIFRECDH SQTDSLEDEE IETFYRMLTQ RVEIDRAFAE AAGSAETLSV EKLVTFLQHQ
     QREEEAGPAL ALSLIERYEP SETAKAQRQM TKDGFLMYLL SADGNAFSLA HRRVYQDMNQ
     PLSHYLVSSS HNTYLLEDQL TGPSSTEAYI RALCKGCRCL ELDCWDGPNQ EPIIYHGYTF
     TSKILFCDVL RAIRDYAFKA SPYPVILSLE NHCSLEQQRV MAHHLRAILG PMLLDQPLDG
     VTTSLPSPEQ LKEKILLKGK KLGGLLPAGG ENGPEATDVS DEDEAAEMED EAVRSQVQHK
     PKEDKLKLVP ELSDMVIYCK SVHFGGFSSP STSGQAFYEM ASFSESRALR LLQESGNSFV
     RHNVGHLSRI YPAGWRTDSS NYSPVEMWNG GCQIVALNFQ TPGPEMDVYL GCFQDNGGCG
     YVLKPAFLRD PDTTFNSRAL TQGPWWAPKK LRVWIISGQQ LPKVNKNKNS IVDPKVIVEI
     HGVGQDVASR QTAVITNNGF NPRWDTEFEF VVAVPDLALV RFMVEDYDSS SKNDFIGQST
     IPWNSLKQGY RHVHLLSKNG DLHPSATLFV KISIQD
//
ID   WIPI1_MOUSE             Reviewed;         446 AA.
AC   Q8R3E3; Q8BGE1; Q8R1A9; Q8R1C7;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=WD repeat domain phosphoinositide-interacting protein 1;
DE            Short=WIPI-1;
DE   AltName: Full=WD40 repeat protein interacting with phosphoinositides of 49 kDa;
DE            Short=WIPI 49 kDa;
GN   Name=Wipi1; Synonyms=D11Ertd498e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Dendritic cell, Embryo, Osteoclast, Pancreas, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 316-325, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: May play a role in autophagy. May regulate the
CC       trafficking of proteins involved in the mannose-6-phosphate
CC       receptor (MPR) recycling pathway (By similarity).
CC   -!- SUBUNIT: Probably interacts with androgen (AR) and the estrogen
CC       receptor (ER). Binds PtdIns3P and to a lesser extent, PtdIns3,5P2
CC       and PtdIns5P in vitro. Interaction with PtdIns3P is required for
CC       recruitment to membranes (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network (By
CC       similarity). Endosome (By similarity). Cytoplasmic vesicle,
CC       clathrin-coated vesicle (By similarity). Note=Trans elements of
CC       the Golgi and peripheral endosomes. Dynamically cycles through
CC       these compartments and is susceptible to conditions that modulate
CC       membrane flux. Enriched in clathrin-coated vesicles (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8R3E3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R3E3-2; Sequence=VSP_016969;
CC       Name=3;
CC         IsoId=Q8R3E3-3; Sequence=VSP_016967, VSP_016968;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the WD repeat SVP1 family.
CC   -!- SIMILARITY: Contains 3 WD repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH24811.1; Type=Erroneous initiation;
CC       Sequence=AAH24883.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK031672; BAC27504.1; -; mRNA.
DR   EMBL; AK034907; BAC28878.1; -; mRNA.
DR   EMBL; AK050495; BAE20673.1; -; mRNA.
DR   EMBL; AK159608; BAE35227.1; -; mRNA.
DR   EMBL; AK170563; BAE41884.1; -; mRNA.
DR   EMBL; BC024811; AAH24811.1; ALT_INIT; mRNA.
DR   EMBL; BC024883; AAH24883.1; ALT_INIT; mRNA.
DR   EMBL; BC025560; AAH25560.1; -; mRNA.
DR   IPI; IPI00153336; -.
DR   IPI; IPI00153737; -.
DR   IPI; IPI00649736; -.
DR   RefSeq; NP_666052.1; NM_145940.2.
DR   UniGene; Mm.35817; -.
DR   ProteinModelPortal; Q8R3E3; -.
DR   SMR; Q8R3E3; 147-201, 235-261, 313-352.
DR   PRIDE; Q8R3E3; -.
DR   Ensembl; ENSMUST00000047201; ENSMUSP00000039340; ENSMUSG00000041895.
DR   Ensembl; ENSMUST00000103060; ENSMUSP00000099349; ENSMUSG00000041895.
DR   GeneID; 52639; -.
DR   KEGG; mmu:52639; -.
DR   UCSC; uc007mcq.1; mouse.
DR   UCSC; uc007mcr.1; mouse.
DR   UCSC; uc007mcs.1; mouse.
DR   CTD; 52639; -.
DR   MGI; MGI:1261864; Wipi1.
DR   eggNOG; roNOG09255; -.
DR   GeneTree; ENSGT00530000062939; -.
DR   HOGENOM; HBG443829; -.
DR   HOVERGEN; HBG056639; -.
DR   InParanoid; Q8R3E3; -.
DR   OMA; GQKNICT; -.
DR   OrthoDB; EOG4Z36DZ; -.
DR   PhylomeDB; Q8R3E3; -.
DR   NextBio; 309255; -.
DR   ArrayExpress; Q8R3E3; -.
DR   Bgee; Q8R3E3; -.
DR   CleanEx; MM_WIPI1; -.
DR   Genevestigator; Q8R3E3; -.
DR   GermOnline; ENSMUSG00000041895; Mus musculus.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00320; WD40; 3.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR   PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Autophagy; Cytoplasmic vesicle;
KW   Direct protein sequencing; Endosome; Golgi apparatus; Repeat;
KW   WD repeat.
FT   CHAIN         1    446       WD repeat domain phosphoinositide-
FT                                interacting protein 1.
FT                                /FTId=PRO_0000051438.
FT   REPEAT      184    224       WD 1.
FT   REPEAT      230    269       WD 2.
FT   REPEAT      312    351       WD 3.
FT   MOTIF       131    136       Nuclear receptor interaction (By
FT                                similarity).
FT   VAR_SEQ     267    270       SRPE -> RCRT (in isoform 3).
FT                                /FTId=VSP_016967.
FT   VAR_SEQ     271    446       Missing (in isoform 3).
FT                                /FTId=VSP_016968.
FT   VAR_SEQ     432    446       IILCRGSQKGKTKQS -> VSIRNP (in isoform 2).
FT                                /FTId=VSP_016969.
SQ   SEQUENCE   446 AA;  48758 MW;  9F7FA1CB802E5344 CRC64;
     MEAEAADAPP GRVEAALSCF SFNQDCTSLA IGTKAGYKLF SLSSVEQLDQ VHGSNEIPDV
     YIVERLFSSS LVVVVSHTKP RQMNVYHFKK GTEICNYSYS SNILSIRLNR QRLLVCLEES
     IYIHNIKDMK LLKTVLDIPS NPTGLCALSI NHSNSYLAYP GSQSTGEIVL YDGNSLKTVC
     TIAAHEGTLA AITFNSSGSK LASASEKGTV IRVFSVPEGQ KLYEFRRGMK RYVTISSLVF
     SMDSQFLCAS SNTETVHIFK MEHLTDSRPE EPSTWSGYMG KMFMAATNYL PAQVSDMMNQ
     DRAFATGRLN FSGQKNICTL STIQKLPRLL VASSDGHLYI YNLDPQDGGE CVLIKTHSLL
     SSGTTEENKE NDLRPSLPPS YAATVARPST SAASTVPGYS EDGGALRGEV IPEHEFATGP
     VCLDDENEFP PIILCRGSQK GKTKQS
//
ID   MBOA2_MOUSE             Reviewed;         519 AA.
AC   Q8R3I2; A9EDS7; Q8BHH5; Q8BM56; Q8R192; Q9CZ73;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Lysophospholipid acyltransferase 2;
DE            Short=LPLAT 2;
DE            EC=2.3.1.-;
DE   AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
DE            EC=2.3.1.23;
DE   AltName: Full=1-acylglycerophosphoethanolamine O-acyltransferase;
DE            EC=2.3.1.n7;
DE   AltName: Full=Lysophosphatidylcholine acyltransferase;
DE            Short=LPCAT;
DE            Short=Lyso-PC acyltransferase;
DE   AltName: Full=Lysophosphatidylcholine acyltransferase 4;
DE            Short=Lyso-PC acyltransferase 4;
DE            Short=mLPCAT4;
DE   AltName: Full=Lysophosphatidylethanolamine acyltransferase;
DE            Short=LPEAT;
DE            Short=Lyso-PE acyltransferase;
DE   AltName: Full=Membrane-bound O-acyltransferase domain-containing protein 2;
DE            Short=O-acyltransferase domain-containing protein 2;
GN   Name=Mboat2; Synonyms=Lpcat4, Oact2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=17890783; DOI=10.1074/jbc.M704509200;
RA   Tamaki H., Shimada A., Itoh Y., Ohya M., Takase J., Miyashita M.,
RA   Miyagawa H., Nozaki H., Nakayama R., Kumagai H.;
RT   "LPT1 encodes a membrane-bound O-acyltransferase involved in the
RT   acylation of lysophospholipids in the yeast Saccharomyces
RT   cerevisiae.";
RL   J. Biol. Chem. 282:34288-34298(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=18287005; DOI=10.1073/pnas.0712245105;
RA   Hishikawa D., Shindou H., Kobayashi S., Nakanishi H., Taguchi R.,
RA   Shimizu T.;
RT   "Discovery of a lysophospholipid acyltransferase family essential for
RT   membrane asymmetry and diversity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2830-2835(2008).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryoid bodies, Medulla oblongata, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=Czech II; TISSUE=Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Acyltransferase which mediates the conversion of
CC       lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or
CC       LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-
CC       phosphocholine or PC) (LPCAT activity). To a lesser extent, also
CC       catalyzes the acylation of lysophosphatidylethanolamine (1-acyl-
CC       sn-glycero-3-phosphoethanolamine or LPE) into
CC       phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-
CC       phosphoethanolamine or PE) (LPEAT activity). Prefers oleoyl-CoA as
CC       the acyl donor. Lysophospholipid acyltransferases (LPLATs)
CC       catalyze the reacylation step of the phospholipid remodeling
CC       pathway also known as the Lands cycle.
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine
CC       = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine.
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycero-3-
CC       phosphoethanolamine = CoA + 1,2-diacyl-sn-glycero-3-
CC       phosphoethanolamine.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5.3 uM for oleoyl-CoA (in the presence of LPC C16:0 as
CC         cosubstrate);
CC         KM=48.15 uM for oleoyl-CoA (in the presence of LPE C16:0 as
CC         cosubstrate);
CC         KM=7.9 uM for LPC C16:0 (in the presence of oleoyl-CoA as
CC         cosubstrate);
CC         KM=27.7 uM for LPE C16:0 (in the presence of oleoyl-CoA as
CC         cosubstrate);
CC         Vmax=24.24 nmol/min/mg enzyme with oleoyl-CoA and LPC C16:0 as
CC         substrates;
CC         Vmax=26.3 nmol/min/mg enzyme with oleoyl-CoA and LPE C16:0 as
CC         substrates;
CC   -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential). Endoplasmic reticulum.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8R3I2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R3I2-2; Sequence=VSP_022458;
CC       Name=3;
CC         IsoId=Q8R3I2-3; Sequence=VSP_022457, VSP_022459;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in epididymis, brain, testis,
CC       and ovary.
CC   -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC27567.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB305046; BAF93902.1; -; mRNA.
DR   EMBL; AB297383; BAG12122.1; -; mRNA.
DR   EMBL; AK012931; BAB28556.1; -; mRNA.
DR   EMBL; AK031824; BAC27567.1; ALT_INIT; mRNA.
DR   EMBL; AK033106; BAC28154.1; -; mRNA.
DR   EMBL; AK034873; BAC28863.1; -; mRNA.
DR   EMBL; AK076045; BAC36144.1; -; mRNA.
DR   EMBL; BC025020; AAH25020.1; -; mRNA.
DR   IPI; IPI00153761; -.
DR   IPI; IPI00468901; -.
DR   IPI; IPI00828734; -.
DR   RefSeq; NP_001076810.1; NM_001083341.1.
DR   RefSeq; NP_080313.2; NM_026037.3.
DR   UniGene; Mm.167671; -.
DR   PhosphoSite; Q8R3I2; -.
DR   PRIDE; Q8R3I2; -.
DR   Ensembl; ENSMUST00000020976; ENSMUSP00000020976; ENSMUSG00000020646.
DR   Ensembl; ENSMUST00000078902; ENSMUSP00000077937; ENSMUSG00000020646.
DR   Ensembl; ENSMUST00000110942; ENSMUSP00000106567; ENSMUSG00000020646.
DR   Ensembl; ENSMUST00000116439; ENSMUSP00000112140; ENSMUSG00000020646.
DR   GeneID; 67216; -.
DR   KEGG; mmu:67216; -.
DR   UCSC; uc007neu.1; mouse.
DR   UCSC; uc007nev.1; mouse.
DR   UCSC; uc007new.1; mouse.
DR   CTD; 67216; -.
DR   MGI; MGI:1914466; Mboat2.
DR   eggNOG; roNOG08997; -.
DR   GeneTree; ENSGT00550000074565; -.
DR   HOGENOM; HBG444569; -.
DR   HOVERGEN; HBG058823; -.
DR   InParanoid; Q8R3I2; -.
DR   OMA; FYSSWYY; -.
DR   OrthoDB; EOG4N5VWQ; -.
DR   PhylomeDB; Q8R3I2; -.
DR   NextBio; 323902; -.
DR   ArrayExpress; Q8R3I2; -.
DR   Bgee; Q8R3I2; -.
DR   Genevestigator; Q8R3I2; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IEA:EC.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR004299; MBOAT_fam.
DR   Pfam; PF03062; MBOAT; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Alternative splicing; Endoplasmic reticulum;
KW   Membrane; Phospholipid biosynthesis; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    519       Lysophospholipid acyltransferase 2.
FT                                /FTId=PRO_0000273021.
FT   TRANSMEM     22     42       Helical; (Potential).
FT   TRANSMEM     61     81       Helical; (Potential).
FT   TRANSMEM     88    108       Helical; (Potential).
FT   TRANSMEM    184    204       Helical; (Potential).
FT   TRANSMEM    236    256       Helical; (Potential).
FT   TRANSMEM    263    283       Helical; (Potential).
FT   TRANSMEM    365    385       Helical; (Potential).
FT   TRANSMEM    415    435       Helical; (Potential).
FT   TRANSMEM    443    463       Helical; (Potential).
FT   VAR_SEQ       1    141       Missing (in isoform 3).
FT                                /FTId=VSP_022457.
FT   VAR_SEQ     100    132       QCCFVFALGYLSVCQITRVYIFDYGQYSADFSG -> H
FT                                (in isoform 2).
FT                                /FTId=VSP_022458.
FT   VAR_SEQ     142    150       TSLAYEIHD -> MDNILLIFQ (in isoform 3).
FT                                /FTId=VSP_022459.
FT   CONFLICT     28     28       F -> S (in Ref. 3; BAB28556).
FT   CONFLICT     40     40       V -> L (in Ref. 3; BAB28556).
SQ   SEQUENCE   519 AA;  58995 MW;  A21F3947612314EE CRC64;
     MATTSTTGST LLQPLSNAVQ LPIDQVNFVV CQLFALLAAV WFRTYLHSSK TSSFIRHVVA
     TLLGLYLAFF CFGWYALHFL VQSGISYCIM IIAGVESMQQ CCFVFALGYL SVCQITRVYI
     FDYGQYSADF SGPMMIITQK ITSLAYEIHD GMFRKDEELT PSQRGLAVRR MPSLLEYVSY
     TCNFMGILAG PLCSYKDYIA FIEGRASHVA QPSENGKDEQ HGKADPSPNA AVTEKLLVCG
     LSLLFHLTIS NMLPVEYNID EHFQATASWP TKATYLYVSL LAARPKYYFA WTLADAINNA
     AGFGFRGYDK NGVARWDLIS NLRIQQIEMS TSFKMFLDNW NIQTALWLKR VCYERATFSP
     TIQTFFLSAI WHGVYPGYYL TFLTGVLMTL AARAVRNNFR HYFLEPPQLK LFYDLITWVA
     TQITISYTVV PFVLLSIKPS FTFYSSWYYC LHVCSILVLL LLPVKKSQRR TSTQENVHLS
     QAKKFDERDN PLGQNSFSTM NNVCNQNRDT GSRHSSLTQ
//
ID   SO3A1_MOUSE             Reviewed;         710 AA.
AC   Q8R3L5; Q3TLX2; Q3U7W0; Q505P2; Q544H3; Q9CTV3; Q9JKV0;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Solute carrier organic anion transporter family member 3A1;
DE   AltName: Full=MJAM;
DE   AltName: Full=Organic anion-transporting polypeptide D;
DE            Short=OATP-D;
DE   AltName: Full=Sodium-independent organic anion transporter D;
DE   AltName: Full=Solute carrier family 21 member 11;
GN   Name=Slco3a1; Synonyms=Oatp3a1, Oatpd, Slc21a11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Kidney;
RA   Isern J., Menoyo A., Melia M.J., Meseguer A.;
RT   "Mus musculus organic anion transporting polypeptide MJAM.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 14-710 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Macrophage, Mammary gland, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 7-710 (ISOFORM 2).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Mediates the Na(+)-independent transport of organic
CC       anions (By similarity). Mediates transport of prostaglandins (PG)
CC       E1 and E2, thyroxine (T4), deltorphin II, BQ-123 and vasopressin
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R3L5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R3L5-2; Sequence=VSP_036839, VSP_036840;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- INDUCTION: By androgens in kidney and lung.
CC   -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60)
CC       family.
CC   -!- SIMILARITY: Contains 1 Kazal-like domain.
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DR   EMBL; AF226324; AAF35370.1; -; mRNA.
DR   EMBL; AK020010; BAB31965.1; -; mRNA.
DR   EMBL; AK037938; BAC29904.1; -; mRNA.
DR   EMBL; AK152488; BAE31259.1; -; mRNA.
DR   EMBL; AK166266; BAE38670.1; -; mRNA.
DR   EMBL; BC025059; AAH25059.1; -; mRNA.
DR   EMBL; BC094464; AAH94464.1; -; mRNA.
DR   IPI; IPI00227963; -.
DR   IPI; IPI00720145; -.
DR   RefSeq; NP_001033732.1; NM_001038643.1.
DR   RefSeq; NP_076397.2; NM_023908.2.
DR   UniGene; Mm.425467; -.
DR   ProteinModelPortal; Q8R3L5; -.
DR   SMR; Q8R3L5; 474-529.
DR   STRING; Q8R3L5; -.
DR   MEROPS; I01.972; -.
DR   PRIDE; Q8R3L5; -.
DR   Ensembl; ENSMUST00000026897; ENSMUSP00000026897; ENSMUSG00000025790.
DR   GeneID; 108116; -.
DR   KEGG; mmu:108116; -.
DR   UCSC; uc009hwg.1; mouse.
DR   CTD; 108116; -.
DR   MGI; MGI:1351867; Slco3a1.
DR   eggNOG; roNOG11378; -.
DR   GeneTree; ENSGT00560000077029; -.
DR   HOVERGEN; HBG098539; -.
DR   InParanoid; Q8R3L5; -.
DR   OMA; CVMCICS; -.
DR   OrthoDB; EOG4ZKJKX; -.
DR   PhylomeDB; Q8R3L5; -.
DR   NextBio; 360100; -.
DR   ArrayExpress; Q8R3L5; -.
DR   Bgee; Q8R3L5; -.
DR   Genevestigator; Q8R3L5; -.
DR   GermOnline; ENSMUSG00000025790; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   InterPro; IPR004156; OA_transporter.
DR   InterPro; IPR002350; Prot_inh_Kazal.
DR   InterPro; IPR011497; Prot_Inh_Kazal_2.
DR   PANTHER; PTHR11388; OA_transporter; 1.
DR   Pfam; PF07648; Kazal_2; 1.
DR   Pfam; PF03137; OATP; 1.
DR   SMART; SM00280; KAZAL; 1.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
DR   TIGRFAMs; TIGR00805; oat; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW   Ion transport; Membrane; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    710       Solute carrier organic anion transporter
FT                                family member 3A1.
FT                                /FTId=PRO_0000191065.
FT   TOPO_DOM      1     40       Cytoplasmic (Potential).
FT   TRANSMEM     41     60       Helical; Name=1; (Potential).
FT   TOPO_DOM     61     79       Extracellular (Potential).
FT   TRANSMEM     80    100       Helical; Name=2; (Potential).
FT   TOPO_DOM    101    106       Cytoplasmic (Potential).
FT   TRANSMEM    107    131       Helical; Name=3; (Potential).
FT   TOPO_DOM    132    174       Extracellular (Potential).
FT   TRANSMEM    175    203       Helical; Name=4; (Potential).
FT   TOPO_DOM    204    222       Cytoplasmic (Potential).
FT   TRANSMEM    223    243       Helical; Name=5; (Potential).
FT   TOPO_DOM    244    261       Extracellular (Potential).
FT   TRANSMEM    262    286       Helical; Name=6; (Potential).
FT   TOPO_DOM    287    344       Cytoplasmic (Potential).
FT   TRANSMEM    345    366       Helical; Name=7; (Potential).
FT   TOPO_DOM    367    386       Extracellular (Potential).
FT   TRANSMEM    387    410       Helical; Name=8; (Potential).
FT   TOPO_DOM    411    414       Cytoplasmic (Potential).
FT   TRANSMEM    415    438       Helical; Name=9; (Potential).
FT   TOPO_DOM    439    539       Extracellular (Potential).
FT   TRANSMEM    540    562       Helical; Name=10; (Potential).
FT   TOPO_DOM    563    571       Cytoplasmic (Potential).
FT   TRANSMEM    572    597       Helical; Name=11; (Potential).
FT   TOPO_DOM    598    630       Extracellular (Potential).
FT   TRANSMEM    631    648       Helical; Name=12; (Potential).
FT   TOPO_DOM    649    705       Cytoplasmic (Potential).
FT   DOMAIN      465    513       Kazal-like.
FT   COMPBIAS     27     32       Poly-Lys.
FT   CARBOHYD    153    153       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    169    169       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    381    381       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    457    457       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    502    502       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    505    505       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    519    519       N-linked (GlcNAc...) (Potential).
FT   DISULFID    471    497       By similarity.
FT   DISULFID    475    486       By similarity.
FT   DISULFID    477    501       By similarity.
FT   VAR_SEQ     667    692       EFFASTLTLDNLGRDPVPAHQTHRTK -> TEYQDIETEKT
FT                                CPESQSPSEDSFVRS (in isoform 2).
FT                                /FTId=VSP_036839.
FT   VAR_SEQ     693    710       Missing (in isoform 2).
FT                                /FTId=VSP_036840.
FT   CONFLICT      7      7       G -> D (in Ref. 1; AAF35370).
FT   CONFLICT     14     14       R -> G (in Ref. 2; BAE38670).
FT   CONFLICT    138    138       G -> V (in Ref. 1; AAF35370).
FT   CONFLICT    143    143       G -> E (in Ref. 1; AAF35370).
FT   CONFLICT    147    147       R -> T (in Ref. 1; AAF35370).
FT   CONFLICT    159    160       EG -> DR (in Ref. 1; AAF35370).
FT   CONFLICT    178    178       L -> M (in Ref. 1; AAF35370).
FT   CONFLICT    428    428       N -> K (in Ref. 1; AAF35370).
FT   CONFLICT    603    603       F -> L (in Ref. 1; AAF35370).
FT   CONFLICT    681    681       D -> G (in Ref. 2; BAE31259).
FT   CONFLICT    687    687       Q -> L (in Ref. 2; BAE31259).
SQ   SEQUENCE   710 AA;  76763 MW;  AC89FB5026441C59 CRC64;
     MQGKKPGGSS GGGRSGELQG DEAQRNKKKK KKVSCFSNIK IFLVSECALM LAQGTVGAYL
     VSVLTTLERR FNLQSADVGV IASSFEIGNL ALILFVSYFG ARGHRPRLIG CGGIVMALGA
     LLSALPEFLT HQYKYEAGEI RWGAEGRDVC ATNGSSSDEG PDPDLICRNR TATNMMYLLL
     IGAQVLLGIG ATPVQPLGVS YIDDHVRRKD SSLYIGILFT MLVFGPACGF ILGSFCTKIY
     VDAVFIDTSN LDITPDDPRW IGAWWGGFLL CGALLFFSSL LMFGFPQSLP PHSDPGMESE
     QAMLPEREYE RPKPSNGVLR HPLEPDSSAS CFQQLRVIPK VTKHLLSNPV FTCIVLAACM
     EIAVVAGFAA FLGKYLEQQF NLTTSSANQL LGMTAIPCAC LGIFLGGLLV KKLSLSALGA
     IRMAMLVNLV STACYVSFLF LGCDTGPVAG VTVRYGNNSA RGSALDPYSP CNNNCECQTD
     SFTPVCGADG ITYLSACFAG CNSTNLTGCA CLTTVPPENA SVVPGKCPSP GCQEAFLTFL
     CVMCVCSLIG AMAQTPSVII LIRTVSPELK SYALGVLFLL LRLLGFIPPP LIFGAGIDST
     CLFWSTFCGE QGACVLYDNV VYRYLYVSIA IALKSFAFIL YTTTWQCLRK NYKRYIKNHE
     GGLSTSEFFA STLTLDNLGR DPVPAHQTHR TKFIYNLEDH EWCENMESVL
//
ID   THOC1_MOUSE             Reviewed;         657 AA.
AC   Q8R3N6; Q8BWD5; Q8BXY3;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=THO complex subunit 1;
DE            Short=Tho1;
DE   AltName: Full=Nuclear matrix protein p84;
GN   Name=Thoc1; Synonyms=Hpr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=16705185; DOI=10.1128/MCB.02163-05;
RA   Wang X., Chang Y., Li Y., Zhang X., Goodrich D.W.;
RT   "Thoc1/Hpr1/p84 is essential for early embryonic development in the
RT   mouse.";
RL   Mol. Cell. Biol. 26:4362-4367(2006).
RN   [4]
RP   INTERACTION WITH THOC5.
RX   PubMed=16909111; DOI=10.1038/sj.onc.1209853;
RA   Mancini A., El Bounkari O., Norrenbrock A.-F., Scherr M., Schaefer D.,
RA   Eder M., Banham A.H., Pulford K., Lyne L., Whetton A.D., Tamura T.;
RT   "FMIP controls the adipocyte lineage commitment of C2C12 cells by
RT   downmodulation of C/EBP alpha.";
RL   Oncogene 26:1020-1027(2007).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19307311; DOI=10.1128/MCB.01633-08;
RA   Wang X., Chinnam M., Wang J., Wang Y., Zhang X., Marcon E., Moens P.,
RA   Goodrich D.W.;
RT   "Thoc1 deficiency compromises gene expression necessary for normal
RT   testis development in the mouse.";
RL   Mol. Cell. Biol. 29:2794-2803(2009).
CC   -!- FUNCTION: Component of the THO subcomplex of the TREX complex. The
CC       TREX complex specifically associates with spliced mRNA and not
CC       with unspliced pre-mRNA. It is recruited to spliced mRNAs by a
CC       transcription-independent mechanism. Binds to mRNA upstream of the
CC       exon-junction complex (EJC) and is recruited in a splicing- and
CC       cap-dependent manner to a region near the 5' end of the mRNA where
CC       it functions in mRNA export. The recruitment occurs via an
CC       interaction between THOC4 and the cap-binding protein NCBP1. UAP56
CC       functions as a bridge between THOC4 and the THO complex (By
CC       similarity).
CC   -!- FUNCTION: Regulates transcriptional elongation of a subset of
CC       genes. Participates in an apoptotic pathway which is characterized
CC       by activation of caspase-6, increases in the expression of BAK1
CC       and BCL2L1 and activation of NF-kappa-B. This pathway does not
CC       require p53/TP53, nor does the presence of p53/TP53 affect the
CC       efficiency of cell killing. Activates a G2/M cell cycle checkpoint
CC       prior to the onset of apoptosis. Apoptosis is inhibited by
CC       association with RB1 (By similarity). Essential for early
CC       embryonic development. Required for normal gene expression during
CC       postnatal testis development.
CC   -!- SUBUNIT: Component of the THO complex, which is composed of THOC1,
CC       THOC2, THOC5, THOC6 and THOC7. Together with THOC3, THOC4 and
CC       UAP56, THO forms the transcription/export (TREX) complex. Binds to
CC       the hypophosphorylated form of RB1. Interacts with THOC2, UAP56
CC       and RNA polymerase II (By similarity). Interacts with THOC5.
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle (By similarity). Nucleus,
CC       nucleoplasm. Nucleus matrix (By similarity). Cytoplasm (By
CC       similarity). Note=Can shuttle between the nucleus and cytoplasm.
CC       Nuclear localization is required for induction of apoptotic cell
CC       death. Translocates to the cytoplasm during the early phase of
CC       apoptosis execution (By similarity).
CC   -!- DEVELOPMENTAL STAGE: Widely expressed during embryonic
CC       development.
CC   -!- DOMAIN: An intact death domain is needed for apoptosis (By
CC       similarity).
CC   -!- PTM: Expression is altered specifically during apoptosis and is
CC       accompanied by the appearance of novel forms with smaller apparent
CC       molecular mass (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice show early embryonic lethality and
CC       severely diminished fertility.
CC   -!- SIMILARITY: Contains 1 death domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK031785; BAC27548.1; -; mRNA.
DR   EMBL; AK032200; BAC27754.1; -; mRNA.
DR   EMBL; AK042867; BAC31387.2; -; mRNA.
DR   EMBL; BC024951; AAH24951.1; -; mRNA.
DR   IPI; IPI00153778; -.
DR   RefSeq; NP_705780.1; NM_153552.3.
DR   UniGene; Mm.219648; -.
DR   UniGene; Mm.329277; -.
DR   ProteinModelPortal; Q8R3N6; -.
DR   SMR; Q8R3N6; 558-657.
DR   STRING; Q8R3N6; -.
DR   PhosphoSite; Q8R3N6; -.
DR   PRIDE; Q8R3N6; -.
DR   Ensembl; ENSMUST00000025137; ENSMUSP00000025137; ENSMUSG00000024287.
DR   GeneID; 225160; -.
DR   KEGG; mmu:225160; -.
DR   UCSC; uc008eal.1; mouse.
DR   CTD; 225160; -.
DR   MGI; MGI:1919668; Thoc1.
DR   GeneTree; ENSGT00390000016232; -.
DR   HOGENOM; HBG402972; -.
DR   HOVERGEN; HBG060294; -.
DR   InParanoid; Q8R3N6; -.
DR   OMA; ILMGNEE; -.
DR   OrthoDB; EOG4HX50P; -.
DR   PhylomeDB; Q8R3N6; -.
DR   NextBio; 377554; -.
DR   ArrayExpress; Q8R3N6; -.
DR   Bgee; Q8R3N6; -.
DR   CleanEx; MM_THOC1; -.
DR   Genevestigator; Q8R3N6; -.
DR   GermOnline; ENSMUSG00000024287; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR000488; Death.
DR   InterPro; IPR011029; DEATH-like.
DR   InterPro; IPR021861; THO_THOC1.
DR   Gene3D; G3DSA:1.10.533.10; DEATH_like; 1.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF11957; efThoc1; 1.
DR   SMART; SM00005; DEATH; 1.
DR   SUPFAM; SSF47986; DEATH_like; 1.
DR   PROSITE; PS50017; DEATH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Cytoplasm; DNA-binding; mRNA processing;
KW   mRNA splicing; mRNA transport; Nucleus; Phosphoprotein; RNA-binding;
KW   Transcription; Transcription regulation; Transport.
FT   CHAIN         1    657       THO complex subunit 1.
FT                                /FTId=PRO_0000072521.
FT   DOMAIN      570    653       Death.
FT   MOTIF       414    430       Nuclear localization signal (By
FT                                similarity).
FT   MOD_RES       2      2       Phosphoserine (By similarity).
FT   MOD_RES     133    133       N6-acetyllysine (By similarity).
FT   MOD_RES     300    300       N6-acetyllysine (By similarity).
FT   MOD_RES     560    560       Phosphoserine (By similarity).
SQ   SEQUENCE   657 AA;  75436 MW;  E4235E395B5A82BC CRC64;
     MSPTPALFSL PEARTRFTKS TREALNNKNI KPLLTAFSQL PGSENEKKCT LDQAFRGVLE
     EEIINHSACE NVLAIISLAI GGVTESVCTA STPFVLLGDV LDCLPLDQCD TIFTFVEKNV
     ATWKSNTFYS AGKNYLLRMC NDLLRRLSKS QNTVFCGRIQ LFLARLFPLS EKSGLNLQSQ
     FNLENVTVFN TNEQESTLGQ KHTEDREEGM DVEEGEMGDD EAPTTCSIPI DYNLYRKFWS
     LQDYFRNPVQ CYEKISWKTF LKYSEEVLAV FKSYKLDDTQ ASRKKMEELK TGGEHVYFAK
     FLTSEKLMDL QLSDSNFRRH ILLQYLILFQ YLKGQVKFKS SNYVLTDEQS LWIEDTTKSV
     YQLLSENPPD GERFSKMVEH ILNTEENWNS WKNEGCPSFV KERASDTKPT RVVRKRAAPE
     DFLGKGPNKK ILIGNEELTR LWNLCPDNME ACKSETREYM PTLEEFFEEA IEQADPENMV
     ESEYKAVNNS NYGWRALRLL ARRSPHFFQP TNQQFKSLPE YLENMVIKLA KELPPPSEEI
     KTGEDEDEED NDALLKENES PDVRRDKPIT GEQIESFANK LGEQWKILAP YLEIKDSDIR
     QIECDSEDMK MRAKQLLVAW QDQEGVHATT DNLISALNKS GLSDLAESLT NDTETNS
//
ID   PP6R2_MOUSE             Reviewed;         923 AA.
AC   Q8R3Q2; Q9CXB7;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Serine/threonine-protein phosphatase 6 regulatory subunit 2;
DE   AltName: Full=SAPS domain family member 2;
GN   Name=Ppp6r2; Synonyms=Kiaa0685, Pp6r2, Saps2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-206.
RC   STRAIN=C57BL/6J; TISSUE=Embryonic lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-670, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=16769727; DOI=10.1074/jbc.M601772200;
RA   Stefansson B., Brautigan D.L.;
RT   "Protein phosphatase 6 subunit with conserved Sit4-associated protein
RT   domain targets IkappaBepsilon.";
RL   J. Biol. Chem. 281:22624-22634(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-672, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-669, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Regulatory subunit of protein phospatase 6 (PP6). May
CC       function as a scaffolding PP6 subunit. Involved in the PP6-
CC       mediated dephosphorylation of NFKBIE opposing its degradation in
CC       response to TNF-alpha.
CC   -!- SUBUNIT: Protein phospatase 6 (PP6) holoenzyme is proposed to be a
CC       heterotrimeric complex formed by the catalytic subunit, a SAPS
CC       domain-containing subunit (PP6R) and an ankyrin repeat-domain
CC       containing regulatory subunit (ARS). Interacts with PPP6C and
CC       NFKBIE. Interacts with ANKRD28 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: Strongest expression in bladder and lower
CC       levels found in heart and pancreas. Very weak expression observed
CC       in all other tissues tested.
CC   -!- SIMILARITY: Belongs to the SAPS family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AK018403; Type=Frameshift; Positions=168;
CC   -----------------------------------------------------------------------
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DR   EMBL; BC024879; AAH24879.1; -; mRNA.
DR   EMBL; AK018403; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00461823; -.
DR   UniGene; Mm.184055; -.
DR   ProteinModelPortal; Q8R3Q2; -.
DR   PhosphoSite; Q8R3Q2; -.
DR   PRIDE; Q8R3Q2; -.
DR   Ensembl; ENSMUST00000042254; ENSMUSP00000043565; ENSMUSG00000036561.
DR   Ensembl; ENSMUST00000088788; ENSMUSP00000086167; ENSMUSG00000036561.
DR   UCSC; uc007xfw.1; mouse.
DR   MGI; MGI:1918724; Ppp6r2.
DR   GeneTree; ENSGT00390000009899; -.
DR   HOGENOM; HBG505370; -.
DR   HOVERGEN; HBG069733; -.
DR   InParanoid; Q8R3Q2; -.
DR   OrthoDB; EOG41VK2F; -.
DR   ArrayExpress; Q8R3Q2; -.
DR   Bgee; Q8R3Q2; -.
DR   CleanEx; MM_SAPS2; -.
DR   Genevestigator; Q8R3Q2; -.
DR   GermOnline; ENSMUSG00000036561; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR007587; SAPS.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   PANTHER; PTHR12634; SAPS; 1.
DR   Pfam; PF04499; SAPS; 2.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein.
FT   CHAIN         1    923       Serine/threonine-protein phosphatase 6
FT                                regulatory subunit 2.
FT                                /FTId=PRO_0000046099.
FT   COMPBIAS    788    793       Poly-Ser.
FT   MOD_RES     289    289       Phosphoserine (By similarity).
FT   MOD_RES     669    669       Phosphoserine.
FT   MOD_RES     670    670       Phosphoserine.
FT   MOD_RES     672    672       Phosphothreonine.
FT   MOD_RES     745    745       Phosphoserine (By similarity).
FT   CONFLICT    106    106       L -> H (in Ref. 2; AK018403).
FT   CONFLICT    167    167       L -> C (in Ref. 2).
FT   CONFLICT    195    195       L -> I (in Ref. 2).
SQ   SEQUENCE   923 AA;  100460 MW;  02F604745D69067B CRC64;
     MFWKFDLNTT SHVDKLLDKE HVTLQELMDE DDILQECKAQ NQKLLDFLCR QQCMEELVNL
     ITQDPPQDME EKVRFKYPNT ACELLTCDVP QISDRLGEDE SLLNLLYDFL DQEPPLNPLL
     ASFFSKTIGN LIARKTEQVI MFLKKKEKFI SQLLKHIGTS ALMDLLLRLV SCVEPVGLRQ
     EVLHWLNEEK IIQRLVALIH PHQDEDRQSN ASQALCDIIR LGRDQGSQLQ ETVEPDPLLI
     TLESQDCVEQ LLKNMFDGDQ TESCLVSGMQ VLLALLEPRR VGTEGLVDSF SQGLERSHSV
     SSSILRGIEP WLKNFHQLLL NPPKKKAILT TIGVLEEPLG NARLHGARLM AALLHTNTPG
     INQELCRLNT MDLLLDLFFK YTWNNFLHLQ VELCIAAILS HAAREEQAEA SGSDGKVEPL
     QGSGDGNGKL ETTPSITSPP ENTMVTHLFQ KCCLVQRILE AWEANDHTQA AGGMRRGNMG
     HLTRIANAVV QNLEQGPVQA HISEVIRGLP ADCRGRWESF VEETLMETNR RNTVDLAFSE
     YQIQQMTANF VDQFGFNDEE FADQDDNINA PFDRIAEINF NIEADEDSPS AALFEACCSD
     RIQPFDDDEE EDIWEDDETR CAARVMARAR FGAPHVSDNY SKNALEHGGQ DRKTGSAVAR
     NVPGLAAPSS PTQKEGPRSE SDSAGTTWTA VFDEPVNPLS ATPGAARDVG SSAWAAGPSV
     VEEKGWAKFT DFQPFCCSET GPRCSSPVDM DHSNAEGGQS PGPEKTFGPT SPCAWNVCVT
     RKAPLVASDS SSSGGSDSED DEKAAGAVEA VCTGHTGKVS PPPRTAEAAV GRAECPDSTV
     LAPACPAPSE VTISPAVATI APSKAGSPTA TIVVSSSVAA AVPPGPIVAV TTAAPAIVAT
     LGTMTKDRKA DALPEGAALN GPV
//
ID   T185B_MOUSE             Reviewed;         350 AA.
AC   Q8R3R5; Q8BSP3;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Transmembrane protein 185B;
DE   AltName: Full=Protein FAM11B;
GN   Name=Tmem185b; Synonyms=Fam11b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Forelimb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the TMEM185 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC27267.1; Type=Frameshift; Positions=20;
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DR   EMBL; AK031130; BAC27267.1; ALT_FRAME; mRNA.
DR   EMBL; BC024712; AAH24712.1; -; mRNA.
DR   IPI; IPI00153803; -.
DR   RefSeq; NP_666215.1; NM_146103.1.
DR   UniGene; Mm.439806; -.
DR   PhosphoSite; Q8R3R5; -.
DR   PRIDE; Q8R3R5; -.
DR   Ensembl; ENSMUST00000069755; ENSMUSP00000111694; ENSMUSG00000037015.
DR   GeneID; 226351; -.
DR   KEGG; mmu:226351; -.
DR   UCSC; uc007ciu.1; mouse.
DR   CTD; 226351; -.
DR   MGI; MGI:1917634; Tmem185b.
DR   GeneTree; ENSGT00390000008194; -.
DR   HOGENOM; HBG507246; -.
DR   HOVERGEN; HBG051528; -.
DR   InParanoid; Q8R3R5; -.
DR   OrthoDB; EOG4SBDZB; -.
DR   NextBio; 378106; -.
DR   ArrayExpress; Q8R3R5; -.
DR   Bgee; Q8R3R5; -.
DR   CleanEx; MM_TMEM185B; -.
DR   Genevestigator; Q8R3R5; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR019396; TM_Fragile-X-F-assoc.
DR   Pfam; PF10269; Tmemb_185A; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    350       Transmembrane protein 185B.
FT                                /FTId=PRO_0000188010.
FT   TRANSMEM     16     36       Helical; (Potential).
FT   TRANSMEM     41     61       Helical; (Potential).
FT   TRANSMEM     81    101       Helical; (Potential).
FT   TRANSMEM    111    131       Helical; (Potential).
FT   TRANSMEM    153    173       Helical; (Potential).
FT   TRANSMEM    177    197       Helical; (Potential).
FT   TRANSMEM    211    231       Helical; (Potential).
FT   TRANSMEM    240    260       Helical; (Potential).
SQ   SEQUENCE   350 AA;  40701 MW;  4DE49C610BEF6614 CRC64;
     MNPRGLFQDF NPSKFLIYAC LLLFSVLLPL RLDGIIQWSY WAVFAPIWLW KLLVIVGASV
     GAGVWARNPR YRTEGEACVE FKAMLIAVGI HLLLLMFEIL VCDRVERGTH FWLLVFMPLF
     FVSPVSVAAC VWGFRHDRSL ELEILCSVNI LQFIFIALRL DRIIHWPWLV VFVPLWILMS
     FLCLVVLYYI VWSLLFLRSL DVVAEQRRTH VTMAISWITI VVPLLIFEVL LVHRLDDHNT
     FSYISIFIPL WLSLLTLMAT TFRRKGGNHW WFGIRRDFCQ FLLEVFPFLR EYGNISYDLH
     HEDSEDAEDA SVSEAPKIAP MFGKKARVVI TQSPGKYVPP PPKLNIDMPD
//
ID   Q8R3S9_MOUSE            Unreviewed;       503 AA.
AC   Q8R3S9;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   30-NOV-2010, entry version 35.
DE   SubName: Full=Ccdc93 protein;
DE   Flags: Fragment;
GN   Name=Ccdc93;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II;
RC   TISSUE=Mammary tumor metastatized to lung. Tumor arose spontaneously;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC024674; AAH24674.1; -; mRNA.
DR   IPI; IPI00416918; -.
DR   UniGene; Mm.25788; -.
DR   Ensembl; ENSMUST00000036025; ENSMUSP00000043442; ENSMUSG00000026339.
DR   MGI; MGI:1918079; Ccdc93.
DR   HOVERGEN; HBG054413; -.
DR   InParanoid; Q8R3S9; -.
DR   ArrayExpress; Q8R3S9; -.
DR   Bgee; Q8R3S9; -.
DR   Genevestigator; Q8R3S9; -.
DR   InterPro; IPR019159; DUF2037.
DR   Pfam; PF09762; KOG2701; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   503 AA;  58447 MW;  D4FC54E1D8A11BCA CRC64;
     AIETKEEMGD YIRSYSISQF QKTYSLPEDD DFIKRKDKAV KTVVDLSDAY KPRRKYRRQR
     GAEELLDEES RVHSTLLEYG RRYGFSRQSK TEKAEDKKTA LAAGLSAAEK ADAHEEDELQ
     AAEEQRIQSL MTKMTAMANE ESRLTASSVG QIVGLCSEEI KQIVSEYAGK QSELSAEESP
     EKLGTSQLHQ RKVISLNKQI LQKSKHLEEL QANHTSLKAK YSDRKKTLTE LKDHGEKLDK
     EQAALEKLEA KADPSMLQNL RALVAMNESL KSQEQEFKAH CREEMARLQQ EIETLKAERA
     PGEKIVSGGE PQGALTSTMT HNEDLDRRYN MEKEKLYKIR LLQARRNREI AILHRKIDEV
     PSRAELIQYQ KRFIELYRQI SAVHKETKQF FTLYNTLDDK KVYLEKEISL LNSIHENFSQ
     AMASPAARDQ FLRQMEQIVE GIKQSRMKME KKKQENKMRR DQLNDQYLEL LEKQRLYFKT
     VKEFKEEGRK NELLLSKIKA KAS
//
ID   STXB6_MOUSE             Reviewed;         210 AA.
AC   Q8R3T5;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Syntaxin-binding protein 6;
GN   Name=Stxbp6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Forms non-fusogenic complexes with SNAP25 and STX1A and
CC       may thereby modulate the formation of functional SNARE complexes
CC       and exocytosis (By similarity).
CC   -!- SUBUNIT: Part of a ternary complex containing SNAP25 and STX1A
CC       that can be dissociated by NAPA and NSF. Interacts with STX4A (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane;
CC       Peripheral membrane protein (By similarity).
CC   -!- SIMILARITY: Contains 1 v-SNARE coiled-coil homology domain.
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DR   EMBL; BC024598; AAH24598.1; -; mRNA.
DR   IPI; IPI00281420; -.
DR   UniGene; Mm.285400; -.
DR   ProteinModelPortal; Q8R3T5; -.
DR   SMR; Q8R3T5; 155-208.
DR   STRING; Q8R3T5; -.
DR   PRIDE; Q8R3T5; -.
DR   Ensembl; ENSMUST00000053768; ENSMUSP00000052639; ENSMUSG00000046314.
DR   Ensembl; ENSMUST00000120531; ENSMUSP00000112551; ENSMUSG00000046314.
DR   MGI; MGI:2384963; Stxbp6.
DR   GeneTree; ENSGT00530000063494; -.
DR   HOGENOM; HBG713147; -.
DR   HOVERGEN; HBG059039; -.
DR   InParanoid; Q8R3T5; -.
DR   OrthoDB; EOG4HT8T5; -.
DR   ArrayExpress; Q8R3T5; -.
DR   Bgee; Q8R3T5; -.
DR   CleanEx; MM_STXBP6; -.
DR   Genevestigator; Q8R3T5; -.
DR   GermOnline; ENSMUSG00000046314; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR001388; Synaptobrevin.
DR   Pfam; PF00957; Synaptobrevin; 1.
DR   PROSITE; PS50892; V_SNARE; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Membrane.
FT   CHAIN         1    210       Syntaxin-binding protein 6.
FT                                /FTId=PRO_0000206783.
FT   DOMAIN      151    210       v-SNARE coiled-coil homology.
SQ   SEQUENCE   210 AA;  23671 MW;  7C116A9F7FAFC2D8 CRC64;
     MSAKSAISKE IFAPLDERML GAVQVKRRTK KKIPFLATGG QGEYLTYICL SVTNKKPTQA
     SITKVKQFEG STSFVRRSQW MLEQLRQVNG IDPNRDSAEF DLLFENAFDQ WVASTASEKC
     TFFQILHHTC QRYLTDRKPE FINCQSKIMG GNSILHSAAD SVTSAVQKAS QALNERGERL
     GRAEEKTEDM KNSAQQFAET AHKLAMKHKC
//
ID   SHLB2_MOUSE             Reviewed;         400 AA.
AC   Q8R3V5; Q3TIQ1; Q3U2J4; Q3U824; Q8K140; Q91ZI7;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Endophilin-B2;
DE   AltName: Full=SH3 domain-containing GRB2-like protein B2;
GN   Name=Sh3glb2; Synonyms=Kiaa1848;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Heart;
RA   Chang N.-S., Doherty J., Schultz L.;
RT   "TIAF1 physically interacts with SH3GLB2.";
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, DBA/2, and NOD;
RC   TISSUE=Bone marrow, and Dendritic cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=FVB/N; TISSUE=Mammary gland, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBUNIT: Homodimer, and heterodimer with SH3GLB1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=2;
CC         IsoId=Q8R3V5-4; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q8R3V5-1; Sequence=VSP_028795;
CC       Name=3;
CC         IsoId=Q8R3V5-3; Sequence=VSP_009280;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the endophilin family.
CC   -!- SIMILARITY: Contains 1 BAR domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH28859.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC       Sequence=BAC98265.2; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF426314; AAL24820.1; -; mRNA.
DR   EMBL; AK129455; BAC98265.2; ALT_INIT; Transcribed_RNA.
DR   EMBL; AK152409; BAE31195.1; -; mRNA.
DR   EMBL; AK155248; BAE33146.1; -; mRNA.
DR   EMBL; AK167762; BAE39795.1; -; mRNA.
DR   EMBL; AL954388; CAM23166.1; -; Genomic_DNA.
DR   EMBL; AL954388; CAM23168.1; -; Genomic_DNA.
DR   EMBL; BC024477; AAH24477.1; -; mRNA.
DR   EMBL; BC028859; AAH28859.1; ALT_SEQ; mRNA.
DR   IPI; IPI00153832; -.
DR   IPI; IPI00169647; -.
DR   IPI; IPI00626834; -.
DR   RefSeq; NP_647463.1; NM_139302.1.
DR   UniGene; Mm.33343; -.
DR   ProteinModelPortal; Q8R3V5; -.
DR   SMR; Q8R3V5; 16-281, 339-400.
DR   STRING; Q8R3V5; -.
DR   PhosphoSite; Q8R3V5; -.
DR   REPRODUCTION-2DPAGE; Q8R3V5; -.
DR   PRIDE; Q8R3V5; -.
DR   Ensembl; ENSMUST00000028214; ENSMUSP00000028214; ENSMUSG00000026860.
DR   Ensembl; ENSMUST00000100215; ENSMUSP00000097788; ENSMUSG00000026860.
DR   Ensembl; ENSMUST00000113620; ENSMUSP00000109250; ENSMUSG00000026860.
DR   GeneID; 227700; -.
DR   KEGG; mmu:227700; -.
DR   UCSC; uc008jcc.1; mouse.
DR   CTD; 227700; -.
DR   MGI; MGI:2385131; Sh3glb2.
DR   GeneTree; ENSGT00550000074464; -.
DR   HOVERGEN; HBG054448; -.
DR   OrthoDB; EOG42FSHZ; -.
DR   NextBio; 378768; -.
DR   ArrayExpress; Q8R3V5; -.
DR   Bgee; Q8R3V5; -.
DR   CleanEx; MM_SH3GLB2; -.
DR   Genevestigator; Q8R3V5; -.
DR   GermOnline; ENSMUSG00000026860; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008093; F:cytoskeletal adaptor activity; IEA:InterPro.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:InterPro.
DR   GO; GO:0046847; P:filopodium assembly; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR004148; BAR.
DR   InterPro; IPR013606; IRSp53/MIM_homology_IMD.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:1.20.1270.80; IRSp53/MIM_homology_IMD; 1.
DR   Pfam; PF03114; BAR; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00721; BAR; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS51021; BAR; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Cytoplasm; SH3 domain.
FT   CHAIN         1    400       Endophilin-B2.
FT                                /FTId=PRO_0000146756.
FT   DOMAIN       24    287       BAR.
FT   DOMAIN      340    400       SH3.
FT   REGION        1     27       Membrane-binding amphipathic helix (By
FT                                similarity).
FT   COILED      205    234       Potential.
FT   VAR_SEQ     188    208       Missing (in isoform 3).
FT                                /FTId=VSP_009280.
FT   VAR_SEQ     280    285       SSQGAI -> R (in isoform 1).
FT                                /FTId=VSP_028795.
FT   CONFLICT      7      7       K -> N (in Ref. 1; AAL24820).
FT   CONFLICT    332    332       L -> M (in Ref. 4; BAE31195).
SQ   SEQUENCE   400 AA;  44503 MW;  0614F451F4B4370F CRC64;
     MDFNMKKLAS DAGIFFTRAV QFTEEKFGQA EKTELDAHFE NLLARADSTK NWTERILRQT
     EVLLQPNPSA RVEEFLYEKL DRKVPSRVTN GELLAQYMAE AASELGPSTP YGKTLIKVSE
     AEKRLGAAER DFIHTASLSF LTPLRNFLEG DWKTISKERR LLQNRRLDLD ACKARLKKAK
     AAEAKATTVP DFQETRPRNY ILSASASALW NDEVDKAEQE LRVAQTEFDR QAEVTRLLLE
     GISSTHVNHL RCLHEFVKSQ TTYYAQCYRH MLDLQKQLGS SQGAIFPGTF VGTTEPASPP
     LSSTSPTTTA ATMPVVPTGA VLAPPEEAAL CLEEVAPPAS GTRKARVLYD YEAADSSELA
     LLADELITVY SLPGMDPDWL IGERGNKKGK VPVTYLELLS
//
ID   I2BP1_MOUSE             Reviewed;         584 AA.
AC   Q8R3Y8; Q8BJC9; Q8C0B1; Q8CI76;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Interferon regulatory factor 2-binding protein 1;
DE            Short=IRF-2-binding protein 1;
DE            Short=IRF-2BP1;
GN   Name=Irf2bp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Eye, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384; SER-436 AND
RP   SER-453, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-453, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Acts as a transcriptional repressor. Acts as a
CC       transcriptional corepressor in a IRF2-dependent manner. This
CC       repression is not mediated at least in part by histone deacetylase
CC       activities (By similarity).
CC   -!- SUBUNIT: Interacts with IRF2. Part of a corepressor complex
CC       containing IRF2 and IRF2BP2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R3Y8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R3Y8-2; Sequence=VSP_032768;
CC   -!- DOMAIN: The C-terminal RING-type zinc finger domain is necessary
CC       for interaction with BAP1 (By similarity).
CC   -!- SIMILARITY: Belongs to the IRF2BP family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK031834; BAC27572.1; -; mRNA.
DR   EMBL; AK087457; BAC39883.1; -; mRNA.
DR   EMBL; BC019164; AAH19164.2; -; mRNA.
DR   EMBL; BC036162; AAH36162.1; -; mRNA.
DR   IPI; IPI00453578; -.
DR   IPI; IPI00889930; -.
DR   RefSeq; NP_848872.2; NM_178757.3.
DR   UniGene; Mm.274237; -.
DR   HSSP; Q9H1B7; 2CS3.
DR   ProteinModelPortal; Q8R3Y8; -.
DR   SMR; Q8R3Y8; 499-574.
DR   PhosphoSite; Q8R3Y8; -.
DR   PRIDE; Q8R3Y8; -.
DR   Ensembl; ENSMUST00000053713; ENSMUSP00000061234; ENSMUSG00000044030.
DR   GeneID; 272359; -.
DR   KEGG; mmu:272359; -.
DR   UCSC; uc009fkc.1; mouse.
DR   CTD; 272359; -.
DR   MGI; MGI:2442159; Irf2bp1.
DR   eggNOG; roNOG09855; -.
DR   GeneTree; ENSGT00390000005089; -.
DR   HOGENOM; HBG717652; -.
DR   HOVERGEN; HBG108364; -.
DR   InParanoid; Q8R3Y8; -.
DR   OMA; PTTKDLA; -.
DR   OrthoDB; EOG4H9XMB; -.
DR   PhylomeDB; Q8R3Y8; -.
DR   NextBio; 393570; -.
DR   ArrayExpress; Q8R3Y8; -.
DR   Bgee; Q8R3Y8; -.
DR   Genevestigator; Q8R3Y8; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR022750; Interferon_reg_fac2-bd1_2.
DR   Pfam; PF11261; IRF-2BP1_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Nucleus;
KW   Phosphoprotein; Repressor; Transcription; Transcription regulation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    584       Interferon regulatory factor 2-binding
FT                                protein 1.
FT                                /FTId=PRO_0000328730.
FT   REGION      503    550       Cys-rich.
FT   COILED      197    217       Potential.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      66     66       Phosphoserine (By similarity).
FT   MOD_RES     125    125       Phosphoserine (By similarity).
FT   MOD_RES     186    186       Phosphoserine (By similarity).
FT   MOD_RES     384    384       Phosphoserine.
FT   MOD_RES     421    421       Phosphoserine (By similarity).
FT   MOD_RES     436    436       Phosphoserine.
FT   MOD_RES     453    453       Phosphoserine.
FT   MOD_RES     457    457       Phosphoserine (By similarity).
FT   VAR_SEQ       1     20       MASVQASRRQWCYLCDLPKM -> M (in isoform 2).
FT                                /FTId=VSP_032768.
FT   CONFLICT     54     54       Q -> H (in Ref. 1; BAC39883).
FT   CONFLICT     81     81       A -> P (in Ref. 1; BAC39883).
FT   CONFLICT    107    107       S -> L (in Ref. 1; BAC39883).
FT   CONFLICT    186    186       S -> T (in Ref. 1; BAC27572).
FT   CONFLICT    372    372       R -> Q (in Ref. 1; BAC27572).
SQ   SEQUENCE   584 AA;  61751 MW;  0A0DF55E967B10BE CRC64;
     MASVQASRRQ WCYLCDLPKM PWAMVWDFSE AVCRGCVNFE GADRIELLID AARQLKRSHV
     LPEGRSPGPP ALKHPTSKDL ASTGSQGSQL PPPQAQAQPS GTGGSVSGPD RYDRATSSSR
     LALPSPALEY TLGSRLANGL GREEAVAEGA RRALLGSIPS LMPPGLLAAA VSGLGGRALT
     LAPGLSPARP LFGSDFEKEK QQRNADCLAE LNEAMRGRAE EWHGRPKAVR EQLLALSACA
     PFNVRFKKDH GLVGRVFAFD ATARPPGYEF ELKLFTEYPC GSGNVYAGVL AVARQMFHDA
     LREPGKALAS SGFKYLEYER RHGSGEWRQL GELLTDGVRS FREPAPAEAL PQQYPEPAPA
     ALCGPPPRAP SRNLAPTPRR RKASPEPEGE TAGKMTTEEQ QQRHWVAPGG PYSSETPGVP
     SPIAALKNVA EALGHSPKDP GGGGGSVRAG GASPAASSTT QPPAQHRLVA RNGEAEVSPT
     AGAEAVSGGG SGTGATPGAP LCCTLCRERL EDTHFVQCPS VPGHKFCFPC SREFIKAQGP
     AGEVYCPSGD KCPLVGSSVP WAFMQGEIAT ILAGDIKVKK ERDP
//
ID   CADM4_MOUSE             Reviewed;         388 AA.
AC   Q8R464;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Cell adhesion molecule 4;
DE   AltName: Full=Immunoglobulin superfamily member 4C;
DE            Short=IgSF4C;
DE   AltName: Full=Nectin-like protein 4;
DE            Short=NECL-4;
DE   AltName: Full=TSLC1-like protein 2;
DE   Flags: Precursor;
GN   Name=Cadm4; Synonyms=Igsf4c, Necl4, Tsll2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=129/SvJ;
RX   PubMed=14659875; DOI=10.1016/j.gene.2003.09.018;
RA   Fukami T., Satoh H., Williams Y.N., Masuda M., Fukuhara H.,
RA   Maruyama T., Yageta M., Kuramochi M., Takamoto S., Murakami Y.;
RT   "Isolation of the mouse Tsll1 and Tsll2 genes, orthologues of the
RT   human TSLC1-like genes 1 and 2 (TSLL1 and TSLL2).";
RL   Gene 323:11-18(2003).
RN   [2]
RP   GLYCOSYLATION.
RX   PubMed=16261159; DOI=10.1038/sj.onc.1209192;
RA   Williams Y.N., Masuda M., Sakurai-Yageta M., Maruyama T., Shibuya M.,
RA   Murakami Y.;
RT   "Cell adhesion and prostate tumor-suppressor activity of TSLL2/IGSF4C,
RT   an immunoglobulin superfamily molecule homologous to TSLC1/IGSF4.";
RL   Oncogene 25:1446-1453(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Involved in the cell-cell adhesion. Has calcium- and
CC       magnesium-independent cell-cell adhesion activity. May have tumor-
CC       suppressor activity.
CC   -!- SUBUNIT: Monomer and homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- TISSUE SPECIFICITY: Expressed in the brain and several organs
CC       including the kidney and liver.
CC   -!- PTM: N-glycosylated.
CC   -!- SIMILARITY: Belongs to the nectin family.
CC   -!- SIMILARITY: Contains 2 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC       domain.
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DR   EMBL; AY059394; AAL29692.1; -; mRNA.
DR   IPI; IPI00153840; -.
DR   RefSeq; NP_694752.1; NM_153112.3.
DR   UniGene; Mm.178322; -.
DR   HSSP; Q8IZQ9; 1Z9M.
DR   ProteinModelPortal; Q8R464; -.
DR   SMR; Q8R464; 24-309.
DR   STRING; Q8R464; -.
DR   PhosphoSite; Q8R464; -.
DR   PRIDE; Q8R464; -.
DR   Ensembl; ENSMUST00000068023; ENSMUSP00000066880; ENSMUSG00000054793.
DR   GeneID; 260299; -.
DR   KEGG; mmu:260299; -.
DR   UCSC; uc009fps.1; mouse.
DR   CTD; 260299; -.
DR   MGI; MGI:2449088; Cadm4.
DR   eggNOG; roNOG11534; -.
DR   GeneTree; ENSGT00600000084002; -.
DR   HOGENOM; HBG402945; -.
DR   HOVERGEN; HBG057086; -.
DR   InParanoid; Q8R464; -.
DR   OMA; TGQEVQT; -.
DR   OrthoDB; EOG412M5K; -.
DR   NextBio; 392067; -.
DR   ArrayExpress; Q8R464; -.
DR   Bgee; Q8R464; -.
DR   CleanEx; MM_CADM4; -.
DR   Genevestigator; Q8R464; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   InterPro; IPR013162; CD80_C2-set.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR003585; Neurexin-like.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3.
DR   Pfam; PF08205; C2-set_2; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00294; 4.1m; 1.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 1.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   1: Evidence at protein level;
KW   Cell adhesion; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Membrane; Phosphoprotein; Repeat; Signal; Transmembrane;
KW   Transmembrane helix; Tumor suppressor.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21    388       Cell adhesion molecule 4.
FT                                /FTId=PRO_0000291981.
FT   TOPO_DOM     25    324       Extracellular (Potential).
FT   TRANSMEM    325    345       Helical; (Potential).
FT   TOPO_DOM    346    388       Cytoplasmic (Potential).
FT   DOMAIN       21    119       Ig-like V-type.
FT   DOMAIN      124    219       Ig-like C2-type 1.
FT   DOMAIN      224    307       Ig-like C2-type 2.
FT   MOD_RES     361    361       Phosphoserine.
FT   CARBOHYD     31     31       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     67     67       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    286    286       N-linked (GlcNAc...) (Potential).
FT   DISULFID     44    104       By similarity.
FT   DISULFID    145    199       By similarity.
FT   DISULFID    245    291       By similarity.
SQ   SEQUENCE   388 AA;  42723 MW;  8E3A9DF1C3B9D23E CRC64;
     MGRARRFQWP LLLLWAAAAG PGTGQEVQTE NVTVAEGGVA EITCRLHQYD GSIVVIQNPA
     RQTLFFNGTR ALKDERFQLE EFSPRRVRIR LSDARLEDEG GYFCQLYTED THHQIATLTV
     LVAPENPVVE VREQAVEGGE VELSCLVPRS RPAAVLRWYR DRKELKGVSS GQENGKVWSV
     ASTVRFRVDR KDDGGIVICE AQNQALPSGH SKQTQYVLDV QYSPTARIHA SQAVVREGDT
     LVLTCAVTGN PRPNQIRWNR GNESLPERAE AVGETLTLPG LVSADNGTYT CEAANKHGHA
     RALYVLVVYD PGAVVEAQTS VPYAIVGGIL ALLVFLIICV LVGMVWCSVR QKGSYLTHEA
     SGLDEQGEAR EAFLNGGDGH KRKEEFFI
//
ID   Q8R4B4_MOUSE            Unreviewed;       365 AA.
AC   Q8R4B4;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 43.
DE   SubName: Full=Down syndrome cell adhesion molecule-like protein;
DE   Flags: Fragment;
GN   Name=Dscaml1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ICR; TISSUE=Brain;
RA   Shimohata A., Amano K., Akagi T., Hashikawa T., Barlow G.,
RA   Korenberg J.R., Yamakawa K.;
RT   "Cloning and characterization of mouse DSCAML1.";
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the NDK family.
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DR   EMBL; AF487346; AAL99984.1; -; mRNA.
DR   IPI; IPI00408489; -.
DR   UniGene; Mm.325499; -.
DR   HSSP; P22392; 1NUE.
DR   ProteinModelPortal; Q8R4B4; -.
DR   STRING; Q8R4B4; -.
DR   PRIDE; Q8R4B4; -.
DR   PhylomeDB; Q8R4B4; -.
DR   Genevestigator; Q8R4B4; -.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:InterPro.
DR   GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR001564; Nucleoside_diP_kinase.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Gene3D; G3DSA:3.30.70.141; NDK; 1.
DR   Pfam; PF00334; NDK; 1.
DR   PRINTS; PR01243; NUCDPKINASE.
DR   SMART; SM00562; NDK; 1.
DR   SUPFAM; SSF54919; NDK; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   2: Evidence at transcript level;
FT   NON_TER     365    365
SQ   SEQUENCE   365 AA;  40482 MW;  286DBB4F528B7E19 CRC64;
     MANLERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVAMKF LRASEEHLKQ HYIDLKDRPF
     FPGLVKYMNS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRTRAEFG
     TRPPPRAGLR SRESGAPSAG GWERAERGRG AAARPAIGPP PRRIGPLYGM WLVTFLLLLD
     SLHKARPEDV GTSLYFVNDS LQHVTFSSSV GVVVPCPAAG SPSAALRWYL ATGDDIYDVP
     HIRHVHANGT LQLFPFSPSA FNSFIHDNDY FCTAENAAGK IRSPNIRIKA VFREPYTVRV
     EDQRSMRGNV AVFKCLIPSS VQEYVSVVSW EKDTVSITPE NRFFITSHGG LYISDVQKED
     ALSTY
//
ID   PURG_MOUSE              Reviewed;         350 AA.
AC   Q8R4E6; Q14B11; Q8R4E7;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Purine-rich element-binding protein gamma;
GN   Name=Purg;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC   STRAIN=B6D2 x J F1, and C57BL/6J; TISSUE=Testis;
RX   MEDLINE=22030815; PubMed=12034829; DOI=10.1093/nar/30.11.2417;
RA   Liu H., Johnson E.M.;
RT   "Distinct proteins encoded by alternative transcripts of the PURG
RT   gene, located contrapodal to WRN on chromosome 8, determined by
RT   differential termination/polyadenylation.";
RL   Nucleic Acids Res. 30:2417-2426(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-342, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND SER-166, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=PURG-A;
CC         IsoId=Q8R4E6-1; Sequence=Displayed;
CC       Name=2; Synonyms=PURG-A;
CC         IsoId=Q8R4E6-2; Sequence=VSP_021320;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is expressed in testis. Isoform 2 is
CC       expressed in blastocyst and kidney.
CC   -!- SIMILARITY: Belongs to the PUR DNA-binding protein family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF479672; AAL86450.1; -; mRNA.
DR   EMBL; AF479673; AAL86451.1; -; mRNA.
DR   EMBL; BC116406; AAI16407.1; -; mRNA.
DR   IPI; IPI00153880; -.
DR   IPI; IPI00408500; -.
DR   RefSeq; NP_001091703.1; NM_001098233.1.
DR   RefSeq; NP_690034.1; NM_152821.2.
DR   UniGene; Mm.159402; -.
DR   UniGene; Mm.475771; -.
DR   ProteinModelPortal; Q8R4E6; -.
DR   SMR; Q8R4E6; 60-324.
DR   PhosphoSite; Q8R4E6; -.
DR   PRIDE; Q8R4E6; -.
DR   Ensembl; ENSMUST00000070340; ENSMUSP00000065002; ENSMUSG00000049184.
DR   Ensembl; ENSMUST00000078058; ENSMUSP00000077205; ENSMUSG00000049184.
DR   GeneID; 75029; -.
DR   KEGG; mmu:75029; -.
DR   UCSC; uc009ljx.1; mouse.
DR   UCSC; uc009ljy.1; mouse.
DR   CTD; 75029; -.
DR   MGI; MGI:1922279; Purg.
DR   eggNOG; maNOG16609; -.
DR   GeneTree; ENSGT00390000015406; -.
DR   HOGENOM; HBG383187; -.
DR   HOVERGEN; HBG006888; -.
DR   InParanoid; Q8R4E6; -.
DR   OMA; KICNSHK; -.
DR   OrthoDB; EOG4PRSRB; -.
DR   PhylomeDB; Q8R4E6; -.
DR   NextBio; 342048; -.
DR   ArrayExpress; Q8R4E6; -.
DR   Bgee; Q8R4E6; -.
DR   CleanEx; MM_PURG; -.
DR   Genevestigator; Q8R4E6; -.
DR   GermOnline; ENSMUSG00000049184; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR006628; PUR_DNA_RNA-bd.
DR   PANTHER; PTHR12611; PUR_DNA_RNA_bd; 1.
DR   Pfam; PF04845; PurA; 1.
DR   SMART; SM00712; PUR; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Nucleus; Phosphoprotein.
FT   CHAIN         1    350       Purine-rich element-binding protein
FT                                gamma.
FT                                /FTId=PRO_0000255953.
FT   DNA_BIND     54    296       By similarity.
FT   COMPBIAS      8     27       Gly-rich.
FT   MOD_RES     163    163       Phosphoserine.
FT   MOD_RES     166    166       Phosphoserine.
FT   MOD_RES     342    342       Phosphoserine.
FT   VAR_SEQ     292    350       VSEVRPPYRNTITVPFKAWTRFGENFIKYEEEMRKICNSHK
FT                                EKRMDGRRASGEEQECLD -> LTNYPKSRENLNLFHCCQT
FT                                KHKEQPYDTPKTVEE (in isoform 2).
FT                                /FTId=VSP_021320.
FT   CONFLICT    222    222       D -> E (in Ref. 2; AAI16407).
SQ   SEQUENCE   350 AA;  39938 MW;  983142173937D7D4 CRC64;
     MERARRRGGG GSGGGRGRGG KNVGGPGLSK SRLYPQAQHS HYPHYSASAT PNQSGGTSEI
     QELASKRVDI QKKRFYLDVK QSSRGRFLKI AEVWIGRGRQ DNIRKSKLTL SLSVAAELKD
     CLGDFIEHYA HLGLKGHRQE HGQSKEQVSR RRQKHSAPSP PVSVGSEEHP HSVLKTDYIE
     RDNRKYYLDL KENQRGRFLR IRQTMMRGTG MIGYFGHSLG QDQTIVLPAQ GMIEFRDALV
     QLIEDYGEGD IEERRCGDDD PLELPEGTSF RVDNKRFYFD VGSNKYGIFL KVSEVRPPYR
     NTITVPFKAW TRFGENFIKY EEEMRKICNS HKEKRMDGRR ASGEEQECLD
//
ID   NTNG1_MOUSE             Reviewed;         539 AA.
AC   Q8R4G0; Q68FE5; Q69ZU3; Q8R4F3; Q8R4F4; Q8R4F5; Q8R4F6; Q8R4F7;
AC   Q8R4F8; Q8R4F9; Q9ESR3; Q9ESR4; Q9ESR5; Q9ESR6; Q9ESR7; Q9ESR8;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Netrin-G1;
DE   AltName: Full=Laminet-1;
DE   Flags: Precursor;
GN   Name=Ntng1; Synonyms=Kiaa0976, Lmnt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B; 1C; 1D; 1E AND 1F),
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP   GLYCOSYLATION.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=20422763; PubMed=10964959;
RA   Nakashiba T., Ikeda T., Nishimura S., Tashiro K., Honjo T.,
RA   Culotti J.G., Itohara S.;
RT   "Netrin-G1: a novel glycosyl phosphatidylinositol-linked mammalian
RT   netrin that is functionally divergent from classical netrins.";
RL   J. Neurosci. 20:6540-6550(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B; 1C; 1D; 1E; 1F; 1G; 1H;
RP   1I AND 1J), AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=21904814; PubMed=11906208; DOI=10.1006/mcne.2001.1089;
RA   Yin Y., Miner J.H., Sanes J.R.;
RT   "Laminets: laminin- and netrin-related genes expressed in distinct
RT   neuronal subsets.";
RL   Mol. Cell. Neurosci. 19:344-358(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1E).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1C).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1C).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   MEDLINE=21664097; PubMed=11804778; DOI=10.1016/S0925-4773(01)00600-1;
RA   Nakashiba T., Nishimura S., Ikeda T., Itohara S.;
RT   "Complementary expression and neurite outgrowth activity of netrin-G
RT   subfamily members.";
RL   Mech. Dev. 111:47-60(2002).
CC   -!- FUNCTION: Promotes neurite outgrowth of both axons and dendrites.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=10;
CC       Name=1A; Synonyms=G1a;
CC         IsoId=Q8R4G0-1; Sequence=Displayed;
CC       Name=1B; Synonyms=G1b;
CC         IsoId=Q8R4G0-2; Sequence=VSP_050547, VSP_050548;
CC       Name=1C; Synonyms=G1c;
CC         IsoId=Q8R4G0-3; Sequence=VSP_050549, VSP_050550;
CC       Name=1D; Synonyms=G1d;
CC         IsoId=Q8R4G0-4; Sequence=VSP_050551;
CC       Name=1E; Synonyms=G1e;
CC         IsoId=Q8R4G0-5; Sequence=VSP_050552, VSP_050553;
CC       Name=1F; Synonyms=G1f;
CC         IsoId=Q8R4G0-6; Sequence=VSP_050554, VSP_050555;
CC       Name=1G;
CC         IsoId=Q8R4G0-7; Sequence=VSP_050558, VSP_050559;
CC       Name=1H;
CC         IsoId=Q8R4G0-8; Sequence=VSP_050560, VSP_050561;
CC       Name=1I;
CC         IsoId=Q8R4G0-9; Sequence=VSP_050556, VSP_050557;
CC       Name=1J;
CC         IsoId=Q8R4G0-10; Sequence=VSP_050546;
CC   -!- TISSUE SPECIFICITY: Expression is restricted primarily to neurons
CC       of the CNS, particularly in the dorsal thalamus, olfactory bulb
CC       and inferior colliculus. Isoform 1A and isoform 1D are the major
CC       products in adult brain.
CC   -!- DEVELOPMENTAL STAGE: Detected in the midbrain and the hindbrain
CC       regions as early as 12 dpc. In the deep nucleus of the cerebellum,
CC       as well as in the inferior colliculus and the thalamic regions,
CC       expression is detected at 14 dpc, persists to postnatal day 0 and
CC       is down-regulated by postnatal day 12. At 14 dpc, expression is
CC       segmented in dorsal thalamus and pretectum in the midbrain and is
CC       regulated in a layer-specific manner in the superior colliculus.
CC       In the olfactory bulb, expression is detected at 14 dpc, increases
CC       by postnatal day 0 and is maintained at a high level through
CC       postnatal day 21 and into adulthood.
CC   -!- PTM: N-glycosylated.
CC   -!- SIMILARITY: Contains 3 laminin EGF-like domains.
CC   -!- SIMILARITY: Contains 1 laminin N-terminal domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32353.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB038662; BAB12005.1; -; mRNA.
DR   EMBL; AB038663; BAB12006.1; -; mRNA.
DR   EMBL; AB038664; BAB12007.1; -; mRNA.
DR   EMBL; AB038665; BAB12008.1; -; mRNA.
DR   EMBL; AB038666; BAB12009.1; -; mRNA.
DR   EMBL; AB038667; BAB12010.1; -; mRNA.
DR   EMBL; AF475069; AAL84778.1; -; mRNA.
DR   EMBL; AF475070; AAL84779.1; -; mRNA.
DR   EMBL; AF475071; AAL84780.1; -; mRNA.
DR   EMBL; AF475072; AAL84781.1; -; mRNA.
DR   EMBL; AF475073; AAL84782.1; -; mRNA.
DR   EMBL; AF475074; AAL84783.1; -; mRNA.
DR   EMBL; AF475075; AAL84784.1; -; mRNA.
DR   EMBL; AF475076; AAL84785.1; -; mRNA.
DR   EMBL; AF475077; AAL84786.1; -; mRNA.
DR   EMBL; AF475078; AAL84787.1; -; mRNA.
DR   EMBL; AK034465; BAC28717.1; -; mRNA.
DR   EMBL; AK173075; BAD32353.1; ALT_INIT; mRNA.
DR   EMBL; BC079881; AAH79881.1; -; mRNA.
DR   IPI; IPI00323012; -.
DR   IPI; IPI00323015; -.
DR   IPI; IPI00323016; -.
DR   IPI; IPI00323017; -.
DR   IPI; IPI00354768; -.
DR   IPI; IPI00354771; -.
DR   IPI; IPI00354773; -.
DR   IPI; IPI00465860; -.
DR   IPI; IPI00469999; -.
DR   IPI; IPI00742371; -.
DR   RefSeq; NP_001156820.1; NM_001163348.1.
DR   RefSeq; NP_001156821.1; NM_001163349.1.
DR   RefSeq; NP_001156822.1; NM_001163350.1.
DR   RefSeq; NP_001156823.1; NM_001163351.1.
DR   RefSeq; NP_109624.1; NM_030699.2.
DR   RefSeq; NP_597995.1; NM_133488.1.
DR   UniGene; Mm.39262; -.
DR   ProteinModelPortal; Q8R4G0; -.
DR   SMR; Q8R4G0; 96-176, 297-536.
DR   DIP; DIP-46447N; -.
DR   STRING; Q8R4G0; -.
DR   PRIDE; Q8R4G0; -.
DR   Ensembl; ENSMUST00000072596; ENSMUSP00000072397; ENSMUSG00000059857.
DR   Ensembl; ENSMUST00000106569; ENSMUSP00000102179; ENSMUSG00000059857.
DR   Ensembl; ENSMUST00000106570; ENSMUSP00000102180; ENSMUSG00000059857.
DR   Ensembl; ENSMUST00000106571; ENSMUSP00000102181; ENSMUSG00000059857.
DR   Ensembl; ENSMUST00000106573; ENSMUSP00000102183; ENSMUSG00000059857.
DR   Ensembl; ENSMUST00000106575; ENSMUSP00000102185; ENSMUSG00000059857.
DR   GeneID; 80883; -.
DR   KEGG; mmu:80883; -.
DR   UCSC; uc008rai.1; mouse.
DR   UCSC; uc008raj.1; mouse.
DR   UCSC; uc008rak.1; mouse.
DR   UCSC; uc008ral.1; mouse.
DR   UCSC; uc008ram.1; mouse.
DR   UCSC; uc008rao.1; mouse.
DR   UCSC; uc008rap.1; mouse.
DR   UCSC; uc008raq.1; mouse.
DR   UCSC; uc008rar.1; mouse.
DR   CTD; 80883; -.
DR   MGI; MGI:1934028; Ntng1.
DR   GeneTree; ENSGT00560000076902; -.
DR   HOVERGEN; HBG052676; -.
DR   InParanoid; Q8R4G0; -.
DR   OMA; YCECFGH; -.
DR   NextBio; 350195; -.
DR   ArrayExpress; Q8R4G0; -.
DR   Bgee; Q8R4G0; -.
DR   CleanEx; MM_NTNG1; -.
DR   Genevestigator; Q8R4G0; -.
DR   GermOnline; ENSMUSG00000059857; Mus musculus.
DR   GO; GO:0046658; C:anchored to plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:InterPro.
DR   GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR002049; EGF_laminin.
DR   InterPro; IPR008211; Laminin_N.
DR   Pfam; PF00053; Laminin_EGF; 3.
DR   Pfam; PF00055; Laminin_N; 1.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00180; EGF_Lam; 3.
DR   SMART; SM00136; LamNT; 1.
DR   PROSITE; PS00022; EGF_1; 3.
DR   PROSITE; PS01186; EGF_2; FALSE_NEG.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 1.
DR   PROSITE; PS50027; EGF_LAM_2; 3.
DR   PROSITE; PS51117; LAMININ_NTER; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Developmental protein;
KW   Differentiation; Disulfide bond; Glycoprotein; GPI-anchor;
KW   Laminin EGF-like domain; Lipoprotein; Membrane; Neurogenesis; Repeat;
KW   Signal.
FT   SIGNAL        1     18       Potential.
FT   CHAIN        19    510       Netrin-G1.
FT                                /FTId=PRO_0000017093.
FT   PROPEP      511    539       Removed in mature form (Potential).
FT                                /FTId=PRO_0000017094.
FT   DOMAIN       46    296       Laminin N-terminal.
FT   DOMAIN      297    356       Laminin EGF-like 1.
FT   DOMAIN      364    419       Laminin EGF-like 2.
FT   DOMAIN      420    469       Laminin EGF-like 3.
FT   LIPID       510    510       GPI-anchor amidated serine (Potential).
FT   CARBOHYD    133    133       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    320    320       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    406    406       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    433    433       N-linked (GlcNAc...) (Potential).
FT   DISULFID    297    306       Potential.
FT   DISULFID    299    315       Potential.
FT   DISULFID    317    326       Potential.
FT   DISULFID    329    354       Potential.
FT   DISULFID    364    373       Potential.
FT   DISULFID    366    384       Potential.
FT   DISULFID    387    396       Potential.
FT   DISULFID    399    417       Potential.
FT   DISULFID    420    432       Potential.
FT   DISULFID    422    438       Potential.
FT   DISULFID    440    449       Potential.
FT   DISULFID    452    462       Potential.
FT   DISULFID    488    497       By similarity.
FT   VAR_SEQ     297    539       Missing (in isoform 1J).
FT                                /FTId=VSP_050546.
FT   VAR_SEQ     363    464       NCECFGHSNRCSYIDLLNTVICVSCKHNTRGQHCELCRLGY
FT                                FRNASAQLDDENVCIECYCNPLGSIHDRCNGSGFCECKTGT
FT                                TGPKCDECLPGNSWYYGCQP -> TPPKFNRIWPNISSLEV
FT                                SNPKQVAPKLALSTVSSVQVANHKRA (in isoform
FT                                1D).
FT                                /FTId=VSP_050551.
FT   VAR_SEQ     363    463       Missing (in isoform 1C).
FT                                /FTId=VSP_050549.
FT   VAR_SEQ     363    418       Missing (in isoform 1B).
FT                                /FTId=VSP_050547.
FT   VAR_SEQ     363    388       NCECFGHSNRCSYIDLLNTVICVSCK -> TPPKFNRIWPN
FT                                ISSLEVSNPKQGRSI (in isoform 1I).
FT                                /FTId=VSP_050556.
FT   VAR_SEQ     363    385       NCECFGHSNRCSYIDLLNTVICV -> TPPKFNRIWPNISS
FT                                LEVSNPKQA (in isoform 1E).
FT                                /FTId=VSP_050552.
FT   VAR_SEQ     363    364       NC -> SK (in isoform 1F).
FT                                /FTId=VSP_050554.
FT   VAR_SEQ     365    539       Missing (in isoform 1F).
FT                                /FTId=VSP_050555.
FT   VAR_SEQ     386    464       Missing (in isoform 1E).
FT                                /FTId=VSP_050553.
FT   VAR_SEQ     389    539       Missing (in isoform 1I).
FT                                /FTId=VSP_050557.
FT   VAR_SEQ     419    463       Missing (in isoform 1G).
FT                                /FTId=VSP_050558.
FT   VAR_SEQ     419    438       ECYCNPLGSIHDRCNGSGFC -> GQFHYDFSFCSVPLELW
FT                                GAG (in isoform 1H).
FT                                /FTId=VSP_050560.
FT   VAR_SEQ     419    419       E -> K (in isoform 1B).
FT                                /FTId=VSP_050548.
FT   VAR_SEQ     439    539       Missing (in isoform 1H).
FT                                /FTId=VSP_050561.
FT   VAR_SEQ     464    464       P -> T (in isoform 1C).
FT                                /FTId=VSP_050550.
FT   VAR_SEQ     464    464       P -> A (in isoform 1G).
FT                                /FTId=VSP_050559.
FT   CONFLICT    166    166       L -> F (in Ref. 2; AAL84778/AAL84780/
FT                                AAL84781/AAL84782/AAL84784/AAL84785/
FT                                AAL84786/AAL84787).
SQ   SEQUENCE   539 AA;  60566 MW;  DDC9BA2C577B29D5 CRC64;
     MYLSRFLSIH ALWVTVSSVM QPYLFVWGHY DVCKSLIYTE EGKVWDYTAC QPESTDMTKY
     LKVKLDPPDI TCGDPPESFC AMGNPYMCNN ECDASTPELA HPPELMFDFE GRHPSTFWQS
     ATWKEYPKPL QVNITLSWSK TIELTDNIVI TFESGRPDQM ILEKSLDYGR TWQPYQYYAT
     DCLHAFHMDP KSVKDLSQHT VLEIICTEEY STGYSTNSKI IHFEIKDRFA FFAGPRLRNM
     ASLYGQLDTT KKLRDFFTVT DLRIRLLRPA VGEIFVDELH LARYFYAISD IKVRGRCKCN
     LHATSCLYDN SKLTCECEHN TTGPDCGKCK KNYQGRPWSP GSYLPIPKGT ANTCIPSISS
     IGNCECFGHS NRCSYIDLLN TVICVSCKHN TRGQHCELCR LGYFRNASAQ LDDENVCIEC
     YCNPLGSIHD RCNGSGFCEC KTGTTGPKCD ECLPGNSWYY GCQPNVCDNE LLHCQNGGTC
     QNNVRCACPD AYTGILCEKL RCEEAGSCGS ESGQGAPPRG SPALLLLTML LGTAGPLVF
//
ID   ARHGC_MOUSE             Reviewed;        1543 AA.
AC   Q8R4H2; Q80U18;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Rho guanine nucleotide exchange factor 12;
DE   AltName: Full=Leukemia-associated RhoGEF;
GN   Name=Arhgef12; Synonyms=Kiaa0382, Larg;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Zinovyeva M.V., Sveshnikova E.V., Visser J.M., Belyavsky A.V.;
RT   "A novel murine gene encoding guanine nucleotide exchange factor and
RT   expressed in non-differentiated hematopoietic cells.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=22380910; PubMed=12492428;
RX   DOI=10.1046/j.1460-9568.2002.02402.x;
RA   Kuner R., Swiercz J.M., Zywietz A., Tappe A., Offermanns S.;
RT   "Characterization of the expression of PDZ-RhoGEF, LARG and
RT   G(alpha)12/G(alpha)13 proteins in the murine nervous system.";
RL   Eur. J. Neurosci. 16:2333-2341(2002).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-637, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May play a role in the regulation of RhoA GTPase by
CC       guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13).
CC       Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase
CC       and may act as GTPase-activating protein (GAP) for GNA12 and GNA13
CC       (By similarity).
CC   -!- SUBUNIT: Interacts with GNA12 and GNA13, probably through the RGS-
CC       like domain, with RHOA, PLXNB1 and PLXNB2, and through its PDZ
CC       domain with IGF1R beta subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). Membrane (Probable).
CC       Note=Translocated to the membrane upon stimulation (Probable).
CC   -!- TISSUE SPECIFICITY: Expressed in brain, predominantly in neuronal
CC       cell bodies.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 RGSL (RGS-like) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65549.1; Type=Erroneous initiation;
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DR   EMBL; AF467766; AAL87100.1; -; mRNA.
DR   EMBL; AK122267; BAC65549.1; ALT_INIT; mRNA.
DR   IPI; IPI00754880; -.
DR   UniGene; Mm.275266; -.
DR   ProteinModelPortal; Q8R4H2; -.
DR   SMR; Q8R4H2; 67-151, 345-559, 766-1138.
DR   MINT; MINT-1774761; -.
DR   STRING; Q8R4H2; -.
DR   PhosphoSite; Q8R4H2; -.
DR   PRIDE; Q8R4H2; -.
DR   Ensembl; ENSMUST00000072767; ENSMUSP00000072547; ENSMUSG00000059495.
DR   UCSC; uc009pba.1; mouse.
DR   MGI; MGI:1916882; Arhgef12.
DR   GeneTree; ENSGT00600000084190; -.
DR   HOGENOM; HBG716584; -.
DR   HOVERGEN; HBG050571; -.
DR   InParanoid; Q8R4H2; -.
DR   OrthoDB; EOG4BRWK1; -.
DR   ArrayExpress; Q8R4H2; -.
DR   Bgee; Q8R4H2; -.
DR   CleanEx; MM_ARHGEF12; -.
DR   Genevestigator; Q8R4H2; -.
DR   GermOnline; ENSMUSG00000059495; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR015212; Regulat_G_prot_signal-like.
DR   InterPro; IPR016137; Regulat_G_prot_signal_superfam.
DR   InterPro; IPR015721; RhoGEF-like.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   PANTHER; PTHR22825; RhoGEF_like; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF09128; RGS-like; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF48097; Regulat_G_prot_signal_superfam; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; GTPase activation;
KW   Guanine-nucleotide releasing factor; Membrane; Phosphoprotein.
FT   CHAIN         1   1543       Rho guanine nucleotide exchange factor
FT                                12.
FT                                /FTId=PRO_0000080931.
FT   DOMAIN       72    151       PDZ.
FT   DOMAIN      367    558       RGSL.
FT   DOMAIN      787    977       DH.
FT   DOMAIN     1019   1132       PH.
FT   COILED      194    262       Potential.
FT   COILED      981   1004       Potential.
FT   MOD_RES      22     22       Phosphoserine.
FT   MOD_RES      41     41       Phosphoserine (By similarity).
FT   MOD_RES     341    341       Phosphoserine (By similarity).
FT   MOD_RES     637    637       Phosphoserine.
FT   MOD_RES     736    736       Phosphothreonine (By similarity).
FT   MOD_RES    1288   1288       Phosphoserine (By similarity).
FT   MOD_RES    1327   1327       Phosphoserine (By similarity).
FT   CONFLICT    307    307       A -> V (in Ref. 2; BAC65549).
FT   CONFLICT    320    320       S -> L (in Ref. 2; BAC65549).
FT   CONFLICT    334    334       E -> QE (in Ref. 2).
FT   CONFLICT   1447   1447       A -> T (in Ref. 2; BAC65549).
SQ   SEQUENCE   1543 AA;  172322 MW;  B017F7EB1CF273D7 CRC64;
     MSGTQSTITD RFPLKKPIRH GSILNRESPT DKKQKVERSS SHDFDPTDSS SKKTKSSSEE
     SRSEIYGLVQ RCVIIQKDDN GFGLTVSGDN PVFVQSVKED GAAMRAGVQT GDRIIKVNGT
     LVTHSNHLEV VKLIRSGSYV ALTVQGRPPG SPQIPLADSE VEPSVTGHMS PIMTSPHSPG
     AAGNMERITS PVLVGEENNV VHNQKVEILR KMLQKEQERL QLLQEDYNRT ATQRLLKEIQ
     EAKKHIPQLQ EQLSKATGSA QDGAVIAPSR PLGDALTLSE AEADPGDGLC RTDWSSGDAS
     RPSSDSADSP KSSLRERSYS EEAPERSEGV QDAEPQSLVG SPSTRGAPHI IGAEDDDFGT
     EHEQINGQCS CFQSIELLKS RPAHLAVFLH HVVSQFDPAT LLCYLYSDLY KQTNSKETRR
     VFLEFHQFFL DRSAHLKVPV PEEISVDLEK RRPELIPEDL HRLYIQTMQE RVHPEVQRHL
     EDFRQKRSMG LTLAESELTK LDAERDKDRG TLEKERACAE QIVTKIEEVL MTAQAVEEER
     SSTMQYVILM YMKYLGVKVK EPRNLEHKRG RIGFLPKIKQ SMKKDREGEE KGKRRGFPSI
     LGPPRRPSRH DNSAIGRAME IQKSRHPKHL STPSSVSPEP QDPAKLRQSG VANEGTDTGY
     LPASSMSSAT SGTALSQEGG RENDTGTKQV GEASAPGDCL DSTPRVPTTV FDFPPPLLDQ
     VQEEECEVER VAEHGTPKPF RKFDSIAFGE SQSEDEQFEN DLETDPPNWQ QLVSREVLLG
     LKPSEIKRQE VINELFYTER AHVRTLKVLD QVFYQRVSRE GILSPSELRK IFSNLEDILQ
     LHVGLNEQMK AVRKRNETSV IDHIGEDLLI WFSGPGEEKL KHAAATFCSN QPFALEMIKS
     RQKKDSRFHT FVQDAESNPL CRRLQLKDII PTQMQRLTKY PLLLDNIAKY TEWPPEREKV
     KKAADHCRQI LNYVNQAVRE AENKQRLEDY QRRLDTSNLK LSEYPNVDEL RNLDLTKRKM
     IHEGPLVWKV NRDKSIDLYT LLLEDILVLL QKQDDRLVLR CHSKILASTA DSKHTFSPVI
     KLSTVLVRQV ATDNKALFVI SMSDNGAQIY ELVAQTVSEK TVWQDLICRM AASVKEQSTK
     PIPLPQPPPC EGDNDEEEPA KLKVEHHDLS VAGLQSPDRV LGLESPLISS KPQSHSLNTP
     GKSAAEHLFV TATQFAKEQH ANGALKEGDG GYPVTIPGPH LPVSEERWAL DALRNLGLLK
     QLLVQQLGLT EKSTQEDWQS FSRYGPASEE VQADSGIRDL ENVKACHARE GQMSFKTGTG
     DIATCDSPRT STESCAAQDS VILASQDSQA SNVLVMDHMI LTPEMPPAEP EGGLDESGEH
     FFDAREAHSD DNPSEGDGAV KKEEKDVNLR ISGNCLILDG YDAVQESSTD EEVASSFPLQ
     PVTGIPAVDS SHQQQHSPQN VHPEGPVSPF TPEFLVQRHW RAMEDTCFEI QSPSCTDSQS
     QILEYIHKIE ADLEHLKKVE ESYALLCQRL AGSALPDKLS DKS
//
ID   NETO1_MOUSE             Reviewed;         533 AA.
AC   Q8R4I7; Q80X39; Q8C4S3; Q8CCM2;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 2.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Neuropilin and tolloid-like protein 1;
DE   AltName: Full=Brain-specific transmembrane protein containing 2 CUB and 1 LDL-receptor class A domains protein 1;
DE   Flags: Precursor;
GN   Name=Neto1; Synonyms=Btcl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   MEDLINE=21940629; PubMed=11943477; DOI=10.1016/S0378-1119(02)00438-9;
RA   Stoehr H., Berger C., Froehlich S., Weber B.H.F.;
RT   "A novel gene encoding a putative transmembrane protein with two
RT   extracellular CUB domains and a low-density lipoprotein class A
RT   module: isolation of alternatively spliced isoforms in retina and
RT   brain.";
RL   Gene 286:223-231(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=12810072; DOI=10.1016/S0006-291X(03)01035-0;
RA   Michishita M., Ikeda T., Nakashiba T., Ogawa M., Tashiro K., Honjo T.,
RA   Doi K., Itohara S., Endo S.;
RT   "A novel gene, Btcl1, encoding CUB and LDLa domains is expressed in
RT   restricted areas of mouse brain.";
RL   Biochem. Biophys. Res. Commun. 306:680-686(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15464227; DOI=10.1016/j.devbrainres.2004.06.012;
RA   Michishita M., Ikeda T., Nakashiba T., Ogawa M., Tashiro K., Honjo T.,
RA   Doi K., Itohara S., Endo S.;
RT   "Expression of Btcl2, a novel member of Btcl gene family, during
RT   development of the central nervous system.";
RL   Brain Res. Dev. Brain Res. 153:135-142(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-417, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR
RP   LOCATION, AND INTERACTION WITH GRIN2A; GRIN2B; DLG2; DLG3 AND DLG4.
RX   PubMed=19243221; DOI=10.1371/journal.pbio.1000041;
RA   Ng D., Pitcher G.M., Szilard R.K., Sertie A., Kanisek M.,
RA   Clapcote S.J., Lipina T., Kalia L.V., Joo D., McKerlie C., Cortez M.,
RA   Roder J.C., Salter M.W., McInnes R.R.;
RT   "Neto1 is a novel CUB-domain NMDA receptor-interacting protein
RT   required for synaptic plasticity and learning.";
RL   PLoS Biol. 7:E41-E41(2009).
CC   -!- FUNCTION: Involved in the development and/or maintenance of
CC       neuronal circuitry. Accessory subunit of the neuronal N-methyl-D-
CC       aspartate receptor (NMDAR) critical for maintaining the abundance
CC       of GRIN2A-containing NMDARs in the postsynaptic density. Regulates
CC       long-term NMDA receptor-dependent synaptic plasticity and
CC       cognition, at least in the context of spatial learning and memory.
CC   -!- SUBUNIT: Interacts with PLZ domains of DLG2, DLG3 and DLG4 via its
CC       C-terminal TRV domain. Interacts with GRIN2A and GRIN2B via its
CC       CUB domains.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential). Cell junction, synapse, postsynaptic cell
CC       membrane, postsynaptic density. Note=Component of the postsynaptic
CC       density (PSD) of excitatory synapses.
CC   -!- TISSUE SPECIFICITY: Expressed only in brain. Present throughout
CC       the central nervous system. Highly expressed in the hippocampal
CC       CA3 region, olfactory bulb and tubercle, caudate putamen, and
CC       neocortex in the adult brain.
CC   -!- DEVELOPMENTAL STAGE: Observed restrictively in brain throughout
CC       embryonic and postnatal stages. Expression pattern in brain
CC       slightly changes from E13 to postnatal day 21 (P21). Expressed in
CC       both cerebrum and cerebellum throughout P0 to P35. In the cerebrum
CC       expression reached a plateau at P14 while expression in the
CC       cerebellum remains constant throughout all postnatal stages.
CC   -!- DISRUPTION PHENOTYPE: Depressed long-term potentiation (LTP) at
CC       Schaffer collateral-CA1 synapses, NMDAR-dependent spatial learning
CC       and memory. Rescued by the ampakine CX546 at physiological doses.
CC   -!- SIMILARITY: Contains 2 CUB domains.
CC   -!- SIMILARITY: Contains 1 LDL-receptor class A domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF448840; AAM18028.1; -; mRNA.
DR   EMBL; AY138990; AAN38318.1; -; mRNA.
DR   EMBL; AK032510; BAC27902.1; -; mRNA.
DR   EMBL; AK081325; BAC38196.1; -; mRNA.
DR   EMBL; BC051145; AAH51145.1; -; mRNA.
DR   IPI; IPI00330652; -.
DR   RefSeq; NP_659195.3; NM_144946.4.
DR   UniGene; Mm.329578; -.
DR   ProteinModelPortal; Q8R4I7; -.
DR   SMR; Q8R4I7; 39-325.
DR   DIP; DIP-48395N; -.
DR   STRING; Q8R4I7; -.
DR   PhosphoSite; Q8R4I7; -.
DR   PRIDE; Q8R4I7; -.
DR   Ensembl; ENSMUST00000058829; ENSMUSP00000057340; ENSMUSG00000050321.
DR   GeneID; 246317; -.
DR   KEGG; mmu:246317; -.
DR   UCSC; uc008fuz.1; mouse.
DR   CTD; 246317; -.
DR   MGI; MGI:2180216; Neto1.
DR   eggNOG; roNOG11571; -.
DR   GeneTree; ENSGT00600000084035; -.
DR   HOGENOM; HBG445620; -.
DR   HOVERGEN; HBG052600; -.
DR   InParanoid; Q8R4I7; -.
DR   OMA; TEAVDCK; -.
DR   OrthoDB; EOG42V8G1; -.
DR   PhylomeDB; Q8R4I7; -.
DR   NextBio; 387225; -.
DR   ArrayExpress; Q8R4I7; -.
DR   Bgee; Q8R4I7; -.
DR   CleanEx; MM_NETO1; -.
DR   Genevestigator; Q8R4I7; -.
DR   GermOnline; ENSMUSG00000050321; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0060076; C:excitatory synapse; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007613; P:memory; IMP:UniProtKB.
DR   GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:UniProtKB.
DR   GO; GO:0008542; P:visual learning; IMP:UniProtKB.
DR   InterPro; IPR000859; CUB.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   Gene3D; G3DSA:2.60.120.290; CUB; 2.
DR   Gene3D; G3DSA:4.10.400.10; LDL_rcpt_classA_cys-rich; 1.
DR   Pfam; PF00431; CUB; 2.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00192; LDLa; 1.
DR   SUPFAM; SSF49854; CUB; 2.
DR   SUPFAM; SSF57424; LDL_rcpt_classA_cys-rich; 1.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Disulfide bond; Glycoprotein; Membrane;
KW   Phosphoprotein; Postsynaptic cell membrane; Receptor; Repeat; Signal;
KW   Synapse; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     22       Potential.
FT   CHAIN        23    533       Neuropilin and tolloid-like protein 1.
FT                                /FTId=PRO_0000021800.
FT   TOPO_DOM     23    344       Extracellular (Potential).
FT   TRANSMEM    345    365       Helical; (Potential).
FT   TOPO_DOM    366    533       Cytoplasmic (Potential).
FT   DOMAIN       41    155       CUB 1.
FT   DOMAIN      172    287       CUB 2.
FT   DOMAIN      291    327       LDL-receptor class A.
FT   MOTIF       531    533       PDZ-binding.
FT   MOD_RES     417    417       Phosphotyrosine.
FT   CARBOHYD    306    306       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    340    340       N-linked (GlcNAc...) (Potential).
FT   DISULFID     41     68       By similarity.
FT   DISULFID     96    118       By similarity.
FT   DISULFID    172    202       By similarity.
FT   DISULFID    229    251       By similarity.
FT   DISULFID    292    304       By similarity.
FT   DISULFID    299    317       By similarity.
FT   DISULFID    311    326       By similarity.
FT   CONFLICT     80     80       I -> F (in Ref. 3; BAC38196).
FT   CONFLICT    514    514       R -> Q (in Ref. 1; AAM18028 and 3;
FT                                BAC38196).
SQ   SEQUENCE   533 AA;  60242 MW;  6375B395421D558F CRC64;
     MIYGRSLFHI IASLIILHSS GATKKGTEKQ ITPETQKSVQ CGTWTKHAEG GVFTSPNYPS
     KYPPDRECVY IIEAAPRQCI ELYFDEKYSI EPSWECKFDH IEVRDGPFGF SPIIGRFCGQ
     QNPPVIKSSG RFLWIKFFAD GELESMGFSA RYNFTPDPDF KDLGVLKPLP ACEFEMGGPE
     GIVESIQILK EGKASASEAV DCKWYIRAPP RSKIYLRFLD YEMQNSNECK RNFVAVYDGS
     SSVEDLKAKF CSTVANDVML RTGLGVIRMW ADEGSRNSRF QMLFTSFQEP PCEGNTFFCH
     SNMCINNTLV CNGLQNCVYP WDENHCKEKR KTSLLDQLTN TSGTVIGVTS CIVIILIIVS
     VIVQIKQPRK KYVQRKSDFD QTVFQEVFEP PHYELCTLRG TGATADFADV AEDFENYHKL
     RRSSSKCIHD HHCGSQLSSA KGSRSNLSTR DASILAEIPT QPVKPLIPPV NRRNILVMKH
     NYSQDAADAC DIDEIEEVPT TSHRLSRHEK SVQRFCLIGS LSKHESEYNT TRV
//
ID   MRP7_MOUSE              Reviewed;        1501 AA.
AC   Q8R4P9; Q3TCQ0; Q3V0D1; Q8R4S1;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Multidrug resistance-associated protein 7;
DE   AltName: Full=ATP-binding cassette sub-family C member 10;
GN   Name=Abcc10; Synonyms=Mrp7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Spleen;
RX   MEDLINE=21940637; PubMed=11943485; DOI=10.1016/S0378-1119(02)00461-4;
RA   Kao H.-H., Huang J.-D., Chang M.-S.;
RT   "cDNA cloning and genomic organization of the murine MRP7, a new ATP-
RT   binding cassette transporter.";
RL   Gene 286:299-306(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-1422 (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: ATP-dependent transporter probably involved in cellular
CC       detoxification through lipophilic anion extrusion (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Mrp7B;
CC         IsoId=Q8R4P9-1; Sequence=Displayed;
CC       Name=2; Synonyms=Mrp7A;
CC         IsoId=Q8R4P9-2; Sequence=VSP_021081, VSP_021082;
CC       Name=3;
CC         IsoId=Q8R4P9-3; Sequence=VSP_021083;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues tested including
CC       liver, brain, heart, skeletal muscle, kidney and spleen.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryo.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC
CC       family. Conjugate transporter (TC 3.A.1.208) subfamily.
CC   -!- SIMILARITY: Contains 2 ABC transmembrane type-1 domains.
CC   -!- SIMILARITY: Contains 2 ABC transporter domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF406642; AAM18535.1; -; mRNA.
DR   EMBL; AF417121; AAM18536.1; -; mRNA.
DR   EMBL; AK133240; BAE21573.1; -; mRNA.
DR   EMBL; AK170600; BAE41905.1; -; mRNA.
DR   IPI; IPI00172274; -.
DR   IPI; IPI00230661; -.
DR   IPI; IPI00798516; -.
DR   RefSeq; NP_660122.1; NM_145140.2.
DR   RefSeq; NP_733780.1; NM_170680.2.
DR   UniGene; Mm.76543; -.
DR   HSSP; P33527; 2CBZ.
DR   ProteinModelPortal; Q8R4P9; -.
DR   SMR; Q8R4P9; 566-825, 872-1490.
DR   STRING; Q8R4P9; -.
DR   PhosphoSite; Q8R4P9; -.
DR   PRIDE; Q8R4P9; -.
DR   Ensembl; ENSMUST00000047970; ENSMUSP00000038041; ENSMUSG00000032842.
DR   Ensembl; ENSMUST00000095261; ENSMUSP00000092895; ENSMUSG00000032842.
DR   GeneID; 224814; -.
DR   KEGG; mmu:224814; -.
DR   UCSC; uc008csn.1; mouse.
DR   UCSC; uc008cso.1; mouse.
DR   CTD; 224814; -.
DR   MGI; MGI:2386976; Abcc10.
DR   eggNOG; roNOG07597; -.
DR   GeneTree; ENSGT00590000083005; -.
DR   HOVERGEN; HBG107141; -.
DR   OMA; CRLPHRL; -.
DR   OrthoDB; EOG4M397Q; -.
DR   PhylomeDB; Q8R4P9; -.
DR   NextBio; 377387; -.
DR   ArrayExpress; Q8R4P9; -.
DR   Bgee; Q8R4P9; -.
DR   Genevestigator; Q8R4P9; -.
DR   GermOnline; ENSMUSG00000032842; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR017940; ABC_transporter_type1.
DR   InterPro; IPR001140; ABC_transptr_TM_dom.
DR   InterPro; IPR011527; ABC_transptrTM_dom_typ1.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF90123; ABC_TM_1; 2.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cell membrane; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1   1501       Multidrug resistance-associated protein
FT                                7.
FT                                /FTId=PRO_0000253577.
FT   TRANSMEM     32     52       Helical; (Potential).
FT   TRANSMEM     70     90       Helical; (Potential).
FT   TRANSMEM    102    122       Helical; (Potential).
FT   TRANSMEM    133    153       Helical; (Potential).
FT   TRANSMEM    172    192       Helical; (Potential).
FT   TRANSMEM    294    314       Helical; (Potential).
FT   TRANSMEM    321    341       Helical; (Potential).
FT   TRANSMEM    392    412       Helical; (Potential).
FT   TRANSMEM    415    435       Helical; (Potential).
FT   TRANSMEM    508    528       Helical; (Potential).
FT   TRANSMEM    539    559       Helical; (Potential).
FT   TRANSMEM    877    897       Helical; (Potential).
FT   TRANSMEM    969    989       Helical; (Potential).
FT   TRANSMEM   1033   1053       Helical; (Potential).
FT   TRANSMEM   1056   1076       Helical; (Potential).
FT   TRANSMEM   1158   1178       Helical; (Potential).
FT   TRANSMEM   1187   1207       Helical; (Potential).
FT   DOMAIN      286    564       ABC transmembrane type-1 1.
FT   DOMAIN      599    825       ABC transporter 1.
FT   DOMAIN      887   1215       ABC transmembrane type-1 2.
FT   DOMAIN     1255   1488       ABC transporter 2.
FT   NP_BIND     634    641       ATP 1 (Potential).
FT   NP_BIND    1289   1296       ATP 2 (Potential).
FT   MOD_RES     464    464       Phosphothreonine (By similarity).
FT   MOD_RES     468    468       Phosphoserine (By similarity).
FT   VAR_SEQ       1     41       Missing (in isoform 2).
FT                                /FTId=VSP_021081.
FT   VAR_SEQ      42     53       LAVLSACHLGTP -> MICGLLFFSFFP (in isoform
FT                                2).
FT                                /FTId=VSP_021082.
FT   VAR_SEQ    1377   1377       M -> MGESQACQRSQREAKNGHWQCSALLT (in
FT                                isoform 3).
FT                                /FTId=VSP_021083.
SQ   SEQUENCE   1501 AA;  163735 MW;  573D5CFA52DDF3BA CRC64;
     MEGLLAQLCG TDAARPLPLW EGDTTGHCFT QLVLSALPHA LLAVLSACHL GTPRTTNHSP
     ALNPGWRLRL AASFLLSIFP LLDLLPVVLP PGSRPGPLWL EVLAGCVTAV AWFTHSLALW
     ALVHSPHGRS RGPLALALAA FLPTPALVLT LLWHCQRGTF LPPLLPGPLG RVCLLILQLA
     AVLAYGLGWA APGGPQEPWT HDPFLSSESQ ETEVAEDGES WLSRFSYAWL APLLARGVRG
     ELQQPRDTCR LPRRLHPAFL ARVFQAHWKE GAQLWRALYR AFGCCYLALG LLKMVGTMLG
     FSGPLLLSLL VGFLEEGQEP LSHGLLYVLG LAGGTVISAV LQNQYGYEVR KVTLQARVAV
     LSTLYRKALK LGPSRPPTGE VLNLLGTDSE RLLNFAGSFH EAWGLPLQLA ITLYLLYQQV
     GMAFLAGLVL ALLLVPVNKV IATRIMASNQ EMLRHKDARV KLMTELLSGI RVIKFFRWEQ
     ALGDRVKACR TKELGRLRVI KYLDAACVYL WAALPVVICI TIFITYVLMG HQLTATKVFT
     ALALVRMLIL PLNNFPWVIN GLLESKVSLD RIQRFLDLPS YSPEAYYSPD PPAEPSTALE
     LHEALFSWDP IGASQKTFIS HLQVKKGMLV GIVGKVGCGK SSLLAAITGE LHRLCGWVAV
     SELSKGFGLA TQEPWIQCAT IRDNILFGKT FDAQLYREVL EACALNDDLS ILPAGDQTEV
     GEKGVTLSGG QRARIALARA VYQEKALYLL DDPLAAVDAD VANHLLHRCI LGVLSHTTRL
     LCTHRTEYLE RADVVLLMEA GQLVRTGPPS EILPLVQAVP TAWAEKEQVA TSGQSPSVCD
     LERTTEEELE VEQSTCGCLV QEESKSEGAV ALHVYRAYWR AMGSGLAAAI LVSLLLMQAT
     RNGADWWLAH WLSQLKAGRN GSREDPASCS PGSTALFSPR LLLFSPGNLY TPLLSTPLHK
     AASNGTADVH FYLIVYATIA GVNSLCTLLR AVLFAAGALQ AAASLHHRLL HRLLMAPVTF
     YDSTPSGRVL NRFSSDVACV DDSLPFLLNI LLANSVGLLG LLAVLGSGLP WLLLLLPPLS
     FVYYSVQGYY RASFRELRRL GSLTWSPLYS HLADTLAGLP VLRAAGATYR FEEENQRLLE
     LNQRCQFASY ATMQWLDIRL QLMGAAVVSA IAGIALVQHQ QGLANPGLVG LVLSYALSLT
     GLLSGLVSSF TQTEAMMVSV ERLEEYSCDV PQEPHSQPLQ SPHQQRISWL TQGSVEFQDV
     VLVYRPGLPN ALDGVTFRVE PGEKLGIVGR TGSGKSSLFL VLFRLLEPNA GRVLLDNVDT
     SQLELAELRS QLAVIPQEPF LFSGTIRENL DPQGLHEDRA LWQALEQCHL SEVAVAMGGL
     DGELGERGQN LSLGQRQLLC LARALLTDAK ILCIDEATAS VDQKTDQLLQ QTICKRFANK
     TVLTIAHRLN TILNSDRVLV LQAGRVVELD SPSALRNQPH SLFQQLLQSS QQGAHSGPSG
     C
//
ID   NUP53_MOUSE             Reviewed;         325 AA.
AC   Q8R4R6; A2ATJ3; Q9D7J2;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Nucleoporin NUP53;
DE   AltName: Full=35 kDa nucleoporin;
DE   AltName: Full=Mitotic phosphoprotein 44;
DE            Short=MP-44;
DE   AltName: Full=Nuclear pore complex protein Nup53;
DE   AltName: Full=Nucleoporin Nup35;
GN   Name=Nup35; Synonyms=Mp44, Nup53;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c;
RA   Guo J.H., Yu L.;
RT   "Molecular cloning and expression analysis of human mitotic
RT   phosphoprotein 44 gene.";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Egg, Submandibular gland, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 214-221, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 156-261.
RA   Handa N., Murayama K., Kukimoto M., Hamana H., Uchikubo T.,
RA   Takemoto C., Terada T., Shirouzu M., Yokoyama S.;
RT   "Crystal structure of the mppn domain of mouse nup35.";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Functions as a component of the nuclear pore complex
CC       (NPC). NPC components, collectively referred to as nucleoporins
CC       (NUPs), can play the role of both NPC structural components and of
CC       docking or interaction partners for transiently associated nuclear
CC       transport factors. May play a role in the association of MAD1 with
CC       the NPC (By similarity).
CC   -!- SUBUNIT: Interacts with TMEM48/NDC1, lamin B, NUP93, NUP155 and
CC       NUP205 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex (By
CC       similarity). Note=Tightly associated with the nuclear membrane and
CC       lamina (By similarity).
CC   -!- SIMILARITY: Belongs to the Nup53 family.
CC   -!- SIMILARITY: Contains 1 RRM Nup35-type domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF411517; AAL86380.1; -; mRNA.
DR   EMBL; AK009187; BAB26128.1; -; mRNA.
DR   EMBL; AK089997; BAC41034.1; -; mRNA.
DR   EMBL; AK136109; BAE22825.1; -; mRNA.
DR   EMBL; AK145775; BAE26644.1; -; mRNA.
DR   EMBL; AL928869; CAM23081.1; -; Genomic_DNA.
DR   EMBL; BC048814; AAH48814.1; -; mRNA.
DR   IPI; IPI00469331; -.
DR   RefSeq; NP_001177108.1; NM_001190179.1.
DR   RefSeq; NP_081367.1; NM_027091.4.
DR   UniGene; Mm.29200; -.
DR   PDB; 1WWH; X-ray; 2.70 A; A/B/C/D=156-261.
DR   PDBsum; 1WWH; -.
DR   ProteinModelPortal; Q8R4R6; -.
DR   SMR; Q8R4R6; 169-249.
DR   STRING; Q8R4R6; -.
DR   PhosphoSite; Q8R4R6; -.
DR   PRIDE; Q8R4R6; -.
DR   Ensembl; ENSMUST00000028382; ENSMUSP00000028382; ENSMUSG00000026999.
DR   GeneID; 69482; -.
DR   KEGG; mmu:69482; -.
DR   UCSC; uc008khs.1; mouse.
DR   CTD; 69482; -.
DR   MGI; MGI:1916732; Nup35.
DR   GeneTree; ENSGT00390000005923; -.
DR   HOGENOM; HBG715239; -.
DR   HOVERGEN; HBG060396; -.
DR   InParanoid; Q8R4R6; -.
DR   OMA; TLGSEPM; -.
DR   NextBio; 329578; -.
DR   ArrayExpress; Q8R4R6; -.
DR   Bgee; Q8R4R6; -.
DR   CleanEx; MM_NUP35; -.
DR   Genevestigator; Q8R4R6; -.
DR   GermOnline; ENSMUSG00000026999; Mus musculus.
DR   GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:UniProtKB-KW.
DR   InterPro; IPR007846; MPPN.
DR   InterPro; IPR017389; Nucleoporin_NUP53.
DR   Pfam; PF05172; MPPN; 1.
DR   PIRSF; PIRSF038119; Nucleoporin_NUP53; 1.
DR   PROSITE; PS51472; RRM_NUP35; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; mRNA transport;
KW   Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW   Translocation; Transport.
FT   CHAIN         1    325       Nucleoporin NUP53.
FT                                /FTId=PRO_0000234295.
FT   DOMAIN      169    249       RRM Nup35-type.
FT   MOD_RES      66     66       Phosphoserine (By similarity).
FT   MOD_RES      73     73       Phosphoserine (By similarity).
FT   MOD_RES      99     99       Phosphoserine (By similarity).
FT   MOD_RES     100    100       Phosphoserine (By similarity).
FT   MOD_RES     106    106       Phosphothreonine (By similarity).
FT   MOD_RES     121    121       Phosphoserine (By similarity).
FT   MOD_RES     128    128       Phosphothreonine (By similarity).
FT   MOD_RES     137    137       Phosphoserine (By similarity).
FT   MOD_RES     258    258       Phosphoserine (By similarity).
FT   MOD_RES     264    264       Phosphothreonine (By similarity).
FT   MOD_RES     272    272       Phosphothreonine (By similarity).
FT   MOD_RES     274    274       Phosphothreonine (By similarity).
FT   MOD_RES     278    278       Phosphoserine (By similarity).
FT   MOD_RES     279    279       Phosphothreonine (By similarity).
FT   MOD_RES     307    307       Phosphothreonine (By similarity).
FT   CONFLICT     13     13       L -> V (in Ref. 1; AAL86380).
FT   HELIX       170    173
FT   STRAND      174    178
FT   HELIX       182    184
FT   HELIX       185    193
FT   STRAND      198    203
FT   STRAND      205    216
FT   HELIX       217    224
FT   TURN        225    228
FT   TURN        232    234
FT   STRAND      238    241
FT   HELIX       245    248
SQ   SEQUENCE   325 AA;  34786 MW;  A8994CBDF25A3C84 CRC64;
     MAAFAVDPQA PTLGSEPMML GSPTSPKTGA NAQFLPGFLM GDLPAPVTPQ PRSISGPSVG
     VMEMRSPLLA GGSPPQPVVP AHKDKSGAPP VRSIYDDISS PGLGSTPLTS RRQANISLLQ
     SPLVGATTPV PGQSMFSPAN IGQPRKTTLS PAQLDPFYTQ GDSLTSEDHL DDTWVTVFGF
     PQASASYILL QFAQYGNILK HVMSNTGNWM HIRYQSKLQA RKALSKDGRI FGESIMIGVK
     PCIDKNVMEN SDRGVLSSPS LAFTTPIRTL GTPTQSGSTP RVSTMRPLAT AYKASTSDYQ
     VISDRQTPKK DESLVSRAME YMFGW
//
ID   CYS1_MOUSE              Reviewed;         145 AA.
AC   Q8R4T1; B7ZP27; Q8R4T0;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Cystin-1;
DE   AltName: Full=Cilia-associated protein;
GN   Name=Cys1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR
RP   LOCATION, DISEASE, AND TISSUE SPECIFICITY.
RC   STRAIN=129/SvJ, and C57BL/6J;
RX   MEDLINE=21843384; PubMed=11854326;
RA   Hou X., Mrug M., Yoder B.K., Lefkowitz E.J., Kremmidiotis G.,
RA   D'Eustachio P., Beier D.R., Guay-Woodford L.M.;
RT   "Cystin, a novel cilia-associated protein, is disrupted in the cpk
RT   mouse model of polycystic kidney disease.";
RL   J. Clin. Invest. 109:533-540(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium. Cytoplasm,
CC       cytoskeleton, cilium axoneme. Note=Expression is enriched in the
CC       ciliary axoneme.
CC   -!- TISSUE SPECIFICITY: Expressed primarily in the kidney and liver.
CC       Expressed at lower levels in the lung, brain and heart.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the fetal kidney.
CC   -!- DISEASE: Note=Defects in Cys1 are a cause of polycystic kidney
CC       disease.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AF390547; AAM08225.1; -; Genomic_DNA.
DR   EMBL; AF390548; AAM08707.1; -; mRNA.
DR   EMBL; BC139298; AAI39299.1; -; mRNA.
DR   EMBL; BC139302; AAI39303.1; -; mRNA.
DR   EMBL; BC145598; AAI45599.1; -; mRNA.
DR   EMBL; BC171971; AAI71971.1; -; mRNA.
DR   IPI; IPI00153922; -.
DR   RefSeq; NP_001004455.2; NM_001004455.2.
DR   RefSeq; NP_001155279.1; NM_001161807.1.
DR   RefSeq; NP_619627.3; NM_138686.3.
DR   UniGene; Mm.52265; -.
DR   STRING; Q8R4T1; -.
DR   PRIDE; Q8R4T1; -.
DR   Ensembl; ENSMUST00000074163; ENSMUSP00000073796; ENSMUSG00000062563.
DR   GeneID; 12879; -.
DR   KEGG; mmu:12879; -.
DR   UCSC; uc007nep.1; mouse.
DR   CTD; 12879; -.
DR   MGI; MGI:2177632; Cys1.
DR   eggNOG; maNOG21334; -.
DR   GeneTree; ENSGT00390000016845; -.
DR   InParanoid; Q8R4T1; -.
DR   OrthoDB; EOG45QHFZ; -.
DR   NextBio; 282480; -.
DR   ArrayExpress; Q8R4T1; -.
DR   Bgee; Q8R4T1; -.
DR   CleanEx; MM_CYS1; -.
DR   Genevestigator; Q8R4T1; -.
DR   GermOnline; ENSMUSG00000062563; Mus musculus.
DR   GO; GO:0035085; C:cilium axoneme; IDA:MGI.
DR   GO; GO:0005932; C:microtubule basal body; IDA:MGI.
PE   2: Evidence at transcript level;
KW   Cell projection; Cilium; Cytoplasm; Cytoskeleton.
FT   CHAIN         1    145       Cystin-1.
FT                                /FTId=PRO_0000261178.
FT   COMPBIAS     13     16       Poly-Arg.
FT   CONFLICT     39     39       P -> R (in Ref. 1; AAM08707).
SQ   SEQUENCE   145 AA;  15506 MW;  056B4925201707DF CRC64;
     MGSGSSRSGR IPRRRRSPDR RQTGPGETAS EGGTADQAPT AAGQEESGRD PRPATPSGGR
     EETLRLLDQL LAESEAWGPQ ELTPRGPARL APAVSPEKKV KGNPEDSCAS EAPGNSPKRP
     EGQSAISYDY SEEELMASIE REYCR
//
ID   LUZP1_MOUSE             Reviewed;        1068 AA.
AC   Q8R4U7; A3KG96; Q3UV18; Q7TS71; Q8BQW1; Q99NG3; Q9CSL6;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Leucine zipper protein 1;
DE   AltName: Full=Leucine zipper motif-containing protein;
GN   Name=Luzp1; Synonyms=Luzp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=129/SvJ;
RX   MEDLINE=96411647; PubMed=8812416; DOI=10.1006/geno.1996.0425;
RA   Sun D.-S., Chang A.C., Jenkins N.A., Gilbert D.J., Copeland N.G.,
RA   Chang N.-C.A.;
RT   "Identification, molecular characterization, and chromosomal
RT   localization of the cDNA encoding a novel leucine zipper motif-
RT   containing protein.";
RL   Genomics 36:54-62(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ; TISSUE=Peritoneal exudate;
RX   PubMed=11702014; DOI=10.1159/000046172;
RA   Lee M.W.-Y., Chang A.C., Sun D.-S., Hsu C.-Y., Chang N.-C.A.;
RT   "Restricted expression of LUZP in neural lineage cells: a study in
RT   embryonic stem cells.";
RL   J. Biomed. Sci. 8:504-511(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-318 AND 661-1068.
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, Embryo, and Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 522-1068.
RC   TISSUE=Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261 AND SER-660, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261 AND SER-660, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-660, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-660, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Also detected in soma and
CC       dendrites of neurons (By similarity).
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in the brain (at
CC       protein level).
CC   -----------------------------------------------------------------------
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DR   EMBL; L49344; AAA98795.1; -; mRNA.
DR   EMBL; AF362727; AAM00269.1; -; Genomic_DNA.
DR   EMBL; AL671173; CAM46203.1; -; Genomic_DNA.
DR   EMBL; AK012514; BAB28289.1; -; mRNA.
DR   EMBL; AK046323; BAC32681.2; ALT_SEQ; mRNA.
DR   EMBL; AK137669; BAE23455.1; -; mRNA.
DR   EMBL; BC053451; AAH53451.1; -; mRNA.
DR   IPI; IPI00322204; -.
DR   RefSeq; NP_077772.2; NM_024452.2.
DR   UniGene; Mm.480631; -.
DR   ProteinModelPortal; Q8R4U7; -.
DR   SMR; Q8R4U7; 312-345.
DR   PhosphoSite; Q8R4U7; -.
DR   PRIDE; Q8R4U7; -.
DR   Ensembl; ENSMUST00000001116; ENSMUSP00000001116; ENSMUSG00000001089.
DR   Ensembl; ENSMUST00000105849; ENSMUSP00000101475; ENSMUSG00000001089.
DR   GeneID; 269593; -.
DR   KEGG; mmu:269593; -.
DR   NMPDR; fig|10090.3.peg.10625; -.
DR   UCSC; uc008vie.1; mouse.
DR   CTD; 269593; -.
DR   MGI; MGI:107629; Luzp1.
DR   GeneTree; ENSGT00550000074495; -.
DR   HOVERGEN; HBG081939; -.
DR   InParanoid; Q8R4U7; -.
DR   OMA; SSITIYP; -.
DR   OrthoDB; EOG4XPQF7; -.
DR   PhylomeDB; Q8R4U7; -.
DR   NextBio; 392911; -.
DR   ArrayExpress; Q8R4U7; -.
DR   Bgee; Q8R4U7; -.
DR   CleanEx; MM_LUZP1; -.
DR   Genevestigator; Q8R4U7; -.
DR   GermOnline; ENSMUSG00000001089; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Nucleus; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1068       Leucine zipper protein 1.
FT                                /FTId=PRO_0000234551.
FT   COILED       11    354       Potential.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     261    261       Phosphoserine.
FT   MOD_RES     339    339       Phosphoserine (By similarity).
FT   MOD_RES     395    395       Phosphoserine (By similarity).
FT   MOD_RES     571    571       Phosphoserine (By similarity).
FT   MOD_RES     575    575       Phosphoserine (By similarity).
FT   MOD_RES     660    660       Phosphoserine.
FT   MOD_RES     678    678       Phosphothreonine (By similarity).
FT   MOD_RES     680    680       Phosphothreonine (By similarity).
FT   MOD_RES     691    691       Phosphoserine (By similarity).
FT   MOD_RES     746    746       Phosphoserine (By similarity).
FT   MOD_RES     906    906       Phosphoserine (By similarity).
FT   CONFLICT    371    371       R -> S (in Ref. 2; AAM00269).
FT   CONFLICT    499    499       S -> N (in Ref. 1; AAA98795).
FT   CONFLICT    594    594       N -> D (in Ref. 1; AAA98795).
FT   CONFLICT    906    906       S -> SASSEV (in Ref. 1; AAA98795 and 4;
FT                                AAH53451).
FT   CONFLICT    925    930       Missing (in Ref. 1; AAA98795 and 4;
FT                                AAH53451).
FT   CONFLICT    935    935       G -> R (in Ref. 1; AAA98795, 2; AAM00269
FT                                and 4; AAH53451).
FT   CONFLICT    950    951       PC -> SP (in Ref. 1; AAA98795 and 4;
FT                                AAH53451).
FT   CONFLICT    956    956       E -> R (in Ref. 2; AAM00269).
FT   CONFLICT    958    958       E -> R (in Ref. 2; AAM00269).
FT   CONFLICT    963    963       Q -> H (in Ref. 1; AAA98795, 2; AAM00269
FT                                and 4; AAH53451).
FT   CONFLICT    971    971       R -> K (in Ref. 1; AAA98795 and 4;
FT                                AAH53451).
FT   CONFLICT    974    974       N -> S (in Ref. 1; AAA98795 and 4;
FT                                AAH53451).
FT   CONFLICT    981    981       L -> R (in Ref. 1; AAA98795 and 4;
FT                                AAH53451).
FT   CONFLICT    983    983       P -> S (in Ref. 1; AAA98795 and 4;
FT                                AAH53451).
FT   CONFLICT   1011   1011       C -> W (in Ref. 1; AAA98795 and 4;
FT                                AAH53451).
SQ   SEQUENCE   1068 AA;  119311 MW;  26D88114F44B788C CRC64;
     MAELTNYKDA ASNRHLRFKL QSLSRRLDEL EEATKNLQRA EDELLDLQDK VIQAEGSDSS
     TLAEIEVLRQ RVLKIEGKDE EIKRAEDLCH TMKEKLEEEE NLTRELKSEI ERLQKRMVDL
     EKLEEALSRS KNECSQLCLS LNEERNLTKK ISSELEMLRV KVKELESSED RLDKTEQSLV
     SELEKLKSLT LSFVNERKYL NEKEKENEKI IKELTQKLEQ NKKMNRDHMR NASTFLERND
     LRIEDGISST LSSKESKRKG SLDYLKQVEN ETRDKSENEK NRNQEDNKVK DLNQEIEKLK
     TQIKHFESLE EELKKMRAKN NDLQDNYLTE LNRNRSLASQ LEEIKLQVRK QKELGNGDIE
     GEDAFLLGRG RHERTKLKGH GSEASVSKHT SRELSPQHKR ERLRNREFAL SNEHYSLSSK
     QASSPVFTNK RAAKASNMGM GTDSGTQETK RTEDRFAPGS SHSEGKRGRE QPSVLSRYPP
     AAQEHTKVWK GAPKPGTESG LKGKVEKTTR TFSDSTHVSV PNDIVGKGDK TSDLSSEAHC
     GKRGQVPGHA SQGTQAVESS CSKAIGALSS SQKASSEGLS KGKKTANGLA ADANFSNSKA
     PILSKYPYSS RSQENILQGF SLPNKEGVDQ PVAVVMEDSS QHEALRCRVI KSSGREKPDS
     DDDLDIESFV TAKLVNTTIT PEPEPKPQPN SREKVKSRGG TRTALFENDK NAAIENDSVK
     PTRPSSNAIE FPDANCAGVK NQRPFSPREA LRSRAIIKPV IIDKDVKKIM GGSGTEVVLE
     KQKSTSKSVT SKVTSSITIY PSDSSGPRAV PSEAPRERHT STSNIQVGPP ELTAISNHVS
     SPLELSIHKH DITLQLTEAE RVGDGSPKNR AEMVVSRSSI LIKPSESVEK NSHVPPAETI
     RWKSHSASSD SRHITVRNAW KSKRDLKCSE DPPTGIGRNM EATNAYTQRP CTDFLELEQP
     RSQPSEQGAR RVGNSGDAPE LSPRRTQSSL TASEVLTRRD RMGGAITAAS CNHSSSMEEG
     EDSTFVTSRR IHNPLEHSEL PGKQGLPEPE PVWTEERLHP AKPYAEED
//
ID   DUS15_MOUSE             Reviewed;         235 AA.
AC   Q8R4V2; A2APC1; Q14AH2;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 3.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Dual specificity protein phosphatase 15;
DE            EC=3.1.3.16;
DE            EC=3.1.3.48;
DE   AltName: Full=Dual specificity protein phosphatase T-DSP10;
GN   Name=Dusp15;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX   MEDLINE=21326039; PubMed=11432789;
RA   Aoki N., Aoyama K., Nagata M., Matsuda T.;
RT   "A growing family of dual specificity phosphatases with low molecular
RT   masses.";
RL   J. Biochem. 130:133-140(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-125 (ISOFORM 1).
RX   MEDLINE=21671825; PubMed=11812828; DOI=10.1093/nar/29.24.4983;
RA   Mu X., Zhao S., Pershad R., Hsieh T.-F., Scarpa A., Wang S.W.,
RA   White R.A., Beremand P.D., Thomas T.L., Gan L., Klein W.H.;
RT   "Gene expression in the developing mouse retina by EST sequencing and
RT   microarray analysis.";
RL   Nucleic Acids Res. 29:4983-4993(2001).
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R4V2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R4V2-2; Sequence=VSP_007294, VSP_007295;
CC         Note=Inactive. Lacks the active site;
CC   -!- TISSUE SPECIFICITY: Isoform 2 is highly expressed in testis.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class dual specificity subfamily.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BU924460; Type=Frameshift; Positions=120;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF357887; AAM00226.1; -; mRNA.
DR   EMBL; AL833801; CAM23680.1; -; Genomic_DNA.
DR   EMBL; BC116841; AAI16842.1; -; mRNA.
DR   EMBL; BC116843; AAI16844.1; -; mRNA.
DR   EMBL; BU924460; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00153936; -.
DR   IPI; IPI00269461; -.
DR   RefSeq; NP_001152848.1; NM_001159376.1.
DR   RefSeq; NP_665687.1; NM_145744.2.
DR   UniGene; Mm.330671; -.
DR   ProteinModelPortal; Q8R4V2; -.
DR   SMR; Q8R4V2; 1-156.
DR   STRING; Q8R4V2; -.
DR   PRIDE; Q8R4V2; -.
DR   Ensembl; ENSMUST00000037715; ENSMUSP00000045815; ENSMUSG00000042662.
DR   Ensembl; ENSMUST00000109811; ENSMUSP00000105436; ENSMUSG00000042662.
DR   GeneID; 252864; -.
DR   KEGG; mmu:252864; -.
DR   UCSC; uc008ngu.1; mouse.
DR   CTD; 252864; -.
DR   MGI; MGI:1934928; Dusp15.
DR   eggNOG; roNOG17064; -.
DR   GeneTree; ENSGT00590000082869; -.
DR   HOGENOM; HBG717377; -.
DR   HOVERGEN; HBG054344; -.
DR   InParanoid; Q8R4V2; -.
DR   OMA; RCLSRKG; -.
DR   OrthoDB; EOG4RFKT3; -.
DR   BRENDA; 3.1.3.16; 244.
DR   BRENDA; 3.1.3.48; 244.
DR   ArrayExpress; Q8R4V2; -.
DR   Bgee; Q8R4V2; -.
DR   CleanEx; MM_DUSP15; -.
DR   Genevestigator; Q8R4V2; -.
DR   GermOnline; ENSMUSG00000042662; Mus musculus.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   InterPro; IPR020417; Dual-sp_phosphatase.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR020422; Dual-sp_phosphatase_subgr_cat.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   Pfam; PF00782; DSPc; 1.
DR   PRINTS; PR01908; ADSPHPHTASE.
DR   SMART; SM00195; DSPc; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Hydrolase; Protein phosphatase.
FT   CHAIN         1    235       Dual specificity protein phosphatase 15.
FT                                /FTId=PRO_0000094825.
FT   DOMAIN       65    135       Tyrosine-protein phosphatase.
FT   ACT_SITE     88     88       Phosphocysteine intermediate (By
FT                                similarity).
FT   VAR_SEQ      88    105       CFAGISRSTTIVIAYVMT -> WPLKHECRARSLSLLQCS
FT                                (in isoform 2).
FT                                /FTId=VSP_007294.
FT   VAR_SEQ     106    235       Missing (in isoform 2).
FT                                /FTId=VSP_007295.
SQ   SEQUENCE   235 AA;  26186 MW;  09A3EB05A0A7F891 CRC64;
     MGNGMTKVLP GLYLGNFIDA KDPDQLGRNK ITHIISIHES PQPLLQDITY LRISVSDTPE
     VPIKKHFKEC VHFIHSCRLN GGNCLVHCFA GISRSTTIVI AYVMTVTGLG WQEVLEAIKA
     SRPIANPNPG FRQQLEEFGW ANSQKLRRQL EERFGEIPFR DEEDLRALLP LCRRCRQGSA
     TSAASATTAS SAAEGTLQRL VPRSPRDSHQ PLPLLARVKQ TFFCLPRCLS RKGGK
//
ID   STAB1_MOUSE             Reviewed;        2571 AA.
AC   Q8R4Y4; Q8K0K6; Q8VC09;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Stabilin-1;
DE   AltName: Full=Fasciclin, EGF-like, laminin-type EGF-like and link domain-containing scavenger receptor 1;
DE            Short=FEEL-1;
DE   Flags: Precursor;
GN   Name=Stab1; Synonyms=Feel1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=21818465; PubMed=11829752; DOI=10.1042/0264-6021:3620155;
RA   Politz O., Gratchev A., McCourt P.A.G., Schledzewski K., Guillot P.,
RA   Johansson S., Svineng G., Franke P., Kannicht C., Kzhyshkowska J.,
RA   Longati P., Velten F.W., Johansson S., Goerdt S.;
RT   "Stabilin-1 and -2 constitute a novel family of fasciclin-like
RT   hyaluronan receptor homologues.";
RL   Biochem. J. 362:155-164(2002).
RN   [2]
RP   PROTEIN SEQUENCE OF 560-570, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1334-2571 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2230-2571 (ISOFORM 2).
RC   TISSUE=Colon, and Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Acts as a scavenger receptor for acetylated low density
CC       lipoprotein. Binds to both Gram-positive and Gram-negative
CC       bacteria and may play a role in defense against bacterial
CC       infection. When inhibited in endothelial tube formation assays,
CC       there is a marked decrease in cell-cell interactions, suggesting a
CC       role in angiogenesis. Involved in the delivery of newly
CC       synthesized CHID1/SI-CLP from the biosynthetic compartment to the
CC       endosomal/lysosomal system (By similarity).
CC   -!- SUBUNIT: Interacts with CHID1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R4Y4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R4Y4-2; Sequence=VSP_050766, VSP_050767;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 16 EGF-like domains.
CC   -!- SIMILARITY: Contains 7 FAS1 domains.
CC   -!- SIMILARITY: Contains 2 laminin EGF-like domains.
CC   -!- SIMILARITY: Contains 1 Link domain.
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DR   EMBL; AF290914; AAL91671.2; -; mRNA.
DR   EMBL; BC031166; AAH31166.1; -; mRNA.
DR   EMBL; BC022136; AAH22136.1; -; mRNA.
DR   IPI; IPI00153959; -.
DR   IPI; IPI00420150; -.
DR   UniGene; Mm.220821; -.
DR   ProteinModelPortal; Q8R4Y4; -.
DR   SMR; Q8R4Y4; 68-361, 739-764, 819-983, 1340-1371, 1399-1577, 1955-2200, 2208-2303, 2315-2463.
DR   STRING; Q8R4Y4; -.
DR   PhosphoSite; Q8R4Y4; -.
DR   PRIDE; Q8R4Y4; -.
DR   Ensembl; ENSMUST00000036618; ENSMUSP00000046199; ENSMUSG00000042286.
DR   UCSC; uc007swv.1; mouse.
DR   MGI; MGI:2178742; Stab1.
DR   GeneTree; ENSGT00550000074173; -.
DR   HOGENOM; HBG717312; -.
DR   HOVERGEN; HBG079218; -.
DR   InParanoid; Q8R4Y4; -.
DR   OrthoDB; EOG4VQ9NC; -.
DR   ArrayExpress; Q8R4Y4; -.
DR   Bgee; Q8R4Y4; -.
DR   CleanEx; MM_STAB1; -.
DR   Genevestigator; Q8R4Y4; -.
DR   GermOnline; ENSMUSG00000042286; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; ISS:UniProtKB.
DR   GO; GO:0051635; F:bacterial cell surface binding; ISS:UniProtKB.
DR   GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
DR   GO; GO:0005041; F:low-density lipoprotein receptor activity; ISS:UniProtKB.
DR   GO; GO:0005044; F:scavenger receptor activity; ISS:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0007267; P:cell-cell signaling; ISS:UniProtKB.
DR   GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
DR   InterPro; IPR016186; C-type_lectin-like.
DR   InterPro; IPR016187; C-type_lectin_fold.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR000782; FAS1_domain.
DR   InterPro; IPR000538; Link.
DR   Gene3D; G3DSA:2.30.180.10; BIgH3_FAS1; 7.
DR   Gene3D; G3DSA:3.10.100.10; C-type_lectin-like; 1.
DR   Pfam; PF02469; Fasciclin; 4.
DR   Pfam; PF00193; Xlink; 1.
DR   SMART; SM00181; EGF; 20.
DR   SMART; SM00554; FAS1; 6.
DR   SMART; SM00445; LINK; 1.
DR   SUPFAM; SSF82153; BIgH3_FAS1; 7.
DR   SUPFAM; SSF56436; C-type_lectin_fold; 1.
DR   PROSITE; PS00022; EGF_1; 7.
DR   PROSITE; PS01186; EGF_2; 15.
DR   PROSITE; PS50026; EGF_3; 20.
DR   PROSITE; PS01248; EGF_LAM_1; 2.
DR   PROSITE; PS50027; EGF_LAM_2; FALSE_NEG.
DR   PROSITE; PS50213; FAS1; 7.
DR   PROSITE; PS01241; LINK_1; 1.
DR   PROSITE; PS50963; LINK_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Inflammatory response;
KW   Laminin EGF-like domain; Membrane; Phosphoprotein; Receptor; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     25       Potential.
FT   CHAIN        26   2571       Stabilin-1.
FT                                /FTId=PRO_0000007711.
FT   TOPO_DOM     26   2475       Extracellular (Potential).
FT   TRANSMEM   2476   2496       Helical; (Potential).
FT   TOPO_DOM   2497   2571       Cytoplasmic (Potential).
FT   DOMAIN      111    149       EGF-like 1.
FT   DOMAIN      157    194       EGF-like 2.
FT   DOMAIN      196    232       EGF-like 3.
FT   DOMAIN      233    272       EGF-like 4.
FT   DOMAIN      357    495       FAS1 1.
FT   DOMAIN      507    642       FAS1 2.
FT   DOMAIN      729    769       EGF-like 5.
FT   DOMAIN      819    859       EGF-like 6.
FT   DOMAIN      862    904       EGF-like 7.
FT   DOMAIN      905    947       EGF-like 8.
FT   DOMAIN      948    987       EGF-like 9.
FT   DOMAIN      989   1119       FAS1 3.
FT   DOMAIN     1129   1254       FAS1 4.
FT   DOMAIN     1328   1393       Laminin EGF-like 1.
FT   DOMAIN     1417   1455       EGF-like 10.
FT   DOMAIN     1456   1497       EGF-like 11.
FT   DOMAIN     1498   1540       EGF-like 12.
FT   DOMAIN     1541   1583       EGF-like 13.
FT   DOMAIN     1583   1709       FAS1 5.
FT   DOMAIN     1725   1865       FAS1 6.
FT   DOMAIN     1966   2031       Laminin EGF-like 2.
FT   DOMAIN     2056   2090       EGF-like 14.
FT   DOMAIN     2091   2131       EGF-like 15.
FT   DOMAIN     2132   2174       EGF-like 16.
FT   DOMAIN     2208   2301       Link.
FT   DOMAIN     2322   2459       FAS1 7.
FT   MOD_RES    1258   1258       Phosphoserine (By similarity).
FT   MOD_RES    1259   1259       Phosphoserine (By similarity).
FT   CARBOHYD    134    134       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    142    142       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    287    287       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    313    313       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    416    416       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    607    607       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    674    674       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    713    713       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    746    746       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    817    817       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1011   1011       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1088   1088       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1097   1097       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1171   1171       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1179   1179       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1223   1223       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1275   1275       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1398   1398       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1450   1450       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1472   1472       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1627   1627       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1728   1728       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2107   2107       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2261   2261       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2290   2290       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2334   2334       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2347   2347       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2379   2379       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2393   2393       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2400   2400       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2424   2424       N-linked (GlcNAc...) (Potential).
FT   DISULFID    113    127       By similarity.
FT   DISULFID    121    137       By similarity.
FT   DISULFID    139    148       By similarity.
FT   DISULFID    161    172       By similarity.
FT   DISULFID    165    182       By similarity.
FT   DISULFID    184    193       By similarity.
FT   DISULFID    200    211       By similarity.
FT   DISULFID    205    218       By similarity.
FT   DISULFID    220    231       By similarity.
FT   DISULFID    237    248       By similarity.
FT   DISULFID    242    258       By similarity.
FT   DISULFID    260    271       By similarity.
FT   DISULFID    733    747       By similarity.
FT   DISULFID    741    757       By similarity.
FT   DISULFID    759    768       By similarity.
FT   DISULFID    823    838       By similarity.
FT   DISULFID    832    847       By similarity.
FT   DISULFID    866    880       By similarity.
FT   DISULFID    874    890       By similarity.
FT   DISULFID    892    903       By similarity.
FT   DISULFID    909    923       By similarity.
FT   DISULFID    917    933       By similarity.
FT   DISULFID    935    946       By similarity.
FT   DISULFID    952    965       By similarity.
FT   DISULFID    959    975       By similarity.
FT   DISULFID   1333   1347       By similarity.
FT   DISULFID   1341   1357       By similarity.
FT   DISULFID   1359   1368       By similarity.
FT   DISULFID   1380   1391       By similarity.
FT   DISULFID   1384   1401       By similarity.
FT   DISULFID   1403   1412       By similarity.
FT   DISULFID   1421   1431       By similarity.
FT   DISULFID   1425   1441       By similarity.
FT   DISULFID   1443   1454       By similarity.
FT   DISULFID   1460   1473       By similarity.
FT   DISULFID   1467   1483       By similarity.
FT   DISULFID   1485   1496       By similarity.
FT   DISULFID   1502   1515       By similarity.
FT   DISULFID   1509   1525       By similarity.
FT   DISULFID   1527   1539       By similarity.
FT   DISULFID   1545   1558       By similarity.
FT   DISULFID   1552   1568       By similarity.
FT   DISULFID   1570   1582       By similarity.
FT   DISULFID   1971   1985       By similarity.
FT   DISULFID   1979   1995       By similarity.
FT   DISULFID   1997   2006       By similarity.
FT   DISULFID   2018   2029       By similarity.
FT   DISULFID   2023   2039       By similarity.
FT   DISULFID   2041   2050       By similarity.
FT   DISULFID   2060   2070       By similarity.
FT   DISULFID   2064   2076       By similarity.
FT   DISULFID   2078   2089       By similarity.
FT   DISULFID   2095   2108       By similarity.
FT   DISULFID   2102   2117       By similarity.
FT   DISULFID   2119   2130       By similarity.
FT   DISULFID   2136   2150       By similarity.
FT   DISULFID   2144   2160       By similarity.
FT   DISULFID   2162   2173       By similarity.
FT   DISULFID   2230   2299       By similarity.
FT   DISULFID   2254   2275       By similarity.
FT   VAR_SEQ    2381   2403       TLSGPDLELHASNATFLSINASR -> VTAGPWAVCSSAVG
FT                                PTQQVLLCS (in isoform 2).
FT                                /FTId=VSP_050766.
FT   VAR_SEQ    2405   2571       Missing (in isoform 2).
FT                                /FTId=VSP_050767.
SQ   SEQUENCE   2571 AA;  276257 MW;  77D00B943DC47718 CRC64;
     MAEPRTLLLL CVLVLCLSDS SFIRGQTVRS KRCDIHTKFV THTPCTACAA IRRQLCPWGW
     SRNFPEKILL DCRYELQLRG AAISLSGCSQ ECWKDVVQKA CCPGYWGSQC FECPGGPATP
     CSGHGTCLDG IEGNGTCVCQ GNFSGSVCQE CRDPNRFGPD CQSVCNCVHG VCSHGPRGDG
     SCRCFAGYTG PHCDQELPVC QSLKCPQNSQ CSAEAPTCKC LPGYTQQDNV CLAPDPCQPS
     ACSPLARCSV TPQGQAQCQC PENYHGDGKV CLPRDPCLTN FGGCPSNSTF CLYRGPGKAT
     CMCRPGMTSI NNNASEGCHV SCKPHSCDRS ATCQVTPDRK TSCVCKNDEV GDGHACYGHL
     LHEVRRANQN GLVFLRLRAA IAMLEQGCQE ILTTSGPFTV LVPSMFSVSS VSSNMNATLA
     QQLCRQHVIA GEHMLENAGP PSTRRWWTLA GQEVTITFKN MRYAYKYEDQ PQQFSIHKAN
     YIAANGVFHT VTALRWQLPP PLPGDSKKTV GQILASTEVF TRFETILENC GLPSILDGPG
     PFTVFAPSNE AVDSLRDGRL IYLFTAGLSK LQELVRYHIY NHGQLTVEKL ISKGRVLTMA
     NQVLTVNISE GGRILLGPGG IPVRRVDVPA ANGVIHMLEG ILLPPTILPI LPKHCDEEQH
     QTVLGSCVDC QALNTSVCPP NSVKMDIFPK ECVYIHDPNG LNVLKKGCAD YCNQTITKRG
     CCKGFFGPDC TQCPGGFSNP CYGKGNCSDG VRGNGACLCF PDYKGIACHI CSDPKKHGEQ
     CQEDCGCVHG LCDNRPGSGG VCQQGTCAPG FQGRFCNESM GNCGSTGLAQ PCHSDAHCVI
     QEGVARCVCH DGFEGNGFSC KRSNPCSRPD RGGCSENAEC VPGDLGTHHC ICHKGWSGDG
     RICVAIDECG LDTRGGCHAD ALCSYVGPGQ SRCTCKLGFA GNGYECSPID PCRVGNGGCH
     GLATCKAVGG GQRVCTCPPH FGGDGFSCYG DIIQELEANA HFSAFSQWFK NSSITLPADS
     RVTALVPSES AIRRLSLEDQ AFWLQPKMLP ELARAHFLQG AFSEEELARL NGQQVATLSA
     TTRWQIHNIS GKVWVQNATV DVPDLLATNG ILHIVSQVLL PPRGDMQTGP GLLQQLDSVP
     AFRLFGEQLK HHKLVAQIEA AKAYTIFVPT NHSLETQGNN SVLGIDTVRH HVILGEALSV
     EVLRKGGHRN SLLGPAHWLV FYNHSGQPEV NHMPLEGPLL EAPGSSLFGL SGILAVGSSR
     CLHSHAEALR EKCINCTRKF RCTQGFQLQD TPRKSCVYRS GLSFSRGCSY TCAKKIQVPD
     CCPGFFGTLC EPCPGGLGGV CSGHGQCQDR FLGNGECRCQ EGFHGTACEM CELGRYGPTC
     SGVCDCDHGL CQEGLRGNGS CVCHAGWQGL RCDQKITDHQ CPKKCDPNAN CIQDSAGIPA
     CVCAAGYSGN GSYCSEVDPC ASGHGGCSPY ANCTKVAPGQ RTCTCQDGYT GDGELCQEIN
     SCLVHNGGCH VHAECIPTGP QQVSCSCREG YSGDGIQTCK LLDPCSQNNG GCSPYAVCKS
     TGDGQRTCSC DATHTVGDGI TCHGRVGLEL LRNKYASFFS LHLLEYKELK GDGPFTVFVP
     HADLISNMSQ DELARIRAHR QLVFRYHVVG CRKLWSQEML DQGYITTLSG HTLRVSEREG
     SIYLNDFARV VSSDLEVVNG VLHFIDHVLL PPDVLHWESG AIPIPQRNVT AAAESFGYKI
     FSRLLTVAGL LPMLQDASHR PFTMLWPTDS ALQALPPDRK NWLFHEDHRD KLAAILRGHM
     IRNIEALASD LPNLGQLRTM HGNTISFSCG LTRPGELIVG EDEAHIVQRH LTFEGGLAYG
     IDQLLEPPDL GARCDRFEPQ PLQMKTCSIC GLEPPCPRGS REQGSPETCW RHYSKFWTTP
     LHSISMRGAY WIPSSFWNRN HMSRGCHRNC VTTVWKPSCC PGHYGINCHA CPGGPRSPCS
     DHGVCLDGIR GSGQCNCHPG FAGTACELCA PGAFGPQCQA CRCTQHGRCD EGLGGSGSCF
     CDEGWTGARC EVQLELQPVC TPPCAPQAVC RLGNSCECSL GYEGDGRVCT VADLCQKGHG
     GCSKHANCSQ VGTVVTCTCL PDYEGDGWSC RARDPCLDGH RGGCSEHADC LNTGPNTRRC
     ECHVGYVGDG LQCLEELEPP VDRCLGGSSP CHTDALCTDL HFQEKQAGVF HIQATSGPYG
     LTFSEAKEAC EGQGAVLASL PQLSAAQQLG FHVCFVGWLA NGSAAHPVVT PAADCGNNRV
     GVVSLGVRKN LSELWDAYCY RVQDVACQCR AGFVGDGIST CNGKLLDVLA ATANFSTFYG
     MLLGYANATQ RGLEFMDFLE DELTYKTLFV PVNKGFVDNM TLSGPDLELH ASNATFLSIN
     ASRGTLLPAH SGLSLFISDT GPDNTSLVPL APGAVVVSHV IVWDIMAFNG IIHALASPLL
     MPPQTRAVLG SEPPPVALSL GVVVTSGTLL GLVAGALYLR ARGKPPGFSF SAFQAEDNAD
     DDFSPWQEGT SPTLVSVPNP VFGSSDIFCE PFDDSVLEED FPDTQRVLKV K
//
ID   LRC8C_MOUSE             Reviewed;         803 AA.
AC   Q8R502; Q3TEP9; Q8C296; Q8R0N7; Q8R3G5;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Leucine-rich repeat-containing protein 8C;
DE   AltName: Full=Protein AD158;
GN   Name=Lrrc8c; Synonyms=Ad158;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=15564382; DOI=10.1242/jcs.01546;
RA   Tominaga K., Johmura Y., Nishizuka M., Imagawa M.;
RT   "Fad24, a mammalian homolog of Noc3p, is a positive regulator in
RT   adipocyte differentiation.";
RL   J. Cell Sci. 117:6217-6226(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212 AND SER-215, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-198, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: May play a role in adipogenesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed at very low levels in adipose
CC       tissue.
CC   -!- SIMILARITY: Contains 13 LRR (leucine-rich) repeats.
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DR   EMBL; AB081508; BAB86302.1; -; mRNA.
DR   EMBL; AK169492; BAE41199.1; -; mRNA.
DR   EMBL; AK089024; BAC40706.1; -; mRNA.
DR   EMBL; AK142337; BAE25036.1; -; mRNA.
DR   EMBL; BC025473; AAH25473.1; -; mRNA.
DR   EMBL; BC026572; AAH26572.1; -; mRNA.
DR   IPI; IPI00404595; -.
DR   RefSeq; NP_598658.1; NM_133897.2.
DR   UniGene; Mm.319847; -.
DR   UniGene; Mm.392291; -.
DR   ProteinModelPortal; Q8R502; -.
DR   SMR; Q8R502; 422-795.
DR   STRING; Q8R502; -.
DR   PhosphoSite; Q8R502; -.
DR   PRIDE; Q8R502; -.
DR   Ensembl; ENSMUST00000067924; ENSMUSP00000066015; ENSMUSG00000054720.
DR   GeneID; 100604; -.
DR   KEGG; mmu:100604; -.
DR   UCSC; uc008ylf.1; mouse.
DR   CTD; 100604; -.
DR   MGI; MGI:2140839; Lrrc8c.
DR   eggNOG; roNOG11231; -.
DR   HOGENOM; HBG445357; -.
DR   HOVERGEN; HBG052360; -.
DR   InParanoid; Q8R502; -.
DR   OMA; CYERALH; -.
DR   OrthoDB; EOG4N8R44; -.
DR   PhylomeDB; Q8R502; -.
DR   NextBio; 354540; -.
DR   ArrayExpress; Q8R502; -.
DR   Bgee; Q8R502; -.
DR   CleanEx; MM_LRRC8C; -.
DR   Genevestigator; Q8R502; -.
DR   GermOnline; ENSMUSG00000054720; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR021040; LRR_protein-8_N.
DR   Pfam; PF12534; DUF3733; 2.
DR   Pfam; PF00560; LRR_1; 2.
DR   SMART; SM00369; LRR_TYP; 1.
DR   PROSITE; PS51450; LRR; 9.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Leucine-rich repeat; Membrane; Phosphoprotein;
KW   Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN         1    803       Leucine-rich repeat-containing protein
FT                                8C.
FT                                /FTId=PRO_0000076248.
FT   TRANSMEM     23     43       Helical; (Potential).
FT   TRANSMEM    126    146       Helical; (Potential).
FT   TRANSMEM    267    287       Helical; (Potential).
FT   TRANSMEM    321    341       Helical; (Potential).
FT   REPEAT      420    443       LRR 1.
FT   REPEAT      446    465       LRR 2.
FT   REPEAT      466    488       LRR 3.
FT   REPEAT      490    513       LRR 4.
FT   REPEAT      541    563       LRR 5.
FT   REPEAT      588    611       LRR 6.
FT   REPEAT      613    635       LRR 7.
FT   REPEAT      637    658       LRR 8.
FT   REPEAT      659    682       LRR 9.
FT   REPEAT      684    704       LRR 10.
FT   REPEAT      705    728       LRR 11.
FT   REPEAT      730    750       LRR 12.
FT   REPEAT      751    774       LRR 13.
FT   MOD_RES     198    198       Phosphothreonine.
FT   MOD_RES     212    212       Phosphoserine.
FT   MOD_RES     215    215       Phosphoserine.
FT   MOD_RES     687    687       Phosphotyrosine (By similarity).
FT   CONFLICT    178    178       V -> A (in Ref. 2; BAC40706).
FT   CONFLICT    653    653       P -> A (in Ref. 2; BAE41199).
FT   CONFLICT    781    781       G -> R (in Ref. 3; AAH25473/AAH26572).
SQ   SEQUENCE   803 AA;  92372 MW;  E99DAC364FF980B5 CRC64;
     MIPVTEFRQF SEQQPAFRVL KPWWDVFTDY LSVAMLMIGV FGCTLQVMQD KIICLPKRVQ
     PAQNHSSVPN VSQAVISTTP LPPPKPSPTN PATVEMKGLK TDLDLQQYSF INQMCYERAL
     HWYAKYFPYL VLIHTLVFML CSNFWFKFPG SSSKIEHFIS ILGKCFDSPW TTRALSEVSG
     EDSEEKDNRK NNMNRSGTIQ SGPEGNLVRS QSLKSIPEKF VVDKSAAGAL DKKEGEQAKA
     LFEKVKKFRL HVEEGDILYA MYVRQTVLKV IKFLIIIAYN SALVSKVQFT VDCNVDIQDM
     TGYKNFSCNH TMAHLFSKLS FCYLCFVSIY GLTCLYTLYW LFYRSLREYS FEYVRQETGI
     DDIPDVKNDF AFMLHMIDQY DPLYSKRFAV FLSEVSENKL KQLNLNNEWT PDKLRQKLQT
     NAHNRLELPL IMLSGLPDTV FEITELQSLK LEIIKNVMIP ATIAQLDNLQ ELCLHQCSVK
     IHSAALSFLK ENLKVLSVKF DDMRELPPWM YGLRNLEELY LVGSLSHDIS KNVTLESLRD
     LKSLKILSIK SNVSKIPQAV VDVSSHLQKM CVHNDGTKLV MLNNLKKMTN LTELELVHCD
     LERIPHAVFS LLSLQELDLK ENNLKSIEEI VSFQHLRKLT VLKLWYNSIA YIPEHIKKLT
     SLERLFFSHN KVEVLPSHLF LCNKIRYLDL SYNDIRFIPP EIGVLQSLQY FSITCNKVES
     LPDELYFCKK LKTLKIGKNS LSVLSPKIGN LLFLSYLDIK GNHFEVLPPE LGDCRALKRA
     GLVVEDALFE TLPSDVREQM KAD
//
ID   Q8R504_MOUSE            Unreviewed;       171 AA.
AC   Q8R504;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   08-FEB-2011, entry version 27.
DE   SubName: Full=Na+/Ca2+ exchanger NCX2 isoform;
DE   Flags: Fragment;
GN   Name=Slc8a2; Synonyms=NCX2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Balb/c; TISSUE=Brain capillary;
RX   MEDLINE=22468877; PubMed=12581871; DOI=10.1016/S0167-4889(02)00397-X;
RA   Yamaji R., Fujita K., Takahashi S., Yoneda H., Nagao K., Masuda W.,
RA   Naito M., Tsuruo T., Miyatake K., Inui H., Nakano Y.;
RT   "Hypoxia up-regulates glyceraldehyde-3-phosphate dehydrogenase in
RT   mouse brain capillary endothelial cells: involvement of Na+/Ca2+
RT   exchanger.";
RL   Biochim. Biophys. Acta 1593:269-276(2003).
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DR   EMBL; AB080745; BAB85834.1; -; mRNA.
DR   IPI; IPI00170310; -.
DR   UniGene; Mm.241147; -.
DR   STRING; Q8R504; -.
DR   Ensembl; ENSMUST00000006175; ENSMUSP00000006175; ENSMUSG00000030376.
DR   MGI; MGI:107996; Slc8a2.
DR   GeneTree; ENSGT00560000077023; -.
DR   InParanoid; Q8R504; -.
DR   ArrayExpress; Q8R504; -.
DR   Bgee; Q8R504; -.
DR   Genevestigator; Q8R504; -.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
FT   NON_TER     171    171
SQ   SEQUENCE   171 AA;  18980 MW;  8F504C70F9505455 CRC64;
     LLTLVFFPVC VVFAWMADKR LLFYKYVYKR CRTDPRSGII IGAEGDPPKS IELDGTFVGT
     EVPGELGALG TGPAEARELD ASRREVIQIL KDLKQKHPDK DLEQLMGIAK YYALLHQQKS
     RAFYRIQATR LMTGAGNVLR RHAADAARRP GATDGAPGDE DDGASRIFFE P
//
ID   MIB2_MOUSE              Reviewed;         973 AA.
AC   Q8R516; A2A9P9; Q52QU8; Q6PEF6; Q8C1N7; Q8VIB4;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 2.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=E3 ubiquitin-protein ligase MIB2;
DE            EC=6.3.2.-;
DE   AltName: Full=Dystrophin-like protein;
DE            Short=Dyslike;
DE   AltName: Full=Mind bomb homolog 2;
DE            Short=Mind bomb-2;
DE   AltName: Full=Skeletrophin;
GN   Name=Mib2; Synonyms=Skd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, FUNCTION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   UBIQUITINATION, AND MUTAGENESIS OF CYS-874 AND CYS-951.
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Thymus;
RX   PubMed=15824097; DOI=10.1074/jbc.M501631200;
RA   Koo B.-K., Yoon K.-J., Yoo K.-W., Lim H.-S., Song R., So J.-H.,
RA   Kim C.-H., Kong Y.-Y.;
RT   "Mind bomb-2 is an E3 ligase for Notch ligand.";
RL   J. Biol. Chem. 280:22335-22342(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Heart;
RA   Takeuchi T.;
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 604-750.
RC   STRAIN=C57BL/6J; TISSUE=Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [7]
RP   PROTEIN SEQUENCE OF 920-926, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination
CC       of Delta receptors, which act as ligands of Notch proteins.
CC       Positively regulates the Delta-mediated Notch signaling by
CC       ubiquitinating the intracellular domain of Delta, leading to
CC       endocytosis of Delta receptors.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with actin monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome. Note=Colocalizes with
CC       endosomal compartments.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8R516-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R516-2; Sequence=VSP_014397, VSP_014400, VSP_014401;
CC       Name=3;
CC         IsoId=Q8R516-3; Sequence=VSP_014398, VSP_014399;
CC         Note=May be produced at very low levels due to a premature stop
CC         codon in the mRNA, leading to nonsense-mediated mRNA decay. No
CC         experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain, heart, liver and
CC       kidney.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in neonate and adult, but
CC       only slightly in embryos. In E10.5 embryos, it is weakly expressed
CC       in the tail bud and limb buds. Expressed in the same pattern than
CC       MIB1 in the skin and intestine at postnatal day 1 (P1) and in the
CC       hair follicle in the skin in the adult.
CC   -!- PTM: Ubiquitinated. Possibly via autoubiquitination.
CC   -!- SIMILARITY: Contains 9 ANK repeats.
CC   -!- SIMILARITY: Contains 2 MIB/HERC2 domains.
CC   -!- SIMILARITY: Contains 2 RING-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 ZZ-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB79447.1; Type=Frameshift; Positions=151, 161;
CC       Sequence=BAB86856.1; Type=Frameshift; Positions=780, 840;
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DR   EMBL; AY974090; AAX84652.1; -; mRNA.
DR   EMBL; AB063290; BAB79447.1; ALT_FRAME; mRNA.
DR   EMBL; AB072336; BAB86856.1; ALT_FRAME; mRNA.
DR   EMBL; AL627405; CAM16749.1; -; Genomic_DNA.
DR   EMBL; CH466594; EDL15023.1; -; Genomic_DNA.
DR   EMBL; BC058086; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK008671; BAC25227.1; -; mRNA.
DR   IPI; IPI00153916; -.
DR   IPI; IPI00420836; -.
DR   IPI; IPI00467304; -.
DR   RefSeq; NP_660106.2; NM_145124.2.
DR   UniGene; Mm.235738; -.
DR   ProteinModelPortal; Q8R516; -.
DR   SMR; Q8R516; 6-78, 89-136, 144-230, 405-809, 847-893, 915-973.
DR   STRING; Q8R516; -.
DR   PhosphoSite; Q8R516; -.
DR   PRIDE; Q8R516; -.
DR   Ensembl; ENSMUST00000077624; ENSMUSP00000076814; ENSMUSG00000029060.
DR   Ensembl; ENSMUST00000116251; ENSMUSP00000111955; ENSMUSG00000029060.
DR   GeneID; 76580; -.
DR   KEGG; mmu:76580; -.
DR   UCSC; uc008wee.1; mouse.
DR   UCSC; uc008wef.1; mouse.
DR   CTD; 76580; -.
DR   MGI; MGI:2679684; Mib2.
DR   GeneTree; ENSGT00590000082925; -.
DR   HOGENOM; HBG713882; -.
DR   HOVERGEN; HBG068386; -.
DR   InParanoid; Q8R516; -.
DR   OMA; TFNPACL; -.
DR   NextBio; 345394; -.
DR   ArrayExpress; Q8R516; -.
DR   Bgee; Q8R516; -.
DR   CleanEx; MM_MIB2; -.
DR   Genevestigator; Q8R516; -.
DR   GermOnline; ENSMUSG00000029060; Mus musculus.
DR   GO; GO:0005769; C:early endosome; IDA:MGI.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR010606; Mib_Herc2.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR000433; Znf_ZZ.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 2.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00023; Ank; 3.
DR   Pfam; PF06701; MIB_HERC2; 2.
DR   Pfam; PF00569; ZZ; 1.
DR   SMART; SM00248; ANK; 8.
DR   SMART; SM00184; RING; 2.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
DR   PROSITE; PS51416; MIB_HERC2; 2.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 2.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; ANK repeat; Cytoplasm;
KW   Direct protein sequencing; Endosome; Ligase; Metal-binding;
KW   Notch signaling pathway; Phosphoprotein; Repeat; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    973       E3 ubiquitin-protein ligase MIB2.
FT                                /FTId=PRO_0000055948.
FT   DOMAIN        1     80       MIB/HERC2 1.
FT   DOMAIN      149    227       MIB/HERC2 2.
FT   REPEAT      480    509       ANK 1.
FT   REPEAT      513    542       ANK 2.
FT   REPEAT      546    575       ANK 3.
FT   REPEAT      579    611       ANK 4.
FT   REPEAT      615    644       ANK 5.
FT   REPEAT      649    679       ANK 6.
FT   REPEAT      683    712       ANK 7.
FT   REPEAT      716    744       ANK 8.
FT   REPEAT      785    814       ANK 9.
FT   ZN_FING      85    132       ZZ-type.
FT   ZN_FING     850    885       RING-type 1.
FT   ZN_FING     929    962       RING-type 2.
FT   MOD_RES     142    142       Phosphothreonine (By similarity).
FT   MOD_RES     144    144       Phosphoserine (By similarity).
FT   MOD_RES     251    251       Phosphoserine.
FT   VAR_SEQ     289    324       Missing (in isoform 2).
FT                                /FTId=VSP_014397.
FT   VAR_SEQ     289    294       FIGQMG -> VSHLFC (in isoform 3).
FT                                /FTId=VSP_014398.
FT   VAR_SEQ     295    973       Missing (in isoform 3).
FT                                /FTId=VSP_014399.
FT   VAR_SEQ     415    422       Missing (in isoform 2).
FT                                /FTId=VSP_014400.
FT   VAR_SEQ     467    474       Missing (in isoform 2).
FT                                /FTId=VSP_014401.
FT   MUTAGEN     874    874       C->S: No effect.
FT   MUTAGEN     951    951       C->S: Abolishes ubiquitin ligase
FT                                activity.
FT   CONFLICT     89     89       I -> T (in Ref. 2; BAB79447/BAB86856).
FT   CONFLICT    131    131       E -> G (in Ref. 2; BAB79447/BAB86856).
FT   CONFLICT    138    138       S -> L (in Ref. 2; BAB79447/BAB86856).
FT   CONFLICT    393    393       V -> S (in Ref. 2; BAB86856).
FT   CONFLICT    407    407       E -> D (in Ref. 2; BAB86856).
FT   CONFLICT    465    465       E -> D (in Ref. 2; BAB86856).
FT   CONFLICT    487    487       V -> L (in Ref. 2; BAB86856).
FT   CONFLICT    537    537       G -> R (in Ref. 2; BAB86856).
FT   CONFLICT    626    626       K -> R (in Ref. 2; BAB86856).
FT   CONFLICT    745    750       LQLLSR -> CSCCQG (in Ref. 6; BAC25227).
FT   CONFLICT    904    904       Q -> R (in Ref. 2; BAB86856).
SQ   SEQUENCE   973 AA;  105961 MW;  3E9406DEB30541D7 CRC64;
     MDLDPHAGVQ VGMRVVRGMD WKWGQQDGGE GGVGTVVELG RHGSPSTPDR TVVVQWDQGT
     RTNYRAGYQG AHDLLLYDNA QIGIRHPNII CDCCKKHGLR GMRWKCRVCF DYDLCTQCYM
     HNKHDLTHAF ERYETSHSRP VTLSPRQGLP RIPLRGIFQG AKVVRGPDWE WGSQDGGEGK
     TGRVVDIRGW DVETGRSVAS VTWADGTTNV YRVGHKGKVD LRCVGEAAGG FYYKEHLPKL
     GKPAELQRRV SADGQPFQRG DKVKCLLDTD VLRDMQEGHG GWNPRMAEFI GQMGTVHRIT
     DRGDVRVQFN HETRWTFHPG ALTKHNSFWV GDVVRVIGDL DTVKRLQAGH GEWTDDMAPA
     LGRVGKVVKV FGDGNLRVAV GGQRWTFSPS CLVAYRPEED ANLDVAERAR ENKSAASVSV
     AGSLSVALDK LRTQKSDPEH PGRLVVEAAL GNVARALDLL RRHPEQASYH PALVVDTKNQ
     GRTALQVAAY LGQVELVRLL LQARASMDLP DDEGNTVLHY TAMGNQPEAT RVLLSAGCAV
     DARNGTRSTA LHVAVQRGFL EVVKILCERG CDVNLPDAHA DTPLHSAISA GAGASSIVEV
     LTEVPGIDVT ATNSQGFTLL HHASLKGHVL AVRKILARAR QLVDAKKEDG FTALHLAALN
     NHREVAQVLI REGRCDVNVR NRKLQSPLHL AVQQAHLGLV PLLVDAGCSV NTEDEEGDTA
     LHVALQRHQL LPLVADRAGG DPGPLQLLSR LQASGLPGCT ELTVGAAVAC FLALEGADVS
     YANHRGRSPL DLATEGRVLK ALQGCAQRFR ERQAGGGGGV PPGPRHVLST PNTVTNLHVS
     GTAGPEAAEC LVCSELALLI LFSPCQHRTV CEECARRMKK CIRCQVVISK KLRPDGSEVV
     NAIQVPGPPR QLVEELQSRY RQMEERITCP ICIDSHIRLV FQCGHGACAP CGAALNACPI
     CRQPIRDRIQ IFV
//
ID   OTU7A_MOUSE             Reviewed;         926 AA.
AC   Q8R554;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=OTU domain-containing protein 7A;
DE            EC=3.4.19.12;
DE   AltName: Full=Zinc finger protein Cezanne 2;
GN   Name=Otud7a; Synonyms=Cezanne2, Otud7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RA   Evans P.C., Coadwell W.J., Kilshaw P.J.;
RT   "Isolation of a novel murine gene, Cezanne 2.";
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has deubiquitinating activity that is directed towards
CC       'Lys-48' or 'Lys-63'-linked polyubiquitin chains. Hydrolyzes both
CC       linear and branched forms of polyubiquitin (By similarity).
CC   -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the peptidase C64 family.
CC   -!- SIMILARITY: Contains 1 A20-type zinc finger.
CC   -!- SIMILARITY: Contains 1 OTU domain.
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DR   EMBL; AJ430384; CAD23048.1; -; mRNA.
DR   IPI; IPI00153939; -.
DR   RefSeq; NP_570950.1; NM_130880.1.
DR   UniGene; Mm.156872; -.
DR   ProteinModelPortal; Q8R554; -.
DR   SMR; Q8R554; 116-561, 889-921.
DR   MEROPS; C64.002; -.
DR   PhosphoSite; Q8R554; -.
DR   PRIDE; Q8R554; -.
DR   Ensembl; ENSMUST00000058476; ENSMUSP00000057282; ENSMUSG00000033510.
DR   GeneID; 170711; -.
DR   KEGG; mmu:170711; -.
DR   UCSC; uc009hfl.1; mouse.
DR   CTD; 170711; -.
DR   MGI; MGI:2158505; Otud7a.
DR   eggNOG; roNOG11785; -.
DR   GeneTree; ENSGT00530000062989; -.
DR   HOGENOM; HBG444533; -.
DR   HOVERGEN; HBG050904; -.
DR   InParanoid; Q8R554; -.
DR   OMA; NGKNGDS; -.
DR   OrthoDB; EOG4BRWK6; -.
DR   PhylomeDB; Q8R554; -.
DR   NextBio; 370222; -.
DR   ArrayExpress; Q8R554; -.
DR   Bgee; Q8R554; -.
DR   CleanEx; MM_OTUD7A; -.
DR   Genevestigator; Q8R554; -.
DR   GermOnline; ENSMUSG00000033510; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR003323; OTU.
DR   InterPro; IPR009060; UBA-like.
DR   InterPro; IPR002653; Znf_A20.
DR   Pfam; PF02338; OTU; 1.
DR   SUPFAM; SSF46934; UBA_like; 1.
DR   PROSITE; PS50802; OTU; 1.
DR   PROSITE; PS51036; ZF_A20; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Metal-binding; Nucleus; Protease;
KW   Thiol protease; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    926       OTU domain-containing protein 7A.
FT                                /FTId=PRO_0000188790.
FT   DOMAIN      201    377       OTU.
FT   ZN_FING     884    919       A20-type.
FT   REGION      170    413       TRAF-binding (By similarity).
FT   REGION      185    452       Catalytic (By similarity).
FT   MOTIF       497    512       Nuclear localization signal (Potential).
FT   ACT_SITE    212    212       Nucleophile (By similarity).
FT   ACT_SITE    370    370       Proton acceptor (By similarity).
SQ   SEQUENCE   926 AA;  100797 MW;  4D6BD05A0410BED9 CRC64;
     MVSSLLPNPP SAECWAALLH DPMTLDMDAV LSDFVRSTGA EPGLARDLLE GKNWDLTAAL
     SDYEQLRQVH TANLPHVFNE GRCAKQAERE LPQPGHKVER PCLQRQDDIA QAEKRLSRGI
     SHASSAIVSL ARSHVANECN NEQFPLEMPI YTFQLPDLSV YSEDFRSFIE RDLIEQATMV
     ALEQAGRLNW WSTVCTSCKR LLPLATTGDG NCLLHAASLG MWGFHDRDLV LRKALYTMMR
     TGAEREALKR RWRWQQTQQN KEEEWEREWT ELLKLASSEP RTHFSKNGSG TGGGVDNSED
     PVYESLEEFH VFVLAHILRR PIVVVADTML RDSGGEAFAP IPFGGIYLPL EVPPNRCHCS
     PLVLAYDQAH FSALVSMEQR DQQREQAVIP LTDSEHKLLP LHFAVDPGKD WEWGKDDNDN
     ARLANLILSL EAKLNLLHSY MNVTWIRIPS ETRAPLAQPE SPTASAGEDV QSLAESLDSD
     RDSVCSNSNS NNGKNGKDKE KEKQRKDKDK TRADSVANKL GSFSKTLGIK LKKNMGGLGG
     LVHGKMGRAN SANGKNGDSA ERNKEKKSKS RKGSKEESGA SASTSPSEKT TPSPTDKASG
     ASPADKGSGS RGDAWKYSTD VKLSLNILRA AMQGERKFIF AGLLLTSHRH QFHEEMIGYY
     LTSAQERFSA EQEQRRRDAA AAAAAATATA TVKRPARRPE AEGAPGPERA SPGPTAAQPT
     QLVLKLKERP SPGTGASARA ARAAGGAASP GPGGGARRAA PGTGGPTPGR SPPAPARQSV
     IHVQAAARDE ACAPTVGALR PCATYPQQNR SLWSQSYSPA RSALRTVNTV ESLAPGGADA
     PGPAEHKSQT YSNGFGAARD GLEFADADAP AARSNAECGR GGPGPAQRRC QRENCAFYGR
     AETEHFCSYC YREELRRRRE ARAARP
//
ID   SNP47_MOUSE             Reviewed;         413 AA.
AC   Q8R570; Q3UNK4; Q8BK87;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Synaptosomal-associated protein 47;
DE            Short=SNAP-47;
DE   AltName: Full=Synaptosomal-associated 47 kDa protein;
GN   Name=Snap47;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=16621800; DOI=10.1074/jbc.M513838200;
RA   Holt M., Varoqueaux F., Wiederhold K., Takamori S., Urlaub H.,
RA   Fasshauer D., Jahn R.;
RT   "Identification of SNAP-47, a novel Qbc-SNARE with ubiquitous
RT   expression.";
RL   J. Biol. Chem. 281:17076-17083(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C3H, and C57BL/6J;
RC   TISSUE=Brain, Cerebellum, Embryo, and Embryonic stem cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in intracellular membrane fusion.
CC   -!- SUBUNIT: Forms a complex containing SNAP47, VAMP2 and STX1A.
CC   -!- SUBCELLULAR LOCATION: Endomembrane system. Cytoplasm, perinuclear
CC       region. Note=Appears to be exclusively membrane-bound. In primary
CC       neurons, widely distributed in both cell bodies and neuronal
CC       processes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R570-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R570-2; Sequence=VSP_028615, VSP_028616;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed with the most abundant
CC       expression in the brain. In brain, most highly expressed in the
CC       glomerular layer of the olfactory bulb, the cortex, striatum,
CC       hippocampus, and colliculi (at protein level).
CC   -!- DEVELOPMENTAL STAGE: Expressed as early as E10 in developing brain
CC       and reaches maximal levels at E18.
CC   -!- SIMILARITY: Belongs to the SVAP1 family.
CC   -!- SIMILARITY: Contains 2 t-SNARE coiled-coil homology domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC35874.1; Type=Frameshift; Positions=312, 330;
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK028053; BAC25723.1; -; mRNA.
DR   EMBL; AK049330; BAC33686.1; -; mRNA.
DR   EMBL; AK075640; BAC35874.1; ALT_FRAME; mRNA.
DR   EMBL; AK144165; BAE25743.1; -; mRNA.
DR   EMBL; AL713994; CAI25399.1; -; Genomic_DNA.
DR   EMBL; BC023182; AAH23182.1; -; mRNA.
DR   EMBL; BC029025; AAH29025.1; -; mRNA.
DR   IPI; IPI00269408; -.
DR   IPI; IPI00869421; -.
DR   RefSeq; NP_653104.1; NM_144521.2.
DR   UniGene; Mm.26680; -.
DR   ProteinModelPortal; Q8R570; -.
DR   SMR; Q8R570; 119-171, 357-412.
DR   PhosphoSite; Q8R570; -.
DR   PRIDE; Q8R570; -.
DR   Ensembl; ENSMUST00000010038; ENSMUSP00000010038; ENSMUSG00000009894.
DR   GeneID; 67826; -.
DR   KEGG; mmu:67826; -.
DR   UCSC; uc007jds.1; mouse.
DR   CTD; 67826; -.
DR   MGI; MGI:1915076; Snap47.
DR   eggNOG; roNOG15493; -.
DR   GeneTree; ENSGT00390000000182; -.
DR   HOGENOM; HBG402999; -.
DR   HOVERGEN; HBG057915; -.
DR   InParanoid; Q8R570; -.
DR   OMA; LEHFWRE; -.
DR   OrthoDB; EOG4H72C0; -.
DR   PhylomeDB; Q8R570; -.
DR   NextBio; 325641; -.
DR   ArrayExpress; Q8R570; -.
DR   Bgee; Q8R570; -.
DR   Genevestigator; Q8R570; -.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PROSITE; PS50192; T_SNARE; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Membrane; Repeat.
FT   CHAIN         1    413       Synaptosomal-associated protein 47.
FT                                /FTId=PRO_0000307152.
FT   DOMAIN      109    171       t-SNARE coiled-coil homology 1.
FT   DOMAIN      350    412       t-SNARE coiled-coil homology 2.
FT   VAR_SEQ     326    333       RPKGCTPH -> CHLFLIIS (in isoform 2).
FT                                /FTId=VSP_028615.
FT   VAR_SEQ     334    413       Missing (in isoform 2).
FT                                /FTId=VSP_028616.
FT   CONFLICT    355    355       F -> S (in Ref. 2; BAC35874).
SQ   SEQUENCE   413 AA;  46524 MW;  A923C061BE7E569D CRC64;
     MSSDMRVHSW SCSYYLDLEK QWVSGKLTLT PHSLKFIVEK TEEVLVGLPL SSIIEIRKES
     SLFIFGAITV LEKGQTKHWF SSLQPSRNVV FNVIEHFWRE LLLSQPGTAA NIPSHVTRGQ
     ELIGLMANSQ KRMEDTAKDL QQQSEQLDSV LKGLEKMESD LDVADRLLTE LETPSWWPFG
     SKFWKMPAEE NLKEGVSSTC EPFGKEGVVI TVPAIISERA ESHSKLGKLT VLVSALEIYD
     SCSLLLHRFE KEDVDDIKVH SPYEVSIRQR FIGKPDVAYQ LISAKMPEVI PILEVQFSSK
     IELLEDALVL RNKVFASSAE RHAASRPKGC TPHRELPTGG QEGEQLQLQK NLPLFSEGEA
     QELTQILSKM KGLALDTEAE LERQDAALDG ITVAVDRATL NVDKQNRRMR KLM
//
ID   KPRB_MOUSE              Reviewed;         369 AA.
AC   Q8R574;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Phosphoribosyl pyrophosphate synthase-associated protein 2;
DE            Short=PRPP synthase-associated protein 2;
DE   AltName: Full=41 kDa phosphoribosypyrophosphate synthetase-associated protein;
DE            Short=PAP41;
GN   Name=Prpsap2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Seems to play a negative regulatory role in 5-
CC       phosphoribose 1-diphosphate synthesis (By similarity).
CC   -!- SUBUNIT: Binds to PRPS1 and PRPS2 (By similarity).
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase
CC       family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK076811; BAC36491.1; -; mRNA.
DR   EMBL; BC023178; AAH23178.1; -; mRNA.
DR   IPI; IPI00153950; -.
DR   RefSeq; NP_001157714.1; NM_001164242.1.
DR   RefSeq; NP_659055.1; NM_144806.2.
DR   UniGene; Mm.27703; -.
DR   ProteinModelPortal; Q8R574; -.
DR   SMR; Q8R574; 19-368.
DR   PhosphoSite; Q8R574; -.
DR   PRIDE; Q8R574; -.
DR   Ensembl; ENSMUST00000004955; ENSMUSP00000004955; ENSMUSG00000020528.
DR   GeneID; 212627; -.
DR   KEGG; mmu:212627; -.
DR   NMPDR; fig|10090.3.peg.23891; -.
DR   UCSC; uc007jie.1; mouse.
DR   CTD; 212627; -.
DR   MGI; MGI:2384838; Prpsap2.
DR   GeneTree; ENSGT00550000074583; -.
DR   HOGENOM; HBG519284; -.
DR   HOVERGEN; HBG001520; -.
DR   InParanoid; Q8R574; -.
DR   OMA; ELNTIFL; -.
DR   OrthoDB; EOG4C87SQ; -.
DR   PhylomeDB; Q8R574; -.
DR   NextBio; 373648; -.
DR   ArrayExpress; Q8R574; -.
DR   Bgee; Q8R574; -.
DR   Genevestigator; Q8R574; -.
DR   GermOnline; ENSMUSG00000020528; Mus musculus.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:InterPro.
DR   GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005946; Rib-P_diPkinase.
DR   TIGRFAMs; TIGR01251; ribP_PPkin; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Nucleotide biosynthesis; Phosphoprotein.
FT   CHAIN         1    369       Phosphoribosyl pyrophosphate synthase-
FT                                associated protein 2.
FT                                /FTId=PRO_0000141083.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     219    219       Phosphoserine (By similarity).
FT   MOD_RES     227    227       Phosphoserine.
FT   MOD_RES     251    251       N6-acetyllysine (By similarity).
SQ   SEQUENCE   369 AA;  40881 MW;  248C5DC742857ED1 CRC64;
     MFCVAPPELE TKMNITKGGL VLFSANSNSS CMELSKKIAE RLGVEMGKVQ VYQEPNRETR
     VQIQESVRGK DVFIIQTISK DVNTTIMELL IMVYACKTSC AKSIIGVIPY FPYSKQCKMR
     KRGSIVSKLL ASMMCKAGLT HLITMDLHQK EIQGFFNIPV DNLRASPFLL QYIQEEIPDY
     RNAVIVAKSP ASAKRAQSFA ERLRLGIAVI HGEAQDAESD LVDGRHSPPM VRSVAAIHPS
     LEIPMLIPKE KPPITVVGDV GGRIAIIVDD IIDDVDSFLA AAETLKERGA YKIFVMATHG
     LLSSDAPRLI EESAIDEVVV TNTIPHEIQK LQCPKIKTVD ISMILSEAIR RIHNGESMSY
     LFRNIGLDD
//
ID   TB22A_MOUSE             Reviewed;         516 AA.
AC   Q8R5A6; Q3U268; Q3U3T0; Q8CA49;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 3.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=TBC1 domain family member 22A;
GN   Name=Tbc1d22a; Synonyms=D15Ertd781e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Heart, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May act as a GTPase-activating protein for Rab family
CC       protein(s) (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R5A6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R5A6-2; Sequence=VSP_016761;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 Rab-GAP TBC domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH23106.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK039627; BAC30403.1; -; mRNA.
DR   EMBL; AK154226; BAE32447.1; -; mRNA.
DR   EMBL; AK154602; BAE32705.1; -; mRNA.
DR   EMBL; AK155459; BAE33274.1; -; mRNA.
DR   EMBL; AK155770; BAE33429.1; -; mRNA.
DR   EMBL; AK146872; BAE27495.1; -; mRNA.
DR   EMBL; BC023106; AAH23106.1; ALT_INIT; mRNA.
DR   EMBL; BC066009; AAH66009.1; -; mRNA.
DR   IPI; IPI00228009; -.
DR   IPI; IPI00653791; -.
DR   RefSeq; NP_663451.2; NM_145476.2.
DR   UniGene; Mm.28904; -.
DR   ProteinModelPortal; Q8R5A6; -.
DR   SMR; Q8R5A6; 195-507.
DR   PhosphoSite; Q8R5A6; -.
DR   PRIDE; Q8R5A6; -.
DR   Ensembl; ENSMUST00000063414; ENSMUSP00000065721; ENSMUSG00000051864.
DR   Ensembl; ENSMUST00000109385; ENSMUSP00000105012; ENSMUSG00000051864.
DR   GeneID; 223754; -.
DR   KEGG; mmu:223754; -.
DR   UCSC; uc007xea.1; mouse.
DR   CTD; 223754; -.
DR   MGI; MGI:1289265; Tbc1d22a.
DR   eggNOG; roNOG12332; -.
DR   GeneTree; ENSGT00510000046400; -.
DR   HOVERGEN; HBG057030; -.
DR   OrthoDB; EOG444KK6; -.
DR   PhylomeDB; Q8R5A6; -.
DR   NextBio; 376878; -.
DR   ArrayExpress; Q8R5A6; -.
DR   Bgee; Q8R5A6; -.
DR   CleanEx; MM_TBC1D22A; -.
DR   Genevestigator; Q8R5A6; -.
DR   GermOnline; ENSMUSG00000051864; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0005097; F:Rab GTPase activator activity; IEA:InterPro.
DR   GO; GO:0032313; P:regulation of Rab GTPase activity; IEA:InterPro.
DR   InterPro; IPR000195; RabGAP/TBC_dom.
DR   Pfam; PF00566; TBC; 1.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; RabGAP_TBC; 2.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; GTPase activation; Phosphoprotein.
FT   CHAIN         1    516       TBC1 domain family member 22A.
FT                                /FTId=PRO_0000208053.
FT   DOMAIN      221    445       Rab-GAP TBC.
FT   MOD_RES     164    164       Phosphoserine (By similarity).
FT   VAR_SEQ       1     41       MASDGARKQFWKRSNSKVPGSIQHVYGAQHPPFDPLLHGTL
FT                                -> MRSGHGQRRGQEAVLEAQQQQGSRAASSMCMEPSTHRL
FT                                IRCYMAPC (in isoform 2).
FT                                /FTId=VSP_016761.
FT   CONFLICT    120    120       E -> D (in Ref. 1; BAE33274/BAE32447).
SQ   SEQUENCE   516 AA;  59362 MW;  A838069E77897B10 CRC64;
     MASDGARKQF WKRSNSKVPG SIQHVYGAQH PPFDPLLHGT LLKSTPKVPT TPVKAKRVST
     FQEFESNTSD AWDAGEDDDE LLAMATESLN SEVVMETAHR VLRNHSQRQS QPSQKTTEPE
     PEPQPIAEPP VPPSGDLRLV KSVSESHTPC PSESTGDTVP LQRSQSLPHS ATVTLSGTSD
     PHALADSALS KRETSRLDKF KQLLAGPNTD LEELRKLSWS GIPKPVRPMT WKLLSGYLPA
     NVDRRPATLQ RKQKEYFAFI EHYYSSRNDE VHQDTYRQIH IDIPRMSPEA LILQPKVTEI
     FERILFIWAI RHPASGYVQG INDLVTPFFV VFICEYTDRE DVDKVDVSSV PAEVLRNIEA
     DTYWCMSKLL DGIQDNYTFA QPGIQMKVKM LEELVSRIDE RVHRHLDGHE VRYLQFAFRW
     MNNLLMRELP LRCTIRLWDT YQSEPEGFSH FHLYVCAAFL VRWRREILEE RDFQELLLFL
     QNLPTARWDD QDVSLLLAEA YRLKFAFADA PNHYKK
//
ID   ACTY_MOUSE              Reviewed;         376 AA.
AC   Q8R5C5;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Beta-centractin;
DE   AltName: Full=Actin-related protein 1B;
DE            Short=ARP1B;
GN   Name=Actr1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 201-215 AND 239-255, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [4]
RP   NITRATION [LARGE SCALE ANALYSIS] AT TYR-4, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16800626; DOI=10.1021/bi060474w;
RA   Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
RA   Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
RA   Squier T.C., Bigelow D.J.;
RT   "Endogenously nitrated proteins in mouse brain: links to
RT   neurodegenerative disease.";
RL   Biochemistry 45:8009-8022(2006).
CC   -!- FUNCTION: Component of a multi-subunit complex involved in
CC       microtubule based vesicle motility. It is associated with the
CC       centrosome (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
CC       cytoskeleton, centrosome (By similarity).
CC   -!- SIMILARITY: Belongs to the actin family. ARP1 subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK088839; BAC40604.1; -; mRNA.
DR   EMBL; BC023020; AAH23020.1; -; mRNA.
DR   IPI; IPI00153990; -.
DR   RefSeq; NP_666219.1; NM_146107.2.
DR   UniGene; Mm.28521; -.
DR   ProteinModelPortal; Q8R5C5; -.
DR   SMR; Q8R5C5; 9-376.
DR   STRING; Q8R5C5; -.
DR   PhosphoSite; Q8R5C5; -.
DR   UCD-2DPAGE; Q8R5C5; -.
DR   PRIDE; Q8R5C5; -.
DR   Ensembl; ENSMUST00000043951; ENSMUSP00000047326; ENSMUSG00000037351.
DR   GeneID; 226977; -.
DR   KEGG; mmu:226977; -.
DR   UCSC; uc007aqx.1; mouse.
DR   CTD; 226977; -.
DR   MGI; MGI:1917446; Actr1b.
DR   GeneTree; ENSGT00560000076554; -.
DR   HOGENOM; HBG559892; -.
DR   HOVERGEN; HBG003771; -.
DR   InParanoid; Q8R5C5; -.
DR   OMA; PDGSMLD; -.
DR   OrthoDB; EOG4NS3BN; -.
DR   PhylomeDB; Q8R5C5; -.
DR   NextBio; 378426; -.
DR   ArrayExpress; Q8R5C5; -.
DR   Bgee; Q8R5C5; -.
DR   CleanEx; MM_ACTR1B; -.
DR   Genevestigator; Q8R5C5; -.
DR   GermOnline; ENSMUSG00000037351; Mus musculus.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004000; Actin-like.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Nitration; Nucleotide-binding.
FT   CHAIN         1    376       Beta-centractin.
FT                                /FTId=PRO_0000089061.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES       4      4       Nitrated tyrosine.
SQ   SEQUENCE   376 AA;  42281 MW;  C038D186113C1A69 CRC64;
     MESYDIIANQ PVVIDNGSGV IKAGFAGDQI PKYCFPNYVG RPKHMRVMAG ALEGDLFIGP
     KAEEHRGLLT IRYPMEHGVV RDWNDMERIW QYVYSKDQLQ TFSEEHPVLL TEAPLNPSKN
     REKAAEVFFE TFNVPALFIS MQAVLSLYAT GRTTGVVLDS GDGVTHAVPI YEGFAMPHSI
     MRVDIAGRDV SRYLRLLLRK EGADFHTSAE FEVVRTIKER ACYLSINPQK DEALETEKVQ
     YTLPDGSTLD VGPARFRAPE LLFQPDLVGD ESEGLHEVLA FAIHKSDMDL RRTLFSNIVL
     SGGSTLFKGF GDRLLSEVKK LAPKDVKIKI SAPQERLYST WIGGSILASL DTFKKMWVSK
     KEYEEDGSRA IHRKTF
//
ID   UBP15_MOUSE             Reviewed;         981 AA.
AC   Q8R5H1; Q3UL25;
DT   22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 15;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 15;
DE   AltName: Full=Ubiquitin thiolesterase 15;
DE   AltName: Full=Ubiquitin-specific-processing protease 15;
GN   Name=Usp15;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6;
RX   MEDLINE=22419901; PubMed=12532266; DOI=10.1007/s00335-002-3035-0;
RA   Angelats C., Wang X.-W., Jermiin L.S., Copeland N.G., Jenkins N.A.,
RA   Baker R.T.;
RT   "Isolation and characterization of the mouse ubiquitin-specific
RT   protease Usp15.";
RL   Mamm. Genome 14:31-46(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, Testis, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Protease that degrades 'Lys-48'-linked polyubiquitin
CC       chains. Protects target proteins against proteasomal degradation
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- SUBUNIT: Identified in a complex with the COP9 signalosome complex
CC       (CSN).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Shuttles between nucleus and cytoplasm (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Experimental confirmation may be lacking for some
CC         isoforms;
CC       Name=1;
CC         IsoId=Q8R5H1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R5H1-2; Sequence=VSP_005262, VSP_005263;
CC       Name=3;
CC         IsoId=Q8R5H1-3; Sequence=VSP_005264;
CC       Name=4;
CC         IsoId=Q8R5H1-4; Sequence=VSP_005265, VSP_005266;
CC   -!- TISSUE SPECIFICITY: Widely expressed with highest levels in
CC       testis, heart and liver.
CC   -!- PTM: Phosphorylated. Phosphorylation protects against
CC       ubiquitination and subsequent degradation by the proteasome (By
CC       similarity).
CC   -!- PTM: Ubiquitinated, leading to degradation by the proteasome (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC   -!- SIMILARITY: Contains 1 DUSP domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF468037; AAL77418.1; -; mRNA.
DR   EMBL; AK046332; BAC32683.1; -; mRNA.
DR   EMBL; AK083303; BAC38854.1; -; mRNA.
DR   EMBL; AK145749; BAE26626.1; -; mRNA.
DR   IPI; IPI00154012; -.
DR   IPI; IPI00222152; -.
DR   IPI; IPI00222154; -.
DR   IPI; IPI00403342; -.
DR   RefSeq; NP_081880.2; NM_027604.3.
DR   UniGene; Mm.244209; -.
DR   UniGene; Mm.470032; -.
DR   ProteinModelPortal; Q8R5H1; -.
DR   SMR; Q8R5H1; 2-222.
DR   STRING; Q8R5H1; -.
DR   MEROPS; C19.022; -.
DR   PhosphoSite; Q8R5H1; -.
DR   PRIDE; Q8R5H1; -.
DR   Ensembl; ENSMUST00000020334; ENSMUSP00000020334; ENSMUSG00000020124.
DR   Ensembl; ENSMUST00000105258; ENSMUSP00000100893; ENSMUSG00000020124.
DR   Ensembl; ENSMUST00000105259; ENSMUSP00000100894; ENSMUSG00000020124.
DR   GeneID; 14479; -.
DR   KEGG; mmu:14479; -.
DR   UCSC; uc007hgn.1; mouse.
DR   UCSC; uc007hgt.1; mouse.
DR   CTD; 14479; -.
DR   MGI; MGI:101857; Usp15.
DR   GeneTree; ENSGT00600000084034; -.
DR   HOGENOM; HBG318284; -.
DR   HOVERGEN; HBG000864; -.
DR   InParanoid; Q8R5H1; -.
DR   OMA; INNRNVK; -.
DR   OrthoDB; EOG4DNF3R; -.
DR   PhylomeDB; Q8R5H1; -.
DR   BRENDA; 3.1.2.15; 244.
DR   NextBio; 286150; -.
DR   ArrayExpress; Q8R5H1; -.
DR   Bgee; Q8R5H1; -.
DR   CleanEx; MM_USP15; -.
DR   Genevestigator; Q8R5H1; -.
DR   GermOnline; ENSMUSG00000020124; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:EC.
DR   GO; GO:0004843; F:ubiquitin-specific protease activity; ISS:UniProtKB.
DR   GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR006615; Pept_C19_DUSP.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19.
DR   InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR   Pfam; PF06337; DUF1055; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00695; DUSP; 1.
DR   SUPFAM; SSF55205; RNA3'_cycl/enolpyr_transf_A/B; 1.
DR   PROSITE; PS51283; DUSP; 1.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; 1.
DR   PROSITE; PS50235; UCH_2_3; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Cytoplasm; Hydrolase; Nucleus;
KW   Phosphoprotein; Protease; Thiol protease; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    981       Ubiquitin carboxyl-terminal hydrolase 15.
FT                                /FTId=PRO_0000080642.
FT   DOMAIN        7    118       DUSP.
FT   ACT_SITE    298    298       Nucleophile (By similarity).
FT   ACT_SITE    891    891       Proton acceptor (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     229    229       Phosphoserine (By similarity).
FT   MOD_RES     961    961       Phosphoserine (By similarity).
FT   MOD_RES     965    965       Phosphoserine (By similarity).
FT   VAR_SEQ      18     25       TLLKTSLR -> DAWLKPRSG (in isoform 2).
FT                                /FTId=VSP_005262.
FT   VAR_SEQ     209    227       LVIEQKNEDGTWPRGPSTP -> PRCIQFFNFTKDLSFISI
FT                                K (in isoform 4).
FT                                /FTId=VSP_005265.
FT   VAR_SEQ     228    981       Missing (in isoform 4).
FT                                /FTId=VSP_005266.
FT   VAR_SEQ     228    256       Missing (in isoform 2).
FT                                /FTId=VSP_005263.
FT   VAR_SEQ     229    981       Missing (in isoform 3).
FT                                /FTId=VSP_005264.
SQ   SEQUENCE   981 AA;  112325 MW;  6D5377C3FEA6E40A CRC64;
     MAEGGAADLD TQRSDIATLL KTSLRKGDTW YLVDSRWFKQ WKKYVGFDSW DKYQMGDQNV
     YPGPIDNSGL LKDGDAQSLK EHLIDELDYI LLPTEGWNKL VSWYTLMEGQ EPIARKVVEQ
     GMFVKHCKVE VYLTELKLCE NGNMNNVVTR RFSKADTIDT IEKEIRKIFN IPDEKEARLW
     NKYMSNTFEP LNKPDSTIQD AGLYQGQVLV IEQKNEDGTW PRGPSTPKSP GASNFSTLPK
     ISPSSLSNNY NNINNRNVKN SNYCLPSYTA YKNYDYSEPG RNNEQPGLCG LSNLGNTCFM
     NSAIQCLSNT PPLTEYFLND KYQEELNFDN PLGMRGEIAK SYAELIKQMW SGKFSYVTPR
     AFKTQVGRFA PQFSGYQQQD CQELLAFLLD GLHEDLNRIR KKPYIQLKDA DGRPDKVVAE
     EAWENHLKRN DSIIVDIFHG LFKSTLVCPE CAKISVTFDP FCYLTLPLPM KKERSLEVYL
     VRMDPLAKPM QYKVIVPKIG NILDLCTALS ALSGVPADKM IVTDIYNHRF HRIFAVDENL
     SSIMERDDIY VFEININRAE DTEHVVIPVC LREKFRHSSY THHTGSSLFG QPFLMAIPRN
     NTEDKLYNLL LLRMCRYVKM STETEETDGH LRCCEDQNIN GNGPNGLHEE GSPSEMETDE
     PDDESSQDQE LPSENENSQS EDSVGGDNDS ENGLCTEETC KGQLTGHKKR LFTFQFNNLG
     NNDINYIKDD TSHIRFDDRQ LRLDERSFLA LDWDPDLKKR YFDENAAEDF EKHESVEYKP
     PKRPFVKLKD CIELFTTKEK LGAEDPWYCP NCKEHQQATK KLDLWSLPPV LVVHLKRFSY
     SRYMRDKLDT LVDFPISDLD MSEFLINPNA GPCRYNLIAV SNHYGGMGGG HYTAFAKNKD
     DGKWYYFDDS SVSTASEDQI VSKAAYVLFY QRQDTFSGTG FFPLDRETKG ASAATGIPLE
     SDEDSNDNDN DLENENCMHT N
//
ID   WASF1_MOUSE             Reviewed;         559 AA.
AC   Q8R5H6; Q91W51; Q9ERQ9;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Wiskott-Aldrich syndrome protein family member 1;
DE            Short=WASP family protein member 1;
DE   AltName: Full=Protein WAVE-1;
GN   Name=Wasf1; Synonyms=Wave1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20428428; PubMed=10970852; DOI=10.1093/emboj/19.17.4589;
RA   Westphal R.S., Soderling S.H., Alto N.M., Langeberg L.K., Scott J.D.;
RT   "Scar/WAVE-1, a Wiskott-Aldrich syndrome protein, assembles an actin-
RT   associated multi-kinase scaffold.";
RL   EMBO J. 19:4589-4600(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=129/Sv;
RX   MEDLINE=22057894; PubMed=12062808; DOI=10.1016/S0378-1119(02)00560-7;
RA   Benachenhou N., Massy I., Vacher J.;
RT   "Characterization and expression analyses of the mouse Wiskott-Aldrich
RT   syndrome protein (WASP) family member Wave1/Scar.";
RL   Gene 290:131-140(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney, and Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 499-507, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Downstream effector molecules involved in the
CC       transmission of signals from tyrosine kinase receptors and small
CC       GTPases to the actin cytoskeleton (By similarity).
CC   -!- SUBUNIT: Component of the WAVE1 complex composed of ABI2, CYFIP2,
CC       C3orf10/HSPC300, NCKAP1 and WASF1/WAVE1. CYFIP2 binds to activated
CC       RAC1 which causes the complex to dissociate, releasing activated
CC       WASF1. The complex can also be activated by NCK1. Binds actin and
CC       the Arp2/3 complex. Interacts with BAIAP2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Note=Dot-like pattern in the cytoplasm. Concentrated in Rac-
CC       regulated membrane-ruffling areas (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain.
CC   -!- DOMAIN: Binds the Arp2/3 complex through the C-terminal region and
CC       actin through verprolin homology (VPH) domain (By similarity).
CC   -!- SIMILARITY: Belongs to the SCAR/WAVE family.
CC   -!- SIMILARITY: Contains 1 WH2 domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF290877; AAG02214.1; -; mRNA.
DR   EMBL; AF467773; AAL75574.1; -; mRNA.
DR   EMBL; BC016896; AAH16896.1; -; mRNA.
DR   EMBL; BC053423; AAH53423.1; -; mRNA.
DR   IPI; IPI00471372; -.
DR   RefSeq; NP_114083.1; NM_031877.3.
DR   UniGene; Mm.41353; -.
DR   ProteinModelPortal; Q8R5H6; -.
DR   SMR; Q8R5H6; 21-185, 496-544.
DR   MINT; MINT-4140216; -.
DR   STRING; Q8R5H6; -.
DR   PhosphoSite; Q8R5H6; -.
DR   PRIDE; Q8R5H6; -.
DR   Ensembl; ENSMUST00000019975; ENSMUSP00000019975; ENSMUSG00000019831.
DR   Ensembl; ENSMUST00000105509; ENSMUSP00000101148; ENSMUSG00000019831.
DR   GeneID; 83767; -.
DR   KEGG; mmu:83767; -.
DR   UCSC; uc007exi.1; mouse.
DR   CTD; 83767; -.
DR   MGI; MGI:1890563; Wasf1.
DR   eggNOG; roNOG13421; -.
DR   GeneTree; ENSGT00550000074443; -.
DR   HOGENOM; HBG715875; -.
DR   HOVERGEN; HBG058482; -.
DR   InParanoid; Q8R5H6; -.
DR   OMA; PEPKRHP; -.
DR   OrthoDB; EOG4C2H9X; -.
DR   NextBio; 350760; -.
DR   PMAP-CutDB; Q8R5H6; -.
DR   ArrayExpress; Q8R5H6; -.
DR   Bgee; Q8R5H6; -.
DR   CleanEx; MM_WASF1; -.
DR   Genevestigator; Q8R5H6; -.
DR   GermOnline; ENSMUSG00000019831; Mus musculus.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR003124; WH2_actin-bd.
DR   Pfam; PF02205; WH2; 1.
DR   SMART; SM00246; WH2; 1.
DR   PROSITE; PS51082; WH2; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Cytoplasm; Cytoskeleton; Direct protein sequencing.
FT   CHAIN         1    559       Wiskott-Aldrich syndrome protein family
FT                                member 1.
FT                                /FTId=PRO_0000188993.
FT   DOMAIN      497    514       WH2.
FT   COMPBIAS    278    283       Poly-Pro.
FT   COMPBIAS    322    332       Poly-Pro.
FT   COMPBIAS    348    359       Poly-Pro.
FT   COMPBIAS    369    374       Poly-Pro.
FT   COMPBIAS    424    435       Poly-Pro.
FT   CONFLICT      2      2       P -> L (in Ref. 2; AAL75574).
FT   CONFLICT    324    324       P -> S (in Ref. 3; AAH16896).
SQ   SEQUENCE   559 AA;  61509 MW;  8746910987D80D16 CRC64;
     MPLVKRNIDP RHLCHTALPR GIKNELECVT NISLANIIRQ LSSLSKYAED IFGELFNEAH
     SFSFRVNSLQ ERVDRLSVSV TQLDPKEEEL SLQDITMRKA FRSSTIQDQQ LFDRKTLPIP
     LQETYDVCEQ PPPLNILTPY RDDGKEGLKF YTNPSYFFDL WKEKMLQDTE DKRKEKRKQK
     QKNLDRPHEP EKVPRAPHDR RREWQKLAQG PELAEDDADL LHKHIEVANG PASHYETRPQ
     TYVDHMDGSY SLSALPFSQM SELLTRAEER VLVRPHEPPP PPPMHGAGDA KPTPTCISSA
     TGLIENRPQS PAAGRTPVFV SPTPPPPPPP LPSALSTSSL RASMTSTPPP PVPPPPPPPA
     TALQAPAVPP PPAPLQIAPG VLHPAPPPIA PPLVQPSPPV ARAAPVCETV PVHPLPQGEV
     QGLPPPPPPP PLPPPGIRPS SPVAVAALAH PPSGLHPAPS TAPGPHAPLM PPSPPSQVLP
     ASEPKRHPST LPVISDARSV LLEAIRKGIQ LRKVEEQREQ EAKHERIEND VATILSRRIA
     VEYSDSEDDS EFDEVDWLE
//
ID   Q8R5L1_MOUSE            Unreviewed;       279 AA.
AC   Q8R5L1;
DT   01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   SubName: Full=Complement component 1, q subcomponent binding protein;
DE   SubName: Full=Complement component 1, q subcomponent binding protein, isoform CRA_b;
DE   SubName: Full=p32-RACK;
GN   Name=C1qbp; ORFNames=DN-393H17.2-001, RP23-83I13.1-001, mCG_21176;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21826357; PubMed=11698413; DOI=10.1074/jbc.M109333200;
RA   Robles-Flores M., Rendon-Huerta E., Gonzalez-Aguilar H.,
RA   Mendoza-Hernandez G., Islas S., Mendoza V., Ponce-Castaneda M.V.,
RA   Gonzalez-Mariscal L., Lopez-Casillas F.;
RT   "p32 (gC1qBP) is a general protein kinase C (PKC)-binding protein;
RT   interaction and cellular localization of P32-PKC complexes in ray
RT   hepatocytes.";
RL   J. Biol. Chem. 277:5247-5255(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Holt K.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RA   Sycamore N.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129; TISSUE=Mammary tumor. Brca1-/fl;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC038075; AAH38075.1; -; mRNA.
DR   EMBL; AF300619; AAL77246.1; -; mRNA.
DR   EMBL; AL596136; CAI26064.1; -; Genomic_DNA.
DR   EMBL; CR936847; CAM46325.1; -; Genomic_DNA.
DR   EMBL; CH466596; EDL12635.1; -; Genomic_DNA.
DR   IPI; IPI00132799; -.
DR   RefSeq; NP_031599.2; NM_007573.2.
DR   UniGene; Mm.30049; -.
DR   HSSP; Q07021; 1P32.
DR   ProteinModelPortal; Q8R5L1; -.
DR   SMR; Q8R5L1; 72-279.
DR   STRING; Q8R5L1; -.
DR   PRIDE; Q8R5L1; -.
DR   Ensembl; ENSMUST00000078528; ENSMUSP00000077612; ENSMUSG00000018446.
DR   GeneID; 12261; -.
DR   KEGG; mmu:12261; -.
DR   NMPDR; fig|10090.3.peg.24593; -.
DR   UCSC; uc007jxf.1; mouse.
DR   CTD; 12261; -.
DR   MGI; MGI:1194505; C1qbp.
DR   GeneTree; ENSGT00390000018406; -.
DR   HOGENOM; HBG715847; -.
DR   HOVERGEN; HBG000914; -.
DR   InParanoid; Q8R5L1; -.
DR   OMA; GLHTEGD; -.
DR   NextBio; 280698; -.
DR   ArrayExpress; Q8R5L1; -.
DR   Bgee; Q8R5L1; -.
DR   Genevestigator; Q8R5L1; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:InterPro.
DR   InterPro; IPR003428; MAM33.
DR   Gene3D; G3DSA:3.10.280.10; MAM33; 1.
DR   Pfam; PF02330; MAM33; 1.
DR   SUPFAM; SSF54529; MAM33; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   279 AA;  31025 MW;  33D459A55CB46A0A CRC64;
     MLPLLRCVPR ALGAAASGLR TAIPAQPLRH LLQPAPRPCL RPFGLLSVRA GSARRSGLLQ
     PPVPCACGCG ALHTEGDKAF VEFLTDEIKE EKKIQKHKSL PKMSGDWELE VNGTEAKLLR
     KVAGEKITVT FNINNSIPPT FDGEEEPSQG QKAEEQEPEL TSTPNFVVEV TKTDGKKTLV
     LDCHYPEDEI GHEDEAESDI FSIKEVSFQA TGDSEWRDTN YTLNTDSLDW ALYDHLMDFL
     ADRGVDNTFA DELVELSTAL EHQEYITFLE DLKSFVKNQ
//
ID   VPS39_MOUSE             Reviewed;         886 AA.
AC   Q8R5L3; Q922I3;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Vam6/Vps39-like protein;
GN   Name=Vps39; Synonyms=Pldn, Vam6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=Swiss Webster / NIH;
RA   Falcon-Perez J.M., Dell'Angelica E.C.;
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in clustering and fusion of late
CC       endosomes and lysosomes (By similarity).
CC   -!- SUBUNIT: Homooligomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Lysosome
CC       membrane; Peripheral membrane protein (By similarity). Late
CC       endosome membrane; Peripheral membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8R5L3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R5L3-2; Sequence=VSP_004076;
CC   -!- SIMILARITY: Belongs to the VAM6/VPS39 family.
CC   -!- SIMILARITY: Contains 1 CNH domain.
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DR   EMBL; AF281050; AAL79766.1; -; mRNA.
DR   EMBL; AF281051; AAL79767.1; -; mRNA.
DR   EMBL; BC007479; AAH07479.1; -; mRNA.
DR   IPI; IPI00154020; -.
DR   IPI; IPI00227698; -.
DR   RefSeq; NP_671495.1; NM_147153.3.
DR   RefSeq; NP_849182.1; NM_178851.3.
DR   UniGene; Mm.246131; -.
DR   ProteinModelPortal; Q8R5L3; -.
DR   STRING; Q8R5L3; -.
DR   PRIDE; Q8R5L3; -.
DR   Ensembl; ENSMUST00000028752; ENSMUSP00000028752; ENSMUSG00000027291.
DR   Ensembl; ENSMUST00000102501; ENSMUSP00000099559; ENSMUSG00000027291.
DR   GeneID; 269338; -.
DR   KEGG; mmu:269338; -.
DR   UCSC; uc008lvj.1; mouse.
DR   UCSC; uc008lvk.1; mouse.
DR   CTD; 269338; -.
DR   MGI; MGI:2443189; Vps39.
DR   GeneTree; ENSGT00530000063596; -.
DR   HOGENOM; HBG464679; -.
DR   HOVERGEN; HBG056493; -.
DR   InParanoid; Q8R5L3; -.
DR   OMA; YVASNHF; -.
DR   OrthoDB; EOG4CRKZD; -.
DR   NextBio; 392787; -.
DR   ArrayExpress; Q8R5L3; -.
DR   Bgee; Q8R5L3; -.
DR   CleanEx; MM_PLDN; -.
DR   CleanEx; MM_VPS39; -.
DR   Genevestigator; Q8R5L3; -.
DR   GermOnline; ENSMUSG00000027291; Mus musculus.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0005083; F:small GTPase regulator activity; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001180; Citron.
DR   InterPro; IPR019452; VPS39/TGF_beta_rcpt-assoc_1.
DR   InterPro; IPR019453; VPS39/TGF_beta_rcpt-assoc_2.
DR   Pfam; PF00780; CNH; 1.
DR   Pfam; PF10366; Vps39_1; 1.
DR   Pfam; PF10367; Vps39_2; 1.
DR   PROSITE; PS50219; CNH; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Endosome; Lysosome; Membrane;
KW   Protein transport; Transport.
FT   CHAIN         1    886       Vam6/Vps39-like protein.
FT                                /FTId=PRO_0000065902.
FT   DOMAIN       15    294       CNH.
FT   VAR_SEQ      47     58       VPADVASPESGS -> G (in isoform 2).
FT                                /FTId=VSP_004076.
SQ   SEQUENCE   886 AA;  101693 MW;  BD46EF52D404C2DA CRC64;
     MHDAFEPVPI LEKLPLQIDC LAAWEEWLLV GTKQGHLLLY RIRKDVVPAD VASPESGSCN
     RFEVTLEKSN KNFSKKIQQI HVVSQFKILV SLLENNIYVH DLLTFQQITT VSKAKGASLF
     TCDLQHTETG EEVLRMCVAV RKKLQLYFWK DREFHELQGD FSVPDVPKSM AWCENSICVG
     FKRDYYLIRV DGKGSIKELF PTGKQLEPLV APLADGKVAV GQDDLTVVLN EEGICTQKCA
     LNWTDIPVAM EHQPPYIVAV LPRYVEIRTL EPRLLVQSIE LQRPRFITSG GSNIIYVASN
     HFVWRLIPVP MATQIQQLLQ DKQFELALQL AEMKDDSDSE KQQQIHHIKN LYAFNLFCQK
     RFDESMQVFA KLGTDPTHVM GLYPDLLPTD YRKQLQYPNP LPTLSGAELE KAHLALIDYL
     TQKRSQLVKK LNDSDHQSST SPLMEGTPTI KSKKKLLQII DTTLLKCYLH TNVALVAPLL
     RLENNHCHIE ESEHVLKKAH KYSELIILYE KKGLHEKALQ VLVDQSKKAN SPLKGHERTV
     QYLQHLGTEN LHLIFSYSVW VLRDFPEDGL KIFTEDLPEV ESLPRDRVLN FLIENFKALA
     IPYLEHIIHV WEETGSQFHN CLIQLYCEKV QSLMKDYLLS LPTGKSPVPA GEEGGELGEY
     RQKLLMFLEI SSHYDPGRLI CDFPFDGLLE ERALLLGRMG KHEQALFIYV HVLKDTKMAK
     EYCHKHYDQN KEGNKDVYLS LLRMYLSPPS IHCLGPIKLE LLEPQANLQA ALQVLELHYS
     KLDTTKAINL LPANTQINDI RIFLEKVLEE NAQKKRFNQV LKNLLHAEFL RVQEERILHQ
     QVKCIITEEK VCMVCKKKIG NSAFARYPNG VVVHYFCSKE VNSADT
//
ID   CADM1_MOUSE             Reviewed;         456 AA.
AC   Q8R5M8; Q6F3J3; Q7TNL1; Q80VG4; Q8K3T6; Q8R4L1; Q9QYL5; Q9QYL6;
AC   Q9Z2H8;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Cell adhesion molecule 1;
DE   AltName: Full=Immunoglobulin superfamily member 4;
DE            Short=IgSF4;
DE   AltName: Full=Nectin-like protein 2;
DE            Short=NECL-2;
DE   AltName: Full=Spermatogenic immunoglobulin superfamily;
DE            Short=SgIgSF;
DE   AltName: Full=Synaptic cell adhesion molecule;
DE            Short=SynCAM;
DE   AltName: Full=Tumor suppressor in lung cancer 1;
DE            Short=TSLC-1;
DE   Flags: Precursor;
GN   Name=Cadm1; Synonyms=Igsf4, Necl2, Ra175, Syncam, SynCam1, Tslc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC   STRAIN=129/SvJ;
RX   PubMed=12242005; DOI=10.1016/S0378-1119(02)00835-1;
RA   Fukami T., Satoh H., Fujita E., Maruyama T., Fukuhara H.,
RA   Kuramochi M., Takamoto S., Momoi T., Murakami Y.;
RT   "Identification of the Tslc1 gene, a mouse orthologue of the human
RT   tumor suppressor TSLC1 gene.";
RL   Gene 295:7-12(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=C57BL/6;
RX   MEDLINE=22192378; PubMed=12202822; DOI=10.1126/science.1072356;
RA   Biederer T., Sara Y., Mozhayeva M., Atasoy D., Liu X., Kavalali E.T.,
RA   Sudhof T.C.;
RT   "SynCAM, a synaptic adhesion molecule that drives synapse assembly.";
RL   Science 297:1525-1531(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 6 AND 7), AND FUNCTION.
RC   TISSUE=Embryonic carcinoma;
RX   PubMed=12799182; DOI=10.1016/S0014-4827(03)00095-8;
RA   Fujita E., Soyama A., Momoi T.;
RT   "RA175, which is the mouse ortholog of TSLC1, a tumor suppressor gene
RT   in human lung cancer, is a cell adhesion molecule.";
RL   Exp. Cell Res. 287:57-66(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, INTERACTION WITH
RP   MPP6, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=12826663; DOI=10.1074/jbc.M305387200;
RA   Shingai T., Ikeda W., Kakunaga S., Morimoto K., Takekuni K., Itoh S.,
RA   Satoh K., Takeuchi M., Imai T., Monden M., Takai Y.;
RT   "Implications of nectin-like molecule-
RT   2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 in cell-cell adhesion and
RT   transmembrane protein localization in epithelial cells.";
RL   J. Biol. Chem. 278:35421-35427(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 49-456 (ISOFORM 2).
RX   PubMed=15893517; DOI=10.1016/j.bbamem.2005.01.013;
RA   Zhou Y., Du G., Hu X., Yu S., Liu Y., Xu Y., Huang X., Liu J., Yin B.,
RA   Fan M., Peng X., Qiang B., Yuan J.;
RT   "Nectin-like molecule 1 is a protein 4.1N associated protein and
RT   recruits protein 4.1N from cytoplasm to the plasma membrane.";
RL   Biochim. Biophys. Acta 1669:142-154(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RC   STRAIN=C57BL/6; TISSUE=Mast cell;
RA   Ito A., Koma Y., Nagano T.;
RT   "A secretion form of SgIGSF/TSLC1.";
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5).
RA   Fujita E., Aikawa K., Momoi T.;
RT   "Neuron-specific isoforms of RA175/TSLC1/SynCAM.";
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   FUNCTION, TISSUE SPECICIFITY, DEVELOPMENTAL STAGE, AND GLYCOSYLATION.
RX   PubMed=12606335; DOI=10.1095/biolreprod.102.012344;
RA   Wakayama T., Koami H., Ariga H., Kobayashi D., Sai Y., Tsuji A.,
RA   Yamamoto M., Iseki S.;
RT   "Expression and functional characterization of the adhesion molecule
RT   spermatogenic immunoglobulin superfamily in the mouse testis.";
RL   Biol. Reprod. 68:1755-1763(2003).
RN   [9]
RP   FUNCTION.
RX   PubMed=15158462; DOI=10.1016/j.bbrc.2004.04.172;
RA   Ito A., Koma Y., Watabe K., Jippo T., Wakayama T., Iseki S.,
RA   Kitamura Y.;
RT   "Contribution of the SgIGSF adhesion molecule to survival of cultured
RT   mast cells in vivo.";
RL   Biochem. Biophys. Res. Commun. 319:200-206(2004).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH CADM1.
RX   PubMed=15811952; DOI=10.1182/blood-2005-02-0817;
RA   Boles K.S., Barchet W., Diacovo T., Cella M., Colonna M.;
RT   "The tumor suppressor TSLC1/NECL-2 triggers NK-cell and CD8+ T-cell
RT   responses through the cell-surface receptor CRTAM.";
RL   Blood 106:779-786(2005).
RN   [11]
RP   FUNCTION.
RX   PubMed=15707673; DOI=10.1016/j.devbrainres.2004.10.015;
RA   Fujita E., Urase K., Soyama A., Kouroku Y., Momoi T.;
RT   "Distribution of RA175/TSLC1/SynCAM, a member of the immunoglobulin
RT   superfamily, in the developing nervous system.";
RL   Brain Res. Dev. Brain Res. 154:199-209(2005).
RN   [12]
RP   INTERACTION WITH CRTAM.
RX   PubMed=15781451; DOI=10.1074/jbc.M502095200;
RA   Galibert L., Diemer G.S., Liu Z., Johnson R.S., Smith J.L., Walzer T.,
RA   Comeau M.R., Rauch C.T., Wolfson M.F., Sorensen R.A.,
RA   Van der Vuurst de Vries A.-R., Branstetter D.G., Koelling R.M.,
RA   Scholler J., Fanslow W.C., Baum P.R., Derry J.M., Yan W.;
RT   "Nectin-like protein 2 defines a subset of T-cell zone dendritic cells
RT   and is a ligand for class-I-restricted T-cell-associated molecule.";
RL   J. Biol. Chem. 280:21955-21964(2005).
RN   [13]
RP   FUNCTION.
RX   PubMed=16605125;
RA   Kitamura Y.;
RT   "MITF and SgIGSF: an essential transcription factor and its target
RT   adhesion molecule for development and survival of mast cells.";
RL   Novartis Found. Symp. 271:4-11(2005).
RN   [14]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=16382161; DOI=10.1128/MCB.26.2.718-726.2006;
RA   Fujita E., Kouroku Y., Ozeki S., Tanabe Y., Toyama Y., Maekawa M.,
RA   Kojima N., Senoo H., Toshimori K., Momoi T.;
RT   "Oligo-astheno-teratozoospermia in mice lacking
RT   RA175/TSLC1/SynCAM/IGSF4A, a cell adhesion molecule in the
RT   immunoglobulin superfamily.";
RL   Mol. Cell. Biol. 26:718-726(2006).
RN   [15]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=16611999; DOI=10.1128/MCB.26.9.3595-3609.2006;
RA   van der Weyden L., Arends M.J., Chausiaux O.E., Ellis P.J.,
RA   Lange U.C., Surani M.A., Affara N., Murakami Y., Adams D.J.,
RA   Bradley A.;
RT   "Loss of TSLC1 causes male infertility due to a defect at the
RT   spermatid stage of spermatogenesis.";
RL   Mol. Cell. Biol. 26:3595-3609(2006).
RN   [16]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16612000; DOI=10.1128/MCB.26.9.3610-3624.2006;
RA   Yamada D., Yoshida M., Williams Y.N., Fukami T., Kikuchi S.,
RA   Masuda M., Maruyama T., Ohta T., Nakae D., Maekawa A., Kitamura T.,
RA   Murakami Y.;
RT   "Disruption of spermatogenic cell adhesion and male infertility in
RT   mice lacking TSLC1/IGSF4, an immunoglobulin superfamily cell adhesion
RT   molecule.";
RL   Mol. Cell. Biol. 26:3610-3624(2006).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [18]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-104 AND ASN-116, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [19]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70; ASN-104; ASN-116;
RP   ASN-168; ASN-304; ASN-307 AND ASN-311, AND MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Mediates homophilic cell-cell adhesion in a Ca(2+)-
CC       independent manner. Also mediates heterophilic cell-cell adhesion
CC       with CADM3 and PVRL3 in a Ca(2+)-independent manner. Acts as a
CC       tumor suppressor in non-small-cell lung cancer (NSCLC) cells.
CC       Interaction with CRTAM promotes natural killer (NK) cell
CC       cytotoxicity and interferon-gamma (IFN-gamma) secretion by CD8+
CC       cells in vitro as well as NK cell-mediated rejection of tumors
CC       expressing CADM3 in vivo. May contribute to the less invasive
CC       phenotypes of lepidic growth tumor cells. In mast cells, may
CC       mediate attachment to and promote communication with nerves.
CC       CADM1, together with MITF, is essential for development and
CC       survival of mast cells in vivo. May act as a synaptic cell
CC       adhesion molecule that drives synapse assembly. May be involved in
CC       neuronal migration, axon growth, pathfinding, and fasciculation on
CC       the axons of differentiating neurons. May play diverse roles in
CC       the spermatogenesis including in the adhesion of spermatocytes and
CC       spermatids to Sertoli cells and for their normal differentiation
CC       into mature spermatozoa.
CC   -!- SUBUNIT: Homodimer. Interacts with CRTAM and EPB41L3/DAL1. The
CC       interaction with EPB41L3/DAL1 may act to anchor CADM1 to the actin
CC       cytoskeleton. Interacts via its C-terminus with the PDZ domain of
CC       MPP3 and the PDZ domain of MPP6.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Note=Associates with perinuclear and plasma membranes in
CC       vivo. Localized to the basolateral plasma membrane of epithelial
CC       cells in gall bladder.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=1;
CC         IsoId=Q8R5M8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8R5M8-2; Sequence=VSP_052470;
CC       Name=3;
CC         IsoId=Q8R5M8-3; Sequence=VSP_052466;
CC       Name=4;
CC         IsoId=Q8R5M8-4; Sequence=VSP_052465;
CC       Name=5;
CC         IsoId=Q8R5M8-5; Sequence=VSP_052464, VSP_052468;
CC       Name=6;
CC         IsoId=Q8R5M8-6; Sequence=VSP_052463, VSP_052469;
CC       Name=7;
CC         IsoId=Q8R5M8-7; Sequence=VSP_052463, VSP_052467;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, lung, kidney, testis,
CC       heart, spleen and liver, but not expressed in skeletal muscle. In
CC       brain, enriched in the synaptic plasma membrane. Expressed
CC       dominantly in epithelial cells but not expressed in fibroblast
CC       cells (at protein level).
CC   -!- DEVELOPMENTAL STAGE: Expressed in spermatogenic cells during early
CC       spermatogenesis. Expression increases in intermediate
CC       spermatogonia through to zygotene spermatocytes but becomes
CC       diminished in the steps from early pachytene spermatocytes through
CC       to round spermatids. After meiosis, expression reappears in
CC       spermatids and is present in elongating spermatids until
CC       spermiation. Not detected in Sertoli cells.
CC   -!- DOMAIN: The cytoplasmic domain appears to play a critical role in
CC       proapoptosis and tumor suppressor activity in NSCLC (By
CC       similarity).
CC   -!- PTM: N-glycosylated.
CC   -!- DISRUPTION PHENOTYPE: Male mice are infertile, due to a defect at
CC       the spermatid stage of spermatogenesis, and show
CC       oligoasthenoteratozoospermia with almost no mature motile
CC       spermatozoa in the epididymis. Heterozygous males and females and
CC       homozygous null females are fertile and have no overt
CC       developmental defects.
CC   -!- SIMILARITY: Belongs to the nectin family.
CC   -!- SIMILARITY: Contains 2 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC       domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC67243.1; Type=Frameshift; Positions=65;
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DR   EMBL; AF434663; AAL86736.1; -; mRNA.
DR   EMBL; AF539424; AAN01614.1; -; mRNA.
DR   EMBL; AB021964; BAA87914.1; -; mRNA.
DR   EMBL; AB021965; BAA87915.1; -; mRNA.
DR   EMBL; AB064265; BAB83501.2; -; mRNA.
DR   EMBL; AY351388; AAQ02381.1; -; mRNA.
DR   EMBL; AF061260; AAC67243.1; ALT_FRAME; mRNA.
DR   EMBL; AB092414; BAC66173.1; -; mRNA.
DR   EMBL; AB183399; BAD30018.1; -; mRNA.
DR   EMBL; AB183400; BAD30019.1; -; mRNA.
DR   EMBL; AB183401; BAD30020.1; -; mRNA.
DR   EMBL; AB183402; BAD30021.1; -; mRNA.
DR   IPI; IPI00322447; -.
DR   IPI; IPI00410985; -.
DR   IPI; IPI00411088; -.
DR   IPI; IPI00461967; -.
DR   IPI; IPI00849429; -.
DR   IPI; IPI00849618; -.
DR   IPI; IPI00849722; -.
DR   RefSeq; NP_001020771.1; NM_001025600.1.
DR   RefSeq; NP_061240.3; NM_018770.3.
DR   RefSeq; NP_997558.2; NM_207675.2.
DR   RefSeq; NP_997559.1; NM_207676.2.
DR   UniGene; Mm.234832; -.
DR   HSSP; Q8IZQ9; 1Z9M.
DR   ProteinModelPortal; Q8R5M8; -.
DR   SMR; Q8R5M8; 47-385, 417-443.
DR   STRING; Q8R5M8; -.
DR   PhosphoSite; Q8R5M8; -.
DR   PRIDE; Q8R5M8; -.
DR   Ensembl; ENSMUST00000034581; ENSMUSP00000034581; ENSMUSG00000032076.
DR   Ensembl; ENSMUST00000085909; ENSMUSP00000083073; ENSMUSG00000032076.
DR   Ensembl; ENSMUST00000114542; ENSMUSP00000110189; ENSMUSG00000032076.
DR   Ensembl; ENSMUST00000114547; ENSMUSP00000110194; ENSMUSG00000032076.
DR   GeneID; 54725; -.
DR   KEGG; mmu:54725; -.
DR   NMPDR; fig|10090.3.peg.20127; -.
DR   UCSC; uc009php.1; mouse.
DR   CTD; 54725; -.
DR   MGI; MGI:1889272; Cadm1.
DR   eggNOG; roNOG11631; -.
DR   GeneTree; ENSGT00600000084002; -.
DR   HOVERGEN; HBG057086; -.
DR   InParanoid; Q8R5M8; -.
DR   PhylomeDB; Q8R5M8; -.
DR   NextBio; 311582; -.
DR   ArrayExpress; Q8R5M8; -.
DR   Bgee; Q8R5M8; -.
DR   CleanEx; MM_CADM1; -.
DR   Genevestigator; Q8R5M8; -.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR   GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0016338; P:calcium-independent cell-cell adhesion; IDA:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0008037; P:cell recognition; IDA:UniProtKB.
DR   GO; GO:0051606; P:detection of stimulus; IDA:UniProtKB.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion; IDA:UniProtKB.
DR   GO; GO:0007156; P:homophilic cell adhesion; IDA:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0042271; P:susceptibility to natural killer cell mediated cytotoxicity; IDA:UniProtKB.
DR   GO; GO:0007416; P:synapse assembly; IDA:MGI.
DR   GO; GO:0009826; P:unidimensional cell growth; IMP:MGI.
DR   InterPro; IPR013162; CD80_C2-set.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR003585; Neurexin-like.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3.
DR   Pfam; PF08205; C2-set_2; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00294; 4.1m; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   PROSITE; PS50835; IG_LIKE; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Cell adhesion; Cell membrane;
KW   Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW   Immunity; Immunoglobulin domain; Membrane; Phosphoprotein; Repeat;
KW   Signal; Spermatogenesis; Transmembrane; Transmembrane helix;
KW   Tumor suppressor.
FT   SIGNAL        1     47       Potential.
FT   CHAIN        48    456       Cell adhesion molecule 1.
FT                                /FTId=PRO_0000291969.
FT   TOPO_DOM     48    388       Extracellular (Potential).
FT   TRANSMEM    389    409       Helical; (Potential).
FT   TOPO_DOM    410    456       Cytoplasmic (Potential).
FT   DOMAIN       48    142       Ig-like V-type.
FT   DOMAIN      147    241       Ig-like C2-type 1.
FT   DOMAIN      246    332       Ig-like C2-type 2.
FT   MOD_RES     448    448       Phosphoserine.
FT   CARBOHYD     70     70       N-linked (GlcNAc...).
FT   CARBOHYD    104    104       N-linked (GlcNAc...).
FT   CARBOHYD    116    116       N-linked (GlcNAc...).
FT   CARBOHYD    168    168       N-linked (GlcNAc...).
FT   CARBOHYD    304    304       N-linked (GlcNAc...).
FT   CARBOHYD    307    307       N-linked (GlcNAc...).
FT   CARBOHYD    311    311       N-linked (GlcNAc...).
FT   DISULFID     67    127       By similarity.
FT   DISULFID    169    223       By similarity.
FT   DISULFID    270    316       By similarity.
FT   VAR_SEQ       1    150       Missing (in isoform 6 and isoform 7).
FT                                /FTId=VSP_052463.
FT   VAR_SEQ     335    336       DP -> GT (in isoform 5).
FT                                /FTId=VSP_052464.
FT   VAR_SEQ     336    374       Missing (in isoform 4).
FT                                /FTId=VSP_052465.
FT   VAR_SEQ     336    363       Missing (in isoform 3).
FT                                /FTId=VSP_052466.
FT   VAR_SEQ     336    352       Missing (in isoform 7).
FT                                /FTId=VSP_052467.
FT   VAR_SEQ     337    456       Missing (in isoform 5).
FT                                /FTId=VSP_052468.
FT   VAR_SEQ     355    365       Missing (in isoform 6).
FT                                /FTId=VSP_052469.
FT   VAR_SEQ     364    374       Missing (in isoform 2).
FT                                /FTId=VSP_052470.
FT   CONFLICT      8      8       S -> C (in Ref. 2; AAN01614 and 7;
FT                                BAD30018).
FT   CONFLICT    266    266       F -> L (in Ref. 3; BAA87914/BAA87915).
FT   CONFLICT    315    315       R -> P (in Ref. 3; BAA87914/BAA87915).
FT   CONFLICT    330    330       M -> I (in Ref. 3; BAA87914/BAA87915).
FT   CONFLICT    356    356       T -> S (in Ref. 2; AAN01614 and 7;
FT                                BAD30018).
FT   CONFLICT    429    429       D -> N (in Ref. 3; BAB83501).
SQ   SEQUENCE   456 AA;  49788 MW;  3226E86C04161C7F CRC64;
     MASAVLPSGS QCAAAAAVAA AAAPPGLRLR LLLLLLSAAA LIPTGDGQNL FTKDVTVIEG
     EVATISCQVN KSDDSVIQLL NPNRQTIYFR DFRPLKDSRF QLLNFSSSEL KVSLTNVSIS
     DEGRYFCQLY TDPPQESYTT ITVLVPPRNL MIDIQKDTAV EGEEIEVNCT AMASKPATTI
     RWFKGNKELK GKSEVEEWSD MYTVTSQLML KVHKEDDGVP VICQVEHPAV TGNLQTQRYL
     EVQYKPQVHI QMTYPLQGLT REGDAFELTC EAIGKPQPVM VTWVRVDDEM PQHAVLSGPN
     LFINNLNKTD NGTYRCEASN IVGKAHSDYM LYVYDPPTTI PPPTTTTTTT TTTTTTILTI
     ITDTTATTEP AVHDSRAGEE GTIGAVDHAV IGGVVAVVVF AMLCLLIILG RYFARHKGTY
     FTHEAKGADD AADADTAIIN AEGGQNNSEE KKEYFI
//
ID   TMX1_MOUSE              Reviewed;         278 AA.
AC   Q8VBT0; Q3UCI8; Q9CSD5;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Thioredoxin-related transmembrane protein 1;
DE   AltName: Full=Thioredoxin domain-containing protein 1;
DE   Flags: Precursor;
GN   Name=Tmx1; Synonyms=Txndc, Txndc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Embryo, Pancreatic islet, and Pituitary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Mammary gland, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: May participate in various redox reactions through the
CC       reversible oxidation of its active center dithiol to a disulfide
CC       and catalyze dithiol-disulfide exchange reactions.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential). Endoplasmic reticulum membrane; Single-pass
CC       type I membrane protein (Potential). Note=Predominantly found in
CC       the endoplasmic reticulum (By similarity).
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK013150; BAB28680.3; -; mRNA.
DR   EMBL; AK030429; BAC26960.1; -; mRNA.
DR   EMBL; AK050567; BAC34326.1; -; mRNA.
DR   EMBL; AK137059; BAE23223.1; -; mRNA.
DR   EMBL; AK150511; BAE29624.1; -; mRNA.
DR   EMBL; AK153027; BAE31660.1; -; mRNA.
DR   EMBL; AK170468; BAE41816.1; -; mRNA.
DR   EMBL; BC017603; AAH17603.1; -; mRNA.
DR   EMBL; BC021533; AAH21533.1; -; mRNA.
DR   IPI; IPI00121341; -.
DR   RefSeq; NP_082615.1; NM_028339.1.
DR   UniGene; Mm.479585; -.
DR   ProteinModelPortal; Q8VBT0; -.
DR   SMR; Q8VBT0; 23-146.
DR   PhosphoSite; Q8VBT0; -.
DR   PRIDE; Q8VBT0; -.
DR   Ensembl; ENSMUST00000021471; ENSMUSP00000021471; ENSMUSG00000021072.
DR   GeneID; 72736; -.
DR   KEGG; mmu:72736; -.
DR   UCSC; uc007ntu.1; mouse.
DR   CTD; 72736; -.
DR   MGI; MGI:1919986; Tmx1.
DR   eggNOG; roNOG10947; -.
DR   GeneTree; ENSGT00390000011580; -.
DR   InParanoid; Q8VBT0; -.
DR   OMA; LLWGAPW; -.
DR   OrthoDB; EOG4KSPKM; -.
DR   PhylomeDB; Q8VBT0; -.
DR   NextBio; 336838; -.
DR   ArrayExpress; Q8VBT0; -.
DR   Bgee; Q8VBT0; -.
DR   CleanEx; MM_TXNDC1; -.
DR   Genevestigator; Q8VBT0; -.
DR   GermOnline; ENSMUSG00000021072; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR017936; Thioredoxin-like.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Electron transport; Endoplasmic reticulum; Membrane;
KW   Phosphoprotein; Redox-active center; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     26       Potential.
FT   CHAIN        27    278       Thioredoxin-related transmembrane protein
FT                                1.
FT                                /FTId=PRO_0000034154.
FT   TOPO_DOM     27    181       Extracellular (Potential).
FT   TRANSMEM    182    202       Helical; (Potential).
FT   TOPO_DOM    203    278       Cytoplasmic (Potential).
FT   DOMAIN       27    132       Thioredoxin.
FT   MOD_RES     245    245       Phosphoserine.
FT   MOD_RES     256    256       Phosphoserine.
FT   MOD_RES     278    278       Phosphoserine (By similarity).
FT   DISULFID     56     59       Redox-active (By similarity).
SQ   SEQUENCE   278 AA;  31396 MW;  EB682243008E3333 CRC64;
     MAHLGRLMVP LAALVLLLWA VPGAHGRRNN VRVLTDENWT SLLEGEWMIE FYAPWCPACQ
     NLQPEWESFA EWGEDLEVKV AKVDVTEQTG LSGRFIITAL PSIYHCKDGE FRRYVGPRTK
     KDFINFVSDK EWKNIEPISS WFGPSSVLMT MMSALFQLSV YIRTSHSYFV HDLGIPAWGS
     YLVFAFATVL SGLLLGLCMI FVADCLCPSK RRKPQQQYAK KTSPEFSQPL KKVEEEQEAD
     EEDVSEEEAE DREGASKATS QSSIRQRCVG LPSATDTS
//
ID   ASPC1_MOUSE             Reviewed;         550 AA.
AC   Q8VBT9; A2ABZ7; A2AC06; Q3UKD1; Q6V7K5; Q9CT64;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Tether containing UBX domain for GLUT4;
DE   AltName: Full=Alveolar soft part sarcoma chromosomal region candidate gene 1 protein homolog;
GN   Name=Aspscr1; Synonyms=Tug;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION
RP   WITH GLUT4, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Liver, and Muscle;
RX   MEDLINE=22923964; PubMed=14562105; DOI=10.1038/nature01989;
RA   Bogan J.S., Hendon N., McKee A.E., Tsao T.-S., Lodish H.F.;
RT   "Functional cloning of TUG as a regulator of GLUT4 glucose transporter
RT   trafficking.";
RL   Nature 425:727-733(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Liver, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   STRUCTURE BY NMR OF 1-90.
RX   PubMed=16501224; DOI=10.1110/ps.051901806;
RA   Tettamanzi M.C., Yu C., Bogan J.S., Hodsdon M.E.;
RT   "Solution structure and backbone dynamics of an N-terminal ubiquitin-
RT   like domain in the GLUT4-regulating protein, TUG.";
RL   Protein Sci. 15:498-508(2006).
CC   -!- FUNCTION: Tethering protein that sequesters GLUT4-containing
CC       vesicles in the cytoplasm in the absence of insulin. Modulates the
CC       amount of GLUT4 that is available at the cell surface.
CC   -!- SUBUNIT: Interacts with GLUT4.
CC   -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Long;
CC         IsoId=Q8VBT9-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short;
CC         IsoId=Q8VBT9-2; Sequence=VSP_020579;
CC       Name=3;
CC         IsoId=Q8VBT9-3; Sequence=VSP_020579, VSP_020580;
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Contains 1 UBX domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY349132; AAR01613.1; -; mRNA.
DR   EMBL; AY349133; AAR01614.1; -; mRNA.
DR   EMBL; AK004509; BAB23341.1; -; mRNA.
DR   EMBL; AK146061; BAE26870.1; -; mRNA.
DR   EMBL; AL663030; CAM27105.1; -; Genomic_DNA.
DR   EMBL; AL663030; CAM27114.1; -; Genomic_DNA.
DR   EMBL; BC019177; AAH19177.1; -; mRNA.
DR   EMBL; BC022115; AAH22115.1; -; mRNA.
DR   EMBL; BC031153; AAH31153.1; -; mRNA.
DR   IPI; IPI00121364; -.
DR   IPI; IPI00381046; -.
DR   IPI; IPI00648116; -.
DR   RefSeq; NP_001157696.1; NM_001164224.1.
DR   RefSeq; NP_081153.1; NM_026877.2.
DR   RefSeq; NP_937866.1; NM_198223.2.
DR   UniGene; Mm.294020; -.
DR   PDB; 2AL3; NMR; -; A=1-90.
DR   PDBsum; 2AL3; -.
DR   ProteinModelPortal; Q8VBT9; -.
DR   SMR; Q8VBT9; 10-85, 386-457.
DR   STRING; Q8VBT9; -.
DR   PhosphoSite; Q8VBT9; -.
DR   REPRODUCTION-2DPAGE; Q8VBT9; -.
DR   PRIDE; Q8VBT9; -.
DR   Ensembl; ENSMUST00000026135; ENSMUSP00000026135; ENSMUSG00000025142.
DR   Ensembl; ENSMUST00000106158; ENSMUSP00000101764; ENSMUSG00000025142.
DR   Ensembl; ENSMUST00000106159; ENSMUSP00000101765; ENSMUSG00000025142.
DR   GeneID; 68938; -.
DR   KEGG; mmu:68938; -.
DR   UCSC; uc007mua.1; mouse.
DR   UCSC; uc007mub.1; mouse.
DR   CTD; 68938; -.
DR   MGI; MGI:1916188; Aspscr1.
DR   GeneTree; ENSGT00510000048362; -.
DR   HOGENOM; HBG714367; -.
DR   HOVERGEN; HBG066860; -.
DR   InParanoid; Q8VBT9; -.
DR   OMA; YLFITPP; -.
DR   OrthoDB; EOG49W2FN; -.
DR   PhylomeDB; Q8VBT9; -.
DR   NextBio; 328221; -.
DR   ArrayExpress; Q8VBT9; -.
DR   Bgee; Q8VBT9; -.
DR   Genevestigator; Q8VBT9; -.
DR   GermOnline; ENSMUSG00000025142; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0019898; C:extrinsic to membrane; IDA:MGI.
DR   GO; GO:0009898; C:internal side of plasma membrane; IDA:MGI.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR   GO; GO:0000300; C:peripheral to membrane of membrane fraction; IDA:MGI.
DR   GO; GO:0012506; C:vesicle membrane; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; IDA:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; IDA:MGI.
DR   GO; GO:0046324; P:regulation of glucose import; IDA:MGI.
DR   InterPro; IPR021569; TUG.
DR   InterPro; IPR001012; UBX.
DR   Pfam; PF11470; TUG; 1.
DR   Pfam; PF00789; UBX; 1.
DR   SMART; SM00166; UBX; 1.
DR   PROSITE; PS50033; UBX; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Membrane;
KW   Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    550       Tether containing UBX domain for GLUT4.
FT                                /FTId=PRO_0000249886.
FT   DOMAIN      382    458       UBX.
FT   REGION      313    376       Interaction with GLUT4.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     278    278       Phosphothreonine (By similarity).
FT   MOD_RES     279    279       Phosphoserine (By similarity).
FT   MOD_RES     496    496       Phosphoserine (By similarity).
FT   VAR_SEQ       1     77       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_020579.
FT   VAR_SEQ     410    430       Missing (in isoform 3).
FT                                /FTId=VSP_020580.
FT   STRAND       12     15
FT   STRAND       21     24
FT   HELIX        32     42
FT   HELIX        47     49
FT   STRAND       51     54
FT   STRAND       57     62
FT   HELIX        65     68
FT   STRAND       75     79
FT   STRAND       81     83
SQ   SEQUENCE   550 AA;  59796 MW;  CC2EB6F7BD43E113 CRC64;
     MAAPAGGGGS AVSVLAPNGR RHTVKVTPST VLLQVLEDTC RRQDFNPSEY DLKFQRTVLD
     LSLQWRFANL PNNAKLEMVP VSRSREGPEN IVRIAFQLDD GSRLQDAFCS RQTLWELLSH
     FAQTRERLQQ LGEKTPVCVY MRNEVTGRAA LQNTTLQSLG LTGGSATIRF VIKQCDTAGK
     QESIAVRSKA PGSPVSSLSA DQASSSTLLP LNSGEFSRGD LNHEGDANTS GTGLEGGPKP
     TDAQTKQSTS EPASAPFVPF SGGGQRLGGP SASLRPLTSP SANSSKSFSG PGGPSKPKKP
     KPGEEPQQEP EPPVDRDPVV YHPDLEDLLQ PWPAEVPDEF FEVTVDDVRR RLAQLKSERK
     RLEEAPLVTK AFREAQMKEK LERYPKVALR VLFPDRYILQ GFFRPSETVG DLRDFVRSHL
     GNPELSFYLF IAPPKMVLDD HTLTLFQANL FPAALVHFGA EEPTGLYLEP GLLEHTVSPS
     TADVLVARCM SRASGSPPLL PAPDPVSLES EPIAEDGALG PPEPIQGTAQ PVKRSLGKVP
     KWLKLPASKR
//
ID   Q8VBU5_MOUSE            Unreviewed;       721 AA.
AC   Q8VBU5;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   11-JAN-2011, entry version 64.
DE   SubName: Full=Phosphodiesterase 4B;
DE   SubName: Full=Phosphodiesterase 4B, cAMP specific;
GN   Name=Pde4b; ORFNames=RP23-57D24.1-001, mCG_113038;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DBA/2J, and C57BL/6J; TISSUE=Whole brain;
RX   MEDLINE=21975488; PubMed=11978849;
RA   Fehr C., Shirley R.L., Belknap J.K., Crabbe J.C., Buck K.J.;
RT   "Congenic mapping of alcohol and pentobarbital withdrawal liability
RT   loci to a <1 centimorgan interval of murine chromosome 4:
RT   identification of Mpdz as a candidate gene.";
RL   J. Neurosci. 22:3730-3738(2002).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RA   Harrison E.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RA   Wallis J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RA   Hall R.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AF326555; AAL37401.1; -; mRNA.
DR   EMBL; AF326556; AAL37402.1; -; mRNA.
DR   EMBL; AL732551; CAM19397.1; -; Genomic_DNA.
DR   EMBL; AL772293; CAM19397.1; JOINED; Genomic_DNA.
DR   EMBL; AL772358; CAM19397.1; JOINED; Genomic_DNA.
DR   EMBL; AL772358; CAM23238.1; -; Genomic_DNA.
DR   EMBL; AL732551; CAM23238.1; JOINED; Genomic_DNA.
DR   EMBL; AL772293; CAM23238.1; JOINED; Genomic_DNA.
DR   EMBL; AL772293; CAM26138.1; -; Genomic_DNA.
DR   EMBL; AL732551; CAM26138.1; JOINED; Genomic_DNA.
DR   EMBL; AL772358; CAM26138.1; JOINED; Genomic_DNA.
DR   EMBL; CH466527; EDL30857.1; -; Genomic_DNA.
DR   IPI; IPI00276327; -.
DR   RefSeq; NP_001171451.1; NM_001177980.1.
DR   RefSeq; NP_062814.2; NM_019840.2.
DR   UniGene; Mm.20181; -.
DR   HSSP; Q07343; 1F0J.
DR   ProteinModelPortal; Q8VBU5; -.
DR   SMR; Q8VBU5; 309-670.
DR   STRING; Q8VBU5; -.
DR   PhosphoSite; Q8VBU5; -.
DR   PRIDE; Q8VBU5; -.
DR   Ensembl; ENSMUST00000106908; ENSMUSP00000102521; ENSMUSG00000028525.
DR   GeneID; 18578; -.
DR   KEGG; mmu:18578; -.
DR   UCSC; uc008twj.1; mouse.
DR   CTD; 18578; -.
DR   MGI; MGI:99557; Pde4b.
DR   HOVERGEN; HBG108239; -.
DR   OMA; GEGHNYF; -.
DR   PhylomeDB; Q8VBU5; -.
DR   NextBio; 294444; -.
DR   ArrayExpress; Q8VBU5; -.
DR   Bgee; Q8VBU5; -.
DR   Genevestigator; Q8VBU5; -.
DR   GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR003607; Metal-dep_PHydrolase_HD_dom.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR023174; PDEase_CS.
DR   Gene3D; G3DSA:1.10.1300.10; PDEase_catalytic_dom; 1.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00471; HDc; 1.
DR   PROSITE; PS00126; PDEASE_I; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Metal-binding.
SQ   SEQUENCE   721 AA;  82075 MW;  B3725A478A7612FB CRC64;
     MTAKNSPKEF TASESEVCIK TFKEQMRLEL ELPKLPGNRP TSPKISPRSS PRNSPCFFRK
     LLVNKSIRQR RRFTVAHTCF DVENGPSPGR SPLDPQAGSS SGLVLHAAFP GHSQRRESFL
     YRSDSDYDLS PKAMSRNSSL PSEQHGDDLI VTPFAQVLAS LRSVRNNFTL LTNLHGAPNK
     RSPAASQAPV SRVSLQEESY QKLAMETLEE LDWCLDQLET IQTYRSVSEM ASNKFKRMLN
     RELTHLSEMS RSGNQVSEYI SNTFLDKQND VEIPSPTQKD REKKKKQQLM TQISGVKKLM
     HSSSLNNTSI SRFGVNTENE DHLAKELEDL NKWGLNIFNV AGYSHNRPLT CIMYAIFQER
     DLLKTFKISS DTFVTYMMTL EDHYHSDVAY HNSLHAADVA QSTHVLLSTP ALDAVFTDLE
     ILAAIFAAAI HDVDHPGVSN QFLINTNSEL ALMYNDESVL ENHHLAVGFK LLQEEHCDIF
     QNLTKKQRQT LRKMVIDMVL ATDMSKHMSL LADLKTMVET KKVTSSGVLL LDNYTDRIQV
     LRNMVHCADL SNPTKSLELY RQWTDRIMEE FFQQGDKERE RGMEISPMCD KHTASVEKSQ
     VGFIDYIVHP LWETWADLVQ PDAQDILDTL EDNRNWYQSM IPQSPSPPLD ERSRDCQGLM
     EKFQFELTLE EEDSEGPEKE GEGHSYFSST KTLCVIDPEN RDSLEETDID IATEDKSPID
     T
//
ID   SC6A8_MOUSE             Reviewed;         640 AA.
AC   Q8VBW1; A2ALM4; Q80YC9; Q8K4R3; Q8R1L0;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Sodium- and chloride-dependent creatine transporter 1;
DE            Short=CT1;
DE            Short=Creatine transporter 1;
DE   AltName: Full=Solute carrier family 6 member 8;
GN   Name=Slc6a8; Synonyms=Crt;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   PubMed=12439290; DOI=10.1097/00004647-200211000-00006;
RA   Ohtsuki S., Tachikawa M., Takanaga H., Shimizu H., Watanabe M.,
RA   Hosoya K., Terasaki T.;
RT   "The blood-brain barrier creatine transporter is a major pathway for
RT   supplying creatine to the brain.";
RL   J. Cereb. Blood Flow Metab. 22:1327-1335(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 1).
RA   Liu Q.-R., Li Q.-F.;
RT   "Cloning and expression of mouse creatine transporter gene.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-640 (ISOFORMS 2 AND 3).
RC   STRAIN=FVB/N; TISSUE=Embryo, and Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Required for the uptake of creatine. Plays an important
CC       role in supplying creatine to the brain via the blood-brain
CC       barrier.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8VBW1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VBW1-2; Sequence=VSP_012133;
CC       Name=3;
CC         IsoId=Q8VBW1-3; Sequence=VSP_012132;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF)
CC       (TC 2.A.22) family. SLC6A8 subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; AB077327; BAC11857.1; -; mRNA.
DR   EMBL; AF459435; AAL66354.1; -; mRNA.
DR   EMBL; AF459436; AAL66355.1; -; Genomic_DNA.
DR   EMBL; AL805924; CAM21057.1; -; Genomic_DNA.
DR   EMBL; BC024444; AAH24444.1; -; mRNA.
DR   EMBL; BC049801; AAH49801.1; -; mRNA.
DR   IPI; IPI00121477; -.
DR   IPI; IPI00480326; -.
DR   IPI; IPI00480478; -.
DR   RefSeq; NP_001136281.1; NM_001142809.1.
DR   RefSeq; NP_001136282.1; NM_001142810.1.
DR   RefSeq; NP_598748.1; NM_133987.2.
DR   UniGene; Mm.274553; -.
DR   ProteinModelPortal; Q8VBW1; -.
DR   STRING; Q8VBW1; -.
DR   PhosphoSite; Q8VBW1; -.
DR   PRIDE; Q8VBW1; -.
DR   Ensembl; ENSMUST00000033752; ENSMUSP00000033752; ENSMUSG00000019558.
DR   GeneID; 102857; -.
DR   KEGG; mmu:102857; -.
DR   UCSC; uc009tmf.1; mouse.
DR   UCSC; uc009tmg.1; mouse.
DR   UCSC; uc009tmh.1; mouse.
DR   CTD; 102857; -.
DR   MGI; MGI:2147834; Slc6a8.
DR   GeneTree; ENSGT00560000076839; -.
DR   HOGENOM; HBG702834; -.
DR   HOVERGEN; HBG071421; -.
DR   InParanoid; Q8VBW1; -.
DR   OMA; PPRETWT; -.
DR   OrthoDB; EOG4M3984; -.
DR   PhylomeDB; Q8VBW1; -.
DR   NextBio; 355683; -.
DR   ArrayExpress; Q8VBW1; -.
DR   Bgee; Q8VBW1; -.
DR   Genevestigator; Q8VBW1; -.
DR   GermOnline; ENSMUSG00000019558; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; IEA:InterPro.
DR   GO; GO:0005328; F:neurotransmitter:sodium symporter activity; IEA:InterPro.
DR   InterPro; IPR000175; Na/ntran_symport.
DR   InterPro; IPR002984; Na/ntran_symport_creatine.
DR   PANTHER; PTHR11616; Na/ntran_symport; 1.
DR   Pfam; PF00209; SNF; 1.
DR   PRINTS; PR01199; CRTTRANSPORT.
DR   PRINTS; PR00176; NANEUSMPORT.
DR   PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR   PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
DR   PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Ion transport; Membrane;
KW   Phosphoprotein; Sodium; Sodium transport; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    640       Sodium- and chloride-dependent creatine
FT                                transporter 1.
FT                                /FTId=PRO_0000214775.
FT   TOPO_DOM      1     60       Cytoplasmic (Potential).
FT   TRANSMEM     61     81       Helical; (Potential).
FT   TOPO_DOM     82     87       Extracellular (Potential).
FT   TRANSMEM     88    108       Helical; (Potential).
FT   TOPO_DOM    109    138       Cytoplasmic (Potential).
FT   TRANSMEM    139    159       Helical; (Potential).
FT   TOPO_DOM    160    230       Extracellular (Potential).
FT   TRANSMEM    231    251       Helical; (Potential).
FT   TOPO_DOM    252    269       Cytoplasmic (Potential).
FT   TRANSMEM    270    290       Helical; (Potential).
FT   TOPO_DOM    291    304       Extracellular (Potential).
FT   TRANSMEM    305    325       Helical; (Potential).
FT   TOPO_DOM    326    341       Cytoplasmic (Potential).
FT   TRANSMEM    342    362       Helical; (Potential).
FT   TOPO_DOM    363    394       Extracellular (Potential).
FT   TRANSMEM    395    415       Helical; (Potential).
FT   TOPO_DOM    416    444       Cytoplasmic (Potential).
FT   TRANSMEM    445    470       Helical; (Potential).
FT   TOPO_DOM    471    484       Extracellular (Potential).
FT   TRANSMEM    485    505       Helical; (Potential).
FT   TOPO_DOM    506    525       Cytoplasmic (Potential).
FT   TRANSMEM    526    546       Helical; (Potential).
FT   TOPO_DOM    547    565       Extracellular (Potential).
FT   TRANSMEM    566    586       Helical; (Potential).
FT   TOPO_DOM    587    640       Cytoplasmic (Potential).
FT   MOD_RES     625    625       Phosphothreonine (By similarity).
FT   CARBOHYD    192    192       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    197    197       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    553    553       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     462    469       Missing (in isoform 3).
FT                                /FTId=VSP_012132.
FT   VAR_SEQ     465    469       Missing (in isoform 2).
FT                                /FTId=VSP_012133.
SQ   SEQUENCE   640 AA;  70999 MW;  67D3AAAC591EEA0B CRC64;
     MAKKSAENGI YSVSGDEKKG PLIVSGPDGA PAKGDGPAGL GAPGGRLAVP PRETWTRQMD
     FIMSCVGFAV GLGNVWRFPY LCYKNGGGVF LIPYVLIALV GGIPIFFLEI SLGQFMKAGS
     INVWNICPLF KGLGYASMVI VFYCNTYYIM VLAWGFYYLV KSFTTTLPWA TCGHTWNTPD
     CVEIFRHEDC ANASLANLTC DQLADRRSPV IEFWENKVLR LSTGLEVPGA LNWEVTLCLL
     ACWVLVYFCV WKGVKSTGKI VYFTATFPYV VLVVLLVRGV LLPGALDGII YYLKPDWSKL
     GSPQVWIDAG TQIFFSYAIG LGALTALGSY NRFNNNCYKD AIILALINSG TSFFAGFVVF
     SILGFMATEQ GVHISKVAES GPGLAFIAYP RAVTLMPVAP LWAALFFFML LLLGLDSQFV
     GVEGFITGLL DLLPASYYFR FQREISVALC CALCFVIDLS MVTDVSGGKG GMYVFQLFDY
     YSASGTTLLW QAFWECVVVA WVYGADRFMD DIACMIGYRP CPWMKWCWSF FTPLVCMGIF
     IFNIVYYEPL VYNNTYVYPW WGEAMGWAFA LSSMLCVPLH LLGCLLRAKG TMAERWQHLT
     QPIWGLHHLE YRAQDADVRG LTTLTPVSES SKVVVVESVM
//
ID   BBX_MOUSE               Reviewed;         907 AA.
AC   Q8VBW5; B8JK46; B8JK47; B8JK48; B8JK49; Q3TZK1; Q6NXY8; Q6PEU3;
AC   Q8BQJ7; Q8C7E0; Q8CDQ0; Q8CDV1; Q8VI48; Q8VI49; Q8VI50; Q9CS94;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   08-FEB-2011, entry version 66.
DE   RecName: Full=HMG box transcription factor BBX;
DE   AltName: Full=Bobby sox homolog;
DE   AltName: Full=HMG box-containing protein 2;
GN   Name=Bbx; Synonyms=Hbp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Lee C.-J., Chan W.-I., Appleby V.J., Orme A.T., Scotting P.J.;
RT   "BBX is expressed in developing CNS and in neuronal tumours.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Pancreas, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS
RP   LEU-30 AND HIS-281.
RC   STRAIN=C3H/He, and NMRI;
RC   TISSUE=Mammary gland, Mammary tumor, and Mesenchymal stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-454, AND FUNCTION.
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=11680820; DOI=10.1007/s002940100241;
RA   Sanchez-Diaz A., Blanco M.A., Jones N., Moreno S.;
RT   "HBP2: a new mammalian protein that complements the fission yeast MBF
RT   transcription complex.";
RL   Curr. Genet. 40:110-118(2001).
RN   [6]
RP   STRUCTURE BY NMR OF 80-148.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the HMG-box domain of murine bobby sox
RT   homolog.";
RL   Submitted (AUG-2005) to the PDB data bank.
CC   -!- FUNCTION: Transcription factor that is necessary for cell cycle
CC       progression from G1 to S phase.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=BbxA;
CC         IsoId=Q8VBW5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VBW5-2; Sequence=VSP_018007, VSP_018008, VSP_018009;
CC       Name=3;
CC         IsoId=Q8VBW5-3; Sequence=VSP_018010;
CC       Name=4;
CC         IsoId=Q8VBW5-4; Sequence=VSP_018011, VSP_018012;
CC   -!- SIMILARITY: Contains 1 HMG box DNA-binding domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL68987.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=AAL68988.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF454943; AAL58872.1; -; mRNA.
DR   EMBL; AF454944; AAL58873.1; -; mRNA.
DR   EMBL; AK017487; BAB30768.1; -; mRNA.
DR   EMBL; AK029532; BAC26500.2; -; mRNA.
DR   EMBL; AK029747; BAC26596.1; -; mRNA.
DR   EMBL; AK049516; BAC33788.1; -; mRNA.
DR   EMBL; AK050488; BAC34285.1; -; mRNA.
DR   EMBL; AK157813; BAE34207.1; -; mRNA.
DR   EMBL; CT571273; CAX15928.1; -; Genomic_DNA.
DR   EMBL; AC109627; CAX15928.1; JOINED; Genomic_DNA.
DR   EMBL; CT571273; CAX15929.1; -; Genomic_DNA.
DR   EMBL; AC109627; CAX15929.1; JOINED; Genomic_DNA.
DR   EMBL; CT571273; CAX15930.1; -; Genomic_DNA.
DR   EMBL; AC109627; CAX15930.1; JOINED; Genomic_DNA.
DR   EMBL; CT571273; CAX15931.1; -; Genomic_DNA.
DR   EMBL; AC109627; CAX15931.1; JOINED; Genomic_DNA.
DR   EMBL; BC057869; AAH57869.1; -; mRNA.
DR   EMBL; BC066821; AAH66821.1; -; mRNA.
DR   EMBL; AF276950; AAL68986.1; -; mRNA.
DR   EMBL; AF276951; AAL68987.1; ALT_SEQ; mRNA.
DR   EMBL; AF276952; AAL68988.1; ALT_INIT; mRNA.
DR   IPI; IPI00625898; -.
DR   IPI; IPI00626888; -.
DR   IPI; IPI00757307; -.
DR   IPI; IPI00757891; -.
DR   RefSeq; NP_081720.2; NM_027444.3.
DR   UniGene; Mm.28940; -.
DR   PDB; 1WZ6; NMR; -; A=80-148.
DR   PDBsum; 1WZ6; -.
DR   ProteinModelPortal; Q8VBW5; -.
DR   SMR; Q8VBW5; 80-153.
DR   STRING; Q8VBW5; -.
DR   PhosphoSite; Q8VBW5; -.
DR   PRIDE; Q8VBW5; -.
DR   Ensembl; ENSMUST00000066037; ENSMUSP00000066384; ENSMUSG00000022641.
DR   Ensembl; ENSMUST00000089399; ENSMUSP00000086821; ENSMUSG00000022641.
DR   Ensembl; ENSMUST00000114488; ENSMUSP00000110132; ENSMUSG00000022641.
DR   Ensembl; ENSMUST00000114489; ENSMUSP00000110133; ENSMUSG00000022641.
DR   GeneID; 70508; -.
DR   KEGG; mmu:70508; -.
DR   UCSC; uc007zkn.1; mouse.
DR   UCSC; uc007zkp.1; mouse.
DR   UCSC; uc007zkq.1; mouse.
DR   UCSC; uc007zkr.1; mouse.
DR   CTD; 70508; -.
DR   MGI; MGI:1917758; Bbx.
DR   GeneTree; ENSGT00530000063757; -.
DR   HOVERGEN; HBG079777; -.
DR   InParanoid; Q8VBW5; -.
DR   OMA; AMENVHR; -.
DR   PhylomeDB; Q8VBW5; -.
DR   NextBio; 331763; -.
DR   ArrayExpress; Q8VBW5; -.
DR   Bgee; Q8VBW5; -.
DR   CleanEx; MM_BBX; -.
DR   Genevestigator; Q8VBW5; -.
DR   GermOnline; ENSMUSG00000022641; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR000910; HMG_HMG1/HMG2.
DR   InterPro; IPR009071; HMG_superfamily.
DR   InterPro; IPR019102; TF_HMG_box_BBX_DUF2028.
DR   Gene3D; G3DSA:1.10.30.10; HMG-box; 1.
DR   Pfam; PF09667; DUF2028; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; DNA-binding; Nucleus;
KW   Phosphoprotein; Polymorphism; Transcription; Transcription regulation.
FT   CHAIN         1    907       HMG box transcription factor BBX.
FT                                /FTId=PRO_0000232886.
FT   DNA_BIND     80    148       HMG box.
FT   COMPBIAS     41     50       Poly-Glu.
FT   COMPBIAS    444    540       Lys-rich.
FT   COMPBIAS    715    718       Poly-Lys.
FT   MOD_RES     159    159       Phosphoserine (By similarity).
FT   MOD_RES     161    161       Phosphothreonine (By similarity).
FT   MOD_RES     477    477       Phosphoserine (By similarity).
FT   MOD_RES     483    483       Phosphoserine (By similarity).
FT   MOD_RES     776    776       Phosphothreonine (By similarity).
FT   MOD_RES     789    789       Phosphoserine (By similarity).
FT   MOD_RES     811    811       Phosphoserine (By similarity).
FT   VAR_SEQ      55    135       Missing (in isoform 2).
FT                                /FTId=VSP_018007.
FT   VAR_SEQ     223    249       Missing (in isoform 2).
FT                                /FTId=VSP_018008.
FT   VAR_SEQ     730    730       S -> SKGPFQSQKKNLFHKIVSKYKHKKEKPNVPE (in
FT                                isoform 2).
FT                                /FTId=VSP_018009.
FT   VAR_SEQ     732    751       Missing (in isoform 3).
FT                                /FTId=VSP_018010.
FT   VAR_SEQ     733    750       SGDKWSHKQFFLDAIHPT -> PFQSQKKNLFHKIVSKYK
FT                                (in isoform 4).
FT                                /FTId=VSP_018011.
FT   VAR_SEQ     751    907       Missing (in isoform 4).
FT                                /FTId=VSP_018012.
FT   VARIANT      30     30       P -> L (in strain: C3H/He).
FT   VARIANT     281    281       Q -> H (in strain: C3H/He).
FT   CONFLICT    269    269       L -> F (in Ref. 1; AAL58872/AAL58873 and
FT                                2; BAB30768).
FT   CONFLICT    450    450       K -> R (in Ref. 2; BAC34285).
FT   CONFLICT    455    455       N -> T (in Ref. 1; AAL58872/AAL58873).
FT   HELIX        86    101
FT   STRAND      103    105
FT   HELIX       109    119
FT   HELIX       123    140
SQ   SEQUENCE   907 AA;  100783 MW;  53E113D4B3DE4DAC CRC64;
     MKGSNRNKDH STEGEGDGKR PKRKCLQWHP LLAKKLLDFS EEEEEDEEEE DIDKVQLLEA
     DGLEQDVAET EDDESPEQRA RRPMNAFLLF CKRHRSLVRQ EHPRLDNRGA TKILADWWAV
     LDPKEKQKYT DMAKEYKDAF MKANPGYRWC PTTNKPVKSP TPTVNPRKKL WAFPPDSSRD
     LPTPKKAKTE VPQLNFGMAD PTQMGGLSML LLAGEHALGT PEASSGTCRP DISESPELRQ
     KSPLFQFAEI SSRTSHPDAP SKQCQASALF QFAEISSSTS QLGGTEPVKR CGNSALFQLA
     EMCLASEGVK MEDTKLIKSK ESDGGRIEEI EKGKEERGTE VEKTTETSFQ KEAEFGKSAK
     GNVRESKDLR DIEQLQMDNV MAIKVEDPKE IRKEPEDDQK YSHFPDFSYS ASSKIIISGV
     PSRKDHMCHP HGIMIIEDPT TLNKPEKIKK KKKKNKLDRH GNDKSTPKKT CKKRQSSESD
     IESVMYTIEA VAKGDWGVDK LGETPRKKVR PSSSGKGGIL DAKPPKKKVK SKEKKVSKEK
     CSDITKESRP PDFLSISASK SVPGEVPEGI KAEPLTPTED ALPPSLPGQA KPEDSDCHRK
     TETCGSRKSE RSCKGALYKT LVSEGMLTSL RANVDRGKRS SGKGNSSDHE GCWSEESWTF
     NQSGTSGSKK FKKKLREDSF LGSAKLDEEF EKKFNSLPQY SPITFDRKCV STPRKKKKTG
     NMSSESTKTS KGSGDKWSHK QFFLDAIHPT EAIFSEDKST TEPAFKVKNA LSIPNTPEPT
     TMQEPLVGSQ KRKARKTKIT HLVRTADGRV SPAGGTLDDK PKEQLQRSLP KVPGTYCGDN
     CSHSTVEEPR SSTPDMPAVS AFFSLAALAE VAAMENVHRG QRSTPLTHDG QPKEMPQAPV
     LISCADQ
//
ID   MPDZ_MOUSE              Reviewed;        2055 AA.
AC   Q8VBX6; B7ZNA1; O08783; Q6P7U4; Q80ZY8; Q8BKJ1; Q8C0H8; Q8VBV5;
AC   Q8VBY0; Q9Z1K3;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Multiple PDZ domain protein;
DE   AltName: Full=Multi-PDZ domain protein 1;
GN   Name=Mpdz; Synonyms=Mupp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6 X CBA; TISSUE=Brain;
RX   MEDLINE=99326529; PubMed=10395806; DOI=10.1006/geno.1999.5853;
RA   Simpson E.H., Suffolk R., Jackson I.J.;
RT   "Identification, sequence, and mapping of mouse multiple PDZ domain
RT   protein gene, Mpdz.";
RL   Genomics 59:102-104(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS SER-541; VAL-691;
RP   ARG-801; ALA-859; ASN-880; SER-914; VAL-977; MET-1338; ASN-1433 AND
RP   ASN-1767.
RC   STRAIN=129/J, A/HeJ, AKR/J, BALB/cJ, C3H/J, C57BL/6J, C57BR/cdJ,
RC   C57L/J, CBA/J, CE/J, DBA/2J, DBA1/J, PL/J, SJL/J, SWR/J, WSP1, WSP2,
RC   WSR1, and WSR2; TISSUE=Brain;
RX   MEDLINE=21975488; PubMed=11978849;
RA   Fehr C., Shirley R.L., Belknap J.K., Crabbe J.C., Buck K.J.;
RT   "Congenic mapping of alcohol and pentobarbital withdrawal liability
RT   loci to a <1 centimorgan interval of murine chromosome 4:
RT   identification of Mpdz as a candidate gene.";
RL   J. Neurosci. 22:3730-3738(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1894-2055 (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Brain, Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1532-2055 (ISOFORM 4).
RC   TISSUE=Pancreas;
RX   MEDLINE=97338076; PubMed=9192623; DOI=10.1073/pnas.94.13.6670;
RA   Lee S.S., Weiss R.S., Javier R.T.;
RT   "Binding of human virus oncoproteins to hDlg/SAP97, a mammalian
RT   homolog of the Drosophila discs large tumor suppressor protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:6670-6675(1997).
RN   [7]
RP   INTERACTION WITH KIT, AND TISSUE SPECIFICITY.
RX   MEDLINE=20472558; PubMed=11018522; DOI=10.1016/S0014-5793(00)02036-6;
RA   Mancini A., Koch A., Stefan M., Niemann H., Tamura T.;
RT   "The direct association of the multiple PDZ domain containing proteins
RT   (MUPP-1) with the human c-Kit C-terminus is regulated by tyrosine
RT   kinase activity.";
RL   FEBS Lett. 482:54-58(2000).
RN   [8]
RP   INTERACTION WITH NG2.
RX   PubMed=10967549;
RX   DOI=10.1002/1097-4644(20001101)79:2<213::AID-JCB50>3.0.CO;2-G;
RA   Barritt D.S., Pearn M.T., Zisch A.H., Lee S.S., Javier R.T.,
RA   Pasquale E.B., Stallcup W.B.;
RT   "The multi-PDZ domain protein MUPP1 is a cytoplasmic ligand for the
RT   membrane-spanning proteoglycan NG2.";
RL   J. Cell. Biochem. 79:213-224(2000).
RN   [9]
RP   INTERACTION WITH ADENOVIRUS TYPE 9 E4-ORF1 PROTEIN.
RX   MEDLINE=20457232; PubMed=11000240;
RX   DOI=10.1128/JVI.74.20.9680-9693.2000;
RA   Lee S.S., Glaunsinger B., Mantovani F., Banks L., Javier R.T.;
RT   "Multi-PDZ domain protein MUPP1 is a cellular target for both
RT   adenovirus E4-ORF1 and high-risk papillomavirus type 18 E6
RT   oncoproteins.";
RL   J. Virol. 74:9680-9693(2000).
RN   [10]
RP   INTERACTION WITH CLDN1 AND F11R, DOMAINS, AND SUBCELLULAR LOCATION.
RX   PubMed=11689568; DOI=10.1074/jbc.M109005200;
RA   Hamazaki Y., Itoh M., Sasaki H., Furuse M., Tsukita S.;
RT   "Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions
RT   through its possible interaction with claudin-1 and junctional
RT   adhesion molecule.";
RL   J. Biol. Chem. 277:455-461(2002).
RN   [11]
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=22291956; PubMed=12403818; DOI=10.1083/jcb.200207050;
RA   Poliak S., Matlis S., Ullmer C., Scherer S.S., Peles E.;
RT   "Distinct claudins and associated PDZ proteins form different
RT   autotypic tight junctions in myelinating Schwann cells.";
RL   J. Cell Biol. 159:361-372(2002).
RN   [12]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=22592538; PubMed=12706259; DOI=10.1016/S0006-8993(03)02338-2;
RA   Sitek B., Poschmann G., Schmidtke K., Ullmer C., Maskri L.,
RA   Andriske M., Stichel C.C., Zhu X.-R., Luebbert H.;
RT   "Expression of MUPP1 protein in mouse brain.";
RL   Brain Res. 970:178-187(2003).
RN   [13]
RP   INTERACTION WITH CXADR, AND DOMAIN.
RX   PubMed=15364909; DOI=10.1074/jbc.M409061200;
RA   Coyne C.B., Voelker T., Pichla S.L., Bergelson J.M.;
RT   "The coxsackievirus and adenovirus receptor interacts with the multi-
RT   PDZ domain protein-1 (MUPP-1) within the tight junction.";
RL   J. Biol. Chem. 279:48079-48084(2004).
RN   [14]
RP   INTERACTION WITH CRB1; MPP5 AND MPP4, AND SUBCELLULAR LOCATION.
RX   PubMed=15316081; DOI=10.1242/jcs.01301;
RA   van de Pavert S.A., Kantardzhieva A., Malysheva A., Meuleman J.,
RA   Versteeg I., Levelt C., Klooster J., Geiger S., Seeliger M.W.,
RA   Rashbass P., Le Bivic A., Wijnholds J.;
RT   "Crumbs homologue 1 is required for maintenance of photoreceptor cell
RT   polarization and adhesion during light exposure.";
RL   J. Cell Sci. 117:4169-4177(2004).
CC   -!- FUNCTION: Interacts with HTR2C and provokes its clustering at the
CC       cell surface. Member of the NMDAR signaling complex that may play
CC       a role in control of AMPAR potentiation and synaptic plasticity in
CC       excitatory synapses (By similarity).
CC   -!- SUBUNIT: Interacts with CLDN5, DLG4, GRIN1, SYNGAP1, CAMK2A and
CC       CAMK2B, HTR2A, HTR2B, HTR2C, PLEKHA1/TAPP1 and PLEKHA2/TAPP2 (By
CC       similarity). Interacts with F11R/JAM, CLDN1, NG2, CXADR, CRB1,
CC       MPP4 and MPP5. Interacts with the adenovirus type 9 E4-ORF1
CC       oncoprotein.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Apical cell membrane; Peripheral membrane
CC       protein; Cytoplasmic side. Cell junction, synapse, postsynaptic
CC       cell membrane, postsynaptic density. Cell projection, dendrite.
CC       Cell junction, tight junction (By similarity). Cell junction,
CC       synapse. Cell junction, synapse, synaptosome (By similarity).
CC       Note=Colocalizes with HTR2C on the apical membrane of epithelial
CC       choroid plexus cells. Highly enriched in postsynaptic densities
CC       (PSD). Localized to punctae on dendrites of hippocampal neurons
CC       and colocalizes with the synaptic marker DLG4. Enriched at the
CC       tight junctions of epithelial cells. Association to the tight
CC       junctions depends on CXADR (By similarity). In the retina,
CC       localizes to the sub-apical region adjacent to the adherens
CC       junction complex at the outer limiting membrane. Localized mainly
CC       in the Schmidt-Lanterman incisures of myelinating Schwann cells.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q8VBX6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VBX6-2; Sequence=VSP_014201;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8VBX6-3; Sequence=VSP_014203;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q8VBX6-4; Sequence=VSP_014202;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q8VBX6-5; Sequence=VSP_014199, VSP_014200;
CC   -!- TISSUE SPECIFICITY: In the brain, it is strongly expressed in the
CC       choroid plexus. Within the hippocampal formation, strongest
CC       expression was seen in the soma of CA1-4 pyramidal cells.
CC       Expressed in most neocortical regions with the strongest
CC       expression in piriform cortex and amygdaloid nuclei but also
CC       detected in the subiculum and olfactory bulb. In the cerebellum,
CC       the highest level of expression was found in Purkinje cells.
CC       Moderately expressed in the granular layer and molecular layer.
CC       Expressed in the pontine nuclei, parts of spinal trigeminal
CC       nuclei, and the principal sensory trigeminal nuclei of the
CC       metencephalon. Expressed in all thalamic and hypothalamic nuclei,
CC       and the substantia nigra (at protein level). Ubiquitously
CC       expressed.
CC   -!- DOMAIN: The PDZ domain 2 mainly binds CAMK2A and CAMK2B. The PDZ
CC       domains 7 and 10 bind the Ad9 E4-ORF1 oncoprotein. The PDZ domain
CC       10 binds the C-terminal PDZ-binding motif of HTR2C. The PDZ
CC       domains 10 and 13 bind PLEKHA1 and PLEKHA2. The PDZ domain 13
CC       binds SYNGAP1 (By similarity). The PDZ domain 1 binds NG2. The PDZ
CC       domain 9 binds F11R. The PDZ domain 10 binds the C-terminus of
CC       CLDN1 and KIT. The PDZ domain 13 binds CXADR.
CC   -!- SIMILARITY: Contains 1 L27 domain.
CC   -!- SIMILARITY: Contains 13 PDZ (DHR) domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC27346.1; Type=Erroneous initiation;
CC       Sequence=BAC34766.1; Type=Erroneous initiation;
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DR   EMBL; AJ131869; CAA10523.1; -; mRNA.
DR   EMBL; AF326526; AAL37372.1; -; mRNA.
DR   EMBL; AF326527; AAL37373.1; -; mRNA.
DR   EMBL; AF326528; AAL37374.1; -; mRNA.
DR   EMBL; AF326529; AAL37375.1; -; mRNA.
DR   EMBL; AF326530; AAL37376.1; -; mRNA.
DR   EMBL; AF326531; AAL37377.2; -; mRNA.
DR   EMBL; AF326532; AAL37378.1; -; mRNA.
DR   EMBL; AF326533; AAL37379.1; -; mRNA.
DR   EMBL; AF326534; AAL37380.1; -; mRNA.
DR   EMBL; AF326535; AAL37381.1; -; mRNA.
DR   EMBL; AF326536; AAL37382.1; -; mRNA.
DR   EMBL; AF326537; AAL37383.1; -; mRNA.
DR   EMBL; AF326538; AAL37384.1; -; mRNA.
DR   EMBL; AF326539; AAL37385.1; -; mRNA.
DR   EMBL; AF326540; AAL37386.1; -; mRNA.
DR   EMBL; AF326541; AAL37387.1; -; mRNA.
DR   EMBL; AF326542; AAL37388.1; -; mRNA.
DR   EMBL; AF326543; AAL37389.1; -; mRNA.
DR   EMBL; AF326544; AAL37390.1; -; mRNA.
DR   EMBL; AK031321; BAC27346.1; ALT_INIT; mRNA.
DR   EMBL; AK051782; BAC34766.1; ALT_INIT; mRNA.
DR   EMBL; CR352325; CAI25220.1; -; Genomic_DNA.
DR   EMBL; AL670939; CAI25220.1; JOINED; Genomic_DNA.
DR   EMBL; AL670939; CAI25921.1; -; Genomic_DNA.
DR   EMBL; CR352325; CAI25921.1; JOINED; Genomic_DNA.
DR   EMBL; BC061504; AAH61504.1; -; mRNA.
DR   EMBL; BC145117; AAI45118.1; -; mRNA.
DR   EMBL; AF000168; AAB57835.1; -; mRNA.
DR   IPI; IPI00404052; -.
DR   IPI; IPI00457729; -.
DR   IPI; IPI00466594; -.
DR   IPI; IPI00474705; -.
DR   IPI; IPI00608031; -.
DR   PIR; T30259; T30259.
DR   RefSeq; NP_034950.2; NM_010820.2.
DR   UniGene; Mm.153039; -.
DR   ProteinModelPortal; Q8VBX6; -.
DR   SMR; Q8VBX6; 2-58, 120-466, 548-782, 995-1232, 1319-1431, 1490-1553, 1610-2055.
DR   DIP; DIP-41165N; -.
DR   MINT; MINT-146667; -.
DR   STRING; Q8VBX6; -.
DR   PhosphoSite; Q8VBX6; -.
DR   PRIDE; Q8VBX6; -.
DR   Ensembl; ENSMUST00000070461; ENSMUSP00000063710; ENSMUSG00000028402.
DR   Ensembl; ENSMUST00000102830; ENSMUSP00000099894; ENSMUSG00000028402.
DR   Ensembl; ENSMUST00000107261; ENSMUSP00000102882; ENSMUSG00000028402.
DR   GeneID; 17475; -.
DR   KEGG; mmu:17475; -.
DR   UCSC; uc008tjx.1; mouse.
DR   UCSC; uc008tjy.1; mouse.
DR   CTD; 17475; -.
DR   MGI; MGI:1343489; Mpdz.
DR   eggNOG; roNOG09825; -.
DR   GeneTree; ENSGT00570000078792; -.
DR   HOVERGEN; HBG080134; -.
DR   OrthoDB; EOG44F688; -.
DR   PhylomeDB; Q8VBX6; -.
DR   NextBio; 292120; -.
DR   ArrayExpress; Q8VBX6; -.
DR   Bgee; Q8VBX6; -.
DR   CleanEx; MM_MPDZ; -.
DR   Genevestigator; Q8VBX6; -.
DR   GermOnline; ENSMUSG00000028402; Mus musculus.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019717; C:synaptosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005923; C:tight junction; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR   InterPro; IPR004172; L27.
DR   InterPro; IPR015132; L27_2.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF09045; L27_2; 1.
DR   Pfam; PF00595; PDZ; 13.
DR   SMART; SM00569; L27; 1.
DR   SMART; SM00228; PDZ; 13.
DR   SUPFAM; SSF50156; PDZ; 13.
DR   PROSITE; PS51022; L27; 1.
DR   PROSITE; PS50106; PDZ; 13.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW   Membrane; Phosphoprotein; Postsynaptic cell membrane; Repeat; Synapse;
KW   Synaptosome; Tight junction.
FT   CHAIN         1   2055       Multiple PDZ domain protein.
FT                                /FTId=PRO_0000094595.
FT   DOMAIN        1     63       L27.
FT   DOMAIN      138    225       PDZ 1.
FT   DOMAIN      258    338       PDZ 2.
FT   DOMAIN      378    464       PDZ 3.
FT   DOMAIN      546    627       PDZ 4.
FT   DOMAIN      693    779       PDZ 5.
FT   DOMAIN      996   1077       PDZ 6.
FT   DOMAIN     1139   1231       PDZ 7.
FT   DOMAIN     1338   1421       PDZ 8.
FT   DOMAIN     1471   1552       PDZ 9.
FT   DOMAIN     1614   1697       PDZ 10.
FT   DOMAIN     1710   1792       PDZ 11.
FT   DOMAIN     1847   1933       PDZ 12.
FT   DOMAIN     1972   2055       PDZ 13.
FT   MOD_RES     231    231       Phosphoserine (By similarity).
FT   MOD_RES     354    354       Phosphoserine (By similarity).
FT   MOD_RES     355    355       Phosphoserine (By similarity).
FT   MOD_RES     359    359       Phosphothreonine (By similarity).
FT   VAR_SEQ      63     87       NIATLATAAADHAHTPQFSSAVISN -> GWHHPQRPSRCS
FT                                KDLVRKGSCFSTG (in isoform 5).
FT                                /FTId=VSP_014199.
FT   VAR_SEQ      88   2055       Missing (in isoform 5).
FT                                /FTId=VSP_014200.
FT   VAR_SEQ    1236   1268       Missing (in isoform 2).
FT                                /FTId=VSP_014201.
FT   VAR_SEQ    1714   1714       Q -> QLQ (in isoform 4).
FT                                /FTId=VSP_014202.
FT   VAR_SEQ    2054   2055       LS -> SLEVTARVEAAQPLAPLLL (in isoform 3).
FT                                /FTId=VSP_014203.
FT   VARIANT     541    541       N -> S (in strain: DBA/2J and DBA1/J).
FT   VARIANT     691    691       G -> V (in strain: DBA/2J, DBA1/J, CE/J,
FT                                A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2
FT                                and 129/J).
FT   VARIANT     801    801       H -> R (in strain: DBA/2J, DBA1/J, CE/J,
FT                                A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2
FT                                and 129/J).
FT   VARIANT     859    859       T -> A (in strain: DBA/2J, DBA1/J, CE/J,
FT                                A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2
FT                                and 129/J).
FT   VARIANT     880    880       S -> N (in strain: DBA/2J, DBA1/J, CE/J,
FT                                A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2
FT                                and 129/J).
FT   VARIANT     914    914       R -> S (in strain: DBA/2J, DBA1/J, CE/J,
FT                                A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2
FT                                and 129/J).
FT   VARIANT     977    977       A -> V (in strain: DBA/2J, DBA1/J, CE/J,
FT                                A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2
FT                                and 129/J).
FT   VARIANT    1338   1338       V -> M (in strain: DBA/2J, DBA1/J, CE/J,
FT                                A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2
FT                                and 129/J).
FT   VARIANT    1433   1433       I -> N (in strain: DBA/2J, DBA1/J, CE/J,
FT                                A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2
FT                                and 129/J).
FT   VARIANT    1767   1767       H -> N (in strain: DBA/2J, DBA1/J, CE/J,
FT                                A/HeJ, BALB/cJ, C57Br/cdJ, C57L/J, WSP2
FT                                and 129/J).
FT   CONFLICT    583    583       S -> N (in Ref. 1; CAA10523).
FT   CONFLICT    588    588       S -> N (in Ref. 1; CAA10523).
FT   CONFLICT    871    871       P -> S (in Ref. 1; CAA10523).
FT   CONFLICT    909    910       PP -> SS (in Ref. 1; CAA10523).
FT   CONFLICT    914    919       RPAPTS -> KPTPTF (in Ref. 1; CAA10523).
FT   CONFLICT    932    932       V -> G (in Ref. 1; CAA10523).
FT   CONFLICT    937    938       EC -> QW (in Ref. 1; CAA10523).
FT   CONFLICT    952    952       S -> N (in Ref. 1; CAA10523).
FT   CONFLICT    956    956       S -> F (in Ref. 1; CAA10523).
FT   CONFLICT    960    960       P -> S (in Ref. 1; CAA10523).
FT   CONFLICT    963    963       P -> A (in Ref. 1; CAA10523).
FT   CONFLICT    967    967       Q -> P (in Ref. 1; CAA10523).
FT   CONFLICT    974    975       SS -> TF (in Ref. 1; CAA10523).
FT   CONFLICT    984    984       N -> T (in Ref. 1; CAA10523).
FT   CONFLICT    996    996       T -> P (in Ref. 1; CAA10523).
FT   CONFLICT   1532   1532       K -> N (in Ref. 6; AAB57835).
FT   CONFLICT   1547   1547       T -> I (in Ref. 6; AAB57835).
FT   CONFLICT   1589   1589       T -> P (in Ref. 1; CAA10523).
FT   CONFLICT   1616   1617       EI -> GV (in Ref. 6; AAB57835).
FT   CONFLICT   1691   1691       L -> V (in Ref. 6; AAB57835).
FT   CONFLICT   1844   1844       G -> R (in Ref. 6; AAB57835).
FT   CONFLICT   1914   1914       A -> V (in Ref. 5; AAH61504).
FT   CONFLICT   1968   1968       P -> S (in Ref. 1; CAA10523).
FT   CONFLICT   1983   1985       GFS -> SFN (in Ref. 1; CAA10523).
SQ   SEQUENCE   2055 AA;  218711 MW;  26EA94B814214B69 CRC64;
     MLETIDKNRA LQAAERLQSK LKERGDVANE DKLSLLKSVL QSPLFSQILN LQTSLQQLKD
     QVNIATLATA AADHAHTPQF SSAVISNLQS ESLLLSPNHG NLEALPGPGA PAVMDGKPTC
     DELDQLIKNM AQGRHVEIFE LLKPPCGGLG FSVVGLRSEN RGELGIFVQE IQEGSVAHRD
     GRLKETDQIL AINGQVLDQT ITHQQAISIL QKAKDTVQLV IARGSLPPVS SPRISRSPSA
     ASTISAHSNP MHWQHVETIE LVNDGSGLGF GIIGGKATGV IVKTILPGGV ADQHGRLCSG
     DHILKIGDTD LAGMSSEQVA QVLRQCGNRV KLMIARGAVE ETPASSSLGI TLSSSTSSTS
     EMRVDASTQK NDESETFDVE LTKNVQGLGI TIAGYIGDKK LEPSGIFVKS ITKSSAVEHD
     GRIQIGDQII AVDGTNLQGF TNQQAVEVLR HTGQTVRLTL MRKGASQEAE LTSRGDTAKD
     VDLPAENCEK DEESLSLKRN TSILPIEEEG FPLLSAELEE AEDVQQEAAL LTKWQRIMGI
     NYEIVVAHVS KFSENSGLGI SLEATVGHHF IRSVLPEGPV GHSGKLFSGD ELLEVNGINL
     LGENHQDVVN ILKELPIDVT MVCCRRTVPP IALSEMDSLD INDLELTEKP HIDLGEFIGS
     SETEDPMLAM SDVDQNAEEI QTPLAMWEAG GQSIELEKGS RGLGFSILDY QDPIDPANTV
     IVIRSLVPGG IAEKDGRLFP GDRLMFVNDI NLENSTLEEA VEALKGAPSG MVRIGVAKPL
     PLSPEEGYVS AKEDAFLCSP HACKESGLSD KALFRADLAL IDTPDAESIA ESRFESQFSP
     DNDSVYSTQA SIFSLHDGTC SDGMNYGPSL PSSPPKDVTS SSEVVLGLHL SLEELYTQNL
     LQRQHAGSPP TDMRPAPTSG FPISDYTTTN AVEQKYECAN PVAWPHSQLP SSLSTSELAP
     ALPAVAQKYL TDQSSLASDA ESVNLQSMSQ EAFERTVTIA KGSSSLGMTV SANKDGLGVI
     VRSIIHGGAI SRDGRIAVGD CILSINEEST ISLTNAQARA MLRRHSLIGP DIKITYVPAE
     HLEEFRVSFG QQAGGIMALD IFSSYTGRDI PELPEREEGE GEESELQNAA YSSWSQPRRV
     ELWREPSKSL GISIVGGRGM GSRLSNGEVM RGIFIKHVLE DSPAGKNGTL KPGDRIIEVD
     GMDLRDASHE QAVEAIRKAG NPVVFMVQSI INRPRKSPLP SLPHSLYPKY SFSSTNPFAD
     SLQLTTDQAP SQSESETEKP ALCNVPPSSP SVFSEMGSDC AQPSATAVSE DEDKEDEFGY
     SWKNIQERYG SLTGQLHVIE LEKGQSGLGL SLAGNKDRTR MSVFIVGIDP TGAAGRDGRL
     QIADELLEIN GQILYGRSHQ NASSIIKCAP SKVKIIFIRN ADAVNQMAVC PGIAADSPSS
     TSDSPQNKEV EPCSTTSASA ADLSSLTDVY QLELPKDQGG LGIAICEEDT INGVMIESLT
     EHGGAAKDGR LKPGDHILAV DDEVVAGCPV EKFISLLKTA KATVKLTVRA ENPACPAVPS
     SAVTVSGERK DNSQTPAVPA PDLEPIPSTS RSSTPAVFAS DPATCPIIPG CETTIEISKG
     QTGLGLSIVG GSDTLLGAII IHEVYEEGAA CKDGRLWAGD QILEVNGIDL RKATHDEAIN
     VLRQTPQRVR LTLYRDEAPY KEEDVCDTFT IELQKRPGKG LGLSIVGKRN DTGVFVSDIV
     KGGIADADGR LMQGDQILMV NGEDVRHATQ EAVAALLKCS LGAVTLEVGR VKAAPFHSER
     RPSQSSQVSE SSLSSFTPPL SGINTSESLE SNSKKNALAS EIQGLRTVEI KKGPADSLGL
     SIAGGVGSPL GDVPIFIAMM HPNGVAAQTQ KLRVGDRIVT ICGTSTDGMT HTQAVNLMKN
     ASGSIEVQVV AGGDVSVVTG HQQELANPCL AFTGLTSSSI FPDDLGPPQS KTITLDRGPD
     GLGFSIVGGY GSPHGDLPIY VKTVFAKGAA AEDGRLKRGD QIIAVNGQSL EGVTHEEAVA
     ILKRTKGTVT LMVLS
//
ID   KKCC1_MOUSE             Reviewed;         505 AA.
AC   Q8VBY2; Q9R054;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Calcium/calmodulin-dependent protein kinase kinase 1;
DE            Short=CaM-KK 1;
DE            Short=CaM-kinase kinase 1;
DE            Short=CaMKK 1;
DE            EC=2.7.11.17;
DE   AltName: Full=CaM-kinase IV kinase;
DE   AltName: Full=Calcium/calmodulin-dependent protein kinase kinase alpha;
DE            Short=CaM-KK alpha;
DE            Short=CaM-kinase kinase alpha;
DE            Short=CaMKK alpha;
GN   Name=Camkk1; Synonyms=Camkk;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20023572; PubMed=10560916; DOI=10.1016/S0301-472X(99)00108-3;
RA   Lawson N.D., Zain M., Zibello T., Picciotto M.R., Nairn A.C.,
RA   Berliner N.;
RT   "Modulation of a calcium/calmodulin-dependent protein kinase cascade
RT   by retinoic acid during neutrophil maturation.";
RL   Exp. Hematol. 27:1682-1690(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   PubMed=17015467; DOI=10.1128/MCB.01452-06;
RA   Blaeser F., Sanders M.J., Truong N., Ko S., Wu L.J., Wozniak D.F.,
RA   Fanselow M.S., Zhuo M., Chatila T.A.;
RT   "Long-term memory deficits in Pavlovian fear conditioning in
RT   Ca2+/calmodulin kinase kinase alpha-deficient mice.";
RL   Mol. Cell. Biol. 26:9105-9115(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 114-129 AND 440-451, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=12654522; DOI=10.1016/S0169-328X(02)00698-8;
RA   Vinet J., Carra S., Blom J.M.C., Harvey M., Brunello N., Barden N.,
RA   Tascedda F.;
RT   "Cloning of mouse Ca2+/calmodulin-dependent protein kinase kinase beta
RT   (CaMKKbeta) and characterization of CaMKKbeta and CaMKKalpha
RT   distribution in the adult mouse brain.";
RL   Brain Res. Mol. Brain Res. 111:216-221(2003).
RN   [6]
RP   FUNCTION IN PHOSPHORYLATION OF CAMK1G.
RX   MEDLINE=22625683; PubMed=12637513; DOI=10.1074/jbc.M300578200;
RA   Takemoto-Kimura S., Terai H., Takamoto M., Ohmae S., Kikumura S.,
RA   Segi E., Arakawa Y., Furuyashiki T., Narumiya S., Bito H.;
RT   "Molecular cloning and characterization of CLICK-III/CaMKIgamma, a
RT   novel membrane-anchored neuronal Ca2+/calmodulin-dependent protein
RT   kinase (CaMK).";
RL   J. Biol. Chem. 278:18597-18605(2003).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458 AND SER-475, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Calcium/calmodulin-dependent protein kinase that belongs
CC       to a proposed calcium-triggered signaling cascade involved in a
CC       number of cellular processes. Phosphorylates CAMK1, CAMK1D, CAMK1G
CC       and CAMK4. Involved in regulating cell apoptosis. Promotes cell
CC       survival by phosphorylating AKT1/PKB that inhibits pro-apoptotic
CC       BAD/Bcl2-antagonist of cell death.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Activated by Ca(2+)/calmodulin. Binding of
CC       calmodulin may releave intrasteric autoinhibition. Partially
CC       inhibited upon phosphorylation by PRCAKA/PKA (By similarity). May
CC       be regulated through phosphorylation by CAMK1 and CAMK4.
CC   -!- SUBUNIT: Interacts with CAMK4 and calmodulin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed. Differentially expressed in
CC       various brain regions.
CC   -!- DOMAIN: The autoinhibitory domain overlaps with the calmodulin
CC       binding region and may be involved in intrasteric autoinhibition.
CC   -!- DOMAIN: The RP domain (arginine/proline-rich) is involved in the
CC       recognition of CAMKI and CAMK4 as substrates (By similarity).
CC   -!- PTM: Appears to be autophosphorylated in a Ca(2+)/calmodulin-
CC       dependent manner. Phosphorylated at multiple sites by PRCAKA/PKA.
CC       Phosphorylation of Ser-458 is blocked upon binding to
CC       Ca(2+)/calmodulin. In vitro, phosphorylated by CAMK1 and CAMK4 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AF117384; AAF08348.1; -; mRNA.
DR   EMBL; AF461706; AAL67849.1; -; Genomic_DNA.
DR   EMBL; AF461702; AAL67849.1; JOINED; Genomic_DNA.
DR   EMBL; AF461703; AAL67849.1; JOINED; Genomic_DNA.
DR   EMBL; AF461705; AAL67849.1; JOINED; Genomic_DNA.
DR   EMBL; AF461704; AAL67849.1; JOINED; Genomic_DNA.
DR   EMBL; BC017529; AAH17529.1; -; mRNA.
DR   IPI; IPI00626535; -.
DR   RefSeq; NP_061371.2; NM_018883.2.
DR   UniGene; Mm.9998; -.
DR   ProteinModelPortal; Q8VBY2; -.
DR   SMR; Q8VBY2; 123-411, 438-463.
DR   MINT; MINT-102795; -.
DR   STRING; Q8VBY2; -.
DR   PhosphoSite; Q8VBY2; -.
DR   PRIDE; Q8VBY2; -.
DR   Ensembl; ENSMUST00000092937; ENSMUSP00000090613; ENSMUSG00000020785.
DR   GeneID; 55984; -.
DR   KEGG; mmu:55984; -.
DR   UCSC; uc007jzt.1; mouse.
DR   CTD; 55984; -.
DR   MGI; MGI:1891766; Camkk1.
DR   eggNOG; roNOG15074; -.
DR   GeneTree; ENSGT00530000063214; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG052262; -.
DR   InParanoid; Q8VBY2; -.
DR   OMA; LHCQKIV; -.
DR   OrthoDB; EOG4TF0JX; -.
DR   PhylomeDB; Q8VBY2; -.
DR   BRENDA; 2.7.11.17; 244.
DR   NextBio; 311694; -.
DR   ArrayExpress; Q8VBY2; -.
DR   Bgee; Q8VBY2; -.
DR   Genevestigator; Q8VBY2; -.
DR   GermOnline; ENSMUSG00000020785; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:EC.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Calmodulin-binding; Cytoplasm; Direct protein sequencing;
KW   Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    505       Calcium/calmodulin-dependent protein
FT                                kinase kinase 1.
FT                                /FTId=PRO_0000086142.
FT   DOMAIN      128    409       Protein kinase.
FT   NP_BIND     134    142       ATP (By similarity).
FT   REGION      167    189       RP domain.
FT   REGION      435    440       Autoinhibitory domain (By similarity).
FT   REGION      438    463       Calmodulin-binding (By similarity).
FT   ACT_SITE    275    275       Proton acceptor (By similarity).
FT   BINDING     157    157       ATP (By similarity).
FT   MOD_RES      74     74       Phosphoserine (By similarity).
FT   MOD_RES     108    108       Phosphothreonine (By similarity).
FT   MOD_RES     458    458       Phosphoserine.
FT   MOD_RES     475    475       Phosphoserine.
FT   MOD_RES     492    492       Phosphoserine (By similarity).
FT   MOD_RES     505    505       Phosphoserine (By similarity).
FT   CONFLICT     99    100       IS -> MC (in Ref. 1; AAF08348).
FT   CONFLICT    198    199       QE -> HD (in Ref. 1; AAF08348).
FT   CONFLICT    382    382       L -> S (in Ref. 1; AAF08348).
FT   CONFLICT    417    417       L -> I (in Ref. 1; AAF08348).
SQ   SEQUENCE   505 AA;  55838 MW;  179915A25628F9C4 CRC64;
     MESGPAVCCQ DPRAELVDRV AAINVAHLEE ADEGPEPARN GVDPPPRARA ASVIPGSASR
     PTPVRPSLSA RKFSLQERPA GSCLGAQVGP YSTGPASHIS PRSWRRPTIE SHRVAISDTE
     DCVQLNQYKL QSEIGKGAYG VVRLAYNESE DRHYAMKVLS KKKLLKQYGF PRRPPPRGSQ
     ATQGGPAKQL LPLERVYQEI AILKKLDHVN VVKLIEVLDD PAEDNLYLVF DLLRKGPVME
     VPCDKPFPEE QARLYLRDII LGLEYLHCQK IVHRDIKPSN LLLGDDGHVK IADFGVSNQF
     EGNDAQLSST AGTPAFMAPE AISDSGQSFS GKALDVWATG VTLYCFVYGK CPFIDDYILT
     LHRKIKNEAV VFPEEPEVSE DLKDLILRML DKNPETRIGV SDIKLHPWVT KHGEEPLPSE
     EEHCSVVEVT EEEVKNSVRL IPSWTTVILV KSMLRKRSFG NPFEPQARRE ERSMSAPGSL
     LMKEGCGEGC KSPELPGVQE DEAAS
//
ID   EMAL3_MOUSE             Reviewed;         897 AA.
AC   Q8VC03; Q8R1S1;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Echinoderm microtubule-associated protein-like 3;
DE            Short=EMAP-3;
GN   Name=Eml3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May modify the assembly dynamics of microtubules, such
CC       that microtubules are slightly longer, but more dynamic (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (Potential).
CC   -!- SIMILARITY: Belongs to the WD repeat EMAP family.
CC   -!- SIMILARITY: Contains 9 WD repeats.
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DR   EMBL; BC022146; AAH22146.1; -; mRNA.
DR   EMBL; BC023878; AAH23878.1; -; mRNA.
DR   EMBL; BC024134; AAH24134.1; -; mRNA.
DR   IPI; IPI00121225; -.
DR   RefSeq; NP_659121.1; NM_144872.1.
DR   UniGene; Mm.31008; -.
DR   ProteinModelPortal; Q8VC03; -.
DR   SMR; Q8VC03; 388-416, 684-709, 730-757.
DR   PhosphoSite; Q8VC03; -.
DR   PRIDE; Q8VC03; -.
DR   Ensembl; ENSMUST00000096241; ENSMUSP00000093960; ENSMUSG00000071647.
DR   GeneID; 225898; -.
DR   KEGG; mmu:225898; -.
DR   UCSC; uc008god.1; mouse.
DR   CTD; 225898; -.
DR   MGI; MGI:2387612; Eml3.
DR   eggNOG; maNOG09851; -.
DR   GeneTree; ENSGT00550000074369; -.
DR   HOGENOM; HBG356915; -.
DR   HOVERGEN; HBG051470; -.
DR   InParanoid; Q8VC03; -.
DR   OMA; EMELVKA; -.
DR   OrthoDB; EOG45755Z; -.
DR   PhylomeDB; Q8VC03; -.
DR   NextBio; 377865; -.
DR   ArrayExpress; Q8VC03; -.
DR   Bgee; Q8VC03; -.
DR   CleanEx; MM_EML3; -.
DR   Genevestigator; Q8VC03; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR005108; HELP.
DR   InterPro; IPR004106; Peptidase_S9A_B_C_N.
DR   InterPro; IPR011047; Quino_AlcDH-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
DR   Pfam; PF03451; HELP; 1.
DR   Pfam; PF00400; WD40; 5.
DR   SMART; SM00320; WD40; 8.
DR   SUPFAM; SSF50993; Peptidase_S9A_N; 1.
DR   SUPFAM; SSF50998; Quin_alc_DH_like; 1.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein; Repeat;
KW   WD repeat.
FT   CHAIN         1    897       Echinoderm microtubule-associated
FT                                protein-like 3.
FT                                /FTId=PRO_0000284391.
FT   REPEAT      304    353       WD 1.
FT   REPEAT      358    401       WD 2.
FT   REPEAT      404    443       WD 3.
FT   REPEAT      458    496       WD 4.
FT   REPEAT      513    552       WD 5.
FT   REPEAT      596    635       WD 6.
FT   REPEAT      679    718       WD 7.
FT   REPEAT      725    764       WD 8.
FT   REPEAT      838    878       WD 9.
FT   COMPBIAS    127    130       Poly-Ser.
FT   COMPBIAS    157    164       Poly-Ser.
FT   COMPBIAS    288    298       Poly-Gly.
FT   COMPBIAS    653    656       Poly-Val.
FT   MOD_RES     177    177       Phosphoserine (By similarity).
FT   MOD_RES     882    882       Phosphothreonine (By similarity).
SQ   SEQUENCE   897 AA;  95695 MW;  F0D1390F323BD5B1 CRC64;
     MDGAAGPGEG PAHETLQTLS QRLRVQEEEM ELVKAALAEA LRLLRLHGST TTLQGSGISA
     PTRNSSITVP PGLPPTCSPS LVTRGTQTEE ELEIVPSSGP PGLSNGPPAL QGGSEEPSGT
     QSEGGCSSSS GAGSPGPPGI LRPVQPLQRS DTPRRNSSSS SSPSERPRQK LSRKAASSAN
     LLLRSGSTES RGNKDPLSSP GGPGSRRSNY NLEGISVKMF LRGRPITMYI PSGIRSLEEL
     PSGPPPETLS LDWVYGYRGR DSRSNLFVLR SGEVVYFIAC VVVLYRPGGG PGGPGGGGQR
     HYRGHTDCVR CLAVHPDGVR VASGQTAGVD KDGKPLQPVV HIWDSETLLK LQEIGLGAFE
     RGVGALAFSA ADQGAFLCVV DDSNEHMLSV WDCSRGVKLA EIKSTNDSVL AVGFSPRDSS
     CIVTSGKSHV HFWNWSGGTG APGNGLLARK QGVFGKYKKP KFIPCFVFLP DGDILTGDSE
     GNILTWGRSV SDSKTPGRGG AKETYTIVAQ AHAHEGSIFA LCLRRDGTVL SGGGRDRRLV
     QWGPGLVALQ EAEIPEHFGA VRAIAEGLGS ELLVGTTKNA LLRGDLAQGF SPVIQGHTDE
     LWGLCTHPSQ NRFLTCGHDR QLCLWDGEGH ALAWSMDLKE TGLCADFHPS GAVVVVGLNT
     GRWLVLDTET REIVSDVTDG NEQLSVVRYS PDGLYLAIGS HDNMIYIYSV SSCGTKSSRF
     GRCMGHSSFI THLDWSKDGN FIMSNSGDYE ILYWDVAGGC KLLRNRYESR DREWATYTCV
     LGFHVYGVWP DGSDGTDINS LCRSHNERVV AVADDFCKVH LFQYPCARAK APSRMYSGHG
     SHVTSVRFTH DDSYLVSLGG KDASIFQWRV LGAGSSGPAP ATPSRTPSLS PASSLDV
//
ID   Q8VC68_MOUSE            Unreviewed;      1726 AA.
AC   Q8VC68;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   SubName: Full=Ankyrin 3, epithelial;
GN   Name=Ank3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC021657; AAH21657.1; -; mRNA.
DR   IPI; IPI00173248; -.
DR   UniGene; Mm.235960; -.
DR   HSSP; P16157; 1N11.
DR   ProteinModelPortal; Q8VC68; -.
DR   SMR; Q8VC68; 60-825, 1429-1533.
DR   STRING; Q8VC68; -.
DR   PRIDE; Q8VC68; -.
DR   UCSC; uc007fna.1; mouse.
DR   HOVERGEN; HBG004234; -.
DR   PhylomeDB; Q8VC68; -.
DR   Genevestigator; Q8VC68; -.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR000488; Death.
DR   InterPro; IPR011029; DEATH-like.
DR   InterPro; IPR000906; ZU5.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 3.
DR   Gene3D; G3DSA:1.10.533.10; DEATH_like; 1.
DR   Pfam; PF00023; Ank; 19.
DR   Pfam; PF00531; Death; 1.
DR   Pfam; PF00791; ZU5; 1.
DR   SMART; SM00248; ANK; 22.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00218; ZU5; 1.
DR   SUPFAM; SSF48403; ANK; 2.
DR   SUPFAM; SSF47986; DEATH_like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 21.
DR   PROSITE; PS50017; DEATH_DOMAIN; 1.
DR   PROSITE; PS51145; ZU5; 1.
PE   2: Evidence at transcript level;
KW   ANK repeat; Repeat.
SQ   SEQUENCE   1726 AA;  188240 MW;  430148B67E00B1CA CRC64;
     MSEEPKEKPA KPAHRKRKGK KSDANASYLR AARAGHLEKA LDYIKNGVDV NICNQNGLNA
     LHLASKEGHV EVVSELLQRE ANVDAATKKG NTALHIASLA GQAEVVKVLV TNGANVNAQS
     QNGFTPLYMA AQENHLEVVR FLLDNGASQS LATEDGFTPL AVALQQGHDQ VVSLLLENDT
     KGKVRLPALH IAARKDDTKA AALLLQNDTN ADVESKSGFT PLHIAAHYGN INVATLLLNR
     AAAVDFTARN DITPLHVASK RGNANMVKLL LDRGAKIDAK TRDGLTPLHC GARSGHEQVV
     EMLLDRSAPI LSKTKNGLSP LHMATQGDHL NCVQLLLQHN VPVDDVTNDY LTALHVAAHC
     GHYKVAKVLL DKKASPNAKA LNGFTPLHIA CKKNRIRVME LLLKHGASIQ AVTESGLTPI
     HVAAFMGHVN IVSQLMHHGA SPNTTNVRGE TALHMAARSG QAEVVRYLVQ DGAQVEAKAK
     DDQTPLHISA RLGKADIVQQ LLQQGASPNA ATTSGYTPLH LAAREGHEDV AAFLLDHGAS
     LSITTKKGFT PLHVAAKYGK LEVASLLLQK SASPDAAGKS GLTPLHVAAH YDNQKVALLL
     LDQGASPHAA AKNGYTPLHI AAKKNQMDIA TSLLEYGADA NAVTRQGIAS VHLAAQEGHV
     DMVSLLLSRN ANVNLSNKSG LTPLHLAAQE DRVNVAEVLV NQGAHVDAQT KMGYTPPHVG
     CHYGNIKIVN FLLQHSAKVN AKTKNGYTAL HQAAQQGHTH IINVLLQNNA SPNELTVNGN
     TALAIARRLG YISVVDTLKV VTEEIMTTTT ITEKHKMNVP ETMNEVLDMS DDEGEDAITG
     DTDKYLGPQD LKELGDDSLP AEGYVGFSLG ARSASLRSFS SDRSYTLNRS SYARDSMMIE
     ELLVPSKEQH LTFTREFDSD SLRHYSWAAD TLDNVNLVSS PVHSGFLVSF MVDARGGSMR
     GSRHHGMRII IPPRKCTAPT RITCRLVKRH KLANPPPMVE GEGLASRLVE MGPAGAQFLG
     PVIVEIPHFG SMRGKERELI VLRSENGETW KEHQFDSKNE DLAELLNGMD EELDSPEELG
     TKRICRIITK DFPQYFAVVS RIKQESNQIG PEGGILSSTT VPLVQASFPE GALTKRIRVG
     LQAQPVPEET VKKILGNKAT FSPIVTVEPR RRKFHKPITM TIPVPPPSGE GVSNGYKGDA
     TPNLRLLCSI TGGTSPAQWE DITGTTPLTF IKDCVSFTTN VSARFWLADC HQVLETVGLA
     SQLYRELICV PYMAKFVVFA KTNDPVESSL RCFCMTDDRV DKTLEQQENF EEVARSKDIE
     VLEGKPIYVD CYGNLAPLTK GGQQLVFNFY SFKENRLPFS IKIRDTSQEP CGRLSFLKEP
     KTTKGLPQTA VCNLNITLPA HKKAEKADRR QSFASLALRK RYSYLTEPSM SPQSPCERTD
     IRMAIVADHL GLSWTELARE LNFSVDEINQ IRVENPNSLI SQSFMLLKKW VTRDGKNATT
     DALTSVLTKI NRIDIVTLLE GPIFDYGNIS GTRSFADENN VFHDPVDGWQ NETPSGSLES
     PAQARRLTGG LLDRLDDSSD QARDSITSYL TGEPGKIEAN GNHTAEVIPE AKAKPYFPES
     QNDIGKQSIK ENLKPKTHGC GRTEEPVSPL TAYQKSLEET SKLVIEDAPK PCVPVGMKKM
     TRTTADGKAR LNLQEEEGST RSEPKQGEGY KVKTKKEIRN VEKKTH
//
ID   RPGF3_MOUSE             Reviewed;         918 AA.
AC   Q8VCC8; Q8BZK9; Q8R1R1;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Rap guanine nucleotide exchange factor 3;
DE   AltName: Full=Exchange factor directly activated by cAMP 1;
DE   AltName: Full=Exchange protein directly activated by cAMP 1;
DE            Short=EPAC 1;
DE   AltName: Full=cAMP-regulated guanine nucleotide exchange factor I;
DE            Short=cAMP-GEFI;
GN   Name=Rapgef3; Synonyms=Epac, Epac1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 640-918 (ISOFORM 2).
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 466-918 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Guanine nucleotide exchange factor (GEF) for RAP1A and
CC       RAP2A small GTPases that is activated by binding cAMP (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC       protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VCC8-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q8VCC8-2; Sequence=VSP_007610;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The DEP domain is involved in membrane localization
CC       independent from regulation by cAMP (By similarity).
CC   -!- SIMILARITY: Contains 1 cyclic nucleotide-binding domain.
CC   -!- SIMILARITY: Contains 1 DEP domain.
CC   -!- SIMILARITY: Contains 1 N-terminal Ras-GEF domain.
CC   -!- SIMILARITY: Contains 1 Ras-GEF domain.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-43 is the initiator.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH20532.1; Type=Erroneous initiation;
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DR   EMBL; BC020532; AAH20532.1; ALT_INIT; mRNA.
DR   EMBL; BC020311; AAH20311.1; -; mRNA.
DR   EMBL; AK034265; BAC28653.1; -; mRNA.
DR   IPI; IPI00331717; -.
DR   IPI; IPI00757993; -.
DR   RefSeq; NP_001171281.1; NM_001177810.1.
DR   RefSeq; NP_001171282.1; NM_001177811.1.
DR   RefSeq; NP_659099.2; NM_144850.2.
DR   UniGene; Mm.24028; -.
DR   ProteinModelPortal; Q8VCC8; -.
DR   SMR; Q8VCC8; 89-918.
DR   STRING; Q8VCC8; -.
DR   PhosphoSite; Q8VCC8; -.
DR   PRIDE; Q8VCC8; -.
DR   Ensembl; ENSMUST00000023109; ENSMUSP00000023109; ENSMUSG00000022469.
DR   GeneID; 223864; -.
DR   KEGG; mmu:223864; -.
DR   UCSC; uc007xla.1; mouse.
DR   CTD; 223864; -.
DR   MGI; MGI:2441741; Rapgef3.
DR   GeneTree; ENSGT00560000077091; -.
DR   HOVERGEN; HBG056985; -.
DR   InParanoid; Q8VCC8; -.
DR   OrthoDB; EOG4WDDB1; -.
DR   NextBio; 376937; -.
DR   ArrayExpress; Q8VCC8; -.
DR   Bgee; Q8VCC8; -.
DR   CleanEx; MM_RAPGEF3; -.
DR   Genevestigator; Q8VCC8; -.
DR   GermOnline; ENSMUSG00000022469; Mus musculus.
DR   GO; GO:0005952; C:cAMP-dependent protein kinase complex; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:MGI.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IEA:InterPro.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR002373; cAMP/cGMP_kin.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR   InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR   InterPro; IPR008937; Ras_GEF.
DR   InterPro; IPR001895; RasGRF_CDC25.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.840.10; RasGRF_CDC25; 1.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   PANTHER; PTHR23113; Ras_GEF; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   PRINTS; PR00103; CAMPKINASE.
DR   SMART; SM00100; cNMP; 1.
DR   SMART; SM00049; DEP; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00229; RasGEFN; 1.
DR   SUPFAM; SSF51206; cNMP_binding; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; FALSE_NEG.
DR   PROSITE; PS00889; CNMP_BINDING_2; FALSE_NEG.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS50186; DEP; 1.
DR   PROSITE; PS00720; RASGEF; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50212; RASGEF_NTER; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; cAMP; cAMP-binding; Cytoplasm;
KW   Guanine-nucleotide releasing factor; Membrane; Nucleotide-binding.
FT   CHAIN         1    918       Rap guanine nucleotide exchange factor 3.
FT                                /FTId=PRO_0000068868.
FT   DOMAIN      110    186       DEP.
FT   DOMAIN      384    521       N-terminal Ras-GEF.
FT   DOMAIN      665    884       Ras-GEF.
FT   NP_BIND     245    363       cAMP.
FT   VAR_SEQ     688    689       QE -> ELIHYVLGPQ (in isoform 2).
FT                                /FTId=VSP_007610.
SQ   SEQUENCE   918 AA;  103533 MW;  DB774BBF7CB4428E CRC64;
     MKVSWPGENH WQVGPAVVES PAVGAPQVGG LPDVVPEGTL LNMVLKRMHR PRCCSYQLVF
     EHRRPSCIQG LRWTPLTNSE DSLDFRVSLE QATTEHVHKA GKLLHRHLLA TYPTLIRDRK
     YHLRLYRHCC SGRELVDGIL ALGLGVHSRS QAVGICQVLL DEGALCHVKH DWTFQDRDAQ
     FYRFPGPEPE PTGTQDVEEE LVEAMALLSQ RGPDALLTVA LRKPPGQRTD EELDLIFEEL
     LHIKAVAHLS NSVKRELAAV LLFEPHSKAG TVLFSQGDKG TSWYIIWKGS VNVVTHGKGL
     VTTLHEGDDF GQLALVNDAP RAATIILREN NCHFLRVDKQ DFNRIIKDVE AKTMRLEEHG
     KVVLVLERTS QGAGPSRPPT PGRNRYTVMS GTPEKILELL LEAMRPDSSA HDPTETFLSD
     FLLTHSVFMP STQLFTALLH HFHVEPADPA GGSEQEHSTY ICNKRQQILR LVGRWVALYS
     PMLHSDPVAT SFLQKLSDLV SRDARLSNLL REQYPERRRH HRLENGCGNV SPQTKARNAP
     VWLPNQEEPL PSSAGAIRVG DKVPYDICRP DHSVLTLHLP VTASVREVMA ALAHEDHWTK
     GQVLVKVNSA GDVVGLQPDA RGVATSLGLN ERLFVVDPQE VHELTPHPEQ LGPTLGSSEM
     LDLVSAKDLA GQLTDHDWNL FNRIHQVQEH LRDVTTANLE RFMRRFNELQ YWVATELCLC
     PVPGSRAQLL RKFIKLAAHL KEQKNLNSFF AVMFGLSNSA ISRLAHTWER LPHKVRKLYS
     ALERLLDPSW NHRVYRLALT KLSPPVIPFM PLLLKDVTFI HEGNHTLVEN LINFEKMRMM
     ARAVRMLHHC RSHSTAPLSP LRSRVSHIHE DSQGSRISTC SEQSLSTRSP ASTWAYVQQL
     KVIDNQRELS RLSRELEP
//
ID   SPON1_MOUSE             Reviewed;         807 AA.
AC   Q8VCC9; Q8K2Q8;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Spondin-1;
DE   AltName: Full=F-spondin;
DE   Flags: Precursor;
GN   Name=Spon1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129, and FVB/N; TISSUE=Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Cell adhesion protein that promotes the attachment of
CC       spinal cord and sensory neuron cells and the outgrowth of neurites
CC       in vitro. May contribute to the growth and guidance of axons in
CC       both the spinal cord and the PNS (By similarity).
CC   -!- SUBUNIT: Binds to the central extracellular domain of APP and
CC       inhibits beta-secretase cleavage of APP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix (By similarity).
CC   -!- SIMILARITY: Contains 1 reelin domain.
CC   -!- SIMILARITY: Contains 1 spondin domain.
CC   -!- SIMILARITY: Contains 6 TSP type-1 domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH30339.1; Type=Erroneous initiation;
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DR   EMBL; BC020531; AAH20531.1; -; mRNA.
DR   EMBL; BC030339; AAH30339.1; ALT_INIT; mRNA.
DR   IPI; IPI00310907; -.
DR   RefSeq; NP_663559.1; NM_145584.2.
DR   UniGene; Mm.334160; -.
DR   ProteinModelPortal; Q8VCC9; -.
DR   SMR; Q8VCC9; 44-183, 199-411, 441-499, 501-610, 613-720, 753-807.
DR   STRING; Q8VCC9; -.
DR   PRIDE; Q8VCC9; -.
DR   Ensembl; ENSMUST00000046687; ENSMUSP00000041157; ENSMUSG00000038156.
DR   GeneID; 233744; -.
DR   KEGG; mmu:233744; -.
DR   UCSC; uc009jhv.1; mouse.
DR   CTD; 233744; -.
DR   MGI; MGI:2385287; Spon1.
DR   GeneTree; ENSGT00550000074594; -.
DR   HOGENOM; HBG444783; -.
DR   HOVERGEN; HBG052920; -.
DR   InParanoid; Q8VCC9; -.
DR   OMA; GTSYRVT; -.
DR   OrthoDB; EOG4H9XJT; -.
DR   NextBio; 381807; -.
DR   ArrayExpress; Q8VCC9; -.
DR   Bgee; Q8VCC9; -.
DR   Genevestigator; Q8VCC9; -.
DR   GermOnline; ENSMUSG00000038156; Mus musculus.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   InterPro; IPR002861; Reeler_dom.
DR   InterPro; IPR009465; Spondin_N.
DR   InterPro; IPR000884; Thrombospondin_1_rpt.
DR   Pfam; PF02014; Reeler; 1.
DR   Pfam; PF00090; TSP_1; 6.
DR   SMART; SM00209; TSP1; 6.
DR   SUPFAM; SSF82895; TSP1; 6.
DR   PROSITE; PS51019; REELIN; 1.
DR   PROSITE; PS51020; SPONDIN; 1.
DR   PROSITE; PS50092; TSP1; 6.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Repeat; Secreted; Signal.
FT   SIGNAL        1     28       Potential.
FT   CHAIN        29    807       Spondin-1.
FT                                /FTId=PRO_0000035866.
FT   DOMAIN       29    194       Reelin.
FT   DOMAIN      195    388       Spondin.
FT   DOMAIN      442    495       TSP type-1 1.
FT   DOMAIN      501    555       TSP type-1 2.
FT   DOMAIN      558    611       TSP type-1 3.
FT   DOMAIN      614    666       TSP type-1 4.
FT   DOMAIN      668    721       TSP type-1 5.
FT   DOMAIN      754    806       TSP type-1 6.
FT   CARBOHYD    214    214       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    681    681       N-linked (GlcNAc...) (Potential).
FT   DISULFID     44    128       By similarity.
FT   DISULFID    156    182       By similarity.
FT   DISULFID    502    538       By similarity.
FT   DISULFID    513    517       By similarity.
FT   DISULFID    548    554       By similarity.
FT   DISULFID    559    595       By similarity.
FT   DISULFID    570    574       By similarity.
FT   DISULFID    605    610       By similarity.
FT   DISULFID    615    650       By similarity.
FT   DISULFID    626    630       By similarity.
FT   DISULFID    660    665       By similarity.
SQ   SEQUENCE   807 AA;  90821 MW;  3116DF867F4AE563 CRC64;
     MRLSPVSLRL SRGPALLALA LPLAAALAFS DETLDKVTKS EGYCSRILRA QGTRREGYTE
     FSLRVEGDPD FYKPGSSYRV TLSAAPPSYF RGFTLIALKE NQEGDKEEDH AGTFQIIDEE
     ETQFMSNCPV AVTESTPRRR TRIQVFWIAP PTGTGCVILK ASIVQKRIIY FQDEGSLTKK
     LCEQDPTLDG VTDRPILDCC ACGTAKYRLT FYGNWSEKTH PKDYPRRANH WSAIIGGSHS
     KNYVLWEYGG YASEGVKQVA ELGSPVKMEE EIRQQSDEVL TVIKAKAQWP AWQPVNVRAA
     PSAEFSVDRT RHLMSFLTMM GPSPDWNVGL SAEDLCTKEC GWVQKVVQDL IPWDAGTDSG
     VTYESPNKPT IPQEKIRPLT SLDHPQSPFY DPEGGSITQV ARVVIERIAR KGEQCNIVPD
     NVDDIVADLA PEEKDEDDTP ETCIYSNWSP WSACSSSTCE KGKRMRQRML KAQLDLSVPC
     PDTQDFQPCM GPGCSDEDGS TCTMSEWITW SPCSVSCGMG MRSRERYVKQ FPEDGSVCML
     PTEETEKCTV NEECSPSSCL VTEWGEWDDC SATCGMGMKK RHRMVKMSPA DGSMCKAETS
     QAEKCMMPEC HTIPCLLSPW SEWSDCSVTC GKGMRTRQRM LKSLAELGDC NEDLEQAEKC
     MLPECPIDCE LSEWSQWSEC NKSCGKGHMI RTRTIQMEPQ FGGVPCPETV QRKKCRTRKC
     LRSPSVQKLR WREARESRRS EQLREESDGE QFPGCRMRPW TAWSECTKLC GGGIQERYMT
     VKKRFKSSQF TSCKDKKEIR ACNVHPC
//
ID   REEP2_MOUSE             Reviewed;         254 AA.
AC   Q8VCD6;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 2.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Receptor expression-enhancing protein 2;
GN   Name=Reep2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15550249; DOI=10.1016/j.cell.2004.11.021;
RA   Saito H., Kubota M., Roberts R.W., Chi Q., Matsunami H.;
RT   "RTP family members induce functional expression of mammalian odorant
RT   receptors.";
RL   Cell 119:679-691(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May enhance the cell surface expression of odorant
CC       receptors (By similarity).
CC   -!- SUBUNIT: Interacts with odorant receptor proteins (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the DP1 family.
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DR   EMBL; AY562230; AAT70675.1; -; mRNA.
DR   EMBL; BC020184; AAH20184.2; -; mRNA.
DR   IPI; IPI00122032; -.
DR   RefSeq; NP_659114.2; NM_144865.1.
DR   UniGene; Mm.293588; -.
DR   ProteinModelPortal; Q8VCD6; -.
DR   PRIDE; Q8VCD6; -.
DR   Ensembl; ENSMUST00000043484; ENSMUSP00000036065; ENSMUSG00000038555.
DR   GeneID; 225362; -.
DR   KEGG; mmu:225362; -.
DR   UCSC; uc008elr.1; mouse.
DR   CTD; 225362; -.
DR   MGI; MGI:2385070; Reep2.
DR   GeneTree; ENSGT00550000074535; -.
DR   HOGENOM; HBG716753; -.
DR   HOVERGEN; HBG056861; -.
DR   InParanoid; Q8VCD6; -.
DR   OMA; KVPKAEP; -.
DR   OrthoDB; EOG4D7Z6W; -.
DR   PhylomeDB; Q8VCD6; -.
DR   NextBio; 377637; -.
DR   ArrayExpress; Q8VCD6; -.
DR   Bgee; Q8VCD6; -.
DR   CleanEx; MM_REEP2; -.
DR   Genevestigator; Q8VCD6; -.
DR   GermOnline; ENSMUSG00000038555; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR004345; TB2_DP1_HVA22.
DR   PANTHER; PTHR12300; TB2_DP1_HVA22; 1.
DR   Pfam; PF03134; TB2_DP1_HVA22; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    254       Receptor expression-enhancing protein 2.
FT                                /FTId=PRO_0000101824.
FT   TRANSMEM      1     21       Helical; (Potential).
FT   TRANSMEM     35     55       Helical; (Potential).
SQ   SEQUENCE   254 AA;  28437 MW;  63F9770A04B122AC CRC64;
     MVSWIISRLV VLIFGTLYPA YSSYKAVKTK NVKEYVKWMM YWIVFAFFTT AETLTDIILS
     WFPFYFELKI AFVIWLLSPY TKGSSVLYRK FVHPTLSNKE KEIDEYITQA RDKSYETMMR
     VGKRGLNLAA NAAVTAAAKG QGVLSEKLRS FSMQDLTLIR DEDALPLQGP DGRLQPGPVG
     LLDTIEDLGD EPALSLRSST SQPDPRTETS EDDLGDKAPK RTKPIKKVPR AEPPASKTLK
     TRPKKKSSGG GDSA
//
ID   GPN1_MOUSE              Reviewed;         372 AA.
AC   Q8VCE2;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=GPN-loop GTPase 1;
DE   AltName: Full=MBD2-interacting protein;
DE            Short=MBDin;
DE   AltName: Full=XPA-binding protein 1;
GN   Name=Gpn1; Synonyms=Mbdin, Xab1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Forms an interface between the RNA polymerase II enzyme
CC       and chaperone/scaffolding protein, suggesting that it is required
CC       to connect RNA polymerase II to regulators of protein complex
CC       formation. May be involved in nuclear localization of XPA (By
CC       similarity).
CC   -!- SUBUNIT: Tightly associated with the RNA polymerase II complex.
CC       Interacts with XPA (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the GPN-loop GTPase family.
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DR   EMBL; AK077645; BAC36923.1; -; mRNA.
DR   EMBL; BC020174; AAH20174.1; -; mRNA.
DR   IPI; IPI00122054; -.
DR   RefSeq; NP_598517.1; NM_133756.4.
DR   UniGene; Mm.348649; -.
DR   ProteinModelPortal; Q8VCE2; -.
DR   SMR; Q8VCE2; 14-261.
DR   STRING; Q8VCE2; -.
DR   PhosphoSite; Q8VCE2; -.
DR   PRIDE; Q8VCE2; -.
DR   Ensembl; ENSMUST00000076949; ENSMUSP00000076217; ENSMUSG00000064037.
DR   GeneID; 74254; -.
DR   KEGG; mmu:74254; -.
DR   UCSC; uc008wyi.1; mouse.
DR   CTD; 74254; -.
DR   MGI; MGI:1921504; Gpn1.
DR   GeneTree; ENSGT00550000074926; -.
DR   HOGENOM; HBG460599; -.
DR   HOVERGEN; HBG047768; -.
DR   InParanoid; Q8VCE2; -.
DR   OMA; TPPYVIN; -.
DR   OrthoDB; EOG41NTMK; -.
DR   PhylomeDB; Q8VCE2; -.
DR   NextBio; 340254; -.
DR   ArrayExpress; Q8VCE2; -.
DR   Bgee; Q8VCE2; -.
DR   Genevestigator; Q8VCE2; -.
DR   GermOnline; ENSMUSG00000064037; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR004130; Uncharacterised_ATP-bd.
DR   Pfam; PF03029; ATP_bind_1; 1.
DR   SMART; SM00382; AAA; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; GTP-binding; Nucleotide-binding;
KW   Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    372       GPN-loop GTPase 1.
FT                                /FTId=PRO_0000066002.
FT   NP_BIND      26     33       GTP (Pootential).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     314    314       Phosphoserine (By similarity).
FT   MOD_RES     338    338       Phosphoserine.
FT   MOD_RES     340    340       Phosphothreonine (By similarity).
SQ   SEQUENCE   372 AA;  41598 MW;  8AD50C8B6E5D1E6A CRC64;
     MAAPVAPSEP QASRAPQPPV CLLVLGMAGS GKTTFVQRLT GHLHNKGCPP YVINLDPAVH
     EVPFPANIDI RDTVKYKEVM KQYGLGPNGG IVTSLNLFAT RFDQVMKFIE KAQNTFRYVL
     IDTPGQIEVF TWSASGTIIT EALASSFPTV VIYVMDTSRS TNPVTFMSNM LYACSILYKT
     KLPFIVVMNK TDIIDHSFAV EWMQDFEAFQ DALNQETTYV SNLTRSMSLV LDEFYSSLRV
     VGVSAVVGTG FDELCTQVTS AAEEYEREYR PEYERLKKSL ANAQSNQQKE QLERLRKDMG
     SVALDPEAGK GNASPVLDPS DLILTRGTLD EEDEEADSDT DDIDHRVTEE SREEPAFQNF
     MEESMAHWKR NK
//
ID   PKHH3_MOUSE             Reviewed;         796 AA.
AC   Q8VCE9; Q3U3Z6; Q8R1H2;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Pleckstrin homology domain-containing family H member 3;
DE            Short=PH domain-containing family H member 3;
DE   Flags: Precursor;
GN   Name=Plekhh3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 384-796 (ISOFORM 3).
RC   STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8VCE9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VCE9-2; Sequence=VSP_029399;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8VCE9-3; Sequence=VSP_029399, VSP_029400, VSP_029401;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q8VCE9-4; Sequence=VSP_029400, VSP_029401;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -!- SIMILARITY: Contains 1 MyTH4 domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK154510; BAE32639.1; -; mRNA.
DR   EMBL; AL590969; CAM19574.1; -; Genomic_DNA.
DR   EMBL; BC020025; AAH20025.1; -; mRNA.
DR   EMBL; BC024538; AAH24538.1; -; mRNA.
DR   IPI; IPI00122067; -.
DR   IPI; IPI00462510; -.
DR   IPI; IPI00875725; -.
DR   IPI; IPI00875990; -.
DR   RefSeq; NP_666142.1; NM_146030.2.
DR   UniGene; Mm.273254; -.
DR   ProteinModelPortal; Q8VCE9; -.
DR   SMR; Q8VCE9; 95-198.
DR   PhosphoSite; Q8VCE9; -.
DR   PRIDE; Q8VCE9; -.
DR   Ensembl; ENSMUST00000043397; ENSMUSP00000046044; ENSMUSG00000035172.
DR   GeneID; 217198; -.
DR   KEGG; mmu:217198; -.
DR   UCSC; uc007lnq.1; mouse.
DR   CTD; 217198; -.
DR   MGI; MGI:2384950; Plekhh3.
DR   eggNOG; roNOG04121; -.
DR   GeneTree; ENSGT00440000034464; -.
DR   HOGENOM; HBG446187; -.
DR   HOVERGEN; HBG052553; -.
DR   InParanoid; Q8VCE9; -.
DR   OMA; DSPDSGW; -.
DR   OrthoDB; EOG495ZR9; -.
DR   PhylomeDB; Q8VCE9; -.
DR   NextBio; 375629; -.
DR   ArrayExpress; Q8VCE9; -.
DR   Bgee; Q8VCE9; -.
DR   Genevestigator; Q8VCE9; -.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR000857; MyTH4_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000159; Ras-assoc.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF00784; MyTH4; 1.
DR   Pfam; PF00788; RA; 1.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   PROSITE; PS00660; FERM_1; FALSE_NEG.
DR   PROSITE; PS00661; FERM_2; FALSE_NEG.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS51016; MYTH4; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Phosphoprotein; Signal.
FT   SIGNAL        1     18       Potential.
FT   CHAIN        19    796       Pleckstrin homology domain-containing
FT                                family H member 3.
FT                                /FTId=PRO_0000311109.
FT   DOMAIN       95    199       PH.
FT   DOMAIN      237    399       MyTH4.
FT   DOMAIN      404    757       FERM.
FT   MOD_RES      30     30       Phosphoserine (By similarity).
FT   CARBOHYD    474    474       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     471    474       RFEN -> S (in isoform 2 and isoform 3).
FT                                /FTId=VSP_029399.
FT   VAR_SEQ     664    705       YDVLELSTEPGGGAPQKLCLGLGAKAMSLSRPGETEPIHSV
FT                                S -> SLVEVLHRSSAWVWEQRPCRSPGLVRQNPSTVSAMV
FT                                MWPPAS (in isoform 3 and isoform 4).
FT                                /FTId=VSP_029400.
FT   VAR_SEQ     706    796       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_029401.
SQ   SEQUENCE   796 AA;  85842 MW;  343C40578FBC0F24 CRC64;
     MPLPGGLWWL LCCRRGFTLL HRDYGDGELS GDGDEDEDDE TFELRTPSPA GGGRGSLDVT
     LTQPTRNGPI SDRLQGWEET WSLIPDKGLP EEDPDIIVKG WLYREPRGGG ARPWLLPRRA
     WFVLTRDSLD QFSSSGKGAR RLGSLVLTSL CSVTGPERRP KETGLWSVTV SGRKHSIRLC
     SPRQAEAERW GVALREVIAS KAPLETPTQL LLRDIQESCG DPEAVALIYR RNPILRHTSS
     ALYAPLLPLP YEVSAPGPGY APLREEAVRL FLALQALEGA RRPGPLMQGV LQTCRDLPAL
     QDELFLQLAK QTSGPAGPPG LPATQDPATL RYWQLLTCMS CTFRPGGAVR GHLLGHLERT
     EQALPDSELA EYARFIRKAL GRTRGRELVP SLAEISALSR RQELLCTVHC PGAGACPVSI
     DSHTTAGEVA RELVGRLGLA RSRNAFALYE QRGAQERALA GGTLVADVLT RFENLTSEEA
     GLEDSPDCGW RLCLRLHGPL HPEGLSPEGH ELPFLFEQAH ALLLRGRPPP PEDTLRALAA
     LRLQSLHRDF SPRGPLPLLD RLLPPPIPPR EQPPCPTRRP PPSAALLAGA LWSPGLAKRR
     AERARRGGTG RSTGSTAQVG GGGASTTAAV LGGWKRLRGM GQAEAMAAYL ALAAQCPGFG
     AARYDVLELS TEPGGGAPQK LCLGLGAKAM SLSRPGETEP IHSVSYGHVA ACQLIGPHTL
     ALRVGDSQLL LQSPQVEEIM ELVNAYLANP SPERPCRSGS SSGPPSQDLP DTSPPSQHQV
     LEEPQGQSGC LKQLQD
//
ID   PEX19_MOUSE             Reviewed;         299 AA.
AC   Q8VCI5; Q4FJU7; Q8CEE1; Q921H0; Q9CZC1; Q9QUQ1;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Peroxisomal biogenesis factor 19;
DE   AltName: Full=Peroxin-19;
DE   AltName: Full=Peroxisomal farnesylated protein;
DE            Short=PxF;
DE   Flags: Precursor;
GN   Name=Pex19; Synonyms=Pxf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC   STRAIN=129/SvJ, and BALB/c; TISSUE=Liver, and Lung;
RA   Kammerer S.;
RL   Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Head, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E.,
RA   Mollenhauer J., Wiemann S., Schick M., Korn B.;
RT   "Cloning of mouse full open reading frames in Gateway(R) system entry
RT   vector (pDONR201).";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 218-227, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: Necessary for early peroxisomal biogenesis. Acts both as
CC       a cytosolic chaperone and as an import receptor for peroxisomal
CC       membrane proteins (PMPs). Binds and stabilizes newly synthesized
CC       PMPs in the cytoplasm by interacting with their hydrophobic
CC       membrane-spanning domains, and targets them to the peroxisome
CC       membrane by binding to the integral membrane protein PEX3.
CC       Excludes CDKN2A from the nucleus and prevents its interaction with
CC       MDM2, which results in active degradation of TP53 (By similarity).
CC   -!- SUBUNIT: Interacts with a broad range of peroxisomal membrane
CC       proteins, including PEX3, PEX10, PEX11A, PEX11B, PEX12, PEX13,
CC       PEX14 and PEX16, PXMP2/PMP22, PXMP4/PMP24, SLC25A17/PMP34,
CC       ABCD1/ALDP, ABCD2/ALDRP, and ABCD3/PMP70. Also interacts with the
CC       tumor suppressor CDKN2A/p19ARF (By similarity).
CC   -!- INTERACTION:
CC       Q64364-1:Cdkn2a; NbExp=1; IntAct=EBI-1810767, EBI-1202306;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Peroxisome
CC       membrane; Lipid-anchor; Cytoplasmic side (By similarity).
CC       Note=Mainly cytoplasmic, some fraction membrane-associated to the
CC       outer surface of peroxisomes (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VCI5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VCI5-2; Sequence=VSP_012652;
CC   -!- SIMILARITY: Belongs to the peroxin-19 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; Y09046; CAA70255.1; -; mRNA.
DR   EMBL; Y09047; CAA70256.1; -; Genomic_DNA.
DR   EMBL; AK012785; BAB28468.1; -; mRNA.
DR   EMBL; AK028449; BAC25957.1; -; mRNA.
DR   EMBL; AK029368; BAC26421.1; -; mRNA.
DR   EMBL; CT010305; CAJ18513.1; -; mRNA.
DR   EMBL; BC012517; AAH12517.1; -; mRNA.
DR   EMBL; BC019767; AAH19767.1; -; mRNA.
DR   IPI; IPI00319131; -.
DR   IPI; IPI00407358; -.
DR   RefSeq; NP_001152997.1; NM_001159525.1.
DR   RefSeq; NP_075528.3; NM_023041.3.
DR   UniGene; Mm.247764; -.
DR   ProteinModelPortal; Q8VCI5; -.
DR   SMR; Q8VCI5; 171-280.
DR   IntAct; Q8VCI5; 4.
DR   STRING; Q8VCI5; -.
DR   PhosphoSite; Q8VCI5; -.
DR   PRIDE; Q8VCI5; -.
DR   Ensembl; ENSMUST00000075895; ENSMUSP00000075289; ENSMUSG00000003464.
DR   Ensembl; ENSMUST00000111252; ENSMUSP00000106883; ENSMUSG00000003464.
DR   GeneID; 19298; -.
DR   KEGG; mmu:19298; -.
DR   CTD; 19298; -.
DR   MGI; MGI:1334458; Pex19.
DR   GeneTree; ENSGT00390000010993; -.
DR   HOGENOM; HBG716659; -.
DR   HOVERGEN; HBG053573; -.
DR   InParanoid; Q8VCI5; -.
DR   OMA; LQNSGMS; -.
DR   OrthoDB; EOG40K80Z; -.
DR   PhylomeDB; Q8VCI5; -.
DR   NextBio; 296241; -.
DR   ArrayExpress; Q8VCI5; -.
DR   Bgee; Q8VCI5; -.
DR   CleanEx; MM_PEX19; -.
DR   Genevestigator; Q8VCI5; -.
DR   GermOnline; ENSMUSG00000003464; Mus musculus.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR006708; Pex19.
DR   PANTHER; PTHR12774; Pex19; 1.
DR   Pfam; PF04614; Pex19; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Direct protein sequencing;
KW   Lipoprotein; Membrane; Methylation; Peroxisome; Peroxisome biogenesis;
KW   Phosphoprotein; Prenylation.
FT   CHAIN         1    296       Peroxisomal biogenesis factor 19.
FT                                /FTId=PRO_0000218760.
FT   PROPEP      297    299       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000396701.
FT   REGION        1     91       Necessary for PEX19 function on
FT                                peroxisome biogenesis (By similarity).
FT   REGION        1     56       Docking to the peroxisome membrane and
FT                                binding to PEX3 (By similarity).
FT   MOD_RES      35     35       Phosphoserine (By similarity).
FT   MOD_RES     146    146       Phosphoserine (By similarity).
FT   MOD_RES     149    149       Phosphoserine (By similarity).
FT   MOD_RES     177    177       Phosphoserine (By similarity).
FT   MOD_RES     184    184       Phosphoserine (By similarity).
FT   MOD_RES     296    296       Cysteine methyl ester (By similarity).
FT   LIPID       296    296       S-farnesyl cysteine (By similarity).
FT   VAR_SEQ      25    116       Missing (in isoform 2).
FT                                /FTId=VSP_012652.
FT   CONFLICT     31     31       K -> E (in Ref. 2; BAB28468).
FT   CONFLICT     55     55       P -> S (in Ref. 1; CAA70255/CAA70256 and
FT                                3; AAH12517).
FT   CONFLICT    110    110       E -> K (in Ref. 2; BAB28468).
SQ   SEQUENCE   299 AA;  32733 MW;  530A3A0C29370E51 CRC64;
     MAAAEEGCGV GVEDDRELEE LLESALDDFD KAKPSPEHAP TISAPDASGP QKRAPGDTAK
     DALFASQEKF FQELFDSELA SQATAEFEKA MKELAEEEPH LVEQFQKLSE AAGRVGSDAS
     SQQEFTSCLK ETLSGLAKNA TELQNSGMSE EELMKAMEGL GMDEGDGEAS ILPIMQSIMQ
     NLLSKDVLYP SLKEITEKYP EWLQSHQDST PPEQFEKYQQ QHSVMVKICE QFEAETPTDS
     EATQRARFEA MLDLMQQLQA LGHPPKELAG EMPPGLNFDL DALNLSGPPG ANGEQCLIM
//
ID   MUL1_MOUSE              Reviewed;         352 AA.
AC   Q8VCM5; A2AM82; A2AM84; B5M498; Q3TDK4; Q8BHF2; Q9DCV9;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Mitochondrial ubiquitin ligase activator of NFKB 1;
DE            EC=6.3.2.-;
DE   AltName: Full=E3 ubiquitin-protein ligase MUL1;
DE   AltName: Full=Growth inhibition and death E3 ligase;
GN   Name=Mul1; Synonyms=Gide;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=18591963; DOI=10.1038/cr.2008.75;
RA   Zhang B., Huang J., Li H.-L., Liu T., Wang Y.-Y., Waterman P.,
RA   Mao A.-P., Xu L.-G., Zhai Z., Liu D., Marrack P., Shu H.-B.;
RT   "GIDE is a mitochondrial E3 ubiquitin ligase that induces apoptosis
RT   and slows growth.";
RL   Cell Res. 18:900-910(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Brain cortex, Head, Kidney, Liver, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that plays a role in the
CC       control of mitochondrial morphology. Promotes mitochondrial
CC       fragmentation and influences mitochondrial localization. Inhibits
CC       cell growth. When overexpressed, activates JNK through MAP3K7/TAK1
CC       and induces caspase-dependent apoptosis. E3 ubiquitin ligases
CC       accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the
CC       form of a thioester and then directly transfer the ubiquitin to
CC       targeted substrates (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Homooligomer. Interacts with MAP3K7/TAK1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass
CC       membrane protein (By similarity). Peroxisome (By similarity).
CC       Note=Transported in mitochondrion-derived vesicles from the
CC       mitochondrion to the peroxisome (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8VCM5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VCM5-2; Sequence=VSP_034454, VSP_034455;
CC         Note=Gene prediction based on EST data;
CC       Name=3;
CC         IsoId=Q8VCM5-3; Sequence=VSP_034453;
CC         Note=Gene prediction based on EST data;
CC   -!- DOMAIN: The zinc finger domain is required for E3 ligase activity
CC       (By similarity).
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; EU935009; ACH72646.1; -; mRNA.
DR   EMBL; AK002416; BAB22084.1; -; mRNA.
DR   EMBL; AK044088; BAC31768.1; -; mRNA.
DR   EMBL; AK076419; BAC36332.1; -; mRNA.
DR   EMBL; AK083295; BAC38848.1; -; mRNA.
DR   EMBL; AK153956; BAE32279.1; -; mRNA.
DR   EMBL; AK170149; BAE41597.1; -; mRNA.
DR   EMBL; AL807249; CAM18879.1; -; Genomic_DNA.
DR   EMBL; AL807249; CAM18880.1; -; Genomic_DNA.
DR   EMBL; AL807249; CAM18881.1; -; Genomic_DNA.
DR   EMBL; BC019516; AAH19516.1; -; mRNA.
DR   IPI; IPI00308263; -.
DR   IPI; IPI00649455; -.
DR   IPI; IPI00649724; -.
DR   RefSeq; NP_080965.2; NM_026689.3.
DR   UniGene; Mm.103413; -.
DR   ProteinModelPortal; Q8VCM5; -.
DR   SMR; Q8VCM5; 299-344.
DR   STRING; Q8VCM5; -.
DR   PRIDE; Q8VCM5; -.
DR   Ensembl; ENSMUST00000044058; ENSMUSP00000039604; ENSMUSG00000041241.
DR   Ensembl; ENSMUST00000105814; ENSMUSP00000101440; ENSMUSG00000041241.
DR   GeneID; 68350; -.
DR   KEGG; mmu:68350; -.
DR   CTD; 68350; -.
DR   MGI; MGI:1915600; Mul1.
DR   eggNOG; roNOG08858; -.
DR   GeneTree; ENSGT00390000012141; -.
DR   HOVERGEN; HBG106376; -.
DR   InParanoid; Q8VCM5; -.
DR   OMA; VIGHYIS; -.
DR   OrthoDB; EOG4D26Q3; -.
DR   PhylomeDB; Q8VCM5; -.
DR   NextBio; 461442; -.
DR   ArrayExpress; Q8VCM5; -.
DR   Bgee; Q8VCM5; -.
DR   Genevestigator; Q8VCM5; -.
DR   GO; GO:0031307; C:integral to mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0004871; F:signal transducer activity; ISS:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006919; P:activation of caspase activity; ISS:UniProtKB.
DR   GO; GO:0007257; P:activation of JUN kinase activity; ISS:UniProtKB.
DR   GO; GO:0006917; P:induction of apoptosis; ISS:UniProtKB.
DR   GO; GO:0000266; P:mitochondrial fission; ISS:UniProtKB.
DR   GO; GO:0051646; P:mitochondrion localization; ISS:UniProtKB.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; ISS:UniProtKB.
DR   InterPro; IPR022170; GIDE.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF12483; GIDE; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Apoptosis; Ligase; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion outer membrane; Peroxisome;
KW   Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    352       Mitochondrial ubiquitin ligase activator
FT                                of NFKB 1.
FT                                /FTId=PRO_0000277662.
FT   TOPO_DOM      1      8       Cytoplasmic (Potential).
FT   TRANSMEM      9     29       Helical; (Potential).
FT   TOPO_DOM     30    238       Mitochondrial intermembrane (Potential).
FT   TRANSMEM    239    259       Helical; (Potential).
FT   TOPO_DOM    260    352       Cytoplasmic (Potential).
FT   ZN_FING     302    340       RING-type.
FT   VAR_SEQ       1     40       MESGSRPSLGQVILLGTSSMVTAVLYSIYRQKAQVAQELK
FT                                -> MVVVLCWLEFHSPSAKDLFWQLYGRWTLEPKSYHQ
FT                                (in isoform 3).
FT                                /FTId=VSP_034453.
FT   VAR_SEQ     111    123       NDYSKIIHQRTNT -> CVSSGFYTSEVVV (in
FT                                isoform 2).
FT                                /FTId=VSP_034454.
FT   VAR_SEQ     124    352       Missing (in isoform 2).
FT                                /FTId=VSP_034455.
FT   CONFLICT     38     38       E -> V (in Ref. 2; BAE41597).
FT   CONFLICT    208    208       V -> F (in Ref. 2; BAB22084).
FT   CONFLICT    242    242       I -> V (in Ref. 1; ACH72646 and 4;
FT                                AAH19516).
SQ   SEQUENCE   352 AA;  39835 MW;  252530F1BD917871 CRC64;
     MESGSRPSLG QVILLGTSSM VTAVLYSIYR QKAQVAQELK GAKKIHLGED LKGILSEAPG
     KCVPYAVIEG AVRSVKETLN SQFVENCKGV IQRLSLQEHK MVWNRTTHLW NDYSKIIHQR
     TNTVPFDLVP HEDGVAVSVR VLKPLDSVDL GLETVYEKFH PSVQSFTDAI GHYISGERPK
     GIQETEEMLK VGATLTGIGE LVLDNNAVRL QPPKQGMQYY LSSQDFDSLL HRQESSVRLW
     KILVLVFGFA TCATLFFILR KQYLHRQERL RQQQLQEEFL EHEAQLLSQA SPEDRESLKS
     ACVVCLSNFK SCVFLECGHV CSCRQCYLAL PEPKRCPICR REITRVIPLY NS
//
ID   FIBG_MOUSE              Reviewed;         436 AA.
AC   Q8VCM7; Q8WUR3; Q91ZP0;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Fibrinogen gamma chain;
DE   Flags: Precursor;
GN   Name=Fgg;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 170-352.
RA   Murakawa M., Freeman M.W.;
RT   "Mouse fibrinogen gamma-chain.";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Fibrinogen has a double function: yielding monomers that
CC       polymerize into fibrin and acting as a cofactor in platelet
CC       aggregation (By similarity).
CC   -!- SUBUNIT: Heterohexamer; disulfide linked. Contains 2 sets of 3
CC       non-identical chains (alpha, beta and gamma). The 2 heterotrimers
CC       are in head to head conformation with the N-termini in a small
CC       central domain (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- DOMAIN: A long coiled coil structure formed by 3 polypeptide
CC       chains connects the central nodule to the C-terminal domains
CC       (distal nodules). The long C-terminal ends of the alpha chains
CC       fold back, contributing a fourth strand to the coiled coil
CC       structure.
CC   -!- PTM: Conversion of fibrinogen to fibrin is triggered by thrombin,
CC       which cleaves fibrinopeptides A and B from alpha and beta chains,
CC       and thus exposes the N-terminal polymerization sites responsible
CC       for the formation of the soft clot. The soft clot is converted
CC       into the hard clot by factor XIIIA which catalyzes the epsilon-
CC       (gamma-glutamyl)lysine cross-linking between gamma chains
CC       (stronger) and between alpha chains (weaker) of different monomers
CC       (By similarity).
CC   -!- SIMILARITY: Contains 1 fibrinogen C-terminal domain.
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DR   EMBL; BC019506; AAH19506.1; -; mRNA.
DR   EMBL; BC019828; AAH19828.1; -; mRNA.
DR   EMBL; AF413206; AAL02226.1; -; mRNA.
DR   IPI; IPI00122312; -.
DR   RefSeq; NP_598623.1; NM_133862.1.
DR   UniGene; Mm.16422; -.
DR   ProteinModelPortal; Q8VCM7; -.
DR   SMR; Q8VCM7; 27-420.
DR   STRING; Q8VCM7; -.
DR   REPRODUCTION-2DPAGE; Q8VCM7; -.
DR   PRIDE; Q8VCM7; -.
DR   Ensembl; ENSMUST00000048486; ENSMUSP00000037018; ENSMUSG00000033860.
DR   GeneID; 99571; -.
DR   KEGG; mmu:99571; -.
DR   UCSC; uc008ppe.1; mouse.
DR   CTD; 99571; -.
DR   MGI; MGI:95526; Fgg.
DR   GeneTree; ENSGT00600000084261; -.
DR   HOVERGEN; HBG099783; -.
DR   InParanoid; Q8VCM7; -.
DR   OMA; DNDKFEG; -.
DR   OrthoDB; EOG4WH8M3; -.
DR   PhylomeDB; Q8VCM7; -.
DR   NextBio; 354021; -.
DR   ArrayExpress; Q8VCM7; -.
DR   Bgee; Q8VCM7; -.
DR   CleanEx; MM_FGG; -.
DR   Genevestigator; Q8VCM7; -.
DR   GermOnline; ENSMUSG00000033860; Mus musculus.
DR   GO; GO:0005938; C:cell cortex; IDA:MGI.
DR   GO; GO:0005577; C:fibrinogen complex; IEA:InterPro.
DR   GO; GO:0030674; F:protein binding, bridging; IEA:InterPro.
DR   GO; GO:0005102; F:receptor binding; IEA:InterPro.
DR   GO; GO:0030168; P:platelet activation; IEA:InterPro.
DR   GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR002181; Fibrinogen_a/b/g_C.
DR   InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR   InterPro; IPR014715; Fibrinogen_a/b/g_C_2.
DR   InterPro; IPR012290; Fibrinogen_a/b/g_coil_dom.
DR   InterPro; IPR020837; Fibrinogen_CS.
DR   Gene3D; G3DSA:3.90.215.10; Fibrinogen_a/b/g_C_1; 1.
DR   Gene3D; G3DSA:4.10.530.10; Fibrinogen_a/b/g_C_2; 1.
DR   Gene3D; G3DSA:1.20.5.50; Fibrinogen_a/b/g_coil; 1.
DR   Pfam; PF08702; Fib_alpha; 1.
DR   Pfam; PF00147; Fibrinogen_C; 1.
DR   SMART; SM00186; FBG; 1.
DR   SUPFAM; SSF56496; Fibrinogen_a/b/g_C; 1.
DR   PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE   2: Evidence at transcript level;
KW   Blood coagulation; Calcium; Coiled coil; Disulfide bond; Glycoprotein;
KW   Isopeptide bond; Secreted; Signal.
FT   SIGNAL        1     25       By similarity.
FT   CHAIN        26    436       Fibrinogen gamma chain.
FT                                /FTId=PRO_0000009100.
FT   DOMAIN      169    415       Fibrinogen C-terminal.
FT   CA_BIND     340    354       By similarity.
FT   CARBOHYD     77     77       N-linked (GlcNAc...) (Potential).
FT   DISULFID     33     33       Interchain (with gamma chain) (By
FT                                similarity).
FT   DISULFID     34     34       Interchain (with gamma chain) (By
FT                                similarity).
FT   DISULFID     44     44       Interchain (with beta chain) (By
FT                                similarity).
FT   DISULFID     48     48       Interchain (with alpha chain) (By
FT                                similarity).
FT   DISULFID    160    160       Interchain (with beta chain) (By
FT                                similarity).
FT   DISULFID    164    164       Interchain (with gamma chain) (By
FT                                similarity).
FT   DISULFID    178    207       By similarity.
FT   DISULFID    351    364       By similarity.
FT   CROSSLNK    423    423       Isoglutamyl lysine isopeptide (Gln-Lys)
FT                                (interchain with K-431) (By similarity).
FT   CROSSLNK    431    431       Isoglutamyl lysine isopeptide (Lys-Gln)
FT                                (interchain with Q-423) (By similarity).
SQ   SEQUENCE   436 AA;  49391 MW;  FF45A34B6C92143E CRC64;
     MSWSLQPPSF LLCCLLLLFS PTGLAYVATR DNCCILDERF GSFCPTTCGI ADFLSSYQTD
     VDNDLRTLED ILFRAENRTT EAKELIKAIQ VYYNPDQPPK PGMIDSATQK SKKMVEEIVK
     YEALLLTHET SIRYLQEIYN SNNQKITNLK QKVAQLEAQC QEPCKDSVQI HDTTGKDCQE
     IANKGAKESG LYFIRPLKAK QQFLVYCEID GSGNGWTVLQ KRIDGSLDFK KNWIQYKEGF
     GHLSPTGTTE FWLGNEKIHL ISMQSTIPYA LRIQLKDWNG RTSTADYAMF RVGPESDKYR
     LTYAYFIGGD AGDAFDGYDF GDDPSDKFFT SHNGMQFSTW DNDNDKFEGN CAEQDGSGWW
     MNKCHAGHLN GVYHQGGTYS KSSTTNGFDD GIIWATWKSR WYSMKETTMK IIPFNRLSIG
     EGQQHHMGGS KQAGDV
//
ID   CGL_MOUSE               Reviewed;         398 AA.
AC   Q8VCN5; Q6H324;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Cystathionine gamma-lyase;
DE            EC=4.4.1.1;
DE   AltName: Full=Gamma-cystathionase;
GN   Name=Cth;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICTIY.
RC   STRAIN=129/SvJ, and C57BL/6J; TISSUE=Kidney, and Spleen;
RX   PubMed=15038791;
RA   Ishii I., Akahoshi N., Yu X.-N., Kobayashi Y., Namekata K., Komaki G.,
RA   Kimura H.;
RT   "Murine cystathionine gamma-lyase: complete cDNA and genomic
RT   sequences, promoter activity, tissue distribution and developmental
RT   expression.";
RL   Biochem. J. 381:113-123(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   DISRUPTION PHENOTYPE, FUNCTION, INTERACTION WITH CALM, AND ENZYME
RP   REGULATION.
RX   PubMed=18948540; DOI=10.1126/science.1162667;
RA   Yang G., Wu L., Jiang B., Yang W., Qi J., Cao K., Meng Q.,
RA   Mustafa A.K., Mu W., Zhang S., Snyder S.H., Wang R.;
RT   "H2S as a physiologic vasorelaxant: hypertension in mice with deletion
RT   of cystathionine gamma-lyase.";
RL   Science 322:587-590(2008).
CC   -!- FUNCTION: Catalyzes the last step in the transsulfuration pathway
CC       from methionine to cysteine. Has broad substrate specificity.
CC       Converts cystathionine to cysteine, ammonia and 2-oxobutanoate.
CC       Converts two cysteine molecules to lanthionine and hydrogen
CC       sulfide. Can also accept homocysteine as substrate. Specificity
CC       depends on the levels of the endogenous substrates. Generates the
CC       endogenous signaling molecule hydrogen sulfide (H2S), and so
CC       contributes to the regulation of blood pressure.
CC   -!- CATALYTIC ACTIVITY: L-cystathionine + H(2)O = L-cysteine + NH(3) +
CC       2-oxobutanoate.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- ENZYME REGULATION: Activated by calmodulin in the presence of
CC       calcium ions.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-
CC       cysteine from L-homocysteine and L-serine: step 2/2.
CC   -!- SUBUNIT: Homotetramer (By similarity). Interacts with CALM in a
CC       calcium-dependent manner.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: Detected in liver and kidney, and at lower
CC       levels in small intestine (at protein level). Highly expressed in
CC       liver and kidney. detected at lower levels in stomach, small
CC       intestine and adipose tissue.
CC   -!- DEVELOPMENTAL STAGE: First detected at low levels in embryonic
CC       liver after 12.5 days of embryonic development. Highly expressed
CC       in liver and kidney after 18.5 days of embryonic development.
CC       Expressed at high levels in liver and kidney after birth and in
CC       adults.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype at birth. Mice exhibit
CC       strongly decreased levels of hydrogen sulfide (H2S) in heart and
CC       aorta. Hydrogen sulfide serum levels are also lower than normal.
CC       No effect on brain hydrogen sulfide levels. Mice develop
CC       hypertension beginning at about seven weeks of age.
CC   -!- SIMILARITY: Belongs to the trans-sulfuration enzymes family.
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DR   EMBL; AY083352; AAL99218.1; -; mRNA.
DR   EMBL; AY262829; AAP86975.1; -; Genomic_DNA.
DR   EMBL; CH466532; EDL11858.1; -; Genomic_DNA.
DR   EMBL; BC019483; AAH19483.1; -; mRNA.
DR   IPI; IPI00122344; -.
DR   RefSeq; NP_666065.1; NM_145953.2.
DR   UniGene; Mm.28301; -.
DR   ProteinModelPortal; Q8VCN5; -.
DR   SMR; Q8VCN5; 9-398.
DR   STRING; Q8VCN5; -.
DR   PhosphoSite; Q8VCN5; -.
DR   PRIDE; Q8VCN5; -.
DR   Ensembl; ENSMUST00000118539; ENSMUSP00000113672; ENSMUSG00000028179.
DR   GeneID; 107869; -.
DR   KEGG; mmu:107869; -.
DR   UCSC; uc008rvj.1; mouse.
DR   CTD; 107869; -.
DR   MGI; MGI:1339968; Cth.
DR   GeneTree; ENSGT00390000000312; -.
DR   HOGENOM; HBG754729; -.
DR   HOVERGEN; HBG005322; -.
DR   InParanoid; Q8VCN5; -.
DR   OrthoDB; EOG4FXR7K; -.
DR   PhylomeDB; Q8VCN5; -.
DR   BRENDA; 4.4.1.1; 244.
DR   NextBio; 359617; -.
DR   ArrayExpress; Q8VCN5; -.
DR   Bgee; Q8VCN5; -.
DR   CleanEx; MM_CTH; -.
DR   Genevestigator; Q8VCN5; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004123; F:cystathionine gamma-lyase activity; ISS:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR   GO; GO:0019344; P:cysteine biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0018272; P:protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine; ISS:UniProtKB.
DR   InterPro; IPR000277; Cys/Met-Metab_PyrdxlP-dep_enz.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase_major_dom.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1.
DR   PANTHER; PTHR11808; Cys_Met_Meta_PP; 1.
DR   Pfam; PF01053; Cys_Met_Meta_PP; 1.
DR   PIRSF; PIRSF001434; CGS; 1.
DR   SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR   PROSITE; PS00868; CYS_MET_METAB_PP; 1.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Cysteine biosynthesis; Cytoplasm; Lyase;
KW   Phosphoprotein; Pyridoxal phosphate.
FT   CHAIN         1    398       Cystathionine gamma-lyase.
FT                                /FTId=PRO_0000114751.
FT   BINDING      61     61       Substrate (By similarity).
FT   BINDING     113    113       Substrate (By similarity).
FT   BINDING     118    118       Substrate (By similarity).
FT   BINDING     338    338       Substrate (By similarity).
FT   MOD_RES     211    211       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
FT   MOD_RES     376    376       Phosphoserine.
SQ   SEQUENCE   398 AA;  43567 MW;  B2F89625B9978599 CRC64;
     MQKDASLSGF LPSFQHFATQ AIHVGQEPEQ WNSRAVVLPI SLATTFKQDF PGQSSGFEYS
     RSGNPTRNCL EKAVAALDGA KHSLAFASGL AATITITHLL KAGDEIICMD EVYGGTNRYF
     RRVASEFGLK ISFVDCSKTK LLEAAITPQT KLVWIETPTN PTLKLADIGA CAQIVHKRGD
     IILVVDNTFM SAYFQRPLAL GADICMCSAT KYMNGHSDVV MGLVSVNSDD LNSRLRFLQN
     SLGAVPSPFD CYLCCRGLKT LQVRMEKHFK NGMAVARFLE TNPRVEKVVY PGLPSHPQHE
     LAKRQCSGCP GMVSFYIKGA LQHAKAFLKN LKLFTLAESL GGYESLAELP AIMTHASVPE
     KDRATLGIND TLIRLSVGLE DEQDLLEDLD RALKAAHP
//
ID   NRBF2_MOUSE             Reviewed;         287 AA.
AC   Q8VCQ3; Q9DCG3;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Nuclear receptor-binding factor 2;
DE            Short=NRBF-2;
GN   Name=Nrbf2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   STRUCTURE BY NMR OF 4-86.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of MIT domain from mouse Nrbf-2.";
RL   Submitted (NOV-2005) to the PDB data bank.
CC   -!- FUNCTION: May modulate transcriptional activation by target
CC       nuclear receptors. Can act as transcriptional activator (in vitro)
CC       (By similarity).
CC   -!- SUBUNIT: Interacts with RRARA, PPARD and PPARG. Interacts with
CC       THRB, RARA, RARG and RXRA in the presence of bound ligand (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm (By similarity).
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DR   EMBL; AK002810; BAB22375.1; -; mRNA.
DR   EMBL; BC019448; AAH19448.1; -; mRNA.
DR   IPI; IPI00553335; -.
DR   RefSeq; NP_001031370.1; NM_001036293.2.
DR   UniGene; Mm.136223; -.
DR   UniGene; Mm.380601; -.
DR   PDB; 2CRB; NMR; -; A=4-86.
DR   PDBsum; 2CRB; -.
DR   ProteinModelPortal; Q8VCQ3; -.
DR   SMR; Q8VCQ3; 4-87.
DR   IntAct; Q8VCQ3; 1.
DR   STRING; Q8VCQ3; -.
DR   PRIDE; Q8VCQ3; -.
DR   Ensembl; ENSMUST00000077839; ENSMUSP00000097254; ENSMUSG00000075000.
DR   GeneID; 641340; -.
DR   KEGG; mmu:641340; -.
DR   UCSC; uc007flw.1; mouse.
DR   CTD; 641340; -.
DR   MGI; MGI:1354950; Nrbf2.
DR   eggNOG; roNOG12894; -.
DR   GeneTree; ENSGT00390000000984; -.
DR   HOGENOM; HBG444672; -.
DR   HOVERGEN; HBG056976; -.
DR   InParanoid; Q8VCQ3; -.
DR   OMA; SQKYSPS; -.
DR   OrthoDB; EOG44TP8B; -.
DR   NextBio; 425540; -.
DR   Bgee; Q8VCQ3; -.
DR   CleanEx; MM_NRBF2; -.
DR   Genevestigator; Q8VCQ3; -.
DR   GermOnline; ENSMUSG00000075000; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR015056; DUF1875.
DR   Pfam; PF08961; DUF1875; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Cytoplasm; Nucleus; Phosphoprotein;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    287       Nuclear receptor-binding factor 2.
FT                                /FTId=PRO_0000235817.
FT   COILED      168    215       Potential.
FT   MOTIF       141    145       Nuclear receptor interaction motif (By
FT                                similarity).
FT   MOD_RES      90     90       Phosphothreonine (By similarity).
FT   MOD_RES     105    105       Phosphoserine (By similarity).
FT   MOD_RES     112    112       Phosphoserine (By similarity).
FT   MOD_RES     268    268       Phosphoserine (By similarity).
FT   MOD_RES     277    277       Phosphoserine (By similarity).
FT   CONFLICT    203    203       K -> E (in Ref. 1; BAB22375).
FT   CONFLICT    245    264       KFAANTGKAKDIPIPNLPPL -> SLQLTRGSQGHSNTQPS
FT                                SS (in Ref. 1; BAB22375).
FT   HELIX         7     23
FT   HELIX        27     45
FT   HELIX        51     85
SQ   SEQUENCE   287 AA;  32501 MW;  81B1C0A0CB575D2E CRC64;
     MEVMEGPLNL AHQQSRRADR LLAAGKYEEA ISCHRKATTY LSEAMKLTES EQAHLSLELQ
     RDSHMKQLLL IQERWKRAKR EERLKAQQST ERDGAPHLQA PPRPSEDAEG QSPLLSQPYI
     PSTERRLPEV QGVFDRDPDT LLFLLQQKNE PSEPCIGSKA PKDDKTIIEE QATKIADLKR
     HVEFLVAENE RLRKENKQLK AEKARLLKGT AEKELDVDAD FVEKSELWGL PSHSESAAAS
     STWQKFAANT GKAKDIPIPN LPPLDFPSPE LPLMELSEDI LKGFMND
//
ID   S35C2_MOUSE             Reviewed;         364 AA.
AC   Q8VCX2;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Solute carrier family 35 member C2;
DE   AltName: Full=Ovarian cancer-overexpressed gene 1 protein;
GN   Name=Slc35c2; Synonyms=Ovcov1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=12461647; DOI=10.1007/s00335-002-2185-4;
RA   Leach R.E., Duniec-Dmuchowski Z.M., Pesole G., Tanaka T.S., Ko M.S.H.,
RA   Armant D.R., Krawetz S.A.;
RT   "Identification, molecular characterization, and tissue expression of
RT   OVCOV1.";
RL   Mamm. Genome 13:619-624(2002).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May play an important role in the cellular response to
CC       tissue hypoxia (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- DEVELOPMENTAL STAGE: Higher expression at embryo stage 7.5 dpc
CC       than 11-17 dpc.
CC   -!- SIMILARITY: Belongs to the TPT transporter family. SLC35C
CC       subfamily.
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DR   EMBL; BC018327; AAH18327.1; -; mRNA.
DR   IPI; IPI00122659; -.
DR   RefSeq; NP_659142.1; NM_144893.1.
DR   UniGene; Mm.21184; -.
DR   ProteinModelPortal; Q8VCX2; -.
DR   PhosphoSite; Q8VCX2; -.
DR   PRIDE; Q8VCX2; -.
DR   Ensembl; ENSMUST00000017808; ENSMUSP00000017808; ENSMUSG00000017664.
DR   Ensembl; ENSMUST00000109298; ENSMUSP00000104921; ENSMUSG00000017664.
DR   Ensembl; ENSMUST00000109299; ENSMUSP00000104922; ENSMUSG00000017664.
DR   Ensembl; ENSMUST00000109300; ENSMUSP00000104923; ENSMUSG00000017664.
DR   GeneID; 228875; -.
DR   KEGG; mmu:228875; -.
DR   UCSC; uc008nxd.1; mouse.
DR   CTD; 228875; -.
DR   MGI; MGI:2385166; Slc35c2.
DR   GeneTree; ENSGT00510000048078; -.
DR   HOGENOM; HBG716748; -.
DR   HOVERGEN; HBG055852; -.
DR   InParanoid; Q8VCX2; -.
DR   OMA; MYHLQPL; -.
DR   PhylomeDB; Q8VCX2; -.
DR   NextBio; 379228; -.
DR   ArrayExpress; Q8VCX2; -.
DR   Bgee; Q8VCX2; -.
DR   CleanEx; MM_SLC35C2; -.
DR   Genevestigator; Q8VCX2; -.
DR   GermOnline; ENSMUSG00000017664; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR004853; DUF250.
DR   Pfam; PF03151; TPT; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    364       Solute carrier family 35 member C2.
FT                                /FTId=PRO_0000213400.
FT   TRANSMEM     14     34       Helical; (Potential).
FT   TRANSMEM     42     62       Helical; (Potential).
FT   TRANSMEM    104    124       Helical; (Potential).
FT   TRANSMEM    136    156       Helical; (Potential).
FT   TRANSMEM    166    186       Helical; (Potential).
FT   TRANSMEM    202    222       Helical; (Potential).
FT   TRANSMEM    238    258       Helical; (Potential).
FT   TRANSMEM    272    292       Helical; (Potential).
FT   TRANSMEM    295    315       Helical; (Potential).
FT   MOD_RES     335    335       Phosphoserine.
FT   CARBOHYD    102    102       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   364 AA;  40302 MW;  334B742A566FB891 CRC64;
     MGRWALDVAF VWKAALTLGL VLLYYCFSIG ITFYNKWLTK SFHFPLFMTM LHLAVIFLFS
     ALSRALVQCS SHKARVVLSW TDYLRRVAPT ALATALDVGL SNWSFLYITV SLYTMTKSSA
     VLFILIFSLI FKLEELRAAL VLVVLLIAGG LFMFTYKSTQ FNVEGFALVL GASFIGGIRW
     TLTQILLQKA DLGLQNPIDT MFHLQPLMFL GLFPLFAIFE GLHLSTSEKI FRFQDTGLLL
     WVLGSLLLGG ILAFGLGFSE FLLVSRTSSL TLSIAGIFKE VCTLLLAAHL LGDQISLLNW
     LGFALCLSGI SLHVALKALH SRGDGGPKPL KSLGSSADLE LLLRSSQQEE EDGEEEYFVT
     QGQQ
//
ID   LPPR2_MOUSE             Reviewed;         343 AA.
AC   Q8VCY8; Q8BIE4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Lipid phosphate phosphatase-related protein type 2;
DE            EC=3.1.3.4;
DE   AltName: Full=Plasticity-related gene 4 protein;
DE            Short=PRG-4;
GN   Name=Lppr2; Synonyms=Prg4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=14750979; DOI=10.1046/j.1460-9568.2003.03078.x;
RA   Savaskan N.E., Brauer A.U., Nitsch R.;
RT   "Molecular cloning and expression regulation of PRG-3, a new member of
RT   the plasticity-related gene family.";
RL   Eur. J. Neurosci. 19:212-220(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: A 1,2-diacylglycerol 3-phosphate + H(2)O = a
CC       1,2-diacyl-sn-glycerol + phosphate.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VCY8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VCY8-2; Sequence=VSP_031012;
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family.
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DR   EMBL; AY438023; AAR98841.1; -; mRNA.
DR   EMBL; AK082453; BAC38494.1; -; mRNA.
DR   EMBL; BC018242; AAH18242.1; -; mRNA.
DR   EMBL; BC023082; AAH23082.1; -; mRNA.
DR   IPI; IPI00222105; -.
DR   IPI; IPI00885978; -.
DR   RefSeq; NP_659184.1; NM_144935.1.
DR   UniGene; Mm.277521; -.
DR   ProteinModelPortal; Q8VCY8; -.
DR   PRIDE; Q8VCY8; -.
DR   Ensembl; ENSMUST00000046371; ENSMUSP00000038616; ENSMUSG00000040563.
DR   GeneID; 235044; -.
DR   KEGG; mmu:235044; -.
DR   UCSC; uc009onb.1; mouse.
DR   MGI; MGI:2384575; BC018242.
DR   eggNOG; roNOG13019; -.
DR   GeneTree; ENSGT00550000074203; -.
DR   HOGENOM; HBG445665; -.
DR   HOVERGEN; HBG108093; -.
DR   InParanoid; Q8VCY8; -.
DR   OMA; MCSSPRV; -.
DR   OrthoDB; EOG4SF96H; -.
DR   BRENDA; 3.1.3.4; 244.
DR   NextBio; 382485; -.
DR   ArrayExpress; Q8VCY8; -.
DR   Bgee; Q8VCY8; -.
DR   CleanEx; MM_BC018242; -.
DR   Genevestigator; Q8VCY8; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008195; F:phosphatidate phosphatase activity; IEA:EC.
DR   InterPro; IPR016118; P_Acid_Pase/Cl_peroxidase_N.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   Gene3D; G3DSA:1.20.144.10; P_Acid_Pase/Cl_peroxidase_N; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; AcPase_VanPerase; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Hydrolase; Membrane;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    343       Lipid phosphate phosphatase-related
FT                                protein type 2.
FT                                /FTId=PRO_0000317539.
FT   TRANSMEM     12     32       Helical; (Potential).
FT   TRANSMEM     72     92       Helical; (Potential).
FT   TRANSMEM    129    149       Helical; (Potential).
FT   TRANSMEM    210    230       Helical; (Potential).
FT   TRANSMEM    239    259       Helical; (Potential).
FT   TRANSMEM    266    286       Helical; (Potential).
FT   CARBOHYD    165    165       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     317    343       NPRPAGRIRHRHGSPHPSRRTVPAVAT -> LSVAQEPETC
FT                                RPHSTPARLTPSKPQNCARRGHLIPSCVSSRAPAMCSSPRV
FT                                PRPRLRSEPTPLPLPLPLPAPTPSQGPSPSSPGPGGPGGGG
FT                                GRGRKLLLPTPLLRDLYTLSGLHPSPFHRDNFSPYLFASRD
FT                                HLL (in isoform 2).
FT                                /FTId=VSP_031012.
SQ   SEQUENCE   343 AA;  36936 MW;  DE2F7F0F0F8215FD CRC64;
     MAGGRPHLKR SFSIIPCFVF VESVLLGIVV LLAYRLEFTD TFPVHTQGFF CYDSAYAKPY
     PGPEAASRAP PALIYALVTA GPTLTILLGE LARAFFPAPP SSSPVSGEST IVSGACCRFS
     PPLRRLVRFL GVYSFGLFTT TIFANAGQVV TGNPTPHFLS VCRPNYTALG CPPPSPDRPG
     PDRFVTDQSA CAGSPSLVAA ARRAFPCKDA ALCAYAVTYT AMYVTLVFRV KGSRLVKPSL
     CLALLCPAFL VGVVRVAEYR NHWSDVLAGF LTGAAIATFL VTCVVHNFQS RPHSGRRLSP
     WEDLSQAPTM DSPLEKNPRP AGRIRHRHGS PHPSRRTVPA VAT
//
ID   Q8VCY9_MOUSE            Unreviewed;       245 AA.
AC   Q8VCY9;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   SubName: Full=Fibroblast growth factor 13;
DE   SubName: Full=Fibroblast growth factor 13, isoform CRA_c;
GN   Name=Fgf13; ORFNames=RP23-387L21.1-001, mCG_50545;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RA   Whitehead S.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RA   Howden P.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC018238; AAH18238.1; -; mRNA.
DR   EMBL; AL713968; CAM22824.1; -; Genomic_DNA.
DR   EMBL; AL672247; CAM22824.1; JOINED; Genomic_DNA.
DR   EMBL; AL672247; CAM27417.1; -; Genomic_DNA.
DR   EMBL; AL713968; CAM27417.1; JOINED; Genomic_DNA.
DR   EMBL; CH466583; EDL42182.1; -; Genomic_DNA.
DR   IPI; IPI00311361; -.
DR   RefSeq; NP_034330.2; NM_010200.2.
DR   UniGene; Mm.7995; -.
DR   HSSP; P31371; 1G82.
DR   ProteinModelPortal; Q8VCY9; -.
DR   SMR; Q8VCY9; 64-201.
DR   STRING; Q8VCY9; -.
DR   Ensembl; ENSMUST00000033473; ENSMUSP00000033473; ENSMUSG00000031137.
DR   GeneID; 14168; -.
DR   KEGG; mmu:14168; -.
DR   UCSC; uc009tht.1; mouse.
DR   CTD; 14168; -.
DR   MGI; MGI:109178; Fgf13.
DR   GeneTree; ENSGT00590000082822; -.
DR   HOVERGEN; HBG007580; -.
DR   InParanoid; Q8VCY9; -.
DR   OMA; EEDSTYT; -.
DR   PhylomeDB; Q8VCY9; -.
DR   NextBio; 285320; -.
DR   ArrayExpress; Q8VCY9; -.
DR   Bgee; Q8VCY9; -.
DR   Genevestigator; Q8VCY9; -.
DR   GO; GO:0008083; F:growth factor activity; IEA:InterPro.
DR   InterPro; IPR008996; Cytokine_IL1-like.
DR   InterPro; IPR002209; GF_heparin-bd.
DR   InterPro; IPR002348; IL1_HBGF.
DR   PANTHER; PTHR11486; IL1_HBGF; 1.
DR   Pfam; PF00167; FGF; 1.
DR   PRINTS; PR00263; HBGFFGF.
DR   PRINTS; PR00262; IL1HBGF.
DR   SMART; SM00442; FGF; 1.
DR   SUPFAM; SSF50353; Cytok_IL1_like; 1.
DR   PROSITE; PS00247; HBGF_FGF; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   245 AA;  27588 MW;  5B96D41AC3A3DF78 CRC64;
     MAAAIASSLI RQKRQARERE KSNACKCVSS PSKGKTSCDK NKLNVFSRVK LFGSKKRRRR
     RPEPQLKGIV TKLYSRQGYH LQLQADGTID GTKDEDSTYT LFNLIPVGLR VVAIQGVQTK
     LYLAMNSEGY LYTSEHFTPE CKFKESVFEN YYVTYSSMIY RQQQSGRGWY LGLNKEGEIM
     KGNHVKKNKP AAHFLPKPLK VAMYKEPSLH DLTEFSRSGS GTPTKSRSVS GVLNGGKSMS
     HNEST
//
ID   SGSM3_MOUSE             Reviewed;         750 AA.
AC   Q8VCZ6; Q3TCB6;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Small G protein signaling modulator 3;
DE   AltName: Full=RUN and TBC1 domain-containing protein 3;
GN   Name=Sgsm3; Synonyms=Cip85, Rutbc3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH GJA1.
RC   TISSUE=Embryo;
RX   PubMed=15709751; DOI=10.1021/bi048306w;
RA   Lan Z., Kurata W.E., Martyn K.D., Jin C., Lau A.F.;
RT   "Novel rab GAP-like protein, CIP85, interacts with connexin43 and
RT   induces its degradation.";
RL   Biochemistry 44:2385-2396(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Dendritic cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver, Mammary tumor, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=17509819; DOI=10.1016/j.ygeno.2007.03.013;
RA   Yang H., Sasaki T., Minoshima S., Shimizu N.;
RT   "Identification of three novel proteins (SGSM1, 2, 3) which modulate
RT   small G protein (RAP and RAB)-mediated signaling pathway.";
RL   Genomics 90:249-260(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   STRUCTURE BY NMR OF 483-549.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the SH3 domain of mouse RUN and TBC1 domain
RT   containing 3.";
RL   Submitted (OCT-2007) to the PDB data bank.
CC   -!- FUNCTION: May play a cooperative role in NF2-mediated growth
CC       suppression of cells (By similarity).
CC   -!- SUBUNIT: Interacts with GJA1. Interaction with GJA1 induces its
CC       degradation. Interacts via its RUN domain with the C-terminal
CC       region of NF2. Interacts with RAB3A, RAB4A, RAB5A, RAB8A, RAB11A,
CC       RAP1A, RAP1B, RAP2A, RAP2B and PDCD6I. No interaction with RAB27A
CC       (By similarity).
CC   -!- INTERACTION:
CC       P08050:Gja1 (xeno); NbExp=1; IntAct=EBI-525155, EBI-476947;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- SIMILARITY: Belongs to the small G protein signaling modulator
CC       family.
CC   -!- SIMILARITY: Contains 1 Rab-GAP TBC domain.
CC   -!- SIMILARITY: Contains 1 RUN domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE42041.1; Type=Erroneous initiation;
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DR   EMBL; AY382616; AAR89983.1; -; mRNA.
DR   EMBL; AK170806; BAE42041.1; ALT_INIT; mRNA.
DR   EMBL; BC018197; AAH18197.1; -; mRNA.
DR   EMBL; BC024122; AAH24122.1; -; mRNA.
DR   EMBL; BC025561; AAH25561.1; -; mRNA.
DR   IPI; IPI00311375; -.
DR   RefSeq; NP_598852.2; NM_134091.2.
DR   UniGene; Mm.274943; -.
DR   PDB; 2YUO; NMR; -; A=483-547.
DR   PDBsum; 2YUO; -.
DR   ProteinModelPortal; Q8VCZ6; -.
DR   SMR; Q8VCZ6; 76-375, 480-551.
DR   IntAct; Q8VCZ6; 4.
DR   MINT; MINT-1326710; -.
DR   STRING; Q8VCZ6; -.
DR   PhosphoSite; Q8VCZ6; -.
DR   PRIDE; Q8VCZ6; -.
DR   Ensembl; ENSMUST00000042506; ENSMUSP00000043311; ENSMUSG00000042303.
DR   GeneID; 105835; -.
DR   KEGG; mmu:105835; -.
DR   NMPDR; fig|10090.3.peg.30296; -.
DR   UCSC; uc007wwb.1; mouse.
DR   CTD; 105835; -.
DR   MGI; MGI:1916329; Sgsm3.
DR   GeneTree; ENSGT00580000081243; -.
DR   HOGENOM; HBG356933; -.
DR   HOVERGEN; HBG108484; -.
DR   InParanoid; Q8VCZ6; -.
DR   OrthoDB; EOG4X97GJ; -.
DR   PhylomeDB; Q8VCZ6; -.
DR   NextBio; 357910; -.
DR   ArrayExpress; Q8VCZ6; -.
DR   Bgee; Q8VCZ6; -.
DR   CleanEx; MM_SGSM3; -.
DR   Genevestigator; Q8VCZ6; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005921; C:gap junction; IDA:UniProtKB.
DR   GO; GO:0005097; F:Rab GTPase activator activity; IEA:InterPro.
DR   GO; GO:0017137; F:Rab GTPase binding; ISS:UniProtKB.
DR   GO; GO:0007050; P:cell cycle arrest; IEA:UniProtKB-KW.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:UniProtKB.
DR   GO; GO:0032486; P:Rap protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0032313; P:regulation of Rab GTPase activity; IEA:InterPro.
DR   InterPro; IPR000195; RabGAP/TBC_dom.
DR   InterPro; IPR004012; Run.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF02759; RUN; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF00566; TBC; 1.
DR   SMART; SM00593; RUN; 1.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; RabGAP_TBC; 2.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50826; RUN; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Coiled coil; Cytoplasm; Growth arrest;
KW   Phosphoprotein; SH3 domain.
FT   CHAIN         1    750       Small G protein signaling modulator 3.
FT                                /FTId=PRO_0000307811.
FT   DOMAIN      114    305       Rab-GAP TBC.
FT   DOMAIN      480    539       SH3.
FT   DOMAIN      555    718       RUN.
FT   COILED      415    439       Potential.
FT   MOD_RES     410    410       Phosphoserine.
FT   CONFLICT    622    622       D -> G (in Ref. 2; BAE42041).
FT   STRAND      483    489
FT   STRAND      506    511
FT   STRAND      514    522
FT   STRAND      525    530
FT   HELIX       531    533
FT   STRAND      534    537
SQ   SEQUENCE   750 AA;  85490 MW;  C0306BE346808B07 CRC64;
     MSGNHTPSAS GPFSALTPSI WPQEILAKYS QKEESSEQPE LCYDEFGFRV DKEGSEPGCS
     QMTGSPLVED PPQRLRWQAH LEFTHNHDVG DLTWDKIAVS LPRSEKLRSL VLAGIPHGMR
     PQLWMRLSGA LQKKKNSELS YREIIKNSSN DETIAAKQIE KDLLRTMPSN ACFANVNSIG
     VPRLRRVLRA LAWLYPEIGY CQGTGMVAAC LLLFLEEEDA FWMMCAIIED LLPASYFSTT
     LLGVQTDQRV LRHLIVQYLP RLDKLLQEHD IELSLITLHW FLTAFASVVH IRLLLRIWDL
     FFYEGSLVLF QTTLGMLRLK EEELIQSENS ASIFNTLSDI PAQMDDAELL LGEAMRLAGS
     LTDVAVETQR RKHLAYLIAD QGQTLGTGTT TNLSQVVRRR TQRRKSGITS LLFGEDDLEA
     LKAKNIKQTE LVADLREAIL RVARHFQCTD PKNCSVELTP DYSMESHQRD HENYVACLRS
     HRRRAKALLD FERHDDDELG FRKNDIITII SQKDEHCWVG ELNGLRGWFP AKFVEVLDER
     SKEYSIAGDD SVTEGVTDLV RGTLCPALKA LFEHGLKKPS LLGGACHPWL FIEEAAGREV
     ERDFDSVYSR LVLCKTYRLD EDGKVLTPEE LLYRAVQSVN VTHDAAHAQM DVKLRSLICV
     GLNEQVLHLW LEVLCSSLPT VEKWYQPWSF LRSPGWVQIK CELRVLCCFA FSLSQDWELP
     ARREEEKQPL KEGVQDMLVK HHLFSWDIDG
//
ID   GRAP1_MOUSE             Reviewed;         806 AA.
AC   Q8VD04; A2AEW7; O35693; Q3T9C3; Q69ZP9;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=GRIP1-associated protein 1;
DE            Short=GRASP-1;
DE   AltName: Full=HCMV-interacting protein;
GN   Name=Gripap1; Synonyms=DXImx47e, Kiaa1167;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-106.
RA   Weber B.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 318-776.
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631 AND SER-634, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBUNIT: Interacts with GRIP1, GRIP2 and AMPA receptors (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Early endosome (By similarity).
CC   -!- PTM: Proteolytically cleaved by caspase-3 (By similarity).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA66184.1; Type=Erroneous initiation;
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DR   EMBL; AK156165; BAE33608.1; -; mRNA.
DR   EMBL; AK172623; BAE43101.1; -; mRNA.
DR   EMBL; AK172699; BAE43133.1; -; mRNA.
DR   EMBL; AL671995; CAM13601.1; -; Genomic_DNA.
DR   EMBL; X97571; CAA66184.1; ALT_INIT; mRNA.
DR   EMBL; AK173119; BAD32397.1; -; Transcribed_RNA.
DR   IPI; IPI00267855; -.
DR   RefSeq; NP_997553.1; NM_207670.1.
DR   UniGene; Mm.194811; -.
DR   ProteinModelPortal; Q8VD04; -.
DR   MINT; MINT-4609304; -.
DR   STRING; Q8VD04; -.
DR   PhosphoSite; Q8VD04; -.
DR   PRIDE; Q8VD04; -.
DR   Ensembl; ENSMUST00000065932; ENSMUSP00000068789; ENSMUSG00000031153.
DR   GeneID; 54645; -.
DR   KEGG; mmu:54645; -.
DR   UCSC; uc009smo.1; mouse.
DR   CTD; 54645; -.
DR   MGI; MGI:1859616; Gripap1.
DR   GeneTree; ENSGT00400000022282; -.
DR   HOVERGEN; HBG080243; -.
DR   OrthoDB; EOG4GB75N; -.
DR   NextBio; 311492; -.
DR   ArrayExpress; Q8VD04; -.
DR   Bgee; Q8VD04; -.
DR   CleanEx; MM_GRIPAP1; -.
DR   Genevestigator; Q8VD04; -.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Coiled coil; Endosome; Phosphoprotein.
FT   CHAIN         1    806       GRIP1-associated protein 1.
FT                                /FTId=PRO_0000087582.
FT   COILED        4    158       Potential.
FT   COILED      204    606       Potential.
FT   COILED      666    700       Potential.
FT   COILED      750    779       Potential.
FT   SITE        563    564       Cleavage; by caspase-3 (By similarity).
FT   MOD_RES     620    620       Phosphoserine (By similarity).
FT   MOD_RES     631    631       Phosphoserine.
FT   MOD_RES     634    634       Phosphoserine.
FT   MOD_RES     655    655       Phosphoserine (By similarity).
FT   MOD_RES     657    657       Phosphoserine (By similarity).
FT   CONFLICT      4      4       A -> R (in Ref. 3; CAA66184).
FT   CONFLICT    502    502       Q -> L (in Ref. 1; BAE33608/BAE43101/
FT                                BAE43133).
SQ   SEQUENCE   806 AA;  92715 MW;  766F7C5B44589020 CRC64;
     MAQALSEEEF QRMQTQLLEL RTNNYQLSDE LRKNGVELSS LRQKVAYLDK EFSKAQKALS
     KSKKAQEVEV LLSENEMLQA KLHSQEEDFR LQNSTLMAEF SKLCSQLEQL ELENRQLKEG
     VPGAAGAHVD GELLRLQAEN TALQKNMAAL QERYGKEAVR PSAVGEGQGD PPGDVLPTPL
     APMPLAEVEL KWEMEREEKK LLWEQLQGLE SSKQAETSRL QEELAKLSEK LKKKQESFCR
     LQTEKETLFN DSRNKIEELQ QRKEADLKAQ LARTQKLQQE LEAANQSLAE LRDQRQGERL
     EHAAALRALQ DQIQTAKTQE LNMLREQTSE LASELQHRQA EYEELMGQKD DLNSQLQESL
     RANSRLLEQL QEIGQEKEQL TQDLQEARKS AEKRKVMLDE LAMETLQEKS QHKEELGAVR
     LRHEKELLGV RARYERELRE LHEDKKRQEE ELRGQIREEK ARTRELENLQ HTVEELQAQV
     HSMDGAKGWF ERRLKEAEES LQQQQQEQEE TLKLCREEHA AELKGKDEEL QNVREQLQQA
     QEERDGHVKT ISNLKQEVKD TVDGQRILEK KGSAVLKDLK RQLHLERKRA DKLQERLQEI
     LTNSKSRTGL EELVLSEMNS PSRTQTGDSS SVSSFSYREI LKEKESSAIP ARSLSSSPQA
     QPPRPAELSD EEVAELFQRL AETQQEKWML EEKVKHLEVS SASMAEDLCR KSAIIETYVM
     DSRIDVSVAA GHTDRSGLGS VLRDLVKPGD ENLREMNKKL QNMLEEQLTK NMHLHKDMEV
     LSQEIVRLSK ECVGSPDPDL EPGEAN
//
ID   CK068_MOUSE             Reviewed;         251 AA.
AC   Q8VD62; Q6LCE3;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=UPF0696 protein C11orf68 homolog;
DE   AltName: Full=Basophilic leukemia-expressed protein Bles03;
DE   AltName: Full=Protein WF-3;
GN   Name=Bles03;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CD-1 X ICR;
RA   Sugihara T.;
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the UPF0696 family.
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DR   EMBL; U64690; AAR00571.1; -; mRNA.
DR   EMBL; BC017542; AAH17542.1; -; mRNA.
DR   EMBL; BC024516; AAH24516.1; -; mRNA.
DR   IPI; IPI00122620; -.
DR   RefSeq; NP_598910.2; NM_134149.2.
DR   UniGene; Mm.329658; -.
DR   ProteinModelPortal; Q8VD62; -.
DR   SMR; Q8VD62; 17-251.
DR   IntAct; Q8VD62; 66.
DR   STRING; Q8VD62; -.
DR   PRIDE; Q8VD62; -.
DR   Ensembl; ENSMUST00000159759; ENSMUSP00000125651; ENSMUSG00000047423.
DR   Ensembl; ENSMUST00000160559; ENSMUSP00000125185; ENSMUSG00000089632.
DR   GeneID; 107242; -.
DR   KEGG; mmu:107242; -.
DR   UCSC; uc008gdb.1; mouse.
DR   MGI; MGI:2147598; AI837181.
DR   eggNOG; maNOG11684; -.
DR   GeneTree; ENSGT00390000011640; -.
DR   HOGENOM; HBG505363; -.
DR   HOVERGEN; HBG054338; -.
DR   InParanoid; Q8VD62; -.
DR   OMA; VEGQLQV; -.
DR   OrthoDB; EOG4GB777; -.
DR   PhylomeDB; Q8VD62; -.
DR   NextBio; 358636; -.
DR   ArrayExpress; Q8VD62; -.
DR   Bgee; Q8VD62; -.
DR   CleanEx; MM_AI837181; -.
DR   Genevestigator; Q8VD62; -.
DR   GermOnline; ENSMUSG00000047423; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:InterPro.
DR   InterPro; IPR015034; DUF1917.
DR   Pfam; PF08939; DUF1917; 1.
PE   2: Evidence at transcript level;
FT   CHAIN         1    251       UPF0696 protein C11orf68 homolog.
FT                                /FTId=PRO_0000228118.
FT   CONFLICT     32     32       A -> G (in Ref. 1; AAR00571).
SQ   SEQUENCE   251 AA;  27539 MW;  74CDE837ECBCF1B3 CRC64;
     MEPNEELEEE DSPGGREDGF TAEHLAAEAM AADMDPWLVF DARTTPATEL DAWLAKYPPS
     QVTRYGDPGS PNSEPVGWIA AYGQGYTPNS GDVQGLQAAW EALQTSGRPI TPGTLRQLAI
     THHVLSGKWL IHLSPGFKLD HAWAGIARAV VEGRLQVAKV SPRAKEGGRQ VICVYTDDFT
     DRLGVLEADS AIRAAGIKCL LTYKPDVYTY LGIYRANRWH LCPTLYESRF QLGGNTRGSR
     VLDRANNVEL T
//
ID   TSYL4_MOUSE             Reviewed;         406 AA.
AC   Q8VD63;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Testis-specific Y-encoded-like protein 4;
DE            Short=TSPY-like protein 4;
GN   Name=Tspyl4; Synonyms=D10Bwg0791e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SIMILARITY: Belongs to the nucleosome assembly protein (NAP)
CC       family.
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DR   EMBL; AK030740; BAC27108.1; -; mRNA.
DR   EMBL; BC017540; AAH17540.1; -; mRNA.
DR   EMBL; BC034656; AAH34656.1; -; mRNA.
DR   IPI; IPI00261240; -.
DR   RefSeq; NP_084479.1; NM_030203.2.
DR   UniGene; Mm.480558; -.
DR   ProteinModelPortal; Q8VD63; -.
DR   SMR; Q8VD63; 193-379.
DR   PhosphoSite; Q8VD63; -.
DR   PRIDE; Q8VD63; -.
DR   Ensembl; ENSMUST00000047935; ENSMUSP00000036360; ENSMUSG00000039485.
DR   GeneID; 72480; -.
DR   KEGG; mmu:72480; -.
DR   UCSC; uc007euu.1; mouse.
DR   CTD; 72480; -.
DR   MGI; MGI:106393; Tspyl4.
DR   GeneTree; ENSGT00530000062882; -.
DR   HOGENOM; HBG126049; -.
DR   HOVERGEN; HBG014779; -.
DR   InParanoid; Q8VD63; -.
DR   OMA; QPVESPR; -.
DR   OrthoDB; EOG4933JV; -.
DR   PhylomeDB; Q8VD63; -.
DR   NextBio; 336316; -.
DR   ArrayExpress; Q8VD63; -.
DR   Bgee; Q8VD63; -.
DR   CleanEx; MM_TSPYL4; -.
DR   Genevestigator; Q8VD63; -.
DR   GermOnline; ENSMUSG00000039485; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   InterPro; IPR002164; NAP_family.
DR   PANTHER; PTHR11875; NAP_family; 1.
DR   Pfam; PF00956; NAP; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    406       Testis-specific Y-encoded-like protein 4.
FT                                /FTId=PRO_0000185674.
FT   MOD_RES      89     89       Phosphoserine.
SQ   SEQUENCE   406 AA;  44811 MW;  BA5E037E80AFA75F CRC64;
     MNGVEGNNEL SLANTTTPSH ASEDLDLKQD QGLQEETDTV REMEAAGEAG ADGGASPDSE
     HCGPELCFRV AENSCAAAAR GLEDAPSPSK GGDAPSAPVA ADDSSKNGCQ LEGPHSPAKP
     KALEACGAVG LGSQQMPGPK KTKEMTTTKC AISVATGKEG EAGAAMQEKK GLQKEKKVAG
     GGKEETRPRA PKINCMDSLE AIDQELSNVN AQADRAFLQL ERKFGRMRRL HMQRRSFIIQ
     NIPGFWVTAF RNHPQLSPMI SGQDEDMMRY MINLEVEELK QPRVGCKFKF IFQSNPYFRN
     EGLVKEYERR SSGRVVSLST PIRWHRGQEP QAHIHRNREG NTIPSFFNWF SDHSLLEFDR
     IAEIIKGELW SNPLQYYLMG DGPRRGVRVP PRQPVESPRS FRFQSG
//
ID   PI3R4_MOUSE             Reviewed;        1358 AA.
AC   Q8VD65; Q56A65; Q8C948; Q8C9D7; Q9CVC5;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Phosphoinositide 3-kinase regulatory subunit 4;
DE            Short=PI3-kinase regulatory subunit 4;
DE            EC=2.7.11.1;
GN   Name=Pik3r4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-536 AND 1188-1358.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Stomach, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-638.
RC   STRAIN=Czech II; TISSUE=Eye, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-894 AND SER-905, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Regulatory subunit of the PI3K complex. May regulate
CC       membrane trafficking late in the endocytic pathway (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Manganese (By similarity).
CC   -!- SUBUNIT: Heterodimer. This subunit, part of a complex composed of
CC       regulatory and catalytic subunits, associates with the
CC       phosphatidylinositol 3-kinase type 3 (PIK3C3) (By similarity).
CC       Forms a complex with BECN1, PIK3C3 and either UVRAG and
CC       KIAA0226/Rubicon, or with ATG14. In this complex, presence of
CC       UVRAG and ATG14 are mutually exclusive (By similarity).
CC   -!- PTM: Myristoylated (By similarity).
CC   -!- PTM: Probably autophosphorylated (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family.
CC   -!- SIMILARITY: Contains 4 HEAT repeats.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 7 WD repeats.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC157514; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK008703; BAB25843.1; -; mRNA.
DR   EMBL; AK042361; BAC31236.1; -; mRNA.
DR   EMBL; AK042953; BAC31417.1; -; mRNA.
DR   EMBL; AK087938; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC017537; AAH17537.1; -; mRNA.
DR   EMBL; BC092149; AAH92149.1; -; mRNA.
DR   IPI; IPI00406045; -.
DR   RefSeq; NP_001074778.1; NM_001081309.1.
DR   UniGene; Mm.274830; -.
DR   ProteinModelPortal; Q8VD65; -.
DR   SMR; Q8VD65; 959-1079.
DR   STRING; Q8VD65; -.
DR   PhosphoSite; Q8VD65; -.
DR   PRIDE; Q8VD65; -.
DR   Ensembl; ENSMUST00000065778; ENSMUSP00000067400; ENSMUSG00000032571.
DR   GeneID; 75669; -.
DR   KEGG; mmu:75669; -.
DR   UCSC; uc009rio.1; mouse.
DR   CTD; 75669; -.
DR   MGI; MGI:1922919; Pik3r4.
DR   eggNOG; roNOG08960; -.
DR   GeneTree; ENSGT00390000016225; -.
DR   HOGENOM; HBG315087; -.
DR   HOVERGEN; HBG079542; -.
DR   InParanoid; Q8VD65; -.
DR   OMA; HFNSGAQ; -.
DR   OrthoDB; EOG451DPV; -.
DR   PhylomeDB; Q8VD65; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 343672; -.
DR   ArrayExpress; Q8VD65; -.
DR   Bgee; Q8VD65; -.
DR   Genevestigator; Q8VD65; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000357; HEAT.
DR   InterPro; IPR021133; HEAT_type_2.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
DR   Pfam; PF02985; HEAT; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Lipoprotein; Myristate; Nucleotide-binding;
KW   Phosphoprotein; Repeat; Serine/threonine-protein kinase; Transferase;
KW   WD repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1358       Phosphoinositide 3-kinase regulatory
FT                                subunit 4.
FT                                /FTId=PRO_0000086525.
FT   DOMAIN       26    324       Protein kinase.
FT   REPEAT      413    450       HEAT 1.
FT   REPEAT      458    495       HEAT 2.
FT   REPEAT      572    610       HEAT 3.
FT   REPEAT      612    648       HEAT 4.
FT   REPEAT      991   1030       WD 1.
FT   REPEAT     1040   1079       WD 2.
FT   REPEAT     1093   1134       WD 3.
FT   REPEAT     1139   1178       WD 4.
FT   REPEAT     1182   1223       WD 5.
FT   REPEAT     1237   1278       WD 6.
FT   REPEAT     1327   1358       WD 7.
FT   NP_BIND      32     40       ATP (By similarity).
FT   COMPBIAS    781    784       Poly-Glu.
FT   COMPBIAS    974    977       Poly-Pro.
FT   ACT_SITE    148    148       Proton acceptor (By similarity).
FT   BINDING      53     53       ATP (By similarity).
FT   MOD_RES     808    808       Phosphoserine (By similarity).
FT   MOD_RES     813    813       Phosphoserine (By similarity).
FT   MOD_RES     814    814       Phosphoserine (By similarity).
FT   MOD_RES     853    853       Phosphoserine (By similarity).
FT   MOD_RES     861    861       Phosphoserine (By similarity).
FT   MOD_RES     865    865       Phosphoserine (By similarity).
FT   MOD_RES     892    892       Phosphoserine (By similarity).
FT   MOD_RES     894    894       Phosphoserine.
FT   MOD_RES     905    905       Phosphoserine.
FT   MOD_RES     925    925       Phosphoserine (By similarity).
FT   MOD_RES    1079   1079       Phosphoserine (By similarity).
FT   MOD_RES    1316   1316       Phosphothreonine (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
FT   CONFLICT    292    305       QMINREPEKRLEAE -> MLQIRAIEFYLTMS (in Ref.
FT                                2; BAC31236).
FT   CONFLICT    511    511       P -> S (in Ref. 2; BAC31417).
FT   CONFLICT    529    603       ELQALHEMVQQKVVTLLSDPENIVKQTLMESGITRLCVFFG
FT                                RQKANDVLLSHMITFLNDKNDWHLRGAFFDSIVG -> GCV
FT                                TPLLKSPSFTPNRYWYLVKAVICDSLGK (in Ref. 2;
FT                                BAC31417).
FT   CONFLICT    529    559       ELQALHEMVQQKVVTLLSDPENIVKQTLMES -> GCVTPL
FT                                LKSPSFTPNRYWYLVKAVICDSLG (in Ref. 2;
FT                                BAC31417).
FT   CONFLICT    621    637       QQGLSDAEEFVIVKALN -> HAPPVPVLGNRSCSGQQ
FT                                (in Ref. 3; AAH92149).
SQ   SEQUENCE   1358 AA;  152599 MW;  113FC5EBBDA01E19 CRC64;
     MGNQLAGIAP SQILSVESYF SDIHDFEYDK SLGSTRFFKV ARAKHREGLV VVKVFAIQDP
     TLPLTSYKQE LEELKIRLHS AQNCLPFQKA AEKASEKAAM LFRQYVRDNL YDRISTRPFL
     NNIEKRWIAF QILTAVDQAH KSGVRHGDIK TENVMVTSWN WVLLTDFASF KPTYLPEDNP
     ADFNYFFDTS RRRTCYIAPE RFVDGGMFAT ELEYMRDPST PLVDLNSNQR ARGELKRAMD
     IFSAGCVIAE LFTEGVPLFD LSQLLAYRNG HFFPEQVLNK IEDRSIRDLV TQMINREPEK
     RLEAEDYLKQ QRGNAFPEIF YTFLQPYMAQ FAKETFLSAD ERILVIRKDL GNIIHNLCGH
     DLPEKAEGES RASGLVVLVS VITSCLQTLK SCDSKLAALE LILHLAPRLS VEILLDRITP
     YLLHFSNDSV PRVRAEALRT LTKVLALVQE VPRNDVNIYP EYILPGIAHL AQDDATIVRL
     AYAENIALLA ETALRFLELV QLKTLNMENE PDNEEVDEAT RPNGDYDTEL QALHEMVQQK
     VVTLLSDPEN IVKQTLMESG ITRLCVFFGR QKANDVLLSH MITFLNDKND WHLRGAFFDS
     IVGVAAYVGW QSSSILKPLL QQGLSDAEEF VIVKALNALT CMCQLGLLQK PHVYEFASDI
     APFLCHPNLW IRYGAVGFIT VVAHQISTAD VYCKLMPYLD PYITQPVIQI ERKLVLLSVL
     KEPVSRSIFD YALRSKDIAS LFRHLHMRQK KRNGSLLDCP PPEDPTIAQL LKKLLSQGMT
     EEEEDKLLAL KDFMMKSNRA KANAVDQSHL HDSSQKGVID LAALGITGRQ VDLVKTKQEP
     DEKRARKHVK QDSNVNEEWK SMFGSLEPPN IPQALPKTSD HEVVQPGKPP RSESSAGICV
     PLSTSPQVSE AAHIPSKKPV IPVVSSTVLP STYQIRITTC KTELQQLIQQ KREQCNAERI
     AKQMMENAEW ESKPPPPGWR PKGLLVAHLH EHKSAVNRIR VSDEHLLFAT CSNDGTVKIW
     NSQKMEGKTT TTRSILTYSR IGGRVKTLTF CQGSHYLAIA SDNGAVQLLG IEASKLPKSP
     KIHPLQSRIL DQKEDGCVVD MHHFNSGAQS VLAYATVNGS LVGWDLRSSS NAWTLKHDLK
     SGLITSFAVD IHQCWLCIGT SSGAMACWDM RFQLPISSHC HPSRARIRRL SMHPLYQSWV
     IAAVQGNNEV SMWDMETGDR RLTLWASSAP PLSELQPSPH SVHGIYCSPA DGNPILLTAG
     SDMKIRFWDL VSPERSYVVA GSTGSPSVSY YKKIIEGTEV VQEIQNKQKV GPSDDTPRRG
     PESLPVGHHD IITDIATFQT TQGFIVTASR DGIVKVWK
//
ID   HIP1_MOUSE              Reviewed;        1029 AA.
AC   Q8VD75; Q3TLS2; Q571K7;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Huntingtin-interacting protein 1;
DE            Short=HIP-1;
DE   AltName: Full=Huntingtin-interacting protein I;
DE            Short=HIP-I;
GN   Name=Hip1; Synonyms=Kiaa4113;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-506.
RC   TISSUE=Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 412-1029.
RC   TISSUE=Embryonic tail;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=97285121; PubMed=9140394; DOI=10.1038/ng0597-44;
RA   Kalchman M.A., Koide H.B., McCutcheon K., Graham R.K., Nichol K.,
RA   Nishiyama K., Kazemi-Esfarjani P., Lynn F.C., Wellington C.,
RA   Metzler M., Goldberg Y.P., Kanazawa I., Geitz R.D., Hayden M.R.;
RT   "HIP1, a human homologue of S. cerevisiae Sla2p, interacts with
RT   membrane-associated huntingtin in the brain.";
RL   Nat. Genet. 16:44-53(1997).
RN   [5]
RP   FUNCTION.
RX   PubMed=11577110; DOI=10.1074/jbc.M108177200;
RA   Mishra S.K., Agostinelli N.R., Brett T.J., Mizukami I., Ross T.S.,
RA   Traub L.M.;
RT   "Clathrin- and AP-2-binding sites in HIP1 uncover a general assembly
RT   role for endocytic accessory proteins.";
RL   J. Biol. Chem. 276:46230-46236(2001).
RN   [6]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=11604514; DOI=10.1128/MCB.21.22.7796-7806.2001;
RA   Rao D.S., Chang J.C., Kumar P.D., Mizukami I., Smithson G.M.,
RA   Bradley S.V., Parlow A.F., Ross T.S.;
RT   "Huntingtin interacting protein 1 is a clathrin coat binding protein
RT   required for differentiation of late spermatogenic progenitors.";
RL   Mol. Cell. Biol. 21:7796-7806(2001).
RN   [7]
RP   FUNCTION, INTERACTION WITH GRIA1, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=12839988; DOI=10.1093/emboj/cdg334;
RA   Metzler M., Li B., Gan L., Georgiou J., Gutekunst C.A., Wang Y.,
RA   Torre E., Devon R.S., Oh R., Legendre-Guillemin V., Rich M.,
RA   Alvarez C., Gertsenstein M., McPherson P.S., Nagy A., Wang Y.T.,
RA   Roder J.C., Raymond L.A., Hayden M.R.;
RT   "Disruption of the endocytic protein HIP1 results in neurological
RT   deficits and decreased AMPA receptor trafficking.";
RL   EMBO J. 22:3254-3266(2003).
RN   [8]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=14998932; DOI=10.1093/hmg/ddh102;
RA   Oravecz-Wilson K.I., Kiel M.J., Li L., Rao D.S., Saint-Dic D.,
RA   Kumar P.D., Provot M.M., Hankenson K.D., Reddy V.N., Lieberman A.P.,
RA   Morrison S.J., Ross T.S.;
RT   "Huntingtin interacting protein 1 mutations lead to abnormal
RT   hematopoiesis, spinal defects and cataracts.";
RL   Hum. Mol. Genet. 13:851-867(2004).
RN   [9]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=17452370; DOI=10.1093/hmg/ddm076;
RA   Bradley S.V., Hyun T.S., Oravecz-Wilson K.I., Li L., Waldorff E.I.,
RA   Ermilov A.N., Goldstein S.A., Zhang C.X., Drubin D.G., Varela K.,
RA   Parlow A., Dlugosz A.A., Ross T.S.;
RT   "Degenerative phenotypes caused by the combined deficiency of murine
RT   HIP1 and HIP1r are rescued by human HIP1.";
RL   Hum. Mol. Genet. 16:1279-1292(2007).
RN   [10]
RP   FUNCTION, AND INTERACTION WITH GRIN2A AND GRIN2B.
RX   PubMed=17329427; DOI=10.1523/JNEUROSCI.5175-06.2007;
RA   Metzler M., Gan L., Wong T.P., Liu L., Helm J., Liu L., Georgiou J.,
RA   Wang Y., Bissada N., Cheng K., Roder J.C., Wang Y.T., Hayden M.R.;
RT   "NMDA receptor function and NMDA receptor-dependent phosphorylation of
RT   huntingtin is altered by the endocytic protein HIP1.";
RL   J. Neurosci. 27:2298-2308(2007).
RN   [11]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=16967501; DOI=10.1002/mrd.20564;
RA   Khatchadourian K., Smith C.E., Metzler M., Gregory M., Hayden M.R.,
RA   Cyr D.G., Hermo L.;
RT   "Structural abnormalities in spermatids together with reduced sperm
RT   counts and motility underlie the reproductive defect in HIP1-/-mice.";
RL   Mol. Reprod. Dev. 74:341-359(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-154, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Plays a role in clathrin-mediated endocytosis and
CC       trafficking. Involved in regulating AMPA receptor trafficking in
CC       the central nervous system in an NMDA-dependent manner. Enhances
CC       androgen receptor (AR)-mediated transcription. May act as a
CC       proapoptotic protein that induces cell death by acting through the
CC       intrinsic apoptosis pathway. Binds 3-phosphoinositides (via ENTH
CC       domain). May act through the ENTH domain to promote cell survival
CC       by stabilizing receptor tyrosine kinases following ligand-induced
CC       endocytosis. May play a functional role in the cell filament
CC       networks. May be required for differentiation, proliferation,
CC       and/or survival of somatic and germline progenitors.
CC   -!- SUBUNIT: Homodimer. Binds actin. Binds HTT (via N-terminus). This
CC       interaction is restricted to the brain. Binds to IFT57. In normal
CC       conditions, it poorly interacts with IFT57, HIP1 being strongly
CC       associated with HTT. However, in mutant HTT proteins with a long
CC       poly-Gln region, interaction between HTT and HIP1 is inhibited,
CC       promoting the interaction between HIP1 and IFT57. Interacts with
CC       CLTB (via N-terminus). Interacts (via coiled coil domain) with AR.
CC       Interacts with AP2A1, AP2A2, CLTC and HIP1R (By similarity).
CC       Interacts with GRIA1, GRIN2A AND GRIN2B.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Endomembrane system (By similarity). Cytoplasmic
CC       vesicle, clathrin-coated vesicle membrane (By similarity).
CC       Note=Shuttles between cytoplasm and nucleus. Nuclear translocation
CC       can be induced by AR (By similarity).
CC   -!- TISSUE SPECIFICITY: Most abundantly expressed in brain. In brain,
CC       expressed in cortical tissue, hippocampus, the molecular layer of
CC       the cerebellum and olfactory bulb. Also expressed in spinal cord
CC       and bone marrow (at protein level). Expressed in reproductive
CC       tissues.
CC   -!- DOMAIN: The pseudo DED region (pDED) mediates the interaction with
CC       IFT57 (By similarity).
CC   -!- DOMAIN: Binds F-actin via the talin-like I/LWEQ domain (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice develop a neurological phenotype by 3
CC       months of age, characterized by wasting, tremor and a gait ataxia
CC       secondary to a rigid thoracolumbar kyphosis. They also display
CC       micro-ophthalmia with nuclear cataracts. Mutant male mice are
CC       mostly infertile and exhibit testicular degeneration with
CC       increased apoptosis of postmeiotic spermatids. In comparison,
CC       Hip1-Hip1r double-knockout mice are dwarfed, afflicted with severe
CC       vertebral defects and die in early adulthood.
CC   -!- SIMILARITY: Belongs to the SLA2 family.
CC   -!- SIMILARITY: Contains 1 ENTH (epsin N-terminal homology) domain.
CC   -!- SIMILARITY: Contains 1 I/LWEQ domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH17516.1; Type=Erroneous initiation;
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DR   EMBL; BC017516; AAH17516.1; ALT_INIT; mRNA.
DR   EMBL; AK166346; BAE38720.1; -; mRNA.
DR   EMBL; AK220182; BAD90367.1; -; mRNA.
DR   IPI; IPI00762919; -.
DR   RefSeq; NP_666113.2; NM_146001.2.
DR   UniGene; Mm.280805; -.
DR   HSSP; O75146; 1R0D.
DR   ProteinModelPortal; Q8VD75; -.
DR   SMR; Q8VD75; 371-472, 481-572, 765-958.
DR   STRING; Q8VD75; -.
DR   PRIDE; Q8VD75; -.
DR   Ensembl; ENSMUST00000060311; ENSMUSP00000059033; ENSMUSG00000039959.
DR   GeneID; 215114; -.
DR   KEGG; mmu:215114; -.
DR   UCSC; uc008zyk.1; mouse.
DR   CTD; 215114; -.
DR   MGI; MGI:1099804; Hip1.
DR   GeneTree; ENSGT00550000074542; -.
DR   HOGENOM; HBG382566; -.
DR   HOVERGEN; HBG005968; -.
DR   InParanoid; Q8VD75; -.
DR   OMA; QRKTQEQ; -.
DR   OrthoDB; EOG4QC14M; -.
DR   NextBio; 374616; -.
DR   ArrayExpress; Q8VD75; -.
DR   Bgee; Q8VD75; -.
DR   Genevestigator; Q8VD75; -.
DR   GO; GO:0030665; C:clathrin coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IDA:UniProtKB.
DR   GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IMP:UniProtKB.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR011417; ANTH.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR013809; Epsin-like_N.
DR   InterPro; IPR002558; ILWEQ.
DR   Gene3D; G3DSA:1.25.40.90; ENTH_VHS; 1.
DR   Pfam; PF07651; ANTH; 1.
DR   Pfam; PF01608; I_LWEQ; 1.
DR   ProDom; PD011820; ILWEQ; 1.
DR   SMART; SM00273; ENTH; 1.
DR   SMART; SM00307; ILWEQ; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF48464; ENTH_VHS; 1.
DR   PROSITE; PS50942; ENTH; 1.
DR   PROSITE; PS50945; I_LWEQ; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Activator; Apoptosis; Coiled coil; Cytoplasm;
KW   Cytoplasmic vesicle; Differentiation; Endocytosis; Membrane;
KW   Neurodegeneration; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   1029       Huntingtin-interacting protein 1.
FT                                /FTId=PRO_0000361654.
FT   DOMAIN       32    160       ENTH.
FT   DOMAIN      763   1004       I/LWEQ.
FT   REGION      410    491       pDED.
FT   REGION      859    916       Important for actin binding (By
FT                                similarity).
FT   COILED      375    636       Potential.
FT   MOD_RES     154    154       Phosphothreonine.
FT   CONFLICT    402    402       M -> V (in Ref. 2; BAE38720).
FT   CONFLICT    427    427       M -> T (in Ref. 2; BAE38720).
SQ   SEQUENCE   1029 AA;  115202 MW;  D17B9EED8555450C CRC64;
     MDRMASSMKQ VSNPLPKVLS RRGVGAGMEA AERESFERTQ TVSVNKAINT QEVAVKEKHA
     RTCILGTHHE KGAQTFWSVV NRLPLSSNAM LCWKFCHVFH KLLRDGHPNV LKDSLRYKNE
     LSDMSRMWGH LSEGYGQLCS IYLKLLRTRM EYHTKNPRFP GNLQMSDRQL DEAGESDVNN
     FFQLTVEMFD YLECELNLFQ TVFNSLDMSR SVSVTTAGQC RLAPLIQVIL DCSHLYDYTV
     KLLFKLHSCL PADTLQGHRD RFMEQFTKLK DLFQRSSNLQ YFKRLIQIPQ LPENPPNFLR
     ASALSEHISP VVVIPAEVSS PDSEPVLEKD DLMDMDASQQ TLFDNKFDDV FGSSLSSDPF
     NFNNQNGVNK DEKDHLIERL YREISGLTGQ LDNMKIESQR AMLQLKGRVS ELEAELAEQQ
     HLGRQAMDDC EFLRTELDEL KRQREDTEKA QRSLTEIERK AQANEQRYSK LKEKYSELVQ
     NHADLLRKNA EVTKQVSVAR QAQVDLEREK KELADSFART QEQQDVLENL KHELATSRQE
     LQVLHSNLET SAQSEAKWLT QIAELEKEQG SLATVAAQRE EELSALRDQL ESTQIKLAGA
     QESMCQQVKD QRKTLLAGIR KAAEREIQEA LSQLEEPTLI SCAGSTDHLL SKVSSVSSCL
     EQLEKNGSQY LACPEDISEL LHSITLLAHL TGDTIIQGSA TSLRAPPEPA DSLTEACRQY
     GRETLAYLSS LEEEGTMENA DVTALRNCLS RVKTLGEELL PRGLDIKQEE LGDLVDKEMA
     ATSAAIEAAT TRIEEILSKS RAGDTGVKLE VNERILGSCT SLMQAIKVLV VASKDLQKEI
     VESGRGTASP KEFYAKNSRW TEGLISASKA VGWGATIMVD AADLVVQGKG KFEELMVCSR
     EIAASTAQLV AASKVKANKG SLNLTQLQQA SRGVNQATAA VVASTISGKS QIEETDSMDF
     SSMTLTQIKR QEMDSQVRVL ELENDLQKER QKLGELRKKH YELAGVAEGW EEGTEASPST
     VQEAIPDKE
//
ID   MYH9_MOUSE              Reviewed;        1960 AA.
AC   Q8VDD5; Q3UHT9; Q3UHU4; Q6KAN6; Q811I2;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 4.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Myosin-9;
DE   AltName: Full=Cellular myosin heavy chain, type A;
DE   AltName: Full=Myosin heavy chain 9;
DE   AltName: Full=Myosin heavy chain, non-muscle IIa;
DE   AltName: Full=Non-muscle myosin heavy chain A;
DE            Short=NMMHC-A;
DE   AltName: Full=Non-muscle myosin heavy chain IIa;
DE            Short=NMMHC II-a;
DE            Short=NMMHC-IIA;
GN   Name=Myh9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=21940628; PubMed=11943476; DOI=10.1016/S0378-1119(02)00455-9;
RA   D'Apolito M., Guarnieri V., Boncristiano M., Zelante L., Savoia A.;
RT   "Cloning of the murine non-muscle myosin heavy chain IIA gene ortholog
RT   of human MYH9 responsible for May-Hegglin, Sebastian, Fechtner, and
RT   Epstein syndromes.";
RL   Gene 286:215-222(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Amnion, Brain, Embryo, Embryonic liver, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-64; 83-102; 126-139; 144-159; 186-199; 210-225;
RP   241-261; 273-299; 302-355; 374-387; 408-419; 476-494; 518-536;
RP   564-613; 618-637; 645-651; 663-678; 683-702; 712-731; 738-755;
RP   765-775; 802-810; 815-821; 834-850; 910-923; 931-938; 941-959;
RP   975-989; 1001-1014; 1023-1035; 1052-1075; 1081-1091; 1106-1124;
RP   1136-1162; 1166-1174; 1182-1191; 1194-1210; 1227-1234; 1249-1260;
RP   1278-1295; 1302-1322; 1343-1353; 1358-1370; 1393-1400; 1405-1413;
RP   1418-1441; 1445-1454; 1484-1492; 1504-1518; 1529-1566; 1593-1602;
RP   1614-1620; 1659-1669; 1677-1694; 1698-1724; 1731-1751; 1754-1770;
RP   1792-1802; 1807-1828; 1844-1855; 1857-1867; 1877-1888; 1899-1912 AND
RP   1923-1932, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RA   Sumpton D.P., Sandilands E., Frame M.C., Bienvenut W.V.;
RL   Submitted (MAR-2008) to UniProtKB.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 626-1960.
RC   STRAIN=ICR; TISSUE=Embryonic tail;
RX   PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of FLJ genes:
RT   the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:127-135(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1066-1960.
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   ISGYLATION.
RX   PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
RA   Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
RA   Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
RT   "Proteomic identification of proteins conjugated to ISG15 in mouse and
RT   human cells.";
RL   Biochem. Biophys. Res. Commun. 336:496-506(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-754, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-181 AND SER-1943, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1939 AND SER-1943, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1939 AND SER-1943, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1943, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1939 AND SER-1943, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Cellular myosin that appears to play a role in
CC       cytokinesis, cell shape, and specialized functions such as
CC       secretion and capping.
CC   -!- SUBUNIT: Myosin is a hexameric protein that consists of 2 heavy
CC       chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2
CC       regulatory light chain subunits (MLC-2). Interacts with SVIL and
CC       SLC6A4 (By similarity). Interacts with PDLIM2.
CC   -!- DOMAIN: The rodlike tail sequence is highly repetitive, showing
CC       cycles of a 28-residue repeat pattern composed of 4 heptapeptides,
CC       characteristic for alpha-helical coiled coils.
CC   -!- PTM: ISGylated.
CC   -!- SIMILARITY: Contains 1 IQ domain.
CC   -!- SIMILARITY: Contains 1 myosin head-like domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE27768.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; AJ312390; CAC85955.1; -; mRNA.
DR   EMBL; AK147203; BAE27761.1; -; mRNA.
DR   EMBL; AK147206; BAE27763.1; -; mRNA.
DR   EMBL; AK147208; BAE27765.1; -; mRNA.
DR   EMBL; AK147209; BAE27766.1; -; mRNA.
DR   EMBL; AK147210; BAE27767.1; -; mRNA.
DR   EMBL; AK147211; BAE27768.1; ALT_INIT; mRNA.
DR   EMBL; AK147215; BAE27772.1; -; mRNA.
DR   EMBL; AK147216; BAE27773.1; -; mRNA.
DR   EMBL; AK147221; BAE27776.1; -; mRNA.
DR   EMBL; AK147222; BAE27777.1; -; mRNA.
DR   EMBL; AK147223; BAE27778.1; -; mRNA.
DR   EMBL; AK147233; BAE27783.1; -; mRNA.
DR   EMBL; AK147235; BAE27785.1; -; mRNA.
DR   EMBL; AK147296; BAE27829.1; -; mRNA.
DR   EMBL; AK147407; BAE27894.1; -; mRNA.
DR   EMBL; AK147430; BAE27906.1; -; mRNA.
DR   EMBL; AL583886; CAM23428.1; -; Genomic_DNA.
DR   EMBL; AK131171; BAD21421.1; -; mRNA.
DR   EMBL; BC044834; AAH44834.1; -; mRNA.
DR   IPI; IPI00123181; -.
DR   RefSeq; NP_071855.2; NM_022410.2.
DR   UniGene; Mm.29677; -.
DR   ProteinModelPortal; Q8VDD5; -.
DR   SMR; Q8VDD5; 4-807, 835-960, 1889-1921.
DR   DIP; DIP-29546N; -.
DR   MINT; MINT-2524850; -.
DR   STRING; Q8VDD5; -.
DR   PhosphoSite; Q8VDD5; -.
DR   PRIDE; Q8VDD5; -.
DR   Ensembl; ENSMUST00000016771; ENSMUSP00000016771; ENSMUSG00000022443.
DR   GeneID; 17886; -.
DR   KEGG; mmu:17886; -.
DR   CTD; 17886; -.
DR   MGI; MGI:107717; Myh9.
DR   HOGENOM; HBG717149; -.
DR   HOVERGEN; HBG004704; -.
DR   InParanoid; Q8VDD5; -.
DR   OMA; ERASRNK; -.
DR   OrthoDB; EOG4TXBR1; -.
DR   PhylomeDB; Q8VDD5; -.
DR   ArrayExpress; Q8VDD5; -.
DR   Bgee; Q8VDD5; -.
DR   CleanEx; MM_MYH9; -.
DR   Genevestigator; Q8VDD5; -.
DR   GermOnline; ENSMUSG00000022443; Mus musculus.
DR   GO; GO:0005826; C:actomyosin contractile ring; ISS:UniProtKB.
DR   GO; GO:0005913; C:cell-cell adherens junction; IDA:MGI.
DR   GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0016459; C:myosin complex; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR   GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
DR   GO; GO:0001931; C:uropod; IDA:MGI.
DR   GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0000146; F:microfilament motor activity; ISS:UniProtKB.
DR   GO; GO:0043495; F:protein anchor; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR   GO; GO:0030048; P:actin filament-based movement; ISS:UniProtKB.
DR   GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR   GO; GO:0043534; P:blood vessel endothelial cell migration; ISS:UniProtKB.
DR   GO; GO:0000904; P:cell morphogenesis involved in differentiation; IMP:MGI.
DR   GO; GO:0016337; P:cell-cell adhesion; IMP:MGI.
DR   GO; GO:0000910; P:cytokinesis; ISS:UniProtKB.
DR   GO; GO:0051295; P:establishment of meiotic spindle localization; IDA:MGI.
DR   GO; GO:0001768; P:establishment of T cell polarity; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0007132; P:meiotic metaphase I; IDA:MGI.
DR   GO; GO:0000212; P:meiotic spindle organization; IDA:MGI.
DR   GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISS:UniProtKB.
DR   GO; GO:0030224; P:monocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0007520; P:myoblast fusion; IMP:MGI.
DR   GO; GO:0030220; P:platelet formation; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR   GO; GO:0032796; P:uropod organization; IMP:MGI.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR004009; Myosin_N.
DR   InterPro; IPR002928; Myosin_tail.
DR   Pfam; PF00612; IQ; 1.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF02736; Myosin_N; 1.
DR   Pfam; PF01576; Myosin_tail_1; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 1.
DR   SMART; SM00242; MYSc; 1.
DR   PROSITE; PS50096; IQ; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; ATP-binding; Calmodulin-binding;
KW   Cell shape; Coiled coil; Direct protein sequencing; Motor protein;
KW   Myosin; Nucleotide-binding; Phosphoprotein; Ubl conjugation.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2   1960       Myosin-9.
FT                                /FTId=PRO_0000123417.
FT   DOMAIN        2    778       Myosin head-like.
FT   DOMAIN      779    808       IQ.
FT   NP_BIND     174    181       ATP (Potential).
FT   REGION      654    676       Actin-binding.
FT   COILED      841   1926       Potential.
FT   MOD_RES       2      2       N-acetylalanine.
FT   MOD_RES       8      8       N6-acetyllysine (By similarity).
FT   MOD_RES      11     11       Phosphotyrosine (By similarity).
FT   MOD_RES      74     74       N6-acetyllysine (By similarity).
FT   MOD_RES     102    102       N6-acetyllysine (By similarity).
FT   MOD_RES     181    181       Phosphothreonine.
FT   MOD_RES     299    299       N6-acetyllysine (By similarity).
FT   MOD_RES     545    545       N6-acetyllysine (By similarity).
FT   MOD_RES     638    638       Phosphothreonine (By similarity).
FT   MOD_RES     754    754       Phosphotyrosine.
FT   MOD_RES    1024   1024       N6-acetyllysine (By similarity).
FT   MOD_RES    1274   1274       N6-acetyllysine (By similarity).
FT   MOD_RES    1357   1357       N6-acetyllysine (By similarity).
FT   MOD_RES    1392   1392       N6-acetyllysine (By similarity).
FT   MOD_RES    1404   1404       N6-acetyllysine (By similarity).
FT   MOD_RES    1408   1408       Phosphotyrosine (By similarity).
FT   MOD_RES    1410   1410       N6-acetyllysine (By similarity).
FT   MOD_RES    1459   1459       N6-acetyllysine (By similarity).
FT   MOD_RES    1638   1638       N6-acetyllysine (By similarity).
FT   MOD_RES    1714   1714       Phosphoserine (By similarity).
FT   MOD_RES    1799   1799       Phosphoserine (By similarity).
FT   MOD_RES    1939   1939       Phosphothreonine.
FT   MOD_RES    1943   1943       Phosphoserine.
FT   CONFLICT   1733   1733       Q -> L (in Ref. 1; CAC85955).
SQ   SEQUENCE   1960 AA;  226372 MW;  AAAC0E83A0A4F24A CRC64;
     MAQQAADKYL YVDKNFINNP LAQADWAAKK LVWVPSSKNG FEPASLKEEV GEEAIVELVE
     NGKKVKVNKD DIQKMNPPKF SKVEDMAELT CLNEASVLHN LKERYYSGLI YTYSGLFCVV
     INPYKNLPIY SEEIVEMYKG KKRHEMPPHI YAITDTAYRS MMQDREDQSI LCTGESGAGK
     TENTKKVIQY LAHVASSHKS KKDQGELERQ LLQANPILEA FGNAKTVKND NSSRFGKFIR
     INFDVNGYIV GANIETYLLE KSRAIRQAKE ERTFHIFYYL LSGAGEHLKT DLLLEPYNKY
     RFLSNGHVTI PGQQDKDMFQ ETMEAMRIMG IPEDEQMGLL RVISGVLQLG NIAFKKERNT
     DQASMPDNTA AQKVSHLLGI NVTDFTRGIL TPRIKVGRDY VQKAQTKEQA DFAIEALAKA
     TYERMFRWLV LRINKALDKT KRQGASFIGI LDIAGFEIFD LNSFEQLCIN YTNEKLQQLF
     NHTMFILEQE EYQREGIEWN FIDFGLDLQP CIDLIEKPAG PPGILALLDE ECWFPKATDK
     SFVEKVVQEQ GTHPKFQKPK QLKDKADFCI IHYAGKVDYK ADEWLMKNMD PLNDNIATLL
     HQSSDKFVSE LWKDVDRIIG LDQVAGMSET ALPGAFKTRK GMFRTVGQLY KEQLAKLMAT
     LRNTNPNFVR CIIPNHEKKA GKLDPHLVLD QLRCNGVLEG IRICRQGFPN RVVFQEFRQR
     YEILTPNSIP KGFMDGKQAC VLMIKALELD SNLYRIGQSK VFFRAGVLAH LEEERDLKIT
     DVIIGFQACC RGYLARKAFA KRQQQLTAMK VLQRNCAAYL RLRNWQWWRL FTKVKPLLNS
     IRHEDELLAK EAELTKVREK HLAAENRLTE METMQSQLMA EKLQLQEQLQ AETELCAEAE
     ELRARLTAKK QELEEICHDL EARVEEEEER CQYLQAEKKK MQQNIQELEE QLEEEESARQ
     KLQLEKVTTE AKLKKLEEDQ IIMEDQNCKL AKEKKLLEDR VAEFTTNLME EEEKSKSLAK
     LKNKHEAMIT DLEERLRREE KQRQELEKTR RKLEGDSTDL SDQIAELQAQ IAELKMQLAK
     KEEELQAALA RVEEEAAQKN MALKKIRELE TQISELQEDL ESERASRNKA EKQKRDLGEE
     LEALKTELED TLDSTAAQQE LRSKREQEVS ILKKTLEDEA KTHEAQIQEM RQKHSQAVEE
     LADQLEQTKR VKATLEKAKQ TLENERGELA NEVKALLQGK GDSEHKRKKV EAQLQELQVK
     FSEGERVRTE LADKVTKLQV ELDSVTGLLS QSDSKSSKLT KDFSALESQL QDTQELLQEE
     NRQKLSLSTK LKQMEDEKNS FREQLEEEEE AKRNLEKQIA TLHAQVTDMK KKMEDGVGCL
     ETAEEAKRRL QKDLEGLSQR LEEKVAAYDK LEKTKTRLQQ ELDDLLVDLD HQRQSVSNLE
     KKQKKFDQLL AEEKTISAKY AEERDRAEAE AREKETKALS LARALEEAME QKAELERLNK
     QFRTEMEDLM SSKDDVGKSV HELEKSKRAL EQQVEEMKTQ LEELEDELQA TEDAKLRLEV
     NLQAMKAQFE RDLQGRDEQS EEKKKQLVRQ VREMEAELED ERKQRSMAMA ARKKLEMDLK
     DLEAHIDTAN KNREEAIKQL RKLQAQMKDC MRELDDTRAS REEILAQAKE NEKKLKSMEA
     EMIQLQEELA AAERAKRQAQ QERDELADEI ANSSGKGALA LEEKRRLEAR IAQLEEELEE
     EQGNTELIND RLKKANLQID QINTDLNLER SHAQKNENAR QQLERQNKEL KAKLQEMESA
     VKSKYKASIA ALEAKIAQLE EQLDNETKER QAASKQVRRT EKKLKDVLLQ VEDERRNAEQ
     FKDQADKAST RLKQLKRQLE EAEEEAQRAN ASRRKLQREL EDATETADAM NREVSSLKNK
     LRRGDLPFVV TRRIVRKGTG DCSDEEVDGK ADGADAKAAE
//
ID   PHIP_MOUSE              Reviewed;        1821 AA.
AC   Q8VDD9; Q3TS96; Q80VI6; Q9EPY1; Q9ESL6;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 2.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=PH-interacting protein;
DE            Short=PHIP;
DE   AltName: Full=IRS-1 PH domain-binding protein;
DE   AltName: Full=Neuronal differentiation-related protein;
DE            Short=NDRP;
DE   AltName: Full=WD repeat-containing protein 11;
GN   Name=Phip; Synonyms=Ndrp, Phip1, Wdr11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-1779.
RA   Antonarakis S.;
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-999, TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, AND INDUCTION.
RC   STRAIN=Swiss Webster / NIH;
RX   MEDLINE=21062561; PubMed=11098134;
RA   Kato H., Chen S., Kiyama H., Ikeda K., Kimura N., Nakashima K.,
RA   Taga T.;
RT   "Identification of a novel WD repeat-containing gene predominantly
RT   expressed in developing and regenerating neurons.";
RL   J. Biochem. 128:923-932(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-893.
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 745-1458.
RC   STRAIN=C57BL/6J; TISSUE=Egg;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 924-1821, FUNCTION, INTERACTION WITH
RP   IRS1 AND IRS2, AND TISSUE SPECIFICITY.
RX   MEDLINE=20568313; PubMed=11018022; DOI=10.1074/jbc.C000611200;
RA   Farhang-Fallah J., Yin X., Trentin G., Cheng A.M., Rozakis-Adcock M.;
RT   "Cloning and characterization of PHIP, a novel insulin receptor
RT   substrate-1 pleckstrin homology domain interacting protein.";
RL   J. Biol. Chem. 275:40492-40497(2000).
RN   [6]
RP   PROTEIN SEQUENCE OF 1589-1596, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   FUNCTION.
RX   PubMed=12242307; DOI=10.1128/MCB.22.20.7325-7336.2002;
RA   Farhang-Fallah J., Randhawa V.K., Nimnual A., Klip A., Bar-Sagi D.,
RA   Rozakis-Adcock M.;
RT   "The pleckstrin homology (PH) domain-interacting protein couples the
RT   insulin receptor substrate 1 PH domain to insulin signaling pathways
RT   leading to mitogenesis and GLUT4 translocation.";
RL   Mol. Cell. Biol. 22:7325-7336(2002).
RN   [8]
RP   FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=17636024; DOI=10.1128/MCB.02409-06;
RA   Podcheko A., Northcott P., Bikopoulos G., Lee A., Bommareddi S.R.,
RA   Kushner J.A., Farhang-Fallah J., Rozakis-Adcock M.;
RT   "Identification of a WD40 repeat-containing isoform of PHIP as a novel
RT   regulator of beta-cell growth and survival.";
RL   Mol. Cell. Biol. 27:6484-6496(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1281 AND SER-1283, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-879; SER-880 AND
RP   SER-881, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1281 AND SER-1283, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Probable regulator of the insulin and insulin-like
CC       growth factor signaling pathways. Stimulates cell proliferation
CC       through regulation of cyclin transcription and has an anti-
CC       apoptotic activity through AKT1 phosphorylation and activation.
CC   -!- SUBUNIT: Interacts with IRS1 and IRS2.
CC   -!- INTERACTION:
CC       Q28224:IRS1 (xeno); NbExp=1; IntAct=EBI-1369766, EBI-1369894;
CC       P35569:Irs1; NbExp=1; IntAct=EBI-1369766, EBI-400825;
CC       P35570:Irs1 (xeno); NbExp=1; IntAct=EBI-1369766, EBI-520230;
CC       P81122:Irs2; NbExp=1; IntAct=EBI-1369766, EBI-1369862;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Widely expressed with most abundant expression
CC       detected in pancreatic islets, brain and skeletal muscle.
CC       Predominantly expressed in developing and regenerating neurons.
CC       Expressed in adult brain (granular layer of the olfactorium bulb,
CC       hippocampus, dentate gyrus and cerebellum internal granular
CC       layer). Expressed in the CA3 region of adult hippocampus, adult
CC       and fetal retina, perinatal dorsal root ganglion and embryonal
CC       olfactory epithelia (at protein level).
CC   -!- DEVELOPMENTAL STAGE: Expressed at highest levels at 17.5 dpc in
CC       the neural layer of the retina and olfactory epithelia.
CC   -!- INDUCTION: In motor neurons after injury.
CC   -!- SIMILARITY: Contains 2 bromo domains.
CC   -!- SIMILARITY: Contains 8 WD repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG45146.1; Type=Miscellaneous discrepancy; Note=Intron retention. This sequence is incomplete at the 5' end and extensively differs from that shown;
CC       Sequence=AAH49950.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=BAB16299.1; Type=Miscellaneous discrepancy; Note=Intron retention. This sequence is incomplete at the 3' end and extensively differs from that shown;
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DR   EMBL; AJ303103; CAC83119.1; -; mRNA.
DR   EMBL; AB049460; BAB16299.1; ALT_SEQ; mRNA.
DR   EMBL; BC049950; AAH49950.1; ALT_TERM; mRNA.
DR   EMBL; AK162189; BAE36779.1; -; mRNA.
DR   EMBL; AF310251; AAG45146.1; ALT_SEQ; mRNA.
DR   IPI; IPI00311490; -.
DR   UniGene; Mm.221688; -.
DR   HSSP; P16649; 1ERJ.
DR   ProteinModelPortal; Q8VDD9; -.
DR   SMR; Q8VDD9; 155-547, 1164-1431.
DR   IntAct; Q8VDD9; 5.
DR   STRING; Q8VDD9; -.
DR   PhosphoSite; Q8VDD9; -.
DR   PRIDE; Q8VDD9; -.
DR   Ensembl; ENSMUST00000034787; ENSMUSP00000034787; ENSMUSG00000032253.
DR   UCSC; uc009qvv.1; mouse.
DR   MGI; MGI:1932404; Phip.
DR   GeneTree; ENSGT00390000010788; -.
DR   HOGENOM; HBG444387; -.
DR   HOVERGEN; HBG108248; -.
DR   InParanoid; Q8VDD9; -.
DR   OrthoDB; EOG41ZF90; -.
DR   ArrayExpress; Q8VDD9; -.
DR   Bgee; Q8VDD9; -.
DR   CleanEx; MM_PHIP; -.
DR   Genevestigator; Q8VDD9; -.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IDA:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptosis; IDA:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
DR   GO; GO:0043568; P:positive regulation of insulin-like growth factor receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0045840; P:positive regulation of mitosis; IMP:UniProtKB.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:MGI.
DR   GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0006606; P:protein import into nucleus; IMP:MGI.
DR   GO; GO:0040008; P:regulation of growth; IMP:MGI.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR011047; Quino_AlcDH-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:1.20.920.10; Bromodomain; 2.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
DR   Pfam; PF00439; Bromodomain; 2.
DR   Pfam; PF00400; WD40; 7.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 2.
DR   SMART; SM00320; WD40; 8.
DR   SUPFAM; SSF47370; Bromodomain; 2.
DR   SUPFAM; SSF50998; Quin_alc_DH_like; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 2.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Bromodomain; Direct protein sequencing; Nucleus;
KW   Phosphoprotein; Repeat; WD repeat.
FT   CHAIN         1   1821       PH-interacting protein.
FT                                /FTId=PRO_0000297758.
FT   REPEAT      181    222       WD 1.
FT   REPEAT      224    262       WD 2.
FT   REPEAT      265    310       WD 3.
FT   REPEAT      319    360       WD 4.
FT   REPEAT      363    402       WD 5.
FT   REPEAT      422    461       WD 6.
FT   REPEAT      464    504       WD 7.
FT   REPEAT      512    551       WD 8.
FT   DOMAIN     1176   1246       Bromo 1.
FT   DOMAIN     1333   1403       Bromo 2.
FT   REGION      924   1129       Mediates interaction with IRS1.
FT   COMPBIAS    867    923       Lys-rich.
FT   COMPBIAS   1752   1758       Poly-Glu.
FT   MOD_RES     136    136       Phosphoserine (By similarity).
FT   MOD_RES     140    140       Phosphotyrosine (By similarity).
FT   MOD_RES     683    683       Phosphoserine (By similarity).
FT   MOD_RES     692    692       Phosphoserine (By similarity).
FT   MOD_RES     832    832       Phosphoserine (By similarity).
FT   MOD_RES     879    879       Phosphoserine.
FT   MOD_RES     880    880       Phosphoserine.
FT   MOD_RES     881    881       Phosphoserine.
FT   MOD_RES    1281   1281       Phosphoserine.
FT   MOD_RES    1283   1283       Phosphoserine.
FT   MOD_RES    1296   1296       Phosphoserine (By similarity).
FT   MOD_RES    1474   1474       Phosphoserine (By similarity).
FT   MOD_RES    1479   1479       Phosphoserine (By similarity).
FT   MOD_RES    1497   1497       N6-acetyllysine (By similarity).
FT   MOD_RES    1524   1524       Phosphoserine (By similarity).
FT   MOD_RES    1525   1525       Phosphoserine (By similarity).
FT   MOD_RES    1533   1533       N6-acetyllysine (By similarity).
FT   MOD_RES    1548   1548       Phosphoserine (By similarity).
FT   MOD_RES    1651   1651       Phosphoserine (By similarity).
FT   MOD_RES    1762   1762       Phosphoserine (By similarity).
FT   CONFLICT    672    672       R -> G (in Ref. 3; AAH49950).
FT   CONFLICT   1065   1065       P -> R (in Ref. 4; BAE36779 and 5;
FT                                AAG45146).
FT   CONFLICT   1155   1155       E -> D (in Ref. 5; AAG45146).
FT   CONFLICT   1392   1392       F -> S (in Ref. 4; BAE36779 and 5;
FT                                AAG45146).
FT   CONFLICT   1776   1776       A -> T (in Ref. 5; AAG45146).
SQ   SEQUENCE   1821 AA;  206726 MW;  92E8DF0833F60FFA CRC64;
     MSRERKGLSE LRSELYFLIA RFLEDGPCQQ AAQVLIREVA EKELLPRRTD WTGKEHPRTY
     QNLVKYYRHL APDHLLQICH RLGPLLEQEI PQSVPGVQTL LGAGRQSLLR TNKSCKHVVW
     KGSALAALHC GRPPESPVNY GSPPSIADTL FSRKLNGKYR LERLVPTAVY QHMKMHKRIL
     GHLSSVYCVT FDRTGRRIFT GSDDCLVKIW ATDDGRLLAT LRGHAAEISD MAVNYENTMI
     AAGSCDKMIR VWCLRTCAPL AVLQGHSASI TSLQFSPLCS GSKRYLSSTG ADGTICFWLW
     DAGTLKINPR PTKFTERPRP GVQMICSSFS AGGMFLATGS TDHIIRVYFF GSGQPEKISE
     LEFHTDKVDS IQFSNTSNRF VSGSRDGTAR IWQFKRREWK SILLDMATRP AGQNLQGIED
     KITKMKVTMV AWDRHDNTVI TAVNNMTLKV WNSYTGQLIH VLMGHEDEVF VLEPHPFDPR
     VLFSAGHDGN VIVWDLARGV KVRSYFNMIE GQGHGAVFDC KCSPDGQHFA CTDSHGHLLI
     FGFGSSSKYD KIADQMFFHS DYRPLIRDAN NFVLDEQTQQ APHLMPPPFL VDVDGNPHPS
     RYQRLVPGRE NCREEQLIPQ MGVTSSGLNQ VLSQQANQDI SPLDSMIQRL QQEQDLRRSG
     EAGVSNASRV NRGSVSSTSE VHSPPNIGLR RSGQIEGVRQ MHSNAPRSEI ATERDLVAWS
     RRVVVPELSA GVASRQEEWR TAKGEEEIKS YRSEEKRKHL TVAKENKILT VSKNHAHEHF
     LDLGDSKKQQ ANQHNYRTRS ALEETPRPLE ELENGTSSSD EGEVLAVSGG TSEEEERAWH
     SDGSSSDYSS DYSDWTADAG INLQPPKKVP KHKTKKPESS SDEEEESENQ KQKHIKKERK
     KANEEKDGPT SPKKKKPKER KQKRLAVGEL TENGLTLEEW LPSAWITDTL PRRCPFVPQM
     GDEVYYFRQG HEAYVEMARK NKIYSINPKK QPWHKMELRE QELMKIVGIK YEVGLPTLCC
     LKLAFLDPDT GKLTGGSFTM KYHDMPDVID FLVLRQQFDD AKYRPWNIGD RFRSVIDDAW
     WFGTIESQEP LQPEYPDSLF QCYNVCWDNG DTEKMSPWDM ELIPNNAVFP EELGTSVPLT
     DVECRSLIYK PLDGEWGANP RDEECERIVG GINQLMTLDI ASAFVAPVDL QAYPMYCTVV
     AYPTDLSTIK QRLENRFYRR FSSLMWEVRY IEHNTRTFNE PGSPIVKSAK FVTDLLLHFI
     KDQTCYNIIP LYNSMKKKVL SDSEEEEKDA DVPGTSTRKR KDHQPRRRLR NRAQSYDIQA
     WKKQCQELLN LIFQCEDSEP FRQPVDLLEY PDYRDIIDTP MDFATVRETL EAGNYESPME
     LCKDVRLIFS NFKAYTPSKR SRIYSMSLRL SAFFEEHISS VLSDYKSALR FHKRNTISKK
     RKKRNRSSSL SSSAASSPER KKRILKPQLK SEVSTSPFSI PTRSVLPRHN AAQMNGKPES
     SSVVRTRSNR VAVDPVVTEQ PSTSSATKAF VSKTNTSAMP GKAMLENSVR HSKALSTLSS
     PDPLTFSHAT KNNSAKENME KEKPVKRKMK SSVFSKASPL PKSAAVIEQG ECKNNVLIPG
     TIQVNGHGGQ PSKLVKRGPG RKPKVEVNTS SGEVTHKKRG RKPKNLQCAK QENSEQNNMH
     PIRADVLPSS TCNFLSETNA VKEDLLQKKS RGGRKPKRKM KTHNLDSELI VPTNVKVLRR
     SNRKKTDDPI DEEEEFEELK GSEPHMRTRN QGRRTAFYNE DDSEEEQRQL LFEDTSLTFG
     TSSRGRVRKL TEKAKANLIG W
//
ID   M3KL4_MOUSE             Reviewed;        1002 AA.
AC   Q8VDG6; Q5DTU6; Q811F5;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 2.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Mitogen-activated protein kinase kinase kinase MLK4;
DE            EC=2.7.11.25;
DE   AltName: Full=Mixed lineage kinase 4;
GN   Name=Mlk4; Synonyms=Kiaa1804;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic intestine;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Activates the JUN N-terminal pathway (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Homodimerization via the leucine zipper domains
CC       is required for autophosphorylation and subsequent activation (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- PTM: Autophosphorylation on serine and threonine residues within
CC       the activation loop plays a role in enzyme activation (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90469.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC       Sequence=BAD90469.1; Type=Frameshift; Positions=724;
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DR   EMBL; AK220424; BAD90469.1; ALT_SEQ; mRNA.
DR   EMBL; BC021891; AAH21891.1; -; mRNA.
DR   EMBL; BC046448; AAH46448.1; -; mRNA.
DR   IPI; IPI00123268; -.
DR   RefSeq; NP_663583.2; NM_145608.2.
DR   UniGene; Mm.216458; -.
DR   HSSP; O89100; 1UTI.
DR   ProteinModelPortal; Q8VDG6; -.
DR   SMR; Q8VDG6; 25-386.
DR   STRING; Q8VDG6; -.
DR   PhosphoSite; Q8VDG6; -.
DR   PRIDE; Q8VDG6; -.
DR   Ensembl; ENSMUST00000034316; ENSMUSP00000034316; ENSMUSG00000031853.
DR   GeneID; 234878; -.
DR   KEGG; mmu:234878; -.
DR   NMPDR; fig|10090.3.peg.19474; -.
DR   UCSC; uc009nyq.1; mouse.
DR   MGI; MGI:2385307; BC021891.
DR   eggNOG; roNOG08253; -.
DR   GeneTree; ENSGT00600000084346; -.
DR   HOGENOM; HBG716519; -.
DR   HOVERGEN; HBG067662; -.
DR   InParanoid; Q8VDG6; -.
DR   OMA; ESALCEC; -.
DR   OrthoDB; EOG44F68G; -.
DR   PhylomeDB; Q8VDG6; -.
DR   BRENDA; 2.7.11.25; 244.
DR   NextBio; 382421; -.
DR   ArrayExpress; Q8VDG6; -.
DR   Bgee; Q8VDG6; -.
DR   CleanEx; MM_BC021891; -.
DR   Genevestigator; Q8VDG6; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004709; F:MAP kinase kinase kinase activity; IEA:EC.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR015785; MAPKKK-like.
DR   InterPro; IPR016231; MAPKKK9/10/11.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   PANTHER; PTHR23257:SF87; MAPKKK-like; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PIRSF; PIRSF000556; MAPKKK9_11; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein; Repeat;
KW   Serine/threonine-protein kinase; SH3 domain; Transferase.
FT   CHAIN         1   1002       Mitogen-activated protein kinase kinase
FT                                kinase MLK4.
FT                                /FTId=PRO_0000302761.
FT   DOMAIN       24     88       SH3.
FT   DOMAIN      110    390       Protein kinase.
FT   DOMAIN      409    430       Leucine-zipper 1.
FT   DOMAIN      444    466       Leucine-zipper 2.
FT   NP_BIND     116    124       ATP (By similarity).
FT   COMPBIAS     85    102       Pro-rich.
FT   ACT_SITE    247    247       Proton acceptor (By similarity).
FT   BINDING     137    137       ATP (By similarity).
FT   MOD_RES     283    283       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     287    287       Phosphoserine; by autocatalysis and
FT                                MAP4K1 (By similarity).
FT   MOD_RES     439    439       Phosphoserine (By similarity).
FT   MOD_RES     498    498       Phosphoserine (By similarity).
FT   MOD_RES     512    512       Phosphoserine (By similarity).
FT   MOD_RES     527    527       Phosphoserine (By similarity).
FT   MOD_RES     531    531       Phosphoserine (By similarity).
FT   MOD_RES     576    576       Phosphothreonine (By similarity).
FT   MOD_RES     598    598       Phosphoserine (By similarity).
FT   MOD_RES     708    708       Phosphoserine (By similarity).
FT   MOD_RES     748    748       Phosphoserine (By similarity).
FT   MOD_RES     781    781       Phosphoserine (By similarity).
FT   CONFLICT    411    411       Missing (in Ref. 2; AAH21891).
SQ   SEQUENCE   1002 AA;  110112 MW;  C4E706833A578C78 CRC64;
     MALPVAEGTA DTPLSPARDD SGSTSSGMWA ALYDYEARGE DELSLRRGQL VEVLSQDAAV
     SGDEGWWAGQ VQRRLGIFPA SYVAPCGPVP PPAPPPPRPC SPVHVDFERL ELKELIGAGG
     FGQVYRATWQ GQEVAVKAAR RDPEQDAAAA AESVRREARL FAMLRHPNII QLRGVCLRQP
     HLCLVLEFAR GGALNRALAA AASDPRAPGP RRARRIPPQV LVNWAVQIAR GMLYLHEEAV
     VPILHRDLKS SNILLLEKIE HDDICNKTLK ITDFGLAREW HRTTRMSAAG TYAWMAPEVI
     RSSLFSKGSD IWSYGVLLWE LLTGEVPYRG IDGLAVAYGV AVNKLTLPIP STCPEPFAKL
     MKECWEQDPH IRPSFALILQ QLTAIEEAVL TNMPQESFHS MQEDWKLEIQ QMFSELRTKE
     KELRSREEEL SRAALQQKSQ ELLLRRREQQ LAEREIDVLE RELNVLIFQL SQEAPHVKKR
     KGRFRRGRLR LKDGHRISLP SDFQHKITVQ ASPTLDKRRS SDSGLCSPPG SPLMLPRLRA
     IQLTSDENNK TRGRNMVFRQ EDFEDVKRSF KKKGCTWGPS SVQTKERPEG RERVRPLSDG
     NSPWSSLLIK SQKTTPLASL FVDQPGSCEE QKLVPEGLEH RKPKQTKFPG QAHVGLPLCK
     DSQREDSSEA ESREEGSPKG SPVNNVGAPM LRKKTESALC ECGMLLASMA LGLDVRKLHG
     AQAPAKPSPK MEKKEEGALQ PASRCQSSPS SLLRQPSAGR APSGGSTLLL PSAPSHSSKS
     SLSMKCLLQA GKEESSLGNA RDLCGPTTLT PDPGSAAPES GCELIPGLRP KTDYGVLRSM
     PHAILEQTGE RLPGCAIVGD KGCHHMQMGS EETPLWLQSA PEDSGLPHSP SPGPQRDLAS
     QASLVKPEGV LGECQACPAL PQRPHTASVR TTSPPTWVCD KDHQVPALAC LLGAQERSRC
     QTPSLLDASI EGQKKDCAMP LCRVKSVMCQ PSIYALEKDF LT
//
ID   VIGLN_MOUSE             Reviewed;        1268 AA.
AC   Q8VDJ3;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Vigilin;
DE   AltName: Full=High density lipoprotein-binding protein;
DE            Short=HDL-binding protein;
GN   Name=Hdlbp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
CC   -!- FUNCTION: Appears to play a role in cell sterol metabolism. It may
CC       function to protect cells from over-accumulation of cholesterol
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- SIMILARITY: Contains 14 KH domains.
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DR   EMBL; BC021765; AAH21765.1; -; mRNA.
DR   EMBL; BC023806; AAH23806.1; -; mRNA.
DR   EMBL; BC025648; AAH25648.1; -; mRNA.
DR   EMBL; BC027779; AAH27779.1; -; mRNA.
DR   EMBL; BC027788; AAH27788.1; -; mRNA.
DR   EMBL; BC035301; AAH35301.1; -; mRNA.
DR   IPI; IPI00123379; -.
DR   RefSeq; NP_598569.1; NM_133808.4.
DR   UniGene; Mm.30012; -.
DR   ProteinModelPortal; Q8VDJ3; -.
DR   SMR; Q8VDJ3; 142-580, 582-1200.
DR   STRING; Q8VDJ3; -.
DR   PhosphoSite; Q8VDJ3; -.
DR   PRIDE; Q8VDJ3; -.
DR   Ensembl; ENSMUST00000042498; ENSMUSP00000043047; ENSMUSG00000034088.
DR   GeneID; 110611; -.
DR   KEGG; mmu:110611; -.
DR   UCSC; uc007cdx.1; mouse.
DR   CTD; 110611; -.
DR   MGI; MGI:99256; Hdlbp.
DR   GeneTree; ENSGT00580000081604; -.
DR   HOGENOM; HBG357724; -.
DR   HOVERGEN; HBG054107; -.
DR   InParanoid; Q8VDJ3; -.
DR   OMA; ELEQMVS; -.
DR   OrthoDB; EOG4M65GT; -.
DR   PhylomeDB; Q8VDJ3; -.
DR   NextBio; 364327; -.
DR   ArrayExpress; Q8VDJ3; -.
DR   Bgee; Q8VDJ3; -.
DR   CleanEx; MM_HDLBP; -.
DR   Genevestigator; Q8VDJ3; -.
DR   GermOnline; ENSMUSG00000034088; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR004088; KH_type_1.
DR   InterPro; IPR018111; KH_type_1_subgr.
DR   Pfam; PF00013; KH_1; 14.
DR   SMART; SM00322; KH; 14.
DR   PROSITE; PS50084; KH_TYPE_1; 14.
PE   1: Evidence at protein level;
KW   Acetylation; Cholesterol metabolism; Cytoplasm; HDL; Lipid metabolism;
KW   Lipid transport; Nucleus; Phosphoprotein; Repeat; RNA-binding;
KW   Steroid metabolism; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1268       Vigilin.
FT                                /FTId=PRO_0000050132.
FT   DOMAIN      150    212       KH 1.
FT   DOMAIN      222    284       KH 2.
FT   DOMAIN      295    357       KH 3.
FT   DOMAIN      364    424       KH 4.
FT   DOMAIN      435    497       KH 5.
FT   DOMAIN      507    570       KH 6.
FT   DOMAIN      581    643       KH 7.
FT   DOMAIN      653    716       KH 8.
FT   DOMAIN      727    790       KH 9.
FT   DOMAIN      800    863       KH 10.
FT   DOMAIN      873    967       KH 11.
FT   DOMAIN      972   1034       KH 12.
FT   DOMAIN     1052   1117       KH 13.
FT   DOMAIN     1127   1190       KH 14.
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES      31     31       Phosphoserine.
FT   MOD_RES     295    295       Phosphothreonine (Potential).
FT   MOD_RES     296    296       Phosphothreonine (Potential).
FT   MOD_RES     437    437       Phosphotyrosine (By similarity).
FT   MOD_RES     944    944       Phosphoserine (By similarity).
FT   MOD_RES    1223   1223       Phosphoserine (By similarity).
SQ   SEQUENCE   1268 AA;  141743 MW;  2502F3D4E9EE230C CRC64;
     MSSVAVLTQE SFAEHRSGLV PQQIKVATLN SEEENDPPTY KDAFPPLPEK AACLESAQEP
     AGAWSNKIRP IKASVITQVF HVPLEERKYK DMNQFGEGEQ AKICLEIMQR TGAHLELSLA
     KDQGLSIMVS GKLDAVMKAR KDIVARLQTQ ASATVPIPKE HHRFVIGKNG EKLQDLELKT
     ATKIQIPRPD DPSNQIKITG TKEGIEKARH EVLLISAEQD KRAVERLEVE KAFHPFIAGP
     YNRLVGEIMQ ETGTRINIPP PSVNRTEIVF TGEKEQLAQA VARIKKIYEE KKKKTTTIAV
     EVKKSQHKYV IGPKGNSLQE ILERTGVSVE IPPSDSISET VILRGEPEKL GQALTEVYAK
     ANSFTVSSVS APSWLHRFII GKKGQNLAKI TQQMPKVHIE FTEGEDKITL EGPTEDVNVA
     QEQIEGMVKD LINRMDYVEI NIDHKFHRHL IGKSGANINR IKDQYKVSVR IPPDSEKSNL
     IRIEGDPQGV QQAKRELLEL ASRMENERTK DLIIEQRFHR TIIGQKGERI REIRDKFPEV
     IINFPDPAQK SDIVQLRGPK NEVEKCTKYM QKMVADLVEN SYSISVPIFK QFHKNIIGKG
     GANIKKIREE SNTKIDLPAE NSNSETIIIT GKRANCEAAR SRILSIQKDL ANIAEVEVSI
     PAKLHNSLIG TKGRLIRSIM EECGGVHIHF PVEGSGSDTV VIRGPSSDVE KAKKQLLHLA
     EEKQTKSFTV DIRAKPEYHK FLIGKGGGKI RKVRDSTGAR IIFPAAEDKD QDLITIIGKE
     DAVREAQKEL EALIQNLENV VEDYMLVDPK HHRHFVIRRG QVLREIAEEY GGVMVSFPRS
     GTQSDKVTLK GAKDCVEAAK KRIQEIIEDL EAQVTVECAI PQKFHRSVMG PKGSRIQQIT
     RDYNVQIKFP DREENPVHSV EPSIQENGDE AGEGREAKET DPGSPRRCDI IIISGRKEKC
     EAAKEALEAL VPVTIEVEVP FDLHRYIIGQ KGSGIRKMMD EFEVNIHVPA PELQSDTIAI
     TGLAANLDRA KAGLLDRVKE LQAEQEDRAL RSFKLSVTVD PKYHPKIIGR KGAVITQIRL
     EHEVNIQFPD KDDGNQPQDQ ITITGYEKNT EAARDAILKI VGELEQMVSE DVPLDHRVHA
     RIIGARGKAI RKIMDEFKVD IRFPQSGAPD PNCVTVTGLP ENVEEAIDHI LNLEEEYLAD
     VVDSEALQVY MKPPAHEESR APSKGFVVRD APWTSNSSEK APDMSSSEEF PSFGAQVAPK
     TLPWGPKR
//
ID   Q8VDM3_MOUSE            Unreviewed;       792 AA.
AC   Q8VDM3;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   SubName: Full=Auts2 protein;
DE   Flags: Fragment;
GN   Name=Auts2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor. C3;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC021509; AAH21509.1; -; mRNA.
DR   IPI; IPI00677049; -.
DR   UniGene; Mm.389695; -.
DR   UniGene; Mm.409595; -.
DR   STRING; Q8VDM3; -.
DR   Ensembl; ENSMUST00000160071; ENSMUSP00000125349; ENSMUSG00000029673.
DR   UCSC; uc008zut.1; mouse.
DR   MGI; MGI:1919847; Auts2.
DR   GeneTree; ENSGT00390000001466; -.
DR   HOGENOM; HBG713331; -.
DR   HOVERGEN; HBG050644; -.
DR   InParanoid; Q8VDM3; -.
DR   ArrayExpress; Q8VDM3; -.
DR   Bgee; Q8VDM3; -.
DR   Genevestigator; Q8VDM3; -.
DR   InterPro; IPR023246; AUTS2.
DR   PRINTS; PR02044; FIBROSIN1LPF.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   792 AA;  88263 MW;  F569EEF530349CF4 CRC64;
     TRPGHPAGST YSEQDILRQE LNTRFLASQS ADRGASLGPP PYLRTEFHQH QHQHQHTHQH
     THQHTFTPFP HAIPPTAIMP TPAPPMVRTP GRNFDKYPTK VDPFYRHSLF HSYPPAVSGI
     PPMIPPTGPF GSLQGAFQPK TSNPIDVAAR PGTVPHTLLQ KDPRLTDPFR PMLRKPGKWC
     AMHVHIAWQI YHHQQKVKKQ MQSDPHKLDF GLKPEFLSRP PGPSLFGAIH HPHDLARPST
     LFSAAGAAHP TGTPFGPPPH HSNFLNPAAH LEPFNRPSTF TGLAAVGGNA FGGLGNPSVT
     PNSVFGHKDS PSVQNFSNPH EPWNRLHRTP PSFPTPPPWL KPGELERSAS AAAHDRDRDV
     DKRDSSVSKD DKERESVEKR HPSHPSPAPP VPVSALGHNR SSTDPTTRGH LNTEAREKDK
     PKEKERDHSG SRKDLTTEEH KAKESHLPER DGHSHEGRAA GEEPKQLSRV PSPYVRTPGV
     DSTRPNSTSS REAEPRKGEP AYENPKKNAE VKVKEERKED HDLPTEAPQA HRTSEAPPPS
     SSASASVHPG PLASMPMTVG VTGIHAMNSI GSLDRTRMVT PFMGLSPIPG GERFPYPSFH
     WDPMRDPLRD PYRDLDMHRR DPLGRDFLLR NDPLHRLSTP RLYEADRSFR DREPHDYSHH
     HHHHHHPLAV DPRREHERGG HLDDRERLHV LREDYEHPRL HPVHPASLDG HLPHPSLLTP
     GLPSMHYPRI SPTAGHQNGL LNKTPPTAAL SAPPPLISTL GGRPGSPRRT TPLSAEIRER
     PPSHTLKDIE AR
//
ID   PSMD2_MOUSE             Reviewed;         908 AA.
AC   Q8VDM4;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=26S proteasome non-ATPase regulatory subunit 2;
DE   AltName: Full=26S proteasome regulatory subunit RPN1;
DE   AltName: Full=26S proteasome regulatory subunit S2;
DE   AltName: Full=26S proteasome subunit p97;
GN   Name=Psmd2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N; TISSUE=Colon, Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20 AND SER-22, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-20, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Acts as a regulatory subunit of the 26 proteasome which
CC       is involved in the ATP-dependent degradation of ubiquitinated
CC       proteins (By similarity).
CC   -!- SIMILARITY: Belongs to the proteasome subunit S2 family.
CC   -!- SIMILARITY: Contains 7 PC repeats.
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DR   EMBL; BC021508; AAH21508.1; -; mRNA.
DR   EMBL; BC024830; AAH24830.1; -; mRNA.
DR   EMBL; BC027388; AAH27388.1; -; mRNA.
DR   EMBL; BC027767; AAH27767.1; -; mRNA.
DR   EMBL; BC027822; AAH27822.1; -; mRNA.
DR   EMBL; BC028851; AAH28851.1; -; mRNA.
DR   EMBL; BC031128; AAH31128.1; -; mRNA.
DR   IPI; IPI00123494; -.
DR   RefSeq; NP_598862.1; NM_134101.2.
DR   UniGene; Mm.243234; -.
DR   ProteinModelPortal; Q8VDM4; -.
DR   SMR; Q8VDM4; 649-750.
DR   STRING; Q8VDM4; -.
DR   PhosphoSite; Q8VDM4; -.
DR   PRIDE; Q8VDM4; -.
DR   Ensembl; ENSMUST00000007212; ENSMUSP00000007212; ENSMUSG00000006998.
DR   GeneID; 21762; -.
DR   KEGG; mmu:21762; -.
DR   UCSC; uc007yqq.1; mouse.
DR   CTD; 21762; -.
DR   MGI; MGI:1096584; Psmd2.
DR   HOGENOM; HBG314403; -.
DR   HOVERGEN; HBG001842; -.
DR   InParanoid; Q8VDM4; -.
DR   OMA; SKFSHDS; -.
DR   OrthoDB; EOG483D3X; -.
DR   PhylomeDB; Q8VDM4; -.
DR   NextBio; 301080; -.
DR   Bgee; Q8VDM4; -.
DR   Genevestigator; Q8VDM4; -.
DR   GermOnline; ENSMUSG00000006998; Mus musculus.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0042176; P:regulation of protein catabolic process; IEA:InterPro.
DR   InterPro; IPR016643; 26S_Psome_Rpn1.
DR   InterPro; IPR002015; APC_proteasome.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF01851; PC_rep; 2.
DR   PIRSF; PIRSF015965; 26S_Psome_Rpn1; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein; Proteasome; Repeat.
FT   CHAIN         1    908       26S proteasome non-ATPase regulatory
FT                                subunit 2.
FT                                /FTId=PRO_0000173811.
FT   REPEAT      409    442       PC 1.
FT   REPEAT      443    479       PC 2.
FT   REPEAT      480    514       PC 3.
FT   REPEAT      517    551       PC 4.
FT   REPEAT      560    589       PC 5.
FT   REPEAT      692    723       PC 6.
FT   REPEAT      742    757       PC 7.
FT   COMPBIAS    623    641       Glu/Lys-rich.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      17     17       Phosphoserine.
FT   MOD_RES      20     20       Phosphothreonine.
FT   MOD_RES      22     22       Phosphoserine.
FT   MOD_RES      90     90       Phosphothreonine (By similarity).
FT   MOD_RES     361    361       Phosphoserine (By similarity).
SQ   SEQUENCE   908 AA;  100203 MW;  1EE5BC93298C2208 CRC64;
     MEEGGRDKTP VQSQQPSATT PSGADEKSSG KERRDAGEKD KEQELSEEDK QLQDELEMLV
     ERLGEKDTSL YRPALEELRR QIRSSTTSMT SVPKPLKFLR PHYGKLKEIY ENMAPGENKC
     FAADIISVLA MTMSGERECL KYRLVGSQEE LASWGHEYVR HLAGEVAKEW QELDDAEKAQ
     REPLLTLVKE IVPYNMAHNA EHEACDLLME IEQVDMLEKD IDENAYAKVC LYLTSCVNYV
     PEPENSALLR CALGVFRKFS RFPEALRLAL MLNDMELVED IFTSCKDVVV QKQMAFMLGR
     HGVFLELSED VEEYEDLTEI MSNVQLNSNF LALARELDIM EPKVPDDIYK THLENNRFGG
     SGSQVDSARM NLASSFVNGF VNAAFGQDKL LTDDGNKWLY KNKDHGMLSA AASLGMILLW
     DVDGGLTQID KYLYSSEDYI KSGALLACGI VNSGVRNECD PALALLSDYV LHNSNTMRLG
     SIFGLGLAYA GSNREDVLTL LLPVMGDSKS SMEVAGVTAL ACGMIAVGSC NGDVTSTILQ
     TIMEKSETEL KDTYARWLPL GLGLNHLGKG EAIEAILAAL EVVSEPFRSF ANTLVDVCAY
     AGSGNVLKVQ QLLHICSEHF DSKEKEEDKD KKEKKDKDKK EAPADMGAHQ GVAVLGIALI
     AMGEEIGAEM ALRTFGHLLR YGEPTLRRAV PLALALISVS NPRLNILDTL SKFSHDADPE
     VSYNSIFAMG MVGSGTNNAR LAAMLRQLAQ YHAKDPNNLF MVRLAQGLTH LGKGTLTLCP
     YHSDRQLMSQ VAVAGLLTVL VSFLDVRNII LGKSHYVLYG LVAAMQPRML VTFDEELRPL
     PVSVRVGQAV DVVGQAGKPK TITGFQTHTT PVLLAHGERA ELATEEFLPV TPILEGFVIL
     RKNPNYDL
//
ID   AT1A1_MOUSE             Reviewed;        1023 AA.
AC   Q8VDN2; Q91Z09;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-1;
DE            Short=Na(+)/K(+) ATPase alpha-1 subunit;
DE            EC=3.6.3.9;
DE   AltName: Full=Sodium pump subunit alpha-1;
DE   Flags: Precursor;
GN   Name=Atp1a1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 55-61; 75-91; 163-173; 178-194; 213-240; 256-264;
RP   360-377; 414-444; 446-458; 477-494; 536-551; 597-605; 613-625;
RP   630-658; 662-683; 699-774 AND 941-950.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15648052; DOI=10.1002/pmic.200401066;
RA   Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA   Hart G.W., Burlingame A.L.;
RT   "Quantitative analysis of both protein expression and serine /
RT   threonine post-translational modifications through stable isotope
RT   labeling with dithiothreitol.";
RL   Proteomics 5:388-398(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-260, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; THR-219; SER-228
RP   AND SER-452, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: This is the catalytic component of the active enzyme,
CC       which catalyzes the hydrolysis of ATP coupled with the exchange of
CC       sodium and potassium ions across the plasma membrane. This action
CC       creates the electrochemical gradient of sodium and potassium ions,
CC       providing the energy for active transport of various nutrients (By
CC       similarity). Melanosome (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + Na(+)(In) + K(+)(Out) = ADP +
CC       phosphate + Na(+)(Out) + K(+)(In).
CC   -!- SUBUNIT: Composed of three subunits: alpha (catalytic), beta and
CC       gamma (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- PTM: Phosphorylation on Tyr-10 modulates pumping activity (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       (TC 3.A.3) family. Type IIC subfamily.
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DR   EMBL; BC010319; AAH10319.1; -; mRNA.
DR   EMBL; BC021496; AAH21496.1; -; mRNA.
DR   EMBL; BC023794; AAH23794.1; -; mRNA.
DR   EMBL; BC025618; AAH25618.1; -; mRNA.
DR   EMBL; BC025627; AAH25627.1; -; mRNA.
DR   EMBL; BC025811; AAH25811.1; -; mRNA.
DR   EMBL; BC032187; AAH32187.1; -; mRNA.
DR   EMBL; BC033435; AAH33435.1; -; mRNA.
DR   EMBL; BC033471; AAH33471.1; -; mRNA.
DR   EMBL; BC042435; AAH42435.1; -; mRNA.
DR   IPI; IPI00311682; -.
DR   RefSeq; NP_659149.1; NM_144900.1.
DR   UniGene; Mm.280103; -.
DR   ProteinModelPortal; Q8VDN2; -.
DR   SMR; Q8VDN2; 26-1023.
DR   DIP; DIP-31885N; -.
DR   MINT; MINT-1797662; -.
DR   STRING; Q8VDN2; -.
DR   PhosphoSite; Q8VDN2; -.
DR   PRIDE; Q8VDN2; -.
DR   Ensembl; ENSMUST00000036493; ENSMUSP00000039657; ENSMUSG00000033161.
DR   GeneID; 11928; -.
DR   KEGG; mmu:11928; -.
DR   UCSC; uc008qrj.1; mouse.
DR   CTD; 11928; -.
DR   MGI; MGI:88105; Atp1a1.
DR   GeneTree; ENSGT00560000076866; -.
DR   HOGENOM; HBG456486; -.
DR   HOVERGEN; HBG004298; -.
DR   InParanoid; Q8VDN2; -.
DR   OMA; SILIHGK; -.
DR   OrthoDB; EOG46MBHS; -.
DR   PhylomeDB; Q8VDN2; -.
DR   BRENDA; 3.6.3.9; 244.
DR   NextBio; 280013; -.
DR   ArrayExpress; Q8VDN2; -.
DR   Bgee; Q8VDN2; -.
DR   CleanEx; MM_ATP1A1; -.
DR   Genevestigator; Q8VDN2; -.
DR   GermOnline; ENSMUSG00000033161; Mus musculus.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; ISS:UniProtKB.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0042383; C:sarcolemma; IDA:MGI.
DR   GO; GO:0003869; F:4-nitrophenylphosphatase activity; IMP:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0005391; F:sodium:potassium-exchanging ATPase activity; IMP:MGI.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   GO; GO:0031947; P:negative regulation of glucocorticoid biosynthetic process; IMP:MGI.
DR   GO; GO:0045822; P:negative regulation of heart contraction; IMP:MGI.
DR   GO; GO:0045823; P:positive regulation of heart contraction; IMP:MGI.
DR   GO; GO:0045989; P:positive regulation of striated muscle contraction; IMP:MGI.
DR   GO; GO:0008217; P:regulation of blood pressure; IGI:MGI.
DR   GO; GO:0002026; P:regulation of the force of heart contraction; IMP:MGI.
DR   GO; GO:0042493; P:response to drug; IMP:MGI.
DR   InterPro; IPR023306; ATPase_cation_domN.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR005775; ATPase_P-typ_cation-ex_asu_euk.
DR   InterPro; IPR006069; ATPase_P-typ_cation-exchng_asu.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023300; ATPase_P-typ_cyto_domA.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Gene3D; G3DSA:2.70.150.10; ATPase_P-typ_cyto_domA; 1.
DR   Gene3D; G3DSA:3.40.1110.10; ATPase_P-typ_cyto_domN; 1.
DR   Gene3D; G3DSA:1.20.1110.10; ATPase_P-typ_TM_dom; 2.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00121; NAKATPASE.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81660; ATPase_cation_domN; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01106; ATPase-IIC_X-K; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 4.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Direct protein sequencing; Hydrolase;
KW   Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Potassium; Potassium transport; Sodium;
KW   Sodium transport; Sodium/potassium transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   PROPEP        1      5       By similarity.
FT                                /FTId=PRO_0000002485.
FT   CHAIN         6   1023       Sodium/potassium-transporting ATPase
FT                                subunit alpha-1.
FT                                /FTId=PRO_0000002486.
FT   TOPO_DOM      6     96       Cytoplasmic (Potential).
FT   TRANSMEM     97    117       Helical; (Potential).
FT   TOPO_DOM    118    129       Extracellular (Potential).
FT   TRANSMEM    130    150       Helical; (Potential).
FT   TOPO_DOM    151    291       Cytoplasmic (Potential).
FT   TRANSMEM    292    312       Helical; (Potential).
FT   TOPO_DOM    313    319       Extracellular (Potential).
FT   TRANSMEM    320    340       Helical; (Potential).
FT   TOPO_DOM    341    789       Cytoplasmic (Potential).
FT   TRANSMEM    790    810       Helical; (Potential).
FT   TOPO_DOM    811    865       Extracellular (Potential).
FT   TRANSMEM    866    886       Helical; (Potential).
FT   TOPO_DOM    887    915       Cytoplasmic (Potential).
FT   TRANSMEM    916    936       Helical; (Potential).
FT   TOPO_DOM    937    952       Extracellular (Potential).
FT   TRANSMEM    953    973       Helical; (Potential).
FT   TOPO_DOM    974    979       Cytoplasmic (Potential).
FT   TRANSMEM    980   1000       Helical; (Potential).
FT   TOPO_DOM   1001   1023       Extracellular (Potential).
FT   REGION       82     84       Phosphoinositide-3 kinase binding (By
FT                                similarity).
FT   ACT_SITE    376    376       4-aspartylphosphate intermediate (By
FT                                similarity).
FT   METAL       717    717       Magnesium (By similarity).
FT   METAL       721    721       Magnesium (By similarity).
FT   MOD_RES      10     10       Phosphotyrosine (By similarity).
FT   MOD_RES      16     16       Phosphoserine.
FT   MOD_RES      47     47       Phosphoserine.
FT   MOD_RES      55     55       Phosphotyrosine (By similarity).
FT   MOD_RES     217    217       Phosphoserine.
FT   MOD_RES     219    219       Phosphothreonine.
FT   MOD_RES     228    228       Phosphoserine.
FT   MOD_RES     260    260       Phosphotyrosine.
FT   MOD_RES     452    452       Phosphoserine.
FT   MOD_RES     943    943       Phosphoserine; by PKA (By similarity).
SQ   SEQUENCE   1023 AA;  112982 MW;  1E806D3FDFC5AD80 CRC64;
     MGKGVGRDKY EPAAVSEHGD KKGKKAKKER DMDELKKEVS MDDHKLSLDE LHRKYGTDLS
     RGLTPARAAE ILARDGPNAL TPPPTTPEWV KFCRQLFGGF SMLLWIGAIL CFLAYGIRSA
     TEEEPPNDDL YLGVVLSAVV IITGCFSYYQ EAKSSKIMES FKNMVPQQAL VIRNGEKMSI
     NAEDVVVGDL VEVKGGDRIP ADLRIISANG CKVDNSSLTG ESEPQTRSPD FTNENPLETR
     NIAFFSTNCV EGTARGIVVY TGDRTVMGRI ATLASGLEGG QTPIAEEIEH FIHLITGVAV
     FLGVSFFILS LILEYTWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN
     LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIHEA DTTENQSGVS FDKTSATWFA
     LSRIAGLCNR AVFQANQENL PILKRAVAGD ASESALLKCI EVCCGSVMEM REKYSKIVEI
     PFNSTNKYQL SIHKNPNASE PKHLLVMKGA PERILDRCSS ILLHGKEQPL DEELKDAFQN
     AYLELGGLGE RVLGFCHLLL PDEQFPEGFQ FDTDDVNFPV DNLCFVGLIS MIDPPRAAVP
     DAVGKCRSAG IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVNQVNPRDA
     KACVVHGSDL KDMTSEELDD ILRYHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN
     DSPALKKADI GVAMGIVGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL
     TSNIPEITPF LIFIIANIPL PLGTVTILCI DLGTDMVPAI SLAYEQAESD IMKRQPRNPK
     TDKLVNERLI SMAYGQIGMI QALGGFFTYF VILAENGFLP FHLLGIRETW DDRWVNDVED
     SYGQQWTYEQ RKIVEFTCHT AFFVSIVVVQ WADLVICKTR RNSVFQQGMK NKILIFGLFE
     ETALAAFLSY CPGMGAALRM YPLKPTWWFC AFPYSLLIFV YDEVRKLIIR RRPGGWVEKE
     TYY
//
ID   CCD92_MOUSE             Reviewed;         314 AA.
AC   Q8VDN4;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Coiled-coil domain-containing protein 92;
GN   Name=Ccdc92; Synonyms=D5Bwg0834e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
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DR   EMBL; AK165371; BAE38150.1; -; mRNA.
DR   EMBL; BC021492; AAH21492.1; -; mRNA.
DR   IPI; IPI00123541; -.
DR   RefSeq; NP_659068.1; NM_144819.2.
DR   UniGene; Mm.389693; -.
DR   ProteinModelPortal; Q8VDN4; -.
DR   PhosphoSite; Q8VDN4; -.
DR   PRIDE; Q8VDN4; -.
DR   Ensembl; ENSMUST00000036206; ENSMUSP00000038075; ENSMUSG00000037979.
DR   GeneID; 215707; -.
DR   KEGG; mmu:215707; -.
DR   UCSC; uc008zqr.1; mouse.
DR   CTD; 215707; -.
DR   MGI; MGI:106485; Ccdc92.
DR   eggNOG; maNOG12076; -.
DR   GeneTree; ENSGT00430000031027; -.
DR   HOGENOM; HBG402829; -.
DR   HOVERGEN; HBG081052; -.
DR   InParanoid; Q8VDN4; -.
DR   OMA; VHLIKER; -.
DR   OrthoDB; EOG4P8FJP; -.
DR   PhylomeDB; Q8VDN4; -.
DR   NextBio; 374811; -.
DR   ArrayExpress; Q8VDN4; -.
DR   Bgee; Q8VDN4; -.
DR   CleanEx; MM_CCDC92; -.
DR   Genevestigator; Q8VDN4; -.
PE   1: Evidence at protein level;
KW   Coiled coil; Phosphoprotein.
FT   CHAIN         1    314       Coiled-coil domain-containing protein 92.
FT                                /FTId=PRO_0000274501.
FT   COILED        1     27       Potential.
FT   COILED       59    113       Potential.
FT   MOD_RES     194    194       Phosphoserine.
SQ   SEQUENCE   314 AA;  35207 MW;  2CE8F50B158A04E5 CRC64;
     MAATNLENQL HSAQKNLLFL QREHASTLKG LHAEIRRLQQ HCTDLTYELT LKSFELTGDS
     SSRTTELKRR CEELEAQLKA KEEENRKLLQ ELEQKNAAIA VLENTVRERE KKYLEELKVK
     SHKLSMLSGE LEQRASTVAY LTSQLHAAKK KLLSSSGTSD ASPAGSPALA SYKPTPPKDK
     LPETPRRRMK KSLSAPLHPE FEEVYRFGAE SRKLLLREPV DAMPDPTPFL LARESAEVQL
     KERPLVIPPI ASDRSATGQH SPARDKPHKT HVGVAHRIHH ATPSQAQPEG EMRAVDQVNA
     SKVVRKHSGT DRTV
//
ID   SIRT2_MOUSE             Reviewed;         389 AA.
AC   Q8VDQ8; Q9CXS5; Q9EQ18; Q9ERJ9;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2003, sequence version 2.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=NAD-dependent deacetylase sirtuin-2;
DE            EC=3.5.1.-;
DE   AltName: Full=SIR2-like protein 2;
DE            Short=mSIR2L2;
GN   Name=Sirt2; Synonyms=Sir2l2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 1), AND SUBCELLULAR LOCATION.
RC   STRAIN=129/Ola;
RX   PubMed=11056054; DOI=10.1006/geno.2000.6360;
RA   Yang Y.H., Chen Y.H., Zhang C.Y., Nimmakayalu M.A., Ward D.C.,
RA   Weissman S.;
RT   "Cloning and characterization of two mouse genes with homology to the
RT   yeast sir2 gene.";
RL   Genomics 69:355-369(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 43-55; 58-69; 79-125; 137-153; 164-174; 213-253;
RP   276-282 AND 348-371, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: NAD-dependent deacetylase, which deacetylates the 'Lys-
CC       40' of alpha-tubulin. Involved in the control of mitotic exit in
CC       the cell cycle, probably via its role in the regulation of
CC       cytoskeleton (By similarity).
CC   -!- CATALYTIC ACTIVITY: NAD(+) + an acetylprotein = nicotinamide + O-
CC       acetyl-ADP-ribose + a protein.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- ENZYME REGULATION: Inhibited by Sirtinol, A3 and M15 small
CC       molecules. Inhibited by nicotinamide (By similarity).
CC   -!- SUBUNIT: Interacts with HDAC6, suggesting that these proteins
CC       belong to a large complex that deacetylate the cytoskeleton (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Colocalizes
CC       with microtubules.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VDQ8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VDQ8-2; Sequence=VSP_008729;
CC   -!- PTM: Phosphorylated at the G2/M transition of the cell cycle (By
CC       similarity).
CC   -!- MISCELLANEOUS: Has some ability to deacetylate histones in vitro,
CC       but seeing its subcellular location, this is unlikely in vivo (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the sirtuin family.
CC   -!- SIMILARITY: Contains 1 deacetylase sirtuin-type domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF299337; AAG39256.1; -; mRNA.
DR   EMBL; AF302272; AAG32038.1; -; Genomic_DNA.
DR   EMBL; AF302265; AAG32038.1; JOINED; Genomic_DNA.
DR   EMBL; AF302266; AAG32038.1; JOINED; Genomic_DNA.
DR   EMBL; AF302267; AAG32038.1; JOINED; Genomic_DNA.
DR   EMBL; AF302268; AAG32038.1; JOINED; Genomic_DNA.
DR   EMBL; AF302269; AAG32038.1; JOINED; Genomic_DNA.
DR   EMBL; AF302270; AAG32038.1; JOINED; Genomic_DNA.
DR   EMBL; AF302271; AAG32038.1; JOINED; Genomic_DNA.
DR   EMBL; AK014042; BAB29128.1; -; mRNA.
DR   EMBL; BC021439; AAH21439.1; -; mRNA.
DR   IPI; IPI00110265; -.
DR   IPI; IPI00473688; -.
DR   RefSeq; NP_001116237.1; NM_001122765.1.
DR   RefSeq; NP_001116238.1; NM_001122766.1.
DR   RefSeq; NP_071877.3; NM_022432.4.
DR   UniGene; Mm.272443; -.
DR   ProteinModelPortal; Q8VDQ8; -.
DR   SMR; Q8VDQ8; 54-356.
DR   STRING; Q8VDQ8; -.
DR   PhosphoSite; Q8VDQ8; -.
DR   PRIDE; Q8VDQ8; -.
DR   Ensembl; ENSMUST00000072965; ENSMUSP00000072732; ENSMUSG00000015149.
DR   GeneID; 64383; -.
DR   KEGG; mmu:64383; -.
DR   NMPDR; fig|10090.3.peg.16053; -.
DR   UCSC; uc009fzt.1; mouse.
DR   UCSC; uc009fzu.1; mouse.
DR   CTD; 64383; -.
DR   MGI; MGI:1927664; Sirt2.
DR   GeneTree; ENSGT00550000074608; -.
DR   HOGENOM; HBG641281; -.
DR   HOVERGEN; HBG057095; -.
DR   InParanoid; Q8VDQ8; -.
DR   OMA; SWMKEKI; -.
DR   OrthoDB; EOG4BVRTZ; -.
DR   PhylomeDB; Q8VDQ8; -.
DR   NextBio; 320059; -.
DR   ArrayExpress; Q8VDQ8; -.
DR   Bgee; Q8VDQ8; -.
DR   Genevestigator; Q8VDQ8; -.
DR   GermOnline; ENSMUSG00000015149; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR   GO; GO:0035035; F:histone acetyltransferase binding; ISS:UniProtKB.
DR   GO; GO:0042826; F:histone deacetylase binding; ISS:UniProtKB.
DR   GO; GO:0017136; F:NAD-dependent histone deacetylase activity; ISS:UniProtKB.
DR   GO; GO:0008134; F:transcription factor binding; ISS:UniProtKB.
DR   GO; GO:0042903; F:tubulin deacetylase activity; ISS:UniProtKB.
DR   GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006342; P:chromatin silencing; IEA:InterPro.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0045843; P:negative regulation of striated muscle tissue development; ISS:UniProtKB.
DR   InterPro; IPR017328; NAD-dep_deAcase_SIR2_euk.
DR   InterPro; IPR003000; NAD-dep_histone_deAcase_SIR2.
DR   PANTHER; PTHR11085; SIR2; 1.
DR   Pfam; PF02146; SIR2; 1.
DR   PIRSF; PIRSF037938; SIR2_euk; 1.
DR   PROSITE; PS50305; SIRTUIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell cycle; Cell division;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; Hydrolase;
KW   Metal-binding; Microtubule; Mitosis; NAD; Phosphoprotein; Zinc.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    389       NAD-dependent deacetylase sirtuin-2.
FT                                /FTId=PRO_0000110259.
FT   DOMAIN       65    340       Deacetylase sirtuin-type.
FT   NP_BIND      84    104       NAD (By similarity).
FT   NP_BIND     167    171       NAD (By similarity).
FT   ACT_SITE    187    187       Proton acceptor (By similarity).
FT   METAL       195    195       Zinc (By similarity).
FT   METAL       200    200       Zinc (By similarity).
FT   METAL       221    221       Zinc (By similarity).
FT   METAL       224    224       Zinc (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      23     23       Phosphoserine.
FT   MOD_RES      25     25       Phosphoserine (By similarity).
FT   MOD_RES     368    368       Phosphoserine (By similarity).
FT   MOD_RES     372    372       Phosphoserine (By similarity).
FT   VAR_SEQ       1     37       Missing (in isoform 2).
FT                                /FTId=VSP_008729.
FT   CONFLICT    230    230       P -> L (in Ref. 1; AAG32038).
FT   CONFLICT    241    241       S -> P (in Ref. 3; AAH21439).
SQ   SEQUENCE   389 AA;  43256 MW;  15F96635445A1BC0 CRC64;
     MAEPDPSDPL ETQAGKVQEA QDSDSDTEGG ATGGEAEMDF LRNLFTQTLG LGSQKERLLD
     ELTLEGVTRY MQSERCRKVI CLVGAGISTS AGIPDFRSPS TGLYANLEKY HLPYPEAIFE
     ISYFKKHPEP FFALAKELYP GQFKPTICHY FIRLLKEKGL LLRCYTQNID TLERVAGLEP
     QDLVEAHGTF YTSHCVNTSC RKEYTMGWMK EKIFSEATPR CEQCQSVVKP DIVFFGENLP
     SRFFSCMQSD FSKVDLLIIM GTSLQVQPFA SLISKAPLAT PRLLINKEKT GQTDPFLGMM
     MGLGGGMDFD SKKAYRDVAW LGDCDQGCLA LADLLGWKKE LEDLVRREHA NIDAQSGSQA
     PNPSTTISPG KSPPPAKEAA RTKEKEEQQ
//
ID   DOCK6_MOUSE             Reviewed;        2080 AA.
AC   Q8VDR9; Q3UM59; Q6PFY0; Q8BJS1; Q9D461;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Dedicator of cytokinesis protein 6;
GN   Name=Dock6; Synonyms=Kiaa1395;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1871-2080 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Aorta, Mammary gland, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 746-2080 (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176; SER-186 AND
RP   SER-878, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Potential guanine nucleotide exchange factor (GEF). GEF
CC       proteins activate some small GTPases by exchanging bound GDP for
CC       free GTP (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8VDR9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VDR9-2; Sequence=VSP_022259, VSP_022260, VSP_022261;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8VDR9-3; Sequence=VSP_022257, VSP_022258;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The DHR-2 domain may mediate some GEF activity (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the DOCK family.
CC   -!- SIMILARITY: Contains 1 DHR-1 (CZH-1) domain.
CC   -!- SIMILARITY: Contains 1 DHR-2 (CZH-2) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH21414.1; Type=Erroneous initiation;
CC       Sequence=BAC37843.1; Type=Frameshift; Positions=160;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK016777; BAB30423.2; -; mRNA.
DR   EMBL; AK080190; BAC37843.1; ALT_FRAME; mRNA.
DR   EMBL; AK145109; BAE26239.1; -; mRNA.
DR   EMBL; BC021414; AAH21414.1; ALT_INIT; mRNA.
DR   EMBL; BC043042; AAH43042.1; -; mRNA.
DR   EMBL; BC057368; AAH57368.2; -; mRNA.
DR   IPI; IPI00222462; -.
DR   IPI; IPI00816918; -.
DR   IPI; IPI00875148; -.
DR   RefSeq; NP_796004.2; NM_177030.3.
DR   UniGene; Mm.128153; -.
DR   ProteinModelPortal; Q8VDR9; -.
DR   SMR; Q8VDR9; 1624-2055.
DR   STRING; Q8VDR9; -.
DR   PhosphoSite; Q8VDR9; -.
DR   PRIDE; Q8VDR9; -.
DR   Ensembl; ENSMUST00000034728; ENSMUSP00000034728; ENSMUSG00000032198.
DR   Ensembl; ENSMUST00000049745; ENSMUSP00000055725; ENSMUSG00000032198.
DR   Ensembl; ENSMUST00000086329; ENSMUSP00000083511; ENSMUSG00000032198.
DR   GeneID; 319899; -.
DR   KEGG; mmu:319899; -.
DR   UCSC; uc009omo.1; mouse.
DR   UCSC; uc009omq.1; mouse.
DR   UCSC; uc009omt.1; mouse.
DR   CTD; 319899; -.
DR   MGI; MGI:1914789; Dock6.
DR   GeneTree; ENSGT00560000076710; -.
DR   HOVERGEN; HBG051390; -.
DR   OrthoDB; EOG4Q2DDM; -.
DR   NextBio; 395613; -.
DR   ArrayExpress; Q8VDR9; -.
DR   Bgee; Q8VDR9; -.
DR   CleanEx; MM_DOCK6; -.
DR   Genevestigator; Q8VDR9; -.
DR   GermOnline; ENSMUSG00000032198; Mus musculus.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0051020; F:GTPase binding; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR010703; DOCK.
DR   InterPro; IPR021816; DUF3398.
DR   Pfam; PF06920; Ded_cyto; 1.
DR   Pfam; PF11878; DUF3398; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Guanine-nucleotide releasing factor;
KW   Phosphoprotein.
FT   CHAIN         1   2080       Dedicator of cytokinesis protein 6.
FT                                /FTId=PRO_0000189994.
FT   DOMAIN      546    784       DHR-1.
FT   DOMAIN     1522   2045       DHR-2.
FT   MOD_RES      40     40       Phosphoserine (By similarity).
FT   MOD_RES     176    176       Phosphoserine.
FT   MOD_RES     186    186       Phosphoserine.
FT   MOD_RES     878    878       Phosphoserine.
FT   MOD_RES    1270   1270       Phosphothreonine (By similarity).
FT   VAR_SEQ     241    244       DEAV -> VGAY (in isoform 3).
FT                                /FTId=VSP_022257.
FT   VAR_SEQ     245   2080       Missing (in isoform 3).
FT                                /FTId=VSP_022258.
FT   VAR_SEQ     905    939       Missing (in isoform 2).
FT                                /FTId=VSP_022259.
FT   VAR_SEQ    1019   1062       DMKLAERLNASLAFFLSDLLSIADRGYIFSLVRAHYKQVAT
FT                                RLQ -> VRKDSAQGCSVVRDPVCHVGLFIHGLFLEHLWFT
FT                                WPWLDVETQL (in isoform 2).
FT                                /FTId=VSP_022260.
FT   VAR_SEQ    1063   2080       Missing (in isoform 2).
FT                                /FTId=VSP_022261.
FT   CONFLICT    145    145       R -> W (in Ref. 1; BAC37843).
SQ   SEQUENCE   2080 AA;  233237 MW;  BD479C142A92BB76 CRC64;
     MAASERRAFA HKINRTVAAE VRKQVSRERS GSPHSSRRSS SSLGVPLTEV IEPLDFEDVL
     LSRPPEVEPG PLRDLIEFPV DDLELLKQPR ECRTTESGVP EDGQLDAQVR AAVEMYSEDW
     VIVRRRYQHL STAYSPITTE TQRERQKGLT CQVFEQDTPG DERTGPEDVD DPQHCSGSPE
     DTPRSSGASG IFSLRNLAAD SLLPTLLEQA APEDVDRRNE ALRRQHRAPT LLTLYPAPDE
     DEAVERCSRP EPPREHFGQR ILVKCLSLKF EIEIEPIFGT LALYDVREKK KISENFYFDL
     NSDSVKGLLR AHGTHPAIST LARSAIFSVT YPSPDIFLVV KLEKVLQQGD ISECCEPYMV
     MKEADTAKNK EKLEKLRLAA EQFCTRLGRY RMPFAWTAVH LANIVSRPQD RDSDSEGERR
     PTWAERRRRG PQDRGYSGDD ACSFSSFRPA TLTVTNFFKQ EAERLSDEDL FKFLADMRRP
     SSLLRRLRPV TAQLKLDISP APENLHFCLS PDLLHVKPYP DPRGRPTKEI LEFPAREVYA
     PHSCYRNLLF VYPHSLNFSS RQGSVRNLAV RIQYMAGEDQ SQALPVIFGK SSCSEFTREA
     FTPVVYHNKS PEFYEEFKLR LPACVTENHH LFFTFYHVSC QPRPGTALET PVGFTWIPLL
     QHGRLRTGPF CLPVSVDQPP PSYSVLTPDV ALPGMRWVDG HKGVFSVELT AVSSVHPQDP
     HLDKFFTLVH VLEEGIFPFR LKETVLSEGT MEQELRASLA ALRLASPEPL VAFSHLVLDK
     LVRLVVRPPI ICGQMVNLGR GAFEAMAHVA SLVHRNLEAV QDSRGHCPLL ASYVHYAFRL
     PGGDLSLPGE APPATVQAAT LARGSGRPAS LYLARSKSIS SSNPDLAVVP GSVDDEVSRI
     LASKGVDRSH SWVNSAYAPG GSKAVLRRVP PYCGADPRQL LHEELALQWV VSGSAVRELV
     LQHAWFFFQL MVKSMELHLL LGQRLDTPRK LRFPGRFLDD IAALVASVGL EVITRVHKDM
     KLAERLNASL AFFLSDLLSI ADRGYIFSLV RAHYKQVATR LQSAPNPTAL LTLRMDFTRI
     LCSHEHYVTL NLPCCPLSPP ASPSPSVSST TSQSSTFSSQ APDPKVTSMF ELSGPFRQQH
     FLSGLLLTEL ALALDPEAEG ASLLHKKAIS AVHSLLCSHD VDSRYAEATV KAKVAELYLP
     LLSLARDTLP QLHGFAEGSG QRSRLASMLD SDTEGEGDIG STINPSVAMA IAGGPLAPGS
     RTSISQGPST AARSGCPLSA ESSRTLLVCV LWVLKNAEPT LLQRWAADLA LPQLGRLLDL
     LYLCLAAFEY KGKKAFERIN SLTFKKSLDM KARLEEAILG TIGARQEMVR RSRERSPFGN
     QENVRWRKSA THWRQTSDRV DKTKDEMEHE ALVDGNLATE ASLVVLDTLE TIVQTVMLSE
     ARESILSAVL KVVLYSLGSA QSALFLQHGL ATQRALVSKF PELLFEEDTE LCADLCLRLL
     RHCGSRISTI RMHASASLYL LMRQNFEIGH NFARVKMLVT MSLSSLVGTT QNFSEEHLRK
     SLKTILTYAE EDIGLRDSTF AEQVQDLMFN LHMILTDTVK MKEHQEDPEM LMDLMYRIAR
     GYQGSPDLRL TWLQNMAGKH AELGNHAEAA QCMVHAAALV AEYLALLEDS RHLPVGCVSF
     QNVSSNVLEE SAISDDILSP DEEGFCSGKN FTELGLVGLL EQAAGYFTMG GLYEAVNEVY
     KNLIPILEAH RDYKKLAAVH GKLQEAFTKI MHQSSGWERV FGTYFRVGFY GTRFGDLDEQ
     EFVYKEPSIT KLAEISHRLE EFYTERFGDD VVEIIKDSNP VDKSKLDPQK AYIQITYVEP
     HFDTYELKDR VTYFDRNYGL RAFLFCTPFT PDGRAHGELA EQHKRKTLLS TEHAFPYIKT
     RIRVCHREET VLTPVEVAIE DMQKKTRELA FATEQDPPDA KMLQMVLQGS VGPTVNQGPL
     EVAQVFLSEI PEDPKLFRHH NKLRLCFKDF CKKCEDALRK NKALIGPDQK EYHRELERHY
     SRLREALQPL LTQRLPQLLA PSSTSLRSSM NRSSFRKADL
//
ID   SNRK_MOUSE              Reviewed;         748 AA.
AC   Q8VDU5; Q91WX6;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=SNF-related serine/threonine-protein kinase;
DE            EC=2.7.11.1;
DE   AltName: Full=SNF1-related kinase;
GN   Name=Snrk;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=BALB/c; TISSUE=Yolk sac;
RX   MEDLINE=22220112; PubMed=12234663; DOI=10.1016/S0378-1119(02)00829-6;
RA   Kertesz N., Samson J., Debacker C., Wu H., Labastie M.-C.;
RT   "Cloning and characterization of human and mouse SNRK sucrose non-
RT   fermenting protein (SNF-1)-related kinases.";
RL   Gene 294:13-24(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May play a role in hematopoietic cell proliferation or
CC       differentiation. Potential mediator of neuronal apoptosis (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activated by phosphorylation on Thr-173 by
CC       STK11 in complex with STE20-related adapter-alpha (STRAD alpha)
CC       pseudo kinase and CAB39 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed in all tissues
CC       examined.
CC   -!- DEVELOPMENTAL STAGE: Expressed from day 8 dpc along the epithelium
CC       of the differentiating neural tube. Expression persists along the
CC       dorsal axis until 12.5 dpc, but becomes progressively restricted
CC       to the more caudal part of the neural tube with much stronger
CC       intensity in the caudal neuropore. Also observed in the endoderm
CC       of the primitive gut between 8.5 and 11.5 dpc, at 10.5 dpc, in the
CC       endocardium and pericardium of the developing heart, and in both
CC       the endothelium and blood cells clustered at the ventral part of
CC       the dorsal aorta. Later in development (12.5 dpc), expressed in
CC       the endocardium and the interventricular septum of the heart.
CC   -!- PTM: Autophosphorylated (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 UBA domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF387809; AAK97440.1; -; mRNA.
DR   EMBL; BC020189; AAH20189.1; -; mRNA.
DR   EMBL; BC094658; AAH94658.1; -; mRNA.
DR   IPI; IPI00346390; -.
DR   RefSeq; NP_001158044.1; NM_001164572.1.
DR   RefSeq; NP_598502.2; NM_133741.2.
DR   UniGene; Mm.257989; -.
DR   UniGene; Mm.441420; -.
DR   ProteinModelPortal; Q8VDU5; -.
DR   SMR; Q8VDU5; 9-333.
DR   PhosphoSite; Q8VDU5; -.
DR   PRIDE; Q8VDU5; -.
DR   Ensembl; ENSMUST00000056150; ENSMUSP00000056389; ENSMUSG00000038145.
DR   Ensembl; ENSMUST00000118886; ENSMUSP00000114132; ENSMUSG00000038145.
DR   Ensembl; ENSMUST00000120173; ENSMUSP00000112919; ENSMUSG00000038145.
DR   GeneID; 20623; -.
DR   KEGG; mmu:20623; -.
DR   UCSC; uc009sen.1; mouse.
DR   CTD; 20623; -.
DR   MGI; MGI:108104; Snrk.
DR   GeneTree; ENSGT00600000084268; -.
DR   HOGENOM; HBG714941; -.
DR   HOVERGEN; HBG093970; -.
DR   InParanoid; Q8VDU5; -.
DR   OMA; TYSWHRR; -.
DR   OrthoDB; EOG4GB75K; -.
DR   PhylomeDB; Q8VDU5; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 299019; -.
DR   ArrayExpress; Q8VDU5; -.
DR   Bgee; Q8VDU5; -.
DR   CleanEx; MM_SNRK; -.
DR   Genevestigator; Q8VDU5; -.
DR   GermOnline; ENSMUSG00000038145; Mus musculus.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    748       SNF-related serine/threonine-protein
FT                                kinase.
FT                                /FTId=PRO_0000225606.
FT   DOMAIN       16    269       Protein kinase.
FT   DOMAIN      291    334       UBA.
FT   NP_BIND      22     30       ATP (By similarity).
FT   ACT_SITE    139    139       Proton acceptor (By similarity).
FT   BINDING      45     45       ATP (By similarity).
FT   MOD_RES      11     11       N6-acetyllysine (By similarity).
FT   MOD_RES     173    173       Phosphothreonine (By similarity).
FT   MOD_RES     390    390       Phosphoserine (By similarity).
FT   MOD_RES     569    569       Phosphoserine.
FT   MOD_RES     606    606       Phosphoserine (By similarity).
FT   CONFLICT      5      5       K -> R (in Ref. 1; AAK97440).
FT   CONFLICT    112    112       N -> D (in Ref. 1; AAK97440).
FT   CONFLICT    549    549       E -> K (in Ref. 1; AAK97440).
SQ   SEQUENCE   748 AA;  81913 MW;  9E3F7EA90136FCDA CRC64;
     MAGFKRGYDG KIAGLYDLDK TLGRGHFAVV KLARHVFTGE KVAVKVIDKT KLDTLATGHL
     FQEVRCMKLV QHPNIVRLYE VIDTQTKLYL ILELGDGGDM FDYIMKHEEG LNEDLAKKYF
     AQIVHAISYC HKLHVVHRDL KPENVVFFEK QGLVKLTDFG FSNKFQPGKK LTTSCGSLAY
     SAPEILLGDE YDAPAVDIWS LGVILFMLVC GQPPFQEAND SETLTMIMDC KYTVPPRVSA
     GCRDLITRML QRDPKRRASL EEIESHPWLQ GVDPSPATKY NIPLVSYKNL SEEEHNSIIQ
     RMVLGDIADR DAIVEALETN RYNHITATYF LLAERILREK QEKEIQTRSA SPSNIKAQFR
     QSWPTKIDVP QDLEDDLTAT PLSHATVPQS PARAGDNVLN GHRSKGLCDP AKKDELPELA
     GPALSTVPPA SMKPAASGRK CLFRVEEDEE EDEEDKKPVS LSTQVVLRRK PSVTNRLTSR
     KSAPVLNQIF EEGESDDEFD MDENLPPKLS RLKMNIASPG TVHKRYHRRK SQGRGSSCSS
     SETSDDDSES RRRLDKDSGF AYSWHRRDSS EGPPGSEGDG GGQSKPSSGG GVDKASPGEQ
     GTGGGSQGGS GGTPSGTAGS SRRCAGPDSS SPSPASASAA PRGAELVQSL KLVSLCLGSQ
     LHGAKYILDP QKALFSSVKV QEKSTWKMCI SAPGPSPSAD LDPVRTKKLR NNALQLPLCE
     KTISVNIQRS RKEGLLCASS PASCCHVI
//
ID   R3GEF_MOUSE             Reviewed;         383 AA.
AC   Q8VDV3; Q3TTM0;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-FEB-2011, entry version 54.
DE   RecName: Full=Guanine nucleotide exchange factor for Rab-3A;
DE   AltName: Full=Rab-3A-interacting-like protein 1;
DE            Short=Rab3A-interacting-like protein 1;
DE   AltName: Full=Rabin3-like 1;
GN   Name=Rab3il1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Guanine nucleotide exchange factor (GEF) for Rab3A, a
CC       GTPase that regulates synaptic vesicle exocytosis (By similarity).
CC   -!- SUBUNIT: Interacts with Rab3A and IHPK1 through the coiled coil
CC       domain. This interaction is competitive. IHPK1 kinase activity is
CC       not required for this interaction (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VDV3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VDV3-2; Sequence=VSP_028346;
CC   -!- SIMILARITY: Belongs to the SEC2 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK132764; BAE21345.1; -; mRNA.
DR   EMBL; AK161298; BAE36305.1; -; mRNA.
DR   EMBL; BC020147; AAH20147.1; -; mRNA.
DR   IPI; IPI00311851; -.
DR   IPI; IPI00867851; -.
DR   RefSeq; NP_653121.1; NM_144538.2.
DR   UniGene; Mm.281969; -.
DR   ProteinModelPortal; Q8VDV3; -.
DR   SMR; Q8VDV3; 76-166.
DR   PhosphoSite; Q8VDV3; -.
DR   PRIDE; Q8VDV3; -.
DR   Ensembl; ENSMUST00000025565; ENSMUSP00000025565; ENSMUSG00000024663.
DR   Ensembl; ENSMUST00000113161; ENSMUSP00000108786; ENSMUSG00000024663.
DR   GeneID; 74760; -.
DR   KEGG; mmu:74760; -.
DR   NMPDR; fig|10090.3.peg.4647; -.
DR   UCSC; uc008gow.1; mouse.
DR   CTD; 74760; -.
DR   MGI; MGI:1922010; Rab3il1.
DR   eggNOG; roNOG10287; -.
DR   GeneTree; ENSGT00390000009036; -.
DR   HOGENOM; HBG315948; -.
DR   HOVERGEN; HBG057034; -.
DR   InParanoid; Q8VDV3; -.
DR   OMA; VCPAAGH; -.
DR   PhylomeDB; Q8VDV3; -.
DR   NextBio; 341572; -.
DR   ArrayExpress; Q8VDV3; -.
DR   Bgee; Q8VDV3; -.
DR   CleanEx; MM_RAB3IL1; -.
DR   Genevestigator; Q8VDV3; -.
DR   InterPro; IPR009449; Sec2p.
DR   Pfam; PF06428; Sec2p; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil;
KW   Guanine-nucleotide releasing factor.
FT   CHAIN         1    383       Guanine nucleotide exchange factor for
FT                                Rab-3A.
FT                                /FTId=PRO_0000305296.
FT   COILED       77    128       Potential.
FT   VAR_SEQ       1     69       Missing (in isoform 2).
FT                                /FTId=VSP_028346.
SQ   SEQUENCE   383 AA;  42713 MW;  30B2F1C12495BF82 CRC64;
     MWSGQPQQDE GLPVGLSAIP VPWKNLGPSK SNRESSGGLV EASTSWEEAQ GEEHPAPAPL
     DVSRLRSSSM EIREKGSEFL KEELYKAQKE LKLKDEECER LCKVRAQLEQ ELEELTASLF
     EEAHKMVREA NMKQATSEKQ LKEAWGKIDM LQAEVTALKT LVITSTPASP NRELHPQLLS
     PTKAGPRKGH SRQKSTSSSL CPVVCPTAGH IPTPDKEGKE VDTTLFAEFQ AWRASPTLDK
     SCPFLERVYR EDVGPCLDFT VQELSALVRT AVEDNTLTIE PVASQTLPAV KVPTVECNNT
     NTCALSGLAR TCHHRIRLGD SDSHYYISPS SRARITAVCN FFTYIRYIQQ GLVRQDAEPM
     FWEIMRLRKG MSLAKLGFFP QEA
//
ID   CI082_MOUSE             Reviewed;         356 AA.
AC   Q8VDY9;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 46.
DE   RecName: Full=Uncharacterized protein C9orf82 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
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DR   EMBL; BC020067; AAH20067.1; -; mRNA.
DR   IPI; IPI00165832; -.
DR   UniGene; Mm.35170; -.
DR   PhosphoSite; Q8VDY9; -.
DR   PRIDE; Q8VDY9; -.
DR   Ensembl; ENSMUST00000030313; ENSMUSP00000030313; ENSMUSG00000028578.
DR   UCSC; uc008tsa.1; mouse.
DR   MGI; MGI:1915020; 5830433M19Rik.
DR   GeneTree; ENSGT00390000017010; -.
DR   HOGENOM; HBG445814; -.
DR   HOVERGEN; HBG054538; -.
DR   InParanoid; Q8VDY9; -.
DR   OrthoDB; EOG4X6C9Q; -.
DR   NextBio; 325517; -.
DR   ArrayExpress; Q8VDY9; -.
DR   Bgee; Q8VDY9; -.
DR   CleanEx; MM_5830433M19RIK; -.
DR   Genevestigator; Q8VDY9; -.
DR   GermOnline; ENSMUSG00000028578; Mus musculus.
PE   1: Evidence at protein level;
KW   Coiled coil; Phosphoprotein.
FT   CHAIN         1    356       Uncharacterized protein C9orf82 homolog.
FT                                /FTId=PRO_0000089718.
FT   COILED      276    306       Potential.
FT   COMPBIAS     19     25       Poly-Ala.
FT   COMPBIAS     71     78       Poly-Ser.
FT   MOD_RES      69     69       Phosphothreonine (By similarity).
FT   MOD_RES      72     72       Phosphoserine (By similarity).
FT   MOD_RES      74     74       Phosphoserine (By similarity).
FT   MOD_RES     183    183       Phosphoserine (By similarity).
FT   MOD_RES     201    201       Phosphoserine (By similarity).
FT   MOD_RES     307    307       Phosphoserine.
SQ   SEQUENCE   356 AA;  37823 MW;  55F23EC665D54C56 CRC64;
     MTGKKSSREK RRKRSGQEAA AALAAPDLVP VLSGSAGGCG SGGCCGVAGG GTSVAGGAER
     SERRKRRSTD SSSSVSGSLQ QETKYLLPSL EKELFLAEHS DLEEGGLDLN VSLKPVSFYI
     SDKKEMLQQC FCIIGEKKLQ KMLPDVLKNC SVEEIKKLCQ EQLELLSEKQ ILKILEGDNG
     LDSDMEEEAD DGCKVAPDLI SQQDTCVDST SSLRENKQPE GLESKQGKGE DSDVLSINAD
     AYDSDIEGPS IDEAAAAATT TPAATAVATA ASEVPENTVQ SEAGQIDDLE RDIEKSVNEI
     LGLAESSPKE PKVATLTVPP PEDVQPSAQQ LELLELEMRA RAIKALMKAG DIKKPV
//
ID   ZDHC5_MOUSE             Reviewed;         715 AA.
AC   Q8VDZ4; Q69ZB5; Q8R2X7;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Probable palmitoyltransferase ZDHHC5;
DE            EC=2.3.1.-;
DE   AltName: Full=Zinc finger DHHC domain-containing protein 5;
DE            Short=DHHC-5;
GN   Name=Zdhhc5; Synonyms=Kiaa1748;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II, and FVB/10; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-91, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247 AND SER-694, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-299; SER-345
RP   AND THR-385, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-380 AND SER-432, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-299; SER-380;
RP   SER-529 AND SER-621, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- CATALYTIC ACTIVITY: Palmitoyl-CoA + protein-cysteine = S-palmitoyl
CC       protein + CoA.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VDZ4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VDZ4-2; Sequence=VSP_006936, VSP_006937;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase
CC       activity (By similarity).
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       ERF2/ZDHHC9 subfamily.
CC   -!- SIMILARITY: Contains 1 DHHC-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32529.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK082513; BAC38513.1; -; mRNA.
DR   EMBL; AK075641; BAC35875.1; -; mRNA.
DR   EMBL; AK173251; BAD32529.1; ALT_INIT; mRNA.
DR   EMBL; BC020051; AAH20051.1; -; mRNA.
DR   EMBL; BC027047; AAH27047.1; -; mRNA.
DR   EMBL; BC065155; AAH65155.1; -; mRNA.
DR   IPI; IPI00124064; -.
DR   IPI; IPI00467627; -.
DR   RefSeq; NP_659136.1; NM_144887.4.
DR   UniGene; Mm.288508; -.
DR   PhosphoSite; Q8VDZ4; -.
DR   PRIDE; Q8VDZ4; -.
DR   Ensembl; ENSMUST00000035840; ENSMUSP00000048198; ENSMUSG00000034075.
DR   Ensembl; ENSMUST00000111645; ENSMUSP00000107272; ENSMUSG00000034075.
DR   GeneID; 228136; -.
DR   KEGG; mmu:228136; -.
DR   UCSC; uc008kiz.1; mouse.
DR   CTD; 228136; -.
DR   MGI; MGI:1923573; Zdhhc5.
DR   GeneTree; ENSGT00550000074293; -.
DR   HOGENOM; HBG443552; -.
DR   HOVERGEN; HBG057186; -.
DR   InParanoid; Q8VDZ4; -.
DR   OMA; SRHIVAS; -.
DR   OrthoDB; EOG40S0FK; -.
DR   PhylomeDB; Q8VDZ4; -.
DR   NextBio; 378935; -.
DR   ArrayExpress; Q8VDZ4; -.
DR   Bgee; Q8VDZ4; -.
DR   CleanEx; MM_ZDHHC5; -.
DR   Genevestigator; Q8VDZ4; -.
DR   GermOnline; ENSMUSG00000034075; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008415; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001594; Znf_DHHC_palmitoyltrfase.
DR   Pfam; PF01529; zf-DHHC; 1.
DR   PROSITE; PS50216; ZF_DHHC; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Alternative splicing; Membrane; Metal-binding;
KW   Phosphoprotein; Transferase; Transmembrane; Transmembrane helix; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    715       Probable palmitoyltransferase ZDHHC5.
FT                                /FTId=PRO_0000212869.
FT   TRANSMEM     14     34       Helical; (Potential).
FT   TRANSMEM     53     73       Helical; (Potential).
FT   TRANSMEM    149    169       Helical; (Potential).
FT   TRANSMEM    192    212       Helical; (Potential).
FT   ZN_FING     104    154       DHHC-type.
FT   ACT_SITE    134    134       S-palmitoyl cysteine intermediate (By
FT                                similarity).
FT   MOD_RES      91     91       Phosphotyrosine.
FT   MOD_RES     247    247       Phosphoserine.
FT   MOD_RES     296    296       Phosphoserine.
FT   MOD_RES     299    299       Phosphoserine.
FT   MOD_RES     345    345       Phosphoserine.
FT   MOD_RES     348    348       Phosphothreonine (By similarity).
FT   MOD_RES     350    350       Phosphothreonine (By similarity).
FT   MOD_RES     380    380       Phosphoserine.
FT   MOD_RES     385    385       Phosphothreonine.
FT   MOD_RES     409    409       Phosphoserine (By similarity).
FT   MOD_RES     422    422       Phosphoserine (By similarity).
FT   MOD_RES     423    423       Phosphoserine (By similarity).
FT   MOD_RES     425    425       Phosphoserine (By similarity).
FT   MOD_RES     429    429       Phosphoserine (By similarity).
FT   MOD_RES     432    432       Phosphoserine.
FT   MOD_RES     436    436       Phosphothreonine (By similarity).
FT   MOD_RES     529    529       Phosphoserine.
FT   MOD_RES     554    554       Phosphoserine (By similarity).
FT   MOD_RES     621    621       Phosphoserine.
FT   MOD_RES     630    630       Phosphotyrosine (By similarity).
FT   MOD_RES     659    659       Phosphothreonine (By similarity).
FT   MOD_RES     679    679       Phosphoserine (By similarity).
FT   MOD_RES     684    684       Phosphoserine (By similarity).
FT   MOD_RES     694    694       Phosphoserine.
FT   MOD_RES     696    696       Phosphothreonine (By similarity).
FT   MOD_RES     704    704       Phosphoserine (By similarity).
FT   VAR_SEQ     641    652       KAPSGVSETEEV -> NPHLVSQRQRK (in isoform
FT                                2).
FT                                /FTId=VSP_006936.
FT   VAR_SEQ     653    715       Missing (in isoform 2).
FT                                /FTId=VSP_006937.
SQ   SEQUENCE   715 AA;  77501 MW;  6FD8E83FA3D3F961 CRC64;
     MPAESGKRFK PSKYVPVSAA AIFLVGATTL FFAFTCPGLS LNVSPAVPIY NAIMFLFVLA
     NFSMATFMDP GIFPRAEEDE DKEDDFRAPL YKTVEIKGIQ VRMKWCATCR FYRPPRCSHC
     SVCDNCVEEF DHHCPWVNNC IGRRNYRYFF LFLLSLTAHI MGVFGFGLLY VLYHIEELSG
     VRTAVTMAVM CVAGLFFIPV AGLTGFHVVL VARGRTTNEQ VTGKFRGGVN PFTNGCCNNV
     SRVLCSSPAP RYLGRPKKEK TIVIRPPFLR PEVSDGQITV KIMDNGIQGE LRRTKSKGSL
     EITESQSADA EPPPPPKPDL SRYTGLRTHL SLATNEDSSL LGKDSPPTPT MYKYRPGYSS
     SSTSAAMPHS SSAKLSRGDS LKEPTSIADS SRHPSYRSEP SLEPESFRSP TFGKSFHFDP
     LSSGSRSSSL KSAQGTGFEL GQLQSIRSEG TTSTSYKSLA NQTRNGSLSY DSLLTPSDSP
     DFESVQAGPE PDPPLGYTSP FLSARLAQQR EAERHPRLLP TGPPHREPSP VRYDNLSRHI
     VASLQEREKL LRQSPPLAGR EEEPGLGDSG IQSTPGSGHA PRTSSSSDDS KRSPLSKTPL
     GRPAVPRFGK PDGLRSRGLG SPEPGTTAPY LGRSISYSSQ KAPSGVSETE EVALQPLLTP
     KDEVQLKTTY SKSNGQPKSI GSASPGPGQP PLSSPTRGGV KKVSGVGGTT YEISV
//
ID   MIO_MOUSE               Reviewed;         875 AA.
AC   Q8VE19;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=WD repeat-containing protein mio;
GN   Name=Mios;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the WD repeat mio family.
CC   -!- SIMILARITY: Contains 7 WD repeats.
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DR   EMBL; BC020002; AAH20002.1; -; mRNA.
DR   IPI; IPI00311785; -.
DR   UniGene; Mm.257151; -.
DR   ProteinModelPortal; Q8VE19; -.
DR   SMR; Q8VE19; 112-150, 260-298.
DR   PhosphoSite; Q8VE19; -.
DR   PRIDE; Q8VE19; -.
DR   Ensembl; ENSMUST00000040017; ENSMUSP00000039301; ENSMUSG00000042447.
DR   UCSC; uc009axk.1; mouse.
DR   MGI; MGI:2182066; Mios.
DR   GeneTree; ENSGT00390000015038; -.
DR   HOGENOM; HBG314438; -.
DR   HOVERGEN; HBG108136; -.
DR   InParanoid; Q8VE19; -.
DR   OrthoDB; EOG4ZKJKJ; -.
DR   NextBio; 387375; -.
DR   ArrayExpress; Q8VE19; -.
DR   Bgee; Q8VE19; -.
DR   Genevestigator; Q8VE19; -.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   SMART; SM00320; WD40; 4.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR   PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Repeat; WD repeat.
FT   CHAIN         1    875       WD repeat-containing protein mio.
FT                                /FTId=PRO_0000329405.
FT   REPEAT       58    100       WD 1.
FT   REPEAT      111    155       WD 2.
FT   REPEAT      182    221       WD 3.
FT   REPEAT      223    261       WD 4.
FT   REPEAT      265    306       WD 5.
FT   REPEAT      320    360       WD 6.
FT   REPEAT      395    437       WD 7.
FT   MOD_RES     766    766       Phosphoserine (By similarity).
SQ   SEQUENCE   875 AA;  98323 MW;  1A5C40C907F7533B CRC64;
     MSGTKPDILW APHQVDRFVV CDSELSLYHV ESAVNSELKA GSLRLSEDSA ATLLSINSDT
     PYMKCVAWYL NYDPECLLAV GQANGRVVLT SLGQDHNSKF KDLIGKEFVP KHARQCNTLA
     WNPLDSNWLA AGLDKHRADF SVLIWDICSK YTPDIVPMEK VRLSAGEAET TLLVTKPLYE
     LGQNDASLSL CWLPRDQKLL LAGMHRNLAI FDLRNTSQKM FVNTKAVQGV TVDPYFHDRV
     ASFYEGQVAI WDLRKFEKPV LTLTEQPKPL TKVAWCPTRT GLLATLTRDS NIIRLYDMQH
     TPTPIGDETE PTIIERSVQP CDNYIASFAW HPTSQNRMIV STPNRTMSDF TVFERISLAW
     SPITSLMWAC GRHLYECAEE ESDNSLEKDI ATKMRLRALS RYGLDTEQVW RNHILAGNED
     PQLKSLWYTL HFMKQYTEDN DQKSPGNKGS LVYAGIKSIV KSSLGMVESS RHNWSGLDKQ
     TDIQNLNEER ILALQLCGWI KKGTDVDVGP FLNSLVQEGE WERAAAVALF NLDIRRAIQI
     LNEGASSEKG DLNLNVVAMA LSGYTDEKNS LWREMCSTLR LQLNNPYLCV MFAFLTSEAG
     AYDGVLYENK VAVRDRVAFA CKFLGDAQLN KYIEKLTNEM KEAGNLEGIL LTGLTKDGVD
     LMESYVDRTG DVQTASYCML QGSPLDVLKD ERVQYWIENY RNLLDAWRFW HKRAEFDIHR
     SKLDPSSKPL AQVFVSCNFC GKSISYSCSS VPHQGRGFSQ YGVSGSPTKS KVTSCPGCRK
     PLPRCALCLI NMGTPVSSCP GGSKSDEKVD LSKDKKLAQF NNWFTWCHNC RHGGHAGHML
     SWFRDHAECP VSACTCKCMQ LDTTGNLVPA ETVQP
//
ID   GD1L1_MOUSE             Reviewed;         370 AA.
AC   Q8VE33; A2A5I0;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Ganglioside-induced differentiation-associated protein 1-like 1;
DE            Short=GDAP1-L1;
GN   Name=Gdap1l1; Synonyms=Gdap1l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the GST superfamily.
CC   -!- SIMILARITY: Contains 1 GST C-terminal domain.
CC   -!- SIMILARITY: Contains 1 GST N-terminal domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AL591488; CAM22394.1; -; Genomic_DNA.
DR   EMBL; BC019941; AAH19941.1; -; mRNA.
DR   IPI; IPI00123756; -.
DR   UniGene; Mm.102080; -.
DR   ProteinModelPortal; Q8VE33; -.
DR   PRIDE; Q8VE33; -.
DR   Ensembl; ENSMUST00000109421; ENSMUSP00000105048; ENSMUSG00000017943.
DR   MGI; MGI:2385163; Gdap1l1.
DR   GeneTree; ENSGT00510000046788; -.
DR   HOGENOM; HBG445548; -.
DR   HOVERGEN; HBG051717; -.
DR   InParanoid; Q8VE33; -.
DR   OMA; RLVLYHW; -.
DR   OrthoDB; EOG4G7BZN; -.
DR   ArrayExpress; Q8VE33; -.
DR   Bgee; Q8VE33; -.
DR   Genevestigator; Q8VE33; -.
DR   GermOnline; ENSMUSG00000017943; Mus musculus.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR017933; Glutathione_S_Trfase/Cl_chnl_C.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:1.20.1050.10; GST_C_like; 1.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   SUPFAM; SSF47616; GST_C_like; 1.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil.
FT   CHAIN         1    370       Ganglioside-induced differentiation-
FT                                associated protein 1-like 1.
FT                                /FTId=PRO_0000186041.
FT   DOMAIN       45    129       GST N-terminal.
FT   DOMAIN      177    344       GST C-terminal.
SQ   SEQUENCE   370 AA;  42318 MW;  7ACDD616D8A9D399 CRC64;
     MATPNNLTPT NCSWWPISAL ESDAAKPVET PDAPEASSPA HWPKESLVLY HWTQSFSSQK
     RLQVRLVIAE KGLACEERDV SLPQSEHKEP WFMRLNLGEE VPVIIHRDNI ISDYDQIIDY
     VERTFTGEHV VALMPEAGSP QHARVLQYRE LLDALPMDAY THGCILHPEL TTDSMIPKYA
     TAEIRRHLAN ATTDLMKLDH EEEPQLSEPY LSKQKKLMAK ILEHDDVSYL KKILGELAMV
     LDQIEAELEK RKLENEGQTC ELWLCGCAFT LADVLLGATL HRLKFLGLSK KYWEDGSRPN
     LQSFFERVQR RFAFRKVLGD IHTTLLSAVI PNAFRLVKRK PPSFFGASFL MGSLGGMGYF
     AYWYLKKKYI
//
ID   OGRL1_MOUSE             Reviewed;         464 AA.
AC   Q8VE52;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Opioid growth factor receptor-like protein 1;
GN   Name=Ogfrl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 186-464.
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the opioid growth factor receptor family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH19747.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AC165368; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC019747; AAH19747.1; ALT_INIT; mRNA.
DR   IPI; IPI00669660; -.
DR   RefSeq; NP_001074548.1; NM_001081079.1.
DR   UniGene; Mm.28013; -.
DR   PRIDE; Q8VE52; -.
DR   Ensembl; ENSMUST00000027343; ENSMUSP00000027343; ENSMUSG00000026158.
DR   GeneID; 70155; -.
DR   KEGG; mmu:70155; -.
DR   CTD; 70155; -.
DR   MGI; MGI:1917405; Ogfrl1.
DR   eggNOG; roNOG13199; -.
DR   GeneTree; ENSGT00390000018730; -.
DR   HOGENOM; HBG445490; -.
DR   HOVERGEN; HBG066276; -.
DR   InParanoid; Q8VE52; -.
DR   OMA; VSFREPT; -.
DR   OrthoDB; EOG4SQWXH; -.
DR   NextBio; 331094; -.
DR   ArrayExpress; Q8VE52; -.
DR   Bgee; Q8VE52; -.
DR   CleanEx; MM_OGFRL1; -.
DR   Genevestigator; Q8VE52; -.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:InterPro.
DR   InterPro; IPR006757; OGF_rcpt.
DR   Pfam; PF04664; OGFr_N; 1.
PE   2: Evidence at transcript level;
FT   CHAIN         1    464       Opioid growth factor receptor-like
FT                                protein 1.
FT                                /FTId=PRO_0000314143.
SQ   SEQUENCE   464 AA;  52268 MW;  5736423F67FB597C CRC64;
     MGNLLGGVSF REPTTVEDCD STWQTDSEPE PEQPGPAGGG EGQQHDEPEQ PKQPPERAGG
     RPRASPVPED HAEAAGAEQG GESTEGNAKP KRSFYAARDL YKYRHQYPNF KDIRYQNDLS
     NLRFYKNKIP FKPDGVYIEE VLNKWKGDYE KLEHNHTYIQ WLFPLREQGL NFYAKELTTY
     EIEEFKKTKE AIRRFLLAYK MMLEFFGIKL IDKTGNVARA GNWQERFQHL NESQHNYLRI
     TRILKSLGEL GYESFKSPLV KFILHEALVE NTIPNIKQSA LEYFVYTIRD RRERRKLLRF
     AQKHYTPSEN FIWGPPKKEL PERSKAQKTP TLPASGSNGQ TSTHKKSKDS KISPGASHVN
     SKSVEEKKGA SREPGEEADK PSPEPGSGDP KPRNTEKDSA ADQSDSPPEK TVPDTAGKGE
     CPTSSEKDGE GEDQSKDSEN PENAGCHAEV VAQQNATNPQ TSSG
//
ID   TAF12_MOUSE             Reviewed;         161 AA.
AC   Q8VE65; Q3V0S7; Q9CZ11; Q9D8Q0;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Transcription initiation factor TFIID subunit 12;
DE   AltName: Full=Transcription initiation factor TFIID 20 kDa subunits;
DE            Short=TAFII-20;
DE            Short=TAFII20;
GN   Name=Taf12;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Pancreas, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: TAFs are components of the transcription factor IID
CC       (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII
CC       complex (TFTC). TAFs components-TIIFD are essential for mediating
CC       regulation of RNA polymerase transcription (By similarity).
CC   -!- SUBUNIT: TFIID and PCAF are composed of TATA binding protein (TBP)
CC       and a number of TBP-associated factors (TAFs). TBP is not part of
CC       TFTC. Interacts directly with TBP; additional interactions between
CC       TAFII20 and TAFII28 or TAFII30 were detected. Component of the
CC       PCAF complex, at least composed of TADA2L/ADA2, TADA3L/ADA3,
CC       TAF5L, SUPT3H, TAF6L, TAF9, TAF10, TAF12 and TRRAP. Component of
CC       the STAGA transcription coactivator-HAT complex, at least composed
CC       of SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L, TAD1L, TAF10,
CC       TAF12, TRRAP and TAF9. Interacts with ATF7 (via its
CC       transactivation domain); the interaction promotes the
CC       transactivation of ATF7 and is prevented by sumoylation of ATF7
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the TAF12 family.
CC   -!- SIMILARITY: Contains 1 histone-fold domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK007811; BAB25276.1; -; mRNA.
DR   EMBL; AK013133; BAB28669.1; -; mRNA.
DR   EMBL; AK132927; BAE21426.1; -; mRNA.
DR   EMBL; BC019668; AAH19668.1; -; mRNA.
DR   IPI; IPI00311877; -.
DR   RefSeq; NP_079855.2; NM_025579.3.
DR   UniGene; Mm.331926; -.
DR   ProteinModelPortal; Q8VE65; -.
DR   SMR; Q8VE65; 55-128.
DR   DIP; DIP-29178N; -.
DR   STRING; Q8VE65; -.
DR   PhosphoSite; Q8VE65; -.
DR   PRIDE; Q8VE65; -.
DR   Ensembl; ENSMUST00000030731; ENSMUSP00000030731; ENSMUSG00000028899.
DR   Ensembl; ENSMUST00000105963; ENSMUSP00000101583; ENSMUSG00000028899.
DR   GeneID; 66464; -.
DR   KEGG; mmu:66464; -.
DR   UCSC; uc008vax.1; mouse.
DR   CTD; 66464; -.
DR   MGI; MGI:1913714; Taf12.
DR   GeneTree; ENSGT00390000002144; -.
DR   HOVERGEN; HBG055174; -.
DR   InParanoid; Q8VE65; -.
DR   OrthoDB; EOG4ZCT5X; -.
DR   PhylomeDB; Q8VE65; -.
DR   NextBio; 321768; -.
DR   ArrayExpress; Q8VE65; -.
DR   Bgee; Q8VE65; -.
DR   Genevestigator; Q8VE65; -.
DR   GermOnline; ENSMUSG00000028899; Mus musculus.
DR   GO; GO:0030914; C:STAGA complex; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0006352; P:transcription initiation, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR003228; TFIID_sub.
DR   Gene3D; G3DSA:1.10.20.10; Histone-fold; 1.
DR   Pfam; PF03847; TFIID_20kDa; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Transcription; Transcription regulation.
FT   CHAIN         1    161       Transcription initiation factor TFIID
FT                                subunit 12.
FT                                /FTId=PRO_0000118908.
FT   MOD_RES      43     43       Phosphothreonine (By similarity).
FT   MOD_RES      51     51       Phosphoserine.
FT   MOD_RES      59     59       Phosphothreonine (By similarity).
FT   CONFLICT     77     77       D -> G (in Ref. 1; BAB28669).
FT   CONFLICT    126    126       M -> I (in Ref. 1; BAB28669).
FT   CONFLICT    157    157       K -> N (in Ref. 1; BAB25276).
SQ   SEQUENCE   161 AA;  17875 MW;  B3C11D70B6E94E35 CRC64;
     MNQFGPSALI NLSSFSSVKP EPASTPPQGS MANSTTVGKI AGTPGTGGRL SPENNQVLTK
     KKLQDLVREV DPNEQLDEDV EEMLLQIADD FIESVVTAAC QLARHRKSST LEVKDVQLHL
     ERQWNMWIPG FGSEEIRPYK KACTTEAHKQ RMALIRKTTK K
//
ID   F1142_MOUSE             Reviewed;         497 AA.
AC   Q8VE88; Q3UE42; Q5QNR1; Q9D310;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Protein FAM114A2;
GN   Name=Fam114a2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Colon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VE88-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VE88-2; Sequence=VSP_022796;
CC   -!- SIMILARITY: Belongs to the FAM114 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK018570; BAB31282.1; -; mRNA.
DR   EMBL; AK149763; BAE29069.1; -; mRNA.
DR   EMBL; AL672236; CAI24469.1; -; Genomic_DNA.
DR   EMBL; AL672236; CAI24470.1; -; Genomic_DNA.
DR   EMBL; BC019518; AAH19518.1; -; mRNA.
DR   IPI; IPI00336509; -.
DR   IPI; IPI00648806; -.
DR   RefSeq; NP_001162138.1; NM_001168667.1.
DR   RefSeq; NP_001162139.1; NM_001168668.1.
DR   RefSeq; NP_080618.1; NM_026342.3.
DR   UniGene; Mm.25632; -.
DR   PRIDE; Q8VE88; -.
DR   Ensembl; ENSMUST00000020831; ENSMUSP00000020831; ENSMUSG00000020523.
DR   Ensembl; ENSMUST00000108850; ENSMUSP00000104478; ENSMUSG00000020523.
DR   GeneID; 67726; -.
DR   KEGG; mmu:67726; -.
DR   CTD; 67726; -.
DR   MGI; MGI:1917629; Fam114a2.
DR   eggNOG; roNOG13707; -.
DR   GeneTree; ENSGT00390000010054; -.
DR   HOGENOM; HBG445321; -.
DR   HOVERGEN; HBG056879; -.
DR   InParanoid; Q8VE88; -.
DR   OMA; LSQMTIV; -.
DR   OrthoDB; EOG4J1180; -.
DR   NextBio; 325383; -.
DR   ArrayExpress; Q8VE88; -.
DR   Bgee; Q8VE88; -.
DR   Genevestigator; Q8VE88; -.
DR   InterPro; IPR007998; DUF719.
DR   PANTHER; PTHR12842; DUF719; 1.
DR   Pfam; PF05334; DUF719; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    497       Protein FAM114A2.
FT                                /FTId=PRO_0000274565.
FT   COMPBIAS    293    298       Poly-Glu.
FT   MOD_RES     203    203       Phosphothreonine.
FT   VAR_SEQ      61     67       Missing (in isoform 2).
FT                                /FTId=VSP_022796.
FT   CONFLICT     14     14       G -> E (in Ref. 3; AAH19518).
FT   CONFLICT    304    304       N -> D (in Ref. 3; AAH19518).
FT   CONFLICT    318    318       V -> I (in Ref. 3; AAH19518).
FT   CONFLICT    438    438       A -> V (in Ref. 3; AAH19518).
FT   CONFLICT    488    488       S -> P (in Ref. 1; BAE29069).
FT   CONFLICT    494    494       S -> P (in Ref. 3; AAH19518).
SQ   SEQUENCE   497 AA;  54045 MW;  9346964631460F6D CRC64;
     MSDKDPPESP VVTGVASTLK DENCEPVEKP EDKSQPVVST RKRPETKPSS DLEASALPAQ
     VSLAVAKETA SKDVPQTGWG YWGSWGKSLL SSASATVATV GQGISNVIEK AETSLGIPSP
     TEISAEVKQA AGEKNAGENG SLLVAAPFGM LSTISTAVQS TGKSVISGGL DALEFIGKKT
     MDVIAEGDPG FKRTKGLMNR TSTLSQVLRE AKDKEEQRPS NEVTMETDKK THYGLLFDEF
     QGLSHLEALE MLSRESEIKV KSILSSLSGE ELQTTRLELE QLKEVFSLAE FCEEEEEERQ
     GDDNFTKEIT DLFAQLHVSS RPEKLARARN TAYKWIRTSL ARPVAEKEEG EKESEAGNTE
     EAQKHSIEDI HAFAIRSLAE LTACSIELFH KTAALVLHGQ KQEVTALERS QTLSQMTVML
     CKDLASLSKE FTTCLTTAGV REKADVLNPV ITAVFLEASN SASYIQDAFQ LLLPVLQISL
     IESKTESSTC EPQSRDL
//
ID   F134B_MOUSE             Reviewed;         356 AA.
AC   Q8VE91; Q7TMY5; Q9CUJ4; Q9D8Z5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Protein FAM134B;
GN   Name=Fam134b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Liver, Pancreas, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=19838196; DOI=10.1038/ng.464;
RA   Kurth I., Pamminger T., Hennings J.C., Soehendra D., Huebner A.K.,
RA   Rotthier A., Baets J., Senderek J., Topaloglu H., Farrell S.A.,
RA   Nuernberg G., Nurnberg P., De Jonghe P., Gal A., Kaether C.,
RA   Timmerman V., Huebner C.A.;
RT   "Mutations in FAM134B, encoding a newly identified Golgi protein,
RT   cause severe sensory and autonomic neuropathy.";
RL   Nat. Genet. 41:1179-1181(2009).
CC   -!- FUNCTION: Required for long-term survival of nociceptive and
CC       autonomic ganglion neurons.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane;
CC       Single-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8VE91-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VE91-2; Sequence=VSP_025687;
CC       Name=3;
CC         IsoId=Q8VE91-3; Sequence=VSP_025688;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in sensory and
CC       autonomic ganglia has demonstrated by in situ hybridizations of
CC       embryonic day 14.5 mouse embryo sections. Detected specifically in
CC       organelle-like intracellular structures of the small and large
CC       neurons of dorsal root ganglia (DRG) and in N2a cells, a tumor
CC       cell line that is related to autonomic ganglion neurons (at
CC       protein level).
CC   -!- SIMILARITY: Belongs to the FAM134 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK007506; BAB25077.1; -; mRNA.
DR   EMBL; AK146972; BAE27577.1; -; mRNA.
DR   EMBL; AK015887; BAB30019.1; -; mRNA.
DR   EMBL; AK167327; BAE39429.1; -; mRNA.
DR   EMBL; BC019494; AAH19494.1; -; mRNA.
DR   EMBL; BC054415; AAH54415.1; -; mRNA.
DR   IPI; IPI00380301; -.
DR   IPI; IPI00851043; -.
DR   IPI; IPI00876547; -.
DR   RefSeq; NP_001030023.1; NM_001034851.1.
DR   RefSeq; NP_079735.2; NM_025459.2.
DR   UniGene; Mm.25311; -.
DR   PhosphoSite; Q8VE91; -.
DR   PRIDE; Q8VE91; -.
DR   Ensembl; ENSMUST00000022881; ENSMUSP00000022881; ENSMUSG00000022270.
DR   Ensembl; ENSMUST00000110435; ENSMUSP00000106065; ENSMUSG00000022270.
DR   Ensembl; ENSMUST00000110438; ENSMUSP00000106068; ENSMUSG00000022270.
DR   Ensembl; ENSMUST00000110439; ENSMUSP00000106069; ENSMUSG00000022270.
DR   GeneID; 66270; -.
DR   KEGG; mmu:66270; -.
DR   UCSC; uc007vjg.1; mouse.
DR   CTD; 66270; -.
DR   MGI; MGI:1913520; Fam134b.
DR   eggNOG; roNOG10824; -.
DR   GeneTree; ENSGT00530000063240; -.
DR   HOVERGEN; HBG071073; -.
DR   OrthoDB; EOG48WC23; -.
DR   NextBio; 321155; -.
DR   ArrayExpress; Q8VE91; -.
DR   Bgee; Q8VE91; -.
DR   Genevestigator; Q8VE91; -.
DR   GO; GO:0005801; C:cis-Golgi network; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
PE   1: Evidence at protein level;
KW   Alternative splicing; Golgi apparatus; Membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    356       Protein FAM134B.
FT                                /FTId=PRO_0000288467.
FT   TRANSMEM     68     88       Helical; (Potential).
FT   MOD_RES     135    135       Phosphoserine.
FT   VAR_SEQ       1     11       MPAGGGCGPGR -> MLGDWAALLPSCLSRCWSE (in
FT                                isoform 2).
FT                                /FTId=VSP_025687.
FT   VAR_SEQ       1     11       MPAGGGCGPGR -> M (in isoform 3).
FT                                /FTId=VSP_025688.
SQ   SEQUENCE   356 AA;  38963 MW;  94B899C82D774FA9 CRC64;
     MPAGGGCGPG RSWEVINSKP DERARLSQCI AESWMNFSMF LQEMSLFKQQ SPGKFCLLVC
     SVCTFFTILG SYIPGVILSY LLLLFAFLCP LFKCNDIGQK IYSKVKSILL KLDFGIGEYI
     NQKKRERSEA DKEKSHKDDS ELDFSALCPK ISLTVAAKEL SVSDTDVSEV SWTDNGTFNL
     SEGYTPQTDT SDDLDRPSEE VFSRDLSDFP SLENGTGTND EDELSLGLPT ELKRKKQQLD
     SAHRPSKERQ SAAGLSLPLK SDQALHLMSN LAGDVITAAM TAAIKDQLEG ARQALTQVAP
     TAGEDTDTEE GDDFELLDQA ELDQIESELG LTQDQGAEAQ QSKKSSGFLS NLLGGH
//
ID   LEGLA_MOUSE             Reviewed;         172 AA.
AC   Q8VED9; Q8C4P8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Galectin-related protein A;
GN   Name=Grpa;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Aorta, Head, Placenta, Spleen, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Does not bind lactose, and may not bind carbohydrates
CC       (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SIMILARITY: Contains 1 galectin domain.
CC   -!- CAUTION: Most of the residues in the galectin domain that have
CC       been shown to be critical for carbohydrate-binding in other
CC       galectins are not conserved.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK041053; BAC30800.1; -; mRNA.
DR   EMBL; AK081513; BAC38245.1; -; mRNA.
DR   EMBL; AK156350; BAE33684.1; -; mRNA.
DR   EMBL; AK167557; BAE39621.1; -; mRNA.
DR   EMBL; AL662817; CAI25751.1; -; Genomic_DNA.
DR   EMBL; BC019131; AAH19131.1; -; mRNA.
DR   IPI; IPI00124501; -.
DR   RefSeq; NP_776113.1; NM_173752.4.
DR   UniGene; Mm.76694; -.
DR   HSSP; P56470; 1X50.
DR   ProteinModelPortal; Q8VED9; -.
DR   SMR; Q8VED9; 38-171.
DR   PhosphoSite; Q8VED9; -.
DR   PRIDE; Q8VED9; -.
DR   Ensembl; ENSMUST00000047028; ENSMUSP00000044342; ENSMUSG00000042363.
DR   GeneID; 216551; -.
DR   KEGG; mmu:216551; -.
DR   UCSC; uc007idj.1; mouse.
DR   MGI; MGI:1916114; 1110067D22Rik.
DR   eggNOG; roNOG15272; -.
DR   GeneTree; ENSGT00550000074181; -.
DR   HOGENOM; HBG717055; -.
DR   HOVERGEN; HBG006255; -.
DR   InParanoid; Q8VED9; -.
DR   OMA; HRIETLS; -.
DR   OrthoDB; EOG40GCS0; -.
DR   PhylomeDB; Q8VED9; -.
DR   NextBio; 375208; -.
DR   ArrayExpress; Q8VED9; -.
DR   Bgee; Q8VED9; -.
DR   CleanEx; MM_1110067D22RIK; -.
DR   Genevestigator; Q8VED9; -.
DR   GO; GO:0005529; F:sugar binding; IEA:UniProtKB-KW.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   InterPro; IPR001079; Galectin_CRD.
DR   Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 1.
DR   PANTHER; PTHR11346; Galectin_bd; 1.
DR   Pfam; PF00337; Gal-bind_lectin; 1.
DR   SMART; SM00908; Gal-bind_lectin; 1.
DR   SMART; SM00276; GLECT; 1.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
DR   PROSITE; PS51304; GALECTIN; 1.
PE   1: Evidence at protein level;
KW   Lectin; Phosphoprotein.
FT   CHAIN         1    172       Galectin-related protein A.
FT                                /FTId=PRO_0000315767.
FT   DOMAIN       39    168       Galectin.
FT   MOD_RES      25     25       Phosphoserine.
SQ   SEQUENCE   172 AA;  18956 MW;  56D40BE7D56FC336 CRC64;
     MAGSVADSDA VVKLDDGHLN NSLGSPVQAD VYFPRLIVPF CGHIKGGMRP GKKVLVMGIV
     DLNPESFAIS LTCGDSEDPP ADVAIELKAV FTDRQLLRNS CISGERGEEQ SAIPYFPFIP
     DQPFRVEILC EHPRFRVFVD GHQLFDFYHR IQTLSAIDTI KINGDLQITK LG
//
ID   GRM1A_MOUSE             Reviewed;         722 AA.
AC   Q8VEF1; Q3U914; Q3UD89; Q69ZH2; Q8BNF1;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=GRAM domain-containing protein 1A;
GN   Name=Gramd1a; Synonyms=D7Bwg0611e, Kiaa1533;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 34-722 (ISOFORM 1).
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 293-722 (ISOFORM 3).
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8VEF1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VEF1-2; Sequence=VSP_025467;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q8VEF1-3; Sequence=VSP_025468;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 GRAM domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH18554.1; Type=Erroneous initiation;
CC       Sequence=BAD32472.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC       Sequence=BAE29255.1; Type=Erroneous initiation;
CC       Sequence=BAE29372.1; Type=Erroneous initiation;
CC       Sequence=BAE29897.1; Type=Erroneous initiation;
CC       Sequence=BAE30853.1; Type=Erroneous initiation;
CC       Sequence=BAE31103.1; Type=Erroneous initiation;
CC       Sequence=BAE32853.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK083837; BAC39036.1; -; mRNA.
DR   EMBL; AK150032; BAE29255.1; ALT_INIT; mRNA.
DR   EMBL; AK150196; BAE29372.1; ALT_INIT; mRNA.
DR   EMBL; AK150837; BAE29897.1; ALT_INIT; mRNA.
DR   EMBL; AK151987; BAE30853.1; ALT_INIT; mRNA.
DR   EMBL; AK152294; BAE31103.1; ALT_INIT; mRNA.
DR   EMBL; AK154821; BAE32853.1; ALT_INIT; mRNA.
DR   EMBL; BC018554; AAH18554.1; ALT_INIT; mRNA.
DR   EMBL; AK173194; BAD32472.1; ALT_SEQ; Transcribed_RNA.
DR   IPI; IPI00124534; -.
DR   IPI; IPI00761341; -.
DR   IPI; IPI00845779; -.
DR   RefSeq; NP_082174.3; NM_027898.3.
DR   UniGene; Mm.27366; -.
DR   IntAct; Q8VEF1; 2.
DR   PhosphoSite; Q8VEF1; -.
DR   PRIDE; Q8VEF1; -.
DR   Ensembl; ENSMUST00000001280; ENSMUSP00000001280; ENSMUSG00000001248.
DR   Ensembl; ENSMUST00000085636; ENSMUSP00000082778; ENSMUSG00000001248.
DR   GeneID; 52857; -.
DR   KEGG; mmu:52857; -.
DR   CTD; 52857; -.
DR   MGI; MGI:105490; Gramd1a.
DR   eggNOG; roNOG14817; -.
DR   GeneTree; ENSGT00580000081380; -.
DR   HOGENOM; HBG505981; -.
DR   HOVERGEN; HBG062004; -.
DR   InParanoid; Q8VEF1; -.
DR   OrthoDB; EOG4255SS; -.
DR   PhylomeDB; Q8VEF1; -.
DR   NextBio; 309647; -.
DR   ArrayExpress; Q8VEF1; -.
DR   Bgee; Q8VEF1; -.
DR   CleanEx; MM_GRAMD1A; -.
DR   Genevestigator; Q8VEF1; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR004182; GRAM.
DR   Pfam; PF02893; GRAM; 1.
DR   SMART; SM00568; GRAM; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    722       GRAM domain-containing protein 1A.
FT                                /FTId=PRO_0000287447.
FT   TRANSMEM    609    629       Helical; (Potential).
FT   DOMAIN       93    160       GRAM.
FT   MOD_RES     265    265       Phosphoserine (By similarity).
FT   MOD_RES     269    269       Phosphoserine (By similarity).
FT   MOD_RES     279    279       Phosphothreonine (By similarity).
FT   MOD_RES     283    283       Phosphoserine (By similarity).
FT   MOD_RES     552    552       Phosphoserine (By similarity).
FT   MOD_RES     562    562       Phosphoserine (By similarity).
FT   VAR_SEQ     495    722       Missing (in isoform 2).
FT                                /FTId=VSP_025467.
FT   VAR_SEQ     495    528       Missing (in isoform 3).
FT                                /FTId=VSP_025468.
FT   CONFLICT     37     37       P -> S (in Ref. 2; AAH18554).
FT   CONFLICT    250    250       V -> M (in Ref. 2; AAH18554).
FT   CONFLICT    303    303       G -> SQ (in Ref. 2; AAH18554).
FT   CONFLICT    705    705       T -> A (in Ref. 1; BAE29897/BAE31103/
FT                                BAE30853).
SQ   SEQUENCE   722 AA;  80699 MW;  323B29510A77F409 CRC64;
     MFDTTPHSGR SSPSSSPSLR KRLQLLPPIR PPPASEPEPG TMVEKGSDSS SEKSGVSGTL
     STQSLGSRNF IRNSKKMQSW YSMLCPTYKQ RNEDFRKLFS KLPEAERLIV DYSCALQREI
     LLQGRLYLSE NWICFYSNIF RWETTISIQL KEVTCLKKEK TAKLIPNAIQ ICTESEKHFF
     TSFGARDRCF LLIFRLWQNA LLEKTLSPRE LWHLVHQCYG SELGLTSEDE DYVCPLQLNG
     LGSPKEVGDV IALSDISPSG AADHSQEPSP VGSRRGRVTP NLSRASSDAD HGAEEDKEEQ
     TDGLDASSSQ TVTPVAEPLS SEPTPPDGPT SSLGPLDLLS REELLTDTSN SSSSTGEEGD
     LAALLPDLSG RLLINSVFHM GAERLQQMLF SDSPFLQGFL QQRKFTDVTL SPWSSDSKCH
     QRRVLTYTIP ISNQLGPKSA SVVETQTLFR RGPQAGGCVV DSEVLTQGIP YQDYFYTAHR
     YCILGLARNK ARLRVSSEIR YRKQPWSLVK SLIEKNSWSG IEDYFHHLDR ELAKAEKLSL
     EEGGKDTRGL LSGLRRRKRP LSWRGHRDGP QHPDPDPCTQ TSMHTSGSLS SRFSEPSVDQ
     GPGAGIPSAL VLISIVLIVL IALNALLFYR LWSLERTAHT FESWHSLALA KGKFPQTATE
     WAEILALQKH FHSVEVHKWR QILRASVELL DEMKFSLEKL HQGITVPDPP LDTQPQPDDS
     FP
//
ID   EPMIP_MOUSE             Reviewed;         606 AA.
AC   Q8VEH5; Q80TS4;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=EPM2A-interacting protein 1;
DE   AltName: Full=Laforin-interacting protein;
GN   Name=Epm2aip1; Synonyms=Kiaa0766;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 265-606.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
CC   -!- SUBUNIT: Interacts with EPM2A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum (By similarity).
CC   -----------------------------------------------------------------------
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DR   EMBL; AK030084; BAC26774.1; -; mRNA.
DR   EMBL; AK032284; BAC27793.1; -; mRNA.
DR   EMBL; BC018474; AAH18474.1; -; mRNA.
DR   EMBL; AK122366; BAC65648.1; -; mRNA.
DR   IPI; IPI00124614; -.
DR   RefSeq; NP_780475.1; NM_175266.4.
DR   UniGene; Mm.209005; -.
DR   ProteinModelPortal; Q8VEH5; -.
DR   STRING; Q8VEH5; -.
DR   PhosphoSite; Q8VEH5; -.
DR   PRIDE; Q8VEH5; -.
DR   Ensembl; ENSMUST00000060711; ENSMUSP00000052904; ENSMUSG00000046785.
DR   GeneID; 77781; -.
DR   KEGG; mmu:77781; -.
DR   NMPDR; fig|10090.3.peg.20955; -.
DR   UCSC; uc009rvr.1; mouse.
DR   CTD; 77781; -.
DR   MGI; MGI:1925031; Epm2aip1.
DR   eggNOG; maNOG19291; -.
DR   GeneTree; ENSGT00550000074433; -.
DR   HOGENOM; HBG283744; -.
DR   HOVERGEN; HBG051494; -.
DR   InParanoid; Q8VEH5; -.
DR   OMA; RMIGENS; -.
DR   OrthoDB; EOG4JHCFX; -.
DR   PhylomeDB; Q8VEH5; -.
DR   NextBio; 347539; -.
DR   ArrayExpress; Q8VEH5; -.
DR   Bgee; Q8VEH5; -.
DR   CleanEx; MM_EPM2AIP1; -.
DR   Genevestigator; Q8VEH5; -.
DR   GermOnline; ENSMUSG00000046785; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Phosphoprotein.
FT   CHAIN         1    606       EPM2A-interacting protein 1.
FT                                /FTId=PRO_0000086993.
FT   MOD_RES     147    147       Phosphoserine (By similarity).
SQ   SEQUENCE   606 AA;  70096 MW;  8D0F88686866D953 CRC64;
     MWMTPKRIRM EVDEALVFRP EWTQRYLVVE PAEGDGALCL VCRRLVASTR ERDVRRHYEA
     EHEFYERFVG DEERAALVER LRQGDMSLAA VLTPEERATR AGLGLCRFLA LKGRGWGEGD
     FVHQCMEVLL REVLPDHVGV LEGIDLSPEI TRQRILSIDS NLRSQLFNRA RDFKAYSLAL
     DDQAFVAYEN YLLVFIRGVG RDLEVQEDLL TIINLTHHFS VGALMSAILE ALQTAGLSLQ
     RMVGLTTTHT LRMIGENSGL VSYMREKAVS PNCWNVIHYS GFLHLELLSS YDVDINQIIN
     TISEWVVMIK TRGVRRPEFQ PLLTESESEH GERVNGRCLN NWLRRGKTLK LIFSLRKEIE
     AFLVSVGATT VHFSDKQWLC DFGFLVDIMD YLREISEELQ ISKVFAAAAF ERICTFEGKL
     SSLQRHMEEV NLTDFPAFSI IVDELKQQFK EDQKIFDPDR YQMVISRLQK DFERHFKDLR
     FIKKDLELFS NPFSFKPEYA PISVRVELTK LQANTDLWNE YRVKDLGQFY AGLSGEAYPI
     IKGVAYKVAS LFDSNQICDK AFAYLTRNQH TLSQPLTDEH LQALFRVATT EMDPRWDDLV
     RERNDS
//
ID   REM2_MOUSE              Reviewed;         341 AA.
AC   Q8VEL9; Q8BPB1;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 2.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=GTP-binding protein REM 2;
DE   AltName: Full=Rad and Gem-like GTP-binding protein 2;
GN   Name=Rem2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Pituitary, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=129; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Binds GTP saturably and exhibits a low intrinsic rate of
CC       GTP hydrolysis (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VEL9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VEL9-2; Sequence=VSP_038749;
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. RGK family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH18219.1; Type=Erroneous initiation;
CC       Sequence=BAC36746.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK077317; BAC36746.1; ALT_INIT; mRNA.
DR   EMBL; AK090165; BAC41120.1; -; mRNA.
DR   EMBL; BC018219; AAH18219.1; ALT_INIT; mRNA.
DR   IPI; IPI00124740; -.
DR   IPI; IPI00955387; -.
DR   RefSeq; NP_542764.2; NM_080726.3.
DR   UniGene; Mm.274727; -.
DR   ProteinModelPortal; Q8VEL9; -.
DR   SMR; Q8VEL9; 114-282.
DR   STRING; Q8VEL9; -.
DR   PhosphoSite; Q8VEL9; -.
DR   Ensembl; ENSMUST00000022783; ENSMUSP00000022783; ENSMUSG00000022176.
DR   GeneID; 140743; -.
DR   KEGG; mmu:140743; -.
DR   UCSC; uc007twe.1; mouse.
DR   CTD; 140743; -.
DR   MGI; MGI:2155260; Rem2.
DR   eggNOG; roNOG11055; -.
DR   GeneTree; ENSGT00600000084219; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG104899; -.
DR   InParanoid; Q8VEL9; -.
DR   OrthoDB; EOG43JC57; -.
DR   PhylomeDB; Q8VEL9; -.
DR   NextBio; 369967; -.
DR   ArrayExpress; Q8VEL9; -.
DR   Bgee; Q8VEL9; -.
DR   CleanEx; MM_REM2; -.
DR   Genevestigator; Q8VEL9; -.
DR   GermOnline; ENSMUSG00000022176; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0008134; F:transcription factor binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR017358; GTP-binding_GEM/REM/Rad.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR020849; Ras_small_GTPase.
DR   InterPro; IPR002078; RNA_pol_sigma_54_int.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   Pfam; PF00071; Ras; 1.
DR   PIRSF; PIRSF038017; GTP-binding_GEM; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; GTP-binding; Membrane;
KW   Nucleotide-binding.
FT   CHAIN         1    341       GTP-binding protein REM 2.
FT                                /FTId=PRO_0000122484.
FT   NP_BIND     122    129       GTP (By similarity).
FT   NP_BIND     230    233       GTP (By similarity).
FT   NP_BIND     261    262       GTP (By similarity).
FT   VAR_SEQ       1     69       Missing (in isoform 2).
FT                                /FTId=VSP_038749.
FT   CONFLICT     13     15       TET -> IEI (in Ref. 2; AAH18219).
FT   CONFLICT    203    203       G -> S (in Ref. 2; AAH18219).
SQ   SEQUENCE   341 AA;  37367 MW;  D7F415A9ABC86125 CRC64;
     MHTDLDTDMD MDTETVALCS SSSRQASPLG TPTPEADTTL LKQKPEKLLA ELDLSGPPPA
     PGVPRRRGSM PVPYKHQLRR AQAVDELDWP PQASPSGSSD SLGSGEAALT QKDGVFKVML
     VGESGVGKST LAGTFGGLQG DHAHEMENSE DTYERRIMVD KEEVTLIVYD IWEQGDAGGW
     LQDHCLQTGD AFLIVFSVTD RRGFSKVPET LLRLRAGRPH HDLPVILVGN KSDLARSREV
     SLEEGRHLAG TLSCKHIETS AALHHNTREL FEGAVRQIRL RRGRGHAGGQ RPEPSSPDGP
     APPTRRESLT KKAKRFLANL VPRNAKFFKQ RSRSCHDLSV L
//
ID   GOLI_MOUSE              Reviewed;         419 AA.
AC   Q8VEM1; Q80VL7; Q9QZQ6;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF130;
DE            EC=6.3.2.-;
DE   AltName: Full=G1-related zinc finger protein;
DE   AltName: Full=Goliath homolog;
DE   AltName: Full=RING finger protein 130;
DE   Flags: Precursor;
GN   Name=Rnf130; Synonyms=G1rp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   INDUCTION.
RX   MEDLINE=20267845; PubMed=10806348; DOI=10.1016/S0378-1119(00)00109-8;
RA   Baker S.J., Reddy E.P.;
RT   "Cloning of murine G1RP, a novel gene related to Drosophila
RT   melanogaster g1.";
RL   Gene 248:33-40(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Acts as an E3 ubiquitin-protein ligase (By similarity).
CC       May have a role during the programmed cell death of hematopoietic
CC       cells.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential). Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: Expression is highest in liver, with lesser
CC       amounts in the lung, spleen, brain, heart, kidney and testis.
CC   -!- INDUCTION: Up-regulated in response to interleukin-3 (IL-3)
CC       withdrawal-induced apoptosis of 32Dcl3 cells (derived from bone
CC       marrow).
CC   -!- SIMILARITY: Contains 1 PA (protease associated) domain.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF171875; AAF05310.1; -; mRNA.
DR   EMBL; AL627187; CAI25115.1; -; Genomic_DNA.
DR   EMBL; AL645913; CAI25115.1; JOINED; Genomic_DNA.
DR   EMBL; AL645913; CAI24372.1; -; Genomic_DNA.
DR   EMBL; AL627187; CAI24372.1; JOINED; Genomic_DNA.
DR   EMBL; BC018199; AAH18199.1; -; mRNA.
DR   EMBL; BC048901; AAH48901.2; -; mRNA.
DR   IPI; IPI00331206; -.
DR   RefSeq; NP_067515.2; NM_021540.3.
DR   UniGene; Mm.359004; -.
DR   ProteinModelPortal; Q8VEM1; -.
DR   SMR; Q8VEM1; 26-187, 261-309.
DR   STRING; Q8VEM1; -.
DR   PRIDE; Q8VEM1; -.
DR   Ensembl; ENSMUST00000102776; ENSMUSP00000099837; ENSMUSG00000020376.
DR   GeneID; 59044; -.
DR   KEGG; mmu:59044; -.
DR   UCSC; uc007irl.1; mouse.
DR   CTD; 59044; -.
DR   MGI; MGI:1891717; Rnf130.
DR   GeneTree; ENSGT00550000074163; -.
DR   HOGENOM; HBG716731; -.
DR   HOVERGEN; HBG057659; -.
DR   InParanoid; Q8VEM1; -.
DR   OMA; GDLASDN; -.
DR   OrthoDB; EOG40VVQ5; -.
DR   PhylomeDB; Q8VEM1; -.
DR   NextBio; 314662; -.
DR   ArrayExpress; Q8VEM1; -.
DR   Bgee; Q8VEM1; -.
DR   CleanEx; MM_RNF130; -.
DR   Genevestigator; Q8VEM1; -.
DR   GermOnline; ENSMUSG00000020376; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; NAS:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   InterPro; IPR003137; Protease-assoc_domain.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Cytoplasm; Glycoprotein; Ligase; Membrane; Metal-binding;
KW   Signal; Transmembrane; Transmembrane helix; Ubl conjugation pathway;
KW   Zinc; Zinc-finger.
FT   SIGNAL        1     27       Potential.
FT   CHAIN        28    419       E3 ubiquitin-protein ligase RNF130.
FT                                /FTId=PRO_0000030719.
FT   TOPO_DOM     28    194       Extracellular (Potential).
FT   TRANSMEM    195    217       Helical; (Potential).
FT   TOPO_DOM    218    419       Cytoplasmic (Potential).
FT   DOMAIN      105    176       PA.
FT   ZN_FING     264    305       RING-type.
FT   CARBOHYD     29     29       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     40     40       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    112    112       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    135    135       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    172    172       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    189    189       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    310    310       K -> R (in Ref. 1; AAF05310).
SQ   SEQUENCE   419 AA;  46376 MW;  4E699A66D658CBF2 CRC64;
     MSGAARAGPA RLAALALLTC SLWPTRADNA SQEYYTALIN VTVQEPGRGT PLTFRIDRGR
     YGLDSPKAEV RGQVLAPLPI HGVADHLGCD PQTRFFVPPN IKQWIALLQR GNCTFKEKIS
     RAAFHNAVAV VIYNNKSKEE PVTMTHPGTG DIIAVMITEL RGKDILSYLE KNISVQMTIA
     VGTRMPPKNF SRGSLVFVSI SFIVLMIISS AWLIFYFIQK IRYTNARDRN QRRLGDAAKK
     AISKLTTRTV KKGDKETDPD FDHCAVCIES YKQNDVVRVL PCKHVFHKSC VDPWLSEHCT
     CPMCKLNILK ALGIVPNLPC TDNVAFDMER LTRTQAVNRR AALGDLAGDS SLGLEPLRTS
     GISPLPQDGE LTPRTGEINI AVTKEWFIIA SFGLLSALTL CYMIIRATAS LNANEVEWF
//
ID   Q8VF74_MOUSE            Unreviewed;       315 AA.
AC   Q8VF74;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   SubName: Full=Olfactory receptor 995;
DE   SubName: Full=Olfactory receptor MOR203-3;
DE   SubName: Full=Olfactory receptor Olfr995;
GN   Name=Olfr995; ORFNames=RP23-429P18.3-001, mCG_1050356;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21676863; PubMed=11802173; DOI=10.1038/nn800;
RA   Zhang X., Firestein S.;
RT   "The olfactory receptor gene superfamily of the mouse.";
RL   Nat. Neurosci. 5:124-133(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21864068; PubMed=11875048; DOI=10.1093/hmg/11.5.535;
RA   Young J.M., Friedman C., Williams E.M., Ross J.A., Tonnes-Priddy L.,
RA   Trask B.J.;
RT   "Different evolutionary processes shaped the mouse and human olfactory
RT   receptor gene families.";
RL   Hum. Mol. Genet. 11:535-546(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RA   Adams M.;
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RA   Brown J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=22974002; PubMed=14611657; DOI=10.1186/gb-2003-4-11-r71;
RA   Young J.M., Shykind B.M., Lane R.P., Tonnes-Priddy L., Ross J.A.,
RA   Walker M., Williams E.M., Trask B.J.;
RT   "Odorant receptor expressed sequence tags demonstrate olfactory
RT   expression of over 400 genes, extensive alternate splicing and unequal
RT   expression levels.";
RL   Genome Biol. 4:R71.1-R71.13(2003).
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RA   Sanders K.;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC125413; AAI25414.1; -; mRNA.
DR   EMBL; BC125415; AAI25416.1; -; mRNA.
DR   EMBL; AY073664; AAL61327.1; -; Genomic_DNA.
DR   EMBL; AY318189; AAP71453.1; -; Genomic_DNA.
DR   EMBL; AL929147; CAM24032.1; -; Genomic_DNA.
DR   EMBL; CH466519; EDL27329.1; -; Genomic_DNA.
DR   IPI; IPI00125284; -.
DR   RefSeq; NP_666645.1; NM_146434.1.
DR   UniGene; Mm.377494; -.
DR   ProteinModelPortal; Q8VF74; -.
DR   STRING; Q8VF74; -.
DR   Ensembl; ENSMUST00000099924; ENSMUSP00000097508; ENSMUSG00000075218.
DR   GeneID; 258426; -.
DR   KEGG; mmu:258426; -.
DR   UCSC; uc008kki.1; mouse.
DR   CTD; 258426; -.
DR   MGI; MGI:3030829; Olfr995.
DR   eggNOG; maNOG17395; -.
DR   GeneTree; ENSGT00560000076992; -.
DR   HOGENOM; HBG755317; -.
DR   HOVERGEN; HBG017625; -.
DR   InParanoid; Q8VF74; -.
DR   OMA; NSKNINH; -.
DR   OrthoDB; EOG4DBTF4; -.
DR   NextBio; 389367; -.
DR   Genevestigator; Q8VF74; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0004984; F:olfactory receptor activity; IEA:InterPro.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR000725; Olfact_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00245; OLFACTORYR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   G-protein coupled receptor; Membrane; Receptor; Transducer;
KW   Transmembrane.
SQ   SEQUENCE   315 AA;  35558 MW;  F0906720E65C5663 CRC64;
     MIQRNTTEVT DFYLLGFGVQ KNTQSILFVV FLVVYVTSMV GNTGMILLIN TNSRLQTPMY
     FFLQNLAFVD ICYTSAITPK MLQNFMVEDS SISYTGCVIQ LLVYATFATS DCYLLAVMAV
     DRYVAICKPL RYPIIMSRQV CVQLVAFSYL MGSINSSVHT GFTFSLSYCN SKNINHFFCD
     VVPIISLSCS NIDINIMLLV IFVGFNLTFT VLVIIFSYIY IMAAILKMSS TAGRKKTFST
     CASHLTAVTI FYGTLAYMYL QPHSDNSEEN MKVASVFYGI VIPMLNPLIY SLRNKEVKEG
     FKAMSRRFLR LKSNP
//
ID   AMOT_MOUSE              Reviewed;        1126 AA.
AC   Q8VHG2; A2AMJ9; A2AMK0; Q6PFB8; Q6ZPZ1;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 3.
DT   08-FEB-2011, entry version 69.
DE   RecName: Full=Angiomotin;
GN   Name=Amot; Synonyms=Kiaa1071;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 183-1126 (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 199-1126 (ISOFORM 1), AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=B6CBAF2; TISSUE=Placenta;
RX   MEDLINE=22294023; PubMed=12406577; DOI=10.1016/S0378-1119(02)00928-9;
RA   Bratt A., Wilson W.J., Troyanovsky B., Aase K., Kessler R.,
RA   Van Meir E.G., Holmgren L.;
RT   "Angiomotin belongs to a novel protein family with conserved coiled-
RT   coil and PDZ binding domains.";
RL   Gene 298:69-77(2002).
RN   [4]
RP   ERRATUM.
RA   Bratt A., Wilson W.J., Troyanovsky B., Aase K., Kessler R.,
RA   Van Meir E.G., Holmgren L.;
RL   Gene 310:231-231(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 588-1126 (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Plays a central role in tight junction maintenance via
CC       the complex formed with ARHGAP17, which acts by regulating the
CC       uptake of polarity proteins at tight junctions. Appears to
CC       regulate endothelial cell migration and tube formation. May also
CC       play a role in the assembly of endothelial cell-cell junctions (By
CC       similarity).
CC   -!- SUBUNIT: Component of a complex whose core is composed of
CC       ARHGAP17, AMOT, MPP5/PALS1, INADL/PATJ and PARD3/PAR3. Interacts
CC       with MAGI1 and angiostatin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction (By
CC       similarity). Note=Localized on the cell surface. May act as a
CC       transmembrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VHG2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VHG2-2; Sequence=VSP_027108, VSP_027109;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, skeletal muscle and
CC       placenta.
CC   -!- DOMAIN: The angiostatin binding domain (850-1047) allows the
CC       binding to angiostatin.
CC   -!- DOMAIN: The coiled coil domain interacts directly with the BAR
CC       domain of ARHGAP17 (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- MISCELLANEOUS: 'Motus' means 'motility' in Latin.
CC   -!- SIMILARITY: Belongs to the angiomotin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH57638.1; Type=Erroneous initiation;
CC       Sequence=AAL73436.1; Type=Erroneous initiation;
CC       Sequence=CAM22158.1; Type=Erroneous initiation;
CC       Sequence=CAM22159.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL807753; CAM22158.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL807753; CAM22159.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BC057638; AAH57638.1; ALT_INIT; mRNA.
DR   EMBL; AF461135; AAL73436.1; ALT_INIT; mRNA.
DR   EMBL; AK129277; BAC98087.1; -; mRNA.
DR   IPI; IPI00830178; -.
DR   IPI; IPI00855118; -.
DR   RefSeq; NP_695231.2; NM_153319.2.
DR   UniGene; Mm.100068; -.
DR   ProteinModelPortal; Q8VHG2; -.
DR   STRING; Q8VHG2; -.
DR   PhosphoSite; Q8VHG2; -.
DR   PRIDE; Q8VHG2; -.
DR   Ensembl; ENSMUST00000125271; ENSMUSP00000116189; ENSMUSG00000041688.
DR   GeneID; 27494; -.
DR   KEGG; mmu:27494; -.
DR   NMPDR; fig|10090.3.peg.22263; -.
DR   UCSC; uc009una.1; mouse.
DR   CTD; 27494; -.
DR   MGI; MGI:108440; Amot.
DR   eggNOG; roNOG10176; -.
DR   GeneTree; ENSGT00530000063846; -.
DR   HOGENOM; HBG445905; -.
DR   HOVERGEN; HBG066485; -.
DR   InParanoid; Q8VHG2; -.
DR   NextBio; 305584; -.
DR   ArrayExpress; Q8VHG2; -.
DR   Bgee; Q8VHG2; -.
DR   CleanEx; MM_AMOT; -.
DR   Genevestigator; Q8VHG2; -.
DR   GO; GO:0005884; C:actin filament; ISS:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR   GO; GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0043532; F:angiostatin binding; ISS:UniProtKB.
DR   GO; GO:0042074; P:cell migration involved in gastrulation; IMP:MGI.
DR   GO; GO:0006935; P:chemotaxis; IMP:MGI.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0040019; P:positive regulation of embryonic development; IMP:MGI.
DR   GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR   InterPro; IPR009114; Angiomotin.
DR   PANTHER; PTHR14826; Angiomotin; 1.
DR   PRINTS; PR01807; ANGIOMOTIN.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Coiled coil; Phosphoprotein;
KW   Tight junction.
FT   CHAIN         1   1126       Angiomotin.
FT                                /FTId=PRO_0000190669.
FT   COILED      408    668       Potential.
FT   COILED      700    730       Potential.
FT   MOTIF      1123   1126       PDZ-binding (By similarity).
FT   COMPBIAS    855    988       Ala-rich.
FT   MOD_RES     307    307       Phosphoserine (By similarity).
FT   MOD_RES     314    314       Phosphoserine (By similarity).
FT   MOD_RES     691    691       Phosphoserine.
FT   MOD_RES     693    693       Phosphoserine (By similarity).
FT   MOD_RES     696    696       Phosphothreonine (By similarity).
FT   MOD_RES     698    698       Phosphotyrosine (By similarity).
FT   MOD_RES    1103   1103       Phosphothreonine (By similarity).
FT   VAR_SEQ     805    853       VLLGGDYRVEPVPSTPSPVPPSTPLLSAHSKTGSRDCSTQT
FT                                ERGPESTK -> KEKESNRSKGTVTDLESVLTLLHTARKRD
FT                                NGPGSREENLESPLSMELDL (in isoform 2).
FT                                /FTId=VSP_027108.
FT   VAR_SEQ     854   1126       Missing (in isoform 2).
FT                                /FTId=VSP_027109.
FT   CONFLICT    298    298       S -> Y (in Ref. 3; AAL73436).
FT   CONFLICT    342    342       S -> P (in Ref. 3; AAL73436 and 2;
FT                                AAH57638).
FT   CONFLICT    409    409       M -> I (in Ref. 3; AAL73436 and 2;
FT                                AAH57638).
FT   CONFLICT    525    556       ENQREKEKLEAELATARSTNEDQRRHIEIRDQ -> FCQPY
FT                                NPAERKAEVRGGRFTIEAQRGHIKIRAR (in Ref. 3;
FT                                AAL73436).
FT   CONFLICT    565    566       VV -> W (in Ref. 3; AAL73436).
FT   CONFLICT    735    735       I -> M (in Ref. 3; AAL73436).
FT   CONFLICT    752    754       PSK -> RE (in Ref. 3; AAL73436).
SQ   SEQUENCE   1126 AA;  120915 MW;  530D84854E943CD4 CRC64;
     MRSSDDQPSG GTTVLQRLLQ EQLRYGNPSE NRSLLAIHQQ ATGNSSPFST GSGNQGPQND
     VLSSQDHHQQ QLVAHPARQE PQGQEIQSEN GVMEKQLSPR MQNNEELPTY EEAKVQSQYF
     RGQQHASVGA AFYVTGVTNQ KMRTEGRPSV QRLTPGKMHQ DEGLRDLKQG HVRSLSERLM
     QMSLATSGVK AHPPVTSAPL SPPQPNDLYK NATSSSEFYK AQGPPPSQHS LKGMEHRGPP
     PEYPFKGVPS QSVVCKSQEP GHFYSEHRLN QPGRTEGQLM RYQHPPEYGA ARATQDISSL
     SLSARNSQPH SPTSSLTAGA SSLPLLQSPP STRLPPGQHL VSNQGDHSAH LSRHQQHLLS
     SQSHQGDHYR HAQASLTSAQ QQPGEAYSAM PRAQQSASYQ PMPADPFAMV SRAQQMVEIL
     SDENRNLRQE LDGCYEKVAR LQKVETEIQR VSEAYENLVK SSSKREALEK AMRNKLEGEI
     RRMHDFNRDL RDRLETANKQ LAEKEYEGSE DTRKTISQLF AKHKENQREK EKLEAELATA
     RSTNEDQRRH IEIRDQALSN AQAKVVKLEE ELKKKQVYVD KVEKMQQALV QLQAACEKRE
     QLEHRLRTRL ERELESLRIQ QRQGNSQPTN ASEYNAAALM ELLREKEERI LALEADMTKW
     EQKYLEENVM RHFALDAAAT VAAQRDTTVI SHSPNTSYDT ALEARIQKEE EEILMANKRC
     LDMEGRIKTL HAQIIEKDAM IKVLQQRSRK EPSKTEQLSS MRPAKSLMSI SNAGSGLLAH
     SSTLTGAPIM EEKRDDKSWK GSLGVLLGGD YRVEPVPSTP SPVPPSTPLL SAHSKTGSRD
     CSTQTERGPE STKTAAVTPI SAPMAGPVAA AAPAAAINAT AATNTATAAT NTTIMVAAAP
     VAVAAVAAPA AAAATPSPAN AAALAAAAAP ATSVSAATSV SAANSISPAA PVAPAAVVPP
     AAPVSPAAAV QIPAAASLTP ATVSPTAATA TAAVAAATTA AITAAAAAAT TAIQVAPATS
     APVPSPASIP APATAQASAP TPTQASTPAP TEPPSPVPTP TPALVQTEGP ANPGASSGPR
     RLSTPNLMCN PDKPDAPAFH SSTLERKTPI QILGQEPDAE MVEYLI
//
ID   AGAP3_MOUSE             Reviewed;         910 AA.
AC   Q8VHH5; Q812F7;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 3;
DE            Short=AGAP-3;
DE   AltName: Full=CRAM-associated GTPase;
DE            Short=CRAG;
DE   AltName: Full=Centaurin-gamma-3;
DE            Short=Cnt-g3;
DE   AltName: Full=MR1-interacting protein;
DE            Short=MRIP-1;
GN   Name=Agap3; Synonyms=Centg3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, MUTAGENESIS OF SER-140 AND 368-LYS-ARG-369,
RP   ENZYME REGULATION, AND FUNCTION.
RX   PubMed=16461359; DOI=10.1083/jcb.200505079;
RA   Qin Q., Inatome R., Hotta A., Kojima M., Yamamura H., Hirai H.,
RA   Yoshizawa T., Tanaka H., Fukami K., Yanagi S.;
RT   "A novel GTPase, CRAG, mediates promyelocytic leukemia protein-
RT   associated nuclear body formation and degradation of expanded
RT   polyglutamine protein.";
RL   J. Cell Biol. 172:497-504(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Gong L., Wu K.;
RT   "Characterization of MRIP-1, a novel ADP-ribosylation factor GTPase-
RT   activating protein.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=15381706; DOI=10.1074/jbc.M410565200;
RA   Meurer S., Pioch S., Wagner K., Mueller-Esterl W., Gross S.;
RT   "AGAP1, a novel binding partner of nitric oxide-sensitive guanylyl
RT   cyclase.";
RL   J. Biol. Chem. 279:49346-49354(2004).
CC   -!- FUNCTION: GTPase-activating protein for the ADP ribosylation
CC       factor family (Potential). GTPase which may be involved in the
CC       degradation of expanded polyglutamine proteins through the
CC       ubiquitin-proteasome pathway.
CC   -!- ENZYME REGULATION: GTPase activity is stimulated by oxidative
CC       stress.
CC   -!- SUBUNIT: Interacts with PML. Interacts with expanded polyglutamine
CC       proteins (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Upon oxidative stress,
CC       translocates to PML nuclear bodies (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VHH5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VHH5-2; Sequence=VSP_018543, VSP_018544, VSP_018545;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in
CC       brain.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in the developing brain.
CC   -!- SIMILARITY: Belongs to the centaurin gamma-like family.
CC   -!- SIMILARITY: Contains 3 ANK repeats.
CC   -!- SIMILARITY: Contains 1 Arf-GAP domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
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DR   EMBL; AB078345; BAC55242.1; -; mRNA.
DR   EMBL; AF459091; AAL68640.1; -; mRNA.
DR   IPI; IPI00128319; -.
DR   IPI; IPI00330052; -.
DR   UniGene; Mm.250703; -.
DR   ProteinModelPortal; Q8VHH5; -.
DR   SMR; Q8VHH5; 125-288, 400-644, 662-879.
DR   STRING; Q8VHH5; -.
DR   PhosphoSite; Q8VHH5; -.
DR   PRIDE; Q8VHH5; -.
DR   Ensembl; ENSMUST00000024123; ENSMUSP00000024123; ENSMUSG00000023353.
DR   Ensembl; ENSMUST00000057281; ENSMUSP00000050807; ENSMUSG00000023353.
DR   UCSC; uc008wru.1; mouse.
DR   UCSC; uc008wrv.1; mouse.
DR   MGI; MGI:2183446; Agap3.
DR   GeneTree; ENSGT00600000084361; -.
DR   HOGENOM; HBG505242; -.
DR   HOVERGEN; HBG054045; -.
DR   InParanoid; Q8VHH5; -.
DR   OrthoDB; EOG479F6D; -.
DR   ArrayExpress; Q8VHH5; -.
DR   Bgee; Q8VHH5; -.
DR   Genevestigator; Q8VHH5; -.
DR   GermOnline; ENSMUSG00000023353; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR001164; ArfGAP.
DR   InterPro; IPR013684; MIRO-like.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR020849; Ras_small_GTPase.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF08477; Miro; 1.
DR   Pfam; PF00169; PH; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF57863; ArfGAP; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS51421; RAS; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ANK repeat; Cytoplasm; GTP-binding;
KW   GTPase activation; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Repeat; Zinc; Zinc-finger.
FT   CHAIN         1    910       Arf-GAP with GTPase, ANK repeat and PH
FT                                domain-containing protein 3.
FT                                /FTId=PRO_0000235916.
FT   DOMAIN      402    640       PH.
FT   DOMAIN      661    781       Arf-GAP.
FT   REPEAT      783    812       ANK 1.
FT   REPEAT      820    849       ANK 2.
FT   REPEAT      853    882       ANK 3.
FT   NP_BIND     133    140       GTP (Potential).
FT   NP_BIND     177    181       GTP (Potential).
FT   NP_BIND     233    236       GTP (Potential).
FT   ZN_FING     676    699       C4-type.
FT   REGION      119    410       Small GTPase-like.
FT   COMPBIAS      6     55       Gly-rich.
FT   MOD_RES     359    359       Phosphothreonine (By similarity).
FT   MOD_RES     361    361       Phosphothreonine (By similarity).
FT   MOD_RES     371    371       Phosphoserine (By similarity).
FT   MOD_RES     478    478       Phosphoserine (By similarity).
FT   VAR_SEQ      17     45       LAAPGGGGAAAQQLVCGGQFGGAGPGAGG -> RGC (in
FT                                isoform 2).
FT                                /FTId=VSP_018543.
FT   VAR_SEQ     376    395       SRKGADLDREKKAAECRVDS -> ICATVSNFSSTKRPFQL
FT                                LPN (in isoform 2).
FT                                /FTId=VSP_018544.
FT   VAR_SEQ     396    910       Missing (in isoform 2).
FT                                /FTId=VSP_018545.
FT   MUTAGEN     140    140       S->N: Abolishes interaction with PML.
FT   MUTAGEN     368    369       KR->EE: Abolishes translocation to PML
FT                                nuclear bodies upon oxidative stress.
SQ   SEQUENCE   910 AA;  97965 MW;  0778B420DFD7ACDB CRC64;
     MNFQAGGGQS PQQQQSLAAP GGGGAAAQQL VCGGQFGGAG PGAGGGGPSQ QLAGGPPQQF
     ALSNSAAIRA EIQRFESVHP NIYAIYDLIE RIEDLALQNQ IREHVISIED SFVNSQEWTL
     SRSVPELKVG IVGNLSSGKS ALVHRYLTGT YVQEESPEGG RFKKEIVVDG QSYLLLIRDE
     GGPPELQFAA WVDAVVFVFS LEDEISFQTV YNYFLRLCSF RNASEVPMVL VGTQDAISAA
     NPRVIDDSRA RKLSTDLKRC TYYETCATYG LNVERVFQDV AQKVVALRKK QQLAIGPCKS
     LPNSPSHSAV SAASIPAVHI NQATNGGSSA FSDYSSSVPS TPSISQRELR IETIAASSTP
     TPIRKQSKRR SNIFTSRKGA DLDREKKAAE CRVDSIGSGR AIPIKQGILL KRSGKSLNKE
     WKKKYVTLCD NGLLTYHPSL HDYMQNIHGK EIDLLRTTVK VPGKRLPRAT PTTAPGTSPR
     ANGLAMERSN TQLGGATGAP HSASSTSLHS ERPHSSAWAG SRPGPEGLHQ RSCSVSSTDQ
     WSEAAALPAS MQHPASGPAE SLSSSPKLEP PPSPHSNRKK HRGKKSTGTP RPDGPSSAAE
     EAEESFEFVV VSLTGQTWHF EASTAEEREL WVQSVQAQIL ASLQGCRSAK DKTRLGNQNT
     ALAVQAVRTV RGNSLCIDCE APNPDWASLN LGALMCIECS GIHRHLGAHL SRVRSLDLDD
     WPPELLAVMT AMGNALANSV WEGALDGYSK PGPEACREEK ERWIRAKYEQ KLFLAPLPSS
     DVPLGQQLLR AVVEDDLRLL VMLLAHGSKE EVNETYGDGD GRTALHLSSA MANVVFTQLL
     IWYGVDVRSR DARGLTPLAY ARRAGSQECA DILIQHGCPG EGCGLAPTPN REPANGTNPS
     AELHRSPSIL
//
ID   ADCY3_MOUSE             Reviewed;        1145 AA.
AC   Q8VHH7;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   11-JAN-2011, entry version 84.
DE   RecName: Full=Adenylate cyclase type 3;
DE            EC=4.6.1.1;
DE   AltName: Full=ATP pyrophosphate-lyase 3;
DE   AltName: Full=Adenylate cyclase type III;
DE            Short=AC-III;
DE   AltName: Full=Adenylate cyclase, olfactive type;
DE   AltName: Full=Adenylyl cyclase 3;
DE            Short=AC3;
GN   Name=Adcy3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Pasternak S., Neumann P.E.;
RT   "Sequence of mouse Adcy3.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mediates odorant detection (possibly) via modulation of
CC       intracellular cAMP concentration (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate.
CC   -!- COFACTOR: Binds 2 magnesium ions per subunit (By similarity).
CC   -!- ENZYME REGULATION: Activated by calcium/calmodulin (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl
CC       cyclase family.
CC   -!- SIMILARITY: Contains 2 guanylate cyclase domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF458089; AAL59384.1; -; mRNA.
DR   IPI; IPI00128323; -.
DR   UniGene; Mm.480743; -.
DR   ProteinModelPortal; Q8VHH7; -.
DR   SMR; Q8VHH7; 307-493, 916-1121.
DR   MINT; MINT-7290275; -.
DR   STRING; Q8VHH7; -.
DR   PhosphoSite; Q8VHH7; -.
DR   PRIDE; Q8VHH7; -.
DR   Ensembl; ENSMUST00000020984; ENSMUSP00000020984; ENSMUSG00000020654.
DR   UCSC; uc007mxm.1; mouse.
DR   MGI; MGI:99675; Adcy3.
DR   HOVERGEN; HBG050458; -.
DR   InParanoid; Q8VHH7; -.
DR   BRENDA; 4.6.1.1; 244.
DR   NextBio; 356544; -.
DR   ArrayExpress; Q8VHH7; -.
DR   Bgee; Q8VHH7; -.
DR   CleanEx; MM_ADCY3; -.
DR   Genevestigator; Q8VHH7; -.
DR   GermOnline; ENSMUSG00000020654; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; TAS:MGI.
DR   GO; GO:0004016; F:adenylate cyclase activity; TAS:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:MGI.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR018297; A/G_cyclase_CS.
DR   Gene3D; G3DSA:3.30.70.1230; A/G_cyclase; 2.
DR   Pfam; PF00211; Guanylate_cyc; 2.
DR   SMART; SM00044; CYCc; 2.
DR   SUPFAM; SSF55073; A/G_cyclase; 2.
DR   PROSITE; PS00452; GUANYLATE_CYCLASE_1; 2.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Calmodulin-binding; cAMP biosynthesis; Glycoprotein;
KW   Lyase; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Olfaction; Repeat; Sensory transduction; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   1145       Adenylate cyclase type 3.
FT                                /FTId=PRO_0000195688.
FT   TOPO_DOM      1     79       Cytoplasmic (Potential).
FT   TRANSMEM     80    100       Helical; (Potential).
FT   TRANSMEM    105    125       Helical; (Potential).
FT   TRANSMEM    139    159       Helical; (Potential).
FT   TRANSMEM    173    193       Helical; (Potential).
FT   TRANSMEM    226    246       Helical; (Potential).
FT   TRANSMEM    381    401       Helical; (Potential).
FT   TOPO_DOM    402    631       Cytoplasmic (Potential).
FT   TRANSMEM    632    652       Helical; (Potential).
FT   TRANSMEM    663    683       Helical; (Potential).
FT   TRANSMEM    707    727       Helical; (Potential).
FT   TRANSMEM    753    773       Helical; (Potential).
FT   TRANSMEM    774    794       Helical; (Potential).
FT   TRANSMEM    834    854       Helical; (Potential).
FT   TOPO_DOM    855   1145       Cytoplasmic (Potential).
FT   METAL       324    324       Magnesium 1 (By similarity).
FT   METAL       324    324       Magnesium 2 (By similarity).
FT   METAL       325    325       Magnesium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       368    368       Magnesium 1 (By similarity).
FT   METAL       368    368       Magnesium 2 (By similarity).
FT   CARBOHYD    735    735       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   1145 AA;  129042 MW;  F6BD93A7AAE47915 CRC64;
     MPRNQGFSDP EYSAEYSAEY SVSLPSDPDR GVGRTHEISV RNSGSCLCLP RFMRLTFVPE
     SLENLYQTYF KRQRHETLLV LVVFAALFDC YVVVMCAVVF SSDKLAPLMV AGFGLVLDII
     LFVLCKKGLL PDRVSRKVVP YLLWLLISAQ ILSYLGLNFS RAHAASDTVG WQAFFVFSFF
     ITLPLSLSPI VIISVVSCVV HTLVLGVTVA QQQQDELEGM QLLREILANV FLYLCAIIVG
     IMSYYMADRK HRKAFLEARQ SLEVKMNLEE QSQQQENLML SILPKHVADE MLKDMKKDES
     QKDQQQFNTM YMYRHENVSI LFADIVGFTQ LSSACSAQEL VKLLNELFAR FDKLAAKYHQ
     LRIKILGDCY YCICGLPDYR EDHAVCSILM GLAMVEAISY VREKTKTGVD MRVGVHTGTV
     LGGVLGQKRW QYDVWSTDVT VANKMEAGGI PGRVHISQST MDCLKGEFDV EPGDGGSRCD
     YLDEKGIETY LIIASKPEVK KTAQNGLNGS AVPNGAPASS KPSSPALIET KEPNGSAHAS
     GSTSEEAEEQ EAQADNPSFP NPRRRLRLQD LADRVVDASE DEHELNQLLN EALLERESAQ
     VVKKRNTFLL TMRFMDPEME TRYSVEKEKQ SGAAFSCSCV VLFCTAMVEI LIDPWLMTNY
     VTFVVGEVLL LILTICSMAA IFPRSFPKKL VAFSSWIDRT RWARNTWAML AIFILVMANV
     VDMLSCLQYY MGPYNMTAGM ELDGGCMENP KYYNYVAVLS LIATIMLVQV SHMVKLTLML
     LVTGAVTALN LYAWCPVFDE YDHKRFQEKD SPMVALEKMQ VLATPGLNGT DSMLLLVPSK
     YSMTVMMFVM MLSFYYFSRH VEKLARTLFL WKIEVHDQKE RVYEMRRWNE ALVTNMLPEH
     VARHFLGSKK RDEELYSQSY DEIGVMFASL PNFADFYTEE SINNGGIECL RFLNEIISDF
     DSLLDNPKFR VITKIKTIGS TYMAASGVTP DVNTNGFTSS SKEEKSDKER WQHLADLADF
     ALAMKDTLTN INNQSFNNFM LRIGMNKGGV LAGVIGARKP HYDIWGNTVN VASRMESTGV
     MGNIQVVEET QVILREYGFR FVRRGPIFVK GKGELLTFFL KGRDRPAAFP NGSSVTLPHQ
     VVDNP
//
ID   WASF3_MOUSE             Reviewed;         501 AA.
AC   Q8VHI6;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Wiskott-Aldrich syndrome protein family member 3;
DE            Short=WASP family protein member 3;
DE   AltName: Full=Protein WAVE-3;
GN   Name=Wasf3; Synonyms=Wave3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12856283; DOI=10.1007/s00335-002-2247-7;
RA   Sossey-Alaoui K., Head K., Nowak N., Cowell J.K.;
RT   "Genomic organization and expression profile of the human and mouse
RT   WAVE gene family.";
RL   Mamm. Genome 14:314-322(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Downstream effector molecules involved in the
CC       transmission of signals from tyrosine kinase receptors and small
CC       GTPases to the actin cytoskeleton (By similarity).
CC   -!- SUBUNIT: Binds actin and the Arp2/3 complex (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC   -!- DOMAIN: Binds the Arp2/3 complex through the C-terminal region and
CC       actin through verprolin homology (VPH) domain.
CC   -!- SIMILARITY: Belongs to the SCAR/WAVE family.
CC   -!- SIMILARITY: Contains 1 WH2 domain.
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DR   EMBL; AF454703; AAL51033.1; -; mRNA.
DR   EMBL; BC027038; AAH27038.1; -; mRNA.
DR   IPI; IPI00128341; -.
DR   RefSeq; NP_660137.1; NM_145155.3.
DR   UniGene; Mm.472750; -.
DR   ProteinModelPortal; Q8VHI6; -.
DR   SMR; Q8VHI6; 21-208, 438-486.
DR   STRING; Q8VHI6; -.
DR   PhosphoSite; Q8VHI6; -.
DR   PRIDE; Q8VHI6; -.
DR   Ensembl; ENSMUST00000016143; ENSMUSP00000016143; ENSMUSG00000029636.
DR   GeneID; 245880; -.
DR   KEGG; mmu:245880; -.
DR   UCSC; uc009anf.1; mouse.
DR   CTD; 245880; -.
DR   MGI; MGI:2658986; Wasf3.
DR   GeneTree; ENSGT00550000074443; -.
DR   HOGENOM; HBG715875; -.
DR   HOVERGEN; HBG058482; -.
DR   InParanoid; Q8VHI6; -.
DR   OMA; DSTVEEX; -.
DR   PhylomeDB; Q8VHI6; -.
DR   NextBio; 386984; -.
DR   ArrayExpress; Q8VHI6; -.
DR   Bgee; Q8VHI6; -.
DR   CleanEx; MM_WASF3; -.
DR   Genevestigator; Q8VHI6; -.
DR   GermOnline; ENSMUSG00000029636; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR003124; WH2_actin-bd.
DR   Pfam; PF02205; WH2; 1.
DR   SMART; SM00246; WH2; 1.
DR   PROSITE; PS51082; WH2; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton.
FT   CHAIN         1    501       Wiskott-Aldrich syndrome protein family
FT                                member 3.
FT                                /FTId=PRO_0000188997.
FT   DOMAIN      439    456       WH2.
FT   COILED       57     93       Potential.
FT   COILED      162    206       Potential.
FT   COMPBIAS    304    310       Poly-Pro.
FT   COMPBIAS    343    350       Poly-Pro.
FT   COMPBIAS    395    410       Poly-Pro.
SQ   SEQUENCE   501 AA;  55204 MW;  FD30EEC6867D4AF1 CRC64;
     MPLVKRNIEP RHLCRGALPE GVTSELECVT NSTLAAIIRQ LSSLSKHAED IFGELFNEAN
     NFYIRANSLQ DRIDRLAVKV TQLDSTVEEV SLQDINMKKA FKSSTIQDQQ VVSKNSIPNP
     VADIYNQSDK PPPLSILTPY RDDKKDGLKF YTDPSYFFDL WKEKMLQDTE DKRKEKRRQK
     EQKRVDGTTR EVKKVRKARN RRQEWNMMAY DKELRPDNRL SQSVHHGASS EGSLSPDTRS
     HTSDVTDYSY PATPNHALQA QPATPSYTAG DAPLHGTTNQ GAEHEYRPSS ASARHMALNR
     PQQPPPPPPP QAPEGSQAST SVAPADYGML PAQIIEYYSP SGPPPPPPPP MIPSAQTAFV
     SPLQMPTQPP FPASAVSTYP TPPHQPSTGL LATAPPPPGP PPPPPGPPGP SSLSSSPMHG
     PPVAEAKRPE PAQPPISDAR SDLLAAIRMG IQLKKVQEQR EQEAKREPVG NDVATILSRR
     IAVEYSDSDD DSEFDENDWS D
//
ID   CSKI2_MOUSE             Reviewed;        1201 AA.
AC   Q8VHK1; Q6ZPX1; Q7TS77;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Caskin-2;
GN   Name=Caskin2; Synonyms=Kiaa1139;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=22035661; PubMed=12040031;
RA   Tabuchi K., Biederer T., Butz S., Suedhof T.C.;
RT   "CASK participates in alternative tripartite complexes in which Mint 1
RT   competes for binding with Caskin 1, a novel CASK-binding protein.";
RL   J. Neurosci. 22:4264-4273(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403 AND SER-409, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SUBUNIT: May not bind CASK.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Contains 6 ANK repeats.
CC   -!- SIMILARITY: Contains 2 SAM (sterile alpha motif) domains.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98107.1; Type=Erroneous initiation;
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DR   EMBL; AF451978; AAL49759.1; -; mRNA.
DR   EMBL; AK129297; BAC98107.1; ALT_INIT; mRNA.
DR   EMBL; BC053083; AAH53083.1; -; mRNA.
DR   IPI; IPI00380698; -.
DR   RefSeq; NP_542374.2; NM_080643.2.
DR   UniGene; Mm.383737; -.
DR   ProteinModelPortal; Q8VHK1; -.
DR   SMR; Q8VHK1; 4-283, 490-618.
DR   STRING; Q8VHK1; -.
DR   PhosphoSite; Q8VHK1; -.
DR   PRIDE; Q8VHK1; -.
DR   Ensembl; ENSMUST00000041684; ENSMUSP00000041328; ENSMUSG00000034471.
DR   GeneID; 140721; -.
DR   KEGG; mmu:140721; -.
DR   UCSC; uc007mip.1; mouse.
DR   CTD; 140721; -.
DR   MGI; MGI:2157062; Caskin2.
DR   eggNOG; roNOG05897; -.
DR   GeneTree; ENSGT00530000063104; -.
DR   HOGENOM; HBG717177; -.
DR   HOVERGEN; HBG051133; -.
DR   InParanoid; Q8VHK1; -.
DR   OrthoDB; EOG415GCP; -.
DR   NextBio; 369947; -.
DR   ArrayExpress; Q8VHK1; -.
DR   Bgee; Q8VHK1; -.
DR   CleanEx; MM_CASKIN2; -.
DR   Genevestigator; Q8VHK1; -.
DR   GermOnline; ENSMUSG00000034471; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 2.
DR   Pfam; PF00023; Ank; 5.
DR   Pfam; PF00536; SAM_1; 2.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00248; ANK; 7.
DR   SMART; SM00454; SAM; 2.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF47769; SAM_homology; 2.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
DR   PROSITE; PS50105; SAM_DOMAIN; 2.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Cytoplasm; Phosphoprotein; Repeat; SH3 domain.
FT   CHAIN         1   1201       Caskin-2.
FT                                /FTId=PRO_0000066984.
FT   REPEAT       48     77       ANK 1.
FT   REPEAT       81    110       ANK 2.
FT   REPEAT      114    143       ANK 3.
FT   REPEAT      147    176       ANK 4.
FT   REPEAT      188    217       ANK 5.
FT   REPEAT      220    249       ANK 6.
FT   DOMAIN      281    347       SH3.
FT   DOMAIN      488    551       SAM 1.
FT   DOMAIN      557    621       SAM 2.
FT   COMPBIAS    686   1140       Pro-rich.
FT   MOD_RES     253    253       Phosphotyrosine.
FT   MOD_RES     336    336       Phosphotyrosine (By similarity).
FT   MOD_RES     384    384       Phosphotyrosine (By similarity).
FT   MOD_RES     393    393       Phosphoserine (By similarity).
FT   MOD_RES     396    396       Phosphoserine (By similarity).
FT   MOD_RES     403    403       Phosphoserine.
FT   MOD_RES     406    406       Phosphoserine (By similarity).
FT   MOD_RES     409    409       Phosphoserine.
FT   MOD_RES     412    412       Phosphoserine (By similarity).
FT   MOD_RES     471    471       Phosphoserine.
FT   MOD_RES     855    855       Phosphoserine (By similarity).
FT   MOD_RES     875    875       Phosphoserine (By similarity).
FT   MOD_RES     879    879       Phosphoserine (By similarity).
FT   CONFLICT     29     29       A -> T (in Ref. 1; AAL49759).
FT   CONFLICT    371    371       S -> P (in Ref. 1; AAL49759).
FT   CONFLICT    374    381       AADDPLPS -> PAEEPPHP (in Ref. 1;
FT                                AAL49759).
FT   CONFLICT    444    444       S -> G (in Ref. 1; AAL49759).
FT   CONFLICT    448    448       G -> V (in Ref. 1; AAL49759).
FT   CONFLICT    454    454       A -> P (in Ref. 1; AAL49759).
FT   CONFLICT    457    457       P -> L (in Ref. 1; AAL49759).
FT   CONFLICT    627    627       H -> Q (in Ref. 1; AAL49759).
FT   CONFLICT   1141   1141       S -> G (in Ref. 3; AAH53083).
SQ   SEQUENCE   1201 AA;  126809 MW;  A4F0742E79547DA7 CRC64;
     MGREQDLILA VKNGDVTCVQ KLVAKVKAAK TKLLGSTKRL NINYQDADGF SALHHAALGG
     SLELIALLLE AQATVDIKDS NGMRPLHYAA WQGRLEPVRL LLRASAAVNA ASLDGQIPLH
     LAAQYGHYEV SEMLLQHQSN PCLVNKLKKT PLDLACEFGR LKVAQLLLNS HLCVALLEGE
     AKDPCDPNYT TPLHLAAKNG HREVIRQLLK AGIEINRQTK TGTALHEAAL YGKTEVVRLL
     LEGGVDVNIR NTYNQTALDI VNQFTTSQAS REIKQLLREA SGILKVRALK DFWNLHDPTA
     LNVRAGDVIT VLEQHPDGRW KGHIHESQRG TDRVGYFPPG IVEVVSKRVG IPVARLPSAP
     TPLRPSFSRI SQPAADDPLP SVPYGQLPRV GLSPDSPAGD RNSVGSEGSV GSIRSAGSGQ
     SSEGTNGHGT GLLIENAQPL PSASEDQGLP GLHAPSPADN LSHRPLAGYR SGEIFTQDVR
     PEQLLEGKDA QAIHNWLSEF QLEGYTAHFL QAGYDVPTIS RMTPEDLTAI GVTKPGHRKK
     IASEIAQLSI AEWLPNYIPV DLLEWLCALG LPQYHKQLVS SGYDSMGLVA DLTWEELQEI
     GVNKLGHQKK LMLGVKRLAE LRRGLLHGEA LGEGGRRMTR GPELMAIEGL ENGEGPTTAG
     PRLLTFQGSE LSPELQAAMA GGGSEPLPLP PARSPSQESI GARSRGSGHS QEQPVPQPSV
     GDPSAPQERN LPEGTERPSK LCSPLPGQGP APYVFMCPQN LPSSPAPGPP PGVPRAFSYL
     AGSPAAPPDP PRPKRRSHSL SRPGPAEGEA EGEAEGPVGS ALGSYATLTR RPGRSTLART
     SPSLTPTRGT PRSQSFALRA RRKGPPPPPP KRLSSVSGST EPPSLDGTSG PKEGATGPRR
     RTLSEPTGPS ESPGPSAPTG PVSDTEEEPG PEGTPPSRGS SGEGLPFAEE GNLTIKQRPK
     PAGPPPRETP VPPGLDFNLT ESDTVKRRPK CKEREPLQTA LLAFGVVGSD TPGPSNPLST
     QAPCDPPSAS SNPPQRSEPS VLPSQGTSAS SLSSVTQSPG HPGPSAGPAL ANSTGSKPNV
     ETEPPAPPAA LLKVPGAGTA PKPVSVACTQ LAFSGPKLAP RLGPRPVPPP RPENTGPVCP
     SRAQQRLEQT SSSLEAALRA AEKSIGTEER DGPTGTSTKH ILDDISTMFD ALADQLDAML
     D
//
ID   MLC1_MOUSE              Reviewed;         382 AA.
AC   Q8VHK5;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Membrane protein MLC1;
GN   Name=Mlc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RA   Steinke V., Meyer J., Syagailo Y.V., Ortega G., Moessner R.,
RA   Schmitt A., Lesch K.P.;
RT   "The genomic organization of the murine Kiaa0027 (Wkl1, Mlc1) gene.";
RL   Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pituitary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be a transporter. May act as a non-selective
CC       neuronal cation channel.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
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DR   EMBL; AF449425; AAL66020.1; -; mRNA.
DR   EMBL; AK030396; BAC26941.1; -; mRNA.
DR   EMBL; BC024719; AAH24719.1; -; mRNA.
DR   IPI; IPI00128391; -.
DR   RefSeq; NP_573504.1; NM_133241.2.
DR   UniGene; Mm.32780; -.
DR   ProteinModelPortal; Q8VHK5; -.
DR   STRING; Q8VHK5; -.
DR   PhosphoSite; Q8VHK5; -.
DR   PRIDE; Q8VHK5; -.
DR   Ensembl; ENSMUST00000042594; ENSMUSP00000047667; ENSMUSG00000035805.
DR   Ensembl; ENSMUST00000109368; ENSMUSP00000104993; ENSMUSG00000035805.
DR   GeneID; 170790; -.
DR   KEGG; mmu:170790; -.
DR   UCSC; uc007xev.1; mouse.
DR   CTD; 170790; -.
DR   MGI; MGI:2157910; Mlc1.
DR   GeneTree; ENSGT00390000015442; -.
DR   HOVERGEN; HBG049239; -.
DR   InParanoid; Q8VHK5; -.
DR   OrthoDB; EOG4QZ7MP; -.
DR   NextBio; 370431; -.
DR   ArrayExpress; Q8VHK5; -.
DR   Bgee; Q8VHK5; -.
DR   Genevestigator; Q8VHK5; -.
DR   GermOnline; ENSMUSG00000035805; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Ion transport; Ionic channel; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    382       Membrane protein MLC1.
FT                                /FTId=PRO_0000096498.
FT   TRANSMEM     58     78       Helical; (Potential).
FT   TRANSMEM     88    107       Helical; (Potential).
FT   TRANSMEM    117    137       Helical; (Potential).
FT   TRANSMEM    148    168       Helical; (Potential).
FT   TRANSMEM    205    225       Helical; (Potential).
FT   TRANSMEM    234    254       Helical; (Potential).
FT   TRANSMEM    263    283       Helical; (Potential).
FT   TRANSMEM    309    329       Helical; (Potential).
FT   COMPBIAS    178    181       Poly-Lys.
SQ   SEQUENCE   382 AA;  41596 MW;  0F5573B1F89327E0 CRC64;
     MTREGQFREE LGYDRMPTLE RGRQDAGRQD PGSYTPDSKP KDLQLSKRLP PCFSYKTWVF
     SVLMGSCLLV TSGFSLYLGN VFPSEMDYLR CAAGSCIPSA IVSFAVGRRN VSAIPNFQIL
     FVSTFAVTTT CLIWFGCKLI LNPSAININF NLILLLLLEL LMAATVIISA RSSEEPCKKK
     KGSISDGSNI LDEVTFPARV LKSYSVVEVI AGVSAVLGGV IALNVEEAVS GPHLSVTFFW
     ILVACFPSAI ASHVTAECPS KCLVEVLIAI SSLTSPLLFT ASGYLSFSVM RVVEIFKDYP
     PAIKSYDVLL LLLLLLLLLQ GGLNTGTAIQ CVSFKVSARL QAASWDPQSC PQERPAGEVV
     RGPLKEFDKE KAWRAVVVQM AQ
//
ID   SETD7_MOUSE             Reviewed;         366 AA.
AC   Q8VHL1; Q6ZPJ6; Q80UU3; Q8C7Y6;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Histone-lysine N-methyltransferase SETD7;
DE            EC=2.1.1.43;
DE   AltName: Full=Histone H3-K4 methyltransferase SETD7;
DE            Short=H3-K4-HMTase SETD7;
DE   AltName: Full=SET domain-containing protein 7;
DE   AltName: Full=SET7/9;
GN   Name=Setd7; Synonyms=Kiaa1717, Set7, Set9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreas;
RX   MEDLINE=21638669; PubMed=11779497; DOI=10.1016/S1097-2765(01)00405-1;
RA   Wang H., Cao R., Xia L., Erdjument-Bromage H., Borchers C., Tempst P.,
RA   Zhang Y.;
RT   "Purification and functional characterization of a histone H3-lysine
RT   4-specific methyltransferase.";
RL   Mol. Cell 8:1207-1217(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and NOD; TISSUE=Brain, and Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129/Sv X 129SvCp; TISSUE=Embryonic stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION.
RX   PubMed=12711597; DOI=10.1074/jbc.M303423200;
RA   Chakrabarti S.K., Francis J., Ziesmann S.M., Garmey J.C.,
RA   Mirmira R.G.;
RT   "Covalent histone modifications underlie the developmental regulation
RT   of insulin gene transcription in pancreatic beta cells.";
RL   J. Biol. Chem. 278:23617-23623(2003).
RN   [6]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=15975555; DOI=10.1016/j.bbrc.2005.06.003;
RA   Jeong K.S., Park J.H., Lee S.;
RT   "The analysis of X-chromosome inactivation-related gene expression
RT   from single mouse embryo with sex-determination.";
RL   Biochem. Biophys. Res. Commun. 333:803-807(2005).
CC   -!- FUNCTION: Histone methyltransferase that specifically
CC       monomethylates 'Lys-4' of histone H3. H3 'Lys-4' methylation
CC       represents a specific tag for epigenetic transcriptional
CC       activation. Plays a central role in the transcriptional activation
CC       of genes such as collagenase or insulin. Recruited by IPF1/PDX-1
CC       to the insulin promoter, leading to activate transcription. Has
CC       also methyltransferase activity toward non-histone proteins such
CC       as p53/TP53, TAF10, and possibly TAF7 by recognizing and binding
CC       the [KR]-[STA]-K in substrate proteins. Monomethylates 'Lys-189'
CC       of TAF10, leading to increase the affinity of TAF10 for RNA
CC       polymerase II. Monomethylates 'Lys-372' of p53/TP53, stabilizing
CC       p53/TP53 and increasing p53/TP53-mediated transcriptional
CC       activation.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC   -!- SUBUNIT: Interacts with IPF1/PDX-1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Chromosome (By
CC       similarity).
CC   -!- DEVELOPMENTAL STAGE: Expressed during all pre-implementation
CC       stages in both male and female embryos.
CC   -!- DOMAIN: The SET domain is necessary but not sufficient for histone
CC       methyltransferase activity (By similarity).
CC   -!- SIMILARITY: Belongs to the histone-lysine methyltransferase
CC       family. SET7 subfamily.
CC   -!- SIMILARITY: Contains 3 MORN repeats.
CC   -!- SIMILARITY: Contains 1 SET domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98238.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF448509; AAL56578.1; -; mRNA.
DR   EMBL; AK129428; BAC98238.1; ALT_INIT; mRNA.
DR   EMBL; AK048924; BAC33493.1; -; mRNA.
DR   EMBL; AK147422; BAE27903.1; -; mRNA.
DR   EMBL; AK147413; BAE27897.1; -; mRNA.
DR   EMBL; AK147667; BAE28059.1; -; mRNA.
DR   EMBL; AK170161; BAE41607.1; -; mRNA.
DR   EMBL; BC050190; AAH50190.1; -; mRNA.
DR   IPI; IPI00331236; -.
DR   RefSeq; NP_542983.3; NM_080793.5.
DR   UniGene; Mm.192111; -.
DR   ProteinModelPortal; Q8VHL1; -.
DR   SMR; Q8VHL1; 29-344.
DR   STRING; Q8VHL1; -.
DR   PRIDE; Q8VHL1; -.
DR   Ensembl; ENSMUST00000037141; ENSMUSP00000043492; ENSMUSG00000037111.
DR   GeneID; 73251; -.
DR   KEGG; mmu:73251; -.
DR   CTD; 73251; -.
DR   MGI; MGI:1920501; Setd7.
DR   eggNOG; roNOG10855; -.
DR   GeneTree; ENSGT00390000004827; -.
DR   HOGENOM; HBG717366; -.
DR   HOVERGEN; HBG028309; -.
DR   InParanoid; Q8VHL1; -.
DR   OMA; GSSVYHF; -.
DR   OrthoDB; EOG43XV3K; -.
DR   BRENDA; 2.1.1.43; 244.
DR   NextBio; 337766; -.
DR   ArrayExpress; Q8VHL1; -.
DR   Bgee; Q8VHL1; -.
DR   Genevestigator; Q8VHL1; -.
DR   GermOnline; ENSMUSG00000037111; Mus musculus.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0018027; P:peptidyl-lysine dimethylation; ISS:UniProtKB.
DR   GO; GO:0018026; P:peptidyl-lysine monomethylation; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR017155; Hist-Lys_N-MeTrfase_SET.
DR   InterPro; IPR003409; MORN.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF02493; MORN; 4.
DR   Pfam; PF00856; SET; 1.
DR   PIRSF; PIRSF037249; Histone_Lys_mtfrase_SET; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   2: Evidence at transcript level;
KW   Activator; Chromatin regulator; Chromosome; Methyltransferase;
KW   Nucleus; Repeat; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    366       Histone-lysine N-methyltransferase SETD7.
FT                                /FTId=PRO_0000186055.
FT   REPEAT       36     58       MORN 1.
FT   REPEAT       59     81       MORN 2.
FT   REPEAT      106    128       MORN 3.
FT   DOMAIN      215    340       SET.
FT   REGION      226    228       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   REGION      256    258       Substrate binding (By similarity).
FT   REGION      266    268       Substrate binding (By similarity).
FT   REGION      296    297       S-adenosyl-L-methionine binding (By
FT                                similarity).
FT   COMPBIAS     51     54       Poly-Phe.
FT   BINDING     245    245       Substrate (By similarity).
FT   BINDING     317    317       Substrate (By similarity).
FT   BINDING     335    335       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     356    356       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
FT   CONFLICT     77     77       E -> V (in Ref. 4; AAH50190).
FT   CONFLICT    165    165       L -> I (in Ref. 1; AAL56578).
SQ   SEQUENCE   366 AA;  40506 MW;  C826EAFCB4B9D345 CRC64;
     MDSDDEVVEE AVEGHLDDDG LPHGFCTVTY SSTDRFEGNF VHGEKNGRGK FFFFDGSTLE
     GYYVDDALQG QGVYTYEDGG VLQGTYVDGE LNGPAQEYDS DGRLIFKGQY KDNNRHGVCW
     IHYPDGGSLV GEVNEDGEMT GEKIAYVYPD QRTALYGKFI DGEMLEGKLA TLMATEEGRP
     HFEVTSGSSV YHFDKSTSSC ISSDALLPDP YESERVYVAD SLISSAGEGL FSKVAVGPNT
     VMSFYNGVRI THQEVDSRDW ALNGNTLSLD EETVIDVPEP YNHVSKYCAS LGHKANHSFT
     PNCVYDLFVH PRFGPIKCIR TLRAVEAEEE LTVAYGYDHS PPGKSGPEAP EWYQVELKAF
     QATQQK
//
ID   GPR98_MOUSE             Reviewed;        6298 AA.
AC   Q8VHN7; Q6ZQ69; Q810D2; Q810D3; Q91ZS0; Q91ZS1;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=G-protein coupled receptor 98;
DE   AltName: Full=Monogenic audiogenic seizure susceptibility protein 1;
DE   AltName: Full=Neurepin;
DE   AltName: Full=Very large G-protein coupled receptor 1;
DE   Flags: Precursor;
GN   Name=Gpr98; Synonyms=Kiaa0686, Mass1, Vlgr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND INVOLVEMENT IN
RP   MONOGENIC AUDIOGENIC SEIZURE SUSCEPTIBILITY.
RC   STRAIN=C57BL/6;
RX   MEDLINE=21432018; PubMed=11545713; DOI=10.1016/S0896-6273(01)00397-X;
RA   Skradski S.L., Clark A.M., Jiang H., White H.S., Fu Y., Ptacek L.J.;
RT   "A novel gene causing a mendelian audiogenic mouse epilepsy.";
RL   Neuron 31:537-544(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DEVELOPMENTAL STAGE.
RC   STRAIN=129/Sv;
RX   MEDLINE=21634833; PubMed=11606593; DOI=10.1074/jbc.M108929200;
RA   McMillan D.R., Kayes-Wandover K.M., Richardson J.A., White P.C.;
RT   "Very large G protein-coupled receptor-1, the largest known cell
RT   surface protein, is highly expressed in the developing central nervous
RT   system.";
RL   J. Biol. Chem. 277:785-792(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 5), AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=15606908; DOI=10.1111/j.1471-4159.2004.02875.x;
RA   Yagi H., Takamura Y., Yoneda T., Konno D., Akagi Y., Yoshida K.,
RA   Sato M.;
RT   "Vlgr1 knockout mice show audiogenic seizure susceptibility.";
RL   J. Neurochem. 92:191-202(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4816-6298.
RC   TISSUE=Pancreatic islet;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [5]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Receptor that may have an important role in the
CC       development of the central nervous system.
CC   -!- SUBUNIT: Interacts with WHRN. Interacts with PDZD7 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SUBCELLULAR LOCATION: Isoform 4: Secreted.
CC   -!- SUBCELLULAR LOCATION: Isoform 5: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q8VHN7-1; Sequence=Displayed;
CC       Name=2; Synonyms=Mass1.2;
CC         IsoId=Q8VHN7-2; Sequence=VSP_017952, VSP_017955, VSP_017959,
CC                                  VSP_017960;
CC       Name=3; Synonyms=Mass1.3;
CC         IsoId=Q8VHN7-3; Sequence=VSP_017951, VSP_017958, VSP_017959,
CC                                  VSP_017960;
CC       Name=4; Synonyms=Neurepin-2, Vlgr1e;
CC         IsoId=Q8VHN7-4; Sequence=VSP_017956, VSP_017957;
CC         Note=Secreted;
CC       Name=5; Synonyms=Neurepin-1, Vlgr1d;
CC         IsoId=Q8VHN7-5; Sequence=VSP_017953, VSP_017954;
CC         Note=Secreted;
CC   -!- DEVELOPMENTAL STAGE: High level expression restricted to the
CC       developing central nervous system and eye. At mid-gestation
CC       expression is prominent in the ventricular zone and in the eye. At
CC       late gestation expression declines.
CC   -!- DISRUPTION PHENOTYPE: Mice display audiogenic epilepsy. Audiogenic
CC       epilepsy syndrome is an autosomal recessive mutation,
CC       characterized by generalized self-sustained convulsive seizures in
CC       which acoustics stimulations evoke wild running, tonic flexion and
CC       extesion pigmentosa with sensorineural deafness. They are induced
CC       by exposing animals to a loud noise during the early stages of
CC       their development.
CC   -!- SIMILARITY: Contains 35 Calx-beta domains.
CC   -!- SIMILARITY: Contains 6 EAR repeats.
CC   -!- SIMILARITY: Contains 1 GPS domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF405693; AAL06013.1; -; mRNA.
DR   EMBL; AF405694; AAL06014.1; -; mRNA.
DR   EMBL; AF435926; AAL30812.1; -; mRNA.
DR   EMBL; AB086166; BAC66505.2; -; mRNA.
DR   EMBL; AB086167; BAC66506.1; -; mRNA.
DR   EMBL; AK129190; BAC98000.3; -; mRNA.
DR   IPI; IPI00754998; -.
DR   IPI; IPI00756354; -.
DR   IPI; IPI00757356; -.
DR   IPI; IPI00876506; -.
DR   IPI; IPI00956931; -.
DR   UniGene; Mm.288694; -.
DR   ProteinModelPortal; Q8VHN7; -.
DR   STRING; Q8VHN7; -.
DR   PRIDE; Q8VHN7; -.
DR   Ensembl; ENSMUST00000095585; ENSMUSP00000093245; ENSMUSG00000069170.
DR   Ensembl; ENSMUST00000109565; ENSMUSP00000105193; ENSMUSG00000069170.
DR   UCSC; uc007rhn.1; mouse.
DR   UCSC; uc007rho.1; mouse.
DR   UCSC; uc007rhp.1; mouse.
DR   UCSC; uc007rhs.1; mouse.
DR   UCSC; uc007rht.1; mouse.
DR   MGI; MGI:1274784; Gpr98.
DR   eggNOG; roNOG06976; -.
DR   GeneTree; ENSGT00390000006373; -.
DR   HOGENOM; HBG356442; -.
DR   HOVERGEN; HBG081572; -.
DR   InParanoid; Q8VHN7; -.
DR   OrthoDB; EOG4Q58NG; -.
DR   ArrayExpress; Q8VHN7; -.
DR   Bgee; Q8VHN7; -.
DR   CleanEx; MM_GPR98; -.
DR   Genevestigator; Q8VHN7; -.
DR   GermOnline; ENSMUSG00000069170; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0002142; C:stereocilia ankle link complex; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; NAS:UniProtKB.
DR   GO; GO:0017022; F:myosin binding; IPI:MGI.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   GO; GO:0016337; P:cell-cell adhesion; NAS:UniProtKB.
DR   GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IMP:MGI.
DR   GO; GO:0060122; P:inner ear receptor stereocilium organization; IMP:MGI.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:InterPro.
DR   InterPro; IPR003644; Calx_beta.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   InterPro; IPR009039; EAR.
DR   InterPro; IPR005492; EPTP.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR000203; GPS_dom.
DR   Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 1.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF03160; Calx-beta; 17.
DR   Pfam; PF03736; EPTP; 1.
DR   Pfam; PF01825; GPS; 1.
DR   SMART; SM00237; Calx_beta; 20.
DR   SMART; SM00303; GPS; 1.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
DR   PROSITE; PS50912; EAR; 6.
DR   PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG.
DR   PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; FALSE_NEG.
DR   PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; FALSE_NEG.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Calcium; Cell membrane; Developmental protein;
KW   G-protein coupled receptor; Membrane; Receptor; Repeat; Secreted;
KW   Sensory transduction; Signal; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     28       Potential.
FT   CHAIN        29   6298       G-protein coupled receptor 98.
FT                                /FTId=PRO_0000232736.
FT   TOPO_DOM     29   5901       Extracellular (Potential).
FT   TRANSMEM   5902   5922       Helical; Name=1; (Potential).
FT   TOPO_DOM   5923   5932       Cytoplasmic (Potential).
FT   TRANSMEM   5933   5953       Helical; Name=2; (Potential).
FT   TOPO_DOM   5954   5973       Extracellular (Potential).
FT   TRANSMEM   5974   5994       Helical; Name=3; (Potential).
FT   TOPO_DOM   5995   6003       Cytoplasmic (Potential).
FT   TRANSMEM   6004   6024       Helical; Name=4; (Potential).
FT   TOPO_DOM   6025   6052       Extracellular (Potential).
FT   TRANSMEM   6053   6073       Helical; Name=5; (Potential).
FT   TOPO_DOM   6074   6097       Cytoplasmic (Potential).
FT   TRANSMEM   6098   6118       Helical; Name=6; (Potential).
FT   TOPO_DOM   6119   6126       Extracellular (Potential).
FT   TRANSMEM   6127   6147       Helical; Name=7; (Potential).
FT   TOPO_DOM   6148   6298       Cytoplasmic (Potential).
FT   DOMAIN       76    115       Calx-beta 1.
FT   DOMAIN      194    234       Calx-beta 2.
FT   DOMAIN      320    361       Calx-beta 3.
FT   DOMAIN      448    489       Calx-beta 4.
FT   DOMAIN      707    746       Calx-beta 5.
FT   DOMAIN      822    862       Calx-beta 6.
FT   DOMAIN      939    980       Calx-beta 7.
FT   DOMAIN     1052   1093       Calx-beta 8.
FT   DOMAIN     1167   1208       Calx-beta 9.
FT   DOMAIN     1500   1540       Calx-beta 10.
FT   DOMAIN     1622   1662       Calx-beta 11.
FT   DOMAIN     1763   1804       Calx-beta 12.
FT   DOMAIN     1907   1937       Calx-beta 13.
FT   DOMAIN     2034   2074       Calx-beta 14.
FT   DOMAIN     2161   2201       Calx-beta 15.
FT   DOMAIN     2279   2319       Calx-beta 16.
FT   DOMAIN     2497   2537       Calx-beta 17.
FT   DOMAIN     2631   2671       Calx-beta 18.
FT   DOMAIN     2745   2785       Calx-beta 19.
FT   DOMAIN     2880   2920       Calx-beta 20.
FT   DOMAIN     3003   3043       Calx-beta 21.
FT   DOMAIN     3127   3167       Calx-beta 22.
FT   REPEAT     3185   3237       EAR 1.
FT   REPEAT     3292   3341       EAR 2.
FT   REPEAT     3343   3389       EAR 3.
FT   REPEAT     3390   3435       EAR 4.
FT   REPEAT     3436   3484       EAR 5.
FT   REPEAT     3487   3530       EAR 6.
FT   DOMAIN     3581   3622       Calx-beta 23.
FT   DOMAIN     3697   3736       Calx-beta 24.
FT   DOMAIN     3831   3872       Calx-beta 25.
FT   DOMAIN     3962   4002       Calx-beta 26.
FT   DOMAIN     4079   4119       Calx-beta 27.
FT   DOMAIN     4195   4235       Calx-beta 28.
FT   DOMAIN     4310   4350       Calx-beta 29.
FT   DOMAIN     4565   4607       Calx-beta 31.
FT   DOMAIN     4687   4728       Calx-beta 32.
FT   DOMAIN     5047   5088       Calx-beta 33.
FT   DOMAIN     5284   5326       Calx-beta 34.
FT   DOMAIN     5420   5461       Calx-beta 35.
FT   DOMAIN     5846   5895       GPS.
FT   VAR_SEQ       1   1804       Missing (in isoform 3).
FT                                /FTId=VSP_017951.
FT   VAR_SEQ       1    720       Missing (in isoform 2).
FT                                /FTId=VSP_017952.
FT   VAR_SEQ     615    616       LE -> VL (in isoform 5).
FT                                /FTId=VSP_017953.
FT   VAR_SEQ     617   6298       Missing (in isoform 5).
FT                                /FTId=VSP_017954.
FT   VAR_SEQ     721    748       QNETSINITVKGDDIPELNETVTLSLDR -> MCLPSLCPS
FT                                HCSFCVDRVETERFVVYFG (in isoform 2).
FT                                /FTId=VSP_017955.
FT   VAR_SEQ    1213   1218       PGGQLA -> TNLSHL (in isoform 4).
FT                                /FTId=VSP_017956.
FT   VAR_SEQ    1219   6298       Missing (in isoform 4).
FT                                /FTId=VSP_017957.
FT   VAR_SEQ    1805   1810       LNLDGG -> MCVACE (in isoform 3).
FT                                /FTId=VSP_017958.
FT   VAR_SEQ    2938   2958       DSEGLTAQIVIDANDGAQGMI -> GMGLSFMNLLTNCESQ
FT                                RTSLF (in isoform 2 and isoform 3).
FT                                /FTId=VSP_017959.
FT   VAR_SEQ    2959   6298       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_017960.
FT   CONFLICT    412    416       SSRFE -> RYNLL (in Ref. 3).
FT   CONFLICT    520    520       A -> S (in Ref. 3; BAC66506).
FT   CONFLICT    859    859       V -> A (in Ref. 1).
FT   CONFLICT    873    873       R -> C (in Ref. 3; BAC66506).
FT   CONFLICT    963    963       S -> T (in Ref. 3; BAC66506).
FT   CONFLICT   1282   1282       E -> K (in Ref. 1).
FT   CONFLICT   1508   1508       G -> E (in Ref. 1).
FT   CONFLICT   1933   1933       S -> P (in Ref. 1).
FT   CONFLICT   1955   1955       L -> M (in Ref. 1).
FT   CONFLICT   1994   1994       A -> T (in Ref. 1).
FT   CONFLICT   2047   2047       V -> A (in Ref. 1).
FT   CONFLICT   2251   2252       NV -> SA (in Ref. 1).
FT   CONFLICT   2672   2672       G -> V (in Ref. 1).
FT   CONFLICT   4816   4832       VITDGARYKVGLVPLKN -> PLIGCPCSSGWCSTMHI
FT                                (in Ref. 4).
FT   CONFLICT   5084   5084       Y -> F (in Ref. 4).
FT   CONFLICT   5127   5127       A -> V (in Ref. 4).
FT   CONFLICT   5205   5205       V -> L (in Ref. 4).
FT   CONFLICT   5282   5282       V -> F (in Ref. 4).
FT   CONFLICT   5314   5315       DA -> EP (in Ref. 4).
FT   CONFLICT   5417   5417       A -> L (in Ref. 4).
FT   CONFLICT   5578   5578       A -> T (in Ref. 4).
FT   CONFLICT   5630   5630       R -> Q (in Ref. 4).
FT   CONFLICT   6122   6122       G -> R (in Ref. 4).
SQ   SEQUENCE   6298 AA;  687458 MW;  F99E731B0ADBD66D CRC64;
     MSVTSEPGMI SSFLLVYLST LFISFVFGEA EIRFTGQTEF FVNETSTTVI RLVIERIGEP
     ANVTAIVSLS GEDTGDFFDT YAAAFIPARG TNRTVYIAVC DDDLPEPDET FTFHLTLQKP
     SANVKLGWPR AASVTILSND NAFGIISFST PSSISVIEPR SRNASVPLTL IREKGTYGMV
     TVTFDVSGGP NPPEEDLNPV RGNITFPPGR ATVIYNVTVL DDEVPENDEL FLIQLRSVEG
     GAEINASRSS VEIIVKKNDS PVNFMQSVYV VPEDDHVLTI PVLRGKDSDG NLIGSDETQV
     SIRYKVMTWD STAHAQQNVD FIDLQPDTTL VFPPFVHESH LKFQIIDDLI PEIAESFHIM
     LLKNTLQGDA VLMGPSTVQV TIKPNDKPYG VLSFNSILFE RPVIIDEDTA SSSRFEEIAV
     VRNGGTHGNV SVSWVLTRNS SDPSPVTADI TPASGTLQFA QGQMLAPISL VVFDDDLPEE
     AEAYLLTILP HTIQGGAEVS EPAQLLFYIQ DSDNVYGEIA FFPGESQKIE SSPSERSLSL
     SLARRGGSKG DVRVIYSALY IPAGAMDPLR AKDGILNTSR RSSLLFPEQN QQVSIKLPIR
     NDAFLQNGAH FLVQLEAVVL VNIFPPIPPV SPRFGEIRNI SLLVTPAIAN GEIGFLSNLP
     IILHEPKDSS AEVVSIPLHR DGTDGQATVY WSLRPSGFNS KAVTLDDAGP FNGSVVFLSG
     QNETSINITV KGDDIPELNE TVTLSLDRVS VDSDVLKSGY TSRDLIILEN DDPGGIFEFS
     YDSRGPYVIK EGDAVELRIT RSRGSLVKQF LRFHVEPRES NEFYGNMGVL EFTPGEREVV
     ITLLTRLDGT PELDEHFWVI LSSHGERESK LGRATLVNIT ILKNDYPHGI IEFVSDGLSA
     SIKESKGEDI YHAVYGVIRT RGNFGAVNVS WMVSPDFTQD VFPVQGTVCF GDQEFFKNIT
     VYSLVDEIPE EMEEFTIILL NATGGAQTGI RTTASLRILR NDDPVYFAEP CVLRVQEGET
     ANFTVLRNGS VDGACTVQYA TVDGKASGEE GDFAPVEKGE TLVFEVGSRE QSISVHVKDD
     GIPETDEPFY IVLFNSTGDT VVYEYGVATV IIEANDDPNG VFSLEPIDKA VEEGKTNAFW
     ILRHRGHFGN VSVAWQLFQN ASLQPGQEFY ETSGTVNFTD GEETKPVILR AFPDRIPEFN
     EFYILRLVNI SGPGGQLAET NFQVTVMIPF NDDPFGIFIL DPECLEREVA EDVLSEDDMS
     YITSFTILRQ QGVFGDVRVG WEVLSREFTA GLPPMIDFIL LGSFPSTVPL QPHMRRHHSG
     TDVLYFSGLE GAFGTVDPKY QPFRNNTIAN FTFSAWVMPN ANTNGFLIAK DDSHGSIYYG
     VKIQTNETHV TLSLHYKTFG SNVTYIAKST VMKYLEEGVW LHVLIILDDG IIEFYLDGKA
     MPRGIKSLKG EAITDGPGIL RIGAGMDGGA RFTGWMQDVR TYERKLTPEE IYELHAVPAR
     TDLHPISGYL EFRQGESNKS FIVAARDDSE EEGEELFLLK LVSVDGGAQI SKENTTARLR
     IQKSDNANGL FGFTGACIPE MTEEGSTVSC VVERTRGALG YVHVFYTISQ IESEGINYLV
     DDFANASGTI TFLPWQRSEV LNLYVLDEDM PELNEYFRVT LVSAVPGDGK LGSTPISGAS
     IDPEKETTGI TVKASDHPYG LMQFSTGLPP QPEDSMSLPA SSVPHITVQE EDGEIRLLVI
     RAQGLLGRVT VGFRTVSLTA FSPEDYQSTA GTLEFQSGER YKYIFVNITD NSIPELEKSF
     KVELLNLDGG VSDLFRVDGS GSGEADTDFF LPPVLPHASL GVASQILVTI AASDHAHGVF
     EFSPESLFVS GTEPEDGYST VVLNVTRTRG ALSAVTLQWK VDSDLDGDLA ITSGNITFET
     GQRIASITVE ILSDEEPELD KALTVSILNV SSGSLGVLTN ATLTILASDD PYGVFIFPNK
     TRPLSVEEAT QNVALSIIRL KGLMGEVAVS YATIDDMEKP PYFPPNLARA TQGGDYISAS
     GLALFRVNQT EATITISILD DAEPERSESV FIELFNSSLV DKVQNRPIPH SPRLGPKVET
     VAHLVIVAND DAFGTVQLSA TSVHVAENHV GPIINVTRTG GTFADVSVKF KAVPITAAAG
     EDYSIASSDV VLLEGETTKA VPIYIINDIY PELEETFLVQ LLNETTGGAT LGPLREAVIT
     IEASDDPYGL FGFQNTKFIV EEPEFNSVRV NVPIIRNSGT LGNVTVQWVA IINGQFATGD
     LRVVSGNVTF APGETIQTLL LEVLADDVPE IEEVVQVQLA AASGGGTIGL DRVANIVIPA
     NDNPYGSVAF VQSVFRVQEP LERSSYANIT VRRSGGHFGR LLLCYGTSDI DVVARAVEEG
     EDVLSYYESP TQGVPDPLWR TWVNVSAVEE TQYTCATLCL KERACSAFSV VSGAEGPRCF
     WMTSWVSGTV NSSDFQTYKK NMTRVASLFS GQAVAGSDYE PVTRQWAVIL EGDEFANLTV
     SVLPDDAPEM DESFLISLLE VHLMNISDSF KNQPTIGHPN TSAVVIGLNG DAFGVFIIYS
     VSPNTSEDGL CVEVQEQPQT SVELVIYRTG GSLGQVMVEW RVVGGTATEG LDFMGAGDIL
     TFAEGETKKM AILTILDDSE PEDNESILVR LGATEGGSRI LPSSDTVTVN ILANDNVAGI
     VSFQTASRSV IGHEGEMLQF HVVRTPPGRG NVTVNWKVVG QNLEVNFANF TGQLFFSEGT
     LNKTIFVHLL DDNIPEEKEV YQVVLYDVKT QGVSPAGVAL LDAQGYAAVL TVEASDEPHG
     VLNFALSSRF VVLQEANVTI QLFVNREFGS LGAINVTYAT VPGIVSLKNN TEGNLAEPES
     DFIPVVGSLV LEEGETTAAI SITVLEDDIP ELKEYFLVNL THVDLIMAPL TSSPPRLDSE
     GLTAQIVIDA NDGAQGMIEW QRNRFEVNET DGVVTLVAQR SRAALGQVSL FMYAQNLEAQ
     AGLDYMRTPQ ILHFTDGERF KHVDVMILDD DMPEGDERFQ LLLTNPSPGL ELGKNTIALI
     TVLANDDGPG VLSFNNSGHI FLREPTSLYV QESVAVLVIV REPAQGLFGT VAVQFVVTEV
     NSSTESKDLS PSKGFIVLEE GVRSKTLRIS AILDTEPEMD EHFVCTLFNP TGGARLGAHV
     QTLITIFQNQ APLGLFSISA VENSATSIDV EESNRSVYLN VSRTNGLDLT ASVQWETVSE
     TAFGMRGMDV VFSIFQSFFD KTALDWCFFT VEGSVYGVML RKSSLVVYRW QGTFVPVEDL
     KVESPKTCEA FNIGVSPYLV ITHGERSGEK PSINSVYMLT AGFRLVLIQT IIISGSCQVR
     HFTSDSQDYF IIASRRNDSE LTQVFRWNGN NFAWHQTLPV RGVLGMALFS RGGSVFLAIS
     QANIRQTSLL FTWSGTQFIN FQELPISGIT QVEALSSGDD VYLCFAKNTF LGNQNAIDIF
     VWEMGHSSLR YFQSLDFAAV KRIRSFTPAS GIVHILLTAQ DGSALYCWNS ELNAFSFVLE
     APAAHDAAFV TVKSLNSSKT LIALVGATDS HLYELTYVSS QSDFIPSLGE LIFEPGDKEA
     IIAVNVLDDT VPEKEESFRV QLKSPRGGAE IGINSSVRVT VLANDGAYGV VAFAQNSLHK
     QLEELERDSL VTLNVERLRG THGRITVAWE AAGSVSDVFP TSGVISFTED QAMSMITLTV
     LADDLPELSE AVVVTLTQIV TEGVEDPLKG ATIDQSRSRS VLTILPSDSP YGAVRWHTES
     LFNRVPEPTE NITVVQLHIV RDKGLFGDIS IHLIAKPNFL LHINNQATED EDFVLQDSVI
     IMKENIKETH AEVAILPDEV PELDEGLIVT IAAVNLVNPN FPAEQPRVQR PRMESAEILI
     EENDDPRGIF NFHVVRDVGG VIIAHEGPPP LNVLQVPVVR MAGTFETVNV YWKATPDSAG
     LEDFQPSHGM LQFADGQVIA PILVTIIDDS EFELLETFTI SLVSVTGGGR LGDDVSVNVV
     IAPNDSPFGI FGFEKKTVMV DGPLLSDDPD SYVTLTVVRS PGGKGAVRLH WAIEEKAKDD
     LSPLNGTLYF DETESQKSVI LHTLKDGMVG EDRRFIIELT AADEVEISPV KGSASVIIRG
     DKSISEVGIA SSSRHIIIGE PSATYNGTAI IDLVRGPGVS GEITVNWKIL PPSRGEFVET
     SGQLTMLDGQ TAATVVIQVL NDDIPEEKCH YEFQLTEISE GRMLHEASVS ARITMVASDA
     PYGRFSFSHE QLHVSKAAQR VNVTVVRSGG SFGRARVLYE TGSRTAEAGW DFVPASGELL
     FEAREKMKSL YIDILDDDLP EGPEEFVLAI TRVDLQGRGY DFTIQENGLQ IDQPPEIGNI
     SIVRIIIMKN DNAEGIIEFD PKYTDISVEE DAGVITLPVL RLHGTYGHVS ADFSSRGFSA
     VPGGYVLRGS SVTFQHGQNL SFINVSIIDD NGSEFEKQFE ILLIGATGGA ILGRHLVSKI
     TIAKSDSPFG IIRFLNQSKI SLPNPSSTMA LHLVLERTGG LLGEIQVSWE VVGPDAEEPL
     PPHNGDFADP VSGTVSFGDG EGGVRSIILR VCPHEETEAE ETFIVQLKPL REAKLDPRAK
     AVTLTIQKFG DPNGVIHFAP ESLSKRRFSE PPPSDGPLLV SFLVTRSKGT SGDIKVHWEL
     SSEFDITRDF LSTRGFFTIA DGESDANFDV HLLPDDVPEI EEEYAVQLVS VEGGAELDLG
     KCTARFSVSA NDDPHGVFAL YSDRQSVLIG QNLDRSIQIN ITRLAGAFGA VAVRVQILSD
     NKEDPVATEN EERQLVITDG ARYKVGLVPL KNQVFLSLGS NFTLQLVSVR LLSGPFYGIP
     TILQEAKNAI LSVPEEAANS QVGFESAAFQ LMDIKAGTSQ VMVSRKGTYG RLSVAWTTGY
     APGSEIPEPI VIGNMTPTLG SLSFVHGEER KGVLLWTFPS PGRPEAFVLH LSGLRSSAAG
     GAQLRSGFTT AEIEPMGVFQ FSPSSRNITV SEDAQTIRIC VQRLFGFHGD LIKVSYETTA
     GSAKPPEDFE AVQKGEVFFQ RFQPEIDFEI TIINDQLPEI EETYYINLTS VETRGLGKGG
     VNWRPRLNPD LSVAVVTIVD NDDLTGAAVS VPVTAGTVAV DSTLLAMETG STTHPNKSKI
     TTIPYTTEVF APVTETVTVS AIPEKLATAH SVISVKPDVV PGTVVASVYG TLSIGPPIVY
     VSEEMKNGTL STADILIQRM GGFAGNVTIT VKTFGGRCAQ KEPSVWPFQD VYGVGNLTTW
     AVEEEDFEEQ LLTLTFLYGE RERKIAVQIL DDDDAEGQEF FYVFLTDPQG GAEIVRGKDS
     TGFSAFAVII ISGSDLHNGI IGFSEESQRG LELREGADKN SQRLVVTRQP NRAFEEVQIF
     WRVTLNQTVT ILQEKGANLT DELRFVAGVT TCTGGQTRCF IHLELNPKKV HQVEMPFFVE
     LYDVTAGAAI NNSARFAPIK LSKSGAPQSL VSFSVGSRLA VAHKKSTLIS LQVARDSGTG
     IMMSVNFITQ ELRSAETVGR VLISPAVSGK DFVRTEGTLV FEPGQKSAVL DVVLTPEAGS
     LNKFPKRFQI VLFDPKGGAR IDKVYGTANI TLISDADSQA VWGLEDLLHR PLHEDILNRV
     LHNLNLRVAT ESTDEQLSAV MLIMEKITME GRNQAFSIKS RTLLYELLCV LINPKRKDTR
     GFSHFVEVAE HFAFSLLTDV TCGSPGEKSK TILDSCPYLS ILALHWNPQQ INGHKFEGKE
     GDYIQIPERL LDVPEAEMLD GKNACTLVQF VEYSSQQWFI AGDNLPALKD KVLSLNVKGQ
     SAQPLPNNNE VLYRIHAAEP RVVPHTSRCL LWNQAAASWL SDSQFCKVVE DASDYVECAC
     SHMSVYAVYA QTDNSSSYNE AFFSAGLICI SGLCLAVVSH MFCARHSMFA AKLLTHMMVA
     SLGTQILFLA SAYASPHLSE ESCSAVAAVA HYLYLCQFSW MLIQSVNFWY VLVVSDEHTE
     RRCLLFCLLS WGLPSFVVIL LILILRGIYH RSMPQIYGLI HGDLCFIPNI YAALFTAALV
     PLMCLVVVFV VFIHAYQLKP QWKGYDDVFR GRTNAAEIPL ILYLFALISM TWLWGGLHMA
     YGHFWMLVLF VIFNSLQGLY VFVVYFILHN QTCCPMKASY TVEMNGHPGP STAFFTPGSG
     IPPAGEINKS TQNLINAMEE VPSDWERSSF QQTSQASPDL KTSPQNGASF PSSGGYGPGS
     LIADEESQEF DDLIFALKTG AGLSVSDNES GQGSQEGGTL TDSQIVELRR IPIADTHL
//
ID   PP16B_MOUSE             Reviewed;         568 AA.
AC   Q8VHQ3;
DT   13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Protein phosphatase 1 regulatory inhibitor subunit 16B;
DE   AltName: Full=CAAX box protein TIMAP;
DE   AltName: Full=TGF-beta-inhibited membrane-associated protein;
DE   Flags: Precursor;
GN   Name=Ppp1r16b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Cerebellum;
RX   MEDLINE=22525552; PubMed=12638124; DOI=10.1016/S1567-133X(02)00010-8;
RA   Magdaleno S., Northcutt G.M., Curran T., Kurschner C.;
RT   "mPPP1R16B is a novel mouse protein phosphatase 1 targeting subunit
RT   whose mRNA is located in cell bodies and dendrites of neurons in four
RT   distinct regions of the brain.";
RL   Gene Expr. Patterns 1:143-149(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Regulator of protein phosphatase 1 (PP1) that acts as a
CC       positive regulator of pulmonary endothelial cell (EC) barrier
CC       function. Involved in PKA-mediated moesin dephosphorylation which
CC       is important in EC barrier protection against thrombin
CC       stimulation. Promotes the interaction of PPP1CA with RPSA/LAMR1
CC       and in turn facilitates the dephosphorylation of RPSA/LAMR1.
CC       Involved in the regulation of endothelial cell filopodia
CC       extension. May be a downstream target for TGF-beta1 signaling
CC       cascade in endothelial cells (By similarity).
CC   -!- SUBUNIT: Interacts with PPP1CA, PPP1CB and MSN. Interacts (via its
CC       fourth ankyrin repeat) with the mature dimeric form of RPSA/LAMR1
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane (By similarity). Cell
CC       membrane; Lipid-anchor (Potential). Nucleus (By similarity).
CC       Note=Co-localizes with RPSA/LAMR1 in the cell membrane (By
CC       similarity).
CC   -!- PTM: Phosphorylated by PKA and, after PKA priming, by GSK3B.
CC       Phosphorylation by GSK3B reduces its association with PP1C and
CC       enhances PP1C activity. Dephosphorylation by its associated PP1C
CC       results in enhanced association with PP1C, but reduced PP1C
CC       activity (By similarity).
CC   -!- MISCELLANEOUS: Repressed by TGF-beta1 which requires denovo
CC       protein synthesis and histone deacetylase (By similarity).
CC   -!- SIMILARITY: Contains 5 ANK repeats.
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DR   EMBL; AF423761; AAL62093.1; -; mRNA.
DR   EMBL; BC054764; AAH54764.1; -; mRNA.
DR   EMBL; BC057542; AAH57542.1; -; mRNA.
DR   IPI; IPI00319920; -.
DR   RefSeq; NP_001153134.1; NM_001159662.1.
DR   RefSeq; NP_694729.1; NM_153089.4.
DR   UniGene; Mm.150540; -.
DR   UniGene; Mm.479582; -.
DR   ProteinModelPortal; Q8VHQ3; -.
DR   SMR; Q8VHQ3; 22-320.
DR   STRING; Q8VHQ3; -.
DR   PhosphoSite; Q8VHQ3; -.
DR   PRIDE; Q8VHQ3; -.
DR   Ensembl; ENSMUST00000045503; ENSMUSP00000039540; ENSMUSG00000037754.
DR   Ensembl; ENSMUST00000052927; ENSMUSP00000062615; ENSMUSG00000037754.
DR   GeneID; 228852; -.
DR   KEGG; mmu:228852; -.
DR   UCSC; uc008nqn.1; mouse.
DR   CTD; 228852; -.
DR   MGI; MGI:2151841; Ppp1r16b.
DR   GeneTree; ENSGT00600000084108; -.
DR   HOGENOM; HBG443814; -.
DR   HOVERGEN; HBG053644; -.
DR   InParanoid; Q8VHQ3; -.
DR   OMA; MAYQGIT; -.
DR   OrthoDB; EOG4W6NVX; -.
DR   NextBio; 379206; -.
DR   ArrayExpress; Q8VHQ3; -.
DR   Bgee; Q8VHQ3; -.
DR   Genevestigator; Q8VHQ3; -.
DR   GermOnline; ENSMUSG00000037754; Mus musculus.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0051489; P:regulation of filopodium assembly; ISS:UniProtKB.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR017417; Pase-1_reg_su_16AB_euk.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 3.
DR   PIRSF; PIRSF038159; PP1_16AB_vert; 1.
DR   SMART; SM00248; ANK; 5.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
PE   2: Evidence at transcript level;
KW   ANK repeat; Cell membrane; Coiled coil; Lipoprotein; Membrane;
KW   Methylation; Nucleus; Palmitate; Phosphoprotein; Prenylation; Repeat.
FT   CHAIN         1    565       Protein phosphatase 1 regulatory
FT                                inhibitor subunit 16B.
FT                                /FTId=PRO_0000067044.
FT   PROPEP      566    568       Removed in mature form (Potential).
FT                                /FTId=PRO_0000396711.
FT   REPEAT      100    129       ANK 1.
FT   REPEAT      133    162       ANK 2.
FT   REPEAT      228    257       ANK 3.
FT   REPEAT      261    290       ANK 4.
FT   REPEAT      531    560       ANK 5.
FT   COILED       15     55       Potential.
FT   MOD_RES     333    333       Phosphoserine (By similarity).
FT   MOD_RES     337    337       Phosphoserine (By similarity).
FT   MOD_RES     565    565       Cysteine methyl ester (Potential).
FT   LIPID       564    564       S-palmitoyl cysteine (Potential).
FT   LIPID       565    565       S-farnesyl cysteine (Potential).
SQ   SEQUENCE   568 AA;  63571 MW;  5D8446C81DEBA3D1 CRC64;
     MASHVDLLTE LQLLEKVPTL ERLRAAQKRR AQQLKKWAQY EQDLLHRKRK HERKRSTGGR
     RKKVSFEASV ALLEASLRND AEEVRYFLKN KVSPDLCNED GLTALHQCCI DNFEEIVKLL
     LSHGANVNAK DNELWTPLHA AATCGHINLV KILVQYGADL LAVNSDGNMP YDLCEDEPTL
     DVIETCMAYQ GITQEKINEM RAAPEQKMIS DIHCMIAAGQ DLDWIDGQGA TLLHIAGANG
     YLRAAELLLD HGVRVDVKDW DGWEPLHAAA FWGQMPMAEL LVSHGASLSA RTSMDEMPID
     LCEEEEFKVL LLELKHKHDV IMKSQLRHKS SLSRRTSSAG SRGKVVRRAS LSDRTNLYRK
     EYEGEAILWQ QRSAAEDQRT STYNGDIRET RTDQENKDPN PRLEKPVLLS EFSTKISRGE
     LDGPVENGLR APVSTYQYAL ANGDIWKMHE MPDYSMAYGN PGVADVPPPW SGFKEQSPQT
     LLELKRQRAA AKLLSHPFLS THLGSSVARS GESSSEGKAP LIGGRTSPYS SNGTSVYYTV
     TSGDPPLLKF KAPMEEMEEK VHGCCRIS
//
ID   ACO11_MOUSE             Reviewed;         594 AA.
AC   Q8VHQ9;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Acyl-coenzyme A thioesterase 11;
DE            Short=Acyl-CoA thioesterase 11;
DE            EC=3.1.2.-;
DE   AltName: Full=Acyl-CoA thioester hydrolase 11;
DE   AltName: Full=Adipose-associated thioesterase;
DE   AltName: Full=Brown fat-inducible thioesterase;
DE            Short=BFIT;
GN   Name=Acot11; Synonyms=Bfit, Thea;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=FVB/N;
RX   MEDLINE=21552902; PubMed=11696000; DOI=10.1042/0264-6021:3600135;
RA   Adams S.H., Chui C., Schilbach S.L., Yu X.X., Goddard A.D.,
RA   Grimaldi J.C., Lee J., Dowd P., Colman S., Lewin D.A.;
RT   "BFIT, a unique acyl-CoA thioesterase induced in thermogenic brown
RT   adipose tissue: cloning, organization of the human gene and assessment
RT   of a potential link to obesity.";
RL   Biochem. J. 360:135-142(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Has acyl-CoA thioesterase activity towards medium (C12)
CC       and long-chain (C18) fatty acyl-CoA substrates.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- INDUCTION: By cold exposure and repressed by heat exposure.
CC   -!- SIMILARITY: Contains 2 acyl coenzyme A hydrolase domains.
CC   -!- SIMILARITY: Contains 1 START domain.
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DR   EMBL; AF416923; AAL40939.1; -; mRNA.
DR   EMBL; BC042492; AAH42492.1; -; mRNA.
DR   IPI; IPI00128588; -.
DR   RefSeq; NP_079866.2; NM_025590.4.
DR   UniGene; Mm.222956; -.
DR   ProteinModelPortal; Q8VHQ9; -.
DR   SMR; Q8VHQ9; 45-584.
DR   STRING; Q8VHQ9; -.
DR   PRIDE; Q8VHQ9; -.
DR   Ensembl; ENSMUST00000102762; ENSMUSP00000099823; ENSMUSG00000034853.
DR   GeneID; 329910; -.
DR   KEGG; mmu:329910; -.
DR   UCSC; uc008tyw.1; mouse.
DR   CTD; 329910; -.
DR   MGI; MGI:1913736; Acot11.
DR   GeneTree; ENSGT00390000004730; -.
DR   HOVERGEN; HBG023847; -.
DR   PhylomeDB; Q8VHQ9; -.
DR   NextBio; 399043; -.
DR   ArrayExpress; Q8VHQ9; -.
DR   Bgee; Q8VHQ9; -.
DR   CleanEx; MM_ACOT11; -.
DR   Genevestigator; Q8VHQ9; -.
DR   GermOnline; ENSMUSG00000034853; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IC:UniProtKB.
DR   GO; GO:0016291; F:acyl-CoA thioesterase activity; TAS:UniProtKB.
DR   GO; GO:0004091; F:carboxylesterase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; NAS:UniProtKB.
DR   GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
DR   GO; GO:0009409; P:response to cold; IEP:BHF-UCL.
DR   InterPro; IPR002913; START_lipid-bd.
DR   InterPro; IPR006683; Thioestr_supf.
DR   Pfam; PF03061; 4HBT; 2.
DR   Pfam; PF01852; START; 1.
DR   SMART; SM00234; START; 1.
DR   PROSITE; PS50848; START; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Phosphoprotein; Repeat; Serine esterase.
FT   CHAIN         1    594       Acyl-coenzyme A thioesterase 11.
FT                                /FTId=PRO_0000053814.
FT   DOMAIN       31    166       Acyl coenzyme A hydrolase 1.
FT   DOMAIN      201    337       Acyl coenzyme A hydrolase 2.
FT   DOMAIN      370    582       START.
FT   REGION       93     95       Coenzyme A binding (By similarity).
FT   REGION      122    124       Coenzyme A binding (By similarity).
FT   REGION      272    274       Coenzyme A binding (By similarity).
FT   BINDING     183    183       Coenzyme A (By similarity).
FT   MOD_RES     368    368       Phosphoserine (By similarity).
SQ   SEQUENCE   594 AA;  67355 MW;  9A51D3BCF38870C9 CRC64;
     MIQNVGNHLR RGFASMFSNR TSRKSISHPE SGDPPTMAEG EGYRNPTEVQ MSQLVLPCHT
     NHRGELSIGQ LLKWIDTTAC LSAERHAGCP CVTASMDDIY FDHTISVGQV VNIKAKVNRA
     FNSSMEVGIQ VVSEDLCSEK QWSVCKALAT FVAHRELSKV KLKQVIPLTE EEKTEHGVAA
     ERRRMRLVYA DTIKDLLTHC VIQDDLDKDC SNMVPAEKTR VESVELVLPP HANHQGNTFG
     GQIMAWMENV ATIAASRLCH AHPTLKAIEM FHFRGPSQVG DRLVLKAIVN NAFKHSMEVG
     VCVEAYRQEA ETQRRHINSA FMTFVVLDKD DQPQKLPWIR PQPGEGERRY REASARKKIR
     LDRKYLVSCK QAEVALSVPW DPSNQVYLSY YNVSSLKTLM AKDNWVLSVE ISEVRLYILE
     EDFLSFHLEM VVNVDAAQVF QLLSDLRRRP EWDKHYRSVE LVQQVDEDDA IYHVISPALS
     GNTKPQDFVI LASRRKPCDN GDPYVIALRS VTLPTHHETP EYQRGETLCS GFCLWREGDQ
     MTKVSYYNQA TPGFLNYVTT NVSGLSSEFY NTFKACESFL LDNRNDLAPS LQTL
//
ID   P66B_MOUSE              Reviewed;         594 AA.
AC   Q8VHR5; Q8C9Q3;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Transcriptional repressor p66-beta;
DE   AltName: Full=GATA zinc finger domain-containing protein 2B;
DE   AltName: Full=p66/p68;
GN   Name=Gatad2b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=21630035; PubMed=11756549; DOI=10.1128/MCB.22.2.536-546.2002;
RA   Feng Q., Cao R., Xia L., Erdjument-Bromage H., Tempst P., Zhang Y.;
RT   "Identification and functional characterization of the p66/p68
RT   components of the MeCP1 complex.";
RL   Mol. Cell. Biol. 22:536-546(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-121; SER-123; SER-130
RP   AND SER-136, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-121 AND SER-123, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-121 AND SER-123, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Has transcriptional repressor activity. Targets MBD3 to
CC       discrete loci in the nucleus (By similarity).
CC   -!- SUBUNIT: Binds MBD2 and MBD3. Binds the MeCP1 complex (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Note=Nuclear, in
CC       discrete foci (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VHR5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VHR5-2; Sequence=VSP_010930, VSP_010931;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: CR1 is required for interaction with MBD3 and
CC       transcription repression (By similarity).
CC   -!- DOMAIN: CR2 is required for localization to discrete loci in the
CC       nucleus (By similarity).
CC   -!- SIMILARITY: Contains 1 GATA-type zinc finger.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF411837; AAL39081.1; -; mRNA.
DR   EMBL; AK041594; BAC30997.1; -; mRNA.
DR   IPI; IPI00128615; -.
DR   IPI; IPI00453989; -.
DR   RefSeq; NP_647465.1; NM_139304.1.
DR   UniGene; Mm.270999; -.
DR   ProteinModelPortal; Q8VHR5; -.
DR   STRING; Q8VHR5; -.
DR   PhosphoSite; Q8VHR5; -.
DR   PRIDE; Q8VHR5; -.
DR   Ensembl; ENSMUST00000049382; ENSMUSP00000041370; ENSMUSG00000042390.
DR   GeneID; 229542; -.
DR   KEGG; mmu:229542; -.
DR   UCSC; uc008qca.1; mouse.
DR   UCSC; uc008qcb.1; mouse.
DR   CTD; 229542; -.
DR   MGI; MGI:2443225; Gatad2b.
DR   GeneTree; ENSGT00390000004097; -.
DR   HOGENOM; HBG717465; -.
DR   HOVERGEN; HBG053401; -.
DR   InParanoid; Q8VHR5; -.
DR   OMA; TSSAIYM; -.
DR   OrthoDB; EOG4CVG6R; -.
DR   PhylomeDB; Q8VHR5; -.
DR   NextBio; 379495; -.
DR   ArrayExpress; Q8VHR5; -.
DR   Bgee; Q8VHR5; -.
DR   CleanEx; MM_GATAD2B; -.
DR   Genevestigator; Q8VHR5; -.
DR   GermOnline; ENSMUSG00000042390; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR000679; Znf_GATA.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   Gene3D; G3DSA:3.30.50.10; Znf_NHR/GATA; 1.
DR   Pfam; PF00320; GATA; 1.
DR   PROSITE; PS00344; GATA_ZN_FINGER_1; FALSE_NEG.
DR   PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Metal-binding; Nucleus;
KW   Phosphoprotein; Repressor; Transcription; Transcription regulation;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    594       Transcriptional repressor p66-beta.
FT                                /FTId=PRO_0000083503.
FT   ZN_FING     415    468       GATA-type.
FT   REGION      166    191       CR1.
FT   REGION      341    481       CR2.
FT   COILED      141    195       Potential.
FT   COILED      450    483       Potential.
FT   MOD_RES     121    121       Phosphothreonine.
FT   MOD_RES     123    123       Phosphoserine.
FT   MOD_RES     130    130       Phosphoserine.
FT   MOD_RES     135    135       Phosphoserine (By similarity).
FT   MOD_RES     136    136       Phosphoserine.
FT   MOD_RES     334    334       Phosphoserine (By similarity).
FT   MOD_RES     335    335       Phosphoserine (By similarity).
FT   MOD_RES     339    339       Phosphoserine (By similarity).
FT   MOD_RES     487    487       Phosphoserine.
FT   VAR_SEQ     475    485       EIEQRLQQQAA -> VRTLTPTCTVI (in isoform
FT                                2).
FT                                /FTId=VSP_010930.
FT   VAR_SEQ     486    594       Missing (in isoform 2).
FT                                /FTId=VSP_010931.
SQ   SEQUENCE   594 AA;  65411 MW;  C57330259EADAAE6 CRC64;
     MDRMTEDALR LNLLKRSLDP ADERDDVLAK RLKMEGHEAM ERLKMLALLK RKDLANLEVP
     HELPTKQDGS GVKGYEEKLN GNLRPHGDNN RTAGRPGKEN INDEPVDMSA RRSEPDRGRL
     TPSPDIIVLS DNEASSPRSS SRMEERLKAA NLEMFKGKGM EERQQLIKQL RDELRLEEAR
     LVLLKKLRQS QLQKENVVQK TPVVQNAASI VQPSPAHVGQ QGLSKLPSRP GAQGIEPQNM
     RTLQGHSVIR SATNTTLPHM LMSQRVIAPN PAQLQGQRGP PKPGIVRTTT PNMNPAISYQ
     PQSSSSVPCQ RTTSSAIYMN LASHIQPGTV NRVSSPLPSP SAMSDAANSQ AAAKLALRKQ
     LEKTLLEIPP PKPPAPLLHF LPSAANSEFI YMVGLEEVVQ SVIDSQGKNC ASLLRVEPFV
     CAQCRTDFTP HWKQEKNGKI LCEQCMTSNQ KKALKAEHTN RLKNAFVKAL QQEQEIEQRL
     QQQAALSPTT APAVSSVSKQ ETIMRHHTLR QAPQPQSSLQ RGIPTSARSM LSNFAQAPQL
     SVPGGLLGMP GVNIAYLNTG IGGHKAPSLA DRQREYLLDM IPPRSISQSI SGQK
//
ID   CCG8_MOUSE              Reviewed;         423 AA.
AC   Q8VHW2;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Voltage-dependent calcium channel gamma-8 subunit;
DE   AltName: Full=Neuronal voltage-gated calcium channel gamma-8 subunit;
GN   Name=Cacng8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=21601102; PubMed=11738816; DOI=10.1016/S0378-1119(01)00738-7;
RA   Chu P.-J., Robertson H.M., Best P.M.;
RT   "Calcium channel gamma subunits provide insights into the evolution of
RT   this gene family.";
RL   Gene 280:37-48(2001).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Thought to stabilize the calcium channel in an
CC       inactivated (closed) state (By similarity).
CC   -!- SUBUNIT: The L-type calcium channel is composed of five subunits:
CC       alpha-1, alpha-2/delta, beta and gamma.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG
CC       subfamily.
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DR   EMBL; AF361350; AAL50045.1; -; mRNA.
DR   IPI; IPI00128826; -.
DR   RefSeq; NP_573453.1; NM_133190.1.
DR   UniGene; Mm.357990; -.
DR   ProteinModelPortal; Q8VHW2; -.
DR   STRING; Q8VHW2; -.
DR   PhosphoSite; Q8VHW2; -.
DR   PRIDE; Q8VHW2; -.
DR   Ensembl; ENSMUST00000092351; ENSMUSP00000090005; ENSMUSG00000053395.
DR   GeneID; 81905; -.
DR   KEGG; mmu:81905; -.
DR   CTD; 81905; -.
DR   MGI; MGI:1932376; Cacng8.
DR   eggNOG; maNOG21792; -.
DR   GeneTree; ENSGT00550000074547; -.
DR   HOGENOM; HBG564649; -.
DR   HOVERGEN; HBG003682; -.
DR   InParanoid; Q8VHW2; -.
DR   OrthoDB; EOG4RXZ0W; -.
DR   NextBio; 350473; -.
DR   Bgee; Q8VHW2; -.
DR   Genevestigator; Q8VHW2; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005262; F:calcium channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   InterPro; IPR008372; VDCC_g8su.
DR   InterPro; IPR008368; VDCC_gsu.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01792; VDCCGAMMA.
DR   PRINTS; PR01796; VDCCGAMMA8.
PE   1: Evidence at protein level;
KW   Calcium; Calcium channel; Calcium transport; Ion transport;
KW   Ionic channel; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    423       Voltage-dependent calcium channel gamma-8
FT                                subunit.
FT                                /FTId=PRO_0000164691.
FT   TRANSMEM     19     39       Helical; (Potential).
FT   TRANSMEM    127    147       Helical; (Potential).
FT   TRANSMEM    157    177       Helical; (Potential).
FT   TRANSMEM    207    227       Helical; (Potential).
FT   TRANSMEM    318    338       Helical; (Potential).
FT   COMPBIAS    245    360       Gly-rich.
FT   MOD_RES     251    251       Phosphoserine.
SQ   SEQUENCE   423 AA;  43453 MW;  D3AD13E18F9EB02D CRC64;
     MESLKRWNEE RGLWCEKGVQ VLLTTIGAFS AFGLMTIAIS TDYWLYTRAL ICNTTNLTAG
     DDGPPHRGGS GSSEKKDPGG LTHSGLWRIC CLEGLKRGVC VKINHFPEDT DYDHDSAEYL
     LRVVRASSIF PILSAILLLL GGVCVAASRV YKSKRNIILG AGILFVAAGL SNIIGVIVYI
     SANAGEPGPK RDEEKKNHYS YGWSFYFGGL SFILAEVIGV LAVNIYIERS REAHCQSRSD
     LLKAGGGAGG SGGSGPSAIL RLPSYRFRYR RRSRSSSRGS SEASPSRDAS PGGPGGPGFA
     STDISMYTLS RDPSKGSVAA GLASAGGGGS GAGVGAYGGA AGAAGGGGAG SERDRGSSAG
     FLTLHNAFPK EAASGVTVTV TGPPAAPAPA PAPPAPAAPA PGTLSKEAAA SNTNTLNRKT
     TPV
//
ID   CCG5_MOUSE              Reviewed;         275 AA.
AC   Q8VHW4;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Voltage-dependent calcium channel gamma-5 subunit;
DE   AltName: Full=Neuronal voltage-gated calcium channel gamma-5 subunit;
GN   Name=Cacng5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=21601102; PubMed=11738816; DOI=10.1016/S0378-1119(01)00738-7;
RA   Chu P.-J., Robertson H.M., Best P.M.;
RT   "Calcium channel gamma subunits provide insights into the evolution of
RT   this gene family.";
RL   Gene 280:37-48(2001).
CC   -!- FUNCTION: Thought to stabilize the calcium channel in an
CC       inactivated (closed) state (By similarity).
CC   -!- SUBUNIT: The L-type calcium channel is composed of five subunits:
CC       alpha-1, alpha-2/delta, beta and gamma.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG
CC       subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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DR   EMBL; AF361347; AAL50042.1; -; mRNA.
DR   IPI; IPI00128831; -.
DR   RefSeq; NP_001186230.1; NM_001199301.1.
DR   RefSeq; NP_542375.1; NM_080644.3.
DR   UniGene; Mm.87663; -.
DR   ProteinModelPortal; Q8VHW4; -.
DR   STRING; Q8VHW4; -.
DR   TCDB; 8.A.16.2.4; Ca+ channel auxiliary subunit gamma1-gamma8 (CCAgamma) family.
DR   PRIDE; Q8VHW4; -.
DR   Ensembl; ENSMUST00000039071; ENSMUSP00000047888; ENSMUSG00000040373.
DR   Ensembl; ENSMUST00000106742; ENSMUSP00000102353; ENSMUSG00000040373.
DR   GeneID; 140723; -.
DR   KEGG; mmu:140723; -.
DR   UCSC; uc007mbb.1; mouse.
DR   CTD; 140723; -.
DR   MGI; MGI:2157946; Cacng5.
DR   GeneTree; ENSGT00550000074547; -.
DR   HOGENOM; HBG446234; -.
DR   HOVERGEN; HBG025923; -.
DR   InParanoid; Q8VHW4; -.
DR   OMA; VLYISNI; -.
DR   OrthoDB; EOG40S0G8; -.
DR   PhylomeDB; Q8VHW4; -.
DR   NextBio; 369951; -.
DR   ArrayExpress; Q8VHW4; -.
DR   Bgee; Q8VHW4; -.
DR   Genevestigator; Q8VHW4; -.
DR   GermOnline; ENSMUSG00000040373; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005262; F:calcium channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   InterPro; IPR008369; VDCC_g5su.
DR   InterPro; IPR008368; VDCC_gsu.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01792; VDCCGAMMA.
DR   PRINTS; PR01793; VDCCGAMMA5.
PE   2: Evidence at transcript level;
KW   Calcium; Calcium channel; Calcium transport; Ion transport;
KW   Ionic channel; Membrane; Transmembrane; Transmembrane helix;
KW   Transport; Voltage-gated channel.
FT   CHAIN         1    275       Voltage-dependent calcium channel gamma-5
FT                                subunit.
FT                                /FTId=PRO_0000164682.
FT   TRANSMEM      8     28       Helical; (Potential).
FT   TRANSMEM    103    123       Helical; (Potential).
FT   TRANSMEM    129    149       Helical; (Potential).
FT   TRANSMEM    181    201       Helical; (Potential).
SQ   SEQUENCE   275 AA;  30894 MW;  37A01454A6CAC1CC CRC64;
     MSACGRKALT LLSSVFAVCG LGLLGIAVST DYWLYLEEGI ILPQNQSTEV KMSLHSGLWR
     VCFLAGEERG RCFTIEYVMP MNSQMTSEST VNVLKMIRSA TPFPLVSLFF MFIGFILSNI
     GHIRPHRTIL AFVSGIFFIL SGLSLVVGLV LYISSINDEM LNRTKDAETY FNYKYGWSFA
     FAAISFLLTE SAGVMSVYLF MKRYTAEDMY RPHPGFYRPR LSNCSDYSGQ FLHPDAWIRG
     RSPSDISSDA SLQMNSNYPA LLKCPDYDQM SSSPC
//
ID   SATB2_MOUSE             Reviewed;         733 AA.
AC   Q8VI24;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=DNA-binding protein SATB2;
DE   AltName: Full=Special AT-rich sequence-binding protein 2;
GN   Name=Satb2; Synonyms=Kiaa1034;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DEVELOPMENTAL STAGE.
RX   MEDLINE=22855719; PubMed=12915443; DOI=10.1093/hmg/ddg248;
RA   FitzPatrick D.R., Carr I.M., McLaren L., Leek J.P., Wightman P.,
RA   Williamson K., Gautier P., McGill N., Hayward C., Firth H.,
RA   Markham A.F., Fantes J.A., Bonthron D.T.;
RT   "Identification of SATB2 as the cleft palate gene on 2q32-q33.";
RL   Hum. Mol. Genet. 12:2491-2501(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH ATF4 AND RUNX2, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=16751105; DOI=10.1016/j.cell.2006.05.012;
RA   Dobreva G., Chahrour M., Dautzenberg M., Chirivella L., Kanzler B.,
RA   Farinas I., Karsenty G., Grosschedl R.;
RT   "SATB2 is a multifunctional determinant of craniofacial patterning and
RT   osteoblast differentiation.";
RL   Cell 125:971-986(2006).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=18255030; DOI=10.1016/j.neuron.2007.12.012;
RA   Alcamo E.A., Chirivella L., Dautzenberg M., Dobreva G., Farinas I.,
RA   Grosschedl R., McConnell S.K.;
RT   "Satb2 regulates callosal projection neuron identity in the developing
RT   cerebral cortex.";
RL   Neuron 57:364-377(2008).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18255031; DOI=10.1016/j.neuron.2007.12.028;
RA   Britanova O., de Juan Romero C., Cheung A., Kwan K.Y., Schwark M.,
RA   Gyorgy A., Vogel T., Akopov S., Mitkovski M., Agoston D., Sestan N.,
RA   Molnar Z., Tarabykin V.;
RT   "Satb2 is a postmitotic determinant for upper-layer neuron
RT   specification in the neocortex.";
RL   Neuron 57:378-392(2008).
CC   -!- FUNCTION: Binds to DNA, at nuclear matrix- or scaffold-associated
CC       regions. Thought to recognize the sugar-phosphate structure of
CC       double-stranded DNA. Transcription factor controlling nuclear gene
CC       expression, by binding to matrix attachment regions (MARs) of DNA
CC       and inducing a local chromatin-loop remodeling. Acts as a docking
CC       site for several chromatin remodeling enzymes and also by
CC       recruiting corepressors (HDACs) or coactivators (HATs) directly to
CC       promoters and enhancers. Required for the initiation of the upper-
CC       layer neurons (UL1) specific genetic program and for the
CC       inactivation of deep-layer neurons (DL) and UL2 specific genes,
CC       probably by modulating Bcl11b expression. Repressor of Ctip2 and
CC       regulatory determinant of corticocortical connections in the
CC       developing cerebral cortex. May play an important role in palate
CC       formation. Acts as a molecular node in a transcriptional network
CC       regulating skeletal development and osteoblast differentiation.
CC   -!- SUBUNIT: Interacts with PIAS1 (By similarity). Interacts with ATF4
CC       and RUNX2; resulting in enhanced DNA binding and transactivation
CC       by these transcription factors.
CC   -!- SUBCELLULAR LOCATION: Nucleus matrix (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VI24-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VI24-2; Sequence=VSP_008967;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in cortical neurons that extend
CC       axons across the corpus callosum. Also expressed in branchial
CC       arches and in cells of the osteoblast lineage, but not in
CC       chondrocytes and osteoclasts.
CC   -!- DEVELOPMENTAL STAGE: Expression first detected at 10.5 dpc in the
CC       maxillary component of the first pharyngeal arch and the lateral
CC       aspect of the frontonasal process in the regions that will
CC       subsequently fuse to form the primary palate. At 11 - 11.5 dpc,
CC       the expression pattern demarcates the region of the medial aspect
CC       of the maxillary process within the primitive oral cavity, which
CC       will form the palate shelf. By 12.5 dpc, symmetrical expression is
CC       seen in the medial edges of the developing palate shelves and this
CC       continues until 13.5 dpc when the strongest expression is in the
CC       mesenchyme underlying the medial edge epithelia. By the time of
CC       palatal shelf fusion at 14.5 dpc the expression is dramatically
CC       down-regulated. No expression detected elsewhere in the embryo at
CC       any stage examined.
CC   -!- PTM: Sumoylated by PIAS1. Sumoylation promotes nuclear
CC       localization, but represses transcription factor activity (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Malformations in 2 of the major axonal
CC       tracts interconnecting the cortical hemispheres: the corpus
CC       callosum (c.c) and the anterior commissure (a.c). Misrouted
CC       afferent and efferent cortical axon connections. Impaired
CC       migration of upper-layer neurons. Ectopic expression of Ctip2.
CC       Craniofacial abnormalities and defects in osteoblast
CC       differentiation and function.
CC   -!- SIMILARITY: Belongs to the CUT homeobox family.
CC   -!- SIMILARITY: Contains 2 CUT DNA-binding domains.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98080.1; Type=Erroneous initiation;
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DR   EMBL; AF319623; AAL37172.1; -; mRNA.
DR   EMBL; AK129270; BAC98080.1; ALT_INIT; mRNA.
DR   IPI; IPI00128650; -.
DR   IPI; IPI00395054; -.
DR   RefSeq; NP_631885.1; NM_139146.2.
DR   UniGene; Mm.145599; -.
DR   ProteinModelPortal; Q8VI24; -.
DR   SMR; Q8VI24; 165-231, 350-437, 473-674.
DR   STRING; Q8VI24; -.
DR   PhosphoSite; Q8VI24; -.
DR   PRIDE; Q8VI24; -.
DR   Ensembl; ENSMUST00000042857; ENSMUSP00000046067; ENSMUSG00000038331.
DR   Ensembl; ENSMUST00000114415; ENSMUSP00000110057; ENSMUSG00000038331.
DR   GeneID; 212712; -.
DR   KEGG; mmu:212712; -.
DR   UCSC; uc007bas.1; mouse.
DR   CTD; 212712; -.
DR   MGI; MGI:2679336; Satb2.
DR   GeneTree; ENSGT00390000008096; -.
DR   HOGENOM; HBG447119; -.
DR   HOVERGEN; HBG054240; -.
DR   InParanoid; Q8VI24; -.
DR   OMA; PPAEDSC; -.
DR   OrthoDB; EOG4DBTD9; -.
DR   NextBio; 373676; -.
DR   ArrayExpress; Q8VI24; -.
DR   Bgee; Q8VI24; -.
DR   CleanEx; MM_SATB2; -.
DR   Genevestigator; Q8VI24; -.
DR   GermOnline; ENSMUSG00000038331; Mus musculus.
DR   GO; GO:0000118; C:histone deacetylase complex; IDA:MGI.
DR   GO; GO:0000790; C:nuclear chromatin; IC:MGI.
DR   GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005667; C:transcription factor complex; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IGI:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0051216; P:cartilage development; IMP:MGI.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:MGI.
DR   GO; GO:0009880; P:embryonic pattern specification; IMP:MGI.
DR   GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0002076; P:osteoblast development; IGI:MGI.
DR   GO; GO:0060021; P:palate development; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   InterPro; IPR003350; Hmoeo_CUT.
DR   InterPro; IPR001356; Homeobox.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR010982; Lambda_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Pfam; PF02376; CUT; 2.
DR   Pfam; PF00046; Homeobox; 1.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
DR   SUPFAM; SSF47413; Lambda_like_DNA; 2.
DR   PROSITE; PS51042; CUT; 2.
DR   PROSITE; PS00027; HOMEOBOX_1; FALSE_NEG.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromatin regulator; Chromosomal rearrangement;
KW   Developmental protein; DNA-binding; Homeobox; Isopeptide bond;
KW   Nucleus; Phosphoprotein; Repeat; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN         1    733       DNA-binding protein SATB2.
FT                                /FTId=PRO_0000202401.
FT   DNA_BIND    350    437       CUT 1.
FT   DNA_BIND    473    560       CUT 2.
FT   DNA_BIND    615    674       Homeobox.
FT   MOD_RES      39     39       Phosphoserine (By similarity).
FT   MOD_RES     446    446       Phosphoserine (By similarity).
FT   MOD_RES     449    449       Phosphoserine (By similarity).
FT   MOD_RES     450    450       Phosphoserine (By similarity).
FT   MOD_RES     452    452       Phosphoserine (By similarity).
FT   MOD_RES     594    594       Phosphoserine (By similarity).
FT   CROSSLNK    233    233       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    350    350       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   VAR_SEQ      58    116       Missing (in isoform 2).
FT                                /FTId=VSP_008967.
SQ   SEQUENCE   733 AA;  82559 MW;  153CFD1CC3491F25 CRC64;
     MERRSESPCL RDSPDRRSGS PDVKGPPPVK VARLEQNGSP MGARGRPNGA VAKAVGGLMI
     PVFCVVEQLD GSLEYDNREE HAEFVLVRKD VLFSQLVETA LLALGYSHSS AAQAQGIIKL
     GRWNPLPLSY VTDAPDATVA DMLQDVYHVV TLKIQLQSCS KLEDLPAEQW NHATVRNALK
     ELLKEMNQST LAKECPLSQS MISSIVNSTY YANVSATKCQ EFGRWYKKYK KIKVERVERE
     NLSDYCVLGQ RPMHLPNMNQ LASLGKTNEQ SPHSQIHHST PIRNQVPALQ PIMSPGLLSP
     QLSPQLVRQQ IAMAHLINQQ IAVSRLLAHQ HPQAINQQFL NHPPIPRAVK PEPTNSSVEV
     SPDIYQQVRD ELKRASVSQA VFARVAFNRT QGLLSEILRK EEDPRTASQS LLVNLRAMQN
     FLNLPEVERD RIYQDERERS MNPNVSMVSS ASSSPSSSRT PQAKTSTPTT DLPIKVDGAN
     VNITAAIYDE IQQEMKRAKV SQALFAKVAA NKSQGWLCEL LRWKENPSPE NRTLWENLCT
     IRRFLNLPQH ERDVIYEEES RHHHSERMQH VVQLPPEPVQ VLHRQQSQPT KESSPPREEA
     PPPPPPTEDS CAKKPRSRTK ISLEALGILQ SFIHDVGLYP DQEAIHTLSA QLDLPKHTII
     KFFQNQRYHV KHHGKLKEHL GSAVDVAEYK DEELLTESEE NDSEEGSEEM YKVEAEEENA
     DKSKAAPAET DQR
//
ID   SORC3_MOUSE             Reviewed;        1219 AA.
AC   Q8VI51; Q9CTR4;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=VPS10 domain-containing receptor SorCS3;
DE   Flags: Precursor;
GN   Name=Sorcs3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Hermey G., Rezgaoui M., Hermans-Borgmeyer I.;
RT   "Cloning of a novel vps10 domain receptor.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 244-261, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1191-1219.
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the SORCS family. SORCS3 subfamily.
CC   -!- SIMILARITY: Contains 6 BNR repeats.
CC   -!- SIMILARITY: Contains 1 PKD domain.
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DR   EMBL; AF276314; AAL36983.1; -; mRNA.
DR   EMBL; AK020713; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00128776; -.
DR   RefSeq; NP_079972.1; NM_025696.3.
DR   UniGene; Mm.70980; -.
DR   ProteinModelPortal; Q8VI51; -.
DR   SMR; Q8VI51; 292-334, 566-642, 795-912.
DR   STRING; Q8VI51; -.
DR   PhosphoSite; Q8VI51; -.
DR   PRIDE; Q8VI51; -.
DR   Ensembl; ENSMUST00000078880; ENSMUSP00000077919; ENSMUSG00000063434.
DR   GeneID; 66673; -.
DR   KEGG; mmu:66673; -.
DR   UCSC; uc008hvx.1; mouse.
DR   CTD; 66673; -.
DR   MGI; MGI:1913923; Sorcs3.
DR   GeneTree; ENSGT00510000046443; -.
DR   HOGENOM; HBG445080; -.
DR   HOVERGEN; HBG059252; -.
DR   InParanoid; Q8VI51; -.
DR   OMA; FSRRCTK; -.
DR   OrthoDB; EOG46HG8Z; -.
DR   PhylomeDB; Q8VI51; -.
DR   NextBio; 322337; -.
DR   ArrayExpress; Q8VI51; -.
DR   Bgee; Q8VI51; -.
DR   Genevestigator; Q8VI51; -.
DR   GermOnline; ENSMUSG00000063434; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR006581; VPS10.
DR   Gene3D; G3DSA:2.60.40.670; PKD; 1.
DR   Pfam; PF00801; PKD; 1.
DR   SMART; SM00602; VPS10; 1.
DR   SUPFAM; SSF49299; PKD; 2.
DR   PROSITE; PS50093; PKD; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Membrane; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     33       Potential.
FT   CHAIN        34   1219       VPS10 domain-containing receptor SorCS3.
FT                                /FTId=PRO_0000033175.
FT   TOPO_DOM     34   1122       Lumenal (Potential).
FT   TRANSMEM   1123   1143       Helical; (Potential).
FT   TOPO_DOM   1144   1219       Cytoplasmic (Potential).
FT   REPEAT      228    239       BNR 1.
FT   REPEAT      276    287       BNR 2.
FT   REPEAT      317    328       BNR 3.
FT   REPEAT      512    523       BNR 4.
FT   REPEAT      589    600       BNR 5.
FT   REPEAT      631    642       BNR 6.
FT   DOMAIN      824    914       PKD.
FT   CARBOHYD    204    204       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    453    453       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    786    786       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    797    797       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    837    837       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    929    929       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    950    950       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   1219 AA;  135985 MW;  ABB3278A2EFEC7C4 CRC64;
     MEAAGTERPA GWPGAPLART GLLLLSTWVL AGAEITWGAT GGPGRLVSPA SRPPVLPPLL
     PRAAENRWPE ELASARRAAA PRRRSRLEPL SQASRGEIRT EAAGMSPEGA RWVPGIPSPS
     QAGSARRTRR AQPPSPLERG DSWATALADG AKGSRPHTKG SREEVRATRT GGASTEELRL
     PSTSFALTGD SAHNQAMVHW SGHNSSVILI LTKLYDFNLG SVTESSLWRS VDYGATYEKL
     NDKVGLKTVL SYLYVNPTNK RKIMLLSDPE MESSVLISSD EGATYQKYRL TFYIQSLLFH
     PKQEDWVLAY SLDQKLYSSM DFGRRWQLMH ERITPNRFYW SVSGLDKEAD LVHMEVRTAD
     GYAHYLTCRI QECAETTRSG PFARSIDISS LVVQDEYIFI QVTIGGRASY YVSYRREAFA
     QIKLPKYSLP KDMHIISTDE NQVFAAVQEW NQNDTYNLYI SDTRGIYFTL AMENIKSSRG
     LMGNIIIELY EVAGIKGIFL ANKKVDDQVK TYITYNKGRD WRLLQAPDVD LRGSPVHCLL
     PFCSLHLHLQ LSENPYSSGR ISSKDTAPGL VVATGNIGSE LSYTDIGVFI SSDGGNTWRQ
     IFDEEYNVWF LDWGGALVAM KHTPLPVRHL WVSFDEGHSW DKYGFTLLPL FVDGALVEAG
     VETHIMTVFG HFSLRSEWQL VKVDYKSIFS RRCTKEDFET WHLLNQGEPC VMGERKIFKK
     RKPGAQCALG REYSGSVVSE PCVCADWDFE CDYGYERHGE SQCVPAFWYN PASPSKDCSL
     GQSYLNSTGY RRIVSNNCTD GLRDKYSAKT QLCPGKAPRG LHVVTTDGRL VAEQGHNATF
     IILMEEGDLQ RTNIQLDFGD GVAVSYANFS PIEDGIRHVY KSAGIFQVTA YAENNLGSDT
     AFLFLHVVCP VEHVHLRVPF VAIRNKDVNI SAVVWPSQLG TLTYFWWFGN STKPLITLDS
     SISFTFLAEG TNTITVQVAA GNALIQDTKE IAVHEYFQSQ LLSFSPNLDY HNPDIPEWRQ
     DIGNVIKRAL IKVTSVPEDQ ILVAVFPGLP TSAELFILPP KNLTERRKGH EGDLEQIVET
     LFNALNQNLV QFELKPGVQV IVYVTQLTLA PLVDSSAGHS SSAMLMLLSV VFVGLAVFLI
     YKFKRKIPWI NIYAQVQHDK EQEMIGSVSQ SENAPKITLS DFTEPEELLD KELDTRVIGS
     IATIASSEST KEIPNCTSV
//
ID   LRP4_MOUSE              Reviewed;        1905 AA.
AC   Q8VI56; A2AGT4; Q8BPX5; Q8CBB3; Q8CCP5;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 3.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Low-density lipoprotein receptor-related protein 4;
DE            Short=LRP-4;
DE   AltName: Full=LDLR dan;
DE   Flags: Precursor;
GN   Name=Lrp4; Synonyms=Kiaa0816;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RA   Simon-Chazottes D.C., Tutois S., Bourgade F., Evans M.J., Kuehn M.R.,
RA   Guenet J.-L.;
RT   "Characterization of an insertional mutation responsible for abnormal
RT   limb development.";
RL   (In) Proceedings of the 14th international mouse genome conference,
RL   abstract#B10, Narita (2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-566 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J; TISSUE=Bone, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 682-1905 (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1887, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Potential cell surface endocytic receptor, which binds
CC       and internalizes extracellular ligands for degradation by
CC       lysosomes.
CC   -!- INTERACTION:
CC       P25304:Agrn (xeno); NbExp=2; IntAct=EBI-2106160, EBI-2106099;
CC       Q62838:Musk (xeno); NbExp=1; IntAct=EBI-2106160, EBI-2106354;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VI56-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VI56-2; Sequence=VSP_010034;
CC   -!- SIMILARITY: Belongs to the LDLR family.
CC   -!- SIMILARITY: Contains 3 EGF-like domains.
CC   -!- SIMILARITY: Contains 8 LDL-receptor class A domains.
CC   -!- SIMILARITY: Contains 20 LDL-receptor class B repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC27835.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC       Sequence=BAC29416.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF247637; AAL36970.1; -; mRNA.
DR   EMBL; AL691489; CAM16480.1; -; Genomic_DNA.
DR   EMBL; AL732478; CAM16480.1; JOINED; Genomic_DNA.
DR   EMBL; AL732478; CAM24075.1; -; Genomic_DNA.
DR   EMBL; AL691489; CAM24075.1; JOINED; Genomic_DNA.
DR   EMBL; BC132240; AAI32241.1; -; mRNA.
DR   EMBL; AK032360; BAC27835.1; ALT_TERM; mRNA.
DR   EMBL; AK036406; BAC29416.1; ALT_SEQ; mRNA.
DR   EMBL; AK129224; BAC98034.1; -; Transcribed_RNA.
DR   IPI; IPI00411145; -.
DR   IPI; IPI00411146; -.
DR   RefSeq; NP_001139329.1; NM_001145857.1.
DR   RefSeq; NP_766256.3; NM_172668.3.
DR   UniGene; Mm.275149; -.
DR   UniGene; Mm.469960; -.
DR   ProteinModelPortal; Q8VI56; -.
DR   SMR; Q8VI56; 25-694, 702-998, 1006-1651.
DR   IntAct; Q8VI56; 4.
DR   MINT; MINT-6801185; -.
DR   STRING; Q8VI56; -.
DR   PhosphoSite; Q8VI56; -.
DR   PRIDE; Q8VI56; -.
DR   Ensembl; ENSMUST00000028689; ENSMUSP00000028689; ENSMUSG00000027253.
DR   Ensembl; ENSMUST00000111341; ENSMUSP00000106973; ENSMUSG00000027253.
DR   GeneID; 228357; -.
DR   KEGG; mmu:228357; -.
DR   UCSC; uc008kvx.1; mouse.
DR   CTD; 228357; -.
DR   MGI; MGI:2442252; Lrp4.
DR   GeneTree; ENSGT00580000081234; -.
DR   HOGENOM; HBG358042; -.
DR   HOVERGEN; HBG049163; -.
DR   InParanoid; Q8VI56; -.
DR   OMA; HTDVHVP; -.
DR   OrthoDB; EOG405S05; -.
DR   PhylomeDB; Q8VI56; -.
DR   NextBio; 378964; -.
DR   ArrayExpress; Q8VI56; -.
DR   Bgee; Q8VI56; -.
DR   Genevestigator; Q8VI56; -.
DR   GermOnline; ENSMUSG00000027253; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:MGI.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0001942; P:hair follicle development; IMP:MGI.
DR   GO; GO:0001822; P:kidney development; IMP:MGI.
DR   GO; GO:0030178; P:negative regulation of Wnt receptor signaling pathway; IDA:MGI.
DR   GO; GO:0042475; P:odontogenesis of dentine-containing tooth; IMP:MGI.
DR   GO; GO:0008104; P:protein localization; IMP:MGI.
DR   GO; GO:0009954; P:proximal/distal pattern formation; IMP:MGI.
DR   GO; GO:0043113; P:receptor clustering; IMP:MGI.
DR   GO; GO:0051124; P:synaptic growth at neuromuscular junction; IMP:MGI.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR001881; EGF_Ca-bd.
DR   InterPro; IPR013091; EGF_Ca-bd_2.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   Gene3D; G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 4.
DR   Gene3D; G3DSA:4.10.400.10; LDL_rcpt_classA_cys-rich; 8.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF00057; Ldl_recept_a; 8.
DR   Pfam; PF00058; Ldl_recept_b; 16.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00192; LDLa; 8.
DR   SMART; SM00135; LY; 20.
DR   SUPFAM; SSF57184; Grow_fac_recept; 1.
DR   SUPFAM; SSF57424; LDL_rcpt_classA_cys-rich; 8.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; FALSE_NEG.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS01209; LDLRA_1; 8.
DR   PROSITE; PS50068; LDLRA_2; 8.
DR   PROSITE; PS51120; LDLRB; 20.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Disulfide bond; EGF-like domain;
KW   Endocytosis; Glycoprotein; Membrane; Phosphoprotein; Receptor; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21   1905       Low-density lipoprotein receptor-related
FT                                protein 4.
FT                                /FTId=PRO_0000017326.
FT   TOPO_DOM     21   1725       Extracellular (Potential).
FT   TRANSMEM   1726   1746       Helical; (Potential).
FT   TOPO_DOM   1747   1905       Cytoplasmic (Potential).
FT   DOMAIN       26     67       LDL-receptor class A 1.
FT   DOMAIN       70    106       LDL-receptor class A 2.
FT   DOMAIN      109    144       LDL-receptor class A 3.
FT   DOMAIN      147    183       LDL-receptor class A 4.
FT   DOMAIN      190    226       LDL-receptor class A 5.
FT   DOMAIN      230    266       LDL-receptor class A 6.
FT   DOMAIN      269    305       LDL-receptor class A 7.
FT   DOMAIN      311    350       LDL-receptor class A 8.
FT   DOMAIN      354    394       EGF-like 1; atypical.
FT   DOMAIN      395    434       EGF-like 2; calcium-binding.
FT   REPEAT      480    522       LDL-receptor class B 1.
FT   REPEAT      523    565       LDL-receptor class B 2.
FT   REPEAT      566    609       LDL-receptor class B 3.
FT   REPEAT      610    652       LDL-receptor class B 4.
FT   REPEAT      653    693       LDL-receptor class B 5.
FT   DOMAIN      698    737       EGF-like 3.
FT   REPEAT      785    827       LDL-receptor class B 6.
FT   REPEAT      828    870       LDL-receptor class B 7.
FT   REPEAT      871    914       LDL-receptor class B 8.
FT   REPEAT      915    956       LDL-receptor class B 9.
FT   REPEAT      957    998       LDL-receptor class B 10.
FT   REPEAT     1093   1135       LDL-receptor class B 11.
FT   REPEAT     1136   1178       LDL-receptor class B 12.
FT   REPEAT     1179   1222       LDL-receptor class B 13.
FT   REPEAT     1223   1263       LDL-receptor class B 14.
FT   REPEAT     1264   1306       LDL-receptor class B 15.
FT   REPEAT     1397   1439       LDL-receptor class B 16.
FT   REPEAT     1440   1482       LDL-receptor class B 17.
FT   REPEAT     1483   1526       LDL-receptor class B 18.
FT   REPEAT     1527   1568       LDL-receptor class B 19.
FT   REPEAT     1569   1610       LDL-receptor class B 20.
FT   MOD_RES    1887   1887       Phosphoserine.
FT   CARBOHYD    264    264       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    498    498       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    719    719       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    901    901       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1077   1077       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1415   1415       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1467   1467       N-linked (GlcNAc...) (Potential).
FT   DISULFID     27     44       By similarity.
FT   DISULFID     34     57       By similarity.
FT   DISULFID     51     66       By similarity.
FT   DISULFID     71     83       By similarity.
FT   DISULFID     78     96       By similarity.
FT   DISULFID     90    105       By similarity.
FT   DISULFID    110    122       By similarity.
FT   DISULFID    117    135       By similarity.
FT   DISULFID    129    143       By similarity.
FT   DISULFID    148    160       By similarity.
FT   DISULFID    155    173       By similarity.
FT   DISULFID    167    182       By similarity.
FT   DISULFID    191    203       By similarity.
FT   DISULFID    198    216       By similarity.
FT   DISULFID    210    225       By similarity.
FT   DISULFID    231    243       By similarity.
FT   DISULFID    238    256       By similarity.
FT   DISULFID    250    265       By similarity.
FT   DISULFID    270    282       By similarity.
FT   DISULFID    277    295       By similarity.
FT   DISULFID    289    304       By similarity.
FT   DISULFID    312    324       By similarity.
FT   DISULFID    319    337       By similarity.
FT   DISULFID    331    349       By similarity.
FT   DISULFID    358    369       By similarity.
FT   DISULFID    365    378       By similarity.
FT   DISULFID    380    393       By similarity.
FT   DISULFID    399    409       By similarity.
FT   DISULFID    405    418       By similarity.
FT   DISULFID    420    433       By similarity.
FT   DISULFID    702    713       By similarity.
FT   DISULFID    709    722       By similarity.
FT   DISULFID    724    736       By similarity.
FT   VAR_SEQ    1564   1620       Missing (in isoform 2).
FT                                /FTId=VSP_010034.
FT   CONFLICT    196    196       F -> L (in Ref. 4; BAC27835).
FT   CONFLICT    325    325       I -> L (in Ref. 4; BAC29416).
FT   CONFLICT    380    380       C -> R (in Ref. 1; AAL36970).
FT   CONFLICT    682    685       HFPM -> LHTP (in Ref. 5).
FT   CONFLICT   1330   1330       G -> S (in Ref. 1; AAL36970).
SQ   SEQUENCE   1905 AA;  211954 MW;  282CA859B76D9BAD CRC64;
     MRRWWGALLL GALLCAHGIA SSLECACGRS HFTCAVSALG ECTCIPAQWQ CDGDNDCGDH
     SDEDGCTLPT CSPLDFHCDN GKCIRRSWVC DGDNDCEDDS DEQDCPPREC EEDEFPCQNG
     YCIRSLWHCD GDNDCGDNSD EQCDMRKCSD KEFRCSDGSC IAEHWYCDGD TDCKDGSDEE
     SCPSAVPSPP CNLEEFQCAY GRCILDIYHC DGDDDCGDWS DESDCSSHQP CRSGEFMCDS
     GLCINSGWRC DGDADCDDQS DERNCTTSMC TAEQFRCRSG RCVRLSWRCD GEDDCADNSD
     EENCENTGSP QCASDQFLCW NGRCIGQRKL CNGINDCGDS SDESPQQNCR PRTGEENCNV
     NNGGCAQKCQ MVRGAVQCTC HTGYRLTEDG RTCQDVNECA EEGYCSQGCT NTEGAFQCWC
     EAGYELRPDR RSCKALGPEP VLLFANRIDI RQVLPHRSEY TLLLNNLENA IALDFHHRRE
     LVFWSDVTLD RILRANLNGS NVEEVVSTGL ESPGGLAVDW VHDKLYWTDS GTSRIEVANL
     DGAHRKVLLW QSLEKPRAIA LHPMEGTIYW TDWGNTPRIE ASSMDGSGRR IIADTHLFWP
     NGLTIDYAGR RMYWVDAKHH VIERANLDGS HRKAVISQGL PHPFAITVFE DSLYWTDWHT
     KSINSANKFT GKNQEIIRNK LHFPMDIHTL HPQRQPAGKN RCGDNNGGCT HLCLPSGQNY
     TCACPTGFRK INSHACAQSL DKFLLFARRM DIRRISFDTE DLSDDVIPLA DVRSAVALDW
     DSRDDHVYWT DVSTDTISRA KWDGTGQEVV VDTSLESPAG LAIDWVTNKL YWTDAGTDRI
     EVANTDGSMR TVLIWENLDR PRDIVVEPMG GYMYWTDWGA SPKIERAGMD ASSRQVIISS
     NLTWPNGLAI DYGSQRLYWA DAGMKTIEFA GLDGSKRKVL IGSQLPHPFG LTLYGQRIYW
     TDWQTKSIQS ADRLTGLDRE TLQENLENLM DIHVFHRQRP PVTTLCAVEN GGCSHLCLRS
     PNPSGFSCTC PTGINLLRDG KTCSPGMNSF LIFARRIDVR MVSLDIPYFA DVVVPINMTM
     KNTIAIGVDP LEGKVYWSDS TLHRISRASL DGSQHEDIIT TGLQTTDGLA VDAIGRKVYW
     TDTGTNRIEV GNLDGSMRKV LVWQNLDSPR AIVLYHEMGF MYWTDWGENA KLERSGMDGS
     DRTVLINNNL GWPNGLTVDK TSSQLLWADA HTERIEVADL NGANRHTLVS PVQHPYGLTL
     LDSYIYWTDW QTRSIHRADK STGSNVILVR SNLPGLMDIQ AVDRAQPLGF NKCGSRNGGC
     SHLCLPRPSG FSCACPTGIQ LKGDRKTCDP SPETYLLFSS RGSIRRISLD TDDHTDVHVP
     VPGLNNVISL DYDSVHGKVY YTDVFLDVIR RADLNGSNME TVIGHGLKTT DGLAVDWVAR
     NLYWTDTGRN TIEASRLDGS CRKVLINNSL DEPRAIAVFP RKGYLFWTDW GHIAKIERAN
     LDGSERKVLI NTDLGWPNGL TLDYDTRRIY WVDAHLDRIE SADLNGKLRQ VLVSHVSHPF
     ALTQQDRWIY WTDWQTKSIQ RVDKYSGRNK ETVLANVEGL MDIIVVSPQR QTGTNACGVN
     NGGCTHLCFA RASDFVCACP DEPDGHPCSL VPGLVPPAPR ATSMNEKSPV LPNTLPTTLH
     SSTTKTRTSL EGAGGRCSER DAQLGLCAHS NEAVPAAPGE GLHVSYAIGG LLSILLILLV
     IAALMLYRHR KSKFTDPGMG NLTYSNPSYR TSTQEVKLEA APKPAVYNQL CYKKEGGPDH
     SYTKEKIKIV EGIRLLAGDD AEWGDLKQLR SSRGGLLRDH VCMKTDTVSI QASSGSLDDT
     ETEQLLQEEQ SECSSVHTAA TPERRGSLPD TGWKHERKLS SESQV
//
ID   PCX3_MOUSE              Reviewed;        2028 AA.
AC   Q8VI59;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Pecanex-like protein 3;
GN   Name=Pcnxl3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX   MEDLINE=20354997; PubMed=10894943;
RA   Saridaki A., Ferraz C., Demaille J., Scherer G., Roux A.-F.;
RT   "Genomic sequencing reveals the structure of the Kcnk6 and map3k11
RT   genes and their close vicinity to the sipa1 gene on mouse chromosome
RT   19.";
RL   Cytogenet. Cell Genet. 89:85-88(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-505, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8VI59-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8VI59-2; Sequence=VSP_033246;
CC   -!- SIMILARITY: Belongs to the pecanex family.
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DR   EMBL; BC096538; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AF237953; AAL62024.1; -; mRNA.
DR   IPI; IPI00128789; -.
DR   IPI; IPI00876328; -.
DR   RefSeq; NP_659117.2; NM_144868.3.
DR   UniGene; Mm.329650; -.
DR   STRING; Q8VI59; -.
DR   PhosphoSite; Q8VI59; -.
DR   PRIDE; Q8VI59; -.
DR   Ensembl; ENSMUST00000068169; ENSMUSP00000063786; ENSMUSG00000054874.
DR   Ensembl; ENSMUST00000113615; ENSMUSP00000109245; ENSMUSG00000054874.
DR   GeneID; 104401; -.
DR   KEGG; mmu:104401; -.
DR   UCSC; uc008gep.1; mouse.
DR   CTD; 104401; -.
DR   MGI; MGI:1861733; Pcnxl3.
DR   GeneTree; ENSGT00390000013164; -.
DR   HOGENOM; HBG564661; -.
DR   HOVERGEN; HBG045627; -.
DR   InParanoid; Q8VI59; -.
DR   OMA; FTHYLLP; -.
DR   OrthoDB; EOG45B1DX; -.
DR   NextBio; 357075; -.
DR   ArrayExpress; Q8VI59; -.
DR   Bgee; Q8VI59; -.
DR   CleanEx; MM_PCNXL3; -.
DR   Genevestigator; Q8VI59; -.
DR   GermOnline; ENSMUSG00000054874; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR007735; Pecanex.
DR   Pfam; PF05041; Pecanex_C; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Glycoprotein; Membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1   2028       Pecanex-like protein 3.
FT                                /FTId=PRO_0000215796.
FT   TRANSMEM     33     53       Helical; (Potential).
FT   TRANSMEM     54     74       Helical; (Potential).
FT   TRANSMEM    793    815       Helical; (Potential).
FT   TRANSMEM    819    836       Helical; (Potential).
FT   TRANSMEM    852    872       Helical; (Potential).
FT   TRANSMEM    880    900       Helical; (Potential).
FT   TRANSMEM    903    923       Helical; (Potential).
FT   TRANSMEM    946    968       Helical; (Potential).
FT   TRANSMEM    980   1000       Helical; (Potential).
FT   TRANSMEM   1053   1073       Helical; (Potential).
FT   TRANSMEM   1078   1098       Helical; (Potential).
FT   TRANSMEM   1244   1264       Helical; (Potential).
FT   TRANSMEM   1280   1300       Helical; (Potential).
FT   COMPBIAS    425    458       Ser-rich.
FT   COMPBIAS    809    812       Poly-Leu.
FT   COMPBIAS   1427   1430       Poly-Cys.
FT   COMPBIAS   1841   1845       Poly-Gly.
FT   COMPBIAS   1853   1924       Pro-rich.
FT   MOD_RES     127    127       Phosphoserine.
FT   MOD_RES     370    370       Phosphothreonine (By similarity).
FT   MOD_RES     505    505       Phosphoserine.
FT   CARBOHYD     95     95       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    319    319       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1770   1770       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     161    568       Missing (in isoform 2).
FT                                /FTId=VSP_033246.
SQ   SEQUENCE   2028 AA;  221573 MW;  B51969382FBFCA89 CRC64;
     MGSQVLQILR QGVWASLTGG WFFDPHQSTF SNCFHLYVWI FLLIFPFLLY MVLPPSLMVA
     GVYCLVVAVI FATIKTVNYR LHAMFDQGEI VEKRNSTMGE QEEEAAQGES SLPRDPGVEM
     TVFRKVSSTP PVRCSSQHSV FGFNQVSELL PRMEDSGPLR DIKELVREQG SNNVIVTSAD
     REMLKLSSQE KLIGDLPQTP PGVVPDPSLP STDSSERSPM AGDGVPWGGS GVADTPMSPL
     LKGSLSQELS KSFLTLTRPD RALVRTSSRR EQCRGTGGYQ PLDRRGSGDP MPQKAGSSDS
     CFSGTDRETL SSFKSEKTNS THLDSPPGGH APEGSDTDPP SEAELPASPD AGVPSDDTLR
     SFDTVIGAGT PPGQTEPLLV VRPKDLALLR PSKRRPPMRG HSPPGRTPRR PLLEGSGFFE
     DEDTSEGSEL SPASSLRSQR RYSTDSSSST SCYSPESSQG AAGGPRKRRA PHGAEEGTAV
     PPKRPYGTQR TPSTASAKTH ARVLSMDGAG GDVLRAPLAG SKAELEAQPG MELAAGEPAV
     LPPEARRGPA ANQPGWRGEL QEEGAVGGAP EETGQRECTS NVRRAQAIRR RHNAGSNPTP
     PASVMGSPPS SLQEAQRGRA ASHSRALTLP SALHFASSLL LTRAGPNVHE ASNFDDTSEG
     AVHYFYDESG VRRSYTFGLA GGGYENPVSQ PGEQAANGAW DRHSHSSSFH SADVPEATGG
     LNLLQPRPVV LQGMQVRRVP LEIPEEQTLM EEAPPRAQHS YKYWFLPGRW TSVRYERLAL
     LALLDRTRGV MENIFGVGLS SLVAFLGYLL LLKGFFTDIW VFQFCLVIAS CQYSLLKSVQ
     PDAASPMHGH NWVIAYSRPV YFCICCLLIW LLDALGTAQP FPPVSLYGLT LFSASFFFCA
     RDVATVFTLC FPFVFLLGLL PQVNTCLMYL LEQIDMHGFG GTAATSPLTA VFSLTRSLLA
     AALLYGFCLG AIKTPWPEQH VPVLFSVFCG LLVAMSYHLS RQSSDPTVLW SLVRSKLFPE
     LEERSLETAR VEPPDPLPEK MRQSVREVLH SDLVMCVVIA VLTFAVSAST VFIALKSVLG
     FVLYALAGAV GFFTHYLLPQ LRKQLPWFCL SQPVLKPLEY SQYEVRGAAQ VMWFEKLYAG
     LQCAEKYLIY PAVVLNALTV DAHTVVSHPD KFCLYCRALL MTVAGLKLLR SAFCCPPQQY
     LTLAFTVLLF HFDYPRLSQG FLLDYFLMSL LCSKLWDLLY KLRFVLTYIA PWQITWGSAF
     HAFAQPFAVP HSAMLFLQAL LSGLFSTPLN PLLGSAVFIM SYARPLKFWE RDYNTKRVDH
     SNTRLVTQLD RNPGADDNNL NSIFYEHLTR SLQHTLCGDL VLGRWGNYGP GDCFVLASDY
     LNALVHLIEV GNGLITFQLR GLEFRGTYCQ QREVEAITEG VEEDEGCCCC EPGHLPRVLS
     FNAAFGQRWL AWEVTASKYV LEGYSISDNN AASMLQVFDL RKILVTYYVK SIIYYVSRSP
     KLETWLNHEG IAAALRPVRA LGYADSDPTF SLSVDEDYDL RLSGLSLPSF CAVHLEWIQY
     CASRRSQPVD QDWNSPLVTL CFGLCVLGRR ALGTASHSMS ASLEPFLYGL HALFKGDFRI
     TSPRDEWVFA DMDLLHRVVA PGVRMALKLH QDHFTSPDEY EEPAALYDAI AANEERLVIS
     HEGDPAWRSA ILSNTPSLLA LRHVMDDASD EYKIIMLNRR HLSFRVIKVN RECVRGLWAG
     QQQELVFLRN RNPERGSIQN AKQALRNMIN SSCDQPLGYP IYVSPLTTSL AGSHPQLRAL
     WGGPVSLGAI ARWLLRSWER LHKGCGAGCN SGGNVDDSDC GGGGGLTSLS NHPPLAHPTP
     ENAAGSSEQP LPPGPSWGPR PSLSGSGDGR PPPLLQWPPP RLPGPPPASP APTEGPRPSR
     PSGPALLNSE GPSGKWSLGG RKGLGGPDGE PASGSPKGGT PKSQAPLDLS LSPDVSSEAS
     PARTTQDLPC LDSSIPEGCT PSGAPGDWPV PAEERESPAA QPLLEHQY
//
ID   Q8VI61_MOUSE            Unreviewed;       303 AA.
AC   Q8VI61;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 41.
DE   SubName: Full=Hexaribonucleotide binding protein 3;
DE   Flags: Fragment;
GN   Name=Rbfox3; Synonyms=D11Bwg0517e, Hrnbp3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c;
RA   Chen W., Winkelmann J.C.;
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AF229056; AAL71903.1; -; mRNA.
DR   IPI; IPI00894965; -.
DR   UniGene; Mm.341103; -.
DR   HSSP; P11940; 1CVJ.
DR   ProteinModelPortal; Q8VI61; -.
DR   STRING; Q8VI61; -.
DR   Ensembl; ENSMUST00000017576; ENSMUSP00000017576; ENSMUSG00000025576.
DR   Ensembl; ENSMUST00000117731; ENSMUSP00000113636; ENSMUSG00000025576.
DR   MGI; MGI:106368; Rbfox3.
DR   GeneTree; ENSGT00390000013767; -.
DR   HOVERGEN; HBG000044; -.
DR   InParanoid; Q8VI61; -.
DR   ArrayExpress; Q8VI61; -.
DR   Bgee; Q8VI61; -.
DR   Genevestigator; Q8VI61; -.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   303 AA;  32865 MW;  74B0AF9F9FB7E935 CRC64;
     TPAQTHPEQP GTEASTQPIA GTQTVPAQDE RAQTDNHELH PSDPTENDEP KRLHVSNIPF
     RFRDPDCGQM FGQFGKILDV EIIFNERGSK GFGFVTFETS SDADRAREKL NGTIVEGRKI
     EVNNATARVM TNGWKLNPVV GTVYGPEFYA VTSFPYPTTG TAVAYRGTHL RGRGRAVYNT
     FRAAPPPPPI PTYGAALEQT LVKMPVPWAG LAPCPLPPQQ TPEPAYPTSP AFPPLSCPFA
     SRVVYQDGFY GAEIYGGYAA YRYAQPAAAT AAAYSDSYGR VYAAADPYHH TIGPTATYSI
     GTM
//
ID   Q8VIE5_MOUSE            Unreviewed;      2561 AA.
AC   Q8VIE5;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   SubName: Full=BetaIV-spectrin sigma1;
GN   Name=Spnb4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21666188; PubMed=11807096; DOI=10.1083/jcb.200110003;
RA   Komada M., Soriano P.;
RT   "Beta]IV-spectrin regulates sodium channel clustering through ankyrin-
RT   G at axon initial segments and nodes of Ranvier.";
RL   J. Cell Biol. 156:337-348(2002).
CC   -!- SIMILARITY: Contains 1 PH domain.
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DR   EMBL; AB055618; BAB83243.1; -; mRNA.
DR   IPI; IPI00856469; -.
DR   RefSeq; NP_115999.2; NM_032610.2.
DR   UniGene; Mm.459123; -.
DR   HSSP; Q01082; 1BKR.
DR   ProteinModelPortal; Q8VIE5; -.
DR   SMR; Q8VIE5; 53-296.
DR   STRING; Q8VIE5; -.
DR   PhosphoSite; Q8VIE5; -.
DR   PRIDE; Q8VIE5; -.
DR   Ensembl; ENSMUST00000011895; ENSMUSP00000011895; ENSMUSG00000011751.
DR   GeneID; 80297; -.
DR   KEGG; mmu:80297; -.
DR   UCSC; uc009fwc.1; mouse.
DR   CTD; 80297; -.
DR   HOGENOM; HBG357452; -.
DR   HOVERGEN; HBG057912; -.
DR   InParanoid; Q8VIE5; -.
DR   NextBio; 350017; -.
DR   ArrayExpress; Q8VIE5; -.
DR   Bgee; Q8VIE5; -.
DR   Genevestigator; Q8VIE5; -.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR016343; Spectrin_bsu.
DR   InterPro; IPR001605; Spectrin_PH.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00435; Spectrin; 14.
DR   PIRSF; PIRSF002297; Spectrin_beta_subunit; 1.
DR   PRINTS; PR00683; SPECTRINPH.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00150; SPEC; 16.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Actin-binding; Repeat.
SQ   SEQUENCE   2561 AA;  288809 MW;  4DF01A9180140F33 CRC64;
     MAQVPGEVDN MEGPAVSNNN NPSARWESPD RGWDREPPAA ANAAASLFEC SRIKALADER
     EAVQKKTFTK WVNSHLARVG CHIGDLYADL RDGFVLTRLL EVLSGEQLPR PTRGRMRIHS
     LENVDKALQF LKEQRVHLEN VGSHDIVDGN HRLTLGLVWT IILRFQIQVI KIETEDNRET
     RSAKDALLLW CQMKTAGYPE VNIQNFTTSW RDGLAFNALI HRHRPDLVDL SKLTKSNANY
     NLQRAFRTAE QHLGLARLLD PEDVNMEAPD EKSIITYVVS FYHYFSKMKA LAVEGKRIGK
     VLDQVLEVDK IIERYEELAA ELLAWIHRTV DLISNQKFAN SLSGVQQQLQ AFTAYCTLEK
     PVKFQEKGNL EVLLFSIQSK LRAHNRRLFV PREGCGIWDI DKAWGELEKA EHEREAALRA
     ELIRQEKLEL LAQRFDHKVA MRESWLNENQ RLVSQDNFGY ELPAVEAAMK KHEAIEADIA
     AYEERVQGVA ELAQALAAEG YYDARRVAAQ RDSVLRQWAL LTGLVGARRT RLEQNLALQK
     VFQEMVYMVD WMEEMQTQLL SRECGQHLVE ADDLLQKHGL LEGDIAAQSE RVEALNAAAL
     RFSQLQGYQP CDPQVICNRV NHVHGCLSEL QEQAARRRAE LEASRSLWAL LQELEEAESW
     ARDKERLLEA TSGSGGAAGT AGGAHDLSST ARLLAQHKIL QGELGGRRAL LQQALRRGEE
     LAAAGGSVGP GAEPLHLAGL AERAASARRR WQRLEEAAAR RERRLQEARA LHQFGADLDG
     LLDWLRDAYR LAAAGDFGHD EASSRRLARQ HRALTGEVEA HRGPVGGLRR QLATLGGASG
     AGPLVVALQV RVVEAEQLFA EVTEVAALRR QWLRDALAVY RMFGEVHACE LWIGEKEQWL
     LAMRVPDSLD DVEVVQHRFE SLDQEMNSLM GRVLDVNQTV QELVEGGHPS SDEVRSCQDH
     LNSRWNRIVE LVEQRKEEMS AVLLVENHVL EVAEVRAQVR EKRRAVESAP RAGGALQWRL
     SGLEAALQAL EPRQAALLEE AALLAERFPA QATRLHQGAE ELGAEWGALA GAAQACGEAV
     AAAGRLQRFL RDLDTFLDWL VRAQEAAGAV EGPLPRSLEE ADGLLARHAA LKEEVDQREE
     DYARIVAASE ALLASEGAEL GPGLALDEWL PHLEVGWHKL LGLWEERREA LVQAHVYQLF
     LRDLCQALAV LRNQEVALSG AELPCTVESV EEAMKRHRDF LTTMELNQQK MQVAVQAAES
     LLRQGNAYGE QAQEAVARLL EKSQENQLRA QQWMQKLLDQ LVLQHFLRDC HELDGWIHEK
     MLMARDGTRE DSHKLHKRWL RHQAFMAELA QNKEWLEKIE REGQQLMQEK PELAASVRKK
     LGEIRQCWAE LESTTQAKAR QLFEASKADQ LVQSFAELDK RLLHMESQLQ DVDPGGDLAT
     VNSQLKKLQS MESQVEEWCR EVGELQAQTA ALPLEQASKE LVGERQSAVG ERLVRLLEPL
     QERRRLLLAS KELHQVAHDL DDELAWVQER LPLAMQTERG TGLQAVQQHI KKNQGLRREI
     QAHGPRLEEV LERAGVLASL RSPEAEAVRR GQEQLQSAWT GLREAAERRQ QTLDAAFQVE
     QYYFDVAEVE AWLGEQELLM MSEDKGKDEQ STLQLLKKHL QLEQGVENYE ESIAQLSRQC
     RALLEMGHPD SEQISRRQSQ VDRLYVALKE LGEERRVSLE QQYWLYQLSR QVDELEHWIA
     EKEVVAGSPE LGQDFEHVSV LQEKFSEFAS ETGTAGRERL AAVNQMVDEL IECGHTAAAT
     MAEWKDGLNE AWAELLELMG TRAQLLAASR ELHKFFSDAR ELQGQIEEKR RRLPRLTAPP
     EPRPSASSMQ RTLRAFEHDL QLLVSQVRQL QEGAAQLRTV YAGEHAEAIA SREQEVLQGW
     KELLAACEDA RLHVSSTADA LRFHSQARDL LSWMDGIAGQ IGAADKPRDV SSVEVLMNYH
     QGLKTELEAR VPELAACQEL GRSLLLNKSA MADEIQAQLD KLGSRKEEVS EKWDRHWEWL
     QQMLEVHQFA QEAVVADAWL TAQEPLLQSR ELGSSVDEVE QLIRRHEAFR KAAAAWEERF
     SSLRRLTTIE KLKAEQSKQP PTPLLGRKFF GDPTELAAKA APLLRPGGYD RGLEPLARRA
     SDTLSAEVRT RVGYVRQELK PERLQPRIDR LPETSGKVEP AAPTAAALDT TDTPGTPAAT
     EQVRPRSERQ ELADRAEELP RRRRSERQES VDQPEETARR RRPERQESAD HEGPHSLTLG
     RYEQMERRRE RRERRIERQE SSEQETPTRG ELVKGKATLA DIVEQLQEKE AGPGIPAGVP
     SLPQPRELPP GRLPNGLEPP ERTPRPDRPR ARDRPKPRRR PRPREGGEGG GSRRSRSAPA
     QGGSAPAPPP PPTHTVQHEG FLLRKRELDA NRKSSNRSWV SLYCVLSKGE LGFYKDSKGP
     ASGGTHGGEP LLSLHKATSE VASDYKKKKH VFKLQTQDGS EFLLQAKDEE EMNGWLEAVA
     NSVAEHAEIA RWGQTLPTTS STDEGNPKRE GGERRASGRR K
//
ID   BSND_MOUSE              Reviewed;         307 AA.
AC   Q8VIM4; Q8C740; Q8CHY0;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 2.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=Barttin;
GN   Name=Bsnd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6;
RX   MEDLINE=21547524; PubMed=11687798; DOI=10.1038/ng752;
RA   Birkenhaeger R., Otto E., Schuermann M.J., Vollmer M., Ruf E.-M.,
RA   Maier-Lutz I., Beekmann F., Fekete A., Omran H., Feldmann D.,
RA   Milford D.V., Jeck N., Konrad M., Landau D., Knoers N.V.A.M.,
RA   Antignac C., Sudbrak R., Kispert A., Hildebrandt F.;
RT   "Mutation of BSND causes Bartter syndrome with sensorineural deafness
RT   and kidney failure.";
RL   Nat. Genet. 29:310-314(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Cochlea;
RA   Nie L., Feng W., Dinglasan J.N., Yamoah E.N.;
RT   "Functional phenotype of inner ear-specific chloride channel ClC-K and
RT   its accessory subunit.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=11734858; DOI=10.1038/35107099;
RA   Estevez R., Boettger T., Stein V., Birkenhaeger R., Otto E.,
RA   Hildebrandt F., Jentsch T.J.;
RT   "Barttin is a Cl- channel beta-subunit crucial for renal Cl-
RT   reabsorption and inner ear K+ secretion.";
RL   Nature 414:558-561(2001).
CC   -!- FUNCTION: Functions as a beta-subunit for CLCNKA and CLCNKB
CC       chloride channels. In the kidney CLCNK/BSND heteromers mediate
CC       chloride reabsorption by facilitating its basolateral efflux. In
CC       the stria, CLCNK/BSND channels drive potassium secretion by
CC       recycling chloride for the basolateral SLC12A2 cotransporter.
CC   -!- SUBUNIT: Interacts with CLCNK channels. Forms probably heteromers
CC       with CLCNKA in the thin ascending limb of Henle and with CLCNKB in
CC       the thick ascending limb and more distal segments.
CC   -!- SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass
CC       membrane protein. Note=Staining in membranes of the renal tubule
CC       is basolateral. Also detected in basolateral membranes of
CC       intercalated cells of the collecting duct, which are known to
CC       express CLCNKB as well. Both acid-secreting alpha-intercalated
CC       cells and base-secreting beta-intercalated cells express this
CC       protein basolaterally, but intervening AQP2-expressing principal
CC       cells appear devoid of protein expression. In the inner ear,
CC       colocalizes with CLCNK in K(+)-secreting marginal cells of the
CC       stria vascularis. The basolateral staining contrasts with the
CC       apical localization of the KCNQ1 K(+) channel. Also found in K(+)-
CC       secreting vestibular dark cells, where it colocalized in
CC       basolateral membranes with CLCNK below apical membranes that
CC       expressed KCNQ1.
CC   -!- TISSUE SPECIFICITY: Expression is evident in inner and outer
CC       stripes of the outer medulla of the kidney, most probably
CC       representing thin limbs of Henle's loop together with some
CC       collecting duct coursing through the outer stripe. In situ
CC       hybridization in fetal kidney at 18.5 dpc revealed a clear
CC       continuity between hybridization signals from the thin limb of
CC       Henle's loop and the distal convoluted tubule, suggesting that
CC       part of the expression pattern may result from expression in the
CC       thick ascending limb of Henle's loop. In addition, strong signals
CC       are present in a subset of cortical tubules, representing distal
CC       convoluted tubules or cortical collecting duct. Strong expression
CC       is also observed in the inner medulla of the kidney. This
CC       expression does not extend all the way to the tip of the papilla.
CC       Thus this signal most probably represents cells of the thin
CC       ascending limbs. In the inner ear, strong and exclusive expression
CC       is detected in marginal cells of the stria vascularis. In addition
CC       to cochlear signal, expression is observed in dark cells localized
CC       at the base of the crista ampullaris of the vestibular organ.
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DR   EMBL; AF391088; AAL33907.1; -; mRNA.
DR   EMBL; AY373833; AAQ81629.1; -; mRNA.
DR   EMBL; AK052587; BAC35049.1; -; mRNA.
DR   EMBL; BC038287; AAH38287.1; -; mRNA.
DR   IPI; IPI00312342; -.
DR   RefSeq; NP_536706.2; NM_080458.2.
DR   UniGene; Mm.135448; -.
DR   STRING; Q8VIM4; -.
DR   PRIDE; Q8VIM4; -.
DR   Ensembl; ENSMUST00000054472; ENSMUSP00000049563; ENSMUSG00000025418.
DR   GeneID; 140475; -.
DR   KEGG; mmu:140475; -.
DR   UCSC; uc008tyj.1; mouse.
DR   CTD; 140475; -.
DR   MGI; MGI:2153465; Bsnd.
DR   eggNOG; roNOG14808; -.
DR   GeneTree; ENSGT00390000008549; -.
DR   HOGENOM; HBG126312; -.
DR   HOVERGEN; HBG050739; -.
DR   InParanoid; Q8VIM4; -.
DR   OrthoDB; EOG4T4CW5; -.
DR   NextBio; 369764; -.
DR   ArrayExpress; Q8VIM4; -.
DR   Bgee; Q8VIM4; -.
DR   Genevestigator; Q8VIM4; -.
DR   GermOnline; ENSMUSG00000025418; Mus musculus.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005887; C:integral to plasma membrane; IDA:UniProtKB.
DR   GO; GO:0043234; C:protein complex; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0030644; P:cellular chloride ion homeostasis; NAS:UniProtKB.
DR   GO; GO:0030007; P:cellular potassium ion homeostasis; NAS:UniProtKB.
DR   GO; GO:0007605; P:sensory perception of sound; NAS:UniProtKB.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    307       Barttin.
FT                                /FTId=PRO_0000065000.
FT   TOPO_DOM      1      5       Cytoplasmic (Potential).
FT   TRANSMEM      6     26       Helical; (Potential).
FT   TOPO_DOM     27     32       Extracellular (Potential).
FT   TRANSMEM     33     53       Helical; (Potential).
FT   TOPO_DOM     54    307       Cytoplasmic (Potential).
FT   CONFLICT     83     83       T -> A (in Ref. 1; AAL33907).
FT   CONFLICT    292    292       D -> N (in Ref. 1 and 3).
SQ   SEQUENCE   307 AA;  33814 MW;  56E37B92EC39F2C7 CRC64;
     MADEKTFRIG FIVLGLFLLS LGTFLMSHDR PQVYGTFYAM GSVMVIGGVI WSMCQCYPKI
     TFVPADSDFQ GILSPKALSL LETGLSEVKS PQPPYVRLWE EAAYDQSLPD FTHIQMKVMG
     YSEDPRPLLA PELKTGASSV REGEPRTAQA WMEAPVVVHR GSDENEGEKS HSQSSPSVGP
     QGSAPLASFH DDLDVGSSEG SSLQPSPNRD EPHRQVPWAS RGPLDRFSDF ALIDDTPTSE
     DTVLDGQARE AALPRKQQWS LRMKGETVQA RAEEPEQEEE DLYYGLPDSP GDPLPDKELG
     FEPDIQG
//
ID   IRGQ_MOUSE              Reviewed;         583 AA.
AC   Q8VIM9; Q7TNC7;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 47.
DE   RecName: Full=Immunity-related GTPase family Q protein;
GN   Name=Irgq; Synonyms=Irgq1; ORFNames=Fksg27;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wang Y.-G., Gong L.;
RT   "Molecular cloning of FKSG27, a novel gene related to cervical
RT   tumor.";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF322649; AAL33885.1; -; mRNA.
DR   EMBL; BC056347; AAH56347.1; -; mRNA.
DR   EMBL; BC080294; AAH80294.1; -; mRNA.
DR   IPI; IPI00129548; -.
DR   RefSeq; NP_694774.3; NM_153134.3.
DR   UniGene; Mm.41108; -.
DR   ProteinModelPortal; Q8VIM9; -.
DR   PhosphoSite; Q8VIM9; -.
DR   PRIDE; Q8VIM9; -.
DR   Ensembl; ENSMUST00000049020; ENSMUSP00000036699; ENSMUSG00000041037.
DR   GeneID; 210146; -.
DR   KEGG; mmu:210146; -.
DR   UCSC; uc009fpv.1; mouse.
DR   CTD; 210146; -.
DR   MGI; MGI:2667176; Irgq.
DR   eggNOG; roNOG04795; -.
DR   GeneTree; ENSGT00510000048991; -.
DR   HOGENOM; HBG126855; -.
DR   HOVERGEN; HBG081807; -.
DR   InParanoid; Q8VIM9; -.
DR   OMA; PWAAEAN; -.
DR   OrthoDB; EOG4JHCH5; -.
DR   NextBio; 372886; -.
DR   ArrayExpress; Q8VIM9; -.
DR   Bgee; Q8VIM9; -.
DR   CleanEx; MM_IRGQ; -.
DR   Genevestigator; Q8VIM9; -.
DR   GermOnline; ENSMUSG00000041037; Mus musculus.
PE   2: Evidence at transcript level;
KW   Coiled coil; Phosphoprotein.
FT   CHAIN         1    583       Immunity-related GTPase family Q protein.
FT                                /FTId=PRO_0000264464.
FT   COILED      155    179       Potential.
FT   COMPBIAS    409    574       Ala-rich.
FT   MOD_RES     203    203       Phosphothreonine (By similarity).
FT   CONFLICT    510    510       P -> T (in Ref. 2; AAH56347).
SQ   SEQUENCE   583 AA;  59323 MW;  2DDB615708C9E596 CRC64;
     MPLPQGDVTA LFLGPPGSGK SALIAALCGK NVDTVEIPDG RQDSGVPSLR AAAPGLFLGE
     LSCPPAAPGP WAAEANLLVL VLPGSEGSEE PLTPALGEAA RAALARGTPL LAVRNLRPGD
     SQNAAKARDE TAALLNSAGL GAAPLFVPPA DCSSSDRCEE LERLQVVLRT QAEALQRLLP
     PAQDGFEVLG AAELEAVREA FETGGLEAAL SWVRAGLERL GSARLDLAVA GTTNVGLVLD
     MLLGLDPGDP GAAPASAPTG PTPYPAPERP NVVLWTVPLG PTATSPAVTP HPTHYDALIL
     VTPGAPTEEN WAQVRSLVSP DAPLVGVRTD GQGEDPPEVL EEEKAQNASD GNSGDARSEG
     KKAGIGDSGC TAARSPEDEL WEVLEEAPPP VFPMRPGGLP GLGTWLQHAL PTAQAGALLL
     ALPPASPRAA RRKAAALRAG AWRPALLASL AAAAAPVPGL GWACDVALLR GQLAEWRRAL
     GLEPAAVARR ERALGLAPGV LATRTRFPGP VTRAEVEARL GSWAGEGTAG GAALSALSFL
     WPTGGAAATG GLGYRAAHGV LLQALDEMLA DAEAVLGPPE PNQ
//
ID   CPIN1_MOUSE             Reviewed;         309 AA.
AC   Q8WTY4; Q3UJW5; Q8VC24; Q91W83;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Anamorsin;
DE   AltName: Full=Cytokine-induced apoptosis inhibitor 1;
DE   AltName: Full=Fe-S cluster assembly protein DRE2 homolog;
GN   Name=Ciapin1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INDUCTION,
RP   AND DISRUPTION PHENOTYPE.
RX   PubMed=14970183; DOI=10.1084/jem.20031858;
RA   Shibayama H., Takai E., Matsumura I., Kouno M., Morii E., Kitamura Y.,
RA   Takeda J., Kanakura Y.;
RT   "Identification of a cytokine-induced antiapoptotic molecule anamorsin
RT   essential for definitive hematopoiesis.";
RL   J. Exp. Med. 199:581-592(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, DBA/2, and NOD;
RC   TISSUE=Cerebellum, Diencephalon, Spinal cord, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=16957168; DOI=10.1369/jhc.6A6960.2006;
RA   Hao Z., Li X., Qiao T., Du R., Zhang G., Fan D.;
RT   "Subcellular localization of CIAPIN1.";
RL   J. Histochem. Cytochem. 54:1437-1444(2006).
CC   -!- FUNCTION: May be required for the maturation of extramitochondrial
CC       Fe/S proteins (By similarity). Has anti-apoptotic effects in the
CC       cell. Involved in negative control of cell death upon cytokine
CC       withdrawal. Promotes development of hematopoietic cells (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- DEVELOPMENTAL STAGE: Expressed from early embryogenesis.
CC   -!- INDUCTION: By cytokines such as IL3 and THPO.
CC   -!- DISRUPTION PHENOTYPE: Death in late gestation due to defective
CC       definitive hematopoiesis in the fetal liver, possibly due to
CC       initiated apoptosis in erythroid cells during terminal maturation.
CC   -!- MISCELLANEOUS: 'Ana-mors-in' means 'anti-death molecule' in Latin.
CC   -!- SIMILARITY: Belongs to the anamorsin family.
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DR   EMBL; AY523555; AAS09959.1; -; mRNA.
DR   EMBL; AK076116; BAC36196.1; -; mRNA.
DR   EMBL; AK079615; BAC37702.1; -; mRNA.
DR   EMBL; AK088757; BAC40550.1; -; mRNA.
DR   EMBL; AK136821; BAE23137.1; -; mRNA.
DR   EMBL; AK146282; BAE27040.1; -; mRNA.
DR   EMBL; AK163705; BAE37466.1; -; mRNA.
DR   EMBL; AK168252; BAE40202.1; -; mRNA.
DR   EMBL; BC016261; AAH16261.1; -; mRNA.
DR   EMBL; BC021864; AAH21864.1; -; mRNA.
DR   EMBL; BC021949; AAH21949.1; -; mRNA.
DR   IPI; IPI00187301; -.
DR   RefSeq; NP_598902.1; NM_134141.4.
DR   UniGene; Mm.27582; -.
DR   ProteinModelPortal; Q8WTY4; -.
DR   SMR; Q8WTY4; 1-170.
DR   STRING; Q8WTY4; -.
DR   PhosphoSite; Q8WTY4; -.
DR   PRIDE; Q8WTY4; -.
DR   Ensembl; ENSMUST00000034233; ENSMUSP00000034233; ENSMUSG00000031781.
DR   GeneID; 109006; -.
DR   KEGG; mmu:109006; -.
DR   UCSC; uc009mxa.1; mouse.
DR   CTD; 109006; -.
DR   MGI; MGI:1922083; Ciapin1.
DR   eggNOG; roNOG12435; -.
DR   GeneTree; ENSGT00390000011417; -.
DR   HOGENOM; HBG316506; -.
DR   HOVERGEN; HBG051104; -.
DR   InParanoid; Q8WTY4; -.
DR   OMA; FVAVVWD; -.
DR   OrthoDB; EOG4NKBWN; -.
DR   PhylomeDB; Q8WTY4; -.
DR   NextBio; 361568; -.
DR   ArrayExpress; Q8WTY4; -.
DR   Bgee; Q8WTY4; -.
DR   CleanEx; MM_CIAPIN1; -.
DR   Genevestigator; Q8WTY4; -.
DR   GermOnline; ENSMUSG00000031781; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR   GO; GO:0006916; P:anti-apoptosis; IMP:MGI.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR   InterPro; IPR007785; Anamorsin.
DR   PANTHER; PTHR13273; DUF689; 1.
DR   Pfam; PF05093; DUF689; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Cytoplasm; Nucleus; Phosphoprotein.
FT   CHAIN         1    309       Anamorsin.
FT                                /FTId=PRO_0000079289.
FT   MOD_RES     181    181       Phosphoserine (By similarity).
FT   MOD_RES     183    183       Phosphoserine (By similarity).
FT   MOD_RES     302    302       Phosphoserine (By similarity).
FT   MOD_RES     304    304       Phosphoserine (By similarity).
SQ   SEQUENCE   309 AA;  33429 MW;  2F1FCB614767C915 CRC64;
     MEEFGISPGQ LVAVFWDKSS PEEALKKLVA RLQELTGSEG QVFMENVTQL LQSSHKESSF
     DVILSGVVPG STSLHSAEVL AEMARILRPG GCLFLKEPVE TAEVNNDKMK TASKLCSALT
     LSGLVEIKEL QREALSPEEV QSVQEHLGYH SDSLRSVRVT GKKPNFEVGS SSQLKLPNKK
     SSSVKPVVDP AAAKLWTLSA NDMEDDSVDL IDSDELLDPE DLKRPDPASL KAPSCGEGKK
     RKACKNCTCG LAEELEREQS KAQSSQPKSA CGNCYLGDAF RCANCPYLGM PAFKPGEQVL
     LSNSNLQDA
//
ID   Q91UZ1_MOUSE            Unreviewed;      1175 AA.
AC   Q91UZ1;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   SubName: Full=Phospholipase C beta 4;
DE   SubName: Full=Phospholipase C, beta 4;
DE   SubName: Full=Plcb4;
GN   Name=Plcb4; ORFNames=RP23-7A19.1-002;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ILS, and ISS;
RX   MEDLINE=21363810; PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PCR rescued clones;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RA   Lovell J.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CAST/EiJ; TISSUE=Brain;
RA   Farber C.R., Corva P.M., Medrano J.F.;
RT   "Characterization of quantitative trait loci influencing growth and
RT   adiposity using congenic mouse strains.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 PI-PLC X-box domain.
CC   -!- SIMILARITY: Contains 1 PI-PLC Y-box domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC129883; AAI29884.1; -; mRNA.
DR   EMBL; AF332071; AAK56099.1; -; mRNA.
DR   EMBL; AF332072; AAK56100.1; -; mRNA.
DR   EMBL; AY902325; AAX90610.1; -; Genomic_DNA.
DR   EMBL; AL928798; CAM26951.1; -; Genomic_DNA.
DR   IPI; IPI00625848; -.
DR   RefSeq; NP_038857.1; NM_013829.2.
DR   UniGene; Mm.38009; -.
DR   HSSP; P10688; 1DJX.
DR   ProteinModelPortal; Q91UZ1; -.
DR   SMR; Q91UZ1; 12-821.
DR   STRING; Q91UZ1; -.
DR   PhosphoSite; Q91UZ1; -.
DR   PRIDE; Q91UZ1; -.
DR   Ensembl; ENSMUST00000035646; ENSMUSP00000038409; ENSMUSG00000039943.
DR   Ensembl; ENSMUST00000110109; ENSMUSP00000105736; ENSMUSG00000039943.
DR   GeneID; 18798; -.
DR   KEGG; mmu:18798; -.
DR   UCSC; uc008mod.1; mouse.
DR   CTD; 18798; -.
DR   MGI; MGI:107464; Plcb4.
DR   HOGENOM; HBG315986; -.
DR   HOVERGEN; HBG053609; -.
DR   InParanoid; Q91UZ1; -.
DR   OMA; KEMRANQ; -.
DR   PhylomeDB; Q91UZ1; -.
DR   NextBio; 295092; -.
DR   ArrayExpress; Q91UZ1; -.
DR   Bgee; Q91UZ1; -.
DR   Genevestigator; Q91UZ1; -.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR015359; Phospholipase_C_EF-hand-like.
DR   InterPro; IPR001711; Phospholipase_C_Pinositol-sp_Y.
DR   InterPro; IPR001192; Pinositol_Phospholipase-C.
DR   InterPro; IPR016280; PLC-beta.
DR   InterPro; IPR009535; PLC-beta_CS.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:3.20.20.190; PLC-like_Pdiesterase_TIM-brl; 2.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF06631; DUF1154; 1.
DR   Pfam; PF09279; efhand_like; 1.
DR   Pfam; PF00388; PI-PLC-X; 1.
DR   Pfam; PF00387; PI-PLC-Y; 1.
DR   PIRSF; PIRSF000956; PLC-beta; 1.
DR   PRINTS; PR00390; PHPHLIPASEC.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00148; PLCXc; 1.
DR   SMART; SM00149; PLCYc; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF51695; PLC-like_Pdiesterase_TIM-brl; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Transducer.
SQ   SEQUENCE   1175 AA;  134528 MW;  FC6919002C512B48 CRC64;
     MAKPYEFNWQ KEVPSFLQEG AVFDRYEEES FVFEPNCLFK VDEFGFFLTW KSEGKEGQVL
     ECSLINSIRQ AAIPKDPKIL AALEAVGKSE NDLEGRILCV CSGTDLVNIG FTYMVAENPE
     VTKQWVEGLR SIIHNFRANN VSPMTCLKKH WMKLAFLTNT TGKIPVRSIT RTFASGKTEK
     VIFQALKELG LPSGKNDEIE PAAFTYEKFY ELTQKICPRT DIEDLFKKIN GDKTDYLTVD
     QLVSFLNEHQ RDPRLNEILF PFYDAKRAMQ IIEMYEPDEE LKKKGLISSD GFCRYLMSDE
     NAPVFLDRLE LYQEMDHPLA HYFISSSHNT YLTGRQFGGK SSVEMYRQVL LAGCRCVELD
     CWDGKGEDQE PIITHGKAMC TDILFKDVIQ AIKETAFVTS EYPVILSFEN HCSKYQQYKM
     SKYCEDLFGD LLLKQALESH PLEPGRPLPS PNDLKRKILI KNKRLKPEVE KKQLEALKSM
     MEAGESAAPA SILEDDNEEE IESADQEEEA HPEYKFGNEL SADDYSHKEA VANSVKKGLV
     TVEDEQAWMA SYKYVGATTN IHPYLSTMIN YAQPVKFQGF HVAEERNIHY NMSSFNESVG
     LGYLKTHAIE FVNYNKRQMS RIYPKGGRVD SSNYMPQIFW NAGCQMVSLN YQTPDLAMQL
     NQGKFEYNGS CGYLLKPDFM RRPDRTFDPF SETPVDGVIA ATCSVQVISG QFLSDKKIGT
     YVEVDMYGLP TDTIRKEFRT RMVMNNGLNP VYNEESFVFR KVILPDLAVL RIAVYDDNNK
     LIGQRILPLD GLQAGYRHIS LRNEGNKPLS LPTIFCNIVL KTYVPDGFGD IVDALSDPKK
     FLSITEKRAD QMRAMGIETS DIADVPSDTS KNDKKGKANP AKANVTPQSS SELRPTTTAA
     LGSGQEAKKG IELIPQVRIE DLKQMKAYLK HLKKQQKELN SLKKKHAKEH STMQKLHCTQ
     VDKIVAQYDK EKSTHEKILE KAMKKKGGSN CLEIKKETEI KIQTLTTDHK SKVKEIVAQH
     TKEWSEMINT HSAEEQEIRD LHLSQQCELL RKLLINAHEQ QTQQLKLSHD RESKEMRAHQ
     AKISMENSKA ISQDKSIKNK AERERRVREL NSSNTKKFLE ERKRLAMKQS KEMDQLKKVQ
     LEHLEFLEKQ NEQAKEMQQM VKLEAEMDRR PATVV
//
ID   TRAM1_MOUSE             Reviewed;         374 AA.
AC   Q91V04;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Translocating chain-associated membrane protein 1;
GN   Name=Tram1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Hartmann E.;
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Stimulatory or required for the translocation of
CC       secretory proteins across the ER membrane (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the TRAM family.
CC   -!- SIMILARITY: Contains 1 TLC (TRAM/LAG1/CLN8) domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY029764; AAK38167.1; -; mRNA.
DR   EMBL; AK088814; BAC40590.1; -; mRNA.
DR   EMBL; BC012401; AAH12401.1; -; mRNA.
DR   IPI; IPI00125907; -.
DR   RefSeq; NP_082449.1; NM_028173.4.
DR   UniGene; Mm.28765; -.
DR   PhosphoSite; Q91V04; -.
DR   PRIDE; Q91V04; -.
DR   Ensembl; ENSMUST00000027068; ENSMUSP00000027068; ENSMUSG00000025935.
DR   GeneID; 72265; -.
DR   KEGG; mmu:72265; -.
DR   UCSC; uc007ait.1; mouse.
DR   CTD; 72265; -.
DR   MGI; MGI:1919515; Tram1.
DR   HOGENOM; HBG445184; -.
DR   HOVERGEN; HBG054402; -.
DR   InParanoid; Q91V04; -.
DR   OMA; RWREHSS; -.
DR   OrthoDB; EOG4QVCC8; -.
DR   NextBio; 335849; -.
DR   ArrayExpress; Q91V04; -.
DR   Bgee; Q91V04; -.
DR   Genevestigator; Q91V04; -.
DR   GermOnline; ENSMUSG00000025935; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:UniProtKB-KW.
DR   InterPro; IPR006634; TLC-dom.
DR   InterPro; IPR013599; TRAM1.
DR   InterPro; IPR016447; Translocation_assoc_membrane.
DR   Pfam; PF08390; TRAM1; 1.
DR   Pfam; PF03798; TRAM_LAG1_CLN8; 1.
DR   PIRSF; PIRSF005449; Translocation_assoc_membrane; 1.
DR   SMART; SM00724; TLC; 1.
DR   PROSITE; PS50922; TLC; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycoprotein; Membrane; Phosphoprotein;
KW   Protein transport; Translocation; Transmembrane; Transmembrane helix;
KW   Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    374       Translocating chain-associated membrane
FT                                protein 1.
FT                                /FTId=PRO_0000185531.
FT   TOPO_DOM      2     29       Cytoplasmic (Potential).
FT   TRANSMEM     30     50       Helical; (Potential).
FT   TOPO_DOM     51     76       Lumenal (Potential).
FT   TRANSMEM     77     97       Helical; (Potential).
FT   TOPO_DOM     98    121       Cytoplasmic (Potential).
FT   TRANSMEM    122    142       Helical; (Potential).
FT   TOPO_DOM    143    159       Lumenal (Potential).
FT   TRANSMEM    160    180       Helical; (Potential).
FT   TOPO_DOM    181    192       Cytoplasmic (Potential).
FT   TRANSMEM    193    213       Helical; (Potential).
FT   TOPO_DOM    214    217       Lumenal (Potential).
FT   TRANSMEM    218    238       Helical; (Potential).
FT   TOPO_DOM    239    251       Cytoplasmic (Potential).
FT   TRANSMEM    252    272       Helical; (Potential).
FT   TOPO_DOM    273    297       Lumenal (Potential).
FT   TRANSMEM    298    318       Helical; (Potential).
FT   TOPO_DOM    319    374       Cytoplasmic (Potential).
FT   DOMAIN      117    326       TLC.
FT   MOD_RES     365    365       Phosphoserine.
FT   CARBOHYD     56     56       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   374 AA;  43039 MW;  E6C65250F68E4393 CRC64;
     MAIRKKSNKN PPLLSHEFLL QNHADIVSCL AMLFLLGLMF EVTAKGAIIF VALQYNVTRP
     ATEEQATESA SLYHYGIKDL ATVLFYMLVA IIIHAIIQEY VLDKINRRMH FSKTKHSKFN
     ESGQLSAFYL FACVWGTFIL ISENYISDPT ILWRAYPHNL MTFQTKFFYI SQLAYWLHAF
     PELYFQKTKK EDIPRQLVYI GLYLFHIAGA YLLNLNHLGL VLLVLHYFVE FLFHISRLFY
     FSDEKYQKGF SLWAVLFVLG RLLTLILSVL TVGFGLARAE NQKLDFSTGN FNVLAVRIAV
     LASICITQAF MMWKFINFQL RRWREHSAFQ APPVKRKPAV TKGRSSRKGT ENGVNGTVTS
     NGADSPRNRK EKSS
//
ID   WDR13_MOUSE             Reviewed;         485 AA.
AC   Q91V09;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=WD repeat-containing protein 13;
GN   Name=Wdr13;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=129, and CD-1; TISSUE=Testis;
RA   Shah V., Singh L., Kumar S.;
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 295-302, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains 5 WD repeats.
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DR   EMBL; AF353243; AAK38600.1; -; mRNA.
DR   EMBL; AF353244; AAK38601.1; -; Genomic_DNA.
DR   IPI; IPI00312767; -.
DR   RefSeq; NP_080413.2; NM_026137.4.
DR   UniGene; Mm.284162; -.
DR   ProteinModelPortal; Q91V09; -.
DR   SMR; Q91V09; 166-294, 302-329.
DR   PhosphoSite; Q91V09; -.
DR   PRIDE; Q91V09; -.
DR   Ensembl; ENSMUST00000033506; ENSMUSP00000033506; ENSMUSG00000031166.
DR   Ensembl; ENSMUST00000115623; ENSMUSP00000111286; ENSMUSG00000031166.
DR   GeneID; 73447; -.
DR   KEGG; mmu:73447; -.
DR   CTD; 73447; -.
DR   MGI; MGI:1914661; Wdr13.
DR   GeneTree; ENSGT00390000006228; -.
DR   HOGENOM; HBG716066; -.
DR   HOVERGEN; HBG055362; -.
DR   InParanoid; Q91V09; -.
DR   OMA; WISREAR; -.
DR   OrthoDB; EOG42Z4Q4; -.
DR   PhylomeDB; Q91V09; -.
DR   ArrayExpress; Q91V09; -.
DR   Bgee; Q91V09; -.
DR   CleanEx; MM_WDR13; -.
DR   Genevestigator; Q91V09; -.
DR   GermOnline; ENSMUSG00000031166; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Nucleus; Phosphoprotein; Repeat; WD repeat.
FT   CHAIN         1    485       WD repeat-containing protein 13.
FT                                /FTId=PRO_0000051362.
FT   REPEAT      170    210       WD 1.
FT   REPEAT      215    254       WD 2.
FT   REPEAT      302    341       WD 3.
FT   REPEAT      406    446       WD 4.
FT   REPEAT      451    484       WD 5.
FT   MOD_RES      70     70       Phosphoserine (By similarity).
FT   MOD_RES     116    116       Phosphoserine.
SQ   SEQUENCE   485 AA;  53664 MW;  E42F6101B7849431 CRC64;
     MAAVWQQVLA VDARYNAYRT PTFPQFRTQY IRRRSQLLRE NAKAGHPPAL RRQYLRLRGQ
     LLGQRYGPLS EPGSARAYSN SIVRSSRTTL DRMEDFEDDP RALGARGHRR SVSRGSYQLQ
     AQMNRAVYED RPPGSVVPTS VAEASRAMAG DTSLSENYAF AGMYHVFDQH VDEAVPRVRF
     ANDDRHRLAC CSLDGSISLC QLVPAPPTVL HVLRGHTRGV SDFAWSLSND ILVSTSLDAT
     MRIWASEDGR CIREIPDPDG AELLCCTFQP VNNNLTVVGN AKHNVHVMNI STGKKVKGGS
     SKLTGRVLAL SFDAPGRLLW AGDDRGSVFS FLFDMATGKL TKAKRLVVHE GSPVTSISAR
     SWVSREARDP SLLINACLNK LLLYRVVDNE GALQLKRSFP IEQSSHPVRS IFCPLMSFRQ
     GACVVTGSED MCVHFFDVER AAKAAVNKLQ GHSAPVLDVS FNCDESLLAS SDASGMVIVW
     RREQK
//
ID   S12A5_MOUSE             Reviewed;        1138 AA.
AC   Q91V14; A2A5L0; Q3UHQ2; Q7TQC9; Q80TI5; Q9Z0M7;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Solute carrier family 12 member 5;
DE   AltName: Full=Electroneutral potassium-chloride cotransporter 2;
DE   AltName: Full=K-Cl cotransporter 2;
DE            Short=mKCC2;
DE   AltName: Full=Neuronal K-Cl cotransporter;
GN   Name=Slc12a5; Synonyms=Kcc2, Kiaa1176;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=ILS, and ISS;
RX   MEDLINE=21363810; PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-227 (ISOFORM 2).
RX   MEDLINE=99177353; PubMed=10077537;
RA   Haapa S., Suomalainen S., Eerikaeinen S., Airaksinen M., Paulin L.,
RA   Savilahti H.;
RT   "An efficient DNA sequencing strategy based on bacteriophage Mu in
RT   vitro DNA transposition reaction.";
RL   Genome Res. 9:308-315(1999).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72 (ISOFORM 1), TISSUE
RP   SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=17715129; DOI=10.1074/jbc.M705095200;
RA   Uvarov P., Ludwig A., Markkanen M., Pruunsild P., Kaila K.,
RA   Delpire E., Timmusk T., Rivera C., Airaksinen M.S.;
RT   "A novel N-terminal isoform of the neuron-specific K-Cl cotransporter
RT   KCC2.";
RL   J. Biol. Chem. 282:30570-30576(2007).
RN   [8]
RP   PROTEIN SEQUENCE OF 532-538; 726-747; 813-819; 833-843; 952-961;
RP   1042-1052; 1078-1085 AND 1091-1101, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=21289258; PubMed=11395011; DOI=10.1016/S0896-6273(01)00297-5;
RA   Huebner C.A., Stein V., Hermans-Borgmeyer I., Meyer T., Ballanyi K.,
RA   Jentsch T.J.;
RT   "Disruption of KCC2 reveals an essential role of K-Cl cotransport
RT   already in early synaptic inhibition.";
RL   Neuron 30:515-524(2001).
RN   [10]
RP   INTERACTION WITH AP2A1, AND MUTAGENESIS OF 680-LEU-LEU-681 AND
RP   684-GLU-GLU-685.
RX   PubMed=18625303; DOI=10.1016/j.cellsig.2008.06.011;
RA   Zhao B., Wong A.Y.C., Murshid A., Bowie D., Presley J.F.,
RA   Bedford F.K.;
RT   "Identification of a novel di-leucine motif mediating K(+)/Cl(-)
RT   cotransporter KCC2 constitutive endocytosis.";
RL   Cell. Signal. 20:1769-1779(2008).
CC   -!- FUNCTION: Mediates electroneutral potassium-chloride cotransport
CC       in mature neurons. Transport occurs under isotonic conditions, but
CC       is activated 20-fold by cell swelling. Important for Cl(-)
CC       homeostasis in neurons.
CC   -!- SUBUNIT: Homomultimer and heteromultimer with other K-Cl
CC       cotransporters (By similarity). Interacts with AP2A1.
CC   -!- SUBCELLULAR LOCATION: Cell projection, dendrite. Cell membrane;
CC       Multi-pass membrane protein. Note=Detected on dendrites, but not
CC       on axons of spinal cord neurons and at GPHN-positive inhibitory
CC       synapses.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=KCC2a;
CC         IsoId=Q91V14-1; Sequence=Displayed;
CC       Name=2; Synonyms=KCC2b;
CC         IsoId=Q91V14-2; Sequence=VSP_029910;
CC   -!- TISSUE SPECIFICITY: Isoform 2 expressed in brainstem and spinal
CC       cord, isoform 1 expressed in brainstem, spinal cord and olfactory
CC       bulb of E17 embryos. Isoforms 1 and 2 expressed in all parts of
CC       the brain and spinal cord in postnatal day 14 mice.
CC   -!- DEVELOPMENTAL STAGE: Isoform 1 predominant isoform in E17 brain.
CC       Isoform 2 predominant isoform during postnatal development.
CC       Detected in the ventral horns of the spinal cord at E12.5, and
CC       throughout the spinal cord at birth.
CC   -!- DISRUPTION PHENOTYPE: Death at birth due to severe motor deficits
CC       including respiratory failure. Mice lacking isoform 2 die within 2
CC       weeks after birth.
CC   -!- SIMILARITY: Belongs to the SLC12A transporter family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65742.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; AF332063; AAK56092.1; -; mRNA.
DR   EMBL; AF332064; AAK56093.1; -; mRNA.
DR   EMBL; AK122460; BAC65742.1; ALT_INIT; mRNA.
DR   EMBL; AK147262; BAE27805.1; -; mRNA.
DR   EMBL; AL591495; CAM26466.1; -; Genomic_DNA.
DR   EMBL; BC054808; AAH54808.1; -; mRNA.
DR   EMBL; AJ011033; CAA09464.1; -; Genomic_DNA.
DR   IPI; IPI00465769; -.
DR   IPI; IPI00877254; -.
DR   RefSeq; NP_065066.2; NM_020333.2.
DR   UniGene; Mm.252987; -.
DR   ProteinModelPortal; Q91V14; -.
DR   STRING; Q91V14; -.
DR   PhosphoSite; Q91V14; -.
DR   PRIDE; Q91V14; -.
DR   Ensembl; ENSMUST00000017884; ENSMUSP00000017884; ENSMUSG00000017740.
DR   GeneID; 57138; -.
DR   KEGG; mmu:57138; -.
DR   CTD; 57138; -.
DR   MGI; MGI:1862037; Slc12a5.
DR   eggNOG; roNOG12599; -.
DR   GeneTree; ENSGT00560000076892; -.
DR   HOGENOM; HBG590211; -.
DR   HOVERGEN; HBG052852; -.
DR   InParanoid; Q91V14; -.
DR   OMA; TWRNFIE; -.
DR   OrthoDB; EOG4THVS8; -.
DR   NextBio; 313501; -.
DR   ArrayExpress; Q91V14; -.
DR   Bgee; Q91V14; -.
DR   CleanEx; MM_SLC12A5; -.
DR   Genevestigator; Q91V14; -.
DR   GermOnline; ENSMUSG00000017740; Mus musculus.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015379; F:potassium:chloride symporter activity; IMP:MGI.
DR   GO; GO:0007612; P:learning; IMP:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR   GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0042493; P:response to drug; IMP:MGI.
DR   GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR   GO; GO:0007268; P:synaptic transmission; IMP:MGI.
DR   GO; GO:0040040; P:thermosensory behavior; IMP:MGI.
DR   InterPro; IPR004841; AA-permease_dom.
DR   InterPro; IPR000076; KCL_cotranspt.
DR   InterPro; IPR004842; Na/K/Cl_cotransptS.
DR   Pfam; PF00324; AA_permease; 2.
DR   PRINTS; PR01081; KCLTRNSPORT.
DR   TIGRFAMs; TIGR00930; 2a30; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cell projection;
KW   Direct protein sequencing; Glycoprotein; Ion transport; Membrane;
KW   Potassium; Potassium transport; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1   1138       Solute carrier family 12 member 5.
FT                                /FTId=PRO_0000178035.
FT   TOPO_DOM      1    133       Cytoplasmic (Potential).
FT   TRANSMEM    134    154       Helical; (Potential).
FT   TRANSMEM    156    176       Helical; (Potential).
FT   TOPO_DOM    177    194       Cytoplasmic (Potential).
FT   TRANSMEM    195    215       Helical; (Potential).
FT   TRANSMEM    217    237       Helical; (Potential).
FT   TOPO_DOM    238    254       Cytoplasmic (Potential).
FT   TRANSMEM    255    275       Helical; (Potential).
FT   TRANSMEM    278    298       Helical; (Potential).
FT   TOPO_DOM    299    418       Cytoplasmic (Potential).
FT   TRANSMEM    419    439       Helical; (Potential).
FT   TRANSMEM    459    479       Helical; (Potential).
FT   TOPO_DOM    480    496       Cytoplasmic (Potential).
FT   TRANSMEM    497    517       Helical; (Potential).
FT   TRANSMEM    570    590       Helical; (Potential).
FT   TOPO_DOM    591    630       Cytoplasmic (Potential).
FT   TRANSMEM    631    651       Helical; (Potential).
FT   TRANSMEM    848    868       Helical; (Potential).
FT   TOPO_DOM    869   1138       Cytoplasmic (Potential).
FT   CARBOHYD    442    442       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    833    833       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1     40       MSRRFTVTSLPPAASAASADPESRRHSVADPRRLPREDVK
FT                                -> MLNNLTDCEDGDGGANP (in isoform 2).
FT                                /FTId=VSP_029910.
FT   MUTAGEN     680    681       LL->AA: Inhibits endocytosis. Abolishes
FT                                interaction with AP2A1.
FT   MUTAGEN     684    685       EE->AA: Decreases endocytosis.
FT   CONFLICT     64     64       Missing (in Ref. 5; AAH54808).
FT   CONFLICT    859    859       G -> D (in Ref. 3; BAE27805).
SQ   SEQUENCE   1138 AA;  126271 MW;  56059F065B89C407 CRC64;
     MSRRFTVTSL PPAASAASAD PESRRHSVAD PRRLPREDVK GDGNPKESSP FINSTDTEKG
     REYDGRNMAL FEEEMDTSPM VSSLLSGLAN YTNLPQGSRE HEEAENNEGG KKKPVQAPRM
     GTFMGVYLPC LQNIFGVILF LRLTWVVGIA GIMESFCMVF ICCSCTMLTA ISMSAIATNG
     VVPAGGSYYM ISRSLGPEFG GAVGLCFYLG TTFAGAMYIL GTIEILLAYL FPAMAIFKAE
     DASGEAAAML NNMRVYGTCV LTCMATVVFV GVKYVNKFAL VFLGCVILSI LAIYAGVIKS
     AFDPPNFPIC LLGNRTLSRH GFDVCAKLAW EGNETVTTRL WGLFCSSRLL NATCDEYFTR
     NNVTEIQGIP GAASGLIKEN LWSSYLTKGV IVERRGMPSV GLADGTPVDM DHPYVFSDMT
     SYFTLLVGIY FPSVTGIMAG SNRSGDLRDA QKSIPTGTIL AIATTSAVYI SSVVLFGACI
     EGVVLRDKFG EAVNGNLVVG TLAWPSPWVI VIGSFFSTCG AGLQSLTGAP RLLQAISRDG
     IVPFLQVFGH GKANGEPTWA LLLTACICEI GILIASLDEV APILSMFFLM CYMFVNLACA
     VQTLLRTPNW RPRFRYYHWT LSFLGMSLCL ALMFICSWYY ALVAMLIAGL IYKYIEYRGA
     EKEWGDGIRG LSLSAARYAL LRLEEGPPHT KNWRPQLLVL VRVDQDQNVV HPQLLSLTSQ
     LKAGKGLTIV GSVLEGTFLD NHPQAQRAEE SIRRLMEAEK VKGFCQVVIS SNLRDGVSHL
     IQSGGLGGLQ HNTVLVGWPR NWRQKEDHQT WRNFIELVRE TTAGHLALLV TKNVSMFPGN
     PERFSEGSID VWWIVHDGGM LMLLPFLLRH HKVWRKCKMR IFTVAQMDDN SIQMKKDLTT
     FLYHLRITAE VEVVEMHESD ISAYTYEKTL VMEQRSQILK QMHLTKNERE REIQSITDES
     RGSIRRKNPA NPRLRLNVPE ETACDNEEKP EEEVQLIHDQ SAPSCPSSSP SPGEEPEGER
     ETDPEVHLTW TKDKSVAEKN KGPSPVSSEG IKDFFSMKPE WENLNQSNVR RMHTAVRLNE
     VIVNKSRDAK LVLLNMPGPP RNRNGDENYM EFLEVLTEQL DRVMLVRGGG REVITIYS
//
ID   NRBP2_MOUSE             Reviewed;         499 AA.
AC   Q91V36; Q8R3M0;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Nuclear receptor-binding protein 2;
GN   Name=Nrbp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 191-499.
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=18619852; DOI=10.1016/j.mcn.2008.05.013;
RA   Larsson J., Forsberg M., Brannvall K., Zhang X.Q., Enarsson M.,
RA   Hedborg F., Forsberg-Nilsson K.;
RT   "Nuclear receptor binding protein 2 is induced during neural
RT   progenitor differentiation and affects cell survival.";
RL   Mol. Cell. Neurosci. 39:32-39(2008).
CC   -!- FUNCTION: May regulate apoptosis of neural progenitor cells during
CC       their differentiation.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Expressed in Purkinje cells of the cerebellum
CC       and neurons in the CA3 region of the hippocampus. Also detected in
CC       non-neural tissues including mesenchymal layer adjacent to
CC       epithelium in developing bronchi of the lung, the epithelium of
CC       the stomach as well as cells in the liver.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the cerebral cortex at E14 (at
CC       protein level). Expressed in the walls of the third and fourth
CC       ventricles, and in the hippocampus during development.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH11468.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC       Sequence=AAH12437.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; AC116487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC011468; AAH11468.1; ALT_INIT; mRNA.
DR   EMBL; BC012437; AAH12437.1; ALT_INIT; mRNA.
DR   EMBL; BC025042; AAH25042.1; -; mRNA.
DR   IPI; IPI00263549; -.
DR   RefSeq; NP_659096.1; NM_144847.1.
DR   UniGene; Mm.101946; -.
DR   ProteinModelPortal; Q91V36; -.
DR   SMR; Q91V36; 28-306, 435-493.
DR   STRING; Q91V36; -.
DR   PRIDE; Q91V36; -.
DR   Ensembl; ENSMUST00000019516; ENSMUSP00000019516; ENSMUSG00000075590.
DR   GeneID; 223649; -.
DR   KEGG; mmu:223649; -.
DR   UCSC; uc007wil.1; mouse.
DR   CTD; 223649; -.
DR   MGI; MGI:2385017; Nrbp2.
DR   eggNOG; roNOG16719; -.
DR   GeneTree; ENSGT00550000074385; -.
DR   HOGENOM; HBG715771; -.
DR   HOVERGEN; HBG082057; -.
DR   InParanoid; Q91V36; -.
DR   OMA; RTKLATF; -.
DR   OrthoDB; EOG4PNXGS; -.
DR   PhylomeDB; Q91V36; -.
DR   NextBio; 376780; -.
DR   ArrayExpress; Q91V36; -.
DR   Bgee; Q91V36; -.
DR   CleanEx; MM_NRBP2; -.
DR   Genevestigator; Q91V36; -.
DR   GermOnline; ENSMUSG00000075590; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0043524; P:negative regulation of neuron apoptosis; IMP:UniProtKB.
DR   GO; GO:0030182; P:neuron differentiation; IEP:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Neurogenesis.
FT   CHAIN         1    499       Nuclear receptor-binding protein 2.
FT                                /FTId=PRO_0000225609.
FT   DOMAIN       36    304       Protein kinase.
FT   CONFLICT    200    200       A -> V (in Ref. 2; AAH11468).
SQ   SEQUENCE   499 AA;  57348 MW;  B46B19E047549170 CRC64;
     MAAPEPAPRR GREREREDES EDESDILEES PCGRWQKRRE QVNQGNMPGI QSTFLAMDTE
     EGVEVVWNEL HFGDRKAFAA HEEKIQTMFE QLALVDHPNI VKLHKYWLDA SEARARVIFI
     TEYVSSGSLK QFLKKTKKNH KAMNARAWKR WCTQILSALS FLHACSPPII HGNLTSDTIF
     IQHNGLIKIG SVWYRIFSNA LPDDLRSPIR AEREELRNLH FFPPEYGEVN DGTAVDIFSF
     GMCALEMAVL EIQANGDTRV TEEAIARARH SLSDPNMREF ILSCLARDPA RRPSAHNLLF
     HRVLFEVHSL KLLAAHCFIQ HQYLMPENVV EEKTKAMDLH AVLAEMPQPH GPPMQWRYSE
     VSFLELDKFL EDVRNGIYPL MNFAAARPLG LPRVLAPPPE EAQKAKTPTP EPFDSETRKV
     VQMQCNLERS EDKARWHLTL LLVLEDRLHR QLTYDLLPTD SAQDLAAELV HYGFLHEDDR
     TKLAAFLETT FLKYRGTQA
//
ID   PP14A_MOUSE             Reviewed;         147 AA.
AC   Q91VC7; Q99MB9;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 14A;
DE   AltName: Full=17 kDa PKC-potentiated inhibitory protein of PP1;
DE   AltName: Full=Protein kinase C-potentiated inhibitor protein of 17 kDa;
DE            Short=CPI-17;
GN   Name=Ppp1r14a; Synonyms=Cpi17;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Smooth muscle;
RX   PubMed=12974676; DOI=10.1042/BJ20030128;
RA   Liu Q.-R., Zhang P.-W., Lin Z., Li Q.-F., Woods A.S., Troncoso J.,
RA   Uhl G.R.;
RT   "GBPI, a novel gastrointestinal- and brain-specific PP1-inhibitory
RT   protein, is activated by PKC and inactivated by PKA.";
RL   Biochem. J. 377:171-181(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yu L.;
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Inhibitor of PPP1CA. Has over 1000-fold higher
CC       inhibitory activity when phosphorylated, creating a molecular
CC       switch for regulating the phosphorylation status of PPP1CA
CC       substrates and smooth muscle contraction (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the PP1 inhibitor family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AY050672; AAL25830.1; -; mRNA.
DR   EMBL; AF352573; AAK35214.1; -; mRNA.
DR   EMBL; BC010832; AAH10832.1; -; mRNA.
DR   IPI; IPI00126719; -.
DR   RefSeq; NP_081007.2; NM_026731.3.
DR   UniGene; Mm.2343; -.
DR   ProteinModelPortal; Q91VC7; -.
DR   SMR; Q91VC7; 22-120.
DR   STRING; Q91VC7; -.
DR   PhosphoSite; Q91VC7; -.
DR   PRIDE; Q91VC7; -.
DR   Ensembl; ENSMUST00000048187; ENSMUSP00000035642; ENSMUSG00000037166.
DR   GeneID; 68458; -.
DR   KEGG; mmu:68458; -.
DR   UCSC; uc009gbn.1; mouse.
DR   CTD; 68458; -.
DR   MGI; MGI:1931139; Ppp1r14a.
DR   eggNOG; roNOG17745; -.
DR   GeneTree; ENSGT00390000003608; -.
DR   HOGENOM; HBG717795; -.
DR   HOVERGEN; HBG054419; -.
DR   InParanoid; Q91VC7; -.
DR   OMA; PIEDFIQ; -.
DR   OrthoDB; EOG4HDSW5; -.
DR   PhylomeDB; Q91VC7; -.
DR   NextBio; 327206; -.
DR   ArrayExpress; Q91VC7; -.
DR   Bgee; Q91VC7; -.
DR   Genevestigator; Q91VC7; -.
DR   GermOnline; ENSMUSG00000037166; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0042325; P:regulation of phosphorylation; IEA:InterPro.
DR   InterPro; IPR008025; PP1_inhibitor.
DR   Gene3D; G3DSA:1.10.150.220; PP1_inhibitor; 1.
DR   PANTHER; PTHR16188; PP1_inhibitor; 1.
DR   Pfam; PF05361; PP1_inhibitor; 1.
DR   SUPFAM; SSF81790; PP1_inhibitor; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Phosphoprotein; Protein phosphatase inhibitor.
FT   CHAIN         1    147       Protein phosphatase 1 regulatory subunit
FT                                14A.
FT                                /FTId=PRO_0000071487.
FT   REGION       35    120       Inhibitory.
FT   MOD_RES      26     26       Phosphoserine (By similarity).
FT   MOD_RES      38     38       Phosphothreonine (By similarity).
FT   MOD_RES     128    128       Phosphoserine (By similarity).
FT   MOD_RES     134    134       Phosphoserine (By similarity).
FT   MOD_RES     136    136       Phosphoserine (By similarity).
FT   CONFLICT    113    113       A -> G (in Ref. 2; AAK35214).
FT   CONFLICT    135    135       L -> P (in Ref. 2; AAK35214).
SQ   SEQUENCE   147 AA;  16649 MW;  1E29065ACEB39C4D CRC64;
     MAAQRLGKRV LSKLQSPSRA RGPGGSPSGL QKRHARVTVK YDRRELQRRL DVEKWIDGCL
     EELYRGRESD MPDEVNIDEL LELDSEEERC RKIQGLLEAC ANPTEDFVQE LLAKLRGLHK
     QPGFPQPSPS DDPSLSPRQD RAHTAPP
//
ID   Q91VH0_MOUSE            Unreviewed;       830 AA.
AC   Q91VH0;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   SubName: Full=Sbf2 protein;
DE   Flags: Fragment;
GN   Name=Sbf2; Synonyms=Mtmr13;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Mix FVB/N;
RC   TISSUE=Mammary tumor. WAP-TGF alpha model. 7 months old;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 myotubularin phosphatase domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC015069; AAH15069.1; -; mRNA.
DR   IPI; IPI00944186; -.
DR   UniGene; Mm.102970; -.
DR   HSSP; P08567; 1PLS.
DR   ProteinModelPortal; Q91VH0; -.
DR   STRING; Q91VH0; -.
DR   PhosphoSite; Q91VH0; -.
DR   PRIDE; Q91VH0; -.
DR   Ensembl; ENSMUST00000033058; ENSMUSP00000033058; ENSMUSG00000038371.
DR   UCSC; uc009jfd.1; mouse.
DR   MGI; MGI:1921831; Sbf2.
DR   HOGENOM; HBG358271; -.
DR   InParanoid; Q91VH0; -.
DR   ArrayExpress; Q91VH0; -.
DR   Bgee; Q91VH0; -.
DR   Genevestigator; Q91VH0; -.
DR   GO; GO:0005774; C:vacuolar membrane; IDA:MGI.
DR   GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR   GO; GO:0019902; F:phosphatase binding; IPI:MGI.
DR   GO; GO:0019208; F:phosphatase regulator activity; IDA:MGI.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IDA:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
DR   GO; GO:0051262; P:protein tetramerization; IPI:MGI.
DR   InterPro; IPR010569; Myotub-related.
DR   InterPro; IPR017906; Myotubularin_phosphatase_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF06602; Myotub-related; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   830 AA;  93823 MW;  234DA0F5B28D76E4 CRC64;
     HASEIILPKQ KEKNTSFRTF SKTIVKGAKK AGKMTIGRQY LLKKRTGTIV EERVNRPGWN
     EEDDISVSDD SELPTSTTLK ASEKSTMEQL VEKACFRDYQ RLGLGTISGN SSRSKPEYFR
     VTASNRLYSL CRSYPGLLVI PQAVQDSSLP RVARCYRHNR LPVVCWKNSR SGTLLLRSGG
     FHGKGVVGLF KSQNSPQAVS TSSLESSSSI EQEKYLQALL TAVIVHQKLR GSSTLTVRPA
     LALSPGVWAS LRSSTRLISS PTSFIDVGAR LAGKDHSASF SNSTYLQNQL LKRQAALYIF
     GEKSQLRSSK VEFAFNCEFV PVEFHEIRQV KASFKKLMRA CIPSTIPTDS EVTFLKALGD
     SEWFPQLHRI MQLAVVVSEV LENGSSVWVC LEEGWDITTQ VTSLAQLLSD PFYRTIAGFR
     TLVEKEWLSF GHKFSQRSSL ALNSQGGGFA PIFFQFLDCV HQVHNQYPTE FEFNLYYLKF
     LAFHYVSNRF KTFLLDSDYE RLEHGTLFDD KGDKHAKKGV CIWECIDKMH TRSPIFFNYL
     YSPVEVEALK PNVNVSSLKK WDYYTEETLS AGPSYDWMML TPKHFPYEES DVAGGAGPQS
     QRKTVWPCYD DVTCSQPDAL TRLFSEIEKL EHKLNQTPER WHQLWEKVTT DLKEEPRTAH
     SLRHSAGSPG IASTNVPSYQ KRPALHPLHR GLGEDQSTTT APSNGVEHRA ATLYSQYTSK
     NDENRSFEGT LYKRGALLKG WKPRWFVLDV TKHQLRYYDS GEDTSCKGHI DLAEVEMVIP
     AGPSMGAPKY TSDKAFFDLK TSKRVYNFCA QDGQSAQQWM DRIQSCISDA
//
ID   Q91VK2_MOUSE            Unreviewed;       276 AA.
AC   Q91VK2;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   SubName: Full=Eef1d protein;
DE   SubName: Full=MCG22130, isoform CRA_b;
GN   Name=Eef1d; ORFNames=mCG_22130;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Mix FVB/N;
RC   TISSUE=Mammary tumor. WAP-TGF alpha model. 7 months old;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family.
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DR   EMBL; BC013059; AAH13059.1; -; mRNA.
DR   EMBL; CH466545; EDL29496.1; -; Genomic_DNA.
DR   IPI; IPI00468771; -.
DR   UniGene; Mm.258927; -.
DR   HSSP; P24534; 1B64.
DR   ProteinModelPortal; Q91VK2; -.
DR   SMR; Q91VK2; 187-276.
DR   STRING; Q91VK2; -.
DR   Ensembl; ENSMUST00000089680; ENSMUSP00000087109; ENSMUSG00000055762.
DR   Ensembl; ENSMUST00000109976; ENSMUSP00000105603; ENSMUSG00000055762.
DR   UCSC; uc007whl.1; mouse.
DR   MGI; MGI:1913906; Eef1d.
DR   GeneTree; ENSGT00390000011747; -.
DR   HOVERGEN; HBG000787; -.
DR   PhylomeDB; Q91VK2; -.
DR   ArrayExpress; Q91VK2; -.
DR   Bgee; Q91VK2; -.
DR   Genevestigator; Q91VK2; -.
DR   GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro.
DR   InterPro; IPR018940; EF-1_beta_acid_region_euk.
DR   InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6.
DR   InterPro; IPR001326; Transl_elong_EF1B_B/D_CS.
DR   InterPro; IPR014038; Transl_elong_fac_EF1B_bsu/dsu.
DR   Gene3D; G3DSA:3.30.70.60; Transl_elong_EF1B/rib_con; 1.
DR   Pfam; PF10587; EF-1_beta_acid; 1.
DR   Pfam; PF00736; EF1_GNE; 1.
DR   SMART; SM00888; EF1_GNE; 1.
DR   SUPFAM; SSF54984; Transl_elong_EF1B_B/D_G_exch; 1.
DR   PROSITE; PS00824; EF1BD_1; 1.
DR   PROSITE; PS00825; EF1BD_2; 1.
PE   2: Evidence at transcript level;
KW   Elongation factor; Protein biosynthesis.
SQ   SEQUENCE   276 AA;  30634 MW;  478F5DBFA2AAD142 CRC64;
     MATNFLAHEK IWFDKFKYDD AERRFYEQMN GPVTSGSRQL KVMLPNSPEA LGQATPGTSS
     GPGASSGPGG DHSELIVRIT SLEVENQNLR GVVQDLQQAI SKLEARLSSL EKSSPTPRAT
     APQTQHVSPM RQVEPPTKKG ATPAEDDEDK DIDLFGSDEE EEDKEAARLR EERLRQYAEK
     KAKKPTLVAK SSILLDVKPW DDETDMAQLE TCVRSIQLDG LVWGASKLVP VGYGIRKLQI
     QCVVEDDKVG TDLLEEEITK FEEHVQSVDI AAFNKI
//
ID   ITM2C_MOUSE             Reviewed;         269 AA.
AC   Q91VK4; Q9JI06; Q9JME8;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Integral membrane protein 2C;
DE   AltName: Full=Transmembrane protein BRI3;
DE   Contains:
DE     RecName: Full=CT-BRI3;
GN   Name=Itm2c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RX   MEDLINE=20145471; PubMed=10679242; DOI=10.1006/bbrc.2000.2170;
RA   Inoue S., Sano H., Ohta M.;
RT   "Growth suppression of Escherichia coli by induction of expression of
RT   mammalian genes with transmembrane or ATPase domains.";
RL   Biochem. Biophys. Res. Commun. 268:553-561(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=21186070; PubMed=11290423; DOI=10.1016/S0378-1119(01)00374-2;
RA   Vidal R., Calero M., Revesz T., Plant G., Ghiso J., Frangione B.;
RT   "Sequence, genomic structure and tissue expression of human BRI3, a
RT   member of the BRI gene family.";
RL   Gene 266:95-102(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR;
RX   MEDLINE=21662689; PubMed=11804340;
RA   Choi S.C., Kim J., Kim T.H., Cho S.Y., Park S.S., Kim K.D., Lee S.H.;
RT   "Cloning and characterization of a type II integral transmembrane
RT   protein gene, Itm2c, that is highly expressed in the mouse brain.";
RL   Mol. Cells 12:391-397(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=14592447; DOI=10.1016/j.bbrc.2003.10.038;
RA   Wu H., Liu G., Li C., Zhao S.;
RT   "bri3, a novel gene, participates in tumor necrosis factor-alpha-
RT   induced cell death.";
RL   Biochem. Biophys. Res. Commun. 311:518-524(2003).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=15606899; DOI=10.1111/j.1471-4159.2004.02840.x;
RA   Wickham L., Benjannet S., Marcinkiewicz E., Chretien M., Seidah N.G.;
RT   "Beta-amyloid protein converting enzyme 1 and brain-specific type II
RT   membrane protein BRI3: binding partners processed by furin.";
RL   J. Neurochem. 92:93-102(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-39, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Negative regulator of beta amyloid peptide production.
CC       May inhibit the processing of APP by blocking its access to alpha-
CC       and beta-secretase. Binding to the beta-secretase-cleaved APP C-
CC       terminal fragment is negligible, suggesting that ITM2C is a poor
CC       gamma-secretase cleavage inhibitor. May play a role in TNF-induced
CC       cell death and neuronal differentiation.
CC   -!- SUBUNIT: Interacts with BACE1. Interacts with APP. Interacts with
CC       STMN2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane; Single-pass type II
CC       membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, especially in the
CC       cortex, hippocampus, cerebellum and olfactory lobe.
CC   -!- PTM: Type I membrane-bound, as well as soluble, furin has a pre-
CC       eminent role in ITM2C proteolytic processing. PCSK7 and PCSK5 may
CC       also be involved although to a lesser extent. The soluble form of
CC       PCSK7 is incapable of processing ITM2C (By similarity).
CC   -!- SIMILARITY: Belongs to the ITM2 family.
CC   -!- SIMILARITY: Contains 1 BRICHOS domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB030199; BAA92762.1; -; mRNA.
DR   EMBL; AF272044; AAF89493.1; -; mRNA.
DR   EMBL; AF282981; AAK00277.1; -; mRNA.
DR   EMBL; AK036377; BAC29403.1; -; mRNA.
DR   EMBL; BC012952; AAH12952.1; -; mRNA.
DR   IPI; IPI00471120; -.
DR   RefSeq; NP_071862.2; NM_022417.3.
DR   UniGene; Mm.29870; -.
DR   ProteinModelPortal; Q91VK4; -.
DR   STRING; Q91VK4; -.
DR   PhosphoSite; Q91VK4; -.
DR   PRIDE; Q91VK4; -.
DR   Ensembl; ENSMUST00000027425; ENSMUSP00000027425; ENSMUSG00000026223.
DR   GeneID; 64294; -.
DR   KEGG; mmu:64294; -.
DR   UCSC; uc007buo.1; mouse.
DR   CTD; 64294; -.
DR   MGI; MGI:1927594; Itm2c.
DR   GeneTree; ENSGT00390000005162; -.
DR   HOGENOM; HBG446485; -.
DR   HOVERGEN; HBG059373; -.
DR   InParanoid; Q91VK4; -.
DR   OMA; NANDSYE; -.
DR   OrthoDB; EOG40ZQZG; -.
DR   PhylomeDB; Q91VK4; -.
DR   NextBio; 320009; -.
DR   ArrayExpress; Q91VK4; -.
DR   Bgee; Q91VK4; -.
DR   CleanEx; MM_ITM2C; -.
DR   Genevestigator; Q91VK4; -.
DR   GermOnline; ENSMUSG00000026223; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005624; C:membrane fraction; TAS:MGI.
DR   GO; GO:0005524; F:ATP binding; IDA:MGI.
DR   GO; GO:0012502; P:induction of programmed cell death; IMP:UniProtKB.
DR   InterPro; IPR007084; BRICHOS.
DR   Pfam; PF04089; BRICHOS; 1.
DR   PROSITE; PS50869; BRICHOS; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Glycoprotein; Lysosome; Membrane;
KW   Phosphoprotein; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN         1    269       Integral membrane protein 2C.
FT                                /FTId=PRO_0000154827.
FT   PEPTIDE     244    269       CT-BRI3.
FT                                /FTId=PRO_0000232646.
FT   TRANSMEM     57     77       Helical; Signal-anchor for type II
FT                                membrane protein; (Potential).
FT   DOMAIN      138    232       BRICHOS.
FT   SITE        243    244       Cleavage; by furin (By similarity).
FT   MOD_RES      39     39       Phosphothreonine.
FT   CARBOHYD    171    171       N-linked (GlcNAc...) (Potential).
FT   CONFLICT     12     12       Missing (in Ref. 1; BAA92762).
FT   CONFLICT    246    246       G -> A (in Ref. 5; AAH12952).
SQ   SEQUENCE   269 AA;  30482 MW;  B949E6E05EA65502 CRC64;
     MVKISFQPAV AGIKADKADK AAASGPASAS APAAEILLTP AREERPPRHR SRKGGSVGGV
     CYLSMGMVVL LMGLVFASVY IYRYFFLAQL ARDNFFHCGV LYEDSLSSQI RTRLELEEDV
     KIYLEENYER INVPVPQFGG GDPADIIHDF QRGLTAYHDI SLDKCYVIEL NTTIVLPPRN
     FWELLMNVKR GTYLPQTYII QEEMVVTEHV RDKEALGSFI YHLCNGKDTY RLRRRSTRRR
     INKRGGKNCN AIRHFENTFV VETLICGVV
//
ID   TE2IP_MOUSE             Reviewed;         393 AA.
AC   Q91VL8; D3YWE8; Q543F4; Q8C2Y1; Q9JJE8; Q9JJE9;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Telomeric repeat-binding factor 2-interacting protein 1;
DE            Short=TERF2-interacting telomeric protein 1;
DE            Short=TRF2-interacting telomeric protein 1;
DE   AltName: Full=Repressor/activator protein 1 homolog;
DE            Short=RAP1 homolog;
GN   Name=Terf2ip; Synonyms=Rap1; ORFNames=MNCb-0448, MNCb-0628;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Eye, Head, Heart, Ovary, Oviduct, Pancreas, Testis, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-286.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S.,
RA   Hashimoto K.;
RT   "Isolation of full-length cDNA clones from mouse brain cDNA library
RT   made by oligo-capping method.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   BIDIRECTIONAL PROMOTER WITH KARS.
RX   PubMed=14659874; DOI=10.1016/j.gene.2003.08.026;
RA   Tan M., Wei C., Price C.M.;
RT   "The telomeric protein Rap1 is conserved in vertebrates and is
RT   expressed from a bidirectional promoter positioned between the Rap1
RT   and KARS genes.";
RL   Gene 323:1-10(2003).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20622869; DOI=10.1038/ncb2081;
RA   Martinez P., Thanasoula M., Carlos A.R., Gomez-Lopez G., Tejera A.M.,
RA   Schoeftner S., Dominguez O., Pisano D.G., Tarsounas M., Blasco M.A.;
RT   "Mammalian Rap1 controls telomere function and gene expression through
RT   binding to telomeric and extratelomeric sites.";
RL   Nat. Cell Biol. 12:768-780(2010).
RN   [9]
RP   FUNCTION IN NF-KAPPA-B PATHWAY, SUBCELLULAR LOCATION, AND INTERACTION
RP   WITH TERF2; CHUK; IKBKB AND IKBKG.
RX   PubMed=20622870; DOI=10.1038/ncb2080;
RA   Teo H., Ghosh S., Luesch H., Ghosh A., Wong E.T., Malik N., Orth A.,
RA   de Jesus P., Perry A.S., Oliver J.D., Tran N.L., Speiser L.J.,
RA   Wong M., Saez E., Schultz P., Chanda S.K., Verma I.M., Tergaonkar V.;
RT   "Telomere-independent Rap1 is an IKK adaptor and regulates NF-kappaB-
RT   dependent gene expression.";
RL   Nat. Cell Biol. 12:758-767(2010).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INTERACTION
RP   WITH TERF2.
RX   PubMed=20339076; DOI=10.1126/science.1185100;
RA   Sfeir A., Kabir S., van Overbeek M., Celli G.B., de Lange T.;
RT   "Loss of Rap1 induces telomere recombination in the absence of NHEJ or
RT   a DNA damage signal.";
RL   Science 327:1657-1661(2010).
CC   -!- FUNCTION: Acts both as a regulator of telomere function and as a
CC       transcription regulator. Involved in the regulation of telomere
CC       length and protection as a component of the shelterin complex
CC       (telosome). In contrast to other components of the shelterin
CC       complex, it is dispensible for telomere capping and does not
CC       participate in the protection of telomeres against non-homologous
CC       end-joining (NHEJ)-mediated repair. Instead, it is required to
CC       negatively regulate telomere recombination and is essential for
CC       repressing homology-directed repair (HDR), which can affect
CC       telomere length. Does not bind DNA directly: recruited to
CC       telomeric double-stranded 5'-TTAGGG-3' repeats via its interaction
CC       with TERF2. Independently of its function in telomeres, also acts
CC       as a transcription regulator: recruited to extratelomeric 5'-
CC       TTAGGG-3' sites via its association with TERF2 or other factors,
CC       and regulates gene expression. When cytoplasmic, associates with
CC       the I-kappa-B-kinase (IKK) complex and acts as a regulator of the
CC       NF-kappa-B signaling by promoting IKK-mediated phosphorylation of
CC       RELA/p65, leading to activate expression of NF-kappa-B target
CC       genes.
CC   -!- SUBUNIT: Homodimer. Component of the shelterin complex (telosome)
CC       composed of TERF1, TERF2, TINF2, TERF2IP ACD and POT1. Binds to
CC       TERF2 (but not TERF1) with its C-terminus. Interacts with
CC       SLX4/BTBD12 (By similarity). Interacts with TERF2; the interaction
CC       is direct. Does not interact with TERF1. Associates with the I-
CC       kappa-B-kinase (IKK) core complex, composed of CHUK, IKBKB and
CC       IKBKG.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Chromosome. Chromosome,
CC       telomere. Note=Associates with chromosomes, both at telomeres and
CC       in extratelomeric sites. Also exists as a cytoplasmic form, where
CC       it associates with the IKK complex.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice are viable and fertile. No major
CC       telomere dysfunction such as telomere fusions are observed. An
CC       increased telomere fragility and recombination due to defects in
CC       HDR are however present. Mice with conditional deletion in
CC       stratified epithelia display shorter telomeres and developed skin
CC       hyperpigmentation in adulthood.
CC   -!- MISCELLANEOUS: Shares a bidirectional promoter with KARS
CC       (PubMed:14659874). This shared promoter with an essential gene
CC       complicated the task when generating knockout mice; the problem
CC       was overcome by generating conditional knockout strategies
CC       (PubMed:20339076 and PubMed:20622869;).
CC   -!- SIMILARITY: Belongs to the RAP1 family.
CC   -!- SIMILARITY: Contains 1 BRCT domain.
CC   -!- SIMILARITY: Contains 1 Myb-like domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA95043.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; AK041613; BAC31005.1; -; mRNA.
DR   EMBL; AK051818; BAC34781.1; -; mRNA.
DR   EMBL; AK081557; BAC38258.1; -; mRNA.
DR   EMBL; AK087729; BAC39985.1; -; mRNA.
DR   EMBL; AK084563; BAC39217.1; -; mRNA.
DR   EMBL; AK148508; BAE28592.1; -; mRNA.
DR   EMBL; AK148537; BAE28607.1; -; mRNA.
DR   EMBL; AK161452; BAE36404.1; -; mRNA.
DR   EMBL; AK165074; BAE38026.1; -; mRNA.
DR   EMBL; AC114648; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC012270; AAH12270.1; -; mRNA.
DR   EMBL; BC017641; AAH17641.1; -; mRNA.
DR   EMBL; AB041557; BAA95042.1; -; mRNA.
DR   EMBL; AB041559; BAA95043.1; ALT_INIT; mRNA.
DR   IPI; IPI00127014; -.
DR   RefSeq; NP_065609.2; NM_020584.2.
DR   UniGene; Mm.213064; -.
DR   ProteinModelPortal; Q91VL8; -.
DR   SMR; Q91VL8; 129-187, 300-392.
DR   STRING; Q91VL8; -.
DR   PhosphoSite; Q91VL8; -.
DR   PRIDE; Q91VL8; -.
DR   Ensembl; ENSMUST00000052138; ENSMUSP00000052170; ENSMUSG00000033430.
DR   GeneID; 57321; -.
DR   KEGG; mmu:57321; -.
DR   CTD; 57321; -.
DR   MGI; MGI:1929871; Terf2ip.
DR   eggNOG; maNOG08331; -.
DR   GeneTree; ENSGT00390000005351; -.
DR   HOGENOM; HBG713232; -.
DR   HOVERGEN; HBG054209; -.
DR   InParanoid; Q91VL8; -.
DR   OMA; HGGGTVC; -.
DR   PhylomeDB; Q91VL8; -.
DR   NextBio; 313686; -.
DR   ArrayExpress; Q91VL8; -.
DR   Bgee; Q91VL8; -.
DR   Genevestigator; Q91VL8; -.
DR   GermOnline; ENSMUSG00000033430; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0048239; P:negative regulation of DNA recombination at telomere; IMP:UniProtKB.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IDA:UniProtKB.
DR   GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR   GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IMP:UniProtKB.
DR   GO; GO:0010833; P:telomere maintenance via telomere lengthening; IMP:UniProtKB.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR015010; Myb_DNA-bd_2.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Pfam; PF08914; Myb_DNA-bind_2; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
DR   PROSITE; PS50172; BRCT; FALSE_NEG.
DR   PROSITE; PS50090; MYB_LIKE; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Chromosome; Cytoplasm; Nucleus;
KW   Phosphoprotein; Telomere; Transcription; Transcription regulation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    393       Telomeric repeat-binding factor 2-
FT                                interacting protein 1.
FT                                /FTId=PRO_0000197127.
FT   DOMAIN       78    101       BRCT.
FT   DOMAIN      125    185       Myb-like.
FT   MOTIF       377    393       Nuclear localization signal (Potential).
FT   COMPBIAS    232    297       Asp/Glu-rich (acidic).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      36     36       Phosphoserine (By similarity).
FT   MOD_RES     151    151       Phosphoserine (By similarity).
FT   MOD_RES     153    153       Phosphoserine (By similarity).
FT   MOD_RES     200    200       Phosphoserine.
FT   MOD_RES     202    202       Phosphoserine (By similarity).
FT   MOD_RES     203    203       Phosphoserine (By similarity).
FT   CONFLICT    281    286       PTPEED -> HTHTQS (in Ref. 4; BAA95042/
FT                                BAA95043).
SQ   SEQUENCE   393 AA;  43353 MW;  7A15CFD83733BE2D CRC64;
     MAEAMDLGKD PNGPTHSSTL FVREDGSAMS FYVRPSSAKR RLSTLILHGG GTVCRVQEPG
     AVLLAQPGEA LAEASGDFIS TQYILDCVDR NEKLDLEAYR LGLTEQASDP KPGASTEGST
     EPEPQPLTGR IAYTDAEDVA ILTYVKENAR SPSSVTGNAL WKAMEKSSLT QHSWQSLKDR
     YLKHLRGQEH KYLLGNAPVS PSSQKLKRKA EQDPEAADSG EPQNKRAPDL PEEECVKGEI
     KENGEADNKL FEEAAPEFGE AVVDESPDFE IHITMCDGDP PTPEEDSETQ PDEEEEEPKV
     STQEVGTAIK VIRQLMEKFN LDLSTVTQAL LKNSGELEAT SSFLESGRRP DGYPIWCRQD
     DLDLQKDDDD TKNALVKKFG AQNVARRIEF RKK
//
ID   CHCH6_MOUSE             Reviewed;         273 AA.
AC   Q91VN4;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 45.
DE   RecName: Full=Coiled-coil-helix-coiled-coil-helix domain-containing protein 6;
GN   Name=Chchd6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N-3; TISSUE=Mammary gland, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 CHCH domain.
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DR   EMBL; BC011331; AAH11331.1; -; mRNA.
DR   EMBL; BC052929; AAH52929.1; -; mRNA.
DR   IPI; IPI00313390; -.
DR   UniGene; Mm.20313; -.
DR   STRING; Q91VN4; -.
DR   PhosphoSite; Q91VN4; -.
DR   PRIDE; Q91VN4; -.
DR   Ensembl; ENSMUST00000032172; ENSMUSP00000032172; ENSMUSG00000030086.
DR   UCSC; uc009cwh.1; mouse.
DR   MGI; MGI:1913348; Chchd6.
DR   HOGENOM; HBG506924; -.
DR   HOVERGEN; HBG050936; -.
DR   InParanoid; Q91VN4; -.
DR   OrthoDB; EOG4P2Q3B; -.
DR   NextBio; 320622; -.
DR   ArrayExpress; Q91VN4; -.
DR   Bgee; Q91VN4; -.
DR   Genevestigator; Q91VN4; -.
DR   GermOnline; ENSMUSG00000030086; Mus musculus.
DR   InterPro; IPR007964; DUF737.
DR   Pfam; PF05300; DUF737; 1.
PE   2: Evidence at transcript level;
FT   CHAIN         1    273       Coiled-coil-helix-coiled-coil-helix
FT                                domain-containing protein 6.
FT                                /FTId=PRO_0000129170.
FT   DOMAIN      228    269       CHCH.
SQ   SEQUENCE   273 AA;  29799 MW;  0B7344E4AD0B11B2 CRC64;
     MGSAESAEAR RVSFEMDEEE RVRVLQGIRL SESVVNRMKD CSQPSAGEQL VPGFGPSSSA
     PVPTVPLPAI SVPTVPAPTT PVPTAPSSSV RGLPGGTCKG PLTDVKVPSA ESGGGLQSSA
     VKEDLKKFQQ EQLAVQDEMV RVAKKEKEAA EKHLKASLPK KKASLTHEQQ QSARLARELE
     DREAELSRCD TFYKEQQGRI QEKNAELYKL SSQQFHEAAS KAESTIKPRR VEPVCSGLQA
     QILRCYRDHL HEVLLCSDLV KAYQHCVSTA RKG
//
ID   ATPG_MOUSE              Reviewed;         298 AA.
AC   Q91VR2;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   11-JAN-2011, entry version 85.
DE   RecName: Full=ATP synthase subunit gamma, mitochondrial;
DE   AltName: Full=F-ATPase gamma subunit;
DE   Flags: Precursor;
GN   Name=Atp5c1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 68-79; 91-136; 144-154; 263-277 AND 286-298, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [3]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79; LYS-90 AND LYS-115, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
CC       synthase or Complex V) produces ATP from ADP in the presence of a
CC       proton gradient across the membrane which is generated by electron
CC       transport complexes of the respiratory chain. F-type ATPases
CC       consist of two structural domains, F(1) - containing the
CC       extramembraneous catalytic core, and F(0) - containing the
CC       membrane proton channel, linked together by a central stalk and a
CC       peripheral stalk. During catalysis, ATP synthesis in the catalytic
CC       domain of F(1) is coupled via a rotary mechanism of the central
CC       stalk subunits to proton translocation. Part of the complex F(1)
CC       domain and the central stalk which is part of the complex rotary
CC       element. The gamma subunit protrudes into the catalytic domain
CC       formed of alpha(3)beta(3). Rotation of the central stalk against
CC       the surrounding alpha(3)beta(3) subunits leads to hydrolysis of
CC       ATP in three separate catalytic sites on the beta subunits.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel. CF(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC       has three main subunits: a, b and c.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane;
CC       Peripheral membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the ATPase gamma chain family.
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DR   EMBL; BC010700; AAH10700.1; -; mRNA.
DR   IPI; IPI00313475; -.
DR   RefSeq; NP_065640.2; NM_020615.4.
DR   UniGene; Mm.12677; -.
DR   UniGene; Mm.391281; -.
DR   ProteinModelPortal; Q91VR2; -.
DR   SMR; Q91VR2; 26-297.
DR   STRING; Q91VR2; -.
DR   PhosphoSite; Q91VR2; -.
DR   UCD-2DPAGE; Q91VR2; -.
DR   PRIDE; Q91VR2; -.
DR   Ensembl; ENSMUST00000114897; ENSMUSP00000110547; ENSMUSG00000025781.
DR   GeneID; 11949; -.
DR   KEGG; mmu:11949; -.
DR   CTD; 11949; -.
DR   MGI; MGI:1261437; Atp5c1.
DR   HOGENOM; HBG586593; -.
DR   HOVERGEN; HBG000933; -.
DR   InParanoid; Q91VR2; -.
DR   OMA; LCGAVHT; -.
DR   PhylomeDB; Q91VR2; -.
DR   NextBio; 280065; -.
DR   ArrayExpress; Q91VR2; -.
DR   Bgee; Q91VR2; -.
DR   Genevestigator; Q91VR2; -.
DR   GermOnline; ENSMUSG00000025781; Mus musculus.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:hydrogen ion transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR000131; ATPase_F1-cplx_gsu.
DR   PANTHER; PTHR11693; ATPase_F1_gamma; 1.
DR   Pfam; PF00231; ATP-synt; 1.
DR   PRINTS; PR00126; ATPASEGAMMA.
DR   SUPFAM; SSF52943; ATPase_gamma; 1.
DR   TIGRFAMs; TIGR01146; ATPsyn_F1gamma; 1.
DR   PROSITE; PS00153; ATPASE_GAMMA; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP synthesis; CF(1); Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Phosphoprotein; Transit peptide;
KW   Transport.
FT   TRANSIT       1     25       Mitochondrion.
FT   CHAIN        26    298       ATP synthase subunit gamma,
FT                                mitochondrial.
FT                                /FTId=PRO_0000002686.
FT   MOD_RES      55     55       N6-acetyllysine (By similarity).
FT   MOD_RES      79     79       N6-acetyllysine.
FT   MOD_RES      90     90       N6-acetyllysine.
FT   MOD_RES     115    115       N6-acetyllysine.
FT   MOD_RES     146    146       Phosphoserine.
FT   MOD_RES     154    154       N6-acetyllysine (By similarity).
FT   MOD_RES     197    197       N6-acetyllysine (By similarity).
SQ   SEQUENCE   298 AA;  32886 MW;  9BD63134AEFF3ABA CRC64;
     MFSRASVVGL SACAVQPQWI QVRNMATLKD ITRRLKSIKN IQKITKSMKM VAAAKYARAE
     RELKPARVYG TGSLALYEKA DIKAPEDKKK HLIIGVSSDR GLCGAIHSSV AKQMKNEVAA
     LTAAGKEVMI VGVGEKIKGI LYRTHSDQFL VSFKDVGRKP PTFGDASVIA LELLNSGYEF
     DEGSIIFNQF KSVISYKTEE KPIFSLNTIA TAETMSIYDD IDADVLQNYQ EYNLANLIYY
     SLKESTTSEQ SARMTAMDNA SKNASDMIDK LTLTFNRTRQ AVITKELIEI ISGAAALD
//
ID   DCA11_MOUSE             Reviewed;         549 AA.
AC   Q91VU6; Q3U836; Q8JZV8;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=DDB1- and CUL4-associated factor 11;
DE   AltName: Full=WD repeat-containing protein 23;
GN   Name=Dcaf11; Synonyms=D14Ucla1, Wdr23;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Colon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Liver, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-73 AND SER-75,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May function as a substrate receptor for CUL4-DDB1 E3
CC       ubiquitin-protein ligase complex (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with DDB1 and CUL4A (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q91VU6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q91VU6-2; Sequence=VSP_008425, VSP_008426;
CC   -!- SIMILARITY: Contains 7 WD repeats.
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DR   EMBL; AK033540; BAC28348.1; -; mRNA.
DR   EMBL; AK152395; BAE31183.1; -; mRNA.
DR   EMBL; BC008545; AAH08545.1; -; mRNA.
DR   EMBL; BC037001; AAH37001.1; -; mRNA.
DR   IPI; IPI00127271; -.
DR   IPI; IPI00378419; -.
DR   RefSeq; NP_001185938.1; NM_001199009.1.
DR   RefSeq; NP_598495.1; NM_133734.3.
DR   UniGene; Mm.11535; -.
DR   ProteinModelPortal; Q91VU6; -.
DR   SMR; Q91VU6; 170-535.
DR   STRING; Q91VU6; -.
DR   PhosphoSite; Q91VU6; -.
DR   PRIDE; Q91VU6; -.
DR   Ensembl; ENSMUST00000072530; ENSMUSP00000072344; ENSMUSG00000022214.
DR   Ensembl; ENSMUST00000117236; ENSMUSP00000113014; ENSMUSG00000022214.
DR   Ensembl; ENSMUST00000121622; ENSMUSP00000113202; ENSMUSG00000022214.
DR   GeneID; 28199; -.
DR   KEGG; mmu:28199; -.
DR   UCSC; uc007tyz.1; mouse.
DR   UCSC; uc007tza.1; mouse.
DR   CTD; 28199; -.
DR   MGI; MGI:90168; Dcaf11.
DR   GeneTree; ENSGT00600000084531; -.
DR   HOGENOM; HBG318747; -.
DR   HOVERGEN; HBG055176; -.
DR   InParanoid; Q91VU6; -.
DR   OMA; EEHDSAW; -.
DR   OrthoDB; EOG44TP7K; -.
DR   PhylomeDB; Q91VU6; -.
DR   NextBio; 306796; -.
DR   ArrayExpress; Q91VU6; -.
DR   Bgee; Q91VU6; -.
DR   CleanEx; MM_WDR23; -.
DR   Genevestigator; Q91VU6; -.
DR   GermOnline; ENSMUSG00000022214; Mus musculus.
DR   GO; GO:0080008; C:CUL4 RING ubiquitin ligase complex; ISS:UniProtKB.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   InterPro; IPR017399; WD_repeat_p23.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 4.
DR   PIRSF; PIRSF038135; WD_repeat_p23; 1.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein; Repeat; Ubl conjugation pathway;
KW   WD repeat.
FT   CHAIN         1    549       DDB1- and CUL4-associated factor 11.
FT                                /FTId=PRO_0000051372.
FT   REPEAT      170    210       WD 1.
FT   REPEAT      216    258       WD 2.
FT   REPEAT      263    302       WD 3.
FT   REPEAT      305    345       WD 4.
FT   REPEAT      353    392       WD 5.
FT   REPEAT      435    480       WD 6.
FT   REPEAT      481    520       WD 7.
FT   MOD_RES      21     21       Phosphoserine.
FT   MOD_RES      73     73       Phosphoserine.
FT   MOD_RES      75     75       Phosphoserine.
FT   VAR_SEQ       1     44       Missing (in isoform 2).
FT                                /FTId=VSP_008425.
FT   VAR_SEQ      45     51       VLAYLLR -> MKMWIWP (in isoform 2).
FT                                /FTId=VSP_008426.
SQ   SEQUENCE   549 AA;  61992 MW;  0ACECBEC90887352 CRC64;
     MGSRNSSSAG SGSLEPSEGL SRRGTGLRRS EEEEEEDEDV DLAQVLAYLL RRGQVRLVQG
     RGAANLQLIQ ALSDSEEEHD SAWDGRLGDR YNPPVDATPD TRELEYNEIK TQVGLATGRL
     GLRRTALQQS FPQMLHQRER GLCHRGSFSL GEQSRVMSHF LPNDLSFTDT YSQKAFCGIY
     SKDGQIFMSA CQDQTIRLYD CRYGRFHKFK SIKARDVGWS VLDVAFTPDG NHFLYSSWSD
     YIHICNIYGE GDTHTALDLR PDERRFAVFS IAVSSDGREV LGGANDGCLY VFDREQNRRT
     LQIESHEDDV NAVAFADISS QILFSGGDDA ICKVWDRRTM REDDPKPVGA LAGHQDGITF
     IDSKGDARYL ISNSKDQTIK LWDIRRFSSR EGMEASRLAA TQQNWDYRWQ QVPKIAWKKL
     KLPGDSSLMT YRGHGVLHTL IRCRFSPAHS TGQQFIYSGC STGKVVVYDL LSGHIVKKLT
     NHKACVRDVS WHPFEEKIVS SSWDGNLRLW QYRQAEYFQD DMPESDMNRV CSSGPTPVPC
     PSVAFSSPQ
//
ID   UBAP2_MOUSE             Reviewed;        1132 AA.
AC   Q91VX2; Q812D6; Q99K40;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-FEB-2011, entry version 54.
DE   RecName: Full=Ubiquitin-associated protein 2;
DE            Short=UBAP-2;
DE   AltName: Full=Protein lingerer homolog 1;
DE            Short=mLig-1;
GN   Name=Ubap2; Synonyms=Lig1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=22412137; PubMed=12524348;
RA   Kuniyoshi H., Baba K., Ueda R., Kondo S., Awano W., Juni N.,
RA   Yamamoto D.;
RT   "Lingerer, a Drosophila gene involved in initiation and termination of
RT   copulation, encodes a set of novel cytoplasmic proteins.";
RL   Genetics 162:1775-1789(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 UBA domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF276965; AAO23024.1; -; mRNA.
DR   EMBL; BC005482; AAH05482.1; -; mRNA.
DR   EMBL; BC007179; AAH07179.1; -; mRNA.
DR   IPI; IPI00457533; -.
DR   RefSeq; NP_081148.1; NM_026872.1.
DR   UniGene; Mm.41864; -.
DR   HSSP; Q80X50; 1WJ7.
DR   ProteinModelPortal; Q91VX2; -.
DR   SMR; Q91VX2; 28-113.
DR   PhosphoSite; Q91VX2; -.
DR   PRIDE; Q91VX2; -.
DR   Ensembl; ENSMUST00000030143; ENSMUSP00000030143; ENSMUSG00000028433.
DR   GeneID; 68926; -.
DR   KEGG; mmu:68926; -.
DR   UCSC; uc008sik.1; mouse.
DR   CTD; 68926; -.
DR   MGI; MGI:1916176; Ubap2.
DR   GeneTree; ENSGT00390000003453; -.
DR   HOGENOM; HBG714879; -.
DR   HOVERGEN; HBG058387; -.
DR   InParanoid; Q91VX2; -.
DR   OMA; QMRLAQV; -.
DR   PhylomeDB; Q91VX2; -.
DR   NextBio; 328205; -.
DR   ArrayExpress; Q91VX2; -.
DR   Bgee; Q91VX2; -.
DR   CleanEx; MM_LIG1; -.
DR   CleanEx; MM_UBAP2; -.
DR   Genevestigator; Q91VX2; -.
DR   InterPro; IPR022166; DUF3697_Uba2.
DR   InterPro; IPR009060; UBA-like.
DR   InterPro; IPR000449; UBA/transl_elong_EF1B_N.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   Pfam; PF12478; DUF3697; 1.
DR   Pfam; PF00627; UBA; 1.
DR   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF46934; UBA_like; 1.
DR   PROSITE; PS50030; UBA; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Phosphoprotein.
FT   CHAIN         1   1132       Ubiquitin-associated protein 2.
FT                                /FTId=PRO_0000270982.
FT   DOMAIN       48     92       UBA.
FT   COMPBIAS    543    795       Ser-rich.
FT   MOD_RES     433    433       Phosphoserine (By similarity).
FT   MOD_RES     440    440       Phosphoserine (By similarity).
FT   MOD_RES     634    634       Phosphoserine (By similarity).
FT   MOD_RES     853    853       Phosphotyrosine (By similarity).
FT   MOD_RES     854    854       Phosphotyrosine (By similarity).
FT   MOD_RES     876    876       Phosphotyrosine (By similarity).
FT   CONFLICT    698    698       T -> A (in Ref. 1; AAO23024).
SQ   SEQUENCE   1132 AA;  117966 MW;  ECF8E72C9134BB38 CRC64;
     MMTSVSNDRC RGAREKPQMP TAHAAQSQKQ VVQATAEQMR LAQVIFDKND SDFEAKVKQL
     MEVTGKNQDE CIVALHDCNG DVNKAINILL EGNSDTTSWE TVGGKKKNFG RESSENKENR
     EKRTEREASR GRGTNNRKGR GGNRVREFKG EENGIDCSQG DKPAERGKRA RGRGFGRGRG
     RGTGRFSAQS MGTFNPADYS ESMSTDGCGT KLAVWEAAQN GTDEGPEGLA KSHSMSQEPP
     SKSSYGLKGA WKNSVEEWTT EDWTEDLSET KVFTASSAPA ENHVTPGHSI DLVALLHKPA
     PPTQATEVNS FETSQQQGFG QALVFTNSQH NNQMAPGTAN STSASSYSPQ SLSSVLGSGF
     GELPQSNMVN ISNSQILDKL KPPGLSPFPA ASSAQQNDTA SPPATTAAWD LKPSAPQPSV
     LSRLDFKSQP EPSPVLSQLS QRQQHQTQAV SVPPPGLESF SSLAKPREST AGDGPSTVSR
     LLQLPNMTVE NIVSAHQPQP KHIKLPKRRV PPASKVPVSA VEMPGSSDVT GLNVQFGALE
     FGSEPSLSEF GSAASASENS NQIPISLYPK SLSEPLNASF PMTSAVQSST YTTSVVTSST
     LTSSALSSTS PVTTSSSYDQ SSVHTRIAYQ SSASPPDSAP GSVANGHGGG RSQHTVDTTS
     SVPAPKKTDP SALPSVSTLP GPASCTALLP SSAQHTATLP SLTPAAAELS SSPLSQLSSS
     LSGHQNSMTS AHATRSTSTP HTHASVESTA SSAAFSAAAT SAPSAPSSGV VLPGSMSTVS
     SLCLGGTTVS VPSSSTRATA LVTSGKAPPN LPQGVPPLLH NQYLVGPGGL LPAYPIYGYD
     ELQMLQSRLP MDYYGIPFAA PTALASRDGN LANNPYSGDV TKFGRGDSAS PAPPTTPAQA
     QQSQSQTHHT AQQPFLNPGL PPGYSYTGLP YYTGVPSAFQ YGPTMFVPPT SAKQHGVALS
     TPPTPFQQAS GYGQHAYSTG YDDLTQGTAA GDYTKGGYGG SSQAPNKSTG SGPGKGVSVS
     SGTGLPDMTG SVYNKTQTFD KQGFHAGTPP PFSLPSALGS TGPLAPAAAP GYAPAPFLHI
     MPAHQQPHSQ LLHHHLQQDA PSGSGQRSQP SSLQPKSQAS KPTYGSAPYW TN
//
ID   NCOA5_MOUSE             Reviewed;         579 AA.
AC   Q91W39; A2A5L2;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Nuclear receptor coactivator 5;
DE            Short=NCoA-5;
DE   AltName: Full=Coactivator independent of AF-2;
DE            Short=CIA;
GN   Name=Ncoa5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   DEVELOPMENTAL STAGE.
RX   MEDLINE=20565767; PubMed=11113208; DOI=10.1128/MCB.21.1.343-353.2001;
RA   Sauve F., McBroom L.D.B., Gallant J., Moraitis A.N., Labrie F.,
RA   Giguere V.;
RT   "CIA, a novel estrogen receptor coactivator with a bifunctional
RT   nuclear receptor interacting determinant.";
RL   Mol. Cell. Biol. 21:343-353(2001).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377 AND SER-381, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-34, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Nuclear receptor coregulator that can have both
CC       coactivator and corepressor functions. Interacts with nuclear
CC       receptors for steroids (ESR1 and ESR2) independently of the
CC       steroid binding domain (AF-2) of the ESR receptors, and with the
CC       orphan nuclear receptor NR1D2. Involved in the coactivation of
CC       nuclear steroid receptors (ER) as well as the corepression of MYC
CC       in response to 17-beta-estradiol (E2) (By similarity).
CC   -!- SUBUNIT: Binds HTATIP2/TIP30. Interacts with YLPM1. Forms a
CC       complex with ILF2, ILF3, YLPM1, KHDRBS1, RBMX and PPP1CA (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- DEVELOPMENTAL STAGE: Expressed in many fetal tissues. High
CC       expression in fetal heart and kidney. Weak expression in fetal
CC       liver.
CC   -!- DOMAIN: Contains one Leu-Xaa-Xaa-Leu-Leu (LxxLL) motif that is
CC       essential for the association with nuclear receptors (By
CC       similarity).
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL591495; CAM26468.1; -; Genomic_DNA.
DR   EMBL; BC017152; AAH17152.1; -; mRNA.
DR   IPI; IPI00313525; -.
DR   RefSeq; NP_659141.1; NM_144892.1.
DR   UniGene; Mm.233080; -.
DR   ProteinModelPortal; Q91W39; -.
DR   SMR; Q91W39; 197-314.
DR   STRING; Q91W39; -.
DR   PhosphoSite; Q91W39; -.
DR   PRIDE; Q91W39; -.
DR   Ensembl; ENSMUST00000040381; ENSMUSP00000046388; ENSMUSG00000039804.
DR   GeneID; 228869; -.
DR   KEGG; mmu:228869; -.
DR   NMPDR; fig|10090.3.peg.7426; -.
DR   UCSC; uc008nwv.1; mouse.
DR   CTD; 228869; -.
DR   MGI; MGI:2385165; Ncoa5.
DR   GeneTree; ENSGT00530000064134; -.
DR   HOGENOM; HBG713301; -.
DR   HOVERGEN; HBG052585; -.
DR   InParanoid; Q91W39; -.
DR   OMA; LMRSSTD; -.
DR   OrthoDB; EOG42BX8N; -.
DR   PhylomeDB; Q91W39; -.
DR   NextBio; 379224; -.
DR   ArrayExpress; Q91W39; -.
DR   Bgee; Q91W39; -.
DR   CleanEx; MM_NCOA5; -.
DR   Genevestigator; Q91W39; -.
DR   GermOnline; ENSMUSG00000039804; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR004154; Anticodon-bd.
DR   Gene3D; G3DSA:3.40.50.800; Anticodon_bd; 1.
DR   SUPFAM; SSF52954; Anticodon_bd; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Nucleus; Phosphoprotein; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    579       Nuclear receptor coactivator 5.
FT                                /FTId=PRO_0000094412.
FT   REGION        1    158       Transcription repression.
FT   REGION      458    579       Transcription activation.
FT   MOTIF       345    349       LXXLL motif.
FT   COMPBIAS      7    196       Arg/Asp-rich (mixed charge).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES       3      3       Phosphothreonine (By similarity).
FT   MOD_RES       9      9       Phosphoserine (By similarity).
FT   MOD_RES      29     29       Phosphoserine.
FT   MOD_RES      34     34       Phosphoserine.
FT   MOD_RES     127    127       Phosphotyrosine (By similarity).
FT   MOD_RES     151    151       Phosphoserine (By similarity).
FT   MOD_RES     377    377       Phosphoserine.
FT   MOD_RES     378    378       Phosphoserine (By similarity).
FT   MOD_RES     381    381       Phosphoserine.
FT   MOD_RES     387    387       Phosphoserine (By similarity).
FT   MOD_RES     404    404       Phosphoserine (By similarity).
FT   MOD_RES     420    420       Phosphothreonine (By similarity).
SQ   SEQUENCE   579 AA;  65319 MW;  145A34199FB02D33 CRC64;
     MNTAPSRPSP TRRDPYSFGD SRDTRRDRSP IRGSPRREPR DGRNGRDARD SRDIRDPRDL
     RDRRDSRDIR DHRDSRSVRE ARDLRDFRDF RDLRDSRDFR DHRDPVYDRY RDIRDSRDPL
     YRREGSYDRY LRVDDYCRRK DDSYFDRYRD SFDGRGPPGP ESQSRAKERL KREERRREEL
     YRRYFEEIQR RFDAERPVDC SVIVVNKQTK DYAESVGRKV RDLGMVVDLI FLNTEVSLSQ
     ALEDVSRGGS PFAIVITQQH QIHRSCTVNI MFGTPQEHRN MPQADAMVLV ARNYERYKND
     CREKEREEIA RQAAKMANDA ILQERDRGGP EEGGRGGHPP AIQSLINLLA DNRYLTAEET
     DKIINYLRER KERLLRSSAD SLPGPISRQP LGAASGSSLK SQPSSQPLQS GQVLPSATPT
     PAAPPTSQQE LQAKILSLFN SGAVAANSSS ASPSVATGSS QNQNFSTAAN SQPQQRPQAS
     GNQPPNIVGQ AGSARNMGPR PGAPSQGLFG QPSSRLAPAS TMASQRPVSS TGINFDNPSV
     QKALDTLIQS GPALSHLVSQ TAAQVGRPQA PMGSYQRHY
//
ID   CSDE1_MOUSE             Reviewed;         798 AA.
AC   Q91W50;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Cold shock domain-containing protein E1;
GN   Name=Csde1; Synonyms=D3Jfr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: RNA-binding protein. May be involved in translationally
CC       coupled mRNA turnover. Implicated with other RNA-binding proteins
CC       in the cytoplasmic deadenylation/translational and decay interplay
CC       of the FOS mRNA mediated by the major coding-region determinant of
CC       instability (mCRD) domain (By similarity).
CC   -!- SUBUNIT: Component of a multi subunit autoregulatory
CC       ribonucleoprotein complex (ARC), at least composed of IGF2BP1,
CC       PABPC1 and CSDE1. Interacts with STRAP. Part of a complex
CC       associated with the FOS mCRD domain and consisting of PABPC1,
CC       PAIP1, HNRPD and SYNCRIP. The interaction with PABPC1 is direct
CC       and RNA-independent (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Contains 9 CSD (cold-shock) domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC016898; AAH16898.1; -; mRNA.
DR   EMBL; BC062097; AAH62097.1; -; mRNA.
DR   IPI; IPI00274747; -.
DR   RefSeq; NP_659150.1; NM_144901.3.
DR   UniGene; Mm.277713; -.
DR   ProteinModelPortal; Q91W50; -.
DR   SMR; Q91W50; 16-90, 125-259, 345-424, 508-581, 673-744.
DR   STRING; Q91W50; -.
DR   PhosphoSite; Q91W50; -.
DR   PRIDE; Q91W50; -.
DR   Ensembl; ENSMUST00000029446; ENSMUSP00000029446; ENSMUSG00000068823.
DR   GeneID; 229663; -.
DR   KEGG; mmu:229663; -.
DR   UCSC; uc008qsg.1; mouse.
DR   CTD; 229663; -.
DR   MGI; MGI:92356; Csde1.
DR   GeneTree; ENSGT00390000016950; -.
DR   HOVERGEN; HBG013042; -.
DR   NextBio; 379579; -.
DR   ArrayExpress; Q91W50; -.
DR   Bgee; Q91W50; -.
DR   CleanEx; MM_CSDE1; -.
DR   Genevestigator; Q91W50; -.
DR   GermOnline; ENSMUSG00000068823; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR019844; Cold-shock_CS.
DR   InterPro; IPR011129; Cold_shock_prot.
DR   InterPro; IPR002059; CSP_DNA-bd.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR016027; NA-bd_OB-fold-like.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 5.
DR   Pfam; PF00313; CSD; 5.
DR   SMART; SM00357; CSP; 5.
DR   SUPFAM; SSF50249; Nucleic_acid_OB; 5.
DR   PROSITE; PS00352; COLD_SHOCK; 4.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Phosphoprotein; Repeat; RNA-binding.
FT   CHAIN         1    798       Cold shock domain-containing protein E1.
FT                                /FTId=PRO_0000100349.
FT   DOMAIN       26     87       CSD 1.
FT   DOMAIN      136    179       CSD 2; truncated.
FT   DOMAIN      186    245       CSD 3.
FT   DOMAIN      297    337       CSD 4; truncated.
FT   DOMAIN      349    410       CSD 5.
FT   DOMAIN      447    507       CSD 6.
FT   DOMAIN      519    579       CSD 7.
FT   DOMAIN      610    670       CSD 8.
FT   DOMAIN      674    735       CSD 9.
FT   MOD_RES      81     81       N6-acetyllysine (By similarity).
FT   MOD_RES     116    116       Phosphoserine (By similarity).
FT   MOD_RES     123    123       Phosphoserine (By similarity).
FT   MOD_RES     444    444       Phosphothreonine (By similarity).
FT   MOD_RES     445    445       Phosphoserine (By similarity).
FT   MOD_RES     481    481       Phosphothreonine (By similarity).
FT   MOD_RES     514    514       Phosphoserine (By similarity).
SQ   SEQUENCE   798 AA;  88791 MW;  731065F734C60009 CRC64;
     MSFDPNLLHN NGHNGYPNGT SAALRETGVI EKLLTSYGFI QCSERQARLF FHCSQYNGNL
     QDLKVGDDVE FEVSSDRRTG KPIAIKLVKI KPEIHPEERM NGQVVCAVPH NLESKSPAAP
     GQSPTGSVCY ERNGEVFYLT YTSEDVEGNV QLETGDKINF VIDNNKHTGA VSARNIMLLK
     KKQARCQGVV CAMKEAFGFI ERGDVVKEIF FHYSEFKGDL ETLQPGDDVE FTIKDRNGKE
     VATDVRLLPQ GTVIFEDISI EHFEGTVTKV IPKVPSKNQN DPLPGRIKVD FVIPKELPFG
     DKDTKSKVTL LEGDHVRFNI STDRRDKLER ATNIEVLSNT FQFTNEAREM GVIAAMRDGF
     GFIKCVDRDA RMFFHFSEIL DGNQLHIADE VEFTVVPDML SAQRNHAIRI KKLPKGTVSF
     HSHSDHRFLG TVEKEATFSN PKTTSPNKGK DKEAEDGIIA YDDCGVKLTI AFQAKDVEGS
     TSPQIGDKVE FSISDKQRPG QQIATCVRLL GRNSNSKRLL GYVATLKDNF GFIETANHDK
     EIFFHYSEFS GDVDSLELGD MVEYSLSKGK GNKVSAEKVN KAHSVNGITE EANPTIYSGK
     VIRPLRGVDP TQIEYQGMIE IVEEGDMKGE VYPFGIVGMA NKGDCLQKGE SVKFQLCVLG
     QNAQTMAYNI TPLRRATVEC VKDQFGFINY EVGDSKKLFF HVKEVQDGVE LQAGDEVEFS
     VILNQRTGKC SACNVWRVCE GPKAVAAPRP DRLVNRLKNI TLDDASAPRL MVLRQPRGPD
     NSMGFGAERK IRQAGVID
//
ID   TMM19_MOUSE             Reviewed;         336 AA.
AC   Q91W52; Q3UU09; Q8BY23; Q8BZK7;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Transmembrane protein 19;
GN   Name=Tmem19;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Dendritic cell, Diencephalon, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q91W52-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q91W52-2; Sequence=VSP_024661;
CC   -!- SIMILARITY: Belongs to the TMEM19 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK034298; BAC28663.1; -; mRNA.
DR   EMBL; AK042426; BAC31256.1; -; mRNA.
DR   EMBL; AK138931; BAE23820.1; -; mRNA.
DR   EMBL; AK155275; BAE33158.1; -; mRNA.
DR   EMBL; AK170143; BAE41594.1; -; mRNA.
DR   EMBL; AK171087; BAE42240.1; -; mRNA.
DR   EMBL; BC016895; AAH16895.1; -; mRNA.
DR   IPI; IPI00226829; -.
DR   IPI; IPI00754022; -.
DR   RefSeq; NP_598444.1; NM_133683.3.
DR   UniGene; Mm.29647; -.
DR   ProteinModelPortal; Q91W52; -.
DR   PRIDE; Q91W52; -.
DR   Ensembl; ENSMUST00000092170; ENSMUSP00000089808; ENSMUSG00000069520.
DR   GeneID; 67226; -.
DR   KEGG; mmu:67226; -.
DR   UCSC; uc007hbb.1; mouse.
DR   CTD; 67226; -.
DR   MGI; MGI:1914476; Tmem19.
DR   eggNOG; roNOG12791; -.
DR   GeneTree; ENSGT00390000017998; -.
DR   HOGENOM; HBG736325; -.
DR   HOVERGEN; HBG057658; -.
DR   InParanoid; Q91W52; -.
DR   OMA; KVPVGTN; -.
DR   OrthoDB; EOG41RPVK; -.
DR   NextBio; 323942; -.
DR   ArrayExpress; Q91W52; -.
DR   Bgee; Q91W52; -.
DR   CleanEx; MM_TMEM19; -.
DR   Genevestigator; Q91W52; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR002794; DUF92_TMEM19.
DR   PANTHER; PTHR13353; DUF92_TM; 1.
DR   Pfam; PF01940; DUF92; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    336       Transmembrane protein 19.
FT                                /FTId=PRO_0000284795.
FT   TRANSMEM     15     35       Helical; (Potential).
FT   TRANSMEM     49     69       Helical; (Potential).
FT   TRANSMEM     78     98       Helical; (Potential).
FT   TRANSMEM    218    238       Helical; (Potential).
FT   TRANSMEM    257    277       Helical; (Potential).
FT   TRANSMEM    313    333       Helical; (Potential).
FT   VAR_SEQ       1      1       M -> MLSIPPPQVLVALFSM (in isoform 2).
FT                                /FTId=VSP_024661.
FT   CONFLICT    182    182       S -> G (in Ref. 1; BAE23820).
SQ   SEQUENCE   336 AA;  36296 MW;  51A809EBEDE978ED CRC64;
     MTDSDDTTCK RYIKMITNIV ILSLIICISL AFWIMSMTAS TYYGNFRPVS PWRWLFSVVV
     PVVIACNGFK KKSLDHSGAL GGLVVGFILT IANFSFFTSL MTFFLSSSKL TKWRGNIKKQ
     LDSEYKEGGQ RNWVQVFCNG AVPTELALLY MIENGPGEMP IDFSKQHTAS WMCLSLLAAL
     ASSAGDTWAS EVAPVLSKSS PRLITTWEKV PVGTNGGVTA VGLASSLLGG TFVGLAYFLT
     QLVFVNDLDI SAPQWPIIAF GGVAGLFGSL VDSFLGATMQ FSGLDERTGL VVSSPTQETK
     HIAGKPILDN NAVNLFSSVL VALLLPTAAS GFWPRE
//
ID   UBL7_MOUSE              Reviewed;         380 AA.
AC   Q91W67; Q9D7P5;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Ubiquitin-like protein 7;
GN   Name=Ubl7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   STRUCTURE BY NMR OF 1-94.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the N-terminal ubiquitin-like domain in mouse
RT   ubiquitin-like protein SB132.";
RL   Submitted (OCT-2005) to the PDB data bank.
CC   -!- SUBUNIT: Binds ubiquitin (By similarity).
CC   -!- SIMILARITY: Contains 1 UBA domain.
CC   -!- SIMILARITY: Contains 1 ubiquitin-like domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK009025; BAB26033.1; -; mRNA.
DR   EMBL; BC016456; AAH16456.1; -; mRNA.
DR   IPI; IPI00399869; -.
DR   RefSeq; NP_081362.2; NM_027086.3.
DR   UniGene; Mm.41735; -.
DR   PDB; 1X1M; NMR; -; A=1-94.
DR   PDBsum; 1X1M; -.
DR   ProteinModelPortal; Q91W67; -.
DR   SMR; Q91W67; 5-97, 336-380.
DR   PhosphoSite; Q91W67; -.
DR   PRIDE; Q91W67; -.
DR   Ensembl; ENSMUST00000069445; ENSMUSP00000070341; ENSMUSG00000055720.
DR   GeneID; 69459; -.
DR   KEGG; mmu:69459; -.
DR   CTD; 69459; -.
DR   MGI; MGI:1916709; Ubl7.
DR   GeneTree; ENSGT00390000015967; -.
DR   HOGENOM; HBG444820; -.
DR   HOVERGEN; HBG054051; -.
DR   InParanoid; Q91W67; -.
DR   OrthoDB; EOG4S7JQJ; -.
DR   NextBio; 329506; -.
DR   ArrayExpress; Q91W67; -.
DR   Bgee; Q91W67; -.
DR   Genevestigator; Q91W67; -.
DR   GermOnline; ENSMUSG00000055720; Mus musculus.
DR   InterPro; IPR009060; UBA-like.
DR   InterPro; IPR000449; UBA/transl_elong_EF1B_N.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   InterPro; IPR015496; Ubiquilin.
DR   InterPro; IPR000626; Ubiquitin.
DR   InterPro; IPR019955; Ubiquitin_supergroup.
DR   PANTHER; PTHR10677; Ubiquilin; 1.
DR   Pfam; PF00627; UBA; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SMART; SM00165; UBA; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF46934; UBA_like; 1.
DR   PROSITE; PS50030; UBA; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Phosphoprotein; Ubl conjugation pathway.
FT   CHAIN         1    380       Ubiquitin-like protein 7.
FT                                /FTId=PRO_0000211022.
FT   DOMAIN       18     98       Ubiquitin-like.
FT   DOMAIN      333    377       UBA.
FT   MOD_RES     230    230       Phosphoserine.
FT   CONFLICT     35     35       L -> P (in Ref. 1; BAB26033).
FT   CONFLICT    228    228       G -> A (in Ref. 1; BAB26033).
FT   CONFLICT    331    331       Q -> H (in Ref. 1; BAB26033).
FT   CONFLICT    336    336       S -> I (in Ref. 1; BAB26033).
FT   STRAND        8     12
FT   STRAND       21     23
FT   HELIX        40     50
FT   TURN         52     54
FT   STRAND       58     65
FT   HELIX        76     79
FT   STRAND       86     93
SQ   SEQUENCE   380 AA;  40407 MW;  6DE0834A7CCEABF2 CRC64;
     MSLSDWHLAV KLADQPLAPK SILQLPETEL GEYSLGGYSI SFLKQLIAGK LQESVPDPEL
     IDLIYCGRKL KDDQTLDFYG IQPGSTVHVL RKSWPEPDQK PEPVDKVAAL REFRVLHTAL
     HSSSSYREAV FKMLSNKESL DQIIVATPGL SSDPIALGVL QDKDLFSVFA DPNMLDTLVP
     AHPALVNAII LVLHSVAGST PMPGADSSSR SMPSSSYRDM PGGFLFDGLS DDEDDFHPST
     RSTPSSSTPS SRPASLGYSG AAGPRPITQS ELATALALAS TPESSSHTPT PGTQGHSSGT
     SPMSSGVQSG TPITNDLFSQ ALQHALQASG QPSLQSQWQP QLQQLRDMGI QDDELSLRAL
     QATGGDIQAA LELIFAGGAP
//
ID   EPN3_MOUSE              Reviewed;         636 AA.
AC   Q91W69; Q9CV55;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Epsin-3;
DE   AltName: Full=EPS-15-interacting protein 3;
GN   Name=Epn3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 68-636.
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex (By similarity).
CC       Cytoplasm, perinuclear region (By similarity). Cytoplasmic
CC       vesicle, clathrin-coated vesicle (By similarity).
CC       Note=Concentrated in the perinuclear region and associated with
CC       clathrin-coated vesicles close to the cell periphery. May shuttle
CC       to the nucleus (By similarity).
CC   -!- INDUCTION: In keratinocytes, by wounding or contact with collagen.
CC   -!- SIMILARITY: Belongs to the epsin family.
CC   -!- SIMILARITY: Contains 1 ENTH (epsin N-terminal homology) domain.
CC   -!- SIMILARITY: Contains 2 UIM (ubiquitin-interacting motif) repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC016454; AAH16454.1; -; mRNA.
DR   EMBL; AK009469; BAB26309.1; -; mRNA.
DR   IPI; IPI00127364; -.
DR   RefSeq; NP_082260.1; NM_027984.3.
DR   UniGene; Mm.248620; -.
DR   ProteinModelPortal; Q91W69; -.
DR   SMR; Q91W69; 12-155.
DR   STRING; Q91W69; -.
DR   PhosphoSite; Q91W69; -.
DR   PRIDE; Q91W69; -.
DR   Ensembl; ENSMUST00000127305; ENSMUSP00000121390; ENSMUSG00000010080.
DR   GeneID; 71889; -.
DR   KEGG; mmu:71889; -.
DR   UCSC; uc007kyu.1; mouse.
DR   CTD; 71889; -.
DR   MGI; MGI:1919139; Epn3.
DR   eggNOG; maNOG07069; -.
DR   GeneTree; ENSGT00550000074611; -.
DR   HOGENOM; HBG444840; -.
DR   HOVERGEN; HBG006690; -.
DR   InParanoid; Q91W69; -.
DR   OMA; WRGDDSP; -.
DR   OrthoDB; EOG4SF97B; -.
DR   PhylomeDB; Q91W69; -.
DR   NextBio; 334860; -.
DR   ArrayExpress; Q91W69; -.
DR   Bgee; Q91W69; -.
DR   CleanEx; MM_EPN3; -.
DR   Genevestigator; Q91W69; -.
DR   GermOnline; ENSMUSG00000010080; Mus musculus.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR013809; Epsin-like_N.
DR   InterPro; IPR001026; Epsin_dom_N.
DR   InterPro; IPR003903; Ubiquitin-int_motif.
DR   Gene3D; G3DSA:1.25.40.90; ENTH_VHS; 1.
DR   Pfam; PF01417; ENTH; 1.
DR   Pfam; PF02809; UIM; 2.
DR   SMART; SM00273; ENTH; 1.
DR   SMART; SM00726; UIM; 2.
DR   SUPFAM; SSF48464; ENTH_VHS; 1.
DR   PROSITE; PS50942; ENTH; 1.
DR   PROSITE; PS50330; UIM; 2.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoplasmic vesicle; Lipid-binding; Phosphoprotein; Repeat.
FT   CHAIN         1    636       Epsin-3.
FT                                /FTId=PRO_0000074520.
FT   DOMAIN       12    144       ENTH.
FT   REPEAT      202    221       UIM 1.
FT   REPEAT      229    248       UIM 2.
FT   REPEAT      315    317       1.
FT   REPEAT      338    340       2.
FT   REPEAT      365    367       3.
FT   REPEAT      381    383       4.
FT   REPEAT      398    400       5.
FT   REPEAT      523    525       1.
FT   REPEAT      536    538       2.
FT   REPEAT      633    635       3.
FT   REGION      315    400       5 X 3 AA repeats of [DE]-P-W.
FT   REGION      523    635       3 X 3 AA repeats of N-P-F.
FT   COMPBIAS    303    628       Pro-rich.
FT   BINDING       8      8       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   BINDING      11     11       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   BINDING      25     25       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   BINDING      30     30       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   BINDING      63     63       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   BINDING      73     73       Phosphatidylinositol lipid headgroup (By
FT                                similarity).
FT   MOD_RES      17     17       Phosphotyrosine (By similarity).
FT   MOD_RES     175    175       Phosphoserine (By similarity).
FT   MOD_RES     179    179       Phosphotyrosine (By similarity).
FT   MOD_RES     387    387       Phosphoserine (By similarity).
FT   MOD_RES     389    389       Phosphothreonine (By similarity).
FT   CONFLICT     82     82       D -> G (in Ref. 2; BAB26309).
FT   CONFLICT    608    608       P -> S (in Ref. 2; BAB26309).
SQ   SEQUENCE   636 AA;  68240 MW;  BD18518618FA7A72 CRC64;
     MTTSALRRQV KNIVHNYSEA EIKVREATSN DPWGPPSSLM SEIADLTFNT VAFAEVMGMV
     WRRLNDSGKN WRHVYKALTL LDYLLKTGSE RVAHQCRENL YTIQTLKDFQ YIDRDGKDQG
     VNVREKVKQV MALLKDEERL RQERTHALKT KERMALEGMG IGSGQLGYSR RSRGSPSSYT
     SASSSPRYAS DLEQARPQTS GEEELQLQLA LAMSREEAER PVPPASHRDE DLQLQLALSL
     SRQEHEKGVR SWKGDDSPVA NGAEPAGQRR QRDREPEREE RKEEEKLKTS QSSILDLADI
     FAPAPALPST HCSADPWDIP GLRPNTEPSG SSWGPSADPW SPVPSGNALS RSQPWDLLPT
     LSSSEPWGRT PVLPSGPPIA DPWAPSSPTR KLPSTGADPW GASMETSDTS ALGGASPFDP
     FAKPLESTEP KESRDSAQAL PTGKSPSTVE LDPFGDSSPS CKQNGMKEPE ALDLGVLGEA
     LPQQPGKEAR PCRTPESFLG PSASSLVNLD SLVKAPLAAR TRNPFLTGLG VPSPTNPFGA
     GDQGRPTLNQ MRTGSPALGL PPGGPVGAPV GSMTYSASLP LPLSSVPVGA TLPASVSVFP
     QAGAFAPPPA SLPQPLLPTS GPMGPLPPQA GTNPFL
//
ID   BORG5_MOUSE             Reviewed;         409 AA.
AC   Q91W92; Q9D8M1;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Cdc42 effector protein 1;
DE   AltName: Full=Binder of Rho GTPases 5;
GN   Name=Cdc42ep1; Synonyms=Borg5, Cep1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N, and FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-210, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-210, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Probably involved in the organization of the actin
CC       cytoskeleton. Induced membrane extensions in fibroblasts (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with RHOQ and CDC42, in a GTP-dependent manner
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane
CC       protein (By similarity). Cytoplasm, cytoskeleton (By similarity).
CC   -!- DOMAIN: The CRIB domain mediates interaction with CDC42 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the BORG/CEP family.
CC   -!- SIMILARITY: Contains 1 CRIB domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK007896; BAB25335.1; -; mRNA.
DR   EMBL; BC016250; AAH16250.1; -; mRNA.
DR   EMBL; BC083130; AAH83130.1; -; mRNA.
DR   IPI; IPI00471127; -.
DR   RefSeq; NP_081495.1; NM_027219.3.
DR   UniGene; Mm.307488; -.
DR   ProteinModelPortal; Q91W92; -.
DR   SMR; Q91W92; 30-56.
DR   STRING; Q91W92; -.
DR   PhosphoSite; Q91W92; -.
DR   PRIDE; Q91W92; -.
DR   Ensembl; ENSMUST00000059619; ENSMUSP00000060930; ENSMUSG00000049521.
DR   GeneID; 104445; -.
DR   KEGG; mmu:104445; -.
DR   UCSC; uc007wrl.1; mouse.
DR   CTD; 104445; -.
DR   MGI; MGI:1929763; Cdc42ep1.
DR   eggNOG; roNOG15911; -.
DR   GeneTree; ENSGT00530000063054; -.
DR   HOGENOM; HBG125438; -.
DR   HOVERGEN; HBG080906; -.
DR   InParanoid; Q91W92; -.
DR   OrthoDB; EOG4M65K3; -.
DR   ArrayExpress; Q91W92; -.
DR   Bgee; Q91W92; -.
DR   CleanEx; MM_CDC42EP1; -.
DR   Genevestigator; Q91W92; -.
DR   GermOnline; ENSMUSG00000049521; Mus musculus.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0007266; P:Rho protein signal transduction; IDA:MGI.
DR   InterPro; IPR000095; PAK_box_Rho-bd.
DR   Pfam; PF00786; PBD; 1.
DR   SMART; SM00285; PBD; 1.
DR   PROSITE; PS50108; CRIB; 1.
PE   1: Evidence at protein level;
KW   Cell shape; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein; Repeat.
FT   CHAIN         1    409       Cdc42 effector protein 1.
FT                                /FTId=PRO_0000212658.
FT   DOMAIN       38     52       CRIB.
FT   REPEAT      235    241       1.
FT   REPEAT      242    248       2.
FT   REPEAT      255    261       3.
FT   REGION      235    284       3 X 7 AA tandem repeats of [PT]-[AT]-A-
FT                                [ENT]-[PT]-[PTS]-[AG].
FT   MOD_RES      19     19       Phosphoserine (By similarity).
FT   MOD_RES      27     27       Phosphoserine (By similarity).
FT   MOD_RES     101    101       Phosphoserine (By similarity).
FT   MOD_RES     106    106       Phosphoserine (By similarity).
FT   MOD_RES     113    113       Phosphoserine (By similarity).
FT   MOD_RES     121    121       Phosphoserine.
FT   MOD_RES     205    205       Phosphoserine (By similarity).
FT   MOD_RES     207    207       Phosphoserine.
FT   MOD_RES     210    210       Phosphoserine.
FT   MOD_RES     368    368       Phosphoserine (By similarity).
FT   MOD_RES     371    371       Phosphoserine (By similarity).
FT   CONFLICT    286    286       A -> V (in Ref. 1; BAB25335).
FT   CONFLICT    325    325       T -> A (in Ref. 1; BAB25335).
FT   CONFLICT    378    378       T -> A (in Ref. 1; BAB25335).
SQ   SEQUENCE   409 AA;  43096 MW;  1794FD0850171F0E CRC64;
     MPGPQGGTGA PTMSLGKLSP VGWVSSSHGK RRLTADMISP PLGDFRHTMH VGRGGDVFGD
     TSFLSNHGGR SGNTHRSPRS FLARKLQQVR RVGVPPRRMA SPAAPSPAPP PISPIIKNAI
     SLPQLNQATY DSLVMGKLSF DSTPASSTDG HSGYGLESGF CTISRLPRVE KHSNRDRDRD
     PDHSQDREQS SFPSEPTPNP ELRRSDSLLS FRFDLDLGPS LLSELLGVMS LSEAPAAETP
     VPTANPPAPA ANPAPTAKPP AHAITTLDAV TSLPASAVTS LPAPAAASSP SRGHFPNGVT
     SVLGPAAEAK PSPVGEGPQV PSNMTFDRHG ASWGASRASW GASRASRHYT EMDARRELAG
     VLPQVHGSWE SLNEDWSTPP ASVRAPVPTS VQVNAFEFAD AEEDDEVKV
//
ID   APC4_MOUSE              Reviewed;         807 AA.
AC   Q91W96; Q99LR5; Q9CZZ0;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Anaphase-promoting complex subunit 4;
DE            Short=APC4;
DE   AltName: Full=Cyclosome subunit 4;
GN   Name=Anapc4; Synonyms=D5Ertd249e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 439-807.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC       (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls
CC       progression through mitosis and the G1 phase of the cell cycle.
CC       The APC/C complex acts by mediating ubiquitination and subsequent
CC       degradation of target proteins: it mainly mediates the formation
CC       of 'Lys-11'-linked polyubiquitin chains and, to a lower extent,
CC       the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin
CC       chains (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: The APC/C is composed of at least 12 subunits (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the APC4 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB27965.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC002259; AAH02259.1; -; mRNA.
DR   EMBL; BC016237; AAH16237.1; -; mRNA.
DR   EMBL; BC024870; AAH24870.1; -; mRNA.
DR   EMBL; AK011994; BAB27965.1; ALT_INIT; mRNA.
DR   IPI; IPI00127493; -.
DR   RefSeq; NP_077175.1; NM_024213.2.
DR   UniGene; Mm.272568; -.
DR   ProteinModelPortal; Q91W96; -.
DR   SMR; Q91W96; 20-118, 722-748.
DR   STRING; Q91W96; -.
DR   PhosphoSite; Q91W96; -.
DR   PRIDE; Q91W96; -.
DR   Ensembl; ENSMUST00000031072; ENSMUSP00000031072; ENSMUSG00000029176.
DR   GeneID; 52206; -.
DR   KEGG; mmu:52206; -.
DR   UCSC; uc008xkw.1; mouse.
DR   CTD; 52206; -.
DR   MGI; MGI:1098673; Anapc4.
DR   GeneTree; ENSGT00390000004612; -.
DR   HOGENOM; HBG714578; -.
DR   HOVERGEN; HBG044815; -.
DR   InParanoid; Q91W96; -.
DR   OMA; PPNENTG; -.
DR   OrthoDB; EOG4D52X4; -.
DR   PhylomeDB; Q91W96; -.
DR   NextBio; 308658; -.
DR   ArrayExpress; Q91W96; -.
DR   Bgee; Q91W96; -.
DR   CleanEx; MM_ANAPC4; -.
DR   Genevestigator; Q91W96; -.
DR   GermOnline; ENSMUSG00000029176; Mus musculus.
DR   GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR   InterPro; IPR017169; APC4.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   PIRSF; PIRSF037303; APC4; 1.
DR   SUPFAM; SSF50978; WD40_like; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Mitosis; Phosphoprotein;
KW   Ubl conjugation pathway.
FT   CHAIN         1    807       Anaphase-promoting complex subunit 4.
FT                                /FTId=PRO_0000064596.
FT   MOD_RES     469    469       Phosphotyrosine (By similarity).
FT   MOD_RES     757    757       Phosphoserine (By similarity).
FT   MOD_RES     758    758       Phosphoserine (By similarity).
FT   MOD_RES     777    777       Phosphoserine (By similarity).
FT   MOD_RES     779    779       Phosphoserine (By similarity).
SQ   SEQUENCE   807 AA;  91708 MW;  1F99C8824BCCC7FC CRC64;
     MLRFPTCFPS FRVVGEKQLP QEIIFLAWSP KRDLIALANT TGEVLLHRLA SFHRVWSFPP
     NESTGKEVTC LAWRPDGKLL AFALADTKKI ILCDVEKPES LHSFSVEAPV SCMHWTEVTV
     ESSVLTSFYN AEDESNLLLP KLPTLPKNYN STSKIFSEEN SDEIIKLLGD VRLNILVLGG
     SSGFIELYAY GMFKIARVTG IAGTCIALCL SSDLKSLSVV TEVSSGGESE VSYFQLETNL
     LYSFLPEVTR MARKFTHISA LLQYINLSLT CMCEAWEEIL MQMDSRLTKF VQEKPTTTSV
     QDEFMHLLLW GKASAELQTL LMNQLTVKGL KKLGQSIESS YSSIQKLVIS HLQSGSESLL
     YHLSELKGMA SWKQKYEPLG LDAAGIEDAI TAVGSFILKA NELLQVIDSS MKNFKAFFRW
     LYVAMLRMTE DHVLPELNKM TQKDITFVAE FLTEHFNEAP DLYNRKGKYF NVERVGQYLK
     DEDDDLVSPP NTEGNQWYDF LQNSTHLKES PLLFPYYPRK SLHFVKRRME NVIDQCLQKP
     ADVIGRSMNQ AICIPLYKDA RSMDCARRLL KFPFLWNNKT SNLHYLLFTI LEDSVYKMCI
     LRRHTDISQS VSNGLIGIKF GSFTSASADK VRRSSYSCLD AQFYDDETVT VILKDSMGRE
     GRDRILVQLS LSLVYNSEDS DEYEFTGSYS TRLDEQGSII PTRTMHFEKH WRLLESMRAQ
     YVAGNGLRKV SCVLSSNLRH VRVFEMDIDD EWEIDESSDD EEEAGGKPVK IKEEVLSESE
     TEAHQDAAAL DPDVVIKVEK LDPELDS
//
ID   HKDC1_MOUSE             Reviewed;         915 AA.
AC   Q91W97; Q3UKJ9;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Putative hexokinase HKDC1;
DE            EC=2.7.1.1;
DE   AltName: Full=Hexokinase domain-containing protein 1;
GN   Name=Hkdc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + D-hexose = ADP + D-hexose 6-phosphate.
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC   -!- SIMILARITY: Belongs to the hexokinase family.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK145980; BAE26802.1; -; mRNA.
DR   EMBL; BC016235; AAH16235.1; -; mRNA.
DR   IPI; IPI00127495; -.
DR   RefSeq; NP_663394.1; NM_145419.1.
DR   UniGene; Mm.213213; -.
DR   HSSP; P05708; 1BG3.
DR   ProteinModelPortal; Q91W97; -.
DR   SMR; Q91W97; 12-909.
DR   PRIDE; Q91W97; -.
DR   Ensembl; ENSMUST00000020277; ENSMUSP00000020277; ENSMUSG00000020080.
DR   GeneID; 216019; -.
DR   KEGG; mmu:216019; -.
DR   UCSC; uc007fhc.1; mouse.
DR   CTD; 216019; -.
DR   MGI; MGI:2384910; Hkdc1.
DR   eggNOG; roNOG09167; -.
DR   GeneTree; ENSGT00390000017159; -.
DR   HOGENOM; HBG446386; -.
DR   HOVERGEN; HBG005020; -.
DR   InParanoid; Q91W97; -.
DR   OMA; CYMEDMS; -.
DR   OrthoDB; EOG47WNMX; -.
DR   PhylomeDB; Q91W97; -.
DR   BRENDA; 2.7.1.1; 244.
DR   NextBio; 374947; -.
DR   ArrayExpress; Q91W97; -.
DR   Bgee; Q91W97; -.
DR   CleanEx; MM_HKDC1; -.
DR   Genevestigator; Q91W97; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004396; F:hexokinase activity; IEA:EC.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR001312; Hexokinase.
DR   InterPro; IPR022673; Hexokinase_C.
DR   InterPro; IPR019807; Hexokinase_CS.
DR   InterPro; IPR022672; Hexokinase_N.
DR   PANTHER; PTHR19443; Hexokinase; 1.
DR   Pfam; PF00349; Hexokinase_1; 2.
DR   Pfam; PF03727; Hexokinase_2; 2.
DR   PRINTS; PR00475; HEXOKINASE.
DR   PROSITE; PS00378; HEXOKINASES; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Glycolysis; Kinase; Nucleotide-binding; Repeat;
KW   Transferase.
FT   CHAIN         1    915       Putative hexokinase HKDC1.
FT                                /FTId=PRO_0000299036.
FT   NP_BIND      84     89       ATP (Potential).
FT   NP_BIND     532    537       ATP (Potential).
FT   REGION      149    175       Glucose-binding (Potential).
FT   REGION      594    620       Glucose-binding (Potential).
FT   BINDING     555    555       ATP (Potential).
FT   CONFLICT    208    208       N -> D (in Ref. 1; BAE26802).
FT   CONFLICT    745    745       M -> T (in Ref. 1; BAE26802).
SQ   SEQUENCE   915 AA;  102259 MW;  1AE1506A9AC0228A CRC64;
     MFAVHLVAFY FTKLKEDQIK KVDRFLYHMR LSDETLVDIM ARFQAEMEKG LGKDTNPTAS
     VKMLPTFVRA IPDGSENGEF LSLDLGGSKF RVLKVQVSQE GQQNVQMESQ FYPMPNEITR
     GNGTELFDYV ADCLADFMKT KNLTHKKLPL GFTFSFPCRQ NKLEEGVLLS WTKKFKARGV
     QDTDVVNRLA TAMKKHKDLD VDILALVNDT VGTMMTCAYD DPNCEVGVII GTGTNACYME
     DMSNIDLVEG DEGRMCINTE WGAFGDDGAL EDIRTEFDRE LDLGSLNPGK QLFEKMISGL
     YMGELVRLIL LKMAKVGLLF GGAKSSALHT KGKIETQHVA AMEMSKEGLA NTREILVDLG
     LEPSESDCIA VQHVCTIVSF RSANLCAAAL ATILTRLREN KKLARLRTTV GMDGTLYKTH
     PQYPKRLHKV VRRLVPNCDV RFLLSESGST KGAAMVTAVA SRVQAQRKQI DKVLALFQLT
     REQLLGVRDK MRAELEYGLK KKTHSLATVK MLPTYVYGMP DGTEKGKFLA LDLGGTNFRV
     LLVKIRRRSV RMYNKIFAIP LEIMQGTGEE LFDHIVQCIA DFLDYMGLKG AQLPLGFTFS
     FPCRQTCIDK GTLVGWTKGF KATDCEGEDV VDMLREAIKR RNEFDLDIVA IVNDTVGTMM
     TCGYEDPRCE IGLIAGTGSN VCYMEEMRNI ELVDGDEGRM CVNTEWGGFG DNGCIDDIRT
     QYDKEVDEGS LNAGKQRYEK MTSGMYLGEI VRRILIDLTR QGLLFRGQIS ERLRTRGIFE
     TKFLSQIESD RLALLQVRRI LQQLGLDSTC EDSIVVKEVC GAVSRRAAQM CGAGMAAIVE
     KRREDQGLQH FKVTVGVDGT LYKLHPHFSR ILQETVKELA PQCDVTFMLS EDGSGKGAAL
     ITAVAKRLQQ PRKDI
//
ID   CXXC5_MOUSE             Reviewed;         317 AA.
AC   Q91WA4; Q3V0R4; Q8CES6; Q8CF49;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=CXXC-type zinc finger protein 5;
GN   Name=Cxxc5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Eye, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=19001364; DOI=10.1074/jbc.M808119200;
RA   Andersson T., Soedersten E., Duckworth J.K., Cascante A., Fritz N.,
RA   Sacchetti P., Cervenka I., Bryja V., Hermanson O.;
RT   "CXXC5 is a novel BMP4-regulated modulator of Wnt signaling in neural
RT   stem cells.";
RL   J. Biol. Chem. 284:3672-3681(2009).
CC   -!- FUNCTION: May indirectly participate in activation of the NF-
CC       kappa-B and MAPK pathways. Acts as a mediator of BMP4-mediated
CC       modulation of canonical Wnt signaling activity in neural stem
CC       cells (By similarity).
CC   -!- SUBUNIT: Interacts with DVL1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity). Note=Colocalizes with DVL1 in large bodies localized
CC       just outside the nuclear membrane (By similarity).
CC   -!- DEVELOPMENTAL STAGE: Expressed in dorsal pallium and in and around
CC       the developing choroid plexus at 10.5 and 12.5 dpc.
CC   -!- SIMILARITY: Contains 1 CXXC-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC25113.1; Type=Frameshift; Positions=245;
CC       Sequence=BAC25458.1; Type=Frameshift; Positions=245;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK005364; BAC25113.1; ALT_FRAME; mRNA.
DR   EMBL; AK015150; BAC25458.1; ALT_FRAME; mRNA.
DR   EMBL; AK132950; BAE21439.1; -; mRNA.
DR   EMBL; BC016207; AAH16207.1; -; mRNA.
DR   EMBL; BC089314; AAH89314.1; -; mRNA.
DR   IPI; IPI00127901; -.
DR   RefSeq; NP_598448.1; NM_133687.2.
DR   UniGene; Mm.94560; -.
DR   ProteinModelPortal; Q91WA4; -.
DR   SMR; Q91WA4; 250-303.
DR   STRING; Q91WA4; -.
DR   PRIDE; Q91WA4; -.
DR   Ensembl; ENSMUST00000060722; ENSMUSP00000054307; ENSMUSG00000046668.
DR   GeneID; 67393; -.
DR   KEGG; mmu:67393; -.
DR   UCSC; uc008emx.1; mouse.
DR   CTD; 67393; -.
DR   MGI; MGI:1914643; Cxxc5.
DR   eggNOG; roNOG05206; -.
DR   GeneTree; ENSGT00510000046972; -.
DR   HOGENOM; HBG445020; -.
DR   HOVERGEN; HBG095668; -.
DR   InParanoid; Q91WA4; -.
DR   OMA; GPKAGVA; -.
DR   OrthoDB; EOG432104; -.
DR   PhylomeDB; Q91WA4; -.
DR   NextBio; 324444; -.
DR   ArrayExpress; Q91WA4; -.
DR   Bgee; Q91WA4; -.
DR   CleanEx; MM_CXXC5; -.
DR   Genevestigator; Q91WA4; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR002857; Znf_CXXC.
DR   Pfam; PF02008; zf-CXXC; 1.
DR   PROSITE; PS51058; ZF_CXXC; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Metal-binding; Nucleus; Zinc; Zinc-finger.
FT   CHAIN         1    317       CXXC-type zinc finger protein 5.
FT                                /FTId=PRO_0000317549.
FT   ZN_FING     251    292       CXXC-type.
FT   COMPBIAS     14     18       Poly-Ser.
FT   CONFLICT     10     10       D -> G (in Ref. 1; BAE21439).
FT   CONFLICT    105    105       A -> G (in Ref. 1; BAC25458).
SQ   SEQUENCE   317 AA;  32812 MW;  215B73C8BA2AE031 CRC64;
     MSSLGGGSQD AGGSSSSSNT NSSSGSGQKA GGTDKSTAVA ATTAPTSVAD DAPPPERRNK
     SGIISEPLNK SLRRSRPLSH YSSFGSSGGG GSMMGVESAD KAAAAAASLL ANGHDLAAAM
     AVDKSNPTSK HKSGAVASLL SKAERATELA AEGQLTLQQF AQSTEMLKRV VQEHLPLMSE
     AGAGLPDMEA VAGAEALNGQ SDFPYLGAFP INPGLFIMTP AGVFLAESAL HMAGLAEYPM
     QGELASAISS GKKKRKRCGM CAPCRRRINC EQCSSCRNRK TGHQICKFRK CEELKKKPSA
     ALEKVMLPSG AAFRWFQ
//
ID   PPAC3_MOUSE             Reviewed;         271 AA.
AC   Q91WB2;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Probable lipid phosphate phosphatase PPAPDC3;
DE            EC=3.1.3.-;
DE   AltName: Full=Nuclear envelope transmembrane protein 39;
DE   AltName: Full=Phosphatidic acid phosphatase type 2 domain-containing protein 3;
GN   Name=Ppapdc3; Synonyms=Net39;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=17062158; DOI=10.1186/1471-2121-7-38;
RA   Chen I.-H., Huber M., Guan T., Bubeck A., Gerace L.;
RT   "Nuclear envelope transmembrane proteins (NETs) that are up-regulated
RT   during myogenesis.";
RL   BMC Cell Biol. 7:38-38(2006).
RN   [4]
RP   FUNCTION, LACK OF ENZYMATIC ACTIVITY, SUBUNIT, INTERACTION WITH MTOR,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, TOPOLOGY, AND INDUCTION.
RX   PubMed=19704009; DOI=10.1128/MCB.00684-09;
RA   Liu G.H., Guan T., Datta K., Coppinger J., Yates J. III, Gerace L.;
RT   "Regulation of myoblast differentiation by the nuclear envelope
RT   protein NET39.";
RL   Mol. Cell. Biol. 29:5800-5812(2009).
CC   -!- FUNCTION: Plays a role as negative regulator of myoblast
CC       differentiation, in part through effects on MTOR signaling. Has no
CC       detectable enzymatic activity. Knockdown in myoblasts strongly
CC       promotes differentiation, whereas overexpression represses
CC       myogenesis.
CC   -!- SUBUNIT: Homo- and heterooligomer. Interacts with MTOR; controls
CC       MTOR-dependent IGF2 expression during myoblast differentiation.
CC   -!- SUBCELLULAR LOCATION: Nucleus envelope. Endoplasmic reticulum
CC       membrane. Membrane; Multi-pass membrane protein. Note=Both the N-
CC       and C-terminal are exposed to the cytoplasm/nucleoplasm.
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart and muscle.
CC   -!- INDUCTION: Up-regulated during myoblast differentiation.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK052883; BAC35188.1; -; mRNA.
DR   EMBL; AK134638; BAE22220.1; -; mRNA.
DR   EMBL; BC016136; AAH16136.1; -; mRNA.
DR   IPI; IPI00127929; -.
DR   RefSeq; NP_663496.1; NM_145521.3.
DR   UniGene; Mm.257236; -.
DR   ProteinModelPortal; Q91WB2; -.
DR   STRING; Q91WB2; -.
DR   PRIDE; Q91WB2; -.
DR   Ensembl; ENSMUST00000057423; ENSMUSP00000054337; ENSMUSG00000051373.
DR   GeneID; 227721; -.
DR   KEGG; mmu:227721; -.
DR   UCSC; uc008jel.1; mouse.
DR   CTD; 227721; -.
DR   MGI; MGI:2445183; Ppapdc3.
DR   GeneTree; ENSGT00390000012789; -.
DR   HOGENOM; HBG713923; -.
DR   HOVERGEN; HBG054746; -.
DR   InParanoid; Q91WB2; -.
DR   OMA; MSSNTCQ; -.
DR   OrthoDB; EOG4FR0SG; -.
DR   PhylomeDB; Q91WB2; -.
DR   NextBio; 378788; -.
DR   ArrayExpress; Q91WB2; -.
DR   Bgee; Q91WB2; -.
DR   Genevestigator; Q91WB2; -.
DR   GermOnline; ENSMUSG00000051373; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR016118; P_Acid_Pase/Cl_peroxidase_N.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   Gene3D; G3DSA:1.20.144.10; P_Acid_Pase/Cl_peroxidase_N; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; AcPase_VanPerase; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Hydrolase; Membrane; Nucleus; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    271       Probable lipid phosphate phosphatase
FT                                PPAPDC3.
FT                                /FTId=PRO_0000239402.
FT   TOPO_DOM      1    112       Cytoplasmic (Potential).
FT   TRANSMEM    113    133       Helical; (Potential).
FT   TOPO_DOM    134    141       Extracellular (Potential).
FT   TRANSMEM    142    162       Helical; (Potential).
FT   TOPO_DOM    163    202       Cytoplasmic (Potential).
FT   TRANSMEM    203    223       Helical; (Potential).
FT   TOPO_DOM    224    239       Extracellular (Potential).
FT   TRANSMEM    240    260       Helical; (Potential).
FT   TOPO_DOM    261    271       Cytoplasmic (Potential).
FT   REGION       70     91       interaction with MTOR.
SQ   SEQUENCE   271 AA;  29710 MW;  91595666F0BF0508 CRC64;
     MPASQSRARA RDRNNVLNRA EFLSLNQPPK GTQEPRSSGR KASGPSTQPP PSSDGARERR
     QSQQLPEEDC MQLNPSFKGI AFNSLLAIDI CMSKRLGVCA GRAASWASAR SMVKLIGITG
     HGIPWIGGTI LCLVRSSTLA GQEVLMNLLL ALLLDIMTVA GVQKLIKRRG PYETSPGLLD
     YLTMDIYAFP AGHASRAAMV SKFFLSHLVL AVPLRVLLVL WAFCVGLSRV MIGRHHITDV
     ISGFIIGYFQ FRLVELVWMS SNTCQMLISA W
//
ID   SETD3_MOUSE             Reviewed;         594 AA.
AC   Q91WC0; Q6PEN3; Q8CD86; Q8CDX8; Q9CZZ1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=SET domain-containing protein 3;
DE   AltName: Full=Endothelial differentiation inhibitory protein D10;
GN   Name=Setd3; Synonyms=D12Ertd771e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Embryonic stem cell;
RX   PubMed=16008511; DOI=10.1089/dna.2005.24.432;
RA   Ishii H., Mimori K., Mori M., Vecchione A.;
RT   "Differentially expressed genes in endothelial differentiation.";
RL   DNA Cell Biol. 24:432-437(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Head, Stomach, Testis, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=FVB/N, and NMRI; TISSUE=Eye, Liver, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q91WC0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q91WC0-2; Sequence=VSP_021195, VSP_021196;
CC       Name=3;
CC         IsoId=Q91WC0-3; Sequence=VSP_021194;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q91WC0-4; Sequence=VSP_021195, VSP_021197, VSP_021198;
CC   -!- SIMILARITY: Contains 1 SET domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY513271; AAS82953.1; -; mRNA.
DR   EMBL; AK011993; BAB27964.1; -; mRNA.
DR   EMBL; AK029403; BAC26435.1; -; mRNA.
DR   EMBL; AK031017; BAC27215.1; -; mRNA.
DR   EMBL; AK031371; BAC27371.1; -; mRNA.
DR   EMBL; AK146777; BAE27425.1; -; mRNA.
DR   EMBL; AK166570; BAE38861.1; -; mRNA.
DR   EMBL; BC016123; AAH16123.1; -; mRNA.
DR   EMBL; BC019973; AAH19973.1; -; mRNA.
DR   EMBL; BC057968; AAH57968.1; -; mRNA.
DR   IPI; IPI00313968; -.
DR   IPI; IPI00622916; -.
DR   IPI; IPI00798528; -.
DR   IPI; IPI00798593; -.
DR   RefSeq; NP_082538.2; NM_028262.3.
DR   UniGene; Mm.159185; -.
DR   HSSP; Q43088; 1OZV.
DR   ProteinModelPortal; Q91WC0; -.
DR   SMR; Q91WC0; 273-323.
DR   STRING; Q91WC0; -.
DR   PhosphoSite; Q91WC0; -.
DR   PRIDE; Q91WC0; -.
DR   Ensembl; ENSMUST00000071095; ENSMUSP00000066413; ENSMUSG00000056770.
DR   Ensembl; ENSMUST00000085012; ENSMUSP00000082085; ENSMUSG00000056770.
DR   GeneID; 52690; -.
DR   KEGG; mmu:52690; -.
DR   UCSC; uc007ozj.1; mouse.
DR   UCSC; uc007ozk.1; mouse.
DR   UCSC; uc007ozl.1; mouse.
DR   CTD; 52690; -.
DR   MGI; MGI:1289184; Setd3.
DR   eggNOG; roNOG05090; -.
DR   GeneTree; ENSGT00530000063630; -.
DR   HOGENOM; HBG268887; -.
DR   HOVERGEN; HBG062823; -.
DR   InParanoid; Q91WC0; -.
DR   OMA; DNAIDRI; -.
DR   OrthoDB; EOG4HX50N; -.
DR   PhylomeDB; Q91WC0; -.
DR   NextBio; 309349; -.
DR   ArrayExpress; Q91WC0; -.
DR   Bgee; Q91WC0; -.
DR   CleanEx; MM_SETD3; -.
DR   Genevestigator; Q91WC0; -.
DR   GermOnline; ENSMUSG00000056770; Mus musculus.
DR   InterPro; IPR015353; Rubisco_LSMT_subst-bd.
DR   InterPro; IPR001214; SET_dom.
DR   Gene3D; G3DSA:3.90.1420.10; Rubisco_LSMT_subst-bd; 1.
DR   Pfam; PF09273; Rubis-subs-bind; 1.
DR   Pfam; PF00856; SET; 1.
DR   SUPFAM; SSF81822; Rubisco_LSMT_subst-bd; 1.
DR   PROSITE; PS50280; SET; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    594       SET domain-containing protein 3.
FT                                /FTId=PRO_0000254176.
FT   DOMAIN       80    320       SET.
FT   MOD_RES      14     14       Phosphothreonine.
FT   MOD_RES      17     17       Phosphothreonine (By similarity).
FT   VAR_SEQ       1    351       Missing (in isoform 3).
FT                                /FTId=VSP_021194.
FT   VAR_SEQ       1    128       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_021195.
FT   VAR_SEQ     226    283       Missing (in isoform 2).
FT                                /FTId=VSP_021196.
FT   VAR_SEQ     284    290       ITTGYNL -> VKISSWG (in isoform 4).
FT                                /FTId=VSP_021197.
FT   VAR_SEQ     291    594       Missing (in isoform 4).
FT                                /FTId=VSP_021198.
FT   CONFLICT    321    321       F -> S (in Ref. 1; AAS82953 and 2;
FT                                BAB27964).
FT   CONFLICT    460    460       R -> Q (in Ref. 2; BAC27215).
SQ   SEQUENCE   594 AA;  67176 MW;  67DA47889A5C9F55 CRC64;
     MGKKSRVKTQ KSGTGATATV SPKEILNLTS ELLQKCSSPA PSPGKEWEEY TQIRALVEKI
     RKKQKGLSVT FDGKREDYFP DLMKWASENG ASVEGFEMVN FKEEGFGLRA TRDIKAEELF
     LWVPRKLLMT VESAKNSVLG PLYSQDRILQ AMGNIALAFH LLCERASPNS FWQPYIQTLP
     SEYDTPLYFE EEEVRCLQST QAIHDVFSQY KNTARQYAYF YKVIQTHPHA NKLPLKESFT
     YEDYRWAVSS VMTRQNQIPT EDGSRVTLAL IPLWDMCNHT NGLITTGYNL EDDRCECVAL
     QDFQAGDQIY IFYGTRSNAE FVIHSGFFFD NNSHDRVKIK LGVSKSDRLY AMKAEVLARA
     GIPTSSVFAL HSTEPPISAQ LLAFLRVFCM TEEELKEHLL GDSAIDRIFT LGNAEFPVSW
     DNEVKLWTFL EDRASLLLKT YKTTIEEDKI VLKNPDLSVR ATMAIKLRLG EKEILEKAVK
     SAAVNREYYR KHMEERAPLP RYEESDLGLL EGGVGDSRLP LVLRKLEEEA GVQESLSLTE
     TVSKVKAAEN GLVNGENLIP NGTRSENESL SPEESENVTG EESSGSMAKV KERL
//
ID   DGLB_MOUSE              Reviewed;         669 AA.
AC   Q91WC9; Q8BU39; Q8BU97; Q8BV05;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Sn1-specific diacylglycerol lipase beta;
DE            Short=DGL-beta;
DE            EC=3.1.1.-;
GN   Name=Daglb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, Lung, and Ovary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=14610053; DOI=10.1083/jcb.200305129;
RA   Bisogno T., Howell F., Williams G., Minassi A., Cascio M.G.,
RA   Ligresti A., Matias I., Schiano-Moriello A., Paul P., Williams E.-J.,
RA   Gangadharan U., Hobbs C., Di Marzo V., Doherty P.;
RT   "Cloning of the first sn1-DAG lipases points to the spatial and
RT   temporal regulation of endocannabinoid signaling in the brain.";
RL   J. Cell Biol. 163:463-468(2003).
CC   -!- FUNCTION: Catalyzes the hydrolysis of diacylglycerol (DAG) to 2-
CC       arachidonoyl-glycerol (2-AG), the most abundant endocannabinoid in
CC       tissues. Required for axonal growth during development and for
CC       retrograde synaptic signaling at mature synapses (By similarity).
CC   -!- COFACTOR: Calcium (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- TISSUE SPECIFICITY: In embryonic brains, it is present in axonal
CC       tracts, while in adults it localizes to dendritic fields,
CC       correlating with the developmental change in requirement for 2-AG
CC       synthesis from the pre- to the postsynaptic compartment (at
CC       protein level).
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase
CC       family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC39734.1; Type=Frameshift; Positions=102;
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DR   EMBL; AK081509; BAC38241.1; -; mRNA.
DR   EMBL; AK086747; BAC39734.1; ALT_FRAME; mRNA.
DR   EMBL; AK087884; BAC40033.1; -; mRNA.
DR   EMBL; AK136372; BAE22951.1; -; mRNA.
DR   EMBL; BC016105; AAH16105.2; -; mRNA.
DR   IPI; IPI00331614; -.
DR   RefSeq; NP_659164.2; NM_144915.3.
DR   UniGene; Mm.469963; -.
DR   ProteinModelPortal; Q91WC9; -.
DR   PhosphoSite; Q91WC9; -.
DR   PRIDE; Q91WC9; -.
DR   Ensembl; ENSMUST00000045593; ENSMUSP00000043088; ENSMUSG00000039206.
DR   GeneID; 231871; -.
DR   KEGG; mmu:231871; -.
DR   UCSC; uc009akj.1; mouse.
DR   CTD; 231871; -.
DR   MGI; MGI:2442032; Daglb.
DR   eggNOG; roNOG07706; -.
DR   GeneTree; ENSGT00530000063682; -.
DR   HOGENOM; HBG715179; -.
DR   HOVERGEN; HBG055573; -.
DR   InParanoid; Q91WC9; -.
DR   OMA; FLPEMVW; -.
DR   NextBio; 380830; -.
DR   ArrayExpress; Q91WC9; -.
DR   Bgee; Q91WC9; -.
DR   CleanEx; MM_DAGLB; -.
DR   Genevestigator; Q91WC9; -.
DR   GermOnline; ENSMUSG00000039206; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004806; F:triglyceride lipase activity; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002921; Lipase_3.
DR   Pfam; PF01764; Lipase_3; 1.
DR   PROSITE; PS00120; LIPASE_SER; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell membrane; Hydrolase; Lipid degradation; Membrane;
KW   Metal-binding; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    669       Sn1-specific diacylglycerol lipase beta.
FT                                /FTId=PRO_0000248351.
FT   TOPO_DOM      1     17       Cytoplasmic (Potential).
FT   TRANSMEM     18     38       Helical; (Potential).
FT   TOPO_DOM     39     58       Extracellular (Potential).
FT   TRANSMEM     59     79       Helical; (Potential).
FT   TOPO_DOM     80    102       Cytoplasmic (Potential).
FT   TRANSMEM    103    123       Helical; (Potential).
FT   TOPO_DOM    124    128       Extracellular (Potential).
FT   TRANSMEM    129    149       Helical; (Potential).
FT   TOPO_DOM    150    669       Cytoplasmic (Potential).
FT   ACT_SITE    443    443       Charge relay system (By similarity).
FT   ACT_SITE    495    495       Charge relay system (By similarity).
FT   MOD_RES     570    570       Phosphoserine (By similarity).
FT   MOD_RES     573    573       Phosphotyrosine (By similarity).
FT   MOD_RES     578    578       Phosphoserine (By similarity).
FT   CONFLICT    467    467       A -> T (in Ref. 1; BAC38241).
SQ   SEQUENCE   669 AA;  73905 MW;  22FBCE0DC7A78522 CRC64;
     MPGMVLFGRR WSLASDDLVF PGSFELFLRV LWWIVSLTLY LTHRRRLDCP GGVLLSTYLI
     VLLVLLAVII CTVLAIVCVS MRGTICNPGP RKSMSKLLYI RLALFLPEMV WASLGAAWVA
     KGIQCDRTVV IGIIATVIVS WIVIAATMVT IIFVFDPLGG KMAPYPPCIP EHLDSNSSNR
     LLTGLKTAAK SVWETRVQFC CCCVGQDDNT RVAFSSTADL FSTYFSDTDL VPSDIAAGFT
     LLHQQQDNIS HSREPPEVVT HTPGQPQETE LDAEVENCHH YMPFAAAAYG WPLYIYRNPF
     TGLCRIGGDC CRARDIEYDA VEGDQHNCHF ASILKTTGLQ YRDFIHISFH DKVYELPFIV
     VLDHRKESVV VAVRGTMSLQ DVLTDLSAES ETLELGIELQ DCVAHKGIAQ AARYIHRRLV
     NDGILSQAFS VAPEYQLVLV GHSLGAGAAA LLAIMLRGAY PQVRAYAFSP PRGLLSKSLY
     EYSKDFVVSL ILGMDVIPRL SVTNMEDLKR RILRVIANCN KPKYKILLHG CWYGLFGGSP
     DNFPTELDEG TQGALTQPLL GEQTLLTRYS PGYCSSDSPL DSPTKYPTLY PPGRIIHLEE
     EGGSGRFGCC SAAQYRARWA HEAEFSKILI GPKMLIDHMP DVMIRALDRV LADRTACVSC
     PGQGGSSVP
//
ID   AAKG2_MOUSE             Reviewed;         566 AA.
AC   Q91WG5; Q6V7V5;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=5'-AMP-activated protein kinase subunit gamma-2;
DE            Short=AMPK gamma2;
DE            Short=AMPK subunit gamma-2;
GN   Name=Prkag2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RC   STRAIN=C57BL/6J;
RA   Zhou G., Jiang D., Zhang Y.;
RT   "Cloning of mouse protein kinase, AMP-activated, gamma 2 non-catalytic
RT   subunit.";
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-71; SER-73;
RP   SER-90; SER-138; SER-158; SER-161 AND SER-162, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: AMPK is responsible for the regulation of fatty acid
CC       synthesis by phosphorylation of acetyl-CoA carboxylase. Also
CC       regulates cholesterol synthesis via phosphorylation and
CC       inactivation of hydroxymethylglutaryl-CoA reductase and hormone-
CC       sensitive lipase. This is a regulatory subunit (By similarity).
CC   -!- SUBUNIT: Heterotrimer of an alpha catalytic subunit, a beta and a
CC       gamma non-catalytic regulatory subunits (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=Q91WG5-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=Q91WG5-2; Sequence=VSP_015586;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase gamma
CC       subunit family.
CC   -!- SIMILARITY: Contains 4 CBS domains.
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DR   EMBL; AY348864; AAQ55224.1; -; mRNA.
DR   EMBL; BC015283; AAH15283.1; -; mRNA.
DR   IPI; IPI00128126; -.
DR   IPI; IPI00649331; -.
DR   RefSeq; NP_001164027.1; NM_001170556.1.
DR   UniGene; Mm.33649; -.
DR   ProteinModelPortal; Q91WG5; -.
DR   SMR; Q91WG5; 253-554.
DR   IntAct; Q91WG5; 1.
DR   STRING; Q91WG5; -.
DR   PhosphoSite; Q91WG5; -.
DR   PRIDE; Q91WG5; -.
DR   Ensembl; ENSMUST00000030784; ENSMUSP00000030784; ENSMUSG00000028944.
DR   GeneID; 108099; -.
DR   KEGG; mmu:108099; -.
DR   UCSC; uc008wsm.1; mouse.
DR   CTD; 108099; -.
DR   MGI; MGI:1336153; Prkag2.
DR   GeneTree; ENSGT00390000009849; -.
DR   HOGENOM; HBG446629; -.
DR   HOVERGEN; HBG050431; -.
DR   InParanoid; Q91WG5; -.
DR   OrthoDB; EOG45DWPQ; -.
DR   PhylomeDB; Q91WG5; -.
DR   NextBio; 360062; -.
DR   ArrayExpress; Q91WG5; -.
DR   Bgee; Q91WG5; -.
DR   Genevestigator; Q91WG5; -.
DR   GermOnline; ENSMUSG00000028944; Mus musculus.
DR   GO; GO:0004679; F:AMP-activated protein kinase activity; TAS:MGI.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006950; P:response to stress; TAS:MGI.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000644; Cysta_beta_synth_core.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 2.
DR   Pfam; PF00571; CBS; 3.
DR   SMART; SM00116; CBS; 4.
DR   PROSITE; PS51371; CBS; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; CBS domain; Fatty acid biosynthesis;
KW   Lipid synthesis; Phosphoprotein; Repeat.
FT   CHAIN         1    566       5'-AMP-activated protein kinase subunit
FT                                gamma-2.
FT                                /FTId=PRO_0000204382.
FT   DOMAIN      272    332       CBS 1.
FT   DOMAIN      354    412       CBS 2.
FT   DOMAIN      427    489       CBS 3.
FT   DOMAIN      501    559       CBS 4.
FT   MOD_RES      65     65       Phosphoserine.
FT   MOD_RES      71     71       Phosphoserine.
FT   MOD_RES      73     73       Phosphoserine.
FT   MOD_RES      86     86       Phosphoserine (By similarity).
FT   MOD_RES      90     90       Phosphoserine.
FT   MOD_RES     129    129       Phosphoserine (By similarity).
FT   MOD_RES     130    130       Phosphoserine (By similarity).
FT   MOD_RES     131    131       Phosphoserine (By similarity).
FT   MOD_RES     134    134       Phosphoserine (By similarity).
FT   MOD_RES     135    135       Phosphoserine (By similarity).
FT   MOD_RES     138    138       Phosphoserine.
FT   MOD_RES     142    142       Phosphothreonine (By similarity).
FT   MOD_RES     143    143       Phosphoserine (By similarity).
FT   MOD_RES     156    156       Phosphothreonine (By similarity).
FT   MOD_RES     157    157       Phosphoserine (By similarity).
FT   MOD_RES     158    158       Phosphoserine.
FT   MOD_RES     160    160       Phosphoserine (By similarity).
FT   MOD_RES     161    161       Phosphoserine.
FT   MOD_RES     162    162       Phosphoserine.
FT   MOD_RES     164    164       Phosphoserine (By similarity).
FT   MOD_RES     165    165       Phosphothreonine (By similarity).
FT   MOD_RES     167    167       Phosphothreonine (By similarity).
FT   MOD_RES     195    195       Phosphoserine (By similarity).
FT   MOD_RES     196    196       Phosphoserine.
FT   MOD_RES     218    218       Phosphoserine (By similarity).
FT   VAR_SEQ       1    240       Missing (in isoform B).
FT                                /FTId=VSP_015586.
FT   CONFLICT    257    257       F -> V (in Ref. 1; AAQ55224).
FT   CONFLICT    516    516       T -> N (in Ref. 1; AAQ55224).
SQ   SEQUENCE   566 AA;  62997 MW;  754DE4D696102C7D CRC64;
     MGSAAMDTKK KKEVSSPGGS SGKKNPSLKR RSLRVHIPDL SSFAMPLLDG DVENSEKHSS
     RKVDSPFSSG SPSRGLFSRG PQPRPSSPVS APVRPKTSPG SPKTVFPFSY QESPPRSPRR
     MSFSGIFRSS SKESSPNSNP STSPGGIRFF SRSRKTSSVS SSPSTPTQVT KQHPFPLESY
     KQEPERPESR IYASSSPPDT GQRFCLAFQS PARPPLASPT YHAPLRTAVL AAAPGPAEAG
     MLEKLEFQEE EDSESGFYMR FMRSHKCYDI VPTSSKLVVF DTTLQVKKAF FALVANGVRA
     APLWESKKQS FVGMLTITDF INILHRYYKS PMVQIYELEE HKIETWRELY LQETFKPLVN
     ISPDASLFDA VYSLIKNKIH RLPVIDPISG NALYILTHKR ILKFLQLFMS DMPKPAFMKQ
     NLDELGIGTY HNIAFIHPDT PIIKALNIFV ERRISALPVV DESGKVVDIY SKFDVINLAA
     EKTYNNLDIT VTQALQHRSQ YFEGVVKCSK LETLETIVDR IVRAEVHRLV VVNEADSIVG
     IISLSDILQA LILTPAGAKQ KETETE
//
ID   DGKG_MOUSE              Reviewed;         788 AA.
AC   Q91WG7;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Diacylglycerol kinase gamma;
DE            Short=DAG kinase gamma;
DE            EC=2.7.1.107;
DE   AltName: Full=88 kDa diacylglycerol kinase;
DE   AltName: Full=Diglyceride kinase gamma;
DE            Short=DGK-gamma;
GN   Name=Dgkg; Synonyms=Dagk3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-
CC       sn-glycerol 3-phosphate.
CC   -!- SIMILARITY: Belongs to the eukaryotic diacylglycerol kinase
CC       family.
CC   -!- SIMILARITY: Contains 1 DAGKc domain.
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
CC   -!- SIMILARITY: Contains 2 phorbol-ester/DAG-type zinc fingers.
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DR   EMBL; BC015278; AAH15278.1; -; mRNA.
DR   IPI; IPI00128127; -.
DR   RefSeq; NP_619591.1; NM_138650.2.
DR   UniGene; Mm.194986; -.
DR   UniGene; Mm.448158; -.
DR   ProteinModelPortal; Q91WG7; -.
DR   SMR; Q91WG7; 1-244, 263-319.
DR   STRING; Q91WG7; -.
DR   PhosphoSite; Q91WG7; -.
DR   PRIDE; Q91WG7; -.
DR   Ensembl; ENSMUST00000089925; ENSMUSP00000087371; ENSMUSG00000022861.
DR   GeneID; 110197; -.
DR   KEGG; mmu:110197; -.
DR   UCSC; uc007ysf.1; mouse.
DR   CTD; 110197; -.
DR   MGI; MGI:105060; Dgkg.
DR   GeneTree; ENSGT00600000084185; -.
DR   HOVERGEN; HBG051345; -.
DR   InParanoid; Q91WG7; -.
DR   OMA; EVMQHAW; -.
DR   OrthoDB; EOG4GHZNH; -.
DR   BRENDA; 2.7.1.107; 244.
DR   NextBio; 363515; -.
DR   ArrayExpress; Q91WG7; -.
DR   Bgee; Q91WG7; -.
DR   CleanEx; MM_DGKG; -.
DR   Genevestigator; Q91WG7; -.
DR   GermOnline; ENSMUSG00000022861; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004143; F:diacylglycerol kinase activity; IEA:EC.
DR   GO; GO:0007205; P:activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway; IEA:InterPro.
DR   InterPro; IPR000756; Diacylglycerol_kin_accessory.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00609; DAGK_acc; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   SMART; SM00109; C1; 2.
DR   SMART; SM00045; DAGKa; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   SMART; SM00054; EFh; 2.
DR   PROSITE; PS50146; DAGK; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Calcium; Kinase; Metal-binding; Nucleotide-binding;
KW   Repeat; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    788       Diacylglycerol kinase gamma.
FT                                /FTId=PRO_0000218460.
FT   DOMAIN      172    207       EF-hand 1.
FT   DOMAIN      217    252       EF-hand 2.
FT   DOMAIN      427    561       DAGKc.
FT   CA_BIND     185    196       1 (Potential).
FT   CA_BIND     230    241       2 (Potential).
FT   ZN_FING     268    318       Phorbol-ester/DAG-type 1.
FT   ZN_FING     333    380       Phorbol-ester/DAG-type 2.
SQ   SEQUENCE   788 AA;  88523 MW;  969298DFD144F5DF CRC64;
     MSEEQWVSLS SEEFDQLQKY SEYSSKKIKD VLAEFNEGGS LRQYDPHKPI SYDVFKLFMR
     AYLEVDLPQP LSTHLFLAFS QKPRQETPDH PKEGASSSEP NVSDYNSDNA AKADEACAPD
     TESKTTKTQA PSKELEAAAP WEDPGALASS SDAPVVYLKD VVCYLSLMET GRPQDKLEFM
     FRLYDSDENG LLDQAEMDQI VSQMLHVAQY LEWDPTELRP ILKEMLQGMD YDKDGFVSLQ
     EWINGGMTTI PLLVLLGMDD SGSKGDGRHA WTLKHFKKPT YCNFCRAMLM GVGKQGLCCI
     YCKYTVHQRC VSKTIHGCVK TNSKAKRSGE VMQHAWVEGN SSVKCDRCHK SIKCYQSVTA
     RHCVWCRMTF HRKCELSTVC DGGELKDHIL LPTSICPVSG DRQGGKSDGS VAAKGELVTQ
     YKIIPSPGTH PLLVLVNPKS GGRQGERILR KFHYLLNPEQ VFNLDNGGPT PGLNFFHDTP
     DFRVLACGGD GTVGWILDCI DKANFTKHPP VAVLPLGTGN DLARCLRWGG GYEGGSLTKI
     LKEIEQSPLV MLDRWYLEVM PREEVENGDQ VPYNIMNNYF SIGVDASIAH RFHMMREKHP
     EKFNSRMKNK LWYFEFGTSE TFAATCKKLH DHIELECDGV EVDLSNIFLE GIAILNIPSM
     YGGTNLWGET KKNRAVIRES RKSVTDPKEL KCCVQDLSDQ LLEVVGLEGA MEMGQIYTGL
     KSAGRRLAQC SSVTIRTNKL LPMQVDGEPW MQPQCTIKIT HKNQAPMMMG PPQKSSFFSL
     RRKSRSKD
//
ID   FRS3_MOUSE              Reviewed;         492 AA.
AC   Q91WJ0;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Fibroblast growth factor receptor substrate 3;
DE            Short=FGFR substrate 3;
DE   AltName: Full=FRS2-beta;
GN   Name=Frs3; Synonyms=Frs2b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   MEDLINE=22574351; PubMed=12688531; DOI=10.1023/A:1022231426309;
RA   Zhou L., McDougall K., Kubu C.J., Verdi J.M., Meakin S.O.;
RT   "Genomic organization and comparative sequence analysis of the mouse
RT   and human FRS2, FRS3 genes.";
RL   Mol. Biol. Rep. 30:15-25(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH FGFR1 AND NTRK1.
RX   MEDLINE=20094977; PubMed=10629055; DOI=10.1128/MCB.20.3.979-989.2000;
RA   Ong S.-H., Guy G.R., Hadari Y.R., Laks S., Gotoh N., Schlessinger J.,
RA   Lax I.;
RT   "FRS2 proteins recruit intracellular signaling pathways by binding to
RT   diverse targets on fibroblast growth factor and nerve growth factor
RT   receptors.";
RL   Mol. Cell. Biol. 20:979-989(2000).
CC   -!- FUNCTION: Adapter protein that links FGR and NGF receptors to
CC       downstream signaling pathways. Involved in the activation of MAP
CC       kinases. Down-regulates ERK2 signaling by interfering with the
CC       phosphorylation and nuclear translocation of ERK2.
CC   -!- SUBUNIT: Binds NGFR, GRB2, PTPN11 and ERK2 (By similarity). Binds
CC       FGFR1 and NTRK1.
CC   -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
CC   -!- PTM: Phosphorylated on tyrosine residues upon stimulation by BFGF
CC       or NGFB.
CC   -!- SIMILARITY: Contains 1 IRS-type PTB domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF456480; AAO15529.1; -; Genomic_DNA.
DR   EMBL; BC014819; AAH14819.1; -; mRNA.
DR   IPI; IPI00128179; -.
DR   RefSeq; NP_659188.1; NM_144939.2.
DR   UniGene; Mm.392206; -.
DR   ProteinModelPortal; Q91WJ0; -.
DR   SMR; Q91WJ0; 6-120.
DR   STRING; Q91WJ0; -.
DR   PRIDE; Q91WJ0; -.
DR   Ensembl; ENSMUST00000024034; ENSMUSP00000024034; ENSMUSG00000023266.
DR   Ensembl; ENSMUST00000113296; ENSMUSP00000108921; ENSMUSG00000023266.
DR   GeneID; 107971; -.
DR   KEGG; mmu:107971; -.
DR   UCSC; uc008cvz.1; mouse.
DR   CTD; 107971; -.
DR   MGI; MGI:2135965; Frs3.
DR   eggNOG; roNOG04045; -.
DR   GeneTree; ENSGT00510000046707; -.
DR   HOGENOM; HBG446324; -.
DR   HOVERGEN; HBG062705; -.
DR   InParanoid; Q91WJ0; -.
DR   OMA; PSECPAQ; -.
DR   PhylomeDB; Q91WJ0; -.
DR   NextBio; 359797; -.
DR   ArrayExpress; Q91WJ0; -.
DR   Bgee; Q91WJ0; -.
DR   CleanEx; MM_FRS3; -.
DR   Genevestigator; Q91WJ0; -.
DR   GermOnline; ENSMUSG00000023266; Mus musculus.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005158; F:insulin receptor binding; IEA:InterPro.
DR   InterPro; IPR002404; Insln_rcpt_S1.
DR   InterPro; IPR011993; PH_type.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF02174; IRS; 1.
DR   SMART; SM00310; PTBI; 1.
DR   PROSITE; PS51064; IRS_PTB; 1.
PE   1: Evidence at protein level;
KW   Lipoprotein; Membrane; Myristate; Phosphoprotein.
FT   INIT_MET      1      1       Removed (Potential).
FT   CHAIN         2    492       Fibroblast growth factor receptor
FT                                substrate 3.
FT                                /FTId=PRO_0000087347.
FT   DOMAIN       13    115       IRS-type PTB.
FT   LIPID         2      2       N-myristoyl glycine (Potential).
SQ   SEQUENCE   492 AA;  53976 MW;  C0A895B9173394E6 CRC64;
     MGSCWSCLDR DSVPHNHPTK FKVTNVDDEG VELGSGVMEL TQSELVLHLH QREAVRWPYL
     CLRRYGYDSN LFSFESGRRC QTGQGIFAFK CSRAEDIFNL LQDLMQCNSI NVTEEPVIIT
     RSSHPPELDL PRGPPQPAGY TVSGFSNGFP GCPGEGPRFS SAPRRPSTSS LRHPSPGEES
     THTLIASEEQ SHTYVNTPTG DEDGRSRHCL QPLPEGRVPL PAQTQGSDQR DPQVLLQPGQ
     VKFVLGPTPA RRQVMKCQSL CPGMQDPPHH NNNEGPSECP AQPKCTYENV SGGLQQGAGW
     RLSPEERGWS GLAHRRAALL HYENLPPLPP VWESQGQQPG GEAGDDGDSR DGLTPSSNGF
     PDGEEDETPL QKPTSTRASA RSHSGFPVPL TRRRGSPRVF NFDFRRQGPE PPRQLNYIQV
     ELKGWGTARP KGPQNPSVSG APGPTPHPVR SSDSYAVIDL KKTAAMSDLQ RALPRDDGAV
     RKTRHNSTDL PL
//
ID   LRRF2_MOUSE             Reviewed;         415 AA.
AC   Q91WK0; Q8BVD1; Q9CU89;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-FEB-2011, entry version 53.
DE   RecName: Full=Leucine-rich repeat flightless-interacting protein 2;
DE            Short=LRR FLII-interacting protein 2;
GN   Name=Lrrfip2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Colon, Intestine, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-114 AND SER-116, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May function as activator of the canonical Wnt signaling
CC       pathway, in association with DVL3, upstream of CTNNB1/beta-catenin
CC       (By similarity).
CC   -!- SUBUNIT: Interacts with DVL3 and FLII (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q91WK0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q91WK0-2; Sequence=VSP_019678;
CC   -!- SIMILARITY: Belongs to the LRRFIP family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK017217; BAB30640.1; -; mRNA.
DR   EMBL; AK078881; BAC37441.1; -; mRNA.
DR   EMBL; BC014761; AAH14761.1; -; mRNA.
DR   IPI; IPI00314075; -.
DR   IPI; IPI00661214; -.
DR   RefSeq; NP_001158310.1; NM_001164838.1.
DR   RefSeq; NP_082018.1; NM_027742.3.
DR   UniGene; Mm.302287; -.
DR   ProteinModelPortal; Q91WK0; -.
DR   SMR; Q91WK0; 337-402.
DR   STRING; Q91WK0; -.
DR   PRIDE; Q91WK0; -.
DR   Ensembl; ENSMUST00000035078; ENSMUSP00000035078; ENSMUSG00000032497.
DR   Ensembl; ENSMUST00000098340; ENSMUSP00000095944; ENSMUSG00000032497.
DR   GeneID; 71268; -.
DR   KEGG; mmu:71268; -.
DR   UCSC; uc009rvm.1; mouse.
DR   UCSC; uc009rvn.1; mouse.
DR   CTD; 71268; -.
DR   MGI; MGI:1918518; Lrrfip2.
DR   eggNOG; roNOG04338; -.
DR   GeneTree; ENSGT00530000063564; -.
DR   HOVERGEN; HBG061558; -.
DR   NextBio; 333415; -.
DR   ArrayExpress; Q91WK0; -.
DR   Bgee; Q91WK0; -.
DR   Genevestigator; Q91WK0; -.
DR   GermOnline; ENSMUSG00000032497; Mus musculus.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR019139; Leu-rich_rep_flightless-int_pr.
DR   PANTHER; PTHR19212; Leu-rich_rep_flightless-int_pr; 1.
DR   Pfam; PF09738; DUF2051; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Phosphoprotein;
KW   Wnt signaling pathway.
FT   CHAIN         1    415       Leucine-rich repeat flightless-
FT                                interacting protein 2.
FT                                /FTId=PRO_0000245247.
FT   COILED       22     49       Potential.
FT   COILED      121    217       Potential.
FT   COILED      260    408       Potential.
FT   MOD_RES     103    103       Phosphoserine (By similarity).
FT   MOD_RES     106    106       Phosphoserine (By similarity).
FT   MOD_RES     107    107       Phosphoserine (By similarity).
FT   MOD_RES     111    111       Phosphoserine.
FT   MOD_RES     114    114       Phosphothreonine.
FT   MOD_RES     116    116       Phosphoserine.
FT   VAR_SEQ      60     74       Missing (in isoform 2).
FT                                /FTId=VSP_019678.
FT   CONFLICT    105    105       Q -> N (in Ref. 1; BAC37441).
SQ   SEQUENCE   415 AA;  47148 MW;  9A877ACA5A7264B8 CRC64;
     MGTPGSGRKR TPVKDRFSAE DEALSNIARE AEARLAAKRA ARAEARDIRM RELERQQREG
     VEDTLSLRSL GSHRLDEKSD KQYAENYTRP SSRNSASATT PLSGQSSRRG SGDTSSLIDP
     DTSLSELRES LSEVEEKYKK AMVSNAQLDN EKNNLIYQVD TLKDVIEEQE EQMAEFYREN
     EEKSKELERQ KHMCSVLQHK MDELKEGLRQ RDELIEKHGL VIIPDSTPNG DVHHEPVVGA
     ITAVSQEAAQ VLESAGEGPL DVRLRKLAGE KDELLSQIRK LKLQLEEERQ KCSRNDGMSG
     DLAGLQNGSD LQFIEMQRDA NRQISEYKFK LSKAEQDIAT LEQSISRLEG QVLRYKTAAE
     NAEKIEDELK AERRKLQREL RTAQDKIEEM EMTNSHLAKR LEKMKANRTA LLAQQ
//
ID   WWOX_MOUSE              Reviewed;         414 AA.
AC   Q91WL8; Q8C8J6; Q920Y2; Q9D2B3; Q9D339; Q9JLF5;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=WW domain-containing oxidoreductase;
DE            EC=1.1.1.-;
GN   Name=Wwox; Synonyms=Wox1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INDUCTION,
RP   SUBCELLULAR LOCATION, MUTAGENESIS OF 51-LYS--ARG-54, DOMAIN, AND
RP   INTERACTION WITH TP53.
RC   TISSUE=Fibroblast;
RX   MEDLINE=21264809; PubMed=11058590; DOI=10.1074/jbc.M007140200;
RA   Chang N.-S., Pratt N., Heath J., Schultz L., Sleve D., Carey G.B.,
RA   Zevotek N.;
RT   "Hyaluronidase induction of a WW domain-containing oxidoreductase that
RT   enhances tumor necrosis factor cytotoxicity.";
RL   J. Biol. Chem. 276:3361-3370(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Colon, Embryo, and Pituitary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 173-414.
RX   PubMed=11979549; DOI=10.1002/gcc.10047;
RA   Krummel K.A., Denison S.R., Calhoun E., Phillips L.A., Smith D.I.;
RT   "The common fragile site FRA16D and its associated gene WWOX are
RT   highly conserved in the mouse at Fra8E1.";
RL   Genes Chromosomes Cancer 34:154-167(2002).
RN   [5]
RP   INTERACTION WITH MAPK8 AND TP53.
RX   PubMed=12514174; DOI=10.1074/jbc.M208373200;
RA   Chang N.-S., Doherty J., Ensign A.;
RT   "JNK1 physically interacts with WW domain-containing oxidoreductase
RT   (WOX1) and inhibits WOX1-mediated apoptosis.";
RL   J. Biol. Chem. 278:9195-9202(2003).
RN   [6]
RP   INTERACTION WITH MAPT.
RX   PubMed=15126504; DOI=10.1074/jbc.M401399200;
RA   Sze C.-I., Su M., Pugazhenthi S., Jambal P., Hsu L.-J., Heath J.,
RA   Schultz L., Chang N.-S.;
RT   "Down-regulation of WW domain-containing oxidoreductase induces Tau
RT   phosphorylation in vitro. A potential role in Alzheimer's disease.";
RL   J. Biol. Chem. 279:30498-30506(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [8]
RP   DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=15026124; DOI=10.1016/j.neuroscience.2003.12.036;
RA   Chen S.-T., Chuang J.-I., Wang J.P., Tsai M.S., Li H., Chang N.-S.;
RT   "Expression of WW domain-containing oxidoreductase WOX1 in the
RT   developing murine nervous system.";
RL   Neuroscience 124:831-839(2004).
RN   [9]
RP   INTERACTION WITH TP53, AND DOMAIN.
RX   PubMed=16219768; DOI=10.1074/jbc.M505590200;
RA   Chang N.-S., Doherty J., Ensign A., Schultz L., Hsu L.-J., Hong Q.;
RT   "WOX1 is essential for tumor necrosis factor-, UV light-,
RT   staurosporine-, and p53-mediated cell death, and its tyrosine 33-
RT   phosphorylated form binds and stabilizes serine 46-phosphorylated
RT   p53.";
RL   J. Biol. Chem. 280:43100-43108(2005).
RN   [10]
RP   INDUCTION.
RX   PubMed=15664696; DOI=10.1016/j.neuroscience.2004.07.054;
RA   Chen S.-T., Chuang J.-I., Cheng C.-L., Hsu L.-J., Chang N.-S.;
RT   "Light-induced retinal damage involves tyrosine 33 phosphorylation,
RT   mitochondrial and nuclear translocation of WW domain-containing
RT   oxidoreductase in vivo.";
RL   Neuroscience 130:397-407(2005).
RN   [11]
RP   DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=17360458; DOI=10.1073/pnas.0609783104;
RA   Aqeilan R.I., Trapasso F., Hussain S., Costinean S., Marshall D.,
RA   Pekarsky Y., Hagan J.P., Zanesi N., Kaou M., Stein G.S., Lian J.B.,
RA   Croce C.M.;
RT   "Targeted deletion of Wwox reveals a tumor suppressor function.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:3949-3954(2007).
RN   [12]
RP   DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=18487609; DOI=10.1074/jbc.M800855200;
RA   Aqeilan R.I., Hassan M.Q., de Bruin A., Hagan J.P., Volinia S.,
RA   Palumbo T., Hussain S., Lee S.-H., Gaur T., Stein G.S., Lian J.B.,
RA   Croce C.M.;
RT   "The WWOX tumor suppressor is essential for postnatal survival and
RT   normal bone metabolism.";
RL   J. Biol. Chem. 283:21629-21639(2008).
RN   [13]
RP   FUNCTION, PHOSPHORYLATION AT TYR-33, SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH HYAL2.
RX   PubMed=19366691; DOI=10.1074/jbc.M806688200;
RA   Hsu L.-J., Schultz L., Hong Q., Van Moer K., Heath J., Li M.-Y.,
RA   Lai F.-J., Lin S.-R., Lee M.-H., Lo C.-P., Lin Y.-S., Chen S.-T.,
RA   Chang N.-S.;
RT   "Transforming growth factor beta1 signaling via interaction with cell
RT   surface Hyal-2 and recruitment of WWOX/WOX1.";
RL   J. Biol. Chem. 284:16049-16059(2009).
CC   -!- FUNCTION: Putative oxidoreductase. Acts as a tumor suppressor and
CC       plays a role in apoptosis. May function synergistically with
CC       p53/TP53 to control genotoxic stress-induced cell death. Plays a
CC       role in TGFB1 signaling and TGFB1-mediated cell death. Inhibits
CC       Wnt signaling, probably by sequestering DVL2 in the cytoplasm (By
CC       similarity). May also play a role in tumor necrosis factor (TNF)-
CC       mediated cell death. Required for normal bone development.
CC   -!- SUBUNIT: Interacts with TP53, TP73/p73 and MAPK8. Interacts with
CC       MAPT/TAU. Forms a ternary complex with TP53 and MDM2 and interacts
CC       with ERBB4, LITAF and WBP1. May interact with COTE1 and SCOTIN (By
CC       similarity). Interacts with HYAL2 and RUNX2. Interacts with TNK2
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Mitochondrion (By
CC       similarity). Note=Partially localizes to the mitochondria (By
CC       similarity). Translocates to the nucleus in response to TGFB1 (By
CC       similarity). Translocates to the nucleus upon genotoxic stress or
CC       TNF stimulation.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=Wox1;
CC         IsoId=Q91WL8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q91WL8-2; Sequence=VSP_016370, VSP_016371;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q91WL8-3; Sequence=VSP_016373, VSP_016374;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q91WL8-4; Sequence=VSP_016372, VSP_016375;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. In the brain, expressed in cortex,
CC       striatum, hippocampus and cerebellum (at protein level). Detected
CC       in embryonic skeleton, in cranofacial bones, vertebrae and limb
CC       bones. Detected in chondrocytes and osteoblasts.
CC   -!- DEVELOPMENTAL STAGE: Expression starts at E8 in the developing
CC       heart. Higher expression in the brain is detected between E12 and
CC       E16. High levels of expression in dorsal root ganglia and spinal
CC       nerves were observed throughout all developmental stages. In later
CC       developmental stages expression is more prominent in skeletal
CC       systems (at protein level).
CC   -!- INDUCTION: By hyaluronidase. Up-regulated in outer and inner
CC       nuclear layers during retinal degeneration.
CC   -!- DOMAIN: The WW 1 domain mediates interaction with TP73, TFAP2C,
CC       LITAF, WBP1 and probably TP53.
CC   -!- PTM: Phosphorylated upon genotoxic stress. Phosphorylation of Tyr-
CC       33 regulates interaction with TP53, TP73 and MAPK8. May also
CC       regulate proapoptotic activity. Phosphorylation by TNK2 is
CC       associated with polyubiquitination and degradation (By
CC       similarity).
CC   -!- PTM: Ubiquitinated when phosphorylated by TNK2, leading to its
CC       degradation (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Indistinguishable from wild-type at birth,
CC       but die after three weeks due to metabolic syndrome characterized
CC       by serum hypoproteinemia, hypoalbuminemia, hypoglycemia,
CC       hypocalcemia, hypotriglyceridemia and hypocholesterolemia, growth
CC       retardation, decreased bone formation and increased bone
CC       resorption. In addition, spontaneous tumor development was
CC       observed.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases
CC       (SDR) family.
CC   -!- SIMILARITY: Contains 2 WW domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF187014; AAF31693.1; -; mRNA.
DR   EMBL; AK018507; BAB31244.1; -; mRNA.
DR   EMBL; AK019911; BAB31911.1; -; mRNA.
DR   EMBL; AK046903; BAC32916.1; -; mRNA.
DR   EMBL; AK078528; BAC37325.1; -; mRNA.
DR   EMBL; BC014716; AAH14716.1; -; mRNA.
DR   EMBL; AY046556; AAL03972.1; -; Genomic_DNA.
DR   EMBL; AY046553; AAL03972.1; JOINED; Genomic_DNA.
DR   EMBL; AY046554; AAL03972.1; JOINED; Genomic_DNA.
DR   EMBL; AY046555; AAL03972.1; JOINED; Genomic_DNA.
DR   IPI; IPI00331266; -.
DR   IPI; IPI00405951; -.
DR   IPI; IPI00656214; -.
DR   IPI; IPI00656224; -.
DR   RefSeq; NP_062519.2; NM_019573.3.
DR   UniGene; Mm.440420; -.
DR   ProteinModelPortal; Q91WL8; -.
DR   SMR; Q91WL8; 10-101, 120-375.
DR   STRING; Q91WL8; -.
DR   PhosphoSite; Q91WL8; -.
DR   PRIDE; Q91WL8; -.
DR   Ensembl; ENSMUST00000004756; ENSMUSP00000004756; ENSMUSG00000004637.
DR   Ensembl; ENSMUST00000109107; ENSMUSP00000104735; ENSMUSG00000004637.
DR   Ensembl; ENSMUST00000109108; ENSMUSP00000104736; ENSMUSG00000004637.
DR   GeneID; 80707; -.
DR   KEGG; mmu:80707; -.
DR   UCSC; uc009noc.1; mouse.
DR   UCSC; uc009nod.1; mouse.
DR   CTD; 80707; -.
DR   MGI; MGI:1931237; Wwox.
DR   eggNOG; roNOG06975; -.
DR   GeneTree; ENSGT00570000078948; -.
DR   HOGENOM; HBG750976; -.
DR   HOVERGEN; HBG078800; -.
DR   InParanoid; Q91WL8; -.
DR   OMA; ILGEWHK; -.
DR   OrthoDB; EOG498V1T; -.
DR   PhylomeDB; Q91WL8; -.
DR   NextBio; 350059; -.
DR   ArrayExpress; Q91WL8; -.
DR   Bgee; Q91WL8; -.
DR   CleanEx; MM_WWOX; -.
DR   Genevestigator; Q91WL8; -.
DR   GermOnline; ENSMUSG00000004637; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0006917; P:induction of apoptosis; IDA:MGI.
DR   GO; GO:0030178; P:negative regulation of Wnt receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0001649; P:osteoblast differentiation; IMP:MGI.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR002198; DH_sc/Rdtase_SDR.
DR   InterPro; IPR002347; Glc/ribitol_DH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00106; adh_short; 1.
DR   Pfam; PF00397; WW; 2.
DR   PRINTS; PR00081; GDHRDH.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF51045; WW_Rsp5_WWP; 2.
DR   PROSITE; PS00061; ADH_SHORT; FALSE_NEG.
DR   PROSITE; PS01159; WW_DOMAIN_1; 2.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Cytoplasm; Mitochondrion; NADP;
KW   Nucleus; Oxidoreductase; Phosphoprotein; Repeat; Tumor suppressor;
KW   Ubl conjugation; Wnt signaling pathway.
FT   CHAIN         1    414       WW domain-containing oxidoreductase.
FT                                /FTId=PRO_0000054816.
FT   DOMAIN       16     49       WW 1.
FT   DOMAIN       57     90       WW 2.
FT   NP_BIND     131    137       NADP (By similarity).
FT   REGION      125    414       Interaction with MAPT.
FT   REGION      209    273       Mediates targeting to the mitochondria.
FT   MOTIF        50     55       Nuclear localization signal.
FT   ACT_SITE    293    293       Proton acceptor (By similarity).
FT   BINDING     260    260       Substrate (By similarity).
FT   MOD_RES      12     12       Phosphothreonine (By similarity).
FT   MOD_RES      14     14       Phosphoserine.
FT   MOD_RES      33     33       Phosphotyrosine.
FT   MOD_RES     287    287       Phosphotyrosine; by TNK2 (By similarity).
FT   VAR_SEQ     137    158       GFETAKSFALHGAHVILACRNL -> ALSPLLGERCIRRRQ
FT                                VLCSVFG (in isoform 2).
FT                                /FTId=VSP_016370.
FT   VAR_SEQ     159    414       Missing (in isoform 2).
FT                                /FTId=VSP_016371.
FT   VAR_SEQ     353    367       QQGAATTVYCAVAPE -> KPCMIGHTCDPNPRN (in
FT                                isoform 4).
FT                                /FTId=VSP_016372.
FT   VAR_SEQ     353    354       QQ -> IL (in isoform 3).
FT                                /FTId=VSP_016373.
FT   VAR_SEQ     355    414       Missing (in isoform 3).
FT                                /FTId=VSP_016374.
FT   VAR_SEQ     368    414       Missing (in isoform 4).
FT                                /FTId=VSP_016375.
FT   MUTAGEN      51     54       KRKR->QGTG: Abolishes the TNF-induced
FT                                nuclear translocation.
FT   CONFLICT    135    135       G -> V (in Ref. 2; BAB31244).
FT   CONFLICT    231    231       V -> A (in Ref. 1 and 4).
SQ   SEQUENCE   414 AA;  46512 MW;  3C83AE3085B6A931 CRC64;
     MAALRYAGLD DTDSEDELPP GWEERTTKDG WVYYANHTEE KTQWEHPKTG KRKRVAGDLP
     YGWEQETDEN GQVFFVDHIN KRTTYLDPRL AFTVDDNPTK PTTRQRYDGS TTAMEILQGR
     DFTGKVVLVT GANSGIGFET AKSFALHGAH VILACRNLSR ASEAVSRILE EWHKAKVEAM
     TLDLAVLRSV QHFAEAFKAK NVSLHVLVCN AGTFALPWGL TKDGLETTFQ VNHLGHFYLV
     QLLQDVLCRS SPARVIVVSS ESHRFTDIND SSGKLDLSRL SPPRSDYWAM LAYNRSKLCN
     ILFSNELHRR LSPRGVTSNA VHPGNMMYSA IHRNSWVYKL LFTLARPFTK SMQQGAATTV
     YCAVAPELEG LGGMYFNNCC RCLPSEEAQS EETARALWEL SERLIQDRLG SPSS
//
ID   U3IP2_MOUSE             Reviewed;         475 AA.
AC   Q91WM3; Q8CFB7;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=U3 small nucleolar RNA-interacting protein 2;
DE   AltName: Full=RRP9 homolog;
DE   AltName: Full=U3 small nucleolar ribonucleoprotein-associated 55 kDa protein;
DE            Short=U3 snoRNP-associated 55 kDa protein;
DE            Short=U3-55K;
GN   Name=Rrp9; Synonyms=Rnu3ip2, U3-55k;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=C57BL/6J;
RX   MEDLINE=22332553; PubMed=12448766;
RA   Urbanek P., Paces J., Kralova J., Dvorak M., Paces V.;
RT   "Cloning and expression of PARP-3 (Adprt3) and U3-55k, two genes
RT   closely linked on mouse chromosome 9.";
RL   Folia Biol. (Praha) 48:182-191(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-51, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-51 AND SER-470,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Component of a nucleolar small nuclear ribonucleoprotein
CC       particle (snoRNP) thought to participate in the processing and
CC       modification of pre-ribosomal RNA (By similarity).
CC   -!- SUBUNIT: Interacts specifically with the U3 small nucleolar RNA
CC       (U3 snoRNA). Binds a sub-fragment of the U3 snoRNA surrounding the
CC       B/C motif (3UBC). This association with the U3BC RNA is dependent
CC       on the binding of a protein called 15.5K to the box B/C motif. The
CC       association of the protein with the U3BC RNA was found to be also
CC       dependent on a conserved RNA structure that flanks the box B/C
CC       motif (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity).
CC   -!- DOMAIN: The WD domains are required for nucleolar localization and
CC       U3 small nucleolar RNAs binding (By similarity).
CC   -!- SIMILARITY: Belongs to the WD repeat RRP9 family.
CC   -!- SIMILARITY: Contains 7 WD repeats.
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DR   EMBL; AF368232; AAN62792.1; -; mRNA.
DR   EMBL; AF368234; AAN62794.1; -; Genomic_DNA.
DR   EMBL; AK076113; BAC36193.1; -; mRNA.
DR   EMBL; BC014703; AAH14703.1; -; mRNA.
DR   IPI; IPI00128256; -.
DR   RefSeq; NP_663595.1; NM_145620.4.
DR   UniGene; Mm.239997; -.
DR   ProteinModelPortal; Q91WM3; -.
DR   SMR; Q91WM3; 136-455.
DR   STRING; Q91WM3; -.
DR   PhosphoSite; Q91WM3; -.
DR   PRIDE; Q91WM3; -.
DR   Ensembl; ENSMUST00000047721; ENSMUSP00000038580; ENSMUSG00000041506.
DR   GeneID; 27966; -.
DR   KEGG; mmu:27966; -.
DR   UCSC; uc009rkb.1; mouse.
DR   CTD; 27966; -.
DR   MGI; MGI:2384313; Rrp9.
DR   eggNOG; roNOG08003; -.
DR   GeneTree; ENSGT00550000075093; -.
DR   HOGENOM; HBG713247; -.
DR   HOVERGEN; HBG079296; -.
DR   InParanoid; Q91WM3; -.
DR   OMA; GSHSSCV; -.
DR   OrthoDB; EOG4XKV6X; -.
DR   PhylomeDB; Q91WM3; -.
DR   NextBio; 306456; -.
DR   ArrayExpress; Q91WM3; -.
DR   Bgee; Q91WM3; -.
DR   Genevestigator; Q91WM3; -.
DR   GermOnline; ENSMUSG00000041506; Mus musculus.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 6.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Repeat; Ribonucleoprotein; RNA-binding;
KW   rRNA processing; WD repeat.
FT   CHAIN         1    475       U3 small nucleolar RNA-interacting
FT                                protein 2.
FT                                /FTId=PRO_0000051314.
FT   REPEAT      144    183       WD 1.
FT   REPEAT      197    236       WD 2.
FT   REPEAT      239    278       WD 3.
FT   REPEAT      281    320       WD 4.
FT   REPEAT      322    360       WD 5.
FT   REPEAT      374    413       WD 6.
FT   REPEAT      419    460       WD 7.
FT   MOTIF         8     40       Nuclear localization signal (Potential).
FT   COMPBIAS     47    105       Glu-rich.
FT   MOD_RES      50     50       Phosphoserine.
FT   MOD_RES      51     51       Phosphoserine.
FT   MOD_RES      53     53       Phosphoserine (By similarity).
FT   MOD_RES      57     57       Phosphoserine (By similarity).
FT   MOD_RES     470    470       Phosphoserine.
FT   MOD_RES     475    475       Phosphoserine (By similarity).
SQ   SEQUENCE   475 AA;  52107 MW;  EF7E2B2D9CD68F6B CRC64;
     MSTAVATRKR AKPAPGPGAA PVAGKRRRKV DSAADRGKSK GGGKMNEEIS SDSESESLAP
     RKTEEEEEEE LEETAQEKKL RLAKLYLEQL RQQEEEKAEA RAFEEDQVAG RLKEDVLEQR
     GRLQKSVAKE IQAPAPTDIR VLRGHQLSIT CLVITPDDLA IFSAAKDCTI IKWSVETGRK
     LHVIPRAKKG AQGQPAGHSS HVLCMAISSD GKYLASGDRS KLILIWEAQS CQHLYTFTGH
     RDAVSGLAFR KGTHQLYSTS HDRSVKVWNA AENSYVETLF GHQDAVAALD ALSRECCVTA
     GGRDGTVRVW KIPEESQLVF YGHQGSIDCI HLINEEHMVS GADDGSVALW GLSKKRPLAL
     QREAHGLHGE PGLEQPFWVS SVAALLNTDL VATGSHNARV RLWQCGEGFR QLDPLCDIPL
     VGFINSLKFS SAGDFLVAGV GQEHRLGRWW RIKEARNSVC IIPLRRLPVS PVAGS
//
ID   F176A_MOUSE             Reviewed;         156 AA.
AC   Q91WM6;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Protein FAM176A;
DE   AltName: Full=Transmembrane protein 166;
GN   Name=Fam176a; Synonyms=Tmem166;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Acts as a regulator of programmed cell death, mediating
CC       both autophagy and apoptosis (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       membrane protein (By similarity). Lysosome membrane; Single-pass
CC       membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the FAM176 family.
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DR   EMBL; AK145140; BAE26256.1; -; mRNA.
DR   EMBL; BC014699; AAH14699.1; -; mRNA.
DR   EMBL; BC027150; AAH27150.1; -; mRNA.
DR   IPI; IPI00128257; -.
DR   UniGene; Mm.205854; -.
DR   PhosphoSite; Q91WM6; -.
DR   PRIDE; Q91WM6; -.
DR   Ensembl; ENSMUST00000042974; ENSMUSP00000037422; ENSMUSG00000035104.
DR   UCSC; uc009clg.1; mouse.
DR   MGI; MGI:2385247; Fam176a.
DR   eggNOG; roNOG16735; -.
DR   GeneTree; ENSGT00400000022026; -.
DR   HOGENOM; HBG446118; -.
DR   HOVERGEN; HBG061487; -.
DR   InParanoid; Q91WM6; -.
DR   OrthoDB; EOG4WDDBW; -.
DR   ArrayExpress; Q91WM6; -.
DR   Bgee; Q91WM6; -.
DR   Genevestigator; Q91WM6; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Apoptosis; Autophagy; Endoplasmic reticulum; Lysosome; Membrane;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    156       Protein FAM176A.
FT                                /FTId=PRO_0000278672.
FT   TRANSMEM     40     60       Helical; (Potential).
SQ   SEQUENCE   156 AA;  17810 MW;  1074F3E67FAD4C40 CRC64;
     MKLPLSPSTE PVATEPLGMA LLSSLLAAWS YISENPERAA LYFVSGVCIG LFLTLAALVM
     RISCHTDCRR GPRRRCLQDR ECSDSSDSED GSEDTASDLS VRRHRRFERT LNKNVFTSAE
     ELERAQRLEE RERIIREIWM NGQPEVPGTR SLNRYY
//
ID   SH319_MOUSE             Reviewed;         789 AA.
AC   Q91X43; O08635; O35146; Q8C7I2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=SH3 domain-containing protein 19;
DE   AltName: Full=Kryn;
GN   Name=Sh3d19;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP   INTERACTION WITH SH3YL1.
RX   PubMed=12615363; DOI=10.1016/S0923-1811(02)00140-8;
RA   Shimomura Y., Aoki N., Ito K., Ito M.;
RT   "Gene expression of Sh3d19, a novel adaptor protein with five Src
RT   homology 3 domains, in anagen mouse hair follicles.";
RL   J. Dermatol. Sci. 31:43-51(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 13-789 (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Colon, and Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 465-789.
RA   Sekely S.A., Kay B.K.;
RL   Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 505-789.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-676, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: May play a role in regulating A disintegrin and
CC       metalloproteases (ADAMs) in the signaling of EGFR-ligand shedding.
CC       May be involved in suppression of Ras-induced cellular
CC       transformation and Ras-mediated activation of ELK1 (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with ADAM12. Isoform 2 (but not isoform 1)
CC       interacts with ADAM9, ADAM10, ADAM15 and ADAM17. Interacts with
CC       SH3GL1 SH3 domain. Interacts via SH3 3 and SH3 4 or SH3 4 and SH3
CC       5 domains with SOS2. Probably forms a trimeric complex with SH3GL1
CC       and SOS2 (By similarity). Interacts with SH3YL1.
CC   -!- INTERACTION:
CC       O08641:Sh3yl1; NbExp=1; IntAct=EBI-2024543, EBI-2024519;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q91X43-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q91X43-2; Sequence=VSP_031185;
CC   -!- TISSUE SPECIFICITY: Expressed in hair follicles.
CC   -!- SIMILARITY: Contains 5 SH3 domains.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB82091.1; Type=Miscellaneous discrepancy; Note=Sequence contamination. Potenial vector sequence;
CC       Sequence=AAH12633.1; Type=Miscellaneous discrepancy; Note=Sequence contamination. Potential vector sequence;
CC       Sequence=AAH31117.1; Type=Erroneous initiation;
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DR   EMBL; D89677; BAA19686.2; -; mRNA.
DR   EMBL; AC133508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC012633; AAH12633.1; ALT_SEQ; mRNA.
DR   EMBL; BC031117; AAH31117.1; ALT_INIT; mRNA.
DR   EMBL; AF003234; AAB82091.1; ALT_SEQ; mRNA.
DR   EMBL; AK050185; BAC34114.1; -; mRNA.
DR   IPI; IPI00830768; -.
DR   IPI; IPI00886292; -.
DR   RefSeq; NP_001075883.2; NM_001082414.2.
DR   UniGene; Mm.2454; -.
DR   ProteinModelPortal; Q91X43; -.
DR   SMR; Q91X43; 418-630, 663-788.
DR   IntAct; Q91X43; 3.
DR   STRING; Q91X43; -.
DR   PhosphoSite; Q91X43; -.
DR   PRIDE; Q91X43; -.
DR   Ensembl; ENSMUST00000029723; ENSMUSP00000029723; ENSMUSG00000028082.
DR   GeneID; 27059; -.
DR   KEGG; mmu:27059; -.
DR   CTD; 27059; -.
DR   MGI; MGI:1350923; Sh3d19.
DR   eggNOG; roNOG10311; -.
DR   GeneTree; ENSGT00550000074287; -.
DR   HOGENOM; HBG506650; -.
DR   HOVERGEN; HBG108486; -.
DR   InParanoid; Q91X43; -.
DR   OrthoDB; EOG4GB75H; -.
DR   NextBio; 305017; -.
DR   ArrayExpress; Q91X43; -.
DR   Bgee; Q91X43; -.
DR   CleanEx; MM_SH3D19; -.
DR   Genevestigator; Q91X43; -.
DR   InterPro; IPR000108; p67phox.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00018; SH3_1; 4.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR00499; P67PHOX.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 5.
DR   SUPFAM; SSF50044; SH3; 5.
DR   PROSITE; PS50002; SH3; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Phosphoprotein; Repeat; SH3 domain.
FT   CHAIN         1    789       SH3 domain-containing protein 19.
FT                                /FTId=PRO_0000318198.
FT   DOMAIN      417    472       SH3 1.
FT   DOMAIN      494    553       SH3 2.
FT   DOMAIN      570    629       SH3 3.
FT   DOMAIN      660    719       SH3 4.
FT   DOMAIN      729    788       SH3 5.
FT   COMPBIAS     29    352       Pro-rich.
FT   MOD_RES     150    150       Phosphoserine (By similarity).
FT   MOD_RES     451    451       Phosphotyrosine (By similarity).
FT   MOD_RES     676    676       Phosphoserine.
FT   VAR_SEQ       1    369       Missing (in isoform 2).
FT                                /FTId=VSP_031185.
FT   CONFLICT    559    559       S -> G (in Ref. 5; BAC34114).
SQ   SEQUENCE   789 AA;  86077 MW;  D3F866FB1A5BEB81 CRC64;
     MNIMNTEQSQ NTIVSRIKAF EGQTNTEIPG LPKKPEIIPR TIPPKPAVSS GKPLVAPKPA
     ANRASGEWDT WAENRLKVTS REGLTPYSSP QEAGITPVTK PELPKKPTPG LTRSVNHETS
     GGRPMAESPD TGKKIPTPAP RPLLPKKSAS TDAPPYPSIP PKLVSAPPRL SVASQAKAFR
     SLGEGLPSNP PVPAPQSKAL GDIDLISFDD DVLPTSGSPA EEPTGSETVL DPFQLPTKTE
     ATKERAVQPA PTRKPTVIRI PAKPGKCLHE EPQSPPPLPA EKPVGNTHSA VSGRPSHSDR
     TRNPELEQAS ESGGLVQGPP RLPPRPVHGK VIPVWRPPPK GAPERPPPPK LPASKSSNKN
     LPFNRSSSDM DLQKKQSHFV SGLSKAKSQI FKNQDPVLPP RPKPGHPLYR KYMLSVPHGI
     ANEDIVSRNP TELSCKRGDV LVILKQAENN YLECQRGEGT GRVHPSQMKI VTPLDERPRG
     RPNDSGHSQK PVDSGAPHAV ALHDFPAEQA DDLSLTSGEI VYLLEKIDAE WYRGKCRNQT
     GVFPANYVKV IVDIPEGRSG KRESFSSHCA KGPRCVARFE YIGDQKDELS FSEGEVIILT
     EYVNEEWGRG EIRDRSGIFP LNFVELVGDH PTSGANILST KVPPKTKNED PGSNSQDSSP
     PGEWCKALHS FTAETSEDLP FKRGDRILIL ERLDSDWYRG RLHDREGIFP AVFVQPCPAE
     AKGVASAIPK GRKVKALYDF LGENEDELSF KAGDVITELE PIDDAWMRGE LMGRAGMFPK
     NYVQFLQVS
//
ID   GORS1_MOUSE             Reviewed;         446 AA.
AC   Q91X51; Q9D3L9;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Golgi reassembly-stacking protein 1;
DE   AltName: Full=Golgi peripheral membrane protein p65;
DE   AltName: Full=Golgi reassembly-stacking protein of 65 kDa;
DE            Short=GRASP65;
GN   Name=Gorasp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 312-446.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Stacking factor involved in the postmitotic assembly of
CC       Golgi stacks from mitotic Golgi fragments. Key structural protein
CC       required for the maintenance of the Golgi apparatus integrity: its
CC       caspase-mediated cleavage is required for fragmentation of the
CC       Golgi during apoptosis. Also mediates, via its interaction with
CC       GM130, the docking of transport vesicles with the Golgi membranes
CC       (By similarity).
CC   -!- SUBUNIT: Homodimer. Forms higher order oligomers under interphase
CC       but not mitotic conditions. Dimers of the protein on one membrane
CC       might be able to interact with dimers on another and so stack
CC       cisternae. Interacts with the C-terminus of GM130 under both
CC       mitotic and non-mitotic conditions. The interaction is critical
CC       for the correct targeting of both proteins to the cis-Golgi. The
CC       complex binds to the vesicle docking protein p115 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane;
CC       Peripheral membrane protein; Cytoplasmic side. Note=Undergoes
CC       rapid exchange with the cytosol (By similarity).
CC   -!- PTM: Phosphorylated by CDC2/B1 and PLK kinases during mitosis.
CC       Phosphorylation cycle correlates with the cisternal stacking
CC       cycle. Phosphorylation of the homodimer prevents the association
CC       of dimers into higher order oligomers, leading to cisternal
CC       unstacking (By similarity).
CC   -!- PTM: Target for caspase-3 cleavage during apoptosis. The cleavage
CC       contributes to Golgi fragmentation and occurs very early in the
CC       execution phase of apoptosis (By similarity).
CC   -!- SIMILARITY: Belongs to the GORASP family.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB30676.1; Type=Erroneous initiation;
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DR   EMBL; BC012251; AAH12251.1; -; mRNA.
DR   EMBL; AK017293; BAB30676.1; ALT_INIT; mRNA.
DR   IPI; IPI00128425; -.
DR   RefSeq; NP_083252.1; NM_028976.2.
DR   UniGene; Mm.104789; -.
DR   ProteinModelPortal; Q91X51; -.
DR   SMR; Q91X51; 17-99, 110-181.
DR   STRING; Q91X51; -.
DR   PhosphoSite; Q91X51; -.
DR   PRIDE; Q91X51; -.
DR   Ensembl; ENSMUST00000035099; ENSMUSP00000035099; ENSMUSG00000032513.
DR   GeneID; 74498; -.
DR   KEGG; mmu:74498; -.
DR   UCSC; uc009sbq.1; mouse.
DR   CTD; 74498; -.
DR   MGI; MGI:1921748; Gorasp1.
DR   GeneTree; ENSGT00390000008686; -.
DR   HOGENOM; HBG713939; -.
DR   HOVERGEN; HBG051826; -.
DR   InParanoid; Q91X51; -.
DR   OMA; SGPEDVC; -.
DR   OrthoDB; EOG40P46V; -.
DR   PhylomeDB; Q91X51; -.
DR   NextBio; 340958; -.
DR   ArrayExpress; Q91X51; -.
DR   Bgee; Q91X51; -.
DR   CleanEx; MM_GORASP1; -.
DR   Genevestigator; Q91X51; -.
DR   GermOnline; ENSMUSG00000032513; Mus musculus.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR007583; GRASP55_65.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   PANTHER; PTHR12893; GRASP55_65; 1.
DR   Pfam; PF04495; GRASP55_65; 2.
DR   SUPFAM; SSF50156; PDZ; 2.
DR   PROSITE; PS50106; PDZ; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Golgi apparatus; Lipoprotein; Membrane; Myristate; Phosphoprotein;
KW   Protein transport; Transport.
FT   INIT_MET      1      1       Removed (Probable).
FT   CHAIN         2    446       Golgi reassembly-stacking protein 1.
FT                                /FTId=PRO_0000087571.
FT   DOMAIN        5     74       PDZ.
FT   REGION      189    201       Essential for the interaction with GM130
FT                                (By similarity).
FT   COMPBIAS    298    301       Poly-Pro.
FT   COMPBIAS    314    355       Ser-rich.
FT   COMPBIAS    351    355       Poly-Ser.
FT   MOD_RES     220    220       Phosphothreonine (By similarity).
FT   MOD_RES     224    224       Phosphothreonine (By similarity).
FT   MOD_RES     251    251       Phosphoserine (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (Probable).
SQ   SEQUENCE   446 AA;  46882 MW;  05A59D996B9AD56B CRC64;
     MGLGASSEQP AGGEGFHLHG VQENSPAQQA GLEPYFDFII TIGHSRLNKE NDTLKALLKA
     NVEKPVKLEV FNMKTMKVRE VEVVPSNMWG GQGLLGASVR FCSFRRASEH VWHVLDVEPS
     SPAALAGLCP YTDYIVGSDQ ILQESEDFFT LIESHEGKPL KLMVYNSESD SCREVTVTPN
     AAWGGEGSLG CGIGYGYLHR IPTQPSSQHK KPPGATPPGT PATTSQLTAF PLGAPPPWPI
     PQDSSGPELG SRQSDFMEAL PQVPGSFMEG QLLGPGSPSH GAADCGGCLR AMEIPLQPPP
     PVQRVMDPGF LDVSGMSLLD SSNISVCPSL SSSTVLTSTA VSVSGPEDIG SSSSSHERGG
     EATWSGSEFE ISFPDSPGAQ AQADHLPRLT LPDGLTSAAS PEEGLSAELL EAQTEEPADT
     ASLDCRAETE GRASQAQATP DPEPGL
//
ID   S1PR5_MOUSE             Reviewed;         400 AA.
AC   Q91X56; Q99MN8;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Sphingosine 1-phosphate receptor 5;
DE            Short=S1P receptor 5;
DE            Short=S1P5;
DE   AltName: Full=Endothelial differentiation G-protein-coupled receptor 8;
DE   AltName: Full=Lysophospholipid receptor B4;
DE   AltName: Full=Sphingosine 1-phosphate receptor Edg-8;
DE            Short=S1P receptor Edg-8;
GN   Name=S1pr5; Synonyms=Edg8, Lpb4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 14-400.
RC   STRAIN=Swiss Webster / NIH;
RA   Yang A.H., Zhang G., Chun J.J.M.;
RT   "Molecular cloning of the mouse sphingosine-1-phosphate receptor gene,
RT   Lpb4.";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-400.
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=11705398; DOI=10.1021/bi011606i;
RA   Im D.-S., Clemens J., Macdonald T.L., Lynch K.R.;
RT   "Characterization of the human and mouse sphingosine 1-phosphate
RT   receptor, S1P5 (Edg-8): structure-activity relationship of
RT   sphingosine1-phosphate receptors.";
RL   Biochemistry 40:14053-14060(2001).
RN   [5]
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND FUNCTION.
RX   PubMed=15703400; DOI=10.1523/JNEUROSCI.4645-04.2005;
RA   Jaillard C., Harrison S., Stankoff B., Aigrot M.S., Calver A.R.,
RA   Duddy G., Walsh F.S., Pangalos M.N., Arimura N., Kaibuchi K., Zalc B.,
RA   Lubetzki C.;
RT   "Edg8/S1P5: an oligodendroglial receptor with dual function on process
RT   retraction and cell survival.";
RL   J. Neurosci. 25:1459-1469(2005).
CC   -!- FUNCTION: Receptor for the lysosphingolipid sphingosine 1-
CC       phosphate (S1P). S1P is a bioactive lysophospholipid that elicits
CC       diverse physiological effect on most types of cells and tissues.
CC       Is coupled to both the G(i/0)alpha and G(12) subclass of
CC       heteromeric G-proteins (By similarity). S1P activation on
CC       oligodendroglial cells modulates two distinct functional pathways
CC       mediating either process retraction or cell survival. S1P
CC       activation on O4-positive pre-oligodendrocytes induces process
CC       retraction via a Rho kinase/collapsin response-mediated protein
CC       signaling pathway. The S1P-induced survival of mature
CC       oligodendrocytes is mediated through a pertussis toxin-sensitive,
CC       Akt-dependent pathway. S1P activation on oligodendroglial cells
CC       modulates two distinct functional pathways mediating either
CC       process retraction or cell survival. These effects depend on the
CC       developmental stage of the cell.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in spleen and brain. In the CNS
CC       expression is restricted to oligodendrocytes.
CC   -!- DEVELOPMENTAL STAGE: Expressed in 7-day and 17-day embryos, but
CC       not in 11-day and 15-day embryos, implying its role in mammalian
CC       development. In oligodendrocytes, expressed throughout development
CC       from the immature stages to the mature myelin-froming cell.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC012232; AAH12232.1; -; mRNA.
DR   EMBL; AF327535; AAK15485.1; -; mRNA.
DR   EMBL; AK081126; BAC38142.1; -; mRNA.
DR   IPI; IPI00128430; -.
DR   RefSeq; NP_444420.1; NM_053190.2.
DR   UniGene; Mm.190619; -.
DR   ProteinModelPortal; Q91X56; -.
DR   SMR; Q91X56; 120-150.
DR   STRING; Q91X56; -.
DR   PRIDE; Q91X56; -.
DR   Ensembl; ENSMUST00000062813; ENSMUSP00000054469; ENSMUSG00000045087.
DR   Ensembl; ENSMUST00000122088; ENSMUSP00000113843; ENSMUSG00000045087.
DR   GeneID; 94226; -.
DR   KEGG; mmu:94226; -.
DR   UCSC; uc009oks.1; mouse.
DR   CTD; 94226; -.
DR   MGI; MGI:2150641; S1pr5.
DR   eggNOG; maNOG18914; -.
DR   GeneTree; ENSGT00590000082727; -.
DR   HOGENOM; HBG714382; -.
DR   HOVERGEN; HBG103071; -.
DR   InParanoid; Q91X56; -.
DR   OMA; PIIYTFT; -.
DR   OrthoDB; EOG4PNXHD; -.
DR   PhylomeDB; Q91X56; -.
DR   NextBio; 352227; -.
DR   ArrayExpress; Q91X56; -.
DR   Bgee; Q91X56; -.
DR   Genevestigator; Q91X56; -.
DR   GermOnline; ENSMUSG00000045087; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; TAS:MGI.
DR   GO; GO:0001619; F:lysosphingolipid and lysophosphatidic acid receptor activity; IEA:InterPro.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR005386; EDG8_S1P_rcpt.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR004061; S1P_rcpt.
DR   PANTHER; PTHR22750:SF15; EDG8_S1P_rcpt; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01561; EDG8RECEPTOR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01523; S1PRECEPTOR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW   Membrane; Palmitate; Receptor; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    400       Sphingosine 1-phosphate receptor 5.
FT                                /FTId=PRO_0000069437.
FT   TOPO_DOM      1     41       Extracellular (By similarity).
FT   TRANSMEM     42     62       Helical; Name=1; (By similarity).
FT   TOPO_DOM     63     68       Cytoplasmic (By similarity).
FT   TRANSMEM     69     89       Helical; Name=2; (By similarity).
FT   TOPO_DOM     90    111       Extracellular (By similarity).
FT   TRANSMEM    112    132       Helical; Name=3; (By similarity).
FT   TOPO_DOM    133    151       Cytoplasmic (By similarity).
FT   TRANSMEM    152    172       Helical; Name=4; (By similarity).
FT   TOPO_DOM    173    192       Extracellular (By similarity).
FT   TRANSMEM    193    213       Helical; Name=5; (By similarity).
FT   TOPO_DOM    214    253       Cytoplasmic (By similarity).
FT   TRANSMEM    254    274       Helical; Name=6; (By similarity).
FT   TOPO_DOM    275    288       Extracellular (By similarity).
FT   TRANSMEM    289    309       Helical; Name=7; (By similarity).
FT   TOPO_DOM    310    400       Cytoplasmic (By similarity).
FT   LIPID       324    324       S-palmitoyl cysteine (By similarity).
FT   CARBOHYD     20     20       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   400 AA;  42331 MW;  A4311B8E8515F3F4 CRC64;
     MEPGLLRPAP VSEVIVLHYN YTGKLRGARY QPGAGLRADA AVCLAVCAFI VLENLAVLLV
     LVRHPRFHAP MFLLLGSLTL SDLLAGAAYA TNILLSGPLT LRLSPALWFA REGGVFVALA
     ASVLSLLAIA LERHLTMARR GPAPAASRAR TLAMAVAAWG ASLLLGLLPA LGWNCLGRLE
     TCSTVLPLYA KAYVLFCVLA FLGILAAICA LYARIYCQVR ANARRLRAGP GSRRATSSSR
     SRHTPRSLAL LRTLSVVLLA FVACWGPLFL LLLLDVACPA RACPVLLQAD PFLGLAMANS
     LLNPIIYTFT NRDLRHALLR LLCCGRGPCN QDSSNSLQRS PSAAGPSGGG LRRCLPPTLD
     RSSSPSEHLS PQQDGVDTSC STGSPGVATA NRSLVPTATD
//
ID   ZFN2B_MOUSE             Reviewed;         257 AA.
AC   Q91X58; Q9D0W4;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=AN1-type zinc finger protein 2B;
DE   AltName: Full=Arsenite-inducible RNA-associated protein-like protein;
DE            Short=AIRAP-like protein;
GN   Name=Zfand2b; Synonyms=Airapl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-187, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   ASSOCIATION WITH PROTEASOMES, AND MUTAGENESIS OF CYS-254.
RX   PubMed=18467495; DOI=10.1073/pnas.0707025105;
RA   Yun C., Stanhill A., Yang Y., Zhang Y., Haynes C.M., Xu C.F.,
RA   Neubert T.A., Mor A., Philips M.R., Ron D.;
RT   "Proteasomal adaptation to environmental stress links resistance to
RT   proteotoxicity with longevity in Caenorhabditis elegans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:7094-7099(2008).
CC   -!- SUBUNIT: upon exposure to arsenite, associates with proteasomes.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum.
CC   -!- SIMILARITY: Contains 2 AN1-type zinc fingers.
CC   -!- SIMILARITY: Contains 2 UIM (ubiquitin-interacting motif) repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK004332; BAB23266.1; -; mRNA.
DR   EMBL; AK151430; BAE30394.1; -; mRNA.
DR   EMBL; BC011495; AAH11495.1; -; mRNA.
DR   IPI; IPI00133226; -.
DR   RefSeq; NP_001153377.1; NM_001159905.1.
DR   RefSeq; NP_001153378.1; NM_001159906.1.
DR   RefSeq; NP_081122.2; NM_026846.3.
DR   UniGene; Mm.32646; -.
DR   ProteinModelPortal; Q91X58; -.
DR   SMR; Q91X58; 1-53, 93-142.
DR   DIP; DIP-46091N; -.
DR   PhosphoSite; Q91X58; -.
DR   PRIDE; Q91X58; -.
DR   Ensembl; ENSMUST00000027394; ENSMUSP00000027394; ENSMUSG00000026197.
DR   GeneID; 68818; -.
DR   KEGG; mmu:68818; -.
DR   UCSC; uc007bnw.1; mouse.
DR   CTD; 68818; -.
DR   MGI; MGI:1916068; Zfand2b.
DR   eggNOG; roNOG09258; -.
DR   GeneTree; ENSGT00530000063249; -.
DR   HOGENOM; HBG715294; -.
DR   HOVERGEN; HBG061194; -.
DR   InParanoid; Q91X58; -.
DR   OMA; MMKLTCD; -.
DR   OrthoDB; EOG45B1GT; -.
DR   PhylomeDB; Q91X58; -.
DR   NextBio; 328001; -.
DR   ArrayExpress; Q91X58; -.
DR   Bgee; Q91X58; -.
DR   CleanEx; MM_ZFAND2B; -.
DR   Genevestigator; Q91X58; -.
DR   GermOnline; ENSMUSG00000026197; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR003903; Ubiquitin-int_motif.
DR   InterPro; IPR000058; Znf_AN1.
DR   Gene3D; G3DSA:4.10.1110.10; Znf_AN1; 2.
DR   Pfam; PF01428; zf-AN1; 2.
DR   SMART; SM00726; UIM; 2.
DR   SMART; SM00154; ZnF_AN1; 2.
DR   PROSITE; PS50330; UIM; 1.
DR   PROSITE; PS51039; ZF_AN1; 2.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Metal-binding; Phosphoprotein; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    257       AN1-type zinc finger protein 2B.
FT                                /FTId=PRO_0000232877.
FT   REPEAT      197    216       UIM 1.
FT   REPEAT      221    240       UIM 2.
FT   ZN_FING       7     52       AN1-type 1.
FT   ZN_FING      97    145       AN1-type 2.
FT   COMPBIAS    170    175       Poly-Ser.
FT   MOD_RES     187    187       Phosphoserine.
FT   MUTAGEN     254    254       C->S: Loss of localization to the
FT                                endoplasmic reticulum.
FT   CONFLICT    174    174       P -> S (in Ref. 1; BAB23266).
SQ   SEQUENCE   257 AA;  27895 MW;  D9B35C96BB3876E2 CRC64;
     MEFPDLGAHC SEPSCQRLDF LPLKCDACSG IFCADHVAYA QHHCGSAYQK DIQVPVCPLC
     NVPVPVARGE PPDRAVGEHI DRDCRSDPAQ QKRKIFTNKC ERSGCRQREM MKLTCDRCGR
     NFCIKHRHPL DHECSGEGHQ TSRAGLAAIS RAQGLASTST APSPSRTLPS SSSPSRATPQ
     LPTRTASPVI ALQNGLSEDE ALQRALELSL AEAKPQVLSS QEEDDLALAQ ALSASEAEYQ
     QQQAQSRSLK PSNCSLC
//
ID   NCALD_MOUSE             Reviewed;         193 AA.
AC   Q91X97; Q3TJS9; Q8BZN9;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Neurocalcin-delta;
GN   Name=Ncald; Synonyms=D15Ertd412e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon, Head, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 51-63, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
CC   -!- FUNCTION: May be involved in the calcium-dependent regulation of
CC       rhodopsin phosphorylation. Binds three calcium ions (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the recoverin family.
CC   -!- SIMILARITY: Contains 4 EF-hand domains.
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DR   EMBL; AK034031; BAC28553.1; -; mRNA.
DR   EMBL; AK048440; BAC33338.1; -; mRNA.
DR   EMBL; AK167313; BAE39416.1; -; mRNA.
DR   EMBL; BC011162; AAH11162.1; -; mRNA.
DR   EMBL; BC026979; AAH26979.1; -; mRNA.
DR   IPI; IPI00263638; -.
DR   RefSeq; NP_001164337.1; NM_001170866.1.
DR   RefSeq; NP_001164338.1; NM_001170867.1.
DR   RefSeq; NP_001164339.1; NM_001170868.1.
DR   RefSeq; NP_598855.2; NM_134094.4.
DR   UniGene; Mm.283370; -.
DR   ProteinModelPortal; Q91X97; -.
DR   SMR; Q91X97; 5-185.
DR   PRIDE; Q91X97; -.
DR   Ensembl; ENSMUST00000090150; ENSMUSP00000087611; ENSMUSG00000051359.
DR   Ensembl; ENSMUST00000116445; ENSMUSP00000112146; ENSMUSG00000051359.
DR   Ensembl; ENSMUST00000119730; ENSMUSP00000113858; ENSMUSG00000051359.
DR   Ensembl; ENSMUST00000120746; ENSMUSP00000112898; ENSMUSG00000051359.
DR   GeneID; 52589; -.
DR   KEGG; mmu:52589; -.
DR   UCSC; uc007vng.1; mouse.
DR   CTD; 52589; -.
DR   MGI; MGI:1196326; Ncald.
DR   eggNOG; maNOG15514; -.
DR   GeneTree; ENSGT00560000076803; -.
DR   HOGENOM; HBG746798; -.
DR   HOVERGEN; HBG108179; -.
DR   InParanoid; Q91X97; -.
DR   OMA; RDCPSGN; -.
DR   OrthoDB; EOG4MKNH8; -.
DR   PhylomeDB; Q91X97; -.
DR   NextBio; 309183; -.
DR   ArrayExpress; Q91X97; -.
DR   Bgee; Q91X97; -.
DR   CleanEx; MM_NCALD; -.
DR   Genevestigator; Q91X97; -.
DR   GermOnline; ENSMUSG00000051359; Mus musculus.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   InterPro; IPR018248; EF-hand.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR001125; Recoverin.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF00036; efhand; 3.
DR   PRINTS; PR00450; RECOVERIN.
DR   SMART; SM00054; EFh; 3.
DR   PROSITE; PS00018; EF_HAND_1; 3.
DR   PROSITE; PS50222; EF_HAND_2; 4.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Lipoprotein; Myristate; Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    193       Neurocalcin-delta.
FT                                /FTId=PRO_0000073783.
FT   DOMAIN       23     58       EF-hand 1.
FT   DOMAIN       60     95       EF-hand 2.
FT   DOMAIN       96    131       EF-hand 3.
FT   DOMAIN      144    179       EF-hand 4.
FT   CA_BIND      73     84       1 (Potential).
FT   CA_BIND     109    120       2 (Potential).
FT   CA_BIND     157    168       3 (Potential).
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
FT   CONFLICT    151    151       K -> N (in Ref. 2; AAH11162).
FT   CONFLICT    186    186       D -> N (in Ref. 1; BAC28553).
SQ   SEQUENCE   193 AA;  22245 MW;  20DD8B6FF47C4CBF CRC64;
     MGKQNSKLRP EVMQDLLEST DFTEHEIQEW YKGFLRDCPS GHLSMEEFKK IYGNFFPYGD
     ASKFAEHVFR TFDANGDGTI DFREFIIALS VTSRGKLEQK LKWAFSMYDL DGNGYISKAE
     MLEIVQAIYK MVSSVMKMPE DESTPEKRTE KIFRQMDTNR DGKLSLEEFI RGAKSDPSIV
     RLLQCDPSSA GQF
//
ID   PEX16_MOUSE             Reviewed;         336 AA.
AC   Q91XC9; Q3UPY2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 2.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Peroxisomal membrane protein PEX16;
DE   AltName: Full=Peroxin-16;
DE   AltName: Full=Peroxisomal biogenesis factor 16;
GN   Name=Pex16;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Required for peroxisome membrane biogenesis. May play a
CC       role in early stages of peroxisome assembly. Can recruit other
CC       peroxisomal proteins, such as PEX3 and PMP34, to de novo
CC       peroxisomes derived from the endoplasmic reticulum (ER). May
CC       function as receptor for PEX3 (By similarity).
CC   -!- SUBUNIT: Interacts with PEX19 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane; Multi-pass membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Belongs to the peroxin-16 family.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK143073; BAE25262.1; -; mRNA.
DR   EMBL; AL731709; CAM20621.1; -; Genomic_DNA.
DR   EMBL; CH466519; EDL27597.1; -; Genomic_DNA.
DR   EMBL; BC010822; AAH10822.1; -; mRNA.
DR   IPI; IPI00128976; -.
DR   RefSeq; NP_660104.2; NM_145122.2.
DR   UniGene; Mm.202782; -.
DR   ProteinModelPortal; Q91XC9; -.
DR   STRING; Q91XC9; -.
DR   PRIDE; Q91XC9; -.
DR   Ensembl; ENSMUST00000028650; ENSMUSP00000028650; ENSMUSG00000027222.
DR   GeneID; 18633; -.
DR   KEGG; mmu:18633; -.
DR   CTD; 18633; -.
DR   MGI; MGI:1338829; Pex16.
DR   GeneTree; ENSGT00390000017790; -.
DR   HOGENOM; HBG715630; -.
DR   HOVERGEN; HBG053572; -.
DR   InParanoid; Q91XC9; -.
DR   OMA; IAESLYI; -.
DR   OrthoDB; EOG4KPTBN; -.
DR   PhylomeDB; Q91XC9; -.
DR   NextBio; 294600; -.
DR   ArrayExpress; Q91XC9; -.
DR   Bgee; Q91XC9; -.
DR   Genevestigator; Q91XC9; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005778; C:peroxisomal membrane; IDA:HGNC.
DR   GO; GO:0007031; P:peroxisome organization; IEA:UniProtKB-KW.
DR   InterPro; IPR013919; Pex16.
DR   Pfam; PF08610; Pex16; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Peroxisome; Peroxisome biogenesis; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    336       Peroxisomal membrane protein PEX16.
FT                                /FTId=PRO_0000366961.
FT   TOPO_DOM      1     84       Cytoplasmic (Potential).
FT   TRANSMEM     85    105       Helical; (Potential).
FT   TOPO_DOM    106    110       Peroxisomal (Potential).
FT   TRANSMEM    111    131       Helical; (Potential).
FT   TOPO_DOM    132    336       Cytoplasmic (Potential).
FT   REGION       66     81       Required for peroxisomal location (By
FT                                similarity).
FT   REGION      221    336       Interaction with PEX19 (By similarity).
FT   CONFLICT    268    268       R -> Q (in Ref. 4; AAH10822).
SQ   SEQUENCE   336 AA;  38677 MW;  C7507C8B482EC8F3 CRC64;
     MEKLRLLSLR YQEYVTRHPA ATAQLETAVR GLSYLLAGRF SDSHELSELV YSASNLLVLL
     NDGILRKELR KKLPVSLSQQ KLLTWLSVLE CVEVFMEMGA AKVWGEVGRW LVIALIQLAK
     AVLRMLLLIW FKAGIQTSPP IVPLDRETQA QPLDGDHNPG SQEPSYVGKR SHRVVRTLQN
     SPSLHSRYWG APQQREIRQK QQQEELSTPP TPLGLQETIA ESLYIARPLL HLLSLGLWGQ
     RSWTPWLLSG VVDMTSLSLL SDRKNLTRRE RLELRRRTIL LLYYLLRSPF YDRFSEAKIL
     FLLQLLTDHI PGVGLVARPL MDYLPSWQKI YFYSWG
//
ID   PNPO_MOUSE              Reviewed;         261 AA.
AC   Q91XF0; Q3TP70; Q3U445; Q3U4X1;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Pyridoxine-5'-phosphate oxidase;
DE            EC=1.4.3.5;
DE   AltName: Full=Pyridoxamine-phosphate oxidase;
GN   Name=Pnpo;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Stomach, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney, and Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 120-138, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-241, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Catalyzes the oxidation of either pyridoxine 5'-
CC       phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal
CC       5'-phosphate (PLP) (By similarity).
CC   -!- CATALYTIC ACTIVITY: Pyridoxamine 5'-phosphate + H(2)O + O(2) =
CC       pyridoxal 5'-phosphate + NH(3) + H(2)O(2).
CC   -!- CATALYTIC ACTIVITY: Pyridoxine 5'-phosphate + O(2) = pyridoxal 5'-
CC       phosphate + H(2)O(2).
CC   -!- COFACTOR: Binds 1 FMN per subunit.
CC   -!- PATHWAY: Cofactor biosynthesis; B6 vitamer interconversion;
CC       pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1.
CC   -!- PATHWAY: Cofactor biosynthesis; B6 vitamer interconversion;
CC       pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the pyridoxamine 5'-phosphate oxidase
CC       family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE32590.1; Type=Erroneous initiation;
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DR   EMBL; AK154004; BAE32309.1; -; mRNA.
DR   EMBL; AK154443; BAE32590.1; ALT_INIT; mRNA.
DR   EMBL; AK164667; BAE37867.1; -; mRNA.
DR   EMBL; AL596384; CAM21902.1; -; Genomic_DNA.
DR   EMBL; BC010785; AAH10785.1; -; mRNA.
DR   EMBL; BC026564; AAH26564.1; -; mRNA.
DR   IPI; IPI00129096; -.
DR   RefSeq; NP_598782.1; NM_134021.2.
DR   UniGene; Mm.254704; -.
DR   ProteinModelPortal; Q91XF0; -.
DR   SMR; Q91XF0; 49-261.
DR   STRING; Q91XF0; -.
DR   PhosphoSite; Q91XF0; -.
DR   PRIDE; Q91XF0; -.
DR   Ensembl; ENSMUST00000018803; ENSMUSP00000018803; ENSMUSG00000018659.
DR   GeneID; 103711; -.
DR   KEGG; mmu:103711; -.
DR   NMPDR; fig|10090.3.peg.25142; -.
DR   UCSC; uc007ldc.1; mouse.
DR   CTD; 103711; -.
DR   MGI; MGI:2144151; Pnpo.
DR   eggNOG; roNOG14899; -.
DR   GeneTree; ENSGT00390000011219; -.
DR   HOGENOM; HBG327559; -.
DR   HOVERGEN; HBG045634; -.
DR   InParanoid; Q91XF0; -.
DR   OMA; FTFFTNY; -.
DR   OrthoDB; EOG4CVG7G; -.
DR   PhylomeDB; Q91XF0; -.
DR   BRENDA; 1.4.3.5; 244.
DR   NextBio; 356069; -.
DR   ArrayExpress; Q91XF0; -.
DR   Bgee; Q91XF0; -.
DR   CleanEx; MM_PNPO; -.
DR   Genevestigator; Q91XF0; -.
DR   GermOnline; ENSMUSG00000018659; Mus musculus.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000659; Pyridoxamine_oxidase.
DR   InterPro; IPR019740; Pyridoxamine_oxidase_CS.
DR   InterPro; IPR019576; Pyridoxamine_oxidase_dimer_C.
DR   InterPro; IPR011576; PyridoxamineP_oxidase_FMN-bd.
DR   InterPro; IPR012349; Split_barrel_FMN-bd.
DR   InterPro; IPR009002; Split_barrel_FMN-bd-related.
DR   Gene3D; G3DSA:2.30.110.10; PNPOx_FMN_bd; 1.
DR   PANTHER; PTHR10851; Pyridox_oxidase; 1.
DR   Pfam; PF10590; PNPOx_C; 1.
DR   Pfam; PF01243; Pyridox_oxidase; 1.
DR   PIRSF; PIRSF000190; Pyd_amn-ph_oxd; 1.
DR   SUPFAM; SSF50475; FMN_binding; 1.
DR   TIGRFAMs; TIGR00558; pdxH; 1.
DR   PROSITE; PS01064; PYRIDOX_OXIDASE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Flavoprotein; FMN; Oxidoreductase;
KW   Phosphoprotein; Pyridoxal phosphate; Pyridoxine biosynthesis.
FT   CHAIN         1    261       Pyridoxine-5'-phosphate oxidase.
FT                                /FTId=PRO_0000167784.
FT   NP_BIND     110    111       FMN (By similarity).
FT   NP_BIND     174    175       FMN (By similarity).
FT   REGION      225    227       Substrate binding (By similarity).
FT   BINDING      95     95       FMN (By similarity).
FT   BINDING      98     98       FMN; via amide nitrogen (By similarity).
FT   BINDING     100    100       Substrate (By similarity).
FT   BINDING     117    117       FMN (By similarity).
FT   BINDING     157    157       Substrate (By similarity).
FT   BINDING     161    161       Substrate (By similarity).
FT   BINDING     165    165       Substrate (By similarity).
FT   MOD_RES      40     40       Phosphoserine (By similarity).
FT   MOD_RES     165    165       Phosphoserine.
FT   MOD_RES     241    241       Phosphoserine.
SQ   SEQUENCE   261 AA;  30114 MW;  D83A54883B4BC0EC CRC64;
     MTCGLLSVTV TFRRPAKWTG YLRHLCCRGA VMDLGPMRKS YRGDREAFEE THLTSLDPMK
     QFASWFDEAV QCPDIGEANA MCVATCTRDG KPSARMLLLK GFGKDGFRFF TNYESRKGKE
     LDSNPFASLV FYWEPLNRQV RVEGPVKKLP EKEAENYFHS RPKSSQIGAV VSRQSSVIPD
     REYLRKKNEE LGQLYQDQEV PKPEYWGGYI LYPQVMEFWQ GQTNRLHDRI VFRRGLATGD
     SPLGPMTHHG EEDWVYERLA P
//
ID   Q91XH6_MOUSE            Unreviewed;       232 AA.
AC   Q91XH6;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   SubName: Full=Vesicle transport through interaction with t-SNAREs 1B homolog;
DE   SubName: Full=Vesicle transport through interaction with t-SNAREs 1B homolog, isoform CRA_c;
GN   Name=Vti1b; ORFNames=mCG_5809;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor. C3;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC009810; AAH09810.1; -; mRNA.
DR   EMBL; BC080204; AAH80204.1; -; mRNA.
DR   EMBL; CH466590; EDL02641.1; -; Genomic_DNA.
DR   IPI; IPI00331284; -.
DR   RefSeq; NP_058080.2; NM_016800.3.
DR   UniGene; Mm.265929; -.
DR   ProteinModelPortal; Q91XH6; -.
DR   SMR; Q91XH6; 1-96, 139-197.
DR   STRING; Q91XH6; -.
DR   PRIDE; Q91XH6; -.
DR   Ensembl; ENSMUST00000055262; ENSMUSP00000057462; ENSMUSG00000021124.
DR   GeneID; 53612; -.
DR   KEGG; mmu:53612; -.
DR   UCSC; uc007nzx.1; mouse.
DR   CTD; 53612; -.
DR   MGI; MGI:1855688; Vti1b.
DR   HOVERGEN; HBG058837; -.
DR   InParanoid; Q91XH6; -.
DR   OMA; DMKYGTY; -.
DR   PhylomeDB; Q91XH6; -.
DR   NextBio; 310327; -.
DR   ArrayExpress; Q91XH6; -.
DR   Bgee; Q91XH6; -.
DR   Genevestigator; Q91XH6; -.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR010989; t-SNARE.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   InterPro; IPR007705; Vesicle_trsprt_v-SNARE_N.
DR   Pfam; PF05008; V-SNARE; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF47661; t-snare; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   232 AA;  26728 MW;  6F55A9AF93530273 CRC64;
     MAASAASSEH FEKLHEIFRG LLEDLQGVPE RLLGTAGTEE KKKLVRDFDE KQQEANETLA
     EMEEELRYAP LTFRNPMMSK LRNYRKDLAK LHREVRSTPL TAAPGGRGDL KYGTYTLENE
     HLNRLQSQRA LLLQGTESLN RATQSIERSH RIATETDQIG TEIIEELGEQ RDQLERTKSR
     LVNTNENLSK SRKILRSMSR KVITNKLLLS VIILLELAIL VGLVYYKFFR HH
//
ID   DLG2_MOUSE              Reviewed;         852 AA.
AC   Q91XM9; Q8BXK7; Q8BYG5;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Disks large homolog 2;
DE   AltName: Full=Channel-associated protein of synapse-110;
DE            Short=Chapsyn-110;
DE   AltName: Full=Postsynaptic density protein PSD-93;
GN   Name=Dlg2; Synonyms=Dlgh2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Cerebellum;
RA   Yamashita T., Mochizuki C., Miyagi Y., Sonoda T., Kawamoto S.;
RT   "Cloning and sequencing of mouse PSD-93 cDNA.";
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 465-852 (ISOFORM 8).
RC   STRAIN=C57BL/6J; TISSUE=Adrenal gland, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=12890763;
RA   Tao Y.-X., Rumbaugh G., Wang G.-D., Petralia R.S., Zhao C.,
RA   Kauer F.W., Tao F., Zhuo M., Wenthold R.J., Raja S.N., Huganir R.L.,
RA   Bredt D.S., Johns R.A.;
RT   "Impaired NMDA receptor-mediated postsynaptic function and blunted
RT   NMDA receptor-dependent persistent pain in mice lacking postsynaptic
RT   density-93 protein.";
RL   J. Neurosci. 23:6703-6712(2003).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=15304517; DOI=10.1074/jbc.M407575200;
RA   Leyland M.L., Dart C.;
RT   "An alternatively spliced isoform of PSD-93/chapsyn 110 binds to the
RT   inwardly rectifying potassium channel, Kir2.1.";
RL   J. Biol. Chem. 279:43427-43436(2004).
RN   [5]
RP   ALTERNATIVE SPLICING.
RX   PubMed=14724236; DOI=10.1523/JNEUROSCI.3865-03.2004;
RA   Parker M.J., Zhao S., Bredt D.S., Sanes J.R., Feng G.;
RT   "PSD93 regulates synaptic stability at neuronal cholinergic
RT   synapses.";
RL   J. Neurosci. 24:378-388(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-414, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-175; SER-365 AND
RP   SER-414, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-58; SER-62; TYR-340;
RP   TYR-348; TYR-500; TYR-505; TYR-732 AND TYR-737, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-414, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [10]
RP   INTERACTION WITH NETO1.
RX   PubMed=19243221; DOI=10.1371/journal.pbio.1000041;
RA   Ng D., Pitcher G.M., Szilard R.K., Sertie A., Kanisek M.,
RA   Clapcote S.J., Lipina T., Kalia L.V., Joo D., McKerlie C., Cortez M.,
RA   Roder J.C., Salter M.W., McInnes R.R.;
RT   "Neto1 is a novel CUB-domain NMDA receptor-interacting protein
RT   required for synaptic plasticity and learning.";
RL   PLoS Biol. 7:E41-E41(2009).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 95-188.
RX   PubMed=20054121; DOI=10.1107/S1744309109043267;
RA   Fiorentini M., Nielsen A.K., Kristensen O., Kastrup J.S., Gajhede M.;
RT   "Structure of the first PDZ domain of human PSD-93.";
RL   Acta Crystallogr. F 65:1254-1257(2009).
CC   -!- FUNCTION: Required for perception of chronic pain through NMDA
CC       receptor signaling. Regulates surface expression of NMDA receptors
CC       in dorsal horn neurons of the spinal cord. Interacts with the
CC       cytoplasmic tail of NMDA receptor subunits as well as inward
CC       rectifying potassium channels. Involved in regulation of synaptic
CC       stability at cholinergic synapses. Part of the postsynaptic
CC       protein scaffold of excitatory synapses.
CC   -!- SUBUNIT: Interacts with NOS1/nNOS through second PDZ domain.
CC       Interacts with KCNJ2/Kir2.1 (via C-terminus) through one of its
CC       PDZ domains (By similarity). Interacts with FRMPD4 (via C-
CC       terminus) (By similarity). Interacts through its PDZ domains with
CC       Neto1. Interacts with LRFN1, LRFN2 and LRFN4. Interacts with FASLG
CC       (By similarity).
CC   -!- INTERACTION:
CC       Q62108:Dlg4; NbExp=1; IntAct=EBI-400138, EBI-300895;
CC   -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor (By similarity). Cell
CC       junction, synapse, postsynaptic cell membrane, postsynaptic
CC       density (By similarity). Cell junction, synapse (By similarity).
CC       Note=Concentrated in soma and postsynaptic density of a subset of
CC       neurons (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC       Name=1; Synonyms=PSD93-alpha;
CC         IsoId=Q91XM9-1; Sequence=Displayed;
CC       Name=2; Synonyms=PSD93-beta;
CC         IsoId=Q91XM9-2; Sequence=VSP_015520;
CC       Name=3; Synonyms=PSD93-gamma;
CC         IsoId=Q91XM9-3; Sequence=VSP_015517, VSP_015522;
CC       Name=4; Synonyms=PSD93-delta;
CC         IsoId=Q91XM9-4; Sequence=VSP_012869;
CC       Name=5;
CC         IsoId=Q91XM9-5; Sequence=VSP_012869, VSP_012870, VSP_012871;
CC         Note=No experimental confirmation available;
CC       Name=6; Synonyms=PSD93 epsilon;
CC         IsoId=Q91XM9-6; Sequence=VSP_015518, VSP_015521;
CC       Name=7; Synonyms=PSD93 zeta;
CC         IsoId=Q91XM9-7; Sequence=VSP_015519, VSP_015523;
CC       Name=8;
CC         IsoId=Q91XM9-8; Sequence=VSP_015524;
CC         Note=Incomplete sequence;
CC   -!- TISSUE SPECIFICITY: Brain. Highest levels of isoform 1 in cortex,
CC       olfactory bulb, thalamus, hypothalamus, striatum and hippocampus.
CC       Highest level of isoform 2 in olfactory bulb. Reduced levels in
CC       cortex and hippocampus. Highest level of isoform 4 in spinal cord.
CC       Low levels of isoform 4, isoform 6, and isoform 7 in superior
CC       cervical ganglion.
CC   -!- DOMAIN: Isoform 7 has an L27 domain close to N-terminus.
CC   -!- PTM: Palmitoylation of isoform 1 and isoform 2 is not required for
CC       targeting to postsynaptic density (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice do not respond to persistent pain.
CC       Postsynaptic surface expression of NMDA receptors and NMDA
CC       receptor-mediated synaptic function are reduced in dorsal horn
CC       neurons of the spinal chord.
CC   -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC   -!- SIMILARITY: Contains 3 PDZ (DHR) domains.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; AF388675; AAK64496.1; -; mRNA.
DR   EMBL; AK046525; BAC32772.1; -; mRNA.
DR   EMBL; AK039754; BAC30440.1; -; mRNA.
DR   IPI; IPI00129282; -.
DR   IPI; IPI00226727; -.
DR   IPI; IPI00466988; -.
DR   IPI; IPI00648194; -.
DR   IPI; IPI00648424; -.
DR   IPI; IPI00649556; -.
DR   IPI; IPI00649737; -.
DR   IPI; IPI00649990; -.
DR   UniGene; Mm.257035; -.
DR   PDB; 2WL7; X-ray; 2.03 A; A=95-188.
DR   PDBsum; 2WL7; -.
DR   ProteinModelPortal; Q91XM9; -.
DR   SMR; Q91XM9; 93-514, 539-852.
DR   DIP; DIP-31569N; -.
DR   IntAct; Q91XM9; 14.
DR   MINT; MINT-136378; -.
DR   STRING; Q91XM9; -.
DR   PhosphoSite; Q91XM9; -.
DR   PRIDE; Q91XM9; -.
DR   Ensembl; ENSMUST00000107196; ENSMUSP00000102814; ENSMUSG00000052572.
DR   UCSC; uc009ihr.1; mouse.
DR   UCSC; uc009ihs.1; mouse.
DR   MGI; MGI:1344351; Dlg2.
DR   GeneTree; ENSGT00560000076879; -.
DR   HOVERGEN; HBG107814; -.
DR   OrthoDB; EOG447FSN; -.
DR   ArrayExpress; Q91XM9; -.
DR   Bgee; Q91XM9; -.
DR   CleanEx; MM_DLG2; -.
DR   Genevestigator; Q91XM9; -.
DR   GermOnline; ENSMUSG00000052572; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0044224; C:juxtaparanode region of axon; IDA:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR   GO; GO:0007268; P:synaptic transmission; IMP:MGI.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR016313; M-assoc_guanylate_kinase.
DR   InterPro; IPR019590; MAGUK_PEST_N.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR019583; PDZ_assoc.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF10608; MAGUK_N_PEST; 1.
DR   Pfam; PF00595; PDZ; 3.
DR   Pfam; PF10600; PDZ_assoc; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   PIRSF; PIRSF001741; MAGUK_DLGH; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 3.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50156; PDZ; 3.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 3.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW   Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Postsynaptic cell membrane; Repeat; SH3 domain; Synapse.
FT   CHAIN         1    852       Disks large homolog 2.
FT                                /FTId=PRO_0000094554.
FT   DOMAIN       98    185       PDZ 1.
FT   DOMAIN      193    280       PDZ 2.
FT   DOMAIN      421    502       PDZ 3.
FT   DOMAIN      536    606       SH3.
FT   DOMAIN      662    837       Guanylate kinase-like.
FT   MOD_RES      28     28       Phosphoserine.
FT   MOD_RES      58     58       Phosphotyrosine.
FT   MOD_RES      62     62       Phosphoserine.
FT   MOD_RES     175    175       Phosphoserine.
FT   MOD_RES     340    340       Phosphotyrosine.
FT   MOD_RES     348    348       Phosphotyrosine.
FT   MOD_RES     365    365       Phosphoserine.
FT   MOD_RES     406    406       Phosphoserine.
FT   MOD_RES     414    414       Phosphoserine.
FT   MOD_RES     500    500       Phosphotyrosine.
FT   MOD_RES     505    505       Phosphotyrosine.
FT   MOD_RES     732    732       Phosphotyrosine.
FT   MOD_RES     737    737       Phosphotyrosine.
FT   LIPID         5      5       S-palmitoyl cysteine (By similarity).
FT   LIPID         7      7       S-palmitoyl cysteine (By similarity).
FT   VAR_SEQ       1     68       MFFACYCALRTNVKKYRYQDEDGPHDHSLPRLTHEVRGPEL
FT                                VHVSEKNLSQIENVHGYVLQSHISPLK -> MNAYLTKQHS
FT                                CSRGSDGMDIGRSAPTLIRDAHCACGWQRNAQGLGYSSQTM
FT                                PSSGPGGPASNRTKLVTLWDSVRKSPHKTSTKGKGNCGERC
FT                                ACPHGWFSPAQ (in isoform 4 and isoform 5).
FT                                /FTId=VSP_012869.
FT   VAR_SEQ       1     61       Missing (in isoform 3).
FT                                /FTId=VSP_015517.
FT   VAR_SEQ       1     42       Missing (in isoform 6).
FT                                /FTId=VSP_015518.
FT   VAR_SEQ       1     14       MFFACYCALRTNVK -> MPVKKKDTDRALSLLEEYCKKLR
FT                                KPEEQLLKNAVKKVMSIFKSSLFQALLDIQEFYEVTLLNSQ
FT                                KSCEQKIEEANHVAQKWEKTLLLDSCRDSLQKSSEHASCSG
FT                                PKENALYIEQNKENQCSENETEEKTCQNQGKCPAQNCSVEA
FT                                PTWMPVHHCT (in isoform 7).
FT                                /FTId=VSP_015519.
FT   VAR_SEQ       1     13       MFFACYCALRTNV -> MICHCKVACTNNTLSLMFGC (in
FT                                isoform 2).
FT                                /FTId=VSP_015520.
FT   VAR_SEQ      43     67       HVSEKNLSQIENVHGYVLQSHISPL -> MFASIWYAKKLG
FT                                RRFVHNARKAKSE (in isoform 6).
FT                                /FTId=VSP_015521.
FT   VAR_SEQ      62     68       SHISPLK -> MQHAFIP (in isoform 3).
FT                                /FTId=VSP_015522.
FT   VAR_SEQ      69     86       Missing (in isoform 7).
FT                                /FTId=VSP_015523.
FT   VAR_SEQ     394    394       S -> RYCMRFLTSSSPVACVSTRMDGWNSSPPTSLALSTF
FT                                LVERCSASMVRWEKLRTWLFCSFCCAH (in isoform
FT                                5).
FT                                /FTId=VSP_012870.
FT   VAR_SEQ     395    852       Missing (in isoform 5).
FT                                /FTId=VSP_012871.
FT   VAR_SEQ     465    503       DQILSVNGIDLRGASHEQAAAALKGAGQTVTIIAQYQPE
FT                                -> VINASVNRTGDRRIWHQGNGKAASSVSCLLPALFPNFV
FT                                L (in isoform 8).
FT                                /FTId=VSP_015524.
FT   CONFLICT    107    107       G -> S (in Ref. 2; BAC32772).
FT   CONFLICT    123    123       G -> D (in Ref. 2; BAC32772).
FT   CONFLICT    213    213       D -> N (in Ref. 2; BAC32772).
FT   CONFLICT    301    301       T -> M (in Ref. 2; BAC32772).
FT   CONFLICT    323    323       P -> S (in Ref. 2; BAC32772).
FT   CONFLICT    585    585       I -> T (in Ref. 2; BAC30440).
FT   CONFLICT    776    776       T -> I (in Ref. 2; BAC30440).
FT   STRAND       95    102
FT   STRAND      111    113
FT   STRAND      128    131
FT   TURN        138    140
FT   STRAND      149    153
FT   HELIX       163    172
FT   STRAND      176    184
SQ   SEQUENCE   852 AA;  94803 MW;  82A2F6ECB2AB8E86 CRC64;
     MFFACYCALR TNVKKYRYQD EDGPHDHSLP RLTHEVRGPE LVHVSEKNLS QIENVHGYVL
     QSHISPLKAS PAPIIVNTDT LDTIPYVNGT EIEYEFEEIT LERGNSGLGF SIAGGTDNPH
     IGGDPGIFIT KIIPGGAAAE DGRLRVNDCI LRVNEVDVSE VSHSKAVEAL KEAGSIVRLY
     VRRRRPILET VVEIKLFKGP KGLGFSIAGG VGDQHIPGDN SIYVTKIIDG GAAQKDGRLQ
     VGDRLLMVNN YSLEEVTHEE AVAILKNTSD VVYLKVGKPT TIYMTDPYGP PDITHSYSPP
     TENHLLSGNN GTLEYKTSLP PIPPGRYSPI PKHMLGEDDY TRPPEPVYST VNKLCDKPAS
     PRHYSPVECD KSFLLSTPYP HYHLGLLPDS DMTSHSQHST ATRQPSVTLQ RAISLEGEPR
     KVVLHKGSTG LGFNIVGGED GEGIFVSFIL AGGPADLSGE LQRGDQILSV NGIDLRGASH
     EQAAAALKGA GQTVTIIAQY QPEDYARFEA KIHDLREQMM NHSMSSGSGS LRTNQKRSLY
     VRAMFDYDKS KDSGLPSQGL SFKYGDILHV INASDDEWWQ ARRVILDGDS EEMGVIPSKR
     RVERKERARL KTVKFNAKPG VIDSKGDIPG LGDDGYGTKT LRGQEDLILS YEPVTRQEIN
     YTRPVIILGP MKDRINDDLI SEFPDKFGSC VPHTTRPKRD YEVDGRDYHF VISREQMEKD
     IQEHKFIEAG QYNDNLYGTS VQSVRFVAER GKHCILDVSG NAIKRLQVAQ LYPIATFIKP
     KSLEPLMEMN KRLTEEQAKK TYDRAIKLEQ EFGEYFTAIV QGDTLEDIYN QCKLVIEEQS
     GPFIWIPSKE KL
//
ID   MTMR4_MOUSE             Reviewed;        1190 AA.
AC   Q91XS1; Q5ND06; Q5ND08;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Myotubularin-related protein 4;
DE            EC=3.1.3.48;
GN   Name=Mtmr4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Bone marrow;
RA   Gorski K.S., Shin T., Otuji M., Suyi T., Pardoll D., Tsuchiya H.;
RT   "Isolation of a FYVE zinc finger containing phosphatase expressed in
RT   mouse bone marrow derived dendritic cells.";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Amnion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: Dephosphorylates proteins phosphorylated on Ser, Thr,
CC       and Tyr residues and low molecular weight phosphatase substrate
CC       para-nitrophenylphosphate. Phosphorylates phosphatidylinositol
CC       3,4,5-trisphosphate (PIP3) (By similarity).
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane;
CC       Peripheral membrane protein (By similarity). Note=Localized to
CC       perinuclear region (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q91XS1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q91XS1-2; Sequence=VSP_028126;
CC         Note=Gene prediction based on EST data;
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class myotubularin subfamily.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 1 myotubularin phosphatase domain.
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DR   EMBL; AF262986; AAK58180.1; -; mRNA.
DR   EMBL; AK146641; BAE27324.1; -; mRNA.
DR   EMBL; AL596086; CAI35136.2; -; Genomic_DNA.
DR   EMBL; AL596086; CAI35138.1; -; Genomic_DNA.
DR   IPI; IPI00129408; -.
DR   IPI; IPI00461622; -.
DR   RefSeq; NP_573478.1; NM_133215.1.
DR   UniGene; Mm.399376; -.
DR   HSSP; P40343; 1VFY.
DR   ProteinModelPortal; Q91XS1; -.
DR   SMR; Q91XS1; 35-573, 1026-1170.
DR   STRING; Q91XS1; -.
DR   PhosphoSite; Q91XS1; -.
DR   PRIDE; Q91XS1; -.
DR   Ensembl; ENSMUST00000092802; ENSMUSP00000090478; ENSMUSG00000018401.
DR   Ensembl; ENSMUST00000103179; ENSMUSP00000099468; ENSMUSG00000018401.
DR   Ensembl; ENSMUST00000119628; ENSMUSP00000112902; ENSMUSG00000018401.
DR   GeneID; 170749; -.
DR   KEGG; mmu:170749; -.
DR   UCSC; uc007ktz.1; mouse.
DR   CTD; 170749; -.
DR   MGI; MGI:2180699; Mtmr4.
DR   GeneTree; ENSGT00580000081198; -.
DR   HOGENOM; HBG715843; -.
DR   HOVERGEN; HBG052526; -.
DR   InParanoid; Q91XS1; -.
DR   OMA; GHCTGPG; -.
DR   OrthoDB; EOG4R501X; -.
DR   PhylomeDB; Q91XS1; -.
DR   BRENDA; 3.1.3.48; 244.
DR   NextBio; 370322; -.
DR   ArrayExpress; Q91XS1; -.
DR   Bgee; Q91XS1; -.
DR   CleanEx; MM_MTMR4; -.
DR   Genevestigator; Q91XS1; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR010569; Myotub-related.
DR   InterPro; IPR017906; Myotubularin_phosphatase_dom.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF06602; Myotub-related; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Hydrolase; Membrane;
KW   Metal-binding; Phosphoprotein; Protein phosphatase; Zinc; Zinc-finger.
FT   CHAIN         1   1190       Myotubularin-related protein 4.
FT                                /FTId=PRO_0000304810.
FT   DOMAIN      153    570       Myotubularin phosphatase.
FT   ZN_FING    1109   1169       FYVE-type.
FT   REGION      320    323       Substrate binding (By similarity).
FT   REGION      345    346       Substrate binding (By similarity).
FT   REGION      407    413       Substrate binding (By similarity).
FT   COILED     1020   1052       Potential.
FT   ACT_SITE    407    407       Phosphocysteine intermediate (By
FT                                similarity).
FT   BINDING     453    453       Substrate (By similarity).
FT   MOD_RES     637    637       Phosphoserine.
FT   VAR_SEQ     497    553       Missing (in isoform 2).
FT                                /FTId=VSP_028126.
SQ   SEQUENCE   1190 AA;  132885 MW;  37E6741227E9DBFF CRC64;
     MGEEGPPSLE YIQAKDLFPP KELVKEEENL QVPFTVLQGE GVEFLGRATD ALIAISNYRL
     HIKFKDSVIN VPLRMIDSVE SRDMFQLHIA CKDSKVVRCH FSTFKQCQEW LSRLSRATAR
     PAKPEDLFAF AYHAWCLGLT EEDQHTHLCQ PGEHIRCRQE AELARMGFDL QNVWRVSHIN
     SNYKLCPSYP QKLLVPVWIT DKELENVASF RSWKRIPVVV YRHLRNGAAI ARCSQPEISW
     WGWRNADDEY LVTSIAKACA LDPGTRASGG SLSTGTNDAS EACDTDFDSS LTACSGVEST
     AAPQKLLILD ARSYTAAVAN RAKGGGCECE EYYPNCEVLF MGMANIHAIR NSFQYLRAVC
     SQMPDPSNWL SALESTKWLQ HLSVMLKAAV LVANTVDREG RPVLVHCSDG WDRTPQIVAL
     AKILLDPYYR TLEGFQVLVE SDWLDFGHKF GDRCGHQENA EDQNEQCPVF LQWLDSVHQL
     LKQFPCLFEF NEAFLVKLVQ HTYSCLYGTF LANNPCEREK RNIYKRTCSV WALLRAGNKN
     FHNFLYTPGS DVVLHPVCHV RALHLWTAVY LPASSPCTLG EENMDLYLSP VAQSQEFSGR
     SLDRLPKTRS MDDLLSACDT SSPLTRTSSD PNLNNHSQEV RGSLEPWHSS PEGAETVIDS
     GVGSPQLTVG EMGLPPPLPS SQKEYLSNKP FKGHKSCSLS YKLLNTSVSW EMKSNTSDIK
     VLEETEALAP DPSAQEEQGR TSDGLGKPPE QFLEKEAVSS LCSVSSKCGG ACDFPEPPQD
     PLTGTPQQPH LDSMQISPSR CTPDHSQGSL CNPPSVASQT PEPNTDLLSQ DPPGSTASIS
     HQEQPSSVPD LIYKKEDAGK RGSKNGQLLE NPRFGKMPLE LARKPISQSQ ISEFSFLGSN
     WDSFQGMMTS FPSGETTPRR LLAYGCCSKR PSNKHIRAAG PCLGGQWAQR EGMKSPVCSS
     HSNGHCTGPG GKNNRMWFSS HPKQVSSTKP SLLSCPSPVP PLYLDDDGLP FPTDVIQHRL
     RQIEAGYRQE VEQLRRQVRE LQMRLDIRHC CAPPAEPPMD YEDDFTCLKE SDGSDTEDFG
     SDHSEDCLSE ASWEPVDKKE TEVTRWVPDH MASHCFNCDC EFWLAKRRHH CRNCGNVFCA
     GCCHLKLPIP DQQLYDPVLV CNSCYEHIQV SRARELMSQH LKKPIATASS
//
ID   WRIP1_MOUSE             Reviewed;         660 AA.
AC   Q91XU0; Q3TCT7; Q6PDF0; Q8BUW5; Q8BWP6; Q8BY55; Q921W3; Q9EQL3;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=ATPase WRNIP1;
DE   AltName: Full=Werner helicase-interacting protein 1;
GN   Name=Wrnip1; Synonyms=Whip;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH WRN,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Testis;
RX   MEDLINE=21283010; PubMed=11301316; DOI=10.1074/jbc.C100035200;
RA   Kawabe Y., Branzei D., Hayashi T., Suzuki H., Masuko T., Onoda F.,
RA   Heo S.-J., Ikeda H., Shimamoto A., Furuichi Y., Seki M., Enomoto T.;
RT   "A novel protein interacts with the Werner's syndrome gene product
RT   physically and functionally.";
RL   J. Biol. Chem. 276:20364-20369(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Cerebellum, Liver, Placenta, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II, and FVB/N-3; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 182-660 (ISOFORM 1).
RA   Shannon M., Ramirez M., Thelen M.P.;
RT   "Characterization of RuvB homologs in human and mouse.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-529, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Functions as a modulator for initiation or reinitiation
CC       events during DNA polymerase delta-mediated DNA synthesis. Has an
CC       intrinsic ATPase activity that functions as a sensor of DNA damage
CC       or of arrested replication forks and regulates the extent of DNA
CC       synthesis (By similarity).
CC   -!- SUBUNIT: Homooligomer; most likely an octamer. Interacts with
CC       POLD1, POLD2 an POLD4. Interacts (via UBZ-type zinc finger) with
CC       polyubiquitin (By similarity). Interacts with the N-terminal
CC       domain of WRN.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Colocalizes with WRN in
CC       granular structures in the nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q91XU0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q91XU0-2; Sequence=VSP_051784, VSP_051785;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG35725.1; Type=Frameshift; Positions=191, 223, 233;
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DR   EMBL; AB056151; BAB60708.1; -; mRNA.
DR   EMBL; AK041886; BAC31091.1; -; mRNA.
DR   EMBL; AK050368; BAC34213.1; -; mRNA.
DR   EMBL; AK082078; BAC38404.1; -; mRNA.
DR   EMBL; AK167570; BAE39633.1; -; mRNA.
DR   EMBL; AK170542; BAE41868.1; -; mRNA.
DR   EMBL; AK170846; BAE42069.1; -; mRNA.
DR   EMBL; AL645808; CAI25647.1; -; Genomic_DNA.
DR   EMBL; BC010482; AAH10482.1; -; mRNA.
DR   EMBL; BC058744; AAH58744.1; -; mRNA.
DR   EMBL; AF208046; AAG35725.1; ALT_FRAME; mRNA.
DR   IPI; IPI00459468; -.
DR   IPI; IPI00648000; -.
DR   RefSeq; NP_084491.3; NM_030215.3.
DR   UniGene; Mm.286680; -.
DR   ProteinModelPortal; Q91XU0; -.
DR   SMR; Q91XU0; 225-658.
DR   STRING; Q91XU0; -.
DR   PhosphoSite; Q91XU0; -.
DR   PRIDE; Q91XU0; -.
DR   Ensembl; ENSMUST00000021832; ENSMUSP00000021832; ENSMUSG00000021400.
DR   GeneID; 78903; -.
DR   KEGG; mmu:78903; -.
DR   UCSC; uc007pzs.1; mouse.
DR   UCSC; uc007pzt.1; mouse.
DR   CTD; 78903; -.
DR   MGI; MGI:1926153; Wrnip1.
DR   eggNOG; roNOG06905; -.
DR   GeneTree; ENSGT00390000008538; -.
DR   HOVERGEN; HBG062192; -.
DR   InParanoid; Q91XU0; -.
DR   OMA; GEDDPGH; -.
DR   OrthoDB; EOG457568; -.
DR   PhylomeDB; Q91XU0; -.
DR   NextBio; 349714; -.
DR   ArrayExpress; Q91XU0; -.
DR   Bgee; Q91XU0; -.
DR   CleanEx; MM_WRNIP1; -.
DR   Genevestigator; Q91XU0; -.
DR   GermOnline; ENSMUSG00000021400; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0000731; P:DNA synthesis involved in DNA repair; ISS:UniProtKB.
DR   GO; GO:0030174; P:regulation of DNA-dependent DNA replication initiation; ISS:UniProtKB.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR021886; MgsA_C.
DR   InterPro; IPR006642; Znf_Rad18_put.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF12002; MgsA_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00734; ZnF_Rad18; 1.
DR   PROSITE; PS00674; AAA; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; DNA damage;
KW   DNA replication; Hydrolase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein.
FT   CHAIN         1    660       ATPase WRNIP1.
FT                                /FTId=PRO_0000084786.
FT   NP_BIND     263    270       ATP (Potential).
FT   MOD_RES      65     65       Phosphoserine (By similarity).
FT   MOD_RES      75     75       Phosphoserine (By similarity).
FT   MOD_RES      85     85       Phosphothreonine (By similarity).
FT   MOD_RES      91     91       Phosphoserine (By similarity).
FT   MOD_RES      92     92       Phosphoserine.
FT   MOD_RES     116    116       Phosphothreonine (By similarity).
FT   MOD_RES     151    151       Phosphoserine (By similarity).
FT   MOD_RES     153    153       Phosphoserine.
FT   MOD_RES     529    529       Phosphotyrosine.
FT   MOD_RES     557    557       Phosphotyrosine (By similarity).
FT   MOD_RES     628    628       N6-acetyllysine (By similarity).
FT   VAR_SEQ     544    568       LADPSALAQAVAAYQGCHFIGMPEC -> EWRRVCVGVGVL
FT                                RGGVLTLVWSHAE (in isoform 2).
FT                                /FTId=VSP_051784.
FT   VAR_SEQ     569    660       Missing (in isoform 2).
FT                                /FTId=VSP_051785.
FT   CONFLICT    180    180       G -> V (in Ref. 2; BAC34213).
FT   CONFLICT    202    203       RA -> P (in Ref. 5; AAG35725).
FT   CONFLICT    232    232       Q -> H (in Ref. 5; AAG35725).
FT   CONFLICT    243    243       Q -> E (in Ref. 1; BAB60708).
FT   CONFLICT    453    453       R -> K (in Ref. 1; BAB60708).
FT   CONFLICT    455    455       V -> M (in Ref. 4; AAH10482).
FT   CONFLICT    499    499       S -> C (in Ref. 2; BAC38404).
FT   CONFLICT    566    566       P -> H (in Ref. 1; BAB60708).
SQ   SEQUENCE   660 AA;  71794 MW;  A9114A131B5F9763 CRC64;
     MEVSGPEDDP FLSQLHQVQC PVCQQMMPAA HINSHLDRCL LLHPAGHAEP AAGSHRAGER
     AKGPSPPGAK RRRLSESSAL KQPATPTAAE SSEGEGEEGD DGGETESRES YDAPPTPSGA
     RLIPDFPVAR SSSPARKGMG KRPAAAAAAG SASPRSWDEA EAQEEEEAGV DGDGDADVDG
     EDDPGHWDAD AADASFGVSA GRAHPRALAA EEIRQMLEGK PLADKMRPDT LQDYIGQSRA
     VGQETLLRSL LEANEIPSLI LWGPPGCGKT TLAHIIANNS KKHSIRFVTL SATNAKTNDV
     RDVIKQAQNE KSFFKRKTIL FIDEIHRFNK SQQDTFLPHV ECGTITLIGA TTENPSFQVN
     AALLSRCRVI VLEKLPVEAM VTILMRAINS LGIHVLDSSR PTDPLSHSSN CSSEPSVFIE
     DKAVDTLAYL SDGDARTGLN GLQLAVLARL SSRKVFCKKS GQTYSPSRVL ITENDVKEGL
     QRSHILYDRA GEEHYNCISA LHKAMRGSDQ NASLYWLARM LEGGEDPLYV ARRLVRFASE
     DIGLADPSAL AQAVAAYQGC HFIGMPECEV LLAQCVVYFA RAPKSIEVYS AYNNVKACLR
     SHQGPLPPVP LHLRNAPTRL MKDLGYGKGY KYNPMYSEPV DQDYLPEELR GVDFFKQRRC
//
ID   BASP1_MOUSE             Reviewed;         226 AA.
AC   Q91XV3;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Brain acid soluble protein 1;
DE   AltName: Full=22 kDa neuronal tissue-enriched acidic protein;
DE   AltName: Full=Neuronal axonal membrane protein NAP-22;
GN   Name=Basp1; Synonyms=Nap22;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C57BL/6J X CBA/J; TISSUE=Spleen;
RA   Hamada K., Sokawa Y., Maekawa S.;
RT   "Mouse NAP-22 (22 kDa neuronal tissue-enriched acidic protein) gene.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 26-52; 92-123 AND 147-225, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31; THR-36; SER-92;
RP   SER-128; SER-160; SER-167; SER-173 AND SER-218, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-31 AND THR-36, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Cell
CC       projection, growth cone. Note=Associated with the membranes of
CC       growth cones that form the tips of elongating axons.
CC   -!- SIMILARITY: Belongs to the BASP1 family.
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DR   EMBL; AB046714; BAB62404.1; -; Genomic_DNA.
DR   IPI; IPI00129519; -.
DR   RefSeq; NP_081671.1; NM_027395.2.
DR   UniGene; Mm.29586; -.
DR   ProteinModelPortal; Q91XV3; -.
DR   STRING; Q91XV3; -.
DR   PhosphoSite; Q91XV3; -.
DR   PRIDE; Q91XV3; -.
DR   Ensembl; ENSMUST00000058845; ENSMUSP00000053943; ENSMUSG00000045763.
DR   GeneID; 70350; -.
DR   KEGG; mmu:70350; -.
DR   UCSC; uc007vix.1; mouse.
DR   CTD; 70350; -.
DR   MGI; MGI:1917600; Basp1.
DR   eggNOG; maNOG21665; -.
DR   GeneTree; ENSGT00530000063966; -.
DR   InParanoid; Q91XV3; -.
DR   OMA; QNIAVNE; -.
DR   NextBio; 331418; -.
DR   ArrayExpress; Q91XV3; -.
DR   Bgee; Q91XV3; -.
DR   Genevestigator; Q91XV3; -.
DR   GermOnline; ENSMUSG00000045763; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0010843; F:promoter binding; IDA:UniProtKB.
DR   GO; GO:0016566; F:specific transcriptional repressor activity; ISS:UniProtKB.
DR   GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR   GO; GO:0072112; P:glomerular visceral epithelial cell differentiation; IDA:UniProtKB.
DR   GO; GO:0032582; P:negative regulation of gene-specific transcription; ISS:UniProtKB.
DR   InterPro; IPR008408; BASP1.
DR   PANTHER; PTHR23212; BASP1; 1.
DR   Pfam; PF05466; BASP1; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell projection; Direct protein sequencing;
KW   Lipoprotein; Membrane; Myristate; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    226       Brain acid soluble protein 1.
FT                                /FTId=PRO_0000142896.
FT   MOD_RES      31     31       Phosphothreonine.
FT   MOD_RES      36     36       Phosphothreonine.
FT   MOD_RES      92     92       Phosphoserine.
FT   MOD_RES     128    128       Phosphoserine.
FT   MOD_RES     160    160       Phosphoserine.
FT   MOD_RES     167    167       Phosphoserine.
FT   MOD_RES     169    169       Phosphoserine (By similarity).
FT   MOD_RES     173    173       Phosphoserine.
FT   MOD_RES     218    218       Phosphoserine.
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
SQ   SEQUENCE   226 AA;  22087 MW;  B41CCAAB447C705D CRC64;
     MGGKLSKKKK GYNVNDEKAK DKDKKAEGAG TEEEGTPKES EPQAAADATE VKESTEEKPK
     DAADGEAKAE EKEADKAAAA KEEAPKAEPE KSEGAAEEQP EPAPAPEQEA AAPGPAAGGE
     APKAGEASAE STGAADGAAP EEGEAKKTEA PAAAGPEAKS DAAPAASDSK PSSAEPAPSS
     KETPAASEAP SSAAKAPAPA APAAAEPQAE APAAAASSEQ SVAVKE
//
ID   Q91XW2_MOUSE            Unreviewed;      2556 AA.
AC   Q91XW2;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 49.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase;
DE            EC=3.1.2.15;
GN   Name=Usp9y;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BALB/c; TISSUE=Testis;
RA   Hall N.M.;
RL   Thesis (2001), Department of Pathology, University of Cambridge,
RL   Cambridge, United Kingdom.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- CATALYTIC ACTIVITY: Ubiquitin C-terminal thioester + H(2)O =
CC       ubiquitin + a thiol.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AJ307017; CAC38831.1; -; mRNA.
DR   IPI; IPI00129561; -.
DR   UniGene; Mm.347376; -.
DR   HSSP; Q93009; 1NB8.
DR   ProteinModelPortal; Q91XW2; -.
DR   SMR; Q91XW2; 1555-1960.
DR   STRING; Q91XW2; -.
DR   MEROPS; C19.051; -.
DR   PhosphoSite; Q91XW2; -.
DR   PRIDE; Q91XW2; -.
DR   Ensembl; ENSMUST00000091188; ENSMUSP00000088727; ENSMUSG00000069044.
DR   UCSC; uc009uzo.1; mouse.
DR   MGI; MGI:1313274; Usp9y.
DR   eggNOG; roNOG12628; -.
DR   GeneTree; ENSGT00600000084366; -.
DR   HOGENOM; HBG358333; -.
DR   HOVERGEN; HBG073749; -.
DR   InParanoid; Q91XW2; -.
DR   OrthoDB; EOG46HG8S; -.
DR   PhylomeDB; Q91XW2; -.
DR   ArrayExpress; Q91XW2; -.
DR   Bgee; Q91XW2; -.
DR   Genevestigator; Q91XW2; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:EC.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 2.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; 1.
DR   PROSITE; PS50235; UCH_2_3; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Protease; Thiol protease; Ubl conjugation pathway.
SQ   SEQUENCE   2556 AA;  292177 MW;  59D949A3C2B5647C CRC64;
     MTITTRGSPV GENESQGQTS DGQPQPSFQQ NQISSSDSSN ETSPTTPPYE QGQGDAPPQH
     EEEDPSFPHT DPAKLEDMIN RSRWVVPVLP KGELEVLLET SIDLTKKGLD VKSEACQRFF
     RDVLTVSFSK ILMDEAVSGW KFEIHRCIIN NTHRLVELCV AKLSQDWFPF LELLAIALNP
     HCKFHVYNGA RPCESVSSSV QFPEDELFAC SPDLHSPKGW LVDLINTFGT LNGFQILHDR
     FTSGSALNVQ TIAAPIKPFG QCYEFLTQHT LRKYFIPVIE VVPQILQKLT NEELKKETKT
     EVKNDTISMI IKFLKNLASR IPGQEETVKN LETFRLKMIL RLLQISSFNG KMNALNEINK
     VLSSVSYYTH GHGNSEGEWL TVERMTEWIQ QNNILSIVLQ DSLHQPQYVE KIEKILRFVI
     KEKALTLQDL NNIWAAQAGK HEAIVKNVHD LLAKLAWNFS PEQLDHLFDC FKASWTNASK
     KQREKLLELI RRLAEDDKDG VMAHKVLNLL WNLAHSDDVP VDIMDLALSA HIKILDYSCS
     QDRDTQKIQW IDCFIEEFRT NNKWVIPALK QIKEICSLFG EAPQNLSQTH QSPRVFYRHD
     LISQLQHNHA LVTLVAENLA AYMNSIRLYA RDHEDYDPQT VRLGSRYSHV QEVQERLNFL
     RFLLKDGQLW LCVSQAKQIW NCLAENAVYF SDREACFMWY SKLMGDEPDL HPDINKEFFE
     SNVLQLDPSL LTENGMKCFE RFFKTVNCRE GKLMIKRKIY MMDDLDLIGL DYLWKVVIQS
     NDDISSRAID LLKEIYTSLG PKLQANQVVI HEDFIQSCFD RLKASYDTLC VLDSEKDNIF
     SCARQEAIRM VRILTVLREY ISEYDSDYHE ERMILPMSRA FRGKHLSFTV RFPNQGKEVE
     DLDILSHTNA TIGSVRRCIL NRMNVNVAHT KIELFIGGEL VASEDDRKLV EQLNLKDKSL
     ITAKFIQINS NMPSSPDSSS DSSAGPPGNH SHNNYRDVSN PEMEKCLPGV IMSLQPRYIS
     FLWQVADLGS MLTVPTLRDG ARILMKLMPP DSTTLEQLRA LCSDHVNLGE RRLGQSLHSL
     FFGSSASQVL YLTEVVYTLL MPAGAPLADI SSDFQYHFLK SGGLPLVLSM LIQNNFLPNT
     DVETRRDAYF SALKIAKLLL TIVGYGHVQA IAEACQPVAD GTDPKTPINQ VTHDQAVVLQ
     NALQSIPNPS SECMLRNVSV HLAQQISGLA SRYIPDICVI RAIQKIIWAA GCGSLELVFS
     PNEDITETYK MTTSTRSNLE VKDEQVCCEA LEVMTLCFAL IPTAMDSLNK EKAWQSFVID
     LLLYCPSKTV RQLAQEQFFL ICTRCCMGHR PLLFFITLLF TILGGAANEK GKHSDVYFTL
     LRRLLTYAYN SNIQVPNVDV LLNDEIDWLK RVRDYIKNTG ETNVEDPILE GHLGVTKELL
     SFQSPEKKYH IGCKTGGANL VKELIDYFIF PASKAYLQYM RSGELPIKQA IPVCGSPATI
     NAGFELLVAL AFGCVRNLKQ IVNCLTELFY IGTPVTTCEA VGEWEYLPPV GPRPPKGFVG
     LKNAGATCYM NSVIQQLFMI PSIRNSILAI DSIWSDTDDD IFKGEKQDSE NNVDPRDDVF
     RYPHQFEDKP TLSKVEDRKE YNIAVLKHLQ ITFGHLAASQ LQYYVPKGFW QQFRLWGEPV
     NLREQHDALE FFNSLVDSLD EAFKALGYPT VLSKVLGGSF ADQKICQGCP HRYECEESFT
     TLNVDIRNHQ NLLDSLEQYV KGDLLEGANA YHCEKCDKKV DTVKRLLIKK LPSVLTIQLK
     RFDYDWEREC AIKFNDYFEF PRELDMEPYT VAGATKLEGD SVNPQTQLIK QNEQSESVIP
     GSTKYRLVGV LVHSGQANGG HYYSYIIQRN GKDSKRSHWF KFDDGDVTEC KMDDDEEMKN
     QCFGGEYMGE VFDHMMKRMS YRRQKRWWNA YILFYERMDI TDEDDEIITY ISELTFTRPH
     QIMSPAIERS VWKQNVQFLH NQMQFSLEYF QFIKKLLTCN AVYLSPAPGQ DHLLPEAEDI
     TMISIQLASR FLFTTGFHTK KIIRGPANDW YDALCILLRH SKNVRFWFVH NVLFNVSNRF
     SEYLLECPSA EIRGTFAKLI VFIAHFSLQD GSSPSPFTSP FANPGPYSQI YDNLSLSDHL
     LKAVLSLLRR EVSEHGRHLQ QYFNLFIMYA SLGLAEKTQL LKLNVPATFM LVSLDEGPGP
     PVKYQYAELS KLHSVVSQLI RCCSVSSRMQ SSINGNPPLP NPFGDPNLSQ PIMPIQQNVA
     DILFMRTTYM KKVIEDCSNS EDTVKLLLFC CWENPQFSCS VLSELLWQVA HSHAYELQPY
     LDLLLQIILF EDSWQAHRIH NALKGIPNDQ DGLFDTIQHS KNHHQKRAYQ CIKWMVTLFN
     SCPVAYQILQ GNGDLKNKWT WAMEWLGDEL ERKPYSGNPQ YTYSNWSPPV QSNETANGYF
     LEKSHSAKMK LTKACDLYPE EDPDDQDALD EHVSHAPQDR TFYLYSHRSH YQQNYVPEQP
     FSGPASHHLN NPQKNDKPQE THESNEEISS CLIKDQ
//
ID   Q91XW9_MOUSE            Unreviewed;       944 AA.
AC   Q91XW9;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   SubName: Full=MCG133388, isoform CRA_f;
DE   SubName: Full=Pcdhgc5 protein;
DE   SubName: Full=Protocadherin gamma C-V;
DE   SubName: Full=Protocadherin gamma C5;
DE   SubName: Full=Protocadherin gamma subfamily C, 5;
GN   Name=Pcdhgc5; ORFNames=mCG_133388;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=99308636; PubMed=10380929; DOI=10.1016/S0092-8674(00)80789-8;
RA   Wu Q., Maniatis T.;
RT   "A striking organization of a large family of human neural cadherin-
RT   like cell adhesion genes.";
RL   Cell 97:779-790(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=20202599; PubMed=10716726; DOI=10.1073/pnas.060027397;
RA   Wu Q., Maniatis T.;
RT   "Large exons encoding multiple ectodomains are a characteristic
RT   feature of protocadherin genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:3124-3129(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=21154914; PubMed=11230163; DOI=10.1101/gr.167301;
RA   Wu Q., Zhang T., Cheng J.-F., Kim Y., Grimwood J., Schmutz J.,
RA   Dickson M., Noonan J.P., Zhang M.Q., Myers R.M., Maniatis T.;
RT   "Comparative DNA sequence analysis of mouse and human protocadherin
RT   gene clusters.";
RL   Genome Res. 11:389-404(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testicle, and Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=22148756; PubMed=12154121; DOI=10.1101/gad.1004802;
RA   Wang X., Su H., Bradley A.;
RT   "Molecular mechanisms governing Pcdh-gamma gene expression: evidence
RT   for a multiple promoter and cis-alternative splicing model.";
RL   Genes Dev. 16:1890-1905(2002).
CC   -!- FUNCTION: Potential calcium-dependent cell-adhesion protein. May
CC       be involved in the establishment and maintenance of specific
CC       neuronal connections in the brain (By similarity).
CC   -!- SIMILARITY: Contains 6 cadherin domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC138677; AAI38678.1; -; mRNA.
DR   EMBL; BC138678; AAI38679.1; -; mRNA.
DR   EMBL; AY013813; AAK26102.1; -; mRNA.
DR   EMBL; AF464163; AAM93564.1; -; mRNA.
DR   EMBL; CH466528; EDL10123.1; -; Genomic_DNA.
DR   IPI; IPI00129572; -.
DR   RefSeq; NP_291061.1; NM_033583.3.
DR   UniGene; Mm.247203; -.
DR   ProteinModelPortal; Q91XW9; -.
DR   SMR; Q91XW9; 24-136, 232-348, 410-668.
DR   STRING; Q91XW9; -.
DR   PRIDE; Q91XW9; -.
DR   Ensembl; ENSMUST00000055935; ENSMUSP00000060949; ENSMUSG00000023036.
DR   GeneID; 93708; -.
DR   KEGG; mmu:93708; -.
DR   UCSC; uc008erg.1; mouse.
DR   CTD; 93708; -.
DR   GeneTree; ENSGT00560000076625; -.
DR   HOGENOM; HBG447181; -.
DR   HOVERGEN; HBG054878; -.
DR   InParanoid; Q91XW9; -.
DR   OMA; PEREIRI; -.
DR   PhylomeDB; Q91XW9; -.
DR   NextBio; 351499; -.
DR   ArrayExpress; Q91XW9; -.
DR   Bgee; Q91XW9; -.
DR   Genevestigator; Q91XW9; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR013164; Cadherin_N.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 6.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF08266; Cadherin_2; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 6.
DR   SUPFAM; SSF49313; Cadherin; 6.
DR   PROSITE; PS00232; CADHERIN_1; 5.
DR   PROSITE; PS50268; CADHERIN_2; 6.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell membrane; Membrane; Repeat;
KW   Transmembrane; Transmembrane helix.
SQ   SEQUENCE   944 AA;  101891 MW;  D11F9991EEA0F8EB CRC64;
     MRPMASPQVA GKWQVLCMLS LCCCGWVSGQ LRYSVVEESE PGTLVGNVAQ DLGLKGTDLL
     SRRLRLGSEE NGRYFSLSLV SGALAVSQKI DRESLCGAST SCLLPVQVVT EHPLELTRVE
     VEILDLNDNS PSFATPDREM RISESAAPGA RFPLDSAQDP DVGTNTVSFY TLSPNSHFSL
     HVKTLKDGKL FPELVLEQQL DRETQARHQL VLTAVDGGTP ARSGTSLISV IVLDVNDNAP
     TFQSSVLRVG LPENTPPGTL LLRLNATDPD EGTNGQLDYS FGDHTSETVK NLFGLDPSSG
     AIHVLGPVDF EESNFYEIHA RARDQGQPAM EGHCVIQVDV GDANDNPPEV LLASLVNPVL
     ESTPVGTVVG LFNVRDRDSG RNGEVSLKTS PNLPFQIKPS ENHYSLLTSQ PLDREATSHY
     TIELLASDAG SPPLHTHLTL RLNISDVNDN APHFTQQLYT AYIPENRPPG SLLCTVAASD
     PDEGDNARLT YSIVGSQIQG APASSFVYVN PEDGRIFAQR TFDYELLQML QIVVGVRDSG
     SPRLHANTSL HVFVLDQNDN APAVLHPRPG REFSAPQRLP RSAPPGSLVT KVTAVDADAG
     HNAWLSYSLL PQSTAPGLFL VSAHTGEVRT ARALLEDDSD TQQVVVLVRD NGDPSLSSTA
     TVLLVLEDED AEEMPKSSDF LTHPPERSDL TLYLIVALAA VSLLSLVTFT FMSAKCLRRH
     EDGDRGGGHC CRGQDSPSRE FYKQSSPNLQ VSSDGTLKYM EVTLRPTDSQ SHCYRTCFSP
     ASDGSDFTFL RPLSVQQPSA LALEPEALRS RSSTLRERSQ QAPPNTDWRF SQAQRPGTSG
     SQNGDETGTW PNNQFDTEML QAMILASASE AADGSSTLGG GAGTMGLSAR YGPQFTLQHV
     PDYRQNVYIP GSNATLTNAA GKRDGKAPAG GNGNKKKSGK KEKK
//
ID   Q91XY7_MOUSE            Unreviewed;       932 AA.
AC   Q91XY7;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   SubName: Full=Protocadherin gamma A12;
DE   SubName: Full=Protocadherin gamma subfamily A, 12;
GN   Name=Pcdhga12;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=99308636; PubMed=10380929; DOI=10.1016/S0092-8674(00)80789-8;
RA   Wu Q., Maniatis T.;
RT   "A striking organization of a large family of human neural cadherin-
RT   like cell adhesion genes.";
RL   Cell 97:779-790(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=20202599; PubMed=10716726; DOI=10.1073/pnas.060027397;
RA   Wu Q., Maniatis T.;
RT   "Large exons encoding multiple ectodomains are a characteristic
RT   feature of protocadherin genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:3124-3129(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=21154914; PubMed=11230163; DOI=10.1101/gr.167301;
RA   Wu Q., Zhang T., Cheng J.-F., Kim Y., Grimwood J., Schmutz J.,
RA   Dickson M., Noonan J.P., Zhang M.Q., Myers R.M., Maniatis T.;
RT   "Comparative DNA sequence analysis of mouse and human protocadherin
RT   gene clusters.";
RL   Genome Res. 11:389-404(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Potential calcium-dependent cell-adhesion protein. May
CC       be involved in the establishment and maintenance of specific
CC       neuronal connections in the brain (By similarity).
CC   -!- SIMILARITY: Contains 6 cadherin domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC054528; AAH54528.1; -; mRNA.
DR   EMBL; BC056998; AAH56998.1; -; mRNA.
DR   EMBL; AY013795; AAK26084.1; -; mRNA.
DR   IPI; IPI00229003; -.
DR   RefSeq; NP_291073.1; NM_033595.4.
DR   UniGene; Mm.247203; -.
DR   ProteinModelPortal; Q91XY7; -.
DR   SMR; Q91XY7; 25-137, 232-345, 354-666.
DR   STRING; Q91XY7; -.
DR   PRIDE; Q91XY7; -.
DR   Ensembl; ENSMUST00000044851; ENSMUSP00000036359; ENSMUSG00000023036.
DR   GeneID; 93724; -.
DR   KEGG; mmu:93724; -.
DR   UCSC; uc008erd.1; mouse.
DR   CTD; 93724; -.
DR   HOVERGEN; HBG054878; -.
DR   NextBio; 351555; -.
DR   ArrayExpress; Q91XY7; -.
DR   Bgee; Q91XY7; -.
DR   Genevestigator; Q91XY7; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR013164; Cadherin_N.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 6.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF08266; Cadherin_2; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 6.
DR   SUPFAM; SSF49313; Cadherin; 6.
DR   PROSITE; PS00232; CADHERIN_1; 5.
DR   PROSITE; PS50268; CADHERIN_2; 6.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell membrane; Membrane; Repeat;
KW   Transmembrane; Transmembrane helix.
SQ   SEQUENCE   932 AA;  100834 MW;  2FA4348E600D0575 CRC64;
     MIPMQRREDC KGLVFLGVLL GMLWKAGSTQ IRYSVPEELE KGSRVGNISK DLGLEPRELE
     KRGVRIVSRG RAQLFALNPR SGSLVTAGRI DREELCMGSI KCQLNLEILM EDIGKIYGVE
     IEVRDINDNA PYFRESELEI KMSENAAAGM RFPLPHAWDP DIGKNSLQSY QLSPNAHFSL
     EVQNGADGNK YPELVLESSL DREEKAAHLL VLTASDAGDP VRTGTARIRV MVVDANDNAP
     AFARSEYRVS VRENVAVGTQ LLLVNATDPD EGANAEVIYS FRYVDDKAAK VFKLDSNLGT
     ISTIGELNHE ESGFYEMEVQ ATDNAGYSAR AKVLVTVLDV NDNAPEVAIT SLTNSVPENS
     PQGTLIALLN VNDQDSGENG QVICSIQENL PFKLEKSYGN YYRLVTDAVL DREEVPSYNI
     TMTATDRGSP PLTTETHLAL DIADTNDNSP VFLQASYWAY IPENNPRGAS IASVTAHDPD
     SDKNAQVTYS LAEDTHQGVP LSSYVSINSD TGVLYALHSF DYEQFPDLQL QVIARDSGDP
     PLSSNVSLSL FVLDQNDNVP EILYPTLPTD GSTGVELAPR SAEPGYLVTK VVAVDRDSGQ
     NAWLSYRLLK ASEPGLFSVG LHTGEISTAR ALMDRDALKQ NLVVSVQDHG QPPLSATVTL
     TVAIADSIPD VLADLDNLES PSTSETSGLT LYLVVAVAAV STVFLVFVLV LLALRLRRWH
     SLRLLRAGGP GLADVAASHF VGVDGVQAFL QTYSHEVSLT AGSRKSHLIF PQPNYADTLI
     SQESCEKTEP LLPSGDSVFS KDNHALNQQA PPNTDWRFSQ AQRPGTSGSQ NGDETGTWPN
     NQFDTEMLQA MILASASEAA DGSSTLGGGA GTMGLSARYG PQFTLQHVPD YRQNVYIPGS
     NATLTNAAGK RDGKAPAGGN GNKKKSGKKE KK
//
ID   Q91Y09_MOUSE            Unreviewed;      1006 AA.
AC   Q91Y09;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   SubName: Full=Protocadherin alpha C2;
GN   Name=Pcdhac2; Synonyms=Pcdha1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=99308636; PubMed=10380929; DOI=10.1016/S0092-8674(00)80789-8;
RA   Wu Q., Maniatis T.;
RT   "A striking organization of a large family of human neural cadherin-
RT   like cell adhesion genes.";
RL   Cell 97:779-790(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=20202599; PubMed=10716726; DOI=10.1073/pnas.060027397;
RA   Wu Q., Maniatis T.;
RT   "Large exons encoding multiple ectodomains are a characteristic
RT   feature of protocadherin genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:3124-3129(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=21154914; PubMed=11230163; DOI=10.1101/gr.167301;
RA   Wu Q., Zhang T., Cheng J.-F., Kim Y., Grimwood J., Schmutz J.,
RA   Dickson M., Noonan J.P., Zhang M.Q., Myers R.M., Maniatis T.;
RT   "Comparative DNA sequence analysis of mouse and human protocadherin
RT   gene clusters.";
RL   Genome Res. 11:389-404(2001).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Potential calcium-dependent cell-adhesion protein. May
CC       be involved in the establishment and maintenance of specific
CC       neuronal connections in the brain (By similarity).
CC   -!- SIMILARITY: Contains 6 cadherin domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY013769; AAK26058.1; -; mRNA.
DR   IPI; IPI00129349; -.
DR   RefSeq; NP_001003672.1; NM_001003672.1.
DR   UniGene; Mm.308500; -.
DR   HSSP; P15116; 1NCJ.
DR   ProteinModelPortal; Q91Y09; -.
DR   SMR; Q91Y09; 35-151, 207-355, 419-570.
DR   STRING; Q91Y09; -.
DR   PhosphoSite; Q91Y09; -.
DR   PRIDE; Q91Y09; -.
DR   Ensembl; ENSMUST00000047479; ENSMUSP00000039888; ENSMUSG00000007440.
DR   GeneID; 353237; -.
DR   KEGG; mmu:353237; -.
DR   UCSC; uc008epk.1; mouse.
DR   CTD; 353237; -.
DR   GeneTree; ENSGT00560000076625; -.
DR   HOGENOM; HBG447181; -.
DR   HOVERGEN; HBG054878; -.
DR   InParanoid; Q91Y09; -.
DR   PhylomeDB; Q91Y09; -.
DR   NextBio; 400365; -.
DR   ArrayExpress; Q91Y09; -.
DR   Bgee; Q91Y09; -.
DR   Genevestigator; Q91Y09; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR013164; Cadherin_N.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 6.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF08266; Cadherin_2; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 6.
DR   SUPFAM; SSF49313; Cadherin; 6.
DR   PROSITE; PS00232; CADHERIN_1; 5.
DR   PROSITE; PS50268; CADHERIN_2; 6.
PE   1: Evidence at protein level;
KW   Calcium; Cell adhesion; Cell membrane; Membrane; Repeat;
KW   Transmembrane; Transmembrane helix.
SQ   SEQUENCE   1006 AA;  109492 MW;  EB7E29DCAF70BC1E CRC64;
     MEQAGARPGA TEHPRPLRPL PWLLLLSFRL LLVLLPGPAA SQLRYSVPEE QSPGALVGNV
     ARALGLELRR LGPGCLRINH LGAPSPRYLE LDLTNGALFV NERIDREALC EQRPRCLLSL
     EVLAHNPVAV SAIEVEILDI NDNSPRFPRP DYQLQVSESV APGARFHIES AQDPDVGANS
     VQTYELSPSE HFELDLKPLQ ENSKVLELVL RKGLDREQTA LHYLVLTAVD GGIPARSGTA
     QIAVRVLDTN DNSPAFDQST YRVQLREDAP PGTLVVKLNA SDPDEGSNGE LRYSLSSYTS
     DRERQLFSID VTTGEVRVSG TLDYEESSSY QIYVQATDRG PVPMAGHCKV LVDIIDVNDN
     APEVVLTDLY SPVPEDVALN TVVALLSVND QDSGSNRKVS LGLEASLPFR LNGFGNSYTL
     VVSGPLDRER VAAYNITVTA TDGGVPPLTS QRTLQVEISD INDNPPSFLK DSYSIYIEEN
     NLPGVLLCTV QATDPDQKEN AEVTYSLLDR EIQGLPVTSY VSINSASGSL YAVNSFDYEK
     FREFFVTVEA QDKGRPPLSS TVTANVYVVD VNDHAPHILY PTSTNTSAAI EMVPRTAPAG
     YLVTKVIAMD SDSGQNAWLF YHLVPTSDSD LFKVELHTGE IRITRKIGDE SGTTFNLTVV
     VRDNGEPPLS ATVAITVAVV DRVSKMLPDT QRHIKSPRTY SEITLYLIIA LSTVSFIFLL
     TIIVLSIIKC YRYTAYGTAC CGGFCGVRER CPAELYKQAN NNIDARIPHG LKVQPHFIEV
     RGNGSLTKTY CYKACLTAGS GSDTFMFYNT GAQTGPGPGG AQASVTDNRQ LTGQSRHSTG
     NLIILKNDAG SQNEPRQPNP DWRYSASLRA GMHSSVHLEE AGILRAGPGG PDQQWPTVSS
     ATPEPEAGEV SPPVGAGVNS NSWTFKYGPG NPKQSGPGEL PDKFIIPGSP AIISIRQEPA
     NNQIDKSDFI TFGKKEETKK KKKKKKGNKT QEKKEKGNST TDNSDQ
//
ID   MK08_MOUSE              Reviewed;         384 AA.
AC   Q91Y86;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 106.
DE   RecName: Full=Mitogen-activated protein kinase 8;
DE            Short=MAP kinase 8;
DE            Short=MAPK 8;
DE            EC=2.7.11.24;
DE   AltName: Full=Stress-activated protein kinase JNK1;
DE   AltName: Full=c-Jun N-terminal kinase 1;
GN   Name=Mapk8; Synonyms=Jnk1, Prkm8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH MAPK8IP3.
RC   TISSUE=Brain;
RX   MEDLINE=99455010; PubMed=10523642;
RA   Ito M., Yoshioka K., Akechi M., Yamashita S., Takamatsu N.,
RA   Sugiyama K., Hibi M., Nakabeppu Y., Shiba T., Yamamoto K.;
RT   "JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein
RT   that functions as a scaffold factor in the JNK signaling pathway.";
RL   Mol. Cell. Biol. 19:7539-7548(1999).
RN   [2]
RP   REGULATION BY MAP2K4.
RC   TISSUE=Embryonic stem cell;
RX   MEDLINE=97250480; PubMed=9096336; DOI=10.1073/pnas.94.7.3004;
RA   Yang D., Tournier C., Wysk M., Lu H.-T., Xu J., Davis R.J.,
RA   Flavell R.A.;
RT   "Targeted disruption of the MKK4 gene causes embryonic death,
RT   inhibition of c-Jun NH2-terminal kinase activation, and defects in AP-
RT   1 transcriptional activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:3004-3009(1997).
RN   [3]
RP   REGULATION BY MAP2K7, AND COFACTOR.
RX   MEDLINE=97352799; PubMed=9207092; DOI=10.1073/pnas.94.14.7337;
RA   Tournier C., Whitmarsh A.J., Cavanagh J., Barrett T., Davis R.J.;
RT   "Mitogen-activated protein kinase kinase 7 is an activator of the c-
RT   Jun NH2-terminal kinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:7337-7342(1997).
RN   [4]
RP   FUNCTION, ENZYME REGULATION, AND INDUCTION.
RC   TISSUE=Embryonic stem cell, and T-cell;
RX   MEDLINE=20269361; PubMed=10811224; DOI=10.1038/35011091;
RA   Dong C., Yang D.D., Tournier C., Whitmarsh A.J., Xu J., Davis R.J.,
RA   Flavell R.A.;
RT   "JNK is required for effector T-cell function but not for T-cell
RT   activation.";
RL   Nature 405:91-94(2000).
RN   [5]
RP   FUNCTION IN PHOSPHORYLATION OF JDP2.
RX   PubMed=11602244; DOI=10.1016/S0014-5793(01)02907-6;
RA   Katz S., Heinrich R., Aronheim A.;
RT   "The AP-1 repressor, JDP2, is a bona fide substrate for the c-Jun N-
RT   terminal kinase.";
RL   FEBS Lett. 506:196-200(2001).
RN   [6]
RP   SUBUNIT, AND PHOSPHORYLATION AT THR-183 AND TYR-185.
RC   TISSUE=Hippocampus;
RX   MEDLINE=21446505; PubMed=11562351; DOI=10.1101/gad.922801;
RA   Whitmarsh A.J., Kuan C.-Y., Kennedy N.J., Kelkar N., Haydar T.F.,
RA   Mordes J.P., Appel M., Rossini A.A., Jones S.N., Flavell R.A.,
RA   Rakic P., Davis R.J.;
RT   "Requirement of the JIP1 scaffold protein for stress-induced JNK
RT   activation.";
RL   Genes Dev. 15:2421-2432(2001).
RN   [7]
RP   INTERACTION WITH SPAG9.
RX   MEDLINE=22295031; PubMed=12391307; DOI=10.1073/pnas.232310199;
RA   Lee C.M., Onesime D., Reddy C.D., Dhanasekaran N., Reddy E.P.;
RT   "JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules
RT   and transcription factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14189-14194(2002).
RN   [8]
RP   IDENTIFICATION IN A COMPLEX WITH MAPK8IP1 AND RGNEF.
RX   PubMed=14499478; DOI=10.1016/S0169-328X(03)00263-8;
RA   Wu J., Zhai J., Lin H., Nie Z., Ge W.-W., Garcia-Bermejo L.,
RA   Muschel R.J., Schlaepfer W.W., Canete-Soler R.;
RT   "Cytoplasmic retention sites in p190RhoGEF confer anti-apoptotic
RT   activity to an EGFP-tagged protein.";
RL   Brain Res. Mol. Brain Res. 117:27-38(2003).
RN   [9]
RP   INTERACTION WITH JAMP.
RX   PubMed=16166642; DOI=10.1128/MCB.25.19.8619-8630.2005;
RA   Kadoya T., Khurana A., Tcherpakov M., Bromberg K.D., Didier C.,
RA   Broday L., Asahara T., Bhoumik A., Ronai Z.;
RT   "JAMP, a Jun N-terminal kinase 1 (JNK1)-associated membrane protein,
RT   regulates duration of JNK activity.";
RL   Mol. Cell. Biol. 25:8619-8630(2005).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [11]
RP   INTERACTION WITH NFE2, AND FUNCTION.
RX   PubMed=19966288; DOI=10.1073/pnas.0909153107;
RA   Lee T.L., Shyu Y.C., Hsu P.H., Chang C.W., Wen S.C., Hsiao W.Y.,
RA   Tsai M.D., Shen C.K.;
RT   "JNK-mediated turnover and stabilization of the transcription factor
RT   p45/NF-E2 during differentiation of murine erythroleukemia cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:52-57(2010).
CC   -!- FUNCTION: Responds to activation by environmental stress and pro-
CC       inflammatory cytokines by phosphorylating a number of
CC       transcription factors, primarily components of AP-1 such as JUN,
CC       JDP2 and ATF2 and thus regulates AP-1 transcriptional activity. In
CC       T-cells, JNK1 and JNK2 are required for polarized differentiation
CC       of T-helper cells into Th1 cells. Phosphorylates heat shock factor
CC       protein 4 (HSF4) (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: Activated by threonine and tyrosine
CC       phosphorylation by either of two dual specificity kinases, MAP2K4
CC       and MAP2K7. Inhibited by dual specificity phosphatases, such as
CC       DUSP1.
CC   -!- SUBUNIT: Binds to at least four scaffolding proteins,
CC       MAPK8IP1/JIP-1, MAPK8IP2/JIP-2, MAPK8IP3/JIP-3/JSAP1 and
CC       SPAG9/MAPK8IP4/JIP-4. These proteins also bind other components of
CC       the JNK signaling pathway. Forms a complex with MAPK8IP1 and
CC       RGNEF. Interacts with TP53 and WWOX. Interacts with JAMP.
CC       Interacts with NFATC4. Interacts with MECOM; regulates JNK
CC       signaling (By similarity). Interacts (phosphorylated form) with
CC       NFE2; the interaction phosphorylates NFE2 in undifferentiated
CC       cells.
CC   -!- INTERACTION:
CC       P05627:Jun; NbExp=1; IntAct=EBI-298784, EBI-764369;
CC   -!- INDUCTION: In T-cells, following T-cell receptor (TCR) activation.
CC       Levels peak 48 hours after TCR and CD-28 costimulation.
CC   -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC       whose phosphorylation activates the MAP kinases.
CC   -!- PTM: Dually phosphorylated on Thr-183 and Tyr-185, which activates
CC       the enzyme.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. MAP kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB005663; BAA85875.1; -; mRNA.
DR   IPI; IPI00129682; -.
DR   RefSeq; NP_057909.1; NM_016700.4.
DR   UniGene; Mm.21495; -.
DR   ProteinModelPortal; Q91Y86; -.
DR   SMR; Q91Y86; 7-364.
DR   IntAct; Q91Y86; 5.
DR   MINT; MINT-1204569; -.
DR   STRING; Q91Y86; -.
DR   PhosphoSite; Q91Y86; -.
DR   PRIDE; Q91Y86; -.
DR   Ensembl; ENSMUST00000111945; ENSMUSP00000107576; ENSMUSG00000021936.
DR   GeneID; 26419; -.
DR   KEGG; mmu:26419; -.
DR   UCSC; uc007szt.1; mouse.
DR   CTD; 26419; -.
DR   MGI; MGI:1346861; Mapk8.
DR   GeneTree; ENSGT00550000074271; -.
DR   HOVERGEN; HBG014652; -.
DR   OrthoDB; EOG48SGT3; -.
DR   PhylomeDB; Q91Y86; -.
DR   BRENDA; 2.7.11.24; 244.
DR   BindingDB; Q91Y86; -.
DR   NextBio; 304433; -.
DR   ArrayExpress; Q91Y86; -.
DR   Bgee; Q91Y86; -.
DR   CleanEx; MM_MAPK8; -.
DR   Genevestigator; Q91Y86; -.
DR   GermOnline; ENSMUSG00000021936; Mus musculus.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004705; F:JUN kinase activity; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0031558; P:induction of apoptosis in response to chemical stimulus; IGI:MGI.
DR   GO; GO:0001503; P:ossification; IMP:MGI.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IMP:MGI.
DR   GO; GO:2000017; P:positive regulation of determination of dorsal identity; IDA:MGI.
DR   GO; GO:0046686; P:response to cadmium ion; IGI:MGI.
DR   InterPro; IPR008351; JNK_MAPK.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR003527; MAP_kinase_CS.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01772; JNKMAPKINASE.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS01351; MAPK; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    384       Mitogen-activated protein kinase 8.
FT                                /FTId=PRO_0000186263.
FT   DOMAIN       26    321       Protein kinase.
FT   NP_BIND      32     40       ATP (By similarity).
FT   MOTIF       183    185       TXY.
FT   ACT_SITE    151    151       Proton acceptor (By similarity).
FT   BINDING      55     55       ATP (By similarity).
FT   MOD_RES     155    155       Phosphoserine (By similarity).
FT   MOD_RES     183    183       Phosphothreonine.
FT   MOD_RES     185    185       Phosphotyrosine.
FT   MOD_RES     255    255       Phosphothreonine (By similarity).
FT   MOD_RES     258    258       Phosphothreonine (By similarity).
FT   MOD_RES     259    259       Phosphotyrosine (By similarity).
FT   MOD_RES     308    308       N6-acetyllysine (By similarity).
FT   MOD_RES     357    357       Phosphotyrosine (By similarity).
FT   MOD_RES     367    367       Phosphothreonine (By similarity).
FT   MOD_RES     377    377       Phosphoserine.
SQ   SEQUENCE   384 AA;  44229 MW;  A7320EF933E9CF85 CRC64;
     MSRSKRDNNF YSVEIGDSTF TVLKRYQNLK PIGSGAQGIV CAAYDAILER NVAIKKLSRP
     FQNQTHAKRA YRELVLMKCV NHKNIIGLLN VFTPQKSLEE FQDVYIVMEL MDANLCQVIQ
     MELDHERMSY LLYQMLCGIK HLHSAGIIHR DLKPSNIVVK SDCTLKILDF GLARTAGTSF
     MMTPYVVTRY YRAPEVILGM GYKENVDLWS VGCIMGEMVC HKILFPGRDY IDQWNKVIEQ
     LGTPCPEFMK KLQPTVRTYV ENRPKYAGYS FEKLFPDVLF PADSEHNKLK ASQARDLLSK
     MLVIDASKRI SVDEALQHPY INVWYDPSEA EAPPPKIPDK QLDEREHTIE EWKELIYKEV
     MDLEERTKNG VIRGQPSPLA QVQQ
//
ID   WASL_MOUSE              Reviewed;         501 AA.
AC   Q91YD9;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Neural Wiskott-Aldrich syndrome protein;
DE            Short=N-WASP;
GN   Name=Wasl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=21443407; PubMed=11559594; DOI=10.1093/embo-reports/kve197;
RA   Lommel S., Benesch S., Rottner K., Franz T., Wehland J., Kuehn R.;
RT   "Actin pedestal formation by enteropathogenic Escherichia coli and
RT   intracellular motility of Shigella flexneri are abolished in N-WASP-
RT   defective cells.";
RL   EMBO Rep. 2:850-857(2001).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-253.
RX   PubMed=12871950; DOI=10.1074/jbc.M302177200;
RA   Suetsugu S., Takenawa T.;
RT   "Translocation of N-WASP by nuclear localization and export signals
RT   into the nucleus modulates expression of HSP90.";
RL   J. Biol. Chem. 278:42515-42523(2003).
RN   [3]
RP   INTERACTION WITH DNMBP.
RX   PubMed=14506234; DOI=10.1074/jbc.M308104200;
RA   Salazar M.A., Kwiatkowski A.V., Pellegrini L., Cestra G., Butler M.H.,
RA   Rossman K.L., Serna D.M., Sondek J., Gertler F.B., De Camilli P.;
RT   "Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology
RT   domains, links dynamin to regulation of the actin cytoskeleton.";
RL   J. Biol. Chem. 278:49031-49043(2003).
RN   [4]
RP   INTERACTION WITH PRPF40A.
RX   PubMed=14697212; DOI=10.1016/j.bbrc.2003.11.139;
RA   Mizutani K., Suetsugu S., Takenawa T.;
RT   "FBP11 regulates nuclear localization of N-WASP and inhibits N-WASP-
RT   dependent microspike formation.";
RL   Biochem. Biophys. Res. Commun. 313:468-474(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253, AND MASS
RP   SPECTROMETRY.
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Regulates actin polymerization by stimulating the actin-
CC       nucleating activity of the Arp2/3 complex (By similarity). Binds
CC       to HSF1/HSTF1 and forms a complex on heat shock promoter elements
CC       (HSE) that negatively regulates HSP90 expression.
CC   -!- SUBUNIT: Interacts with NOSTRIN (By similarity). Binds actin and
CC       the Arp2/3 complex. Interacts with CDC42. Binds to SH3 domains of
CC       GRB2. Interacts with the C-terminal SH3 domain of DNMBP. Interacts
CC       with the WW domains of PRPF40A/FBP11.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus.
CC       Note=Preferentially localized in the cytoplasm when phosphorylated
CC       and in the nucleus when unphosphorylated.
CC   -!- SIMILARITY: Contains 1 CRIB domain.
CC   -!- SIMILARITY: Contains 1 WH1 domain.
CC   -!- SIMILARITY: Contains 2 WH2 domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ318416; CAC69994.1; -; mRNA.
DR   IPI; IPI00468996; -.
DR   RefSeq; NP_082735.2; NM_028459.2.
DR   UniGene; Mm.1574; -.
DR   PDB; 3M3N; X-ray; 7.00 A; W=399-444.
DR   PDBsum; 3M3N; -.
DR   ProteinModelPortal; Q91YD9; -.
DR   SMR; Q91YD9; 26-147, 192-250, 397-446.
DR   DIP; DIP-29788N; -.
DR   IntAct; Q91YD9; 4.
DR   STRING; Q91YD9; -.
DR   PhosphoSite; Q91YD9; -.
DR   PRIDE; Q91YD9; -.
DR   Ensembl; ENSMUST00000031695; ENSMUSP00000031695; ENSMUSG00000029684.
DR   GeneID; 73178; -.
DR   KEGG; mmu:73178; -.
DR   CTD; 73178; -.
DR   MGI; MGI:1920428; Wasl.
DR   GeneTree; ENSGT00550000074443; -.
DR   HOGENOM; HBG717283; -.
DR   HOVERGEN; HBG000222; -.
DR   InParanoid; Q91YD9; -.
DR   OMA; SKKCCGV; -.
DR   OrthoDB; EOG4JM7Q1; -.
DR   PhylomeDB; Q91YD9; -.
DR   ArrayExpress; Q91YD9; -.
DR   Bgee; Q91YD9; -.
DR   CleanEx; MM_WASL; -.
DR   Genevestigator; Q91YD9; -.
DR   GermOnline; ENSMUSG00000029684; Mus musculus.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; IC:MGI.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005083; F:small GTPase regulator activity; IEA:InterPro.
DR   GO; GO:0045010; P:actin nucleation; TAS:MGI.
DR   GO; GO:0008154; P:actin polymerization or depolymerization; IEA:InterPro.
DR   GO; GO:0006461; P:protein complex assembly; IEA:InterPro.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0009617; P:response to bacterium; IMP:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR000697; EVH1.
DR   InterPro; IPR000095; PAK_box_Rho-bd.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR011026; WASP_C.
DR   InterPro; IPR003124; WH2_actin-bd.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00786; PBD; 1.
DR   Pfam; PF00568; WH1; 1.
DR   Pfam; PF02205; WH2; 2.
DR   SMART; SM00285; PBD; 1.
DR   SMART; SM00461; WH1; 1.
DR   SMART; SM00246; WH2; 2.
DR   SUPFAM; SSF47912; WASP_C; 2.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS50229; WH1; 1.
DR   PROSITE; PS51082; WH2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Cytoplasm; Cytoskeleton; Nucleus;
KW   Phosphoprotein; Repeat; Transcription; Transcription regulation.
FT   CHAIN         1    501       Neural Wiskott-Aldrich syndrome protein.
FT                                /FTId=PRO_0000189001.
FT   DOMAIN       31    138       WH1.
FT   DOMAIN      200    213       CRIB.
FT   DOMAIN      401    418       WH2 1.
FT   DOMAIN      429    446       WH2 2.
FT   COMPBIAS    274    385       Pro-rich.
FT   COMPBIAS    482    501       Asp-rich.
FT   MOD_RES     253    253       Phosphotyrosine.
FT   MOD_RES     480    480       Phosphoserine (By similarity).
FT   MOD_RES     481    481       Phosphoserine (By similarity).
FT   MUTAGEN     253    253       Y->E: No effect on phosphorylation.
FT                                Protein preferentially localized in
FT                                cytoplasm.
FT   MUTAGEN     253    253       Y->F: Abolishes phosphorylation. Protein
FT                                preferentially localized in nucleus.
SQ   SEQUENCE   501 AA;  54274 MW;  F5ABF44DF9A9F716 CRC64;
     MSSGQQPPRR VTNVGSLLLT PQENESLFSF LGKKCVTMSS AVVQLYAADR NCMWAKKCSG
     VACLVKDNPQ RSYFLRIFDI KDGKLLWEQE LYNNFVYNSP RGYFHTFAGD TCQVALNFAN
     EEEAKKFRKA VTDLLGRRQR KSEKRRDAPN GPNLPMATVD IKNPEITTNR FYGSQVNNIS
     HTKEKKKGKA KKKRLTKADI GTPSNFQHIG HVGWDPNTGF DLNNLDPELK NLFDMCGISE
     AQLKDRETSK VIYDFIEKTG GVEAVKNELR RQAPPPPPPS RGGPPPPPPP PHSSGPPPPP
     ARGRGAPPPP PSRAPTAAPP PPPPSRPGVV VPPPPPNRMY PPPPPALPSS APSGPPPPPP
     PSMAGSTAPP PPPPPPPPPG PPPPPGLPSD GDHQVPAPSG NKAALLDQIR EGAQLKKVEQ
     NSRPVSCSGR DALLDQIRQG IQLKSVSDGQ ESTPPTPAPT SGIVGALMEV MQKRSKAIHS
     SDEDEDDDDE EDFEDDDEWE D
//
ID   RBM5_MOUSE              Reviewed;         815 AA.
AC   Q91YE7; Q3UZ19; Q99KV9;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=RNA-binding protein 5;
DE   AltName: Full=Putative tumor suppressor LUCA15;
DE   AltName: Full=RNA-binding motif protein 5;
GN   Name=Rbm5; Synonyms=Luca15;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Heath E., Morgan G.T., Sablitzky F.;
RT   "Def-3 defines a novel sub-nuclear domain and co-localises with
RT   LUCA15.";
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Fetal kidney, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, Czech II, and FVB/N;
RC   TISSUE=Eye, Fetal brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69 AND SER-621, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-624, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 484-491 IN COMPLEX WITH B2M
RP   AND H2-K1.
RX   PubMed=16761314; DOI=10.1002/eji.200635895;
RA   Auphan-Anezin N., Mazza C., Guimezanes A., Barrett-Wilt G.A.,
RA   Montero-Julian F., Roussel A., Hunt D.F., Malissen B.,
RA   Schmitt-Verhulst A.-M.;
RT   "Distinct orientation of the alloreactive monoclonal CD8 T cell
RT   activation program by three different peptide/MHC complexes.";
RL   Eur. J. Immunol. 36:1856-1866(2006).
CC   -!- FUNCTION: Component of the spliceosome A complex. Regulates
CC       alternative splicing of a number of mRNAs. May modulate splice
CC       site pairing after recruitment of the U1 and U2 snRNPs to the 5'
CC       and 3' splice sites of the intron. May both positively and
CC       negatively regulate aopotosis by regulating the alternative
CC       splicing of several genes involved in this process, including FAS
CC       and CASP2/caspase-2. In the case of FAS, promotes production of a
CC       soluble form of FAS that inhibits apoptosis. In the case of
CC       CASP2/caspase-2, promotes production of a catalytically active
CC       form of CASP2/Caspase-2 that induces apoptosis (By similarity).
CC   -!- SUBUNIT: Component of the spliceosome A complex (also known as the
CC       prespliceosome). Appears to dissociate from the spliceosome upon
CC       formation of the spliceosome B complex (also known as the
CC       precatalytic spliceosome), in which the heterotrimeric U4/U6.U5
CC       snRNPs are bound. Interacts with U2AF2; this interaction is
CC       direct. Also interacts with ACIN1, PRPF8, SFRS3, SNRPB, SNRPN,
CC       SNRNP70 and SNRNP200; these interactions may be indirect (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q91YE7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q91YE7-2; Sequence=VSP_021003;
CC   -!- SIMILARITY: Belongs to the RBM5/RBM10 family.
CC   -!- SIMILARITY: Contains 1 C2H2-type zinc finger.
CC   -!- SIMILARITY: Contains 1 G-patch domain.
CC   -!- SIMILARITY: Contains 1 RanBP2-type zinc finger.
CC   -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ309168; CAC69136.1; -; mRNA.
DR   EMBL; AK134183; BAE22042.1; -; mRNA.
DR   EMBL; AK146880; BAE27501.1; -; mRNA.
DR   EMBL; BC003988; AAH03988.1; -; mRNA.
DR   EMBL; BC023854; AAH23854.1; -; mRNA.
DR   EMBL; BC031899; AAH31899.1; -; mRNA.
DR   EMBL; BC043058; AAH43058.1; -; mRNA.
DR   EMBL; BC054729; AAH54729.1; -; mRNA.
DR   IPI; IPI00130160; -.
DR   IPI; IPI00798508; -.
DR   RefSeq; NP_683732.1; NM_148930.3.
DR   UniGene; Mm.259197; -.
DR   PDB; 2CLV; X-ray; 1.90 A; C/M=484-491.
DR   PDB; 2OL3; X-ray; 2.90 A; P=484-491.
DR   PDBsum; 2CLV; -.
DR   PDBsum; 2OL3; -.
DR   ProteinModelPortal; Q91YE7; -.
DR   SMR; Q91YE7; 94-181, 229-318.
DR   STRING; Q91YE7; -.
DR   PhosphoSite; Q91YE7; -.
DR   PRIDE; Q91YE7; -.
DR   Ensembl; ENSMUST00000035199; ENSMUSP00000035199; ENSMUSG00000032580.
DR   GeneID; 83486; -.
DR   KEGG; mmu:83486; -.
DR   UCSC; uc009rmx.1; mouse.
DR   CTD; 83486; -.
DR   MGI; MGI:1933204; Rbm5.
DR   GeneTree; ENSGT00510000046476; -.
DR   HOGENOM; HBG713245; -.
DR   HOVERGEN; HBG000318; -.
DR   InParanoid; Q91YE7; -.
DR   OMA; YTQYSQD; -.
DR   OrthoDB; EOG4VT5WV; -.
DR   PhylomeDB; Q91YE7; -.
DR   NextBio; 350596; -.
DR   ArrayExpress; Q91YE7; -.
DR   Bgee; Q91YE7; -.
DR   CleanEx; MM_RBM5; -.
DR   Genevestigator; Q91YE7; -.
DR   GermOnline; ENSMUSG00000032580; Mus musculus.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0043065; P:positive regulation of apoptosis; ISS:UniProtKB.
DR   GO; GO:0000381; P:regulation of alternative nuclear mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:0000245; P:spliceosome assembly; ISS:UniProtKB.
DR   InterPro; IPR000467; G_patch.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   Pfam; PF01585; G-patch; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF00641; zf-RanBP; 1.
DR   SMART; SM00443; G_patch; 1.
DR   SMART; SM00360; RRM; 2.
DR   SMART; SM00355; ZnF_C2H2; 1.
DR   SMART; SM00547; ZnF_RBZ; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
DR   PROSITE; PS50102; RRM; 2.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
DR   PROSITE; PS50199; ZF_RANBP2_2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; FALSE_NEG.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Apoptosis;
KW   Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW   Phosphoprotein; Repeat; RNA-binding; Spliceosome; Zinc; Zinc-finger.
FT   CHAIN         1    815       RNA-binding protein 5.
FT                                /FTId=PRO_0000253050.
FT   DOMAIN       98    178       RRM 1.
FT   DOMAIN      231    315       RRM 2.
FT   DOMAIN      743    789       G-patch.
FT   ZN_FING     181    210       RanBP2-type.
FT   ZN_FING     647    672       C2H2-type.
FT   REGION      321    809       Required for interaction with U2AF2 (By
FT                                similarity).
FT   REGION      452    535       Sufficient for interaction with ACIN1,
FT                                PRPF8, SFRS3, SNRPB, SNRPN, SNRNP70 and
FT                                SNRNP200 (By similarity).
FT   COMPBIAS      6     71       Arg-rich.
FT   COMPBIAS    462    497       Tyr-rich.
FT   MOD_RES      59     59       Phosphoserine (By similarity).
FT   MOD_RES      69     69       Phosphoserine.
FT   MOD_RES      78     78       Phosphoserine.
FT   MOD_RES     542    542       N6-acetyllysine (By similarity).
FT   MOD_RES     621    621       Phosphoserine.
FT   MOD_RES     624    624       Phosphoserine.
FT   MOD_RES     712    712       Phosphotyrosine (By similarity).
FT   VAR_SEQ     455    455       Missing (in isoform 2).
FT                                /FTId=VSP_021003.
FT   CONFLICT    272    272       Q -> K (in Ref. 2; BAE22042).
FT   CONFLICT    693    693       E -> G (in Ref. 2; BAE22042).
FT   CONFLICT    726    726       F -> L (in Ref. 2; BAE22042).
FT   CONFLICT    798    798       S -> P (in Ref. 2; BAE22042).
SQ   SEQUENCE   815 AA;  92311 MW;  BCDADD4A8FB4EAC9 CRC64;
     MGSDKRVSRT ERSGRYGSII DRDDRDERES RSRRRDSDYK RSSDDRRGDR YDDYRDYDSP
     ERERERRNSD RSEDGYHSDG DYGEHDYRHD ISDERESKTI MLRGLPITIT ESDIREMMES
     FEGPQPADVR LMKRKTGVSR GFAFVEFYHL QDATSWMEAN QKKLVIQGKH IAMHYSNPRP
     KFEDWLCNKC CLNNFRKRLK CFRCGADKFD SEQEVPPGTT ESAQSVDYYC DTIILRNIAP
     HTVVDSIMTA LSPYASLAVN NIRLIKDKQT QQNRGFAFVQ LSSAMDASQL LQILQSLHPP
     LKIDGKTIGV DFAKSARKDL VLPDGNRVSA FSVASTAIAA AQWSSTQSQS GEGGSVDYSY
     MQPGQDGYTQ YTQYSQDYQQ FYQQQAGGLE SDTSATSGTT VTTTSAAVVS QSPQLYNQTS
     NPPGSPTEEA QPSTSTSTQA PAASPTGVVP GTKYAVPDTS TYQYDESSGY YYDPTTGLYY
     DPNSQYYYNS LTQQYLYWDG EKETYVPAAE ASSNQQTGLP STKEGKEKKE KPKSKTAQQI
     AKDMERWAKS LNKQKENFKN SFQPVNSLRE EERRESAAAD AGFALFEKKG ALAERQQLLP
     ELVRNGDEEN PLKRGLVAAY SGDSDNEEEL VERLESEEEK LADWKKMACL LCRRQFPNRD
     ALVRHQQLSD LHKQNMDIYR RSRLSEQELE ALELREREMK YRDRAAERRE KYGIPEPPEP
     KRKKQFDAGT VNYEQPTKDG IDHSNIGNKM LQAMGWREGS GLGRKCQGIT APIEAQVRLK
     GAGLGAKGSA YGLSGADSYK DAVRKAMFAR FTEME
//
ID   SYNP2_MOUSE             Reviewed;        1087 AA.
AC   Q91YE8; Q8C592;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 2.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Synaptopodin-2;
DE   AltName: Full=Myopodin;
GN   Name=Synpo2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 2), TISSUE SPECIFICITY, SUBCELLULAR
RP   LOCATION, FUNCTION, AND INTERACTION WITH ACTIN.
RC   STRAIN=129S6/SvEvTac; TISSUE=Muscle;
RX   MEDLINE=21541543; PubMed=11673475; DOI=10.1083/jcb.200012039;
RA   Weins A., Schwarz K., Faul C., Barisoni L., Linke W.A., Mundel P.;
RT   "Differentiation and stress-dependent nuclear-cytoplasmic
RT   redistribution of myopodin, a novel actin bundling protein.";
RL   J. Cell Biol. 155:393-404(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 894-1078 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J; TISSUE=Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Has an actin-binding and actin-bundling activity.
CC   -!- SUBUNIT: Interacts with actin.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between
CC       the nucleus and the cytoplasm in a differentiation-dependent and
CC       stress-induced fashion. Localizes to the Z-disk in mature striated
CC       muscle (By similarity). The nuclear export is XPO1-dependent.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q91YE8-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q91YE8-2; Sequence=VSP_011493, VSP_011494;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, heart, colon,
CC       stomach, uterus and lung. Expression is restricted to muscle cell
CC       layers in colon, uterus and stomach.
CC   -!- SIMILARITY: Belongs to the synaptopodin family.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AJ306625; CAC67798.1; -; mRNA.
DR   EMBL; AC121315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC121540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK079194; BAC37575.1; -; mRNA.
DR   IPI; IPI00130162; -.
DR   IPI; IPI00831458; -.
DR   UniGene; Mm.34359; -.
DR   ProteinModelPortal; Q91YE8; -.
DR   SMR; Q91YE8; 2-89.
DR   STRING; Q91YE8; -.
DR   PhosphoSite; Q91YE8; -.
DR   PRIDE; Q91YE8; -.
DR   Ensembl; ENSMUST00000051443; ENSMUSP00000051570; ENSMUSG00000050315.
DR   MGI; MGI:2153070; Synpo2.
DR   eggNOG; roNOG13000; -.
DR   GeneTree; ENSGT00530000063754; -.
DR   HOVERGEN; HBG079226; -.
DR   OrthoDB; EOG4TB4B0; -.
DR   PhylomeDB; Q91YE8; -.
DR   ArrayExpress; Q91YE8; -.
DR   Bgee; Q91YE8; -.
DR   CleanEx; MM_SYNPO2; -.
DR   Genevestigator; Q91YE8; -.
DR   GermOnline; ENSMUSG00000050315; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Cytoplasm; Nucleus;
KW   Phosphoprotein.
FT   CHAIN         1   1087       Synaptopodin-2.
FT                                /FTId=PRO_0000187674.
FT   DOMAIN        6     88       PDZ.
FT   COMPBIAS    390    395       Poly-Arg.
FT   COMPBIAS    406    415       Poly-Glu.
FT   COMPBIAS    591    650       Pro-rich.
FT   COMPBIAS    745    859       Pro-rich.
FT   MOD_RES     885    885       Phosphothreonine (By similarity).
FT   VAR_SEQ       1    330       Missing (in isoform 2).
FT                                /FTId=VSP_011493.
FT   VAR_SEQ     331    347       SGKDQSRPHKHRARHAR -> MIPCSHQFSTICVLSPG
FT                                (in isoform 2).
FT                                /FTId=VSP_011494.
FT   CONFLICT    894    894       Q -> E (in Ref. 3; BAC37575).
FT   CONFLICT   1067   1067       K -> E (in Ref. 3; BAC37575).
SQ   SEQUENCE   1087 AA;  116527 MW;  BA2BAE2797947131 CRC64;
     MGTGDFICIS MTGGAPWGFR LQGGKEEQQP LQVAKIRSQS KASGSGLREG DEVVSINGNP
     CADLTYPEVI KLMEGITDSL HLLVKRPSSG TSETLDSESE TTNHQHLTHE GPMESTTLQI
     QQATETQSED FFLAPVQTKV PLTEDQSNAW GYAECPKEEQ APPMLGSQEG HLVEEVILRQ
     KAEAGQPGHV VELQLSLSKE RHQCTSGPIV TLQGNDKSTS PDPDWSSQLE RTVHINSIPA
     PEKADTSLTS STSSGRELRV IQGRDPGGAG LPQVEVILDC SDRLKAEECR LQTGRGCVAS
     PVEGGRSEAP PSLVSFAVSS EGTEHGEDQR SGKDQSRPHK HRARHARLRR SESLSEKQVK
     EAKSKCKSIA LLLTDAPNPN SKGVLMFKKR RRRARKYTLV SYGTGELERE EEEEEDQEAG
     DKDEISEVAF LGTSESEVDE ELLSDVDDNT QVVNFDWDSG LVDIEKRLNR GDKMEMLPDT
     TGKGALMFAK RRERMEQFTA QNEEEKTGGM AGGGPDALQT DGLRTMTSYQ RKEESVRMQS
     SVSESSFQMG RSLASVPQQN GFSGVSETAG AQRMFPMNRT AKPFLGSMNQ PAAPFSPTRS
     VTSPISDFPA PPPYSAVSPP PEAFSRGVSS PVAGPAQPPP WPQPAPWSQP AFYDSSEQIA
     SRDERIAVPA KRTGILQEAK RRGTTKPMFT FKETKVSPNP ELLSLLQNAE GKRGTGGDSG
     PEEDYLSLGA EACNFMQSSA KQKTPPPVAP KPAVKSPSSS QPVAPVSPVW SPGVAPAQRP
     AFSTSNPPNP PQVTAVSSIK IAQPAAPPAR PASALNLAGP FKGPQAVVVS HNYTPKPSAP
     TPLVNAAPAG AGGPSNELPG MSGKGAQLFA KRQSRMEKYV VDSDTVQAHT VRAQSPTPSL
     PASWKYSSNV RAPPPVAYNP IHSPSYPLAA IKSQPPGAQA SKTSKKKGKK PLNTLDVMKH
     QPYQLNASLF TFQPPDSKDG LPQKSTVKVS SAPAMKQALP PRQANVGSPT NAQASSVYSV
     PAYTSQPNFF AAEATSPVSA SPVPVSVPTS PKQESTSTSY FVAPRPKFSA KKSGVTVQVW
     KPSVVEE
//
ID   ATG13_MOUSE             Reviewed;         516 AA.
AC   Q91YI1; A2AH18; Q80TU9;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Autophagy-related protein 13;
GN   Name=Atg13; Synonyms=D2Ertd391e, Kiaa0652;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Dendritic cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
RP   SPLICING.
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=129, and FVB/N; TISSUE=Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 91-516 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   FUNCTION, INTERACTION WITH ULK1 AND RB1CC1, PHOSPHORYLATION, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=19258318; DOI=10.1074/jbc.M900573200;
RA   Ganley I.G., Lam du H., Wang J., Ding X., Chen S., Jiang X.;
RT   "ULK1.ATG13.FIP200 complex mediates mTOR signaling and is essential
RT   for autophagy.";
RL   J. Biol. Chem. 284:12297-12305(2009).
RN   [8]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=19211835; DOI=10.1091/mbc.E08-12-1248;
RA   Hosokawa N., Hara T., Kaizuka T., Kishi C., Takamura A., Miura Y.,
RA   Iemura S., Natsume T., Takehana K., Yamada N., Guan J.L., Oshiro N.,
RA   Mizushima N.;
RT   "Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200
RT   complex required for autophagy.";
RL   Mol. Biol. Cell 20:1981-1991(2009).
CC   -!- FUNCTION: Autophagy factor required for autophagosome formation.
CC       Target of the TOR kinase signaling pathway that regulates
CC       autophagy through the control of the phosphorylation status of
CC       ATG13 and ULK1, and the regulation of the ATG13-ULK1-RB1CC1
CC       complex.
CC   -!- SUBUNIT: Part of a complex consisting of ATG13, ULK1 and RB1CC1.
CC       Interacts with ATG101 (By similarity). Interacts with ULK1 (via C-
CC       terminus) (By similarity). Interacts with ULK2 (via C-terminus)
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Preautophagosomal
CC       structure. Note=Under starvation conditions, is localized to
CC       puncate structures primarily representing the isolation membrane
CC       that sequesters a portion of the cytoplasm resulting in the
CC       formation of an autophagosome.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q91YI1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q91YI1-2; Sequence=VSP_034922;
CC   -!- PTM: Phosphorylated by ULK1 and ULK2 (By similarity).
CC       Phosphorylated under nutrient-rich conditions; dephosphorylated
CC       during starvation or following treatment with rapamycin.
CC   -!- SIMILARITY: Belongs to the ATG13 metazoan family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65621.3; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA;
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DR   EMBL; AK149672; BAE29016.1; -; mRNA.
DR   EMBL; AK171206; BAE42312.1; -; mRNA.
DR   EMBL; AK171440; BAE42453.1; -; mRNA.
DR   EMBL; AL714023; CAM14512.1; -; Genomic_DNA.
DR   EMBL; AL714023; CAM14513.1; -; Genomic_DNA.
DR   EMBL; CH466519; EDL27574.1; -; Genomic_DNA.
DR   EMBL; BC016669; AAH16669.1; -; mRNA.
DR   EMBL; BC023673; AAH23673.1; -; mRNA.
DR   EMBL; BC023712; AAH23712.1; -; mRNA.
DR   EMBL; BC033419; AAH33419.1; -; mRNA.
DR   EMBL; AK122339; BAC65621.3; ALT_SEQ; Transcribed_RNA.
DR   IPI; IPI00130212; -.
DR   IPI; IPI00403320; -.
DR   RefSeq; NP_663503.1; NM_145528.2.
DR   UniGene; Mm.28492; -.
DR   Ensembl; ENSMUST00000028678; ENSMUSP00000028678; ENSMUSG00000027244.
DR   GeneID; 51897; -.
DR   KEGG; mmu:51897; -.
DR   UCSC; uc008kwn.1; mouse.
DR   CTD; 51897; -.
DR   MGI; MGI:1196429; Atg13.
DR   eggNOG; roNOG07256; -.
DR   GeneTree; ENSGT00390000007055; -.
DR   HOGENOM; HBG715441; -.
DR   InParanoid; Q91YI1; -.
DR   OMA; GEGFQTV; -.
DR   OrthoDB; EOG4HMJ99; -.
DR   NextBio; 308208; -.
DR   ArrayExpress; Q91YI1; -.
DR   Bgee; Q91YI1; -.
DR   Genevestigator; Q91YI1; -.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0000407; C:pre-autophagosomal structure; IDA:UniProtKB.
DR   GO; GO:0070969; C:ULK1-ATG13-FIP200 complex; IPI:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0000045; P:autophagic vacuole assembly; IMP:UniProtKB.
DR   InterPro; IPR018731; Autophagy-rel_p13.
DR   Pfam; PF10033; ATG13; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Autophagy; Cytoplasm;
KW   Phosphoprotein.
FT   CHAIN         1    516       Autophagy-related protein 13.
FT                                /FTId=PRO_0000345151.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     360    360       Phosphoserine.
FT   VAR_SEQ     263    299       Missing (in isoform 2).
FT                                /FTId=VSP_034922.
SQ   SEQUENCE   516 AA;  56441 MW;  04B4E49BB19449F2 CRC64;
     METELSSQDR KDLDKFIKFF ALKTVQVIVQ ARLGEKICTR SSSSPTGSDW FNLAIKDIPE
     VTHEAKKALS GQLPAVGRSM CVEISLKTSE GDSMELEIWC LEMNEKCDKE IKVSYTVYNR
     LSLLLKSLLA ITRVTPAYRL SRKQGHEYVI LYRIYFGEVQ LNGLGEGFQT VRVGTVGTPV
     GTLTLSCAYR INLAFMSTRQ FERTPPIMGI IIDHFVDRPY PSSSPMHPCN YRTAEDAGVA
     YPSVEDSQEV CTTSFSTSPP SQLSSSRLSY QPAVLGLGSA DLAYPVVFTA GLNTTHAHQL
     MVPGKEGGVT LAPSHPTHGA QADPERLVMH MPSDGTHCAA TPSSSEDTET VSNSSEGRAS
     PHDILETIFV RKVGAFVNKP INQVTVTSLD IPFAMFAPKN LELEDADPMV NPPESPETTS
     PLHGSLHSDG SSGGSGGSTH DDFVMIDFKP AFSKDDILPM DLGTFYREFQ NPPQLSSLSI
     DFGAQSMAED LDSLPEKLAV HEKNVREFDA FVETLQ
//
ID   GRLF1_MOUSE             Reviewed;        1499 AA.
AC   Q91YM2; Q3UGY1; Q69ZC4;
DT   04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Glucocorticoid receptor DNA-binding factor 1;
GN   Name=Grlf1; Synonyms=Kiaa1722;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 163-1499.
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1105, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1105, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1087 AND TYR-1105, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-773 AND SER-980, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Represses transcription of the glucocorticoid receptor
CC       by binding to the cis-acting regulatory sequence 5'-
CC       GAGAAAAGAAACTGGAGAAACTC-3'. May participate in the regulation of
CC       retinal development and degeneration. May transduce signals from
CC       p21-ras to the nucleus, acting via the ras GTPase-activating
CC       protein (GAP). May also act as a tumor suppressor (By similarity).
CC   -!- SUBUNIT: Interacts with p120GAP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- PTM: Tyrosine phosphorylated (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 4 FF domains.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
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DR   EMBL; AK147326; BAE27848.1; -; mRNA.
DR   EMBL; AK147688; BAE28076.1; -; mRNA.
DR   EMBL; AK173242; BAD32520.1; -; Transcribed_RNA.
DR   IPI; IPI00480321; -.
DR   RefSeq; NP_766327.3; NM_172739.4.
DR   UniGene; Mm.28646; -.
DR   UniGene; Mm.400358; -.
DR   ProteinModelPortal; Q91YM2; -.
DR   SMR; Q91YM2; 13-249, 1242-1437.
DR   STRING; Q91YM2; -.
DR   PhosphoSite; Q91YM2; -.
DR   PRIDE; Q91YM2; -.
DR   Ensembl; ENSMUST00000075845; ENSMUSP00000075242; ENSMUSG00000058230.
DR   GeneID; 232906; -.
DR   KEGG; mmu:232906; -.
DR   UCSC; uc009fhw.1; mouse.
DR   CTD; 232906; -.
DR   MGI; MGI:1929494; Grlf1.
DR   GeneTree; ENSGT00600000084250; -.
DR   HOGENOM; HBG444653; -.
DR   HOVERGEN; HBG051844; -.
DR   InParanoid; Q91YM2; -.
DR   OMA; TIRNINK; -.
DR   OrthoDB; EOG4DZ1TC; -.
DR   NextBio; 381321; -.
DR   ArrayExpress; Q91YM2; -.
DR   Bgee; Q91YM2; -.
DR   CleanEx; MM_GRLF1; -.
DR   Genevestigator; Q91YM2; -.
DR   GermOnline; ENSMUSG00000058230; Mus musculus.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0005096; F:GTPase activator activity; TAS:MGI.
DR   GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; TAS:MGI.
DR   GO; GO:0043116; P:negative regulation of vascular permeability; IMP:MGI.
DR   GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR   GO; GO:0008360; P:regulation of cell shape; IDA:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR002713; FF_domain.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF01846; FF; 1.
DR   Pfam; PF00071; Ras; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00441; FF; 4.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; GTPase activation; Nucleus; Phosphoprotein; Repeat;
KW   Repressor; Transcription; Transcription regulation; Tumor suppressor.
FT   CHAIN         1   1499       Glucocorticoid receptor DNA-binding
FT                                factor 1.
FT                                /FTId=PRO_0000056731.
FT   DOMAIN      270    327       FF 1.
FT   DOMAIN      369    422       FF 2.
FT   DOMAIN      429    483       FF 3.
FT   DOMAIN      485    539       FF 4.
FT   DOMAIN     1249   1436       Rho-GAP.
FT   COMPBIAS   1440   1487       Pro-rich.
FT   MOD_RES     589    589       Phosphoserine (By similarity).
FT   MOD_RES     685    685       Phosphothreonine (By similarity).
FT   MOD_RES     773    773       Phosphoserine.
FT   MOD_RES     963    963       Phosphothreonine (By similarity).
FT   MOD_RES     970    970       Phosphoserine (By similarity).
FT   MOD_RES     975    975       Phosphoserine (By similarity).
FT   MOD_RES     980    980       Phosphoserine.
FT   MOD_RES    1072   1072       Phosphoserine (By similarity).
FT   MOD_RES    1087   1087       Phosphotyrosine.
FT   MOD_RES    1105   1105       Phosphotyrosine.
FT   MOD_RES    1134   1134       Phosphoserine (By similarity).
FT   MOD_RES    1150   1150       Phosphoserine (By similarity).
FT   MOD_RES    1179   1179       Phosphoserine (By similarity).
FT   MOD_RES    1195   1195       Phosphoserine (By similarity).
SQ   SEQUENCE   1499 AA;  170393 MW;  7E13EC38257CE950 CRC64;
     MMMARKQDVR IPTYNISVVG LSGTEKEKGQ CGIGKSCLCN RFVRPSADEF HLDHTSVLST
     SDFGGRVVNN DHFLYWGEVS RSLEDCVECK MHIVEQTEFI DDQTFQPHRS TALQPYIKRA
     AATKLASAEK LMYFCTDQLG LEQDFEQKQM PDGKLLVDGF LLGIDVSRGM NRNFDDQLKF
     VSNLYNQLAK TKKPIVVVLT KCDEGVERYI RDAHTFALSK KNLQVVETSA RSNVNVDLAF
     STLVQLIDKS RGKTKIIPYF EALKQQSQQI ATAKDKYEWL VSRIVKNHNE NWPSVSRKMQ
     ASPEYQDYVY LEGTQKAKKL FLQHIHRLKH EHIERRRKLY LAALPLAFEA LIPNLDEVDH
     LSCIKAKKLL ETKPEFLKWF VVLEETPWDA TSHIDNMENE RIPFDLMDTV PAEQLYETHL
     EKLRNERKRA EMRRAFKENL ETSPFITPGK PWEEARSFIM NEDFYQWLEE SVYMDIYGKH
     QKQIIDRAKE EFQELLLEYS ELFYELELDA KPSKEKMGVI QDVLGEEQRF KALQKLQAER
     DALILKHIHF VYHPTKETCP SCPACVDAKI EHLISSRFIR PSDRNQKNSL SDLNIDRINL
     VILGKDGLAR ELANEIRALC TNDDKYVIDG KMYELSLRPI EGNVRLPVNS FQTPTFQPHG
     CLCLYNSKES LSYVVESIEK SRESTLGRRD NHLVHLPLTL ILVNKRGDTS GETLHSLIQQ
     GQQIASKLQC VFLDPASAGI GYGRNINEKQ ISQVLKGLLD SKRNLNLVSS TASIKDLADV
     DLRIVMCLMC GDPFSADDVL SPVLQSQTCK SSHCGSSNSV LLELPIGLHK KRIELSVLSY
     HSSFSIRKSR LVHGYIVFYS AKRKASLAML RAFLCEVQDI IPIQLVALTD GAIDVLDNDL
     SREQLTEGEE IAQEIDGRFT SIPCSQPQHK LELFHPFFKD VVEKKNIIEA THMYDNVAEA
     CSTTEEVFNS PRAGSPLCNS NLQDSEEDVE PPSYHLFRED ATLPSLSKDH SKFSMELEGN
     DGLSFIMSNF ESKLNNKVPP PVKPKPPVHF DITKDLSYLD QGHREGQRKS MSSSPWMPQD
     GFDPSDYAEP MDAVVKPRNE EENIYSVPHD STQGKIITIR NINKAQSNGS GNGSDSEMDT
     SSLERGRKVS AVSKPVLYRT RCTRLGRFAS YRTSFSVGSD DELGPIRKKE EDQASQGYKG
     DNAVIPYETD EDPRRRNILR SLRRNTKKPK PKPRPSITKA TWESNYFGVP LTTVVTPEKP
     IPIFIERCIE YIEATGLSTE GIYRVSGNKS EMESLQRQFD QDHNLDLAEK DFTVNTVAGA
     MKSFFSELPD PLVPYSMQID LVEAHKINDR EQKLHALKEV LKKFPKENHE VFKYVISHLN
     KVSHNNKVNL MTSENLSICF WPTLMRPDFS SMDALTATRS YQTIIELFIQ QCPFFFYNRP
     ISEPPGAAPG SPSAMAPTVP FLTSTPATSQ PSPPQSPPPT PQSPMQPLLS SQLQAEHTL
//
ID   TBRG4_MOUSE             Reviewed;         630 AA.
AC   Q91YM4; O89082; Q3TKZ4; Q6ZQ19; Q8C6D1;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Protein TBRG4;
DE   AltName: Full=Transforming growth factor beta regulator 4;
GN   Name=Tbrg4; Synonyms=Kiaa0948;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and DBA/2; TISSUE=Blastocyst, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 216-371 (ISOFORMS 1/2).
RC   STRAIN=BALB/c; TISSUE=Spleen;
RX   MEDLINE=99012997; PubMed=9798653; DOI=10.1016/S0161-5890(98)00031-5;
RA   Chu C.C., Paul W.E.;
RT   "Expressed genes in interleukin-4 treated B cells identified by cDNA
RT   representational difference analysis.";
RL   Mol. Immunol. 35:487-502(1998).
CC   -!- FUNCTION: May play a role in cell cycle progression (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q91YM4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q91YM4-2; Sequence=VSP_022461;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the FAST kinase family.
CC   -!- SIMILARITY: Contains 1 RAP domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC36538.1; Type=Erroneous termination; Positions=309; Note=Translated as Gln;
CC       Sequence=BAC36037.1; Type=Erroneous initiation;
CC       Sequence=BAC98055.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK129245; BAC98055.1; ALT_INIT; mRNA.
DR   EMBL; AK075897; BAC36037.1; ALT_INIT; mRNA.
DR   EMBL; AK166760; BAE38999.1; -; mRNA.
DR   EMBL; AK168088; BAE40061.1; -; mRNA.
DR   EMBL; AL603787; CAI24214.1; -; Genomic_DNA.
DR   EMBL; BC016483; AAH16483.1; -; mRNA.
DR   EMBL; BC031155; AAH31155.1; -; mRNA.
DR   EMBL; BC031910; AAH31910.1; -; mRNA.
DR   EMBL; U89434; AAC36538.1; ALT_SEQ; mRNA.
DR   IPI; IPI00453815; -.
DR   IPI; IPI00828226; -.
DR   RefSeq; NP_001123929.1; NM_001130457.1.
DR   RefSeq; NP_598772.1; NM_134011.2.
DR   UniGene; Mm.247761; -.
DR   STRING; Q91YM4; -.
DR   PhosphoSite; Q91YM4; -.
DR   PRIDE; Q91YM4; -.
DR   Ensembl; ENSMUST00000000394; ENSMUSP00000000394; ENSMUSG00000000384.
DR   Ensembl; ENSMUST00000093343; ENSMUSP00000091034; ENSMUSG00000000384.
DR   GeneID; 21379; -.
DR   KEGG; mmu:21379; -.
DR   UCSC; uc007hza.1; mouse.
DR   CTD; 21379; -.
DR   MGI; MGI:1100868; Tbrg4.
DR   eggNOG; roNOG12886; -.
DR   GeneTree; ENSGT00530000063266; -.
DR   HOGENOM; HBG444468; -.
DR   HOVERGEN; HBG094028; -.
DR   InParanoid; Q91YM4; -.
DR   OMA; EWLELKS; -.
DR   OrthoDB; EOG4H72B8; -.
DR   NextBio; 300608; -.
DR   ArrayExpress; Q91YM4; -.
DR   Bgee; Q91YM4; -.
DR   CleanEx; MM_TBRG4; -.
DR   Genevestigator; Q91YM4; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IEA:InterPro.
DR   GO; GO:0045333; P:cellular respiration; ISS:UniProtKB.
DR   InterPro; IPR013579; FAST_2.
DR   InterPro; IPR010622; FAST_Leu-rich.
DR   InterPro; IPR013584; RAP.
DR   Pfam; PF06743; FAST_1; 1.
DR   Pfam; PF08368; FAST_2; 1.
DR   Pfam; PF08373; RAP; 1.
DR   SMART; SM00952; RAP; 1.
DR   PROSITE; PS51286; RAP; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    630       Protein TBRG4.
FT                                /FTId=PRO_0000273027.
FT   DOMAIN      560    618       RAP.
FT   MOD_RES      62     62       Phosphothreonine (By similarity).
FT   VAR_SEQ      77    107       ASRPEQLLELLGSDHSLHHNHAALILIRLSY -> D (in
FT                                isoform 2).
FT                                /FTId=VSP_022461.
FT   CONFLICT    166    166       V -> L (in Ref. 2; BAC36037).
FT   CONFLICT    224    224       T -> I (in Ref. 2; BAC36037).
FT   CONFLICT    286    286       F -> S (in Ref. 5; AAC36538).
FT   CONFLICT    316    316       A -> V (in Ref. 5; AAC36538).
FT   CONFLICT    327    327       P -> S (in Ref. 5; AAC36538).
SQ   SEQUENCE   630 AA;  71513 MW;  22BD82426988C195 CRC64;
     MAVRLMKRCT CLLREATRLV PTVAPVGRLR LAGVSCKTLT SSVSSPSSGS LAELLGKEQV
     FTPYPEHQEL DFLIEKASRP EQLLELLGSD HSLHHNHAAL ILIRLSYLLS EKPKEKALLA
     EDARFQRLVK LVDSQITCVW HGTLVKLLRS LYTLVLPQIS KELQSVEQEV RWRLRRLKYK
     HLVFLAESCA SFMKEQHSQE LLAELLMHLE RRWTEINDSR TLVTMMTMAG HLSESLMNHL
     EDKCLELVEQ FGPDELRKVL VTLAAQSRRS VPLLRAISYH LVQKPFPMTK GMLLDLAYAY
     GKLSFHQTQV SQRLAADLLP FIPSMTPGEV ARCAKSFAFL KWLNLPLFEA FTQHLLSRVQ
     DVSLSHVCSV LLAFARLNFH PEQEEDQFFS MVHEKLDPVL GSLEPALQVD LVWALCVLQH
     VHETELHTVL HPGLHARFLE SKSPKDQSTF QKLVHINTTA LLEHPEYKGP FLPASAVAPI
     PSPSNKKMTP LQKELQETLK ALLGNTDKGS LEVATQYGWV LDAEVLLDAD GHFLPLRNFV
     APHLAQPVGN QPLPPGAKRI AFLRWEFPNF NSRSKDLLGR FVLARRHVLA AGFLVVDVPY
     YEWLDLKSEW QKSAYLKDKM RKAMAEELAK
//
ID   CL004_MOUSE             Reviewed;         552 AA.
AC   Q91YN0; Q3UVK4;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Uncharacterized protein C12orf4 homolog;
GN   Name=D6Wsu163e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Adipose tissue, Corpora quadrigemina, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK045541; BAC32412.1; -; mRNA.
DR   EMBL; AK046707; BAC32841.1; -; mRNA.
DR   EMBL; AK137201; BAE23265.1; -; mRNA.
DR   EMBL; BC016429; AAH16429.1; -; mRNA.
DR   IPI; IPI00130300; -.
DR   RefSeq; NP_613060.1; NM_138594.3.
DR   UniGene; Mm.44228; -.
DR   ProteinModelPortal; Q91YN0; -.
DR   PRIDE; Q91YN0; -.
DR   Ensembl; ENSMUST00000032497; ENSMUSP00000032497; ENSMUSG00000030347.
DR   GeneID; 28040; -.
DR   KEGG; mmu:28040; -.
DR   UCSC; uc009dvm.1; mouse.
DR   CTD; 28040; -.
DR   MGI; MGI:107893; D6Wsu163e.
DR   eggNOG; roNOG13319; -.
DR   HOGENOM; HBG281371; -.
DR   HOVERGEN; HBG057511; -.
DR   InParanoid; Q91YN0; -.
DR   OMA; RERQGIE; -.
DR   OrthoDB; EOG4NGGMD; -.
DR   PhylomeDB; Q91YN0; -.
DR   NextBio; 306564; -.
DR   ArrayExpress; Q91YN0; -.
DR   Bgee; Q91YN0; -.
DR   Genevestigator; Q91YN0; -.
DR   GermOnline; ENSMUSG00000030347; Mus musculus.
DR   InterPro; IPR019311; DUF2362.
DR   PANTHER; PTHR16525; DUF2362; 1.
DR   Pfam; PF10154; DUF2362; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    552       Uncharacterized protein C12orf4 homolog.
FT                                /FTId=PRO_0000089843.
FT   MOD_RES     241    241       Phosphoserine.
SQ   SEQUENCE   552 AA;  63644 MW;  79C9C39ECBA14BCE CRC64;
     MKKNRERFCN KEREFVYKFQ VGRERLELRV PLRFPVEENA SHLHGRLMLL HSLPCFIESD
     LKDALSRFIE EESLRDHDSD AEACLEAVKS GEVDLHQLAS AWAKAYAETT LEHARPEEPD
     WDEDFADVYH DLIHSPASET LLNLEHNYFV SISELIGERD VELKKLRERQ GIEMEKVMQE
     LGKSLTDQDV NSLAAQHFES QQDLENKWSN ELKQSTAIQK QEYQEWVIKL HQDLKNPNNS
     SLSEEIKVQP SQFRESADAA GRIYEEQRKL EESFTIHLGA QLKTMHNLRL LRADMLDFCK
     HKRTHGSGVK LHRLQTALSL YSTSLCGLVL LVDNRINSYS GIKRDFATVC QECTDFHFPR
     IEEQLEVVQQ VALYARTQRK SKCKEARDSG NQNGGSDDKS KNAERNYLNI LPGEFYITRH
     SNLSEIHVAF HLCVDDNVKS GNITARDPAI MGLRNILKVC CTHDITTISI PLLLVHDMSE
     EMTIPWCLRR AELVFKCVKG FMMEMASWDG GISRTVQFLV PQSISEEMFY QLSNMLPQIF
     RVSSTLTLTS KH
//
ID   CSDC2_MOUSE             Reviewed;         154 AA.
AC   Q91YQ3;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Cold shock domain-containing protein C2;
DE   AltName: Full=RNA-binding protein PIPPin;
GN   Name=Csdc2; Synonyms=Pippin;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: RNA-binding factor which binds specifically to the very
CC       3'-UTR ends of both histone H1 and H3.3 mRNAs, encompassing the
CC       polyadenylation signal. Might play a central role in the negative
CC       regulation of histone variant synthesis in the developing brain
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity). Note=PIPPin-RNA complexes are located to the nucleus
CC       (By similarity).
CC   -!- SIMILARITY: Contains 1 CSD (cold-shock) domain.
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DR   EMBL; AK028916; BAC26194.1; -; mRNA.
DR   EMBL; BC016109; AAH16109.1; -; mRNA.
DR   IPI; IPI00130363; -.
DR   RefSeq; NP_663448.2; NM_145473.3.
DR   UniGene; Mm.22524; -.
DR   ProteinModelPortal; Q91YQ3; -.
DR   SMR; Q91YQ3; 69-136.
DR   STRING; Q91YQ3; -.
DR   PRIDE; Q91YQ3; -.
DR   Ensembl; ENSMUST00000038757; ENSMUSP00000044441; ENSMUSG00000042109.
DR   GeneID; 105859; -.
DR   KEGG; mmu:105859; -.
DR   UCSC; uc007wxs.1; mouse.
DR   CTD; 105859; -.
DR   MGI; MGI:2146027; Csdc2.
DR   GeneTree; ENSGT00390000000022; -.
DR   HOGENOM; HBG717773; -.
DR   HOVERGEN; HBG050947; -.
DR   InParanoid; Q91YQ3; -.
DR   OrthoDB; EOG4WM4W3; -.
DR   NextBio; 357940; -.
DR   ArrayExpress; Q91YQ3; -.
DR   Bgee; Q91YQ3; -.
DR   CleanEx; MM_CSDC2; -.
DR   Genevestigator; Q91YQ3; -.
DR   GermOnline; ENSMUSG00000042109; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR019844; Cold-shock_CS.
DR   InterPro; IPR011129; Cold_shock_prot.
DR   InterPro; IPR002059; CSP_DNA-bd.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR016027; NA-bd_OB-fold-like.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   Pfam; PF00313; CSD; 1.
DR   SMART; SM00357; CSP; 1.
DR   SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR   PROSITE; PS00352; COLD_SHOCK; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; mRNA processing; Nucleus; RNA-binding.
FT   CHAIN         1    154       Cold shock domain-containing protein C2.
FT                                /FTId=PRO_0000100352.
FT   DOMAIN       69    136       CSD.
FT   CONFLICT      7      7       S -> L (in Ref. 1; BAC26194).
SQ   SEQUENCE   154 AA;  16827 MW;  85CD90FF2F5E35E0 CRC64;
     MTSESTSPPV VPPLHSPKSP VWPTFPFHRE GSRIWERGGG IAPRDLPSPL PTKRTRTYSA
     TARASAGPVF KGVCKQFSRS QGHGFITPEN GSEDIFVHVS DIEGEYVPVE GDEVTYKICP
     IPPKNQKFQA VEVVLTQLAP HTPHETWSGQ VVGS
//
ID   TWF1_MOUSE              Reviewed;         350 AA.
AC   Q91YR1; O09132; Q52L77; Q80X09;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Twinfilin-1;
DE   AltName: Full=Protein A6;
GN   Name=Twf1; Synonyms=Ptk9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   MEDLINE=97390125; PubMed=9249064; DOI=10.1016/S0378-1119(97)00073-5;
RA   Beeler J.F., Patel B.K.R., Chedid M., LaRochelle W.J.;
RT   "Cloning and characterization of the mouse homolog of the human A6
RT   gene.";
RL   Gene 193:31-37(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH TWF2
RP   AND PHOSPHOINOSITIDE, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=22829901; PubMed=12807912; DOI=10.1074/jbc.M303642200;
RA   Vartiainen M.K., Sarkkinen E.M., Matilainen T., Salminen M.,
RA   Lappalainen P.;
RT   "Mammals have two twinfilin isoforms whose subcellular localizations
RT   and tissue distributions are differentially regulated.";
RL   J. Biol. Chem. 278:34347-34355(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT HIS-51.
RC   STRAIN=NMRI; TISSUE=Mammary gland, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   MEDLINE=20136056; PubMed=10669753;
RX   DOI=10.1128/MCB.20.5.1772-1783.2000;
RA   Vartiainen M., Ojala P.J., Auvinen P., Peranen J., Lappalainen P.;
RT   "Mouse A6/twinfilin is an actin monomer-binding protein that localizes
RT   to the regions of rapid actin dynamics.";
RL   Mol. Cell. Biol. 20:1772-1783(2000).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH G-ACTIN AND CAPPING PROTEINS.
RX   PubMed=15282541; DOI=10.1038/sj.emboj.7600310;
RA   Falck S., Paavilainen V.O., Wear M.A., Grossmann J.G., Cooper J.A.,
RA   Lappalainen P.;
RT   "Biological role and structural mechanism of twinfilin-capping protein
RT   interaction.";
RL   EMBO J. 23:3010-3019(2004).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH G-ACTIN AND CAPPING PROTEINS.
RX   PubMed=16511569; DOI=10.1038/sj.emboj.7601019;
RA   Helfer E., Nevalainen E.M., Naumanen P., Romero S., Didry D.,
RA   Pantaloni D., Lappalainen P., Carlier M.-F.;
RT   "Mammalian twinfilin sequesters ADP-G-actin and caps filament barbed
RT   ends: implications in motility.";
RL   EMBO J. 25:1184-1195(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-349, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-142.
RX   MEDLINE=22301982; PubMed=12207032; DOI=10.1074/jbc.M208225200;
RA   Paavilainen V.O., Merckel M.C., Falck S., Ojala P.J., Pohl E.,
RA   Wilmanns M., Lappalainen P.;
RT   "Structural conservation between the actin monomer-binding sites of
RT   twinfilin and actin-depolymerizing factor (ADF)/cofilin.";
RL   J. Biol. Chem. 277:43089-43095(2002).
RN   [11]
RP   STRUCTURE BY NMR OF 161-313.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the second tandem cofilin-domain of mouse
RT   twinfilin.";
RL   Submitted (JUN-2006) to the PDB data bank.
CC   -!- FUNCTION: Actin-binding protein involved in motile and
CC       morphological processes. Inhibits actin polymerization, likely by
CC       sequestering G-actin. By capping the barbed ends of filaments, it
CC       also regulates motility. Seems to play an important role in
CC       clathrin-mediated endocytosis and distribution of endocytic
CC       organelles.
CC   -!- SUBUNIT: Interacts with G-actin; ADP-actin form and capping
CC       protein (CP). May also be able to interact with TWF2 and
CC       phosphoinositides, PI(4,5)P2. When bound to PI(4,5)P2, it is down-
CC       regulated.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
CC       Note=Diffuse cytoplasmic localization with perinuclear and G-
CC       actin-rich cortical actin structures sublocalization. Also found
CC       at membrane ruffles and cell-cell contacts.
CC   -!- TISSUE SPECIFICITY: Widely expressed with highest levels in brain,
CC       liver and kidney. Also expressed in heart, lung and testis. Not
CC       detected in spleen or skeletal muscle.
CC   -!- DEVELOPMENTAL STAGE: Expression was widespread throughout the
CC       embryonic stages analyzed; E10.5, E12.5, E14.5 and E18.5. At
CC       E14.5, strongest expression was observed in the developing central
CC       and peripheral nervous system (CNS and PNS, respectively) and in
CC       the olfactory sensory epithelium. In the CNS, the proliferating
CC       neuronal precursors in the ventricular zone expressed it more than
CC       the postmitotic neurons. At E18.5, highest expression levels were
CC       detected in the mechanosensory hair cells of the inner ear and in
CC       the differentiated keratinocytes of the skin.
CC   -!- PTM: Phosphorylated on serine and threonine residues (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC       Twinfilin subfamily.
CC   -!- SIMILARITY: Contains 2 ADF-H domains.
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Molecular embrace -
CC       Issue 73 of August 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt073.shtml";
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DR   EMBL; U82324; AAB66592.1; -; mRNA.
DR   EMBL; AY267188; AAP31404.1; -; mRNA.
DR   EMBL; AK147990; BAE28272.1; -; mRNA.
DR   EMBL; AK150852; BAE29908.1; -; mRNA.
DR   EMBL; BC015081; AAH15081.1; -; mRNA.
DR   EMBL; BC094034; AAH94034.1; -; mRNA.
DR   IPI; IPI00314844; -.
DR   RefSeq; NP_032997.3; NM_008971.4.
DR   UniGene; Mm.480555; -.
DR   PDB; 1M4J; X-ray; 1.60 A; A/B=1-142.
DR   PDB; 2D8B; NMR; -; A=161-313.
DR   PDB; 2HD7; NMR; -; A=176-316.
DR   PDB; 3DAW; X-ray; 2.55 A; B=169-322.
DR   PDBsum; 1M4J; -.
DR   PDBsum; 2D8B; -.
DR   PDBsum; 2HD7; -.
DR   PDBsum; 3DAW; -.
DR   ProteinModelPortal; Q91YR1; -.
DR   SMR; Q91YR1; 7-139, 161-313.
DR   STRING; Q91YR1; -.
DR   PhosphoSite; Q91YR1; -.
DR   PRIDE; Q91YR1; -.
DR   Ensembl; ENSMUST00000023087; ENSMUSP00000023087; ENSMUSG00000022451.
DR   GeneID; 19230; -.
DR   KEGG; mmu:19230; -.
DR   NMPDR; fig|10090.3.peg.30503; -.
DR   UCSC; uc007xjl.1; mouse.
DR   CTD; 19230; -.
DR   MGI; MGI:1100520; Twf1.
DR   eggNOG; roNOG08673; -.
DR   GeneTree; ENSGT00530000063868; -.
DR   HOGENOM; HBG447415; -.
DR   HOVERGEN; HBG000848; -.
DR   InParanoid; Q91YR1; -.
DR   OMA; VIRKIEI; -.
DR   OrthoDB; EOG4TTGJJ; -.
DR   PhylomeDB; Q91YR1; -.
DR   NextBio; 296036; -.
DR   ArrayExpress; Q91YR1; -.
DR   Bgee; Q91YR1; -.
DR   Genevestigator; Q91YR1; -.
DR   GermOnline; ENSMUSG00000022451; Mus musculus.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
DR   InterPro; IPR002108; Actin-bd_cofilin/tropomyosin.
DR   Pfam; PF00241; Cofilin_ADF; 2.
DR   SMART; SM00102; ADF; 2.
DR   PROSITE; PS51263; ADF_H; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Actin-binding; Cytoplasm; Cytoskeleton;
KW   Phosphoprotein; Polymorphism; Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    350       Twinfilin-1.
FT                                /FTId=PRO_0000214951.
FT   DOMAIN        2    139       ADF-H 1.
FT   DOMAIN      175    313       ADF-H 2.
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES     143    143       Phosphoserine (By similarity).
FT   MOD_RES     309    309       Phosphotyrosine.
FT   MOD_RES     349    349       Phosphothreonine.
FT   VARIANT      51     51       Q -> H.
FT   CONFLICT    345    345       A -> R (in Ref. 1; AAB66592 and 2;
FT                                AAP31404).
FT   HELIX        11     21
FT   TURN         22     24
FT   STRAND       26     32
FT   STRAND       34     43
FT   HELIX        49     57
FT   HELIX        58     60
FT   STRAND       67     77
FT   STRAND       80     88
FT   HELIX        95    112
FT   HELIX       114    116
FT   STRAND      117    125
FT   HELIX       126    129
FT   HELIX       131    138
FT   HELIX       184    194
FT   STRAND      202    206
FT   TURN        207    210
FT   STRAND      211    216
FT   HELIX       225    228
FT   STRAND      235    245
FT   STRAND      248    258
FT   STRAND      262    264
FT   HELIX       266    274
FT   HELIX       277    283
FT   STRAND      292    300
FT   HELIX       305    313
SQ   SEQUENCE   350 AA;  40079 MW;  643CBBA18D38D4E0 CRC64;
     MSHQTGIQAS EDVKEIFARA RNGKYRLLKI SIENEQLVVG SCSPPSDSWE QDYDSFVLPL
     LEDKQPCYVL FRLDSQNAQG YEWIFIAWSP DHSHVRQKML YAATRATLKK EFGGGHIKDE
     VFGTVKEDVS LHGYKKYLLS QSSPAPLTAA EEELRQIKIN EVQTDVSVDT KHQTLQGVAF
     PISRDAFQAL EKLSKKQLNY VQLEIDIKNE TIILANTENT ELRDLPKRIP KDSARYHFFL
     YKHSHEGDYL ESVVFIYSMP GYTCSIRERM LYSSCKSPLL EIVERQLQMD VIRKIEIDNG
     DELTADFLYD EVHPKQHAHK QSFAKPKGPA GKRGIRRLIR GPAEAEATTD
//
ID   KCC1A_MOUSE             Reviewed;         374 AA.
AC   Q91YS8;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Calcium/calmodulin-dependent protein kinase type 1;
DE            EC=2.7.11.17;
DE   AltName: Full=CaM kinase I;
DE            Short=CaM-KI;
DE   AltName: Full=CaM kinase I alpha;
DE            Short=CaMKI-alpha;
GN   Name=Camk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   FUNCTION IN ERK ACTIVATION.
RX   PubMed=15150258; DOI=10.1074/jbc.M401501200;
RA   Schmitt J.M., Wayman G.A., Nozaki N., Soderling T.R.;
RT   "Calcium activation of ERK mediated by calmodulin kinase I.";
RL   J. Biol. Chem. 279:24064-24072(2004).
CC   -!- FUNCTION: Calcium/calmodulin-dependent protein kinase belonging to
CC       a proposed calcium-triggered signaling cascade involved in a
CC       number of cellular processes like transcriptional regulation,
CC       hormone production, translational regulation, regulation of actin
CC       filament organization and neurite outgrowth. Involved in calcium-
CC       dependent activation of the ERK pathway (By similarity).
CC       Recognizes the substrate consensus sequence [MVLIF]-x-R-x(2)-[ST]-
CC       x(3)-[MVLIF]. Phosphorylates EIF4G3/eIF4GII. In vitro
CC       phosphorylates CREB1, ATF1, CTFR, MYL9, SYN1/synapsin I and
CC       SYNII/synapsin II (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Activated by Ca(2+)/calmodulin. Binding of
CC       calmodulin results in a conformational change that generates
CC       functional binding sites for both, substrate and ATP, and thus
CC       releaves autoinhibition. Must be phosphorylated to be maximally
CC       active. Phosphorylated by CAMKK1 or CAMKK2 (By similarity).
CC   -!- SUBUNIT: Monomer. Interacts with XPO1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Predominantly cytoplasmic (By similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- DOMAIN: The autoinhibitory domain overlaps with the calmodulin
CC       binding region and interacts in the inactive folded state with the
CC       catalytic domain as a pseudosubstrate (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. CaMK subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC014825; AAH14825.1; -; mRNA.
DR   IPI; IPI00130439; -.
DR   RefSeq; NP_598687.1; NM_133926.2.
DR   UniGene; Mm.277373; -.
DR   ProteinModelPortal; Q91YS8; -.
DR   SMR; Q91YS8; 10-316.
DR   STRING; Q91YS8; -.
DR   PhosphoSite; Q91YS8; -.
DR   PRIDE; Q91YS8; -.
DR   Ensembl; ENSMUST00000032409; ENSMUSP00000032409; ENSMUSG00000030272.
DR   GeneID; 52163; -.
DR   KEGG; mmu:52163; -.
DR   UCSC; uc009dfk.1; mouse.
DR   CTD; 52163; -.
DR   MGI; MGI:1098535; Camk1.
DR   GeneTree; ENSGT00600000084207; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108055; -.
DR   InParanoid; Q91YS8; -.
DR   OMA; GNTAYTH; -.
DR   OrthoDB; EOG46Q6SS; -.
DR   PhylomeDB; Q91YS8; -.
DR   BRENDA; 2.7.11.17; 244.
DR   NextBio; 308578; -.
DR   ArrayExpress; Q91YS8; -.
DR   Bgee; Q91YS8; -.
DR   CleanEx; MM_CAMK1; -.
DR   Genevestigator; Q91YS8; -.
DR   GermOnline; ENSMUSG00000030272; Mus musculus.
DR   GO; GO:0005954; C:calcium- and calmodulin-dependent protein kinase complex; TAS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:EC.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0006913; P:nucleocytoplasmic transport; IDA:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR   GO; GO:0007165; P:signal transduction; IDA:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; ATP-binding; Calmodulin-binding; Cytoplasm;
KW   Developmental protein; Differentiation; Kinase; Neurogenesis;
KW   Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    374       Calcium/calmodulin-dependent protein
FT                                kinase type 1.
FT                                /FTId=PRO_0000086077.
FT   DOMAIN       20    276       Protein kinase.
FT   NP_BIND      26     34       ATP (By similarity).
FT   REGION      276    316       Autoinhibitory domain (By similarity).
FT   REGION      296    317       Calmodulin-binding (By similarity).
FT   MOTIF       315    321       Nuclear export signal (By similarity).
FT   ACT_SITE    141    141       Proton acceptor (By similarity).
FT   BINDING      49     49       ATP (By similarity).
FT   MOD_RES     177    177       Phosphothreonine; by CaMKK1 and CaMKK2
FT                                (By similarity).
SQ   SEQUENCE   374 AA;  41624 MW;  37889CDA717D3AB2 CRC64;
     MPGAVEGPRW KQAEDIRDIY DFRDVLGTGA FSEVILAEDK RTQKLVAIKC IAKKALEGKE
     GSMENEIAVL HKIKHPNIVA LDDIYESGGH LYLIMQLVSG GELFDRIVEK GFYTERDASR
     LIFQVLDAVK YLHDLGIVHR DLKPENLLYY SLDEDSKIMI SDFGLSKMED PGSVLSTACG
     TPGYVAPEVL AQKPYSKAVD CWSIGVIAYI LLCGYPPFYD ENDAKLFEQI LKAEYEFDSP
     YWDDISDSAK DFIRHLMEKD PEKRFTCEQA LQHPWIAGDT ALDKNIHQSV SEQIKKNFAK
     SKWKQAFNAT AVVRHMRKLQ LGTSQEGQGQ TGSHGELLTP TAGGPAAGCC CRDCCVEPGS
     ELPPAPPPSS RAMD
//
ID   NDUV1_MOUSE             Reviewed;         464 AA.
AC   Q91YT0;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial;
DE            EC=1.6.5.3;
DE            EC=1.6.99.3;
DE   AltName: Full=Complex I-51kD;
DE            Short=CI-51kD;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 51 kDa subunit;
DE   Flags: Precursor;
GN   Name=Ndufv1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 21-29.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=10870971;
RX   DOI=10.1002/(SICI)1522-2683(20000501)21:9<1853::AID-ELPS1853>3.3.CO;2-P;
RA   Tsugita A., Kawakami T., Uchida T., Sakai T., Kamo M., Matsui T.,
RA   Watanabe Y., Morimasa T., Hosokawa K., Toda T.;
RT   "Proteome analysis of mouse brain: two-dimensional electrophoresis
RT   profiles of tissue proteins during the course of aging.";
RL   Electrophoresis 21:1853-1871(2000).
RN   [4]
RP   PROTEIN SEQUENCE OF 29-48; 72-81; 89-126; 138-147; 153-219; 258-267;
RP   275-297; 303-329; 370-375; 387-394 AND 402-449, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81; LYS-104 AND LYS-375, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory
CC       chain NADH dehydrogenase (Complex I) that is believed to belong to
CC       the minimal assembly required for catalysis. Complex I functions
CC       in the transfer of electrons from NADH to the respiratory chain.
CC       The immediate electron acceptor for the enzyme is believed to be
CC       ubiquinone (By similarity).
CC   -!- CATALYTIC ACTIVITY: NADH + ubiquinone = NAD(+) + ubiquinol.
CC   -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor.
CC   -!- COFACTOR: Binds 1 FMN (Potential).
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster (Potential).
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits. This is a
CC       component of the flavoprotein-sulfur (FP) fragment of the enzyme
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein; Matrix side (By similarity).
CC   -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK075692; BAC35893.1; -; mRNA.
DR   EMBL; BC014818; AAH14818.1; -; mRNA.
DR   EMBL; BC041682; AAH41682.1; -; mRNA.
DR   IPI; IPI00130460; -.
DR   PIR; PC7078; PC7078.
DR   RefSeq; NP_598427.1; NM_133666.2.
DR   UniGene; Mm.29842; -.
DR   ProteinModelPortal; Q91YT0; -.
DR   SMR; Q91YT0; 36-460.
DR   STRING; Q91YT0; -.
DR   PhosphoSite; Q91YT0; -.
DR   PRIDE; Q91YT0; -.
DR   Ensembl; ENSMUST00000042497; ENSMUSP00000042967; ENSMUSG00000037916.
DR   GeneID; 17995; -.
DR   KEGG; mmu:17995; -.
DR   NMPDR; fig|10090.3.peg.4389; -.
DR   UCSC; uc008fye.1; mouse.
DR   CTD; 17995; -.
DR   MGI; MGI:107851; Ndufv1.
DR   eggNOG; roNOG08219; -.
DR   GeneTree; ENSGT00390000010641; -.
DR   HOGENOM; HBG669338; -.
DR   HOVERGEN; HBG006542; -.
DR   InParanoid; Q91YT0; -.
DR   OMA; IDQYSHK; -.
DR   PhylomeDB; Q91YT0; -.
DR   BRENDA; 1.6.5.3; 244.
DR   BRENDA; 1.6.99.3; 244.
DR   NextBio; 292979; -.
DR   ArrayExpress; Q91YT0; -.
DR   Bgee; Q91YT0; -.
DR   CleanEx; MM_NDUFV1; -.
DR   Genevestigator; Q91YT0; -.
DR   GermOnline; ENSMUSG00000037916; Mus musculus.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:EC.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR   InterPro; IPR019575; NADH-UbQ_OxRdtase_Fsu_4Fe4S-bd.
DR   InterPro; IPR011537; NADH-UbQ_OxRdtase_suF.
DR   InterPro; IPR011538; NADH_UbQ_OxRdtase_51kDa_su.
DR   InterPro; IPR019554; Soluble_ligand-bd.
DR   Pfam; PF01512; Complex1_51K; 1.
DR   Pfam; PF10589; NADH_4Fe-4S; 1.
DR   Pfam; PF10531; SLBB; 1.
DR   SMART; SM00928; NADH_4Fe-4S; 1.
DR   TIGRFAMs; TIGR01959; nuoF_fam; 1.
DR   PROSITE; PS00644; COMPLEX1_51K_1; 1.
DR   PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Acetylation; Direct protein sequencing; Electron transport;
KW   Flavoprotein; FMN; Iron; Iron-sulfur; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase;
KW   Respiratory chain; Transit peptide; Transport; Ubiquinone.
FT   TRANSIT       1     20       Mitochondrion.
FT   CHAIN        21    464       NADH dehydrogenase [ubiquinone]
FT                                flavoprotein 1, mitochondrial.
FT                                /FTId=PRO_0000019978.
FT   NP_BIND      87     96       NAD(H) (By similarity).
FT   NP_BIND     199    247       FMN (By similarity).
FT   METAL       379    379       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       382    382       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       385    385       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       425    425       Iron-sulfur (4Fe-4S) (Potential).
FT   MOD_RES      81     81       N6-acetyllysine.
FT   MOD_RES     104    104       N6-acetyllysine.
FT   MOD_RES     375    375       N6-acetyllysine.
SQ   SEQUENCE   464 AA;  50834 MW;  611EAB1546D2A630 CRC64;
     MLAARHFLGG LVPVRVSVRF SSGTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGALRRG
     DWYKTKEILL KGPDWILGEM KTSGLRGRGG AGFPTGLKWS FMNKPSDGRP KYLVVNADEG
     EPGTCKDREI MRHDPHKLVE GCLVGGRAMG ARAAYIYIRG EFYNEASNLQ VAIREAYEAG
     LIGKNACGSD YDFDVFVVRG AGAYICGEET ALIESIEGKQ GKPRLKPPFP ADVGVFGCPT
     TVANVETVAV SPTICRRGGT WFAGFGRERN SGTKLFNISG HVNHPCTVEE EMSVPLKELI
     EKHAGGVTGG WDNLLAVIPG GSSTPLIPKS VCETVLMDFD ALVQAQTGLG TAAVIVMDRS
     TDIVKAIARL IEFYKHESCG QCTPCREGVD WMNKVMARFV KGDARPAEID SLWEISKQIE
     GHTICALGDG AAWPVQGLIR HFRPELEDRM QRFAQQHRAW QAAS
//
ID   LZTS2_MOUSE             Reviewed;         671 AA.
AC   Q91YU6; Q569X6;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 2.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Leucine zipper putative tumor suppressor 2;
DE   AltName: Full=Protein LAPSER1;
GN   Name=Lzts2; Synonyms=Kiaa1813, Lapser1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NMRI; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18490357; DOI=10.1093/hmg/ddn153;
RA   Sudo H., Maru Y.;
RT   "LAPSER1/LZTS2: a pluripotent tumor suppressor linked to the
RT   inhibition of katanin-mediated microtubule severing.";
RL   Hum. Mol. Genet. 17:2524-2540(2008).
CC   -!- FUNCTION: Negative regulator of katanin-mediated microtubule
CC       severing and release from the centrosome. Required for central
CC       spindle formation and the completion of cytokinesis. May
CC       negatively regulate axonal outgrowth by preventing the formation
CC       of microtubule bundles that are necessary for transport within the
CC       elongating axon. Negative regulator of the Wnt signaling pathway.
CC       Represses beta-catenin-mediated transcriptional activation by
CC       promoting the nuclear exclusion of beta-catenin (By similarity).
CC   -!- SUBUNIT: Interacts with KATNB1. Also interacts with CTNNB1, gamma-
CC       tubulin and KIF23 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytoskeleton, centrosome. Note=Localized to the centrosome
CC       throughout the cell cycle (By similarity). Localized to the
CC       midbody in cells undergoing cytokinesis (By similarity).
CC   -!- SIMILARITY: Belongs to the LZTS2 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98256.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK129446; BAC98256.1; ALT_INIT; mRNA.
DR   EMBL; BC014695; AAH14695.1; -; mRNA.
DR   EMBL; BC092263; AAH92263.1; -; mRNA.
DR   IPI; IPI00130506; -.
DR   RefSeq; NP_001123997.1; NM_001130525.1.
DR   RefSeq; NP_001123998.1; NM_001130526.1.
DR   RefSeq; NP_663478.2; NM_145503.2.
DR   UniGene; Mm.28204; -.
DR   UniGene; Mm.329877; -.
DR   ProteinModelPortal; Q91YU6; -.
DR   IntAct; Q91YU6; 5.
DR   STRING; Q91YU6; -.
DR   PhosphoSite; Q91YU6; -.
DR   PRIDE; Q91YU6; -.
DR   Ensembl; ENSMUST00000039016; ENSMUSP00000045478; ENSMUSG00000035342.
DR   GeneID; 226154; -.
DR   KEGG; mmu:226154; -.
DR   UCSC; uc008hqk.1; mouse.
DR   CTD; 226154; -.
DR   MGI; MGI:2385095; Lzts2.
DR   eggNOG; roNOG08379; -.
DR   GeneTree; ENSGT00510000046769; -.
DR   HOGENOM; HBG713386; -.
DR   HOVERGEN; HBG052381; -.
DR   InParanoid; Q91YU6; -.
DR   OrthoDB; EOG4H19VQ; -.
DR   NextBio; 378036; -.
DR   ArrayExpress; Q91YU6; -.
DR   Bgee; Q91YU6; -.
DR   CleanEx; MM_LZTS2; -.
DR   Genevestigator; Q91YU6; -.
DR   GermOnline; ENSMUSG00000035342; Mus musculus.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR009638; Fez1.
DR   Pfam; PF06818; Fez1; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Microtubule; Mitosis; Phosphoprotein; Wnt signaling pathway.
FT   CHAIN         1    671       Leucine zipper putative tumor suppressor
FT                                2.
FT                                /FTId=PRO_0000182975.
FT   REGION        1    333       Required for centrosomal localization (By
FT                                similarity).
FT   REGION      449    671       Sufficient for interaction with CTNNB1
FT                                (By similarity).
FT   REGION      452    671       Sufficient for interaction with KATNB1
FT                                and for inhibition of katanin-mediated
FT                                microtubule severing (By similarity).
FT   COILED      329    651       Potential.
FT   MOTIF       633    642       Nuclear export signal (By similarity).
FT   COMPBIAS    188    306       Ser-rich.
FT   MOD_RES     572    572       Phosphoserine (By similarity).
FT   CONFLICT    327    327       H -> Q (in Ref. 2; AAH14695/AAH92263).
SQ   SEQUENCE   671 AA;  72637 MW;  9032F0F55F45DBE7 CRC64;
     MAIVHTLPVP LEPARETATA PKTPAMGSVS SLISGRPCPG GPAPQRHHGV PGPTFFRQQD
     GLLRGGYEAQ EPLCPAVPPR KAVPGNSFTY VNEDFRTESP PSPSSDVEDP REHQAHNAHL
     RGPPPKLIPV SGKLEKNMEK ILIRPTAFKP VLPKPRGAPS LPGFLGPRAA GLSGSQGSLT
     QLFGGPASSS SSSSSSSAAD KPLALSGWAS GCPSGTLSDS GRNSLSSLPT YSTGGAEPTT
     NSPGGHLPSH GPGRGALPGP ARGVPTGPSH SDSGRSSSSK STGSLGGRVA GGLLGSGARA
     SPGSSSGGDR SPPPPPPPPP SDEALLHCVL EGKLRDREAE LQQLRDSMDE SEATVCQAFG
     ARQRRWPRER GEDCAAQAQQ ATQRVQRAQQ LLQLQVFQLQ QEKRQLQDDF AQLLQEREQL
     ERRCATFERE QRELGPRLEE TKWEVCQKSG EISLLKQQLK ESQAELVQKG SELVALRVAL
     REARATLRVS EGRARGLQEA ARAREQELEA CSQELQRYRQ EAERLREKAG HLDAEASGLR
     DPPVPPATTD PFLLAESDEA KVQRAAAGAG GSLRAQVERL RQELQREQRR GDEQRDSFEG
     ERLAWQAEKE QVIRYQKQLQ HNYIQMYRRN RQLEQELQQL SLELEARELA DLGLAESAPC
     ICLEEITATE I
//
ID   SSF1_MOUSE              Reviewed;         470 AA.
AC   Q91YU8;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Suppressor of SWI4 1 homolog;
DE            Short=Ssf-1;
DE   AltName: Full=Peter Pan homolog;
GN   Name=Ppan; Synonyms=Ssf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May have a role in cell growth (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity).
CC   -!- SIMILARITY: Contains 1 Brix domain.
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DR   EMBL; BC014688; AAH14688.1; -; mRNA.
DR   IPI; IPI00130510; -.
DR   UniGene; Mm.2930; -.
DR   ProteinModelPortal; Q91YU8; -.
DR   STRING; Q91YU8; -.
DR   PhosphoSite; Q91YU8; -.
DR   PRIDE; Q91YU8; -.
DR   Ensembl; ENSMUST00000004203; ENSMUSP00000004203; ENSMUSG00000004100.
DR   UCSC; uc009ojk.1; mouse.
DR   MGI; MGI:2178445; Ppan.
DR   GeneTree; ENSGT00530000064158; -.
DR   HOGENOM; HBG749683; -.
DR   HOVERGEN; HBG026954; -.
DR   InParanoid; Q91YU8; -.
DR   OrthoDB; EOG4P2Q1Q; -.
DR   PhylomeDB; Q91YU8; -.
DR   NextBio; 382469; -.
DR   ArrayExpress; Q91YU8; -.
DR   Bgee; Q91YU8; -.
DR   CleanEx; MM_PPAN; -.
DR   Genevestigator; Q91YU8; -.
DR   GermOnline; ENSMUSG00000004100; Mus musculus.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR007109; Brix.
DR   Pfam; PF04427; Brix; 1.
DR   SMART; SM00879; Brix; 1.
DR   SUPFAM; SSF52954; Anticodon_bd; 1.
DR   PROSITE; PS50833; BRIX; 1.
PE   2: Evidence at transcript level;
KW   Nucleus; Phosphoprotein.
FT   CHAIN         1    470       Suppressor of SWI4 1 homolog.
FT                                /FTId=PRO_0000120258.
FT   DOMAIN       29    292       Brix.
FT   MOD_RES     238    238       Phosphoserine (By similarity).
FT   MOD_RES     240    240       Phosphoserine (By similarity).
SQ   SEQUENCE   470 AA;  52725 MW;  2255C918FAAE66C2 CRC64;
     MGQSGRSRHQ KRNRAQAQLR NLESYAAQPH SFVFTRGRAG RNVRQLSLDV RRVMEPLTAT
     RLQVRKKNSL KDCVAVAGPL GVTHFLILTK TDNSVYLKLM RLPGGPTLTF QISKYTLIRD
     VVSSLRRHRM HEQQFNHPPL LVLNSFGPQG MHIKLMATMF QNLFPSINVH TVNLNTIKRC
     LLINYNPDSQ ELDFRHYSVK VVPVGASRGM KKLLQEKFPN MSRLQDISEL LATGVGLSDS
     EVEPDGEHNT TELPQAVAGR GNMQAQQSAV RLTEIGPRMT LQLIKIQEGV GNGNVLFHSF
     VHKTEEELQA ILAAKEEKLR LKAQRQNQQA ENLQRKQELR EAHKKKSLAG IKRARARADG
     DSDAEDPGAP PEAVGAGQPE DEEDDAEYFR QAVGEEPDED LFPTAAKRRR PGGPLGKKQR
     GKEQRPGNKG RGQGGNWQAL KLQGRSQRGK AKPRPRATHQ DSRPASRRRN
//
ID   TTC1_MOUSE              Reviewed;         292 AA.
AC   Q91Z38; Q3TLM0;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Tetratricopeptide repeat protein 1;
DE            Short=TPR repeat protein 1;
GN   Name=Ttc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBUNIT: Interacts with the GAP domain of NF1 (By similarity).
CC   -!- SIMILARITY: Contains 3 TPR repeats.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK077715; BAC36975.1; -; mRNA.
DR   EMBL; AK166431; BAE38772.1; -; mRNA.
DR   EMBL; BC010236; AAH10236.1; -; mRNA.
DR   IPI; IPI00130475; -.
DR   RefSeq; NP_598556.1; NM_133795.1.
DR   UniGene; Mm.271974; -.
DR   ProteinModelPortal; Q91Z38; -.
DR   SMR; Q91Z38; 114-234.
DR   STRING; Q91Z38; -.
DR   PhosphoSite; Q91Z38; -.
DR   PRIDE; Q91Z38; -.
DR   Ensembl; ENSMUST00000048578; ENSMUSP00000040779; ENSMUSG00000041278.
DR   GeneID; 66827; -.
DR   KEGG; mmu:66827; -.
DR   UCSC; uc007imx.1; mouse.
DR   CTD; 66827; -.
DR   MGI; MGI:1914077; Ttc1.
DR   HOGENOM; HBG622538; -.
DR   HOVERGEN; HBG001208; -.
DR   InParanoid; Q91Z38; -.
DR   OMA; AINDCSK; -.
DR   PhylomeDB; Q91Z38; -.
DR   NextBio; 322755; -.
DR   ArrayExpress; Q91Z38; -.
DR   Bgee; Q91Z38; -.
DR   CleanEx; MM_TTC1; -.
DR   Genevestigator; Q91Z38; -.
DR   GermOnline; ENSMUSG00000041278; Mus musculus.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR023114; Elongated_TPR_rpt_dom.
DR   InterPro; IPR001440; TPR-1.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.10.150.160; Elongated_TPR_rpt_dom; 1.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
DR   Pfam; PF00515; TPR_1; 2.
DR   SMART; SM00028; TPR; 3.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Repeat; TPR repeat.
FT   CHAIN         1    292       Tetratricopeptide repeat protein 1.
FT                                /FTId=PRO_0000106377.
FT   REPEAT      116    149       TPR 1.
FT   REPEAT      155    188       TPR 2.
FT   REPEAT      189    222       TPR 3.
FT   MOD_RES      67     67       Phosphoserine (By similarity).
FT   MOD_RES      69     69       Phosphoserine (By similarity).
FT   MOD_RES      90     90       Phosphoserine (By similarity).
SQ   SEQUENCE   292 AA;  33263 MW;  C88711F320DD1106 CRC64;
     MEEKSEDCKV PEDLFNGLKV ADPQEGESAS PMVSDPKGQH CQSKLPKAAE AHPQDDHVEE
     ECFHDCSASF EEEQPGAHVA GSKASDDSSS ELDEEYLIEL EKNMPEEEKQ KRREESAKLK
     EEGNERFKRG DYMEAESSYS QALQMCPACF QKDRSVLFSN RAAARMKQDK KETAITDCSK
     AIQLNPTYIR AILRRAELYE KTDKLDEALE DYKSVLEKDP SVHQAREACM RLPKQIEERN
     ERLKEEMLGK LKDLGNLVLR PFGLSTENFQ IKQDSSTGSY SINFVQNPNN NR
//
ID   FNBP2_MOUSE             Reviewed;        1071 AA.
AC   Q91Z67; B2RY13; Q3V1V8; Q61054;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=SLIT-ROBO Rho GTPase-activating protein 2;
DE            Short=srGAP2;
DE   AltName: Full=Formin-binding protein 2;
DE   AltName: Full=Formin-binding protein 27;
DE            Short=FBP-27;
GN   Name=Srgap2; Synonyms=Fbp27, Fnbp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 432-836.
RX   MEDLINE=21526632; PubMed=11672528; DOI=10.1016/S0092-8674(01)00530-X;
RA   Wong K., Ren X.R., Huang Y.Z., Xie Y., Liu G., Saito H., Tang H.,
RA   Wen L., Brady-Kalnay S.M., Mei L., Wu J.Y., Xiong W.C., Rao Y.;
RT   "Signal transduction in neuronal migration: roles of GTPase activating
RT   proteins and the small GTPase Cdc42 in the Slit-Robo pathway.";
RL   Cell 107:209-221(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 538-1071.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 732-782.
RC   STRAIN=FVB;
RX   MEDLINE=96183189; PubMed=8605874;
RA   Chan D.C., Bedford M.T., Leder P.;
RT   "Formin binding proteins bear WWP/WW domains that bind proline-rich
RT   peptides and functionally resemble SH3 domains.";
RL   EMBO J. 15:1045-1054(1996).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-799, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Putative GTPase-activating protein for Rho family small
CC       GTPases (By similarity).
CC   -!- SUBUNIT: Probably interacts with ROBO1. Interacts with FASLG (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 FCH domain.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC109299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC120217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC165436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC151081; AAI51082.1; -; mRNA.
DR   EMBL; BC151082; AAI51083.1; -; mRNA.
DR   EMBL; BC158055; AAI58056.1; -; mRNA.
DR   EMBL; BC172152; AAI72152.1; -; mRNA.
DR   EMBL; AY057900; AAL27032.1; -; mRNA.
DR   EMBL; AK132220; BAE21041.1; -; mRNA.
DR   EMBL; U40752; AAC52480.1; -; mRNA.
DR   IPI; IPI00676293; -.
DR   PIR; S64712; S64712.
DR   RefSeq; NP_001074480.2; NM_001081011.2.
DR   UniGene; Mm.476747; -.
DR   ProteinModelPortal; Q91Z67; -.
DR   SMR; Q91Z67; 501-679, 723-787.
DR   STRING; Q91Z67; -.
DR   PhosphoSite; Q91Z67; -.
DR   PRIDE; Q91Z67; -.
DR   Ensembl; ENSMUST00000097588; ENSMUSP00000095195; ENSMUSG00000026425.
DR   GeneID; 14270; -.
DR   KEGG; mmu:14270; -.
DR   UCSC; uc007cng.1; mouse.
DR   CTD; 14270; -.
DR   MGI; MGI:109605; Srgap2.
DR   GeneTree; ENSGT00600000084084; -.
DR   HOVERGEN; HBG051637; -.
DR   OrthoDB; EOG4MSCXF; -.
DR   PhylomeDB; Q91Z67; -.
DR   NextBio; 285639; -.
DR   ArrayExpress; Q91Z67; -.
DR   Bgee; Q91Z67; -.
DR   CleanEx; MM_SRGAP2; -.
DR   Genevestigator; Q91Z67; -.
DR   GermOnline; ENSMUSG00000026425; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR001060; FCH.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50133; FCH; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; GTPase activation; Phosphoprotein; SH3 domain.
FT   CHAIN         1   1071       SLIT-ROBO Rho GTPase-activating protein
FT                                2.
FT                                /FTId=PRO_0000056768.
FT   DOMAIN       22     87       FCH.
FT   DOMAIN      489    679       Rho-GAP.
FT   DOMAIN      728    787       SH3.
FT   COILED      363    401       Potential.
FT   COILED      940    968       Potential.
FT   MOD_RES     799    799       Phosphoserine.
FT   MOD_RES     916    916       Phosphoserine (By similarity).
FT   MOD_RES     990    990       Phosphoserine (By similarity).
FT   MOD_RES     993    993       Phosphoserine (By similarity).
FT   MOD_RES     994    994       Phosphoserine (By similarity).
FT   MOD_RES    1053   1053       Phosphoserine (By similarity).
FT   MOD_RES    1061   1061       Phosphoserine (By similarity).
FT   MOD_RES    1065   1065       Phosphothreonine (By similarity).
FT   CONFLICT    598    598       A -> V (in Ref. 3; AAL27032).
FT   CONFLICT    612    612       T -> S (in Ref. 3; AAL27032).
FT   CONFLICT    662    662       A -> S (in Ref. 3; AAL27032).
FT   CONFLICT    737    737       F -> C (in Ref. 3; AAL27032).
FT   CONFLICT    765    765       W -> L (in Ref. 3; AAL27032).
SQ   SEQUENCE   1071 AA;  120798 MW;  9093C63476BA605D CRC64;
     MTSPAKFKKD KEIIAEYDTQ VKEIRAQLTE QMKCLDQQCE LRVQLLQDLQ DFFRKKAEIE
     MDYSRNLEKL AERFLAKTRS TKDQQFKKDQ NVLSPVNCWN LLLNQVKRES RDHTTLSDIY
     LNNIIPRFVQ VSEDSGRLFK KSKEVGQQLQ DDLMKVLNEL YSVMKTYHMY NADSISAQSK
     LKEAEKQEEK QIGKSVKQED RQTPRSPDST ANVRIEEKHV RRSSVKKIEK MKEKRQAKYT
     ENKLKAIKAR NEYLLALEAT NASVFKYYIH DLSDIIDQCC DLGYHASLNR ALRTFLSAEL
     NLEQSKHEGL DAIENAVENL DATSDKQRLM EMYNNVFCPP MKFEFQPHMG DMASQLCAQQ
     PVQSELVQRC QQLQSRLSTL KIENEEVKKT MEATLQTIQD IVTVEDFDVS DCFQYSNSME
     SVKSTVSETF MSKPSIAKRR ANQQETEQFY FTKMKEYLEG RNLITKLQAK HDLLQKTLGE
     SQRTDCSLAR RSSTVRKQDS SQAIPLVVES CIRFISRHGL QHEGIFRVSG SQVEVNDIKN
     AFERGEDPLA GDQNDHDMDS IAGVLKLYFR GLEHPLFPKD IFHDLIACVT MDNLQERAVH
     IRKVLLVLPK PTLIIMRYLF AFLNHLSQFS EENMMDPYNL AICFGPSLMS VPEGHDQVSC
     QAHVNELIKT IIIQHENIFP NPRELEGPIY SRGGSMEDYC DSTHGETTSA EDSTQDVTAE
     HHTSDDECEP IEAIAKFDYV GRTARELSFK KGASLLLYQR ASDDWWEGRH NGIDGLIPHQ
     YIVVQDTEDG VVERSSPKSE IEVMSEPPEE KVTARTGASC PSGGHVADIY LANINKQRKR
     PESGSIRKAF RSDSHGLGSS LTDSSSLGVG ASCRPSSQPI MSQNLPKEGP DKCSISGHGS
     LNSISRHSSL KNRMDSPQIR KTATAGRSKS FNNHRPMDPE VIAQDIEATM NSALNELQEL
     ERQSSAKHTP DVVLDTLEPL KTSPVVAPTS EPSSPLHTQL LKDPEPAFQR SASTAGDIAC
     AFRPVKSVKM AAPVKPPATR PKPTVFPKTN ATSPGVNSSA SPQATDKSCT V
//
ID   SRGP1_MOUSE             Reviewed;        1062 AA.
AC   Q91Z69; Q08E84;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=SLIT-ROBO Rho GTPase-activating protein 1;
DE            Short=srGAP1;
DE   AltName: Full=Rho GTPase-activating protein 13;
GN   Name=Srgap1; Synonyms=Arhgap13;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 353-1062.
RX   MEDLINE=21526632; PubMed=11672528; DOI=10.1016/S0092-8674(01)00530-X;
RA   Wong K., Ren X.R., Huang Y.Z., Xie Y., Liu G., Saito H., Tang H.,
RA   Wen L., Brady-Kalnay S.M., Mei L., Wu J.Y., Xiong W.C., Rao Y.;
RT   "Signal transduction in neuronal migration: roles of GTPase activating
RT   proteins and the small GTPase Cdc42 in the Slit-Robo pathway.";
RL   Cell 107:209-221(2001).
CC   -!- FUNCTION: GTPase-activating protein for RhoA and Cdc42 small
CC       GTPases. Together with CDC42 seems to be involved in the pathway
CC       mediating the repulsive signaling of Robo and Slit proteins in
CC       neuronal migration. SLIT2, probably through interaction with
CC       ROBO1, increases the interaction of SRGAP1 with ROBO1 and
CC       inactivates CDC42 (By similarity).
CC   -!- SUBUNIT: Interacts with ROBO1, CDC42 and RHOA. Interacts with
CC       FASLG (By similarity).
CC   -!- SIMILARITY: Contains 1 FCH domain.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL27030.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; BC120892; AAI20893.1; -; mRNA.
DR   EMBL; BC120893; AAI20894.1; -; mRNA.
DR   EMBL; AY057898; AAL27030.1; ALT_INIT; mRNA.
DR   IPI; IPI00670247; -.
DR   UniGene; Mm.288698; -.
DR   PDB; 2GNC; X-ray; 1.80 A; A/B=725-776.
DR   PDBsum; 2GNC; -.
DR   ProteinModelPortal; Q91Z69; -.
DR   SMR; Q91Z69; 493-674, 722-776.
DR   STRING; Q91Z69; -.
DR   PhosphoSite; Q91Z69; -.
DR   PRIDE; Q91Z69; -.
DR   Ensembl; ENSMUST00000020322; ENSMUSP00000020322; ENSMUSG00000020121.
DR   UCSC; uc007hgb.1; mouse.
DR   MGI; MGI:2152936; Srgap1.
DR   eggNOG; roNOG11782; -.
DR   GeneTree; ENSGT00600000084084; -.
DR   HOVERGEN; HBG051637; -.
DR   OrthoDB; EOG4SJ5D1; -.
DR   ArrayExpress; Q91Z69; -.
DR   Bgee; Q91Z69; -.
DR   CleanEx; MM_SRGAP1; -.
DR   Genevestigator; Q91Z69; -.
DR   GermOnline; ENSMUSG00000020121; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005100; F:Rho GTPase activator activity; IDA:MGI.
DR   GO; GO:0017048; F:Rho GTPase binding; IDA:MGI.
DR   GO; GO:0016477; P:cell migration; IDA:MGI.
DR   GO; GO:0007266; P:Rho protein signal transduction; IDA:MGI.
DR   InterPro; IPR001060; FCH.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50133; FCH; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; GTPase activation; Phosphoprotein;
KW   SH3 domain.
FT   CHAIN         1   1062       SLIT-ROBO Rho GTPase-activating protein
FT                                1.
FT                                /FTId=PRO_0000056766.
FT   DOMAIN       22     87       FCH.
FT   DOMAIN      481    671       Rho-GAP.
FT   DOMAIN      720    779       SH3.
FT   COILED      352    382       Potential.
FT   COILED      933    960       Potential.
FT   COMPBIAS    831    834       Poly-Pro.
FT   COMPBIAS    886    889       Poly-Arg.
FT   COMPBIAS   1004   1009       Poly-Ser.
FT   MOD_RES     883    883       Phosphoserine (By similarity).
FT   MOD_RES     894    894       Phosphoserine (By similarity).
FT   MOD_RES     976    976       Phosphoserine (By similarity).
FT   MOD_RES     978    978       Phosphothreonine (By similarity).
FT   MOD_RES     981    981       Phosphothreonine (By similarity).
FT   MOD_RES     982    982       Phosphoserine (By similarity).
FT   MOD_RES     985    985       Phosphoserine (By similarity).
FT   MOD_RES     987    987       Phosphoserine (By similarity).
FT   MOD_RES    1006   1006       Phosphoserine (By similarity).
FT   MOD_RES    1009   1009       Phosphoserine (By similarity).
FT   CONFLICT    574    574       F -> V (in Ref. 2; AAL27030).
FT   CONFLICT    721    724       EPIE -> RGPSR (in Ref. 2; AAL27030).
FT   CONFLICT    797    797       S -> G (in Ref. 2; AAL27030).
FT   STRAND      725    729
FT   STRAND      746    754
FT   STRAND      757    762
FT   STRAND      765    770
FT   HELIX       771    773
SQ   SEQUENCE   1062 AA;  121430 MW;  D0FA749750A9081A CRC64;
     MSTPSRFKKD KEIIAEYESQ VKEIRAQLVE QQKCLEQQTE MRVQLLQDLQ DFFRKKAEIE
     TEYSRNLEKL AERFMAKTRS TKDHQQFKKD QNLLSPVNCW YLLLNQVRRE SKDHATLSDI
     YLNNVIMRFM QISEDSTRMF KKSKEIAFQL HEDLMKVLNE LYTVMKTYHM YHSESISAES
     KLKEAEKQEE KQIGRSGDPV FHIRLEERHQ RRSSVKKIEK MKEKRQAKYS ENKLKSIKAR
     NEYLLTLEAT NASVFKYYIH DLSDLIDCCD LGYHASLNRA LRTYLSAEYN LETSRHEGLD
     IIENAVDNLE PRSDKQRFME MYPAAFCPPM KFEFQSHMGD EVCQVSAQQP VQAELMLRNQ
     QLQSRLATLK IESEEVKKTT EATLQTIQDM VTIEDYDVSE CFQHSRSTES VKSTVSETYL
     SKPSIAKRRA NQQETEQFYF MKLREFLEGS NLITKLQAKH DLLQRTLGEG HRAEYMTTSR
     GRRNSHARHQ DSGQVIPLIV ESCIRFINLY GLQHQGIFRV SGSQVEVNDI KNSFERGENP
     LSDEQSNHDI NSVAGVLKLY FRGLENPLFP KERFTDLISC IRIDNLYERA LHIRKLLLTL
     PRSVLIVMRY LFAFLNHLSQ YSDENMMDPY NLAICFGPTL MPVPEIQDQV SCQAHVNEIV
     KTIIIHHETI FPDAKELDGP VYEKCMAGGD YCDSPYSEHG TLEEVDQDAG TEPHTSEDEC
     EPIEAIAKFD YVGRSARELS FKKGASLLLY HRASEDWWEG RHNGIDGLVP HQYIVVQDMD
     DTFSDTLSQK ADSEASSGPV TEDKSSSKDM NSPTDRHSDS YLARQRKRGE PPPPGRRPGR
     TSDGHCPLHP PHALSNSSID LGSPNLASHP RGLLQNRGLN NDSPERRRRP GHGSLTNISR
     HDSLKKIDSP PIRRSTSSGQ YTGFNDHKPL DPETIAQDIE ETMNTALNEL RELERQSTVK
     HAPDVVLDTL EQVKNSPTPA TSTESLSPLH NVALRGSEPQ IRRSTSSSSE TMSTFKPMVA
     PRMGVQLKPP ALRPKPAVLP KTNPTMGPAA PSQGPTDKSC TM
//
ID   BMP2K_MOUSE             Reviewed;        1138 AA.
AC   Q91Z96; Q8C8L7;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=BMP-2-inducible protein kinase;
DE            Short=BIKe;
DE            EC=2.7.11.1;
GN   Name=Bmp2k; Synonyms=Bike;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   MEDLINE=21551155; PubMed=11500515; DOI=10.1074/jbc.M106163200;
RA   Kearns A.E., Donohue M.M., Sanyal B., Demay M.B.;
RT   "Cloning and characterization of a novel protein kinase that impairs
RT   osteoblast differentiation in vitro.";
RL   J. Biol. Chem. 276:42213-42218(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1010 AND SER-1013, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1010; SER-1012 AND
RP   SER-1013, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1010; SER-1012 AND
RP   SER-1013, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May be involved in osteoblast differentiation.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q91Z96-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q91Z96-2; Sequence=VSP_008094, VSP_008095;
CC   -!- TISSUE SPECIFICITY: Expressed in spleen, kidney, lung, brain,
CC       heart, diaphragm and calvaria but not in liver.
CC   -!- PTM: Autophosphorylated.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY050249; AAK91585.1; -; mRNA.
DR   EMBL; AK046752; BAC32854.1; -; mRNA.
DR   IPI; IPI00313513; -.
DR   IPI; IPI00336574; -.
DR   RefSeq; NP_542439.1; NM_080708.1.
DR   UniGene; Mm.281490; -.
DR   UniGene; Mm.460821; -.
DR   UniGene; Mm.480237; -.
DR   ProteinModelPortal; Q91Z96; -.
DR   SMR; Q91Z96; 37-316.
DR   STRING; Q91Z96; -.
DR   PhosphoSite; Q91Z96; -.
DR   PRIDE; Q91Z96; -.
DR   Ensembl; ENSMUST00000035635; ENSMUSP00000037970; ENSMUSG00000034663.
DR   GeneID; 140780; -.
DR   KEGG; mmu:140780; -.
DR   UCSC; uc008yfo.1; mouse.
DR   UCSC; uc008yfp.1; mouse.
DR   CTD; 140780; -.
DR   MGI; MGI:2155456; Bmp2k.
DR   GeneTree; ENSGT00510000046552; -.
DR   HOGENOM; HBG283730; -.
DR   HOVERGEN; HBG050703; -.
DR   InParanoid; Q91Z96; -.
DR   OMA; RRPDIFQ; -.
DR   OrthoDB; EOG4D52X1; -.
DR   PhylomeDB; Q91Z96; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 369977; -.
DR   ArrayExpress; Q91Z96; -.
DR   Bgee; Q91Z96; -.
DR   CleanEx; MM_BMP2K; -.
DR   Genevestigator; Q91Z96; -.
DR   GermOnline; ENSMUSG00000034663; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019208; F:phosphatase regulator activity; IDA:MGI.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0030500; P:regulation of bone mineralization; IDA:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1   1138       BMP-2-inducible protein kinase.
FT                                /FTId=PRO_0000085664.
FT   DOMAIN       48    313       Protein kinase.
FT   NP_BIND      54     62       ATP (By similarity).
FT   COMPBIAS    421    546       Gln/His-rich.
FT   ACT_SITE    177    177       Proton acceptor (By similarity).
FT   BINDING      76     76       ATP (By similarity).
FT   MOD_RES      10     10       Phosphoserine (By similarity).
FT   MOD_RES     375    375       Phosphoserine (By similarity).
FT   MOD_RES     667    667       Phosphoserine (By similarity).
FT   MOD_RES     672    672       Phosphoserine (By similarity).
FT   MOD_RES     715    715       Phosphoserine (By similarity).
FT   MOD_RES     927    927       Phosphoserine (By similarity).
FT   MOD_RES     960    960       Phosphoserine (By similarity).
FT   MOD_RES     983    983       Phosphothreonine (By similarity).
FT   MOD_RES    1010   1010       Phosphoserine.
FT   MOD_RES    1012   1012       Phosphoserine.
FT   MOD_RES    1013   1013       Phosphoserine.
FT   MOD_RES    1022   1022       Phosphoserine (By similarity).
FT   MOD_RES    1087   1087       Phosphoserine (By similarity).
FT   MOD_RES    1091   1091       Phosphoserine (By similarity).
FT   VAR_SEQ     638    649       NRLGASTPSDKT -> SKGHLKAYFASQ (in isoform
FT                                2).
FT                                /FTId=VSP_008094.
FT   VAR_SEQ     650   1138       Missing (in isoform 2).
FT                                /FTId=VSP_008095.
SQ   SEQUENCE   1138 AA;  126185 MW;  8EDDE02F1333840D CRC64;
     MKKFSRMPKS EGSGGGAAAG GAAGGGLGGG FASSSMGVRV FAVGRYQVTL EESLAEGGFS
     TVFLVRTHSG IRCALKRMYV NNTPDLNICK REITIMKELS GHKNIVGYLD CAVNSISDNV
     WEVLILMEYC RAGQVVNQMN KKLQTGFTES EVLQIFCDTC EAVARLHQCK TPIIHRDLKV
     ENILLNDAGN YVLCDFGSAT NKFLNPQKDG VNVVEEEIKK YTTLSYRAPE MINLYGGKPI
     TTKADIWALG CLLYKLCFFT LPFGESQVAI CDGSFTIPDN SRYSHNVHCL IRFMLEPDPE
     CRPDIFQVSY FAFKFAKKDC PVSNINNSFL PSTLPEPMTA TEAAARKSQM KARITDTIGP
     TETSIAPRQR PKANSTAATS SVLTIQSSAT PVKVPAPGEF SNHKPKGALR PGNGSEVLMV
     QGPPQQPPQQ HRVLQQLQQG DWRLQQLHLH RHPHHHHQQQ QQQQQQQQQQ QLQQQQQQQQ
     QLLQNAYLQQ YQHAMHQQHI LQQQFLMHSV YQPQPPASQY PAMMQQYQQA FLQQQMLARH
     QQPAQQVSPE YLTSPQEFSP ALVSYASSLP AQVGTIVDSS YGANRSVAEK EAVANFTNQK
     TISHPPDMSG WNPFGEDNFS KLTEEELLDR EFDLLRSNRL GASTPSDKTV DLPPAPHSRP
     PEEPFASVPF ISHSGSPEKK TTEHSPNQKS ITANLTKNGG SSPLCKDQRA GKKTSENPVI
     RGQVQKGHDD SESDFESDPP SPKSSEEEQE DEDAQGEHGD FNDDDTEPEN LGHRPLLMDS
     EDEEEDDKHS SDSECEQAKT KRGDTSSLRR DKPGVAPDTA LLTPARSPAD ALTPSQEFDV
     FGAVPFFAAP APQSLQHRGD GKNLSQHAFP EQEDFDVFTK APFNKKVSVQ DWPAVGPDAR
     PLPARPRSVD IFGSTPFQPF SVSASKSESK EDVFGLVPFE EITGSQQQQK VKQRSLQKLS
     SRQRRTKQDV SKSNGKRHHG TPTSAKKTLK PPYRTPERAR RHKKVGRRDS QSSNEFLTIS
     DSKENISVAL TDGKDRASVL PSDESLLDPF GAKPFHPPDL WHQPHQGLSD ICVDHTTILP
     GRPRQNSVHG SFHSAETLRM DDFGAVPFTE LVVQSVTPQQ SQPVELDPFG AAPFPSKQ
//
ID   VANG2_MOUSE             Reviewed;         521 AA.
AC   Q91ZD4; Q923Z8;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 3.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Vang-like protein 2;
DE   AltName: Full=Loop-tail protein 1;
DE   AltName: Full=Loop-tail-associated protein;
DE   AltName: Full=Van Gogh-like protein 2;
GN   Name=Vangl2; Synonyms=Lpp1, Ltap;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT LP
RP   ASN-464.
RC   STRAIN=C57BL/6;
RX   MEDLINE=21566157; PubMed=11709546; DOI=10.1093/hmg/10.22.2593;
RA   Murdoch J.N., Doudney K., Paternotte C., Copp A.J., Stanier P.;
RT   "Severe neural tube defects in the loop-tail mouse result from
RT   mutation of Lpp1, a novel gene involved in floor plate
RT   specification.";
RL   Hum. Mol. Genet. 10:2593-2601(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP   AND VARIANTS LP GLU-255 AND ASN-464.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=21324747; PubMed=11431695; DOI=10.1038/90081;
RA   Kibar Z., Vogan K.J., Groulx N., Justice M.J., Underhill D.A.,
RA   Gros P.;
RT   "Ltap, a mammalian homolog of Drosophila Strabismus/Van Gogh, is
RT   altered in the mouse neural tube mutant loop-tail.";
RL   Nat. Genet. 28:251-255(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   DISEASE.
RX   PubMed=11440971;
RA   Henderson D.J., Conway S.J., Greene N.D.E., Gerrelli D., Murdoch J.N.,
RA   Anderson R.H., Copp A.J.;
RT   "Cardiovascular defects associated with abnormalities in midline
RT   development in the loop-tail mouse mutant.";
RL   Circ. Res. 89:6-12(2001).
RN   [5]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   MEDLINE=22621962; PubMed=12724779; DOI=10.1038/nature01618;
RA   Montcouquiol M., Rachel R.A., Lanford P.J., Copeland N.G.,
RA   Jenkins N.A., Kelley M.W.;
RT   "Identification of Vangl2 and Scrb1 as planar polarity genes in
RT   mammals.";
RL   Nature 423:173-177(2003).
RN   [6]
RP   INTERACTION WITH DVL1; DVL2 AND DVL3.
RX   PubMed=15456783; DOI=10.1074/jbc.M408675200;
RA   Torban E., Wang H.-J., Groulx N., Gros P.;
RT   "Independent mutations in mouse Vangl2 that cause neural tube defects
RT   in looptail mice impair interaction with members of the Dishevelled
RT   family.";
RL   J. Biol. Chem. 279:52703-52713(2004).
RN   [7]
RP   INTERACTION WITH MAGI3.
RX   PubMed=15195140; DOI=10.1038/sj.onc.1207817;
RA   Yao R., Natsume Y., Noda T.;
RT   "MAGI-3 is involved in the regulation of the JNK signaling pathway as
RT   a scaffold protein for frizzled and Ltap.";
RL   Oncogene 23:6023-6030(2004).
RN   [8]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=15637299; DOI=10.1161/01.RES.0000154912.08695.88;
RA   Phillips H.M., Murdoch J.N., Chaudhry B., Copp A.J., Henderson D.J.;
RT   "Vangl2 acts via RhoA signaling to regulate polarized cell movements
RT   during development of the proximal outflow tract.";
RL   Circ. Res. 96:292-299(2005).
RN   [9]
RP   INTERACTION WITH FZD3 AND SCRIB, AND TISSUE SPECIFICITY.
RX   PubMed=16687519; DOI=10.1523/JNEUROSCI.4680-05.2006;
RA   Montcouquiol M., Sans N., Huss D., Kach J., Dickman J.D., Forge A.,
RA   Rachel R.A., Copeland N.G., Jenkins N.A., Bogani D., Murdoch J.,
RA   Warchol M.E., Wenthold R.J., Kelley M.W.;
RT   "Asymmetric localization of Vangl2 and Fz3 indicate novel mechanisms
RT   for planar cell polarity in mammals.";
RL   J. Neurosci. 26:5265-5275(2006).
CC   -!- FUNCTION: Involved in the control of early morphogenesis and
CC       patterning of both axial midline structures and the development of
CC       neural plate. Plays a role in the regulation of planar cell
CC       polarity, particularly in the orientation of stereociliary bundles
CC       in the cochlea. Required for polarization and movement of
CC       myocardializing cells in the outflow tract and seems to act via
CC       RHOA signaling to regulate this process.
CC   -!- SUBUNIT: Interacts through its C-terminal region with the N-
CC       terminal half of DVL1, DVL2 and DVL3. The PDZ domain of DVL1, DVL2
CC       and DVL3 is required for the interaction. Variants Glu-255 and
CC       Asn-464 impair interaction with the DVL proteins. Also interacts
CC       with the PDZ domains of MAGI3, SCRIB/SCRB1 and FZD3.
CC   -!- INTERACTION:
CC       P51141:Dvl1; NbExp=1; IntAct=EBI-1750744, EBI-1538407;
CC       Q60838:Dvl2; NbExp=2; IntAct=EBI-1750744, EBI-641940;
CC       Q61062:Dvl3; NbExp=1; IntAct=EBI-1750744, EBI-1538450;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- TISSUE SPECIFICITY: Primarily expressed in the brain and
CC       epididymis. Not detected in the cochlea of Lp mice.
CC   -!- DEVELOPMENTAL STAGE: In the embryo, strongly expressed in the
CC       neuroectoderm from the earliest stages of neural induction through
CC       the late stages of neural tube closure. Detected in the dorso-
CC       ventral axis of the neural tube, but not in the floor plate.
CC       Expression is low at day E7; it peaks at E11, and it remains
CC       strong at E15 and E17. Also expressed in the cochlear epithelium
CC       at days E14.5 and E16.5. Detected at low levels in the outflow
CC       tract myocardium from E9.5 with levels increasing by E11.5.
CC   -!- DISEASE: Note=Defects in Vangl2 are a cause of the loop-tail (Lp)
CC       mutant phenotype. Heterozygous Lp mice exhibit a characteristic
CC       looped tail, while homozygous embryos show a completely open
CC       neural tube in the hindbrain and spinal region, a condition
CC       similar to the severe craniorachischisis defect in humans.
CC       Homozygotes also have complex cardiovascular defects including
CC       double-outlet right ventricle, perimembranous ventricular defects,
CC       double-sided aortic arch and associated abnormalities in the
CC       aortic arch arteries. Homozygotes show cytoplasmic accumulation of
CC       Vangl2 instead of the normal membrane localization, and Rhoa
CC       expression, which is detected in the mesenchymal cushion cells
CC       adjacent to the outflow tract, is lost in homozygotes. Homozygous
CC       embryos typically die shortly before or at birth.
CC   -!- SIMILARITY: Belongs to the Vang family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY035370; AAK63188.3; -; mRNA.
DR   EMBL; AF365875; AAK91927.1; -; mRNA.
DR   EMBL; BC052195; AAH52195.1; -; mRNA.
DR   IPI; IPI00154106; -.
DR   RefSeq; NP_277044.1; NM_033509.3.
DR   UniGene; Mm.36148; -.
DR   UniGene; Mm.392110; -.
DR   ProteinModelPortal; Q91ZD4; -.
DR   IntAct; Q91ZD4; 7.
DR   STRING; Q91ZD4; -.
DR   PRIDE; Q91ZD4; -.
DR   Ensembl; ENSMUST00000027837; ENSMUSP00000027837; ENSMUSG00000026556.
DR   Ensembl; ENSMUST00000111263; ENSMUSP00000106894; ENSMUSG00000026556.
DR   GeneID; 93840; -.
DR   KEGG; mmu:93840; -.
DR   UCSC; uc007dpi.1; mouse.
DR   CTD; 93840; -.
DR   MGI; MGI:2135272; Vangl2.
DR   GeneTree; ENSGT00390000012496; -.
DR   HOVERGEN; HBG058215; -.
DR   NextBio; 351697; -.
DR   ArrayExpress; Q91ZD4; -.
DR   Bgee; Q91ZD4; -.
DR   CleanEx; MM_VANGL2; -.
DR   Genevestigator; Q91ZD4; -.
DR   GermOnline; ENSMUSG00000026556; Mus musculus.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0060187; C:cell pole; IDA:MGI.
DR   GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0009952; P:anterior/posterior pattern formation; IMP:MGI.
DR   GO; GO:0045176; P:apical protein localization; IMP:MGI.
DR   GO; GO:0090103; P:cochlea morphogenesis; IMP:MGI.
DR   GO; GO:0060028; P:convergent extension involved in axis elongation; IMP:MGI.
DR   GO; GO:0022007; P:convergent extension involved in neural plate elongation; IMP:MGI.
DR   GO; GO:0048546; P:digestive tract morphogenesis; IGI:MGI.
DR   GO; GO:0048105; P:establishment of body hair planar orientation; IMP:MGI.
DR   GO; GO:0090177; P:establishment of planar polarity involved in neural tube closure; IMP:MGI.
DR   GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IMP:MGI.
DR   GO; GO:0001942; P:hair follicle development; IMP:MGI.
DR   GO; GO:0001947; P:heart looping; IMP:UniProtKB.
DR   GO; GO:0060122; P:inner ear receptor stereocilium organization; IMP:MGI.
DR   GO; GO:0060490; P:lateral sprouting involved in lung morphogenesis; IMP:MGI.
DR   GO; GO:0003149; P:membranous septum morphogenesis; IGI:MGI.
DR   GO; GO:0003150; P:muscular septum morphogenesis; IGI:MGI.
DR   GO; GO:0060488; P:orthogonal dichotomous subdivision of terminal units involved in lung branching morphogenesis; IMP:MGI.
DR   GO; GO:0003402; P:planar cell polarity pathway involved in axis elongation; IGI:MGI.
DR   GO; GO:0090179; P:planar cell polarity pathway involved in neural tube closure; IGI:MGI.
DR   GO; GO:0060489; P:planar dichotomous subdivision of terminal units involved in lung branching morphogenesis; IMP:MGI.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:MGI.
DR   GO; GO:0007266; P:Rho protein signal transduction; IMP:MGI.
DR   GO; GO:0035058; P:sensory cilium assembly; IGI:MGI.
DR   GO; GO:0048103; P:somatic stem cell division; IMP:MGI.
DR   GO; GO:0035019; P:somatic stem cell maintenance; IMP:MGI.
DR   GO; GO:0042060; P:wound healing; IGI:MGI.
DR   InterPro; IPR009539; Strabismus.
DR   PANTHER; PTHR20886; Strabismus; 1.
DR   Pfam; PF06638; Strabismus; 1.
DR   PIRSF; PIRSF007991; Strabismus; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Disease mutation; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    521       Vang-like protein 2.
FT                                /FTId=PRO_0000186196.
FT   TOPO_DOM      1    108       Cytoplasmic (Potential).
FT   TRANSMEM    109    129       Helical; Name=1; (Potential).
FT   TOPO_DOM    130    147       Extracellular (Potential).
FT   TRANSMEM    148    168       Helical; Name=2; (Potential).
FT   TOPO_DOM    169    178       Cytoplasmic (Potential).
FT   TRANSMEM    179    199       Helical; Name=3; (Potential).
FT   TOPO_DOM    200    217       Extracellular (Potential).
FT   TRANSMEM    218    238       Helical; Name=4; (Potential).
FT   TOPO_DOM    239    521       Cytoplasmic (Potential).
FT   VARIANT     255    255       D -> E (in Lp).
FT   VARIANT     464    464       S -> N (in Lp).
SQ   SEQUENCE   521 AA;  59771 MW;  94ECEF3EE63DF5BC CRC64;
     MDTESQYSGY SYKSGHSRSS RKHRDRRDRH RSKSRDGSRG DKSVTIQAPG EPLLDNESTR
     GDERDDNWGE TTTVVTGTSE HSISHDDLTR IAKDMEDSVP LDCSRHLGVA AGAILALLSF
     LTPLAFLLLP PLLWREELEP CGTACEGLFI SVAFKLLILL LGSWALFFRR PKASLPRVFV
     LRALLMVLVF LLVISYWLFY GVRILDARER SYQGVVQFAV SLVDALLFVH YLAVVLLELR
     QLQPQFTLKV VRSTDGASRF YNVGHLSIQR VAVWILEKYY HDFPVYNPAL LNLPKSVLAK
     KVSGFKVYSL GEENSTNNST GQSRAVIAAA ARRRDNSHNE YYYEEAEHER RVRKRRARLV
     VAVEEAFTHI KRLQEEEQKN PREVMDPREA AQAIFASMAR AMQKYLRTTK QQPYHTMESI
     LQHLEFCITH DMTPKAFLER YLAAGPTIQY HKERWLAKQW TLVSEEPVTN GLKDGIVFLL
     KRQDFSLVVS TKKVPFFKLS EEFVDPKSHK FVMRLQSETS V
//
ID   CELR3_MOUSE             Reviewed;        3301 AA.
AC   Q91ZI0; Q9ESD0;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Cadherin EGF LAG seven-pass G-type receptor 3;
DE   Flags: Precursor;
GN   Name=Celsr3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6;
RX   MEDLINE=21839555; PubMed=11850187; DOI=10.1016/S0925-4773(01)00623-2;
RA   Tissir F., De-Backer O., Goffinet A.M., Lambert de Rouvroit C.A.;
RT   "Developmental expression profiles of Celsr (Flamingo) genes in the
RT   mouse.";
RL   Mech. Dev. 112:157-160(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2574-3046, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=21534880; PubMed=11677057; DOI=10.1016/S0925-4773(01)00515-9;
RA   Formstone C.J., Little P.F.R.;
RT   "The flamingo-related mouse Celsr family (Celsr1-3) genes exhibit
RT   distinct patterns of expression during embryonic development.";
RL   Mech. Dev. 109:91-94(2001).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=20253755; PubMed=10790539; DOI=10.1007/s003350010073;
RA   Formstone C.J., Barclay J., Rees M., Little P.F.R.;
RT   "Chromosomal localization of Celsr2 and Celsr3 in the mouse; Celsr3 is
RT   a candidate for the tippy (tip) lethal mutant on chromosome 9.";
RL   Mamm. Genome 11:392-394(2000).
CC   -!- FUNCTION: Receptor that may have an important role in cell/cell
CC       signaling during nervous system formation.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in the CNS and in the eye.
CC   -!- DEVELOPMENTAL STAGE: Predominantly expressed in the CNS, the
CC       emerging dorsal root ganglia and cranial ganglia. In the CNS,
CC       expression is uniform along the rostrocaudal axis. No expression
CC       is detected until somite stages. Between E10 and E12, expression
CC       is strong in the marginal zone (MZ), and lower in the ventricular
CC       zone (VZ). At E15, expression is restricted to the brain and
CC       olfactory epithelium. In the brain, it is low in VZ but strong in
CC       external fields, particularly those with ongoing migration, such
CC       as the telencephalic cortical plate, the olfactory bulb, the
CC       cerebellum and the tectum. In the newborn and postnatal stages,
CC       expression is high in differentiated neuronal fields.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       LN-TM7 subfamily.
CC   -!- SIMILARITY: Contains 9 cadherin domains.
CC   -!- SIMILARITY: Contains 7 EGF-like domains.
CC   -!- SIMILARITY: Contains 1 GPS domain.
CC   -!- SIMILARITY: Contains 1 laminin EGF-like domain.
CC   -!- SIMILARITY: Contains 2 laminin G-like domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG17057.1; Type=Frameshift; Positions=2575, 2578;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF427498; AAL25099.1; -; mRNA.
DR   EMBL; AF188752; AAG17057.1; ALT_FRAME; mRNA.
DR   IPI; IPI00284505; -.
DR   RefSeq; NP_536685.2; NM_080437.2.
DR   UniGene; Mm.39945; -.
DR   ProteinModelPortal; Q91ZI0; -.
DR   SMR; Q91ZI0; 294-1262, 1366-1505, 1712-1748, 1924-2103.
DR   STRING; Q91ZI0; -.
DR   PhosphoSite; Q91ZI0; -.
DR   PRIDE; Q91ZI0; -.
DR   Ensembl; ENSMUST00000024238; ENSMUSP00000024238; ENSMUSG00000023473.
DR   GeneID; 107934; -.
DR   KEGG; mmu:107934; -.
DR   UCSC; uc009rrb.1; mouse.
DR   CTD; 107934; -.
DR   MGI; MGI:1858236; Celsr3.
DR   GeneTree; ENSGT00580000081266; -.
DR   HOGENOM; HBG357942; -.
DR   HOVERGEN; HBG050887; -.
DR   InParanoid; Q91ZI0; -.
DR   OrthoDB; EOG4C87RG; -.
DR   NextBio; 359739; -.
DR   ArrayExpress; Q91ZI0; -.
DR   Bgee; Q91ZI0; -.
DR   Genevestigator; Q91ZI0; -.
DR   GermOnline; ENSMUSG00000023473; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007413; P:axonal fasciculation; IMP:MGI.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   InterPro; IPR022624; DUF3497.
DR   InterPro; IPR006209; EGF.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR002049; EGF_laminin.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR001879; GPCR_2_extracellular_dom.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR   InterPro; IPR000203; GPS_dom.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR012680; Laminin_G_2.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 9.
DR   Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 2.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF00028; Cadherin; 8.
DR   Pfam; PF12003; DUF3497; 1.
DR   Pfam; PF00008; EGF; 3.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF02793; HRM; 1.
DR   Pfam; PF00053; Laminin_EGF; 1.
DR   Pfam; PF02210; Laminin_G_2; 2.
DR   PRINTS; PR00205; CADHERIN.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   SMART; SM00112; CA; 9.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00180; EGF_Lam; 1.
DR   SMART; SM00303; GPS; 1.
DR   SMART; SM00008; HormR; 1.
DR   SMART; SM00282; LamG; 2.
DR   SUPFAM; SSF49313; Cadherin; 9.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00232; CADHERIN_1; 7.
DR   PROSITE; PS50268; CADHERIN_2; 8.
DR   PROSITE; PS00022; EGF_1; 5.
DR   PROSITE; PS01186; EGF_2; 4.
DR   PROSITE; PS50026; EGF_3; 6.
DR   PROSITE; PS01248; EGF_LAM_1; 1.
DR   PROSITE; PS50027; EGF_LAM_2; 1.
DR   PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG.
DR   PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR   PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE   2: Evidence at transcript level;
KW   Calcium; Cell membrane; Developmental protein; Disulfide bond;
KW   EGF-like domain; G-protein coupled receptor; Glycoprotein;
KW   Hydroxylation; Laminin EGF-like domain; Membrane; Receptor; Repeat;
KW   Signal; Transducer; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     31       Potential.
FT   CHAIN        32   3301       Cadherin EGF LAG seven-pass G-type
FT                                receptor 3.
FT                                /FTId=PRO_0000012919.
FT   TOPO_DOM     32   2531       Extracellular (Potential).
FT   TRANSMEM   2532   2552       Helical; Name=1; (Potential).
FT   TOPO_DOM   2553   2563       Cytoplasmic (Potential).
FT   TRANSMEM   2564   2584       Helical; Name=2; (Potential).
FT   TOPO_DOM   2585   2592       Extracellular (Potential).
FT   TRANSMEM   2593   2613       Helical; Name=3; (Potential).
FT   TOPO_DOM   2614   2634       Cytoplasmic (Potential).
FT   TRANSMEM   2635   2655       Helical; Name=4; (Potential).
FT   TOPO_DOM   2656   2673       Extracellular (Potential).
FT   TRANSMEM   2674   2694       Helical; Name=5; (Potential).
FT   TOPO_DOM   2695   2716       Cytoplasmic (Potential).
FT   TRANSMEM   2717   2737       Helical; Name=6; (Potential).
FT   TOPO_DOM   2738   2744       Extracellular (Potential).
FT   TRANSMEM   2745   2765       Helical; Name=7; (Potential).
FT   TOPO_DOM   2766   3301       Cytoplasmic (Potential).
FT   DOMAIN      317    424       Cadherin 1.
FT   DOMAIN      425    536       Cadherin 2.
FT   DOMAIN      537    642       Cadherin 3.
FT   DOMAIN      643    747       Cadherin 4.
FT   DOMAIN      748    849       Cadherin 5.
FT   DOMAIN      850    952       Cadherin 6.
FT   DOMAIN      953   1058       Cadherin 7.
FT   DOMAIN     1059   1160       Cadherin 8.
FT   DOMAIN     1161   1257       Cadherin 9.
FT   DOMAIN     1366   1424       EGF-like 1; calcium-binding.
FT   DOMAIN     1426   1460       EGF-like 2; calcium-binding.
FT   DOMAIN     1464   1503       EGF-like 3; calcium-binding.
FT   DOMAIN     1504   1708       Laminin G-like 1.
FT   DOMAIN     1711   1747       EGF-like 4; calcium-binding.
FT   DOMAIN     1751   1933       Laminin G-like 2.
FT   DOMAIN     1935   1971       EGF-like 5; calcium-binding.
FT   DOMAIN     1972   2002       EGF-like 6; calcium-binding.
FT   DOMAIN     2003   2042       EGF-like 7; calcium-binding.
FT   DOMAIN     2044   2079       EGF-like 8; calcium-binding.
FT   DOMAIN     2066   2113       Laminin EGF-like.
FT   DOMAIN     2468   2520       GPS.
FT   COMPBIAS   2720   2724       Poly-Leu.
FT   MOD_RES    1952   1952       (3R)-3-hydroxyaspartate (Potential).
FT   CARBOHYD    623    623       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    838    838       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1173   1173       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1213   1213       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1308   1308       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1318   1318       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1638   1638       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1702   1702       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1759   1759       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2042   2042       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2166   2166       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2185   2185       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2375   2375       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2465   2465       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2497   2497       N-linked (GlcNAc...) (Potential).
FT   DISULFID   1370   1381       By similarity.
FT   DISULFID   1375   1412       By similarity.
FT   DISULFID   1414   1423       By similarity.
FT   DISULFID   1430   1441       By similarity.
FT   DISULFID   1435   1450       By similarity.
FT   DISULFID   1452   1459       By similarity.
FT   DISULFID   1468   1479       By similarity.
FT   DISULFID   1473   1489       By similarity.
FT   DISULFID   1491   1502       By similarity.
FT   DISULFID   1682   1708       By similarity.
FT   DISULFID   1715   1726       By similarity.
FT   DISULFID   1720   1735       By similarity.
FT   DISULFID   1737   1746       By similarity.
FT   DISULFID   1904   1933       By similarity.
FT   DISULFID   1939   1950       By similarity.
FT   DISULFID   1944   1959       By similarity.
FT   DISULFID   1961   1970       By similarity.
FT   DISULFID   1974   1985       By similarity.
FT   DISULFID   1979   1997       By similarity.
FT   DISULFID   1999   2008       By similarity.
FT   DISULFID   2016   2029       By similarity.
FT   DISULFID   2031   2041       By similarity.
FT   DISULFID   2048   2063       By similarity.
FT   DISULFID   2050   2066       By similarity.
FT   DISULFID   2068   2078       By similarity.
FT   DISULFID   2087   2096       By similarity.
FT   DISULFID   2099   2111       By similarity.
FT   CONFLICT   2713   2713       L -> LR (in Ref. 2; AAG17057).
FT   CONFLICT   3024   3024       R -> P (in Ref. 2; AAG17057).
SQ   SEQUENCE   3301 AA;  358462 MW;  A6B18F2DF7F4DEB6 CRC64;
     MARRPLWWGL PGPSTPVLLL LLLSLFPFSR EELGGGGDQD WDPGVATTTG PRAQIGSGAV
     ALCPESPGVW EDGDPGLGVR EPVFMRLRVG RQNARNGRGA PEQPNAEVVV QALGSREQEA
     GQGPGYLLCW HPEISSCGRT GPLRRGSLPL DALSPGDSDL RNSSPHPSEL LAQPDGSRPV
     AFQRNARRSI RKRVETSRCC GKLWEPGHKG QGERSATSTV ERGPFRRDCL PGSLGSGLGE
     DSAPRAVRTA PTPGSAPRES RTAPGRMRSR GLFRRRFLFE RPGPRPPGFP TGPEAKQILS
     TNQARPRRAA NRHPQFPQYN YQTLVPENEA AGTSVLRVVA QDPDPGEAGR LIYSLAALMN
     SRSLELFSID PQSGLIRTAA ALDRESMERH YLRVTAQDHG SPRLSATTMV AVTVADRNDH
     APVFEQAQYR ETLRENVEEG YPILQLRATD GDAPPNANLR YRFVGSPAVR TAAAAAFEID
     PRSGLISTSG RVDREHMESY ELVVEASDQG QEPGPRSATV RVHITVLDEN DNAPQFGEKR
     YVAQVREDVR PHTVVLRVTA TDKDKDANGL VHYNIISGNS RGHFAIDSLT GEIQVMAPLD
     FEAEREYALR IRAQDAGRPP LSNNTGLASI QVVDINDHAP IFVSTPFQVS VLENAPLGHS
     VIHIQAVDAD HGENSRLEYS LTGVASDTPF VINSATGWVS VSGPLDRESV EHYFFGVEAR
     DHGSPPLSAS ASVTVTVLDV NDNRPEFTMK EYHLRLNEDA AVGTSVVSVT AVDRDANSAI
     SYQITGGNTR NRFAISTQGG VGLVTLALPL DYKQERYFKL VLTASDRALH DHCYVHINIT
     DANTHRPVFQ SAHYSVSMNE DRPVGSTVVV ISASDDDVGE NARITYLLED NLPQFRIDAD
     SGAITLQAPL DYEDQVTYTL AITARDNGIP QKADTTYVEV MVNDVNDNAP QFVASHYTGL
     VSEDAPPFTS VLQISATDRD AHANGRVQYT FQNGEDGDGD FTIEPTSGIV RTVRRLDREA
     VPVYELTAYA VDRGVPPLRT PVSIQVTVQD VNDNAPVFPA EEFEVRVKEN SIVGSVVAQI
     TAVDPDDGPN AHIMYQIVEG NIPELFQMDI FSGELTALID LDYEARQEYV IVVQATSAPL
     VSRATVHVRL VDQNDNSPVL NNFQILFNNY VSNRSDTFPS GIIGRIPAYD PDVSDHLFYS
     FERGNELQLL VVNRTSGELR LSRKLDNNRP LVASMLVTVT DGLHSVTAQC VLRVVIITEE
     LLANSLTVRL ENMWQERFLS PLLGHFLEGV AAVLATPTED VFIFNIQNDT DVGGTVLNVS
     FSALAPRGAG AGAAGPWFSS EELQEQLYVR RAALAARSLL DVLPFDDNVC LREPCENYMK
     CVSVLRFDSS APFLASTSTL FRPIQPIAGL RCRCPPGFTG DFCETELDLC YSNPCRNGGA
     CARREGGYTC VCRPRFTDCE LDTEAGRCVP GVCRNGGTCT NAPNGGFRCQ CPAGGAFEGP
     RCEVAARSFP PSSFVMFRGL RQRFHLTLSL SFATVQPSGL LFYNGRLNEK HDFLALELVA
     GQVRLTYSTG ESNTVVSPTV PGGLSDGQWH TVHLRYYNKP RTDALGGAQG PSKDKVAVLS
     VDDCNVAVAL QFGAEIGNYS CAAAGVQTSS KKSLDLTGPL LLGGVPNLPE NFPVSHKDFI
     GCMRDLHIDG RRMDMAAFVA NNGTMAGCQA KSHFCASGPC KNNGFCSERW GGFSCDCPVG
     FGGKDCRLTM AHPYHFQGNG TLSWDFGNDM AVSVPWYLGL SFRTRATKGI LMQVQLGPHS
     VLLCKLDRGL LSVTLNRASG HTVHLLLDQM TVSDGRWHDL RLELQEEPGG RRGHHIFMVS
     LDFTLFQDTM AMGGELQGLK VKQLHVGGLP PSSKEEGHQG LVGCIQGVWI GFTPFGSSAL
     LPPSHRVNVE PGCTVTNPCA SGPCPPHADC KDLWQTFSCT CRPGYYGPGC VDACLLNPCQ
     NQGSCRHLQG APHGYTCDCV SGYFGQHCEH RVDQQCPRGW WGSPTCGPCN CDVHKGFDPN
     CNKTNGQCHC KEFHYRPRGS DSCLPCDCYP VGSTSRSCAP HSGQCPCRPG ALGRQCNSCD
     SPFAEVTASG CRVLYDACPK SLRSGVWWPQ TKFGVLATVP CPRGALGAAV RLCDEDQGWL
     EPDLFNCTSP AFRELSLLLD GLELNKTALD TVEAKKLAQR LREVTGQTDH YFSQDVRVTA
     RLLAYLLAFE SHQQGFGLTA TQDAHFNENL LWAGSALLAP ETGHLWAALG QRAPGGSPGS
     AGLVQHLEEY AATLARNMEL TYLNPVGLVT PNIMLSIDRM EHPSSTQGAR RYPRYHSNLF
     RGQDAWDPHT HVLLPSQASQ PSPSEVLPTS SNAENATASS VVSPPAPLEP ESEPGISIVI
     LLVYRALGGL LPAQFQAERR GARLPQNPVM NSPVVSVAVF HGRNFLRGVL VSPINLEFRL
     LQTANRSKAI CVQWDPPGPT DQHGMWTARD CELVHRNGSH ARCRCSRTGT FGVLMDASPR
     ERLEGDLELL AVFTHVVVAV SVTALVLTAA VLLSLRSLKS NVRGIHANVA AALGVAELLF
     LLGIHRTHNQ LLCTAVAILL HYFFLSTFAW LLVQGLHLYR MQVEPRNVDR GAMRFYHALG
     WGVPAVLLGL AVGLDPEGYG NPDFCWISIH EPLIWSFAGP IVLVIVMNGT MFLLAARTSC
     STGQREAKKT SVLTLRSSFL LLLLVSASWL FGLLAVNHSI LAFHYLHAGL CGLQGLAVLL
     LFCVLNADAR AAWTPACLGK KAAPEETRPA PGPGSGAYNN TALFEESGLI RITLGASTVS
     SVSSARSGRA QDQDSQRGRS YLRDNVLVRH GSTAEHTERS LQAHAGPTDL DVAMFHRDAG
     ADSDSDSDLS LEEERSLSIP SSESEDNGRT RGRFQRPLRR AAQSERLLAH PKDVDGNDLL
     SYWPALGECE AAPCALQAWG SERRLGLDSN KDAANNNQPE LALTSGDETS LGRAQRQRKG
     ILKNRLQYPL VPQSRGTPEL SWCRAATLGH RAVPAASYGR IYAGGGTGSL SQPASRYSSR
     EQLDLLLRRQ LSKERLEEVP VPAPVLHPLS RPGSQERLDT APARLEARDR GSTLPRRQPP
     RDYPGTMAGR FGSRDALDLG APREWLSTLP PPRRNRDLDP QHPPLPLSPQ RQLSRDPLLP
     SRPLDSLSRI SNSREGLDQV PSRHPSREAL GPAPQLLRAR EDPASGPSHG PSTEQLDILS
     SILASFNSSA LSSVQSSSTP SGPHTTATAS ALGPSTPRSA TSHSISELSP DSEVPRSEGH
     S
//
ID   SH2B1_MOUSE             Reviewed;         756 AA.
AC   Q91ZM2; O54867; Q05DJ7; Q792R7; Q91ZM3; Q91ZV5; Q9WVM5;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=SH2B adapter protein 1;
DE   AltName: Full=Pro-rich, PH and SH2 domain-containing signaling mediator;
DE            Short=PSM;
DE   AltName: Full=SH2 domain-containing protein 1B;
DE   AltName: Full=SH2-B PH domain-containing signaling mediator 1;
GN   Name=Sh2b1; Synonyms=Sh2bpsm1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP   INTERACTION WITH INSR.
RX   MEDLINE=98158317; PubMed=9498552;
RA   Riedel H., Wang J., Hansen H., Yousaf N.;
RT   "PSM, an insulin-dependent, pro-rich, PH, SH2 domain containing
RT   partner of the insulin receptor.";
RL   J. Biochem. 122:1105-1113(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), ALTERNATIVE SPLICING (ISOFORMS
RP   1; 2 AND 3), TISSUE SPECIFICITY, AND INTERACTION WITH INSR AND ISR1.
RX   MEDLINE=20063688; PubMed=10594240; DOI=10.1007/s003359901183;
RA   Nelms K., O'Neill T.J., Li S., Hubbard S.R., Gustafson T.A.,
RA   Paul W.E.;
RT   "Alternative splicing, gene localization, and binding of SH2-B to the
RT   insulin receptor kinase domain.";
RL   Mamm. Genome 10:1160-1167(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), FUNCTION, AND
RP   PHOSPHORYLATION.
RC   TISSUE=Brain;
RX   MEDLINE=21538785; PubMed=11502739; DOI=10.1074/jbc.M104191200;
RA   Yousaf N., Deng Y., Kang Y., Riedel H.;
RT   "Four PSM/SH2-B alternative splice variants and their differential
RT   roles in mitogenesis.";
RL   J. Biol. Chem. 276:40940-40948(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 518-631, AND INTERACTION WITH INSR AND
RP   IGF1R.
RX   MEDLINE=98123072; PubMed=9452421; DOI=10.1074/jbc.273.6.3136;
RA   Wang J., Riedel H.;
RT   "Insulin-like growth factor-I receptor and insulin receptor
RT   association with a Src homology-2 domain-containing putative
RT   adapter.";
RL   J. Biol. Chem. 273:3136-3139(1998).
RN   [7]
RP   FUNCTION IN GH SIGNALING, AND INTERACTION WITH JAK2.
RC   TISSUE=Kidney;
RX   MEDLINE=98001592; PubMed=9343427;
RA   Rui L., Mathews L.S., Hotta K., Gustafson T.A., Carter-Su C.;
RT   "Identification of SH2-Bbeta as a substrate of the tyrosine kinase
RT   JAK2 involved in growth hormone signaling.";
RL   Mol. Cell. Biol. 17:6633-6644(1997).
RN   [8]
RP   FUNCTION IN LEPTIN SIGNALING, AND INTERACTION WITH JAK2; ISR1 AND
RP   ISR2.
RX   PubMed=15316008; DOI=10.1074/jbc.M408495200;
RA   Duan C., Li M., Rui L.;
RT   "SH2-B promotes insulin receptor substrate 1 (IRS1)- and IRS2-mediated
RT   activation of the phosphatidylinositol 3-kinase pathway in response to
RT   leptin.";
RL   J. Biol. Chem. 279:43684-43691(2004).
RN   [9]
RP   FUNCTION IN LEPTIN SIGNALING.
RX   PubMed=16098827; DOI=10.1016/j.cmet.2005.07.004;
RA   Ren D., Li M., Duan C., Rui L.;
RT   "Identification of SH2-B as a key regulator of leptin sensitivity,
RT   energy balance, and body weight in mice.";
RL   Cell Metab. 2:95-104(2005).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND SER-127, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 519-627 IN COMPLEX WITH JAK2.
RX   PubMed=16824542; DOI=10.1016/j.jmb.2006.05.070;
RA   Hu J., Hubbard S.R.;
RT   "Structural basis for phosphotyrosine recognition by the Src homology-
RT   2 domains of the adapter proteins SH2-B and APS.";
RL   J. Mol. Biol. 361:69-79(2006).
CC   -!- FUNCTION: Adapter protein for several members of the tyrosine
CC       kinase receptor family. Involved in multiple signaling pathways
CC       mediated by Janus kinase (JAK) and receptor tyrosine kinases,
CC       including the receptors of insulin (INS), insulin-like growth
CC       factor I (IGF1), nerve growth factor (NGF), brain-derived
CC       neurotrophic factor (BDNF), glial cell line-derived neurotrophic
CC       factor (GDNF), platelet-derived growth factor (PDGF) and
CC       fibroblast growth factors (FGFs). In growth hormone (GH)
CC       signaling, autophosphorylated ('Tyr-813') JAK2 recruits SH2B1,
CC       which in turn is phosphorylated by JAK2 on tyrosine residues.
CC       These phosphotyrosines form potential binding sites for other
CC       signaling proteins. GH also promotes serine/threonine
CC       phosphorylation of SH2B1 and these phosphorylated residues may
CC       serve to recruit other proteins to the GHR-JAK2-SH2B1 complexes,
CC       such as RAC1. In leptin (LEP) signaling, binds to and potentiates
CC       the activation of JAK2 by globally enhancing downstream pathways.
CC       In response to leptin, binds simultaneously to both, JAK2 and IRS1
CC       or IRS2, thus mediating formation of a complex of JAK2, SH2B1 and
CC       IRS1 or IRS2. Mediates tyrosine phosphorylation of IRS1 and IRS2,
CC       resulting in activation of the PI 3-kinase pathway. Acts as
CC       positive regulator of NGF-mediated activation of the Akt/Forkhead
CC       pathway; prolongs NGF-induced phosphorylation of AKT1 on 'Ser-473'
CC       and AKT1 enzymatic activity. Enhances the kinase activity of the
CC       cytokine receptor-associated tyrosine kinase JAK2 and of other
CC       receptor tyrosine kinases, such as FGFR3 and NTRK1. For JAK2, the
CC       mechanism seems to involve dimerization of both, SH2B1 and JAK2.
CC       Enhances RET phosphorylation and kinase activity (By similarity).
CC       Isoforms seem to be differentially involved in IGF-I and PDGF-
CC       induced mitogenesis, according the order: isoform 3 > isoform 4 >
CC       isoform 1 > isoform 2.
CC   -!- SUBUNIT: Self-associates. Homopentamer (By similarity). Forms a
CC       heteromultimeric complex with SH2B2 (By similarity). Interacts
CC       with SH2B2. Isoform 1 interacts via its SH2 domain with JAK2.
CC       Isoform 2 interacts via its SH2 domain and its N-terminus with
CC       JAK2; the SH2 domain is required for the major interaction with
CC       JAK2 phosphorylated on tyrosine residues; the N-terminus provides
CC       a low-affinity binding to JAK2 independent of JAK2
CC       phosphorylation. Isoform 3 interacts via its SH2 domain with JAK2.
CC       Isoform 1 interacts via its SH2 domain with INSR; the interaction
CC       requires receptor activation. Isoform 3 interacts via its SH2
CC       domain with INSR; the interaction requires receptor activation and
CC       requires INSR phosphorylation at 'Tyr-1175'. Isoform 1 interacts
CC       with IGF1R; the interaction requires receptor activation. Isoform
CC       2 interacts via its SH2 domain with FGFR3; the interaction
CC       requires FGFR3 'Tyr-719' and 'Tyr-755'. Isoform 2 interacts with
CC       RET; the interaction requires RET kinase activity and RET 'Tyr-
CC       982'. Isoform 2 interacts with RAC1. Isoform 2 interacts with
CC       PDGFRA and/or PDGFRB; the interaction requires receptor
CC       activation. Interacts with ISR1 and ISR2. Isoform 3 is probably
CC       part of a complex consisting of INSR, ISR1 and SH2B1. Probably
CC       part of a ternary complex consisting of SH2B1, JAK2 and ISR1 or
CC       ISR2. May interact with FCER1G (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane
CC       (Probable). Nucleus (By similarity). Note=Shuttles between the
CC       nucleus and the cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1; Synonyms=Alpha;
CC         IsoId=Q91ZM2-1; Sequence=Displayed;
CC       Name=2; Synonyms=Beta;
CC         IsoId=Q91ZM2-2; Sequence=VSP_032032;
CC       Name=3; Synonyms=Gamma;
CC         IsoId=Q91ZM2-3; Sequence=VSP_032033;
CC       Name=4; Synonyms=Delta;
CC         IsoId=Q91ZM2-4; Sequence=VSP_032034;
CC       Name=5;
CC         IsoId=Q91ZM2-5; Sequence=VSP_032029, VSP_032031;
CC       Name=6; Synonyms=Sh2bpsm1 gamma;
CC         IsoId=Q91ZM2-6; Sequence=VSP_032030, VSP_032033;
CC   -!- TISSUE SPECIFICITY: Widely expressed with highest levels in liver,
CC       brain and heart. Isoform 3 is widely expressed.
CC   -!- PTM: Phosphorylated on tyrosine residues in response to IGF-I and
CC       PDGF stimulation.
CC   -!- SIMILARITY: Belongs to the SH2B adapter family.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF020526; AAC33414.1; -; mRNA.
DR   EMBL; AF380422; AAL07566.1; -; mRNA.
DR   EMBL; AF074329; AAD41655.1; -; mRNA.
DR   EMBL; AF421138; AAL16069.1; -; mRNA.
DR   EMBL; AF421139; AAL16070.1; -; mRNA.
DR   EMBL; AK168439; BAE40344.1; -; mRNA.
DR   EMBL; AK170444; BAE41802.1; -; mRNA.
DR   EMBL; BC011422; AAH11422.1; -; mRNA.
DR   EMBL; BC051978; AAH51978.1; -; mRNA.
DR   EMBL; AF036355; AAC39955.2; -; mRNA.
DR   IPI; IPI00283476; -.
DR   IPI; IPI00284016; -.
DR   IPI; IPI00315068; -.
DR   IPI; IPI00875102; -.
DR   IPI; IPI00889250; -.
DR   IPI; IPI00889278; -.
DR   PIR; JC5886; JC5886.
DR   RefSeq; NP_001074928.1; NM_001081459.1.
DR   RefSeq; NP_035493.2; NM_011363.2.
DR   UniGene; Mm.8538; -.
DR   PDB; 2HDV; X-ray; 2.00 A; A/B=519-627.
DR   PDB; 2HDX; X-ray; 2.35 A; A/B/C/D/E/F=519-627.
DR   PDBsum; 2HDV; -.
DR   PDBsum; 2HDX; -.
DR   ProteinModelPortal; Q91ZM2; -.
DR   SMR; Q91ZM2; 23-84, 241-379, 520-627.
DR   STRING; Q91ZM2; -.
DR   Ensembl; ENSMUST00000032978; ENSMUSP00000032978; ENSMUSG00000030733.
DR   Ensembl; ENSMUST00000098049; ENSMUSP00000095657; ENSMUSG00000030733.
DR   GeneID; 20399; -.
DR   KEGG; mmu:20399; -.
DR   UCSC; uc009jrk.1; mouse.
DR   CTD; 20399; -.
DR   MGI; MGI:1201407; Sh2b1.
DR   GeneTree; ENSGT00530000063355; -.
DR   HOVERGEN; HBG006707; -.
DR   OMA; ATPMVQL; -.
DR   OrthoDB; EOG4ZPDV6; -.
DR   PhylomeDB; Q91ZM2; -.
DR   ArrayExpress; Q91ZM2; -.
DR   Bgee; Q91ZM2; -.
DR   CleanEx; MM_SH2B1; -.
DR   Genevestigator; Q91ZM2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0001726; C:ruffle; TAS:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0006928; P:cellular component movement; IDA:MGI.
DR   GO; GO:0030032; P:lamellipodium assembly; IDA:MGI.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR015012; Phe_ZIP.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000980; SH2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF08916; Phe_ZIP; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00252; SH2; 1.
DR   SUPFAM; SSF109805; Phe_ZIP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
DR   PROSITE; PS50001; SH2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Membrane; Nucleus;
KW   Phosphoprotein; SH2 domain.
FT   CHAIN         1    756       SH2B adapter protein 1.
FT                                /FTId=PRO_0000323594.
FT   DOMAIN      267    376       PH.
FT   DOMAIN      527    625       SH2.
FT   REGION        1    555       Interaction with JAK2 (low-affinity
FT                                binding; independent of JAK2
FT                                phosphorylation) (By similarity).
FT   REGION       24     85       Required for self-association (By
FT                                similarity).
FT   REGION       85    196       Interaction with RAC1 (By similarity).
FT   REGION      100    243       Required for NGF signaling (By
FT                                similarity).
FT   REGION      224    233       Required for nuclear localization (By
FT                                similarity).
FT   MOD_RES      88     88       Phosphoserine (By similarity).
FT   MOD_RES      96     96       Phosphoserine (By similarity).
FT   MOD_RES     126    126       Phosphoserine.
FT   MOD_RES     127    127       Phosphoserine.
FT   MOD_RES     439    439       Phosphotyrosine; by JAK1, JAK2 and PDGFR
FT                                (By similarity).
FT   MOD_RES     494    494       Phosphotyrosine; by JAK1, JAK2 (By
FT                                similarity).
FT   MOD_RES     624    624       Phosphotyrosine (By similarity).
FT   VAR_SEQ     437    443       GAYGGLS -> AVDSEKT (in isoform 5).
FT                                /FTId=VSP_032029.
FT   VAR_SEQ     441    460       Missing (in isoform 6).
FT                                /FTId=VSP_032030.
FT   VAR_SEQ     444    756       Missing (in isoform 5).
FT                                /FTId=VSP_032031.
FT   VAR_SEQ     632    756       ERSTSRDPAQPSEPPPWTDPPHPGAEEASGAPEVAAATAAA
FT                                AKERQEKEKAGSGGVQEELVPVAELVPMVELEEAIAPGTEA
FT                                QGGAGSSGDLEVSLMVQLQQLPLGGNGEEGGHPRAINNQYS
FT                                FV -> GREQAGSHAGVCEGDRCYPDASSTLLPFGASDCVT
FT                                EHLP (in isoform 2).
FT                                /FTId=VSP_032032.
FT   VAR_SEQ     632    756       ERSTSRDPAQPSEPPPWTDPPHPGAEEASGAPEVAAATAAA
FT                                AKERQEKEKAGSGGVQEELVPVAELVPMVELEEAIAPGTEA
FT                                QGGAGSSGDLEVSLMVQLQQLPLGGNGEEGGHPRAINNQYS
FT                                FV -> GEQSRSAGEEVPVHPRSEAGSRLGAMQGCARATDA
FT                                TPMPPPPSCPSERVTV (in isoform 3 and
FT                                isoform 6).
FT                                /FTId=VSP_032033.
FT   VAR_SEQ     632    756       ERSTSRDPAQPSEPPPWTDPPHPGAEEASGAPEVAAATAAA
FT                                AKERQEKEKAGSGGVQEELVPVAELVPMVELEEAIAPGTEA
FT                                QGGAGSSGDLEVSLMVQLQQLPLGGNGEEGGHPRAINNQYS
FT                                FV -> GEQSRSAGEEVPVHPRSENGAPPVTQPSPLNPLHG
FT                                QIPHILGQKRRRGRQKLRQPQPQQPKRGKRKRKRAVEGSRK
FT                                SWSPWLSWSPWLNWKRP (in isoform 4).
FT                                /FTId=VSP_032034.
FT   CONFLICT    172    172       W -> C (in Ref. 2; AAD41655).
FT   CONFLICT    399    399       F -> L (in Ref. 5; AAH11422).
FT   CONFLICT    564    564       Y -> C (in Ref. 2; AAD41655).
FT   HELIX       522    524
FT   HELIX       534    541
FT   TURN        542    544
FT   HELIX       545    548
FT   STRAND      551    556
FT   STRAND      558    560
FT   STRAND      563    570
FT   STRAND      573    581
FT   STRAND      587    589
FT   STRAND      592    596
FT   HELIX       597    606
FT   TURN        612    616
SQ   SEQUENCE   756 AA;  79625 MW;  388BDC44267E6DE8 CRC64;
     MNGAPSPEDG VFPSPPALPP PPPPSWQEFC ESHARAAALD LARRFRLYLA SHPQYAEPGA
     EAAFSGRFAE LFLQHFEAEV ARASGSLSPP VLAPLSPGVE IPPSHDLSLE SCRVGGPLAV
     LGPSRSSEDL AGPLPSSVPS STTSSKPKLK KRFSLRSVGR SVRGSVRGIL QWRGAVDSPS
     QAGPLETTSG PPVLGGNSNS NSSGGAGTVG RALANDGTSP GERWTHRFER LRLSRGGGTL
     KDGAGMIQRE ELLSFMGAEE AAPDPAGVGR GGGAAGLTSG GGGQPQWQKC RLLLRSEGEG
     GGGSRLEFFV PPKASRPRLS IPCSTITDVR TATALEMPDR ENTFVVKVEG PSEYILETSD
     ALHVKAWVSD IQECLSPGPC PAISPRPMTL PLAPGTSFFT KDNTDSLELP CLNHSESLPS
     QDLLLGPSES NDRLSQGAYG GLSDRPSASF SPSSASIAAS HFDSMELLPP ELPPRIPIEE
     GPPAGTVHPL STPYPPLDTP EAATGSFLFQ GESEGGEGDQ PLSGYPWFHG MLSRLKAAQL
     VLEGGTGSHG VFLVRQSETR RGEYVLTFNF QGKAKHLRLS LNEEGQCRVQ HLWFQSIFDM
     LEHFRVHPIP LESGGSSDVV LVSYVPSQRQ QERSTSRDPA QPSEPPPWTD PPHPGAEEAS
     GAPEVAAATA AAAKERQEKE KAGSGGVQEE LVPVAELVPM VELEEAIAPG TEAQGGAGSS
     GDLEVSLMVQ LQQLPLGGNG EEGGHPRAIN NQYSFV
//
ID   NECA2_MOUSE             Reviewed;         389 AA.
AC   Q91ZP9; Q1LZI4; Q8C492;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=N-terminal EF-hand calcium-binding protein 2;
DE            Short=EF-hand calcium-binding protein 2;
DE   AltName: Full=Neuronal calcium-binding protein 2;
GN   Name=Necab2; Synonyms=Efcbp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC   STRAIN=NMRI; TISSUE=Embryo;
RX   MEDLINE=21521128; PubMed=11641222;
RA   Bernier G., Vukovich W., Neidhardt L., Herrmann B.G., Gruss P.;
RT   "Isolation and characterization of a downstream target of Pax6 in the
RT   mammalian retinal primordium.";
RL   Development 128:3987-3994(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-389 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q91ZP9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q91ZP9-2; Sequence=VSP_024215;
CC   -!- TISSUE SPECIFICITY: Expressed in the iris, in the ciliary margin
CC       of the retina and in the inner portion of the neural retina.
CC   -!- DEVELOPMENTAL STAGE: Expressed in retina, retinal pigmented
CC       epithelium, Rathke's pouch, corneal epithelium, the infundibulum
CC       and olfactory placodes at 10.5 dpc (at protein level). Expressed
CC       in the inner region of the neural retina, including the ganglion
CC       cell layer at 17.5 dpc (at protein level). Expressed in the optic
CC       sulcus and in the pre-tectum at 8.5 dpc. Expressed in the optic
CC       vesicle, in the midline position in the roof of the midbrain and
CC       in the pre-tectum at 9.0-9.5 dpc. Expressed in the olfactory
CC       placodes at 10.5 dpc. Expressed in retinal-pigmented epithelium
CC       and in the neural retina, with strong expression in the ciliary
CC       margin at 12.5-13.5 dpc.
CC   -!- INDUCTION: Up-regulated by PAX6.
CC   -!- SIMILARITY: Contains 1 ABM domain.
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC38589.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF411253; AAL04151.1; -; mRNA.
DR   EMBL; BC115857; AAI15858.1; -; mRNA.
DR   EMBL; BC115963; AAI15964.1; -; mRNA.
DR   EMBL; AK082727; BAC38589.1; ALT_INIT; mRNA.
DR   IPI; IPI00131287; -.
DR   IPI; IPI00667108; -.
DR   RefSeq; NP_473436.1; NM_054095.2.
DR   UniGene; Mm.356184; -.
DR   ProteinModelPortal; Q91ZP9; -.
DR   SMR; Q91ZP9; 69-128, 289-377.
DR   PRIDE; Q91ZP9; -.
DR   Ensembl; ENSMUST00000098363; ENSMUSP00000095966; ENSMUSG00000031837.
DR   GeneID; 117148; -.
DR   KEGG; mmu:117148; -.
DR   CTD; 117148; -.
DR   MGI; MGI:2152211; Necab2.
DR   GeneTree; ENSGT00390000009734; -.
DR   HOGENOM; HBG446692; -.
DR   HOVERGEN; HBG050433; -.
DR   InParanoid; Q91ZP9; -.
DR   OMA; LEDLFHT; -.
DR   OrthoDB; EOG46T31S; -.
DR   NextBio; 369524; -.
DR   ArrayExpress; Q91ZP9; -.
DR   Bgee; Q91ZP9; -.
DR   CleanEx; MM_NECAB2; -.
DR   Genevestigator; Q91ZP9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR   InterPro; IPR007138; Antibiotic_mOase.
DR   InterPro; IPR011008; Dimeric_a/b-barrel.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF03992; ABM; 1.
DR   SMART; SM00054; EFh; 2.
DR   SUPFAM; SSF54909; Dimer_A_B_barrel; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Coiled coil; Cytoplasm; Repeat.
FT   CHAIN         1    389       N-terminal EF-hand calcium-binding
FT                                protein 2.
FT                                /FTId=PRO_0000282614.
FT   DOMAIN       63     98       EF-hand 1.
FT   DOMAIN       97    132       EF-hand 2.
FT   DOMAIN      287    377       ABM.
FT   CA_BIND      76     87       1 (Potential).
FT   CA_BIND     110    121       2 (Potential).
FT   COILED      173    198       Potential.
FT   VAR_SEQ       1    129       Missing (in isoform 2).
FT                                /FTId=VSP_024215.
SQ   SEQUENCE   389 AA;  43441 MW;  493F29BAFFD864EA CRC64;
     MCERAARLCR AGAHRLLREP PPQGRALGGL LRWVGARMGE PRAPLVPDIP SADPGPGPAA
     SRGGTAVILD IFRRADKNDD GKLSLEEFQL FFADGVLNEK ELEGLFHTID SDNTNHVDTK
     ELCDYFVEHM GDYEDVLASL ETLNHSVLKA MGYTKKVYEG GSNVDQFVTR FLLKETANQI
     QSLLSSVESA VEAIEEQTSQ IRQDHCKPSH AVNESRYGGP TPPYIPNHKL VAPEPMKSLP
     VATGEPKEDG LEGQISRLAE LIGRLESKTL SFDLQQRLSD EEGTNMHLQL VRQEMAVCPE
     QLSEFLDSLR QYLRSTAEER NCFHVAAVRM ADGLTFVIYE FWETEEEWKR HLQSPVCKAF
     RHVKVDTLSQ PEALSQISVP AAWCTSGRD
//
ID   SNX18_MOUSE             Reviewed;         614 AA.
AC   Q91ZR2;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Sorting nexin-18;
DE   AltName: Full=Sorting nexin-associated Golgi protein 1;
GN   Name=Snx18; Synonyms=Snag1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RA   Cohn J.B., Bernstein A., Stanford W.L.;
RT   "SNAG1, a novel SH3 and PX domain containing protein.";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May be involved in several stages of intracellular
CC       trafficking. Plays a role in endocytosis via clathrin-coated pits,
CC       but also clathrin-independent, actin-dependent fluid-phase
CC       endocytosis. Plays a role in macropinocytosis. Binds to membranes
CC       enriched in phosphatidylinositol 4,5-bisphosphate and promotes
CC       membrane tubulation. Stimulates the GTPase activity of DNM2.
CC       Promotes DNM2 location at the plasma membrane (By similarity).
CC   -!- SUBUNIT: Heterodimer with SNX9. Interacts with ITCH. Interacts
CC       with dynamin, SYNJ1 and WASL. Interacts with the AP-1 complex (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane
CC       protein; Cytoplasmic side (By similarity). Endosome membrane;
CC       Peripheral membrane protein; Cytoplasmic side (By similarity).
CC       Cell membrane; Peripheral membrane protein; Cytoplasmic side (By
CC       similarity). Note=Localized at sites of endocytosis at the cell
CC       membrane. Detected on newly formed macropinosomes. Partially
CC       colocalized with clathrin and dynamin at the cell membrane.
CC       Transiently recruited to clathrin-coated pits at a late stage of
CC       clathrin-coated vesicle formation (By similarity).
CC   -!- DOMAIN: The PX domain mediates interaction with membranes enriched
CC       in phosphatidylinositol-4,5-bisphosphate (By similarity).
CC   -!- SIMILARITY: Belongs to the sorting nexin family.
CC   -!- SIMILARITY: Contains 1 PX (phox homology) domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; AF408408; AAL02105.1; -; mRNA.
DR   IPI; IPI00131329; -.
DR   UniGene; Mm.33721; -.
DR   ProteinModelPortal; Q91ZR2; -.
DR   SMR; Q91ZR2; 3-62, 244-614.
DR   MINT; MINT-5209459; -.
DR   STRING; Q91ZR2; -.
DR   PhosphoSite; Q91ZR2; -.
DR   PRIDE; Q91ZR2; -.
DR   Ensembl; ENSMUST00000037864; ENSMUSP00000039662; ENSMUSG00000042364.
DR   MGI; MGI:2137642; Snx18.
DR   eggNOG; roNOG05551; -.
DR   GeneTree; ENSGT00510000046469; -.
DR   HOVERGEN; HBG009996; -.
DR   OrthoDB; EOG48SGSS; -.
DR   PhylomeDB; Q91ZR2; -.
DR   ArrayExpress; Q91ZR2; -.
DR   Bgee; Q91ZR2; -.
DR   CleanEx; MM_SNX18; -.
DR   Genevestigator; Q91ZR2; -.
DR   GermOnline; ENSMUSG00000042364; Mus musculus.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001683; Phox.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR014536; Snx9.
DR   InterPro; IPR019497; Sorting_nexin_WASP-bd-dom.
DR   Gene3D; G3DSA:3.30.1520.10; PX; 1.
DR   Pfam; PF10456; BAR_3_WASP_bdg; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PIRSF; PIRSF027744; Snx9; 1.
DR   SMART; SM00312; PX; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF64268; PX; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50195; PX; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Endocytosis; Endosome; Lipid-binding; Membrane;
KW   Phosphoprotein; Protein transport; SH3 domain; Transport.
FT   CHAIN         1    614       Sorting nexin-18.
FT                                /FTId=PRO_0000213867.
FT   DOMAIN        1     61       SH3.
FT   DOMAIN      266    376       PX.
FT   BINDING     302    302       Phosphatidylinositol 4,5-bisphosphate (By
FT                                similarity).
FT   BINDING     304    304       Phosphatidylinositol 4,5-bisphosphate (By
FT                                similarity).
FT   BINDING     328    328       Phosphatidylinositol 4,5-bisphosphate (By
FT                                similarity).
FT   BINDING     342    342       Phosphatidylinositol 4,5-bisphosphate (By
FT                                similarity).
FT   MOD_RES     184    184       Phosphotyrosine (By similarity).
FT   MOD_RES     187    187       Phosphoserine (By similarity).
FT   MOD_RES     188    188       Phosphothreonine (By similarity).
FT   MOD_RES     190    190       Phosphoserine (By similarity).
FT   MOD_RES     193    193       Phosphoserine (By similarity).
SQ   SEQUENCE   614 AA;  67904 MW;  BACED9D104571098 CRC64;
     MALRARALYD FKSENPGEIS LREHEVLSLC SEQDIEGWLE GINSRGDRGL FPASYVQVIR
     APEPGPPADG GPGAPARYAN VPPGGFEPLP AAPPAAFPPL LQPQASPGSF QPPGAGFPYG
     GGALQPSPQQ LYGGYQASLG SDDDWDDEWD DSSTVADEPG ALGSGAYPDL DGSSSAGGGA
     AGRYRLSTRS DLSLGSRGVS APPAPSVWSQ ELGHGEPQPQ SLLHLRQVGR GGLRAGRGVR
     LREGWGQAVR GAGSYGPEWQ ENPYPFQCTI DDPTKQTKFK GMKSYISYKL VPTHTQVPVH
     RRYKHFDWLY ARLAEKFPVI SVPHLPEKQA TGRFEEDFIS KRRKGLIWWM NHMASHPVLA
     QCDVFQHFLT CPSSTDEKAW KQGKRKAEKD EMVGANFFLT LSTPPAAALD LQEVESKIDG
     FKCFTKKMDD SALQLNHTAN EFARKQVTGF KKEYQKVGQS FRGLSQAFEL DQQAFSVGLN
     QAIAFTGDAY DAIGELFAEQ PRQDLDPVMD LLALYQGHLA NFPDIIHVQK GALTKVKESR
     RHVEEGKMEV QKADGIQDRC NTISFATLAE IHHFHQIRVR DFKSQMQHFL QQQIIFFQKV
     TQKLEEALHK YDSV
//
ID   DYST_MOUSE              Reviewed;        7389 AA.
AC   Q91ZU6; Q3I6J6; Q60824; Q60845; Q8K5D4; Q91ZU7; Q91ZU8; Q9WU50;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Dystonin;
DE   AltName: Full=Bullous pemphigoid antigen 1;
DE            Short=BPA;
DE   AltName: Full=Dystonia musculorum protein;
DE   AltName: Full=Hemidesmosomal plaque protein;
DE   AltName: Full=Microtubule actin cross-linking factor 2;
GN   Name=Dst; Synonyms=Bpag1, Macf2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 5), TISSUE SPECIFICITY,
RP   AND ALTERNATIVE SPLICING.
RC   STRAIN=BALB/c; TISSUE=Muscle, and Neuron;
RX   MEDLINE=21405767; PubMed=11514586; DOI=10.1083/jcb.200012098;
RA   Leung C.L., Zheng M., Prater S.M., Liem R.K.H.;
RT   "The BPAG1 locus: alternative splicing produces multiple isoforms with
RT   distinct cytoskeletal linker domains, including predominant isoforms
RT   in neurons and muscles.";
RL   J. Cell Biol. 154:691-697(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-511 (ISOFORM 7), AND PARTIAL
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
RC   TISSUE=Brain;
RX   MEDLINE=95400297; PubMed=7670468; DOI=10.1038/ng0795-301;
RA   Brown A., Bernier G., Mathieu M., Rossant J., Kothary R.;
RT   "The mouse dystonia musculorum gene is a neural isoform of bullous
RT   pemphigoid antigen 1.";
RL   Nat. Genet. 10:301-306(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-304 (ISOFORM 6).
RC   STRAIN=C3H;
RX   PubMed=16289082; DOI=10.1016/j.yexcr.2005.10.002;
RA   Young K.G., Pinheiro B., Kothary R.;
RT   "A Bpag1 isoform involved in cytoskeletal organization surrounding the
RT   nucleus.";
RL   Exp. Cell Res. 312:121-134(2006).
RN   [4]
RP   PROTEIN SEQUENCE OF 580-584; 1043-1047 AND 1053-1057, AND X-RAY
RP   CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 580-803.
RX   PubMed=17161423; DOI=10.1016/j.jmb.2006.11.036;
RA   Jefferson J.J., Ciatto C., Shapiro L., Liem R.K.;
RT   "Structural analysis of the plakin domain of bullous pemphigoid
RT   antigen1 (BPAG1) suggests that plakins are members of the spectrin
RT   superfamily.";
RL   J. Mol. Biol. 366:244-257(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6693-7389 (ISOFORM 3), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6870-7389 (ISOFORM 4).
RC   STRAIN=C57BL/6J; TISSUE=Fetal skin, and Fetal spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, AND
RP   INTERACTION WITH PRPH.
RC   STRAIN=BALB/c;
RX   MEDLINE=99268151; PubMed=9971739; DOI=10.1083/jcb.144.3.435;
RA   Leung C.L., Sun D., Liem R.K.;
RT   "The intermediate filament protein peripherin is the specific
RT   interaction partner of mouse BPAG1-n (dystonin) in neurons.";
RL   J. Cell Biol. 144:435-446(1999).
RN   [7]
RP   PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RC   STRAIN=Swiss Webster / NIH;
RA   Kubo Y., Ohba M., Iwashita S.;
RT   "Molecular network in NGF-mediated neural differentiation.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1100; SER-1527 AND
RP   THR-1533 (ISOFORM 5), AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7182, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Cytoskeletal linker protein. Anchors keratin-containing
CC       intermediate filaments to the inner plaque of hemidesmosomes. The
CC       proteins may self-aggregate to form filaments or a two-dimensional
CC       mesh.
CC   -!- SUBUNIT: Homodimer. Interacts with the neuronal intermediate
CC       filament protein, Prph. Interacts with MAPRE1; probably required
CC       for targeting to the growing microtubule plus ends (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Note=Associated with the microtubule network at the growing distal
CC       tip of microtubules (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage, Alternative splicing; Named isoforms=7;
CC       Name=2; Synonyms=BPAG1-b;
CC         IsoId=Q91ZU6-1; Sequence=Displayed;
CC       Name=1; Synonyms=BPAG1-a;
CC         IsoId=Q91ZU6-2; Sequence=VSP_050483;
CC       Name=3;
CC         IsoId=Q91ZU6-3; Sequence=VSP_050484, VSP_050485, VSP_050486;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q91ZU6-4; Sequence=VSP_050485, VSP_050486;
CC         Note=No experimental confirmation available;
CC       Name=5; Synonyms=BPAG1-e;
CC         IsoId=Q91ZU6-5; Sequence=VSP_038954, VSP_038958, VSP_038959;
CC         Note=Ref.7 (BAB93448) sequence is in conflict in positions:
CC         2325:G->D, 2416:A->T, 2530:K->Q. Phosphorylated on Thr-1100,
CC         Ser-1527 and Thr-1533;
CC       Name=6; Synonyms=BPAG1-n1;
CC         IsoId=Q91ZU6-6; Sequence=VSP_038955, VSP_038956, VSP_038957;
CC         Note=Ref.2 (AAC52231) sequence is in conflict in position:
CC         101:E->K;
CC       Name=7; Synonyms=BPAG1-n2;
CC         IsoId=Q91ZU6-7; Sequence=VSP_038956, VSP_038957;
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in the heart and
CC       skeletal muscle and at low levels in the skin in the adult.
CC       Expressed in the myocardium, skeletal muscle masses, vertebrae
CC       cartilage, and epithelia of the tongue of 14.5 day embryos.
CC       Isoform 5 is expressed at high levels in the skin in both the
CC       adult and 14.5 day embryos.
CC   -!- DOMAIN: The microtubule tip localization signal (MtLS) motif;
CC       mediates interaction with MAPRE1 and targeting to the growing
CC       microtubule plus ends (By similarity).
CC   -!- SIMILARITY: Belongs to the plakin or cytolinker family.
CC   -!- SIMILARITY: Contains 1 actin-binding domain.
CC   -!- SIMILARITY: Contains 2 CH (calponin-homology) domains.
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
CC   -!- SIMILARITY: Contains 1 GAR domain.
CC   -!- SIMILARITY: Contains 5 plectin repeats.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SIMILARITY: Contains 19 spectrin repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC52231.1; Type=Frameshift; Positions=52;
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DR   EMBL; AF396877; AAK83382.1; -; mRNA.
DR   EMBL; AF396879; AAK83384.1; -; mRNA.
DR   EMBL; AF396878; AAK83383.1; -; mRNA.
DR   EMBL; U22452; AAC52230.1; -; mRNA.
DR   EMBL; U25158; AAC52231.1; ALT_FRAME; mRNA.
DR   EMBL; DQ023311; AAY46942.1; -; mRNA.
DR   EMBL; AK051626; BAC34695.1; -; mRNA.
DR   EMBL; AK037206; BAC29753.1; -; mRNA.
DR   EMBL; AF115383; AAD22959.1; -; mRNA.
DR   EMBL; AB085694; BAB93448.1; -; mRNA.
DR   IPI; IPI00131432; -.
DR   IPI; IPI00230689; -.
DR   IPI; IPI00230690; -.
DR   IPI; IPI00230692; -.
DR   IPI; IPI00277410; -.
DR   IPI; IPI00284272; -.
DR   IPI; IPI00623531; -.
DR   PIR; A60776; A60776.
DR   PIR; I49290; I49290.
DR   PIR; I49298; I49298.
DR   RefSeq; NP_598594.2; NM_133833.2.
DR   RefSeq; NP_604443.2; NM_134448.2.
DR   UniGene; Mm.478284; -.
DR   PDB; 2IAK; X-ray; 3.00 A; A=580-803.
DR   PDBsum; 2IAK; -.
DR   ProteinModelPortal; Q91ZU6; -.
DR   SMR; Q91ZU6; 3-255, 268-479, 583-795, 1548-1927, 3848-3910, 4006-4039, 4497-4658.
DR   STRING; Q91ZU6; -.
DR   PhosphoSite; Q91ZU6; -.
DR   REPRODUCTION-2DPAGE; IPI00230689; -.
DR   REPRODUCTION-2DPAGE; IPI00230690; -.
DR   REPRODUCTION-2DPAGE; IPI00284272; -.
DR   PRIDE; Q91ZU6; -.
DR   Ensembl; ENSMUST00000097786; ENSMUSP00000095393; ENSMUSG00000026131.
DR   GeneID; 13518; -.
DR   KEGG; mmu:13518; -.
DR   UCSC; uc007aoi.1; mouse.
DR   UCSC; uc007aoj.1; mouse.
DR   CTD; 13518; -.
DR   MGI; MGI:104627; Dst.
DR   GeneTree; ENSGT00600000084106; -.
DR   HOVERGEN; HBG031127; -.
DR   Bgee; Q91ZU6; -.
DR   CleanEx; MM_DST; -.
DR   Genevestigator; Q91ZU6; -.
DR   GermOnline; ENSMUSG00000026131; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0035371; C:microtubule plus end; ISS:UniProtKB.
DR   GO; GO:0060053; C:neurofilament cytoskeleton; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0051010; F:microtubule plus-end binding; ISS:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007050; P:cell cycle arrest; IEA:InterPro.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IMP:MGI.
DR   GO; GO:0045104; P:intermediate filament cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0008090; P:retrograde axon cargo transport; IMP:MGI.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR003108; GAS2_dom.
DR   InterPro; IPR001101; Plectin_repeat.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 2.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Gene3D; G3DSA:3.30.920.20; GAS2_dom; 1.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF02187; GAS2; 1.
DR   Pfam; PF00681; Plectin; 5.
DR   Pfam; PF00435; Spectrin; 19.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM00243; GAS2; 1.
DR   SMART; SM00250; PLEC; 9.
DR   SMART; SM00150; SPEC; 32.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS51460; GAR; 1.
DR   PROSITE; PS50002; SH3; FALSE_NEG.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Alternative promoter usage;
KW   Alternative splicing; Calcium; Cell adhesion; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Direct protein sequencing; Microtubule; Phosphoprotein;
KW   Repeat; SH3 domain.
FT   CHAIN         1   7389       Dystonin.
FT                                /FTId=PRO_0000078141.
FT   DOMAIN       35    252       Actin-binding.
FT   DOMAIN       35    138       CH 1.
FT   DOMAIN      151    252       CH 2.
FT   REPEAT      701    801       Spectrin 1.
FT   DOMAIN      889    941       SH3.
FT   REPEAT     1582   1624       Plectin 1.
FT   REPEAT     1657   1701       Plectin 2.
FT   REPEAT     1772   1815       Plectin 3.
FT   REPEAT     1816   1844       Plectin 4.
FT   REPEAT     1848   1889       Plectin 5.
FT   REPEAT     3845   3925       Spectrin 2.
FT   REPEAT     3997   4079       Spectrin 3.
FT   REPEAT     4440   4548       Spectrin 4.
FT   REPEAT     4552   4657       Spectrin 5.
FT   REPEAT     4775   4877       Spectrin 6.
FT   REPEAT     5208   5315       Spectrin 7.
FT   REPEAT     5322   5423       Spectrin 8.
FT   REPEAT     5430   5532       Spectrin 9.
FT   REPEAT     5647   5751       Spectrin 10.
FT   REPEAT     5758   5856       Spectrin 11.
FT   REPEAT     6002   6082       Spectrin 12.
FT   REPEAT     6089   6191       Spectrin 13.
FT   REPEAT     6197   6300       Spectrin 14.
FT   REPEAT     6308   6410       Spectrin 15.
FT   REPEAT     6415   6519       Spectrin 16.
FT   REPEAT     6523   6629       Spectrin 17.
FT   REPEAT     6636   6736       Spectrin 18.
FT   REPEAT     6741   6844       Spectrin 19.
FT   DOMAIN     7015   7050       EF-hand 1.
FT   DOMAIN     7051   7086       EF-hand 2.
FT   DOMAIN     7091   7169       GAR.
FT   CA_BIND    7028   7039       1 (Potential).
FT   CA_BIND    7064   7075       2 (Potential).
FT   MOTIF      7369   7372       Microtubule tip localization signal.
FT   COMPBIAS   2362   2422       Asp-rich.
FT   MOD_RES      40     40       Phosphothreonine (By similarity).
FT   MOD_RES      42     42       Phosphothreonine (By similarity).
FT   MOD_RES    7182   7182       Phosphoserine.
FT   VAR_SEQ       1    381       MAGYLSPAAYMYVEEQEYLQAYEDVLERYKDERDKVQKKTF
FT                                TKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLP
FT                                REKGRMRFHRLQNVQIALDYLKRRQVKLVNIRNDDITDGNP
FT                                KLTLGLIWTIILHFQISDIHVTGESEDMSAKERLLLWTQQA
FT                                TEGYAGVRCENFTTCWRDGKLFNAIIHKYRPDLIDMNTVAV
FT                                QSNLANLEHAFYVAEKIGVIRLLDPEDVDVSSPDEKSVITY
FT                                VSSLYDAFPKVPEGGEGIGANDVEVKWIEYQNMVNYLIQWI
FT                                RHHVVTMSERTFPNNPLELKALYNQYLQFKEKEIPPKEMEK
FT                                SKIKRLYKLLEIWIEFGRIKLLQGYHPNDIEKEWGKLIIAM
FT                                LEREKALRPEVE -> MRISCPFIVVPLINSCISFSNESLD
FT                                GH (in isoform 5).
FT                                /FTId=VSP_038954.
FT   VAR_SEQ       1     30       MAGYLSPAAYMYVEEQEYLQAYEDVLERYK -> MIAAAFL
FT                                VLLRPYSIQCALFLLLLLLGTVATIVFFCCWHRKLQKGRHP
FT                                MKSVFSGRSRSRDAALRSHHFRSEGFRASPRHIRRRVAAAA
FT                                AARLEEVKPVVEVHHQSEQESSGRKRRIKKNSRVQPEFYHS
FT                                VQGASTRRPSSGNASYRCSMSSSADFSDEDDFSQKSGSASP
FT                                APGDTLPWNLPKHERSKRKIQGGSVLDPAERAVLRIA (in
FT                                isoform 6).
FT                                /FTId=VSP_038955.
FT   VAR_SEQ     512    512       Q -> NLVSEFKQKCDQQSMIIQKTEKEVRSLSAELSASKE
FT                                EKRREEQKAQLQRAQVQELNDRLKRVQDELHLKTIEEQMTH
FT                                RKMILLQEESDKFKRSADEFRKKMEKLMESKVVTETDLSGI
FT                                KHDFVSLQRENFRAQENAKLWETNIRELERQLQCYREKMQQ
FT                                GPPVEANHYQKCRRLEEELLAQRREVENLKQKMDQQIKEHE
FT                                HQLLRLQCEIQKKSTTQDHTFASAFDTAGRECHHPAEISPG
FT                                NSGHLNLKTRLPLSRWTQEPHQTEGKWPHRAAEQLPKEVQF
FT                                RQPGAPLDRESSQPCYSEYFSQTSTELQITFDDKNPITRLS
FT                                ELETMREQALHPSRPPVTYQDDKLERELVKLLTPLEIAKNK
FT                                QCGMHTEVTTLKQEKRLGSSAGGWMLEGCRTSGGLKGDFLK
FT                                KSVEPEASPSLDLNQACSVRDEEFQFQGLRHTVTGRQLVEA
FT                                KLLDMRTVEQLRLGLKTVEEVQRSLSKFLTKATSIAGLYLE
FT                                SSKEKMSFTSAAQKIIIDKMIALAFLEAQAATGFIIDPVSG
FT                                QTYCVEDAVLHGIVDPEFRSRLLEAEKAVLGYSHASKTLSV
FT                                FQAMENRMLDRKKGKHILEAQIASGGVIDPVRGVRVPPEMA
FT                                VQQGLLNNAVLQFLHEPSSNTRVFPNPNNKQALYYSELLQI
FT                                CVFDVDCQCFLLPFGEREISNLNIEKTHKIAVVDTKTGAEL
FT                                TAFEAFQRNLIDKGIYLELSGQQYQWKEATFFDSYGHPSHM
FT                                LTDTKTGLQFNISEAVEQGTLDKALVQKYQEGLTTLTELAD
FT                                FLLSKVVPKKDLHSPIAGYWLTASGERISLLKASRRNLVDR
FT                                VTALRCLEAQICTGGIIDPLTGKKYRVAEALHRGLVDEGFA
FT                                QQLRQCELVITGISHPVSNKMMSVVEAVNANIISKEMGMRC
FT                                LEFQYLTGGLIEPKVFSRLTIEEALHVGIIDVLIATRLKDQ
FT                                KSYVRDIMCPQTKRKLTYKEALEKADFDFHTGLKLLEVSEP
FT                                LGTGISNLYYSSQ (in isoform 6 and isoform
FT                                7).
FT                                /FTId=VSP_038956.
FT   VAR_SEQ     513   7389       Missing (in isoform 6 and isoform 7).
FT                                /FTId=VSP_038957.
FT   VAR_SEQ    1432   1432       K -> MKRSKENSEHGAYSDLLQRQRATMVENSKLTGKISE
FT                                LETMVAELKKQKSRVEEELPKVKEAAENELRKQQRNVEDIA
FT                                LQKLRAESEAKQYRRELETIVREKEAAERELERVRQLTAEA
FT                                EARRAAVEENLRNFRSQLQENTFTRQTLEDHLRRKDSSLSD
FT                                LEQQKRALVEELQRKRDHEEELLRLVKQMERDLAFQKQVAE
FT                                KQLKEKQKVELEARRKITEIQFSCRESAAVAQARPQREQGR
FT                                QKEEELKQQVDELTLANRKAEKEMRELKYELSAVQLEKASS
FT                                EEKARLLKDKLDETNNTLKCLKEDLERKDQAQERYSQQLRD
FT                                LGGQLNQTTDKAEEVRQEANDLKKIKHTYQLELESLHQEKG
FT                                KLQREVDRVTRAHALAERNIQCLNSQVHASRDEKDLSEERR
FT                                RLCQRKSDHLKEEFERSHAQLLQNIQAEKENNDKIQKLNKE
FT                                LEKSNECAETLKQKVDELTRQNNETKLMMQRIQAESKNIVR
FT                                EKQAIQQRCEVLRIQADGFKDQLRNTNEHLHKQTKTEQDFH
FT                                RKIKSLEDDLAQSQNLVSEFKQKCDQQSMIIQKTEKEVRSL
FT                                SAELSASKEEKRREEQKAQLQRAQVQELNDRLKRVQDELHL
FT                                KTIEEQMTHRKMILLQEESDKFKRSADEFRKKMEKLMESKV
FT                                VTETDLSGIKHDFVSLQRENFRAQENAKLWETNIRELERQL
FT                                QCYREKMQQGPPVEANHYQKCRRLEEELLAQRREVENLKQK
FT                                MDQQIKEHEHQLLRLQCEIQKKSTTQDHTFASAFDTAGREC
FT                                HHPAEISPGNSGHLNLKTRLPLSRWTQEPHQTEGKWPHRAA
FT                                EQLPKEVQFRQPGAPLDRESSQPCYSEYFSQTSTELQITFD
FT                                DKNPITRLSELETMREQALHPSRPPVTYQDDKLERELVKLL
FT                                TPLEIAKNKQCGMHTEVTTLKQEKRLGSSAGGWMLEGCRTS
FT                                GGLKGDFLKKSVEPEASPSLDLNQACSVRDEEFQFQGLRHT
FT                                VTGRQLVEAKLLDMRTVEQLRLGLKTVEEVQRSLSKFLTKA
FT                                TSIAGLYLESSKEKMSFTSAAQKIIIDKMIALAFLEAQAAT
FT                                GFIIDPVSGQTYCVEDAVLHGIVDPEFRSRLLEAEKAVLGY
FT                                SHASKTLSVFQAMENRMLDRKKGKHILEAQIASGGVIDPVR
FT                                GVRVPPEMAVQQGLLNNAVLQFLHEPSSNTRVFPNPNNKQA
FT                                LYYSELLQICVFDVDCQCFLLPFGEREISNLNIEKTHKIAV
FT                                VDTKTGAELTAFEAFQRNLIDKGIYLELSGQQYQWKEATFF
FT                                DSYGHPSHMLTDTKTGLQFNISEAVEQGTLDKALVQKYQEG
FT                                LTTLTELADFLLSKVVPKKDLHSPIAGYWLTASGERISLLK
FT                                ASRRNLVDRVTALRCLEAQICTGGIIDPLTGKKYRVAEALH
FT                                RGLVDEGFAQQLRQCELVITGISHPVSNKMMSVVEAVNANI
FT                                ISKEMGMRCLEFQYLTGGLIEPKVFSRLTIEEALHVGIIDV
FT                                LIATRLKDQKSYVRDIMCPQTKRKLTYKEALEKADFDFHTG
FT                                LKLLEVSEPLGTGISNLYYSSQ (in isoform 5).
FT                                /FTId=VSP_038958.
FT   VAR_SEQ    1433   7389       Missing (in isoform 5).
FT                                /FTId=VSP_038959.
FT   VAR_SEQ    1549   3557       Missing (in isoform 1).
FT                                /FTId=VSP_050483.
FT   VAR_SEQ    7125   7130       Missing (in isoform 3).
FT                                /FTId=VSP_050484.
FT   VAR_SEQ    7170   7193       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_050485.
FT   VAR_SEQ    7261   7261       K -> KILHPLTRNYGKPWLANSKMSTPCKAAECPDFPVSS
FT                                AE (in isoform 3 and isoform 4).
FT                                /FTId=VSP_050486.
FT   CONFLICT   6193   6193       T -> A (in Ref. 1; AAK83383).
FT   CONFLICT   7097   7097       G -> E (in Ref. 5; BAC29753/BAC34695).
FT   CONFLICT   7241   7241       G -> A (in Ref. 5; BAC29753/BAC34695).
SQ   SEQUENCE   7389 AA;  833638 MW;  BFED827ED8A88AAD CRC64;
     MAGYLSPAAY MYVEEQEYLQ AYEDVLERYK DERDKVQKKT FTKWINQHLM KVRKHVNDLY
     EDLRDGHNLI SLLEVLSGDT LPREKGRMRF HRLQNVQIAL DYLKRRQVKL VNIRNDDITD
     GNPKLTLGLI WTIILHFQIS DIHVTGESED MSAKERLLLW TQQATEGYAG VRCENFTTCW
     RDGKLFNAII HKYRPDLIDM NTVAVQSNLA NLEHAFYVAE KIGVIRLLDP EDVDVSSPDE
     KSVITYVSSL YDAFPKVPEG GEGIGANDVE VKWIEYQNMV NYLIQWIRHH VVTMSERTFP
     NNPLELKALY NQYLQFKEKE IPPKEMEKSK IKRLYKLLEI WIEFGRIKLL QGYHPNDIEK
     EWGKLIIAML EREKALRPEV ERLDMLQQIA TRVQRDSVSC EDKLILARNA LQSDSKRLES
     GVQFQNEAEI AGYILECENL LRQHVIDVQI LIDGKYYQAD QLVQRVAKLR DEIMALRNEC
     SSVYSKGRML TTEQTKLMIS GITQSLNSGF AQTLHPSLNS GLTQSLTPSL TSSSVTSGLS
     SGMTSRLTPS VTPVYAPGFP SVVAPNFSLG VEPNSLQTLK LMQIRKPLLK SSLLDQNLTE
     EEVNMKFVQD LLNWVDEMQV QLDRTEWGSD LPSVESHLEN HKNVHRAIEE FESSLKEAKI
     SEIQMTAPLK LSYTDKLHRL ESQYAKLLNT SRNQERHLDT LHNFVTRATN ELIWLNEKEE
     SEVAYDWSER NSSVARKKSY HVELMRELEQ KEESIKAVQE IAEQLLLENH PARLTIEAYR
     AAMQTQWSWI LQLCQCVEQH IQENSAYFEF FNDAKEATDY LRNLKDAIQR KYSCDRSSSI
     HKLEDLVQES MEKEELLQYR SVVAGLMGRA KTVVQLKPRN PDNPLKTSIP IKAICDYRQI
     EITIYKDDEC VLANNSHRAK WKVISPTGNE AVVPSVCFTV PPPNKEAVDF ANRIEQQYQS
     VLTLWHESHI NMKSVVSWHY LVNEIDRIRA SNVASIKTML PGEHQQVLSN LQSRLEDFLE
     DSQESQIFSG SDISQLEKEV SVCRKYYQEL LKSAEREEQE ESVYNLYISE VRNIRLRLES
     CEDRLIRQIR TPLERDDLHE SMLRITEQEK LKKELDRLKD DLGTITNKCE EFFSQAADSP
     SVPALRSELS VVIQSLSQIY SMSSTYIEKL KTVNLVLKNT QAAEALVKLY ETKLCEEEAV
     IADKNNIENL MSTLKQWRSE VDEKREVFHA LEDELQKAKA ISDEMFKTHK ERDLDFDWHK
     EKADQLVERW QSVHVQIDNR LRDLEGIGKS LKHYRDSYHP LDDWIQHIET TQRKIQENQP
     ENSKALALQL NQQKMLVSEI EVKQSKMDEC QKYSEQYSAA VKDYELQTMT YRAMVESQQK
     SPVKRRRIQS SADLVIQEFM DLRTRYTALV TLMTQYIKFA GDSLKRLEEE EKSLDEEKKQ
     HIEKAKELQK WVSNISKTLG DGEKAGKPLF SKQQMSSKEI STKKEQFSEA LQTTQIFLAK
     HGDKLTEEER SDLEKQVKTL QEGYNLLFSE SLKQQELQPS GESKVPEKPD KVIAGTINQT
     TGEVLSVFQA VLRGLIDYET GIRLLEAQLV ITGLISPELR KCFDLRDAES HGLIDEQVLR
     QLKELNRAKQ LISTASPTSI PVLDSLAQGM VSESMAIRVL EILLSAGPLL VPATGEHLTL
     QQAFQQNLIS SALFSKVLER QDTCKDLIDP CTSEKVSLTD MVQRSILQEN TRMWLLPVRP
     QEAGRITLKC GRSVSILRAA HEGLIDRETM FRLLGAQLLS GGLIDCNSGQ KMTVEEAVAE
     GVIDRDTASS ILTYQVQTGG IVHSNPAKRL TVDEAVQCEL ITSSSALLVL EAQRGYVGLI
     WPHSGEIFPT SSSLQQELIT NELASKILNG RQKIAALYIP ESSQVIGLDA AKQLGIIDNN
     TASVLKDVKL PDKMPDLGDL EDCKNAKRWL SFCKFQPSTV HDYRQEEGGS DGEEPVTAQS
     SEQTKKLFLS YLMVNSYMDA HTGQRLLLYD GDLDEAVSML LESCGAELGA DTSTRESLSV
     LTIPDAFPDC ALSEEKHECS ADKCHYSHPG HKESLENAKW DMNEAFCKMG NNDSNGELPR
     PENLADTTVV QKGSESPSRV RVPKPTSSST QPEGSVLRPE SGSILKGCKS QSEPVTKKYP
     DGTNHSHFLT SETSRPCDSN EREDEENIQK GPSVFDYSPR LSALLSHDEL RQSQGRFSDT
     STPQNTGYLC EASTLSPSDQ RVLADQSTRE KFQDRFLGIA AISVSLQGAP CGQKPVDTEC
     SSSQVHYHSE ESMSDASAES GATRQTDESE KTGSKVEDNS CTMVPGGGSR NDNTSDCGPL
     SHKGAIDAGD YETSLLAGQQ SDTATDSDSD DYFYDTPLFE DEDHDSLILQ GDDRDCLQPE
     DYDTSLQEEN DRTPPPDDIF YDVMKEKENP EFPHGGMDES LGVENKVCCP QGFPVGIEKP
     ELYLAGEKEF NSGGSEQLVE SVSESENPPG LWDSESDSLT EGEIIGRKER LGASLTPDGH
     WRGDREECDT SRESQSDTDG VGSIQSSESY RPYMSDGSDL DEEDNGGRSS EDSGDGRGGQ
     GVADEGGEPQ YQADPTQLYT AIRKEHGGET QNVSDMIPLD KTHSYSPLET QHGAGVFQPE
     SAGKGGWDTE RSSHPELTTE ADEEDEASLS THMATKGVSL SNAEGTASEE IRLVQGPDSS
     GILKAEDLEN VSPEISPSSD NIVRSEAELG GGASEDGHLS FTGSDRDQQG PGRGLVKGRD
     GQSDKLVDET SIREMGFQKE GVLMSSPEEG GEEERDLEPF PNGSATESLN MGKSQVPPLL
     THTEELSHRG APHTTTMTTT MTLEGEAKNV QTGLTESPVL LETLAEIFDT PASKVTRADL
     TSAVTASEMK SQVKEDSLTG GPEKETGPCT SLGHCDKCIH VDMLEPNEHT PSCALVAPPT
     VKDNLCSVNN AGEKSVRPQE DWPPAAEVRL SDACVEESIS EGKAGILQFT PENSDSTLSR
     LPHQSVAGWG KSADSVQARL PVSGVRHTSA DTLDVGCPQL ESSREKASAE EEPHRERALS
     LKPQEREHHM LGFVEDGRSI LKSSLDKVHM NLQEVGDPSA GTGTKISIQN LIRRAILSEL
     PNEVSNVPSH GISPISNSSE VRAESGGDPF CITSFLHLLK QNQPPQETPG ISELAKVLTQ
     MDCDPEQRGL GSELLPPQLK NAFYKLLFDG YATEKDQAEA LGQTSCAVPK MAEEKPHVCS
     DLRNKEGHHC PLNPQAVGEA EVEPFSVHIA ALPGGEKLGE LCSEPPEHSE STSGSKERSS
     DGSSKEKCSN GLQQCLQHTE KMHEYLVLLQ DMKPPLDNQA SVESSLEALK SQLKQLEAFE
     LGLAPIAVFL RKDLKLAEEF LKSFPSDLPR RHHEELSKSH QRLQNAFSSL SSVSSERMKL
     IKLAINSEMS KLAVRHEDFL HKLTSYSDWV SEKSRSVKAI QTVNVQDTEL VKNSVKFLKN
     VLADLSHTKM QLETTAFDVQ SFISDYAQDL SPSQSRQLLR LLNTTQKGFL DLQELVTTEA
     DRLEALLQLE QELGHQKVVA ERQQEYREKL QGLCDLLTQT ENRLISNQEA FVIGDGTVEL
     QKYQSKQEEL QRDMQGSTQA MEEIVRNTEL FLKESGDELS QADRALIEQK LNEVKMKCAQ
     LNLKAEQSRK ELDKAVTTAL KEETEKVAAV RQLEESKTKI ENLLNWLSNV EEDSEGVWTK
     HTQPMEQNGT YLHEGDSKLG AGEEDEVNGN LLETDAEGHS EATKGNLNQQ YEKVKAQHGK
     IMAQHQAVLL ATQSAQVLLE KQGHYLSPEE KEKLQKNTQE LKVHYEKVLA ECEKKVKLTH
     SLQEELEKFD TDYSEFEHWL QQSEQELANL EAGADDLSGL MDKLTRQKSF SEDVISHKGD
     LRYITISGNR VIDAAKSCSK RDSDRIGKDS VETSATHREV QTKLDQVTDR FRSLYSKCSV
     LGNNLKDLVD QYQQYEDASC GLLSGLQACE AKASKHLREP IALDPKNLQR QLEETKALQG
     QISSQQVAVE KLKKTAEVLL DAKGSLLPAK NDIQKTLDDI VGRYDDLSKC VNERNEKLQI
     TLTRSLSVQD ALDEMLDWMG SVESSLVKPG QVPLNSTALQ DLISKDTMLE QDITGRQSSI
     NAMNEKVKTF IETTDPSTAS SLQAKMKDLS ARFSEASQKH KEKLAKMVEL KAKVEQFEKL
     SDKLQTFLET QSQALTEVAM PGKDVPELSQ HMQESTAKFL EHRKDLEALH SLLKEISSHG
     LPGDKALVFE KTNNLSRKFK EMEDTIQEKK DALSSCQEQL SAFQTLAQSL KTWIKETTKQ
     VPVVKPSLGT EDLRKSLEET KKLQEKWNLK APEIHKASNS GVSLCNLLSA LISPAKAIAA
     AKSGGVILNG EGTDTNTQDF LANKGLTSIK KDMTDISHSY EDLGLLLKDK IVELNTKLSK
     LQKAQEESSA MMQWLEKMNK TASRWRQTPT PADTESVKLQ VEQNKSFEAE LKQNVNKVQE
     LKDKLSELLE ENPEAPEAQS WKQALAEMDT KWQELNQLTM DRQQKLEESS NNLTQFQTTE
     AQLKQWLMEK ELMVSVLGPL SIDPNMLNTQ KQQVQILLQE FDTRKPQYEQ LTAAGQGILS
     RPGEDPSLHG IVNEQLEAVT QKWDNLTGQL RDRCDWIDQA IVKSTQYQSL LRSLSGTLTE
     LDDKLSSGLT SGALPDAVNQ QLEAAQRLKQ EIEQQAPKIK EAQEVCEDLS ALVKEEYLKA
     ELSRQLEGIL KSFKDIEQKT ENHVQHLQSA CASSHQFQQM SKDFQAWLDA KKEEQRDSPP
     ISAKLDVLES LLNSQKDFGK TFTEQSNIYE KTISEGENLL LKTQGAEKAA LQLQLNTMKT
     DWDRFRKQVK EREEKLKDSL EKALKYREQV ETLRPWIDRC QHSLDGVTFS LDPTESESSI
     AELKSLQKEM DHHFGMLELL NNTANSLLSV CEVDKEAVTE ENQSLMEKVN RVTEQLQSKT
     VSLENMAQKF KEFQEVSRDT QRQLQDTKEQ LEVHHSLGPQ AYSNKHLSVL QAQQKSLQTL
     KQQVDEAKRL AQDLVVEAAD SKGTSDVLLQ AETLAEEHSE LSQQVDEKCS FLETKLQGLG
     HFQNTIREMF SQFTECDDEL DGMAPVGRDA ETLRKQKACM QTFLKKLEAL MASNDSANRT
     CKMMLATEET SPDLIGVKRD LEALSKQCNK LLDRAKTREE QVDGATEKLE EFHRKLEEFS
     TLLQKAEEHE ESQGPVGTET ETINQQLDVF KVFQKEEIEP LQVKQQDVNW LGQGLIQSAA
     ANTCTQGLEH DLDSVNSRWK TLNKKVAQRT SQLQEALLHC GRFQDALESL LSWMADTEEL
     VANQKPPSAE FKVVKAQIQE QKLLQRLLED RKSTVEVIKR EGEKIAASAE PADRVKLTRQ
     LSLLDSRWEA LLSRAEARNR QLEGISVVAQ EFHGTLEPLN EWLTAVEKKL ANSEPIGTQA
     PKLEEQISQH KALQEDILLR KQSVDQALLN GLELLKQTTG DEVLIIQDKL EAIKARYKDI
     TKLSADVAKT LEHALQLAGQ LQSMHKELCN WLDKVEVELL SYETQGLKGE AASQVQERQK
     ELKNEVRSNK ALVDSLNEVS SALLELVPCR AKEGLEKTIA DDNEPLPDCE PTQSRHKVEE
     IDAAILRSQQ FEQAADAELS WITETQKKLM SLGDIRLEQD QTSAQLQVQK AFTMDILRHK
     DIIDELVTSG HKIMTTSGEE EKQSMKKKLD KVLKKYDAVC QINSERHLQL ERAQSLVSQF
     WETYEELWPW LTETQRIISQ LPAPALEYET FERQQEEHRQ LRELIAEHKP HIDKMNKTGP
     QLLELSPKEG IYIQEKYVAA DTLYSQIKED VKKRAVVLDE AISQSTQFHD KIDQILESLE
     RIAERLRQPP SISAEVEKIK EQIGENKSVS VDMEKLQPLY ETLRQRGEEM IARSEGTEKD
     VSARAVQDKL DQMVFIWGSI HTLVEEREAK LLDVMELAEK FWCDHMSLVV TIKDTQDFIR
     DLEDPGIDPS VVKQQQEAAE AIREEIDGLQ EELDMVITLG SELIAACGEP DKPIVKKSID
     ELNSAWDSLN KAWKDRVDRL EEAMQAAVQY QDGLQGIFDW VDIAGDKLAT MSPIGTDLET
     VKQQIEELKQ FKSEAYQQQM EMERLNHQAE LLLKKVTEEA DKHTVQDPLM ELKLIWDSLD
     ERIVSRQHKL EGTLLALGQF QHALDELLAW LTHTKGLLSE QKPVGGDPKA IEIELAKHHV
     LQNDVLAHQS TVEAVNKAGN DLIESSEGEE ASNLQYKLRI LNQRWQDILE KTDQRKQQLD
     SALRQAKGFH GEIEDLQQWL TDTERHLLAS KPLGGLPETA KEQLNAHMEV CTAFAIKEET
     YKSLMLRGQQ MLARCPRSAE TNIDQDITNL KEKWESVKSK LNEKKTKLEE ALHLAMNFHN
     SLQDFINWLT QAEQTLNVAS RPSLILDTIL FQIDEHKVFA NEVNSHREQI IELDKTGTHL
     KYFSQKQDVV LIKNLLISVQ SRWEKVVQRL VERGRSLDEA RKRAKQFHEA WSKLMEWLEE
     SEKSLDSELE IANDPDKIKA QLVQHKEFQK SLGGKHSVYD TTNRTGRSLK EKTSLADDNL
     KLDNMLSELR DKWDTICGKS VERQNKLEEA LLFSGQFTDA LQALIDWLYR VEPQLAEDQP
     VHGDIDLVMS LIDNHKVFQK ELGKRTSSVQ ALKRSARELI EGSRDDSSWV RVQMQELSTR
     WETVCALSIS KQTRLESALQ QAEEFHSVVH TLLEWLAEAE QTLRFHGALP DDEDALRTLI
     EQHKEFMKRL EEKRAELSKA TGMGDALLAV CHPDSITTIK HWITIIQARF EEVLAWAKQH
     QQRLAGALAG LIAKQELLET LLAWLQWAET TLTEKDKEVI PQEIEEVKTL IAEHQTFMEE
     MTRKQPDVDK VTKTYKRRAT DPPSLQSHIP VLDKGRAGRK RFPASGFYPS GSQTQIETKN
     PRVNLLVSKW QQVWLLALER RRKLNDALDR LEELREFANF DFDIWRKKYM RWMNHKKSRV
     MDFFRRIDKD QDGKITRQEF IDGILSSKFP TSRLEMSAVA DIFDRDGDGY IDYYEFVAAL
     HPNKDAYKPI TDADKIGDEV TRQVAKCKCA KRFQVEQIGD NKYRFFLGNQ FGDSQQLRLV
     RILRSTVMVR VGGGWMALDE FLVKNDPCRV HHHGSKMLRS ESNSSITATQ PTLAKGRTNM
     ELREKFILAD GASQGMAAFR PRGRRSRPSS RGASPNRSTS GSSHACQAAS PPVPAAASTP
     KGTPIQGSKL RLPGYLSGKG FHSGEDSALI TTAAARVRTQ FAESRKTPSR PGSRAGSKAG
     SRASSRRGSD ASDFDISEIQ SVCSDVETVP QTHRPVPRAG SRPSTAKPSK IPTPQRRSPA
     SKLDKSSKR
//
ID   DCBD2_MOUSE             Reviewed;         769 AA.
AC   Q91ZV3; A6X950; Q8BKI4;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Discoidin, CUB and LCCL domain-containing protein 2;
DE   AltName: Full=Endothelial and smooth muscle cell-derived neuropilin-like protein;
DE   Flags: Precursor;
GN   Name=Dcbld2; Synonyms=Esdn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR;
RX   PubMed=11447234; DOI=10.1074/jbc.M105293200;
RA   Kobuke K., Furukawa Y., Sugai M., Tanigaki K., Ohashi N.,
RA   Matsumori A., Sasayama S., Honjo T., Tashiro K.;
RT   "ESDN, a novel neuropilin-like membrane protein cloned from vascular
RT   cells with the longest secretory signal sequence among eukaryotes, is
RT   up-regulated after vascular injury.";
RL   J. Biol. Chem. 276:34105-34114(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 168-769.
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Contains 1 CUB domain.
CC   -!- SIMILARITY: Contains 1 F5/8 type C domain.
CC   -!- SIMILARITY: Contains 1 LCCL domain.
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DR   EMBL; AF387548; AAL30179.1; -; mRNA.
DR   EMBL; CT027564; CAO78160.1; -; Genomic_DNA.
DR   EMBL; BC066097; AAH66097.1; -; mRNA.
DR   EMBL; AK051889; BAC34801.1; -; mRNA.
DR   IPI; IPI00131452; -.
DR   RefSeq; NP_082799.2; NM_028523.3.
DR   UniGene; Mm.373589; -.
DR   ProteinModelPortal; Q91ZV3; -.
DR   SMR; Q91ZV3; 67-452.
DR   STRING; Q91ZV3; -.
DR   PhosphoSite; Q91ZV3; -.
DR   PRIDE; Q91ZV3; -.
DR   Ensembl; ENSMUST00000046663; ENSMUSP00000039915; ENSMUSG00000035107.
DR   GeneID; 73379; -.
DR   KEGG; mmu:73379; -.
DR   UCSC; uc007zno.1; mouse.
DR   CTD; 73379; -.
DR   MGI; MGI:1920629; Dcbld2.
DR   eggNOG; roNOG12469; -.
DR   HOGENOM; HBG715002; -.
DR   HOVERGEN; HBG106294; -.
DR   InParanoid; Q91ZV3; -.
DR   OMA; FKTSGCY; -.
DR   OrthoDB; EOG4KKZ2H; -.
DR   NextBio; 338119; -.
DR   ArrayExpress; Q91ZV3; -.
DR   Bgee; Q91ZV3; -.
DR   CleanEx; MM_DCBLD2; -.
DR   Genevestigator; Q91ZV3; -.
DR   GermOnline; ENSMUSG00000035107; Mus musculus.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0005887; C:integral to plasma membrane; ISS:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR   GO; GO:0042060; P:wound healing; ISS:UniProtKB.
DR   InterPro; IPR000421; Coagulation_factor_5/8-type_C.
DR   InterPro; IPR000859; CUB.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR004043; LCCL.
DR   Gene3D; G3DSA:2.60.120.290; CUB; 1.
DR   Gene3D; G3DSA:2.170.130.20; LCCL; 1.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF03815; LCCL; 1.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00231; FA58C; 1.
DR   SMART; SM00603; LCCL; 1.
DR   SUPFAM; SSF49854; CUB; 1.
DR   SUPFAM; SSF49785; Gal_bind_like; 1.
DR   SUPFAM; SSF69848; LCCL; 1.
DR   PROSITE; PS01180; CUB; 1.
DR   PROSITE; PS01285; FA58C_1; 1.
DR   PROSITE; PS01286; FA58C_2; FALSE_NEG.
DR   PROSITE; PS50022; FA58C_3; 1.
DR   PROSITE; PS50820; LCCL; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     63       Potential.
FT   CHAIN        64    769       Discoidin, CUB and LCCL domain-containing
FT                                protein 2.
FT                                /FTId=PRO_0000021079.
FT   TOPO_DOM     64    523       Extracellular (Potential).
FT   TRANSMEM    524    544       Helical; (Potential).
FT   TOPO_DOM    545    769       Cytoplasmic (Potential).
FT   DOMAIN       69    184       CUB.
FT   DOMAIN      184    282       LCCL.
FT   DOMAIN      289    446       F5/8 type C.
FT   COMPBIAS    503    506       Poly-Thr.
FT   MOD_RES     601    601       Phosphoserine (By similarity).
FT   MOD_RES     710    710       Phosphotyrosine (By similarity).
FT   MOD_RES     727    727       Phosphotyrosine (By similarity).
FT   MOD_RES     744    744       Phosphotyrosine (By similarity).
FT   CARBOHYD     92     92       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    152    152       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    269    269       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    469    469       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    511    511       N-linked (GlcNAc...) (Potential).
FT   DISULFID     69     96       By similarity.
FT   DISULFID    123    145       By similarity.
FT   DISULFID    212    234       By similarity.
FT   DISULFID    289    446       By similarity.
FT   CONFLICT    478    479       Missing (in Ref. 3).
SQ   SEQUENCE   769 AA;  83774 MW;  73C1F1646FA3F017 CRC64;
     MASRAPLRAA RSPQGPGGPA APAATGRAAL PSAGCCPLPP GRNSSSRPRL LLLLLLLLQD
     AGGQQGDGCG HTVLGPESGT LTSINYPHTY PNSTVCEWEI RVRTGERIRI KFGDFDIEDS
     DYCHLNYLKI FNGIGVSRTE IGKYCGLGLQ MNQSIESKGS EVTVLFMSGT HAAGRGFLAS
     YSVIDKEDLI TCLDTVSNFL EPEFSKYCPA GCLLPFAEIS GTIPHGYRDS SPLCMAGIHA
     GVVSNVLGGQ ISIVISKGTP YYESSLANNV TSTVGYLSAS LFTFKTSGCY GTLGMESGVI
     ADPQITASSA LEWTDHMGQE NSWTAEKARL RKPGPPWAAF ATDEHQWLQI DLNKEKKITG
     IVTTGSTMIE HSYYVSAYRV LYSDDGQRWT VYREPGVDQD KIFQGNKDYH KDVRNNFLPP
     IIARFIRVNP VQWQQKIAMK VELLGCQFTL KGRLPKLTPP PRNGNNLRNT TARPKLGKGR
     APKFTQVLQP RSRNELPVQP AETTTTPDIK NTTVTPSVTK DVALAAVLVP VLVMALTTLI
     LILVCAWHWR NRKKKTEGAY DLPHWDRAGW WKGMKQLLPA KSVDHEETPV RYSTSEVSHL
     SAREVTTVLQ ADSAEYAQPL VGGIVGTLHQ RSTFKPEEGK EAGYADLDPY NSPMQEVYHA
     YAEPLPVTGP EYATPIVMDM SGHPTASVGL PSTSTFKTAG TQPHALVGTY NTLLSRTDSC
     SSGQAQYDTP KGGKSAATPE ELVYQVPQST QELSGAGRDE KFDAFKEIL
//
ID   SMCA5_MOUSE             Reviewed;        1051 AA.
AC   Q91ZW3; Q8C791; Q8CA22; Q8VDG1; Q925M9;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5;
DE            EC=3.6.4.-;
DE   AltName: Full=Sucrose nonfermenting protein 2 homolog;
DE            Short=mSnf2h;
GN   Name=Smarca5; Synonyms=Snf2h;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   TISSUE=Erythroleukemia;
RX   PubMed=10914549; DOI=10.1038/sj.leu.2401807;
RA   Stopka T., Zakova D., Fuchs O., Kubrova O., Blafkova J., Jelinek J.,
RA   Necas E., Zivny J.;
RT   "Chromatin remodeling gene SMARCA5 is dysregulated in primitive
RT   hematopoietic cells of acute leukemia.";
RL   Leukemia 14:1247-1252(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=21259974; PubMed=11359880;
RX   DOI=10.1046/j.1471-4159.2001.00324.x;
RA   Lazzaro M.A., Picketts D.J.;
RT   "Cloning and characterization of the murine Imitation Switch (ISWI)
RT   genes: differential expression patterns suggest distinct developmental
RT   roles for Snf2h and Snf2l.";
RL   J. Neurochem. 77:1145-1156(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 440-1007.
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE NORC COMPLEX,
RP   AND INTERACTION WITH BAZ2A.
RX   MEDLINE=21423468; PubMed=11532953; DOI=10.1093/emboj/20.17.4892;
RA   Strohner R., Nemeth A., Jansa P., Hofmann-Rohrer U., Santoro R.,
RA   Laengst G., Grummt I.;
RT   "NoRC -- a novel member of mammalian ISWI-containing chromatin
RT   remodeling machines.";
RL   EMBO J. 20:4892-4900(2001).
RN   [6]
RP   FUNCTION, IDENTIFICATION IN THE WICH COMPLEX, AND INTERACTION WITH
RP   BAZ1B.
RX   MEDLINE=21977304; PubMed=11980720; DOI=10.1093/emboj/21.9.2231;
RA   Bozhenok L., Wade P.A., Varga-Weisz P.;
RT   "WSTF-ISWI chromatin remodeling complex targets heterochromatic
RT   replication foci.";
RL   EMBO J. 21:2231-2241(2002).
RN   [7]
RP   FUNCTION, IDENTIFICATION IN THE NORC COMPLEX, AND INTERACTION WITH
RP   BAZ2A AND HDAC1.
RX   PubMed=12198165; DOI=10.1093/emboj/cdf460;
RA   Zhou Y., Santoro R., Grummt I.;
RT   "The chromatin remodeling complex NoRC targets HDAC1 to the ribosomal
RT   gene promoter and represses RNA polymerase I transcription.";
RL   EMBO J. 21:4632-4640(2002).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH BAZ2A; DNMT1; DNMT3B AND HDAC1.
RX   PubMed=12368916; DOI=10.1038/ng1010;
RA   Santoro R., Li J., Grummt I.;
RT   "The nucleolar remodeling complex NoRC mediates heterochromatin
RT   formation and silencing of ribosomal gene transcription.";
RL   Nat. Genet. 32:393-396(2002).
RN   [9]
RP   FUNCTION.
RX   PubMed=14617767; DOI=10.1073/pnas.2336105100;
RA   Stopka T., Skoultchi A.I.;
RT   "The ISWI ATPase Snf2h is required for early mouse development.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:14097-14102(2003).
RN   [10]
RP   REVIEW, AND CHARACTERIZATION OF ISWI COMPLEXES.
RX   PubMed=15284901; DOI=10.1139/o04-044;
RA   Dirscherl S.S., Krebs J.E.;
RT   "Functional diversity of ISWI complexes.";
RL   Biochem. Cell Biol. 82:482-489(2004).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [12]
RP   INTERACTION WITH MYO1C.
RX   PubMed=16514417; DOI=10.1038/sj.embor.7400657;
RA   Percipalle P., Fomproix N., Cavellan E., Voit R., Reimer G.,
RA   Krueger T., Thyberg J., Scheer U., Grummt I.,
RA   Oestlund Farrants A.-K.O.;
RT   "The chromatin remodelling complex WSTF-SNF2h interacts with nuclear
RT   myosin 1 and has a role in RNA polymerase I transcription.";
RL   EMBO Rep. 7:525-530(2006).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55 AND SER-65, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [15]
RP   FUNCTION, AND INTERACTION WITH BAZ1B.
RX   PubMed=19092802; DOI=10.1038/nature07668;
RA   Xiao A., Li H., Shechter D., Ahn S.H., Fabrizio L.A.,
RA   Erdjument-Bromage H., Ishibe-Murakami S., Wang B., Tempst P.,
RA   Hofmann K., Patel D.J., Elledge S.J., Allis C.D.;
RT   "WSTF regulates the H2A.X DNA damage response via a novel tyrosine
RT   kinase activity.";
RL   Nature 457:57-62(2009).
CC   -!- FUNCTION: Helicase that possesses intrinsic ATP-dependent
CC       nucleosome-remodeling activity. Complexes containing SMARCA5 are
CC       capable of forming ordered nucleosome arrays on chromatin; this
CC       may require intact histone H4 tails. Also required for replication
CC       of pericentric heterochromatin in S-phase specifically in
CC       conjunction with BAZ1A. Probably plays a role in repression of
CC       polI dependent transcription of the rDNA locus, through the
CC       recruitment of the SIN3/HDAC1 corepressor complex to the rDNA
CC       promoter. Essential component of the WICH complex, a chromatin
CC       remodeling complex that mobilizes nucleosomes and reconfigures
CC       irregular chromatin to a regular nucleosomal array structure. The
CC       WICH complex regulates the transcription of various genes, has a
CC       role in RNA polymerase I and RNA polymerase III transcription,
CC       mediates the histone H2AX phosphorylation at 'Tyr-142', and is
CC       involved in the maintenance of chromatin structures during DNA
CC       replication processes. Essential component of the NoRC (nucleolar
CC       remodeling complex) complex, a complex that mediates silencing of
CC       a fraction of rDNA by recruiting histone-modifying enzymes and DNA
CC       methyltransferases, leading to heterochromatin formation and
CC       transcriptional silencing.
CC   -!- SUBUNIT: Catalytic subunit of the four known chromatin-remodeling
CC       complexes: CHRAC, RSF, ACF/WCRF, and WICH. Each complex contains
CC       subunits which may regulate the specificity or catalytic activity
CC       of SMARCA5. ACF/WCRF contains BAZ1A; CHRAC contains BAZ1A, CHRAC1,
CC       and POLE3; RSF contains HBXAP; WICH contains BAZ1B/WSTF.SMARCA5 is
CC       the catalytic subunit of the NoRC chromatin-remodeling complex,
CC       which also contains BAZ2A/TIP5. The BAZ2A/TIP5 subunit of NoRC
CC       also interacts with DNMT1, DNMT3B and HDAC1, which allows NoRC to
CC       actively suppress rDNA transcription by a combination of
CC       nucleosome remodeling, histone deacetylation, and DNA methylation.
CC       Catalytic subunit of SMARCA5/cohesin/NuRD complexes. Component of
CC       the B-WICH complex, at least composed of SMARCA5/SNF2H,
CC       BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Interacts
CC       with MYO1C.
CC   -!- INTERACTION:
CC       Q9Z277:Baz1b; NbExp=1; IntAct=EBI-927547, EBI-927576;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- DEVELOPMENTAL STAGE: Expressed in CD34-positive erythrocyte
CC       progenitor cells. Down-regulated upon differentiation.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SIMILARITY: Contains 2 SANT domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH21922.1; Type=Erroneous initiation;
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DR   EMBL; AF375046; AAL25793.1; -; mRNA.
DR   EMBL; AF325921; AAK52454.1; -; mRNA.
DR   EMBL; BC021922; AAH21922.1; ALT_INIT; mRNA.
DR   EMBL; BC053069; AAH53069.1; -; mRNA.
DR   EMBL; AK039811; BAC30458.1; -; mRNA.
DR   EMBL; AK052320; BAC34934.2; -; mRNA.
DR   IPI; IPI00396739; -.
DR   RefSeq; NP_444354.2; NM_053124.2.
DR   UniGene; Mm.246803; -.
DR   ProteinModelPortal; Q91ZW3; -.
DR   SMR; Q91ZW3; 162-686, 742-1020.
DR   DIP; DIP-36073N; -.
DR   IntAct; Q91ZW3; 8.
DR   MINT; MINT-1867515; -.
DR   STRING; Q91ZW3; -.
DR   PhosphoSite; Q91ZW3; -.
DR   PRIDE; Q91ZW3; -.
DR   Ensembl; ENSMUST00000043359; ENSMUSP00000044361; ENSMUSG00000031715.
DR   GeneID; 93762; -.
DR   KEGG; mmu:93762; -.
DR   UCSC; uc009mja.1; mouse.
DR   CTD; 93762; -.
DR   MGI; MGI:1935129; Smarca5.
DR   GeneTree; ENSGT00590000082988; -.
DR   HOGENOM; HBG717285; -.
DR   HOVERGEN; HBG056329; -.
DR   InParanoid; Q91ZW3; -.
DR   OMA; KEILFYR; -.
DR   OrthoDB; EOG44J2H9; -.
DR   PhylomeDB; Q91ZW3; -.
DR   NextBio; 351651; -.
DR   ArrayExpress; Q91ZW3; -.
DR   Bgee; Q91ZW3; -.
DR   Genevestigator; Q91ZW3; -.
DR   GermOnline; ENSMUSG00000031715; Mus musculus.
DR   GO; GO:0005677; C:chromatin silencing complex; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR   GO; GO:0016563; F:transcription activator activity; IMP:MGI.
DR   GO; GO:0000183; P:chromatin silencing at rDNA; IDA:UniProtKB.
DR   GO; GO:0006302; P:double-strand break repair; IMP:BHF-UCL.
DR   GO; GO:0009790; P:embryo development; IMP:MGI.
DR   InterPro; IPR015194; ATPase_nucl-remodel_HAND-dom.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR001005; SANT_DNA-bd.
DR   InterPro; IPR017884; SANT_eukarya.
DR   InterPro; IPR015195; SLIDE.
DR   InterPro; IPR000330; SNF2_N.
DR   Pfam; PF09110; HAND; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF09111; SLIDE; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF46689; Homeodomain_like; 2.
DR   SUPFAM; SSF101224; Nucl_remodel_ATPase_ISWI_HAND; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; FALSE_NEG.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51293; SANT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Chromatin regulator; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Repeat.
FT   CHAIN         1   1051       SWI/SNF-related matrix-associated actin-
FT                                dependent regulator of chromatin
FT                                subfamily A member 5.
FT                                /FTId=PRO_0000074355.
FT   DOMAIN      191    356       Helicase ATP-binding.
FT   DOMAIN      486    637       Helicase C-terminal.
FT   DOMAIN      839    891       SANT 1.
FT   DOMAIN      942   1006       SANT 2.
FT   NP_BIND     204    211       ATP (Potential).
FT   MOTIF       307    310       DEAH box.
FT   COMPBIAS      7     13       Poly-Pro.
FT   MOD_RES      55     55       Phosphothreonine.
FT   MOD_RES      65     65       Phosphoserine.
FT   MOD_RES     112    112       Phosphothreonine (By similarity).
FT   MOD_RES     114    114       Phosphothreonine (By similarity).
FT   MOD_RES     115    115       Phosphoserine (By similarity).
FT   MOD_RES     136    136       Phosphoserine.
FT   MOD_RES     439    439       N6-acetyllysine (By similarity).
FT   MOD_RES     698    698       Phosphoserine (By similarity).
FT   MOD_RES     754    754       Phosphoserine (By similarity).
FT   CONFLICT     44     45       AP -> GS (in Ref. 2; AAK52454).
FT   CONFLICT    143    143       R -> C (in Ref. 2; AAK52454).
FT   CONFLICT    157    157       S -> R (in Ref. 2; AAK52454).
FT   CONFLICT    249    249       K -> R (in Ref. 2; AAK52454).
FT   CONFLICT    318    318       K -> N (in Ref. 2; AAK52454).
FT   CONFLICT    373    373       C -> S (in Ref. 2; AAK52454).
FT   CONFLICT    498    498       G -> S (in Ref. 2; AAK52454).
SQ   SEQUENCE   1051 AA;  121627 MW;  C6CB69E7FADE73FC CRC64;
     MSSAVEPPPP PPPESAPSKP SAAGAGGSSS GNKGGPEGGA APAAPCAAGS GPADTEMEEV
     FDHGSPGKQK EIQEPDPTYE EKMQTDRANR FEYLLKQTEL FAHFIQPAAQ KTPTSPLKMK
     PGRPRVKKDE KQNLLSVGDY RHRRTEQEED EELLTESSKA TNVCTRFEDS PSYVKWGKLR
     DYQVRGLNWL ISLYENGING ILADEMGLGK TLQTISLLGY MKHYRNIPGP HMVLVPKSTL
     HNWMSEFKKW VPTLRSVCLI GDKEQRAAFV RDVLLPGEWD VCVTSYEMLI KEKSVFKKFN
     WRYLVIDEAH RIKNEKSKLS EIVREFKTTN RLLLTGTPLQ NNLHELWSLL NFLLPDVFNS
     ADDFDSWFDT NNCLGDQKLV ERLHMVLRPF LLRRIKADVE KSLPPKKEVK IYVGLSKMQR
     EWYTRILMKD IDILNSAGKM DKMRLLNILM QLRKCCNHPY LFDGAEPGPP YTTDMHLVTN
     SGKMVVLDKL LPKLKEQGSR VLIFSQMTRV LDILEDYCMW RNYEYCRLDG QTPHDERQDS
     INAYNEPNST KFVFMLSTRA GGLGINLATA DVVILYDSDW NPQVDLQAMD RAHRIGQTKT
     VRVFRFITDN TVEERIVERA EMKLRLDSIV IQQGRLVDQN LNKIGKDEML QMIRHGATHV
     FASKESEITD EDIDGILERG AKKTAEMNEK LSKMGESSLR NFTMDTESSV YNFEGEDYRE
     KQKIAFTEWI EPPKRERKAN YAVDAYFREA LRVSEPKAPK APRPPKQPNV QDFQFFPPRL
     FELLEKEILY YRKTIGYKVP RSPDLPNAAQ AQKEEQLKID EAEPLNDEEL EEKEKLLTQG
     FTNWNKRDFN QFIKANEKWG RDDIENIARE VEGKTPEEVI EYSAVFWERC NELQDIEKIM
     AQIERGEARI QRRISIKKAL DTKIGRYKAP FHQLRISYGT NKGKNYTEEE DRFLICMLHK
     LGFDKENVYD ELRQCIRNSP QFRFDWFLKS RTAMELQRRC NTLITLIERE NMELEEKEKA
     EKKKRGPKPS TQKRKMDGAP DGRGRKKKLK L
//
ID   LRP1_MOUSE              Reviewed;        4545 AA.
AC   Q91ZX7; Q61291; Q920Y4;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Prolow-density lipoprotein receptor-related protein 1;
DE            Short=LRP-1;
DE   AltName: Full=Alpha-2-macroglobulin receptor;
DE            Short=A2MR;
DE   AltName: CD_antigen=CD91;
DE   Contains:
DE     RecName: Full=Low-density lipoprotein receptor-related protein 1 85 kDa subunit;
DE              Short=LRP-85;
DE   Contains:
DE     RecName: Full=Low-density lipoprotein receptor-related protein 1 515 kDa subunit;
DE              Short=LRP-515;
DE   Contains:
DE     RecName: Full=Low-density lipoprotein receptor-related protein 1 intracellular domain;
DE              Short=LRPICD;
DE   Flags: Precursor;
GN   Name=Lrp1; Synonyms=A2mr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=93250049; PubMed=8485155; DOI=10.1016/0167-4781(93)90244-8;
RA   Van Leuven F., Stas L., Raymakers L., Overbergh L., De Strooper B.,
RA   Hilliker C., Lorent K., Fias E., Umans L., Torrekens S., Serneels L.,
RA   Moechars D., Van den Berghe H.;
RT   "Molecular cloning and sequencing of the murine alpha-2-macroglobulin
RT   receptor cDNA.";
RL   Biochim. Biophys. Acta 1173:71-74(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=129/J, and CBA;
RX   MEDLINE=22145789; PubMed=12151109; DOI=10.1016/S0167-4781(02)00419-0;
RA   Smeijers L., Willems S., Lauwers A., Thiry E., van Leuven F.,
RA   Roebroek A.J.M.;
RT   "Functional expression of murine LRP1 requires correction of Lrp1 cDNA
RT   sequences.";
RL   Biochim. Biophys. Acta 1577:155-158(2002).
RN   [3]
RP   INTERACTION WITH MAFB.
RX   PubMed=15135046; DOI=10.1016/j.febslet.2004.03.069;
RA   Petersen H.H., Hilpert J., Jacobsen C., Lauwers A., Roebroek A.J.M.,
RA   Willnow T.E.;
RT   "Low-density lipoprotein receptor-related protein interacts with MafB,
RT   a regulator of hindbrain development.";
RL   FEBS Lett. 565:23-27(2004).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=1423604; DOI=10.1016/0092-8674(92)90511-A;
RA   Herz J., Clouthier D.E., Hammer R.E.;
RT   "LDL receptor-related protein internalizes and degrades uPA-PAI-1
RT   complexes and is essential for embryo implantation.";
RL   Cell 71:411-421(1992).
RN   [5]
RP   ERRATUM.
RX   PubMed=8490961; DOI=10.1016/0092-8674(93)90130-I;
RA   Herz J., Couthier D.E., Hammer R.E.;
RL   Cell 73:428-428(1993).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4521; SER-4524 AND
RP   THR-4525, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4521, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-730; ASN-2128 AND
RP   ASN-3049, AND MASS SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-447, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Endocytic receptor involved in endocytosis and in
CC       phagocytosis of apoptotic cells. Required for early embryonic
CC       development. Involved in cellular lipid homeostasis. Involved in
CC       the plasma clearance of chylomicron remnants and activated LRPAP1
CC       (alpha 2-macroglobulin), as well as the local metabolism of
CC       complexes between plasminogen activators and their endogenous
CC       inhibitors. May modulate cellular events, such as APP metabolism,
CC       kinase-dependent intracellular signaling, neuronal calcium
CC       signaling as well as neurotransmission.
CC   -!- SUBUNIT: Heterodimer of an 85-kDa membrane-bound carboxyl subunit
CC       and a non-covalently attached 515-kDa amino-terminal subunit.
CC       Found in a complex with PID1/PCLI1, LRP1 and CUBNI. Interacts with
CC       SNX17, PID1/PCLI1, PDGF and CUBN. The intracellular domain
CC       interacts with SHC1, GULP1 and DAB1. Interacts with LRPAP1 (By
CC       similarity). Intracellular domain interacts with MAFB.
CC   -!- INTERACTION:
CC       P97318:Dab1; NbExp=1; IntAct=EBI-300955, EBI-81680;
CC       Q62108:Dlg4; NbExp=1; IntAct=EBI-300955, EBI-300895;
CC       Q9WVI9:Mapk8ip1; NbExp=1; IntAct=EBI-300955, EBI-74515;
CC       Q9ERE9:Mapk8ip2; NbExp=1; IntAct=EBI-300955, EBI-74576;
CC       Q9D6K5:Synj2bp; NbExp=1; IntAct=EBI-300955, EBI-300910;
CC   -!- SUBCELLULAR LOCATION: Low-density lipoprotein receptor-related
CC       protein 1 85 kDa subunit: Cell membrane; Single-pass type I
CC       membrane protein (By similarity). Membrane, coated pit (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Low-density lipoprotein receptor-related
CC       protein 1 515 kDa subunit: Cell membrane; Peripheral membrane
CC       protein; Extracellular side (By similarity). Membrane, coated pit
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Low-density lipoprotein receptor-related
CC       protein 1 intracellular domain: Cytoplasm (By similarity). Nucleus
CC       (By similarity). Note=After cleavage, the intracellular domain
CC       (LRPICD) is detected both in the cytoplasm and in the nucleus (By
CC       similarity).
CC   -!- PTM: Phosphorylated on serine and threonine residues (By
CC       similarity).
CC   -!- PTM: Phosphorylated on tyrosine residues upon stimulation with
CC       PDGF. Tyrosine phosphorylation promotes interaction with SHC1 (By
CC       similarity).
CC   -!- PTM: Cleaved into a 85 kDa membrane-spanning subunit (LRP-85) and
CC       a 515 kDa large extracellular domain (LRP-515) that remains non-
CC       covalently associated. Gamma-secretase-dependent cleavage of LRP-
CC       85 releases the intracellular domain from the membrane (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Death during early embryogenesis around 14
CC       dpc.
CC   -!- SIMILARITY: Belongs to the LDLR family.
CC   -!- SIMILARITY: Contains 22 EGF-like domains.
CC   -!- SIMILARITY: Contains 31 LDL-receptor class A domains.
CC   -!- SIMILARITY: Contains 34 LDL-receptor class B repeats.
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DR   EMBL; X67469; CAA47817.1; ALT_SEQ; mRNA.
DR   EMBL; AF367720; AAL09566.1; -; mRNA.
DR   EMBL; AF369477; AAL09567.1; -; Genomic_DNA.
DR   EMBL; AF369389; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369390; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369391; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369392; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369393; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369394; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369395; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369396; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369397; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369398; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369399; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369400; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369401; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369402; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369403; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369404; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369405; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369406; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369407; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369408; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369409; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369410; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369411; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369412; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369413; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369414; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369415; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369416; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369417; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369418; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369419; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369420; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369421; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369422; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369423; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369424; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369425; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369426; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369427; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369428; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369429; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369430; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369431; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369432; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369433; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369434; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369435; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369436; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369437; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369438; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369439; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369440; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369441; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369442; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369443; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369444; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369445; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369446; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369447; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369448; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369449; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369450; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369451; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369452; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369453; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369454; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369455; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369456; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369457; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369458; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369459; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369460; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369461; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369462; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369463; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369464; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369465; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369466; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369467; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369468; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369469; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369470; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369471; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369472; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369473; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369474; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369475; AAL09567.1; JOINED; Genomic_DNA.
DR   EMBL; AF369476; AAL09567.1; JOINED; Genomic_DNA.
DR   IPI; IPI00119063; -.
DR   PIR; S25111; S25111.
DR   RefSeq; NP_032538.2; NM_008512.2.
DR   UniGene; Mm.271854; -.
DR   HSSP; Q07954; 1J8E.
DR   ProteinModelPortal; Q91ZX7; -.
DR   SMR; Q91ZX7; 26-105, 119-193, 201-469, 487-846, 852-1582, 1584-1839, 1892-2151, 2164-2519, 2524-3334, 3413-4413.
DR   IntAct; Q91ZX7; 11.
DR   STRING; Q91ZX7; -.
DR   PhosphoSite; Q91ZX7; -.
DR   PRIDE; Q91ZX7; -.
DR   Ensembl; ENSMUST00000049149; ENSMUSP00000044004; ENSMUSG00000040249.
DR   GeneID; 16971; -.
DR   KEGG; mmu:16971; -.
DR   UCSC; uc007hjx.1; mouse.
DR   CTD; 16971; -.
DR   MGI; MGI:96828; Lrp1.
DR   GeneTree; ENSGT00580000081329; -.
DR   HOGENOM; HBG378855; -.
DR   HOVERGEN; HBG006292; -.
DR   InParanoid; Q91ZX7; -.
DR   OrthoDB; EOG42BX7K; -.
DR   NextBio; 291026; -.
DR   ArrayExpress; Q91ZX7; -.
DR   Bgee; Q91ZX7; -.
DR   Genevestigator; Q91ZX7; -.
DR   GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral to plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0043277; P:apoptotic cell clearance; IMP:MGI.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0030178; P:negative regulation of Wnt receptor signaling pathway; IDA:MGI.
DR   GO; GO:0010875; P:positive regulation of cholesterol efflux; IMP:BHF-UCL.
DR   GO; GO:0032429; P:regulation of phospholipase A2 activity; IMP:BHF-UCL.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR006150; Cys_repeat_1.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR001881; EGF_Ca-bd.
DR   InterPro; IPR013091; EGF_Ca-bd_2.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR009030; Growth_fac_rcpt.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   Gene3D; G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 8.
DR   Gene3D; G3DSA:4.10.400.10; LDL_rcpt_classA_cys-rich; 31.
DR   Pfam; PF07645; EGF_CA; 2.
DR   Pfam; PF00057; Ldl_recept_a; 31.
DR   Pfam; PF00058; Ldl_recept_b; 16.
DR   SMART; SM00181; EGF; 17.
DR   SMART; SM00179; EGF_CA; 3.
DR   SMART; SM00192; LDLa; 31.
DR   SMART; SM00135; LY; 35.
DR   SMART; SM00289; WR1; 4.
DR   SUPFAM; SSF57184; Grow_fac_recept; 2.
DR   SUPFAM; SSF57424; LDL_rcpt_classA_cys-rich; 29.
DR   PROSITE; PS00010; ASX_HYDROXYL; 3.
DR   PROSITE; PS00022; EGF_1; 5.
DR   PROSITE; PS01186; EGF_2; 8.
DR   PROSITE; PS50026; EGF_3; 6.
DR   PROSITE; PS01187; EGF_CA; 2.
DR   PROSITE; PS01209; LDLRA_1; 27.
DR   PROSITE; PS50068; LDLRA_2; 31.
DR   PROSITE; PS51120; LDLRB; 34.
PE   1: Evidence at protein level;
KW   Calcium; Cell membrane; Coated pit; Cytoplasm; Developmental protein;
KW   Disulfide bond; EGF-like domain; Endocytosis; Glycoprotein; Membrane;
KW   Metal-binding; Nucleus; Phosphoprotein; Receptor; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     19       Potential.
FT   CHAIN        20   4545       Prolow-density lipoprotein receptor-
FT                                related protein 1.
FT                                /FTId=PRO_0000273273.
FT   CHAIN        20  ?3944       Low-density lipoprotein receptor-related
FT                                protein 1 515 kDa subunit.
FT                                /FTId=PRO_0000302753.
FT   CHAIN     ?3945   4545       Low-density lipoprotein receptor-related
FT                                protein 1 85 kDa subunit.
FT                                /FTId=PRO_0000302754.
FT   CHAIN     ?4442   4545       Low-density lipoprotein receptor-related
FT                                protein 1 intracellular domain.
FT                                /FTId=PRO_0000302755.
FT   TOPO_DOM     20   4424       Extracellular (Potential).
FT   TRANSMEM   4425   4445       Helical; (Potential).
FT   TOPO_DOM   4446   4545       Cytoplasmic (Potential).
FT   DOMAIN       26     67       LDL-receptor class A 1.
FT   DOMAIN       71    111       LDL-receptor class A 2.
FT   DOMAIN      112    150       EGF-like 1.
FT   DOMAIN      151    190       EGF-like 2; calcium-binding (Potential).
FT   REPEAT      293    335       LDL-receptor class B 1.
FT   REPEAT      336    379       LDL-receptor class B 2.
FT   REPEAT      380    423       LDL-receptor class B 3.
FT   DOMAIN      475    521       EGF-like 3.
FT   REPEAT      572    614       LDL-receptor class B 4.
FT   REPEAT      615    660       LDL-receptor class B 5.
FT   REPEAT      661    711       LDL-receptor class B 6.
FT   REPEAT      712    755       LDL-receptor class B 7.
FT   DOMAIN      804    844       EGF-like 4.
FT   DOMAIN      853    893       LDL-receptor class A 3.
FT   DOMAIN      894    934       LDL-receptor class A 4.
FT   DOMAIN      935    974       LDL-receptor class A 5.
FT   DOMAIN      975   1014       LDL-receptor class A 6.
FT   DOMAIN     1014   1054       LDL-receptor class A 7.
FT   DOMAIN     1061   1100       LDL-receptor class A 8.
FT   DOMAIN     1103   1143       LDL-receptor class A 9.
FT   DOMAIN     1144   1183       LDL-receptor class A 10.
FT   DOMAIN     1184   1223       EGF-like 5.
FT   DOMAIN     1224   1263       EGF-like 6.
FT   REPEAT     1310   1356       LDL-receptor class B 8.
FT   REPEAT     1357   1399       LDL-receptor class B 9.
FT   REPEAT     1400   1446       LDL-receptor class B 10.
FT   REPEAT     1447   1491       LDL-receptor class B 11.
FT   REPEAT     1492   1532       LDL-receptor class B 12.
FT   DOMAIN     1537   1580       EGF-like 7.
FT   REPEAT     1628   1670       LDL-receptor class B 13.
FT   REPEAT     1671   1714       LDL-receptor class B 14.
FT   REPEAT     1715   1754       LDL-receptor class B 15.
FT   REPEAT     1755   1799       LDL-receptor class B 16.
FT   DOMAIN     1847   1888       EGF-like 8.
FT   REPEAT     1935   1977       LDL-receptor class B 17.
FT   REPEAT     1978   2020       LDL-receptor class B 18.
FT   REPEAT     2021   2064       LDL-receptor class B 19.
FT   REPEAT     2065   2108       LDL-receptor class B 20.
FT   DOMAIN     2156   2196       EGF-like 9.
FT   REPEAT     2254   2295       LDL-receptor class B 21.
FT   REPEAT     2296   2344       LDL-receptor class B 22.
FT   REPEAT     2345   2389       LDL-receptor class B 23.
FT   REPEAT     2390   2432       LDL-receptor class B 24.
FT   REPEAT     2433   2474       LDL-receptor class B 25.
FT   DOMAIN     2479   2519       EGF-like 10.
FT   DOMAIN     2523   2564       LDL-receptor class A 11.
FT   DOMAIN     2565   2603       LDL-receptor class A 12.
FT   DOMAIN     2604   2642       LDL-receptor class A 13.
FT   DOMAIN     2643   2691       LDL-receptor class A 14.
FT   DOMAIN     2695   2733       LDL-receptor class A 15.
FT   DOMAIN     2733   2772       LDL-receptor class A 16.
FT   DOMAIN     2773   2815       LDL-receptor class A 17.
FT   DOMAIN     2817   2856       LDL-receptor class A 18.
FT   DOMAIN     2857   2900       LDL-receptor class A 19.
FT   DOMAIN     2903   2941       LDL-receptor class A 20.
FT   DOMAIN     2942   2982       EGF-like 11.
FT   DOMAIN     2983   3023       EGF-like 12; calcium-binding (Potential).
FT   REPEAT     3070   3114       LDL-receptor class B 26.
FT   REPEAT     3115   3157       LDL-receptor class B 27.
FT   REPEAT     3158   3201       LDL-receptor class B 28.
FT   REPEAT     3202   3244       LDL-receptor class B 29.
FT   REPEAT     3245   3285       LDL-receptor class B 30.
FT   DOMAIN     3291   3332       EGF-like 13.
FT   DOMAIN     3333   3372       LDL-receptor class A 21.
FT   DOMAIN     3373   3411       LDL-receptor class A 22.
FT   DOMAIN     3412   3451       LDL-receptor class A 23.
FT   DOMAIN     3452   3492       LDL-receptor class A 24.
FT   DOMAIN     3493   3534       LDL-receptor class A 25.
FT   DOMAIN     3535   3573       LDL-receptor class A 26.
FT   DOMAIN     3574   3612       LDL-receptor class A 27.
FT   DOMAIN     3612   3650       LDL-receptor class A 28.
FT   DOMAIN     3653   3693       LDL-receptor class A 29.
FT   DOMAIN     3694   3734       LDL-receptor class A 30.
FT   DOMAIN     3740   3779       LDL-receptor class A 31.
FT   DOMAIN     3782   3824       EGF-like 14.
FT   DOMAIN     3825   3862       EGF-like 15.
FT   REPEAT     3913   3955       LDL-receptor class B 31.
FT   REPEAT     3971   4013       LDL-receptor class B 32.
FT   REPEAT     4014   4057       LDL-receptor class B 33.
FT   REPEAT     4058   4102       LDL-receptor class B 34.
FT   DOMAIN     4148   4184       EGF-like 16.
FT   DOMAIN     4197   4233       EGF-like 17.
FT   DOMAIN     4233   4269       EGF-like 18.
FT   DOMAIN     4269   4305       EGF-like 19.
FT   DOMAIN     4305   4341       EGF-like 20.
FT   DOMAIN     4341   4376       EGF-like 21.
FT   DOMAIN     4374   4410       EGF-like 22.
FT   REGION     4446   4545       Interaction with MAFB.
FT   MOTIF      3941   3944       Recognition site for proteolytical
FT                                processing (Potential).
FT   MOTIF      4503   4508       Endocytosis signal (Potential).
FT   METAL       872    872       Calcium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       875    875       Calcium 1 (By similarity).
FT   METAL       877    877       Calcium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       879    879       Calcium 1 (By similarity).
FT   METAL       885    885       Calcium 1 (By similarity).
FT   METAL       886    886       Calcium 1 (By similarity).
FT   METAL      1033   1033       Calcium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL      1036   1036       Calcium 2 (By similarity).
FT   METAL      1038   1038       Calcium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL      1040   1040       Calcium 2 (By similarity).
FT   METAL      1046   1046       Calcium 2 (By similarity).
FT   METAL      1047   1047       Calcium 2 (By similarity).
FT   METAL      1081   1081       Calcium 3; via carbonyl oxygen (By
FT                                similarity).
FT   METAL      1084   1084       Calcium 3 (By similarity).
FT   METAL      1086   1086       Calcium 3; via carbonyl oxygen (By
FT                                similarity).
FT   METAL      1088   1088       Calcium 3 (By similarity).
FT   METAL      1094   1094       Calcium 3 (By similarity).
FT   METAL      1095   1095       Calcium 3 (By similarity).
FT   MOD_RES    4461   4461       Phosphothreonine (By similarity).
FT   MOD_RES    4508   4508       Phosphotyrosine (By similarity).
FT   MOD_RES    4518   4518       Phosphoserine (By similarity).
FT   MOD_RES    4521   4521       Phosphoserine.
FT   MOD_RES    4524   4524       Phosphoserine.
FT   MOD_RES    4525   4525       Phosphothreonine.
FT   CARBOHYD    115    115       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    137    137       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    186    186       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    240    240       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    275    275       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    358    358       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    447    447       N-linked (GlcNAc...).
FT   CARBOHYD    730    730       N-linked (GlcNAc...).
FT   CARBOHYD    929    929       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1051   1051       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1155   1155       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1156   1156       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1196   1196       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1219   1219       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1512   1512       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1559   1559       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1576   1576       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1617   1617       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1646   1646       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1724   1724       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1734   1734       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1764   1764       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1826   1826       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1934   1934       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1996   1996       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2049   2049       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2118   2118       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2128   2128       N-linked (GlcNAc...).
FT   CARBOHYD   2473   2473       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2503   2503       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2522   2522       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2602   2602       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2621   2621       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2639   2639       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2816   2816       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2906   2906       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3049   3049       N-linked (GlcNAc...).
FT   CARBOHYD   3090   3090       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3265   3265       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3334   3334       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3489   3489       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3663   3663       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3789   3789       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3840   3840       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3954   3954       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   4076   4076       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   4126   4126       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   4180   4180       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   4279   4279       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   4280   4280       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   4365   4365       N-linked (GlcNAc...) (Potential).
FT   DISULFID     28     41       By similarity.
FT   DISULFID     35     54       By similarity.
FT   DISULFID     48     65       By similarity.
FT   DISULFID     73     86       By similarity.
FT   DISULFID     80     99       By similarity.
FT   DISULFID     93    109       By similarity.
FT   DISULFID    116    125       By similarity.
FT   DISULFID    121    134       By similarity.
FT   DISULFID    136    149       By similarity.
FT   DISULFID    155    165       By similarity.
FT   DISULFID    161    174       By similarity.
FT   DISULFID    176    189       By similarity.
FT   DISULFID    479    494       By similarity.
FT   DISULFID    490    505       By similarity.
FT   DISULFID    507    520       By similarity.
FT   DISULFID    808    819       By similarity.
FT   DISULFID    815    828       By similarity.
FT   DISULFID    830    843       By similarity.
FT   DISULFID    855    867       By similarity.
FT   DISULFID    862    880       By similarity.
FT   DISULFID    874    891       By similarity.
FT   DISULFID    896    908       By similarity.
FT   DISULFID    903    921       By similarity.
FT   DISULFID    915    932       By similarity.
FT   DISULFID    937    949       By similarity.
FT   DISULFID    944    962       By similarity.
FT   DISULFID    956    972       By similarity.
FT   DISULFID    977    990       By similarity.
FT   DISULFID    985   1003       By similarity.
FT   DISULFID    997   1012       By similarity.
FT   DISULFID   1016   1028       By similarity.
FT   DISULFID   1023   1041       By similarity.
FT   DISULFID   1035   1052       By similarity.
FT   DISULFID   1063   1076       By similarity.
FT   DISULFID   1070   1089       By similarity.
FT   DISULFID   1083   1098       By similarity.
FT   DISULFID   1105   1119       By similarity.
FT   DISULFID   1113   1132       By similarity.
FT   DISULFID   1126   1141       By similarity.
FT   DISULFID   1146   1160       By similarity.
FT   DISULFID   1153   1173       By similarity.
FT   DISULFID   1167   1183       By similarity.
FT   DISULFID   1186   1197       By similarity.
FT   DISULFID   1193   1207       By similarity.
FT   DISULFID   1209   1222       By similarity.
FT   DISULFID   1228   1238       By similarity.
FT   DISULFID   1234   1247       By similarity.
FT   DISULFID   1249   1262       By similarity.
FT   DISULFID   1541   1554       By similarity.
FT   DISULFID   1550   1564       By similarity.
FT   DISULFID   1566   1579       By similarity.
FT   DISULFID   1851   1862       By similarity.
FT   DISULFID   1858   1872       By similarity.
FT   DISULFID   1874   1887       By similarity.
FT   DISULFID   2160   2171       By similarity.
FT   DISULFID   2167   2181       By similarity.
FT   DISULFID   2183   2195       By similarity.
FT   DISULFID   2483   2494       By similarity.
FT   DISULFID   2490   2504       By similarity.
FT   DISULFID   2506   2518       By similarity.
FT   DISULFID   2525   2538       By similarity.
FT   DISULFID   2533   2551       By similarity.
FT   DISULFID   2545   2562       By similarity.
FT   DISULFID   2567   2579       By similarity.
FT   DISULFID   2574   2592       By similarity.
FT   DISULFID   2586   2601       By similarity.
FT   DISULFID   2606   2618       By similarity.
FT   DISULFID   2613   2631       By similarity.
FT   DISULFID   2625   2640       By similarity.
FT   DISULFID   2645   2667       By similarity.
FT   DISULFID   2661   2680       By similarity.
FT   DISULFID   2674   2689       By similarity.
FT   DISULFID   2697   2709       By similarity.
FT   DISULFID   2704   2722       By similarity.
FT   DISULFID   2716   2731       By similarity.
FT   DISULFID   2735   2747       By similarity.
FT   DISULFID   2742   2760       By similarity.
FT   DISULFID   2754   2770       By similarity.
FT   DISULFID   2775   2788       By similarity.
FT   DISULFID   2782   2801       By similarity.
FT   DISULFID   2795   2813       By similarity.
FT   DISULFID   2819   2831       By similarity.
FT   DISULFID   2826   2844       By similarity.
FT   DISULFID   2838   2854       By similarity.
FT   DISULFID   2859   2871       By similarity.
FT   DISULFID   2866   2885       By similarity.
FT   DISULFID   2879   2898       By similarity.
FT   DISULFID   2905   2918       By similarity.
FT   DISULFID   2913   2931       By similarity.
FT   DISULFID   2925   2940       By similarity.
FT   DISULFID   2945   2957       By similarity.
FT   DISULFID   2953   2966       By similarity.
FT   DISULFID   2968   2981       By similarity.
FT   DISULFID   2987   2997       By similarity.
FT   DISULFID   2993   3006       By similarity.
FT   DISULFID   3008   3022       By similarity.
FT   DISULFID   3295   3306       By similarity.
FT   DISULFID   3302   3316       By similarity.
FT   DISULFID   3318   3331       By similarity.
FT   DISULFID   3335   3347       By similarity.
FT   DISULFID   3342   3360       By similarity.
FT   DISULFID   3354   3370       By similarity.
FT   DISULFID   3375   3387       By similarity.
FT   DISULFID   3382   3400       By similarity.
FT   DISULFID   3394   3409       By similarity.
FT   DISULFID   3414   3427       By similarity.
FT   DISULFID   3421   3440       By similarity.
FT   DISULFID   3434   3449       By similarity.
FT   DISULFID   3454   3467       By similarity.
FT   DISULFID   3461   3480       By similarity.
FT   DISULFID   3474   3490       By similarity.
FT   DISULFID   3495   3508       By similarity.
FT   DISULFID   3502   3521       By similarity.
FT   DISULFID   3515   3532       By similarity.
FT   DISULFID   3537   3549       By similarity.
FT   DISULFID   3544   3562       By similarity.
FT   DISULFID   3556   3571       By similarity.
FT   DISULFID   3576   3588       By similarity.
FT   DISULFID   3583   3601       By similarity.
FT   DISULFID   3595   3610       By similarity.
FT   DISULFID   3614   3626       By similarity.
FT   DISULFID   3621   3639       By similarity.
FT   DISULFID   3633   3648       By similarity.
FT   DISULFID   3655   3667       By similarity.
FT   DISULFID   3662   3680       By similarity.
FT   DISULFID   3674   3691       By similarity.
FT   DISULFID   3696   3710       By similarity.
FT   DISULFID   3704   3723       By similarity.
FT   DISULFID   3717   3732       By similarity.
FT   DISULFID   3742   3755       By similarity.
FT   DISULFID   3750   3768       By similarity.
FT   DISULFID   3762   3777       By similarity.
FT   DISULFID   3786   3799       By similarity.
FT   DISULFID   3793   3808       By similarity.
FT   DISULFID   3810   3823       By similarity.
FT   DISULFID   3829   3839       By similarity.
FT   DISULFID   3835   3848       By similarity.
FT   DISULFID   3850   3861       By similarity.
FT   DISULFID   4152   4161       By similarity.
FT   DISULFID   4157   4170       By similarity.
FT   DISULFID   4172   4183       By similarity.
FT   DISULFID   4201   4211       By similarity.
FT   DISULFID   4205   4221       By similarity.
FT   DISULFID   4223   4232       By similarity.
FT   DISULFID   4237   4247       By similarity.
FT   DISULFID   4241   4257       By similarity.
FT   DISULFID   4259   4268       By similarity.
FT   DISULFID   4273   4283       By similarity.
FT   DISULFID   4277   4293       By similarity.
FT   DISULFID   4295   4304       By similarity.
FT   DISULFID   4309   4319       By similarity.
FT   DISULFID   4313   4329       By similarity.
FT   DISULFID   4331   4340       By similarity.
FT   DISULFID   4345   4353       By similarity.
FT   DISULFID   4348   4364       By similarity.
FT   DISULFID   4366   4375       By similarity.
FT   DISULFID   4378   4388       By similarity.
FT   DISULFID   4382   4398       By similarity.
FT   DISULFID   4400   4409       By similarity.
FT   CONFLICT   2642   2642       A -> T (in Ref. 2; AAL09567).
SQ   SEQUENCE   4545 AA;  504742 MW;  9904CF5DF5EE333E CRC64;
     MLTPPLLLLL PLLSALVSGA TMDAPKTCSP KQFACRDQIT CISKGWRCDG ERDCPDGSDE
     APEICPQSKA QRCPPNEHSC LGTELCVPMS RLCNGIQDCM DGSDEGAHCR ELRANCSRMG
     CQHHCVPTPS GPTCYCNSSF QLQADGKTCK DFDECSVYGT CSQLCTNTDG SFTCGCVEGY
     LLQPDNRSCK AKNEPVDRPP VLLIANSQNI LATYLSGAQV STITPTSTRQ TTAMDFSYAN
     ETVCWVHVGD SAAQTQLKCA RMPGLKGFVD EHTINISLSL HHVEQMAIDW LTGNFYFVDD
     IDDRIFVCNR NGDTCVTLLD LELYNPKGIA LDPAMGKVFF TDYGQIPKVE RCDMDGQNRT
     KLVDSKIVFP HGITLDLVSR LVYWADAYLD YIEVVDYEGK GRQTIIQGIL IEHLYGLTVF
     ENYLYATNSD NANTQQKTSV IRVNRFNSTE YQVVTRVDKG GALHIYHQRR QPRVRSHACE
     NDQYGKPGGC SDICLLANSH KARTCRCRSG FSLGSDGKSC KKPEHELFLV YGKGRPGIIR
     GMDMGAKVPD EHMIPIENLM NPRALDFHAE TGFIYFADTT SYLIGRQKID GTERETILKD
     GIHNVEGVAV DWMGDNLYWT DDGPKKTISV ARLEKAAQTR KTLIEGKMTH PRAIVVDPLN
     GWMYWTDWEE DPKDSRRGRL ERAWMDGSHR DIFVTSKTVL WPNGLSLDIP AGRLYWVDAF
     YDRIETILLN GTDRKIVYEG PELNHAFGLC HHGNYLFWTE YRSGSVYRLE RGVAGAPPTV
     TLLRSERPPI FEIRMYDAQQ QQVGTNKCRV NNGGCSSLCL ATPGSRQCAC AEDQVLDTDG
     VTCLANPSYV PPPQCQPGEF ACANNRCIQE RWKCDGDNDC LDNSDEAPAL CHQHTCPSDR
     FKCENNRCIP NRWLCDGDND CGNSEDESNA TCSARTCPPN QFSCASGRCI PISWTCDLDD
     DCGDRSDESA SCAYPTCFPL TQFTCNNGRC ININWRCDND NDCGDNSDEA GCSHSCSSTQ
     FKCNSGRCIP EHWTCDGDND CGDYSDETHA NCTNQATRPP GGCHSDEFQC RLDGLCIPLR
     WRCDGDTDCM DSSDEKSCEG VTHVCDPNVK FGCKDSARCI SKAWVCDGDS DCEDNSDEEN
     CEALACRPPS HPCANNTSVC LPPDKLCDGK DDCGDGSDEG ELCDQCSLNN GGCSHNCSVA
     PGEGIVCSCP LGMELGSDNH TCQIQSYCAK HLKCSQKCDQ NKFSVKCSCY EGWVLEPDGE
     SCRSLDPFKP FIIFSNRHEI RRIDLHKGDY SVLVPGLRNT IALDFHLSQS ALYWTDVVED
     KIYRGKLLDN GALTSFEVVI QYGLATPEGL AVDWIAGNIY WVESNLDQIE VAKLDGTLRT
     TLLAGDIEHP RAIALDPRDG ILFWTDWDAS LPRIEAASMS GAGRRTIHRE TGSGGWPNGL
     TVDYLEKRIL WIDARSDAIY SARYDGSGHM EVLRGHEFLS HPFAVTLYGG EVYWTDWRTN
     TLAKANKWTG HNVTVVQRTN TQPFDLQVYH PSRQPMAPNP CEANGGRGPC SHLCLINYNR
     TVSCACPHLM KLHKDNTTCY EFKKFLLYAR QMEIRGVDLD APYYNYIISF TVPDIDNVTV
     LDYDAREQRV YWSDVRTQAI KRAFINGTGV ETVVSADLPN AHGLAVDWVS RNLFWTSYDT
     NKKQINVARL DGSFKNAVVQ GLEQPHGLVV HPLRGKLYWT DGDNISMANM DGSNHTLLFS
     GQKGPVGLAI DFPESKLYWI SSGNHTINRC NLDGSELEVI DTMRSQLGKA TALAIMGDKL
     WWADQVSEKM GTCNKADGSG SVVLRNSTTL VMHMKVYDES IQLEHEGTNP CSVNNGDCSQ
     LCLPTSETTR SCMCTAGYSL RSGQQACEGV GSFLLYSVHE GIRGIPLDPN DKSDALVPVS
     GTSLAVGIDF HAENDTIYWV DMGLSTISRA KRDQTWREDV VTNGIGRVEG IAVDWIAGNI
     YWTDQGFDVI EVARLNGSFR YVVISQGLDK PRAITVHPEK GYLFWTEWGH YPRIERSRLD
     GTERVVLVNV SISWPNGISV DYQGGKLYWC DARMDKIERI DLETGENREV VLSSNNMDMF
     SVSVFEDFIY WSDRTHANGS IKRGCKDNAT DSVPLRTGIG VQLKDIKVFN RDRQKGTNVC
     AVANGGCQQL CLYRGGGQRA CACAHGMLAE DGASCREYAG YLLYSERTIL KSIHLSDERN
     LNAPVQPFED PEHMKNVIAL AFDYRAGTSP GTPNRIFFSD IHFGNIQQIN DDGSGRTTIV
     ENVGSVEGLA YHRGWDTLYW TSYTTSTITR HTVDQTRPGA FERETVITMS GDDHPRAFVL
     DECQNLMFWT NWNELHPSIM RAALSGANVL TLIEKDIRTP NGLAIDHRAE KLYFSDATLD
     KIERCEYDGS HRYVILKSEP VHPFGLAVYG EHIFWTDWVR RAVQRANKYV GSDMKLLRVD
     IPQQPMGIIA VANDTNSCEL SPCRINNGGC QDLCLLTHQG HVNCSCRGGR ILQEDFTCRA
     VNSSCRAQDE FECANGECIS FSLTCDGVSH CKDKSDEKPS YCNSRRCKKT FRQCNNGRCV
     SNMLWCNGVD DCGDGSDEIP CNKTACGVGE FRCRDGSCIG NSSRCNQFVD CEDASDEMNC
     SATDCSSYFR LGVKGVLFQP CERTSLCYAP SWVCDGANDC GDYSDERDCP GVKRPRCPLN
     YFACPSGRCI PMSWTCDKED DCENGEDETH CNKFCSEAQF ECQNHRCISK QWLCDGSDDC
     GDGSDEAAHC EGKTCGPSSF SCPGTHVCVP ERWLCDGDKD CTDGADESVT AGCLYNSTCD
     DREFMCQNRL CIPKHFVCDH DRDCADGSDE SPECEYPTCG PNEFRCANGR CLSSRQWECD
     GENDCHDHSD EAPKNPHCTS PEHKCNASSQ FLCSSGRCVA EALLCNGQDD CGDGSDERGC
     HVNECLSRKL SGCSQDCEDL KIGFKCRCRP GFRLKDDGRT CADLDECSTT FPCSQLCINT
     HGSYKCLCVE GYAPRGGDPH SCKAVTDEEP FLIFANRYYL RKLNLDGSNY TLLKQGLNNA
     VALDFDYREQ MIYWTDVTTQ GSMIRRMHLN GSNVQVLHRT GLSNPDGLAV DWVGGNLYWC
     DKGRDTIEVS KLNGAYRTVL VSSGLREPRA LVVDVQNGYL YWTDWGDHSL IGRIGMDGSG
     RSIIVDTKIT WPNGLTVDYV TERIYWADAR EDYIEFASLD GSNRHVVLSQ DIPHIFALTL
     FEDYVYWTDW ETKSINRAHK TTGANKTLLI STLHRPMDLH VFHALRQPDV PNHPCKVNNG
     GCSNLCLLSP GGGHKCACPT NFYLGGDGRT CVSNCTASQF VCKNDKCIPF WWKCDTEDDC
     GDHSDEPPDC PEFKCRPGQF QCSTGICTNP AFICDGDNDC QDNSDEANCD IHVCLPSQFK
     CTNTNRCIPG IFRCNGQDNC GDGEDERDCP EVTCAPNQFQ CSITKRCIPR VWVCDRDNDC
     VDGSDEPANC TQMTCGVDEF RCKDSGRCIP ARWKCDGEDD CGDGSDEPKE ECDERTCEPY
     QFRCKNNRCV PGRWQCDYDN DCGDNSDEES CTPRPCSESE FSCANGRCIA GRWKCDGDHD
     CADGSDEKDC TPRCDMDQFQ CKSGHCIPLR WRCDADADCM DGSDEEACGT GVRTCPLDEF
     QCNNTLCKPL AWKCDGEDDC GDNSDENPEE CARFICPPNR PFRCKNDRVC LWIGRQCDGV
     DNCGDGTDEE DCEPPTAQNP HCKDKKEFLC RNQRCLSSSL RCNMFDDCGD GSDEEDCSID
     PKLTSCATNA SMCGDEARCV RTEKAAYCAC RSGFHTVPGQ PGCQDINECL RFGTCSQLCN
     NTKGGHLCSC ARNFMKTHNT CKAEGSEYQV LYIADDNEIR SLFPGHPHSA YEQTFQGDES
     VRIDAMDVHV KAGRVYWTNW HTGTISYRSL PPAAPPTTSN RHRRQIDRGV THLNISGLKM
     PRGIAIDWVA GNVYWTDSGR DVIEVAQMKG ENRKTLISGM IDEPHAIVVD PLRGTMYWSD
     WGNHPKIETA AMDGTLRETL VQDNIQWPTG LAVDYHNERL YWADAKLSVI GSIRLNGTDP
     IVAADSKRGL SHPFSIDVFE DYIYGVTYIN NRVFKIHKFG HSPLINLTGG LSHASDVVLY
     HQHKQPEVTN PCDRKKCEWL CLLSPSGPVC TCPNGKRLDN GTCVPVPSPT PPPDAPRPGT
     CTLQCFNGGS CFLNARRQPK CRCQPRYTGD KCELDQCWEY CHNGGTCAAS PSGMPTCRCP
     TGFTGPKCTA QVCAGYCSNN STCTVNQGNQ PQCRCLPGFL GDRCQYRQCS GFCENFGTCQ
     MAADGSRQCR CTVYFEGPRC EVNKCSRCLQ GACVVNKQTG DVTCNCTDGR VAPSCLTCID
     HCSNGGSCTM NSKMMPECQC PPHMTGPRCE EQVVSQQQPG HMASILIPLL LLLLLLLVAG
     VVFWYKRRVR GAKGFQHQRM TNGAMNVEIG NPTYKMYEGG EPDDVGGLLD ADFALDPDKP
     TNFTNPVYAT LYMGGHGSRH SLASTDEKRE LLGRGPEDEI GDPLA
//
ID   SYUB_MOUSE              Reviewed;         133 AA.
AC   Q91ZZ3;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Beta-synuclein;
GN   Name=Sncb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=21367613; PubMed=11474193;
RA   Sopher B.L., Koszdin K.L., McClain M.E., Myrick S.B., Martinez R.A.,
RA   Smith A.C., La Spada A.R.;
RT   "Genomic organization, chromosome location, and expression analysis of
RT   mouse beta-synuclein, a candidate for involvement in
RT   neurodegeneration.";
RL   Cytogenet. Cell Genet. 93:117-123(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 60-84, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
CC   -!- FUNCTION: May be involved in neuronal plasticity (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in the brain.
CC   -!- PTM: Phosphorylated. Phosphorylation by G-protein coupled receptor
CC       kinases (GRK) is more efficient than phosphorylation by CK1, CK2
CC       and CaM-kinase II (By similarity).
CC   -!- SIMILARITY: Belongs to the synuclein family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF348164; AAK83238.1; -; Genomic_DNA.
DR   EMBL; AF348162; AAK83238.1; JOINED; Genomic_DNA.
DR   EMBL; AF348163; AAK83238.1; JOINED; Genomic_DNA.
DR   EMBL; BC019409; AAH19409.1; -; mRNA.
DR   IPI; IPI00131614; -.
DR   RefSeq; NP_291088.1; NM_033610.2.
DR   UniGene; Mm.200843; -.
DR   HSSP; P37840; 1XQ8.
DR   ProteinModelPortal; Q91ZZ3; -.
DR   SMR; Q91ZZ3; 1-133.
DR   STRING; Q91ZZ3; -.
DR   PhosphoSite; Q91ZZ3; -.
DR   UCD-2DPAGE; Q91ZZ3; -.
DR   PRIDE; Q91ZZ3; -.
DR   Ensembl; ENSMUST00000036825; ENSMUSP00000043074; ENSMUSG00000034891.
DR   GeneID; 104069; -.
DR   KEGG; mmu:104069; -.
DR   UCSC; uc007qpc.1; mouse.
DR   CTD; 104069; -.
DR   MGI; MGI:1889011; Sncb.
DR   eggNOG; roNOG18011; -.
DR   GeneTree; ENSGT00390000016161; -.
DR   HOGENOM; HBG715579; -.
DR   HOVERGEN; HBG000481; -.
DR   InParanoid; Q91ZZ3; -.
DR   OMA; DSPQEEY; -.
DR   OrthoDB; EOG40S0HC; -.
DR   NextBio; 356459; -.
DR   ArrayExpress; Q91ZZ3; -.
DR   Bgee; Q91ZZ3; -.
DR   CleanEx; MM_SNCB; -.
DR   Genevestigator; Q91ZZ3; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
DR   GO; GO:0042417; P:dopamine metabolic process; IGI:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptosis; IGI:MGI.
DR   InterPro; IPR001058; Synuclein.
DR   InterPro; IPR002461; Synuclein_beta.
DR   Gene3D; G3DSA:1.10.287.700; Synuclein; 1.
DR   PANTHER; PTHR13820; Synuclein; 1.
DR   PANTHER; PTHR13820:SF4; Synuclein_beta; 1.
DR   Pfam; PF01387; Synuclein; 1.
DR   PRINTS; PR01213; BSYNUCLEIN.
DR   PRINTS; PR01211; SYNUCLEIN.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Phosphoprotein; Repeat.
FT   CHAIN         1    133       Beta-synuclein.
FT                                /FTId=PRO_0000286176.
FT   REPEAT       20     30       1.
FT   REPEAT       31     41       2.
FT   REPEAT       42     55       3; approximate.
FT   REPEAT       56     66       4.
FT   REGION       20     66       4 X 11 AA tandem repeats of [EGS]-K-T-K-
FT                                [EQ]-[GQ]-V-X(4).
FT   MOD_RES     117    117       Phosphoserine; by BARK1, CK2 and GRK5 (By
FT                                similarity).
SQ   SEQUENCE   133 AA;  14052 MW;  8274D8A6A0D8E4D5 CRC64;
     MDVFMKGLSM AKEGVVAAAE KTKQGVTEAA EKTKEGVLYV GSKTSGVVQG VASVAEKTKE
     QASHLGGAVF SGAGNIAAAT GLVKKEEFPT DLKPEEVAQE AAEEPLIEPL MEPEGESYED
     SPQEEYQEYE PEA
//
ID   FRM4B_MOUSE             Reviewed;         981 AA.
AC   Q920B0; Q3V1S1; Q9ESP9;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=FERM domain-containing protein 4B;
DE   AltName: Full=GRP1-binding protein GRSP1;
DE   AltName: Full=Golgi-associated band 4.1-like protein;
DE            Short=GOBLIN;
GN   Name=Frmd4b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, ALTERNATIVE
RP   SPLICING, AND INTERACTION WITH GRP1.
RC   TISSUE=Brain, and Lung;
RX   PubMed=11445584; DOI=10.1074/jbc.M105260200;
RA   Klarlund J.K., Holik J., Chawla A., Park J.G., Buxton J., Czech M.P.;
RT   "Signaling complexes of the FERM domain-containing protein GRSP1 bound
RT   to ARF exchange factor GRP1.";
RL   J. Biol. Chem. 276:40065-40070(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Brain;
RA   Watanabe N.M., Kusumi A., Dan I.;
RT   "Mus musculus mRNA for Golgi-associated band 4.1-like protein, Goblin,
RT   complete cds.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-621 AND SER-644, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Member of GRP1 signaling complexes that are acutely
CC       recruited to plasma membrane ruffles in response to insulin
CC       receptor signaling. May function as a scaffolding protein.
CC   -!- SUBUNIT: Interacts with GRP1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=Additional isoforms seem to exist. A longer isoform
CC         which differs in the N-terminus is expressed in the brain;
CC       Name=1;
CC         IsoId=Q920B0-1; Sequence=Displayed;
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF327857; AAL26917.1; -; mRNA.
DR   EMBL; AB042027; BAB17031.1; -; mRNA.
DR   EMBL; AK132280; BAE21079.1; -; mRNA.
DR   EMBL; BC052390; AAH52390.1; -; mRNA.
DR   IPI; IPI00319524; -.
DR   RefSeq; NP_660130.2; NM_145148.2.
DR   UniGene; Mm.27789; -.
DR   ProteinModelPortal; Q920B0; -.
DR   SMR; Q920B0; 4-312.
DR   STRING; Q920B0; -.
DR   PhosphoSite; Q920B0; -.
DR   PRIDE; Q920B0; -.
DR   Ensembl; ENSMUST00000032146; ENSMUSP00000032146; ENSMUSG00000030064.
DR   Ensembl; ENSMUST00000113355; ENSMUSP00000108982; ENSMUSG00000030064.
DR   Ensembl; ENSMUST00000113359; ENSMUSP00000108986; ENSMUSG00000030064.
DR   GeneID; 232288; -.
DR   KEGG; mmu:232288; -.
DR   UCSC; uc009dau.1; mouse.
DR   CTD; 232288; -.
DR   MGI; MGI:2141794; Frmd4b.
DR   eggNOG; roNOG05924; -.
DR   GeneTree; ENSGT00560000077123; -.
DR   HOVERGEN; HBG062800; -.
DR   InParanoid; Q920B0; -.
DR   OrthoDB; EOG4CC40P; -.
DR   NextBio; 381022; -.
DR   ArrayExpress; Q920B0; -.
DR   Bgee; Q920B0; -.
DR   CleanEx; MM_FRMD4B; -.
DR   Genevestigator; Q920B0; -.
DR   GermOnline; ENSMUSG00000030064; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0001726; C:ruffle; IPI:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR021774; DUF3338.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH_type.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF11819; DUF3338; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   PRINTS; PR00935; BAND41.
DR   SMART; SM00295; B41; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Phosphoprotein.
FT   CHAIN         1    981       FERM domain-containing protein 4B.
FT                                /FTId=PRO_0000219447.
FT   DOMAIN        5    307       FERM.
FT   COILED      360    397       Potential.
FT   COILED      481    505       Potential.
FT   MOD_RES     551    551       Phosphoserine (By similarity).
FT   MOD_RES     555    555       Phosphoserine (By similarity).
FT   MOD_RES     575    575       Phosphoserine (By similarity).
FT   MOD_RES     609    609       Phosphoserine (By similarity).
FT   MOD_RES     613    613       Phosphothreonine (By similarity).
FT   MOD_RES     621    621       Phosphotyrosine.
FT   MOD_RES     644    644       Phosphoserine.
FT   MOD_RES     862    862       Phosphoserine (By similarity).
FT   CONFLICT      8      8       Q -> R (in Ref. 2; BAB17031).
FT   CONFLICT    170    170       D -> G (in Ref. 3; BAE21079).
FT   CONFLICT    748    748       P -> S (in Ref. 2; BAB17031).
FT   CONFLICT    863    864       PQ -> TK (in Ref. 2; BAB17031).
FT   CONFLICT    932    932       S -> N (in Ref. 2; BAB17031).
SQ   SEQUENCE   981 AA;  111566 MW;  E8332CB283CF829A CRC64;
     MTEGRHCQVH LLDDRRLELL VQPKLLSREL LDLVASHFNL KEKEYFGITF IDDTGQENWL
     QLDHRVLEHD LPKKPGPTLL HFAVRFYIES ISFLKDKNTV ELFFLNAKAC VHKGQIEVDS
     ETIFKLAALV LQESKGDYTS DENARKDLKT LPVFPTKTLQ EHPSLAYCED RVIEHYLKIK
     GLTRGQAVVQ YMKIVEALPT YGVHYYAVKD KQGLPWWLGI SYKGIGQYDL QDKVKPRKLF
     QWKQLENLYF REKKFAVEVH DPRRISVSRR TFGQSGLFVQ TWYANSSLIK SIWVMAISQH
     QFYLDRKQSK AKIPSARSLD DIAMDLTETG TQRGSKLVTL EAKSQFIMAS NGSLISSGSQ
     DSEGMEEQKR EKILELKKKE KLLQEKLLQK VEELKKICLR EAELTGRMPK EYPLNIGEKP
     PQVRRRVGTT FKLDDNLLPT EEDPALQELE SNFLIQQKLV EAAKKLASEP DLCKTVKKKR
     KQDYTDAVKR LQEIENSINE YRIRCGKKPS QKAAVVPPED IIPSESSSLS DTTTYDDPND
     SFTLAGQRPS SVPHSPRILP PKSLGIERIH FRKSSINEQF MDTRHSREML STHSSPYKTL
     ERRPQGGRSM PTTPVLTRNA YSSSHLEPDS SSQHCRQRSG SLESQSHLLS EMDSDKPFFT
     LSKSQRSSST EILDDGSSYT SQSSSEYYCV TPAASPYYTT QTLDTRARGR RRSKKHSVST
     SNSGSMPNLA QKDPLRNGVY SKGQDPPPSG YYIAGYPPYA ECDLYYSGGY VYENDTEGQY
     SVNPSYRSSA HYGYDRQRDY SRSFHEDEVD RVPHNPYATL RLPRKAAVKS EHITKNIHKA
     LVAEHLRGWY QRASGQKDQG HSPQTSFDSD RGSQRCLGFA GLQVPCSPSS RASSYSSVSS
     TNASGNWRTQ LTIGLSEYEN PVHSPYTSYY GSIYNPLSSP SRQYAETTPL DGTDGSQLED
     NLEGSEQRLF WHEDSKPGTL V
//
ID   SP16H_MOUSE             Reviewed;        1047 AA.
AC   Q920B9; Q3TZ48; Q3UFH0; Q921H4;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 2.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=FACT complex subunit SPT16;
DE   AltName: Full=Chromatin-specific transcription elongation factor 140 kDa subunit;
DE   AltName: Full=FACT 140 kDa subunit;
DE   AltName: Full=FACTp140;
DE   AltName: Full=Facilitates chromatin transcription complex subunit SPT16;
GN   Name=Supt16h; Synonyms=Fact140, Factp140;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=21363811; PubMed=11471063; DOI=10.1007/s003350020036;
RA   McGuire M.V., Suthipinijtham P., Gascoigne N.R.J.;
RT   "The mouse Supt16h/Fact140 gene, encoding part of the FACT chromatin
RT   transcription complex, maps close to Tcra and is highly expressed in
RT   thymus.";
RL   Mamm. Genome 12:664-667(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-637.
RC   STRAIN=C57BL/6J; TISSUE=Inner ear, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 803-1047.
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-979; SER-982 AND
RP   SER-986, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Component of the FACT complex, a general chromatin
CC       factor that acts to reorganize nucleosomes. The FACT complex is
CC       involved in multiple processes that require DNA as a template such
CC       as mRNA elongation, DNA replication and DNA repair. During
CC       transcription elongation the FACT complex acts as a histone
CC       chaperone that both destabilizes and restores nucleosomal
CC       structure. It facilitates the passage of RNA polymerase II and
CC       transcription by promoting the dissociation of one histone H2A-H2B
CC       dimer from the nucleosome, then subsequently promotes the
CC       reestablishment of the nucleosome following the passage of RNA
CC       polymerase II. The FACT complex is probably also involved in
CC       phosphorylation of 'Ser-392' of p53/TP53 via its association with
CC       CK2 (casein kinase II). Also involved in vitamin D-coupled
CC       transcription regulation via its association with the WINAC
CC       complex, a chromatin-remodeling complex recruited by vitamin D
CC       receptor (VDR), which is required for the ligand-bound VDR-
CC       mediated transrepression of the CYP27B1 gene (By similarity).
CC   -!- SUBUNIT: Component of the FACT complex, a stable heterodimer of
CC       SSRP1 and SUPT16H. Also component of a CK2-SPT16-SSRP1 complex
CC       which forms following UV irradiation, composed of SSRP1, SUPT16H,
CC       CSNK2A1, CSNK2A2 and CSNK2B. Component of the WINAC complex, at
CC       least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2,
CC       SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and
CC       TOP2B. Interacts with NEK9. Binds to histone H2A-H2B. Interacts
CC       with GTF2E2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Colocalizes with
CC       RNA polymerase II on chromatin. Recruited to actively transcribed
CC       loci.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed in brain, liver,
CC       heart, kidneys, lungs, spleen, thymus, ovary, and testes, with
CC       highest levels of expression observed in thymus.
CC   -!- DOMAIN: The Glu-rich acidic region in C-terminus is essential for
CC       FACT activity (By similarity).
CC   -!- PTM: ADP-ribosylated. ADP-ribosylation by PARP1 is induced by
CC       genotoxic stress and correlates with dissociation of FACT from
CC       chromatin.
CC   -!- SIMILARITY: Belongs to the peptidase M24 family. SPT16 subfamily.
CC   -!- CAUTION: Although related to the peptidase M24 family, this
CC       protein lacks conserved active site residues suggesting that it
CC       may lack peptidase activity.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH12433.1; Type=Erroneous initiation;
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DR   EMBL; AF323667; AAL04452.1; -; mRNA.
DR   EMBL; AK148506; BAE28591.1; -; mRNA.
DR   EMBL; AK158116; BAE34362.1; -; mRNA.
DR   EMBL; BC012433; AAH12433.1; ALT_INIT; mRNA.
DR   IPI; IPI00120344; -.
DR   RefSeq; NP_291096.2; NM_033618.3.
DR   UniGene; Mm.21662; -.
DR   UniGene; Mm.480661; -.
DR   ProteinModelPortal; Q920B9; -.
DR   SMR; Q920B9; 1-435.
DR   STRING; Q920B9; -.
DR   MEROPS; M24.974; -.
DR   PhosphoSite; Q920B9; -.
DR   PRIDE; Q920B9; -.
DR   Ensembl; ENSMUST00000046709; ENSMUSP00000042283; ENSMUSG00000035726.
DR   GeneID; 114741; -.
DR   KEGG; mmu:114741; -.
DR   UCSC; uc007tor.1; mouse.
DR   CTD; 114741; -.
DR   MGI; MGI:1890948; Supt16h.
DR   GeneTree; ENSGT00390000014495; -.
DR   HOGENOM; HBG589021; -.
DR   HOVERGEN; HBG092544; -.
DR   InParanoid; Q920B9; -.
DR   OrthoDB; EOG40K7Z3; -.
DR   PhylomeDB; Q920B9; -.
DR   NextBio; 368789; -.
DR   ArrayExpress; Q920B9; -.
DR   Bgee; Q920B9; -.
DR   CleanEx; MM_SUPT16H; -.
DR   Genevestigator; Q920B9; -.
DR   GermOnline; ENSMUSG00000035726; Mus musculus.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR013719; DUF1747_euk.
DR   InterPro; IPR013953; FACT_Spt16p.
DR   InterPro; IPR000994; Pept_M24_structural-domain.
DR   InterPro; IPR000640; Transl_elong_EFG/EF2_C.
DR   Gene3D; G3DSA:3.90.230.10; Peptidase_M24_cat_core; 1.
DR   Gene3D; G3DSA:3.30.70.240; Transl_elong_EFG/EF2_C; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   Pfam; PF08512; Rtt106; 1.
DR   Pfam; PF08644; SPT16; 1.
DR   SUPFAM; SSF55920; Peptidase_M24_cat_core; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ADP-ribosylation; Chromosome; Coiled coil; DNA damage;
KW   DNA repair; DNA replication; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1047       FACT complex subunit SPT16.
FT                                /FTId=PRO_0000245170.
FT   COILED      465    507       Potential.
FT   COMPBIAS    438    443       Poly-Glu.
FT   COMPBIAS    926   1011       Glu-rich (acidic).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     139    139       N6-acetyllysine (By similarity).
FT   MOD_RES     196    196       N6-acetyllysine (By similarity).
FT   MOD_RES     223    223       N6-acetyllysine (By similarity).
FT   MOD_RES     508    508       Phosphoserine (By similarity).
FT   MOD_RES     513    513       N6-acetyllysine (By similarity).
FT   MOD_RES     632    632       Phosphotyrosine (By similarity).
FT   MOD_RES     650    650       Phosphoserine (By similarity).
FT   MOD_RES     732    732       N6-acetyllysine (By similarity).
FT   MOD_RES     786    786       N6-acetyllysine (By similarity).
FT   MOD_RES     904    904       N6-acetyllysine (By similarity).
FT   MOD_RES     932    932       Phosphoserine (By similarity).
FT   MOD_RES     979    979       Phosphoserine.
FT   MOD_RES     982    982       Phosphoserine.
FT   MOD_RES     986    986       Phosphoserine.
FT   MOD_RES    1015   1015       Phosphoserine (By similarity).
FT   CONFLICT    453    453       R -> G (in Ref. 1; AAL04452).
FT   CONFLICT    862    862       K -> E (in Ref. 1; AAL04452).
SQ   SEQUENCE   1047 AA;  119825 MW;  51931F5639CD221E CRC64;
     MAVTLDKDAY YRRVKRLYSN WRKGEDEYAS IDAIVVSVGV DEEIVYAKST ALQTWLFGYE
     LTDTIMVFCD DKIIFMASKK KVEFLKQIAN TKGNENANGA PAITLLVREK NESNKSSFDK
     MIDAIKESKS GKKIGVFSKD KFPGEFMKSW SDCLNKEGFD KVDISAVVAY TIAVKEDGEL
     NLMKKAASIT SEVFNKFFKE RVMEIVDADE KVRHSKLAES VEKAIEEKKY LAGADPSTVE
     MCYPPIIQSG GNYNLKFSVV SDKNHMHFGA ITCAMGIRFK SYCSNLVRTL MVDPTQEVQE
     NYNFLLQLQE ELLKELRHGV KICDVYNSVM DVVKKQKPEL LNKITKNLGF GMGIEFREGS
     LVINSKNQYK LKKGMVFSIN LGFSDLTNKE GKKPEEKTYA LFIGDTVLVD EDGPATILTS
     VKKKVKNVGI FLKNEDDEEE EEEKDEAEDL LGRGSRAALL TERTRNEMTA EEKRRAHQKE
     LAAQLNEEAK RRLTEQKGEQ QIQKARKSNV SYKNPSLMPK EPHIREMKIY IDKKYETVIM
     PVFGIATPFH IATIKNISMS VEGDYTYLRI NFYCPGSALG RNEGNIFPNP EATFVKEITY
     RASNMKAPGE QTVPALNLQN AFRIIKEVQK RYKTREAEEK EKEGIVKQDS LVINLNRSNP
     KLKDLYIRPN IAQKRMQGSL EAHVNGFRFT SVRGDKVDIL YNNIKHALFQ PCDGEMIIVL
     HFHLKNAVMF GKKRHTDVQF YTEVGEITTD LGKHQHMHDR DDLYAEQMER EMRHKLKTAF
     KNFIEKVEAL TKEELEFEVP FRDLGFNGAP YRSTCLLQPT SSALVNATEW PPFVVTLDEV
     ELIHFERVQF HLKNFDMVIV YKDYSKKVTM INAIPVASLD PIKEWLNSCD LKYTEGVQSL
     NWTKIMKTIV DDPEGFFEQG GWSFLEPEGE GSDAEDGDSE SEIEDETFNP SEDDYEEEEE
     DSDEDYSSEA EESDYSKESL GSEEESGKDW DELEEEARKA DRESRYEEEE EQSRSMSRKR
     KASVHSSGRG SNRGSRHSSA PPKKKRK
//
ID   KCNH5_MOUSE             Reviewed;         988 AA.
AC   Q920E3; Q8C035;
DT   28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 2.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Potassium voltage-gated channel subfamily H member 5;
DE   AltName: Full=Ether-a-go-go potassium channel 2;
DE            Short=Eag2;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv10.2;
GN   Name=Kcnh5; Synonyms=Eag2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 32-203.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Saganich M.J., Vega-Saenz de Miera E.C., Rudy B.;
RT   "Cloning of the mouse eag2 potassium channel.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium
CC       channel. Elicits a non-inactivating outward rectifying current (By
CC       similarity). Channel properties may be modulated by cAMP and
CC       subunit assembly.
CC   -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC       heterotetrameric complex of pore-forming alpha subunits that can
CC       associate with modulating beta subunits. Heteromultimer with
CC       KCNH1/EAG (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position.
CC   -!- SIMILARITY: Belongs to the potassium channel family. H (Eag)
CC       (TC 1.A.1.20) subfamily. Kv10.2/KCNH5 sub-subfamily.
CC   -!- SIMILARITY: Contains 1 cyclic nucleotide-binding domain.
CC   -!- SIMILARITY: Contains 1 PAC (PAS-associated C-terminal) domain.
CC   -!- SIMILARITY: Contains 1 PAS (PER-ARNT-SIM) domain.
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DR   EMBL; AK032438; BAC27869.1; -; mRNA.
DR   EMBL; AF309565; AAL09442.1; -; mRNA.
DR   IPI; IPI00223584; -.
DR   RefSeq; NP_766393.2; NM_172805.3.
DR   UniGene; Mm.44465; -.
DR   ProteinModelPortal; Q920E3; -.
DR   SMR; Q920E3; 26-133, 419-472, 475-662.
DR   STRING; Q920E3; -.
DR   PhosphoSite; Q920E3; -.
DR   PRIDE; Q920E3; -.
DR   Ensembl; ENSMUST00000042299; ENSMUSP00000046864; ENSMUSG00000034402.
DR   GeneID; 238271; -.
DR   KEGG; mmu:238271; -.
DR   UCSC; uc007nwz.1; mouse.
DR   CTD; 238271; -.
DR   MGI; MGI:3584508; Kcnh5.
DR   GeneTree; ENSGT00550000074394; -.
DR   HOGENOM; HBG717083; -.
DR   HOVERGEN; HBG101348; -.
DR   InParanoid; Q920E3; -.
DR   OrthoDB; EOG47PX5C; -.
DR   NextBio; 383713; -.
DR   ArrayExpress; Q920E3; -.
DR   Bgee; Q920E3; -.
DR   Genevestigator; Q920E3; -.
DR   GermOnline; ENSMUSG00000034402; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:two-component sensor activity; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003949; K_chnl_volt-dep_EAG.
DR   InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PRINTS; PR01463; EAGCHANLFMLY.
DR   PRINTS; PR01464; EAGCHANNEL.
DR   SMART; SM00100; cNMP; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF51206; cNMP_binding; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; FALSE_NEG.
DR   PROSITE; PS00889; CNMP_BINDING_2; FALSE_NEG.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Calmodulin-binding; Glycoprotein; Ion transport; Ionic channel;
KW   Isopeptide bond; Membrane; Potassium; Potassium channel;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport;
KW   Ubl conjugation; Voltage-gated channel.
FT   CHAIN         1    988       Potassium voltage-gated channel subfamily
FT                                H member 5.
FT                                /FTId=PRO_0000054011.
FT   TOPO_DOM      1    217       Cytoplasmic (Potential).
FT   TRANSMEM    218    238       Helical; Name=Segment S1; (Potential).
FT   TOPO_DOM    239    243       Extracellular (Potential).
FT   TRANSMEM    244    264       Helical; Name=Segment S2; (Potential).
FT   TOPO_DOM    265    291       Cytoplasmic (Potential).
FT   TRANSMEM    292    312       Helical; Name=Segment S3; (Potential).
FT   TOPO_DOM    313    319       Extracellular (Potential).
FT   TRANSMEM    320    340       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TOPO_DOM    341    346       Cytoplasmic (Potential).
FT   TRANSMEM    347    367       Helical; Name=Segment S5; (Potential).
FT   TOPO_DOM    368    419       Extracellular (Potential).
FT   INTRAMEM    420    440       Pore-forming; Name=Segment H5;
FT                                (Potential).
FT   TOPO_DOM    441    446       Extracellular (Potential).
FT   TRANSMEM    447    467       Helical; Name=Segment S6; (Potential).
FT   TOPO_DOM    468    988       Cytoplasmic (Potential).
FT   DOMAIN       14     86       PAS.
FT   DOMAIN       91    143       PAC.
FT   NP_BIND     550    668       cNMP.
FT   REGION      704    715       Calmodulin-binding (Potential).
FT   REGION      909    948       CAD (involved in subunit assembly) (By
FT                                similarity).
FT   MOTIF       432    437       Selectivity filter (By similarity).
FT   CARBOHYD    403    403       N-linked (GlcNAc...) (Potential).
FT   CROSSLNK    785    785       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
SQ   SEQUENCE   988 AA;  111782 MW;  0EEE1F577F5C18BB CRC64;
     MPGGKRGLVA PQNTFLENIV RRSSESSFLL GNAQIVDWPV VYSNDGFCKL SGYHRADVMQ
     KSSTCSFMYG ELTDKKTIEK VRQTFDNYES NCFEVLLYKK NRTPVWFYMQ IAPIRNEHEK
     VVLFLCTFKD ITLFKQPIED DSTKGWTKFA RLTRALTNSR SVLQQLTPMN KTETVHKHSR
     LAEVLQLGSD ILPQYKQEAP KTPPHIILHY CAFKTTWDWV ILILTFYTAI MVPYNVSFKT
     KQNNIAWLVL DSVVDVIFLV DIVLNFHTTF VGPGGEVISD PKLIRMNYLK TWFVIDLLSC
     LPYDIINAFE NVDEGISSLF SSLKVVRLLR LGRVARKLDH YLEYGAAVLV LLVCVFGLVA
     HWLACIWYSI GDYEVIDEVT NTIQIDSWLY QLALSIGTPY RYNTSAGIWE GGPSKDSLYV
     SSLYFTMTSL TTIGFGNIAP TTDVEKMFSV AMMMVGSLLY ATIFGNVTTI FQQMYANTNR
     YHEMLNNVRD FLKLYQVPKG LSERVMDYIV STWSMSKGID TEKVLSICPK DMRADICVHL
     NRKVFNEHPA FQLASDGCLR ALAVEFQTIH CAPGDLIYHA GESVDALCFV VSGSLEVIQD
     EEVVAILGKG DVFGDIFWKE TTLAHACANV RALTYCDLHI IKREALLKVL DFYTAFANSF
     SRNLTLTCNL RKRIIFRKIS DVKKEEEERL RQKNEVTLSI PVDHPVRKLF QKFKQQKELR
     IQGSAQSDPE RSQLQVESRP LQNGASITGT SVVTVSQITP IQTSLAYVKT SESLKQNNRD
     AMELKPNGGA EPKCLKVNSP IRMKNGNGKG WLRLKNNMGA QEEKKEDWNN VTKAESMGLL
     SEDPKGSDSE NSVTKNPLRK TDSCDSGITK SDLRLDKAGE ARSPLEHSPS QADVKHSFYP
     IPEQALQTTL QEVKHELKED IQLLSCRMTA LEKQVAEILK LLSEKSVPQT SSPKPQIPLQ
     VPPQIPCQDI FSVSRPESPE SDKDEINF
//
ID   CORO6_MOUSE             Reviewed;         471 AA.
AC   Q920M5; Q3TZ14; Q5F262; Q5F263; Q5F264; Q5F265; Q920M3; Q920M4;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-FEB-2011, entry version 59.
DE   RecName: Full=Coronin-6;
DE   AltName: Full=Coronin-like protein E;
DE            Short=Clipin-E;
GN   Name=Coro6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
RC   STRAIN=ICR; TISSUE=Brain;
RA   Watanabe N., Takeuchi K., Kusumi A.;
RT   "Expression and function of mammalian clipin E/coronin 6.";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC   STRAIN=C57BL/6J; TISSUE=Inner ear;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=A;
CC         IsoId=Q920M5-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=Q920M5-2; Sequence=VSP_011749;
CC       Name=C;
CC         IsoId=Q920M5-3; Sequence=VSP_011750;
CC       Name=D;
CC         IsoId=Q920M5-4; Sequence=VSP_011749, VSP_021487;
CC   -!- SIMILARITY: Contains 5 WD repeats.
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DR   EMBL; AB070894; BAB64361.1; -; mRNA.
DR   EMBL; AB070895; BAB64362.1; -; mRNA.
DR   EMBL; AB070896; BAB64363.1; -; mRNA.
DR   EMBL; AK158179; BAE34396.1; -; mRNA.
DR   EMBL; AL607072; CAI52031.1; -; Genomic_DNA.
DR   EMBL; AL607072; CAI52032.1; -; Genomic_DNA.
DR   EMBL; AL607072; CAI52033.1; -; Genomic_DNA.
DR   EMBL; AL607072; CAI52034.1; -; Genomic_DNA.
DR   IPI; IPI00120762; -.
DR   IPI; IPI00120764; -.
DR   IPI; IPI00263646; -.
DR   IPI; IPI00648746; -.
DR   RefSeq; NP_624354.1; NM_139128.1.
DR   RefSeq; NP_624355.1; NM_139129.1.
DR   RefSeq; NP_624356.1; NM_139130.2.
DR   UniGene; Mm.33477; -.
DR   ProteinModelPortal; Q920M5; -.
DR   SMR; Q920M5; 9-393.
DR   PhosphoSite; Q920M5; -.
DR   PRIDE; Q920M5; -.
DR   Ensembl; ENSMUST00000021190; ENSMUSP00000021190; ENSMUSG00000020836.
DR   Ensembl; ENSMUST00000052515; ENSMUSP00000056862; ENSMUSG00000020836.
DR   Ensembl; ENSMUST00000108391; ENSMUSP00000104028; ENSMUSG00000020836.
DR   GeneID; 216961; -.
DR   KEGG; mmu:216961; -.
DR   UCSC; uc007kgr.1; mouse.
DR   UCSC; uc007kgs.1; mouse.
DR   UCSC; uc007kgt.1; mouse.
DR   CTD; 216961; -.
DR   MGI; MGI:2183448; Coro6.
DR   GeneTree; ENSGT00550000074317; -.
DR   HOVERGEN; HBG059978; -.
DR   OMA; QEERITA; -.
DR   PhylomeDB; Q920M5; -.
DR   NextBio; 375460; -.
DR   ArrayExpress; Q920M5; -.
DR   Bgee; Q920M5; -.
DR   CleanEx; MM_CORO6; -.
DR   Genevestigator; Q920M5; -.
DR   GermOnline; ENSMUSG00000020836; Mus musculus.
DR   InterPro; IPR015505; Coronin.
DR   InterPro; IPR015048; DUF1899.
DR   InterPro; IPR015049; DUF1900.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   PANTHER; PTHR10856; Coronin; 1.
DR   Pfam; PF08953; DUF1899; 1.
DR   Pfam; PF08954; DUF1900; 1.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM00320; WD40; 3.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Coiled coil; Repeat; WD repeat.
FT   CHAIN         1    471       Coronin-6.
FT                                /FTId=PRO_0000050932.
FT   REPEAT       79    119       WD 1.
FT   REPEAT      129    169       WD 2.
FT   REPEAT      173    212       WD 3.
FT   REPEAT      216    259       WD 4.
FT   REPEAT      264    304       WD 5.
FT   COILED      426    468       Potential.
FT   MOD_RES     338    338       N6-acetyllysine (By similarity).
FT   VAR_SEQ     212    251       Missing (in isoform C).
FT                                /FTId=VSP_011750.
FT   VAR_SEQ     214    247       ARPHEGARPLRAVFTADGKLLSTGFSRMSERQLA -> FAA
FT                                HEGMRPMRAVFTRLGHIFTTGFTRMSQRELG (in
FT                                isoform B and isoform D).
FT                                /FTId=VSP_011749.
FT   VAR_SEQ     432    432       Q -> QQ (in isoform D).
FT                                /FTId=VSP_021487.
SQ   SEQUENCE   471 AA;  52599 MW;  4C5D043454E0F007 CRC64;
     MSRRVVRQSK FRHVFGQAAK ADQAYEDIRV SKVTWDSAFC AVNPKFLAII VEAGGGGAFI
     VLPLAKTGRV DKNYPLVTGH TGPVLDIDWC PHNDNVIASA SDDTTVMVWQ IPDYTPVRNI
     TEPVITLEGH SKRVGILSWH PTARNVLLSA GGDNVIIIWN VGTGEVLLSL DDIHPDVIHS
     VCWNSNGSLL ATTCKDKTLR IIDPRKSQVV AERARPHEGA RPLRAVFTAD GKLLSTGFSR
     MSERQLALWD PNNFEEPVAL QEMDTSNGVL LPFYDPDSSI VYLCGKGDSS IRYFEITEEP
     PFVHYLNTFS SKEPQRGMGF MPKRGLDVSK CEIARFYKLH ERKCEPIIMT VPRKSDLFQD
     DLYPDTPGPE PALEADEWLS GQDAEPVLIS LKEGYVPPKH RELRVTKRNI LDVRPPASPR
     RSQSASEAPL SQHTLETLLE EIKALRDRVQ AQEERITALE NMLCELVDGT D
//
ID   SYT17_MOUSE             Reviewed;         470 AA.
AC   Q920M7; Q3UXZ2;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Synaptotagmin-17;
DE   AltName: Full=Protein B/K;
DE   AltName: Full=Synaptotagmin XVII;
DE            Short=SytXVII;
GN   Name=Syt17; Synonyms=Bk;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=21573689; PubMed=11716773; DOI=10.1042/0264-6021:3600441;
RA   Fukuda M., Mikoshiba K.;
RT   "The N-terminal cysteine cluster is essential for membrane targeting
RT   of B/K protein.";
RL   Biochem. J. 360:441-448(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-470.
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the synaptotagmin family.
CC   -!- SIMILARITY: Contains 2 C2 domains.
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DR   EMBL; AB069667; BAB69676.1; -; mRNA.
DR   EMBL; AK135098; BAE22421.1; -; mRNA.
DR   IPI; IPI00310436; -.
DR   RefSeq; NP_619590.1; NM_138649.1.
DR   UniGene; Mm.156558; -.
DR   HSSP; P21707; 1K5W.
DR   ProteinModelPortal; Q920M7; -.
DR   SMR; Q920M7; 178-461.
DR   STRING; Q920M7; -.
DR   PhosphoSite; Q920M7; -.
DR   PRIDE; Q920M7; -.
DR   Ensembl; ENSMUST00000081574; ENSMUSP00000080284; ENSMUSG00000058420.
DR   GeneID; 110058; -.
DR   KEGG; mmu:110058; -.
DR   NMPDR; fig|10090.3.peg.17493; -.
DR   UCSC; uc009jju.1; mouse.
DR   CTD; 110058; -.
DR   MGI; MGI:104966; Syt17.
DR   eggNOG; roNOG10771; -.
DR   GeneTree; ENSGT00600000084331; -.
DR   HOGENOM; HBG716633; -.
DR   HOVERGEN; HBG108530; -.
DR   InParanoid; Q920M7; -.
DR   OMA; PPPISYD; -.
DR   OrthoDB; EOG4Q58PH; -.
DR   PhylomeDB; Q920M7; -.
DR   NextBio; 363241; -.
DR   ArrayExpress; Q920M7; -.
DR   Bgee; Q920M7; -.
DR   CleanEx; MM_SYT17; -.
DR   Genevestigator; Q920M7; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008021; C:synaptic vesicle; IEA:InterPro.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   InterPro; IPR014705; BKprotein.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR001565; Synaptotagmin.
DR   PANTHER; PTHR10024:SF25; BKprotein; 1.
DR   Pfam; PF00168; C2; 2.
DR   PRINTS; PR00399; SYNAPTOTAGMN.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 2.
PE   2: Evidence at transcript level;
KW   Membrane; Repeat.
FT   CHAIN         1    470       Synaptotagmin-17.
FT                                /FTId=PRO_0000311937.
FT   DOMAIN      182    290       C2 1.
FT   DOMAIN      319    422       C2 2.
FT   COMPBIAS     19     36       Cys-rich.
FT   CONFLICT      2      7       LEPLNE -> PPQWPQ (in Ref. 2; BAE22421).
SQ   SEQUENCE   470 AA;  53293 MW;  7F3C3036901D9D1C CRC64;
     MLEPLNEGLL SRISDVLLCG WTCQHCCQRC YESSCCQSSE DEVEILGPFP AQTPPWLMAS
     RSNDKDGDSV HTASDVPLTP RTNSPDGRRS SSDTSKSTYS LTRRISSLDS RRPSSPLIDI
     KPVEFGVLSA KKESIQPSVL RRTYTPDDYF RKFEPRLYSL DSNLDDVDSL TDEEIMSKYQ
     LGMLHFSTQY DLLHNHLTVR VIEARDLPPP ISHDGSRQDM AHSNPYVKIC LLPDQKNSKQ
     TGVKRKTQKP VFEERYTFEI PFLEAQRRTL LLTVVDFDKF SRHCVIGKVA VPLCEVDLVK
     GGHWWKALIP SSQNEVELGE LLLSLNYLPS AGRLNVDIIR AKQLLQTDVS QGSDPFVKIQ
     LVHGLKLVKT KKTSFLRGTI DPFYNESFSF KVPQEELENA SLVFTVFGHN MKSSNDFIGR
     IVIGQYSSGP SESNHWRRML NTHRTAVEQW HSLRSRAECD RVSPASLEVT
//
ID   SYT12_MOUSE             Reviewed;         421 AA.
AC   Q920N7;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Synaptotagmin-12;
DE   AltName: Full=Synaptotagmin XII;
DE            Short=SytXII;
GN   Name=Syt12;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=21523930; PubMed=11514560; DOI=10.1074/jbc.M105356200;
RA   Fukuda M., Kanno E., Ogata Y., Mikoshiba K.;
RT   "Mechanism of the SDS-resistant synaptotagmin clustering mediated by
RT   the cysteine cluster at the interface between the transmembrane and
RT   spacer domains.";
RL   J. Biol. Chem. 276:40319-40325(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Adipose tissue, and Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: May be involved in Ca(2+)-dependent exocytosis of
CC       secretory vesicles through Ca(2+) and phospholipid binding to the
CC       C2 domain or may serve as Ca(2+) sensors in the process of
CC       vesicular trafficking and exocytosis (By similarity).
CC   -!- SUBUNIT: Homodimer. Can also form heterodimers (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane; Single-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the synaptotagmin family.
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; AB062804; BAB69674.1; -; mRNA.
DR   EMBL; AK046627; BAC32812.1; -; mRNA.
DR   EMBL; AK083139; BAC38779.1; -; mRNA.
DR   IPI; IPI00120798; -.
DR   RefSeq; NP_598925.1; NM_134164.5.
DR   UniGene; Mm.262270; -.
DR   ProteinModelPortal; Q920N7; -.
DR   SMR; Q920N7; 152-420.
DR   STRING; Q920N7; -.
DR   PhosphoSite; Q920N7; -.
DR   PRIDE; Q920N7; -.
DR   Ensembl; ENSMUST00000059295; ENSMUSP00000055237; ENSMUSG00000049303.
DR   GeneID; 171180; -.
DR   KEGG; mmu:171180; -.
DR   UCSC; uc008gad.1; mouse.
DR   CTD; 171180; -.
DR   MGI; MGI:2159601; Syt12.
DR   GeneTree; ENSGT00600000084331; -.
DR   HOGENOM; HBG445851; -.
DR   HOVERGEN; HBG057176; -.
DR   InParanoid; Q920N7; -.
DR   OMA; EYHLSVI; -.
DR   OrthoDB; EOG4DV5MC; -.
DR   PhylomeDB; Q920N7; -.
DR   NextBio; 370588; -.
DR   ArrayExpress; Q920N7; -.
DR   Bgee; Q920N7; -.
DR   CleanEx; MM_SYT12; -.
DR   Genevestigator; Q920N7; -.
DR   GermOnline; ENSMUSG00000049303; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR001565; Synaptotagmin.
DR   Pfam; PF00168; C2; 2.
DR   PRINTS; PR00399; SYNAPTOTAGMN.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cytoplasmic vesicle; Membrane; Repeat; Synapse;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    421       Synaptotagmin-12.
FT                                /FTId=PRO_0000183973.
FT   TOPO_DOM      1     18       Vesicular (Potential).
FT   TRANSMEM     19     39       Helical; (Potential).
FT   TOPO_DOM     40    421       Cytoplasmic (Potential).
FT   DOMAIN      168    272       C2 1.
FT   DOMAIN      285    388       C2 2.
SQ   SEQUENCE   421 AA;  46680 MW;  4E854C7B2089597C CRC64;
     MAVDVTEYHL SVIKSPPGWE VGVYAAGALA LLGIAAVSLW KLWTSGSFPS PSPFPNYDYR
     YLQQKYGEAY VEAKLKRVPP WNDQRTTTRG PPSRKGSLSI EDTFESISEL GPLELMGREL
     DLAPYGTLRK SQSADSLNSI SSVSNTFGQD FTLGQVEVSM DYDGASHTLH VAVLQGKDLL
     EREEATFESC FMRVSLLPDE QIVGISRIQR NAYSIFFDEK FSVPLDPTAL EEKSLRFSVF
     GIDEDERNVS TGVVELKLSV LDLPLQPFSG WLYLQDQNKA ADAVGEILLS LSYLPTAERL
     TVVVVKAKNL IWTNEKSTAD PFVKVYLLQD GRKMSKKKTA VKRDDPNPVF NEAMIFSVPA
     IVLQDLSLRV TVAESSSDGR GDNVGHVIIG PGVSGMGTTH WNQMLATLRR PVSMWHPVRR
     N
//
ID   DBC1_MOUSE              Reviewed;         760 AA.
AC   Q920P3; Q80ZL2; Q812F0; Q8C1C9; Q920P4; Q9QXL0;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Deleted in bladder cancer protein 1 homolog;
DE   AltName: Full=BMP/retinoic acid-inducible neural-specific protein 1;
DE   AltName: Full=Protein FAM5A;
DE   Flags: Precursor;
GN   Name=Dbc1; Synonyms=Brinp, Brinp1, Dbccr1, Fam5a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Brain, and Embryonic stem cell;
RX   PubMed=15193423; DOI=10.1016/j.molbrainres.2004.04.001;
RA   Kawano H., Nakatani T., Mori T., Ueno S., Fukaya M., Abe A.,
RA   Kobayashi M., Toda F., Watanabe M., Matsuoka I.;
RT   "Identification and characterization of novel developmentally
RT   regulated neural-specific proteins, BRINP family.";
RL   Brain Res. Mol. Brain Res. 125:60-75(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Ochal L.K., Sowden M.P., Messing E.M., Wheeless L.L., Reeder J.E.;
RT   "Mouse DBCCR1 cDNA.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Corpora quadrigemina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Inhibits cell proliferation by negative regulation of
CC       the G1/S transition. Mediates cell death which is not of the
CC       classical apoptotic type and regulates expression of components of
CC       the plasminogen pathway (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q920P3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q920P3-2; Sequence=VSP_017024, VSP_017025;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in brain.
CC   -!- DEVELOPMENTAL STAGE: Expressed from 9.5 dpc.
CC   -!- SIMILARITY: Belongs to the FAM5 family.
CC   -!- SIMILARITY: Contains 1 MACPF domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB060587; BAB70600.1; -; Genomic_DNA.
DR   EMBL; AB060589; BAB70601.1; -; mRNA.
DR   EMBL; AB088118; BAC55204.1; -; Genomic_DNA.
DR   EMBL; AF202896; AAF17579.1; -; mRNA.
DR   EMBL; AK028321; BAC25879.1; -; mRNA.
DR   EMBL; AK045420; BAC32355.1; -; mRNA.
DR   EMBL; BX088573; CAI26033.1; -; Genomic_DNA.
DR   EMBL; BX649413; CAI26033.1; JOINED; Genomic_DNA.
DR   EMBL; BX649413; CAI24368.1; -; Genomic_DNA.
DR   EMBL; BX088573; CAI24368.1; JOINED; Genomic_DNA.
DR   EMBL; BC048789; AAH48789.1; -; mRNA.
DR   EMBL; BC079630; AAH79630.1; -; mRNA.
DR   IPI; IPI00135131; -.
DR   IPI; IPI00719940; -.
DR   RefSeq; NP_064351.2; NM_019967.2.
DR   UniGene; Mm.248788; -.
DR   ProteinModelPortal; Q920P3; -.
DR   SMR; Q920P3; 92-153.
DR   STRING; Q920P3; -.
DR   PRIDE; Q920P3; -.
DR   Ensembl; ENSMUST00000030036; ENSMUSP00000030036; ENSMUSG00000028351.
DR   GeneID; 56710; -.
DR   KEGG; mmu:56710; -.
DR   UCSC; uc008thw.1; mouse.
DR   UCSC; uc008thx.1; mouse.
DR   CTD; 56710; -.
DR   MGI; MGI:1928478; Dbc1.
DR   eggNOG; roNOG09856; -.
DR   GeneTree; ENSGT00390000008571; -.
DR   HOGENOM; HBG445938; -.
DR   HOVERGEN; HBG081412; -.
DR   InParanoid; Q920P3; -.
DR   OMA; PLPLMPE; -.
DR   OrthoDB; EOG480HW3; -.
DR   PhylomeDB; Q920P3; -.
DR   NextBio; 313175; -.
DR   ArrayExpress; Q920P3; -.
DR   Bgee; Q920P3; -.
DR   CleanEx; MM_DBC1; -.
DR   Genevestigator; Q920P3; -.
DR   GermOnline; ENSMUSG00000028351; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0007050; P:cell cycle arrest; IEA:UniProtKB-KW.
DR   GO; GO:0008219; P:cell death; ISS:UniProtKB.
DR   InterPro; IPR020864; MACPF.
DR   Pfam; PF01823; MACPF; 1.
DR   SMART; SM00457; MACPF; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell cycle; Cytoplasm; Glycoprotein;
KW   Growth arrest; Signal.
FT   SIGNAL        1     16       Potential.
FT   CHAIN        17    760       Deleted in bladder cancer protein 1
FT                                homolog.
FT                                /FTId=PRO_0000045767.
FT   DOMAIN       68    251       MACPF.
FT   CARBOHYD    156    156       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    433    433       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    443    443       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    553    553       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    599    599       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    630    630       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    676    676       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     308    320       DEFKSFMKRLPSN -> GTQTTTVNASGQT (in
FT                                isoform 2).
FT                                /FTId=VSP_017024.
FT   VAR_SEQ     321    760       Missing (in isoform 2).
FT                                /FTId=VSP_017025.
FT   CONFLICT     62     62       R -> Q (in Ref. 3; BAC25879).
FT   CONFLICT    157    158       AT -> VP (in Ref. 2; AAF17579).
FT   CONFLICT    550    551       QM -> FQR (in Ref. 2; AAF17579).
FT   CONFLICT    608    608       W -> V (in Ref. 2; AAF17579).
SQ   SEQUENCE   760 AA;  88641 MW;  746E954368F1E49A CRC64;
     MNWRFVELLY FLFVWGRISV QPSRQEPAGT DQHVSKEFDW LISDRGPFHH SRSYLSFVER
     HRQGFTTRYK IYREFARWKV RNTAIERRDL VRHPVPLMPE FQRSIRLLGR RPTTQQFIDT
     IIKKYGTHLL ISATLGGEEA LTMYMDKSRL DRKSGNATQS VEALHQLASS YFVDRDGTMR
     RLHEIQISTG AIKVTETRTG PLGCNSYDNL DSVSSVLLQS TESKLHLQGL QIIFPQYLQE
     KFVQSALSYI MCNGEGEYVC QNSQCRCQCA EEFPQCNCPI TDIQIMEFTL ANMAKAWTEA
     YKDLENSDEF KSFMKRLPSN HFLTIGSIHQ HWGNDWDLQS RYKLLQSATE AQRQKIQRTA
     RKLFGLSVRC RHNPNHQLPR ERTIQQWLAR VQSLLYCNEN GFWGTFLESQ RSCVCHGSTT
     LCQRPIPCII GGNNSCAMCS LANISLCGSC NKGYKLYRGR CEPQNVDSER SEQFISFETD
     LDFQDLELKY LLQKMDSRLY VHTTFISNEI RLDTFFDPRW RKRMSLTLKS NKNRMDFIHM
     VIGMSMRICQ MRNSSLDPMF FVYVNPFSGS HSEGWNMPFG EFGYPRWEKI RLQNSQCYNW
     TLLLGNRWKT FFETVHIYLR SRTRLPTLRN ETGQGPVDLS DPSKRQFYIK ISDVQVFGYS
     LRFNADLLRS AVQQVNQSYT QGGQFYSSSS VMLLMLDIRD RINRLAPPVA PGKPQLDLFS
     CMLKHRLKLT NSEIIRVNHA LDLYNTEILK QSDQMTAKLC
//
ID   MSI2H_MOUSE             Reviewed;         346 AA.
AC   Q920Q6; Q8BQ90; Q920Q7;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-FEB-2011, entry version 73.
DE   RecName: Full=RNA-binding protein Musashi homolog 2;
DE            Short=Musashi-2;
GN   Name=Msi2; Synonyms=Msi2h;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION,
RP   PHOSPHORYLATION, INDUCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=C57BL/6, and ICR; TISSUE=Brain;
RX   MEDLINE=21472407; PubMed=11588182;
RA   Sakakibara S., Nakamura Y., Satoh H., Okano H.;
RT   "RNA-binding protein Musashi2: developmentally regulated expression in
RT   neural precursor cells and subpopulations of neurons in mammalian
RT   CNS.";
RL   J. Neurosci. 21:8091-8107(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=129/Ola; TISSUE=Embryo;
RX   MEDLINE=22882817; PubMed=12923295; DOI=10.1073/pnas.1734197100;
RA   Aubert J., Stavridis M.P., Tweedie S., O'Reilly M., Vierlinger K.,
RA   Li M., Ghazal P., Pratt T., Mason J.O., Roy D., Smith A.;
RT   "Screening for mammalian neural genes via fluorescence-activated cell
RT   sorter purification of neural precursors from Sox1-gfp knock-in
RT   mice.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11836-11841(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6, and ICR; TISSUE=Brain, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   FUNCTION.
RX   PubMed=12407178; DOI=10.1073/pnas.232087499;
RA   Sakakibara S., Nakamura Y., Yoshida T., Shibata S., Koike M.,
RA   Takano H., Ueda S., Uchiyama Y., Noda T., Okano H.;
RT   "RNA-binding protein Musashi family: roles for CNS stem cells and a
RT   subpopulation of ependymal cells revealed by targeted disruption and
RT   antisense ablation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:15194-15199(2002).
CC   -!- FUNCTION: RNA binding protein that regulates the expression of
CC       target mRNAs at the translation level. May play a role in the
CC       proliferation and maintenance of stem cells in the central nervous
CC       system.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Associated with polysomes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Msi2L;
CC         IsoId=Q920Q6-1; Sequence=Displayed;
CC       Name=2; Synonyms=Msi2S;
CC         IsoId=Q920Q6-2; Sequence=VSP_011173;
CC       Name=3;
CC         IsoId=Q920Q6-3; Sequence=VSP_011172, VSP_011174;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Expressed in proliferating neural
CC       precursor cells.
CC   -!- INDUCTION: Up-regulated in astrocytes after brain injury.
CC   -!- PTM: Phosphorylated.
CC   -!- SIMILARITY: Belongs to the Musashi family.
CC   -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AB056102; BAB69484.1; -; mRNA.
DR   EMBL; AB056103; BAB69485.1; -; mRNA.
DR   EMBL; BK001483; DAA01567.1; -; mRNA.
DR   EMBL; AK049637; BAC33851.1; -; mRNA.
DR   EMBL; AK049688; BAC33873.1; -; mRNA.
DR   EMBL; AK051269; BAC34584.1; -; mRNA.
DR   IPI; IPI00120924; -.
DR   IPI; IPI00462899; -.
DR   IPI; IPI00462900; -.
DR   RefSeq; NP_473384.1; NM_054043.3.
DR   UniGene; Mm.400451; -.
DR   UniGene; Mm.428433; -.
DR   UniGene; Mm.474737; -.
DR   ProteinModelPortal; Q920Q6; -.
DR   SMR; Q920Q6; 19-188.
DR   STRING; Q920Q6; -.
DR   PRIDE; Q920Q6; -.
DR   Ensembl; ENSMUST00000092794; ENSMUSP00000090470; ENSMUSG00000069769.
DR   GeneID; 76626; -.
DR   KEGG; mmu:76626; -.
DR   UCSC; uc007kvl.1; mouse.
DR   UCSC; uc007kvm.1; mouse.
DR   UCSC; uc007kvn.1; mouse.
DR   CTD; 76626; -.
DR   MGI; MGI:1923876; Msi2.
DR   GeneTree; ENSGT00560000076532; -.
DR   HOGENOM; HBG756718; -.
DR   HOVERGEN; HBG002295; -.
DR   InParanoid; Q920Q6; -.
DR   OMA; WQTSPES; -.
DR   PhylomeDB; Q920Q6; -.
DR   NextBio; 345476; -.
DR   ArrayExpress; Q920Q6; -.
DR   Bgee; Q920Q6; -.
DR   CleanEx; MM_MSI2; -.
DR   Genevestigator; Q920Q6; -.
DR   GermOnline; ENSMUSG00000069769; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005844; C:polysome; IDA:MGI.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0008266; F:poly(U) RNA binding; IDA:MGI.
DR   GO; GO:0048864; P:stem cell development; IMP:UniProtKB.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Phosphoprotein; Repeat;
KW   RNA-binding.
FT   CHAIN         1    346       RNA-binding protein Musashi homolog 2.
FT                                /FTId=PRO_0000081653.
FT   DOMAIN       21    111       RRM 1.
FT   DOMAIN      110    187       RRM 2.
FT   COMPBIAS    253    260       Poly-Ala.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   VAR_SEQ     264    282       VLNSYSAQPNFGAPASPAG -> GRKVYGAGGSQACLVCRG
FT                                R (in isoform 3).
FT                                /FTId=VSP_011172.
FT   VAR_SEQ     264    281       Missing (in isoform 2).
FT                                /FTId=VSP_011173.
FT   VAR_SEQ     283    346       Missing (in isoform 3).
FT                                /FTId=VSP_011174.
SQ   SEQUENCE   346 AA;  36939 MW;  C2C75F2D7077AF61 CRC64;
     MEANGSPGTS GSANDSQHDP GKMFIGGLSW QTSPDSLRDY FSKFGEIREC MVMRDPTTKR
     SRGFGFVTFA DPASVDKVLG QPHHELDSKT IDPKVAFPRR AQPKMVTRTK KIFVGGLSAN
     TVVEDVKQYF EQFGKVEDAM LMFDKTTNRH RGFGFVTFEN EDVVEKVCEI HFHEINNKMV
     ECKKAQPKEV MFPPGTRGRA RGLPYTMDAF MLGMGMLGYP NFVATYGRGY PGFAPSYGYQ
     FPGFPAAAYG PVAAAAVAAA RGSVLNSYSA QPNFGAPASP AGSNPARPGG FPGANSPGPV
     ADLYGPASQD SGVGNYISAA SPQPGSGFGH GIAGPLIATA FTNGYH
//
ID   ALS2_MOUSE              Reviewed;        1651 AA.
AC   Q920R0; Q8JZR1; Q9CXJ3;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   09-MAY-2003, sequence version 2.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Alsin;
DE   AltName: Full=Amyotrophic lateral sclerosis 2 protein homolog;
GN   Name=Als2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=21470351; PubMed=11586298; DOI=10.1038/ng1001-166;
RA   Hadano S., Hand C.K., Osuga H., Yanagisawa Y., Otomo A., Devon R.S.,
RA   Miyamoto N., Showguchi-Miyata J., Okada Y., Singaraja R.,
RA   Figlewicz D.A., Kwiatkowski T., Hosler B.A., Sagie T., Skaug J.,
RA   Nasir J., Brown R.H. Jr., Scherer S.W., Rouleau G.A., Hayden M.R.,
RA   Ikeda J.-E.;
RT   "A gene encoding a putative GTPase regulator is mutated in familial
RT   amyotrophic lateral sclerosis 2.";
RL   Nat. Genet. 29:166-173(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 847-1651 (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477 AND SER-486, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May act as a GTPase regulator (By similarity). Controls
CC       survival and growth of spinal motoneurons (By similarity).
CC   -!- SUBUNIT: Forms a heteromeric complex with ALS2CL. Interacts with
CC       ALS2CL (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q920R0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q920R0-2; Sequence=VSP_050525, VSP_050526;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 8 MORN repeats.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 5 RCC1 repeats.
CC   -!- SIMILARITY: Contains 1 VPS9 domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB053307; BAB69016.1; -; mRNA.
DR   EMBL; BC031479; AAH31479.1; -; mRNA.
DR   EMBL; BC046828; AAH46828.1; -; mRNA.
DR   EMBL; AK014320; BAB29271.2; -; mRNA.
DR   IPI; IPI00170364; -.
DR   IPI; IPI00309844; -.
DR   RefSeq; NP_001153420.2; NM_001159948.2.
DR   RefSeq; NP_082993.4; NM_028717.6.
DR   RefSeq; NP_666221.1; NM_146109.3.
DR   UniGene; Mm.272078; -.
DR   ProteinModelPortal; Q920R0; -.
DR   SMR; Q920R0; 15-216, 292-325, 503-680, 1041-1243.
DR   STRING; Q920R0; -.
DR   PhosphoSite; Q920R0; -.
DR   PRIDE; Q920R0; -.
DR   Ensembl; ENSMUST00000027178; ENSMUSP00000027178; ENSMUSG00000026024.
DR   GeneID; 74018; -.
DR   KEGG; mmu:74018; -.
DR   UCSC; uc007bdm.1; mouse.
DR   UCSC; uc007bdn.1; mouse.
DR   CTD; 74018; -.
DR   MGI; MGI:1921268; Als2.
DR   GeneTree; ENSGT00600000084242; -.
DR   HOGENOM; HBG446556; -.
DR   HOVERGEN; HBG037320; -.
DR   InParanoid; Q920R0; -.
DR   OrthoDB; EOG4FTVZP; -.
DR   NextBio; 339546; -.
DR   ArrayExpress; Q920R0; -.
DR   Bgee; Q920R0; -.
DR   Genevestigator; Q920R0; -.
DR   GermOnline; ENSMUSG00000026024; Mus musculus.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0043197; C:dendritic spine; IDA:MGI.
DR   GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR   GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0043234; C:protein complex; ISS:UniProtKB.
DR   GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISS:UniProtKB.
DR   GO; GO:0017137; F:Rab GTPase binding; ISS:UniProtKB.
DR   GO; GO:0017112; F:Rab guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0030676; F:Rac guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR   GO; GO:0016197; P:endosome transport; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0007528; P:neuromuscular junction development; IMP:MGI.
DR   GO; GO:0032855; P:positive regulation of Rac GTPase activity; ISS:UniProtKB.
DR   GO; GO:0008104; P:protein localization; IMP:MGI.
DR   GO; GO:0001881; P:receptor recycling; IMP:MGI.
DR   GO; GO:0051036; P:regulation of endosome size; ISS:UniProtKB.
DR   GO; GO:0032313; P:regulation of Rab GTPase activity; IDA:MGI.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR   GO; GO:0016050; P:vesicle organization; IDA:MGI.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR003409; MORN.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000408; Reg_chr_condens.
DR   InterPro; IPR009091; Reg_csome_cond/b-lactamase_inh.
DR   InterPro; IPR003123; VPS9.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:2.130.10.30; Reg_csome_cond/b-lactamase_inh; 2.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Pfam; PF02493; MORN; 7.
DR   Pfam; PF00415; RCC1; 4.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF02204; VPS9; 1.
DR   PRINTS; PR00633; RCCNDNSATION.
DR   SMART; SM00698; MORN; 8.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   SUPFAM; SSF50985; RCC1/BLIP-II; 2.
DR   PROSITE; PS00741; DH_1; FALSE_NEG.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
DR   PROSITE; PS00625; RCC1_1; FALSE_NEG.
DR   PROSITE; PS00626; RCC1_2; 2.
DR   PROSITE; PS50012; RCC1_3; 4.
DR   PROSITE; PS51205; VPS9; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing;
KW   Guanine-nucleotide releasing factor; Phosphoprotein; Repeat.
FT   CHAIN         1   1651       Alsin.
FT                                /FTId=PRO_0000080904.
FT   REPEAT       59    108       RCC1 1.
FT   REPEAT      109    167       RCC1 2.
FT   REPEAT      169    218       RCC1 3.
FT   REPEAT      519    570       RCC1 4.
FT   REPEAT      572    621       RCC1 5.
FT   DOMAIN      684    879       DH.
FT   DOMAIN      895   1001       PH.
FT   REPEAT     1043   1065       MORN 1.
FT   REPEAT     1066   1088       MORN 2.
FT   REPEAT     1094   1116       MORN 3.
FT   REPEAT     1117   1139       MORN 4.
FT   REPEAT     1145   1167       MORN 5.
FT   REPEAT     1169   1191       MORN 6.
FT   REPEAT     1192   1214       MORN 7.
FT   REPEAT     1215   1238       MORN 8.
FT   DOMAIN     1507   1651       VPS9.
FT   MOD_RES     477    477       Phosphoserine.
FT   MOD_RES     486    486       Phosphoserine.
FT   MOD_RES     527    527       N6-acetyllysine (By similarity).
FT   MOD_RES    1338   1338       Phosphothreonine (By similarity).
FT   MOD_RES    1458   1458       Phosphoserine (By similarity).
FT   VAR_SEQ     855    928       TSPEYQKLQDSSSCYESLALHLGKKRKEAEYTLSFWKTFPG
FT                                KMTDSLRKPERRLLCESSNRALSLQHAGRFSVN -> VGFV
FT                                CAPPNTREAKSQSSLFALSLLKMLGPGAGEMAQWVRAPDCS
FT                                SEGLEFKSQQPHGGSQPPVMRSDALFWSV (in isoform
FT                                2).
FT                                /FTId=VSP_050525.
FT   VAR_SEQ     929   1651       Missing (in isoform 2).
FT                                /FTId=VSP_050526.
FT   CONFLICT    318    318       I -> V (in Ref. 2; AAH46828).
FT   CONFLICT    469    469       S -> L (in Ref. 2; AAH46828).
FT   CONFLICT    764    764       V -> F (in Ref. 2; AAH46828).
FT   CONFLICT   1206   1206       V -> L (in Ref. 3; BAB29271).
FT   CONFLICT   1296   1296       R -> H (in Ref. 1; BAB69016).
FT   CONFLICT   1452   1452       S -> L (in Ref. 1; BAB69016).
SQ   SEQUENCE   1651 AA;  182554 MW;  D2D2E915AB016BE2 CRC64;
     MDSKKKSSTE AEGSKERGLV HVWQAGSFSL TPERLPGWGG KTVLQAALGV RHGVLLTEDG
     EVYSFGTLPW KSESAEICPS SPLLESALVG HHVITVATGS FHSGAVTESG VVYMWGENAA
     GQCAVANQQY VPEPSPVSIS DSETSPSLAV RILQLACGEE HTLALSLSRE IWAWGTGCQL
     GLITTTFPVT KPQKVEHLAG RVVLQVACGA FHSLALVQCL PPQDLKPVPE RCNQCSQLLI
     TMTDKEDHVI ISDSHCCPLG VTLSESQAEK HASPAPSPHP EALDEQGEVF ENTVVEAELN
     MGSSQTTSGS AISTQQNIVG TAEVSSARTA PSYPDTHAVT AYLQKLSEHS MRENHEPGEK
     PPQVQPLVEE AVPDLHSPPT TSTSALNSLV VSCASAVGVR VAATYEAGAL SLKKVMNFYS
     TAPCETAAQS GSASTGPESL KDLREEQVKQ ESLQGKKSSS LMDIREEESE GGSRRLSLPG
     LLSQVSPRLL RKAARVKTRT VVLTPTYSGE ADALLPSLRT EVWTWGKGKE GQLGHGDVLP
     RLQPLCVKCL DGKEVIHLEA GGSHSLALTA KSQVYSWGSN TFGQLGHSEF PTTVPRLSKV
     SSENGVWSVA AGQDYSLFLV DTEDFQPGLY YSGRQDRAEG DTLPENPSGT KTPVLLSCSK
     LGYISRVTAG KDSYLALVDK NIMGYIASLH ELASTERRFY SKLSEIKSQI LRPLLSLENL
     GTVTTVQLLQ EVASRFSKLC YLIGQHGASL SSYLQGMKEA SSLVIMKHSS LFLDSYTEYC
     TSVSNFLVMG GFQLLAKPAI DFLNKNQELL QDLSEVNDEN TQLMEILNML FFLPIRRLHN
     YAKVLLKLAT CFEVTSPEYQ KLQDSSSCYE SLALHLGKKR KEAEYTLSFW KTFPGKMTDS
     LRKPERRLLC ESSNRALSLQ HAGRFSVNWF ILFNDALVHA QFSTHHVFPL ATLWAEPLSE
     EAGSVNGLKI TTPEEQFTLI SSTPQEKTKW LRAISQAVDQ ALRGTSDFPL YGGGSSVQRQ
     EPPISRSAKY TFYKDTRLKD ATYDGRWLSG KPHGRGVLKW PDGKMYSGMF RNGLEDGYGE
     YRIPNKALNK EDHYVGHWKE GKMCGQGVYS YASGEVFEGC FQDNMRHGHG LLRSGKLTSS
     SPSMFIGQWV MDKKAGYGVF DDITRGEKYM GMWQDDVCQG NGVVVTQFGL YYEGNFHLNK
     MMGNGVLLSE DDTIYEGEFS DDWTLSGKGT LTMPHGDYIE GYFSGEWGSG IKITGTYFKP
     SLYESDKDKP KAFRKLGNLA VAADEKWRAV FEECWRQLGC ESPGQGEVWK AWDNIAVALT
     TNRRQHKDSP EILSRSQTQT LESLEYIPQH IGAFSVEKYD DIKKYLIKAC DTPLHPLGRL
     VETLVAVYRM TYVGVGANRR LLQEAVKEIK SYLKRIFQLV RFLFPELPEE GSTIPLSAPL
     PTGRRSFCTG KSDSRSESPE PGYVVTSSGL LLPVLLPRLY PPLFMLYALD NDREEDIYWE
     CVLRLNKQPD IALLGFLGVQ KKFWPATLSI LGESKKVLST TKDACFASAV ECLQQISTTF
     TPSDKLKVIQ QTFEEISQSV LASLQEDFLW SMDDLFPVFL YVVLRARIRN LGSEVHLIED
     LMDPFLQHGE QGIMFTTLKA CYFQIQREKL N
//
ID   CXG3_MOUSE              Reviewed;         269 AA.
AC   Q921C1; Q53ZP5; Q8BHJ3;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Gap junction gamma-3 protein;
DE   AltName: Full=Connexin-29;
DE            Short=Cx29;
DE   AltName: Full=Gap junction epsilon-1 protein;
GN   Name=Gjc3; Synonyms=Cx29, Gje1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   PubMed=16926269; DOI=10.1152/physiolgenomics.00284.2005;
RA   Wilson M.D., Cheung J., Martindale D.W., Scherer S.W., Koop B.F.;
RT   "Comparative analysis of the paired immunoglobulin-like receptor
RT   (PILR) locus in six mammalian genomes: duplication, conversion, and
RT   the birth of new genes.";
RL   Physiol. Genomics 27:201-218(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Corpora quadrigemina, and Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-269.
RX   MEDLINE=21392673; PubMed=11501764; DOI=10.1515/BC.2001.122;
RA   Soehl G., Eiberger J., Jung Y., Kozak C., Willecke K.;
RT   "The mouse gap junction gene Connexin29 is highly expressed in sciatic
RT   nerve and regulated during brain development.";
RL   Biol. Chem. 382:973-978(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 12-269.
RC   STRAIN=129/SvEv;
RX   MEDLINE=22146346; PubMed=12151525;
RA   Altevogt B.M., Kleopa K.A., Postma F.R., Scherer S.S., Paul D.L.;
RT   "Connexin29 is uniquely distributed within myelinating glial cells of
RT   the central and peripheral nervous systems.";
RL   J. Neurosci. 22:6458-6470(2002).
CC   -!- FUNCTION: One gap junction consists of a cluster of closely packed
CC       pairs of transmembrane channels, the connexons, through which
CC       materials of low MW diffuse from one cell to a neighboring cell
CC       (By similarity).
CC   -!- SUBUNIT: A connexon is composed of a hexamer of connexins (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity). Cell junction, gap junction (By similarity).
CC   -!- TISSUE SPECIFICITY: CNS specific. Expression is restricted to
CC       brain, spinal cord, and sciatic nerve.
CC   -!- SIMILARITY: Belongs to the connexin family. Gamma-type subfamily.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-12 is the initiator.
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DR   EMBL; AY823670; AAX39497.1; -; Genomic_DNA.
DR   EMBL; AY289210; AAP41202.1; -; mRNA.
DR   EMBL; AY293564; AAP50246.1; -; mRNA.
DR   EMBL; AY297108; AAP51160.1; -; mRNA.
DR   EMBL; AK034037; BAC28554.1; -; mRNA.
DR   EMBL; AK045577; BAC32421.1; -; mRNA.
DR   EMBL; AK047368; BAC33038.1; -; mRNA.
DR   EMBL; AK147913; BAE28224.1; -; mRNA.
DR   EMBL; CH466529; EDL19225.1; -; Genomic_DNA.
DR   EMBL; CH466529; EDL19226.1; -; Genomic_DNA.
DR   EMBL; BC125305; AAI25306.1; -; mRNA.
DR   EMBL; AJ297318; CAC29245.1; -; Genomic_DNA.
DR   EMBL; AF503616; AAM21146.1; -; Genomic_DNA.
DR   IPI; IPI00121653; -.
DR   RefSeq; NP_536698.2; NM_080450.4.
DR   UniGene; Mm.332771; -.
DR   UniGene; Mm.477152; -.
DR   ProteinModelPortal; Q921C1; -.
DR   SMR; Q921C1; 13-228.
DR   STRING; Q921C1; -.
DR   PhosphoSite; Q921C1; -.
DR   PRIDE; Q921C1; -.
DR   Ensembl; ENSMUST00000077119; ENSMUSP00000076367; ENSMUSG00000056966.
DR   GeneID; 118446; -.
DR   KEGG; mmu:118446; -.
DR   CTD; 118446; -.
DR   MGI; MGI:2153041; Gjc3.
DR   GeneTree; ENSGT00560000076845; -.
DR   HOGENOM; HBG717760; -.
DR   HOVERGEN; HBG107788; -.
DR   InParanoid; Q921C1; -.
DR   OMA; GDEQSEF; -.
DR   OrthoDB; EOG49CQ8J; -.
DR   PhylomeDB; Q921C1; -.
DR   ArrayExpress; Q921C1; -.
DR   Bgee; Q921C1; -.
DR   CleanEx; MM_GJE1; -.
DR   Genevestigator; Q921C1; -.
DR   GermOnline; ENSMUSG00000056966; Mus musculus.
DR   GO; GO:0005922; C:connexon complex; IEA:InterPro.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043209; C:myelin sheath; IDA:MGI.
DR   GO; GO:0042552; P:myelination; IMP:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR   InterPro; IPR000500; Connexin.
DR   InterPro; IPR019570; Connexin_CCC.
DR   InterPro; IPR017990; Connexin_CS.
DR   InterPro; IPR013092; Connexin_N.
DR   PANTHER; PTHR11984; Connexin; 1.
DR   Pfam; PF00029; Connexin; 1.
DR   Pfam; PF10582; Connexin_CCC; 1.
DR   PRINTS; PR00206; CONNEXIN.
DR   PROSITE; PS00407; CONNEXINS_1; 1.
DR   PROSITE; PS00408; CONNEXINS_2; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Gap junction; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    269       Gap junction gamma-3 protein.
FT                                /FTId=PRO_0000354706.
FT   TOPO_DOM      1     33       Extracellular (Potential).
FT   TRANSMEM     34     54       Helical; (Potential).
FT   TOPO_DOM     55     86       Cytoplasmic (Potential).
FT   TRANSMEM     87    107       Helical; (Potential).
FT   TOPO_DOM    108    145       Extracellular (Potential).
FT   TRANSMEM    146    166       Helical; (Potential).
FT   TOPO_DOM    167    205       Cytoplasmic (Potential).
FT   TRANSMEM    206    226       Helical; (Potential).
FT   TOPO_DOM    227    269       Extracellular (Potential).
SQ   SEQUENCE   269 AA;  30293 MW;  13D9FF9C25C85D6A CRC64;
     MLLLELPIKC RMCGRFLRQL LAQESQHSTP VGRFLLPMLM GFRLLILVSS GPGVFGNDEN
     EFICHLGQPG CKTICYDVFR PLSPLRFWAF QVILMAVPSA IYVAFTLYHV IGYWEVPGKE
     NKEQETQISK GDHSKDVSGA KSLKLLWAYV AHLGVRLALE GAALGVQYNL YGFKMSSTFI
     CREDPCIGST TCFQSHPSEK TIFLNIMFGI SGACFLFIFL ELALLGLGRF WRIYKHKLSF
     LKKLPTSESS VRSKDTTDEL SVVEAKEPF
//
ID   BRWD1_MOUSE             Reviewed;        2304 AA.
AC   Q921C3; Q921C2;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Bromodomain and WD repeat-containing protein 1;
DE   AltName: Full=WD repeat-containing protein 9;
GN   Name=Brwd1; Synonyms=Wdr9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RA   Scott H.S., Barras C., Mittaz L., Michaud J., Guidi S., Scamuffa N.,
RA   Antonarakis S.;
RT   "Isolation and characterization of a new chromosome 21 gene, WDR9,
RT   with different alternatively spliced transcripts and different protein
RT   forms.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   TISSUE SPECIFICITY.
RX   PubMed=12359327; DOI=10.1016/S0167-4781(02)00421-9;
RA   Ramos V.C., Vidal-Taboada J.M., Bergonon S., Egeo A., Fisher E.M.C.,
RA   Scartezzini P., Oliva R.;
RT   "Characterisation and expression analysis of the WDR9 gene, located in
RT   the Down critical region-2 of the human chromosome 21.";
RL   Biochim. Biophys. Acta 1577:377-383(2002).
RN   [3]
RP   DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, INTERACTION WITH SMARCA4,
RP   AND FUNCTION.
RX   PubMed=12889071; DOI=10.1002/dvdy.10344;
RA   Huang H., Rambaldi I., Daniels E., Featherstone M.;
RT   "Expression of the Wdr9 gene and protein products during mouse
RT   development.";
RL   Dev. Dyn. 227:608-614(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1830, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1782; SER-1784 AND
RP   SER-1789, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2040, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1751 AND SER-1752, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May be a transcriptional activator. May be involved in
CC       chromatin remodeling.
CC   -!- SUBUNIT: Interacts with SMARCA4.
CC   -!- INTERACTION:
CC       O35845:Smarca4; NbExp=1; IntAct=EBI-926536, EBI-371515;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A;
CC         IsoId=Q921C3-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=Q921C3-2; Sequence=VSP_018552, VSP_018553;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- DEVELOPMENTAL STAGE: Broadly expressed during development.
CC       Expression begins to increase at 7.5 dpc, peaks at 10.5-11.5 dpc,
CC       and decreases from 14.5 dpc. Weakly expressed at late embryonic
CC       stages.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Contains 2 bromo domains.
CC   -!- SIMILARITY: Contains 8 WD repeats.
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DR   EMBL; AJ292467; CAC44373.1; -; mRNA.
DR   EMBL; AJ292468; CAC44374.1; -; mRNA.
DR   IPI; IPI00121655; -.
DR   IPI; IPI00750042; -.
DR   RefSeq; NP_001096649.1; NM_001103179.1.
DR   RefSeq; NP_660107.2; NM_145125.3.
DR   UniGene; Mm.240871; -.
DR   ProteinModelPortal; Q921C3; -.
DR   SMR; Q921C3; 175-549, 1089-1264, 1320-1430.
DR   IntAct; Q921C3; 1.
DR   PhosphoSite; Q921C3; -.
DR   PRIDE; Q921C3; -.
DR   Ensembl; ENSMUST00000023631; ENSMUSP00000023631; ENSMUSG00000022914.
DR   GeneID; 93871; -.
DR   KEGG; mmu:93871; -.
DR   UCSC; uc008aci.2; mouse.
DR   UCSC; uc008ack.2; mouse.
DR   CTD; 93871; -.
DR   MGI; MGI:1890651; Brwd1.
DR   GeneTree; ENSGT00390000010788; -.
DR   HOGENOM; HBG444387; -.
DR   HOVERGEN; HBG080933; -.
DR   InParanoid; Q921C3; -.
DR   ArrayExpress; Q921C3; -.
DR   Bgee; Q921C3; -.
DR   CleanEx; MM_BRWD1; -.
DR   Genevestigator; Q921C3; -.
DR   GermOnline; ENSMUSG00000022914; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0030528; F:transcription regulator activity; IDA:MGI.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:1.20.920.10; Bromodomain; 2.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00439; Bromodomain; 2.
DR   Pfam; PF00400; WD40; 8.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 2.
DR   SMART; SM00320; WD40; 8.
DR   SUPFAM; SSF47370; Bromodomain; 2.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 2.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 6.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Bromodomain; Cytoplasm; Nucleus;
KW   Phosphoprotein; Repeat; Transcription; Transcription regulation;
KW   WD repeat.
FT   CHAIN         1   2304       Bromodomain and WD repeat-containing
FT                                protein 1.
FT                                /FTId=PRO_0000235986.
FT   REPEAT      184    223       WD 1.
FT   REPEAT      226    265       WD 2.
FT   REPEAT      268    311       WD 3.
FT   REPEAT      322    365       WD 4.
FT   REPEAT      366    405       WD 5.
FT   REPEAT      424    463       WD 6.
FT   REPEAT      466    506       WD 7.
FT   REPEAT      514    553       WD 8.
FT   DOMAIN     1178   1248       Bromo 1.
FT   DOMAIN     1332   1402       Bromo 2.
FT   COMPBIAS    661    668       Poly-Gln.
FT   COMPBIAS    817    867       Ser-rich.
FT   COMPBIAS   1454   1457       Poly-Arg.
FT   COMPBIAS   1479   1568       Ser-rich.
FT   MOD_RES     418    418       Phosphoserine (By similarity).
FT   MOD_RES     697    697       Phosphoserine (By similarity).
FT   MOD_RES     702    702       Phosphoserine (By similarity).
FT   MOD_RES     792    792       Phosphoserine (By similarity).
FT   MOD_RES    1276   1276       Phosphothreonine (By similarity).
FT   MOD_RES    1291   1291       Phosphoserine (By similarity).
FT   MOD_RES    1609   1609       Phosphoserine (By similarity).
FT   MOD_RES    1611   1611       Phosphoserine (By similarity).
FT   MOD_RES    1751   1751       Phosphoserine.
FT   MOD_RES    1752   1752       Phosphoserine.
FT   MOD_RES    1782   1782       Phosphoserine.
FT   MOD_RES    1784   1784       Phosphoserine.
FT   MOD_RES    1789   1789       Phosphoserine.
FT   MOD_RES    1830   1830       Phosphoserine.
FT   MOD_RES    1889   1889       Phosphoserine (By similarity).
FT   MOD_RES    1890   1890       Phosphoserine (By similarity).
FT   MOD_RES    2004   2004       Phosphoserine (By similarity).
FT   MOD_RES    2040   2040       Phosphoserine.
FT   VAR_SEQ    2179   2294       ESVRKDREPHTKMRPCMLNEKDAVQMHSDTLKAKTVPEKVP
FT                                RRCATVAANKIKMMCNLKEVVSGPENVGIRTISRKLPYRQA
FT                                SAAAKKKLLSVYKEDDAPIHSENEKELYLRRFRS -> GKP
FT                                SSSNSPKTARHPRQSKGPRLNVDDNDWEDLDYAKAKGVVRL
FT                                SKIQTRNQGRRTVRYHDGEDDRSIESALELTDRTLRP (in
FT                                isoform B).
FT                                /FTId=VSP_018552.
FT   VAR_SEQ    2295   2304       Missing (in isoform B).
FT                                /FTId=VSP_018553.
SQ   SEQUENCE   2304 AA;  259026 MW;  422ECDED832A529E CRC64;
     MAEPSPARRP VPLIESELYF LIARYLSAGP CRRAAQVLVQ ELEQYQLLPK RLDWEGNEHN
     RSYEELVLSN KHVAPDHLLQ ICQRIGPMLD KEVPPSKERG TSRLGAGRQS LLRTAKDCRH
     TVWKGSAFAA LHRGRPPEMP VNYGPPPSLV EIHRGRQLTG CSTFSTAFPG TMYQHIKMHR
     RILGHLSAVY CVAFDRTGHR IFTGSDDCLV KIWSTHNGRL LSTLRGHSAE ISDMAVNYEN
     TLIAAGSCDK VIRVWCLRTC APVAVLQGHT GSITSLQFSP MAKGPQRYMV STGADGTVCF
     WQWDLESLKF SPRPLKFTEK PRPGVQMLCS SFSVGGMFLA TGSTDHVIRM YFLGFDAPEK
     IAELESHTDK VDSIQFCNNG DRFLSGSRDG TARIWRFEQL EWRSILLDMS ARISGDTSSE
     EERFMKPKVT MIAWNQDDST VVTAVNDHVL KVWSSYTGQL LHNLLGHADE VFVLETHPFD
     SRIMLSAGHD GSIFIWDITK GIKMKHYFNM IEGQGHGAVF DCKFSQDGQH FACTDSHGHL
     LIFGFGCSKP YEKIPDQMFF HTDYRPLIRD SNNYVLDEQT QQAPHLMPPP FLVDVDGNPH
     PTKFQRLVPG RENSADEHLV PQLGYVATSD GEVIEQIISL HTNDSGDASP ESSVLDGMIR
     QLQQQQDQRL GVDQDGTANG LPSGEGTPRR GSFRRLSLDI QSPPNIGLRR SGQVEGVRQM
     HQNAPRSQIA TERDLQAWKR RVVVPEAPPG MFRRLEDIRI ERGEEERNLY VIGRKKKTFQ
     VPQKSNSMVL VSQSRQRTCR RKYANYSRRN ADQCELSSGN ESSGSVRHET SYDQSEGSCS
     SEDDEWRNDR RSGSDSDSSS DSSSQYSDWT ADTGINLQPP LRMSCRRRVT RFCSTSEDEM
     SMENISPPKR RRKRRKESKP KRESLRRMTP AELANMEHLY EFHPPVWITD TTLRKSPFVP
     QMGDEVIYFP QGHEAYIEAV RRNNIYELNP HKEPWGKMDL RDQELVKIVG LRYEVGPPTL
     LCLKLAFIDP ATGRLTDKSF SIRYHDMPDV IDLLVLRPFY DEARQRNWQP CDRFRSIIDD
     AWWFGTVLSQ DPYQPQYPDS HFQCYIVRWD NTETEKLSPW DMEPIPDNVD PPKELGASIS
     VTSDELEKLL YKPQEGEWGQ RSRDEECDRI ISGIDQLLNL DIAAAFAGPV DLCTYPKYCT
     VVAYPTDLYT IRMRLVNRFY RRLSALIWEV RYIEHNARTF NEPESVIARS AKKITDQLLK
     FIKNQDCTNI SELCNTSDND EDDSADDLDD SDLPKTSSGR RKVHNWKRRS RASGCIESDW
     RRQCKALLIL IFQCEDSEPF RQPVDLDEYP DYRDIIDTPM DFGTVRETLE AGNYDSPVEF
     CKDIRLIFSN AKAYTPNKRS KIYSMTLRLS ALFEEKMKKI SFDFKIGQKF KEKLRRSQRF
     KQRQNCNGAV PGDRRRRNVK QKQFKSQTKV IPQLMCPPSQ STSSKVPLSA TRKTSAGVSS
     GFTSGDSSDS AGSLERVRRQ RPEVLRSGSV LFGSEMEDFL ATSSSSSASN SSEESKASPG
     ARESSLRSGV LRGSNLGVTR TRAARRKAGS VSLENGCGRK ATRKRVYLSD SDNNSVETDE
     NLKNRKCGSS RKVLRKCAAV AASKIKLMSD AEDSSSESPC SGRKLPHRNA SAVARKKLLH
     NSDDQSLKSE TEELKDQNQS LLISGPHSVH NSISDSESDS DLRATRKTWN ANGCTSHTAA
     TCKTKSRPIE SSEEDSRCHG SDHGPSSTGD PSTSGQKLRA DSISEEADSE PESSVLCKNT
     HLCKKAKILS DSEDCEEKCG ERRGPEVEGS PVSEALREAI LAPQCLSHRG SETDVDSDGG
     AVREKSYSNE NGSVSLENGQ RRKVSRKSSS DKESNLQVTQ KSPKDRSSPS RITQRASVAT
     DKMKLTSDAE DLSLESVCTR SKRRRKKPAR FACTPAKTAL SSEEKHAHCE VPEAQPACRN
     KLPEPEHQDS AENPSQAASA DLNSGGGSSF EQRKSIQSRQ MGAVCVRPPP KTQSSSAGLS
     QENARSQTLD SETSLPSESV LTQKATVESN FEEELNYGLR RWNGRRLRTY GKAPLSRTAQ
     VTPSLQASAE VGVKRRRMHP EVDGEDVPGQ MGSSGCGPDT SPKASDLGSV TDSDVDCTDN
     TQTQRKKKRK GKARVLSKES VRKDREPHTK MRPCMLNEKD AVQMHSDTLK AKTVPEKVPR
     RCATVAANKI KMMCNLKEVV SGPENVGIRT ISRKLPYRQA SAAAKKKLLS VYKEDDAPIH
     SENEKELYLR RFRSRKEKAQ PTPR
//
ID   RAB31_MOUSE             Reviewed;         194 AA.
AC   Q921E2; Q8BKP0;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Ras-related protein Rab-31;
GN   Name=Rab31;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC34585.1; Type=Erroneous initiation;
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DR   EMBL; AK051270; BAC34585.1; ALT_INIT; mRNA.
DR   EMBL; BC013063; AAH13063.1; -; mRNA.
DR   IPI; IPI00222632; -.
DR   RefSeq; NP_598446.2; NM_133685.2.
DR   UniGene; Mm.29274; -.
DR   ProteinModelPortal; Q921E2; -.
DR   SMR; Q921E2; 3-167.
DR   STRING; Q921E2; -.
DR   PhosphoSite; Q921E2; -.
DR   PRIDE; Q921E2; -.
DR   Ensembl; ENSMUST00000070673; ENSMUSP00000068195; ENSMUSG00000056515.
DR   GeneID; 106572; -.
DR   KEGG; mmu:106572; -.
DR   UCSC; uc008dgh.1; mouse.
DR   CTD; 106572; -.
DR   MGI; MGI:1914603; Rab31.
DR   GeneTree; ENSGT00550000074186; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; Q921E2; -.
DR   OMA; MMAIREL; -.
DR   OrthoDB; EOG48KRC8; -.
DR   PhylomeDB; Q921E2; -.
DR   NextBio; 358266; -.
DR   ArrayExpress; Q921E2; -.
DR   Bgee; Q921E2; -.
DR   CleanEx; MM_RAB31; -.
DR   Genevestigator; Q921E2; -.
DR   GermOnline; ENSMUSG00000056515; Mus musculus.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; GTP-binding; Lipoprotein; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Prenylation.
FT   CHAIN         1    194       Ras-related protein Rab-31.
FT                                /FTId=PRO_0000121233.
FT   NP_BIND      12     19       GTP (By similarity).
FT   NP_BIND      60     64       GTP (By similarity).
FT   NP_BIND     118    121       GTP (By similarity).
FT   MOTIF        34     42       Effector region (By similarity).
FT   MOD_RES      35     35       Phosphoserine.
FT   LIPID       193    193       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   LIPID       194    194       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   CONFLICT     49     49       C -> W (in Ref. 1; BAC34585).
SQ   SEQUENCE   194 AA;  21331 MW;  4EBCAF6E2431AD02 CRC64;
     MAIRELKVCL LGDTGVGKSS IVCRFVQDHF DHNISPTIGA SFMTKTVPCG NELHKFLIWD
     TAGQERFHSL APMYYRGSAA AVIVYDITKQ DSFHTLKKWV KELKEHGPEN IVMAIAGNKC
     DLSDIREVPL KDAKEYAESI GAIVVETSAK NAINIEELFQ GISRQIPPLG PQENGNSGGI
     KLGNQSLQAS RRCC
//
ID   TADBP_MOUSE             Reviewed;         414 AA.
AC   Q921F2; Q3U591; Q3V0E7;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-FEB-2011, entry version 81.
DE   RecName: Full=TAR DNA-binding protein 43;
DE            Short=TDP-43;
GN   Name=Tardbp; Synonyms=Tdp43;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 276-293, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 192-265 IN COMPLEX WITH
RP   SINGLE-STRANDED DNA, AND SUBUNIT.
RX   PubMed=19174564; DOI=10.1093/nar/gkp013;
RA   Kuo P.H., Doudeva L.G., Wang Y.T., Shen C.K., Yuan H.S.;
RT   "Structural insights into TDP-43 in nucleic-acid binding and domain
RT   interactions.";
RL   Nucleic Acids Res. 37:1799-1808(2009).
CC   -!- FUNCTION: DNA and RNA-binding protein which regulates
CC       transcription and splicing. Involved in the regulation of CFTR
CC       splicing. It promotes CFTR exon 9 skipping by binding to the UG
CC       repeated motifs in the polymorphic region near the 3'-splice site
CC       of this exon. The resulting aberrant splicing is associated with
CC       pathological features typical of cystic fibrosis. May also be
CC       involved in microRNA biogenesis, apoptosis and cell division (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer. Binds specifically to pyrimidine-rich motifs
CC       of TAR DNA and to single stranded TG repeated sequences. Binds to
CC       RNA, specifically to UG repeated sequences with a minimun of six
CC       contiguous repeats.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- DOMAIN: The RRM domains can bind to both DNA and RNA.
CC   -!- PTM: Hyperphosphorylated (By similarity).
CC   -!- PTM: Ubiquitinated (By similarity).
CC   -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK133207; BAE21557.1; -; mRNA.
DR   EMBL; AK153803; BAE32189.1; -; mRNA.
DR   EMBL; BC012873; AAH12873.1; -; mRNA.
DR   EMBL; BC025544; AAH25544.1; -; mRNA.
DR   EMBL; BC027772; AAH27772.1; -; mRNA.
DR   EMBL; BC031126; AAH31126.1; -; mRNA.
DR   EMBL; BC033475; AAH33475.1; -; mRNA.
DR   IPI; IPI00121758; -.
DR   RefSeq; NP_663531.1; NM_145556.4.
DR   UniGene; Mm.22453; -.
DR   UniGene; Mm.378962; -.
DR   PDB; 3D2W; X-ray; 1.65 A; A=192-265.
DR   PDBsum; 3D2W; -.
DR   ProteinModelPortal; Q921F2; -.
DR   SMR; Q921F2; 90-264.
DR   STRING; Q921F2; -.
DR   PhosphoSite; Q921F2; -.
DR   REPRODUCTION-2DPAGE; Q921F2; -.
DR   PRIDE; Q921F2; -.
DR   Ensembl; ENSMUST00000045180; ENSMUSP00000038113; ENSMUSG00000041459.
DR   GeneID; 230908; -.
DR   KEGG; mmu:230908; -.
DR   UCSC; uc008vvg.1; mouse.
DR   CTD; 230908; -.
DR   MGI; MGI:2387629; Tardbp.
DR   GeneTree; ENSGT00570000079202; -.
DR   HOGENOM; HBG379398; -.
DR   HOVERGEN; HBG058671; -.
DR   InParanoid; Q921F2; -.
DR   OMA; FFSQYGE; -.
DR   PhylomeDB; Q921F2; -.
DR   NextBio; 380280; -.
DR   ArrayExpress; Q921F2; -.
DR   Bgee; Q921F2; -.
DR   CleanEx; MM_TARDBP; -.
DR   Genevestigator; Q921F2; -.
DR   GermOnline; ENSMUSG00000041459; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; DNA-binding; mRNA processing;
KW   mRNA splicing; Nucleus; Phosphoprotein; Repeat; Repressor;
KW   RNA-binding; Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN         1    414       TAR DNA-binding protein 43.
FT                                /FTId=PRO_0000081973.
FT   DOMAIN      104    200       RRM 1.
FT   DOMAIN      191    262       RRM 2.
FT   COMPBIAS    274    413       Gly-rich.
FT   MOD_RES      91     91       Phosphoserine (By similarity).
FT   MOD_RES      92     92       Phosphoserine (By similarity).
FT   CONFLICT      8      8       T -> K (in Ref. 1; BAE32189).
FT   CONFLICT     96     96       V -> G (in Ref. 1; BAE32189).
FT   CONFLICT    298    298       G -> C (in Ref. 1; BAE21557).
FT   STRAND      192    195
FT   HELIX       204    211
FT   STRAND      217    221
FT   STRAND      228    235
FT   HELIX       237    243
FT   STRAND      247    249
FT   STRAND      254    256
SQ   SEQUENCE   414 AA;  44548 MW;  2BE6A695EC2CA106 CRC64;
     MSEYIRVTED ENDEPIEIPS EDDGTVLLST VTAQFPGACG LRYRNPVSQC MRGVRLVEGI
     LHAPDAGWGN LVYVVNYPKD NKRKMDETDA SSAVKVKRAV QKTSDLIVLG LPWKTTEQDL
     KDYFSTFGEV LMVQVKKDLK TGHSKGFGFV RFTEYETQVK VMSQRHMIDG RWCDCKLPNS
     KQSPDEPLRS RKVFVGRCTE DMTAEELQQF FCQYGEVVDV FIPKPFRAFA FVTFADDKVA
     QSLCGEDLII KGISVHISNA EPKHNSNRQL ERSGRFGGNP GGFGNQGGFG NSRGGGAGLG
     NNQGGNMGGG MNFGAFSINP AMMAAAQAAL QSSWGMMGML ASQQNQSGPS GNNQSQGSMQ
     REPNQAFGSG NNSYSGSNSG APLGWGSASN AGSGSGFNGG FGSSMDSKSS GWGM
//
ID   HNRLL_MOUSE             Reviewed;         591 AA.
AC   Q921F4; Q3UIK6; Q6IR44; Q8BIP6; Q91W02; Q99J40;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 3.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Heterogeneous nuclear ribonucleoprotein L-like;
GN   Name=Hnrpll;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Embryonic heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J, and Czech II;
RC   TISSUE=Embryonic germ cell, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 (ISOFORM 3), AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   FUNCTION, MUTAGENESIS OF VAL-136, INDUCTION, AND STRUCTURE BY NMR OF
RP   RRM 1.
RX   PubMed=19100700; DOI=10.1016/j.immuni.2008.11.004;
RA   Wu Z., Jia X., de la Cruz L., Su X.-C., Marzolf B., Troisch P.,
RA   Zak D., Hamilton A., Whittle B., Yu D., Sheahan D., Bertram E.,
RA   Aderem A., Otting G., Goodnow C.C., Hoyne G.F.;
RT   "Memory T cell RNA rearrangement programmed by heterogeneous nuclear
RT   ribonucleoprotein hnRNPLL.";
RL   Immunity 29:863-875(2008).
RN   [5]
RP   STRUCTURE BY NMR OF 119-316.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of RNA binding domains in heterogeneous nuclear
RT   ribonucleoprotein L-like.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- FUNCTION: RNA-binding protein that functions as regulator of
CC       alternative splicing for multiple target mRNAs, including
CC       PTPRC/CD45 and STAT5A. Required for alternative splicing of PTPRC.
CC   -!- SUBUNIT: Interacts with HNRNPL (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q921F4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q921F4-4; Sequence=VSP_013290, VSP_013291;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q921F4-5; Sequence=VSP_026132, VSP_026133;
CC         Note=Contains a phosphoserine at position 64;
CC   -!- INDUCTION: Up-regulated in stimulated T-cells.
CC   -!- PTM: Isoform 3 is phosphorylated at 'Ser-64'.
CC   -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE27500.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK034860; BAC28858.1; -; mRNA.
DR   EMBL; AK146879; BAE27500.1; ALT_INIT; mRNA.
DR   EMBL; BC004763; AAH04763.1; -; mRNA.
DR   EMBL; BC012849; AAH12849.2; -; mRNA.
DR   EMBL; BC071184; AAH71184.1; -; mRNA.
DR   IPI; IPI00121760; -.
DR   IPI; IPI00463538; -.
DR   IPI; IPI00555009; -.
DR   RefSeq; NP_659051.3; NM_144802.3.
DR   UniGene; Mm.64579; -.
DR   PDB; 1WEX; NMR; -; A=117-204.
DR   PDB; 2E5I; NMR; -; A=200-316.
DR   PDBsum; 1WEX; -.
DR   PDBsum; 2E5I; -.
DR   ProteinModelPortal; Q921F4; -.
DR   SMR; Q921F4; 118-316, 379-589.
DR   STRING; Q921F4; -.
DR   PhosphoSite; Q921F4; -.
DR   PRIDE; Q921F4; -.
DR   Ensembl; ENSMUST00000061331; ENSMUSP00000058308; ENSMUSG00000024095.
DR   GeneID; 72692; -.
DR   KEGG; mmu:72692; -.
DR   UCSC; uc008dqk.1; mouse.
DR   CTD; 72692; -.
DR   MGI; MGI:1919942; Hnrpll.
DR   HOGENOM; HBG320095; -.
DR   HOVERGEN; HBG105786; -.
DR   InParanoid; Q921F4; -.
DR   OMA; HDGYGSH; -.
DR   OrthoDB; EOG49S662; -.
DR   NextBio; 336749; -.
DR   ArrayExpress; Q921F4; -.
DR   Bgee; Q921F4; -.
DR   CleanEx; MM_HNRPLL; -.
DR   Genevestigator; Q921F4; -.
DR   GermOnline; ENSMUSG00000024095; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR   GO; GO:0033120; P:positive regulation of RNA splicing; ISS:UniProtKB.
DR   InterPro; IPR006536; HnRNP-L_PTB.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 4.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 3.
DR   TIGRFAMs; TIGR01649; hnRNP-L_PTB; 1.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Phosphoprotein; Repeat;
KW   Ribonucleoprotein; RNA-binding.
FT   CHAIN         1    591       Heterogeneous nuclear ribonucleoprotein
FT                                L-like.
FT                                /FTId=PRO_0000081610.
FT   DOMAIN      125    199       RRM 1.
FT   DOMAIN      215    293       RRM 2.
FT   DOMAIN      384    458       RRM 3.
FT   COMPBIAS      2      8       Poly-Ser.
FT   COMPBIAS     58    116       Gly-rich.
FT   VAR_SEQ       1    480       Missing (in isoform 3).
FT                                /FTId=VSP_026132.
FT   VAR_SEQ     317    326       DRGKGRQRQA -> GRYFTNFRMY (in isoform 2).
FT                                /FTId=VSP_013290.
FT   VAR_SEQ     327    591       Missing (in isoform 2).
FT                                /FTId=VSP_013291.
FT   VAR_SEQ     522    591       LCNDHEVLPFIKYKVFDAKASAKTLSGLLEWKCKTDAVEAL
FT                                TALNHYQIRVPNGSNPYTLKLCFSTSSHL -> VGTEESSV
FT                                RMLRFVFYVYVVFHSSASFENFSKILLFVVSLVWVCVRRAY
FT                                RLVVLDGFLC (in isoform 3).
FT                                /FTId=VSP_026133.
FT   MUTAGEN     136    136       V->D: Alters RRM 1 stability. Abolishes
FT                                regulation of alternative splicing.
FT   CONFLICT      4      4       S -> T (in Ref. 2; AAH12849).
FT   CONFLICT    101    101       S -> SGGG (in Ref. 2; AAH12849).
FT   STRAND      125    131
FT   HELIX       138    145
FT   TURN        146    148
FT   STRAND      151    157
FT   TURN        158    161
FT   STRAND      162    169
FT   HELIX       170    182
FT   STRAND      186    191
FT   STRAND      193    196
FT   STRAND      198    201
FT   STRAND      216    224
FT   HELIX       231    238
FT   TURN        239    241
FT   STRAND      244    263
FT   HELIX       264    274
FT   STRAND      283    289
FT   STRAND      302    309
SQ   SEQUENCE   591 AA;  64125 MW;  431C0167DF619FB7 CRC64;
     MSSSSSSSPK EETYEEDREF ESQAKRLKTE EGEIVYSAEE SENRQEATPQ AGSDSDSGGG
     DGGDGDGGSG GGGDGEEGEG GEEGDEGDGD EGGSGGDEGG SGGGPRSMPL STEGGGSHHK
     VSVSPVVHVR GLCESVVEAD LVEALEKFGT ICYVMMMPFK RQALVEFENI DSAKECVTFA
     ADVPVYIAGQ QAFFNYSTSK RITRPGNTDD PSGGNKVLLL SIQNPLYPIT VDVLYTVCNP
     VGKVQRIVIF KRNGIQAMVE FESVLCAQKA KAALNGADIY AGCCTLKIEY ARPTRLNVIR
     NDNDSWDYTK PYLGRRDRGK GRQRQAILGD HPSSFRHDGY GSHGPLLPLP SRYRMGSRDT
     PELVAYPLPQ ASSSYMHGGS PSGSVVMVSG LHQLKMNCSR VFNLFCLYGN IEKVKFMKTI
     PGTALVEMGD EYAVERAVTH LNNVKLFGKR LNVCVSKQHS VVPSQIFELE DGTSSYKDFA
     MSKNNRFTSA GQASKNIIQP PSCVLHYYNV PLCVTEETFT KLCNDHEVLP FIKYKVFDAK
     ASAKTLSGLL EWKCKTDAVE ALTALNHYQI RVPNGSNPYT LKLCFSTSSH L
//
ID   ETFD_MOUSE              Reviewed;         616 AA.
AC   Q921G7; Q3U7K2; Q8BK82; Q9DCT9;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial;
DE            Short=ETF-QO;
DE            Short=ETF-ubiquinone oxidoreductase;
DE            EC=1.5.5.1;
DE   AltName: Full=Electron-transferring-flavoprotein dehydrogenase;
DE            Short=ETF dehydrogenase;
DE   Flags: Precursor;
GN   Name=Etfdh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Kidney, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 212-222, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-95; LYS-152; LYS-222 AND
RP   LYS-343, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- FUNCTION: Accepts electrons from ETF and reduces ubiquinone (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Reduced electron-transferring flavoprotein +
CC       ubiquinone = electron-transferring flavoprotein + ubiquinol.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster (By similarity).
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane (By
CC       similarity).
CC   -!- PTM: Acetylation of Lys-95 and Lys-222 is observed in liver
CC       mitochondria from fasted mice but not from fed mice.
CC   -!- SIMILARITY: Belongs to the ETF-QO/fixC family.
CC   -!- SIMILARITY: Contains 1 4Fe-4S ferredoxin-type domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK002483; BAB22135.1; -; mRNA.
DR   EMBL; AK075673; BAC35888.1; -; mRNA.
DR   EMBL; AK141684; BAE24798.1; -; mRNA.
DR   EMBL; AK152624; BAE31367.1; -; mRNA.
DR   EMBL; AK169686; BAE41304.1; -; mRNA.
DR   EMBL; BC012522; AAH12522.1; -; mRNA.
DR   IPI; IPI00121322; -.
DR   RefSeq; NP_080070.2; NM_025794.2.
DR   UniGene; Mm.28336; -.
DR   ProteinModelPortal; Q921G7; -.
DR   SMR; Q921G7; 38-616.
DR   STRING; Q921G7; -.
DR   PhosphoSite; Q921G7; -.
DR   PRIDE; Q921G7; -.
DR   Ensembl; ENSMUST00000029386; ENSMUSP00000029386; ENSMUSG00000027809.
DR   GeneID; 66841; -.
DR   KEGG; mmu:66841; -.
DR   CTD; 66841; -.
DR   MGI; MGI:106100; Etfdh.
DR   eggNOG; roNOG12984; -.
DR   GeneTree; ENSGT00390000010773; -.
DR   HOGENOM; HBG291987; -.
DR   HOVERGEN; HBG005615; -.
DR   InParanoid; Q921G7; -.
DR   OMA; IFYWILR; -.
DR   OrthoDB; EOG42RD6T; -.
DR   PhylomeDB; Q921G7; -.
DR   BRENDA; 1.5.5.1; 244.
DR   NextBio; 322795; -.
DR   ArrayExpress; Q921G7; -.
DR   Bgee; Q921G7; -.
DR   CleanEx; MM_ETFDH; -.
DR   Genevestigator; Q921G7; -.
DR   GermOnline; ENSMUSG00000027809; Mus musculus.
DR   GO; GO:0017133; C:mitochondrial electron transfer flavoprotein complex; TAS:MGI.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; ISS:UniProtKB.
DR   GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043783; F:oxidoreductase activity, oxidizing metal ions with flavin as acceptor; ISS:UniProtKB.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR007859; ETFD_OxRdtase.
DR   InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2.
DR   Pfam; PF05187; ETF_QO; 1.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Acetylation; Direct protein sequencing; Electron transport;
KW   FAD; Flavoprotein; Iron; Iron-sulfur; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
KW   Transit peptide; Transport; Ubiquinone.
FT   TRANSIT       1     32       Mitochondrion (Potential).
FT   CHAIN        33    616       Electron transfer flavoprotein-ubiquinone
FT                                oxidoreductase, mitochondrial.
FT                                /FTId=PRO_0000008662.
FT   INTRAMEM    108    129       By similarity.
FT   INTRAMEM    427    446       By similarity.
FT   DOMAIN      576    605       4Fe-4S ferredoxin-type.
FT   NP_BIND      70     84       FAD (Potential).
FT   METAL       560    560       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       585    585       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       588    588       Iron-sulfur (4Fe-4S) (Potential).
FT   METAL       591    591       Iron-sulfur (4Fe-4S) (Potential).
FT   BINDING     304    304       Ubiquinone; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     305    305       Ubiquinone; via amide nitrogen (By
FT                                similarity).
FT   MOD_RES      95     95       N6-acetyllysine.
FT   MOD_RES     152    152       N6-acetyllysine.
FT   MOD_RES     222    222       N6-acetyllysine.
FT   MOD_RES     343    343       N6-acetyllysine.
FT   CONFLICT    342    342       W -> C (in Ref. 1; BAB22135).
FT   CONFLICT    355    355       G -> W (in Ref. 1; BAC35888).
SQ   SEQUENCE   616 AA;  68091 MW;  1E5C6F85725E3CEE CRC64;
     MLVRLTKLSC PAYHWFHALK IKKCLPLCAP RCSSTSAVPQ ITTHYTVHPR EKDKRWEGVN
     MERFAEEADV VIVGAGPAGL SAAIRLKQLA AEQGKDIRVC LVEKAAQIGA HTLSGACLDP
     AAFKELFPDW KEKGAPLNTP VTEDRFAILT EKHRIPVPIL PGLPMNNHGN YIVRLGHLVS
     WMGEQAEALG VEVYPGYAAA EVLYHEDGSV KGIATNDVGI QKDGAPKTTF ERGLELHAKV
     TVFAEGCHGH LAKQLYKKFD LRASCDAQTY GIGLKELWII DEKKWKPGRV DHTVGWPLDR
     HTYGGSFLYH LNEGEPLVAV GFVVGLDYQN PYLSPFREFQ RWKHHPSIQP TLEGGKRIAY
     GARALNEGGL QSIPKLTFPG GLLIGCSPGF MNVPKIKGTH TAMKSGSLAA ESIFKQLTSE
     NLQSKTTGLH VTEYEDNLKQ SWVWKELHAV RNIRPSCHGI LGVYGGMIYT GIFYWILRGM
     EPWTLKHKGS DSDQLKPAKD CTPIEYPKPD GQISFDLLSS VALSGTNHEH DQPAHLTLKD
     DSIPVNRNLS IYDGPEQRFC PAGVYEFVPL EQGDGFRLQI NAQNCVHCKT CDIKDPSQNI
     NWVVPEGGGG PAYNGM
//
ID   TRFE_MOUSE              Reviewed;         697 AA.
AC   Q921I1; O35421; Q3UBW7; Q58E69; Q61803; Q62357; Q62358; Q62359;
AC   Q63915; Q64515; Q8VII5; Q922C0;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 100.
DE   RecName: Full=Serotransferrin;
DE            Short=Transferrin;
DE   AltName: Full=Beta-1 metal-binding globulin;
DE   AltName: Full=Siderophilin;
DE   Flags: Precursor;
GN   Name=Tf; Synonyms=Trf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Liver;
RA   Lai D.-Z.;
RT   "Construction of a robust CHO cell-line for biopharmaceutical
RT   production.";
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Amnion, Bone marrow, Liver, and Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RC   STRAIN=BALB/c;
RX   MEDLINE=98284323; PubMed=9621303;
RX   DOI=10.1002/(SICI)1098-2795(199807)50:3<273::AID-MRD3>3.3.CO;2-C;
RA   Chaudhary J., Skinner M.K.;
RT   "Comparative sequence analysis of the mouse and human transferrin
RT   promoters: hormonal regulation of the transferrin promoter in Sertoli
RT   cells.";
RL   Mol. Reprod. Dev. 50:273-283(1998).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 66-131; 277-337; 462-496 AND 526-575.
RX   MEDLINE=88086992; PubMed=3693348;
RA   Chen L.-H., Bissell M.J.;
RT   "Transferrin mRNA level in the mouse mammary gland is regulated by
RT   pregnancy and extracellular matrix.";
RL   J. Biol. Chem. 262:17247-17250(1987).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 268-307.
RC   TISSUE=Placenta;
RX   MEDLINE=94068311; PubMed=8248032; DOI=10.1016/S0143-4004(05)80458-8;
RA   Kasik J.W., Rice E.J.;
RT   "Transferrin gene expression in maternal liver, fetal liver and
RT   placenta during pregnancy in the mouse.";
RL   Placenta 14:365-371(1993).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 282-412.
RX   MEDLINE=87280033; PubMed=3611056;
RA   Pentecost B.T., Teng C.T.;
RT   "Lactotransferrin is the major estrogen inducible protein of mouse
RT   uterine secretions.";
RL   J. Biol. Chem. 262:10134-10139(1987).
RN   [8]
RP   PROTEIN SEQUENCE OF 332-343 AND 659-667, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [9]
RP   TISSUE SPECIFICITY.
RX   PubMed=2601714;
RA   Idzerda R.L., Behringer R.R., Theisen M., Huggenvik J.I.,
RA   McKnight G.S., Brinster R.L.;
RT   "Expression from the transferrin gene promoter in transgenic mice.";
RL   Mol. Cell. Biol. 9:5154-5162(1989).
RN   [10]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-513, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Plasma;
RX   PubMed=17330941; DOI=10.1021/pr0604559;
RA   Bernhard O.K., Kapp E.A., Simpson R.J.;
RT   "Enhanced analysis of the mouse plasma proteome using cysteine-
RT   containing tryptic glycopeptides.";
RL   J. Proteome Res. 6:987-995(2007).
CC   -!- FUNCTION: Transferrins are iron binding transport proteins which
CC       can bind two Fe(3+) ions in association with the binding of an
CC       anion, usually bicarbonate. It is responsible for the transport of
CC       iron from sites of absorption and heme degradation to those of
CC       storage and utilization. Serum transferrin may also have a further
CC       role in stimulating cell proliferation.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
CC   -!- SIMILARITY: Belongs to the transferrin family.
CC   -!- SIMILARITY: Contains 2 transferrin-like domains.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF440692; AAL34533.1; -; mRNA.
DR   EMBL; AK085754; BAC39532.1; -; mRNA.
DR   EMBL; AK142599; BAE25124.1; -; mRNA.
DR   EMBL; AK146549; BAE27253.1; -; mRNA.
DR   EMBL; AK149559; BAE28960.1; -; mRNA.
DR   EMBL; AK149595; BAE28981.1; -; mRNA.
DR   EMBL; AK150782; BAE29847.1; -; mRNA.
DR   EMBL; AK168419; BAE40332.1; -; mRNA.
DR   EMBL; AK168938; BAE40747.1; -; mRNA.
DR   EMBL; BC008559; AAH08559.1; -; mRNA.
DR   EMBL; BC012313; AAH12313.1; -; mRNA.
DR   EMBL; BC022986; AAH22986.1; -; mRNA.
DR   EMBL; BC092046; AAH92046.1; -; mRNA.
DR   EMBL; AF027336; AAB84034.1; -; Genomic_DNA.
DR   EMBL; M23013; AAA40488.1; -; mRNA.
DR   EMBL; M23014; AAA40489.1; -; mRNA.
DR   EMBL; M23015; AAA40490.1; -; mRNA.
DR   EMBL; M23016; AAA40491.1; -; mRNA.
DR   EMBL; S67217; AAB28966.2; -; mRNA.
DR   EMBL; J03299; AAA39438.1; -; mRNA.
DR   IPI; IPI00139788; -.
DR   PIR; A28446; A28446.
DR   RefSeq; NP_598738.1; NM_133977.2.
DR   UniGene; Mm.37214; -.
DR   ProteinModelPortal; Q921I1; -.
DR   SMR; Q921I1; 22-697.
DR   IntAct; Q921I1; 2.
DR   MINT; MINT-1202663; -.
DR   STRING; Q921I1; -.
DR   MEROPS; S60.972; -.
DR   PhosphoSite; Q921I1; -.
DR   REPRODUCTION-2DPAGE; IPI00139788; -.
DR   REPRODUCTION-2DPAGE; Q921I1; -.
DR   PRIDE; Q921I1; -.
DR   Ensembl; ENSMUST00000035158; ENSMUSP00000035158; ENSMUSG00000032554.
DR   Ensembl; ENSMUST00000112645; ENSMUSP00000108264; ENSMUSG00000032554.
DR   GeneID; 22041; -.
DR   KEGG; mmu:22041; -.
DR   UCSC; uc009rgi.1; mouse.
DR   CTD; 22041; -.
DR   MGI; MGI:98821; Trf.
DR   eggNOG; roNOG10662; -.
DR   GeneTree; ENSGT00390000001619; -.
DR   HOVERGEN; HBG000055; -.
DR   InParanoid; Q921I1; -.
DR   OMA; AETTEDC; -.
DR   OrthoDB; EOG4CRKZG; -.
DR   PhylomeDB; Q921I1; -.
DR   NextBio; 301824; -.
DR   ArrayExpress; Q921I1; -.
DR   Bgee; Q921I1; -.
DR   CleanEx; MM_TRF; -.
DR   Genevestigator; Q921I1; -.
DR   GermOnline; ENSMUSG00000032554; Mus musculus.
DR   GO; GO:0030139; C:endocytic vesicle; IDA:MGI.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0055037; C:recycling endosome; IDA:MGI.
DR   GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; IEA:InterPro.
DR   GO; GO:0006826; P:iron ion transport; IMP:MGI.
DR   GO; GO:0060395; P:SMAD protein signal transduction; IDA:MGI.
DR   InterPro; IPR001156; Peptidase_S60.
DR   InterPro; IPR016357; Transferrin.
DR   InterPro; IPR018195; Transferrin_Fe_BS.
DR   PANTHER; PTHR11485; Peptidase_S60; 1.
DR   Pfam; PF00405; Transferrin; 2.
DR   PIRSF; PIRSF002549; Transferrin; 1.
DR   PRINTS; PR00422; TRANSFERRIN.
DR   SMART; SM00094; TR_FER; 2.
DR   PROSITE; PS00205; TRANSFERRIN_LIKE_1; 1.
DR   PROSITE; PS00206; TRANSFERRIN_LIKE_2; 2.
DR   PROSITE; PS00207; TRANSFERRIN_LIKE_3; 2.
DR   PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Ion transport; Iron; Iron transport; Metal-binding; Methylation;
KW   Phosphoprotein; Repeat; Secreted; Signal; Transport.
FT   SIGNAL        1     19       By similarity.
FT   CHAIN        20    697       Serotransferrin.
FT                                /FTId=PRO_0000035716.
FT   DOMAIN       25    347       Transferrin-like 1.
FT   DOMAIN      360    682       Transferrin-like 2.
FT   METAL        82     82       Iron 1 (By similarity).
FT   METAL       114    114       Iron 1 (By similarity).
FT   METAL       207    207       Iron 1 (By similarity).
FT   METAL       268    268       Iron 1 (By similarity).
FT   METAL       410    410       Iron 2 (By similarity).
FT   METAL       448    448       Iron 2 (By similarity).
FT   METAL       537    537       Iron 2 (By similarity).
FT   METAL       605    605       Iron 2 (By similarity).
FT   BINDING     139    139       Carbonate 1 (By similarity).
FT   BINDING     143    143       Carbonate 1 (By similarity).
FT   BINDING     145    145       Carbonate 1; via amide nitrogen (By
FT                                similarity).
FT   BINDING     146    146       Carbonate 1; via amide nitrogen (By
FT                                similarity).
FT   BINDING     474    474       Carbonate 2 (By similarity).
FT   BINDING     478    478       Carbonate 2 (By similarity).
FT   BINDING     480    480       Carbonate 2; via amide nitrogen (By
FT                                similarity).
FT   BINDING     481    481       Carbonate 2; via amide nitrogen (By
FT                                similarity).
FT   MOD_RES      42     42       Omega-N-methylated arginine (By
FT                                similarity).
FT   MOD_RES     537    537       Phosphotyrosine (By similarity).
FT   CARBOHYD    513    513       N-linked (GlcNAc...).
FT   DISULFID     28     67       By similarity.
FT   DISULFID     38     58       By similarity.
FT   DISULFID    137    213       By similarity.
FT   DISULFID    156    350       By similarity.
FT   DISULFID    177    193       By similarity.
FT   DISULFID    180    196       By similarity.
FT   DISULFID    190    198       By similarity.
FT   DISULFID    246    260       By similarity.
FT   DISULFID    363    395       By similarity.
FT   DISULFID    373    386       By similarity.
FT   DISULFID    420    692       By similarity.
FT   DISULFID    435    655       By similarity.
FT   DISULFID    472    543       By similarity.
FT   DISULFID    496    683       By similarity.
FT   DISULFID    506    520       By similarity.
FT   DISULFID    517    526       By similarity.
FT   DISULFID    583    597       By similarity.
FT   DISULFID    633    638       By similarity.
FT   CONFLICT      3      4       LT -> FA (in Ref. 1; AAL34533).
FT   CONFLICT     69     69       K -> R (in Ref. 5; AAA40488).
FT   CONFLICT     71     74       ISAS -> HASG (in Ref. 3; AAH08559).
FT   CONFLICT     72     72       S -> A (in Ref. 5; AAA40488).
FT   CONFLICT     85     85       W -> L (in Ref. 5; AAA40488).
FT   CONFLICT    104    104       Y -> C (in Ref. 5; AAA40488).
FT   CONFLICT    113    113       Y -> S (in Ref. 5; AAA40488).
FT   CONFLICT    123    124       GT -> ER (in Ref. 5; AAA40488).
FT   CONFLICT    135    135       K -> E (in Ref. 2; BAE29847).
FT   CONFLICT    283    283       W -> L (in Ref. 6; AAB28966).
FT   CONFLICT    307    307       P -> L (in Ref. 6; AAB28966).
FT   CONFLICT    350    351       CP -> SA (in Ref. 7; AAA39438).
FT   CONFLICT    487    487       G -> C (in Ref. 5; AAA40490).
FT   CONFLICT    527    527       A -> D (in Ref. 5; AAA40491).
FT   CONFLICT    529    529       N -> S (in Ref. 2; BAE29847).
FT   CONFLICT    575    575       K -> N (in Ref. 5; AAA40491).
FT   CONFLICT    697    697       H -> S (in Ref. 1; AAL34533).
SQ   SEQUENCE   697 AA;  76724 MW;  0996A0C3B64CB1B9 CRC64;
     MRLTVGALLA CAALGLCLAV PDKTVKWCAV SEHENTKCIS FRDHMKTVLP PDGPRLACVK
     KTSYPDCIKA ISASEADAMT LDGGWVYDAG LTPNNLKPVA AEFYGSVEHP QTYYYAVAVV
     KKGTDFQLNQ LEGKKSCHTG LGRSAGWVIP IGLLFCKLSE PRSPLEKAVS SFFSGSCVPC
     ADPVAFPKLC QLCPGCGCSS TQPFFGYVGA FKCLKDGGGD VAFVKHTTIF EVLPEKADRD
     QYELLCLDNT RKPVDQYEDC YLARIPSHAV VARKNNGKED LIWEILKVAQ EHFGKGKSKD
     FQLFSSPLGK DLLFKDSAFG LLRVPPRMDY RLYLGHNYVT AIRNQQEGVC PEGSIDNSPV
     KWCALSHLER TKCDEWSIIS EGKIECESAE TTEDCIEKIV NGEADAMTLD GGHAYIAGQC
     GLVPVMAEYY ESSNCAIPSQ QGIFPKGYYA VAVVKASDTS ITWNNLKGKK SCHTGVDRTA
     GWNIPMGMLY NRINHCKFDE FFSQGCAPGY EKNSTLCDLC IGPLKCAPNN KEEYNGYTGA
     FRCLVEKGDV AFVKHQTVLD NTEGKNPAEW AKNLKQEDFE LLCPDGTRKP VKDFASCHLA
     QAPNHVVVSR KEKAARVKAV LTSQETLFGG SDCTGNFCLF KSTTKDLLFR DDTKCFVKLP
     EGTTPEKYLG AEYMQSVGNM RKCSTSRLLE ACTFHKH
//
ID   SH3B4_MOUSE             Reviewed;         962 AA.
AC   Q921I6; Q8BXV5; Q8BY95; Q8C007;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=SH3 domain-binding protein 4;
GN   Name=Sh3bp4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Skin, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Functions in transferrin receptor internalization at the
CC       plasma membrane through a cargo-specific control of clathrin-
CC       mediated endocytosis (By similarity).
CC   -!- SUBUNIT: Homodimer or homooligomer. Interacts with DNM2, EPS15,
CC       clathrin, the adapter protein complex 2/AP-2 and TFRC (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit (By
CC       similarity). Cytoplasmic vesicle, clathrin-coated vesicle (By
CC       similarity). Nucleus (By similarity). Note=Specifically associated
CC       with transferrin receptor-containing clathrin-coated pits and
CC       clathrin-coated vesicles. May also localize to the nucleus (By
CC       similarity).
CC   -!- DOMAIN: The SH3 domain mediates localization to the clathrin-
CC       coated pits and vesicles. The SH3 domain mediates interaction with
CC       DNM2 and the cytoplasmic part of TFRC with a lower affinity (By
CC       similarity).
CC   -!- PTM: Phosphorylated upon EGF stimulation. Phosphorylation prevents
CC       interaction with DNM2 (By similarity).
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK028826; BAC26140.1; -; mRNA.
DR   EMBL; AK032634; BAC27961.1; -; mRNA.
DR   EMBL; AK041504; BAC30966.1; -; mRNA.
DR   EMBL; AK043259; BAC31506.1; -; mRNA.
DR   EMBL; BC012284; AAH12284.1; -; mRNA.
DR   EMBL; BC034733; AAH34733.1; -; mRNA.
DR   IPI; IPI00405836; -.
DR   RefSeq; NP_598577.1; NM_133816.2.
DR   UniGene; Mm.170983; -.
DR   HSSP; P08631; 1BU1.
DR   ProteinModelPortal; Q921I6; -.
DR   SMR; Q921I6; 29-115.
DR   PhosphoSite; Q921I6; -.
DR   PRIDE; Q921I6; -.
DR   Ensembl; ENSMUST00000066279; ENSMUSP00000067581; ENSMUSG00000036206.
DR   GeneID; 98402; -.
DR   KEGG; mmu:98402; -.
DR   UCSC; uc007byv.1; mouse.
DR   CTD; 98402; -.
DR   MGI; MGI:2138297; Sh3bp4.
DR   eggNOG; roNOG06321; -.
DR   GeneTree; ENSGT00390000013151; -.
DR   HOGENOM; HBG444428; -.
DR   HOVERGEN; HBG057439; -.
DR   InParanoid; Q921I6; -.
DR   OMA; CRAELDS; -.
DR   OrthoDB; EOG4M0F10; -.
DR   PhylomeDB; Q921I6; -.
DR   NextBio; 353456; -.
DR   ArrayExpress; Q921I6; -.
DR   Bgee; Q921I6; -.
DR   CleanEx; MM_SH3BP4; -.
DR   Genevestigator; Q921I6; -.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005905; C:coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR000906; ZU5.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   Pfam; PF00791; ZU5; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   Coated pit; Cytoplasmic vesicle; Endocytosis; Membrane; Nucleus;
KW   Phosphoprotein; SH3 domain.
FT   CHAIN         1    962       SH3 domain-binding protein 4.
FT                                /FTId=PRO_0000274575.
FT   DOMAIN       55    114       SH3.
FT   MOD_RES     131    131       Phosphoserine (By similarity).
FT   MOD_RES     245    245       Phosphoserine (By similarity).
FT   MOD_RES     636    636       Phosphoserine (By similarity).
FT   CONFLICT    312    312       Q -> K (in Ref. 1; BAC30966).
FT   CONFLICT    340    340       V -> E (in Ref. 1; BAC27961).
FT   CONFLICT    534    534       Q -> K (in Ref. 1; BAC27961).
SQ   SEQUENCE   962 AA;  107584 MW;  11154849455F4063 CRC64;
     MAAQRIRAAN ASGLPRCKSE GTLIDLSEGF SETSFNDVKV PSPSALLVDN PTPFGNAKEV
     IAIKDYCPNN FTTLKFSKGD HLYVLDTSGG EWWYAHNTTE MGYIPSSYVQ PLNYRNSTLS
     DSGMIDNLPD SPEEVAKELD LLGGGWTDDQ KESGRPYSNN PFWNGVRTNP FLNGNAQPST
     DELNPKSTVD LLLFDTGTSS FTESSSATTN STGNIFDELP ATNGLQVEQP VKRDNPFFRS
     KRSYSLSELS VLQAKSDAPP TSSFFTGLKS PVPEQFQSRE DFRTAWLNHR KLARSCHDLD
     LLGQSPGWGQ TQAVETNIVC KLDSSGGSVQ LPDTNISIHV PEGHVAPGET QQISMKALLD
     PPLDLNSDRS TSVSPVVEVK LSNLEVSTFI ILEMKVSAEV KGDIFSKSTV VLQCLRSDSK
     EGPYVPIPLA YSYGDTIQVQ LDNLEPCMYL AIVAQGPNIL YPSTVWDFIN KRVTVGLYGP
     KHIHPSFKTV VTIFGHDCAP KTLLVSEVTR QAPSPAPVAL QLWGKHQFIL SRPQDLRVCM
     FSNMTNYEVK ANEQARVVRG FQMKLGKVSR LIFSVISQNP NELSDFTLRV QVKDDQDTIL
     TQFCVQTPQP PPKSAIKPSG QRRFLKKNEV GKIILSPFVV TTKYPTFQDR PVSSLKFGKL
     LKTVVRQNKS HYLLEYKKGD VVALLSEERI RLKGQLWTKE WYIGYYQGKV GLVHTKNVLV
     VGKARPSLFS GPELSTSVLL EQILRPCKFL TYIYASVRTL LMENISSWRA FADALGYGNL
     PLTFFCRAEL DSEPERVASV LEKLKEDCNN PDNKDRKSFQ KELVMALLKM DCQGLVVRLI
     QDFVLLTTAV EVAQRWRELA EKLAKVSKQQ MDAYESPHRD RNGVVDSEAM WKPAYDFLLT
     WSHQIGDSYR DVIQELHIGL DKMKNPITRR WKHLTGTLIL VNSLDILRAA AFSPADHDDF
     VI
//
ID   BCL7B_MOUSE             Reviewed;         202 AA.
AC   Q921K9; O89022; Q3TV31; Q3U2W0;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=B-cell CLL/lymphoma 7 protein family member B;
GN   Name=Bcl7b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=99132633; PubMed=9931421; DOI=10.1016/S0378-1119(98)00514-9;
RA   Jadayel D.M., Osborne L.R., Coignet L.J.A., Zani V.J., Tsui L.-C.,
RA   Scherer S.W., Dyer M.J.S.;
RT   "The BCL7 gene family: deletion of BCL7B in Williams syndrome.";
RL   Gene 224:35-44(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION.
RX   PubMed=14647414; DOI=10.1038/sj.onc.1207234;
RA   Bonner A.E., Lemon W.J., Devereux T.R., Lubet R.A., You M.;
RT   "Molecular profiling of mouse lung tumors: association with tumor
RT   progression, lung development, and human lung adenocarcinomas.";
RL   Oncogene 23:1166-1176(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND SER-122, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May play a role in lung tumor development or
CC       progression.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q921K9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q921K9-2; Sequence=VSP_019280, VSP_019281;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the BCL7 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA09501.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ011145; CAA09501.1; ALT_INIT; mRNA.
DR   EMBL; AK131643; BAE20736.1; -; mRNA.
DR   EMBL; AK155076; BAE33030.1; -; mRNA.
DR   EMBL; AK160439; BAE35789.1; -; mRNA.
DR   EMBL; BC011471; AAH11471.1; -; mRNA.
DR   IPI; IPI00121944; -.
DR   IPI; IPI00760066; -.
DR   RefSeq; NP_033875.2; NM_009745.2.
DR   UniGene; Mm.405834; -.
DR   ProteinModelPortal; Q921K9; -.
DR   STRING; Q921K9; -.
DR   PhosphoSite; Q921K9; -.
DR   PRIDE; Q921K9; -.
DR   Ensembl; ENSMUST00000031692; ENSMUSP00000031692; ENSMUSG00000029681.
DR   Ensembl; ENSMUST00000111187; ENSMUSP00000106818; ENSMUSG00000029681.
DR   GeneID; 12054; -.
DR   KEGG; mmu:12054; -.
DR   UCSC; uc008zxw.1; mouse.
DR   CTD; 12054; -.
DR   MGI; MGI:1332238; Bcl7b.
DR   eggNOG; roNOG15698; -.
DR   GeneTree; ENSGT00390000002172; -.
DR   HOGENOM; HBG715533; -.
DR   HOVERGEN; HBG008481; -.
DR   InParanoid; Q921K9; -.
DR   OMA; VRKXKEK; -.
DR   OrthoDB; EOG45757S; -.
DR   PhylomeDB; Q921K9; -.
DR   NextBio; 280355; -.
DR   ArrayExpress; Q921K9; -.
DR   Bgee; Q921K9; -.
DR   CleanEx; MM_BCL7B; -.
DR   Genevestigator; Q921K9; -.
DR   GermOnline; ENSMUSG00000029681; Mus musculus.
DR   InterPro; IPR006804; BCL_N.
DR   PANTHER; PTHR12767; BCL_N; 1.
DR   Pfam; PF04714; BCL_N; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    202       B-cell CLL/lymphoma 7 protein family
FT                                member B.
FT                                /FTId=PRO_0000239830.
FT   MOD_RES     114    114       Phosphoserine (By similarity).
FT   MOD_RES     118    118       Phosphoserine.
FT   MOD_RES     122    122       Phosphoserine.
FT   VAR_SEQ      57     58       KE -> GF (in isoform 2).
FT                                /FTId=VSP_019280.
FT   VAR_SEQ      59    202       Missing (in isoform 2).
FT                                /FTId=VSP_019281.
FT   CONFLICT     24     24       A -> D (in Ref. 2; BAE33030).
FT   CONFLICT    192    192       Q -> K (in Ref. 2; BAE33030).
SQ   SEQUENCE   202 AA;  22238 MW;  B5976CFF00AB3CC3 CRC64;
     MSGRSVRAET RSRAKDDIKK VMAAIEKVRK WEKKWVTVGD TSLRIFKWVP VTDSKEKEKS
     KSNNTAAREP NGFPSDASAN SSLLLEFQDE NSNQSSVSDV YQLKVDSSTN SSPSPQQSES
     LSPAHTSDFR TDDSQPPTLG QEILEEPSLP ASEVADEPPT LTKEEPVPVE TQTTEEEEDS
     GAPPLKRFCV DQPVVPQTTS ES
//
ID   FA49B_MOUSE             Reviewed;         324 AA.
AC   Q921M7;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Protein FAM49B;
GN   Name=Fam49b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the FAM49 family.
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DR   EMBL; AK028062; BAC25731.1; -; mRNA.
DR   EMBL; AK075613; BAC35858.1; -; mRNA.
DR   EMBL; BC011343; AAH11343.1; -; mRNA.
DR   IPI; IPI00122015; -.
DR   RefSeq; NP_659095.1; NM_144846.5.
DR   UniGene; Mm.246108; -.
DR   ProteinModelPortal; Q921M7; -.
DR   PRIDE; Q921M7; -.
DR   Ensembl; ENSMUST00000063838; ENSMUSP00000066359; ENSMUSG00000022378.
DR   GeneID; 223601; -.
DR   KEGG; mmu:223601; -.
DR   UCSC; uc007vze.1; mouse.
DR   CTD; 223601; -.
DR   MGI; MGI:1923520; Fam49b.
DR   eggNOG; roNOG13331; -.
DR   GeneTree; ENSGT00390000015159; -.
DR   HOGENOM; HBG713695; -.
DR   HOVERGEN; HBG057586; -.
DR   InParanoid; Q921M7; -.
DR   OMA; DELQAYK; -.
DR   OrthoDB; EOG451DR3; -.
DR   PhylomeDB; Q921M7; -.
DR   NextBio; 376751; -.
DR   ArrayExpress; Q921M7; -.
DR   Bgee; Q921M7; -.
DR   CleanEx; MM_0910001A06RIK; -.
DR   Genevestigator; Q921M7; -.
DR   GermOnline; ENSMUSG00000022378; Mus musculus.
DR   InterPro; IPR009828; DUF1394.
DR   PANTHER; PTHR12422; DUF1394; 1.
PE   2: Evidence at transcript level;
FT   CHAIN         1    324       Protein FAM49B.
FT                                /FTId=PRO_0000187061.
SQ   SEQUENCE   324 AA;  36776 MW;  EE370E3D003A6E38 CRC64;
     MGNLLKVLTC TDLEQGPNFF LDFENAQPTE SEKEIYNQVN VVLKDAEGIL EDLQSYRGAG
     HEIREAIQHP ADEKLQEKAW GAVVPLVGKL KKFYEFSQRL EAALRGLLGA LTSTPYSPTQ
     HLEREQALAK QFAEILHFTL RFDELKMTNP AIQNDFSYYR RTLSRMRINN VPAEGENEVN
     NELANRMSLF YAEATPMLKT LSDATTKFVS ENKNLPIENT TDCLSTMASV CRVMLETPEY
     RSRFTNEETV SFCLRVMVGV IILYDHVHPV GAFAKTSKID MKGCIKVLKD QPPNSVEGLL
     NALRYTTKHL NDETTSKQIR SMLQ
//
ID   RIN1_MOUSE              Reviewed;         763 AA.
AC   Q921Q7;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Ras and Rab interactor 1;
DE   AltName: Full=Ras interaction/interference protein 1;
GN   Name=Rin1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   MEDLINE=22462230; PubMed=12574403;
RA   Dhaka A., Costa R.M., Hu H., Irvin D.K., Patel A., Kornblum H.I.,
RA   Silva A.J., O'Dell T.J., Colicelli J.;
RT   "The RAS effector RIN1 modulates the formation of aversive memories.";
RL   J. Neurosci. 23:748-757(2003).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-35, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-35, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Ras effector protein, which may serve as an inhibitory
CC       modulator of neuronal plasticity in aversive memory formation. Can
CC       affect Ras signaling at different levels. First, by competing with
CC       RAF1 protein for binding to activated Ras. Second, by enhancing
CC       signaling from ABL1 and ABL2, which regulate cytoskeletal
CC       remodeling. Third, by activating RAB5A, possibly by functioning as
CC       a guanine nucleotide exchange factor (GEF) for RAB5A, by
CC       exchanging bound GDP for free GTP, and facilitating Ras-activated
CC       receptor endocytosis (By similarity).
CC   -!- SUBUNIT: Interacts with the GTP-bound form of Ras proteins (NRAS,
CC       HRAS and KRAS). This interaction prevents the association between
CC       RAF1 and Ras. Interacts with 14-3-3 proteins YWHAB, YWHAE and
CC       YWHAZ when phosphorylated on Ser-340. Interacts with the SH3
CC       domain of ABL1 and ABL2. Interacts with RAB5A. The interaction
CC       with Ras is probably regulated and antagonized by the interaction
CC       with 14-3-3 proteins. The interaction with 14-3-3 proteins is
CC       regulated by phosphorylation on Ser-340 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane (By
CC       similarity). Cytoplasm, cytoskeleton (By similarity). Note=Some
CC       amount is membrane-associated (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain. Weakly or no
CC       expressed in other tissues, except in testis, where it is
CC       expressed at intermediate level. In brain, it is mainly expressed
CC       in postnatal forebrain neurons in which it is localized in
CC       dendrites and colocalizes with Ras.
CC   -!- PTM: Phosphorylated on tyrosine residues by ABL1 and ABL2.
CC       Phosphorylated on Ser-340 by PKD (By similarity).
CC   -!- SIMILARITY: Belongs to the RIN (Ras interaction/interference)
CC       family.
CC   -!- SIMILARITY: Contains 1 Ras-associating domain.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
CC   -!- SIMILARITY: Contains 1 VPS9 domain.
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DR   EMBL; BC011277; AAH11277.1; -; mRNA.
DR   IPI; IPI00122131; -.
DR   RefSeq; NP_663470.1; NM_145495.2.
DR   UniGene; Mm.271922; -.
DR   ProteinModelPortal; Q921Q7; -.
DR   SMR; Q921Q7; 64-149.
DR   DIP; DIP-46280N; -.
DR   STRING; Q921Q7; -.
DR   PhosphoSite; Q921Q7; -.
DR   PRIDE; Q921Q7; -.
DR   Ensembl; ENSMUST00000025818; ENSMUSP00000025818; ENSMUSG00000024883.
DR   GeneID; 225870; -.
DR   KEGG; mmu:225870; -.
DR   UCSC; uc008gca.1; mouse.
DR   CTD; 225870; -.
DR   MGI; MGI:2385695; Rin1.
DR   eggNOG; maNOG09128; -.
DR   GeneTree; ENSGT00530000063053; -.
DR   HOGENOM; HBG445303; -.
DR   HOVERGEN; HBG036105; -.
DR   InParanoid; Q921Q7; -.
DR   OMA; CATKFRV; -.
DR   OrthoDB; EOG4Z0B5B; -.
DR   PhylomeDB; Q921Q7; -.
DR   NextBio; 377829; -.
DR   ArrayExpress; Q921Q7; -.
DR   Bgee; Q921Q7; -.
DR   CleanEx; MM_RIN1; -.
DR   Genevestigator; Q921Q7; -.
DR   GermOnline; ENSMUSG00000024883; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR000159; Ras-assoc.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR003123; VPS9.
DR   InterPro; IPR013995; VPS9_sub.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF02204; VPS9; 1.
DR   SMART; SM00314; RA; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00167; VPS9; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50001; SH2; FALSE_NEG.
DR   PROSITE; PS51205; VPS9; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Endocytosis; GTPase activation; Membrane;
KW   Phosphoprotein; SH2 domain.
FT   CHAIN         1    763       Ras and Rab interactor 1.
FT                                /FTId=PRO_0000191318.
FT   DOMAIN       68    151       SH2.
FT   DOMAIN      445    587       VPS9.
FT   DOMAIN      613    695       Ras-associating.
FT   COMPBIAS    247    256       Pro-rich.
FT   COMPBIAS    402    601       Leu-rich.
FT   MOD_RES      35     35       Phosphotyrosine.
FT   MOD_RES     198    198       Phosphoserine (By similarity).
FT   MOD_RES     239    239       Phosphothreonine (By similarity).
FT   MOD_RES     246    246       Phosphoserine (By similarity).
FT   MOD_RES     319    319       Phosphoserine (By similarity).
FT   MOD_RES     323    323       Phosphoserine (By similarity).
FT   MOD_RES     340    340       Phosphoserine; by PKD (By similarity).
FT   MOD_RES     590    590       Phosphoserine.
FT   MOD_RES     598    598       Phosphoserine (By similarity).
FT   MOD_RES     621    621       Phosphotyrosine (By similarity).
SQ   SEQUENCE   763 AA;  83014 MW;  0CE76F66A4773438 CRC64;
     MEDPGETGAH PLGATNLNFV PGHQQKEKPS TDPLYDTPDT RGVQAGGSQQ PARTVSLRER
     LLITRPVWLQ LRANAAAALH VLRTEPPGTF LVRKSNTRQC QALCVRLPEA SGPSFVSSHY
     IEESTGGVSL EGSELMFQDL VQLICGYCRT RAIHQAATHK ELEAISHLGM EFWSSSLNTK
     DQQRPSEAPP IPRLKARSPQ ELDQGTGAAL CFFNPLFPGD LGPTKREKFK RSFKVRVSTE
     TSSPLSPPAV PPPPVPVLPG TSSSQTERLP PRQLLQRESS VGYRVPGSAA SPCLPPLPSL
     QEVDCCSPSS SEEEGSSGSP TTSPRLSRPR HRRPLLRSMS SAFCSLLAPE RQVGRAATML
     MQNRYTAVGQ LVQDLLTQVR AGPEPRELQG IRQALSRARA MLSAELGPEK LLPPERLELV
     LEKSLHRSVL KPLRPILAAR LRRRLSADGS LGRLAEGFRL ARTQGPGAFG SHLTLSSPVE
     TEQVRQKLLQ LLRAYSPSAQ VKWLLQACKL LYTALKSQAG ENAGADEFLP LLSLVLAQCD
     LPDLLLEAEY MSELLEPTLL TGEGGYYLTS LSASLALLSG LSQARALPLS PAQELQRSLA
     LWEQRRLPAT HSFQHLLRVA YQDPSTGCTS KTLAVPPGSS IATLSQLCAT KFRVTQPDAF
     GLFLYKDQGY HRLPPEALAH RLPATGYLIY RRAERPETQG AVAEKAKTGS KGPEAGAWEE
     ETGGLNREGK PRIAVDQEGK DQARGGHIGP EEQKAEGSQA LEE
//
ID   TOIP1_MOUSE             Reviewed;         520 AA.
AC   Q921T2; Q3U7A4;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-FEB-2011, entry version 62.
DE   RecName: Full=Torsin-1A-interacting protein 1;
DE   AltName: Full=Lamina-associated polypeptide 1B;
GN   Name=Tor1aip1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 108-520.
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Possible role in membrane attachment and assembly of the
CC       nuclear lamina (By similarity).
CC   -!- SUBUNIT: Binds to A- and B-type lamins. Interacts with ATP1B4 and
CC       TOR1A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus inner membrane; Single-pass membrane
CC       protein (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the TOR1AIP family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE31466.1; Type=Erroneous initiation;
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DR   EMBL; BC010841; AAH10841.1; -; mRNA.
DR   EMBL; AK152751; BAE31466.1; ALT_INIT; mRNA.
DR   IPI; IPI00122215; -.
DR   RefSeq; NP_001153490.1; NM_001160018.1.
DR   RefSeq; NP_001153491.1; NM_001160019.1.
DR   RefSeq; NP_659040.2; NM_144791.2.
DR   UniGene; Mm.211654; -.
DR   STRING; Q921T2; -.
DR   PhosphoSite; Q921T2; -.
DR   PRIDE; Q921T2; -.
DR   Ensembl; ENSMUST00000027738; ENSMUSP00000027738; ENSMUSG00000026466.
DR   GeneID; 208263; -.
DR   KEGG; mmu:208263; -.
DR   UCSC; uc007dbu.1; mouse.
DR   CTD; 208263; -.
DR   MGI; MGI:3582693; Tor1aip1.
DR   eggNOG; roNOG13648; -.
DR   GeneTree; ENSGT00390000012166; -.
DR   HOVERGEN; HBG083152; -.
DR   NextBio; 372239; -.
DR   ArrayExpress; Q921T2; -.
DR   Bgee; Q921T2; -.
DR   CleanEx; MM_TOR1AIP1; -.
DR   Genevestigator; Q921T2; -.
DR   GermOnline; ENSMUSG00000026466; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR008662; Lamina-ass_polypeptide_CLAP1C.
DR   Pfam; PF05609; LAP1C; 2.
PE   1: Evidence at protein level;
KW   Coiled coil; Membrane; Nucleus; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    520       Torsin-1A-interacting protein 1.
FT                                /FTId=PRO_0000228836.
FT   TOPO_DOM      1    276       Nuclear (Potential).
FT   TRANSMEM    277    297       Helical; (Potential).
FT   TOPO_DOM    298    520       Lumenal (Potential).
FT   COILED      298    325       Potential.
FT   COMPBIAS     22    129       Arg-rich.
FT   MOD_RES      60     60       Phosphoserine.
FT   MOD_RES     134    134       Phosphoserine (By similarity).
FT   MOD_RES     140    140       Phosphoserine (By similarity).
FT   MOD_RES     151    151       Phosphoserine.
FT   MOD_RES     153    153       Phosphoserine (By similarity).
FT   MOD_RES     154    154       Phosphoserine (By similarity).
FT   MOD_RES     164    164       Phosphoserine (By similarity).
FT   MOD_RES     165    165       Phosphoserine (By similarity).
FT   MOD_RES     170    170       Phosphoserine (By similarity).
FT   MOD_RES     235    235       Phosphothreonine (By similarity).
FT   MOD_RES     241    241       Phosphoserine (By similarity).
FT   CONFLICT    108    108       S -> A (in Ref. 2).
FT   CONFLICT    254    254       N -> D (in Ref. 2; BAE31466).
FT   CONFLICT    260    260       E -> DQDFPAHENQPLLLTSGCQENPQEWVDRAVRMRSRM
FT                                AYNNIQKSNFGNQSPSTSRPQ (in Ref. 2;
FT                                BAE31466).
SQ   SEQUENCE   520 AA;  58415 MW;  C1CAAB63DBEF0B90 CRC64;
     MAGERWQAEG PGEGWAIYVT PRAPIREGRR RLDPRNGDSS DAPAYGAHPS RRGRREVRFS
     EEPAEVYGDF EPRAAKERSP GGRRTPPEKF RPASAGEEVR ESAYNLRSRP RRQRRAQEAE
     EMKTRRSARL EQHSQQPQLS PATSGRGLRD SPSSSEDREE DEPSSRPVTS QTASKKTLRT
     PEASVMNEDP ISNLCRPPLR SPRLDSTYQT NGNTKTNERE ATIVQQVNFF EEGETEDDLE
     SSYSDITIRA RSSNSLESRE SAIHHPNEPS VKIKWWLLGL VAILAVGLFW FFHTPAVETT
     AVQEFQNQMK QLQSKYQSQN EKLWKRGTTF LEKHLNSSLP RPQPAILLLT AAQDAAEVLK
     CLSEQIADAY SSFRSVRAIR IDGAGKAAQD SDLVKHEVDQ ELTDGFKNGQ NAAVVHRFES
     LPAGSTLIFY KYCDHENAAF KDVALVLTVL LEEKTLEASL GLKEIEEKVR DFLKVKFTSS
     STASSYNHMD PDKLNGLWSR ISHLVLPVQP ENTLKAGSCL
//
ID   TRAF7_MOUSE             Reviewed;         594 AA.
AC   Q922B6; Q99JV3;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=E3 ubiquitin-protein ligase TRAF7;
DE            EC=6.3.2.-;
DE   AltName: Full=TNF receptor-associated factor 7;
GN   Name=Traf7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-15, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: E3 ubiquitin ligase capable of auto-ubiquitination,
CC       following phosphorylation by MAP3K3. Potentiates MEKK3-mediated
CC       activation of the NF-kappa-B, JUN/AP1 and DDIT3 transcriptional
CC       regulators. Induces apoptosis when overexpressed (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Homodimer. Interacts with MAP3K3 and promotes the kinase
CC       activity of this enzyme (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle (By similarity).
CC       Note=Colocalizes with MAP3K3 to vesicle-like structures throughout
CC       the cytoplasm (By similarity).
CC   -!- PTM: Phosphorylated by MAP3K3 (By similarity).
CC   -!- PTM: Ubiquitinates itself upon phosphorylation (By similarity).
CC   -!- SIMILARITY: Belongs to the WD repeat TRAF7 family.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SIMILARITY: Contains 1 TRAF-type zinc finger.
CC   -!- SIMILARITY: Contains 7 WD repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC005649; AAH05649.1; -; mRNA.
DR   EMBL; BC008598; AAH08598.1; -; mRNA.
DR   IPI; IPI00474463; -.
DR   UniGene; Mm.275150; -.
DR   ProteinModelPortal; Q922B6; -.
DR   SMR; Q922B6; 42-207, 299-593.
DR   STRING; Q922B6; -.
DR   PRIDE; Q922B6; -.
DR   Ensembl; ENSMUST00000088464; ENSMUSP00000085812; ENSMUSG00000052752.
DR   NMPDR; fig|10090.3.peg.2321; -.
DR   UCSC; uc008awq.1; mouse.
DR   MGI; MGI:3042141; Traf7.
DR   GeneTree; ENSGT00550000074285; -.
DR   HOVERGEN; HBG055270; -.
DR   NextBio; 377255; -.
DR   ArrayExpress; Q922B6; -.
DR   Bgee; Q922B6; -.
DR   CleanEx; MM_TRAF7; -.
DR   Genevestigator; Q922B6; -.
DR   GermOnline; ENSMUSG00000052752; Mus musculus.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0000151; C:ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000185; P:activation of MAPKKK activity; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0042981; P:regulation of apoptosis; ISS:UniProtKB.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR013323; SIAH-type.
DR   InterPro; IPR008974; TRAF-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   InterPro; IPR001293; Znf_TRAF.
DR   Gene3D; G3DSA:3.90.890.10; SIAH-type; 1.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00400; WD40; 7.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF49599; Traf_like; 2.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 5.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS50145; ZF_TRAF; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Cytoplasmic vesicle; Ligase; Metal-binding; Phosphoprotein;
KW   Repeat; Transcription; Transcription regulation; Ubl conjugation;
KW   Ubl conjugation pathway; WD repeat; Zinc; Zinc-finger.
FT   CHAIN         1    594       E3 ubiquitin-protein ligase TRAF7.
FT                                /FTId=PRO_0000051297.
FT   REPEAT      318    357       WD 1.
FT   REPEAT      361    398       WD 2.
FT   REPEAT      401    437       WD 3.
FT   REPEAT      439    478       WD 4.
FT   REPEAT      481    518       WD 5.
FT   REPEAT      521    562       WD 6.
FT   REPEAT      565    593       WD 7.
FT   ZN_FING      55     89       RING-type.
FT   ZN_FING     146    216       TRAF-type.
FT   MOD_RES      12     12       Phosphoserine.
FT   MOD_RES      15     15       Phosphoserine.
FT   MOD_RES      29     29       Phosphoserine (By similarity).
SQ   SEQUENCE   594 AA;  66487 MW;  18009319608AD0B2 CRC64;
     MPPINTPRRS DSAISVRSLH SESSMSLRST FSLPEEEEEP EPLVFAEQPS VKLCCQLCCS
     VFKDPVITTC GHTFCRRCAL KSEKCPVDNA KLTVVVNNIA VAEQIGELFI HCRHGCHAAG
     TGKPGVFEVD PRGCPFTIKL SARKDHESSC DYRPVRCPNN PSCPPLLKMN LEAHLKECEH
     IKCPHSKYGC TFIGNQDTYE THLETCRFEG LKEFLQQTDD RFHEMHVALA QKDQEIAFLR
     SMLGKLSEKI DQLEKSLELK FDVLDENQSK LSEDLMEFRR DASMLNDELS HINARLNMGI
     LGSYDPQQIF KCKGTFVGHQ GPVWCLCVYS MGDLLFSGSS DKTIKVWDTC TTYKCQKTLE
     GHDGIVLALC IQGCKLYSGS ADCTIIVWDI QNLQKVNTIR AHDNPVCTLV SSHNMLFSGS
     LKAIKVWDIV GTELKLKKEL TGLNHWVRAL VAAQSYLYSG SYQTIKIWDI RTLDCIHVLQ
     TSGGSVYSIA VTNHHIVCGT YENLIHVWDI ESKEQVRTLT GHVGTVYALA VISTPDQTKV
     FSASYDRSLR VWSMDNMICT QTLLRHQGSV TALAVSRGRL FSGAVDSTVK VWTC
//
ID   SSFA2_MOUSE             Reviewed;        1252 AA.
AC   Q922B9; A5D8Z6; Q08E80; Q14BJ9; Q544I3; Q68FN1; Q75WU7; Q8CH96;
AC   Q8VEF7;
DT   13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Sperm-specific antigen 2 homolog;
DE   AltName: Full=Ki-ras-induced actin-interacting protein;
GN   Name=Ssfa2; Synonyms=Kiaa1927, Krap;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX   PubMed=14673706; DOI=10.1007/s10038-003-0106-3;
RA   Inokuchi J., Komiya M., Baba I., Naito S., Sasazuki T., Shirasawa S.;
RT   "Deregulated expression of KRAP, a novel gene encoding actin-
RT   interacting protein, in human colon cancer cells.";
RL   J. Hum. Genet. 49:46-52(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-1252.
RC   TISSUE=Brain;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-85; SER-90; SER-268;
RP   SER-442; SER-667; SER-736; SER-738 AND SER-1154, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649; SER-736 AND
RP   SER-738, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Located near the plasma
CC       membrane. Associated with actin filaments. May also exist as a
CC       membrane-bound form with extracellular regions (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q922B9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q922B9-2; Sequence=VSP_023869;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q922B9-3; Sequence=VSP_023868;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH08560.1; Type=Erroneous initiation;
CC       Sequence=AAH18526.3; Type=Erroneous termination; Positions=1249; Note=Translated as Gln;
CC       Sequence=AAI22520.1; Type=Erroneous initiation;
CC       Sequence=BAC29756.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB120565; BAC87833.1; -; mRNA.
DR   EMBL; BC008560; AAH08560.1; ALT_INIT; mRNA.
DR   EMBL; BC018526; AAH18526.3; ALT_TERM; mRNA.
DR   EMBL; BC079535; AAH79535.1; -; mRNA.
DR   EMBL; BC115799; AAI15800.1; -; mRNA.
DR   EMBL; BC122519; AAI22520.1; ALT_INIT; mRNA.
DR   EMBL; BC141883; AAI41884.1; -; mRNA.
DR   EMBL; AK037213; BAC29756.1; ALT_INIT; mRNA.
DR   EMBL; AB093303; BAC41485.1; -; mRNA.
DR   IPI; IPI00275810; -.
DR   IPI; IPI00755121; -.
DR   IPI; IPI00830670; -.
DR   RefSeq; NP_542125.3; NM_080558.4.
DR   UniGene; Mm.272881; -.
DR   STRING; Q922B9; -.
DR   PhosphoSite; Q922B9; -.
DR   PRIDE; Q922B9; -.
DR   Ensembl; ENSMUST00000111785; ENSMUSP00000107415; ENSMUSG00000027007.
DR   GeneID; 70599; -.
DR   KEGG; mmu:70599; -.
DR   CTD; 70599; -.
DR   MGI; MGI:1917849; Ssfa2.
DR   GeneTree; ENSGT00530000063345; -.
DR   HOVERGEN; HBG082646; -.
DR   InParanoid; Q922B9; -.
DR   OrthoDB; EOG4N30PG; -.
DR   NextBio; 331942; -.
DR   ArrayExpress; Q922B9; -.
DR   Bgee; Q922B9; -.
DR   CleanEx; MM_SSFA2; -.
DR   Genevestigator; Q922B9; -.
DR   GermOnline; ENSMUSG00000027007; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Phosphoprotein.
FT   CHAIN         1   1252       Sperm-specific antigen 2 homolog.
FT                                /FTId=PRO_0000072212.
FT   COILED      955   1031       Potential.
FT   MOD_RES      85     85       Phosphothreonine.
FT   MOD_RES      90     90       Phosphoserine.
FT   MOD_RES     161    161       Phosphoserine (By similarity).
FT   MOD_RES     163    163       Phosphothreonine (By similarity).
FT   MOD_RES     165    165       Phosphoserine (By similarity).
FT   MOD_RES     166    166       Phosphoserine (By similarity).
FT   MOD_RES     268    268       Phosphoserine.
FT   MOD_RES     299    299       Phosphoserine (By similarity).
FT   MOD_RES     328    328       Phosphoserine (By similarity).
FT   MOD_RES     366    366       Phosphoserine.
FT   MOD_RES     442    442       Phosphoserine.
FT   MOD_RES     609    609       Phosphoserine (By similarity).
FT   MOD_RES     649    649       Phosphoserine.
FT   MOD_RES     667    667       Phosphoserine.
FT   MOD_RES     724    724       Phosphotyrosine (By similarity).
FT   MOD_RES     731    731       Phosphotyrosine (By similarity).
FT   MOD_RES     736    736       Phosphoserine.
FT   MOD_RES     738    738       Phosphoserine.
FT   MOD_RES     745    745       Phosphoserine (By similarity).
FT   MOD_RES    1051   1051       Phosphoserine (By similarity).
FT   MOD_RES    1056   1056       Phosphoserine (By similarity).
FT   MOD_RES    1059   1059       Phosphoserine (By similarity).
FT   MOD_RES    1154   1154       Phosphoserine.
FT   VAR_SEQ       1   1063       Missing (in isoform 2).
FT                                /FTId=VSP_023869.
FT   VAR_SEQ       1    151       Missing (in isoform 3).
FT                                /FTId=VSP_023868.
FT   CONFLICT    319    319       A -> T (in Ref. 2; AAH79535/AAH08560 and
FT                                3; BAC29756).
FT   CONFLICT   1071   1071       M -> I (in Ref. 2; AAH79535/AAI15800/
FT                                AAH08560 and 3; BAC29756).
FT   CONFLICT   1240   1240       S -> A (in Ref. 1; BAC87833).
SQ   SEQUENCE   1252 AA;  136935 MW;  AC1735E985272590 CRC64;
     MNRPLSAEAE EELEWQVASR RRKAWAKCRS SWQASETEDL STETTTQDED EDDEEDLPGT
     KLPAPAGRGN VPNEKIAIWL KDCRTPLGAS LDEQSSGTPK GVLVRNGGSF EDDLSLGAEA
     NHLHEPDAQV ENCNNILAKE RRLQFHQKGR SMNSTGSGKS SGTVSSVSEL LELYEEDPEE
     ILYNLGFGRD EPDIASKIPS RFFNSSSFAR GIDIKVFLSA QMQRMEVENP NYALTSRFRQ
     IEVLTTVANA FSSLYSQVSG TPLQRIGSMS SVTSTKEVAD SPPPLTRSNT ANRLMKTLSK
     LNLCVDKTEK GEGGSSPAAE KGRTLSISLS EDGGGGKSDP KLQKVVKKKE SSSMLATVTE
     EVSGSSSTVT DSVDADRLSE EADSTISHQE ESEESREAHS QEKDPLRKSA VTDPDLGHDG
     RVSSHCELES SSELKSAQAS SSEKEPCAPL TIPSIRNIMT QQKDSFEMEE VQSTEGEAPH
     VPATCQLSLA KSKRDHLLRT ASQHSDSSGF AEDSTDCVSL NHLLVNESLQ AMGSSADSCD
     SETTVTSLGE DHVTPTAQDQ PYFNESEEES LAPLQKGRAK VEIVAEKRKA DNQDFPQCVT
     AENAGNNEST KGPCEPGHQI TETGEHPPLA ATGELPREES VESDVEKGSE CEFAQYTTHH
     ILRSLASFEA QGSGMSSEKK TGFPSSVDRV NTALQRAQMK VCSMSGQRVG RSLIKSKDLL
     KQRYLLAKAG YPLRRSQSLP TTLLSPVRVV SSVNVRLSPG KETRCSPPSF TYKYTPEEEQ
     DLEKQGTEHD GQSLVKSTIF IPPPSVKKEE APQSEGTRLE ECHHGRLAPC PQFAPISQST
     CSLHSVHSEW QDRPLCEHMR TLSAHSVPNI SGAACSAFSP FGCPYSHRHA AHPYRACSVN
     PPSAIEMQLR RVLHDIRSSL QNLSQYPMTR GPDLAAAPYS TQNSSVLPLY ENTFQELQVV
     RRSLNLFRTQ MMDLELAMLR QQTVVYPHMT EEDRYEVDQL QGLRNSVRME LQDLEMQLEE
     RLLGLDEQLR AVRVPSPFRP SALPGMCGSR SVDNLSCPSP LNVMEPVTEL MREQSYLKSE
     LGLGLGDMAY EIPPGESSES VFSQATSESS SVCSSPSHTN RRSRGLPGSK PRARLVARKK
     IFRASVALTP TAPSRTGSVQ TPPDLESSEE AGGAEEASPV VGLASHVEEE PEDLSLMPAA
     EEMHRNVEQD ELQQVIREIK ESIVGEIRRE IVSGLLAAVS SSKAPGPKQD SH
//
ID   PP6R3_MOUSE             Reviewed;         844 AA.
AC   Q922D4; Q6ZPM9; Q8BTW6; Q9D2X9;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Serine/threonine-protein phosphatase 6 regulatory subunit 3;
DE   AltName: Full=SAPS domain family member 3;
GN   Name=Ppp6r3; Synonyms=D19Ertd703e, Kiaa1558, Pp6r3, Saps3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Cecum, Thymus, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=16769727; DOI=10.1074/jbc.M601772200;
RA   Stefansson B., Brautigan D.L.;
RT   "Protein phosphatase 6 subunit with conserved Sit4-associated protein
RT   domain targets IkappaBepsilon.";
RL   J. Biol. Chem. 281:22624-22634(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-820 AND SER-824, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
CC   -!- FUNCTION: Regulatory subunit of protein phospatase 6 (PP6). May
CC       function as a scaffolding PP6 subunit. May have an important role
CC       in maintaining immune self-tolerance (By similarity).
CC   -!- SUBUNIT: Protein phospatase 6 (PP6) holoenzyme is proposed to be a
CC       heterotrimeric complex formed by the catalytic subunit, a SAPS
CC       domain-containing subunit (PP6R) and an ankyrin repeat-domain
CC       containing regulatory subunit (ARS). Interacts with PPP6C and
CC       ANKRD28 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q922D4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q922D4-2; Sequence=VSP_017145;
CC       Name=3;
CC         IsoId=Q922D4-3; Sequence=VSP_017146, VSP_017147;
CC       Name=4;
CC         IsoId=Q922D4-4; Sequence=VSP_017148, VSP_017149;
CC   -!- TISSUE SPECIFICITY: Strongest expression observed in lung, spleen,
CC       bladder and liver and weaker levels present in brain, heart,
CC       kidney, skeletal muscle and pancreas.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the SAPS family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98202.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK129392; BAC98202.1; ALT_INIT; mRNA.
DR   EMBL; AK018652; BAB31326.1; -; mRNA.
DR   EMBL; AK035236; BAC28993.1; -; mRNA.
DR   EMBL; AK088526; BAC40403.1; -; mRNA.
DR   EMBL; BC008529; AAH08529.1; -; mRNA.
DR   IPI; IPI00122858; -.
DR   IPI; IPI00719971; -.
DR   IPI; IPI00720007; -.
DR   IPI; IPI00720066; -.
DR   RefSeq; NP_001157631.1; NM_001164159.1.
DR   RefSeq; NP_083275.1; NM_028999.1.
DR   RefSeq; NP_083732.1; NM_029456.2.
DR   UniGene; Mm.284686; -.
DR   ProteinModelPortal; Q922D4; -.
DR   PhosphoSite; Q922D4; -.
DR   PRIDE; Q922D4; -.
DR   Ensembl; ENSMUST00000025846; ENSMUSP00000025846; ENSMUSG00000024908.
DR   Ensembl; ENSMUST00000113997; ENSMUSP00000109630; ENSMUSG00000024908.
DR   GeneID; 52036; -.
DR   KEGG; mmu:52036; -.
DR   UCSC; uc008fwk.1; mouse.
DR   UCSC; uc008fwl.1; mouse.
DR   UCSC; uc008fwm.1; mouse.
DR   UCSC; uc008fwo.1; mouse.
DR   CTD; 52036; -.
DR   MGI; MGI:1921807; Ppp6r3.
DR   eggNOG; roNOG11200; -.
DR   GeneTree; ENSGT00390000009899; -.
DR   HOGENOM; HBG505370; -.
DR   HOVERGEN; HBG069733; -.
DR   InParanoid; Q922D4; -.
DR   OMA; MKTTWGV; -.
DR   OrthoDB; EOG4S4PFN; -.
DR   PhylomeDB; Q922D4; -.
DR   NextBio; 308408; -.
DR   ArrayExpress; Q922D4; -.
DR   Bgee; Q922D4; -.
DR   CleanEx; MM_SAPS3; -.
DR   Genevestigator; Q922D4; -.
DR   GermOnline; ENSMUSG00000024908; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR007587; SAPS.
DR   PANTHER; PTHR12634; SAPS; 1.
DR   Pfam; PF04499; SAPS; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein.
FT   CHAIN         1    844       Serine/threonine-protein phosphatase 6
FT                                regulatory subunit 3.
FT                                /FTId=PRO_0000046101.
FT   MOD_RES     550    550       Phosphoserine (By similarity).
FT   MOD_RES     588    588       Phosphoserine.
FT   MOD_RES     602    602       Phosphothreonine (By similarity).
FT   MOD_RES     605    605       Phosphoserine (By similarity).
FT   MOD_RES     693    693       Phosphoserine (By similarity).
FT   MOD_RES     820    820       Phosphothreonine.
FT   MOD_RES     824    824       Phosphoserine.
FT   VAR_SEQ     487    497       DLPDEVRERWE -> GKLVNNLITCV (in isoform
FT                                4).
FT                                /FTId=VSP_017148.
FT   VAR_SEQ     498    844       Missing (in isoform 4).
FT                                /FTId=VSP_017149.
FT   VAR_SEQ     516    548       AFSDYQMQQMTSNFIDQFGFNDEKFADQDDIGN -> VTTC
FT                                HIHSSSDDEIDFKDTGFSQDSSLQQVSHT (in isoform
FT                                3).
FT                                /FTId=VSP_017146.
FT   VAR_SEQ     516    532       Missing (in isoform 2).
FT                                /FTId=VSP_017145.
FT   VAR_SEQ     549    844       Missing (in isoform 3).
FT                                /FTId=VSP_017147.
SQ   SEQUENCE   844 AA;  94653 MW;  1C70ED57ECEF1D45 CRC64;
     MFWKFDLHSS SHIDTLLERE DVTLKELMDE EDVLQECKAQ NRKLIEFLLK AECLEDLVSF
     IIEEPPQDMD EKIRYKYPNI SCELLTSDVS QMNDRLGEDE SLLMKLYSFL LNESPLNPLL
     ASFFSKVLSI LISRKPEQIV DFLKKKRDFV DLIIKHIGTS AIMDLLLRLL TCIEPPQPRQ
     DVLNWLNEER IIQRLVEIVH PSQEEDRHSN ASQSLCEIVR LSRDQMLQVQ NSTEPDPLLA
     TLEKQEIIEQ LLSNIFHKEK NESAIVSAIQ ILLTLLETRR PTFEGHIEIC PPGMSHSACS
     VNKSVLEAIR GRLGSFHELL LEPPKKSVMK TTWGILDPPV GNTRLNVIRL ISSLLQTNTS
     SINGDLMELN SIGVILDMFF KYTWNNFLHT QVEICIALIL ASPFENAENG TITDQDSTGD
     NLLLKHLFQK CQLIERILEA WDTNEKKQAE GGRRHGYMGH LTRIANCIVH STDKGPNSAL
     VQQLIKDLPD EVRERWETFC TNSLGETNKR NTVDLAFSDY QMQQMTSNFI DQFGFNDEKF
     ADQDDIGNVS FDRVSDINFT LNTNESGNIA LFEACCKERI QQFDDGGSDE EDIWEEKHIA
     FTPESQRRSS SGSTDSEEST DSEEEDGAKQ DLFESSSANT EDKMEVDLNE PPTWSANFDV
     PMETTHGAPL DSVGSDVWST EEPMPTKETG WASFSEFTSS LSTKESLRSN SPVEMETSTE
     SVDPLTPGAA ALATQPEAPG SMAMEASSDG EEDAESTDKV TETVMNGGMK ETLSLTVDAK
     TETAVFKSEE EKLSTSQDAA CKDAEETPEP AEAKCTAPLT PSSSPEQRTD QPSMPSDPSV
     NGPV
//
ID   PCY2_MOUSE              Reviewed;         404 AA.
AC   Q922E4; Q99J50;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Ethanolamine-phosphate cytidylyltransferase;
DE            EC=2.7.7.14;
DE   AltName: Full=CTP:phosphoethanolamine cytidylyltransferase;
DE   AltName: Full=Phosphorylethanolamine transferase;
GN   Name=Pcyt2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: CTP + ethanolamine phosphate = diphosphate +
CC       CDP-ethanolamine.
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC       biosynthesis; phosphatidylethanolamine from ethanolamine: step
CC       2/3.
CC   -!- SIMILARITY: Belongs to the cytidylyltransferase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC003473; AAH03473.1; -; mRNA.
DR   EMBL; BC008276; AAH08276.1; -; mRNA.
DR   IPI; IPI00311395; -.
DR   RefSeq; NP_077191.2; NM_024229.2.
DR   UniGene; Mm.21439; -.
DR   ProteinModelPortal; Q922E4; -.
DR   SMR; Q922E4; 20-368.
DR   STRING; Q922E4; -.
DR   PhosphoSite; Q922E4; -.
DR   UCD-2DPAGE; Q922E4; -.
DR   PRIDE; Q922E4; -.
DR   Ensembl; ENSMUST00000026129; ENSMUSP00000026129; ENSMUSG00000025137.
DR   GeneID; 68671; -.
DR   KEGG; mmu:68671; -.
DR   UCSC; uc007mtp.1; mouse.
DR   CTD; 68671; -.
DR   MGI; MGI:1915921; Pcyt2.
DR   HOGENOM; HBG378440; -.
DR   HOVERGEN; HBG000865; -.
DR   InParanoid; Q922E4; -.
DR   OMA; KEPQPGE; -.
DR   OrthoDB; EOG4NGGMV; -.
DR   PhylomeDB; Q922E4; -.
DR   BRENDA; 2.7.7.14; 244.
DR   NextBio; 327664; -.
DR   ArrayExpress; Q922E4; -.
DR   Bgee; Q922E4; -.
DR   CleanEx; MM_PCYT2; -.
DR   Genevestigator; Q922E4; -.
DR   GermOnline; ENSMUSG00000025137; Mus musculus.
DR   GO; GO:0004306; F:ethanolamine-phosphate cytidylyltransferase activity; IEA:EC.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR004821; Cyt_trans-rel.
DR   InterPro; IPR004820; Cytidylyltransf.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 2.
DR   Pfam; PF01467; CTP_transf_2; 2.
DR   TIGRFAMs; TIGR00125; cyt_tran_rel; 2.
PE   1: Evidence at protein level;
KW   Nucleotidyltransferase; Phospholipid biosynthesis; Repeat;
KW   Transferase.
FT   CHAIN         1    404       Ethanolamine-phosphate
FT                                cytidylyltransferase.
FT                                /FTId=PRO_0000208462.
FT   REGION       26    234       Catalytic 1 (Potential).
FT   REGION      235    367       Catalytic 2 (Potential).
FT   ACT_SITE     35     35       By similarity.
FT   ACT_SITE     38     38       By similarity.
FT   ACT_SITE    244    244       By similarity.
FT   ACT_SITE    247    247       By similarity.
FT   CONFLICT    110    110       C -> S (in Ref. 1; AAH03473).
SQ   SEQUENCE   404 AA;  45235 MW;  D45A76E2EB0C9327 CRC64;
     MIRNGHGAAS AAGLKGPGDQ RIVRVWCDGC YDMVHYGHSN QLRQARAMGD YLIVGVHTDE
     EIAKHKGPPV FTQEERYKMV QAIKWVDEVV PAAPYVTTLE TLDKHNCDFC VHGNDITLTV
     DGRDTYEEVK QAGRYRECKR TQGVSTTDLV GRMLLVTKAH HSSQEMSSEY REYADSFGKP
     PHPTPAGDTL SSEVSSQCPG GQSPWTGVSQ FLQTSQKIIQ FASGKEPQPG ETVIYVAGAF
     DLFHIGHVDF LQEVHKLAKR PYVIAGLHFD QEVNRYKGKN YPIMNLHERT LSVLACRYVS
     EVVIGAPYSV TAELLNHFKV DLVCHGKTEI VPDRDGSDPY QEPKRRGIFY QIDSGSDLTT
     DLIVQRIIKN RLEYEARNQK KEAKELAFLE ATKQQEAPPG GEID
//
ID   Q922F2_MOUSE            Unreviewed;       253 AA.
AC   Q922F2;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 2.
DT   08-MAR-2011, entry version 62.
DE   SubName: Full=Rsrc2 protein;
DE   Flags: Fragment;
GN   Name=Rsrc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N;
RC   TISSUE=Mammary tumor. Metallothionien-TGF alpha model. 10 month old
RC   virgin mouse. Taken by biopsy.;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
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DR   EMBL; BC008229; AAH08229.2; -; mRNA.
DR   IPI; IPI00471271; -.
DR   UniGene; Mm.276341; -.
DR   UniGene; Mm.480328; -.
DR   STRING; Q922F2; -.
DR   Ensembl; ENSMUST00000050827; ENSMUSP00000050563; ENSMUSG00000029422.
DR   MGI; MGI:1913489; Rsrc2.
DR   GeneTree; ENSGT00600000084172; -.
DR   HOGENOM; HBG278234; -.
DR   OrthoDB; EOG4PVP0Z; -.
DR   ArrayExpress; Q922F2; -.
DR   Bgee; Q922F2; -.
DR   Genevestigator; Q922F2; -.
PE   1: Evidence at protein level;
FT   NON_TER     253    253
SQ   SEQUENCE   253 AA;  30732 MW;  C300BE4579BCE610 CRC64;
     MAAIDTERDG LALEKTSPDR EKKKEQSDIS ISPRASKHHY SRSRSRSRER KRKSDDGRKH
     RSRSRSKEGR RHESKDKSSK RHKSEEHNDK EHSSDKGRER LNSSENGEDR HKRKERKSSR
     GRSHSRSRSR ERRHRSRSRE RKKSRSRSRD RKKSRSRSRD RKKSRSRSRD RKRRIRTRSR
     SRSRHRHRTR SRSRSRSRSR DRKKRIEKPR RFSRSLSRTP SPPPFRGRNT AMDAQEALAR
     RLERAKKLQK KKK
//
ID   TBB6_MOUSE              Reviewed;         447 AA.
AC   Q922F4;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Tubulin beta-6 chain;
GN   Name=Tubb6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 104-121; 242-251; 253-262; 283-297; 310-318;
RP   337-350 AND 363-379, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [3]
RP   POLYGLUTAMYLATION.
RX   PubMed=15890843; DOI=10.1126/science.1113010;
RA   Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M.,
RA   Temurak N., van Dijk J., Boucher D., van Dorsselaer A.,
RA   Suryavanshi S., Gaertig J., Edde B.;
RT   "Tubulin polyglutamylase enzymes are members of the TTL domain protein
RT   family.";
RL   Science 308:1758-1762(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-106, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   POLYGLYCYLATION.
RX   PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA   Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M.,
RA   Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J.,
RA   Janke C.;
RT   "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT   polyglycylation.";
RL   Cell 137:1076-1087(2009).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. It
CC       binds two moles of GTP, one at an exchangeable site on the beta
CC       chain and one at a non-exchangeable site on the alpha-chain (By
CC       similarity).
CC   -!- SUBUNIT: Dimer of alpha and beta chains (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC   -!- DOMAIN: The highly acidic C-terminal region may bind cations such
CC       as calcium.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- PTM: Some glutamate residues at the C-terminus are either
CC       polyglutamylated or polyglycylated. These 2 modifications occur
CC       exclusively on glutamate residues and result in either
CC       polyglutamate or polyglycine chains on the gamma-carboxyl group.
CC       Glycylation is mainly limited to tubulin incorporated into
CC       axonemes (cilia and flagella) whereas glutamylation is prevalent
CC       in neuronal cells, centrioles, axonemes, and the mitotic spindle.
CC       Both modifications can coexist on the same protein on adjacent
CC       residues, and lowering polyglycylation levels increases
CC       polyglutamylation, and reciprocally. The precise function of such
CC       modifications is still unclear but they are regulate the assembly
CC       and dynamics of axonemal microtubules.
CC   -!- SIMILARITY: Belongs to the tubulin family.
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DR   EMBL; BC008225; AAH08225.1; -; mRNA.
DR   IPI; IPI00122928; -.
DR   RefSeq; NP_080749.2; NM_026473.2.
DR   UniGene; Mm.181860; -.
DR   ProteinModelPortal; Q922F4; -.
DR   SMR; Q922F4; 2-427.
DR   STRING; Q922F4; -.
DR   PhosphoSite; Q922F4; -.
DR   PRIDE; Q922F4; -.
DR   Ensembl; ENSMUST00000001513; ENSMUSP00000001513; ENSMUSG00000001473.
DR   GeneID; 67951; -.
DR   KEGG; mmu:67951; -.
DR   UCSC; uc008fmd.1; mouse.
DR   CTD; 67951; -.
DR   MGI; MGI:1915201; Tubb6.
DR   HOGENOM; HBG750007; -.
DR   HOVERGEN; HBG000089; -.
DR   InParanoid; Q922F4; -.
DR   OMA; YYNQASS; -.
DR   OrthoDB; EOG4W6NW0; -.
DR   PhylomeDB; Q922F4; -.
DR   NextBio; 326054; -.
DR   ArrayExpress; Q922F4; -.
DR   Bgee; Q922F4; -.
DR   CleanEx; MM_TUBB6; -.
DR   Genevestigator; Q922F4; -.
DR   GermOnline; ENSMUSG00000001473; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR   InterPro; IPR013838; Beta-tubulin_BS.
DR   InterPro; IPR002453; Beta_tubulin.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR023123; Tubulin_C.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   Gene3D; G3DSA:3.30.1330.20; Tubulin/FtsZ_2-layer-sand-dom; 1.
DR   Gene3D; G3DSA:1.10.287.600; Tubulin_C; 1.
DR   Gene3D; G3DSA:3.40.50.1440; Tubulin_FtsZ; 1.
DR   PANTHER; PTHR11588; Tubulin; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01163; BETATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF55307; Tub_FtsZ_C; 1.
DR   SUPFAM; SSF52490; Tubulin_FtsZ; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
DR   PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding;
KW   Microtubule; Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1    447       Tubulin beta-6 chain.
FT                                /FTId=PRO_0000048256.
FT   NP_BIND     140    146       GTP (Potential).
FT   MOD_RES      56     56       Phosphoserine (By similarity).
FT   MOD_RES     106    106       Phosphotyrosine.
SQ   SEQUENCE   447 AA;  50090 MW;  B02883BCF61CB514 CRC64;
     MREIVHIQAG QCGNQIGTKF WEVISDEHGI DQAGGYVGDS ALQLERISVY YNESSSKKYV
     PRAALVDLEP GTMDSVRSGP FGQLFRPDNF IFGQTGAGNN WAKGHYTEGA ELVDSVLDVV
     RKECEHCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVM PSPKVSDTVV
     EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTSL
     RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTARGSQQ YRALTVPELT QQMFDAKNMM
     AACDPRHGRY LTVATVFRGP MSMKEVDEQM LAIQNKNSSY FVEWIPNNVK VAVCDIPPRG
     LKMASTFIGN STAIQELFKR ISEQFSAMFR RKAFLHWFTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDATV NDGEEAFEDE DEEEINE
//
ID   Q922G6_MOUSE            Unreviewed;       298 AA.
AC   Q922G6;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   SubName: Full=Spryd3 protein;
DE   Flags: Fragment;
GN   Name=Spryd3; Synonyms=BC008150;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N;
RC   TISSUE=Mammary tumor. Metallothionien-TGF alpha model. 10 month old
RC   virgin mouse. Taken by biopsy.;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC008150; AAH08150.1; -; mRNA.
DR   IPI; IPI00762638; -.
DR   UniGene; Mm.385009; -.
DR   ProteinModelPortal; Q922G6; -.
DR   PhosphoSite; Q922G6; -.
DR   PRIDE; Q922G6; -.
DR   Ensembl; ENSMUST00000154032; ENSMUSP00000121493; ENSMUSG00000036966.
DR   MGI; MGI:2446175; Spryd3.
DR   GeneTree; ENSGT00530000063160; -.
DR   HOVERGEN; HBG079840; -.
DR   OrthoDB; EOG4229JP; -.
DR   ArrayExpress; Q922G6; -.
DR   Bgee; Q922G6; -.
DR   Genevestigator; Q922G6; -.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR003877; SPRY_rcpt.
DR   Pfam; PF00622; SPRY; 1.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   298 AA;  32898 MW;  E8E1D12DBC700F3E CRC64;
     IGCGIEPVSF DVQTAQIFFT KNGKRVGSTI MPMSPDGLFP AVGMHSLGEE VRLHLNAELG
     REDDSVMMVD SYEDEWGRLH DVRVCGTLLE YLGKGKSIVD VGLAQARHPL STRSHYFEVE
     IVDPGEKCYI ALGLARKDYP KNRHPGWSRG SVAYHADDGK IFHGSGVGDP FGPRCYKGDI
     MGCGIMFPRD YILDSEGDSD DSCDTVILSP TARAVRNVRN VMYLHQEGEE EEEEEEEEED
     GEEIEQEHEG KKVVVFFTRN GKIIGKKDAV VPSGGFFPTI GMLSCGEKVK VDLHPLSG
//
ID   ANM3_MOUSE              Reviewed;         532 AA.
AC   Q922H1; Q80VU9; Q8BFV5;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Protein arginine N-methyltransferase 3;
DE            EC=2.1.1.-;
DE   AltName: Full=Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3;
GN   Name=Prmt3; Synonyms=Hrmt1l3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 2).
RC   STRAIN=129/SvJ;
RA   Hauser L.J., Webb L.S., Dhar M.S., Mural R.M., Larimer F.W.,
RA   Johnson D.K.;
RT   "Genomic organization, chromosomal mapping, and expression analysis of
RT   the murine Prmt3 and Htatip2 genes.";
RL   Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 114-532 (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   STRUCTURE BY NMR OF 38-145.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the C2H2 zinc finger domain of the protein
RT   arginine N-methyltransferase 3 from Mus musculus.";
RL   Submitted (NOV-2004) to the PDB data bank.
CC   -!- FUNCTION: Methylates (mono and asymmetric dimethylation) the
CC       guanidino nitrogens of arginyl residues in some proteins (By
CC       similarity).
CC   -!- ENZYME REGULATION: Inhibited by N-ethylmaleimide and high
CC       concentrations of zinc chloride (By similarity).
CC   -!- SUBUNIT: May exist as a monomer or homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q922H1-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q922H1-2; Sequence=VSP_010498;
CC   -!- DOMAIN: The zinc-finger is responsible for substrate specificity
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the protein arginine N-methyltransferase
CC       family.
CC   -!- SIMILARITY: Contains 1 C2H2-type zinc finger.
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DR   EMBL; AY151050; AAN84530.1; -; Genomic_DNA.
DR   EMBL; AK031738; BAC27531.1; -; mRNA.
DR   EMBL; AK086646; BAC39708.1; -; mRNA.
DR   EMBL; BC008128; AAH08128.1; -; mRNA.
DR   EMBL; BC050775; AAH50775.1; -; mRNA.
DR   IPI; IPI00262117; -.
DR   IPI; IPI00417140; -.
DR   RefSeq; NP_598501.1; NM_133740.2.
DR   UniGene; Mm.33202; -.
DR   UniGene; Mm.349442; -.
DR   PDB; 1WIR; NMR; -; A=38-145.
DR   PDBsum; 1WIR; -.
DR   ProteinModelPortal; Q922H1; -.
DR   SMR; Q922H1; 38-145, 208-532.
DR   STRING; Q922H1; -.
DR   PhosphoSite; Q922H1; -.
DR   PRIDE; Q922H1; -.
DR   Ensembl; ENSMUST00000032715; ENSMUSP00000032715; ENSMUSG00000030505.
DR   Ensembl; ENSMUST00000085271; ENSMUSP00000082373; ENSMUSG00000030505.
DR   GeneID; 71974; -.
DR   KEGG; mmu:71974; -.
DR   UCSC; uc009hbt.1; mouse.
DR   CTD; 71974; -.
DR   MGI; MGI:1919224; Prmt3.
DR   GeneTree; ENSGT00550000074406; -.
DR   HOGENOM; HBG715060; -.
DR   HOVERGEN; HBG001793; -.
DR   InParanoid; Q922H1; -.
DR   OMA; EKNCHNR; -.
DR   OrthoDB; EOG40S0FT; -.
DR   PhylomeDB; Q922H1; -.
DR   NextBio; 335102; -.
DR   ArrayExpress; Q922H1; -.
DR   Bgee; Q922H1; -.
DR   CleanEx; MM_PRMT3; -.
DR   Genevestigator; Q922H1; -.
DR   GermOnline; ENSMUSG00000030505; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR010456; Ribosomal-L11_MeTrfase_PrmA.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   Pfam; PF06325; PrmA; 1.
DR   SMART; SM00355; ZnF_C2H2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Metal-binding;
KW   Methyltransferase; Phosphoprotein; S-adenosyl-L-methionine;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    532       Protein arginine N-methyltransferase 3.
FT                                /FTId=PRO_0000212327.
FT   ZN_FING      46     69       C2H2-type.
FT   BINDING     227    227       S-adenosyl-L-methionine (By similarity).
FT   BINDING     236    236       S-adenosyl-L-methionine (By similarity).
FT   BINDING     260    260       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING     282    282       S-adenosyl-L-methionine (By similarity).
FT   BINDING     311    311       S-adenosyl-L-methionine (By similarity).
FT   MOD_RES      22     22       Phosphoserine (By similarity).
FT   MOD_RES      24     24       Phosphoserine (By similarity).
FT   VAR_SEQ     417    420       Missing (in isoform 2).
FT                                /FTId=VSP_010498.
FT   STRAND       49     51
FT   STRAND       54     57
FT   HELIX        58     67
FT   HELIX        73     79
FT   HELIX        84     96
FT   HELIX       101    105
FT   HELIX       116    119
FT   STRAND      122    125
FT   HELIX       127    130
FT   HELIX       133    136
SQ   SEQUENCE   532 AA;  59902 MW;  878ADDCCF4054F17 CRC64;
     MCSLAAGNGR GAELGPEPLE LSDSGDDAGW EDEDADTEPA HGRQHTPCLF CDRLFASAEE
     TFSHCKLEHQ FNIDSMVHKH GLEFYGYIKL INFIRLKNPT VEYMNSIYNP VPWEKDEYLK
     PVLEDDLLLQ FDVEDLYEPV STPFSYPNGL SESASVVEKL KHMEARALSA EAALARARED
     LQKMKQFAQD FVMNVDVRTC SSTTTIADLQ EDEDGVYFSS YGHYGIHEEM LKDKVRTESY
     RDFIYQNPHI FKDKVVLDVG CGTGILSMFA AKVGAKKVIA VDQSEILYQA MDIIRLNKLE
     DTIVLIKGKI EEVSLPVEKV DVIISEWMGY FLLFESMLDS VLYAKSKYLA KGGSVYPDIC
     TISLVAVSDV SKHADRIAFW DDVYGFNMSC MKKAVIPEAV VEVVDHKTLI SDPCDIKMDG
     KHIDCHTTSI SDLEFSSDFT LRTTKTAMCT AVAGYFDIYF EKNCHNRVVF STGPQSTKTH
     WKQTVFLLEK PFPVKAGEAL KGKITVHKNK KDPRSLIVTL TLNSSTQTYS LQ
//
ID   CLIP1_MOUSE             Reviewed;        1391 AA.
AC   Q922J3; Q571L7;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=CAP-Gly domain-containing linker protein 1;
DE   AltName: Full=Restin;
GN   Name=Clip1; Synonyms=Kiaa4046, Rsn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryonic tail;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; SER-199 AND
RP   SER-203, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-890, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [6]
RP   STRUCTURE BY NMR OF 58-128.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the 1st CAP-Gly domain in mouse CLIP-
RT   170/Restin.";
RL   Submitted (NOV-2005) to the PDB data bank.
CC   -!- FUNCTION: Seems to be a intermediate filament associated protein
CC       that links endocytic vesicles to microtubules (By similarity).
CC   -!- INTERACTION:
CC       Q80TV8:Clasp1; NbExp=1; IntAct=EBI-776187, EBI-908322;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity). Note=Associated with the
CC       cytoskeleton (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q922J3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q922J3-2; Sequence=VSP_019425;
CC   -!- SIMILARITY: Contains 2 CAP-Gly domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90357.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK220172; BAD90357.1; ALT_INIT; mRNA.
DR   EMBL; BC007191; AAH07191.1; -; mRNA.
DR   IPI; IPI00123063; -.
DR   IPI; IPI00761270; -.
DR   RefSeq; NP_062739.2; NM_019765.4.
DR   UniGene; Mm.241109; -.
DR   UniGene; Mm.441802; -.
DR   PDB; 2CP7; NMR; -; A=58-128.
DR   PDBsum; 2CP7; -.
DR   ProteinModelPortal; Q922J3; -.
DR   SMR; Q922J3; 4-130, 180-339.
DR   IntAct; Q922J3; 2.
DR   STRING; Q922J3; -.
DR   PhosphoSite; Q922J3; -.
DR   PRIDE; Q922J3; -.
DR   Ensembl; ENSMUST00000111566; ENSMUSP00000107192; ENSMUSG00000049550.
DR   GeneID; 56430; -.
DR   KEGG; mmu:56430; -.
DR   UCSC; uc008zoa.1; mouse.
DR   UCSC; uc008zob.1; mouse.
DR   CTD; 56430; -.
DR   MGI; MGI:1928401; Clip1.
DR   eggNOG; roNOG05148; -.
DR   GeneTree; ENSGT00550000074375; -.
DR   HOVERGEN; HBG007123; -.
DR   OrthoDB; EOG42Z4PQ; -.
DR   NextBio; 312602; -.
DR   ArrayExpress; Q922J3; -.
DR   Bgee; Q922J3; -.
DR   CleanEx; MM_CLIP1; -.
DR   Genevestigator; Q922J3; -.
DR   GermOnline; ENSMUSG00000049550; Mus musculus.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IDA:MGI.
DR   GO; GO:0051010; F:microtubule plus-end binding; IDA:MGI.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR023092; CAP-Gly_CS.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   InterPro; IPR001878; Znf_CCHC.
DR   Gene3D; G3DSA:2.30.30.190; CAP-Gly_domain; 2.
DR   Pfam; PF01302; CAP_GLY; 2.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF74924; CAP-Gly_domain; 2.
DR   PROSITE; PS00845; CAP_GLY_1; 2.
DR   PROSITE; PS50245; CAP_GLY_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Microtubule; Phosphoprotein; Repeat.
FT   CHAIN         1   1391       CAP-Gly domain-containing linker protein
FT                                1.
FT                                /FTId=PRO_0000240672.
FT   DOMAIN       78    120       CAP-Gly 1.
FT   DOMAIN      231    273       CAP-Gly 2.
FT   COILED      349   1306       Potential.
FT   MOTIF      1372   1385       CCHC-box.
FT   COMPBIAS    305    330       Ser-rich.
FT   MOD_RES      48     48       Phosphoserine (By similarity).
FT   MOD_RES     146    146       Phosphoserine (By similarity).
FT   MOD_RES     181    181       Phosphothreonine (By similarity).
FT   MOD_RES     192    192       Phosphoserine (By similarity).
FT   MOD_RES     194    194       Phosphoserine.
FT   MOD_RES     196    196       Phosphoserine (By similarity).
FT   MOD_RES     199    199       Phosphoserine.
FT   MOD_RES     203    203       Phosphoserine.
FT   MOD_RES     786    786       Phosphothreonine (By similarity).
FT   MOD_RES     890    890       Phosphoserine.
FT   MOD_RES    1317   1317       Phosphoserine (By similarity).
FT   VAR_SEQ     695    770       Missing (in isoform 2).
FT                                /FTId=VSP_019425.
FT   CONFLICT     47     47       S -> F (in Ref. 1; BAD90357).
FT   STRAND       63     66
FT   STRAND       71     79
FT   STRAND       81     83
FT   STRAND       85     95
FT   STRAND       97    103
FT   STRAND      116    119
FT   HELIX       121    123
SQ   SEQUENCE   1391 AA;  155814 MW;  061BED1FB3D4068D CRC64;
     MSMLKPSGLK APTKILKPGS TALKTPAAAA APVEKTIPSE KASGPPSSET QEEFVDDFRV
     GERVWVNGNK PGFIQFLGET QFAPGQWAGI VLDEPIGKND GSVAGVRYFQ CEPLKGIFTR
     PSKLTRKVQA EDEANGLQAA PGRTASPLST AAATMVSSSP ATPSNIPHKP SQSTAKEPSA
     TPQISNLTKT ASESISNLSE AGSVKKGERE LKVGDRVLVG GTKAGVVRFL GETDFAKGEW
     CGVELDEPLG KNDGAVAGTR YFQCQPKYGL FAPVHKVTKI GFPSTTPAKA KAAAVRRVMA
     ATPASLKRSP SASSLSSMSS VASSVSSKPS RTGLLTETSS RYARKISGTT ALQEALKEKQ
     QHIEQLLAER DLERAEVAKA TSHVGEIEQE LALARDGHDQ HVLELEAKMD QLRTMVEAAD
     REKVELLNQL EEEKRKVEDL QFRVEEESIT KGDLEVATVS EKSRIMELEK DLALRAQEVA
     ELRRRLESSK PPGDVDMSLS LLQEISALQE KLEAIHTDHQ GEMTSLKEHF GAREEAFQKE
     IKALHTATEK LSKENESLRS KLDHANKENS DVIALWKSKL ETAIASHQQA MEELKVSFSK
     GIGTDSAEFA ELKTQIERLR LDYQHEIESL QSKQDSERSA HAKEMETMQA KLMKIIKEKE
     DSLEAVKARL DSAEDQHLVE MEDTLNKLQE AEIKVKELEV LQAKYTEQSE VIGNFTSQLS
     AVKEKLLDLD ALRKANSEGK LELETLRQQL EGAEKQIKNL ETERNAESSK ANSITKELQE
     KELVLTGLQD SLNQVNQVKE TLEKELQTLK EKFASTSEEA VSAQTRMQDT VNKLHQKEEQ
     FNVLSSELEK LRENLTDMEA KFKEKDDRED QLVKAKEKLE NDIAEIMKMS GDNSSQLTKM
     NDELRLKERS VEELQLKLTK ANENASFLQK SIGEVTLKAE QSQQQAARKH EEEKKELEEK
     LLELEKKMET SYNQCQDLKA KYEKASSETK TKHEEILQNL QKMLADTEDK LKAAQEANRD
     LMQDMEELKT QADKAKAAQT AEDAMQIMEQ MTKEKTETLA SLEDTKQTNA RLQNELDTLK
     ENNLKTVEEL NKSKELLSVE NQKMEEFKKE IETLKQAAAQ KSQQLSALQE ENVKLAEELG
     RTRDEVTSHQ KLEEERSVLN NQLLEMKKRE SEFRKDADEE KASLQKSISL TSALLTEKDA
     ELEKLRNEVT VLRGENATAK SLHSVVQTLE SDKVKLELKV KNLELQLKEN KRQLSSSSGN
     TDAQAEEDER AQESQIDFLN SVIVDLQRKN QDLKMKVEMM SEAALNGNGE DLNSYDSDDQ
     EKQSKKKPRL FCDICDCFDL HDTEDCPTQA QMSEDPPHST HHGSRSEERP YCEICEMFGH
     WATNCNDDET F
//
ID   T132A_MOUSE             Reviewed;        1018 AA.
AC   Q922P8; Q69ZF9; Q8BX93;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Transmembrane protein 132A;
DE   AltName: Full=HSPA5-binding protein 1;
DE   Flags: Precursor;
GN   Name=Tmem132a; Synonyms=Kiaa1583;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in embryonic and postnatal development
CC       of the brain. Increased resistance to cell death induced by serum
CC       starvation in cultured cells. Regulates cAMP-induced GFAP gene
CC       expression via STAT3 phosphorylation (By similarity).
CC   -!- SUBUNIT: Interacts with HSPA5/GRP78 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type I
CC       membrane protein (By similarity). Endoplasmic reticulum membrane;
CC       Single-pass type I membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the TMEM132 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC33373.1; Type=Erroneous termination; Positions=660; Note=Translated as Cys;
CC       Sequence=BAD32485.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK173207; BAD32485.1; ALT_INIT; mRNA.
DR   EMBL; AK048556; BAC33373.1; ALT_SEQ; mRNA.
DR   EMBL; BC006896; AAH06896.2; -; mRNA.
DR   IPI; IPI00464151; -.
DR   RefSeq; NP_598565.2; NM_133804.2.
DR   UniGene; Mm.27387; -.
DR   PRIDE; Q922P8; -.
DR   Ensembl; ENSMUST00000025645; ENSMUSP00000025645; ENSMUSG00000024736.
DR   GeneID; 98170; -.
DR   KEGG; mmu:98170; -.
DR   UCSC; uc008grc.1; mouse.
DR   CTD; 98170; -.
DR   MGI; MGI:2147810; Tmem132a.
DR   eggNOG; roNOG05901; -.
DR   GeneTree; ENSGT00550000074550; -.
DR   HOGENOM; HBG445262; -.
DR   HOVERGEN; HBG099719; -.
DR   InParanoid; Q922P8; -.
DR   OMA; QRKEPPD; -.
DR   OrthoDB; EOG44J2HC; -.
DR   PhylomeDB; Q922P8; -.
DR   NextBio; 353338; -.
DR   ArrayExpress; Q922P8; -.
DR   Bgee; Q922P8; -.
DR   CleanEx; MM_TMEM132A; -.
DR   Genevestigator; Q922P8; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Membrane;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     32       Potential.
FT   CHAIN        33   1018       Transmembrane protein 132A.
FT                                /FTId=PRO_0000287097.
FT   TOPO_DOM     33    846       Extracellular (Potential).
FT   TRANSMEM    847    867       Helical; (Potential).
FT   TOPO_DOM    868   1018       Cytoplasmic (Potential).
FT   REGION      606    911       Binds to HSPA5/GRP78 (By similarity).
FT   REGION      666   1018       Confers cellular localization similar to
FT                                full-length form (By similarity).
FT   CARBOHYD    276    276       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    386    386       L -> M (in Ref. 2; BAC33373).
SQ   SEQUENCE   1018 AA;  110239 MW;  7BDFA487B5B51648 CRC64;
     MTERKAAAPR GPYGAWFCLL VALALEVVRV SSNHDTLDPI YLPVALELLD APEHFRVQQV
     GHYPPANSSL ASRSETFLLM QPWPRAQPLL RASYPPFATQ QVVPPRVTEP HRRPVPWDVR
     AVSVEAAVTP AEPYARVLFH LKGQDWPPGP GSLPCARLHA THPAGTAHRA CRFQPSLGAC
     VVELQFPSHW FSQSATTRAE LAYTLEPAGE GPGGCGLGTE EEPREQALPV GGVELHPEDP
     PQYQEVPLDE AVTLRAPDVP MRPGQLFTAT LLLRHNFTAS LLTLRIKVKK GLQVIAARPA
     QPTLWTAKLD RFKGSKHHTS LITCHRAGPA GPDSSPLELS EFLWVDFAVE NSTGGGVAVT
     RPVTWQLEYP GQAPEAEKDK MVWEILVSER DIRALIPLAK AEELVNTAPL TGVPQRIPVR
     LVTVDSGGAL EEVTEHIGCE SANTQVLQVS EACDAVFVAG QESRGAKGVR VDFWWRRLRA
     SLKLTVWAPL LPLRIELTDT TLEQIRGWRV PGSAEGQLEP ETAAEEVERR SRGCRLQYQR
     AGVRFLVPFA AHPLDGGRRL THLLGPDWLL DVSHLVAAHA HVQDPRIASL EGGRILVGRE
     PGVTSIEVRS PLSDAILGEQ ALAVTDDKVS VLDLRVQPVM GISLSLSRGM SHPGEVTATC
     WAQSALPAPK QEVALSLWLS FSDHTLAPAE LYDRNDLGLS VSAEEPSAVL PAEEQGAQLG
     VVVSGVGAEG LPLHVALHPP EPCRRGRHRV PLASGTAWLG LPPLPTPVPA LPSSPVRTSP
     FTEATVEGKR QIAGDMGGHV GIRGKFERAE EEAGKEENEA KEEEEDEEEM VPAPQRVTDL
     ELGMYALLGI FCLAILIFLV NGVVFVLRYQ RKEPPDSATD PASPQPHNWV WLGTNQEELS
     RQLDRCSSSG PPKGEGGCPC ESGAGGDAST VAPSASESPA GSSSTLARKE AGGRRKRVEF
     VTFAPAPPTQ PPEEPVGAPA VQSILVAGEE DIRWVCEDMG LKDPEELRNY MERIRGSS
//
ID   MOSC2_MOUSE             Reviewed;         338 AA.
AC   Q922Q1;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=MOSC domain-containing protein 2, mitochondrial;
DE            EC=1.-.-.-;
DE   Flags: Precursor;
GN   Name=Mosc2; Synonyms=Mg87;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=C57BL/6J;
RX   PubMed=14651853; DOI=10.1016/S0092-8674(03)00926-7;
RA   Mootha V.K., Bunkenborg J., Olsen J.V., Hjerrild M., Wisniewski J.R.,
RA   Stahl E., Bolouri M.S., Ray H.N., Sihag S., Kamal M., Patterson N.,
RA   Lander E.S., Mann M.;
RT   "Integrated analysis of protein composition, tissue diversity, and
RT   gene regulation in mouse mitochondria.";
RL   Cell 115:629-640(2003).
CC   -!- FUNCTION: Catalytic component of the benzamidoxime prodrug-
CC       converting complex, a complex required to reduce N-hydroxylated
CC       structures, such as benzamidoxime (By similarity).
CC   -!- COFACTOR: Molybdenum (By similarity).
CC   -!- SUBUNIT: Component of a complex composed of cytochrome b5, NADH-
CC       cytochrome b5 reductase (CYB5R3) and MOSC2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Peripheral
CC       membrane protein.
CC   -!- SIMILARITY: Contains 1 MOSC domain.
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DR   EMBL; AK051230; BAC34565.1; -; mRNA.
DR   EMBL; BC006888; AAH06888.1; -; mRNA.
DR   IPI; IPI00123276; -.
DR   RefSeq; NP_598445.1; NM_133684.3.
DR   UniGene; Mm.177724; -.
DR   ProteinModelPortal; Q922Q1; -.
DR   PhosphoSite; Q922Q1; -.
DR   PRIDE; Q922Q1; -.
DR   Ensembl; ENSMUST00000068725; ENSMUSP00000066715; ENSMUSG00000073481.
DR   GeneID; 67247; -.
DR   KEGG; mmu:67247; -.
DR   UCSC; uc007dyq.1; mouse.
DR   CTD; 67247; -.
DR   MGI; MGI:1914497; Mosc2.
DR   eggNOG; roNOG08994; -.
DR   GeneTree; ENSGT00530000063150; -.
DR   HOGENOM; HBG607918; -.
DR   HOVERGEN; HBG081982; -.
DR   InParanoid; Q922Q1; -.
DR   OMA; VAKLWIY; -.
DR   OrthoDB; EOG4M399B; -.
DR   PhylomeDB; Q922Q1; -.
DR   NextBio; 324002; -.
DR   ArrayExpress; Q922Q1; -.
DR   Bgee; Q922Q1; -.
DR   CleanEx; MM_MOSC2; -.
DR   Genevestigator; Q922Q1; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR005302; MoCF_Sase_C.
DR   InterPro; IPR005303; MOSC_N.
DR   InterPro; IPR011037; Pyrv_Knase-like_insert_dom.
DR   Pfam; PF03473; MOSC; 1.
DR   Pfam; PF03476; MOSC_N; 1.
DR   SUPFAM; SSF50800; PK_B_barrel_like; 1.
DR   PROSITE; PS51340; MOSC; 1.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane; Molybdenum;
KW   Oxidoreductase; Transit peptide.
FT   TRANSIT       1     35       Mitochondrion (Potential).
FT   CHAIN        36    338       MOSC domain-containing protein 2,
FT                                mitochondrial.
FT                                /FTId=PRO_0000273342.
FT   DOMAIN      188    336       MOSC.
SQ   SEQUENCE   338 AA;  38194 MW;  436E6C7224B807DA CRC64;
     MGSSSSTALA RLGLPGQPRS TWLGVAALGL AAVALGTVAW RRTRPRRRRQ LQQVGTVSKV
     WIYPIKSCKG VSVCETECTD MGLRCGKVRD RFWMVVKEDG HMVTARQEPR LVLVSITLEN
     NYLTLEAPGM EQIVLPIKLP SSNKIHNCRL FGLDIKGRDC GDEVAQWFTN YLKTQAYRLV
     QFDTSMKGRT TKKLYPSESY LQNYEVAYPD CSPVHLISEA SLVDLNTRLK KKVKMEYFRP
     NIVVSGCEAF EEDTWDELLI GDVEMKRVLS CPRCVLTTVD PDTGIIDRKE PLETLKSYRL
     CDPSVKSIYQ SSPLFGMYFS VEKLGSLRVG DPVYRMVD
//
ID   CP070_MOUSE             Reviewed;         422 AA.
AC   Q922R1;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 53.
DE   RecName: Full=UPF0183 protein C16orf70 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the UPF0183 family.
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DR   EMBL; BC006874; AAH06874.1; -; mRNA.
DR   IPI; IPI00123321; -.
DR   UniGene; Mm.27186; -.
DR   PRIDE; Q922R1; -.
DR   Ensembl; ENSMUST00000034361; ENSMUSP00000034361; ENSMUSG00000031889.
DR   UCSC; uc009nbt.1; mouse.
DR   MGI; MGI:2443049; D230025D16Rik.
DR   GeneTree; ENSGT00390000015992; -.
DR   HOGENOM; HBG599216; -.
DR   HOVERGEN; HBG023195; -.
DR   InParanoid; Q922R1; -.
DR   OrthoDB; EOG43FGWV; -.
DR   ArrayExpress; Q922R1; -.
DR   Bgee; Q922R1; -.
DR   CleanEx; MM_D230025D16RIK; -.
DR   Genevestigator; Q922R1; -.
DR   GermOnline; ENSMUSG00000031889; Mus musculus.
DR   InterPro; IPR005373; UPF0183.
DR   PANTHER; PTHR13465; UPF0183; 1.
DR   Pfam; PF03676; UPF0183; 1.
PE   2: Evidence at transcript level;
FT   CHAIN         1    422       UPF0183 protein C16orf70 homolog.
FT                                /FTId=PRO_0000221084.
SQ   SEQUENCE   422 AA;  47402 MW;  5639E30A26D96F14 CRC64;
     MLDLEVVPER SLGNEQWEFT LGMPLAQAVA ILQKHCRIIR NVQVLYSEQS PLSHDLILNL
     TQDGITLLFD AFNQRLKVIE VCELTKVKLK YCGVHFNSQA IAPTIEQIDQ SFGATHPGVY
     NSTEQLFHLN FRGLSFSFQL DSWTEAPKYE PNFAHGLASL QIPHGATVKR MYIYSGNSLQ
     DTKAPVMPLS CFLGNVYAES VDVLRDGTGP SGLRLRLLAA GCGPGVLADA KMRVFERAVY
     FGDSCQDVLS MLGSPHKVFY KSEDKMKIHS PSPHKQVPSK CNDYFFNYFT LGVDILFDAN
     THKVKKFVLH TNYPGHYNFN IYHRCEFKIP LAIKKENAGG QTEICTTYSK WDSIQDLLGH
     PVEKPVVLHR SSSPNNTNPF GSTFCFGLQR MIFEVMQNNH IASVTLYGPP RPGAHLRTAE
     LP
//
ID   PDIA6_MOUSE             Reviewed;         440 AA.
AC   Q922R8; Q8BK54;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 3.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Protein disulfide-isomerase A6;
DE            EC=5.3.4.1;
DE   AltName: Full=Thioredoxin domain-containing protein 7;
DE   Flags: Precursor;
GN   Name=Pdia6; Synonyms=Txndc7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 119-132 AND 393-409, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [5]
RP   STRUCTURE BY NMR OF 16-132.
RG   RIKEN structural genomics initiative (RSGI);
RT   "The solution structure of the first thioredoxin domain of mouse
RT   protein disulfide-isomerase A6.";
RL   Submitted (OCT-2006) to the PDB data bank.
CC   -!- FUNCTION: May function as a chaperone that inhibits aggregation of
CC       misfolded proteins. Plays a role in platelet aggregation and
CC       activation by agonists such as convulxin, collagen and thrombin
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Catalyzes the rearrangement of -S-S- bonds in
CC       proteins.
CC   -!- SUBUNIT: Part a large chaperone multiprotein complex comprising
CC       DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1,
CC       UGT1A1 and very small amounts of ERP29, but not, or at very low
CC       levels, CALR nor CANX. Interacts with ITGB3 following platelet
CC       stimulation (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (By similarity).
CC       Cell membrane (By similarity). Melanosome (By similarity).
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC   -!- SIMILARITY: Contains 2 thioredoxin domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH06865.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC       Sequence=BAC36392.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; AK076558; BAC36392.1; ALT_INIT; mRNA.
DR   EMBL; BC006865; AAH06865.2; ALT_INIT; mRNA.
DR   IPI; IPI00222496; -.
DR   RefSeq; NP_082235.1; NM_027959.3.
DR   UniGene; Mm.222825; -.
DR   PDB; 2DML; NMR; -; A=16-132.
DR   PDBsum; 2DML; -.
DR   ProteinModelPortal; Q922R8; -.
DR   SMR; Q922R8; 20-392.
DR   STRING; Q922R8; -.
DR   PhosphoSite; Q922R8; -.
DR   REPRODUCTION-2DPAGE; Q922R8; -.
DR   PRIDE; Q922R8; -.
DR   Ensembl; ENSMUST00000057288; ENSMUSP00000052912; ENSMUSG00000020571.
DR   GeneID; 71853; -.
DR   KEGG; mmu:71853; -.
DR   CTD; 71853; -.
DR   MGI; MGI:1919103; Pdia6.
DR   HOVERGEN; HBG053548; -.
DR   InParanoid; Q922R8; -.
DR   OrthoDB; EOG49W2FG; -.
DR   BRENDA; 5.3.4.1; 244.
DR   ArrayExpress; Q922R8; -.
DR   Bgee; Q922R8; -.
DR   CleanEx; MM_PDIA6; -.
DR   Genevestigator; Q922R8; -.
DR   GermOnline; ENSMUSG00000020571; Mus musculus.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:EC.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   InterPro; IPR005788; Disulphide_isomerase.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR017936; Thioredoxin-like.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 2.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 3.
DR   TIGRFAMs; TIGR01126; pdi_dom; 2.
DR   PROSITE; PS00014; ER_TARGET; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 2.
DR   PROSITE; PS51352; THIOREDOXIN_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Chaperone; Direct protein sequencing;
KW   Disulfide bond; Endoplasmic reticulum; Isomerase; Membrane;
KW   Phosphoprotein; Redox-active center; Repeat; Signal.
FT   SIGNAL        1     19       By similarity.
FT   CHAIN        20    440       Protein disulfide-isomerase A6.
FT                                /FTId=PRO_0000034238.
FT   DOMAIN       20    133       Thioredoxin 1.
FT   DOMAIN      151    287       Thioredoxin 2.
FT   MOTIF       437    440       Prevents secretion from ER (Potential).
FT   COMPBIAS    422    434       Asp/Glu-rich (acidic).
FT   MOD_RES     428    428       Phosphoserine.
FT   DISULFID     55     58       Redox-active (By similarity).
FT   DISULFID    190    193       Redox-active (By similarity).
FT   CONFLICT    224    224       V -> M (in Ref. 1; BAC36392).
FT   STRAND       25     27
FT   TURN         32     34
FT   HELIX        35     38
FT   TURN         39     41
FT   STRAND       46     51
FT   HELIX        59     61
FT   HELIX        62     71
FT   TURN         72     75
FT   TURN         83     85
FT   STRAND      100    104
FT   HELIX       122    132
SQ   SEQUENCE   440 AA;  48100 MW;  E9FFA1F91AE06A20 CRC64;
     MARLVLGLVS CTFFLAVSGL YSSSDDVIEL TPSNFNREVI QSDGLWLVEF YAPWCGHCQR
     LTPEWKKAAT ALKDVVKVGA VNADKHQSLG GQYGVQGFPT IKIFGANKNK PEDYQGGRTG
     EAIVDAALSA LRQLVKDRLG GRSGGYSSGK QGRGDSSSKK DVVELTDDTF DKNVLDSEDV
     WMVEFYAPWC GHCKNLEPEW AAAATEVKEQ TKGKVKLAAV DATVNQVLAS RYGIKGFPTI
     KIFQKGESPV DYDGGRTRSD IVSRALDLFS DNAPPPELLE IINEDIAKKT CEEHQLCVVA
     VLPHILDTGA AGRNSYLEVL LKLADKYKKK MWGWLWTEAG AQYELENALG IGGFGYPAMA
     AINARKMKFA LLKGSFSEQG INEFLRELSF GRGSTAPVGG GSFPTITPRE PWDGKDGELP
     VEDDIDLSDV ELDDLEKDEL
//
ID   PDE2A_MOUSE             Reviewed;         916 AA.
AC   Q922S4; Q8K2U1;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   08-FEB-2011, entry version 84.
DE   RecName: Full=cGMP-dependent 3',5'-cyclic phosphodiesterase;
DE            EC=3.1.4.17;
DE   AltName: Full=Cyclic GMP-stimulated phosphodiesterase;
DE            Short=CGS-PDE;
DE            Short=cGSPDE;
GN   Name=Pde2a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 805-814, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.86 ANGSTROMS) OF 183-549 IN COMPLEX WITH
RP   CGMP, DOMAIN GAF 1, AND SUBUNIT.
RX   PubMed=12271124; DOI=10.1073/pnas.192374899;
RA   Martinez S.E., Wu A.Y., Glavas N.A., Tang X.-B., Turley S.,
RA   Hol W.G.J., Beavo J.A.;
RT   "The two GAF domains in phosphodiesterase 2A have distinct roles in
RT   dimerization and in cGMP binding.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13260-13265(2002).
CC   -!- FUNCTION: Cyclic nucleotide phosphodiesterase with a dual-
CC       specificity for the second messengers cAMP and cGMP, which are key
CC       regulators of many important physiological processes (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Nucleoside 3',5'-cyclic phosphate + H(2)O =
CC       nucleoside 5'-phosphate.
CC   -!- COFACTOR: Binds 2 divalent metal cations per subunit. Site 1 may
CC       preferentially bind zinc ions, while site 2 has a preference for
CC       magnesium and/or manganese ions (By similarity).
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein
CC       (Potential).
CC   -!- DOMAIN: GAF 1 functions as a dimerization domain, whereas GAF 2
CC       binds cGMP, which causes activation of the catalytic activity of
CC       the enzyme.
CC   -!- MISCELLANEOUS: cGMP binds at an allosteric activator site.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
CC       family. PDE2 subfamily.
CC   -!- SIMILARITY: Contains 2 GAF domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC006845; AAH06845.1; -; mRNA.
DR   EMBL; BC029810; AAH29810.1; -; mRNA.
DR   EMBL; BC057029; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00623742; -.
DR   UniGene; Mm.247564; -.
DR   PDB; 1MC0; X-ray; 2.86 A; A=190-549.
DR   PDBsum; 1MC0; -.
DR   ProteinModelPortal; Q922S4; -.
DR   SMR; Q922S4; 198-892.
DR   STRING; Q922S4; -.
DR   PhosphoSite; Q922S4; -.
DR   PRIDE; Q922S4; -.
DR   Ensembl; ENSMUST00000032889; ENSMUSP00000032889; ENSMUSG00000030653.
DR   UCSC; uc009ioq.1; mouse.
DR   MGI; MGI:2446107; Pde2a.
DR   GeneTree; ENSGT00590000082915; -.
DR   HOVERGEN; HBG053540; -.
DR   BRENDA; 3.1.4.17; 244.
DR   ArrayExpress; Q922S4; -.
DR   Bgee; Q922S4; -.
DR   CleanEx; MM_PDE2A; -.
DR   Genevestigator; Q922S4; -.
DR   GermOnline; ENSMUSG00000030653; Mus musculus.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:EC.
DR   GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR003607; Metal-dep_PHydrolase_HD_dom.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR023174; PDEase_CS.
DR   Gene3D; G3DSA:1.10.1300.10; PDEase_catalytic_dom; 1.
DR   Pfam; PF01590; GAF; 2.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00065; GAF; 2.
DR   SMART; SM00471; HDc; 1.
DR   PROSITE; PS00126; PDEASE_I; 1.
PE   1: Evidence at protein level;
KW   3D-structure; cAMP; cGMP; cGMP-binding; Direct protein sequencing;
KW   Hydrolase; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1    916       cGMP-dependent 3',5'-cyclic
FT                                phosphodiesterase.
FT                                /FTId=PRO_0000198797.
FT   DOMAIN      216    353       GAF 1.
FT   DOMAIN      385    524       GAF 2.
FT   REGION      609    867       Catalytic (By similarity).
FT   REGION      632    636       Substrate binding (By similarity).
FT   ACT_SITE    632    632       Proton donor (By similarity).
FT   METAL       636    636       Divalent metal cation 1 (By similarity).
FT   METAL       672    672       Divalent metal cation 1 (By similarity).
FT   METAL       673    673       Divalent metal cation 1 (By similarity).
FT   METAL       673    673       Divalent metal cation 2 (By similarity).
FT   METAL       784    784       Divalent metal cation 1 (By similarity).
FT   BINDING     407    407       cGMP.
FT   BINDING     422    422       cGMP.
FT   BINDING     475    475       cGMP.
FT   BINDING     673    673       Substrate (By similarity).
FT   BINDING     784    784       Substrate (By similarity).
FT   MOD_RES     885    885       Phosphoserine (By similarity).
FT   HELIX       199    210
FT   HELIX       217    231
FT   STRAND      234    242
FT   STRAND      244    246
FT   STRAND      248    254
FT   STRAND      257    271
FT   HELIX       272    278
FT   HELIX       284    286
FT   HELIX       289    299
FT   STRAND      306    312
FT   TURN        314    316
FT   STRAND      318    330
FT   HELIX       337    381
FT   TURN        382    384
FT   TURN        386    388
FT   HELIX       389    401
FT   STRAND      403    411
FT   STRAND      413    421
FT   HELIX       440    448
FT   STRAND      452    455
FT   HELIX       468    471
FT   STRAND      478    484
FT   STRAND      490    499
FT   STRAND      502    504
FT   HELIX       507    535
SQ   SEQUENCE   916 AA;  103288 MW;  51C03B086633BF20 CRC64;
     MRRQPAASQD PLAQKPEPPG SRDDRLEDAL LSLGAVIDIA GLRQAARDAL SAVLPKVETV
     YTYLLDGESR LVCEDPPHEL PQEGKIREAV ISQKRLSCNG LGPSDLLGKP LARLVAPLAP
     DMQVLVIPLL DKETGSVAAV ILVHCGQLSD SEEQSLQVVE KHALVALRRV QALQQRRPEA
     VQNTSVDASE DQKDEKGYTD HDRKILQLCG ELFDLDATSL QLKVLQYLQQ ETQATHCCLL
     LVSEDNLQLS CKVIGDKVLG EEVSFPLTMG RLGQVVEDKQ CIQLKDLTSD DVQQLQNMLG
     CELQAMLCVP VISRATDQVV ALACAFNKLG GDFFTDEDEH VIQHCFHYTG TVLTSTLAFQ
     KEQKLKCECQ ALLQVAKNLF THLDDVSVLL QEIITEARNL SNAEICSVFL LDQNELVAKV
     FDGGVVDDES YEIRIPADQG IAGHVATTGQ ILNIPDAYAH PLFYRGVDDS TGFRTRNILC
     FPIKNENQEV IGVAELVNKI NGPWFSKFDE DLATAFSIYC GISIAHSLLY KKVNEAQYRS
     HLANEMMMYH MKVSDDEYTK LLHDGIQPVA AIDSNFANFT YTPRSLPEDD TSMAILSMLQ
     DMNFINNYKI DCPTLARFCL MVKKGYRDPP YHNWMHAFSV SHFCYLLYKN LELSNYLEDI
     EIFALFISCM CHDLDHRGTN NSFQVASKSV LAALYSSEGS VMERHHFAQA IAILNTHGCN
     IFDHFSRKDY QRMLDLMRDI ILATDLAHHL RIFKDLQKMA EVGYDRNNRQ HHRLLLCLLM
     TSCDLSDQTK GWKTTRKIAE LIYKEFFSQG DLEKAMGNRP MEMMDREKAY IPELQISFME
     HIAMPIYKLL QDLFPKAAEL YERVASNREH WTKVSHKFTI RGLPSNNSLD FLDEEYEVPD
     LDGTRAPVNG CCSLEG
//
ID   K2C5_MOUSE              Reviewed;         580 AA.
AC   Q922U2; Q920F2;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Keratin, type II cytoskeletal 5;
DE   AltName: Full=Cytokeratin-5;
DE            Short=CK-5;
DE   AltName: Full=Keratin-5;
DE            Short=K5;
DE   AltName: Full=Type-II keratin Kb5;
GN   Name=Krt5; Synonyms=Krt2-5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=129/Ola;
RX   MEDLINE=21301816; PubMed=11408584;
RA   Peters B., Kirfel J., Bussow H., Vidal M., Magin T.M.;
RT   "Complete cytolysis and neonatal lethality in keratin 5 knockout mice
RT   reveal its fundamental role in skin integrity and in epidermolysis
RT   bullosa simplex.";
RL   Mol. Biol. Cell 12:1775-1789(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 326-337 AND 455-465, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-61 AND SER-72,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC       Keratin-5 associates with keratin-14. Interacts with TCHP (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in epidermis.
CC   -!- MISCELLANEOUS: There are two types of cytoskeletal and
CC       microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to
CC       basic; 56-70 kDa).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF306785; AAL16774.1; -; Genomic_DNA.
DR   EMBL; BC006780; AAH06780.1; -; mRNA.
DR   IPI; IPI00139301; -.
DR   RefSeq; NP_081287.1; NM_027011.2.
DR   UniGene; Mm.451847; -.
DR   ProteinModelPortal; Q922U2; -.
DR   SMR; Q922U2; 160-197, 205-311, 328-398, 419-473.
DR   MINT; MINT-218160; -.
DR   STRING; Q922U2; -.
DR   PhosphoSite; Q922U2; -.
DR   PRIDE; Q922U2; -.
DR   Ensembl; ENSMUST00000023709; ENSMUSP00000023709; ENSMUSG00000061527.
DR   GeneID; 110308; -.
DR   KEGG; mmu:110308; -.
DR   UCSC; uc007xtw.1; mouse.
DR   CTD; 110308; -.
DR   MGI; MGI:96702; Krt5.
DR   HOGENOM; HBG715391; -.
DR   HOVERGEN; HBG013015; -.
DR   InParanoid; Q922U2; -.
DR   OMA; CGVGGYG; -.
DR   OrthoDB; EOG4P8FJ6; -.
DR   PhylomeDB; Q922U2; -.
DR   NextBio; 363739; -.
DR   ArrayExpress; Q922U2; -.
DR   Bgee; Q922U2; -.
DR   CleanEx; MM_KRT5; -.
DR   Genevestigator; Q922U2; -.
DR   GermOnline; ENSMUSG00000061527; Mus musculus.
DR   GO; GO:0045095; C:keratin filament; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR016044; F.
DR   InterPro; IPR001664; IF.
DR   InterPro; IPR018039; Intermediate_filament_CS.
DR   InterPro; IPR003054; Keratin_II.
DR   PANTHER; PTHR23239; IF; 1.
DR   PANTHER; PTHR23239:SF18; Keratin_II; 1.
DR   Pfam; PF00038; Filament; 1.
DR   PRINTS; PR01276; TYPE2KERATIN.
DR   PROSITE; PS00226; IF; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Direct protein sequencing; Intermediate filament;
KW   Keratin; Phosphoprotein.
FT   CHAIN         1    580       Keratin, type II cytoskeletal 5.
FT                                /FTId=PRO_0000063728.
FT   REGION        1    161       Head.
FT   REGION      162    471       Rod.
FT   REGION      162    197       Coil 1A.
FT   REGION      198    216       Linker 1.
FT   REGION      217    309       Coil 1B.
FT   REGION      310    332       Linker 12.
FT   REGION      333    471       Coil 2.
FT   REGION      472    580       Tail.
FT   COMPBIAS      2     38       Ser-rich.
FT   COMPBIAS     39    133       Gly-rich.
FT   COMPBIAS    495    562       Gly-rich.
FT   SITE        413    413       Stutter.
FT   MOD_RES      21     21       Phosphoserine.
FT   MOD_RES      57     57       Phosphotyrosine (By similarity).
FT   MOD_RES      61     61       Phosphoserine.
FT   MOD_RES      63     63       Phosphotyrosine (By similarity).
FT   MOD_RES      72     72       Phosphoserine.
FT   CONFLICT    139    139       V -> I (in Ref. 1; AAL16774).
SQ   SEQUENCE   580 AA;  61767 MW;  304B341FD4224B41 CRC64;
     MSRQSSVSFR SGGSRSFSAA SAITPSVSRT SFSSVSRSGG GGGGRISLGG ACGAGGYGSR
     SLYNVGGSKR ISYSSGGGSF RNQFGAGGFG FGGGAGSGFG FGGGAGSGFG FGGGAGFGGG
     YGGAGFPVCP PGGIQEVTVN QNLLTPLNLQ IDPTIQRVRT EEREQIKTLN NKFASFIDKV
     RFLEQQNKVL DTKWALLQEQ GTKTIKQNLD PLFEQYINNL RRQLDGVLGE RGRLDSELRN
     MQDLVEDYKN KYEDEINKRT TAENEFVMLK KDVDAAYMNK VELEARVDAL MDEINFMKMF
     FDAELSQMQT HVSDTSVVLS MDNNRSLDLD SIIAEVKAQY EDIANRSRTE AESWYQTKYE
     ELQQTAGRHG DDLRNTKHEI SEMNRMIQRL RSEIDNVKKQ CANLQNAIAE AEQRGELALK
     DARNKLTELE EALQKAKQDM ARLLREYQEL MNTKLALDVE IATYRKLLEG EECRLSGEGV
     GPVNISVVTN SVSSGYGGGS SIGVGSGFGG GLGSGFAGGL GPRFTRGGGG LGLGSGLSVG
     GSGFSAGSSQ GGMSFGSGGG SGSSVKFVST TSSSRRSFKS
//
ID   Q923F1_MOUSE            Unreviewed;       241 AA.
AC   Q923F1;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   SubName: Full=Chloride channel, nucleotide-sensitive, 1A;
DE   SubName: Full=Chloride channel, nucleotide-sensitive, 1A, isoform CRA_b;
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Clns1a; ORFNames=mCG_7058;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N;
RC   TISSUE=Mammary tumor. Metallothionien-TGF alpha model. 10 month old
RC   virgin mouse. Taken by biopsy.;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Medulla oblongata;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Medulla oblongata;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Medulla oblongata;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Medulla oblongata;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Medulla oblongata;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Medulla oblongata;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Medulla oblongata;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [11]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [12]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC005575; AAH05575.3; -; mRNA.
DR   EMBL; AK031877; BAC27588.1; -; mRNA.
DR   EMBL; AK169259; BAE41022.1; -; mRNA.
DR   EMBL; CH466531; EDL16318.1; -; Genomic_DNA.
DR   IPI; IPI00124248; -.
DR   RefSeq; NP_076160.1; NM_023671.1.
DR   UniGene; Mm.21482; -.
DR   ProteinModelPortal; Q923F1; -.
DR   SMR; Q923F1; 24-139.
DR   STRING; Q923F1; -.
DR   PhosphoSite; Q923F1; -.
DR   PRIDE; Q923F1; -.
DR   Ensembl; ENSMUST00000026506; ENSMUSP00000026506; ENSMUSG00000025439.
DR   GeneID; 12729; -.
DR   KEGG; mmu:12729; -.
DR   UCSC; uc009ijr.1; mouse.
DR   CTD; 12729; -.
DR   MGI; MGI:109638; Clns1a.
DR   GeneTree; ENSGT00390000010063; -.
DR   HOGENOM; HBG444799; -.
DR   HOVERGEN; HBG003108; -.
DR   InParanoid; Q923F1; -.
DR   OMA; PEEHLYV; -.
DR   PhylomeDB; Q923F1; -.
DR   NextBio; 282030; -.
DR   ArrayExpress; Q923F1; -.
DR   Bgee; Q923F1; -.
DR   Genevestigator; Q923F1; -.
DR   InterPro; IPR003521; ICln_channel.
DR   PRINTS; PR01348; ICLNCHANNEL.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   241 AA;  26523 MW;  54F9565DDEAEBC1E CRC64;
     MLSPAMSFLK SFPPPGSADG LRLQQPDTEA VLNGKGLGTG TLYIAESRLS WLDGSGLGFS
     LEYPTISLHA VSRDPNAYPQ EHLYVMVNAK LGEESKEPLS DEDEEDNDDV EPISEFRFVP
     SDKSALEAMF TAMCECQALH PDPEDEDSDD YDGEEYDVEA HEQGQGDIPT FYTYEEGLSH
     LTAEGQATLE RLEGMLSQSV SSQYNMAGVR TEDSVRNYED GMEVETTPTV AGQFEDADVD
     H
//
ID   Q923G3_MOUSE            Unreviewed;       272 AA.
AC   Q923G3;
DT   01-DEC-2001, integrated into UniProtKB/TrEMBL.
DT   01-DEC-2001, sequence version 1.
DT   08-FEB-2011, entry version 62.
DE   SubName: Full=Capping protein (Actin filament) muscle Z-line, beta;
DE   SubName: Full=Capping protein (Actin filament) muscle Z-line, beta, isoform CRA_c;
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Capzb; ORFNames=RP23-247I1.3-001, mCG_122335;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II;
RC   TISSUE=Mammary tumor metastatized to lung. Tumor arose spontaneously;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Hall R.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Heart, and Activated spleen;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Heart, and Activated spleen;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Heart, and Activated spleen;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Heart, and Activated spleen;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Heart, and Activated spleen;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Heart, and Activated spleen;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [11]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Heart, and Activated spleen;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [12]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Heart;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [13]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NOD; TISSUE=Activated spleen;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; BC002053; AAH02053.1; -; mRNA.
DR   EMBL; AK156778; BAE33851.1; -; mRNA.
DR   EMBL; AK168738; BAE40579.1; -; mRNA.
DR   EMBL; AL807811; CAM18537.1; -; Genomic_DNA.
DR   EMBL; CH466615; EDL13298.1; -; Genomic_DNA.
DR   IPI; IPI00269481; -.
DR   PIR; C54819; C54819.
DR   RefSeq; NP_033928.1; NM_009798.3.
DR   UniGene; Mm.2945; -.
DR   HSSP; P14315; 1IZN.
DR   ProteinModelPortal; Q923G3; -.
DR   SMR; Q923G3; 2-270.
DR   STRING; Q923G3; -.
DR   PRIDE; Q923G3; -.
DR   Ensembl; ENSMUST00000102508; ENSMUSP00000099566; ENSMUSG00000028745.
DR   GeneID; 12345; -.
DR   KEGG; mmu:12345; -.
DR   UCSC; uc008vlw.1; mouse.
DR   CTD; 12345; -.
DR   MGI; MGI:104652; Capzb.
DR   GeneTree; ENSGT00390000017957; -.
DR   HOVERGEN; HBG050789; -.
DR   NextBio; 280980; -.
DR   ArrayExpress; Q923G3; -.
DR   Bgee; Q923G3; -.
DR   Genevestigator; Q923G3; -.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR   GO; GO:0008290; C:F-actin capping protein complex; IEA:InterPro.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0030032; P:lamellipodium assembly; IMP:MGI.
DR   InterPro; IPR019771; F-actin_capping_bsu_CS.
DR   InterPro; IPR001698; WASH_F-actin_cap_beta.
DR   PANTHER; PTHR10619; Factin_cap_beta; 1.
DR   Pfam; PF01115; F_actin_cap_B; 1.
DR   PRINTS; PR00192; FACTINCAPB.
DR   PROSITE; PS00231; F_ACTIN_CAPPING_BETA; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   272 AA;  30629 MW;  E6466A68B1254FD0 CRC64;
     MSDQQLDCAL DLMRRLPPQQ IEKNLSDLID LVPSLCEDLL SSVDQPLKIA RDKVVGKDYL
     LCDYNRDGDS YRSPWSNKYD PPLEDGAMPS ARLRKLEVEA NNAFDQYRDL YFEGGVSSVY
     LWDLDHGFAG VILIKKAGDG SKKIKGCWDS IHVVEVQEKS SGRTAHYKLT STVMLWLQTN
     KSGSGTMNLG GSLTRQMEKD ETVSDCSPHI ANIGRLVEDM ENKIRSTLNE IYFGKTKDIV
     NGLRSVQTFA DKSKQEALKN DLVEALKRKQ QC
//
ID   CSMD1_MOUSE             Reviewed;        3564 AA.
AC   Q923L3; Q8BUV1; Q8BYQ3;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=CUB and sushi domain-containing protein 1;
DE   AltName: Full=CUB and sushi multiple domains protein 1;
DE   Flags: Precursor;
GN   Name=Csmd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6;
RX   MEDLINE=21365705; PubMed=11472063; DOI=10.1006/geno.2001.6587;
RA   Sun P.C., Uppaluri R., Schmidt A.P., Pashia M.E., Quant E.C.,
RA   Sunwoo J.B., Gollin S.M., Scholnick S.B.;
RT   "Transcript map of the 8p23 putative tumor suppressor region.";
RL   Genomics 75:17-25(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 3250-3564 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q923L3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q923L3-2; Sequence=VSP_009037;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q923L3-3; Sequence=VSP_009036;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the CSMD family.
CC   -!- SIMILARITY: Contains 14 CUB domains.
CC   -!- SIMILARITY: Contains 28 Sushi (CCP/SCR) domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC30095.1; Type=Erroneous initiation;
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DR   EMBL; AY017475; AAG54083.1; -; mRNA.
DR   EMBL; AK038679; BAC30095.1; ALT_INIT; mRNA.
DR   EMBL; AK082377; BAC38482.1; -; mRNA.
DR   IPI; IPI00124438; -.
DR   IPI; IPI00395221; -.
DR   IPI; IPI00469649; -.
DR   RefSeq; NP_444401.2; NM_053171.2.
DR   UniGene; Mm.436988; -.
DR   ProteinModelPortal; Q923L3; -.
DR   SMR; Q923L3; 2-3335.
DR   PRIDE; Q923L3; -.
DR   Ensembl; ENSMUST00000082104; ENSMUSP00000080751; ENSMUSG00000060924.
DR   GeneID; 94109; -.
DR   KEGG; mmu:94109; -.
DR   UCSC; uc009kzr.1; mouse.
DR   CTD; 94109; -.
DR   MGI; MGI:2137383; Csmd1.
DR   eggNOG; roNOG05297; -.
DR   GeneTree; ENSGT00600000084158; -.
DR   HOGENOM; HBG506160; -.
DR   HOVERGEN; HBG051134; -.
DR   InParanoid; Q923L3; -.
DR   OrthoDB; EOG451DPS; -.
DR   NextBio; 352095; -.
DR   ArrayExpress; Q923L3; -.
DR   Bgee; Q923L3; -.
DR   CleanEx; MM_CSMD1; -.
DR   Genevestigator; Q923L3; -.
DR   GermOnline; ENSMUSG00000060924; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR016060; Complement_control_module.
DR   InterPro; IPR000859; CUB.
DR   InterPro; IPR000436; Sushi_SCR_CCP.
DR   Gene3D; G3DSA:2.10.70.10; Complement_control_module; 28.
DR   Gene3D; G3DSA:2.60.120.290; CUB; 14.
DR   Pfam; PF00431; CUB; 14.
DR   Pfam; PF00084; Sushi; 28.
DR   SMART; SM00032; CCP; 28.
DR   SMART; SM00042; CUB; 14.
DR   SUPFAM; SSF57535; Complement_control_module; 28.
DR   SUPFAM; SSF49854; CUB; 14.
DR   PROSITE; PS01180; CUB; 14.
DR   PROSITE; PS50923; SUSHI; 28.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Membrane; Repeat;
KW   Signal; Sushi; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     29       Potential.
FT   CHAIN        30   3564       CUB and sushi domain-containing protein
FT                                1.
FT                                /FTId=PRO_0000021026.
FT   TOPO_DOM     30   3487       Extracellular (Potential).
FT   TRANSMEM   3488   3508       Helical; (Potential).
FT   TOPO_DOM   3509   3564       Cytoplasmic (Potential).
FT   DOMAIN       32    140       CUB 1.
FT   DOMAIN      143    204       Sushi 1.
FT   DOMAIN      208    312       CUB 2.
FT   DOMAIN      347    408       Sushi 2.
FT   DOMAIN      411    522       CUB 3.
FT   DOMAIN      525    582       Sushi 3.
FT   DOMAIN      584    692       CUB 4.
FT   DOMAIN      695    756       Sushi 4.
FT   DOMAIN      758    866       CUB 5.
FT   DOMAIN      871    928       Sushi 5.
FT   DOMAIN      930   1040       CUB 6.
FT   DOMAIN     1043   1102       Sushi 6.
FT   DOMAIN     1104   1212       CUB 7.
FT   DOMAIN     1215   1275       Sushi 7.
FT   DOMAIN     1277   1386       CUB 8.
FT   DOMAIN     1389   1449       Sushi 8.
FT   DOMAIN     1451   1559       CUB 9.
FT   DOMAIN     1562   1623       Sushi 9.
FT   DOMAIN     1625   1733       CUB 10.
FT   DOMAIN     1739   1800       Sushi 10.
FT   DOMAIN     1802   1910       CUB 11.
FT   DOMAIN     1913   1972       Sushi 11.
FT   DOMAIN     1974   2082       CUB 12.
FT   DOMAIN     2085   2144       Sushi 12.
FT   DOMAIN     2146   2257       CUB 13.
FT   DOMAIN     2256   2317       Sushi 13.
FT   DOMAIN     2319   2430       CUB 14.
FT   DOMAIN     2430   2492       Sushi 14.
FT   DOMAIN     2493   2554       Sushi 15.
FT   DOMAIN     2555   2619       Sushi 16.
FT   DOMAIN     2620   2677       Sushi 17.
FT   DOMAIN     2678   2735       Sushi 18.
FT   DOMAIN     2736   2793       Sushi 19.
FT   DOMAIN     2794   2856       Sushi 20.
FT   DOMAIN     2857   2914       Sushi 21.
FT   DOMAIN     2918   2975       Sushi 22.
FT   DOMAIN     2976   3034       Sushi 23.
FT   DOMAIN     3035   3094       Sushi 24.
FT   DOMAIN     3095   3152       Sushi 25.
FT   DOMAIN     3153   3210       Sushi 26.
FT   DOMAIN     3214   3272       Sushi 27.
FT   DOMAIN     3273   3332       Sushi 28.
FT   CARBOHYD     40     40       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     57     57       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    587    587       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    686    686       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    955    955       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1015   1015       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1034   1034       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1184   1184       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1197   1197       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1399   1399       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1454   1454       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1572   1572       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1644   1644       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1792   1792       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1805   1805       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1882   1882       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2018   2018       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2149   2149       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2154   2154       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2187   2187       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2358   2358       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2394   2394       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2400   2400       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2445   2445       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2470   2470       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2503   2503       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2605   2605       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2750   2750       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2761   2761       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2795   2795       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2894   2894       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2963   2963       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3022   3022       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3056   3056       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3086   3086       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3228   3228       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3260   3260       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3339   3339       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3379   3379       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   3386   3386       N-linked (GlcNAc...) (Potential).
FT   DISULFID     32     58       By similarity.
FT   DISULFID    145    185       By similarity.
FT   DISULFID    171    202       By similarity.
FT   DISULFID    208    234       By similarity.
FT   DISULFID    349    389       By similarity.
FT   DISULFID    375    406       By similarity.
FT   DISULFID    411    437       By similarity.
FT   DISULFID    527    567       By similarity.
FT   DISULFID    553    580       By similarity.
FT   DISULFID    584    610       By similarity.
FT   DISULFID    697    738       By similarity.
FT   DISULFID    723    754       By similarity.
FT   DISULFID    758    784       By similarity.
FT   DISULFID    873    913       By similarity.
FT   DISULFID    899    926       By similarity.
FT   DISULFID    930    956       By similarity.
FT   DISULFID   1045   1085       By similarity.
FT   DISULFID   1071   1100       By similarity.
FT   DISULFID   1104   1130       By similarity.
FT   DISULFID   1217   1258       By similarity.
FT   DISULFID   1244   1273       By similarity.
FT   DISULFID   1277   1304       By similarity.
FT   DISULFID   1391   1431       By similarity.
FT   DISULFID   1417   1447       By similarity.
FT   DISULFID   1451   1477       By similarity.
FT   DISULFID   1564   1604       By similarity.
FT   DISULFID   1590   1621       By similarity.
FT   DISULFID   1625   1651       By similarity.
FT   DISULFID   1741   1781       By similarity.
FT   DISULFID   1767   1798       By similarity.
FT   DISULFID   1802   1828       By similarity.
FT   DISULFID   1915   1955       By similarity.
FT   DISULFID   1941   1970       By similarity.
FT   DISULFID   1974   2000       By similarity.
FT   DISULFID   2087   2127       By similarity.
FT   DISULFID   2113   2142       By similarity.
FT   DISULFID   2146   2172       By similarity.
FT   DISULFID   2258   2300       By similarity.
FT   DISULFID   2286   2315       By similarity.
FT   DISULFID   2319   2347       By similarity.
FT   DISULFID   2432   2473       By similarity.
FT   DISULFID   2459   2490       By similarity.
FT   DISULFID   2495   2537       By similarity.
FT   DISULFID   2521   2552       By similarity.
FT   DISULFID   2557   2602       By similarity.
FT   DISULFID   2588   2617       By similarity.
FT   DISULFID   2622   2662       By similarity.
FT   DISULFID   2648   2675       By similarity.
FT   DISULFID   2680   2720       By similarity.
FT   DISULFID   2706   2733       By similarity.
FT   DISULFID   2738   2778       By similarity.
FT   DISULFID   2764   2791       By similarity.
FT   DISULFID   2796   2841       By similarity.
FT   DISULFID   2827   2854       By similarity.
FT   DISULFID   2859   2899       By similarity.
FT   DISULFID   2885   2912       By similarity.
FT   DISULFID   2920   2960       By similarity.
FT   DISULFID   2946   2973       By similarity.
FT   DISULFID   2978   3019       By similarity.
FT   DISULFID   3005   3032       By similarity.
FT   DISULFID   3037   3079       By similarity.
FT   DISULFID   3063   3092       By similarity.
FT   DISULFID   3097   3137       By similarity.
FT   DISULFID   3123   3150       By similarity.
FT   DISULFID   3155   3195       By similarity.
FT   DISULFID   3181   3208       By similarity.
FT   DISULFID   3216   3257       By similarity.
FT   DISULFID   3243   3270       By similarity.
FT   DISULFID   3275   3317       By similarity.
FT   DISULFID   3302   3330       By similarity.
FT   VAR_SEQ     102   3564       Missing (in isoform 3).
FT                                /FTId=VSP_009036.
FT   VAR_SEQ    3332   3347       SKGVREVNETVTKTPV -> I (in isoform 2).
FT                                /FTId=VSP_009037.
SQ   SEQUENCE   3564 AA;  387870 MW;  70824C55B0674609 CRC64;
     MTAWRKFKSL LLPLVLAVLC AGLLTAAKGQ NCGGLVQGPN GTIESPGFPH GYPNYANCTW
     IIITGERNRI QLSFHTFALE EDFDILSVYD GQPQQGNLKV RLSGFQLPSS IVSTGSLLTL
     WFTTDFAVSA QGFKAMYEVL PSHTCGNPGE ILKGVLHGTR FNIGDKIRYS CLSGYILEGH
     AILTCIVSPG NGASWDFPAP FCRAEGACGG TLRGTSGSIS SPHFPSEYDN NADCTWTILA
     EPGDTIALVF TDFQLEEGYD FLEISGTEAP SIWLTGMNLP SPVISSKNWL RLHFTSDSNH
     RRKGFNAQFQ VKKAIELKSR GVKMLPSKDS SHKNSVLTQG GVSLISDMCP DPGIPDNGRR
     AGSDFRVGAN VQFSCEDNYV LQGAKGITCQ RVTETLAAWN DHRPICRART CGSNLRGPSG
     VITSPNYPVQ YEDNAHCVWV ITTTDPDKVI KLAFEEFELE RGYDTLTVGD AGKVGDTRSV
     LYVLTGSSVP DLIVSMSNQM WLHLQSDDSI GSPGFKAVYQ EIEKGGCGDP GIPAYGKRTG
     SSFLHGDTLT FECQAAFELV GERVITCQKN NQWSGNKPSC VFSCFFNFTA PSGIILSPNY
     PEEYGNNMNC VWLIISEPGS RIHLIFKDFD VEPQFDFLAV KDDGISDITV LGTFSGNEVP
     AQLASSGHIV RLEFQSDHST TGRGFNITYT TFGQNECHDP GIPVNGRRFG DRFLLGSSVS
     FHCDDGFVKT QGSESITCIL QDGNVVWSST VPRCEAPCGG HLTASSGVIL PPGWPGYYKD
     SLNCEWVIEA KPGHSIKITF DRFQTEVNYD TLEVRDGPTS SSPLIGEYHG TQAPQFLIST
     GNYMYLLFTT DSSRASVGFL IHYESVTLES DSCLDPGIPV NGQRHGSNFG IRSTVTFSCD
     PGYTLSDDEP LVCEKNHQWN HALPSCDALC GGYIHGKSGT VLSPGFPDFY PNSLNCTWTI
     EVSHGKGVQM NFHTFHLESS HDYLLITEDG SFSEPVARLT GSVLPHTIKA GLFGNFTAQL
     RFISDFSISY EGFNITFAEY DLEPCDDPGV PAFSRRIGFQ FGVGDTLAFT CFQGYRLEGA
     TKLTCLGGGR RVWSAPLPRC VAECGASVKG NEGTLLSPNF PSHYDNNHEC IYKIETEAGK
     GIHLRARTFQ LFEGDTLKVY DGKDSSSRSL GVFTRSEFMG LVLNSTSNYL RLEFNTNGSD
     TAQGFQLTYT SFDLVKCEDP GIPNYGYRIR DDGHFTDTVV LYSCNPGYAM HGSSTLTCLS
     GDRRVWDKPM PSCVAECGGL VHAATSGRIL SPGYPAPYDN NLHCTWTIEA DPGKTISLHF
     IVFDTETAHD ILKVWDGPVD SNILLKEWSG SALPEDIHST FNSLTLQFDS DFFISKSGFS
     IQFSTSIAST CNDPGMPQNG TRYGDSREPG DTITFQCDPG YQLQGPAKIT CVQLNNRFFW
     QPDPPSCIAA CGGNLTGPAG VILSPNYPQP YPPGKECDWR IKVNPDFVIA LIFKSFSMEP
     SYDFLHIYEG EDSNSPLIGS FQGSQAPERI ESSGNSLFLA FRSDASVGLS GFAIEFKEKP
     REACFDPGNI MNGTRIGTDF KLGSTVTYQC DSGYKIVDPS SIECVTGADG KPSWDRALPA
     CQAPCGGQYT GSEGVVLSPN YPHNYTAGQM CVYSITVPKE FVVFGQFAYF QTALNDLAEL
     FDGTHPQARL LSSLSGSHSG ETLPLATSNQ ILLRFSAKSG ASARGFHFVY QAVPRTSDTQ
     CSSVPEPRYG RRIGSEFSAG SIVRFECNPG YLLQGSTAIR CQSVPNALAQ WNDTIPSCVV
     PCSGNFTQRR GTILSPGYPE PYGNNLNCVW KIIVSEGSGI QIQVISFATE QNWDSLEIHD
     GGDMTAPRLG SFSGTTVPAL LNSTSNQLCL HFQSDISVAA AGFHLEYKTV GLAACQEPAL
     PSNGIKIGDR YMVNDVLSFQ CEPGYTLQGR SHISCMPGTV RRWNYPSPLC IATCGGTLTS
     MSGVILSPGF PGSYPNNLDC TWKISLPIGY GAHIQFLNFS TEANHDYLEI QNGPYHSSPM
     MGQFSGPDLP TSLLSTTHET LIRFYSDHSQ NRQGFKLSYQ AYELQNCPDP PAFQNGFMIN
     SDYSVGQSIS FECYPGYILL GHPVLTCQHG TDRNWNYPFP RCDAPCGYNV TSQNGTIYSP
     GFPDEYPILK DCLWLVTVPP GHGVYINFTL LQTEAVNDYI AVWDGPDQNS PQLGVFSGNT
     APETAYSSTN QVLLKFHSDF SNGGFFVLNF HAFQLKRCPP PPAVPQADLL TEDEDFEIGD
     FVKYQCHPGY TLLGSDTLTC KLSSQLLFQG SPPTCEAQCP ANEVRTESSG VILSPGYPGN
     YFNSQTCAWS IKVKPNFNIT LFVDTFQSEK QFDALEVFDG SSGRSPLLVV LSGNHTEQSN
     FTSRSNHLYL RWSTDHATSK KGFKIRYAAP YCSLTSTLRN GGILNKTAGA VGSKVHYFCK
     PGYRMIGHSN ATCRRNPVGV YQWDSMAPLC QAVSCGIPEA PGNGSFTGNE FTLDSKVTYE
     CNEGFKLDAS QEATTVCQED GLWSNRGKPP TCKPVPCPSI EGQLSEHVLW RLVSGSLNEY
     GAQVLLSCSP GYFLQGQRLL QCQANGTWST EEDRPRCKVI SCGSLSFPPN GNKIGTLTIY
     GATAIFTCNT GYTLVGSHVR ECLANGLWSG SETRCLAGHC GSPDPIVNGH ISGDGFSYRD
     TVVYQCNPGF RLVGTSVRIC CRTTSGRGRL TVCVPITCGH PGNPAHGLTN GTEFNLNDLV
     NFTCHTGYRL QGASRAQCRS NGQWSSPLPI CRVVNCSDPG SVENAVRHGQ QNFPESFEYG
     TSVMYHCKTG FYLLGSSALT CMASGLWDRS LPKCLAISCG HPGVPANAVL TGELFTYGAT
     VQYSCKGGQI LTGNSTRVCQ EDSHWSGSLP HCSGNSPGFC GDPGTPAHGS RLGDEFKTKS
     LLRFSCEMGH QLRGFAERTC LVNGSWSGVQ PVCEAVSCGN PGTPTNGMIL SSDGILFSSS
     VIYACWEGYK TSGLMTRHCT ANGTWTGTAP DCTIISCGDP GTLPNGIQFG TDFTFNKTVS
     YQCNPGYLME PPTSPTIRCT KDGTWNQSRP LCKAVLCNQP PPVPNGKVEG SDFRWGASIS
     YSCVDGYQLS HSAILSCEGR GVWKGEVPQC LPVFCGDPGT PAEGRLSGKS FTFKSEVFIQ
     CKPPFVLVGS SRRTCQADGI WSGIQPTCID PAHTACPDPG TPHFGIQNSS KGYEVGSTVF
     FRCRKGYHIQ GSTTRTCLAN LTWSGIQTEC IPHACRQPET PAHADVRAID LPAFGYTLVY
     TCHPGFFLAG GSEHRTCKAD MKWTGKSPVC KSKGVREVNE TVTKTPVPSD VFFINSVWKG
     YYEYLGKRQP ATLTVDWFNA TSSKVNATFT AASRVQLELT GVYKKEEAHL LLKAFHIKGP
     ADIFVSKFEN DNWGLDGYVS SGLERGGFSF QGDIHGKDFG KFKLERQDPS NSDADSSNHY
     QGTSSGSVAA AILVPFFALI LSGFAFYLYK HRTRPKVQYN GYAGHENSNG QASFENPMYD
     TNLKPTEAKA VRFDTTLNTV CTVV
//
ID   PP16A_MOUSE             Reviewed;         524 AA.
AC   Q923M0; Q4V9Z1;
DT   13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 16A;
DE   AltName: Full=Myosin phosphatase targeting subunit 3;
DE   Flags: Precursor;
GN   Name=Ppp1r16a; Synonyms=Mypt3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ISOPRENYLATION AT CYS-521.
RX   MEDLINE=21234869; PubMed=11336659; DOI=10.1042/0264-6021:3560257;
RA   Skinner J.A., Saltiel A.R.;
RT   "Cloning and identification of MYPT3: a prenylatable myosin targeting
RT   subunit of protein phosphatase 1.";
RL   Biochem. J. 356:257-267(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-433, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Inhibits protein phosphatase 1 activity toward
CC       phosphorylase, myosin light chain and myosin substrates.
CC   -!- SUBUNIT: Binds PP1.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis, followed by liver,
CC       heart, brain and lung.
CC   -!- SIMILARITY: Contains 5 ANK repeats.
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DR   EMBL; AY010723; AAG40949.1; -; mRNA.
DR   EMBL; BC057450; AAH57450.1; -; mRNA.
DR   EMBL; BC096620; AAH96620.1; -; mRNA.
DR   IPI; IPI00124473; -.
DR   RefSeq; NP_203535.1; NM_033371.2.
DR   UniGene; Mm.322901; -.
DR   ProteinModelPortal; Q923M0; -.
DR   SMR; Q923M0; 22-323.
DR   STRING; Q923M0; -.
DR   PhosphoSite; Q923M0; -.
DR   PRIDE; Q923M0; -.
DR   Ensembl; ENSMUST00000037551; ENSMUSP00000037356; ENSMUSG00000033819.
DR   GeneID; 73062; -.
DR   KEGG; mmu:73062; -.
DR   UCSC; uc007wlo.1; mouse.
DR   CTD; 73062; -.
DR   MGI; MGI:1920312; Ppp1r16a.
DR   GeneTree; ENSGT00600000084108; -.
DR   HOGENOM; HBG443814; -.
DR   HOVERGEN; HBG053644; -.
DR   InParanoid; Q923M0; -.
DR   OMA; DVCGDEE; -.
DR   OrthoDB; EOG434W62; -.
DR   PhylomeDB; Q923M0; -.
DR   NextBio; 337395; -.
DR   ArrayExpress; Q923M0; -.
DR   Bgee; Q923M0; -.
DR   Genevestigator; Q923M0; -.
DR   GermOnline; ENSMUSG00000033819; Mus musculus.
DR   GO; GO:0005829; C:cytosol; TAS:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR017417; Pase-1_reg_su_16AB_euk.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 2.
DR   Pfam; PF00023; Ank; 4.
DR   PIRSF; PIRSF038159; PP1_16AB_vert; 1.
DR   SMART; SM00248; ANK; 5.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
PE   1: Evidence at protein level;
KW   ANK repeat; Cell membrane; Coiled coil; Lipoprotein; Membrane;
KW   Methylation; Palmitate; Phosphoprotein; Prenylation; Repeat.
FT   CHAIN         1    521       Protein phosphatase 1 regulatory subunit
FT                                16A.
FT                                /FTId=PRO_0000067041.
FT   PROPEP      522    524       Removed in mature form (Probable).
FT                                /FTId=PRO_0000396708.
FT   REPEAT       70     99       ANK 1.
FT   REPEAT      103    132       ANK 2.
FT   REPEAT      136    165       ANK 3.
FT   REPEAT      231    260       ANK 4.
FT   REPEAT      264    293       ANK 5.
FT   COILED      448    469       Potential.
FT   MOD_RES     433    433       Phosphotyrosine.
FT   MOD_RES     521    521       Cysteine methyl ester (Probable).
FT   LIPID       520    520       S-palmitoyl cysteine (Probable).
FT   LIPID       521    521       S-farnesyl cysteine (Probable).
SQ   SEQUENCE   524 AA;  57530 MW;  A0F682A794475429 CRC64;
     MAEHLELLAE MPMVGRMSTQ ERLKHAQKRR AQQVKMWAQA EKEAHSKKGH GERPWKEVAG
     LRPRKHVLFP PSVALLEAAA RNDLEEVRQF LTSGVSPNLA NEDGLTALHQ CCIDDFQEMA
     QQLLDAGADV NARDSECWTP LHAAATCGHL HLVELLISRG ADLLAVNSDG NMPYDLCEDA
     QTLDCLETAM ANQGITQEGI EEARAVPELC MLNDLQNRLQ AGANLSDPLD HGATLLHIAA
     ANGFSEVATL LLEQGASLSA KDHDGWEPLH AAAYWGQVHL VELLVAHGAD LNGKSLVDET
     PLDVCGDEEV RAKLLELKHK QDALLRAQGR QRSLLRRRTS SAGSRGKVVR RVSLTHRTNL
     YRKEHAQEAI VWQQPPPTSP EPLEDEDRQT DAELRLQPPE DDGPEVARPH NGQVGAPPGR
     HLYSKRLDRS VSYHLSPEEN SAPDALVRDK AHHTLAELKR QRAAAKLQRP APEGPETFEP
     GLSVDAGTSQ PDCGFSTIGD PPLLKLTAPS EEASVEKRPC CLLM
//
ID   KCC2G_MOUSE             Reviewed;         529 AA.
AC   Q923T9; Q3U3H3; Q8VED3;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Calcium/calmodulin-dependent protein kinase type II subunit gamma;
DE            Short=CaM kinase II subunit gamma;
DE            Short=CaMK-II subunit gamma;
DE            EC=2.7.11.17;
GN   Name=Camk2g;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6;
RA   Szendro P.I., Cadenas C., Eichele G.;
RT   "Identification of a mouse Ca2+/calmodulin-dependent protein kinase
RT   II.";
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=NOD; TISSUE=Dendritic cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-287, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND THR-287, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: CaM-kinase II (CAMK2) is a prominent kinase in the
CC       central nervous system that may function in long-term potentiation
CC       and neurotransmitter release.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Autophosphorylation of CAMK2 plays an important
CC       role in the regulation of the kinase activity.
CC   -!- SUBUNIT: CAMK2 is composed of four different chains: alpha, beta,
CC       gamma, and delta. The different isoforms assemble into homo- or
CC       heteromultimeric holoenzymes composed of 8 to 12 subunits.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1;
CC         IsoId=Q923T9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q923T9-2; Sequence=VSP_004779;
CC       Name=3;
CC         IsoId=Q923T9-3; Sequence=VSP_004780;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. CaMK subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF395884; AAK84142.1; -; mRNA.
DR   EMBL; AK154764; BAE32813.1; -; mRNA.
DR   EMBL; BC019162; AAH19162.1; -; mRNA.
DR   EMBL; BC025597; AAH25597.1; -; mRNA.
DR   IPI; IPI00124695; -.
DR   IPI; IPI00228044; -.
DR   IPI; IPI00228045; -.
DR   RefSeq; NP_001034227.1; NM_001039138.1.
DR   RefSeq; NP_001034228.1; NM_001039139.1.
DR   RefSeq; NP_848712.2; NM_178597.4.
DR   UniGene; Mm.235182; -.
DR   ProteinModelPortal; Q923T9; -.
DR   SMR; Q923T9; 3-302, 389-523.
DR   STRING; Q923T9; -.
DR   PhosphoSite; Q923T9; -.
DR   PRIDE; Q923T9; -.
DR   Ensembl; ENSMUST00000071816; ENSMUSP00000071720; ENSMUSG00000021820.
DR   Ensembl; ENSMUST00000080440; ENSMUSP00000079298; ENSMUSG00000021820.
DR   Ensembl; ENSMUST00000100837; ENSMUSP00000098398; ENSMUSG00000021820.
DR   GeneID; 12325; -.
DR   KEGG; mmu:12325; -.
DR   UCSC; uc007skt.1; mouse.
DR   UCSC; uc007sku.1; mouse.
DR   UCSC; uc007skv.1; mouse.
DR   CTD; 12325; -.
DR   MGI; MGI:88259; Camk2g.
DR   eggNOG; roNOG13785; -.
DR   GeneTree; ENSGT00550000074354; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108055; -.
DR   InParanoid; Q923T9; -.
DR   OMA; APSTGMQ; -.
DR   OrthoDB; EOG42JNR7; -.
DR   PhylomeDB; Q923T9; -.
DR   BRENDA; 2.7.11.17; 244.
DR   NextBio; 280908; -.
DR   ArrayExpress; Q923T9; -.
DR   Bgee; Q923T9; -.
DR   Genevestigator; Q923T9; -.
DR   GermOnline; ENSMUSG00000021820; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:EC.
DR   GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IMP:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; IMP:MGI.
DR   InterPro; IPR013543; Ca/CaM-dep_prot_kinase-assoc.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF08332; CaMKII_AD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Calmodulin-binding; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN         1    529       Calcium/calmodulin-dependent protein
FT                                kinase type II subunit gamma.
FT                                /FTId=PRO_0000086102.
FT   DOMAIN       14    272       Protein kinase.
FT   NP_BIND      20     28       ATP (By similarity).
FT   REGION      291    301       Calmodulin-binding (By similarity).
FT   ACT_SITE    136    136       Proton acceptor (By similarity).
FT   BINDING      43     43       ATP (By similarity).
FT   MOD_RES     235    235       Phosphoserine.
FT   MOD_RES     287    287       Phosphothreonine.
FT   MOD_RES     307    307       Phosphothreonine (By similarity).
FT   MOD_RES     311    311       Phosphoserine (By similarity).
FT   MOD_RES     315    315       Phosphoserine (By similarity).
FT   MOD_RES     319    319       Phosphoserine (By similarity).
FT   MOD_RES     325    325       Phosphoserine (By similarity).
FT   MOD_RES     349    349       Phosphoserine (By similarity).
FT   MOD_RES     352    352       Phosphoserine (By similarity).
FT   MOD_RES     375    375       Phosphothreonine (By similarity).
FT   MOD_RES     381    381       Phosphoserine (By similarity).
FT   MOD_RES     382    382       Phosphothreonine (By similarity).
FT   MOD_RES     384    384       Phosphoserine (By similarity).
FT   MOD_RES     387    387       Phosphothreonine (By similarity).
FT   MOD_RES     388    388       Phosphothreonine (By similarity).
FT   VAR_SEQ     331    364       Missing (in isoform 3).
FT                                /FTId=VSP_004780.
FT   VAR_SEQ     331    341       Missing (in isoform 2).
FT                                /FTId=VSP_004779.
SQ   SEQUENCE   529 AA;  59607 MW;  EE1D127BBA178544 CRC64;
     MATTATCTRF TDDYQLFEEL GKGAFSVVRR CVKKTSTQEY AAKIINTKKL SARDHQKLER
     EARICRLLKH PNIVRLHDSI SEEGFHYLVF DLVTGGELFE DIVAREYYSE ADASHCIHQI
     LESVNHIHQH DIVHRDLKPE NLLLASKCKG AAVKLADFGL AIEVQGEQQA WFGFAGTPGY
     LSPEVLRKDP YGKPVDIWAC GVILYILLVG YPPFWDEDQH KLYQQIKAGA YDFPSPEWDT
     VTPEAKNLIN QMLTINPAKR ITADQALKHP WVCQRSTVAS MMHRQETVEC LRKFNARRKL
     KGAILTTMLV SRNFSAAKSL LNKKSDGGVK KRKSSSSVHL MPQSNNKNSL VSPAQEPAPL
     QTAMEPQTTV VHNATDGIKG STESCNTTTE DEDLKVRKQE IIKITEQLIE AINNGDFEAY
     TKICDPGLTS FEPEALGNLV EGMDFHKFYF ENLLSKNSKP IHTTILNPHV HVIGEDAACI
     AYIRLTQYID GQGRPRTSQS EETRVWHRRD GKWLNVHYHC SGAPAAPLQ
//
ID   TM1L1_MOUSE             Reviewed;         474 AA.
AC   Q923U0; B0QZV4; Q5SRC7; Q5SRC9; Q99KE0; Q9D6Y5;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=TOM1-like protein 1;
DE   AltName: Full=Src-activating and signaling molecule protein;
DE   AltName: Full=Target of Myb-like protein 1;
GN   Name=Tom1l1; Synonyms=Srcasm;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, PHOSPHORYLATION, AND
RP   MUTAGENESIS OF TYR-392; 440-TYR-TYR-441 AND TYR-457.
RC   STRAIN=C57BL/6J; TISSUE=Keratinocyte;
RX   MEDLINE=21659738; PubMed=11711534; DOI=10.1074/jbc.M106813200;
RA   Seykora J.T., Mei L., Dotto G.P., Stein P.L.;
RT   "'Srcasm: a novel Src activating and signaling molecule.";
RL   J. Biol. Chem. 277:2812-2822(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Carcinoma;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Probable adapter protein involved in signaling pathways.
CC       Interacts with the SH2 and SH3 domains of various signaling
CC       proteins when it is phosphorylated. May promotes FYN activation,
CC       possibly by disrupting intramolecular SH3-dependent interactions.
CC   -!- SUBUNIT: Interacts with the SH2 and SH3 domains of FYN when
CC       phosphorylated. Also interacts with GRB2 and PIK3R1 when
CC       phosphorylated.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack. Endosome
CC       membrane (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q923U0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q923U0-2; Sequence=VSP_003996;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q923U0-3; Sequence=VSP_003997;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Strongly expressed in brain and kidney,
CC       expressed at intermediate levels skin and heart, and weakly
CC       expressed in thymus. Not expressed in liver and spleen.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity). Phosphorylated on tyrosines by FYN.
CC   -!- SIMILARITY: Belongs to the TOM1 family.
CC   -!- SIMILARITY: Contains 1 GAT domain.
CC   -!- SIMILARITY: Contains 1 VHS domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF395837; AAK83377.1; -; mRNA.
DR   EMBL; AK009826; BAB26526.1; -; mRNA.
DR   EMBL; AK083630; BAC38972.1; -; mRNA.
DR   EMBL; AL672199; CAI24236.1; -; Genomic_DNA.
DR   EMBL; AL672199; CAI24238.1; -; Genomic_DNA.
DR   EMBL; AL672199; CAQ12613.1; -; Genomic_DNA.
DR   EMBL; BC004710; AAH04710.1; -; mRNA.
DR   IPI; IPI00124710; -.
DR   IPI; IPI00230595; -.
DR   IPI; IPI00230596; -.
DR   UniGene; Mm.167868; -.
DR   ProteinModelPortal; Q923U0; -.
DR   SMR; Q923U0; 9-155, 158-291.
DR   STRING; Q923U0; -.
DR   PhosphoSite; Q923U0; -.
DR   PRIDE; Q923U0; -.
DR   Ensembl; ENSMUST00000020849; ENSMUSP00000020849; ENSMUSG00000020541.
DR   Ensembl; ENSMUST00000107869; ENSMUSP00000103501; ENSMUSG00000020541.
DR   UCSC; uc007kxa.1; mouse.
DR   UCSC; uc007kxc.1; mouse.
DR   MGI; MGI:1919193; Tom1l1.
DR   GeneTree; ENSGT00600000084107; -.
DR   HOGENOM; HBG388010; -.
DR   HOVERGEN; HBG025068; -.
DR   InParanoid; Q923U0; -.
DR   OMA; PSNHPAM; -.
DR   OrthoDB; EOG4HQDJ9; -.
DR   PhylomeDB; Q923U0; -.
DR   ArrayExpress; Q923U0; -.
DR   Bgee; Q923U0; -.
DR   CleanEx; MM_TOM1L1; -.
DR   Genevestigator; Q923U0; -.
DR   GermOnline; ENSMUSG00000020541; Mus musculus.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR   GO; GO:0030295; F:protein kinase activator activity; IDA:MGI.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:MGI.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR004152; GAT.
DR   InterPro; IPR014645; TOM1.
DR   InterPro; IPR002014; VHS.
DR   InterPro; IPR018205; VHS_subgroup.
DR   Gene3D; G3DSA:1.25.40.90; ENTH_VHS; 1.
DR   Pfam; PF03127; GAT; 1.
DR   Pfam; PF00790; VHS; 1.
DR   PIRSF; PIRSF036948; TOM1; 1.
DR   SMART; SM00288; VHS; 1.
DR   SUPFAM; SSF48464; ENTH_VHS; 1.
DR   PROSITE; PS50909; GAT; 1.
DR   PROSITE; PS50179; VHS; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endosome; Golgi apparatus; Membrane;
KW   Phosphoprotein; Protein transport; SH3-binding; Transport.
FT   CHAIN         1    474       TOM1-like protein 1.
FT                                /FTId=PRO_0000072567.
FT   DOMAIN       22    154       VHS.
FT   DOMAIN      199    287       GAT.
FT   REGION      392    395       Interaction with GRB2.
FT   REGION      441    444       Interaction with PIK3R1.
FT   MOTIF       420    424       SH3-binding.
FT   MOTIF       457    460       SH2-binding.
FT   MOD_RES     313    313       Phosphoserine (By similarity).
FT   MOD_RES     320    320       Phosphoserine (By similarity).
FT   MOD_RES     457    457       Phosphotyrosine.
FT   VAR_SEQ       1    247       Missing (in isoform 2).
FT                                /FTId=VSP_003996.
FT   VAR_SEQ     125    200       Missing (in isoform 3).
FT                                /FTId=VSP_003997.
FT   MUTAGEN     392    392       Y->F: Specifically abolishes interaction
FT                                with GRB2; mild decrease in
FT                                phosphorylation.
FT   MUTAGEN     440    441       YY->FF: Specifically abolishes
FT                                interaction with PIK3R1; mild decrease in
FT                                phosphorylation.
FT   MUTAGEN     457    457       Y->F: Abolishes phosphorylation by FYN
FT                                and interaction with FYN.
FT   CONFLICT    414    414       A -> V (in Ref. 2; BAB26526).
SQ   SEQUENCE   474 AA;  52695 MW;  4663AD9C0E6C292C CRC64;
     MAFGKSHRDP YATSVGHLIE KATFAGVLTE DWGQFLHICD IINTTQDGPK DAVKALKKRI
     SKNYNHKEIQ LSLSLIDMCV QNCGPSFQSL IVKKEFIKDT LVKLLNPRYT LPLETQNRIL
     NFIKTWSQGF PGGVDVSEVK EVYLDLLKKG VQFPPSDGEP ETRQEAGQIS PNRPTSVPTA
     PALSSIIAPK NPTISLVPEQ IGKLHSELDM VKMNVKVMTA ILMENTPGSE NHEDIELLRK
     LYKTGREMQE RIMDLLVVVE NEDVTMELIQ VNEDLNNAVL GYERFTRNQQ RLLEQKRNRT
     EATRTSSEPS APSCDLLDLS PIVPVPTPNE GALNSVNAQL SGLSVSSLSP VITNNLYPSL
     QPQRDLLASE DIEIPTLFPQ RTSQNLASSH TYDNFHSNSV LLQPVSLHTA TAAAAANQRL
     PPLPSSHPVL KDGDLQPPNY YEVMEFDPLA PTTEAVYEEI DGYHQKEAQS HSDC
//
ID   TGS1_MOUSE              Reviewed;         853 AA.
AC   Q923W1; A2AJF7; Q6DI60; Q6PEA7; Q8R0W9;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 2.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Trimethylguanosine synthase;
DE            EC=2.1.1.-;
DE   AltName: Full=Nuclear receptor coactivator 6-interacting protein;
DE   AltName: Full=PRIP-interacting protein with methyltransferase motif;
DE            Short=PIMT;
DE            Short=PIPMT;
GN   Name=Tgs1; Synonyms=Ncoa6ip, Pimt;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH NCOA6,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Spleen;
RX   MEDLINE=21417756; PubMed=11517327; DOI=10.1073/pnas.181347498;
RA   Zhu Y.-J., Qi C., Cao W.-Q., Yeldandi A.V., Rao M.S., Reddy J.K.;
RT   "Cloning and characterization of PIMT, a protein with a
RT   methyltransferase domain, which interacts with and enhances nuclear
RT   receptor coactivator PRIP function.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:10380-10385(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Limb, Liver, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Catalyzes the 2 serial methylation steps for the
CC       conversion of the 7-monomethylguanosine (m(7)G) caps of snRNAs and
CC       snoRNAs to a 2,2,7-trimethylguanosine (m(2,2,7)G) cap structure.
CC       The enzyme is specific for guanine, and N7 methylation must
CC       precede N2 methylation. Hypermethylation of the m7G cap of U
CC       snRNAs leads to their concentration in nuclear foci, their
CC       colocalization with coilin and the formation of canonical Cajal
CC       bodies (CBs). Plays a role in transcriptional regulation (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + m(7)G(5')pppR-RNA =
CC       S-adenosyl-L-homocysteine + m(2,7)G(5')pppR-RNA.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + m(2,7)G(5')pppR-RNA
CC       = S-adenosyl-L-homocysteine + m(2,2,7)G(5')pppR-RNA.
CC   -!- SUBUNIT: May form homooligomers. Interacts with CREBBP/CBP,
CC       EED/WAIT1, EP300/P300, NCOA6/PRIP, PPARBP/PBP and SMN (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus, Cajal
CC       body.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       Trimethylguanosine synthase family.
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DR   EMBL; AF389908; AAK84355.1; -; mRNA.
DR   EMBL; AL732617; CAM17201.1; -; Genomic_DNA.
DR   EMBL; BC026368; AAH26368.1; -; mRNA.
DR   EMBL; BC058183; AAH58183.1; -; mRNA.
DR   EMBL; BC075728; AAH75728.1; -; mRNA.
DR   IPI; IPI00124779; -.
DR   RefSeq; NP_473430.3; NM_054089.4.
DR   UniGene; Mm.171323; -.
DR   ProteinModelPortal; Q923W1; -.
DR   SMR; Q923W1; 626-836.
DR   STRING; Q923W1; -.
DR   PhosphoSite; Q923W1; -.
DR   PRIDE; Q923W1; -.
DR   Ensembl; ENSMUST00000052712; ENSMUSP00000054112; ENSMUSG00000028233.
DR   GeneID; 116940; -.
DR   KEGG; mmu:116940; -.
DR   UCSC; uc008rwi.1; mouse.
DR   CTD; 116940; -.
DR   MGI; MGI:2151797; Tgs1.
DR   eggNOG; roNOG14810; -.
DR   GeneTree; ENSGT00390000018056; -.
DR   HOGENOM; HBG716472; -.
DR   HOVERGEN; HBG059797; -.
DR   InParanoid; Q923W1; -.
DR   OMA; CSRAFVE; -.
DR   OrthoDB; EOG43TZTV; -.
DR   PhylomeDB; Q923W1; -.
DR   NextBio; 369376; -.
DR   ArrayExpress; Q923W1; -.
DR   Bgee; Q923W1; -.
DR   Genevestigator; Q923W1; -.
DR   GermOnline; ENSMUSG00000028233; Mus musculus.
DR   GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0009452; P:RNA capping; IEA:InterPro.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR019012; RNA_cap_Gua-N2-MeTrfase.
DR   Pfam; PF09445; Methyltransf_15; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Methyltransferase; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    853       Trimethylguanosine synthase.
FT                                /FTId=PRO_0000204469.
FT   COMPBIAS    612    622       Lys-rich.
FT   BINDING     711    711       S-adenosyl-L-methionine (By similarity).
FT   MOD_RES      61     61       Phosphothreonine (By similarity).
FT   MOD_RES      81     81       Phosphoserine (By similarity).
FT   MOD_RES      85     85       Phosphoserine (By similarity).
FT   MOD_RES     152    152       Phosphoserine (By similarity).
FT   MOD_RES     295    295       Phosphoserine (By similarity).
FT   MOD_RES     405    405       Phosphoserine (By similarity).
FT   MOD_RES     431    431       Phosphoserine.
FT   CONFLICT    512    512       F -> L (in Ref. 3; AAH75728).
FT   CONFLICT    633    633       V -> G (in Ref. 1; AAK84355).
SQ   SEQUENCE   853 AA;  96790 MW;  A69974BE660DA3AF CRC64;
     MCCEKWNHVA EMLLFIEDRE EEYKILCLCS RAFVEDRKLY NLGLKGYYVK SSGNNAGDQG
     TEEEEDGHSN GTAESHSPNE SDLDSEAKLM RSMGLPIQFG RMSSHENFEM SMNARNKAKV
     KQKRRKHQKR YLDEMVRESW RNDYEEDDLV VSDDPSSVEH CENNRTCEIQ SKAGSEVENL
     PVENTLAPKL EVPENWEKYW NEYGEGLLWQ SWQEKYPDQT LSSEPWNLPD TKEEWEQHYS
     QLYWYYLEQF QYWEAQGWTF TASQNCDKDV YTSHTEVDQN AESSLKADVM TFSSSPNIVE
     DEIPGSNDND HNEIITAINN ITVSAEKVEQ SQLDSSQHCD EPLSEITGKE CPASGGSDSC
     NGTPKENDIS ENRSSDQPAK ELQESSGTNK GKHRPHHNGA DGHESDDDPP EHKPSKVKRS
     HELDVDENPD SEVDDNGFLL GFKHGSGQKY GGIPNFSHRQ VRYLEKNVKY KSKYLDLRKQ
     MPVKSKHILF TEDSGKPFVV CKSKVRSKVE KFLKWVNERV DEETSQDSLS QNKMQDTCTS
     SDSEEQDMSL EKADNLMETR DPEPEKCQII SSATELEAEK SEVGSLVATV PENCSTEEIP
     NSPHAETEVE IKKKKKKNKN KKINDLPPEI ASVPELAKYW AQRYRLFSRF DDGIKLDKEG
     WFSVTPEKIA EHIAGRVSQA FRCDVVVDAF CGVGGNTIQF ALTGKRVIAI DIDPVKIDLA
     RNNAEVYGIA DKIEFICGDF LLLAPCLKAD VVFLSPPWGG PDYATAETFD IRTMMSPDGF
     EIFRLSQKIT NNIVYFLPRN ADIDQVASLA GLGGQVEIEQ NFLNNKLKTI TAYFGDLIRR
     PALLKTSTSE AEV
//
ID   GPC5B_MOUSE             Reviewed;         410 AA.
AC   Q923Z0; Q8CCV3;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=G-protein coupled receptor family C group 5 member B;
DE   AltName: Full=Retinoic acid-induced gene 2 protein;
DE            Short=RAIG-2;
DE   Flags: Precursor;
GN   Name=Gprc5b; Synonyms=Raig2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Tao Q., Lotan R.;
RT   "Molecular cloning and characterization of mouse retinoic acid-
RT   inducible orphan G protein-coupled receptors.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Unknown. This retinoic acid-inducible G-protein coupled
CC       receptor provide evidence for a possible interaction between
CC       retinoid and G-protein signaling pathways (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
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DR   EMBL; AF378831; AAK58076.1; -; mRNA.
DR   EMBL; AK032047; BAC27669.1; -; mRNA.
DR   EMBL; BC020004; AAH20004.1; -; mRNA.
DR   IPI; IPI00124890; -.
DR   RefSeq; NP_071865.1; NM_022420.2.
DR   UniGene; Mm.103439; -.
DR   STRING; Q923Z0; -.
DR   PhosphoSite; Q923Z0; -.
DR   PRIDE; Q923Z0; -.
DR   Ensembl; ENSMUST00000008878; ENSMUSP00000008878; ENSMUSG00000008734.
DR   GeneID; 64297; -.
DR   KEGG; mmu:64297; -.
DR   UCSC; uc009jkx.1; mouse.
DR   CTD; 64297; -.
DR   MGI; MGI:1927596; Gprc5b.
DR   eggNOG; roNOG10601; -.
DR   HOGENOM; HBG445102; -.
DR   HOVERGEN; HBG051794; -.
DR   InParanoid; Q923Z0; -.
DR   OMA; RRFLWGV; -.
DR   OrthoDB; EOG4229KM; -.
DR   PhylomeDB; Q923Z0; -.
DR   NextBio; 320021; -.
DR   ArrayExpress; Q923Z0; -.
DR   Bgee; Q923Z0; -.
DR   Genevestigator; Q923Z0; -.
DR   GermOnline; ENSMUSG00000008734; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR017978; GPCR_3_C.
DR   Pfam; PF00003; 7tm_3; 1.
DR   PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; FALSE_NEG.
DR   PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; FALSE_NEG.
DR   PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; FALSE_NEG.
DR   PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Receptor; Signal; Transducer; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     28       Potential.
FT   CHAIN        29    410       G-protein coupled receptor family C group
FT                                5 member B.
FT                                /FTId=PRO_0000012966.
FT   TOPO_DOM     29     56       Extracellular (Potential).
FT   TRANSMEM     57     77       Helical; Name=1; (Potential).
FT   TOPO_DOM     78     94       Cytoplasmic (Potential).
FT   TRANSMEM     95    115       Helical; Name=2; (Potential).
FT   TOPO_DOM    116    126       Extracellular (Potential).
FT   TRANSMEM    127    147       Helical; Name=3; (Potential).
FT   TOPO_DOM    148    164       Cytoplasmic (Potential).
FT   TRANSMEM    165    185       Helical; Name=4; (Potential).
FT   TOPO_DOM    186    199       Extracellular (Potential).
FT   TRANSMEM    200    220       Helical; Name=5; (Potential).
FT   TOPO_DOM    221    234       Cytoplasmic (Potential).
FT   TRANSMEM    235    255       Helical; Name=6; (Potential).
FT   TOPO_DOM    256    271       Extracellular (Potential).
FT   TRANSMEM    272    292       Helical; Name=7; (Potential).
FT   TOPO_DOM    293    410       Cytoplasmic (Potential).
FT   CARBOHYD     30     30       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    118    118       D -> G (in Ref. 2; BAC27669).
SQ   SEQUENCE   410 AA;  45899 MW;  E1DA5283270FFF34 CRC64;
     MFLVLERKMR THQVFPLPLL LVIASVASEN ASTSRGCGLD LLPQYVSLCD LDAIWGIVVE
     AVAGAGALIT LLLMLILLVR LPFIKDKERK RPVCLHFLFL LGTLGLFGLT FAFIIQMDET
     ICSIRRFLWG VLFALCFSCL LSQAWRVRRL VRQGTSPASW QLVSLALCLM LVQVIIATEW
     LVLTVLRDTK PACAYEPMDF VMALIYDMVL LAITLAQSLF TLCGKFKRWK VNGAFILVTT
     FLSALIWVVW MTMYLFGNSL IKQGDAWSDP TLAITLAASG WVFVIFHAIP EIHYTLLPPL
     QENPPNYFDT SQPRMRETAF DEEMHLPRAY MENKAFSMDE HNAALRSAVG FSNGSLEQRS
     SSLGKKPSSL GNRPSAPFRS NVYQPTEMAV VLNGGTIPTA PPSHTGRHHW
//
ID   CIC_MOUSE               Reviewed;        2510 AA.
AC   Q924A2; Q3UH79; Q3UHP4; Q6PDJ8; Q8CGE4; Q8CHH0; Q9CW61;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 2.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Protein capicua homolog;
GN   Name=Cic; Synonyms=Kiaa0306;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), POSSIBLE FUNCTION, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=12393275; DOI=10.1016/S0169-328X(02)00439-4;
RA   Lee C.-J., Chan W.-I., Cheung M., Cheng Y.-C., Appleby V.J.,
RA   Orme A.T., Scotting P.J.;
RT   "CIC, a member of a novel subfamily of the HMG-box superfamily, is
RT   transiently expressed in developing granule neurons.";
RL   Brain Res. Mol. Brain Res. 106:151-156(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1056-2510 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1662-2510 (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1162-2510 (ISOFORM 1).
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1809, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=15981098; DOI=10.1007/s11060-004-4598-2;
RA   Lee C.-J., Chan W.-I., Scotting P.J.;
RT   "CIC, a gene involved in cerebellar development and ErbB signaling, is
RT   significantly expressed in medulloblastomas.";
RL   J. Neurooncol. 73:101-108(2005).
RN   [8]
RP   FUNCTION, INTERACTION WITH ATXN1, TISSUE SPECIFICITY, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17190598; DOI=10.1016/j.cell.2006.11.038;
RA   Lam Y.C., Bowman A.B., Jafar-Nejad P., Lim J., Richman R., Fryer J.D.,
RA   Hyun E.D., Duvick L.A., Orr H.T., Botas J., Zoghbi H.Y.;
RT   "ATAXIN-1 interacts with the repressor Capicua in its native complex
RT   to cause SCA1 neuropathology.";
RL   Cell 127:1335-1347(2006).
RN   [9]
RP   INTERACTION WITH ATXN1L.
RX   PubMed=17322884; DOI=10.1038/ng1977;
RA   Bowman A.B., Lam Y.C., Jafar-Nejad P., Chen H.-K., Richman R.,
RA   Samaco R.C., Fryer J.D., Kahle J.J., Orr H.T., Zoghbi H.Y.;
RT   "Duplication of Atxn1l suppresses SCA1 neuropathology by decreasing
RT   incorporation of polyglutamine-expanded ataxin-1 into native
RT   complexes.";
RL   Nat. Genet. 39:373-379(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2192; SER-2195; SER-2299
RP   AND SER-2304, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Transcriptional repressor which may play a role in
CC       development of the central nervous system (CNS).
CC   -!- SUBUNIT: Isoforms 1 and 2 interact with ATXN1. Interacts with
CC       ATXN1L.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=L;
CC         IsoId=Q924A2-4; Sequence=Displayed;
CC       Name=2; Synonyms=S;
CC         IsoId=Q924A2-2; Sequence=VSP_026140, VSP_026141, VSP_039804;
CC   -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are present in
CC       cerebellum (at protein level).
CC   -!- DEVELOPMENTAL STAGE: Expressed postnatally in the hippocampus,
CC       neocortex, olfactory bulb and cerebellum. Expressed in the
CC       hippocampus from P0 to P15. Expressed in the posterior region of
CC       the neocortex at P4, the anterior region at P9, and is then lost
CC       by P15. Expressed in the cerebellum from P0, specifically within
CC       the external granule layer (EGL) which contains granule cell
CC       precursors. By P7 expression is distributed throughout the EGL and
CC       is reduced in the inner granule cell layer (IGL) where granule
CC       cells finally differentiate. Expression in the IGL continues to
CC       diminish up to P15, when granule cell neurogenesis is complete.
CC   -!- SIMILARITY: Contains 1 HMG box DNA-binding domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC41408.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF363690; AAK73516.1; -; mRNA.
DR   EMBL; AK004685; BAB23472.1; -; mRNA.
DR   EMBL; AK147276; BAE27813.1; -; mRNA.
DR   EMBL; AK147535; BAE27978.1; -; mRNA.
DR   EMBL; AC156992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC040463; AAH40463.1; -; mRNA.
DR   EMBL; BC058665; AAH58665.1; -; mRNA.
DR   EMBL; AB093224; BAC41408.1; ALT_SEQ; mRNA.
DR   IPI; IPI00653910; -.
DR   IPI; IPI00761255; -.
DR   RefSeq; NP_001103601.1; NM_001110131.1.
DR   RefSeq; NP_001103602.1; NM_001110132.1.
DR   RefSeq; NP_082158.2; NM_027882.3.
DR   UniGene; Mm.28833; -.
DR   ProteinModelPortal; Q924A2; -.
DR   SMR; Q924A2; 1104-1177.
DR   STRING; Q924A2; -.
DR   PhosphoSite; Q924A2; -.
DR   PRIDE; Q924A2; -.
DR   Ensembl; ENSMUST00000005578; ENSMUSP00000005578; ENSMUSG00000005442.
DR   Ensembl; ENSMUST00000094696; ENSMUSP00000092284; ENSMUSG00000005442.
DR   GeneID; 71722; -.
DR   KEGG; mmu:71722; -.
DR   UCSC; uc009fsb.1; mouse.
DR   UCSC; uc009fsc.1; mouse.
DR   CTD; 71722; -.
DR   MGI; MGI:1918972; Cic.
DR   eggNOG; roNOG05806; -.
DR   GeneTree; ENSGT00530000063757; -.
DR   HOVERGEN; HBG081174; -.
DR   InParanoid; Q924A2; -.
DR   OMA; HREPEEA; -.
DR   OrthoDB; EOG4K0QQN; -.
DR   NextBio; 334331; -.
DR   ArrayExpress; Q924A2; -.
DR   Bgee; Q924A2; -.
DR   CleanEx; MM_CIC; -.
DR   Genevestigator; Q924A2; -.
DR   GermOnline; ENSMUSG00000005442; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR000910; HMG_HMG1/HMG2.
DR   InterPro; IPR009071; HMG_superfamily.
DR   Gene3D; G3DSA:1.10.30.10; HMG-box; 1.
DR   Pfam; PF00505; HMG_box; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; HMG-box; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Nucleus; Phosphoprotein; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN         1   2510       Protein capicua homolog.
FT                                /FTId=PRO_0000048599.
FT   DNA_BIND   1107   1175       HMG box.
FT   REGION      935    953       Interaction with ATXN1.
FT   COMPBIAS     36     77       Glu-rich.
FT   COMPBIAS    339    441       Pro-rich.
FT   COMPBIAS    612   1045       Pro-rich.
FT   COMPBIAS   1415   2202       Pro-rich.
FT   COMPBIAS   2426   2503       Pro-rich.
FT   MOD_RES    1049   1049       Phosphoserine (By similarity).
FT   MOD_RES    1053   1053       Phosphoserine (By similarity).
FT   MOD_RES    1080   1080       Phosphoserine (By similarity).
FT   MOD_RES    1186   1186       Phosphoserine (By similarity).
FT   MOD_RES    1403   1403       Phosphoserine (By similarity).
FT   MOD_RES    1625   1625       Phosphoserine (By similarity).
FT   MOD_RES    1809   1809       Phosphoserine.
FT   MOD_RES    2192   2192       Phosphothreonine.
FT   MOD_RES    2195   2195       Phosphoserine.
FT   MOD_RES    2275   2275       Phosphoserine (By similarity).
FT   MOD_RES    2280   2280       Phosphoserine (By similarity).
FT   MOD_RES    2284   2284       Phosphoserine (By similarity).
FT   MOD_RES    2299   2299       Phosphoserine.
FT   MOD_RES    2304   2304       Phosphoserine.
FT   MOD_RES    2311   2311       Phosphoserine (By similarity).
FT   MOD_RES    2364   2364       Phosphoserine (By similarity).
FT   VAR_SEQ       1    907       Missing (in isoform 2).
FT                                /FTId=VSP_026140.
FT   VAR_SEQ     908    929       VPSSYPSHPAPKKEVIMGRPGT -> MYSAHRPLIPASGAA
FT                                SRGLGMF (in isoform 2).
FT                                /FTId=VSP_026141.
FT   VAR_SEQ    2250   2250       K -> NR (in isoform 2).
FT                                /FTId=VSP_039804.
FT   CONFLICT   1089   1089       D -> E (in Ref. 2; BAE27978).
FT   CONFLICT   1963   1963       S -> SA (in Ref. 1; AAK73516).
FT   CONFLICT   2059   2059       T -> TA (in Ref. 1; AAK73516).
FT   CONFLICT   2115   2115       A -> P (in Ref. 2; BAB23472).
FT   CONFLICT   2156   2156       E -> G (in Ref. 2; BAE27978).
FT   CONFLICT   2212   2212       G -> V (in Ref. 2; BAE27813).
FT   CONFLICT   2364   2364       S -> L (in Ref. 2; BAB23472).
FT   CONFLICT   2401   2401       D -> N (in Ref. 2; BAB23472).
SQ   SEQUENCE   2510 AA;  258130 MW;  092C6CA3CC71B6D9 CRC64;
     MKPMKKACPG LAGSASGSKS PPATRAKALR RRGAGEGDKP EEEEEAQPQE QAGPEEAEEG
     EEEEAERDPG AEGTHPELQP NDPTPGLTED PKGDGEAGRW EPSLSRKTAT FKSRAPKKKY
     VEEHGTGNVG VVGAPEERER TPEDASALGV PPRPPTSTRS SSTDTASEHS ADLEDEPPEA
     CGPGPWPSTG TSEGYDLRQL RSQRVLARRG DGLFLPAVVR QVRRSQDLGV QFPGDRALTF
     YEGVPGGGVD VVLDVTPPPG ALMVGTAVCT CVEPGVAAYR EGVVVEVATK PAAYKVRLSP
     GPSSHAGPPG TLPQAQQTLH REPEEAVWVT RSSLRLLRPP WEPGALLRKH PAGPEEEQAE
     PGPALPPCPS SVEPKQPEDA EVSNISFGSN LGTRCEEGEE KHPPSLGTPV LLPLPPPQLL
     SPPPKSPAFG GPGRPSEQPS PCQEGSQGGS RSSSVASLEK GAAPAARART PLTAAQQKYK
     KGDVVCTPNG IRKKFNGKQW RRLCSRDGCM KESQRRGYCS RHLSMRTKEM EGLADSGPGG
     TGRPAGVAAR EGSTEFDWGD ETSRDSEASS VAARGDSRPR LVAPADLSRF EFDECEAAVM
     LVSLGSSRSG TPSFSPVSTQ SPFSPAPSPS PSPLFGFRPA NFSPINASPV IQRTAVRSRH
     LSASTPKAGV LTPPDLGPHP PPPAPRERHS SGILPTFQTN LTFTVPISPG RRKTELLPHP
     GTLGASGAGG GGAAPDFPKS DSLDSGVDSV SHTPTPSTPA GFRAVSPAVP FSRSRQPSPL
     LLLPPPAGLT SDPGPSVRRV PAVQRDSPVI VRNPDVPLPS KFPGEVGTAG EARAGGPGRS
     CRETPVPPGV ASGKPGLPPP LPAPVPITVP PAAPTAVAQP MPTLGLASSP FQPVAFHPSP
     AALLPVLVPS SYPSHPAPKK EVIMGRPGTV WTNVEPRSVA VFPWHSLVPF LAPSQPDPSV
     QPSEAQQPAS HPVASNQSKE PAESAAVAHE QPPGGTGGAD PGRPPGAVCP ESPGPGPPLT
     LGGVDPGKSL PPTTEEEAPG PPGEPRLDSE TESDHDDAFL SIMSPEIQLP LPPGKRRTQS
     LSALPKERDS SSEKDGRSPN KREKDHIRRP MNAFMIFSKR HRALVHQRHP NQDNRTVSKI
     LGEWWYALGP KEKQKYHDLA FQVKEAHFKA HPDWKWCNKD RKKSSSEAKP ASLGLAGGHK
     ETRERSMSET GTAAAPGVSS ELLSVAAQTL LSSDTKVPGS GPCGAERLHA VGAPGSARPR
     AFSHSGVHSL DGGEVDSQAL QELTQMVSGP ASYSGPKPSP QYGAPGSFAA PGEGGTLATS
     GRPPLLPSRA SRSQRAASED MTSDEERMVI CEEEGDDDVI ADDSFGTTDI DLKCKERVTD
     SESGDSSGED PEGNKGFGRK VFSPVIRSSF THCRPTLDPE PPGPPDPPAA FSKGYGPTPS
     SSSSPASTSV SVSTSFSLGS GTFKTQESGQ GSTAVPLRPP PPGAGGPATP SKATRFPPTD
     SATFRRKRPE SVGSLEAPGP SVIAAPPSGG GNLLQTLVLP PSKEDREGTR VPSAPAPPLA
     YGAPAAPLCR PAATMVTNVV RPVSSTPVPI ASKPFPTSGR AEASSNDIAG ARTEMGTGSR
     VPGGSPMGVS LVYSDKKSAA AATSPAPHLV AGPLLGTVGK APATVTNLLV GTPGYGAPAS
     PAVQFIAQGA PGSATPAGSG ASTGSGPNGP VPLGILQPGA LGKAGGITQV QYILPTLPQQ
     LQVAPAPAPA PGTKAAAPSG PAPTTSIRFT LPPGTSTNGK VLAATAPTAG IPILQSVPSA
     PPPKAQSVSP VQATPSGGSA QLLPGKVLVP LAAPSMSVRG GGAGQPLPLV SSPFSVPVQN
     GAQQPSKIIQ LTPVPVSTPS GLVPPLSPAT MPGPTSQPQK VLLPSSTRIT YVQSAGGHTL
     PLGTSSACSQ TGTVTSYGPT SSVALGFTSL GPSGPAFVQP LLSGQAPLLA PGQVGVSPVP
     SPQLPPACTA SGGPVITAFY PGSPAPTSAP LGPPSQAPPS LVYTVATSTT PPAATILPKG
     PPASATATPA PTSPFPSATG SMTYSLVAPK AQRPSPKAPQ KVKAAIASIP VGSFESGTTG
     RPGSTPRQSS DSGVAREPAA PESELEGQPT PPAPPPPTET WPPTARSSPP PPLPAEERPG
     TKGPETASKF PSSSSDWRVP GLGLESRGEP PTPPSPAPAT GPSGSSSGSS EGSSGRAAGD
     TPERKEVTSS GKKMKVRPPP LKKTFDSVDK VLSEVDFEER FAELPEFRPE EVLPSPTLQS
     LATSPRAILG SYRKKRKNST DLDSAPEDPT SPKRKMRRRS SCSSEPNTPK SAKCEGDIFT
     FDRTGTETED VLGELEYEKV PYSSLRRTLD QRRALVMQLF QDHGFFPSAQ ATAAFQARYA
     DIFPSKVCLQ LKIREVRQKI MQAATPTEQP PGAEAPLPGP PPTGMAATPV PTPSPAGGPD
     PTSPGSDSGT AQVAPPLPPP PEPGPGQPGW EGAPQPSPPP SGPSTAATGR
//
ID   MED15_MOUSE             Reviewed;         792 AA.
AC   Q924H2;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2002, sequence version 2.
DT   08-FEB-2011, entry version 58.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 15;
DE   AltName: Full=Mediator complex subunit 15;
DE   AltName: Full=Positive cofactor 2 glutamine/Q-rich-associated protein;
DE            Short=PC2 glutamine/Q-rich-associated protein;
DE            Short=mPcqap;
GN   Name=Med15; Synonyms=Pcqap;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=21309066; PubMed=11414760; DOI=10.1006/geno.2001.6566;
RA   Berti L., Mittler G., Przemeck G.K.H., Stelzer G., Guenzler B.,
RA   Amati F., Conti E., Dallapiccola B., Hrabe' de Angelis M., Novelli G.,
RA   Meisterernst M.;
RT   "Isolation and characterization of a novel gene from the DiGeorge
RT   chromosomal region that encodes for a mediator subunit.";
RL   Genomics 74:320-332(2001).
CC   -!- FUNCTION: Component of the Mediator complex, a coactivator
CC       involved in the regulated transcription of nearly all RNA
CC       polymerase II-dependent genes. Mediator functions as a bridge to
CC       convey information from gene-specific regulatory proteins to the
CC       basal RNA polymerase II transcription machinery. Mediator is
CC       recruited to promoters by direct interactions with regulatory
CC       proteins and serves as a scaffold for the assembly of a functional
CC       preinitiation complex with RNA polymerase II and the general
CC       transcription factors. Required for cholesterol-dependent gene
CC       regulation. Positively regulates the Nodal signaling pathway (By
CC       similarity).
CC   -!- SUBUNIT: Component of the Mediator complex, which is composed of
CC       MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13,
CC       MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21,
CC       MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31,
CC       CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8
CC       subunits form a distinct module termed the CDK8 module. Mediator
CC       containing the CDK8 module is less active than Mediator lacking
CC       this module in supporting transcriptional activation. Individual
CC       preparations of the Mediator complex lacking one or more distinct
CC       subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and
CC       TRAP. Interacts with SMAD2, SMAD3, SREBF1 and SREBF2. Interacts
CC       with WWTR1 (By similarity). Interacts with TRIM11 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- DEVELOPMENTAL STAGE: At E9.5 ubiquitously expressed at low levels
CC       with slightly elevated levels in the pharyngeal arches and in the
CC       forelimb buds. At E10.5 expression was more pronounced in the
CC       first and second pharyngeal arches, the nasal processes and the
CC       limb buds. At E11.5 expression is high in frontonasal region,
CC       maxillary and mandibular processes of the first and second
CC       pharyngeal arch and developing fore and hindlimbs. From E11.5-
CC       E12.5 expression is seen in the distal parts of the developing
CC       limbs and in the facial region. At E12.5 transcripts were found in
CC       the developing hair follicles of the vibrissae.
CC   -!- PTM: Ubiquitinated by TRIM11, leading to proteasomal degradation
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 15 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK58424.1; Type=Frameshift; Positions=665;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF328770; AAK58424.1; ALT_FRAME; mRNA.
DR   IPI; IPI00125670; -.
DR   UniGene; Mm.208970; -.
DR   ProteinModelPortal; Q924H2; -.
DR   SMR; Q924H2; 5-78.
DR   STRING; Q924H2; -.
DR   PhosphoSite; Q924H2; -.
DR   PRIDE; Q924H2; -.
DR   Ensembl; ENSMUST00000012259; ENSMUSP00000012259; ENSMUSG00000012114.
DR   UCSC; uc007yls.1; mouse.
DR   MGI; MGI:2137379; Med15.
DR   GeneTree; ENSGT00600000084417; -.
DR   HOGENOM; HBG125478; -.
DR   HOVERGEN; HBG053529; -.
DR   InParanoid; Q924H2; -.
DR   ArrayExpress; Q924H2; -.
DR   Bgee; Q924H2; -.
DR   CleanEx; MM_MED15; -.
DR   Genevestigator; Q924H2; -.
DR   GermOnline; ENSMUSG00000012114; Mus musculus.
DR   GO; GO:0016592; C:mediator complex; IEA:InterPro.
DR   GO; GO:0016455; F:RNA polymerase II transcription mediator activity; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEA:InterPro.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR019087; Mediator_Med15_met.
DR   Pfam; PF09606; ARC105_Med_act; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Activator; Cytoplasm; Nucleus; Phosphoprotein;
KW   Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN         1    792       Mediator of RNA polymerase II
FT                                transcription subunit 15.
FT                                /FTId=PRO_0000058265.
FT   REGION        9     73       Interaction with SREBF1 (By similarity).
FT   MOTIF       548    565       Nuclear localization signal (Potential).
FT   COMPBIAS    161    176       Poly-Gln.
FT   COMPBIAS    180    199       Poly-Gln.
FT   COMPBIAS    211    222       Poly-Gln.
FT   COMPBIAS    230    242       Poly-Gln.
FT   COMPBIAS    246    259       Poly-Gln.
FT   COMPBIAS    453    460       Poly-Pro.
FT   COMPBIAS    603    609       Poly-Pro.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     604    604       Phosphothreonine (By similarity).
SQ   SEQUENCE   792 AA;  87061 MW;  71C879DCD3925E62 CRC64;
     MDVWGQETDW RSAAFRLKLV SQIEDAMRKA GVAHSKSSKD MESHVFLKAK TRDEYLSLVA
     RLIIHFRDIH NKKSQASVSD PMNALQSLTG GPTPGAAGIG MPPRGPGQSL GGMGGLGAMG
     QPLPLSGQPP PGTSGMAPHG MAVVSTTTPQ TQLQLQQVAL QQQQQRQQQQ QFQQQQAALQ
     QQQQQQQQQQ QQQQFQAQQN AMQQQFQAVV QQQQLQQQQQ QQHLIKLHHQ SQQQQIQQQQ
     LQRMAQLQLQ QQQQQQQQQA LQAQPPMQQP SMQQPQPPPS QALPQQLSQL HHPQHHQPPP
     QAQQSPIAQN QPPQIPPQSQ SQPLVSRAQA LPGPMLYAAQ QQLKFVRAPM VVQQPQVQPQ
     VQQVQPQVQP QAAVQAAQSA QMVAPGVQMI AEALAQGGMH VRARFPPTST MSAGPSSSIS
     LGGQPTTQVS QSSLTMLSSP SPGQQVQTPQ SMPPPPQPSP QPGSQPNSNV SSGPAPSPSS
     FLPSPSPQPS QSPVTARTPQ NFSVPSPGPL NTPVNPSSVM SPAGSSQAEE QQYLDKLKQL
     SKYIEPLRRM INKIDKNEDR KKDLSKMKSL LDILTDPSKR CPLKTLQKCE IALEKLKNDM
     AVPTPPPPPV LPTKQQDLCQ PLLDAVLANI RSPVFNHSLY RTFVPAMMAI HGPPIVSPVV
     CSRKSPVRRF EEDERQSIPN VLQGEVARLD PKFLVNLDPS HCSNNGTVHL ICKLDDKDLP
     SVPPLELSVP ADYPAQSPMW IDRQWQYDAN PFLQSVHRCM TSRLLQLPDK HSVTALLNTW
     AQSIHQACLS AA
//
ID   MTA3_MOUSE              Reviewed;         591 AA.
AC   Q924K8; Q8VC18;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Metastasis-associated protein MTA3;
GN   Name=Mta3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RC   STRAIN=129/Sv;
RX   MEDLINE=21376123; PubMed=11483358; DOI=10.1016/S0378-1119(01)00563-7;
RA   Simpson A., Uitto J., Rodeck U., Mahoney M.G.;
RT   "Differential expression and subcellular distribution of the mouse
RT   metastasis-associated proteins Mta1 and Mta3.";
RL   Gene 273:29-39(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   STRUCTURE BY NMR OF 267-323.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the myb-like DNA-binding domain of mouse MTA3
RT   protein.";
RL   Submitted (NOV-2005) to the PDB data bank.
CC   -!- FUNCTION: Plays a role in maintenance of the normal epithelial
CC       architecture through the repression of SNAI1 transcription in a
CC       histone deacetylase-dependent manner, and thus the regulation of
CC       E-cadherin levels (By similarity).
CC   -!- SUBUNIT: Component of the nucleosome-remodeling and histone-
CC       deacetylase multiprotein complex (NuRD) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q924K8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q924K8-2; Sequence=VSP_001605, VSP_001606;
CC   -!- TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung, liver
CC       and kidney.
CC   -!- SIMILARITY: Contains 1 BAH domain.
CC   -!- SIMILARITY: Contains 1 ELM2 domain.
CC   -!- SIMILARITY: Contains 1 GATA-type zinc finger.
CC   -!- SIMILARITY: Contains 1 SANT domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF288138; AAK83045.1; -; mRNA.
DR   EMBL; BC022124; AAH22124.1; -; mRNA.
DR   IPI; IPI00125745; -.
DR   IPI; IPI00221805; -.
DR   RefSeq; NP_001164525.1; NM_001171054.1.
DR   RefSeq; NP_473423.1; NM_054082.2.
DR   UniGene; Mm.277668; -.
DR   PDB; 2CRG; NMR; -; A=267-323.
DR   PDBsum; 2CRG; -.
DR   ProteinModelPortal; Q924K8; -.
DR   SMR; Q924K8; 5-145, 267-323.
DR   PhosphoSite; Q924K8; -.
DR   PRIDE; Q924K8; -.
DR   Ensembl; ENSMUST00000067826; ENSMUSP00000068931; ENSMUSG00000055817.
DR   GeneID; 116871; -.
DR   KEGG; mmu:116871; -.
DR   UCSC; uc008dsi.1; mouse.
DR   CTD; 116871; -.
DR   MGI; MGI:2151172; Mta3.
DR   GeneTree; ENSGT00580000081398; -.
DR   HOGENOM; HBG403019; -.
DR   HOVERGEN; HBG002598; -.
DR   InParanoid; Q924K8; -.
DR   OMA; PINYAAI; -.
DR   OrthoDB; EOG4QZ7KJ; -.
DR   PhylomeDB; Q924K8; -.
DR   NextBio; 369242; -.
DR   ArrayExpress; Q924K8; -.
DR   Bgee; Q924K8; -.
DR   CleanEx; MM_MTA3; -.
DR   Genevestigator; Q924K8; -.
DR   GermOnline; ENSMUSG00000055817; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR001025; BAH_dom.
DR   InterPro; IPR000949; ELM2_dom.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR001005; SANT_DNA-bd.
DR   InterPro; IPR017884; SANT_eukarya.
DR   InterPro; IPR000679; Znf_GATA.
DR   Pfam; PF01426; BAH; 1.
DR   Pfam; PF01448; ELM2; 1.
DR   Pfam; PF00320; GATA; 1.
DR   SMART; SM00439; BAH; 1.
DR   SMART; SM00717; SANT; 1.
DR   SMART; SM00401; ZnF_GATA; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
DR   PROSITE; PS51038; BAH; 1.
DR   PROSITE; PS51156; ELM2; 1.
DR   PROSITE; PS00344; GATA_ZN_FINGER_1; FALSE_NEG.
DR   PROSITE; PS50114; GATA_ZN_FINGER_2; FALSE_NEG.
DR   PROSITE; PS51293; SANT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; DNA-binding;
KW   Metal-binding; Nucleus; Zinc; Zinc-finger.
FT   CHAIN         1    591       Metastasis-associated protein MTA3.
FT                                /FTId=PRO_0000083499.
FT   DOMAIN        1    147       BAH.
FT   DOMAIN      148    258       ELM2.
FT   DOMAIN      265    317       SANT.
FT   ZN_FING     377    404       GATA-type; atypical.
FT   VAR_SEQ     506    512       YADRHAE -> CKTLFNS (in isoform 2).
FT                                /FTId=VSP_001605.
FT   VAR_SEQ     513    591       Missing (in isoform 2).
FT                                /FTId=VSP_001606.
FT   CONFLICT    166    166       E -> EG (in Ref. 2; AAH22124).
FT   HELIX       272    284
FT   HELIX       289    294
FT   STRAND      298    300
FT   HELIX       302    313
SQ   SEQUENCE   591 AA;  67077 MW;  ABA5CB9E86FCE7E2 CRC64;
     MAANMYRVGD YVYFENSSSN PYLIRRIEEL NKTASGNVEA KVVCFYRRRD ISNTLIMLAD
     KHAKETEEES ETPVEADLTE KQKHQLKHRE LFLSRQYESL PATHIRGKCS VALLNETESV
     LSYLDKEDTF FYSLVYDPSV KTLLADKGEI RVGPKYQADI PDMLPEDSDE REQSKLEVKV
     WDPNSPLTDR QIDQFLVVAR AVGTFARALD CSSSVRQPSL HMSAAAASRD ITLFHAMDTL
     YRHGYDLSSA ISVLVPLGGP VLCRDEMEEW SASEACLFEE ALEKYGKDFN DIRQDFLPWK
     SLTSIIEYYY MWKTTDRYVQ QKRLKAAEAE SKLKQVYIPT YKPNPNQISS SNGKAGTVNG
     AVGTQFQPQS ALLGRACESC YATQSHQWYS WGPPNMQCRL CATCWLYWKK YGGLKMPTQS
     DEEKSPSPTA EDPRARSHMS RQALQGMPVR NTGSPKSAVK TRQAFFLRTT YFTKIARQVC
     KSTLRLRQAA RRPFVAINYA AIRAEYADRH AELSGSPLKS RSTRKPLSCI IGYLEIHPAK
     KPNVIRSPPS LQTPATKRML AAPNHTSLSI LGKRNYSHHN GLDGPERWLS R
//
ID   S12A6_MOUSE             Reviewed;        1150 AA.
AC   Q924N4; Q924N3;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Solute carrier family 12 member 6;
DE   AltName: Full=Electroneutral potassium-chloride cotransporter 3;
DE   AltName: Full=K-Cl cotransporter 3;
GN   Name=Slc12a6; Synonyms=Kcc3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND GLYCOSYLATION.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=21143254; PubMed=11246162; DOI=10.1016/S0306-4522(00)00567-4;
RA   Pearson M.M., Lu J., Mount D.B., Delpire E.;
RT   "Localization of the K(+)-Cl(-) cotransporter, KCC3, in the central
RT   and peripheral nervous systems: expression in the choroid plexus,
RT   large neurons and white matter tracts.";
RL   Neuroscience 103:481-491(2001).
RN   [2]
RP   PROTEIN SEQUENCE OF 601-608; 1054-1061 AND 1103-1113, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [3]
RP   FUNCTION.
RX   MEDLINE=99278405; PubMed=10347194; DOI=10.1074/jbc.274.23.16355;
RA   Mount D.B., Mercado A., Song L., Xu J., George A.L. Jr., Delpire E.,
RA   Gamba G.;
RT   "Cloning and characterization of KCC3 and KCC4, new members of the
RT   cation-chloride cotransporter gene family.";
RL   J. Biol. Chem. 274:16355-16362(1999).
RN   [4]
RP   DISEASE.
RX   MEDLINE=22297722; PubMed=12368912; DOI=10.1038/ng1002;
RA   Howard H.C., Mount D.B., Rochefort D., Byun N., Dupre N., Lu J.,
RA   Fan X., Song L., Riviere J.-B., Prevost C., Horst J., Simonati A.,
RA   Lemcke B., Welch R., England R., Zhan F.Q., Mercado A., Siesser W.B.,
RA   George A.L. Jr., McDonald M.P., Bouchard J.-P., Mathieu J.,
RA   Delpire E., Rouleau G.A.;
RT   "The K-Cl cotransporter KCC3 is mutant in a severe peripheral
RT   neuropathy associated with agenesis of the corpus callosum.";
RL   Nat. Genet. 32:384-392(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1032, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1007 AND SER-1032, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Mediates electroneutral potassium-chloride cotransport.
CC       May be activated by cell swelling. May contribute to cell volume
CC       homeostasis in single cells.
CC   -!- SUBUNIT: Homomultimer and heteromultimer with other K-Cl
CC       cotransporters (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q924N4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q924N4-2; Sequence=VSP_006117, VSP_006118;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is highly expressed throughout the
CC       brain and detected at lower levels in kidney. Highly expressed in
CC       highly myelinated white matter of the brain, but not in gray
CC       matter. Detected in the corpus callosum, in packed cell layers of
CC       the hippocampus and in Purkinje neurons within the cerebellum.
CC       Highly expressed in white matter in the spinal cord, but not in
CC       dorsal root ganglia or sciatic nerve. Colocalizes with the
CC       oligodendrocyte marker CNP. Isoform 2 is highly expressed in
CC       kidney, but not detected in brain.
CC   -!- PTM: N-glycosylated.
CC   -!- DISEASE: Note=Defects in Slc12a6 are a cause of locomotor
CC       abnormalities beginning at 2 weeks of age. Slc12a6 deficient mice
CC       show hypomyelination, decompaction of myelin, demyelination,
CC       axonal swelling and fiber degeneration.
CC   -!- SIMILARITY: Belongs to the SLC12A transporter family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF211854; AAK81895.1; -; mRNA.
DR   EMBL; AF211855; AAK81896.1; -; mRNA.
DR   IPI; IPI00125829; -.
DR   IPI; IPI00857354; -.
DR   UniGene; Mm.479575; -.
DR   ProteinModelPortal; Q924N4; -.
DR   IntAct; Q924N4; 16.
DR   STRING; Q924N4; -.
DR   PhosphoSite; Q924N4; -.
DR   PRIDE; Q924N4; -.
DR   Ensembl; ENSMUST00000028549; ENSMUSP00000028549; ENSMUSG00000027130.
DR   Ensembl; ENSMUST00000053666; ENSMUSP00000051490; ENSMUSG00000027130.
DR   UCSC; uc008lou.2; mouse.
DR   UCSC; uc008low.2; mouse.
DR   MGI; MGI:2135960; Slc12a6.
DR   GeneTree; ENSGT00560000076892; -.
DR   HOGENOM; HBG590211; -.
DR   HOVERGEN; HBG052852; -.
DR   InParanoid; Q924N4; -.
DR   OrthoDB; EOG476JZG; -.
DR   PhylomeDB; Q924N4; -.
DR   ArrayExpress; Q924N4; -.
DR   Bgee; Q924N4; -.
DR   CleanEx; MM_SLC12A6; -.
DR   Genevestigator; Q924N4; -.
DR   GermOnline; ENSMUSG00000027130; Mus musculus.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR   InterPro; IPR004841; AA-permease_dom.
DR   InterPro; IPR018491; K/Cl_cotranspt_1/3.
DR   InterPro; IPR000076; KCL_cotranspt.
DR   InterPro; IPR004842; Na/K/Cl_cotransptS.
DR   Pfam; PF00324; AA_permease; 2.
DR   Pfam; PF03522; KCl_Cotrans_1; 1.
DR   PRINTS; PR01081; KCLTRNSPORT.
DR   TIGRFAMs; TIGR00930; 2a30; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing; Glycoprotein;
KW   Ion transport; Membrane; Phosphoprotein; Potassium;
KW   Potassium transport; Symport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1   1150       Solute carrier family 12 member 6.
FT                                /FTId=PRO_0000178038.
FT   TOPO_DOM      1    185       Cytoplasmic (Potential).
FT   TRANSMEM    186    206       Helical; (Potential).
FT   TRANSMEM    208    228       Helical; (Potential).
FT   TOPO_DOM    229    235       Cytoplasmic (Potential).
FT   TRANSMEM    236    256       Helical; (Potential).
FT   TRANSMEM    277    297       Helical; (Potential).
FT   TOPO_DOM    298    319       Cytoplasmic (Potential).
FT   TRANSMEM    320    340       Helical; (Potential).
FT   TRANSMEM    343    363       Helical; (Potential).
FT   TOPO_DOM    364    480       Cytoplasmic (Potential).
FT   TRANSMEM    481    501       Helical; (Potential).
FT   TRANSMEM    518    538       Helical; (Potential).
FT   TOPO_DOM    539    558       Cytoplasmic (Potential).
FT   TRANSMEM    559    579       Helical; (Potential).
FT   TRANSMEM    632    652       Helical; (Potential).
FT   TOPO_DOM    653    689       Cytoplasmic (Potential).
FT   TRANSMEM    690    710       Helical; (Potential).
FT   TRANSMEM    789    809       Helical; (Potential).
FT   TOPO_DOM    810   1150       Cytoplasmic (Potential).
FT   COMPBIAS    227    230       Poly-Cys.
FT   MOD_RES      32     32       Phosphoserine (By similarity).
FT   MOD_RES    1007   1007       Phosphoserine.
FT   MOD_RES    1029   1029       Phosphoserine (By similarity).
FT   MOD_RES    1032   1032       Phosphoserine.
FT   CARBOHYD    504    504       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1     51       Missing (in isoform 2).
FT                                /FTId=VSP_006117.
FT   VAR_SEQ      52     90       PETSRSEPMSELSGATTSLATVALDPSSDRTSNPQDVTE
FT                                -> MPHFTVTKVEDPEEGAAGPLSPEPSSAEVKARIQDPQE
FT                                P (in isoform 2).
FT                                /FTId=VSP_006118.
SQ   SEQUENCE   1150 AA;  127497 MW;  CC9EA4816C0F5F0E CRC64;
     MHPPEATTKM SSVRFMVTPT KIDDIPGLSD TSPDLSSRSS SRVRFSSRES VPETSRSEPM
     SELSGATTSL ATVALDPSSD RTSNPQDVTE DPSQNSITGE HSQLLDDGHK KARNAYLNNS
     NYEEGDEYFD KNLALFEEEM DTRPKVSSLL NRMANYTNLT QGAKEHEEAE NITEGKKKPT
     KSPQMGTFMG VYLPCLQNIF GVILFLRLTW VVGTAGILQA FAIVLICCCC TMLTAISMSA
     IATNGVVPAG GSYFMISRAL GPEFGGAVGL CFYLGTTFAA AMYILGAIEI FLVYIVPRAA
     IFRSDDALKE SAAMLNNMRV YGTAFLVLMV LVVFIGVRYV NKFASLFLAC VIVSILAIYA
     GAIKSSFAPP HFPVCMLGNR TLSSRHLDIC SKTKEVDNMT VPSKLWGFFC NSSQFFNATC
     DEYFVHNNVI SIQGIPGLAS GIITENLWSN YLPKGEIIEK PSAKSSDVLG NLNHEYVLAD
     ITTSFTLLVG IFFPSVTGIM AGSNRSGDLK DAQKSIPIGT ILAILTTSFV YLSNVVLFGA
     CIEGVVLRDK FGDAVKGNLV VGTLSWPSPW VIVIGSFFST CGAGLQSLTG APRLLQAIAK
     DNIIPFLRVF GHSKANGEPT WALLLTAAIA ELGILIASLD LVAPILSMFF LMCYLFVNLA
     CALQTLLRTP NWRPRFRYYH WALSFMGMSI CLALMFISSW YYAIVAMVIA GMIYKYIEYQ
     GAEKEWGDGI RGLSLSAARF ALLRLEEGPP HTKNWRPQLL VLLKLDEDLH VKHPRLLTFA
     SQLKAGKGLT IVGSVIVGNF LENYGDALAA EQTIKHLMEA EKVKGFCQLV VAAKLKEGIS
     HLIQSCGLGG MKHNTVVMGW PNGWRQSEDA RAWKTFIGTV RVTTAAHLAL LVAKNVSFFP
     SNVEQFSEGN IDVRWIVHDG GMLMLLPFLL KQHKVWRKCS IRIFTVAQLE DNSIQMKKDL
     ATFLYHLRIE AEVEVVEMHD SDISAYTYER TLMMEQRSQM LRHMRLSKTE RDREAQLVKD
     RNSMLRLTSI GSDEDEETET YQEKVHMTWT KDKYMASRGQ KVKSMEGFQD LLNMRPDQSN
     VRRMHTAVKL NEVIVNKSHE AKLVLLNMPG PPRNPEGDEN YMEFLEVLTE GLERVLLVRG
     GGSEVITIYS
//
ID   SPRE2_MOUSE             Reviewed;         410 AA.
AC   Q924S7;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Sprouty-related, EVH1 domain-containing protein 2;
DE            Short=Spred-2;
GN   Name=Spred2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH
RP   RAS, TISSUE SPECIFICITY, AND FUNCTION.
RX   MEDLINE=21385651; PubMed=11493923; DOI=10.1038/35088082;
RA   Wakioka T., Sasaki A., Kato R., Shouda T., Matsumoto A., Miyoshi K.,
RA   Tsuneoka M., Komiya S., Baron R., Yoshimura A.;
RT   "Spred is a Sprouty-related suppressor of Ras signalling.";
RL   Nature 412:647-651(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=15580519; DOI=10.1007/s00418-004-0725-6;
RA   Engelhardt C.M., Bundschu K., Messerschmitt M., Renne T., Walter U.,
RA   Reinhard M., Schuh K.;
RT   "Expression and subcellular localization of Spred proteins in mouse
RT   and human tissues.";
RL   Histochem. Cell Biol. 122:527-538(2004).
CC   -!- FUNCTION: Tyrosine kinase substrate that inhibits growth-factor-
CC       mediated activation of MAP kinase.
CC   -!- SUBUNIT: Interacts with ras.
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity). Cytoplasmic vesicle, secretory
CC       vesicle membrane; Peripheral membrane protein; Cytoplasmic side
CC       (Potential). Cytoplasm. Note=Especially found in the cytoplasm of
CC       the stratum spinosum cells called membrane-coated granules (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in lung, liver and
CC       testis. In testis, it is specially found in mature spermatids
CC       projecting into the lumen of the seminiferous. Strongly expressed
CC       in glandular epithelia. Also expressed in embryonic tissues such
CC       as heart, lung, liver and brain.
CC   -!- PTM: Phosphorylated on tyrosine. Phosphorylation of Tyr-224 and
CC       Tyr-227 are required for ubiquitination (By similarity).
CC   -!- PTM: Ubiquitinated; leading to degradation by the proteasome (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 KBD domain.
CC   -!- SIMILARITY: Contains 1 SPR (sprouty) domain.
CC   -!- SIMILARITY: Contains 1 WH1 domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AB063496; BAB62849.1; -; mRNA.
DR   EMBL; AK036430; BAC29425.1; -; mRNA.
DR   EMBL; BC066013; AAH66013.1; -; mRNA.
DR   IPI; IPI00125974; -.
DR   RefSeq; NP_277058.1; NM_033523.4.
DR   UniGene; Mm.266627; -.
DR   ProteinModelPortal; Q924S7; -.
DR   SMR; Q924S7; 1-124.
DR   STRING; Q924S7; -.
DR   PhosphoSite; Q924S7; -.
DR   PRIDE; Q924S7; -.
DR   Ensembl; ENSMUST00000093298; ENSMUSP00000090987; ENSMUSG00000045671.
DR   GeneID; 114716; -.
DR   KEGG; mmu:114716; -.
DR   UCSC; uc007icr.1; mouse.
DR   CTD; 114716; -.
DR   MGI; MGI:2150019; Spred2.
DR   GeneTree; ENSGT00390000003347; -.
DR   HOVERGEN; HBG057556; -.
DR   NextBio; 368741; -.
DR   ArrayExpress; Q924S7; -.
DR   Bgee; Q924S7; -.
DR   CleanEx; MM_SPRED2; -.
DR   Genevestigator; Q924S7; -.
DR   GermOnline; ENSMUSG00000045671; Mus musculus.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005173; F:stem cell factor receptor binding; IPI:MGI.
DR   GO; GO:0000188; P:inactivation of MAPK activity; IMP:MGI.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:InterPro.
DR   InterPro; IPR000697; EVH1.
DR   InterPro; IPR023337; KBD.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR007875; Sprouty.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF05210; Sprouty; 1.
DR   Pfam; PF00568; WH1; 1.
DR   PROSITE; PS51488; KBD; 1.
DR   PROSITE; PS51227; SPR; 1.
DR   PROSITE; PS50229; WH1; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoplasmic vesicle; Membrane; Phosphoprotein;
KW   Ubl conjugation.
FT   CHAIN         1    410       Sprouty-related, EVH1 domain-containing
FT                                protein 2.
FT                                /FTId=PRO_0000076911.
FT   DOMAIN        5    122       WH1.
FT   DOMAIN      197    252       KBD.
FT   DOMAIN      300    408       SPR.
FT   MOD_RES     224    224       Phosphotyrosine (By similarity).
FT   MOD_RES     227    227       Phosphotyrosine (By similarity).
SQ   SEQUENCE   410 AA;  46794 MW;  8A652D06CE8D3BB1 CRC64;
     MTEETHPDDD SYIVRVKAVV MTRDDSSGGW FPQEGGGISR VGVCKVMHPE GNGRSGFLIH
     GERQKDKLVV LECYVRKDLV YTKANPTFHH WKVDNRKFGL TFQSPADARA FDRGVRKAIE
     DLIEGSTTSS STLHNEAELG DDDVFTTATD SSSNSSQKRE PTTRTISSPT SCEHRKIYTL
     DPYPMDHYHP DQRLPRSYPQ VTFPEDDEEI VRINPREKIW MTGYEDYRHA PVRGKYLDTT
     EDADSYVRFA KGEVPKHEYT YPYVDSSDFG FGEDPKGSVI KTQPPRAKSR RRKENGERSR
     CVYCRDMFNH EENRRGHCQD APDAVRTCIR RVSCMWCADS MLYHCMSDPE GDYTDPCSCD
     TSDEKFCLRW MALIALSFLA PCMCCYLPLR ACHRCGVMCR CCGGKHKAAA
//
ID   SPRE1_MOUSE             Reviewed;         444 AA.
AC   Q924S8; Q3U2W6; Q6PET8;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Sprouty-related, EVH1 domain-containing protein 1;
DE            Short=Spred-1;
GN   Name=Spred1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION,
RP   INTERACTION WITH RAS, PHOSPHORYLATION, TISSUE SPECIFICITY, AND
RP   FUNCTION.
RX   MEDLINE=21385651; PubMed=11493923; DOI=10.1038/35088082;
RA   Wakioka T., Sasaki A., Kato R., Shouda T., Matsumoto A., Miyoshi K.,
RA   Tsuneoka M., Komiya S., Baron R., Yoshimura A.;
RT   "Spred is a Sprouty-related suppressor of Ras signalling.";
RL   Nature 412:647-651(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=12646235; DOI=10.1016/S0006-291X(03)00259-6;
RA   Kato R., Nonami A., Taketomi T., Wakioka T., Kuroiwa A., Matsuda Y.,
RA   Yoshimura A.;
RT   "Molecular cloning of mammalian Spred-3 which suppresses tyrosine
RT   kinase-mediated Erk activation.";
RL   Biochem. Biophys. Res. Commun. 302:767-772(2003).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=15580519; DOI=10.1007/s00418-004-0725-6;
RA   Engelhardt C.M., Bundschu K., Messerschmitt M., Renne T., Walter U.,
RA   Reinhard M., Schuh K.;
RT   "Expression and subcellular localization of Spred proteins in mouse
RT   and human tissues.";
RL   Histochem. Cell Biol. 122:527-538(2004).
RN   [7]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=15465815; DOI=10.1074/jbc.M405189200;
RA   Nonami A., Kato R., Taniguchi K., Yoshiga D., Taketomi T.,
RA   Fukuyama S., Harada M., Sasaki A., Yoshimura A.;
RT   "Spred-1 negatively regulates interleukin-3-mediated ERK/mitogen-
RT   activated protein (MAP) kinase activation in hematopoietic cells.";
RL   J. Biol. Chem. 279:52543-52551(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Tyrosine kinase substrate that inhibits growth-factor-
CC       mediated activation of MAP kinase. Negatively regulates
CC       hematopoiesis of bone marrow.
CC   -!- SUBUNIT: Homodimer and heterodimer. Interacts with CAV1. Able to
CC       interact with SPRED2 to form heterodimers (By similarity).
CC       Interacts with ras.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC       Membrane, caveola; Peripheral membrane protein. Nucleus.
CC       Note=Localized in cholesterol-rich membrane raft/caveola fractions
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q924S8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q924S8-2; Sequence=VSP_012412, VSP_012413;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in brain. Weakly expressed in lung,
CC       heart, liver, kidney, intestine, spleen, testis, thymus, colon and
CC       ovary. Also expressed in embryonic tissues such as heart, lung,
CC       liver and brain. Highly expressed in interleukin-3-dependent
CC       hematopoietic cell lines (BaF3 and MC9) and bone marrow-derived
CC       mast cells (BMMC).
CC   -!- PTM: Phosphorylated on tyrosine.
CC   -!- SIMILARITY: Contains 1 KBD domain.
CC   -!- SIMILARITY: Contains 1 SPR (sprouty) domain.
CC   -!- SIMILARITY: Contains 1 WH1 domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB063495; BAB62848.1; -; mRNA.
DR   EMBL; AK155065; BAE33024.1; -; mRNA.
DR   EMBL; AL807741; CAM17918.1; -; Genomic_DNA.
DR   EMBL; AL928959; CAM17918.1; JOINED; Genomic_DNA.
DR   EMBL; AL928959; CAM26783.1; -; Genomic_DNA.
DR   EMBL; AL807741; CAM26783.1; JOINED; Genomic_DNA.
DR   EMBL; BC057874; AAH57874.1; -; mRNA.
DR   EMBL; BC079606; AAH79606.1; -; mRNA.
DR   IPI; IPI00125975; -.
DR   IPI; IPI00461756; -.
DR   RefSeq; NP_277059.1; NM_033524.2.
DR   UniGene; Mm.245890; -.
DR   UniGene; Mm.392720; -.
DR   UniGene; Mm.392726; -.
DR   UniGene; Mm.397626; -.
DR   ProteinModelPortal; Q924S8; -.
DR   SMR; Q924S8; 10-126.
DR   STRING; Q924S8; -.
DR   PhosphoSite; Q924S8; -.
DR   PRIDE; Q924S8; -.
DR   Ensembl; ENSMUST00000028829; ENSMUSP00000028829; ENSMUSG00000027351.
DR   GeneID; 114715; -.
DR   KEGG; mmu:114715; -.
DR   UCSC; uc008lrh.1; mouse.
DR   UCSC; uc008lri.1; mouse.
DR   CTD; 114715; -.
DR   MGI; MGI:2150016; Spred1.
DR   eggNOG; roNOG13143; -.
DR   GeneTree; ENSGT00390000003347; -.
DR   HOGENOM; HBG714079; -.
DR   HOVERGEN; HBG057556; -.
DR   InParanoid; Q924S8; -.
DR   OMA; GLSCVTV; -.
DR   OrthoDB; EOG40CHH0; -.
DR   PhylomeDB; Q924S8; -.
DR   NextBio; 368737; -.
DR   ArrayExpress; Q924S8; -.
DR   Bgee; Q924S8; -.
DR   Genevestigator; Q924S8; -.
DR   GermOnline; ENSMUSG00000027351; Mus musculus.
DR   GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005173; F:stem cell factor receptor binding; IPI:MGI.
DR   GO; GO:0000188; P:inactivation of MAPK activity; IMP:MGI.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:InterPro.
DR   InterPro; IPR000697; EVH1.
DR   InterPro; IPR023337; KBD.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR007875; Sprouty.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF05210; Sprouty; 1.
DR   Pfam; PF00568; WH1; 1.
DR   PROSITE; PS51488; KBD; 1.
DR   PROSITE; PS51227; SPR; 1.
DR   PROSITE; PS50229; WH1; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Membrane; Nucleus;
KW   Phosphoprotein.
FT   CHAIN         1    444       Sprouty-related, EVH1 domain-containing
FT                                protein 1.
FT                                /FTId=PRO_0000076908.
FT   DOMAIN        6    123       WH1.
FT   DOMAIN      234    286       KBD.
FT   DOMAIN      334    442       SPR.
FT   MOD_RES     239    239       Phosphoserine.
FT   VAR_SEQ     196    229       IPFSQQGLDIQSRSMEYVQRQISKECGSLKSQTR -> VRR
FT                                RILFPCIAYIEKLGVLQNTKALRSFPCYETI (in
FT                                isoform 2).
FT                                /FTId=VSP_012412.
FT   VAR_SEQ     230    444       Missing (in isoform 2).
FT                                /FTId=VSP_012413.
FT   CONFLICT    144    144       T -> I (in Ref. 2; AAH57874).
SQ   SEQUENCE   444 AA;  50664 MW;  B716DCB4AEA9F171 CRC64;
     MSEETATSDN DNSYARVRAV VMTRDDSSGG WLPLGGSGLS SVTVFRVPHQ EENGCADFFI
     RGERLRDKMV VLECMLKKDL IYNKVTPTFH HWKIDDKKFG LTFQSPADAR AFDRGIRRAI
     EDISLGCPAS KTEAEGGDDD LQTTEEDTSR SLVKDHFFQQ ETVVTSEPYR SSDIRPLPFE
     DLNARRVYLQ SQVSQIPFSQ QGLDIQSRSM EYVQRQISKE CGSLKSQTRV PLKSIRHVSF
     QDEDEIVRIN PRDILIRRYA DYRHPDMWKN DLERDDTDSS VPFSKQDSKK SDYLYHCGDE
     TKLSSLKDSV VFKTQPPSLK FKSKRRKEDG ERSRCVYCQE RFNHEENARG KCQDAPDPVK
     RCIYQVSCML CAESMLYHCM SDSEGDFSDP CSCDTSDDKF CLRWLALVAL SFIVPCMCCY
     VPLRMCHRCG EACGCCGGKH KAAG
//
ID   XRCC4_MOUSE             Reviewed;         326 AA.
AC   Q924T3; Q8BKC9; Q8BU02; Q9D6U6;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=DNA repair protein XRCC4;
DE   AltName: Full=X-ray repair cross-complementing protein 4;
GN   Name=Xrcc4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=11738935; DOI=10.1016/S0921-8777(01)00107-0;
RA   Mori M., Itsukaichi H., Nakamura A., Sato K.;
RT   "Molecular characterization of ionizing radiation-hypersensitive
RT   mutant M10 cells.";
RL   Mutat. Res. 487:85-92(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Eye, Thymus, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=9875844; DOI=10.1016/S0092-8674(00)81714-6;
RA   Gao Y., Sun Y., Frank K.M., Dikkes P., Fujiwara Y., Seidl K.J.,
RA   Sekiguchi J.M., Rathbun G.A., Swat W., Wang J., Bronson R.T.,
RA   Malynn B.A., Bryans M., Zhu C., Chaudhuri J., Davidson L., Ferrini R.,
RA   Stamato T., Orkin S.H., Greenberg M.E., Alt F.W.;
RT   "A critical role for DNA end-joining proteins in both lymphogenesis
RT   and neurogenesis.";
RL   Cell 95:891-902(1998).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230 AND THR-231, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Involved in DNA nonhomologous end joining (NHEJ)
CC       required for double-strand break repair and V(D)J recombination.
CC       Binds to DNA and to DNA ligase IV (LIG4). The LIG4-XRCC4 complex
CC       is responsible for the NHEJ ligation step, and XRCC4 enhances the
CC       joining activity of LIG4. Binding of the LIG4-XRCC4 complex to DNA
CC       ends is dependent on the assembly of the DNA-dependent protein
CC       kinase complex DNA-PK to these DNA ends (By similarity).
CC   -!- SUBUNIT: Homodimer and homotetramer in solution. The homodimer
CC       associates with LIG4, and the LIG4-XRCC4 complex associates in a
CC       DNA-dependent manner with the DNA-PK complex formed by the Ku
CC       p70/p86 dimer (XRCC6/XRCC5) and PRKDC. Seems to interact directly
CC       with PRKDC but not with the Ku p70/86 dimer. Interacts with
CC       XLF/Cernunnos. Interacts with APTX and APLF (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q924T3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q924T3-2; Sequence=VSP_009475;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylation by CK2 promotes interaction with APTX (By
CC       similarity).
CC   -!- PTM: Monoubiquitinated (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice show growth defects, premature
CC       senescence, IR sensitivity, and inability to support V(D)J
CC       recombination. XRCC4 deficiency causes late embryonic lethality
CC       accompanied by defective lymphogenesis and defective neurogenesis
CC       manifested by extensive apoptotic death of newly generated
CC       postmitotic neuronal cells.
CC   -!- SIMILARITY: Belongs to the XRCC4 family.
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DR   EMBL; AB055154; BAB62316.1; -; mRNA.
DR   EMBL; AK009951; BAB26604.1; -; mRNA.
DR   EMBL; AK053612; BAC35447.1; -; mRNA.
DR   EMBL; AK088281; BAC40256.1; -; mRNA.
DR   EMBL; BC025538; AAH25538.1; -; mRNA.
DR   IPI; IPI00403043; -.
DR   IPI; IPI00403044; -.
DR   RefSeq; NP_082288.1; NM_028012.4.
DR   UniGene; Mm.37531; -.
DR   ProteinModelPortal; Q924T3; -.
DR   SMR; Q924T3; 1-199.
DR   STRING; Q924T3; -.
DR   PhosphoSite; Q924T3; -.
DR   PRIDE; Q924T3; -.
DR   Ensembl; ENSMUST00000022115; ENSMUSP00000022115; ENSMUSG00000021615.
DR   GeneID; 108138; -.
DR   KEGG; mmu:108138; -.
DR   UCSC; uc007rjn.1; mouse.
DR   CTD; 108138; -.
DR   MGI; MGI:1333799; Xrcc4.
DR   eggNOG; roNOG13838; -.
DR   GeneTree; ENSGT00390000017079; -.
DR   HOGENOM; HBG715521; -.
DR   HOVERGEN; HBG059517; -.
DR   InParanoid; Q924T3; -.
DR   OrthoDB; EOG48WC3N; -.
DR   ArrayExpress; Q924T3; -.
DR   Bgee; Q924T3; -.
DR   Genevestigator; Q924T3; -.
DR   GermOnline; ENSMUSG00000021615; Mus musculus.
DR   GO; GO:0005958; C:DNA-dependent protein kinase-DNA ligase 4 complex; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0007417; P:central nervous system development; IMP:MGI.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IMP:MGI.
DR   GO; GO:0033152; P:immunoglobulin V(D)J recombination; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0045190; P:isotype switching; IMP:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptosis; IMP:MGI.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI.
DR   GO; GO:0050769; P:positive regulation of neurogenesis; IMP:MGI.
DR   GO; GO:0002328; P:pro-B cell differentiation; IMP:MGI.
DR   GO; GO:0010332; P:response to gamma radiation; IMP:MGI.
DR   GO; GO:0010165; P:response to X-ray; IMP:MGI.
DR   GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR   InterPro; IPR010585; DNA_ds_break_repair_XRCC4.
DR   InterPro; IPR014751; XRCC4_C.
DR   InterPro; IPR009089; XRCC4_N.
DR   Gene3D; G3DSA:1.20.5.370; XRCC4_C; 1.
DR   Gene3D; G3DSA:2.170.210.10; XRCC4_N; 1.
DR   Pfam; PF06632; XRCC4; 1.
DR   SUPFAM; SSF50809; XRCC4_N; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; DNA damage; DNA recombination;
KW   DNA repair; Nucleus; Phosphoprotein; Ubl conjugation.
FT   CHAIN         1    326       DNA repair protein XRCC4.
FT                                /FTId=PRO_0000066048.
FT   REGION      180    212       Interacts with LIG4 (By similarity).
FT   COILED      131    165       Potential.
FT   COILED      185    209       Potential.
FT   MOD_RES     230    230       Phosphoserine.
FT   MOD_RES     231    231       Phosphothreonine.
FT   MOD_RES     254    254       Phosphoserine; by PRKDC (By similarity).
FT   MOD_RES     312    312       Phosphoserine; by PRKDC (By similarity).
FT   MOD_RES     319    319       Phosphoserine (By similarity).
FT   MOD_RES     320    320       Phosphoserine (By similarity).
FT   VAR_SEQ     293    326       LASSLPQTLKEESTSAENMSLETLRNSSPEDLFD -> KKK
FT                                YPSIMSTKVQRSLGEGGHG (in isoform 2).
FT                                /FTId=VSP_009475.
FT   CONFLICT     27     27       A -> T (in Ref. 3; BAB26604/BAC35447).
FT   CONFLICT     54     54       Q -> P (in Ref. 3; BAC40256).
FT   CONFLICT     93     93       Q -> R (in Ref. 3; BAB26604/BAC35447).
FT   CONFLICT    125    125       E -> D (in Ref. 3; BAB26604/BAC35447).
SQ   SEQUENCE   326 AA;  37061 MW;  58BD3422F7D2CBDB CRC64;
     MERKVSRIYL ASEPNVPYFL QVSWERAIGS GFVITLTDGH SAWTATVSEL EISQEADDMA
     MEKGKYIDEL RKALVPGSGA AGTYKFLFSK ESQHFSLEKE LKDVSFRLGS FNLDKVSNSA
     EVIRELICYC LDTITEKQAK NEHLQKENER LLRDWNDVQG RFEKCVSAKE ALEADLYQRF
     ILVLNEKKTK IRSLHKLLNE VQQLEESTKP ERENPCSDKT PEEHGLYDGS TDEESGAPVQ
     AAETLHKDDS IFSSPDVTDI APSRKRRHRM QKNLGTEPKM APQELPLQEK ERLASSLPQT
     LKEESTSAEN MSLETLRNSS PEDLFD
//
ID   TRI66_MOUSE             Reviewed;        1242 AA.
AC   Q924W6; Q5SEK4;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Tripartite motif-containing protein 66;
DE   AltName: Full=Transcriptional intermediary factor 1 delta;
GN   Name=Trim66; Synonyms=Tif1d;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
RP   2).
RX   MEDLINE=21418998; PubMed=11528127;
RA   Amid C., Bahr A., Mujica A., Sampson N., Bikar S.E., Winterpacht A.,
RA   Zabel B., Hankeln T., Schmidt E.R.;
RT   "Comparative genomic sequencing reveals a strikingly similar
RT   architecture of a conserved syntenic region on human chromosome
RT   11p15.3 (including gene ST5) and mouse chromosome 7.";
RL   Cytogenet. Cell Genet. 93:284-290(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, MOTIF, INTERACTION WITH CBX5, CBX1 AND CBX3,
RP   MUTAGENESIS OF VAL-889 AND LEU-891, AND SUBCELLULAR LOCATION.
RX   PubMed=15322135; DOI=10.1074/jbc.M404779200;
RA   Khetchoumian K., Teletin M., Mark M., Lerouge T., Cervino M.,
RA   Oulad-Abdelghani M., Chambon P., Losson R.;
RT   "TIF1delta, a novel HP1-interacting member of the transcriptional
RT   intermediary factor 1 (TIF1) family expressed by elongating
RT   spermatids.";
RL   J. Biol. Chem. 279:48329-48341(2004).
CC   -!- FUNCTION: May function as transcription repressor; The repressive
CC       effects are mediated, at least in part, by recruitment of
CC       deacetylase activity. May play a role as negative regulator of
CC       postmeiotic genes acting through CBX3 complex formation and
CC       centromere association.
CC   -!- SUBUNIT: Can form homo- and heterodimers. Interacts with CBX5,
CC       CBX1 and CBX3 via PxVxL motif.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Forms discrete foci within the
CC       centromeric chromocenter and surrounding nucleoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q924W6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q924W6-2; Sequence=VSP_026555, VSP_026556;
CC   -!- TISSUE SPECIFICITY: Predominant in testis, specifically in
CC       elongating spermatids.
CC   -!- DEVELOPMENTAL STAGE: No significant expression in testis of 2- or
CC       3-week-old mouse, but clear detection at the age of 4 weeks.
CC   -!- SIMILARITY: Contains 2 B box-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 bromo domain.
CC   -!- SIMILARITY: Contains 1 PHD-type zinc finger.
CC   -----------------------------------------------------------------------
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DR   EMBL; AJ307670; CAC38114.1; -; Genomic_DNA.
DR   EMBL; AY572455; AAS78677.1; -; mRNA.
DR   IPI; IPI00656263; -.
DR   IPI; IPI00853877; -.
DR   UniGene; Mm.183528; -.
DR   ProteinModelPortal; Q924W6; -.
DR   SMR; Q924W6; 4-103, 994-1175.
DR   STRING; Q924W6; -.
DR   PRIDE; Q924W6; -.
DR   Ensembl; ENSMUST00000033339; ENSMUSP00000033339; ENSMUSG00000031026.
DR   Ensembl; ENSMUST00000106740; ENSMUSP00000102351; ENSMUSG00000031026.
DR   Ensembl; ENSMUST00000106741; ENSMUSP00000102352; ENSMUSG00000031026.
DR   MGI; MGI:2152406; Trim66.
DR   GeneTree; ENSGT00530000062982; -.
DR   HOVERGEN; HBG057849; -.
DR   InParanoid; Q924W6; -.
DR   ArrayExpress; Q924W6; -.
DR   Bgee; Q924W6; -.
DR   CleanEx; MM_TRIM66; -.
DR   Genevestigator; Q924W6; -.
DR   GO; GO:0010369; C:chromocenter; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
DR   GO; GO:0016564; F:transcription repressor activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:MGI.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:1.20.920.10; Bromodomain; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00249; PHD; 2.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; FALSE_NEG.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS50119; ZF_BBOX; 2.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Bromodomain; Coiled coil; Metal-binding;
KW   Nucleus; Repeat; Zinc; Zinc-finger.
FT   CHAIN         1   1242       Tripartite motif-containing protein 66.
FT                                /FTId=PRO_0000220376.
FT   DOMAIN     1084   1156       Bromo.
FT   ZN_FING       1     46       B box-type 1; atypical.
FT   ZN_FING      60    101       B box-type 2.
FT   ZN_FING     996   1043       PHD-type.
FT   COILED      130    200       Potential.
FT   MOTIF       887    891       PxVxL motif.
FT   COMPBIAS    329    493       Pro-rich.
FT   VAR_SEQ      97     98       Missing (in isoform 2).
FT                                /FTId=VSP_026555.
FT   VAR_SEQ     794    825       MESEDCTRFSDSVGQGPTASSLDGSKDLAIPS -> V (in
FT                                isoform 2).
FT                                /FTId=VSP_026556.
FT   MUTAGEN     889    889       V->A: Drastic decrease of CBX5, CBX1 and
FT                                CBX3 binding; When associated with A-891.
FT   MUTAGEN     891    891       L->A: Drastic decrease of CBX5, CBX1 and
FT                                CBX3 binding; When associated with A-889.
FT   CONFLICT     43     43       I -> L (in Ref. 2; CAC38114).
FT   CONFLICT    879    879       T -> A (in Ref. 2; CAC38114).
FT   CONFLICT    919    919       S -> N (in Ref. 2; CAC38114).
SQ   SEQUENCE   1242 AA;  136759 MW;  5CBAEDB6DD4633B8 CRC64;
     MARNCSECKE KRAAHILCTY CNRWLCSSCT EEHRHVPAPG GPIFARAQKG SSGVNGGSGD
     FALYCPLHTQ EVLKLFCETC DVLTCHSCLM VEHKEHRCRH VEEVLQNQRM LLESVTSQVA
     HKKSSLQTSA KQIEDRIFEV KHQHRKVENQ IKMAKMVLMN ELNKQANGLI EELEGITNER
     KRKLEQQLQS IMVLNRQFEH VQNFINWAVC SKSSVPFLFS KELIVFQMQR LLETRCNTDP
     GSPWSIRFTW EPNFWTKQLA SLGCITTEGG QLTRADAAAA SYGSLQGQPS FYQSHQAPMA
     QQEALSHPSH KFQSPALCSS SVCCSHCSPV SPSLKGQVPP PSIHPAHSFR QPSEMVPHQL
     GSLQCSTLLP REKELACSPH PPKLMQPWLE PQPPAEQEST SQRPGPQLVS QPVCIVPPQD
     VQPGAHAQPT IQTPSIQVQL GHHQKLKLSH FQQQPQQQPP PPPPPPPPPQ HAPPPLPPSQ
     HLASSQHESP PGPACSQNVD IMHHKFELEE MQKDLELLLQ AQQPSLQLSQ TKSPQHLQQT
     IVGQINYIVR QPAPVQSQSQ EETLQVTEEP PAPEGPKPAL PVDKNTAAPL PQTSGEETPH
     SVPPVDGTSQ HSSPNVVRKH ATSVSIMGFS NTVEMELSST RLARTIEPQI HRVSSLTAAP
     THTIPSLLSG PPQTVSSLMS VSNHAMPSLT ASHLQPVPNL VRGTFQSTSN LRGDSSQAIT
     GLASNHSQAG PSLMSGHTQA APSLATCPLQ GMPPVSDVHV EPRSVSSPGS GPAAESLGTR
     DGAESSLGNA LCKMESEDCT RFSDSVGQGP TASSLDGSKD LAIPSELEEP INLSVKKPFL
     APVINTSTAL QQYRNPKEYE NFEQGALELD TKENSDIRTI SSEPKIPYVR LERLKICAAS
     SGEMPVFKLK PQKNSQDGSF LLVIECGTES SSMSIKVSQN SLPDASQGPG LGGRKVTVTS
     LTGQQPQEVE STSEEHRLIP RAPGAKKNTP APIENEDFCA VCINGGELLC CDRCPKVYHL
     SCHVPALLSF PGGEWVCTLC RSLTQPEMEY DCENARYGHP GVRVLPGLSM YDQKKCEKLV
     LSLCCNSLSL PFHEPVSPLA RHYYQIIKRP MDLSIIRRKL QKKDPAHYTT PEEVVSDVRL
     MFWNCAKFNY PDSEVAEAGR CLEVFFEGWL KEIYPDKCFA QPQQEDSDSE DVSGESGCST
     PQGFPWPPYM QEGIQPKRRR RHMENEKTKR VSFRLANSIS QV
//
ID   TRPS1_MOUSE             Reviewed;        1281 AA.
AC   Q925H1;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-FEB-2011, entry version 73.
DE   RecName: Full=Zinc finger transcription factor Trps1;
GN   Name=Trps1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOMENTAL STAGE.
RC   TISSUE=Fetal intestine;
RX   MEDLINE=21181829; PubMed=11285235; DOI=10.1093/emboj/20.7.1715;
RA   Malik T.H., Shoichet S.A., Latham P., Kroll T.G., Peters L.L.,
RA   Shivdasani R.A.;
RT   "Transcriptional repression and developmental functions of the
RT   atypical vertebrate GATA protein TRPS1.";
RL   EMBO J. 20:1715-1725(2001).
RN   [2]
RP   INTERACTION WITH RNF4.
RX   PubMed=12885770; DOI=10.1074/jbc.M306259200;
RA   Kaiser F.J., Moeroey T., Chang G.T., Horsthemke B., Luedecke H.J.;
RT   "The RING finger protein RNF4, a co-regulator of transcription,
RT   interacts with the TRPS1 transcription factor.";
RL   J. Biol. Chem. 278:38780-38785(2003).
CC   -!- FUNCTION: Transcriptional repressor. Binds specifically to GATA
CC       sequences and represses expression of GATA-regulated genes at
CC       selected sites and stages in vertebrate development.
CC   -!- SUBUNIT: Interacts with RNF4; regulates TRPS1 repressor activity.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: In the embryo, expression is detected in both
CC       visceral and skeletal tissues. Found in the maxilla, mandible,
CC       snout, prospective phalanges and in the femoral head within the
CC       developing hip. Also expressed in the hair follicles.
CC   -!- DEVELOPMENTAL STAGE: Detected prior to E7.5, with peak levels at
CC       around E11.5. In the developing limbs and face, levels are highest
CC       at E13.5 and decline dramatically thereafter.
CC   -!- PTM: Sumoylated. Sumoylation in the repressor domain inhibits the
CC       transcription repression activity. Sumoylation on Lys-1201 is the
CC       major site. Appears to be sumoylated on multiple sites (By
CC       similarity).
CC   -!- SIMILARITY: Contains 7 C2H2-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 GATA-type zinc finger.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF346836; AAK39508.1; -; mRNA.
DR   IPI; IPI00126883; -.
DR   UniGene; Mm.30466; -.
DR   UniGene; Mm.442375; -.
DR   UniGene; Mm.476882; -.
DR   ProteinModelPortal; Q925H1; -.
DR   SMR; Q925H1; 218-245, 330-360, 426-468, 500-579, 605-644, 690-719, 890-938.
DR   STRING; Q925H1; -.
DR   PhosphoSite; Q925H1; -.
DR   PRIDE; Q925H1; -.
DR   Ensembl; ENSMUST00000077935; ENSMUSP00000077089; ENSMUSG00000038679.
DR   UCSC; uc007vqz.1; mouse.
DR   MGI; MGI:1927616; Trps1.
DR   GeneTree; ENSGT00550000074392; -.
DR   HOGENOM; HBG281997; -.
DR   HOVERGEN; HBG067120; -.
DR   InParanoid; Q925H1; -.
DR   ArrayExpress; Q925H1; -.
DR   Bgee; Q925H1; -.
DR   CleanEx; MM_TRPS1; -.
DR   Genevestigator; Q925H1; -.
DR   GermOnline; ENSMUSG00000038679; Mus musculus.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0016564; F:transcription repressor activity; IPI:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR000679; Znf_GATA.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   Gene3D; G3DSA:3.30.50.10; Znf_NHR/GATA; 1.
DR   Pfam; PF00320; GATA; 1.
DR   PRINTS; PR00619; GATAZNFINGER.
DR   SMART; SM00355; ZnF_C2H2; 9.
DR   SMART; SM00401; ZnF_GATA; 1.
DR   PROSITE; PS00344; GATA_ZN_FINGER_1; 1.
DR   PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW   Repeat; Repressor; Transcription; Transcription regulation;
KW   Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1   1281       Zinc finger transcription factor Trps1.
FT                                /FTId=PRO_0000083509.
FT   ZN_FING     222    247       C2H2-type 1; atypical.
FT   ZN_FING     333    358       C2H2-type 2; atypical.
FT   ZN_FING     614    637       C2H2-type 3; atypical.
FT   ZN_FING     666    689       C2H2-type 4.
FT   ZN_FING     692    715       C2H2-type 5.
FT   ZN_FING     896    920       GATA-type.
FT   ZN_FING    1215   1237       C2H2-type 6.
FT   ZN_FING    1243   1267       C2H2-type 7.
FT   REGION      985   1184       Mediates interaction with RNF4.
FT   REGION     1163   1281       Transcriptional repressor domain (By
FT                                similarity).
FT   MOD_RES     127    127       Phosphoserine (By similarity).
FT   MOD_RES     157    157       Phosphoserine (By similarity).
FT   MOD_RES     178    178       Phosphoserine (By similarity).
FT   MOD_RES     184    184       Phosphoserine (By similarity).
FT   MOD_RES     892    892       Phosphoserine (By similarity).
FT   MOD_RES     978    978       Phosphoserine (By similarity).
FT   MOD_RES    1066   1066       Phosphoserine (By similarity).
FT   MOD_RES    1081   1081       Phosphoserine (By similarity).
FT   MOD_RES    1085   1085       Phosphoserine (By similarity).
FT   CROSSLNK   1192   1192       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK   1201   1201       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
SQ   SEQUENCE   1281 AA;  141035 MW;  F0A71900C2357898 CRC64;
     MVRKKHPPLR NVASEGEGQT LEPTATESKV SGKNKELSAD QMSENTDQSD VAELNSKEEH
     STHGQEPSSS GKKDLQISGL SEKAGFNYES PSKGGSLVSF PHDEVTDRNM LAFSSPAAGG
     VCEPLKSPQR AEADDPQDMA CTPSGDSLET KEEHKMSPKA TEETGPVQSG QANCQGLSPV
     SVASKNPQVP SDGGVRLSKP KGDLLVNDNP DPAPLSPELQ DFKCNICGYG YYGNDPTDLI
     KHFRKYHLGL HNRTRQDAEL DSKILALHNM VQFSHSKDFQ KVNRSVLSGV LQDISSSRPA
     LLNGTYDVQV TSGGTFIGIG RKTPDCQGNT KYFRCKFCNF TYMGNSSTEL EQHFLQTHPN
     KIKVSLPSSE GVKPSEKNSN KSIPALRASD SGDVGKWQDK MTVKAGDDTP VGYSVPIKPL
     DSSRQNGTEA TSYYWCKFCS FSCESSSSLK LLEHYGKQHG AVQSGGLNPE LNDKLPRGSV
     INQNDLAKSV EGEPLTKPEK GLSGAKKKDF PSKGAEDNMV TSYNCQFCDF RYSKSHGPDV
     IVVGPLLRHY QQLHNIHKCT IKHCPFCPRG LCSPEKHLGE ITYPFACRKS NCSHCALLLL
     HLSPGVAGSS RVKHQCHQCS FSTPDVDVLL FHYETVHESQ ASDVKQEANH LLGSDGQQAV
     RDSKEHSCTK CDFITQVEEE ISRHYRRAHS CYKCRQCSFT AADTQSLLEH FNTVHCQEQE
     ITTANGEEGG HAIPTIKEEP KIDLKVYSLL NPDSKMGETV PESIVKREKL DDKEGLKDKI
     WTESSTDDLR GVAWRGADIL RGSPSYTQAS LGLLTPVSSS QEQTKTLRDS PNVEAAHLAR
     PMYGLAVDTK GFLQGAPAGS EKSASLTQQY PASGESKTKD ESQSLLRRRR GSGVFCANCL
     TTKTSLWRKN ANGGYVCNAC GLYQKLHSTP RPLNIIKQNN GEQIIRRRTR KRLNPEALQA
     EQLNKQQRGS GEEQVNGSPL ERRSEDHLSE SHPREIPLPS LSKYEAQGSL TKSHSAQQPV
     LVSQALDIHK RMQPLHIQIK SPQESTGDPG NSSSVSDGKG SSERGSPIEK YMRPAKHPNY
     SPPGSPIEKY QYPLFGVPFV HNDFQSEADW LRFWSKYKLS VPGNPHYLSH VPGLPNPCQN
     YVPYPTFNLP PHFSAVGSDN DIPLDLAIKH SRPGPTANGA SKEKTKAPPT VKNEDPLNVV
     KTEKVDRSTQ DELSTKCVHC GIVFLDEVMY ALHMSCHGDS GPFQCSICQH LCTDKYDFTT
     HIQRGLHRNN AQAEKNGKPK E
//
ID   ATAD3_MOUSE             Reviewed;         591 AA.
AC   Q925I1; Q3UE74; Q69ZM7; Q8C6C6;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=ATPase family AAA domain-containing protein 3;
DE   AltName: Full=AAA-ATPase TOB3;
GN   Name=Atad3; Synonyms=Atad3a, Kiaa1273;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c;
RA   Parng C., Piepenhagen P.A., Casanova J., Pillai S.;
RT   "TOB3 is a novel AAA-ATPase involved in protein secretion.";
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryonic tail;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Lung, and Sympathetic ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, Colon, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 302-311 AND 478-485, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-490 AND LYS-512, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q925I1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q925I1-2; Sequence=VSP_015643;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF343079; AAK38648.1; -; mRNA.
DR   EMBL; AK075921; BAC36055.1; -; mRNA.
DR   EMBL; AK148974; BAE28707.1; -; mRNA.
DR   EMBL; AK149702; BAE29037.1; -; mRNA.
DR   EMBL; AK150037; BAE29259.1; -; mRNA.
DR   EMBL; AK166099; BAE38570.1; -; mRNA.
DR   EMBL; AK173141; BAD32419.1; -; Unassigned_RNA.
DR   EMBL; BC023301; AAH23301.1; -; mRNA.
DR   EMBL; BC058373; AAH58373.1; -; mRNA.
DR   EMBL; BC060036; AAH60036.1; -; mRNA.
DR   IPI; IPI00126913; -.
DR   IPI; IPI00464208; -.
DR   RefSeq; NP_849534.2; NM_179203.3.
DR   UniGene; Mm.241152; -.
DR   ProteinModelPortal; Q925I1; -.
DR   SMR; Q925I1; 308-562.
DR   STRING; Q925I1; -.
DR   PhosphoSite; Q925I1; -.
DR   PRIDE; Q925I1; -.
DR   Ensembl; ENSMUST00000030903; ENSMUSP00000030903; ENSMUSG00000029036.
DR   Ensembl; ENSMUST00000105594; ENSMUSP00000101219; ENSMUSG00000029036.
DR   GeneID; 108888; -.
DR   KEGG; mmu:108888; -.
DR   UCSC; uc008wen.1; mouse.
DR   CTD; 108888; -.
DR   MGI; MGI:1919214; Atad3a.
DR   GeneTree; ENSGT00560000077230; -.
DR   HOGENOM; HBG380192; -.
DR   HOVERGEN; HBG058506; -.
DR   InParanoid; Q925I1; -.
DR   OMA; AVNDRID; -.
DR   OrthoDB; EOG4ZCT46; -.
DR   PhylomeDB; Q925I1; -.
DR   NextBio; 361415; -.
DR   ArrayExpress; Q925I1; -.
DR   Bgee; Q925I1; -.
DR   CleanEx; MM_ATAD3A; -.
DR   Genevestigator; Q925I1; -.
DR   GermOnline; ENSMUSG00000029036; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR021911; DUF3523.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF12037; DUF3523; 1.
DR   SMART; SM00382; AAA; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Coiled coil;
KW   Direct protein sequencing; Nucleotide-binding.
FT   CHAIN         1    591       ATPase family AAA domain-containing
FT                                protein 3.
FT                                /FTId=PRO_0000084801.
FT   NP_BIND     351    358       ATP (Potential).
FT   COILED       55    216       Potential.
FT   MOD_RES     490    490       N6-acetyllysine.
FT   MOD_RES     512    512       N6-acetyllysine.
FT   VAR_SEQ     422    501       EKISEDLRATLNAFLHRTGQHSSKFMLVLASNQPEQFDWAI
FT                                NDRIDEMVCFALPQREERERLVRMYFDKYVLKPATEGKQ
FT                                -> R (in isoform 2).
FT                                /FTId=VSP_015643.
FT   CONFLICT    376    376       T -> K (in Ref. 2; BAC36055).
SQ   SEQUENCE   591 AA;  66742 MW;  66B599114B94620E CRC64;
     MSWLFGIKGP KGEGTGPPLP LPPAQPGAEG GGDRGAGDRP SPKDKWSNFD PTGLERAAKA
     ARELEHSRHA KEALSLAQMQ EQTLQLEQQS KLKEYEAAVE QLKSEQIRVQ AEERRKTLTE
     ETRQHQARAQ YQDKLARQRY EDQLKQQQLL NEENLRKQEE SVQKQEAIRR ATVEREMELR
     HKNEMLRVEA EARARAKADR ENADIIREQI RLKAAEHRQT ILESIRTAGT LLGEGFRAFV
     TDWDKVTATV AGLTLLAVGV YSAKNATSVA GRYIEARLGK PSLVRETSRI SVLEALRHPI
     QVSRRLVSRP QDALEGVILS PSLEARVRDI AIATRNTKKN KSLYRNVLMY GPPGTGKTLF
     AKKLALHSGM DYAIMTGGDV APMGREGVTA MHKVFDWAST SRRGLLLFVD EADAFLRKRA
     TEKISEDLRA TLNAFLHRTG QHSSKFMLVL ASNQPEQFDW AINDRIDEMV CFALPQREER
     ERLVRMYFDK YVLKPATEGK QRLKVAQFDY GKKCSEVAQL TEGMSGREIA QLAVAWQAMA
     YSSEDGVLTE AMMDARVQDA VQQHQQKMQW LKVERPDSQT NKPPHPSLLS C
//
ID   MED1_MOUSE              Reviewed;        1575 AA.
AC   Q925J9; A2A526; A2A528; O88323; Q3UHV0; Q6AXD5; Q8BW37; Q8BX19;
AC   Q8VDQ7; Q925K0;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 1;
DE   AltName: Full=Mediator complex subunit 1;
DE   AltName: Full=Peroxisome proliferator-activated receptor-binding protein;
DE            Short=PBP;
DE            Short=PPAR-binding protein;
DE   AltName: Full=Thyroid hormone receptor-associated protein complex 220 kDa component;
DE            Short=Trap220;
DE   AltName: Full=Thyroid receptor-interacting protein 2;
DE            Short=TR-interacting protein 2;
DE            Short=TRIP-2;
GN   Name=Med1; Synonyms=Crsp210, Drip205, Pbp, Pparbp, Trap220, Trip2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, TISSUE SPECIFICITY,
RP   AND INTERACTION WITH PPARA; PPARG; RARA; RXRA AND THRB.
RC   TISSUE=Liver;
RX   MEDLINE=97467333; PubMed=9325263; DOI=10.1074/jbc.272.41.25500;
RA   Zhu Y., Qi C., Jain S., Rao M.S., Reddy J.K.;
RT   "Isolation and characterization of PBP, a protein that interacts with
RT   peroxisome proliferator-activated receptor.";
RL   J. Biol. Chem. 272:25500-25506(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND VARIANTS SER-960 AND
RP   MET-1348.
RC   STRAIN=ILS, and ISS;
RX   MEDLINE=21363810; PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY,
RP   DEVELOPMENTAL STAGE, AND VARIANTS SER-960 AND MET-1348.
RC   STRAIN=129/Ola;
RX   PubMed=14500757; DOI=10.1210/me.2003-0097;
RA   Landles C., Chalk S., Steel J.H., Rosewell I., Spencer-Dene B.,
RA   Lalani E.-N., Parker M.G.;
RT   "The thyroid hormone receptor-associated protein TRAP220 is required
RT   at distinct embryonic stages in placental, cardiac, and hepatic
RT   development.";
RL   Mol. Endocrinol. 17:2418-2435(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-389 (ISOFORMS 1/4), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-964 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, and Ovary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6, and Czech II; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=10882104; DOI=10.1016/S1097-2765(00)80247-6;
RA   Ito M., Yuan C.-X., Okano H.J., Darnell R.B., Roeder R.G.;
RT   "Involvement of the TRAP220 component of the TRAP/SMCC coactivator
RT   complex in embryonic development and thyroid hormone action.";
RL   Mol. Cell 5:683-693(2000).
RN   [8]
RP   INTERACTION WITH YWHAH.
RX   MEDLINE=21168078; PubMed=11266503; DOI=10.1210/me.15.4.501;
RA   Zilliacus J., Holter E., Wakui H., Tazawa H., Treuter E.,
RA   Gustafsson J.-A.;
RT   "Regulation of glucocorticoid receptor activity by 14-3-3-dependent
RT   intracellular relocalization of the corepressor RIP140.";
RL   Mol. Endocrinol. 15:501-511(2001).
RN   [9]
RP   FUNCTION.
RX   PubMed=12037571; DOI=10.1038/417563a;
RA   Ge K., Guermah M., Yuan C.-X., Ito M., Wallberg A.E., Spiegelman B.M.,
RA   Roeder R.G.;
RT   "Transcription coactivator TRAP220 is required for PPAR gamma 2-
RT   stimulated adipogenesis.";
RL   Nature 417:563-567(2002).
RN   [10]
RP   FUNCTION, AND INTERACTION OF THE MEDIATOR COMPLEX WITH ESR1 AND ESR2.
RX   PubMed=11867769; DOI=10.1073/pnas.261715899;
RA   Kang Y.K., Guermah M., Yuan C.-X., Roeder R.G.;
RT   "The TRAP/Mediator coactivator complex interacts directly with
RT   estrogen receptors alpha and beta through the TRAP220 subunit and
RT   directly enhances estrogen receptor function in vitro.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:2642-2647(2002).
RN   [11]
RP   FUNCTION, AND INTERACTION WITH PPARGC1A.
RX   PubMed=14636573; DOI=10.1016/S1097-2765(03)00391-5;
RA   Wallberg A.E., Yamamura S., Malik S., Spiegelman B.M., Roeder R.G.;
RT   "Coordination of p300-mediated chromatin remodeling and TRAP/mediator
RT   function through coactivator PGC-1alpha.";
RL   Mol. Cell 12:1137-1149(2003).
RN   [12]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15150259; DOI=10.1074/jbc.M402391200;
RA   Jia Y., Qi C., Kashireddy P., Surapureddi S., Zhu Y.-J., Rao M.S.,
RA   Le Roith D., Chambon P., Gonzalez F.J., Reddy J.K.;
RT   "Transcription coactivator PBP, the peroxisome proliferator-activated
RT   receptor (PPAR)-binding protein, is required for PPARalpha-regulated
RT   gene expression in liver.";
RL   J. Biol. Chem. 279:24427-24434(2004).
RN   [13]
RP   ERRATUM.
RA   Jia Y., Qi C., Kashireddy P., Surapureddi S., Zhu Y.-J., Rao M.S.,
RA   Le Roith D., Chambon P., Gonzalez F.J., Reddy J.K.;
RL   J. Biol. Chem. 279:29870-29870(2004).
RN   [14]
RP   FUNCTION, AND INTERACTION OF THE MEDIATOR COMPLEX WITH THRA.
RX   PubMed=15340084; DOI=10.1128/MCB.24.18.8244-8254.2004;
RA   Malik S., Guermah M., Yuan C.-X., Wu W., Yamamura S., Roeder R.G.;
RT   "Structural and functional organization of TRAP220, the TRAP/mediator
RT   subunit that is targeted by nuclear receptors.";
RL   Mol. Cell. Biol. 24:8244-8254(2004).
RN   [15]
RP   FUNCTION, AND ASSOCIATION WITH PROMOTER REGIONS.
RX   PubMed=16137621; DOI=10.1016/j.molcel.2005.08.008;
RA   Park S.W., Li G., Lin Y.-P., Barrero M.J., Ge K., Roeder R.G.,
RA   Wei L.-N.;
RT   "Thyroid hormone-induced juxtaposition of regulatory elements/factors
RT   and chromatin remodeling of Crabp1 dependent on MED1/TRAP220.";
RL   Mol. Cell 19:643-653(2005).
RN   [16]
RP   FUNCTION, INTERACTION WITH GATA1, AND ASSOCIATION WITH PROMOTER
RP   REGIONS.
RX   PubMed=17132730; DOI=10.1073/pnas.0604494103;
RA   Stumpf M., Waskow C., Kroetschel M., van Essen D., Rodriguez P.,
RA   Zhang X., Guyot B., Roeder R.G., Borggrefe T.;
RT   "The mediator complex functions as a coactivator for GATA-1 in
RT   erythropoiesis via subunit Med1/TRAP220.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:18504-18509(2006).
RN   [17]
RP   ERRATUM.
RA   Stumpf M., Waskow C., Kroetschel M., van Essen D., Rodriguez P.,
RA   Zhang X., Guyot B., Roeder R.G., Borggrefe T.;
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1442-1442(2007).
RN   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-953 AND SER-955, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 641-654 IN COMPLEX WITH RARB
RP   AND RXRA.
RX   PubMed=15528208; DOI=10.1074/jbc.M409302200;
RA   Pogenberg V., Guichou J.F., Vivat-Hannah V., Kammerer S., Perez E.,
RA   Germain P., de Lera A.R., Gronemeyer H., Royer C.A., Bourguet W.;
RT   "Characterization of the interaction between retinoic acid
RT   receptor/retinoid X receptor (RAR/RXR) heterodimers and
RT   transcriptional coactivators through structural and fluorescence
RT   anisotropy studies.";
RL   J. Biol. Chem. 280:1625-1633(2005).
CC   -!- FUNCTION: Component of the Mediator complex, a coactivator
CC       involved in the regulated transcription of nearly all RNA
CC       polymerase II-dependent genes. Mediator functions as a bridge to
CC       convey information from gene-specific regulatory proteins to the
CC       basal RNA polymerase II transcription machinery. Mediator is
CC       recruited to promoters by direct interactions with regulatory
CC       proteins and serves as a scaffold for the assembly of a functional
CC       preinitiation complex with RNA polymerase II and the general
CC       transcription factors. Essential for embryogenesis, including
CC       development of the central nervous system, heart, liver and
CC       placenta and for erythropoiesis. Also required for normal
CC       transcriptional control of thyroid-stimulating hormone beta (TSHB)
CC       in the pituitary.
CC   -!- SUBUNIT: Interacts with AR, CTNNB1, GABPA, GLI3, TP53 and VDR (By
CC       similarity). Binds DNA (By similarity). Component of the Mediator
CC       complex, which is composed of MED1, MED4, MED6, MED7, MED8, MED9,
CC       MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17,
CC       MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26,
CC       MED27, MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The
CC       MED12, MED13, CCNC and CDK8 subunits form a distinct module termed
CC       the CDK8 module. Mediator containing the CDK8 module is less
CC       active than Mediator lacking this module in supporting
CC       transcriptional activation. Individual preparations of the
CC       Mediator complex lacking one or more distinct subunits have been
CC       variously termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. This subunit
CC       specifically interacts with a number of nuclear receptors in a
CC       ligand-dependent fashion including ESR1, ESR2, PPARA, PPARG, RXRA,
CC       RXRG, THRA and THRB. Interacts with GATA1, PPARGC1A and YWHAH.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=A subset of the protein may
CC       enter the nucleolus subsequent to phosphorylation by MAPK1 or
CC       MAPK3 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q925J9-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q925J9-2; Sequence=VSP_051893, VSP_051896;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q925J9-3; Sequence=VSP_051894, VSP_051895;
CC       Name=4;
CC         IsoId=Q925J9-4; Sequence=VSP_051892;
CC   -!- TISSUE SPECIFICITY: Widely expressed in the adult, with high
CC       levels of expression in the liver, lung, intestinal mucosa, kidney
CC       cortex, thymic cortex, splenic follicle and seminiferous
CC       epithelium in testis. Also expressed in the adult heart, brain,
CC       spleen and skeletal muscle.
CC   -!- DEVELOPMENTAL STAGE: Widely expressed during embryonic
CC       development; at stages E9.5-10.5, expression is strongest in
CC       neural tissues. At E11.5-E12.5, expression is abundant throughout
CC       embryonic tissues, being strongest in the developing liver,
CC       primitive gut, nasopharynx, and developing limb buds. Moderately
CC       expressed at this stage in the brain and optic stalk, branchial
CC       arch and urogential ridge. Expressed at a low level in the heart.
CC       By stage E13.5-E14.5, expression is abundant in the forebrain,
CC       vagus nerve, dorsal root ganglia, nasopharynx, kidney, liver,
CC       pancreas, intestine, gut, thymus, lung, genital tubercle, tongue
CC       and lower jaw. Moderately expressed in the midbrain and expressed
CC       at a low level in the heart and large blood vessels. In the
CC       developing placenta, expression is moderate in the giant and
CC       spongiotrophoblast cell layers and strongest in the labyrinthine
CC       portion throughout E9.5-E13.5.
CC   -!- PTM: Phosphorylated by MAPK1 or MAPK3 during G2/M phase which may
CC       enhance protein stability and promote entry into the nucleolus (By
CC       similarity). Phosphorylated upon DNA damage, probably by ATM or
CC       ATR.
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH21440.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; AF000294; AAC31118.1; -; mRNA.
DR   EMBL; AF332073; AAK56101.1; -; mRNA.
DR   EMBL; AF332074; AAK56102.1; -; mRNA.
DR   EMBL; AY176046; AAN75014.1; -; Genomic_DNA.
DR   EMBL; AK049203; BAC33607.2; -; mRNA.
DR   EMBL; AK054437; BAC35779.2; -; mRNA.
DR   EMBL; AK147199; BAE27757.1; -; mRNA.
DR   EMBL; AL591205; CAM21264.1; -; Genomic_DNA.
DR   EMBL; AL591205; CAM21266.1; -; Genomic_DNA.
DR   EMBL; BC021440; AAH21440.1; ALT_INIT; mRNA.
DR   EMBL; BC079636; AAH79636.1; -; mRNA.
DR   IPI; IPI00313307; -.
DR   IPI; IPI00474642; -.
DR   IPI; IPI00648562; -.
DR   IPI; IPI00656238; -.
DR   PIR; T02885; T02885.
DR   RefSeq; NP_001073587.1; NM_001080118.1.
DR   RefSeq; NP_038662.2; NM_013634.2.
DR   RefSeq; NP_598788.2; NM_134027.2.
DR   UniGene; Mm.12926; -.
DR   PDB; 1XDK; X-ray; 2.90 A; C/D/G/H=641-654.
DR   PDBsum; 1XDK; -.
DR   PhosphoSite; Q925J9; -.
DR   PRIDE; Q925J9; -.
DR   Ensembl; ENSMUST00000018304; ENSMUSP00000018304; ENSMUSG00000018160.
DR   Ensembl; ENSMUST00000092735; ENSMUSP00000090411; ENSMUSG00000018160.
DR   Ensembl; ENSMUST00000107541; ENSMUSP00000103165; ENSMUSG00000018160.
DR   Ensembl; ENSMUST00000107545; ENSMUSP00000103169; ENSMUSG00000018160.
DR   GeneID; 19014; -.
DR   KEGG; mmu:19014; -.
DR   UCSC; uc007lfo.1; mouse.
DR   UCSC; uc007lfp.1; mouse.
DR   UCSC; uc007lfq.1; mouse.
DR   CTD; 19014; -.
DR   MGI; MGI:1100846; Med1.
DR   eggNOG; roNOG06896; -.
DR   GeneTree; ENSGT00590000083089; -.
DR   HOVERGEN; HBG101127; -.
DR   InParanoid; Q925J9; -.
DR   OMA; RNKKPSL; -.
DR   OrthoDB; EOG40CHG4; -.
DR   NextBio; 295432; -.
DR   ArrayExpress; Q925J9; -.
DR   Bgee; Q925J9; -.
DR   CleanEx; MM_MED1; -.
DR   Genevestigator; Q925J9; -.
DR   GermOnline; ENSMUSG00000018160; Mus musculus.
DR   GO; GO:0016592; C:mediator complex; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR   GO; GO:0007420; P:brain development; IMP:MGI.
DR   GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR   GO; GO:0006260; P:DNA replication; IMP:MGI.
DR   GO; GO:0035050; P:embryonic heart tube development; IMP:MGI.
DR   GO; GO:0035162; P:embryonic hemopoiesis; IMP:MGI.
DR   GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
DR   GO; GO:0001892; P:embryonic placenta development; IMP:MGI.
DR   GO; GO:0060750; P:epithelial cell proliferation involved in mammary gland duct elongation; IMP:MGI.
DR   GO; GO:0045444; P:fat cell differentiation; IMP:MGI.
DR   GO; GO:0007595; P:lactation; IMP:MGI.
DR   GO; GO:0001889; P:liver development; IMP:MGI.
DR   GO; GO:0060745; P:mammary gland branching involved in pregnancy; IMP:MGI.
DR   GO; GO:0060744; P:mammary gland branching involved in thelarche; IMP:MGI.
DR   GO; GO:0009887; P:organ morphogenesis; IMP:MGI.
DR   GO; GO:0033601; P:positive regulation of mammary gland epithelial cell proliferation; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0006590; P:thyroid hormone generation; IMP:MGI.
DR   InterPro; IPR019680; Mediator_Med1_met/fun.
DR   Pfam; PF10744; Med1-Trap220; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Alternative splicing;
KW   Developmental protein; DNA-binding; Nucleus; Phosphoprotein; Repeat;
KW   Transcription; Transcription regulation.
FT   CHAIN         1   1575       Mediator of RNA polymerase II
FT                                transcription subunit 1.
FT                                /FTId=PRO_0000058553.
FT   REGION        1    670       Interaction with the Mediator complex and
FT                                THRA (By similarity).
FT   REGION       16    590       Interaction with ESR1 (By similarity).
FT   REGION      108    212       Interaction with the Mediator complex (By
FT                                similarity).
FT   REGION      215    390       Interaction with the Mediator complex (By
FT                                similarity).
FT   REGION      405    644       Interaction with THRA (By similarity).
FT   REGION      542    789       Interaction with VDR (By similarity).
FT   REGION      622    701       Interaction with PPARGC1A and THRA (By
FT                                similarity).
FT   REGION      637    716       Interaction with GATA1.
FT   REGION      656   1066       Interaction with ESR1 (By similarity).
FT   REGION     1251   1423       Interaction with TP53 (By similarity).
FT   MOTIF       604    608       LXXLL motif 1.
FT   MOTIF       645    649       LXXLL motif 2.
FT   COMPBIAS   1078   1484       Ser-rich.
FT   COMPBIAS   1498   1523       Lys-rich.
FT   MOD_RES      15     15       N6-acetyllysine (By similarity).
FT   MOD_RES      18     18       Phosphoserine (By similarity).
FT   MOD_RES     664    664       Phosphoserine (By similarity).
FT   MOD_RES     770    770       Phosphoserine (By similarity).
FT   MOD_RES     771    771       Phosphoserine (By similarity).
FT   MOD_RES     772    772       Phosphoserine (By similarity).
FT   MOD_RES     774    774       Phosphoserine (By similarity).
FT   MOD_RES     795    795       Phosphoserine (By similarity).
FT   MOD_RES     805    805       Phosphothreonine (By similarity).
FT   MOD_RES     953    953       Phosphoserine.
FT   MOD_RES     955    955       Phosphoserine.
FT   MOD_RES    1032   1032       Phosphothreonine; by MAPK1 or MAPK3 (By
FT                                similarity).
FT   MOD_RES    1049   1049       Phosphoserine (By similarity).
FT   MOD_RES    1051   1051       Phosphothreonine (By similarity).
FT   MOD_RES    1057   1057       Phosphothreonine (By similarity).
FT   MOD_RES    1136   1136       Phosphoserine (By similarity).
FT   MOD_RES    1157   1157       Phosphoserine (By similarity).
FT   MOD_RES    1179   1179       N6-acetyllysine (By similarity).
FT   MOD_RES    1209   1209       Phosphoserine (By similarity).
FT   MOD_RES    1217   1217       Phosphothreonine (By similarity).
FT   MOD_RES    1225   1225       Phosphoserine (By similarity).
FT   MOD_RES    1234   1234       Phosphoserine (By similarity).
FT   MOD_RES    1254   1254       Phosphoserine (By similarity).
FT   MOD_RES    1356   1356       N6-acetyllysine (By similarity).
FT   MOD_RES    1405   1405       Phosphoserine (By similarity).
FT   MOD_RES    1435   1435       Phosphoserine (By similarity).
FT   MOD_RES    1441   1441       Phosphoserine (By similarity).
FT   MOD_RES    1442   1442       Phosphothreonine (By similarity).
FT   MOD_RES    1459   1459       Phosphothreonine; by MAPK1 or MAPK3 (By
FT                                similarity).
FT   MOD_RES    1465   1465       Phosphoserine (By similarity).
FT   MOD_RES    1481   1481       Phosphoserine (By similarity).
FT   MOD_RES    1483   1483       Phosphoserine (By similarity).
FT   MOD_RES    1484   1484       Phosphoserine (By similarity).
FT   MOD_RES    1523   1523       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1     15       Missing (in isoform 4).
FT                                /FTId=VSP_051892.
FT   VAR_SEQ     548    632       YGMTTGNNPMSGTTTPTNTFPGGPITTLFNMSMSIKDRHES
FT                                VGHGEDFSKVSQNPILTSLLQITGNGGSTIGSSPTPPHHTP
FT                                PPV -> VEEKRQDKPSLGHLPPIQVCSPSCLKDGKDMKST
FT                                CTYLLLLLLLLEFMVFCFFFFFLTYSSVFGLHVKGLWTKIC
FT                                SDVQEYFSVS (in isoform 2).
FT                                /FTId=VSP_051893.
FT   VAR_SEQ     548    556       YGMTTGNNP -> SKNPELGSG (in isoform 3).
FT                                /FTId=VSP_051894.
FT   VAR_SEQ     557   1575       Missing (in isoform 3).
FT                                /FTId=VSP_051895.
FT   VAR_SEQ     633   1575       Missing (in isoform 2).
FT                                /FTId=VSP_051896.
FT   VARIANT     960    960       T -> S (in strain: ISS and 129/Ola).
FT   VARIANT    1348   1348       T -> M (in strain: ISS and 129/Ola).
FT   CONFLICT     84     84       I -> L (in Ref. 1; AAC31118).
FT   CONFLICT    198    198       A -> T (in Ref. 6; AAH21440).
FT   CONFLICT    211    211       L -> H (in Ref. 4; BAE27757).
FT   CONFLICT    303    303       F -> S (in Ref. 1; AAC31118).
FT   CONFLICT    382    389       LPDGQSLQ -> VLPNKAVS (in Ref. 4;
FT                                BAC35779).
FT   CONFLICT    948    948       E -> K (in Ref. 4; BAC33607).
FT   CONFLICT    964    964       G -> A (in Ref. 4; BAC33607).
FT   CONFLICT   1323   1323       G -> S (in Ref. 1; AAC31118).
FT   CONFLICT   1387   1387       G -> R (in Ref. 1; AAC31118).
FT   HELIX       643    649
SQ   SEQUENCE   1575 AA;  167141 MW;  C3B8121A26003A22 CRC64;
     MKAQGETEDS ERLSKMSSLL ERLHAKFNQN RPWSETIKLV RQVMEKRVVM SSGGHQHLVS
     CLETLQKALK VTSLPAMTDR LESIARQNGL GSHLSASGTE CYITSDMFYV EVQLDPAGQL
     CDVKVAHHGE NPVSCPELVQ QLREKNFEEF SKHLKGLVNL YNLPGDNKLK TKMYLALQSL
     EQDLSKMAIM YWKATNAAPL DKILHGSVGY LTPRSGGHLM NMKYYASPSD LLDDKTASPI
     ILHEKNVPRS LGMNASVTIE GTSAMYKLPI APLIMGSHPA DNKWTPSFSA VTSANSVDLP
     ACFFLKFPQP IPVSKAFVQK LQNCTGIPLF ETPPTYLPLY ELITQFELSK DPDPLPLNHN
     MRFYAALPGQ QHCYFLNKDA PLPDGQSLQG TLVSKITFQH PGRVPLILNM IRHQVAYNTL
     IGSCVKRTIL KEDSPGLLQF EVCPLSESRF SVSFQHPVND SLVCVVMDVQ DSTHVSCKLY
     KGLSDALICT DDFIAKVVQR CMSIPVTMRA IRRKAETIQA DTPALSLIAE TVEDMVKKNL
     PPASSPGYGM TTGNNPMSGT TTPTNTFPGG PITTLFNMSM SIKDRHESVG HGEDFSKVSQ
     NPILTSLLQI TGNGGSTIGS SPTPPHHTPP PVSSMAGNTK NHPMLMNLLK DNPAQDFSTL
     YGSSPLERQN SSSGSPRMEM CSGSNKAKKK KSSRVPPDKP KHQTEDDFQR ELFSMDVDSQ
     NPMFDVSMTA DALDTPHITP APSQCSTPPA TYPQPVSHPQ PSIQRMVRLS SSDSIGPDVT
     DILSDIAEEA SKLPSTSDDC PPIGTPVRDS SSSGHSQSAL FDSDVFQTNN NENPYTDPAD
     LIADAAGSPN SDSPTNHFFP DGVDFNPDLL NSQSQSGFGE EYFDESSQSG DNDDFKGFAS
     QALNTLGMPM LGGDNGEPKF KGSSQADTVD FSIISVAGKA LGAADLMEHH SGSQSPLLTT
     GELGKEKTQK RVKEGNGTGA SSGSGPGSDS KPGKRSRTPS NDGKSKDKPP KRKKADTEGK
     SPSHSSSNRP FTPPTSTGGS KSPGSSGRSQ TPPGVATPPI PKITIQIPKG TVMVGKPSSH
     SQYTSSGSVS SSGSKSHHSH SSSSSSLASA STSGKVKSSK SEGSSSSKLS GSMYASQGSS
     GSSQSKNSSQ TGGKPGSSPI TKHGLSSGSS STKMKPQGKP SSLMNPSISK PNISPSHSRP
     PGGSDKLASP MKPVPGTPPS SKAKSPISSG SSGSHVSGTS SSSGMKSSSG SASSGSVSQK
     TPPASNSCTP SSSSFSSSGS SMSSSQNQHG SSKGKSPSRN KKPSLTAVID KLKHGVVTSG
     PGGEDPIDSQ MGASTNSSNH PMSSKHNTSG GEFQSKREKS DKDKSKVSAS GGSVDSSKKT
     SESKNVGSTG VAKIIISKHD GGSPSIKAKV TLQKPGESGG DGLRPQIASS KNYGSPLISG
     STPKHERGSP SHSKSPAYTP QNVDSESESG SSIAERSYQN SPSSEDGIRP LPEYSTEKHK
     KHKKEKKKVR DKDRDKKKSH SMKPENWSKS PISSDPTASV TNNPILSADR PSRLSPDFMI
     GEEDDDLMDV ALIGN
//
ID   TALDO_MOUSE             Reviewed;         337 AA.
AC   Q93092; P70358; P70703; Q52KM4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 2.
DT   08-MAR-2011, entry version 101.
DE   RecName: Full=Transaldolase;
DE            EC=2.2.1.2;
GN   Name=Taldo1; Synonyms=Tal, Taldo;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=98192510; PubMed=9524206; DOI=10.1016/S0378-1119(97)00639-2;
RA   Kusuda J., Hirai M., Toyoda A., Tanuma R., Nomura-Kitabayashi A.,
RA   Hashimoto K.;
RT   "Cloning and chromosomal localization of a paralog and a mouse homolog
RT   of the human transaldolase gene.";
RL   Gene 209:13-21(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N, and FVB/N-3; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 87-97 AND 259-265, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 13-337.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Crystal structure of mouse transaldolase.";
RL   Submitted (DEC-2005) to the PDB data bank.
CC   -!- FUNCTION: Transaldolase is important for the balance of
CC       metabolites in the pentose-phosphate pathway (By similarity).
CC   -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde
CC       3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate.
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-
CC       ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative
CC       stage): step 2/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U67611; AAB83955.1; -; mRNA.
DR   EMBL; U63158; AAB08722.1; ALT_SEQ; mRNA.
DR   EMBL; U63159; AAB08723.1; ALT_SEQ; mRNA.
DR   EMBL; BC004754; AAH04754.1; -; mRNA.
DR   EMBL; BC094277; AAH94277.1; -; mRNA.
DR   IPI; IPI00124692; -.
DR   RefSeq; NP_035658.1; NM_011528.4.
DR   UniGene; Mm.29182; -.
DR   PDB; 2CWN; X-ray; 2.10 A; A/B=13-337.
DR   PDB; 2E1D; X-ray; 2.00 A; A/B=11-334.
DR   PDBsum; 2CWN; -.
DR   PDBsum; 2E1D; -.
DR   ProteinModelPortal; Q93092; -.
DR   SMR; Q93092; 11-331.
DR   STRING; Q93092; -.
DR   PhosphoSite; Q93092; -.
DR   REPRODUCTION-2DPAGE; IPI00124692; -.
DR   REPRODUCTION-2DPAGE; Q93092; -.
DR   PRIDE; Q93092; -.
DR   Ensembl; ENSMUST00000026576; ENSMUSP00000026576; ENSMUSG00000025503.
DR   GeneID; 21351; -.
DR   KEGG; mmu:21351; -.
DR   UCSC; uc009kkv.1; mouse.
DR   CTD; 21351; -.
DR   MGI; MGI:1274789; Taldo1.
DR   eggNOG; roNOG07008; -.
DR   GeneTree; ENSGT00390000017361; -.
DR   HOGENOM; HBG286747; -.
DR   HOVERGEN; HBG054014; -.
DR   InParanoid; Q93092; -.
DR   OMA; DTGDFHA; -.
DR   OrthoDB; EOG4GQQ5B; -.
DR   PhylomeDB; Q93092; -.
DR   BRENDA; 2.2.1.2; 244.
DR   NextBio; 300544; -.
DR   ArrayExpress; Q93092; -.
DR   Bgee; Q93092; -.
DR   CleanEx; MM_TALDO1; -.
DR   Genevestigator; Q93092; -.
DR   GermOnline; ENSMUSG00000025503; Mus musculus.
DR   GO; GO:0004801; F:sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity; IEA:EC.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001585; Transaldolase.
DR   InterPro; IPR004730; Transaldolase_1.
DR   InterPro; IPR018225; Transaldolase_AS.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   PANTHER; PTHR10683; Transaldolase; 1.
DR   Pfam; PF00923; Transaldolase; 1.
DR   TIGRFAMs; TIGR00874; talAB; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Pentose shunt; Phosphoprotein; Transferase.
FT   CHAIN         1    337       Transaldolase.
FT                                /FTId=PRO_0000173565.
FT   ACT_SITE    142    142       By similarity.
FT   MOD_RES       4      4       Phosphoserine (By similarity).
FT   MOD_RES     219    219       N6-acetyllysine (By similarity).
FT   MOD_RES     237    237       Phosphoserine (By similarity).
FT   MOD_RES     269    269       N6-acetyllysine (By similarity).
FT   MOD_RES     286    286       N6-acetyllysine (By similarity).
FT   MOD_RES     321    321       N6-acetyllysine (By similarity).
FT   HELIX        14     18
FT   TURN         19     21
FT   STRAND       22     27
FT   HELIX        31     33
FT   HELIX        35     37
FT   STRAND       40     43
FT   HELIX        46     53
FT   HELIX        56     58
FT   HELIX        59     72
FT   HELIX        76     96
FT   STRAND      103    106
FT   HELIX       109    111
FT   HELIX       115    131
FT   HELIX       136    138
FT   STRAND      139    144
FT   HELIX       147    160
FT   STRAND      164    169
FT   HELIX       172    181
FT   STRAND      184    190
FT   HELIX       191    200
FT   HELIX       208    210
FT   HELIX       212    226
FT   STRAND      232    236
FT   HELIX       241    245
FT   TURN        246    249
FT   STRAND      250    255
FT   HELIX       257    265
FT   HELIX       276    279
FT   HELIX       291    299
FT   HELIX       302    330
SQ   SEQUENCE   337 AA;  37387 MW;  B0AD351FD778367F CRC64;
     MSGSPVKRQR MESALDQLKQ FTTVVADTGD FNAIDEYKPQ DATTNPSLIL AAAQMPAYQE
     LVEEAIAYGK KLGGPQEEQI KNAIDKLFVL FGAEILKKIP GRVSTEVDAR LSFDKDAMVA
     RARRLIELYK EAGVGKDRIL IKLSSTWEGI QAGKELEEQH GIHCNMTLLF SFAQAVACAE
     AGVTLISPFV GRILDWHVAN TDKKSYEPQE DPGVKSVTKI YNYYKKFGYK TIVMGASFRN
     TGEIKALAGC DFLTISPKLL GELLKDNSKL APALSVKAAQ TSDSEKIHLD EKAFRWLHNE
     DQMAVEKLSD GIRKFAADAI KLERMLTERM FSAENGK
//
ID   CAC1D_MOUSE             Reviewed;        2179 AA.
AC   Q99246; Q7TSD2; Q8R2I9; Q8R2J0;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=Voltage-dependent L-type calcium channel subunit alpha-1D;
DE   AltName: Full=Calcium channel, L type, alpha-1 polypeptide isoform 2;
DE   AltName: Full=Voltage-gated calcium channel subunit alpha Cav1.3;
GN   Name=Cacna1d; Synonyms=Cach3, Cacn4, Cacnl1a2, Cchl1a2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), INDUCTION, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6; TISSUE=Heart;
RX   MEDLINE=22917442; PubMed=12900400; DOI=10.1074/jbc.M307598200;
RA   Xu M., Welling A., Paparisto S., Hofmann F., Klugbauer N.;
RT   "Enhanced expression of L-type Cav1.3 calcium channels in murine
RT   embryonic hearts from Cav1.2-deficient mice.";
RL   J. Biol. Chem. 278:40837-40841(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Brain;
RA   Okamoto T., Kobayashi T., Hino O.;
RT   "Cloning of the L-type Ca2+ channel alpha1D-subunit from mouse brain
RT   and characterization of its expression in the liver.";
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1168-1463 (ISOFORMS 2/3).
RC   STRAIN=ICR; TISSUE=Ovary;
RX   MEDLINE=91056091; PubMed=2173707;
RA   Perez-Reyes E., Wei X., Castellano A., Birnbaumer L.;
RT   "Molecular diversity of L-type calcium channels. Evidence for
RT   alternative splicing of the transcripts of three non-allelic genes.";
RL   J. Biol. Chem. 265:20430-20436(1990).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=10929716; DOI=10.1016/S0092-8674(00)00013-1;
RA   Platzer J., Engel J., Schrott-Fischer A., Stephan K., Bova S.,
RA   Chen H., Zheng H., Striessnig J.;
RT   "Congenital deafness and sinoatrial node dysfunction in mice lacking
RT   class D L-type Ca2+ channels.";
RL   Cell 102:89-97(2000).
RN   [5]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=11581302; DOI=10.1172/JCI13310;
RA   Namkung Y., Skrypnyk N., Jeong M.J., Lee T., Lee M.S., Kim H.L.,
RA   Chin H., Suh P.G., Kim S.S., Shin H.S.;
RT   "Requirement for the L-type Ca(2+) channel alpha(1D) subunit in
RT   postnatal pancreatic beta cell generation.";
RL   J. Clin. Invest. 108:1015-1022(2001).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=12700358; DOI=10.1073/pnas.0935295100;
RA   Mangoni M.E., Couette B., Bourinet E., Platzer J., Reimer D.,
RA   Striessnig J., Nargeot J.;
RT   "Functional role of L-type Cav1.3 Ca2+ channels in cardiac pacemaker
RT   activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5543-5548(2003).
RN   [7]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=16354915; DOI=10.1523/JNEUROSCI.3411-05.2005;
RA   Brandt A., Khimich D., Moser T.;
RT   "Few CaV1.3 channels regulate the exocytosis of a synaptic vesicle at
RT   the hair cell ribbon synapse.";
RL   J. Neurosci. 25:11577-11585(2005).
RN   [8]
RP   INTERACTION WITH CABP1 AND CABP4.
RX   PubMed=17947313; DOI=10.1113/jphysiol.2007.142307;
RA   Cui G., Meyer A.C., Calin-Jageman I., Neef J., Haeseleer F., Moser T.,
RA   Lee A.;
RT   "Ca2+-binding proteins tune Ca2+-feedback to Cav1.3 channels in mouse
RT   auditory hair cells.";
RL   J. Physiol. (Lond.) 585:791-803(2007).
CC   -!- FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the
CC       entry of calcium ions into excitable cells and are also involved
CC       in a variety of calcium-dependent processes, including muscle
CC       contraction, hormone or neurotransmitter release, gene expression,
CC       cell motility, cell division and cell death. The isoform alpha-1D
CC       gives rise to L-type calcium currents. Long-lasting (L-type)
CC       calcium channels belong to the 'high-voltage activated' (HVA)
CC       group. They are blocked by dihydropyridines (DHP),
CC       phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA
CC       (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-
CC       GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA).
CC   -!- SUBUNIT: Voltage-dependent calcium channels are multisubunit
CC       complexes, consisting of alpha-1, alpha-2, beta and delta subunits
CC       in a 1:1:1:1 ratio. The channel activity is directed by the pore-
CC       forming and voltage-sensitive alpha-1 subunit. In many cases, this
CC       subunit is sufficient to generate voltage-sensitive calcium
CC       channel activity. The auxiliary subunits beta and alpha-2/delta
CC       linked by a disulfide bridge regulate the channel activity.
CC       Interacts (via IQ domain) with CABP1 and CABP4 in a calcium
CC       independent manner. Interacts with RIMBP2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q99246-2; Sequence=Displayed;
CC       Name=2; Synonyms=Cav1.3(1a);
CC         IsoId=Q99246-3; Sequence=VSP_027091, VSP_027092;
CC       Name=3; Synonyms=Cav1.3(1b);
CC         IsoId=Q99246-4; Sequence=VSP_027090, VSP_027091, VSP_027092;
CC   -!- TISSUE SPECIFICITY: Expressed in the inner hair cells (IHC) of the
CC       cochlea.
CC   -!- DEVELOPMENTAL STAGE: Isoform 2 and isoform 3 are expressed in
CC       heart at 12.5 dpc (at protein level). Expressed in the heart at
CC       9.5, 12.5 and 15.5 dpc. Isoform 2 and isoform 3 are expressed in
CC       heart at 9.5 and 12.5 dpc.
CC   -!- INDUCTION: Up-regulated in CACNA1C knockout mice.
CC   -!- DOMAIN: Each of the four internal repeats contains five
CC       hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one
CC       positively charged transmembrane segment (S4). S4 segments
CC       probably represent the voltage-sensor and are characterized by a
CC       series of positively charged amino acids at every third position.
CC   -!- DISRUPTION PHENOTYPE: deafness, bradycardia and diabetic traits.
CC   -!- SIMILARITY: Belongs to the calcium channel alpha-1 subunit
CC       (TC 1.A.1.11) family. CACNA1D subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ437291; CAD26883.1; -; mRNA.
DR   EMBL; AJ437292; CAD26884.1; -; mRNA.
DR   EMBL; AB086123; BAC77259.1; -; mRNA.
DR   EMBL; M57975; AAA63292.1; -; mRNA.
DR   IPI; IPI00230232; -.
DR   IPI; IPI00380726; -.
DR   IPI; IPI00855172; -.
DR   RefSeq; NP_001077085.1; NM_001083616.1.
DR   RefSeq; NP_083257.2; NM_028981.2.
DR   UniGene; Mm.9772; -.
DR   ProteinModelPortal; Q99246; -.
DR   SMR; Q99246; 160-212, 1568-1648.
DR   STRING; Q99246; -.
DR   PhosphoSite; Q99246; -.
DR   PRIDE; Q99246; -.
DR   Ensembl; ENSMUST00000057695; ENSMUSP00000057745; ENSMUSG00000015968.
DR   Ensembl; ENSMUST00000112249; ENSMUSP00000107868; ENSMUSG00000015968.
DR   Ensembl; ENSMUST00000112250; ENSMUSP00000107869; ENSMUSG00000015968.
DR   GeneID; 12289; -.
DR   KEGG; mmu:12289; -.
DR   CTD; 12289; -.
DR   MGI; MGI:88293; Cacna1d.
DR   eggNOG; roNOG09300; -.
DR   HOVERGEN; HBG050763; -.
DR   OrthoDB; EOG47D9F6; -.
DR   NextBio; 280770; -.
DR   ArrayExpress; Q99246; -.
DR   Bgee; Q99246; -.
DR   Genevestigator; Q99246; -.
DR   GermOnline; ENSMUSG00000015968; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; IC:MGI.
DR   GO; GO:0005891; C:voltage-gated calcium channel complex; TAS:MGI.
DR   GO; GO:0008331; F:high voltage-gated calcium channel activity; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007188; P:G-protein signaling, coupled to cAMP nucleotide second messenger; IMP:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR005452; LVDCC_a1dsu.
DR   InterPro; IPR014873; VDCC_a1su_IQ.
DR   InterPro; IPR005446; VDCC_L_a1su.
DR   InterPro; IPR002077; VDCCAlpha1.
DR   Pfam; PF08763; Ca_chan_IQ; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   PRINTS; PR00167; CACHANNEL.
DR   PRINTS; PR01630; LVDCCALPHA1.
DR   PRINTS; PR01636; LVDCCALPHA1D.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Calcium channel; Calcium transport;
KW   Coiled coil; Disulfide bond; Ion transport; Ionic channel; Membrane;
KW   Phosphoprotein; Repeat; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN         1   2179       Voltage-dependent L-type calcium channel
FT                                subunit alpha-1D.
FT                                /FTId=PRO_0000053935.
FT   TOPO_DOM      1    126       Cytoplasmic (Potential).
FT   TRANSMEM    127    145       Helical; Name=S1 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    146    163       Extracellular (Potential).
FT   TRANSMEM    164    183       Helical; Name=S2 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    184    195       Cytoplasmic (Potential).
FT   TRANSMEM    196    214       Helical; Name=S3 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    215    235       Extracellular (Potential).
FT   TRANSMEM    236    254       Helical; Name=S4 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    255    273       Cytoplasmic (Potential).
FT   TRANSMEM    274    293       Helical; Name=S5 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    294    381       Extracellular (Potential).
FT   TRANSMEM    382    406       Helical; Name=S6 of repeat I;
FT                                (Potential).
FT   TOPO_DOM    407    543       Cytoplasmic (Potential).
FT   TRANSMEM    544    563       Helical; Name=S1 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    564    578       Extracellular (Potential).
FT   TRANSMEM    579    597       Helical; Name=S2 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    598    605       Cytoplasmic (Potential).
FT   TRANSMEM    606    624       Helical; Name=S3 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    625    634       Extracellular (Potential).
FT   TRANSMEM    635    653       Helical; Name=S4 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    654    672       Cytoplasmic (Potential).
FT   TRANSMEM    673    693       Helical; Name=S5 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    694    747       Extracellular (Potential).
FT   TRANSMEM    748    772       Helical; Name=S6 of repeat II;
FT                                (Potential).
FT   TOPO_DOM    773    906       Cytoplasmic (Potential).
FT   TRANSMEM    907    925       Helical; Name=S1 of repeat III;
FT                                (Potential).
FT   TOPO_DOM    926    941       Extracellular (Potential).
FT   TRANSMEM    942    961       Helical; Name=S2 of repeat III;
FT                                (Potential).
FT   TOPO_DOM    962    973       Cytoplasmic (Potential).
FT   TRANSMEM    974    992       Helical; Name=S3 of repeat III;
FT                                (Potential).
FT   TOPO_DOM    993    998       Extracellular (Potential).
FT   TRANSMEM    999   1018       Helical; Name=S4 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1019   1037       Cytoplasmic (Potential).
FT   TRANSMEM   1038   1057       Helical; Name=S5 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1058   1147       Extracellular (Potential).
FT   TRANSMEM   1148   1168       Helical; Name=S6 of repeat III;
FT                                (Potential).
FT   TOPO_DOM   1169   1225       Cytoplasmic (Potential).
FT   TRANSMEM   1226   1244       Helical; Name=S1 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1245   1259       Extracellular (Potential).
FT   TRANSMEM   1260   1279       Helical; Name=S2 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1280   1286       Cytoplasmic (Potential).
FT   TRANSMEM   1287   1308       Helical; Name=S3 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1309   1333       Extracellular (Potential).
FT   TRANSMEM   1334   1353       Helical; Name=S4 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1354   1372       Cytoplasmic (Potential).
FT   TRANSMEM   1373   1392       Helical; Name=S5 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1393   1459       Extracellular (Potential).
FT   TRANSMEM   1460   1484       Helical; Name=S6 of repeat IV;
FT                                (Potential).
FT   TOPO_DOM   1485   2179       Cytoplasmic (Potential).
FT   REPEAT      113    409       I.
FT   REPEAT      529    775       II.
FT   REPEAT      893   1175       III.
FT   REPEAT     1212   1487       IV.
FT   CA_BIND    1513   1524       By similarity.
FT   REGION      429    446       Binding to the beta subunit (By
FT                                similarity).
FT   REGION     1095   1185       Dihydropyridine binding (By similarity).
FT   REGION     1440   1506       Dihydropyridine binding (By similarity).
FT   REGION     1452   1495       Phenylalkylamine binding (By similarity).
FT   COILED      771    810       Potential.
FT   COMPBIAS      1      7       Poly-Met.
FT   COMPBIAS    673    679       Poly-Leu.
FT   COMPBIAS    847    858       Poly-Glu.
FT   SITE        364    364       Calcium ion selectivity and permeability
FT                                (By similarity).
FT   SITE        725    725       Calcium ion selectivity and permeability
FT                                (By similarity).
FT   SITE       1121   1121       Calcium ion selectivity and permeability
FT                                (By similarity).
FT   SITE       1426   1426       Calcium ion selectivity and permeability
FT                                (By similarity).
FT   MOD_RES    1495   1495       Phosphoserine; by PKA (By similarity).
FT   MOD_RES    1923   1923       Phosphoserine (By similarity).
FT   VAR_SEQ       1     22       MMMMMMMKKMQHQRQHQEDHAN -> MNLPTFSSDLILIKS
FT                                VLSQETDARYKGRVVSAVESTEDFSQAFA (in isoform
FT                                3).
FT                                /FTId=VSP_027090.
FT   VAR_SEQ     493    513       WCWWKRRGAAKTGPSGCRRWG -> C (in isoform 2
FT                                and isoform 3).
FT                                /FTId=VSP_027091.
FT   VAR_SEQ    1311   1325       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_027092.
FT   CONFLICT    445    445       V -> A (in Ref. 2; BAC77259).
FT   CONFLICT    868    868       T -> I (in Ref. 2; BAC77259).
FT   CONFLICT   1871   1871       G -> E (in Ref. 2; BAC77259).
FT   CONFLICT   2043   2043       Y -> S (in Ref. 2; BAC77259).
SQ   SEQUENCE   2179 AA;  247005 MW;  573A8D15211611EA CRC64;
     MMMMMMMKKM QHQRQHQEDH ANEANYARGT RLPISGEGPT SQPNSSKQTV LSWQAAIDAA
     RQAKAAQTMS TSAPPPVGSL SQRKRQQYAK SKKQGNSSNS RPARALFCLS LNNPIRRACI
     SIVEWKPFDI FILLAIFANC VALAIYIPFP EDDSNSTNHN LEKVEYAFLI IFTVETFLKI
     IAYGLLLHPN AYVRNGWNLL DFVIVIVGLF SVILEQLTKE TEGGNHSSGK SGGFDVKALR
     AFRVLRPLRL VSGVPSLQVV LNSIIKAMVP LLHIALLVLF VIIIYAIIGL ELFIGKMHKT
     CFFADSDIVA EEDPAPCAFS GNGRQCTANG TECRSGWVGP NGGITNFDNF AFAMLTVFQC
     ITMEGWTDVL YWVNDAIGWE WPWVYFVSLI ILGSFFVLNL VLGVLSGEFS KEREKAKARG
     DFQKLREKQQ LEEDLKGYLD WITQVEDIDP ENEEEGGEEG KRNTSMPTSE TESVNTENVS
     GEGETQGCCG TLWCWWKRRG AAKTGPSGCR RWGQAISKSK LSRRWRRWNR FNRRRCRAAV
     KSVTFYWLVI VLVFLNTLTI SSEHYNQPDW LTQIQDIANK VLLALFTCEM LVKMYSLGLQ
     AYFVSLFNRF DCFVVCGGIT ETILVELELM SPLGVSVFRC VRLLRIFKVT RHWTSLSNLV
     ASLLNSMKSI ASLLLLLFLF IIIFSLLGMQ LFGGKFNFDE TQTKRSTFDN FPQALLTVFQ
     ILTGEDWNAV MYDGIMAYGG PSSSGMIVCI YFIILFICGN YILLNVFLAI AVDNLADAES
     LNTAQKEEAE EKERKKIARK ESLENKKNNK PEVNQIANSD NKVTIDDYQE DAEDKDPYPP
     CDVPVGEEEE EEEEDEPEVP AGPRPRRTSE LNMKEKIAPI PEGSAFFILS KTNPIRVGCH
     KLINHHIFTN LILVFIMLSS AALAAEDPIR SHSFRNTILG YFDYAFTAIF TVEILLKMTT
     FGAFLHKGAF CRNYFNLLDM LVVGVSLVSF GIQSSAISVV KILRVLRVLR PLRAINRAKG
     LKHVVQCVFV AIRTIGNIMI VTTLLQFMFA CIGVQLFKGK FYRCTDEAKS NPEECRGLFI
     LYKDGDVDSP VVRERIWQNS DFNFDNVLSA MMALFTVSTF EGWPALLYKA IDSNGENVGP
     VYNYRVEISI FFIIYIIIVA FFMMNIFVGF VIVTFQEQGE KEYKNCELDK NQRQCVEYAL
     KARPLRRYIP KNPYQYKFWY VVNSSPFEYM MFVLIMLNTL CLAMQHYEQS KMFNDAMDIL
     NMVFTGVFTV EMVLKVIAFK PKGYFSDAWN TFDSLIVIGS IIDVALSEAD PSESETIPLP
     TATPGNSEES NRISITFFRL FRVMRLVKLL SRGEGIRTLL WTFIKSFQAL PYVALLIAML
     FFIYAVIGMQ MFGKVAMRDN NQINRNNNFQ TFPQAVLLLF RCATGEAWQE IMLACLPGKL
     CDPDSDYNPG EEYTCGSNFA IVYFISFYML CAFLIINLFV AVIMDNFDYL TRDWSILGPH
     HLDEFKRIWS EYDPEAKGRI KHLDVVTLLR RIQPPLGFGK LCPHRVACKR LVAMNMPLNS
     DGTVMFNATL FALVRTALKI KTEGNLEQAN EELRAVIKKI WKKTSMKLLD QVVPPAGDDE
     VTVGKFYATF LIQDYFRKFK KRKEQGLVGK YPAKNTTIAL QAGLRTLHDI GPEIRRAISC
     DLQDDEPEDS KPEEEDVFKR NGALLGNHVN HVNSDRRDSL QQTNTTHRPL HVQRPSMPPA
     SDTEKPLFPP AGNSGCHNHH NHNSIGKQAP TSTNANLNNA NMSKAAHGKP PSIGNLEHVS
     ENGHYSCKHD RELQRRSSIK RTRYYETYIR SESGDEQFPT ICREDPEIHG YFRDPRCLGE
     QEYFSSEECC GDDSSPTWSR QNYNYYNRYP GSSMDFERPR GYHHPQGFLE DDDSPTGYDS
     RRSPRRRLLP PTPPSHRRSS FNFECLRRQS SQDDVLPSPA LPHRAALPLH LMQQQIMAVA
     GLDSSKAQKY SPSHSTRSWA TPPATPPYRD WSPCYTPLIQ VDRSESMDQV NGSLPSLHRS
     SWYTDEPDIS YRTFTPASLT VPSSFRNKNS DKQRSADSLV EAVLISEGLG RYARDPKFVS
     ATKHEIADAC DLTIDEMESA ASTLLNGSVC PRANGDMGPI SHRQDYELQD FGPGYSDEEP
     DPGREEEDLA DEMICITTL
//
ID   MEP50_MOUSE             Reviewed;         342 AA.
AC   Q99J09; Q3TFJ1; Q8BSH8; Q9CZY5;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Methylosome protein 50;
DE            Short=MEP-50;
DE   AltName: Full=WD repeat-containing protein 77;
GN   Name=Wdr77; Synonyms=Mep50;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Amnion, Embryo, Head, Liver, and Mesonephros;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH SUZ12.
RX   PubMed=16712789; DOI=10.1016/j.bbrc.2006.05.014;
RA   Furuno K., Masatsugu T., Sonoda M., Sasazuki T., Yamamoto K.;
RT   "Association of Polycomb group SUZ12 with WD-repeat protein MEP50 that
RT   binds to histone H2A selectively in vitro.";
RL   Biochem. Biophys. Res. Commun. 345:1051-1058(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   FUNCTION IN METHYLATION OF PIWI PROTEINS.
RX   PubMed=19584108; DOI=10.1101/gad.1814809;
RA   Vagin V.V., Wohlschlegel J., Qu J., Jonsson Z., Huang X., Chuma S.,
RA   Girard A., Sachidanandam R., Hannon G.J., Aravin A.A.;
RT   "Proteomic analysis of murine Piwi proteins reveals a role for
RT   arginine methylation in specifying interaction with Tudor family
RT   members.";
RL   Genes Dev. 23:1749-1762(2009).
CC   -!- FUNCTION: Non-catalytic component of the 20S PRMT5-containing
CC       methyltransferase complex, which modifies specific arginines to
CC       dimethylarginines in several spliceosomal Sm proteins. This
CC       modification targets Sm proteins to the survival of motor neurons
CC       (SMN) complex for assembly into small nuclear ribonucleoprotein
CC       core particles. Might play a role in transcription regulation (By
CC       similarity). The 20S PRMT5-containing methyltransferase complex
CC       also methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4),
CC       methylation of Piwi proteins being required for the interaction
CC       with Tudor domain-containing proteins and subsequent localization
CC       to the meiotic nuage.
CC   -!- SUBUNIT: Component of the methylosome, a 20S complex containing at
CC       least PRMT5, CLNS1A and WDR77. Directly interacts with PRMT5, as
CC       well as with several Sm proteins, including SNRPB and SNRPD2 and,
CC       more weakly, SNRPD3 and SNRPE. Interacts with SUZ12 and histone
CC       H2A/HIST2H2AC, but not with histones H2B, H3 nor H4. Interacts
CC       with CTDP1 and LSM11. Interacts with APEX1, AR and NKX3-1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity).
CC   -!- SIMILARITY: Contains 5 WD repeats.
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DR   EMBL; AK012014; BAB27975.1; -; mRNA.
DR   EMBL; AK032897; BAC28076.1; -; mRNA.
DR   EMBL; AK048488; BAC33350.1; -; mRNA.
DR   EMBL; AK050391; BAC34232.1; -; mRNA.
DR   EMBL; AK163839; BAE37512.1; -; mRNA.
DR   EMBL; AK169128; BAE40907.1; -; mRNA.
DR   EMBL; BC005755; AAH05755.1; -; mRNA.
DR   IPI; IPI00114819; -.
DR   RefSeq; NP_081708.1; NM_027432.3.
DR   UniGene; Mm.5110; -.
DR   ProteinModelPortal; Q99J09; -.
DR   SMR; Q99J09; 13-329.
DR   STRING; Q99J09; -.
DR   PhosphoSite; Q99J09; -.
DR   PRIDE; Q99J09; -.
DR   Ensembl; ENSMUST00000010278; ENSMUSP00000010278; ENSMUSG00000000561.
DR   GeneID; 70465; -.
DR   KEGG; mmu:70465; -.
DR   UCSC; uc008qvo.1; mouse.
DR   CTD; 70465; -.
DR   MGI; MGI:1917715; Wdr77.
DR   eggNOG; roNOG14887; -.
DR   GeneTree; ENSGT00390000010711; -.
DR   HOGENOM; HBG402957; -.
DR   HOVERGEN; HBG052458; -.
DR   InParanoid; Q99J09; -.
DR   OMA; MRKETPP; -.
DR   OrthoDB; EOG4MPHQT; -.
DR   PhylomeDB; Q99J09; -.
DR   NextBio; 331685; -.
DR   ArrayExpress; Q99J09; -.
DR   Bgee; Q99J09; -.
DR   CleanEx; MM_WDR77; -.
DR   Genevestigator; Q99J09; -.
DR   GermOnline; ENSMUSG00000000561; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; IMP:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IGI:MGI.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:MGI.
DR   GO; GO:0060528; P:secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development; IMP:MGI.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 4.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Phosphoprotein; Repeat; WD repeat.
FT   CHAIN         1    342       Methylosome protein 50.
FT                                /FTId=PRO_0000051075.
FT   REPEAT       78    116       WD 1.
FT   REPEAT      123    162       WD 2.
FT   REPEAT      165    205       WD 3.
FT   REPEAT      209    250       WD 4.
FT   REPEAT      253    293       WD 5.
FT   MOD_RES       5      5       Phosphothreonine.
FT   CONFLICT    267    285       SVPLLTSLSEDCSLAVLDS -> RCCVSPGTWKGWVGTVVK
FT                                E (in Ref. 2; AAH05755).
FT   CONFLICT    286    342       Missing (in Ref. 2; AAH05755).
SQ   SEQUENCE   342 AA;  36943 MW;  E9C52BC4D6E5AC36 CRC64;
     MRKDTPPPLV PPAAREWNLP PNAPACMERQ LEAARYRSDG SLLLGVSSLS GRCWVGSLWF
     FKDPSAAPNE GFCSAGVQTE AGVADLTWVG DKGILVASDS GAVELWELDE NETLIVSKFC
     KYEHDDIVST VTVLSSGTQA VSGSKDCCIK IWDLAQQVSL NSYRAHAGQV TCVAASPHKD
     SVFLSCSEDS RILLWDTRCP KPASQMACNA SGYLPTALAW HPQQSEVFVF GDENGSVSLV
     DTKNASCTLS SAVHSQGVTR LVFSPHSVPL LTSLSEDCSL AVLDSSLSEV FRSRAHRDFV
     RDATWSPLNH SLLTTVGWDH QVIHHVVPLE PLPNPGPDSV VE
//
ID   MCLN1_MOUSE             Reviewed;         580 AA.
AC   Q99J21;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Mucolipin-1;
DE   AltName: Full=Mucolipidin;
GN   Name=Mcoln1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX   PubMed=11897010;
RA   Falardeau J.L., Kennedy J.C., Acierno J.S. Jr., Sun M., Stahl S.,
RA   Goldin E., Slaugenhaupt S.A.;
RT   "Cloning and characterization of the mouse Mcoln1 gene reveals an
RT   alternatively spliced transcript not seen in humans.";
RL   BMC Genomics 3:3-3(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Diencephalon, Extraembryonic tissue, Placenta, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-34, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-33 AND SER-547, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Cation channel probably playing a role in the endocytic
CC       pathway and in the control of membrane trafficking of proteins and
CC       lipids. Could play a major role in Ca(2+) transport regulating
CC       lysosomal exocytosis (By similarity).
CC   -!- ENZYME REGULATION: Channel function is transiently modulated by
CC       changes in Ca(2+), and inhibited by a reduction of pH; pH changes
CC       modify the aggregation state of unitary channels (By similarity).
CC   -!- SUBUNIT: Forms multimeric complexes (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity). Late endosome membrane; Multi-pass membrane
CC       protein (By similarity). Lysosome membrane; Multi-pass membrane
CC       protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99J21-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99J21-2; Sequence=VSP_010821;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with the highest expression
CC       in brain, liver and kidney.
CC   -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
CC       Polycystin subfamily. MCOLN1 sub-subfamily.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF302009; AAL58667.1; -; mRNA.
DR   EMBL; AK028385; BAC25922.1; -; mRNA.
DR   EMBL; AK034471; BAC28719.1; -; mRNA.
DR   EMBL; AK049606; BAC33838.1; -; mRNA.
DR   EMBL; BC005651; AAH05651.1; -; mRNA.
DR   IPI; IPI00114839; -.
DR   IPI; IPI00453501; -.
DR   RefSeq; NP_444407.1; NM_053177.1.
DR   UniGene; Mm.8356; -.
DR   ProteinModelPortal; Q99J21; -.
DR   STRING; Q99J21; -.
DR   PhosphoSite; Q99J21; -.
DR   PRIDE; Q99J21; -.
DR   Ensembl; ENSMUST00000004683; ENSMUSP00000004683; ENSMUSG00000004567.
DR   Ensembl; ENSMUST00000111076; ENSMUSP00000106705; ENSMUSG00000004567.
DR   GeneID; 94178; -.
DR   KEGG; mmu:94178; -.
DR   UCSC; uc009krq.1; mouse.
DR   CTD; 94178; -.
DR   MGI; MGI:1890498; Mcoln1.
DR   eggNOG; roNOG13913; -.
DR   GeneTree; ENSGT00390000017126; -.
DR   HOVERGEN; HBG052430; -.
DR   OMA; FKLMLQV; -.
DR   OrthoDB; EOG4V9TQN; -.
DR   NextBio; 352125; -.
DR   ArrayExpress; Q99J21; -.
DR   Bgee; Q99J21; -.
DR   CleanEx; MM_MCOLN1; -.
DR   Genevestigator; Q99J21; -.
DR   GermOnline; ENSMUSG00000004567; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0006816; P:calcium ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR013122; PKD1_2_channel.
DR   Pfam; PF08016; PKD_channel; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Calcium transport; Cell membrane;
KW   Endosome; Ion transport; Ionic channel; Lysosome; Membrane;
KW   Phosphoprotein; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    580       Mucolipin-1.
FT                                /FTId=PRO_0000215364.
FT   TRANSMEM     73     93       Helical; (Potential).
FT   TRANSMEM    297    317       Helical; (Potential).
FT   TRANSMEM    350    370       Helical; (Potential).
FT   TRANSMEM    388    408       Helical; (Potential).
FT   TRANSMEM    428    448       Helical; (Potential).
FT   TRANSMEM    497    517       Helical; (Potential).
FT   MOD_RES      10     10       Phosphoserine.
FT   MOD_RES      33     33       Phosphothreonine.
FT   MOD_RES      34     34       Phosphothreonine.
FT   MOD_RES     547    547       Phosphoserine.
FT   VAR_SEQ     526    580       HPGGTGTEKSELQAYIEQCQDSPTSGKFRRGSGSACSLFCC
FT                                CGRDSPEDHSLLVN -> RTNHRNWFSSFTVWIIDLNTSYQ
FT                                LCSKCLYLPHHLTGFLPLSYHLLLKTIYLFRGERRLCTAQC
FT                                VWKLETTCGNQLSSSTMWSHQV (in isoform 2).
FT                                /FTId=VSP_010821.
SQ   SEQUENCE   580 AA;  65506 MW;  F64D2E6C5D4C041C CRC64;
     MATPAGRRAS ETERLLTPNP GYGTQVGTSP APTTPTEEED LRRRLKYFFM SPCDKFRAKG
     RKPCKLMLQV VKILVVTVQL ILFGLSNQLV VTFREENTIA FRHLFLLGYS DGSDDTFAAY
     TQEQLYQAIF YAVDQYLILP EISLGRYAYV RGGGGPWANG SALALCQRYY HRGHVDPAND
     TFDIDPRVVT DCIQVDPPDR PPDIPSEDLD FLDGSASYKN LTLKFHKLIN VTIHFQLKTI
     NLQSLINNEI PDCYTFSILI TFDNKAHSGR IPIRLETKTH IQECKHPSVS RHGDNSFRLL
     FDVVVILTCS LSFLLCARSL LRGFLLQNEF VVFMWRRRGR EISLWERLEF VNGWYILLVT
     SDVLTISGTV MKIGIEAKNL ASYDVCSILL GTSTLLVWVG VIRYLTFFHK YNILIATLRV
     ALPSVMRFCC CVAVIYLGYC FCGWIVLGPY HVKFRSLSMV SECLFSLING DDMFVTFAAM
     QAQQGHSSLV WLFSQLYLYS FISLFIYMVL SLFIALITGA YDTIKHPGGT GTEKSELQAY
     IEQCQDSPTS GKFRRGSGSA CSLFCCCGRD SPEDHSLLVN
//
ID   THUM1_MOUSE             Reviewed;         350 AA.
AC   Q99J36; Q3U6Y3;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=THUMP domain-containing protein 1;
GN   Name=Thumpd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-88, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-88, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-88, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-86 AND SER-88,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- SIMILARITY: Belongs to the THUMPD1 family.
CC   -!- SIMILARITY: Contains 1 THUMP domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK032078; BAC27685.1; -; mRNA.
DR   EMBL; AK152912; BAE31591.1; -; mRNA.
DR   EMBL; BC004776; AAH04776.1; -; mRNA.
DR   IPI; IPI00114862; -.
DR   RefSeq; NP_663560.1; NM_145585.1.
DR   UniGene; Mm.26392; -.
DR   ProteinModelPortal; Q99J36; -.
DR   SMR; Q99J36; 126-254.
DR   PhosphoSite; Q99J36; -.
DR   PRIDE; Q99J36; -.
DR   Ensembl; ENSMUST00000033236; ENSMUSP00000033236; ENSMUSG00000030942.
DR   GeneID; 233802; -.
DR   KEGG; mmu:233802; -.
DR   NMPDR; fig|10090.3.peg.17517; -.
DR   UCSC; uc009jlo.1; mouse.
DR   CTD; 233802; -.
DR   MGI; MGI:2444479; Thumpd1.
DR   eggNOG; roNOG13633; -.
DR   GeneTree; ENSGT00390000002365; -.
DR   HOGENOM; HBG445123; -.
DR   HOVERGEN; HBG053030; -.
DR   InParanoid; Q99J36; -.
DR   OMA; AQYVQAK; -.
DR   OrthoDB; EOG4P8FJT; -.
DR   PhylomeDB; Q99J36; -.
DR   NextBio; 461488; -.
DR   ArrayExpress; Q99J36; -.
DR   Bgee; Q99J36; -.
DR   CleanEx; MM_THUMPD1; -.
DR   Genevestigator; Q99J36; -.
DR   GermOnline; ENSMUSG00000030942; Mus musculus.
DR   InterPro; IPR004114; THUMP.
DR   Pfam; PF02926; THUMP; 1.
DR   SMART; SM00981; THUMP; 1.
DR   PROSITE; PS51165; THUMP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    350       THUMP domain-containing protein 1.
FT                                /FTId=PRO_0000072531.
FT   DOMAIN      147    254       THUMP.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       8      8       Phosphoserine.
FT   MOD_RES      86     86       Phosphoserine.
FT   MOD_RES      88     88       Phosphoserine.
SQ   SEQUENCE   350 AA;  38885 MW;  AD24B88A009749F8 CRC64;
     MATTAQQSPQ PVAGKRKGKS QFLPAKRARR GDAGGPRQLE PGLQGILITC NMNERKCVEE
     AYSLLNEYGD DMYGPEKFID KDQQPSGSEG EDDDAEAALK KEVGDIKAST EKRLRRFQSV
     ESGANNVVFI RTLGIEPEKL VHHILQDMYK TKKKKTRVIL RMLPISGTCK AFLEDMKKYA
     ETFLEPWFKA PNKGTFQIVY KSRNNSHMNR EEVIKELAGI VGSLNSENKV DLTNPEYTVV
     VEIIKAVCCL SVVKDYVLFR KYNLQEVVKS AKDSQPHPKL GNGKEAKLEP DSKLSQSDPP
     EGNQVAPESI EELGQTEPGS ETQAGSEGDA KPEPESQVSE VPKTNENELS
//
ID   STML2_MOUSE             Reviewed;         353 AA.
AC   Q99JB2; Q9DCG8;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Stomatin-like protein 2;
DE            Short=SLP-2;
GN   Name=Stoml2; Synonyms=Slp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=FVB; TISSUE=Kidney;
RA   Chang J.G., Chan W.L.;
RT   "Mouse stomatin-like protein 2 (MSLP2) mRNA.";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N, and FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH CACNA2D2.
RX   PubMed=16928863; DOI=10.1523/JNEUROSCI.2764-06.2006;
RA   Davies A., Douglas L., Hendrich J., Wratten J., Tran Van Minh A.,
RA   Foucault I., Koch D., Pratt W.S., Saibil H.R., Dolphin A.C.;
RT   "The calcium channel alpha2delta-2 subunit partitions with CaV2.1 into
RT   lipid rafts in cerebellum: implications for localization and
RT   function.";
RL   J. Neurosci. 26:8748-8757(2006).
CC   -!- SUBUNIT: Interacts with CACNA2D2.
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC       similarity). Cytoplasm (By similarity). Cytoplasm, cytoskeleton
CC       (By similarity). Note=Associated with the cytoskeleton (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the band 7/mec-2 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF323178; AAG53404.1; -; mRNA.
DR   EMBL; AK002793; BAB22363.1; -; mRNA.
DR   EMBL; BC003425; AAH03425.1; -; mRNA.
DR   EMBL; BC069941; AAH69941.1; -; mRNA.
DR   IPI; IPI00115117; -.
DR   RefSeq; NP_075720.1; NM_023231.2.
DR   UniGene; Mm.331565; -.
DR   ProteinModelPortal; Q99JB2; -.
DR   SMR; Q99JB2; 70-216.
DR   STRING; Q99JB2; -.
DR   PhosphoSite; Q99JB2; -.
DR   REPRODUCTION-2DPAGE; Q99JB2; -.
DR   PRIDE; Q99JB2; -.
DR   Ensembl; ENSMUST00000030169; ENSMUSP00000030169; ENSMUSG00000028455.
DR   GeneID; 66592; -.
DR   KEGG; mmu:66592; -.
DR   NMPDR; fig|10090.3.peg.9459; -.
DR   UCSC; uc008soy.1; mouse.
DR   CTD; 66592; -.
DR   MGI; MGI:1913842; Stoml2.
DR   GeneTree; ENSGT00550000074454; -.
DR   HOGENOM; HBG714701; -.
DR   HOVERGEN; HBG061488; -.
DR   InParanoid; Q99JB2; -.
DR   OMA; DYWGIRC; -.
DR   OrthoDB; EOG405S1P; -.
DR   PhylomeDB; Q99JB2; -.
DR   NextBio; 322100; -.
DR   ArrayExpress; Q99JB2; -.
DR   Bgee; Q99JB2; -.
DR   CleanEx; MM_STOML2; -.
DR   Genevestigator; Q99JB2; -.
DR   GermOnline; ENSMUSG00000028455; Mus musculus.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   InterPro; IPR001107; Band_7.
DR   InterPro; IPR001972; Stomatin.
DR   PANTHER; PTHR10264; Stomatin; 1.
DR   Pfam; PF01145; Band_7; 1.
DR   PRINTS; PR00721; STOMATIN.
DR   SMART; SM00244; PHB; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein.
FT   CHAIN         1    353       Stomatin-like protein 2.
FT                                /FTId=PRO_0000094032.
FT   MOD_RES     124    124       Phosphotyrosine (By similarity).
FT   MOD_RES     145    145       N6-acetyllysine (By similarity).
FT   MOD_RES     233    233       N6-acetyllysine (By similarity).
FT   CONFLICT      5      5       A -> R (in Ref. 2; BAB22363).
FT   CONFLICT    152    152       S -> F (in Ref. 2; BAB22363).
SQ   SEQUENCE   353 AA;  38385 MW;  391D269576F6E6BB CRC64;
     MLARAARGTG ALLLRGSVQA SGRVPRRASS GLPRNTVILF VPQQEAWVVE RMGRFHRILE
     PGLNVLIPVL DRIRYVQSLK EIVINVPEQS AVTLDNVTLQ IDGVLYLRIM DPYKASYGVE
     DPEYAVTQLA QTTMRSELGK LSLDKVFRER ESLNANIVDA INQAADCWGI RCLRYEIKDI
     HVPPRVKESM QMQVEAERRK RATVLESEGT RESAINVAEG KKQAQILASE AEKAEQINQA
     AGEASAVLAK AKAKAEAIRI LAGALTQHNG DAAASLTVAE QYVSAFSKLA KDSNTVLLPS
     NPSDVTSMVA QAMGVYGALT KAPVPGAQNS SQSRRDVQAT DTSIEELGRV KLS
//
ID   PACN3_MOUSE             Reviewed;         424 AA.
AC   Q99JB8; Q9EQP9;
DT   13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Protein kinase C and casein kinase II substrate protein 3;
GN   Name=Pacsin3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20534871; PubMed=11082044;
RA   Modregger J., Ritter B., Witter B., Paulsson M., Plomann M.;
RT   "All three PACSIN isoforms bind to endocytic proteins and inhibit
RT   endocytosis.";
RL   J. Cell Sci. 113:4511-4521(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=21100457; PubMed=11179684; DOI=10.1016/S0378-1119(00)00531-X;
RA   Sumoy L., Pluvinet R., Andreu N., Estivill X., Escarceller M.;
RT   "PACSIN 3 is a novel SH3 domain cytoplasmic adapter protein of the
RT   pacsin-syndapin-FAP52 gene family.";
RL   Gene 262:199-205(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Neuron;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276 AND SER-354, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: May play a role in vesicle formation and transport.
CC   -!- SUBUNIT: Homo- and hetero-aggregates with other PACSINs. Binds
CC       dynamin 1, synaptojanin, synapsin 1 and the neural Wiskott-Aldrich
CC       syndrome protein (N-WASP). Also interacts with MDC9 and MDC15 (By
CC       similarity).
CC   -!- INTERACTION:
CC       O88839:Adam15; NbExp=1; IntAct=EBI-77834, EBI-77874;
CC       Q61072:Adam9; NbExp=1; IntAct=EBI-77834, EBI-77983;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane;
CC       Peripheral membrane protein; Cytoplasmic side (By similarity).
CC       Note=Detected at the inner aspect of the plasma membrane in cells
CC       or myotubes (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle, heart and
CC       lung.
CC   -!- PTM: Phosphorylated by casein kinase 2 (CK2) and protein kinase C
CC       (PKC) (Probable).
CC   -!- SIMILARITY: Belongs to the PACSIN family.
CC   -!- SIMILARITY: Contains 1 FCH domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF149824; AAG31022.1; -; mRNA.
DR   EMBL; AF242531; AAK29208.1; -; mRNA.
DR   EMBL; BC003884; AAH03884.1; -; mRNA.
DR   IPI; IPI00319933; -.
DR   RefSeq; NP_083009.1; NM_028733.3.
DR   RefSeq; NP_112019.2; NM_030880.2.
DR   UniGene; Mm.236650; -.
DR   ProteinModelPortal; Q99JB8; -.
DR   SMR; Q99JB8; 15-301, 366-420.
DR   IntAct; Q99JB8; 2.
DR   STRING; Q99JB8; -.
DR   PhosphoSite; Q99JB8; -.
DR   PRIDE; Q99JB8; -.
DR   Ensembl; ENSMUST00000028694; ENSMUSP00000028694; ENSMUSG00000027257.
DR   Ensembl; ENSMUST00000059566; ENSMUSP00000054391; ENSMUSG00000027257.
DR   Ensembl; ENSMUST00000111349; ENSMUSP00000106981; ENSMUSG00000027257.
DR   GeneID; 80708; -.
DR   KEGG; mmu:80708; -.
DR   UCSC; uc008kvo.1; mouse.
DR   CTD; 80708; -.
DR   MGI; MGI:1891410; Pacsin3.
DR   GeneTree; ENSGT00510000046376; -.
DR   HOGENOM; HBG446365; -.
DR   HOVERGEN; HBG053486; -.
DR   InParanoid; Q99JB8; -.
DR   OMA; EQAFESC; -.
DR   OrthoDB; EOG44QT13; -.
DR   PhylomeDB; Q99JB8; -.
DR   NextBio; 350063; -.
DR   ArrayExpress; Q99JB8; -.
DR   Bgee; Q99JB8; -.
DR   Genevestigator; Q99JB8; -.
DR   GermOnline; ENSMUSG00000027257; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IDA:MGI.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0045806; P:negative regulation of endocytosis; IDA:MGI.
DR   InterPro; IPR001060; FCH.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00611; FCH; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00055; FCH; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50133; FCH; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Coiled coil; Cytoplasm; Endocytosis; Membrane;
KW   Phosphoprotein; SH3 domain.
FT   CHAIN         1    424       Protein kinase C and casein kinase II
FT                                substrate protein 3.
FT                                /FTId=PRO_0000161801.
FT   DOMAIN       10     73       FCH.
FT   DOMAIN      363    424       SH3.
FT   COILED      174    217       Potential.
FT   MOD_RES     276    276       Phosphoserine.
FT   MOD_RES     319    319       Phosphoserine.
FT   MOD_RES     324    324       Phosphothreonine (By similarity).
FT   MOD_RES     327    327       Phosphoserine (By similarity).
FT   MOD_RES     344    344       Phosphoserine (By similarity).
FT   MOD_RES     354    354       Phosphoserine.
FT   MOD_RES     383    383       Phosphoserine (By similarity).
FT   CONFLICT    360    360       R -> G (in Ref. 1; AAG31022).
SQ   SEQUENCE   424 AA;  48585 MW;  00475BC0321485B7 CRC64;
     MAPEEDAGGE VLGGSFWEAG NYRRTVQRVE DGHRLCGDLV SCFQERARIE KAYAQQLADW
     ARKWRGAVEK GPQYGTLEKA WHAFFTAAER LSELHLEVRE KLHGPDSERV RTWQRGAFHR
     PVLGGFRESR AAEDGFRKAQ KPWLKRLKEV EASKKSYHTA RKDEKTAQTR ESHAKADSSM
     SQEQLRKLQE RVGRCTKEAE KMKTQYEQTL AELNRYTPRY MEDMEQAFES CQAAERQRLL
     FFKDVLLTLH QHLDLSSSDK FHELHRDLQQ SIEAASDEED LRWWRSTHGP GMAMNWPQFE
     EWSLDTQRAI SRKEKGGRSP DEVTLTSIVP TRDGTAPPPQ SPSSPGSGQD EDWSDEESPR
     KVATGVRVRA LYDYAGQEAD ELSFRAGEEL LKMSEEDEQG WCQGQLQSGR IGLYPANYVE
     CVGA
//
ID   PSIP1_MOUSE             Reviewed;         528 AA.
AC   Q99JF8; A2BI10; A2BI11; Q3TEJ7; Q3TTD7; Q3UTA1; Q80WQ7; Q99JF7;
AC   Q99LR4; Q9CT03;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=PC4 and SFRS1-interacting protein;
DE   AltName: Full=Lens epithelium-derived growth factor;
DE            Short=mLEDGF;
GN   Name=Psip1; Synonyms=Ledgf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Testis;
RA   Bashein A.M., Brady G.;
RL   Thesis (2000), University of Manchester, United Kingdom.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA   Yu L.;
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and Czech II; TISSUE=Brain, Limb, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-248.
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Egg, Embryo, Testis, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-134 AND THR-141, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272 AND SER-274, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-129; SER-272
RP   AND SER-274, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272 AND SER-274, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-274, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176; SER-272 AND
RP   SER-274, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Transcriptional coactivator involved in neuroepithelial
CC       stem cell differentiation and neurogenesis. Involved in particular
CC       in lens epithelial cell gene regulation and stress responses. May
CC       play an important role in lens epithelial to fiber cell terminal
CC       differentiation. May play a protective role during stress-induced
CC       apoptosis (By similarity).
CC   -!- SUBUNIT: Interacts with IFRD1/PC4. Interacts POGZ and CDCA7L (By
CC       similarity). Murine leukemia virus (MLV) integrase does not
CC       interact with PSIP1.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Ledgfa, p75;
CC         IsoId=Q99JF8-1; Sequence=Displayed;
CC       Name=2; Synonyms=Ledgfb, p52;
CC         IsoId=Q99JF8-2; Sequence=VSP_014299, VSP_014300;
CC         Note=Ref.4 (AAH52177) sequence is in conflict in positions:
CC         324:HQTTCNLQ->QLKALIQ;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the HDGF family.
CC   -!- SIMILARITY: Contains 1 PWWP domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ308965; CAC34944.1; -; mRNA.
DR   EMBL; AJ308966; CAC34945.1; -; mRNA.
DR   EMBL; AF339082; AAO32949.1; -; mRNA.
DR   EMBL; AF339083; AAO32950.1; -; mRNA.
DR   EMBL; BX682545; CAM20466.1; -; Genomic_DNA.
DR   EMBL; BX682545; CAM20467.1; -; Genomic_DNA.
DR   EMBL; BC002260; AAH02260.1; -; mRNA.
DR   EMBL; BC043079; AAH43079.1; -; mRNA.
DR   EMBL; BC052177; AAH52177.1; -; mRNA.
DR   EMBL; AK011572; BAB27707.3; -; mRNA.
DR   EMBL; AK139598; BAE24079.1; -; mRNA.
DR   EMBL; AK161426; BAE36388.1; -; mRNA.
DR   EMBL; AK169600; BAE41251.1; -; mRNA.
DR   IPI; IPI00115257; -.
DR   IPI; IPI00608118; -.
DR   RefSeq; NP_598709.1; NM_133948.4.
DR   UniGene; Mm.105331; -.
DR   UniGene; Mm.448301; -.
DR   ProteinModelPortal; Q99JF8; -.
DR   SMR; Q99JF8; 5-93, 346-429.
DR   STRING; Q99JF8; -.
DR   PhosphoSite; Q99JF8; -.
DR   PRIDE; Q99JF8; -.
DR   Ensembl; ENSMUST00000030207; ENSMUSP00000030207; ENSMUSG00000028484.
DR   Ensembl; ENSMUST00000107215; ENSMUSP00000102833; ENSMUSG00000028484.
DR   GeneID; 101739; -.
DR   KEGG; mmu:101739; -.
DR   UCSC; uc008tkw.1; mouse.
DR   UCSC; uc008tkx.1; mouse.
DR   CTD; 101739; -.
DR   MGI; MGI:2142116; Psip1.
DR   GeneTree; ENSGT00530000063013; -.
DR   HOVERGEN; HBG108300; -.
DR   InParanoid; Q99JF8; -.
DR   OMA; DSNQPQH; -.
DR   OrthoDB; EOG4V438N; -.
DR   PhylomeDB; Q99JF8; -.
DR   NextBio; 355092; -.
DR   ArrayExpress; Q99JF8; -.
DR   Bgee; Q99JF8; -.
DR   CleanEx; MM_PSIP1; -.
DR   Genevestigator; Q99JF8; -.
DR   GermOnline; ENSMUSG00000028484; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR021567; LEDGF.
DR   InterPro; IPR000313; PWWP.
DR   InterPro; IPR017859; Treacle-like_TCS.
DR   Pfam; PF11467; LEDGF; 1.
DR   Pfam; PF00855; PWWP; 1.
DR   PRINTS; PR01503; TREACLE.
DR   SMART; SM00293; PWWP; 1.
DR   PROSITE; PS50812; PWWP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; DNA-binding; Nucleus;
KW   Phosphoprotein; Transcription; Transcription regulation.
FT   CHAIN         1    528       PC4 and SFRS1-interacting protein.
FT                                /FTId=PRO_0000191709.
FT   DOMAIN        7     64       PWWP.
FT   COILED      306    332       Potential.
FT   COILED      369    393       Potential.
FT   MOTIF       146    156       Nuclear localization signal (By
FT                                similarity).
FT   MOD_RES     105    105       Phosphoserine (By similarity).
FT   MOD_RES     106    106       Phosphoserine.
FT   MOD_RES     122    122       Phosphothreonine (By similarity).
FT   MOD_RES     129    129       Phosphoserine.
FT   MOD_RES     134    134       Phosphothreonine.
FT   MOD_RES     141    141       Phosphothreonine.
FT   MOD_RES     176    176       Phosphoserine.
FT   MOD_RES     269    269       Phosphothreonine (By similarity).
FT   MOD_RES     270    270       Phosphoserine (By similarity).
FT   MOD_RES     271    271       Phosphothreonine (By similarity).
FT   MOD_RES     272    272       Phosphoserine.
FT   MOD_RES     274    274       Phosphoserine.
FT   MOD_RES     432    432       Phosphoserine (By similarity).
FT   MOD_RES     435    435       Phosphothreonine (By similarity).
FT   MOD_RES     441    441       Phosphoserine (By similarity).
FT   MOD_RES     520    520       Phosphoserine (By similarity).
FT   MOD_RES     525    525       Phosphothreonine (By similarity).
FT   VAR_SEQ     324    331       QQNKDEGK -> HQTTCNLQ (in isoform 2).
FT                                /FTId=VSP_014299.
FT   VAR_SEQ     332    528       Missing (in isoform 2).
FT                                /FTId=VSP_014300.
SQ   SEQUENCE   528 AA;  59697 MW;  4A9AE28245843AB6 CRC64;
     MTRDFKPGDL IFAKMKGYPH WPARVDEVPD GAVKPPTNKL PIFFFGTHET AFLGPKDIFP
     YSENKEKYGK PNKRKGFNEG LWEIDNNPKV KFSSQQASTK QSNASSDVEV EEKETNVSKE
     DTDQEEKASN EDVTKAVDIT TPKAARRGRK RKAEKQVDTE EAGMVTAATA SNVKASPKRG
     RPAATEVKIP KPRGRPKVVK QPCPSDGDMV IDEDKSKKKG PEEKQPKKQL KKEEEGQKEE
     EKPRKEPDKK EGKKEVESKR KNLAKPGVTS TSDSEDEDDQ EGEKKRKGGR NFQAAHRRNM
     LKGQHEKEAG DRKRKQEEQM ETEQQNKDEG KKPEVKKVEK KRETSMDSRL QRIHAEIKNS
     LKIDNLDVNR CIEALDELAS LQVTMQQAQK HTEMITTLKK IRRFKVSQVI MEKSTMLYNK
     FKNMFLVGEG DSVITQVLNK SLAEQRQHEE ANKTKDQGKK GPNKKLEKEP TGTKSLNGGS
     DAQESNHPQH NGDSNEDGKD SREASSKTKP PGEEREAEIS LKESTLDN
//
ID   ETBR2_MOUSE             Reviewed;         481 AA.
AC   Q99JG2; O88313; Q80UB9; Q99JG1;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Endothelin B receptor-like protein 2;
DE            Short=ETBR-LP-2;
DE   AltName: Full=G-protein coupled receptor 37-like 1;
DE   Flags: Precursor;
GN   Name=Gpr37l1; Synonyms=Etbrlp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Liver;
RA   Marazziti D., Golini E., Magrelli A., Matteoni R.,
RA   Tocchini-Valentini G.P.;
RT   "Genomic analysis of GPR37 and related orphan G-protein coupled
RT   receptor genes highly expressed in the mammalian brain.";
RL   Curr. Genomics 2:253-260(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 28-481.
RC   STRAIN=C57BL/6; TISSUE=Hippocampus;
RA   Matsuo N., Kawamoto S., Matsubara K., Okubo K.;
RT   "Cloning of a cDNA encoding a novel G-protein coupled receptor
RT   uniquely expressed in the adult brain.";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 256-454.
RX   MEDLINE=22584407; PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA   Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA   Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA   Bergmann J.E., Gaitanaris G.A.;
RT   "The G protein-coupled receptor repertoires of human and mouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Orphan receptor (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (Probable).
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA32062.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ306537; CAC34842.1; -; Genomic_DNA.
DR   EMBL; AJ306538; CAC34843.1; -; Genomic_DNA.
DR   EMBL; AB016602; BAA32062.1; ALT_INIT; mRNA.
DR   EMBL; AY255561; AAO85073.1; -; mRNA.
DR   IPI; IPI00468685; -.
DR   RefSeq; NP_602320.2; NM_134438.3.
DR   UniGene; Mm.272290; -.
DR   ProteinModelPortal; Q99JG2; -.
DR   STRING; Q99JG2; -.
DR   PhosphoSite; Q99JG2; -.
DR   PRIDE; Q99JG2; -.
DR   Ensembl; ENSMUST00000027682; ENSMUSP00000027682; ENSMUSG00000026424.
DR   GeneID; 171469; -.
DR   KEGG; mmu:171469; -.
DR   CTD; 171469; -.
DR   MGI; MGI:1928503; Gpr37l1.
DR   GeneTree; ENSGT00550000074261; -.
DR   HOGENOM; HBG445389; -.
DR   HOVERGEN; HBG051808; -.
DR   InParanoid; Q99JG2; -.
DR   OMA; WDFLVLF; -.
DR   OrthoDB; EOG4CNQS6; -.
DR   NextBio; 371005; -.
DR   ArrayExpress; Q99JG2; -.
DR   Bgee; Q99JG2; -.
DR   CleanEx; MM_GPR37L1; -.
DR   Genevestigator; Q99JG2; -.
DR   GermOnline; ENSMUSG00000026424; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR003909; GPR37_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01421; GPR37ORPHANR.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; FALSE_NEG.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Phosphoprotein; Receptor; Signal; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     24       Potential.
FT   CHAIN        25    481       Endothelin B receptor-like protein 2.
FT                                /FTId=PRO_0000012797.
FT   TOPO_DOM     25    134       Extracellular (Potential).
FT   TRANSMEM    135    155       Helical; Name=1; (Potential).
FT   TOPO_DOM    156    167       Cytoplasmic (Potential).
FT   TRANSMEM    168    188       Helical; Name=2; (Potential).
FT   TOPO_DOM    189    205       Extracellular (Potential).
FT   TRANSMEM    206    226       Helical; Name=3; (Potential).
FT   TOPO_DOM    227    251       Cytoplasmic (Potential).
FT   TRANSMEM    252    272       Helical; Name=4; (Potential).
FT   TOPO_DOM    273    310       Extracellular (Potential).
FT   TRANSMEM    311    331       Helical; Name=5; (Potential).
FT   TOPO_DOM    332    360       Cytoplasmic (Potential).
FT   TRANSMEM    361    381       Helical; Name=6; (Potential).
FT   TOPO_DOM    382    398       Extracellular (Potential).
FT   TRANSMEM    399    419       Helical; Name=7; (Potential).
FT   TOPO_DOM    420    481       Cytoplasmic (Potential).
FT   COMPBIAS    418    439       Cys-rich.
FT   MOD_RES     471    471       Phosphoserine.
FT   CARBOHYD    105    105       N-linked (GlcNAc...) (Potential).
FT   DISULFID    203    286       By similarity.
SQ   SEQUENCE   481 AA;  52729 MW;  D7CF26B83B7F6E8C CRC64;
     MRWLWPLAVS LVVVLTVGLS GVSGAATSSL GGHRAKVQEQ QSRPRRGTKD EGPKEVQHYV
     PEEWAEYPKP IHPAGLQPTK TLEATSPNPD KDGATPGNGQ ELRVNLTGTP SQRLQIQNPL
     YPVTESSYSA YAIMLLALVV FAVGIVGNLS VMCIVWHSYY LKSAWNSILA SLALWDFLVL
     FFCLPIVIFN EITKQRLLGD VSCRAVPFME VSSLGVTTFS LCALGIDRFH VATSTLPKVR
     PIERCQSILA KLAVIWVGSM MLAVPELLLW QLAQEPAPTA GTVDSCIMKP SADLPESVYS
     LVMTYQNARM WWYFGCYFCL PILFTVTCQL VTWRVRGPPG RKPECRAGRH EQCESQLNST
     VVGLTVVYAF CTLPENVCNI VVAYLSTELT RQTLDLLGLI NQFSTFFKGA ITPVLLLCIC
     RPLGQAFLDC CCCCCCEECG GASDSSATVS ADSKLKAEVS SSIYFHKPRE SPPLLPLGTP
     C
//
ID   KLH22_MOUSE             Reviewed;         634 AA.
AC   Q99JN2; D3YW27; Q8BT13;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Kelch-like protein 22;
GN   Name=Klhl22; Synonyms=Kelchl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-12; 45-59; 66-76; 158-184; 196-204; 240-256;
RP   268-294; 320-329; 419-434; 495-508 AND 596-603, CLEAVAGE OF INITIATOR
RP   METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RA   Bienvenut W.V., Sandilands E., Serrels B., Brunton V.G., Frame M.C.;
RL   Submitted (FEB-2008) to UniProtKB.
CC   -!- FUNCTION: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3
CC       ubiquitin ligase complex required for cell division. BCR E3
CC       ubiquitin ligase complexes mediate the ubiquitination of target
CC       proteins (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Component of the BCR(KLHL22) E3 ubiquitin ligase complex,
CC       at least composed of CUL3, KLHL22 and RBX1 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99JN2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99JN2-2; Sequence=VSP_019452;
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC   -!- SIMILARITY: Contains 6 Kelch repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK028197; BAC25806.1; -; mRNA.
DR   EMBL; AK143514; BAE25409.1; -; mRNA.
DR   EMBL; AC087802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC005800; AAH05800.1; -; mRNA.
DR   IPI; IPI00224738; -.
DR   IPI; IPI00762900; -.
DR   RefSeq; NP_663454.3; NM_145479.4.
DR   UniGene; Mm.282807; -.
DR   UniGene; Mm.477359; -.
DR   ProteinModelPortal; Q99JN2; -.
DR   SMR; Q99JN2; 22-280, 297-592.
DR   PRIDE; Q99JN2; -.
DR   Ensembl; ENSMUST00000090146; ENSMUSP00000087607; ENSMUSG00000022750.
DR   Ensembl; ENSMUST00000120488; ENSMUSP00000112412; ENSMUSG00000022750.
DR   GeneID; 224023; -.
DR   KEGG; mmu:224023; -.
DR   UCSC; uc007yma.1; mouse.
DR   UCSC; uc007ymc.1; mouse.
DR   CTD; 224023; -.
DR   MGI; MGI:1337995; Klhl22.
DR   eggNOG; roNOG12371; -.
DR   GeneTree; ENSGT00560000076541; -.
DR   HOVERGEN; HBG105890; -.
DR   OMA; ETHCYDP; -.
DR   OrthoDB; EOG4ZGPC4; -.
DR   NextBio; 377017; -.
DR   ArrayExpress; Q99JN2; -.
DR   Bgee; Q99JN2; -.
DR   CleanEx; MM_KLHL22; -.
DR   Genevestigator; Q99JN2; -.
DR   GermOnline; ENSMUSG00000022750; Mus musculus.
DR   GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0051301; P:cell division; ISS:UniProtKB.
DR   InterPro; IPR011705; BACK.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR013069; BTB_POZ.
DR   InterPro; IPR017096; Kelch-like_gigaxonin.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Gene3D; G3DSA:2.120.10.80; Kelch-typ_b-propeller; 1.
DR   Pfam; PF07707; BACK; 1.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF01344; Kelch_1; 5.
DR   PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
DR   SMART; SM00875; BACK; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00612; Kelch; 6.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   PROSITE; PS50097; BTB; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Direct protein sequencing;
KW   Kelch repeat; Repeat; Ubl conjugation pathway.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    634       Kelch-like protein 22.
FT                                /FTId=PRO_0000242156.
FT   DOMAIN       50    117       BTB.
FT   REPEAT      299    349       Kelch 1.
FT   REPEAT      350    399       Kelch 2.
FT   REPEAT      400    446       Kelch 3.
FT   REPEAT      448    493       Kelch 4.
FT   REPEAT      495    544       Kelch 5.
FT   REPEAT      545    593       Kelch 6.
FT   MOD_RES       2      2       N-acetylalanine.
FT   VAR_SEQ     634    634       D -> STPSHSQSLWLPFCEPWSVW (in isoform 2).
FT                                /FTId=VSP_019452.
FT   CONFLICT     22     22       C -> L (in Ref. 1; BAC25806).
FT   CONFLICT    428    428       Y -> C (in Ref. 1; BAC25806).
SQ   SEQUENCE   634 AA;  71687 MW;  E34C21B5919620EB CRC64;
     MAEEQDFAQL CRLPTQPSHS HCVNNTYRST QHSQALLRGL LALRDSGILF DVVLVVEGKH
     IEAHRILLAA SCDYFRGMFA GGLKEMEQEE VLIHGVSYNA MCQILHFIYT SELELSLSNV
     QETLVAACQL QIPEIIHFCC DFLMSWVDEE NILDVYRLAD LFDLNHLTQQ LDTYILKNFV
     AFSRTDKYRQ LPLEKVYSLL SSNRLEVSCE TEVYEGALLY HYSLEQVQAD QISLNEPPKL
     LETVRFPLME AEVLQRLHDK LGPSPLRDTV ASALMYHRNE ILQPSLQGPQ TELRSDFQCV
     VGFGGIHSTP STILSDQAKY LNPLLGEWKH FTASLAPRMS NQGIAVLNNF VYLIGGDNNV
     QGFRAESRCW RYDPRHNRWF QIQSLQQEHA DLCVCVVGKY IYAVAGRDYH NDLSAVERYD
     PATNSWDYVA PLKKEVYAHA GTTLQGKMYI TCGRRGEDYL KETHCYDPGS NTWHTLADGP
     VRRAWHGMAA LLDKLFVIGG SNNDAGYRRD VHQVACYSCT SRQWSSVCPL PAGHGEPGIA
     VLDSRIYVLG GRSHNRGSRT GYVHIYDMEK DCWEEGPQLN NSISGLAACV LTLPRSLLHE
     QPRGTPNRSQ ADADFASEVM SVSDWEEFDN SSED
//
ID   HOME3_MOUSE             Reviewed;         356 AA.
AC   Q99JP6; Q9Z215;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-FEB-2011, entry version 73.
DE   RecName: Full=Homer protein homolog 3;
DE            Short=Homer-3;
GN   Name=Homer3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2-356 (ISOFORM 2).
RC   STRAIN=C3H; TISSUE=Myotube;
RX   MEDLINE=99023644; PubMed=9808458; DOI=10.1016/S0896-6273(00)80588-7;
RA   Xiao B., Tu J.C., Petralia R.S., Yuan J.P., Doan A., Breder C.D.,
RA   Ruggiero A., Lanahan A.A., Wenthold R.J., Worley P.F.;
RT   "Homer regulates the association of group 1 metabotropic glutamate
RT   receptors with multivalent complexes of homer-related, synaptic
RT   proteins.";
RL   Neuron 21:707-716(1998).
RN   [3]
RP   INTERACTION WITH METABOTROPIC GLUTAMATE AND ITPR1 RECEPTORS.
RX   MEDLINE=99023645; PubMed=9808459; DOI=10.1016/S0896-6273(00)80589-9;
RA   Tu J.C., Xiao B., Yuan J.P., Lanahan A.A., Leoffert K., Li M.,
RA   Linden D.J., Worley P.F.;
RT   "Homer binds a novel proline-rich motif and links group 1 metabotropic
RT   glutamate receptors with IP3 receptors.";
RL   Neuron 21:717-726(1998).
RN   [4]
RP   INTERACTION WITH GRM1 AND GRM5.
RX   PubMed=11418862; DOI=10.1038/35082096;
RA   Ango F., Prezeau L., Muller T., Tu J.C., Xiao B., Worley P.F.,
RA   Pin J.P., Bockaert J., Fagni L.;
RT   "Agonist-independent activation of metabotropic glutamate receptors by
RT   the intracellular protein Homer.";
RL   Nature 411:962-965(2001).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
CC   -!- FUNCTION: Postsynaptic density scaffolding protein. Binds and
CC       cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1,
CC       RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with
CC       ER-associated ITPR1 receptors, it aids the coupling of surface
CC       receptors to intracellular calcium release. Isoforms can be
CC       differently regulated and may play an important role in
CC       maintaining the plasticity at glutamatergic synapses (By
CC       similarity).
CC   -!- SUBUNIT: Isoform 1 and isoform 2 encode coiled-coil structures
CC       that mediate homo- and heteromultimerization.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell junction,
CC       synapse, postsynaptic cell membrane, postsynaptic density (By
CC       similarity). Cell junction, synapse (By similarity).
CC       Note=Postsynaptic density of neuronal cells (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99JP6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99JP6-2; Sequence=VSP_009078;
CC   -!- TISSUE SPECIFICITY: Expressed in the cerebellum, hippocampus, lung
CC       and thymus.
CC   -!- DOMAIN: The WH1 domain interacts with the PPXXF motif in GRM1,
CC       GRM5, RYR1, RYR2, ITPR1, SHANK 1 and SHANK3.
CC   -!- SIMILARITY: Belongs to the Homer family.
CC   -!- SIMILARITY: Contains 1 WH1 domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC005773; AAH05773.1; -; mRNA.
DR   EMBL; AF093261; AAC71025.1; -; mRNA.
DR   IPI; IPI00262616; -.
DR   IPI; IPI00395047; -.
DR   UniGene; Mm.440659; -.
DR   ProteinModelPortal; Q99JP6; -.
DR   SMR; Q99JP6; 2-118, 285-356.
DR   MINT; MINT-3370168; -.
DR   STRING; Q99JP6; -.
DR   PhosphoSite; Q99JP6; -.
DR   PRIDE; Q99JP6; -.
DR   Ensembl; ENSMUST00000003669; ENSMUSP00000003669; ENSMUSG00000003573.
DR   Ensembl; ENSMUST00000110124; ENSMUSP00000105751; ENSMUSG00000003573.
DR   UCSC; uc009lzs.1; mouse.
DR   UCSC; uc009lzt.1; mouse.
DR   MGI; MGI:1347359; Homer3.
DR   GeneTree; ENSGT00390000017850; -.
DR   HOVERGEN; HBG051918; -.
DR   NextBio; 304615; -.
DR   ArrayExpress; Q99JP6; -.
DR   Bgee; Q99JP6; -.
DR   CleanEx; MM_HOMER3; -.
DR   Genevestigator; Q99JP6; -.
DR   GermOnline; ENSMUSG00000003573; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR   GO; GO:0007216; P:metabotropic glutamate receptor signaling pathway; TAS:MGI.
DR   InterPro; IPR000697; EVH1.
DR   InterPro; IPR011993; PH_type.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00568; WH1; 1.
DR   SMART; SM00461; WH1; 1.
DR   PROSITE; PS50229; WH1; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Coiled coil;
KW   Cytoplasm; Membrane; Phosphoprotein; Postsynaptic cell membrane;
KW   Synapse.
FT   CHAIN         1    356       Homer protein homolog 3.
FT                                /FTId=PRO_0000191012.
FT   DOMAIN        1    113       WH1.
FT   COILED       94    122       Potential.
FT   COILED      191    353       Potential.
FT   MOD_RES     159    159       Phosphoserine.
FT   MOD_RES     254    254       Phosphoserine (By similarity).
FT   VAR_SEQ     267    267       Q -> QEIQ (in isoform 2).
FT                                /FTId=VSP_009078.
SQ   SEQUENCE   356 AA;  39678 MW;  6195F90F0E1D0F3F CRC64;
     MSTAREQPIF STRAHVFQID PTTKRNWIPA GKHALTVSYF YDATRNVYRI ISIGGAKAII
     NSTVTPNMTF TKTSQKFGQW ADSRANTVYG LGFASEQQLT QFAEKFQEVK EAARLAREKS
     QDGGEFTSTG LALASHQVPP SPLVSTNGPG EEKLFRSQSA DTPGPTERER LKKMLSEGSV
     GEVQWEAEFF ALQDSNQRLA GALREANAAA TQWRQQLEVQ RAEAELLRQR VAELEAQVAV
     EPVRAGEKEA TSQSVEQLEA RVQTKDQTLK NQSTGTREAP DTAEREETQQ QVQDLETRNA
     ELEQQLRAME CNLEEARAER ERARAEVGRA AQLLDVRLFE LSELREGLAR LAEAAP
//
ID   GGT7_MOUSE              Reviewed;         662 AA.
AC   Q99JP7; Q91V91;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Gamma-glutamyltransferase 7;
DE            Short=GGT 7;
DE            EC=2.3.2.2;
DE   AltName: Full=Gamma-glutamyltransferase-like 3;
DE   AltName: Full=Gamma-glutamyltranspeptidase 7;
DE   Contains:
DE     RecName: Full=Gamma-glutamyltransferase 7 heavy chain;
DE   Contains:
DE     RecName: Full=Gamma-glutamyltransferase 7 light chain;
DE   Flags: Precursor;
GN   Name=Ggt7; Synonyms=Ggtl3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary cancer;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 552-662.
RC   STRAIN=ILS, and ISS;
RX   MEDLINE=21363810; PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Cleaves glutathione conjugates (By similarity).
CC   -!- CATALYTIC ACTIVITY: (5-L-glutamyl)-peptide + an amino acid =
CC       peptide + 5-L-glutamyl amino acid.
CC   -!- PATHWAY: Sulfur metabolism; glutathione metabolism.
CC   -!- SUBUNIT: Heterodimer composed of the light and heavy chains. The
CC       active site is located in the light chain. Interacts with FAM57A
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK032051; BAC27672.1; -; mRNA.
DR   EMBL; BC005772; AAH05772.1; -; mRNA.
DR   EMBL; AF332053; AAK56082.1; -; mRNA.
DR   EMBL; AF332054; AAK56083.1; -; mRNA.
DR   IPI; IPI00115429; -.
DR   RefSeq; NP_659035.2; NM_144786.2.
DR   UniGene; Mm.41757; -.
DR   ProteinModelPortal; Q99JP7; -.
DR   SMR; Q99JP7; 133-659.
DR   STRING; Q99JP7; -.
DR   MEROPS; T03.017; -.
DR   PhosphoSite; Q99JP7; -.
DR   PRIDE; Q99JP7; -.
DR   Ensembl; ENSMUST00000029131; ENSMUSP00000029131; ENSMUSG00000027603.
DR   GeneID; 207182; -.
DR   KEGG; mmu:207182; -.
DR   UCSC; uc008nkq.1; mouse.
DR   CTD; 207182; -.
DR   MGI; MGI:1913385; Ggt7.
DR   GeneTree; ENSGT00550000074591; -.
DR   HOGENOM; HBG738311; -.
DR   HOVERGEN; HBG039468; -.
DR   InParanoid; Q99JP7; -.
DR   OrthoDB; EOG483D48; -.
DR   PhylomeDB; Q99JP7; -.
DR   BRENDA; 2.3.2.2; 244.
DR   NextBio; 371879; -.
DR   ArrayExpress; Q99JP7; -.
DR   Bgee; Q99JP7; -.
DR   CleanEx; MM_GGT7; -.
DR   Genevestigator; Q99JP7; -.
DR   GermOnline; ENSMUSG00000027603; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008415; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003840; F:gamma-glutamyltransferase activity; IEA:EC.
DR   GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000101; GGT_peptidase.
DR   PANTHER; PTHR11686; GGT_peptidase; 1.
DR   Pfam; PF01019; G_glu_transpept; 1.
DR   PRINTS; PR01210; GGTRANSPTASE.
DR   PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acyltransferase; Glutathione biosynthesis; Glycoprotein; Membrane;
KW   Phosphoprotein; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix; Zymogen.
FT   CHAIN         1    472       Gamma-glutamyltransferase 7 heavy chain
FT                                (By similarity).
FT                                /FTId=PRO_0000011068.
FT   CHAIN       473    662       Gamma-glutamyltransferase 7 light chain
FT                                (By similarity).
FT                                /FTId=PRO_0000011069.
FT   TOPO_DOM      1    106       Cytoplasmic (Potential).
FT   TRANSMEM    107    127       Helical; Signal-anchor for type II
FT                                membrane protein; (Potential).
FT   TOPO_DOM    128    662       Extracellular (Potential).
FT   MOD_RES      72     72       Phosphoserine (By similarity).
FT   MOD_RES      83     83       Phosphoserine.
FT   CARBOHYD    198    198       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    267    267       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    283    283       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    330    330       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    353    353       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    394    394       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    519    519       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    523    523       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    586    586       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    148    148       H -> S (in Ref. 1; BAC27672).
SQ   SEQUENCE   662 AA;  70302 MW;  BA7F32512CC4F381 CRC64;
     MAAENEASQE SALGAYSPVD YMSITSFPRL PEDEPAPAAP LRGRKDEDAF LGDPDTDPDS
     FLKSARLQRL PSSSSEMGSQ DGSPLRETRK DPFSAAAAEC SCRQDGLTVI VTACLTFATG
     VTVALVMQIY FGDPQIFQQG AVVTDASHCT ALGMEVLSKQ GSSVDAAVAA ALCLGIVAPH
     SSGLGGGGVM LVHDIRRNES HLIDFRESAP GALREEALQR SWDTKPGLLV GVPGMVKGLH
     EAHQLYGRLP WSQVLAFAAA VAQDGFNVTH DLAHALAEQL PPNASDRFLD TFLPLGHPPL
     PGSLLRRPDL AEVLDILGTS GPAAFYNGGN LTLEMVAEAQ HAGGVITEED FSNYSALTEK
     PVCGVYRGHL VLSPPPPHTG PALISALNIL EGFNLTSLVS REQALHWVAE TLKIALALAS
     RLGDPVYDST ITESMDDMLS KVEAANFRGH ISDSQAAPAP LLPVYELDGA PTAAQVLVMG
     PDDFIVAMVS SLNRPFGSGL LTPSGILLNS QMLDFSWPNR TANHSAPSLE NSVQPGKRPL
     SFLLPTVVRP AEGLCGTYLA LGANGAARGL SGLTQVLLNV LTLNRNLSDS LARGRLHPDL
     QSNLLQVDSE FTEEEIEFLE ARGHHVEKVD VLSWVHGSRR TNTFIIGVKD PRSPDAAGAT
     IL
//
ID   MST4_MOUSE              Reviewed;         416 AA.
AC   Q99JT2;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Serine/threonine-protein kinase MST4;
DE            EC=2.7.11.1;
DE   AltName: Full=Mammalian STE20-like protein kinase 4;
DE            Short=MST-4;
DE   AltName: Full=STE20-like kinase MST4;
GN   Name=Mst4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Mediator of cell growth. Modulates apoptosis (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Interaction with Golgi matrix protein GOLGA2
CC       leads to autophosphorylation on Thr-178, possibly as a consequence
CC       of stabilization of dimer formation. May also be activated by C-
CC       terminal cleavage (By similarity).
CC   -!- SUBUNIT: Homodimer. Interacts with PDCD10 and GOLGA2 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus
CC       membrane; Peripheral membrane protein; Cytoplasmic side (By
CC       similarity). Note=Localizes to the Golgi apparatus (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AK034609; BAC28768.1; -; mRNA.
DR   EMBL; BC005708; AAH05708.1; -; mRNA.
DR   IPI; IPI00115494; -.
DR   RefSeq; NP_598490.1; NM_133729.1.
DR   UniGene; Mm.391246; -.
DR   ProteinModelPortal; Q99JT2; -.
DR   SMR; Q99JT2; 17-300.
DR   STRING; Q99JT2; -.
DR   PhosphoSite; Q99JT2; -.
DR   PRIDE; Q99JT2; -.
DR   Ensembl; ENSMUST00000033444; ENSMUSP00000033444; ENSMUSG00000031112.
DR   GeneID; 70415; -.
DR   KEGG; mmu:70415; -.
DR   UCSC; uc009tdr.1; mouse.
DR   MGI; MGI:1917665; 2610018G03Rik.
DR   GeneTree; ENSGT00600000084209; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108518; -.
DR   InParanoid; Q99JT2; -.
DR   OMA; DSSYVTK; -.
DR   OrthoDB; EOG4MPHQB; -.
DR   PhylomeDB; Q99JT2; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 331563; -.
DR   ArrayExpress; Q99JT2; -.
DR   Bgee; Q99JT2; -.
DR   CleanEx; MM_2610018G03RIK; -.
DR   Genevestigator; Q99JT2; -.
DR   GermOnline; ENSMUSG00000031112; Mus musculus.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0042981; P:regulation of apoptosis; ISS:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Apoptosis; ATP-binding; Cytoplasm; Golgi apparatus; Kinase; Magnesium;
KW   Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    416       Serine/threonine-protein kinase MST4.
FT                                /FTId=PRO_0000086405.
FT   DOMAIN       24    274       Protein kinase.
FT   NP_BIND      30     38       ATP (By similarity).
FT   ACT_SITE    144    144       Proton acceptor (By similarity).
FT   BINDING      53     53       ATP (By similarity).
FT   MOD_RES       4      4       Phosphoserine (By similarity).
FT   MOD_RES     178    178       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     300    300       Phosphoserine (By similarity).
FT   MOD_RES     304    304       Phosphoserine (By similarity).
FT   MOD_RES     306    306       Phosphoserine (By similarity).
FT   MOD_RES     325    325       Phosphoserine (By similarity).
FT   MOD_RES     327    327       Phosphothreonine (By similarity).
SQ   SEQUENCE   416 AA;  46614 MW;  87EF04547F8BE681 CRC64;
     MAHSPVAVQV PGMQNNIADP EELFTKLERI GKGSFGEVFK GIDNRTQQVV AIKIIDLEEA
     EDEIEDIQQE ITVLSQCDSS YVTKYYGSYL KGSKLWIIME YLGGGSALDL LRAGPFDEFQ
     IATMLKEILK GLDYLHSEKK IHRDIKAANV LLSEQGDVKL ADFGVAGQLT DTQIKRNTFV
     GTPFWMAPEV IQQSAYDSKA DIWSLGITAI ELAKGEPPNS DMHPMRVLFL IPKNNPPTLI
     GDFTKSFKEF IDACLNKDPS FRPTAKELLK HKFIVKNSKK TSYLTELIDR FKRWKAEGHS
     DEESDSEGSD SESSSRESNP HPEWSFTTVR KKPDPKKLQN GEEQDLVQTL SCLSMIITPA
     FAELKQQDEN NASRNQAIEE LEKSIAVAET ACPGITDKMV KKLIEKFQKC SADESP
//
ID   GORS2_MOUSE             Reviewed;         451 AA.
AC   Q99JX3; Q3U9D2; Q8CCD0; Q91W68;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Golgi reassembly-stacking protein 2;
DE            Short=GRS2;
DE   AltName: Full=Golgi reassembly-stacking protein of 55 kDa;
DE            Short=GRASP55;
GN   Name=Gorasp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR
RP   LOCATION.
RX   MEDLINE=99417576; PubMed=10487747; DOI=10.1093/emboj/18.18.4949;
RA   Shorter J., Watson R., Giannakou M.-E., Clarke M., Warren G.,
RA   Barr F.A.;
RT   "GRASP55, a second mammalian GRASP protein involved in the stacking of
RT   Golgi cisternae in a cell-free system.";
RL   EMBO J. 18:4949-4960(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Colon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411 AND SER-432, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May be involved in assembly and membrane stacking of the
CC       Golgi cisternae, and in the process by which Golgi stacks reform
CC       after mitotic breakdown. May regulate the intracellular transport
CC       and presentation of a defined set of transmembrane proteins, such
CC       as transmembrane TGFA.
CC   -!- SUBUNIT: Forms a RAB2 effector complex with BLZF1/Golgin 45 in the
CC       medial Golgi. Interacts with members of the p24 cargo receptors.
CC       Interacts with CNIH and the cytoplasmic domain of transmembrane
CC       TGFA, prior its transit in the trans-Golgi. Does not interact with
CC       GM130. Interacts with KCTD5 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Lipid-anchor.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99JX3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99JX3-2; Sequence=VSP_011301;
CC   -!- PTM: Myristoylated. Myristoylation is essential for the Golgi
CC       targeting (By similarity).
CC   -!- PTM: Palmitoylated (By similarity).
CC   -!- PTM: Phosphorylated in mitotic cells (By similarity).
CC   -!- SIMILARITY: Belongs to the GORASP family.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
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DR   EMBL; AK033413; BAC28276.1; -; mRNA.
DR   EMBL; AK077683; BAC36954.1; -; mRNA.
DR   EMBL; AK077706; BAC36969.1; -; mRNA.
DR   EMBL; AK148337; BAE28492.1; -; mRNA.
DR   EMBL; AK151843; BAE30735.1; -; mRNA.
DR   EMBL; AK152475; BAE31249.1; -; mRNA.
DR   EMBL; AK152544; BAE31299.1; -; mRNA.
DR   EMBL; AK152603; BAE31351.1; -; mRNA.
DR   EMBL; AK153049; BAE31677.1; -; mRNA.
DR   EMBL; AK169382; BAE41129.1; -; mRNA.
DR   EMBL; BC005600; AAH05600.1; -; mRNA.
DR   EMBL; BC016455; AAH16455.1; -; mRNA.
DR   IPI; IPI00165716; -.
DR   IPI; IPI00461744; -.
DR   RefSeq; NP_081628.3; NM_027352.4.
DR   UniGene; Mm.271950; -.
DR   UniGene; Mm.470827; -.
DR   ProteinModelPortal; Q99JX3; -.
DR   SMR; Q99JX3; 14-170.
DR   STRING; Q99JX3; -.
DR   PhosphoSite; Q99JX3; -.
DR   PRIDE; Q99JX3; -.
DR   Ensembl; ENSMUST00000028509; ENSMUSP00000028509; ENSMUSG00000014959.
DR   GeneID; 70231; -.
DR   KEGG; mmu:70231; -.
DR   UCSC; uc008jzn.1; mouse.
DR   CTD; 70231; -.
DR   MGI; MGI:2135962; Gorasp2.
DR   GeneTree; ENSGT00390000008686; -.
DR   HOGENOM; HBG713939; -.
DR   HOVERGEN; HBG051826; -.
DR   InParanoid; Q99JX3; -.
DR   OMA; PELVNPG; -.
DR   PhylomeDB; Q99JX3; -.
DR   NextBio; 331212; -.
DR   ArrayExpress; Q99JX3; -.
DR   Bgee; Q99JX3; -.
DR   CleanEx; MM_GORASP2; -.
DR   Genevestigator; Q99JX3; -.
DR   GermOnline; ENSMUSG00000014959; Mus musculus.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR007583; GRASP55_65.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   PANTHER; PTHR12893; GRASP55_65; 1.
DR   Pfam; PF04495; GRASP55_65; 2.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 2.
DR   PROSITE; PS50106; PDZ; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Golgi apparatus; Lipoprotein; Membrane;
KW   Methylation; Myristate; Palmitate; Phosphoprotein.
FT   INIT_MET      1      1       Removed (Probable).
FT   CHAIN         2    451       Golgi reassembly-stacking protein 2.
FT                                /FTId=PRO_0000087546.
FT   DOMAIN        5     75       PDZ.
FT   COMPBIAS    278    377       Pro-rich.
FT   MOD_RES      30     30       Omega-N-methylated arginine (By
FT                                similarity).
FT   MOD_RES      47     47       Omega-N-methylated arginine (By
FT                                similarity).
FT   MOD_RES     214    214       Phosphoserine (By similarity).
FT   MOD_RES     222    222       Phosphothreonine (By similarity).
FT   MOD_RES     225    225       Phosphothreonine; by MAPK (By
FT                                similarity).
FT   MOD_RES     411    411       Phosphoserine.
FT   MOD_RES     417    417       Phosphothreonine (By similarity).
FT   MOD_RES     432    432       Phosphoserine.
FT   MOD_RES     435    435       Phosphothreonine (By similarity).
FT   MOD_RES     448    448       Phosphoserine (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (Probable).
FT   VAR_SEQ       1     68       Missing (in isoform 2).
FT                                /FTId=VSP_011301.
FT   CONFLICT     93     93       Q -> L (in Ref. 3; AAH16455).
FT   CONFLICT    352    352       P -> L (in Ref. 2; BAC28276).
SQ   SEQUENCE   451 AA;  47038 MW;  7E37234E827B459A CRC64;
     MGSSQSVEIP GGGTEGYHVL RVQENSPGHR AGLEPFFDFI VSINGSRLNK DNDTLKDLLK
     ANVEKPVKML IYSSKTLELR EASVTPSNLW GGQGLLGVSI RFCSFDGANE NVWHVLEVES
     NSPAALAGLR PHSDYIIGAD TVMNESEDLF SLIETHEAKP LKLYVYNTDT DNCREVIITP
     NSAWGGEGSL GCGIGYGYLH RIPTRPFEEG KKISLPGQMT GTPITPLKDG FTEVQLSSVS
     PPSLSPPGTT GVEQSLSGLS ISSAPPAVSN VLSTGVPTVP LLPPQVNQSL ASMPPMNPAT
     TLPSLMPLSA GLPSLPNLPS LSNFNLPAPH IMPGVGLPEL GSPGLPPLPS LPPRNLPGIA
     PLPMLSDFLP SFPLVPEGSS AASAGEPLSS LPAMGPPSDP VMTTAKADAS SLTVDVTSPA
     SKVPTTVEDR VSDCTPAVEK PVSDADASEP S
//
ID   LPP3_MOUSE              Reviewed;         312 AA.
AC   Q99JY8; Q3TVM4; Q3TXR7; Q8BTB7;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Lipid phosphate phosphohydrolase 3;
DE            EC=3.1.3.4;
DE   AltName: Full=PAP2-beta;
DE   AltName: Full=Phosphatidate phosphohydrolase type 2b;
DE   AltName: Full=Phosphatidic acid phosphatase 2b;
DE            Short=PAP-2b;
DE            Short=PAP2b;
GN   Name=Ppap2b; Synonyms=Lpp3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 283-293, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   FUNCTION, AND DISEASE.
RX   PubMed=12925589; DOI=10.1242/dev.00635;
RA   Escalante-Alcalde D., Hernandez L., Le Stunff H., Maeda R., Lee H.-S.,
RA   Cheng G. Jr., Sciorra V.A., Daar I., Spiegel S., Morris A.J.,
RA   Stewart C.L.;
RT   "The lipid phosphatase LPP3 regulates extra-embryonic vasculogenesis
RT   and axis patterning.";
RL   Development 130:4623-4637(2003).
CC   -!- FUNCTION: Catalyzes the conversion of phosphatidic acid (PA) to
CC       diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic
CC       acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1-
CC       phosphate (S-1-P) (By similarity). Essential to the formation of
CC       the chorioallantoic placenta and extraembryonic vasculature. Also
CC       mediates gastrulation and axis formation, probably by regulating
CC       the Wnt signaling pathway.
CC   -!- CATALYTIC ACTIVITY: A 1,2-diacylglycerol 3-phosphate + H(2)O = a
CC       1,2-diacyl-sn-glycerol + phosphate.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- DISEASE: Note=Ppap2b deficient embryos fail to form a
CC       chorioallantoic placenta and yolk sac vasculature. A subset of
CC       embryos also show a shortening of the anterior-posterior axis and
CC       frequent duplication of axial structures. Loss of Ppap2b results
CC       in a marked increase in beta-catenin-mediated T-cell factor (TCF)
CC       transcription.
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK159136; BAE34848.1; -; mRNA.
DR   EMBL; AK160056; BAE35594.1; -; mRNA.
DR   EMBL; BC005558; AAH05558.1; -; mRNA.
DR   IPI; IPI00115626; -.
DR   RefSeq; NP_542122.1; NM_080555.2.
DR   UniGene; Mm.348326; -.
DR   ProteinModelPortal; Q99JY8; -.
DR   SMR; Q99JY8; 142-271.
DR   STRING; Q99JY8; -.
DR   PhosphoSite; Q99JY8; -.
DR   PRIDE; Q99JY8; -.
DR   Ensembl; ENSMUST00000064139; ENSMUSP00000065719; ENSMUSG00000028517.
DR   GeneID; 67916; -.
DR   KEGG; mmu:67916; -.
DR   UCSC; uc008tye.1; mouse.
DR   CTD; 67916; -.
DR   MGI; MGI:1915166; Ppap2b.
DR   eggNOG; roNOG07493; -.
DR   GeneTree; ENSGT00550000074203; -.
DR   HOGENOM; HBG403182; -.
DR   HOVERGEN; HBG002048; -.
DR   InParanoid; Q99JY8; -.
DR   OMA; PESKNGG; -.
DR   OrthoDB; EOG40CHHS; -.
DR   PhylomeDB; Q99JY8; -.
DR   BRENDA; 3.1.3.4; 244.
DR   NextBio; 325938; -.
DR   ArrayExpress; Q99JY8; -.
DR   Bgee; Q99JY8; -.
DR   CleanEx; MM_PPAP2B; -.
DR   Genevestigator; Q99JY8; -.
DR   GermOnline; ENSMUSG00000028517; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042577; F:lipid phosphatase activity; IMP:MGI.
DR   GO; GO:0008195; F:phosphatidate phosphatase activity; IEA:EC.
DR   GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR   GO; GO:0060070; P:canonical Wnt receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:BHF-UCL.
DR   GO; GO:0006644; P:phospholipid metabolic process; IMP:MGI.
DR   GO; GO:0051091; P:positive regulation of transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
DR   GO; GO:0030111; P:regulation of Wnt receptor signaling pathway; IDA:MGI.
DR   InterPro; IPR016118; P_Acid_Pase/Cl_peroxidase_N.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   Gene3D; G3DSA:1.20.144.10; P_Acid_Pase/Cl_peroxidase_N; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; AcPase_VanPerase; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Direct protein sequencing;
KW   Endoplasmic reticulum; Glycoprotein; Hydrolase; Membrane;
KW   Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    312       Lipid phosphate phosphohydrolase 3.
FT                                /FTId=PRO_0000220913.
FT   TOPO_DOM      1     33       Cytoplasmic (Potential).
FT   TRANSMEM     34     54       Helical; (Potential).
FT   TOPO_DOM     55     85       Lumenal (Potential).
FT   TRANSMEM     86    106       Helical; (Potential).
FT   TOPO_DOM    107    123       Cytoplasmic (Potential).
FT   TRANSMEM    124    144       Helical; (Potential).
FT   TOPO_DOM    145    194       Lumenal (Potential).
FT   TRANSMEM    195    215       Helical; (Potential).
FT   TOPO_DOM    216    226       Cytoplasmic (Potential).
FT   TRANSMEM    227    247       Helical; (Potential).
FT   TOPO_DOM    248    258       Lumenal (Potential).
FT   TRANSMEM    259    279       Helical; (Potential).
FT   TOPO_DOM    280    312       Cytoplasmic (Potential).
FT   MOD_RES      19     19       Phosphoserine (By similarity).
FT   MOD_RES     110    110       Phosphotyrosine (By similarity).
FT   MOD_RES     298    298       Phosphoserine (By similarity).
FT   CARBOHYD    171    171       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    187    187       S -> C (in Ref. 1; BAE34848).
SQ   SEQUENCE   312 AA;  35216 MW;  D782986E04B57D7D CRC64;
     MQSYKYDKAI VPESKNGGSP ALNNNPRKGG SKRVLLICLD LFCLFMAALP FLIIETSTIK
     PYRRGFYCND ESIKYPLKVS ETINDAVLCA VGIVIAILAI ITGEFYRIYY LKEKSRSTTQ
     NPYVAALYKQ VGCFLFGCAI SQSFTDIAKV SIGRLRPHFL SVCDPDFSQI NCSEGYIQNY
     RCRGEDSKVQ EARKSFFSGH ASFSMFTMLY LVLYLQARFT WRGARLLRPL LQFTLLMMAF
     YTGLSRVSDY KHHPSDVLAG FAQGALVACC IVFFVSDLFK TKTSLSLPAP AIRREILSPV
     DIIDRNNHHN MV
//
ID   ARP3_MOUSE              Reviewed;         418 AA.
AC   Q99JY9; Q9DC56;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Actin-related protein 3;
DE   AltName: Full=Actin-like protein 3;
GN   Name=Actr3; Synonyms=Arp3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Lung, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 103-123 AND 199-219, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-418, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-418, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Functions as ATP-binding component of the Arp2/3 complex
CC       which is involved in regulation of actin polymerization and
CC       together with an activating nucleation-promoting factor (NPF)
CC       mediates the formation of branched actin networks. Seems to
CC       contact the pointed end of the daughter actin filament (By
CC       similarity).
CC   -!- SUBUNIT: Component of the Arp2/3 complex composed of ARP2, ARP3,
CC       ARPC1B, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-
CC       ARC and ARPC5/p16-ARC. Interacts with WHDC1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Cell projection (By similarity).
CC   -!- SIMILARITY: Belongs to the actin family. ARP3 subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK004554; BAB23368.1; -; mRNA.
DR   EMBL; AK083343; BAC38876.1; -; mRNA.
DR   EMBL; BC005557; AAH05557.1; -; mRNA.
DR   EMBL; BC080806; AAH80806.1; -; mRNA.
DR   IPI; IPI00115627; -.
DR   RefSeq; NP_076224.1; NM_023735.1.
DR   UniGene; Mm.183102; -.
DR   ProteinModelPortal; Q99JY9; -.
DR   SMR; Q99JY9; 3-417.
DR   STRING; Q99JY9; -.
DR   PRIDE; Q99JY9; -.
DR   Ensembl; ENSMUST00000027579; ENSMUSP00000027579; ENSMUSG00000026341.
DR   GeneID; 74117; -.
DR   KEGG; mmu:74117; -.
DR   UCSC; uc007cke.1; mouse.
DR   CTD; 74117; -.
DR   MGI; MGI:1921367; Actr3.
DR   HOGENOM; HBG559892; -.
DR   HOVERGEN; HBG003771; -.
DR   InParanoid; Q99JY9; -.
DR   OMA; KYPIRHG; -.
DR   OrthoDB; EOG4XKV6W; -.
DR   PhylomeDB; Q99JY9; -.
DR   NextBio; 339820; -.
DR   ArrayExpress; Q99JY9; -.
DR   Bgee; Q99JY9; -.
DR   CleanEx; MM_ACTR3; -.
DR   Genevestigator; Q99JY9; -.
DR   GermOnline; ENSMUSG00000026341; Mus musculus.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004000; Actin-like.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR015623; Arp3.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   PANTHER; PTHR11937:SF31; Arp3; 1.
DR   Pfam; PF00022; Actin; 1.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; ATP-binding; Cell projection; Cytoplasm;
KW   Cytoskeleton; Direct protein sequencing; Nucleotide-binding;
KW   Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    418       Actin-related protein 3.
FT                                /FTId=PRO_0000089080.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      16     16       Phosphotyrosine (By similarity).
FT   MOD_RES     202    202       Phosphotyrosine (By similarity).
FT   MOD_RES     231    231       Phosphotyrosine (By similarity).
FT   MOD_RES     240    240       N6-acetyllysine (By similarity).
FT   MOD_RES     244    244       N6-acetyllysine (By similarity).
FT   MOD_RES     251    251       N6-acetyllysine (By similarity).
FT   MOD_RES     254    254       N6-acetyllysine (By similarity).
FT   MOD_RES     418    418       Phosphoserine.
FT   CONFLICT    176    176       H -> P (in Ref. 1; BAB23368).
SQ   SEQUENCE   418 AA;  47357 MW;  806FED7A08ABA455 CRC64;
     MAGRLPACVV DCGTGYTKLG YAGNTEPQFI IPSCIAIKES AKVGDQAQRR VMKGVDDLDF
     FIGDEAIEKP TYATKWPIRH GIVEDWDLME RFMEQVIFKY LRAEPEDHYF LLTEPPLNTP
     ENREYTAEIM FESFNVPGLY IAVQAVLALA ASWTSRQVGE RTLTGTVIDS GDGVTHVIPV
     AEGYVIGSCI KHIPIAGRDI TYFIQQLLRD REVGIPPEQS LETAKAVKER YSYVCPDLVK
     EFNKYDTDGS KWIKQYTGVN AISKKEFSID VGYERFLGPE IFFHPEFANP DFTQPISEVV
     DEVIQNCPID VRRPLYKNIV LSGGSTMFRD FGRRLQRDLK RTVDARLKLS EELSGGRLKP
     KPIDVQVITH HMQRYAVWFG GSMLASTPEF YQVCHTKKDY EEIGPSICRH NPVFGVMS
//
ID   NLGN1_MOUSE             Reviewed;         843 AA.
AC   Q99K10;
DT   23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2003, sequence version 2.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Neuroligin-1;
DE   Flags: Precursor;
GN   Name=Nlgn1; Synonyms=Kiaa1070;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=21226491; PubMed=11329178; DOI=10.1002/glia.1050;
RA   Gilbert M., Smith J., Roskams A.J., Auld V.J.;
RT   "Neuroligin 3 is a vertebrate gliotactin expressed in the olfactory
RT   ensheathing glia, a growth-promoting class of macroglia.";
RL   Glia 34:151-164(2001).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 39-635 IN COMPLEX WITH NRX1B,
RP   DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-109 AND ASN-547.
RX   PubMed=18084303; DOI=10.1038/nsmb1350;
RA   Chen X., Liu H., Shim A.H., Focia P.J., He X.;
RT   "Structural basis for synaptic adhesion mediated by neuroligin-
RT   neurexin interactions.";
RL   Nat. Struct. Mol. Biol. 15:50-56(2008).
CC   -!- FUNCTION: Neuronal cell surface protein thought to be involved in
CC       cell-cell-interactions by forming intercellular junctions through
CC       binding to beta-neurexins. Seems to play role in formation or
CC       maintenance of synaptic junctions. In vitro, triggers the de novo
CC       formation of presynaptic structures (By similarity). May be
CC       involved in specification of excitatory synapses.
CC   -!- SUBUNIT: Interacts with neurexin 1-beta, neurexin 2-beta and
CC       neurexin 3-beta, and through its C-terminus with DLG4/PSD-95 third
CC       PDZ domain. Interacts with AIP1 and PDZRN3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein (By similarity). Cell junction, synapse (By similarity).
CC       Cell junction, synapse, postsynaptic cell membrane, postsynaptic
CC       density (By similarity). Note=Enriched in synaptic plasma
CC       membranes and clustered in synaptic clefts and postsynaptic
CC       densities (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99K10-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q99K10-2; Sequence=VSP_007528, VSP_007529, VSP_007530;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in olfactory bulb.
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65715.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK122433; BAC65715.1; ALT_INIT; mRNA.
DR   EMBL; BC005523; AAH05523.1; -; mRNA.
DR   IPI; IPI00309113; -.
DR   IPI; IPI00309114; -.
DR   RefSeq; NP_619607.2; NM_138666.3.
DR   UniGene; Mm.316080; -.
DR   UniGene; Mm.478636; -.
DR   PDB; 3B3Q; X-ray; 2.40 A; A/B=46-635.
DR   PDBsum; 3B3Q; -.
DR   ProteinModelPortal; Q99K10; -.
DR   SMR; Q99K10; 52-631.
DR   DIP; DIP-32027N; -.
DR   STRING; Q99K10; -.
DR   MEROPS; S09.994; -.
DR   PhosphoSite; Q99K10; -.
DR   PRIDE; Q99K10; -.
DR   Ensembl; ENSMUST00000075054; ENSMUSP00000074565; ENSMUSG00000063887.
DR   Ensembl; ENSMUST00000108308; ENSMUSP00000103944; ENSMUSG00000063887.
DR   GeneID; 192167; -.
DR   KEGG; mmu:192167; -.
DR   UCSC; uc008otc.1; mouse.
DR   CTD; 192167; -.
DR   MGI; MGI:2179435; Nlgn1.
DR   GeneTree; ENSGT00600000084208; -.
DR   HOGENOM; HBG716688; -.
DR   HOVERGEN; HBG008839; -.
DR   InParanoid; Q99K10; -.
DR   OMA; TDITLRP; -.
DR   OrthoDB; EOG4CZBF6; -.
DR   PhylomeDB; Q99K10; -.
DR   NextBio; 371168; -.
DR   ArrayExpress; Q99K10; -.
DR   Bgee; Q99K10; -.
DR   CleanEx; MM_NLGN1; -.
DR   Genevestigator; Q99K10; -.
DR   GermOnline; ENSMUSG00000063887; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005887; C:integral to plasma membrane; IMP:UniProtKB.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042043; F:neurexin binding; IMP:UniProtKB.
DR   GO; GO:0016339; P:calcium-dependent cell-cell adhesion; ISS:UniProtKB.
DR   GO; GO:0045664; P:regulation of neuron differentiation; IDA:UniProtKB.
DR   GO; GO:0002087; P:regulation of respiratory gaseous exchange by neurological system process; IGI:MGI.
DR   GO; GO:0050804; P:regulation of synaptic transmission; IGI:MGI.
DR   GO; GO:0007416; P:synapse assembly; IDA:UniProtKB.
DR   GO; GO:0016080; P:synaptic vesicle targeting; IMP:UniProtKB.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   InterPro; IPR000460; Neuroligin.
DR   PANTHER; PTHR11559; CarbesteraseB; 1.
DR   Pfam; PF00135; COesterase; 1.
DR   PRINTS; PR01090; NEUROLIGIN.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell adhesion; Cell junction;
KW   Cell membrane; Disulfide bond; Glycoprotein; Membrane;
KW   Postsynaptic cell membrane; Signal; Synapse; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     45       Potential.
FT   CHAIN        46    843       Neuroligin-1.
FT                                /FTId=PRO_0000008641.
FT   TOPO_DOM     46    697       Extracellular (Potential).
FT   TRANSMEM    698    718       Helical; (Potential).
FT   TOPO_DOM    719    843       Cytoplasmic (Potential).
FT   CARBOHYD    109    109       N-linked (GlcNAc...) (complex).
FT   CARBOHYD    303    303       N-linked (GlcNAc...) (complex) (By
FT                                similarity).
FT   CARBOHYD    343    343       N-linked (GlcNAc...) (complex) (By
FT                                similarity).
FT   CARBOHYD    547    547       N-linked (GlcNAc...).
FT   CARBOHYD    683    683       O-linked (GalNAc...) (By similarity).
FT   CARBOHYD    686    686       O-linked (GalNAc...) (By similarity).
FT   DISULFID    117    153
FT   DISULFID    342    353
FT   DISULFID    512    546
FT   VAR_SEQ     165    184       Missing (in isoform 2).
FT                                /FTId=VSP_007528.
FT   VAR_SEQ     236    269       GFLSTGDQAAKGNYGLLDLIQALRWTSENIGFFG -> EKE
FT                                TIKETISVALQALRTKGGGFIPKQATYKRCE (in
FT                                isoform 2).
FT                                /FTId=VSP_007529.
FT   VAR_SEQ     270    843       Missing (in isoform 2).
FT                                /FTId=VSP_007530.
FT   STRAND       54     57
FT   STRAND       60     63
FT   STRAND       65     67
FT   STRAND       77     84
FT   HELIX        91     93
FT   STRAND      105    109
FT   STRAND      122    124
FT   TURN        128    130
FT   HELIX       133    137
FT   HELIX       139    145
FT   STRAND      147    149
FT   STRAND      155    160
FT   STRAND      193    198
FT   STRAND      202    206
FT   HELIX       209    211
FT   HELIX       215    221
FT   STRAND      224    228
FT   HELIX       233    237
FT   STRAND      241    245
FT   HELIX       249    264
FT   HELIX       266    268
FT   STRAND      270    280
FT   HELIX       282    290
FT   TURN        297    308
FT   STRAND      310    316
FT   STRAND      319    321
FT   STRAND      324    327
FT   HELIX       329    339
FT   HELIX       347    356
FT   HELIX       359    363
FT   STRAND      375    377
FT   STRAND      382    385
FT   HELIX       389    395
FT   STRAND      402    408
FT   TURN        409    412
FT   HELIX       413    416
FT   HELIX       417    419
FT   STRAND      422    424
FT   HELIX       428    443
FT   HELIX       451    459
FT   HELIX       469    484
FT   HELIX       486    498
FT   STRAND      503    508
FT   TURN        525    528
FT   HELIX       529    532
FT   TURN        536    538
FT   STRAND      542    544
FT   HELIX       550    569
FT   STRAND      572    576
FT   TURN        600    602
FT   STRAND      604    611
FT   STRAND      613    617
FT   HELIX       620    627
FT   HELIX       630    633
SQ   SEQUENCE   843 AA;  94149 MW;  69E50709CF7D2E1F CRC64;
     MALPRCMWPN YVWRAMMACV VHRGSGAPLT LCLLGCLLQT FHVLSQKLDD VDPLVTTNFG
     KIRGIKKELN NEILGPVIQF LGVPYAAPPT GEHRFQPPEP PSPWSDIRNA TQFAPVCPQN
     IIDGRLPEVM LPVWFTNNLD VVSSYVQDQS EDCLYLNIYV PTEDGPLTKK HTDDLGDNDG
     AEDEDIRDSG GPKPVMVYIH GGSYMEGTGN LYDGSVLASY GNVIVITVNY RLGVLGFLST
     GDQAAKGNYG LLDLIQALRW TSENIGFFGG DPLRITVFGS GAGGSCVNLL TLSHYSEGNR
     WSNSTKGLFQ RAIAQSGTAL SSWAVSFQPA KYARILATKV GCNVSDTVEL VECLQKKPYK
     ELVDQDVQPA RYHIAFGPVI DGDVIPDDPQ ILMEQGEFLN YDIMLGVNQG EGLKFVENIV
     DSDDGVSASD FDFAVSNFVD NLYGYPEGKD VLRETIKFMY TDWADRHNPE TRRKTLLALF
     TDHQWVAPAV ATADLHSNFG SPTYFYAFYH HCQTDQVPAW ADAAHGDEVP YVLGIPMIGP
     TELFPCNFSK NDVMLSAVVM TYWTNFAKTG DPNQPVPQDT KFIHTKPNRF EEVAWTRYSQ
     KDQLYLHIGL KPRVKEHYRA NKVNLWLELV PHLHNLNDIS QYTSTTTKVP STDITLRPTR
     KNSTPVTSAF PTAKQDDPKQ QPSPFSVDQR DYSTELSVTI AVGASLLFLN ILAFAALYYK
     KDKRRHDVHR RCSPQRTTTN DLTHAPEEEI MSLQMKHTDL DHECESIHPH EVVLRTACPP
     DYTLAMRRSP DDIPLMTPNT ITMIPNTIPG IQPLHTFNTF TGGQNNTLPH PHPHPHSHST
     TRV
//
ID   ARFG2_MOUSE             Reviewed;         520 AA.
AC   Q99K28; Q9D758; Q9JIH1;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=ADP-ribosylation factor GTPase-activating protein 2;
DE            Short=ARF GAP 2;
DE   AltName: Full=GTPase-activating protein ZNF289;
DE   AltName: Full=Zinc finger protein 289;
GN   Name=Arfgap2; Synonyms=Zfp289, Znf289;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP   AND DEVELOPMENTAL STAGE.
RC   TISSUE=Mammary epithelium;
RX   MEDLINE=21192231; PubMed=11278321; DOI=10.1074/jbc.M006931200;
RA   Singh J., Itahana Y., Parrinello S., Murata K., Desprez P.-Y.;
RT   "Molecular cloning and characterization of a zinc finger protein
RT   involved in Id-1-stimulated mammary edithelial cell growth.";
RL   J. Biol. Chem. 276:11852-11858(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Amnion, Bone marrow, and Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation
CC       factor 1 (ARF1). May regulate coatomer-mediated protein transport
CC       from the Golgi complex to the endoplasmic reticulum. Hydrolysis of
CC       ARF1-bound GTP may lead to dissociation of coatomer from Golgi-
CC       derived membranes to allow fusion with target membranes (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with the coatomer complex. Interacts with the
CC       C-terminal appendage domain of COPG (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus
CC       membrane; Peripheral membrane protein; Cytoplasmic side (By
CC       similarity). Note=Also found on peripheral punctate structures
CC       likely to be endoplasmic reticulum-Golgi intermediate compartment
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99K28-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99K28-2; Sequence=VSP_023305;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in liver, heart and kidney.
CC       Low expression in skeletal muscle and spleen.
CC   -!- DEVELOPMENTAL STAGE: High levels in mammary glands of virgin mice
CC       and in mammary glands of pregnant mice associated with extensive
CC       proliferation of ductal cells and lobulo-alveolar development.
CC       Expression declines at the beginning of lactation when the glands
CC       fully differentiate. No expression after day 2 of lactation until
CC       day 21. Expression may be controlled by ID1.
CC   -!- SIMILARITY: Contains 1 Arf-GAP domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF229439; AAF91258.1; -; mRNA.
DR   EMBL; AK009565; BAB26362.1; -; mRNA.
DR   EMBL; AK168489; BAE40376.1; -; mRNA.
DR   EMBL; AK169144; BAE40923.1; -; mRNA.
DR   EMBL; AK149837; BAE29114.1; -; mRNA.
DR   EMBL; AL732478; CAM24080.1; -; Genomic_DNA.
DR   EMBL; AL732478; CAM24081.1; -; Genomic_DNA.
DR   EMBL; BC005495; AAH05495.1; -; mRNA.
DR   IPI; IPI00109656; -.
DR   IPI; IPI00120571; -.
DR   RefSeq; NP_001159496.1; NM_001166024.1.
DR   RefSeq; NP_076343.2; NM_023854.2.
DR   UniGene; Mm.386861; -.
DR   UniGene; Mm.43636; -.
DR   UniGene; Mm.458847; -.
DR   HSSP; Q9NP61; 2CRW.
DR   ProteinModelPortal; Q99K28; -.
DR   SMR; Q99K28; 5-126.
DR   STRING; Q99K28; -.
DR   PhosphoSite; Q99K28; -.
DR   PRIDE; Q99K28; -.
DR   Ensembl; ENSMUST00000028691; ENSMUSP00000028691; ENSMUSG00000027255.
DR   Ensembl; ENSMUST00000080008; ENSMUSP00000078920; ENSMUSG00000027255.
DR   GeneID; 77038; -.
DR   KEGG; mmu:77038; -.
DR   UCSC; uc008kvq.1; mouse.
DR   CTD; 77038; -.
DR   MGI; MGI:1924288; Arfgap2.
DR   GeneTree; ENSGT00390000005436; -.
DR   HOVERGEN; HBG050563; -.
DR   OMA; DTDATWG; -.
DR   OrthoDB; EOG447FTM; -.
DR   PhylomeDB; Q99K28; -.
DR   NextBio; 346350; -.
DR   ArrayExpress; Q99K28; -.
DR   Bgee; Q99K28; -.
DR   Genevestigator; Q99K28; -.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001164; ArfGAP.
DR   Pfam; PF01412; ArfGap; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SUPFAM; SSF57863; ArfGAP; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; ER-Golgi transport;
KW   Golgi apparatus; GTPase activation; Membrane; Metal-binding;
KW   Phosphoprotein; Protein transport; Transport; Zinc; Zinc-finger.
FT   CHAIN         1    520       ADP-ribosylation factor GTPase-activating
FT                                protein 2.
FT                                /FTId=PRO_0000278469.
FT   DOMAIN       11    127       Arf-GAP.
FT   ZN_FING      26     49       C4-type.
FT   REGION       97    520       Required for interaction with coatomer
FT                                (By similarity).
FT   COILED      241    307       Potential.
FT   MOD_RES     145    145       Phosphoserine.
FT   MOD_RES     336    336       Phosphoserine.
FT   MOD_RES     431    431       Phosphoserine (By similarity).
FT   MOD_RES     497    497       Phosphoserine (By similarity).
FT   VAR_SEQ     206    206       E -> ESMYLSAKGPSCTRE (in isoform 2).
FT                                /FTId=VSP_023305.
FT   CONFLICT    467    467       N -> D (in Ref. 1; AAF91258).
SQ   SEQUENCE   520 AA;  56598 MW;  9B06038602F15014 CRC64;
     MAASPSKTEI QTIFKRLRAI PTNKACFDCG AKSPSWASIT YGVFLCIDCS GVHRSLGVHL
     SFIRSTELDS NWSWLQLRCM QVGGNANATA FFRQHGCMAN DANTKYTSRA AQMYREKIRQ
     LGSAALTRHG TDLWIDSMNS APSHSPEKKD SDFFTEHTQA PAWDTAATDP SGTQQPALPS
     ESSSLAQPEQ GPNTDLLGTS PQASLELKSS IIGKKKPAAA KKGLGAKKGL GAQKVSNQSF
     TEIERQAQVA EKLREQQAAD AKKQAEESMV ASMRLAYQEL QIDRKKEEKK LQNLEGKKRE
     QAERLGMGLV SRSSISHSVL SEMQMIEQET PLSAKSSRSQ LDLFDDVGTF ASGPPKYKDN
     PFSLGETFGS RWDSDAAWGM DRVEEKEPEV TISSIRPISE RTASRREVET RSSGLESSEA
     RQKFAGAKAI SSDMFFGREV DSEYEARSRL QQLSGSSAIS SSDLFGNMDG AHGGGTVSLG
     NVLPTADIAQ FKQGVKSVAG KMAVLANGVM NSLQDRYGSY
//
ID   ES8L2_MOUSE             Reviewed;         729 AA.
AC   Q99K30; Q91VT7;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Epidermal growth factor receptor kinase substrate 8-like protein 2;
DE            Short=EPS8-like protein 2;
DE   AltName: Full=Epidermal growth factor receptor pathway substrate 8-related protein 2;
DE            Short=EPS8-related protein 2;
GN   Name=Eps8l2; Synonyms=Eps8r2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   TISSUE SPECIFICITY.
RX   PubMed=14565974; DOI=10.1091/mbc.E03-06-0427;
RA   Offenhaeuser N., Borgonovo A., Disanza A., Romano P., Ponzanelli I.,
RA   Iannolo G., Di Fiore P.P., Scita G.;
RT   "The eps8 family of proteins links growth factor stimulation to actin
RT   reorganization generating functional redundancy in the Ras/Rac
RT   pathway.";
RL   Mol. Biol. Cell 15:91-98(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242 AND SER-483, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Stimulates guanine exchange activity of SOS1. May play a
CC       role in membrane ruffling and remodeling of the actin cytoskeleton
CC       (By similarity).
CC   -!- SUBUNIT: Interacts with ABI1. Part of a complex that contains
CC       SOS1, ABI1 and EPS8L2. Associates with F-actin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99K30-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99K30-2; Sequence=VSP_019093, VSP_019094;
CC   -!- TISSUE SPECIFICITY: Detected in fetal kidney, adrenal gland,
CC       salivary gland, stomach, gut, cartilage and skin. Detected in
CC       adult ovary, placenta, skin, adrenal gland, salivary gland,
CC       kidney, intestine and stomach.
CC   -!- SIMILARITY: Belongs to the EPS8 family.
CC   -!- SIMILARITY: Contains 1 PID domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; BC005492; AAH05492.1; -; mRNA.
DR   EMBL; BC009098; AAH09098.1; -; mRNA.
DR   IPI; IPI00115492; -.
DR   IPI; IPI00759947; -.
DR   RefSeq; NP_573454.2; NM_133191.2.
DR   UniGene; Mm.27451; -.
DR   ProteinModelPortal; Q99K30; -.
DR   SMR; Q99K30; 46-175, 498-552, 615-700.
DR   STRING; Q99K30; -.
DR   PhosphoSite; Q99K30; -.
DR   PRIDE; Q99K30; -.
DR   Ensembl; ENSMUST00000026577; ENSMUSP00000026577; ENSMUSG00000025504.
DR   GeneID; 98845; -.
DR   KEGG; mmu:98845; -.
DR   UCSC; uc009kkt.1; mouse.
DR   CTD; 98845; -.
DR   MGI; MGI:2138828; Eps8l2.
DR   eggNOG; roNOG15377; -.
DR   GeneTree; ENSGT00390000003646; -.
DR   HOGENOM; HBG445840; -.
DR   HOVERGEN; HBG003090; -.
DR   InParanoid; Q99K30; -.
DR   OMA; PYNILDV; -.
DR   OrthoDB; EOG4X0MRS; -.
DR   PhylomeDB; Q99K30; -.
DR   NextBio; 353685; -.
DR   ArrayExpress; Q99K30; -.
DR   Bgee; Q99K30; -.
DR   CleanEx; MM_EPS8L2; -.
DR   Genevestigator; Q99K30; -.
DR   GermOnline; ENSMUSG00000025504; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR013625; PTB.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF08416; PTB; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS01179; PID; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Phosphoprotein; SH3 domain.
FT   CHAIN         1    729       Epidermal growth factor receptor kinase
FT                                substrate 8-like protein 2.
FT                                /FTId=PRO_0000239085.
FT   DOMAIN       46    202       PID.
FT   DOMAIN      495    554       SH3.
FT   MOD_RES       8      8       Phosphoserine (By similarity).
FT   MOD_RES      21     21       Phosphoserine (By similarity).
FT   MOD_RES     217    217       Phosphoserine (By similarity).
FT   MOD_RES     242    242       Phosphoserine.
FT   MOD_RES     462    462       Phosphoserine (By similarity).
FT   MOD_RES     483    483       Phosphoserine.
FT   MOD_RES     573    573       Phosphoserine (By similarity).
FT   VAR_SEQ     357    400       IINTCGSPDIARSVSSPLLSTDAVSFLRGHLVPKEMTLWES
FT                                LGE -> VTGAGTGRGRGQQSDPHGFGVEETSAHLSILKLC
FT                                LGSQEATVHP (in isoform 2).
FT                                /FTId=VSP_019093.
FT   VAR_SEQ     401    729       Missing (in isoform 2).
FT                                /FTId=VSP_019094.
FT   CONFLICT    177    177       G -> R (in Ref. 1; AAH09098).
SQ   SEQUENCE   729 AA;  82229 MW;  A11DE82FF2C0BD18 CRC64;
     MSQSASMSCC PGAANGSLGR SDGVPRMSAK DLFEQRKKYS NSNVIMHETS QYHVQHLATF
     IMDKSEAIAS VDDAIRKLVQ LSSKEKVWAQ EVLLQVNDKS LRLLDVESQE ELENFPLPTV
     QHSQTVLNQL RYPSVLLLVC QDSDQNKPDI HFFHCDEVEA ELVQEDIESA LADYRLGKKM
     RPQTLKGHQE KIRQRQSILP PPQSPAPIPF QRQPGDSPQA KNRVGLPLPV PFSEPGYRRR
     ESQDEEPRAV LAQRIEKETQ ILNCTLDDIE WFVARLQKAA EAFKQLNQRK KGKKKNKKGP
     AEGVLTLRAR PPSEGEFVDC FQKTKLAINL LAKLQKHIQN PSAAELVHFL FGPLDLIINT
     CGSPDIARSV SSPLLSTDAV SFLRGHLVPK EMTLWESLGE TWMRPRSEWP REPQVPLYVP
     KFRSGWEPPL DVLQEAPWEV EGLASVPSDQ LTPKNRLSVR HSPKHSLSSE SQAPEDIAPP
     GSSPHANRGY QPTPAMTKYV KILYDFTARN ANELSVLKDE VLEVLEDGRQ WWKLRNRSGQ
     AGYVPCNILA EARQEDVGAP LEQSGQKYWG PASPTHKLPP IFAGNKEELI HHMDEVNDEL
     MKKISHIKTQ PQRNFRVERS QPVHLPLTFE SGPDEVRAWL EAKAFSARIV ENLGILTGPQ
     LFSLNKEELK KVCGEEGSRV YSQLTVQKAF LEKQQSGSEL EKLMSKIRRA EDSYTSQHTS
     PESEGAPHL
//
ID   RRAGC_MOUSE             Reviewed;         398 AA.
AC   Q99K70; A2A7K7; Q3TL69; Q6IQZ6; Q8CFT7; Q9Z124;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Ras-related GTP-binding protein C;
DE            Short=Rag C;
DE            Short=RagC;
DE   AltName: Full=GTPase-interacting protein 2;
DE   AltName: Full=TIB929;
GN   Name=Rragc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6;
RX   PubMed=10660099; DOI=10.1016/S0304-3835(99)00285-2;
RA   Nakaji T., Kataoka T.R., Watabe K., Nishiyama K., Nojima H.,
RA   Shimada Y., Sato F., Matsushima H., Endo Y., Kuroda Y., Kitamura Y.,
RA   Ito A., Maeda S.;
RT   "A new member of the GTPase superfamily that is upregulated in highly
RT   metastatic cells.";
RL   Cancer Lett. 147:139-147(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, Czech II, and FVB/N;
RC   TISSUE=Liver, Mammary gland, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Has guanine nucleotide-binding activity but weak
CC       intrinsic GTPase activity. Probably required for the amino acid-
CC       induced relocalization of mTORC1 to the lysosomes and its
CC       subsequent activation by the GTPase RHEB. This is a crucial step
CC       in the activation of the TOR signaling cascade by amino acids (By
CC       similarity).
CC   -!- SUBUNIT: Forms a heterodimer with RRAGA in a sequence-independent
CC       manner. Binds GTP. Interacts with NOL8 and RRAGB (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Lysosome (By similarity). Note=Predominantly
CC       cytoplasmic. May shuttle between the cytoplasm and nucleus,
CC       depending on the bound nucleotide state of associated RRAGA (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99K70-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99K70-2; Sequence=VSP_052076, VSP_052077;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed most abundantly in kidney.
CC       Moderately expressed in brain, ovary, and testis, and detected at
CC       lower levels in heart, liver, and muscle. Not detected in lung,
CC       spleen, and small intestine. Widely expressed in tumor cells, with
CC       expression being specifically up-regulated in highly metastatic
CC       cells.
CC   -!- SIMILARITY: Belongs to the GTR/RAG GTP-binding protein family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA75671.1; Type=Frameshift; Positions=19, 56, 68, 71;
CC   -----------------------------------------------------------------------
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DR   EMBL; AB017616; BAA75671.1; ALT_FRAME; mRNA.
DR   EMBL; AK159355; BAE35013.1; -; mRNA.
DR   EMBL; AK166658; BAE38923.1; -; mRNA.
DR   EMBL; AL606962; CAM20100.1; -; Genomic_DNA.
DR   EMBL; BC005417; AAH05417.1; -; mRNA.
DR   EMBL; BC037732; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC071245; AAH71245.1; -; mRNA.
DR   IPI; IPI00463574; -.
DR   IPI; IPI00468702; -.
DR   RefSeq; NP_059503.2; NM_017475.2.
DR   UniGene; Mm.220922; -.
DR   UniGene; Mm.473825; -.
DR   ProteinModelPortal; Q99K70; -.
DR   SMR; Q99K70; 60-236.
DR   STRING; Q99K70; -.
DR   PhosphoSite; Q99K70; -.
DR   PRIDE; Q99K70; -.
DR   Ensembl; ENSMUST00000030399; ENSMUSP00000030399; ENSMUSG00000028646.
DR   GeneID; 54170; -.
DR   KEGG; mmu:54170; -.
DR   UCSC; uc008uqm.1; mouse.
DR   CTD; 54170; -.
DR   MGI; MGI:1858751; Rragc.
DR   GeneTree; ENSGT00550000074708; -.
DR   HOGENOM; HBG329490; -.
DR   HOVERGEN; HBG059482; -.
DR   InParanoid; Q99K70; -.
DR   OMA; LKAVTHN; -.
DR   OrthoDB; EOG4CG08D; -.
DR   PhylomeDB; Q99K70; -.
DR   NextBio; 311018; -.
DR   ArrayExpress; Q99K70; -.
DR   Bgee; Q99K70; -.
DR   CleanEx; MM_RRAGC; -.
DR   Genevestigator; Q99K70; -.
DR   GermOnline; ENSMUSG00000028646; Mus musculus.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:HGNC.
DR   GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:HGNC.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   InterPro; IPR006762; Gtr1_RagA.
DR   PANTHER; PTHR11259; Gtr1_RagA; 1.
DR   Pfam; PF04670; Gtr1_RagA; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; GTP-binding; Lysosome;
KW   Nucleotide-binding; Nucleus; Phosphoprotein.
FT   CHAIN         1    398       Ras-related GTP-binding protein C.
FT                                /FTId=PRO_0000239952.
FT   NP_BIND      67     74       GTP (By similarity).
FT   NP_BIND     115    119       GTP (By similarity).
FT   NP_BIND     177    180       GTP (By similarity).
FT   MOD_RES      94     94       Phosphoserine (By similarity).
FT   VAR_SEQ     147    182       DDYMEALTRLHITVSKAYKVNPDMNFEVFIHKVDGL -> V
FT                                VRHDGVCTSLVAKRQRKGGKLFVSFVMCLKLLSFQ (in
FT                                isoform 2).
FT                                /FTId=VSP_052076.
FT   VAR_SEQ     183    398       Missing (in isoform 2).
FT                                /FTId=VSP_052077.
FT   CONFLICT     19     20       AD -> R (in Ref. 1; BAA75671).
FT   CONFLICT     55     55       G -> R (in Ref. 1; BAA75671).
FT   CONFLICT     56     56       A -> DA (in Ref. 1; BAA75671).
FT   CONFLICT     71     71       S -> H (in Ref. 1; BAA75671).
FT   CONFLICT    376    398       CSHQTSAPSLKALAHNGTPRNAI -> TSCR (in Ref.
FT                                2; BAE38923).
FT   CONFLICT    386    386       K -> R (in Ref. 1; BAA75671).
SQ   SEQUENCE   398 AA;  44121 MW;  094F670E44B37A25 CRC64;
     MSLQYGAEET PLAGSYGAAD SFPKDFGYGV EEEEEEAAAG GGGGAGAGGG CGPGGADSSK
     PRILLMGLRR SGKSSIQKVV FHKMSPNETL FLESTNKIYK DDISNSSFVN FQIWDFPGQM
     DFFDPTFDYE MIFRGTGALI YVIDAQDDYM EALTRLHITV SKAYKVNPDM NFEVFIHKVD
     GLSDDHKIET QRDIHQRAND DLADAGLEKL HLSFYLTSIY DHSIFEAFSK VVQKLIPQLP
     TLENLLNIFI SNSGIEKAFL FDVVSKIYIA TDSSPVDMQS YELCCDMIDV VIDVSCIYGL
     KEDGSGSAYD KESMAIIKLN NTTVLYLKEV TKFLALVCIL REESFERKGL IDYNFHCFRK
     AIHEVFEVGV TSHRSCSHQT SAPSLKALAH NGTPRNAI
//
ID   MED24_MOUSE             Reviewed;         987 AA.
AC   Q99K74; A3KFP0; Q8R004; Q9D277; Q9WVF1;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 24;
DE   AltName: Full=Mediator complex subunit 24;
DE   AltName: Full=Thyroid hormone receptor-associated protein 4;
DE   AltName: Full=Thyroid hormone receptor-associated protein complex 100 kDa component;
DE            Short=Trap100;
DE            Short=mTRAP100;
GN   Name=Med24; Synonyms=D11Ertd307e, Thrap4, Trap100;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH
RP   MED1, AND TISSUE SPECIFICITY.
RX   MEDLINE=99333122; PubMed=10406464; DOI=10.1210/me.13.7.1130;
RA   Zhang J., Fondell J.D.;
RT   "Identification of mouse TRAP100: a transcriptional coregulatory
RT   factor for thyroid hormone and vitamin D receptors.";
RL   Mol. Endocrinol. 13:1130-1140(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=ILS, and ISS;
RX   MEDLINE=21363810; PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Cecum, and Dendritic cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   FUNCTION, INTERACTION WITH MED10, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=12093747; DOI=10.1093/emboj/cdf348;
RA   Ito M., Okano H.J., Darnell R.B., Roeder R.G.;
RT   "The TRAP100 component of the TRAP/Mediator complex is essential in
RT   broad transcriptional events and development.";
RL   EMBO J. 21:3464-3475(2002).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C3H;
RX   MEDLINE=21973491; PubMed=11934987; DOI=10.1126/science.1068943;
RA   Stevens J.L., Cantin G.T., Wang G., Shevchenko A., Shevchenko A.,
RA   Berk A.J.;
RT   "Transcription control by E1A and MAP kinase pathway via Sur2 mediator
RT   subunit.";
RL   Science 296:755-758(2002).
CC   -!- FUNCTION: Component of the Mediator complex, a coactivator
CC       involved in the regulated transcription of nearly all RNA
CC       polymerase II-dependent genes. Mediator functions as a bridge to
CC       convey information from gene-specific regulatory proteins to the
CC       basal RNA polymerase II transcription machinery. Mediator is
CC       recruited to promoters by direct interactions with regulatory
CC       proteins and serves as a scaffold for the assembly of a functional
CC       preinitiation complex with RNA polymerase II and the general
CC       transcription factors (By similarity). Required for basal and
CC       activator-dependent transcription.
CC   -!- SUBUNIT: Component of the Mediator complex, which is composed of
CC       MED1, MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13,
CC       MED13L, MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21,
CC       MED22, MED23, MED24, MED25, MED26, MED27, MED29, MED30, MED31,
CC       CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8
CC       subunits form a distinct module termed the CDK8 module. Mediator
CC       containing the CDK8 module is less active than Mediator lacking
CC       this module in supporting transcriptional activation. Individual
CC       preparations of the Mediator complex lacking one or more distinct
CC       subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC and
CC       TRAP. Interacts with AR (By similarity). Interacts with MED1 and
CC       MED10.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q99K74-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99K74-2; Sequence=VSP_028355, VSP_028356;
CC       Name=3;
CC         IsoId=Q99K74-3; Sequence=VSP_028357, VSP_028358;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in the adrenal gland, brain,
CC       epididymis, heart, kidney, liver, ovary, pancreas, prostate,
CC       skeletal muscle, small intestine, spleen, stomach, testis and
CC       thymus.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout development; expression
CC       levels drop immediately after birth. Strongly expressed throughout
CC       the primitive nervous system, the hepatic primoridium and the
CC       earliest limb buds.
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 24 family.
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DR   EMBL; AF126543; AAD42776.1; -; mRNA.
DR   EMBL; AF483498; AAL90772.1; -; mRNA.
DR   EMBL; AF483499; AAL90773.1; -; mRNA.
DR   EMBL; AK020269; BAB32051.1; -; mRNA.
DR   EMBL; AK154618; BAE32717.1; -; mRNA.
DR   EMBL; AL590963; CAM46193.1; -; Genomic_DNA.
DR   EMBL; BC005409; AAH05409.1; -; mRNA.
DR   IPI; IPI00165717; -.
DR   IPI; IPI00474362; -.
DR   IPI; IPI00857417; -.
DR   RefSeq; NP_035999.2; NM_011869.2.
DR   UniGene; Mm.246493; -.
DR   STRING; Q99K74; -.
DR   PhosphoSite; Q99K74; -.
DR   PRIDE; Q99K74; -.
DR   Ensembl; ENSMUST00000017354; ENSMUSP00000017354; ENSMUSG00000017210.
DR   Ensembl; ENSMUST00000021257; ENSMUSP00000021257; ENSMUSG00000017210.
DR   GeneID; 23989; -.
DR   KEGG; mmu:23989; -.
DR   UCSC; uc007lha.1; mouse.
DR   CTD; 23989; -.
DR   MGI; MGI:1344385; Med24.
DR   eggNOG; roNOG08300; -.
DR   GeneTree; ENSGT00390000016438; -.
DR   HOVERGEN; HBG055588; -.
DR   OrthoDB; EOG4F1X2C; -.
DR   PhylomeDB; Q99K74; -.
DR   NextBio; 303889; -.
DR   ArrayExpress; Q99K74; -.
DR   Bgee; Q99K74; -.
DR   CleanEx; MM_MED24; -.
DR   Genevestigator; Q99K74; -.
DR   GO; GO:0016592; C:mediator complex; IDA:MGI.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; IMP:MGI.
DR   InterPro; IPR021429; Mediator_Med24_N.
DR   Pfam; PF11277; Med24_N; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Nucleus; Phosphoprotein; Repeat;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    987       Mediator of RNA polymerase II
FT                                transcription subunit 24.
FT                                /FTId=PRO_0000305912.
FT   MOTIF       128    132       LXXLL motif 1.
FT   MOTIF       344    348       LXXLL motif 2.
FT   MOTIF       446    450       LXXLL motif 3.
FT   MOTIF       555    559       LXXLL motif 4.
FT   MOTIF       786    790       LXXLL motif 5.
FT   MOTIF       855    859       LXXLL motif 6.
FT   MOD_RES     860    860       Phosphoserine (By similarity).
FT   MOD_RES     871    871       Phosphoserine (By similarity).
FT   VAR_SEQ       1     50       Missing (in isoform 2).
FT                                /FTId=VSP_028355.
FT   VAR_SEQ     187    187       S -> SLHTSQGLGQGGTRANQPTA (in isoform 2).
FT                                /FTId=VSP_028356.
FT   VAR_SEQ     661    758       VVIMNSILEHMCADVLQQTATQIKFPSTGVDTMPYWNLLPP
FT                                KRPIKEVLTDIFAKVLEKGWVDSRSIHILDTLLHMGGVYWF
FT                                CNNLIKELLKETRKEH -> SVPRPRQVCGRESAPPGTNIP
FT                                PHALGLRFPGSRSATTSSSIQAPTSPPCLAAEAVHIQGSWT
FT                                LAPSFAFPYHSLAFLVTHSLSWLSRCLVCVSVSRGF (in
FT                                isoform 3).
FT                                /FTId=VSP_028357.
FT   VAR_SEQ     759    987       Missing (in isoform 3).
FT                                /FTId=VSP_028358.
FT   CONFLICT     26     26       N -> K (in Ref. 3; BAB32051).
FT   CONFLICT    503    503       Q -> H (in Ref. 1; AAD42776).
FT   CONFLICT    541    541       D -> E (in Ref. 1; AAD42776).
FT   CONFLICT    566    566       K -> N (in Ref. 1; AAD42776).
FT   CONFLICT    608    608       K -> N (in Ref. 1; AAD42776).
FT   CONFLICT    699    699       L -> F (in Ref. 1; AAD42776).
FT   CONFLICT    888    888       T -> R (in Ref. 1; AAD42776).
FT   CONFLICT    940    940       S -> T (in Ref. 1; AAD42776).
FT   CONFLICT    963    963       K -> E (in Ref. 1; AAD42776).
FT   CONFLICT    970    970       D -> H (in Ref. 1; AAD42776).
SQ   SEQUENCE   987 AA;  109985 MW;  713C6A02C3C0B294 CRC64;
     MKVVNLKQAI LQAWKERWSD YQWAINMKKF FPKGATWDIL NLAEALLEQA MIGPSPNPLI
     LSYLKYAISS QMVSCSSVLT AISKFDDFSR DLCVQALLDI MDMFCDRLSC HGKAEECIGL
     CRALLSALHW LLRCTAASAE RLQEGLEAGT PAPGEKQLAL CLQCLEKTLS STKNRALLHI
     AKLEEASSWT AIEHSLLKLG EILANLSNPQ LRSQAERCGT LIRSIPSMLS VHSEQLHKTG
     FPTIHALILL EGTMNLTGEM QPLVEQLMMV KRMQHIPTPL FVLEIWKACF VGLIESPEGT
     QELKWTAFTY LKIPQVLVKL KKYFHGEKDF TEDVNCAFEF LLKLTPLLDK ADQRCNCDCT
     NFLLQECNKQ GLLSEVNFAS LVGKRTADRD PQLKSSENAN IQPNPGLILR AEPTVTNILK
     TMDADHSKSP EGLLGVLGHM LSGKSLDLLL AAAAATGKLK SFARKFINLN EFTTHGSGES
     TKTASVRALL FDISFLMLCH VAQTYGSEVI LSESSSGEEV PFFETWMQTC MPEEGKILNP
     DHPCFRPDST KVESLVALLN NSSEMKLVQM KWHEACLSIS AAILEILNAW ENGVLAFESI
     QKITDNIKGK VCSLAVCAVA WLVAHVRMLG LDEREKSLQM IRQLAGPLYS ENTLQFYNER
     VVIMNSILEH MCADVLQQTA TQIKFPSTGV DTMPYWNLLP PKRPIKEVLT DIFAKVLEKG
     WVDSRSIHIL DTLLHMGGVY WFCNNLIKEL LKETRKEHTL RAVQLLYSIF CLDMQQVTLV
     LLGHILPGLL TDSSKWHSLM DPPGTALAKL AVWCALSSYS SHKGQASSRQ KKRHREDIED
     YVSLFPVEDM QPSKLMRLLS SSDDDANILS SPTDRSMNSS LSASQLHTVN MRDPLNRVLA
     NLFLLISSIL GSRTAGPHTQ FVQWFMEECV GCLEQDSRGS ILQFMPFTTV SELVKVSAMS
     SPKVVLAITD LSLPLGRQVA AKAIAAL
//
ID   CD019_MOUSE             Reviewed;         313 AA.
AC   Q99K99; Q8BQG8; Q9DCE0;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 44.
DE   RecName: Full=Uncharacterized protein C4orf19 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104 AND SER-107, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
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DR   EMBL; AK002869; BAB22418.1; -; mRNA.
DR   EMBL; AK050792; BAC34413.1; -; mRNA.
DR   EMBL; AK159779; BAE35363.1; -; mRNA.
DR   EMBL; BC004797; AAH04797.1; -; mRNA.
DR   IPI; IPI00120778; -.
DR   RefSeq; NP_083830.3; NM_029554.4.
DR   UniGene; Mm.38143; -.
DR   ProteinModelPortal; Q99K99; -.
DR   PhosphoSite; Q99K99; -.
DR   PRIDE; Q99K99; -.
DR   Ensembl; ENSMUST00000081747; ENSMUSP00000080443; ENSMUSG00000060512.
DR   GeneID; 76261; -.
DR   KEGG; mmu:76261; -.
DR   MGI; MGI:1923511; 0610040J01Rik.
DR   eggNOG; roNOG15925; -.
DR   GeneTree; ENSGT00390000013778; -.
DR   HOGENOM; HBG126558; -.
DR   HOVERGEN; HBG099521; -.
DR   InParanoid; Q99K99; -.
DR   OMA; IQSYLFD; -.
DR   OrthoDB; EOG49CQ93; -.
DR   PhylomeDB; Q99K99; -.
DR   NextBio; 344875; -.
DR   ArrayExpress; Q99K99; -.
DR   Bgee; Q99K99; -.
DR   CleanEx; MM_0610040J01RIK; -.
DR   Genevestigator; Q99K99; -.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    313       Uncharacterized protein C4orf19 homolog.
FT                                /FTId=PRO_0000286562.
FT   MOD_RES     104    104       Phosphothreonine.
FT   MOD_RES     107    107       Phosphoserine.
FT   CONFLICT    161    161       V -> M (in Ref. 2; AAH04797).
FT   CONFLICT    194    194       T -> A (in Ref. 2; AAH04797).
FT   CONFLICT    226    226       L -> Q (in Ref. 2; AAH04797).
FT   CONFLICT    270    270       S -> N (in Ref. 2; AAH04797).
FT   CONFLICT    271    271       E -> D (in Ref. 1; BAC34413).
FT   CONFLICT    272    272       R -> P (in Ref. 2; AAH04797).
SQ   SEQUENCE   313 AA;  33916 MW;  8BD6A1CB5AE6D0F3 CRC64;
     MGCRCCKMIQ SYLFDPVQVP SPGFVNEVNN CKLEEDDTVR LKGTQNSEVE VPRNALHDGS
     LSNSESRGST TGLPHQGPLP QEDSEERPCV EKQGIVNGIS PTATLQSVRS SRLHQVDNSS
     WASSPWVATI DSAHLAQPFL EGEDYRKQSC LLPTLEGTQM VGHGDCRAPA EALAVADHIP
     YIPAPDYPQL WSPTVDNADP EEKDCLFENH SEVEPLPGIQ PRVSQLGLNV PFSLQRSWDS
     LNEAGTTEVL SDYFKEEGPT HPTPAADSGS EREDPHTYNG DREGVVVDED AEVAEALAAL
     EAATAGEDAD DAD
//
ID   Q99KC3_MOUSE            Unreviewed;       432 AA.
AC   Q99KC3;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 44.
DE   SubName: Full=Nop2 protein;
GN   Name=Nop2; Synonyms=Nol1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N;
RC   TISSUE=Mammary tumor. Metallothionien-TGF alpha model. 10 month old
RC   virgin mouse. Taken by biopsy.;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC004733; AAH04733.1; -; mRNA.
DR   IPI; IPI00311453; -.
DR   UniGene; Mm.29203; -.
DR   HSSP; O50082; 1IXK.
DR   ProteinModelPortal; Q99KC3; -.
DR   SMR; Q99KC3; 2-210.
DR   STRING; Q99KC3; -.
DR   Ensembl; ENSMUST00000044200; ENSMUSP00000047123; ENSMUSG00000038279.
DR   MGI; MGI:107891; Nop2.
DR   eggNOG; roNOG08643; -.
DR   GeneTree; ENSGT00550000074621; -.
DR   InParanoid; Q99KC3; -.
DR   ArrayExpress; Q99KC3; -.
DR   Bgee; Q99KC3; -.
DR   Genevestigator; Q99KC3; -.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR   InterPro; IPR001678; Fmu/NOL1/Nop2p.
DR   InterPro; IPR018314; Fmu/NOL1/Nop2p_CS.
DR   InterPro; IPR011023; Nop2p.
DR   InterPro; IPR012586; P120R.
DR   InterPro; IPR023267; RCMT.
DR   Pfam; PF01189; Nol1_Nop2_Fmu; 1.
DR   Pfam; PF08062; P120R; 3.
DR   PRINTS; PR02008; RCMTFAMILY.
DR   TIGRFAMs; TIGR00446; nop2p; 1.
DR   PROSITE; PS01153; NOL1_NOP2_SUN; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   432 AA;  46816 MW;  22BAC56482A42E9B CRC64;
     MALAPQEHER ILDMCCAPGG KTSYIAQLME NTGVILANDA NADRLKSVVG NLHRLGVTNT
     IISHYDGRQF PKVVGGFDRV LLDAPCSGTG VISKDPAVKT NKDEKDIQRC AHLQKELLLS
     AIDSVNAASK TGGYLVYCTC SITVEENEWV VDYALKKRNV RLVPTGLDFG QEGFTRFQAR
     RFHPTLRSTR RFYPHTHNMD GFFIAKFKKF SNSIPQPHAG NSAAATPTEP DLKDQVTPKS
     ENGSQPTKKA RGAVKAKQQL LRQPHSKKPF QKLNGIAKGP GLSTEPSVPD AQVSTRPSQS
     AGNADVNSKR KRSEKLKQRG PKWKPSKEAA VPKPSAPSRV EDSGTPPVPT PSEIRAAPRP
     KDCAPSLGKA KKKQKGKQQL AQQPANGAAP LKEDAVSKGP SAPFVSPHSS TRPPPAKRRK
     SMTKGNSQPL LS
//
ID   MAOM_MOUSE              Reviewed;         589 AA.
AC   Q99KE1; Q3TBM8;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=NAD-dependent malic enzyme, mitochondrial;
DE            Short=NAD-ME;
DE            EC=1.1.1.38;
DE   AltName: Full=Malic enzyme 2;
DE   Flags: Precursor;
GN   Name=Me2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Spleen, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = pyruvate + CO(2) + NADH.
CC   -!- COFACTOR: Divalent metal cations. Prefers magnesium or manganese
CC       (By similarity).
CC   -!- ENZYME REGULATION: Subject to allosteric activation by fumarate
CC       (By similarity).
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- MISCELLANEOUS: This isoenzyme can also use NADP(+) but is more
CC       effective with NAD(+) (By similarity).
CC   -!- SIMILARITY: Belongs to the malic enzymes family.
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DR   EMBL; AK042289; BAC31216.1; -; mRNA.
DR   EMBL; AK050933; BAC34467.1; -; mRNA.
DR   EMBL; AK050980; BAC34483.1; -; mRNA.
DR   EMBL; AK156403; BAE33701.1; -; mRNA.
DR   EMBL; AK171157; BAE42281.1; -; mRNA.
DR   EMBL; BC004709; AAH04709.1; -; mRNA.
DR   IPI; IPI00115977; -.
DR   RefSeq; NP_663469.1; NM_145494.2.
DR   UniGene; Mm.36817; -.
DR   ProteinModelPortal; Q99KE1; -.
DR   SMR; Q99KE1; 23-573.
DR   STRING; Q99KE1; -.
DR   PhosphoSite; Q99KE1; -.
DR   REPRODUCTION-2DPAGE; Q99KE1; -.
DR   PRIDE; Q99KE1; -.
DR   Ensembl; ENSMUST00000025439; ENSMUSP00000025439; ENSMUSG00000024556.
DR   GeneID; 107029; -.
DR   KEGG; mmu:107029; -.
DR   UCSC; uc008fox.1; mouse.
DR   CTD; 107029; -.
DR   MGI; MGI:2147351; Me2.
DR   eggNOG; roNOG14422; -.
DR   GeneTree; ENSGT00390000000754; -.
DR   HOGENOM; HBG289821; -.
DR   HOVERGEN; HBG000746; -.
DR   InParanoid; Q99KE1; -.
DR   OMA; QALRFHR; -.
DR   OrthoDB; EOG402WRR; -.
DR   PhylomeDB; Q99KE1; -.
DR   BRENDA; 1.1.1.38; 244.
DR   NextBio; 358536; -.
DR   ArrayExpress; Q99KE1; -.
DR   Bgee; Q99KE1; -.
DR   CleanEx; MM_ME2; -.
DR   Genevestigator; Q99KE1; -.
DR   GermOnline; ENSMUSG00000024556; Mus musculus.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0016619; F:malate dehydrogenase (oxaloacetate-decarboxylating) activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR015884; Malic_enzyme_CS.
DR   InterPro; IPR012301; Malic_N.
DR   InterPro; IPR012302; Malic_NAD-bd.
DR   InterPro; IPR001891; Malic_OxRdtase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.10380; G3DSA:3.40.50.10380; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00390; malic; 1.
DR   Pfam; PF03949; Malic_M; 1.
DR   PIRSF; PIRSF000106; ME; 1.
DR   PRINTS; PR00072; MALOXRDTASE.
DR   SMART; SM00919; Malic_M; 1.
DR   PROSITE; PS00331; MALIC_ENZYMES; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Allosteric enzyme; Metal-binding; Mitochondrion; NAD;
KW   Oxidoreductase; Transit peptide.
FT   TRANSIT       1     18       Mitochondrion (By similarity).
FT   CHAIN        19    589       NAD-dependent malic enzyme,
FT                                mitochondrial.
FT                                /FTId=PRO_0000018538.
FT   NP_BIND     311    328       NAD (By similarity).
FT   ACT_SITE    112    112       Proton donor (By similarity).
FT   ACT_SITE    183    183       Proton acceptor (By similarity).
FT   METAL       255    255       Divalent metal cation (By similarity).
FT   METAL       256    256       Divalent metal cation (By similarity).
FT   METAL       279    279       Divalent metal cation (By similarity).
FT   BINDING     165    165       NAD (By similarity).
FT   BINDING     279    279       NAD (By similarity).
FT   BINDING     421    421       NAD (By similarity).
FT   SITE        279    279       Important for activity (By similarity).
FT   MOD_RES     156    156       N6-acetyllysine (By similarity).
FT   MOD_RES     224    224       N6-acetyllysine (By similarity).
FT   MOD_RES     240    240       N6-acetyllysine (By similarity).
FT   MOD_RES     272    272       N6-acetyllysine (By similarity).
FT   MOD_RES     346    346       N6-acetyllysine (By similarity).
SQ   SEQUENCE   589 AA;  65799 MW;  CD77AD5744B08CAB CRC64;
     MFSRLRAVTT PCTLTCRRVH LKEKGKPLML NPRTNKGMAF TLQERQMLGL QGLLPPKIET
     QDIQALRFHR NLKKMTSPLE KYIYIMGIQE RNEKLFYRIL QDDIESLMPI VYTPTVGLAC
     CQYGHIFRRP KGLFISISDR GHVRSIVDNW PENHVKAVVV TDGERILGLG DLGVYGMGIP
     VGKLCLYTAC AGIQPEKCLP VCIDVGTDNM ALLKDPFYMG LYQKRDRSQL YDDLMDEFMK
     AITDRYGRNT LIQFEDFGNH NAFRFLRKYQ QKYCTFNDDI QGTAAVALSG LLAAQRVINK
     PVSEHKILFL GAGEAALGIA NLIVLSMVES GLSEEEAQRK IWMFDKSGLL VKGRTASIDS
     NQEPYAHAAP ESIPATFEDA VNKLKPSVII GVAGAGPLFT HGVIKAMASI NERPIIFALS
     NPTAQAECTA EDAYTLTEGR CLFASGSPFE PVKLQDGRVF TPGQGNNAYI FPGVALAVIL
     CEARHISDTV FLEAAKALTT QLTDAELAQG RLYPSLANIQ EVSANIAIKL AEYLYANKMA
     FRYPEPEDKA RYVRERIWRS NYVSLLPDVY DWPESSLTPP QITEEKLPH
//
ID   RBM10_MOUSE             Reviewed;         930 AA.
AC   Q99KG3; Q3TIY0; Q3U5B8; Q3UKI8; Q80U75; Q8BTP8;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=RNA-binding protein 10;
DE   AltName: Full=RNA-binding motif protein 10;
GN   Name=Rbm10; Synonyms=Kiaa0122;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Amnion, Liver, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-736 AND SER-738, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-733; SER-736 AND
RP   SER-738, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-736 AND SER-738, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-736 AND SER-738, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Not known. Binds to RNA homopolymers, with a preference
CC       for poly(G) and poly(U) and little for poly(A) (By similarity).
CC   -!- SUBUNIT: Associates with the spliceosome. Component of a large
CC       chromatin remodeling complex, at least composed of MYSM1, PCAF,
CC       RBM10 and KIF11/TRIP5 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q99KG3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99KG3-2; Sequence=VSP_034905;
CC       Name=3;
CC         IsoId=Q99KG3-3; Sequence=VSP_034906;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 C2H2-type zinc finger.
CC   -!- SIMILARITY: Contains 1 G-patch domain.
CC   -!- SIMILARITY: Contains 1 RanBP2-type zinc finger.
CC   -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65490.3; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK122208; BAC65490.3; ALT_INIT; Transcribed_RNA.
DR   EMBL; AK089105; BAC40753.1; -; mRNA.
DR   EMBL; AK145991; BAE26813.1; -; mRNA.
DR   EMBL; AK153736; BAE32161.1; -; mRNA.
DR   EMBL; AK167666; BAE39715.1; -; mRNA.
DR   EMBL; AL672073; CAM21277.1; -; Genomic_DNA.
DR   EMBL; AL807240; CAM21277.1; JOINED; Genomic_DNA.
DR   EMBL; AL807240; CAM23098.1; -; Genomic_DNA.
DR   EMBL; AL672073; CAM23098.1; JOINED; Genomic_DNA.
DR   EMBL; AL672073; CAM21279.1; -; Genomic_DNA.
DR   EMBL; AL807240; CAM21279.1; JOINED; Genomic_DNA.
DR   EMBL; AL807240; CAM23096.1; -; Genomic_DNA.
DR   EMBL; AL672073; CAM23096.1; JOINED; Genomic_DNA.
DR   EMBL; AL672073; CAM21278.1; -; Genomic_DNA.
DR   EMBL; AL807240; CAM21278.1; JOINED; Genomic_DNA.
DR   EMBL; AL807240; CAM23097.1; -; Genomic_DNA.
DR   EMBL; AL672073; CAM23097.1; JOINED; Genomic_DNA.
DR   EMBL; BC004674; AAH04674.1; -; mRNA.
DR   IPI; IPI00116031; -.
DR   IPI; IPI00468834; -.
DR   IPI; IPI00776254; -.
DR   RefSeq; NP_001161247.1; NM_001167775.1.
DR   RefSeq; NP_001161248.1; NM_001167776.1.
DR   RefSeq; NP_663602.1; NM_145627.2.
DR   UniGene; Mm.279194; -.
DR   UniGene; Mm.383632; -.
DR   UniGene; Mm.458777; -.
DR   UniGene; Mm.475412; -.
DR   HSSP; P08199; 1FJC.
DR   ProteinModelPortal; Q99KG3; -.
DR   SMR; Q99KG3; 127-208, 298-387.
DR   PhosphoSite; Q99KG3; -.
DR   PRIDE; Q99KG3; -.
DR   Ensembl; ENSMUST00000115374; ENSMUSP00000111032; ENSMUSG00000031060.
DR   Ensembl; ENSMUST00000115376; ENSMUSP00000111034; ENSMUSG00000031060.
DR   GeneID; 236732; -.
DR   KEGG; mmu:236732; -.
DR   UCSC; uc009sth.1; mouse.
DR   CTD; 236732; -.
DR   MGI; MGI:2384310; Rbm10.
DR   GeneTree; ENSGT00510000046476; -.
DR   HOGENOM; HBG713245; -.
DR   HOVERGEN; HBG000318; -.
DR   InParanoid; Q99KG3; -.
DR   OMA; MEANQHS; -.
DR   OrthoDB; EOG4DZ1TN; -.
DR   NextBio; 383047; -.
DR   ArrayExpress; Q99KG3; -.
DR   Bgee; Q99KG3; -.
DR   Genevestigator; Q99KG3; -.
DR   GO; GO:0016585; C:chromatin remodeling complex; ISS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR000467; G_patch.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   Pfam; PF01585; G-patch; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   Pfam; PF00641; zf-RanBP; 1.
DR   SMART; SM00443; G_patch; 1.
DR   SMART; SM00360; RRM; 2.
DR   SMART; SM00355; ZnF_C2H2; 1.
DR   SMART; SM00547; ZnF_RBZ; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
DR   PROSITE; PS50102; RRM; 2.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
DR   PROSITE; PS50199; ZF_RANBP2_2; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Metal-binding; Nucleus;
KW   Phosphoprotein; Repeat; RNA-binding; Zinc; Zinc-finger.
FT   CHAIN         1    930       RNA-binding protein 10.
FT                                /FTId=PRO_0000345017.
FT   DOMAIN      129    209       RRM 1.
FT   DOMAIN      300    384       RRM 2.
FT   DOMAIN      858    904       G-patch.
FT   ZN_FING     212    242       RanBP2-type.
FT   ZN_FING     759    784       C2H2-type; atypical.
FT   COMPBIAS     80     87       Poly-Arg.
FT   COMPBIAS    113    125       Poly-Glu.
FT   MOD_RES      50     50       Phosphoserine (By similarity).
FT   MOD_RES      60     60       Phosphoserine (By similarity).
FT   MOD_RES      61     61       Phosphoserine (By similarity).
FT   MOD_RES      65     65       Phosphoserine (By similarity).
FT   MOD_RES      89     89       Phosphoserine (By similarity).
FT   MOD_RES      91     91       Phosphothreonine (By similarity).
FT   MOD_RES     288    288       Phosphoserine (By similarity).
FT   MOD_RES     383    383       N6-acetyllysine (By similarity).
FT   MOD_RES     723    723       Phosphoserine (By similarity).
FT   MOD_RES     733    733       Phosphoserine.
FT   MOD_RES     736    736       Phosphoserine.
FT   MOD_RES     738    738       Phosphoserine.
FT   MOD_RES     797    797       Phosphoserine (By similarity).
FT   VAR_SEQ      68    144       Missing (in isoform 2).
FT                                /FTId=VSP_034905.
FT   VAR_SEQ     354    354       Missing (in isoform 3).
FT                                /FTId=VSP_034906.
FT   CONFLICT    188    188       M -> V (in Ref. 2; BAE26813).
FT   CONFLICT    355    355       E -> VR (in Ref. 1; BAC65490).
FT   CONFLICT    428    428       P -> H (in Ref. 2; BAE39715).
SQ   SEQUENCE   930 AA;  103494 MW;  E59A2AB20AF1C08C CRC64;
     MEYERRGGRG DRTGRYGATD RSQDDSGENR SRDHDYRDMD YRSYPREYGS QEGKHEYDDS
     SEEQSAEDSY EASPGSETQR RRRRRHRHSP TGPPGFPRDG DYRDQDYRTE QGEEEEEEDE
     EEEEEKASNI VMLRMLPQAA TEDDIRGQLQ SHGVQAREVR LMRNKSSGQS RGFAFVEFSH
     LQDATRWMEA NQHSLNILGQ KVSMHYSDPK PKINEDWLCN KCGVQNFKRR EKCFKCGVPK
     SEAEQKLPLG TRLDQQALPL GGRELSQGLL PLPQPYQAQG VLTSQALSQG SEPSSENAND
     TIILRNLNPH STMDSILGAL APYAVLSSSN VRVIKDKQTQ LNRGFAFIQL STIVEAAQLL
     QILQALHPPL TIDGKTINVE FAKGSKRDMA SNEGSRINAA SVASTAIAAA QWAISQASQG
     GESAWAAPEE PPVDYSYYQQ DEGYGSSQGT DSLYAHGYLK NSKGPGMTGT KGDPAGTGPE
     ASLEAGADSV SLQAFSRAQP GAAPGLYQQS AEGSSGQSTA TNSQSYTIIS PAVLKAELQS
     PTQPSSSAFP PATSPTAPEA YSQYPVPDVS TYQYDETSGY YYDPQTGLYY DPNSQYYYNA
     QSQQYLYWDG ERRTYIPALE QSADGHKDTG ASSKEGKEKK EKHKTKTAQQ IAKDMERWAR
     SLNKQKENFK NSFQPISALR DDERRESATA DAGYAILEKK GALAERQHTS MDLPKLASDD
     RPSPPRGLVA AYSGESDSEE EQERGGPERE EKLTDWQKLA CLLCRRQFPS KEALIRHQQL
     SGLHKQNLEI HRRAHLSENE LEALEKNDME QMKYRDRAAE RREKYGIPEP PEPKRRKYGG
     ISTASVDFEQ PTRDGLGSDN IGSRMLQAMG WKEGSGLGRK KQGIVTPIEA QTRVRGSGLG
     ARGSSYGVTS TESYKETLHK TMVTRFNEAQ
//
ID   STK24_MOUSE             Reviewed;         431 AA.
AC   Q99KH8;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Serine/threonine-protein kinase 24;
DE            EC=2.7.11.1;
GN   Name=Stk24;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-341, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Protein kinase that act on both serine and threonine
CC       residues (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC004650; AAH04650.1; -; mRNA.
DR   IPI; IPI00116065; -.
DR   RefSeq; NP_663440.1; NM_145465.2.
DR   UniGene; Mm.390756; -.
DR   UniGene; Mm.442081; -.
DR   UniGene; Mm.472866; -.
DR   ProteinModelPortal; Q99KH8; -.
DR   SMR; Q99KH8; 8-298.
DR   STRING; Q99KH8; -.
DR   PhosphoSite; Q99KH8; -.
DR   PRIDE; Q99KH8; -.
DR   Ensembl; ENSMUST00000079817; ENSMUSP00000078746; ENSMUSG00000063410.
DR   GeneID; 223255; -.
DR   KEGG; mmu:223255; -.
DR   NMPDR; fig|10090.3.peg.29591; -.
DR   UCSC; uc007vac.1; mouse.
DR   CTD; 223255; -.
DR   MGI; MGI:2385007; Stk24.
DR   GeneTree; ENSGT00600000084209; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108518; -.
DR   InParanoid; Q99KH8; -.
DR   OMA; DEIQIAT; -.
DR   OrthoDB; EOG4WWRJP; -.
DR   PhylomeDB; Q99KH8; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 376675; -.
DR   ArrayExpress; Q99KH8; -.
DR   Bgee; Q99KH8; -.
DR   CleanEx; MM_STK24; -.
DR   Genevestigator; Q99KH8; -.
DR   GermOnline; ENSMUSG00000063410; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    431       Serine/threonine-protein kinase 24.
FT                                /FTId=PRO_0000086712.
FT   DOMAIN       24    274       Protein kinase.
FT   NP_BIND      30     38       ATP (By similarity).
FT   ACT_SITE    144    144       Proton acceptor (By similarity).
FT   BINDING      53     53       ATP (By similarity).
FT   MOD_RES       4      4       Phosphoserine.
FT   MOD_RES     178    178       Phosphothreonine (By similarity).
FT   MOD_RES     299    299       Phosphoserine (By similarity).
FT   MOD_RES     303    303       Phosphoserine (By similarity).
FT   MOD_RES     304    304       Phosphoserine (By similarity).
FT   MOD_RES     305    305       Phosphoserine (By similarity).
FT   MOD_RES     308    308       Phosphoserine (By similarity).
FT   MOD_RES     341    341       Phosphothreonine.
SQ   SEQUENCE   431 AA;  47954 MW;  BB0A47D9701AEB00 CRC64;
     MAHSPVQSGL PGMQNLKADP EELFTKLEKI GKGSFGEVFK GIDNRTQKVV AIKIIDLEEA
     EDEIEDIQQE ITVLSQCDSP YVTKYYGSYL KDTKLWIIME YLGGGSALDL LEPGPLDEIQ
     IATILREILK GLDYLHSEKK IHRDIKAANV LLSEHGEVKL ADFGVAGQLT DTQIKRNTFV
     GTPFWMAPEV IKQSAYDSKA DIWSLGITAI ELAKGEPPHS ELHPMKVLFL IPKNNPPTLE
     GNYSKPLKEF VEACLNKEPS FRPTAKELLK HKFIIRNAKK TSYLTELIDR YKRWKAEQSH
     EDSSSEDSDV ETDGQASGGS DSGDWIFTIR EKDPKNLENG TLQLSDLERN KMKDIPKRPF
     SQCLSTIISP LFAELKEKSQ ACGGNLGSIE ELRGAIYLAE EACPGISDTM VAQLVQRLQR
     YSLSGGGASA H
//
ID   ACON_MOUSE              Reviewed;         780 AA.
AC   Q99KI0; Q3UDK9; Q3ULG9; Q3UNH7; Q505P4;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Aconitate hydratase, mitochondrial;
DE            Short=Aconitase;
DE            EC=4.2.1.3;
DE   AltName: Full=Citrate hydro-lyase;
DE   Flags: Precursor;
GN   Name=Aco2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 32-56; 59-84; 96-138; 143-160; 234-245; 251-258;
RP   313-323; 371-395; 402-409; 412-424; 430-457; 466-474; 480-517;
RP   522-587; 592-605; 608-628; 634-648; 657-671; 694-739 AND 744-767, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-50, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
RN   [5]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-144, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Heart;
RX   PubMed=17451654; DOI=10.1016/j.bbrc.2007.04.015;
RA   Jeon H.B., Choi E.S., Yoon J.H., Hwang J.H., Chang J.W., Lee E.K.,
RA   Choi H.W., Park Z.-Y., Yoo Y.J.;
RT   "A proteomics approach to identify the ubiquitinated proteins in mouse
RT   heart.";
RL   Biochem. Biophys. Res. Commun. 357:731-736(2007).
CC   -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via
CC       cis-aconitate (By similarity).
CC   -!- CATALYTIC ACTIVITY: Citrate = isocitrate.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. Binding of a 3Fe-4S
CC       cluster leads to an inactive enzyme (By similarity).
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       isocitrate from oxaloacetate: step 2/2.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- PTM: Acetylation of Lys-50 is observed in liver mitochondria from
CC       fasted mice but not from fed mice.
CC   -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK143917; BAE25602.1; -; mRNA.
DR   EMBL; AK144207; BAE25770.1; -; mRNA.
DR   EMBL; AK145511; BAE26479.1; -; mRNA.
DR   EMBL; AK150027; BAE29252.1; -; mRNA.
DR   EMBL; AK165411; BAE38169.1; -; mRNA.
DR   EMBL; BC004645; AAH04645.1; -; mRNA.
DR   EMBL; BC094462; AAH94462.1; -; mRNA.
DR   IPI; IPI00116074; -.
DR   RefSeq; NP_542364.1; NM_080633.2.
DR   UniGene; Mm.154581; -.
DR   ProteinModelPortal; Q99KI0; -.
DR   SMR; Q99KI0; 29-780.
DR   IntAct; Q99KI0; 8.
DR   STRING; Q99KI0; -.
DR   PhosphoSite; Q99KI0; -.
DR   REPRODUCTION-2DPAGE; Q99KI0; -.
DR   PRIDE; Q99KI0; -.
DR   Ensembl; ENSMUST00000023116; ENSMUSP00000023116; ENSMUSG00000022477.
DR   GeneID; 11429; -.
DR   KEGG; mmu:11429; -.
DR   NMPDR; fig|10090.3.peg.30319; -.
DR   UCSC; uc007wxp.1; mouse.
DR   CTD; 11429; -.
DR   MGI; MGI:87880; Aco2.
DR   eggNOG; roNOG05633; -.
DR   GeneTree; ENSGT00530000063060; -.
DR   HOGENOM; HBG295973; -.
DR   HOVERGEN; HBG000248; -.
DR   InParanoid; Q99KI0; -.
DR   OMA; KHGIRWV; -.
DR   OrthoDB; EOG4BCDM9; -.
DR   PhylomeDB; Q99KI0; -.
DR   BRENDA; 4.2.1.3; 244.
DR   NextBio; 278704; -.
DR   ArrayExpress; Q99KI0; -.
DR   Bgee; Q99KI0; -.
DR   CleanEx; MM_ACO2; -.
DR   Genevestigator; Q99KI0; -.
DR   GermOnline; ENSMUSG00000022477; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0003994; F:aconitate hydratase activity; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR   InterPro; IPR015937; Acoase/IPM_deHydtase.
DR   InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR   InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR   InterPro; IPR015932; Aconitase/IPMdHydase_lsu_aba_2.
DR   InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR   InterPro; IPR006248; Aconitase_mito-like.
DR   InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR   Gene3D; G3DSA:3.30.499.10; Acnase/IPM_dHydase_lsu_aba_1/3; 2.
DR   Gene3D; G3DSA:3.20.19.10; Aconitase/3IPM_dehydase_swvl; 1.
DR   Gene3D; G3DSA:3.40.1060.10; Aconitase/IPMdHydase_lsu_aba_2; 1.
DR   PANTHER; PTHR11670; Aconitase-like_core; 1.
DR   PANTHER; PTHR11670:SF5; Aconitase_mito; 1.
DR   Pfam; PF00330; Aconitase; 1.
DR   Pfam; PF00694; Aconitase_C; 1.
DR   PRINTS; PR00415; ACONITASE.
DR   SUPFAM; SSF52016; Aconitase/3IPM_dehydase_swvl; 1.
DR   SUPFAM; SSF53732; Aconitase_N; 1.
DR   TIGRFAMs; TIGR01340; aconitase_mito; 1.
DR   PROSITE; PS00450; ACONITASE_1; 1.
DR   PROSITE; PS01244; ACONITASE_2; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Acetylation; Direct protein sequencing; Iron; Iron-sulfur;
KW   Isopeptide bond; Lyase; Metal-binding; Mitochondrion;
KW   Pyrrolidone carboxylic acid; Transit peptide;
KW   Tricarboxylic acid cycle; Ubl conjugation.
FT   TRANSIT       1     27       Mitochondrion (By similarity).
FT   CHAIN        28    780       Aconitate hydratase, mitochondrial.
FT                                /FTId=PRO_0000000542.
FT   REGION      192    194       Substrate binding (By similarity).
FT   REGION      670    671       Substrate binding (By similarity).
FT   METAL       385    385       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       448    448       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       451    451       Iron-sulfur (4Fe-4S) (By similarity).
FT   BINDING      99     99       Substrate (By similarity).
FT   BINDING     474    474       Substrate (By similarity).
FT   BINDING     479    479       Substrate (By similarity).
FT   BINDING     607    607       Substrate (By similarity).
FT   MOD_RES      28     28       Pyrrolidone carboxylic acid (By
FT                                similarity).
FT   MOD_RES      50     50       N6-acetyllysine.
FT   MOD_RES     573    573       N6-acetyllysine (By similarity).
FT   MOD_RES     605    605       N6-acetyllysine (By similarity).
FT   CROSSLNK    144    144       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CONFLICT      7      8       LV -> P (in Ref. 1; BAE25770).
FT   CONFLICT    618    618       L -> F (in Ref. 2; AAH94462).
FT   CONFLICT    758    758       F -> L (in Ref. 1; BAE29252).
SQ   SEQUENCE   780 AA;  85464 MW;  9B515846E875D581 CRC64;
     MAPYSLLVTR LQKALGVRQY HVASVLCQRA KVAMSHFEPS EYIRYDLLEK NINIVRKRLN
     RPLTLSEKIV YGHLDDPANQ EIERGKTYLR LRPDRVAMQD ATAQMAMLQF ISSGLPKVAV
     PSTIHCDHLI EAQVGGEKDL RRAKDINQEV YNFLATAGAK YGVGFWRPGS GIIHQIILEN
     YAYPGVLLIG TDSHTPNGGG LGGICIGVGG ADAVDVMAGI PWELKCPKVI GVKLTGSLSG
     WTSPKDVILK VAGILTVKGG TGAIVEYHGP GVDSISCTGM ATICNMGAEI GATTSVFPYN
     HRMKKYLSKT GRTDIANLAE EFKDHLVPDP GCQYDQVIEI NLNELKPHIN GPFTPDLAHP
     VADVGTVAEK EGWPLDIRVG LIGSCTNSSY EDMGRSAAVA KQALAHGLKC KSQFTITPGS
     EQIRATIERD GYAQILRDVG GIVLANACGP CIGQWDRKDI KKGEKNTIVT SYNRNFTGRN
     DANPETHAFV TSPEIVTALA IAGTLKFNPE TDFLTGKDGK KFKLEAPDAD ELPRSDFDPG
     QDTYQHPPKD SSGQRVDVSP TSQRLQLLEP FDKWDGKDLE DLQILIKVKG KCTTDHISAA
     GPWLKFRGHL DNISNNLLIG AINIENGKAN SVRNAVTQEF GPVPDTARYY KKHGIRWVVI
     GDENYGEGSS REHAALEPRH LGGRAIITKS FARIHETNLK KQGLLPLTFA DPSDYNKIHP
     VDKLTIQGLK DFAPGKPLKC VIKHPNGTQE TILLNHTFNE TQIEWFRAGS ALNRMKELQQ
//
ID   DCTN2_MOUSE             Reviewed;         402 AA.
AC   Q99KJ8;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Dynactin subunit 2;
DE   AltName: Full=50 kDa dynein-associated polypeptide;
DE   AltName: Full=Dynactin complex 50 kDa subunit;
DE            Short=DCTN-50;
DE   AltName: Full=Growth cone membrane protein 23-48K;
DE            Short=GMP23-48K;
DE   AltName: Full=p50 dynamitin;
GN   Name=Dctn2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 66-75; 78-92; 103-117; 157-171; 195-217 AND
RP   310-321, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Brain;
RX   MEDLINE=97289622; PubMed=9144527; DOI=10.1006/bbrc.1997.6447;
RA   Abe T.K., Tanaka H., Iwanaga T., Odani S., Kuwano R.;
RT   "The presence of the 50-kDa subunit of dynactin complex in the nerve
RT   growth cone.";
RL   Biochem. Biophys. Res. Commun. 233:295-299(1997).
RN   [3]
RP   PROTEIN SEQUENCE OF 320-333.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [4]
RP   INTERACTION WITH BICD2.
RX   MEDLINE=21376052; PubMed=11483508; DOI=10.1093/emboj/20.15.4041;
RA   Hoogenraad C.C., Akhmanova A., Howell S.A., Dortland B.R.,
RA   de Zeeuw C.I., Willemsen R., Visser P., Grosveld F., Galjart N.;
RT   "Mammalian Golgi-associated Bicaudal-D2 functions in the dynein-
RT   dynactin pathway by interacting with these complexes.";
RL   EMBO J. 20:4041-4054(2001).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CEP135.
RX   PubMed=14983524; DOI=10.1002/cm.10175;
RA   Uetake Y., Terada Y., Matuliene J., Kuriyama R.;
RT   "Interaction of Cep135 with a p50 dynactin subunit in mammalian
RT   centrosomes.";
RL   Cell Motil. Cytoskeleton 58:53-66(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-86, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Modulates cytoplasmic dynein binding to an organelle,
CC       and plays a role in prometaphase chromosome alignment and spindle
CC       organization during mitosis. Involved in anchoring microtubules to
CC       centrosomes. May play a role in synapse formation during brain
CC       development.
CC   -!- SUBUNIT: Subunit of dynactin, a multiprotein complex associated
CC       with dynein. Interacts with MAPRE1 (By similarity). Interacts with
CC       BICD2 and CEP135. Interacts with ECM29 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome.
CC       Membrane; Peripheral membrane protein (By similarity).
CC   -!- DEVELOPMENTAL STAGE: Present at high levels in both cytoplasmic
CC       and membrane-associated forms in neonates. Levels of membrane-
CC       associated form are greatly reduced in the adult.
CC   -!- SIMILARITY: Belongs to the dynactin subunit 2 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC004613; AAH04613.1; -; mRNA.
DR   IPI; IPI00116112; -.
DR   RefSeq; NP_081427.1; NM_027151.2.
DR   UniGene; Mm.167537; -.
DR   ProteinModelPortal; Q99KJ8; -.
DR   MINT; MINT-1866067; -.
DR   STRING; Q99KJ8; -.
DR   PhosphoSite; Q99KJ8; -.
DR   REPRODUCTION-2DPAGE; Q99KJ8; -.
DR   UCD-2DPAGE; Q99KJ8; -.
DR   PRIDE; Q99KJ8; -.
DR   Ensembl; ENSMUST00000026479; ENSMUSP00000026479; ENSMUSG00000025410.
DR   GeneID; 69654; -.
DR   KEGG; mmu:69654; -.
DR   UCSC; uc007hiu.1; mouse.
DR   CTD; 69654; -.
DR   MGI; MGI:107733; Dctn2.
DR   GeneTree; ENSGT00390000003427; -.
DR   HOGENOM; HBG315337; -.
DR   HOVERGEN; HBG051323; -.
DR   InParanoid; Q99KJ8; -.
DR   OMA; THLDTTQ; -.
DR   OrthoDB; EOG4CC41M; -.
DR   PhylomeDB; Q99KJ8; -.
DR   NextBio; 329986; -.
DR   ArrayExpress; Q99KJ8; -.
DR   Bgee; Q99KJ8; -.
DR   CleanEx; MM_DCTN2; -.
DR   Genevestigator; Q99KJ8; -.
DR   GermOnline; ENSMUSG00000025410; Mus musculus.
DR   GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR   GO; GO:0030426; C:growth cone; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:motor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR006996; Dynamitin_2su.
DR   Pfam; PF04912; Dynamitin; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Dynein; Membrane; Microtubule;
KW   Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    402       Dynactin subunit 2.
FT                                /FTId=PRO_0000079822.
FT   COILED       99    132       Potential.
FT   COILED      215    245       Potential.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      83     83       Phosphoserine.
FT   MOD_RES      86     86       Phosphotyrosine.
SQ   SEQUENCE   402 AA;  44117 MW;  EA0D8E04E92726AC CRC64;
     MADPKYADLP GIARNEPDVY ETSDLPEDDQ AEFDAEELSS TSVEHIIVNP NAAYDKFKDK
     RVGTKGLDFS DRIGKTKRTG YESGDYEMLG EGLGVKETPQ QKYQRLLHEV QELTTEVEKI
     KTTVKESATE EKLTPVVLAK QLAALKQQLV ASHLEKLLGP DAAINLADPD GALAKRLLLQ
     LEATKSSKGS SGGKATAGAP PDSSLVTYEL HSRPEQDKFS QAAKVAELEK RLTELEATVR
     CDQDAQNPLS AGLQGACLME TVELLQAKVS ALDLAVLDQV EARLQSVLGK VNEIAKHKAS
     VEDADTQNKV HQLYETIQRW SPVASTLPEL VQRLVTIKQL HEQAMQFGQL LTHLDTTQQM
     MASSLKDNTA LLTQVQTTMR ENLATVEGNF ASIDARMKRL GK
//
ID   REEP3_MOUSE             Reviewed;         254 AA.
AC   Q99KK1; Q9CZM8; Q9D8G3;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Receptor expression-enhancing protein 3;
GN   Name=Reep3; Synonyms=D10Ucla1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15550249; DOI=10.1016/j.cell.2004.11.021;
RA   Saito H., Kubota M., Roberts R.W., Chi Q., Matsunami H.;
RT   "RTP family members induce functional expression of mammalian odorant
RT   receptors.";
RL   Cell 119:679-691(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Corpus striatum, Embryo, Small intestine, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150; SER-152; THR-200
RP   AND SER-209, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May enhance the cell surface expression of odorant
CC       receptors (By similarity).
CC   -!- SUBUNIT: Interacts with odorant receptor proteins (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the DP1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB25434.1; Type=Erroneous termination; Positions=182; Note=Translated as Gln;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AY562231; AAT70676.1; -; mRNA.
DR   EMBL; AK008058; BAB25434.1; ALT_SEQ; mRNA.
DR   EMBL; AK012403; BAB28218.1; -; mRNA.
DR   EMBL; AK047728; BAC33141.1; -; mRNA.
DR   EMBL; AK079649; BAC37714.1; -; mRNA.
DR   EMBL; BC004607; AAH04607.1; -; mRNA.
DR   IPI; IPI00187315; -.
DR   RefSeq; NP_848721.1; NM_178606.4.
DR   UniGene; Mm.41272; -.
DR   IntAct; Q99KK1; 1.
DR   PhosphoSite; Q99KK1; -.
DR   PRIDE; Q99KK1; -.
DR   Ensembl; ENSMUST00000020023; ENSMUSP00000020023; ENSMUSG00000019873.
DR   GeneID; 28193; -.
DR   KEGG; mmu:28193; -.
DR   UCSC; uc007flq.1; mouse.
DR   CTD; 28193; -.
DR   MGI; MGI:88930; Reep3.
DR   eggNOG; roNOG10300; -.
DR   GeneTree; ENSGT00550000074535; -.
DR   HOGENOM; HBG716753; -.
DR   HOVERGEN; HBG056861; -.
DR   InParanoid; Q99KK1; -.
DR   OMA; PYQTLPE; -.
DR   OrthoDB; EOG4WH8MK; -.
DR   NextBio; 306788; -.
DR   ArrayExpress; Q99KK1; -.
DR   Bgee; Q99KK1; -.
DR   CleanEx; MM_REEP3; -.
DR   Genevestigator; Q99KK1; -.
DR   GermOnline; ENSMUSG00000019873; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR004345; TB2_DP1_HVA22.
DR   PANTHER; PTHR12300; TB2_DP1_HVA22; 1.
DR   Pfam; PF03134; TB2_DP1_HVA22; 1.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    254       Receptor expression-enhancing protein 3.
FT                                /FTId=PRO_0000101827.
FT   TRANSMEM      1     21       Helical; (Potential).
FT   TRANSMEM     35     55       Helical; (Potential).
FT   TRANSMEM     59     79       Helical; (Potential).
FT   MOD_RES     150    150       Phosphoserine.
FT   MOD_RES     152    152       Phosphoserine.
FT   MOD_RES     200    200       Phosphothreonine.
FT   MOD_RES     209    209       Phosphoserine.
FT   CONFLICT     50     50       V -> I (in Ref. 2; BAB28218).
FT   CONFLICT    179    179       K -> E (in Ref. 2; BAB28218).
FT   CONFLICT    222    222       S -> F (in Ref. 2; BAB28218).
FT   CONFLICT    234    235       RK -> PQ (in Ref. 2; BAB28218).
FT   CONFLICT    249    250       RP -> TT (in Ref. 2; BAB28218).
SQ   SEQUENCE   254 AA;  29214 MW;  2F211016F4256EA2 CRC64;
     MVSWMISRAV VLVFGMLYPA YYSYKAVKTK NVKEYVRWMM YWIVFALYTV IETVADQTLA
     WFPLYYELKI AFVIWLLSPY TRGASLIYRK FLHPLLSSKE REIDDYIVQA KERGYETMVN
     FGRQGLNLAA AAAVTAAVKS QGAITERLRS FSMHDLTAIQ GDEPVGHRPY QTLPEAKRKG
     KQATESPAYG IPLKDGSEQT DEEAEGPFSD DEMVTHKALR RSQSMKSVKT IKGRKEVRYG
     SLKYKVKKRP QVYF
//
ID   SYHM_MOUSE              Reviewed;         505 AA.
AC   Q99KK9;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Probable histidyl-tRNA synthetase, mitochondrial;
DE            EC=6.1.1.21;
DE   AltName: Full=Histidine--tRNA ligase;
DE            Short=HisRS;
DE   AltName: Full=Histidine--tRNA ligase-like;
DE   Flags: Precursor;
GN   Name=Hars2; Synonyms=Harsl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + L-histidine + tRNA(His) = AMP +
CC       diphosphate + L-histidyl-tRNA(His).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; BC004596; AAH04596.1; -; mRNA.
DR   IPI; IPI00116138; -.
DR   RefSeq; NP_542367.1; NM_080636.1.
DR   UniGene; Mm.282700; -.
DR   ProteinModelPortal; Q99KK9; -.
DR   SMR; Q99KK9; 53-502.
DR   STRING; Q99KK9; -.
DR   PhosphoSite; Q99KK9; -.
DR   PRIDE; Q99KK9; -.
DR   Ensembl; ENSMUST00000019287; ENSMUSP00000019287; ENSMUSG00000019143.
DR   GeneID; 70791; -.
DR   KEGG; mmu:70791; -.
DR   NMPDR; fig|10090.3.peg.3820; -.
DR   UCSC; uc008eor.1; mouse.
DR   CTD; 70791; -.
DR   MGI; MGI:1918041; Hars2.
DR   GeneTree; ENSGT00390000005922; -.
DR   HOGENOM; HBG616575; -.
DR   HOVERGEN; HBG002731; -.
DR   InParanoid; Q99KK9; -.
DR   OMA; QLFQDPR; -.
DR   PhylomeDB; Q99KK9; -.
DR   BRENDA; 6.1.1.21; 244.
DR   NextBio; 332262; -.
DR   ArrayExpress; Q99KK9; -.
DR   Bgee; Q99KK9; -.
DR   Genevestigator; Q99KK9; -.
DR   GermOnline; ENSMUSG00000019143; Mus musculus.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:EC.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:InterPro.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb_cons-dom.
DR   InterPro; IPR006195; Aminoacyl-tRNA-synth_II.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR015807; His-tRNA-synth_IIa_sub.
DR   InterPro; IPR004516; His-tRNA_synth_IIA.
DR   Gene3D; G3DSA:3.40.50.800; Anticodon_bd; 1.
DR   PANTHER; PTHR11476; His-tRNA_synth; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR   SUPFAM; SSF52954; Anticodon_bd; 1.
DR   TIGRFAMs; TIGR00442; hisS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Ligase;
KW   Mitochondrion; Nucleotide-binding; Phosphoprotein;
KW   Protein biosynthesis; Transit peptide.
FT   TRANSIT       1     31       Mitochondrion (Potential).
FT   CHAIN        32    505       Probable histidyl-tRNA synthetase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000254584.
FT   MOD_RES      66     66       Phosphoserine (By similarity).
FT   MOD_RES     443    443       N6-acetyllysine (By similarity).
SQ   SEQUENCE   505 AA;  56985 MW;  1865426DF408DA1E CRC64;
     MPHLGPLRRR AWAALLGQLL RPPSTVCTRG CHSQVAKAVL TSEQLKSHQE KPNFVIKVPK
     GTRDLSPQQM VVREKILDKI ISCFKRHGAK GLDTPAFELK EMLTEKYEDN FGLMYDLKDQ
     GGELLSLRYD LTVPFARYLA MNKLKKMKRY QVGKVWRRES PAIAQGRYRE FCQCDFDIAG
     EFDPMIPDAE CLRIMCEILS GLQLGDFLIK VNDRRVVDGI FAVCGVPESK LRTICSSMDK
     LDKMSWEGVR HEMVAKKGLA PEVADRIGDF VQYHGGISLV EDLFKDPRLS QSQLALQGLG
     DLKLLFEYLR LFGIADKISL DLSLARGLDY YTGVIYEAVL LESPAQAGKE TLSVGSVAAG
     GRYDNLVAQF DPKGHHVPCV GLSIGVERIF YLVEQKMKMS GEKVRTTETQ VFVATPQKNF
     LQERLKIIAE LWDAGIKAEM LYKNNPKLLT QLHYCEKADI PLMVIIGEQE RNEGVIKLRS
     VASREEVTIN RESLVAEIQK RLSES
//
ID   RNF34_MOUSE             Reviewed;         376 AA.
AC   Q99KR6; Q3UV45;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF34;
DE            EC=6.3.2.-;
DE   AltName: Full=Phafin-1;
DE   AltName: Full=RING finger protein 34;
DE   AltName: Full=RING finger protein RIFF;
GN   Name=Rnf34;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Hong W.;
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone, Bone marrow, Corpora quadrigemina, Head, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Has E3 ubiquitin-protein ligase activity. Regulates the
CC       levels of CASP8 and CASP10 by targeting them for proteasomal
CC       degradation. Protects cells against apoptosis induced by TNF.
CC       Binds phosphatidylinositol-5-phosphate and phosphatidylinositol-3-
CC       phosphate (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with CASP8 and CASP10 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle (By similarity).
CC       Endomembrane system; Peripheral membrane protein (By similarity).
CC   -!- PTM: Auto-ubiquitinated (in vitro) (By similarity).
CC   -!- PTM: Proteolytically cleaved by caspases upon induction of
CC       apoptosis by TNF (By similarity).
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SIMILARITY: Contains 2 SAP domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF434815; AAL30770.1; -; mRNA.
DR   EMBL; AK045696; BAC32461.1; -; mRNA.
DR   EMBL; AK046274; BAC32666.1; -; mRNA.
DR   EMBL; AK046381; BAC32697.1; -; mRNA.
DR   EMBL; AK077221; BAC36693.1; -; mRNA.
DR   EMBL; AK132330; BAE21109.1; -; mRNA.
DR   EMBL; AK137606; BAE23428.1; -; mRNA.
DR   EMBL; AK150976; BAE30005.1; -; mRNA.
DR   EMBL; AK159753; BAE35344.1; -; mRNA.
DR   EMBL; BC004042; AAH04042.1; -; mRNA.
DR   IPI; IPI00116227; -.
DR   RefSeq; NP_085041.1; NM_030564.1.
DR   UniGene; Mm.388529; -.
DR   ProteinModelPortal; Q99KR6; -.
DR   SMR; Q99KR6; 26-153, 325-376.
DR   STRING; Q99KR6; -.
DR   PhosphoSite; Q99KR6; -.
DR   PRIDE; Q99KR6; -.
DR   Ensembl; ENSMUST00000031434; ENSMUSP00000031434; ENSMUSG00000029474.
DR   GeneID; 80751; -.
DR   KEGG; mmu:80751; -.
DR   NMPDR; fig|10090.3.peg.12400; -.
DR   UCSC; uc008zmp.1; mouse.
DR   CTD; 80751; -.
DR   MGI; MGI:2153340; Rnf34.
DR   eggNOG; roNOG12800; -.
DR   GeneTree; ENSGT00390000012719; -.
DR   HOGENOM; HBG445295; -.
DR   HOVERGEN; HBG055079; -.
DR   InParanoid; Q99KR6; -.
DR   OMA; SVFRKKH; -.
DR   OrthoDB; EOG4HX51R; -.
DR   PhylomeDB; Q99KR6; -.
DR   NextBio; 350117; -.
DR   ArrayExpress; Q99KR6; -.
DR   Bgee; Q99KR6; -.
DR   CleanEx; MM_RNF34; -.
DR   Genevestigator; Q99KR6; -.
DR   GermOnline; ENSMUSG00000029474; Mus musculus.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 2.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS50800; SAP; FALSE_NEG.
DR   PROSITE; PS50178; ZF_FYVE; FALSE_NEG.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Ligase; Membrane; Metal-binding; Nucleus; Phosphoprotein;
KW   Repeat; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    376       E3 ubiquitin-protein ligase RNF34.
FT                                /FTId=PRO_0000056073.
FT   DOMAIN      115    134       SAP 1.
FT   DOMAIN      268    282       SAP 2.
FT   ZN_FING      56    107       FYVE-type.
FT   ZN_FING     329    364       RING-type.
FT   COMPBIAS    222    245       Asp/Glu-rich.
FT   SITE        236    237       Cleavage; by caspase-3 (By similarity).
FT   MOD_RES     258    258       Phosphoserine (By similarity).
FT   MOD_RES     260    260       Phosphoserine.
SQ   SEQUENCE   376 AA;  42030 MW;  FE4AB65DAE9381BC CRC64;
     MKAGATSMWA SCCGLLNEVM GTGAVRGQQA GFPGSTGPFR FTPSSDFPTY PPAATEGPNI
     VCKACGLSFS VFRKKHVCCD CKKDFCSLCS VSQENLRRCS TCHLLQETAF QRPQLMRLKV
     KDLRQYLLLR NIPTDTCREK EDLVDLVLCH RGLGSGDDLD SSSLNSSRSQ TSSFFTQSLF
     SNYTPPSATV SSFQGELMDR DGAFRSEVLA QVQSEIASAN TDDDDDDDDD DDDDEDDDDE
     QEEEEQNPGL SKKKARASLS DLSSLEEVEG MSVRQLKEIL ARNFVNYSGC CEKWELVEKV
     NRLYKENEEN QKSYGERMQL QDEEDDSLCR ICMDAVIDCV LLECGHMVTC TKCGKRMSEC
     PICRQYVVRA VHVFKS
//
ID   TMM49_MOUSE             Reviewed;         406 AA.
AC   Q99KU0; A2V655; Q3TX07; Q8BHD3;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Transmembrane protein 49;
DE   AltName: Full=NF-E2-inducible protein 2;
DE            Short=Protein ni-2;
DE   AltName: Full=Vacuole membrane protein 1;
GN   Name=Tmem49; Synonyms=Vmp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Spleen;
RA   Yamazaki S., Muta T., Takeshige K.;
RT   "A novel lipopolysaccharide-inducible gene (#25).";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Nagata Y., Oda M., Haruta H., Todokoro K.;
RT   "NF-E2 induceble novel gene.";
RL   Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Stress-induced protein that, when overexpressed,
CC       promotes formation of intracellular vacuoles followed by cell
CC       death. May be involved in the cytoplasmic vacuolization of acinar
CC       cells during the early stage of acute pancreatitis (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate
CC       compartment membrane; Multi-pass membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the TMEM49 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB047550; BAF47367.1; -; mRNA.
DR   EMBL; AB076609; BAD06453.1; -; mRNA.
DR   EMBL; AK043091; BAC31456.1; -; mRNA.
DR   EMBL; AK077443; BAC36803.1; -; mRNA.
DR   EMBL; AK159468; BAE35109.1; -; mRNA.
DR   EMBL; AL592222; CAI25358.1; -; Genomic_DNA.
DR   EMBL; AL604063; CAI25358.1; JOINED; Genomic_DNA.
DR   EMBL; AL604063; CAI25797.1; -; Genomic_DNA.
DR   EMBL; AL592222; CAI25797.1; JOINED; Genomic_DNA.
DR   EMBL; BC004013; AAH04013.1; -; mRNA.
DR   IPI; IPI00387192; -.
DR   RefSeq; NP_083754.2; NM_029478.3.
DR   UniGene; Mm.390398; -.
DR   UniGene; Mm.480374; -.
DR   PRIDE; Q99KU0; -.
DR   Ensembl; ENSMUST00000018315; ENSMUSP00000018315; ENSMUSG00000018171.
DR   GeneID; 75909; -.
DR   KEGG; mmu:75909; -.
DR   CTD; 75909; -.
DR   MGI; MGI:1923159; Tmem49.
DR   eggNOG; roNOG08399; -.
DR   GeneTree; ENSGT00390000007230; -.
DR   HOGENOM; HBG591351; -.
DR   HOVERGEN; HBG057290; -.
DR   InParanoid; Q99KU0; -.
DR   OMA; XIPNPLF; -.
DR   OrthoDB; EOG4K0QNM; -.
DR   PhylomeDB; Q99KU0; -.
DR   NextBio; 344239; -.
DR   ArrayExpress; Q99KU0; -.
DR   Bgee; Q99KU0; -.
DR   CleanEx; MM_TMEM49; -.
DR   Genevestigator; Q99KU0; -.
DR   GO; GO:0033116; C:ER-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    406       Transmembrane protein 49.
FT                                /FTId=PRO_0000284547.
FT   TOPO_DOM      1     77       Cytoplasmic (Potential).
FT   TRANSMEM     78     98       Helical; (Potential).
FT   TOPO_DOM     99    109       Extracellular (Potential).
FT   TRANSMEM    110    130       Helical; (Potential).
FT   TOPO_DOM    131    250       Cytoplasmic (Potential).
FT   TRANSMEM    251    271       Helical; (Potential).
FT   TOPO_DOM    272    273       Extracellular (Potential).
FT   TRANSMEM    274    294       Helical; (Potential).
FT   TOPO_DOM    295    305       Cytoplasmic (Potential).
FT   TRANSMEM    306    326       Helical; (Potential).
FT   TOPO_DOM    327    363       Extracellular (Potential).
FT   TRANSMEM    364    384       Helical; (Potential).
FT   TOPO_DOM    385    406       Cytoplasmic (Potential).
FT   CONFLICT     13     13       I -> V (in Ref. 2; BAD06453 and 5;
FT                                AAH04013).
FT   CONFLICT    228    228       E -> K (in Ref. 3; BAE35109).
FT   CONFLICT    347    347       Q -> H (in Ref. 1; BAF47367).
SQ   SEQUENCE   406 AA;  45960 MW;  2EFE789F29E2CF5D CRC64;
     MAENGKNCDQ RRIAMSKDQH NGSLTDPSSV HEKKRRDREE RQNIVLWRQP LITLQYFSLE
     TLVVLKEWTS KLWHRQSIVV SFLLLLAALV ATYYVEGAHQ QYVQRIEKQF LLYAYWIGLG
     ILSSVGLGTG LHTFLLYLGP HIASVTLAAY ECNSVNFPEP PYPDQIICPE EEGAEGAISL
     WSIISKVRIE ACMWGIGTAI GELPPYFMAR AARLSGAEPD DEEYQEFEEM LEHAEAAQDF
     ASRAKLAVQK LVQKVGFFGI LACASIPNPL FDLAGITCGH FLVPFWTFFG ATLIGKAIIK
     MHIQKIFVIV TFSKHIVEQM VTFIGAVPGI GPSLQKPFQE YLEAQRQKLH HRSEAGTPQG
     ENWLSWMFEK LVVAMVCYFV LSIINSMAQN YAKRIQQRLN SEEKTK
//
ID   DJB11_MOUSE             Reviewed;         358 AA.
AC   Q99KV1; A6X957; Q543I7; Q8BK79; Q8VCY1; Q8VHB1;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=DnaJ homolog subfamily B member 11;
DE   AltName: Full=APOBEC1-binding protein 2;
DE            Short=ABBP-2;
DE   AltName: Full=ER-associated DNAJ;
DE   AltName: Full=ER-associated Hsp40 co-chaperone;
DE   AltName: Full=ER-associated dnaJ protein 3;
DE            Short=ERdj3;
DE            Short=ERj3p;
DE   Flags: Precursor;
GN   Name=Dnajb11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=21588215; PubMed=11584023; DOI=10.1074/jbc.M109215200;
RA   Lau P.P., Villanueva H., Kobayashi K., Nakamuta M., Chang B.H.-J.,
RA   Chan L.;
RT   "A DnaJ protein, apobec-1-binding protein-2, modulates apolipoprotein
RT   B mRNA editing.";
RL   J. Biol. Chem. 276:46445-46452(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N; TISSUE=Colon, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   COMPONENT OF A CHAPERONE COMPLEX.
RX   PubMed=12475965; DOI=10.1091/mbc.E02-05-0311;
RA   Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
RT   "A subset of chaperones and folding enzymes form multiprotein
RT   complexes in endoplasmic reticulum to bind nascent proteins.";
RL   Mol. Biol. Cell 13:4456-4469(2002).
RN   [6]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH DENATURED SUBSTRATES.
RX   PubMed=15525676; DOI=10.1091/mbc.E04-05-0434;
RA   Shen Y., Hendershot L.M.;
RT   "ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue,
RT   serves as a cofactor for BiP's interactions with unfolded
RT   substrates.";
RL   Mol. Biol. Cell 16:40-50(2005).
CC   -!- FUNCTION: Serves as a co-chaperone for HSPA5. Binds directly to
CC       both unfolded proteins that are substrates for ERAD and nascent
CC       unfolded peptide chains, but dissociates from the HSPA5-unfolded
CC       protein complex before folding is completed. May help recruiting
CC       HSPA5 and other chaperones to the substrate. Stimulates HSPA5
CC       ATPase activity (By similarity).
CC   -!- SUBUNIT: Part a large chaperone multiprotein complex comprising
CC       DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1,
CC       UGT1A1 and very small amounts of ERP29, but not, or at very low
CC       levels, CALR nor CANX. Binds to denatured substrates in an ATP-
CC       independent manner. Interacts via the J domain with HSPA5 in an
CC       ATP-dependent manner (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC   -!- PTM: Contains high-mannose Endo H-sensitive carbohydrates (By
CC       similarity).
CC   -!- PTM: Cys-169, Cys-171, Cys-193 and Cys-196 form intramolecular
CC       disulfide bonds. The preferential partner for each Cys is not
CC       known (By similarity).
CC   -!- SIMILARITY: Contains 1 J domain.
CC   -!- CAUTION: PubMed:11584023 reported a cytosolic, as well as nuclear
CC       subcellular location. This result was obtained using an N-
CC       terminally GFP-tagged construct which most probably affected
CC       signal peptide-driven targeting to the ER. As a consequence, the
CC       in vivo revelance of the observed interaction with APOBEC1, a
CC       nuclear protein, is dubious.
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DR   EMBL; AY054981; AAL17676.1; -; mRNA.
DR   EMBL; AK050500; BAC34293.1; -; mRNA.
DR   EMBL; AK075785; BAC35956.1; -; mRNA.
DR   EMBL; AK075953; BAC36079.1; -; mRNA.
DR   EMBL; AK148511; BAE28593.1; -; mRNA.
DR   EMBL; AK166730; BAE38977.1; -; mRNA.
DR   EMBL; CT027991; CAO78022.1; -; Genomic_DNA.
DR   EMBL; BC003999; AAH03999.1; -; mRNA.
DR   EMBL; BC018282; AAH18282.1; -; mRNA.
DR   EMBL; BC040747; AAH40747.1; -; mRNA.
DR   IPI; IPI00320241; -.
DR   RefSeq; NP_001177733.1; NM_001190804.1.
DR   RefSeq; NP_001177734.1; NM_001190805.1.
DR   RefSeq; NP_080676.3; NM_026400.5.
DR   UniGene; Mm.37516; -.
DR   UniGene; Mm.477367; -.
DR   ProteinModelPortal; Q99KV1; -.
DR   SMR; Q99KV1; 18-90, 132-343.
DR   STRING; Q99KV1; -.
DR   PhosphoSite; Q99KV1; -.
DR   REPRODUCTION-2DPAGE; Q99KV1; -.
DR   PRIDE; Q99KV1; -.
DR   Ensembl; ENSMUST00000004574; ENSMUSP00000004574; ENSMUSG00000004460.
DR   GeneID; 67838; -.
DR   KEGG; mmu:67838; -.
DR   UCSC; uc007yso.1; mouse.
DR   CTD; 67838; -.
DR   MGI; MGI:1915088; Dnajb11.
DR   eggNOG; roNOG05421; -.
DR   GeneTree; ENSGT00490000043321; -.
DR   HOGENOM; HBG635315; -.
DR   HOVERGEN; HBG066727; -.
DR   InParanoid; Q99KV1; -.
DR   OMA; FRIKVLK; -.
DR   OrthoDB; EOG4KD6M9; -.
DR   PhylomeDB; Q99KV1; -.
DR   NextBio; 325665; -.
DR   ArrayExpress; Q99KV1; -.
DR   Bgee; Q99KV1; -.
DR   CleanEx; MM_DNAJB11; -.
DR   Genevestigator; Q99KV1; -.
DR   GermOnline; ENSMUSG00000004460; Mus musculus.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IDA:MGI.
DR   GO; GO:0016556; P:mRNA modification; IDA:MGI.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_N.
DR   InterPro; IPR018253; Heat_shock_DnaJ_CS.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR003095; Hsp_DnaJ.
DR   Gene3D; G3DSA:1.10.287.110; DnaJ_N; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; DnaJ_N; 1.
DR   SUPFAM; SSF49493; HSP40_DnaJ_pep; 2.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW   Signal.
FT   SIGNAL        1     22       By similarity.
FT   CHAIN        23    358       DnaJ homolog subfamily B member 11.
FT                                /FTId=PRO_0000007261.
FT   DOMAIN       25     90       J.
FT   CARBOHYD    261    261       N-linked (GlcNAc...) (Probable).
FT   CONFLICT      9      9       F -> L (in Ref. 2; BAC35956).
FT   CONFLICT     88     88       T -> A (in Ref. 4; AAH18282).
FT   CONFLICT    217    217       R -> L (in Ref. 1; AAL17676).
FT   CONFLICT    240    240       R -> P (in Ref. 1; AAL17676).
FT   CONFLICT    255    255       G -> E (in Ref. 2; BAC35956).
SQ   SEQUENCE   358 AA;  40555 MW;  E53CE0B3DF7465B8 CRC64;
     MAPQNLSTFC LLLLYLIGTV IAGRDFYKIL GVPRSASIKD IKKAYRKLAL QLHPDRNPDD
     PQAQEKFQDL GAAYEVLSDS EKRKQYDTYG EEGLKDGHQS SHGDIFSHFF GDFGFMFGGT
     PRQQDRNIPR GSDIIVDLEV TLEEVYAGNF VEVVRNKPVA RQAPGKRKCN CRQEMRTTQL
     GPGRFQMTQE VVCDECPNVK LVNEERTLEV EIEPGVRDGM EYPFIGEGEP HVDGEPGDLR
     FRIKVVKHRI FERRGDDLYT NVTVSLVEAL VGFEMDITHL DGHKVHISRD KITRPGAKLW
     KKGEGLPNFD NNNIKGSLII TFDVDFPKEQ LTEEAKEGIK QLLKQGPVQK VYNGLQGY
//
ID   MLF2_MOUSE              Reviewed;         247 AA.
AC   Q99KX1;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Myeloid leukemia factor 2;
DE   AltName: Full=Myelodysplasia-myeloid leukemia factor 2;
GN   Name=Mlf2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- INTERACTION:
CC       P42227:Stat3; NbExp=2; IntAct=EBI-646781, EBI-602878;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the MLF family.
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DR   EMBL; BC003975; AAH03975.1; -; mRNA.
DR   IPI; IPI00116372; -.
DR   RefSeq; NP_001163812.1; NM_001170341.1.
DR   RefSeq; NP_663360.1; NM_145385.2.
DR   UniGene; Mm.29737; -.
DR   ProteinModelPortal; Q99KX1; -.
DR   IntAct; Q99KX1; 2.
DR   PhosphoSite; Q99KX1; -.
DR   PRIDE; Q99KX1; -.
DR   Ensembl; ENSMUST00000032214; ENSMUSP00000032214; ENSMUSG00000030120.
DR   GeneID; 30853; -.
DR   KEGG; mmu:30853; -.
DR   UCSC; uc009dso.1; mouse.
DR   CTD; 30853; -.
DR   MGI; MGI:1353554; Mlf2.
DR   GeneTree; ENSGT00390000005023; -.
DR   HOGENOM; HBG717252; -.
DR   HOVERGEN; HBG019060; -.
DR   InParanoid; Q99KX1; -.
DR   OMA; GANCQTF; -.
DR   OrthoDB; EOG41RPW8; -.
DR   PhylomeDB; Q99KX1; -.
DR   NextBio; 307266; -.
DR   ArrayExpress; Q99KX1; -.
DR   Bgee; Q99KX1; -.
DR   CleanEx; MM_MLF2; -.
DR   Genevestigator; Q99KX1; -.
DR   GermOnline; ENSMUSG00000030120; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006952; P:defense response; ISS:UniProtKB.
DR   InterPro; IPR019376; Myeloid_leukemia_factor.
DR   Pfam; PF10248; Mlf1IP; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Phosphoprotein.
FT   CHAIN         1    247       Myeloid leukemia factor 2.
FT                                /FTId=PRO_0000220755.
FT   MOD_RES     143    143       Phosphoserine (By similarity).
FT   MOD_RES     151    151       Phosphoserine (By similarity).
FT   MOD_RES     237    237       Phosphoserine.
SQ   SEQUENCE   247 AA;  28055 MW;  00097529ECAB0123 CRC64;
     MFRFMRDVEP EDPMFLMDPF AIHRQHMSRM LSGGFGYSPF LSITDGNMPA TRPASRRMQA
     GAVSPFGMLG MSGGFMDMFG MMNDMIGNME HMAAGGNCQT FSSSTVISYS NTGDGAPKVY
     QETSEMRSAP GGIRETRRTV RDSDSGLEQM SIGHHIRDRA HILQRSRNHR TGDQEERQDY
     INLDESEAAA FDDEWRRETS RYRQQRPLEF RRHEASVGGG RRAEGPPRLA IQGPEDSPSR
     QSRRYDW
//
ID   GAK_MOUSE               Reviewed;        1305 AA.
AC   Q99KY4; Q6P1I8; Q6P9S5; Q8BM74; Q8K0Q4;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 2.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Cyclin-G-associated kinase;
DE            EC=2.7.11.1;
GN   Name=Gak;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Blastocyst, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, Colon, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-827, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Associates with cyclin G and CDK5. Seems to act as an
CC       auxilin homolog that is involved in the uncoating of clathrin-
CC       coated vesicles by Hsc70 in non-neuronal cells. Expression
CC       oscillates slightly during the cell cycle, peaking at G1 (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region (By
CC       similarity). Golgi apparatus, trans-Golgi network (By similarity).
CC       Cell junction, focal adhesion (By similarity). Note=Localizes to
CC       the perinuclear area and to the trans-Golgi network. Also seen on
CC       the plasma membrane, probably at focals adhesions (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99KY4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99KY4-2; Sequence=VSP_015821;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family.
CC   -!- SIMILARITY: Contains 1 C2 tensin-type domain.
CC   -!- SIMILARITY: Contains 1 J domain.
CC   -!- SIMILARITY: Contains 1 phosphatase tensin-type domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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DR   EMBL; AK034637; BAC28779.1; -; mRNA.
DR   EMBL; AK166682; BAE38941.1; -; mRNA.
DR   EMBL; BC003958; AAH03958.1; -; mRNA.
DR   EMBL; BC030859; AAH30859.1; -; mRNA.
DR   EMBL; BC060622; AAH60622.1; -; mRNA.
DR   EMBL; BC065052; AAH65052.1; -; mRNA.
DR   IPI; IPI00420480; -.
DR   IPI; IPI00620823; -.
DR   RefSeq; NP_705797.1; NM_153569.1.
DR   UniGene; Mm.276647; -.
DR   ProteinModelPortal; Q99KY4; -.
DR   SMR; Q99KY4; 28-336, 398-744, 1132-1305.
DR   MINT; MINT-1869993; -.
DR   STRING; Q99KY4; -.
DR   PhosphoSite; Q99KY4; -.
DR   PRIDE; Q99KY4; -.
DR   Ensembl; ENSMUST00000046603; ENSMUSP00000036705; ENSMUSG00000062234.
DR   Ensembl; ENSMUST00000112579; ENSMUSP00000108198; ENSMUSG00000062234.
DR   GeneID; 231580; -.
DR   KEGG; mmu:231580; -.
DR   CTD; 231580; -.
DR   MGI; MGI:2442153; Gak.
DR   GeneTree; ENSGT00550000074191; -.
DR   HOGENOM; HBG446617; -.
DR   HOVERGEN; HBG004322; -.
DR   InParanoid; Q99KY4; -.
DR   OrthoDB; EOG44MXR7; -.
DR   PhylomeDB; Q99KY4; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 380626; -.
DR   PMAP-CutDB; Q99KY4; -.
DR   ArrayExpress; Q99KY4; -.
DR   Bgee; Q99KY4; -.
DR   CleanEx; MM_GAK; -.
DR   Genevestigator; Q99KY4; -.
DR   GermOnline; ENSMUSG00000062234; Mus musculus.
DR   GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR001623; DnaJ_N.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR014019; Phosphatase_tensin-typ.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR014020; Tensin_phosphatase_C2-dom.
DR   Gene3D; G3DSA:1.10.287.110; DnaJ_N; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF10409; PTEN_C2; 1.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF46565; DnaJ_N; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51182; C2_TENSIN; 1.
DR   PROSITE; PS00636; DNAJ_1; FALSE_NEG.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51181; PPASE_TENSIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell cycle; Cell junction;
KW   Cytoplasm; Golgi apparatus; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1   1305       Cyclin-G-associated kinase.
FT                                /FTId=PRO_0000085959.
FT   DOMAIN       40    317       Protein kinase.
FT   DOMAIN      397    564       Phosphatase tensin-type.
FT   DOMAIN      570    708       C2 tensin-type.
FT   DOMAIN     1241   1305       J.
FT   NP_BIND      46     54       ATP (By similarity).
FT   ACT_SITE    173    173       Proton acceptor (By similarity).
FT   BINDING      69     69       ATP (By similarity).
FT   MOD_RES      16     16       Phosphoserine (By similarity).
FT   MOD_RES     454    454       Phosphoserine (By similarity).
FT   MOD_RES     613    613       Phosphotyrosine (By similarity).
FT   MOD_RES     768    768       Phosphoserine (By similarity).
FT   MOD_RES     774    774       Phosphothreonine (By similarity).
FT   MOD_RES     776    776       Phosphoserine (By similarity).
FT   MOD_RES     778    778       Phosphoserine (By similarity).
FT   MOD_RES     803    803       Phosphothreonine (By similarity).
FT   MOD_RES     813    813       Phosphoserine (By similarity).
FT   MOD_RES     815    815       Phosphoserine (By similarity).
FT   MOD_RES     824    824       Phosphoserine (By similarity).
FT   MOD_RES     827    827       Phosphoserine.
FT   MOD_RES     836    836       Phosphoserine (By similarity).
FT   MOD_RES     938    938       Phosphoserine (By similarity).
FT   MOD_RES    1072   1072       Phosphoserine (By similarity).
FT   MOD_RES    1171   1171       Phosphoserine (By similarity).
FT   VAR_SEQ     748    796       Missing (in isoform 2).
FT                                /FTId=VSP_015821.
FT   CONFLICT    301    301       V -> E (in Ref. 1; BAE38941 and 2;
FT                                AAH65052).
FT   CONFLICT    822    822       D -> G (in Ref. 1; BAC28779).
FT   CONFLICT    868    868       A -> V (in Ref. 2; AAH03958/AAH30859).
SQ   SEQUENCE   1305 AA;  143641 MW;  4FC416FE52650ED2 CRC64;
     MSLLQSALDF LAGPGSLGGA AGRDQSDFVG QTVELGELRL RVRRVLAEGG FAFVYEAQDL
     GSGREYALKR LLSNEEEKNR AIIQEVCFLK KLSGHPNIVQ FCSAASIGKE ESDTGQAEFL
     LLTELCKGQL VEFLKRVECK GPLSCDSILK IFYQTCRAVQ HMHRQKPPII HRDLKVENLL
     LSNQGTIKLC DFGSATTISH YPDYSWSAQK RAMVEEEITR NTTPMYRTPE IVDLYSNFPI
     GEKQDIWALG CILYLLCFRQ HPFEDGAKLR IVNGKYSIPV NDTRYTVFHD LIRAMLKVNP
     VERLSIAEVV RQLQEIAAAR NVNPKAPITE LLEQNGGYGN SGPSRAQPPC GGTVNSSGVL
     ALAEYDQPYG GFLDILRGGT ERLFTNLKDT SSKVIQSVAN YAKGDLDISY ITSRIAVMSF
     PAEGVESAIK NNIEDVRMFL DAKHPGHYAV YNLSPRIYRA SKFHNRVTEC GWAVRRAPHL
     HSLYTLCRSM HAWLREDHRN VCVVHCMDGR AASAVAVCAF LCFCRLFSTA EAAVYMFSMK
     RCPPGIWPSH KRYIEYVCDM VAEEPITPHS KPMLVKSVVM TPVPLFSKQR NGCRPFCEVY
     VGEERVTTTS QEYDRMKEFK IEDGKAVIPL GVTVQGDVLI IIYHARATLG GRLQAKMASM
     KMFQIQFHTG FVPRNATTVK FAKYDLDACD IQEKYPDLFQ VNLEVEVEPR DRPSREAPPW
     ENTSLRGLNP KILFSNREEQ QDILSKFGKP ELPRQPGSTA QYDAEAGSPE AEITESDSPQ
     SSSTDTNHFL HTLDWQEEKE PETGLDNTSP KESQSVLIAD GDGSEVSDEE EASFPSEERK
     PGAGEDTPRL AAGTKQQDLI FDVGMLAAPQ EPVQPEEGVD LLGLHSEGDL RPAAPLQACG
     VPSSNTDLLS CLLEPSDAAQ VGPPGDLLGG EAPLLLASPV SPLGLQNNLQ GKVPDTVDPF
     DQFLLSSNSD TQPCSKPDLF GEFLNSDSVA SSTAFPSTHS APPPSCSTAF LHLGDLPAEP
     SKVIASSSHP DLLGGWDTWA DTATPGPASI PVPEGTLFSS AGHPAPPGPN PSQTKSQNLD
     PFADLSDLSS SLQGLPAGLP AGGFVGAPAP TQKSNSPWQA NRPTAPGTSW TPQAKPAPRA
     SEQLRSHFSV IGAREERGVR VPSFAQKPKV SENDFEDLLP NQGFSKSDKK GPKTMAEMRK
     QELARDTDPL KLKLLDWIEG KERNIRALLS TLHTVLWDGE SRWTPVSMAD LVTPEQVKKQ
     YRRAVLVVHP DKATGQPYEQ YAKMIFMELN DAWSEFENQG SRPLF
//
ID   PA1_MOUSE               Reviewed;         253 AA.
AC   Q99L02;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=PAXIP1-associated protein 1;
DE   AltName: Full=PTIP-associated protein 1;
GN   Name=Pa1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
CC   -!- SUBUNIT: Interacts with PAXIP1/PTIP; the interaction is direct and
CC       is required for the association with the rest of the PTIP complex.
CC       Component of the MLL3/MLL4 complex at least composed of MLL3,
CC       MLL4, ASH2L, RBBP5, DPY30, WDR5, NCOA6, KDM6A, PAXIP1/PTIP and
CC       C16orf53/PA1 (By similarity).
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DR   EMBL; AK082775; BAC38614.1; -; mRNA.
DR   EMBL; BC003932; AAH03932.1; -; mRNA.
DR   IPI; IPI00116202; -.
DR   RefSeq; NP_084516.1; NM_030240.1.
DR   UniGene; Mm.345385; -.
DR   ProteinModelPortal; Q99L02; -.
DR   STRING; Q99L02; -.
DR   PhosphoSite; Q99L02; -.
DR   PRIDE; Q99L02; -.
DR   Ensembl; ENSMUST00000032918; ENSMUSP00000032918; ENSMUSG00000030680.
DR   GeneID; 67278; -.
DR   KEGG; mmu:67278; -.
DR   NMPDR; fig|10090.3.peg.17662; -.
DR   UCSC; uc009jtx.1; mouse.
DR   MGI; MGI:1914528; 2900092E17Rik.
DR   eggNOG; roNOG05667; -.
DR   GeneTree; ENSGT00390000016049; -.
DR   HOGENOM; HBG443931; -.
DR   HOVERGEN; HBG080642; -.
DR   InParanoid; Q99L02; -.
DR   OMA; ESEDWCV; -.
DR   OrthoDB; EOG4TMR32; -.
DR   PhylomeDB; Q99L02; -.
DR   NextBio; 324086; -.
DR   ArrayExpress; Q99L02; -.
DR   Bgee; Q99L02; -.
DR   CleanEx; MM_2900092E17RIK; -.
DR   Genevestigator; Q99L02; -.
DR   GermOnline; ENSMUSG00000030680; Mus musculus.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein.
FT   CHAIN         1    253       PAXIP1-associated protein 1.
FT                                /FTId=PRO_0000248335.
FT   COMPBIAS     47    159       Glu-rich.
FT   MOD_RES     202    202       N6-acetyllysine (By similarity).
FT   MOD_RES     236    236       Phosphoserine.
SQ   SEQUENCE   253 AA;  27723 MW;  AA5E4C4503A5C6FF CRC64;
     MSLALGHGTI AGSTAAPLSE EGEVTSGLQA LAVEDTGGPS VSASKAEEEG KGSQEEAGRE
     GSRPEEALEA PSAASDERAE GEAEDWCVPC SDEEVELPAN GQSWMPPPSE IQRLYELLAT
     QGTLELQAEI LPRRPPTPEA QSEEERSDEE PEAKEEEEEK PHMPTEFDFD DEPMTPKDSL
     IDRRRTPGSS ARSQKREARL DKVLSDMKRH KKLEEQILRT GRDLFSLDSE GPSPTSPPLR
     SSGNSLFPRQ RKY
//
ID   CDS2_MOUSE              Reviewed;         444 AA.
AC   Q99L43; Q3TMD1; Q6NSU1;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Phosphatidate cytidylyltransferase 2;
DE            EC=2.7.7.41;
DE   AltName: Full=CDP-DAG synthase 2;
DE   AltName: Full=CDP-DG synthase 2;
DE   AltName: Full=CDP-diacylglycerol synthase 2;
DE            Short=CDS 2;
DE   AltName: Full=CDP-diglyceride pyrophosphorylase 2;
DE   AltName: Full=CDP-diglyceride synthase 2;
DE   AltName: Full=CTP:phosphatidate cytidylyltransferase 2;
GN   Name=Cds2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Inglis S.L., Hunt D.M., Halford S.;
RT   "Isolation and characterization of murine Cds (CDP-diacylglycerol
RT   synthase) 1 and 2.";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryonic stem cell, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Embryo, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; THR-30; SER-32 AND
RP   SER-46, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
CC   -!- FUNCTION: Provides CDP-diacylglycerol an important precursor for
CC       the synthesis of phosphatidylinositol, phosphatidylglycerol, and
CC       cardiolipin (By similarity).
CC   -!- CATALYTIC ACTIVITY: CTP + phosphatidate = diphosphate + CDP-
CC       diacylglycerol.
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CC       CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC       membrane protein; Matrix side (Potential).
CC   -!- SIMILARITY: Belongs to the CDS family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AY159802; AAO17790.1; -; mRNA.
DR   EMBL; AK036328; BAC29384.1; -; mRNA.
DR   EMBL; AK147541; BAE27984.1; -; mRNA.
DR   EMBL; AK166001; BAE38511.1; -; mRNA.
DR   EMBL; BC003852; AAH03852.1; -; mRNA.
DR   EMBL; BC069879; AAH69879.1; -; mRNA.
DR   IPI; IPI00468999; -.
DR   RefSeq; NP_619592.1; NM_138651.6.
DR   UniGene; Mm.284503; -.
DR   STRING; Q99L43; -.
DR   PhosphoSite; Q99L43; -.
DR   PRIDE; Q99L43; -.
DR   Ensembl; ENSMUST00000103181; ENSMUSP00000099470; ENSMUSG00000058793.
DR   GeneID; 110911; -.
DR   KEGG; mmu:110911; -.
DR   NMPDR; fig|10090.3.peg.6963; -.
DR   UCSC; uc008mmo.1; mouse.
DR   CTD; 110911; -.
DR   MGI; MGI:1332236; Cds2.
DR   GeneTree; ENSGT00390000016175; -.
DR   HOGENOM; HBG629124; -.
DR   HOVERGEN; HBG002485; -.
DR   InParanoid; Q99L43; -.
DR   OMA; FNTLRSH; -.
DR   OrthoDB; EOG4V437K; -.
DR   PhylomeDB; Q99L43; -.
DR   BRENDA; 2.7.7.41; 244.
DR   NextBio; 364917; -.
DR   ArrayExpress; Q99L43; -.
DR   Bgee; Q99L43; -.
DR   Genevestigator; Q99L43; -.
DR   GermOnline; ENSMUSG00000058793; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IEA:EC.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000374; PC_trans.
DR   InterPro; IPR016720; PC_Trfase_euk.
DR   Pfam; PF01148; CTP_transf_1; 1.
DR   PIRSF; PIRSF018269; PC_trans_euk; 1.
DR   PROSITE; PS01315; CDS; 1.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Nucleotidyltransferase; Phospholipid biosynthesis; Phosphoprotein;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN         1    444       Phosphatidate cytidylyltransferase 2.
FT                                /FTId=PRO_0000090717.
FT   TRANSMEM     78     98       Helical; (Potential).
FT   TRANSMEM    129    149       Helical; (Potential).
FT   TRANSMEM    165    185       Helical; (Potential).
FT   TRANSMEM    212    232       Helical; (Potential).
FT   TRANSMEM    261    281       Helical; (Potential).
FT   TRANSMEM    339    359       Helical; (Potential).
FT   MOD_RES      20     20       Phosphoserine.
FT   MOD_RES      22     22       Phosphoserine (By similarity).
FT   MOD_RES      30     30       Phosphothreonine.
FT   MOD_RES      32     32       Phosphoserine.
FT   MOD_RES      36     36       Phosphoserine (By similarity).
FT   MOD_RES      46     46       Phosphoserine.
FT   CONFLICT     43     43       L -> P (in Ref. 3; AAH69879).
SQ   SEQUENCE   444 AA;  51314 MW;  6A3568A7E90A6C53 CRC64;
     MTELRQRVVR EDAPPEDKES ESEAKLDGET ASDSESRAET APLPTSVDDT PEVLNRALSN
     LSSRWKNWWV RGILTLAMIA FFFIIIYLGP MVLMMIVMCV QIKCFHEIIT IGYNVYHSYD
     LPWFRTLSWY FLLCVNYFFY GETVTDYFFT LVQREEPLRI LSKYHRFISF ALYLTGFCMF
     VLSLVKKHYR LQFYMFGWTH VTLLIVVTQS HLVIHNLFEG MIWFIVPISC VICNDIMAYM
     FGFFFGRTPL IKLSPKKTWE GFIGGFFATV VFGLLLSYVM SGYRCFVCPV EYNNDTNSFT
     VDCEPSDLFR LQEYNIPGVI QSAIGWKTVR MYPFQIHSIA LSTFASLIGP FGGFFASGFK
     RAFKIKDFAN TIPGHGGIMD RFDCQYLMAT FVNVYIASFI RGPNPSKLIQ QFLTLRPDQQ
     LHIFNTLKSH LTDKGILTSA LEDE
//
ID   IF2B_MOUSE              Reviewed;         331 AA.
AC   Q99L45; Q9CSH6; Q9CT12;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Eukaryotic translation initiation factor 2 subunit 2;
DE   AltName: Full=Eukaryotic translation initiation factor 2 subunit beta;
DE            Short=eIF-2-beta;
GN   Name=Eif2s2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION IN AN EIF2 COMPLEX WITH EIF2S1; CELF1; CALR; CALR3;
RP   HSPA5 AND HSP90B1.
RX   PubMed=16931514; DOI=10.1074/jbc.M605701200;
RA   Timchenko L.T., Salisbury E., Wang G.-L., Nguyen H., Albrecht J.H.,
RA   Hershey J.W., Timchenko N.A.;
RT   "Age-specific CUGBP1-eIF2 complex increases translation of
RT   CCAAT/enhancer-binding protein beta in old liver.";
RL   J. Biol. Chem. 281:32806-32819(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: eIF-2 functions in the early steps of protein synthesis
CC       by forming a ternary complex with GTP and initiator tRNA. This
CC       complex binds to a 40S ribosomal subunit, followed by mRNA binding
CC       to form a 43S preinitiation complex. Junction of the 60S ribosomal
CC       subunit to form the 80S initiation complex is preceded by
CC       hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP
CC       binary complex. In order for eIF-2 to recycle and catalyze another
CC       round of initiation, the GDP bound to eIF-2 must exchange with GTP
CC       by way of a reaction catalyzed by eIF-2B (By similarity).
CC   -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma
CC       chain (By similarity). Component of an EIF2 complex at least
CC       composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and
CC       HSPA5.
CC   -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB28490.2; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK011503; BAB27663.1; -; mRNA.
DR   EMBL; AK012817; BAB28490.2; ALT_INIT; mRNA.
DR   EMBL; BC003848; AAH03848.1; -; mRNA.
DR   IPI; IPI00116302; -.
DR   RefSeq; NP_080306.1; NM_026030.2.
DR   UniGene; Mm.377134; -.
DR   UniGene; Mm.470088; -.
DR   ProteinModelPortal; Q99L45; -.
DR   SMR; Q99L45; 172-311.
DR   STRING; Q99L45; -.
DR   PhosphoSite; Q99L45; -.
DR   PRIDE; Q99L45; -.
DR   Ensembl; ENSMUST00000099173; ENSMUSP00000096777; ENSMUSG00000074656.
DR   GeneID; 67204; -.
DR   KEGG; mmu:67204; -.
DR   NMPDR; fig|10090.3.peg.7232; -.
DR   UCSC; uc008njw.1; mouse.
DR   CTD; 67204; -.
DR   MGI; MGI:1914454; Eif2s2.
DR   GeneTree; ENSGT00390000001804; -.
DR   HOGENOM; HBG738095; -.
DR   HOVERGEN; HBG000927; -.
DR   InParanoid; Q99L45; -.
DR   OMA; ETQQSET; -.
DR   OrthoDB; EOG42Z4QJ; -.
DR   PhylomeDB; Q99L45; -.
DR   NextBio; 323872; -.
DR   ArrayExpress; Q99L45; -.
DR   Bgee; Q99L45; -.
DR   Genevestigator; Q99L45; -.
DR   GermOnline; ENSMUSG00000052825; Mus musculus.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003743; F:translation initiation factor activity; ISS:UniProtKB.
DR   InterPro; IPR002735; Transl_init_fac_IF2/IF5.
DR   InterPro; IPR016189; Transl_init_fac_IF2/IF5_N.
DR   InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd.
DR   Gene3D; G3DSA:3.30.30.50; G3DSA:3.30.30.50; 1.
DR   Pfam; PF01873; eIF-5_eIF-2B; 1.
DR   SMART; SM00653; eIF2B_5; 1.
DR   SUPFAM; SSF100966; Transl_init_fac_IF2/IF5_N; 1.
DR   SUPFAM; SSF75689; Transl_init_fac_IF2/IF5_Zn-bd; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Initiation factor; Metal-binding; Phosphoprotein;
KW   Protein biosynthesis; Zinc; Zinc-finger.
FT   CHAIN         1    331       Eukaryotic translation initiation factor
FT                                2 subunit 2.
FT                                /FTId=PRO_0000137407.
FT   ZN_FING     279    303       C4-type (Potential).
FT   COMPBIAS     14     21       Poly-Lys.
FT   COMPBIAS     79     87       Poly-Lys.
FT   COMPBIAS    124    129       Poly-Lys.
FT   MOD_RES       2      2       Phosphoserine (By similarity).
FT   MOD_RES      67     67       Phosphoserine.
FT   MOD_RES     105    105       Phosphoserine (By similarity).
FT   MOD_RES     263    263       N6-acetyllysine (By similarity).
FT   MOD_RES     291    291       N6-acetyllysine (By similarity).
SQ   SEQUENCE   331 AA;  38092 MW;  E91BEBBF330B7A5C CRC64;
     MSGDEMIFDP TMSKKKKKKK KPFMLDEEGD AQTEETQPSE TKEVEPEPTE EKDVDADEED
     SRKKDASDDL DDLNFFNQKK KKKKTKKIFD IDEAEEAIKD VKIESDAQEP AEPEDDLDIM
     LGNKKKKKKN VKFPEEDEIL EKDEALEDED SKKDDGISFS SQTAWAGSER DYTYEELLNR
     VFNIMREKNP DMVAGEKRKF VMKPPQVVRV GTKKTSFVNF TDICKLLHRQ PKHLLAFLLA
     ELGTSGSIDG NNQLVIKGRF QQKQIENVLR RYIKEYVTCH TCRSPDTILQ KDTRLYFLQC
     ETCHSRCSVA SIKTGFQAVT GKRAQLRAKA N
//
ID   SNTB1_MOUSE             Reviewed;         537 AA.
AC   Q99L88; O35925;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Beta-1-syntrophin;
DE   AltName: Full=59 kDa dystrophin-associated protein A1 basic component 1;
DE            Short=DAPA1B;
DE   AltName: Full=Syntrophin-2;
GN   Name=Sntb1; Synonyms=Snt2b1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH DMD; DTNA AND UTRN.
RX   MEDLINE=97362062; PubMed=9214383; DOI=10.1083/jcb.138.1.81;
RA   Peters M.F., Adams M.E., Froehner S.C.;
RT   "Differential association of syntrophin pairs with the dystrophin
RT   complex.";
RL   J. Cell Biol. 138:81-93(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH SCN4A AND SCN5A.
RX   MEDLINE=98075111; PubMed=9412493;
RA   Gee S.H., Madhavan R., Levinson S.R., Caldwell J.H., Sealock R.,
RA   Froehner S.C.;
RT   "Interaction of muscle and brain sodium channels with multiple members
RT   of the syntrophin family of dystrophin-associated proteins.";
RL   J. Neurosci. 18:128-137(1998).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; THR-73; THR-213;
RP   SER-218 AND SER-235, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-218, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Adapter protein that binds to and probably organizes the
CC       subcellular localization of a variety of membrane proteins. May
CC       link various receptors to the actin cytoskeleton and the
CC       dystrophin glycoprotein complex.
CC   -!- SUBUNIT: Monomer and homodimer (Probable). Interacts with the
CC       viral HTLV-1 TAX protein and other members of the syntrophin
CC       family: SNTA1 and SNTB2 (By similarity). Interacts with the
CC       dystrophin protein DMD and related proteins DTNA and UTRN and with
CC       the sodium channel proteins SCN4A and SCN5A.
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Peripheral
CC       membrane protein; Cytoplasmic side. Cell junction. Cytoplasm,
CC       cytoskeleton. Note=In skeletal muscle, it localizes at the
CC       cytoplasmic side of the sarcolemmal membrane and at neuromuscular
CC       junctions.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99L88-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99L88-2; Sequence=VSP_006356, VSP_006357;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at high levels in the
CC       liver.
CC   -!- DOMAIN: The PH 1 domain mediates the oligomerization in a calcium
CC       dependent manner (By similarity).
CC   -!- DOMAIN: The PDZ domain binds to the last three or four amino acids
CC       of ion channels and receptor proteins. The association with
CC       dystrophin or related proteins probably leaves the PDZ domain
CC       available to recruit proteins to the membrane (By similarity).
CC   -!- DOMAIN: The SU domain binds calmodulin in a calcium-dependent
CC       manner (By similarity).
CC   -!- PTM: Phosphorylated by CaM-kinase II (By similarity).
CC   -!- SIMILARITY: Belongs to the syntrophin family.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -!- SIMILARITY: Contains 1 SU (syntrophin unique) domain.
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DR   EMBL; U89997; AAB66697.1; -; mRNA.
DR   EMBL; BC003748; AAH03748.1; -; mRNA.
DR   IPI; IPI00116414; -.
DR   IPI; IPI00230613; -.
DR   RefSeq; NP_057876.1; NM_016667.3.
DR   UniGene; Mm.309425; -.
DR   ProteinModelPortal; Q99L88; -.
DR   SMR; Q99L88; 15-298.
DR   STRING; Q99L88; -.
DR   PhosphoSite; Q99L88; -.
DR   PRIDE; Q99L88; -.
DR   Ensembl; ENSMUST00000039769; ENSMUSP00000041294; ENSMUSG00000060429.
DR   Ensembl; ENSMUST00000110200; ENSMUSP00000105829; ENSMUSG00000060429.
DR   GeneID; 20649; -.
DR   KEGG; mmu:20649; -.
DR   UCSC; uc007vsk.1; mouse.
DR   CTD; 20649; -.
DR   MGI; MGI:101781; Sntb1.
DR   eggNOG; roNOG13535; -.
DR   GeneTree; ENSGT00550000074581; -.
DR   HOGENOM; HBG314224; -.
DR   HOVERGEN; HBG054204; -.
DR   InParanoid; Q99L88; -.
DR   OMA; CHASAEM; -.
DR   OrthoDB; EOG4BRWKJ; -.
DR   NextBio; 299067; -.
DR   ArrayExpress; Q99L88; -.
DR   Bgee; Q99L88; -.
DR   CleanEx; MM_SNTB1; -.
DR   Genevestigator; Q99L88; -.
DR   GermOnline; ENSMUSG00000060429; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR015482; Syntrophin.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   PANTHER; PTHR10554; Syntrophin; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00233; PH; 2.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Alternative splicing; Calcium;
KW   Calmodulin-binding; Cell junction; Cell membrane; Cytoplasm;
KW   Cytoskeleton; Membrane; Phosphoprotein; Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    537       Beta-1-syntrophin.
FT                                /FTId=PRO_0000184010.
FT   DOMAIN       18    297       PH 1.
FT   DOMAIN      111    194       PDZ.
FT   DOMAIN      321    432       PH 2.
FT   DOMAIN      481    537       SU.
FT   REGION      517    537       Calmodulin-binding (By similarity).
FT   COMPBIAS      2     12       Poly-Ala.
FT   COMPBIAS     13     16       Poly-Gly.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      71     71       Phosphoserine.
FT   MOD_RES      73     73       Phosphothreonine.
FT   MOD_RES      86     86       Phosphoserine.
FT   MOD_RES     213    213       Phosphothreonine.
FT   MOD_RES     218    218       Phosphoserine.
FT   MOD_RES     235    235       Phosphoserine.
FT   MOD_RES     388    388       Phosphoserine (By similarity).
FT   VAR_SEQ     262    276       RQLEIHSPDAKHTVI -> STHPSDLIPIQGWAA (in
FT                                isoform 2).
FT                                /FTId=VSP_006356.
FT   VAR_SEQ     277    537       Missing (in isoform 2).
FT                                /FTId=VSP_006357.
SQ   SEQUENCE   537 AA;  58081 MW;  91A5E4DD0A97A665 CRC64;
     MAVAAAAVAA PAGGGGARAQ RSGLLEVLVR DRWHKVLVNL SEDALVLSCE EGAAAYNGIG
     AATNGSFCRG SGTGHPVPGV AQAPDSPAGV RTAFTDLPEQ VPESISNQKR GVKVLKQELG
     GLGISIKGGK ENKMPILISK IFKGLAADQT QALYVGDAIL SVNGADLRDA THDEAVQALK
     RAGKEVLLEV KYMREATPYV KKGSPVSEIG WETPPPESPR LGGGSAEPLS SQSFSFHRDR
     KSIPLKMCYV TRNMTLADPE NRQLEIHSPD AKHTVILRSK DSATAQAWFS AIHSNAGDLL
     TRVVADIREQ LGKTGIAGSR EIRHLGWLAE KVPGESEKQW KPALVVLTEK DLLIYDSMPR
     RKEAWFSPVH SYPLLATRLV HSGPGKGSPQ AGMDLSFATR TGTKQGIETH LFRAEISRDL
     SHWTRSIVQG CHNSAELTAE ITTACTYRNQ ECRLTIHYDN GFSISTEPQD GAFPKTIIQS
     PYEKLKMSSD DGIRMLYLDF GGKEGEIQLD LHSCPKPIVF IIHSFLSAKI TRLGLVA
//
ID   MCRS1_MOUSE             Reviewed;         462 AA.
AC   Q99L90; O35255; Q32P11;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Microspherule protein 1;
DE   AltName: Full=58 kDa microspherule protein;
GN   Name=Mcrs1; Synonyms=Msp58;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98316645; PubMed=9654073;
RX   DOI=10.1046/j.1432-1327.1998.2530734.x;
RA   Ren Y., Busch R.K., Perlaky L., Busch H.;
RT   "The 58-kDa microspherule protein (MSP58), a nucleolar protein,
RT   interacts with nucleolar protein p120.";
RL   Eur. J. Biochem. 253:734-742(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, Mammary tumor, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Modulates the transcription repressor activity of DAXX
CC       by recruiting it to the nucleolus (By similarity). May be an
CC       inhibitor of TERT telomerase activity.
CC   -!- SUBUNIT: Binds to NOP2, DAXX, PINX1 and TERT. Component of the
CC       chromatin-remodeling INO80 complex, at least composed of ACTL6A,
CC       ACTR5, ACTR8, RVBL1, RVBL2, INO80, INO80B, INO80C, INO80D and
CC       INO80E. Component of some MLL1/MLL complex, at least composed of
CC       the core components MLL, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as
CC       well as the facultative components C17orf49, CHD8, E2F6, HSP70,
CC       IN80C, KIAA1267, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20,
CC       PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6,
CC       TAF7, TAF9 and TEX10. Interacts with CCDC85B (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains 1 FHA domain.
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DR   EMBL; AF015309; AAC53590.1; -; mRNA.
DR   EMBL; AK088116; BAC40155.1; -; mRNA.
DR   EMBL; BC003746; AAH03746.1; -; mRNA.
DR   EMBL; BC085099; AAH85099.1; -; mRNA.
DR   EMBL; BC108340; AAI08341.1; -; mRNA.
DR   IPI; IPI00320267; -.
DR   RefSeq; NP_001157628.1; NM_001164156.1.
DR   RefSeq; NP_058046.2; NM_016766.3.
DR   UniGene; Mm.383472; -.
DR   ProteinModelPortal; Q99L90; -.
DR   SMR; Q99L90; 346-443.
DR   STRING; Q99L90; -.
DR   PhosphoSite; Q99L90; -.
DR   PRIDE; Q99L90; -.
DR   Ensembl; ENSMUST00000041190; ENSMUSP00000043901; ENSMUSG00000037570.
DR   GeneID; 51812; -.
DR   KEGG; mmu:51812; -.
DR   UCSC; uc007xpb.1; mouse.
DR   CTD; 51812; -.
DR   MGI; MGI:1858420; Mcrs1.
DR   eggNOG; roNOG04529; -.
DR   GeneTree; ENSGT00390000005536; -.
DR   HOGENOM; HBG713280; -.
DR   HOVERGEN; HBG052434; -.
DR   InParanoid; Q99L90; -.
DR   OMA; IQERWYA; -.
DR   OrthoDB; EOG4BCDN0; -.
DR   PhylomeDB; Q99L90; -.
DR   NextBio; 308068; -.
DR   Bgee; Q99L90; -.
DR   CleanEx; MM_MCRS1; -.
DR   Genevestigator; Q99L90; -.
DR   GermOnline; ENSMUSG00000037570; Mus musculus.
DR   GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR008984; SMAD_FHA_domain.
DR   Gene3D; G3DSA:2.60.200.20; FHA; 1.
DR   Pfam; PF00498; FHA; 1.
DR   SMART; SM00240; FHA; 1.
DR   SUPFAM; SSF49879; SMAD_FHA; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Nucleus; Phosphoprotein.
FT   CHAIN         1    462       Microspherule protein 1.
FT                                /FTId=PRO_0000096306.
FT   DOMAIN      363    419       FHA.
FT   COILED      301    335       Potential.
FT   MOTIF       113    123       Nuclear localization signal (Potential).
FT   COMPBIAS     11    102       Ser-rich.
FT   MOD_RES      22     22       Phosphoserine (By similarity).
FT   MOD_RES     102    102       Phosphoserine (By similarity).
FT   MOD_RES     103    103       Phosphothreonine (By similarity).
FT   MOD_RES     108    108       Phosphoserine (By similarity).
FT   MOD_RES     123    123       N6-acetyllysine (By similarity).
FT   MOD_RES     130    130       N6-acetyllysine (By similarity).
FT   MOD_RES     282    282       Phosphoserine.
FT   CONFLICT    193    193       R -> K (in Ref. 1; AAC53590).
FT   CONFLICT    274    274       K -> R (in Ref. 1; AAC53590).
FT   CONFLICT    298    298       D -> N (in Ref. 1; AAC53590).
FT   CONFLICT    314    315       RE -> QK (in Ref. 1; AAC53590).
FT   CONFLICT    368    368       A -> T (in Ref. 1; AAC53590).
SQ   SEQUENCE   462 AA;  51692 MW;  47A73672270E2014 CRC64;
     MDKDSQGLLD SSLMASGTAS RSEDEESLAG QKRASSQALG TIPKRRSSSR FIKRKKFDDE
     LVESSLAKSS TRVKGAGGVE SGRCSGSEPS SSEKKKVSKA PSTPVPPSPA PTPGLTKRVK
     KSKQPLQVTK DLGRWKPADD LLLINAVLQT NDLTSVHLGV KFSCRFTLRE VQERWYALLY
     DPVISKLACQ AMRQLHPEAI AAIQSKALFS KAEEQLLSKV GSSSQPTLET FQDLLHTHPD
     AFYLARTAKA LQAHWQLMKQ YYLLEDQTVQ PLPKGDQVLN FSDAEDLIDD SKLKDMRDEV
     LEHELTVADR RQKREIRQLE QELHKWQVLV DSITGMGSPD FDNQTLAVLR GRMVRYLMRS
     REITLGRATK DNQIDVDLSL EGPAWKISRK QGVIKLKNNG DFFIANEGRR PIYIDGRPVL
     CGSKWRLSNN SVVEIASLRF VFLINQDLIA LIRAEAAKIT PQ
//
ID   CSN1_MOUSE              Reviewed;         471 AA.
AC   Q99LD4; B0QZT1; Q8C2J7;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-FEB-2011, entry version 70.
DE   RecName: Full=COP9 signalosome complex subunit 1;
DE            Short=SGN1;
DE            Short=Signalosome subunit 1;
DE   AltName: Full=G protein pathway suppressor 1;
DE            Short=GPS-1;
DE   AltName: Full=JAB1-containing signalosome subunit 1;
GN   Name=Gps1; Synonyms=Cops1, Csn1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION IN THE CSN COMPLEX.
RC   STRAIN=C57BL/6;
RX   MEDLINE=98372877; PubMed=9707402; DOI=10.1016/S0960-9822(07)00372-7;
RA   Wei N., Tsuge T., Serino G., Dohmae N., Takio K., Matsui M.,
RA   Deng X.-W.;
RT   "The COP9 complex is conserved between plants and mammals and is
RT   related to the 26S proteasome regulatory complex.";
RL   Curr. Biol. 8:919-922(1998).
RN   [5]
RP   INTERACTION WITH CAPN8, DOMAIN, AND TISSUE SPECIFICITY.
RX   PubMed=16476741; DOI=10.1074/jbc.M509244200;
RA   Hata S., Koyama S., Kawahara H., Doi N., Maeda T.,
RA   Toyama-Sorimachi N., Abe K., Suzuki K., Sorimachi H.;
RT   "Stomach-specific calpain, nCL-2, localizes in mucus cells and
RT   proteolyzes the beta-subunit of coatomer complex, beta-COP.";
RL   J. Biol. Chem. 281:11214-11224(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-459 AND SER-463, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-454; THR-459 AND
RP   SER-463, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
CC   -!- FUNCTION: Essential component of the COP9 signalosome complex
CC       (CSN), a complex involved in various cellular and developmental
CC       processes. The CSN complex is an essential regulator of the
CC       ubiquitin (Ubl) conjugation pathway by mediating the deneddylation
CC       of the cullin subunits of SCF-type E3 ligase complexes, leading to
CC       decrease the Ubl ligase activity of SCF-type complexes such as
CC       SCF, CSA or DDB2. The complex is also involved in phosphorylation
CC       of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP,
CC       possibly via its association with CK2 and PKD kinases. CSN-
CC       dependent phosphorylation of TP53 and JUN promotes and protects
CC       degradation by the Ubl system, respectively. Suppresses G-protein-
CC       and mitogen-activated protein kinase-mediated signal transduction
CC       (By similarity).
CC   -!- SUBUNIT: Component of the CSN complex, composed of COPS1/GPS1,
CC       COPS2, COPS3, COPS4, COPS5, COP6, COPS7 (COPS7A or COPS7B) and
CC       COPS8. In the complex, it probably interacts directly with COPS2,
CC       COPS3, COPS4 and CSN5. Interacts directly with inositol kinase
CC       ITPK1 (By similarity). Interacts with CAPN8.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99LD4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99LD4-2; Sequence=VSP_011883;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in the base region of the oxyntic
CC       and pyloric mucosae.
CC   -!- DOMAIN: The PCI domain is necessary and sufficient for the
CC       interactions with other CSN subunits of the complex (By
CC       similarity). Mediates the interaction with CAPN8.
CC   -!- DOMAIN: The N-terminal part (1-196), which is not required for
CC       deneddylating activity and CSN complex formation, is nevertheless
CC       essential for other aspects of CSN complex function, such as
CC       repression of c-fos/FOS expression (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Belongs to the CSN1 family.
CC   -!- SIMILARITY: Contains 1 PCI domain.
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DR   EMBL; AK088490; BAC40386.1; -; mRNA.
DR   EMBL; AL663090; CAQ12769.1; -; Genomic_DNA.
DR   EMBL; BC003350; AAH03350.1; -; mRNA.
DR   IPI; IPI00116793; -.
DR   IPI; IPI00968372; -.
DR   UniGene; Mm.30195; -.
DR   UniGene; Mm.310704; -.
DR   ProteinModelPortal; Q99LD4; -.
DR   STRING; Q99LD4; -.
DR   PhosphoSite; Q99LD4; -.
DR   PRIDE; Q99LD4; -.
DR   Ensembl; ENSMUST00000106143; ENSMUSP00000101749; ENSMUSG00000025156.
DR   Ensembl; ENSMUST00000116305; ENSMUSP00000112007; ENSMUSG00000025156.
DR   UCSC; uc007muo.1; mouse.
DR   UCSC; uc007mup.1; mouse.
DR   MGI; MGI:2384801; Gps1.
DR   eggNOG; roNOG09020; -.
DR   GeneTree; ENSGT00510000046608; -.
DR   HOVERGEN; HBG030722; -.
DR   PhylomeDB; Q99LD4; -.
DR   NextBio; 372621; -.
DR   Bgee; Q99LD4; -.
DR   CleanEx; MM_GPS1; -.
DR   Genevestigator; Q99LD4; -.
DR   GermOnline; ENSMUSG00000025156; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008180; C:signalosome; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR019585; 26S_proteasome_reg_su-Rpn7.
DR   InterPro; IPR000717; PCI_dom.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF01399; PCI; 1.
DR   Pfam; PF10602; RPN7; 1.
DR   SMART; SM00088; PINT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW   Signalosome.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    471       COP9 signalosome complex subunit 1.
FT                                /FTId=PRO_0000120960.
FT   DOMAIN      240    408       PCI.
FT   MOD_RES     357    357       Phosphotyrosine (By similarity).
FT   MOD_RES     447    447       N6-acetyllysine (By similarity).
FT   MOD_RES     448    448       Phosphoserine (By similarity).
FT   MOD_RES     454    454       Phosphoserine.
FT   MOD_RES     459    459       Phosphothreonine.
FT   MOD_RES     463    463       Phosphoserine.
FT   MOD_RES     468    468       Phosphoserine (By similarity).
FT   VAR_SEQ     448    471       SPPREGSQGELTPANSQSRMSTNM -> VKSLGCEGMGGTH
FT                                TASTEPSLSTAVSS (in isoform 2).
FT                                /FTId=VSP_011883.
SQ   SEQUENCE   471 AA;  53442 MW;  578A269A8FF63D61 CRC64;
     MQIDVDPQED PQNAPDVNYV VENPTLDLEQ YAASYSGLMR IERLQFIADR CPPLRVEALK
     MALSFVQRTF NVDMYEEIHR KLSEATRELQ NAPDAIPESG VEPPPLDTAW VEATRKKALL
     KLEKLDTDLK NYKGNSIKES IRRGHDDLGD HYLDCGDLSN ALKCYSRARD YCTSAKHVIN
     MCLNVIKVSV YLQNWSHVLS YVSKAESTPE IAEQRGERDS QTQAILTKLK CAAGLAELAA
     RKYKQAAKCF LLASFDHCDF PELLSPSNVA VYGGLCALAT FDRQELQRNV ISSSSFKLFL
     ELEPQVRDII FKFYESKYAS CLKMLDEMKD NLLLDMYLAP HVRTLYTQIR NRALIQYFSP
     YVSADMHKMA AAFNTTVAAL EDELTQLILE GLINARIDSH SKILYARDVD QRSTTFEKSL
     LMGKEFQRRA KAMILRAAVL RNQIHVKSPP REGSQGELTP ANSQSRMSTN M
//
ID   DDAH2_MOUSE             Reviewed;         285 AA.
AC   Q99LD8;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=N(G),N(G)-dimethylarginine dimethylaminohydrolase 2;
DE            Short=DDAH-2;
DE            Short=Dimethylarginine dimethylaminohydrolase 2;
DE            EC=3.5.3.18;
DE   AltName: Full=DDAHII;
DE   AltName: Full=Dimethylargininase-2;
GN   Name=Ddah2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PROTEIN SEQUENCE OF 183-194, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and
CC       N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS.
CC       Has therefore a role in the regulation of nitric oxide generation
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: N(omega),N(omega)-dimethyl-L-arginine + H(2)O
CC       = dimethylamine + L-citrulline.
CC   -!- SIMILARITY: Belongs to the DDAH family.
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DR   EMBL; BC003328; AAH03328.1; -; mRNA.
DR   IPI; IPI00336881; -.
DR   RefSeq; NP_001177378.1; NM_001190449.1.
DR   UniGene; Mm.1457; -.
DR   ProteinModelPortal; Q99LD8; -.
DR   SMR; Q99LD8; 10-279.
DR   STRING; Q99LD8; -.
DR   REPRODUCTION-2DPAGE; IPI00336881; -.
DR   UCD-2DPAGE; Q99LD8; -.
DR   PRIDE; Q99LD8; -.
DR   Ensembl; ENSMUST00000007255; ENSMUSP00000007255; ENSMUSG00000007039.
DR   GeneID; 51793; -.
DR   KEGG; mmu:51793; -.
DR   NMPDR; fig|10090.3.peg.2760; -.
DR   UCSC; uc008cfi.1; mouse.
DR   CTD; 51793; -.
DR   MGI; MGI:1859016; Ddah2.
DR   GeneTree; ENSGT00390000009331; -.
DR   HOGENOM; HBG714724; -.
DR   HOVERGEN; HBG055937; -.
DR   InParanoid; Q99LD8; -.
DR   OMA; PTACSEA; -.
DR   OrthoDB; EOG4QJRP2; -.
DR   PhylomeDB; Q99LD8; -.
DR   BRENDA; 3.5.3.18; 244.
DR   ArrayExpress; Q99LD8; -.
DR   Bgee; Q99LD8; -.
DR   CleanEx; MM_DDAH2; -.
DR   Genevestigator; Q99LD8; -.
DR   GermOnline; ENSMUSG00000007039; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016403; F:dimethylargininase activity; ISS:UniProtKB.
DR   GO; GO:0000052; P:citrulline metabolic process; ISS:UniProtKB.
DR   InterPro; IPR003198; Amidino_trans.
DR   Pfam; PF02274; Amidinotransf; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase.
FT   CHAIN         1    285       N(G),N(G)-dimethylarginine
FT                                dimethylaminohydrolase 2.
FT                                /FTId=PRO_0000171122.
FT   ACT_SITE    171    171       Proton donor (By similarity).
FT   ACT_SITE    276    276       Nucleophile (Potential).
SQ   SEQUENCE   285 AA;  29646 MW;  3795D0BA2D314EE5 CRC64;
     MGTPGEGLGR CSHALIRGVP ESLASGEGAG AGLPALDLAK AQREHGVLGG KLRQRLGLQL
     LELPPEESLP LGPLLGDTAV IQGDTALITR PWSPARRPEV DGVRKALQDL GLRIVEMGDE
     NATLDGTDVL FTGREFFVGL SKWTNHRGAE IVADTFRDFA VSTVPVSGSS HLRGLCGMGG
     PRTVVAGSSE AAQKAVRAMA ALTDHPYASL TLPDDAASDC LFLRPGLPGA TPFLLHRGGG
     DLPNSQEALQ KLSDVTLVPV SCSELEKAGA GLSSLCLVLS TRPHC
//
ID   CV028_MOUSE             Reviewed;         505 AA.
AC   Q99LF4; Q3TA04; Q3TI25; Q3UDW6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=UPF0027 protein C22orf28 homolog;
GN   Name=D10Wsu52e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RA   Ding N.-Z., He M., Hu J.S., He C.-Q., Sun Y.H., Chen J.G.;
RT   "Cloning of the mouse P55 gene.";
RL   Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, DBA/2, and NOD;
RC   TISSUE=Embryo, Macrophage, Placenta, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the UPF0027 (rtcB) family.
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DR   EMBL; AY424364; AAR02005.1; -; mRNA.
DR   EMBL; AK145891; BAE26729.1; -; mRNA.
DR   EMBL; AK145916; BAE26747.1; -; mRNA.
DR   EMBL; AK149885; BAE29145.1; -; mRNA.
DR   EMBL; AK150376; BAE29508.1; -; mRNA.
DR   EMBL; AK150470; BAE29587.1; -; mRNA.
DR   EMBL; AK151042; BAE30059.1; -; mRNA.
DR   EMBL; AK151182; BAE30183.1; -; mRNA.
DR   EMBL; AK151932; BAE30808.1; -; mRNA.
DR   EMBL; AK152144; BAE30981.1; -; mRNA.
DR   EMBL; AK153434; BAE31991.1; -; mRNA.
DR   EMBL; AK168038; BAE40021.1; -; mRNA.
DR   EMBL; AK172175; BAE42866.1; -; mRNA.
DR   EMBL; BC003288; AAH03288.1; -; mRNA.
DR   IPI; IPI00116850; -.
DR   RefSeq; NP_663397.1; NM_145422.4.
DR   UniGene; Mm.9257; -.
DR   ProteinModelPortal; Q99LF4; -.
DR   SMR; Q99LF4; 11-505.
DR   STRING; Q99LF4; -.
DR   PhosphoSite; Q99LF4; -.
DR   PRIDE; Q99LF4; -.
DR   Ensembl; ENSMUST00000001834; ENSMUSP00000001834; ENSMUSG00000001783.
DR   GeneID; 28088; -.
DR   KEGG; mmu:28088; -.
DR   UCSC; uc007gni.1; mouse.
DR   CTD; 28088; -.
DR   MGI; MGI:106379; D10Wsu52e.
DR   eggNOG; roNOG05785; -.
DR   GeneTree; ENSGT00390000015260; -.
DR   HOGENOM; HBG364447; -.
DR   HOVERGEN; HBG081383; -.
DR   InParanoid; Q99LF4; -.
DR   OMA; AQSLFDH; -.
DR   PhylomeDB; Q99LF4; -.
DR   NextBio; 306634; -.
DR   ArrayExpress; Q99LF4; -.
DR   Bgee; Q99LF4; -.
DR   Genevestigator; Q99LF4; -.
DR   GermOnline; ENSMUSG00000001783; Mus musculus.
DR   InterPro; IPR001233; UPF0027.
DR   PANTHER; PTHR11118; UPF0027; 1.
DR   Pfam; PF01139; UPF0027; 1.
DR   SUPFAM; SSF103365; UPF0027; 1.
DR   PROSITE; PS01288; UPF0027; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Phosphoprotein.
FT   CHAIN         1    505       UPF0027 protein C22orf28 homolog.
FT                                /FTId=PRO_0000255243.
FT   MOD_RES     439    439       Phosphoserine (By similarity).
FT   MOD_RES     496    496       N6-acetyllysine (By similarity).
FT   CONFLICT     30     30       M -> V (in Ref. 2; BAE42866).
FT   CONFLICT    125    125       R -> H (in Ref. 2; BAE42866).
FT   CONFLICT    165    165       A -> V (in Ref. 2; BAE40021).
FT   CONFLICT    178    178       W -> R (in Ref. 2; BAE29145).
FT   CONFLICT    205    205       N -> S (in Ref. 2; BAE42866).
SQ   SEQUENCE   505 AA;  55249 MW;  3488A9BF91460480 CRC64;
     MSRNYNDELQ FLDKINKNCW RIKKGFVPNM QVEGVFYVND ALEKLMFEEL RNACRGGGVG
     GFLPAMKQIG NVAALPGIVH RSIGLPDVHS GYGFAIGNMA AFDMNDPEAV VSPGGVGFDI
     NCGVRLLRTN LDESDVQPVK EQLAQAMFDH IPVGVGSKGV IPMNAKDLEE ALEMGVDWSL
     REGYAWAEDK EHCEEYGRML QADPNKVSPR AKKRGLPQLG TLGAGNHYAE IQVVDEIFNE
     YAAKKMGIDH KGQVCVMIHS GSRGLGHQVA TDALVAMEKA MKRDKIIVND RQLACARIAS
     PEGQDYLKGM AAAGNYAWVN RSSMTFLTRQ AFAKVFNTTP DDLDLHVIYD VSHNIAKVEQ
     HVVDGKERTL LVHRKGSTRA FPPHHPLIAV DYQLTGQPVL IGGTMGTCSY VLTGTEQGMT
     ETFGTTCHGA GRALSRAKSR RNLDFQDVLD KLADMGIAIR VASPKLVMEE APESYKNVTD
     VVNTCHDAGI SKKAIKLRPI AVIKG
//
ID   TMM51_MOUSE             Reviewed;         249 AA.
AC   Q99LG1; Q3TPZ3;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Transmembrane protein 51;
GN   Name=Tmem51;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109 AND SER-114, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-188, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
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DR   EMBL; AK077758; BAC36994.1; -; mRNA.
DR   EMBL; AK164026; BAE37592.1; -; mRNA.
DR   EMBL; BC003277; AAH03277.1; -; mRNA.
DR   IPI; IPI00116876; -.
DR   RefSeq; NP_663377.1; NM_145402.3.
DR   UniGene; Mm.27587; -.
DR   ProteinModelPortal; Q99LG1; -.
DR   PhosphoSite; Q99LG1; -.
DR   PRIDE; Q99LG1; -.
DR   Ensembl; ENSMUST00000036572; ENSMUSP00000042919; ENSMUSG00000040616.
DR   GeneID; 214359; -.
DR   KEGG; mmu:214359; -.
DR   UCSC; uc008vpr.1; mouse.
DR   CTD; 214359; -.
DR   MGI; MGI:2384874; Tmem51.
DR   GeneTree; ENSGT00390000009278; -.
DR   HOGENOM; HBG443721; -.
DR   HOVERGEN; HBG061167; -.
DR   InParanoid; Q99LG1; -.
DR   OMA; AQGNKTE; -.
DR   OrthoDB; EOG4F1X49; -.
DR   PhylomeDB; Q99LG1; -.
DR   NextBio; 374278; -.
DR   ArrayExpress; Q99LG1; -.
DR   Bgee; Q99LG1; -.
DR   CleanEx; MM_TMEM51; -.
DR   Genevestigator; Q99LG1; -.
DR   GermOnline; ENSMUSG00000040616; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    249       Transmembrane protein 51.
FT                                /FTId=PRO_0000072578.
FT   TRANSMEM     17     37       Helical; (Potential).
FT   TRANSMEM     64     84       Helical; (Potential).
FT   MOD_RES     109    109       Phosphoserine.
FT   MOD_RES     114    114       Phosphoserine.
FT   MOD_RES     188    188       Phosphoserine.
FT   MOD_RES     230    230       Phosphothreonine (By similarity).
SQ   SEQUENCE   249 AA;  27398 MW;  5A9BA7C95C6286A8 CRC64;
     MMAQSKANGS HYALTAIGLG MLVLGVIMAM WNLVPGFSPA DKPTSQGNKT EGGGGILKSK
     TFSVAYVLVG AGMMLLLLAI CLSIRDKRRM RQSEELARIQ QQAGTVPHSQ EEDSQEEEED
     VSSRYYVPSY EEVMNTGYPE TRGQEQNPRL SISLPSYESL TGLDEATPTS TRAETETSPG
     HAPDRQNSKL AKRLKPLKVR RIKSEKLHLK DFRITLPDKN VPPPSIEPLT PPPLYDEVQA
     KAPDARPPD
//
ID   PTSS1_MOUSE             Reviewed;         473 AA.
AC   Q99LH2; O55024; Q3UV14; Q8C2S8;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Phosphatidylserine synthase 1;
DE            Short=PSS-1;
DE            Short=PtdSer synthase 1;
DE            EC=2.7.8.-;
DE   AltName: Full=Serine-exchange enzyme I;
GN   Name=Ptdss1; Synonyms=Pssa;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   TISSUE=Liver;
RX   MEDLINE=98184830; PubMed=9516423; DOI=10.1074/jbc.273.13.7293;
RA   Stone S.J., Cui Z., Vance J.E.;
RT   "Cloning and expression of mouse liver phosphatidylserine synthase-1
RT   cDNA. Overexpression in rat hepatoma cells inhibits the CDP-
RT   ethanolamine pathway for phosphatidylethanolamine biosynthesis.";
RL   J. Biol. Chem. 273:7293-7302(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart, Oviduct, Thymus, and Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Catalyzes a base-exchange reaction in which the polar
CC       head group of phosphatidylcholine is replaced by L-serine.
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylserine biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- MISCELLANEOUS: May provide a precursor for the biosynthesis of
CC       phosphatidylethanolamine. Phosphatidylserine can be decarboxylated
CC       to phosphatidylethanolamine.
CC   -!- SIMILARITY: Belongs to the phosphatidyl serine synthase family.
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DR   EMBL; AF042731; AAB97845.1; -; mRNA.
DR   EMBL; AK036990; BAC29660.1; -; mRNA.
DR   EMBL; AK054101; BAC35656.1; -; mRNA.
DR   EMBL; AK085857; BAC39555.1; -; mRNA.
DR   EMBL; AK088048; BAC40117.1; -; mRNA.
DR   EMBL; AK137681; BAE23459.1; -; mRNA.
DR   EMBL; BC003260; AAH03260.1; -; mRNA.
DR   IPI; IPI00320378; -.
DR   RefSeq; NP_032985.2; NM_008959.3.
DR   UniGene; Mm.281464; -.
DR   STRING; Q99LH2; -.
DR   PhosphoSite; Q99LH2; -.
DR   PRIDE; Q99LH2; -.
DR   Ensembl; ENSMUST00000021990; ENSMUSP00000021990; ENSMUSG00000021518.
DR   GeneID; 19210; -.
DR   KEGG; mmu:19210; -.
DR   UCSC; uc007qzz.1; mouse.
DR   CTD; 19210; -.
DR   MGI; MGI:1276575; Ptdss1.
DR   eggNOG; roNOG09319; -.
DR   GeneTree; ENSGT00530000063576; -.
DR   HOVERGEN; HBG053765; -.
DR   InParanoid; Q99LH2; -.
DR   OMA; EFFYRPH; -.
DR   OrthoDB; EOG4PNXGW; -.
DR   PhylomeDB; Q99LH2; -.
DR   NextBio; 295952; -.
DR   ArrayExpress; Q99LH2; -.
DR   Bgee; Q99LH2; -.
DR   CleanEx; MM_PTDSS1; -.
DR   Genevestigator; Q99LH2; -.
DR   GermOnline; ENSMUSG00000021518; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006659; P:phosphatidylserine biosynthetic process; IEA:InterPro.
DR   InterPro; IPR004277; PSS.
DR   PANTHER; PTHR12615; PSS; 1.
DR   Pfam; PF03034; PSS; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Phospholipid biosynthesis; Phosphoprotein; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    473       Phosphatidylserine synthase 1.
FT                                /FTId=PRO_0000056830.
FT   TRANSMEM     36     56       Helical; (Potential).
FT   TRANSMEM     73     93       Helical; (Potential).
FT   TRANSMEM    103    123       Helical; (Potential).
FT   TRANSMEM    187    207       Helical; (Potential).
FT   TRANSMEM    217    237       Helical; (Potential).
FT   TRANSMEM    287    307       Helical; (Potential).
FT   TRANSMEM    310    330       Helical; (Potential).
FT   TRANSMEM    356    376       Helical; (Potential).
FT   TRANSMEM    381    401       Helical; (Potential).
FT   MOD_RES     417    417       Phosphoserine (By similarity).
FT   MOD_RES     424    424       Phosphotyrosine (By similarity).
FT   MOD_RES     425    425       Phosphoserine (By similarity).
FT   MOD_RES     442    442       Phosphoserine (By similarity).
FT   CONFLICT    166    166       D -> E (in Ref. 1; AAB97845).
FT   CONFLICT    169    171       AFG -> SFA (in Ref. 1; AAB97845).
FT   CONFLICT    225    225       C -> H (in Ref. 1; AAB97845).
FT   CONFLICT    250    250       F -> L (in Ref. 2; BAC40117).
FT   CONFLICT    288    288       A -> G (in Ref. 1; AAB97845).
FT   CONFLICT    305    305       F -> S (in Ref. 1; AAB97845).
FT   CONFLICT    322    322       G -> C (in Ref. 1; AAB97845 and 2;
FT                                BAC40117).
SQ   SEQUENCE   473 AA;  55604 MW;  F185CA20FFADB84A CRC64;
     MASCVGSRTL SKDDVNYRMH FRMINEQQVE DITIDFFYRP HTITLLSFTI ISLMYFAFTR
     DDSVPEDNIW RGILSVIFFF LIISVLAFPN GPFTRPHPAL WRMVFGLSVL YFLFLVFLLF
     LNFEQVKSLM YWLDPNLRYA TREADIMEYA VNCHVITWER IVSHFDIFAF GHFWGWAMKA
     LLIRSYGLCW TISITWELTE LFFMHLLPNF AECWWDQVIL DILLCNGGGI WLGMVVCRFL
     EMRTYHWASF KDIHTTTGKI KRAVLQFTPA SWTYVRWFDP KSSFQRVAGI YLFMIIWQLT
     ELNTFFLKHI FVFQASHPLS WGRILFIGCI TAPTVRQYYA YLTDTQCKRV GTQCWVFGVI
     GFLEAIVCIK FGQDLFSKTQ ILYVMLWLLC VAFTTFLCLY GMVWYAEHYG HREKTYSECE
     DGTYSPEISW HHGKGSKGSE DSPPKHSSNH ESHSSRRRNR HSKSKVTNGV GKK
//
ID   3BP5L_MOUSE             Reviewed;         392 AA.
AC   Q99LH9; Q3UMF7; Q8BUC2; Q91YX6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=SH3 domain-binding protein 5-like;
DE            Short=SH3BP-5-like;
GN   Name=Sh3bp5l; Synonyms=Kiaa1720;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Head, Mammary gland, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361 AND SER-377, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SIMILARITY: Belongs to the SH3BP5 family.
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DR   EMBL; AK086088; BAC39606.1; -; mRNA.
DR   EMBL; AK144928; BAE26141.1; -; mRNA.
DR   EMBL; AK156171; BAE33611.1; -; mRNA.
DR   EMBL; AK172333; BAE42951.1; -; mRNA.
DR   EMBL; AL845463; CAI25448.1; -; Genomic_DNA.
DR   EMBL; BC003251; AAH03251.1; -; mRNA.
DR   EMBL; BC094418; AAH94418.1; -; mRNA.
DR   EMBL; BC013661; AAH13661.1; -; mRNA.
DR   IPI; IPI00116907; -.
DR   RefSeq; NP_001154810.1; NM_001161338.1.
DR   RefSeq; NP_077800.3; NM_024480.4.
DR   UniGene; Mm.290534; -.
DR   ProteinModelPortal; Q99LH9; -.
DR   PhosphoSite; Q99LH9; -.
DR   PRIDE; Q99LH9; -.
DR   Ensembl; ENSMUST00000073128; ENSMUSP00000072872; ENSMUSG00000013646.
DR   Ensembl; ENSMUST00000116376; ENSMUSP00000112077; ENSMUSG00000013646.
DR   GeneID; 79566; -.
DR   KEGG; mmu:79566; -.
DR   UCSC; uc007jbe.1; mouse.
DR   CTD; 79566; -.
DR   MGI; MGI:1933124; Sh3bp5l.
DR   GeneTree; ENSGT00390000018500; -.
DR   HOGENOM; HBG716595; -.
DR   HOVERGEN; HBG057307; -.
DR   InParanoid; Q99LH9; -.
DR   OMA; DGQELGP; -.
DR   OrthoDB; EOG4PZJ78; -.
DR   NextBio; 349957; -.
DR   ArrayExpress; Q99LH9; -.
DR   Bgee; Q99LH9; -.
DR   CleanEx; MM_SH3BP5L; -.
DR   Genevestigator; Q99LH9; -.
DR   InterPro; IPR007940; SH3-bd_5.
DR   PANTHER; PTHR19423; SH3_bd_5; 1.
DR   Pfam; PF05276; SH3BP5; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Phosphoprotein.
FT   CHAIN         1    392       SH3 domain-binding protein 5-like.
FT                                /FTId=PRO_0000317509.
FT   COILED       59    140       Potential.
FT   COILED      169    272       Potential.
FT   COMPBIAS     52     55       Poly-Glu.
FT   MOD_RES     342    342       Phosphoserine (By similarity).
FT   MOD_RES     349    349       Phosphoserine (By similarity).
FT   MOD_RES     361    361       Phosphoserine.
FT   MOD_RES     377    377       Phosphoserine.
FT   CONFLICT    148    148       R -> P (in Ref. 1; BAC39606).
FT   CONFLICT    181    181       N -> K (in Ref. 1; BAC39606).
FT   CONFLICT    304    304       D -> N (in Ref. 1; BAE26141).
SQ   SEQUENCE   392 AA;  43374 MW;  E80AEED11306392C CRC64;
     MADLKKAAGG RETPQGELRS EVVEDEGPRS PVAEEPGGSG SNSSETKLSP REEEELDPRI
     QEELEHLNQA SEEINQVELQ LDEARTTYRR ILQESARKLN TQGSHLGSCI EKARPYYEAR
     RLAKEAQQET QKAALRYERA VSMHNAAREM VFVAEQGVMA DKNRLDPTWQ EMLNHATCKV
     NEAEEERLRG EREHQRVTRL CQQAEARVQA LQKTLRRAIG KSRPYFELKA QFSQILEEHK
     AKVTELEQQV AQAKTRYSVA LRNLEQISEQ IHARRRGLPP HPLGPRRSSP VGAEAGPEGI
     EDGDSGIEGA EGGGLEEGSS LGPGPGPDTD TLSLLSLRTV ASDLQKCDSV EHLRGLSDHA
     SLDGQELGAQ SRGRRGSDIG VRGGRHQRSV SL
//
ID   CLCC1_MOUSE             Reviewed;         539 AA.
AC   Q99LI2; A2AEK9;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Chloride channel CLIC-like protein 1;
DE   Flags: Precursor;
GN   Name=Clcc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-429 AND SER-433, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Seems to act as a chloride ion channel (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential). Endoplasmic reticulum (By similarity). Golgi
CC       apparatus (By similarity). Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the chloride channel MCLC family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM17753.1; Type=Erroneous gene model prediction;
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DR   EMBL; AK169803; BAE41377.1; -; mRNA.
DR   EMBL; AK171296; BAE42376.1; -; mRNA.
DR   EMBL; AL671917; CAM17753.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL671917; CAM17754.1; -; Genomic_DNA.
DR   EMBL; BC003247; AAH03247.1; -; mRNA.
DR   IPI; IPI00280015; -.
DR   RefSeq; NP_001171242.1; NM_001177771.1.
DR   RefSeq; NP_663518.1; NM_145543.2.
DR   UniGene; Mm.214545; -.
DR   ProteinModelPortal; Q99LI2; -.
DR   STRING; Q99LI2; -.
DR   PhosphoSite; Q99LI2; -.
DR   PRIDE; Q99LI2; -.
DR   Ensembl; ENSMUST00000029483; ENSMUSP00000029483; ENSMUSG00000027884.
DR   Ensembl; ENSMUST00000106609; ENSMUSP00000102220; ENSMUSG00000027884.
DR   Ensembl; ENSMUST00000106610; ENSMUSP00000102221; ENSMUSG00000027884.
DR   Ensembl; ENSMUST00000106611; ENSMUSP00000102222; ENSMUSG00000027884.
DR   Ensembl; ENSMUST00000106613; ENSMUSP00000102224; ENSMUSG00000027884.
DR   GeneID; 229725; -.
DR   KEGG; mmu:229725; -.
DR   UCSC; uc008qzk.1; mouse.
DR   CTD; 229725; -.
DR   MGI; MGI:2385186; Clcc1.
DR   GeneTree; ENSGT00390000016611; -.
DR   HOVERGEN; HBG060364; -.
DR   InParanoid; Q99LI2; -.
DR   OrthoDB; EOG4CC41V; -.
DR   PhylomeDB; Q99LI2; -.
DR   NextBio; 379649; -.
DR   ArrayExpress; Q99LI2; -.
DR   Bgee; Q99LI2; -.
DR   CleanEx; MM_CLCC1; -.
DR   Genevestigator; Q99LI2; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR009231; Chloride_chnl_CLIC-like.
DR   Pfam; PF05934; MCLC; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Golgi apparatus; Membrane; Nucleus;
KW   Phosphoprotein; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     18       Potential.
FT   CHAIN        19    539       Chloride channel CLIC-like protein 1.
FT                                /FTId=PRO_0000297683.
FT   TRANSMEM    185    205       Helical; (Potential).
FT   TRANSMEM    216    236       Helical; (Potential).
FT   TRANSMEM    330    350       Helical; (Potential).
FT   MOD_RES     429    429       Phosphoserine.
FT   MOD_RES     433    433       Phosphoserine.
FT   MOD_RES     459    459       Phosphoserine (By similarity).
FT   MOD_RES     476    476       Phosphothreonine (By similarity).
FT   MOD_RES     497    497       Phosphoserine.
FT   MOD_RES     498    498       Phosphoserine (By similarity).
FT   MOD_RES     513    513       Phosphoserine (By similarity).
FT   MOD_RES     521    521       Phosphoserine (By similarity).
SQ   SEQUENCE   539 AA;  60621 MW;  252A3E095B56C1C4 CRC64;
     MLCRLLLCEC LLLITGYAHD DDWIDPTDML NYDAASGTMR KSQVRSGTSE KKEVSPDSSE
     AEELSDCLHR LDSLTHKVDS CEKKKMKDYE SQSNPVFRRY LNKILIEAGK LGLPDENKVE
     MRYDAEILLS RQTLLEIQKF LSGEEWKPGA LDDALSDILI NFKCHDSEAW KWQFEDYFGV
     DPYNVFMVLL CLLCLVVLVA TELWTYVRWY TQMKRIFIIS FLLSLAWNWI YLYKMAFAQH
     QANIAGMEPF DNLCAKKMDW TGSLWEWFTS SWTYKDDPCQ KYYELLIVNP IWLVPPTKAL
     AITFTNFVTE PLKHIGKGAG EFIKALMKEI PVLLQIPVLA ILALAVLSFC YGAGRSVPML
     RHFGGPDREP PRALEPDDRR RQKGLDYRLH GGAGDADFSY RGPAGSIEQG PYDKMHASKR
     DALRQRFHSG NKSPEVLRAF DLPDTEAQEH PEVVPSHKSP IMNTNLETGE LPGESTPTEY
     SQSAKDVSGQ VPSAGKSSPT VDKAQLKTDS ECSPPGGCPP SKEAAVAAHG TEPVSSPCG
//
ID   HGS_MOUSE               Reviewed;         775 AA.
AC   Q99LI8; Q61691; Q8BQW3;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   08-FEB-2011, entry version 86.
DE   RecName: Full=Hepatocyte growth factor-regulated tyrosine kinase substrate;
GN   Name=Hgs; Synonyms=Hrs;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RX   MEDLINE=96026002; PubMed=7565774;
RA   Komada M., Kitamura N.;
RT   "Growth factor-induced tyrosine phosphorylation of Hrs, a novel 115-
RT   kilodalton protein with a structurally-conserved putative zinc finger
RT   domain.";
RL   Mol. Cell. Biol. 15:6213-6221(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH STAM1, AND DOMAIN.
RX   MEDLINE=98070470; PubMed=9407053; DOI=10.1074/jbc.272.52.32785;
RA   Asao H., Sasaki Y., Arita T., Tanaka N., Endo K., Kasai H.,
RA   Takeshita T., Endo Y., Fujita T., Sugamura K.;
RT   "Hrs is associated with STAM, a signal-transducing adaptor molecule.
RT   Its suppressive effect on cytokine-induced cell growth.";
RL   J. Biol. Chem. 272:32785-32791(1997).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=98296261; PubMed=9630564; DOI=10.1016/S0378-1119(98)00184-X;
RA   Lu L., Komada M., Kitamura N.;
RT   "Human Hrs, a tyrosine kinase substrate in growth factor-stimulated
RT   cells: cDNA cloning and mapping of the gene to chromosome 17.";
RL   Gene 213:125-132(1998).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=10364163;
RA   Komada M., Soriano P.;
RT   "Hrs, a FYVE finger protein localized to early endosomes, is
RT   implicated in vesicular traffic and required for ventral folding
RT   morphogenesis.";
RL   Genes Dev. 13:1475-1485(1999).
RN   [7]
RP   INTERACTION WITH STAM2, AND SUBCELLULAR LOCATION.
RX   PubMed=10651905; DOI=10.1046/j.1365-2443.2000.00303.x;
RA   Takata H., Kato M., Denda K., Kitamura N.;
RT   "A hrs binding protein having a Src homology 3 domain is involved in
RT   intracellular degradation of growth factors and their receptors.";
RL   Genes Cells 5:57-69(2000).
RN   [8]
RP   INTERACTION WITH SMAD1; SMAD2 AND SMAD3, DISRUPTION PHENOTYPE, AND
RP   FUNCTION.
RX   PubMed=11094085; DOI=10.1128/MCB.20.24.9346-9355.2000;
RA   Miura S., Takeshita T., Asao H., Kimura Y., Murata K., Sasaki Y.,
RA   Hanai J., Beppu H., Tsukazaki T., Wrana J.L., Miyazono K.,
RA   Sugamura K.;
RT   "Hgs (Hrs), a FYVE domain protein, is involved in Smad signaling
RT   through cooperation with SARA.";
RL   Mol. Cell. Biol. 20:9346-9355(2000).
RN   [9]
RP   MUTAGENESIS OF ARG-183 AND CYS-215, AND SUBCELLULAR LOCATION.
RX   PubMed=11493665;
RA   Raiborg C., Bremnes B., Mehlum A., Gillooly D.J., D'Arrigo A.,
RA   Stang E., Stenmark H.;
RT   "FYVE and coiled-coil domains determine the specific localisation of
RT   Hrs to early endosomes.";
RL   J. Cell Sci. 114:2255-2263(2001).
RN   [10]
RP   INTERACTION WITH UBIQUITIN, AND MUTAGENESIS OF SER-270.
RX   PubMed=11988743; DOI=10.1038/ncb791;
RA   Raiborg C., Bache K.G., Gillooly D.J., Madshus I.H., Stang E.,
RA   Stenmark H.;
RT   "Hrs sorts ubiquitinated proteins into clathrin-coated microdomains of
RT   early endosomes.";
RL   Nat. Cell Biol. 4:394-398(2002).
RN   [11]
RP   PHOSPHORYLATION AT TYR-329 AND TYR-334, MASS SPECTROMETRY, MUTAGENESIS
RP   OF LEU-269; SER-270; TYR-329 AND TYR-334, AND SUBCELLULAR LOCATION.
RX   PubMed=12953068; DOI=10.1242/jcs.00723;
RA   Urbe S., Sachse M., Row P.E., Preisinger C., Barr F.A., Strous G.,
RA   Klumperman J., Clague M.J.;
RT   "The UIM domain of Hrs couples receptor sorting to vesicle
RT   formation.";
RL   J. Cell Sci. 116:4169-4179(2003).
RN   [12]
RP   INTERACTION WITH TSG101.
RX   PubMed=12802020; DOI=10.1073/pnas.0932599100;
RA   Lu Q., Hope L.W., Brasch M., Reinhard C., Cohen S.N.;
RT   "TSG101 interaction with HRS mediates endosomal trafficking and
RT   receptor down-regulation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7626-7631(2003).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, AND MASS
RP   SPECTROMETRY.
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-308, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Involved in intracellular signal transduction mediated
CC       by cytokines and growth factors. When associated with STAM, it
CC       suppresses DNA signaling upon stimulation by IL-2 and GM-CSF.
CC       Could be a direct effector of PI3-kinase in vesicular pathway via
CC       early endosomes and may regulate trafficking to early and late
CC       endosomes by recruiting clathrin. May concentrate ubiquitinated
CC       receptors within clathrin-coated regions. Involved in down-
CC       regulation of receptor tyrosine kinase via multivesicular body
CC       (MVBs) when complexed with STAM (ESCRT-0 complex). The ESCRT-0
CC       complex binds ubiquitin and acts as sorting machinery that
CC       recognizes ubiquitinated receptors and transfers them to further
CC       sequential lysosomal sorting/trafficking processes. May contribute
CC       to the efficient recruitment of SMADs to the activin receptor
CC       complex. Involved in receptor recycling via its association with
CC       the CART complex, a multiprotein complex required for efficient
CC       transferrin receptor recycling but not for EGFR degradation.
CC   -!- SUBUNIT: Component of the ESCRT-0 complex composed of STAM or
CC       STAM2 and HGS. Part of a complex at least composed of HSG, STAM2
CC       (or probably STAM) and EPS15. Interacts with STAM. Interacts with
CC       STAM2. Interacts with EPS15; the interaction is direct, calcium-
CC       dependent and inhibited by SNAP25. Interacts with NF2; the
CC       interaction is direct. Interacts with ubiquitin; the interaction
CC       is direct. Interacts with VPS37C. Interacts with SMAD1, SMAD2 and
CC       SMAD3. Interacts with TSG101; the interaction mediates the
CC       association with the ESCRT-I complex. Interacts with SNAP25; the
CC       interaction is direct and decreases with addition of increasing
CC       concentrations of free calcium. Interacts with SNX1; the
CC       interaction is direct. Component of a 550 kDa membrane complex at
CC       least composed of HGS and SNX1 but excluding EGFR. Component of
CC       the CART complex, at least composed of ACTN4, HGS/HRS, MYO5B and
CC       TRIM3. Interacts with TRAK1 and TRAK2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Early endosome membrane;
CC       Peripheral membrane protein; Cytoplasmic side. Endosome,
CC       multivesicular body membrane; Peripheral membrane protein.
CC   -!- TISSUE SPECIFICITY: Ubiquitous expression in adult and fetal
CC       tissues with higher expression in testis.
CC   -!- DOMAIN: Has a double-sided UIM that can bind 2 ubiquitin
CC       molecules, one on each side of the helix (By similarity).
CC   -!- DOMAIN: The FYVE-type zinc finger domain mediates interactions
CC       with phosphatidylinositol 3-phosphate in membranes of early
CC       endosomes and penetrates bilayers. The FYVE domain insertion into
CC       PtdIns(3)P-enriched membranes is substantially increased in acidic
CC       conditions (By similarity).
CC   -!- PTM: Phosphorylated on Tyr-334. This phosphorylation occurs in
CC       response to EGF. A minor site of phosphorylation on Tyr-329 is
CC       detected. Protein phosphorylation may also be triggered in
CC       response to IL-2, GM-CSF and HGF.
CC   -!- PTM: Ubiquitinated by ITCH (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice show a defect in ventral folding
CC       morphogenesis, exhibiting two bilateral heart tubes and absence of
CC       foregut, and died around embryonic day 11. Significantly enlarged
CC       endosomes were also detected in cells of the endoderm.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 1 UIM (ubiquitin-interacting motif) repeat.
CC   -!- SIMILARITY: Contains 1 VHS domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; D50050; BAA08768.1; -; mRNA.
DR   EMBL; AK046299; BAC32676.1; -; mRNA.
DR   EMBL; BC003239; AAH03239.1; -; mRNA.
DR   IPI; IPI00649267; -.
DR   PIR; I49759; I49759.
DR   RefSeq; NP_001152800.1; NM_001159328.1.
DR   RefSeq; NP_032270.3; NM_008244.3.
DR   UniGene; Mm.7919; -.
DR   ProteinModelPortal; Q99LI8; -.
DR   SMR; Q99LI8; 1-221, 402-499.
DR   DIP; DIP-29102N; -.
DR   IntAct; Q99LI8; 2.
DR   MINT; MINT-267768; -.
DR   STRING; Q99LI8; -.
DR   PhosphoSite; Q99LI8; -.
DR   PRIDE; Q99LI8; -.
DR   Ensembl; ENSMUST00000026900; ENSMUSP00000026900; ENSMUSG00000025793.
DR   GeneID; 15239; -.
DR   KEGG; mmu:15239; -.
DR   UCSC; uc007msy.1; mouse.
DR   CTD; 15239; -.
DR   MGI; MGI:104681; Hgs.
DR   GeneTree; ENSGT00550000074629; -.
DR   HOVERGEN; HBG062917; -.
DR   InParanoid; Q99LI8; -.
DR   NextBio; 287839; -.
DR   ArrayExpress; Q99LI8; -.
DR   Bgee; Q99LI8; -.
DR   CleanEx; MM_HGS; -.
DR   Genevestigator; Q99LI8; -.
DR   GermOnline; ENSMUSG00000025793; Mus musculus.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   InterPro; IPR008942; ENTH_VHS.
DR   InterPro; IPR017073; Ubi-bd_Hrs_VPS27.
DR   InterPro; IPR003903; Ubiquitin-int_motif.
DR   InterPro; IPR002014; VHS.
DR   InterPro; IPR018205; VHS_subgroup.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:1.25.40.90; ENTH_VHS; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF00790; VHS; 1.
DR   PIRSF; PIRSF036956; Hrs_Vps27; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00726; UIM; 1.
DR   SMART; SM00288; VHS; 1.
DR   SUPFAM; SSF48464; ENTH_VHS; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS50330; UIM; 1.
DR   PROSITE; PS50179; VHS; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Endosome; Membrane; Metal-binding;
KW   Phosphoprotein; Protein transport; Transport; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    775       Hepatocyte growth factor-regulated
FT                                tyrosine kinase substrate.
FT                                /FTId=PRO_0000098709.
FT   DOMAIN       15    143       VHS.
FT   REPEAT      258    277       UIM.
FT   ZN_FING     160    220       FYVE-type.
FT   REGION      225    541       Interaction with SNX1 (By similarity).
FT   REGION      443    541       Interaction with SNAP25 and TRAK2 (By
FT                                similarity).
FT   REGION      452    570       Interaction with STAM1.
FT   REGION      478    775       Interaction with NF2 (By similarity).
FT   COMPBIAS    503    558       Gln-rich.
FT   COMPBIAS    559    763       Pro-rich.
FT   MOD_RES     132    132       Phosphotyrosine (By similarity).
FT   MOD_RES     207    207       N6-acetyllysine (By similarity).
FT   MOD_RES     216    216       Phosphotyrosine.
FT   MOD_RES     240    240       Phosphoserine (By similarity).
FT   MOD_RES     286    286       Phosphotyrosine (By similarity).
FT   MOD_RES     308    308       Phosphotyrosine.
FT   MOD_RES     329    329       Phosphotyrosine.
FT   MOD_RES     334    334       Phosphotyrosine.
FT   MUTAGEN     183    183       R->A: 100-fold loss of affinity for PIP3
FT                                and accumulation in the cytosol.
FT   MUTAGEN     215    215       C->S: Accumulation in proteinaceous
FT                                aggregates devoid of membranes and no
FT                                interaction with PI3P.
FT   MUTAGEN     269    269       L->A: Loss of protein phosphorylation at
FT                                Y-329 and Y-334; when associated with A-
FT                                270.
FT   MUTAGEN     270    270       S->A: Loss of protein phosphorylation at
FT                                Y-329 and Y-334; when associated with A-
FT                                269.
FT   MUTAGEN     270    270       S->E: No interaction with ubiquitin.
FT   MUTAGEN     329    329       Y->F: No change in the phosphorylation
FT                                level. Loss of protein phosphorylation;
FT                                when associated with F-334.
FT   MUTAGEN     334    334       Y->F: No change in the phosphorylation
FT                                level. Loss of protein phosphorylation;
FT                                when associated with F-329.
FT   CONFLICT     23     23       T -> S (in Ref. 3; AAH03239).
FT   CONFLICT    584    584       P -> S (in Ref. 2; BAC32676).
SQ   SEQUENCE   775 AA;  86015 MW;  0E68BF5AB514865B CRC64;
     MGRGSGTFER LLDKATSQLL LETDWESILQ ICDLIRQGDT QAKYAVNSIK KKVNDKNPHV
     ALYALEVMES VVKNCGQTVH DEVANKQTME ELKELLKRQV EVNVRNKILY LIQAWAHAFR
     NEPKYKVVQD TYQIMKVEGH VFPEFKESDA MFAAERAPDW VDAEECHRCR VQFGVVTRKH
     HCRACGQIFC GKCSSKYSTI PKFGIEKEVR VCEPCYEQLN KKAEGKASST TELPPEYLTS
     PLSQQSQLPP KRDETALQEE EELQLALALS QSEAEEKERM RQKTTYTAHP KAEPTPLASS
     APPAGSLYSS PVNSSAPLAE DIDPELARYL NRNYWEKKQE EARKSPTPSA PVPLTEPAAQ
     PGEGHTAPNS MAEAPLPETD SQPITPCSGP FSEYQNGESE ESHEQFLKAL QNAVSTFVNR
     MKSNHMRGRS ITNDSAVLSL FQSINTMHPQ LLELLNQLDE RRLYYEGLQD KLAQIRDARG
     ALSALREEHR EKLRRAAEEA ERQRQIQLAQ KLEIMRQKKQ EYLEVQRQLA IQRLQEQEKE
     RQMRLEQQKQ TVQMRAQMPA FPLPYAQLQA MPTAGGVLYQ PSGPTSFPAT FSPAGSVEGS
     PMHGVYMSQP APATGPYPSM PGTTADPSMV SAYMYPTGAP GAQAAPQAQA GPTTSPAYSS
     YQPTPTPGYQ SVASQAPQSL PAISQPPQTS NIGYMGSQPM SMGYQPYNMQ NLMTALPGQD
     ASLPAQQPYI PGQQPLYQQM APSTGPPQQQ PPVAQPAPTQ GPPAQGSEAQ LISFD
//
ID   CT2NL_MOUSE             Reviewed;         638 AA.
AC   Q99LJ0; Q6ZPR0; Q8BSV1;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=CTTNBP2 N-terminal-like protein;
GN   Name=Cttnbp2nl; Synonyms=Kiaa1433;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pituitary, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98169.1; Type=Erroneous initiation;
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DR   EMBL; AK129359; BAC98169.1; ALT_INIT; mRNA.
DR   EMBL; AK029901; BAC26666.1; -; mRNA.
DR   EMBL; AK030438; BAC26964.1; -; mRNA.
DR   EMBL; BC003236; AAH03236.1; -; mRNA.
DR   IPI; IPI00453812; -.
DR   RefSeq; NP_001156804.1; NM_001163332.1.
DR   RefSeq; NP_001156805.1; NM_001163333.1.
DR   RefSeq; NP_084525.1; NM_030249.4.
DR   UniGene; Mm.200327; -.
DR   ProteinModelPortal; Q99LJ0; -.
DR   PhosphoSite; Q99LJ0; -.
DR   PRIDE; Q99LJ0; -.
DR   Ensembl; ENSMUST00000077548; ENSMUSP00000076751; ENSMUSG00000062127.
DR   Ensembl; ENSMUST00000098763; ENSMUSP00000096359; ENSMUSG00000062127.
DR   GeneID; 80281; -.
DR   KEGG; mmu:80281; -.
DR   UCSC; uc008quu.1; mouse.
DR   CTD; 80281; -.
DR   MGI; MGI:1933137; Cttnbp2nl.
DR   eggNOG; roNOG14428; -.
DR   GeneTree; ENSGT00550000074495; -.
DR   HOGENOM; HBG755282; -.
DR   HOVERGEN; HBG081371; -.
DR   InParanoid; Q99LJ0; -.
DR   OMA; GINQRFH; -.
DR   OrthoDB; EOG45TCN9; -.
DR   NextBio; 349965; -.
DR   ArrayExpress; Q99LJ0; -.
DR   Bgee; Q99LJ0; -.
DR   CleanEx; MM_CTTNBP2NL; -.
DR   Genevestigator; Q99LJ0; -.
DR   GermOnline; ENSMUSG00000062127; Mus musculus.
DR   InterPro; IPR019131; Cortactin-binding_p2_N.
DR   Pfam; PF09727; CortBP2; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Phosphoprotein.
FT   CHAIN         1    638       CTTNBP2 N-terminal-like protein.
FT                                /FTId=PRO_0000226998.
FT   COILED       87    284       Potential.
FT   MOD_RES     444    444       Phosphoserine (By similarity).
FT   MOD_RES     481    481       Phosphoserine.
FT   MOD_RES     484    484       Phosphoserine (By similarity).
FT   MOD_RES     488    488       Phosphoserine.
FT   MOD_RES     522    522       Phosphoserine (By similarity).
FT   MOD_RES     526    526       Phosphoserine (By similarity).
FT   MOD_RES     556    556       Phosphoserine (By similarity).
FT   MOD_RES     559    559       Phosphoserine (By similarity).
FT   MOD_RES     567    567       Phosphoserine (By similarity).
FT   MOD_RES     589    589       Phosphothreonine (By similarity).
FT   MOD_RES     591    591       Phosphoserine (By similarity).
FT   CONFLICT     92     92       N -> D (in Ref. 2; BAC26964).
SQ   SEQUENCE   638 AA;  69841 MW;  9E3CC4364E73972C CRC64;
     MNLEKLSKPE LLTLFSILEG ELEARDLVIE ALKAQHRDTF IEERYGKYNI SDPLMALQRD
     FETLKEKNDS EKQPVCTNPL SVLKAVMKQC KNMQERMLSQ LAAAESRHRK VILDLEEERQ
     RHAQDTAEGD DVTYMLEKER ERLTQQLEFE KSQVKKFEKE QKKLSSQLEE ERTRHKQLSS
     MLVLECRKAT SKAAEEGQKA GELSLKLDKE KSRASKLEEE LAAERKRGLQ TEAQVEKQLS
     EFDIEREQLR AKLNREENRT RALKEEVESL KKLVKDLEAA QQHRSTSEQG REPVTMSRGT
     ATEPPMRVSA FCQTESVQTE RSHGSVITKL TDTGLPGPTT AAYSYAKANG HCDPEIQTTR
     ELTSDSSTEN QGPPREKSAV AAQEKPVENG GCPVGTETPV TMPSHLPSSG SSLSPSSTAS
     SSLTSSPCSS PVLTKRLLGS AASSPGYQSS YQVGINQRFH AARHKFQSQA DQDQQASGLQ
     SPPSRDLSPT LLDNSAAKQL ARNTVTQVLS RFTNQGPIKP VSPNSSPFGT DYRNLASTAS
     PRGDTSHSPT PGKVSSPLSP LSPGIKSPTI PRAERGNPPP IPPKKPGLTP SQSATTPVTK
     THSQASSLAA TEDLASSCSP SAVVANGKDV EILLPTSS
//
ID   PWP1_MOUSE              Reviewed;         501 AA.
AC   Q99LL5; Q9D6T6;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Periodic tryptophan protein 1 homolog;
GN   Name=Pwp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49 AND SER-493, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May play an important role in cell growth and/or
CC       transcription (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the WD repeat PWP1 family.
CC   -!- SIMILARITY: Contains 5 WD repeats.
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DR   EMBL; AK009972; BAB26622.1; -; mRNA.
DR   EMBL; AK082158; BAC38427.1; -; mRNA.
DR   EMBL; BC003199; AAH03199.1; -; mRNA.
DR   EMBL; BC023137; AAH23137.1; -; mRNA.
DR   IPI; IPI00320422; -.
DR   RefSeq; NP_598754.2; NM_133993.3.
DR   UniGene; Mm.18834; -.
DR   ProteinModelPortal; Q99LL5; -.
DR   SMR; Q99LL5; 204-462.
DR   STRING; Q99LL5; -.
DR   PhosphoSite; Q99LL5; -.
DR   PRIDE; Q99LL5; -.
DR   Ensembl; ENSMUST00000001836; ENSMUSP00000001836; ENSMUSG00000001785.
DR   GeneID; 103136; -.
DR   KEGG; mmu:103136; -.
DR   UCSC; uc007gnd.1; mouse.
DR   CTD; 103136; -.
DR   MGI; MGI:1914735; Pwp1.
DR   HOGENOM; HBG748186; -.
DR   HOVERGEN; HBG001543; -.
DR   InParanoid; Q99LL5; -.
DR   OMA; CNFLAST; -.
DR   OrthoDB; EOG4STS4J; -.
DR   PhylomeDB; Q99LL5; -.
DR   NextBio; 355805; -.
DR   ArrayExpress; Q99LL5; -.
DR   Bgee; Q99LL5; -.
DR   CleanEx; MM_PWP1; -.
DR   Genevestigator; Q99LL5; -.
DR   GermOnline; ENSMUSG00000001785; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 3.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Nucleus; Phosphoprotein; Repeat; WD repeat.
FT   CHAIN         1    501       Periodic tryptophan protein 1 homolog.
FT                                /FTId=PRO_0000051172.
FT   REPEAT      185    229       WD 1.
FT   REPEAT      253    293       WD 2.
FT   REPEAT      296    336       WD 3.
FT   REPEAT      382    422       WD 4.
FT   REPEAT      427    467       WD 5.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      21     21       Phosphothreonine (By similarity).
FT   MOD_RES      49     49       Phosphoserine.
FT   MOD_RES      58     58       Phosphoserine (By similarity).
FT   MOD_RES      64     64       Phosphoserine (By similarity).
FT   MOD_RES      85     85       Phosphothreonine (By similarity).
FT   MOD_RES     484    484       Phosphoserine (By similarity).
FT   MOD_RES     493    493       Phosphoserine.
FT   CONFLICT    247    247       K -> R (in Ref. 1; BAB26622).
SQ   SEQUENCE   501 AA;  55587 MW;  704A050633F0C2B1 CRC64;
     MNRSRQVTCV AWVRRGVAKE TPDKVELSKE EVNRLIAEAK GKLQEEGGSE EEEAGNPSED
     GMQSGPTQAP PRESLEDGDP QDDRTLDDDE LAGYDLDNYD EEDNPDAETI GESLLGLTVY
     GSNDQDPYVT LKDTEQYEHE DFLIKPTDNL IVCGRAEQEQ CNLEVHVYNQ EEESFYVHHD
     ILLSAYPLSV EWLNFDPSPD ASTGNYIAVG NMTPVIEVWD LDIVDSLEPV FTLGSKLSKK
     KKKKGKKSSS AEGHTDAVLD LSWNKTVRNV LASASADSTV VLWDLSVGKS VARLTAHTDK
     VQTLQFHPFE AQTLISGSYD KSVALYDCRD PSQNHRQWRF SGQIERVTWN HFSPCHFLAS
     TDDGFVYNLD ARSDKPIFTL NAHNDEISGL DLSSQIKGCL VTASADKFVK IWDILGDRPS
     LIHSRDMKMG VLFCSSCCPD LPFVYAFGGQ KEGLRVWDIS TVSSVNEAFG RRERLVIGGT
     KGLSVSGPCG SRSPQQTPME S
//
ID   PARK7_MOUSE             Reviewed;         189 AA.
AC   Q99LX0; O88306; Q3THB9; Q3U509;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Protein DJ-1;
DE            EC=3.4.-.-;
DE   AltName: Full=Parkinson disease protein 7 homolog;
DE   Flags: Precursor;
GN   Name=Park7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   MEDLINE=21125241; PubMed=11223268; DOI=10.1016/S0378-1119(00)00590-4;
RA   Taira T., Takahashi K., Kitagawa R., Iguchi-Ariga S.M.M., Ariga H.;
RT   "Molecular cloning of human and mouse DJ-1 genes and identification of
RT   Sp1-dependent activation of the human DJ-1 promoter.";
RL   Gene 263:285-292(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, and NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 13-27; 63-89 AND 99-122, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [6]
RP   INDUCTION.
RX   PubMed=14749723; DOI=10.1038/sj.embor.7400074;
RA   Taira T., Saito Y., Niki T., Iguchi-Ariga S.M., Takahashi K.,
RA   Ariga H.;
RT   "DJ-1 has a role in antioxidative stress to prevent cell death.";
RL   EMBO Rep. 5:213-218(2004).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15784737; DOI=10.1073/pnas.0501282102;
RA   Kim R.H., Smith P.D., Aleyasin H., Hayley S., Mount M.P., Pownall S.,
RA   Wakeham A., You-Ten A.J., Kalia S.K., Horne P., Westaway D.,
RA   Lozano A.M., Anisman H., Park D.S., Mak T.W.;
RT   "Hypersensitivity of DJ-1-deficient mice to 1-methyl-4-phenyl-1,2,3,6-
RT   tetrahydropyrindine (MPTP) and oxidative stress.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:5215-5220(2005).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17015834; DOI=10.1073/pnas.0607260103;
RA   Clements C.M., McNally R.S., Conti B.J., Mak T.W., Ting J.P.;
RT   "DJ-1, a cancer- and Parkinson's disease-associated protein,
RT   stabilizes the antioxidant transcriptional master regulator Nrf2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15091-15096(2006).
RN   [9]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-46; CYS-53 AND
RP   CYS-106.
RX   PubMed=17766438; DOI=10.1073/pnas.0703219104;
RA   Andres-Mateos E., Perier C., Zhang L., Blanchard-Fillion B.,
RA   Greco T.M., Thomas B., Ko H.S., Sasaki M., Ischiropoulos H.,
RA   Przedborski S., Dawson T.M., Dawson V.L.;
RT   "DJ-1 gene deletion reveals that DJ-1 is an atypical peroxiredoxin-
RT   like peroxidase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:14807-14812(2007).
RN   [10]
RP   FUNCTION.
RX   PubMed=19276172; DOI=10.1096/fj.08-125153;
RA   Waak J., Weber S.S., Waldenmaier A., Gorner K., Alunni-Fabbroni M.,
RA   Schell H., Vogt-Weisenhorn D., Pham T.T., Reumers V., Baekelandt V.,
RA   Wurst W., Kahle P.J.;
RT   "Regulation of astrocyte inflammatory responses by the Parkinson's
RT   disease-associated gene DJ-1.";
RL   FASEB J. 23:2478-2489(2009).
RN   [11]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=20800516; DOI=10.1016/j.bcmd.2010.07.014;
RA   Xu X., Martin F., Friedman J.S.;
RT   "The familial Parkinson's disease gene DJ-1 (PARK7) is expressed in
RT   red cells and plays a role in protection against oxidative damage.";
RL   Blood Cells Mol. Dis. 45:227-232(2010).
RN   [12]
RP   INTERACTION WITH BBS1; CLCF1; MTERF AND OTUD7B.
RX   PubMed=21097510; DOI=10.1074/jbc.M110.147371;
RA   McNally R.S., Davis B.K., Clements C.M., Accavitti-Loper M.A.,
RA   Mak T.W., Ting J.P.;
RT   "DJ-1 enhances cell survival through the binding of cezanne, a
RT   negative regulator of NF-{kappa}B.";
RL   J. Biol. Chem. 0:0-0(2010).
RN   [13]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=21068725; DOI=10.1038/nature09536;
RA   Guzman J.N., Sanchez-Padilla J., Wokosin D., Kondapalli J., Ilijic E.,
RA   Schumacker P.T., Surmeier D.J.;
RT   "Oxidant stress evoked by pacemaking in dopaminergic neurons is
RT   attenuated by DJ-1.";
RL   Nature 468:696-700(2010).
RN   [14]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20186336; DOI=10.1371/journal.pone.0009367;
RA   Krebiehl G., Ruckerbauer S., Burbulla L.F., Kieper N., Maurer B.,
RA   Waak J., Wolburg H., Gizatullina Z., Gellerich F.N., Woitalla D.,
RA   Riess O., Kahle P.J., Proikas-Cezanne T., Kruger R.;
RT   "Reduced basal autophagy and impaired mitochondrial dynamics due to
RT   loss of Parkinson's disease-associated protein DJ-1.";
RL   PLoS ONE 5:E9367-E9367(2010).
CC   -!- FUNCTION: Protects cells against oxidative stress and cell death.
CC       Plays a role in regulating expression or stability of the
CC       mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in
CC       dopaminergic neurons of the substantia nigra pars compacta and
CC       attenuates the oxidative stress induced by calcium entry into the
CC       neurons via L-type channels during pacemaking. Eliminates hydrogen
CC       peroxide and protects cells against hydrogen peroxide-induced cell
CC       death. May act as an atypical peroxiredoxin-like peroxidase that
CC       scavenges hydrogen peroxide. Following removal of a C-terminal
CC       peptide, displays protease activity and enhanced cytoprotective
CC       action against oxidative stress-induced apoptosis. Stabilizes
CC       NFE2L2 by preventing its association with KEAP1 and its subsequent
CC       ubiquitination. Binds to OTUD7B and inhibits its deubiquitinating
CC       activity. Enhances RELA nuclear translocation. Binds to a number
CC       of mRNAs containing multiple copies of GG or CC motifs and
CC       partially inhibits their translation but dissociates following
CC       oxidative stress. Required for correct mitochondrial morphology
CC       and function and for autophagy of dysfunctional mitochondria.
CC       Regulates astrocyte inflammatory responses. Acts as a positive
CC       regulator of androgen receptor-dependent transcription. Prevents
CC       aggregation of SNCA. Plays a role in fertilization. Has no
CC       proteolytic activity. Has cell-growth promoting activity and
CC       transforming activity. May function as a redox-sensitive
CC       chaperone.
CC   -!- SUBUNIT: Homodimer. Binds EFCAB6/DJBP and PIAS2. Part of a ternary
CC       complex containing PARK7, EFCAB6/DJBP and AR (By similarity).
CC       Interacts (via N-terminus) with OTUD7B. Interacts with BBS1, CLCF1
CC       and MTERF.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Mitochondrion (By similarity). Note=Under normal
CC       conditions, located predominantly in the cytoplasm and, to a
CC       lesser extent, in the nucleus and mitochondrion. Translocates to
CC       the mitochondrion and subsequently to the nucleus in response to
CC       oxidative stress and exerts an increased cytoprotective effect
CC       against oxidative damage (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in erythroblasts and in mature red
CC       blood cells from peripheral blood (at protein level).
CC   -!- DEVELOPMENTAL STAGE: Expression increases during erythroid
CC       development (at protein level).
CC   -!- INDUCTION: By hydrogen peroxide.
CC   -!- PTM: Sumoylated on Lys-130 by PIAS2 or PIAS4; which is essential
CC       for cell-growth promoting activity and transforming activity (By
CC       similarity).
CC   -!- PTM: Undergoes cleavage of a C-terminal peptide and subsequent
CC       activation of protease activity in response to oxidative stress
CC       (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Increased sensitivity of embryonic cortical
CC       neurons to oxidative stress. Age-dependent increase in
CC       mitochondrial hydrogen peroxide production and reduced
CC       mitochondrial aconitase activity. Down-regulation of Slc25a14 and
CC       Slc25a27, compromised calcium-induced uncoupling and increased
CC       oxidation of mitochondrial matrix proteins specifically in the
CC       dopaminergic neurons of the substantia nigra pars compacta.
CC       Reduced N2el2 protein expression. Impaired mitochondrial function
CC       and morphology with reduced autophagy leading to accumulation of
CC       defective mitochondria.
CC   -!- SIMILARITY: Belongs to the peptidase C56 family.
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DR   EMBL; AB015652; BAA29063.2; -; mRNA.
DR   EMBL; AK146368; BAE27118.1; -; mRNA.
DR   EMBL; AK153948; BAE32271.1; -; mRNA.
DR   EMBL; AK168341; BAE40278.1; -; mRNA.
DR   EMBL; AL607084; CAM19230.1; -; Genomic_DNA.
DR   EMBL; BC002187; AAH02187.1; -; mRNA.
DR   IPI; IPI00117264; -.
DR   RefSeq; NP_065594.2; NM_020569.3.
DR   UniGene; Mm.277349; -.
DR   ProteinModelPortal; Q99LX0; -.
DR   SMR; Q99LX0; 1-189.
DR   STRING; Q99LX0; -.
DR   MEROPS; C56.002; -.
DR   PhosphoSite; Q99LX0; -.
DR   REPRODUCTION-2DPAGE; Q99LX0; -.
DR   UCD-2DPAGE; Q99LX0; -.
DR   PRIDE; Q99LX0; -.
DR   Ensembl; ENSMUST00000030805; ENSMUSP00000030805; ENSMUSG00000028964.
DR   Ensembl; ENSMUST00000105673; ENSMUSP00000101298; ENSMUSG00000028964.
DR   Ensembl; ENSMUST00000105674; ENSMUSP00000101299; ENSMUSG00000028964.
DR   Ensembl; ENSMUST00000105675; ENSMUSP00000101300; ENSMUSG00000028964.
DR   GeneID; 57320; -.
DR   KEGG; mmu:57320; -.
DR   UCSC; uc008vxz.1; mouse.
DR   CTD; 57320; -.
DR   MGI; MGI:2135637; Park7.
DR   GeneTree; ENSGT00390000001231; -.
DR   HOGENOM; HBG646910; -.
DR   HOVERGEN; HBG053511; -.
DR   InParanoid; Q99LX0; -.
DR   OMA; GDHYKYS; -.
DR   OrthoDB; EOG4DJJXJ; -.
DR   PhylomeDB; Q99LX0; -.
DR   NextBio; 313682; -.
DR   ArrayExpress; Q99LX0; -.
DR   Bgee; Q99LX0; -.
DR   Genevestigator; Q99LX0; -.
DR   GermOnline; ENSMUSG00000028964; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051920; F:peroxiredoxin activity; IMP:MGI.
DR   GO; GO:0003723; F:RNA binding; TAS:MGI.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR   GO; GO:0008283; P:cell proliferation; TAS:MGI.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IMP:UniProtKB.
DR   GO; GO:0051583; P:dopamine uptake; IMP:MGI.
DR   GO; GO:0042743; P:hydrogen peroxide metabolic process; IMP:MGI.
DR   GO; GO:0051899; P:membrane depolarization; IMP:MGI.
DR   GO; GO:0060081; P:membrane hyperpolarization; IMP:MGI.
DR   GO; GO:2000277; P:positive regulation of oxidative phosphorylation uncoupler activity; IMP:UniProtKB.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IDA:MGI.
DR   InterPro; IPR006287; DJ1.
DR   InterPro; IPR002818; ThiJ/PfpI.
DR   Pfam; PF01965; DJ-1_PfpI; 1.
DR   TIGRFAMs; TIGR01383; not_thiJ; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Autophagy; Chaperone; Cytoplasm;
KW   Direct protein sequencing; Fertilization; Hydrolase;
KW   Inflammatory response; Isopeptide bond; Mitochondrion; Nucleus;
KW   Oxidation; Phosphoprotein; Protease; RNA-binding; Stress response;
KW   Tumor suppressor; Ubl conjugation; Zymogen.
FT   CHAIN         1      ?       Protein DJ-1.
FT                                /FTId=PRO_0000157850.
FT   PROPEP        ?    189       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000405560.
FT   ACT_SITE    106    106       By similarity.
FT   ACT_SITE    126    126       By similarity.
FT   MOD_RES      67     67       Phosphotyrosine (By similarity).
FT   MOD_RES     106    106       Cysteine sulfinic acid (-SO2H) (By
FT                                similarity).
FT   MOD_RES     148    148       N6-acetyllysine (By similarity).
FT   CROSSLNK    130    130       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   MUTAGEN      46     46       C->A: Sulfinic acid detected following
FT                                treatment with hydrogen peroxide.
FT   MUTAGEN      53     53       C->A: Sulfinic acid detected following
FT                                treatment with hydrogen peroxide.
FT   MUTAGEN     106    106       C->A: No sulfinic acid detected following
FT                                treatment with hydrogen peroxide.
FT   CONFLICT    127    127       P -> T (in Ref. 2; BAE40278).
SQ   SEQUENCE   189 AA;  20021 MW;  877C825CCA07468F CRC64;
     MASKRALVIL AKGAEEMETV IPVDVMRRAG IKVTVAGLAG KDPVQCSRDV MICPDTSLED
     AKTQGPYDVV VLPGGNLGAQ NLSESPMVKE ILKEQESRKG LIAAICAGPT ALLAHEVGFG
     CKVTTHPLAK DKMMNGSHYS YSESRVEKDG LILTSRGPGT SFEFALAIVE ALVGKDMANQ
     VKAPLVLKD
//
ID   NDUS5_MOUSE             Reviewed;         106 AA.
AC   Q99LY9; Q3U734;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 5;
DE   AltName: Full=Complex I-15 kDa;
DE            Short=CI-15 kDa;
DE   AltName: Full=NADH-ubiquinone oxidoreductase 15 kDa subunit;
GN   Name=Ndufs5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 1-7; 16-27 AND 57-68, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Accessory subunit of the mitochondrial membrane
CC       respiratory chain NADH dehydrogenase (Complex I), that is believed
CC       not to be involved in catalysis. Complex I functions in the
CC       transfer of electrons from NADH to the respiratory chain. The
CC       immediate electron acceptor for the enzyme is believed to be
CC       ubiquinone (By similarity).
CC   -!- SUBUNIT: Mammalian complex I is composed of 45 different subunits.
CC       This is a component of the iron-sulfur (IP) fragment of the enzyme
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein; Matrix side (By similarity).
CC   -!- SIMILARITY: Belongs to the complex I NDUFS5 subunit family.
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DR   EMBL; AK148505; BAE28590.1; -; mRNA.
DR   EMBL; AK152845; BAE31538.1; -; mRNA.
DR   EMBL; AL606932; CAM18556.1; -; Genomic_DNA.
DR   EMBL; CH466521; EDK98017.1; -; Genomic_DNA.
DR   EMBL; CH466552; EDL30376.1; -; Genomic_DNA.
DR   EMBL; BC081434; AAH81434.1; -; mRNA.
DR   IPI; IPI00117300; -.
DR   RefSeq; NP_001025445.1; NM_001030274.1.
DR   RefSeq; XP_003086650.1; XM_003086602.1.
DR   UniGene; Mm.375824; -.
DR   UniGene; Mm.42805; -.
DR   STRING; Q99LY9; -.
DR   PRIDE; Q99LY9; -.
DR   Ensembl; ENSMUST00000030401; ENSMUSP00000030401; ENSMUSG00000028648.
DR   Ensembl; ENSMUST00000106206; ENSMUSP00000101812; ENSMUSG00000028648.
DR   Ensembl; ENSMUST00000106207; ENSMUSP00000101813; ENSMUSG00000028648.
DR   GeneID; 100504968; -.
DR   GeneID; 595136; -.
DR   KEGG; mmu:100504968; -.
DR   KEGG; mmu:595136; -.
DR   UCSC; uc008upu.1; mouse.
DR   CTD; 595136; -.
DR   MGI; MGI:1890889; Ndufs5.
DR   GeneTree; ENSGT00390000002919; -.
DR   HOGENOM; HBG716328; -.
DR   HOVERGEN; HBG001646; -.
DR   InParanoid; Q99LY9; -.
DR   OMA; PFFDVQK; -.
DR   OrthoDB; EOG4BCDPF; -.
DR   PhylomeDB; Q99LY9; -.
DR   NextBio; 414443; -.
DR   ArrayExpress; Q99LY9; -.
DR   Bgee; Q99LY9; -.
DR   Genevestigator; Q99LY9; -.
DR   GermOnline; ENSMUSG00000028648; Mus musculus.
DR   GermOnline; ENSMUSG00000043062; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR019342; NADH_UbQ_OxRdtase_FeS-su5.
DR   Pfam; PF10200; Ndufs5; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Respiratory chain;
KW   Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    106       NADH dehydrogenase [ubiquinone] iron-
FT                                sulfur protein 5.
FT                                /FTId=PRO_0000118787.
SQ   SEQUENCE   106 AA;  12648 MW;  DA74C0EEE1EB5C54 CRC64;
     MPFLDIQKKL GISLDRHFMF LSAEQPYKNA ARCHAFEKEW IECAHGIGGT RAKKECKIEF
     DDFEECLLRY KTMRRMHDIK KQREKLMKEG KYTPPPHHSG REEPRP
//
ID   PTPRT_MOUSE             Reviewed;        1454 AA.
AC   Q99M80; Q99M81; Q99M82; Q9JIZ1; Q9JIZ2; Q9JKC2; Q9JLP0;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2003, sequence version 2.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Receptor-type tyrosine-protein phosphatase T;
DE            Short=R-PTP-T;
DE            EC=3.1.3.48;
DE   AltName: Full=RPTPmam4;
DE   AltName: Full=Receptor-type tyrosine-protein phosphatase rho;
DE            Short=RPTP-rho;
DE            Short=mRPTPrho;
DE   Flags: Precursor;
GN   Name=Ptprt;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 5), AND ALTERNATIVE
RP   SPLICING.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=22730707; PubMed=11423001;
RA   Besco J.A., Frostholm A., Popesco M.C., Burghes A.H.M., Rotter A.;
RT   "Genomic organization and alternative splicing of the human and mouse
RT   RPTPrho genes.";
RL   BMC Genomics 2:1-1(2001).
RN   [2]
RP   ERRATUM.
RX   MEDLINE=22730717; PubMed=11814386;
RA   Besco J.A., Frostholm A., Popesco M.C., Burghes A.H.M., Rotter A.;
RL   BMC Genomics 2:5-5(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
RA   Buchli A.D., Zimmermann D.R., Pfister F., Vaughan L.;
RT   "RPTPmam4: a fourth member of the MAM family of receptor protein
RT   tyrosine phosphatases expressed in adult brain.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
RA   Mizuta M., Bergman B., Miki T., Hutton J.C.;
RT   "Molecular cloning and functional characterization on mouse receptor-
RT   like protein tyrosine phosphatase, mRPTPrho, which mediates cell-cell
RT   adhesion of pancreatic beta cells.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=98146229; PubMed=9486824;
RX   DOI=10.1002/(SICI)1096-9861(19980222)391:4<444::AID-CNE3>3.0.CO;2-0;
RA   McAndrew P.E., Frostholm A., Evans J.E., Zdilar D., Goldowitz D.,
RA   Chiu I.-M., Burghes A.H.M., Rotter A.;
RT   "Novel receptor protein tyrosine phosphatase (RPTPrho) and acidic
RT   fibroblast growth factor (FGF-1) transcripts delineate a rostrocaudal
RT   boundary in the granule cell layer of the murine cerebellar cortex.";
RL   J. Comp. Neurol. 391:444-455(1998).
CC   -!- FUNCTION: May be involved in both signal transduction and cellular
CC       adhesion in the CNS. May have specific signaling roles in the
CC       tyrosine phosphorylation/dephosphorylation pathway in the anterior
CC       compartment of the adult cerebellar cortex.
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q99M80-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99M80-2; Sequence=VSP_007803, VSP_007806;
CC       Name=3; Synonyms=RPTPrho2;
CC         IsoId=Q99M80-3; Sequence=VSP_007803, VSP_007804;
CC       Name=4; Synonyms=RPTPrho1;
CC         IsoId=Q99M80-4; Sequence=VSP_007803;
CC       Name=5;
CC         IsoId=Q99M80-5; Sequence=VSP_007803, VSP_007805;
CC   -!- TISSUE SPECIFICITY: Expression is restricted to the CNS.
CC       Distributed throughout the brain and spinal cord.
CC   -!- DEVELOPMENTAL STAGE: Exceptionally high levels found in the cortex
CC       and olfactory bulbs during perinatal development and are down-
CC       regulated during postnatal week 2. Expression in the cerebellar
CC       cortex is restricted to the granule cell layer of lobules 1-6.
CC       Anterior and posterior compartments become discernible only during
CC       postnatal weeks 2 and 6.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 2B subfamily.
CC   -!- SIMILARITY: Contains 4 fibronectin type-III domains.
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 1 MAM domain.
CC   -!- SIMILARITY: Contains 2 tyrosine-protein phosphatase domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF152556; AAD34158.4; -; mRNA.
DR   EMBL; AY026861; AAK18741.1; -; mRNA.
DR   EMBL; AY026862; AAK18742.1; -; mRNA.
DR   EMBL; AY026863; AAK18743.1; -; mRNA.
DR   EMBL; AF244125; AAF44712.1; -; mRNA.
DR   EMBL; AF162856; AAF82400.2; -; mRNA.
DR   EMBL; AF162857; AAF82401.1; -; mRNA.
DR   IPI; IPI00117289; -.
DR   IPI; IPI00336658; -.
DR   IPI; IPI00336660; -.
DR   IPI; IPI00620415; -.
DR   IPI; IPI00874897; -.
DR   RefSeq; NP_067439.1; NM_021464.4.
DR   UniGene; Mm.235807; -.
DR   UniGene; Mm.381206; -.
DR   ProteinModelPortal; Q99M80; -.
DR   SMR; Q99M80; 33-595, 877-1453.
DR   STRING; Q99M80; -.
DR   PhosphoSite; Q99M80; -.
DR   PRIDE; Q99M80; -.
DR   Ensembl; ENSMUST00000080004; ENSMUSP00000078917; ENSMUSG00000053141.
DR   Ensembl; ENSMUST00000109442; ENSMUSP00000105068; ENSMUSG00000053141.
DR   GeneID; 19281; -.
DR   KEGG; mmu:19281; -.
DR   UCSC; uc008nrw.1; mouse.
DR   UCSC; uc008nrx.1; mouse.
DR   UCSC; uc008nrz.1; mouse.
DR   CTD; 19281; -.
DR   MGI; MGI:1321152; Ptprt.
DR   eggNOG; roNOG06182; -.
DR   HOVERGEN; HBG062785; -.
DR   OMA; NRNDEGF; -.
DR   PhylomeDB; Q99M80; -.
DR   BRENDA; 3.1.3.48; 244.
DR   ArrayExpress; Q99M80; -.
DR   Bgee; Q99M80; -.
DR   CleanEx; MM_PTPRT; -.
DR   Genevestigator; Q99M80; -.
DR   GermOnline; ENSMUSG00000053141; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0051393; F:alpha-actinin binding; IDA:MGI.
DR   GO; GO:0045294; F:alpha-catenin binding; IDA:MGI.
DR   GO; GO:0008013; F:beta-catenin binding; IDA:MGI.
DR   GO; GO:0045296; F:cadherin binding; IPI:MGI.
DR   GO; GO:0070097; F:delta-catenin binding; IPI:MGI.
DR   GO; GO:0045295; F:gamma-catenin binding; IPI:MGI.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IMP:MGI.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0016790; F:thiolester hydrolase activity; IDA:MGI.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:MGI.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR000998; MAM_dom.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 4.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF00629; MAM; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00020; MAMDOMAIN.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 3.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00137; MAM; 1.
DR   SMART; SM00194; PTPc; 2.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
DR   SUPFAM; SSF49265; FN_III-like; 3.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00740; MAM_1; 1.
DR   PROSITE; PS50060; MAM_2; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Immunoglobulin domain; Membrane; Protein phosphatase; Receptor;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     29       Potential.
FT   CHAIN        30   1454       Receptor-type tyrosine-protein
FT                                phosphatase T.
FT                                /FTId=PRO_0000025464.
FT   TOPO_DOM     30    770       Extracellular (Potential).
FT   TRANSMEM    771    791       Helical; (Potential).
FT   TOPO_DOM    792   1454       Cytoplasmic (Potential).
FT   DOMAIN       34    195       MAM.
FT   DOMAIN      197    288       Ig-like C2-type.
FT   DOMAIN      292    383       Fibronectin type-III 1.
FT   DOMAIN      390    484       Fibronectin type-III 2.
FT   DOMAIN      485    588       Fibronectin type-III 3.
FT   DOMAIN      670    767       Fibronectin type-III 4.
FT   DOMAIN      902   1156       Tyrosine-protein phosphatase 1.
FT   DOMAIN     1188   1450       Tyrosine-protein phosphatase 2.
FT   REGION     1097   1103       Substrate binding (By similarity).
FT   ACT_SITE   1097   1097       Phosphocysteine intermediate (By
FT                                similarity).
FT   ACT_SITE   1391   1391       Phosphocysteine intermediate (By
FT                                similarity).
FT   BINDING    1065   1065       Substrate (By similarity).
FT   BINDING    1141   1141       Substrate (By similarity).
FT   CARBOHYD     82     82       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    102    102       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    141    141       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    212    212       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    425    425       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    514    514       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    551    551       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    605    605       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    658    658       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    688    688       N-linked (GlcNAc...) (Potential).
FT   DISULFID    217    271       Potential.
FT   VAR_SEQ     731    749       Missing (in isoform 2, isoform 3, isoform
FT                                4 and isoform 5).
FT                                /FTId=VSP_007803.
FT   VAR_SEQ     794    794       R -> RRNAYSYSYYL (in isoform 3).
FT                                /FTId=VSP_007804.
FT   VAR_SEQ     794    794       R -> RRNAYSYSYYLSQR (in isoform 5).
FT                                /FTId=VSP_007805.
FT   VAR_SEQ    1007   1007       R -> RHPAEHTVGTATLGRAASPGM (in isoform
FT                                2).
FT                                /FTId=VSP_007806.
FT   CONFLICT     13     16       Missing (in Ref. 1; AAD34158).
FT   CONFLICT     21     21       R -> P (in Ref. 1; AAD34158).
FT   CONFLICT     34     37       GGCS -> RGVF (in Ref. 1; AAD34158).
FT   CONFLICT     87     87       A -> T (in Ref. 4; AAF82401).
FT   CONFLICT    254    254       A -> S (in Ref. 4; AAF82401).
FT   CONFLICT    266    266       I -> V (in Ref. 4; AAF82401).
FT   CONFLICT    602    602       T -> S (in Ref. 4; AAF82401).
FT   CONFLICT    822    822       A -> T (in Ref. 4; AAF82401).
FT   CONFLICT    825    825       G -> S (in Ref. 4; AAF82401).
FT   CONFLICT    844    845       TD -> N (in Ref. 4; AAF82401).
FT   CONFLICT   1016   1016       D -> A (in Ref. 4; AAF82401).
FT   CONFLICT   1049   1049       Y -> H (in Ref. 1; AAD34158).
FT   CONFLICT   1050   1050       H -> N (in Ref. 4; AAF82401).
FT   CONFLICT   1076   1076       L -> V (in Ref. 4; AAF82401).
FT   CONFLICT   1103   1103       R -> K (in Ref. 1; AAD34158).
FT   CONFLICT   1259   1259       F -> L (in Ref. 4; AAF82401).
FT   CONFLICT   1266   1266       L -> I (in Ref. 4; AAF82401).
FT   CONFLICT   1269   1269       T -> S (in Ref. 4; AAF82401).
SQ   SEQUENCE   1454 AA;  163012 MW;  C60464F7B423F8A8 CRC64;
     MGSLGGLALC LLRLLLLGLQ RPPLPGAGAQ SAAGGCSFDE HYSNCGYSVA LGTNGFTWEQ
     INTWEKPMLD PAVPTGSFMM VNSSGRASGQ KAHLLLPTLK ENDTHCIDFH YYFSSRDRSS
     PGALNVYVKV NGGPQGNPVW NVSGVVTEGW VKAELAISTF WPHFYQVIFE SVSLKGHPGY
     IAVDEVRVLA HPCRKAPHFL RLQNVEVNVG QNATFQCIAG GKWSQHDKLW LQQWNGRDTA
     LMVTRVVNHR RFSATVSVAD TSQRSISKYR CVIRSDGGSG VSNYAELIVK EPPTPIAPPE
     LLAVGATYLW IKPNANSIIG DGPIILKEVE YRTTTGTWAE THIVDSPNYK LWHLDPDVEY
     EIRVLLTRPG EGGTGPPGPP LTTRTKCADP VHGPQNVEIV DIRARQLTLQ WEPFGYAVTR
     CHSYNLTVQY QYVFNQQQYE AEEVIQTSSH YTLRGLRPFM TIRLRLLLSN PEGRMESEEL
     VVQTEEDVPG AVPLESIQGG PFEEKIYIQW KPPNETNGVI TLYEINYKAV GSLDPSADLS
     SQRGKVFKLR NETHHLFVGL YPGTTYSFTI KASTAKGFGP PVTTRIATKI SAPSMPEYDA
     DTPLNETDTT ITVMLKPAQS RGAPVSVYQL VVKEERLQKS RRAADIIECF SVPVSYRNAS
     NLDSLHYFAA ELKPSNLPVT QPFTVGDNKT YNGYWNPPLS PLKSYSIYFQ ALSKANGETK
     INCVRLATKG APMGSAQVTP GTPLCLLTTA STQNSNTVEP EKQVDNTVKM AGVIAGLLMF
     IIILLGVMLT IKRRKLAKKQ KETQSGAQRE MGPVASTDKP TAKLGTNRND EGFSSSSQDV
     NGFTDGSRGE LSQPTLTIQT HPYRTCDPVE MSYPRDQFQP AIRVADLLQH ITQMKRGQGY
     GFKEEYEALP EGQTASWDTA KEDENRNKNR YGNIISYDHS RVRLLVLDGD PHSDYINANY
     IDGYHRPRHY IATQGPMQET VKDFWRMIWQ ENSASIVMVT NLVEVGRVKC VRYWPDDTEV
     YGDIKVTLIE TEPLAEYVIR TFTVQKKGYH EIRELRLFHF TSWPDHGVPC YATGLLGFVR
     QVKFLNPPEA GPIVVHCSAG AGRTGCFIAI DTMLDMAENE GVVDIFNCVR ELRAQRVNLV
     QTEEQYVFVH DAILEACLCG NTAIPVCEFR SLYYNISRLD PQTNSSQIKD EFQTLNIVTP
     RVRPEDCSIG LLPRNHDKNR SMDVLPLDRC LPFLISVDGE SSNYINAALM DSHKQPAAFV
     VTQHPLPNTV ADFWRLVFDY NCSSVVMLNE MDTAQLCMQY WPEKTSGCYG PIQVEFVSAD
     IDEDIIHRIF RICNMARPQD GYRIVQHLQY IGWPAYRDTP PSKRSLLKVV RRLEKWQEQY
     DGREGRTVVH CLNGGGRSGT FCAICSVCEM IQQQNIIDVF HIVKTLRNNK SNMVETLEQY
     KFVYEVALEY LSSF
//
ID   DNJA3_MOUSE             Reviewed;         480 AA.
AC   Q99M87; Q8BSM0; Q99L09; Q99P71; Q99P76; Q9CT11; Q9DBJ7; Q9DC44;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=DnaJ homolog subfamily A member 3, mitochondrial;
DE   AltName: Full=DnaJ protein Tid-1;
DE            Short=mTid-1;
DE   AltName: Full=Tumorous imaginal discs protein Tid56 homolog;
DE   Flags: Precursor;
GN   Name=Dnaja3; Synonyms=Tid1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND INTERACTION WITH
RP   RASA1.
RC   STRAIN=C57BL/6 X CBA;
RX   PubMed=11116152; DOI=10.1074/jbc.M009267200;
RA   Trentin G.A., Yin X., Tahir S., Lhotak S., Farhang-Fallah J., Li Y.,
RA   Rozakis-Adcock M.;
RT   "A mouse homologue of the Drosophila tumor suppressor l(2)tid gene
RT   defines a novel Ras GTPase-activating protein (RasGAP)-binding
RT   protein.";
RL   J. Biol. Chem. 276:13087-13095(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Forelimb, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Modulates apoptotic signal transduction or effector
CC       structures within the mitochondrial matrix. Affect cytochrome C
CC       release from the mitochondria and caspase 3 activation, but not
CC       caspase 8 activation. Isoform 1 increases apoptosis triggered by
CC       both TNF and the DNA-damaging agent mytomycin C; in sharp
CC       contrast, isoform 2 suppresses apoptosis. Can modulate IFN-gamma-
CC       mediated transcriptional activity (By similarity).
CC   -!- SUBUNIT: Interacts with JAK2, HSPA9B and IFN-gammaR2 chain.
CC       Interacts with Ras GTPase-activating protein 1 (RASA1).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Tid-1L, TID1L;
CC         IsoId=Q99M87-1; Sequence=Displayed;
CC       Name=2; Synonyms=Tid-1S, TID1S;
CC         IsoId=Q99M87-2; Sequence=VSP_007427, VSP_007428;
CC       Name=3;
CC         IsoId=Q99M87-3; Sequence=VSP_007440;
CC   -!- DOMAIN: Modulation of apoptosis, i.e proapoptotic activity of
CC       isoform 1 and antiapoptotic activity of isoform 2, is J domain-
CC       dependent (By similarity).
CC   -!- PTM: Tyrosine phosphorylated.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 CR-type zinc finger.
CC   -!- SIMILARITY: Contains 1 J domain.
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DR   EMBL; AY009320; AAG37303.1; -; mRNA.
DR   EMBL; AF325535; AAK11222.1; -; mRNA.
DR   EMBL; AF326358; AAK11223.1; -; mRNA.
DR   EMBL; AK004575; BAB23384.1; -; mRNA.
DR   EMBL; AK004910; BAB23661.1; -; mRNA.
DR   EMBL; AK011535; BAB27682.2; -; mRNA.
DR   EMBL; AK031250; BAC27321.1; -; mRNA.
DR   EMBL; BC003920; AAH03920.1; -; mRNA.
DR   EMBL; BC027240; AAH27240.1; -; mRNA.
DR   IPI; IPI00120414; -.
DR   IPI; IPI00279858; -.
DR   IPI; IPI00347634; -.
DR   RefSeq; NP_001128584.1; NM_001135112.1.
DR   RefSeq; NP_076135.3; NM_023646.4.
DR   UniGene; Mm.248337; -.
DR   ProteinModelPortal; Q99M87; -.
DR   SMR; Q99M87; 87-160, 203-429.
DR   IntAct; Q99M87; 1.
DR   STRING; Q99M87; -.
DR   PhosphoSite; Q99M87; -.
DR   PRIDE; Q99M87; -.
DR   Ensembl; ENSMUST00000060067; ENSMUSP00000053842; ENSMUSG00000004069.
DR   Ensembl; ENSMUST00000115853; ENSMUSP00000111519; ENSMUSG00000004069.
DR   Ensembl; ENSMUST00000115854; ENSMUSP00000111520; ENSMUSG00000004069.
DR   GeneID; 83945; -.
DR   KEGG; mmu:83945; -.
DR   UCSC; uc007yac.1; mouse.
DR   UCSC; uc007yad.1; mouse.
DR   CTD; 83945; -.
DR   MGI; MGI:1933786; Dnaja3.
DR   GeneTree; ENSGT00580000081611; -.
DR   HOVERGEN; HBG051371; -.
DR   InParanoid; Q99M87; -.
DR   OMA; GQTKQKK; -.
DR   OrthoDB; EOG4CVG73; -.
DR   PhylomeDB; Q99M87; -.
DR   NextBio; 350822; -.
DR   ArrayExpress; Q99M87; -.
DR   Bgee; Q99M87; -.
DR   CleanEx; MM_DNAJA3; -.
DR   Genevestigator; Q99M87; -.
DR   GermOnline; ENSMUSG00000004069; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005083; F:small GTPase regulator activity; IPI:MGI.
DR   GO; GO:0051082; F:unfolded protein binding; IPI:MGI.
DR   GO; GO:0006924; P:activation-induced cell death of T cells; IMP:MGI.
DR   GO; GO:0007569; P:cell aging; IDA:MGI.
DR   GO; GO:0009790; P:embryo development; IMP:MGI.
DR   GO; GO:0006264; P:mitochondrial DNA replication; IMP:MGI.
DR   GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:MGI.
DR   GO; GO:0009408; P:response to heat; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IPI:MGI.
DR   GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR   InterPro; IPR012724; DnaJ.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_N.
DR   InterPro; IPR018253; Heat_shock_DnaJ_CS.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR003095; Hsp_DnaJ.
DR   InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR   Gene3D; G3DSA:1.10.287.110; DnaJ_N; 1.
DR   Gene3D; G3DSA:2.10.230.10; HSP_DnaJ_cys-rich; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; DnaJ_N; 1.
DR   SUPFAM; SSF49493; HSP40_DnaJ_pep; 2.
DR   SUPFAM; SSF57938; HSP_DnaJ_cys-rich; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51188; ZF_CR; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Apoptosis; Chaperone; Metal-binding;
KW   Mitochondrion; Phosphoprotein; Repeat; Transit peptide; Zinc;
KW   Zinc-finger.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    480       DnaJ homolog subfamily A member 3,
FT                                mitochondrial.
FT                                /FTId=PRO_0000007257.
FT   DOMAIN       93    158       J.
FT   REPEAT      236    243       CXXCXGXG motif.
FT   REPEAT      253    260       CXXCXGXG motif.
FT   REPEAT      275    282       CXXCXGXG motif.
FT   REPEAT      289    296       CXXCXGXG motif.
FT   ZN_FING     223    301       CR-type.
FT   METAL       236    236       Zinc 1 (By similarity).
FT   METAL       239    239       Zinc 1 (By similarity).
FT   METAL       253    253       Zinc 2 (By similarity).
FT   METAL       256    256       Zinc 2 (By similarity).
FT   METAL       275    275       Zinc 2 (By similarity).
FT   METAL       278    278       Zinc 2 (By similarity).
FT   METAL       289    289       Zinc 1 (By similarity).
FT   METAL       292    292       Zinc 1 (By similarity).
FT   MOD_RES     169    169       Phosphoserine (By similarity).
FT   VAR_SEQ     211    261       Missing (in isoform 3).
FT                                /FTId=VSP_007440.
FT   VAR_SEQ     448    453       GRTMDS -> KRSTGN (in isoform 2).
FT                                /FTId=VSP_007427.
FT   VAR_SEQ     454    480       Missing (in isoform 2).
FT                                /FTId=VSP_007428.
FT   CONFLICT    403    403       D -> H (in Ref. 2; BAB23661).
FT   CONFLICT    456    456       G -> E (in Ref. 2; BAB23384).
SQ   SEQUENCE   480 AA;  52443 MW;  30AA5557C18665A8 CRC64;
     MAAWCSPRWL RVAVGTPRLP AAAGRGVQQP QGGVVATSLC RKLCVSAFGL SMGAHGPRAL
     LTLRPGVRLT GTKSFPFVCT TSFHTSASLA KDDYYQILGV PRNASQKDIK KAYYQLAKKY
     HPDTNKDDPK AKEKFSQLAE AYEVLSDEVK RKQYDAYGSA GFDPGTSSSG QGYWRGGPSV
     DPEELFRKIF GEFSSSPFGD FQNVFDQPQE YIMELTFNQA AKGVNKEFTV NIMDTCERCD
     GKGNEPGTKV QHCHYCGGSG METINTGPFV MRSTCRRCGG RGSIITNPCV VCRGAGQAKQ
     KKRVTIPVPA GVEDGQTVRM PVGKREIFVT FRVQKSPVFR RDGADIHSDL FISIAQAILG
     GTAKAQGLYE TINVTIPAGI QTDQKIRLTG KGIPRINSYG YGDHYIHIKI RVPKRLSSRQ
     QNLILSYAED ETDVEGTVNG VTHTSTGGRT MDSSAGSKDR REAGEDNEGF LSKLKKIFTS
//
ID   RB6I2_MOUSE             Reviewed;        1120 AA.
AC   Q99MI1; Q80TK7; Q8BPL1; Q8C7Y1; Q99MI2;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=ELKS/Rab6-interacting/CAST family member 1;
DE            Short=ERC-1;
DE   AltName: Full=CAZ-associated structural protein 2;
DE            Short=CAST2;
DE   AltName: Full=Rab6-interacting protein 2;
GN   Name=Erc1; Synonyms=Cast2, Kiaa1081, Rab6ip2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND INTERACTION WITH RAB6A AND RAB6B.
RX   MEDLINE=21927812; PubMed=11929610;
RX   DOI=10.1034/j.1600-0854.2002.030406.x;
RA   Monier S., Jollivet F., Janoueix-Lerosey I., Johannes L., Goud B.;
RT   "Characterization of novel Rab6-interacting proteins involved in
RT   endosome-to-TGN transport.";
RL   Traffic 3:289-297(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX   PubMed=14723704; DOI=10.1111/j.1356-9597.2004.00697.x;
RA   Deguchi-Tawarada M., Inoue E., Takao-Rikitsu E., Inoue M., Ohtsuka T.,
RA   Takai Y.;
RT   "CAST2: identification and characterization of a protein structurally
RT   related to the presynaptic cytomatrix protein CAST.";
RL   Genes Cells 9:15-23(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-351 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 691-1120 (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Regulatory subunit of the IKK complex. Probably recruits
CC       IkappaBalpha/NFKBIA to the complex (By similarity). May be
CC       involved in the organization of the cytomatrix at the nerve
CC       terminals active zone (CAZ) which regulates neurotransmitter
CC       release. May be involved in vesicle trafficking at the CAZ. May be
CC       involved in Rab-6 regulated endosomes to Golgi transport.
CC   -!- SUBUNIT: Interacts with the GTB-bound forms of RAB6A isoform 1 and
CC       isoform 2 and with RAB6B. The interaction was strongest with
CC       RAB6B, followed by RAB6A isoform 2 and weakest with RAB6A isoform
CC       1. Part of a complex with CHUK, IKBKB and IKBKG. Interacts with
CC       CHUK, IKBKB and IKBKG. The interaction with IKBKG is independent
CC       of CHUK and IKBKB. Interacts with NFKBIA (By similarity). Isoform
CC       2 interacts through its C-terminus with the PDZ domains of RIMS1
CC       and RIMS2. Interacts with ERC2/CAST1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC       protein. Golgi apparatus membrane; Peripheral membrane protein.
CC       Note=In neurons, localized closed to presynaptic membrane.
CC       Recruited on Golgi membranes by RAB6A in a GTP-dependent manner.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=B, beta;
CC         IsoId=Q99MI1-1; Sequence=Displayed;
CC       Name=2; Synonyms=A;
CC         IsoId=Q99MI1-2; Sequence=VSP_011460, VSP_011462, VSP_011463;
CC       Name=3;
CC         IsoId=Q99MI1-3; Sequence=VSP_011460, VSP_011461;
CC       Name=4;
CC         IsoId=Q99MI1-4; Sequence=VSP_011456, VSP_011457, VSP_011458,
CC                                  VSP_011459;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- SIMILARITY: Contains 1 FIP-RBD domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF340028; AAK26381.1; -; mRNA.
DR   EMBL; AF340029; AAK26382.1; -; mRNA.
DR   EMBL; AY316692; AAP83581.1; -; mRNA.
DR   EMBL; AK048990; BAC33505.1; -; mRNA.
DR   EMBL; AK053824; BAC35542.1; -; mRNA.
DR   EMBL; AK122437; BAC65719.1; -; Transcribed_RNA.
DR   IPI; IPI00117731; -.
DR   IPI; IPI00117733; -.
DR   IPI; IPI00226953; -.
DR   IPI; IPI00457547; -.
DR   RefSeq; NP_444434.2; NM_053204.2.
DR   RefSeq; NP_835186.1; NM_178085.3.
DR   UniGene; Mm.288860; -.
DR   UniGene; Mm.446801; -.
DR   ProteinModelPortal; Q99MI1; -.
DR   STRING; Q99MI1; -.
DR   PhosphoSite; Q99MI1; -.
DR   PRIDE; Q99MI1; -.
DR   Ensembl; ENSMUST00000032279; ENSMUSP00000032279; ENSMUSG00000030172.
DR   Ensembl; ENSMUST00000071356; ENSMUSP00000071314; ENSMUSG00000030172.
DR   Ensembl; ENSMUST00000079582; ENSMUSP00000078534; ENSMUSG00000030172.
DR   Ensembl; ENSMUST00000112732; ENSMUSP00000108352; ENSMUSG00000030172.
DR   GeneID; 111173; -.
DR   KEGG; mmu:111173; -.
DR   UCSC; uc009dmk.1; mouse.
DR   UCSC; uc009dmn.1; mouse.
DR   CTD; 111173; -.
DR   MGI; MGI:2151013; Erc1.
DR   eggNOG; roNOG10776; -.
DR   GeneTree; ENSGT00390000015969; -.
DR   HOGENOM; HBG446371; -.
DR   HOVERGEN; HBG051496; -.
DR   InParanoid; Q99MI1; -.
DR   OrthoDB; EOG434W5B; -.
DR   PhylomeDB; Q99MI1; -.
DR   NextBio; 365451; -.
DR   ArrayExpress; Q99MI1; -.
DR   Bgee; Q99MI1; -.
DR   CleanEx; MM_ERC1; -.
DR   Genevestigator; Q99MI1; -.
DR   GermOnline; ENSMUSG00000030172; Mus musculus.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0017137; F:Rab GTPase binding; IDA:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0042147; P:retrograde transport, endosome to Golgi; IDA:MGI.
DR   InterPro; IPR019323; CAZ_cplx_RIM-bd_prot.
DR   InterPro; IPR010356; Haemolysin_E.
DR   InterPro; IPR019018; Rab11-bd_FIP_dom_C.
DR   Gene3D; G3DSA:1.20.1170.10; Haemolysin_E; 1.
DR   Pfam; PF10174; Cast; 1.
DR   Pfam; PF09457; RBD-FIP; 1.
DR   PROSITE; PS51511; FIP_RBD; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Golgi apparatus;
KW   Membrane; Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1   1120       ELKS/Rab6-interacting/CAST family member
FT                                1.
FT                                /FTId=PRO_0000097177.
FT   DOMAIN     1050   1112       FIP-RBD.
FT   COILED      144    992       Potential.
FT   COILED     1060   1104       Potential.
FT   MOD_RES      17     17       Phosphoserine (By similarity).
FT   MOD_RES      21     21       Phosphoserine (By similarity).
FT   MOD_RES      75     75       Phosphoserine (By similarity).
FT   MOD_RES     191    191       Phosphoserine (By similarity).
FT   MOD_RES     252    252       Phosphoserine.
FT   MOD_RES    1050   1050       Phosphothreonine (By similarity).
FT   VAR_SEQ       1    151       Missing (in isoform 4).
FT                                /FTId=VSP_011456.
FT   VAR_SEQ     440    467       Missing (in isoform 4).
FT                                /FTId=VSP_011457.
FT   VAR_SEQ     525    547       DALRLRLEEKETMLNKKTKQIQD -> KSFCDLCRIQSIPS
FT                                FILLYICYV (in isoform 4).
FT                                /FTId=VSP_011458.
FT   VAR_SEQ     548   1120       Missing (in isoform 4).
FT                                /FTId=VSP_011459.
FT   VAR_SEQ     834    877       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_011460.
FT   VAR_SEQ    1012   1012       Q -> QDEEEGIWALSSAILFRT (in isoform 3).
FT                                /FTId=VSP_011461.
FT   VAR_SEQ    1013   1020       IIQPLLEL -> DEEEGIWA (in isoform 2).
FT                                /FTId=VSP_011462.
FT   VAR_SEQ    1021   1120       Missing (in isoform 2).
FT                                /FTId=VSP_011463.
FT   CONFLICT    121    121       D -> G (in Ref. 3; BAC35542).
FT   CONFLICT   1070   1070       Q -> K (in Ref. 4; BAC65719).
SQ   SEQUENCE   1120 AA;  128331 MW;  A542B526FAEDF9C7 CRC64;
     MYGSARSVGK VEPSSQSPGR SPRLPRSPRL GHRRTNSTGG SSGNSVGGGS GKTLSMENIQ
     SLNAAYATSG PMYLSDHENV GAETPKSTMT LGRSGGRLPY GVRMTAMGSS PNIASSGVAS
     DTIAFGEHHL PPVSMASTVP HSLRQARDNT IMDLQTQLKE VLRENDLLRK DVEVKESKLS
     SSMNSIKTFW SPELKKERAL RKDEASKITI WKEQYRVVQE ENQHMQMTIQ ALQDELRIQR
     DLNQLFQQDS SSRTGEPCVA ELTEENFQRL HAEHERQAKE LFLLRKTLEE MELRIETQKQ
     TLNARDESIK KLLEMLQSKG LSAKATEEDH ERTRRLAEAE MHVHHLESLL EQKEKENNML
     REEMHRRFEN APDSAKTKAL QTVIEMKDSK ISSMERGLRD LEEEIQMLKS NGALSSEERE
     EEMKQMEVYR SHSKFMKNKV EQLKEELSSK DAQGEELKKR AAGLQSEIGQ VKQELSRKDT
     ELLALQTKLE TLTNQFSDSK QHIEVLKESL TAKEQRAAIL QTEVDALRLR LEEKETMLNK
     KTKQIQDMAE EKGTQAGEIH DLKDMLDVKE RKVNVLQKKI ENLQEQLRDK EKQMSSLKER
     VKSLQADTTN TDTALTTLEE ALADKERTIE RLKEQRDRDE REKQEEIDTY KKDLKDLREK
     VSLLQGDLSE KEASLLDIKE HASSLASSGL KKDSRLKTLE IALEQKKEEC LKMESQLKKA
     HEATLEARAS PEMSDRIQQL EREISRYKDE SSKAQTEVDR LLEILKEVEN EKNDKDKKIA
     ELESLTSRQV KDQNKKVANL KHKEQVEKKK SAQMLEEARR REDSLSDSSQ QLQDSLRKKD
     DRIEELEEAL RESVQITAER EMVLAQEESA RTNAEKQVEE LLMAMEKVKQ ELESMKAKLS
     STQQSLAEKE THLTNLRAER RKHLEEVLEM KQEALLAAIS EKDANIALLE LSSSKKKTQE
     EVAALKREKD RLVQQLKQQT QNRMKLMADN YEDDHFRSSR SNQTNHKPSP DQIIQPLLEL
     DQNRSKLKLY IGHLTALCHD RDPLILRGLT PPASYNADGE QAAWENELQQ MTQEQLQNEL
     EKVEGDNAEL QEFANTILQQ IADHCPDILE QVVNALEESS
//
ID   ARBK1_MOUSE             Reviewed;         689 AA.
AC   Q99MK8; Q99LL8;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Beta-adrenergic receptor kinase 1;
DE            Short=Beta-ARK-1;
DE            EC=2.7.11.15;
DE   AltName: Full=G-protein-coupled receptor kinase 2;
GN   Name=Adrbk1; Synonyms=Grk2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lymphoma;
RX   PubMed=8638670;
RA   Hughes R.J., Anderson K.L., Kiel D., Insel P.A.;
RT   "Cloning of GRK2 cDNA from S49 murine lymphoma cells.";
RL   Am. J. Physiol. 270:C885-C891(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-689.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Specifically phosphorylates the agonist-occupied form of
CC       the beta-adrenergic and closely related receptors, probably
CC       inducing a desensitization of them.
CC   -!- CATALYTIC ACTIVITY: ATP + [beta-adrenergic receptor] = ADP +
CC       [beta-adrenergic receptor] phosphate.
CC   -!- SUBUNIT: Interacts with GIT1. Interacts with, and phosphorylates
CC       chemokine-stimulated CCR5. Interacts with ARRB1 (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. GPRK subfamily.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 RGS domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF333028; AAK21896.1; -; mRNA.
DR   EMBL; BC003196; AAH03196.1; -; mRNA.
DR   IPI; IPI00320687; -.
DR   UniGene; Mm.254144; -.
DR   ProteinModelPortal; Q99MK8; -.
DR   SMR; Q99MK8; 28-670.
DR   DIP; DIP-32413N; -.
DR   STRING; Q99MK8; -.
DR   PhosphoSite; Q99MK8; -.
DR   PRIDE; Q99MK8; -.
DR   Ensembl; ENSMUST00000088737; ENSMUSP00000086114; ENSMUSG00000024858.
DR   MGI; MGI:87940; Adrbk1.
DR   GeneTree; ENSGT00550000074318; -.
DR   HOGENOM; HBG443643; -.
DR   HOVERGEN; HBG050559; -.
DR   InParanoid; Q99MK8; -.
DR   OMA; IQRGSAN; -.
DR   OrthoDB; EOG4W3SMD; -.
DR   BRENDA; 2.7.11.15; 244.
DR   ArrayExpress; Q99MK8; -.
DR   Bgee; Q99MK8; -.
DR   CleanEx; MM_ADRBK1; -.
DR   Genevestigator; Q99MK8; -.
DR   GermOnline; ENSMUSG00000024858; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047696; F:beta-adrenergic receptor kinase activity; IEA:EC.
DR   GO; GO:0004703; F:G-protein coupled receptor kinase activity; IDA:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0002029; P:desensitization of G-protein coupled receptor protein signaling pathway; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:MGI.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR000239; GPCR_kinase.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR000342; Regulat_G_prot_signal.
DR   InterPro; IPR016137; Regulat_G_prot_signal_superfam.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR00717; GPCRKINASE.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00315; RGS; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF48097; Regulat_G_prot_signal_superfam; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    689       Beta-adrenergic receptor kinase 1.
FT                                /FTId=PRO_0000085629.
FT   DOMAIN       54    175       RGS.
FT   DOMAIN      191    453       Protein kinase.
FT   DOMAIN      454    521       AGC-kinase C-terminal.
FT   DOMAIN      558    652       PH.
FT   NP_BIND     197    205       ATP (By similarity).
FT   REGION        2    190       N-terminal.
FT   ACT_SITE    317    317       Proton acceptor (By similarity).
FT   BINDING     220    220       ATP (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     350    350       Phosphoserine (By similarity).
FT   MOD_RES     353    353       Phosphothreonine (By similarity).
FT   MOD_RES     670    670       Phosphoserine (By similarity).
FT   CONFLICT    160    160       D -> N (in Ref. 1; AAK21896).
FT   CONFLICT    374    374       W -> C (in Ref. 1; AAK21896).
FT   CONFLICT    520    520       E -> V (in Ref. 1; AAK21896).
FT   CONFLICT    600    600       L -> F (in Ref. 1; AAK21896).
FT   CONFLICT    679    679       P -> R (in Ref. 1; AAK21896).
SQ   SEQUENCE   689 AA;  79639 MW;  508F32B287DD99C6 CRC64;
     MADLEAVLAD VSYLMAMEKS KATPAARASK KILLPEPSIR SVMQKYLEDR GEVTFEKIFS
     QKLGYLLFRD FCLNHLEEAK PLVEFYEEIK KYEKLETEEE RVVRSREIFD SYIMKELLAC
     SHPFSKNATE HVQGHLVKKQ VPPDLFQPYI EEICQNLRGD VFQKFIESDK FTRFCQWKNV
     ELNIHLTMND FSVHRIIGRG GFGEVYGCRK ADTGKMYAMK CLDKKRIKMK QGETLALNER
     IMLSLVSTGD CPFIVCMSYA FHTPDKLSFI LDLMNGGDLH YHLSQHGVFS EADMRFYAAE
     IILGLEHMHN RFVVYRDLKP ANILLDEHGH VRISDLGLAC DFSKKRPHAS VGTHGYMAPE
     VLQKGVAYDS SADWFSLGCM LFKLLRGHSP FRQHKTKDKH EIDRMTLTMA VELPDSFSPE
     LRSLLEGLLQ RDVNRRLGCL GRGAQEVKES PFFRSLDWQM VFLQKYPPPL IPPRGEVNAA
     DAFDIGSFDE EDTKGIKLLD SDQELYRNFP LTISERWQQE VAETVFDTIN AETDRLEARK
     KAKNKQLGHE EDYALGKDCI VHGYMSKMGN PFLTQWQRRY FYLFPNRLEW RGEGEAPQSL
     LTMEEIQSVE ETQIKERKCL LLKIRGGKQF VLQCDSDPEL VQWKKELRDA YREAQQLVQR
     VPKMKNKPRS PVVELSKVPL IQRGSANGL
//
ID   SYK_MOUSE               Reviewed;         595 AA.
AC   Q99MN1;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Lysyl-tRNA synthetase;
DE            EC=6.1.1.6;
DE   AltName: Full=Lysine--tRNA ligase;
DE            Short=LysRS;
GN   Name=Kars;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   MEDLINE=21231131; PubMed=11331948; DOI=10.1007/s003350020008;
RA   Maas S., Kim Y.G., Rich A.;
RT   "Genomic clustering of tRNA-specific adenosine deaminase ADAT1 and two
RT   tRNA synthetases.";
RL   Mamm. Genome 12:387-393(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   BIDIRECTIONAL PROMOTER WITH TERF2IP.
RX   PubMed=14659874; DOI=10.1016/j.gene.2003.08.026;
RA   Tan M., Wei C., Price C.M.;
RT   "The telomeric protein Rap1 is conserved in vertebrates and is
RT   expressed from a bidirectional promoter positioned between the Rap1
RT   and KARS genes.";
RL   Gene 323:1-10(2003).
RN   [4]
RP   INTERACTION WITH MIFT.
RX   PubMed=14975237; DOI=10.1016/S1074-7613(04)00020-2;
RA   Lee Y.N., Nechushtan H., Figov N., Razin E.;
RT   "The function of lysyl-tRNA synthetase and Ap4A as signaling
RT   regulators of MITF activity in FcepsilonRI-activated mast cells.";
RL   Immunity 20:145-151(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: Catalyzes the specific attachment of an amino acid to
CC       its cognate tRNA in a 2 step reaction: the amino acid (AA) is
CC       first activated by ATP to form AA-AMP and then transferred to the
CC       acceptor end of the tRNA.
CC   -!- CATALYTIC ACTIVITY: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate
CC       + L-lysyl-tRNA(Lys).
CC   -!- SUBUNIT: Homodimer (By similarity); also part of a multisubunit
CC       complex that groups AIMP1, AIMP2, EEF1A1 and tRNA ligases for Arg,
CC       Asp, Glu, Gln, Ile, Leu, Lys, Met and Pro. Interacts with AIMP2
CC       (via N-terminus) and MITF.
CC   -!- INTERACTION:
CC       P25118:Tnfrsf1a; NbExp=1; IntAct=EBI-960115, EBI-518014;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: The N-terminal domain (1-65) is a functional tRNA-binding
CC       domain and is involved in the interaction with DARS, but has a
CC       repulsive role in the binding to EEF1A1. A central domain (208-
CC       259) is involved in homodimerization. The C-terminal domain (452-
CC       597) is not required for interaction with AIMP2 (By similarity).
CC   -!- MISCELLANEOUS: It is likely that the same gene provides both this
CC       cytoplasmic isoform and an additional mitochondrial isoform.
CC   -!- MISCELLANEOUS: Shares a bidirectional promoter with Terf2ip/Rap1
CC       (PubMed:14659874).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF328904; AAK19309.1; -; Genomic_DNA.
DR   EMBL; AF328894; AAK19309.1; JOINED; Genomic_DNA.
DR   EMBL; AF328895; AAK19309.1; JOINED; Genomic_DNA.
DR   EMBL; AF328896; AAK19309.1; JOINED; Genomic_DNA.
DR   EMBL; AF328897; AAK19309.1; JOINED; Genomic_DNA.
DR   EMBL; AF328898; AAK19309.1; JOINED; Genomic_DNA.
DR   EMBL; AF328899; AAK19309.1; JOINED; Genomic_DNA.
DR   EMBL; AF328900; AAK19309.1; JOINED; Genomic_DNA.
DR   EMBL; AF328901; AAK19309.1; JOINED; Genomic_DNA.
DR   EMBL; AF328902; AAK19309.1; JOINED; Genomic_DNA.
DR   EMBL; AF328903; AAK19309.1; JOINED; Genomic_DNA.
DR   EMBL; BC036289; AAH36289.1; -; mRNA.
DR   IPI; IPI00620145; -.
DR   RefSeq; NP_444322.1; NM_053092.2.
DR   UniGene; Mm.196544; -.
DR   UniGene; Mm.410491; -.
DR   ProteinModelPortal; Q99MN1; -.
DR   SMR; Q99MN1; 70-572.
DR   IntAct; Q99MN1; 1.
DR   STRING; Q99MN1; -.
DR   PhosphoSite; Q99MN1; -.
DR   PRIDE; Q99MN1; -.
DR   Ensembl; ENSMUST00000034426; ENSMUSP00000034426; ENSMUSG00000031948.
DR   GeneID; 85305; -.
DR   KEGG; mmu:85305; -.
DR   UCSC; uc009nne.1; mouse.
DR   CTD; 85305; -.
DR   MGI; MGI:1934754; Kars.
DR   GeneTree; ENSGT00550000074841; -.
DR   HOVERGEN; HBG002562; -.
DR   OrthoDB; EOG4KSPJH; -.
DR   PhylomeDB; Q99MN1; -.
DR   BRENDA; 6.1.1.6; 244.
DR   NextBio; 351352; -.
DR   ArrayExpress; Q99MN1; -.
DR   Bgee; Q99MN1; -.
DR   CleanEx; MM_KARS; -.
DR   Genevestigator; Q99MN1; -.
DR   GermOnline; ENSMUSG00000031948; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:InterPro.
DR   InterPro; IPR004364; Aminoacyl-tRNA-synt_II.
DR   InterPro; IPR018150; Aminoacyl-tRNA-synt_II-like.
DR   InterPro; IPR006195; Aminoacyl-tRNA-synth_II.
DR   InterPro; IPR002313; Lys-tRNA-synth_II.
DR   InterPro; IPR018149; Lys-tRNA-synth_II_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR016027; NA-bd_OB-fold-like.
DR   InterPro; IPR004365; NA-bd_OB_tRNA-helicase.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   PANTHER; PTHR22594; aa-tRNA-synt_II; 1.
DR   PANTHER; PTHR22594:SF4; tRNA-synt_lys_2; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti; 1.
DR   PRINTS; PR00982; TRNASYNTHLYS.
DR   SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR   TIGRFAMs; TIGR00499; lysS_bact; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Protein biosynthesis.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    595       Lysyl-tRNA synthetase.
FT                                /FTId=PRO_0000152766.
FT   NP_BIND     321    323       ATP (By similarity).
FT   NP_BIND     329    330       ATP (By similarity).
FT   NP_BIND     492    493       ATP (By similarity).
FT   NP_BIND     548    551       ATP (By similarity).
FT   METAL       485    485       Calcium (By similarity).
FT   METAL       492    492       Calcium (By similarity).
FT   BINDING     275    275       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     299    299       Substrate (By similarity).
FT   BINDING     337    337       Substrate (By similarity).
FT   BINDING     339    339       Substrate (By similarity).
FT   BINDING     495    495       Substrate (By similarity).
FT   BINDING     499    499       Substrate (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      86     86       N6-acetyllysine (By similarity).
FT   MOD_RES     139    139       N6-acetyllysine (By similarity).
FT   MOD_RES     400    400       N6-acetyllysine (By similarity).
FT   MOD_RES     585    585       Phosphothreonine (By similarity).
FT   MOD_RES     594    594       Phosphoserine.
SQ   SEQUENCE   595 AA;  67840 MW;  055889E87C11AA97 CRC64;
     MATLQESEVK VDGEQKLSKN ELKRRLKAEK KLAEKEAKQK ELSEKQLNQT ASAPNHTADN
     GVGAEEETLD PNQYYKIRSQ AVQQLKVTGE DPYPHKFHVD ISLTQFIQEY SHLQPGDHLT
     DVTLKVAGRI HAKRASGGKL IFYDLRGEGV KLQVMANSRN YKSEEEFVHI NNKLRRGDII
     GVEGNPGKTK KGELSIIPQE ITLLSPCLHM LPHLHFGLKD KETRYRQRYL DLILNDFVRQ
     KFIVRSKIIT YIRSFLDELG FLEIETPMMN IIPGGAVAKP FITYHNELDM NLYMRIAPEL
     YHKMLVVGGI DRVYEIGRQF RNEGIDLTHN PEFTTCEFYM AYADYHDLME ITEKMLSGMV
     KSITGSYKIT YHPDGPEGQA YEVDFTPPFR RISMVEELEK ALGVKLPETS LFETEETRKI
     LDDICVAKAV ECPPPRTTAR LLDKLVGEFL EVTCISPTFI CDHPQIMSPL AKWHRSKEGL
     TERFELFVMK KEICNAYTEL NDPVRQRQLF EEQAKAKAAG DDEAMFIDEN FCTALEYGLP
     PTAGWGMGID RLTMFLTDSN NIKEVLLFPA MKPEDKKETA ATTETPESTE ASPSV
//
ID   BRAP_MOUSE              Reviewed;         591 AA.
AC   Q99MP8; Q8CC00; Q8CHX1; Q99MP7; Q9CXX8;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=BRCA1-associated protein;
DE            EC=6.3.2.-;
DE   AltName: Full=BRAP2;
DE   AltName: Full=Impedes mitogenic signal propagation;
DE            Short=IMP;
GN   Name=Brap;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC   STRAIN=ICR; TISSUE=Testis;
RX   PubMed=14607334; DOI=10.1016/S0304-3835(03)00443-9;
RA   Nakajima A., Kataoka K., Hong M., Sakaguchi M., Huh N.-H.;
RT   "BRPK, a novel protein kinase showing increased expression in mouse
RT   cancer cell lines with higher metastatic potential.";
RL   Cancer Lett. 201:195-201(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 102-591 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Negatively regulates MAP kinase activation by limiting
CC       the formation of Raf/MEK complexes probably by inactivation of the
CC       KSR1 scaffold protein. Also acts as a Ras responsive E3 ubiquitin
CC       ligase that, on activation of Ras, is modified by auto-
CC       polyubiquitination resulting in the release of inhibition of
CC       Raf/MEK complex formation. May also act as a cytoplasmic retention
CC       protein with a role in regulating nuclear transport (By
CC       similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with the nuclear localization signal of BRCA1
CC       and with the N-terminal of KSR1. The C-terminal portion of BRCA1
CC       interacts with DDB1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=alpha;
CC         IsoId=Q99MP8-1; Sequence=Displayed;
CC       Name=2; Synonyms=beta;
CC         IsoId=Q99MP8-2; Sequence=VSP_050761;
CC       Name=3;
CC         IsoId=Q99MP8-3; Sequence=VSP_050762;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Isoform 2 is highly expressed in testis, lower
CC       levels in brain, heart, lung, stomach, colon, uterus, liver and
CC       kidney. Isoform 1 is only expressed in the testis. Isoform 2 is
CC       predominant over isoform 1 in both fetal and adult testis.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SIMILARITY: Contains 1 UBP-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB29036.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF321920; AAK28079.1; -; mRNA.
DR   EMBL; AF321921; AAK28080.1; -; mRNA.
DR   EMBL; BC038490; AAH38490.1; -; mRNA.
DR   EMBL; AK013885; BAB29036.1; ALT_INIT; mRNA.
DR   EMBL; AK034212; BAC28633.1; -; mRNA.
DR   IPI; IPI00117933; -.
DR   IPI; IPI00453542; -.
DR   IPI; IPI00453543; -.
DR   RefSeq; NP_082503.2; NM_028227.2.
DR   UniGene; Mm.153372; -.
DR   ProteinModelPortal; Q99MP8; -.
DR   SMR; Q99MP8; 255-374.
DR   STRING; Q99MP8; -.
DR   PhosphoSite; Q99MP8; -.
DR   PRIDE; Q99MP8; -.
DR   Ensembl; ENSMUST00000031414; ENSMUSP00000031414; ENSMUSG00000029458.
DR   GeneID; 72399; -.
DR   KEGG; mmu:72399; -.
DR   UCSC; uc008zkc.1; mouse.
DR   CTD; 72399; -.
DR   MGI; MGI:1919649; Brap.
DR   eggNOG; roNOG10534; -.
DR   GeneTree; ENSGT00500000044909; -.
DR   HOGENOM; HBG604662; -.
DR   HOVERGEN; HBG050729; -.
DR   InParanoid; Q99MP8; -.
DR   OMA; LTILCNH; -.
DR   OrthoDB; EOG4HHP1Z; -.
DR   PhylomeDB; Q99MP8; -.
DR   NextBio; 336190; -.
DR   ArrayExpress; Q99MP8; -.
DR   Bgee; Q99MP8; -.
DR   CleanEx; MM_BRAP; -.
DR   Genevestigator; Q99MP8; -.
DR   GermOnline; ENSMUSG00000029458; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR011422; BRAP2.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 2.
DR   Pfam; PF07576; BRAP2; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   Pfam; PF02148; zf-UBP; 1.
DR   ProDom; PD017029; BRAP2; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Ligase; Metal-binding;
KW   Phosphoprotein; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    591       BRCA1-associated protein.
FT                                /FTId=PRO_0000055826.
FT   ZN_FING     263    303       RING-type.
FT   ZN_FING     314    375       UBP-type.
FT   COILED      430    536       Potential.
FT   MOD_RES      52     52       Phosphoserine (By similarity).
FT   MOD_RES     116    116       Phosphoserine.
FT   MOD_RES     118    118       Phosphoserine (By similarity).
FT   VAR_SEQ       1    217       Missing (in isoform 3).
FT                                /FTId=VSP_050762.
FT   VAR_SEQ       1     30       Missing (in isoform 2).
FT                                /FTId=VSP_050761.
FT   CONFLICT    111    111       N -> I (in Ref. 3).
SQ   SEQUENCE   591 AA;  66991 MW;  DF925A28C0388E72 CRC64;
     MSVSLVVIRL ELAGHSPVPT DFGFSAAAGE MSDEEIKKKT LASAVACLEG KSAGEKAAII
     HQHLGRREMT DVIIETMKAR ADEVRDTVEE KKPSAAPVSA QRSREQSESV NTAPESPSKQ
     LPDQISFFSG NPSVEIVHGI MHLYKTNKMT SLKEDVRRSA MLCVLTVPAT MTSHDLMKFV
     APFNDVIEQM KIIRDSTPNQ YMVLIKFSAQ ADADSFYMAC NGRQFNSIED DVCQLVYVER
     AEVLKSEDGA SLPVMDLTEL PKCTVCLERM DESVNGILTT LCNHSFHSQC LQRWDDTTCP
     VCRYCQTPEP VEENKCFECG VQENLWICLI CGHIGCGRYV SRHAYKHFEE TQHTYAMQLT
     NHRVWDYAGD NYVHRLVASK TDGKIVQYEC EGDTCQEEKI DALQLEYSYL LTSQLESQRI
     YWENKIVRIE KDTAEEINNM KTKFKETIEK CDSLELRLSD LLKEKQSVER KCTQLNTRVA
     KLSTELQEEQ ELNKCLRANQ LVLQNQLKEE EKLLKETCAQ KDLQITEIQE QLRDVMFYLE
     TQQQISHLPA ETRQEIQEGQ INIAMASAPN PPSSGAGGKL QSRKGRSKRG K
//
ID   PERQ1_MOUSE             Reviewed;        1044 AA.
AC   Q99MR1; Q571A0; Q6Y7W9;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=PERQ amino acid-rich with GYF domain-containing protein 1;
DE   AltName: Full=GRB10-interacting GYF protein 1;
GN   Name=Gigyf1; Synonyms=Kiaa4110, Perq1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=21138439; PubMed=11239002; DOI=10.1093/nar/29.6.1352;
RA   Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P.,
RA   Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C.,
RA   Miller W., Koop B.F.;
RT   "Comparative analysis of the gene-dense ACHE/TFR2 region on human
RT   chromosome 7q22 with the orthologous region on mouse chromosome 5.";
RL   Nucleic Acids Res. 29:1352-1365(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSSUE SPECIFICITY, INTERACTION WITH
RP   GRB10, MUTAGENESIS OF TRP-500; GLY-504; TYR-505 AND PHE-506, AND
RP   FUNCTION.
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   MEDLINE=22803289; PubMed=12771153; DOI=10.1074/jbc.M211572200;
RA   Giovannone B., Lee E., Laviola L., Giorgino F., Cleveland K.A.,
RA   Smith R.J.;
RT   "Two novel proteins that are linked to insulin-like growth factor
RT   (IGF-I) receptors by the Grb10 adapter and modulate IGF-I signaling.";
RL   J. Biol. Chem. 278:31564-31573(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 308-1041.
RC   TISSUE=Pancreatic islet;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May act cooperatively with GRB10 to regulate tyrosine
CC       kinase receptor signaling. May increase IGF1 receptor
CC       phosphorylation under IGF1 stimulation as well as phosphorylation
CC       of IRS1 and SHC1.
CC   -!- SUBUNIT: Interacts with GRB10. This transient binding is increased
CC       under IGF1 stimulation and leads to recruitment of GIGYF1/GRB10
CC       complex to IGF1 receptor.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Lower expression in skeletal
CC       muscle, liver and testis.
CC   -!- SIMILARITY: Belongs to the PERQ family.
CC   -!- SIMILARITY: Contains 1 GYF domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK28827.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF312033; AAK28827.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AY176042; AAO46886.1; -; mRNA.
DR   EMBL; AK220289; BAD90214.1; -; mRNA.
DR   IPI; IPI00117983; -.
DR   RefSeq; NP_113596.2; NM_031408.2.
DR   UniGene; Mm.268344; -.
DR   ProteinModelPortal; Q99MR1; -.
DR   SMR; Q99MR1; 476-544.
DR   MINT; MINT-266563; -.
DR   STRING; Q99MR1; -.
DR   PhosphoSite; Q99MR1; -.
DR   PRIDE; Q99MR1; -.
DR   Ensembl; ENSMUST00000031727; ENSMUSP00000031727; ENSMUSG00000029714.
DR   GeneID; 57330; -.
DR   KEGG; mmu:57330; -.
DR   UCSC; uc009acq.1; mouse.
DR   CTD; 57330; -.
DR   MGI; MGI:1888677; Gigyf1.
DR   eggNOG; roNOG14993; -.
DR   GeneTree; ENSGT00410000025767; -.
DR   HOGENOM; HBG443544; -.
DR   HOVERGEN; HBG082121; -.
DR   InParanoid; Q99MR1; -.
DR   OMA; LQLQHKF; -.
DR   OrthoDB; EOG4CJVGP; -.
DR   PhylomeDB; Q99MR1; -.
DR   NextBio; 313694; -.
DR   ArrayExpress; Q99MR1; -.
DR   Bgee; Q99MR1; -.
DR   CleanEx; MM_GIGYF1; -.
DR   Genevestigator; Q99MR1; -.
DR   GermOnline; ENSMUSG00000029714; Mus musculus.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IPI:MGI.
DR   InterPro; IPR003169; GYF.
DR   Pfam; PF02213; GYF; 1.
DR   SMART; SM00444; GYF; 1.
DR   SUPFAM; SSF55277; GYF; 1.
DR   PROSITE; PS50829; GYF; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1   1044       PERQ amino acid-rich with GYF domain-
FT                                containing protein 1.
FT                                /FTId=PRO_0000058315.
FT   DOMAIN      476    524       GYF.
FT   COMPBIAS    333    341       Poly-Glu.
FT   COMPBIAS    550    744       Gln-rich.
FT   COMPBIAS    601    604       Poly-Gln.
FT   COMPBIAS    694    697       Poly-Glu.
FT   COMPBIAS    707    712       Poly-Gln.
FT   COMPBIAS    720    723       Poly-Glu.
FT   COMPBIAS    741    744       Poly-Gln.
FT   COMPBIAS    884    887       Poly-Glu.
FT   COMPBIAS    970    984       Poly-Gln.
FT   MOD_RES     634    634       Phosphoserine (By similarity).
FT   MUTAGEN     500    500       W->A: Decreases binding to GRB10.
FT   MUTAGEN     504    504       G->A: Decreases binding to GRB10.
FT   MUTAGEN     505    505       Y->A: Decreases binding to GRB10.
FT   MUTAGEN     506    506       F->A: Abolishes binding to GRB10.
FT   CONFLICT     58     58       Missing (in Ref. 2; AAO46886).
FT   CONFLICT    275    275       R -> K (in Ref. 2; AAO46886).
FT   CONFLICT    343    343       S -> A (in Ref. 2; AAO46886).
FT   CONFLICT    404    404       G -> A (in Ref. 2; AAO46886).
FT   CONFLICT    895    895       G -> S (in Ref. 1; AAK28827).
FT   CONFLICT    973    975       Missing (in Ref. 1; AAK28827).
SQ   SEQUENCE   1044 AA;  116238 MW;  3EE2247C7C760065 CRC64;
     MAAETLNFGP EWLRALSSGG SVASPPPSPA MPKYKLADYR YGREEMLALY VKENKVPEEL
     QDKEFAAVLQ EEPLQPLALE PLTEEEQRNF SLSVNSVAVL RLMGKGAGPP LPATSRGRGS
     TRSRGRGRGD SCFYQRSIEE GDGAFGRNPR EIQRSQSWDD RGERRFEKPA RRDGVRSGFE
     EGGAGPRKEH ARSDSENWRS LREEQEDDGS WRLGAGPRRD GDRWRSTSPD GGPRSAGWRE
     HGERRRKFDF DLRGERGGCG EEDGRVGGGN SHLRRCRGLD GFEDDKDGLP EWCLEDEDEE
     MGTFDASGAF LPLKKGPKEA IPEEQELDFR GLEEEEEEEE EPSEGVDEER PEAGGKEATP
     LPPPENSSSP SSLPALGPLW TTNEEGGEAV EKELPPAEGD ELRGLSLSPR ISSPPGPPGD
     LEDEEGLKHL QQEAEKLVAS LQDSSLEEEQ FTAAMQTQGL RHSTAATALP LSHGAARKWF
     YKDPQGEIQG PFTTQEMAEW FQAGYFSMSL LVKRGCDEGF QPLGEVIKMW GRVPFAPGPS
     PPPLLGNMDQ ERLKKQQELA AAALYQQLQH QHFLQLVGSR QLPQCTTLRE KAAMGDLTPP
     QQQQLTTFLQ QLQALKTPRG GDQNLLPTMS RSLSVPDSGP LWDLHTSASS QSGGEASLWD
     IPINSSTQGP ILEQLQLQHK FQERREVELR AKREEEERKR REEKRRQQQQ QQEEQKRRQE
     EEELFRRKQV RQQELLLKLL QQQQATNVPV PPAPSSPPPL WAGLAKQGLS MKTLLELQME
     SERQLHKQAA PREPLRAQAP NHRVQLGGLG SAPLNQWVSE AGPLWGGPDK SGGSSGGNLG
     LWEDTLKSGG SLARSLGLKS SRSSPSLSDS YSHLSGRPVR KKTEEEEKLL KLLQGIPRPQ
     DGFTQWCEQM LHTLSTAGSL DVPMAVAILK EVESPYDVHD YIRSCLGDTL EAKEFAKQFL
     ERRAKQKASQ QRQQQQQQQQ QQQQEAWLSS TSLQTAFQAN HSTKLGPGEG SKAKRRALML
     HSDPSILGYS LHGPSGEIES VDDY
//
ID   S12A9_MOUSE             Reviewed;         914 AA.
AC   Q99MR3;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Solute carrier family 12 member 9;
DE   AltName: Full=Cation-chloride cotransporter-interacting protein 1;
DE   AltName: Full=Potassium-chloride transporter 9;
GN   Name=Slc12a9; Synonyms=Cip1, Slc12a8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=21138439; PubMed=11239002; DOI=10.1093/nar/29.6.1352;
RA   Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P.,
RA   Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C.,
RA   Miller W., Koop B.F.;
RT   "Comparative analysis of the gene-dense ACHE/TFR2 region on human
RT   chromosome 7q22 with the orthologous region on mouse chromosome 5.";
RL   Nucleic Acids Res. 29:1352-1365(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=FVB/N;
RA   Mount D.B.;
RT   "Cloning of mouse Slc12a8, a new member of the cation-chloride
RT   cotransporter gene family.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-218; ASN-228 AND ASN-243,
RP   AND MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: May be an inhibitor of SLC12A1. Seems to correspond to a
CC       subunit of a multimeric transport system and thus, additional
CC       subunits may be required for its function (By similarity).
CC   -!- SUBUNIT: Interacts with SLC12A1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the SLC12A transporter family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF312033; AAK28822.1; -; Genomic_DNA.
DR   EMBL; AF314957; AAL26866.1; -; mRNA.
DR   EMBL; BC046982; AAH46982.1; -; mRNA.
DR   IPI; IPI00117986; -.
DR   UniGene; Mm.235625; -.
DR   ProteinModelPortal; Q99MR3; -.
DR   PRIDE; Q99MR3; -.
DR   Ensembl; ENSMUST00000039991; ENSMUSP00000038106; ENSMUSG00000037344.
DR   UCSC; uc009ace.1; mouse.
DR   MGI; MGI:1933532; Slc12a9.
DR   eggNOG; roNOG06037; -.
DR   GeneTree; ENSGT00560000076892; -.
DR   HOGENOM; HBG403147; -.
DR   HOVERGEN; HBG106223; -.
DR   InParanoid; Q99MR3; -.
DR   OrthoDB; EOG4B2SWJ; -.
DR   PhylomeDB; Q99MR3; -.
DR   NextBio; 350746; -.
DR   ArrayExpress; Q99MR3; -.
DR   Bgee; Q99MR3; -.
DR   Genevestigator; Q99MR3; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR004841; AA-permease_dom.
DR   Pfam; PF00324; AA_permease; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Membrane; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    914       Solute carrier family 12 member 9.
FT                                /FTId=PRO_0000331416.
FT   TOPO_DOM      1     36       Cytoplasmic (Potential).
FT   TRANSMEM     37     57       Helical; (Potential).
FT   TOPO_DOM     58     72       Extracellular (Potential).
FT   TRANSMEM     73     93       Helical; (Potential).
FT   TOPO_DOM     94    119       Cytoplasmic (Potential).
FT   TRANSMEM    120    140       Helical; (Potential).
FT   TOPO_DOM    141    167       Extracellular (Potential).
FT   TRANSMEM    168    188       Helical; (Potential).
FT   TOPO_DOM    189    193       Cytoplasmic (Potential).
FT   TRANSMEM    194    214       Helical; (Potential).
FT   TOPO_DOM    215    262       Extracellular (Potential).
FT   TRANSMEM    263    283       Helical; (Potential).
FT   TOPO_DOM    284    297       Cytoplasmic (Potential).
FT   TRANSMEM    298    318       Helical; (Potential).
FT   TOPO_DOM    319    338       Extracellular (Potential).
FT   TRANSMEM    339    359       Helical; (Potential).
FT   TOPO_DOM    360    376       Cytoplasmic (Potential).
FT   TRANSMEM    377    399       Helical; (Potential).
FT   TOPO_DOM    400    416       Extracellular (Potential).
FT   TRANSMEM    417    437       Helical; (Potential).
FT   TOPO_DOM    438    466       Cytoplasmic (Potential).
FT   TRANSMEM    467    487       Helical; (Potential).
FT   TOPO_DOM    488    740       Extracellular (Potential).
FT   TRANSMEM    741    761       Helical; (Potential).
FT   TOPO_DOM    762    914       Cytoplasmic (Potential).
FT   COMPBIAS    715    718       Poly-Ser.
FT   COMPBIAS    811    816       Poly-Glu.
FT   CARBOHYD    218    218       N-linked (GlcNAc...).
FT   CARBOHYD    228    228       N-linked (GlcNAc...).
FT   CARBOHYD    243    243       N-linked (GlcNAc...).
SQ   SEQUENCE   914 AA;  96314 MW;  AF766F0A788CBEA3 CRC64;
     MASESSPLLA YRLLGEEGAA FPPNGAGVSG VPSARKLSTF LGVVVPTVLS MFSIVVFLRI
     GFVVGHAGLL QALAMLLVAY IILALTVLSV CAIATNGAVR GGGAYFMISR TLGPEVGGSI
     GLMFYLANVC GCAVSLLGLV ESILDVFGAD ATGSSGIQVL PQGYGWNLLY GSLLLGLVGG
     VCTLGAGLYA RASFLTFLLV SGSLASVLVS FVAVGPRNIP LAPRPGTNAS SVPHRHGHFT
     GFNGSTLRDN LGAGYAEDYT TGAMMTFASV FAVLFNGCTG IMAGANMSGE LKDPSRAIPL
     GTIIAVAYTF FIYILLFFLS SFTCDRALLQ EDYGFFRDIS LWPPLVLIGI YATALSASMS
     SLIGASRILH ALAQDDLFGV ILAPAKVVSG GGNPWGAVLY SWGLVQLVLL AGKLNTLAAV
     VTVFYLVAYA AVDLSCLSLE WASAPNFRPT FSLFSWHTCL LGVASCLLMM FLISPGAAGG
     SLLLMGLLSA LLTARGGPSS WGYVSQALLF HQVRKYLLRL DVRKEHVKFW RPQLLLLVGN
     PRGALPLLRL ANQLKKGGLY VLGHVTLGDL DSLPSDPVQP QYGAWLSLVD LAQVKAFVDL
     TLSPSVRQGA QHLLRISGLG GMKPNTLVLG FYDDAPPQDH FLTDPAFSEP AEGTREGGSP
     ALSTLFPPPR APGSPRALSP QDYVATVADA LKMNKNVVLA RACGALPPER LSRGSSSSAQ
     LHHVDVWPLN LLRPRGGPGY VDVCGLFLLQ MATILSMVPA WHSARLRIFL CLGPREAPGA
     AEGRLRALLS QLRIRAEVQE VVWGEGAETG EPEEEEGDFV NGGRGDEEAE ALACSANALV
     RAQQGRGTVG GPGGPEGRDG EEGPTTALTF LYLPRPPADP ARYPRYLALL ETLSRDLGPT
     LLIHGVTPVT CTDL
//
ID   SRRT_MOUSE              Reviewed;         875 AA.
AC   Q99MR6; Q3UD04; Q5D042; Q8VEE6; Q99MR4; Q99MR5; Q99MR7;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Serrate RNA effector molecule homolog;
DE   AltName: Full=Arsenite-resistance protein 2;
GN   Name=Srrt; Synonyms=Ars2, Asr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS
RP   A; B; C AND D).
RC   STRAIN=129/Sv;
RX   MEDLINE=21138439; PubMed=11239002; DOI=10.1093/nar/29.6.1352;
RA   Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P.,
RA   Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C.,
RA   Miller W., Koop B.F.;
RT   "Comparative analysis of the gene-dense ACHE/TFR2 region on human
RT   chromosome 7q22 with the orthologous region on mouse chromosome 5.";
RL   Nucleic Acids Res. 29:1352-1365(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 477-875 (ISOFORM C).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=18086880; DOI=10.1128/MCB.01565-07;
RA   Wilson M.D., Wang D., Wagner R., Breyssens H., Gertsenstein M.,
RA   Lobe C., Lu X., Nagy A., Burke R.D., Koop B.F., Howard P.L.;
RT   "ARS2 is a conserved eukaryotic gene essential for early mammalian
RT   development.";
RL   Mol. Cell. Biol. 28:1503-1514(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-543, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION,
RP   INTERACTION WITH NCBP1 AND DROSHA, AND DISRUPTION PHENOTYPE.
RX   PubMed=19632182; DOI=10.1016/j.cell.2009.04.046;
RA   Gruber J.J., Zatechka D.S., Sabin L.R., Yong J., Lum J.J., Kong M.,
RA   Zong W.-X., Zhang Z., Lau C.-K., Rawlings J., Cherry S., Ihle J.N.,
RA   Dreyfuss G., Thompson C.B.;
RT   "Ars2 links the nuclear cap-binding complex to RNA interference and
RT   cell proliferation.";
RL   Cell 138:328-339(2009).
CC   -!- FUNCTION: Acts as a mediator between the cap-binding complex (CBC)
CC       and the primary microRNAs (miRNAs) processing machinery during
CC       cell proliferation. Contributes to the stability and delivery of
CC       capped primary miRNA transcripts to the primary miRNA processing
CC       complex containing DGCR8 and DROSHA, thereby playing a role in
CC       RNA-mediated gene silencing (RNAi) by miRNAs. Binds capped RNAs
CC       (m7GpppG-capped RNA); however interaction is probably mediated via
CC       its interaction with NCBP1/CBP80 component of the CBC complex.
CC       Involved in cell cycle progression at S phase. Does not directly
CC       confer arsenite resistance but rather modulates arsenic
CC       sensitivity.
CC   -!- SUBUNIT: Interacts with CASP8AP2/FLASH, NCBP1/CBP80 and DROSHA.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Cytoplasm.
CC       Note=Predominantly nuclear. Shuttles between the nucleus and the
CC       cytoplasm in a CRM1-dependent way.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=A;
CC         IsoId=Q99MR6-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=Q99MR6-2; Sequence=VSP_000325;
CC       Name=C;
CC         IsoId=Q99MR6-3; Sequence=VSP_000325, VSP_000326;
CC       Name=D;
CC         IsoId=Q99MR6-4; Sequence=VSP_000326;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed, with a preference for
CC       proliferating cells. Highly expressed in hematopoietic tissues and
CC       reduced or absent expression in parenchymal organs like liver and
CC       kidney.
CC   -!- INDUCTION: Upon cell proliferation.
CC   -!- DISRUPTION PHENOTYPE: Death around the time of implantation.
CC       Deletion in adults leads to proliferative arrest and bone marrow
CC       hypoplasia whereas parenchymal organs composed of nonproliferating
CC       cells are unaffected.
CC   -!- SIMILARITY: Belongs to the ARS2 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH19117.1; Type=Erroneous initiation;
CC       Sequence=BAE29458.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF312033; AAK28817.1; -; Genomic_DNA.
DR   EMBL; AF312033; AAK28818.1; -; Genomic_DNA.
DR   EMBL; AF312033; AAK28819.1; -; Genomic_DNA.
DR   EMBL; AF312033; AAK28820.1; -; Genomic_DNA.
DR   EMBL; BC019117; AAH19117.1; ALT_INIT; mRNA.
DR   EMBL; BC066831; AAH66831.1; -; mRNA.
DR   EMBL; AK150310; BAE29458.1; ALT_INIT; mRNA.
DR   IPI; IPI00224644; -.
DR   IPI; IPI00224645; -.
DR   IPI; IPI00266463; -.
DR   IPI; IPI00761620; -.
DR   RefSeq; NP_001103379.1; NM_001109909.1.
DR   RefSeq; NP_001103380.1; NM_001109910.1.
DR   RefSeq; NP_113582.1; NM_031405.2.
DR   UniGene; Mm.387734; -.
DR   ProteinModelPortal; Q99MR6; -.
DR   STRING; Q99MR6; -.
DR   PhosphoSite; Q99MR6; -.
DR   PRIDE; Q99MR6; -.
DR   Ensembl; ENSMUST00000040873; ENSMUSP00000043123; ENSMUSG00000037364.
DR   GeneID; 83701; -.
DR   KEGG; mmu:83701; -.
DR   UCSC; uc009acb.1; mouse.
DR   UCSC; uc009acc.1; mouse.
DR   CTD; 83701; -.
DR   MGI; MGI:1933527; Srrt.
DR   GeneTree; ENSGT00390000005492; -.
DR   HOGENOM; HBG717208; -.
DR   InParanoid; Q99MR6; -.
DR   OMA; ICWNLNN; -.
DR   OrthoDB; EOG4N30NP; -.
DR   NextBio; 350735; -.
DR   ArrayExpress; Q99MR6; -.
DR   Bgee; Q99MR6; -.
DR   CleanEx; MM_ARS2; -.
DR   Genevestigator; Q99MR6; -.
DR   GermOnline; ENSMUSG00000037364; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0008283; P:cell proliferation; IMP:UniProtKB.
DR   GO; GO:0031053; P:primary microRNA processing; IMP:UniProtKB.
DR   InterPro; IPR007042; Arsenate-R_2.
DR   InterPro; IPR021933; DUF3546.
DR   Pfam; PF04959; ARS2; 1.
DR   Pfam; PF12066; DUF3546; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW   RNA-mediated gene silencing.
FT   CHAIN         1    875       Serrate RNA effector molecule homolog.
FT                                /FTId=PRO_0000220966.
FT   COMPBIAS     10     82       Arg-rich.
FT   COMPBIAS    258    401       Glu-rich.
FT   COMPBIAS    759    827       Pro-rich.
FT   MOD_RES       8      8       Phosphotyrosine (By similarity).
FT   MOD_RES      67     67       Phosphoserine (By similarity).
FT   MOD_RES      74     74       Phosphoserine.
FT   MOD_RES     136    136       Phosphoserine (By similarity).
FT   MOD_RES     492    492       Phosphoserine (By similarity).
FT   MOD_RES     539    539       Phosphoserine (By similarity).
FT   MOD_RES     543    543       Phosphothreonine.
FT   MOD_RES     623    623       Phosphotyrosine (By similarity).
FT   MOD_RES     624    624       Phosphotyrosine (By similarity).
FT   VAR_SEQ     775    779       ILPPG -> S (in isoform B and isoform C).
FT                                /FTId=VSP_000325.
FT   VAR_SEQ     809    815       Missing (in isoform C and isoform D).
FT                                /FTId=VSP_000326.
FT   CONFLICT    567    567       E -> G (in Ref. 3; BAE29458).
SQ   SEQUENCE   875 AA;  100452 MW;  9571445674452886 CRC64;
     MGDSDDEYDR RRRDKFRRER SDYDRSRERD ERRRGDDWND REWDRGRERR SRGEYRDYDR
     NRRERFSPPR HELSPPQKRM RRDWDEHSSD PYHSGYDMPY AGGGGGPTYG PPQPWGHPDV
     HIMQHHVLPI QARLGSIAEI DLGVPPPIMK SFKEFLLSLD DSVDETEAVK RYNDYKLDFR
     RQQMQDFFLA HKDEEWFRSK YHPDEVGKRR QEARGALQNR LKVFLSLMES GWFDNLLLDI
     DKADAIVKML DAAVIKMEGG TENDLRILEQ EEEEEQAGKT GEASKKEEAR AGPALGEGER
     KANDKDEKKE DGKQAENDSS NDDKTKKSEG DGDKEEKKEE AEKEAKKSKK RNRKQSGDDS
     FDEGSVSESE SESEGGQAEE EKEEAEEALK EKEKPKEEEK EKPKDAAGLE CKPRPLHKTC
     SLFMRNIAPN ISRAEIISLC KRYPGFMRVA LSEPQPERRF FRRGWVTFDR SVNIKEICWN
     LQNIRLRECE LSPGVNRDLT RRVRNINGIT QHKQIVRNDI KLAAKLIHTL DDRTQLWASE
     PGTPPVPTSL PSQNPILKNI TDYLIEEVSA EEEELLGSSG GPPPEEPPKE GNPAEINVER
     DEKLIKVLDK LLLYLRIVHS LDYYNTCEYP NEDEMPNRCG IIHVRGPMPP NRISHGEVLE
     WQKTFEEKLT PLLSVRESLS EEEAQKMGRK DPEQEVEKFV TSNTQELGKD KWLCPLSGKK
     FKGPEFVRKH IFNKHAEKIE EVKKEVAFFN NFLTDAKRPA LPEIKPAQPP GPAQILPPGL
     TPGLPYPHQT PQGLMPYGQP RPPILGYGAG AVRPAVPTGG PPYPHAPYGA GRGNYDAFRG
     QGGYPGKPRN RMVRGDPRAI VEYRDLDAPD DVDFF
//
ID   CECR6_MOUSE             Reviewed;         572 AA.
AC   Q99MX7;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   30-NOV-2010, entry version 45.
DE   RecName: Full=Cat eye syndrome critical region protein 6 homolog;
GN   Name=Cecr6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=21275466; PubMed=11381032; DOI=10.1101/gr.154901;
RA   Footz T.K., Brinkman-Mills P., Banting G.S., Maier S.A., Riazi M.A.,
RA   Bridgland L.J., Hu S., Birren B., Minoshima S., Shimizu N., Pan H.,
RA   Nguyen T., Fang F., Fu Y., Ray L., Wu H., Shaull S., Phan S., Yao Z.,
RA   Chen F., Huan A., Hu P., Wang Q., Loh P., Qi S., Roe B.A.,
RA   McDermid H.E.;
RT   "Analysis of the cat eye syndrome critical region in humans and the
RT   region of conserved synteny in mice: a search for candidate genes at
RT   or near the human chromosome 22 pericentromere.";
RL   Genome Res. 11:1053-1070(2001).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-529, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
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DR   EMBL; AF277399; AAK17095.1; -; mRNA.
DR   IPI; IPI00118167; -.
DR   RefSeq; NP_291045.1; NM_033567.1.
DR   UniGene; Mm.23088; -.
DR   PhosphoSite; Q99MX7; -.
DR   PRIDE; Q99MX7; -.
DR   GeneID; 94047; -.
DR   KEGG; mmu:94047; -.
DR   UCSC; uc009dnk.1; mouse.
DR   CTD; 94047; -.
DR   MGI; MGI:2136977; Cecr6.
DR   HOVERGEN; HBG095946; -.
DR   PhylomeDB; Q99MX7; -.
DR   NextBio; 352007; -.
DR   Genevestigator; Q99MX7; -.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    572       Cat eye syndrome critical region protein
FT                                6 homolog.
FT                                /FTId=PRO_0000089467.
FT   COMPBIAS     19     22       Poly-Pro.
FT   COMPBIAS     34    305       Gly-rich.
FT   COMPBIAS     62     66       Poly-Gly.
FT   COMPBIAS     92     95       Poly-Ala.
FT   COMPBIAS    163    171       Poly-Cys.
FT   COMPBIAS    232    235       Poly-Val.
FT   COMPBIAS    536    544       Poly-Pro.
FT   MOD_RES     529    529       Phosphotyrosine.
SQ   SEQUENCE   572 AA;  58158 MW;  5AC65BBE56503A1C CRC64;
     MHPALGHPRA LSSAPASFPP PPAAARLQPL FLRGGSSRGR RGSGDSSTST STSRGGCGGR
     RGGGGGSPSS STGAEREDDD ESISISKPLV PAAAALPGPP AQGGVPVSAT APAAASSTST
     PTSSCSMTAA DFGAGAAAGT VGGPGSRSAV GAGGTGTGGA ASCCSCCCCC CGRPTRSGRR
     GRRRGCSPSP GCRWGYQALS VVLLLAQGGL LDLYLIAVTD LYWCSWIATD LVVVVGWAIF
     FAKNSRGRRG GPANSMHNHH QLHHHSAPPL HLSAAASAGA GAKARGGRGG SGGSGAGPGT
     TGAAGEFAFA YLAWLIYSIA FTPKVVLILG TSILDLIELR APFGTTGFRL TMALSVPLLY
     SLVRAISEAG APPGSAGPLL LQPQQHRAAG CFLGTCLDLL DSFTLVELML DGRVPLPAHL
     RYLLIAVYFL TLASPVLWLY ELNTATAAPS WGQTSGPGSC SRLLRLLGGC LVDVPLLALR
     SLLVVSYQQP LSIFMLKNLF FLGCRGLEAL EGCWDRGSWV SPSRARSSYG APPSAPPPPP
     PPPPQGGSQR GHLENEGGPH GYVNTLAVAS QN
//
ID   CADM3_MOUSE             Reviewed;         396 AA.
AC   Q99N28; Q8BSQ8; Q8K1H8;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Cell adhesion molecule 3;
DE   AltName: Full=Immunoglobulin superfamily member 4B;
DE            Short=IgSF4B;
DE   AltName: Full=Nectin-like protein 1;
DE            Short=NECL-1;
DE   AltName: Full=Synaptic cell adhesion molecule 3;
DE   AltName: Full=TSLC1-like protein 1;
DE   Flags: Precursor;
GN   Name=Cadm3; Synonyms=Igsf4b, Necl1, Syncam3, Tsll1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=129/SvJ;
RX   PubMed=14659875; DOI=10.1016/j.gene.2003.09.018;
RA   Fukami T., Satoh H., Williams Y.N., Masuda M., Fukuhara H.,
RA   Maruyama T., Yageta M., Kuramochi M., Takamoto S., Murakami Y.;
RT   "Isolation of the mouse Tsll1 and Tsll2 genes, orthologues of the
RT   human TSLC1-like genes 1 and 2 (TSLL1 and TSLL2).";
RL   Gene 323:11-18(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH EPB41L1,
RP   SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=15893517; DOI=10.1016/j.bbamem.2005.01.013;
RA   Zhou Y., Du G., Hu X., Yu S., Liu Y., Xu Y., Huang X., Liu J., Yin B.,
RA   Fan M., Peng X., Qiang B., Yuan J.;
RT   "Nectin-like molecule 1 is a protein 4.1N associated protein and
RT   recruits protein 4.1N from cytoplasm to the plasma membrane.";
RL   Biochim. Biophys. Acta 1669:142-154(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 128-396.
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, INTERACTION WITH PVRL3; DLG3; MPP6 AND CASK, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=15741237; DOI=10.1242/jcs.01656;
RA   Kakunaga S., Ikeda W., Itoh S., Deguchi-Tawarada M., Ohtsuka T.,
RA   Mizoguchi A., Takai Y.;
RT   "Nectin-like molecule-1/TSLL1/SynCAM3: a neural tissue-specific
RT   immunoglobulin-like cell-cell adhesion molecule localizing at non-
RT   junctional contact sites of presynaptic nerve terminals, axons and
RT   glia cell processes.";
RL   J. Cell Sci. 118:1267-1277(2005).
CC   -!- FUNCTION: Involved in the cell-cell adhesion. Has both calcium-
CC       independent homophilic cell-cell adhesion activity and calcium-
CC       independent heterophilic cell-cell adhesion activity with IGSF4,
CC       PVRL1 and PVRL3. Interaction with EPB41L1 may regulate structure
CC       or function of cell-cell junctions.
CC   -!- SUBUNIT: Homodimer. Can form trans-heterodimers with PVRL3/nectin-
CC       3. Interacts with EPB41L1, DLG3, MPP6 and CASK.
CC   -!- SUBCELLULAR LOCATION: Cell junction. Cell membrane; Single-pass
CC       type I membrane protein. Note=Localized at the cell-cell attached
CC       sites of the plasma membrane.
CC   -!- TISSUE SPECIFICITY: Mainly expressed in brain, in neuronal cell
CC       bodies of cerebellum, cortex, hippocampus, hypothalamus and spinal
CC       cord. In spinal cord predominantly expressed in motor neurons.
CC       Expressed in axons, presynaptic nerve terminals, glia cell
CC       processes.
CC   -!- DEVELOPMENTAL STAGE: At E14.5 predominantly expressed in the
CC       nervous system.
CC   -!- DOMAIN: The cytoplasmic region mediates interaction with EPB41L1,
CC       DLG3, MPP6 and CASK.
CC   -!- SIMILARITY: Belongs to the nectin family.
CC   -!- SIMILARITY: Contains 2 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC       domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH29659.1; Type=Erroneous initiation;
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DR   EMBL; AY059393; AAL29691.1; -; mRNA.
DR   EMBL; AF195662; AAG35584.1; -; mRNA.
DR   EMBL; AK030782; BAC27137.1; -; mRNA.
DR   EMBL; AK038917; BAC30168.1; -; mRNA.
DR   EMBL; AK053077; BAC35258.1; -; mRNA.
DR   EMBL; BC029659; AAH29659.1; ALT_INIT; mRNA.
DR   IPI; IPI00118020; -.
DR   RefSeq; NP_444429.1; NM_053199.3.
DR   UniGene; Mm.330524; -.
DR   ProteinModelPortal; Q99N28; -.
DR   SMR; Q99N28; 25-319, 352-383.
DR   STRING; Q99N28; -.
DR   PRIDE; Q99N28; -.
DR   Ensembl; ENSMUST00000111220; ENSMUSP00000106851; ENSMUSG00000005338.
DR   GeneID; 94332; -.
DR   KEGG; mmu:94332; -.
DR   UCSC; uc007dri.1; mouse.
DR   CTD; 94332; -.
DR   MGI; MGI:2137858; Cadm3.
DR   eggNOG; roNOG08155; -.
DR   GeneTree; ENSGT00600000084002; -.
DR   HOVERGEN; HBG057086; -.
DR   OrthoDB; EOG4Z62NM; -.
DR   PhylomeDB; Q99N28; -.
DR   NextBio; 352309; -.
DR   ArrayExpress; Q99N28; -.
DR   Bgee; Q99N28; -.
DR   CleanEx; MM_CADM3; -.
DR   Genevestigator; Q99N28; -.
DR   GermOnline; ENSMUSG00000005338; Mus musculus.
DR   GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:HGNC.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion; IDA:HGNC.
DR   GO; GO:0007156; P:homophilic cell adhesion; IDA:HGNC.
DR   GO; GO:0008104; P:protein localization; IMP:MGI.
DR   InterPro; IPR013162; CD80_C2-set.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR003585; Neurexin-like.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3.
DR   Pfam; PF08205; C2-set_2; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00294; 4.1m; 1.
DR   SMART; SM00409; IG; 2.
DR   SMART; SM00408; IGc2; 1.
DR   PROSITE; PS50835; IG_LIKE; 3.
PE   1: Evidence at protein level;
KW   Calcium; Cell adhesion; Cell junction; Cell membrane; Disulfide bond;
KW   Glycoprotein; Immunoglobulin domain; Membrane; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     22       By similarity.
FT   CHAIN        23    396       Cell adhesion molecule 3.
FT                                /FTId=PRO_0000046068.
FT   TOPO_DOM     23    328       Extracellular (Potential).
FT   TRANSMEM    329    349       Helical; (Potential).
FT   TOPO_DOM    350    396       Cytoplasmic (Potential).
FT   DOMAIN       23    124       Ig-like V-type.
FT   DOMAIN      128    226       Ig-like C2-type 1.
FT   DOMAIN      231    313       Ig-like C2-type 2.
FT   CARBOHYD     23     23       N-linked (GlcNAc...) (Potential).
FT   DISULFID     48    108       By similarity.
FT   DISULFID    150    207       By similarity.
FT   DISULFID    252    297       By similarity.
SQ   SEQUENCE   396 AA;  42964 MW;  C1ADF8B57D141F3A CRC64;
     MGAPSALPLL LLLACSWAPG GANLSQDDSQ PWTSDETVVA GGTVVLKCQV KDHEDSSLQW
     SNPAQQTLYF GEKRALRDNR IQLVSSTPHE LSISISNVAL ADEGEYTCSI FTMPVRTAKS
     LVTVLGIPQK PIITGYKSSL REKETATLNC QSSGSKPAAQ LTWRKGDQEL HGDQTRIQED
     PNGKTFTVSS SVSFQVTRED DGANIVCSVN HESLKGADRS TSQRIEVLYT PTAMIRPEPA
     HPREGQKLLL HCEGRGNPVP QQYVWVKEGS EPPLKMTQES ALIFPFLNKS DSGTYGCTAT
     SNMGSYTAYF TLNVNDPSPV PSSSSTYHAI IGGIVAFIVF LLLILLIFLG HYLIRHKGTY
     LTHEAKGSDD APDADTAIIN AEGGQSGGDD KKEYFI
//
ID   SYTL2_MOUSE             Reviewed;         950 AA.
AC   Q99N50; B2RS48; B7ZNS4; Q8BT37; Q99J89; Q99J90; Q99N51; Q99N52;
AC   Q99N55; Q99N56;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2003, sequence version 2.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Synaptotagmin-like protein 2;
DE   AltName: Full=Exophilin-4;
GN   Name=Sytl2; Synonyms=Slp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH NRXN1.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=21139758; PubMed=11243866; DOI=10.1006/bbrc.2001.4512;
RA   Fukuda M., Mikoshiba K.;
RT   "Synaptotagmin-like protein 1-3: a novel family of C-terminal-type
RT   tandem C2 proteins.";
RL   Biochem. Biophys. Res. Commun. 281:1226-1233(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6 AND 7), AND
RP   TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=21226169; PubMed=11327731; DOI=10.1006/bbrc.2001.4803;
RA   Fukuda M., Saegusa C., Mikoshiba K.;
RT   "Novel splicing isoforms of synaptotagmin-like proteins 2 and 3:
RT   identification of the Slp homology domain.";
RL   Biochem. Biophys. Res. Commun. 283:513-519(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 11), FUNCTION, SUBCELLULAR
RP   LOCATION, INTERACTION WITH RAB27A, PROTEOLYTIC PROCESSING, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=18266782; DOI=10.1111/j.1600-0854.2008.00714.x;
RA   Holt O., Kanno E., Bossi G., Booth S., Daniele T., Santoro A.,
RA   Arico M., Saegusa C., Fukuda M., Griffiths G.M.;
RT   "Slp1 and Slp2-a localize to the plasma membrane of CTL and contribute
RT   to secretion from the immunological synapse.";
RL   Traffic 9:446-457(2008).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   INTERACTION WITH RAB27A.
RX   MEDLINE=21883924; PubMed=11773082; DOI=10.1074/jbc.M112414200;
RA   Kuroda T.S., Fukuda M., Ariga H., Mikoshiba K.;
RT   "The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2
RT   functions as a novel Rab27A binding domain.";
RL   J. Biol. Chem. 277:9212-9218(2002).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-698; LYS-699;
RP   LYS-700; LYS-705 AND LYS-706.
RX   PubMed=15543135; DOI=10.1038/ncb1197;
RA   Kuroda T.S., Fukuda M.;
RT   "Rab27A-binding protein Slp2-a is required for peripheral melanosome
RT   distribution and elongated cell shape in melanocytes.";
RL   Nat. Cell Biol. 6:1195-1203(2004).
RN   [8]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INTERACTION
RP   WITH RAB27A AND RAB27B.
RX   PubMed=16716193; DOI=10.1111/j.1365-2443.2006.00964.x;
RA   Saegusa C., Tanaka T., Tani S., Itohara S., Mikoshiba K., Fukuda M.;
RT   "Decreased basal mucus secretion by Slp2-a-deficient gastric surface
RT   mucous cells.";
RL   Genes Cells 11:623-631(2006).
RN   [9]
RP   SUBCELLULAR LOCATION, INTERACTION WITH RAB27A, AND TISSUE SPECIFICITY.
RX   PubMed=17182843; DOI=10.1091/mbc.E06-10-0914;
RA   Yu M., Kasai K., Nagashima K., Torii S., Yokota-Hashimoto H.,
RA   Okamoto K., Takeuchi T., Gomi H., Izumi T.;
RT   "Exophilin4/Slp2-a targets glucagon granules to the plasma membrane
RT   through unique Ca2+-inhibitory phospholipid-binding activity of the
RT   C2A domain.";
RL   Mol. Biol. Cell 18:688-696(2007).
RN   [10]
RP   ALTERNATIVE SPLICING (ISOFORMS 9 AND 10).
RX   PubMed=16376427; DOI=10.1016/j.molimm.2005.10.019;
RA   Mascarell L., Auger R., Kanellopoulos J.M., Truffa-Bachi P.;
RT   "The usage of alternative splice sites in Mus musculus synaptotagmin-
RT   like 2 gene is modulated by cyclosporin A and FK506 in T-
RT   lymphocytes.";
RL   Mol. Immunol. 43:1846-1854(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-799, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263; SER-279; SER-400;
RP   SER-488 AND SER-578, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621
RP   (ISOFORM 2), AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Isoform 11 acts as a RAB27A effector protein and plays a
CC       role in cytotoxic granule exocytosis in lymphocytes. Required for
CC       cytotoxic granule docking at the immunologic synapse. Isoform 1
CC       may play a role in melanosome transport and vesicle trafficking.
CC       It controls melanosome distribution in the cell periphery and
CC       regulates melanocyte morphology. Isoform 1 acts as a positive
CC       mediator of mucus secretion by the surface mucus cells of the
CC       stomach. Mediates basal mucus secretion by gastric surface cells
CC       by promoting the proper granule biognesis and docking of mucus
CC       granules with the apical plasma membrane.
CC   -!- SUBUNIT: Monomer. Binds NRXN1. Binds RAB27A that has been
CC       activated by GTP-binding. Interacts with RAB27B.
CC   -!- INTERACTION:
CC       Q9CS84:Nrxn1; NbExp=1; IntAct=EBI-398197, EBI-399696;
CC       Q9ERI2:Rab27a; NbExp=1; IntAct=EBI-398197, EBI-398172;
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Melanosome membrane; Peripheral
CC       membrane protein (Potential). Note=Bound to melanosomes. Isoform 1
CC       is localized mainly on peripheral melanosomes but not on less
CC       mature melanosomes around the nucleus.
CC   -!- SUBCELLULAR LOCATION: Isoform 11: Cell membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=11;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1; Synonyms=Slp2-a;
CC         IsoId=Q99N50-1; Sequence=Displayed;
CC       Name=2; Synonyms=Slp2-b;
CC         IsoId=Q99N50-2; Sequence=VSP_007889;
CC       Name=3; Synonyms=Slp2-a delta 2S-I;
CC         IsoId=Q99N50-3; Sequence=VSP_007892;
CC         Note=Phosphorylated on Ser-621;
CC       Name=4; Synonyms=Slp2-a delta 2S-II;
CC         IsoId=Q99N50-4; Sequence=VSP_007893;
CC       Name=5; Synonyms=Slp2-a delta 2S-III;
CC         IsoId=Q99N50-5; Sequence=VSP_007894;
CC       Name=6; Synonyms=Slp2-c;
CC         IsoId=Q99N50-6; Sequence=VSP_007890;
CC       Name=7; Synonyms=Slp2-d delta 2S-IV;
CC         IsoId=Q99N50-7; Sequence=VSP_007891;
CC       Name=8;
CC         IsoId=Q99N50-8; Sequence=VSP_007890, VSP_007894;
CC         Note=No experimental confirmation available;
CC       Name=9; Synonyms=Slp2-e;
CC         IsoId=Q99N50-9; Sequence=Not described;
CC         Note=Due to intron retention;
CC       Name=10; Synonyms=Slp2-f;
CC         IsoId=Q99N50-10; Sequence=Not described;
CC         Note=Due to intron retention;
CC       Name=11;
CC         IsoId=Q99N50-11; Sequence=VSP_007893, VSP_007894;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain, lung, kidney,
CC       testis and in embryos after day 7. Detected at lower levels in
CC       skeletal muscle. Expressed in pancreatic alpha cells. Isoform 6 is
CC       highly expressed in brain, but not detectable in the other tissues
CC       tested. Isoform 1 is expressed abundantly in the stomach and is
CC       predominantly localized at the apical region of gastric-surface
CC       mucus cells. Isoform 11 is expressed in cytotoxic T-lymphocytes
CC       (CTL).
CC   -!- DOMAIN: The RabBD domain mediates interaction with RAB27A (By
CC       similarity).
CC   -!- DOMAIN: The C2 1 domain mediates localization to the cell membrane
CC       (By similarity).
CC   -!- PTM: Isoform 1 is highly susceptible to proteolytic degradation
CC       and is stabilized by the interaction with RAB27A.
CC   -!- DISRUPTION PHENOTYPE: Mice show a reduced number of mucus
CC       granules, a deficiency of granule docking with the apical plasma
CC       membrane in the gastric-surface mucus cells and reduction of mucus
CC       secretion by gastric primary cells.
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -!- SIMILARITY: Contains 1 RabBD (Rab-binding) domain.
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DR   EMBL; AB057756; BAB41084.1; -; mRNA.
DR   EMBL; AB050742; BAB32652.1; -; mRNA.
DR   EMBL; AB057754; BAB41082.1; -; mRNA.
DR   EMBL; AB057755; BAB41083.1; -; mRNA.
DR   EMBL; AB057757; BAB41085.1; -; mRNA.
DR   EMBL; AB057760; BAB41088.1; -; mRNA.
DR   EMBL; AB057761; BAB41089.1; -; mRNA.
DR   EMBL; AB057762; BAB41090.1; -; mRNA.
DR   EMBL; AB057763; BAB41091.1; -; mRNA.
DR   EMBL; AK027924; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC138714; AAI38715.1; -; mRNA.
DR   EMBL; BC145398; AAI45399.1; -; mRNA.
DR   IPI; IPI00118092; -.
DR   IPI; IPI00320921; -.
DR   IPI; IPI00336618; -.
DR   IPI; IPI00336619; -.
DR   IPI; IPI00336621; -.
DR   IPI; IPI00336622; -.
DR   IPI; IPI00467898; -.
DR   IPI; IPI00468887; -.
DR   IPI; IPI00944088; -.
DR   RefSeq; NP_001035174.1; NM_001040085.1.
DR   RefSeq; NP_001035176.1; NM_001040087.1.
DR   RefSeq; NP_001035177.1; NM_001040088.1.
DR   RefSeq; NP_113571.2; NM_031394.2.
DR   UniGene; Mm.26751; -.
DR   ProteinModelPortal; Q99N50; -.
DR   SMR; Q99N50; 10-56, 643-942.
DR   IntAct; Q99N50; 2.
DR   STRING; Q99N50; -.
DR   PhosphoSite; Q99N50; -.
DR   PRIDE; Q99N50; -.
DR   Ensembl; ENSMUST00000032846; ENSMUSP00000032846; ENSMUSG00000030616.
DR   Ensembl; ENSMUST00000098310; ENSMUSP00000095912; ENSMUSG00000030616.
DR   Ensembl; ENSMUST00000107210; ENSMUSP00000102828; ENSMUSG00000030616.
DR   Ensembl; ENSMUST00000107211; ENSMUSP00000102829; ENSMUSG00000030616.
DR   GeneID; 83671; -.
DR   KEGG; mmu:83671; -.
DR   UCSC; uc009iha.1; mouse.
DR   UCSC; uc009ihb.1; mouse.
DR   UCSC; uc009ihc.1; mouse.
DR   UCSC; uc009ihg.1; mouse.
DR   UCSC; uc009ihh.1; mouse.
DR   UCSC; uc009ihk.1; mouse.
DR   CTD; 83671; -.
DR   MGI; MGI:1933366; Sytl2.
DR   GeneTree; ENSGT00550000074462; -.
DR   HOVERGEN; HBG060218; -.
DR   OrthoDB; EOG4QC15M; -.
DR   NextBio; 350686; -.
DR   ArrayExpress; Q99N50; -.
DR   Bgee; Q99N50; -.
DR   CleanEx; MM_SYTL2; -.
DR   Genevestigator; Q99N50; -.
DR   GermOnline; ENSMUSG00000030616; Mus musculus.
DR   GO; GO:0019897; C:extrinsic to plasma membrane; IDA:UniProtKB.
DR   GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0042043; F:neurexin binding; IDA:UniProtKB.
DR   GO; GO:0017137; F:Rab GTPase binding; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0070257; P:positive regulation of mucus secretion; IMP:UniProtKB.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR010911; Rab-bd_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00168; C2; 2.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS50916; RABBD; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Exocytosis; Membrane;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1    950       Synaptotagmin-like protein 2.
FT                                /FTId=PRO_0000190214.
FT   DOMAIN        1     57       RabBD.
FT   DOMAIN      646    750       C2 1.
FT   DOMAIN      795    897       C2 2.
FT   COMPBIAS    596    636       Ser-rich.
FT   MOD_RES     263    263       Phosphoserine.
FT   MOD_RES     279    279       Phosphoserine.
FT   MOD_RES     400    400       Phosphoserine.
FT   MOD_RES     488    488       Phosphoserine.
FT   MOD_RES     578    578       Phosphoserine.
FT   MOD_RES     799    799       Phosphoserine.
FT   VAR_SEQ       1    695       Missing (in isoform 7).
FT                                /FTId=VSP_007891.
FT   VAR_SEQ       1    574       Missing (in isoform 6 and isoform 8).
FT                                /FTId=VSP_007890.
FT   VAR_SEQ       1    487       MIDLSFLTEEEQDAILKVLQRDAALKRAEEERVRHLPEKIK
FT                                DDQQLKNMSGQWFYEAKAKRHRDKIHGADIIRASMRRKKLP
FT                                AAAEQNKDTAMRAKESWVNNVNKDAVLPPEIAVVEEPEDDT
FT                                DPAGPSSSLVDPASSVIDMSQESTRTPAVSLPKQRKNPFNS
FT                                PKLPEDHSLQQTKPEQSKTGKAGLFQISKEGELSESKEKSS
FT                                IPDMPRQQLEKPKQTVSTEPENASHTKAPIPKARKLIYKSN
FT                                DLEKDDNQSFPRQRRDSLNARGAPRGILKRNSSSSSTDSET
FT                                LRLNYNLDPKSKILSPGLTIHERISEKEFSLEDDSSTSSLE
FT                                PLKHVRFSAVKNELPQSPRPVLGQEVGEFTVLESDQLQNGT
FT                                EDAGDIEEFQNHPELSHKTPLSHYQLVSSPSDSGREREQLM
FT                                SSGSAPRDEIPCHSDILPTGPQCVESSSVINGQQEKSSHFT
FT                                KLPSELSKSPSDELTQCGEPEPSQTADHSFRDHRQG -> M
FT                                EKLNFKCMPQEPPDETIFPQKTLSIEPSKENEGKNTEYFGT
FT                                QVIKKACSEQEIQESIVKTSILPKVSKDTFNDRLQKLLAEA
FT                                TLPASQTSGKEVHEQQALKVGVSENGKSFAKDEEEVTGLRE
FT                                SPKEPQRRNQQDCSVDKLLKESTRTPLSPLQSPLEAVTTRP
FT                                ISPLKDDLLFEKWMKENHSPSADQREITAPFPQGVGILAGA
FT                                DLIQKGKHCNTEAMLQLAAEGSPPLAQLPHSFDGVSSSPAD
FT                                MSLSWDAQLPSENGTLPSQKEISEAIEKVVLPSKPAATDVN
FT                                AVLQKLLREAGEVDAKLPEREQTAGTPSCPQRVSPLWPAPD
FT                                PVVPNKDFHSFCTVPDTTHEGRSHLSARMSPSAHATMSPTS
FT                                TVTQYGQRLLQEVAETVRETVIQPKSQYPEFRAGLEKLLKE
FT                                TLQTSLSKDKKDTMTISPSALTGSCEMSHQLSSEFHLTEIQ
FT                                ETVEKAEAPSVTESSFDVGLEKLLKEMSEGPCQLQASGRRD
FT                                TLEKQPSQVEQAGFMGEIPHHILDGPGASKMKVSCSGLESQ
FT                                ISQCDKQLGGDEAVTGPLIDVQDNKSGFEVPECSQLHEDHK
FT                                IETNGTIQFVEDKGREKVITGETQASQEPGFEEAPKEMSVS
FT                                RNKHSIVLLETKGKAIKTREVKLVLATPYKRQEEEQGPEAC
FT                                SEYEFSDGNTSSNRENGRNTSS (in isoform 2).
FT                                /FTId=VSP_007889.
FT   VAR_SEQ      85    111       Missing (in isoform 3).
FT                                /FTId=VSP_007892.
FT   VAR_SEQ     539    555       DQKADQEPDTNECIPGI -> V (in isoform 4 and
FT                                isoform 11).
FT                                /FTId=VSP_007893.
FT   VAR_SEQ     587    626       Missing (in isoform 5, isoform 8 and
FT                                isoform 11).
FT                                /FTId=VSP_007894.
FT   MUTAGEN     698    698       K->Q: Loss of membrane localization; when
FT                                associated with Q-699; Q-700; Q-705 and
FT                                Q-706.
FT   MUTAGEN     699    699       K->Q: Loss of membrane localization; when
FT                                associated with Q-698; Q-700; Q-705 and
FT                                Q-706.
FT   MUTAGEN     700    700       K->Q: Loss of membrane localization; when
FT                                associated with Q-698; Q-699; Q-705 and
FT                                Q-706.
FT   MUTAGEN     705    705       K->Q: Loss of membrane localization; when
FT                                associated with Q-698; Q-699; Q-700 and
FT                                Q-706.
FT   MUTAGEN     706    706       K->Q: Loss of membrane localization; when
FT                                associated with Q-698; Q-699; Q-700 and
FT                                Q-705.
SQ   SEQUENCE   950 AA;  106806 MW;  226B59F5A32FA4A4 CRC64;
     MIDLSFLTEE EQDAILKVLQ RDAALKRAEE ERVRHLPEKI KDDQQLKNMS GQWFYEAKAK
     RHRDKIHGAD IIRASMRRKK LPAAAEQNKD TAMRAKESWV NNVNKDAVLP PEIAVVEEPE
     DDTDPAGPSS SLVDPASSVI DMSQESTRTP AVSLPKQRKN PFNSPKLPED HSLQQTKPEQ
     SKTGKAGLFQ ISKEGELSES KEKSSIPDMP RQQLEKPKQT VSTEPENASH TKAPIPKARK
     LIYKSNDLEK DDNQSFPRQR RDSLNARGAP RGILKRNSSS SSTDSETLRL NYNLDPKSKI
     LSPGLTIHER ISEKEFSLED DSSTSSLEPL KHVRFSAVKN ELPQSPRPVL GQEVGEFTVL
     ESDQLQNGTE DAGDIEEFQN HPELSHKTPL SHYQLVSSPS DSGREREQLM SSGSAPRDEI
     PCHSDILPTG PQCVESSSVI NGQQEKSSHF TKLPSELSKS PSDELTQCGE PEPSQTADHS
     FRDHRQGSEE EHSPVLKTLE RRAARKLPSK SLEDIPSDSS NQAKVDNLPE ELVRSAEDDQ
     KADQEPDTNE CIPGISTVPS LPDNQFSHPD KLKRMSKSVP AFLQDESDDR ETDTASESSY
     QLRRYKKSPS SLTNLSSSSG MTSLSSASGS VMSVYSGDFG NLEVKGSVQF ALDYVESLKE
     LHVFVAQCKD LAAADVKKQR SDPYVKTYLL PDKGKMGKKK TLVVKKTLNP VYNEILRYKI
     ERQFLKTQKL NLSVWHRDTF KRNSFLGEVE LDLETWDWDS KQNKQLKWYP LKRKTAPVAL
     ETENRGEMKL ALQYVPEPSP GKKLPTTGEV HIWVKECLDL PLLRGSHLNS FVKCTILPDT
     SRKSRQKTRA VGKTTNPVFN HTMVYDGFRP EDLMEACVEL TVWDHYKLTN QFLGGLRIGF
     GTGKSYGTEV DWMDSTSEEV ALWEKMVNSP NTWVEATLPL RMLLIAKLSK
//
ID   RAF1_MOUSE              Reviewed;         648 AA.
AC   Q99N57; Q3UR68; Q58E75; Q91WH1; Q99N58; Q9QUU8;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 2.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=RAF proto-oncogene serine/threonine-protein kinase;
DE            EC=2.7.11.1;
DE   AltName: Full=Proto-oncogene c-RAF;
DE            Short=cRaf;
DE   AltName: Full=Raf-1;
GN   Name=Raf1; Synonyms=Craf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   MEDLINE=21481893; PubMed=11597136; DOI=10.1006/geno.2001.6627;
RA   Gray T.A., Azama K., Whitmore K., Min A., Abe S., Nicholls R.D.;
RT   "Phylogenetic conservation of the makorin-2 gene, encoding a multiple
RT   zinc-finger protein, antisense to the raf1 proto-oncogene.";
RL   Genomics 77:119-126(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II, and FVB/N; TISSUE=Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND
RP   TISSUE SPECIFICITY.
RX   MEDLINE=91360260; PubMed=1886707;
RA   Dozier C., Ansieau S., Ferreira E., Coll J., Stehelin D.;
RT   "An alternatively spliced c-mil/raf mRNA is predominantly expressed in
RT   chicken muscular tissues and conserved among vertebrate species.";
RL   Oncogene 6:1307-1311(1991).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Involved in the transduction of mitogenic signals from
CC       the cell membrane to the nucleus. Part of the Ras-dependent
CC       signaling pathway from receptors to the nucleus. Protects cells
CC       from apoptosis mediated by STK3 (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
CC   -!- SUBUNIT: Forms a multiprotein complex with Ras (M-Ras/MRAS), SHOC2
CC       and protein phosphatase 1 (PPP1CA, PPP1CB and PPP1CC). Interacts
CC       with Ras proteins; the interaction is antagonized by RIN1. Weakly
CC       interacts with RIT1 (By similarity). Interacts with STK3; the
CC       interaction inhibits its pro-apoptotic activity. Interacts (when
CC       phosphorylated at Ser-259) with YWHAZ (unphosphorylated at 'Thr-
CC       232').
CC   -!- INTERACTION:
CC       P28028:Braf; NbExp=1; IntAct=EBI-397757, EBI-2584830;
CC       Q969H4:CNKSR1 (xeno); NbExp=1; IntAct=EBI-397757, EBI-741671;
CC       P32883-2:Kras; NbExp=2; IntAct=EBI-397757, EBI-644285;
CC       P70336:Rock2; NbExp=1; IntAct=EBI-397757, EBI-771800;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=6C;
CC         IsoId=Q99N57-1; Sequence=Displayed;
CC       Name=2; Synonyms=1A;
CC         IsoId=Q99N57-2; Sequence=VSP_034629;
CC   -!- TISSUE SPECIFICITY: Present in all tissues tested: testis, ovary,
CC       small intestine, colon, peripheral blood leukocytes, fetal liver,
CC       bone marrow, thymus, lymph node and spleen, and the cell lines
CC       melanoma G361, lung carcinoma A549, colorectal adenocarcinoma
CC       SW480, Burkitt's lymphoma Raji and lymphoblastic leukemia MOLT-4.
CC       In skeletal muscle, isoform 1 is more abundant than isoform 2.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC       Phosphorylation at Thr-269 increases its kinase activity.
CC       Phosphorylation at Ser-259 induces the interaction with YWHAZ and
CC       inactivates kinase activity. Dephosphorylation of Ser-259 by the
CC       complex containing protein phosphatase 1, SHOC2 and M-Ras/MRAS
CC       relieves inactivation, leading to stimulate RAF1 activity.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. RAF subfamily.
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 RBD (Ras-binding) domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB057655; BAB39748.1; -; mRNA.
DR   EMBL; AB057663; BAB39743.2; -; mRNA.
DR   EMBL; AK141745; BAE24820.1; -; mRNA.
DR   EMBL; BC015273; AAH15273.1; -; mRNA.
DR   EMBL; BC092040; AAH92040.1; -; mRNA.
DR   EMBL; X55432; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00118101; -.
DR   IPI; IPI00830899; -.
DR   RefSeq; NP_084056.1; NM_029780.3.
DR   UniGene; Mm.184163; -.
DR   ProteinModelPortal; Q99N57; -.
DR   SMR; Q99N57; 56-131, 136-187, 340-615.
DR   IntAct; Q99N57; 12.
DR   STRING; Q99N57; -.
DR   PhosphoSite; Q99N57; -.
DR   PRIDE; Q99N57; -.
DR   Ensembl; ENSMUST00000000451; ENSMUSP00000000451; ENSMUSG00000000441.
DR   Ensembl; ENSMUST00000112949; ENSMUSP00000108571; ENSMUSG00000000441.
DR   GeneID; 110157; -.
DR   KEGG; mmu:110157; -.
DR   UCSC; uc009dix.1; mouse.
DR   CTD; 110157; -.
DR   MGI; MGI:97847; Raf1.
DR   eggNOG; roNOG12302; -.
DR   HOGENOM; HBG506535; -.
DR   HOVERGEN; HBG001886; -.
DR   InParanoid; Q99N57; -.
DR   OMA; DGPSCIS; -.
DR   OrthoDB; EOG4QVCBJ; -.
DR   PhylomeDB; Q99N57; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 363431; -.
DR   ArrayExpress; Q99N57; -.
DR   Bgee; Q99N57; -.
DR   CleanEx; MM_RAF1; -.
DR   Genevestigator; Q99N57; -.
DR   GermOnline; ENSMUSG00000000441; Mus musculus.
DR   GO; GO:0005829; C:cytosol; TAS:MGI.
DR   GO; GO:0005886; C:plasma membrane; TAS:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005057; F:receptor signaling protein activity; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IGI:MGI.
DR   GO; GO:0007010; P:cytoskeleton organization; IMP:MGI.
DR   GO; GO:0007243; P:intracellular protein kinase cascade; TAS:MGI.
DR   GO; GO:0048011; P:nerve growth factor receptor signaling pathway; IMP:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR003116; Raf-like_ras-bd.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   Pfam; PF02196; RBD; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00455; RBD; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50898; RBD; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Kinase; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Proto-oncogene;
KW   Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    648       RAF proto-oncogene serine/threonine-
FT                                protein kinase.
FT                                /FTId=PRO_0000086597.
FT   DOMAIN       56    131       RBD.
FT   DOMAIN      349    609       Protein kinase.
FT   ZN_FING     138    184       Phorbol-ester/DAG-type.
FT   NP_BIND     355    363       ATP (By similarity).
FT   ACT_SITE    468    468       Proton acceptor (By similarity).
FT   METAL       139    139       Zinc 1 (By similarity).
FT   METAL       152    152       Zinc 2 (By similarity).
FT   METAL       155    155       Zinc 2 (By similarity).
FT   METAL       165    165       Zinc 1 (By similarity).
FT   METAL       168    168       Zinc 1 (By similarity).
FT   METAL       173    173       Zinc 2 (By similarity).
FT   METAL       176    176       Zinc 2 (By similarity).
FT   METAL       184    184       Zinc 1 (By similarity).
FT   BINDING     375    375       ATP (By similarity).
FT   MOD_RES      43     43       Phosphoserine (By similarity).
FT   MOD_RES     244    244       Phosphoserine (By similarity).
FT   MOD_RES     252    252       Phosphoserine (By similarity).
FT   MOD_RES     257    257       Phosphoserine (By similarity).
FT   MOD_RES     258    258       Phosphothreonine (By similarity).
FT   MOD_RES     259    259       Phosphoserine (By similarity).
FT   MOD_RES     268    268       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     269    269       Phosphothreonine (By similarity).
FT   MOD_RES     289    289       Phosphoserine (By similarity).
FT   MOD_RES     294    294       Phosphoserine (By similarity).
FT   MOD_RES     301    301       Phosphoserine (By similarity).
FT   MOD_RES     338    338       Phosphoserine (By similarity).
FT   MOD_RES     499    499       Phosphoserine (By similarity).
FT   MOD_RES     612    612       Phosphoserine (By similarity).
FT   MOD_RES     621    621       Phosphoserine.
FT   MOD_RES     642    642       Phosphoserine (By similarity).
FT   VAR_SEQ     278    278       E -> ESNSLNASPRACSRRFCLRGR (in isoform
FT                                2).
FT                                /FTId=VSP_034629.
FT   CONFLICT    522    522       D -> N (in Ref. 3; AAH92040).
FT   CONFLICT    543    543       A -> T (in Ref. 3; AAH92040).
SQ   SEQUENCE   648 AA;  72917 MW;  B70104AEF51C44A5 CRC64;
     MEHIQGAWKT ISNGFGLKDA VFDGSSCISP TIVQQFGYQR RASDDGKLTD SSKTSNTIRV
     FLPNKQRTVV NVRNGMSLHD CLMKALKVRG LQPECCAVFR LLQEHKGKKA RLDWNTDAAS
     LIGEELQVDF LDHVPLTTHN FARKTFLKLA FCDICQKFLL NGFRCQTCGY KFHEHCSTKV
     PTMCVDWSNI RQLLLFPNST VGDSGVPAPP SFPMRRMRES VSRMPASSQH RYSTPHAFTF
     NTSSPSSEGS LSQRQRSTST PNVHMVSTTL HVDSRMIEDA IRSHSESASP SALSSSPNNL
     SPTGWSQPKT PVPAQRERAP GSGTQEKNKI RPRGQRDSSY YWEIEASEVM LSTRIGSGSF
     GTVYKGKWHG DVAVKILKVV DPTPEQLQAF RNEVAVLRKT RHVNILLFMG YMTKDNLAIV
     TQWCEGSSLY KHLHVQETKF QMFQLIDIAR QTAQGMDYLH AKNIIHRDMK SNNIFLHEGL
     TVKIGDFGLA TVKSRWSGSQ QVEQPTGSVL WMAPEVIRMQ DDNPFSFQSD VYSYGIVLYE
     LMAGELPYAH INNRDQIIFM VGRGYASPDL SRLYKNCPKA MKRLVADCVK KVKEERPLFP
     QILSSIELLQ HSLPKINRSA SEPSLHRAAH TEDINACTLT TSPRLPVF
//
ID   SYTL1_MOUSE             Reviewed;         567 AA.
AC   Q99N80; Q99J26;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2003, sequence version 2.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Synaptotagmin-like protein 1;
DE   AltName: Full=Exophilin-7;
GN   Name=Sytl1; Synonyms=Slp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH NRXN1.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=21139758; PubMed=11243866; DOI=10.1006/bbrc.2001.4512;
RA   Fukuda M., Mikoshiba K.;
RT   "Synaptotagmin-like protein 1-3: a novel family of C-terminal-type
RT   tandem C2 proteins.";
RL   Biochem. Biophys. Res. Commun. 281:1226-1233(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary cancer;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH RAB27A.
RX   MEDLINE=21883924; PubMed=11773082; DOI=10.1074/jbc.M112414200;
RA   Kuroda T.S., Fukuda M., Ariga H., Mikoshiba K.;
RT   "The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2
RT   functions as a novel Rab27A binding domain.";
RL   J. Biol. Chem. 277:9212-9218(2002).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB27A, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=18266782; DOI=10.1111/j.1600-0854.2008.00714.x;
RA   Holt O., Kanno E., Bossi G., Booth S., Daniele T., Santoro A.,
RA   Arico M., Saegusa C., Fukuda M., Griffiths G.M.;
RT   "Slp1 and Slp2-a localize to the plasma membrane of CTL and contribute
RT   to secretion from the immunological synapse.";
RL   Traffic 9:446-457(2008).
CC   -!- FUNCTION: Binds phosphatidylinositol 3,4,5-triphosphate (By
CC       similarity). May play a role in vesicle trafficking. Acts as a
CC       RAB27A effector protein and may play a role in cytotoxic granule
CC       exocytosis in lymphocytes.
CC   -!- SUBUNIT: Monomer. Binds NCF2 and NRXN1 (By similarity). Binds
CC       RAB27A that has been activated by GTP-binding via its N-terminus.
CC   -!- INTERACTION:
CC       Q9CS84:Nrxn1; NbExp=1; IntAct=EBI-398182, EBI-399696;
CC       Q9ERI2:Rab27a; NbExp=1; IntAct=EBI-398182, EBI-398172;
CC   -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane
CC       protein. Cell membrane.
CC   -!- TISSUE SPECIFICITY: Highly expressed in lung. Detected at lower
CC       levels in spleen, liver and kidney, and at very low levels in
CC       heart, brain and skeletal muscle. Expressed in cytotoxic T-
CC       lymphocytes (CTL).
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -!- SIMILARITY: Contains 1 RabBD (Rab-binding) domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB050741; BAB32651.1; -; mRNA.
DR   EMBL; BC005623; AAH05623.1; -; mRNA.
DR   IPI; IPI00118188; -.
DR   UniGene; Mm.25660; -.
DR   ProteinModelPortal; Q99N80; -.
DR   SMR; Q99N80; 40-86, 269-562.
DR   IntAct; Q99N80; 2.
DR   STRING; Q99N80; -.
DR   PhosphoSite; Q99N80; -.
DR   PRIDE; Q99N80; -.
DR   Ensembl; ENSMUST00000030674; ENSMUSP00000030674; ENSMUSG00000028860.
DR   MGI; MGI:1933365; Sytl1.
DR   GeneTree; ENSGT00550000074462; -.
DR   HOVERGEN; HBG057965; -.
DR   InParanoid; Q99N80; -.
DR   OrthoDB; EOG483D4P; -.
DR   ArrayExpress; Q99N80; -.
DR   Bgee; Q99N80; -.
DR   CleanEx; MM_SYTL1; -.
DR   Genevestigator; Q99N80; -.
DR   GermOnline; ENSMUSG00000028860; Mus musculus.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0019897; C:extrinsic to plasma membrane; IDA:UniProtKB.
DR   GO; GO:0042470; C:melanosome; IDA:UniProtKB.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005625; C:soluble fraction; IDA:UniProtKB.
DR   GO; GO:0042043; F:neurexin binding; IDA:UniProtKB.
DR   GO; GO:0017137; F:Rab GTPase binding; IEA:InterPro.
DR   GO; GO:0006887; P:exocytosis; IDA:UniProtKB.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR010911; Rab-bd_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00168; C2; 2.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS50916; RABBD; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Exocytosis; Membrane; Phosphoprotein; Repeat.
FT   CHAIN         1    567       Synaptotagmin-like protein 1.
FT                                /FTId=PRO_0000190212.
FT   DOMAIN       31     87       RabBD.
FT   DOMAIN      273    373       C2 1.
FT   DOMAIN      414    516       C2 2.
FT   COMPBIAS    241    262       Ser-rich.
FT   MOD_RES     397    397       Phosphoserine (By similarity).
FT   CONFLICT    178    178       H -> Q (in Ref. 1; BAB32651).
SQ   SEQUENCE   567 AA;  62362 MW;  13ACC780131F65FB CRC64;
     MPQRGHPSQE RLWALPSLPM AHGPGSEVEG LLDLSFLTEE EQEAISDVLK RDAHLRQLEE
     GRVSKLRASL EDPWQLKILT GDWFQEARSQ RHHHAHFGSD LVRASIRRKK SPKGDQALGS
     DGEAEAAGED TIEGEPESRV SIEVAAPERS TETQGPDLSS PYVPSKASEG QEEEPQDHEC
     ELEAPGEGGV QVAEADPELD PEQKAEQESQ PTPAQSKATS KILENGEEAP GLGPSLDRML
     SSSSSVSSLN SSTLSGSLMS LSGEEAGTVQ VRGSVLFSLH YEPGTSELRV QVIQCQGLAA
     ARRRRSDPYV KSYLLPDKQS KRKTSVKKRN LNPIFNETLR HSVQQADLPG RVLSLSVWHR
     ESLGRNIFLG EVEVPLDTWN WDSEATWLPL QPRVPPSPDE LPSRGLLSLS LKYVPAGSEG
     GGQPQSGELH FWVKEAQSLV PLRPGSLDTY IQCSVLPDDS RASRQRTRVV RRSLSPVFNH
     TMVYDGFGPA DLRQACAELS LWDHGALASR QLGGTRLSLG TGSSYGLQVP WMDSTPEEKQ
     LWQTLLERPC EWVDGLLPLR TNLVPRA
//
ID   RM01_MOUSE              Reviewed;         336 AA.
AC   Q99N96; Q3UQP5; Q8K351; Q9CWW4;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=39S ribosomal protein L1, mitochondrial;
DE            Short=L1mt;
DE            Short=MRP-L1;
DE   Flags: Precursor;
GN   Name=Mrpl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, and Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 11-336.
RX   MEDLINE=21293042; PubMed=11279069; DOI=10.1074/jbc.M100826200;
RA   Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A.,
RA   Watanabe K.;
RT   "Structural compensation for the deficit of rRNA with proteins in the
RT   mammalian mitochondrial ribosome. Systematic analysis of protein
RT   components of the large ribosomal subunit from mammalian
RT   mitochondria.";
RL   J. Biol. Chem. 276:21724-21736(2001).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the ribosomal protein L1P family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH61042.1; Type=Erroneous initiation;
CC       Sequence=BAB26866.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAB26866.1; Type=Frameshift; Positions=7;
CC       Sequence=BAB40837.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK010343; BAB26866.1; ALT_SEQ; mRNA.
DR   EMBL; AK142249; BAE24994.1; -; mRNA.
DR   EMBL; BC028774; AAH28774.1; -; mRNA.
DR   EMBL; BC061042; AAH61042.1; ALT_INIT; mRNA.
DR   EMBL; AB049632; BAB40837.1; ALT_INIT; mRNA.
DR   IPI; IPI00118237; -.
DR   RefSeq; NP_444388.2; NM_053158.2.
DR   UniGene; Mm.295499; -.
DR   ProteinModelPortal; Q99N96; -.
DR   SMR; Q99N96; 95-313.
DR   STRING; Q99N96; -.
DR   PRIDE; Q99N96; -.
DR   Ensembl; ENSMUST00000036437; ENSMUSP00000037046; ENSMUSG00000029486.
DR   Ensembl; ENSMUST00000117766; ENSMUSP00000112977; ENSMUSG00000029486.
DR   GeneID; 94061; -.
DR   KEGG; mmu:94061; -.
DR   UCSC; uc008yfi.1; mouse.
DR   CTD; 94061; -.
DR   MGI; MGI:2137202; Mrpl1.
DR   eggNOG; roNOG09550; -.
DR   HOGENOM; HBG713326; -.
DR   HOVERGEN; HBG061212; -.
DR   InParanoid; Q99N96; -.
DR   OMA; VEIELNM; -.
DR   OrthoDB; EOG4K6G54; -.
DR   NextBio; 352027; -.
DR   ArrayExpress; Q99N96; -.
DR   Bgee; Q99N96; -.
DR   CleanEx; MM_MRPL1; -.
DR   Genevestigator; Q99N96; -.
DR   GermOnline; ENSMUSG00000029486; Mus musculus.
DR   GO; GO:0005762; C:mitochondrial large ribosomal subunit; IDA:MGI.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:MGI.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IDA:MGI.
DR   InterPro; IPR002143; Ribosomal_L1.
DR   InterPro; IPR016094; Ribosomal_L1_2-a/b-sand.
DR   InterPro; IPR016095; Ribosomal_L1_3-a/b-sand.
DR   InterPro; IPR005879; Ribosomal_L1_mit.
DR   Gene3D; G3DSA:3.30.190.20; Ribosomal_L1_2-a/b-sand; 2.
DR   Gene3D; G3DSA:3.40.50.790; Ribosomal_L1_3-a/b-sand; 1.
DR   Pfam; PF00687; Ribosomal_L1; 1.
DR   SUPFAM; SSF56808; Ribosomal_L1; 1.
DR   TIGRFAMs; TIGR01170; rplA_mito; 1.
PE   1: Evidence at protein level;
KW   Mitochondrion; Phosphoprotein; Ribonucleoprotein; Ribosomal protein;
KW   Transit peptide.
FT   TRANSIT       1     50       Mitochondrion (Potential).
FT   CHAIN        51    336       39S ribosomal protein L1, mitochondrial.
FT                                /FTId=PRO_0000252441.
FT   COMPBIAS     44     50       Poly-Ala.
FT   MOD_RES      85     85       Phosphoserine.
FT   CONFLICT     56     56       K -> E (in Ref. 2; BAB26866).
FT   CONFLICT     94     94       K -> R (in Ref. 2; BAB26866).
FT   CONFLICT    118    118       D -> G (in Ref. 2; BAB26866).
FT   CONFLICT    131    131       T -> R (in Ref. 2; BAB26866).
FT   CONFLICT    140    140       K -> R (in Ref. 2; BAB26866).
FT   CONFLICT    180    180       A -> V (in Ref. 2; BAB26866).
SQ   SEQUENCE   336 AA;  37597 MW;  328783081296B824 CRC64;
     MAAAVRCLRR VLIHHQRHCL CKMASQASLY PCSVNSLLHN RHFAAAAAAA TKPARKIKKG
     AKEKTSDEKP VDDIEKIKSY TYMESDPEDD VYLKRLYPRR IYEVEKAIHL LKKFQVLDFT
     NPKQGVYLDL TLDMALGKKK TVEPFASVIA LPHLFSSEVN KVAVFTANAS EIKIAEENGA
     AFAGGTDLVK KIMDDEVVVD FYVAVPEIMG ELNPLRKKLK KRFPKATRNS IGRDIPKMLE
     LFKTAHEIMV DEERQNFLST KIATLDMPSD QIAANLQAVI NEVCKHRPLN LGPFVVRAFL
     RSSTSEGLLL KTDSLLPKEA KTTEAETEET QTAEAA
//
ID   ACS2L_MOUSE             Reviewed;         682 AA.
AC   Q99NB1; Q8K0M6;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Acetyl-coenzyme A synthetase 2-like, mitochondrial;
DE            EC=6.2.1.1;
DE   AltName: Full=Acetate--CoA ligase 2;
DE   AltName: Full=Acetyl-CoA synthetase 2;
DE            Short=AceCS2;
DE   AltName: Full=Acyl-CoA synthetase short-chain family member 1;
DE   Flags: Precursor;
GN   Name=Acss1; Synonyms=Acas2, Acas2l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   MEDLINE=21179204; PubMed=11150295; DOI=10.1074/jbc.M008782200;
RA   Fujino T., Kondo J., Ishikawa M., Morikawa K., Yamamoto T.T.;
RT   "Acetyl-CoA synthetase 2, a mitochondrial matrix enzyme involved in
RT   the oxidation of acetate.";
RL   J. Biol. Chem. 276:11420-11426(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 262-682.
RC   TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, INTERACTION WITH SIRT3, ENZYME REGULATION, MASS
RP   SPECTROMETRY, AND ACETYLATION AT LYS-635.
RX   PubMed=16790548; DOI=10.1073/pnas.0604392103;
RA   Hallows W.C., Lee S., Denu J.M.;
RT   "Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:10230-10235(2006).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19187775; DOI=10.1016/j.cmet.2008.12.008;
RA   Sakakibara I., Fujino T., Ishii M., Tanaka T., Shimosawa T., Miura S.,
RA   Zhang W., Tokutake Y., Yamamoto J., Awano M., Iwasaki S., Motoike T.,
RA   Okamura M., Inagaki T., Kita K., Ezaki O., Naito M., Kuwaki T.,
RA   Chohnan S., Yamamoto T.T., Hammer R.E., Kodama T., Yanagisawa M.,
RA   Sakai J.;
RT   "Fasting-induced hypothermia and reduced energy production in mice
RT   lacking acetyl-CoA synthetase 2.";
RL   Cell Metab. 9:191-202(2009).
CC   -!- FUNCTION: Important for maintaining normal body temperature during
CC       fasting and for energy homeostasis. Essential for energy
CC       expenditure under ketogenic conditions. Converts acetate to
CC       acetyl-CoA so that it can be used for oxidation through the
CC       tricarboxylic cycle to produce ATP and CO(2).
CC   -!- CATALYTIC ACTIVITY: ATP + acetate + CoA = AMP + diphosphate +
CC       acetyl-CoA.
CC   -!- ENZYME REGULATION: Inhibited by acetylation at Lys-635 and
CC       activated by deacetylation.
CC   -!- SUBUNIT: Interacts with SIRT3.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart, testis, kidney,
CC       skeletal muscle, lung and spleen. Detected at low levels in brain.
CC   -!- INDUCTION: By fasting.
CC   -!- PTM: Reversibly acetylated at Lys-635. The acetyl-CoA synthase
CC       activity is inhibited by acetylation and activated by
CC       deacetylation.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype at birth, but exhibit
CC       significant growth retardation at the time of weaning. Attain
CC       normal size and weight when fed normally. Exhibit hypothermia and
CC       hypoglycemia when fed high-fat, low-carbohydrate diet, leading to
CC       50% mortality. Display strongly reduced whole-body acetate
CC       oxidation when fasting. Fasting adults exhibit hypothermia,
CC       reduced capacity to sustain running and low ATP levels.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH30930.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB046742; BAB21612.1; -; mRNA.
DR   EMBL; AK088244; BAC40232.1; -; mRNA.
DR   EMBL; BC030930; AAH30930.1; ALT_INIT; mRNA.
DR   IPI; IPI00469942; -.
DR   RefSeq; NP_542142.1; NM_080575.2.
DR   UniGene; Mm.7044; -.
DR   ProteinModelPortal; Q99NB1; -.
DR   SMR; Q99NB1; 48-672.
DR   STRING; Q99NB1; -.
DR   PhosphoSite; Q99NB1; -.
DR   PRIDE; Q99NB1; -.
DR   Ensembl; ENSMUST00000028944; ENSMUSP00000028944; ENSMUSG00000027452.
DR   GeneID; 68738; -.
DR   KEGG; mmu:68738; -.
DR   UCSC; uc008muf.1; mouse.
DR   CTD; 68738; -.
DR   MGI; MGI:1915988; Acss1.
DR   GeneTree; ENSGT00550000074278; -.
DR   HOVERGEN; HBG014401; -.
DR   InParanoid; Q99NB1; -.
DR   OMA; VNCLDQH; -.
DR   OrthoDB; EOG4RFKS6; -.
DR   PhylomeDB; Q99NB1; -.
DR   BRENDA; 6.2.1.1; 244.
DR   Pathway_Interaction_DB; hdac_classiii_pathway; Signaling events mediated by HDAC Class III.
DR   NextBio; 327818; -.
DR   ArrayExpress; Q99NB1; -.
DR   Bgee; Q99NB1; -.
DR   CleanEx; MM_ACSS1; -.
DR   Genevestigator; Q99NB1; -.
DR   GermOnline; ENSMUSG00000027452; Mus musculus.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; ISS:UniProtKB.
DR   GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006085; P:acetyl-CoA biosynthetic process; ISS:UniProtKB.
DR   InterPro; IPR011904; Ac_CoA_lig.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   Pfam; PF00501; AMP-binding; 1.
DR   TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Ligase; Mitochondrion; Nucleotide-binding;
KW   Transit peptide.
FT   TRANSIT       1     38       Mitochondrion (Potential).
FT   CHAIN        39    682       Acetyl-coenzyme A synthetase 2-like,
FT                                mitochondrial.
FT                                /FTId=PRO_0000000597.
FT   MOD_RES     389    389       N6-acetyllysine (By similarity).
FT   MOD_RES     635    635       N6-acetyllysine.
FT   CONFLICT    332    332       W -> C (in Ref. 3; AAH30930).
SQ   SEQUENCE   682 AA;  74623 MW;  1B21981D29F9C8E7 CRC64;
     MAARSLGSGV GRLLRGLQGR SGQSGWSLSV SRSTATRLPG CVPAAAQPGS YPALSAQAAQ
     EPAAFWGPLA RDTLVWDTPY HTVWDCDFRT GKIGWFLGGQ LNVSVNCLDQ HVQKSPETIA
     LIWERDEPGT EVRITYRELL ETTCRLANTL KRHGVHRGDR VAIYMPVSPL AVAAMLACAR
     IGAIHTVVFA GFSAESLAGR INDAKCKAVI TFNQGLRGGR VVELKKIVDE AVKSCPTVQH
     VLVAHRTDTK VPMGSLDIPL EQEMAKEAPV CTPESMSSED MLFMLYTSGS TGTPKGLVHT
     QAGYLLYAAM THKLVFDYQP GDVFGCVADI GWITGHSYVV YGPLCNGATT VLFESTPVYP
     DAGRYWETVQ RLKINQFYGA PTAVRLLLKY GDAWVKKYDR SSLRTLGSVG EPINHEAWEW
     LHKVVGDGRC TLVDTWWQTE TGGICIAPRP SEDGAEILPG MAMRPFFGIV PVLMDEKGNV
     LEGGDVSGAL CISQAWPGMA RTIYGDHQRF VDAYFRAYPG YYFTGDGAHR TEGGYYQITG
     RMDDVINISG HRLGTAEIED AMADHPAVPE TAVIGYPHDI KGEAAFAFIV LKDNISDENM
     VVNELKLSVA TKIAKYAVPD QILVVKRLPK TRSGKVMRRL LRKIITSRGQ DLGDTTTLED
     PSVITEILSA FQKYEEQRAA TN
//
ID   SF3B1_MOUSE             Reviewed;        1304 AA.
AC   Q99NB9; Q9CSK5;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Splicing factor 3B subunit 1;
DE   AltName: Full=Pre-mRNA-splicing factor SF3b 155 kDa subunit;
DE            Short=SF3b155;
DE   AltName: Full=Spliceosome-associated protein 155;
DE            Short=SAP 155;
GN   Name=Sf3b1; Synonyms=Sap155;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RX   MEDLINE=21189985; PubMed=11252167; DOI=10.1007/s003350010258;
RA   Isono K., Abe K., Tomaru Y., Okazaki Y., Hayashizaki Y., Koseki H.;
RT   "Molecular cloning, genetic mapping, and expression of the mouse Sf3b1
RT   (SAP155) gene for the U2 snRNP component of spliceosome.";
RL   Mamm. Genome 12:192-198(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-490.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-142, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-142; THR-207; THR-211;
RP   THR-223; THR-227; THR-267; THR-313; THR-326 AND THR-328, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129 AND THR-278, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Subunit of the splicing factor SF3B required for 'A'
CC       complex assembly formed by the stable binding of U2 snRNP to the
CC       branchpoint sequence (BPS) in pre-mRNA. Sequence independent
CC       binding of SF3A/SF3B complex upstream of the branch site is
CC       essential, it may anchor U2 snRNP to the pre-mRNA. May also be
CC       involved in the assembly of the 'E' complex. Belongs also to the
CC       minor U12-dependent spliceosome, which is involved in the splicing
CC       of rare class of nuclear pre-mRNA intron (By similarity).
CC   -!- SUBUNIT: Component of splicing factor SF3B which is composed of at
CC       least eight subunits; SF3B1/SAP155/SF3B155, SF3B2/SAP145/SF3B145,
CC       SF3B3/SAP130/SF3B130, SF3B4/SAP49/SF3B49, SF3B14A, PHF5A/SF3B14B,
CC       SF3B10 and SF3B125. Component of the U11/U12 snRNPs that are part
CC       of the U12-type spliceosome. Component of the B-WICH complex, at
CC       least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C,
CC       ERCC6, MYBBP1A and DDX21. SF3B associates with the splicing factor
CC       SF3A and a 12S RNA unit to form the U2 small nuclear
CC       ribonucleoproteins complex (U2 snRNP). SF3B1 interacts directly
CC       with the splicing factor U2AF. Phosphorylated form interacts with
CC       PPP1R8 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- PTM: Phosphorylated. Phosphorylation occurs concomitantly with the
CC       splicing catalytic steps. Phosphorylation on Thr-244, Thr-248 and
CC       Thr-313 by cyclin-dependent kinases promotes interaction with
CC       PPP1R8 during mitosis (By similarity).
CC   -!- SIMILARITY: Belongs to the SF3B1 family.
CC   -!- SIMILARITY: Contains 11 HEAT repeats.
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DR   EMBL; AB037890; BAB40140.1; -; mRNA.
DR   EMBL; AK012632; BAB28369.1; -; mRNA.
DR   IPI; IPI00623284; -.
DR   UniGene; Mm.279736; -.
DR   ProteinModelPortal; Q99NB9; -.
DR   SMR; Q99NB9; 379-424, 584-718, 1015-1085, 1129-1155.
DR   STRING; Q99NB9; -.
DR   PhosphoSite; Q99NB9; -.
DR   PRIDE; Q99NB9; -.
DR   Ensembl; ENSMUST00000027127; ENSMUSP00000027127; ENSMUSG00000025982.
DR   UCSC; uc007azx.1; mouse.
DR   MGI; MGI:1932339; Sf3b1.
DR   GeneTree; ENSGT00390000018393; -.
DR   HOGENOM; HBG330902; -.
DR   HOVERGEN; HBG079173; -.
DR   InParanoid; Q99NB9; -.
DR   OrthoDB; EOG4RJG0Q; -.
DR   PhylomeDB; Q99NB9; -.
DR   ArrayExpress; Q99NB9; -.
DR   Bgee; Q99NB9; -.
DR   CleanEx; MM_SF3B1; -.
DR   Genevestigator; Q99NB9; -.
DR   GermOnline; ENSMUSG00000025982; Mus musculus.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0009952; P:anterior/posterior pattern formation; IGI:MGI.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR015016; SF3b_su1.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 2.
DR   Pfam; PF08920; SF3b1; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Repeat; Spliceosome.
FT   CHAIN         1   1304       Splicing factor 3B subunit 1.
FT                                /FTId=PRO_0000174324.
FT   REPEAT      529    568       HEAT 1.
FT   REPEAT      569    603       HEAT 2.
FT   REPEAT      604    641       HEAT 3.
FT   REPEAT      643    677       HEAT 4.
FT   REPEAT      680    718       HEAT 5.
FT   REPEAT      763    801       HEAT 6.
FT   REPEAT      843    881       HEAT 7.
FT   REPEAT     1010   1048       HEAT 8.
FT   REPEAT     1052   1090       HEAT 9.
FT   REPEAT     1122   1160       HEAT 10.
FT   REPEAT     1163   1201       HEAT 11.
FT   REGION      223    491       Interaction with PPP1R8 (By similarity).
FT   MOD_RES     129    129       Phosphoserine.
FT   MOD_RES     141    141       N6-acetyllysine (By similarity).
FT   MOD_RES     142    142       Phosphothreonine.
FT   MOD_RES     194    194       Phosphoserine (By similarity).
FT   MOD_RES     207    207       Phosphothreonine.
FT   MOD_RES     211    211       Phosphothreonine.
FT   MOD_RES     223    223       Phosphothreonine.
FT   MOD_RES     227    227       Phosphothreonine.
FT   MOD_RES     235    235       Phosphothreonine (By similarity).
FT   MOD_RES     244    244       Phosphothreonine (By similarity).
FT   MOD_RES     248    248       Phosphothreonine (By similarity).
FT   MOD_RES     257    257       Phosphothreonine (By similarity).
FT   MOD_RES     261    261       Phosphothreonine (By similarity).
FT   MOD_RES     267    267       Phosphothreonine.
FT   MOD_RES     273    273       Phosphothreonine (By similarity).
FT   MOD_RES     278    278       Phosphothreonine.
FT   MOD_RES     296    296       Phosphothreonine (By similarity).
FT   MOD_RES     299    299       Phosphothreonine (By similarity).
FT   MOD_RES     313    313       Phosphothreonine.
FT   MOD_RES     316    316       Phosphothreonine (By similarity).
FT   MOD_RES     322    322       Phosphoserine (By similarity).
FT   MOD_RES     326    326       Phosphothreonine.
FT   MOD_RES     328    328       Phosphothreonine.
FT   MOD_RES     332    332       Phosphoserine (By similarity).
FT   MOD_RES     341    341       Phosphothreonine (By similarity).
FT   MOD_RES     344    344       Phosphoserine (By similarity).
FT   MOD_RES     349    349       Phosphoserine (By similarity).
FT   MOD_RES     350    350       Phosphothreonine (By similarity).
FT   MOD_RES     354    354       Phosphothreonine (By similarity).
FT   MOD_RES     400    400       Phosphoserine (By similarity).
FT   MOD_RES     432    432       Phosphothreonine (By similarity).
FT   MOD_RES     434    434       Phosphothreonine (By similarity).
FT   MOD_RES     436    436       Phosphothreonine (By similarity).
FT   MOD_RES     488    488       Phosphoserine (By similarity).
FT   MOD_RES     554    554       N6-acetyllysine (By similarity).
FT   MOD_RES     562    562       N6-acetyllysine (By similarity).
SQ   SEQUENCE   1304 AA;  145816 MW;  12F051757D2A2DEE CRC64;
     MAKIAKTHED IEAQIREIQG KKAALDEAQG VGLDSTGYYD QEIYGGSDSR FAGYVTSIAA
     TELEDDDDDY SSSTSLLGQK KPGYHAPVAL LNDIPQSTEQ YDPFAEHRPP KIADREDEYK
     KHRRTMIISP ERLDPFADGG KTPDPKMNAR TYMDVMREQH LTKEEREIRQ QLAEKAKAGE
     LKVVNGAAAS QPPSKRKRRW DQTADQTPGA TPKKLSSWDQ AETPGHTPSL RWDETPGRAK
     GSETPGATPG SKIWDPTPSH TPAGAATPGR GDTPGHATPG HGGATSSARK NRWDETPKTE
     RDTPGHGSGW AETPRTDRGG DSIGETPTPG ASKRKSRWDE TPASQMGGST PVLTPGKTPI
     GTPAMNMATP TPGHIMSMTP EQLQAWRWER EIDERNRPLS DEELDAMFPE GYKVLPPPAG
     YVPIRTPARK LTATPTPLGG MTGFHMQTED RTMKSVNDQP SGNLPFLKPD DIQYFDKLLV
     DVDESTLSPE EQKERKIMKL LLKIKNGTPP MRKAALRQIT DKAREFGAGP LFNQILPLLM
     SPTLEDQERH LLVKVIDRIL YKLDDLVRPY VHKILVVIEP LLIDEDYYAR VEGREIISNL
     AKAAGLATMI STMRPDIDNM DEYVRNTTAR AFAVVASALG IPSLLPFLKA VCKSKKSWQA
     RHTGIKIVQQ IAILMGCAIL PHLRSLVEII EHGLVDEQQK VRTISALAIA ALAEAATPYG
     IESFDSVLKP LWKGIRQHRG KGLAAFLKAI GYLIPLMDAE YANYYTREVM LILIREFQSP
     DEEMKKIVLK VVKQCCGTDG VEANYIKTEI LPPFFKHFWQ HRMALDRRNY RQLVDTTVEL
     ANKVGAAEII SRIVDDLKDE AEQYRKMVME TIEKIMGNLG AADIDHKLEE QLIDGILYAF
     QEQTTEDSVM LNGFGTVVNA LGKRVKPYLP QICGTVLWRL NNKSAKVRQQ AADLISRTAV
     VMKTCQEEKL MGHLGVVLYE YLGEEYPEVL GSILGALKAI VNVIGMHKMT PPIKDLLPRL
     TPILKNRHEK VQENCIDLVG RIADRGAEYV SAREWMRICF ELLELLKAHK KAIRRATVNT
     FGYIAKAIGP HDVLATLLNN LKVQERQNRV CTTVAIAIVA ETCSPFTVLP ALMNEYRVPE
     LNVQNGVLKS LSFLFEYIGE MGKDYIYAVT PLLEDALMDR DLVHRQTASA VVQHMSLGVY
     GFGCEDSLNH LLNYVWPNVF ETSPHVIQAV MGALEGLRVA IGPCRMLQYC LQGLFHPARK
     VRDVYWKIYN SIYIGSQDAL IAHYPRIYND DKNTYIRYDL DYIL
//
ID   RIMS1_MOUSE             Reviewed;        1463 AA.
AC   Q99NE5; Q5DU35; Q5J8K0; Q5J8K1; Q5J8K2; Q5J8K3; Q5J8K4;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   11-JAN-2011, entry version 82.
DE   RecName: Full=Regulating synaptic membrane exocytosis protein 1;
DE   AltName: Full=Rab-3-interacting molecule 1;
DE            Short=RIM 1;
DE   AltName: Full=Rab-3-interacting protein 1;
GN   Name=Rims1; Synonyms=Kiaa0340, Rab3ip1, Rim1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING,
RP   MUTAGENESIS OF ARG-33, AND INTERACTION WITH RAB3A; RAB3B AND RAB3D.
RC   TISSUE=Brain;
RX   MEDLINE=21413899; PubMed=11431472; DOI=10.1074/jbc.M103337200;
RA   Wang X., Hu B., Zimmermann B., Kilimann M.W.;
RT   "Rim1 and rabphilin-3 bind Rab3-GTP by composite determinants
RT   partially related through N-terminal alpha-helix motifs.";
RL   J. Biol. Chem. 276:32480-32488(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4; 5 AND 6).
RA   Wang X., Hu B., Kilimann M.W.;
RL   Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 202-1463 (ISOFORM 7).
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   CHARACTERIZATION.
RX   PubMed=11797009; DOI=10.1038/415321a;
RA   Schoch S., Castillo P.E., Jo T., Mukherjee K., Geppert M., Wang Y.,
RA   Schmitz F., Malenka R.C., Suedhof T.C.;
RT   "RIM1alpha forms a protein scaffold for regulating neurotransmitter
RT   release at the active zone.";
RL   Nature 415:321-326(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346; SER-812; THR-1025;
RP   SER-1027 AND SER-1451, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-716; SER-812; SER-1023;
RP   THR-1025 AND SER-1448, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Rab effector involved in exocytosis. May act as scaffold
CC       protein that regulates neurotransmitter release at the active
CC       zone. Essential for maintaining normal probability of
CC       neurotransmitter release and for regulating release during short-
CC       term synaptic plasticity.
CC   -!- SUBUNIT: Binds SNAP25, SYT1 and CACNA1B. Interaction with SYT1 is
CC       enhanced by calcium ions. Interaction with SNAP25 is weaker in the
CC       presence of calcium ions. Binds RIM binding proteins 1 and 2;
CC       interacts with PPFIA3 and PPFIA4 (By similarity). Binds RAB3A,
CC       RAB3B and RAB3D that have been activated by GTP-binding. Binds
CC       UNC13A.
CC   -!- INTERACTION:
CC       Q9CZV8:Fbxl20; NbExp=2; IntAct=EBI-775541, EBI-1551033;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       (By similarity). Cell junction, synapse (By similarity). Cell
CC       junction, synapse, presynaptic cell membrane; Peripheral membrane
CC       protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC         Comment=A number of isoforms are produced;
CC       Name=1;
CC         IsoId=Q99NE5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99NE5-2; Sequence=VSP_022231, VSP_022232;
CC       Name=3;
CC         IsoId=Q99NE5-3; Sequence=VSP_022235;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q99NE5-4; Sequence=VSP_022235, VSP_022236;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q99NE5-5; Sequence=VSP_022234;
CC         Note=No experimental confirmation available;
CC       Name=6;
CC         IsoId=Q99NE5-6; Sequence=VSP_022233;
CC         Note=No experimental confirmation available;
CC       Name=7;
CC         IsoId=Q99NE5-7; Sequence=VSP_022230, VSP_022233, VSP_022237,
CC                                  VSP_022238;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 RabBD (Rab-binding) domain.
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DR   EMBL; AJ310531; CAC32041.1; -; mRNA.
DR   EMBL; AY356534; AAR14797.1; -; mRNA.
DR   EMBL; AY356535; AAR14798.1; -; mRNA.
DR   EMBL; AY356536; AAR14799.1; -; mRNA.
DR   EMBL; AY356537; AAR14800.1; -; mRNA.
DR   EMBL; AY356538; AAR14801.1; -; mRNA.
DR   EMBL; AK220335; BAD90402.1; -; mRNA.
DR   IPI; IPI00118692; -.
DR   IPI; IPI00136021; -.
DR   IPI; IPI00553549; -.
DR   IPI; IPI00553696; -.
DR   IPI; IPI00553828; -.
DR   IPI; IPI00816873; -.
DR   IPI; IPI00816908; -.
DR   RefSeq; NP_001012641.1; NM_001012623.1.
DR   RefSeq; NP_001012642.1; NM_001012624.1.
DR   RefSeq; NP_001012643.1; NM_001012625.1.
DR   RefSeq; NP_444500.1; NM_053270.1.
DR   RefSeq; NP_898839.2; NM_183018.2.
DR   UniGene; Mm.380549; -.
DR   UniGene; Mm.461684; -.
DR   UniGene; Mm.60061; -.
DR   ProteinModelPortal; Q99NE5; -.
DR   SMR; Q99NE5; 136-193, 418-526, 580-706, 1295-1442.
DR   IntAct; Q99NE5; 5.
DR   MINT; MINT-1210408; -.
DR   STRING; Q99NE5; -.
DR   PRIDE; Q99NE5; -.
DR   GeneID; 116837; -.
DR   KEGG; mmu:116837; -.
DR   CTD; 116837; -.
DR   MGI; MGI:2152971; Rims1.
DR   HOVERGEN; HBG058147; -.
DR   NextBio; 369178; -.
DR   CleanEx; MM_RIMS1; -.
DR   Genevestigator; Q99NE5; -.
DR   GermOnline; ENSMUSG00000041670; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
DR   GO; GO:0017137; F:Rab GTPase binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR   GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:MGI.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR010911; Rab-bd_domain.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 2.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00239; C2; 2.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50916; RABBD; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Exocytosis;
KW   Membrane; Metal-binding; Neurotransmitter transport; Phosphoprotein;
KW   Repeat; Synapse; Transport; Zinc; Zinc-finger.
FT   CHAIN         1   1463       Regulating synaptic membrane exocytosis
FT                                protein 1.
FT                                /FTId=PRO_0000190199.
FT   DOMAIN       22    205       RabBD.
FT   DOMAIN      440    526       PDZ.
FT   DOMAIN      579    685       C2 1.
FT   DOMAIN     1309   1411       C2 2.
FT   ZN_FING     133    193       FYVE-type.
FT   MOD_RES     346    346       Phosphoserine.
FT   MOD_RES     716    716       Phosphoserine.
FT   MOD_RES     812    812       Phosphoserine.
FT   MOD_RES    1023   1023       Phosphoserine.
FT   MOD_RES    1025   1025       Phosphothreonine.
FT   MOD_RES    1027   1027       Phosphoserine.
FT   MOD_RES    1441   1441       Phosphothreonine (By similarity).
FT   MOD_RES    1448   1448       Phosphoserine.
FT   MOD_RES    1450   1450       Phosphoserine (By similarity).
FT   MOD_RES    1451   1451       Phosphoserine.
FT   MOD_RES    1454   1454       Phosphoserine (By similarity).
FT   MOD_RES    1463   1463       Phosphoserine (By similarity).
FT   VAR_SEQ     369    369       K -> KEEEYQTRYRSDPNLARYPVKAPLEEQQMRMHARVS
FT                                RARHERRHSDVALPHTEAAAAVSAETTAGKRAQTTARVSPP
FT                                ESPRARAPAAQPPAEHGPPPPRPAPGPAEPPEPRVPEPLRK
FT                                QGRLDPGSAVLLRKAKREKAESMLRNDSLSSDQSESVRPSP
FT                                PKPHRPKRGGKRRQMSVSSS (in isoform 7).
FT                                /FTId=VSP_022230.
FT   VAR_SEQ     373    388       GVSTPEYTSCEDVELE -> YQTRYRSDPNLARYPV (in
FT                                isoform 2).
FT                                /FTId=VSP_022231.
FT   VAR_SEQ     389   1463       Missing (in isoform 2).
FT                                /FTId=VSP_022232.
FT   VAR_SEQ     853   1016       Missing (in isoform 6 and isoform 7).
FT                                /FTId=VSP_022233.
FT   VAR_SEQ     904   1016       Missing (in isoform 5).
FT                                /FTId=VSP_022234.
FT   VAR_SEQ     904    931       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_022235.
FT   VAR_SEQ     956   1016       Missing (in isoform 4).
FT                                /FTId=VSP_022236.
FT   VAR_SEQ    1150   1170       FTPKMQGRRMGTSGRAIIKST -> LTLVLLMMALPYKFVQ
FT                                KSRLF (in isoform 7).
FT                                /FTId=VSP_022237.
FT   VAR_SEQ    1171   1463       Missing (in isoform 7).
FT                                /FTId=VSP_022238.
FT   MUTAGEN      33     33       R->G: Abolishes interaction with RAB3A.
SQ   SEQUENCE   1463 AA;  163161 MW;  1E0BE5D522924738 CRC64;
     MSSAVGPRGP RPPTVPPPMQ ELPDLSHLTE EERNIIMAVM DRQKEEEEKE EAMLKCVVRD
     MAKPAACKTP RNAESQPHQP PLNIFRCVCV PRKPSSEEGG PDRNWRLHQQ FESYKEQVRK
     IGEEARRYQG EHKDDAPTCG ICHKTKFADG CGHLCSYCRT KFCARCGGRV SLRSNNEDKV
     VMWVCNLCRK QQEILTKSGA WFFGSGPQQP SQDGTLSDTA TGAGSEVPRE KKARLQERSR
     SQTPLSTAAV SSQDTASHGA PLDRNKGAEP SQQALGPEQK QASRSRSEPP RERKKAPGLS
     EQNGKGGQKS ERKRVPKSVV QPGEGTADER ERKERRETRR LEKGRSQDYP DRLEKREDGR
     VAEDEKQRKE EEGVSTPEYT SCEDVELESE SVSEKGDLDY WLDPATWHSR ETSPISSHPV
     TWQPSKEGDR LIGRVILNKR TTMPKESGAL LGLKVVGGKM TDLGRLGAFI TKVKKGSLAD
     VVGHLRAGDE VLEWNGKPLP GATNEEVYNI ILESKSEPQV EIIVSRPIGD IPRIPESSHP
     PLESSSSSFE SQKMERPSIS VISPTSPGAL KDAPQVLPGQ LSVKLWYDKV GHQLIVNVLQ
     ATDLPPRVDG RPRNPYVKMY FLPDRSDKSK RRTKTVKKLL EPKWNQTFVY SHVHRRDFRE
     RMLEITVWDQ PRVQDEESEF LGEILIELET ALLDDEPHWY KLQTHDESSL PLPQPSPFMP
     RRHIHGESSS KKLQRSQRIS DSDISDYEVD DGIGVVPPVG YRASARESKA TTLTVPEQQR
     TTHHRSRSVS PHRGDDQGRP RSRLPNVPLQ RSLDEIHPTR RSRSPTRHHD ASRSLADHRS
     RHAESQYSSE PDSELLMLPR AKRGRSAECL HMTSELQPSL DRARSASTNC LRPDTSLHSP
     ERERGRWSPS LARRRPASPR IQIQHASPEN DRHSRKSERS SIQKQSRKGT ASDADRVLPP
     CLSRRGYAIP RATDQPVIRG KHTTRSRSSE HSSIRTLCSM HHLAPGGSAP PSPLLTRTHR
     QGSPTQSPPA DTSFGSRRGR QLPQVPVRSG SIEQASLVVE ERTRQMKMKV HRFKQTTGSG
     SSQELDHEQY SKYNIHKDQY RSCDNASAKS SDSDVSDVSA ISRASSTSRL SSTSFMSEQS
     ERPRGRISSF TPKMQGRRMG TSGRAIIKST SVSGEIYTLE HNDGSQSDTA VGTVGAGGKK
     RRSSLSAKVV AIVSRRSRST SQLSQTESGH KKLKSTIQRS TETGMAAEMR KMVRQPSRES
     TDGSINSYSS EGNLIFPGVR VGPDSQFSDF LDGLGPAQLV GRQTLATPAM GDIQIGMEDK
     KGQLEVEVIR ARSLTQKPGS KSTPAPYVKV YLLENGACIA KKKTRIARKT LDPLYQQSLV
     FDESPQGKVL QVIVWGDYGR MDHKCFMGVA QILLEELDLS SMVIGWYKLF PPSSLVDPTL
     TPLTRRASQS SLESSSGPPC IRS
//
ID   NELF_MOUSE              Reviewed;         532 AA.
AC   Q99NF2; A2AJ93; A2AJ94; Q8BPT0; Q8C9R5; Q9DBF4; Q9ERZ1;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Nasal embryonic luteinizing hormone-releasing hormone factor;
DE            Short=Nasal embryonic LHRH factor;
DE   AltName: Full=Juxtasynaptic attractor of caldendrin on dendritic boutons protein;
DE            Short=Jacob protein;
GN   Name=Nelf; Synonyms=Jac;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY,
RP   SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC   STRAIN=NIH Swiss;
RX   MEDLINE=20357114; PubMed=10898796;
RA   Kramer P.R., Wray S.;
RT   "Novel gene expressed in nasal region influences outgrowth of
RT   olfactory axons and migration of luteinizing hormone-releasing hormone
RT   (LHRH) neurons.";
RL   Genes Dev. 14:1824-1834(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RA   Dieterich D.C., Hoffmann B., Seidenbecher C.I., Kreutz M.R.;
RT   "Characterization of the novel brain-specific protein Jacob.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 4 AND 5).
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=15018815; DOI=10.1016/S1567-133X(01)00004-7;
RA   Kramer P.R., Wray S.;
RT   "Nasal embryonic LHRH factor (NELF) expression within the CNS and PNS
RT   of the rodent.";
RL   Gene Expr. Patterns 1:23-26(2001).
CC   -!- FUNCTION: Influences outgrowth of olfactory axons and migration of
CC       LHRH neurons. Couples NMDA receptor signaling to the nucleus (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with CABP1 and KPNA1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC       Nucleus (By similarity). Note=Found on the outside of the LHRH
CC       cell membrane and axons projecting from the olfactory pit and
CC       epithelium. Myristoylation is a prerequisite for extranuclear
CC       localization (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q99NF2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99NF2-2; Sequence=VSP_014767;
CC       Name=3;
CC         IsoId=Q99NF2-3; Sequence=VSP_014768;
CC       Name=4;
CC         IsoId=Q99NF2-4; Sequence=VSP_014764, VSP_014767, VSP_014769;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q99NF2-5; Sequence=VSP_014765, VSP_014766;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in adult brain and liver. In the
CC       brain, expressed in the cortex, hippocampus, olfactory bulb and
CC       thalamus.
CC   -!- DEVELOPMENTAL STAGE: At E14.5 embryo found at high levels within
CC       the forebrain, olfactory epithelium and olfactory pit. At E12.5
CC       embryo detected on olfactory axons including olfactory pathway on
CC       which the LHRH neurons move. From E11.5 to E17.5 embryos expressed
CC       in LHRH (luteinizing hormone-releasing hormone) neurons as they
CC       migrate from the olfactory pit into the developing forebrain.
CC   -!- MISCELLANEOUS: Transport from dendrites to the nucleus is induced
CC       by NMDA receptor activation and results in a rapid stripping of
CC       synaptic contacts and a reduction of dendritic complexity (By
CC       similarity).
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AF266508; AAF74501.2; -; mRNA.
DR   EMBL; AJ278902; CAC27332.1; -; mRNA.
DR   EMBL; AK004986; BAB23721.1; -; mRNA.
DR   EMBL; AK019560; BAC25597.1; -; mRNA.
DR   EMBL; AK041478; BAC30955.1; -; mRNA.
DR   EMBL; AK045384; BAC32338.1; -; mRNA.
DR   EMBL; AK053402; BAC35375.1; -; mRNA.
DR   EMBL; AL732585; CAM17991.1; -; Genomic_DNA.
DR   EMBL; AL732585; CAM17992.1; -; Genomic_DNA.
DR   EMBL; BC006642; AAH06642.1; -; mRNA.
DR   IPI; IPI00119317; -.
DR   IPI; IPI00272207; -.
DR   IPI; IPI00404118; -.
DR   IPI; IPI00460021; -.
DR   IPI; IPI00607923; -.
DR   RefSeq; NP_001034475.1; NM_001039386.1.
DR   RefSeq; NP_001034476.1; NM_001039387.1.
DR   RefSeq; NP_001171125.1; NM_001177654.1.
DR   RefSeq; NP_001171126.1; NM_001177655.1.
DR   RefSeq; NP_064672.2; NM_020276.3.
DR   UniGene; Mm.42956; -.
DR   ProteinModelPortal; Q99NF2; -.
DR   DIP; DIP-46058N; -.
DR   STRING; Q99NF2; -.
DR   PhosphoSite; Q99NF2; -.
DR   PRIDE; Q99NF2; -.
DR   Ensembl; ENSMUST00000006646; ENSMUSP00000006646; ENSMUSG00000006476.
DR   Ensembl; ENSMUST00000074422; ENSMUSP00000074022; ENSMUSG00000006476.
DR   Ensembl; ENSMUST00000100334; ENSMUSP00000097908; ENSMUSG00000006476.
DR   Ensembl; ENSMUST00000102931; ENSMUSP00000099995; ENSMUSG00000006476.
DR   GeneID; 56876; -.
DR   KEGG; mmu:56876; -.
DR   UCSC; uc008iqa.1; mouse.
DR   UCSC; uc008iqb.1; mouse.
DR   UCSC; uc008iqc.1; mouse.
DR   UCSC; uc008iqe.1; mouse.
DR   CTD; 56876; -.
DR   MGI; MGI:1861755; Nelf.
DR   GeneTree; ENSGT00390000000459; -.
DR   HOGENOM; HBG445237; -.
DR   HOVERGEN; HBG080324; -.
DR   InParanoid; Q99NF2; -.
DR   OMA; CPGCAQL; -.
DR   OrthoDB; EOG4HDSTG; -.
DR   NextBio; 313453; -.
DR   ArrayExpress; Q99NF2; -.
DR   Bgee; Q99NF2; -.
DR   CleanEx; MM_NELF; -.
DR   Genevestigator; Q99NF2; -.
DR   GermOnline; ENSMUSG00000006476; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Lipoprotein; Membrane; Myristate;
KW   Nucleus; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    532       Nasal embryonic luteinizing hormone-
FT                                releasing hormone factor.
FT                                /FTId=PRO_0000096779.
FT   MOD_RES     290    290       Phosphoserine (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
FT   VAR_SEQ       1      1       M -> MRGAPVTM (in isoform 4).
FT                                /FTId=VSP_014764.
FT   VAR_SEQ     212    226       DDVPIRTWFPKENLF -> GEGLIFGPGQIPAGL (in
FT                                isoform 5).
FT                                /FTId=VSP_014765.
FT   VAR_SEQ     227    532       Missing (in isoform 5).
FT                                /FTId=VSP_014766.
FT   VAR_SEQ     238    239       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_014767.
FT   VAR_SEQ     240    262       Missing (in isoform 3).
FT                                /FTId=VSP_014768.
FT   VAR_SEQ     280    309       Missing (in isoform 4).
FT                                /FTId=VSP_014769.
FT   CONFLICT    248    248       K -> N (in Ref. 3; BAC35375).
SQ   SEQUENCE   532 AA;  60293 MW;  DE83212A82B90987 CRC64;
     MGAAASRRRA LRSEAMSSVA AKVRAARAFG EYLSQSHPEN RNGADHLLAD AYSGHDGSPE
     MQPAPQNKRR LSLVSNGRYE GSISDEAVSG KPAIEGPQPH VYTISREPAL LPGSEAEAIE
     LAVVKGRRQR ERHPHHHSQP LRASPGSSRE DISRPCQSWA GSRQGSKECP GCAQLVPGPS
     SRAFGLEQPP LPEAPGRHKK LERMYSVDGV SDDVPIRTWF PKENLFSFQT ATTTMQAISV
     FRGYAERKRR KRENDSASVI QRNFRKHLRM VGSRRVKAQT FAERRERSFS RSWSDPTPMK
     ADTSHDSRDS SDLQSSHCTL DEACEDLDWD TEKGLEAMAC NTEGFLPPKV MLISSKVPKA
     EYIPTIIRRD DPSIIPILYD HEHATFEDIL EEIEKKLNIY HKGAKIWKML IFCQGGPGHL
     YLLKNKVATF AKVEKEEDMI HFWKRLSRLM SKVNPEPNVI HIMGCYILGN PNGEKLFQNL
     RTLMTPYKVT FESPLELSAQ GKQMIETYFD FRLYRLWKSR QHSKLLDFDD VL
//
ID   ANR17_MOUSE             Reviewed;        2603 AA.
AC   Q99NH0; Q3TV99; Q5F4T7; Q6PG69; Q6ZQ66; Q8CHT4;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 2.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Ankyrin repeat domain-containing protein 17;
DE   AltName: Full=Ankyrin repeat domain-containing protein FOE;
DE   AltName: Full=Gene trap ankyrin repeat protein;
GN   Name=Ankrd17; Synonyms=Foe, Gtar, Kiaa0697;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Chen X., Shen J.C.-K.;
RT   "A novel ankyrin repeat domain-containing protein.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING,
RP   FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC   STRAIN=129/Sv;
RX   PubMed=11165478; DOI=10.1016/S0925-4773(00)00530-X;
RA   Watt A.J., Jones E.A., Ure J.M., Peddie D., Wilson D.I.,
RA   Forrester L.M.;
RT   "A gene trap integration provides an early in situ marker for hepatic
RT   specification of the foregut endoderm.";
RL   Mech. Dev. 100:205-215(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1034-1482 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1482-2603 (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1902-2603 (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=11740861; DOI=10.1006/excr.2001.5396;
RA   Jones E.A., Tosh D., Wilson D.I., Lindsay S., Forrester L.M.;
RT   "Hepatic differentiation of murine embryonic stem cells.";
RL   Exp. Cell Res. 272:15-22(2002).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2043, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1631, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2040, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2401, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Earliest specific in situ marker of hepatic
CC       differentiation during embryogenesis, useful for characterization
CC       of inductive events involved in hepatic specification.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Detected around the
CC       nucleolus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=The N-terminus of another isoform lacking the first 141
CC         amino acids is described in (PubMed:11165478);
CC       Name=1;
CC         IsoId=Q99NH0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99NH0-2; Sequence=VSP_028866, VSP_028867, VSP_028871;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q99NH0-3; Sequence=VSP_028868, VSP_028869, VSP_028870;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in fetal liver. Detected in
CC       adult liver cells, ovarian oocytes, seminiferous tubules of the
CC       testes and pelvic region of the kidney. It was not detected in
CC       heart, gut, lung, spleen and skeletal muscle.
CC   -!- DEVELOPMENTAL STAGE: Expressed at 8.0-8.5 dpc in the foregut
CC       endoderm and at 9.5 dpc in cells migrating into the septum
CC       transversum. At 10.5 dpc, highly expressed exclusively in the
CC       fetal liver. From 10.5 dpc, expressed in the developping liver
CC       throughout gestation and in neonates. At 17.5 dpc, detected in the
CC       dorsal root ganglia of the peripheral nervous system.
CC   -!- SIMILARITY: Contains 25 ANK repeats.
CC   -!- SIMILARITY: Contains 1 KH domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH39213.1; Type=Erroneous initiation;
CC       Sequence=BAC98003.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA;
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DR   EMBL; AF130371; AAQ13559.1; -; mRNA.
DR   EMBL; AC117578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC162171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY026253; AAK07672.1; -; mRNA.
DR   EMBL; AK160263; BAE35720.1; -; mRNA.
DR   EMBL; AK129193; BAC98003.1; ALT_SEQ; Transcribed_RNA.
DR   EMBL; BC039213; AAH39213.1; ALT_INIT; mRNA.
DR   EMBL; BC057195; AAH57195.1; -; mRNA.
DR   IPI; IPI00118794; -.
DR   IPI; IPI00272501; -.
DR   IPI; IPI00465535; -.
DR   RefSeq; NP_112148.2; NM_030886.2.
DR   UniGene; Mm.245522; -.
DR   UniGene; Mm.441490; -.
DR   HSSP; P16157; 1N11.
DR   ProteinModelPortal; Q99NH0; -.
DR   SMR; Q99NH0; 232-714, 1068-1404.
DR   IntAct; Q99NH0; 1.
DR   STRING; Q99NH0; -.
DR   PRIDE; Q99NH0; -.
DR   Ensembl; ENSMUST00000014421; ENSMUSP00000014421; ENSMUSG00000055204.
DR   Ensembl; ENSMUST00000081914; ENSMUSP00000080587; ENSMUSG00000055204.
DR   GeneID; 81702; -.
DR   KEGG; mmu:81702; -.
DR   CTD; 81702; -.
DR   MGI; MGI:1932101; Ankrd17.
DR   GeneTree; ENSGT00600000084171; -.
DR   HOGENOM; HBG403061; -.
DR   HOVERGEN; HBG071352; -.
DR   InParanoid; Q99NH0; -.
DR   OMA; KNPAPVQ; -.
DR   OrthoDB; EOG4K9BB8; -.
DR   NextBio; 350426; -.
DR   ArrayExpress; Q99NH0; -.
DR   Bgee; Q99NH0; -.
DR   CleanEx; MM_ANKRD17; -.
DR   Genevestigator; Q99NH0; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0007492; P:endoderm development; TAS:MGI.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR004088; KH_type_1.
DR   InterPro; IPR018111; KH_type_1_subgr.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 7.
DR   Pfam; PF00023; Ank; 18.
DR   Pfam; PF00013; KH_1; 1.
DR   SMART; SM00248; ANK; 25.
DR   SMART; SM00322; KH; 1.
DR   SUPFAM; SSF48403; ANK; 3.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 20.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ANK repeat; Coiled coil; Cytoplasm; Nucleus;
KW   Phosphoprotein; Repeat; RNA-binding.
FT   CHAIN         1   2603       Ankyrin repeat domain-containing protein
FT                                17.
FT                                /FTId=PRO_0000307918.
FT   REPEAT      229    258       ANK 1.
FT   REPEAT      262    291       ANK 2.
FT   REPEAT      296    325       ANK 3.
FT   REPEAT      329    358       ANK 4.
FT   REPEAT      362    391       ANK 5.
FT   REPEAT      396    425       ANK 6.
FT   REPEAT      429    458       ANK 7.
FT   REPEAT      462    491       ANK 8.
FT   REPEAT      495    524       ANK 9.
FT   REPEAT      529    558       ANK 10.
FT   REPEAT      559    588       ANK 11.
FT   REPEAT      592    621       ANK 12.
FT   REPEAT      625    654       ANK 13.
FT   REPEAT      659    688       ANK 14.
FT   REPEAT      692    721       ANK 15.
FT   REPEAT     1078   1107       ANK 16.
FT   REPEAT     1111   1140       ANK 17.
FT   REPEAT     1145   1174       ANK 18.
FT   REPEAT     1178   1207       ANK 19.
FT   REPEAT     1213   1242       ANK 20.
FT   REPEAT     1247   1276       ANK 21.
FT   REPEAT     1280   1309       ANK 22.
FT   REPEAT     1315   1344       ANK 23.
FT   REPEAT     1348   1377       ANK 24.
FT   REPEAT     1381   1410       ANK 25.
FT   DOMAIN     1721   1785       KH.
FT   COILED     1438   1522       Potential.
FT   COMPBIAS      4     40       Ala-rich.
FT   COMPBIAS     94    106       Gly-rich.
FT   COMPBIAS    854   1004       Gln-rich.
FT   COMPBIAS   1533   1537       Poly-Thr.
FT   COMPBIAS   1599   1696       Ser-rich.
FT   COMPBIAS   1946   2102       Ser-rich.
FT   MOD_RES     799    799       Phosphoserine (By similarity).
FT   MOD_RES    1329   1329       Phosphotyrosine (By similarity).
FT   MOD_RES    1453   1453       Phosphoserine (By similarity).
FT   MOD_RES    1631   1631       Phosphoserine.
FT   MOD_RES    1692   1692       Phosphoserine (By similarity).
FT   MOD_RES    1696   1696       Phosphoserine (By similarity).
FT   MOD_RES    1705   1705       Phosphoserine (By similarity).
FT   MOD_RES    2038   2038       Phosphoserine (By similarity).
FT   MOD_RES    2040   2040       Phosphoserine.
FT   MOD_RES    2041   2041       Phosphoserine (By similarity).
FT   MOD_RES    2043   2043       Phosphoserine.
FT   MOD_RES    2055   2055       Phosphoserine (By similarity).
FT   MOD_RES    2063   2063       Phosphoserine (By similarity).
FT   MOD_RES    2401   2401       Phosphoserine.
FT   VAR_SEQ       1    141       Missing (in isoform 2).
FT                                /FTId=VSP_028866.
FT   VAR_SEQ     774   1024       Missing (in isoform 2).
FT                                /FTId=VSP_028867.
FT   VAR_SEQ    1024   1024       Missing (in isoform 3).
FT                                /FTId=VSP_028868.
FT   VAR_SEQ    1597   1600       GESK -> VSFL (in isoform 3).
FT                                /FTId=VSP_028869.
FT   VAR_SEQ    1601   2603       Missing (in isoform 3).
FT                                /FTId=VSP_028870.
FT   VAR_SEQ    1723   2603       Missing (in isoform 2).
FT                                /FTId=VSP_028871.
FT   CONFLICT    347    347       K -> E (in Ref. 3; AAK07672).
FT   CONFLICT    357    357       E -> G (in Ref. 3; AAK07672).
FT   CONFLICT    908    908       F -> L (in Ref. 3; AAK07672).
SQ   SEQUENCE   2603 AA;  274213 MW;  246DAA0E473C3D55 CRC64;
     MEKATVPAAA EGEGSPPAAA AVAAPPAAAA AEVGGGARPA SSPRGMVRVC DLLLKKKPPQ
     QQQQQQPPHH KAKRNRTCRP PSSSESSSDS DNSGGGGGGG GGGGGGTSSN NSEEEEDDDD
     EEEEVSEVES FILDQDDLEN PMLETASKLL LSGTADGADL RTVDPETQAR LEALLEAAGI
     GKLSTADGKA FADPEVLRRL TSSVSCALDE AAAALTRMRA ESTANAGQSD NRSLAEACSE
     GDVNAVRKLL IEGRSVNEHT EEGESLLCLA CSAGYYELAQ VLLAMHANVE DRGIKGDITP
     LMAAANGGHV KIVKLLLAHK ADVNAQSSTG NTALTYACAG GYVDVVKVLL ESGASIEDHN
     ENGHTPLMEA GSAGHVEVAR LLLENGAGIN THSNEFKESA LTLACYKGHL EMVRFLLEAG
     ADQEHKTDEM HTALMEACMD GHVEVARLLL DSGAQVNMPA DSFESPLTLA ACGGHVELAA
     LLIERGASLE EVNDEGYTPL MEAAREGHEE MVALLLGQGA NINAQTEETQ ETALTLACCG
     GFLEVADFLI KAGADIELGC STPLMEAAQE GHLELVKYLL AAGANVHATT ATGDTALTYA
     CENGHTDVAD VLLQAGADLE HESEGGRTPL MKAARAGHVC TVQFLISKGA NVNRTTANND
     HTVLSLACAG GHLAVVELLL AHGADPTHRL KDGSTMLIEA AKGGHTSVVC YLLDYPNNLL
     AAPPPDVTQL TPPSHDLNRA PRVPVQALPM VVPPQEPDKP PANLAATLPV RSKAASKQKS
     NSHLPANSQD VQGYITNQSP ESIVEEAQGK LTELEQRIKE AIEKNAQLQS LELAHADQLT
     KEKIEELNKT REEQIQKKQK ILEELQKVER ELQLKTQQQL KKQYLEVKAQ RIQLQQQQQQ
     SCQHLGLFTS VGVGEQLSEG DYARLQQVDP VLLKDEPQQT AAQMGFAPIQ PLAMPQALPL
     ATGPLPPGSI ANLTELQGVI VGQPVLGQAQ LAGLGQGILT ETQQGLMVAS PAQTLNDTLD
     DIMAAVSGRA SAMSNTPTHS IAASVSQPQT PTPSPIISPS AMLPIYPAID IDAQTESNHD
     TALTLACAGG HEELVQTLLE RGASIEHRDK KGFTPLILAA TAGHVGVVEI LLDNGADIEA
     QSERTKDTPL SLACSGGRQE VVELLLARGA NKEHRNVSDY TPLSLAASGG YVNIIKILLN
     AGAEINSRTG SKLGISPLML AAMNGHTAAV KLLLDMGSDI NAQIETNRNT ALTLACFQGR
     TEVVSLLLDR KANVEHRAKT GLTPLMEAAS GGYAEVGRVL LDKGADVNAP PVPSSRDTAL
     TIAADKGHYK FCELLIGKGA HIDVRNKKGN TPLWLAANGG HLDVVQLLVQ ATADVDAADN
     RKITPLMAAF RKGHVKVVRY LVKEVNQFPS DSECMRYIAT ITDKEMLKKC HLCMESIVQA
     KDRQAAEANK NASILLEELD LEKLREESRR LALAAKREKR KEKRRKKKEE QRRKLEEIEA
     KNKENFELQA AQEKEKLKVE EEPEVLTEPP SATTTTTIGI SATWTTLAGS HGKRNNTITT
     TSSKRKNRKN KITPENVQII FDDPLPISYS QPEKVNGESK SSSTSESGDS DNMRISSCSD
     ESSNSNSSRK SNNHASAVVT TTMASKKQPS VLVTFPKEER KSVSGKASIK LSETVNEGTS
     NSLSTCTKSG PSPLSSPNGK LTVASPKRGP KREEGWKEVV RRSKKVSVPS TVISRVIGRG
     GCNINAIREC TGAHIDIDKQ KDKTGDRIIT IRGGTESTRQ ATQLINALIK DPDKEIDELI
     PKNRLKSSTA NSKIGSSAPT TTAANSSLMG IKMTTVALSS TSQTATALTV PAISSASTHK
     TIKNPVNNVR PGFPVSLPLA YPPPQFAHAL LAAQTFQQIR PPRLPMTHFG GTFPPAQSTW
     GPFPVRPLSP ARATNSPKPH MVPRHSNQNS SGSQVNSAGS LTSSPTTTAS SSASAVPGTT
     SNGSPSSPSV RRQLFVTVVK TSNATTTTVT TTASNNSTAP TNATYPMPTA KEHYPVSSPS
     SPSPPAQPGG VSRNSPLDCG SASPNKGASA SEQEASSPPV VEPANSRPPH SSSSSGSSSG
     HSTQQQPPGS VPQEPRPPLQ QSQVPSPDVR MTVPPTATSS APVAVPSTAP VTYPMPQTQM
     GCSQPPKMEA PAIRPPSHAT AAPHKTPAPV QSSSASVLNV NHIKRPHSVP SSVQLPSTLS
     TQSACQNSVH PANKPVAPNF SAPLPFGPFS TLFENNPTNA HAFWGGPVVS SQSTPESMLS
     GKSSYLPNSD PLHQSDTSKA PGFRPPLQRP APSPSGIVNM DTPYGSVTPS STHLGNFASS
     LSGGQMYGPG APLGGAPLGG APTAANFNRQ HFSPLSLLTP CSSASNESPA QSVSSGVRAP
     SPAPSSVPLG SEKPSSVSQD RKVPVPIGTE RSARIRQTGT SAPSVIGSNL STSVGHSGIW
     SFEGIGGNQD KVDWCNPGMG NPMIHRPMSD PGVFSQHQAM ERDSTGIVTP SGTFHQHVPA
     GYMDFPKVGS MPFSVYGNAM LPPVAPIADG AGGPIFNGPH SAEPSWNSLI KMVSSSTENN
     GPQTVWTGPW APHMNSVHMN QLG
//
ID   HPBP1_MOUSE             Reviewed;         357 AA.
AC   Q99P31; Q9CYV8;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Hsp70-binding protein 1;
DE            Short=HspBP1;
DE   AltName: Full=Heat shock protein-binding protein 1;
DE   AltName: Full=Hsp70-interacting protein 1;
GN   Name=Hspbp1; Synonyms=Hspbp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Mammary gland;
RA   Guerriero V. Jr., Raynes D.A.;
RT   "Mouse HspBP sequence.";
RL   Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Embryo, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Inhibits HSPA1A chaperone activity by changing the
CC       conformation of the ATP-binding domain of HSPA1A and interfering
CC       with ATP binding. Interferes with ubiquitination mediated by STUB1
CC       and inhibits chaperone-assisted degradation of target proteins (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with the ATP-binding domain of HSPA1A. Detected
CC       in a ternary complex containing STUB1, HSPA1A and HSPBP1 (By
CC       similarity).
CC   -!- SIMILARITY: Contains 4 ARM repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB28756.1; Type=Frameshift; Positions=7;
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DR   EMBL; AF338351; AAK11657.1; -; mRNA.
DR   EMBL; AK013263; BAB28756.1; ALT_FRAME; mRNA.
DR   EMBL; AK088469; BAC40373.1; -; mRNA.
DR   EMBL; BC014758; AAH14758.1; -; mRNA.
DR   IPI; IPI00120257; -.
DR   RefSeq; NP_077134.1; NM_024172.3.
DR   UniGene; Mm.6803; -.
DR   ProteinModelPortal; Q99P31; -.
DR   SMR; Q99P31; 82-348.
DR   STRING; Q99P31; -.
DR   PhosphoSite; Q99P31; -.
DR   PRIDE; Q99P31; -.
DR   Ensembl; ENSMUST00000079970; ENSMUSP00000078886; ENSMUSG00000063802.
DR   GeneID; 66245; -.
DR   KEGG; mmu:66245; -.
DR   UCSC; uc009eyc.1; mouse.
DR   CTD; 66245; -.
DR   MGI; MGI:1913495; Hspbp1.
DR   eggNOG; maNOG16787; -.
DR   GeneTree; ENSGT00510000048482; -.
DR   HOGENOM; HBG717738; -.
DR   HOVERGEN; HBG053282; -.
DR   InParanoid; Q99P31; -.
DR   OMA; LQQHEEY; -.
DR   OrthoDB; EOG4ZKJN2; -.
DR   PhylomeDB; Q99P31; -.
DR   NextBio; 321075; -.
DR   ArrayExpress; Q99P31; -.
DR   Bgee; Q99P31; -.
DR   CleanEx; MM_1500019G21RIK; -.
DR   Genevestigator; Q99P31; -.
DR   GermOnline; ENSMUSG00000063802; Mus musculus.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50176; ARM_REPEAT; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1    357       Hsp70-binding protein 1.
FT                                /FTId=PRO_0000084037.
FT   REPEAT      130    172       ARM 1.
FT   REPEAT      175    215       ARM 2.
FT   REPEAT      218    257       ARM 3.
FT   REPEAT      260    299       ARM 4.
FT   MOD_RES     349    349       Phosphoserine (By similarity).
FT   MOD_RES     354    354       Phosphoserine (By similarity).
FT   CONFLICT    109    109       A -> L (in Ref. 2; BAB28756).
SQ   SEQUENCE   357 AA;  39167 MW;  6D6BB583730E3474 CRC64;
     MADKGSGGSR LPLALPPASQ GCSSGGSGSS AGGSGNPRPP RNLQGLLQMA ITAGSQEPDP
     PPEPMSEERR QWLQEAMSAA FRGQREEVEQ MKNCLRVLSQ ATPAMAGEAE LATDQQEREG
     ALELLADLCE NMDNAADFCQ LSGMHLLVGR YLEAGAAGLR WRAAQLIGTC SQNVAAIQEQ
     VLGLGALRKL LRLLDRDSCD TVRVKALFAI SCLVREQEAG LLQFLRLDGF SVLMRAMQQQ
     VQKLKVKSAF LLQNLLVGHP EHKGTLCSMG MVQQLVALVR TEHSPFHEHV LGALCSLVTD
     FPQGVRECRE PELGLEELLR HRCQLLQQRE EYQEELEFCE KLLQTCFSSP TDDSMDR
//
ID   RTN4_MOUSE              Reviewed;        1162 AA.
AC   Q99P72; Q5DTK9; Q7TNB7; Q80W95; Q8BGK7; Q8BGM9; Q8K290; Q8K3G8;
AC   Q9CTE3;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Reticulon-4;
DE   AltName: Full=Neurite outgrowth inhibitor;
DE            Short=Nogo protein;
GN   Name=Rtn4; Synonyms=Kiaa0886, Nogo;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=129/Sv;
RX   MEDLINE=22376540; PubMed=12488097; DOI=10.1016/S0022-2836(02)01179-8;
RA   Oertle T., Huber C., van der Putten H., Schwab M.E.;
RT   "Genomic structure and functional characterisation of the promoters of
RT   human and mouse nogo/rtn4.";
RL   J. Mol. Biol. 325:299-323(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   TISSUE=Adipocyte;
RA   Coulson A.C., Craggs P.D., Morris N.J.;
RT   "Mouse vp20/RTN4C cDNA.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c;
RA   Jin W., Long M., Li R., Ju G.;
RT   "Cloning and expression of the mouse Nogo-A protein.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 585-1162.
RA   Tozaki H., Hirata T.;
RT   "The partial sequence of mouse nogo-A cDNA clone#4109.";
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   PROTEIN SEQUENCE OF 975-982; 1061-1074 AND 1079-1090, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1133-1162.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [10]
RP   INTERACTION WITH RTN4IP1.
RX   MEDLINE=22061975; PubMed=12067236;
RX   DOI=10.1046/j.1471-4159.2002.00788.x;
RA   Hu W.-H., Hausmann O.N., Yan M.-S., Walters W.M., Wong P.K.Y.,
RA   Bethea J.R.;
RT   "Identification and characterization of a novel Nogo-interacting
RT   mitochondrial protein (NIMP).";
RL   J. Neurochem. 81:36-45(2002).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-690; SER-836
RP   AND SER-839, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145; SER-165; THR-171;
RP   SER-426; SER-857 AND TYR-861, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-105 AND SER-165,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145 AND SER-344, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-105, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [17]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX   PubMed=20093372; DOI=10.1093/cercor/bhp307;
RA   Mathis C., Schroeter A., Thallmair M., Schwab M.E.;
RT   "Nogo-a regulates neural precursor migration in the embryonic mouse
RT   cortex.";
RL   Cereb. Cortex 20:2380-2390(2010).
RN   [18]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20573699; DOI=10.1242/dev.048371;
RA   Petrinovic M.M., Duncan C.S., Bourikas D., Weinman O., Montani L.,
RA   Schroeter A., Maerki D., Sommer L., Stoeckli E.T., Schwab M.E.;
RT   "Neuronal Nogo-A regulates neurite fasciculation, branching and
RT   extension in the developing nervous system.";
RL   Development 137:2539-2550(2010).
CC   -!- FUNCTION: Developmental neurite growth regulatory factor with a
CC       role as a negative regulator of axon-axon adhesion and growth, and
CC       as a facilitator of neurite branching. Regulates neurite
CC       fasciculation, branching and extension in the developing nervous
CC       system. Involved in down-regulation of growth, stabilization of
CC       wiring and restriction of plasticity in the adult CNS. Regulates
CC       the radial migration of cortical neurons via an RTN4R-LINGO1
CC       containing receptor complex. May inhibit BACE1 activity and
CC       amyloid precursor protein processing.
CC   -!- SUBUNIT: Binds to RTN4R. Interacts with Bcl-xl and Bcl-2.
CC       Interacts in trans with CNTNAP1. Interacts with ATL1 (By
CC       similarity). Interacts with RTN4IP1.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity). Note=Anchored to the membrane of
CC       the endoplasmic reticulum through 2 putative transmembrane domains
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q99P72-2; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99P72-3; Sequence=VSP_018089, VSP_018090;
CC       Name=3;
CC         IsoId=Q99P72-1; Sequence=VSP_018088, VSP_018091;
CC   -!- DEVELOPMENTAL STAGE: Expressed in radial glial cells, migrating
CC       postmitotic as well as postmigratory neurons of the embryonic
CC       cortex.
CC   -!- DOMAIN: Three regions, residues 59-172, 544-725 and the loop 66
CC       amino acids, between the two transmembrane domains, known as Nogo-
CC       66 loop, appear to be responsible for the inhibitory effect on
CC       neurite outgrowth and the spreading of neurons. This Nogo-66 loop,
CC       mediates also the binding of RTN4 to its receptor (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Embryos show defects in the development of
CC       fore- and hindlimb innervation. Increased fasciculation and
CC       decreased branching of nerves innervating fore- and hindlimbs
CC       seen. Disturbances of the radial migration pattern of neuronal
CC       precursor cells seen in embryonic cortex.
CC   -!- SIMILARITY: Contains 1 reticulon domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH32192.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BC056373; Type=Erroneous termination; Positions=721; Note=Translated as Glu;
CC   -!- WEB RESOURCE: Name=Protein Spotlight; Note=Nerve regrowth: nipped
CC       by a no-go - Issue 69 of April 2006;
CC       URL="http://www.expasy.org/spotlight/back_issues/sptlt069.shtml";
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DR   EMBL; AY102280; AAM73502.1; -; mRNA.
DR   EMBL; AY102284; AAM73506.1; -; mRNA.
DR   EMBL; AY102286; AAM73507.1; -; Genomic_DNA.
DR   EMBL; AY102286; AAM73511.1; -; Genomic_DNA.
DR   EMBL; AF326337; AAK08076.1; -; mRNA.
DR   EMBL; AY114152; AAM77068.1; -; mRNA.
DR   EMBL; AK220511; BAD90301.1; -; mRNA.
DR   EMBL; AL929371; CAI24273.1; -; Genomic_DNA.
DR   EMBL; AL929371; CAI24274.1; -; Genomic_DNA.
DR   EMBL; BC032192; AAH32192.1; ALT_INIT; mRNA.
DR   EMBL; BC056373; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AB073672; BAC75974.1; -; mRNA.
DR   EMBL; AK003859; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00120415; -.
DR   IPI; IPI00270767; -.
DR   IPI; IPI00469392; -.
DR   RefSeq; NP_077188.1; NM_024226.4.
DR   RefSeq; NP_918940.1; NM_194051.3.
DR   RefSeq; NP_918943.1; NM_194054.3.
DR   UniGene; Mm.192580; -.
DR   UniGene; Mm.440639; -.
DR   UniGene; Mm.472973; -.
DR   PDB; 2KO2; NMR; -; A=1025-1090.
DR   PDBsum; 2KO2; -.
DR   ProteinModelPortal; Q99P72; -.
DR   SMR; Q99P72; 1025-1084.
DR   MINT; MINT-188330; -.
DR   STRING; Q99P72; -.
DR   PhosphoSite; Q99P72; -.
DR   PRIDE; Q99P72; -.
DR   Ensembl; ENSMUST00000060992; ENSMUSP00000053754; ENSMUSG00000020458.
DR   Ensembl; ENSMUST00000102843; ENSMUSP00000099907; ENSMUSG00000020458.
DR   GeneID; 68585; -.
DR   KEGG; mmu:68585; -.
DR   UCSC; uc007ihk.1; mouse.
DR   UCSC; uc007ihn.1; mouse.
DR   UCSC; uc007iho.1; mouse.
DR   CTD; 68585; -.
DR   MGI; MGI:1915835; Rtn4.
DR   eggNOG; roNOG06216; -.
DR   GeneTree; ENSGT00390000009934; -.
DR   HOVERGEN; HBG023134; -.
DR   InParanoid; Q99P72; -.
DR   OMA; VIHSSAE; -.
DR   OrthoDB; EOG4XH010; -.
DR   NextBio; 327502; -.
DR   ArrayExpress; Q99P72; -.
DR   Bgee; Q99P72; -.
DR   CleanEx; MM_RTN4; -.
DR   Genevestigator; Q99P72; -.
DR   GermOnline; ENSMUSG00000020458; Mus musculus.
DR   GO; GO:0030176; C:integral to endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR   GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR   GO; GO:0007413; P:axonal fasciculation; IMP:UniProtKB.
DR   GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; IMP:MGI.
DR   GO; GO:0021801; P:cerebral cortex radial glia guided migration; IMP:UniProtKB.
DR   GO; GO:0019987; P:negative regulation of anti-apoptosis; ISS:UniProtKB.
DR   GO; GO:0030517; P:negative regulation of axon extension; IMP:UniProtKB.
DR   GO; GO:2000172; P:regulation of branching morphogenesis of a nerve; IMP:UniProtKB.
DR   InterPro; IPR003388; Reticulon.
DR   PANTHER; PTHR10994; Reticulon; 1.
DR   Pfam; PF02453; Reticulon; 1.
DR   PROSITE; PS50845; RETICULON; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing;
KW   Direct protein sequencing; Endoplasmic reticulum; Membrane;
KW   Neurogenesis; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1   1162       Reticulon-4.
FT                                /FTId=PRO_0000168166.
FT   TOPO_DOM      1    988       Cytoplasmic (Potential).
FT   TRANSMEM    989   1009       Helical; (Potential).
FT   TOPO_DOM   1010   1078       Lumenal (Potential).
FT   TRANSMEM   1079   1099       Helical; (Potential).
FT   TOPO_DOM   1100   1162       Cytoplasmic (Potential).
FT   DOMAIN      975   1162       Reticulon.
FT   COMPBIAS     31     57       Glu-rich.
FT   COMPBIAS     68    160       Pro-rich.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES       7      7       Phosphoserine (By similarity).
FT   MOD_RES      11     11       Phosphoserine (By similarity).
FT   MOD_RES      12     12       Phosphoserine (By similarity).
FT   MOD_RES      16     16       Phosphoserine.
FT   MOD_RES     105    105       Phosphoserine.
FT   MOD_RES     145    145       Phosphoserine.
FT   MOD_RES     165    165       Phosphoserine.
FT   MOD_RES     167    167       Phosphoserine (By similarity).
FT   MOD_RES     171    171       Phosphothreonine.
FT   MOD_RES     344    344       Phosphoserine.
FT   MOD_RES     426    426       Phosphoserine.
FT   MOD_RES     690    690       Phosphoserine.
FT   MOD_RES     836    836       Phosphoserine.
FT   MOD_RES     839    839       Phosphoserine.
FT   MOD_RES     857    857       Phosphoserine.
FT   MOD_RES     861    861       Phosphotyrosine.
FT   MOD_RES    1074   1074       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1    963       Missing (in isoform 3).
FT                                /FTId=VSP_018088.
FT   VAR_SEQ       1    116       Missing (in isoform 2).
FT                                /FTId=VSP_018089.
FT   VAR_SEQ     117    169       LPPAAAVLPSKLPEDDEPPARPPAPAGASPLAEPAAPPSTP
FT                                AAPKRRGSGSVD -> MAPPLAGGGQKGGAASEAWVPSLFV
FT                                GVSGSTCTAAKSLVPIPARSSRLSAARN (in isoform
FT                                2).
FT                                /FTId=VSP_018090.
FT   VAR_SEQ     964    974       AVLSAELNKTS -> MDDQKKRWKDK (in isoform
FT                                3).
FT                                /FTId=VSP_018091.
FT   CONFLICT      4      4       I -> V (in Ref. 4; BAD90301).
FT   CONFLICT     16     16       S -> R (in Ref. 4; BAD90301).
FT   CONFLICT     21     21       P -> L (in Ref. 4; BAD90301).
FT   CONFLICT     67     67       A -> V (in Ref. 3; AAM77068).
FT   CONFLICT    413    413       G -> S (in Ref. 3; AAM77068 and 4;
FT                                BAD90301).
FT   CONFLICT    429    429       R -> S (in Ref. 3; AAM77068 and 4;
FT                                BAD90301).
FT   CONFLICT    448    448       S -> T (in Ref. 3; AAM77068 and 4;
FT                                BAD90301).
FT   CONFLICT    487    490       KTSP -> HASA (in Ref. 6; AAH32192).
FT   CONFLICT    651    651       S -> A (in Ref. 3; AAM77068, 6; AAH32192
FT                                and 4; BAD90301).
FT   CONFLICT    665    665       A -> V (in Ref. 4; BAD90301).
FT   CONFLICT    692    692       E -> G (in Ref. 3; AAM77068 and 7;
FT                                BAC75974).
FT   CONFLICT    733    733       E -> D (in Ref. 4; BAD90301).
FT   CONFLICT    772    772       V -> L (in Ref. 4; BAD90301).
FT   CONFLICT    916    916       S -> F (in Ref. 7; BAC75974).
FT   CONFLICT    990    990       V -> VY (in Ref. 3; AAM77068).
FT   HELIX      1031   1035
FT   HELIX      1044   1053
FT   TURN       1054   1056
FT   HELIX      1057   1063
FT   HELIX      1069   1082
FT   HELIX      1087   1089
SQ   SEQUENCE   1162 AA;  126613 MW;  855697FBEE11781F CRC64;
     MEDIDQSSLV SSSADSPPRP PPAFKYQFVT EPEDEEDEED EEEEEDDEDL EELEVLERKP
     AAGLSAAPVP PAAAPLLDFS SDSVPPAPRG PLPAAPPTAP ERQPSWERSP AASAPSLPPA
     AAVLPSKLPE DDEPPARPPA PAGASPLAEP AAPPSTPAAP KRRGSGSVDE TLFALPAASE
     PVIPSSAEKI MDLKEQPGNT VSSGQEDFPS VLFETAASLP SLSPLSTVSF KEHGYLGNLS
     AVASTEGTIE ETLNEASREL PERATNPFVN RESAEFSVLE YSEMGSSFNG SPKGESAMLV
     ENTKEEVIVR SKDKEDLVCS AALHNPQESP ATLTKVVKED GVMSPEKTMD IFNEMKMSVV
     APVREEYADF KPFEQAWEVK DTYEGSRDVL AARANMESKV DKKCFEDSLE QKGHGKDSES
     RNENASFPRT PELVKDGSRA YITCDSFSSA TESTAANIFP VLEDHTSENK TDEKKIEERK
     AQIITEKTSP KTSNPFLVAI HDSEADYVTT DNLSKVTEAV VATMPEGLTP DLVQEACESE
     LNEATGTKIA YETKVDLVQT SEAIQESIYP TAQLCPSFEE AEATPSPVLP DIVMEAPLNS
     LLPSTGASVA QPSASPLEVP SPVSYDGIKL EPENPPPYEE AMSVALKTSD SKEEIKEPES
     FNAAAQEAEA PYISIACDLI KETKLSTEPS PEFSNYSEIA KFEKSVPDHC ELVDDSSPES
     EPVDLFSDDS IPEVPQTQEE AVMLMKESLT EVSETVTQHK HKERLSASPQ EVGKPYLESF
     QPNLHITKDA ASNEIPTLTK KETISLQMEE FNTAIYSNDD LLSSKEDKMK ESETFSDSSP
     IEIIDEFPTF VSAKDDSPKE YTDLEVSNKS EIANVQSGAN SLPCSELPCD LSFKNTYPKD
     EAHVSDEFSK SRSSVSKVPL LLPNVSALES QIEMGNIVKP KVLTKEAEEK LPSDTEKEDR
     SLTAVLSAEL NKTSVVDLLY WRDIKKTGVV FGASLFLLLS LTVFSIVSVT AYIALALLSV
     TISFRIYKGV IQAIQKSDEG HPFRAYLESE VAISEELVQK YSNSALGHVN STIKELRRLF
     LVDDLVDSLK FAVLMWVFTY VGALFNGLTL LILALISLFS IPVIYERHQA QIDHYLGLAN
     KSVKDAMAKI QAKIPGLKRK AE
//
ID   NCKX3_MOUSE             Reviewed;         645 AA.
AC   Q99PD7; Q99JR2; Q99PD8;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2001, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Sodium/potassium/calcium exchanger 3;
DE   AltName: Full=Na(+)/K(+)/Ca(2+)-exchange protein 3;
DE   Flags: Precursor;
GN   Name=Slc24a3; Synonyms=Nckx3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=129/SvJ, and CD-1; TISSUE=Brain, and Embryonic stem cell;
RX   MEDLINE=21303617; PubMed=11294880; DOI=10.1074/jbc.M102314200;
RA   Kraev A., Quednau B.D., Leach S., Li X.-F., Dong H., Winkfein R.,
RA   Perizzolo M., Cai X., Yang R., Philipson K.D., Lytton J.;
RT   "Molecular cloning of a third member of the potassium-dependent
RT   sodium-calcium exchanger gene family, NCKX3.";
RL   J. Biol. Chem. 276:23161-23172(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 323-645.
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Transports 1 Ca(2+) and 1 K(+) in exchange for 4 Na(+)
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Abundant in the brain. Highest levels found in
CC       selected thalamic nuclei, hippocampal CA1 neurons and in layer IV
CC       of the cerebral cortex.
CC   -!- SIMILARITY: Belongs to the sodium/potassium/calcium exchanger
CC       family. SLC24A subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF314821; AAG60049.1; -; mRNA.
DR   EMBL; AF314822; AAG60050.1; -; Genomic_DNA.
DR   EMBL; BC005742; AAH05742.1; -; mRNA.
DR   IPI; IPI00120928; -.
DR   UniGene; Mm.217171; -.
DR   STRING; Q99PD7; -.
DR   PhosphoSite; Q99PD7; -.
DR   PRIDE; Q99PD7; -.
DR   Ensembl; ENSMUST00000110007; ENSMUSP00000105634; ENSMUSG00000063873.
DR   MGI; MGI:2137513; Slc24a3.
DR   GeneTree; ENSGT00560000076876; -.
DR   HOGENOM; HBG444187; -.
DR   HOVERGEN; HBG054881; -.
DR   InParanoid; Q99PD7; -.
DR   OrthoDB; EOG4TTGHN; -.
DR   ArrayExpress; Q99PD7; -.
DR   Bgee; Q99PD7; -.
DR   Genevestigator; Q99PD7; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; TAS:MGI.
DR   GO; GO:0008273; F:calcium, potassium:sodium antiporter activity; IDA:MGI.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; TAS:MGI.
DR   InterPro; IPR004481; K-dep_Na/Ca-exchanger-like.
DR   InterPro; IPR004837; NaCa_Exmemb.
DR   Pfam; PF01699; Na_Ca_ex; 2.
DR   TIGRFAMs; TIGR00367; K_NaCaexchng; 1.
PE   2: Evidence at transcript level;
KW   Antiport; Calcium; Calcium transport; Glycoprotein; Ion transport;
KW   Membrane; Potassium; Potassium transport; Repeat; Signal; Sodium;
KW   Sodium transport; Symport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL        1     43       Potential.
FT   CHAIN        44    645       Sodium/potassium/calcium exchanger 3.
FT                                /FTId=PRO_0000019371.
FT   TOPO_DOM     44    106       Extracellular (Potential).
FT   TRANSMEM    107    127       Helical; (Potential).
FT   TOPO_DOM    128    151       Cytoplasmic (Potential).
FT   TRANSMEM    152    172       Helical; (Potential).
FT   TOPO_DOM    173    181       Extracellular (Potential).
FT   TRANSMEM    182    202       Helical; (Potential).
FT   TOPO_DOM    203    209       Cytoplasmic (Potential).
FT   TRANSMEM    210    230       Helical; (Potential).
FT   TOPO_DOM    231    234       Extracellular (Potential).
FT   TRANSMEM    235    255       Helical; (Potential).
FT   TOPO_DOM    256    486       Cytoplasmic (Potential).
FT   TRANSMEM    487    507       Helical; (Potential).
FT   TOPO_DOM    508    512       Extracellular (Potential).
FT   TRANSMEM    513    533       Helical; (Potential).
FT   TOPO_DOM    534    551       Cytoplasmic (Potential).
FT   TRANSMEM    552    572       Helical; (Potential).
FT   TOPO_DOM    573    582       Extracellular (Potential).
FT   TRANSMEM    583    603       Helical; (Potential).
FT   TOPO_DOM    604    617       Cytoplasmic (Potential).
FT   TRANSMEM    618    638       Helical; (Potential).
FT   TOPO_DOM    639    645       Extracellular (Potential).
FT   REPEAT      148    188       Alpha-1.
FT   REPEAT      520    551       Alpha-2.
FT   COMPBIAS    424    430       Poly-Glu.
FT   CARBOHYD     70     70       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     85     85       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   645 AA;  71915 MW;  C62DEB6CB4A01C96 CRC64;
     MPPPGDQDCA RRRSRRRRRD LLLSQLCFLA SVALLLWSLS SLREQKELDL MDLIGEDRKW
     MVGRKLMQVN DTLTSEDAGL QSSKNCTEPA LHEFPRDIFS NEDRRQGAVV LHVLCAMYMF
     YALAIVCDDF FVPSLEKICE RLHLSEDVAG ATFMAAGSSA PELFTSVIGV FITKGDVGVG
     TIVGSAVFNI LCIIGVCGLF AGQVVALSSW CLLRDSIYYT LSVVALIVFI YDEKVSWWES
     LVLVLMYLIY IVIMKYNACI HQCFERRTKG AGNMVNGLAN NAEIDDSSNC DATVVLLKKA
     NFHRKASVIM VDELLSAYPH QLSFSEAGLR IMITSHFPPK TRLSMASRML INERQRLINS
     RAYTNGESEV AIKIPIKHTV ENGTGPSSAP DRGVNGTRRD DIVAETDNET ENENEDNENN
     ESDEEEEEDE DDDEGPYTPF DPPSGKLETV KWAFTWPLSF VLYFTVPNCN KPHWEKWFMV
     TFASSTLWIA AFSYMMVWMV TIIGYTLGIP DVIMGITFLA AGTSVPDCMA SLIVARQGMG
     DMAVSNSIGS NVFDILIGLG LPWALQTLAV DYGSYIRLNS RGLIYSVGLL LASVFVTVFG
     VHLNKWQLDK KLGCGCLFLY GVFLCFSIMT EFNVFTFVNL PMCGD
//
ID   OGFR_MOUSE              Reviewed;         633 AA.
AC   Q99PG2; A2ACT6; Q99L33;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Opioid growth factor receptor;
DE            Short=OGFr;
DE   AltName: Full=Zeta-type opioid receptor;
GN   Name=Ogfr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6;
RX   PubMed=11113537; DOI=10.1016/S0169-328X(00)00232-1;
RA   Zagon I.S., Verderame M.F., Zimmer W.E., McLaughlin P.J.;
RT   "Molecular characterization and distribution of the opioid growth
RT   factor receptor (OGFr) in mouse.";
RL   Brain Res. Mol. Brain Res. 84:106-114(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Receptor for opioid growth factor (OGF), also known as
CC       Met-enkephalin. Seems to be involved in growth regulation (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=The OGF/OGFR complex is probably translocated to
CC       the nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99PG2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99PG2-2; Sequence=VSP_004061, VSP_004062;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined, including
CC       brain, heart, lung, liver, kidney and skeletal muscle.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the opioid growth factor receptor family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF303894; AAK01353.1; -; mRNA.
DR   EMBL; AL669926; CAM26816.1; -; Genomic_DNA.
DR   EMBL; BC003875; AAH03875.1; -; mRNA.
DR   IPI; IPI00121018; -.
DR   IPI; IPI00230639; -.
DR   RefSeq; NP_113550.3; NM_031373.3.
DR   UniGene; Mm.250418; -.
DR   UniGene; Mm.481733; -.
DR   ProteinModelPortal; Q99PG2; -.
DR   STRING; Q99PG2; -.
DR   PhosphoSite; Q99PG2; -.
DR   PRIDE; Q99PG2; -.
DR   Ensembl; ENSMUST00000029087; ENSMUSP00000029087; ENSMUSG00000049401.
DR   Ensembl; ENSMUST00000078560; ENSMUSP00000077637; ENSMUSG00000049401.
DR   GeneID; 72075; -.
DR   KEGG; mmu:72075; -.
DR   UCSC; uc008ojj.1; mouse.
DR   UCSC; uc008ojk.1; mouse.
DR   CTD; 72075; -.
DR   MGI; MGI:1919325; Ogfr.
DR   GeneTree; ENSGT00390000018730; -.
DR   HOGENOM; HBG126096; -.
DR   HOVERGEN; HBG024736; -.
DR   InParanoid; Q99PG2; -.
DR   OMA; PEDPKSQ; -.
DR   OrthoDB; EOG4FBHTH; -.
DR   PhylomeDB; Q99PG2; -.
DR   ArrayExpress; Q99PG2; -.
DR   Bgee; Q99PG2; -.
DR   CleanEx; MM_OGFR; -.
DR   Genevestigator; Q99PG2; -.
DR   GermOnline; ENSMUSG00000049401; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   InterPro; IPR006757; OGF_rcpt.
DR   Pfam; PF04664; OGFr_N; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Cytoplasm; Growth regulation;
KW   Nucleus; Phosphoprotein; Receptor; Repeat.
FT   CHAIN         1    633       Opioid growth factor receptor.
FT                                /FTId=PRO_0000058031.
FT   REPEAT      467    475       1.
FT   REPEAT      476    484       2.
FT   REPEAT      485    493       3.
FT   REPEAT      494    502       4.
FT   REPEAT      503    511       5.
FT   REPEAT      512    520       6.
FT   REPEAT      521    529       7.
FT   REPEAT      530    538       8.
FT   REPEAT      539    547       9.
FT   REPEAT      548    556       10.
FT   REPEAT      557    565       11.
FT   REPEAT      566    574       12.
FT   REPEAT      575    583       13.
FT   REPEAT      584    592       14.
FT   REGION      467    592       14 X approximate tandem repeats.
FT   MOTIF       257    286       Bipartite nuclear localization signal
FT                                (Potential).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     337    337       Phosphoserine (By similarity).
FT   MOD_RES     340    340       Phosphoserine (By similarity).
FT   MOD_RES     361    361       Phosphoserine (By similarity).
FT   MOD_RES     403    403       Phosphoserine (By similarity).
FT   MOD_RES     452    452       Phosphoserine (By similarity).
FT   VAR_SEQ     504    512       Missing (in isoform 2).
FT                                /FTId=VSP_004061.
FT   VAR_SEQ     563    589       Missing (in isoform 2).
FT                                /FTId=VSP_004062.
FT   CONFLICT     19     19       E -> D (in Ref. 3; AAH03875).
FT   CONFLICT    317    318       GR -> SW (in Ref. 3; AAH03875).
SQ   SEQUENCE   633 AA;  70679 MW;  0B18933C0A0C891F CRC64;
     MDDPECDSTW EDESEEDGED GQADDTTDED TGDDDGDAEE ARPSLFQSRM TRYRNWRAMQ
     DMQRYRHNYP DLTDQDCNGD MCNLSFYKNE ICFQPNGFLI EDILQNWKDN YDLLEENHSY
     IQWLFPLREP GVNWHAKPLT LKEVEAFKSS KEVRERLVRA YELMLGFYGI QLEDRNTGAV
     CRAQNFQPRF HNLNSHSHNN LRITRILKSL GELGLEHYQA PLVRFFLEET LVQHKLPSVR
     QSALDYFLFA VRCRHQRREL VHFAWEHFKP RREFVWGPRD KLRRFRPQTI SRPLMGLGQA
     DKDEGPGDPS QEAGTQGRTC GSGRDLSGDS GTAEDLSLLS AKPQDVGTLD GDQRHEAKSP
     SPKESKKRKL EGNRQEQVPG EPDPQGVSEV EKIALNLEGC ALSPTSQEPR EAEQPCLVAR
     VANEVRKRRK VEEGAEGDGV ASNTQVQASA LSPTPSECPE SQKDGNGPED PKSQVGPEDP
     KSQVGPEDPK SQVGPEDPKS QVGPEDPKGQ VEPEDPKGQV GPEDPKGQVG PEDPKGQVGP
     EDPKSQVGPE DPKSQVEPED PKSQVEPEDP KSQVEPEDPK SQVGPEDPQS QVGPEQAASK
     SLGEDPDSDT TGTSMSESEE LARIEASVEP PKP
//
ID   LPIN2_MOUSE             Reviewed;         893 AA.
AC   Q99PI5; Q8C357; Q8C7I8; Q8CC85; Q8CHR7;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Phosphatidate phosphatase LPIN2;
DE            EC=3.1.3.4;
DE   AltName: Full=Lipin-2;
GN   Name=Lpin2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=20578762; PubMed=11138012; DOI=10.1038/83685;
RA   Peterfy M., Phan J., Xu P., Reue K.;
RT   "Lipodystrophy in the fld mouse results from mutation of a new gene
RT   encoding a nuclear protein, lipin.";
RL   Nat. Genet. 27:121-124(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-276 AND 659-893 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cecum, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186; SER-187 AND
RP   SER-245, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   TISSUE SPECIFICITY, CATALYTIC ACTIVITY, COFACTOR, AND ENZYME
RP   REGULATION.
RX   PubMed=17158099; DOI=10.1074/jbc.M610745200;
RA   Donkor J., Sariahmetoglu M., Dewald J., Brindley D.N., Reue K.;
RT   "Three mammalian lipins act as phosphatidate phosphatases with
RT   distinct tissue expression patterns.";
RL   J. Biol. Chem. 282:3450-3457(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   SUBCELLULAR LOCATION, FUNCTION, PHOSPHORYLATION AT 106-SER, AND
RP   INDUCTION.
RX   PubMed=19136718; DOI=10.1074/jbc.M807882200;
RA   Gropler M.C., Harris T.E., Hall A.M., Wolins N.E., Gross R.W., Han X.,
RA   Chen Z., Finck B.N.;
RT   "Lipin 2 is a liver-enriched phosphatidate phosphohydrolase enzyme
RT   that is dynamically regulated by fasting and obesity in mice.";
RL   J. Biol. Chem. 284:6763-6772(2009).
RN   [8]
RP   SUBCELLULAR LOCATION, FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND
RP   MUTAGENESIS OF SER-731.
RX   PubMed=19717560; DOI=10.1074/jbc.M109.023663;
RA   Donkor J., Zhang P., Wong S., O'Loughlin L., Dewald J., Kok B.P.,
RA   Brindley D.N., Reue K.;
RT   "A conserved serine residue is required for the phosphatidate
RT   phosphatase activity but not the transcriptional coactivator functions
RT   of lipin-1 and lipin-2.";
RL   J. Biol. Chem. 284:29968-29978(2009).
CC   -!- FUNCTION: Plays important roles in controlling the metabolism of
CC       fatty acids at differents levels. Acts as a magnesium-dependent
CC       phosphatidate phosphatase enzyme which catalyzes the conversion of
CC       phosphatidic acid to diacylglycerol during triglyceride,
CC       phosphatidylcholine and phosphatidylethanolamine biosynthesis in
CC       the reticulum endoplasmic membrane. Acts also as a nuclear
CC       transcriptional coactivator for PPARGC1A to modulate lipid
CC       metabolism.
CC   -!- CATALYTIC ACTIVITY: A 1,2-diacylglycerol 3-phosphate + H(2)O = a
CC       1,2-diacyl-sn-glycerol + phosphate.
CC   -!- COFACTOR: Mg(2+).
CC   -!- ENZYME REGULATION: Inhibited by N-ethylmaleimide.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol. Endoplasmic
CC       reticulum membrane. Note=Translocates from cytosol to endoplasmic
CC       reticulum membrane with increasing levels of oleate.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99PI5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99PI5-2; Sequence=VSP_010387, VSP_010388;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed at high level in liver and to some
CC       extend in lung, kidney, placenta, spleen, thymus, lymph node,
CC       prostate, testes, small intestine, and colon. Expressed also in
CC       circulating red blood cells and site of lymphopoiesis.
CC   -!- INDUCTION: By fasting in hepatocytes. Up-regulated in fld/fld
CC       (defect in LPIN1) mice. Up-regulated at protein level but not at
CC       transcript level in ob/ob and db/db mice, two obese mice models.
CC   -!- DOMAIN: Contains 1 Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic
CC       motif known to be essential for phosphatidate phosphatase activity
CC       (By similarity).
CC   -!- DOMAIN: Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL) motif, a motif
CC       known to be a transcriptional binding motif (By similarity).
CC   -!- SIMILARITY: Belongs to the lipin family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF286723; AAG52761.1; -; mRNA.
DR   EMBL; AK033662; BAC28415.1; -; mRNA.
DR   EMBL; AK050138; BAC34088.1; -; mRNA.
DR   EMBL; AK086834; BAC39754.1; -; mRNA.
DR   EMBL; BC039698; AAH39698.1; -; mRNA.
DR   IPI; IPI00319673; -.
DR   IPI; IPI00407062; -.
DR   RefSeq; NP_075020.2; NM_022882.4.
DR   UniGene; Mm.227924; -.
DR   ProteinModelPortal; Q99PI5; -.
DR   STRING; Q99PI5; -.
DR   PhosphoSite; Q99PI5; -.
DR   PRIDE; Q99PI5; -.
DR   Ensembl; ENSMUST00000053173; ENSMUSP00000053756; ENSMUSG00000024052.
DR   Ensembl; ENSMUST00000112647; ENSMUSP00000108266; ENSMUSG00000024052.
DR   GeneID; 64898; -.
DR   KEGG; mmu:64898; -.
DR   UCSC; uc008dmc.1; mouse.
DR   UCSC; uc008dmd.1; mouse.
DR   CTD; 64898; -.
DR   MGI; MGI:1891341; Lpin2.
DR   GeneTree; ENSGT00390000011286; -.
DR   HOGENOM; HBG444642; -.
DR   HOVERGEN; HBG052338; -.
DR   InParanoid; Q99PI5; -.
DR   PhylomeDB; Q99PI5; -.
DR   NextBio; 320209; -.
DR   ArrayExpress; Q99PI5; -.
DR   Bgee; Q99PI5; -.
DR   CleanEx; MM_LPIN2; -.
DR   Genevestigator; Q99PI5; -.
DR   GermOnline; ENSMUSG00000024052; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008195; F:phosphatidate phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
DR   InterPro; IPR023214; HAD-like_dom.
DR   InterPro; IPR007651; Lipin_N.
DR   InterPro; IPR013209; LNS2.
DR   Gene3D; G3DSA:3.40.50.1000; HAD-like_dom; 1.
DR   Pfam; PF04571; Lipin_N; 1.
DR   Pfam; PF08235; LNS2; 1.
DR   SMART; SM00775; LNS2; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Endoplasmic reticulum;
KW   Fatty acid metabolism; Hydrolase; Lipid metabolism; Membrane; Nucleus;
KW   Phosphoprotein; Transcription; Transcription regulation.
FT   CHAIN         1    893       Phosphatidate phosphatase LPIN2.
FT                                /FTId=PRO_0000209882.
FT   REGION        1    108       N-LIP.
FT   REGION      632    834       C-LIP.
FT   MOTIF       153    158       Nuclear localization signal (Potential).
FT   MOTIF       686    690       DXDXT motif.
FT   MOTIF       697    701       LXXIL motif.
FT   MOD_RES     106    106       Phosphoserine.
FT   MOD_RES     186    186       Phosphoserine.
FT   MOD_RES     187    187       Phosphoserine.
FT   MOD_RES     243    243       Phosphoserine.
FT   MOD_RES     245    245       Phosphoserine.
FT   VAR_SEQ     388    459       VHKRSQHQGPDDIYLDDLKALEPEVAALYFPKSDTDPGSRQ
FT                                WPESDTFSGSQSPQSVGSAAADSGTECLSDS -> LVWLKN
FT                                NCLLGDRCISGYDHGCVSRGPTWQLMTDSSARGPNALFWPL
FT                                WAPGTQPYIRQNMHIPKMNRNKNTF (in isoform 2).
FT                                /FTId=VSP_010387.
FT   VAR_SEQ     460    893       Missing (in isoform 2).
FT                                /FTId=VSP_010388.
FT   MUTAGEN     731    731       S->D: Abolishes phosphatidate phosphatase
FT                                activity but does not prevent membrane
FT                                association.
FT   MUTAGEN     731    731       S->L: Abolishes phosphatidate phosphatase
FT                                activity but does not prevent membrane
FT                                association nor coactivator activity.
FT   CONFLICT    839    839       R -> S (in Ref. 2; BAC34088).
SQ   SEQUENCE   893 AA;  99613 MW;  8C7FD7881946F8EA CRC64;
     MNYVGQLAGQ VLVTVKELYK GINQATLSGC IDVVVVRQQD GSYQCSPFHV RFGKLGVLRS
     KEKVIDIEIN GSAVDLHMKL GDNGEAFFVE ETEEEYEKLP AYLATSPIPT EDQFFKHIET
     PLVKSSGNER PAQSSDVSHT LESEAVFTQS SVKKKKRRRK KCKQDNRKEE QAASPVAEDV
     GDVGVSSDDE KRAQAARGSS NASLKEEDYK EPSLFHSGDN YPLSDGDWSP LETTYPQAVC
     PKSDSELEVK PSESLLRSEP HMEWTWGGFP ESTKVTKRER YDYHPRTATI TPSENTHFRV
     IPSEDSLIRE VEKDATVEDT TCTIVKPKPR ALCKQLSDAA STELPESPLE APQISSLLDA
     DPVPSPSAEA PSEPKPAAKD SPTKKKGVHK RSQHQGPDDI YLDDLKALEP EVAALYFPKS
     DTDPGSRQWP ESDTFSGSQS PQSVGSAAAD SGTECLSDSA MDLPDVTLSL CGGLSENGEI
     SKEKFMEHII TYHEFAENPG LIDNPNLVIR IYNRYYNWAL AAPMILSLQV FQKSLPKATV
     ESWVKDKMPK KSGRWWFWRK KESMIKQLPE TKEGKSEVPP ANDLPSNAEE PTSARPAEND
     TSSDEGSQEL EESIKVDPIT VETLSHCGTA SYKKSLRLSS DQIAKLKLHD GPNDVVFSIT
     TQYQGTCRCA GTIYLWNWND KVIISDIDGT ITKSDALGQI LPQLGKDWTH QGIARLYHSI
     NENGYKFLYC SARAIGMADM TRGYLHWVND KGTILPRGPL MLSPSSLFSA FHREVIEKKP
     EKFKIECLND IKNLFAPSRQ PFYAAFGNRP NDVYAYTQVG VPDCRIFTVN PKGELIQERT
     KGNKSSYHRL SELVEHVFPL LSKEQNSAFP CPEFSSFCYW RDPIPDLDLD DLA
//
ID   NTRI_MOUSE              Reviewed;         344 AA.
AC   Q99PJ0;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2002, sequence version 2.
DT   08-FEB-2011, entry version 85.
DE   RecName: Full=Neurotrimin;
DE   Flags: Precursor;
GN   Name=Ntm; Synonyms=Hnt, Nt;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Brain;
RA   Kim T.H., Choi S.C., Kim J., Jeon J.W., Kim K.D., Lee S.H.;
RT   "Cloning and expression of mouse neurotrimin gene in the developing
RT   nervous system.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Neural cell adhesion molecule.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily. IgLON
CC       family.
CC   -!- SIMILARITY: Contains 3 Ig-like C2-type (immunoglobulin-like)
CC       domains.
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DR   EMBL; AF282980; AAK00276.1; -; mRNA.
DR   EMBL; BC023307; AAH23307.1; -; mRNA.
DR   IPI; IPI00417005; -.
DR   UniGene; Mm.283138; -.
DR   ProteinModelPortal; Q99PJ0; -.
DR   SMR; Q99PJ0; 33-336.
DR   MINT; MINT-1177225; -.
DR   STRING; Q99PJ0; -.
DR   PRIDE; Q99PJ0; -.
DR   Ensembl; ENSMUST00000115237; ENSMUSP00000110892; ENSMUSG00000059974.
DR   UCSC; uc009oqt.1; mouse.
DR   MGI; MGI:2446259; Ntm.
DR   GeneTree; ENSGT00600000084036; -.
DR   HOGENOM; HBG443583; -.
DR   HOVERGEN; HBG017341; -.
DR   OMA; HLIVSPK; -.
DR   ArrayExpress; Q99PJ0; -.
DR   Bgee; Q99PJ0; -.
DR   CleanEx; MM_HNT; -.
DR   Genevestigator; Q99PJ0; -.
DR   GermOnline; ENSMUSG00000059974; Mus musculus.
DR   GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3.
DR   Pfam; PF07679; I-set; 3.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 2.
DR   PROSITE; PS50835; IG_LIKE; 3.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW   GPI-anchor; Immunoglobulin domain; Lipoprotein; Membrane; Repeat;
KW   Signal.
FT   SIGNAL        1     33       Potential.
FT   CHAIN        34    321       Neurotrimin.
FT                                /FTId=PRO_0000015112.
FT   PROPEP      322    344       Removed in mature form (Potential).
FT                                /FTId=PRO_0000015113.
FT   DOMAIN       39    126       Ig-like C2-type 1.
FT   DOMAIN      136    218       Ig-like C2-type 2.
FT   DOMAIN      222    309       Ig-like C2-type 3.
FT   LIPID       321    321       GPI-anchor amidated asparagine
FT                                (Potential).
FT   CARBOHYD     44     44       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     70     70       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    152    152       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    284    284       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    292    292       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    305    305       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    321    321       N-linked (GlcNAc...) (Potential).
FT   DISULFID     57    115       Potential.
FT   DISULFID    157    201       Potential.
FT   DISULFID    243    295       Potential.
FT   CONFLICT     75     75       L -> P (in Ref. 1; AAK00276).
FT   CONFLICT     92     92       S -> G (in Ref. 1; AAK00276).
FT   CONFLICT    119    119       T -> I (in Ref. 1; AAK00276).
FT   CONFLICT    187    187       E -> Q (in Ref. 1; AAK00276).
FT   CONFLICT    213    213       R -> P (in Ref. 1; AAK00276).
FT   CONFLICT    225    225       I -> F (in Ref. 1; AAK00276).
SQ   SEQUENCE   344 AA;  37984 MW;  C885BBA52C148554 CRC64;
     MGVCGYLFLP WKCLVVVSLR LLFLVPTGVP VRSGDATFPK AMDNVTVRQG ESATLRCTID
     NRVTRVAWLN RSTILYAGND KWCLDPRVVL LSNTQTQYSI EIQNVDVYDE GPYTCSVQTD
     NHPKTSRVHL IVQVSPKIVE ISSDISINEG NNISLTCIAT GRPEPTVTWR HISPKAVGFV
     SEDEYLEIQG ITREQSGEYE CSASNDVAAP VVRRVKVTVN YPPYISEAKG TGVPVGQKGT
     LQCEASAVPS AEFQWFKDDK RLVEGKKGVK VENRPFLSKL TFFNVSEHDY GNYTCVASNK
     LGHTNASIML FGPGAVSEVN NGTSRRAGCI WLLPLLVLHL LLKF
//
ID   UBXN6_MOUSE             Reviewed;         442 AA.
AC   Q99PL6; B8JJA5; Q3TTP1; Q3UG19; Q8C4D6; Q91W79; Q9D7L9;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=UBX domain-containing protein 6;
DE   AltName: Full=UBX domain-containing protein 1;
GN   Name=Ubxn6; Synonyms=Ubxd1, Ubxdc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=21240214; PubMed=11342112; DOI=10.1016/S0167-4781(00)00248-7;
RA   Carim-Todd L., Escarceller M., Estivill X., Sumoy L.;
RT   "Identification and characterization of UBXD1, a novel UBX domain-
RT   containing gene on human chromosome 19p13, and its mouse ortholog.";
RL   Biochim. Biophys. Acta 1517:298-301(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Testis, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Colon, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=18656546; DOI=10.1016/j.biocel.2008.06.008;
RA   Madsen L., Andersen K.M., Prag S., Moos T., Semple C.A., Seeger M.,
RA   Hartmann-Petersen R.;
RT   "Ubxd1 is a novel co-factor of the human p97 ATPase.";
RL   Int. J. Biochem. Cell Biol. 40:2927-2942(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Acts in a complex with VCP and cooperates with USP7 in
CC       promoting MDM2 deubiquitination and stabilization. MDM2
CC       stabilization leads to MDM2-dependent TP53 degradation (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with VCP through the PUB domain (By
CC       similarity). Interacts with SYVN1, HERPUD1, MDM2 and USP7 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Cytoplasm, cytoskeleton, centrosome (By similarity).
CC       Note=Localizes at the centrosome both in interphase and during
CC       mitosis (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99PL6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99PL6-2; Sequence=VSP_007454;
CC   -!- TISSUE SPECIFICITY: Widely expressed (at protein level). Highest
CC       expression in brain (at protein level).
CC   -!- SIMILARITY: Contains 1 PUB (PUG) domain.
CC   -!- SIMILARITY: Contains 1 UBX domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB26082.1; Type=Frameshift; Positions=435;
CC       Sequence=BAC38512.1; Type=Frameshift; Positions=394;
CC       Sequence=BAE36284.1; Type=Frameshift; Positions=390;
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DR   EMBL; AF272895; AAK13259.1; -; mRNA.
DR   EMBL; AK009117; BAB26082.1; ALT_FRAME; mRNA.
DR   EMBL; AK082510; BAC38512.1; ALT_FRAME; mRNA.
DR   EMBL; AK148170; BAE28390.1; -; mRNA.
DR   EMBL; AK161273; BAE36284.1; ALT_FRAME; mRNA.
DR   EMBL; CH466559; EDL23709.1; -; Genomic_DNA.
DR   EMBL; CT009719; CAX15602.1; -; Genomic_DNA.
DR   EMBL; BC016412; AAH16412.1; -; mRNA.
DR   EMBL; BC049963; AAH49963.1; -; mRNA.
DR   IPI; IPI00121151; -.
DR   IPI; IPI00323058; -.
DR   RefSeq; NP_077752.1; NM_024432.2.
DR   UniGene; Mm.28000; -.
DR   ProteinModelPortal; Q99PL6; -.
DR   SMR; Q99PL6; 335-409.
DR   STRING; Q99PL6; -.
DR   PhosphoSite; Q99PL6; -.
DR   PRIDE; Q99PL6; -.
DR   Ensembl; ENSMUST00000019722; ENSMUSP00000019722; ENSMUSG00000019578.
DR   GeneID; 66530; -.
DR   KEGG; mmu:66530; -.
DR   UCSC; uc008dat.1; mouse.
DR   CTD; 66530; -.
DR   MGI; MGI:1913780; Ubxn6.
DR   eggNOG; roNOG12681; -.
DR   GeneTree; ENSGT00510000047499; -.
DR   HOGENOM; HBG714607; -.
DR   HOVERGEN; HBG061370; -.
DR   InParanoid; Q99PL6; -.
DR   OMA; AIGFQKV; -.
DR   OrthoDB; EOG48D0VV; -.
DR   PhylomeDB; Q99PL6; -.
DR   NextBio; 321948; -.
DR   ArrayExpress; Q99PL6; -.
DR   Bgee; Q99PL6; -.
DR   Genevestigator; Q99PL6; -.
DR   GermOnline; ENSMUSG00000019578; Mus musculus.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR018997; PUB_domain.
DR   InterPro; IPR001012; UBX.
DR   Pfam; PF09409; PUB; 1.
DR   Pfam; PF00789; UBX; 1.
DR   SMART; SM00166; UBX; 1.
DR   PROSITE; PS50033; UBX; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Cytoskeleton; Nucleus;
KW   Phosphoprotein; Ubl conjugation pathway.
FT   CHAIN         1    442       UBX domain-containing protein 6.
FT                                /FTId=PRO_0000211026.
FT   DOMAIN      175    244       PUB.
FT   DOMAIN      332    408       UBX.
FT   COMPBIAS     55     61       Poly-Ala.
FT   MOD_RES      36     36       Phosphoserine.
FT   MOD_RES     336    336       Phosphotyrosine (By similarity).
FT   VAR_SEQ       1     53       Missing (in isoform 2).
FT                                /FTId=VSP_007454.
FT   CONFLICT    151    151       T -> S (in Ref. 2; BAC38512).
FT   CONFLICT    400    400       L -> V (in Ref. 2; BAB26082).
SQ   SEQUENCE   442 AA;  49796 MW;  9240DB2870F25B11 CRC64;
     MKKFFQEIKA DIKFKSAGPG QKLTDSAGEK TTKGKSPQLA LRQPRQGPTD EAQMAAAAAL
     ARLEQKQPRA RGPTSQDSIR NQVRKELQAE ATSSNNPGAP GTNSVPEPKE EISPHLAVPG
     VFFICPLTGV TLRRDQRDAH IKQAILSHFS TDPVAASIMK IHTFNRDRDR VKLGVDTIAK
     YLDNIHLHPE EEKYQKIKLQ NKVFQERINC LEGSHEFFEA IGFKKVTLPV PDQEGQEEFY
     VLGEDARAQP QNLARHKQQL LDAEPVRATL DRQLRVFRPS ALASHFELPS DFFSLTAEEV
     KREQRLRTEA VERLSSLRTK AMREKEEQRE LRKYTYALVR VRLPDGCLLQ GTFYAREKLS
     ALFRFVREAL QNDWLPFELR ASGGQKLEEN EALALNECGL VPSALLTFSW DASVLEDIRA
     AGAEPAKSVL RPELLAAIEQ LS
//
ID   Q99PL9_MOUSE            Unreviewed;        28 AA.
AC   Q99PL9;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   08-FEB-2011, entry version 45.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Crocc; Synonyms=Mfap2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129/SvJ;
RX   MEDLINE=20556468; PubMed=11102756; DOI=10.1016/S0945-053X(00)00115-3;
RA   Segade F., Broekelmann T.J., Pierce R.A., Mecham R.P.;
RT   "Revised genomic structure of the human MAGP1 gene and identification
RT   of alternate transcripts in human and mouse tissues.";
RL   Matrix Biol. 19:671-682(2000).
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DR   EMBL; AF268473; AAG49555.1; -; Genomic_DNA.
DR   IPI; IPI00654326; -.
DR   UniGene; Mm.80685; -.
DR   STRING; Q99PL9; -.
DR   Ensembl; ENSMUST00000040222; ENSMUSP00000037679; ENSMUSG00000040860.
DR   Ensembl; ENSMUST00000097816; ENSMUSP00000095425; ENSMUSG00000040860.
DR   Ensembl; ENSMUST00000102491; ENSMUSP00000099549; ENSMUSG00000040860.
DR   MGI; MGI:3529431; Crocc.
DR   GeneTree; ENSGT00600000084289; -.
DR   InParanoid; Q99PL9; -.
DR   ArrayExpress; Q99PL9; -.
DR   Bgee; Q99PL9; -.
DR   Genevestigator; Q99PL9; -.
DR   GO; GO:0035253; C:ciliary rootlet; IDA:MGI.
DR   GO; GO:0019894; F:kinesin binding; IPI:MGI.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
SQ   SEQUENCE   28 AA;  3007 MW;  A63210F4E54AB8B7 CRC64;
     VSTLKAQLHQ ELRRSSASVS LPSGTPEK
//
ID   ACBG1_MOUSE             Reviewed;         721 AA.
AC   Q99PU5; Q6ZQ79;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Long-chain-fatty-acid--CoA ligase ACSBG1;
DE            EC=6.2.1.3;
DE   AltName: Full=Acyl-CoA synthetase bubblegum family member 1;
DE            Short=mBG1;
DE   AltName: Full=Gonadotropin-regulated long chain acyl CoA synthetase;
DE            Short=GR-LACS;
DE   AltName: Full=Lipidosin;
GN   Name=Acsbg1; Synonyms=Kiaa0631, Lpd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, TISSUE
RP   SPECIFICITY, AND MUTAGENESIS OF GLY-281 AND LYS-287.
RC   TISSUE=Brain;
RX   MEDLINE=20563802; PubMed=11112418; DOI=10.1006/bbrc.2000.3897;
RA   Moriya-Sato A., Hida A., Inagawa-Ogashiwa M., Wada M.R., Sugiyama K.,
RA   Shimizu J., Yabuki T., Seyama Y., Hashimoto N.;
RT   "Novel acyl-CoA synthetase in adrenoleukodystrophy target tissues.";
RL   Biochem. Biophys. Res. Commun. 279:62-68(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   PubMed=16125341; DOI=10.1016/j.gene.2005.07.006;
RA   Sheng Y., Li J., Dufau M.L., Tsai-Morris C.-H.;
RT   "The gonadotropin-regulated long-chain acyl CoA synthetase gene: a
RT   novel downstream Sp1/Sp3 binding element critical for transcriptional
RT   promoter activity.";
RL   Gene 360:20-26(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Oviduct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=12975357; DOI=10.1074/jbc.M310075200;
RA   Pei Z., Oey N.A., Zuidervaart M.M., Jia Z., Li Y., Steinberg S.J.,
RA   Smith K.D., Watkins P.A.;
RT   "The acyl-CoA synthetase 'bubblegum' (lipidosin): further
RT   characterization and role in neuronal fatty acid beta-oxidation.";
RL   J. Biol. Chem. 278:47070-47078(2003).
RN   [7]
RP   ENZYME ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND DEVELOPMENTAL STAGE.
RX   PubMed=14516277; DOI=10.1042/BJ20031062;
RA   Fraisl P., Forss-Petter S., Zigman M., Berger J.;
RT   "Murine bubblegum orthologue is a microsomal very long-chain acyl-CoA
RT   synthetase.";
RL   Biochem. J. 377:85-93(2004).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=16469493; DOI=10.1016/j.jsbmb.2005.10.005;
RA   Li J., Sheng Y., Tang P.-Z., Tsai-Morris C.-H., Dufau M.L.;
RT   "Tissue-cell- and species-specific expression of gonadotropin-
RT   regulated long chain acyl-CoA synthetase (GR-LACS) in gonads, adrenal
RT   and brain. Identification of novel forms in the brain.";
RL   J. Steroid Biochem. Mol. Biol. 98:207-217(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-655, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Mediates activation of long-chain fatty acids for both
CC       synthesis of cellular lipids, and degradation via beta-oxidation.
CC       Able to activate long-chain fatty acids. Can activate diverse
CC       saturated, monosaturated and polyunsaturated fatty acids (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a long-chain carboxylic acid + CoA = AMP
CC       + diphosphate + an acyl-CoA.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasmic
CC       vesicle. Microsome. Endoplasmic reticulum.
CC   -!- TISSUE SPECIFICITY: Mainly expressed in brain. Also expressed in
CC       adrenal gland and testis. In brain, it is present in cerebral
CC       cortical and cerebellar neurons and in steroidogenic cells of the
CC       adrenal gland, testis and ovary (at protein level).
CC   -!- DEVELOPMENTAL STAGE: First detected on embryonic day 18 and
CC       increases steadily towards adulthood.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family. Bubblegum subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97989.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; AB050554; BAB32783.1; -; mRNA.
DR   EMBL; DQ009026; AAY58226.1; -; Genomic_DNA.
DR   EMBL; DQ009013; AAY58226.1; JOINED; Genomic_DNA.
DR   EMBL; DQ009014; AAY58226.1; JOINED; Genomic_DNA.
DR   EMBL; DQ009015; AAY58226.1; JOINED; Genomic_DNA.
DR   EMBL; DQ009016; AAY58226.1; JOINED; Genomic_DNA.
DR   EMBL; DQ009017; AAY58226.1; JOINED; Genomic_DNA.
DR   EMBL; DQ009018; AAY58226.1; JOINED; Genomic_DNA.
DR   EMBL; DQ009019; AAY58226.1; JOINED; Genomic_DNA.
DR   EMBL; DQ009020; AAY58226.1; JOINED; Genomic_DNA.
DR   EMBL; DQ009021; AAY58226.1; JOINED; Genomic_DNA.
DR   EMBL; DQ009022; AAY58226.1; JOINED; Genomic_DNA.
DR   EMBL; DQ009023; AAY58226.1; JOINED; Genomic_DNA.
DR   EMBL; DQ009024; AAY58226.1; JOINED; Genomic_DNA.
DR   EMBL; DQ009025; AAY58226.1; JOINED; Genomic_DNA.
DR   EMBL; AK129179; BAC97989.1; ALT_INIT; mRNA.
DR   EMBL; AK054103; BAC35657.1; -; mRNA.
DR   EMBL; BC057322; AAH57322.1; -; mRNA.
DR   IPI; IPI00453834; -.
DR   PIR; JC7557; JC7557.
DR   RefSeq; NP_444408.1; NM_053178.2.
DR   UniGene; Mm.20592; -.
DR   ProteinModelPortal; Q99PU5; -.
DR   SMR; Q99PU5; 99-707.
DR   STRING; Q99PU5; -.
DR   PhosphoSite; Q99PU5; -.
DR   PRIDE; Q99PU5; -.
DR   Ensembl; ENSMUST00000034822; ENSMUSP00000034822; ENSMUSG00000032281.
DR   GeneID; 94180; -.
DR   KEGG; mmu:94180; -.
DR   NMPDR; fig|10090.3.peg.20220; -.
DR   UCSC; uc009prj.1; mouse.
DR   CTD; 94180; -.
DR   MGI; MGI:2385656; Acsbg1.
DR   eggNOG; roNOG05521; -.
DR   GeneTree; ENSGT00600000084439; -.
DR   HOGENOM; HBG721674; -.
DR   HOVERGEN; HBG054660; -.
DR   InParanoid; Q99PU5; -.
DR   OMA; PHFMSSP; -.
DR   OrthoDB; EOG43R3MF; -.
DR   PhylomeDB; Q99PU5; -.
DR   BRENDA; 6.2.1.3; 244.
DR   NextBio; 352133; -.
DR   ArrayExpress; Q99PU5; -.
DR   Bgee; Q99PU5; -.
DR   CleanEx; MM_ACSBG1; -.
DR   Genevestigator; Q99PU5; -.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; ISS:HGNC.
DR   GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; ISS:HGNC.
DR   GO; GO:0001676; P:long-chain fatty acid metabolic process; ISS:HGNC.
DR   GO; GO:0051384; P:response to glucocorticoid stimulus; IMP:MGI.
DR   GO; GO:0000038; P:very long-chain fatty acid metabolic process; ISS:HGNC.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   Pfam; PF00501; AMP-binding; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum;
KW   Fatty acid metabolism; Ligase; Lipid metabolism; Microsome;
KW   Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1    721       Long-chain-fatty-acid--CoA ligase ACSBG1.
FT                                /FTId=PRO_0000315810.
FT   NP_BIND     279    287       ATP (By similarity).
FT   NP_BIND     469    474       ATP (By similarity).
FT   BINDING     547    547       ATP (By similarity).
FT   BINDING     562    562       ATP (By similarity).
FT   BINDING     698    698       ATP (By similarity).
FT   MOD_RES     132    132       Phosphotyrosine (By similarity).
FT   MOD_RES     135    135       Phosphotyrosine (By similarity).
FT   MOD_RES     136    136       Phosphotyrosine (By similarity).
FT   MOD_RES     655    655       Phosphotyrosine.
FT   MUTAGEN     281    281       G->A: Abolishes enzyme activity; when
FT                                associated with M-287.
FT   MUTAGEN     287    287       K->M: Abolishes enzyme activity; when
FT                                associated with A-281.
FT   CONFLICT    299    299       T -> I (in Ref. 3; BAC97989).
SQ   SEQUENCE   721 AA;  80426 MW;  C3A8C91333E984FE CRC64;
     MPRGSEAGYC CLSRDSNMPD SRDDQQQGAS LGTSQDNSQT SSLIDGQTLS KESPSHGLEL
     SAPEKARAAS LDGAEEALWT TRADGRVRLR LEPFCTQRPY TVHQMFYEAL DKYGNLSALG
     FKRKDKWERI SYYQYYLIAR KVAKGFLKLG LERAHSVAIL GFNSPEWFFS AVGTVFAGGI
     VTGIYTTSSP EACQYISHDC RANVIVVDTQ KQLEKILKIW KDLPHLKAVV IYQEPPPKKM
     ANVYTMEELI ELGQEVPEEA LDAIIDTQQP NQCCVLVYTS GTTGNPKGVM LSQDNITWTA
     RYGSQAGDIQ PAEVQQEVVV SYLPLSHIAA QIYDLWTGIQ WGAQVCFADP DALKGTLVNT
     LREVEPTSHM GVPRVWEKIM ERIQEVAAQS GFIRRKMLLW AMSVTLEQNL TCPSNDLKPF
     TSRLADYLVL ARVRQALGFA KCQKNFYGAA PMTAETQRFF LGLNIRLYAG YGLSESTGPH
     FMSSPYNYRL YSSGRVVPGC RVKLVNQDAD GIGEICLWGR TIFMGYLNME DKTCEAIDSE
     GWLHTGDMGR LDADGFLYIT GRLKELIITA GGENVPPVPI EEAVKMELPI ISSAMLIGDQ
     RKFLSMLLTL KCTLDPETSE PTDSLTEQAV EFCQRVGSKA STVSEIVGQR DEAVYQAIHE
     GIQRVNANAA ARPYHIQKWA ILQRDFSISG GELGPTMKLK RLTVLEKYKD IIDSFYQEQK
     Q
//
ID   BAP1_MOUSE              Reviewed;         728 AA.
AC   Q99PU7; Q3TCR6; Q6ZQE6;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase BAP1;
DE            EC=3.4.19.12;
DE   AltName: Full=BRCA1-associated protein 1;
DE   AltName: Full=Ubiquitin C-terminal hydrolase X4;
DE            Short=UCH-X4;
GN   Name=Bap1; Synonyms=Kiaa0272;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Mizuta R.;
RT   "Ubiquitin C-terminal hydrolase.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Fetal brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=98187701; PubMed=9528852; DOI=10.1038/sj.onc.1201861;
RA   Jensen D.E., Proctor M., Marquis S.T., Gardner H.P., Ha S.I.,
RA   Chodosh L.A., Ishov A.M., Tommerup N., Vissing H., Sekido Y.,
RA   Minna J., Borodovsky A., Schultz D.C., Wilkinson K.D., Maul G.G.,
RA   Barlev N., Berger S., Prendergast G.C., Rauscher F.J. III;
RT   "BAP1: a novel ubiquitin hydrolase which binds to the BRCA1 RING
RT   finger and enhances BRCA1-mediated cell growth suppression.";
RL   Oncogene 16:1097-1112(1998).
RN   [6]
RP   MUTAGENESIS OF CYS-91 AND 716-ARG--ARG-721.
RX   PubMed=18757409; DOI=10.1158/0008-5472.CAN-08-0365;
RA   Ventii K.H., Devi N.S., Friedrich K.L., Chernova T.A., Tighiouart M.,
RA   Van Meir E.G., Wilkinson K.D.;
RT   "BRCA1-associated protein-1 is a tumor suppressor that requires
RT   deubiquitinating activity and nuclear localization.";
RL   Cancer Res. 68:6953-6962(2008).
CC   -!- FUNCTION: Deubiquitinating enzyme that plays a key role in
CC       chromatin by mediating deubiquitination of histone H2A and HCFC1.
CC       Catalytic component of the PR-DUB complex, a complex that
CC       specifically mediates deubiquitination of histone H2A
CC       monoubiquitinated at 'Lys-119' (H2AK119ub1). Does not
CC       deubiquitinate monoubiquitinated histone H2B. Acts as a regulator
CC       of cell growth by mediating deubiquitination of HCFC1 N-terminal
CC       and C-terminal chains, with some specificity toward 'Lys-48'-
CC       linked polyubiquitin chains compared to 'Lys-63'-linked
CC       polyubiquitin chains. Deubiquitination of HCFC1 does not lead to
CC       increase stability of HCFC1. Interferes with the BRCA1 and BARD1
CC       heterodimer activity by inhibiting their ability to mediate
CC       ubiquitination and autoubiquitination. It however does not mediate
CC       deubiquitination of BRCA1 and BARD1. Acts as a tumor suppressor
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- SUBUNIT: Component of the PR-DUB complex, at least composed of
CC       BAP1 and ASXL1. Interacts with BRCA1 (via the RING finger).
CC       Interacts (via HBM-like motif) with HCFC1 (By similarity).
CC   -!- INTERACTION:
CC       P38398:BRCA1 (xeno); NbExp=2; IntAct=EBI-1791471, EBI-349905;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Mainly nuclear. Binds to chromatin (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in mammary glands, testis and
CC       ovary. Up-regulated in mammary glands during puberty, pregnancy,
CC       and as a result of parity.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- MISCELLANEOUS: Has the ability to ability to suppress
CC       tumorigenicity when expressed in NCI-H226 cells (PubMed:18757409).
CC   -!- SIMILARITY: Belongs to the peptidase C12 family. BAP1 subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97918.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; AB047820; BAB32976.1; -; mRNA.
DR   EMBL; AK129108; BAC97918.1; ALT_INIT; mRNA.
DR   EMBL; AK170576; BAE41889.1; -; mRNA.
DR   EMBL; BC050901; AAH50901.1; -; mRNA.
DR   IPI; IPI00453853; -.
DR   RefSeq; NP_081364.1; NM_027088.2.
DR   UniGene; Mm.3779; -.
DR   ProteinModelPortal; Q99PU7; -.
DR   SMR; Q99PU7; 4-250.
DR   IntAct; Q99PU7; 6.
DR   MEROPS; C12.004; -.
DR   PhosphoSite; Q99PU7; -.
DR   PRIDE; Q99PU7; -.
DR   Ensembl; ENSMUST00000022458; ENSMUSP00000022458; ENSMUSG00000021901.
DR   GeneID; 104416; -.
DR   KEGG; mmu:104416; -.
DR   UCSC; uc007sxh.1; mouse.
DR   CTD; 104416; -.
DR   MGI; MGI:1206586; Bap1.
DR   GeneTree; ENSGT00510000046560; -.
DR   HOGENOM; HBG713259; -.
DR   HOVERGEN; HBG054042; -.
DR   InParanoid; Q99PU7; -.
DR   OMA; AKAHNSH; -.
DR   OrthoDB; EOG4XPQFC; -.
DR   PhylomeDB; Q99PU7; -.
DR   BRENDA; 3.4.19.12; 244.
DR   NextBio; 357097; -.
DR   ArrayExpress; Q99PU7; -.
DR   Bgee; Q99PU7; -.
DR   CleanEx; MM_BAP1; -.
DR   Genevestigator; Q99PU7; -.
DR   GermOnline; ENSMUSG00000021901; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0035517; C:PR-DUB complex; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; ISS:UniProtKB.
DR   GO; GO:0004843; F:ubiquitin-specific protease activity; ISS:UniProtKB.
DR   GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISS:UniProtKB.
DR   GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR   GO; GO:0001558; P:regulation of cell growth; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR001578; Peptidase_C12.
DR   Gene3D; G3DSA:3.40.532.10; Peptidase_C12; 1.
DR   PANTHER; PTHR10589; Peptidase_C12; 1.
DR   Pfam; PF01088; Peptidase_C12; 1.
DR   PRINTS; PR00707; UBCTHYDRLASE.
DR   PROSITE; PS00140; UCH_1; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Coiled coil; Cytoplasm; Hydrolase; Nucleus;
KW   Phosphoprotein; Protease; Thiol protease; Ubl conjugation pathway.
FT   CHAIN         1    728       Ubiquitin carboxyl-terminal hydrolase
FT                                BAP1.
FT                                /FTId=PRO_0000211070.
FT   REGION      595    720       Interaction with BRCA1 (By similarity).
FT   COILED      629    660       Potential.
FT   MOTIF       363    366       HBM-like motif (By similarity).
FT   MOTIF       716    721       Nuclear localization signal (By
FT                                similarity).
FT   ACT_SITE     91     91       Nucleophile (Probable).
FT   ACT_SITE    169    169       Proton donor (By similarity).
FT   SITE        184    184       Important for enzyme activity (By
FT                                similarity).
FT   MOD_RES     327    327       Phosphoserine (By similarity).
FT   MOD_RES     395    395       Phosphoserine (By similarity).
FT   MOD_RES     486    486       Phosphothreonine (By similarity).
FT   MOD_RES     488    488       Phosphoserine (By similarity).
FT   MOD_RES     581    581       Phosphoserine (By similarity).
FT   MOD_RES     582    582       Phosphoserine (By similarity).
FT   MOD_RES     591    591       Phosphoserine (By similarity).
FT   MUTAGEN      91     91       C->A: Abolishes ability to suppress
FT                                tumorigenicity when expressed in NCI-H226
FT                                cells.
FT   MUTAGEN     716    721       RRKRSR->AAAAAA: Abolishes ability to
FT                                suppress tumorigenicity when expressed in
FT                                NCI-H226 cells.
FT   CONFLICT    725    725       A -> V (in Ref. 2; BAC97918).
SQ   SEQUENCE   728 AA;  80492 MW;  2BDEAFB09CD276DB CRC64;
     MNKGWLELES DPGLFTLLVE DFGVKGVQVE EIYDLQSKCQ GPVYGFIFLF KWIEERRSRR
     KVSTLVDDTS VIDDDIVNNM FFAHQLIPNS CATHALLSVL LNCSNVDLGP TLSRMKDFTK
     GFSPESKGYA IGNAPELAKA HNSHARPEPR HLPEKQNGLS AVRTMEAFHF VSYVPITGRL
     FELDGLKVYP IDHGPWGEDE EWTDKARRVI MERIGLATAG EPYHDIRFNL MAVVPDRRIK
     YETRLHVLKV NRQTVLEALQ QLIRVTQPEL IQTHKSQESQ LPEESKPASS KSPLGLEAGR
     TPVASECTQT DGAEEVAGSC PQTTTHSPPS KCKLVVKPPG SSLNGVPPNP APIVQRLPAF
     LDNHNYAKSP MQEEEDLAAG VGRSRVPVRA PQQYSEDEDD YEDEDEDVQN TNPAIRYKRK
     GTGKPGSLSN SSDGQLSVLQ PNTINVLTEK LQESQKDLSV PLSIKTSSGA GSPAVAVPTH
     SQPSPTPSNE STDTASEIGS AFNSPLRSPI RSANPTRPSS PVTSHISKVL FGEDDSLLRV
     DCIRYNRAVR DLGPVISTGL LHLAEDGVLS PLALTEGGKG SSPSTRSSQG SQGSSGLEEK
     EVVEVTESRD KPGLNRSSEP LSGEKYSPKE LLALLKCVEA EIANYEACLK EEVEKRKKFK
     IDDQRRTHNY DEFICTFISM LAQEGMLANL VEQNISVRRR QGVSIGRLHK QRKPDRRKRS
     RPYKAKRQ
//
ID   DHX30_MOUSE             Reviewed;        1217 AA.
AC   Q99PU8; Q3U4Z4; Q3UFA0; Q3UJS4; Q91WA7; Q99KN7;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Putative ATP-dependent RNA helicase DHX30;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAH box protein 30;
GN   Name=Dhx30; Synonyms=Helg;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=CNS;
RA   Tsukahara M., Ji Z., Noguchi S., Masatoshi T., Tsunoo H.;
RT   "A novel helicase family gene 'HELG' is highly expressed in embryonic
RT   neural cells and is required for gastrulation in the mouse.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J, DBA/2, and NOD;
RC   TISSUE=Sympathetic ganglion, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Identified in a complex with TFAM and SSBP1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 3: Mitochondrion matrix,
CC       mitochondrion nucleoid (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm (By similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid
CC       (By similarity). Cytoplasm (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q99PU8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99PU8-2; Sequence=VSP_019747;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q99PU8-3; Sequence=VSP_019746;
CC         Note=Phosphorylated on Ser-15 (By similarity);
CC   -!- PTM: Isoform 3 is phosphorylated on Ser-15 (By similarity).
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 DRBM (double-stranded RNA-binding) domain.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
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DR   EMBL; AB047557; BAB32789.1; -; mRNA.
DR   EMBL; AK146326; BAE27081.1; -; mRNA.
DR   EMBL; AK148778; BAE28661.1; -; mRNA.
DR   EMBL; AK153969; BAE32286.1; -; mRNA.
DR   EMBL; BC004082; AAH04082.1; -; mRNA.
DR   EMBL; BC016202; AAH16202.1; -; mRNA.
DR   IPI; IPI00127902; -.
DR   IPI; IPI00270064; -.
DR   IPI; IPI00761204; -.
DR   RefSeq; NP_579925.1; NM_133347.1.
DR   UniGene; Mm.276305; -.
DR   ProteinModelPortal; Q99PU8; -.
DR   SMR; Q99PU8; 67-175, 257-356, 448-1174.
DR   PhosphoSite; Q99PU8; -.
DR   PRIDE; Q99PU8; -.
DR   Ensembl; ENSMUST00000035056; ENSMUSP00000035056; ENSMUSG00000032480.
DR   Ensembl; ENSMUST00000062368; ENSMUSP00000062622; ENSMUSG00000032480.
DR   Ensembl; ENSMUST00000111991; ENSMUSP00000107622; ENSMUSG00000032480.
DR   GeneID; 72831; -.
DR   KEGG; mmu:72831; -.
DR   UCSC; uc009rtg.1; mouse.
DR   UCSC; uc009rth.1; mouse.
DR   UCSC; uc009rti.1; mouse.
DR   CTD; 72831; -.
DR   MGI; MGI:1920081; Dhx30.
DR   eggNOG; roNOG10072; -.
DR   GeneTree; ENSGT00550000074257; -.
DR   HOVERGEN; HBG081437; -.
DR   OMA; MVERSLR; -.
DR   NextBio; 337009; -.
DR   ArrayExpress; Q99PU8; -.
DR   Bgee; Q99PU8; -.
DR   CleanEx; MM_DHX30; -.
DR   Genevestigator; Q99PU8; -.
DR   GermOnline; ENSMUSG00000032480; Mus musculus.
DR   GO; GO:0042645; C:mitochondrial nucleoid; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR011709; DUF1605.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF07717; DUF1605; 1.
DR   Pfam; PF04408; HA2; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS50137; DS_RBD; FALSE_NEG.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Helicase; Hydrolase;
KW   Mitochondrion; Mitochondrion nucleoid; Nucleotide-binding;
KW   Phosphoprotein; RNA-binding.
FT   CHAIN         1   1217       Putative ATP-dependent RNA helicase
FT                                DHX30.
FT                                /FTId=PRO_0000245539.
FT   DOMAIN       76    144       DRBM.
FT   DOMAIN      467    635       Helicase ATP-binding.
FT   DOMAIN      677    850       Helicase C-terminal.
FT   NP_BIND     480    487       ATP (By similarity).
FT   MOTIF       582    585       DEAH box.
FT   COMPBIAS    211    222       Poly-Glu.
FT   COMPBIAS   1033   1036       Poly-Glu.
FT   MOD_RES     119    119       Phosphoserine (By similarity).
FT   MOD_RES     127    127       Phosphoserine (By similarity).
FT   MOD_RES     171    171       Phosphoserine (By similarity).
FT   MOD_RES     249    249       Phosphoserine (By similarity).
FT   VAR_SEQ       1     64       MVTPVCNSSTWQPKDSSFLSWPEMFSLDSFRKDRTQHRQRQ
FT                                CKLPPPRLPPMCVNPAPGGTITR -> MAAARRLMALAAGV
FT                                SPRLRPPDPLVASGRQGCSRGFSSSFVRSDGTQEAAEVESE
FT                                VAPSEPGEGDGSMVN (in isoform 3).
FT                                /FTId=VSP_019746.
FT   VAR_SEQ       1     23       Missing (in isoform 2).
FT                                /FTId=VSP_019747.
FT   CONFLICT     45     45       P -> H (in Ref. 2; BAE27081).
FT   CONFLICT     83     83       V -> G (in Ref. 2; BAE27081).
FT   CONFLICT    142    142       Q -> E (in Ref. 2; BAE27081).
FT   CONFLICT    168    168       R -> C (in Ref. 2; BAE27081).
FT   CONFLICT    180    180       E -> D (in Ref. 2; BAE27081).
FT   CONFLICT    272    272       L -> M (in Ref. 2; BAE27081).
FT   CONFLICT    342    342       D -> G (in Ref. 2; BAE27081).
FT   CONFLICT    663    663       R -> W (in Ref. 2; BAE27081/BAE32286).
FT   CONFLICT    783    783       K -> R (in Ref. 2; BAE27081).
FT   CONFLICT    822    822       R -> Q (in Ref. 2; BAE27081).
FT   CONFLICT    991    991       Y -> H (in Ref. 2; BAE27081).
FT   CONFLICT   1211   1211       M -> V (in Ref. 3; AAH16202).
SQ   SEQUENCE   1217 AA;  136668 MW;  C6157413C98A1200 CRC64;
     MVTPVCNSST WQPKDSSFLS WPEMFSLDSF RKDRTQHRQR QCKLPPPRLP PMCVNPAPGG
     TITRASRDLL KEFPQPKNLL NSVIGRALGI SHAKDKLVYV HTNGPKKKKV TLHIKWPKSV
     EVEGYGSKKI DAERQAAAAA CQLFKGWGLL GPRNELFDAA KYRVLADRFG SPADSWWRPE
     PTMPPTSWRQ LNPENIRPGG PAGLSRSLGR EEEEDEEEEL EEGTIDVTEF LSMTQQDSHN
     PLRDSRGGSF EMTDDDSAIR ALTQFPLPKN LLAKVIQIAT SSSTAKNLMQ FHTVGTKTKL
     ATLTLLWPCP MTFVAKGRRK AEAENKAAAL ACKKLKSLGL VDRNNEPLTH AMYNLASLRE
     LGETQRRPCT IQVPEPILRK IEAFLSHYPV DSSWISPELR LQSDDILPLG KDSGPLSDPI
     TGKPYMPLSE AEEVRLSQSL LELWRRRGPI WQEAPQLPVD PHRDTILSAI EQHPVVVISG
     DTGCGKTTRI PQLLLERYVT EGRGARCNVI ITQPRRISAV SVAQRVSHEL GPSLRRNVGF
     QVRLESKPPA RGGALLFCTV GILLRKLQSN PSLEGVSHVI VDEVHERDVN TDFLLILLKG
     LQRLNPALRL VLMSATGDNE RFSRYFGGCP VIKVPGFMYP VKEHYLEDIL AKLGKHQYPH
     RHRHHESEDE CALDLDLVTD LVLHIDARGE PGGILCFLPG WQEIKGVQQR LQEALGMHES
     KYLILPVHSN IPMMDQKAIF QQPPLGVRKI VLATNIAETS ITVNDIVHVV DSGLHKEERY
     DLKTKVSCLE TVWVSRANVI QRRGRAGRCQ SGFAYHLFPR SRLEKMVPFQ VPEILRTPLE
     NLVLQAKIHM PEKTAVEFLS KAVDSPNIKA VDEAVILLQE IGVLDQREYL TTLGQRLAHI
     STDPRLAKAI VLAAIFRCLH PLLVVVSCLT RDPFSSSLQN RAEVDKVKAL LSHDSGSDHL
     AFVRAVAGWE EVLRWQDRTS RENYLEENLL YAPSLRFIHG LIKQFSENIY EAFLVGKPSD
     CTLPSAQCNE YSEEEELVKG VLMAGLYPNL IQVRQGKVTR QGKFKPNSVT YRTKSGNILL
     HKSTINREAT RLRSRWLTYF MAVKSNGSVF VRDSSQVHPL AVLLLTDGDV HIRDDGRRAT
     ISLSDSDLLR LEGDSRTVRL LREFRRALGR MVERSLRSEL AALPLSVQQE HGQLLALLAE
     LLRGPCGSFD MRKTADD
//
ID   PRP8_MOUSE              Reviewed;        2335 AA.
AC   Q99PV0; A5D6Q4; Q5ND30; Q5ND31; Q7TQK2; Q8BRZ5; Q8K001;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   24-NOV-2009, sequence version 2.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Pre-mRNA-processing-splicing factor 8;
DE   AltName: Full=Splicing factor Prp8;
GN   Name=Prpf8; Synonyms=Prp8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=Swiss Webster / NIH; TISSUE=Embryo;
RX   PubMed=11275560;
RA   Takahashi A., Muramatsu H., Takagi S., Fujisawa H., Miyake Y.,
RA   Muramatsu T.;
RT   "A splicing factor, Prp8: preferential localization in the testis and
RT   ovary in adult mice.";
RL   J. Biochem. 129:599-606(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, Mammary tumor, and Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-772.
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15169873; DOI=10.1091/mbc.E04-03-0253;
RA   Saitoh N., Spahr C.S., Patterson S.D., Bubulya P., Neuwald A.F.,
RA   Spector D.L.;
RT   "Proteomic analysis of interchromatin granule clusters.";
RL   Mol. Biol. Cell 15:3876-3890(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1318, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2042, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
CC   -!- FUNCTION: Central component of the spliceosome, which may play a
CC       role in aligning the pre-mRNA 5'- and 3'-exons for ligation.
CC       Interacts with U5 snRNA, and with pre-mRNA 5'-splice sites in B
CC       spliceosomes and 3'-splice sites in C spliceosomes.
CC   -!- SUBUNIT: Part of the U5 snRNP complex, and of U5.4/6 and
CC       U5.U4atac/U6atac snRNP complexes in U2- and U12-dependent
CC       spliceosomes, respectively. Found in a mRNA splicing-dependent
CC       exon junction complex (EJC) with SRRM1. Interacts with U5 snRNP
CC       proteins SNRP116 and WDR57/SPF38. Interacts with EFTUD2 and
CC       SNRNP200 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in testis (preferentially
CC       in the outer cell layer), and moderately in ovary (preferentially
CC       in granulosa cells).
CC   -!- DEVELOPMENTAL STAGE: During embryogenesis, is highly expressed at
CC       day 9.5 of gestation, and its expression decreases progressively
CC       during embryogenesis.
CC   -!- DOMAIN: The MPN domain has structural similarity with viral
CC       ribonucleases and RNase H, but unlike RNases, it does not bind any
CC       metal ions (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Contains 1 MPN (JAB/Mov34) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH54103.1; Type=Erroneous initiation;
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DR   EMBL; AB047391; BAB32671.1; -; mRNA.
DR   EMBL; AL591496; CAI35387.1; -; Genomic_DNA.
DR   EMBL; BC034648; AAH34648.1; -; mRNA.
DR   EMBL; BC054103; AAH54103.1; ALT_INIT; mRNA.
DR   EMBL; BC093481; AAH93481.1; -; mRNA.
DR   EMBL; AK041017; BAC30783.1; -; mRNA.
DR   IPI; IPI00121596; -.
DR   RefSeq; NP_619600.2; NM_138659.2.
DR   UniGene; Mm.3757; -.
DR   ProteinModelPortal; Q99PV0; -.
DR   SMR; Q99PV0; 1760-2016, 2069-2314.
DR   STRING; Q99PV0; -.
DR   PhosphoSite; Q99PV0; -.
DR   PRIDE; Q99PV0; -.
DR   Ensembl; ENSMUST00000018449; ENSMUSP00000018449; ENSMUSG00000020850.
DR   Ensembl; ENSMUST00000102510; ENSMUSP00000099568; ENSMUSG00000020850.
DR   GeneID; 192159; -.
DR   KEGG; mmu:192159; -.
DR   UCSC; uc007kdx.1; mouse.
DR   CTD; 192159; -.
DR   MGI; MGI:2179381; Prpf8.
DR   GeneTree; ENSGT00390000015210; -.
DR   HOGENOM; HBG398200; -.
DR   HOVERGEN; HBG052796; -.
DR   InParanoid; Q99PV0; -.
DR   OMA; RSGMSHD; -.
DR   OrthoDB; EOG45HRWF; -.
DR   PhylomeDB; Q99PV0; -.
DR   NextBio; 371143; -.
DR   ArrayExpress; Q99PV0; -.
DR   Bgee; Q99PV0; -.
DR   CleanEx; MM_PRPF8; -.
DR   Genevestigator; Q99PV0; -.
DR   GermOnline; ENSMUSG00000020850; Mus musculus.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000398; P:nuclear mRNA splicing, via spliceosome; IEA:InterPro.
DR   InterPro; IPR000555; Mov34_MPN_PAD1.
DR   InterPro; IPR012591; Pre-mRNA-splicing_factor-8.
DR   InterPro; IPR012984; PRO_C.
DR   InterPro; IPR012592; PROCN.
DR   InterPro; IPR021983; PRP8_domainIV.
DR   InterPro; IPR019581; Prp8_U5-snRNA-bd.
DR   InterPro; IPR019580; Prp8_U6-snRNA-bd.
DR   InterPro; IPR019582; RRM_spliceosomal_PrP8.
DR   Pfam; PF01398; Mov34; 1.
DR   Pfam; PF08082; PRO8NT; 1.
DR   Pfam; PF08083; PROCN; 1.
DR   Pfam; PF08084; PROCT; 1.
DR   Pfam; PF12134; PRP8_domainIV; 1.
DR   Pfam; PF10598; RRM_4; 1.
DR   Pfam; PF10597; U5_2-snRNA_bdg; 1.
DR   Pfam; PF10596; U6-snRNA_bdg; 1.
DR   ProDom; PD149576; Pre-mRNA-splicing_factor-8; 1.
DR   SMART; SM00232; JAB_MPN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Ribonucleoprotein; RNA-binding; Spliceosome.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   2335       Pre-mRNA-processing-splicing factor 8.
FT                                /FTId=PRO_0000097041.
FT   DOMAIN     2099   2233       MPN.
FT   REGION     1669   2034       Involved in interaction with pre-mRNA 5'
FT                                splice site (By similarity).
FT   REGION     2301   2335       Required for interaction with EFTUD2 and
FT                                SNRNP200 (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES    1318   1318       Phosphothreonine.
FT   MOD_RES    1463   1463       N6-acetyllysine (By similarity).
FT   MOD_RES    1539   1539       Phosphoserine (By similarity).
FT   MOD_RES    2042   2042       Phosphothreonine.
FT   MOD_RES    2064   2064       Phosphothreonine (By similarity).
FT   MOD_RES    2079   2079       Phosphoserine (By similarity).
FT   CONFLICT    797    797       D -> V (in Ref. 1; BAB32671).
FT   CONFLICT   2191   2195       QDVTT -> THASA (in Ref. 3; AAH54103).
SQ   SEQUENCE   2335 AA;  273616 MW;  C1A7A989B1AFB3B7 CRC64;
     MAGVFPYRGP GNPVPGPLAP LPDYMSEEKL QEKARKWQQL QAKRYAEKRK FGFVDAQKED
     MPPEHVRKII RDHGDMTNRK FRHDKRVYLG ALKYMPHAVL KLLENMPMPW EQIRDVPVLY
     HITGAISFVN EIPWVIEPVY ISQWGSMWIM MRREKRDRRH FKRMRFPPFD DEEPPLDYAD
     NILDVEPLEA IQLELDPEED APVLDWFYDH QPLRDSRKYV NGSTYQRWQF TLPMMSTLYR
     LANQLLTDLV DDNYFYLFDL KAFFTSKALN MAIPGGPKFE PLVRDINLQD EDWNEFNDIN
     KIIIRQPIRT EYKIAFPYLY NNLPHHVHLT WYHTPNVVFI KTEDPDLPAF YFDPLINPIS
     HRHSVKSQEP LPDDDEEFEL PEFVEPFLKD TPLYTDNTAN GIALLWAPRP FNLRSGRTRR
     ALDIPLVKNW YREHCPAGQP VKVRVSYQKL LKYYVLNALK HRPPKAQKKR YLFRSFKATK
     FFQSTKLDWV EVGLQVCRQG YNMLNLLIHR KNLNYLHLDY NFNLKPVKTL TTKERKKSRF
     GNAFHLCREV LRLTKLVVDS HVQYRLGNVD AFQLADGLQY IFAHVGQLTG MYRYKYKLMR
     QIRMCKDLKH LIYYRFNTGP VGKGPGCGFW AAGWRVWLFF MRGITPLLER WLGNLLARQF
     EGRHSKGVAK TVTKQRVESH FDLELRAAVM HDILDMMPEG IKQNKARTIL QHLSEAWRCW
     KANIPWKVPG LPTPIENMIL RYVKAKADWW TNTAHYNRER IRRGATVDKT VCKKNLGRLT
     RLYLKAEQER QHNYLKDGPY ITAEEAVAVY TTTVHWLESR RFSPIPFPPL SYKHDTKLLI
     LALERLKEAY SVKSRLNQSQ REELGLIEQA YDNPHEALSR IKRHLLTQRA FKEVGIEFMD
     LYSHLVPVYD VEPLEKITDA YLDQYLWYEA DKRRLFPPWI KPADTEPPPL LVYKWCQGIN
     NLQDVWETSE GECNVMLESR FEKMYEKIDL TLLNRLLRLI VDHNIADYMT AKNNVVINYK
     DMNHTNSYGI IRGLQFASFI VQYYGLVMDL LVLGLHRASE MAGPPQMPND FLSFQDIATE
     AAHPIRLFCR YIDRIHIFFR FTADEARDLI QRYLTEHPDP NNENIVGYNN KKCWPRDARM
     RLMKHDVNLG RAVFWDIKNR LPRSVTTVQW ENSFVSVYSK DNPNLLFNMC GFECRILPKC
     RTSYEEFTHK DGVWNLQNEV TKERTAQCFL RVDDESMQRF HNRVRQILMA SGSTTFTKIV
     NKWNTALIGL MTYFREAVVN TQELLDLLVK CENKIQTRIK IGLNSKMPSR FPPVVFYTPK
     ELGGLGMLSM GHVLIPQSDL RWSKQTDVGI THFRSGMSHE EDQLIPNLYR YIQPWESEFI
     DSQRVWAEYA LKRQEAIAQN RRLTLEDLED SWDRGIPRIN TLFQKDRHTL AYDKGWRVRT
     DFKQYQVLKQ NPFWWTHQRH DGKLWNLNNY RTDMIQALGG VEGILEHTLF KGTYFPTWEG
     LFWEKASGFE ESMKWKKLTN AQRSGLNQIP NRRFTLWWSP TINRANVYVG FQVQLDLTGI
     FMHGKIPTLK ISLIQIFRAH LWQKIHESIV MDLCQVFDQE LDALEIETVQ KETIHPRKSY
     KMNSSCADIL LFASYKWNVS RPSLLADSKD VMDSTTTQKY WIDIQLRWGD YDSHDIERYA
     RAKFLDYTTD NMSIYPSPTG VLIAIDLAYN LHSAYGNWFP GSKPLIQQAM AKIMKANPAL
     YVLRERIRKG LQLYSSEPTE PYLSSQNYGE LFSNQIIWFV DDTNVYRVTI HKTFEGNLTT
     KPINGAIFIF NPRTGQLFLK IIHTSVWAGQ KRLGQLAKWK TAEEVAALIR SLPVEEQPKQ
     IIVTRKGMLD PLEVHLLDFP NIVIKGSELQ LPFQACLKVE KFGDLILKAT EPQMVLFNLY
     DDWLKTISSY TAFSRLILIL RALHVNNDRA KVILKPDKTT VTEPHHIWPT LTDEEWIKVE
     VQLKDLILAD YGKKNNVNVA SLTQSEIRDI ILGMEISAPS QQRQQIAEIE KQTKEQSQLT
     ATQTRTVNKH GDEIITSTTS NYETQTFSSK TEWRVRAISA ANLHLRTNHI YVSSDDIKET
     GYTYILPKNV LKKFICISDL RAQIAGYLYG VSPPDNPQVK EIRCIVMVPQ WGTHQTVHLP
     SQLPQHEYLK EMEPLGWIHT QPNESPQLSP QDVTTHAKIM ADNPSWDGEK TIIITCSFTP
     GSCTLTAYKL TPSGYEWGRQ NTDKGNNPKG YLPSHYERVQ MLLSDRFLGF FMVPAQSSWN
     YNFMGVRHDP NMKYELQLAN PKEFYHEVHR PSHFLNFALL QEGEVYSADR EDLYA
//
ID   BC11B_MOUSE             Reviewed;         884 AA.
AC   Q99PV8; Q8C2I1; Q99PV6; Q99PV7; Q9JLF8;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=B-cell lymphoma/leukemia 11B;
DE            Short=BCL-11B;
DE   AltName: Full=B-cell CLL/lymphoma 11B;
DE   AltName: Full=COUP-TF-interacting protein 2;
DE   AltName: Full=Radiation-induced tumor suppressor gene 1 protein;
DE            Short=mRit1;
GN   Name=Bcl11b; Synonyms=Ctip2, Rit1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANTS
RP   THR-676; CYS-783 AND SER-849.
RX   PubMed=12565905; DOI=10.1016/S0006-291X(02)03069-3;
RA   Wakabayashi Y., Inoue J., Takahashi Y., Matsuki A., Kosugi-Okano H.,
RA   Shinbo T., Mishima Y., Niwa O., Kominami R.;
RT   "Homozygous deletions and point mutations of the Rit1/Bcl11b gene in
RT   gamma-ray induced mouse thymic lymphomas.";
RL   Biochem. Biophys. Res. Commun. 301:598-603(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH TFCOUP1;
RP   EAR2 AND ARP1.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=20209406; PubMed=10744719; DOI=10.1074/jbc.275.14.10315;
RA   Avram D., Fields A., Pretty On Top K., Nevrivy D.J., Ishmael J.E.,
RA   Leid M.;
RT   "Isolation of a novel family of C(2)H(2) zinc finger proteins
RT   implicated in transcriptional repression mediated by chicken ovalbumin
RT   upstream promoter transcription factor (COUP-TF) orphan nuclear
RT   receptors.";
RL   J. Biol. Chem. 275:10315-10322(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 331-884.
RC   STRAIN=NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   FUNCTION.
RX   PubMed=12717433; DOI=10.1038/ni927;
RA   Wakabayashi Y., Watanabe H., Inoue J., Takeda N., Sakata J.,
RA   Mishima Y., Hitomi J., Yamamoto T., Utsuyama M., Niwa O., Aizawa S.,
RA   Kominami R.;
RT   "Bcl11b is required for differentiation and survival of alphabeta T
RT   lymphocytes.";
RL   Nat. Immunol. 4:533-539(2003).
RN   [6]
RP   INTERACTION WITH SIRT1.
RX   PubMed=12930829; DOI=10.1074/jbc.M307477200;
RA   Senawong T., Peterson V.J., Avram D., Shepherd D.M., Frye R.A.,
RA   Minucci S., Leid M.;
RT   "Involvement of the histone deacetylase SIRT1 in chicken ovalbumin
RT   upstream promoter transcription factor (COUP-TF)-interacting protein
RT   2-mediated transcriptional repression.";
RL   J. Biol. Chem. 278:43041-43050(2003).
CC   -!- FUNCTION: Tumor-suppressor protein involved in T-cell lymphomas.
CC       May function on the P53-signaling pathway. May be a key regulator
CC       of both differentiation and survival during thymocyte development.
CC       Repress transcription through direct, TFCOUP2-independent binding
CC       to a GC-rich response element.
CC   -!- SUBUNIT: Interacts with TFCOUP1, SIRT1, ARP1 and EAR2.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Alpha;
CC         IsoId=Q99PV8-1; Sequence=Displayed;
CC       Name=2; Synonyms=Beta;
CC         IsoId=Q99PV8-2; Sequence=VSP_009568;
CC         Note=May be due to exon skipping;
CC       Name=3; Synonyms=Gamma;
CC         IsoId=Q99PV8-3; Sequence=VSP_009566;
CC         Note=May be due to exon skipping;
CC   -!- TISSUE SPECIFICITY: Expressed in brain and thymus.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in the developing embryo.
CC   -!- SIMILARITY: Contains 6 C2H2-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF63683.1; Type=Frameshift; Positions=135, 221, 227, 252, 259, 264;
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DR   EMBL; AB043551; BAB32728.1; -; mRNA.
DR   EMBL; AB043553; BAB32729.1; -; mRNA.
DR   EMBL; AB043583; BAB32730.1; -; mRNA.
DR   EMBL; AF186019; AAF63683.1; ALT_FRAME; mRNA.
DR   EMBL; BC019503; AAH19503.1; -; mRNA.
DR   EMBL; AK088588; BAC40438.1; -; mRNA.
DR   IPI; IPI00121608; -.
DR   IPI; IPI00407012; -.
DR   IPI; IPI00407013; -.
DR   RefSeq; NP_001073352.1; NM_001079883.1.
DR   RefSeq; NP_067374.2; NM_021399.2.
DR   UniGene; Mm.392694; -.
DR   ProteinModelPortal; Q99PV8; -.
DR   SMR; Q99PV8; 217-251, 417-566, 749-878.
DR   STRING; Q99PV8; -.
DR   PhosphoSite; Q99PV8; -.
DR   PRIDE; Q99PV8; -.
DR   Ensembl; ENSMUST00000066060; ENSMUSP00000068258; ENSMUSG00000048251.
DR   Ensembl; ENSMUST00000109891; ENSMUSP00000105517; ENSMUSG00000048251.
DR   GeneID; 58208; -.
DR   KEGG; mmu:58208; -.
DR   UCSC; uc007ozh.1; mouse.
DR   UCSC; uc007ozi.1; mouse.
DR   CTD; 58208; -.
DR   MGI; MGI:1929913; Bcl11b.
DR   GeneTree; ENSGT00530000063542; -.
DR   HOGENOM; HBG355234; -.
DR   HOVERGEN; HBG050673; -.
DR   InParanoid; Q99PV8; -.
DR   OMA; DDDAGGC; -.
DR   OrthoDB; EOG4CNQQK; -.
DR   PhylomeDB; Q99PV8; -.
DR   NextBio; 314201; -.
DR   ArrayExpress; Q99PV8; -.
DR   Bgee; Q99PV8; -.
DR   CleanEx; MM_BCL11B; -.
DR   CleanEx; MM_RIT1; -.
DR   Genevestigator; Q99PV8; -.
DR   GermOnline; ENSMUSG00000048251; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0001077; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0046632; P:alpha-beta T cell differentiation; IMP:MGI.
DR   GO; GO:0007409; P:axonogenesis; IMP:MGI.
DR   GO; GO:0003382; P:epithelial cell morphogenesis; IMP:MGI.
DR   GO; GO:0003334; P:keratinocyte development; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptosis; IMP:MGI.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IDA:MGI.
DR   GO; GO:0042475; P:odontogenesis of dentine-containing tooth; IMP:MGI.
DR   GO; GO:0043368; P:positive T cell selection; IMP:MGI.
DR   GO; GO:0031077; P:post-embryonic camera-type eye development; IMP:MGI.
DR   GO; GO:0010837; P:regulation of keratinocyte proliferation; IMP:MGI.
DR   GO; GO:0019216; P:regulation of lipid metabolic process; IMP:MGI.
DR   GO; GO:0043588; P:skin development; IMP:MGI.
DR   GO; GO:0021773; P:striatal medium spiny neuron differentiation; IMP:MGI.
DR   GO; GO:0033077; P:T cell differentiation in thymus; IMP:MGI.
DR   GO; GO:0033153; P:T cell receptor V(D)J recombination; IMP:MGI.
DR   GO; GO:0048538; P:thymus development; IMP:MGI.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 4.
DR   Pfam; PF00096; zf-C2H2; 2.
DR   SMART; SM00355; ZnF_C2H2; 6.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Metal-binding; Nucleus;
KW   Phosphoprotein; Polymorphism; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    884       B-cell lymphoma/leukemia 11B.
FT                                /FTId=PRO_0000047105.
FT   ZN_FING     221    251       C2H2-type 1.
FT   ZN_FING     426    453       C2H2-type 2.
FT   ZN_FING     454    481       C2H2-type 3.
FT   ZN_FING     786    813       C2H2-type 4.
FT   ZN_FING     814    843       C2H2-type 5.
FT   ZN_FING     844    874       C2H2-type 6.
FT   COMPBIAS    560    647       Gly-rich.
FT   MOD_RES      96     96       Phosphoserine (By similarity).
FT   MOD_RES     119    119       Phosphothreonine (By similarity).
FT   MOD_RES     256    256       Phosphoserine (By similarity).
FT   MOD_RES     260    260       Phosphothreonine (By similarity).
FT   MOD_RES     277    277       Phosphoserine (By similarity).
FT   MOD_RES     313    313       Phosphothreonine (By similarity).
FT   MOD_RES     318    318       Phosphoserine (By similarity).
FT   MOD_RES     358    358       Phosphoserine (By similarity).
FT   MOD_RES     376    376       Phosphothreonine (By similarity).
FT   MOD_RES     381    381       Phosphoserine (By similarity).
FT   MOD_RES     416    416       Phosphothreonine (By similarity).
FT   MOD_RES     482    482       Phosphoserine (By similarity).
FT   MOD_RES     487    487       Phosphoserine (By similarity).
FT   MOD_RES     492    492       Phosphoserine (By similarity).
FT   MOD_RES     495    495       Phosphoserine (By similarity).
FT   MOD_RES     496    496       Phosphoserine (By similarity).
FT   MOD_RES     664    664       Phosphoserine (By similarity).
FT   MOD_RES     744    744       Phosphothreonine (By similarity).
FT   MOD_RES     755    755       Phosphoserine (By similarity).
FT   MOD_RES     762    762       Phosphoserine (By similarity).
FT   MOD_RES     841    841       N6-acetyllysine (By similarity).
FT   VAR_SEQ      21    214       Missing (in isoform 3).
FT                                /FTId=VSP_009566.
FT   VAR_SEQ     142    213       Missing (in isoform 2).
FT                                /FTId=VSP_009568.
FT   VARIANT     676    676       K -> T (in gamma induced thymic
FT                                lymphomas).
FT   VARIANT     783    783       R -> C (in gamma induced thymic
FT                                lymphomas).
FT   VARIANT     849    849       C -> S (in gamma induced thymic
FT                                lymphomas).
FT   CONFLICT     20     20       P -> R (in Ref. 1; BAB32730).
FT   CONFLICT    379    379       P -> S (in Ref. 2; AAF63683).
FT   CONFLICT    806    807       RS -> KN (in Ref. 2; AAF63683).
SQ   SEQUENCE   884 AA;  94566 MW;  9A86B7E34450B2F2 CRC64;
     MSRRKQGNPQ HLSQRELITP EADHVEATIL EEDEGLEIEE PSSLGLMVGG PDPDLLTCGQ
     CQMNFPLGDI LVFIEHKKKQ CGGLGPCYDK VLDKSSPPPS SRSELRRVSE PVEIGIQVTP
     DEDDHLLSPT KGICPKQENI AGPCRPAQLP SMAPIAASSS HPPTSVITSP LRALGVLPPC
     FPLPCCGARP ISGDGTQGEG QMEAPFGCQC ELSGKDEPSS YICTTCKQPF NSAWFLLQHA
     QNTHGFRIYL EPGPASTSLT PRLTIPPPLG PETVAQSPLM NFLGDSNPFN LLRMTGPILR
     DHPGFGEGRL PGTPPLFSPP PRHHLDPHRL SAEEMGLVAQ HPSAFDRVMR LNPMAIDSPA
     MDFSRRLREL AGNSSTPPPV SPGRGNPMHR LLNPFQPSPK SPFLSTPPLP PMPAGTPPPQ
     PPAKSKSCEF CGKTFKFQSN LIVHRRSHTG EKPYKCQLCD HACSQASKLK RHMKTHMHKA
     GSLAGRSDDG LSAASSPEPG TSELPGDLKA ADGDFRHHES DPSLGPEPED DEDEEEEEEE
     LLLENESRPE SSFSMDSELG RGRENGGGVP PGVAGAGAAA AALADEKALA LGKVMEDAGL
     GALPQYGEKR GAFLKRAGDT GDAGAVGCGD AGAPGAVNGR GGAFAPGAEP FPALFPRKPA
     PLPSPGLGGP ALHAAKRIKV EKDLELPPAA LIPSENVYSQ WLVGYAASRH FMKDPFLGFT
     DARQSPFATS SEHSSENGSL RFSTPPGDLL DGGLSGRSGT ASGGSTPHLG GPGPGRPSSK
     EGRRSDTCEY CGKVFKNCSN LTVHRRSHTG ERPYKCELCN YACAQSSKLT RHMKTHGQIG
     KEVYRCDICQ MPFSVYSTLE KHMKKWHGEH LLTNDVKIEQ AERS
//
ID   COX6C_MOUSE             Reviewed;          76 AA.
AC   Q9CPQ1; Q52KC6;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Cytochrome c oxidase subunit 6C;
DE   AltName: Full=Cytochrome c oxidase polypeptide VIc;
GN   Name=Cox6c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   PRELIMINARY NUCLEOTIDE SEQUENCE.
RX   MEDLINE=91249818; PubMed=1645653;
RX   DOI=10.1111/j.1432-1033.1991.tb15989.x;
RA   Schneyder B., Mell O., Anthony G., Kadenbach B.;
RT   "Cross reactivity of monoclonal antibodies and cDNA hybridization
RT   suggest evolutionary relationships between cytochrome c oxidase
RT   subunits VIa and VIc and between VIIa and VIIb.";
RL   Eur. J. Biochem. 198:85-92(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 21-38 AND 48-66, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-61, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- FUNCTION: This protein is one of the nuclear-coded polypeptide
CC       chains of cytochrome c oxidase, the terminal oxidase in
CC       mitochondrial electron transport (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
CC   -!- PTM: Acetylation of Lys-61 is observed in liver mitochondria from
CC       fasted mice but not from fed mice.
CC   -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 6c family.
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DR   EMBL; AK012602; BAB28348.1; -; mRNA.
DR   EMBL; AK013459; BAB28866.1; -; mRNA.
DR   EMBL; BC024666; AAH24666.1; -; mRNA.
DR   EMBL; BC094413; AAH94413.1; -; mRNA.
DR   IPI; IPI00131771; -.
DR   PIR; S16083; S16083.
DR   RefSeq; NP_444301.1; NM_053071.2.
DR   UniGene; Mm.548; -.
DR   ProteinModelPortal; Q9CPQ1; -.
DR   SMR; Q9CPQ1; 7-76.
DR   STRING; Q9CPQ1; -.
DR   PhosphoSite; Q9CPQ1; -.
DR   PRIDE; Q9CPQ1; -.
DR   Ensembl; ENSMUST00000014457; ENSMUSP00000014457; ENSMUSG00000014313.
DR   GeneID; 12864; -.
DR   KEGG; mmu:12864; -.
DR   UCSC; uc007vmi.1; mouse.
DR   CTD; 12864; -.
DR   MGI; MGI:104614; Cox6c.
DR   eggNOG; roNOG17665; -.
DR   GeneTree; ENSGT00390000004573; -.
DR   HOGENOM; HBG505631; -.
DR   HOVERGEN; HBG051091; -.
DR   InParanoid; Q9CPQ1; -.
DR   OMA; LYKFGVA; -.
DR   OrthoDB; EOG42JNT3; -.
DR   PhylomeDB; Q9CPQ1; -.
DR   NextBio; 282432; -.
DR   ArrayExpress; Q9CPQ1; -.
DR   Bgee; Q9CPQ1; -.
DR   CleanEx; MM_COX6C; -.
DR   Genevestigator; Q9CPQ1; -.
DR   GermOnline; ENSMUSG00000014313; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:InterPro.
DR   InterPro; IPR004204; Cyt_c_oxidase_su6c.
DR   Gene3D; G3DSA:4.10.93.10; COX6C; 1.
DR   PANTHER; PTHR12916; COX6C; 1.
DR   Pfam; PF02937; COX6C; 1.
DR   ProDom; PD015032; Cyt_c_oxidase_su6c; 1.
DR   SUPFAM; SSF81415; COX6C; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Transmembrane; Transmembrane helix.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2     76       Cytochrome c oxidase subunit 6C.
FT                                /FTId=PRO_0000191302.
FT   TOPO_DOM      4     14       Mitochondrial matrix (By similarity).
FT   TRANSMEM     15     55       Helical; (By similarity).
FT   TOPO_DOM     56     76       Mitochondrial intermembrane (By
FT                                similarity).
FT   MOD_RES      61     61       N6-acetyllysine.
SQ   SEQUENCE   76 AA;  8469 MW;  BE02A028CF77D5F4 CRC64;
     MSSGALLPKP QMRGLLAKRL RVHIAGAFIV ALGVAAAYKF GVAEPRKKAY AEFYRNYDSM
     KDFEEMRKAG IFQSAK
//
ID   TOM22_MOUSE             Reviewed;         142 AA.
AC   Q9CPQ3; Q543M4; Q9D8D3;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Mitochondrial import receptor subunit TOM22 homolog;
DE   AltName: Full=Translocase of outer membrane 22 kDa subunit homolog;
GN   Name=Tomm22; Synonyms=Tom22;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2;
RC   TISSUE=Bone marrow, Hippocampus, Small intestine, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Central receptor component of the translocase of the
CC       outer membrane of mitochondria (TOM complex) responsible for the
CC       recognition and translocation of cytosolically synthesized
CC       mitochondrial preproteins. Together with the peripheral receptor
CC       TOM20 functions as the transit peptide receptor and facilitates
CC       the movement of preproteins into the translocation pore (By
CC       similarity).
CC   -!- SUBUNIT: Forms part of the preprotein translocase complex of the
CC       outer mitochondrial membrane (TOM complex) which consists of at
CC       least 7 different proteins (TOMM5, TOMM6, TOMM7, TOMM20, TOMM22,
CC       TOMM40 and TOMM70). Interacts with PPP2R2B and TOMM40 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC       membrane protein (By similarity).
CC   -!- DOMAIN: The N-terminal domain (residues 1-62) is important for
CC       binding to the unfolded mature imported proteins. Residues (49-71)
CC       of the cytoplasmic domain interacts with TOMM20 while the C-
CC       terminal segment (residues 63-82) binds presequence of
CC       preproteins. Requires the transmembrane domain (TMD), a short
CC       segment (the import sequence) in the cytoplasmic domain localizing
CC       separately from the TMD and the C-tail signal in the C-terminal
CC       domain for efficient targeting and integration into the TOM
CC       complex (By similarity).
CC   -!- SIMILARITY: Belongs to the Tom22 family.
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DR   EMBL; AK008133; BAB25482.1; -; mRNA.
DR   EMBL; AK009868; BAB26553.1; -; mRNA.
DR   EMBL; AK013471; BAB28871.1; -; mRNA.
DR   EMBL; AK049442; BAC33752.1; -; mRNA.
DR   EMBL; AK150360; BAE29495.1; -; mRNA.
DR   EMBL; AK152843; BAE31536.1; -; mRNA.
DR   EMBL; AK167803; BAE39830.1; -; mRNA.
DR   EMBL; BC056920; AAH56920.1; -; mRNA.
DR   IPI; IPI00315135; -.
DR   RefSeq; NP_766197.2; NM_172609.3.
DR   UniGene; Mm.246435; -.
DR   UniGene; Mm.477995; -.
DR   STRING; Q9CPQ3; -.
DR   PhosphoSite; Q9CPQ3; -.
DR   PRIDE; Q9CPQ3; -.
DR   Ensembl; ENSMUST00000023062; ENSMUSP00000023062; ENSMUSG00000022427.
DR   GeneID; 223696; -.
DR   KEGG; mmu:223696; -.
DR   UCSC; uc007wud.1; mouse.
DR   CTD; 223696; -.
DR   MGI; MGI:2450248; Tomm22.
DR   GeneTree; ENSGT00390000016475; -.
DR   HOGENOM; HBG380734; -.
DR   HOVERGEN; HBG061819; -.
DR   InParanoid; Q9CPQ3; -.
DR   OMA; DLEKTQV; -.
DR   OrthoDB; EOG441QD4; -.
DR   PhylomeDB; Q9CPQ3; -.
DR   NextBio; 376826; -.
DR   ArrayExpress; Q9CPQ3; -.
DR   Bgee; Q9CPQ3; -.
DR   Genevestigator; Q9CPQ3; -.
DR   GermOnline; ENSMUSG00000022427; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   InterPro; IPR005683; Tom22.
DR   Pfam; PF04281; Tom22; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   Phosphoprotein; Protein transport; Receptor; Translocation;
KW   Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    142       Mitochondrial import receptor subunit
FT                                TOM22 homolog.
FT                                /FTId=PRO_0000076108.
FT   TOPO_DOM      2     83       Cytoplasmic (Potential).
FT   TRANSMEM     84    103       Helical; (Potential).
FT   TOPO_DOM    104    142       Mitochondrial intermembrane (Potential).
FT   REGION       41     50       Import sequence; necessary for
FT                                mitochondrion outer membrane localization
FT                                and integration in the TOM complex (By
FT                                similarity).
FT   REGION       83    103       TMD; necessary for mitochondrion outer
FT                                membrane localization and integration in
FT                                the TOM complex (By similarity).
FT   REGION      123    142       C-tail signal; necessary for
FT                                mitochondrion outer membrane localization
FT                                and integration in the TOM complex (By
FT                                similarity).
FT   COMPBIAS     35     38       Poly-Asp.
FT   COMPBIAS    110    118       Poly-Gln.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      15     15       Phosphoserine (By similarity).
FT   MOD_RES      43     43       Phosphothreonine (By similarity).
FT   CONFLICT     38     38       D -> H (in Ref. 1; BAB25482).
FT   CONFLICT     65     65       A -> T (in Ref. 1; BAB25482).
SQ   SEQUENCE   142 AA;  15537 MW;  A5182A39B6EBBFDA CRC64;
     MAAAVAAAGA GEPLSPEELL PKAEAEKAEE ELEEDDDDEL DETLSERLWG LTEMFPERVR
     SAAGATFDLS LFVAQKMYRF SRAALWIGTT SFMILVLPVV FETEKLQMEQ QQQLQQRQIL
     LGPNTGLSGG MPGALPPLPG KM
//
ID   RL17_MOUSE              Reviewed;         184 AA.
AC   Q9CPR4;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=60S ribosomal protein L17;
GN   Name=Rpl17;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SIMILARITY: Belongs to the ribosomal protein L22P family.
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DR   EMBL; AK011133; BAB27424.1; -; mRNA.
DR   EMBL; AK011132; BAB27423.1; -; mRNA.
DR   IPI; IPI00453768; -.
DR   UniGene; Mm.276337; -.
DR   UniGene; Mm.471280; -.
DR   ProteinModelPortal; Q9CPR4; -.
DR   SMR; Q9CPR4; 1-168.
DR   STRING; Q9CPR4; -.
DR   PhosphoSite; Q9CPR4; -.
DR   PRIDE; Q9CPR4; -.
DR   Ensembl; ENSMUST00000075682; ENSMUSP00000096958; ENSMUSG00000062328.
DR   Ensembl; ENSMUST00000079716; ENSMUSP00000078654; ENSMUSG00000062328.
DR   UCSC; uc008fpw.1; mouse.
DR   MGI; MGI:2448270; Rpl17.
DR   GeneTree; ENSGT00390000014873; -.
DR   HOVERGEN; HBG000955; -.
DR   InParanoid; Q9CPR4; -.
DR   OrthoDB; EOG4WWRKV; -.
DR   PhylomeDB; Q9CPR4; -.
DR   Bgee; Q9CPR4; -.
DR   CleanEx; MM_RPL17; -.
DR   Genevestigator; Q9CPR4; -.
DR   GermOnline; ENSMUSG00000062328; Mus musculus.
DR   GermOnline; ENSMUSG00000067748; Mus musculus.
DR   GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR001063; Ribosomal_L22.
DR   InterPro; IPR018260; Ribosomal_L22/L17_CS.
DR   InterPro; IPR005721; Ribosomal_L22/L17_euk/arc.
DR   Gene3D; G3DSA:3.90.470.10; Ribosomal_L22; 1.
DR   PANTHER; PTHR11593; Ribosomal_L22/17; 1.
DR   Pfam; PF00237; Ribosomal_L22; 1.
DR   SUPFAM; SSF54843; Ribosomal_L22; 1.
DR   TIGRFAMs; TIGR01038; L22_arch; 1.
DR   PROSITE; PS00464; RIBOSOMAL_L22; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein; Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    184       60S ribosomal protein L17.
FT                                /FTId=PRO_0000125333.
FT   MOD_RES       5      5       Phosphoserine (By similarity).
SQ   SEQUENCE   184 AA;  21423 MW;  3337867F610D1CA0 CRC64;
     MVRYSLDPEN PTKSCKSRGS NLRVHFKNTR ETAQAIKGMH IRKATKYLKD VTLKKQCVPF
     RRYNGGVGRC AQAKQWGWTQ GRWPKKSAEF LLHMLKNAES NAELKGLDVD SLVIEHIQVN
     KAPKMRRRTY RAHGRINPYM SSPCHIEMIL TEKEQIVPKP EEEVAQKKKI SQKKLKKQKL
     MPRE
//
ID   SIKE1_MOUSE             Reviewed;         207 AA.
AC   Q9CPR7; Q8CBP5;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Suppressor of IKBKE 1;
DE   AltName: Full=Suppressor of IKK-epsilon;
GN   Name=Sike1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Colon, Head, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Physiological suppressor of IKK-epsilon and TBK1 that
CC       plays an inhibitory role in virus- and TLR3-triggered IRF3.
CC       Inhibits TLR3-mediated activation of interferon-stimulated
CC       response elements (ISRE) and the IFN-beta promoter. May act by
CC       disrupting the interactions of IKBKE or TBK1 with TICAM1/TRIF,
CC       IRF3 and DDX58/RIG-I. Does not inhibit NF-kappa-B activation
CC       pathways (By similarity).
CC   -!- SUBUNIT: Interacts with IKBKE and TBK1 via its coiled coil region.
CC       Interaction with TBK1 is disrupted upon viral infection or TLR3
CC       stimulation (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the SIKE family.
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DR   EMBL; AK014113; BAB29165.1; -; mRNA.
DR   EMBL; AK014247; BAB29223.1; -; mRNA.
DR   EMBL; AK017694; BAB30879.1; -; mRNA.
DR   EMBL; AK019264; BAB31636.1; -; mRNA.
DR   EMBL; AK033553; BAC28353.1; -; mRNA.
DR   EMBL; AK035590; BAC29116.1; -; mRNA.
DR   EMBL; BC004090; AAH04090.1; -; mRNA.
DR   IPI; IPI00461173; -.
DR   RefSeq; NP_079955.1; NM_025679.3.
DR   UniGene; Mm.208619; -.
DR   UniGene; Mm.33937; -.
DR   ProteinModelPortal; Q9CPR7; -.
DR   IntAct; Q9CPR7; 1.
DR   PhosphoSite; Q9CPR7; -.
DR   PRIDE; Q9CPR7; -.
DR   Ensembl; ENSMUST00000029447; ENSMUSP00000029447; ENSMUSG00000027854.
DR   GeneID; 66641; -.
DR   KEGG; mmu:66641; -.
DR   UCSC; uc008qsf.1; mouse.
DR   CTD; 66641; -.
DR   MGI; MGI:1913891; Sike1.
DR   eggNOG; roNOG17271; -.
DR   GeneTree; ENSGT00390000018003; -.
DR   HOGENOM; HBG445550; -.
DR   HOVERGEN; HBG055808; -.
DR   InParanoid; Q9CPR7; -.
DR   OMA; QYQEDAS; -.
DR   OrthoDB; EOG4BG8X5; -.
DR   PhylomeDB; Q9CPR7; -.
DR   NextBio; 322249; -.
DR   ArrayExpress; Q9CPR7; -.
DR   Bgee; Q9CPR7; -.
DR   CleanEx; MM_5730470L24RIK; -.
DR   Genevestigator; Q9CPR7; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR008555; DUF837.
DR   PANTHER; PTHR12186; DUF837; 1.
DR   Pfam; PF05769; DUF837; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Phosphoprotein.
FT   CHAIN         1    207       Suppressor of IKBKE 1.
FT                                /FTId=PRO_0000299051.
FT   COILED       70    102       Potential.
FT   COILED      164    192       Potential.
FT   MOD_RES      74     74       Phosphoserine (By similarity).
FT   CONFLICT     64     64       M -> V (in Ref. 1; BAC29116).
SQ   SEQUENCE   207 AA;  23522 MW;  FF12E0F36B948437 CRC64;
     MSCTIEKILT DAKTLLERLR EHDAAAESLV DQSAALHRRV AAMREAGAVL PEQYQEDASD
     VKDMSKYKPH ILLSQENTQI RDLQQENREL WVSLEEHQDA LELIMSKYRK QMLQLMVAKK
     AVDAEPVLKA HQSHSAEIES QIDRICEMGA VMRRAVQVDD NQFCKVQERL AQLELENKEL
     RELLSISSES LQVGKESSVA PASQTIK
//
ID   CB088_MOUSE             Reviewed;         106 AA.
AC   Q9CPS8;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=UPF0733 protein C2orf88 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-40, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SIMILARITY: Belongs to the UPF0733 family.
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DR   EMBL; AK006110; BAB24413.1; -; mRNA.
DR   EMBL; AK006523; BAB24632.1; -; mRNA.
DR   EMBL; AK010796; BAB27186.1; -; mRNA.
DR   EMBL; BC048645; AAH48645.1; -; mRNA.
DR   IPI; IPI00131912; -.
DR   RefSeq; NP_659202.1; NM_144953.2.
DR   UniGene; Mm.236287; -.
DR   PhosphoSite; Q9CPS8; -.
DR   PRIDE; Q9CPS8; -.
DR   Ensembl; ENSMUST00000050567; ENSMUSP00000055413; ENSMUSG00000043629.
DR   Ensembl; ENSMUST00000114492; ENSMUSP00000110136; ENSMUSG00000043629.
DR   Ensembl; ENSMUST00000114493; ENSMUSP00000110137; ENSMUSG00000043629.
DR   GeneID; 67080; -.
DR   KEGG; mmu:67080; -.
DR   UCSC; uc007ayr.1; mouse.
DR   MGI; MGI:1914330; 1700019D03Rik.
DR   eggNOG; maNOG21561; -.
DR   GeneTree; ENSGT00390000011537; -.
DR   InParanoid; Q9CPS8; -.
DR   OMA; KQTFPFP; -.
DR   OrthoDB; EOG4X3H2W; -.
DR   NextBio; 323514; -.
DR   ArrayExpress; Q9CPS8; -.
DR   Bgee; Q9CPS8; -.
DR   Genevestigator; Q9CPS8; -.
PE   1: Evidence at protein level;
KW   Lipoprotein; Myristate; Phosphoprotein.
FT   INIT_MET      1      1       Removed (Potential).
FT   CHAIN         2    106       UPF0733 protein C2orf88 homolog.
FT                                /FTId=PRO_0000348431.
FT   MOD_RES      24     24       Phosphoserine.
FT   MOD_RES      40     40       Phosphoserine.
FT   LIPID         2      2       N-myristoyl glycine (Potential).
SQ   SEQUENCE   106 AA;  11926 MW;  FB7560A5419DD80A CRC64;
     MGCMKSKETF PFPTTLDIDK LHESEEAFIP DDSSQYRTPS PGEQQQVQEV KKLPEPGAVI
     GALILEFADR LASEIVEDAL QQWACENIQY YNIPYIESEG SDTTIN
//
ID   GLOD4_MOUSE             Reviewed;         298 AA.
AC   Q9CPV4; Q3UUS8; Q9CY26; Q9D9F5;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Glyoxalase domain-containing protein 4;
GN   Name=Glod4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Liver, Testis, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBUNIT: Interacts with NUDT9 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9CPV4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CPV4-2; Sequence=VSP_023650, VSP_023651;
CC       Name=3;
CC         IsoId=Q9CPV4-3; Sequence=VSP_023649;
CC   -!- SIMILARITY: Belongs to the glyoxalase I family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK006979; BAB24818.1; -; mRNA.
DR   EMBL; AK010992; BAB27311.1; -; mRNA.
DR   EMBL; AK012569; BAB28324.1; -; mRNA.
DR   EMBL; AK013212; BAB28716.1; -; mRNA.
DR   EMBL; AK138073; BAE23546.1; -; mRNA.
DR   EMBL; AL591129; CAI35102.1; -; Genomic_DNA.
DR   EMBL; BC061012; AAH61012.1; -; mRNA.
DR   IPI; IPI00110721; -.
DR   IPI; IPI00112630; -.
DR   IPI; IPI00831130; -.
DR   RefSeq; NP_080305.2; NM_026029.3.
DR   UniGene; Mm.46397; -.
DR   HSSP; Q4FWG9; 2C21.
DR   ProteinModelPortal; Q9CPV4; -.
DR   SMR; Q9CPV4; 5-132, 138-258.
DR   STRING; Q9CPV4; -.
DR   PhosphoSite; Q9CPV4; -.
DR   REPRODUCTION-2DPAGE; Q9CPV4; -.
DR   PRIDE; Q9CPV4; -.
DR   Ensembl; ENSMUST00000017430; ENSMUSP00000017430; ENSMUSG00000017286.
DR   Ensembl; ENSMUST00000021205; ENSMUSP00000021205; ENSMUSG00000017286.
DR   GeneID; 67201; -.
DR   KEGG; mmu:67201; -.
DR   UCSC; uc007kfl.1; mouse.
DR   CTD; 67201; -.
DR   MGI; MGI:1914451; Glod4.
DR   eggNOG; roNOG14244; -.
DR   GeneTree; ENSGT00390000012340; -.
DR   HOGENOM; HBG382066; -.
DR   HOVERGEN; HBG056038; -.
DR   InParanoid; Q9CPV4; -.
DR   OMA; YRLGNDF; -.
DR   OrthoDB; EOG4SF95R; -.
DR   NextBio; 323864; -.
DR   ArrayExpress; Q9CPV4; -.
DR   Bgee; Q9CPV4; -.
DR   CleanEx; MM_GLOD4; -.
DR   Genevestigator; Q9CPV4; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Mitochondrion.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    298       Glyoxalase domain-containing protein 4.
FT                                /FTId=PRO_0000280392.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   VAR_SEQ       1     30       MATRRALHFVFKVKNRFQTVHFFRDVLGMQ -> MICGSVL
FT                                NSPD (in isoform 3).
FT                                /FTId=VSP_023649.
FT   VAR_SEQ     278    291       AMEADKSDEWFATR -> GEGCTDRVRTANPG (in
FT                                isoform 2).
FT                                /FTId=VSP_023650.
FT   VAR_SEQ     292    298       Missing (in isoform 2).
FT                                /FTId=VSP_023651.
FT   CONFLICT     46     46       N -> Y (in Ref. 1; BAB27311).
FT   CONFLICT     84     84       N -> K (in Ref. 1; BAB24818).
FT   CONFLICT    214    214       L -> I (in Ref. 1; BAB27311).
SQ   SEQUENCE   298 AA;  33317 MW;  F2CD5FD2387A78CE CRC64;
     MATRRALHFV FKVKNRFQTV HFFRDVLGMQ VLRHEEFEEG CKAACNGPYD GKWSKTMVGF
     GPEDDHFVAE LTYNYGIGDY KLGNDFMGIT LASSQAVSNA RKLEWPLSKV AEGIFETEAP
     GGYKFYLQDR SPSQSDPVLK VTLAVSDLQK SLNYWSNLLG MKIYEQDEEK QRALLGYADN
     QCKLELQGIQ GAVDHAAAFG RIAFSCPQKE LPDLEDLMKR ESHSILTPLV SLDTPGKATV
     QVVILADPDG HEICFVGDEA FRELSKMDPK GSKLLDDAME ADKSDEWFAT RNKPKASG
//
ID   CNTP2_MOUSE             Reviewed;        1332 AA.
AC   Q9CPW0; Q6P2K4; Q6ZQ31;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Contactin-associated protein-like 2;
DE   AltName: Full=Cell recognition molecule Caspr2;
DE   Flags: Precursor;
GN   Name=Cntnap2; Synonyms=Kiaa0868;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 295-1332 (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   CHARACTERIZATION.
RX   MEDLINE=21450957; PubMed=11567047;
RA   Poliak S., Gollan L., Salomon D., Berglund E.O., Ohara R., Ranscht B.,
RA   Peles E.;
RT   "Localization of Caspr2 in myelinated nerves depends on axon-glia
RT   interactions and the generation of barriers along the axon.";
RL   J. Neurosci. 21:7568-7575(2001).
CC   -!- FUNCTION: May play a role in the formation of functional distinct
CC       domains critical for saltatory conduction of nerve impulses in
CC       myelinated nerve fibers. Seems to demarcate the juxtaparanodal
CC       region of the axo-glial junction.
CC   -!- SUBUNIT: Associates with KCNA2.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9CPW0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CPW0-2; Sequence=VSP_014977;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: In sciatic nerve predominantly found at the
CC       juxtaparanodal regions.
CC   -!- DEVELOPMENTAL STAGE: Detected at postnatal day 8 in sciatic nerve
CC       at the paranodes and the juxtaparanodal region. Is progressively
CC       translocated to the adjacent juxtaparanodal region until it
CC       becomes completely absent from the paranodes in the adult.
CC   -!- SIMILARITY: Belongs to the neurexin family.
CC   -!- SIMILARITY: Contains 2 EGF-like domains.
CC   -!- SIMILARITY: Contains 1 F5/8 type C domain.
CC   -!- SIMILARITY: Contains 1 fibrinogen C-terminal domain.
CC   -!- SIMILARITY: Contains 4 laminin G-like domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98042.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK017341; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK013139; BAB28674.1; -; mRNA.
DR   EMBL; AK129232; BAC98042.1; ALT_INIT; mRNA.
DR   EMBL; BC029826; AAH29826.1; -; mRNA.
DR   EMBL; BC064467; AAH64467.1; -; mRNA.
DR   IPI; IPI00420554; -.
DR   IPI; IPI00467267; -.
DR   RefSeq; NP_001004357.2; NM_001004357.2.
DR   RefSeq; NP_080047.1; NM_025771.3.
DR   UniGene; Mm.440084; -.
DR   UniGene; Mm.477298; -.
DR   ProteinModelPortal; Q9CPW0; -.
DR   SMR; Q9CPW0; 31-536, 555-597, 799-951, 970-1003.
DR   STRING; Q9CPW0; -.
DR   PRIDE; Q9CPW0; -.
DR   Ensembl; ENSMUST00000060839; ENSMUSP00000056299; ENSMUSG00000039419.
DR   Ensembl; ENSMUST00000069147; ENSMUSP00000064082; ENSMUSG00000039419.
DR   Ensembl; ENSMUST00000114641; ENSMUSP00000110288; ENSMUSG00000039419.
DR   GeneID; 66797; -.
DR   KEGG; mmu:66797; -.
DR   UCSC; uc009bst.1; mouse.
DR   UCSC; uc009bsx.1; mouse.
DR   CTD; 66797; -.
DR   MGI; MGI:1914047; Cntnap2.
DR   GeneTree; ENSGT00560000076804; -.
DR   HOGENOM; HBG443585; -.
DR   HOVERGEN; HBG057718; -.
DR   InParanoid; Q9CPW0; -.
DR   OrthoDB; EOG4RV2QH; -.
DR   NextBio; 322675; -.
DR   ArrayExpress; Q9CPW0; -.
DR   Bgee; Q9CPW0; -.
DR   CleanEx; MM_CNTNAP2; -.
DR   Genevestigator; Q9CPW0; -.
DR   GermOnline; ENSMUSG00000039419; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0044224; C:juxtaparanode region of axon; IDA:BHF-UCL.
DR   GO; GO:0005102; F:receptor binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; TAS:BHF-UCL.
DR   GO; GO:0045163; P:clustering of voltage-gated potassium channels; IMP:BHF-UCL.
DR   GO; GO:0021761; P:limbic system development; IEP:BHF-UCL.
DR   GO; GO:0031175; P:neuron projection development; IGI:MGI.
DR   GO; GO:0008038; P:neuron recognition; TAS:BHF-UCL.
DR   GO; GO:0071205; P:protein localization to juxtaparanode region of axon; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR000421; Coagulation_factor_5/8-type_C.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   InterPro; IPR006209; EGF.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR002181; Fibrinogen_a/b/g_C.
DR   InterPro; IPR008979; Galactose-bd-like.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR012680; Laminin_G_2.
DR   InterPro; IPR003585; Neurexin-like.
DR   Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 5.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF00754; F5_F8_type_C; 1.
DR   Pfam; PF02210; Laminin_G_2; 4.
DR   SMART; SM00294; 4.1m; 1.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00231; FA58C; 1.
DR   SMART; SM00282; LamG; 4.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 4.
DR   SUPFAM; SSF56496; Fibrinogen_a/b/g_C; 1.
DR   SUPFAM; SSF49785; Gal_bind_like; 1.
DR   PROSITE; PS00022; EGF_1; FALSE_NEG.
DR   PROSITE; PS01186; EGF_2; FALSE_NEG.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01285; FA58C_1; 1.
DR   PROSITE; PS01286; FA58C_2; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
DR   PROSITE; PS00514; FIBRINOGEN_C_1; FALSE_NEG.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Membrane; Phosphoprotein; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     27       Potential.
FT   CHAIN        28   1332       Contactin-associated protein-like 2.
FT                                /FTId=PRO_0000019507.
FT   TOPO_DOM     28   1262       Extracellular (Potential).
FT   TRANSMEM   1263   1283       Helical; (Potential).
FT   TOPO_DOM   1284   1332       Cytoplasmic (Potential).
FT   DOMAIN       35    181       F5/8 type C.
FT   DOMAIN      187    368       Laminin G-like 1.
FT   DOMAIN      373    552       Laminin G-like 2.
FT   DOMAIN      554    591       EGF-like 1.
FT   DOMAIN      592    798       Fibrinogen C-terminal.
FT   DOMAIN      799    963       Laminin G-like 3.
FT   DOMAIN      964   1002       EGF-like 2.
FT   DOMAIN     1023   1214       Laminin G-like 4.
FT   MOD_RES    1304   1304       Phosphoserine (By similarity).
FT   MOD_RES    1307   1307       Phosphoserine (By similarity).
FT   CARBOHYD    289    289       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    346    346       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    363    363       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    379    379       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    436    436       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    507    507       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    546    546       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    630    630       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    735    735       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1117   1117       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1199   1199       N-linked (GlcNAc...) (Potential).
FT   DISULFID     35    181       By similarity.
FT   DISULFID    336    368       By similarity.
FT   DISULFID    520    552       By similarity.
FT   DISULFID    558    569       By similarity.
FT   DISULFID    563    578       By similarity.
FT   DISULFID    580    590       By similarity.
FT   DISULFID    936    963       By similarity.
FT   DISULFID    967    980       By similarity.
FT   DISULFID    974    989       By similarity.
FT   DISULFID    991   1001       By similarity.
FT   DISULFID   1179   1215       By similarity.
FT   VAR_SEQ       1   1224       Missing (in isoform 2).
FT                                /FTId=VSP_014977.
FT   CONFLICT    357    357       G -> E (in Ref. 3; AAH64467).
FT   CONFLICT    538    538       Q -> H (in Ref. 3; AAH64467).
FT   CONFLICT   1192   1192       K -> N (in Ref. 3; AAH64467).
SQ   SEQUENCE   1332 AA;  148197 MW;  6AA097C69D83F0A5 CRC64;
     MVMSLRAGYR AALSLWILSS FICRAWTAPS TFQKCDEPLI SGLPHVSFSS SSSLSSSYAP
     GYAKINKRGG AGGWSPSDSD HYQWLQVDFG NRKQISAIAT QGRYSSSDWV TQYRMLYSDT
     GRNWKPYHQD GNIWAFPGNI NSDSVVRHDL QHAVVARYVR IVPLDWNGEG HIGLRAEVYG
     CAYWADVINF DGHGVLPYRF RNKKMKTLKD VIALKFKTSE SEGVLLHGEG QQGDYITLEL
     KKAKLVLSLN LGSNQLGPIY GHTSVTSGSL LDDHHWHSVL IERQGRSINL TLDRSMQHFR
     TNGEFDYLDL DYEITFGGIP FSGKPSSSNR KNFKGCMESI NYNGVNITDL ARRKKLGPSN
     MGNLSFSCVE PYTVPVFFNA TSYLEVPGRL NQDLFSVSFQ FRTWNPSGLL LFSHFADNLG
     NVEIDLVESK VGVHINNTQT KTSQIDISSG SGLNDGQWHE VRFLAKENFA VLTIDGDEAS
     AVRTNSPLQV KTGEKYFFGG FLNHMNNASY SALQPSFQGC MQLIQVDDQL VNLYEVAQRK
     PGSFANVTID MCAIIDRCVP NHCEHGGKCS QTWDSFKCTC DETGYSGATC HNSIYEPSCE
     AYKHLGQTSN YYWIDPDGSG PLGPLKVYCN MTEDKVWTIV SHDLQMQTTV VGYNPEKYSV
     TQLIYSASMD QISAITSSAE YCEQYVSYFC RMSRLLNTPD GSPYTWWVGK ANEKHYYWGG
     SEPGIQKCAC GIERNCTDPK YYCNCDADYK QWRKDAGFLS YKDHLPVSQV VVGDTDRQGS
     EAKLSVGPLR CQGDRNYWNA ASFPNPSSYL HFSTFQGETS ADISFYFKTL IPRGVFLENL
     GNTDFIKLEL KSATEVSFSF DVGNGPVEIV VRSPSPLNDD QWHRVTAERN VKQASLQVDR
     LPQQIRKAPT EGHTRLELYS QLFVGGAGGQ QGFLGCIRSL RMNGVTLDLE ERAKVTSGFK
     SGCSGHCTSY GANCENGGKC IEKYHGYSCD CSNTAYDGTF CNKDVGAFFE EGMWLRYNFQ
     APAVTARDTG SRAENSADQQ QHLAPDLAQE QIHFSFSTTK APCILLYVSS LTTDFLAVLV
     KPTGNLQIRY NLGGTREPFN IDVDHRNMAN GQPHSVNITR HERTIILKLD HYPAVGYHLP
     SSSDTLFNSP KSLFLGKVIE TGKIDQEIHK YNTPGFTGCL SRVQFNHIAP LKAALRQTNA
     SAHVHIQGEL VESNCGASPL TLSPMSSATD PWHLDHLDSA SADFPYNPGQ GQAIRNGVNR
     NSAIIGGVIA VVIFTILCTL VFLIRYMFRH KGTYHTNEAK GAESAESADA AIMNNDPNFT
     ETIDESKKEW LI
//
ID   ADXL_MOUSE              Reviewed;         174 AA.
AC   Q9CPW2; Q6P8M0; Q9CV00;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Adrenodoxin-like protein, mitochondrial;
DE   AltName: Full=Ferredoxin-1-like protein;
DE   Flags: Precursor;
GN   Name=Fdx1l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Small intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- COFACTOR: Binds 1 2Fe-2S cluster (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9CPW2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CPW2-2; Sequence=VSP_032498;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC   -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB26771.1; Type=Frameshift; Positions=10;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK008401; BAB25650.1; -; mRNA.
DR   EMBL; AK010211; BAB26771.1; ALT_FRAME; mRNA.
DR   EMBL; AK020979; BAB32267.1; -; mRNA.
DR   EMBL; BC061189; AAH61189.1; -; mRNA.
DR   IPI; IPI00132087; -.
DR   IPI; IPI00889305; -.
DR   RefSeq; NP_001034913.1; NM_001039824.2.
DR   UniGene; Mm.196137; -.
DR   HSSP; P00259; 1XLQ.
DR   ProteinModelPortal; Q9CPW2; -.
DR   SMR; Q9CPW2; 56-158.
DR   PRIDE; Q9CPW2; -.
DR   Ensembl; ENSMUST00000010348; ENSMUSP00000010348; ENSMUSG00000079677.
DR   GeneID; 68165; -.
DR   KEGG; mmu:68165; -.
DR   NMPDR; fig|10090.3.peg.19710; -.
DR   UCSC; uc009okb.1; mouse.
DR   CTD; 68165; -.
DR   MGI; MGI:1915415; Fdx1l.
DR   GeneTree; ENSGT00530000063577; -.
DR   HOGENOM; HBG524254; -.
DR   HOVERGEN; HBG055801; -.
DR   InParanoid; Q9CPW2; -.
DR   OMA; KFRATGS; -.
DR   OrthoDB; EOG4MKNHB; -.
DR   PhylomeDB; Q9CPW2; -.
DR   NextBio; 326570; -.
DR   CleanEx; MM_FDX1L; -.
DR   Genevestigator; Q9CPW2; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001055; Adrenodoxin.
DR   InterPro; IPR018298; Adrenodoxin_Fe-S_BS.
DR   InterPro; IPR012675; Beta-grasp_ferredoxin-type.
DR   InterPro; IPR001041; Ferredoxin.
DR   Gene3D; G3DSA:3.10.20.30; Ferredoxin_fold; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   PRINTS; PR00355; ADRENODOXIN.
DR   SUPFAM; SSF54292; Ferredoxin; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS00814; ADX; 1.
PE   2: Evidence at transcript level;
KW   2Fe-2S; Alternative splicing; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Mitochondrion; Transit peptide; Transport.
FT   TRANSIT       1     43       Mitochondrion (Potential).
FT   CHAIN        44    174       Adrenodoxin-like protein, mitochondrial.
FT                                /FTId=PRO_0000325953.
FT   DOMAIN       59    161       2Fe-2S ferredoxin-type.
FT   METAL        96     96       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL       102    102       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL       105    105       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL       142    142       Iron-sulfur (2Fe-2S) (By similarity).
FT   VAR_SEQ       1    126       Missing (in isoform 2).
FT                                /FTId=VSP_032498.
FT   CONFLICT     11     11       A -> G (in Ref. 1; BAB26771).
SQ   SEQUENCE   174 AA;  18766 MW;  F0E2506668F7038A CRC64;
     MAASMARGVS ARVLLRAAGG SWGPRAGHAA VTSRTFGTTG ERRAGEEAAD SPELPRDVVN
     VVFVDRSGKR IPVRGKVGDN VLYLAQRHGV DLEGACEASL ACSTCHVYVS EAHLDLLPPP
     EEREDDMLDM APLLQENSRL GCQIVLTPEL EGVEFALPKI TRNFYVDGHI PKPH
//
ID   CHMP3_MOUSE             Reviewed;         224 AA.
AC   Q9CQ10; Q9D2Z2; Q9D7A5;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Charged multivesicular body protein 3;
DE   AltName: Full=Chromatin-modifying protein 3;
DE   AltName: Full=Vacuolar protein sorting-associated protein 24;
GN   Name=Vps24; Synonyms=Chmp3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cecum, Testis, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
CC   -!- FUNCTION: Probable core component of the endosomal sorting
CC       required for transport complex III (ESCRT-III) which is involved
CC       in multivesicular bodies (MVBs) formation and sorting of endosomal
CC       cargo proteins into MVBs. MVBs contain intraluminal vesicles
CC       (ILVs) that are generated by invagination and scission from the
CC       limiting membrane of the endosome and mostly are delivered to
CC       lysosomes enabling degradation of membrane proteins, such as
CC       stimulated growth factor receptors, lysosomal enzymes and lipids.
CC       The MVB pathway appears to require the sequential function of
CC       ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly
CC       dissociate from the invaginating membrane before the ILV is
CC       released. The ESCRT machinery also functions in topologically
CC       equivalent membrane fission events, such as the terminal stages of
CC       cytokinesis. ESCRT-III proteins are believed to mediate the
CC       necessary vesicle extrusion and/or membrane fission activities,
CC       possibly in conjunction with the AAA ATPase VPS4. Selectively
CC       binds to phosphatidylinositol 3,5-bisphosphate PtdIns(3,5)P2 and
CC       PtdIns(3,4)P2 in preference to other phosphoinositides tested.
CC       Involved in late stages of cytokinesis. Required for
CC       sorting/trafficking of EGF receptor (By similarity).
CC   -!- SUBUNIT: Probable core component of the endosomal sorting required
CC       for transport complex III (ESCRT-III). ESCRT-III components are
CC       thought to multimerize to form a flat lattice on the perimeter
CC       membrane of the endosome. Several assembly forms of ESCRT-III may
CC       exist that interact and act sequentally. Forms a metastable
CC       monomer in solution; its core structure (without part of the
CC       putative autoinhibitory C-terminal acidic region) oligomerizes
CC       into a flat lattice via two different dimerization interfaces. In
CC       vitro, heteromerizes with CHMP2A (but not CHMP4) to form helical
CC       tubular structures that expose membrane-interacting sites on the
CC       outside whereas VPS4B can associate on the inside of the tubule.
CC       May interact with IGFBP7; the relevance of such interaction
CC       however remains unclear. Interacts with CHMP2A. Interacts with
CC       CHMP4A; the interaction requires the release of CHMP4A
CC       autoinhibition. Interacts with VPS4A. Interacts with STAMBP; the
CC       interaction appears to relieve the autoinhibition of CHMP3 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity).
CC       Membrane; Lipid-anchor (By similarity). Endosome (By similarity).
CC       Late endosome membrane (By similarity). Note=Localizes to the
CC       midbody of dividing cells (By similarity).
CC   -!- DOMAIN: The acidic C-terminus and the basic N-termminus are
CC       thought to render the protein in a closed, soluble and inactive
CC       conformation through an autoinhibitory intramolecular interaction.
CC       The open and active conformation, which enables membrane binding
CC       and oligomerization, is achieved by interaction with other
CC       cellular binding partners, probably including other ESCRT
CC       components.
CC   -!- SIMILARITY: Belongs to the SNF7 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK009414; BAB26273.1; -; mRNA.
DR   EMBL; AK014818; BAB29566.1; -; mRNA.
DR   EMBL; AK016677; BAB30375.1; -; mRNA.
DR   EMBL; AK018611; BAB31306.1; -; mRNA.
DR   EMBL; AK083562; BAC38951.1; -; mRNA.
DR   EMBL; BC049964; AAH49964.1; -; mRNA.
DR   IPI; IPI00347275; -.
DR   RefSeq; NP_080059.2; NM_025783.3.
DR   UniGene; Mm.181278; -.
DR   ProteinModelPortal; Q9CQ10; -.
DR   SMR; Q9CQ10; 5-181.
DR   STRING; Q9CQ10; -.
DR   PhosphoSite; Q9CQ10; -.
DR   PRIDE; Q9CQ10; -.
DR   Ensembl; ENSMUST00000059462; ENSMUSP00000109815; ENSMUSG00000053119.
DR   Ensembl; ENSMUST00000065364; ENSMUSP00000068410; ENSMUSG00000053119.
DR   GeneID; 66700; -.
DR   KEGG; mmu:66700; -.
DR   UCSC; uc009cgw.1; mouse.
DR   CTD; 66700; -.
DR   MGI; MGI:1913950; Vps24.
DR   eggNOG; roNOG15553; -.
DR   GeneTree; ENSGT00550000074896; -.
DR   HOGENOM; HBG713119; -.
DR   HOVERGEN; HBG107031; -.
DR   InParanoid; Q9CQ10; -.
DR   OMA; CVILAKE; -.
DR   OrthoDB; EOG4VT5ZB; -.
DR   PhylomeDB; Q9CQ10; -.
DR   NextBio; 322405; -.
DR   ArrayExpress; Q9CQ10; -.
DR   Bgee; Q9CQ10; -.
DR   CleanEx; MM_VPS24; -.
DR   Genevestigator; Q9CQ10; -.
DR   GermOnline; ENSMUSG00000053119; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR005024; Snf7.
DR   Pfam; PF03357; Snf7; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Coiled coil; Cytoplasm; Endosome;
KW   Isopeptide bond; Lipoprotein; Membrane; Myristate; Phosphoprotein;
KW   Protein transport; Transport; Ubl conjugation.
FT   INIT_MET      1      1       Removed (Potential).
FT   CHAIN         2    224       Charged multivesicular body protein 3.
FT                                /FTId=PRO_0000211481.
FT   REGION        2    113       Intramolecular interaction with C-
FT                                terminus (By similarity).
FT   REGION      151    224       Interaction with VPS4A (By similarity).
FT   REGION      151    222       Intramolecular interaction with N-
FT                                terminus (By similarity).
FT   REGION      196    224       Interaction with STAMBP (By similarity).
FT   COILED       22     54       Potential.
FT   COILED      149    224       Potential.
FT   MOTIF       201    213       MIT-interacting motif (By similarity).
FT   MOD_RES     116    116       Phosphoserine (By similarity).
FT   MOD_RES     126    126       Phosphothreonine (By similarity).
FT   MOD_RES     200    200       Phosphoserine.
FT   LIPID         2      2       N-myristoyl glycine (Potential).
FT   CROSSLNK    179    179       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CONFLICT      7      7       T -> S (in Ref. 1; BAB26273).
FT   CONFLICT    161    161       A -> V (in Ref. 1; BAB31306).
FT   CONFLICT    170    170       F -> L (in Ref. 1; BAB31306).
SQ   SEQUENCE   224 AA;  25219 MW;  DC1A566E86D82A07 CRC64;
     MGLFGKTQEK PPKELVNEWS LKIRKEMRVV DRQIRDIQRE EEKVKRSVKD AAKKGQKEVC
     VVLAKEMIRS RKAVSKLYAS KAHMNSVLMG MKNQLAVLRV AGSLQKSTEV MKAMQSLVKI
     PEIQATMREL SKEMMKAGII EEMLEDTFES MDDQEEMEEA AEMEIDRILF EITAGALGKA
     PSKVTDALPE PEPAGAMAAS EEGEEEEDEE DLEAMQSRLA TLRS
//
ID   PDRO_MOUSE              Reviewed;         161 AA.
AC   Q9CQ22; Q9CYS0;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Ragulator complex protein PDRO;
DE   AltName: Full=p27Kip1-releasing factor from RhoA;
DE            Short=p27RF-Rho;
GN   Name=Pdro;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Head, Ovary, Tongue, and Uterus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N; TISSUE=Lung, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-28, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH MAPKSP1 AND ROBLD3,
RP   AND DEVELOPMENTAL STAGE.
RX   PubMed=19177150; DOI=10.1038/emboj.2008.308;
RA   Nada S., Hondo A., Kasai A., Koike M., Saito K., Uchiyama Y.,
RA   Okada M.;
RT   "The novel lipid raft adaptor p18 controls endosome dynamics by
RT   anchoring the MEK-ERK pathway to late endosomes.";
RL   EMBO J. 28:477-489(2009).
CC   -!- FUNCTION: Regulator of the TOR pathway, a signaling cascade that
CC       promotes cell growth in response to growth factors, energy levels,
CC       and amino acids. As part of the Ragulator complex, recruits the
CC       Rag GTPases and the mTORC1 complex to lysosomes, a key step in
CC       activation of the TOR signaling cascade by amino acids. Directly
CC       responsible for anchoring the Ragulator complex to membranes. Also
CC       required for late endosomes/lysosomes biogenesis it may regulate
CC       both the recycling of receptors through endosomes and the MAPK
CC       signaling pathway through recruitment of some of its components to
CC       late endosomes. May be involved in cholesterol homeostasis
CC       regulating LDL uptake and cholesterol release from late
CC       endosomes/lysosomes. May also play a role in RHOA activation.
CC   -!- SUBUNIT: Part of the Ragulator complex composed of PDRO, MAPKSP1
CC       and ROBLD3 (By similarity). Interacts with MAPKSP1 and ROBLD3; the
CC       interaction is direct. The Ragulator complex interacts with both
CC       the mTORC1 complex and heterodimers of the Rag GTPases RRAGA,
CC       RRAGB, RRAGC and RRAGD (By similarity). Interacts with RRAGB and
CC       RRAGD; the interaction is direct indicating that it probably
CC       constitutes the main RAG-interacting subunit of the Ragulator
CC       complex (By similarity). Interacts with MMP14 (By similarity).
CC       Interacts with CDKN1B; prevents the interaction of CDKN1B with
CC       RHOA leaving RHOA in a form accessible to activation by ARHGEF2
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane; Lipid-anchor;
CC       Cytoplasmic side (By similarity). Lysosome membrane; Lipid-anchor;
CC       Cytoplasmic side (By similarity). Cell membrane (By similarity).
CC   -!- DEVELOPMENTAL STAGE: At E6.5 expressed throughout the embryo with
CC       relative abundance in the visceral endoderm.
CC   -!- DISRUPTION PHENOTYPE: Embryos die at egg cylinder stage due to
CC       growth retardation, associated with altered endosomes and
CC       lysosomes organizations and impaired membrane protein transport in
CC       the visceral endoderm.
CC   -!- SIMILARITY: Belongs to the PDRO family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK009320; BAB26214.1; -; mRNA.
DR   EMBL; AK013389; BAB28825.1; -; mRNA.
DR   EMBL; AK019947; BAB31928.1; -; mRNA.
DR   EMBL; AK144476; BAE25909.1; -; mRNA.
DR   EMBL; BC020142; AAH20142.1; -; mRNA.
DR   EMBL; BC092062; AAH92062.1; -; mRNA.
DR   EMBL; BC096412; AAH96412.1; -; mRNA.
DR   EMBL; BC115458; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC115459; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC126973; AAI26974.1; -; mRNA.
DR   IPI; IPI00315187; -.
DR   RefSeq; NP_079881.2; NM_025605.3.
DR   UniGene; Mm.214841; -.
DR   UniGene; Mm.30003; -.
DR   UniGene; Mm.359278; -.
DR   ProteinModelPortal; Q9CQ22; -.
DR   STRING; Q9CQ22; -.
DR   PhosphoSite; Q9CQ22; -.
DR   PRIDE; Q9CQ22; -.
DR   Ensembl; ENSMUST00000033131; ENSMUSP00000033131; ENSMUSG00000030842.
DR   GeneID; 66508; -.
DR   KEGG; mmu:66508; -.
DR   UCSC; uc009ipw.1; mouse.
DR   MGI; MGI:1913758; 2400001E08Rik.
DR   eggNOG; maNOG17350; -.
DR   GeneTree; ENSGT00390000016789; -.
DR   HOGENOM; HBG315154; -.
DR   HOVERGEN; HBG081218; -.
DR   InParanoid; Q9CQ22; -.
DR   OMA; VSKIAAY; -.
DR   OrthoDB; EOG4GQQ65; -.
DR   PhylomeDB; Q9CQ22; -.
DR   NextBio; 321896; -.
DR   Bgee; Q9CQ22; -.
DR   CleanEx; MM_2400001E08RIK; -.
DR   Genevestigator; Q9CQ22; -.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0071986; C:Ragulator complex; ISS:UniProtKB.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0016049; P:cell growth; ISS:UniProtKB.
DR   GO; GO:0034613; P:cellular protein localization; IMP:UniProtKB.
DR   GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR   GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB.
DR   GO; GO:0032439; P:endosome localization; IMP:UniProtKB.
DR   GO; GO:0007032; P:endosome organization; IMP:UniProtKB.
DR   GO; GO:0032418; P:lysosome localization; IMP:UniProtKB.
DR   GO; GO:0007040; P:lysosome organization; IMP:UniProtKB.
DR   GO; GO:0043410; P:positive regulation of MAPKKK cascade; IMP:UniProtKB.
DR   GO; GO:0032008; P:positive regulation of TOR signaling cascade; ISS:UniProtKB.
DR   GO; GO:0010874; P:regulation of cholesterol efflux; ISS:UniProtKB.
DR   GO; GO:0010872; P:regulation of cholesterol esterification; ISS:UniProtKB.
DR   GO; GO:0060620; P:regulation of cholesterol import; ISS:UniProtKB.
DR   GO; GO:0001919; P:regulation of receptor recycling; IMP:UniProtKB.
PE   1: Evidence at protein level;
KW   Cell membrane; Endosome; Lipid-binding; Lipoprotein; Lysosome;
KW   Membrane; Myristate; Phosphoprotein.
FT   INIT_MET      1      1       Removed (Potential).
FT   CHAIN         2    161       Ragulator complex protein PDRO.
FT                                /FTId=PRO_0000274293.
FT   REGION      121    161       Interaction with MAPKSP1 and ROBLD3 (By
FT                                similarity).
FT   MOD_RES      27     27       Phosphoserine (By similarity).
FT   MOD_RES      28     28       Phosphothreonine.
FT   MOD_RES      40     40       Phosphotyrosine (By similarity).
FT   MOD_RES      63     63       Phosphoserine.
FT   LIPID         2      2       N-myristoyl glycine (Potential).
FT   CONFLICT     82     82       M -> I (in Ref. 1; BAB28825).
SQ   SEQUENCE   161 AA;  17749 MW;  D50CC6C05C36B457 CRC64;
     MGCCYSSENE DSDQDREERK LLLDPSSTPT KALNGAEPNY HSLPSARTDE QALLSSILAK
     TASNIIDVSA ADSQGMEQHE YMDRARQYST RLAVLSSSLT HWKKLPPLPS LTSQPHQVLA
     SEPIPFSDLQ QVSRIAAYAY SALSQIRVDA KEELVVQFGI P
//
ID   NDUA2_MOUSE             Reviewed;          99 AA.
AC   Q9CQ75; Q9WUB2;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2;
DE   AltName: Full=Complex I-B8;
DE            Short=CI-B8;
DE   AltName: Full=NADH-ubiquinone oxidoreductase B8 subunit;
GN   Name=Ndufa2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Skeletal muscle;
RX   MEDLINE=99254010; PubMed=10318868; DOI=10.1074/jbc.274.20.14429;
RA   Murdock D.G., Boone B.E., Esposito L.A., Wallace D.C.;
RT   "Up-regulation of nuclear and mitochondrial genes in the skeletal
RT   muscle of mice lacking the heart/muscle isoform of the adenine
RT   nucleotide translocator.";
RL   J. Biol. Chem. 274:14429-14433(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 47-56 AND 76-98, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-64 AND LYS-75, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- FUNCTION: Accessory subunit of the mitochondrial membrane
CC       respiratory chain NADH dehydrogenase (Complex I), that is believed
CC       not to be involved in catalysis. Complex I functions in the
CC       transfer of electrons from NADH to the respiratory chain. The
CC       immediate electron acceptor for the enzyme is believed to be
CC       ubiquinone (By similarity).
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein; Matrix side (By similarity).
CC   -!- PTM: Acetylation of Lys-64 and Lys-75 is observed in liver
CC       mitochondria from fasted mice but not from fed mice.
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DR   EMBL; AF124786; AAD30475.1; -; mRNA.
DR   EMBL; AK003608; BAB22887.1; -; mRNA.
DR   EMBL; AK018732; BAB31375.1; -; mRNA.
DR   EMBL; BC006815; AAH06815.1; -; mRNA.
DR   IPI; IPI00315302; -.
DR   RefSeq; NP_035015.2; NM_010885.4.
DR   UniGene; Mm.29867; -.
DR   ProteinModelPortal; Q9CQ75; -.
DR   SMR; Q9CQ75; 15-99.
DR   STRING; Q9CQ75; -.
DR   PhosphoSite; Q9CQ75; -.
DR   PRIDE; Q9CQ75; -.
DR   Ensembl; ENSMUST00000014438; ENSMUSP00000014438; ENSMUSG00000014294.
DR   GeneID; 17991; -.
DR   KEGG; mmu:17991; -.
DR   UCSC; uc008eoj.1; mouse.
DR   CTD; 17991; -.
DR   MGI; MGI:1343103; Ndufa2.
DR   eggNOG; roNOG17410; -.
DR   GeneTree; ENSGT00390000006178; -.
DR   HOGENOM; HBG464594; -.
DR   HOVERGEN; HBG082012; -.
DR   InParanoid; Q9CQ75; -.
DR   OMA; LRLHLCQ; -.
DR   OrthoDB; EOG4GXFPB; -.
DR   PhylomeDB; Q9CQ75; -.
DR   NextBio; 292967; -.
DR   ArrayExpress; Q9CQ75; -.
DR   Bgee; Q9CQ75; -.
DR   Genevestigator; Q9CQ75; -.
DR   GermOnline; ENSMUSG00000014294; Mus musculus.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; TAS:MGI.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; TAS:MGI.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR016464; NADH_Ub_cplx-1_asu_su-2.
DR   InterPro; IPR007741; Ribosome/NADH_DH.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   Pfam; PF05047; L51_S25_CI-B8; 1.
DR   PIRSF; PIRSF005822; NDUA2; 1.
DR   SMART; SM00916; L51_S25_CI-B8; 1.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Disulfide bond;
KW   Electron transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2     99       NADH dehydrogenase [ubiquinone] 1 alpha
FT                                subcomplex subunit 2.
FT                                /FTId=PRO_0000118790.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      64     64       N6-acetyllysine.
FT   MOD_RES      75     75       N6-acetyllysine.
FT   DISULFID     24     58       Redox-active (By similarity).
FT   CONFLICT     12     12       A -> T (in Ref. 1; AAD30475).
SQ   SEQUENCE   99 AA;  10916 MW;  BB06EFCADD6E30EC CRC64;
     MAAAAASRAV GAKLGLREIR VHLCQRSPGS QGVRDFIVQR YVELKKAHPN LPILIRECSE
     VQPKLWARYA FGQEKTVSLN NLSADEVTRA MQNVLSGKA
//
ID   FIS1_MOUSE              Reviewed;         152 AA.
AC   Q9CQ92;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Mitochondrial fission 1 protein;
DE   AltName: Full=FIS1 homolog;
DE   AltName: Full=Tetratricopeptide repeat protein 11;
DE            Short=TPR repeat protein 11;
GN   Name=Fis1; Synonyms=Ttc11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Liver, Small intestine, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 20-32; 54-64; 72-83 AND 96-108, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   STRUCTURE BY NMR.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of RSGI RUH-001, a FIS1p-like and CGI-135
RT   homologous domain from a mouse cDNA.";
RL   Submitted (AUG-2002) to the PDB data bank.
CC   -!- FUNCTION: Promotes the fragmentation of the mitochondrial network
CC       and its perinuclear clustering. Can induce cytochrome c release
CC       from the mitochondrion to the cytosol, ultimately leading to
CC       apoptosis. Also mediates peroxisomal fission (By similarity).
CC   -!- SUBUNIT: Interacts with DNM1L/DLP1 through the TPR region.
CC       Interacts with MARCH5 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC       membrane protein. Peroxisome membrane; Single-pass membrane
CC       protein (By similarity).
CC   -!- DOMAIN: The C-terminus is required for mitochondrial or
CC       peroxisomal localization, while the N-terminus is necessary for
CC       mitochondrial or peroxisomal fission, localization and regulation
CC       of the interaction with DNM1L (By similarity).
CC   -!- PTM: Ubiquitinated by MARCH5 (By similarity).
CC   -!- SIMILARITY: Belongs to the FIS1 family.
CC   -!- SIMILARITY: Contains 1 TPR repeat.
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DR   EMBL; AK004479; BAB23324.1; -; mRNA.
DR   EMBL; AK004917; BAB23668.1; -; mRNA.
DR   EMBL; AK008078; BAB25445.1; -; mRNA.
DR   EMBL; AK008323; BAB25601.1; -; mRNA.
DR   EMBL; AK008916; BAB25966.1; -; mRNA.
DR   EMBL; BC010783; AAH10783.1; -; mRNA.
DR   IPI; IPI00132217; -.
DR   RefSeq; NP_001156715.1; NM_001163243.1.
DR   RefSeq; NP_079838.1; NM_025562.3.
DR   UniGene; Mm.25849; -.
DR   PDB; 1IYG; NMR; -; A=1-120.
DR   PDBsum; 1IYG; -.
DR   ProteinModelPortal; Q9CQ92; -.
DR   SMR; Q9CQ92; 1-122.
DR   PhosphoSite; Q9CQ92; -.
DR   PRIDE; Q9CQ92; -.
DR   Ensembl; ENSMUST00000019198; ENSMUSP00000019198; ENSMUSG00000019054.
DR   GeneID; 66437; -.
DR   KEGG; mmu:66437; -.
DR   UCSC; uc009abf.1; mouse.
DR   CTD; 66437; -.
DR   MGI; MGI:1913687; Fis1.
DR   eggNOG; maNOG20307; -.
DR   GeneTree; ENSGT00390000000592; -.
DR   HOGENOM; HBG446741; -.
DR   HOVERGEN; HBG081530; -.
DR   InParanoid; Q9CQ92; -.
DR   OMA; RDFLFYL; -.
DR   OrthoDB; EOG4XSKRC; -.
DR   PhylomeDB; Q9CQ92; -.
DR   NextBio; 321685; -.
DR   ArrayExpress; Q9CQ92; -.
DR   Bgee; Q9CQ92; -.
DR   Genevestigator; Q9CQ92; -.
DR   GermOnline; ENSMUSG00000019054; Mus musculus.
DR   GO; GO:0031307; C:integral to mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0005779; C:integral to peroxisomal membrane; ISS:UniProtKB.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; ISS:UniProtKB.
DR   GO; GO:0000266; P:mitochondrial fission; ISS:UniProtKB.
DR   GO; GO:0016559; P:peroxisome fission; ISS:UniProtKB.
DR   InterPro; IPR016543; Tetratricopeptide_rpt_11_Fis1.
DR   InterPro; IPR011990; TPR-like_helical.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
DR   PIRSF; PIRSF008835; TPR_repeat_11_Fis1; 1.
DR   PROSITE; PS50005; TPR; FALSE_NEG.
DR   PROSITE; PS50293; TPR_REGION; FALSE_NEG.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Apoptosis; Direct protein sequencing;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane; Peroxisome;
KW   TPR repeat; Transmembrane; Transmembrane helix; Ubl conjugation.
FT   CHAIN         1    152       Mitochondrial fission 1 protein.
FT                                /FTId=PRO_0000106394.
FT   TOPO_DOM      1    122       Cytoplasmic (Potential).
FT   TRANSMEM    123    143       Helical; (Potential).
FT   TOPO_DOM    144    152       Mitochondrial intermembrane (Potential).
FT   REPEAT       71    104       TPR.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   HELIX         2      6
FT   HELIX        11     27
FT   HELIX        32     44
FT   STRAND       45     47
FT   HELIX        48     61
FT   HELIX        68     83
FT   HELIX        87    100
FT   HELIX       105    120
SQ   SEQUENCE   152 AA;  17009 MW;  B012DF491518A4B1 CRC64;
     MEAVLNELVS VEDLKNFERK FQSEQAAGSV SKSTQFEYAW CLVRSKYNED IRRGIVLLEE
     LLPKGSKEEQ RDYVFYLAVG NYRLKEYEKA LKYVRGLLQT EPQNNQAKEL ERLIDKAMKK
     DGLVGMAIVG GMALGVAGLA GLIGLAVSKS KS
//
ID   NDUB4_MOUSE             Reviewed;         129 AA.
AC   Q9CQC7;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4;
DE   AltName: Full=Complex I-B15;
DE            Short=CI-B15;
DE   AltName: Full=NADH-ubiquinone oxidoreductase B15 subunit;
GN   Name=Ndufb4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 6-40; 46-67 AND 73-85, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Accessory subunit of the mitochondrial membrane
CC       respiratory chain NADH dehydrogenase (Complex I), that is believed
CC       not to be involved in catalysis. Complex I functions in the
CC       transfer of electrons from NADH to the respiratory chain. The
CC       immediate electron acceptor for the enzyme is believed to be
CC       ubiquinone (By similarity).
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass
CC       membrane protein; Matrix side (By similarity).
CC   -!- SIMILARITY: Belongs to the complex I NDUFB4 subunit family.
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DR   EMBL; AK009807; BAB26515.1; -; mRNA.
DR   EMBL; AK018707; BAB31358.1; -; mRNA.
DR   EMBL; BC056229; AAH56229.1; -; mRNA.
DR   IPI; IPI00132390; -.
DR   RefSeq; NP_080886.1; NM_026610.1.
DR   RefSeq; XP_001476621.1; XM_001476571.2.
DR   RefSeq; XP_001478493.1; XM_001478443.2.
DR   UniGene; Mm.379154; -.
DR   UniGene; Mm.390788; -.
DR   ProteinModelPortal; Q9CQC7; -.
DR   STRING; Q9CQC7; -.
DR   PRIDE; Q9CQC7; -.
DR   Ensembl; ENSMUST00000023514; ENSMUSP00000023514; ENSMUSG00000022820.
DR   GeneID; 100041273; -.
DR   GeneID; 100042503; -.
DR   GeneID; 68194; -.
DR   KEGG; mmu:100041273; -.
DR   KEGG; mmu:100042503; -.
DR   KEGG; mmu:68194; -.
DR   UCSC; uc007zei.1; mouse.
DR   CTD; 68194; -.
DR   MGI; MGI:1915444; Ndufb4.
DR   GeneTree; ENSGT00390000007133; -.
DR   HOVERGEN; HBG001159; -.
DR   InParanoid; Q9CQC7; -.
DR   OMA; EYDISPE; -.
DR   OrthoDB; EOG49KFRZ; -.
DR   PhylomeDB; Q9CQC7; -.
DR   NextBio; 450843; -.
DR   ArrayExpress; Q9CQC7; -.
DR   Bgee; Q9CQC7; -.
DR   Genevestigator; Q9CQC7; -.
DR   GermOnline; ENSMUSG00000022820; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR009866; NADH_UbQ_OxRdtase_NDUFB4_su.
DR   PANTHER; PTHR15469; NDUFB4; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Respiratory chain;
KW   Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    129       NADH dehydrogenase [ubiquinone] 1 beta
FT                                subcomplex subunit 4.
FT                                /FTId=PRO_0000118801.
FT   TRANSMEM     88    105       Helical; (Potential).
FT   MOD_RES       2      2       N-acetylserine (By similarity).
SQ   SEQUENCE   129 AA;  15081 MW;  9E76B5087F095062 CRC64;
     MSGSKYKPAP LATLPSTLDP AEYDVSPETR RAQVERLSIR ARLKREYLLQ YNDPKRVSHI
     EDPALIRWTY ARSANIYPNF RPTPKNSLLG AVAGFGPLIF WYYVFKTDRD RKERLIQEGK
     LDRKFNISY
//
ID   RAB5A_MOUSE             Reviewed;         215 AA.
AC   Q9CQD1; Q9DCN5;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Ras-related protein Rab-5A;
GN   Name=Rab5a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryonic stem cell, Head, and Small intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 23-33; 82-110 AND 184-195, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   INTERACTION WITH SGSM1 AND SGSM3.
RX   PubMed=17509819; DOI=10.1016/j.ygeno.2007.03.013;
RA   Yang H., Sasaki T., Minoshima S., Shimizu N.;
RT   "Identification of three novel proteins (SGSM1, 2, 3) which modulate
RT   small G protein (RAP and RAB)-mediated signaling pathway.";
RL   Genomics 90:249-260(2007).
CC   -!- FUNCTION: Required for the fusion of plasma membranes and early
CC       endosomes.
CC   -!- ENZYME REGULATION: Regulated by guanine nucleotide exchange
CC       factors (GEFs) which promote the exchange of bound GDP for free
CC       GTP.
CC   -!- SUBUNIT: Binds EEA1. Interacts with ALS2CL, SUN2, ZFYVE20 and
CC       RUFY1. Interacts with RIN1 and GAPVD1, which regulate its pathway,
CC       probably by acting as a GEF (By similarity). Interacts with SGSM1
CC       and SGSM3.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (By similarity). Early endosome membrane; Lipid-anchor (By
CC       similarity). Melanosome (By similarity).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR   EMBL; AK002631; BAB22245.1; -; mRNA.
DR   EMBL; AK008198; BAB25527.1; -; mRNA.
DR   EMBL; AK010495; BAB26985.1; -; mRNA.
DR   EMBL; AK081999; BAC38391.1; -; mRNA.
DR   EMBL; BC004842; AAH04842.1; -; mRNA.
DR   EMBL; BC034370; AAH34370.1; -; mRNA.
DR   IPI; IPI00132410; -.
DR   RefSeq; NP_080163.1; NM_025887.4.
DR   UniGene; Mm.329123; -.
DR   ProteinModelPortal; Q9CQD1; -.
DR   SMR; Q9CQD1; 15-184.
DR   IntAct; Q9CQD1; 1.
DR   STRING; Q9CQD1; -.
DR   PhosphoSite; Q9CQD1; -.
DR   PRIDE; Q9CQD1; -.
DR   Ensembl; ENSMUST00000017975; ENSMUSP00000017975; ENSMUSG00000017831.
DR   GeneID; 271457; -.
DR   KEGG; mmu:271457; -.
DR   UCSC; uc008czn.1; mouse.
DR   CTD; 271457; -.
DR   MGI; MGI:105926; Rab5a.
DR   GeneTree; ENSGT00550000074186; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; Q9CQD1; -.
DR   OMA; NEPQNTG; -.
DR   OrthoDB; EOG4Z0B6M; -.
DR   PhylomeDB; Q9CQD1; -.
DR   NextBio; 393462; -.
DR   ArrayExpress; Q9CQD1; -.
DR   Bgee; Q9CQD1; -.
DR   CleanEx; MM_RAB5A; -.
DR   Genevestigator; Q9CQD1; -.
DR   GermOnline; ENSMUSG00000017831; Mus musculus.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030139; C:endocytic vesicle; IDA:MGI.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0045121; C:membrane raft; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0001726; C:ruffle; IDA:MGI.
DR   GO; GO:0019003; F:GDP binding; ISS:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Direct protein sequencing; Endosome;
KW   GTP-binding; Lipoprotein; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Prenylation; Protein transport; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    215       Ras-related protein Rab-5A.
FT                                /FTId=PRO_0000121106.
FT   NP_BIND      27     35       GTP (By similarity).
FT   NP_BIND      75     79       GTP (By similarity).
FT   NP_BIND     133    136       GTP (By similarity).
FT   NP_BIND     163    165       GTP (By similarity).
FT   MOTIF        49     57       Effector region (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     202    202       Phosphothreonine (By similarity).
FT   LIPID       212    212       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   LIPID       213    213       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   CONFLICT    119    119       Q -> R (in Ref. 1; BAB22245).
SQ   SEQUENCE   215 AA;  23599 MW;  9CDE2FD9B37C261A CRC64;
     MANRGATRPN GPNTGNKICQ FKLVLLGESA VGKSSLVLRF VKGQFHEFQE STIGAAFLTQ
     TVCLDDTTVK FEIWDTAGQE RYHSLAPMYY RGAQAAIVVY DITNEESFAR AKNWVKELQR
     QASPNIVIAL SGNKADLANK RAVDFQEAQS YADDNSLLFM ETSAKTSMNV NEIFMAIAKK
     LPKNEPQNPG ANSARGRGVD LTEPAQPARS QCCSN
//
ID   RGS10_MOUSE             Reviewed;         181 AA.
AC   Q9CQE5; Q9D3L2;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Regulator of G-protein signaling 10;
DE            Short=RGS10;
GN   Name=Rgs10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, Thymus, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Inhibits signal transduction by increasing the GTPase
CC       activity of G protein alpha subunits thereby driving them into
CC       their inactive GDP-bound form. Associates specifically with the
CC       activated forms of the G protein subunits G(i)-alpha and G(z)-
CC       alpha but fails to interact with the structurally and functionally
CC       distinct G(s)-alpha subunit. Activity on G(z)-alpha is inhibited
CC       by palmitoylation of the G-protein (By similarity).
CC   -!- SIMILARITY: Contains 1 RGS domain.
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DR   EMBL; AK009686; BAB26440.1; -; mRNA.
DR   EMBL; AK009283; BAB26193.1; -; mRNA.
DR   EMBL; AK017314; BAB30688.1; -; mRNA.
DR   EMBL; AK088009; BAC40091.1; -; mRNA.
DR   IPI; IPI00132450; -.
DR   RefSeq; NP_080694.1; NM_026418.2.
DR   UniGene; Mm.18635; -.
DR   ProteinModelPortal; Q9CQE5; -.
DR   SMR; Q9CQE5; 30-164.
DR   STRING; Q9CQE5; -.
DR   PhosphoSite; Q9CQE5; -.
DR   PRIDE; Q9CQE5; -.
DR   Ensembl; ENSMUST00000033133; ENSMUSP00000033133; ENSMUSG00000030844.
DR   GeneID; 67865; -.
DR   KEGG; mmu:67865; -.
DR   UCSC; uc009jyw.1; mouse.
DR   CTD; 67865; -.
DR   MGI; MGI:1915115; Rgs10.
DR   GeneTree; ENSGT00540000071162; -.
DR   HOGENOM; HBG713967; -.
DR   HOVERGEN; HBG013233; -.
DR   InParanoid; Q9CQE5; -.
DR   OMA; PKSTAKW; -.
DR   OrthoDB; EOG4JM7QV; -.
DR   PhylomeDB; Q9CQE5; -.
DR   NextBio; 325763; -.
DR   ArrayExpress; Q9CQE5; -.
DR   Bgee; Q9CQE5; -.
DR   CleanEx; MM_RGS10; -.
DR   Genevestigator; Q9CQE5; -.
DR   GermOnline; ENSMUSG00000030844; Mus musculus.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000342; Regulat_G_prot_signal.
DR   InterPro; IPR016137; Regulat_G_prot_signal_superfam.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48097; Regulat_G_prot_signal_superfam; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   2: Evidence at transcript level;
KW   Lipoprotein; Palmitate; Phosphoprotein; Signal transduction inhibitor.
FT   CHAIN         1    181       Regulator of G-protein signaling 10.
FT                                /FTId=PRO_0000204208.
FT   DOMAIN       41    156       RGS.
FT   MOD_RES      16     16       Phosphoserine (By similarity).
FT   LIPID        74     74       S-palmitoyl cysteine (By similarity).
FT   CONFLICT     73     73       A -> E (in Ref. 1; BAB30688).
SQ   SEQUENCE   181 AA;  21151 MW;  9897860505962286 CRC64;
     MFTRAVSRLS RKRPPSDIHD GDGSSSSGHQ SLKSTAKWAS SLENLLEDPE GVQRFREFLK
     KEFSEENVLF WLACEDFKKT EDRKQMQEKA KEIYMTFLSN KASSQVNVEG QSRLTEKILE
     EPHPLMFQKL QDQIFNLMKY DSYSRFLKSD LFLKPKRTEE EEEEPPDAQT AAKRASRIYN
     T
//
ID   CF203_MOUSE             Reviewed;         240 AA.
AC   Q9CQF4; Q3TQU4;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Uncharacterized protein C6orf203 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Egg, Pancreas, Stomach, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-110, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK006199; BAB24454.1; -; mRNA.
DR   EMBL; AK007370; BAB24992.1; -; mRNA.
DR   EMBL; AK008795; BAB25900.1; -; mRNA.
DR   EMBL; AK163304; BAE37288.1; -; mRNA.
DR   EMBL; BC013506; AAH13506.1; -; mRNA.
DR   IPI; IPI00132478; -.
DR   RefSeq; NP_080687.1; NM_026411.1.
DR   UniGene; Mm.209953; -.
DR   ProteinModelPortal; Q9CQF4; -.
DR   SMR; Q9CQF4; 141-194.
DR   STRING; Q9CQF4; -.
DR   PhosphoSite; Q9CQF4; -.
DR   PRIDE; Q9CQF4; -.
DR   Ensembl; ENSMUST00000019932; ENSMUSP00000019932; ENSMUSG00000019797.
DR   GeneID; 67851; -.
DR   KEGG; mmu:67851; -.
DR   UCSC; uc007ezk.1; mouse.
DR   MGI; MGI:1915101; 1700021F05Rik.
DR   eggNOG; roNOG13394; -.
DR   GeneTree; ENSGT00390000009366; -.
DR   HOGENOM; HBG279757; -.
DR   HOVERGEN; HBG081118; -.
DR   InParanoid; Q9CQF4; -.
DR   OMA; YRVVLRR; -.
DR   PhylomeDB; Q9CQF4; -.
DR   NextBio; 325717; -.
DR   ArrayExpress; Q9CQF4; -.
DR   Bgee; Q9CQF4; -.
DR   CleanEx; MM_1700021F05RIK; -.
DR   Genevestigator; Q9CQF4; -.
DR   GermOnline; ENSMUSG00000019797; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    240       Uncharacterized protein C6orf203 homolog.
FT                                /FTId=PRO_0000089560.
FT   COMPBIAS    100    125       Glu-rich.
FT   MOD_RES     106    106       Phosphoserine.
FT   MOD_RES     110    110       Phosphothreonine.
FT   MOD_RES     116    116       Phosphoserine (By similarity).
SQ   SEQUENCE   240 AA;  27847 MW;  92A79152831F27BB CRC64;
     MAVPGVRLLT GALRKPDAWT RLWGVIQGTS SHKLCASWNR YLYFSSTKLN TSNYKTLFRN
     IFSLRLPELL VSPECYFPFS IRLKSNINSK KSTKKTLQKE ADEEDSDEET SYPERSEQEE
     ELESEPGVAK DYKDLEKVVQ SFRYDVILKT GLDVGRNKVE DAFYKGELRL NGEKLWKKSR
     TVKVGDTLDL ITGENKETGT EVVMRILLKK VYEEKTENDK HRVVLRRWKS LKLPKKTLSK
//
ID   MET10_MOUSE             Reviewed;         553 AA.
AC   Q9CQG2; Q3UMA9; Q9D062;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-FEB-2011, entry version 68.
DE   RecName: Full=Putative methyltransferase METT10D;
DE            EC=2.1.1.-;
DE   AltName: Full=Methyltransferase 10 domain-containing protein;
GN   Name=Mett10d;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Amnion, Embryo, and Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9CQG2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CQG2-2; Sequence=VSP_029342;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       METT10D/rlmF family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK145022; BAE26189.1; -; mRNA.
DR   EMBL; AK011780; BAB27835.1; -; mRNA.
DR   EMBL; AK012739; BAB28440.1; -; mRNA.
DR   EMBL; AK145662; BAE26574.1; -; mRNA.
DR   EMBL; AK168798; BAE40630.1; -; mRNA.
DR   EMBL; AL604066; CAI24250.1; -; Genomic_DNA.
DR   EMBL; AL607024; CAI24250.1; JOINED; Genomic_DNA.
DR   EMBL; AL607024; CAI24379.1; -; Genomic_DNA.
DR   EMBL; AL604066; CAI24379.1; JOINED; Genomic_DNA.
DR   EMBL; BC049897; AAH49897.1; -; mRNA.
DR   EMBL; BC054724; AAH54724.1; -; mRNA.
DR   IPI; IPI00387384; -.
DR   IPI; IPI00648432; -.
DR   RefSeq; NP_080473.1; NM_026197.3.
DR   UniGene; Mm.45748; -.
DR   ProteinModelPortal; Q9CQG2; -.
DR   SMR; Q9CQG2; 42-291.
DR   PhosphoSite; Q9CQG2; -.
DR   PRIDE; Q9CQG2; -.
DR   Ensembl; ENSMUST00000092912; ENSMUSP00000090590; ENSMUSG00000010554.
DR   Ensembl; ENSMUST00000100858; ENSMUSP00000098420; ENSMUSG00000010554.
DR   GeneID; 67493; -.
DR   KEGG; mmu:67493; -.
DR   NMPDR; fig|10090.3.peg.24699; -.
DR   UCSC; uc007kch.1; mouse.
DR   CTD; 67493; -.
DR   MGI; MGI:1914743; Mett10d.
DR   GeneTree; ENSGT00390000016694; -.
DR   HOVERGEN; HBG058052; -.
DR   PhylomeDB; Q9CQG2; -.
DR   NextBio; 324738; -.
DR   ArrayExpress; Q9CQG2; -.
DR   Bgee; Q9CQG2; -.
DR   CleanEx; MM_METT10D; -.
DR   Genevestigator; Q9CQG2; -.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR017182; S-AdoMet-dep_MeTrfase_Mett10D.
DR   InterPro; IPR010286; SAM-Mtase_prd.
DR   PANTHER; PTHR13393; DUF890; 1.
DR   Pfam; PF05971; Methyltransf_10; 1.
DR   PIRSF; PIRSF037350; Mtase_ZK1128_prd; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Methyltransferase; Phosphoprotein;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    553       Putative methyltransferase METT10D.
FT                                /FTId=PRO_0000310768.
FT   BINDING      82     82       S-adenosyl-L-methionine (By similarity).
FT   BINDING     110    110       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING     133    133       S-adenosyl-L-methionine (By similarity).
FT   BINDING     164    164       S-adenosyl-L-methionine (By similarity).
FT   BINDING     184    184       S-adenosyl-L-methionine (By similarity).
FT   MOD_RES     329    329       Phosphoserine (By similarity).
FT   MOD_RES     450    450       Phosphoserine.
FT   VAR_SEQ     267    296       Missing (in isoform 2).
FT                                /FTId=VSP_029342.
FT   CONFLICT    498    498       R -> H (in Ref. 1; BAE26189).
FT   CONFLICT    533    533       R -> G (in Ref. 1; BAB27835).
SQ   SEQUENCE   553 AA;  62341 MW;  9087B88833F3B783 CRC64;
     MALSKSMHAR NRYKDKPPDF AYLASKYPDF KQHIQINLNG RVSLNFKDPE AVRALTCTLL
     REDFGLSIDI PLERLIPTVP LRLNYIHWVE DLIGHQDSDK TTLRRGIDIG TGASCIYPLL
     GATLNGWYFL ATEVDDMCFN YAKKNVEQNN LSDLIKVVKV PQKTLLMDAL KEESEIVYDF
     CMCNPPFFAN QLEAKGVNSR NSRRPPPSSV NTGGITEIMA EGGELEFVKR IIHDSLQLKK
     RLRWYSCMLG KKCSLAPLKE ELRIQGVPKV TFTEFCQGRT MRWALAWSFY DDVTVPSPPS
     KRRKLEKPRK PITFVVLESV MKELSLKASS LGSETAEGIV VVTTWIEKIL TDLKVQHKRI
     PCGREEVSLF LTAIENSWIH LRRKRRERVR QLREVPRAPE DVILALEERK STPKELSSGQ
     DVAHSPQESA LCGLDVPGGE AAADGGHCLS QKLLCQEETP EATEDERDEE RGGMEAMESC
     KGSSNGAQDG EASEKGDRLD GAAGRYLFKC LVNIKKEAGD AVVEMHWVEG QNRDLMNQLC
     TYVRNQILRL VAS
//
ID   TM100_MOUSE             Reviewed;         134 AA.
AC   Q9CQG9;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Transmembrane protein 100;
GN   Name=Tmem100;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 8-23, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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DR   EMBL; AK003574; BAB22866.1; -; mRNA.
DR   EMBL; AK007878; BAB25325.1; -; mRNA.
DR   EMBL; AL645932; CAI24062.1; -; Genomic_DNA.
DR   EMBL; BC034841; AAH34841.1; -; mRNA.
DR   IPI; IPI00132522; -.
DR   RefSeq; NP_080709.1; NM_026433.2.
DR   UniGene; Mm.212428; -.
DR   ProteinModelPortal; Q9CQG9; -.
DR   PRIDE; Q9CQG9; -.
DR   Ensembl; ENSMUST00000092788; ENSMUSP00000090464; ENSMUSG00000069763.
DR   GeneID; 67888; -.
DR   KEGG; mmu:67888; -.
DR   UCSC; uc007kwm.1; mouse.
DR   CTD; 67888; -.
DR   MGI; MGI:1915138; Tmem100.
DR   eggNOG; roNOG17291; -.
DR   GeneTree; ENSGT00390000018520; -.
DR   HOGENOM; HBG715170; -.
DR   HOVERGEN; HBG054506; -.
DR   InParanoid; Q9CQG9; -.
DR   OMA; GGAELSC; -.
DR   OrthoDB; EOG47H5RR; -.
DR   PhylomeDB; Q9CQG9; -.
DR   NextBio; 325850; -.
DR   ArrayExpress; Q9CQG9; -.
DR   Bgee; Q9CQG9; -.
DR   CleanEx; MM_TMEM100; -.
DR   Genevestigator; Q9CQG9; -.
DR   GermOnline; ENSMUSG00000069763; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    134       Transmembrane protein 100.
FT                                /FTId=PRO_0000240847.
FT   TRANSMEM     56     76       Helical; (Potential).
FT   TRANSMEM     84    104       Helical; (Potential).
SQ   SEQUENCE   134 AA;  14504 MW;  8E7A4C4DEA71FC72 CRC64;
     MTEESTKENL GAPKSPTPVT MEKNPKREVV VTTGPLVSEV QLMAATGGAE LSCYRCIIPF
     AVVVFITGIV VTAVAYSFNS HGSIISIFGL VLLSSGLFLL ASSALCWKVR QRNKKVKRRE
     SQTALVVNQR CLFA
//
ID   NDUB5_MOUSE             Reviewed;         189 AA.
AC   Q9CQH3;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 5, mitochondrial;
DE   AltName: Full=Complex I-SGDH;
DE            Short=CI-SGDH;
DE   AltName: Full=NADH-ubiquinone oxidoreductase SGDH subunit;
DE   Flags: Precursor;
GN   Name=Ndufb5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Colon, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 54-66; 124-131; 136-150 AND 161-176, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Accessory subunit of the mitochondrial membrane
CC       respiratory chain NADH dehydrogenase (Complex I), that is believed
CC       not to be involved in catalysis. Complex I functions in the
CC       transfer of electrons from NADH to the respiratory chain. The
CC       immediate electron acceptor for the enzyme is believed to be
CC       ubiquinone (By similarity).
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass
CC       membrane protein; Matrix side (By similarity).
CC   -!- SIMILARITY: Belongs to the complex I NDUFB5 subunit family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK018562; BAB31277.1; -; mRNA.
DR   EMBL; AK004372; BAB23279.1; -; mRNA.
DR   EMBL; AK013223; BAB28724.1; -; mRNA.
DR   EMBL; BC025155; AAH25155.1; -; mRNA.
DR   IPI; IPI00132531; -.
DR   RefSeq; NP_079592.2; NM_025316.2.
DR   UniGene; Mm.28058; -.
DR   STRING; Q9CQH3; -.
DR   PRIDE; Q9CQH3; -.
DR   Ensembl; ENSMUST00000029217; ENSMUSP00000029217; ENSMUSG00000027673.
DR   GeneID; 66046; -.
DR   KEGG; mmu:66046; -.
DR   UCSC; uc008owq.1; mouse.
DR   CTD; 66046; -.
DR   MGI; MGI:1913296; Ndufb5.
DR   GeneTree; ENSGT00390000009980; -.
DR   HOGENOM; HBG714657; -.
DR   HOVERGEN; HBG003008; -.
DR   InParanoid; Q9CQH3; -.
DR   OMA; VKDYEKM; -.
DR   PhylomeDB; Q9CQH3; -.
DR   NextBio; 320462; -.
DR   ArrayExpress; Q9CQH3; -.
DR   Bgee; Q9CQH3; -.
DR   Genevestigator; Q9CQH3; -.
DR   GermOnline; ENSMUSG00000027673; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR019173; NADH_UbQ_OxRdtase_B5_su.
DR   Pfam; PF09781; NDUF_B5; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Respiratory chain;
KW   Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT       1     46       Mitochondrion (By similarity).
FT   CHAIN        47    189       NADH dehydrogenase [ubiquinone] 1 beta
FT                                subcomplex subunit 5, mitochondrial.
FT                                /FTId=PRO_0000020053.
FT   TRANSMEM     73     93       Helical; (Potential).
SQ   SEQUENCE   189 AA;  21710 MW;  8D998EA6CD683DE3 CRC64;
     MAAMSLLQRA SVSALTALSC RRAGPRLGVG SFLTRSFPKT VAPVRHSGDH GKRLFVVKPS
     LYYDARFLRL MKFYLMLTGI PVIIGITLVN IFIGEAELAE IPEGYIPEHW EYYKHPISRW
     IARNFYDGPE KNYEKTLAIL QIESEKAELR LKEQEVRRLM RARGDGPWYQ FPTPEKEFID
     HSPKATPDN
//
ID   DENR_MOUSE              Reviewed;         198 AA.
AC   Q9CQJ6; Q3UXY1;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Density-regulated protein;
DE            Short=DRP;
GN   Name=Denr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in the translation of target mRNAs by
CC       scanning and recognition of the initiation codon (By similarity).
CC   -!- SUBUNIT: Interacts with MCTS1 (By similarity).
CC   -!- SIMILARITY: Belongs to the DENR family.
CC   -!- SIMILARITY: Contains 1 SUI1 domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK017647; BAB30854.1; -; mRNA.
DR   EMBL; AK018762; BAB31392.1; -; mRNA.
DR   EMBL; AK135127; BAE22432.1; -; mRNA.
DR   EMBL; BC043922; AAH43922.1; -; mRNA.
DR   IPI; IPI00330057; -.
DR   RefSeq; NP_080879.1; NM_026603.4.
DR   UniGene; Mm.28549; -.
DR   ProteinModelPortal; Q9CQJ6; -.
DR   SMR; Q9CQJ6; 113-194.
DR   STRING; Q9CQJ6; -.
DR   PhosphoSite; Q9CQJ6; -.
DR   PRIDE; Q9CQJ6; -.
DR   Ensembl; ENSMUST00000023869; ENSMUSP00000023869; ENSMUSG00000023106.
DR   GeneID; 68184; -.
DR   KEGG; mmu:68184; -.
DR   UCSC; uc008zor.1; mouse.
DR   CTD; 68184; -.
DR   MGI; MGI:1915434; Denr.
DR   eggNOG; roNOG17381; -.
DR   GeneTree; ENSGT00390000014349; -.
DR   HOGENOM; HBG436297; -.
DR   HOVERGEN; HBG005471; -.
DR   InParanoid; Q9CQJ6; -.
DR   OMA; EYCEYYP; -.
DR   OrthoDB; EOG49PB0M; -.
DR   PhylomeDB; Q9CQJ6; -.
DR   NextBio; 326634; -.
DR   ArrayExpress; Q9CQJ6; -.
DR   Bgee; Q9CQJ6; -.
DR   CleanEx; MM_DENR; -.
DR   Genevestigator; Q9CQJ6; -.
DR   GermOnline; ENSMUSG00000023106; Mus musculus.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:InterPro.
DR   InterPro; IPR005873; Drp1.
DR   InterPro; IPR001950; TIF_SUI1.
DR   Pfam; PF01253; SUI1; 1.
DR   SUPFAM; SSF55159; TIF_SUI1; 1.
DR   TIGRFAMs; TIGR01159; DRP1; 1.
DR   PROSITE; PS50296; SUI1; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    198       Density-regulated protein.
FT                                /FTId=PRO_0000130601.
FT   DOMAIN      115    182       SUI1.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      69     69       Phosphothreonine (By similarity).
FT   MOD_RES      73     73       Phosphoserine (By similarity).
SQ   SEQUENCE   198 AA;  22166 MW;  8482AA9E13E27A10 CRC64;
     MATDISESSG ADCKGDTKNS AKLDADYPLR VLYCGVCSLP TEYCEYMPDV AKCRQWLEKN
     FPNEFAKLTV ENSPKQETGI TEGQGPVGEE EEKKKQKRGG RGQIKQKKKT VPQKVTIAKI
     PRAKKKYVTR VCGLATFEID LKEAQRFFAQ KFSCGASVTG EDEIIIQGDF TDDIIDVIQE
     KWPEVDDDSI EDLGEVKK
//
ID   TOM6_MOUSE              Reviewed;          74 AA.
AC   Q9CQN3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Mitochondrial import receptor subunit TOM6 homolog;
DE   AltName: Full=Overexpressed breast tumor protein homolog;
DE   AltName: Full=Translocase of outer membrane 6 kDa subunit homolog;
GN   Name=Tomm6; Synonyms=Obtp, Tom6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBUNIT: Forms part of the preprotein translocase complex of the
CC       outer mitochondrial membrane (TOM complex) which consists of at
CC       least 7 different proteins (TOMM5, TOMM6, TOMM7, TOMM20, TOMM22,
CC       TOMM40 and TOMM70) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the Tom6 family.
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DR   EMBL; AK003291; BAB22694.1; -; mRNA.
DR   EMBL; AK010470; BAB26963.1; -; mRNA.
DR   EMBL; AK019199; BAB31597.1; -; mRNA.
DR   EMBL; BC021590; AAH21590.1; -; mRNA.
DR   EMBL; BC037589; AAH37589.1; -; mRNA.
DR   IPI; IPI00132765; -.
DR   RefSeq; NP_001158201.1; NM_001164729.1.
DR   RefSeq; NP_079641.1; NM_025365.3.
DR   UniGene; Mm.89912; -.
DR   STRING; Q9CQN3; -.
DR   PhosphoSite; Q9CQN3; -.
DR   PRIDE; Q9CQN3; -.
DR   Ensembl; ENSMUST00000113301; ENSMUSP00000108926; ENSMUSG00000033475.
DR   Ensembl; ENSMUST00000113302; ENSMUSP00000108927; ENSMUSG00000033475.
DR   GeneID; 66119; -.
DR   KEGG; mmu:66119; -.
DR   UCSC; uc008cvx.1; mouse.
DR   CTD; 66119; -.
DR   MGI; MGI:1913369; Tomm6.
DR   eggNOG; maNOG21328; -.
DR   GeneTree; ENSGT00390000002376; -.
DR   HOGENOM; HBG282058; -.
DR   HOVERGEN; HBG054583; -.
DR   InParanoid; Q9CQN3; -.
DR   OMA; NVGDWLR; -.
DR   OrthoDB; EOG4FJ8BH; -.
DR   NextBio; 461264; -.
DR   ArrayExpress; Q9CQN3; -.
DR   Bgee; Q9CQN3; -.
DR   Genevestigator; Q9CQN3; -.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW   Protein transport; Transport.
FT   CHAIN         1     74       Mitochondrial import receptor subunit
FT                                TOM6 homolog.
FT                                /FTId=PRO_0000302857.
FT   MOD_RES      63     63       Phosphoserine (By similarity).
SQ   SEQUENCE   74 AA;  7865 MW;  70D5EEF02B17A0FD CRC64;
     MASSGVTVSA AGSASEASEV PDNVGDWLRG VFRFATDRND FRRNLILNLG LFAAGVWLAR
     NLSDIDLMAP QPGV
//
ID   Q9CQN9_MOUSE            Unreviewed;       254 AA.
AC   Q9CQN9;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   08-FEB-2011, entry version 47.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Senp7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RA   Adachi J., Aizawa K., Akahira S., Akimura T., Arai A., Aono H.,
RA   Arakawa T., Bono H., Carninci P., Fukuda S., Fukunishi Y., Furuno M.,
RA   Hanagaki T., Hara A., Hayatsu N., Hiramoto K., Hiraoka T., Hori F.,
RA   Imotani K., Ishii Y., Itoh M., Izawa M., Kasukawa T., Kato H.,
RA   Kawai J., Kojima Y., Konno H., Kouda M., Koya S., Kurihara C.,
RA   Matsuyama T., Miyazaki A., Nishi K., Nomura K., Numazaki R., Ohno M.,
RA   Okazaki Y., Okido T., Owa C., Saito H., Saito R., Sakai C., Sakai K.,
RA   Sano H., Sasaki D., Shibata K., Shibata Y., Shinagawa A., Shiraki T.,
RA   Sogabe Y., Suzuki H., Tagami M., Tagawa A., Takahashi F., Tanaka T.,
RA   Tejima Y., Toya T., Yamamura T., Yasunishi A., Yoshida K., Yoshino M.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK012740; BAB28441.1; -; mRNA.
DR   EMBL; AK013090; BAB28642.1; -; mRNA.
DR   IPI; IPI00132774; -.
DR   RefSeq; NP_001003972.1; NM_001003972.1.
DR   RefSeq; NP_001003973.1; NM_001003973.1.
DR   UniGene; Mm.255784; -.
DR   ProteinModelPortal; Q9CQN9; -.
DR   PRIDE; Q9CQN9; -.
DR   Ensembl; ENSMUST00000049128; ENSMUSP00000043023; ENSMUSG00000052917.
DR   GeneID; 66315; -.
DR   KEGG; mmu:66315; -.
DR   UCSC; uc007zmg.1; mouse.
DR   CTD; 66315; -.
DR   MGI; MGI:1913565; Senp7.
DR   GeneTree; ENSGT00530000063531; -.
DR   HOVERGEN; HBG075878; -.
DR   NextBio; 321295; -.
DR   ArrayExpress; Q9CQN9; -.
DR   Bgee; Q9CQN9; -.
DR   Genevestigator; Q9CQN9; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   254 AA;  28150 MW;  6FDC620531127BC1 CRC64;
     MDRARPGRRR ASSEIVTEGK RKKSSPADLQ KITKLLTVKS EDVLAQSPLS KLRGSECWWT
     RSLRNKVICL DHKKPKAARG CPPKGLPKRH LRVMLTNVLW TDLGREFRKT LPRKDANLCA
     PSKVQSDSLP STSVDSIETC QRLDPLHQSL NLSERTPRVI LTDIRQTELG RKYLKIPPVT
     EASLSDTANL KSEQLSSSSD GSLESCQSVN HHKSFLSERL TSKKGKKSTT ATGQTETDQP
     SPGPACTNKA AFVI
//
ID   AT5F1_MOUSE             Reviewed;         256 AA.
AC   Q9CQQ7;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=ATP synthase subunit b, mitochondrial;
DE            Short=ATPase subunit b;
DE   Flags: Precursor;
GN   Name=Atp5f1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 71-90; 115-139; 145-154; 164-183 AND 195-221, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [3]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-115; LYS-131; LYS-162;
RP   LYS-188; LYS-221; LYS-225 AND LYS-233, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
CC       synthase or Complex V) produces ATP from ADP in the presence of a
CC       proton gradient across the membrane which is generated by electron
CC       transport complexes of the respiratory chain. F-type ATPases
CC       consist of two structural domains, F(1) - containing the
CC       extramembraneous catalytic core, and F(0) - containing the
CC       membrane proton channel, linked together by a central stalk and a
CC       peripheral stalk. During catalysis, ATP synthesis in the catalytic
CC       domain of F(1) is coupled via a rotary mechanism of the central
CC       stalk subunits to proton translocation. Part of the complex F(0)
CC       domain and the peripheric stalk, which acts as a stator to hold
CC       the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC       relative to the rotary elements.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel. CF(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC       has three main subunits: a, b and c.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC   -!- SIMILARITY: Belongs to the eukaryotic ATPase B chain family.
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DR   EMBL; AK002960; BAB22481.1; -; mRNA.
DR   EMBL; AK011312; BAB27538.1; -; mRNA.
DR   IPI; IPI00341282; -.
DR   RefSeq; NP_033855.2; NM_009725.3.
DR   UniGene; Mm.251152; -.
DR   ProteinModelPortal; Q9CQQ7; -.
DR   SMR; Q9CQQ7; 121-225.
DR   STRING; Q9CQQ7; -.
DR   PhosphoSite; Q9CQQ7; -.
DR   PRIDE; Q9CQQ7; -.
DR   Ensembl; ENSMUST00000090671; ENSMUSP00000088168; ENSMUSG00000000563.
DR   Ensembl; ENSMUST00000118209; ENSMUSP00000113022; ENSMUSG00000000563.
DR   GeneID; 11950; -.
DR   KEGG; mmu:11950; -.
DR   UCSC; uc008qvm.1; mouse.
DR   CTD; 11950; -.
DR   MGI; MGI:1100495; Atp5f1.
DR   GeneTree; ENSGT00390000001958; -.
DR   HOGENOM; HBG716119; -.
DR   HOVERGEN; HBG050604; -.
DR   InParanoid; Q9CQQ7; -.
DR   OMA; KRRLDYQ; -.
DR   OrthoDB; EOG4K3KXB; -.
DR   PhylomeDB; Q9CQQ7; -.
DR   NextBio; 280069; -.
DR   ArrayExpress; Q9CQQ7; -.
DR   Bgee; Q9CQQ7; -.
DR   Genevestigator; Q9CQQ7; -.
DR   GermOnline; ENSMUSG00000000563; Mus musculus.
DR   GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR008688; ATPase_F0-cplx_bsu_mt.
DR   InterPro; IPR013837; ATPase_F0-cplx_bsu_mt_met.
DR   PANTHER; PTHR12733; ATPase_F0_B_mt_met; 1.
DR   Pfam; PF05405; Mt_ATP-synt_B; 1.
PE   1: Evidence at protein level;
KW   Acetylation; CF(0); Direct protein sequencing; Hydrogen ion transport;
KW   Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Transit peptide; Transport.
FT   TRANSIT       1     42       Mitochondrion (By similarity).
FT   CHAIN        43    256       ATP synthase subunit b, mitochondrial.
FT                                /FTId=PRO_0000002514.
FT   MOD_RES     115    115       N6-acetyllysine.
FT   MOD_RES     131    131       N6-acetyllysine.
FT   MOD_RES     162    162       N6-acetyllysine.
FT   MOD_RES     188    188       N6-acetyllysine.
FT   MOD_RES     221    221       N6-acetyllysine.
FT   MOD_RES     225    225       N6-acetyllysine.
FT   MOD_RES     233    233       N6-acetyllysine.
SQ   SEQUENCE   256 AA;  28949 MW;  6B385AE4DE6CB784 CRC64;
     MLSRVVLSAA ATAAPCLKNA AALGPGVLQA TRAFHTGQPR LAPLPPLPEY GGKVRLGLIP
     EEFFQFLYPK TGVTGPYVLG TGLSLYFLSK EIYVITPETF STISVVGLIV YVIKKYGASF
     GEFIDKLNEE KIAQLEEVKQ SSMKQIQDAI DMEKAQQALV QKRHYLFDVQ RNNIALALEV
     TYRERLHKAY KEVKNRLDYH ISVQNMMRRK EEEHMIDWVE KHVVKSISVQ QEKETIAKCI
     EDLKLLAKKA QAQPIM
//
ID   S2546_MOUSE             Reviewed;         418 AA.
AC   Q9CQS4; Q3TUD3; Q3UGG7; Q8VDX9;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Solute carrier family 25 member 46;
GN   Name=Slc25a46;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Forelimb, Lung, Small intestine, and Xiphoid cartilage;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier family.
CC   -!- SIMILARITY: Contains 2 Solcar repeats.
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DR   EMBL; AK004625; BAB23420.1; -; mRNA.
DR   EMBL; AK008131; BAB25481.1; -; mRNA.
DR   EMBL; AK030346; BAC26914.1; -; mRNA.
DR   EMBL; AK031117; BAC27260.1; -; mRNA.
DR   EMBL; AK147936; BAE28241.1; -; mRNA.
DR   EMBL; AK160834; BAE36038.1; -; mRNA.
DR   EMBL; BC020087; AAH20087.1; -; mRNA.
DR   IPI; IPI00387392; -.
DR   RefSeq; NP_080441.1; NM_026165.3.
DR   UniGene; Mm.23896; -.
DR   ProteinModelPortal; Q9CQS4; -.
DR   SMR; Q9CQS4; 312-416.
DR   STRING; Q9CQS4; -.
DR   PhosphoSite; Q9CQS4; -.
DR   PRIDE; Q9CQS4; -.
DR   Ensembl; ENSMUST00000060396; ENSMUSP00000053325; ENSMUSG00000024259.
DR   GeneID; 67453; -.
DR   KEGG; mmu:67453; -.
DR   UCSC; uc008ehz.1; mouse.
DR   CTD; 67453; -.
DR   MGI; MGI:1914703; Slc25a46.
DR   GeneTree; ENSGT00390000015874; -.
DR   HOGENOM; HBG715470; -.
DR   HOVERGEN; HBG059752; -.
DR   InParanoid; Q9CQS4; -.
DR   OMA; QSSEQLN; -.
DR   PhylomeDB; Q9CQS4; -.
DR   NextBio; 324610; -.
DR   ArrayExpress; Q9CQS4; -.
DR   Bgee; Q9CQS4; -.
DR   CleanEx; MM_SLC25A46; -.
DR   Genevestigator; Q9CQS4; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   Pfam; PF00153; Mito_carr; 1.
DR   PROSITE; PS50920; SOLCAR; 2.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW   Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    418       Solute carrier family 25 member 46.
FT                                /FTId=PRO_0000291829.
FT   TRANSMEM    103    123       Helical; Name=1; (Potential).
FT   TRANSMEM    167    187       Helical; Name=2; (Potential).
FT   TRANSMEM    202    222       Helical; Name=3; (Potential).
FT   TRANSMEM    258    278       Helical; Name=4; (Potential).
FT   TRANSMEM    314    334       Helical; Name=5; (Potential).
FT   TRANSMEM    382    402       Helical; Name=6; (Potential).
FT   REPEAT       96    187       Solcar 1.
FT   REPEAT      311    413       Solcar 2.
FT   MOD_RES      35     35       Phosphoserine.
FT   MOD_RES      45     45       Phosphothreonine (By similarity).
FT   CONFLICT     48     48       D -> G (in Ref. 1; BAE28241).
FT   CONFLICT     59     59       E -> G (in Ref. 1; BAE36038).
FT   CONFLICT     85     85       G -> S (in Ref. 2; AAH20087).
SQ   SEQUENCE   418 AA;  46224 MW;  621A9892D62C6CD9 CRC64;
     MHPRRPEGFD GLGYRGGVRD DPAFGGPFHA RSFGSGTELG HWVTTPPDIP GSRNLHWGEK
     SPSYGVPSAP PTLEGSAEEP FPGGGEGPRP GPSSEQLNRF AGFGIGLASL FTENVLAHPC
     IVLRRQCQVN YHARHYHLTP FSIINIMYSF NKTQGPRALW KGMGSTFIVQ GVTLGAEGII
     SEFTPLPREV SHKLNPKQIG EHLLLKCLTY MVAMPFYSAS LIETVQSEII RDNTGILECV
     KEGIGRVIGL GVPHSKRLLP LFSLIFPTVL HGVLHYIISS IIQKIVLLIL KRKTYNSHLA
     ESTSPMQNML DAYFPELIAN FAASLCSDVI LYPLETVLHR LHIQGTRTII DNTDLGYEVL
     PINTQYEGMR DCINTIKQEE GVFGFYKGFG AVIIQYTLHA TILQITKMIY STLLQNSI
//
ID   SC61B_MOUSE             Reviewed;          96 AA.
AC   Q9CQS8;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Protein transport protein Sec61 subunit beta;
GN   Name=Sec61b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-16 AND 47-57, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Necessary for protein translocation in the endoplasmic
CC       reticulum (By similarity).
CC   -!- SUBUNIT: Heterotrimeric complex composed of SEC61-alpha, SEC61-
CC       beta and SEC61-gamma. Part of a complex composed of SEC61, SEC62
CC       and SEC63. Interacts with SEC62 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the SEC61-beta family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK004505; BAB23338.1; -; mRNA.
DR   EMBL; AK008739; BAB25868.1; -; mRNA.
DR   EMBL; BC002089; AAH02089.1; -; mRNA.
DR   EMBL; BC081445; AAH81445.1; -; mRNA.
DR   IPI; IPI00133030; -.
DR   RefSeq; NP_077133.1; NM_024171.2.
DR   UniGene; Mm.20188; -.
DR   ProteinModelPortal; Q9CQS8; -.
DR   SMR; Q9CQS8; 61-96.
DR   IntAct; Q9CQS8; 1.
DR   STRING; Q9CQS8; -.
DR   PhosphoSite; Q9CQS8; -.
DR   PRIDE; Q9CQS8; -.
DR   Ensembl; ENSMUST00000065678; ENSMUSP00000067681; ENSMUSG00000053317.
DR   GeneID; 66212; -.
DR   KEGG; mmu:66212; -.
DR   UCSC; uc008sur.1; mouse.
DR   CTD; 66212; -.
DR   MGI; MGI:1913462; Sec61b.
DR   HOGENOM; HBG749385; -.
DR   HOVERGEN; HBG061281; -.
DR   InParanoid; Q9CQS8; -.
DR   OMA; RSPSKTV; -.
DR   OrthoDB; EOG4STS6D; -.
DR   PhylomeDB; Q9CQS8; -.
DR   NextBio; 320979; -.
DR   ArrayExpress; Q9CQS8; -.
DR   Bgee; Q9CQS8; -.
DR   CleanEx; MM_SEC61B; -.
DR   Genevestigator; Q9CQS8; -.
DR   GermOnline; ENSMUSG00000053317; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043022; F:ribosome binding; IDA:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:UniProtKB-KW.
DR   InterPro; IPR005609; Sec61_beta.
DR   InterPro; IPR016482; Sec61_beta_euk.
DR   Pfam; PF03911; Sec61_beta; 1.
DR   PIRSF; PIRSF006398; Sec61_beta_euk; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Endoplasmic reticulum; Lipoprotein;
KW   Membrane; Palmitate; Phosphoprotein; Protein transport; Translocation;
KW   Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2     96       Protein transport protein Sec61 subunit
FT                                beta.
FT                                /FTId=PRO_0000157255.
FT   TOPO_DOM      2     70       Cytoplasmic (Potential).
FT   TRANSMEM     71     91       Helical; (Potential).
FT   MOD_RES       5      5       Phosphothreonine (By similarity).
FT   MOD_RES       7      7       Phosphoserine (By similarity).
FT   MOD_RES      13     13       Phosphoserine (By similarity).
FT   MOD_RES      14     14       Phosphoserine (By similarity).
FT   MOD_RES      17     17       Phosphoserine.
FT   MOD_RES      19     19       Phosphoserine (By similarity).
FT   MOD_RES      29     29       Phosphoserine (By similarity).
FT   MOD_RES      30     30       Phosphothreonine (By similarity).
FT   LIPID        39     39       N-palmitoyl cysteine (By similarity).
SQ   SEQUENCE   96 AA;  9958 MW;  5FAFF4197A742049 CRC64;
     MPGPTPSGTN VGSSGRSPSK AVAARAAGST VRQRKNASCG TRSAGRTTSA GTGGMWRFYT
     EDSPGLKVGP VPVLVMSLLF IAAVFMLHIW GKYTRS
//
ID   MFAP1_MOUSE             Reviewed;         439 AA.
AC   Q9CQU1; Q3TU29; Q8CCL1; Q9CSJ5;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Microfibrillar-associated protein 1;
GN   Name=Mfap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Colon, Embryo, Embryonic liver, Head, Olfactory bulb,
RC   Pancreatic islet, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-118, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-133, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-267, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-53, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-53; SER-116;
RP   SER-118; SER-132; SER-133 AND THR-267, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-133 AND
RP   THR-211, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-267, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Component of the elastin-associated microfibrils (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix (By similarity).
CC   -!- SIMILARITY: Belongs to the MFAP1 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK012688; BAB28412.3; -; mRNA.
DR   EMBL; AK014483; BAB29385.1; -; mRNA.
DR   EMBL; AK018514; BAB31249.1; -; mRNA.
DR   EMBL; AK032586; BAC27936.1; ALT_TERM; mRNA.
DR   EMBL; AK050561; BAC34325.1; -; mRNA.
DR   EMBL; AK077604; BAC36894.1; -; mRNA.
DR   EMBL; AK088766; BAC40557.1; -; mRNA.
DR   EMBL; AK088946; BAC40667.1; -; mRNA.
DR   EMBL; AK161000; BAE36142.1; -; mRNA.
DR   EMBL; BC005728; AAH05728.1; -; mRNA.
DR   IPI; IPI00228590; -.
DR   RefSeq; NP_001075444.1; NM_001081975.3.
DR   RefSeq; NP_080496.1; NM_026220.4.
DR   UniGene; Mm.270393; -.
DR   UniGene; Mm.440764; -.
DR   ProteinModelPortal; Q9CQU1; -.
DR   PhosphoSite; Q9CQU1; -.
DR   PRIDE; Q9CQU1; -.
DR   Ensembl; ENSMUST00000056732; ENSMUSP00000049548; ENSMUSG00000048222.
DR   Ensembl; ENSMUST00000089926; ENSMUSP00000087372; ENSMUSG00000068479.
DR   GeneID; 100034361; -.
DR   GeneID; 67532; -.
DR   KEGG; mmu:100034361; -.
DR   KEGG; mmu:67532; -.
DR   UCSC; uc008lzg.1; mouse.
DR   CTD; 100034361; -.
DR   CTD; 67532; -.
DR   MGI; MGI:1914782; Mfap1.
DR   GeneTree; ENSGT00390000006487; -.
DR   HOGENOM; HBG608598; -.
DR   HOVERGEN; HBG052462; -.
DR   InParanoid; Q9CQU1; -.
DR   OMA; HRGAFYL; -.
DR   OrthoDB; EOG4B2SZ9; -.
DR   PhylomeDB; Q9CQU1; -.
DR   NextBio; 440476; -.
DR   ArrayExpress; Q9CQU1; -.
DR   Bgee; Q9CQU1; -.
DR   Genevestigator; Q9CQU1; -.
DR   GermOnline; ENSMUSG00000048222; Mus musculus.
DR   GermOnline; ENSMUSG00000068479; Mus musculus.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
DR   InterPro; IPR009730; MFAP1_C.
DR   PANTHER; PTHR15327; MFAP1_C; 1.
DR   Pfam; PF06991; MFAP1_C; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Extracellular matrix; Phosphoprotein; Secreted.
FT   CHAIN         1    439       Microfibrillar-associated protein 1.
FT                                /FTId=PRO_0000096459.
FT   COMPBIAS    134    139       Poly-Glu.
FT   MOD_RES      30     30       Phosphoserine (By similarity).
FT   MOD_RES      47     47       Phosphotyrosine (By similarity).
FT   MOD_RES      52     52       Phosphoserine.
FT   MOD_RES      53     53       Phosphoserine.
FT   MOD_RES     116    116       Phosphoserine.
FT   MOD_RES     118    118       Phosphoserine.
FT   MOD_RES     132    132       Phosphoserine.
FT   MOD_RES     133    133       Phosphoserine.
FT   MOD_RES     211    211       Phosphothreonine.
FT   MOD_RES     267    267       Phosphothreonine.
FT   MOD_RES     340    340       N6-acetyllysine (By similarity).
FT   MOD_RES     432    432       Phosphoserine (By similarity).
SQ   SEQUENCE   439 AA;  51954 MW;  5B57B1F1C42421E8 CRC64;
     MSVPSALMKQ PPIQSTAGAV PVRNEKGEIS MEKVKVKRYV SGKRPDYAPM ESSDEEDEEF
     QFIKKAKEQE AEPEEQEEDS SSDPRLRRLQ NRISEDVEER LARHRKIVEP EVVGESDSEV
     EGDAWRLERE DSSEEEEEEI DDEEIERRRG MMRQRAQERK NEEMEVMEVE DEGRSGEESE
     SESEYEEYTD SEDEMEPRLK PVFIRKKDRV TVQEREAEAL KQKELEQEAK RMAEERRKYT
     LKIVEEETKK ELEENKRSLA ALDALNTDDE NDEEEYEAWK VRELKRIKRE REDREALEKE
     KAEIERMRNL TEEERRAELR ANGKVITNKA VKGKYKFLQK YYHRGAFFMD EDEEVYKRDF
     SAPTLEDHFN KTILPKVMQV KNFGRSGRTK YTHLVDQDTT SFDSAWGQES AQNTKFFKQK
     AAGVRDVFER PSAKKRKTT
//
ID   TIM16_MOUSE             Reviewed;         125 AA.
AC   Q9CQV1; Q6EIX1;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit TIM16;
DE   AltName: Full=Mitochondria-associated granulocyte macrophage CSF-signaling molecule;
DE   AltName: Full=Presequence translocated-associated motor subunit PAM16;
GN   Name=Pam16; Synonyms=Magmas, Tim16, Timm16;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=21622933; PubMed=11750097; DOI=10.1016/S0301-472X(01)00749-4;
RA   Jubinsky P.T., Messer A., Bender J., Morris R.E., Ciraolo G.M.,
RA   Witte D.P., Hawley R.G., Short M.K.;
RT   "Identification and characterization of Magmas, a novel mitochondria-
RT   associated protein involved in granulocyte-macrophage colony-
RT   stimulating factor signal transduction.";
RL   Exp. Hematol. 29:1392-1402(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15984936;
RA   Peng J., Huang C.-H., Short M.K., Jubinsky P.T.;
RT   "Magmas gene structure and evolution.";
RL   In Silico Biol. 5:251-263(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Cerebellum;
RA   Hoshino J., Aruga J., Mikoshiba K.;
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Small intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Probable component of the PAM complex, a complex
CC       required for the translocation of transit peptide-containing
CC       proteins from the inner membrane into the mitochondrial matrix in
CC       an ATP-dependent manner. May be required to regulate the ATP-
CC       dependent activity (By similarity).
CC   -!- SUBUNIT: Probable component of the PAM complex at least composed
CC       of a mitochondrial HSP70 protein, GRPEL1 or GRPEL2, TIMM44,
CC       TIMM16/PAM16 and TIMM14/DNAJC19 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein (By similarity).
CC   -!- DOMAIN: The J-like region, although related to the J domain does
CC       not have co-chaperone activity (By similarity).
CC   -!- SIMILARITY: Belongs to the TIM16/PAM16 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF349454; AAL57766.1; -; mRNA.
DR   EMBL; AY320045; AAQ86806.1; -; Genomic_DNA.
DR   EMBL; AB073618; BAB91135.1; -; mRNA.
DR   EMBL; AK003227; BAB22656.1; -; mRNA.
DR   EMBL; AK008380; BAB25635.1; -; mRNA.
DR   EMBL; BC024346; AAH24346.1; -; mRNA.
DR   EMBL; BC096419; AAH96419.1; -; mRNA.
DR   IPI; IPI00133167; -.
DR   RefSeq; NP_079847.1; NM_025571.1.
DR   RefSeq; XP_001477733.1; XM_001477683.2.
DR   RefSeq; XP_003085727.1; XM_003085679.1.
DR   UniGene; Mm.354760; -.
DR   UniGene; Mm.391649; -.
DR   ProteinModelPortal; Q9CQV1; -.
DR   SMR; Q9CQV1; 54-113.
DR   STRING; Q9CQV1; -.
DR   PRIDE; Q9CQV1; -.
DR   Ensembl; ENSMUST00000014445; ENSMUSP00000014445; ENSMUSG00000014301.
DR   Ensembl; ENSMUST00000057649; ENSMUSP00000062209; ENSMUSG00000045886.
DR   GeneID; 100042179; -.
DR   GeneID; 66449; -.
DR   KEGG; mmu:100042179; -.
DR   KEGG; mmu:66449; -.
DR   UCSC; uc007xzx.1; mouse.
DR   CTD; 66449; -.
DR   MGI; MGI:1913699; Pam16.
DR   eggNOG; roNOG17463; -.
DR   GeneTree; ENSGT00390000012037; -.
DR   HOGENOM; HBG734654; -.
DR   HOVERGEN; HBG094040; -.
DR   InParanoid; Q9CQV1; -.
DR   OMA; VMGAQVV; -.
DR   OrthoDB; EOG4J9N1K; -.
DR   PhylomeDB; Q9CQV1; -.
DR   NextBio; 453066; -.
DR   ArrayExpress; Q9CQV1; -.
DR   Bgee; Q9CQV1; -.
DR   Genevestigator; Q9CQV1; -.
DR   GermOnline; ENSMUSG00000045886; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:UniProtKB-KW.
DR   InterPro; IPR005341; Protein_transpt.
DR   PANTHER; PTHR12388; Protein_transpt; 1.
DR   Pfam; PF03656; Pam16; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Protein transport; Translocation; Transport.
FT   CHAIN         1    125       Mitochondrial import inner membrane
FT                                translocase subunit TIM16.
FT                                /FTId=PRO_0000214079.
FT   REGION       58    110       J-like.
SQ   SEQUENCE   125 AA;  13785 MW;  54A71AB4EEA452ED CRC64;
     MAKYLAQIIV MGVQVVGRAF ARALRQEFAA SQAAADARGR AGHQSAAASN LSGLSLQEAQ
     QILNVSKLSP EEVQKNYEHL FKVNDKSVGG SFYLQSKVVR AKERLDEELR IQAQEDREKG
     QKPKT
//
ID   F134C_MOUSE             Reviewed;         466 AA.
AC   Q9CQV4; Q3TQL8; Q3U9Q7; Q8BQC4; Q922X3;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Protein FAM134C;
GN   Name=Fam134c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Corpora quadrigemina, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=19838196; DOI=10.1038/ng.464;
RA   Kurth I., Pamminger T., Hennings J.C., Soehendra D., Huebner A.K.,
RA   Rotthier A., Baets J., Senderek J., Topaloglu H., Farrell S.A.,
RA   Nuernberg G., Nurnberg P., De Jonghe P., Gal A., Kaether C.,
RA   Timmerman V., Huebner C.A.;
RT   "Mutations in FAM134B, encoding a newly identified Golgi protein,
RT   cause severe sensory and autonomic neuropathy.";
RL   Nat. Genet. 41:1179-1181(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9CQV4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CQV4-2; Sequence=VSP_025689;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Mainly expressed in the central nervous system
CC       and in parenchymatous organs including liver, lung and kidney.
CC   -!- SIMILARITY: Belongs to the FAM134 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK004960; BAB23700.1; -; mRNA.
DR   EMBL; AK004979; BAB23715.1; -; mRNA.
DR   EMBL; AK051025; BAC34501.1; -; mRNA.
DR   EMBL; AK151685; BAE30609.1; -; mRNA.
DR   EMBL; AK160000; BAE35548.1; -; mRNA.
DR   EMBL; AK163482; BAE37364.1; -; mRNA.
DR   EMBL; BX255926; CAM24470.1; -; Genomic_DNA.
DR   EMBL; BC006712; AAH06712.1; -; mRNA.
DR   EMBL; BC016089; AAH16089.1; -; mRNA.
DR   IPI; IPI00133174; -.
DR   IPI; IPI00177282; -.
DR   RefSeq; NP_080777.1; NM_026501.2.
DR   RefSeq; NP_083209.1; NM_028933.3.
DR   UniGene; Mm.33881; -.
DR   ProteinModelPortal; Q9CQV4; -.
DR   PhosphoSite; Q9CQV4; -.
DR   PRIDE; Q9CQV4; -.
DR   Ensembl; ENSMUST00000017946; ENSMUSP00000017946; ENSMUSG00000017802.
DR   Ensembl; ENSMUST00000107295; ENSMUSP00000102916; ENSMUSG00000017802.
DR   GeneID; 67998; -.
DR   KEGG; mmu:67998; -.
DR   UCSC; uc007lni.1; mouse.
DR   CTD; 67998; -.
DR   MGI; MGI:1915248; Fam134c.
DR   eggNOG; roNOG04572; -.
DR   GeneTree; ENSGT00530000063240; -.
DR   HOGENOM; HBG715298; -.
DR   HOVERGEN; HBG096339; -.
DR   InParanoid; Q9CQV4; -.
DR   OMA; VYHRLWD; -.
DR   OrthoDB; EOG4DBTDM; -.
DR   PhylomeDB; Q9CQV4; -.
DR   NextBio; 326174; -.
DR   ArrayExpress; Q9CQV4; -.
DR   Bgee; Q9CQV4; -.
DR   Genevestigator; Q9CQV4; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    466       Protein FAM134C.
FT                                /FTId=PRO_0000288470.
FT   TRANSMEM     81    101       Helical; (Potential).
FT   TRANSMEM    169    186       Helical; (Potential).
FT   TRANSMEM    187    207       Helical; (Potential).
FT   MOD_RES     229    229       Phosphoserine (By similarity).
FT   MOD_RES     258    258       Phosphoserine (By similarity).
FT   MOD_RES     260    260       Phosphoserine (By similarity).
FT   MOD_RES     274    274       Phosphoserine (By similarity).
FT   MOD_RES     283    283       Phosphothreonine (By similarity).
FT   MOD_RES     285    285       Phosphoserine (By similarity).
FT   MOD_RES     288    288       Phosphoserine (By similarity).
FT   MOD_RES     307    307       Phosphothreonine (By similarity).
FT   MOD_RES     310    310       Phosphothreonine (By similarity).
FT   MOD_RES     313    313       Phosphoserine (By similarity).
FT   MOD_RES     320    320       Phosphoserine (By similarity).
FT   MOD_RES     360    360       Phosphoserine (By similarity).
FT   MOD_RES     435    435       Phosphoserine (By similarity).
FT   MOD_RES     436    436       Phosphoserine (By similarity).
FT   MOD_RES     440    440       Phosphothreonine (By similarity).
FT   VAR_SEQ       1    181       Missing (in isoform 2).
FT                                /FTId=VSP_025689.
FT   CONFLICT    340    340       P -> H (in Ref. 1; BAE37364).
FT   CONFLICT    360    360       S -> T (in Ref. 1; BAE30609).
SQ   SEQUENCE   466 AA;  51638 MW;  5333A7910F023A6C CRC64;
     MEEAEGVAAA PGPASGLAFR GRRAMSGSWE RDQQVEAAQR TLVEVLGPYE PLLSRVQAAL
     VWERPARSAL WCLGLNAAFW FFALTSLRFV FLLAFSLMII VCIDQWKNKI WPEINVPRPD
     ALDNESWGFV HPRLLSVPEL CHHVAEVWVS GTIFIRNLLL FKKQNPGKFC LLSCGVLTFL
     AMLGRYIPGL LLSYLMLVII MMWPLAVYHR LWDRAYVRLK PVLQRLDFSV RGYMMSKQRE
     RQLRRRALHS ERATDSHSDS EEELAAFCPQ LDDSTVAREL AITDSEHSDA EVSCTENGTF
     NLSRGQTPLT EGSEDLDGHS DPEESFARDL PDFPSINVDP AGLDDEDDTS IGMPSLMYRS
     PPGAGDTQVL PASRNEAALP ELLLSSLPGG SNLTSNLASL VSQGMIQLAL SEASQTDPSG
     PPPRRATRGF LRAPSSDLDT DAEGDDFELL DQSELNQLDP ASSRSH
//
ID   TIM14_MOUSE             Reviewed;         116 AA.
AC   Q9CQV7; Q8R1N1; Q9D896;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit TIM14;
DE   AltName: Full=DnaJ homolog subfamily C member 19;
GN   Name=Dnajc19; Synonyms=Tim14, Timm14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Pancreas, Small intestine, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Probable component of the PAM complex, a complex
CC       required for the translocation of transit peptide-containing
CC       proteins from the inner membrane into the mitochondrial matrix in
CC       an ATP-dependent manner. May act as a co-chaperone that stimulate
CC       the ATP-dependent activity (By similarity).
CC   -!- SUBUNIT: Probable component of the PAM complex at least composed
CC       of a mitochondrial HSP70 protein, GRPEL1 or GRPEL2, TIMM44,
CC       TIMM16/PAM16 and TIMM14/DNAJC19 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass
CC       membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9CQV7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CQV7-2; Sequence=VSP_016390;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q9CQV7-3; Sequence=VSP_016391;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the TIM14 family.
CC   -!- SIMILARITY: Contains 1 J domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK007866; BAB25317.1; -; mRNA.
DR   EMBL; AK008267; BAB25565.1; -; mRNA.
DR   EMBL; AK010204; BAB26767.1; -; mRNA.
DR   EMBL; AK012051; BAB27993.1; -; mRNA.
DR   EMBL; BC024335; AAH24335.1; -; mRNA.
DR   IPI; IPI00111111; -.
DR   IPI; IPI00468992; -.
DR   IPI; IPI00624902; -.
DR   RefSeq; NP_001021382.1; NM_001026211.1.
DR   RefSeq; NP_080608.3; NM_026332.3.
DR   RefSeq; XP_003084767.1; XM_003084719.1.
DR   UniGene; Mm.274266; -.
DR   ProteinModelPortal; Q9CQV7; -.
DR   SMR; Q9CQV7; 48-116.
DR   STRING; Q9CQV7; -.
DR   PhosphoSite; Q9CQV7; -.
DR   PRIDE; Q9CQV7; -.
DR   Ensembl; ENSMUST00000011029; ENSMUSP00000011029; ENSMUSG00000027679.
DR   Ensembl; ENSMUST00000108195; ENSMUSP00000103830; ENSMUSG00000027679.
DR   GeneID; 100503724; -.
DR   GeneID; 67713; -.
DR   KEGG; mmu:100503724; -.
DR   KEGG; mmu:67713; -.
DR   UCSC; uc008oxm.1; mouse.
DR   UCSC; uc008oxo.1; mouse.
DR   UCSC; uc008oxp.1; mouse.
DR   CTD; 67713; -.
DR   MGI; MGI:1914963; Dnajc19.
DR   eggNOG; maNOG20087; -.
DR   GeneTree; ENSGT00390000017303; -.
DR   HOVERGEN; HBG057483; -.
DR   OMA; NKIREAH; -.
DR   OrthoDB; EOG43XV50; -.
DR   PhylomeDB; Q9CQV7; -.
DR   NextBio; 325345; -.
DR   ArrayExpress; Q9CQV7; -.
DR   Bgee; Q9CQV7; -.
DR   CleanEx; MM_DNAJC19; -.
DR   Genevestigator; Q9CQV7; -.
DR   GermOnline; ENSMUSG00000057330; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001623; DnaJ_N.
DR   Gene3D; G3DSA:1.10.287.110; DnaJ_N; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; DnaJ_N; 1.
DR   PROSITE; PS00636; DNAJ_1; FALSE_NEG.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Chaperone; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Protein transport; Translocation;
KW   Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    116       Mitochondrial import inner membrane
FT                                translocase subunit TIM14.
FT                                /FTId=PRO_0000071101.
FT   TOPO_DOM      2      3       Mitochondrial intermembrane (Potential).
FT   TRANSMEM      4     24       Helical; (Potential).
FT   TOPO_DOM     25    116       Mitochondrial matrix (Potential).
FT   DOMAIN       62    116       J.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      93     93       N6-acetyllysine (By similarity).
FT   VAR_SEQ      95    116       GSPYIAAKINEAKDLLEGQAKK -> PLVEEGLKPIPICRS
FT                                CSSICRRSILSCSTSYDQNKNPFTVCVCVHSSAHTGIHTPV
FT                                KPCETTM (in isoform 2).
FT                                /FTId=VSP_016390.
FT   VAR_SEQ      95    116       GSPYIAAKINEAKDLLEGQAKK -> KQLLLLYWTVNGIAN
FT                                SWCYECLCVSSFPVVDHIVVS (in isoform 3).
FT                                /FTId=VSP_016391.
SQ   SEQUENCE   116 AA;  12437 MW;  51E4313DB4F6083E CRC64;
     MASTVVAVGL TIAAAGFAGR YVLQAMKHVE PQVKQVFQSL PKSAFGGGYY RGGFEPKMTK
     REAALILGVS PTANKGKIRD AHRRIMLLNH PDKGGSPYIA AKINEAKDLL EGQAKK
//
ID   1433B_MOUSE             Reviewed;         246 AA.
AC   Q9CQV8; O70455; Q3TY33; Q3UAN6;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=14-3-3 protein beta/alpha;
DE   AltName: Full=Protein kinase C inhibitor protein 1;
DE            Short=KCIP-1;
DE   Contains:
DE     RecName: Full=14-3-3 protein beta/alpha, N-terminally processed;
GN   Name=Ywhab;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Karpitskiy V.V., Shaw A.S.;
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow, Embryo, Kidney, Liver, Thymus, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-12; 14-57; 61-70; 84-117; 128-169; 196-246 AND
RP   215-224, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   NITRATION [LARGE SCALE ANALYSIS] AT TYR-84 AND TYR-106, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16800626; DOI=10.1021/bi060474w;
RA   Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H.,
RA   Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J.,
RA   Squier T.C., Bigelow D.J.;
RT   "Endogenously nitrated proteins in mouse brain: links to
RT   neurodegenerative disease.";
RL   Biochemistry 45:8009-8022(2006).
CC   -!- FUNCTION: Adapter protein implicated in the regulation of a large
CC       spectrum of both general and specialized signaling pathway. Binds
CC       to a large number of partners, usually by recognition of a
CC       phosphoserine or phosphothreonine motif. Binding generally results
CC       in the modulation of the activity of the binding partner.
CC   -!- SUBUNIT: Homodimer, and heterodimer with YWHAG, YWHAE and YWHAQ.
CC       Interacts with SSH1 and TORC2/CRTC2. Interacts with GAB2 and YAP1
CC       (phosphorylated form) (By similarity).
CC   -!- INTERACTION:
CC       O54918:Bcl2l11; NbExp=1; IntAct=EBI-771608, EBI-526067;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Melanosome (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Long;
CC         IsoId=Q9CQV8-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=Q9CQV8-2; Sequence=VSP_018634;
CC         Note=No experimental confirmation available. Contains a
CC         N-acetylmethionine at position 1 (By similarity);
CC   -!- PTM: Isoform alpha differs from isoform beta in being
CC       phosphorylated (By similarity).
CC   -!- PTM: Isoform Short contains a N-acetylmethionine at position 1 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the 14-3-3 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF058797; AAC14343.1; -; mRNA.
DR   EMBL; AK002632; BAB22246.1; -; mRNA.
DR   EMBL; AK004872; BAB23631.1; -; mRNA.
DR   EMBL; AK011389; BAB27587.1; -; mRNA.
DR   EMBL; AK083367; BAC38886.1; -; mRNA.
DR   EMBL; AK144061; BAE25678.1; -; mRNA.
DR   EMBL; AK150414; BAE29538.1; -; mRNA.
DR   EMBL; AK151294; BAE30278.1; -; mRNA.
DR   EMBL; AK158932; BAE34730.1; -; mRNA.
DR   IPI; IPI00230682; -.
DR   IPI; IPI00760000; -.
DR   RefSeq; NP_061223.2; NM_018753.6.
DR   UniGene; Mm.34319; -.
DR   UniGene; Mm.477730; -.
DR   ProteinModelPortal; Q9CQV8; -.
DR   SMR; Q9CQV8; 3-233.
DR   IntAct; Q9CQV8; 612.
DR   STRING; Q9CQV8; -.
DR   PhosphoSite; Q9CQV8; -.
DR   UCD-2DPAGE; Q9CQV8; -.
DR   PRIDE; Q9CQV8; -.
DR   Ensembl; ENSMUST00000018470; ENSMUSP00000018470; ENSMUSG00000018326.
DR   GeneID; 54401; -.
DR   KEGG; mmu:54401; -.
DR   UCSC; uc008ntp.1; mouse.
DR   CTD; 54401; -.
DR   MGI; MGI:1891917; Ywhab.
DR   GeneTree; ENSGT00550000074221; -.
DR   HOGENOM; HBG611720; -.
DR   HOVERGEN; HBG050423; -.
DR   InParanoid; Q9CQV8; -.
DR   OMA; MGREYRE; -.
DR   OrthoDB; EOG4N30PR; -.
DR   PhylomeDB; Q9CQV8; -.
DR   NextBio; 311260; -.
DR   ArrayExpress; Q9CQV8; -.
DR   Bgee; Q9CQV8; -.
DR   Genevestigator; Q9CQV8; -.
DR   GermOnline; ENSMUSG00000018326; Mus musculus.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0019904; F:protein domain specific binding; IDA:MGI.
DR   GO; GO:0006605; P:protein targeting; IDA:MGI.
DR   InterPro; IPR000308; 14-3-3.
DR   PANTHER; PTHR18860; 14-3-3; 1.
DR   PIRSF; PIRSF000868; 14-3-3; 1.
DR   PRINTS; PR00305; 1433ZETA.
DR   PROSITE; PS00796; 1433_1; 1.
DR   PROSITE; PS00797; 1433_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative initiation; Cytoplasm;
KW   Direct protein sequencing; Nitration; Phosphoprotein.
FT   CHAIN         1    246       14-3-3 protein beta/alpha.
FT                                /FTId=PRO_0000367902.
FT   INIT_MET      1      1       Removed; alternate (By similarity).
FT   CHAIN         2    246       14-3-3 protein beta/alpha, N-terminally
FT                                processed.
FT                                /FTId=PRO_0000000005.
FT   SITE         58     58       Interaction with phosphoserine on
FT                                interacting protein (By similarity).
FT   SITE        129    129       Interaction with phosphoserine on
FT                                interacting protein (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine; in 14-3-3 protein
FT                                beta/alpha; alternate (By similarity).
FT   MOD_RES       2      2       N-acetylthreonine; in 14-3-3 protein
FT                                beta/alpha, N-terminally processed (By
FT                                similarity).
FT   MOD_RES       6      6       Phosphoserine (By similarity).
FT   MOD_RES      70     70       N6-acetyllysine (By similarity).
FT   MOD_RES      84     84       Nitrated tyrosine.
FT   MOD_RES     106    106       Nitrated tyrosine.
FT   MOD_RES     117    117       N6-acetyllysine (By similarity).
FT   MOD_RES     186    186       Phosphoserine (By similarity).
FT   VAR_SEQ       1      2       Missing (in isoform Short).
FT                                /FTId=VSP_018634.
FT   CONFLICT     10     10       Q -> H (in Ref. 1; AAC14343).
FT   CONFLICT     74     74       N -> D (in Ref. 1; AAC14343).
FT   CONFLICT    126    126       D -> Y (in Ref. 2; BAE29538/BAE30278).
SQ   SEQUENCE   246 AA;  28086 MW;  51C366ED85B38EED CRC64;
     MTMDKSELVQ KAKLAEQAER YDDMAAAMKA VTEQGHELSN EERNLLSVAY KNVVGARRSS
     WRVISSIEQK TERNEKKQQM GKEYREKIEA ELQDICNDVL ELLDKYLILN ATQAESKVFY
     LKMKGDYFRY LSEVASGENK QTTVSNSQQA YQEAFEISKK EMQPTHPIRL GLALNFSVFY
     YEILNSPEKA CSLAKTAFDE AIAELDTLNE ESYKDSTLIM QLLRDNLTLW TSENQGDEGD
     AGEGEN
//
ID   YKT6_MOUSE              Reviewed;         198 AA.
AC   Q9CQW1; O88595;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Synaptobrevin homolog YKT6;
DE            EC=2.3.1.-;
DE   Flags: Precursor;
GN   Name=Ykt6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   PubMed=11323436; DOI=10.1074/jbc.M102786200;
RA   Zhang T., Hong W.;
RT   "Ykt6 forms a SNARE complex with syntaxin 5, GS28, and Bet1 and
RT   participates in a late stage in endoplasmic reticulum-Golgi
RT   transport.";
RL   J. Biol. Chem. 276:27480-27487(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Amnion, Bone marrow, Kidney, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NMRI; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Vesicular soluble NSF attachment protein receptor (v-
CC       SNARE) mediating vesicle docking and fusion to a specific acceptor
CC       cellular compartment. Functions in endoplasmic reticulum to Golgi
CC       transport; as part of a SNARE complex composed of GOSR1, GOSR2 and
CC       STX5. Functions in early/recycling endosome to TGN transport; as
CC       part of a SNARE complex composed of BET1L, GOSR1 and STX5. Has a
CC       S-palmitoyl transferase activity (By similarity).
CC   -!- SUBUNIT: Identified in 2 different SNARE complexes; the first one
CC       composed of GOSR1, GOSR2 and STX5 and the second one composed of
CC       BET1L, GOSR1 and STX5 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity).
CC       Cytoplasmic vesicle membrane; Lipid-anchor; Cytoplasmic side (By
CC       similarity). Golgi apparatus membrane; Lipid-anchor; Cytoplasmic
CC       side (By similarity). Note=Probably cycles through vesicles
CC       between Golgi and endosomes (By similarity).
CC   -!- DOMAIN: The longin domain regulates palmitoylation and membrane
CC       targeting (By similarity).
CC   -!- PTM: Palmitoylated; catalyzes its own palmitoylation.
CC       Palmitoylation is required for Golgi targeting (By similarity).
CC   -!- PTM: Farnesylation is required for Golgi targeting (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the synaptobrevin family.
CC   -!- SIMILARITY: Contains 1 longin domain.
CC   -!- SIMILARITY: Contains 1 v-SNARE coiled-coil homology domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF076956; AAC26834.1; -; mRNA.
DR   EMBL; AK002916; BAB22455.1; -; mRNA.
DR   EMBL; AK007486; BAB25062.1; -; mRNA.
DR   EMBL; AK147098; BAE27674.1; -; mRNA.
DR   EMBL; AK150472; BAE29589.1; -; mRNA.
DR   EMBL; AK159253; BAE34934.1; -; mRNA.
DR   EMBL; AL645469; CAI25267.1; -; Genomic_DNA.
DR   EMBL; BC006760; AAH06760.1; -; mRNA.
DR   IPI; IPI00453771; -.
DR   RefSeq; NP_062635.2; NM_019661.4.
DR   UniGene; Mm.294821; -.
DR   HSSP; P36015; 1IOU.
DR   ProteinModelPortal; Q9CQW1; -.
DR   SMR; Q9CQW1; 1-192.
DR   STRING; Q9CQW1; -.
DR   PRIDE; Q9CQW1; -.
DR   Ensembl; ENSMUST00000002818; ENSMUSP00000002818; ENSMUSG00000002741.
DR   GeneID; 56418; -.
DR   KEGG; mmu:56418; -.
DR   UCSC; uc007hxp.1; mouse.
DR   CTD; 56418; -.
DR   MGI; MGI:1927550; Ykt6.
DR   eggNOG; roNOG15699; -.
DR   GeneTree; ENSGT00390000015164; -.
DR   HOGENOM; HBG324813; -.
DR   HOVERGEN; HBG088939; -.
DR   InParanoid; Q9CQW1; -.
DR   OMA; KIILXAR; -.
DR   OrthoDB; EOG4FFD2W; -.
DR   PhylomeDB; Q9CQW1; -.
DR   NextBio; 312560; -.
DR   ArrayExpress; Q9CQW1; -.
DR   Bgee; Q9CQW1; -.
DR   CleanEx; MM_YKT6; -.
DR   Genevestigator; Q9CQW1; -.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:HGNC.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral to plasma membrane; ISS:HGNC.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoleyltransferase activity; ISS:HGNC.
DR   GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; ISS:HGNC.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; ISS:HGNC.
DR   GO; GO:0006903; P:vesicle targeting; ISS:HGNC.
DR   InterPro; IPR010908; Longin.
DR   InterPro; IPR011012; Longin-like.
DR   InterPro; IPR001388; Synaptobrevin.
DR   Gene3D; G3DSA:3.30.450.50; Longin; 1.
DR   Pfam; PF00957; Synaptobrevin; 1.
DR   SUPFAM; SSF64356; Longin_like; 1.
DR   PROSITE; PS50859; LONGIN; 1.
DR   PROSITE; PS00417; SYNAPTOBREVIN; FALSE_NEG.
DR   PROSITE; PS50892; V_SNARE; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Cytoplasmic vesicle; ER-Golgi transport;
KW   Golgi apparatus; Lipoprotein; Membrane; Methylation; Palmitate;
KW   Prenylation; Protein transport; Transferase; Transport.
FT   CHAIN         1    195       Synaptobrevin homolog YKT6.
FT                                /FTId=PRO_0000280710.
FT   PROPEP      196    198       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000396662.
FT   DOMAIN        8    131       Longin.
FT   DOMAIN      138    198       v-SNARE coiled-coil homology.
FT   MOD_RES     195    195       Cysteine methyl ester (By similarity).
FT   LIPID       194    194       S-palmitoyl cysteine (By similarity).
FT   LIPID       195    195       S-farnesyl cysteine (By similarity).
FT   CONFLICT     95     95       E -> D (in Ref. 1; AAC26834).
FT   CONFLICT    165    165       E -> V (in Ref. 1; AAC26834).
SQ   SEQUENCE   198 AA;  22314 MW;  50A6E4EA7614592B CRC64;
     MKLYSLSVLY KGDPKAVLLK AAYDVSSFSF FQRSSVQEFM TFTSQLIVER SGKGSRASVK
     EQEYLCHVYV RSDSLAGVVI ADSEYPSRVA FTLLEKVLDE FSKQVDRIDW PVGSPATIQY
     TGLDDHLSKY QNPREADPMS KVQAELDETK IILHNTMESL LERGEKLDDL VSKSEVLGTQ
     SKAFYKTARK QNSCCAIM
//
ID   CYB5B_MOUSE             Reviewed;         146 AA.
AC   Q9CQX2; Q9D1M6; Q9D8R3;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Cytochrome b5 type B;
DE   AltName: Full=Cytochrome b5 outer mitochondrial membrane isoform;
DE   Flags: Precursor;
GN   Name=Cyb5b; Synonyms=Cyb5m;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Mammary gland, Pancreas, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Cytochrome b5 is a membrane bound hemoprotein which
CC       function as an electron carrier for several membrane bound
CC       oxygenases (By similarity).
CC   -!- SUBUNIT: Component of a complex composed of cytochrome b5, NADH-
CC       cytochrome b5 reductase (CYB5R3) and MOSC2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the cytochrome b5 family.
CC   -!- SIMILARITY: Contains 1 cytochrome b5 heme-binding domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK003333; BAB22721.1; -; mRNA.
DR   EMBL; AK003815; BAB23012.1; -; mRNA.
DR   EMBL; AK007780; BAB25251.1; -; mRNA.
DR   EMBL; AK019263; BAB31635.1; -; mRNA.
DR   EMBL; AK052810; BAC35156.1; -; mRNA.
DR   EMBL; AK088970; BAC40677.1; -; mRNA.
DR   EMBL; BC054749; AAH54749.1; -; mRNA.
DR   EMBL; BC058812; AAH58812.1; -; mRNA.
DR   EMBL; BC062980; AAH62980.1; -; mRNA.
DR   IPI; IPI00315794; -.
DR   RefSeq; NP_079834.2; NM_025558.5.
DR   UniGene; Mm.20242; -.
DR   ProteinModelPortal; Q9CQX2; -.
DR   SMR; Q9CQX2; 19-102.
DR   STRING; Q9CQX2; -.
DR   PhosphoSite; Q9CQX2; -.
DR   PRIDE; Q9CQX2; -.
DR   Ensembl; ENSMUST00000034400; ENSMUSP00000034400; ENSMUSG00000031924.
DR   GeneID; 66427; -.
DR   KEGG; mmu:66427; -.
DR   UCSC; uc009nhg.1; mouse.
DR   CTD; 66427; -.
DR   MGI; MGI:1913677; Cyb5b.
DR   GeneTree; ENSGT00510000046507; -.
DR   HOGENOM; HBG629516; -.
DR   HOVERGEN; HBG002653; -.
DR   InParanoid; Q9CQX2; -.
DR   OMA; DVHPSDL; -.
DR   OrthoDB; EOG40ZR00; -.
DR   PhylomeDB; Q9CQX2; -.
DR   NextBio; 321663; -.
DR   ArrayExpress; Q9CQX2; -.
DR   Bgee; Q9CQX2; -.
DR   CleanEx; MM_CYB5B; -.
DR   Genevestigator; Q9CQX2; -.
DR   GermOnline; ENSMUSG00000031924; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   InterPro; IPR023271; Aquaporin_like.
DR   InterPro; IPR001199; Cyt_B5.
DR   InterPro; IPR018506; Cyt_B5_heme-BS.
DR   Gene3D; G3DSA:3.10.120.10; Cyt_B5; 1.
DR   Gene3D; G3DSA:1.20.1080.10; MIP; 1.
DR   Pfam; PF00173; Cyt-b5; 1.
DR   PRINTS; PR00363; CYTOCHROMEB5.
DR   SUPFAM; SSF55856; Cyt_B5; 1.
DR   PROSITE; PS00191; CYTOCHROME_B5_1; 1.
DR   PROSITE; PS50255; CYTOCHROME_B5_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Electron transport; Heme; Iron; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix; Transport.
FT   PROPEP        1     11       By similarity.
FT                                /FTId=PRO_0000006473.
FT   CHAIN        12    146       Cytochrome b5 type B.
FT                                /FTId=PRO_0000006474.
FT   TRANSMEM    119    136       Helical; (Potential).
FT   DOMAIN       20     96       Cytochrome b5 heme-binding.
FT   METAL        55     55       Iron (heme axial ligand) (By similarity).
FT   METAL        79     79       Iron (heme axial ligand) (By similarity).
FT   MOD_RES      30     30       N6-acetyllysine (By similarity).
FT   MOD_RES      33     33       Phosphoserine.
FT   CONFLICT     31     31       R -> E (in Ref. 1; BAB25251).
FT   CONFLICT    142    142       D -> G (in Ref. 1; BAB22721).
SQ   SEQUENCE   146 AA;  16318 MW;  4ADA7C96A5F311DD CRC64;
     MATPEASGSG EKVEGSEPSV TYYRLEEVAK RNSAEETWMV IHGRVYDITR FLSEHPGGEE
     VLLEQAGADA TESFEDVGHS PDAREMLKQY YIGDVHPSDL KPKGDDKDPS KNNSCQSSWA
     YWFVPIVGAI LIGFLYRHFW ADSKSS
//
ID   RT36_MOUSE              Reviewed;         102 AA.
AC   Q9CQX8; Q4VA25;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=28S ribosomal protein S36, mitochondrial;
DE            Short=MRP-S36;
DE            Short=S36mt;
GN   Name=Mrps36;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Heart, Pancreas, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-59 AND SER-60, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBUNIT: Component of the mitochondrial ribosome small subunit
CC       (28S) which comprises a 12S rRNA and about 30 distinct proteins.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
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DR   EMBL; AK003111; BAB22573.1; -; mRNA.
DR   EMBL; AK003765; BAB22983.1; -; mRNA.
DR   EMBL; AK007512; BAB25081.1; -; mRNA.
DR   EMBL; AK009050; BAB26047.1; -; mRNA.
DR   EMBL; BC028499; AAH28499.1; -; mRNA.
DR   EMBL; BC096576; AAH96576.1; -; mRNA.
DR   IPI; IPI00315808; -.
DR   RefSeq; NP_079645.1; NM_025369.3.
DR   UniGene; Mm.306173; -.
DR   PhosphoSite; Q9CQX8; -.
DR   PRIDE; Q9CQX8; -.
DR   Ensembl; ENSMUST00000109333; ENSMUSP00000104957; ENSMUSG00000061474.
DR   GeneID; 66128; -.
DR   KEGG; mmu:66128; -.
DR   UCSC; uc007rrl.1; mouse.
DR   CTD; 66128; -.
DR   MGI; MGI:1913378; Mrps36.
DR   eggNOG; maNOG20661; -.
DR   GeneTree; ENSGT00390000017443; -.
DR   HOGENOM; HBG446904; -.
DR   HOVERGEN; HBG050076; -.
DR   InParanoid; Q9CQX8; -.
DR   OMA; PLIKFPD; -.
DR   OrthoDB; EOG447FVZ; -.
DR   NextBio; 320716; -.
DR   Bgee; Q9CQX8; -.
DR   CleanEx; MM_MRPS36; -.
DR   Genevestigator; Q9CQX8; -.
DR   GermOnline; ENSMUSG00000060389; Mus musculus.
DR   GO; GO:0005763; C:mitochondrial small ribosomal subunit; ISS:UniProtKB.
PE   1: Evidence at protein level;
KW   Mitochondrion; Phosphoprotein; Ribonucleoprotein; Ribosomal protein.
FT   CHAIN         1    102       28S ribosomal protein S36, mitochondrial.
FT                                /FTId=PRO_0000087734.
FT   MOD_RES      59     59       Phosphothreonine.
FT   MOD_RES      60     60       Phosphoserine.
SQ   SEQUENCE   102 AA;  11101 MW;  4582A0E4603BA764 CRC64;
     MGSKMASATR VVQVVKPHAP LIKFPNRRDK PKLSASEALG SAALPSHSSA ISQHSKGSTS
     PDLLMHQGPP DTAEIIKSLP QKYRRKPMSQ EEMEFIQRGG PE
//
ID   F103A_MOUSE             Reviewed;         119 AA.
AC   Q9CQY2; Q3TV69; Q9CWI1;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Protein FAM103A1;
GN   Name=Fam103a1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Cecum, Head, Stomach, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, C57BL/6J, and FVB/N;
RC   TISSUE=Brain, Kidney, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the FAM103 family.
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DR   EMBL; AK010694; BAB27126.1; -; mRNA.
DR   EMBL; AK011881; BAB27895.1; -; mRNA.
DR   EMBL; AK018614; BAB31308.1; -; mRNA.
DR   EMBL; AK079819; BAC37755.1; -; mRNA.
DR   EMBL; AK081301; BAC38188.1; -; mRNA.
DR   EMBL; AK085230; BAC39395.1; -; mRNA.
DR   EMBL; AK150938; BAE29973.1; -; mRNA.
DR   EMBL; AK160347; BAE35751.1; -; mRNA.
DR   EMBL; AK169392; BAE41139.1; -; mRNA.
DR   EMBL; BC058367; AAH58367.1; -; mRNA.
DR   EMBL; BC091760; AAH91760.1; -; mRNA.
DR   EMBL; BC096399; AAH96399.1; -; mRNA.
DR   IPI; IPI00133339; -.
DR   RefSeq; NP_080273.1; NM_025997.2.
DR   RefSeq; XP_001479190.1; XM_001479140.2.
DR   RefSeq; XP_003084836.1; XM_003084788.1.
DR   UniGene; Mm.241472; -.
DR   STRING; Q9CQY2; -.
DR   PhosphoSite; Q9CQY2; -.
DR   PRIDE; Q9CQY2; -.
DR   Ensembl; ENSMUST00000042166; ENSMUSP00000039065; ENSMUSG00000038646.
DR   Ensembl; ENSMUST00000085097; ENSMUSP00000082178; ENSMUSG00000048648.
DR   Ensembl; ENSMUST00000118190; ENSMUSP00000113339; ENSMUSG00000038646.
DR   GeneID; 100048057; -.
DR   GeneID; 67148; -.
DR   KEGG; mmu:100048057; -.
DR   KEGG; mmu:67148; -.
DR   UCSC; uc009icl.1; mouse.
DR   CTD; 67148; -.
DR   MGI; MGI:1914398; Fam103a1.
DR   eggNOG; roNOG17367; -.
DR   GeneTree; ENSGT00390000011190; -.
DR   HOGENOM; HBG126961; -.
DR   HOVERGEN; HBG081491; -.
DR   InParanoid; Q9CQY2; -.
DR   OMA; DNRRGWP; -.
DR   OrthoDB; EOG44TP98; -.
DR   PhylomeDB; Q9CQY2; -.
DR   NextBio; 461479; -.
DR   Bgee; Q9CQY2; -.
DR   CleanEx; MM_2610204K14RIK; -.
DR   Genevestigator; Q9CQY2; -.
DR   GermOnline; ENSMUSG00000038646; Mus musculus.
DR   GermOnline; ENSMUSG00000048648; Mus musculus.
PE   2: Evidence at transcript level;
KW   Phosphoprotein.
FT   CHAIN         1    119       Protein FAM103A1.
FT                                /FTId=PRO_0000089984.
FT   COMPBIAS     92    119       Gln/Tyr-rich.
FT   MOD_RES      36     36       Phosphoserine (By similarity).
FT   CONFLICT     95     95       Q -> E (in Ref. 1; BAB27126).
SQ   SEQUENCE   119 AA;  14556 MW;  43C7E1C68E14011C CRC64;
     MSDTSEEIPN FEEMFASRFT KDDKEYQEYL KRPPESPPIV EEWNSRAGGN QRNRGNWLQD
     NRQFRGRDNR RGWPSDNRSN QWHGRSWGNN NYPQQRPEPY YQQQYTQYGH NQRPPYGYY
//
ID   RL14_MOUSE              Reviewed;         217 AA.
AC   Q9CR57; Q9D8Q1;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=60S ribosomal protein L14;
GN   Name=Rpl14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SIMILARITY: Belongs to the ribosomal protein L14e family.
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DR   EMBL; AK007807; BAB25272.1; -; mRNA.
DR   EMBL; AK012277; BAB28136.1; -; mRNA.
DR   EMBL; AK013912; BAB29051.1; -; mRNA.
DR   IPI; IPI00133185; -.
DR   RefSeq; NP_080250.1; NM_025974.2.
DR   UniGene; Mm.289810; -.
DR   ProteinModelPortal; Q9CR57; -.
DR   SMR; Q9CR57; 3-120.
DR   STRING; Q9CR57; -.
DR   PhosphoSite; Q9CR57; -.
DR   PRIDE; Q9CR57; -.
DR   Ensembl; ENSMUST00000050737; ENSMUSP00000077118; ENSMUSG00000025794.
DR   GeneID; 67115; -.
DR   KEGG; mmu:67115; -.
DR   NMPDR; fig|10090.3.peg.21055; -.
DR   UCSC; uc009scr.1; mouse.
DR   CTD; 67115; -.
DR   MGI; MGI:1914365; Rpl14.
DR   GeneTree; ENSGT00390000007888; -.
DR   HOGENOM; HBG499844; -.
DR   HOVERGEN; HBG005187; -.
DR   InParanoid; Q9CR57; -.
DR   OrthoDB; EOG4Z0B71; -.
DR   PhylomeDB; Q9CR57; -.
DR   NextBio; 323609; -.
DR   ArrayExpress; Q9CR57; -.
DR   Bgee; Q9CR57; -.
DR   CleanEx; MM_RPL14; -.
DR   Genevestigator; Q9CR57; -.
DR   GermOnline; ENSMUSG00000025794; Mus musculus.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR002784; Ribosomal_L14e.
DR   InterPro; IPR014722; Transl_SH3-like_sub.
DR   Gene3D; G3DSA:2.30.30.30; Ribosomal_L2; 1.
DR   Pfam; PF01929; Ribosomal_L14e; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Phosphoprotein; Repeat; Ribonucleoprotein;
KW   Ribosomal protein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    217       60S ribosomal protein L14.
FT                                /FTId=PRO_0000132032.
FT   REPEAT      173    177       1-1; approximate.
FT   REPEAT      178    182       1-2.
FT   REPEAT      183    187       1-3.
FT   REPEAT      188    192       1-4.
FT   REPEAT      195    197       2-1.
FT   REPEAT      198    200       2-2.
FT   REGION      173    192       4 X 5 AA tandem repeats of Q-K-A-[APS]-X.
FT   REGION      195    200       2 X 3 AA tandem repeats of K-G-Q.
FT   MOD_RES      71     71       N6-acetyllysine (By similarity).
FT   MOD_RES      79     79       N6-acetyllysine (By similarity).
FT   MOD_RES      85     85       N6-acetyllysine (By similarity).
FT   MOD_RES     139    139       Phosphoserine (By similarity).
FT   CONFLICT     26     26       A -> T (in Ref. 1; BAB25272).
SQ   SEQUENCE   217 AA;  23564 MW;  1DB57CAA155D05A9 CRC64;
     MVFRRYVEVG RVAYISFGPH AGKLVAIVDV IDQNRALVDG PCTRVRRQAM PFKCMQLTDF
     ILKFPHSARQ KYVRKAWEKA DINTKWAATR WAKKIDARER KAKMTDFDRF KVMKAKKMRN
     RIIKTEVKKL QRAAILKASP KKAAVAKAAI AAAAAAAAAK AKVPAKKATG PGKKAAGQKA
     PAQKAAGQKA APPAKGQKGQ KTPAQKAPAP KAAGKKA
//
ID   G45IP_MOUSE             Reviewed;         222 AA.
AC   Q9CR59; Q8BT05;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Growth arrest and DNA damage-inducible proteins-interacting protein 1;
GN   Name=Gadd45gip1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney, Testis, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Acts as a negative regulator of G1 to S cell cycle phase
CC       progression by inhibiting cyclin-dependent kinases. Inhibitory
CC       effects are additive with GADD45 proteins but occurs also in the
CC       absence of GADD45 proteins. Acts as a repressor of the orphan
CC       nuclear receptor NR4A1 by inhibiting AB domain-mediated
CC       transcriptional activity. May be involved in the hormone-mediated
CC       regulation of NR4A1 transcriptional activity (By similarity).
CC   -!- SUBUNIT: Interacts with GADD45A, GADD45B and GADD45G. Interacts
CC       with NR4A1 via the NR4A1 AB domain (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -----------------------------------------------------------------------
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DR   EMBL; AK002738; BAB22318.1; -; mRNA.
DR   EMBL; AK003314; BAB22710.1; -; mRNA.
DR   EMBL; AK028227; BAC25826.1; -; mRNA.
DR   EMBL; AK009723; BAB26464.1; -; mRNA.
DR   EMBL; AK019570; BAB31797.1; -; mRNA.
DR   EMBL; BC061069; AAH61069.1; -; mRNA.
DR   IPI; IPI00133193; -.
DR   RefSeq; NP_899202.3; NM_183358.4.
DR   UniGene; Mm.255539; -.
DR   UniGene; Mm.467206; -.
DR   ProteinModelPortal; Q9CR59; -.
DR   STRING; Q9CR59; -.
DR   PhosphoSite; Q9CR59; -.
DR   PRIDE; Q9CR59; -.
DR   Ensembl; ENSMUST00000036734; ENSMUSP00000037783; ENSMUSG00000033751.
DR   GeneID; 102060; -.
DR   KEGG; mmu:102060; -.
DR   UCSC; uc009mnj.1; mouse.
DR   CTD; 102060; -.
DR   MGI; MGI:1914947; Gadd45gip1.
DR   eggNOG; roNOG17246; -.
DR   GeneTree; ENSGT00390000013719; -.
DR   HOGENOM; HBG261042; -.
DR   HOVERGEN; HBG068845; -.
DR   InParanoid; Q9CR59; -.
DR   OMA; MPQMIEN; -.
DR   OrthoDB; EOG4CC42T; -.
DR   PhylomeDB; Q9CR59; -.
DR   NextBio; 355256; -.
DR   ArrayExpress; Q9CR59; -.
DR   Bgee; Q9CR59; -.
DR   Genevestigator; Q9CR59; -.
DR   GermOnline; ENSMUSG00000033751; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR018472; Damage-induce-interacting_prot.
DR   Pfam; PF10147; CR6_interact; 1.
PE   2: Evidence at transcript level;
KW   Cell cycle; Coiled coil; Nucleus; Phosphoprotein.
FT   CHAIN         1    222       Growth arrest and DNA damage-inducible
FT                                proteins-interacting protein 1.
FT                                /FTId=PRO_0000228621.
FT   COILED       98    207       Potential.
FT   MOTIF       184    200       Nuclear localization signal (Potential).
FT   COMPBIAS     28     31       Poly-Pro.
FT   MOD_RES     221    221       Phosphoserine (By similarity).
FT   CONFLICT    184    184       K -> Q (in Ref. 1; BAC25826).
SQ   SEQUENCE   222 AA;  25820 MW;  1CB0F5AF4ACFF504 CRC64;
     MAALAMRSGY LLRLSVALGP RSRSYRAPPP PRRRPGPHSP DPENLLTPRW QLTPRYVAKQ
     FGRHGAISGV PPASLWPTPE QLRELEAEEQ EWYPSLATMQ ESLRLQQQAL EARRQAREQR
     IAECMAKMPQ MIENWRKQKR ERWEKIQADK ERRARLQAEA QERLGYHVDP RSARFQELLQ
     DLDKQQRKRL KEERQRQKKE ARIAAMASAE AQDSAVSGEP SS
//
ID   NDUB7_MOUSE             Reviewed;         137 AA.
AC   Q9CR61;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 7;
DE   AltName: Full=Complex I-B18;
DE            Short=CI-B18;
DE   AltName: Full=NADH-ubiquinone oxidoreductase B18 subunit;
GN   Name=Ndufb7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 8-35; 38-65; 72-97 AND 122-137, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Accessory subunit of the mitochondrial membrane
CC       respiratory chain NADH dehydrogenase (Complex I), that is believed
CC       not to be involved in catalysis. Complex I functions in the
CC       transfer of electrons from NADH to the respiratory chain. The
CC       immediate electron acceptor for the enzyme is believed to be
CC       ubiquinone (By similarity).
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein; Matrix side (By similarity).
CC   -!- SIMILARITY: Belongs to the complex I NDUFB7 subunit family.
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DR   EMBL; AK003300; BAB22701.1; -; mRNA.
DR   EMBL; AK002678; BAB22280.1; -; mRNA.
DR   EMBL; BC034787; AAH34787.1; -; mRNA.
DR   IPI; IPI00133215; -.
DR   RefSeq; NP_080119.1; NM_025843.3.
DR   UniGene; Mm.29683; -.
DR   STRING; Q9CR61; -.
DR   PhosphoSite; Q9CR61; -.
DR   PRIDE; Q9CR61; -.
DR   Ensembl; ENSMUST00000036996; ENSMUSP00000037341; ENSMUSG00000033938.
DR   GeneID; 66916; -.
DR   KEGG; mmu:66916; -.
DR   UCSC; uc009mkk.1; mouse.
DR   CTD; 66916; -.
DR   MGI; MGI:1914166; Ndufb7.
DR   eggNOG; roNOG16392; -.
DR   GeneTree; ENSGT00390000018759; -.
DR   HOGENOM; HBG714360; -.
DR   HOVERGEN; HBG001948; -.
DR   InParanoid; Q9CR61; -.
DR   OMA; YCEHLDY; -.
DR   OrthoDB; EOG49CQ96; -.
DR   PhylomeDB; Q9CR61; -.
DR   NextBio; 323013; -.
DR   ArrayExpress; Q9CR61; -.
DR   Bgee; Q9CR61; -.
DR   Genevestigator; Q9CR61; -.
DR   GermOnline; ENSMUSG00000033938; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008698; NADH_UbQ_OxRdtase_B18_su.
DR   PANTHER; PTHR20900; NDUFB7; 1.
DR   Pfam; PF05676; NDUF_B7; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; Lipoprotein; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Myristate;
KW   Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    137       NADH dehydrogenase [ubiquinone] 1 beta
FT                                subcomplex subunit 7.
FT                                /FTId=PRO_0000118812.
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
SQ   SEQUENCE   137 AA;  16331 MW;  1B83033240133FE9 CRC64;
     MGAHLTRRYL WDASVEPDPE KIPSFPPDLG FPERKERVMV ATQQEMMDAQ LTLQQRDYCA
     HYLIRLLKCK RDSFPNFLAC KHEQHDWDYC EHLDYVKRMK EFERERRLLQ RKKRRALKEA
     RVAQGQGEGE VGPEVAL
//
ID   UCRI_MOUSE              Reviewed;         274 AA.
AC   Q9CR68; Q5SVV1;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Cytochrome b-c1 complex subunit Rieske, mitochondrial;
DE            EC=1.10.2.2;
DE   AltName: Full=Complex III subunit 5;
DE   AltName: Full=Cytochrome b-c1 complex subunit 5;
DE   AltName: Full=Rieske iron-sulfur protein;
DE            Short=RISP;
DE   AltName: Full=Ubiquinol-cytochrome c reductase iron-sulfur subunit;
DE   Contains:
DE     RecName: Full=Cytochrome b-c1 complex subunit 11;
DE     AltName: Full=Complex III subunit IX;
DE     AltName: Full=Ubiquinol-cytochrome c reductase 8 kDa protein;
DE   Flags: Precursor;
GN   Name=Uqcrfs1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 8-46; 85-92; 94-101; 131-151; 156-163; 171-177 AND
RP   183-204, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Component of the ubiquinol-cytochrome c reductase
CC       complex (complex III or cytochrome b-c1 complex), which is a
CC       respiratory chain that generates an electrochemical potential
CC       coupled to ATP synthesis.
CC   -!- FUNCTION: The transit peptide of the Rieske protein seems to form
CC       part of the bc1 complex and is considered to be the subunit 11/IX
CC       of that complex (By similarity).
CC   -!- CATALYTIC ACTIVITY: QH(2) + 2 ferricytochrome c = Q + 2
CC       ferrocytochrome c + 2 H(+).
CC   -!- COFACTOR: Binds 1 2Fe-2S cluster per subunit (By similarity).
CC   -!- SUBUNIT: The bc1 complex contains 11 subunits: 3 respiratory
CC       subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core
CC       proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight
CC       proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9,
CC       UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1) (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
CC   -!- MISCELLANEOUS: The Rieske protein is a high potential 2Fe-2S
CC       protein.
CC   -!- SIMILARITY: Contains 1 Rieske domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK003966; BAB23097.1; -; mRNA.
DR   EMBL; AK012180; BAB28081.1; -; mRNA.
DR   EMBL; AK014470; BAB29374.1; -; mRNA.
DR   EMBL; AK153139; BAE31751.1; -; mRNA.
DR   EMBL; AK152391; BAE31179.1; -; mRNA.
DR   EMBL; AL611944; CAI24872.1; -; Genomic_DNA.
DR   EMBL; BC019934; AAH19934.1; -; mRNA.
DR   IPI; IPI00133240; -.
DR   RefSeq; NP_079986.1; NM_025710.2.
DR   UniGene; Mm.181933; -.
DR   ProteinModelPortal; Q9CR68; -.
DR   SMR; Q9CR68; 1-57, 79-274.
DR   STRING; Q9CR68; -.
DR   PhosphoSite; Q9CR68; -.
DR   PRIDE; Q9CR68; -.
DR   Ensembl; ENSMUST00000042834; ENSMUSP00000045284; ENSMUSG00000038462.
DR   GeneID; 66694; -.
DR   KEGG; mmu:66694; -.
DR   NMPDR; fig|10090.3.peg.27643; -.
DR   UCSC; uc007pyv.1; mouse.
DR   CTD; 66694; -.
DR   MGI; MGI:1913944; Uqcrfs1.
DR   eggNOG; roNOG07292; -.
DR   GeneTree; ENSGT00390000001014; -.
DR   HOGENOM; HBG668715; -.
DR   HOVERGEN; HBG001040; -.
DR   InParanoid; Q9CR68; -.
DR   OMA; DYRRAEV; -.
DR   OrthoDB; EOG4VMFG4; -.
DR   PhylomeDB; Q9CR68; -.
DR   BRENDA; 1.10.2.2; 244.
DR   NextBio; 322393; -.
DR   ArrayExpress; Q9CR68; -.
DR   Bgee; Q9CR68; -.
DR   Genevestigator; Q9CR68; -.
DR   GermOnline; ENSMUSG00000038462; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008121; F:ubiquinol-cytochrome-c reductase activity; IEA:EC.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   InterPro; IPR011070; Globular_prot_asu/bsu.
DR   InterPro; IPR017941; Rieske_2Fe-2S.
DR   InterPro; IPR014349; Rieske_Fe-S_prot.
DR   InterPro; IPR005805; Rieske_Fe-S_prot_C.
DR   InterPro; IPR015248; Ubiqinol_cyt_c_Rdtase_N.
DR   InterPro; IPR006317; Ubiquinol_cyt_c_Rdtase_Fe-S-su.
DR   InterPro; IPR004192; Ubiquinol_cyt_Rdtase_TM.
DR   Gene3D; G3DSA:2.102.10.10; Rieske_reg; 1.
DR   Gene3D; G3DSA:1.20.5.270; Ubiquinol_cyt_Rdtase_TM; 1.
DR   PANTHER; PTHR10134; Rieske; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   Pfam; PF09165; Ubiq-Cytc-red_N; 1.
DR   Pfam; PF02921; UCR_TM; 1.
DR   PRINTS; PR00162; RIESKE.
DR   SUPFAM; SSF56568; AlphaBeta_subunt; 1.
DR   SUPFAM; SSF50022; Rieske_dom; 1.
DR   SUPFAM; SSF81502; UCR_TM_region; 1.
DR   TIGRFAMs; TIGR01416; Rieske_proteo; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   1: Evidence at protein level;
KW   2Fe-2S; Direct protein sequencing; Disulfide bond; Electron transport;
KW   Iron; Iron-sulfur; Membrane; Metal-binding; Mitochondrion;
KW   Mitochondrion inner membrane; Oxidoreductase; Respiratory chain;
KW   Transit peptide; Transmembrane; Transport.
FT   CHAIN         1     78       Cytochrome b-c1 complex subunit 11 (By
FT                                similarity).
FT                                /FTId=PRO_0000307244.
FT   TRANSIT       1     78       Mitochondrion (By similarity).
FT   CHAIN        79    274       Cytochrome b-c1 complex subunit Rieske,
FT                                mitochondrial.
FT                                /FTId=PRO_0000030667.
FT   DOMAIN      187    272       Rieske.
FT   METAL       217    217       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL       219    219       Iron-sulfur (2Fe-2S); via pros nitrogen
FT                                (By similarity).
FT   METAL       236    236       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL       239    239       Iron-sulfur (2Fe-2S); via pros nitrogen
FT                                (By similarity).
FT   DISULFID    222    238       By similarity.
SQ   SEQUENCE   274 AA;  29368 MW;  17E55DE0BBD09961 CRC64;
     MLSVAARSGP FAPVLSATSR GVAGALRPLL QGAVPAASEP PVLDVKRPFL CRESLSGQAA
     ARPLVATVGL NVPASVRFSH TDVKVPDFSD YRRAEVLDST KSSKESSEAR KGFSYLVTAT
     TTVGVAYAAK NVVSQFVSSM SASADVLAMS KIEIKLSDIP EGKNMAFKWR GKPLFVRHRT
     KKEIDQEAAV EVSQLRDPQH DLDRVKKPEW VILIGVCTHL GCVPIANAGD FGGYYCPCHG
     SHYDASGRIR KGPAPLNLEV PAYEFTSDDV VVVG
//
ID   CHSP1_MOUSE             Reviewed;         148 AA.
AC   Q9CR86;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Calcium-regulated heat stable protein 1;
DE   AltName: Full=Calcium-regulated heat-stable protein of 24 kDa;
DE            Short=CRHSP-24;
GN   Name=Carhsp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Pancreas;
RA   Lee S.-H., Williams J.;
RT   "Identification and regulation of the phosphorylation sites on the
RT   novel calcineurin substrate CRHSP-24.";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Kidney, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-33 AND SER-42,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-33 AND SER-42,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-33, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-33, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-33 AND SER-42,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: May play a role in acinar cell metabolism.
CC   -!- SUBUNIT: Interacts with STYX.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- PTM: Dephosphorylated by calcineurin in a Ca(2+) dependent manner
CC       (By similarity).
CC   -!- SIMILARITY: Contains 1 CSD (cold-shock) domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
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CC   -----------------------------------------------------------------------
DR   EMBL; AF414101; AAL07470.1; -; mRNA.
DR   EMBL; AK004711; BAB23495.1; -; mRNA.
DR   EMBL; AK002853; BAB22408.1; -; mRNA.
DR   EMBL; AK003926; BAB23077.1; -; mRNA.
DR   EMBL; BC011225; AAH11225.1; -; mRNA.
DR   IPI; IPI00133349; -.
DR   RefSeq; NP_080097.1; NM_025821.2.
DR   RefSeq; XP_003086339.1; XM_003086291.1.
DR   UniGene; Mm.142095; -.
DR   ProteinModelPortal; Q9CR86; -.
DR   SMR; Q9CR86; 63-126.
DR   STRING; Q9CR86; -.
DR   PhosphoSite; Q9CR86; -.
DR   PRIDE; Q9CR86; -.
DR   Ensembl; ENSMUST00000008537; ENSMUSP00000008537; ENSMUSG00000008393.
DR   GeneID; 100040232; -.
DR   GeneID; 52502; -.
DR   KEGG; mmu:100040232; -.
DR   KEGG; mmu:52502; -.
DR   UCSC; uc007yct.1; mouse.
DR   CTD; 52502; -.
DR   MGI; MGI:1196368; Carhsp1.
DR   GeneTree; ENSGT00390000000022; -.
DR   HOGENOM; HBG717773; -.
DR   HOVERGEN; HBG050947; -.
DR   InParanoid; Q9CR86; -.
DR   OMA; ASEGPVY; -.
DR   OrthoDB; EOG4V4390; -.
DR   PhylomeDB; Q9CR86; -.
DR   NextBio; 459697; -.
DR   Bgee; Q9CR86; -.
DR   CleanEx; MM_CARHSP1; -.
DR   Genevestigator; Q9CR86; -.
DR   GermOnline; ENSMUSG00000008393; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR019844; Cold-shock_CS.
DR   InterPro; IPR011129; Cold_shock_prot.
DR   InterPro; IPR002059; CSP_DNA-bd.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR016027; NA-bd_OB-fold-like.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   Pfam; PF00313; CSD; 1.
DR   SMART; SM00357; CSP; 1.
DR   SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR   PROSITE; PS00352; COLD_SHOCK; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein.
FT   CHAIN         1    148       Calcium-regulated heat stable protein 1.
FT                                /FTId=PRO_0000100231.
FT   DOMAIN       63    130       CSD.
FT   MOD_RES      31     31       Phosphoserine.
FT   MOD_RES      33     33       Phosphoserine.
FT   MOD_RES      42     42       Phosphoserine.
FT   MOD_RES      53     53       Phosphoserine (By similarity).
FT   MOD_RES     147    147       Phosphoserine (By similarity).
SQ   SEQUENCE   148 AA;  16062 MW;  117F3FE85D11BC93 CRC64;
     MSSEPPPPPL QPPTHQTSVG LLDTPRTRDR SPSPLRGNVV PSPLPTRRTR TFSATVRASQ
     GPVYKGVCKC FCRSKGHGFI TPADGGPDIF LHISDVEGEY VPVEGDEVTY KMCSIPPKNE
     KLQAVEVVIT HLAPGTKHET WSGHVISN
//
ID   NECP1_MOUSE             Reviewed;         275 AA.
AC   Q9CR95; Q3TH13; Q78JW3; Q8C4P1;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 2.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Adaptin ear-binding coat-associated protein 1;
DE   AltName: Full=NECAP endocytosis-associated protein 1;
DE            Short=NECAP-1;
GN   Name=Necap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Embryonic head, Embryonic heart, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION, INTERACTION WITH AP1G1 AND AP2A1, TISSUE SPECIFICITY,
RP   SUBCELLULAR LOCATION, AND FUNCTION.
RX   MEDLINE=22954133; PubMed=14555962; DOI=10.1038/sj.embor.7400004;
RA   Ritter B., Philie J., Girard M., Tung E.C., Blondeau F.,
RA   McPherson P.S.;
RT   "Identification of a family of endocytic proteins that define a new
RT   alpha-adaptin ear-binding motif.";
RL   EMBO Rep. 4:1089-1095(2003).
RN   [4]
RP   MUTAGENESIS OF TRP-272; VAL-273; GLN-274 AND PHE-275, AND INTERACTION
RP   WITH AP2A1; AP2A2 AND AP1G1.
RX   PubMed=15359277; DOI=10.1038/sj.emboj.7600378;
RA   Ritter B., Denisov A.Y., Philie J., Deprez C., Tung E.C., Gehring K.,
RA   McPherson P.S.;
RT   "Two WXXF-based motifs in NECAPs define the specificity of accessory
RT   protein binding to AP-1 and AP-2.";
RL   EMBO J. 23:3701-3710(2004).
RN   [5]
RP   INTERACTION WITH GGA1; GGA2; GGA3 AND AP1G1.
RX   PubMed=14665628; DOI=10.1074/jbc.M311873200;
RA   Mattera R., Ritter B., Sidhu S.S., McPherson P.S., Bonifacino J.S.;
RT   "Definition of the consensus motif recognized by gamma-adaptin ear
RT   domains.";
RL   J. Biol. Chem. 279:8018-8028(2004).
RN   [6]
RP   STRUCTURE BY NMR OF 1-133.
RA   Denisov A.Y., Ritter B., McPherson P.S., Gehring K.;
RT   "Solution structure of NECAP1 protein.";
RL   Submitted (JUL-2005) to the PDB data bank.
CC   -!- FUNCTION: Involved in endocytosis (By similarity).
CC   -!- SUBUNIT: Interacts with AP1G1 and AP2A1 components of the adapter
CC       protein complexes AP-1 and AP-2. Interacts with the GAE domain
CC       proteins GGA1, GGA2 and GGA3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle
CC       membrane. Cell membrane. Note=Colocalizes with AP-2 at the plasma
CC       membrane.
CC   -!- TISSUE SPECIFICITY: Expressed primarily in brain (at protein
CC       level).
CC   -!- DOMAIN: The WXXF motifs mediate binding of accessory proteins to
CC       the ear-domain of AP-1, GGAs and AP-2 through hydrophobic
CC       interactions. Selective binding to the GAE domains of AP-1 or to
CC       the alpha-ear domain of AP-2 is tuned by the acidic context
CC       surrounding the motif and the properties of the second residue of
CC       the motif itself. The WXXF motif 1, which is preceded by an acidic
CC       residue and has a glycine in second position mediates specific
CC       interaction with AP-1. The WXXF motif 2, which is followed by the
CC       C-terminal carboxyl group negative charge, allows specific
CC       interaction with AP-2.
CC   -!- SIMILARITY: Belongs to the NECAP family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK004805; BAB23577.2; -; mRNA.
DR   EMBL; AK005263; BAB23915.2; -; mRNA.
DR   EMBL; AK081598; BAC38266.1; -; mRNA.
DR   EMBL; AK168500; BAE40385.1; -; mRNA.
DR   EMBL; BC011466; AAH11466.2; -; mRNA.
DR   EMBL; BK000656; DAA01433.1; -; mRNA.
DR   IPI; IPI00225533; -.
DR   RefSeq; NP_080543.2; NM_026267.2.
DR   UniGene; Mm.288114; -.
DR   PDB; 1TQZ; NMR; -; A=1-133.
DR   PDBsum; 1TQZ; -.
DR   ProteinModelPortal; Q9CR95; -.
DR   SMR; Q9CR95; 1-133.
DR   MINT; MINT-4125077; -.
DR   STRING; Q9CR95; -.
DR   PhosphoSite; Q9CR95; -.
DR   PRIDE; Q9CR95; -.
DR   Ensembl; ENSMUST00000032477; ENSMUSP00000032477; ENSMUSG00000030327.
DR   GeneID; 67602; -.
DR   KEGG; mmu:67602; -.
DR   UCSC; uc009dpt.1; mouse.
DR   CTD; 67602; -.
DR   MGI; MGI:1914852; Necap1.
DR   GeneTree; ENSGT00390000009359; -.
DR   HOVERGEN; HBG060621; -.
DR   InParanoid; Q9CR95; -.
DR   OMA; ESQEMDS; -.
DR   OrthoDB; EOG4M399M; -.
DR   PhylomeDB; Q9CR95; -.
DR   NextBio; 325013; -.
DR   ArrayExpress; Q9CR95; -.
DR   Bgee; Q9CR95; -.
DR   CleanEx; MM_NECAP1; -.
DR   Genevestigator; Q9CR95; -.
DR   GermOnline; ENSMUSG00000030327; Mus musculus.
DR   GO; GO:0030125; C:clathrin vesicle coat; IDA:UniProtKB.
DR   GO; GO:0005905; C:coated pit; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR012466; NECAP-1.
DR   Pfam; PF07933; DUF1681; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Cytoplasmic vesicle; Endocytosis;
KW   Membrane; Phosphoprotein; Protein transport; Repeat; Transport.
FT   CHAIN         1    275       Adaptin ear-binding coat-associated
FT                                protein 1.
FT                                /FTId=PRO_0000213068.
FT   MOTIF       252    255       WXXF motif 1.
FT   MOTIF       272    275       WXXF motif 2.
FT   MOD_RES     207    207       Phosphoserine (By similarity).
FT   MUTAGEN     270    270       S->D: Loss of binding to AP-2 and can
FT                                bind to AP-1; when associated with G-273.
FT   MUTAGEN     272    272       W->A,F,Y: Loss of binding to AP-2.
FT   MUTAGEN     273    273       V->A,D,E,I: No effect on binding to AP-2.
FT   MUTAGEN     273    273       V->G: Loss of binding to AP-2 and can
FT                                bind to AP-1; when associated with D-270.
FT   MUTAGEN     273    273       V->L,N,P,S: Loss of binding to AP-2.
FT   MUTAGEN     274    274       Q->A,M,N,S,T: No effect on binding to AP-
FT                                2.
FT   MUTAGEN     275    275       F->A,F,Y: Loss of binding to AP-2.
FT   MUTAGEN     275    275       F->W: No effect on binding to AP-2.
FT   STRAND       15     21
FT   STRAND       27     30
FT   HELIX        33     36
FT   STRAND       39     41
FT   STRAND       43     50
FT   STRAND       53     61
FT   STRAND       70     74
FT   STRAND       82     84
FT   STRAND       92     98
FT   TURN         99    101
FT   STRAND      102    109
FT   HELIX       113    127
SQ   SEQUENCE   275 AA;  29639 MW;  B238B083746FF915 CRC64;
     MAAELEYESV LCVKPDVSVY RIPPRASNRG YRASDWKLDQ PDWTGRLRIT SKGKIAYIKL
     EDKVSGELFA QAPVEQYPGI AVETVTDSSR YFVIRIQDGT GRSAFIGIGF TDRGDAFDFN
     VSLQDHFKWV KQETEISKES QEMDNRPKLD LGFKEGQTIK LSIGNITAKK GGASKPRASG
     TGGLSLLPPP PGGKVTIPPP SSSVAISNHV TPPPIPKSNH GGNDSDILLD LDSPAPVSTS
     APAPVSTSND LWGDFSTASS SVPNQAPQPS NWVQF
//
ID   EXOS5_MOUSE             Reviewed;         235 AA.
AC   Q9CRA8; Q8K1J2;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Exosome complex exonuclease RRP46;
DE            EC=3.1.13.-;
DE   AltName: Full=Exosome component 5;
DE   AltName: Full=Ribosomal RNA-processing protein 46;
GN   Name=Exosc5; Synonyms=D7Wsu180e, Rrp46;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pancreas, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Component of the exosome 3'->5' exoribonuclease complex,
CC       a complex that degrades inherently unstable mRNAs containing AU-
CC       rich elements (AREs) within their 3'-untranslated regions.
CC       Required for the 3'-processing of the 7S pre-RNA to the mature
CC       5.8S rRNA. Has a 3'-5' exonuclease activity (By similarity).
CC   -!- SUBUNIT: Component of the exosome core complex at least composed
CC       of the core components EXOSC1, EXOSC2, EXOSC3, EXOSC4, EXOSC5,
CC       EXOSC6, EXOSC7, EXOSC8 and EXOSC9. Also associated with the GTPase
CC       RAN (By similarity). Interacts directly with EXOSC1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity).
CC   -!- SIMILARITY: Belongs to the RNase PH family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK007372; BAB24993.1; -; mRNA.
DR   EMBL; AK006475; BAB24607.1; -; mRNA.
DR   EMBL; BC034358; AAH34358.1; -; mRNA.
DR   IPI; IPI00133532; -.
DR   RefSeq; NP_613052.1; NM_138586.3.
DR   UniGene; Mm.207484; -.
DR   UniGene; Mm.27853; -.
DR   ProteinModelPortal; Q9CRA8; -.
DR   SMR; Q9CRA8; 26-234.
DR   IntAct; Q9CRA8; 1.
DR   STRING; Q9CRA8; -.
DR   PhosphoSite; Q9CRA8; -.
DR   PRIDE; Q9CRA8; -.
DR   Ensembl; ENSMUST00000079634; ENSMUSP00000078580; ENSMUSG00000061286.
DR   GeneID; 27998; -.
DR   KEGG; mmu:27998; -.
DR   UCSC; uc009fti.1; mouse.
DR   CTD; 27998; -.
DR   MGI; MGI:107889; Exosc5.
DR   GeneTree; ENSGT00550000075002; -.
DR   HOGENOM; HBG737187; -.
DR   HOVERGEN; HBG051520; -.
DR   InParanoid; Q9CRA8; -.
DR   OMA; IFQFYRD; -.
DR   OrthoDB; EOG4PZJ7M; -.
DR   PhylomeDB; Q9CRA8; -.
DR   NextBio; 306496; -.
DR   ArrayExpress; Q9CRA8; -.
DR   Bgee; Q9CRA8; -.
DR   CleanEx; MM_EXOSC5; -.
DR   Genevestigator; Q9CRA8; -.
DR   GermOnline; ENSMUSG00000061286; Mus musculus.
DR   GO; GO:0000178; C:exosome (RNase complex); IEA:UniProtKB-KW.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000175; F:3'-5'-exoribonuclease activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR001247; ExoRNase_PH_dom1.
DR   InterPro; IPR015847; ExoRNase_PH_dom2.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   Pfam; PF01138; RNase_PH; 1.
DR   Pfam; PF03725; RNase_PH_C; 1.
DR   SUPFAM; SSF55666; 3_ExoRNase; 1.
DR   SUPFAM; SSF54211; Ribosomal_S5_D2-typ_fold; 1.
PE   1: Evidence at protein level;
KW   Exonuclease; Exosome; Hydrolase; Nuclease; Nucleus; Phosphoprotein;
KW   RNA-binding; rRNA processing.
FT   CHAIN         1    235       Exosome complex exonuclease RRP46.
FT                                /FTId=PRO_0000139976.
FT   MOD_RES      20     20       Phosphoserine (By similarity).
FT   MOD_RES      27     27       Phosphoserine.
FT   CONFLICT     11     11       L -> V (in Ref. 2; AAH34358).
SQ   SEQUENCE   235 AA;  25194 MW;  08752915141CF65D CRC64;
     MEGAKRADAN LLTDTGTESS PRSPVCSLRH FACEQNLLSR PDGSASFLQG DTSVLAGVYG
     PAEVKVSKEI FNKATLEVIL RPKIGLPGVA EKSRERLVRN TCEAVVLGAL HPRTSITVVL
     QVVSDAGSLL ACCLNAACMA LVDAGVPMRA LFCGVTCALD SDGNLVLDPT TKQEKEARAI
     LTFALDSAEQ KLLMSTTKGL YSDAELQQCL AAAQAASQHI FRFYRESLQR RYSKS
//
ID   FGOP2_MOUSE             Reviewed;         253 AA.
AC   Q9CRA9; Q3TEX1; Q3TW81; Q9D7R0;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=FGFR1 oncogene partner 2 homolog;
GN   Name=Fgfr1op2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Cerebellum, Lung, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in wound healing pathway (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9CRA9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CRA9-2; Sequence=VSP_027541;
CC   -!- SIMILARITY: Belongs to the SIKE family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK004662; BAB23452.1; -; mRNA.
DR   EMBL; AK005320; BAB23951.1; -; mRNA.
DR   EMBL; AK008983; BAB26006.1; -; mRNA.
DR   EMBL; AK151318; BAE30299.1; -; mRNA.
DR   EMBL; AK152617; BAE31360.1; -; mRNA.
DR   EMBL; AK153137; BAE31749.1; -; mRNA.
DR   EMBL; AK159805; BAE35385.1; -; mRNA.
DR   EMBL; AK169380; BAE41127.1; -; mRNA.
DR   EMBL; AK169383; BAE41130.1; -; mRNA.
DR   EMBL; BC028876; AAH28876.1; -; mRNA.
DR   IPI; IPI00110657; -.
DR   IPI; IPI00133534; -.
DR   RefSeq; NP_080494.1; NM_026218.2.
DR   UniGene; Mm.333499; -.
DR   STRING; Q9CRA9; -.
DR   PhosphoSite; Q9CRA9; -.
DR   PRIDE; Q9CRA9; -.
DR   Ensembl; ENSMUST00000067404; ENSMUSP00000098352; ENSMUSG00000040242.
DR   Ensembl; ENSMUST00000111663; ENSMUSP00000107292; ENSMUSG00000040242.
DR   GeneID; 67529; -.
DR   KEGG; mmu:67529; -.
DR   UCSC; uc009esc.1; mouse.
DR   CTD; 67529; -.
DR   MGI; MGI:1914779; Fgfr1op2.
DR   eggNOG; roNOG08975; -.
DR   GeneTree; ENSGT00390000018003; -.
DR   HOGENOM; HBG445550; -.
DR   HOVERGEN; HBG055808; -.
DR   InParanoid; Q9CRA9; -.
DR   OMA; CEDEERI; -.
DR   OrthoDB; EOG4SQWXR; -.
DR   NextBio; 324831; -.
DR   ArrayExpress; Q9CRA9; -.
DR   Bgee; Q9CRA9; -.
DR   CleanEx; MM_FGFR1OP2; -.
DR   Genevestigator; Q9CRA9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR008555; DUF837.
DR   PANTHER; PTHR12186; DUF837; 1.
DR   Pfam; PF05769; DUF837; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; Coiled coil; Cytoplasm.
FT   CHAIN         1    253       FGFR1 oncogene partner 2 homolog.
FT                                /FTId=PRO_0000299042.
FT   COILED        5    104       Potential.
FT   COILED      160    223       Potential.
FT   MOD_RES       7      7       N6-acetyllysine (By similarity).
FT   VAR_SEQ     133    170       Missing (in isoform 2).
FT                                /FTId=VSP_027541.
FT   CONFLICT    108    108       M -> V (in Ref. 1; BAE35385).
FT   CONFLICT    211    211       N -> D (in Ref. 1; BAE41127).
SQ   SEQUENCE   253 AA;  29374 MW;  07A077BAB5071119 CRC64;
     MSCTIEKALA DAKALVERLR DHDDAAESLI EQTTALSKRV EAMKQYQEEI QELNEVARHR
     PRSTLVMGIQ QENRQIRELQ QENKELRTSL EEHQSALELI MSKYREQMFR LLMASKKDDP
     GIIMKLKEQH SKIDMVHRNS CEGFFLDASR HILEAPQHGL ERRHLEANQN ELQAHVDQIT
     EMAAVMRKAI EIDEQQGCKE QERIFQLEQE NKGLREILQI TRESFLNLRK DDASESTSLS
     ALVTNSDLSL RKS
//
ID   MTFP1_MOUSE             Reviewed;         166 AA.
AC   Q9CRB8; Q9CZX4;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Mitochondrial fission process protein 1;
DE   AltName: Full=Mitochondrial 18 kDa protein;
DE            Short=MTP18;
GN   Name=Mtfp1; Synonyms=Mtp18;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Liver, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 63-73, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Involved in the mitochondrial division probably by
CC       regulating membrane fission. Loss-of-function leads to apoptosis
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC       membrane protein (Potential).
CC   -!- SIMILARITY: Belongs to the MTFP1 family.
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DR   EMBL; AK006148; BAB24432.1; -; mRNA.
DR   EMBL; AK010971; BAB27300.1; -; mRNA.
DR   EMBL; AK012058; BAB27999.1; -; mRNA.
DR   EMBL; AK078381; BAC37244.1; -; mRNA.
DR   EMBL; BC058737; AAH58737.1; -; mRNA.
DR   IPI; IPI00315908; -.
DR   RefSeq; NP_080719.2; NM_026443.4.
DR   UniGene; Mm.41719; -.
DR   STRING; Q9CRB8; -.
DR   PRIDE; Q9CRB8; -.
DR   Ensembl; ENSMUST00000004868; ENSMUSP00000004868; ENSMUSG00000004748.
DR   GeneID; 67900; -.
DR   KEGG; mmu:67900; -.
DR   UCSC; uc007hug.1; mouse.
DR   CTD; 67900; -.
DR   MGI; MGI:1916686; 1700020C11Rik.
DR   GeneTree; ENSGT00390000004019; -.
DR   HOGENOM; HBG315196; -.
DR   HOVERGEN; HBG052517; -.
DR   InParanoid; Q9CRB8; -.
DR   OMA; AIPVIIH; -.
DR   OrthoDB; EOG451DRX; -.
DR   PhylomeDB; Q9CRB8; -.
DR   NextBio; 325898; -.
DR   ArrayExpress; Q9CRB8; -.
DR   Bgee; Q9CRB8; -.
DR   CleanEx; MM_1700020C11RIK; -.
DR   Genevestigator; Q9CRB8; -.
DR   GermOnline; ENSMUSG00000004748; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR   InterPro; IPR001765; Carbonic_anhydrase.
DR   InterPro; IPR019560; Mitochondrial_18_kDa_protein_.
DR   PANTHER; PTHR11002; Carbonic_anhydrase; 1.
DR   PANTHER; PTHR11002:SF2; Mitochondrial_18_kDa_protein_; 1.
DR   Pfam; PF10558; MTP18; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Direct protein sequencing; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    166       Mitochondrial fission process protein 1.
FT                                /FTId=PRO_0000212412.
FT   TRANSMEM     34     54       Helical; (Potential).
FT   TRANSMEM     78     98       Helical; (Potential).
FT   TRANSMEM    129    149       Helical; (Potential).
FT   CONFLICT    152    152       S -> N (in Ref. 1; BAB27999).
SQ   SEQUENCE   166 AA;  18314 MW;  05B2A63491EE597E CRC64;
     MSEQQRQGAE RDLYRDTWVR YLGYANEVGE AFRSLVPAAV VWLSYGVSSS YVLADAIDKG
     KKAGEVPSPE AGRNTRMALA VVDTFVWQSL ASVAIPGFTI NRLCAASLYV LGTMTHWPPT
     VRKWTTTTLG LLAIPVIIHP IDRSVDFLLD SSLRKLYPSV EKPSTP
//
ID   CHCH3_MOUSE             Reviewed;         227 AA.
AC   Q9CRB9;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Coiled-coil-helix-coiled-coil-helix domain-containing protein 3, mitochondrial;
DE   Flags: Precursor;
GN   Name=Chchd3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=C57BL/6J;
RX   PubMed=14651853; DOI=10.1016/S0092-8674(03)00926-7;
RA   Mootha V.K., Bunkenborg J., Olsen J.V., Hjerrild M., Wisniewski J.R.,
RA   Stahl E., Bolouri M.S., Ray H.N., Sihag S., Kamal M., Patterson N.,
RA   Lander E.S., Mann M.;
RT   "Integrated analysis of protein composition, tissue diversity, and
RT   gene regulation in mouse mitochondria.";
RL   Cell 115:629-640(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Contains 1 CHCH domain.
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DR   EMBL; AK002263; BAB21974.1; -; mRNA.
DR   EMBL; AK003519; BAB22832.1; -; mRNA.
DR   EMBL; BC021941; AAH21941.1; -; mRNA.
DR   IPI; IPI00133562; -.
DR   RefSeq; NP_079612.1; NM_025336.1.
DR   UniGene; Mm.21501; -.
DR   ProteinModelPortal; Q9CRB9; -.
DR   STRING; Q9CRB9; -.
DR   PhosphoSite; Q9CRB9; -.
DR   PRIDE; Q9CRB9; -.
DR   Ensembl; ENSMUST00000066379; ENSMUSP00000070149; ENSMUSG00000053768.
DR   GeneID; 66075; -.
DR   KEGG; mmu:66075; -.
DR   UCSC; uc009bgo.1; mouse.
DR   CTD; 66075; -.
DR   MGI; MGI:1913325; Chchd3.
DR   HOGENOM; HBG506924; -.
DR   HOVERGEN; HBG050936; -.
DR   InParanoid; Q9CRB9; -.
DR   OMA; SALANQY; -.
DR   OrthoDB; EOG46MBKQ; -.
DR   PhylomeDB; Q9CRB9; -.
DR   NextBio; 320556; -.
DR   ArrayExpress; Q9CRB9; -.
DR   Bgee; Q9CRB9; -.
DR   Genevestigator; Q9CRB9; -.
DR   GermOnline; ENSMUSG00000053768; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   InterPro; IPR007964; DUF737.
DR   Pfam; PF05300; DUF737; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Mitochondrion; Phosphoprotein; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    227       Coiled-coil-helix-coiled-coil-helix
FT                                domain-containing protein 3,
FT                                mitochondrial.
FT                                /FTId=PRO_0000129164.
FT   DOMAIN      176    217       CHCH.
FT   MOD_RES      49     49       Phosphotyrosine (By similarity).
FT   MOD_RES      50     50       Phosphoserine (By similarity).
FT   MOD_RES      58     58       Phosphoserine.
FT   MOD_RES     142    142       N6-acetyllysine (By similarity).
SQ   SEQUENCE   227 AA;  26335 MW;  055B1AF5A6DB808E CRC64;
     MGGTASTRRV TFEADENENI TVVKGIRLSE NVIDRMKESS PSGSKSQRYS SVYGASVSDE
     DLKRRVAEEL ALEQAKKESE HQRRLKQARD LERERAAANE QLTRAVLRER ISSEEERMKA
     KHLARQLEEK DRVMRKQDAF YKEQLARLEE RSSEFYKVTT EEYQKAAEEV EAKFKRYEYH
     PVCADLQTKI LQCYRQNTQQ TLSCSALASQ YMHCVNHAKQ SMLEKGG
//
ID   OCAD1_MOUSE             Reviewed;         247 AA.
AC   Q9CRD0; Q3TEC2; Q3TJS3; Q7TNB3; Q922M2;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=OCIA domain-containing protein 1;
GN   Name=Ociad1; Synonyms=Asrij;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6;
RX   MEDLINE=22769961; PubMed=12889067; DOI=10.1002/dvdy.10332;
RA   Mukhopadhyay A., Das D., Inamdar M.S.;
RT   "Embryonic stem cell and tissue-specific expression of a novel
RT   conserved gene, asrij.";
RL   Dev. Dyn. 227:578-586(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Brain cortex, Cecum, Corpora quadrigemina, Medulla oblongata,
RC   Pancreas, Placenta, Testis, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-131, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- SUBCELLULAR LOCATION: Endosome.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9CRD0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CRD0-2; Sequence=VSP_027623;
CC       Name=3;
CC         IsoId=Q9CRD0-3; Sequence=VSP_027624, VSP_027625;
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in the brain and at
CC       lower levels in the heart, ovary, testis and kidney. Expression is
CC       strongest in embryonic stem cells and in the blood vessels.
CC   -!- DEVELOPMENTAL STAGE: First detected at embryonic day (E) 6.5 in
CC       the primitive streak region of the epiblast and extraembryonic
CC       vasculature. Expression in the E8.5 yolk sac is seen within blood
CC       islands and the capillary plexus. As embryogenesis proceeds,
CC       expression becomes prominent in the blood islands and the
CC       primitive blood vessels of the yolk sac. By E8-8.5, a more
CC       generalized expression pattern is seen in the neural folds and
CC       caudally in the presomitic mesoderm and primitive streak regions.
CC       A definite increase in vascular expression is seen in the embryo
CC       by E9.5. Tissue-specific expression is initially seen from early
CC       E9.5 in the anterior-most regions of the head, mainly in the optic
CC       vesicle and branchial arches. At E11.5 and E13.5, strong
CC       expression is seen in the embryonic stem cells of the blood
CC       vessels, especially in the capillaries of the brain and in the
CC       hyaline vasculature of the eye. Weak expression is also seen in
CC       the lingual vessels and in the neural crest-derived regions of the
CC       jaw. A rapid increase in expression in the trunk is seen between
CC       E9.5 and E10.5 and by E13.5, expression is more localized.
CC       Expression is not detected in the embryonic heart at early E9.5
CC       and from E11.5 onward, increasing expression is seen in the
CC       atrium, ventricle, and outflow tracts of the heart.
CC   -!- MISCELLANEOUS: 'Asrij' stands for 'blood' in Sanskrit as this
CC       protein is strongly expressed in blood vessels.
CC   -!- SIMILARITY: Belongs to the OCIAD1 family.
CC   -!- SIMILARITY: Contains 1 OCIA domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE39422.1; Type=Frameshift; Positions=235;
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DR   EMBL; AF295357; AAG59858.1; -; mRNA.
DR   EMBL; AF295358; AAG59859.1; -; Genomic_DNA.
DR   EMBL; AY208935; AAP41523.1; -; mRNA.
DR   EMBL; AK006013; BAB24366.1; -; mRNA.
DR   EMBL; AK007636; BAB25152.1; -; mRNA.
DR   EMBL; AK043603; BAC31593.1; -; mRNA.
DR   EMBL; AK077904; BAC37055.1; -; mRNA.
DR   EMBL; AK078102; BAC37125.1; -; mRNA.
DR   EMBL; AK078909; BAC37453.1; -; mRNA.
DR   EMBL; AK080795; BAC38024.1; -; mRNA.
DR   EMBL; AK082769; BAC38610.1; -; mRNA.
DR   EMBL; AK082781; BAC38616.1; -; mRNA.
DR   EMBL; AK159811; BAE35391.1; -; mRNA.
DR   EMBL; AK167320; BAE39422.1; ALT_FRAME; mRNA.
DR   EMBL; AK169715; BAE41326.1; -; mRNA.
DR   EMBL; BC006937; AAH06937.1; -; mRNA.
DR   IPI; IPI00133608; -.
DR   IPI; IPI00407938; -.
DR   IPI; IPI00856842; -.
DR   RefSeq; NP_001153359.1; NM_001159887.1.
DR   RefSeq; NP_001153360.1; NM_001159888.1.
DR   RefSeq; NP_001153361.1; NM_001159889.1.
DR   RefSeq; NP_075918.1; NM_023429.4.
DR   UniGene; Mm.247039; -.
DR   ProteinModelPortal; Q9CRD0; -.
DR   STRING; Q9CRD0; -.
DR   PhosphoSite; Q9CRD0; -.
DR   PRIDE; Q9CRD0; -.
DR   Ensembl; ENSMUST00000031038; ENSMUSP00000031038; ENSMUSG00000029152.
DR   Ensembl; ENSMUST00000071081; ENSMUSP00000069412; ENSMUSG00000029152.
DR   GeneID; 68095; -.
DR   KEGG; mmu:68095; -.
DR   UCSC; uc008xsu.1; mouse.
DR   CTD; 68095; -.
DR   MGI; MGI:1915345; Ociad1.
DR   eggNOG; roNOG05815; -.
DR   GeneTree; ENSGT00530000063690; -.
DR   HOGENOM; HBG714376; -.
DR   HOVERGEN; HBG108207; -.
DR   InParanoid; Q9CRD0; -.
DR   OMA; KYDSNVS; -.
DR   OrthoDB; EOG470TJJ; -.
DR   PhylomeDB; Q9CRD0; -.
DR   NextBio; 326408; -.
DR   ArrayExpress; Q9CRD0; -.
DR   Bgee; Q9CRD0; -.
DR   CleanEx; MM_OCIAD1; -.
DR   Genevestigator; Q9CRD0; -.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   InterPro; IPR009764; OCIA.
DR   PANTHER; PTHR13336; OCIA; 1.
DR   Pfam; PF07051; OCIA; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Endosome; Phosphoprotein.
FT   CHAIN         1    247       OCIA domain-containing protein 1.
FT                                /FTId=PRO_0000299384.
FT   DOMAIN        1    112       OCIA.
FT   MOD_RES     108    108       Phosphoserine (By similarity).
FT   MOD_RES     123    123       Phosphoserine (By similarity).
FT   MOD_RES     131    131       N6-acetyllysine.
FT   MOD_RES     193    193       Phosphoserine (By similarity).
FT   VAR_SEQ     185    235       Missing (in isoform 2).
FT                                /FTId=VSP_027623.
FT   VAR_SEQ     186    189       PEPN -> RNFS (in isoform 3).
FT                                /FTId=VSP_027624.
FT   VAR_SEQ     190    247       Missing (in isoform 3).
FT                                /FTId=VSP_027625.
FT   CONFLICT    151    151       D -> G (in Ref. 2; BAE41326).
SQ   SEQUENCE   247 AA;  27610 MW;  00EDDB3D12B16853 CRC64;
     MNGRADFREP NAQVSRPIPD IGGGYIPTEE EWRLFAECHE ECFWFRSVPL AATSMLITQG
     LISKGILSSH PKYGSIPKLL FACIVGYFAG KLSYVKTCQE KFKKLENSPL GEALRSGELR
     RSSPPGHYTQ KPKFDSNVSG QSSFGTSPAA DNIEKEALPR YEPIPFSASM NESTPTGITD
     HIAQGPEPNL EESPKRKGVT YEELRSKNRE SYGVTLPHKT DPSVRPMQER VPKKEVKVNK
     YGDTWDE
//
ID   TTC35_MOUSE             Reviewed;         297 AA.
AC   Q9CRD2; Q925K1;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Tetratricopeptide repeat protein 35;
DE            Short=TPR repeat protein 35;
GN   Name=Ttc35; Synonyms=Kiaa0103;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-297.
RC   STRAIN=ISS;
RX   MEDLINE=21363810; PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [4]
RP   IDENTIFICATION, AND SUBCELLULAR LOCATION.
RX   MEDLINE=21477416; PubMed=11593002; DOI=10.1073/pnas.211201898;
RA   Dreger M., Bengtsson L., Schoeneberg T., Otto H., Hucho F.;
RT   "Nuclear envelope proteomics: novel integral membrane proteins of the
RT   inner nuclear membrane.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:11943-11948(2001).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Contains 3 TPR repeats.
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DR   EMBL; AK015968; BAB30057.1; -; mRNA.
DR   EMBL; AK014989; BAB29657.1; -; mRNA.
DR   EMBL; BC004716; AAH04716.1; -; mRNA.
DR   EMBL; AF332065; AAK56094.1; -; mRNA.
DR   IPI; IPI00133612; -.
DR   RefSeq; NP_080012.1; NM_025736.2.
DR   UniGene; Mm.244512; -.
DR   ProteinModelPortal; Q9CRD2; -.
DR   SMR; Q9CRD2; 55-286.
DR   STRING; Q9CRD2; -.
DR   PhosphoSite; Q9CRD2; -.
DR   PRIDE; Q9CRD2; -.
DR   Ensembl; ENSMUST00000022962; ENSMUSP00000022962; ENSMUSG00000022337.
DR   GeneID; 66736; -.
DR   KEGG; mmu:66736; -.
DR   UCSC; uc007vpm.1; mouse.
DR   CTD; 66736; -.
DR   MGI; MGI:1913986; Ttc35.
DR   GeneTree; ENSGT00390000011922; -.
DR   HOGENOM; HBG558758; -.
DR   HOVERGEN; HBG055231; -.
DR   InParanoid; Q9CRD2; -.
DR   OMA; ASWAANQ; -.
DR   OrthoDB; EOG41ZFBF; -.
DR   PhylomeDB; Q9CRD2; -.
DR   NextBio; 322511; -.
DR   ArrayExpress; Q9CRD2; -.
DR   Bgee; Q9CRD2; -.
DR   CleanEx; MM_TTC35; -.
DR   Genevestigator; Q9CRD2; -.
DR   GermOnline; ENSMUSG00000022337; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 2.
DR   PROSITE; PS50005; TPR; 2.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Nucleus; Repeat; TPR repeat.
FT   CHAIN         1    297       Tetratricopeptide repeat protein 35.
FT                                /FTId=PRO_0000106354.
FT   REPEAT       87    120       TPR 1.
FT   REPEAT      155    188       TPR 2.
FT   REPEAT      192    225       TPR 3.
FT   MOD_RES     255    255       N6-acetyllysine (By similarity).
SQ   SEQUENCE   297 AA;  34935 MW;  009366B7A3B5BCEA CRC64;
     MAKVTERYDV TWEEMRDKMR KWREENSRNS EQIMEVGEEL INDYASKLGD DIWIIYEQVM
     IAALDYGRDD LALFCLQELR RQFPGSHRVK RLTGMRFEAM ERYDDAIQLY DRILQEDPTN
     TAARKRKIAI RKAQGKTVEA IRELNEYLEQ FVGDQEAWHE LAELYINEHD YAKAAFCLEE
     LMMTNPHNHL YCQQYAEVKY TQGGLENLEL SRKYFAQALK LNNRNMRALF GLYMSASHIA
     SNPKASAKMK KDNIKYASWA ANQINRAYQF AGRSKKETKY SLKAVEDMLE TLQITQS
//
ID   Q9CS23_MOUSE            Unreviewed;       160 AA.
AC   Q9CS23;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   08-FEB-2011, entry version 47.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Herc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RA   Adachi J., Aizawa K., Akahira S., Akimura T., Arai A., Aono H.,
RA   Arakawa T., Bono H., Carninci P., Fukuda S., Fukunishi Y., Furuno M.,
RA   Hanagaki T., Hara A., Hayatsu N., Hiramoto K., Hiraoka T., Hori F.,
RA   Imotani K., Ishii Y., Itoh M., Izawa M., Kasukawa T., Kato H.,
RA   Kawai J., Kojima Y., Konno H., Kouda M., Koya S., Kurihara C.,
RA   Matsuyama T., Miyazaki A., Nishi K., Nomura K., Numazaki R., Ohno M.,
RA   Okazaki Y., Okido T., Owa C., Saito H., Saito R., Sakai C., Sakai K.,
RA   Sano H., Sasaki D., Shibata K., Shibata Y., Shinagawa A., Shiraki T.,
RA   Sogabe Y., Suzuki H., Tagami M., Tagawa A., Takahashi F., Tanaka T.,
RA   Tejima Y., Toya T., Yamamura T., Yasunishi A., Yoshida K., Yoshino M.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK019286; BAB31647.1; -; mRNA.
DR   IPI; IPI00676574; -.
DR   UniGene; Mm.244179; -.
DR   STRING; Q9CS23; -.
DR   PhosphoSite; Q9CS23; -.
DR   Ensembl; ENSMUST00000042824; ENSMUSP00000044801; ENSMUSG00000038664.
DR   Ensembl; ENSMUST00000098618; ENSMUSP00000096218; ENSMUSG00000038664.
DR   MGI; MGI:2384589; Herc1.
DR   GeneTree; ENSGT00590000082801; -.
DR   InParanoid; Q9CS23; -.
DR   ArrayExpress; Q9CS23; -.
DR   Bgee; Q9CS23; -.
DR   Genevestigator; Q9CS23; -.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
FT   NON_TER     160    160
SQ   SEQUENCE   160 AA;  17550 MW;  1F4F6F946D5BE46E CRC64;
     GVDAGLRVGG RCVHKQTGRH ATLLGVVKEG STSAKVQWDE AEITISDTPL YNLEPCEPLL
     FDVARFRGLT ASVLLDLTYL TGIHEDVGKQ SIKRHEKKHR HESEEKGDIE QKPESESILD
     VRTGLMSDDV KSQGTTSSKS ENEIASFSLE PTLPGVESQH
//
ID   Q9CS54_MOUSE            Unreviewed;       197 AA.
AC   Q9CS54;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   08-FEB-2011, entry version 47.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Srp72;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RA   Adachi J., Aizawa K., Akahira S., Akimura T., Arai A., Aono H.,
RA   Arakawa T., Bono H., Carninci P., Fukuda S., Fukunishi Y., Furuno M.,
RA   Hanagaki T., Hara A., Hayatsu N., Hiramoto K., Hiraoka T., Hori F.,
RA   Imotani K., Ishii Y., Itoh M., Izawa M., Kasukawa T., Kato H.,
RA   Kawai J., Kojima Y., Konno H., Kouda M., Koya S., Kurihara C.,
RA   Matsuyama T., Miyazaki A., Nishi K., Nomura K., Numazaki R., Ohno M.,
RA   Okazaki Y., Okido T., Owa C., Saito H., Saito R., Sakai C., Sakai K.,
RA   Sano H., Sasaki D., Shibata K., Shibata Y., Shinagawa A., Shiraki T.,
RA   Sogabe Y., Suzuki H., Tagami M., Tagawa A., Takahashi F., Tanaka T.,
RA   Tejima Y., Toya T., Yamamura T., Yasunishi A., Yoshida K., Yoshino M.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
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DR   EMBL; AK017869; BAB30981.1; -; mRNA.
DR   IPI; IPI00882041; -.
DR   RefSeq; NP_079967.1; NM_025691.1.
DR   UniGene; Mm.296976; -.
DR   UniGene; Mm.461699; -.
DR   STRING; Q9CS54; -.
DR   Ensembl; ENSMUST00000101087; ENSMUSP00000098648; ENSMUSG00000036323.
DR   Ensembl; ENSMUST00000120550; ENSMUSP00000113312; ENSMUSG00000036323.
DR   GeneID; 66661; -.
DR   KEGG; mmu:66661; -.
DR   CTD; 66661; -.
DR   MGI; MGI:1333795; Srp72.
DR   GeneTree; ENSGT00390000013264; -.
DR   HOVERGEN; HBG100507; -.
DR   InParanoid; Q9CS54; -.
DR   ArrayExpress; Q9CS54; -.
DR   Bgee; Q9CS54; -.
DR   Genevestigator; Q9CS54; -.
DR   GO; GO:0008312; F:7S RNA binding; IEA:InterPro.
DR   GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro.
DR   InterPro; IPR013699; Signal_recog_part_SRP72_RNA-bd.
DR   Pfam; PF08492; SRP72; 1.
PE   1: Evidence at protein level;
FT   NON_TER       1      1
SQ   SEQUENCE   197 AA;  21226 MW;  27F8169495DC6E82 CRC64;
     KQNSKDIHTL AQLISAYSLV DPEKAKALSK HLPSSDSMSL KVDVEALENS PGATYIRKKG
     GKVTGDNQSK EQGQGDLKKK KKKKKGKLPK NYDPKVTPDP ERWLPMRERS YYRGRKKGKK
     KDQIGKGTQG ATAGASSELD ASKAVSSPPT SPRPGSAATI SSSASNIVPP RHQKPAGAPA
     TKKKQQQKKK KGGKSGW
//
ID   Q9CS69_MOUSE            Unreviewed;       374 AA.
AC   Q9CS69;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   08-FEB-2011, entry version 57.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Sltm;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RA   Adachi J., Aizawa K., Akahira S., Akimura T., Arai A., Aono H.,
RA   Arakawa T., Bono H., Carninci P., Fukuda S., Fukunishi Y., Furuno M.,
RA   Hanagaki T., Hara A., Hayatsu N., Hiramoto K., Hiraoka T., Hori F.,
RA   Imotani K., Ishii Y., Itoh M., Izawa M., Kasukawa T., Kato H.,
RA   Kawai J., Kojima Y., Konno H., Kouda M., Koya S., Kurihara C.,
RA   Matsuyama T., Miyazaki A., Nishi K., Nomura K., Numazaki R., Ohno M.,
RA   Okazaki Y., Okido T., Owa C., Saito H., Saito R., Sakai C., Sakai K.,
RA   Sano H., Sasaki D., Shibata K., Shibata Y., Shinagawa A., Shiraki T.,
RA   Sogabe Y., Suzuki H., Tagami M., Tagawa A., Takahashi F., Tanaka T.,
RA   Tejima Y., Toya T., Yamamura T., Yasunishi A., Yoshida K., Yoshino M.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK017715; BAB30891.1; -; mRNA.
DR   IPI; IPI00473550; -.
DR   UniGene; Mm.22379; -.
DR   HSSP; Q61474; 2MST.
DR   ProteinModelPortal; Q9CS69; -.
DR   STRING; Q9CS69; -.
DR   PRIDE; Q9CS69; -.
DR   Ensembl; ENSMUST00000085386; ENSMUSP00000082504; ENSMUSG00000032212.
DR   MGI; MGI:1913910; Sltm.
DR   eggNOG; roNOG15007; -.
DR   GeneTree; ENSGT00590000082875; -.
DR   ArrayExpress; Q9CS69; -.
DR   Bgee; Q9CS69; -.
DR   Genevestigator; Q9CS69; -.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   2: Evidence at transcript level;
FT   NON_TER       1      1
FT   NON_TER     374    374
SQ   SEQUENCE   374 AA;  39050 MW;  B4FAF8B156267AD5 CRC64;
     SAAAAALQPT SCLGSALLSQ NGCRCRGRGS LGRLWAGGRE EDHGAAGYRP QVRAEAPQLG
     HQRGQDGTGL PAEAGKKQEA DELSGDASVE DDSFVKDGEE EENEKDIAGS GDGTQEVSKP
     LPSEGSLAEA DHTAHEEMEA NATGKEAEDD NISVTIQAED AITLDFDGDD LLETGKNVKI
     TDSEASKPKD VQDAIAQSPE KEAKDYEMNP NHKDGKKEDS VKGEPVEKEA RESAKKAESG
     DKEKDTLKKG PSSTGASGQA KSSSKESKDS KTSSKDDKGS TGSAGGSSGS STKNIWVSGL
     SSNTKAADLK NLFGKYGKVL SAKVVTNARS PGAKCYGIVT MSSSTEVSRC VAHLHRTELH
     GQLISVEKVK GDPS
//
ID   NRX1A_MOUSE             Reviewed;        1514 AA.
AC   Q9CS84; O88722; Q80Y87; Q8CHE6;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 3.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Neurexin-1-alpha;
DE   AltName: Full=Neurexin I-alpha;
DE   Flags: Precursor;
GN   Name=Nrxn1; Synonyms=Kiaa0578;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [2]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 298-437 (ISOFORMS 1; 2 AND 3/4).
RC   STRAIN=CD-1; TISSUE=Brain;
RA   Graveley B.R., Philipps D.L.;
RT   "Sequencing of the neurexin genes.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1126-1514 (ISOFORMS 1/2/3).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1463-1505 (ISOFORMS 1/2/3/4).
RC   STRAIN=C57BL/10; TISSUE=Brain;
RX   PubMed=10408888; DOI=10.1006/mcne.1999.0740;
RA   Gorecki D.C., Szklarczyk A., Lukasiuk K., Kaczmarek L., Simons J.P.;
RT   "Differential seizure-induced and developmental changes of neurexin
RT   expression.";
RL   Mol. Cell. Neurosci. 13:218-227(1999).
RN   [7]
RP   INTERACTION WITH SYTL1.
RX   MEDLINE=21139758; PubMed=11243866; DOI=10.1006/bbrc.2001.4512;
RA   Fukuda M., Mikoshiba K.;
RT   "Synaptotagmin-like protein 1-3: a novel family of C-terminal-type
RT   tandem C2 proteins.";
RL   Biochem. Biophys. Res. Commun. 281:1226-1233(2001).
RN   [8]
RP   INTERACTION WITH SYT13.
RX   MEDLINE=21092932; PubMed=11171101; DOI=10.1042/0264-6021:3540249;
RA   Fukuda M., Mikoshiba K.;
RT   "Characterization of KIAA1427 protein as an atypical synaptotagmin
RT   (Syt XIII).";
RL   Biochem. J. 354:249-257(2001).
CC   -!- FUNCTION: Neuronal cell surface protein that may be involved in
CC       cell recognition and cell adhesion. May mediate intracellular
CC       signaling.
CC   -!- SUBUNIT: The cytoplasmic C-terminal region binds to CASK, CASKIN1
CC       and APBA1. The laminin G-like domain 2 binds to NXPH1 (By
CC       similarity). Interacts with SYT13 and SYTL1.
CC   -!- INTERACTION:
CC       Q99N80:Sytl1; NbExp=1; IntAct=EBI-399696, EBI-398182;
CC       Q99N50:Sytl2; NbExp=1; IntAct=EBI-399696, EBI-398197;
CC       Q99N48:Sytl3; NbExp=1; IntAct=EBI-399696, EBI-398260;
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1;
CC         IsoId=Q9CS84-1; Sequence=Displayed;
CC       Name=2; Synonyms=Alpha-2B;
CC         IsoId=Q9CS84-2; Sequence=VSP_003484;
CC       Name=3; Synonyms=Alpha-2C;
CC         IsoId=Q9CS84-3; Sequence=VSP_003485;
CC       Name=4;
CC         IsoId=Q9CS84-4; Sequence=VSP_016400, VSP_003485, VSP_016401;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the neurexin family.
CC   -!- SIMILARITY: Contains 3 EGF-like domains.
CC   -!- SIMILARITY: Contains 6 laminin G-like domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC41433.2; Type=Erroneous initiation;
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DR   EMBL; AB093249; BAC41433.2; ALT_INIT; mRNA.
DR   EMBL; BC047146; AAH47146.1; -; mRNA.
DR   EMBL; AF387674; AAK70469.1; -; Genomic_DNA.
DR   EMBL; AF387674; AAK70470.1; -; Genomic_DNA.
DR   EMBL; AF387674; AAK70471.1; -; Genomic_DNA.
DR   EMBL; AK017578; BAB30815.1; -; mRNA.
DR   EMBL; AJ006802; CAA07257.1; -; mRNA.
DR   IPI; IPI00230050; -.
DR   IPI; IPI00230051; -.
DR   IPI; IPI00403860; -.
DR   IPI; IPI00468539; -.
DR   RefSeq; NP_064648.3; NM_020252.3.
DR   RefSeq; NP_796258.2; NM_177284.2.
DR   UniGene; Mm.480021; -.
DR   PDB; 3BOD; X-ray; 1.70 A; A=1132-1334.
DR   PDB; 3MW2; X-ray; 2.69 A; A/B=1132-1334.
DR   PDBsum; 3BOD; -.
DR   PDBsum; 3MW2; -.
DR   ProteinModelPortal; Q9CS84; -.
DR   SMR; Q9CS84; 221-258, 279-475, 489-906, 913-1074, 1093-1127, 1130-1334.
DR   IntAct; Q9CS84; 10.
DR   STRING; Q9CS84; -.
DR   PhosphoSite; Q9CS84; -.
DR   PRIDE; Q9CS84; -.
DR   Ensembl; ENSMUST00000054059; ENSMUSP00000057294; ENSMUSG00000024109.
DR   GeneID; 18189; -.
DR   KEGG; mmu:18189; -.
DR   UCSC; uc008dvy.1; mouse.
DR   UCSC; uc008dvz.1; mouse.
DR   CTD; 18189; -.
DR   MGI; MGI:1096391; Nrxn1.
DR   eggNOG; roNOG14987; -.
DR   GeneTree; ENSGT00560000076996; -.
DR   HOGENOM; HBG358378; -.
DR   HOVERGEN; HBG052670; -.
DR   InParanoid; Q9CS84; -.
DR   OMA; GDQGKSK; -.
DR   OrthoDB; EOG41G339; -.
DR   NextBio; 293528; -.
DR   ArrayExpress; Q9CS84; -.
DR   Bgee; Q9CS84; -.
DR   CleanEx; MM_NRXN1; -.
DR   Genevestigator; Q9CS84; -.
DR   GermOnline; ENSMUSG00000024109; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; TAS:MGI.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:MGI.
DR   GO; GO:0005246; F:calcium channel regulator activity; IGI:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007269; P:neurotransmitter secretion; IGI:MGI.
DR   GO; GO:0007416; P:synapse assembly; IGI:MGI.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR012680; Laminin_G_2.
DR   InterPro; IPR003585; Neurexin-like.
DR   Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 6.
DR   Pfam; PF02210; Laminin_G_2; 6.
DR   SMART; SM00294; 4.1m; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00282; LamG; 6.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 6.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; FALSE_NEG.
DR   PROSITE; PS01186; EGF_2; FALSE_NEG.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 6.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Cell adhesion;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW   Metal-binding; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     30       Potential.
FT   CHAIN        31   1514       Neurexin-1-alpha.
FT                                /FTId=PRO_0000043164.
FT   TOPO_DOM     31   1438       Extracellular (Potential).
FT   TRANSMEM   1439   1459       Helical; (Potential).
FT   TOPO_DOM   1460   1514       Cytoplasmic (Potential).
FT   DOMAIN       31    217       Laminin G-like 1.
FT   DOMAIN      219    256       EGF-like 1.
FT   DOMAIN      283    480       Laminin G-like 2.
FT   DOMAIN      487    679       Laminin G-like 3.
FT   DOMAIN      683    720       EGF-like 2.
FT   DOMAIN      725    898       Laminin G-like 4.
FT   DOMAIN      912   1087       Laminin G-like 5.
FT   DOMAIN     1090   1127       EGF-like 3.
FT   DOMAIN     1133   1331       Laminin G-like 6.
FT   COMPBIAS     13     21       Poly-Leu.
FT   COMPBIAS   1361   1364       Poly-Thr.
FT   COMPBIAS   1446   1449       Poly-Ala.
FT   METAL       329    329       Calcium (By similarity).
FT   METAL       346    346       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       414    414       Calcium; via carbonyl oxygen (By
FT                                similarity).
FT   CARBOHYD    125    125       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    190    190       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    797    797       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1230   1230       N-linked (GlcNAc...) (Potential).
FT   DISULFID    228    243       By similarity.
FT   DISULFID    245    255       By similarity.
FT   DISULFID    444    480       By similarity.
FT   DISULFID    650    679       By similarity.
FT   DISULFID    687    698       By similarity.
FT   DISULFID    692    707       By similarity.
FT   DISULFID    709    719       By similarity.
FT   DISULFID   1059   1087       By similarity.
FT   DISULFID   1094   1105       By similarity.
FT   DISULFID   1099   1114       By similarity.
FT   DISULFID   1116   1126       By similarity.
FT   VAR_SEQ       1    320       Missing (in isoform 4).
FT                                /FTId=VSP_016400.
FT   VAR_SEQ     379    393       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_003485.
FT   VAR_SEQ     387    393       Missing (in isoform 2).
FT                                /FTId=VSP_003484.
FT   VAR_SEQ    1410   1412       Missing (in isoform 4).
FT                                /FTId=VSP_016401.
FT   STRAND     1133   1135
FT   STRAND     1142   1145
FT   STRAND     1154   1161
FT   STRAND     1168   1177
FT   STRAND     1184   1189
FT   STRAND     1197   1199
FT   STRAND     1222   1226
FT   STRAND     1231   1235
FT   STRAND     1241   1243
FT   STRAND     1286   1291
FT   HELIX      1314   1319
FT   STRAND     1325   1327
FT   STRAND     1331   1333
SQ   SEQUENCE   1514 AA;  166169 MW;  412281FE441F0EFC CRC64;
     MGTALVQRGG CCLLCLSLLL LGCWAELGSG LEFPGAEGQW TRFPKWNACC ESEMSFQLKT
     RSARGLVLYF DDEGFCDFLE LILTRGGRLQ LSFSIFCAEP ATLLADTPVN DGAWHSVRIR
     RQFRNTTLYI DRAEAKWVEV KSKRRDMTVF SGLFVGGLPP ELRAAALKLT LASVREREPF
     KGWIRDVRVN SSQALPVDGG EVKLDDEPPN SGGGSPCEAG EEGEGGVCLN GGVCSVVDDQ
     AVCDCSRTGF RGKDCSQEDN NVEGLAHLMM GDQGKSKGKE EYIATFKGSE YFCYDLSQNP
     IQSSSDEITL SFKTLQRNGL MLHTGKSADY VNLALKNGAV SLVINLGSGA FEALVEPVNG
     KFNDNAWHDV KVTRNLRQHS GIGHAMVNKL HCSVTISVDG ILTTTGYTQE DYTMLGSDDF
     FYVGGSPSTA DLPGSPVSNN FMGCLKEVVY KNNDVRLELS RLAKQGDPKM KIHGVVAFKC
     ENVATLDPIT FETPESFISL PKWNAKKTGS ISFDFRTTEP NGLILFSHGK PRHQKDAKHP
     QMIKVDFFAI EMLDGHLYLL LDMGSGTIKI KALQKKVNDG EWYHVDFQRD GRSGTISVNT
     LRTPYTAPGE SEILDLDDEL YLGGLPENKA GLVFPTEVWT ALLNYGYVGC IRDLFIDGQS
     KDIRQMAEIQ STAGVKPSCS KETAKPCLSN PCKNNGMCRD GWNRYVCDCS GTGYLGRSCE
     REATVLSYDG SMFMKIQLPV VMHTEAEDVS LRFRSQRAYG ILMATTSRDS ADTLRLELDA
     GRVKLTVNLD CIRINCNSSK GPETLFAGYN LNDNEWHTVR VVRRGKSLKL TVDDQQAMTG
     QMAGDHTRLE FHNIETGIIT ERRYLSSVPS NFIGHLQSLT FNGMAYIDLC KNGDIDYCEL
     NARFGFRNII ADPVTFKTKS SYVALATLQA YTSMHLFFQF KTTSLDGLIL YNSGDGNDFI
     VVELVKGYLH YVFDLGNGAN LIKGSSNKPL NDNQWHNVMI SRDTSNLHTV KIDTKITTQI
     TAGARNLDLK SDLYIGGVAK ETYKSLPKLV HAKEGFQGCL ASVDLNGRLP DLISDALFCN
     GQIERGCEGP STTCQEDSCS NQGVCLQQWD GFSCDCSMTS FSGPLCNDPG TTYIFSKGGG
     QITYKWPPND RPSTRADRLA IGFSTVQKEA VLVRVDSSSG LGDYLELHIH QGKIGVKFNV
     GTDDIAIEES NAIINDGKYH VVRFTRSGGN ATLQVDSWPV IERYPAGNND NERLAIARQR
     IPYRLGRVVD EWLLDKGRQL TIFNSQATII IGGKEQGQPF QGQLSGLYYN GLKVLNMAAE
     NDANIAIVGN VRLVGEVPSS MTTESTATAM QSEMSTSIME TTTTLATSTA RRGKPPTKEP
     ISQTTDDILV ASAECPSDDE DIDPCEPSSG GLANPTRVGG REPYPGSAEV IRESSSTTGM
     VVGIVAAAAL CILILLYAMY KYRNRDEGSY HVDESRNYIS NSAQSNGAVV KEKQPSSAKS
     ANKNKKNKDK EYYV
//
ID   PAR3L_MOUSE             Reviewed;        1203 AA.
AC   Q9CSB4; Q5SV53;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Partitioning defective 3 homolog B;
DE   AltName: Full=Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 19 protein homolog;
DE   AltName: Full=PAR3-beta;
DE   AltName: Full=Partitioning defective 3-like protein;
DE            Short=PAR3-L protein;
GN   Name=Pard3b; Synonyms=Als2cr19, Par3l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-213 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-368; SER-730; SER-746
RP   AND SER-749, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-990, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   STRUCTURE BY NMR OF 478-591.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of PDZ domain in protein XP_110852.";
RL   Submitted (NOV-2004) to the PDB data bank.
CC   -!- FUNCTION: Putative adapter protein involved in asymmetrical cell
CC       division and cell polarization processes. May play a role in the
CC       formation of epithelial tight junctions (By similarity).
CC   -!- SUBUNIT: Interacts with PARD6B. Interacts with INSC/inscuteable
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endomembrane system (By similarity). Cell
CC       junction (By similarity). Cell junction, tight junction (By
CC       similarity). Note=Partially localized along the cell-cell contact
CC       region. Colocalizes with TJP1 to epithelial tight junctions (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9CSB4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CSB4-2; Sequence=VSP_022017;
CC         Note=Sequence incomplete. No experimental confirmation
CC         available;
CC   -!- SIMILARITY: Belongs to the PAR3 family.
CC   -!- SIMILARITY: Contains 3 PDZ (DHR) domains.
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DR   EMBL; AL645727; CAI24504.1; -; Genomic_DNA.
DR   EMBL; AL662815; CAI24504.1; JOINED; Genomic_DNA.
DR   EMBL; AL645669; CAI24504.1; JOINED; Genomic_DNA.
DR   EMBL; AL645544; CAI24504.1; JOINED; Genomic_DNA.
DR   EMBL; AL662920; CAI24504.1; JOINED; Genomic_DNA.
DR   EMBL; AL645669; CAI24824.1; -; Genomic_DNA.
DR   EMBL; AL662920; CAI24824.1; JOINED; Genomic_DNA.
DR   EMBL; AL662815; CAI24824.1; JOINED; Genomic_DNA.
DR   EMBL; AL645727; CAI24824.1; JOINED; Genomic_DNA.
DR   EMBL; AL645544; CAI24824.1; JOINED; Genomic_DNA.
DR   EMBL; AL645544; CAI25199.1; -; Genomic_DNA.
DR   EMBL; AL645669; CAI25199.1; JOINED; Genomic_DNA.
DR   EMBL; AL645727; CAI25199.1; JOINED; Genomic_DNA.
DR   EMBL; AL662815; CAI25199.1; JOINED; Genomic_DNA.
DR   EMBL; AL662920; CAI25199.1; JOINED; Genomic_DNA.
DR   EMBL; AL662815; CAI25349.1; -; Genomic_DNA.
DR   EMBL; AL645544; CAI25349.1; JOINED; Genomic_DNA.
DR   EMBL; AL645669; CAI25349.1; JOINED; Genomic_DNA.
DR   EMBL; AL645727; CAI25349.1; JOINED; Genomic_DNA.
DR   EMBL; AL662920; CAI25349.1; JOINED; Genomic_DNA.
DR   EMBL; AL662920; CAI26112.1; -; Genomic_DNA.
DR   EMBL; AL645544; CAI26112.1; JOINED; Genomic_DNA.
DR   EMBL; AL645669; CAI26112.1; JOINED; Genomic_DNA.
DR   EMBL; AL645727; CAI26112.1; JOINED; Genomic_DNA.
DR   EMBL; AL662815; CAI26112.1; JOINED; Genomic_DNA.
DR   EMBL; AK013352; BAB28805.1; -; mRNA.
DR   IPI; IPI00515652; -.
DR   IPI; IPI00817028; -.
DR   RefSeq; NP_001074519.2; NM_001081050.2.
DR   UniGene; Mm.35153; -.
DR   UniGene; Mm.441881; -.
DR   PDB; 1WG6; NMR; -; A=478-591.
DR   PDBsum; 1WG6; -.
DR   ProteinModelPortal; Q9CSB4; -.
DR   SMR; Q9CSB4; 2-83, 199-288, 377-591.
DR   STRING; Q9CSB4; -.
DR   PhosphoSite; Q9CSB4; -.
DR   PRIDE; Q9CSB4; -.
DR   Ensembl; ENSMUST00000075374; ENSMUSP00000074837; ENSMUSG00000052062.
DR   GeneID; 72823; -.
DR   KEGG; mmu:72823; -.
DR   CTD; 72823; -.
DR   MGI; MGI:1919301; Pard3b.
DR   GeneTree; ENSGT00590000082971; -.
DR   HOGENOM; HBG715081; -.
DR   HOVERGEN; HBG053508; -.
DR   InParanoid; Q9CSB4; -.
DR   OMA; KIHHLEY; -.
DR   OrthoDB; EOG4VDPZB; -.
DR   PhylomeDB; Q9CSB4; -.
DR   NextBio; 336989; -.
DR   ArrayExpress; Q9CSB4; -.
DR   Bgee; Q9CSB4; -.
DR   Genevestigator; Q9CSB4; -.
DR   GermOnline; ENSMUSG00000052062; Mus musculus.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   InterPro; IPR021922; DUF3534.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF12053; DUF3534; 1.
DR   Pfam; PF00595; PDZ; 2.
DR   SMART; SM00228; PDZ; 3.
DR   SUPFAM; SSF50156; PDZ; 3.
DR   PROSITE; PS50106; PDZ; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell cycle; Cell division;
KW   Cell junction; Membrane; Phosphoprotein; Repeat; Tight junction.
FT   CHAIN         1   1203       Partitioning defective 3 homolog B.
FT                                /FTId=PRO_0000185073.
FT   DOMAIN      201    289       PDZ 1.
FT   DOMAIN      383    468       PDZ 2.
FT   DOMAIN      496    585       PDZ 3.
FT   COMPBIAS   1109   1162       Pro-rich.
FT   MOD_RES     368    368       Phosphoserine.
FT   MOD_RES     730    730       Phosphoserine.
FT   MOD_RES     746    746       Phosphoserine.
FT   MOD_RES     749    749       Phosphoserine.
FT   MOD_RES     990    990       Phosphoserine.
FT   MOD_RES     998    998       Phosphotyrosine (By similarity).
FT   VAR_SEQ     169    213       DSTQNVENKEAMNGEQAGLLSLHRPKDELSDMTRAVEISGE
FT                                GDPL -> RTLIGNSSSGEFSALFWLLWALHSCAWINTHSK
FT                                HITENKIKTFKD (in isoform 2).
FT                                /FTId=VSP_022017.
FT   STRAND      493    499
FT   STRAND      512    514
FT   STRAND      527    531
FT   HELIX       538    540
FT   STRAND      549    553
FT   HELIX       563    576
FT   STRAND      584    590
SQ   SEQUENCE   1203 AA;  132780 MW;  7A9D63ED45BD3109 CRC64;
     MKVTVCFGRT GIVVPCKDGQ LRVRELTQQA LQRYLKTRDQ DPGYWVKIHH LEYTDGGILD
     PDDVLADVVE DKDKLIAVFD EQEPLQKTES PGGNPADRQS PDAFETEVAA QLAAFKPVGG
     EIVVTPSALK LGTPLLVRRS SDPAPGPHAD AQPSTASLSG QSLKPVVLDS TQNVENKEAM
     NGEQAGLLSL HRPKDELSDM TRAVEISGEG DPLGIHVVPF FSSLSGRILG LFIRGIEENS
     RCKQEGLFQE NECIVKINNV ELLDKTFAQA QDVFRQAMKS PSVILHVLLP QNREQYEKSV
     IGPLNIFGNN DGASRTKAAP PARGKPGLKA VHLTRASSPE GEEPASPQQS KSPRVPRLGR
     KPSSPSLSPL MGFGSKKNAK KIKIDLKKGP EGLGFTVVTR DSSIHGPGPI FVKNILPKGA
     AVKDGRLQSG DRILEVNGRD VTGRTQEELV AMLRSTKQGE TVSLVIARQE GSFLPRELKG
     EPDCYALSLE SSEQLTLEIP LNDSGSAGLG VSLKGNKSRE TGTDLGIFIK SIIHGGAAFK
     DGRLRMNDQL IAVNGETLLG KSNHEAMETL RRSMSMEGNI RGMIQLVILR RPERPLEELS
     ECGALSRPGF ENCQEALSTS RRNDSSILYP FGTYSPQDKR KDLLLPSDGW AENEVPPSPP
     PHPALEWGLE DFSHSSGVDS TGYFPDQHVN FRTVTPVRQP ELINLKASKS MDLVPDEGKV
     QSLADRRSDS PGKDFGPTLG LKKSSSLESL QTAVAEVRKN DLPFHRPRPH MVRGRGCNES
     FRAAIDKSYD GPEEADADGL SDKSSRSGHT ALNCESAPQG NPELDNVENK AKNIKKTKEK
     EKKKGKGKLK VKEKKLKEEH EDAERKMKRK GFGAMLRFGK KKDDKVGKAE QKGAQKSGHP
     EEEELERMKE ERERIGAKHQ ELREKQARGL VDYATAVTGP VHDMDDDEMD PNYARVNHFR
     EPCASANVFR SPSPLRAGPL AYPRDGRPLS PDHLEGLYAK VNKPYHPPAL ADSGRPMAGT
     TDRIQKLRKE YYQARREGFL LYEDENTRAR PSDHDLRWVS GKGPDGSTHN LRFEGMERQY
     ASLPRGGSAD PVDYLTASPR GRYNDRELPY YPGPHPVHAP RGSYPRPPDL RATDLRYPQY
     YPPPPAHQHK GPFRQDVPPS PPQHQRVPVY QEMGRAGPRG SSPDQYPYRN QDPRQKNPMT
     AAV
//
ID   SNW1_MOUSE              Reviewed;         536 AA.
AC   Q9CSN1;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 3.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=SNW domain-containing protein 1;
DE   AltName: Full=Nuclear protein SkiP;
DE   AltName: Full=Ski-interacting protein;
GN   Name=Snw1; Synonyms=Skiip;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-232, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-232, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   INTERACTION WITH ATP1B4.
RX   PubMed=17592128; DOI=10.1073/pnas.0704809104;
RA   Pestov N.B., Ahmad N., Korneenko T.V., Zhao H., Radkov R., Schaer D.,
RA   Roy S., Bibert S., Geering K., Modyanov N.N.;
RT   "Evolution of Na,K-ATPase betam-subunit into a coregulator of
RT   transcription in placental mammals.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:11215-11220(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224 AND SER-232, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Involved in vitamin D-mediated transcription. Can
CC       function as a splicing factor in pre-mRNA splicing (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with the SKI oncogene and with CHES1/FOXN3.
CC       Identified in the spliceosome C complex, at least composed of AQR,
CC       ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48,
CC       DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRPA1,
CC       HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK, HNRPM, HNRPR,
CC       HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1,
CC       PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6,
CC       PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3,
CC       SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2,
CC       SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2,
CC       SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8. Also
CC       associates with non-spliceosomal proteins (By similarity).
CC       Interacts with ATP1B4.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the SNW family.
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DR   EMBL; AK012384; BAB28203.2; -; mRNA.
DR   EMBL; BY734581; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00317298; -.
DR   RefSeq; NP_079783.2; NM_025507.2.
DR   UniGene; Mm.271174; -.
DR   MINT; MINT-1346847; -.
DR   STRING; Q9CSN1; -.
DR   PhosphoSite; Q9CSN1; -.
DR   PRIDE; Q9CSN1; -.
DR   Ensembl; ENSMUST00000021428; ENSMUSP00000021428; ENSMUSG00000021039.
DR   GeneID; 66354; -.
DR   KEGG; mmu:66354; -.
DR   UCSC; uc007ojf.1; mouse.
DR   CTD; 66354; -.
DR   MGI; MGI:1913604; Snw1.
DR   HOGENOM; HBG627562; -.
DR   HOVERGEN; HBG047516; -.
DR   InParanoid; Q9CSN1; -.
DR   OrthoDB; EOG4RBQJG; -.
DR   PhylomeDB; Q9CSN1; -.
DR   ArrayExpress; Q9CSN1; -.
DR   Bgee; Q9CSN1; -.
DR   CleanEx; MM_SNW1; -.
DR   Genevestigator; Q9CSN1; -.
DR   GermOnline; ENSMUSG00000021039; Mus musculus.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   InterPro; IPR017862; SKI-int_prot_SKIP.
DR   InterPro; IPR004015; SKI-int_prot_SKIP_SNW-dom.
DR   PANTHER; PTHR12096; SKIP_SNW; 1.
DR   Pfam; PF02731; SKIP_SNW; 1.
PE   1: Evidence at protein level;
KW   Acetylation; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Spliceosome.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    536       SNW domain-containing protein 1.
FT                                /FTId=PRO_0000084828.
FT   REGION      174    339       SNW.
FT   COMPBIAS    219    233       Pro-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     115    115       N6-acetyllysine (By similarity).
FT   MOD_RES     224    224       Phosphoserine.
FT   MOD_RES     232    232       Phosphoserine.
FT   MOD_RES     234    234       Phosphoserine (By similarity).
SQ   SEQUENCE   536 AA;  61475 MW;  1B5D050105BC6AAC CRC64;
     MALTSFLPAP TQLSQDQLEA EERARSQRSL QTSLVSSRRE PPPYGYRKGW IPRLLEDFGD
     GGAFPEIHVA QYPLDMGRKK KMSNALAIQV DPEGKIKYDA IARQGQSKDK VIYSKYTDLV
     PKEVMNADDP DLQRPDEEAI KEITEKTRVA LEKSVSQKVA AAMPVRAADK LAPAQYIRYT
     PSQQGVAFNS GAKQRVIRMV EMQKEPMEPP RFKINKKIPR GPPSPPAPVM HSPSRKMTVK
     EQQEWKIPPC ISNWKNAKGY TIPIDKRLAA DGRGLQTVHI NENFAKLAEA LYIADRKARE
     AVEMRAQVER KMAQKEKEKH EEKLREMAQK ARERRAGIKT HVEKEDGEAR ERDEIRHDRR
     KERQHDRNLS RAAPDKRSKL QRNENRDISE VIALGVPNPR TSNEVQYDQR LFNQSKGMDS
     GFAGGEDEIY NVYDQAWRGG KDMAQSIYRP SKNLDKDMYG DDLEARIKTN RFVPDKEFSG
     SDRKQRGREG PVQFEEDPFG LDKFLEEAKQ HGGSKRPSDS SRPKEHEHEG KKRRKE
//
ID   RANB3_MOUSE             Reviewed;         491 AA.
AC   Q9CT10; A6H6I9; Q3TIS4; Q3U2G4; Q3UYG7;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Ran-binding protein 3;
DE            Short=RanBP3;
GN   Name=Ranbp3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Liver, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-33; SER-40;
RP   TYR-47 AND SER-148, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Acts as a cofactor for XPO1/CRM1-mediated nuclear
CC       export, perhaps as export complex scaffolding protein. Bound to
CC       XPO1/CRM1, stabilizes the XPO1/CRM1-cargo interaction. In the
CC       absence of Ran-bound GTP prevents binding of XPO1/CRM1 to the
CC       nuclear pore complex. Binds to CHC1/RCC1 and increases the guanine
CC       nucleotide exchange activity of CHC1/RCC1. Recruits XPO1/CRM1 to
CC       CHC1/RCC1 in a Ran-dependent manner. Negative regulator of TGF-
CC       beta signaling through interaction with the R-SMAD proteins, SMAD2
CC       and SMAD3, and mediating their nuclear export (By similarity).
CC   -!- SUBUNIT: Interacts with CHC1 in a Ran-stimulated manner. Interacts
CC       with XPO1. Interacts (via its C-terminal R domain) with SMAD2
CC       (dephosphorylated form via its MH1 and MH2 domains); the
CC       interaction results in the nuclear export of SMAD2 and termination
CC       of the TGF-beta signaling. Interacts (via its C-terminal R domain)
CC       with SMAD3 (dephosphorylated form via its MH1 domain); the
CC       interaction results in the nuclear export of SMAD3 and termination
CC       of the TGF-beta signaling (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 RanBD1 domain.
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DR   EMBL; AK011541; BAB27684.1; -; mRNA.
DR   EMBL; AK133949; BAE21946.1; -; mRNA.
DR   EMBL; AK134696; BAE22245.1; -; mRNA.
DR   EMBL; AK155301; BAE33176.1; -; mRNA.
DR   EMBL; AK167731; BAE39772.1; -; mRNA.
DR   EMBL; BC145892; AAI45893.1; -; mRNA.
DR   EMBL; BC145894; AAI45895.1; -; mRNA.
DR   IPI; IPI00135190; -.
DR   RefSeq; NP_082209.1; NM_027933.2.
DR   UniGene; Mm.29608; -.
DR   ProteinModelPortal; Q9CT10; -.
DR   SMR; Q9CT10; 301-440.
DR   STRING; Q9CT10; -.
DR   PhosphoSite; Q9CT10; -.
DR   PRIDE; Q9CT10; -.
DR   Ensembl; ENSMUST00000002445; ENSMUSP00000002445; ENSMUSG00000002372.
DR   GeneID; 71810; -.
DR   KEGG; mmu:71810; -.
DR   UCSC; uc008dcv.1; mouse.
DR   CTD; 71810; -.
DR   MGI; MGI:1919060; Ranbp3.
DR   eggNOG; roNOG04363; -.
DR   GeneTree; ENSGT00530000063644; -.
DR   HOGENOM; HBG446070; -.
DR   HOVERGEN; HBG061383; -.
DR   InParanoid; Q9CT10; -.
DR   OMA; EAKMPAP; -.
DR   OrthoDB; EOG4XSKQ3; -.
DR   NextBio; 334576; -.
DR   ArrayExpress; Q9CT10; -.
DR   Bgee; Q9CT10; -.
DR   CleanEx; MM_RANBP3; -.
DR   Genevestigator; Q9CT10; -.
DR   GermOnline; ENSMUSG00000002372; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046907; P:intracellular transport; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR000156; RanBP.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00638; Ran_BP1; 1.
DR   SMART; SM00160; RanBD; 1.
DR   PROSITE; PS50196; RANBD1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Nucleus; Phosphoprotein; Protein transport;
KW   Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    491       Ran-binding protein 3.
FT                                /FTId=PRO_0000097167.
FT   DOMAIN      302    442       RanBD1.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      21     21       N6-acetyllysine (By similarity).
FT   MOD_RES      28     28       Phosphoserine (By similarity).
FT   MOD_RES      32     32       Phosphoserine.
FT   MOD_RES      33     33       Phosphoserine.
FT   MOD_RES      40     40       Phosphoserine.
FT   MOD_RES      47     47       Phosphotyrosine.
FT   MOD_RES      56     56       Phosphothreonine (By similarity).
FT   MOD_RES      57     57       Phosphoserine (By similarity).
FT   MOD_RES      58     58       Phosphoserine (By similarity).
FT   MOD_RES     138    138       Phosphoserine (By similarity).
FT   MOD_RES     146    146       Phosphoserine.
FT   MOD_RES     148    148       Phosphoserine.
FT   MOD_RES     257    257       Phosphoserine (By similarity).
FT   MOD_RES     277    277       Phosphoserine (By similarity).
FT   MOD_RES     279    279       Phosphoserine (By similarity).
FT   MOD_RES     281    281       Phosphoserine (By similarity).
FT   MOD_RES     283    283       Phosphoserine (By similarity).
FT   MOD_RES     463    463       Phosphoserine (By similarity).
FT   CONFLICT    259    259       P -> T (in Ref. 1; BAE39772).
FT   CONFLICT    293    293       L -> P (in Ref. 1; BAB27684).
FT   CONFLICT    317    317       T -> K (in Ref. 1; BAB27684).
FT   CONFLICT    472    472       S -> P (in Ref. 1; BAB27684).
SQ   SEQUENCE   491 AA;  52573 MW;  6BEFB98D5B0B38B7 CRC64;
     MADLANEEKP AVAPSVFVFQ KDKGQKRSAG SSSPEAGEDS DHEDGNYCPP VKRERTSSLT
     HSEEKSSGFR LKPPTLIHGQ APSAGLPSQK PREQQRGVLR PAVLQAPQPK VLSQTVPSSG
     TNGVSMPADC TGPATSVSPE NLTQRSPSES AEETHTLEEK VPQKTPHGTS EEGHCEEEQA
     APQAFVFGQN LRDRVKLMNE NASVADVDSA AHPSSETPSA TNYFLQYISS SADNATHSAD
     NSTKFVFGQN MSERVLSPPK LNEANSDTSR ETTHAQSGSE SSSQEAAPKK ESLAESAAAY
     TKATAWTCLL EKVEVITGEE AESNVLQIQC KLFVFDKTSQ SWVERGRGLL RLNDMASTDD
     GTLQSRLVMR TQGSLRLILN TKLWAQMQMD KASEKSIRIT ATDAEDQGVK VFLISASSKD
     TGQLYAALHH RILALRSRAE QEQEAKAPPP EPGATRATEE EDSDEDAVLA PSGVTGAGTG
     DEGDGQAPGS T
//
ID   LHPL3_MOUSE             Reviewed;         222 AA.
AC   Q9CTN8;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   08-MAR-2011, entry version 51.
DE   RecName: Full=Lipoma HMGIC fusion partner-like 3 protein;
GN   Name=Lhfpl3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-222.
RC   STRAIN=C57BL/6J; TISSUE=Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the LHFP family.
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DR   EMBL; AK020916; BAB32253.1; -; mRNA.
DR   RefSeq; NP_084266.1; NM_029990.1.
DR   UniGene; Mm.371712; -.
DR   UniGene; Mm.468581; -.
DR   STRING; Q9CTN8; -.
DR   PRIDE; Q9CTN8; -.
DR   Ensembl; ENSMUST00000115141; ENSMUSP00000110794; ENSMUSG00000058361.
DR   GeneID; 269629; -.
DR   KEGG; mmu:269629; -.
DR   UCSC; uc008wpu.1; mouse.
DR   CTD; 269629; -.
DR   MGI; MGI:1925076; Lhfpl3.
DR   eggNOG; roNOG12502; -.
DR   GeneTree; ENSGT00550000074479; -.
DR   HOGENOM; HBG443761; -.
DR   HOVERGEN; HBG056723; -.
DR   InParanoid; Q9CTN8; -.
DR   OrthoDB; EOG4NS3CH; -.
DR   ArrayExpress; Q9CTN8; -.
DR   Bgee; Q9CTN8; -.
DR   CleanEx; MM_LHFPL3; -.
DR   Genevestigator; Q9CTN8; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR019372; Lipome_HGMIC_fus_partner-like.
DR   Pfam; PF10242; L_HGMIC_fpl; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    222       Lipoma HMGIC fusion partner-like 3
FT                                protein.
FT                                /FTId=PRO_0000244767.
FT   TRANSMEM     22     42       Helical; (Potential).
FT   TRANSMEM     96    116       Helical; (Potential).
FT   TRANSMEM    126    146       Helical; (Potential).
FT   TRANSMEM    177    197       Helical; (Potential).
SQ   SEQUENCE   222 AA;  24686 MW;  1F8BEECF56457B39 CRC64;
     MLPAQEAAKL YHTNYVRNSR AIGVLWAIFT ICFAIINVVC FIQPYWIGDG VDTPQAGYFG
     LFHYCIGNGF SRELTCRGSF TDFSTLPSGA FKAASFFIGL SMMLIIACIV CFTLFFFCNT
     ATVYKICAWM QLTFAACLVL GCMIFPDGWD SDEAKRMCGE KTDKYTLGAC SVRWAYILAI
     IGILDALILS FLAVVLGNRQ DSLMAEELKA ENKVLLSQYS LE
//
ID   Q9CV53_MOUSE            Unreviewed;        99 AA.
AC   Q9CV53;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   SubName: Full=Putative uncharacterized protein;
DE   Flags: Fragment;
GN   Name=Gcsh;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RA   Adachi J., Aizawa K., Akahira S., Akimura T., Arai A., Aono H.,
RA   Arakawa T., Bono H., Carninci P., Fukuda S., Fukunishi Y., Furuno M.,
RA   Hanagaki T., Hara A., Hayatsu N., Hiramoto K., Hiraoka T., Hori F.,
RA   Imotani K., Ishii Y., Itoh M., Izawa M., Kasukawa T., Kato H.,
RA   Kawai J., Kojima Y., Konno H., Kouda M., Koya S., Kurihara C.,
RA   Matsuyama T., Miyazaki A., Nishi K., Nomura K., Numazaki R., Ohno M.,
RA   Okazaki Y., Okido T., Owa C., Saito H., Saito R., Sakai C., Sakai K.,
RA   Sano H., Sasaki D., Shibata K., Shibata Y., Shinagawa A., Shiraki T.,
RA   Sogabe Y., Suzuki H., Tagami M., Tagawa A., Takahashi F., Tanaka T.,
RA   Tejima Y., Toya T., Yamamura T., Yasunishi A., Yoshida K., Yoshino M.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 lipoyl-binding domain.
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DR   EMBL; AK009543; BAB26349.1; -; mRNA.
DR   IPI; IPI00556699; -.
DR   UniGene; Mm.258462; -.
DR   HSSP; P16048; 1HTP.
DR   ProteinModelPortal; Q9CV53; -.
DR   STRING; Q9CV53; -.
DR   Ensembl; ENSMUST00000040484; ENSMUSP00000037131; ENSMUSG00000034424.
DR   MGI; MGI:1915383; Gcsh.
DR   InParanoid; Q9CV53; -.
DR   ArrayExpress; Q9CV53; -.
DR   Bgee; Q9CV53; -.
DR   Genevestigator; Q9CV53; -.
DR   GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR002930; GCV_H.
DR   InterPro; IPR017453; GCV_H_sub.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   PANTHER; PTHR11715; GCV_H; 1.
DR   Pfam; PF01597; GCV_H; 1.
DR   SUPFAM; SSF51230; Hybrid_motif; 1.
DR   TIGRFAMs; TIGR00527; gcvH; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
PE   2: Evidence at transcript level;
KW   Lipoyl.
FT   NON_TER       1      1
SQ   SEQUENCE   99 AA;  10913 MW;  8B993E27E0A4B49E CRC64;
     AQEALGDVVY CSLPEVGTKL KKQEEFGALE SVKAASELYS PLSGEVTEVN EALAENPGLV
     NKSCYEDGWL IKMTLSDPSE MDELMSEEAY EKYVKSIEE
//
ID   PP13G_MOUSE             Reviewed;         347 AA.
AC   Q9CW07;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Putative protein phosphatase 1 regulatory inhibitor subunit 3G;
GN   Name=Ppp1r3g;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 59-347.
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SIMILARITY: Contains 1 CBM21 (carbohydrate binding type-21)
CC       domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB24130.1; Type=Frameshift; Positions=103;
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DR   EMBL; AC134860; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK005570; BAB24130.1; ALT_FRAME; mRNA.
DR   IPI; IPI00850288; -.
DR   RefSeq; NP_083904.1; NM_029628.1.
DR   UniGene; Mm.44745; -.
DR   ProteinModelPortal; Q9CW07; -.
DR   SMR; Q9CW07; 185-344.
DR   Ensembl; ENSMUST00000132661; ENSMUSP00000122712; ENSMUSG00000050423.
DR   GeneID; 76487; -.
DR   KEGG; mmu:76487; -.
DR   CTD; 76487; -.
DR   MGI; MGI:1923737; Ppp1r3g.
DR   GeneTree; ENSGT00530000062978; -.
DR   HOVERGEN; HBG106533; -.
DR   OrthoDB; EOG4HHP37; -.
DR   Bgee; Q9CW07; -.
DR   Genevestigator; Q9CW07; -.
DR   InterPro; IPR005036; CBM_21.
DR   Pfam; PF03370; CBM_21; 1.
DR   PROSITE; PS51159; CBM21; 1.
PE   2: Evidence at transcript level;
FT   CHAIN         1    347       Putative protein phosphatase 1 regulatory
FT                                inhibitor subunit 3G.
FT                                /FTId=PRO_0000394966.
FT   DOMAIN      200    339       CBM21.
SQ   SEQUENCE   347 AA;  37823 MW;  5485AD47C87CA657 CRC64;
     MDPSGEQLHR SEASSSTSSG DPQSAEELSV PEVLCVESGT SETPIPDAQL QDRPLSPQKG
     AALPEQEELQ EYRRSRARSF SLPADPILQA AKLLQQRQQA GQPSSEGGAP AGDCCSKCKK
     RVQFADSLGL SLASVKHFSE AEEPQVPPAV LSRLHSFPLR AEDLQQLGGL LAVATMPDPL
     LVPCARLRPH FQLPELRAAE ERLRRQRVCL ERVQCSQPPR AEVTGSGRVI SCPGPRAVAV
     RYTFTEWRTF LDVPAELDPE SVEPLPPLQS GDSGSKAEDS EEGPGTERFH FSLCLPPGLQ
     PKEGEDAGAW GVAIHFAVCY RCEQGEYWDN NEGANYTLRY VCSTDPL
//
ID   RAVR1_MOUSE             Reviewed;         748 AA.
AC   Q9CW46; Q5DTT6; Q811K0; Q8C3Z1; Q8CA14;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Ribonucleoprotein PTB-binding 1;
DE   AltName: Full=Protein raver-1;
GN   Name=Raver1; Synonyms=Kiaa1978;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PTBP1; VCL
RP   AND ACTN1, IDENTIFICATION IN A COMPLEX WITH VCL AND ACTN1, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Embryo;
RX   PubMed=11724819; DOI=10.1083/jcb.200105044;
RA   Huettelmaier S., Illenberger S., Grosheva I., Ruediger M.,
RA   Singer R.H., Jockusch B.M.;
RT   "Raver1, a dual compartment protein, is a ligand for PTB/hnRNPI and
RT   microfilament attachment proteins.";
RL   J. Cell Biol. 155:775-786(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Fetal heart, Liver, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 261-748 (ISOFORM 1).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   Identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 519-748 (ISOFORM 1).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Embryo, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION.
RX   PubMed=14633994; DOI=10.1093/emboj/cdg609;
RA   Gromak N., Rideau A., Southby J., Scadden A.D.J., Gooding C.,
RA   Huettelmaier S., Singer R.H., Smith C.W.J.;
RT   "The PTB interacting protein raver1 regulates alpha-tropomyosin
RT   alternative splicing.";
RL   EMBO J. 22:6356-6364(2003).
RN   [6]
RP   INTERACTION WITH RAVER2, AND TISSUE SPECIFICITY.
RX   PubMed=16051233; DOI=10.1016/j.febslet.2005.07.001;
RA   Kleinhenz B., Fabienke M., Swiniarski S., Wittenmayer N., Kirsch J.,
RA   Jockusch B.M., Arnold H.H., Illenberger S.;
RT   "Raver2, a new member of the hnRNP family.";
RL   FEBS Lett. 579:4254-4258(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576 AND SER-626, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND THR-469, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [10]
RP   STRUCTURE BY NMR OF 61-135.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the RNA binding domain from mouse hypothetical
RT   protein BAB23670.";
RL   Submitted (JUN-2005) to the PDB data bank.
CC   -!- FUNCTION: Cooperates with PTBP1 to modulate regulated alternative
CC       splicing events. Promotes exon skipping. Cooperates with PTBP1 to
CC       modulate switching between mutually exclusive exons during
CC       maturation of the TPM1 pre-mRNA.
CC   -!- SUBUNIT: Interacts with PTBP1, RAVER2, VCL and ACTN1. Part of a
CC       complex containing RAVER1, VCL and ACTN1.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Nuclear, in
CC       perinucleolar structures. Shuttles between nucleus and cytoplasm.
CC       Cytoplasm, at focal contacts and cell-cell contacts. Associated
CC       with myotubes during muscle differentiation.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9CW46-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CW46-2; Sequence=VSP_017037, VSP_017038;
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB23670.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY275472; AAP33691.1; -; mRNA.
DR   EMBL; AK004919; BAB23670.1; ALT_INIT; mRNA.
DR   EMBL; AK039928; BAC30481.1; -; mRNA.
DR   EMBL; AK084478; BAC39194.1; -; mRNA.
DR   EMBL; AK220434; BAD90266.1; -; mRNA.
DR   EMBL; BC043698; AAH43698.1; -; mRNA.
DR   EMBL; BC108392; AAI08393.1; -; mRNA.
DR   IPI; IPI00406706; -.
DR   IPI; IPI00719915; -.
DR   RefSeq; NP_082187.1; NM_027911.3.
DR   UniGene; Mm.432511; -.
DR   PDB; 1WI6; NMR; -; A=61-135.
DR   PDBsum; 1WI6; -.
DR   ProteinModelPortal; Q9CW46; -.
DR   SMR; Q9CW46; 39-307.
DR   IntAct; Q9CW46; 1.
DR   MINT; MINT-1707126; -.
DR   STRING; Q9CW46; -.
DR   PhosphoSite; Q9CW46; -.
DR   PRIDE; Q9CW46; -.
DR   Ensembl; ENSMUST00000010349; ENSMUSP00000010349; ENSMUSG00000010205.
DR   Ensembl; ENSMUST00000115486; ENSMUSP00000111149; ENSMUSG00000010205.
DR   Ensembl; ENSMUST00000115487; ENSMUSP00000111150; ENSMUSG00000010205.
DR   GeneID; 71766; -.
DR   KEGG; mmu:71766; -.
DR   UCSC; uc009okd.1; mouse.
DR   CTD; 71766; -.
DR   MGI; MGI:1919016; Raver1.
DR   eggNOG; roNOG04232; -.
DR   GeneTree; ENSGT00390000006046; -.
DR   HOGENOM; HBG714713; -.
DR   HOVERGEN; HBG059515; -.
DR   InParanoid; Q9CW46; -.
DR   OMA; DREPMGL; -.
DR   OrthoDB; EOG4KPT9P; -.
DR   NextBio; 334445; -.
DR   ArrayExpress; Q9CW46; -.
DR   Bgee; Q9CW46; -.
DR   CleanEx; MM_RAVER1; -.
DR   Genevestigator; Q9CW46; -.
DR   GermOnline; ENSMUSG00000010205; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 3.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 3.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm; Nucleus;
KW   Phosphoprotein; Repeat; RNA-binding.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    748       Ribonucleoprotein PTB-binding 1.
FT                                /FTId=PRO_0000081488.
FT   DOMAIN       59    130       RRM 1.
FT   DOMAIN      132    210       RRM 2.
FT   DOMAIN      221    299       RRM 3.
FT   REGION      307    401       Interaction with PTBP1.
FT   MOTIF        45     60       Nuclear localization signal (Potential).
FT   MOTIF       743    746       Nuclear localization signal (Potential).
FT   COMPBIAS    432    629       Pro-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      14     14       Phosphoserine.
FT   MOD_RES     469    469       Phosphothreonine.
FT   MOD_RES     480    480       Phosphoserine (By similarity).
FT   MOD_RES     576    576       Phosphoserine.
FT   MOD_RES     626    626       Phosphoserine.
FT   MOD_RES     677    677       Phosphoserine (By similarity).
FT   MOD_RES     716    716       Phosphoserine (By similarity).
FT   MOD_RES     720    720       Phosphoserine (By similarity).
FT   VAR_SEQ     253    270       LACGQDGQLKGFAVLEYE -> TCVIMASLELRDPPAFSS
FT                                (in isoform 2).
FT                                /FTId=VSP_017037.
FT   VAR_SEQ     271    748       Missing (in isoform 2).
FT                                /FTId=VSP_017038.
FT   CONFLICT      1      1       M -> K (in Ref. 1; BAB23670).
FT   CONFLICT    397    397       Missing (in Ref. 3; BAD90266).
FT   STRAND       61     64
FT   HELIX        72     78
FT   TURN         79     81
FT   STRAND       84     90
FT   TURN         91     94
FT   STRAND       95    102
FT   HELIX       103    113
FT   STRAND      116    120
FT   STRAND      122    127
SQ   SEQUENCE   748 AA;  79382 MW;  B0D775F14BD5B214 CRC64;
     MAADVSVTHR PPLSPEAEAE AETPETVDRR APEQELPPLD PEEIRKRLEH TERQFRNRRK
     ILIRGLPGDV TNQEVHDLLS DYELKYCFVD KYKGTAFVTL LNGEQAEAAI NTFHQSRLRE
     RELSVQLQPT DALLCVANLP PSLTQAQFEE LVRPFGSLER CFLVYSERTG HSKGYGFAEY
     MKKDSAARAK SDLLGKPLGP RTLYVHWTDA GQLTPALLHS RCLCVDHLPP GFSDVDALRR
     ALSVVYTPTF CQLACGQDGQ LKGFAVLEYE TAEMAEAAQE RADGQALGDS HLRVSFCAPG
     PPGRSMLAAL IAAQATALNR GKGLLPEPNL LQLLNNLGPS ASLQLLLNPL LHGGASGKQG
     LLGAPPAMPL LSGPALSTAL LQLALQSQSQ NQSQGQKKPG ILGDSPLGTL QAGAQPSNSL
     LGELSAGGGL APELPPRRGK PQPLLPPLLG PSGGDREPMG LGPPATQLTP PPAPVGLRGS
     NHRGLPKDSG PLPTPPGVSL LGEPPKDYRI PLNPYLNLHS LLPSSNLAGK ETRGWGGSGR
     GRRPAEPPLP SPAVPGGGSG SNNGNKAFQM KSRLLSPIAS NRLPPEPGLP DSYGFDYPTD
     VGPRRLFSHP REPTLGAHGP SRHKMSPPPS SFNEPRSGGG SGGPLSHFYS GSPTSYFTSG
     LQAGLKQSHL NKAVGSSPMG SSEGLLGLGP GPNGHSHLLK TPLGGQKRSF SHLLPSPEPS
     PEGSYVGQHS QGLGGHYADS YLKRKRIF
//
ID   FA54B_MOUSE             Reviewed;         289 AA.
AC   Q9CWE0; Q3UJK3; Q8BTP7;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Protein FAM54B;
GN   Name=Fam54b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, DBA/2, and NOD;
RC   TISSUE=Heart, Olfactory bulb, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9CWE0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CWE0-2; Sequence=VSP_034340;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the MTFR1/FAM54 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK010825; BAB27207.1; -; mRNA.
DR   EMBL; AK089141; BAC40763.1; -; mRNA.
DR   EMBL; AK145362; BAE26389.1; -; mRNA.
DR   EMBL; AK146416; BAE27152.1; -; mRNA.
DR   EMBL; AK164004; BAE37584.1; -; mRNA.
DR   EMBL; AK169047; BAE40835.1; -; mRNA.
DR   EMBL; AK171703; BAE42619.1; -; mRNA.
DR   EMBL; BC026808; AAH26808.1; -; mRNA.
DR   IPI; IPI00109033; -.
DR   IPI; IPI00458939; -.
DR   RefSeq; NP_084035.1; NM_029759.3.
DR   UniGene; Mm.30153; -.
DR   PhosphoSite; Q9CWE0; -.
DR   PRIDE; Q9CWE0; -.
DR   Ensembl; ENSMUST00000097848; ENSMUSP00000095460; ENSMUSG00000046671.
DR   Ensembl; ENSMUST00000102550; ENSMUSP00000099609; ENSMUSG00000046671.
DR   Ensembl; ENSMUST00000116279; ENSMUSP00000111983; ENSMUSG00000046671.
DR   GeneID; 76824; -.
DR   KEGG; mmu:76824; -.
DR   UCSC; uc008vfh.1; mouse.
DR   CTD; 76824; -.
DR   MGI; MGI:1924074; Fam54b.
DR   eggNOG; roNOG08932; -.
DR   GeneTree; ENSGT00530000063223; -.
DR   HOGENOM; HBG402934; -.
DR   HOVERGEN; HBG103166; -.
DR   InParanoid; Q9CWE0; -.
DR   OMA; SASPECC; -.
DR   OrthoDB; EOG4KPTBJ; -.
DR   PhylomeDB; Q9CWE0; -.
DR   NextBio; 345897; -.
DR   ArrayExpress; Q9CWE0; -.
DR   Bgee; Q9CWE0; -.
DR   Genevestigator; Q9CWE0; -.
DR   InterPro; IPR007972; DUF729.
DR   PANTHER; PTHR14215; DUF729; 1.
DR   Pfam; PF05308; DUF729; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    289       Protein FAM54B.
FT                                /FTId=PRO_0000341567.
FT   MOD_RES     100    100       Phosphoserine.
FT   MOD_RES     234    234       Phosphoserine (By similarity).
FT   MOD_RES     235    235       Phosphoserine.
FT   MOD_RES     258    258       Phosphoserine (By similarity).
FT   VAR_SEQ      94    289       VMQRNASVPNLRGSEERLLALKKPALPALSRTTELQDELSH
FT                                LRSQIAKIVAADAASASLTPDFFSSGSSNVSSPLPCFGSSL
FT                                HSTTSFVISDITEETEVEVPELPTVPLLCSASPECCKPEHK
FT                                TTCSSSEEDDCISLSKASSFADMMGILKDFHRIKQSQDLSR
FT                                SLLKEEDPAVLISEVLRRKFALKEEDISRKGN -> EIFFF
FT                                HGLSPSRKEK (in isoform 2).
FT                                /FTId=VSP_034340.
FT   CONFLICT     33     33       P -> L (in Ref. 1; BAE27152).
FT   CONFLICT    158    158       S -> Y (in Ref. 1; BAE27152).
FT   CONFLICT    188    188       E -> K (in Ref. 1; BAE27152).
SQ   SEQUENCE   289 AA;  31726 MW;  3CA0B5A8F33699B5 CRC64;
     MEANVTIPIW QNKPHGAARS VVRRIGTNLP LKPCPRASFE TLPNISDLCL KDVPPVPTLA
     DIAWIAADEE ETYARVRSDT RPLRHTWKPS PLIVMQRNAS VPNLRGSEER LLALKKPALP
     ALSRTTELQD ELSHLRSQIA KIVAADAASA SLTPDFFSSG SSNVSSPLPC FGSSLHSTTS
     FVISDITEET EVEVPELPTV PLLCSASPEC CKPEHKTTCS SSEEDDCISL SKASSFADMM
     GILKDFHRIK QSQDLSRSLL KEEDPAVLIS EVLRRKFALK EEDISRKGN
//
ID   TBB2B_MOUSE             Reviewed;         445 AA.
AC   Q9CWF2; Q3TG26;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Tubulin beta-2B chain;
GN   Name=Tubb2b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 104-121; 217-241; 263-276; 310-318 AND 381-390,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [3]
RP   POLYGLUTAMYLATION.
RX   PubMed=15890843; DOI=10.1126/science.1113010;
RA   Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M.,
RA   Temurak N., van Dijk J., Boucher D., van Dorsselaer A.,
RA   Suryavanshi S., Gaertig J., Edde B.;
RT   "Tubulin polyglutamylase enzymes are members of the TTL domain protein
RT   family.";
RL   Science 308:1758-1762(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-36, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   POLYGLYCYLATION.
RX   PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA   Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M.,
RA   Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J.,
RA   Janke C.;
RT   "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT   polyglycylation.";
RL   Cell 137:1076-1087(2009).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=19465910; DOI=10.1038/ng.380;
RA   Jaglin X.H., Poirier K., Saillour Y., Buhler E., Tian G.,
RA   Bahi-Buisson N., Fallet-Bianco C., Phan-Dinh-Tuy F., Kong X.P.,
RA   Bomont P., Castelnau-Ptakhine L., Odent S., Loget P., Kossorotoff M.,
RA   Snoeck I., Plessis G., Parent P., Beldjord C., Cardoso C., Represa A.,
RA   Flint J., Keays D.A., Cowan N.J., Chelly J.;
RT   "Mutations in the beta-tubulin gene TUBB2B result in asymmetrical
RT   polymicrogyria.";
RL   Nat. Genet. 41:746-752(2009).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. It
CC       binds two moles of GTP, one at an exchangeable site on the beta
CC       chain and one at a non-exchangeable site on the alpha-chain (By
CC       similarity). TUBB2B is implicated in neuronal migration (By
CC       similarity).
CC   -!- SUBUNIT: Dimer of alpha and beta chains (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC   -!- TISSUE SPECIFICITY: Strong expression is detected in the
CC       developing cortex and peripheral nervous system, as well as in the
CC       adult cerebellum, hippocampus and olfactory bulb.
CC   -!- PTM: Some glutamate residues at the C-terminus are either
CC       polyglutamylated or polyglycylated. These 2 modifications occur
CC       exclusively on glutamate residues and result in either
CC       polyglutamate or polyglycine chains on the gamma-carboxyl group.
CC       Glycylation is mainly limited to tubulin incorporated into
CC       axonemes (cilia and flagella) whereas glutamylation is prevalent
CC       in neuronal cells, centrioles, axonemes, and the mitotic spindle.
CC       Both modifications can coexist on the same protein on adjacent
CC       residues, and lowering polyglycylation levels increases
CC       polyglutamylation, and reciprocally. The precise function of such
CC       modifications is still unclear but they are regulate the assembly
CC       and dynamics of axonemal microtubules.
CC   -!- SIMILARITY: Belongs to the tubulin family.
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DR   EMBL; AK010786; BAB27182.1; -; mRNA.
DR   EMBL; AK168908; BAE40722.1; -; mRNA.
DR   IPI; IPI00109061; -.
DR   RefSeq; NP_076205.1; NM_023716.2.
DR   UniGene; Mm.379227; -.
DR   UniGene; Mm.472121; -.
DR   HSSP; P02554; 1FFX.
DR   ProteinModelPortal; Q9CWF2; -.
DR   SMR; Q9CWF2; 2-428.
DR   STRING; Q9CWF2; -.
DR   PhosphoSite; Q9CWF2; -.
DR   PRIDE; Q9CWF2; -.
DR   Ensembl; ENSMUST00000075774; ENSMUSP00000075178; ENSMUSG00000045136.
DR   GeneID; 73710; -.
DR   KEGG; mmu:73710; -.
DR   UCSC; uc007qbd.1; mouse.
DR   CTD; 73710; -.
DR   MGI; MGI:1920960; Tubb2b.
DR   eggNOG; roNOG14625; -.
DR   GeneTree; ENSGT00600000084255; -.
DR   HOGENOM; HBG750007; -.
DR   HOVERGEN; HBG000089; -.
DR   InParanoid; Q9CWF2; -.
DR   OMA; MGEYEED; -.
DR   OrthoDB; EOG4DFPNJ; -.
DR   PhylomeDB; Q9CWF2; -.
DR   NextBio; 338865; -.
DR   ArrayExpress; Q9CWF2; -.
DR   Bgee; Q9CWF2; -.
DR   CleanEx; MM_TUBB2B; -.
DR   Genevestigator; Q9CWF2; -.
DR   GermOnline; ENSMUSG00000045136; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR   InterPro; IPR013838; Beta-tubulin_BS.
DR   InterPro; IPR002453; Beta_tubulin.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR023123; Tubulin_C.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   Gene3D; G3DSA:3.30.1330.20; Tubulin/FtsZ_2-layer-sand-dom; 1.
DR   Gene3D; G3DSA:1.10.287.600; Tubulin_C; 1.
DR   Gene3D; G3DSA:3.40.50.1440; Tubulin_FtsZ; 1.
DR   PANTHER; PTHR11588; Tubulin; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01163; BETATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF55307; Tub_FtsZ_C; 1.
DR   SUPFAM; SSF52490; Tubulin_FtsZ; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
DR   PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Cytoskeleton; Direct protein sequencing; GTP-binding;
KW   Microtubule; Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1    445       Tubulin beta-2B chain.
FT                                /FTId=PRO_0000262652.
FT   NP_BIND     140    146       GTP (Potential).
FT   MOD_RES      36     36       Phosphotyrosine.
FT   CONFLICT    123    123       E -> G (in Ref. 1; BAE40722).
FT   CONFLICT    358    358       P -> H (in Ref. 1; BAE40722).
SQ   SEQUENCE   445 AA;  49953 MW;  4DC3956EFF880746 CRC64;
     MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGSYHGDS DLQLERINVY YNEATGNKYV
     PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
     RKESESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVM PSPKVSDTVV
     EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL
     RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDSKNMM
     AACDPRHGRY LTVAAIFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG
     LKMSATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDATA DEQGEFEEEE GEDEA
//
ID   BBS2_MOUSE              Reviewed;         721 AA.
AC   Q9CWF6;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Bardet-Biedl syndrome 2 protein homolog;
GN   Name=Bbs2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster / NIH; TISSUE=Fetus;
RX   PubMed=11285252; DOI=10.1093/hmg/10.8.865;
RA   Nishimura D.Y., Searby C.C., Carmi R., Elbedour K., Van Maldergem L.,
RA   Fulton A.B., Lam B.L., Powell B.R., Swiderski R.E., Bugge K.E.,
RA   Haider N.B., Kwitek-Black A.E., Ying L., Duhl D.M., Gorman S.M.,
RA   Heon E., Iannaccone A., Bonneau D., Biesecker L.G., Jacobson S.G.,
RA   Stone E.M., Sheffield V.C.;
RT   "Positional cloning of a novel gene on chromosome 16q causing Bardet-
RT   Biedl syndrome (BBS2).";
RL   Hum. Mol. Genet. 10:865-874(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=18317593; DOI=10.1172/JCI32357;
RA   Rahmouni K., Fath M.A., Seo S., Thedens D.R., Berry C.J., Weiss R.,
RA   Nishimura D.Y., Sheffield V.C.;
RT   "Leptin resistance contributes to obesity and hypertension in mouse
RT   models of Bardet-Biedl syndrome.";
RL   J. Clin. Invest. 118:1458-1467(2008).
CC   -!- FUNCTION: The BBSome complex is required for ciliogenesis but is
CC       dispensable for centriolar satellite function. This ciliogenic
CC       function is mediated in part by the Rab8 GDP/GTP exchange factor,
CC       which localizes to the basal body and contacts the BBSome.
CC       Rab8(GTP) enters the primary cilium and promotes extension of the
CC       ciliary membrane. Firstly the BBSome associates with the ciliary
CC       membrane and binds to Rabin8, the guanosyl exchange factor (GEF)
CC       for Rab8 and then the Rab8-GTP localizes to the cilium and
CC       promotes docking and fusion of carrier vesicles to the base of the
CC       ciliary membrane (By similarity).
CC   -!- SUBUNIT: Part of BBSome complex, that contains BBS1, BBS2, BBS4,
CC       BBS5, BBS7, BBS8, BBS9 and BBIP10. The BBSome complex binds to
CC       PCM1 and tubulin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane (By
CC       similarity). Cytoplasm (By similarity). Note=Localizes to
CC       nonmembranous centriolar satellites in the cytoplasm (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: In mice obesity is associated with
CC       hyperleptinemia and resistance to the anorectic and weight-
CC       reducing effects of leptinan mice are resistant to the metabolic
CC       actions of leptin.
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DR   EMBL; AF342737; AAK28553.1; -; mRNA.
DR   EMBL; AK010779; BAB27176.1; -; mRNA.
DR   EMBL; BC057184; AAH57184.1; -; mRNA.
DR   IPI; IPI00109070; -.
DR   RefSeq; NP_080392.1; NM_026116.2.
DR   UniGene; Mm.292107; -.
DR   ProteinModelPortal; Q9CWF6; -.
DR   STRING; Q9CWF6; -.
DR   PhosphoSite; Q9CWF6; -.
DR   PRIDE; Q9CWF6; -.
DR   Ensembl; ENSMUST00000034206; ENSMUSP00000034206; ENSMUSG00000031755.
DR   GeneID; 67378; -.
DR   KEGG; mmu:67378; -.
DR   UCSC; uc009mvs.1; mouse.
DR   CTD; 67378; -.
DR   MGI; MGI:2135267; Bbs2.
DR   GeneTree; ENSGT00390000017113; -.
DR   HOGENOM; HBG315825; -.
DR   HOVERGEN; HBG031114; -.
DR   InParanoid; Q9CWF6; -.
DR   OMA; ESHVVHP; -.
DR   OrthoDB; EOG4V9TQ3; -.
DR   NextBio; 324396; -.
DR   ArrayExpress; Q9CWF6; -.
DR   Bgee; Q9CWF6; -.
DR   CleanEx; MM_BBS2; -.
DR   Genevestigator; Q9CWF6; -.
DR   GermOnline; ENSMUSG00000031755; Mus musculus.
DR   GO; GO:0060170; C:cilium membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031514; C:motile cilium; IMP:BHF-UCL.
DR   GO; GO:0030534; P:adult behavior; IMP:MGI.
DR   GO; GO:0048854; P:brain morphogenesis; IMP:MGI.
DR   GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR   GO; GO:0060271; P:cilium morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0045444; P:fat cell differentiation; IEP:BHF-UCL.
DR   GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR   GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:MGI.
DR   GO; GO:0045494; P:photoreceptor cell maintenance; IMP:MGI.
DR   GO; GO:0033365; P:protein localization to organelle; IDA:BHF-UCL.
DR   GO; GO:0060296; P:regulation of cilium beat frequency involved in ciliary motility; IMP:BHF-UCL.
DR   GO; GO:0007288; P:sperm axoneme assembly; IMP:MGI.
DR   GO; GO:0021756; P:striatum development; IMP:MGI.
DR   InterPro; IPR016616; Bardet-Biedl_syndrome_2_prot.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF01839; FG-GAP; 1.
DR   PIRSF; PIRSF013684; BBS2; 1.
DR   SUPFAM; SSF50978; WD40_like; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Cell projection; Cilium; Cytoplasm; Membrane.
FT   CHAIN         1    721       Bardet-Biedl syndrome 2 protein homolog.
FT                                /FTId=PRO_0000064844.
SQ   SEQUENCE   721 AA;  79932 MW;  C91D9B7834B614F4 CRC64;
     MLLPVFTLKL RHKISPRMVA IGRYDGTHPC LAAATQAGKV FIHNPHTRSQ HFSASRVFQS
     PLESDVSLLN INQTVSCLGS GVLNPELGYD TLLVGTQTSL LAYDIYNNSD LFYREVSDGA
     NAIVLGTLGD IAPPLAIIGG NCALQGFDHE GNDLFWTVTG DNVHSLALCD FDGDGKTELL
     VGSEDFDIRV FKEDEIVAEM TETEIVTSLC PMYGSRFGYA LSNGTVGVYD KTARYWRIKS
     KNHAMSIHAF DINSDGVCEL ITGWSNGKVD ARSDRTGEVI FKDNFSSAVA GVVEGDYRMD
     GHVQLICCSV DGEIRGYLPG TAEMKGNLLD TSVEQDLIRE LSQKKQNLLL ELRNYEESTK
     AELSSPLNEA DGQKGIIPAN TRLHTALSVN MGNDLQDAHA ELGISTSNDT IIRAVLIFAE
     GIFVGESHVV HPSIHNLSSS LRVPITPPKD VPVDLHLKTF VGYRSSTQFH VFELTRQLPR
     FTMYALTSPD AASEPVSYVN FSVAERTQRM VTWLNQNFLL PEDSNVQNSP FHVCFTSLRN
     GGQLYIKMKQ SGEITVNTDD IDLAGDIIQS IASFFAIEDL QVEADFPVYF EELRKVLVKV
     DEYHSVHQKL SADMADNSNL IRSLLVRAED ARLMRDMKTM KSRYMELYDL NKDLLNGYKI
     RCNNHTELLG NLKAVNQAIQ RAGRLRVGKP KNQVISACRD AIRSNNINTL FRIMRVGTAP
     S
//
ID   SNX2_MOUSE              Reviewed;         519 AA.
AC   Q9CWK8; Q3UKW3; Q9CQV0;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 2.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Sorting nexin-2;
GN   Name=Snx2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, Kidney, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=12388759; DOI=10.1091/mbc.E02-03-0145;
RA   Schwarz D.G., Griffin C.T., Schneider E.A., Yee D., Magnuson T.;
RT   "Genetic analysis of sorting nexins 1 and 2 reveals a redundant and
RT   essential function in mice.";
RL   Mol. Biol. Cell 13:3588-3600(2002).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May be involved in several stages of intracellular
CC       trafficking. Component of the retromer complex, a complex required
CC       to retrieve lysosomal enzyme receptors (IGF2R and M6PR) from
CC       endosomes to the trans-Golgi network. Interacts with membranes
CC       containing phosphatidylinositol 3-phosphate (PtdIns(3P)) or
CC       phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) (By
CC       similarity).
CC   -!- SUBUNIT: Component of the retromer complex composed of VPS26
CC       (VPS26A or VPS26B), VPS29, VPS35, SNX1 and SNX2. Interacts with
CC       FNBP1. Interacts with SNX6 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane
CC       protein; Cytoplasmic side (By similarity).
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice are born at the
CC       expected Mendelian ratio and are fertile. Mice lacking both Snx1
CC       and Snx2 die during embryonic development, around 9.5 and 11.5
CC       dpc.
CC   -!- SIMILARITY: Belongs to the sorting nexin family.
CC   -!- SIMILARITY: Contains 1 PX (phox homology) domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK002692; BAB22287.1; -; mRNA.
DR   EMBL; AK005470; BAB24060.1; -; mRNA.
DR   EMBL; AK010572; BAB27035.1; -; mRNA.
DR   EMBL; AK075929; BAC36060.1; -; mRNA.
DR   EMBL; AK145840; BAE26688.1; -; mRNA.
DR   IPI; IPI00109212; -.
DR   RefSeq; NP_080662.1; NM_026386.1.
DR   UniGene; Mm.252171; -.
DR   ProteinModelPortal; Q9CWK8; -.
DR   SMR; Q9CWK8; 140-266.
DR   STRING; Q9CWK8; -.
DR   PhosphoSite; Q9CWK8; -.
DR   PRIDE; Q9CWK8; -.
DR   Ensembl; ENSMUST00000037850; ENSMUSP00000039243; ENSMUSG00000034484.
DR   GeneID; 67804; -.
DR   KEGG; mmu:67804; -.
DR   UCSC; uc008exr.1; mouse.
DR   CTD; 67804; -.
DR   MGI; MGI:1915054; Snx2.
DR   GeneTree; ENSGT00550000074512; -.
DR   HOGENOM; HBG445848; -.
DR   HOVERGEN; HBG000618; -.
DR   InParanoid; Q9CWK8; -.
DR   OMA; YKVTTKT; -.
DR   OrthoDB; EOG4BK53T; -.
DR   PhylomeDB; Q9CWK8; -.
DR   NextBio; 325603; -.
DR   ArrayExpress; Q9CWK8; -.
DR   Bgee; Q9CWK8; -.
DR   CleanEx; MM_SNX2; -.
DR   Genevestigator; Q9CWK8; -.
DR   GermOnline; ENSMUSG00000034484; Mus musculus.
DR   GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   InterPro; IPR001683; Phox.
DR   InterPro; IPR005329; Sorting_nexin_N.
DR   InterPro; IPR015404; Vps5_C.
DR   Gene3D; G3DSA:3.30.1520.10; PX; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF03700; Sorting_nexin; 1.
DR   Pfam; PF09325; Vps5; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; PX; 1.
DR   PROSITE; PS50195; PX; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Endosome; Lipid-binding; Membrane; Phosphoprotein;
KW   Protein transport; Transport.
FT   CHAIN         1    519       Sorting nexin-2.
FT                                /FTId=PRO_0000213839.
FT   DOMAIN      140    269       PX.
FT   BINDING     183    183       Phosphatidylinositol 3-phosphate (By
FT                                similarity).
FT   BINDING     185    185       Phosphatidylinositol 3-phosphate; via
FT                                amide nitrogen and carbonyl oxygen (By
FT                                similarity).
FT   BINDING     211    211       Phosphatidylinositol 3-phosphate (By
FT                                similarity).
FT   BINDING     235    235       Phosphatidylinositol 3-phosphate (By
FT                                similarity).
FT   MOD_RES     119    119       Phosphoserine.
FT   MOD_RES     185    185       Phosphoserine.
FT   MOD_RES     277    277       Phosphoserine (By similarity).
FT   MOD_RES     447    447       N6-acetyllysine (By similarity).
FT   MOD_RES     469    469       N6-acetyllysine (By similarity).
FT   CONFLICT    245    245       R -> I (in Ref. 1; BAB27035).
FT   CONFLICT    428    428       R -> P (in Ref. 1; BAB27035).
SQ   SEQUENCE   519 AA;  58471 MW;  55DD0BB74E82CD82 CRC64;
     MAAEREPPPL GDVKPTDFEE LEDGEDLFTS TVSTLESSPS SPEPASLPAE DISANSNGSK
     PVEVVLDDDR EDLFAEATEE VSLDSPEREL ILSSEPSPAV TPVTPTTLIA PRIESKSISA
     PVIFDRSRDE IEEEANGDIF DIEIGVSDPE KVGDGMNAYM AYRVTTKTSL SMFSKSEFSV
     KRRFSDFLGL HSKLASKYLH VGYIVPPAPE KSIVGMTKVK VGKEDSSSTE FVEKRRAALE
     RYLQRTVKHP TLLQDPDLRQ FLESSELPRA VNTQALSGAG ILRMVNKAAD AVNKMTIKMN
     ESDAWFEEKQ QQFENLDQQL RKLHASVEAL VCHRKELSAN TAAFAKSAAM LGNSEDHTAL
     SRALSQLAEV EEKIDQLHQE QAFADFYMFS ELLSDYIRLI AAVKGVFDHR MKCWQKWEDA
     QITLLKKRET EAKMMVANKP DKIQQAKNEI REWEAKVQQG ERDFEQISKT IRKEVGRFEK
     ERVKDFKAVI IKYLESLVQT QQQLIKYWEA FLPEAKAIA
//
ID   CTBL1_MOUSE             Reviewed;         563 AA.
AC   Q9CWL8; Q3UL41; Q80X64; Q8VHE3;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Beta-catenin-like protein 1;
DE   AltName: Full=Nuclear-associated protein;
DE            Short=NAP;
GN   Name=Ctnnbl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12659813; DOI=10.1016/S0888-7543(02)00038-1;
RA   Jabbour L.S., Welter J.F., Kollar J., Hering T.M.;
RT   "Sequence, gene structure, and expression pattern of CTNNBL1, a minor-
RT   class intron-containing gene - evidence for a role in apoptosis.";
RL   Genomics 81:292-303(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-545, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Induces apoptosis in CHO cells (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY009405; AAK27389.1; -; mRNA.
DR   EMBL; AK010547; BAB27020.1; -; mRNA.
DR   EMBL; AK044690; BAC32034.1; -; mRNA.
DR   EMBL; AK077616; BAC36902.1; -; mRNA.
DR   EMBL; AK145598; BAE26532.1; -; mRNA.
DR   EMBL; AK145719; BAE26609.1; -; mRNA.
DR   EMBL; BC050787; AAH50787.1; -; mRNA.
DR   IPI; IPI00622716; -.
DR   RefSeq; NP_079956.3; NM_025680.4.
DR   UniGene; Mm.45193; -.
DR   ProteinModelPortal; Q9CWL8; -.
DR   STRING; Q9CWL8; -.
DR   PhosphoSite; Q9CWL8; -.
DR   PRIDE; Q9CWL8; -.
DR   Ensembl; ENSMUST00000029178; ENSMUSP00000029178; ENSMUSG00000027649.
DR   GeneID; 66642; -.
DR   KEGG; mmu:66642; -.
DR   UCSC; uc008nph.1; mouse.
DR   CTD; 66642; -.
DR   MGI; MGI:1913892; Ctnnbl1.
DR   GeneTree; ENSGT00390000006931; -.
DR   HOGENOM; HBG314242; -.
DR   HOVERGEN; HBG051212; -.
DR   InParanoid; Q9CWL8; -.
DR   OMA; MLREKKM; -.
DR   OrthoDB; EOG4BZN2F; -.
DR   NextBio; 322253; -.
DR   ArrayExpress; Q9CWL8; -.
DR   Bgee; Q9CWL8; -.
DR   CleanEx; MM_CTNNBL1; -.
DR   Genevestigator; Q9CWL8; -.
DR   GermOnline; ENSMUSG00000027649; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR013180; DUF1716_euk.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF08216; DUF1716; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Nucleus; Phosphoprotein.
FT   CHAIN         1    563       Beta-catenin-like protein 1.
FT                                /FTId=PRO_0000079491.
FT   COMPBIAS     22     25       Poly-Glu.
FT   COMPBIAS     68     75       Poly-Glu.
FT   MOD_RES      91     91       N6-acetyllysine (By similarity).
FT   MOD_RES     389    389       Phosphoserine (By similarity).
FT   MOD_RES     545    545       Phosphoserine.
FT   CONFLICT    121    121       I -> V (in Ref. 2; BAC32034).
FT   CONFLICT    148    148       G -> C (in Ref. 3; AAH50787).
FT   CONFLICT    399    400       TE -> QQ (in Ref. 1; AAK27389).
FT   CONFLICT    418    418       L -> M (in Ref. 2; BAC36902).
SQ   SEQUENCE   563 AA;  64980 MW;  89B67CF3A379C3D2 CRC64;
     MDVGELLSYQ PNRGTKRPRD DEEEELKTRR KQTGPRERGR YREEEATAAE DTADDKKRLL
     QIIDRDGEEE EEEEEPLDES SVKKMILTFE KRSYKNQELR IKFPDNPEKF MESELDLNDI
     IQEMHVVATM PDLYHLLVEL SAVQSLLGLL GHDNTDVSIA VVDLLQELTD IDTLHESEEG
     AEVLIDALVD GQVAALLVQN LERLDESVRE EADGVHNTLA IVENMAEFRP EMCTEAAQQG
     LLQWLLKRLK AKMPFDANKL YCSEVLAILL QDNDENRELL GELDGIDVLL QQLSVFKRHN
     PSTAEEQEMM ENLFDALCSC LMLSSNRERF LKGEGLQLMN LMLREKKVSR SSALKVLDHA
     MIGPEGTDNC HKFVDILGLR TIFPLFMKSP RKIKKVGTTE KEHEEHVCSI LASLLRNLRG
     QQRTRLLNKF TENDSEKVDR LMELHFKYLS AMQVADKKIE GEKHDIVRRG EIIDNDMEDE
     FYLRRLDAGL FILQHICYIM AEICNANVPQ IRQRVHQILN MRGSSIKIVR HIIKEYAENI
     GDGRSPEFRE TEQKRILALL ENF
//
ID   ARHGP_MOUSE             Reviewed;         618 AA.
AC   Q9CWR0; Q3TYF3; Q8R1Q4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Rho guanine nucleotide exchange factor 25;
DE   AltName: Full=Guanine nucleotide exchange factor GEFT;
DE   AltName: Full=Rac/Cdc42/Rho exchange factor GEFT;
DE   AltName: Full=RhoA/Rac/Cdc42 guanine nucleotide exchange factor GEFT;
DE   AltName: Full=p63RhoGEF;
GN   Name=Arhgef25; Synonyms=D10Ertd610e, Geft;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   MEDLINE=22565978; PubMed=12547822; DOI=10.1074/jbc.M208896200;
RA   Guo X., Stafford L.J., Bryan B., Xia C., Ma W., Wu X., Liu D.,
RA   Songyang Z., Liu M.;
RT   "A Rac/Cdc42-specific exchange factor, GEFT, induces cell
RT   proliferation, transformation, and migration.";
RL   J. Biol. Chem. 278:13207-13215(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 313-618.
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, INTERACTION WITH RHO GTPASES, AND TISSUE SPECIFICITY.
RX   PubMed=15322108; DOI=10.1074/jbc.M406216200;
RA   Bryan B., Kumar V., Stafford L.J., Cai Y., Wu G., Liu M.;
RT   "GEFT, a Rho family guanine nucleotide exchange factor, regulates
RT   neurite outgrowth and dendritic spine formation.";
RL   J. Biol. Chem. 279:45824-45832(2004).
RN   [5]
RP   FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=16314529; DOI=10.1128/MCB.25.24.11089-11101.2005;
RA   Bryan B.A., Mitchell D.C., Zhao L., Ma W., Stafford L.J., Teng B.B.,
RA   Liu M.;
RT   "Modulation of muscle regeneration, myogenesis, and adipogenesis by
RT   the Rho family guanine nucleotide exchange factor GEFT.";
RL   Mol. Cell. Biol. 25:11089-11101(2005).
RN   [6]
RP   FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=16496360; DOI=10.1002/jnr.20814;
RA   Bryan B.A., Cai Y., Liu M.;
RT   "The Rho-family guanine nucleotide exchange factor GEFT enhances
RT   retinoic acid- and cAMP-induced neurite outgrowth.";
RL   J. Neurosci. Res. 83:1151-1159(2006).
RN   [7]
RP   INTERACTION WITH BVES, AND SUBCELLULAR LOCATION.
RX   PubMed=18541910; DOI=10.1073/pnas.0802345105;
RA   Smith T.K., Hager H.A., Francis R., Kilkenny D.M., Lo C.W.,
RA   Bader D.M.;
RT   "Bves directly interacts with GEFT, and controls cell shape and
RT   movement through regulation of Rac1/Cdc42 activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:8298-8303(2008).
CC   -!- FUNCTION: May play a role in actin cytoskeleton reorganization in
CC       different tissues since its activation induces formation of actin
CC       stress fibers. It works as a guanine nucleotide exchange factor
CC       for Rho family of small GTPases. Links specifically G alpha q/11-
CC       coupled receptors to RHOA activation (By similarity). May be an
CC       important regulator of processes involved in axon and dendrite
CC       formation. In neurons seems to be an exchange factor primarily for
CC       RAC1. Involved in skeletal myogenesis.
CC   -!- SUBUNIT: Interacts with activated GNAQ and GNA11 (By similarity).
CC       Interacts (via the DH domain) with BVES (via the C-terminus
CC       cytoplasmic tail). Interacts with RHOA, CDC42 and RAC1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere (By
CC       similarity). Cell membrane. Cytoplasm, myofibril. Note=Highly
CC       colocalizes with actin regions (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9CWR0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CWR0-2; Sequence=VSP_031876;
CC   -!- TISSUE SPECIFICITY: Highly expressed in excitable tissues, such as
CC       brain, heart and muscle. Elevated expression in hippocampus and
CC       cerebellum.
CC   -!- INDUCTION: Transcriptionally up-regulated during myogenic
CC       differentiation and down-regulated during adipogenic
CC       differentiation. Protein levels up-regulated during retinoic acid
CC       and dibutyric cAMP-induced outgrowth of neurites.
CC   -!- DOMAIN: The guanine nucleotide exchange activity is autoinhibited
CC       by the PH domain (By similarity).
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF487515; AAO49464.1; -; mRNA.
DR   EMBL; AK010452; BAB26951.1; -; mRNA.
DR   EMBL; AK158684; BAE34610.1; -; mRNA.
DR   EMBL; BC023367; AAH23367.1; -; mRNA.
DR   IPI; IPI00109434; -.
DR   IPI; IPI00886360; -.
DR   RefSeq; NP_001159885.1; NM_001166413.1.
DR   RefSeq; NP_082303.2; NM_028027.3.
DR   UniGene; Mm.272230; -.
DR   HSSP; Q64096; 1KZG.
DR   ProteinModelPortal; Q9CWR0; -.
DR   SMR; Q9CWR0; 188-529.
DR   DIP; DIP-46119N; -.
DR   STRING; Q9CWR0; -.
DR   PRIDE; Q9CWR0; -.
DR   Ensembl; ENSMUST00000019611; ENSMUSP00000019611; ENSMUSG00000019467.
DR   GeneID; 52666; -.
DR   KEGG; mmu:52666; -.
DR   UCSC; uc007hik.1; mouse.
DR   CTD; 52666; -.
DR   MGI; MGI:1277173; D10Ertd610e.
DR   eggNOG; roNOG15389; -.
DR   GeneTree; ENSGT00560000076675; -.
DR   HOGENOM; HBG713288; -.
DR   HOVERGEN; HBG065330; -.
DR   InParanoid; Q9CWR0; -.
DR   OrthoDB; EOG4ZGPCF; -.
DR   NextBio; 309295; -.
DR   ArrayExpress; Q9CWR0; -.
DR   Bgee; Q9CWR0; -.
DR   CleanEx; MM_D10ERTD610E; -.
DR   Genevestigator; Q9CWR0; -.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   PROSITE; PS00741; DH_1; FALSE_NEG.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasm;
KW   Guanine-nucleotide releasing factor; Membrane.
FT   CHAIN         1    618       Rho guanine nucleotide exchange factor
FT                                25.
FT                                /FTId=PRO_0000322133.
FT   DOMAIN      199    375       DH.
FT   DOMAIN      387    505       PH.
FT   REGION      317    338       Important for binding to Rho GTPases (By
FT                                similarity).
FT   REGION      506    532       Sufficient to bind activated GNAQ (By
FT                                similarity).
FT   VAR_SEQ       1     33       MKPPDRPTPGRTDRILGVMGGMLRACAVPGQEG -> MEQS
FT                                QGSINSVTRAICQVLVDAFR (in isoform 2).
FT                                /FTId=VSP_031876.
FT   CONFLICT    148    148       G -> E (in Ref. 2; BAE34610).
FT   CONFLICT    215    215       E -> V (in Ref. 2; BAE34610).
SQ   SEQUENCE   618 AA;  68262 MW;  F5D016FACE96D3DB CRC64;
     MKPPDRPTPG RTDRILGVMG GMLRACAVPG QEGPPERDPL GPGSTKTESD CIEEDQTGQR
     EPEVLAWAPQ PESYSIAVSE GSMSASAVSG LAALSGPSSG LSSDPCSPIP PGPVTGLRRW
     LDHSKHCLSV ETEAESGQTG QCENWTLGPT LTTGQELPEL TLLTTLLEGP GDKAQPAEEE
     TLSQAPKNEE EQKKMALERS MFVLGELVET ERTYEDDLGQ IVEGYMATMA TQGVPESLRG
     RDRIVFGNIQ QIYEWHRDYF LQELQQCLKD PDWLAQLFIK HERRLHMYVV YCQNKPKSEH
     VLSEFGDSYF EELRQQLGHR LQLNDLLIKP VQRIMKYQLL LKDFLKYYRR AGKDTEELEQ
     AVEVMCFVPK RCNDMMSLGR LRGFEGKLTA QGKLLGQDTF LVTEPEAGGL LSSRGRERRV
     FLFEQIIIFS EALGGGGRGG AQPGYVYKNS IKVSCLGLEG NLQGNPCRFA LTSRGPEGGI
     QRYVLQASDP AVSQAWIKQV AQILESQRDF LNALQSPIEY QRRESQTNSL GRPGGPWVGS
     PGRMRPGDLA QASMHTPING SLPSLLLLPR GEVSRVLLPL DTQALSDTPQ TPHDSPALPT
     VNTPPCQARL AKLDEDEL
//
ID   DDAH1_MOUSE             Reviewed;         285 AA.
AC   Q9CWS0; Q3UF65;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=N(G),N(G)-dimethylarginine dimethylaminohydrolase 1;
DE            Short=DDAH-1;
DE            Short=Dimethylarginine dimethylaminohydrolase 1;
DE            EC=3.5.3.18;
DE   AltName: Full=DDAHI;
DE   AltName: Full=Dimethylargininase-1;
GN   Name=Ddah1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, and Sympathetic ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 33-42; 121-136; 160-175; 212-230; 238-247 AND
RP   268-281, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=17273169; DOI=10.1038/nm1543;
RA   Leiper J., Nandi M., Torondel B., Murray-Rust J., Malaki M.,
RA   O'Hara B., Rossiter S., Anthony S., Madhani M., Selwood D., Smith C.,
RA   Wojciak-Stothard B., Rudiger A., Stidwill R., McDonald N.Q.,
RA   Vallance P.;
RT   "Disruption of methylarginine metabolism impairs vascular
RT   homeostasis.";
RL   Nat. Med. 13:198-203(2007).
CC   -!- FUNCTION: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and
CC       N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS.
CC       Has therefore a role in the regulation of nitric oxide generation.
CC   -!- CATALYTIC ACTIVITY: N(omega),N(omega)-dimethyl-L-arginine + H(2)O
CC       = dimethylamine + L-citrulline.
CC   -!- ENZYME REGULATION: Inhibited by zinc ions (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- TISSUE SPECIFICITY: Detected in skeletal muscle, lung, heart and
CC       brain (at protein level). Detected in liver, kidney and lung.
CC   -!- DISRUPTION PHENOTYPE: Death at embryonic stages. Heterozygous mice
CC       show no visible phenotype, but have higher than normal tissue and
CC       plasma levels of asymmetric dimethylarginine (ADMA). They have
CC       increased mean arterial blood pressure and systemic vascular
CC       resistance, and decreased cardiac output and heart rate, probably
CC       due to reduced levels of nitric oxide (NO).
CC   -!- SIMILARITY: Belongs to the DDAH family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK010430; BAB26932.1; -; mRNA.
DR   EMBL; AK143507; BAE25405.1; -; mRNA.
DR   EMBL; AK148907; BAE28696.1; -; mRNA.
DR   EMBL; BC034505; AAH34505.1; -; mRNA.
DR   IPI; IPI00109482; -.
DR   RefSeq; NP_081269.1; NM_026993.3.
DR   UniGene; Mm.234247; -.
DR   ProteinModelPortal; Q9CWS0; -.
DR   SMR; Q9CWS0; 8-282.
DR   STRING; Q9CWS0; -.
DR   REPRODUCTION-2DPAGE; Q9CWS0; -.
DR   PRIDE; Q9CWS0; -.
DR   Ensembl; ENSMUST00000029845; ENSMUSP00000029845; ENSMUSG00000028194.
DR   GeneID; 69219; -.
DR   KEGG; mmu:69219; -.
DR   NMPDR; fig|10090.3.peg.9122; -.
DR   UCSC; uc008rqr.1; mouse.
DR   CTD; 69219; -.
DR   MGI; MGI:1916469; Ddah1.
DR   GeneTree; ENSGT00390000009331; -.
DR   HOGENOM; HBG714724; -.
DR   HOVERGEN; HBG055937; -.
DR   InParanoid; Q9CWS0; -.
DR   OMA; AYAANCI; -.
DR   OrthoDB; EOG4320ZN; -.
DR   BRENDA; 3.5.3.18; 244.
DR   NextBio; 328909; -.
DR   ArrayExpress; Q9CWS0; -.
DR   Bgee; Q9CWS0; -.
DR   CleanEx; MM_DDAH1; -.
DR   Genevestigator; Q9CWS0; -.
DR   GermOnline; ENSMUSG00000028194; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0016403; F:dimethylargininase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000052; P:citrulline metabolic process; ISS:UniProtKB.
DR   InterPro; IPR003198; Amidino_trans.
DR   Pfam; PF02274; Amidinotransf; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Hydrolase; Metal-binding;
KW   Zinc.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    285       N(G),N(G)-dimethylarginine
FT                                dimethylaminohydrolase 1.
FT                                /FTId=PRO_0000171119.
FT   ACT_SITE    173    173       Proton donor (By similarity).
FT   ACT_SITE    274    274       Nucleophile (By similarity).
FT   METAL       274    274       Zinc (By similarity).
FT   BINDING      30     30       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING      73     73       Substrate (By similarity).
FT   BINDING      78     78       Substrate (By similarity).
FT   BINDING      79     79       Substrate (By similarity).
FT   BINDING      98     98       Substrate (By similarity).
FT   BINDING     145    145       Substrate (By similarity).
FT   BINDING     268    268       Substrate; via carbonyl oxygen (By
FT                                similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
SQ   SEQUENCE   285 AA;  31381 MW;  290B8DDF5AAE7928 CRC64;
     MAGLGHPSAF GRATHAVVRA PPESLCRHAL RRSQGEEVDF ARAERQHELY VGVLGSKLGL
     QVVQLPADES LPDCVFVEDV AVVCEETALI TRPGAPSRRK EVDMMKEALE KLQLNIVEMK
     DENATLDGGD VLFTGREFFV GLSKRTNQRG AEILADTFKD YAVSTVPVAD SLHLKSFCSM
     AGPNLIAIGS SESAQKALKI MQQMSDHRYD KLTVPDDMAA NCIYLNIPSK GHVLLHRTPE
     EYPESAKVYE KLKDHLLIPV SNSEMEKVDG LLTCCSVFIN KKIDS
//
ID   DDX47_MOUSE             Reviewed;         455 AA.
AC   Q9CWX9;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 2.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Probable ATP-dependent RNA helicase DDX47;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 47;
GN   Name=Ddx47;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity).
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX47/RRP3
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
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DR   EMBL; AK010310; BAB26843.2; -; mRNA.
DR   EMBL; AK076982; BAC36547.1; -; mRNA.
DR   IPI; IPI00187240; -.
DR   RefSeq; NP_080636.2; NM_026360.3.
DR   UniGene; Mm.166524; -.
DR   ProteinModelPortal; Q9CWX9; -.
DR   SMR; Q9CWX9; 13-393.
DR   STRING; Q9CWX9; -.
DR   PhosphoSite; Q9CWX9; -.
DR   PRIDE; Q9CWX9; -.
DR   Ensembl; ENSMUST00000032326; ENSMUSP00000032326; ENSMUSG00000030204.
DR   GeneID; 67755; -.
DR   KEGG; mmu:67755; -.
DR   UCSC; uc009eld.1; mouse.
DR   CTD; 67755; -.
DR   MGI; MGI:1915005; Ddx47.
DR   GeneTree; ENSGT00550000074750; -.
DR   HOGENOM; HBG737336; -.
DR   HOVERGEN; HBG100512; -.
DR   InParanoid; Q9CWX9; -.
DR   OMA; SATMTSK; -.
DR   OrthoDB; EOG4TXBRS; -.
DR   PhylomeDB; Q9CWX9; -.
DR   NextBio; 325481; -.
DR   ArrayExpress; Q9CWX9; -.
DR   Bgee; Q9CWX9; -.
DR   CleanEx; MM_DDX47; -.
DR   Genevestigator; Q9CWX9; -.
DR   GermOnline; ENSMUSG00000030204; Mus musculus.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; RNA-binding.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    455       Probable ATP-dependent RNA helicase
FT                                DDX47.
FT                                /FTId=PRO_0000055051.
FT   DOMAIN       55    226       Helicase ATP-binding.
FT   DOMAIN      237    397       Helicase C-terminal.
FT   NP_BIND      68     75       ATP (By similarity).
FT   MOTIF        24     52       Q motif.
FT   MOTIF       174    177       DEAD box.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       9      9       Phosphoserine (By similarity).
SQ   SEQUENCE   455 AA;  50639 MW;  AEAEC9287BD86DFA CRC64;
     MAADEEPDSP SGALQTAAEE EETKTFKDLG VTDVLCEACD QLGWAKPTKI QIEAIPLALQ
     GRDIIGLAET GSGKTGAFAL PILNALLETP QRLFALVLTP TRELAFQISE QFEALGSSIG
     VQCAVIVGGI DSMSQSLALA KKPHIVIATP GRLIDHLENT KGFNLRALKY LVMDEADRIL
     NMDFETEVDK ILKVIPRDRK TFLFSATMTK KVQKLQRAAL KNPVKCAVSS KYQTVEKLQQ
     YYLFIPSKFK DTYLVYILNE LAGNSFMIFC STCNNTQRTA LLLRNLGFTA IPLHGQMSQS
     KRLGSLNKFK AKARSILLAT DVASRGLDIP HVDVVVNFDI PTHSKDYIHR VGRTARAGRS
     GKAITFVTQY DVELFQRIEH LIGKKLPVFP TQDEEVMMLT ERVNEAQRFA RMELREHGEK
     KKRKREDAGD DDDKEGAIGV RNKVAGGKMK KRKGR
//
ID   RBM8A_MOUSE             Reviewed;         174 AA.
AC   Q9CWZ3; Q3UT38; Q6GTD4; Q9D6U5;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 3.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=RNA-binding protein 8A;
DE   AltName: Full=RNA-binding motif protein 8A;
DE   AltName: Full=Ribonucleoprotein RBM8A;
GN   Name=Rbm8a; Synonyms=Rbm8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Egg, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Component of a splicing-dependent multiprotein exon
CC       junction complex (EJC) deposited at splice junction on mRNAs. The
CC       EJC is a dynamic structure consisting of a few core proteins and
CC       several more peripheral nuclear and cytoplasmic associated factors
CC       that join the complex only transiently either during EJC assembly
CC       or during subsequent mRNA metabolism. Core components of the EJC,
CC       that remains bound to spliced mRNAs throughout all stages of mRNA
CC       metabolism, functions to mark the position of the exon-exon
CC       junction in the mature mRNA and thereby influences downstream
CC       processes of gene expression including mRNA splicing, nuclear mRNA
CC       export, subcellular mRNA localization, translation efficiency and
CC       nonsense-mediated mRNA decay (NMD). The heterodimer MAGOH-RBM8A
CC       interacts with PYM that function to enhance the translation of
CC       EJC-bearing spliced mRNAs by recruiting them to the ribosomal 48S
CC       preinitiation complex. Remains associated with mRNAs in the
CC       cytoplasm until the mRNAs engage the translation machinery. Its
CC       removal from cytoplasmic mRNAs requires translation initiation
CC       from EJC-bearing spliced mRNAs. Associates preferentially with
CC       mRNAs produced by splicing. Does not interact with pre-mRNAs,
CC       introns, or mRNAs produced from intronless cDNAs. Associates with
CC       both nuclear mRNAs and newly exported cytoplasmic mRNAs. Complex
CC       with MAGOH is a component of the nonsense mediated decay (NMD)
CC       pathway (By similarity).
CC   -!- SUBUNIT: Heterodimer with MAGOH. Part of the exon junction complex
CC       (EJC) core complex that contains CASC3, EIF4A3, MAGOH and RBM8A.
CC       Found in a mRNA splicing-dependent EJC, at least composed of
CC       ACIN1, CASC3, DEK, EIF4A3, MAGOH, NCBP1, NCBP2, PNN, NXF1, RBM8A,
CC       UPF2, UPF3A, UPF3B, RNPS1, SAP18, SRRM1 and THOC4. Found in a
CC       post-splicing complex with NXF1, RBM8A, UPF1, UPF2, UPF3A, UPF3B
CC       and RNPS1. Interacts with BAT1, MAGOH, OVCA1, UPF3B, RNPS1, SRRM1
CC       and THOC4. Identified in the spliceosome C complex, at least
CC       composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23,
CC       DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1,
CC       GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK,
CC       HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1,
CC       PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B,
CC       PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2,
CC       SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2,
CC       SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2,
CC       SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8.
CC       Interacts with WIBG/PYM; the interaction is direct and leads to
CC       dissociate the EJC from spliced mRNAs. Associates with polysomes
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Nucleus speckle (By
CC       similarity). Cytoplasm (By similarity). Note=Nucleocytoplasmic
CC       shuttling protein. Travels to the cytoplasm as part of the exon
CC       junction complex (EJC) bound to mRNA. Colocalizes with the core
CC       EJC, THOC4, NXF1 and UAP56 in the nucleus and nuclear speckles (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9CWZ3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CWZ3-2; Sequence=VSP_010251;
CC   -!- SIMILARITY: Belongs to the RBM8A family.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK009953; BAB26605.1; -; mRNA.
DR   EMBL; AK010284; BAB26820.1; -; mRNA.
DR   EMBL; AK082925; BAC38693.1; -; mRNA.
DR   EMBL; AK139805; BAE24142.1; -; mRNA.
DR   EMBL; CH466620; EDL38900.1; -; Genomic_DNA.
DR   EMBL; BC020086; AAH20086.1; -; mRNA.
DR   EMBL; BC058376; AAH58376.1; -; mRNA.
DR   EMBL; BC132651; AAI32652.1; -; mRNA.
DR   EMBL; BC132653; AAI32654.1; -; mRNA.
DR   IPI; IPI00109860; -.
DR   IPI; IPI00410937; -.
DR   RefSeq; NP_001034607.1; NM_001039518.2.
DR   RefSeq; NP_001095877.1; NM_001102407.1.
DR   RefSeq; NP_080151.2; NM_025875.2.
DR   UniGene; Mm.261972; -.
DR   UniGene; Mm.441390; -.
DR   ProteinModelPortal; Q9CWZ3; -.
DR   SMR; Q9CWZ3; 12-155.
DR   IntAct; Q9CWZ3; 1.
DR   STRING; Q9CWZ3; -.
DR   PhosphoSite; Q9CWZ3; -.
DR   Ensembl; ENSMUST00000048915; ENSMUSP00000044548; ENSMUSG00000038374.
DR   GeneID; 545388; -.
DR   GeneID; 60365; -.
DR   KEGG; mmu:545388; -.
DR   KEGG; mmu:60365; -.
DR   UCSC; uc008qnk.1; mouse.
DR   UCSC; uc008qnl.1; mouse.
DR   CTD; 60365; -.
DR   MGI; MGI:1913129; Rbm8a.
DR   GeneTree; ENSGT00550000074641; -.
DR   HOGENOM; HBG756718; -.
DR   HOVERGEN; HBG055173; -.
DR   InParanoid; Q9CWZ3; -.
DR   OrthoDB; EOG42822W; -.
DR   PhylomeDB; Q9CWZ3; -.
DR   NextBio; 314841; -.
DR   ArrayExpress; Q9CWZ3; -.
DR   Bgee; Q9CWZ3; -.
DR   CleanEx; MM_RBM8A; -.
DR   Genevestigator; Q9CWZ3; -.
DR   GermOnline; ENSMUSG00000038374; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR   GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR008111; RNA-bd_8.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PRINTS; PR01738; RNABINDINGM8.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; mRNA processing;
KW   mRNA splicing; mRNA transport; Nonsense-mediated mRNA decay; Nucleus;
KW   Phosphoprotein; RNA-binding; Spliceosome; Translation regulation;
KW   Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    174       RNA-binding protein 8A.
FT                                /FTId=PRO_0000081764.
FT   DOMAIN       73    151       RRM.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      42     42       Phosphoserine (By similarity).
FT   MOD_RES      46     46       Phosphoserine (By similarity).
FT   MOD_RES      56     56       Phosphoserine.
FT   MOD_RES     166    166       Phosphoserine (By similarity).
FT   MOD_RES     168    168       Phosphoserine (By similarity).
FT   VAR_SEQ      43     43       Missing (in isoform 2).
FT                                /FTId=VSP_010251.
FT   CONFLICT     14     14       D -> N (in Ref. 1; BAB26605).
FT   CONFLICT     43     43       K -> E (in Ref. 1; BAC38693).
FT   CONFLICT     51     51       R -> Q (in Ref. 1; BAE24142 and 3;
FT                                AAI32652/AAI32654).
FT   CONFLICT     58     58       E -> K (in Ref. 1; BAE24142 and 3;
FT                                AAI32652/AAI32654).
FT   CONFLICT     61     61       G -> S (in Ref. 1; BAE24142 and 3;
FT                                AAI32652/AAI32654).
SQ   SEQUENCE   174 AA;  19888 MW;  70B666394BF6CCFE CRC64;
     MADVLDLHEA GGEDFAMDED GDESIHKLKE KAKKRKGRGF GSKEGSRARM REDYDSVEQD
     GDEPGPQRSV EGWILFVTGV HEEATEEDIH DKFAEYGEIK NIHLNLDRRT GYLKGYTLVE
     YETYKEAQAA MEGLNGQDLM GQPISVDWCF VRGPPKGKRR GGRRRSRSPD RRRR
//
ID   SNAG_MOUSE              Reviewed;         312 AA.
AC   Q9CWZ7; Q3TPT4;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Gamma-soluble NSF attachment protein;
DE            Short=SNAP-gamma;
DE   AltName: Full=N-ethylmaleimide-sensitive factor attachment protein gamma;
GN   Name=Napg; Synonyms=Snapg;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryonic stem cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Required for vesicular transport between the endoplasmic
CC       reticulum and the Golgi apparatus (By similarity).
CC   -!- SUBUNIT: Binds RIP11 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the SNAP family.
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DR   EMBL; AK010275; BAB26812.1; -; mRNA.
DR   EMBL; AK154573; BAE32685.1; -; mRNA.
DR   EMBL; AK164149; BAE37651.1; -; mRNA.
DR   EMBL; AK167372; BAE39468.1; -; mRNA.
DR   EMBL; BC026977; AAH26977.1; -; mRNA.
DR   IPI; IPI00109870; -.
DR   RefSeq; NP_082293.1; NM_028017.1.
DR   UniGene; Mm.292687; -.
DR   ProteinModelPortal; Q9CWZ7; -.
DR   SMR; Q9CWZ7; 2-276.
DR   STRING; Q9CWZ7; -.
DR   PhosphoSite; Q9CWZ7; -.
DR   PRIDE; Q9CWZ7; -.
DR   Ensembl; ENSMUST00000025474; ENSMUSP00000025474; ENSMUSG00000024581.
DR   GeneID; 108123; -.
DR   KEGG; mmu:108123; -.
DR   UCSC; uc008fdp.1; mouse.
DR   CTD; 108123; -.
DR   MGI; MGI:104561; Napg.
DR   eggNOG; roNOG14546; -.
DR   GeneTree; ENSGT00390000010109; -.
DR   HOGENOM; HBG387031; -.
DR   HOVERGEN; HBG001648; -.
DR   InParanoid; Q9CWZ7; -.
DR   OMA; HAAKAYE; -.
DR   OrthoDB; EOG4QNMWK; -.
DR   PhylomeDB; Q9CWZ7; -.
DR   NextBio; 360112; -.
DR   ArrayExpress; Q9CWZ7; -.
DR   Bgee; Q9CWZ7; -.
DR   Genevestigator; Q9CWZ7; -.
DR   GermOnline; ENSMUSG00000024581; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:InterPro.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000744; NSF_attach.
DR   InterPro; IPR011990; TPR-like_helical.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
DR   PANTHER; PTHR13768; NSF_attach; 1.
PE   1: Evidence at protein level;
KW   ER-Golgi transport; Membrane; Phosphoprotein; Protein transport;
KW   Transport.
FT   CHAIN         1    312       Gamma-soluble NSF attachment protein.
FT                                /FTId=PRO_0000219064.
FT   MOD_RES     284    284       Phosphoserine.
FT   MOD_RES     307    307       Phosphotyrosine (By similarity).
SQ   SEQUENCE   312 AA;  34732 MW;  12F47490EAFC57F3 CRC64;
     MAAQKINEGL EHLAKAEKYL KTGFLKWKPD YDSAASEYGK AAVAFKNAKQ FEQAKDACLR
     EAVAHENNRA LFHAAKAYEQ AGMMLKEMQK LPEAVQLIEK ASMMYLENGT PDTAAMALER
     AGKLIENVDP EKAVQLYQQT ANVFENEERL RQAVELLGKA SRLLVRGRRF DEAALSIQKE
     KNIYKEIENY PTCYKKTIAQ VLVHLHRNDY VAAERCVRES YSIPGFNGSE DCAALEQLLE
     GYDQQDQDQV SEVCNSPLFK YMDNDYAKLG LSLVVPGGGI KKKSPATPQA KPDGAAGMAA
     EEEEDEYSGG LC
//
ID   RGS19_MOUSE             Reviewed;         216 AA.
AC   Q9CX84; Q99L50;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Regulator of G-protein signaling 19;
DE            Short=RGS19;
GN   Name=Rgs19;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Inhibits signal transduction by increasing the GTPase
CC       activity of G protein alpha subunits thereby driving them into
CC       their inactive GDP-bound form. Binds to G-alpha subfamily 1
CC       members, with the order G(i)a3 > G(i)a1 > G(o)a >> G(z)a/G(i)a2.
CC       Activity on G(z)-alpha is inhibited by phosphorylation and
CC       palmitoylation of the G-protein (By similarity).
CC   -!- SUBUNIT: Interacts with GIPC PDZ domain (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor (By similarity).
CC   -!- PTM: Fatty acylated. Heavily palmitoylated in the cysteine string
CC       motif (By similarity).
CC   -!- PTM: Phosphorylated, mainly on serine residues (By similarity).
CC   -!- SIMILARITY: Contains 1 RGS domain.
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DR   EMBL; AK019401; BAB31703.1; -; mRNA.
DR   EMBL; BC003838; AAH03838.1; -; mRNA.
DR   IPI; IPI00109806; -.
DR   RefSeq; NP_080722.1; NM_026446.3.
DR   UniGene; Mm.274366; -.
DR   ProteinModelPortal; Q9CX84; -.
DR   SMR; Q9CX84; 79-206.
DR   IntAct; Q9CX84; 2.
DR   MINT; MINT-1341963; -.
DR   STRING; Q9CX84; -.
DR   PhosphoSite; Q9CX84; -.
DR   PRIDE; Q9CX84; -.
DR   Ensembl; ENSMUST00000002532; ENSMUSP00000002532; ENSMUSG00000002458.
DR   Ensembl; ENSMUST00000108776; ENSMUSP00000104406; ENSMUSG00000002458.
DR   Ensembl; ENSMUST00000108778; ENSMUSP00000104408; ENSMUSG00000002458.
DR   GeneID; 56470; -.
DR   KEGG; mmu:56470; -.
DR   UCSC; uc008onc.1; mouse.
DR   CTD; 56470; -.
DR   MGI; MGI:1915153; Rgs19.
DR   GeneTree; ENSGT00560000076525; -.
DR   HOVERGEN; HBG013233; -.
DR   InParanoid; Q9CX84; -.
DR   OrthoDB; EOG418BPC; -.
DR   PhylomeDB; Q9CX84; -.
DR   NextBio; 312734; -.
DR   ArrayExpress; Q9CX84; -.
DR   Bgee; Q9CX84; -.
DR   CleanEx; MM_RGS19; -.
DR   Genevestigator; Q9CX84; -.
DR   GermOnline; ENSMUSG00000002458; Mus musculus.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000342; Regulat_G_prot_signal.
DR   InterPro; IPR016137; Regulat_G_prot_signal_superfam.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48097; Regulat_G_prot_signal_superfam; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   2: Evidence at transcript level;
KW   Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Signal transduction inhibitor.
FT   CHAIN         1    216       Regulator of G-protein signaling 19.
FT                                /FTId=PRO_0000204230.
FT   DOMAIN       90    206       RGS.
FT   REGION      207    216       Interaction with GIPC (By similarity).
FT   COMPBIAS     39     49       Poly-Cys.
FT   MOD_RES      24     24       Phosphoserine (By similarity).
FT   MOD_RES      97     97       Phosphoserine (By similarity).
FT   MOD_RES     151    151       Phosphoserine; by MAPK1 and MAPK3 (By
FT                                similarity).
FT   CONFLICT     82     82       K -> E (in Ref. 2; AAH03838).
SQ   SEQUENCE   216 AA;  24678 MW;  4F166A6607184F31 CRC64;
     MPTPHEAEKQ HTGPEEADRP PSMSSHDAAP SGPPSRNPCC LCWCCCCSCS WNQERQRAWQ
     VSRESKLQPL PSCEVCTPPS PKEVQSWAQS FDKLMHSPTG RSVFRAFLRT EYSEENMLFW
     LACEELKAEA NQHVVDEKAR LIYEDYVSIL SPKEVSLDSR VREGINRKMQ EPSPHTFDDA
     QLQIYTLMHR DSYPRFLTSP TYRSLLLQGA PQSSEA
//
ID   TBC15_MOUSE             Reviewed;         671 AA.
AC   Q9CXF4; Q3UI41;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=TBC1 domain family member 15;
DE   AltName: Full=GTPase-activating protein RAB7;
DE            Short=GAP for RAB7;
DE            Short=Rab7-GAP;
GN   Name=Tbc1d15;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Colon, Kidney, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=16055087; DOI=10.1016/j.bbrc.2005.07.070;
RA   Zhang X.M., Walsh B., Mitchell C.A., Rowe T.;
RT   "TBC domain family, member 15 is a novel mammalian Rab GTPase-
RT   activating protein with substrate preference for Rab7.";
RL   Biochem. Biophys. Res. Commun. 335:154-161(2005).
RN   [3]
RP   FUNCTION.
RX   PubMed=20363736; DOI=10.1074/jbc.M110.111633;
RA   Peralta E.R., Martin B.C., Edinger A.L.;
RT   "Differential effects of TBC1D15 and mammalian Vps39 on Rab7
RT   activation state, lysosomal morphology, and growth factor
RT   dependence.";
RL   J. Biol. Chem. 285:16814-16821(2010).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-180, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: Acts as a GTPase activating protein for RAB7A. Does not
CC       act on RAB4, RAB5 or RAB6.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Ubiquitous, with highest expression in heart,
CC       liver and testis and lower expression in brain, spleen, lung,
CC       kidney and skeletal muscle.
CC   -!- SIMILARITY: Contains 1 Rab-GAP TBC domain.
CC   -!- CAUTION: PubMed:16055087 showns that TBC1D15 can also functions as
CC       GTPase activating for RAB11 at a lower extend than for RAB7,
CC       however this function is not confirmed by PubMed:20363736.
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DR   EMBL; AK014477; BAB29380.1; -; mRNA.
DR   EMBL; AK078875; BAC37435.1; -; mRNA.
DR   EMBL; AK147085; BAE27665.1; -; mRNA.
DR   IPI; IPI00110247; -.
DR   RefSeq; NP_079982.3; NM_025706.3.
DR   UniGene; Mm.444918; -.
DR   ProteinModelPortal; Q9CXF4; -.
DR   SMR; Q9CXF4; 302-591.
DR   IntAct; Q9CXF4; 1.
DR   STRING; Q9CXF4; -.
DR   PhosphoSite; Q9CXF4; -.
DR   PRIDE; Q9CXF4; -.
DR   Ensembl; ENSMUST00000020339; ENSMUSP00000020339; ENSMUSG00000020130.
DR   GeneID; 66687; -.
DR   KEGG; mmu:66687; -.
DR   UCSC; uc007hax.1; mouse.
DR   CTD; 66687; -.
DR   MGI; MGI:1913937; Tbc1d15.
DR   GeneTree; ENSGT00550000074386; -.
DR   HOGENOM; HBG715338; -.
DR   HOVERGEN; HBG057668; -.
DR   InParanoid; Q9CXF4; -.
DR   OMA; EVMWTEL; -.
DR   OrthoDB; EOG4M65H2; -.
DR   PhylomeDB; Q9CXF4; -.
DR   ArrayExpress; Q9CXF4; -.
DR   Bgee; Q9CXF4; -.
DR   CleanEx; MM_TBC1D15; -.
DR   Genevestigator; Q9CXF4; -.
DR   GermOnline; ENSMUSG00000020130; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005097; F:Rab GTPase activator activity; IDA:UniProtKB.
DR   GO; GO:0032313; P:regulation of Rab GTPase activity; IDA:UniProtKB.
DR   InterPro; IPR021935; DUF3548.
DR   InterPro; IPR000195; RabGAP/TBC_dom.
DR   Pfam; PF12068; DUF3548; 1.
DR   Pfam; PF00566; TBC; 1.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; RabGAP_TBC; 2.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; GTPase activation; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    671       TBC1 domain family member 15.
FT                                /FTId=PRO_0000208043.
FT   DOMAIN      329    539       Rab-GAP TBC.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      70     70       Phosphoserine (By similarity).
FT   MOD_RES     180    180       Phosphotyrosine.
FT   MOD_RES     205    205       Phosphoserine.
FT   MOD_RES     215    215       Phosphotyrosine (By similarity).
FT   MOD_RES     655    655       Phosphoserine (By similarity).
FT   MOD_RES     669    669       Phosphothreonine (By similarity).
SQ   SEQUENCE   671 AA;  76527 MW;  A822B14AE4268FDE CRC64;
     MAAAGVVSGK IIYEQEGVYI HSSCGKANDQ DSLISGILRV LEKDAEVIVD WRPLDDALDS
     SSILCAGKDS SSVVEWTQAP KERAHRGSDQ QSSYEAEWDM VTTVSFKKKP HTNGDAPGHR
     NGKSKWSFLF SLADLKSVKQ SKEGMGWSYL VFCLKDDVML PALHFHQGDS KLLIESLEKY
     VVLCESPQDS RTLLVNCQNK SLSQSFENLL DEPAYGLIQK IKKDPYTATM VGFSKVTNYI
     FDSLRGSDPS THQRPPSEMA DFLSDAIPGL KINQQEEPGF EVITRIDLGE RPVVQRREPV
     SLEEWNKSLD PEGRLVAVES MKQKIFRGGL SHSLRKQAWK FLLGYFPWDS TKEERTQLQK
     QKTDEYFRMK LQWKSVSEAQ EKRNSRLRDY RSLIEKDVNR TDRTNKFYEG QDNPGLILLH
     DILMTYCMYD FDLGYVQGMS DLLSPLLYVM ENEVDAFWCF ASYMDQMHQN FEEQMQGMKT
     QLIQLSTLLR LLDSGFCSYL ESQDSGYLYF CFRWLLIRFK REFSFLDILR LWEVMWTELP
     CKNFHLLLCC AILESEKQQI MAKHYGFNEI LKHINELSMK IDVEDILCKA EAISLQMAQC
     KELPQAVCEI LGLQDSEITT PDSDTDENVG SPCPVSAFPS STLPILAASE AKDDSPTQTL
     ASPNACRLTP A
//
ID   PPIL4_MOUSE             Reviewed;         492 AA.
AC   Q9CXG3; Q3TJX1; Q68FC7; Q9CT22;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 2.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Peptidyl-prolyl cis-trans isomerase-like 4;
DE            Short=PPIase;
DE            EC=5.2.1.8;
DE   AltName: Full=Cyclophilin-like protein PPIL4;
DE   AltName: Full=Rotamase PPIL4;
GN   Name=Ppil4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Head;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: PPIases accelerate the folding of proteins. It catalyzes
CC       the cis-trans isomerization of proline imidic peptide bonds in
CC       oligopeptides (By similarity).
CC   -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline
CC       (omega=0).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIL4
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK011443; BAB27623.1; -; mRNA.
DR   EMBL; AK014406; BAB29330.1; -; mRNA.
DR   EMBL; AK167258; BAE39374.1; -; mRNA.
DR   EMBL; BC079912; AAH79912.1; -; mRNA.
DR   IPI; IPI00110280; -.
DR   RefSeq; NP_080417.2; NM_026141.3.
DR   UniGene; Mm.38927; -.
DR   ProteinModelPortal; Q9CXG3; -.
DR   SMR; Q9CXG3; 2-167, 240-320.
DR   PhosphoSite; Q9CXG3; -.
DR   PRIDE; Q9CXG3; -.
DR   Ensembl; ENSMUST00000015901; ENSMUSP00000015901; ENSMUSG00000015757.
DR   GeneID; 67418; -.
DR   KEGG; mmu:67418; -.
DR   NMPDR; fig|10090.3.peg.13350; -.
DR   UCSC; uc007eip.1; mouse.
DR   CTD; 67418; -.
DR   MGI; MGI:1914668; Ppil4.
DR   eggNOG; roNOG10782; -.
DR   HOGENOM; HBG610621; -.
DR   HOVERGEN; HBG057731; -.
DR   InParanoid; Q9CXG3; -.
DR   OMA; AQILEMV; -.
DR   OrthoDB; EOG4QVCC7; -.
DR   PhylomeDB; Q9CXG3; -.
DR   BRENDA; 5.2.1.8; 244.
DR   NextBio; 324510; -.
DR   ArrayExpress; Q9CXG3; -.
DR   Bgee; Q9CXG3; -.
DR   CleanEx; MM_PPIL4; -.
DR   Genevestigator; Q9CXG3; -.
DR   GermOnline; ENSMUSG00000015757; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR   InterPro; IPR015891; Cyclophilin-like.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR002130; PPIase_cyclophilin.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Gene3D; G3DSA:2.40.100.10; PPIase_cyclophilin; 1.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM00360; RRM; 1.
DR   SUPFAM; SSF50891; CSA_PPIase; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; FALSE_NEG.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   2: Evidence at transcript level;
KW   Isomerase; Nucleus; Phosphoprotein; RNA-binding; Rotamase.
FT   CHAIN         1    492       Peptidyl-prolyl cis-trans isomerase-like
FT                                4.
FT                                /FTId=PRO_0000233053.
FT   DOMAIN        1    161       PPIase cyclophilin-type.
FT   DOMAIN      240    318       RRM.
FT   COMPBIAS    321    388       Lys-rich.
FT   MOD_RES     178    178       Phosphoserine (By similarity).
FT   CONFLICT    234    234       D -> E (in Ref. 1; BAB29330).
FT   CONFLICT    258    258       I -> L (in Ref. 1; BAB29330).
SQ   SEQUENCE   492 AA;  57230 MW;  8938D66664EF640E CRC64;
     MAVLLETTLG DVVIDLYTEE RPRACLNFLK LCKIKYYNYC LIHNVQRDFI IQTGDPTGTG
     RGGESIFGQL YGDQASFFEA EKVPRIKHKK KGTVSMVNNG SDQHGSQFLI TTGENLDYLD
     GVHTVFGEVT EGMDIVKKIN ETFVDKDFVP YQDIRINHTV ILDDPFDDPP DLLIPDRSPE
     PTKEQLDSGR IGADEEIDDF KGRSAEEVEE IKAEKEAKTQ AILLEMVGDL PDADIKPPEN
     VLFVCKLNPV TTDEDLEIIF SRFGPIRSCE VIRDWKTGES LCYAFIEFEK EEDCEKAFFK
     MDNVLIDDRR IHVDFSQSVA KVKWKGKGGK YTKSDFKEYE KEQDKPANLV LKEKVKPKQD
     AKYDLILDEQ GEDSKSSHSH TSKKHKKKTR HCSEEKEDEE YMPIKNPNQD IYREMGFGHY
     EEEESCWEKQ KNEKRDRRQN RSRSRSRERD GHYSNSHKPK YQTEPYERER SRKRDRSRSP
     KKSKAKEKSK YR
//
ID   ABCB8_MOUSE             Reviewed;         717 AA.
AC   Q9CXJ4; Q8C695; Q8C7W4;
DT   16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=ATP-binding cassette sub-family B member 8, mitochondrial;
DE   Flags: Precursor;
GN   Name=Abcb8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, Pituitary, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBUNIT: Monomer (Potential).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC       membrane protein (Potential).
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB
CC       family. Multidrug resistance exporter (TC 3.A.1.201) subfamily.
CC   -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain.
CC   -!- SIMILARITY: Contains 1 ABC transporter domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK014319; BAB29270.1; -; mRNA.
DR   EMBL; AK030624; BAC27052.1; -; mRNA.
DR   EMBL; AK049152; BAC33571.1; -; mRNA.
DR   EMBL; AK076315; BAC36297.1; -; mRNA.
DR   EMBL; AK166704; BAE38958.1; -; mRNA.
DR   EMBL; BC015301; AAH15301.1; -; mRNA.
DR   IPI; IPI00459383; -.
DR   RefSeq; NP_083296.2; NM_029020.2.
DR   UniGene; Mm.283914; -.
DR   HSSP; Q7RBT4; 2GHI.
DR   ProteinModelPortal; Q9CXJ4; -.
DR   SMR; Q9CXJ4; 116-696.
DR   STRING; Q9CXJ4; -.
DR   PRIDE; Q9CXJ4; -.
DR   Ensembl; ENSMUST00000073076; ENSMUSP00000072826; ENSMUSG00000028973.
DR   Ensembl; ENSMUST00000115077; ENSMUSP00000110729; ENSMUSG00000028973.
DR   GeneID; 74610; -.
DR   KEGG; mmu:74610; -.
DR   UCSC; uc008wrh.1; mouse.
DR   CTD; 74610; -.
DR   MGI; MGI:1351667; Abcb8.
DR   GeneTree; ENSGT00550000074497; -.
DR   HOGENOM; HBG758042; -.
DR   HOVERGEN; HBG008358; -.
DR   InParanoid; Q9CXJ4; -.
DR   OMA; HEFITSF; -.
DR   OrthoDB; EOG4XWFXD; -.
DR   PhylomeDB; Q9CXJ4; -.
DR   NextBio; 341207; -.
DR   ArrayExpress; Q9CXJ4; -.
DR   Bgee; Q9CXJ4; -.
DR   Genevestigator; Q9CXJ4; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR017940; ABC_transporter_type1.
DR   InterPro; IPR001140; ABC_transptr_TM_dom.
DR   InterPro; IPR011527; ABC_transptrTM_dom_typ1.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF90123; ABC_TM_1; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Nucleotide-binding; Transit peptide; Transmembrane;
KW   Transmembrane helix; Transport.
FT   TRANSIT       1     38       Mitochondrion (By similarity).
FT   CHAIN        39    717       ATP-binding cassette sub-family B member
FT                                8, mitochondrial.
FT                                /FTId=PRO_0000356233.
FT   TRANSMEM     65     85       Helical; (Potential).
FT   TRANSMEM    127    147       Helical; (Potential).
FT   TRANSMEM    178    198       Helical; (Potential).
FT   TRANSMEM    278    298       Helical; (Potential).
FT   TRANSMEM    365    385       Helical; (Potential).
FT   DOMAIN      130    419       ABC transmembrane type-1.
FT   DOMAIN      454    691       ABC transporter.
FT   NP_BIND     489    496       ATP (Potential).
FT   CONFLICT    101    101       S -> Y (in Ref. 1; BAC33571).
FT   CONFLICT    157    157       I -> M (in Ref. 1; BAC36297).
FT   CONFLICT    225    225       F -> L (in Ref. 1; BAC36297).
SQ   SEQUENCE   717 AA;  78000 MW;  E573D4276B9658EB CRC64;
     MLVHLFRFGI RGGPVPGWSL QSLRFQTFSA ARSSDDRLSS HLLRTVAQLR VQLRAHLPRA
     PPASHWSPSA WCWVGGTLVV PAVLWQHPRL CLIALCEAKE SPPAQPTRAP ELRFNWKLFW
     HFLHPHLLAL GAAIVLALGA ALVNVQIPLL LGQLVEIVAK YTRDHMGSFV SESRKLSVQL
     LLLYGVQGLL TFGYLVLLSH IGERMAMDMR KALFSSLLRQ DIAFFDAKKT GQLVSRLTTD
     VQEFKSSFKL VISQGLRSCT QVIGSLVSLS MLSPRLTLML AVVTPALMGV GTLMGSGLRK
     LSRQCQEQIA RATGVADEAL GNVRTVRAFA MEKREEERYQ AELESCCCKA EELGRGIALF
     QGLSNIAFNC MVLGTLFIGG SLVAGQQLKG GDLMSFLVAS QTVQRSMASL SVLFGQVVRG
     LSAGARVFEY MALSPVIPLT GGYCIPNKDI RGSITFQNVT FSYPCRPGFN VLKDFTLKLP
     SGKIVALVGQ SGGGKTTVAS LLERFYDPEA GSVTLDGHDL RTLNPSWLRG QVIGFISQEP
     VLFATTIMEN IRFGKLDASD EEVYTAAREA NAHEFISSFP DGYSTVVGER GTTLSGGQKQ
     RLAIARALIK QPTVLILDEA TSALDAESER VVQEALDRAS AGRTVLVIAH RLSTVRAAHS
     IIVMANGQVC EAGTHEELLK KGGLYSELIR RQTLDASLTS TPPAEKPEDP KSCQSKA
//
ID   RBM33_MOUSE             Reviewed;        1231 AA.
AC   Q9CXK9; Q3U5Z3; Q8C5J6;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   08-FEB-2011, entry version 61.
DE   RecName: Full=RNA-binding protein 33;
DE   AltName: Full=Proline-rich protein 8;
DE   AltName: Full=RNA-binding motif protein 33;
GN   Name=Rbm33; Synonyms=Prr8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 576-1231 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Head, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-243, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-243 AND SER-816,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9CXK9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CXK9-2; Sequence=VSP_030148, VSP_030149;
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR   EMBL; AK014289; BAB29246.1; -; mRNA.
DR   EMBL; AK078210; BAC37175.1; -; mRNA.
DR   EMBL; AK153360; BAE31932.1; -; mRNA.
DR   EMBL; AC134530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   IPI; IPI00110429; -.
DR   IPI; IPI00759858; -.
DR   RefSeq; NP_082510.1; NM_028234.1.
DR   UniGene; Mm.304075; -.
DR   ProteinModelPortal; Q9CXK9; -.
DR   SMR; Q9CXK9; 1157-1228.
DR   PhosphoSite; Q9CXK9; -.
DR   PRIDE; Q9CXK9; -.
DR   Ensembl; ENSMUST00000030920; ENSMUSP00000030920; ENSMUSG00000048271.
DR   GeneID; 381626; -.
DR   KEGG; mmu:381626; -.
DR   UCSC; uc008wty.1; mouse.
DR   CTD; 381626; -.
DR   MGI; MGI:1919670; Rbm33.
DR   eggNOG; maNOG07237; -.
DR   GeneTree; ENSGT00530000063891; -.
DR   HOVERGEN; HBG108398; -.
DR   NextBio; 402319; -.
DR   ArrayExpress; Q9CXK9; -.
DR   Bgee; Q9CXK9; -.
DR   CleanEx; MM_PRR8; -.
DR   Genevestigator; Q9CXK9; -.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50102; RRM; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Phosphoprotein.
FT   CHAIN         1   1231       RNA-binding protein 33.
FT                                /FTId=PRO_0000285045.
FT   COILED      840    891       Potential.
FT   COMPBIAS    344    719       Pro-rich.
FT   COMPBIAS    641    911       Gln-rich.
FT   COMPBIAS    655    692       His-rich.
FT   MOD_RES      41     41       Phosphoserine.
FT   MOD_RES     243    243       Phosphoserine.
FT   MOD_RES     792    792       Phosphoserine (By similarity).
FT   MOD_RES     816    816       Phosphoserine.
FT   VAR_SEQ     285    320       ELSAEAKAALLEFEERERQHKQGRYGSRRGGRRGGS -> G
FT                                NSWFWPVGKLIKFPHPFLACFLDLYFHFRSLHIFL (in
FT                                isoform 2).
FT                                /FTId=VSP_030148.
FT   VAR_SEQ     321   1231       Missing (in isoform 2).
FT                                /FTId=VSP_030149.
FT   CONFLICT    794    794       P -> S (in Ref. 1; BAE31932).
SQ   SEQUENCE   1231 AA;  137325 MW;  6A85C1D1D122B27C CRC64;
     MAAALGAGGG AGAGDDDFDQ FDKPGAERSW RRRAADEDWD SELEDDLLGE DLLSGKKNQS
     DLSDEELNDD LLQSDNEEEE NFSSQGVTIS LNTTSGIVTS FELSDNTNDQ SGEQESEYEQ
     GDDELAYHKP EEQELYTQEY PEEGQYEGHD AELTEDQIEY GDEPEEEQLY SDEVLDIEIN
     EPLDEFTDEE YLQAYGGQQG LQVREDCEAE DDLDEITDSQ VASETHEGGM ETLELQKDIK
     EESDEEDDDD EESGRLRFKT ERKEGTIIRL SDVTRERRNI PETLELSAEA KAALLEFEER
     ERQHKQGRYG SRRGGRRGGS LMCRGMGDQR RDNSERGRMK EHRPALLPTQ PSVVAHSPRL
     IPPPQPQPPP PPPPPPPQQQ PIRSLFQQQQ LQPLLPLQHP HHPSPPQGVH MPPQIETPRM
     MLTPPPVTPQ QPKNIHINPH FKGTVVTPVQ VPLLPVPSQP RPAVGPQRFP GPPEFPQHTP
     GPVPNSFNQP PRLPLQDQWR APPPPQERDP FFLGVSGEPR FPSHLFLEQR SPPPPPPPPT
     LLNSSHPVPT QSPLPFTQPG PAFNQQGQQP VFPRERPVRP ALQPPGPVGI LHFSQPGSAT
     ARPFIPPRQP FLPSPGQPFL PTHAQPNLQG PLHPPLPPPH QPQPQPQQPQ QQPQHHQHQP
     PLQPPLQPPH QPPPQHQPPP QHQPQQHQHH HHLSAPPPPL MPMSQPQFRP HVQTAQPQPS
     SSRMQCTPHQ GLRHNAASQN ISKRPMQQMQ PTAPRNSNLR ELPIAPSHVL EMSGNRCSST
     PVAQVKSIVN TSPPCRAVVS SRSSQGNTDA KAKPLSPEAQ PKEEAKPEAE FPDEDEETRL
     YRLKIEEQKR LREEILKQKE LRRQQQAGAR KKELLERLAQ QQQQQQQQQH QPQQQQQQPQ
     QIYGSQTSME QEELAATPSP TNGNPLLPFP GAQCRQNVKT RLLVKNQDIT TASVQPKAVN
     FVPPGANVQH QGQHLRPLKH LRQLPHKVLQ VKPMDMEETP HSPQAARVTS LQGRPQDTKP
     GVKRTVMHRA NSGGGGDGPH VSSKVRVIKL SGGQGGESDG FSHTEGQPQR LPQPPDMRQQ
     PTRKVTLTKG VPQQPQHLPV GPHMYPAIPP GIKSIQGIHP AKKAIMHGRG RGVAGPMGRG
     RLMPNKQNLR VVECKPQPCV VSVEGLSSST TDVQLKSLLM SVGPIQSLQM LPQQRKAIAK
     FKEPAHALAF QQKFHRHMID LSHINVALIV E
//
ID   CHODL_MOUSE             Reviewed;         273 AA.
AC   Q9CXM0; Q8VI31;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-2002, sequence version 2.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Chondrolectin;
DE   AltName: Full=Transmembrane protein MT75;
DE   Flags: Precursor;
GN   Name=Chodl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Weng L., Smits P., Hubner R., Wouters J., Merregaert J.;
RT   "Mt75, a low expressed c-type lectin gene involving in
RT   chondrogenesis.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- SIMILARITY: Contains 1 C-type lectin domain.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=Chondrolectin;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_335";
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DR   EMBL; AF311699; AAL50354.1; -; mRNA.
DR   EMBL; AK014255; BAB29226.1; -; mRNA.
DR   IPI; IPI00110486; -.
DR   UniGene; Mm.77895; -.
DR   ProteinModelPortal; Q9CXM0; -.
DR   SMR; Q9CXM0; 32-181.
DR   STRING; Q9CXM0; -.
DR   PRIDE; Q9CXM0; -.
DR   Ensembl; ENSMUST00000023568; ENSMUSP00000023568; ENSMUSG00000022860.
DR   MGI; MGI:2179069; Chodl.
DR   GeneTree; ENSGT00390000001844; -.
DR   HOVERGEN; HBG050945; -.
DR   OrthoDB; EOG408N8P; -.
DR   ArrayExpress; Q9CXM0; -.
DR   Bgee; Q9CXM0; -.
DR   CleanEx; MM_CHODL; -.
DR   Genevestigator; Q9CXM0; -.
DR   GermOnline; ENSMUSG00000022860; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC.
DR   GO; GO:0005529; F:sugar binding; IEA:UniProtKB-KW.
DR   InterPro; IPR001304; C-type_lectin.
DR   InterPro; IPR016186; C-type_lectin-like.
DR   InterPro; IPR016187; C-type_lectin_fold.
DR   Gene3D; G3DSA:3.10.100.10; C-type_lectin-like; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; C-type_lectin_fold; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; FALSE_NEG.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Lectin; Membrane; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     21       Potential.
FT   CHAIN        22    273       Chondrolectin.
FT                                /FTId=PRO_0000017416.
FT   TOPO_DOM     22    216       Extracellular (Potential).
FT   TRANSMEM    217    237       Helical; (Potential).
FT   TOPO_DOM    238    273       Cytoplasmic (Potential).
FT   DOMAIN       35    179       C-type lectin.
FT   CARBOHYD     86     86       N-linked (GlcNAc...) (Potential).
FT   DISULFID     61    178       By similarity.
FT   DISULFID    144    170       By similarity.
FT   CONFLICT     24     24       V -> W (in Ref. 2; BAB29226).
FT   CONFLICT    179    179       T -> K (in Ref. 2; BAB29226).
SQ   SEQUENCE   273 AA;  30304 MW;  E052D933F244F4C7 CRC64;
     MIRIASLLLG AALLCAQGAF ARRVVSGQKV CFADVKHPCY KMAYFHELSS RVSFQEARLA
     CESEGGVLLS LENEAEQKLI ESMLQNLTKP GTGISDGDFW IGLLRSGDGQ TSGACPDLYQ
     WSDGSSSQFR NWYTDEPSCG SEKCVVMYHQ PTANPGLGGP YLYQWNDDRC NMKHNYICTY
     EPEIHPTEPA EKPYLTNQPE ETHENVVVTE AGIIPNLIYV IIPTIPLLLL ILVALGTCCF
     QMLHKSKGRS KTSPNQSTLW ISKSTRKESG MEV
//
ID   GBG10_MOUSE             Reviewed;          68 AA.
AC   Q9CXP8; A2ALW6; Q56A84;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-10;
DE   Flags: Precursor;
GN   Name=Gng10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC       involved as a modulator or transducer in various transmembrane
CC       signaling systems. The beta and gamma chains are required for the
CC       GTPase activity, for replacement of GDP by GTP, and for G protein-
CC       effector interaction. Interacts with beta-1 and beta-2, but not
CC       with beta-3 (By similarity).
CC   -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and
CC       gamma.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- SIMILARITY: Belongs to the G protein gamma family.
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DR   EMBL; AK014158; BAB29183.1; -; mRNA.
DR   EMBL; AL805972; CAM17655.1; -; Genomic_DNA.
DR   EMBL; BC023670; AAH23670.1; -; mRNA.
DR   EMBL; BC055434; AAH55434.1; -; mRNA.
DR   IPI; IPI00110583; -.
DR   RefSeq; NP_079553.1; NM_025277.3.
DR   UniGene; Mm.41780; -.
DR   ProteinModelPortal; Q9CXP8; -.
DR   SMR; Q9CXP8; 11-60.
DR   STRING; Q9CXP8; -.
DR   PRIDE; Q9CXP8; -.
DR   Ensembl; ENSMUST00000041160; ENSMUSP00000042705; ENSMUSG00000038607.
DR   GeneID; 14700; -.
DR   KEGG; mmu:14700; -.
DR   UCSC; uc008szp.1; mouse.
DR   CTD; 14700; -.
DR   MGI; MGI:1336169; Gng10.
DR   GeneTree; ENSGT00550000074352; -.
DR   HOGENOM; HBG444905; -.
DR   HOVERGEN; HBG014983; -.
DR   InParanoid; Q9CXP8; -.
DR   OMA; STMQRLV; -.
DR   OrthoDB; EOG43FGZM; -.
DR   PhylomeDB; Q9CXP8; -.
DR   NextBio; 286663; -.
DR   ArrayExpress; Q9CXP8; -.
DR   Bgee; Q9CXP8; -.
DR   Genevestigator; Q9CXP8; -.
DR   GermOnline; ENSMUSG00000038607; Mus musculus.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; IEA:InterPro.
DR   InterPro; IPR015898; G-protein_gamma_dom.
DR   InterPro; IPR001770; Gprotein-gamma.
DR   Gene3D; G3DSA:4.10.260.10; G-protein_gamma_dom; 1.
DR   PANTHER; PTHR13809; Gprotein-gamma; 1.
DR   Pfam; PF00631; G-gamma; 1.
DR   PRINTS; PR00321; GPROTEING.
DR   SMART; SM00224; GGL; 1.
DR   SUPFAM; SSF48670; G-protein_gamma-like; 1.
DR   PROSITE; PS50058; G_PROTEIN_GAMMA; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Lipoprotein; Membrane; Methylation; Prenylation;
KW   Transducer.
FT   CHAIN         1     65       Guanine nucleotide-binding protein
FT                                G(I)/G(S)/G(O) subunit gamma-10.
FT                                /FTId=PRO_0000012657.
FT   PROPEP       66     68       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000012658.
FT   MOD_RES      65     65       Cysteine methyl ester (By similarity).
FT   LIPID        65     65       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   68 AA;  7229 MW;  FCE33C306AE7EE5A CRC64;
     MSSGASVSAL QRLVEQLKLE AGVERIKVSQ AAAELQQYCI QNACKDALLL GVPAGSNPFR
     EPRSCALL
//
ID   Q9CXX2_MOUSE            Unreviewed;       182 AA.
AC   Q9CXX2;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   30-NOV-2010, entry version 56.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Vamp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RA   Adachi J., Aizawa K., Akahira S., Akimura T., Arai A., Aono H.,
RA   Arakawa T., Bono H., Carninci P., Fukuda S., Fukunishi Y., Furuno M.,
RA   Hanagaki T., Hara A., Hayatsu N., Hiramoto K., Hiraoka T., Hori F.,
RA   Imotani K., Ishii Y., Itoh M., Izawa M., Kasukawa T., Kato H.,
RA   Kawai J., Kojima Y., Konno H., Kouda M., Koya S., Kurihara C.,
RA   Matsuyama T., Miyazaki A., Nishi K., Nomura K., Numazaki R., Ohno M.,
RA   Okazaki Y., Okido T., Owa C., Saito H., Saito R., Sakai C., Sakai K.,
RA   Sano H., Sasaki D., Shibata K., Shibata Y., Shinagawa A., Shiraki T.,
RA   Sogabe Y., Suzuki H., Tagami M., Tagawa A., Takahashi F., Tanaka T.,
RA   Tejima Y., Toya T., Yamamura T., Yasunishi A., Yoshida K., Yoshino M.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=93354436; PubMed=8350916; DOI=10.1038/364581b0;
RA   Patarnello T., Bargelloni L., Rossetto O., Schiavo G., Montecucco C.;
RT   "Neurotransmission and secretion.";
RL   Nature 364:581-582(1993).
CC   -!- SIMILARITY: Contains 1 v-SNARE coiled-coil homology domain.
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DR   EMBL; AK013893; BAB29042.1; -; mRNA.
DR   IPI; IPI00407347; -.
DR   PIR; S35552; S35552.
DR   UniGene; Mm.10626; -.
DR   UniGene; Mm.441028; -.
DR   HSSP; P47194; 1L4A.
DR   ProteinModelPortal; Q9CXX2; -.
DR   SMR; Q9CXX2; 27-94.
DR   STRING; Q9CXX2; -.
DR   PRIDE; Q9CXX2; -.
DR   PhylomeDB; Q9CXX2; -.
DR   Genevestigator; Q9CXX2; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR001388; Synaptobrevin.
DR   Pfam; PF00957; Synaptobrevin; 1.
DR   PRINTS; PR00219; SYNAPTOBREVN.
DR   PROSITE; PS00417; SYNAPTOBREVIN; 1.
DR   PROSITE; PS50892; V_SNARE; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil.
SQ   SEQUENCE   182 AA;  20121 MW;  650194992010D61D CRC64;
     MSAPAQPPAE GTEGAAPGGG PPGPPPNMTS NRRLQQTQAQ VEEVVDIMRV NVDKVLERDQ
     KLSELDDRAD ALQAGASQFE SSAAKLKRKY WWKNCKMMIM LGAICAIIVV VIVRMKISFG
     YRNDCKNGPP RNWNFPRNLM LGEGKAEACA SQEEPFSRCC YICRPCCLNS EIHLPLPPEC
     LD
//
ID   RT28_MOUSE              Reviewed;         186 AA.
AC   Q9CY16; Q8R2K6;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=28S ribosomal protein S28, mitochondrial;
DE            Short=MRP-S28;
DE            Short=S28mt;
DE   Flags: Precursor;
GN   Name=Mrps28;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBUNIT: Component of the mitochondrial ribosome small subunit
CC       (28S) which comprises a 12S rRNA and about 30 distinct proteins.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
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DR   EMBL; AK011036; BAB27349.1; -; mRNA.
DR   EMBL; BC028530; AAH28530.1; -; mRNA.
DR   IPI; IPI00110672; -.
DR   RefSeq; NP_079710.3; NM_025434.3.
DR   UniGene; Mm.38460; -.
DR   ProteinModelPortal; Q9CY16; -.
DR   PhosphoSite; Q9CY16; -.
DR   PRIDE; Q9CY16; -.
DR   Ensembl; ENSMUST00000042148; ENSMUSP00000038305; ENSMUSG00000040269.
DR   GeneID; 66230; -.
DR   KEGG; mmu:66230; -.
DR   NMPDR; fig|10090.3.peg.7763; -.
DR   UCSC; uc008ooq.1; mouse.
DR   CTD; 66230; -.
DR   MGI; MGI:1913480; Mrps28.
DR   eggNOG; roNOG16451; -.
DR   GeneTree; ENSGT00390000001057; -.
DR   HOGENOM; HBG387113; -.
DR   HOVERGEN; HBG036126; -.
DR   InParanoid; Q9CY16; -.
DR   OMA; SKEEHHE; -.
DR   OrthoDB; EOG48KRCG; -.
DR   NextBio; 321027; -.
DR   ArrayExpress; Q9CY16; -.
DR   Bgee; Q9CY16; -.
DR   CleanEx; MM_MRPS28; -.
DR   Genevestigator; Q9CY16; -.
DR   GermOnline; ENSMUSG00000040269; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   InterPro; IPR019375; Ribosomal_S28_mit.
DR   InterPro; IPR022967; RNA-binding_domain_S1.
DR   Pfam; PF10246; MRP-S35; 1.
DR   SMART; SM00316; S1; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Mitochondrion; Ribonucleoprotein; Ribosomal protein;
KW   Transit peptide.
FT   TRANSIT       1     70       Mitochondrion (By similarity).
FT   CHAIN        71    186       28S ribosomal protein S28, mitochondrial.
FT                                /FTId=PRO_0000087715.
FT   MOD_RES     132    132       N6-acetyllysine (By similarity).
FT   CONFLICT     60     60       S -> L (in Ref. 1; AAH28530).
SQ   SEQUENCE   186 AA;  20520 MW;  74EFA7A6611823B4 CRC64;
     MAALCRSHAG TAGSRFLRAL VFSKPLRNAS TESGSESATH DSSAPRARSG GFASALERHS
     DLQRKAELRL ESPKPVESFA SMLRHSPLTQ LGPAKDKLVI GRIFHIVEDD LYIDFGGKFH
     CVCKRPDVDG EKYQRGTRVR LRLLDLELTS RFLGGTTDTT ILEADAVLLG LQEIRDSKSR
     EEQPSK
//
ID   SSRA_MOUSE              Reviewed;         286 AA.
AC   Q9CY50; Q3TIM3; Q99MP2;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Translocon-associated protein subunit alpha;
DE            Short=TRAP-alpha;
DE   AltName: Full=Signal sequence receptor subunit alpha;
DE            Short=SSR-alpha;
DE   Flags: Precursor;
GN   Name=Ssr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RA   Mesbah K., Babinet C., Barra J.;
RT   "Mus musculus TRAP alpha cDNA.";
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2; TISSUE=Embryonic liver, and Mammary gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-260, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136 AND ASN-143, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: TRAP proteins are part of a complex whose function is to
CC       bind calcium to the ER membrane and thereby regulate the retention
CC       of ER resident proteins. May be involved in the recycling of the
CC       translocation apparatus after completion of the translocation
CC       process or may function as a membrane-bound chaperone facilitating
CC       folding of translocated proteins.
CC   -!- SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and
CC       TRAP-gamma (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       type I membrane protein (By similarity).
CC   -!- DOMAIN: Shows a remarkable charge distribution with the N-terminus
CC       being highly negatively charged, and the cytoplasmic C-terminus
CC       positively charged.
CC   -!- MISCELLANEOUS: Seems to bind calcium (By similarity).
CC   -!- SIMILARITY: Belongs to the TRAP-alpha family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF326229; AAK16151.2; -; mRNA.
DR   EMBL; AF395811; AAK82421.1; -; mRNA.
DR   EMBL; AK010884; BAB27245.1; -; mRNA.
DR   EMBL; AK166235; BAE38650.1; -; mRNA.
DR   EMBL; AK167793; BAE39823.1; -; mRNA.
DR   EMBL; BC011255; AAH11255.1; -; mRNA.
DR   IPI; IPI00755329; -.
DR   RefSeq; NP_080241.3; NM_025965.3.
DR   UniGene; Mm.426670; -.
DR   UniGene; Mm.476789; -.
DR   ProteinModelPortal; Q9CY50; -.
DR   STRING; Q9CY50; -.
DR   PhosphoSite; Q9CY50; -.
DR   PRIDE; Q9CY50; -.
DR   Ensembl; ENSMUST00000021864; ENSMUSP00000021864; ENSMUSG00000021427.
DR   GeneID; 107513; -.
DR   KEGG; mmu:107513; -.
DR   UCSC; uc007qdd.1; mouse.
DR   CTD; 107513; -.
DR   MGI; MGI:105082; Ssr1.
DR   eggNOG; roNOG14801; -.
DR   GeneTree; ENSGT00400000022103; -.
DR   HOVERGEN; HBG009736; -.
DR   OrthoDB; EOG4M0F2V; -.
DR   PhylomeDB; Q9CY50; -.
DR   NextBio; 358946; -.
DR   ArrayExpress; Q9CY50; -.
DR   Bgee; Q9CY50; -.
DR   CleanEx; MM_SSR1; -.
DR   Genevestigator; Q9CY50; -.
DR   GermOnline; ENSMUSG00000021427; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR005595; TRAP_alpha.
DR   Pfam; PF03896; TRAP_alpha; 1.
PE   1: Evidence at protein level;
KW   Calcium; Endoplasmic reticulum; Glycoprotein; Membrane;
KW   Phosphoprotein; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     21       Potential.
FT   CHAIN        22    286       Translocon-associated protein subunit
FT                                alpha.
FT                                /FTId=PRO_0000033282.
FT   TOPO_DOM     22    207       Lumenal (Potential).
FT   TRANSMEM    208    228       Helical; (Potential).
FT   TOPO_DOM    229    286       Cytoplasmic (Potential).
FT   MOD_RES     247    247       Phosphoserine (By similarity).
FT   MOD_RES     260    260       Phosphothreonine.
FT   MOD_RES     268    268       Phosphoserine.
FT   CARBOHYD    136    136       N-linked (GlcNAc...).
FT   CARBOHYD    143    143       N-linked (GlcNAc...).
FT   CARBOHYD    191    191       N-linked (GlcNAc...) (Potential).
FT   CONFLICT     27     27       G -> V (in Ref. 1; AAK16151/AAK82421).
SQ   SEQUENCE   286 AA;  32065 MW;  780D1C6880700C8D CRC64;
     MRLLPRLLLL FLLAFPAAVL LRGGPGGSLA LAQDPTEDEE IVEDSIIEDE DDEAEVEEDE
     PTDLAEDKEE EDVSSEPEAS PSADTTILFV KGEDFPANNI VKFLVGFTNK GTEDFIVESL
     DASFRYPQDY QFYIQNFTAL PLNTVVPPQR QATFEYSFIP AEPMGGRPFG LVINLNYKDL
     NGNVFQDAVF NQTVTVIERE DGLDGETIFM YMFLAGLGLL VVVGLHQLLE SRKRKRPIQK
     VEMGTSSQND VDMSWIPQET LNQINKASPR RQPRKRAQKR SVGSDE
//
ID   PAIRB_MOUSE             Reviewed;         407 AA.
AC   Q9CY58; Q8BHS2; Q8BHU0; Q91WP3; Q9CSN0; Q9DBY6;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Plasminogen activator inhibitor 1 RNA-binding protein;
DE   AltName: Full=PAI1 RNA-binding protein 1;
DE            Short=PAI-RBP1;
DE   AltName: Full=SERPINE1 mRNA-binding protein 1;
GN   Name=Serbp1; Synonyms=Pairbp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Embryo, Embryonic liver, Lung, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=FVB/N; TISSUE=Eye, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25 AND SER-390, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-234; SER-252 AND
RP   TYR-244, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: May play a role in the regulation of mRNA stability.
CC       Binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region
CC       which confers cyclic nucleotide regulation of message decay (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with CHD3 and TDRD3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Cytoplasm, perinuclear region (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9CY58-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CY58-2; Sequence=VSP_011633;
CC       Name=3;
CC         IsoId=Q9CY58-3; Sequence=VSP_011632, VSP_011633;
CC       Name=4;
CC         IsoId=Q9CY58-4; Sequence=VSP_011634, VSP_011635;
CC         Note=May be due to intron retention. No experimental
CC         confirmation available;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK004678; BAB23466.1; -; mRNA.
DR   EMBL; AK010860; BAB27229.1; -; mRNA.
DR   EMBL; AK012390; BAB28207.1; -; mRNA.
DR   EMBL; AK045190; BAC32255.1; -; mRNA.
DR   EMBL; AK088278; BAC40253.1; -; mRNA.
DR   EMBL; BC013665; AAH13665.1; -; mRNA.
DR   EMBL; BC030502; AAH30502.1; -; mRNA.
DR   IPI; IPI00471475; -.
DR   IPI; IPI00471476; -.
DR   IPI; IPI00471477; -.
DR   IPI; IPI00471478; -.
DR   RefSeq; NP_001107037.1; NM_001113565.1.
DR   RefSeq; NP_001107038.1; NM_001113566.1.
DR   RefSeq; NP_080090.2; NM_025814.2.
DR   UniGene; Mm.240490; -.
DR   UniGene; Mm.440861; -.
DR   ProteinModelPortal; Q9CY58; -.
DR   STRING; Q9CY58; -.
DR   PhosphoSite; Q9CY58; -.
DR   PRIDE; Q9CY58; -.
DR   Ensembl; ENSMUST00000042990; ENSMUSP00000039110; ENSMUSG00000036371.
DR   GeneID; 66870; -.
DR   KEGG; mmu:66870; -.
DR   UCSC; uc009cfh.1; mouse.
DR   UCSC; uc009cfj.1; mouse.
DR   UCSC; uc009cfl.1; mouse.
DR   UCSC; uc009cfm.1; mouse.
DR   CTD; 66870; -.
DR   MGI; MGI:1914120; Serbp1.
DR   GeneTree; ENSGT00520000055591; -.
DR   HOGENOM; HBG713968; -.
DR   HOVERGEN; HBG056357; -.
DR   InParanoid; Q9CY58; -.
DR   OMA; FSVDKPI; -.
DR   OrthoDB; EOG4DZ1W6; -.
DR   PhylomeDB; Q9CY58; -.
DR   NextBio; 322883; -.
DR   ArrayExpress; Q9CY58; -.
DR   Bgee; Q9CY58; -.
DR   CleanEx; MM_SERBP1; -.
DR   Genevestigator; Q9CY58; -.
DR   GermOnline; ENSMUSG00000036371; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; ISS:HGNC.
DR   InterPro; IPR006861; HABP4_PAIRBP1-bd.
DR   Pfam; PF04774; HABP4_PAI-RBP1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; Nucleus; Phosphoprotein;
KW   RNA-binding.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    407       Plasminogen activator inhibitor 1 RNA-
FT                                binding protein.
FT                                /FTId=PRO_0000058183.
FT   MOD_RES      25     25       Phosphoserine.
FT   MOD_RES      61     61       Phosphothreonine (By similarity).
FT   MOD_RES      68     68       N6-acetyllysine (By similarity).
FT   MOD_RES      85     85       Phosphoserine (By similarity).
FT   MOD_RES     122    122       N6-acetyllysine (By similarity).
FT   MOD_RES     140    140       N6-acetyllysine (By similarity).
FT   MOD_RES     197    197       Phosphoserine (By similarity).
FT   MOD_RES     203    203       Phosphoserine (By similarity).
FT   MOD_RES     211    211       N6-acetyllysine (By similarity).
FT   MOD_RES     221    221       Phosphoserine (By similarity).
FT   MOD_RES     232    232       Phosphothreonine (By similarity).
FT   MOD_RES     234    234       Phosphoserine.
FT   MOD_RES     244    244       Phosphotyrosine.
FT   MOD_RES     252    252       Phosphoserine.
FT   MOD_RES     255    255       Phosphothreonine (By similarity).
FT   MOD_RES     327    327       Phosphoserine (By similarity).
FT   MOD_RES     329    329       Phosphoserine.
FT   MOD_RES     390    390       Phosphoserine.
FT   MOD_RES     391    391       Phosphoserine (By similarity).
FT   MOD_RES     393    393       Phosphoserine (By similarity).
FT   VAR_SEQ     203    208       Missing (in isoform 3).
FT                                /FTId=VSP_011632.
FT   VAR_SEQ     233    247       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_011633.
FT   VAR_SEQ     233    235       ESP -> LVF (in isoform 4).
FT                                /FTId=VSP_011634.
FT   VAR_SEQ     236    407       Missing (in isoform 4).
FT                                /FTId=VSP_011635.
FT   CONFLICT      5      5       L -> P (in Ref. 1; BAC40253).
FT   CONFLICT    403    403       F -> S (in Ref. 1; BAB23466).
SQ   SEQUENCE   407 AA;  44714 MW;  AC4F61EF7F38A8E5 CRC64;
     MPGHLQEGFG CVVTNRFDQL FDDESDPFEV LKAAENKKKE AGGGGVGGPG AKSAAQAAAQ
     TNSNAAGKQL RKESQKDRKN PLPPSVGVAD KKEETQPPVA LKKEGIRRVG RRPDQQLQGD
     GKLIDRRAER RPPRERRFEK PLEEKGEGGE FSVDRPIIER PIRGRGGLGR GRGGRGRGMG
     RGDGFDSRGK REFDRHSGSD RSSFSHYSGL KHEDKRGGSG SHNWGTVKDE LTESPKYIQK
     QISYNCSDLD QSNVTEETPE GEEHPVADTE NKENEVEEVK EEGPKEMTLD EWKAIQNKDR
     AKVEFNIRKP NEGADGQWKK GFVLHKSKSE EAHAEDSVMD HHFRKPANDI TSQLEINFGD
     LGRPGRGGRG GRGGRGRGGR PNRGSRTDKS SASAPDVDDP EAFPALA
//
ID   BIEA_MOUSE              Reviewed;         295 AA.
AC   Q9CY64; Q3T9C6; Q80WR6; Q9DD21;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Biliverdin reductase A;
DE            Short=BVR A;
DE            EC=1.3.1.24;
DE   AltName: Full=Biliverdin-IX alpha-reductase;
DE   Flags: Precursor;
GN   Name=Blvra;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryonic liver, Kidney, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Reduces the gamma-methene bridge of the open
CC       tetrapyrrole, biliverdin IX alpha, to bilirubin with the
CC       concomitant oxidation of a NADH or NADPH cofactor (By similarity).
CC   -!- CATALYTIC ACTIVITY: Bilirubin + NAD(P)(+) = biliverdin + NAD(P)H.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- PATHWAY: Porphyrin metabolism; protoheme degradation.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- MISCELLANEOUS: Uses the reactants NADH or NADPH depending on the
CC       pH; NADH is used at the acidic pH range (6-6.9) and NADPH at the
CC       alkaline range (8.5-8.7). NADPH, however, is the probable reactant
CC       in biological systems (By similarity).
CC   -!- SIMILARITY: Belongs to the gfo/idh/mocA family. Biliverdin
CC       reductase subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK002231; BAB21950.1; -; mRNA.
DR   EMBL; AK010847; BAB27219.1; -; mRNA.
DR   EMBL; AK172620; BAE43098.1; -; mRNA.
DR   EMBL; BC052146; AAH52146.1; -; mRNA.
DR   IPI; IPI00330627; -.
DR   RefSeq; NP_080954.4; NM_026678.4.
DR   UniGene; Mm.22028; -.
DR   ProteinModelPortal; Q9CY64; -.
DR   SMR; Q9CY64; 8-291.
DR   STRING; Q9CY64; -.
DR   PhosphoSite; Q9CY64; -.
DR   PRIDE; Q9CY64; -.
DR   Ensembl; ENSMUST00000002064; ENSMUSP00000002064; ENSMUSG00000001999.
DR   GeneID; 109778; -.
DR   KEGG; mmu:109778; -.
DR   NMPDR; fig|10090.3.peg.6848; -.
DR   UCSC; uc008meq.1; mouse.
DR   CTD; 109778; -.
DR   MGI; MGI:88170; Blvra.
DR   GeneTree; ENSGT00390000011072; -.
DR   HOGENOM; HBG717259; -.
DR   HOVERGEN; HBG003218; -.
DR   InParanoid; Q9CY64; -.
DR   OMA; ERKEDQY; -.
DR   OrthoDB; EOG46HGB7; -.
DR   PhylomeDB; Q9CY64; -.
DR   BRENDA; 1.3.1.24; 244.
DR   NextBio; 362743; -.
DR   ArrayExpress; Q9CY64; -.
DR   Bgee; Q9CY64; -.
DR   CleanEx; MM_BLVRA; -.
DR   Genevestigator; Q9CY64; -.
DR   GermOnline; ENSMUSG00000001999; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004074; F:biliverdin reductase activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0042167; P:heme catabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR017094; Biliverdin_Rdtase_A.
DR   InterPro; IPR015249; Biliverdin_Rdtase_cat.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR000683; Oxidoreductase_N.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF09166; Biliv-reduc_cat; 1.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   PIRSF; PIRSF037032; Biliverdin_reductase_A; 1.
DR   ProDom; PD040165; Biliverdin_Rdtase_cat; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Metal-binding; NAD; NADP; Oxidoreductase;
KW   Phosphoprotein; Zinc.
FT   PROPEP        1      2       By similarity.
FT                                /FTId=PRO_0000010854.
FT   CHAIN         3    295       Biliverdin reductase A.
FT                                /FTId=PRO_0000010855.
FT   NP_BIND      15     20       NAD or NADP (By similarity).
FT   NP_BIND      76     79       NAD or NADP (By similarity).
FT   COMPBIAS     11     16       Poly-Val.
FT   METAL       279    279       Zinc (Potential).
FT   METAL       280    280       Zinc (Potential).
FT   METAL       291    291       Zinc (Potential).
FT   METAL       292    292       Zinc (Potential).
FT   BINDING      97     97       NAD or NADP; via carbonyl oxygen (By
FT                                similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     173    173       Phosphothreonine (By similarity).
FT   MOD_RES     177    177       Phosphoserine (By similarity).
FT   MOD_RES     229    229       Phosphoserine (By similarity).
FT   MOD_RES     236    236       Phosphoserine (By similarity).
FT   MOD_RES     247    247       N6-acetyllysine (By similarity).
FT   MOD_RES     252    252       N6-acetyllysine (By similarity).
FT   CONFLICT     27     27       L -> S (in Ref. 2; AAH52146).
FT   CONFLICT    295    295       Q -> QWGGSFRYL (in Ref. 1; BAB21950).
SQ   SEQUENCE   295 AA;  33525 MW;  F2E1682BD77032A4 CRC64;
     MSTEPKRKFG VVVVGVGRAG SVRIRDLKDP HSSAFLNLIG YVSRRELGSL DNVRQISLED
     ALRSQEVDVA YICTESSSHE DYIRQFLQAG KHVLVEYPMA LSFAAAQELW ELAAQKGRVL
     HEEHIELLME EFEFLKREVA GKELLKGSLR FTASPLEEEK FGFPAFSGIS RLTWLVSLFG
     ELSLISATME NRKEDQYMKM TVQLETQNKS PLSWIEEKGP GLKRNRHISI HFKSGSLEEV
     PNVGVNKNIF LKDQDIFIQK LLGQVSAEDL AAEKKRILHC LELASDIQRL CHRKQ
//
ID   RM44_MOUSE              Reviewed;         333 AA.
AC   Q9CY73; Q8VE61;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=39S ribosomal protein L44, mitochondrial;
DE            Short=L44mt;
DE            Short=MRP-L44;
DE            EC=3.1.26.-;
DE   Flags: Precursor;
GN   Name=Mrpl44;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 219-333.
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251 AND SER-255, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
CC   -!- FUNCTION: Component of the 39S subunit of mitochondrial ribosome
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9CY73-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q9CY73-2; Sequence=VSP_014126, VSP_014127;
CC   -!- SIMILARITY: Contains 1 DRBM (double-stranded RNA-binding) domain.
CC   -!- SIMILARITY: Contains 1 RNase III domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK019986; BAB31953.1; -; mRNA.
DR   EMBL; BC019727; AAH19727.1; -; mRNA.
DR   IPI; IPI00607969; -.
DR   IPI; IPI00665641; -.
DR   UniGene; Mm.238455; -.
DR   ProteinModelPortal; Q9CY73; -.
DR   SMR; Q9CY73; 122-179, 233-307.
DR   PRIDE; Q9CY73; -.
DR   Ensembl; ENSMUST00000027464; ENSMUSP00000027464; ENSMUSG00000026248.
DR   UCSC; uc007bqx.1; mouse.
DR   MGI; MGI:1916413; Mrpl44.
DR   GeneTree; ENSGT00390000016956; -.
DR   HOGENOM; HBG281208; -.
DR   HOVERGEN; HBG054127; -.
DR   InParanoid; Q9CY73; -.
DR   OrthoDB; EOG45HRZC; -.
DR   ArrayExpress; Q9CY73; -.
DR   Bgee; Q9CY73; -.
DR   CleanEx; MM_MRPL44; -.
DR   Genevestigator; Q9CY73; -.
DR   GermOnline; ENSMUSG00000026248; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   InterPro; IPR001159; Ds-RNA-bd.
DR   InterPro; IPR014720; dsRNA-bd-like.
DR   InterPro; IPR000999; RNase_III.
DR   Gene3D; G3DSA:3.30.160.20; dsRNA-bd-like; 1.
DR   Gene3D; G3DSA:1.10.1520.10; RNase_III; 1.
DR   SUPFAM; SSF69065; RNase_III; 1.
DR   PROSITE; PS50137; DS_RBD; 1.
DR   PROSITE; PS00517; RNASE_3_1; FALSE_NEG.
DR   PROSITE; PS50142; RNASE_3_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endonuclease; Hydrolase; Mitochondrion;
KW   Nuclease; Phosphoprotein; Ribonucleoprotein; Ribosomal protein;
KW   RNA-binding; Transit peptide.
FT   TRANSIT       1     30       Mitochondrion (By similarity).
FT   CHAIN        31    333       39S ribosomal protein L44, mitochondrial.
FT                                /FTId=PRO_0000030822.
FT   DOMAIN       86    228       RNase III.
FT   DOMAIN      236    306       DRBM.
FT   COMPBIAS     54     57       Poly-Pro.
FT   MOD_RES     251    251       Phosphoserine.
FT   MOD_RES     255    255       Phosphoserine.
FT   VAR_SEQ     217    220       DFLI -> VGNG (in isoform 2).
FT                                /FTId=VSP_014126.
FT   VAR_SEQ     221    333       Missing (in isoform 2).
FT                                /FTId=VSP_014127.
SQ   SEQUENCE   333 AA;  37524 MW;  D827D1F88E8736F3 CRC64;
     MASAVFRLLQ QGPRRLLAPA VPTLAPPVRG VKKGFRAAFR FQKELERWRL LRCPPPPVRR
     SEKPNWDYHA EVQAFGSRLQ ETFSLDLLKT AFINSCYIKS EEAKRQSLGI EKEAALLNLK
     DNQELFEQGL SFSHRCLTQF LEDEFPDLPA EGTESLVSFL TGEAVVCHVA RNLAVEQLTL
     SAEFPVPLPV LRQTFFAVIG ALLQSSGPER AALFIRDFLI TQMTGKELFE MWPVVNPMGL
     LVEELKKRDI SAPESRLTRQ SGSTTALPLY FVGLYCDRKL IAEGPGETVL VAEEEAARVA
     LRKLYGFTEN RRPWDYSKPK ESPKRAEQTS VAS
//
ID   CJ058_MOUSE             Reviewed;         218 AA.
AC   Q9CYH2;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 2.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=UPF0765 protein C10orf58 homolog;
DE   Flags: Precursor;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 91-103 AND 196-206, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted (Potential).
CC   -!- SIMILARITY: Belongs to the UPF0765 family.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK017688; BAB30875.2; -; mRNA.
DR   EMBL; BC056635; AAH56635.1; -; mRNA.
DR   IPI; IPI00187272; -.
DR   RefSeq; NP_081740.2; NM_027464.3.
DR   UniGene; Mm.27227; -.
DR   ProteinModelPortal; Q9CYH2; -.
DR   PRIDE; Q9CYH2; -.
DR   Ensembl; ENSMUST00000022317; ENSMUSP00000022317; ENSMUSG00000021792.
DR   Ensembl; ENSMUST00000118466; ENSMUSP00000112377; ENSMUSG00000021792.
DR   GeneID; 70564; -.
DR   KEGG; mmu:70564; -.
DR   UCSC; uc007tci.1; mouse.
DR   MGI; MGI:1917814; 5730469M10Rik.
DR   GeneTree; ENSGT00530000063724; -.
DR   HOVERGEN; HBG060239; -.
DR   InParanoid; Q9CYH2; -.
DR   OMA; CFLCREE; -.
DR   OrthoDB; EOG4CNQSH; -.
DR   NextBio; 331876; -.
DR   ArrayExpress; Q9CYH2; -.
DR   Bgee; Q9CYH2; -.
DR   CleanEx; MM_5730469M10RIK; -.
DR   Genevestigator; Q9CYH2; -.
DR   GermOnline; ENSMUSG00000021792; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   InterPro; IPR000866; AhpC/TSA.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Pfam; PF00578; AhpC-TSA; 1.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Secreted; Signal.
FT   SIGNAL        1     21       Potential.
FT   CHAIN        22    218       UPF0765 protein C10orf58 homolog.
FT                                /FTId=PRO_0000019551.
SQ   SEQUENCE   218 AA;  24395 MW;  A59CC8F53FACBC4C CRC64;
     MGMWSIGVGA VGAAAVALLL ANTDMFLSKP RKAALEYLED IDLKTLEKEP RTFKAKELWE
     KNGAVIMAVR RPGCFLCRAE AADLMSLKPK LDELGVPLYA VVKEQVKREV EDFQPYFKGE
     IFLDEKKKFY GPERRKMMFM GLIRLGVWYN SFRAWNGGFS GNLEGEGFIL GGVFVIGSGK
     QGILLEHREK EFGDRVNPLS VLEAVKKIKL QTPASGRS
//
ID   NJMU_MOUSE              Reviewed;         393 AA.
AC   Q9CYI0; Q7TMQ9;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Protein Njmu-R1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Muellerian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May have a role in spermatogenesis (By similarity).
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DR   EMBL; AK135352; BAE22498.1; -; mRNA.
DR   EMBL; AK153246; BAE31837.1; -; mRNA.
DR   EMBL; AL591146; CAI24748.1; -; Genomic_DNA.
DR   EMBL; BC055024; AAH55024.1; -; mRNA.
DR   IPI; IPI00344786; -.
DR   RefSeq; NP_081748.1; NM_027472.3.
DR   UniGene; Mm.86860; -.
DR   PhosphoSite; Q9CYI0; -.
DR   PRIDE; Q9CYI0; -.
DR   Ensembl; ENSMUST00000103225; ENSMUSP00000099515; ENSMUSG00000057181.
DR   GeneID; 70591; -.
DR   KEGG; mmu:70591; -.
DR   UCSC; uc007klv.1; mouse.
DR   MGI; MGI:1917841; 5730455P16Rik.
DR   GeneTree; ENSGT00390000005481; -.
DR   HOGENOM; HBG446140; -.
DR   HOVERGEN; HBG006503; -.
DR   InParanoid; Q9CYI0; -.
DR   OrthoDB; EOG4PNXH2; -.
DR   NextBio; 331926; -.
DR   ArrayExpress; Q9CYI0; -.
DR   Bgee; Q9CYI0; -.
DR   CleanEx; MM_5730455P16RIK; -.
DR   Genevestigator; Q9CYI0; -.
PE   2: Evidence at transcript level;
FT   CHAIN         1    393       Protein Njmu-R1.
FT                                /FTId=PRO_0000096866.
SQ   SEQUENCE   393 AA;  44422 MW;  336D40805D12169A CRC64;
     MLPSLQESLD GDEKELESSE EGGSAEERRL EPPPSSHYCL YSFRGSRLTQ NRGDSDDGRS
     GGINAETPSG DDFSLSLVDT NLPSEVEPEL RSFIAKRLSK GAVFEGLGNV ASVELRIPGY
     RVGCYYCLFQ QEKLLPEIAA MESEHNPSEY VVCFLGGSEK GLELFRLELD KYIQGLKNNM
     NCEERSLGND VKSYLNSWYE DVVCPIQRVV LLFQEKLTFL LHAALSYTPV EFKESDEKTK
     RDINRFLSVA SLQGLIHEGT MTSLCMAMTE EQHKSVIIDC SGPQPQFHNA GSNRFCEDWM
     QAFLHGAEAG NPFLFRQVLE NFKLKAIQDT NNLKRFIRQA EMNHYALFKC YMFLKNCGSG
     DILLKIVKVE HEEMPEAKSV VAVLEEFMRE ALV
//
ID   GAPR1_MOUSE             Reviewed;         154 AA.
AC   Q9CYL5; Q3TJ42; Q8BTK4;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Golgi-associated plant pathogenesis-related protein 1;
DE            Short=GAPR-1;
DE            Short=Golgi-associated PR-1 protein;
DE   AltName: Full=Glioma pathogenesis-related protein 2;
DE            Short=GliPR 2;
GN   Name=Glipr2; Synonyms=Gapr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBUNIT: Homodimer. Interacts with CAV1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Lipid-anchor.
CC       Note=Binds lipid-enriched microdomains of Golgi membranes not only
CC       by ionic interactions but also through the myristate (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the CRISP family.
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DR   EMBL; AK017557; BAB30803.1; -; mRNA.
DR   EMBL; AK089960; BAC41014.1; -; mRNA.
DR   EMBL; AK154433; BAE32583.1; -; mRNA.
DR   EMBL; AK167595; BAE39653.1; -; mRNA.
DR   EMBL; BC031750; AAH31750.1; -; mRNA.
DR   IPI; IPI00416279; -.
DR   RefSeq; NP_081726.1; NM_027450.3.
DR   UniGene; Mm.22213; -.
DR   ProteinModelPortal; Q9CYL5; -.
DR   SMR; Q9CYL5; 4-152.
DR   STRING; Q9CYL5; -.
DR   PhosphoSite; Q9CYL5; -.
DR   PRIDE; Q9CYL5; -.
DR   Ensembl; ENSMUST00000030202; ENSMUSP00000030202; ENSMUSG00000028480.
DR   GeneID; 384009; -.
DR   KEGG; mmu:384009; -.
DR   UCSC; uc008srf.1; mouse.
DR   CTD; 384009; -.
DR   MGI; MGI:1917770; Glipr2.
DR   eggNOG; roNOG08111; -.
DR   GeneTree; ENSGT00390000020276; -.
DR   HOGENOM; HBG689653; -.
DR   HOVERGEN; HBG051701; -.
DR   InParanoid; Q9CYL5; -.
DR   OMA; FEENVPP; -.
DR   OrthoDB; EOG48GW4H; -.
DR   PhylomeDB; Q9CYL5; -.
DR   NextBio; 404299; -.
DR   ArrayExpress; Q9CYL5; -.
DR   Bgee; Q9CYL5; -.
DR   CleanEx; MM_GLIPR2; -.
DR   Genevestigator; Q9CYL5; -.
DR   GermOnline; ENSMUSG00000028480; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR001283; Allrgn_V5/Tpx1.
DR   InterPro; IPR018244; Allrgn_V5/Tpx1_CS.
DR   InterPro; IPR014044; CAP_domain.
DR   Gene3D; G3DSA:3.40.33.10; CAP_domain; 1.
DR   PANTHER; PTHR10334; Allrgn_V5/Tpx1; 1.
DR   Pfam; PF00188; SCP; 1.
DR   PRINTS; PR00837; V5TPXLIKE.
DR   SMART; SM00198; SCP; 1.
DR   SUPFAM; SSF55797; SCP-like_extracellular; 1.
DR   PROSITE; PS01009; CRISP_1; 1.
DR   PROSITE; PS01010; CRISP_2; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Coiled coil; Golgi apparatus; Lipoprotein; Membrane; Myristate.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    154       Golgi-associated plant pathogenesis-
FT                                related protein 1.
FT                                /FTId=PRO_0000211525.
FT   REGION       91     98       Interaction with CAV1 (By similarity).
FT   COILED       30     50       Potential.
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
FT   CONFLICT     54     54       H -> R (in Ref. 1; BAC41014).
FT   CONFLICT     75     75       T -> A (in Ref. 1; BAC41014).
SQ   SEQUENCE   154 AA;  17090 MW;  0F00D6180D0B5FFD CRC64;
     MGKSASKQFN NEVLKAHNEY RAQHGVPPLK LCKKLNREAQ QYSEALASTR ILKHSPESSR
     GQCGENLAWA SYDQTGKDVA DRWYSEIKSY NFQQPGFTSG TGHFTAMVWK NTKKIGVGKA
     SASDGSSFVV ARYFPAGNIV NQGFFEENVP PPKK
//
ID   SPCS2_MOUSE             Reviewed;         226 AA.
AC   Q9CYN2; Q3THR2; Q80X74; Q921V8; Q9CXK1;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Signal peptidase complex subunit 2;
DE            EC=3.4.-.-;
DE   AltName: Full=Microsomal signal peptidase 25 kDa subunit;
DE            Short=SPase 25 kDa subunit;
GN   Name=Spcs2; Synonyms=Spc25;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2; TISSUE=Embryo, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Blastocyst, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Component of the microsomal signal peptidase complex
CC       which removes signal peptides from nascent proteins as they are
CC       translocated into the lumen of the endoplasmic reticulum (By
CC       similarity).
CC   -!- SUBUNIT: Component of the microsomal signal peptidase complex
CC       which consists of five members: SEC11A, SEC11C, SPCS1, SPCS2 and
CC       SPCS3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane
CC       protein (By similarity). Endoplasmic reticulum membrane; Multi-
CC       pass membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the SPCS2 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB29262.1; Type=Erroneous termination; Positions=224; Note=Translated as Lys;
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DR   EMBL; AK014310; BAB29262.1; ALT_SEQ; mRNA.
DR   EMBL; AK017504; BAB30777.1; -; mRNA.
DR   EMBL; AK077510; BAC36836.1; -; mRNA.
DR   EMBL; AK134578; BAE22190.1; -; mRNA.
DR   EMBL; AK168173; BAE40134.1; -; mRNA.
DR   EMBL; BC010547; AAH10547.2; -; mRNA.
DR   EMBL; BC050150; AAH50150.1; -; mRNA.
DR   IPI; IPI00228236; -.
DR   RefSeq; NP_079944.1; NM_025668.3.
DR   UniGene; Mm.30043; -.
DR   STRING; Q9CYN2; -.
DR   PhosphoSite; Q9CYN2; -.
DR   PRIDE; Q9CYN2; -.
DR   Ensembl; ENSMUST00000036274; ENSMUSP00000041152; ENSMUSG00000035227.
DR   GeneID; 66624; -.
DR   KEGG; mmu:66624; -.
DR   UCSC; uc009imd.1; mouse.
DR   CTD; 66624; -.
DR   MGI; MGI:1913874; Spcs2.
DR   eggNOG; roNOG09117; -.
DR   GeneTree; ENSGT00440000038181; -.
DR   HOGENOM; HBG444386; -.
DR   HOVERGEN; HBG093979; -.
DR   InParanoid; Q9CYN2; -.
DR   OMA; KWDGAAV; -.
DR   OrthoDB; EOG4RV2SD; -.
DR   NextBio; 322198; -.
DR   ArrayExpress; Q9CYN2; -.
DR   Bgee; Q9CYN2; -.
DR   Genevestigator; Q9CYN2; -.
DR   GermOnline; ENSMUSG00000035227; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005792; C:microsome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005787; C:signal peptidase complex; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR   InterPro; IPR009582; SigPept_cplx_su2.
DR   Pfam; PF06703; SPC25; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Endoplasmic reticulum; Hydrolase; Membrane; Microsome;
KW   Protease; Transmembrane; Transmembrane helix.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    226       Signal peptidase complex subunit 2.
FT                                /FTId=PRO_0000221160.
FT   TOPO_DOM      2     86       Cytoplasmic (Potential).
FT   TRANSMEM     87    107       Helical; (Potential).
FT   TOPO_DOM    108    111       Lumenal (Potential).
FT   TRANSMEM    112    132       Helical; (Potential).
FT   TOPO_DOM    133    226       Cytoplasmic (Potential).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     169    169       N6-acetyllysine (By similarity).
FT   MOD_RES     191    191       N6-acetyllysine (By similarity).
FT   CONFLICT    110    110       S -> P (in Ref. 2; AAH50150).
FT   CONFLICT    209    209       E -> D (in Ref. 1; BAB29262).
SQ   SEQUENCE   226 AA;  24978 MW;  F8516C51FFED4DF9 CRC64;
     MAASASQGGR SGGGGGSSGA GGGPSCGTSS SRSGLLDKWK IDDKPVKIDK WDGSAVKNSL
     DDSAKKVLLE KYKYVENFGL IDGRLTICTI SCFFAIVALI WDYMHPFPES KPVLALCVIS
     YFVMMGILTI YTSYKEKSIF LVAHRKDPTG MDPDDIWQLS SSLKRFDDKY TLKLTFISGR
     TKQQREAEFT KSIAKFFDHS GTLVMDAYEP EISRLHDSLA TERKIK
//
ID   AGM1_MOUSE              Reviewed;         542 AA.
AC   Q9CYR6; B2RS40; Q543F9;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Phosphoacetylglucosamine mutase;
DE            Short=PAGM;
DE            EC=5.4.2.3;
DE   AltName: Full=Acetylglucosamine phosphomutase;
DE   AltName: Full=N-acetylglucosamine-phosphate mutase;
DE   AltName: Full=Phosphoglucomutase-3;
DE            Short=PGM 3;
GN   Name=Pgm3; Synonyms=Agm1, Pgm-3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Cerebellum, Embryo, Heart, Kidney, Placenta, Spinal ganglion,
RC   and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   STRUCTURE BY NMR OF 442-540.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the C-terminal domain of mouse
RT   phosphoacetylglucosamine mutase (PAGM).";
RL   Submitted (JAN-2006) to the PDB data bank.
CC   -!- FUNCTION: Interconverts GlcNAc-6-P and GlcNAc-1-P (By similarity).
CC   -!- CATALYTIC ACTIVITY: N-acetyl-alpha-D-glucosamine 1-phosphate = N-
CC       acetyl-D-glucosamine 6-phosphate.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC       glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate
CC       from alpha-D-glucosamine 6-phosphate (route I): step 2/2.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK013402; BAB28834.1; -; mRNA.
DR   EMBL; AK028066; BAC25733.1; -; mRNA.
DR   EMBL; AK049337; BAC33692.1; -; mRNA.
DR   EMBL; AK051706; BAC34728.1; -; mRNA.
DR   EMBL; AK160913; BAE36087.1; -; mRNA.
DR   EMBL; AK165513; BAE38229.1; -; mRNA.
DR   EMBL; AK169082; BAE40866.1; -; mRNA.
DR   EMBL; AK169787; BAE41366.1; -; mRNA.
DR   EMBL; BC138700; AAI38701.1; -; mRNA.
DR   IPI; IPI00318898; -.
DR   RefSeq; NP_001157218.1; NM_001163746.1.
DR   RefSeq; NP_082628.3; NM_028352.4.
DR   UniGene; Mm.390201; -.
DR   PDB; 1WJW; NMR; -; A=442-540.
DR   PDBsum; 1WJW; -.
DR   ProteinModelPortal; Q9CYR6; -.
DR   SMR; Q9CYR6; 1-541.
DR   STRING; Q9CYR6; -.
DR   PhosphoSite; Q9CYR6; -.
DR   PRIDE; Q9CYR6; -.
DR   Ensembl; ENSMUST00000070064; ENSMUSP00000070871; ENSMUSG00000056131.
DR   GeneID; 109785; -.
DR   KEGG; mmu:109785; -.
DR   CTD; 109785; -.
DR   MGI; MGI:97566; Pgm3.
DR   GeneTree; ENSGT00390000000509; -.
DR   HOVERGEN; HBG024321; -.
DR   InParanoid; Q9CYR6; -.
DR   OMA; INQTVGD; -.
DR   OrthoDB; EOG4TMR1V; -.
DR   PhylomeDB; Q9CYR6; -.
DR   BRENDA; 5.4.2.3; 244.
DR   ArrayExpress; Q9CYR6; -.
DR   Bgee; Q9CYR6; -.
DR   CleanEx; MM_PGM3; -.
DR   Genevestigator; Q9CYR6; -.
DR   GermOnline; ENSMUSG00000056131; Mus musculus.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004610; F:phosphoacetylglucosamine mutase activity; IMP:MGI.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IDA:MGI.
DR   GO; GO:0009790; P:embryo development; IMP:MGI.
DR   GO; GO:0019255; P:glucose 1-phosphate metabolic process; IDA:MGI.
DR   GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IMP:MGI.
DR   InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR   InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR   InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR   InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR   InterPro; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR016657; PAGM.
DR   Gene3D; G3DSA:3.40.120.10; A-D-PHexomutase_a/b/a-I/II/III; 3.
DR   Pfam; PF02878; PGM_PMM_I; 2.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   Pfam; PF00408; PGM_PMM_IV; 1.
DR   PIRSF; PIRSF016408; PAGM; 1.
DR   SUPFAM; SSF53738; A-D-PHexomutase_a/b/a-I/II/III; 4.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Isomerase; Magnesium; Metal-binding;
KW   Phosphoprotein.
FT   CHAIN         1    542       Phosphoacetylglucosamine mutase.
FT                                /FTId=PRO_0000148014.
FT   ACT_SITE     64     64       Phosphoserine intermediate (By
FT                                similarity).
FT   METAL        64     64       Magnesium; via phosphate group (By
FT                                similarity).
FT   METAL       276    276       Magnesium (By similarity).
FT   METAL       278    278       Magnesium (By similarity).
FT   METAL       280    280       Magnesium (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      64     64       Phosphoserine.
FT   STRAND      449    454
FT   STRAND      459    462
FT   STRAND      470    474
FT   HELIX       477    487
FT   STRAND      488    496
FT   STRAND      498    512
FT   HELIX       513    530
SQ   SEQUENCE   542 AA;  59453 MW;  B00E3D0F38BE4090 CRC64;
     MDLEAVCKRS ALHAKPQGLI LQYGTAGFRT NAQHLDHIMF RMGLLAVLRS KQTRSTIGVM
     VTASHNPEED NGVKLVDPLG EMLAPSWEEH ATCLASAEEQ DVRQVLAAIV EKEAVDLTQT
     AFVVIARDTR PSSEKLSQSV IDGVTVLGGQ FHDYGLLTTP QLHYMVYCRN SGGRYGQATV
     EGYCQKLSKA FVDLTNQVSC SGDVKRSVKV DCANGIGALK LREMEHYFSR GLSVLLFNDG
     TQGRLNHLCG ADFVKSQQKP PQGIEMKSGE RCCSFDGDAD RIVYYYCDAD GHFHLIDGDK
     IATLISSFLK ELLLEIGESV NLGVVQTAYA NGSSTRYLEE VMKVPVYCTK TGVKHLHHKA
     QEFDIGVYFE ANGHGTALFS EAVEVKIKRL AQELDDGKGK AARTLASIID LFNQAAGDAI
     SDMLVIEAIL ALKGLTVQQW DAIYVDLPNR QLKVKVADRR VISTTDAERQ AVTPPGLQEA
     INDLVKKYTL ARAFVRPSGT EDIVRVYAEA NSQESADRLA YEVSLLVFQL AGGIGERPQP
     TF
//
ID   CAP2_MOUSE              Reviewed;         476 AA.
AC   Q9CYT6; Q80YU7; Q9D6L0;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Adenylyl cyclase-associated protein 2;
DE            Short=CAP 2;
GN   Name=Cap2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NMRI; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: May have a regulatory bifunctional role.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the CAP family.
CC   -!- SIMILARITY: Contains 1 C-CAP/cofactor C-like domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK010235; BAB26786.1; -; mRNA.
DR   EMBL; AK013331; BAB28795.1; -; mRNA.
DR   EMBL; AK033071; BAC28143.1; -; mRNA.
DR   EMBL; AK035556; BAC29104.1; -; mRNA.
DR   EMBL; BC050752; AAH50752.2; -; mRNA.
DR   EMBL; BC057937; AAH57937.1; -; mRNA.
DR   IPI; IPI00112001; -.
DR   RefSeq; NP_080332.1; NM_026056.4.
DR   UniGene; Mm.44529; -.
DR   ProteinModelPortal; Q9CYT6; -.
DR   SMR; Q9CYT6; 36-220, 323-474.
DR   STRING; Q9CYT6; -.
DR   PhosphoSite; Q9CYT6; -.
DR   PRIDE; Q9CYT6; -.
DR   Ensembl; ENSMUST00000021802; ENSMUSP00000021802; ENSMUSG00000021373.
DR   GeneID; 67252; -.
DR   KEGG; mmu:67252; -.
DR   UCSC; uc007qhf.1; mouse.
DR   CTD; 67252; -.
DR   MGI; MGI:1914502; Cap2.
DR   eggNOG; roNOG13903; -.
DR   GeneTree; ENSGT00390000017955; -.
DR   HOGENOM; HBG444917; -.
DR   HOVERGEN; HBG003080; -.
DR   InParanoid; Q9CYT6; -.
DR   OMA; ELNQGEN; -.
DR   OrthoDB; EOG4HT8SH; -.
DR   PhylomeDB; Q9CYT6; -.
DR   NextBio; 324014; -.
DR   ArrayExpress; Q9CYT6; -.
DR   Bgee; Q9CYT6; -.
DR   Genevestigator; Q9CYT6; -.
DR   GermOnline; ENSMUSG00000021373; Mus musculus.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR   InterPro; IPR001837; Adenylate_cyclase-assoc_CAP.
DR   InterPro; IPR013912; Adenylate_cyclase-assoc_CAP_C.
DR   InterPro; IPR013992; Adenylate_cyclase-assoc_CAP_N.
DR   InterPro; IPR017901; C-CAP_CF_C-like.
DR   InterPro; IPR016098; CAP/MinC_C.
DR   InterPro; IPR018106; CAP_CS.
DR   InterPro; IPR006599; CARP_motif.
DR   Gene3D; G3DSA:2.160.20.70; CAP/MinC_C; 1.
DR   PANTHER; PTHR10652; CAP; 1.
DR   Pfam; PF08603; CAP_C; 1.
DR   Pfam; PF01213; CAP_N; 1.
DR   SMART; SM00673; CARP; 2.
DR   SUPFAM; SSF101278; Adenylate_cyclase-assoc_CAP_N; 1.
DR   SUPFAM; SSF69340; CARP; 1.
DR   PROSITE; PS51329; C_CAP_COFACTOR_C; 1.
DR   PROSITE; PS01088; CAP_1; 1.
DR   PROSITE; PS01089; CAP_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Phosphoprotein.
FT   CHAIN         1    476       Adenylyl cyclase-associated protein 2.
FT                                /FTId=PRO_0000205701.
FT   DOMAIN      317    454       C-CAP/cofactor C-like.
FT   MOD_RES     261    261       Phosphoserine.
FT   MOD_RES     300    300       Phosphoserine (By similarity).
FT   CONFLICT    132    132       H -> D (in Ref. 1; BAB26786).
SQ   SEQUENCE   476 AA;  52862 MW;  318F0E48768FDD1F CRC64;
     MTDMAGLMER LERAVIRLEQ LSAGLDGPPR GCGEVNGVNG GVAPSVEAFD KLINSMVAEF
     LKNSRVLAGD VETHAEMVHG AFQAQRAFLL MVSQYQQPQE NEVAVLLKPI SEKIQEIQTF
     RERNRGSNMF NHLSAVSESI AALGWIAVSP KPGPYVKEMN DAATFYTNRV LKDYKHSDLR
     HVDWVRSYLN IWSELQAYIR EHHTTGLTWS KTGPVASTAS AFSILSSGPG LPPPPPPPPP
     PGPPPPFENE DKKEEPSPSR SALFAQLNQG EAITKGLRHV TDDKKTYKNP SLRAQGQIRS
     PTKTHTPSPT SPKSNSPQKH TPVLELEGKK WRVEYQEDRN DLVISETELK QVAYIFKCDK
     STLQIKGKVN SITVDNCKKF GLVFDHVVGI VEVINSKDIQ IQVMGRVPTI SINKTEGCHL
     YLSEDALDCE IVSAKSSEMN VLVPQDDDYR EFPIPEQFKT IWDGSKLVTE PAEIMA
//
ID   QCR1_MOUSE              Reviewed;         480 AA.
AC   Q9CZ13; Q9CWL6;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Cytochrome b-c1 complex subunit 1, mitochondrial;
DE   AltName: Full=Complex III subunit 1;
DE   AltName: Full=Core protein I;
DE   AltName: Full=Ubiquinol-cytochrome-c reductase complex core protein 1;
DE   Flags: Precursor;
GN   Name=Uqcrc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 59-80; 86-99; 112-134; 143-163; 214-222; 229-248;
RP   256-276; 379-390; 397-442; 448-470 AND 473-479, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [3]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-138 AND LYS-248, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- FUNCTION: This is a component of the ubiquinol-cytochrome c
CC       reductase complex (complex III or cytochrome b-c1 complex), which
CC       is part of the mitochondrial respiratory chain. This protein may
CC       mediate formation of the complex between cytochromes c and c1 (By
CC       similarity).
CC   -!- SUBUNIT: The bc1 complex contains 11 subunits: 3 respiratory
CC       subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core
CC       proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight
CC       proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9,
CC       UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1) (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane (By
CC       similarity).
CC   -!- PTM: Acetylation of Lys-138 is observed in liver mitochondria from
CC       fasted mice but not from fed mice.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. UQCRC1/QCR1
CC       subfamily.
CC   -!- CAUTION: Does not seem to have a protease activity as it lack the
CC       zinc-binding site.
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DR   EMBL; AK013128; BAB28666.1; -; mRNA.
DR   EMBL; AK010553; BAB27022.1; -; mRNA.
DR   IPI; IPI00111885; -.
DR   RefSeq; NP_079683.2; NM_025407.2.
DR   UniGene; Mm.335460; -.
DR   ProteinModelPortal; Q9CZ13; -.
DR   SMR; Q9CZ13; 35-476.
DR   STRING; Q9CZ13; -.
DR   MEROPS; M16.975; -.
DR   MEROPS; M16.981; -.
DR   PhosphoSite; Q9CZ13; -.
DR   REPRODUCTION-2DPAGE; IPI00111885; -.
DR   REPRODUCTION-2DPAGE; Q9CZ13; -.
DR   UCD-2DPAGE; Q9CZ13; -.
DR   PRIDE; Q9CZ13; -.
DR   Ensembl; ENSMUST00000026743; ENSMUSP00000026743; ENSMUSG00000025651.
DR   GeneID; 22273; -.
DR   KEGG; mmu:22273; -.
DR   CTD; 22273; -.
DR   MGI; MGI:107876; Uqcrc1.
DR   GeneTree; ENSGT00550000074701; -.
DR   HOGENOM; HBG476859; -.
DR   HOVERGEN; HBG006393; -.
DR   InParanoid; Q9CZ13; -.
DR   OrthoDB; EOG44BB26; -.
DR   PhylomeDB; Q9CZ13; -.
DR   NextBio; 302387; -.
DR   ArrayExpress; Q9CZ13; -.
DR   Bgee; Q9CZ13; -.
DR   CleanEx; MM_UQCRC1; -.
DR   Genevestigator; Q9CZ13; -.
DR   GermOnline; ENSMUSG00000025651; Mus musculus.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IDA:MGI.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR011249; Metalloenz_metal-bd.
DR   InterPro; IPR011237; Pept_M16_core.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   Gene3D; G3DSA:3.30.830.10; Pept_M16_core; 2.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; Metalloenz_metal-bd; 2.
DR   PROSITE; PS00143; INSULINASE; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW   Respiratory chain; Transit peptide; Transport.
FT   TRANSIT       1     34       Mitochondrion (By similarity).
FT   CHAIN        35    480       Cytochrome b-c1 complex subunit 1,
FT                                mitochondrial.
FT                                /FTId=PRO_0000026787.
FT   MOD_RES     111    111       N6-acetyllysine (By similarity).
FT   MOD_RES     138    138       N6-acetyllysine.
FT   MOD_RES     248    248       N6-acetyllysine.
FT   MOD_RES     381    381       Phosphothreonine (By similarity).
FT   CONFLICT    223    223       N -> H (in Ref. 1; BAB27022).
FT   CONFLICT    318    318       C -> Y (in Ref. 1; BAB27022).
SQ   SEQUENCE   480 AA;  52769 MW;  9C6D480DC9D5E429 CRC64;
     MAASAVCRAA CSGTQVLLRT RRSPALLRLP ALRGTATFAQ ALQSVPETQV SILDNGLRVA
     SEQSSHATCT VGVWIDAGSR YETEKNNGAG YFLEHLAFKG TKNRPGNALE KEVESIGAHL
     NAYSTREHTA YLIKALSKDL PKVVELLADI VQNSSLEDSQ IEKERDVILR EMQENDASMQ
     NVVFDYLHAT AFQGTPLAQA VEGPSENVRR LSRTDLTDYL NRNYKAPRMV LAAAGGVEHQ
     QLLDLAQKHL SSVSRVYEED AVPGLTPCRF TGSEIRHRDD ALPLAHVAIA VEGPGWANPD
     NVTLQVANAI IGHYDCTCGG GVHLSSPLAS VAVANKLCQS FQTFNISYSD TGLLGAHFVC
     DAMSIDDMVF FLQGQWMRLC TSATESEVTR GKNILRNALV SHLDGTTPVC EDIGRSLLTY
     GRRIPLAEWE SRIQEVDAQM LRDICSKYFY DQCPAVAGYG PIEQLPDYNR IRSGMFWLRF
//
ID   Q9CZ22_MOUSE            Unreviewed;       218 AA.
AC   Q9CZ22;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   08-FEB-2011, entry version 46.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Tpd52l2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Whole body;
RA   Adachi J., Aizawa K., Akahira S., Akimura T., Arai A., Aono H.,
RA   Arakawa T., Bono H., Carninci P., Fukuda S., Fukunishi Y., Furuno M.,
RA   Hanagaki T., Hara A., Hayatsu N., Hiramoto K., Hiraoka T., Hori F.,
RA   Imotani K., Ishii Y., Itoh M., Izawa M., Kasukawa T., Kato H.,
RA   Kawai J., Kojima Y., Konno H., Kouda M., Koya S., Kurihara C.,
RA   Matsuyama T., Miyazaki A., Nishi K., Nomura K., Numazaki R., Ohno M.,
RA   Okazaki Y., Okido T., Owa C., Saito H., Saito R., Sakai C., Sakai K.,
RA   Sano H., Sasaki D., Shibata K., Shibata Y., Shinagawa A., Shiraki T.,
RA   Sogabe Y., Suzuki H., Tagami M., Tagawa A., Takahashi F., Tanaka T.,
RA   Tejima Y., Toya T., Yamamura T., Yasunishi A., Yoshida K., Yoshino M.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK013085; BAB28639.1; -; mRNA.
DR   IPI; IPI00319046; -.
DR   UniGene; Mm.136648; -.
DR   STRING; Q9CZ22; -.
DR   Ensembl; ENSMUST00000149163; ENSMUSP00000117690; ENSMUSG00000000827.
DR   MGI; MGI:1913564; Tpd52l2.
DR   GeneTree; ENSGT00390000015988; -.
DR   HOVERGEN; HBG058643; -.
DR   ArrayExpress; Q9CZ22; -.
DR   Bgee; Q9CZ22; -.
DR   Genevestigator; Q9CZ22; -.
DR   InterPro; IPR007327; TPD52.
DR   PANTHER; PTHR19307; TPD52; 1.
DR   Pfam; PF04201; TPD52; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   218 AA;  23859 MW;  81F2897E2BB0AA41 CRC64;
     MDSASQDINL NSPNKGVLSD FMTDVPVDPG VVHRTPVVEG LTEGEEEELR AELAKVEEEI
     VTLRQVLAAK ERHCGELKRR LGLSTLGELK QNLSRSWHDV QVSTAYVKTS EKLGEWNEKV
     TQSDLYKKTQ ETLSQAGQKT SAALSTMGSA ISRKLGDMSS YSIRHSISMP VMRNSATFKS
     FEDRVGTIKS QVVGGRENGS DNLPPGSGDQ TLPDHAPF
//
ID   CARKD_MOUSE             Reviewed;         343 AA.
AC   Q9CZ42; Q9CQX9; Q9D7G7; Q9DC93;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Carbohydrate kinase domain-containing protein;
DE   Flags: Precursor;
GN   Name=Carkd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Brain, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-81, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-81, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9CZ42-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CZ42-2; Sequence=VSP_033831;
CC       Name=3;
CC         IsoId=Q9CZ42-3; Sequence=VSP_033832;
CC   -!- SIMILARITY: Belongs to the YjeF family.
CC   -!- SIMILARITY: Contains 1 YjeF C-terminal domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK003048; BAB22531.1; -; mRNA.
DR   EMBL; AK009254; BAB26172.1; -; mRNA.
DR   EMBL; AK012456; BAB28251.1; -; mRNA.
DR   EMBL; AK013028; BAB28607.1; -; mRNA.
DR   EMBL; AK013069; BAB28632.1; -; mRNA.
DR   EMBL; AK013420; BAB28847.1; -; mRNA.
DR   EMBL; AK154142; BAE32403.1; -; mRNA.
DR   EMBL; AK171034; BAE42200.1; -; mRNA.
DR   EMBL; BC019538; AAH19538.1; -; mRNA.
DR   EMBL; BC021955; AAH21955.1; -; mRNA.
DR   IPI; IPI00112032; -.
DR   IPI; IPI00894581; -.
DR   IPI; IPI00895023; -.
DR   RefSeq; NP_001177286.1; NM_001190357.1.
DR   RefSeq; NP_081271.2; NM_026995.4.
DR   UniGene; Mm.64911; -.
DR   ProteinModelPortal; Q9CZ42; -.
DR   PhosphoSite; Q9CZ42; -.
DR   PRIDE; Q9CZ42; -.
DR   Ensembl; ENSMUST00000033901; ENSMUSP00000033901; ENSMUSG00000031505.
DR   GeneID; 69225; -.
DR   KEGG; mmu:69225; -.
DR   UCSC; uc009kvg.1; mouse.
DR   CTD; 69225; -.
DR   MGI; MGI:1913353; Carkd.
DR   eggNOG; roNOG14531; -.
DR   GeneTree; ENSGT00390000000917; -.
DR   HOGENOM; HBG622920; -.
DR   HOVERGEN; HBG057182; -.
DR   InParanoid; Q9CZ42; -.
DR   OMA; VQKGEQD; -.
DR   OrthoDB; EOG49CQ85; -.
DR   PhylomeDB; Q9CZ42; -.
DR   NextBio; 328919; -.
DR   ArrayExpress; Q9CZ42; -.
DR   Bgee; Q9CZ42; -.
DR   Genevestigator; Q9CZ42; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   InterPro; IPR000631; UPF_carb_kinase-rel.
DR   Pfam; PF01256; Carb_kinase; 1.
DR   TIGRFAMs; TIGR00196; yjeF_cterm; 1.
DR   PROSITE; PS01049; YJEF_C_1; FALSE_NEG.
DR   PROSITE; PS01050; YJEF_C_2; FALSE_NEG.
DR   PROSITE; PS51383; YJEF_C_3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Glycoprotein; Phosphoprotein; Signal.
FT   SIGNAL        1     29       Potential.
FT   CHAIN        30    343       Carbohydrate kinase domain-containing
FT                                protein.
FT                                /FTId=PRO_0000337022.
FT   DOMAIN       49    340       YjeF C-terminal.
FT   MOD_RES      81     81       Phosphotyrosine.
FT   CARBOHYD    236    236       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    293    293       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1     45       Missing (in isoform 2).
FT                                /FTId=VSP_033831.
FT   VAR_SEQ       1     29       MAVHACGAAAAVVALLSAAIALQWSPLYA -> MGFRCVAI
FT                                RACGG (in isoform 3).
FT                                /FTId=VSP_033832.
FT   CONFLICT    203    203       H -> N (in Ref. 1; BAB22531).
SQ   SEQUENCE   343 AA;  36717 MW;  D0202FE6716F80D5 CRC64;
     MAVHACGAAA AVVALLSAAI ALQWSPLYAV LQRALSLHTA HATKDMENLF QLVRNIVPAL
     TSKKHKGQDG RIGIVGGCQE YTGAPYFAGI SALKVGADLT HVFCAREAAP VIKSYSPELI
     VHPVLDSSNA VEEVEKWLPR LHALVVGPGL GRDDLLLNNV RGILESTKAR DIPVVIDADG
     LWLVAQQPAL IHSYHKAILT PNHVEFSRLW EAVLSSPMDS NDLKGSTLKL SQALGNITVV
     QKGEQDLISN GQQVLVCNQE GSSRRCGGQG DLLSGSLGVM VHWALRAGPE KTNGSSPLLV
     AAWGACTLTR ECNRQAFQKY GRSTTTTDMI TEVGTAFSRL FTT
//
ID   NSF1C_MOUSE             Reviewed;         370 AA.
AC   Q9CZ44; A2AT03; Q80Y15; Q8BYL3;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=NSFL1 cofactor p47;
DE   AltName: Full=p97 cofactor p47;
GN   Name=Nsfl1c;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-167, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-140 AND
RP   SER-176, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Reduces the ATPase activity of VCP. Necessary for the
CC       fragmentation of Golgi stacks during mitosis and for VCP-mediated
CC       reassembly of Golgi stacks after mitosis. May play a role in VCP-
CC       mediated formation of transitional endoplasmic reticulum (tER) (By
CC       similarity).
CC   -!- SUBUNIT: Part of a ternary complex containing STX5A, NSFL1C and
CC       VCP. NSFL1C forms a homotrimer that binds to one end of a VCP
CC       homohexamer. The complex binds to membranes enriched in
CC       phosphatidylethanolamine-containing lipids and promotes Golgi
CC       membrane fusion. Interaction with VCIP135 leads to dissociation of
CC       the complex via ATP hydrolysis by VCP. Binds ubiquitin and mono-
CC       ubiquitinated proteins via its N-terminal UBA-like domain when
CC       bound to VCP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Golgi apparatus,
CC       Golgi stack (By similarity). Chromosome (By similarity).
CC       Note=Predominantly nuclear in interphase cells. Bound to the axial
CC       elements of sex chromosomes in pachytene spermatocytes. A small
CC       proportion of the protein is cytoplasmic, associated with Golgi
CC       stacks (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9CZ44-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CZ44-2; Sequence=VSP_009264, VSP_009265, VSP_009266;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q9CZ44-3; Sequence=VSP_009264;
CC   -!- PTM: Phosphorylated during mitosis. Phosphorylation inhibits
CC       interaction with Golgi membranes and is required for the
CC       fragmentation of the Golgi stacks during mitosis (By similarity).
CC   -!- SIMILARITY: Belongs to the NSFL1C family.
CC   -!- SIMILARITY: Contains 1 SEP domain.
CC   -!- SIMILARITY: Contains 1 UBX domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK013024; BAB28604.1; -; mRNA.
DR   EMBL; AK039136; BAC30250.1; -; mRNA.
DR   EMBL; AL928719; CAM23816.1; -; Genomic_DNA.
DR   EMBL; BC050936; AAH50936.1; -; mRNA.
DR   IPI; IPI00387232; -.
DR   IPI; IPI00399449; -.
DR   IPI; IPI00399450; -.
DR   RefSeq; NP_938085.1; NM_198326.2.
DR   UniGene; Mm.419479; -.
DR   ProteinModelPortal; Q9CZ44; -.
DR   SMR; Q9CZ44; 1-46, 171-246, 253-370.
DR   STRING; Q9CZ44; -.
DR   PhosphoSite; Q9CZ44; -.
DR   REPRODUCTION-2DPAGE; Q9CZ44; -.
DR   PRIDE; Q9CZ44; -.
DR   Ensembl; ENSMUST00000028949; ENSMUSP00000028949; ENSMUSG00000027455.
DR   Ensembl; ENSMUST00000089140; ENSMUSP00000086542; ENSMUSG00000027455.
DR   GeneID; 386649; -.
DR   KEGG; mmu:386649; -.
DR   UCSC; uc008ndw.1; mouse.
DR   CTD; 386649; -.
DR   MGI; MGI:3042273; Nsfl1c.
DR   GeneTree; ENSGT00520000055567; -.
DR   HOVERGEN; HBG054517; -.
DR   OMA; GQRFYAG; -.
DR   OrthoDB; EOG4K6G4D; -.
DR   PhylomeDB; Q9CZ44; -.
DR   Bgee; Q9CZ44; -.
DR   CleanEx; MM_NSFL1C; -.
DR   Genevestigator; Q9CZ44; -.
DR   GermOnline; ENSMUSG00000027455; Mus musculus.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR012989; SEP_domain.
DR   InterPro; IPR009060; UBA-like.
DR   InterPro; IPR001012; UBX.
DR   Pfam; PF08059; SEP; 1.
DR   Pfam; PF00789; UBX; 1.
DR   SMART; SM00553; SEP; 1.
DR   SMART; SM00166; UBX; 1.
DR   SUPFAM; SSF102848; SEP; 1.
DR   SUPFAM; SSF46934; UBA_like; 1.
DR   PROSITE; PS51399; SEP; 1.
DR   PROSITE; PS50033; UBX; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromosome; Golgi apparatus; Lipid-binding;
KW   Nucleus; Phosphoprotein.
FT   CHAIN         1    370       NSFL1 cofactor p47.
FT                                /FTId=PRO_0000210989.
FT   DOMAIN      179    244       SEP.
FT   DOMAIN      291    368       UBX.
FT   MOTIF       109    115       Nuclear localization signal.
FT   MOTIF       172    175       Nuclear localization signal.
FT   COMPBIAS     84     90       Poly-Glu.
FT   MOD_RES      74     74       Phosphoserine.
FT   MOD_RES     114    114       Phosphoserine.
FT   MOD_RES     140    140       Phosphoserine.
FT   MOD_RES     165    165       Phosphoserine (By similarity).
FT   MOD_RES     167    167       Phosphotyrosine.
FT   MOD_RES     176    176       Phosphoserine.
FT   MOD_RES     272    272       Phosphoserine (By similarity).
FT   VAR_SEQ      93     93       R -> RSR (in isoform 2 and isoform 3).
FT                                /FTId=VSP_009264.
FT   VAR_SEQ     262    262       S -> R (in isoform 2).
FT                                /FTId=VSP_009265.
FT   VAR_SEQ     263    370       Missing (in isoform 2).
FT                                /FTId=VSP_009266.
FT   CONFLICT     13     13       V -> A (in Ref. 1; BAC30250).
SQ   SEQUENCE   370 AA;  40710 MW;  32C9C20F82125D58 CRC64;
     MAEERQDALR EFVAVTGTEE DRARFFLESA GWDLQIALAS FYEDGGDEDI VTISQATPSS
     VSRGTAPSDN RVTSFRDLIH DQDEEEEEEE GQRFYAGGSE RSGQQIVGPP RKKSPNELVD
     DLFKGAKEHG AVAVERVTKS PGETSKPRPF AGGGYRLGAA PEEESAYVAG ERRRHSGQDV
     HVVLKLWKTG FSLDNGDLRS YQDPSNAQFL ESIRRGEVPA ELRRLAHGGQ VNLDMEDHRD
     EDFVKPKGAF KAFTGEGQKL GSTAPQVLNT SSPAQQAENE AKASSSILIN EAEPTTNIQI
     RLADGGRLVQ KFNHSHRISD IRLFIVDARP AMAATSFVLM TTFPNKELAD ENQTLKEANL
     LNAVIVQRLT
//
ID   RM55_MOUSE              Reviewed;         127 AA.
AC   Q9CZ83; Q8R030;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 50.
DE   RecName: Full=39S ribosomal protein L55, mitochondrial;
DE            Short=L55mt;
DE            Short=MRP-L55;
DE   Flags: Precursor;
GN   Name=Mrpl55;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBUNIT: Component of the mitochondrial ribosome large subunit
CC       (39S) which comprises a 16S rRNA and about 50 distinct proteins
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9CZ83-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CZ83-2; Sequence=VSP_022478;
CC         Note=No experimental confirmation available;
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DR   EMBL; AK012885; BAB28535.1; -; mRNA.
DR   EMBL; BC028538; AAH28538.1; -; mRNA.
DR   IPI; IPI00336870; -.
DR   IPI; IPI00648969; -.
DR   RefSeq; NP_080311.1; NM_026035.2.
DR   UniGene; Mm.282694; -.
DR   Ensembl; ENSMUST00000045697; ENSMUSP00000048814; ENSMUSG00000036860.
DR   Ensembl; ENSMUST00000108784; ENSMUSP00000104412; ENSMUSG00000036860.
DR   Ensembl; ENSMUST00000108785; ENSMUSP00000104413; ENSMUSG00000036860.
DR   Ensembl; ENSMUST00000116374; ENSMUSP00000112075; ENSMUSG00000036860.
DR   GeneID; 67212; -.
DR   KEGG; mmu:67212; -.
DR   NMPDR; fig|10090.3.peg.23793; -.
DR   UCSC; uc007jdj.1; mouse.
DR   UCSC; uc007jdk.1; mouse.
DR   CTD; 67212; -.
DR   MGI; MGI:1914462; Mrpl55.
DR   eggNOG; roNOG16705; -.
DR   GeneTree; ENSGT00390000010309; -.
DR   HOVERGEN; HBG080171; -.
DR   OMA; PRRMLAM; -.
DR   OrthoDB; EOG4DJJZ7; -.
DR   PhylomeDB; Q9CZ83; -.
DR   NextBio; 323894; -.
DR   ArrayExpress; Q9CZ83; -.
DR   Bgee; Q9CZ83; -.
DR   CleanEx; MM_MRPL55; -.
DR   Genevestigator; Q9CZ83; -.
DR   GO; GO:0005762; C:mitochondrial large ribosomal subunit; ISS:UniProtKB.
DR   GO; GO:0003735; F:structural constituent of ribosome; ISS:UniProtKB.
DR   GO; GO:0006412; P:translation; ISS:UniProtKB.
DR   InterPro; IPR018615; Ribosomal_L55_mit.
DR   Pfam; PF09776; Mitoc_L55; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Mitochondrion; Ribonucleoprotein;
KW   Ribosomal protein; Transit peptide.
FT   TRANSIT       1     32       Mitochondrion (Potential).
FT   CHAIN        33    127       39S ribosomal protein L55, mitochondrial.
FT                                /FTId=PRO_0000273100.
FT   VAR_SEQ       7      7       L -> LSACTSVR (in isoform 2).
FT                                /FTId=VSP_022478.
FT   CONFLICT     18     18       A -> P (in Ref. 2; AAH28538).
SQ   SEQUENCE   127 AA;  15122 MW;  A4ED7AA477DD0605 CRC64;
     MPLAILLSLL RHCGVRAALP TPRHLHTSPW RADCSRASLT RLRRQAYARL YPVLLVKQDG
     STIHIRYREP RRMLAMPLDL DALSPEERRA RFRKREAQLQ QKREEEPEVV DSFDTERYKQ
     FWTKTKK
//
ID   SCRN1_MOUSE             Reviewed;         414 AA.
AC   Q9CZC8; Q3UKR2; Q8CCL3;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Secernin-1;
GN   Name=Scrn1; Synonyms=Kiaa0193;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Pancreas, Placenta, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 33-51 AND 262-302, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
CC   -!- FUNCTION: Regulates exocytosis in mast cells. Increases both the
CC       extent of secretion and the sensitivity of mast cells to
CC       stimulation with calcium (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- MISCELLANEOUS: 'Secern' is an archaic English term meaning
CC       'secrete'.
CC   -!- SIMILARITY: Belongs to the peptidase C69 family. Secernin
CC       subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97894.1; Type=Erroneous initiation;
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DR   EMBL; AK012765; BAB28453.1; -; mRNA.
DR   EMBL; AK032573; BAC27931.1; -; mRNA.
DR   EMBL; AK050481; BAC34280.1; -; mRNA.
DR   EMBL; AK082953; BAC38706.1; -; mRNA.
DR   EMBL; AK145904; BAE26739.1; -; mRNA.
DR   EMBL; AK129084; BAC97894.1; ALT_INIT; mRNA.
DR   EMBL; BC023889; AAH23889.1; -; mRNA.
DR   IPI; IPI00112536; -.
DR   RefSeq; NP_081544.1; NM_027268.2.
DR   UniGene; Mm.41557; -.
DR   ProteinModelPortal; Q9CZC8; -.
DR   STRING; Q9CZC8; -.
DR   MEROPS; C69.003; -.
DR   PhosphoSite; Q9CZC8; -.
DR   PRIDE; Q9CZC8; -.
DR   Ensembl; ENSMUST00000019268; ENSMUSP00000019268; ENSMUSG00000019124.
DR   GeneID; 69938; -.
DR   KEGG; mmu:69938; -.
DR   UCSC; uc009bzw.1; mouse.
DR   CTD; 69938; -.
DR   MGI; MGI:1917188; Scrn1.
DR   eggNOG; roNOG08098; -.
DR   GeneTree; ENSGT00390000013474; -.
DR   HOGENOM; HBG430518; -.
DR   HOVERGEN; HBG056050; -.
DR   InParanoid; Q9CZC8; -.
DR   OMA; AFPPRTK; -.
DR   OrthoDB; EOG4GF3F4; -.
DR   PhylomeDB; Q9CZC8; -.
DR   NextBio; 330643; -.
DR   ArrayExpress; Q9CZC8; -.
DR   Bgee; Q9CZC8; -.
DR   CleanEx; MM_SCRN1; -.
DR   Genevestigator; Q9CZC8; -.
DR   GermOnline; ENSMUSG00000019124; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:InterPro.
DR   GO; GO:0006887; P:exocytosis; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR005322; Peptidase_C69.
DR   Pfam; PF03577; Peptidase_C69; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Exocytosis.
FT   CHAIN         1    414       Secernin-1.
FT                                /FTId=PRO_0000221437.
FT   CONFLICT    127    127       L -> I (in Ref. 1; BAE26739).
FT   CONFLICT    391    391       E -> K (in Ref. 1; BAC27931).
SQ   SEQUENCE   414 AA;  46326 MW;  F5C530AC5562D3BA CRC64;
     MSGAPPSYSF VALPPRAKDG LVVFGKNSAR PRDEVQEVVY FPAVDHDAES KVECTYISID
     QVPRTHAIVI SRPAWLWGAE MGANEHGVCI ANEAINAREP AAETEALLGM DLVRLGLERG
     TTAKEALDII VSLLDEHGQG GNYYEDAHSC HSFQSAYLLV DRDEAWVLET VGKYWAAERI
     TEGVRCICNH LSLATKLDEE HPELRTYAQS QGWWTGDDEF NFAQVFSPAD DRLDCCAGQD
     SLEKQEESIT VQTMINILRD KASGVCIDSE SFLTTASIVS VLPQNRSSPC IHYFTGTPDP
     SRSIFKPFIF VDDVKLVPKA QSPCFGDDDP AKKEPRFQEK PDRRHELYKA HEWARAVIES
     DEEQGRTLRK TMLELEKQGL EAMDEILSSP EPPDPAEVGD LFYDCVDTEM KFFK
//
ID   MXRA7_MOUSE             Reviewed;         178 AA.
AC   Q9CZH7; A2AA24; B2RVR9; Q8C6F8;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Matrix-remodeling-associated protein 7;
DE   AltName: Full=Transmembrane anchor protein 1;
GN   Name=Mxra7; Synonyms=Tmap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -----------------------------------------------------------------------
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DR   EMBL; AK012601; BAB28347.1; -; mRNA.
DR   EMBL; AK075801; BAC35969.1; -; mRNA.
DR   EMBL; AL645542; CAM25278.1; -; Genomic_DNA.
DR   EMBL; BC147320; AAI47321.1; -; mRNA.
DR   EMBL; BC147321; AAI47322.1; -; mRNA.
DR   IPI; IPI00226263; -.
DR   RefSeq; NP_080556.1; NM_026280.3.
DR   UniGene; Mm.479270; -.
DR   UniGene; Mm.64962; -.
DR   ProteinModelPortal; Q9CZH7; -.
DR   PRIDE; Q9CZH7; -.
DR   Ensembl; ENSMUST00000021170; ENSMUSP00000021170; ENSMUSG00000020814.
DR   GeneID; 67622; -.
DR   KEGG; mmu:67622; -.
DR   UCSC; uc007mmf.1; mouse.
DR   CTD; 67622; -.
DR   MGI; MGI:1914872; Mxra7.
DR   eggNOG; maNOG21585; -.
DR   GeneTree; ENSGT00530000064433; -.
DR   HOVERGEN; HBG070029; -.
DR   InParanoid; Q9CZH7; -.
DR   OMA; MESAAEY; -.
DR   OrthoDB; EOG4BZN43; -.
DR   NextBio; 325069; -.
DR   ArrayExpress; Q9CZH7; -.
DR   Bgee; Q9CZH7; -.
DR   CleanEx; MM_MXRA7; -.
DR   Genevestigator; Q9CZH7; -.
DR   GermOnline; ENSMUSG00000020814; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    178       Matrix-remodeling-associated protein 7.
FT                                /FTId=PRO_0000239449.
FT   TRANSMEM      7     27       Helical; (Potential).
FT   MOD_RES      79     79       Phosphoserine.
FT   MOD_RES      94     94       Phosphoserine.
FT   CONFLICT     75     76       EP -> DA (in Ref. 1; BAB28347).
SQ   SEQUENCE   178 AA;  19458 MW;  85F1FADBF44C4495 CRC64;
     MESPVELLAA LPALVTALAL LLAWLLLRRG AARVPAPEST ASDEAPGAPA PPEPPESCAP
     EPAPEGPSQS ERVAEPEESE AEEPAAEGRQ DEDSDSEMGP PTEEPEEEDG AAFSFKYSPG
     QLRGSQYKKM MTKEELEEEH RVQKEQLAAI FKLMKDNKDT FGEMSDGDMQ EQLRLYDM
//
ID   HS12B_MOUSE             Reviewed;         685 AA.
AC   Q9CZJ2;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Heat shock 70 kDa protein 12B;
GN   Name=Hspa12b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 577-591, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   IDENTIFICATION, AND TISSUE SPECIFICITY.
RX   MEDLINE=22457227; PubMed=12552099; DOI=10.1073/pnas.252764399;
RA   Han Z., Truong Q.A., Park S., Breslow J.L.;
RT   "Two Hsp70 family members expressed in atherosclerotic lesions.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1256-1261(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- TISSUE SPECIFICITY: Expressed most strongly in heart with little
CC       or no expression in other tissues. In the aorta, preferentially
CC       expressed in lesions.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
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DR   EMBL; AK012548; BAB28308.1; -; mRNA.
DR   EMBL; BC011103; AAH11103.1; -; mRNA.
DR   EMBL; AY196790; AAO37639.1; -; mRNA.
DR   IPI; IPI00224776; -.
DR   RefSeq; NP_082582.1; NM_028306.3.
DR   UniGene; Mm.277465; -.
DR   ProteinModelPortal; Q9CZJ2; -.
DR   PhosphoSite; Q9CZJ2; -.
DR   PRIDE; Q9CZJ2; -.
DR   Ensembl; ENSMUST00000099349; ENSMUSP00000096950; ENSMUSG00000074793.
DR   GeneID; 72630; -.
DR   KEGG; mmu:72630; -.
DR   UCSC; uc008mkr.1; mouse.
DR   CTD; 72630; -.
DR   MGI; MGI:1919880; Hspa12b.
DR   GeneTree; ENSGT00390000014360; -.
DR   HOGENOM; HBG282805; -.
DR   HOVERGEN; HBG051928; -.
DR   InParanoid; Q9CZJ2; -.
DR   OMA; INLYCCA; -.
DR   OrthoDB; EOG4HX50H; -.
DR   PhylomeDB; Q9CZJ2; -.
DR   NextBio; 336623; -.
DR   ArrayExpress; Q9CZJ2; -.
DR   Bgee; Q9CZJ2; -.
DR   CleanEx; MM_HSPA12B; -.
DR   Genevestigator; Q9CZJ2; -.
DR   GermOnline; ENSMUSG00000074793; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   PROSITE; PS00297; HSP70_1; FALSE_NEG.
DR   PROSITE; PS00329; HSP70_2; FALSE_NEG.
DR   PROSITE; PS01036; HSP70_3; FALSE_NEG.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Nucleotide-binding;
KW   Phosphoprotein.
FT   CHAIN         1    685       Heat shock 70 kDa protein 12B.
FT                                /FTId=PRO_0000078295.
FT   MOD_RES      42     42       Phosphothreonine.
FT   MOD_RES     666    666       Phosphothreonine (By similarity).
SQ   SEQUENCE   685 AA;  76119 MW;  641FE753180EBE2B CRC64;
     MLTVPEMGLQ GLYISSSPER SPVPSPPGSP RTQESCGIAP LTPSQSPKPE ARALQQASFS
     VVVAIDFGTT SSGYAFSFAS DPEAIHMMRK WEGGDPGVAH QKTPTCLLLT PEGIFHSFGY
     TARDYYHDLD PEEARDWLYF EKFKMKIHSA TDLTLKTQLE AVNGKKMLAL EVFAHALRFF
     KEHALQELRE QSECMLEKGA VRWVLTVPAI WKQPAKQFMR EAAYLAGLVS REDAEKLLIA
     LEPEAASVYC RKLRLHQLMD LSSRTAGRGR LGERRSIDSS FRHAREQLRR SRHSRTFLVE
     AGVGELWAEM QEGDRYMVAD CGGGTVDLTV HQLEQPHGTL KELYKASGGP YGAVGVDLAF
     EQLLCRIFGE DFIAKFKRQR PAAWVDLTIA FEARKRTAGP HRAGALNISL PFSFIDFYRK
     QRGHNVETAL RRSSVNLVKW SSQGMLRMSC EAMNELFQPT VSGIIQHIEM LLAKPEVQGV
     KLLFLVGGFA ESAVLQHAVQ EALGTRGLRV VVPHDVGLTI LKGAVLFGQA PGVVRVRRSP
     LTYGVGVLNR FVPGHHPPEK LLVRDGRRWC TDVFERFVAA EQSVALGEEV RRSYCPARPG
     QRRVLINLYC CAAEDARFIT DPGVRKCGAL SLELEPEGCP ENTGTSPSRR EIRAAMQFGD
     TEIKVTAVDV STNRSVRAAI DFLSN
//
ID   SHSA9_MOUSE             Reviewed;         424 AA.
AC   Q9CZN4; D4NZG2; D4NZG3;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Protein shisa-9;
DE   AltName: Full=Cystine-knot AMPAR modulating protein of 44 kDa;
DE            Short=CKAMP44;
DE   Flags: Precursor;
GN   Name=Shisa9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), FUNCTION,
RP   IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A AMPA RECEPTOR
RP   COMPLEX, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=20185686; DOI=10.1126/science.1184178;
RA   von Engelhardt J., Mack V., Sprengel R., Kavenstock N., Li K.W.,
RA   Stern-Bach Y., Smit A.B., Seeburg P.H., Monyer H.;
RT   "CKAMP44: A brain-specific protein attenuating short-term synaptic
RT   plasticity in the dentate gyrus.";
RL   Science 327:1518-1522(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Regulator of short-term neuronal synaptic plasticity in
CC       the dentate gyrus. Associates with AMPA receptors (ionotropic
CC       glutamate receptors) in synaptic spines and promotes AMPA receptor
CC       desensitization at excitatory synapses.
CC   -!- SUBUNIT: Component of some AMPA receptors (ionotropic glutamate
CC       receptors) complex, at least composed of some AMPA receptor
CC       (GRIA1, GRIA2 and/or GRIA3), CACNG2 and SHISA9, as well as low
CC       level of DLG4.
CC   -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine membrane;
CC       Single-pass type I membrane protein. Cell junction, synapse.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9CZN4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CZN4-2; Sequence=VSP_039229, VSP_039230;
CC         Note=No experimental confirmation available;
CC       Name=3; Synonyms=Ckamp44a;
CC         IsoId=Q9CZN4-3; Sequence=VSP_039231;
CC       Name=4; Synonyms=Ckamp44b;
CC         IsoId=Q9CZN4-4; Sequence=VSP_039231, VSP_039232;
CC   -!- TISSUE SPECIFICITY: Brain-specific. Mainly expressed in neurons,
CC       including in hippocampus, cerebral cortex, striatum, thalamus,
CC       olfactory bulb and cerebellum. Expressed in most brain structures
CC       during embryonic and postnatal development.
CC   -!- DOMAIN: The extracellular domain contains a pattern of cysteine
CC       similar to the snail conotoxin Con-ikot-ikot (AC P0CB20), a toxin
CC       known to disrupt AMPA receptors (ionotropic glutamate receptor)
CC       desensitization (PubMed:20185686).
CC   -!- DISRUPTION PHENOTYPE: Induces an increase in the paired-pulse
CC       ratio of AMPA currents in lateral and medial perforant path-
CC       granule cell synapses.
CC   -!- SIMILARITY: Belongs to the shisa family. SHISA9 subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB28201.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC   -----------------------------------------------------------------------
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DR   EMBL; GU479981; ADD64956.1; -; mRNA.
DR   EMBL; GU479982; ADD64957.1; -; mRNA.
DR   EMBL; AC154289; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC129020; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK012380; BAB28201.1; ALT_INIT; mRNA.
DR   IPI; IPI00808044; -.
DR   IPI; IPI00956857; -.
DR   IPI; IPI00968396; -.
DR   IPI; IPI00968411; -.
DR   RefSeq; NP_082553.2; NM_028277.2.
DR   UniGene; Mm.310139; -.
DR   Ensembl; ENSMUST00000023138; ENSMUSP00000023138; ENSMUSG00000022494.
DR   GeneID; 72555; -.
DR   KEGG; mmu:72555; -.
DR   UCSC; uc007yfr.1; mouse.
DR   CTD; 72555; -.
DR   MGI; MGI:1919805; Shisa9.
DR   eggNOG; roNOG15045; -.
DR   GeneTree; ENSGT00510000047247; -.
DR   HOGENOM; HBG715189; -.
DR   InParanoid; Q9CZN4; -.
DR   OrthoDB; EOG4VHK6X; -.
DR   ArrayExpress; Q9CZN4; -.
DR   Bgee; Q9CZN4; -.
DR   Genevestigator; Q9CZN4; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0032591; C:dendritic spine membrane; IDA:UniProtKB.
DR   GO; GO:0008328; C:ionotropic glutamate receptor complex; IDA:UniProtKB.
DR   GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR   GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW   Glycoprotein; Membrane; Signal; Synapse; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     23       Potential.
FT   CHAIN        24    424       Protein shisa-9.
FT                                /FTId=PRO_0000394254.
FT   TOPO_DOM     24    149       Extracellular (Potential).
FT   TRANSMEM    150    170       Helical; (Potential).
FT   TOPO_DOM    171    424       Cytoplasmic (Potential).
FT   CARBOHYD     45     45       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     89     89       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    116    116       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     189    194       ALADVM -> RIQRSF (in isoform 2).
FT                                /FTId=VSP_039229.
FT   VAR_SEQ     195    424       Missing (in isoform 2).
FT                                /FTId=VSP_039230.
FT   VAR_SEQ     231    231       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_039231.
FT   VAR_SEQ     283    298       Missing (in isoform 4).
FT                                /FTId=VSP_039232.
SQ   SEQUENCE   424 AA;  46842 MW;  0DE039C1C29E9947 CRC64;
     MRRVLRLLLG CFLTELCARM CRAQERSGHG QLAQLGGVLL LTGGNRSGAA SGEAGEGVGG
     SDAPPTRAPT PDSCRGYFDV MGQWDPPFNC SSGDFIFCCG TCGFRFCCTF KKRRLNQSTC
     TNYDTPLWLN TGKPPARKDD PLHDPTKDKT NLIVYIICGV VAVMVLVGIF TKLGLEKAHR
     PQREHMSRAL ADVMRPQGHC NTDHMERDLN IVVHVQHYEN MDSRTPINNL HTTQMNNAVP
     TSPLLQQMGH PHSYPNLGQI SNPYEQQPPG KELNKYASLK AVGNSDGDWA VATLKSPKAD
     KVNDDFYAKR RHLAELAVKG NLPLHPVRVE DEPRAFSPEH GPAQQNGQKS RTNKMPPHPL
     AYNSTANFKT WDPSDQSLRR QAYGNKGKLG IAESGSCDPL GTRTQHFPPT QPYFITNSKT
     EVTV
//
ID   RAB3B_MOUSE             Reviewed;         219 AA.
AC   Q9CZT8; Q80WV9; Q920F1;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Ras-related protein Rab-3B;
GN   Name=Rab3b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129/SvOla; TISSUE=Brain;
RA   Schluter O.M., Benseler F., Suedhof T.C.;
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 25-35; 73-83; 122-136 AND 179-186, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Protein transport. Probably involved in vesicular
CC       traffic (By similarity).
CC   -!- SUBUNIT: Binds RIMS1 and RIMS2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
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DR   EMBL; AF312036; AAG60046.1; -; mRNA.
DR   EMBL; AF307514; AAL09395.1; -; Genomic_DNA.
DR   EMBL; AK012165; BAB28071.1; -; mRNA.
DR   EMBL; AK082959; BAC38710.1; -; mRNA.
DR   EMBL; BC051918; AAH51918.2; -; mRNA.
DR   EMBL; BC057173; AAH57173.1; -; mRNA.
DR   IPI; IPI00113112; -.
DR   RefSeq; NP_076026.1; NM_023537.5.
DR   UniGene; Mm.41580; -.
DR   ProteinModelPortal; Q9CZT8; -.
DR   SMR; Q9CZT8; 18-187.
DR   MINT; MINT-1341069; -.
DR   STRING; Q9CZT8; -.
DR   PhosphoSite; Q9CZT8; -.
DR   PRIDE; Q9CZT8; -.
DR   Ensembl; ENSMUST00000003502; ENSMUSP00000003502; ENSMUSG00000003411.
DR   Ensembl; ENSMUST00000106650; ENSMUSP00000102261; ENSMUSG00000003411.
DR   GeneID; 69908; -.
DR   KEGG; mmu:69908; -.
DR   UCSC; uc008ubu.1; mouse.
DR   CTD; 69908; -.
DR   MGI; MGI:1917158; Rab3b.
DR   GeneTree; ENSGT00600000084147; -.
DR   HOVERGEN; HBG009351; -.
DR   PhylomeDB; Q9CZT8; -.
DR   NextBio; 330587; -.
DR   ArrayExpress; Q9CZT8; -.
DR   Bgee; Q9CZT8; -.
DR   CleanEx; MM_RAB3B; -.
DR   Genevestigator; Q9CZT8; -.
DR   GermOnline; ENSMUSG00000003411; Mus musculus.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0018125; P:peptidyl-cysteine methylation; IDA:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0017157; P:regulation of exocytosis; IDA:MGI.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; GTP-binding; Lipoprotein;
KW   Membrane; Methylation; Nucleotide-binding; Phosphoprotein;
KW   Prenylation; Protein transport; Transport.
FT   CHAIN         1    219       Ras-related protein Rab-3B.
FT                                /FTId=PRO_0000121082.
FT   NP_BIND      29     37       GTP (By similarity).
FT   NP_BIND      77     81       GTP (By similarity).
FT   NP_BIND     135    138       GTP (By similarity).
FT   NP_BIND     165    167       GTP (By similarity).
FT   MOTIF        51     59       Effector region (By similarity).
FT   MOD_RES     188    188       Phosphoserine.
FT   MOD_RES     219    219       Cysteine methyl ester (By similarity).
FT   LIPID       217    217       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   LIPID       219    219       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   219 AA;  24757 MW;  494B3A0686D325C8 CRC64;
     MASVTDGKTG IKDASDQNFD YMFKLLIIGN SSVGKTSFLF RYADDTFTPA FVSTVGIDFK
     VKTVYRHEKR VKLQIWDTAG QERYRTITTA YYRGAMGFIL MYDITNEESF NAVQDWATQI
     KTYSWDNAQV ILVGNKCDME EERVVPTEKG RLLAEQLGFD FFEASAKENI SVRQAFERLV
     DAICDKMSDS MDTDPSVLGA SKTTRLSDTP PLLQQNCSC
//
ID   CISY_MOUSE              Reviewed;         464 AA.
AC   Q9CZU6; Q3UDP3;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Citrate synthase, mitochondrial;
DE            EC=2.3.3.1;
DE   Flags: Precursor;
GN   Name=Cs;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Sone H., Shimano H., Yamada N.;
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Egg;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N, and FVB/N-3; TISSUE=Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 35-43; 58-73; 77-92; 223-256; 328-351; 376-393 AND
RP   429-450, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O + oxaloacetate = citrate +
CC       CoA.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       isocitrate from oxaloacetate: step 1/2.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- MISCELLANEOUS: Citrate synthase is found in nearly all cells
CC       capable of oxidative metabolism.
CC   -!- SIMILARITY: Belongs to the citrate synthase family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB056479; BAB63945.1; -; mRNA.
DR   EMBL; AK012151; BAB28063.1; -; mRNA.
DR   EMBL; AK145643; BAE26560.1; -; mRNA.
DR   EMBL; AK149990; BAE29218.1; -; mRNA.
DR   EMBL; AK163273; BAE37268.1; -; mRNA.
DR   EMBL; AK166814; BAE39041.1; -; mRNA.
DR   EMBL; AK167125; BAE39273.1; -; mRNA.
DR   EMBL; BC013554; AAH13554.1; -; mRNA.
DR   EMBL; BC029754; AAH29754.1; -; mRNA.
DR   IPI; IPI00113141; -.
DR   RefSeq; NP_080720.1; NM_026444.3.
DR   UniGene; Mm.392905; -.
DR   UniGene; Mm.58836; -.
DR   ProteinModelPortal; Q9CZU6; -.
DR   SMR; Q9CZU6; 28-464.
DR   STRING; Q9CZU6; -.
DR   PhosphoSite; Q9CZU6; -.
DR   PRIDE; Q9CZU6; -.
DR   Ensembl; ENSMUST00000005826; ENSMUSP00000005826; ENSMUSG00000005683.
DR   GeneID; 12974; -.
DR   KEGG; mmu:12974; -.
DR   NMPDR; fig|10090.3.peg.23025; -.
DR   UCSC; uc007hmj.1; mouse.
DR   CTD; 12974; -.
DR   MGI; MGI:88529; Cs.
DR   GeneTree; ENSGT00390000006813; -.
DR   HOGENOM; HBG309523; -.
DR   HOVERGEN; HBG005336; -.
DR   InParanoid; Q9CZU6; -.
DR   OMA; WELIYED; -.
DR   OrthoDB; EOG4FBHSR; -.
DR   PhylomeDB; Q9CZU6; -.
DR   BRENDA; 2.3.3.1; 244.
DR   NextBio; 282742; -.
DR   ArrayExpress; Q9CZU6; -.
DR   Bgee; Q9CZU6; -.
DR   CleanEx; MM_CS; -.
DR   Genevestigator; Q9CZU6; -.
DR   GermOnline; ENSMUSG00000005683; Mus musculus.
DR   GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR   GO; GO:0004108; F:citrate (Si)-synthase activity; ISS:UniProtKB.
DR   GO; GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR   InterPro; IPR002020; Citrate_synthase-like.
DR   InterPro; IPR016141; Citrate_synthase-like_core.
DR   InterPro; IPR019810; Citrate_synthase_AS.
DR   InterPro; IPR010109; Citrate_synthase_euk.
DR   Gene3D; G3DSA:1.10.580.10; Citrate_synthase_lrg_a-sub; 1.
DR   PANTHER; PTHR11739; Citrate_synth; 1.
DR   Pfam; PF00285; Citrate_synt; 1.
DR   PRINTS; PR00143; CITRTSNTHASE.
DR   SUPFAM; SSF48256; Citrate_synthase_core; 1.
DR   TIGRFAMs; TIGR01793; cit_synth_euk; 1.
DR   PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Mitochondrion; Transferase;
KW   Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT       1     27       Mitochondrion (By similarity).
FT   CHAIN        28    464       Citrate synthase, mitochondrial.
FT                                /FTId=PRO_0000005472.
FT   ACT_SITE    301    301       By similarity.
FT   ACT_SITE    347    347       By similarity.
FT   ACT_SITE    402    402       By similarity.
FT   MOD_RES     327    327       N6-acetyllysine (By similarity).
FT   MOD_RES     366    366       N6-acetyllysine (By similarity).
FT   MOD_RES     375    375       N6-acetyllysine (By similarity).
FT   MOD_RES     382    382       N6-acetyllysine (By similarity).
FT   MOD_RES     393    393       N6-acetyllysine (By similarity).
SQ   SEQUENCE   464 AA;  51737 MW;  710639871C31EED5 CRC64;
     MALLTAATRL LGAKNSSCLV LAARHASASS TNLKDVLSNL IPKEQARIKT FKQQHGKTVV
     GQITVDMMYG GMRGMKGLVY ETSVLDPDEG IRFRGYSIPE CQKMLPKAKG GEEPLPEGLF
     WLLVTGQMPT EEQVSWLSRE WAKRAALPSH VVTMLDNFPT NLHPMSQLSA AITALNSESN
     FARAYAEGMN RAKYWELIYE DCMDLIAKLP CVAAKIYRNL YREGSSIGAI DSRLDWSHNF
     TNMLGYTDPQ FTELMRLYLT IHSDHEGGNV SAHTSHLVGS ALSDPYLSFA AAMNGLAGPL
     HGLANQEVLV WLTQLQKEVG KDVSDEKLRD YIWNTLNSGR VVPGYGHAVL RKTDPRYSCQ
     REFALKHLPK DPMFKLVAQL YKIVPNILLE QGKAKNPWPN VDAHSGVLLQ YYGMTEMNYY
     TVLFGVSRAL GVLAQLIWSR ALGFPLERPK SMSTDGLMKF VDSK
//
ID   FXL20_MOUSE             Reviewed;         436 AA.
AC   Q9CZV8; A7YE80; Q3UMN2; Q571F7; Q8BZ95;
DT   21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 3.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=F-box/LRR-repeat protein 20;
DE   AltName: Full=F-box and leucine-rich repeat protein 20;
DE   AltName: Full=F-box/LRR-repeat protein 2-like;
GN   Name=Fbxl20; Synonyms=Fbl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, INTERACTION WITH RIMS1; SKP1 AND CUL1,
RP   AND DISRUPTION PHENOTYPE.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=17803915; DOI=10.1016/j.cell.2007.06.052;
RA   Yao I., Takagi H., Ageta H., Kahyo T., Sato S., Hatanaka K.,
RA   Fukuda Y., Chiba T., Morone N., Yuasa S., Inokuchi K., Ohtsuka T.,
RA   Macgregor G.R., Tanaka K., Setou M.;
RT   "SCRAPPER-dependent ubiquitination of active zone protein RIM1
RT   regulates synaptic vesicle release.";
RL   Cell 130:943-957(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Natural killer cell;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-417 AND SER-421, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-417, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-
CC       box protein)-type E3 ubiquitin ligase complex. Isoform 3 regulates
CC       neural transmission by binding and ubiquitinating RIMS1, a
CC       modulator of presynaptic plasticity.
CC   -!- SUBUNIT: Interacts with SKP1A and CUL1.
CC   -!- INTERACTION:
CC       Q99NE5:Rims1; NbExp=2; IntAct=EBI-1551033, EBI-775541;
CC       P0CG47:RPS27A (xeno); NbExp=1; IntAct=EBI-1551033, EBI-413034;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Isoform 3 is present at the
CC       presynaptic membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9CZV8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9CZV8-4; Sequence=VSP_038354;
CC         Note=No experimental confirmation available;
CC       Name=3; Synonyms=Scrapper;
CC         IsoId=Q9CZV8-3; Sequence=VSP_030770;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain.
CC   -!- DISRUPTION PHENOTYPE: Altered electrophysiological synaptic
CC       activity, with increased frequency of miniature excitatory
CC       postsynaptic currents.
CC   -!- SIMILARITY: Contains 1 F-box domain.
CC   -!- SIMILARITY: Contains 12 LRR (leucine-rich) repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC29349.1; Type=Miscellaneous discrepancy; Note=Intron retention;
CC       Sequence=BAD90157.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; EF649694; ABU95014.1; -; mRNA.
DR   EMBL; AK012109; BAB28039.1; -; mRNA.
DR   EMBL; AK036217; BAC29349.1; ALT_SEQ; mRNA.
DR   EMBL; AK144786; BAE26066.1; -; mRNA.
DR   EMBL; AK220232; BAD90157.1; ALT_INIT; mRNA.
DR   EMBL; AL591205; CAM21260.1; -; Genomic_DNA.
DR   EMBL; AL591209; CAM21260.1; JOINED; Genomic_DNA.
DR   EMBL; AL591209; CAM20406.1; -; Genomic_DNA.
DR   EMBL; AL591205; CAM20406.1; JOINED; Genomic_DNA.
DR   IPI; IPI00605645; -.
DR   IPI; IPI00874641; -.
DR   IPI; IPI00954305; -.
DR   RefSeq; NP_082425.1; NM_028149.1.
DR   UniGene; Mm.218350; -.
DR   ProteinModelPortal; Q9CZV8; -.
DR   SMR; Q9CZV8; 24-69, 77-414.
DR   IntAct; Q9CZV8; 8.
DR   STRING; Q9CZV8; -.
DR   PhosphoSite; Q9CZV8; -.
DR   PRIDE; Q9CZV8; -.
DR   Ensembl; ENSMUST00000075071; ENSMUSP00000074580; ENSMUSG00000020883.
DR   Ensembl; ENSMUST00000103143; ENSMUSP00000099432; ENSMUSG00000020883.
DR   GeneID; 72194; -.
DR   KEGG; mmu:72194; -.
DR   CTD; 72194; -.
DR   MGI; MGI:1919444; Fbxl20.
DR   eggNOG; roNOG10353; -.
DR   GeneTree; ENSGT00560000076716; -.
DR   HOGENOM; HBG381563; -.
DR   HOVERGEN; HBG051586; -.
DR   InParanoid; Q9CZV8; -.
DR   OrthoDB; EOG4KPTB9; -.
DR   PhylomeDB; Q9CZV8; -.
DR   NextBio; 335667; -.
DR   ArrayExpress; Q9CZV8; -.
DR   Bgee; Q9CZV8; -.
DR   CleanEx; MM_FBXL20; -.
DR   Genevestigator; Q9CZV8; -.
DR   GermOnline; ENSMUSG00000020883; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   InterPro; IPR001810; F-box_dom_cyclin-like.
DR   InterPro; IPR022364; F-box_dom_Skp2-like.
DR   InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR   Pfam; PF00646; F-box; 1.
DR   SMART; SM00256; FBOX; 1.
DR   SMART; SM00367; LRR_CC; 2.
DR   SUPFAM; SSF81383; F-box_dom_Skp2-like; 1.
DR   PROSITE; PS50181; FBOX; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Leucine-rich repeat; Phosphoprotein;
KW   Repeat; Ubl conjugation pathway.
FT   CHAIN         1    436       F-box/LRR-repeat protein 20.
FT                                /FTId=PRO_0000119871.
FT   DOMAIN       22     68       F-box.
FT   REPEAT       90    115       LRR 1.
FT   REPEAT      116    141       LRR 2.
FT   REPEAT      142    167       LRR 3.
FT   REPEAT      168    193       LRR 4.
FT   REPEAT      194    219       LRR 5.
FT   REPEAT      220    245       LRR 6.
FT   REPEAT      246    271       LRR 7.
FT   REPEAT      272    297       LRR 8.
FT   REPEAT      298    323       LRR 9.
FT   REPEAT      324    349       LRR 10.
FT   REPEAT      353    377       LRR 11.
FT   REPEAT      378    403       LRR 12.
FT   MOD_RES     417    417       Phosphothreonine.
FT   MOD_RES     421    421       Phosphoserine.
FT   VAR_SEQ       1     14       Missing (in isoform 2).
FT                                /FTId=VSP_038354.
FT   VAR_SEQ       1     14       MRRDVNGVTKSRFE -> MAPSRDRLLHFGFKAT (in
FT                                isoform 3).
FT                                /FTId=VSP_030770.
FT   CONFLICT     40     40       L -> P (in Ref. 2; BAB28039).
FT   CONFLICT    379    381       HSL -> PSF (in Ref. 2; BAB28039).
SQ   SEQUENCE   436 AA;  48396 MW;  3218F38C02EA1BCE CRC64;
     MRRDVNGVTK SRFEMFSNSD EAVINKKLPK ELLLRIFSFL DVVTLCRCAQ VSRAWNVLAL
     DGSNWQRIDL FDFQRDIEGR VVENISKRCG GFLRKLSLRG CLGVGDNALR TFAQNCRNIE
     VLSLNGCTKT TDATCTSLSK FCSKLRHLDL ASCTSITNMS LKALSEGCPL LEQLNISWCD
     QVTKDGIQAL VRGCGGLKAL FLKGCTQLED EALKYIGAHC PELVTLNLQT CLQITDEGLI
     TICRGCHKLQ SLCASGCSNI TDAILNALGQ NCPRLRILEV ARCSQLTDVG FTTLARNCHE
     LEKMDLEECV QITDSTLIQL SIHCPRLQVL SLSHCELITD DGIRHLGNGA CAHDQLEVIE
     LDNCPLITDA SLEHLKSCHS LERIELYDCQ QITRAGIKRL RTHLPNIKVH AYFAPVTPPP
     SVGGSRQRFC RCCIIL
//
ID   TM55A_MOUSE             Reviewed;         257 AA.
AC   Q9CZX7;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Transmembrane protein 55A;
DE            EC=3.1.3.78;
DE   AltName: Full=PtdIns-4,5-P2 4-Ptase II;
DE   AltName: Full=Type II phosphatidylinositol 4,5-bisphosphate 4-phosphatase;
GN   Name=Tmem55a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Epididymis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of
CC       phosphatidylinositol 4,5-bisphosphate. Does not hydrolyze
CC       phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol
CC       3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4-
CC       bisphosphate, phosphatidylinositol 5-monophosphate,
CC       phosphatidylinositol 4-monophosphate and phosphatidylinositol 3-
CC       monophosphate (By similarity).
CC   -!- CATALYTIC ACTIVITY: 1-phosphatidyl-myo-inositol 4,5-bisphosphate +
CC       H(2)O = 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate.
CC   -!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-
CC       bisphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 5-phosphate
CC       + phosphate.
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane; Multi-pass membrane
CC       protein (By similarity). Lysosome membrane; Multi-pass membrane
CC       protein (By similarity).
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK012054; BAB27995.1; -; mRNA.
DR   EMBL; AK033845; BAC28493.1; -; mRNA.
DR   EMBL; AK049213; BAC33613.1; -; mRNA.
DR   EMBL; BC021435; AAH21435.1; -; mRNA.
DR   IPI; IPI00113239; -.
DR   RefSeq; NP_082540.1; NM_028264.4.
DR   UniGene; Mm.478837; -.
DR   ProteinModelPortal; Q9CZX7; -.
DR   PhosphoSite; Q9CZX7; -.
DR   PRIDE; Q9CZX7; -.
DR   Ensembl; ENSMUST00000029875; ENSMUSP00000029875; ENSMUSG00000028221.
DR   GeneID; 72519; -.
DR   KEGG; mmu:72519; -.
DR   UCSC; uc008sbg.1; mouse.
DR   CTD; 72519; -.
DR   MGI; MGI:1919769; Tmem55a.
DR   GeneTree; ENSGT00390000003680; -.
DR   HOGENOM; HBG381966; -.
DR   HOVERGEN; HBG080409; -.
DR   InParanoid; Q9CZX7; -.
DR   OMA; PVQPEGT; -.
DR   OrthoDB; EOG4D26QF; -.
DR   PhylomeDB; Q9CZX7; -.
DR   NextBio; 336410; -.
DR   ArrayExpress; Q9CZX7; -.
DR   Bgee; Q9CZX7; -.
DR   CleanEx; MM_TMEM55A; -.
DR   Genevestigator; Q9CZX7; -.
DR   GermOnline; ENSMUSG00000028221; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR019178; Transmembrane_protein_55A/B.
DR   PANTHER; PTHR21014; Transmembrane_protein_55A/B; 1.
DR   Pfam; PF09788; Tmemb_55A; 1.
PE   1: Evidence at protein level;
KW   Endosome; Hydrolase; Lysosome; Membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    257       Transmembrane protein 55A.
FT                                /FTId=PRO_0000235229.
FT   TRANSMEM    192    212       Helical; (Potential).
FT   TRANSMEM    227    247       Helical; (Potential).
FT   MOTIF       107    113       CX5R motif.
FT   ACT_SITE    107    107       By similarity.
FT   MOD_RES      18     18       Phosphoserine.
SQ   SEQUENCE   257 AA;  28038 MW;  0330A735DBCEC243 CRC64;
     MAADGVDERS PLLSASHSGN VTPTAPPYLQ ESSPRAELPP PYTAIASPGT SGIPVINCRV
     CQSLINLDGK LHQHVVKCTV CNEATPIKTP PTGKKYVRCP CNCLLICKDT SRRIGCPRPN
     CRRIINLGPV MLISEEQPAQ PALPIQPEGT RVVCGHCGNT FLWMELRFNT LAKCPHCKKI
     SSVGSALPRR RCCAYVTIGM ICIFIAVGLT VGTQDFSRRF HATYVSWAIA YLLGLICLIR
     ACYWGAIRVS YPEHGFA
//
ID   TMM85_MOUSE             Reviewed;         183 AA.
AC   Q9CZX9; A2AGJ7; Q9D1D9;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Transmembrane protein 85;
GN   Name=Tmem85;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=BALB/c, and C57BL/6J; TISSUE=Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May mediate anti-apoptotic activity (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the TMEM85 family.
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DR   EMBL; AK003668; BAB22926.1; -; mRNA.
DR   EMBL; AK012047; BAB27992.1; -; mRNA.
DR   EMBL; AK078165; BAC37155.1; -; mRNA.
DR   EMBL; AK167745; BAE39782.1; -; mRNA.
DR   EMBL; AL683897; CAM17484.1; -; Genomic_DNA.
DR   EMBL; CH466519; EDL27839.1; -; Genomic_DNA.
DR   EMBL; BC051926; AAH51926.1; -; mRNA.
DR   IPI; IPI00113243; -.
DR   RefSeq; NP_080795.1; NM_026519.3.
DR   UniGene; Mm.220942; -.
DR   ProteinModelPortal; Q9CZX9; -.
DR   STRING; Q9CZX9; -.
DR   PhosphoSite; Q9CZX9; -.
DR   PRIDE; Q9CZX9; -.
DR   Ensembl; ENSMUST00000028551; ENSMUSP00000028551; ENSMUSG00000027131.
DR   GeneID; 68032; -.
DR   KEGG; mmu:68032; -.
DR   UCSC; uc008loy.1; mouse.
DR   CTD; 68032; -.
DR   MGI; MGI:1915282; Tmem85.
DR   eggNOG; roNOG15322; -.
DR   GeneTree; ENSGT00390000006970; -.
DR   HOGENOM; HBG609692; -.
DR   HOVERGEN; HBG056123; -.
DR   InParanoid; Q9CZX9; -.
DR   OMA; IMMVGMM; -.
DR   OrthoDB; EOG405S2H; -.
DR   PhylomeDB; Q9CZX9; -.
DR   NextBio; 326250; -.
DR   ArrayExpress; Q9CZX9; -.
DR   Bgee; Q9CZX9; -.
DR   CleanEx; MM_TMEM85; -.
DR   Genevestigator; Q9CZX9; -.
DR   GermOnline; ENSMUSG00000027131; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   InterPro; IPR009445; DUF1077_TMEM85.
DR   PANTHER; PTHR19315; DUF1077; 1.
DR   Pfam; PF06417; DUF1077; 1.
DR   PIRSF; PIRSF017207; UCP017207_TM-p85; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    183       Transmembrane protein 85.
FT                                /FTId=PRO_0000251915.
FT   TRANSMEM     84    104       Helical; (Potential).
FT   TRANSMEM    129    149       Helical; (Potential).
FT   CONFLICT      9      9       A -> R (in Ref. 1; BAB22926).
SQ   SEQUENCE   183 AA;  20117 MW;  7FED8D53F092D161 CRC64;
     MTTQGGLVAN RGRRFKWAIE LSGPGGGSRG RSDRGSGQGD SLYPVGYLDK QVPDTSVQET
     DRILVEKRCW DIALGPLKQI PMNLFIMYMA GNTISIFPTM MVCMMAWRPI QALMAISATF
     KMLESSSQKF LQGLVYLIGN LMGLALAVYK CQSMGLLPTH ASDWLAFIEP PERMEFSGGG
     LLL
//
ID   MDM1_MOUSE              Reviewed;         708 AA.
AC   Q9D067; Q61841; Q61842; Q9DBR6;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 2.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Nuclear protein MDM1;
DE   AltName: Full=Mdm4 transformed 3T3 cell double minute 1 protein;
GN   Name=Mdm1; Synonyms=Mdm-1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c;
RX   MEDLINE=89034221; PubMed=3182840;
RA   Snyder L.C., Trusko S.P., Freeman N., Eshleman J.R., Fakharzadeh S.S.,
RA   George D.L.;
RT   "A gene amplified in a transformed mouse cell line undergoes complex
RT   transcriptional processing and encodes a nuclear protein.";
RL   J. Biol. Chem. 263:17150-17158(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Additional isoforms may exist;
CC       Name=1;
CC         IsoId=Q9D067-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D067-2; Sequence=VSP_027551, VSP_027552;
CC       Name=3; Synonyms=Mdm1a;
CC         IsoId=Q9D067-3; Sequence=VSP_027549, VSP_027550;
CC       Name=4;
CC         IsoId=Q9D067-4; Sequence=VSP_027548;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in
CC       the testis.
CC   -!- SIMILARITY: Belongs to the MDM1 family.
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DR   EMBL; M20823; AAA39511.1; -; mRNA.
DR   EMBL; M20824; AAA39512.1; -; mRNA.
DR   EMBL; AK004789; BAB23566.1; -; mRNA.
DR   EMBL; AK011769; BAB27830.1; -; mRNA.
DR   IPI; IPI00172264; -.
DR   IPI; IPI00857599; -.
DR   IPI; IPI00857816; -.
DR   IPI; IPI00943408; -.
DR   PIR; A31794; A31794.
DR   PIR; B31794; B31794.
DR   RefSeq; NP_001156376.1; NM_001162904.1.
DR   RefSeq; NP_001156377.1; NM_001162905.1.
DR   RefSeq; NP_034915.2; NM_010785.2.
DR   RefSeq; NP_683724.2; NM_148922.3.
DR   UniGene; Mm.101191; -.
DR   UniGene; Mm.442618; -.
DR   STRING; Q9D067; -.
DR   PhosphoSite; Q9D067; -.
DR   Ensembl; ENSMUST00000020437; ENSMUSP00000020437; ENSMUSG00000020212.
DR   GeneID; 17245; -.
DR   KEGG; mmu:17245; -.
DR   NMPDR; fig|10090.3.peg.22895; -.
DR   UCSC; uc007hdt.1; mouse.
DR   CTD; 17245; -.
DR   MGI; MGI:96951; Mdm1.
DR   eggNOG; maNOG07090; -.
DR   GeneTree; ENSGT00390000004106; -.
DR   HOVERGEN; HBG108124; -.
DR   InParanoid; Q9D067; -.
DR   OMA; PSRRIQG; -.
DR   OrthoDB; EOG4FR0R8; -.
DR   NextBio; 291700; -.
DR   ArrayExpress; Q9D067; -.
DR   Bgee; Q9D067; -.
DR   CleanEx; MM_MDM1; -.
DR   Genevestigator; Q9D067; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Nucleus; Phosphoprotein.
FT   CHAIN         1    708       Nuclear protein MDM1.
FT                                /FTId=PRO_0000299060.
FT   COILED      322    355       Potential.
FT   MOD_RES     315    315       Phosphoserine (By similarity).
FT   MOD_RES     501    501       Phosphoserine (By similarity).
FT   MOD_RES     503    503       Phosphoserine (By similarity).
FT   MOD_RES     581    581       Phosphoserine (By similarity).
FT   VAR_SEQ     171    215       Missing (in isoform 4).
FT                                /FTId=VSP_027548.
FT   VAR_SEQ     217    222       FRNKSQ -> AQEMRF (in isoform 3).
FT                                /FTId=VSP_027549.
FT   VAR_SEQ     223    708       Missing (in isoform 3).
FT                                /FTId=VSP_027550.
FT   VAR_SEQ     607    607       D -> EG (in isoform 2).
FT                                /FTId=VSP_027551.
FT   VAR_SEQ     652    672       MGKPRTNNLQLHPHDAFNDED -> N (in isoform
FT                                2).
FT                                /FTId=VSP_027552.
FT   CONFLICT     40     40       R -> K (in Ref. 2; BAB27830).
FT   CONFLICT    438    438       S -> L (in Ref. 1; AAA39511).
FT   CONFLICT    442    442       K -> E (in Ref. 2; BAB23566).
FT   CONFLICT    456    456       Q -> P (in Ref. 2; BAB23566).
FT   CONFLICT    472    472       D -> G (in Ref. 1; AAA39511).
SQ   SEQUENCE   708 AA;  79689 MW;  FF3BE0BA5167FB28 CRC64;
     MPVRFKGLSE YQRNFLWKKS YLSESYNPSV GQKYSWAGLR SDQLGITKEP GFISKRRVPY
     HDPQISKYLE WNGTVRKKDT LVPPEPQAFG TPKPQEAEQG EDANQEAVLS LEASRVPKRT
     RSHSADSRAE GVSDTVEKHQ GVTRSHAPVS ADVELRPSSK QPLSQSIDPR LDRHLRKKAG
     LAVVPTNNAL RNSEYQRQFV WKTSKESAPV FASNQVFRNK SQIIPQFQGN TFTHETEYKR
     NFKGLTPVKE PKSREYLKGN SSLEMLTPVK KADEPLDLEV DMASEDSDQS VKKPASWRHQ
     RLGKVNSEYR AKFLSPAQYF YKAGAWTRVK ENLSNQVKEL REKAESYRKR VQGTHFSRDH
     LNQIMSDSNC CWDVSSVTSS EGTVSSNIRA LDLAGDLTNH RTPQKHPPTK LEERKVASGE
     QPLKNSTRRL EMPEPAASVR RKLAWDAEES TKEDTQEEPR AEEDGREERG QDKQTCAVEL
     EKPDTQTPKA DRLTEGSETS SVSSGKGGRL PTPRLRELGI QRTHHDLTTP AVGGAVLVSP
     SKVKPPGLEQ RRRASSQDGL ETLKKDITKK GKPRPMSLLT SPAAGMKTVD PLPLREDCEA
     NVLRFADTLP VSKILDRQPS TPGQLPPCAP PYCHPSSRIQ GRLRDPEFQH NMGKPRTNNL
     QLHPHDAFND EDADRLSEIS ARSAVSSLRA FQTLARAQKR KENFWGKP
//
ID   MGRN1_MOUSE             Reviewed;         532 AA.
AC   Q9D074; Q3U5V9; Q3UDA1; Q6ZQ97; Q8BZM9;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=E3 ubiquitin-protein ligase MGRN1;
DE            EC=6.3.2.-;
DE   AltName: Full=Mahogunin RING finger protein 1;
GN   Name=Mgrn1; Synonyms=Kiaa0544;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 318-532 (ISOFORM 4).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Diencephalon, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 102-532 (ISOFORM 3).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=12438443;
RA   Phan L.K., Lin F., LeDuc C.A., Chung W.K., Leibel R.L.;
RT   "The mouse mahoganoid coat color mutation disrupts a novel C3HC4 RING
RT   domain protein.";
RL   J. Clin. Invest. 110:1449-1459(2002).
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, UBIQUITINATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=12560552; DOI=10.1126/science.1079694;
RA   He L., Lu X.-Y., Jolly A.F., Eldridge A.G., Watson S.J., Jackson P.K.,
RA   Barsh G.S., Gunn T.M.;
RT   "Spongiform degeneration in mahoganoid mutant mice.";
RL   Science 299:710-712(2003).
RN   [6]
RP   DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=17075880; DOI=10.1002/dvdy.20992;
RA   Cota C.D., Bagher P., Pelc P., Smith C.O., Bodner C.R., Gunn T.M.;
RT   "Mice with mutations in Mahogunin ring finger-1 (Mgrn1) exhibit
RT   abnormal patterning of the left-right axis.";
RL   Dev. Dyn. 235:3438-3447(2006).
RN   [7]
RP   ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX   PubMed=17083490; DOI=10.1111/j.1600-0749.2006.00340.x;
RA   Bagher P., Jiao J., Owen Smith C., Cota C.D., Gunn T.M.;
RT   "Characterization of Mahogunin Ring Finger-1 expression in mice.";
RL   Pigment Cell Res. 19:635-643(2006).
RN   [8]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=17720281; DOI=10.1016/j.neurobiolaging.2007.07.012;
RA   Sun K., Johnson B.S., Gunn T.M.;
RT   "Mitochondrial dysfunction precedes neurodegeneration in mahogunin
RT   (Mgrn1) mutant mice.";
RL   Neurobiol. Aging 28:1840-1852(2007).
RN   [9]
RP   FUNCTION, INTERACTION WITH TSG101, DISRUPTION PHENOTYPE, AND
RP   MUTAGENESIS OF 278-CYS--CYS-281 AND 384-PRO--PRO-387.
RX   PubMed=19703557; DOI=10.1016/j.bbadis.2009.08.009;
RA   Jiao J., Sun K., Walker W.P., Bagher P., Cota C.D., Gunn T.M.;
RT   "Abnormal regulation of TSG101 in mice with spongiform
RT   neurodegeneration.";
RL   Biochim. Biophys. Acta 1792:1027-1035(2009).
RN   [10]
RP   INTERACTION WITH PRNP, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=19524515; DOI=10.1016/j.cell.2009.03.042;
RA   Chakrabarti O., Hegde R.S.;
RT   "Functional depletion of mahogunin by cytosolically exposed prion
RT   protein contributes to neurodegeneration.";
RL   Cell 137:1136-1147(2009).
RN   [11]
RP   ALTERNATIVE SPLICING, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19422019; DOI=10.1002/dvg.20529;
RA   Jiao J., Kim H.Y., Liu R.R., Hogan C.A., Sun K., Tam L.M., Gunn T.M.;
RT   "Transgenic analysis of the physiological functions of Mahogunin Ring
RT   Finger-1 isoforms.";
RL   Genesis 47:524-534(2009).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase. Mediates TSG101
CC       monoubiquitination at multiple sites. Plays a role in the
CC       regulation of endosome-to-lysosome trafficking. Impairs MC1R- and
CC       MC4R-signaling by competing with GNAS-binding to MCRs and
CC       inhibiting agonist-induced cAMP production. Does not inhibit
CC       ADRB2-signaling. Does not promote MC1R ubiquitination (By
CC       similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with MC1R and MC4R (By similarity). Interacts
CC       with TSG101. Interacts with mislocalized cytosolically exposed
CC       PRNP; this interaction alters MGRN1 subcellular location and
CC       causes lysosomal enlargement.
CC   -!- INTERACTION:
CC       P04273:PRNP (xeno); NbExp=1; IntAct=EBI-2368450, EBI-986426;
CC   -!- SUBCELLULAR LOCATION: Early endosome. Note=The endosomal
CC       localization is dependent on the interaction with TSG101 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Cell membrane (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Isoform 5: Cytoplasm. Nucleus. Note=In the
CC       cytoplasm, predominantly localized to the perinuclear region and
CC       discrete vesicular structures. In the nucleus, broadly
CC       distributed, but excluded from nucleoli.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1; Synonyms=I;
CC         IsoId=Q9D074-1; Sequence=Displayed;
CC         Note=Sufficient for normal development, pigmentation and
CC         neuronal integrity;
CC       Name=2;
CC         IsoId=Q9D074-2; Sequence=VSP_019854;
CC       Name=3; Synonyms=III;
CC         IsoId=Q9D074-3; Sequence=VSP_019856;
CC         Note=Sufficient for normal development, pigmentation and
CC         neuronal integrity;
CC       Name=4; Synonyms=II;
CC         IsoId=Q9D074-4; Sequence=VSP_019855;
CC         Note=Partial rescue of the phenotype of mutant null mice;
CC       Name=5; Synonyms=IV;
CC         IsoId=Q9D074-5; Sequence=VSP_019855, VSP_019856;
CC         Note=Unable to rescue the phenotype of mutant null mice. No
CC         experimental confirmation available. This sequence has been
CC         deduced from the description in Ref.11;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in
CC       brain, heart, kidney and liver. In the CNS, especially prominent
CC       in the Purkinje cells of the cerebellum. In the skin, expressed in
CC       the basal layer of the epidermis and hair follicles, primarily in
CC       the outer root sheath. Isoforms 1, 3, 4 and 5 are equally
CC       expressed in the liver. Isoforms 1, 3 and 4 are most abundant in
CC       brain, kidney and heart, respectively.
CC   -!- DEVELOPMENTAL STAGE: In presomite and early somite stage embryos,
CC       most strongly expressed in the node and more weakly in the
CC       neuroepithelium. In 6- to 12-somite embryos, strongest expression
CC       in the node, symmetrically in the floor plate of the neural tube
CC       and in the developing heart; weaker expression in paraxial
CC       mesoderm, somites, neuroepithelium, as well as in hind- and
CC       foregut pockets. By 9.5 dpc, virtually ubiquitous.
CC   -!- DOMAIN: The RING finger is required for ubiquitin ligase activity.
CC   -!- PTM: Autoubiquitinated in vitro.
CC   -!- DISRUPTION PHENOTYPE: Mutant mice have a pleiotropic phenotype
CC       that includes the absence of yellow hair pigment, curly hair and
CC       whiskers, abnormal craniofacial patterning, reduced embryonic
CC       viability due to mispatterning of the left-right body axis and
CC       age-dependent spongiform neurodegeneration. Many months before
CC       onset of vacuolation, mitochondrial complex IV expression and
CC       activity is significantly reduced in mutant brains and oxidative
CC       stress is increased. A global reduction of ubiquitinated proteins
CC       in the brain is observed. At 1 month of age, null mutant mouse
CC       brains have less ubiquitinated TSG101, while adult mutant brains
CC       contain more ubiquitinated and insoluble TSG101 than wild type. At
CC       1 month of age, significant increase in EGFR levels in the brains
CC       of null mutant mice relative to wild-type mice, suggesting an
CC       impaired trafficking to the lysosome for degradation.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK011747; BAB27816.2; -; mRNA.
DR   EMBL; AK034100; BAC28587.1; -; mRNA.
DR   EMBL; AK088533; BAC40408.1; -; mRNA.
DR   EMBL; AK150176; BAE29360.1; -; mRNA.
DR   EMBL; AK153407; BAE31967.1; -; mRNA.
DR   EMBL; BC046830; AAH46830.1; -; mRNA.
DR   EMBL; AK129161; BAC97971.1; -; mRNA.
DR   IPI; IPI00187513; -.
DR   IPI; IPI00406217; -.
DR   IPI; IPI00460741; -.
DR   IPI; IPI00775949; -.
DR   IPI; IPI00969332; -.
DR   RefSeq; NP_083933.1; NM_029657.3.
DR   UniGene; Mm.291326; -.
DR   UniGene; Mm.391848; -.
DR   ProteinModelPortal; Q9D074; -.
DR   SMR; Q9D074; 273-320.
DR   IntAct; Q9D074; 7.
DR   STRING; Q9D074; -.
DR   PhosphoSite; Q9D074; -.
DR   PRIDE; Q9D074; -.
DR   Ensembl; ENSMUST00000023159; ENSMUSP00000023159; ENSMUSG00000022517.
DR   Ensembl; ENSMUST00000070658; ENSMUSP00000068314; ENSMUSG00000022517.
DR   Ensembl; ENSMUST00000090460; ENSMUSP00000087946; ENSMUSG00000022517.
DR   GeneID; 17237; -.
DR   KEGG; mmu:17237; -.
DR   UCSC; uc007yap.1; mouse.
DR   UCSC; uc007yaq.1; mouse.
DR   CTD; 17237; -.
DR   MGI; MGI:2447670; Mgrn1.
DR   eggNOG; roNOG05825; -.
DR   GeneTree; ENSGT00390000009925; -.
DR   HOVERGEN; HBG061762; -.
DR   OMA; ETKPSDD; -.
DR   OrthoDB; EOG47SSDK; -.
DR   PhylomeDB; Q9D074; -.
DR   NextBio; 291678; -.
DR   ArrayExpress; Q9D074; -.
DR   Bgee; Q9D074; -.
DR   CleanEx; MM_MGRN1; -.
DR   Genevestigator; Q9D074; -.
DR   GermOnline; ENSMUSG00000022517; Mus musculus.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; ISS:UniProtKB.
DR   GO; GO:0045744; P:negative regulation of G-protein coupled receptor protein signaling pathway; ISS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasm; Endosome; Ligase;
KW   Membrane; Metal-binding; Nucleus; Phosphoprotein; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    532       E3 ubiquitin-protein ligase MGRN1.
FT                                /FTId=PRO_0000246688.
FT   ZN_FING     277    316       RING-type.
FT   MOTIF       384    387       Required for TSG101-binding.
FT   MOD_RES     501    501       Phosphoserine (By similarity).
FT   VAR_SEQ      29     29       S -> SA (in isoform 2).
FT                                /FTId=VSP_019854.
FT   VAR_SEQ     355    355       S -> SCPFKKSKSHPASLASKKPKRET (in isoform
FT                                4 and isoform 5).
FT                                /FTId=VSP_019855.
FT   VAR_SEQ     520    532       ALGPESCSVGIEE -> GWSTSMETPHSLGTTSSPWPLLSG
FT                                SSPEPGVAELTPF (in isoform 3 and isoform
FT                                5).
FT                                /FTId=VSP_019856.
FT   MUTAGEN     278    281       CVVC->AVVA: Loss of ubiquitin-protein
FT                                ligase activity. Increase in TSG101-
FT                                binding.
FT   MUTAGEN     384    387       PSAP->ASAA: Loss of TSG101-binding.
FT   CONFLICT     15     15       I -> F (in Ref. 1; BAE29360).
FT   CONFLICT     31     31       N -> D (in Ref. 1; BAE29360).
FT   CONFLICT     36     36       H -> R (in Ref. 1; BAE29360).
SQ   SEQUENCE   532 AA;  58477 MW;  89C2C1A28F9417EE CRC64;
     MGSILSRRIA GVEDIDIQAN SAYRYPPKSG NYFASHFFMG GEKFDTPHPE GYLFGENMDL
     NFLGSRPVQF PYVTPAPHEP VKTLRSLVNI RKDSLRLVRY KEDADSPTED GEKPRVLYSL
     EFTFDADARV AITIYCQAVE ELVNGVAVYS CKNPSLQSET VHYKRGVSQQ FSLPSFKIDF
     SEWKDDELNF DLDRGVFPVV IQAVVDEGDV VEVTGHAHVL LAAFEKHVDG SFSVKPLKQK
     QIVDRVSYLL QEIYGIENKN NQETKPSDDE NSDNSSECVV CLSDLRDTLI LPCRHLCLCT
     SCADTLRYQA NNCPICRLPF RALLQIRAVR KKPGALSPIS FSPVLAQSVD HDEHSSSDSI
     PPGYEPISLL EALNGLRAVS PAIPSAPLYE EITYSGISDG LSQASCPLAG LDRIMESGLQ
     KGKTQSKSPD STLRSPSFPI HEEDEEKLSE DSDAPLPPSG VELVLRESSS PESFGTEEGD
     EPSLKQGSRV PSIDDVLQDG SPQHHGCSQP VPPADIYLPA LGPESCSVGI EE
//
ID   HNRPM_MOUSE             Reviewed;         729 AA.
AC   Q9D0E1; Q6P1B2; Q99JQ0;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-FEB-2011, entry version 84.
DE   RecName: Full=Heterogeneous nuclear ribonucleoprotein M;
DE            Short=hnRNP M;
GN   Name=Hnrnpm; Synonyms=Hnrpm;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 449-455, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
CC   -!- FUNCTION: Pre-mRNA binding protein in vivo, binds avidly to
CC       poly(G) and poly(U) RNA homopolymers in vitro. Involved in
CC       splicing. Acts as a receptor for carcinoembryonic antigen in
CC       Kupffer cells, may initiate a series of signaling events leading
CC       to tyrosine phosphorylation of proteins and induction of IL-1
CC       alpha, IL-6, IL-10 and tumor necrosis factor alpha cytokines (By
CC       similarity).
CC   -!- SUBUNIT: Identified in the spliceosome C complex, at least
CC       composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23,
CC       DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1,
CC       GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK,
CC       HNRNPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH,
CC       MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19,
CC       PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1,
CC       SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB,
CC       SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1,
CC       SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9D0E1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D0E1-2; Sequence=VSP_011933;
CC   -!- PTM: Sumoylated (By similarity).
CC   -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK011521; BAB27675.1; -; mRNA.
DR   EMBL; BC005758; AAH05758.1; -; mRNA.
DR   EMBL; BC065172; AAH65172.1; -; mRNA.
DR   IPI; IPI00132443; -.
DR   IPI; IPI00480357; -.
DR   RefSeq; NP_001103383.1; NM_001109913.1.
DR   RefSeq; NP_084080.1; NM_029804.3.
DR   UniGene; Mm.311439; -.
DR   ProteinModelPortal; Q9D0E1; -.
DR   SMR; Q9D0E1; 69-295, 651-729.
DR   STRING; Q9D0E1; -.
DR   PhosphoSite; Q9D0E1; -.
DR   PRIDE; Q9D0E1; -.
DR   Ensembl; ENSMUST00000087582; ENSMUSP00000084864; ENSMUSG00000059208.
DR   Ensembl; ENSMUST00000114385; ENSMUSP00000110027; ENSMUSG00000059208.
DR   GeneID; 76936; -.
DR   KEGG; mmu:76936; -.
DR   UCSC; uc008bze.1; mouse.
DR   UCSC; uc008bzf.1; mouse.
DR   CTD; 76936; -.
DR   MGI; MGI:1926465; Hnrnpm.
DR   GeneTree; ENSGT00410000025635; -.
DR   HOGENOM; HBG715601; -.
DR   HOVERGEN; HBG054880; -.
DR   InParanoid; Q9D0E1; -.
DR   OMA; DRMGANN; -.
DR   NextBio; 346119; -.
DR   ArrayExpress; Q9D0E1; -.
DR   Bgee; Q9D0E1; -.
DR   Genevestigator; Q9D0E1; -.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 3.
DR   Pfam; PF00076; RRM_1; 3.
DR   SMART; SM00360; RRM; 3.
DR   PROSITE; PS50102; RRM; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Direct protein sequencing;
KW   mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Repeat;
KW   Ribonucleoprotein; RNA-binding; Spliceosome; Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    729       Heterogeneous nuclear ribonucleoprotein
FT                                M.
FT                                /FTId=PRO_0000081865.
FT   DOMAIN       70    148       RRM 1.
FT   DOMAIN      203    280       RRM 2.
FT   REPEAT      399    404       1.
FT   REPEAT      406    411       2.
FT   REPEAT      414    419       3.
FT   REPEAT      425    430       4.
FT   REPEAT      432    437       5.
FT   REPEAT      439    444       6.
FT   REPEAT      445    450       7.
FT   REPEAT      452    457       8.
FT   REPEAT      460    465       9.
FT   REPEAT      467    472       10.
FT   REPEAT      474    479       11.
FT   REPEAT      481    486       12.
FT   REPEAT      492    497       13.
FT   REPEAT      499    504       14.
FT   REPEAT      506    511       15.
FT   REPEAT      513    518       16.
FT   REPEAT      520    525       17.
FT   REPEAT      527    532       18.
FT   REPEAT      539    544       19.
FT   REPEAT      546    551       20.
FT   REPEAT      553    558       21.
FT   REPEAT      561    566       22.
FT   REPEAT      566    571       23.
FT   REPEAT      574    579       24.
FT   REPEAT      579    584       25.
FT   REPEAT      587    592       26.
FT   REPEAT      602    607       27.
FT   DOMAIN      652    728       RRM 3.
FT   REGION      399    607       27 X 6 AA repeats of [GEVSTPAN]-[ILMV]-
FT                                [DE]-[RH]-[MLVI]-[GAV].
FT   COMPBIAS    389    395       Poly-Gly.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     276    276       N6-acetyllysine (By similarity).
FT   MOD_RES     431    431       Phosphoserine (By similarity).
FT   MOD_RES     467    467       Phosphoserine (By similarity).
FT   MOD_RES     512    512       Phosphoserine (By similarity).
FT   MOD_RES     527    527       Phosphoserine (By similarity).
FT   MOD_RES     539    539       Phosphoserine.
FT   MOD_RES     587    587       Phosphoserine (By similarity).
FT   MOD_RES     617    617       Phosphoserine.
FT   MOD_RES     632    632       Phosphoserine (By similarity).
FT   MOD_RES     636    636       Phosphoserine (By similarity).
FT   MOD_RES     697    697       N6-acetyllysine (By similarity).
FT   MOD_RES     700    700       Phosphoserine (By similarity).
FT   VAR_SEQ     159    197       Missing (in isoform 2).
FT                                /FTId=VSP_011933.
FT   CONFLICT    357    357       E -> G (in Ref. 2; AAH05758).
SQ   SEQUENCE   729 AA;  77649 MW;  D42650B419362D6B CRC64;
     MAAGVEAAAE VAATEPKMEE ESGAPCVPSG NGAPGPKGEE RPTQNEKRKE KNIKRGGNRF
     EPYSNPTKRY RAFITNIPFD VKWQSLKDLV KEKVGEVTYV ELLMDAEGKS RGCAVVEFKM
     EESMKKAAEV LNKHSLSGRP LKVKEDPDGE HARRAMQKVM ATTGGMGMGP GGPGMINIPP
     SILNNPNIPN EIIHALQAGR LGSTVFVANL DYKVGWKKLK EVFSMAGVVV RADILEDKDG
     KSRGIGIVTF EQSIEAVQAI SMFNGQLLFD RPMHVKMDER ALPKGDFFPP ERPQQLPHGL
     GGIGMGLGPG GQPIDANHLS KGIGMGNLGP AGMGMEGIGF GINKIGGMEG PFGGGMENMG
     RFGSGMNMGR INEILSNALK RGEIIAKQGG GGAGGSVPGI ERMGPGIDRI SGAGMERMGA
     GLGHGMDRVG SEIERMGLVM DRMGSVERMG SSIERMGPLG LDHMASSIER MGQTMERIGS
     GVERMGAGMG FGLERMAAPI DRVGQTIERM GSGVERMGPA IERMGLSMDR MVPTGMGASL
     ERMGPVMDRM ATGLERMGAN NLERMGLERM GANSLERMGL ERMGANSLER MGPAMGPALG
     AGIERMGLAM GGAGGASFDR AIEMERGNFG GSFAGSFGGA GGHAPGVARK ACQIFVRNLP
     FDFTWKMLKD KFNECGHVLY ADIKMENGKS KGCGVVKFES PEVAERACRM MNGMKLSGRE
     IDVRIDRNA
//
ID   LYSM1_MOUSE             Reviewed;         226 AA.
AC   Q9D0E3;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=LysM and putative peptidoglycan-binding domain-containing protein 1;
GN   Name=Lysmd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, Embryo, and Ovary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Fetal brain, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SIMILARITY: Contains 1 LysM repeat.
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DR   EMBL; AK011517; BAB27671.1; -; mRNA.
DR   EMBL; AK054348; BAC35742.1; -; mRNA.
DR   EMBL; AK154180; BAE32423.1; -; mRNA.
DR   EMBL; BC024838; AAH24838.1; -; mRNA.
DR   EMBL; BC100548; AAI00549.1; -; mRNA.
DR   IPI; IPI00132447; -.
DR   RefSeq; NP_694761.1; NM_153121.2.
DR   UniGene; Mm.341945; -.
DR   ProteinModelPortal; Q9D0E3; -.
DR   SMR; Q9D0E3; 34-95.
DR   PhosphoSite; Q9D0E3; -.
DR   PRIDE; Q9D0E3; -.
DR   Ensembl; ENSMUST00000066386; ENSMUSP00000067811; ENSMUSG00000053769.
DR   GeneID; 217779; -.
DR   KEGG; mmu:217779; -.
DR   UCSC; uc008qie.1; mouse.
DR   CTD; 217779; -.
DR   MGI; MGI:1919409; Lysmd1.
DR   eggNOG; roNOG05589; -.
DR   GeneTree; ENSGT00520000055632; -.
DR   HOGENOM; HBG716662; -.
DR   HOVERGEN; HBG079723; -.
DR   InParanoid; Q9D0E3; -.
DR   OMA; RMQQRAV; -.
DR   OrthoDB; EOG43N7DW; -.
DR   PhylomeDB; Q9D0E3; -.
DR   NextBio; 457821; -.
DR   Bgee; Q9D0E3; -.
DR   Genevestigator; Q9D0E3; -.
DR   GermOnline; ENSMUSG00000051031; Mus musculus.
DR   GermOnline; ENSMUSG00000053769; Mus musculus.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   InterPro; IPR018392; Peptidoglycan-bd_lysin.
DR   InterPro; IPR002482; Peptidoglycan-bd_Lysin_sg.
DR   Pfam; PF01476; LysM; 1.
DR   SMART; SM00257; LysM; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    226       LysM and putative peptidoglycan-binding
FT                                domain-containing protein 1.
FT                                /FTId=PRO_0000247998.
FT   REPEAT       42     85       LysM.
FT   MOD_RES      23     23       Phosphoserine.
FT   MOD_RES      99     99       Phosphoserine.
SQ   SEQUENCE   226 AA;  24814 MW;  B378600A2F754B0F CRC64;
     MASPSRQPPL GGSGLLHGSR ARSYGSLVQS SCSPVRERRL EHQLEPGDTL AGLALKYGVT
     MEQIKRTNRL YTNDSIFLKK TLYIPILSEP RDLFNGLDSE EENDGEEEVR PSKDEIGSSS
     GRRKNRGSGS GRPNGTGLPP HQETSTPSHD LSASDFLKKL DSQISLSKKA AAQKLRKGES
     GVPEEDTGLY PSSPRMQQRA VLGPVPLTRT SRTQTLRDQE DEIFKL
//
ID   NKAP_MOUSE              Reviewed;         415 AA.
AC   Q9D0F4; Q8BTK6; Q8BYT5; Q8R324; Q9CSH4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=NF-kappa-B-activating protein;
GN   Name=Nkap;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=22898119; PubMed=14550261; DOI=10.1016/j.bbrc.2003.09.074;
RA   Chen D., Li Z., Yang Q., Zhang J., Zhai Z., Shu H.-B.;
RT   "Identification of a nuclear protein that promotes NF-kappaB
RT   activation.";
RL   Biochem. Biophys. Res. Commun. 310:720-724(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
CC   -!- FUNCTION: Acts as a transcriptional repressor. Plays a role as a
CC       transcriptional corepressor of the Notch-mediated signaling
CC       required for T cell development. Also involved in the TNF and IL-1
CC       induced NF-kappa-B activation. Associates with chromatin at the
CC       Notch-regulated SKP2 promoter (By similarity).
CC   -!- SUBUNIT: Component of the Notch corepressor complex. Interacts
CC       with CIR1 and HDAC3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the UPF0396 family.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AY388959; AAQ90403.1; -; mRNA.
DR   EMBL; AK011492; BAB27654.1; -; mRNA.
DR   EMBL; AK012826; BAB28497.3; -; mRNA.
DR   EMBL; AK038344; BAC29972.1; -; mRNA.
DR   EMBL; AK089943; BAC41010.1; -; mRNA.
DR   EMBL; BC026774; AAH26774.1; -; mRNA.
DR   IPI; IPI00458918; -.
DR   RefSeq; NP_080213.3; NM_025937.4.
DR   UniGene; Mm.55422; -.
DR   ProteinModelPortal; Q9D0F4; -.
DR   STRING; Q9D0F4; -.
DR   PhosphoSite; Q9D0F4; -.
DR   PRIDE; Q9D0F4; -.
DR   Ensembl; ENSMUST00000016553; ENSMUSP00000016553; ENSMUSG00000016409.
DR   GeneID; 67050; -.
DR   KEGG; mmu:67050; -.
DR   UCSC; uc009syg.1; mouse.
DR   CTD; 67050; -.
DR   MGI; MGI:1914300; Nkap.
DR   eggNOG; roNOG16835; -.
DR   GeneTree; ENSGT00510000047021; -.
DR   HOGENOM; HBG279805; -.
DR   HOVERGEN; HBG068915; -.
DR   InParanoid; Q9D0F4; -.
DR   OMA; YSRPYGS; -.
DR   OrthoDB; EOG4JDH7S; -.
DR   PhylomeDB; Q9D0F4; -.
DR   NextBio; 323428; -.
DR   ArrayExpress; Q9D0F4; -.
DR   Bgee; Q9D0F4; -.
DR   CleanEx; MM_NKAP; -.
DR   Genevestigator; Q9D0F4; -.
DR   GermOnline; ENSMUSG00000016409; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0016564; F:transcription repressor activity; ISS:UniProtKB.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; ISS:UniProtKB.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR009269; DUF926.
DR   PANTHER; PTHR13087; DUF926; 1.
DR   Pfam; PF06047; DUF926; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Notch signaling pathway; Nucleus; Phosphoprotein;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN         1    415       NF-kappa-B-activating protein.
FT                                /FTId=PRO_0000259646.
FT   REGION      177    272       Necessary for interaction with CIR1 (By
FT                                similarity).
FT   REGION      273    415       Necessary for interaction with HDAC3 and
FT                                transcriptional repression (By
FT                                similarity).
FT   COMPBIAS      8     86       Arg-rich.
FT   COMPBIAS    180    259       Lys-rich.
FT   MOD_RES       9      9       Phosphoserine (By similarity).
FT   MOD_RES      62     62       Phosphoserine (By similarity).
FT   MOD_RES     110    110       N6-acetyllysine (By similarity).
FT   MOD_RES     147    147       Phosphoserine.
FT   MOD_RES     155    155       Phosphoserine (By similarity).
FT   MOD_RES     159    159       Phosphothreonine (By similarity).
FT   MOD_RES     261    261       Phosphoserine (By similarity).
FT   MOD_RES     262    262       Phosphoserine (By similarity).
FT   MOD_RES     264    264       Phosphoserine (By similarity).
FT   MOD_RES     265    265       Phosphoserine (By similarity).
FT   MOD_RES     266    266       Phosphoserine (By similarity).
FT   MOD_RES     269    269       Phosphoserine (By similarity).
FT   CONFLICT    185    185       K -> E (in Ref. 2; BAC41010).
FT   CONFLICT    191    191       D -> E (in Ref. 3; AAH26774).
FT   CONFLICT    194    195       KK -> QE (in Ref. 2; BAC41010).
FT   CONFLICT    293    293       P -> A (in Ref. 2; BAC29972).
SQ   SEQUENCE   415 AA;  47227 MW;  F9B254B486CD363C CRC64;
     MAPVSGSRSP EREASGAKRR SPSRSPKSIK SSRSPRCRRS RSRSCSRFGD RNGLSHSLSG
     FSQSSRNQSY RSRSRSRSRE RPSAQRSAPF ASASSSAYYG GYSRPYGGDK PWPSLLDKER
     EESLRQKRLS ERERIGELGA PEVWGLSPKN PEPDSDEHTP VEDEEPKKST TSASSSEDDK
     KKKRKSSHSK DRAKKKRKKK SSKRKHKKYS EDSDSDSESD TDSSDEDSKR RAKKAKKKDK
     KKKRRGKKYK KKKSKKNRKE SSDSSSKESQ EEFLENPWKD RSKAEEPSDL IGPEAPKTLA
     SQDDKPLNYG HALLPGEGAA MAEYVKAGKR IPRRGEIGLT SEEIASFECS GYVMSGSRHR
     RMEAVRLRKE NQIYSADEKR ALASFNQEER RKRENKILAS FREMVYRKTK GKDDK
//
ID   STX17_MOUSE             Reviewed;         301 AA.
AC   Q9D0I4; B1AVI3; Q9D330;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Syntaxin-17;
GN   Name=Stx17;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Colon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Implicated in vesicle trafficking to lysosomes. Could be
CC       involved in processes related to cell division (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane
CC       protein (By similarity). Note=Appears to be associated with a
CC       membrane compartment, perhaps a subset of the ER such as exit or
CC       entrance sites (By similarity).
CC   -!- SIMILARITY: Belongs to the syntaxin family.
CC   -!- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain.
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DR   EMBL; AK011400; BAB27592.1; -; mRNA.
DR   EMBL; AK018526; BAB31255.1; -; mRNA.
DR   EMBL; AK034718; BAC28806.1; -; mRNA.
DR   EMBL; AK154503; BAE32634.1; -; mRNA.
DR   EMBL; AL683893; CAM14010.1; -; Genomic_DNA.
DR   EMBL; BC028639; AAH28639.1; -; mRNA.
DR   IPI; IPI00316431; -.
DR   RefSeq; NP_080619.2; NM_026343.2.
DR   UniGene; Mm.171334; -.
DR   ProteinModelPortal; Q9D0I4; -.
DR   SMR; Q9D0I4; 161-228.
DR   STRING; Q9D0I4; -.
DR   PhosphoSite; Q9D0I4; -.
DR   PRIDE; Q9D0I4; -.
DR   Ensembl; ENSMUST00000064765; ENSMUSP00000068087; ENSMUSG00000061455.
DR   Ensembl; ENSMUST00000107720; ENSMUSP00000103348; ENSMUSG00000061455.
DR   GeneID; 67727; -.
DR   KEGG; mmu:67727; -.
DR   UCSC; uc008sux.1; mouse.
DR   CTD; 67727; -.
DR   MGI; MGI:1914977; Stx17.
DR   eggNOG; roNOG05543; -.
DR   GeneTree; ENSGT00390000013283; -.
DR   HOGENOM; HBG447405; -.
DR   HOVERGEN; HBG055257; -.
DR   InParanoid; Q9D0I4; -.
DR   OMA; IQKFIKV; -.
DR   OrthoDB; EOG4ZGPDF; -.
DR   PhylomeDB; Q9D0I4; -.
DR   NextBio; 325387; -.
DR   ArrayExpress; Q9D0I4; -.
DR   Bgee; Q9D0I4; -.
DR   CleanEx; MM_STX17; -.
DR   Genevestigator; Q9D0I4; -.
DR   GermOnline; ENSMUSG00000061455; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR   InterPro; IPR010989; t-SNARE.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   Pfam; PF05739; SNARE; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF47661; t-snare; 1.
DR   PROSITE; PS00914; SYNTAXIN; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Coiled coil; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    301       Syntaxin-17.
FT                                /FTId=PRO_0000210229.
FT   TOPO_DOM      1    229       Cytoplasmic (Potential).
FT   TRANSMEM    230    250       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   TOPO_DOM    251    301       Vesicular (Potential).
FT   DOMAIN      161    223       t-SNARE coiled-coil homology.
FT   COILED       49     76       Potential.
FT   COILED      101    128       Potential.
FT   MOD_RES      41     41       N6-acetyllysine (By similarity).
FT   MOD_RES     288    288       Phosphoserine (By similarity).
FT   CONFLICT    294    294       S -> G (in Ref. 1; BAB31255).
SQ   SEQUENCE   301 AA;  33221 MW;  3715C8D747FF7FF6 CRC64;
     MSEDEEKVKL RRLEPAIQKF TKIVIPTDLE RLRKHQINIE KYQRCRIWDK LHEEHINAGR
     TVQQLRSNIR EMEKLCLKVH KDDLVLLKRM IDPVKEAAAT ATAEFLQLHL ESVEELKKQV
     NDEELLQPSL TRSTTVDGVL HTGEAEAASQ SLTQIYALPE IPQDQNAAES WETLEADLIE
     LSHLVTDMSL LVSSQQEKID SIADHVNSAA VNVEEGTKNL QKAAKYKLAA LPVAGALIGG
     VVGGPIGLLA GFKVAGIAAA LGGGVLGFTG GKLIQRRKQK MMEKLTSSCP DLPSQSDKKR
     S
//
ID   ARL2_MOUSE              Reviewed;         184 AA.
AC   Q9D0J4; Q9WUM1;
DT   13-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=ADP-ribosylation factor-like protein 2;
GN   Name=Arl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Linari M., Hanzal-Bayer M., Becker J.;
RT   "Identification of Mus musculus arf like protein 2 (ARL2).";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION IN A COMPLEX WITH SLC25A4 AND ARL2BP, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=11809823; DOI=10.1091/mbc.01-05-0245;
RA   Sharer J.D., Shern J.F., Van Valkenburgh H., Wallace D.C., Kahn R.A.;
RT   "ARL2 and BART enter mitochondria and bind the adenine nucleotide
RT   transporter.";
RL   Mol. Biol. Cell 13:71-83(2002).
RN   [5]
RP   INTERACTION WITH PDE6D, GTP/GDP-BINDING, AND MUTAGENESIS OF THR-30 AND
RP   GLN-70.
RX   PubMed=15979089; DOI=10.1016/j.jmb.2005.05.036;
RA   Hanzal-Bayer M., Linari M., Wittinghofer A.;
RT   "Properties of the interaction of Arf-like protein 2 with PDEdelta.";
RL   J. Mol. Biol. 350:1074-1082(2005).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH HUMAN PDE6D AND
RP   GTP.
RX   MEDLINE=21977290; PubMed=11980706; DOI=10.1093/emboj/21.9.2095;
RA   Hanzal-Bayer M., Renault L., Roversi P., Wittinghofer A., Hillig R.C.;
RT   "The complex of Arl2-GTP and PDE delta: from structure to function.";
RL   EMBO J. 21:2095-2106(2002).
CC   -!- FUNCTION: Small GTP-binding protein which cycles between an
CC       inactive GDP-bound and an active GTP-bound form, and the rate of
CC       cycling is regulated by guanine nucleotide exchange factors (GEF)
CC       and GTPase-activating proteins (GAP). GTP-binding protein that
CC       does not act as an allosteric activator of the cholera toxin
CC       catalytic subunit. Regulates formation of new microtubules and
CC       centrosome integrity. Prevents the TBCD-induced microtubule
CC       destruction. Participates in association with TBCD, in the
CC       disassembly of the apical junction complexes. Antagonizes the
CC       effect of TBCD on epithelial cell detachment and tight and
CC       adherens junctions disassembly. Together with ARL2, plays a role
CC       in the nuclear translocation, retention and transcriptional
CC       activity of STAT3. Component of a regulated secretory pathway
CC       involved in Ca(2+)-dependent release of acetylcholine. Required
CC       for normal progress through the cell cycle.
CC   -!- SUBUNIT: Found in a complex with ARL2, ARL2BP and SLC25A6. Found
CC       in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E
CC       and TBCD. Interacts with SCOC and ELMOD2. Interacts with ARL2BP;
CC       the GTP-bound form interacts with ARL2BP. Interacts with TBCD; the
CC       GDP-bound form interacts preferentially with TBCD. Interacts with
CC       UNC119 (By similarity). Found in a complex with ARL2, ARL2BP and
CC       SLC25A4. Interacts with PDE6D; the GTP-bound form interacts with
CC       PDE6D.
CC   -!- INTERACTION:
CC       O43924:PDE6D (xeno); NbExp=1; IntAct=EBI-1033319, EBI-712685;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Cytoplasm, cytoskeleton, centrosome. Nucleus. Cytoplasm. Note=The
CC       complex formed with ARL2BP, ARL2 and SLC25A6 is expressed in
CC       mitochondria. Not detected in the Golgi, nucleus and on the
CC       mitotic spindle. Centrosome-associated throughout the cell cycle.
CC       Not detected to interphase microtubules (By similarity). The
CC       complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in
CC       mitochondria.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, lung, cerebellum, liver,
CC       kidney, hippocampus, spleen, cortex and heart (at protein level).
CC   -!- PTM: Not N-myristoylated.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
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DR   EMBL; AF143680; AAD33908.1; -; mRNA.
DR   EMBL; AK011366; BAB27572.1; -; mRNA.
DR   EMBL; BC060259; AAH60259.1; -; mRNA.
DR   IPI; IPI00315504; -.
DR   RefSeq; NP_062696.2; NM_019722.3.
DR   UniGene; Mm.21071; -.
DR   PDB; 1KSG; X-ray; 2.30 A; A=1-184.
DR   PDB; 1KSH; X-ray; 1.80 A; A=1-184.
DR   PDB; 1KSJ; X-ray; 2.60 A; A=1-184.
DR   PDBsum; 1KSG; -.
DR   PDBsum; 1KSH; -.
DR   PDBsum; 1KSJ; -.
DR   ProteinModelPortal; Q9D0J4; -.
DR   SMR; Q9D0J4; 1-179.
DR   DIP; DIP-36659N; -.
DR   IntAct; Q9D0J4; 3.
DR   MINT; MINT-236357; -.
DR   STRING; Q9D0J4; -.
DR   PhosphoSite; Q9D0J4; -.
DR   PRIDE; Q9D0J4; -.
DR   Ensembl; ENSMUST00000025893; ENSMUSP00000025893; ENSMUSG00000024944.
DR   GeneID; 56327; -.
DR   KEGG; mmu:56327; -.
DR   UCSC; uc008gho.1; mouse.
DR   CTD; 56327; -.
DR   MGI; MGI:1928393; Arl2.
DR   eggNOG; maNOG19143; -.
DR   GeneTree; ENSGT00600000084074; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG002073; -.
DR   InParanoid; Q9D0J4; -.
DR   OMA; TDGLVWV; -.
DR   OrthoDB; EOG4K0QPF; -.
DR   PhylomeDB; Q9D0J4; -.
DR   NextBio; 312306; -.
DR   ArrayExpress; Q9D0J4; -.
DR   Bgee; Q9D0J4; -.
DR   CleanEx; MM_ARL2; -.
DR   Genevestigator; Q9D0J4; -.
DR   GermOnline; ENSMUSG00000024944; Mus musculus.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051297; P:centrosome organization; ISS:UniProtKB.
DR   GO; GO:0051457; P:maintenance of protein location in nucleus; ISS:UniProtKB.
DR   GO; GO:0034260; P:negative regulation of GTPase activity; ISS:UniProtKB.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISS:UniProtKB.
DR   GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:UniProtKB.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0070830; P:tight junction assembly; ISS:UniProtKB.
DR   InterPro; IPR006688; ARF.
DR   InterPro; IPR006689; ARF/SAR.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   PANTHER; PTHR11711; ARF/SAR; 1.
DR   Pfam; PF00025; Arf; 1.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00177; ARF; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51417; ARF; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cytoplasm; Cytoskeleton; GTP-binding;
KW   Isopeptide bond; Lipoprotein; Mitochondrion; Myristate;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Ubl conjugation.
FT   INIT_MET      1      1       Removed (Potential).
FT   CHAIN         2    184       ADP-ribosylation factor-like protein 2.
FT                                /FTId=PRO_0000207454.
FT   NP_BIND      23     30       GTP.
FT   NP_BIND      66     70       GTP.
FT   NP_BIND     125    128       GTP.
FT   BINDING      68     68       GTP; via amide nitrogen.
FT   MOD_RES      45     45       Phosphoserine (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (Potential).
FT   CROSSLNK     71     71       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   MUTAGEN      30     30       T->L: Reduces affinity to GTP and GDP.
FT                                Inhibits interaction with PDE6D.
FT   MUTAGEN      70     70       Q->L: Does not reduce affinity fo GTP and
FT                                GDP. Enhances interaction with PDE6D.
FT   CONFLICT     33     33       L -> S (in Ref. 1; AAD33908).
FT   HELIX         2     12
FT   STRAND       16     22
FT   HELIX        29     35
FT   STRAND       48     54
FT   STRAND       60     67
FT   HELIX        71     80
FT   STRAND       85     92
FT   TURN         96     98
FT   HELIX        99    110
FT   HELIX       113    115
FT   STRAND      119    125
FT   HELIX       135    141
FT   HELIX       144    146
FT   STRAND      152    156
FT   TURN        159    162
FT   HELIX       165    178
SQ   SEQUENCE   184 AA;  20864 MW;  8B3741700BFED3F8 CRC64;
     MGLLTILKKM KQKERELRLL MLGLDNAGKT TILKKFNGED VDTISPTLGF NIKTLEHRGF
     KLNIWDVGGQ KSLRSYWRNY FESTDGLIWV VDSADRQRMQ DCQRELQSLL VEERLAGATL
     LIFANKQDLP GALSCNAIQE ALELDSIRSH HWRIQGCSAV TGEDLLPGID WLLDDISSRV
     FTAD
//
ID   ARM10_MOUSE             Reviewed;         306 AA.
AC   Q9D0L7; Q80ZY2; Q9CUN3; Q9CZ87;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Armadillo repeat-containing protein 10;
GN   Name=Armc10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N, and FVB/N-3; TISSUE=Colon, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: May play a role in cell survival and cell growth. May
CC       suppress the transcriptional activity of p53/TP53 (By similarity).
CC   -!- SUBUNIT: Interacts with the DNA-binding domain of p53/TP53 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9D0L7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D0L7-2; Sequence=VSP_027363;
CC   -!- SIMILARITY: Contains 1 ARM repeat.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB29775.1; Type=Frameshift; Positions=Several;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK011303; BAB27529.1; -; mRNA.
DR   EMBL; AK012872; BAB28526.1; -; mRNA.
DR   EMBL; AK015272; BAB29775.1; ALT_FRAME; mRNA.
DR   EMBL; BC038487; AAH38487.1; -; mRNA.
DR   EMBL; BC046281; AAH46281.2; -; mRNA.
DR   EMBL; BC058573; AAH58573.1; -; mRNA.
DR   IPI; IPI00137460; -.
DR   IPI; IPI00757909; -.
DR   RefSeq; NP_080310.1; NM_026034.4.
DR   UniGene; Mm.260782; -.
DR   ProteinModelPortal; Q9D0L7; -.
DR   SMR; Q9D0L7; 62-124.
DR   PhosphoSite; Q9D0L7; -.
DR   PRIDE; Q9D0L7; -.
DR   Ensembl; ENSMUST00000072896; ENSMUSP00000072669; ENSMUSG00000038525.
DR   Ensembl; ENSMUST00000073956; ENSMUSP00000073611; ENSMUSG00000038525.
DR   GeneID; 67211; -.
DR   KEGG; mmu:67211; -.
DR   UCSC; uc008wos.1; mouse.
DR   CTD; 67211; -.
DR   MGI; MGI:1914461; Armc10.
DR   eggNOG; roNOG06214; -.
DR   GeneTree; ENSGT00550000074488; -.
DR   HOVERGEN; HBG080349; -.
DR   OrthoDB; EOG4NKBWH; -.
DR   NextBio; 323890; -.
DR   ArrayExpress; Q9D0L7; -.
DR   Bgee; Q9D0L7; -.
DR   CleanEx; MM_ARMC10; -.
DR   Genevestigator; Q9D0L7; -.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR006911; DUF634.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF04826; DUF634; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50176; ARM_REPEAT; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endoplasmic reticulum; Growth regulation;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    306       Armadillo repeat-containing protein 10.
FT                                /FTId=PRO_0000297708.
FT   TRANSMEM      7     29       Helical; (Potential).
FT   REPEAT      101    143       ARM.
FT   MOD_RES      43     43       Phosphoserine.
FT   VAR_SEQ      44     57       Missing (in isoform 2).
FT                                /FTId=VSP_027363.
FT   CONFLICT     74     74       P -> T (in Ref. 1; BAB29775).
FT   CONFLICT    191    191       L -> P (in Ref. 1; BAB28526).
SQ   SEQUENCE   306 AA;  33311 MW;  127912DC336B4E04 CRC64;
     MGGARDVGWV AAGLVLGAGA CYCIYRLTRG PRRGGRRLRP SRSAEDLTDG SYDDILNAEQ
     LKKLLYLLES TDDPVITEKA LVTLGNNAAF STNQAIIREL GGIPIVGNKI NSLNQSIKEK
     ALNALNNLSV NVENQTKIKI YVPQVCEDVF ADPLNSAVQL AGLRLLTNMT VTNDYQHLLS
     GSVAGLFHLL LLGNGSTKVQ VLKLLLNLSE NPAMTEGLLS VQVDSSFLSL YDGQVANEIL
     LRALTLFQNI NNCLKVEGRL ANQIPFAKGS LFFLLYGEEC AQKMRALACH HDVDVKEKAL
     AIKPKF
//
ID   MCES_MOUSE              Reviewed;         465 AA.
AC   Q9D0L8; Q3V3U9; Q6ZQC6; Q9D5F1;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=mRNA cap guanine-N7 methyltransferase;
DE            EC=2.1.1.56;
DE   AltName: Full=RG7MT1;
DE   AltName: Full=mRNA (guanine-N(7)-)-methyltransferase;
DE   AltName: Full=mRNA cap methyltransferase;
GN   Name=Rnmt; Synonyms=Kiaa0398;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-15 AND SER-64,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-100, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: mRNA-capping methyltransferase that methylates the N7
CC       position of the added guanosine to the 5'-cap structure of mRNAs.
CC       Binds RNA containing 5'-terminal GpppC (By similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + G(5')pppR-RNA = S-
CC       adenosyl-L-homocysteine + m(7)G(5')pppR-RNA.
CC   -!- SUBUNIT: Interacts with importin alpha, leading to stimulate both
CC       RNA-binding and methyltransferase activity. Interaction with
CC       importin alpha and beta is required for its nuclear localization,
CC       importin beta dissociating in response to RanGTP, allowing RNMT-
CC       importin alpha to bind RNA substrates. Interacts with elongating
CC       form of polymerase II and RNGTT (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9D0L8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D0L8-2; Sequence=VSP_020243;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q9D0L8-3; Sequence=VSP_020242;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. mRNA cap
CC       methyltransferase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC97940.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK129130; BAC97940.1; ALT_INIT; mRNA.
DR   EMBL; AK011300; BAB27527.1; -; mRNA.
DR   EMBL; AK015403; BAB29834.1; -; mRNA.
DR   EMBL; AK031780; BAE43278.1; -; mRNA.
DR   EMBL; BC021794; AAH21794.1; -; mRNA.
DR   EMBL; AK082331; BAC38469.1; -; mRNA.
DR   IPI; IPI00317422; -.
DR   IPI; IPI00453849; -.
DR   IPI; IPI00785256; -.
DR   RefSeq; NP_001164424.1; NM_001170953.1.
DR   RefSeq; NP_080716.1; NM_026440.4.
DR   UniGene; Mm.27544; -.
DR   HSSP; Q8SR66; 1RI5.
DR   ProteinModelPortal; Q9D0L8; -.
DR   SMR; Q9D0L8; 158-465.
DR   STRING; Q9D0L8; -.
DR   PhosphoSite; Q9D0L8; -.
DR   PRIDE; Q9D0L8; -.
DR   Ensembl; ENSMUST00000009679; ENSMUSP00000009679; ENSMUSG00000009535.
DR   Ensembl; ENSMUST00000025427; ENSMUSP00000025427; ENSMUSG00000009535.
DR   GeneID; 67897; -.
DR   KEGG; mmu:67897; -.
DR   UCSC; uc008fnj.1; mouse.
DR   UCSC; uc008fnk.1; mouse.
DR   CTD; 67897; -.
DR   MGI; MGI:1915147; Rnmt.
DR   eggNOG; roNOG09678; -.
DR   GeneTree; ENSGT00390000002368; -.
DR   HOGENOM; HBG377892; -.
DR   HOVERGEN; HBG081963; -.
DR   InParanoid; Q9D0L8; -.
DR   OMA; FMRNFNN; -.
DR   OrthoDB; EOG4FXR80; -.
DR   PhylomeDB; Q9D0L8; -.
DR   BRENDA; 2.1.1.56; 244.
DR   NextBio; 325886; -.
DR   ArrayExpress; Q9D0L8; -.
DR   Bgee; Q9D0L8; -.
DR   CleanEx; MM_RNMT; -.
DR   Genevestigator; Q9D0L8; -.
DR   GermOnline; ENSMUSG00000009535; Mus musculus.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0004482; F:mRNA (guanine-N7-)-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0006370; P:mRNA capping; ISS:UniProtKB.
DR   InterPro; IPR016899; mRNA_G-N7_MeTrfase.
DR   InterPro; IPR004971; Pox_MCEL.
DR   Pfam; PF03291; Pox_MCEL; 1.
DR   PIRSF; PIRSF028762; ABD1; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Methyltransferase; mRNA capping;
KW   mRNA processing; Nucleus; Phosphoprotein; RNA-binding;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    465       mRNA cap guanine-N7 methyltransferase.
FT                                /FTId=PRO_0000248323.
FT   REGION      165    166       mRNA cap binding (By similarity).
FT   MOTIF       113    115       Nuclear localization signal (By
FT                                similarity).
FT   BINDING     169    169       S-adenosyl-L-methionine (By similarity).
FT   BINDING     194    194       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING     197    197       mRNA cap (By similarity).
FT   BINDING     203    203       mRNA cap (By similarity).
FT   BINDING     216    216       S-adenosyl-L-methionine (By similarity).
FT   BINDING     228    228       mRNA cap (By similarity).
FT   BINDING     250    250       S-adenosyl-L-methionine (By similarity).
FT   BINDING     273    273       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen (By similarity).
FT   BINDING     277    277       mRNA cap (By similarity).
FT   BINDING     359    359       mRNA cap (By similarity).
FT   BINDING     456    456       mRNA cap (By similarity).
FT   MOD_RES      11     11       Phosphoserine.
FT   MOD_RES      15     15       Phosphoserine.
FT   MOD_RES      64     64       Phosphoserine.
FT   MOD_RES     100    100       Phosphoserine.
FT   VAR_SEQ     315    369       Missing (in isoform 3).
FT                                /FTId=VSP_020242.
FT   VAR_SEQ     370    465       Missing (in isoform 2).
FT                                /FTId=VSP_020243.
FT   CONFLICT     32     32       E -> K (in Ref. 2; BAB29834).
FT   CONFLICT     53     53       L -> H (in Ref. 2; BAE43278).
SQ   SEQUENCE   465 AA;  53291 MW;  D1422D9621EE2A1A CRC64;
     MEGSAKASVA SDPESPPGGN EPAAASGQRL PENTPPCQQV DQPKMQKEFG EDLVEQNSSY
     VQDSPSKKRK LDVEIILEEK HSEDDGGSAK RSKLERGDVS EDEPSLGRLN QTKRKLQPQD
     DEVPQKLQKL EEGHSSAVAA HYNELQEVGL AKRSQSRIFY LRNFNNWIKS ILIGEILEKV
     RQRKTRDITV LDLGCGKGGD LLKWRKGRIS RLVCADIADI SMKQCQQRYE DMRCRRDNEH
     IFSAEFITAD CSKELLVEKF RDPEMYFDVC SCQFACHYSF ESQVQADTML RNACGRLNPG
     GYFIGTTPNS FELIRRLEAS ETESFGNEIY TVKFQKKGNY PLFGCKYDFN LEGVVDVPEF
     LVYFPLLTEM AKKYNMKLIY KKTFLEFYEE KIKNNENKML LKRMQALEQY PAHENSKLAS
     EKVGDYTHAA EYLKKSQVRL PLGTLSKSEW EATSIYLVFA FEKQQ
//
ID   KPRA_MOUSE              Reviewed;         356 AA.
AC   Q9D0M1;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Phosphoribosyl pyrophosphate synthase-associated protein 1;
DE            Short=PRPP synthase-associated protein 1;
DE   AltName: Full=39 kDa phosphoribosypyrophosphate synthase-associated protein;
DE            Short=PAP39;
GN   Name=Prpsap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Seems to play a negative regulatory role in 5-
CC       phosphoribose 1-diphosphate synthesis (By similarity).
CC   -!- SUBUNIT: Binds to PRPS1 and PRPS2 (By similarity).
CC   -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase
CC       family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK011290; BAB27520.1; -; mRNA.
DR   EMBL; BC029621; AAH29621.1; -; mRNA.
DR   IPI; IPI00755389; -.
DR   RefSeq; NP_080640.1; NM_026364.1.
DR   UniGene; Mm.25125; -.
DR   UniGene; Mm.478758; -.
DR   ProteinModelPortal; Q9D0M1; -.
DR   SMR; Q9D0M1; 7-350.
DR   PhosphoSite; Q9D0M1; -.
DR   PRIDE; Q9D0M1; -.
DR   Ensembl; ENSMUST00000021153; ENSMUSP00000021153; ENSMUSG00000015869.
DR   Ensembl; ENSMUST00000106391; ENSMUSP00000101999; ENSMUSG00000015869.
DR   GeneID; 67763; -.
DR   KEGG; mmu:67763; -.
DR   NMPDR; fig|10090.3.peg.25672; -.
DR   UCSC; uc007mld.1; mouse.
DR   CTD; 67763; -.
DR   MGI; MGI:1915013; Prpsap1.
DR   GeneTree; ENSGT00550000074583; -.
DR   HOVERGEN; HBG001520; -.
DR   InParanoid; Q9D0M1; -.
DR   OrthoDB; EOG4C87SQ; -.
DR   PhylomeDB; Q9D0M1; -.
DR   ArrayExpress; Q9D0M1; -.
DR   Bgee; Q9D0M1; -.
DR   Genevestigator; Q9D0M1; -.
DR   GermOnline; ENSMUSG00000015869; Mus musculus.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:InterPro.
DR   GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005946; Rib-P_diPkinase.
DR   TIGRFAMs; TIGR01251; ribP_PPkin; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Nucleotide biosynthesis; Phosphoprotein.
FT   CHAIN         1    356       Phosphoribosyl pyrophosphate synthase-
FT                                associated protein 1.
FT                                /FTId=PRO_0000141080.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     215    215       Phosphoserine.
SQ   SEQUENCE   356 AA;  39432 MW;  0BCEA75BFE55401E CRC64;
     MNAARTGYRV FSANSTAACT ELAKRITERL GAELGKSVVY QETNGETRVE IKESVRGQDI
     FIIQTIPRDV NTAVMELLIM AYALKTACAR NIIGVIPYFP YSKQSKMRKR GSIVCKLLAS
     MLAKAGLTHI ITMDLHQKEI QGFFSFPVDN LRASPFLLQY IQEEIPNYRN AVIVAKSPDA
     AKRAQSYAER LRLGLAVIHG EAQCTELDMD DGRHSPPMVK NATVHPGLEL PLMMAKEKPP
     ITVVGDVGGR IAIIVDDIID DVESFVAAAE ILKERGAYKI YVMATHGILS AEAPRLIEES
     PIDEVVVTNT VPHELQKLQC PKIKTVDISL ILSEAIRRIH NGESMAYLFR NITVDD
//
ID   DYL2_MOUSE              Reviewed;          89 AA.
AC   Q9D0M5; A7M7R8; Q3TFB4;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Dynein light chain 2, cytoplasmic;
DE   AltName: Full=8 kDa dynein light chain b;
DE            Short=DLC8;
DE            Short=DLC8b;
DE   AltName: Full=Dynein light chain LC8-type 2;
GN   Name=Dynll2; Synonyms=Dlc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH BMF, IDENTIFICATION IN
RP   THE CYTOPLASMIC DYNEIN 1 COMPLEX, AND IDENTIFICATION IN THE MYOSIN V
RP   COMPLEX.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=21432178; PubMed=11546872; DOI=10.1126/science.1062257;
RA   Puthalakath H., Villunger A., O'Reilly L.A., Beaumont J.G.,
RA   Coultas L., Cheney R.E., Huang D.C.S., Strasser A.;
RT   "Bmf: a proapoptotic BH3-only protein regulated by interaction with
RT   the myosin V actin motor complex, activated by anoikis.";
RL   Science 293:1829-1832(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, Kidney, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH DYNC1I1.
RX   PubMed=11148209; DOI=10.1074/jbc.M010320200;
RA   Lo K.W., Naisbitt S., Fan J.S., Sheng M., Zhang M.;
RT   "The 8-kDa dynein light chain binds to its targets via a conserved
RT   (K/R)XTQT motif.";
RL   J. Biol. Chem. 276:14059-14066(2001).
RN   [6]
RP   STRUCTURE BY NMR, SUBCELLULAR LOCATION, AND BINDING SITE.
RX   PubMed=14561217; DOI=10.1042/BJ20031251;
RA   Day C.L., Puthalakath H., Skea G., Strasser A., Barsukov I.,
RA   Lian L.Y., Huang D.C., Hinds M.G.;
RT   "Localization of dynein light chains 1 and 2 and their pro-apoptotic
RT   ligands.";
RL   Biochem. J. 377:597-605(2004).
CC   -!- FUNCTION: Acts as one of several non-catalytic accessory
CC       components of the cytoplasmic dynein 1 complex that are thought to
CC       be involved in linking dynein to cargos and to adapter proteins
CC       that regulate dynein function. Cytoplasmic dynein 1 acts as a
CC       motor for the intracellular retrograde motility of vesicles and
CC       organelles along microtubules. May play a role in changing or
CC       maintaining the spatial distribution of cytoskeletal structures
CC       (By similarity).
CC   -!- SUBUNIT: Homodimer. The cytoplasmic dynein 1 complex consists of
CC       two catalytic heavy chains (HCs) and a number of non-catalytic
CC       subunits which present intermediate chains (ICs), light
CC       intermediate chains (LICs) and light chains (LCs); the composition
CC       seems to vary in respect to the IC, LIC and LC composition. The
CC       heavy chain homodimer serves as a scaffold for the probable
CC       homodimeric assembly of the respective non-catalytic subunits.
CC       Dynein ICs and LICs bind directly to the HC dimer and the LCs
CC       assemble on the IC dimer. Interacts with DYNC1I1. Interacts with
CC       BMF. Component of the myosin V motor complex.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- SIMILARITY: Belongs to the dynein light chain family.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AY029255; AAK38749.1; -; mRNA.
DR   EMBL; AK011284; BAB27516.1; -; mRNA.
DR   EMBL; AK028319; BAC25877.1; -; mRNA.
DR   EMBL; AK049645; BAC33856.1; -; mRNA.
DR   EMBL; AK078434; BAC37271.1; -; mRNA.
DR   EMBL; AK160114; BAE35638.1; -; mRNA.
DR   EMBL; AK169212; BAE40984.1; -; mRNA.
DR   EMBL; AL606805; CAO91831.1; -; Genomic_DNA.
DR   EMBL; BC011289; AAH11289.1; -; mRNA.
DR   EMBL; BC040822; AAH40822.1; -; mRNA.
DR   IPI; IPI00132734; -.
DR   RefSeq; NP_001161943.1; NM_001168471.1.
DR   RefSeq; NP_001161944.1; NM_001168472.1.
DR   RefSeq; NP_080832.1; NM_026556.4.
DR   UniGene; Mm.246436; -.
DR   PDB; 1RE6; NMR; -; A/B=1-89.
DR   PDBsum; 1RE6; -.
DR   ProteinModelPortal; Q9D0M5; -.
DR   SMR; Q9D0M5; 1-89.
DR   IntAct; Q9D0M5; 1.
DR   STRING; Q9D0M5; -.
DR   PhosphoSite; Q9D0M5; -.
DR   REPRODUCTION-2DPAGE; Q9D0M5; -.
DR   PRIDE; Q9D0M5; -.
DR   Ensembl; ENSMUST00000020775; ENSMUSP00000020775; ENSMUSG00000020483.
DR   Ensembl; ENSMUST00000107923; ENSMUSP00000103556; ENSMUSG00000020483.
DR   GeneID; 68097; -.
DR   KEGG; mmu:68097; -.
DR   UCSC; uc007kva.1; mouse.
DR   CTD; 68097; -.
DR   MGI; MGI:1915347; Dynll2.
DR   eggNOG; roNOG16765; -.
DR   GeneTree; ENSGT00390000000378; -.
DR   HOGENOM; HBG627578; -.
DR   HOVERGEN; HBG002133; -.
DR   InParanoid; Q9D0M5; -.
DR   OMA; EKFTIEK; -.
DR   OrthoDB; EOG473PSW; -.
DR   PhylomeDB; Q9D0M5; -.
DR   NextBio; 326412; -.
DR   ArrayExpress; Q9D0M5; -.
DR   Bgee; Q9D0M5; -.
DR   CleanEx; MM_DYNLL2; -.
DR   Genevestigator; Q9D0M5; -.
DR   GermOnline; ENSMUSG00000020483; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030286; C:dynein complex; NAS:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0016459; C:myosin complex; IDA:UniProtKB.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0046907; P:intracellular transport; NAS:UniProtKB.
DR   GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR   InterPro; IPR019763; Dynein_light_1/2_CS.
DR   InterPro; IPR001372; Dynein_light_chain_typ-1/2.
DR   Gene3D; G3DSA:3.30.740.10; Dynein_light1; 1.
DR   PANTHER; PTHR11886; Dynein_light1; 1.
DR   Pfam; PF01221; Dynein_light; 1.
DR   SUPFAM; SSF54648; Dynein_light_chain_typ-1/2; 1.
DR   PROSITE; PS01239; DYNEIN_LIGHT_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Cytoskeleton; Dynein;
KW   Microtubule; Motor protein; Transport.
FT   CHAIN         1     89       Dynein light chain 2, cytoplasmic.
FT                                /FTId=PRO_0000195133.
FT   SITE         41     41       Interaction with myosin V motor complex.
FT   MOD_RES       5      5       N6-acetyllysine (By similarity).
FT   STRAND        7     11
FT   HELIX        16     31
FT   HELIX        36     50
FT   STRAND       57     61
FT   TURN         67     69
FT   STRAND       71     78
FT   STRAND       81     87
SQ   SEQUENCE   89 AA;  10350 MW;  45364D32C0077F8E CRC64;
     MSDRKAVIKN ADMSEDMQQD AVDCATQAME KYNIEKDIAA YIKKEFDKKY NPTWHCIVGR
     NFGSYVTHET KHFIYFYLGQ VAILLFKSG
//
ID   RM45_MOUSE              Reviewed;         306 AA.
AC   Q9D0Q7; Q3TZL8; Q8VDW2;
DT   04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=39S ribosomal protein L45, mitochondrial;
DE            Short=L45mt;
DE            Short=MRP-L45;
DE   Flags: Precursor;
GN   Name=Mrpl45;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the ribosomal protein L45 family.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK011163; BAB27440.1; -; mRNA.
DR   EMBL; AK081922; BAC38375.1; -; mRNA.
DR   EMBL; AK157771; BAE34190.1; -; mRNA.
DR   EMBL; BC020130; AAH20130.1; -; mRNA.
DR   IPI; IPI00132895; -.
DR   RefSeq; NP_080203.1; NM_025927.4.
DR   UniGene; Mm.5381; -.
DR   ProteinModelPortal; Q9D0Q7; -.
DR   PhosphoSite; Q9D0Q7; -.
DR   PRIDE; Q9D0Q7; -.
DR   Ensembl; ENSMUST00000019026; ENSMUSP00000019026; ENSMUSG00000018882.
DR   GeneID; 67036; -.
DR   KEGG; mmu:67036; -.
DR   NMPDR; fig|10090.3.peg.25159; -.
DR   UCSC; uc007ldx.1; mouse.
DR   CTD; 67036; -.
DR   MGI; MGI:1914286; Mrpl45.
DR   GeneTree; ENSGT00390000012679; -.
DR   HOGENOM; HBG714314; -.
DR   HOVERGEN; HBG044506; -.
DR   InParanoid; Q9D0Q7; -.
DR   OMA; SRALGWW; -.
DR   OrthoDB; EOG4HHP2V; -.
DR   PhylomeDB; Q9D0Q7; -.
DR   NextBio; 323370; -.
DR   ArrayExpress; Q9D0Q7; -.
DR   Bgee; Q9D0Q7; -.
DR   CleanEx; MM_MRPL45; -.
DR   Genevestigator; Q9D0Q7; -.
DR   GermOnline; ENSMUSG00000018882; Mus musculus.
DR   GO; GO:0005744; C:mitochondrial inner membrane presequence translocase complex; IEA:InterPro.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   InterPro; IPR007379; Tim44-related/Ribosome_L45.
DR   Pfam; PF04280; Tim44; 1.
DR   SMART; SM00978; Tim44; 1.
PE   2: Evidence at transcript level;
KW   Mitochondrion; Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    306       39S ribosomal protein L45, mitochondrial.
FT                                /FTId=PRO_0000030564.
FT   CONFLICT    130    130       A -> T (in Ref. 2; AAH20130).
SQ   SEQUENCE   306 AA;  35411 MW;  6476F542371FE5DC CRC64;
     MAAPVPRGLS SLYRTLGWWS RQPILVTQST TVVQVKTKSR FRPPTPEPKY KTEKEFLEYA
     RKAGLVIPQE RLERPIHLAC TAGIFDPYVP PEGDARMSSL SKEGLTQRTE RLRKNAASQL
     AIRKIREFDA NFKTKDFPEK AKDIFIEAHL CLNNSDHDRL HTLVTEHCFP DMVWDLKYKT
     VRWGFVESLE PAQVVHVRCS GLVNQSNMYG QVTVRLHTRQ TLAIYDRFGR LMYGQEDVPK
     DVLEYVVFER HLMNPYGSWR MHAKIVPAWA PPKQPILKTL MIPGPQLKPW EEYEETQGEA
     QKPQLA
//
ID   LSM12_MOUSE             Reviewed;         195 AA.
AC   Q9D0R8; A2AWS3;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Protein LSM12 homolog;
GN   Name=Lsm12;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-73 AND THR-75, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SIMILARITY: Belongs to the LSM12 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM16077.1; Type=Erroneous gene model prediction;
CC       Sequence=CAM25069.1; Type=Erroneous gene model prediction;
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DR   EMBL; AK011126; BAB27419.1; -; mRNA.
DR   EMBL; AK075668; BAC35885.1; -; mRNA.
DR   EMBL; AK132889; BAE21407.1; -; mRNA.
DR   EMBL; AK151118; BAE30127.1; -; mRNA.
DR   EMBL; BX323852; CAM16076.1; -; Genomic_DNA.
DR   EMBL; AL954730; CAM16076.1; JOINED; Genomic_DNA.
DR   EMBL; BX323852; CAM16077.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL954730; CAM16077.1; JOINED; Genomic_DNA.
DR   EMBL; AL954730; CAM25068.1; -; Genomic_DNA.
DR   EMBL; BX323852; CAM25068.1; JOINED; Genomic_DNA.
DR   EMBL; AL954730; CAM25069.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BX323852; CAM25069.1; JOINED; Genomic_DNA.
DR   EMBL; BC027784; AAH27784.1; -; mRNA.
DR   IPI; IPI00132973; -.
DR   RefSeq; NP_766535.1; NM_172947.3.
DR   UniGene; Mm.259079; -.
DR   ProteinModelPortal; Q9D0R8; -.
DR   PhosphoSite; Q9D0R8; -.
DR   PRIDE; Q9D0R8; -.
DR   Ensembl; ENSMUST00000021297; ENSMUSP00000021297; ENSMUSG00000020922.
DR   GeneID; 268490; -.
DR   KEGG; mmu:268490; -.
DR   UCSC; uc007lqs.1; mouse.
DR   CTD; 268490; -.
DR   MGI; MGI:1919592; Lsm12.
DR   eggNOG; roNOG15352; -.
DR   GeneTree; ENSGT00390000006956; -.
DR   HOGENOM; HBG446415; -.
DR   HOVERGEN; HBG057351; -.
DR   InParanoid; Q9D0R8; -.
DR   OMA; TLKCASS; -.
DR   OrthoDB; EOG4CJVJ4; -.
DR   PhylomeDB; Q9D0R8; -.
DR   NextBio; 392331; -.
DR   ArrayExpress; Q9D0R8; -.
DR   Bgee; Q9D0R8; -.
DR   CleanEx; MM_LSM12; -.
DR   Genevestigator; Q9D0R8; -.
DR   InterPro; IPR019181; RNA-processing_Lsm_domain.
DR   PANTHER; PTHR13542; RNA-processing_Lsm_domain; 1.
DR   Pfam; PF09793; AD; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    195       Protein LSM12 homolog.
FT                                /FTId=PRO_0000305127.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      73     73       Phosphothreonine.
FT   MOD_RES      75     75       Phosphothreonine.
FT   MOD_RES     168    168       N6-acetyllysine (By similarity).
FT   MOD_RES     195    195       Phosphoserine (By similarity).
SQ   SEQUENCE   195 AA;  21701 MW;  BCEDE62DA43D86C7 CRC64;
     MAAPPGEYFS VGSQVSCRTC QEQRLQGEVV AFDYQSKMLA LKCPSSSGKP NHADILLINL
     QYVSEVEIIN DRTETPPPLA SLNVSKLASK ARTEKEEKLS QAYAISAGVS LEGQQLFQTI
     HKTIKDCKWQ EKNIVVMEEV VITPPYQVEN CKGKEGSALS HVRKIVEKHF RDVESQKILQ
     RSQAQQPQKE AALSS
//
ID   RCAS1_MOUSE             Reviewed;         213 AA.
AC   Q9D0V7; Q0VET4; Q3TVG2; Q3TWY4; Q9QYD0;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2003, sequence version 2.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Receptor-binding cancer antigen expressed on SiSo cells;
DE   AltName: Full=Cancer-associated surface antigen RCAS1;
DE   AltName: Full=Estrogen receptor-binding fragment-associated gene 9 protein;
GN   Name=Ebag9; Synonyms=Rcas1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND INDUCTION.
RC   TISSUE=Brain;
RX   MEDLINE=21268948; PubMed=11374862; DOI=10.1006/bbrc.2001.4892;
RA   Tsuchiya F., Ikeda K., Tsutsumi O., Hiroi H., Momoeda M., Taketani Y.,
RA   Muramatsu M., Inoue S.;
RT   "Molecular cloning and characterization of mouse EBAG9, homolog of a
RT   human cancer associated surface antigen: expression and regulation by
RT   estrogen.";
RL   Biochem. Biophys. Res. Commun. 284:2-10(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RA   Nakashima M., Sonoda K., Watanabe T.;
RT   "Human type II receptor like cancer associated surface antigen
RT   (RCAS1).";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May participate in suppression of cell proliferation and
CC       induces apoptotic cell death through activation of interleukin-1-
CC       beta converting enzyme (ICE)-like proteases (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type
CC       III membrane protein (By similarity). Note=Predominantly located
CC       in the Golgi (By similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain,
CC       spleen, liver, kidney and testis.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the developing embryo.
CC   -!- INDUCTION: By 17-beta-estradiol (E2).
CC   -!- DOMAIN: The coiled coil domain is necessary for the
CC       homodimerization (By similarity).
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AY009091; AAG41054.1; -; mRNA.
DR   EMBL; AF076524; AAF23857.1; -; mRNA.
DR   EMBL; AK004366; BAB23277.1; -; mRNA.
DR   EMBL; AK159499; BAE35132.1; -; mRNA.
DR   EMBL; AK160149; BAE35657.1; -; mRNA.
DR   EMBL; BC108397; AAI08398.1; -; mRNA.
DR   EMBL; BC119118; AAI19119.1; -; mRNA.
DR   EMBL; BC119120; AAI19121.1; -; mRNA.
DR   EMBL; BC144740; AAI44741.1; -; mRNA.
DR   IPI; IPI00154113; -.
DR   PIR; JC7696; JC7696.
DR   RefSeq; NP_062353.3; NM_019480.4.
DR   UniGene; Mm.287896; -.
DR   ProteinModelPortal; Q9D0V7; -.
DR   STRING; Q9D0V7; -.
DR   PhosphoSite; Q9D0V7; -.
DR   PRIDE; Q9D0V7; -.
DR   Ensembl; ENSMUST00000022964; ENSMUSP00000022964; ENSMUSG00000022339.
DR   GeneID; 55960; -.
DR   KEGG; mmu:55960; -.
DR   UCSC; uc007vpz.1; mouse.
DR   CTD; 55960; -.
DR   MGI; MGI:1859920; Ebag9.
DR   GeneTree; ENSGT00390000004040; -.
DR   HOGENOM; HBG279385; -.
DR   HOVERGEN; HBG059707; -.
DR   InParanoid; Q9D0V7; -.
DR   OMA; FKICTCL; -.
DR   OrthoDB; EOG4XPQGZ; -.
DR   PhylomeDB; Q9D0V7; -.
DR   NextBio; 311658; -.
DR   ArrayExpress; Q9D0V7; -.
DR   Bgee; Q9D0V7; -.
DR   Genevestigator; Q9D0V7; -.
DR   GermOnline; ENSMUSG00000022339; Mus musculus.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   InterPro; IPR017025; Cancer-assoc_antigen_RCAS1.
DR   PIRSF; PIRSF034247; RCAS1; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Coiled coil; Golgi apparatus; Membrane; Phosphoprotein;
KW   Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN         1    213       Receptor-binding cancer antigen expressed
FT                                on SiSo cells.
FT                                /FTId=PRO_0000097196.
FT   TOPO_DOM      1      7       Extracellular (Potential).
FT   TRANSMEM      8     27       Helical; Signal-anchor for type III
FT                                membrane protein; (Potential).
FT   TOPO_DOM     28    213       Cytoplasmic (Potential).
FT   COILED      163    211       Potential.
FT   COMPBIAS    160    163       Poly-Glu.
FT   MOD_RES      36     36       Phosphoserine.
FT   MOD_RES      41     41       Phosphothreonine (By similarity).
FT   MOD_RES      48     48       Phosphotyrosine (By similarity).
FT   MOD_RES      86     86       Phosphoserine (By similarity).
FT   MOD_RES      94     94       Phosphotyrosine (By similarity).
FT   CONFLICT     11     11       V -> G (in Ref. 3; AAF23857).
FT   CONFLICT    115    115       P -> A (in Ref. 3; AAF23857).
FT   CONFLICT    150    150       D -> G (in Ref. 3; BAE35132).
FT   CONFLICT    157    157       N -> S (in Ref. 3; AAF23857).
SQ   SEQUENCE   213 AA;  24319 MW;  349FAD1E2AEFF529 CRC64;
     MAITQFRLFK VCTCLATVFS FLKRLICRSG RGRKLSGDQI TLPTTVDYSS VPKQTDVEEW
     TSWDEDAPTS VKIEGGNGNV ATQQNSLEQL EPDYFKDMTP TIRKTQKIVI KKREPLNFGV
     PDGSTGFSSR LAATQDMPFI HQSSELGDLD TWQENSNAWE EEEDAAWQAE EVLRQQKIAD
     REKRAAEQQR KKMEKEAQRL MKKEQNKIGV KLS
//
ID   CBY1_MOUSE              Reviewed;         127 AA.
AC   Q9D1C2;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Protein chibby homolog 1;
DE   AltName: Full=Cytosolic leucine-rich protein;
DE   AltName: Full=PIGEA-14;
DE   AltName: Full=PKD2 interactor, Golgi and endoplasmic reticulum-associated 1;
GN   Name=Cby1; Synonyms=Cby, Pgea1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Huang C.-H.;
RT   "A novel cytosolic leucine-rich protein.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=17261658; DOI=10.1161/CIRCULATIONAHA.106.642298;
RA   Singh A.M., Li F.-Q., Hamazaki T., Kasahara H., Takemaru K.,
RA   Terada N.;
RT   "Chibby, an antagonist of the Wnt/beta-catenin pathway, facilitates
RT   cardiomyocyte differentiation of murine embryonic stem cells.";
RL   Circulation 115:617-626(2007).
RN   [5]
RP   FUNCTION.
RX   PubMed=17403895; DOI=10.1128/MCB.01640-06;
RA   Li F.-Q., Singh A.M., Mofunanya A., Love D., Terada N., Moon R.T.,
RA   Takemaru K.;
RT   "Chibby promotes adipocyte differentiation through inhibition of beta-
RT   catenin signaling.";
RL   Mol. Cell. Biol. 27:4347-4354(2007).
CC   -!- FUNCTION: Inhibits the Wnt/Wingless pathway by binding to beta-
CC       catenin and inhibiting beta-catenin-mediated transcriptional
CC       activation through competition with TCF/LEF transcription factors.
CC       Has also been shown to play a role in regulating the intracellular
CC       trafficking of polycystin-2/PKD2 and possibly of other
CC       intracellular proteins (By similarity). Promotes adipocyte and
CC       cardiomyocyte differentiation.
CC   -!- SUBUNIT: Homodimer. Interacts with polycystin-2/PKD2 and GM130.
CC       Interacts with the C-terminal region of beta-catenin (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle (By similarity). Golgi
CC       apparatus, trans-Golgi network (By similarity). Note=Nuclear, in a
CC       punctate manner. Also found in the trans-Golgi (By similarity).
CC   -!- TISSUE SPECIFICITY: Found in heart, brain, lung, liver, muscle,
CC       kidney and testis. Levels are approximately 3-fold higher in
CC       embryonic and adult heart than in lung or liver.
CC   -!- DEVELOPMENTAL STAGE: Ubiquitously expressed in early stages of
CC       embryonic stem cell differentiation but decreases at later stages
CC       when high expression is restricted to cardiomyocytes.
CC   -!- MISCELLANEOUS: 'Chibby' is Japanese for 'small'; the gene was so
CC       named for the RNAi phenotype seen in flies.
CC   -!- SIMILARITY: Belongs to the chibby family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF331040; AAL56061.1; -; mRNA.
DR   EMBL; AK003719; BAB22956.1; -; mRNA.
DR   EMBL; BC005733; AAH05733.1; -; mRNA.
DR   IPI; IPI00133582; -.
DR   RefSeq; NP_082910.1; NM_028634.3.
DR   UniGene; Mm.294441; -.
DR   ProteinModelPortal; Q9D1C2; -.
DR   STRING; Q9D1C2; -.
DR   PhosphoSite; Q9D1C2; -.
DR   PRIDE; Q9D1C2; -.
DR   Ensembl; ENSMUST00000023064; ENSMUSP00000023064; ENSMUSG00000022428.
DR   GeneID; 73739; -.
DR   KEGG; mmu:73739; -.
DR   UCSC; uc007wuc.1; mouse.
DR   CTD; 73739; -.
DR   MGI; MGI:1920989; Cby1.
DR   eggNOG; maNOG20586; -.
DR   GeneTree; ENSGT00510000047043; -.
DR   HOGENOM; HBG715193; -.
DR   HOVERGEN; HBG050816; -.
DR   InParanoid; Q9D1C2; -.
DR   OMA; LRKRNQQ; -.
DR   OrthoDB; EOG4JT072; -.
DR   PhylomeDB; Q9D1C2; -.
DR   NextBio; 338953; -.
DR   ArrayExpress; Q9D1C2; -.
DR   Bgee; Q9D1C2; -.
DR   CleanEx; MM_CBY1; -.
DR   Genevestigator; Q9D1C2; -.
DR   GermOnline; ENSMUSG00000022428; Mus musculus.
DR   GO; GO:0005932; C:microtubule basal body; IDA:MGI.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:UniProtKB.
DR   GO; GO:0042384; P:cilium assembly; IMP:MGI.
DR   GO; GO:0045444; P:fat cell differentiation; IMP:UniProtKB.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt receptor signaling pathway; IMP:MGI.
PE   2: Evidence at transcript level;
KW   Coiled coil; Differentiation; Golgi apparatus; Nucleus;
KW   Phosphoprotein.
FT   CHAIN         1    127       Protein chibby homolog 1.
FT                                /FTId=PRO_0000058355.
FT   REGION       60    112       Minimal region for the interaction with
FT                                PKD2 (By similarity).
FT   COILED       68    110       Potential.
FT   MOD_RES       9      9       Phosphoserine (By similarity).
SQ   SEQUENCE   127 AA;  14535 MW;  7CE38A48D045CCC7 CRC64;
     MPLFGSIFSP KKTPPRKSAS LSNLHSLDRS TRELELGLDY GTPTMNLAGQ SLKFENGQWV
     ADSVISGGVD RRETQRLRKR NQQLEEENNL LRLKVDILLD MLSETTAESH LKDKELDELK
     VTNRRRK
//
ID   TBCB_MOUSE              Reviewed;         244 AA.
AC   Q9D1E6; Q9CWR6; Q9DCZ6;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Tubulin-folding cofactor B;
DE   AltName: Full=Cytoskeleton-associated protein 1;
DE   AltName: Full=Cytoskeleton-associated protein CKAPI;
DE   AltName: Full=Tubulin-specific chaperone B;
GN   Name=Tbcb; Synonyms=Ckap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH TBCE.
RX   PubMed=17184771; DOI=10.1016/j.yexcr.2006.09.002;
RA   Kortazar D., Fanarraga M.L., Carranza G., Bellido J., Villegas J.C.,
RA   Avila J., Zabala J.C.;
RT   "Role of cofactors B (TBCB) and E (TBCE) in tubulin heterodimer
RT   dissociation.";
RL   Exp. Cell Res. 313:425-436(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-98, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP   STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=17217416; DOI=10.1111/j.1471-4159.2006.04328.x;
RA   Lopez-Fanarraga M., Carranza G., Bellido J., Kortazar D.,
RA   Villegas J.C., Zabala J.C.;
RT   "Tubulin cofactor B plays a role in the neuronal growth cone.";
RL   J. Neurochem. 100:1680-1687(2007).
RN   [6]
RP   STRUCTURE BY NMR OF 11-92.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of a N-terminal ubiquitin-like domain in mouse
RT   tubulin-specific chaperone B.";
RL   Submitted (NOV-2003) to the PDB data bank.
RN   [7]
RP   STRUCTURE BY NMR OF 134-233.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the CAP-Gly domain in mouse tubulin-specific
RT   chaperone B.";
RL   Submitted (NOV-2003) to the PDB data bank.
CC   -!- FUNCTION: Binds to alpha-tubulin folding intermediates after their
CC       interaction with cytosolic chaperonin in the pathway leading from
CC       newly synthesized tubulin to properly folded heterodimer (By
CC       similarity). Involved in regulation of tubulin heterodimer
CC       dissociation. May function as a negative regulator of axonal
CC       growth.
CC   -!- SUBUNIT: Supercomplex made of cofactors A to E. Cofactors A and D
CC       function by capturing and stabilizing tubulin in a quasi-native
CC       conformation. Cofactor E binds to the cofactor D-tubulin complex;
CC       interaction with cofactor C then causes the release of tubulin
CC       polypeptides that are committed to the native state (By
CC       similarity). Cofactors B and E can form a heterodimer which binds
CC       to alpha-tubulin and enhances their ability to dissociate tubulin
CC       heterodimers. Binds to GAN.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
CC       Note=Colocalizes with microtubules. In differentiated neurons,
CC       located in the cytoplasm. In differentiating neurons, accumulates
CC       at the growth cone.
CC   -!- TISSUE SPECIFICITY: Widely expressed with highest levels in brain.
CC       Broadly distributed throughout the neonate brain but restricted
CC       mainly to ependymary cells in the adult brain where it is
CC       concentrated in the cilia.
CC   -!- DEVELOPMENTAL STAGE: In the embryo, expression increases at E12.5-
CC       E14.5. Levels are highest in pre- and postnatal stages which
CC       coincide with peaks of cerebral and cerebellar neurogenesis (at
CC       protein level).
CC   -!- PTM: Phosphorylation by PAK1 is required for normal function.
CC       Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- PTM: Ubiquitinated in the presence of GAN which targets it for
CC       degradation by the proteasome (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice display significantly longer axons than
CC       wild-type mice. Overexpression of Tbcb causes microtubule
CC       depolymerization, growth cone retraction and axonal damage
CC       followed by neuronal degeneration.
CC   -!- SIMILARITY: Belongs to the TBCB family.
CC   -!- SIMILARITY: Contains 1 CAP-Gly domain.
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DR   EMBL; AK002316; BAB22009.1; -; mRNA.
DR   EMBL; AK003655; BAB22918.2; -; mRNA.
DR   EMBL; AK010438; BAB26939.1; -; mRNA.
DR   EMBL; BC010684; AAH10684.1; -; mRNA.
DR   IPI; IPI00315948; -.
DR   RefSeq; NP_079824.2; NM_025548.3.
DR   UniGene; Mm.27947; -.
DR   PDB; 1V6E; NMR; -; A=11-92.
DR   PDB; 1WHG; NMR; -; A=134-233.
DR   PDBsum; 1V6E; -.
DR   PDBsum; 1WHG; -.
DR   ProteinModelPortal; Q9D1E6; -.
DR   SMR; Q9D1E6; 11-92, 134-233.
DR   STRING; Q9D1E6; -.
DR   PhosphoSite; Q9D1E6; -.
DR   PRIDE; Q9D1E6; -.
DR   Ensembl; ENSMUST00000006254; ENSMUSP00000006254; ENSMUSG00000006095.
DR   GeneID; 66411; -.
DR   KEGG; mmu:66411; -.
DR   UCSC; uc009gds.1; mouse.
DR   CTD; 66411; -.
DR   MGI; MGI:1913661; Tbcb.
DR   eggNOG; roNOG12611; -.
DR   GeneTree; ENSGT00550000074375; -.
DR   HOGENOM; HBG385175; -.
DR   HOVERGEN; HBG003239; -.
DR   InParanoid; Q9D1E6; -.
DR   OMA; WVGVRYD; -.
DR   OrthoDB; EOG44XJHQ; -.
DR   PhylomeDB; Q9D1E6; -.
DR   NextBio; 321613; -.
DR   ArrayExpress; Q9D1E6; -.
DR   Bgee; Q9D1E6; -.
DR   CleanEx; MM_TBCB; -.
DR   Genevestigator; Q9D1E6; -.
DR   GermOnline; ENSMUSG00000006095; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   InterPro; IPR023092; CAP-Gly_CS.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   Gene3D; G3DSA:2.30.30.190; CAP-Gly_domain; 1.
DR   Pfam; PF01302; CAP_GLY; 1.
DR   SUPFAM; SSF74924; CAP-Gly_domain; 1.
DR   PROSITE; PS00845; CAP_GLY_1; 1.
DR   PROSITE; PS50245; CAP_GLY_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Chaperone; Cytoplasm; Cytoskeleton;
KW   Developmental protein; Differentiation; Microtubule; Neurogenesis;
KW   Phosphoprotein; Ubl conjugation.
FT   CHAIN         1    244       Tubulin-folding cofactor B.
FT                                /FTId=PRO_0000083535.
FT   DOMAIN      183    225       CAP-Gly.
FT   MOD_RES      65     65       Phosphoserine; by PAK1 (By similarity).
FT   MOD_RES      98     98       Phosphotyrosine.
FT   MOD_RES     110    110       Phosphoserine (By similarity).
FT   MOD_RES     114    114       Phosphotyrosine (By similarity).
FT   MOD_RES     128    128       Phosphoserine; by PAK1 (By similarity).
FT   MOD_RES     219    219       N6-acetyllysine (By similarity).
FT   CONFLICT     84     84       R -> S (in Ref. 1; BAB26939).
FT   STRAND       11     17
FT   STRAND       20     22
FT   STRAND       24     28
FT   HELIX        34     44
FT   TURN         49     51
FT   STRAND       55     57
FT   STRAND       59     61
FT   STRAND       63     66
FT   STRAND       70     73
FT   STRAND       76     78
FT   STRAND       84     88
FT   HELIX       137    147
FT   HELIX       150    156
FT   STRAND      164    167
FT   STRAND      170    173
FT   STRAND      175    184
FT   STRAND      186    200
FT   STRAND      206    208
FT   TURN        218    220
FT   STRAND      221    224
FT   HELIX       226    228
SQ   SEQUENCE   244 AA;  27386 MW;  03BC7F0134F9289C CRC64;
     MEVTGISAPT VMVFISSSLN SFRSEKRYSR SLTIAEFKCK LELVVGSPAS CMELELYGAD
     DKFYSKLDQE DALLGSYPVD DGCRIHVIDH SGVRLGEYED VSKVEKYEIS PEAYERRQNT
     VRSFMKRSKL GPYNEELRAQ QEAEAAQRLS EEKAQASAIS VGSRCEVRAP DHSLRRGTVM
     YVGLTDFKPG YWVGVRYDEP LGKNDGSVNG KRYFECQAKY GAFVKPSAVT VGDFPEEDYG
     LDEM
//
ID   AKTS1_MOUSE             Reviewed;         257 AA.
AC   Q9D1F4; A2RT52;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Proline-rich AKT1 substrate 1;
DE            Short=Proline-rich AKT substrate;
GN   Name=Akt1s1; Synonyms=Pras;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=14973226; DOI=10.1523/JNEUROSCI.5209-03.2004;
RA   Saito A., Narasimhan P., Hayashi T., Okuno S., Ferrand-Drake M.,
RA   Chan P.H.;
RT   "Neuroprotective role of a proline-rich Akt substrate in apoptotic
RT   neuronal cell death after stroke: relationships with nerve growth
RT   factor.";
RL   J. Neurosci. 24:1584-1593(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-204 AND
RP   SER-213, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   FUNCTION.
RX   PubMed=16397181; DOI=10.1161/01.STR.0000198826.56611.a2;
RA   Saito A., Hayashi T., Okuno S., Nishi T., Chan P.H.;
RT   "Modulation of proline-rich akt substrate survival signaling pathways
RT   by oxidative stress in mouse brains after transient focal cerebral
RT   ischemia.";
RL   Stroke 37:513-517(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117; SER-203; SER-204;
RP   SER-212 AND SER-213, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88; SER-92; SER-203 AND
RP   SER-204, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Subunit of mTORC1, which regulates cell growth and
CC       survival in response to nutrient and hormonal signals. mTORC1 is
CC       activated in response to growth factors or amino-acids. Growth
CC       factor-stimulated mTORC1 activation involves a AKT1-mediated
CC       phosphorylation of TSC1-TSC2, which leads to the activation of the
CC       RHEB GTPase that potently activates the protein kinase activity of
CC       mTORC1. Amino-acid-signaling to mTORC1 requires its relocalization
CC       to the lysosomes mediated by the Ragulator complex and the Rag
CC       GTPases. Activated mTORC1 up-regulates protein synthesis by
CC       phosphorylating key regulators of mRNA translation and ribosome
CC       synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from
CC       inhibiting the elongation initiation factor 4E (eiF4E). mTORC1
CC       phosphorylates and activates S6K1 at 'Thr-389', which then
CC       promotes protein synthesis by phosphorylating PDCD4 and targeting
CC       it for degradation. Within mTORC1, AKT1S1 negatively regulates
CC       mTOR activity in a manner that is dependent on its phosphorylation
CC       state and binding to 14-3-3. Inhibits RHEB-GTP-dependent mTORC1
CC       activation. Substrate for AKT1 phosphorylation, but can also be
CC       activated by AKT1-independent mechanisms. May also play a role in
CC       nerve growth factor-mediated neuroprotection.
CC   -!- SUBUNIT: Part of the mammalian target of rapamycin complex 1
CC       (mTORC1) which contains MTOR, LST8, RPTOR and AKT1S1. mTORC1 binds
CC       to and is inhibited by FKBP12-rapamycin. Interacts directly with
CC       RPTOR. The phosphorylated form interacts with 14-3-3 proteins and
CC       with phosphorylated AKT1 following transient focal cerebral
CC       ischemia in vivo.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Note=Found in the
CC       cytosolic fraction of the brain. Colocalizes with cortical neurons
CC       following ischemic/reperfusion injury.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK003638; BAB22905.1; -; mRNA.
DR   EMBL; AK141771; BAE24829.1; -; mRNA.
DR   EMBL; AK154110; BAE32383.1; -; mRNA.
DR   EMBL; BC132372; AAI32373.1; -; mRNA.
DR   EMBL; BC132374; AAI32375.1; -; mRNA.
DR   IPI; IPI00133685; -.
DR   RefSeq; NP_080546.1; NM_026270.3.
DR   UniGene; Mm.148007; -.
DR   UniGene; Mm.431538; -.
DR   ProteinModelPortal; Q9D1F4; -.
DR   STRING; Q9D1F4; -.
DR   PhosphoSite; Q9D1F4; -.
DR   PRIDE; Q9D1F4; -.
DR   Ensembl; ENSMUST00000054343; ENSMUSP00000049764; ENSMUSG00000011096.
DR   Ensembl; ENSMUST00000107880; ENSMUSP00000103512; ENSMUSG00000011096.
DR   Ensembl; ENSMUST00000107882; ENSMUSP00000103514; ENSMUSG00000011096.
DR   Ensembl; ENSMUST00000107885; ENSMUSP00000103517; ENSMUSG00000011096.
DR   GeneID; 67605; -.
DR   KEGG; mmu:67605; -.
DR   UCSC; uc009grd.1; mouse.
DR   CTD; 67605; -.
DR   MGI; MGI:1914855; Akt1s1.
DR   GeneTree; ENSGT00390000017397; -.
DR   HOGENOM; HBG715339; -.
DR   HOVERGEN; HBG059465; -.
DR   InParanoid; Q9D1F4; -.
DR   OrthoDB; EOG4V6ZHQ; -.
DR   NextBio; 325025; -.
DR   ArrayExpress; Q9D1F4; -.
DR   Bgee; Q9D1F4; -.
DR   CleanEx; MM_AKT1S1; -.
DR   Genevestigator; Q9D1F4; -.
DR   GermOnline; ENSMUSG00000011096; Mus musculus.
DR   GO; GO:0044445; C:cytosolic part; IDA:UniProtKB.
DR   GO; GO:0043526; P:neuroprotection; IDA:UniProtKB.
DR   GO; GO:0045884; P:regulation of survival gene product expression; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein.
FT   CHAIN         1    257       Proline-rich AKT1 substrate 1.
FT                                /FTId=PRO_0000253447.
FT   COMPBIAS     35     43       Poly-Pro.
FT   COMPBIAS     77     97       Pro-rich.
FT   MOD_RES      88     88       Phosphoserine.
FT   MOD_RES      92     92       Phosphoserine.
FT   MOD_RES     117    117       Phosphoserine.
FT   MOD_RES     184    184       Phosphoserine (By similarity).
FT   MOD_RES     199    199       Phosphothreonine (By similarity).
FT   MOD_RES     203    203       Phosphoserine.
FT   MOD_RES     204    204       Phosphoserine.
FT   MOD_RES     212    212       Phosphoserine.
FT   MOD_RES     213    213       Phosphoserine.
FT   MOD_RES     247    247       Phosphothreonine; by PKB/AKT1 (By
FT                                similarity).
SQ   SEQUENCE   257 AA;  27483 MW;  4BFFC8630DBBA5EC CRC64;
     MASGRPEELW EAVVGAAERF QARTGTELVL LTAAPPPPPR PGPCAYAAHG RGALAEAARR
     CLHDIAQAHR AATATRPPGP PPAPQPPSPA PSPPPRPALA REDEEEDEDE PTETETSGER
     LGGSDNGGLF MMDEDATLQD LPPFCESDPE STDDGSLSEE TPAGPTACPQ PPATALPTQQ
     YAKSLPVSVP VWAFKEKRTE ARSSDEENGP PSSPDLDRIA ASMRALVLRE AEDTQVFGDL
     PRPRLNTSDF QKLKRKY
//
ID   RAB1B_MOUSE             Reviewed;         201 AA.
AC   Q9D1G1; Q3U0N1;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Ras-related protein Rab-1B;
GN   Name=Rab1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 11-21; 59-69; 72-100; 109-122; 138-153 AND
RP   173-187, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Protein transport. Regulates vesicular transport between
CC       the endoplasmic reticulum and successive Golgi compartments (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with MICAL1, MICAL2 and MICAL3. Interacts with
CC       GDI1; the interaction requires the GDP-bound state. Interacts with
CC       CHM/REP1; the interaction requires the GDP-bound form and is
CC       necessary for prenylation by GGTase II (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor; Cytoplasmic side.
CC       Cytoplasm. Note=Targeted by REP1 to membranes of specific
CC       subcellular compartments including endoplasmic reticulum, Golgi
CC       apparatus, and intermediate vesicles between these two
CC       compartments. In the GDP-form, colocalizes with GDI in the
CC       cytoplasm (By similarity).
CC   -!- PTM: Prenylated; by GGTase II, only after interaction of the
CC       substrate with Rab escort protein 1 (REP1) (By similarity).
CC   -!- MISCELLANEOUS: Rab-1B binds GTP and GDP and possesses intrinsic
CC       GTPase activity (By similarity).
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK003609; BAB22888.1; -; mRNA.
DR   EMBL; AK156726; BAE33821.1; -; mRNA.
DR   EMBL; BC016408; AAH16408.1; -; mRNA.
DR   IPI; IPI00133706; -.
DR   RefSeq; NP_083852.1; NM_029576.3.
DR   UniGene; Mm.182563; -.
DR   ProteinModelPortal; Q9D1G1; -.
DR   SMR; Q9D1G1; 4-173.
DR   STRING; Q9D1G1; -.
DR   PhosphoSite; Q9D1G1; -.
DR   PRIDE; Q9D1G1; -.
DR   Ensembl; ENSMUST00000025804; ENSMUSP00000025804; ENSMUSG00000024870.
DR   GeneID; 76308; -.
DR   KEGG; mmu:76308; -.
DR   UCSC; uc008gcf.1; mouse.
DR   CTD; 76308; -.
DR   MGI; MGI:1923558; Rab1b.
DR   GeneTree; ENSGT00550000074219; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG009351; -.
DR   InParanoid; Q9D1G1; -.
DR   OMA; TMANEIK; -.
DR   OrthoDB; EOG48D0WM; -.
DR   PhylomeDB; Q9D1G1; -.
DR   NextBio; 344943; -.
DR   ArrayExpress; Q9D1G1; -.
DR   Bgee; Q9D1G1; -.
DR   CleanEx; MM_RAB1B; -.
DR   Genevestigator; Q9D1G1; -.
DR   GermOnline; ENSMUSG00000024870; Mus musculus.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR003579; GTPase_Rab.
DR   InterPro; IPR013753; Ras.
DR   InterPro; IPR001806; Ras_GTPase.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   InterPro; IPR020851; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00175; RAB; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; GTP-binding;
KW   Lipoprotein; Membrane; Methylation; Nucleotide-binding; Prenylation;
KW   Protein transport; Transport.
FT   CHAIN         1    201       Ras-related protein Rab-1B.
FT                                /FTId=PRO_0000121062.
FT   NP_BIND      15     22       GTP (By similarity).
FT   NP_BIND      63     67       GTP (By similarity).
FT   NP_BIND     121    124       GTP (By similarity).
FT   REGION       64     83       Switch 2 region; required for interaction
FT                                with REP1/CHM (By similarity).
FT   MOTIF        37     45       Effector region (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     201    201       Cysteine methyl ester (Potential).
FT   LIPID       200    200       S-geranylgeranyl cysteine (By
FT                                similarity).
FT   LIPID       201    201       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   201 AA;  22187 MW;  870DFF52AEF4B2BE CRC64;
     MNPEYDYLFK LLLIGDSGVG KSCLLLRFAD DTYTESYIST IGVDFKIRTI ELDGKTIKLQ
     IWDTAGQERF RTITSSYYRG AHGIIVVYDV TDQESYANVK QWLQEIDRYA SENVNKLLVG
     NKSDLTTKKV VDNTTAKEFA DSLGVPFLET SAKNATNVEQ AFMTMAAEIK KRMGPGAASG
     GERPNLKIDS TPVKPASGGC C
//
ID   CHRD1_MOUSE             Reviewed;         331 AA.
AC   Q9D1P4; Q9CSI5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Cysteine and histidine-rich domain-containing protein 1;
DE   AltName: Full=CHORD domain-containing protein 1;
DE            Short=CHORD-containing protein 1;
DE            Short=Chp-1;
DE   AltName: Full=Protein morgana;
GN   Name=Chordc1; Synonyms=Chp1, Morgana;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=12965203; DOI=10.1016/S0014-5793(03)00892-5;
RA   Brancaccio M., Menini N., Bongioanni D., Ferretti R., De Acetis M.,
RA   Silengo L., Tarone G.;
RT   "Chp-1 and melusin, two CHORD containing proteins in vertebrates.";
RL   FEBS Lett. 551:47-52(2003).
RN   [4]
RP   INTERACTION WITH HSP90AB1.
RX   PubMed=15642353; DOI=10.1016/j.febslet.2004.12.005;
RA   Wu J., Luo S., Jiang H., Li H.;
RT   "Mammalian CHORD-containing protein 1 is a novel heat shock protein
RT   90-interacting protein.";
RL   FEBS Lett. 579:421-426(2005).
RN   [5]
RP   INTERACTION WITH HSP90AA1 AND PPP5C, FUNCTION, AND INDUCTION.
RX   PubMed=16083881; DOI=10.1016/j.febslet.2005.07.024;
RA   Hahn J.-S.;
RT   "Regulation of Nod1 by Hsp90 chaperone complex.";
RL   FEBS Lett. 579:4513-4519(2005).
RN   [6]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=17253150; DOI=10.1007/s11064-006-9271-z;
RA   Gerstner J.R., Landry C.F.;
RT   "The zinc-binding protein chordc1 undergoes complex diurnal changes in
RT   mRNA expression during mouse brain development.";
RL   Neurochem. Res. 32:241-250(2007).
RN   [7]
RP   FUNCTION.
RX   PubMed=20493909; DOI=10.1016/j.bbamcr.2010.05.005;
RA   Michowski W., Ferretti R., Wisniewska M.B., Ambrozkiewicz M.,
RA   Beresewicz M., Fusella F., Skibinska-Kijek A., Zablocka B.,
RA   Brancaccio M., Tarone G., Kuznicki J.;
RT   "Morgana/CHP-1 is a novel chaperone able to protect cells from
RT   stress.";
RL   Biochim. Biophys. Acta 1803:1043-1049(2010).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20230755; DOI=10.1016/j.devcel.2009.12.020;
RA   Ferretti R., Palumbo V., Di Savino A., Velasco S., Sbroggio M.,
RA   Sportoletti P., Micale L., Turco E., Silengo L., Palumbo G.,
RA   Hirsch E., Teruya-Feldstein J., Bonaccorsi S., Pandolfi P.P.,
RA   Gatti M., Tarone G., Brancaccio M.;
RT   "Morgana/chp-1, a ROCK inhibitor involved in centrosome duplication
RT   and tumorigenesis.";
RL   Dev. Cell 18:486-495(2010).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47 AND THR-204, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Regulates centrosome duplication, probably by inhibiting
CC       the kinase activity of ROCK2. Proposed to act as co-chaperone for
CC       HSP90. May play a role in the regulation of NOD1 via a HSP90
CC       chaperone complex. In vitro, has intrinsic chaperone activity.
CC       This function may be achieved by inhibiting association of ROCK2
CC       with NPM1. Involved in stress response. Prevents tumorigenesis (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with HSP90AA1, HSP90AB1 and PPP5C. Interacts
CC       with ROCK1 and ROCK2 (By similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in
CC       spleen, lung and brain (at protein level). Expressed in
CC       proliferating myoblasts and its expression remained steady after.
CC       Its expression undergoes diurnal and circadian changes in
CC       hypothalamus. Highly expressed during the dark-light transition
CC       (ZT20.5 (zeitgeber time 20.5) and ZT2.5).
CC   -!- DEVELOPMENTAL STAGE: Weakly expressed at ZT8.5 and highly
CC       expressed at ZT14.5 at P6. At P6 highly expressed at ZT14.5 in
CC       hippocampus, prefrontal cortex and cerebellum. First detected and
CC       widely distributed at P1 and that continued throughout postnatal
CC       development. Expression is evident in the cortical plate (CP) at
CC       E17. Lower levels of expression is also evident in intermediate
CC       (IZ) and subventricular (SVZ) zones at this age. A more diffuse
CC       expression pattern is evident in early postnatal cortex with only
CC       slight differences in intensity throughout cortical layers. By
CC       P14, a more laminated distribution pattern becomes evident with a
CC       punctate distribution apparent in deep cortical layers.
CC   -!- INDUCTION: By Heat shock in a HSF1-dependent manner.
CC   -!- DISRUPTION PHENOTYPE: Results in centrosome amplification and
CC       lethality. Cells become polyploid or undergo apoptosis. Embryos
CC       are no longer detected after 3.5 dpc.
CC   -!- SIMILARITY: Contains 2 CHORD domains.
CC   -!- SIMILARITY: Contains 1 CS domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK003259; BAB22675.1; -; mRNA.
DR   EMBL; AK012747; BAB28444.1; -; mRNA.
DR   EMBL; AK132696; BAE21307.1; -; mRNA.
DR   EMBL; BC018374; AAH18374.1; -; mRNA.
DR   IPI; IPI00134017; -.
DR   RefSeq; NP_080120.1; NM_025844.2.
DR   UniGene; Mm.479183; -.
DR   ProteinModelPortal; Q9D1P4; -.
DR   SMR; Q9D1P4; 1-68, 148-220, 229-319.
DR   MINT; MINT-1215377; -.
DR   STRING; Q9D1P4; -.
DR   PhosphoSite; Q9D1P4; -.
DR   PRIDE; Q9D1P4; -.
DR   Ensembl; ENSMUST00000001825; ENSMUSP00000001825; ENSMUSG00000001774.
DR   GeneID; 66917; -.
DR   KEGG; mmu:66917; -.
DR   UCSC; uc009ogm.1; mouse.
DR   CTD; 66917; -.
DR   MGI; MGI:1914167; Chordc1.
DR   eggNOG; roNOG13315; -.
DR   GeneTree; ENSGT00390000005180; -.
DR   HOGENOM; HBG717278; -.
DR   HOVERGEN; HBG052156; -.
DR   InParanoid; Q9D1P4; -.
DR   OMA; GNEENKK; -.
DR   OrthoDB; EOG43N7D5; -.
DR   PhylomeDB; Q9D1P4; -.
DR   NextBio; 323017; -.
DR   ArrayExpress; Q9D1P4; -.
DR   Bgee; Q9D1P4; -.
DR   Genevestigator; Q9D1P4; -.
DR   GO; GO:0008270; F:zinc ion binding; IDA:MGI.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IDA:UniProtKB.
DR   GO; GO:2000299; P:negative regulation of Rho-dependent protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0010824; P:regulation of centrosome duplication; IMP:UniProtKB.
DR   GO; GO:0080134; P:regulation of response to stress; IDA:UniProtKB.
DR   GO; GO:0006950; P:response to stress; IEA:UniProtKB-KW.
DR   InterPro; IPR007051; CHORD.
DR   InterPro; IPR007052; CS-like_domain.
DR   InterPro; IPR017447; CS_domain.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   Pfam; PF04968; CHORD; 2.
DR   Pfam; PF04969; CS; 1.
DR   SUPFAM; SSF49764; HSP20_chap; 1.
DR   PROSITE; PS51401; CHORD; 2.
DR   PROSITE; PS51203; CS; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chaperone; Metal-binding; Phosphoprotein; Repeat;
KW   Stress response; Zinc.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    331       Cysteine and histidine-rich domain-
FT                                containing protein 1.
FT                                /FTId=PRO_0000317771.
FT   DOMAIN        5     64       CHORD 1.
FT   DOMAIN      157    216       CHORD 2.
FT   DOMAIN      227    316       CS.
FT   REGION        2     77       Interaction with PPP5C.
FT   REGION       65    316       Interaction with HSP90AA1 and HSP90AB1.
FT   METAL         5      5       Zinc 1 (By similarity).
FT   METAL        10     10       Zinc 1 (By similarity).
FT   METAL        24     24       Zinc 1 (By similarity).
FT   METAL        27     27       Zinc 2 (By similarity).
FT   METAL        42     42       Zinc 2 (By similarity).
FT   METAL        43     43       Zinc 2 (By similarity).
FT   METAL        59     59       Zinc 2 (By similarity).
FT   METAL        64     64       Zinc 1 (By similarity).
FT   METAL       157    157       Zinc 3 (By similarity).
FT   METAL       162    162       Zinc 3 (By similarity).
FT   METAL       176    176       Zinc 3 (By similarity).
FT   METAL       179    179       Zinc 4 (By similarity).
FT   METAL       194    194       Zinc 4 (By similarity).
FT   METAL       195    195       Zinc 4 (By similarity).
FT   METAL       211    211       Zinc 4 (By similarity).
FT   METAL       216    216       Zinc 3 (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      47     47       Phosphothreonine.
FT   MOD_RES      51     51       Phosphoserine (By similarity).
FT   MOD_RES     200    200       Phosphoserine (By similarity).
FT   MOD_RES     204    204       Phosphothreonine.
SQ   SEQUENCE   331 AA;  37351 MW;  8E02FD5F4EB89BB9 CRC64;
     MALLCYNRGC GQRFDPEANS DDACTYHPGV PVFHDALKGW SCCKRRTTDF SDFLSIVGCT
     KGRHNSEKPP EPVKPEVKTT EKKELSELKP KFQEHIIQAP KPVEAIKRPS PDEPMTNLEL
     KISASLKQAL DKLKLSSGSE EDKKEEDSDE IKIGTSCKNG GCSKTYQGLQ SLEEVCVYHS
     GVPIFHEGMK YWSCCRRKTS DFNTFLAQEG CTRGKHVWTK KDAGKKVVPC RHDWHQTGGE
     VTISVYAKNS LPELSQVEAN STLLNVHIVF EGEKEFHQNV KLWGVIDVKR SYVTMTATKI
     EITMRKAEPM QWASLELPTT KKQEKQKDIA D
//
ID   LIGO1_MOUSE             Reviewed;         614 AA.
AC   Q9D1T0; Q3TQJ4; Q6VVF9; Q7TT38;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Leucine-rich repeat and immunoglobulin-like domain-containing nogo receptor-interacting protein 1;
DE   AltName: Full=Leucine-rich repeat neuronal protein 1;
DE   AltName: Full=Leucine-rich repeat neuronal protein 6A;
DE   Flags: Precursor;
GN   Name=Lingo1; Synonyms=Lern1, Lrrn6a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 411-614, DEVELOPMENTAL STAGE, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=14686891; DOI=10.1111/j.1460-9568.2003.03003.x;
RA   Carim-Todd L., Escarceller M., Estivill X., Sumoy L.;
RT   "LRRN6A/LERN1 (leucine-rich repeat neuronal protein 1), a novel gene
RT   with enriched expression in limbic system and neocortex.";
RL   Eur. J. Neurosci. 18:3167-3182(2003).
RN   [4]
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH NGRF; RTN4R AND MYT1L.
RX   PubMed=18186492; DOI=10.1002/dneu.20607;
RA   Llorens F., Gil V., Iraola S., Carim-Todd L., Marti E., Estivill X.,
RA   Soriano E., Del Rio J.A., Sumoy L.;
RT   "Developmental analysis of Lingo-1/Lern1 protein expression in the
RT   mouse brain: Interaction of its intracellular domain with Myt1l.";
RL   Dev. Neurobiol. 68:521-541(2008).
RN   [5]
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17726113; DOI=10.1073/pnas.0700901104;
RA   Inoue H., Lin L., Lee X., Shao Z., Mendes S., Snodgrass-Belt P.,
RA   Sweigard H., Engber T., Pepinsky B., Yang L., Beal M.F., Mi S.,
RA   Isacson O.;
RT   "Inhibition of the leucine-rich repeat protein LINGO-1 enhances
RT   survival, structure, and function of dopaminergic neurons in
RT   Parkinson's disease models.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:14430-14435(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-596, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   FUNCTION.
RX   PubMed=20093372; DOI=10.1093/cercor/bhp307;
RA   Mathis C., Schroeter A., Thallmair M., Schwab M.E.;
RT   "Nogo-a regulates neural precursor migration in the embryonic mouse
RT   cortex.";
RL   Cereb. Cortex 20:2380-2390(2010).
CC   -!- FUNCTION: Functional component of the Nogo receptor signaling
CC       complex (RTN4R/NGFR) in RhoA activation responsible for some
CC       inhibition of axonal regeneration by myelin-associated factors. Is
CC       also an important negative regulator of oligodentrocyte
CC       differentiation and axonal myelination (By similarity). Acts in
CC       conjunction with RTN4 and RTN4R in regulating neuronal precursor
CC       cell motility during cortical development.
CC   -!- SUBUNIT: Homotetramer. Forms ternary complex with RTN4R/NGFR and
CC       RTN4R/TNFRSF19 (By similarity).
CC   -!- INTERACTION:
CC       P12023:App; NbExp=1; IntAct=EBI-2012981, EBI-78814;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Highly specific expression in the central
CC       nervous system. Predominant expression in neocortex, amygdala,
CC       hippocampus, thalamus and entorhinal cortex, with lower levels in
CC       cerebellum and basal nuclei.
CC   -!- DEVELOPMENTAL STAGE: Expressed broadly at high levels in the whole
CC       embryo and becomes progressively restricted to the central nervous
CC       system by E14.5. Extensively expressed across the central nervous
CC       system through late embryogenesis and during postnatal
CC       development, with a peak of expression around the first week after
CC       birth.
CC   -!- INDUCTION: Up-regulated in brain from MPTP-intoxicated mice, a
CC       model for Parkinson disease.
CC   -!- DOMAIN: The intracellular domain of LINGO1 interact with MYT1L.
CC   -!- PTM: N-glycosylated. Contains predominantly high-mannose glycans
CC       (By similarity).
CC   -!- DISRUPTION PHENOTYPE: In mice lacking Lingo1 and MPTP-intoxicated,
CC       a model for Parkinson disease, the dopaminergic neurons survival
CC       is increased and behavioral abnormalities reduced.
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 13 LRR (leucine-rich) repeats.
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DR   EMBL; AK027262; BAB32403.1; -; mRNA.
DR   EMBL; AK163538; BAE37388.1; -; mRNA.
DR   EMBL; BC052384; AAH52384.2; -; mRNA.
DR   EMBL; BC065696; AAH65696.1; -; mRNA.
DR   EMBL; AY324324; AAQ97219.1; -; mRNA.
DR   IPI; IPI00134200; -.
DR   RefSeq; NP_851419.1; NM_181074.4.
DR   UniGene; Mm.246605; -.
DR   HSSP; P21809; 2FT3.
DR   ProteinModelPortal; Q9D1T0; -.
DR   SMR; Q9D1T0; 36-508.
DR   IntAct; Q9D1T0; 2.
DR   STRING; Q9D1T0; -.
DR   PhosphoSite; Q9D1T0; -.
DR   PRIDE; Q9D1T0; -.
DR   Ensembl; ENSMUST00000053568; ENSMUSP00000059050; ENSMUSG00000049556.
DR   Ensembl; ENSMUST00000114247; ENSMUSP00000109885; ENSMUSG00000049556.
DR   Ensembl; ENSMUST00000114256; ENSMUSP00000109894; ENSMUSG00000049556.
DR   GeneID; 235402; -.
DR   KEGG; mmu:235402; -.
DR   UCSC; uc009pth.1; mouse.
DR   CTD; 235402; -.
DR   MGI; MGI:1915522; Lingo1.
DR   eggNOG; maNOG11092; -.
DR   GeneTree; ENSGT00600000084155; -.
DR   HOVERGEN; HBG057546; -.
DR   InParanoid; Q9D1T0; -.
DR   OrthoDB; EOG40S0F8; -.
DR   PhylomeDB; Q9D1T0; -.
DR   NextBio; 382644; -.
DR   ArrayExpress; Q9D1T0; -.
DR   Bgee; Q9D1T0; -.
DR   Genevestigator; Q9D1T0; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005154; F:epidermal growth factor receptor binding; IPI:MGI.
DR   GO; GO:0021954; P:central nervous system neuron development; IDA:MGI.
DR   GO; GO:0048715; P:negative regulation of oligodendrocyte differentiation; IMP:MGI.
DR   GO; GO:0031175; P:neuron projection development; IDA:MGI.
DR   GO; GO:0043491; P:protein kinase B signaling cascade; IDA:MGI.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR000372; LRR-contain_N.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00560; LRR_1; 3.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00369; LRR_TYP; 1.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00013; LRRNT; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS51450; LRR; 10.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW   Leucine-rich repeat; Membrane; Phosphoprotein; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     35       Potential.
FT   CHAIN        36    614       Leucine-rich repeat and immunoglobulin-
FT                                like domain-containing nogo receptor-
FT                                interacting protein 1.
FT                                /FTId=PRO_0000328643.
FT   TOPO_DOM     36    555       Extracellular (Potential).
FT   TRANSMEM    556    576       Helical; (Potential).
FT   TOPO_DOM    577    614       Cytoplasmic (Potential).
FT   REPEAT       64     87       LRR 1.
FT   REPEAT       88    111       LRR 2.
FT   REPEAT      112    135       LRR 3.
FT   REPEAT      137    159       LRR 4.
FT   REPEAT      160    183       LRR 5.
FT   REPEAT      184    207       LRR 6.
FT   REPEAT      209    231       LRR 7.
FT   REPEAT      256    279       LRR 8.
FT   REPEAT      280    303       LRR 9.
FT   REPEAT      305    327       LRR 10.
FT   REPEAT      328    351       LRR 11.
FT   REPEAT      353    377       LRR 12.
FT   DOMAIN      405    507       Ig-like C2-type.
FT   REPEAT      453    478       LRR 13.
FT   MOD_RES     596    596       Phosphoserine.
FT   CARBOHYD    138    138       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    196    196       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    258    258       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    268    268       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    287    287       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    335    335       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    486    486       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    536    536       N-linked (GlcNAc...) (Potential).
FT   DISULFID     36     42       By similarity.
FT   DISULFID     40     51       By similarity.
FT   DISULFID    367    390       By similarity.
FT   DISULFID    369    415       By similarity.
FT   DISULFID    440    491       By similarity.
FT   CONFLICT    491    491       C -> G (in Ref. 3; AAQ97219).
SQ   SEQUENCE   614 AA;  69101 MW;  41CFF40C21335681 CRC64;
     MLAGGMRSMP SPLLACWQPI LLLVLGSVLS GSATGCPPRC ECSAQDRAVL CHRKRFVAVP
     EGIPTETRLL DLGKNRIKTL NQDEFASFPH LEELELNENI VSAVEPGAFN NLFNLRTLGL
     RSNRLKLIPL GVFTGLSNLT KLDISENKIV ILLDYMFQDL YNLKSLEVGD NDLVYISHRA
     FSGLNSLEQL TLEKCNLTSI PTEALSHLHG LIVLRLRHLN INAIRDYSFK RLYRLKVLEI
     SHWPYLDTMT PNCLYGLNLT SLSITHCNLT AVPYLAVRHL VYLRFLNLSY NPIGTIEGSM
     LHELLRLQEI QLVGGQLAVV EPYAFRGLNY LRVLNVSGNQ LTTLEESAFH SVGNLETLIL
     DSNPLACDCR LLWVFRRRWR LNFNRQQPTC ATPEFVQGKE FKDFPDVLLP NYFTCRRAHI
     RDRKAQQVFV DEGHTVQFVC RADGDPPPAI LWLSPRKHLV SAKSNGRLTV FPDGTLEVRY
     AQVQDNGTYL CIAANAGGND SMPAHLHVRS YSPDWPHQPN KTFAFISNQP GEGEANSTRA
     TVPFPFDIKT LIIATTMGFI SFLGVVLFCL VLLFLWSRGK GNTKHNIEIE YVPRKSDAGI
     SSADAPRKFN MKMI
//
ID   TPC6B_MOUSE             Reviewed;         158 AA.
AC   Q9D289;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Trafficking protein particle complex subunit 6B;
GN   Name=Trappc6b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in vesicular transport from endoplasmic
CC       reticulum to Golgi (By similarity).
CC   -!- SUBUNIT: Part of the multisubunit TRAPP (transport protein
CC       particle) complex. Homodimer. Heterodimer with TRAPPC3 (By
CC       similarity). Endoplasmic reticulum (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network (By
CC       similarity). Endoplasmic reticulum (By similarity).
CC   -!- SIMILARITY: Belongs to the TRAPP small subunits family. BET3
CC       subfamily.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK020026; BAB31972.1; -; mRNA.
DR   EMBL; AK089083; BAC40741.1; -; mRNA.
DR   EMBL; BC031464; AAH31464.1; -; mRNA.
DR   IPI; IPI00134426; -.
DR   RefSeq; NP_084333.1; NM_030057.2.
DR   UniGene; Mm.290070; -.
DR   ProteinModelPortal; Q9D289; -.
DR   SMR; Q9D289; 2-157.
DR   PhosphoSite; Q9D289; -.
DR   PRIDE; Q9D289; -.
DR   Ensembl; ENSMUST00000021380; ENSMUSP00000021380; ENSMUSG00000020993.
DR   GeneID; 78232; -.
DR   KEGG; mmu:78232; -.
DR   UCSC; uc007npy.1; mouse.
DR   CTD; 78232; -.
DR   MGI; MGI:1925482; Trappc6b.
DR   eggNOG; roNOG13090; -.
DR   GeneTree; ENSGT00390000012948; -.
DR   HOGENOM; HBG619271; -.
DR   HOVERGEN; HBG056159; -.
DR   InParanoid; Q9D289; -.
DR   OMA; YLEHAPK; -.
DR   OrthoDB; EOG4NVZMM; -.
DR   PhylomeDB; Q9D289; -.
DR   NextBio; 348473; -.
DR   ArrayExpress; Q9D289; -.
DR   Bgee; Q9D289; -.
DR   CleanEx; MM_TRAPPC6B; -.
DR   Genevestigator; Q9D289; -.
DR   GermOnline; ENSMUSG00000020993; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004383; F:guanylate cyclase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   InterPro; IPR011644; Haem_NO-bd.
DR   InterPro; IPR007194; TRAPP_component.
DR   Pfam; PF04051; TRAPP; 1.
DR   SUPFAM; SSF111126; Haem_NO-bd; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Endoplasmic reticulum; ER-Golgi transport;
KW   Golgi apparatus; Transport.
FT   CHAIN         1    158       Trafficking protein particle complex
FT                                subunit 6B.
FT                                /FTId=PRO_0000211588.
FT   MOD_RES      98     98       N6-acetyllysine (By similarity).
SQ   SEQUENCE   158 AA;  17936 MW;  DA7A047BC4807B9B CRC64;
     MADEALFLLL HNEMVSGVYK SAEQGEVENG RCVTKLESMG FRVGQGLIER FTKDTARFKD
     ELDIMKFICK DFWTTVFKKQ IDNLRTNHQG IYVLQDNKFR LLIQLSAGKQ YLEHASKYLA
     FTCGLIRGGL SNLGIKSIVT AEVSSMPACK FQVMIQKL
//
ID   SAAL1_MOUSE             Reviewed;         474 AA.
AC   Q9D2C2; Q3UYS6; Q8R2L2;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Protein SAAL1;
GN   Name=Saal1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Ovary, Testis, Thymus, and Uterus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 190-474 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-14, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-378 AND THR-387, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9D2C2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D2C2-2; Sequence=VSP_023483;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Belongs to the SAAL1 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK019878; BAB31898.1; -; mRNA.
DR   EMBL; AK030833; BAC27152.1; -; mRNA.
DR   EMBL; AK033202; BAC28195.1; -; mRNA.
DR   EMBL; AK132193; BAE21024.1; -; mRNA.
DR   EMBL; AK134418; BAE22136.1; -; mRNA.
DR   EMBL; BC028473; AAH28473.1; -; mRNA.
DR   EMBL; BC087944; AAH87944.1; -; mRNA.
DR   IPI; IPI00134680; -.
DR   IPI; IPI00462627; -.
DR   RefSeq; NP_084509.1; NM_030233.1.
DR   UniGene; Mm.289866; -.
DR   PhosphoSite; Q9D2C2; -.
DR   PRIDE; Q9D2C2; -.
DR   Ensembl; ENSMUST00000143082; ENSMUSP00000120658; ENSMUSG00000006763.
DR   GeneID; 78935; -.
DR   KEGG; mmu:78935; -.
DR   UCSC; uc009gyu.1; mouse.
DR   CTD; 78935; -.
DR   MGI; MGI:1926185; Saal1.
DR   eggNOG; roNOG09815; -.
DR   GeneTree; ENSGT00510000048056; -.
DR   HOGENOM; HBG713555; -.
DR   HOVERGEN; HBG061166; -.
DR   InParanoid; Q9D2C2; -.
DR   OMA; SAIYASQ; -.
DR   OrthoDB; EOG4NKBVF; -.
DR   PhylomeDB; Q9D2C2; -.
DR   NextBio; 349808; -.
DR   ArrayExpress; Q9D2C2; -.
DR   Bgee; Q9D2C2; -.
DR   CleanEx; MM_SAAL1; -.
DR   Genevestigator; Q9D2C2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0006953; P:acute-phase response; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000096; Serum_amyloid_A.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   PANTHER; PTHR23424; Serum_amyloid_A; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    474       Protein SAAL1.
FT                                /FTId=PRO_0000279541.
FT   MOD_RES       6      6       Phosphoserine.
FT   MOD_RES      14     14       Phosphoserine.
FT   MOD_RES     378    378       Phosphothreonine.
FT   MOD_RES     387    387       Phosphothreonine.
FT   VAR_SEQ     414    474       EKVAQGLKEGQLSKQKCSCAFQSLLPLYGPAVEDFVKVVRE
FT                                VDEALADDLEDSFPSVKAQT -> VGGSISDFFSKIKGADY
FT                                LMS (in isoform 2).
FT                                /FTId=VSP_023483.
SQ   SEQUENCE   474 AA;  52769 MW;  08D96FEF6B18B443 CRC64;
     MDRNPSPPPP TCGSEDEEDL GGGDRIGSTV YSKHWLFGVL SGLIQIVTPE SGTSGSADEE
     EQADLAEEME NEICRVWDMS MDEDVALFLQ EFKAPDIFMG VLAKSPCPRL REICVGILGN
     MACFREICES ISKNEDHGQV LLQCLCDSDP PTLLETCRLL LTCLSQTEVA SVWVRRIREH
     PSVYANVCFI MSSSTNVDLL VKVGEVVDKL FDLDEKLMLE WIRKGATRLP GQPHEDSEEQ
     PVFSIVPCVL EAAKQVRSEN LEGLDVYMRI LQLLTTVDDG VQAIVQCPDT GNDTWRLLFD
     LVCHEFCQPD DPPVILQEQK TVLASVFSVL SAISASRAEQ EHLKIEEGDL PLIDSLIRVL
     QNMEHCQKKP ENPSESDTEE PTICGPTQDD FHMKILKDIS CEFLSNIFQV LTKEKVAQGL
     KEGQLSKQKC SCAFQSLLPL YGPAVEDFVK VVREVDEALA DDLEDSFPSV KAQT
//
ID   DTNA_MOUSE              Reviewed;         746 AA.
AC   Q9D2N4; P97319; Q61498; Q61499; Q9QZZ5; Q9WUL9; Q9WUM0;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 2.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Dystrobrevin alpha;
DE            Short=DTN-A;
DE   AltName: Full=Alpha-dystrobrevin;
GN   Name=Dtna; Synonyms=Dtn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 7).
RC   TISSUE=Brain;
RX   MEDLINE=96205975; PubMed=8631824; DOI=10.1074/jbc.271.13.7802;
RA   Blake D.J., Nawrotzki R., Peters M.F., Froehner S.C., Davies K.E.;
RT   "Isoform diversity of dystrobrevin, the murine 87-kDa postsynaptic
RT   protein.";
RL   J. Biol. Chem. 271:7802-7810(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC   STRAIN=129/Sv; TISSUE=Brain;
RX   MEDLINE=97224465; PubMed=9119373; DOI=10.1006/geno.1996.4515;
RA   Ambrose H.J., Blake D.J., Nawrotzki R.A., Davies K.E.;
RT   "Genomic organization of the mouse dystrobrevin gene: comparative
RT   analysis with the dystrophin gene.";
RL   Genomics 39:359-369(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RC   TISSUE=Muscle;
RX   MEDLINE=98369056; PubMed=9701558;
RA   Nawrotzki R., Loh N.Y., Ruegg M.A., Davies K.E., Blake D.J.;
RT   "Characterisation of alpha-dystrobrevin in muscle.";
RL   J. Cell Sci. 111:2595-2605(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4 AND 6).
RC   STRAIN=C3H; TISSUE=Muscle;
RX   MEDLINE=20035753; PubMed=10570976; DOI=10.1016/S0378-1119(99)00358-3;
RA   Enigk R.E., Maimone M.M.;
RT   "Differential expression and developmental regulation of a novel
RT   alpha-dystrobrevin isoform in muscle.";
RL   Gene 238:479-488(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   INTERACTION WITH SNTA1.
RX   MEDLINE=96032613; PubMed=7547961; DOI=10.1021/bi00038a014;
RA   Madhavan R., Jarrett H.W.;
RT   "Interactions between dystrophin glycoprotein complex proteins.";
RL   Biochemistry 34:12204-12209(1995).
RN   [7]
RP   INTERACTION WITH SNTB1.
RX   MEDLINE=97362062; PubMed=9214383; DOI=10.1083/jcb.138.1.81;
RA   Peters M.F., Adams M.E., Froehner S.C.;
RT   "Differential association of syntrophin pairs with the dystrophin
RT   complex.";
RL   J. Cell Biol. 138:81-93(1997).
RN   [8]
RP   INTERACTION WITH DYSTROBREVIN BINDING PROTEIN 1.
RX   MEDLINE=21316514; PubMed=11316798; DOI=10.1074/jbc.M010418200;
RA   Benson M.A., Newey S.E., Martin-Rendon E., Hawkes R., Blake D.J.;
RT   "Dysbindin, a novel coiled-coil-containing protein that interacts with
RT   the dystrobrevins in muscle and brain.";
RL   J. Biol. Chem. 276:24232-24241(2001).
RN   [9]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH MAGEE1.
RX   PubMed=14623885; DOI=10.1074/jbc.M312205200;
RA   Albrecht D.E., Froehner S.C.;
RT   "DAMAGE, a novel alpha-dystrobrevin-associated MAGE protein in
RT   dystrophin complexes.";
RL   J. Biol. Chem. 279:7014-7023(2004).
CC   -!- FUNCTION: Involved in synapse maturation and required for normal
CC       muscle function.
CC   -!- SUBUNIT: Interacts with dystrophin, utrophin and the syntrophins
CC       SNTA1, SNTB1, SNTB2, SNTG1 and SNTG2. Isoforms 5 and 6 do not
CC       interact with syntrophin. Isoforms 3 and 4 do not interact with
CC       utrophin. Binds dystrobrevin binding protein 1. Interacts with
CC       MAGEE1.
CC   -!- INTERACTION:
CC       Q91WZ8:Dtnbp1; NbExp=1; IntAct=EBI-296019, EBI-643186;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell junction, synapse. Cell
CC       membrane. Note=In peripheral nerves, co-localizes with MAGEE1 in
CC       the Schwann cell membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1;
CC         IsoId=Q9D2N4-1; Sequence=Displayed;
CC       Name=2; Synonyms=Alpha-dystrobrevin-1, Alpha-DB1;
CC         IsoId=Q9D2N4-2; Sequence=VSP_004215, VSP_004220;
CC       Name=3; Synonyms=Alpha-dystrobrevin-2B, Alpha-DB2B;
CC         IsoId=Q9D2N4-3; Sequence=VSP_004221, VSP_004222;
CC       Name=4; Synonyms=Alpha-dystrobrevin-2A, Alpha-DB2A;
CC         IsoId=Q9D2N4-4; Sequence=VSP_004218, VSP_004219;
CC       Name=5; Synonyms=Alpha-dystrobrevin-3, Alpha-DB3;
CC         IsoId=Q9D2N4-5; Sequence=VSP_004214, VSP_004216, VSP_004217;
CC       Name=6; Synonyms=Alpha-dystrobrevin-3, Alpha-DB3;
CC         IsoId=Q9D2N4-6; Sequence=VSP_004216, VSP_004217;
CC       Name=7;
CC         IsoId=Q9D2N4-7; Sequence=VSP_004214, VSP_004215, VSP_004218,
CC                                  VSP_004219;
CC   -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, heart, lung and
CC       brain. Sarcolemma and neuromuscular junction in skeletal muscle.
CC       Isoform 2 is restricted to the neuromuscular junction. Isoforms 5
CC       and 6 are only expressed in muscle.
CC   -!- DEVELOPMENTAL STAGE: Expression of alpha-dystrobrevin is up-
CC       regulated during differentiation, with isoforms 2, 5 and 6
CC       expressed earliest and isoform 3 and 4 expressed later.
CC   -!- DOMAIN: The coiled coil domain mediates the interaction with
CC       dystrophin and utrophin.
CC   -!- PTM: Phosphorylation of isoform 2 on tyrosine kinase substrate
CC       domain present in the C-terminus.
CC   -!- SIMILARITY: Belongs to the dystrophin family. Dystrobrevin
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 ZZ-type zinc finger.
CC   -----------------------------------------------------------------------
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DR   EMBL; X95226; CAA64518.1; -; mRNA.
DR   EMBL; X95227; CAA64519.1; -; mRNA.
DR   EMBL; Z79787; CAB02145.1; -; Genomic_DNA.
DR   EMBL; Z79788; CAB02145.1; JOINED; Genomic_DNA.
DR   EMBL; Z79789; CAB02145.1; JOINED; Genomic_DNA.
DR   EMBL; Z79790; CAB02145.1; JOINED; Genomic_DNA.
DR   EMBL; Z79791; CAB02145.1; JOINED; Genomic_DNA.
DR   EMBL; Z79792; CAB02145.1; JOINED; Genomic_DNA.
DR   EMBL; Z79793; CAB02145.1; JOINED; Genomic_DNA.
DR   EMBL; Z79794; CAB02145.1; JOINED; Genomic_DNA.
DR   EMBL; Z79795; CAB02145.1; JOINED; Genomic_DNA.
DR   EMBL; Z79796; CAB02145.1; JOINED; Genomic_DNA.
DR   EMBL; Z79797; CAB02145.1; JOINED; Genomic_DNA.
DR   EMBL; AJ009669; CAA08770.1; -; mRNA.
DR   EMBL; AF143544; AAD33915.1; -; mRNA.
DR   EMBL; AF143543; AAD33914.1; -; mRNA.
DR   EMBL; AF143542; AAD33913.1; -; mRNA.
DR   EMBL; AK019477; BAB31746.1; -; mRNA.
DR   IPI; IPI00135042; -.
DR   IPI; IPI00222692; -.
DR   IPI; IPI00222693; -.
DR   IPI; IPI00222694; -.
DR   IPI; IPI00410809; -.
DR   IPI; IPI00466606; -.
DR   IPI; IPI00755441; -.
DR   RefSeq; NP_034217.2; NM_010087.3.
DR   UniGene; Mm.94371; -.
DR   ProteinModelPortal; Q9D2N4; -.
DR   IntAct; Q9D2N4; 9.
DR   MINT; MINT-197169; -.
DR   STRING; Q9D2N4; -.
DR   PhosphoSite; Q9D2N4; -.
DR   PRIDE; Q9D2N4; -.
DR   Ensembl; ENSMUST00000025156; ENSMUSP00000025156; ENSMUSG00000024302.
DR   Ensembl; ENSMUST00000047954; ENSMUSP00000037475; ENSMUSG00000024302.
DR   Ensembl; ENSMUST00000075123; ENSMUSP00000074624; ENSMUSG00000024302.
DR   Ensembl; ENSMUST00000115832; ENSMUSP00000111498; ENSMUSG00000024302.
DR   Ensembl; ENSMUST00000115833; ENSMUSP00000111499; ENSMUSG00000024302.
DR   Ensembl; ENSMUST00000115834; ENSMUSP00000111500; ENSMUSG00000024302.
DR   GeneID; 13527; -.
DR   KEGG; mmu:13527; -.
DR   UCSC; uc008efs.1; mouse.
DR   UCSC; uc008efv.1; mouse.
DR   UCSC; uc008efw.1; mouse.
DR   UCSC; uc008efx.1; mouse.
DR   CTD; 13527; -.
DR   MGI; MGI:106039; Dtna.
DR   eggNOG; roNOG10345; -.
DR   GeneTree; ENSGT00550000074400; -.
DR   HOVERGEN; HBG005539; -.
DR   InParanoid; Q9D2N4; -.
DR   OrthoDB; EOG40GCQ7; -.
DR   ArrayExpress; Q9D2N4; -.
DR   Bgee; Q9D2N4; -.
DR   CleanEx; MM_DTNA; -.
DR   Genevestigator; Q9D2N4; -.
DR   GermOnline; ENSMUSG00000024302; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016014; C:dystrobrevin complex; NAS:UniProtKB.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0042383; C:sarcolemma; TAS:MGI.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR017432; Distrobrevin.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR015153; EF-hand_dom_typ1.
DR   InterPro; IPR015154; EF-hand_dom_typ2.
DR   InterPro; IPR000433; Znf_ZZ.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF09068; efhand_1; 1.
DR   Pfam; PF09069; efhand_2; 1.
DR   Pfam; PF00569; ZZ; 1.
DR   PIRSF; PIRSF038204; Distrobrevin; 1.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Coiled coil;
KW   Cytoplasm; Membrane; Metal-binding; Phosphoprotein; Synapse; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    746       Dystrobrevin alpha.
FT                                /FTId=PRO_0000080037.
FT   ZN_FING     237    284       ZZ-type.
FT   REGION        1    288       Interaction with MAGEE1.
FT   REGION      397    447       Syntrophin-binding region.
FT   COILED      458    557       Potential.
FT   MOD_RES     666    666       Phosphoserine (By similarity).
FT   VAR_SEQ     334    334       V -> VDTW (in isoform 5 and isoform 7).
FT                                /FTId=VSP_004214.
FT   VAR_SEQ     363    419       Missing (in isoform 2 and isoform 7).
FT                                /FTId=VSP_004215.
FT   VAR_SEQ     364    371       PPKDSEVE -> DGAHGGCV (in isoform 5 and
FT                                isoform 6).
FT                                /FTId=VSP_004216.
FT   VAR_SEQ     372    746       Missing (in isoform 5 and isoform 6).
FT                                /FTId=VSP_004217.
FT   VAR_SEQ     559    570       TQGASSPRSSPS -> VMHEIIPLEERT (in isoform
FT                                3).
FT                                /FTId=VSP_004221.
FT   VAR_SEQ     559    567       TQGASSPRS -> VSYVPYCRS (in isoform 4 and
FT                                isoform 7).
FT                                /FTId=VSP_004218.
FT   VAR_SEQ     560    561       QG -> R (in isoform 2).
FT                                /FTId=VSP_004220.
FT   VAR_SEQ     568    746       Missing (in isoform 4 and isoform 7).
FT                                /FTId=VSP_004219.
FT   VAR_SEQ     571    746       Missing (in isoform 3).
FT                                /FTId=VSP_004222.
FT   CONFLICT    241    241       V -> L (in Ref. 1; CAA64519).
FT   CONFLICT    251    251       M -> I (in Ref. 5; BAB31746).
FT   CONFLICT    259    259       Q -> P (in Ref. 4; AAD33915).
FT   CONFLICT    416    416       D -> N (in Ref. 4; AAD33915/AAD33914).
SQ   SEQUENCE   746 AA;  84067 MW;  6AB7EF3B69250A09 CRC64;
     MIEDSGKRGN TMAERRQLFA EMRAQDLDRI RLSTYRTACK LRFVQKKCNL HLVDIWNVIE
     ALRENALNNL DPNIELNVAR LEAVLSTIFY QLNKRMPTTH QIHVEQSISL LLNFLLAAFD
     PEGHGKISVF AVKMALATLC GGKIMDKLRY IFSMISDSSG VMVYGRYDQF LREVLKLPTA
     VFEGPSFGYT EQSARSCFSQ QKKVTLNGFL DTLMSDPPPQ CLVWLPLLHR LANVENVFHP
     VECSYCHSES MMGFRYRCQQ CHNYQLCQDC FWRGHAGGSH SNQHQMKEYT SWKSPAKKLT
     NALSKSLSCA SSREPLHPMF PDQPEKPLNL AHIVPPRPVT SMNDTLFSHS VPSSGSPFIT
     RSSPPKDSEV EQNKMLARAA PAFLKGRGIQ YSLNVADRLA DEHVLIGLYV NMLRNDPPCM
     LESSNRLDEE HRLIARYAAR LAAESSSSQP TQQRSAPDIS FTIDANKQQR QLIAELENKN
     REILQEIQRL RVEHEQASQP TPEKAQQNPT LLAELRLLRQ RKDELEQRMS ALQESRRELM
     VQLEGLMKLL KEEELKQGTQ GASSPRSSPS HTISRPIPMP IRSASACPTP THTPQDSLTG
     VGGDVQEAFA QSSRRNLRSD LLVAADSITN TMSSLVKELN SEVASETEST VDSEFSRPQF
     EDLAPSPTSE KAFLAQIHSR KPGYIHGGAA STTHGDMVPE DGDPYTQPED GNYENESVRQ
     LENELQLEEY LKQKLQDEAY QVSLQG
//
ID   MOBP_MOUSE              Reviewed;         170 AA.
AC   Q9D2P8; O35713; Q792D7; Q792D8; Q9JLY4; Q9JLY5; Q9JLY6;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Myelin-associated oligodendrocyte basic protein;
GN   Name=Mobp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6;
RX   MEDLINE=96133585; PubMed=8551331;
RA   Holz A., Schaeren-Wiemers N., Schaefer C., Pott U., Colello R.J.,
RA   Schwab M.E.;
RT   "Molecular and developmental characterization of novel cDNAs of the
RT   myelin-associated/oligodendrocytic basic protein.";
RL   J. Neurosci. 16:467-477(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS
RP   1; 2; 3; 4 AND 5).
RC   STRAIN=129/Sv;
RX   MEDLINE=99263202; PubMed=10328883; DOI=10.1006/mcne.1999.0745;
RA   McCallion A.S., Stewart G.J., Montague P., Griffiths I.R.,
RA   Davies R.W.;
RT   "Splicing pattern, transcript start distribution, and DNA sequence of
RT   the mouse gene (Mobp) encoding myelin-associated oligodendrocytic
RT   basic protein.";
RL   Mol. Cell. Neurosci. 13:229-236(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
RP   2).
RC   STRAIN=CAST/Ei, and SJL/J;
RA   Lee I.Y., Baxter D.H., Qin S., Hood L.E.;
RT   "Genomic sequence analysis of laminin receptor loci in mice.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Corpora quadrigemina, and Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in compacting or stabilizing the myelin
CC       sheath possibly by binding the negatively charged acidic
CC       phospholipids of the cytoplasmic membrane (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Note=Present
CC       in the major dense line of CNS myelin (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1; Synonyms=MOBP170;
CC         IsoId=Q9D2P8-1; Sequence=Displayed;
CC       Name=2; Synonyms=MOBP81;
CC         IsoId=Q9D2P8-2; Sequence=VSP_023936, VSP_023942;
CC       Name=3; Synonyms=MOBP73;
CC         IsoId=Q9D2P8-3; Sequence=VSP_023937, VSP_023941;
CC       Name=4; Synonyms=MOBP69;
CC         IsoId=Q9D2P8-4; Sequence=VSP_023938, VSP_023939;
CC       Name=5; Synonyms=MOBP74;
CC         IsoId=Q9D2P8-5; Sequence=VSP_023940, VSP_023941;
CC   -----------------------------------------------------------------------
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DR   EMBL; U81317; AAB65617.1; -; mRNA.
DR   EMBL; AF120475; AAF60192.1; -; Genomic_DNA.
DR   EMBL; AF120476; AAF60193.1; -; Genomic_DNA.
DR   EMBL; AF120475; AAF60193.1; JOINED; Genomic_DNA.
DR   EMBL; AF120475; AAF60194.1; -; Genomic_DNA.
DR   EMBL; AF120476; AAF60195.1; -; Genomic_DNA.
DR   EMBL; AF120475; AAF60195.1; JOINED; Genomic_DNA.
DR   EMBL; AF120477; AAF60196.1; -; Genomic_DNA.
DR   EMBL; AF120475; AAF60196.1; JOINED; Genomic_DNA.
DR   EMBL; DQ360291; ABC95974.1; -; Genomic_DNA.
DR   EMBL; DQ360292; ABC95978.1; -; Genomic_DNA.
DR   EMBL; AK013799; BAB28998.1; -; mRNA.
DR   EMBL; AK019323; BAB31666.1; -; mRNA.
DR   EMBL; AK028057; BAC25727.1; -; mRNA.
DR   EMBL; AK083103; BAC38761.1; -; mRNA.
DR   EMBL; AK140055; BAE24224.1; -; mRNA.
DR   EMBL; BC048492; AAH48492.1; -; mRNA.
DR   IPI; IPI00133833; -.
DR   IPI; IPI00135106; -.
DR   IPI; IPI00459474; -.
DR   IPI; IPI00831462; -.
DR   IPI; IPI00831551; -.
DR   RefSeq; NP_001034453.1; NM_001039364.2.
DR   RefSeq; NP_001034454.1; NM_001039365.2.
DR   RefSeq; NP_032640.1; NM_008614.2.
DR   UniGene; Mm.40461; -.
DR   ProteinModelPortal; Q9D2P8; -.
DR   SMR; Q9D2P8; 1-68.
DR   STRING; Q9D2P8; -.
DR   PhosphoSite; Q9D2P8; -.
DR   PRIDE; Q9D2P8; -.
DR   Ensembl; ENSMUST00000035103; ENSMUSP00000035103; ENSMUSG00000032517.
DR   Ensembl; ENSMUST00000068698; ENSMUSP00000071084; ENSMUSG00000032517.
DR   Ensembl; ENSMUST00000093773; ENSMUSP00000091287; ENSMUSG00000032517.
DR   Ensembl; ENSMUST00000111626; ENSMUSP00000107253; ENSMUSG00000032517.
DR   Ensembl; ENSMUST00000111627; ENSMUSP00000107254; ENSMUSG00000032517.
DR   GeneID; 17433; -.
DR   KEGG; mmu:17433; -.
DR   UCSC; uc009scj.1; mouse.
DR   CTD; 17433; -.
DR   MGI; MGI:108511; Mobp.
DR   eggNOG; roNOG08323; -.
DR   GeneTree; ENSGT00390000013933; -.
DR   HOVERGEN; HBG081977; -.
DR   InParanoid; Q9D2P8; -.
DR   OMA; CACQRIR; -.
DR   OrthoDB; EOG4JWVG3; -.
DR   NextBio; 292060; -.
DR   ArrayExpress; Q9D2P8; -.
DR   Bgee; Q9D2P8; -.
DR   CleanEx; MM_MOBP; -.
DR   Genevestigator; Q9D2P8; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019911; F:structural constituent of myelin sheath; IDA:MGI.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Repeat.
FT   CHAIN         1    170       Myelin-associated oligodendrocyte basic
FT                                protein.
FT                                /FTId=PRO_0000281026.
FT   REPEAT       93    101       1.
FT   REPEAT      105    110       2.
FT   REPEAT      111    115       3; half-length.
FT   REGION       93    115       3 X 9 AA approximate tandem repeats.
FT   COMPBIAS     75    155       Pro-rich.
FT   VAR_SEQ      69     81       SRRATSPQRPKHQ -> RLRRRSRSTPRKK (in
FT                                isoform 2).
FT                                /FTId=VSP_023936.
FT   VAR_SEQ      69     73       SRRAT -> RTVRK (in isoform 3).
FT                                /FTId=VSP_023937.
FT   VAR_SEQ      69     69       S -> R (in isoform 4).
FT                                /FTId=VSP_023938.
FT   VAR_SEQ      70    170       Missing (in isoform 4).
FT                                /FTId=VSP_023939.
FT   VAR_SEQ      70     73       RRAT -> MTFW (in isoform 5).
FT                                /FTId=VSP_023940.
FT   VAR_SEQ      74    170       Missing (in isoform 3 and isoform 5).
FT                                /FTId=VSP_023941.
FT   VAR_SEQ      82    170       Missing (in isoform 2).
FT                                /FTId=VSP_023942.
FT   CONFLICT      5      5       M -> V (in Ref. 2; AAF60192/AAF60193/
FT                                AAF60194/AAF60195/AAF60196).
SQ   SEQUENCE   170 AA;  19197 MW;  E3132C958C631BC4 CRC64;
     MSQKMAKEGP RLSKNQKFSE HFSIHCCPPF TFLNSKREIV DRKYSICKSG CFYQKKEEDW
     ICCACQKTSR RATSPQRPKH QPAASPVVVR APPAKPKSPL MPAKPRSPPR PAKPRSPSRT
     ERQPRPRPEV RPPPAKQKPP QKSKQPARSS PLRGPGTSRG GSPTRAPRFW
//
ID   CJ088_MOUSE             Reviewed;         444 AA.
AC   Q9D2Q3;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Uncharacterized protein C10orf88 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Thymus, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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CC   -----------------------------------------------------------------------
DR   EMBL; AK019097; BAB31544.1; -; mRNA.
DR   EMBL; AK088850; BAC40612.1; -; mRNA.
DR   EMBL; AK148008; BAE28285.1; -; mRNA.
DR   EMBL; BC044749; AAH44749.1; -; mRNA.
DR   IPI; IPI00271998; -.
DR   RefSeq; NP_080931.1; NM_026655.3.
DR   UniGene; Mm.121122; -.
DR   PhosphoSite; Q9D2Q3; -.
DR   PRIDE; Q9D2Q3; -.
DR   Ensembl; ENSMUST00000059438; ENSMUSP00000050128; ENSMUSG00000040177.
DR   GeneID; 68277; -.
DR   KEGG; mmu:68277; -.
DR   UCSC; uc009kbg.1; mouse.
DR   MGI; MGI:1915527; 2310057M21Rik.
DR   eggNOG; roNOG08522; -.
DR   GeneTree; ENSGT00390000017384; -.
DR   HOGENOM; HBG283311; -.
DR   HOVERGEN; HBG081190; -.
DR   InParanoid; Q9D2Q3; -.
DR   OMA; VLDDSEH; -.
DR   OrthoDB; EOG4K0QNC; -.
DR   PhylomeDB; Q9D2Q3; -.
DR   NextBio; 326906; -.
DR   ArrayExpress; Q9D2Q3; -.
DR   Bgee; Q9D2Q3; -.
DR   CleanEx; MM_2310057M21RIK; -.
DR   Genevestigator; Q9D2Q3; -.
DR   GermOnline; ENSMUSG00000040177; Mus musculus.
DR   GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
PE   2: Evidence at transcript level;
FT   CHAIN         1    444       Uncharacterized protein C10orf88 homolog.
FT                                /FTId=PRO_0000260086.
SQ   SEQUENCE   444 AA;  48743 MW;  40949A5121D57A23 CRC64;
     METAIEDAGL DRGPTLTSSW DAACGALTQS LFLTRTGPRA QDLDFEQLLE PPAPSQDPVS
     LKSSLSPRDE NPCFIYLNCG PNGGEEILSV GVLSSARNME VYLGEEYCGT SRGKTACTVL
     DDSEHEKILL YKKYLKLDSP THACKIKLLS FGEKQCVLVS KVVVHLRPRS ADPSPRSAAL
     GSRIDLDNIQ TIMESMGSRL SPGAQQLMSM IRFQQQNRLP IGDQLQSVLG SAGHKHLMAL
     QSSPSPAVLD KASSTPFPFR TGLTPSAITE NLKALIDKSA QPSGEGNTTN HDEGHLMPQN
     HSLESDLKNA VSSFLPKKAS GSSSVPSSEL LPFLQNLCSQ VNHLRVGHNA RWQENISKPR
     EGMVGVPMEE QPVCSYLEKI LSKNMELMEK KLMDHIDERI YQLQEHIDAK MALLVDLLRG
     PNSPPPGMPL RHYDSRERLS NGER
//
ID   CORO7_MOUSE             Reviewed;         922 AA.
AC   Q9D2V7; Q3UDJ4; Q6P8Y8; Q8C9V7;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Coronin-7;
DE            Short=Crn7;
DE   AltName: Full=70 kDa WD repeat tumor rejection antigen homolog;
GN   Name=Coro7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Kidney, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15327992; DOI=10.1016/j.febslet.2004.07.066;
RA   Rybakin V., Stumpf M., Schulze A., Majoul I.V., Noegel A.A., Hasse A.;
RT   "Coronin 7, the mammalian POD-1 homologue, localizes to the Golgi
RT   apparatus.";
RL   FEBS Lett. 573:161-167(2004).
CC   -!- FUNCTION: May play a role in the maintenance of the Golgi
CC       apparatus morphology and in the protein export from the Golgi (By
CC       similarity).
CC   -!- SUBUNIT: Interacted with clathrin adapter AP1 complex. This
CC       interaction takes place at Golgi membranes and not AP1-positive
CC       endosomal membranes (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Golgi apparatus
CC       membrane. Cytoplasmic vesicle. Note=Predominantly cytoplasmic.
CC       Detected on vesicle-like cytoplasmic structures and on the cis-
CC       Golgi. Not associated with actin filaments.
CC   -!- TISSUE SPECIFICITY: In the adult, widely expressed with highest
CC       levels in brain, thymus and kidney and low levels in skeletal and
CC       heart muscle. Not expressed in lung. In the eye, strongly
CC       expressed in the outer plexiform layer of the retina. In the
CC       intestine, expressed both in terminally differentiated epithelial
CC       cells and in crypt epithelium. In the embryo, strongest expression
CC       is seen in brain, thymus, intestine, apical epidermal layers of
CC       the skin and developing lens fibers of the eye.
CC   -!- DEVELOPMENTAL STAGE: In the embryo, expressed from 5 dpc and
CC       levels increase strongly until 15 dpc.
CC   -!- PTM: The membrane-associated form is phosphorylated on tyrosine
CC       residues.
CC   -!- SIMILARITY: Belongs to the WD repeat coronin family.
CC   -!- SIMILARITY: Contains 8 WD repeats.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK018739; BAB31380.1; -; mRNA.
DR   EMBL; AK040408; BAC30588.1; -; mRNA.
DR   EMBL; AK150051; BAE29267.1; -; mRNA.
DR   EMBL; BC061006; AAH61006.1; -; mRNA.
DR   IPI; IPI00135390; -.
DR   RefSeq; NP_084481.3; NM_030205.4.
DR   UniGene; Mm.325512; -.
DR   UniGene; Mm.477052; -.
DR   ProteinModelPortal; Q9D2V7; -.
DR   SMR; Q9D2V7; 6-390, 467-863.
DR   STRING; Q9D2V7; -.
DR   PhosphoSite; Q9D2V7; -.
DR   PRIDE; Q9D2V7; -.
DR   Ensembl; ENSMUST00000038552; ENSMUSP00000048489; ENSMUSG00000039637.
DR   GeneID; 78885; -.
DR   KEGG; mmu:78885; -.
DR   UCSC; uc007xzy.1; mouse.
DR   CTD; 78885; -.
DR   MGI; MGI:1926135; Coro7.
DR   GeneTree; ENSGT00550000074317; -.
DR   HOGENOM; HBG356893; -.
DR   HOVERGEN; HBG051080; -.
DR   InParanoid; Q9D2V7; -.
DR   OMA; GHQDQIF; -.
DR   OrthoDB; EOG49S65R; -.
DR   PhylomeDB; Q9D2V7; -.
DR   NextBio; 349664; -.
DR   ArrayExpress; Q9D2V7; -.
DR   Bgee; Q9D2V7; -.
DR   CleanEx; MM_CORO7; -.
DR   Genevestigator; Q9D2V7; -.
DR   GermOnline; ENSMUSG00000039637; Mus musculus.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000299; C:integral to membrane of membrane fraction; IDA:MGI.
DR   GO; GO:0005625; C:soluble fraction; IDA:MGI.
DR   InterPro; IPR015505; Coronin.
DR   InterPro; IPR015049; DUF1900.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
DR   PANTHER; PTHR10856; Coronin; 1.
DR   Pfam; PF08954; DUF1900; 2.
DR   Pfam; PF00400; WD40; 6.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 6.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Cytoplasmic vesicle; Golgi apparatus;
KW   Membrane; Phosphoprotein; Repeat; WD repeat.
FT   CHAIN         1    922       Coronin-7.
FT                                /FTId=PRO_0000050935.
FT   REPEAT       75    115       WD 1.
FT   REPEAT      124    163       WD 2.
FT   REPEAT      166    205       WD 3.
FT   REPEAT      209    253       WD 4.
FT   REPEAT      539    581       WD 5.
FT   REPEAT      589    629       WD 6.
FT   REPEAT      632    671       WD 7.
FT   REPEAT      725    765       WD 8.
FT   MOD_RES     469    469       N6-acetyllysine (By similarity).
FT   MOD_RES     912    912       Phosphoserine (By similarity).
FT   CONFLICT    364    364       V -> M (in Ref. 1; BAB31380).
FT   CONFLICT    372    372       W -> R (in Ref. 1; BAC30588).
FT   CONFLICT    468    468       S -> C (in Ref. 1; BAB31380).
FT   CONFLICT    518    518       Q -> E (in Ref. 1; BAB31380).
SQ   SEQUENCE   922 AA;  100812 MW;  0B7F1C4166940936 CRC64;
     MSRFKVSKFR HMEARPSRRE AWISDIRAVT TPTCGNHIKS SCSLIAFNSD RPGVLGVISL
     EGHEENKRHV TYLGCHSDLV TDLDFSPFDD FLLASGSADR TIKLWRLSGT GEALPSVPGV
     VLGPEELPVE VLQFHPTVDG VLVSTAGKTV KVWDVAKQQP LTELEAHKDL VQSAVWSRDG
     AIVGTACKDK QLRIFDPRAR TQASQSTQAH ENNRDIRLAW TGIQEHLVST GFNQMREREA
     KLWDTRLFSS ALASVTLDTS PGPLIPLLDP DSGLLVLAGK GENQLYCYEV TPQQPALSPV
     TQCILENVLR GAALVPRRAL AVMSCEVLQV LQLSDTAIIP ISHHVPRKAV EFHEDLFPDT
     AGSVPASDAH MWWAGDNQQV QKVSLNPARR PHPCFTSSLV PTMEPAPDMV QPAEMPRADT
     DLSEGFSSPS SLMSPSTPSS LGPSLSSTSG IGTSPSQRSL QSLLGPSSKF RHTQGSLLHR
     DSHITNLKGL NLTTPGESDG FCANRLRVAV PLLSSGGQVA VLELQKPGRL PDTALPTLQN
     GTAVMDLVWD PFDPHRLAVA GEDARIRLWR VPPGGLENVL TTPETVLTGH TEKIYSLRFH
     PLAADVLASS SYDLTVRIWD LQTGAERLKL QGHQDQIFSL AWSPDGKQLA TVCKDGHVRV
     YEPRSSPLPL QEGPGPEGGR GARIVWVCDG GCLLVSGFDS RSERQLQLYI ADALAQGPSA
     LLGLDVAPST LLPSYDPDTG LVLLTGKGDT RVFLYEVLPE APFFLECNSF TSPDPHKGFV
     LLPKTECDIQ DVEFARCLRL RQTSLEPVAF RLPRVRKEFF QDDVFPDTAV TWEPALSAKA
     WFEGANGQPR LLSLQPPGMT PVSQAPREVP ARRAPSSAQY LEEKSDQQKK EELLNAMVAK
     LGNREDPLPQ DSFEGVDEDE WD
//
ID   RUFY3_MOUSE             Reviewed;         469 AA.
AC   Q9D394; Q3U348; Q3UF96; Q6PE64; Q8VD10;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Protein RUFY3;
DE   AltName: Full=Rap2-interacting protein x;
DE            Short=RIPx;
DE   AltName: Full=Single axon-regulated protein;
DE            Short=Singar;
GN   Name=Rufy3; Synonyms=D5Bwg0860e, Ripx;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 27-469 (ISOFORM 4).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Hippocampus, Medulla oblongata, and Sympathetic ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E.,
RA   Mollenhauer J., Wiemann S., Schick M., Korn B.;
RT   "Cloning of mouse full open reading frames in Gateway(R) system entry
RT   vector (pDONR201).";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 (ISOFORMS 2 AND 4),
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 65-247.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Crystal structure of the RUN domain of mouse RAP2 interacting protein
RT   X.";
RL   Submitted (JUN-2005) to the PDB data bank.
CC   -!- FUNCTION: Implicated in the formation of a single axon by
CC       developing neurons. May inhibit the formation of additional axons
CC       by inhibition of PI3K in minor neuronal processes (By similarity).
CC   -!- SUBUNIT: Interacts with PIK3CA and PIK3R1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell projection (By similarity).
CC       Note=Enriched in F-actin enriched filopodia and lamellipodia of
CC       growth cones of axons and minor processes of hippocampal neurons
CC       in culture (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9D394-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D394-2; Sequence=VSP_019792, VSP_019794;
CC         Note=Phosphorylated on Ser-27. Ref.1 (BAE32941) sequence is in
CC         conflict in position: 55:V->A;
CC       Name=3;
CC         IsoId=Q9D394-3; Sequence=VSP_019793;
CC       Name=4;
CC         IsoId=Q9D394-4; Sequence=VSP_019792;
CC         Note=Phosphorylated on Ser-27;
CC   -!- PTM: Isoform 1 is partially phosphorylated (By similarity).
CC   -!- SIMILARITY: Contains 1 RUN domain.
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DR   EMBL; AK018184; BAB31113.1; -; mRNA.
DR   EMBL; AK083242; BAC38826.1; -; mRNA.
DR   EMBL; AK148795; BAE28665.1; -; mRNA.
DR   EMBL; AK154941; BAE32941.1; -; mRNA.
DR   EMBL; CT010404; CAJ18610.1; -; mRNA.
DR   EMBL; BC017648; AAH17648.1; -; mRNA.
DR   EMBL; BC049127; AAH49127.1; -; mRNA.
DR   EMBL; BC058259; AAH58259.1; -; mRNA.
DR   IPI; IPI00453965; -.
DR   IPI; IPI00622482; -.
DR   IPI; IPI00761269; -.
DR   IPI; IPI00762081; -.
DR   RefSeq; NP_081806.1; NM_027530.2.
DR   UniGene; Mm.270469; -.
DR   PDB; 2CXF; X-ray; 3.07 A; A=65-247.
DR   PDB; 2CXL; X-ray; 3.20 A; A=65-247.
DR   PDB; 2DWG; X-ray; 3.22 A; A/B=65-237.
DR   PDB; 2DWK; X-ray; 2.00 A; A=65-237.
DR   PDBsum; 2CXF; -.
DR   PDBsum; 2CXL; -.
DR   PDBsum; 2DWG; -.
DR   PDBsum; 2DWK; -.
DR   ProteinModelPortal; Q9D394; -.
DR   SMR; Q9D394; 65-231.
DR   STRING; Q9D394; -.
DR   PRIDE; Q9D394; -.
DR   Ensembl; ENSMUST00000031229; ENSMUSP00000031229; ENSMUSG00000029291.
DR   Ensembl; ENSMUST00000087029; ENSMUSP00000084255; ENSMUSG00000029291.
DR   Ensembl; ENSMUST00000101048; ENSMUSP00000098609; ENSMUSG00000029291.
DR   Ensembl; ENSMUST00000113238; ENSMUSP00000108864; ENSMUSG00000029291.
DR   GeneID; 52822; -.
DR   KEGG; mmu:52822; -.
DR   UCSC; uc008xzw.1; mouse.
DR   UCSC; uc008xzx.1; mouse.
DR   UCSC; uc008xzy.1; mouse.
DR   UCSC; uc008xzz.1; mouse.
DR   CTD; 52822; -.
DR   MGI; MGI:106484; Rufy3.
DR   eggNOG; roNOG08636; -.
DR   GeneTree; ENSGT00550000074558; -.
DR   HOVERGEN; HBG057053; -.
DR   OrthoDB; EOG41G348; -.
DR   NextBio; 309587; -.
DR   ArrayExpress; Q9D394; -.
DR   Bgee; Q9D394; -.
DR   CleanEx; MM_RUFY3; -.
DR   Genevestigator; Q9D394; -.
DR   GermOnline; ENSMUSG00000029291; Mus musculus.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   InterPro; IPR004012; Run.
DR   Pfam; PF02759; RUN; 1.
DR   SMART; SM00593; RUN; 1.
DR   PROSITE; PS50826; RUN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cell projection;
KW   Coiled coil; Developmental protein; Differentiation; Neurogenesis;
KW   Phosphoprotein.
FT   CHAIN         1    469       Protein RUFY3.
FT                                /FTId=PRO_0000245834.
FT   DOMAIN       95    227       RUN.
FT   COILED      267    464       Potential.
FT   MOD_RES     181    181       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1     60       MSALTPPTDMPTPTTDKITQAAMETIYLCKFRVSMDGEWLC
FT                                LRELDDISLTPDPEPTHED -> MAESPAPGAAAESCGEEQ
FT                                ERGGERRPSEPLEPRGASARGADREDEAGPSEPDSPVAAPF
FT                                FLLYPGDGGAGFTARPPPQRAWRTPPSPGSPLPFLLLSYPS
FT                                GGSGGGGKHH (in isoform 2 and isoform 4).
FT                                /FTId=VSP_019792.
FT   VAR_SEQ      58     58       H -> HEDSWEDLTDLVEQVRADP (in isoform 3).
FT                                /FTId=VSP_019793.
FT   VAR_SEQ     446    469       SEKDLVKQAKTLNSAANKLIPKHH -> RLRQAERGRQSAE
FT                                LDNRLFKQDFGDKINSLQLEVEALTRQRTQLELELKQEKER
FT                                KSQNRGTPGKGAQKPELRMDGKHRIQEENVKLKKPLEESHR
FT                                LLTHPAEEQGQPSLSEKPQVCQLCQEDDSLTKNTCRNCRGT
FT                                FCNACTTNELPLPSSIKPERVCNPCHEQLIKQYS (in
FT                                isoform 2).
FT                                /FTId=VSP_019794.
FT   CONFLICT    224    224       M -> I (in Ref. 3; AAH17648).
FT   CONFLICT    251    251       S -> G (in Ref. 1; BAE32941).
FT   HELIX        66     90
FT   HELIX        99    113
FT   HELIX       130    139
FT   HELIX       141    143
FT   HELIX       144    151
FT   HELIX       159    173
FT   HELIX       176    184
FT   HELIX       187    190
FT   TURN        191    193
FT   HELIX       199    201
FT   HELIX       203    211
FT   HELIX       212    217
FT   HELIX       226    229
SQ   SEQUENCE   469 AA;  53007 MW;  CFB8D2C3363D06BD CRC64;
     MSALTPPTDM PTPTTDKITQ AAMETIYLCK FRVSMDGEWL CLRELDDISL TPDPEPTHED
     PNYLMANERM NLMNMAKLSI KGLIESALNL GRTLDSDYAP LQQFFVVMEH CLKHGLKAKK
     TFLGQNKSFW GPLELVEKLV PEAAEITASV KDLPGLKTPV GRGRAWLRLA LMQKKLSEYM
     KALINKKELL SEFYEVNALM MEEEGAIIAG LLVGLNVIDA NFCMKGEDLD SQVGVIDFSM
     YLKDGNSSKG SEGDGQITAI LDQKNYVEEL NRHLNATVNN LQTKVDLLEK SNTKLTEELA
     VANNRIITLQ EEMERVKEES SYLLESNRKG PKQDRTAEGQ ALSEARKHLK EETQLRLDVE
     KELELQISMR QEMELAMKML EKDVCEKQDA LVSLRQQLDD LRALKHELAF KLQSSDLGVK
     QKSELNSRLE EKTNQMAATI KQLEQSEKDL VKQAKTLNSA ANKLIPKHH
//
ID   CAPON_MOUSE             Reviewed;         503 AA.
AC   Q9D3A8; Q80TZ6;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Carboxyl-terminal PDZ ligand of neuronal nitric oxide synthase protein;
DE   AltName: Full=C-terminal PDZ ligand of neuronal nitric oxide synthase protein;
DE   AltName: Full=Nitric oxide synthase 1 adaptor protein;
GN   Name=Nos1ap; Synonyms=Capon, Kiaa0464;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 195-503 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   INTERACTION WITH RASD1 AND NOS1.
RX   MEDLINE=20537828; PubMed=11086993; DOI=10.1016/S0896-6273(00)00095-7;
RA   Fang M., Jaffrey S.R., Sawa A., Ye K., Luo X., Snyder S.H.;
RT   "Dexras1: a G protein specifically coupled to neuronal nitric oxide
RT   synthase via CAPON.";
RL   Neuron 28:183-193(2000).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183; SER-187 AND
RP   SER-370, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Adapter protein involved in neuronal nitric-oxide (NO)
CC       synthesis regulation via its association with nNOS/NOS1. The
CC       complex formed with NOS1 and synapsins is necessary for specific
CC       NO and synapsin functions at a presynaptic level. Mediates an
CC       indirect interaction between NOS1 and RASD1 leading to enhance the
CC       ability of NOS1 to activate RASD1. Competes with DLG4 for
CC       interaction with NOS1, possibly affecting NOS1 activity by
CC       regulating the interaction between NOS1 and DLG4 (By similarity).
CC   -!- SUBUNIT: Interacts with the PDZ domain of NOS1 or the second PDZ
CC       domain of DLG4 through its C-terminus. Interacts with RASD1 and
CC       SYN1, SYN2 and SYN3 via its PID domain. Forms a ternary complex
CC       with NOS1 and SYN1 (By similarity). Forms a ternary complex with
CC       NOS1 and RASD1.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9D3A8-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q9D3A8-2; Sequence=VSP_012462, VSP_012463;
CC   -!- SIMILARITY: Contains 1 PID domain.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK018149; BAB31095.1; -; mRNA.
DR   EMBL; AK122290; BAC65572.3; -; Transcribed_RNA.
DR   IPI; IPI00135786; -.
DR   IPI; IPI00515529; -.
DR   UniGene; Mm.65316; -.
DR   ProteinModelPortal; Q9D3A8; -.
DR   SMR; Q9D3A8; 18-171.
DR   STRING; Q9D3A8; -.
DR   PhosphoSite; Q9D3A8; -.
DR   PRIDE; Q9D3A8; -.
DR   Ensembl; ENSMUST00000082106; ENSMUSP00000080753; ENSMUSG00000038473.
DR   UCSC; uc007dmg.1; mouse.
DR   MGI; MGI:1917979; Nos1ap.
DR   GeneTree; ENSGT00510000046975; -.
DR   HOGENOM; HBG715549; -.
DR   HOVERGEN; HBG050788; -.
DR   InParanoid; Q9D3A8; -.
DR   OrthoDB; EOG49KFQP; -.
DR   ArrayExpress; Q9D3A8; -.
DR   Bgee; Q9D3A8; -.
DR   Genevestigator; Q9D3A8; -.
DR   GermOnline; ENSMUSG00000038473; Mus musculus.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00640; PID; 1.
DR   SMART; SM00462; PTB; 1.
DR   PROSITE; PS01179; PID; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Phosphoprotein.
FT   CHAIN         1    503       Carboxyl-terminal PDZ ligand of neuronal
FT                                nitric oxide synthase protein.
FT                                /FTId=PRO_0000089317.
FT   DOMAIN       26    191       PID.
FT   REGION      491    503       Interaction with NOS1 (By similarity).
FT   COILED      318    359       Potential.
FT   MOTIF       501    503       PDZ-binding (By similarity).
FT   COMPBIAS    269    272       Poly-Ser.
FT   COMPBIAS    297    304       Poly-Gln.
FT   MOD_RES     183    183       Phosphoserine.
FT   MOD_RES     187    187       Phosphoserine.
FT   MOD_RES     262    262       Phosphoserine (By similarity).
FT   MOD_RES     367    367       Phosphoserine (By similarity).
FT   MOD_RES     370    370       Phosphoserine.
FT   VAR_SEQ     313    325       LKDQLAAEAAARL -> SLLPSSQAPLSWA (in
FT                                isoform 2).
FT                                /FTId=VSP_012462.
FT   VAR_SEQ     326    503       Missing (in isoform 2).
FT                                /FTId=VSP_012463.
SQ   SEQUENCE   503 AA;  55851 MW;  056F67E6CD03E381 CRC64;
     MPSKTKYNLV DDGHDLRIPL HNEDSFQHGI SFEAKYVGSL DVPRPNSRVE IVAAMRRIRY
     EFKAKNIKKK KVSIMVSVDG VKVILKKKKK KKEWTWDESK MLVMQDPIYK IFYVSHDSQD
     LKIFSYIARD GASNIFRCNV FKSKKKSQAM RIVRTVAQAF EVCHKLSLQH TQQNADGQED
     GESERNSDGS GDPGRQLTGA ERVSTAAAEE TDIDAVEVPL PGNDILEFSR GVTDLDAVGK
     DGGSHIDSTV SPHPQEPMLT ASPRMLLPSS SSKPPGLGTG TPLSTHHQMQ LLQQLLQQQQ
     QQTQVAVAQV LLLKDQLAAE AAARLEAQAR VHQLLLQNKD MLQHISLLVK QVQELELKLS
     GQNTMGSQDS LLEITFRSGA LPVLCESTTP KPEDLHSPLL GAGLADFAHP AGSPLGRHDC
     LVKLECFRFL PPEDTQPMMA QGEPLLGGLE LIKFRESGIA SEYESNTDES EERDSWSQEE
     LPRLLNVLQR QELGDSLDDE IAV
//
ID   TTYH1_MOUSE             Reviewed;         450 AA.
AC   Q9D3A9; Q6L751; Q6P0A7; Q8BRL4; Q8C7M4; Q9D5D1; Q9EQN7; Q9ESC3;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Protein tweety homolog 1;
DE            Short=mTTY1;
GN   Name=Ttyh1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=BALB/c;
RX   MEDLINE=20408891; PubMed=10950931; DOI=10.1006/geno.2000.6259;
RA   Campbell H.D., Kamei M., Claudianos C., Woollatt E., Sutherland G.R.,
RA   Suzuki Y., Hida M., Sugano S., Young I.G.;
RT   "Human and mouse homologues of the Drosophila melanogaster tweety
RT   (tty) gene: a novel gene family encoding predicted transmembrane
RT   proteins.";
RL   Genomics 68:89-92(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15010458; DOI=10.1074/jbc.M313813200;
RA   Suzuki M., Mizuno A.;
RT   "A novel human Cl(-) channel family related to Drosophila flightless
RT   locus.";
RL   J. Biol. Chem. 279:22461-22468(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain cortex, Head, Hippocampus, Medulla oblongata, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=17116230; DOI=10.1111/j.1471-4159.2006.04237.x;
RA   Matthews C.A., Shaw J.E., Hooper J.A., Young I.G., Crouch M.F.,
RA   Campbell H.D.;
RT   "Expression and evolution of the mammalian brain gene Ttyh1.";
RL   J. Neurochem. 100:693-707(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448 AND SER-449, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Probable chloride channel. Isoform 3 may be a Ca(2+)-
CC       independent and swelling-activated chloride channel, possibly
CC       involved in regulation of cell volume. May be involved in cell
CC       adhesion (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q9D3A9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D3A9-2; Sequence=VSP_029766;
CC       Name=3; Synonyms=TTYH1s;
CC         IsoId=Q9D3A9-3; Sequence=VSP_029764;
CC       Name=4;
CC         IsoId=Q9D3A9-4; Sequence=VSP_029765;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q9D3A9-5; Sequence=VSP_029762, VSP_029763;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Restricted mainly to neural tissues. Strongly
CC       expressed in brain and eye.
CC   -!- SIMILARITY: Belongs to the tweety family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF190991; AAG15842.1; -; mRNA.
DR   EMBL; AF190699; AAG02615.1; -; mRNA.
DR   EMBL; DQ104403; AAZ06803.1; -; Genomic_DNA.
DR   EMBL; AB162929; BAD20188.1; -; mRNA.
DR   EMBL; AK015486; BAB29865.1; -; mRNA.
DR   EMBL; AK018148; BAB31094.1; -; mRNA.
DR   EMBL; AK043998; BAC31730.1; -; mRNA.
DR   EMBL; AK048413; BAC33329.1; -; mRNA.
DR   EMBL; AK049903; BAC33980.1; -; mRNA.
DR   EMBL; BC046310; AAH46310.1; -; mRNA.
DR   EMBL; BC065694; AAH65694.1; -; mRNA.
DR   IPI; IPI00113244; -.
DR   IPI; IPI00420152; -.
DR   IPI; IPI00551270; -.
DR   IPI; IPI00623995; -.
DR   IPI; IPI00875552; -.
DR   RefSeq; NP_001001454.2; NM_001001454.3.
DR   RefSeq; NP_001103235.1; NM_001109765.1.
DR   RefSeq; NP_067299.2; NM_021324.5.
DR   UniGene; Mm.29729; -.
DR   PhosphoSite; Q9D3A9; -.
DR   PRIDE; Q9D3A9; -.
DR   Ensembl; ENSMUST00000032594; ENSMUSP00000032594; ENSMUSG00000030428.
DR   Ensembl; ENSMUST00000079415; ENSMUSP00000078384; ENSMUSG00000030428.
DR   Ensembl; ENSMUST00000086397; ENSMUSP00000083585; ENSMUSG00000030428.
DR   Ensembl; ENSMUST00000086398; ENSMUSP00000083586; ENSMUSG00000030428.
DR   Ensembl; ENSMUST00000108591; ENSMUSP00000104232; ENSMUSG00000030428.
DR   Ensembl; ENSMUST00000119661; ENSMUSP00000113937; ENSMUSG00000030428.
DR   GeneID; 57776; -.
DR   KEGG; mmu:57776; -.
DR   UCSC; uc009eww.1; mouse.
DR   CTD; 57776; -.
DR   MGI; MGI:1889007; Ttyh1.
DR   eggNOG; maNOG08892; -.
DR   GeneTree; ENSGT00390000010182; -.
DR   HOVERGEN; HBG108621; -.
DR   NextBio; 313948; -.
DR   ArrayExpress; Q9D3A9; -.
DR   Bgee; Q9D3A9; -.
DR   CleanEx; MM_TTYH1; -.
DR   Genevestigator; Q9D3A9; -.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0031527; C:filopodium membrane; IDA:MGI.
DR   GO; GO:0032433; C:filopodium tip; IDA:MGI.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0016337; P:cell-cell adhesion; IDA:MGI.
DR   GO; GO:0031589; P:cell-substrate adhesion; IDA:MGI.
DR   GO; GO:0046847; P:filopodium assembly; IDA:MGI.
DR   InterPro; IPR006990; Tweety.
DR   PANTHER; PTHR12424; Tweety; 1.
DR   Pfam; PF04906; Tweety; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Cell membrane; Chloride;
KW   Chloride channel; Glycoprotein; Ion transport; Ionic channel;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    450       Protein tweety homolog 1.
FT                                /FTId=PRO_0000312241.
FT   TOPO_DOM      1     43       Extracellular (Potential).
FT   TRANSMEM     44     64       Helical; Name=1; (Potential).
FT   TOPO_DOM     65     88       Cytoplasmic (Potential).
FT   TRANSMEM     89    109       Helical; Name=2; (Potential).
FT   TOPO_DOM    110    214       Extracellular (Potential).
FT   TRANSMEM    215    235       Helical; Name=3; (Potential).
FT   TOPO_DOM    236    240       Cytoplasmic (Potential).
FT   TRANSMEM    241    261       Helical; Name=4; (Potential).
FT   TOPO_DOM    262    390       Extracellular (Potential).
FT   TRANSMEM    391    411       Helical; Name=5; (Potential).
FT   TOPO_DOM    412    450       Cytoplasmic (Potential).
FT   COMPBIAS    424    433       Poly-Asp.
FT   MOD_RES     448    448       Phosphoserine.
FT   MOD_RES     449    449       Phosphoserine.
FT   CARBOHYD    130    130       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    284    284       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    355    355       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ       1     96       Missing (in isoform 5).
FT                                /FTId=VSP_029762.
FT   VAR_SEQ      97    102       ALLVGC -> MQRSNS (in isoform 5).
FT                                /FTId=VSP_029763.
FT   VAR_SEQ     423    450       SDDYDDTDDDDPFNPQESKRFVQWQSSI -> RNPNALCSG
FT                                SLPSEPPLQSGACSPLCSFPGCWRRPH (in isoform
FT                                3).
FT                                /FTId=VSP_029764.
FT   VAR_SEQ     423    450       SDDYDDTDDDDPFNPQESKRFVQWQSSI -> RNPNALCSG
FT                                SLPSEPPLQSGACLSSMLLSWLLEKAPLT (in isoform
FT                                4).
FT                                /FTId=VSP_029765.
FT   VAR_SEQ     443    450       FVQWQSSI -> LYQNRDRSLRRESRIFACSATRVI (in
FT                                isoform 2).
FT                                /FTId=VSP_029766.
FT   CONFLICT     15     15       L -> P (in Ref. 1; AAG02615/AAG15842).
FT   CONFLICT     21     21       R -> L (in Ref. 3; BAC31730).
FT   CONFLICT    116    116       S -> T (in Ref. 3; BAB29865).
FT   CONFLICT    151    151       V -> M (in Ref. 3; BAB29865).
FT   CONFLICT    288    288       E -> G (in Ref. 1; AAG02615/AAG15842 and
FT                                2; BAD20188).
FT   CONFLICT    427    427       D -> Y (in Ref. 3; BAB29865).
SQ   SEQUENCE   450 AA;  49032 MW;  53A93E0EC7D16EB8 CRC64;
     MGAPPGYRPS AWVHLLHQLP RADFQLRPVP SGFAPRDQEY QQALLLVAAL AGLGLGLSLI
     FIAVYLIRFC CCRPPEPHGA KSPPPGGGCV TWSCIAALLV GCAGIGIGFY GNSETSDGVS
     QLSSALLHAN HTLSTIDDVV LETVERLGEA VKTELTTLEE VLSVRMELVA ATRGARRQAE
     AAAQYLQGLA FWQGVSLSPV QVAEDVTFVE EYRWLAYVLL LLLVLLVCLF TLLGLAKQSK
     WLVVVMTAMS LLVLVLSWGS MGLEAATAVG LSDFCSNPDT YVLNLTQEET GLSSDILSYY
     FLCNQAVSNP FQQRLTLSQR ALASIHSQLQ GLEREAIPQF SAAQKPLLSL EETLNVTERS
     FHQLVALLHC RSLHKDYGSA LRGLCEDALE GLLFLMLFSL LSAGALATTL CSLPRAWALF
     PPSDDYDDTD DDDPFNPQES KRFVQWQSSI
//
ID   ATPD_MOUSE              Reviewed;         168 AA.
AC   Q9D3D9;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=ATP synthase subunit delta, mitochondrial;
DE   AltName: Full=F-ATPase delta subunit;
DE   Flags: Precursor;
GN   Name=Atp5d;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 137-150 AND 157-165, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-136, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Heart;
RX   PubMed=17451654; DOI=10.1016/j.bbrc.2007.04.015;
RA   Jeon H.B., Choi E.S., Yoon J.H., Hwang J.H., Chang J.W., Lee E.K.,
RA   Choi H.W., Park Z.-Y., Yoo Y.J.;
RT   "A proteomics approach to identify the ubiquitinated proteins in mouse
RT   heart.";
RL   Biochem. Biophys. Res. Commun. 357:731-736(2007).
CC   -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
CC       synthase or Complex V) produces ATP from ADP in the presence of a
CC       proton gradient across the membrane which is generated by electron
CC       transport complexes of the respiratory chain. F-type ATPases
CC       consist of two structural domains, F(1) - containing the
CC       extramembraneous catalytic core, and F(0) - containing the
CC       membrane proton channel, linked together by a central stalk and a
CC       peripheral stalk. During catalysis, ATP turnover in the catalytic
CC       domain of F(1) is coupled via a rotary mechanism of the central
CC       stalk subunits to proton translocation. Part of the complex F(1)
CC       domain and of the central stalk which is part of the complex
CC       rotary element. Rotation of the central stalk against the
CC       surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in
CC       three separate catalytic sites on the beta subunits.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel. CF(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC       seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or
CC       A6L).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC   -!- SIMILARITY: Belongs to the ATPase epsilon chain family.
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DR   EMBL; AK018011; BAB31035.1; -; mRNA.
DR   EMBL; BC008273; AAH08273.1; -; mRNA.
DR   IPI; IPI00453777; -.
DR   RefSeq; NP_079589.2; NM_025313.2.
DR   UniGene; Mm.278560; -.
DR   ProteinModelPortal; Q9D3D9; -.
DR   SMR; Q9D3D9; 37-167.
DR   STRING; Q9D3D9; -.
DR   PhosphoSite; Q9D3D9; -.
DR   UCD-2DPAGE; Q9D3D9; -.
DR   PRIDE; Q9D3D9; -.
DR   Ensembl; ENSMUST00000003156; ENSMUSP00000003156; ENSMUSG00000003072.
DR   Ensembl; ENSMUST00000105367; ENSMUSP00000101006; ENSMUSG00000003072.
DR   GeneID; 66043; -.
DR   KEGG; mmu:66043; -.
DR   CTD; 66043; -.
DR   MGI; MGI:1913293; Atp5d.
DR   HOGENOM; HBG663981; -.
DR   HOVERGEN; HBG001856; -.
DR   InParanoid; Q9D3D9; -.
DR   OMA; QVDVPTQ; -.
DR   OrthoDB; EOG4894NT; -.
DR   PhylomeDB; Q9D3D9; -.
DR   NextBio; 320454; -.
DR   ArrayExpress; Q9D3D9; -.
DR   Bgee; Q9D3D9; -.
DR   Genevestigator; Q9D3D9; -.
DR   GermOnline; ENSMUSG00000003072; Mus musculus.
DR   GO; GO:0046933; F:hydrogen ion transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR001469; ATPase_F1-cplx_dsu/esu.
DR   InterPro; IPR020547; ATPase_F1-cplx_dsu/esu_C.
DR   InterPro; IPR020546; ATPase_F1-cplx_dsu/esu_N.
DR   Gene3D; G3DSA:2.60.15.10; ATPase_F1_d/e; 1.
DR   PANTHER; PTHR13822; ATPase_F1_d/e; 1.
DR   Pfam; PF02823; ATP-synt_DE_N; 1.
DR   ProDom; PD000944; ATPase_F1-cplx_dsu/esu; 1.
DR   SUPFAM; SSF46604; ATPsynt_DE; 1.
DR   SUPFAM; SSF51344; ATPsynt_DE; 1.
DR   TIGRFAMs; TIGR01216; ATP_synt_epsi; 1.
PE   1: Evidence at protein level;
KW   ATP synthesis; CF(1); Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Isopeptide bond; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Transit peptide;
KW   Transport; Ubl conjugation.
FT   TRANSIT       1     22       Mitochondrion (By similarity).
FT   CHAIN        23    168       ATP synthase subunit delta,
FT                                mitochondrial.
FT                                /FTId=PRO_0000002662.
FT   CROSSLNK    136    136       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
SQ   SEQUENCE   168 AA;  17600 MW;  EC3DF1B581B630E9 CRC64;
     MLPASLLRHP GLRRLMLQAR TYAEAAAAPA PAAGPGQMSF TFASPTQVFF DSANVKQVDV
     PTLTGAFGIL ASHVPTLQVL RPGLVVVHTE DGTTTKYFVS SGSVTVNADS SVQLLAEEAV
     TLDMLDLGAA RANLEKAQSE LSGAADEAAR AEIQIRIEAN EALVKALE
//
ID   F174A_MOUSE             Reviewed;         190 AA.
AC   Q9D3L0; Q3UF92; Q8CC46; Q8VDR1; Q9D238; Q9D6W5; Q9D6Z3;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 2.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Membrane protein FAM174A;
DE   AltName: Full=Transmembrane protein 157;
DE   Flags: Precursor;
GN   Name=Fam174a; Synonyms=Tmem157;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Diencephalon, Head, Sympathetic ganglion, Tongue, and
RC   Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- SIMILARITY: Belongs to the FAM174 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB26509.1; Type=Frameshift; Positions=167;
CC       Sequence=BAB26567.1; Type=Frameshift; Positions=166;
CC       Sequence=BAE28669.1; Type=Frameshift; Positions=154;
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DR   EMBL; AK009797; BAB26509.1; ALT_FRAME; mRNA.
DR   EMBL; AK009892; BAB26567.1; ALT_FRAME; mRNA.
DR   EMBL; AK017318; BAB30690.1; -; mRNA.
DR   EMBL; AK020633; BAB32159.1; -; mRNA.
DR   EMBL; AK033948; BAC28523.1; -; mRNA.
DR   EMBL; AK148807; BAE28669.1; ALT_FRAME; mRNA.
DR   EMBL; BC021428; AAH21428.1; -; mRNA.
DR   IPI; IPI00317487; -.
DR   RefSeq; NP_080597.2; NM_026321.4.
DR   UniGene; Mm.272705; -.
DR   ProteinModelPortal; Q9D3L0; -.
DR   PRIDE; Q9D3L0; -.
DR   Ensembl; ENSMUST00000059975; ENSMUSP00000057670; ENSMUSG00000051185.
DR   GeneID; 67698; -.
DR   KEGG; mmu:67698; -.
DR   UCSC; uc007cex.1; mouse.
DR   CTD; 67698; -.
DR   MGI; MGI:1914948; Fam174a.
DR   eggNOG; roNOG17892; -.
DR   GeneTree; ENSGT00530000064028; -.
DR   HOVERGEN; HBG098565; -.
DR   InParanoid; Q9D3L0; -.
DR   OMA; PNPGDKP; -.
DR   OrthoDB; EOG4T1HP8; -.
DR   PhylomeDB; Q9D3L0; -.
DR   NextBio; 325293; -.
DR   ArrayExpress; Q9D3L0; -.
DR   Bgee; Q9D3L0; -.
DR   Genevestigator; Q9D3L0; -.
DR   GermOnline; ENSMUSG00000051185; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR009565; DUF1180.
DR   Pfam; PF06679; DUF1180; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     31       Potential.
FT   CHAIN        32    190       Membrane protein FAM174A.
FT                                /FTId=PRO_0000263651.
FT   TOPO_DOM     32    123       Extracellular (Potential).
FT   TRANSMEM    124    144       Helical; (Potential).
FT   TOPO_DOM    145    190       Cytoplasmic (Potential).
FT   CARBOHYD     83     83       N-linked (GlcNAc...) (Potential).
FT   CONFLICT     33     33       P -> R (in Ref. 2; AAH21428).
FT   CONFLICT     84     84       D -> G (in Ref. 2; AAH21428).
FT   CONFLICT    131    131       V -> G (in Ref. 1; BAB26509).
FT   CONFLICT    134    134       A -> P (in Ref. 1; BAB26509).
FT   CONFLICT    137    137       V -> G (in Ref. 1; BAB26509).
FT   CONFLICT    144    144       V -> I (in Ref. 2; AAH21428).
FT   CONFLICT    152    152       K -> R (in Ref. 1; BAB32159).
FT   CONFLICT    166    166       M -> K (in Ref. 1; BAB30690).
FT   CONFLICT    176    176       E -> K (in Ref. 1; BAB30690).
FT   CONFLICT    181    181       T -> P (in Ref. 1; BAB26567).
FT   CONFLICT    189    189       R -> K (in Ref. 1; BAB26567).
SQ   SEQUENCE   190 AA;  19986 MW;  D7EEB04A6E04D1F9 CRC64;
     MPTPRGCSGP CHFLAPAFVL LLLPALSGSG AVPSMVVREV QESKSPKPGP HTLSPLPPGP
     TAAQPRGQAQ SDAAGLPGAE SRNDSIPGAG SEADGLEGKA GEGSQGGSLA VSPSPGDKPM
     TQRALTVLVV VSAAVLVYFV VRTVRMRRRN RKTRRYGVLD TNIENMELTP LEQDDEDDDN
     TLFDANHPRR
//
ID   PACRL_MOUSE             Reviewed;         248 AA.
AC   Q9D3X5;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=PACRG-like protein;
GN   Name=Pacrgl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
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DR   EMBL; AK016966; BAB30527.1; -; mRNA.
DR   EMBL; AK032498; BAC27898.1; -; mRNA.
DR   EMBL; BC018481; AAH18481.1; -; mRNA.
DR   IPI; IPI00136738; -.
DR   RefSeq; NP_080031.1; NM_025755.3.
DR   UniGene; Mm.29409; -.
DR   ProteinModelPortal; Q9D3X5; -.
DR   PRIDE; Q9D3X5; -.
DR   Ensembl; ENSMUST00000030968; ENSMUSP00000030968; ENSMUSG00000029089.
DR   GeneID; 66768; -.
DR   KEGG; mmu:66768; -.
DR   UCSC; uc008xjs.1; mouse.
DR   CTD; 66768; -.
DR   MGI; MGI:1914018; Pacrgl.
DR   eggNOG; roNOG04918; -.
DR   GeneTree; ENSGT00530000063549; -.
DR   HOGENOM; HBG279944; -.
DR   HOVERGEN; HBG102880; -.
DR   InParanoid; Q9D3X5; -.
DR   OMA; INPFGEQ; -.
DR   OrthoDB; EOG4HQDK8; -.
DR   PhylomeDB; Q9D3X5; -.
DR   NextBio; 322602; -.
DR   ArrayExpress; Q9D3X5; -.
DR   Bgee; Q9D3X5; -.
DR   Genevestigator; Q9D3X5; -.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR019399; Parkin_co-regulated_protein.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF10274; ParcG; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    248       PACRG-like protein.
FT                                /FTId=PRO_0000278244.
FT   MOD_RES      47     47       Phosphoserine.
SQ   SEQUENCE   248 AA;  27290 MW;  B255BBCE0AABCAC9 CRC64;
     MQRSECSGGV QLRNRATGSN DQRTSSSTQM KHRTTVQRSK SSSLTSSPEA ARRARPRPSD
     KLNPKTINPF GEQPRAPTAF AAIYSQGGIP CRLVHGSVKH RLQWECPPEI LPFDPLLITL
     AEGLRETKHP YTFVSKEGFR ELLLVKGAPE KAIPLLPRLI PVLKAALVHS DDEVFERGLS
     ALVQLSVVVG PSLNGHLKLL LTSLSKRLMD KKFKEPITSA LQKLEQHGGN ASLIIIKSKI
     PTYCSICC
//
ID   MFA3L_MOUSE             Reviewed;         409 AA.
AC   Q9D3X9; Q80TV6; Q8BJA9;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Microfibrillar-associated protein 3-like;
DE   Flags: Precursor;
GN   Name=Mfap3l; Synonyms=Kiaa0626;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 60-409 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9D3X9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D3X9-2; Sequence=VSP_014096;
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK016959; BAB30523.1; -; mRNA.
DR   EMBL; AK089654; BAC40939.1; -; mRNA.
DR   EMBL; BC095950; AAH95950.1; -; mRNA.
DR   EMBL; AK122332; BAC65614.1; -; mRNA.
DR   IPI; IPI00136754; -.
DR   IPI; IPI00607916; -.
DR   RefSeq; NP_001171352.1; NM_001177881.1.
DR   RefSeq; NP_001171353.1; NM_001177882.1.
DR   RefSeq; NP_082032.1; NM_027756.4.
DR   UniGene; Mm.23242; -.
DR   ProteinModelPortal; Q9D3X9; -.
DR   SMR; Q9D3X9; 20-176.
DR   PRIDE; Q9D3X9; -.
DR   Ensembl; ENSMUST00000034066; ENSMUSP00000034066; ENSMUSG00000031647.
DR   GeneID; 71306; -.
DR   KEGG; mmu:71306; -.
DR   UCSC; uc009ltf.1; mouse.
DR   UCSC; uc009ltg.1; mouse.
DR   CTD; 71306; -.
DR   MGI; MGI:1918556; Mfap3l.
DR   eggNOG; roNOG10062; -.
DR   GeneTree; ENSGT00390000011576; -.
DR   HOGENOM; HBG446881; -.
DR   HOVERGEN; HBG052463; -.
DR   InParanoid; Q9D3X9; -.
DR   OMA; RHTPEGQ; -.
DR   OrthoDB; EOG4N30P4; -.
DR   PhylomeDB; Q9D3X9; -.
DR   NextBio; 333509; -.
DR   ArrayExpress; Q9D3X9; -.
DR   Bgee; Q9D3X9; -.
DR   CleanEx; MM_MFAP3L; -.
DR   Genevestigator; Q9D3X9; -.
DR   GermOnline; ENSMUSG00000031647; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF07679; I-set; 1.
DR   SMART; SM00408; IGc2; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     28       Potential.
FT   CHAIN        29    409       Microfibrillar-associated protein 3-like.
FT                                /FTId=PRO_0000014870.
FT   TOPO_DOM     29    148       Extracellular (Potential).
FT   TRANSMEM    149    169       Helical; (Potential).
FT   TOPO_DOM    170    409       Cytoplasmic (Potential).
FT   CARBOHYD     33     33       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     37     37       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     67     67       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    111    111       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    135    135       N-linked (GlcNAc...) (Potential).
FT   DISULFID     68    125       By similarity.
FT   VAR_SEQ       1    103       Missing (in isoform 2).
FT                                /FTId=VSP_014096.
FT   CONFLICT    283    283       R -> G (in Ref. 1; BAC40939).
SQ   SEQUENCE   409 AA;  45342 MW;  BC0B3FA7568AA4C8 CRC64;
     MGLQKSHLTV CLPPSVPFLI LVSTLATAKS VTNSTLNGTD VVLGSVPVII ARTDHIIVKE
     GSSALINCSA YGFPDLEFKW YNSVGKLLKE MDDEKEKGGG KWQMLDGGLL NITKVSFSDR
     GKYTCVASNI YGTINNTVTL RVIFTSGDMG VYYMVVCLVA FTIVMILNIT RLCMMSSHLK
     KTEKAINEFF RTEGAEKLQK AFEIAKRIPI ITSAKTLELA KVTQFKTMEF ARYIEELARS
     VPLPPLIMNC RTIMEEIMEV VGLEEQGQNF VRHTPEGQEA PDRDEVYTIP NSLKRSESPT
     ADSDASSLHE QPQQIAIKVS VHPQSKRDHV DDQEGGHFEV KDEEETEPSE EHSPETAEPS
     TDITTTELTS EETSPVEAPE RGLPPAHLET TEPAVTCDRN TCIIYESHV
//
ID   OXSM_MOUSE              Reviewed;         459 AA.
AC   Q9D404;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial;
DE            EC=2.3.1.41;
DE   AltName: Full=Beta-ketoacyl-ACP synthase;
DE   Flags: Precursor;
GN   Name=Oxsm;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Heart, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: May play a role in the biosynthesis of lipoic acid as
CC       well as longer chain fatty acids required for optimal
CC       mitochondrial function (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + malonyl-[acyl-
CC       carrier-protein] = 3-oxoacyl-[acyl-carrier-protein] + CO(2) +
CC       [acyl-carrier-protein].
CC   -!- ENZYME REGULATION: Inhibited by cerulenin (By similarity).
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the beta-ketoacyl-ACP synthases family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK016905; BAB30490.1; -; mRNA.
DR   EMBL; AK083617; BAC38969.1; -; mRNA.
DR   EMBL; AK084829; BAC39286.1; -; mRNA.
DR   IPI; IPI00136333; -.
DR   RefSeq; NP_081971.1; NM_027695.3.
DR   UniGene; Mm.197960; -.
DR   ProteinModelPortal; Q9D404; -.
DR   SMR; Q9D404; 40-459.
DR   STRING; Q9D404; -.
DR   PhosphoSite; Q9D404; -.
DR   PRIDE; Q9D404; -.
DR   Ensembl; ENSMUST00000022311; ENSMUSP00000022311; ENSMUSG00000021786.
DR   Ensembl; ENSMUST00000112624; ENSMUSP00000108243; ENSMUSG00000021786.
DR   Ensembl; ENSMUST00000112625; ENSMUSP00000108244; ENSMUSG00000021786.
DR   GeneID; 71147; -.
DR   KEGG; mmu:71147; -.
DR   UCSC; uc007sgw.1; mouse.
DR   CTD; 71147; -.
DR   MGI; MGI:1918397; Oxsm.
DR   GeneTree; ENSGT00530000063309; -.
DR   HOGENOM; HBG757733; -.
DR   HOVERGEN; HBG082096; -.
DR   InParanoid; Q9D404; -.
DR   OMA; KDHAYAL; -.
DR   OrthoDB; EOG41JZC4; -.
DR   PhylomeDB; Q9D404; -.
DR   BRENDA; 2.3.1.41; 244.
DR   NextBio; 333127; -.
DR   ArrayExpress; Q9D404; -.
DR   Bgee; Q9D404; -.
DR   CleanEx; MM_OXSM; -.
DR   Genevestigator; Q9D404; -.
DR   GermOnline; ENSMUSG00000021786; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; ISS:HGNC.
DR   GO; GO:0006637; P:acyl-CoA metabolic process; ISS:HGNC.
DR   GO; GO:0051792; P:medium-chain fatty acid biosynthetic process; ISS:HGNC.
DR   GO; GO:0051790; P:short-chain fatty acid biosynthetic process; ISS:HGNC.
DR   InterPro; IPR017568; 3-oxoacyl-ACP_synth-2.
DR   InterPro; IPR000794; Beta-ketoacyl_synthase.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016039; Thiolase-like.
DR   InterPro; IPR016038; Thiolase-like_subgr.
DR   Gene3D; G3DSA:3.40.47.10; Thiolase-like_subgr; 2.
DR   PANTHER; PTHR11712; Ketoacyl_synth; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   PIRSF; PIRSF000447; KAS_II; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 2.
DR   TIGRFAMs; TIGR03150; fabF; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Acyltransferase; Fatty acid biosynthesis;
KW   Lipid synthesis; Mitochondrion; Transferase; Transit peptide.
FT   TRANSIT       1     27       Mitochondrion (Potential).
FT   CHAIN        28    459       3-oxoacyl-[acyl-carrier-protein]
FT                                synthase, mitochondrial.
FT                                /FTId=PRO_0000232661.
FT   MOD_RES     174    174       N6-acetyllysine (By similarity).
SQ   SEQUENCE   459 AA;  48628 MW;  47F9733FBBF08BE1 CRC64;
     MLSKCLQHFL KATISHPYPA SYSWLISKHR FYGTVPAAML RRRVVITGIG LVTPLGVGTQ
     LVWDRLLRGE SGIVSVVGDE YKNIPCSVAA YVPRGPHEGQ FNEENFVSKS DAKSMSSSTI
     MAVGAAELAL KDSGWHPKRE ADQVATGVAI GMGMVPLEVI SETALLFQTK GYNKVSPFFV
     PKILINMAAG QVSIRYKLKG PNHSVSTACT TGAHAVGDSF RFIAHGDADV MVAGGTDSCI
     SPLSLAGFSR ARALSSNPDP KLACRPFHPE RDGFVMGEGA AVLVLEEHEH AVQRGARIYA
     EILGYGLSGD AGHITAPDPE GEGALRCMAA AVKDAGVSPE QISYVNAHAT STPLGDAAEN
     RAIKRLFRDH ACALAISSTK GATGHLLGAA GAVEATFTAL ACYHQKLPPT LNLDCTEPEF
     DLNYVPLESQ EWKAEGRCIG LTNSFGFGGT NATLCIAGM
//
ID   DLGP1_MOUSE             Reviewed;         992 AA.
AC   Q9D415; Q52KF6; Q5DTK5; Q6P6N4; Q6XBF4; Q8BZL7; Q8BZQ1; Q8C0G0;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 3.
DT   08-FEB-2011, entry version 84.
DE   RecName: Full=Disks large-associated protein 1;
DE            Short=DAP-1;
DE   AltName: Full=Guanylate kinase-associated protein;
DE   AltName: Full=PSD-95/SAP90-binding protein 1;
DE   AltName: Full=SAP90/PSD-95-associated protein 1;
DE            Short=SAPAP1;
GN   Name=Dlgap1; Synonyms=Kiaa4162;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RC   STRAIN=ICR;
RX   PubMed=15024750; DOI=10.1002/cne.20060;
RA   Welch J.M., Wang D., Feng G.;
RT   "Differential mRNA expression and protein localization of the
RT   SAP90/PSD-95-associated proteins (SAPAPs) in the nervous system of the
RT   mouse.";
RL   J. Comp. Neurol. 472:24-39(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 660-992 (ISOFORM 4).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 210-992 (ISOFORM 4).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134; SER-352; SER-362;
RP   SER-412; SER-437; SER-446; SER-499; SER-509; SER-516 AND SER-947, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-123, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389; SER-421; THR-436;
RP   SER-509 AND SER-516, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Part of the postsynaptic scaffold in neuronal cells.
CC   -!- SUBUNIT: Interacts with the guanylate kinase-like domain of DLG1,
CC       DLG2, DLG3, DLG4 and AIP1. Interacts with the PDZ domain of
CC       SHANK1, SHANK2 and SHANK3. Found in a complex with DLG4 and
CC       SHANK1, SHANK2 or SHANK3. Found in a complex with DLG4 and BEGAIN.
CC       Interacts with DYL2 and LRFN1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       (By similarity). Cell junction, synapse, postsynaptic cell
CC       membrane, postsynaptic density (By similarity). Cell junction,
CC       synapse (By similarity). Note=Found in postsynaptic density of
CC       neuronal cells (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1; Synonyms=SAPAP1;
CC         IsoId=Q9D415-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D415-2; Sequence=VSP_015409;
CC         Note=No experimental confirmation available;
CC       Name=3; Synonyms=GKAP1a;
CC         IsoId=Q9D415-3; Sequence=VSP_015412;
CC       Name=4; Synonyms=GKAP1b;
CC         IsoId=Q9D415-4; Sequence=VSP_015409, VSP_015413, VSP_015414;
CC       Name=5;
CC         IsoId=Q9D415-5; Sequence=VSP_015410, VSP_015411;
CC         Note=No experimental confirmation available;
CC       Name=6;
CC         IsoId=Q9D415-6; Sequence=VSP_015408;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highest levels in the neocortex, part of the
CC       hippocampus, the granule cell layer of the cerebellum, the
CC       glomerular layer of the olfactory bulb, the inner plexiform layer
CC       of the retina, the ventral and dorsal horn of the spinal chord,
CC       the neuromuscular junction and the submandibular ganglion.
CC   -!- SIMILARITY: Belongs to the SAPAP family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90519.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY243846; AAP70755.2; -; mRNA.
DR   EMBL; AK031410; BAC27391.1; -; mRNA.
DR   EMBL; AK033901; BAC28508.1; -; mRNA.
DR   EMBL; AK034182; BAC28619.1; -; mRNA.
DR   EMBL; AK220515; BAD90519.1; ALT_INIT; mRNA.
DR   EMBL; BC062120; AAH62120.1; -; mRNA.
DR   EMBL; BC094369; AAH94369.1; -; mRNA.
DR   IPI; IPI00136402; -.
DR   IPI; IPI00473783; -.
DR   IPI; IPI00648461; -.
DR   IPI; IPI00648858; -.
DR   IPI; IPI00649710; -.
DR   IPI; IPI00650032; -.
DR   RefSeq; NP_081988.3; NM_027712.3.
DR   RefSeq; NP_808307.2; NM_177639.6.
DR   UniGene; Mm.311840; -.
DR   UniGene; Mm.367369; -.
DR   ProteinModelPortal; Q9D415; -.
DR   MINT; MINT-136157; -.
DR   STRING; Q9D415; -.
DR   PhosphoSite; Q9D415; -.
DR   PRIDE; Q9D415; -.
DR   Ensembl; ENSMUST00000003366; ENSMUSP00000003366; ENSMUSG00000003279.
DR   Ensembl; ENSMUST00000060072; ENSMUSP00000052858; ENSMUSG00000003279.
DR   GeneID; 224997; -.
DR   KEGG; mmu:224997; -.
DR   UCSC; uc008dkz.1; mouse.
DR   UCSC; uc008dla.1; mouse.
DR   UCSC; uc008dlb.1; mouse.
DR   UCSC; uc008dlc.1; mouse.
DR   UCSC; uc008dle.1; mouse.
DR   UCSC; uc008dlg.1; mouse.
DR   CTD; 224997; -.
DR   MGI; MGI:1346065; Dlgap1.
DR   GeneTree; ENSGT00550000074473; -.
DR   HOVERGEN; HBG018957; -.
DR   InParanoid; Q9D415; -.
DR   OMA; CANLPVN; -.
DR   PhylomeDB; Q9D415; -.
DR   NextBio; 377488; -.
DR   ArrayExpress; Q9D415; -.
DR   Bgee; Q9D415; -.
DR   Genevestigator; Q9D415; -.
DR   GermOnline; ENSMUSG00000003279; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007268; P:synaptic transmission; TAS:MGI.
DR   InterPro; IPR005026; GKAP.
DR   Pfam; PF03359; GKAP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Membrane;
KW   Phosphoprotein; Postsynaptic cell membrane; Synapse.
FT   CHAIN         1    992       Disks large-associated protein 1.
FT                                /FTId=PRO_0000174289.
FT   REGION      665    676       Interaction with DYL2 (By similarity).
FT   REGION      687    698       Interaction with DYL2 (By similarity).
FT   MOTIF       990    992       PDZ-binding (By similarity).
FT   MOD_RES     123    123       Phosphotyrosine.
FT   MOD_RES     134    134       Phosphoserine.
FT   MOD_RES     352    352       Phosphoserine.
FT   MOD_RES     362    362       Phosphoserine.
FT   MOD_RES     389    389       Phosphoserine.
FT   MOD_RES     412    412       Phosphoserine.
FT   MOD_RES     421    421       Phosphoserine.
FT   MOD_RES     436    436       Phosphothreonine.
FT   MOD_RES     437    437       Phosphoserine.
FT   MOD_RES     446    446       Phosphoserine.
FT   MOD_RES     499    499       Phosphoserine.
FT   MOD_RES     509    509       Phosphoserine.
FT   MOD_RES     516    516       Phosphoserine.
FT   MOD_RES     947    947       Phosphoserine.
FT   VAR_SEQ     398    992       Missing (in isoform 6).
FT                                /FTId=VSP_015408.
FT   VAR_SEQ     537    546       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_015409.
FT   VAR_SEQ     538    538       V -> E (in isoform 5).
FT                                /FTId=VSP_015410.
FT   VAR_SEQ     539    992       Missing (in isoform 5).
FT                                /FTId=VSP_015411.
FT   VAR_SEQ     547    574       Missing (in isoform 3).
FT                                /FTId=VSP_015412.
FT   VAR_SEQ     924    944       ERRAPPPVPKKPAKGPAPLIR -> VEQCRFCMVHLKPCTN
FT                                AGQSK (in isoform 4).
FT                                /FTId=VSP_015413.
FT   VAR_SEQ     945    992       Missing (in isoform 4).
FT                                /FTId=VSP_015414.
FT   CONFLICT    383    383       L -> P (in Ref. 3; BAD90519).
FT   CONFLICT    397    397       K -> R (in Ref. 1; AAP70755).
FT   CONFLICT    431    431       P -> H (in Ref. 2; BAC27391).
FT   CONFLICT    752    752       S -> F (in Ref. 2; BAC28619).
SQ   SEQUENCE   992 AA;  110374 MW;  9962C8B56A33EE13 CRC64;
     MKGLSGSRSH HHGITCEAAC DSLSHHSDHK PYLLSPVDHH PADHPYYTQR NSFQAECVGP
     FSDPLASSTF PRRHYTSQQE LKDESALVPR TLATKANRLP TNLLDQFERQ LPLSRDGYHT
     LQYKRTAVEH RSDSPGRIRH LVHSVQKLFT KSHSLEGPSK GSVNGGKASP DESQTLRYGK
     RSKSKERRSE SKARSNASNA SPTSPSWWSS DDNLDGDMCL YHTPSGVMTM GRCPDRSASQ
     YFMEAYNTIS EQAVKASRSN NDIKCSTCAN LPVTLDAPLL KKSAWSSTLT VSRAREVYQK
     ASVNMDQAMV KSEACQQERS CQYLQVPQDE WSGYTPRGKD DEIPCRRMRS GSYIKAMGDE
     DSGDSDTSPK PSPKVAARRE SYLKATQPSL TELTTLKISN EHSPKLQIRS HSYLRAVSEV
     SINRSLDSLD PAGLLTSPKF RSRNESYMRA MSTISQVSEM EVNGQFESVC ESVFSELESQ
     AVEALDLPLP GCFRMRSHSY VRAIEKGCSQ DDECVSLRSS SPPRTTTTVR TIQSSTGVIK
     LSSAVEVSSC ITTYKKTPPP VPPRTTTKPF ISITAQSSTE SAQDAYMDGQ GQRGDMISQS
     GLSNSTESLD SMKALTAAIE AANAQIHGPA SQHMGSNAAA VTTTTTIATV TTEDRKKDFK
     KNRCLSIGIQ VDDAEEPEKM AESKTSNKFQ SVGVQVEEEK CFRRFTRSNS VTTAVQADLD
     FHDNLENSLE SIEDNSCPGP MARQFSRDAS TSTVSIQGSG NHYHACAADD DFDTDFDPSI
     LPPPDPWIDS ITEDPLEAVQ RSVCHRDGHW FLKLLQAERD RMEGWCKLME REERENNLPE
     DILGKIRTAV GSAQLLMAQK FYQFRELCEE NLNPNAHPRP TSQDLAGFWD MLQLSIENIS
     MKFDELHQLK ANNWKQMDPL DKKERRAPPP VPKKPAKGPA PLIRERSLES SQRQEARKRL
     MAAKRAASVR QNSATESAES IEIYIPEAQT RL
//
ID   CLVS1_MOUSE             Reviewed;         354 AA.
AC   Q9D4C9; Q3UWV3; Q497H3; Q8BJE8; Q8BXX0;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Clavesin-1;
DE   AltName: Full=Retinaldehyde-binding protein 1-like 1;
GN   Name=Clvs1; Synonyms=Rlbp1l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Egg, Eye, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Required for normal morphology of late endosomes and/or
CC       lysosomes in neurons. Binds phosphatidylinositol 3,5-bisphosphate
CC       (PtdIns(3,5)P2) (By similarity).
CC   -!- SUBUNIT: Forms a complex with clathrin heavy chain and gamma-
CC       adaptin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC       membrane; Peripheral membrane protein (By similarity). Early
CC       endosome membrane; Peripheral membrane protein (By similarity).
CC       Cytoplasmic vesicle, clathrin-coated vesicle (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9D4C9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D4C9-2; Sequence=VSP_027331;
CC       Name=3;
CC         IsoId=Q9D4C9-3; Sequence=VSP_027330;
CC   -!- DOMAIN: The CRAL-TRIO domain is required for targeting to the
CC       membrane and for binding PtdIns(3,5)P2 (By similarity).
CC   -!- MISCELLANEOUS: Binding to PtdIns(3,5)P2 is not required for
CC       localization (By similarity).
CC   -!- SIMILARITY: Contains 1 CRAL-TRIO domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE22811.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK016622; BAB30342.1; -; mRNA.
DR   EMBL; AK043072; BAC31451.1; -; mRNA.
DR   EMBL; AK084350; BAC39166.1; -; mRNA.
DR   EMBL; AK136083; BAE22811.1; ALT_INIT; mRNA.
DR   EMBL; AL671970; CAM15541.1; -; Genomic_DNA.
DR   EMBL; AL844180; CAM15541.1; JOINED; Genomic_DNA.
DR   EMBL; AL844180; CAM23455.1; -; Genomic_DNA.
DR   EMBL; AL671970; CAM23455.1; JOINED; Genomic_DNA.
DR   EMBL; BC062923; AAH62923.1; -; mRNA.
DR   EMBL; BC100556; AAI00557.1; -; mRNA.
DR   IPI; IPI00137094; -.
DR   IPI; IPI00857245; -.
DR   IPI; IPI00857655; -.
DR   RefSeq; NP_083216.1; NM_028940.2.
DR   UniGene; Mm.477282; -.
DR   HSSP; P49638; 1R5L.
DR   ProteinModelPortal; Q9D4C9; -.
DR   SMR; Q9D4C9; 29-287.
DR   PhosphoSite; Q9D4C9; -.
DR   PRIDE; Q9D4C9; -.
DR   Ensembl; ENSMUST00000038841; ENSMUSP00000035649; ENSMUSG00000041216.
DR   Ensembl; ENSMUST00000108348; ENSMUSP00000103985; ENSMUSG00000041216.
DR   GeneID; 74438; -.
DR   KEGG; mmu:74438; -.
DR   UCSC; uc008rye.1; mouse.
DR   CTD; 74438; -.
DR   MGI; MGI:1921688; Clvs1.
DR   eggNOG; roNOG09434; -.
DR   GeneTree; ENSGT00550000074253; -.
DR   HOGENOM; HBG716080; -.
DR   HOVERGEN; HBG101105; -.
DR   InParanoid; Q9D4C9; -.
DR   OMA; WKGDLAK; -.
DR   OrthoDB; EOG4RXZ0J; -.
DR   PhylomeDB; Q9D4C9; -.
DR   NextBio; 340757; -.
DR   ArrayExpress; Q9D4C9; -.
DR   Bgee; Q9D4C9; -.
DR   CleanEx; MM_RLBP1L1; -.
DR   Genevestigator; Q9D4C9; -.
DR   GO; GO:0030136; C:clathrin-coated vesicle; ISS:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR   GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISS:UniProtKB.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   GO; GO:0007040; P:lysosome organization; ISS:UniProtKB.
DR   InterPro; IPR001071; CRAL-bd_toc_tran.
DR   InterPro; IPR001251; CRAL-bd_TRIO_C.
DR   InterPro; IPR008273; CRAL-bd_TRIO_N.
DR   InterPro; IPR011074; Sec14p-like_N.
DR   Gene3D; G3DSA:3.40.525.10; CRAL_bd_TRIO_C; 1.
DR   Pfam; PF00650; CRAL_TRIO; 1.
DR   Pfam; PF03765; CRAL_TRIO_N; 1.
DR   PRINTS; PR00180; CRETINALDHBP.
DR   SMART; SM00516; SEC14; 1.
DR   SUPFAM; SSF52087; CRAL_TRIO_C; 1.
DR   SUPFAM; SSF46938; Sec14p_like_N; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasmic vesicle; Endosome; Golgi apparatus;
KW   Lipid-binding; Membrane.
FT   CHAIN         1    354       Clavesin-1.
FT                                /FTId=PRO_0000297656.
FT   DOMAIN      118    279       CRAL-TRIO.
FT   VAR_SEQ       1    279       Missing (in isoform 3).
FT                                /FTId=VSP_027330.
FT   VAR_SEQ     153    354       Missing (in isoform 2).
FT                                /FTId=VSP_027331.
FT   CONFLICT    307    307       H -> Q (in Ref. 1; BAE22811).
SQ   SEQUENCE   354 AA;  40613 MW;  894F8BB1EE4E8AEF CRC64;
     MGPVSVLPSP QSLSTWEGDL AKMTHLQAGL SPDTIEKARL ELNENPDILH QDIQQVRDMI
     ITRPDIGFLR TDDAFILRFL RARKFHQADA FRLLAQYFQY RQLNLDMFKN FKADDPGIKR
     ALIDGFPGVL ENRDHYGRKI LLLFAANWDQ SRNSFTDILR AILLSLEVLI EDPELQINGF
     ILIIDWSNFS FKQASKLTPS ILKLAIEGLQ DSFPARFGGV HFVNQPWYIH ALYTLIKPFL
     KDKTRKRIFL HGNNLNSLHQ LIHPEFLPSE FGGTLPPYDM GTWARTLLGP DYSDENDYTH
     TSYNAMHVKH TCSNLERECS PKPMKRSQSV VEAGTLKHEE KGENENTQPL LALD
//
ID   PPAC2_MOUSE             Reviewed;         292 AA.
AC   Q9D4F2;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Presqualene diphosphate phosphatase;
DE            EC=3.1.3.-;
DE   AltName: Full=Phosphatidic acid phosphatase type 2 domain-containing protein 2;
GN   Name=Ppapdc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Phosphatase that dephosphorylates presqualene
CC       diphosphate (PSDP) into presqualene monophosphate (PSMP),
CC       suggesting that it may be indirectly involved in innate immunity.
CC       PSDP is a bioactive lipid that rapidly remodels to presqualene
CC       monophosphate PSMP upon cell activation. Displays diphosphate
CC       phosphatase activity with a substrate preference for PSDP > FDP >
CC       phosphatidic acid (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the PA-phosphatase related phosphoesterase
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK016572; BAB30313.1; -; mRNA.
DR   EMBL; BC052412; AAH52412.1; -; mRNA.
DR   IPI; IPI00137172; -.
DR   RefSeq; NP_083198.1; NM_028922.3.
DR   UniGene; Mm.441887; -.
DR   ProteinModelPortal; Q9D4F2; -.
DR   SMR; Q9D4F2; 175-270.
DR   PhosphoSite; Q9D4F2; -.
DR   PRIDE; Q9D4F2; -.
DR   Ensembl; ENSMUST00000045674; ENSMUSP00000047776; ENSMUSG00000040105.
DR   GeneID; 74411; -.
DR   KEGG; mmu:74411; -.
DR   UCSC; uc008hcr.1; mouse.
DR   CTD; 74411; -.
DR   MGI; MGI:1921661; Ppapdc2.
DR   eggNOG; maNOG17524; -.
DR   GeneTree; ENSGT00390000012789; -.
DR   HOGENOM; HBG713923; -.
DR   HOVERGEN; HBG054746; -.
DR   InParanoid; Q9D4F2; -.
DR   OMA; KLGVCAG; -.
DR   OrthoDB; EOG4P2Q35; -.
DR   PhylomeDB; Q9D4F2; -.
DR   NextBio; 340685; -.
DR   ArrayExpress; Q9D4F2; -.
DR   Bgee; Q9D4F2; -.
DR   Genevestigator; Q9D4F2; -.
DR   GermOnline; ENSMUSG00000040105; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR016118; P_Acid_Pase/Cl_peroxidase_N.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   Gene3D; G3DSA:1.20.144.10; P_Acid_Pase/Cl_peroxidase_N; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; AcPase_VanPerase; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    292       Presqualene diphosphate phosphatase.
FT                                /FTId=PRO_0000239397.
FT   TRANSMEM    132    152       Helical; (Potential).
FT   TRANSMEM    162    182       Helical; (Potential).
FT   TRANSMEM    226    246       Helical; (Potential).
FT   TRANSMEM    258    278       Helical; (Potential).
FT   MOD_RES      58     58       Phosphoserine (By similarity).
FT   MOD_RES      60     60       Phosphoserine (By similarity).
FT   MOD_RES      67     67       Phosphoserine.
SQ   SEQUENCE   292 AA;  31744 MW;  8B28C6DCA0BE7F17 CRC64;
     MPSPRRTIEG RPLGSSGGSS VPGSPAHGGG SGGGRFEFQS LLNCRAGADP ACARLRASDS
     PVHRRGSFPL AASGPAQAAP APPPEDARMN LNPSFLGIAL RSLLAIDLWL SKKLGVCAGE
     SSAWGSVRPL MKLLEISGHG IPWLLGTLYC LLRSDSWAGR EVLMNLLFAL LLDLLLVAVI
     KGLVRRRRPA HNQKDMFFTL SVDRYSFPSG HATRAALVSR FILNHLVLAI PLRVLVVLWA
     FVLGLSRVML GRHNVTDVAF GFFLGYMQYS IVDYCWLSPH NVPVLFVLWN QQ
//
ID   EXOC2_MOUSE             Reviewed;         924 AA.
AC   Q9D4H1;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Exocyst complex component 2;
DE   AltName: Full=Exocyst complex component Sec5;
GN   Name=Exoc2; Synonyms=Sec5, Sec5l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   STRUCTURE BY NMR OF RALA-BINDING DOMAIN.
RX   MEDLINE=22616004; PubMed=12624092; DOI=10.1074/jbc.M300155200;
RA   Mott H.R., Nietlispach D., Hopkins L.J., Mirey G., Camonis J.H.,
RA   Owen D.;
RT   "Structure of the GTPase-binding domain of Sec5 and elucidation of its
RT   Ral binding site.";
RL   J. Biol. Chem. 278:17053-17059(2003).
CC   -!- FUNCTION: Component of the exocyst complex involved in the docking
CC       of exocystic vesicles with fusion sites on the plasma membrane (By
CC       similarity).
CC   -!- SUBUNIT: The exocyst complex is composed of EXOC1, EXOC2, EXOC3,
CC       EXOC4, EXOC5, EXOC6, EXOC7 and EXOC8. Interacts with RALA and
CC       GNEFR/DELGEF. Interaction with GNEFR occurs only in the presence
CC       of magnesium or manganese and is stimulated by dCTP or GTP.
CC   -!- DOMAIN: Interacts with RALA through the TIG domain.
CC   -!- SIMILARITY: Belongs to the SEC5 family.
CC   -!- SIMILARITY: Contains 1 IPT/TIG domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK016532; BAB30290.1; -; mRNA.
DR   EMBL; AK050068; BAC34056.1; -; mRNA.
DR   EMBL; BC048154; AAH48154.1; -; mRNA.
DR   EMBL; BC049102; AAH49102.1; -; mRNA.
DR   IPI; IPI00655041; -.
DR   RefSeq; NP_079864.1; NM_025588.2.
DR   UniGene; Mm.293510; -.
DR   PDB; 1HK6; NMR; -; A=5-97.
DR   PDBsum; 1HK6; -.
DR   ProteinModelPortal; Q9D4H1; -.
DR   SMR; Q9D4H1; 5-97.
DR   STRING; Q9D4H1; -.
DR   PhosphoSite; Q9D4H1; -.
DR   PRIDE; Q9D4H1; -.
DR   Ensembl; ENSMUST00000021785; ENSMUSP00000021785; ENSMUSG00000021357.
DR   Ensembl; ENSMUST00000102946; ENSMUSP00000100010; ENSMUSG00000021357.
DR   GeneID; 66482; -.
DR   KEGG; mmu:66482; -.
DR   UCSC; uc007pzc.1; mouse.
DR   CTD; 66482; -.
DR   MGI; MGI:1913732; Exoc2.
DR   GeneTree; ENSGT00390000010872; -.
DR   HOGENOM; HBG314434; -.
DR   HOVERGEN; HBG028469; -.
DR   InParanoid; Q9D4H1; -.
DR   OMA; YYAEVET; -.
DR   OrthoDB; EOG4XWFX4; -.
DR   NextBio; 321816; -.
DR   ArrayExpress; Q9D4H1; -.
DR   Bgee; Q9D4H1; -.
DR   CleanEx; MM_EXOC2; -.
DR   Genevestigator; Q9D4H1; -.
DR   GermOnline; ENSMUSG00000021357; Mus musculus.
DR   GO; GO:0000145; C:exocyst; TAS:MGI.
DR   GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR   GO; GO:0017160; F:Ral GTPase binding; IDA:MGI.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0045921; P:positive regulation of exocytosis; TAS:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002909; IPT_TIG_rcpt.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF01833; TIG; 1.
DR   SUPFAM; SSF81296; Ig_E-set; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Coiled coil; Exocytosis; Phosphoprotein;
KW   Protein transport; Transport.
FT   CHAIN         1    924       Exocyst complex component 2.
FT                                /FTId=PRO_0000118919.
FT   DOMAIN        8     93       IPT/TIG.
FT   COILED      240    260       Potential.
FT   MOD_RES     432    432       Phosphoserine (By similarity).
FT   MOD_RES     435    435       Phosphoserine.
FT   MOD_RES     454    454       N6-acetyllysine (By similarity).
FT   STRAND        9     14
FT   STRAND       22     29
FT   TURN         35     37
FT   STRAND       41     43
FT   TURN         49     51
FT   STRAND       56     58
FT   STRAND       60     63
FT   STRAND       69     71
FT   STRAND       73     76
FT   STRAND       79     81
FT   STRAND       85     87
SQ   SEQUENCE   924 AA;  103959 MW;  457BAD92EAA3040B CRC64;
     MSRSRQPPLV TGISPNEGIP WTKVTIRGEN LGTGPTDLIG LTICGHNCLL TAEWMSASKI
     VCRVGQAKND KGDIIVTTKS GGKGTSTVSF KLLKPEKIGI LDQSAVWVDE MNYYDMRTDR
     NKGIPPLSLR PANPLGIEIE KCKLPQKNLE VLFHGMSADF TSENFSAAWY LIENHSTTSF
     EQLKMAVTNL KRQANKKSEG SLAYVKGGLS TFFEAQDALS AIHQKLEADG TEKVEGSMTQ
     KLENVLNRAS NTADTLFQEV LGRKDKADST RNALNVLQRF KFLFNLPLNI KRNIQKGDYD
     VVINDYEKAK SLFGKTEVQV FKKYYAEVEA GIEDLRELLL KKLLETPSTL HDQKRYIRYL
     SDLHAPGDPA WQCIGAQHKW TLKLMQDCKE GHMKSLKGHP GPHSPMLDLD NDVRPSVLGH
     LSQTASLKRG SSFQSGRDDT WRYKTPHRVA FVEKLTKLVL SQLPNFWKLW ISYVNGSLFS
     ETAEKSGQSE RSKNVRQRQN DFKKMIQEVM HSLVKLIRGA LLPLSLREGD GRQYGGWEVQ
     AELSGQWLAH VIQTIRLTYE SLTALEIPND MLQIIQDLIL DLRIRCIMVT LQHTAEEIKR
     LAEKEDWVVD NEGLTSLPCQ FEQSIVHSLQ SLKGVVDCKP GEASVFQQPK TQEEVCQLCI
     NIMQVFIYCL EQLSTKPDAD IDTTHLSVDV SSPDLFGSIH EDFSLTSEQR LLIVLSNCCY
     LERHTFLNIA EHFEKHNFQG IEKITQVSMA SLKELDQRLF ENYIELKADP IVGSLEPGIY
     AGYFDWKDCL PPAGVRNYLK EALVNIIAVH AEVFTISKEL VPRVLARVVE AVSEELSRLM
     QCVSSFSRNG ALQARLEICA LRDTVAIYLT SESRSSFKQA LEALPQLASG ADKKSLEELL
     NKFKSSMHLQ LTCFQAASPA VMKT
//
ID   AMOL1_MOUSE             Reviewed;         882 AA.
AC   Q9D4H4; Q571F1;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Angiomotin-like protein 1;
GN   Name=Amotl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-882.
RC   TISSUE=Pancreatic islet;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Seino S., Nishimura M.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645; SER-718 AND
RP   SER-730, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SIMILARITY: Belongs to the angiomotin family.
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DR   EMBL; AK016526; BAB30287.1; -; mRNA.
DR   EMBL; AK220238; BAD90163.1; -; mRNA.
DR   IPI; IPI00970062; -.
DR   UniGene; Mm.159552; -.
DR   ProteinModelPortal; Q9D4H4; -.
DR   STRING; Q9D4H4; -.
DR   PhosphoSite; Q9D4H4; -.
DR   PRIDE; Q9D4H4; -.
DR   Ensembl; ENSMUST00000013220; ENSMUSP00000013220; ENSMUSG00000013076.
DR   UCSC; uc009oep.1; mouse.
DR   MGI; MGI:1922973; Amotl1.
DR   eggNOG; roNOG12989; -.
DR   GeneTree; ENSGT00530000063846; -.
DR   HOVERGEN; HBG066485; -.
DR   InParanoid; Q9D4H4; -.
DR   OrthoDB; EOG43R3M0; -.
DR   ArrayExpress; Q9D4H4; -.
DR   Bgee; Q9D4H4; -.
DR   CleanEx; MM_AMOTL1; -.
DR   Genevestigator; Q9D4H4; -.
DR   GermOnline; ENSMUSG00000013076; Mus musculus.
DR   GO; GO:0005923; C:tight junction; IDA:MGI.
DR   InterPro; IPR009114; Angiomotin.
DR   PANTHER; PTHR14826; Angiomotin; 1.
DR   PRINTS; PR01807; ANGIOMOTIN.
PE   1: Evidence at protein level;
KW   Coiled coil; Phosphoprotein.
FT   CHAIN         1    882       Angiomotin-like protein 1.
FT                                /FTId=PRO_0000190671.
FT   COILED      185    205       Potential.
FT   COILED      363    559       Potential.
FT   COILED      590    619       Potential.
FT   COILED      662    687       Potential.
FT   MOTIF       879    882       PDZ-binding.
FT   MOD_RES     221    221       Phosphoserine (By similarity).
FT   MOD_RES     350    350       Phosphoserine (By similarity).
FT   MOD_RES     645    645       Phosphoserine.
FT   MOD_RES     718    718       Phosphoserine.
FT   MOD_RES     728    728       Phosphothreonine (By similarity).
FT   MOD_RES     730    730       Phosphoserine.
FT   MOD_RES     734    734       Phosphoserine (By similarity).
FT   CONFLICT    135    135       Missing (in Ref. 2; BAD90163).
SQ   SEQUENCE   882 AA;  98424 MW;  88AAFE83FFA56046 CRC64;
     MRGSEDVASG RVLQRLIQEQ LRYGTPTENM NLLAIQHQAT GSAGPAHATT NFSSTETLTQ
     EDPQMVYQSA RQEPQGQEHQ GDNTVMEKQV RSTQPQQNNE ELPTYEEAKA QSQFFRGQQQ
     QQQQQQQQQQ QQQQQGQGPL SHTYYMAGGT SQKSRTEGRP TVNRANSGQA HKDEALKELK
     QGHVRSLSER IMQLSLERNG AKQHLPSSGN GKSFKAGGEP SPAQPVCKAL DPRGPPPEYP
     FKTKPMKSPV SKNQDHGLYY NDQHPGVLHE MVKPYPAPQP ARTEVAVLRY QPPPEYGVTS
     RPCQLPFPST VQQHSPMSSQ TSSIGGTLHS VSLPLPLPIS LAASQPLPAS PNQQLGPDAF
     AIVERAQQMV EILTEENRVL HQELQGCYDN ADKLHKFEKE LQSISEAYES LVKSTTKRES
     LDKAMRTKLE GEIRRLHDFN RDLRDRLETA NRQLSSREYD GHEDKAAESH YVSQNKEFLK
     EKEKLEMELA AVRTASEDHR RHIEILDQAL SNAQARVIKL EEELREKQAY VEKVEKLQQA
     LTQLQSACEK RGQMERRLRT WLERELDALR TQQKHGTGPP VSLPECNAPA LMELVREKEE
     RILALEADMT KWEQKYLEES TIRHFAMSAA AAATAERDTT ISNHSRNGSY GESSLEAHIW
     PEEEEVVQAN RRCQDMEYTI KNLHAKIIEK DAMIKVLQQR SRKDAGKTDS ASLRPARSVP
     SIAAATGTHS RQTSLTSSQL TEEKKEEKTT WKGSIGFLLG KEHQGQASAP LLPTTPASAL
     SLPASTTSAS STHAKTGSKD SSTQTDKSTE LFWPSMASLP SRGRLSTAPS NSPILKHPAA
     KGAVEKQENS PGHGKASEHR GRVSNLLHKP EFPDGEMMEV LI
//
ID   PHF14_MOUSE             Reviewed;         881 AA.
AC   Q9D4H9; Q810Z6; Q8C284; Q8CGF8; Q9D1Q8;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=PHD finger protein 14;
GN   Name=Phf14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=FVB/N;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 513-881.
RC   STRAIN=129S6/SvEvTac;
RA   Brathwaite M.E., Waeltz P., Qian Y., Dudekula D., Schlessinger D.,
RA   Nagaraja R.;
RT   "Genomic sequence analysis in the mouse T-complex region.";
RL   Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-280 AND SER-283, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-280; SER-283 AND
RP   SER-287, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291 AND SER-295, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9D4H9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D4H9-2; Sequence=VSP_010349;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q9D4H9-3; Sequence=VSP_010348;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Contains 2 PHD-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB22644.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK003209; BAB22644.1; ALT_INIT; mRNA.
DR   EMBL; AK016517; BAB30282.1; -; mRNA.
DR   EMBL; AK089073; BAC40735.1; -; mRNA.
DR   EMBL; BC040236; AAH40236.1; -; mRNA.
DR   EMBL; AY162410; AAO17166.1; -; Genomic_DNA.
DR   IPI; IPI00137250; -.
DR   IPI; IPI00415328; -.
DR   IPI; IPI00415329; -.
DR   RefSeq; NP_001161854.1; NM_001168382.1.
DR   RefSeq; NP_083680.2; NM_029404.3.
DR   UniGene; Mm.212411; -.
DR   ProteinModelPortal; Q9D4H9; -.
DR   SMR; Q9D4H9; 312-374, 681-773.
DR   PhosphoSite; Q9D4H9; -.
DR   PRIDE; Q9D4H9; -.
DR   Ensembl; ENSMUST00000115510; ENSMUSP00000111172; ENSMUSG00000029629.
DR   Ensembl; ENSMUST00000115511; ENSMUSP00000111173; ENSMUSG00000029629.
DR   GeneID; 75725; -.
DR   KEGG; mmu:75725; -.
DR   UCSC; uc009aye.1; mouse.
DR   UCSC; uc009ayf.1; mouse.
DR   CTD; 75725; -.
DR   MGI; MGI:1923539; Phf14.
DR   eggNOG; roNOG06833; -.
DR   GeneTree; ENSGT00600000084089; -.
DR   HOVERGEN; HBG053584; -.
DR   OMA; EKQLIKM; -.
DR   OrthoDB; EOG437RD8; -.
DR   NextBio; 343786; -.
DR   ArrayExpress; Q9D4H9; -.
DR   Bgee; Q9D4H9; -.
DR   CleanEx; MM_PHF14; -.
DR   Genevestigator; Q9D4H9; -.
DR   GermOnline; ENSMUSG00000029629; Mus musculus.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 2.
DR   Pfam; PF00628; PHD; 2.
DR   SMART; SM00249; PHD; 3.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 2.
DR   PROSITE; PS01359; ZF_PHD_1; 2.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Metal-binding; Phosphoprotein; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    881       PHD finger protein 14.
FT                                /FTId=PRO_0000059307.
FT   ZN_FING     312    373       PHD-type 1.
FT   ZN_FING     718    772       PHD-type 2.
FT   COMPBIAS     62    129       Glu-rich.
FT   MOD_RES     201    201       Phosphoserine (By similarity).
FT   MOD_RES     273    273       Phosphoserine (By similarity).
FT   MOD_RES     280    280       Phosphothreonine.
FT   MOD_RES     283    283       Phosphoserine.
FT   MOD_RES     287    287       Phosphoserine.
FT   MOD_RES     291    291       Phosphoserine.
FT   MOD_RES     295    295       Phosphoserine.
FT   MOD_RES     523    523       Phosphoserine (By similarity).
FT   MOD_RES     546    546       Phosphoserine (By similarity).
FT   MOD_RES     828    828       Phosphoserine (By similarity).
FT   VAR_SEQ     879    881       NLT -> CDECRLCYHFGCLDPPLKKSPKQTGYGWICQECD
FT                                SSSSKEDENEAEKKNASQELSMEQKTPKK (in isoform
FT                                2).
FT                                /FTId=VSP_010349.
FT   VAR_SEQ     879    881       Missing (in isoform 3).
FT                                /FTId=VSP_010348.
FT   CONFLICT    133    133       V -> I (in Ref. 2; AAH40236).
SQ   SEQUENCE   881 AA;  99105 MW;  21E0EA172F96B20D CRC64;
     MDRSSKRRQV KPLAASLLEA LDYDSSDDSD FKVGDASDSE GSGNGSEDPS KDSGEGSCSD
     SEENILEEEL NEDIQVKEEQ LKNSTEEIMP SDKQLIKMEK KEEEENGERP RKKKEKEKEK
     EKEREKDKEK ATVSDSAAAS AAGTTPATSP PAVTSPSVPT TTTTTTEEQV SEPKKWNLRR
     NRPLLDFVSM EELNAMDDYD SEDDNDWRPT VVKRKGRSAS QKEGSDGDNE DDDDEGSGSE
     EDENDEGNDE DHSSPASEAG GKKKRSKVLS RNSADDEELT NDSLTLSQSK SNEDSLILEK
     SQNWSSQKMD HILICCVCLG DNSEDADEII QCDNCGITVH EGCYGVDGES DSIMSSASEN
     STEPWFCDAC KCGVSPSCEL CPNQDGIFKE TDAGRWVHIV CALYVPGVAF GDIDKLRPVT
     LTEMNYSKYG AKECSFCEDP RFARTGVCIS CDAGMCRAYF HVTCAQKEGL LSEAAAEEDI
     ADPFFAYCKQ HADRLDRKWK RKNYLALQSY CKMSLQEREK QLSPEAQARI NARLQQYRAK
     AELARSTRPQ AWVPREKLPR PLTSSASAIR KLMRKAELMG ISTDIFPVDN SDTSSSVDGR
     RKHKQPALTA DFVNYYFERN MRMIQIQENM AEQKNIKDKL ENEQEKLHVE YNKLCESLEE
     LQNLNGKLRS EGQGIWALLG RITGQKLNVP AILRAPKERK PSKKEGGTQK TSALPTVLYS
     CGICKKNHDQ HLLLLCDTCK LHYHLGCLDP PLTRMPRKTK NSYWQCSECD QAGSSDMEAE
     MAMETLPDGT KRSRRQIKEP VKFVPQDVPP EPKKIPIRNT RTRGRKRSFV PEEEKHEERV
     PRERRQRQSV LQKKPKAEDL RTECSTCKGT GDNENLVRNL T
//
ID   PHF6_MOUSE              Reviewed;         364 AA.
AC   Q9D4J7; Q80T86; Q8BYT8; Q8C1B5;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=PHD finger protein 6;
GN   Name=Phf6; Synonyms=Kiaa1823;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Skin, Testis, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=22345003; PubMed=12415272; DOI=10.1038/ng1040;
RA   Lower K.M., Turner G., Kerr B.A., Mathews K.D., Shaw M.A.,
RA   Gedeon A.K., Schelley S., Hoyme H.E., White S.M., Delatycki M.B.,
RA   Lampe A.K., Clayton-Smith J., Stewart H., van Ravenswaay C.M.A.,
RA   de Vries B.B.A., Cox B., Grompe M., Ross S., Thomas P., Mulley J.C.,
RA   Gecz J.;
RT   "Mutations in PHF6 are associated with Boerjeson-Forssman-Lehmann
RT   syndrome.";
RL   Nat. Genet. 32:661-665(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-357, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
CC   -!- FUNCTION: May play a role in transcriptional regulation (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Nucleus, nucleolus
CC       (By similarity). Note=Nuclear, it particularly localizes to the
CC       nucleolus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9D4J7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D4J7-2; Sequence=VSP_009375;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: At 12.5 dpc it is highly expressed in the
CC       embryonic central nervous system and at lower levels in other
CC       tissues. Very low levels present throughout the adult brain.
CC   -!- DEVELOPMENTAL STAGE: Expression is high in the embryonic and early
CC       postnatal stages.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Contains 2 PHD-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC29968.1; Type=Frameshift; Positions=284;
CC       Sequence=BAC65842.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK016480; BAB30260.1; -; mRNA.
DR   EMBL; AK028498; BAC25980.1; -; mRNA.
DR   EMBL; AK038320; BAC29968.1; ALT_FRAME; mRNA.
DR   EMBL; AK122560; BAC65842.1; ALT_INIT; mRNA.
DR   EMBL; BC043127; AAH43127.1; -; mRNA.
DR   EMBL; BC055330; AAH55330.1; -; mRNA.
DR   EMBL; BC057374; AAH57374.1; -; mRNA.
DR   IPI; IPI00137302; -.
DR   IPI; IPI00399702; -.
DR   RefSeq; NP_081918.1; NM_027642.1.
DR   UniGene; Mm.26870; -.
DR   ProteinModelPortal; Q9D4J7; -.
DR   STRING; Q9D4J7; -.
DR   PhosphoSite; Q9D4J7; -.
DR   PRIDE; Q9D4J7; -.
DR   Ensembl; ENSMUST00000078944; ENSMUSP00000077971; ENSMUSG00000025626.
DR   GeneID; 70998; -.
DR   KEGG; mmu:70998; -.
DR   UCSC; uc009teo.1; mouse.
DR   UCSC; uc009teq.1; mouse.
DR   CTD; 70998; -.
DR   MGI; MGI:1918248; Phf6.
DR   GeneTree; ENSGT00530000063780; -.
DR   HOVERGEN; HBG049389; -.
DR   PhylomeDB; Q9D4J7; -.
DR   NextBio; 332793; -.
DR   ArrayExpress; Q9D4J7; -.
DR   Bgee; Q9D4J7; -.
DR   CleanEx; MM_PHF6; -.
DR   Genevestigator; Q9D4J7; -.
DR   GermOnline; ENSMUSG00000025626; Mus musculus.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 2.
DR   SMART; SM00249; PHD; 2.
DR   PROSITE; PS01359; ZF_PHD_1; FALSE_NEG.
DR   PROSITE; PS50016; ZF_PHD_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Metal-binding; Nucleus; Phosphoprotein; Repeat;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    364       PHD finger protein 6.
FT                                /FTId=PRO_0000059294.
FT   ZN_FING      79    131       PHD-type 1; degenerate.
FT   ZN_FING     277    329       PHD-type 2; degenerate.
FT   MOTIF        13     16       Nuclear localization signal (Potential).
FT   MOTIF       129    133       Nuclear localization signal (Potential).
FT   MOTIF       157    169       Nucleolar localization signal
FT                                (Potential).
FT   MOD_RES     120    120       Phosphoserine (By similarity).
FT   MOD_RES     138    138       Phosphoserine (By similarity).
FT   MOD_RES     145    145       Phosphoserine (By similarity).
FT   MOD_RES     154    154       Phosphoserine (By similarity).
FT   MOD_RES     155    155       Phosphoserine (By similarity).
FT   MOD_RES     199    199       Phosphoserine (By similarity).
FT   MOD_RES     203    203       Phosphoserine (By similarity).
FT   MOD_RES     204    204       Phosphoserine (By similarity).
FT   MOD_RES     357    357       Phosphothreonine.
FT   VAR_SEQ       1     80       Missing (in isoform 2).
FT                                /FTId=VSP_009375.
SQ   SEQUENCE   364 AA;  41139 MW;  D147BCE8C553F211 CRC64;
     MSSSIEQKKG STRQRKCGFC KSNRDKECGQ LLISENQKVA AHHKCMLFSS ALVSSHSDNE
     SLGGFSIEDV QKEIKRGTKL MCSLCHCPGA TIGCDVKTCH RTYHYHCALH DKAQIREKPS
     QGIYMVYCRK HKKTAHNSEA DLEESFNEHE LEPSSPKTKK KSRKGRPRKT NLKGLPEDSR
     STSSHGTDEM ESSSYRDRSP HRSSPNDTRP KCGFCHVGEE ENEARGKLHI FNAKKAAAHY
     KCMLFSSGTV QLTTTSRAEF GDFDIKTVLQ EIKRGKRMKC TLCSQPGATI GCEIKACVKT
     YHYHCGVQDK AKYIENMSRG IYKLYCKNHS GNDERDEEDE ERESKSRGRV AIDQQLTQQQ
     LNGN
//
ID   Q9D525_MOUSE            Unreviewed;       344 AA.
AC   Q9D525;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   SubName: Full=Putative uncharacterized protein;
DE   SubName: Full=Sorting nexin 16;
DE   SubName: Full=Sorting nexin 16, isoform CRA_b;
GN   Name=Snx16; ORFNames=mCG_1636;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RA   Adachi J., Aizawa K., Akahira S., Akimura T., Arai A., Aono H.,
RA   Arakawa T., Bono H., Carninci P., Fukuda S., Fukunishi Y., Furuno M.,
RA   Hanagaki T., Hara A., Hayatsu N., Hiramoto K., Hiraoka T., Hori F.,
RA   Imotani K., Ishii Y., Itoh M., Izawa M., Kasukawa T., Kato H.,
RA   Kawai J., Kojima Y., Konno H., Kouda M., Koya S., Kurihara C.,
RA   Matsuyama T., Miyazaki A., Nishi K., Nomura K., Numazaki R., Ohno M.,
RA   Okazaki Y., Okido T., Owa C., Saito H., Saito R., Sakai C., Sakai K.,
RA   Sano H., Sasaki D., Shibata K., Shibata Y., Shinagawa A., Shiraki T.,
RA   Sogabe Y., Suzuki H., Tagami M., Tagawa A., Takahashi F., Tanaka T.,
RA   Tejima Y., Toya T., Yamamura T., Yasunishi A., Yoshida K., Yoshino M.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC019424; AAH19424.1; -; mRNA.
DR   EMBL; AK015872; BAB30011.1; -; mRNA.
DR   EMBL; CH466577; EDL05159.1; -; Genomic_DNA.
DR   IPI; IPI00896061; -.
DR   RefSeq; NP_001120663.1; NM_001127191.1.
DR   RefSeq; NP_083344.3; NM_029068.3.
DR   UniGene; Mm.440548; -.
DR   HSSP; P03069; 1IHQ.
DR   ProteinModelPortal; Q9D525; -.
DR   SMR; Q9D525; 111-216.
DR   STRING; Q9D525; -.
DR   PRIDE; Q9D525; -.
DR   Ensembl; ENSMUST00000029047; ENSMUSP00000029047; ENSMUSG00000027534.
DR   GeneID; 74718; -.
DR   KEGG; mmu:74718; -.
DR   CTD; 74718; -.
DR   MGI; MGI:1921968; Snx16.
DR   GeneTree; ENSGT00390000005651; -.
DR   HOVERGEN; HBG057106; -.
DR   InParanoid; Q9D525; -.
DR   OMA; PYVPVPM; -.
DR   PhylomeDB; Q9D525; -.
DR   NextBio; 341470; -.
DR   ArrayExpress; Q9D525; -.
DR   Bgee; Q9D525; -.
DR   Genevestigator; Q9D525; -.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   InterPro; IPR001683; Phox.
DR   Gene3D; G3DSA:3.30.1520.10; PX; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; PX; 1.
DR   PROSITE; PS50195; PX; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   344 AA;  38817 MW;  F8AD14C543A8EBC6 CRC64;
     MATPYVPVPM PIGNSASSFT NNRNQRSSSF GSVSTSSTSS KGQLEDSAVG SLKQTNVQDQ
     MDSASSMCGS PLIRTKFTGT DSSIEYSARP REAEEQHPEA VNWEDRPSTP TILGYEVMEE
     RAKFTVYKIL VKKSPEESWV VFRRYTDFSR LNDKLKEMFP GFRLALPPKR WFKDNYNAEF
     LEDRQLGLQA FLQNLVAHKD IANCLAVREF LCLDDPPGPF DSLEESRAFC ETLEETNYHL
     QRELLEKQKE VESLKKLLGE KQLHIDALET RIRTLSLEPG ASLYVSRAEG GQILRVEPSV
     LQVNRDVLDE ESRADHKPHF NSREAGSVIA GIEVAQLAYN AEDD
//
ID   ATAD1_MOUSE             Reviewed;         361 AA.
AC   Q9D5T0; Q3U8V2; Q9D7A4;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=ATPase family AAA domain-containing protein 1;
GN   Name=Atad1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow, Cecum, Embryo, Lung, Testis, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
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DR   EMBL; AK009419; BAB26274.1; -; mRNA.
DR   EMBL; AK014967; BAB29643.1; -; mRNA.
DR   EMBL; AK030719; BAC27097.1; -; mRNA.
DR   EMBL; AK033639; BAC28402.1; -; mRNA.
DR   EMBL; AK150469; BAE29586.1; -; mRNA.
DR   EMBL; AK152059; BAE30915.1; -; mRNA.
DR   EMBL; AK165953; BAE38481.1; -; mRNA.
DR   EMBL; BC029085; AAH29085.1; -; mRNA.
DR   EMBL; BC043051; AAH43051.1; -; mRNA.
DR   IPI; IPI00108410; -.
DR   RefSeq; NP_080763.2; NM_026487.3.
DR   UniGene; Mm.27123; -.
DR   ProteinModelPortal; Q9D5T0; -.
DR   SMR; Q9D5T0; 78-355.
DR   PhosphoSite; Q9D5T0; -.
DR   PRIDE; Q9D5T0; -.
DR   Ensembl; ENSMUST00000070210; ENSMUSP00000069962; ENSMUSG00000013662.
DR   GeneID; 67979; -.
DR   KEGG; mmu:67979; -.
DR   UCSC; uc008hfo.1; mouse.
DR   CTD; 67979; -.
DR   MGI; MGI:1915229; Atad1.
DR   eggNOG; roNOG10094; -.
DR   HOGENOM; HBG724153; -.
DR   HOVERGEN; HBG057074; -.
DR   InParanoid; Q9D5T0; -.
DR   OMA; KNENXDR; -.
DR   OrthoDB; EOG412M5T; -.
DR   PhylomeDB; Q9D5T0; -.
DR   NextBio; 326122; -.
DR   ArrayExpress; Q9D5T0; -.
DR   Bgee; Q9D5T0; -.
DR   CleanEx; MM_ATAD1; -.
DR   Genevestigator; Q9D5T0; -.
DR   GermOnline; ENSMUSG00000013662; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   Pfam; PF00004; AAA; 1.
DR   SMART; SM00382; AAA; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Isopeptide bond; Nucleotide-binding;
KW   Phosphoprotein; Ubl conjugation.
FT   CHAIN         1    361       ATPase family AAA domain-containing
FT                                protein 1.
FT                                /FTId=PRO_0000084792.
FT   NP_BIND     133    140       ATP (Potential).
FT   MOD_RES     114    114       N6-acetyllysine (By similarity).
FT   MOD_RES     146    146       Phosphothreonine (By similarity).
FT   MOD_RES     322    322       Phosphoserine.
FT   CROSSLNK     46     46       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CONFLICT    123    123       L -> M (in Ref. 1; BAB26274).
FT   CONFLICT    206    206       H -> L (in Ref. 1; BAB26274).
SQ   SEQUENCE   361 AA;  40744 MW;  2FAE88BA7E7140BC CRC64;
     MVHAEAFSRP LSRNEVVGLI FRLTIFGAVT YFTIKWMVDA IDPTRKQKVE AQKQAEKLMK
     QIGVKNVKLS EYEMSIAAHL VDPLNMHVTW SDIAGLDDVI TDLKDTVILP IKKKHLFENS
     RLLQPPKGVL LYGPPGCGKT LIAKATAKEA GCRFINLQPS TLTDKWYGES QKLAAAVFSL
     AIKLQPSIIF IDEIDSFLRN RSSSDHEATA MMKAQFMSLW DGLDTDHSCQ VIVMGATNRP
     QDLDSAIMRR MPTRFHINQP ALKQREAILK LILKNENVDR HVDLLEVAQE TDGFSGSDLK
     EMCRDAALLC VREYVNSTSE ESHDEDEIRP VQQQDLHRAI EKMKKSKDAA FQNVLTHVCL
     D
//
ID   CUL5_MOUSE              Reviewed;         780 AA.
AC   Q9D5V5; Q8BMQ6; Q8BV53; Q8C098;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Cullin-5;
DE            Short=CUL-5;
GN   Name=Cul5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain, Medulla oblongata, Ovary, Testis, and Uterus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Core component of multiple SCF-like ECS (Elongin BC-
CC       Cullin 2/5-SOCS-box protein) E3 ubiquitin-protein ligase
CC       complexes, which mediate the ubiquitination and subsequent
CC       proteasomal degradation of target proteins. As a scaffold protein
CC       may contribute to catalysis through positioning of the substrate
CC       and the ubiquitin-conjugating enzyme. The functional specificity
CC       of the E3 ubiquitin-protein ligase complex depends on the variable
CC       substrate recognition component. ECS(SOCS1) seems to direct
CC       ubiquitination of JAk2. Seems to be involved poteosomal
CC       degradation of p53/TP53 stimulated by adenovirus E1B-55 kDa
CC       protein. May form a cell surface vasopressin receptor (By
CC       similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Component of multiple ECS (Elongin BC-CUL2/5-SOCS-box
CC       protein) E3 ubiquitin-protein ligase complexes formed of CUL5, the
CC       Elongin BC (TCEB1 and TCEB2), RBX2 and a variable SOCS box domain-
CC       containing protein as substrate-specific recognition component.
CC       Component of the probable ECS(LRRC41) complex with the substrate
CC       recognition component LRRC41. Component of the probable ECS(SOCS1)
CC       complex with the substrate recognition component SOCS1. Component
CC       of the probable ECS(WSB1) complex with the substrate recognition
CC       subunit WSB1. Component of the probable ECS(SOCS3) complex with
CC       the substrate recognition component SOCS3. Component of the
CC       probable ECS(SPSB1) complex with the substrate recognition
CC       component SPSB1. Component of the probable ECS(SPSB2) complex with
CC       the substrate recognition component SPSB2. Component of the
CC       probable ECS(SPSB4) complex with the substrate recognition
CC       component SPSB4. Component of the probable ECS(RAB40C) complex
CC       with the substrate recognition subunit RAB40C. May also form
CC       complexes containing CUL5, Elongin BC (TCEB1 and TCEB2), RBX1 and
CC       TCEB3. May also form complexes containing CUL5, elongin BC complex
CC       (TCEB1 and TCEB2), RBX1 and VHL. Interacts with RNF7/RBX2, LRRC41,
CC       SOCS3, SPSB1, SPSB2, SPSB4 and RAB40C. Interacts with ASB1, ASB2,
CC       ASB6, ASB7 and ASB12 (By similarity).
CC   -!- PTM: Neddylated. Deneddylated via its interaction with the COP9
CC       signalosome (CSN) complex (By similarity).
CC   -!- SIMILARITY: Belongs to the cullin family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK014894; BAB29609.1; -; mRNA.
DR   EMBL; AK030306; BAC26889.1; -; mRNA.
DR   EMBL; AK031955; BAC27621.1; -; mRNA.
DR   EMBL; AK046030; BAC32575.1; -; mRNA.
DR   EMBL; AK080305; BAC37872.1; -; mRNA.
DR   EMBL; BC075710; AAH75710.1; -; mRNA.
DR   IPI; IPI00331507; -.
DR   RefSeq; NP_001155090.1; NM_001161618.1.
DR   RefSeq; NP_082083.2; NM_027807.3.
DR   UniGene; Mm.218910; -.
DR   UniGene; Mm.481537; -.
DR   PDB; 2WZK; X-ray; 2.05 A; A=1-384.
DR   PDBsum; 2WZK; -.
DR   ProteinModelPortal; Q9D5V5; -.
DR   SMR; Q9D5V5; 12-386, 401-780.
DR   STRING; Q9D5V5; -.
DR   PhosphoSite; Q9D5V5; -.
DR   PRIDE; Q9D5V5; -.
DR   Ensembl; ENSMUST00000034529; ENSMUSP00000034529; ENSMUSG00000032030.
DR   GeneID; 75717; -.
DR   KEGG; mmu:75717; -.
DR   NMPDR; fig|10090.3.peg.20206; -.
DR   UCSC; uc009pmi.1; mouse.
DR   CTD; 75717; -.
DR   MGI; MGI:1922967; Cul5.
DR   GeneTree; ENSGT00550000074299; -.
DR   HOGENOM; HBG357137; -.
DR   HOVERGEN; HBG099672; -.
DR   InParanoid; Q9D5V5; -.
DR   OMA; KLMLDSW; -.
DR   OrthoDB; EOG46Q6RZ; -.
DR   PhylomeDB; Q9D5V5; -.
DR   NextBio; 343766; -.
DR   ArrayExpress; Q9D5V5; -.
DR   Bgee; Q9D5V5; -.
DR   CleanEx; MM_CUL5; -.
DR   Genevestigator; Q9D5V5; -.
DR   GermOnline; ENSMUSG00000032030; Mus musculus.
DR   GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR016157; Cullin_CS.
DR   InterPro; IPR016158; Cullin_homology.
DR   InterPro; IPR001373; Cullin_N.
DR   InterPro; IPR019559; Cullin_neddylation_domain.
DR   InterPro; IPR016159; Cullin_repeat-like_dom.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2.
DR   Pfam; PF00888; Cullin; 1.
DR   Pfam; PF10557; Cullin_Nedd8; 1.
DR   SMART; SM00182; CULLIN; 1.
DR   SMART; SM00884; Cullin_Nedd8; 1.
DR   SUPFAM; SSF75632; Cullin_homology; 1.
DR   SUPFAM; SSF74788; Cullin_repeat-like; 1.
DR   PROSITE; PS01256; CULLIN_1; 1.
DR   PROSITE; PS50069; CULLIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Isopeptide bond; Phosphoprotein; Ubl conjugation;
KW   Ubl conjugation pathway.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    780       Cullin-5.
FT                                /FTId=PRO_0000119798.
FT   MOD_RES     210    210       Phosphothreonine (By similarity).
FT   CROSSLNK    724    724       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in NEDD8) (By
FT                                similarity).
FT   CONFLICT    573    573       W -> C (in Ref. 1; BAC27621).
FT   HELIX        15     31
FT   HELIX        37     53
FT   HELIX        59     81
FT   HELIX        86    103
FT   TURN        104    108
FT   HELIX       109    111
FT   HELIX       112    115
FT   HELIX       134    146
FT   HELIX       148    167
FT   HELIX       174    176
FT   HELIX       181    186
FT   HELIX       196    200
FT   HELIX       202    224
FT   HELIX       228    248
FT   HELIX       257    269
FT   HELIX       271    273
FT   HELIX       274    278
FT   TURN        285    288
FT   HELIX       290    300
FT   HELIX       308    320
FT   HELIX       324    329
FT   HELIX       330    332
FT   TURN        333    335
FT   HELIX       337    359
FT   HELIX       363    382
SQ   SEQUENCE   780 AA;  90974 MW;  C6EE7A1AF1038C0D CRC64;
     MATSNLLKNK GSLQFEDKWD FMHPIVLKLL RQESVTKQQW FDLFSDVHAV CLWDDKGSSK
     IHQALKEDIL EFIKQAQARV LSHQDDTALL KAYIVEWRKF FTQCDILPKP FCQLEVTLLG
     KQSSNKKSNM EDSIVRKLML DTWNESIFSN IKNRLQDSAM KLVHAERLGE AFDSQLVIGV
     RESYVNLCSN PEDKLQIYRD NFEKAYLDST ERFYRTQAPS YLQQNGVQNY MKYADAKLKE
     EEKRALRYLE TRRECNSVEA LMECCVNALV TSFKETILAE CQGMIKRNET EKLHLMFSLM
     DKVPNGIEPM LKDLEEHIIS AGLADMVAAA ETITTDSEKY VEQLLTLFNR FSKLVKEAFQ
     DDPRFLTARD KAYKAVVNDA TIFKLELPLK QKGVGLKTQP ESKCPELLAN YCDMLLRKTP
     LSKKLTSEEI EAKLKEVLLV LKYVQNKDVF MRYHKAHLTR RLILDISADS EIEENMVEWL
     REVGMPADYV NKLARMFQDI KVSEDLNQAF KEMHKNNKLA LPADSVNIKI LNAGAWSRSS
     EKVFVSLPTE LEDLIPEVEE FYKKNHSGRK LHWHHLMSNG IITFKNEVGQ YDLEVTTFQL
     AVLFAWNQRP REKISFENLK LATELPDAEL RRTLWSLVAF PKLKRQVLLY DPQVNSPKDF
     TEGTLFSVNQ DFSLIKNAKV QKRGKINLIG RLQLTTERMR EEENEGIVQL RILRTQEAII
     QIMKMRKKIS NAQLQTELVE ILKNMFLPQK KMIKEQMEWL IEHRYIRRDE ADINTFIYMA
//
ID   SYAP1_MOUSE             Reviewed;         365 AA.
AC   Q9D5V6; Q3UI67; Q9D870;
DT   09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Synapse-associated protein 1;
GN   Name=Syap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Heart, Small intestine, Spinal ganglion, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-262, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SIMILARITY: Contains 1 BSD domain.
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DR   EMBL; AK008390; BAB25643.1; -; mRNA.
DR   EMBL; AK014893; BAB29608.1; -; mRNA.
DR   EMBL; AK051251; BAC34575.1; -; mRNA.
DR   EMBL; AK147055; BAE27639.1; -; mRNA.
DR   EMBL; BC021373; AAH21373.1; -; mRNA.
DR   IPI; IPI00317599; -.
DR   RefSeq; NP_080208.2; NM_025932.2.
DR   UniGene; Mm.44207; -.
DR   ProteinModelPortal; Q9D5V6; -.
DR   SMR; Q9D5V6; 144-231.
DR   STRING; Q9D5V6; -.
DR   PhosphoSite; Q9D5V6; -.
DR   REPRODUCTION-2DPAGE; IPI00317599; -.
DR   PRIDE; Q9D5V6; -.
DR   Ensembl; ENSMUST00000033723; ENSMUSP00000033723; ENSMUSG00000031357.
DR   GeneID; 67043; -.
DR   KEGG; mmu:67043; -.
DR   UCSC; uc009uun.1; mouse.
DR   CTD; 67043; -.
DR   MGI; MGI:1914293; Syap1.
DR   GeneTree; ENSGT00390000007662; -.
DR   HOGENOM; HBG278505; -.
DR   HOVERGEN; HBG057553; -.
DR   InParanoid; Q9D5V6; -.
DR   OMA; WVDTNDE; -.
DR   OrthoDB; EOG473PS3; -.
DR   PhylomeDB; Q9D5V6; -.
DR   NextBio; 323404; -.
DR   ArrayExpress; Q9D5V6; -.
DR   Bgee; Q9D5V6; -.
DR   CleanEx; MM_SYAP1; -.
DR   Genevestigator; Q9D5V6; -.
DR   GermOnline; ENSMUSG00000031357; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   InterPro; IPR005607; BSD.
DR   Pfam; PF03909; BSD; 1.
DR   SMART; SM00751; BSD; 1.
DR   PROSITE; PS50858; BSD; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein.
FT   CHAIN         1    365       Synapse-associated protein 1.
FT                                /FTId=PRO_0000072356.
FT   DOMAIN      172    224       BSD.
FT   MOD_RES     205    205       N6-acetyllysine (By similarity).
FT   MOD_RES     262    262       Phosphothreonine.
FT   MOD_RES     283    283       Phosphoserine (By similarity).
FT   MOD_RES     341    341       Phosphotyrosine (By similarity).
FT   CONFLICT    243    243       E -> K (in Ref. 1; BAB25643).
SQ   SEQUENCE   365 AA;  41350 MW;  7553E79C0C50E96B CRC64;
     MFGGLSSWLG LKPPEGAAAE GEEPPSRDGD KLSAGAAPSE ESPERPVEPT EEQQQQPPTE
     DPQFLHQAKG LGNYLYNFAS AATKKITESV TETAQTIKKS VEEGKIDDIL DKTILGDFQK
     EQKKFVEEQN TKKSEAAVPP WVESHDEETI QQQILALSAD KRNFLRDPPA GVQFNFDFDQ
     MYPVALVMLQ EDELLSKMRF ALVPKLVKEE VFWRNYFYRI SLIKQSAQLT ALAAQQQASG
     KEEKSSNRDD NLPLTEAVRP KTPPVVIKSQ LKSQEDEEEI STSPGVSEFV SDAFDTCSLN
     QEDLRKEMEQ LVLDKKQEEA TALEEDSTDW EKELQQELQE YEVVAESEKR DENWDKEIEK
     MLQES
//
ID   RFIP1_MOUSE             Reviewed;         645 AA.
AC   Q9D620; Q3UBC2; Q8BN24;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Rab11 family-interacting protein 1;
DE            Short=Rab11-FIP1;
DE   AltName: Full=Rab-coupling protein;
GN   Name=Rab11fip1; Synonyms=Rcp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358 AND SER-383, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-346, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: A Rab11 effector protein involved in the endosomal
CC       recycling process. Also involved in controlling membrane
CC       trafficking along the phagocytic pathway and phagocytosis (By
CC       similarity).
CC   -!- SUBUNIT: Homooligomer. Interacts with RAB4A, RAB11A, RAB11B and
CC       RAB25 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Recycling endosome (By similarity).
CC       Cytoplasmic vesicle, phagosome membrane (By similarity).
CC       Note=Membrane-bound. RAB11A rather than RAB4A mediates RAB11FIP1
CC       localization in the endocytic recycling compartment (ERC).
CC       Colocalizes with RAB11A at phagosomes (By similarity).
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 FIP-RBD domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK014696; BAB29507.1; -; mRNA.
DR   EMBL; AK151024; BAE30042.1; -; mRNA.
DR   IPI; IPI00317548; -.
DR   UniGene; Mm.205335; -.
DR   ProteinModelPortal; Q9D620; -.
DR   SMR; Q9D620; 14-150, 605-637.
DR   STRING; Q9D620; -.
DR   PhosphoSite; Q9D620; -.
DR   PRIDE; Q9D620; -.
DR   Ensembl; ENSMUST00000033878; ENSMUSP00000033878; ENSMUSG00000031488.
DR   MGI; MGI:1923017; Rab11fip1.
DR   GeneTree; ENSGT00530000063203; -.
DR   HOVERGEN; HBG079127; -.
DR   OrthoDB; EOG42JNQP; -.
DR   ArrayExpress; Q9D620; -.
DR   Bgee; Q9D620; -.
DR   CleanEx; MM_RAB11FIP1; -.
DR   Genevestigator; Q9D620; -.
DR   GermOnline; ENSMUSG00000031488; Mus musculus.
DR   GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR019018; Rab11-bd_FIP_dom_C.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF09457; RBD-FIP; 1.
DR   SMART; SM00239; C2; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS51511; FIP_RBD; 1.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Endosome; Membrane; Phosphoprotein;
KW   Protein transport; Transport.
FT   CHAIN         1    645       Rab11 family-interacting protein 1.
FT                                /FTId=PRO_0000097305.
FT   DOMAIN        5    110       C2.
FT   DOMAIN      573    635       FIP-RBD.
FT   REGION      581    645       Necessary for interaction with RAB4A and
FT                                RAB11A, subcellular location and
FT                                endosomal recycling (By similarity).
FT   COMPBIAS    211    220       Poly-Lys.
FT   MOD_RES     158    158       Phosphoserine (By similarity).
FT   MOD_RES     201    201       Phosphoserine (By similarity).
FT   MOD_RES     204    204       Phosphoserine (By similarity).
FT   MOD_RES     238    238       Phosphoserine (By similarity).
FT   MOD_RES     301    301       Phosphoserine (By similarity).
FT   MOD_RES     339    339       Phosphoserine (By similarity).
FT   MOD_RES     340    340       Phosphoserine (By similarity).
FT   MOD_RES     342    342       Phosphoserine (By similarity).
FT   MOD_RES     344    344       Phosphoserine.
FT   MOD_RES     346    346       Phosphoserine.
FT   MOD_RES     357    357       Phosphoserine.
FT   MOD_RES     358    358       Phosphoserine.
FT   MOD_RES     383    383       Phosphoserine.
FT   MOD_RES     434    434       Phosphoserine (By similarity).
FT   MOD_RES     492    492       Phosphoserine (By similarity).
FT   MOD_RES     496    496       Phosphoserine (By similarity).
FT   MOD_RES     497    497       Phosphoserine (By similarity).
FT   CONFLICT     60     60       T -> S (in Ref. 1; BAE30042).
FT   CONFLICT    207    207       E -> K (in Ref. 1; BAE30042).
FT   CONFLICT    256    256       Q -> H (in Ref. 1; BAE30042).
FT   CONFLICT    283    283       T -> A (in Ref. 1; BAE30042).
SQ   SEQUENCE   645 AA;  70698 MW;  282F30E058194F8E CRC64;
     MSLAASAGRG PGTMWSPTHV QVTVLQARGL RAKGPGGTSD AYAVIQVGKE KYATSVSERT
     LGAPVWREEA TFELPPLLSS GAAPAAAATL QLTVLHRALL GLDKFLGRAE VDLRELHRDQ
     GRRKKQWYTL KSKPGKKDKE RGEIEVDIQF MRNNMTASMF DLSMKDKSRN PFGKLKDKIK
     GKNKDSASDT ASAIVPSVTP SVDSDDESFS KDKKKKSKIK TLFSKSSLQK TPLSQSMSVL
     PTSKSDKVLL RAGDFQSQWD DDAHEDESSS ASDVMSHKRT SSTDQQPNQS NFSLPKKEGL
     SFLGGLRSKN DSLSRSTVCI NGNHVYMEQP EARSEIRESS PSNSPSPQGF RRKHLFSSTE
     NLAARSPKEP GEGGGTSSDR RLSDSSTKDS MKSMSLPSYR PLTSGDNRES MSPANVEAAR
     ETKDSKKQES KKSSLLSLVT GKRDAAAKGS ESEPLPTVSE KEKERKGALV EAQLREEDLM
     RRPEKDALPV ASQWGSSLNP FEDVQISDPG ATTESRSEPK PPVPAARVPQ TKAVKPRPHP
     VKPMNTTATK IANSSLGTAT IITENLISEA LMKKYQPSDP AFAYAQLTHD ELIQLVLKQK
     ETISKKEFQV RELEDYIDNL LVRVMEETPN ILRVPAQMGK KAGKM
//
ID   FA84A_MOUSE             Reviewed;         292 AA.
AC   Q9D650; Q99K34;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Protein FAM84A;
GN   Name=Fam84a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the FAM84 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK014625; BAB29470.1; -; mRNA.
DR   EMBL; BC005488; AAH05488.1; -; mRNA.
DR   IPI; IPI00320004; -.
DR   RefSeq; NP_083283.2; NM_029007.2.
DR   UniGene; Mm.227253; -.
DR   ProteinModelPortal; Q9D650; -.
DR   PhosphoSite; Q9D650; -.
DR   PRIDE; Q9D650; -.
DR   Ensembl; ENSMUST00000020926; ENSMUSP00000020926; ENSMUSG00000020607.
DR   GeneID; 105005; -.
DR   KEGG; mmu:105005; -.
DR   UCSC; uc007nbn.1; mouse.
DR   CTD; 105005; -.
DR   MGI; MGI:2145011; Fam84a.
DR   eggNOG; roNOG10437; -.
DR   GeneTree; ENSGT00390000013755; -.
DR   HOGENOM; HBG713831; -.
DR   HOVERGEN; HBG054465; -.
DR   InParanoid; Q9D650; -.
DR   OrthoDB; EOG4M399T; -.
DR   NextBio; 357398; -.
DR   ArrayExpress; Q9D650; -.
DR   Bgee; Q9D650; -.
DR   Genevestigator; Q9D650; -.
DR   GermOnline; ENSMUSG00000020607; Mus musculus.
DR   InterPro; IPR007053; NC.
DR   Pfam; PF04970; NC; 1.
PE   2: Evidence at transcript level;
FT   CHAIN         1    292       Protein FAM84A.
FT                                /FTId=PRO_0000234426.
FT   COMPBIAS     71     74       Poly-His.
FT   CONFLICT    153    153       V -> I (in Ref. 2; AAH05488).
SQ   SEQUENCE   292 AA;  32676 MW;  D500C38DC50AFAFA CRC64;
     MGNQLDRITH LNYSELPTGD PSGIEKDELR VGVAYFFSDE EEDLDERGQP DKFGVKGPPG
     CSPCPESPSR HHHHLLHQLV LNETQFSAFR GQECIFSKVT GGPQGADLSV YAVTALPAIC
     EPGDLLELLW LQPATEQPAP APHWAVYVGG GQVIHLHQGE IRQDSLYQAG AANVGRVVNS
     WYRYRPLVAE LVVQNACGHL GLKSEEICWT NSESFAAWCR FGKREFKAGG EVPAGTQPPQ
     QQYYLKVHLE ENKVHTARFH SLEDLIREKR RIDASGRLRV LQELEDFVDD KE
//
ID   GBRA4_MOUSE             Reviewed;         552 AA.
AC   Q9D6F4;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   04-MAY-2001, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Gamma-aminobutyric acid receptor subunit alpha-4;
DE   AltName: Full=GABA(A) receptor subunit alpha-4;
DE   Flags: Precursor;
GN   Name=Gabra4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: GABA, the major inhibitory neurotransmitter in the
CC       vertebrate brain, mediates neuronal inhibition by binding to the
CC       GABA/benzodiazepine receptor and opening an integral chloride
CC       channel.
CC   -!- SUBUNIT: Generally pentameric. There are five types of GABA(A)
CC       receptor chains: alpha, beta, gamma, delta, and rho.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, postsynaptic cell
CC       membrane; Multi-pass membrane protein. Cell membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9)
CC       family. Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily.
CC       GABRA4 sub-subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK013727; BAB28975.1; -; mRNA.
DR   IPI; IPI00109065; -.
DR   RefSeq; NP_034381.1; NM_010251.2.
DR   UniGene; Mm.248731; -.
DR   ProteinModelPortal; Q9D6F4; -.
DR   SMR; Q9D6F4; 285-344.
DR   STRING; Q9D6F4; -.
DR   PRIDE; Q9D6F4; -.
DR   Ensembl; ENSMUST00000031121; ENSMUSP00000031121; ENSMUSG00000029211.
DR   GeneID; 14397; -.
DR   KEGG; mmu:14397; -.
DR   UCSC; uc008xqy.1; mouse.
DR   CTD; 14397; -.
DR   MGI; MGI:95616; Gabra4.
DR   GeneTree; ENSGT00550000074441; -.
DR   HOGENOM; HBG506497; -.
DR   HOVERGEN; HBG051707; -.
DR   InParanoid; Q9D6F4; -.
DR   OMA; FLCLAAC; -.
DR   OrthoDB; EOG4MPHQ4; -.
DR   PhylomeDB; Q9D6F4; -.
DR   NextBio; 285935; -.
DR   ArrayExpress; Q9D6F4; -.
DR   Bgee; Q9D6F4; -.
DR   Genevestigator; Q9D6F4; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005230; F:extracellular ligand-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0004890; F:GABA-A receptor activity; IEA:InterPro.
DR   GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IEA:InterPro.
DR   InterPro; IPR006028; GABAA_rcpt.
DR   InterPro; IPR001390; GABAAa_rcpt.
DR   InterPro; IPR005434; GABBAa4_rcpt.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR006201; Neur_channel.
DR   InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR   InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR   Gene3D; G3DSA:2.70.170.10; Neur_chan_lig_bd; 1.
DR   PANTHER; PTHR18945; Neur_channel; 1.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   PRINTS; PR01079; GABAARALPHA.
DR   PRINTS; PR01617; GABAARALPHA4.
DR   PRINTS; PR00253; GABAARECEPTR.
DR   PRINTS; PR00252; NRIONCHANNEL.
DR   SUPFAM; SSF90112; Neu_channel_TM; 1.
DR   SUPFAM; SSF63712; Neur_chan_LBD; 1.
DR   TIGRFAMs; TIGR00860; LIC; 1.
DR   PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Chloride; Chloride channel;
KW   Disulfide bond; Glycoprotein; Ion transport; Ionic channel;
KW   Ligand-gated ion channel; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Receptor; Signal; Synapse; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     35       Potential.
FT   CHAIN        36    552       Gamma-aminobutyric acid receptor subunit
FT                                alpha-4.
FT                                /FTId=PRO_0000000442.
FT   TOPO_DOM     36    258       Extracellular (Probable).
FT   TRANSMEM    259    280       Helical; (Probable).
FT   TRANSMEM    285    306       Helical; (Probable).
FT   TRANSMEM    318    340       Helical; (Probable).
FT   TOPO_DOM    341    521       Cytoplasmic (Probable).
FT   TRANSMEM    522    541       Helical; (Probable).
FT   MOD_RES     140    140       Phosphoserine (By similarity).
FT   MOD_RES     142    142       Phosphoserine (By similarity).
FT   CARBOHYD     47     47       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    144    144       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    157    157       N-linked (GlcNAc...) (Potential).
FT   DISULFID    172    186       By similarity.
SQ   SEQUENCE   552 AA;  60878 MW;  213C16C423D7F97B CRC64;
     MVSVQKVPAI ALCSGVSLAL LHFLCLAACL NESPGQNSKD EKLCPENFTR ILDSLLDGYD
     NRLRPGFGGP VTEVKTDIYV TSFGPVSDVE MEYTMDVFFR QTWIDKRLKY DGPIEILRLN
     NMMVTKVWTP DTFFRNGKKS VSHNMTAPNK LFRIMRNGTI LYTMRLTISA ECPMRLVDFP
     MDGHACPLKF GSYAYPKSEM IYTWTKGPEK SVEVPKESSS LVQYDLIGQT VSSETIKSIT
     GEYIVMTVYF HLRRKMGYFM IQTYIPCIMT VILSQVSFWI NKESVPARTV FGITTVLTMT
     TLSISARHSL PKVSYATAMD WFIAVCFAFV FSALIEFAAV NYFTNIQMQK AKKKISKPPP
     EVPAAPVLKE KHTETSLQNT HANLNMRKRT NALVHSESDV KSRTEVGNHS SKTSAVQESS
     EATPKAHLAS SPNPFSRANA AETMSAAARG LSSAASPSPH GTLRPASLGS ASTRPAFGSR
     LGRIKTTVNT TGAAGNVSAT PPPPAPPPSG SGTSKIDKYA RILFPVTFGA FNMVYWVVYL
     SKDTMEKSES LM
//
ID   TBB4_MOUSE              Reviewed;         444 AA.
AC   Q9D6F9; Q62364; Q80Y54;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 3.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Tubulin beta-4 chain;
GN   Name=Tubb4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 3-19; 47-77; 104-121; 163-174; 242-276; 283-297;
RP   310-318; 321-359; 363-379 AND 381-390, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 66-444.
RX   MEDLINE=85289512; PubMed=3839797; DOI=10.1083/jcb.101.3.852;
RA   Lewis S.A., Lee M.G.-S., Cowan N.J.;
RT   "Five mouse tubulin isotypes and their regulated expression during
RT   development.";
RL   J. Cell Biol. 101:852-861(1985).
RN   [5]
RP   POLYGLUTAMYLATION.
RX   PubMed=15890843; DOI=10.1126/science.1113010;
RA   Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M.,
RA   Temurak N., van Dijk J., Boucher D., van Dorsselaer A.,
RA   Suryavanshi S., Gaertig J., Edde B.;
RT   "Tubulin polyglutamylase enzymes are members of the TTL domain protein
RT   family.";
RL   Science 308:1758-1762(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-36, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-366, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RA   Lubec G., Kang S.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [8]
RP   POLYGLYCYLATION.
RX   PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA   Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M.,
RA   Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J.,
RA   Janke C.;
RT   "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT   polyglycylation.";
RL   Cell 137:1076-1087(2009).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. It
CC       binds two moles of GTP, one at an exchangeable site on the beta
CC       chain and one at a non-exchangeable site on the alpha-chain.
CC   -!- SUBUNIT: Dimer of alpha and beta chains.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- DOMAIN: The highly acidic C-terminal region may bind cations such
CC       as calcium.
CC   -!- PTM: Some glutamate residues at the C-terminus are either
CC       polyglutamylated or polyglycylated. These 2 modifications occur
CC       exclusively on glutamate residues and result in either
CC       polyglutamate or polyglycine chains on the gamma-carboxyl group.
CC       Glycylation is mainly limited to tubulin incorporated into
CC       axonemes (cilia and flagella) whereas glutamylation is prevalent
CC       in neuronal cells, centrioles, axonemes, and the mitotic spindle.
CC       Both modifications can coexist on the same protein on adjacent
CC       residues, and lowering polyglycylation levels increases
CC       polyglutamylation, and reciprocally. The precise function of such
CC       modifications is still unclear but they are regulate the assembly
CC       and dynamics of axonemal microtubules.
CC   -!- SIMILARITY: Belongs to the tubulin family.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK013717; BAB28967.1; -; mRNA.
DR   EMBL; BC049112; AAH49112.1; -; mRNA.
DR   EMBL; BC054831; AAH54831.1; -; mRNA.
DR   EMBL; M28730; AAA40509.1; -; mRNA.
DR   IPI; IPI00109073; -.
DR   RefSeq; NP_033477.2; NM_009451.3.
DR   UniGene; Mm.7420; -.
DR   ProteinModelPortal; Q9D6F9; -.
DR   SMR; Q9D6F9; 2-427.
DR   STRING; Q9D6F9; -.
DR   PhosphoSite; Q9D6F9; -.
DR   REPRODUCTION-2DPAGE; IPI00109073; -.
DR   REPRODUCTION-2DPAGE; Q9D6F9; -.
DR   PRIDE; Q9D6F9; -.
DR   Ensembl; ENSMUST00000071135; ENSMUSP00000071135; ENSMUSG00000062591.
DR   GeneID; 22153; -.
DR   KEGG; mmu:22153; -.
DR   CTD; 22153; -.
DR   MGI; MGI:107848; Tubb4.
DR   eggNOG; roNOG14625; -.
DR   GeneTree; ENSGT00600000084215; -.
DR   HOGENOM; HBG750007; -.
DR   HOVERGEN; HBG000089; -.
DR   InParanoid; Q9D6F9; -.
DR   OMA; MQLERIN; -.
DR   OrthoDB; EOG4DFPNJ; -.
DR   PhylomeDB; Q9D6F9; -.
DR   NextBio; 302070; -.
DR   ArrayExpress; Q9D6F9; -.
DR   Bgee; Q9D6F9; -.
DR   CleanEx; MM_TUBB4; -.
DR   Genevestigator; Q9D6F9; -.
DR   GermOnline; ENSMUSG00000062591; Mus musculus.
DR   GO; GO:0005929; C:cilium; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0033269; C:internode region of axon; IDA:MGI.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0043209; C:myelin sheath; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR   InterPro; IPR013838; Beta-tubulin_BS.
DR   InterPro; IPR002453; Beta_tubulin.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR023123; Tubulin_C.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   Gene3D; G3DSA:3.30.1330.20; Tubulin/FtsZ_2-layer-sand-dom; 1.
DR   Gene3D; G3DSA:1.10.287.600; Tubulin_C; 1.
DR   Gene3D; G3DSA:3.40.50.1440; Tubulin_FtsZ; 1.
DR   PANTHER; PTHR11588; Tubulin; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01163; BETATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF55307; Tub_FtsZ_C; 1.
DR   SUPFAM; SSF52490; Tubulin_FtsZ; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
DR   PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE   1: Evidence at protein level;
KW   Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; GTP-binding; Microtubule;
KW   Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1    444       Tubulin beta-4 chain.
FT                                /FTId=PRO_0000048254.
FT   NP_BIND     140    146       GTP (Potential).
FT   MOD_RES      36     36       Phosphotyrosine.
FT   MOD_RES     290    290       Phosphothreonine (By similarity).
FT   MOD_RES     366    366       Phosphothreonine.
FT   CONFLICT     73     73       M -> I (in Ref. 4; AAA40509).
FT   CONFLICT    111    111       E -> Q (in Ref. 4; AAA40509).
FT   CONFLICT    270    270       F -> L (in Ref. 4; AAA40509).
FT   CONFLICT    293    293       M -> V (in Ref. 4; AAA40509).
FT   CONFLICT    303    303       C -> S (in Ref. 4; AAA40509).
FT   CONFLICT    351    351       T -> A (in Ref. 4; AAA40509).
FT   CONFLICT    400    400       G -> A (in Ref. 4; AAA40509).
FT   CONFLICT    427    427       D -> G (in Ref. 1; BAB28967).
SQ   SEQUENCE   444 AA;  49586 MW;  F7429D057C11A3F5 CRC64;
     MREIVHLQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLERINVY YNEATGGNYV
     PRAVLVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDAVLDVV
     RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEFP DRIMNTFSVV PSPKVSDTVV
     EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL
     RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQMFDAKNMM
     AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LSVQSKNSSY FVEWIPNNVK TAVCDIPPRG
     LKMAATFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDATA EEGEFEEEAE EEVA
//
ID   CA190_MOUSE             Reviewed;         239 AA.
AC   Q9D6I9;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 48.
DE   RecName: Full=Uncharacterized protein C1orf190 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
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DR   EMBL; AK013564; BAB28908.1; -; mRNA.
DR   IPI; IPI00109147; -.
DR   RefSeq; NP_080823.1; NM_026547.1.
DR   UniGene; Mm.132803; -.
DR   ProteinModelPortal; Q9D6I9; -.
DR   PhosphoSite; Q9D6I9; -.
DR   PRIDE; Q9D6I9; -.
DR   Ensembl; ENSMUST00000030469; ENSMUSP00000030469; ENSMUSG00000028701.
DR   GeneID; 68075; -.
DR   KEGG; mmu:68075; -.
DR   UCSC; uc008ugg.1; mouse.
DR   MGI; MGI:1915325; 1520402A15Rik.
DR   GeneTree; ENSGT00530000063790; -.
DR   HOGENOM; HBG714712; -.
DR   HOVERGEN; HBG099631; -.
DR   InParanoid; Q9D6I9; -.
DR   OMA; MELAYLR; -.
DR   OrthoDB; EOG4TQMBC; -.
DR   PhylomeDB; Q9D6I9; -.
DR   NextBio; 326362; -.
DR   ArrayExpress; Q9D6I9; -.
DR   Bgee; Q9D6I9; -.
DR   CleanEx; MM_1520402A15RIK; -.
DR   Genevestigator; Q9D6I9; -.
PE   2: Evidence at transcript level;
FT   CHAIN         1    239       Uncharacterized protein C1orf190 homolog.
FT                                /FTId=PRO_0000271079.
SQ   SEQUENCE   239 AA;  25830 MW;  5BFF6F204DCFB2D1 CRC64;
     MEGTAESQTP DLRDVEGKVG RKIPEGLLRG LRGECELGTS GDVLLPGAPS TGHGLGDKIM
     ALRMELAYLR AIDVKILQQL VTLNEGIEAV RWLLEERGTL TSHCSSLTSS QYSLTGGSPG
     RSRRGSWDSL PDTSSTDRLD SVSIGSFLDT VTPRELDEQG LPGPSCPEID WAKVIPTEDR
     ARTEVDMTST KLGSLTATWK LPGDGLQCGP PEPSEDGNAN QGFEAHWYWG QCQDDVTFL
//
ID   NDUB8_MOUSE             Reviewed;         186 AA.
AC   Q9D6J5; Q9D6M7;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial;
DE   AltName: Full=Complex I-ASHI;
DE            Short=CI-ASHI;
DE   AltName: Full=NADH-ubiquinone oxidoreductase ASHI subunit;
DE   Flags: Precursor;
GN   Name=Ndufb8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 35-43; 87-98 AND 160-186, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Accessory subunit of the mitochondrial membrane
CC       respiratory chain NADH dehydrogenase (Complex I), that is believed
CC       not to be involved in catalysis. Complex I functions in the
CC       transfer of electrons from NADH to the respiratory chain. The
CC       immediate electron acceptor for the enzyme is believed to be
CC       ubiquinone (By similarity).
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Single-pass
CC       membrane protein; Matrix side (By similarity).
CC   -!- SIMILARITY: Belongs to the complex I NDUFB8 subunit family.
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DR   EMBL; AK010177; BAB26749.1; -; mRNA.
DR   EMBL; AK013516; BAB28893.1; -; mRNA.
DR   EMBL; BC043019; AAH43019.1; -; mRNA.
DR   IPI; IPI00387430; -.
DR   RefSeq; NP_080337.1; NM_026061.2.
DR   UniGene; Mm.2060; -.
DR   STRING; Q9D6J5; -.
DR   PRIDE; Q9D6J5; -.
DR   Ensembl; ENSMUST00000026222; ENSMUSP00000026222; ENSMUSG00000025204.
DR   GeneID; 67264; -.
DR   KEGG; mmu:67264; -.
DR   UCSC; uc008hpw.1; mouse.
DR   CTD; 67264; -.
DR   MGI; MGI:1914514; Ndufb8.
DR   GeneTree; ENSGT00390000000628; -.
DR   HOGENOM; HBG280205; -.
DR   HOVERGEN; HBG000931; -.
DR   InParanoid; Q9D6J5; -.
DR   OMA; EPIHWDL; -.
DR   OrthoDB; EOG48GW47; -.
DR   PhylomeDB; Q9D6J5; -.
DR   NextBio; 324046; -.
DR   ArrayExpress; Q9D6J5; -.
DR   Bgee; Q9D6J5; -.
DR   Genevestigator; Q9D6J5; -.
DR   GermOnline; ENSMUSG00000025204; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005747; C:mitochondrial respiratory chain complex I; IEA:InterPro.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:InterPro.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR008699; NADH_UbQ_OxRdtase_ASHI_su.
DR   InterPro; IPR016551; NADH_UbQ_OxRdtase_b-cplx_su8.
DR   PANTHER; PTHR12840; NDUFB8; 1.
DR   PIRSF; PIRSF009288; NDUB8; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Respiratory chain;
KW   Transit peptide; Transmembrane; Transmembrane helix; Transport.
FT   TRANSIT       1     28       Mitochondrion (By similarity).
FT   CHAIN        29    186       NADH dehydrogenase [ubiquinone] 1 beta
FT                                subcomplex subunit 8, mitochondrial.
FT                                /FTId=PRO_0000020047.
FT   TRANSMEM    133    153       Helical; (Potential).
FT   CONFLICT    105    105       I -> V (in Ref. 1; BAB26749).
SQ   SEQUENCE   186 AA;  21876 MW;  DBD21FF09C9F90C1 CRC64;
     MAAARAAALG VRWLQRTTRG VVPLEARRAF HMTKDMLPGS YPRTPEERAA AAKKYNMRVE
     DYEPYPDDGM GYGDYPMLPN RSQHERDPWY QWDHSELRMN WGEPIHWDLD MYIRNRVDTS
     PTPVSWDVMC KHLFGFVAFM VFMFWVGHVF PSYQPVGPKQ YPYNNLYLER GGDPTKEPEP
     VVHYDI
//
ID   CALL3_MOUSE             Reviewed;         149 AA.
AC   Q9D6P8; Q99K52;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Calmodulin-like protein 3;
GN   Name=Calml3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be similar to that of authentic calmodulin and may
CC       actually compete with calmodulin by binding, with different
CC       affinities, to cellular substrates (By similarity).
CC   -!- MISCELLANEOUS: Binds four calcium ions (By similarity).
CC   -!- SIMILARITY: Belongs to the calmodulin family.
CC   -!- SIMILARITY: Contains 4 EF-hand domains.
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DR   EMBL; AK010118; BAB26712.1; -; mRNA.
DR   EMBL; BC005457; AAH05457.1; -; mRNA.
DR   IPI; IPI00109368; -.
DR   RefSeq; NP_081692.1; NM_027416.3.
DR   UniGene; Mm.20079; -.
DR   HSSP; P62161; 1QX7.
DR   ProteinModelPortal; Q9D6P8; -.
DR   SMR; Q9D6P8; 4-148.
DR   STRING; Q9D6P8; -.
DR   PhosphoSite; Q9D6P8; -.
DR   PRIDE; Q9D6P8; -.
DR   Ensembl; ENSMUST00000077698; ENSMUSP00000076880; ENSMUSG00000063130.
DR   GeneID; 70405; -.
DR   KEGG; mmu:70405; -.
DR   UCSC; uc007pja.1; mouse.
DR   CTD; 70405; -.
DR   MGI; MGI:1917655; Calml3.
DR   eggNOG; roNOG05550; -.
DR   GeneTree; ENSGT00560000076590; -.
DR   HOGENOM; HBG746798; -.
DR   HOVERGEN; HBG012180; -.
DR   InParanoid; Q9D6P8; -.
DR   OMA; CITTQEL; -.
DR   OrthoDB; EOG4DNF5P; -.
DR   PhylomeDB; Q9D6P8; -.
DR   NextBio; 331547; -.
DR   ArrayExpress; Q9D6P8; -.
DR   Bgee; Q9D6P8; -.
DR   CleanEx; MM_CALML3; -.
DR   Genevestigator; Q9D6P8; -.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   InterPro; IPR018248; EF-hand.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   Pfam; PF00036; efhand; 4.
DR   SMART; SM00054; EFh; 4.
DR   PROSITE; PS00018; EF_HAND_1; 4.
DR   PROSITE; PS50222; EF_HAND_2; 4.
PE   2: Evidence at transcript level;
KW   Calcium; Methylation; Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    149       Calmodulin-like protein 3.
FT                                /FTId=PRO_0000284521.
FT   DOMAIN        8     43       EF-hand 1.
FT   DOMAIN       44     79       EF-hand 2.
FT   DOMAIN       81    116       EF-hand 3.
FT   DOMAIN      117    149       EF-hand 4.
FT   CA_BIND      21     32       1.
FT   CA_BIND      57     68       2.
FT   CA_BIND      94    105       3.
FT   CA_BIND     130    141       4.
FT   MOD_RES     116    116       N6,N6,N6-trimethyllysine (By similarity).
FT   CONFLICT     68     68       E -> K (in Ref. 2; AAH05457).
SQ   SEQUENCE   149 AA;  16701 MW;  B4BA3C842D7186E0 CRC64;
     MADQLTEEQI AEFKEAFSLF DKDGDGSITT QELGTVMRSL GQNPTEAELQ GMVNEIDKDG
     NGTVDFPEFL TMMSRKMKDT DSEEEIREAF RVFDKDGNGF VSAAELRHVM TKLGEKLSDE
     EVDEMIQAAD TDGDGQVNYE EFVHMLVSK
//
ID   IDH3A_MOUSE             Reviewed;         366 AA.
AC   Q9D6R2; Q3UAM8; Q8C8A1; Q9D1L1;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial;
DE            EC=1.1.1.41;
DE   AltName: Full=Isocitric dehydrogenase subunit alpha;
DE   AltName: Full=NAD(+)-specific ICDH subunit alpha;
DE   Flags: Precursor;
GN   Name=Idh3a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and DBA/2;
RC   TISSUE=Bone marrow, Heart, Tongue, Visual cortex, and Wolffian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 59-85; 101-188; 206-214 AND 300-336, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B.,
RA   Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY: Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) +
CC       NADH.
CC   -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By
CC       similarity).
CC   -!- SUBUNIT: Heterooligomer of subunits alpha, beta, and gamma in the
CC       apparent ratio of 2:1:1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9D6R2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D6R2-2; Sequence=VSP_014517;
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK003393; BAB22760.1; -; mRNA.
DR   EMBL; AK010065; BAB26679.1; -; mRNA.
DR   EMBL; AK032787; BAC28021.1; -; mRNA.
DR   EMBL; AK047951; BAC33199.1; -; mRNA.
DR   EMBL; AK150618; BAE29708.1; -; mRNA.
DR   EMBL; AK151304; BAE30286.1; -; mRNA.
DR   EMBL; AK152353; BAE31145.1; -; mRNA.
DR   EMBL; AK153459; BAE32011.1; -; mRNA.
DR   EMBL; AK158646; BAE34596.1; -; mRNA.
DR   EMBL; AK159051; BAE34785.1; -; mRNA.
DR   EMBL; AK168049; BAE40031.1; -; mRNA.
DR   EMBL; AK168149; BAE40114.1; -; mRNA.
DR   EMBL; AK169152; BAE40931.1; -; mRNA.
DR   EMBL; BC034273; AAH34273.1; -; mRNA.
DR   EMBL; BC049956; AAH49956.1; -; mRNA.
DR   IPI; IPI00459725; -.
DR   IPI; IPI00608078; -.
DR   RefSeq; NP_083849.1; NM_029573.2.
DR   UniGene; Mm.279195; -.
DR   ProteinModelPortal; Q9D6R2; -.
DR   SMR; Q9D6R2; 18-362.
DR   STRING; Q9D6R2; -.
DR   PhosphoSite; Q9D6R2; -.
DR   REPRODUCTION-2DPAGE; Q9D6R2; -.
DR   UCD-2DPAGE; Q9D6R2; -.
DR   PRIDE; Q9D6R2; -.
DR   Ensembl; ENSMUST00000034818; ENSMUSP00000034818; ENSMUSG00000032279.
DR   GeneID; 67834; -.
DR   KEGG; mmu:67834; -.
DR   NMPDR; fig|10090.3.peg.20219; -.
DR   UCSC; uc009prg.1; mouse.
DR   UCSC; uc009pri.1; mouse.
DR   CTD; 67834; -.
DR   MGI; MGI:1915084; Idh3a.
DR   eggNOG; roNOG14850; -.
DR   GeneTree; ENSGT00550000074918; -.
DR   HOGENOM; HBG518924; -.
DR   HOVERGEN; HBG052080; -.
DR   InParanoid; Q9D6R2; -.
DR   OMA; GGNSKCS; -.
DR   OrthoDB; EOG4GMTX7; -.
DR   PhylomeDB; Q9D6R2; -.
DR   BRENDA; 1.1.1.41; 244.
DR   NextBio; 325657; -.
DR   ArrayExpress; Q9D6R2; -.
DR   Bgee; Q9D6R2; -.
DR   CleanEx; MM_IDH3A; -.
DR   Genevestigator; Q9D6R2; -.
DR   GermOnline; ENSMUSG00000032279; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR001804; Isocitrate/isopropylmalate_DH.
DR   InterPro; IPR004434; Isocitrate_DH_NAD.
DR   Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1.
DR   PANTHER; PTHR11835; IDH_IMDH_dimeric; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   TIGRFAMs; TIGR00175; mito_nad_idh; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Direct protein sequencing;
KW   Magnesium; Manganese; Metal-binding; Mitochondrion; NAD;
KW   Oxidoreductase; Transit peptide; Tricarboxylic acid cycle.
FT   TRANSIT       1     27       Mitochondrion (By similarity).
FT   CHAIN        28    366       Isocitrate dehydrogenase [NAD] subunit
FT                                alpha, mitochondrial.
FT                                /FTId=PRO_0000014438.
FT   METAL       233    233       Magnesium or manganese (By similarity).
FT   METAL       257    257       Magnesium or manganese (By similarity).
FT   METAL       261    261       Magnesium or manganese (By similarity).
FT   BINDING     115    115       Substrate (By similarity).
FT   BINDING     125    125       Substrate (By similarity).
FT   BINDING     146    146       Substrate (By similarity).
FT   BINDING     233    233       Substrate (By similarity).
FT   SITE        153    153       Critical for catalysis (By similarity).
FT   SITE        200    200       Critical for catalysis (By similarity).
FT   MOD_RES     343    343       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1     78       Missing (in isoform 2).
FT                                /FTId=VSP_014517.
FT   CONFLICT    306    306       A -> T (in Ref. 1; BAC33199).
SQ   SEQUENCE   366 AA;  39639 MW;  9F1D68C269376955 CRC64;
     MAGSAWVSKV SRLLGAFHNT KQVTRGFAGG VQTVTLIPGD GIGPEISASV MKIFDAAKAP
     IQWEERNVTA IQGPGGKWMI PPEAKESMDK NKMGLKGPLK TPIAAGHPSM NLLLRKTFDL
     YANVRPCVSI EGYKTPYTDV NIVTIRENTE GEYSGIEHVI VDGVVQSIKL ITEEASKRIA
     EFAFEYARNN HRSNVTAVHK ANIMRMSDGL FLQKCREVAE NCKDIKFNEM YLDTVCLNMV
     QDPSQFDVLV MPNLYGDILS DLCAGLIGGL GVTPSGNIGA NGVAIFESVH GTAPDIAGKD
     MANPTALLLS AVMMLRHMGL FDHAAKIEAA CFATIKDGKS LTKDLGGNAK CSDFTEEICR
     RVKDLD
//
ID   CQ059_MOUSE             Reviewed;         360 AA.
AC   Q9D6W8; Q3TE21;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Uncharacterized protein C17orf59 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
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DR   EMBL; AK169875; BAE41427.1; -; mRNA.
DR   EMBL; AK009886; BAB26563.1; -; mRNA.
DR   EMBL; AK151629; BAE30563.1; -; mRNA.
DR   EMBL; AL645902; CAI24443.1; -; Genomic_DNA.
DR   IPI; IPI00461272; -.
DR   RefSeq; NP_082281.2; NM_028005.3.
DR   UniGene; Mm.340257; -.
DR   ProteinModelPortal; Q9D6W8; -.
DR   IntAct; Q9D6W8; 2.
DR   MINT; MINT-218992; -.
DR   STRING; Q9D6W8; -.
DR   PhosphoSite; Q9D6W8; -.
DR   PRIDE; Q9D6W8; -.
DR   Ensembl; ENSMUST00000051888; ENSMUSP00000059143; ENSMUSG00000045176.
DR   GeneID; 71923; -.
DR   KEGG; mmu:71923; -.
DR   UCSC; uc007jpb.1; mouse.
DR   MGI; MGI:1919173; 2310047M10Rik.
DR   GeneTree; ENSGT00490000043453; -.
DR   HOVERGEN; HBG060339; -.
DR   InParanoid; Q9D6W8; -.
DR   OMA; NPAPPEG; -.
DR   OrthoDB; EOG4TXBT6; -.
DR   PhylomeDB; Q9D6W8; -.
DR   NextBio; 334964; -.
DR   ArrayExpress; Q9D6W8; -.
DR   Bgee; Q9D6W8; -.
DR   Genevestigator; Q9D6W8; -.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR019314; DUF2365.
DR   Pfam; PF10157; DUF2365; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    360       Uncharacterized protein C17orf59 homolog.
FT                                /FTId=PRO_0000393961.
FT   COMPBIAS    236    261       Pro-rich.
FT   MOD_RES     130    130       Phosphoserine.
FT   MOD_RES     201    201       Phosphothreonine (By similarity).
FT   MOD_RES     204    204       Phosphoserine (By similarity).
FT   CONFLICT    285    285       L -> V (in Ref. 1; BAE41427).
FT   CONFLICT    300    300       I -> T (in Ref. 1; BAE41427).
SQ   SEQUENCE   360 AA;  38011 MW;  C74C6ED72FF92EB0 CRC64;
     MEAAQGRLGP EPELSVGAEH QAATFSGRPS RTPSKPPSVR TLSGEEEAES VGVSSRHPRA
     SPKTWSGSIA HGPELDTWED KPSSRATPSG ARGRRGVPGS EHAPPPSSWY PEPEPSEDQP
     SALRVCRRGS PGGVEMNVEL PQQEGDDDDD EDEEAAAGRA GRSFPSRLQD SRSLDGLSGA
     CGGGGSSSSG ETGAGGGRRA TISSPLELEG TVSRHGDLTH FVANNLQLKI RLSGAPPPVP
     PASVRPCLTP APTPTIPPID PDVLRDLERL SRELGGRVDR LLRGLGGAVQ ELTALSVGCI
     QTYRDAVDSL GEAVDMSIKG MYTLLARCEE LERALQPVQG LARQVRDIRR TLEVLEALCK
//
ID   GLGB_MOUSE              Reviewed;         702 AA.
AC   Q9D6Y9;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=1,4-alpha-glucan-branching enzyme;
DE            EC=2.4.1.18;
DE   AltName: Full=Brancher enzyme;
DE   AltName: Full=Glycogen-branching enzyme;
GN   Name=Gbe1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Required for sufficient glycogen accumulation. The alpha
CC       1-6 branches of glycogen play an important role in increasing the
CC       solubility of the molecule and, consequently, in reducing the
CC       osmotic pressure within cells (By similarity).
CC   -!- CATALYTIC ACTIVITY: Transfers a segment of a (1->4)-alpha-D-glucan
CC       chain to a primary hydroxy group in a similar glucan chain.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
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DR   EMBL; AK009815; BAB26519.1; -; mRNA.
DR   EMBL; AK050365; BAC34210.1; -; mRNA.
DR   EMBL; BC017541; AAH17541.1; -; mRNA.
DR   IPI; IPI00109823; -.
DR   RefSeq; NP_083079.1; NM_028803.3.
DR   UniGene; Mm.396102; -.
DR   ProteinModelPortal; Q9D6Y9; -.
DR   SMR; Q9D6Y9; 68-699.
DR   STRING; Q9D6Y9; -.
DR   CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   PhosphoSite; Q9D6Y9; -.
DR   PRIDE; Q9D6Y9; -.
DR   Ensembl; ENSMUST00000023393; ENSMUSP00000023393; ENSMUSG00000022707.
DR   GeneID; 74185; -.
DR   KEGG; mmu:74185; -.
DR   UCSC; uc007zqu.1; mouse.
DR   CTD; 74185; -.
DR   MGI; MGI:1921435; Gbe1.
DR   GeneTree; ENSGT00390000017040; -.
DR   HOGENOM; HBG302308; -.
DR   HOVERGEN; HBG051734; -.
DR   InParanoid; Q9D6Y9; -.
DR   OMA; EDWNMGD; -.
DR   OrthoDB; EOG4F1X2K; -.
DR   PhylomeDB; Q9D6Y9; -.
DR   BRENDA; 2.4.1.18; 244.
DR   NextBio; 340028; -.
DR   ArrayExpress; Q9D6Y9; -.
DR   Bgee; Q9D6Y9; -.
DR   CleanEx; MM_GBE1; -.
DR   Genevestigator; Q9D6Y9; -.
DR   GermOnline; ENSMUSG00000022707; Mus musculus.
DR   GO; GO:0003844; F:1,4-alpha-glucan branching enzyme activity; IEA:EC.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR006048; A-amylase_b_C.
DR   InterPro; IPR013780; Glyco_hydro_13_b.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR004193; Glyco_hydro_13_N.
DR   InterPro; IPR013781; Glyco_hydro_sg_catalytic.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   Gene3D; G3DSA:2.60.40.1180; Glyco_hydro_13_b; 1.
DR   Gene3D; G3DSA:3.20.20.80; Glyco_hydro_cat; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   Pfam; PF02922; CBM_48; 1.
DR   SUPFAM; SSF51445; Glyco_hydro_cat; 1.
DR   SUPFAM; SSF81296; Ig_E-set; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Glycogen biosynthesis; Glycogen storage disease;
KW   Glycosyltransferase; Phosphoprotein; Transferase.
FT   CHAIN         1    702       1,4-alpha-glucan-branching enzyme.
FT                                /FTId=PRO_0000188776.
FT   ACT_SITE    251    251       By similarity.
FT   ACT_SITE    286    286       By similarity.
FT   ACT_SITE    291    291       By similarity.
FT   ACT_SITE    355    355       By similarity.
FT   ACT_SITE    357    357       By similarity.
FT   ACT_SITE    412    412       By similarity.
FT   ACT_SITE    480    480       By similarity.
FT   ACT_SITE    481    481       By similarity.
FT   MOD_RES      68     68       N6-acetyllysine (By similarity).
FT   MOD_RES     173    173       Phosphotyrosine (By similarity).
SQ   SEQUENCE   702 AA;  80364 MW;  BE2284A5CED7C060 CRC64;
     MAAPAAPAAG ETGPDARLEA ALADVPELAR LLEIDPYLKP FAADFQRRYK KFSQVLHDIG
     ENEGGIDKFS RGYESFGIHR CSDGGIYCKE WAPGAEGVFL TGEFSGWNPF SHPYKKLEYG
     KWELYIPPKQ NKSPLIPHGS KLKVVITSKS GEILYRISPW AKYVVRENNN VNYDWIHWAP
     EDPYKFKHSR PKKPRSLRIY ESHVGISSHE GKIASYKHFT SNVLPRIKDL GYNCIQLMAI
     MEHAYYASFG YQITSFFAAS SRYGTPEELK ELVDTAHSMG IVVLLDVVHS HASKNSEDGL
     NMFDGTDSCY FHSGPRGTHD LWDSRLFIYS SWEVLRFLLS NIRWWLEEYC FDGFRFDGVT
     SMLYHHHGMG QGFSGDYNEY FGLQVDEDAL IYLMLANHLA HTLYPDSITI AEDVSGMPAL
     CSPTSQGGGG FDYRLAMAIP DKWIQLLKEF KDEDWNMGNI VYTLTNRRYL EKCVAYAESH
     DQALVGDKTL AFWLMDAEMY TNMSVLAPFT PVIDRGIQLH KMIRLITHGL GGEGYLNFMG
     NEFGHPEWLD FPRKGNNESY HYARRQFNLT DDDLLRYKFL NNFDRDMNRL EERCGWLSAP
     QAYVSEKHEA NKTITFERAG LLFIFNFHPS KSYTDYRVGT ATPGKFKIVL DSDAAEYGGH
     QRLDHNTNYF AEAFEHNGRP YSLLVYIPSR VALILQNVDL QN
//
ID   NOP56_MOUSE             Reviewed;         580 AA.
AC   Q9D6Z1; Q3UD45; Q8BVL1; Q8VDT2; Q99LT8; Q9CT15;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2003, sequence version 2.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Nucleolar protein 56;
DE   AltName: Full=Nucleolar protein 5A;
GN   Name=Nop56; Synonyms=Nol5a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, Thymus, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513 AND SER-536, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513; SER-536 AND
RP   THR-545, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; THR-467; SER-529;
RP   SER-536 AND SER-543, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513 AND SER-536, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513; SER-536 AND
RP   SER-554, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513; SER-536 AND
RP   SER-554, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513; SER-536 AND
RP   SER-543, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Required for 60S ribosomal subunit biogenesis (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity).
CC   -!- SIMILARITY: Belongs to the NOP5/NOP56 family.
CC   -!- SIMILARITY: Contains 1 Nop domain.
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DR   EMBL; AK009799; BAB26511.1; -; mRNA.
DR   EMBL; AK011481; BAB27647.3; -; mRNA.
DR   EMBL; AK077795; BAC37015.1; -; mRNA.
DR   EMBL; AK150258; BAE29417.1; -; mRNA.
DR   EMBL; BC002231; AAH02231.1; -; mRNA.
DR   EMBL; BC021355; AAH21355.1; -; mRNA.
DR   IPI; IPI00318048; -.
DR   RefSeq; NP_077155.2; NM_024193.2.
DR   UniGene; Mm.29363; -.
DR   ProteinModelPortal; Q9D6Z1; -.
DR   SMR; Q9D6Z1; 3-410.
DR   STRING; Q9D6Z1; -.
DR   PhosphoSite; Q9D6Z1; -.
DR   PRIDE; Q9D6Z1; -.
DR   Ensembl; ENSMUST00000103198; ENSMUSP00000099487; ENSMUSG00000027405.
DR   GeneID; 67134; -.
DR   KEGG; mmu:67134; -.
DR   UCSC; uc008mil.1; mouse.
DR   CTD; 67134; -.
DR   MGI; MGI:1914384; Nop56.
DR   GeneTree; ENSGT00550000075068; -.
DR   HOGENOM; HBG611715; -.
DR   InParanoid; Q9D6Z1; -.
DR   OMA; FEHAAGY; -.
DR   OrthoDB; EOG41G342; -.
DR   PhylomeDB; Q9D6Z1; -.
DR   NextBio; 323680; -.
DR   Bgee; Q9D6Z1; -.
DR   CleanEx; MM_NOL5A; -.
DR   Genevestigator; Q9D6Z1; -.
DR   GermOnline; ENSMUSG00000027405; Mus musculus.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR012974; NOP5_N.
DR   InterPro; IPR012976; NOSIC.
DR   InterPro; IPR002687; SnoRNA-bd_dom.
DR   Pfam; PF01798; Nop; 1.
DR   Pfam; PF08156; NOP5NT; 1.
DR   Pfam; PF08060; NOSIC; 1.
DR   SMART; SM00931; NOSIC; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Ribosome biogenesis.
FT   CHAIN         1    580       Nucleolar protein 56.
FT                                /FTId=PRO_0000219027.
FT   DOMAIN      263    411       Nop.
FT   COMPBIAS    438    576       Lys-rich.
FT   MOD_RES     406    406       Phosphoserine (By similarity).
FT   MOD_RES     466    466       Phosphoserine.
FT   MOD_RES     467    467       Phosphothreonine.
FT   MOD_RES     513    513       Phosphoserine.
FT   MOD_RES     529    529       Phosphoserine.
FT   MOD_RES     536    536       Phosphoserine.
FT   MOD_RES     543    543       Phosphoserine.
FT   MOD_RES     545    545       Phosphothreonine.
FT   MOD_RES     554    554       Phosphoserine.
FT   MOD_RES     566    566       Phosphoserine (By similarity).
FT   CONFLICT    170    170       Q -> K (in Ref. 1; BAC37015).
FT   CONFLICT    182    182       I -> V (in Ref. 1; BAB27647).
FT   CONFLICT    436    436       T -> A (in Ref. 2; AAH21355).
SQ   SEQUENCE   580 AA;  64464 MW;  60AA1D43E349ADD7 CRC64;
     MVLLHVLFEH AVGYALLALK EVEEISLLLP QVEECVLNLG KFHNVVRLVA FCPFSSSQVA
     LENANAVSEG VVHEDLRLLL ETYLPSKKKK VLLGVGDPKI GAAIQEELGY NCQTGGVIAE
     ILRGVRLHFH NLVKGLTDLS ACKAQLGLGH SYSRAKVKFN VNRVDNMIIQ SISLLDQLDK
     DINTFSMRVR EWYGYHFPEL VKIVNDNATY CRLAQFIGNR RELNEEKLEK LEEITMDGAK
     AKAILDASRS SMGMDISAID LINIESFSSR VVSLSEYRQS LHTYLRSKMS QVAPSLSALI
     GEAVGARLIA HAGSLTNLAK YPASTVQILG AEKALFRALK TRGNTPKYGL IFHSTFIGRA
     AAKNKGRISR YLANKCSIAS RIDCFSEVPT SVFGEKLREQ VEERLSFYET GEIPRKNLDV
     MKEAVVQAEE AAAEITRKLE KQEKKRLKKE KKRLAALALA SSENSSTPEE CEEVNEKSKK
     KKKLKPQENG MEDPPVSLPK SKKKKAPKEE LASDLEEMAT SSAKRKKSSP KEEVASEPEE
     AASPTTPKKK RKFSEEPEVA ANFTKSSTKK KKKSQKAQED
//
ID   DUS26_MOUSE             Reviewed;         211 AA.
AC   Q9D700; Q8VCZ5;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 2.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Dual specificity protein phosphatase 26;
DE            EC=3.1.3.16;
DE            EC=3.1.3.48;
DE   AltName: Full=Dual specificity phosphatase SKRP3;
GN   Name=Dusp26; Synonyms=Skrp3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Zama T., Aoki R., Murata M., Ikeda Y.;
RT   "Identification of a novel dual specificity phosphatase, SKRP3.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=16581800; DOI=10.1128/MCB.26.8.3282-3294.2006;
RA   Hu Y., Mivechi N.F.;
RT   "Association and regulation of heat shock transcription factor 4b with
RT   both extracellular signal-regulated kinase mitogen-activated protein
RT   kinase and dual-specificity tyrosine phosphatase DUSP26.";
RL   Mol. Cell. Biol. 26:3282-3294(2006).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=17001450; DOI=10.1007/s11010-006-9313-5;
RA   Takagaki K., Shima H., Tanuma N., Nomura M., Satoh T., Watanabe M.,
RA   Kikuchi K.;
RT   "Characterization of a novel low-molecular-mass dual specificity
RT   phosphatase-4 (LDP-4) expressed in brain.";
RL   Mol. Cell. Biochem. 296:177-184(2007).
CC   -!- FUNCTION: Inactivates MAPK1 and MAPK3 which leads to
CC       dephosphorylation of heat shock factor protein 4 and a reduction
CC       in its DNA-binding activity (By similarity).
CC   -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate.
CC   -!- CATALYTIC ACTIVITY: A phosphoprotein + H(2)O = a protein +
CC       phosphate.
CC   -!- SUBUNIT: Interacts with HSF4 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Golgi apparatus (By similarity).
CC   -!- TISSUE SPECIFICITY: Brain and skeletal muscle. In the brain it is
CC       expressed ubiquitously except in the hippocampus.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class dual specificity subfamily.
CC   -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain.
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DR   EMBL; AB104416; BAD91016.1; -; mRNA.
DR   EMBL; AK009781; BAB26501.2; -; mRNA.
DR   EMBL; BC018204; AAH18204.1; -; mRNA.
DR   IPI; IPI00122779; -.
DR   RefSeq; NP_080145.1; NM_025869.3.
DR   UniGene; Mm.23916; -.
DR   HSSP; P51452; 1VHR.
DR   ProteinModelPortal; Q9D700; -.
DR   SMR; Q9D700; 61-210.
DR   STRING; Q9D700; -.
DR   PRIDE; Q9D700; -.
DR   Ensembl; ENSMUST00000036631; ENSMUSP00000046794; ENSMUSG00000039661.
DR   GeneID; 66959; -.
DR   KEGG; mmu:66959; -.
DR   UCSC; uc009ljb.1; mouse.
DR   CTD; 66959; -.
DR   MGI; MGI:1914209; Dusp26.
DR   eggNOG; roNOG15864; -.
DR   GeneTree; ENSGT00550000074474; -.
DR   HOGENOM; HBG717377; -.
DR   HOVERGEN; HBG001524; -.
DR   InParanoid; Q9D700; -.
DR   OMA; SKWRGGA; -.
DR   OrthoDB; EOG4BCDP2; -.
DR   PhylomeDB; Q9D700; -.
DR   BRENDA; 3.1.3.16; 244.
DR   BRENDA; 3.1.3.48; 244.
DR   NextBio; 323124; -.
DR   ArrayExpress; Q9D700; -.
DR   Bgee; Q9D700; -.
DR   CleanEx; MM_DUSP26; -.
DR   Genevestigator; Q9D700; -.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
DR   GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IEA:InterPro.
DR   GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR   InterPro; IPR020417; Dual-sp_phosphatase.
DR   InterPro; IPR000340; Dual-sp_phosphatase_cat-dom.
DR   InterPro; IPR020405; Dual-sp_phosphatase_famA.
DR   InterPro; IPR020422; Dual-sp_phosphatase_subgr_cat.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   Pfam; PF00782; DSPc; 1.
DR   PRINTS; PR01908; ADSPHPHTASE.
DR   PRINTS; PR01909; ADSPHPHTASEA.
DR   SMART; SM00195; DSPc; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Golgi apparatus; Hydrolase; Nucleus; Protein phosphatase.
FT   CHAIN         1    211       Dual specificity protein phosphatase 26.
FT                                /FTId=PRO_0000292220.
FT   DOMAIN       61    206       Tyrosine-protein phosphatase.
FT   ACT_SITE    152    152       Phosphocysteine intermediate (By
FT                                similarity).
SQ   SEQUENCE   211 AA;  23946 MW;  952A6C7561E9B046 CRC64;
     MCPGNWLWAS MTFMARFSRG SSRSPVRTRG SLEEMPSVHH PFLNVFELER LLYTGKTACN
     HADEVWPGLY LGDQDMANNR RELRRLGITH VLNASHNRWR GTPEAYEGLG IRYLGVEAHD
     SPAFDMSIHF QTAADFIHRA LSQPGGKILV HCAVGVSRSA TLVLAYLMLY HHFTLVEAIK
     KVKDHRGITP NRGFLRQLLA LDRRLRQGLE A
//
ID   TMX2_MOUSE              Reviewed;         295 AA.
AC   Q9D710; Q8BW13;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Thioredoxin-related transmembrane protein 2;
DE   AltName: Full=Thioredoxin domain-containing protein 14;
DE   Flags: Precursor;
GN   Name=Tmx2; Synonyms=Txndc14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Mammary gland, Testis, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N, and NMRI; TISSUE=Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- DOMAIN: The thioredoxin domain lacks the 2 redox-active cysteines,
CC       suggesting that it lacks thioredoxin activity (By similarity).
CC   -!- DOMAIN: The di-lysine motif confers endoplasmic reticulum
CC       localization for type I membrane proteins (By similarity).
CC   -!- SIMILARITY: Contains 1 thioredoxin domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK009759; BAB26483.1; -; mRNA.
DR   EMBL; AK075750; BAC35930.1; -; mRNA.
DR   EMBL; AK145245; BAE26323.1; -; mRNA.
DR   EMBL; AK170587; BAE41896.1; -; mRNA.
DR   EMBL; BC013544; AAH13544.1; -; mRNA.
DR   EMBL; BC110994; AAI10995.1; -; mRNA.
DR   IPI; IPI00459309; -.
DR   RefSeq; NP_080144.1; NM_025868.3.
DR   UniGene; Mm.239765; -.
DR   UniGene; Mm.371621; -.
DR   HSSP; P10599; 1M7T.
DR   ProteinModelPortal; Q9D710; -.
DR   SMR; Q9D710; 137-260.
DR   PhosphoSite; Q9D710; -.
DR   PRIDE; Q9D710; -.
DR   Ensembl; ENSMUST00000053664; ENSMUSP00000059582; ENSMUSG00000050043.
DR   Ensembl; ENSMUST00000111665; ENSMUSP00000107294; ENSMUSG00000050043.
DR   GeneID; 66958; -.
DR   KEGG; mmu:66958; -.
DR   UCSC; uc008kix.1; mouse.
DR   CTD; 66958; -.
DR   MGI; MGI:1914208; Tmx2.
DR   eggNOG; maNOG12620; -.
DR   GeneTree; ENSGT00390000003751; -.
DR   InParanoid; Q9D710; -.
DR   OMA; EQHVGNI; -.
DR   OrthoDB; EOG47SSF8; -.
DR   NextBio; 461954; -.
DR   Bgee; Q9D710; -.
DR   CleanEx; MM_TXNDC14; -.
DR   Genevestigator; Q9D710; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   InterPro; IPR017936; Thioredoxin-like.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; FALSE_NEG.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Phosphoprotein; Signal; Transmembrane; Transmembrane helix.
FT   CHAIN         1    295       Thioredoxin-related transmembrane protein
FT                                2.
FT                                /FTId=PRO_0000315754.
FT   SIGNAL        1     48       Potential.
FT   TOPO_DOM     49    102       Extracellular (Potential).
FT   TRANSMEM    103    125       Helical; (Potential).
FT   TOPO_DOM    126    295       Cytoplasmic (Potential).
FT   DOMAIN      114    269       Thioredoxin.
FT   MOTIF       292    295       Di-lysine motif.
FT   MOD_RES     243    243       Phosphoserine (By similarity).
FT   CONFLICT    247    247       S -> F (in Ref. 1; BAC35930).
FT   CONFLICT    294    294       D -> V (in Ref. 1; BAC35930).
SQ   SEQUENCE   295 AA;  33943 MW;  25E4477F7BB17E3C CRC64;
     MAVLAPLIAL VYSVPRLSRW LARPYCLLSA LLSIAFLLVR KLPPICNGLP TQREDGNPCD
     FDWREVEILM FLSAIVMMKN RRSITVEQHV GNIFMFSKVA NAILFFRLDI RMGLLYLTLC
     IVFLMTCKPP LYMGPEYIKY FNDKTIDEEL ERDKRVTWIV EFFANWSNDC QSFAPIYADL
     SLKYNCSGLN FGKVDVGRYT DVSTRYKVST SPLTRQLPTL ILFQGGKEVI RRPQIDKKGR
     AVSWTFSEEN VIREFNLNEL YQRAKKHSKG GDMSEEKPVD PAPTTVPDGE NKKDK
//
ID   ARMC1_MOUSE             Reviewed;         282 AA.
AC   Q9D7A8; Q8CBW1;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Armadillo repeat-containing protein 1;
GN   Name=Armc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Placenta, Tongue, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Contains 1 ARM repeat.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK009402; BAB26266.1; -; mRNA.
DR   EMBL; AK034483; BAC28724.1; -; mRNA.
DR   EMBL; AK079299; BAC37600.1; -; mRNA.
DR   EMBL; AK082783; BAC38617.1; -; mRNA.
DR   EMBL; AK144184; BAE25753.1; -; mRNA.
DR   EMBL; AK145993; BAE26814.1; -; mRNA.
DR   EMBL; AK167233; BAE39357.1; -; mRNA.
DR   EMBL; BC021451; AAH21451.1; -; mRNA.
DR   EMBL; BC051067; AAH51067.1; -; mRNA.
DR   IPI; IPI00110100; -.
DR   RefSeq; NP_083116.1; NM_028840.2.
DR   UniGene; Mm.200383; -.
DR   UniGene; Mm.316007; -.
DR   ProteinModelPortal; Q9D7A8; -.
DR   SMR; Q9D7A8; 144-205.
DR   STRING; Q9D7A8; -.
DR   PhosphoSite; Q9D7A8; -.
DR   PRIDE; Q9D7A8; -.
DR   Ensembl; ENSMUST00000029125; ENSMUSP00000029125; ENSMUSG00000027599.
DR   GeneID; 74252; -.
DR   KEGG; mmu:74252; -.
DR   UCSC; uc008oro.1; mouse.
DR   CTD; 74252; -.
DR   MGI; MGI:1921502; Armc1.
DR   eggNOG; roNOG07663; -.
DR   GeneTree; ENSGT00390000014100; -.
DR   HOGENOM; HBG713829; -.
DR   HOVERGEN; HBG055281; -.
DR   InParanoid; Q9D7A8; -.
DR   OMA; EVEQNTD; -.
DR   OrthoDB; EOG48KRBS; -.
DR   PhylomeDB; Q9D7A8; -.
DR   NextBio; 340246; -.
DR   ArrayExpress; Q9D7A8; -.
DR   Bgee; Q9D7A8; -.
DR   CleanEx; MM_ARMC1; -.
DR   Genevestigator; Q9D7A8; -.
DR   GermOnline; ENSMUSG00000027599; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0030001; P:metal ion transport; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR006121; HeavyMe_transpt.
DR   InterPro; IPR016617; UCP013899_metal-bd.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF00514; Arm; 1.
DR   PIRSF; PIRSF013899; UCP013899; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF55008; HeavyMe_transpt; 1.
DR   PROSITE; PS50176; ARM_REPEAT; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Phosphoprotein.
FT   CHAIN         1    282       Armadillo repeat-containing protein 1.
FT                                /FTId=PRO_0000240883.
FT   REPEAT       39     81       ARM.
FT   MOD_RES     260    260       Phosphoserine (By similarity).
FT   CONFLICT    135    135       L -> W (in Ref. 1; BAC28724).
SQ   SEQUENCE   282 AA;  31247 MW;  F92D73386FA531BF CRC64;
     MNSSSSTMNE EPDALSVVNQ LRDLAADPLN RRAIVQDQGC LPGLILFMDH PNPPVVHSAL
     LALRYLAECR ANREKMKGEL GMMLSLQNVI QKTTTPGETK LLASEIYDIL QSSNLADGDS
     FNEMNSRRRK AQFFLGTTNK RAKTVVLHID GLDDTSRRNL CEEALLKIKG VISFTFQMAV
     QRCVVRIRSD LKAEALASAI ASTKVMKAQQ VVKSESGEEM LVPFQDAPVE VEENTELPDY
     LPEDESPTKE QDKAVSRVGS HPEGGASWLS TAANFLSRSF YW
//
ID   ISCU_MOUSE              Reviewed;         168 AA.
AC   Q9D7P6; Q4VBC7; Q8K344;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Iron-sulfur cluster assembly enzyme ISCU, mitochondrial;
DE   AltName: Full=NifU-like N-terminal domain-containing protein;
DE   AltName: Full=NifU-like protein;
DE   Flags: Precursor;
GN   Name=Iscu; Synonyms=Nifun;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, Thymus, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary gland, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   STRUCTURE BY NMR OF 45-161.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of iron-sulfur cluster protein (ISCU).";
RL   Submitted (NOV-2004) to the PDB data bank.
CC   -!- FUNCTION: Involved in the assembly or repair of [Fe-S] clusters
CC       that are present in iron-sulfur proteins. Binds iron (By
CC       similarity).
CC   -!- SUBUNIT: Binds NFS1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the nifU family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK009021; BAB26031.1; -; mRNA.
DR   EMBL; AK039834; BAC30464.1; -; mRNA.
DR   EMBL; AK083247; BAC38830.1; -; mRNA.
DR   EMBL; BC028800; AAH28800.1; -; mRNA.
DR   EMBL; BC048409; AAH48409.1; -; mRNA.
DR   EMBL; BC096049; AAH96049.1; -; mRNA.
DR   IPI; IPI00110578; -.
DR   RefSeq; NP_079802.1; NM_025526.4.
DR   UniGene; Mm.29497; -.
DR   PDB; 1WFZ; NMR; -; A=45-161.
DR   PDBsum; 1WFZ; -.
DR   ProteinModelPortal; Q9D7P6; -.
DR   SMR; Q9D7P6; 45-161.
DR   STRING; Q9D7P6; -.
DR   PhosphoSite; Q9D7P6; -.
DR   PRIDE; Q9D7P6; -.
DR   Ensembl; ENSMUST00000026937; ENSMUSP00000026937; ENSMUSG00000025825.
DR   GeneID; 66383; -.
DR   KEGG; mmu:66383; -.
DR   NMPDR; fig|10090.3.peg.12212; -.
DR   UCSC; uc008yyp.1; mouse.
DR   CTD; 66383; -.
DR   MGI; MGI:1913633; Iscu.
DR   eggNOG; roNOG15736; -.
DR   GeneTree; ENSGT00390000015813; -.
DR   HOVERGEN; HBG052621; -.
DR   OMA; FTNPRNV; -.
DR   OrthoDB; EOG4SJ5G2; -.
DR   PhylomeDB; Q9D7P6; -.
DR   NextBio; 321509; -.
DR   Bgee; Q9D7P6; -.
DR   Genevestigator; Q9D7P6; -.
DR   GermOnline; ENSMUSG00000025825; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR   InterPro; IPR011339; ISC_FeS_clus_asmbl_IscU.
DR   InterPro; IPR002871; NIF_FeS_clus_asmbl_NifU_N.
DR   PANTHER; PTHR10093; NIF_FeS_clus_asmbl_NifU_N; 1.
DR   Pfam; PF01592; NifU_N; 1.
DR   TIGRFAMs; TIGR01999; iscU; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Iron; Metal-binding; Mitochondrion; Phosphoprotein;
KW   Transit peptide.
FT   TRANSIT       1     35       Mitochondrion (Potential).
FT   CHAIN        36    168       Iron-sulfur cluster assembly enzyme ISCU,
FT                                mitochondrial.
FT                                /FTId=PRO_0000019693.
FT   MOD_RES      15     15       Phosphoserine (By similarity).
FT   STRAND       58     67
FT   TURN         68     71
FT   STRAND       72     80
FT   STRAND       82     92
FT   HELIX        97    110
FT   HELIX       115    120
FT   HELIX       123    130
FT   HELIX       134    136
FT   HELIX       137    159
SQ   SEQUENCE   168 AA;  18098 MW;  06B6350434FEAAF6 CRC64;
     MAAATGAGRL RRAASALLLR SPRLPARELS APARLYHKKV VDHYENPRNV GSLDKTSKNV
     GTGLVGAPAC GDVMKLQIQV DEKGKIVDAR FKTFGCGSAI ASSSLATEWV KGKTVEEALT
     IKNTDIAKEL CLPPVKLHCS MLAEDAIKAA LADYKLKQES KKEEPEKQ
//
ID   RL22L_MOUSE             Reviewed;         122 AA.
AC   Q9D7S7; Q9CXU8;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=60S ribosomal protein L22-like 1;
GN   Name=Rpl22l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND SER-120, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND SER-120, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND SER-120, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9D7S7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D7S7-2; Sequence=VSP_019380;
CC   -!- SIMILARITY: Belongs to the ribosomal protein L22e family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK008915; BAB25965.1; -; mRNA.
DR   EMBL; AK013966; BAB29090.1; -; mRNA.
DR   EMBL; BC026533; AAH26533.1; -; mRNA.
DR   IPI; IPI00110724; -.
DR   IPI; IPI00762362; -.
DR   RefSeq; NP_080793.1; NM_026517.2.
DR   UniGene; Mm.371630; -.
DR   ProteinModelPortal; Q9D7S7; -.
DR   SMR; Q9D7S7; 8-111.
DR   STRING; Q9D7S7; -.
DR   PhosphoSite; Q9D7S7; -.
DR   PRIDE; Q9D7S7; -.
DR   Ensembl; ENSMUST00000043867; ENSMUSP00000043111; ENSMUSG00000039221.
DR   GeneID; 68028; -.
DR   KEGG; mmu:68028; -.
DR   UCSC; uc008ouf.1; mouse.
DR   UCSC; uc008oug.1; mouse.
DR   CTD; 68028; -.
DR   MGI; MGI:1915278; Rpl22l1.
DR   GeneTree; ENSGT00390000003719; -.
DR   HOGENOM; HBG716459; -.
DR   HOVERGEN; HBG004373; -.
DR   InParanoid; Q9D7S7; -.
DR   OMA; FTLDLTH; -.
DR   OrthoDB; EOG4BRWNB; -.
DR   PhylomeDB; Q9D7S7; -.
DR   NextBio; 326242; -.
DR   ArrayExpress; Q9D7S7; -.
DR   Bgee; Q9D7S7; -.
DR   CleanEx; MM_RPL22L1; -.
DR   Genevestigator; Q9D7S7; -.
DR   GermOnline; ENSMUSG00000039221; Mus musculus.
DR   GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR002671; Ribosomal_L22e.
DR   PANTHER; PTHR10064; Ribosomal_L22e; 1.
DR   Pfam; PF01776; Ribosomal_L22e; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein; Ribonucleoprotein;
KW   Ribosomal protein.
FT   CHAIN         1    122       60S ribosomal protein L22-like 1.
FT                                /FTId=PRO_0000240633.
FT   MOD_RES     118    118       Phosphoserine.
FT   MOD_RES     120    120       Phosphoserine.
FT   VAR_SEQ       4      4       Missing (in isoform 2).
FT                                /FTId=VSP_019380.
SQ   SEQUENCE   122 AA;  14467 MW;  2B536FF82D32A1D3 CRC64;
     MAPQKDKKPK KSTWRFHLDL THPVEDGIFD SGNFEQFLRE KVKVNGKTGN LGNVVHIERL
     KNKITVVSEK QFSKRYLKYL TKKYLKKNNL RDWLRVVASD KETYELRYFQ ISQDEDGSES
     ED
//
ID   LYSM2_MOUSE             Reviewed;         215 AA.
AC   Q9D7V2; Q80ZR2;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 2.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=LysM and putative peptidoglycan-binding domain-containing protein 2;
GN   Name=Lysmd2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9D7V2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D7V2-2; Sequence=VSP_020124;
CC   -!- SIMILARITY: Contains 1 LysM repeat.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK008800; BAB25902.1; -; mRNA.
DR   EMBL; BC048545; AAH48545.1; -; mRNA.
DR   IPI; IPI00110862; -.
DR   IPI; IPI00785357; -.
DR   UniGene; Mm.19119; -.
DR   ProteinModelPortal; Q9D7V2; -.
DR   SMR; Q9D7V2; 66-126.
DR   PhosphoSite; Q9D7V2; -.
DR   PRIDE; Q9D7V2; -.
DR   Ensembl; ENSMUST00000034702; ENSMUSP00000034702; ENSMUSG00000032184.
DR   UCSC; uc009qsq.1; mouse.
DR   UCSC; uc009qsr.1; mouse.
DR   MGI; MGI:1917332; Lysmd2.
DR   eggNOG; roNOG17089; -.
DR   GeneTree; ENSGT00520000055632; -.
DR   HOGENOM; HBG716662; -.
DR   HOVERGEN; HBG079723; -.
DR   InParanoid; Q9D7V2; -.
DR   OrthoDB; EOG4F4SC5; -.
DR   ArrayExpress; Q9D7V2; -.
DR   Bgee; Q9D7V2; -.
DR   Genevestigator; Q9D7V2; -.
DR   GermOnline; ENSMUSG00000032184; Mus musculus.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   InterPro; IPR018392; Peptidoglycan-bd_lysin.
DR   InterPro; IPR002482; Peptidoglycan-bd_Lysin_sg.
DR   Pfam; PF01476; LysM; 1.
DR   SMART; SM00257; LysM; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    215       LysM and putative peptidoglycan-binding
FT                                domain-containing protein 2.
FT                                /FTId=PRO_0000248003.
FT   REPEAT       73    116       LysM.
FT   MOD_RES      33     33       Phosphoserine (By similarity).
FT   MOD_RES     208    208       Phosphotyrosine (By similarity).
FT   MOD_RES     213    213       Phosphotyrosine (By similarity).
FT   VAR_SEQ       1     91       Missing (in isoform 2).
FT                                /FTId=VSP_020124.
FT   CONFLICT    103    106       TNDC -> NNER (in Ref. 1; BAB25902).
FT   CONFLICT    143    143       F -> L (in Ref. 1; BAB25902).
FT   CONFLICT    148    148       E -> D (in Ref. 1; BAB25902).
FT   CONFLICT    165    165       D -> E (in Ref. 1; BAB25902).
FT   CONFLICT    171    171       P -> L (in Ref. 1; BAB25902).
FT   CONFLICT    181    181       Q -> H (in Ref. 1; BAB25902).
FT   CONFLICT    196    196       K -> E (in Ref. 1; BAB25902).
SQ   SEQUENCE   215 AA;  23694 MW;  1CB7CEAC83F12276 CRC64;
     MADLSPAPAL REGGPRAHRP SAPSPPPRSR STSEPEEAEL SLSLARTKTR SYGSTASVRA
     PLGARVIERH VEHRVRAGDT LQGIALKYGV TMEQIKRANK LFTNDCIFLK KTLSIPILSE
     KPLLFNGLNS IDSPESETVD SSFCQEEEPV VSEEELPPPS PQDPDPKPAQ PEEVSARDFL
     QRLDLQIKLS TQAARKLKEE SRDEESPYAA SLYHS
//
ID   GGCT_MOUSE              Reviewed;         188 AA.
AC   Q9D7X8; Q3URJ2; Q66JQ5;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Gamma-glutamylcyclotransferase;
DE            EC=2.3.2.4;
GN   Name=Ggct;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver, Skin, Spinal cord, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Catalyzes the formation of 5-oxoproline from gamma-
CC       glutamyl dipeptides and may play a significant role in glutathione
CC       homeostasis. Induces release of cytochrome c from mitochondria
CC       with resultant induction of apoptosis (By similarity).
CC   -!- CATALYTIC ACTIVITY: (Gamma-L-glutamyl)-L-amino acid = 5-oxoproline
CC       + L-amino acid.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK008719; BAB25854.1; -; mRNA.
DR   EMBL; AK050049; BAC34049.1; -; mRNA.
DR   EMBL; AK079465; BAC37656.1; -; mRNA.
DR   EMBL; AK141474; BAE24696.1; -; mRNA.
DR   EMBL; CH466597; EDK98717.1; -; Genomic_DNA.
DR   EMBL; BC080818; AAH80818.1; -; mRNA.
DR   IPI; IPI00111004; -.
DR   RefSeq; NP_080913.1; NM_026637.3.
DR   UniGene; Mm.294708; -.
DR   ProteinModelPortal; Q9D7X8; -.
DR   SMR; Q9D7X8; 15-183.
DR   STRING; Q9D7X8; -.
DR   PhosphoSite; Q9D7X8; -.
DR   REPRODUCTION-2DPAGE; Q66JQ5; -.
DR   REPRODUCTION-2DPAGE; Q9D7X8; -.
DR   PRIDE; Q9D7X8; -.
DR   Ensembl; ENSMUST00000131475; ENSMUSP00000120154; ENSMUSG00000002797.
DR   GeneID; 110175; -.
DR   KEGG; mmu:110175; -.
DR   UCSC; uc009cah.1; mouse.
DR   CTD; 110175; -.
DR   MGI; MGI:95700; Ggct.
DR   eggNOG; roNOG13267; -.
DR   GeneTree; ENSGT00500000044921; -.
DR   HOGENOM; HBG542988; -.
DR   HOVERGEN; HBG050922; -.
DR   InParanoid; Q9D7X8; -.
DR   OMA; DFGNFQG; -.
DR   OrthoDB; EOG4907B2; -.
DR   PhylomeDB; Q9D7X8; -.
DR   NextBio; 326834; -.
DR   ArrayExpress; Q9D7X8; -.
DR   Bgee; Q9D7X8; -.
DR   CleanEx; MM_A030007L17RIK; -.
DR   Genevestigator; Q9D7X8; -.
DR   GermOnline; ENSMUSG00000002797; Mus musculus.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0008415; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003839; F:gamma-glutamylcyclotransferase activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0001836; P:release of cytochrome c from mitochondria; ISS:UniProtKB.
DR   InterPro; IPR009288; AIG2-like.
DR   InterPro; IPR013024; Butirosin_synth_BtrG-like.
DR   InterPro; IPR017939; G-Glutamylcylcotransferase.
DR   Gene3D; G3DSA:3.10.490.10; Butirosin_synth_BtrG-like; 1.
DR   PANTHER; PTHR12935; G-Glutamylcylcotransferase; 1.
DR   Pfam; PF06094; AIG2; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Transferase.
FT   CHAIN         1    188       Gamma-glutamylcyclotransferase.
FT                                /FTId=PRO_0000089581.
FT   REGION       19     22       Substrate binding (By similarity).
FT   ACT_SITE     98     98       Proton acceptor (By similarity).
FT   CONFLICT     45     45       R -> C (in Ref. 2; EDK98717 and 3;
FT                                AAH80818).
SQ   SEQUENCE   188 AA;  21166 MW;  E03657B103BA7421 CRC64;
     MASSDCEGHA GQEGETFLYF AYGSNLLTER IHLRNPSAVF CCVARLQDFK LDFGNFQGKM
     SERWHGGIAT IFQSPGDEVW GVVWRMNKSN ISSLDEQEGV KSGVYVVIEI KVSTREGKEI
     TCRSYLMTNY ESAPPSPQYK KVICMGAKEN GLPQEYQEKL KAIEPNEYKG KISDEMEDII
     KKGESKLS
//
ID   FIP1_MOUSE              Reviewed;         581 AA.
AC   Q9D824; Q8BWX7; Q99LH0; Q9DBB2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Pre-mRNA 3'-end-processing factor FIP1;
DE   AltName: Full=FIP1-like 1 protein;
GN   Name=Fip1l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-558 (ISOFORM 3).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryonic spinal cord, Liver, and Small intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479; THR-481; SER-483
RP   AND SER-487, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; SER-88 AND SER-479,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280 AND SER-479, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Component of the cleavage and polyadenylation
CC       specificity factor (CPSF) complex that plays a key role in pre-
CC       mRNA 3'-end formation, recognizing the AAUAAA signal sequence and
CC       interacting with poly(A) polymerase and other factors to bring
CC       about cleavage and poly(A) addition. FIP1L1 contributes to poly(A)
CC       site recognition and stimulates poly(A) addition. Binds to U-rich
CC       RNA sequence elements surrounding the poly(A) site. May act to
CC       tether poly(A) polymerase to the CPSF complex (By similarity).
CC   -!- SUBUNIT: Component of the cleavage and polyadenylation specificity
CC       factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and
CC       FIP1L1. Found in a complex with CPSF1, FIP1L1 and PAPOLA.
CC       Interacts with CPSF1, CPSF4, CSTF2, CSTF3 and PAPOLA (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9D824-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D824-2; Sequence=VSP_016734;
CC       Name=3;
CC         IsoId=Q9D824-3; Sequence=VSP_016734, VSP_016735;
CC       Name=4;
CC         IsoId=Q9D824-4; Sequence=VSP_016733, VSP_016735, VSP_016736;
CC   -!- SIMILARITY: Belongs to the FIP1 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK005061; BAB23785.1; -; mRNA.
DR   EMBL; AK008561; BAB25745.1; -; mRNA.
DR   EMBL; AK049672; BAC33867.1; -; mRNA.
DR   EMBL; AK164105; BAE37629.1; -; mRNA.
DR   EMBL; BC003263; AAH03263.1; -; mRNA.
DR   IPI; IPI00110716; -.
DR   IPI; IPI00116897; -.
DR   IPI; IPI00119501; -.
DR   IPI; IPI00667065; -.
DR   RefSeq; NP_001153045.1; NM_001159573.1.
DR   RefSeq; NP_001153046.1; NM_001159574.1.
DR   RefSeq; NP_077145.2; NM_024183.5.
DR   UniGene; Mm.272468; -.
DR   STRING; Q9D824; -.
DR   PhosphoSite; Q9D824; -.
DR   PRIDE; Q9D824; -.
DR   Ensembl; ENSMUST00000080164; ENSMUSP00000079059; ENSMUSG00000029227.
DR   Ensembl; ENSMUST00000113534; ENSMUSP00000109162; ENSMUSG00000029227.
DR   Ensembl; ENSMUST00000113535; ENSMUSP00000109163; ENSMUSG00000029227.
DR   Ensembl; ENSMUST00000113536; ENSMUSP00000109164; ENSMUSG00000029227.
DR   GeneID; 66899; -.
DR   KEGG; mmu:66899; -.
DR   UCSC; uc008xtm.1; mouse.
DR   UCSC; uc008xtn.1; mouse.
DR   UCSC; uc008xto.1; mouse.
DR   UCSC; uc008xtp.1; mouse.
DR   CTD; 66899; -.
DR   MGI; MGI:1914149; Fip1l1.
DR   eggNOG; roNOG06125; -.
DR   GeneTree; ENSGT00600000084416; -.
DR   HOVERGEN; HBG059889; -.
DR   OMA; HDSEEGD; -.
DR   OrthoDB; EOG4S4PGB; -.
DR   PhylomeDB; Q9D824; -.
DR   NextBio; 322965; -.
DR   ArrayExpress; Q9D824; -.
DR   Bgee; Q9D824; -.
DR   CleanEx; MM_FIP1L1; -.
DR   Genevestigator; Q9D824; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR007854; Fip1.
DR   Pfam; PF05182; Fip1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; mRNA processing; Nucleus;
KW   Phosphoprotein; RNA-binding.
FT   CHAIN         1    581       Pre-mRNA 3'-end-processing factor FIP1.
FT                                /FTId=PRO_0000215038.
FT   REGION        1    332       Necessary for stimulating PAPOLA activity
FT                                (By similarity).
FT   REGION        1    110       Sufficient for interaction with PAPOLA
FT                                (By similarity).
FT   REGION      136    219       Sufficient for interaction with CPSF4 (By
FT                                similarity).
FT   REGION      428    581       Sufficient for interaction with CPSF1 and
FT                                CSTF3 (By similarity).
FT   COMPBIAS    332    391       Pro-rich.
FT   COMPBIAS    441    549       Arg-rich.
FT   COMPBIAS    457    581       Glu-rich.
FT   MOD_RES      80     80       Phosphothreonine (By similarity).
FT   MOD_RES      84     84       Phosphoserine (By similarity).
FT   MOD_RES      86     86       Phosphoserine.
FT   MOD_RES      88     88       Phosphoserine.
FT   MOD_RES     234    234       Phosphothreonine (By similarity).
FT   MOD_RES     235    235       Phosphoserine (By similarity).
FT   MOD_RES     270    270       N6-acetyllysine (By similarity).
FT   MOD_RES     280    280       Phosphoserine.
FT   MOD_RES     479    479       Phosphoserine.
FT   MOD_RES     481    481       Phosphothreonine.
FT   MOD_RES     483    483       Phosphoserine.
FT   MOD_RES     487    487       Phosphoserine.
FT   MOD_RES     541    541       Phosphoserine (By similarity).
FT   MOD_RES     566    566       Phosphoserine (By similarity).
FT   VAR_SEQ     211    211       T -> TAEDCTMEVTPGAEIQDGRFNLFK (in isoform
FT                                4).
FT                                /FTId=VSP_016733.
FT   VAR_SEQ     248    283       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_016734.
FT   VAR_SEQ     365    373       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_016735.
FT   VAR_SEQ     487    581       SDEERYRYREYAERGYERHRASREKEERHRERRHREKEETR
FT                                HKSSRSNSRRRHESEEGDSHRRHKHKKSKRSKEGKEAGSEP
FT                                VPEQESTEAAPAE -> RFVGCAGP (in isoform 4).
FT                                /FTId=VSP_016736.
SQ   SEQUENCE   581 AA;  64959 MW;  2E8D6DF558168035 CRC64;
     MSAGEVERLV ELSGGTGGDE EEEWLYGGPW DVHVHSDLAK DLDENEVERP EEENASANPP
     SGIEEEAAEN GVAKPKVTET EDDSDSDSDD DEDDVHVTIG DIKTGAPQYG SYGTAPVNLN
     IKAGGRVYGN TGTKVKGVDL DAPGSINGVP LLEVDLDSFE DKPWRKPGAD LSDYFNYGFN
     EDTWKAYCEK QKRIRMGLEV IPVTSTTNKI TVQQGRTGNS EKEAALPSTK AEFTSPPSLF
     KTGLPPSRNS TSSQSQTSTA SRKASSSVGK WQDRYGRAES PDLRRLPGAI DVIGQTITIS
     RVEGRRRANE NSNIQVLSDR SATEVDNNFS KPPPFFPPGA PPTHLPPPPF LPPPPTVSTA
     PPLIPPPGIP ITVPPPGFPP PPGAPPPSLI PTIESGHSSG YDSRSARAFP YGNVAFPHLT
     SSAPSWPSLV DTTKQWDYYA RREKDRDRDR ERDRDRERER DRDRERERTR ERERERDHSP
     TPSVFNSDEE RYRYREYAER GYERHRASRE KEERHRERRH REKEETRHKS SRSNSRRRHE
     SEEGDSHRRH KHKKSKRSKE GKEAGSEPVP EQESTEAAPA E
//
ID   APLF_MOUSE              Reviewed;         499 AA.
AC   Q9D842; Q8BZL5; Q99LX6;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Aprataxin and PNK-like factor;
DE            EC=4.2.99.18;
DE   AltName: Full=Apurinic-apyrimidinic endonuclease APLF;
GN   Name=Aplf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon, and Small intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Nuclease involved in single-strand and double-strand DNA
CC       break repair. Recruited to sites of DNA damage through interaction
CC       with poly(ADP-ribose), a polymeric post-translational modification
CC       synthesized transiently at sites of chromosomal damage to
CC       accelerate DNA strand break repair reactions. Displays apurinic-
CC       apyrimidinic (AP) endonuclease and 3'-5' exonuclease activities in
CC       vitro. Also able to introduce nicks at hydroxyuracil and other
CC       types of pyrimidine base damage (By similarity).
CC   -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
CC       apyrimidinic site in DNA is broken by a beta-elimination reaction,
CC       leaving a 3'-terminal unsaturated sugar and a product with a
CC       terminal 5'-phosphate.
CC   -!- SUBUNIT: Interacts with LIG4, PARP1, XRCC1, XRCC4 and XRCC5 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol. Note=Localizes
CC       to DNA damage sites. Accumulates at single-strand breaks and
CC       double-strand breaks via the PBZ-type zinc fingers (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9D842-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D842-2; Sequence=VSP_014983, VSP_014984;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q9D842-3; Sequence=VSP_014982, VSP_014984;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The PBZ-type zinc fingers (also named CYR) mediate non-
CC       covalent poly(ADP-ribose)-binding. Poly(ADP-ribose)-binding is
CC       dependent on the presence of zinc and promotes its recruitment to
CC       DNA damage sites (By similarity).
CC   -!- DOMAIN: The FHA-like domain mediates interaction with XRCC1 and
CC       XRCC4 (By similarity).
CC   -!- PTM: Poly-ADP-ribosylated. In addition to binding non covalently
CC       poly(ADP-ribose) via its PBZ-type zinc fingers, the protein is
CC       also covalently poly-ADP-ribosylated by PARP1 (By similarity).
CC   -!- PTM: Phosphorylated in an ATM-dependent manner upon double-strand
CC       DNA break (By similarity).
CC   -!- SIMILARITY: Belongs to the APLF family.
CC   -!- SIMILARITY: Contains 1 FHA-like domain.
CC   -!- SIMILARITY: Contains 2 PBZ-type zinc fingers.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK008513; BAB25711.1; -; mRNA.
DR   EMBL; AK034191; BAC28625.1; -; mRNA.
DR   EMBL; BC002179; AAH02179.1; -; mRNA.
DR   IPI; IPI00110815; -.
DR   IPI; IPI00406210; -.
DR   IPI; IPI00649943; -.
DR   RefSeq; NP_001163960.1; NM_001170489.1.
DR   RefSeq; NP_077213.2; NM_024251.4.
DR   UniGene; Mm.31770; -.
DR   ProteinModelPortal; Q9D842; -.
DR   SMR; Q9D842; 1-104.
DR   STRING; Q9D842; -.
DR   PhosphoSite; Q9D842; -.
DR   PRIDE; Q9D842; -.
DR   Ensembl; ENSMUST00000032130; ENSMUSP00000032130; ENSMUSG00000030051.
DR   Ensembl; ENSMUST00000065997; ENSMUSP00000066232; ENSMUSG00000030051.
DR   GeneID; 72103; -.
DR   KEGG; mmu:72103; -.
DR   UCSC; uc009ctq.1; mouse.
DR   UCSC; uc009ctr.1; mouse.
DR   CTD; 72103; -.
DR   MGI; MGI:1919353; Aplf.
DR   GeneTree; ENSGT00390000010591; -.
DR   HOGENOM; HBG279634; -.
DR   HOVERGEN; HBG095728; -.
DR   InParanoid; Q9D842; -.
DR   OMA; ECTLRNS; -.
DR   OrthoDB; EOG4Q8501; -.
DR   PhylomeDB; Q9D842; -.
DR   NextBio; 335444; -.
DR   ArrayExpress; Q9D842; -.
DR   Bgee; Q9D842; -.
DR   Genevestigator; Q9D842; -.
DR   GermOnline; ENSMUSG00000030051; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; ISS:UniProtKB.
DR   GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; ISS:UniProtKB.
DR   GO; GO:0004520; F:endodeoxyribonuclease activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; ISS:UniProtKB.
DR   GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR   GO; GO:0000012; P:single strand break repair; ISS:UniProtKB.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR008984; SMAD_FHA_domain.
DR   InterPro; IPR019406; Znf_C2H2_APLF-like.
DR   Gene3D; G3DSA:2.60.200.20; FHA; 1.
DR   Pfam; PF10283; zf-CCHH; 2.
DR   SUPFAM; SSF49879; SMAD_FHA; 1.
PE   2: Evidence at transcript level;
KW   ADP-ribosylation; Alternative splicing; Coiled coil; Cytoplasm;
KW   DNA damage; DNA repair; Lyase; Metal-binding; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Zinc; Zinc-finger.
FT   CHAIN         1    499       Aprataxin and PNK-like factor.
FT                                /FTId=PRO_0000089343.
FT   DOMAIN        1    108       FHA-like.
FT   ZN_FING     372    393       PBZ-type 1.
FT   ZN_FING     414    435       PBZ-type 2.
FT   COMPBIAS    274    277       Poly-Ser.
FT   COMPBIAS    445    485       Asp-rich.
FT   MOD_RES     116    116       Phosphoserine; by ATM (By similarity).
FT   VAR_SEQ       1    108       Missing (in isoform 2).
FT                                /FTId=VSP_014983.
FT   VAR_SEQ       1     32       MPSDFFLQPLDGGPRVPVGPGQTVIGRGPLLG -> MPSVP
FT                                EGGGYE (in isoform 3).
FT                                /FTId=VSP_014982.
FT   VAR_SEQ     493    499       SSLHLKH -> RFMRRKK (in isoform 2 and
FT                                isoform 3).
FT                                /FTId=VSP_014984.
FT   CONFLICT    178    178       R -> H (in Ref. 2; AAH02179).
FT   CONFLICT    470    470       S -> F (in Ref. 1; BAB25711).
SQ   SEQUENCE   499 AA;  54968 MW;  4B41A9C0C8937963 CRC64;
     MPSDFFLQPL DGGPRVPVGP GQTVIGRGPL LGITDKRVSR RHAILEVVDS QLRIKPIHRN
     PCFYQSSEKS QHSPMETQVW SQLHPGDSFS LLLDKYAFRV FSAESEVEME CTLRNSQMLD
     EDDILSEMQK SPVVNLPDKT TGASQLQGSP EITKTKCPTI DPMSSSGECR AFSEHQPRPT
     QRKRILPAWM LAESLSDQSL STPAEGGDKD VIQRSGKAGT CEDRTPGNTS WHGKKRLSPS
     GNSKSVSAEQ DPGKKCRKAD QEGPGVSSEN VPESSSSNIV KDPDVDIVKT NKQKDGILIE
     ELGEVSKHKA ATKPTTNEEG ESCARVQSKS PPEKSQGCHP ESSSAPSSPD ALHTDTADPV
     LGCSEESKVR RTACMYGANC YRRNPLHFQH FSHPGDSDYG EVHGTDEGVI GDRPECPYGA
     SCYRKNPQHK MEYRHSALPA RVALDEDDDD VGQPSDDEDE EDYEPTDEDS DWHPGKDDEE
     QEDVDELLKE AKSSLHLKH
//
ID   Q9D852_MOUSE            Unreviewed;       459 AA.
AC   Q9D852;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   08-FEB-2011, entry version 40.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=2010300C02Rik;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RA   Adachi J., Aizawa K., Akahira S., Akimura T., Arai A., Aono H.,
RA   Arakawa T., Bono H., Carninci P., Fukuda S., Fukunishi Y., Furuno M.,
RA   Hanagaki T., Hara A., Hayatsu N., Hiramoto K., Hiraoka T., Hori F.,
RA   Imotani K., Ishii Y., Itoh M., Izawa M., Kasukawa T., Kato H.,
RA   Kawai J., Kojima Y., Konno H., Kouda M., Koya S., Kurihara C.,
RA   Matsuyama T., Miyazaki A., Nishi K., Nomura K., Numazaki R., Ohno M.,
RA   Okazaki Y., Okido T., Owa C., Saito H., Saito R., Sakai C., Sakai K.,
RA   Sano H., Sasaki D., Shibata K., Shibata Y., Shinagawa A., Shiraki T.,
RA   Sogabe Y., Suzuki H., Tagami M., Tagawa A., Takahashi F., Tanaka T.,
RA   Tejima Y., Toya T., Yamamura T., Yasunishi A., Yoshida K., Yoshino M.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK008485; BAB25692.1; -; mRNA.
DR   IPI; IPI00662408; -.
DR   UniGene; Mm.142607; -.
DR   Ensembl; ENSMUST00000114917; ENSMUSP00000110567; ENSMUSG00000026090.
DR   MGI; MGI:1919347; 2010300C02Rik.
DR   GeneTree; ENSGT00530000064039; -.
DR   HOVERGEN; HBG071624; -.
DR   ArrayExpress; Q9D852; -.
DR   Bgee; Q9D852; -.
DR   Genevestigator; Q9D852; -.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   459 AA;  48710 MW;  94E764973DC32512 CRC64;
     MAPPERDMSP FKGDMAPPKG IMEPPNRDTS LPKGDTPPPE TITDTNLETP SDTERQDQSV
     QKEEELTLVV VPRPEGVGTE SSTAPAPSPP VPKSCLKHKA LVTIGSPAES PLKEPGPAVQ
     DKAVVPPARP RPTQAATSGG PERTALGRKN ERSAEPQRSS VKRFSVTSSR ARARVSGSRL
     PEYSAHVPAG GRAPLLRSGL AWKSEAALDD LQVLPKPQDR KTMGGDPQNS GDVGAGQAGP
     GKSPQEAEPC ASSVQEPANG EDQSPFPVKL RSTSLSLKYR DSSAQEAKAI KRYSAEVRLE
     KGGLALLPKD EQSHVGAAPA LRGSRSPNGQ GKGKTRSPEQ PGTKPPLPRK PLLPSLTLPY
     PPTGLDTSPG ESERLIPVIL PPEPRKEKLS NQGAEKGQPP AATGPGADGQ PTPPWITMAR
     QKRRGAPDLP VNQEEKPGSR ILKTETGSKP RWPREPRSL
//
ID   CJ035_MOUSE             Reviewed;         120 AA.
AC   Q9D882;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Uncharacterized protein C10orf35 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Small intestine, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
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DR   EMBL; AK008338; BAB25613.1; -; mRNA.
DR   EMBL; AK035688; BAC29152.1; -; mRNA.
DR   EMBL; BC024943; AAH24943.1; -; mRNA.
DR   IPI; IPI00111050; -.
DR   RefSeq; NP_081527.1; NM_027251.3.
DR   UniGene; Mm.294126; -.
DR   IntAct; Q9D882; 6.
DR   MINT; MINT-219062; -.
DR   STRING; Q9D882; -.
DR   PRIDE; Q9D882; -.
DR   Ensembl; ENSMUST00000064050; ENSMUSP00000063504; ENSMUSG00000020083.
DR   GeneID; 69894; -.
DR   KEGG; mmu:69894; -.
DR   UCSC; uc007fgs.1; mouse.
DR   MGI; MGI:1917144; 2010107G23Rik.
DR   eggNOG; roNOG17719; -.
DR   GeneTree; ENSGT00390000009341; -.
DR   HOGENOM; HBG281539; -.
DR   HOVERGEN; HBG056578; -.
DR   InParanoid; Q9D882; -.
DR   OMA; FNRGHGA; -.
DR   OrthoDB; EOG4DZ1WS; -.
DR   PhylomeDB; Q9D882; -.
DR   NextBio; 330561; -.
DR   ArrayExpress; Q9D882; -.
DR   Bgee; Q9D882; -.
DR   CleanEx; MM_2010107G23RIK; -.
DR   Genevestigator; Q9D882; -.
DR   GermOnline; ENSMUSG00000020083; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
PE   2: Evidence at transcript level;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    120       Uncharacterized protein C10orf35 homolog.
FT                                /FTId=PRO_0000089791.
FT   TRANSMEM     91    111       Helical; (Potential).
FT   MOD_RES      61     61       Phosphoserine (By similarity).
SQ   SEQUENCE   120 AA;  13118 MW;  92C337D6CC6B4460 CRC64;
     MVRILANGEI VQDDDPRVRT TTQHRSSSSQ QGFFNRGHGA PPGGPGPRQQ QAGARLGAAQ
     SPFSDLNRQL VNMGFPQWHL GNHVVEPVTS ILLLFLLMML GVRGLLLVGL VYLVSHLSQR
//
ID   ARP5L_MOUSE             Reviewed;         153 AA.
AC   Q9D898;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-FEB-2011, entry version 61.
DE   RecName: Full=Actin-related protein 2/3 complex subunit 5-like protein;
DE   AltName: Full=Arp2/3 complex 16 kDa subunit 2;
DE            Short=ARC16-2;
GN   Name=Arpc5l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 90-102, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
CC   -!- FUNCTION: May function as component of the Arp2/3 complex which is
CC       involved in regulation of actin polymerization and together with
CC       an activating nucleation-promoting factor (NPF) mediates the
CC       formation of branched actin networks (By similarity).
CC   -!- SUBUNIT: May be a component of the Arp2/3 complex in which it may
CC       replace ARPC5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC   -!- SIMILARITY: Belongs to the ARPC5 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK008255; BAB25561.1; -; mRNA.
DR   EMBL; BC024482; AAH24482.1; -; mRNA.
DR   IPI; IPI00111117; -.
DR   RefSeq; NP_083085.1; NM_028809.1.
DR   UniGene; Mm.38155; -.
DR   UniGene; Mm.440770; -.
DR   ProteinModelPortal; Q9D898; -.
DR   SMR; Q9D898; 8-152.
DR   STRING; Q9D898; -.
DR   REPRODUCTION-2DPAGE; Q9D898; -.
DR   PRIDE; Q9D898; -.
DR   Ensembl; ENSMUST00000090993; ENSMUSP00000088516; ENSMUSG00000026755.
DR   GeneID; 74192; -.
DR   KEGG; mmu:74192; -.
DR   UCSC; uc008joa.1; mouse.
DR   CTD; 74192; -.
DR   MGI; MGI:1921442; Arpc5l.
DR   GeneTree; ENSGT00390000014806; -.
DR   HOVERGEN; HBG050583; -.
DR   PhylomeDB; Q9D898; -.
DR   NextBio; 340058; -.
DR   ArrayExpress; Q9D898; -.
DR   Bgee; Q9D898; -.
DR   CleanEx; MM_ARPC5L; -.
DR   Genevestigator; Q9D898; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0030833; P:regulation of actin filament polymerization; IEA:InterPro.
DR   InterPro; IPR006789; ARP2/3_p16_Arc.
DR   Gene3D; G3DSA:1.25.40.190; p16_Arc; 1.
DR   PANTHER; PTHR12644; p16_Arc; 1.
DR   Pfam; PF04699; P16-Arc; 1.
DR   SUPFAM; SSF69103; p16_Arc; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    153       Actin-related protein 2/3 complex subunit
FT                                5-like protein.
FT                                /FTId=PRO_0000279481.
FT   MOD_RES      64     64       Phosphoserine (By similarity).
SQ   SEQUENCE   153 AA;  16980 MW;  F01A86DC009ECEC1 CRC64;
     MARNTLSSRF RRVDIDEFDE NKFVDEHEEA AAAAGEPGPD PCEVDGLLRQ GDMLRAFHAA
     LRNSPINTKN QAVKERAQGV VLKVLTNFKS SEIEQAVQSL DRNGIDLLMK YIYKGFEKPT
     ENSSAVLLQW HEKALAVGGL GSIIRVLTAR KTV
//
ID   JAM3_MOUSE              Reviewed;         310 AA.
AC   Q9D8B7; Q8BT59; Q9D1M9; Q9EPK4;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Junctional adhesion molecule C;
DE            Short=JAM-C;
DE   AltName: Full=JAM-2;
DE   AltName: Full=Junctional adhesion molecule 3;
DE            Short=JAM-3;
DE   Flags: Precursor;
GN   Name=Jam3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20489356; PubMed=11036763;
RA   Aurrand-Lions M.A., Duncan L., Du Pasquier L., Imhof B.A.;
RT   "Cloning of JAM-2 and JAM-3: an emerging junctional adhesion molecular
RT   family?";
RL   Curr. Top. Microbiol. Immunol. 251:91-98(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=21264728; PubMed=11053409; DOI=10.1074/jbc.M005458200;
RA   Aurrand-Lions M.A., Duncan L., Ballestrem C., Imhof B.A.;
RT   "JAM-2, a novel immunoglobulin superfamily molecule, expressed by
RT   endothelial and lymphatic cells.";
RL   J. Biol. Chem. 276:2733-2741(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Small intestine, and Wolffian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 84-91 AND 146-154, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=11739175; DOI=10.1182/blood.V98.13.3699;
RA   Aurrand-Lions M.A., Johnson-Leger C., Wong C., Du Pasquier L.,
RA   Imhof B.A.;
RT   "Heterogeneity of endothelial junctions is reflected by differential
RT   expression and specific subcellular localization of the three JAM
RT   family members.";
RL   Blood 98:3699-3707(2001).
RN   [7]
RP   REVIEW, AND NOMENCLATURE.
RX   MEDLINE=22695901; PubMed=12810109; DOI=10.1016/S1471-4906(03)00117-0;
RA   Muller W.A.;
RT   "Leukocyte-endothelial-cell interactions in leukocyte transmigration
RT   and the inflammatory response.";
RL   Trends Immunol. 24:327-334(2003).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-192 AND ASN-198, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
CC   -!- FUNCTION: May participate in cell-cell adhesion distinct from
CC       tight junctions.
CC   -!- SUBUNIT: Interacts with JAM2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- TISSUE SPECIFICITY: Endothelial cells.
CC   -!- SIMILARITY: Belongs to the immunoglobulin superfamily.
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC       domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ300304; CAC20704.1; -; mRNA.
DR   EMBL; AK008187; BAB25519.1; -; mRNA.
DR   EMBL; AK003326; BAB22715.1; -; mRNA.
DR   EMBL; AK013156; BAB28683.1; -; mRNA.
DR   EMBL; AK017692; BAC25526.1; -; mRNA.
DR   EMBL; AK032833; BAC28049.1; -; mRNA.
DR   EMBL; BC024357; AAH24357.1; -; mRNA.
DR   IPI; IPI00453847; -.
DR   RefSeq; NP_075766.1; NM_023277.3.
DR   UniGene; Mm.28770; -.
DR   ProteinModelPortal; Q9D8B7; -.
DR   SMR; Q9D8B7; 29-237.
DR   MINT; MINT-1344650; -.
DR   STRING; Q9D8B7; -.
DR   PRIDE; Q9D8B7; -.
DR   Ensembl; ENSMUST00000034472; ENSMUSP00000034472; ENSMUSG00000031990.
DR   GeneID; 83964; -.
DR   KEGG; mmu:83964; -.
DR   UCSC; uc009oqj.1; mouse.
DR   CTD; 83964; -.
DR   MGI; MGI:1933825; Jam3.
DR   eggNOG; roNOG09320; -.
DR   GeneTree; ENSGT00600000084033; -.
DR   HOGENOM; HBG446408; -.
DR   HOVERGEN; HBG000518; -.
DR   InParanoid; Q9D8B7; -.
DR   OMA; YSWYRND; -.
DR   OrthoDB; EOG4D26QH; -.
DR   PhylomeDB; Q9D8B7; -.
DR   NextBio; 350838; -.
DR   ArrayExpress; Q9D8B7; -.
DR   Bgee; Q9D8B7; -.
DR   CleanEx; MM_JAM3; -.
DR   Genevestigator; Q9D8B7; -.
DR   GermOnline; ENSMUSG00000031990; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0033010; C:paranodal junction; IDA:MGI.
DR   GO; GO:0005923; C:tight junction; IDA:MGI.
DR   GO; GO:0005178; F:integrin binding; IPI:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
DR   GO; GO:0002250; P:adaptive immune response; IMP:MGI.
DR   GO; GO:0007160; P:cell-matrix adhesion; IDA:MGI.
DR   GO; GO:0030010; P:establishment of cell polarity; IDA:MGI.
DR   GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IMP:MGI.
DR   GO; GO:0042552; P:myelination; IMP:MGI.
DR   GO; GO:0002318; P:myeloid progenitor cell differentiation; IMP:MGI.
DR   GO; GO:0001780; P:neutrophil homeostasis; IMP:MGI.
DR   GO; GO:0090138; P:regulation of actin cytoskeleton organization by cell-cell adhesion; IMP:MGI.
DR   GO; GO:0007286; P:spermatid development; IMP:MGI.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Disulfide bond;
KW   Glycoprotein; Immunoglobulin domain; Membrane; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     29       Potential.
FT   CHAIN        30    310       Junctional adhesion molecule C.
FT                                /FTId=PRO_0000015072.
FT   TOPO_DOM     30    241       Extracellular (Potential).
FT   TRANSMEM    242    262       Helical; (Potential).
FT   TOPO_DOM    263    310       Cytoplasmic (Potential).
FT   DOMAIN       35    127       Ig-like V-type.
FT   DOMAIN      139    236       Ig-like C2-type.
FT   CARBOHYD    104    104       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    192    192       N-linked (GlcNAc...).
FT   CARBOHYD    198    198       N-linked (GlcNAc...).
FT   DISULFID     53    115       Potential.
FT   DISULFID    160    219       Potential.
FT   CONFLICT     44     44       H -> Q (in Ref. 3; BAB25519).
FT   CONFLICT    172    172       S -> N (in Ref. 3; BAB25519).
FT   CONFLICT    303    303       R -> K (in Ref. 3; BAB22715).
FT   CONFLICT    306    307       SS -> IA (in Ref. 3; BAB22715).
SQ   SEQUENCE   310 AA;  34838 MW;  4B92BCB51D0A4B0A CRC64;
     MALSRRLRLR LYARLPDFFL LLLFRGCMIE AVNLKSSNRN PVVHEFESVE LSCIITDSQT
     SDPRIEWKKI QDGQTTYVYF DNKIQGDLAG RTDVFGKTSL RIWNVTRSDS AIYRCEVVAL
     NDRKEVDEIT IELIVQVKPV TPVCRIPAAV PVGKTATLQC QESEGYPRPH YSWYRNDVPL
     PTDSRANPRF QNSSFHVNSE TGTLVFNAVH KDDSGQYYCI ASNDAGAARC EGQDMEVYDL
     NIAGIIGGVL VVLIVLAVIT MGICCAYRRG CFISSKQDGE SYKSPGKHDG VNYIRTSEEG
     DFRHKSSFVI
//
ID   RL4_MOUSE               Reviewed;         419 AA.
AC   Q9D8E6; Q9CY08;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=60S ribosomal protein L4;
GN   Name=Rpl4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic liver, and Small intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-13; 165-171 AND 353-363, CLEAVAGE OF INITIATOR
RP   METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
RA   Kanor S., Quadroni M., Bienvenut W.V.;
RL   Submitted (MAR-2006) to UniProtKB.
RN   [4]
RP   INTERACTION WITH IPO9.
RX   MEDLINE=21681405; PubMed=11823430; DOI=10.1093/emboj/21.3.377;
RA   Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D.;
RT   "Importins fulfil a dual function as nuclear import receptors and
RT   cytoplasmic chaperones for exposed basic domains.";
RL   EMBO J. 21:377-386(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- SUBUNIT: May bind IPO9 with low affinity. Interacts with RBM3 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the ribosomal protein L4P family.
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DR   EMBL; AK008098; BAB25458.1; -; mRNA.
DR   EMBL; AK011068; BAB27375.1; -; mRNA.
DR   EMBL; BC003459; AAH03459.1; -; mRNA.
DR   IPI; IPI00111412; -.
DR   RefSeq; NP_077174.1; NM_024212.4.
DR   UniGene; Mm.280083; -.
DR   ProteinModelPortal; Q9D8E6; -.
DR   SMR; Q9D8E6; 1-369.
DR   MINT; MINT-1859608; -.
DR   STRING; Q9D8E6; -.
DR   PhosphoSite; Q9D8E6; -.
DR   PRIDE; Q9D8E6; -.
DR   Ensembl; ENSMUST00000034966; ENSMUSP00000034966; ENSMUSG00000032399.
DR   GeneID; 67891; -.
DR   KEGG; mmu:67891; -.
DR   NMPDR; fig|10090.3.peg.20359; -.
DR   UCSC; uc009qbn.1; mouse.
DR   CTD; 67891; -.
DR   MGI; MGI:1915141; Rpl4.
DR   GeneTree; ENSGT00390000018145; -.
DR   HOGENOM; HBG316531; -.
DR   HOVERGEN; HBG001453; -.
DR   InParanoid; Q9D8E6; -.
DR   OMA; TKAFRNI; -.
DR   OrthoDB; EOG483D4X; -.
DR   PhylomeDB; Q9D8E6; -.
DR   NextBio; 325862; -.
DR   ArrayExpress; Q9D8E6; -.
DR   Bgee; Q9D8E6; -.
DR   CleanEx; MM_RPL4; -.
DR   Genevestigator; Q9D8E6; -.
DR   GermOnline; ENSMUSG00000032399; Mus musculus.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR002136; Ribosomal_L4/L1e.
DR   InterPro; IPR013000; Ribosomal_L4/L1e_euk/arc_CS.
DR   Pfam; PF00573; Ribosomal_L4; 1.
DR   PROSITE; PS00939; RIBOSOMAL_L1E; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Phosphoprotein;
KW   Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    419       60S ribosomal protein L4.
FT                                /FTId=PRO_0000129351.
FT   COMPBIAS    307    419       Lys-rich.
FT   MOD_RES       2      2       N-acetylalanine.
FT   MOD_RES      14     14       N6-acetyllysine (By similarity).
FT   MOD_RES     106    106       N6-acetyllysine (By similarity).
FT   MOD_RES     295    295       Phosphoserine.
FT   MOD_RES     333    333       N6-acetyllysine (By similarity).
FT   MOD_RES     365    365       Phosphoserine (By similarity).
FT   CONFLICT    161    161       Y -> F (in Ref. 1; BAB27375).
SQ   SEQUENCE   419 AA;  47154 MW;  E736E656A60BE85B CRC64;
     MACARPLISV YSEKGESSGK NVTLPAVFKA PIRPDIVNFV HTNLRKNNRQ PYAVSELAGH
     QTSAESWGTG RAVARIPRVR GGGTHRSGQG AFGNMCRGGR MFAPTKTWRR WHRRVNTTQK
     RYAICSALAA SALPALVMSK GHRIEEVPEL PLVVEDKVEG YKKTKEAVQL LKKLKAWNDI
     KKVYASQRMR AGKGKMRNRR RIQRRGPCII YNEDNGIIKA FRNIPGITLL NVSKLNILKL
     APGGHVGRFC IWTESAFRKL DELYGTWRKA ASLKSNYNLP MHKMMNTDLS RILKSPEIQR
     ALRAPRKKIH RRVLKKNPLK NLRIMLKLNP YAKTMRRNTI LRQARNHKLR VKKLEAAATA
     LATKSEKVVP EKGTADKKPA VGKKGKKVDA KKQKPAGKKV VAKKPAEKKP TTEEKKPAA
//
ID   EF1G_MOUSE              Reviewed;         437 AA.
AC   Q9D8N0; Q920C5; Q9CRT5; Q9CSU3; Q9D004;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Elongation factor 1-gamma;
DE            Short=EF-1-gamma;
DE   AltName: Full=eEF-1B gamma;
GN   Name=Eef1g;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Thymus;
RA   Lee Y., Lu X., He W.;
RT   "Mouse elongation factor-like protein, mRNA sequence.";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Embryonic head, Pancreas, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 234-241, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Probably plays a role in anchoring the complex to other
CC       cellular components (By similarity).
CC   -!- SUBUNIT: EF-1 is composed of four subunits: alpha, beta, delta,
CC       and gamma (By similarity).
CC   -!- SIMILARITY: Contains 1 EF-1-gamma C-terminal domain.
CC   -!- SIMILARITY: Contains 1 GST C-terminal domain.
CC   -!- SIMILARITY: Contains 1 GST N-terminal domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF321126; AAL23895.1; -; mRNA.
DR   EMBL; AK007869; BAB25320.1; -; mRNA.
DR   EMBL; AK011951; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK011973; BAB27948.1; -; mRNA.
DR   EMBL; AK014277; BAB29238.3; -; mRNA.
DR   EMBL; AK050636; BAC34356.1; -; mRNA.
DR   EMBL; AK081859; BAC38351.1; -; mRNA.
DR   EMBL; BC083071; AAH83071.1; -; mRNA.
DR   IPI; IPI00318841; -.
DR   RefSeq; NP_080283.3; NM_026007.4.
DR   UniGene; Mm.247762; -.
DR   UniGene; Mm.379129; -.
DR   ProteinModelPortal; Q9D8N0; -.
DR   SMR; Q9D8N0; 1-216, 276-437.
DR   STRING; Q9D8N0; -.
DR   PhosphoSite; Q9D8N0; -.
DR   REPRODUCTION-2DPAGE; Q9D8N0; -.
DR   PRIDE; Q9D8N0; -.
DR   Ensembl; ENSMUST00000052248; ENSMUSP00000093955; ENSMUSG00000071644.
DR   GeneID; 67160; -.
DR   KEGG; mmu:67160; -.
DR   NMPDR; fig|10090.3.peg.4630; -.
DR   UCSC; uc008goi.1; mouse.
DR   CTD; 67160; -.
DR   MGI; MGI:1914410; Eef1g.
DR   GeneTree; ENSGT00390000007552; -.
DR   HOGENOM; HBG436026; -.
DR   HOVERGEN; HBG051444; -.
DR   InParanoid; Q9D8N0; -.
DR   OMA; NKQATEQ; -.
DR   OrthoDB; EOG43JC4V; -.
DR   PhylomeDB; Q9D8N0; -.
DR   NextBio; 323762; -.
DR   ArrayExpress; Q9D8N0; -.
DR   Bgee; Q9D8N0; -.
DR   CleanEx; MM_EEF1G; -.
DR   Genevestigator; Q9D8N0; -.
DR   GermOnline; ENSMUSG00000071644; Mus musculus.
DR   GO; GO:0005853; C:eukaryotic translation elongation factor 1 complex; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR017933; Glutathione_S_Trfase/Cl_chnl_C.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   InterPro; IPR012335; Thioredoxin_fold.
DR   InterPro; IPR001662; Transl_elong_EF1_G_con.
DR   Gene3D; G3DSA:1.20.1050.10; GST_C_like; 1.
DR   Gene3D; G3DSA:3.40.30.10; Thioredoxin_fold; 1.
DR   Gene3D; G3DSA:3.30.70.1010; Transl_elong_EF1_G_con; 1.
DR   Pfam; PF00647; EF1G; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SUPFAM; SSF47616; GST_C_like; 1.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 1.
DR   SUPFAM; SSF89942; Transl_elong_EF1_G_con; 1.
DR   PROSITE; PS50040; EF1G_C; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Elongation factor;
KW   Phosphoprotein; Protein biosynthesis.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    437       Elongation factor 1-gamma.
FT                                /FTId=PRO_0000208814.
FT   DOMAIN        2     87       GST N-terminal.
FT   DOMAIN       88    216       GST C-terminal.
FT   DOMAIN      276    437       EF-1-gamma C-terminal.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      43     43       Phosphothreonine (By similarity).
FT   MOD_RES      46     46       Phosphothreonine (By similarity).
FT   MOD_RES     132    132       N6-acetyllysine (By similarity).
FT   MOD_RES     147    147       N6-acetyllysine (By similarity).
FT   MOD_RES     434    434       N6-acetyllysine (By similarity).
FT   CONFLICT      4      4       G -> E (in Ref. 2; BAB29238).
FT   CONFLICT    173    173       K -> R (in Ref. 1; AAL23895).
FT   CONFLICT    227    227       K -> N (in Ref. 2; BAB27948).
FT   CONFLICT    340    340       N -> T (in Ref. 1; AAL23895).
FT   CONFLICT    413    413       V -> G (in Ref. 1; AAL23895).
SQ   SEQUENCE   437 AA;  50061 MW;  403A9C0E95E27454 CRC64;
     MAAGTLYTYP ENWRAFKALI AAQYSGAQVR VLSAPPHFHF GQTNRTPEFL RKFPAGKVPA
     FEGDDGFCVF ESNAIAYYVS NEELRGSTPE AAAQVVQWVS FADSDIVPPA STWVFPTLGI
     MHHNKQATEN AKEEVKRILG LLDTHLKTRT FLVGERVTLA DITVVCTLLW LYKQVLEPSF
     RQAFPNTNRW FLTCINQPQF RAILGEVKLC EKMAQFDAKK FAESQPKKDT PRKEKGSREE
     KQKPQAERKE EKKAAAPAPE EEMDECEQAL AAEPKAKDPF AHLPKSTFVL DEFKRKYSNE
     DTLSVALPYF WEHFDKDGWS LWYAEYRFPE ELTQTFMSCN LITGMFQRLD KLRKNAFASV
     ILFGTNNSSS ISGVWVFRGQ ELAFPLSPDW QVDYESYTWR KLDPGSEETQ TLVREYFSWE
     GTFQHVGKAV NQGKIFK
//
ID   ARFG3_MOUSE             Reviewed;         523 AA.
AC   Q9D8S3; Q544V6; Q8BW06; Q99KN8;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=ADP-ribosylation factor GTPase-activating protein 3;
DE            Short=ARF GAP 3;
GN   Name=Arfgap3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Amnion, Pancreas, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: GTPase-activating protein (GAP) for ADP ribosylation
CC       factor 1 (ARF1). Hydrolysis of ARF1-bound GTP may lead to
CC       dissociation of coatomer from Golgi-derived membranes to allow
CC       fusion with target membranes (By similarity).
CC   -!- ENZYME REGULATION: GAP activity stimulated by phosphatidylinositol
CC       4,5-bisphosphate (PIP2) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus
CC       membrane; Peripheral membrane protein; Cytoplasmic side (By
CC       similarity). Note=Also found on peripheral punctate structures
CC       likely to be endoplasmic reticulum-Golgi intermediate compartment
CC       (By similarity).
CC   -!- SIMILARITY: Contains 1 Arf-GAP domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK007732; BAB25220.1; -; mRNA.
DR   EMBL; AK028990; BAC26229.1; -; mRNA.
DR   EMBL; AK075788; BAC35959.1; -; mRNA.
DR   EMBL; AK169107; BAE40889.1; -; mRNA.
DR   EMBL; BC004081; AAH04081.1; -; mRNA.
DR   EMBL; BC060369; AAH60369.1; -; mRNA.
DR   IPI; IPI00111931; -.
DR   RefSeq; NP_079721.2; NM_025445.4.
DR   UniGene; Mm.258910; -.
DR   ProteinModelPortal; Q9D8S3; -.
DR   SMR; Q9D8S3; 3-136.
DR   PhosphoSite; Q9D8S3; -.
DR   PRIDE; Q9D8S3; -.
DR   Ensembl; ENSMUST00000067215; ENSMUSP00000064893; ENSMUSG00000054277.
DR   GeneID; 66251; -.
DR   KEGG; mmu:66251; -.
DR   UCSC; uc007xah.1; mouse.
DR   CTD; 66251; -.
DR   MGI; MGI:1913501; Arfgap3.
DR   eggNOG; roNOG07761; -.
DR   GeneTree; ENSGT00390000005436; -.
DR   HOGENOM; HBG736886; -.
DR   HOVERGEN; HBG050563; -.
DR   InParanoid; Q9D8S3; -.
DR   OrthoDB; EOG4N8R4S; -.
DR   ArrayExpress; Q9D8S3; -.
DR   Bgee; Q9D8S3; -.
DR   Genevestigator; Q9D8S3; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008060; F:ARF GTPase activator activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009306; P:protein secretion; ISS:UniProtKB.
DR   GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001164; ArfGAP.
DR   Pfam; PF01412; ArfGap; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SUPFAM; SSF57863; ArfGAP; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; ER-Golgi transport; Golgi apparatus;
KW   GTPase activation; Membrane; Metal-binding; Phosphoprotein;
KW   Protein transport; Transport; Zinc; Zinc-finger.
FT   CHAIN         1    523       ADP-ribosylation factor GTPase-activating
FT                                protein 3.
FT                                /FTId=PRO_0000074194.
FT   DOMAIN       10    126       Arf-GAP.
FT   ZN_FING      25     48       C4-type.
FT   COMPBIAS    348    408       Ser-rich.
FT   MOD_RES     143    143       Phosphoserine (By similarity).
FT   MOD_RES     223    223       N6-acetyllysine (By similarity).
FT   MOD_RES     228    228       N6-acetyllysine (By similarity).
FT   MOD_RES     229    229       N6-acetyllysine (By similarity).
FT   MOD_RES     270    270       Phosphoserine (By similarity).
FT   MOD_RES     331    331       Phosphoserine (By similarity).
FT   MOD_RES     377    377       Phosphoserine (By similarity).
FT   MOD_RES     435    435       Phosphoserine (By similarity).
FT   MOD_RES     460    460       Phosphoserine (By similarity).
FT   CONFLICT    208    208       P -> PA (in Ref. 1; BAB25220).
FT   CONFLICT    361    361       S -> SS (in Ref. 1; BAB25220/BAC26229 and
FT                                2; AAH04081).
SQ   SEQUENCE   523 AA;  57456 MW;  FC093B11DB765BC3 CRC64;
     MGDPSKQDIL AIFKRLRSVP TNKVCFDCGA KNPSWASISY GVFLCIDCSG SHRSLGVHLS
     FIRSTELDSN WSWFQLRCMQ VGGNSNASSF FHQHGCATKD TNAKYNSRAA QLYREKIKTL
     ATQATRRHGT DLWLDSCAAP PVSPPPKEED FFASHASLEV SGAMQASAQP ESASSTPWGL
     ETTPEKHEGG PGQGPSVEGL NTPGKAAPEV SSIIKKKPNQ AKKGLGAKKG SLGAQKLTNT
     SFTEIEKQAQ AVDKRKEQED LARGAPKEES IVSSLRLAYK DLEISRKKDE RLNLSGQKKV
     EAERLGMGFG SCRSGISHSV TSDMQTIEQE SPTLAKPRRK YQEDPEDSYF SSSSKWSEQS
     SRYFDDPMEL RSSSFSSWDD GADSYWKKDS SRDPEPAMRS TGSSDRPSAR RKPEYEPIGS
     TDEAQKKFGN VKAISSDMYF GIQAQTDFET RARLERLSTS SSISSADLFD EQRKQTAGNY
     NLSNVLPNAP DMAQFKQGVR SVAGKLSVFA NGVMTSIQDR YGS
//
ID   BOLA1_MOUSE             Reviewed;         137 AA.
AC   Q9D8S9;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=BolA-like protein 1;
GN   Name=Bola1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   STRUCTURE BY NMR OF 13-128.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of Bola1 protein from Mus musculus.";
RL   Submitted (NOV-2003) to the PDB data bank.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Could be secreted via a non-
CC       classical export pathway (By similarity).
CC   -!- SIMILARITY: Belongs to the bolA/yrbA family.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK007718; BAB25210.1; -; mRNA.
DR   EMBL; BC027558; AAH27558.1; -; mRNA.
DR   IPI; IPI00111953; -.
DR   RefSeq; NP_081251.1; NM_026975.2.
DR   UniGene; Mm.104531; -.
DR   PDB; 1V60; NMR; -; A=13-128.
DR   PDBsum; 1V60; -.
DR   ProteinModelPortal; Q9D8S9; -.
DR   SMR; Q9D8S9; 13-128.
DR   STRING; Q9D8S9; -.
DR   PhosphoSite; Q9D8S9; -.
DR   PRIDE; Q9D8S9; -.
DR   Ensembl; ENSMUST00000016087; ENSMUSP00000016087; ENSMUSG00000015943.
DR   Ensembl; ENSMUST00000107099; ENSMUSP00000102716; ENSMUSG00000015943.
DR   GeneID; 69168; -.
DR   KEGG; mmu:69168; -.
DR   NMPDR; fig|10090.3.peg.8604; -.
DR   UCSC; uc008qmg.1; mouse.
DR   CTD; 69168; -.
DR   MGI; MGI:1916418; Bola1.
DR   eggNOG; roNOG16400; -.
DR   GeneTree; ENSGT00510000048165; -.
DR   HOGENOM; HBG739421; -.
DR   HOVERGEN; HBG080902; -.
DR   InParanoid; Q9D8S9; -.
DR   OMA; DISPPCL; -.
DR   OrthoDB; EOG4G1MHQ; -.
DR   PhylomeDB; Q9D8S9; -.
DR   NextBio; 328754; -.
DR   ArrayExpress; Q9D8S9; -.
DR   Bgee; Q9D8S9; -.
DR   CleanEx; MM_BOLA1; -.
DR   Genevestigator; Q9D8S9; -.
DR   GermOnline; ENSMUSG00000015943; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   InterPro; IPR002634; BolA.
DR   Gene3D; G3DSA:3.30.300.90; BolA; 1.
DR   PANTHER; PTHR12735; BolA; 1.
DR   Pfam; PF01722; BolA; 1.
DR   SUPFAM; SSF82657; BolA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Phosphoprotein; Secreted.
FT   CHAIN         1    137       BolA-like protein 1.
FT                                /FTId=PRO_0000201234.
FT   MOD_RES      81     81       Phosphoserine (By similarity).
FT   STRAND       27     29
FT   HELIX        31     43
FT   STRAND       47     53
FT   STRAND       57     59
FT   STRAND       66     73
FT   HELIX        75     77
FT   HELIX        82     92
FT   HELIX        94     97
FT   TURN         98    100
FT   STRAND      102    109
FT   TURN        111    116
SQ   SEQUENCE   137 AA;  14379 MW;  EC5B187A3C597155 CRC64;
     MLSARSAQCM VSMATRSCVS RGSAGSAAAG PVEAAIRAKL EQALSPEVLE LRNESGGHAV
     PAGSETHFRV AVVSSRFEGM SPLQRHRLVH EALSEELAGP VHALAIQAKT PAQWRENPQL
     DISPPCLGGS KKTRGTS
//
ID   F18B1_MOUSE             Reviewed;         205 AA.
AC   Q9D8T4; Q3UBJ3;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Protein FAM18B1;
GN   Name=Fam18b1; Synonyms=Fam18b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow macrophage, Liver, Ovary, Pancreas, and Uterus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the FAM18/TVP23 family.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK007707; BAB25202.1; -; mRNA.
DR   EMBL; AK050027; BAC34036.1; -; mRNA.
DR   EMBL; AK077277; BAC36725.1; -; mRNA.
DR   EMBL; AK150936; BAE29971.1; -; mRNA.
DR   EMBL; AL645847; CAI25651.1; -; Genomic_DNA.
DR   EMBL; BC115504; AAI15505.1; -; mRNA.
DR   EMBL; BC115505; AAI15506.1; -; mRNA.
DR   IPI; IPI00111992; -.
DR   RefSeq; NP_080486.1; NM_026210.4.
DR   UniGene; Mm.9806; -.
DR   PhosphoSite; Q9D8T4; -.
DR   PRIDE; Q9D8T4; -.
DR   Ensembl; ENSMUST00000014321; ENSMUSP00000014321; ENSMUSG00000014177.
DR   GeneID; 67510; -.
DR   KEGG; mmu:67510; -.
DR   UCSC; uc007jkh.1; mouse.
DR   CTD; 67510; -.
DR   MGI; MGI:1914760; Fam18b.
DR   eggNOG; roNOG11488; -.
DR   GeneTree; ENSGT00390000004428; -.
DR   HOGENOM; HBG526983; -.
DR   HOVERGEN; HBG051531; -.
DR   InParanoid; Q9D8T4; -.
DR   OMA; KQFLRQT; -.
DR   OrthoDB; EOG49PB0J; -.
DR   PhylomeDB; Q9D8T4; -.
DR   NextBio; 324782; -.
DR   ArrayExpress; Q9D8T4; -.
DR   Bgee; Q9D8T4; -.
DR   Genevestigator; Q9D8T4; -.
DR   GermOnline; ENSMUSG00000014177; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR008564; DUF846_euk.
DR   PANTHER; PTHR13019; DUF846_euk; 1.
DR   Pfam; PF05832; DUF846; 1.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    205       Protein FAM18B1.
FT                                /FTId=PRO_0000212829.
FT   TRANSMEM     34     53       Helical; (Potential).
FT   TRANSMEM     54     72       Helical; (Potential).
FT   TRANSMEM    126    146       Helical; (Potential).
FT   TRANSMEM    152    172       Helical; (Potential).
FT   MOD_RES       6      6       Phosphoserine.
SQ   SEQUENCE   205 AA;  23305 MW;  4E55E71E681A85CD CRC64;
     MLSQDSNDDT EDVSLFDAEE ETTNRPRKSK IRHPVASFFH LFFRVSAVVV YLLCELLSSS
     FIACMVTIIL LLSCDFWAVK NVTGRLMVGL RWWNHIDEDG KSHWVFESRK STPQDNKTIS
     EAESRIFWLG LIACPVLWVI FAFSALFSFR VKWLAVVIMG VVLQGANLYG YIRCKVGSKK
     NLTSMATSYL GKQFLRQNTG DGQTS
//
ID   OCAD2_MOUSE             Reviewed;         154 AA.
AC   Q9D8W7;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=OCIA domain-containing protein 2;
GN   Name=Ociad2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Endosome (Probable).
CC   -!- SIMILARITY: Contains 1 OCIA domain.
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DR   EMBL; AK007617; BAB25138.1; -; mRNA.
DR   EMBL; BC044883; AAH44883.1; -; mRNA.
DR   IPI; IPI00112139; -.
DR   RefSeq; NP_081226.1; NM_026950.3.
DR   UniGene; Mm.274892; -.
DR   PhosphoSite; Q9D8W7; -.
DR   PRIDE; Q9D8W7; -.
DR   Ensembl; ENSMUST00000087195; ENSMUSP00000084445; ENSMUSG00000029153.
DR   GeneID; 433904; -.
DR   KEGG; mmu:433904; -.
DR   UCSC; uc008xsw.1; mouse.
DR   CTD; 433904; -.
DR   MGI; MGI:1916377; Ociad2.
DR   eggNOG; roNOG16225; -.
DR   GeneTree; ENSGT00530000063690; -.
DR   HOGENOM; HBG714580; -.
DR   HOVERGEN; HBG054610; -.
DR   InParanoid; Q9D8W7; -.
DR   OMA; PKSKLHI; -.
DR   OrthoDB; EOG4BCDP6; -.
DR   PhylomeDB; Q9D8W7; -.
DR   NextBio; 409095; -.
DR   ArrayExpress; Q9D8W7; -.
DR   Bgee; Q9D8W7; -.
DR   CleanEx; MM_OCIAD2; -.
DR   Genevestigator; Q9D8W7; -.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   InterPro; IPR009764; OCIA.
DR   PANTHER; PTHR13336; OCIA; 1.
DR   Pfam; PF07051; OCIA; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Endosome.
FT   CHAIN         1    154       OCIA domain-containing protein 2.
FT                                /FTId=PRO_0000299393.
FT   DOMAIN        1    120       OCIA.
FT   MOD_RES      41     41       N6-acetyllysine (By similarity).
SQ   SEQUENCE   154 AA;  16926 MW;  CBA0DB1590C1ED04 CRC64;
     MASVSTHGNQ EKSPHLPPLS KQSLLFCPKS KLHIHRGEIA KIIRECQEES FWKRALPFSL
     ISMLVTQGLV HQGYLAANPR FGSLPKVALA GLLGFGLGKA SYIRVCQSKF HSFEDQLRGA
     GFGPEHNRHC LLTCEDCKTR RGLSEKAGSQ PSAS
//
ID   CUTC_MOUSE              Reviewed;         272 AA.
AC   Q9D8X1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Copper homeostasis protein cutC homolog;
GN   Name=Cutc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in copper homeostasis. Can bind one
CC       Cu(1+) per subunit (By similarity).
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the CutC family.
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DR   EMBL; AK007591; BAB25124.1; -; mRNA.
DR   EMBL; BC026775; AAH26775.1; -; mRNA.
DR   IPI; IPI00112176; -.
DR   RefSeq; NP_001107034.1; NM_001113562.1.
DR   UniGene; Mm.20257; -.
DR   ProteinModelPortal; Q9D8X1; -.
DR   SMR; Q9D8X1; 23-271.
DR   STRING; Q9D8X1; -.
DR   PRIDE; Q9D8X1; -.
DR   Ensembl; ENSMUST00000112047; ENSMUSP00000107678; ENSMUSG00000025193.
DR   GeneID; 66388; -.
DR   KEGG; mmu:66388; -.
DR   UCSC; uc008hov.1; mouse.
DR   CTD; 66388; -.
DR   MGI; MGI:1913638; Cutc.
DR   GeneTree; ENSGT00390000008454; -.
DR   HOGENOM; HBG535337; -.
DR   HOVERGEN; HBG051267; -.
DR   InParanoid; Q9D8X1; -.
DR   OMA; PVYAMIR; -.
DR   OrthoDB; EOG4VT5Z1; -.
DR   PhylomeDB; Q9D8X1; -.
DR   NextBio; 321525; -.
DR   ArrayExpress; Q9D8X1; -.
DR   Bgee; Q9D8X1; -.
DR   CleanEx; MM_CUTC; -.
DR   Genevestigator; Q9D8X1; -.
DR   GermOnline; ENSMUSG00000025193; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
DR   GO; GO:0055070; P:copper ion homeostasis; IEA:InterPro.
DR   InterPro; IPR005627; CutC.
DR   Gene3D; G3DSA:3.20.20.380; CutC; 1.
DR   PANTHER; PTHR12598; CutC; 1.
DR   Pfam; PF03932; CutC; 1.
DR   SUPFAM; SSF110395; CutC; 1.
PE   2: Evidence at transcript level;
KW   Copper; Cytoplasm; Metal-binding; Nucleus.
FT   CHAIN         1    272       Copper homeostasis protein cutC homolog.
FT                                /FTId=PRO_0000215089.
SQ   SEQUENCE   272 AA;  29004 MW;  7FE099BCDDA2512C CRC64;
     MKKGASCERK QAWISSGKAG AGNGFLMEVC VDSVESAVNA ERGGAGRIEL CSGLLEGGTT
     PSMGVLQVVK QSVQIPVFVM IRPRGGDFLY SDREVEVMKA DIRLAKLYGA DGLVFGALTE
     DGHIDKELCL SLVALCRPLP VTFHRAFDMV HDPMAALETL LTLGFERVLT SGCDSSALEG
     LPLIKQLIDQ AKGRIVVMPG GGITDKNLQR ILEGSGATEF HCSARSSRDS GMKFRNSSVA
     MGASLAHSEY SLKVTDVTKV RTLNAIAKDV LV
//
ID   EFHD2_MOUSE             Reviewed;         240 AA.
AC   Q9D8Y0; Q9D0P4;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=EF-hand domain-containing protein D2;
DE   AltName: Full=Swiprosin-1;
GN   Name=Efhd2; Synonyms=Sws1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PROTEIN SEQUENCE OF 177-188 AND 198-206, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15749887;
RA   Mielenz D., Vettermann C., Hampel M., Lang C., Avramidou A., Karas M.,
RA   Jacek H.-M.;
RT   "Lipid rafts associate with intracellular B cell receptors and exhibit
RT   a B cell stage-specific protein composition.";
RL   J. Immunol. 174:3508-3517(2005).
RN   [4]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=17673920; DOI=10.1038/sj.cdd.4402206;
RA   Avramidou A., Kroczek C., Lang C., Schuh W., Jaeck H.-M., Mielenz D.;
RT   "The novel adaptor protein Swiprosin-1 enhances BCR signals and
RT   contributes to BCR-induced apoptosis.";
RL   Cell Death Differ. 14:1936-1947(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-83, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May regulate B-cell receptor (BCR)-induced immature and
CC       primary B-cell apoptosis. Plays a role as negative regulator of
CC       the canonical NF-kappa-B-activating branch. Controls spontaneous
CC       apoptosis through the regulation of BCL2L1 abundance.
CC   -!- SUBUNIT: Interacts with CASP9; with inactive form (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane raft. Note=In immature B-cell line
CC       WEHI231.
CC   -!- TISSUE SPECIFICITY: Detected in thymus, kidney, spleen, lung,
CC       liver and brain. Highest abundance in brain and lowest in kidney
CC       and thymus.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout B-cell differentiation,
CC       with highest expression in immature bone marrow B cells.
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK007560; BAB25108.1; -; mRNA.
DR   EMBL; AK011219; BAB27476.1; -; mRNA.
DR   IPI; IPI00112223; -.
DR   UniGene; Mm.395598; -.
DR   ProteinModelPortal; Q9D8Y0; -.
DR   SMR; Q9D8Y0; 88-239.
DR   STRING; Q9D8Y0; -.
DR   PhosphoSite; Q9D8Y0; -.
DR   REPRODUCTION-2DPAGE; Q9D8Y0; -.
DR   PRIDE; Q9D8Y0; -.
DR   Ensembl; ENSMUST00000036854; ENSMUSP00000044502; ENSMUSG00000040659.
DR   MGI; MGI:106504; Efhd2.
DR   GeneTree; ENSGT00390000012058; -.
DR   HOGENOM; HBG716095; -.
DR   HOVERGEN; HBG051446; -.
DR   InParanoid; Q9D8Y0; -.
DR   OrthoDB; EOG4THVVM; -.
DR   ArrayExpress; Q9D8Y0; -.
DR   Bgee; Q9D8Y0; -.
DR   CleanEx; MM_EFHD2; -.
DR   Genevestigator; Q9D8Y0; -.
DR   GermOnline; ENSMUSG00000040659; Mus musculus.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   SMART; SM00054; EFh; 2.
DR   PROSITE; PS00018; EF_HAND_1; FALSE_NEG.
DR   PROSITE; PS50222; EF_HAND_2; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Calcium; Direct protein sequencing; Membrane;
KW   Phosphoprotein; Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    240       EF-hand domain-containing protein D2.
FT                                /FTId=PRO_0000073646.
FT   DOMAIN       92    127       EF-hand 1.
FT   DOMAIN      128    163       EF-hand 2.
FT   CA_BIND     105    116       1 (Potential).
FT   CA_BIND     141    152       2 (Potential).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      74     74       Phosphoserine.
FT   MOD_RES      76     76       Phosphoserine (By similarity).
FT   MOD_RES      83     83       Phosphotyrosine.
FT   MOD_RES     233    233       N6-acetyllysine (By similarity).
FT   CONFLICT     14     14       L -> V (in Ref. 1; BAB27476).
FT   CONFLICT    172    172       Q -> H (in Ref. 1; BAB27476).
SQ   SEQUENCE   240 AA;  26791 MW;  F11E549BFCB2C247 CRC64;
     MATDELASKL SRRLQMEGEG GEATEQPGLN GAAAAAAAEA PDETAQALGS ADDELSAKLL
     RRADLNQGIG EPQSPSRRVF NPYTEFKEFS RKQIKDMEKM FKQYDAGRDG FIDLMELKLM
     MEKLGAPQTH LGLKSMIQEV DEDFDSKLSF REFLLIFRKA AAGELQEDSG LQVLARLSEI
     DVSTEGVKGA KNFFEAKVQA INVSSRFEEE IKAEQEERKK QAEEVKQRKA AFKELQSTFK
//
ID   ATG7_MOUSE              Reviewed;         698 AA.
AC   Q9D906; Q3TCD9; Q8K4Q5;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Ubiquitin-like modifier-activating enzyme ATG7;
DE   AltName: Full=ATG12-activating enzyme E1 ATG7;
DE   AltName: Full=Autophagy-related protein 7;
DE            Short=APG7-like;
DE            Short=mAGP7;
DE   AltName: Full=Ubiquitin-activating enzyme E1-like protein;
GN   Name=Atg7; Synonyms=Apg7l;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN GABARAPL1-ATG7 INTERMEDIATE
RP   CONJUGATE FORMATION, TISSUE SPECIFICITY, INTERACTION WITH ATG12, AND
RP   MUTAGENESIS OF CYS-567.
RC   TISSUE=Brain;
RX   MEDLINE=21888283; PubMed=11890701; DOI=10.1006/bbrc.2002.6645;
RA   Tanida I., Tanida-Miyake E., Nishitani T., Komatsu M., Yamazaki H.,
RA   Ueno T., Kominami E.;
RT   "Murine Apg12p has a substrate preference for murine Apg7p over three
RT   Apg8p homologs.";
RL   Biochem. Biophys. Res. Commun. 292:256-262(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Pancreas, Spleen, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH ATG10 AND ATG12.
RX   MEDLINE=22370793; PubMed=12482611; DOI=10.1016/S0014-5793(02)03739-0;
RA   Mizushima N., Yoshimori T., Ohsumi Y.;
RT   "Mouse Apg10 as an Apg12-conjugating enzyme: analysis by the
RT   conjugation-mediated yeast two-hybrid method.";
RL   FEBS Lett. 532:450-454(2002).
RN   [5]
RP   FUNCTION.
RX   PubMed=20723759; DOI=10.1016/j.cell.2010.07.018;
RA   Radoshevich L., Murrow L., Chen N., Fernandez E., Roy S., Fung C.,
RA   Debnath J.;
RT   "ATG12 conjugation to ATG3 regulates mitochondrial homeostasis and
RT   cell death.";
RL   Cell 142:590-600(2010).
CC   -!- FUNCTION: Functions as an E1 enzyme essential for multisubstrates
CC       such as ATG8-like proteins and ATG12. Forms intermediate
CC       conjugates with ATG8-like proteins (GABARAP, GABARAPL1, GABARAPL2
CC       or MAP1LC3A). PE-conjugation to ATG8-like proteins is essential
CC       for autophagy. Also acts as an E1 enzyme for ATG12 conjugation to
CC       ATG5 and ATG3.
CC   -!- SUBUNIT: Homodimer. Interacts with ATG3 and ATG12. The complex,
CC       composed of ATG3 and ATG7, plays a role in the conjugation of
CC       ATG12 to ATG5 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- TISSUE SPECIFICITY: Widely expressed, especially in kidney, liver,
CC       lymph nodes and bone marrow.
CC   -!- DOMAIN: The C-terminal part of the protein is essential for the
CC       dimerization and interaction with ATG3 and ATG12 (By similarity).
CC   -!- SIMILARITY: Belongs to the ATG7 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB079385; BAC10416.1; -; mRNA.
DR   EMBL; AK007484; BAB25060.1; -; mRNA.
DR   EMBL; AK035604; BAC29122.1; -; mRNA.
DR   EMBL; AK161133; BAE36208.1; -; mRNA.
DR   EMBL; AK170769; BAE42018.1; -; mRNA.
DR   EMBL; AK172272; BAE42917.1; -; mRNA.
DR   EMBL; BC058597; AAH58597.1; -; mRNA.
DR   IPI; IPI00463195; -.
DR   RefSeq; NP_083111.1; NM_028835.3.
DR   UniGene; Mm.275332; -.
DR   ProteinModelPortal; Q9D906; -.
DR   SMR; Q9D906; 347-502.
DR   STRING; Q9D906; -.
DR   PhosphoSite; Q9D906; -.
DR   PRIDE; Q9D906; -.
DR   Ensembl; ENSMUST00000032457; ENSMUSP00000032457; ENSMUSG00000030314.
DR   GeneID; 74244; -.
DR   KEGG; mmu:74244; -.
DR   UCSC; uc009dhz.1; mouse.
DR   CTD; 74244; -.
DR   MGI; MGI:1921494; Atg7.
DR   GeneTree; ENSGT00390000017509; -.
DR   HOGENOM; HBG619497; -.
DR   HOVERGEN; HBG080877; -.
DR   InParanoid; Q9D906; -.
DR   OMA; ANEIWES; -.
DR   OrthoDB; EOG43N7C8; -.
DR   PhylomeDB; Q9D906; -.
DR   NextBio; 340222; -.
DR   ArrayExpress; Q9D906; -.
DR   Bgee; Q9D906; -.
DR   CleanEx; MM_ATG7; -.
DR   Genevestigator; Q9D906; -.
DR   GermOnline; ENSMUSG00000030314; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019778; F:APG12 activating enzyme activity; IMP:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004839; F:ubiquitin activating enzyme activity; IDA:MGI.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0006914; P:autophagy; IMP:MGI.
DR   GO; GO:0055013; P:cardiac muscle cell development; IMP:MGI.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IMP:MGI.
DR   GO; GO:0016044; P:cellular membrane organization; IMP:MGI.
DR   GO; GO:0021955; P:central nervous system neuron axonogenesis; IMP:MGI.
DR   GO; GO:0021680; P:cerebellar Purkinje cell layer development; IMP:MGI.
DR   GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR   GO; GO:0001889; P:liver development; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptosis; IMP:MGI.
DR   GO; GO:0050877; P:neurological system process; IMP:MGI.
DR   GO; GO:0006996; P:organelle organization; IMP:MGI.
DR   GO; GO:0031401; P:positive regulation of protein modification process; IDA:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0030163; P:protein catabolic process; IMP:MGI.
DR   GO; GO:0032446; P:protein modification by small protein conjugation; IMP:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0021860; P:pyramidal neuron development; IMP:MGI.
DR   GO; GO:0031396; P:regulation of protein ubiquitination; IMP:MGI.
DR   GO; GO:0042594; P:response to starvation; IMP:MGI.
DR   InterPro; IPR006285; E1-like_Apg7.
DR   InterPro; IPR009036; Molybdenum_cofac_synth_MoeB.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 2.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; MoeB; 1.
DR   TIGRFAMs; TIGR01381; E1_like_apg7; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Autophagy; Cytoplasm; Protein transport; Transport;
KW   Ubl conjugation pathway.
FT   CHAIN         1    698       Ubiquitin-like modifier-activating enzyme
FT                                ATG7.
FT                                /FTId=PRO_0000212807.
FT   ACT_SITE    567    567       Glycyl thioester intermediate (Probable).
FT   MOD_RES     302    302       N6-acetyllysine (By similarity).
FT   MUTAGEN     567    567       C->S: Instead of the formation of an
FT                                intermediate complex with a thiol ester
FT                                bond between ATG7 (E1-like enzyme) and
FT                                GABARAPL1 (MAP1LC3, GABARAP or GABARAPL;
FT                                substrates), a stable complex with an O-
FT                                ester bond is formed.
FT   CONFLICT     22     22       F -> L (in Ref. 1; BAC10416).
SQ   SEQUENCE   698 AA;  77520 MW;  79D94EA7464C6ADB CRC64;
     MGDPGLAKLQ FAPFNSALDV GFWHELTQKK LNEYRLDEAP KDIKGYYYNG DSAGLPTRLT
     LEFSAFDMSA STPAHCCPAM GTLHNTNTLE AFKTADKKLL LEQSANEIWE AIKSGAALEN
     PMLLNKFLLL TFADLKKYHF YYWFCCPALC LPESIPLIRG PVSLDQRLSP KQIQALEHAY
     DDLCRAEGVT ALPYFLFKYD DDTVLVSLLK HYSDFFQGQR TKITVGVYDP CNLAQYPGWP
     LRNFLVLAAH RWSGSFQSVE VLCFRDRTMQ GARDVTHSII FEVKLPEMAF SPDCPKAVGW
     EKNQKGGMGP RMVNLSGCMD PKRLAESSVD LNLKLMCWRL VPTLDLDKVV SVKCLLLGAG
     TLGCNVARTL MGWGVRHVTF VDNAKISYSN PVRQPLYEFE DCLGGGKPKA LAAAERLQKI
     FPGVNARGFN MSIPMPGHPV NFSDVTMEQA RRDVEQLEQL IDNHDVIFLL MDTRESRWLP
     TVIAASKRKL VINAALGFDT FVVMRHGLKK PKQQGAGDLC PSHLVAPADL GSSLFANIPG
     YKLGCYFCND VVAPGDSTRD RTLDQQCTVS RPGLAVIAGA LAVELMVSVL QHPEGGYAIA
     SSSDDRMNEP PTSLGLVPHQ IRGFLSRFDN VLPVSLAFDK CTACSPKVLD QYEREGFTFL
     AKVFNSSHSF LEDLTGLTLL HQETQAAEIW DMSDEETV
//
ID   L12R1_MOUSE             Reviewed;         195 AA.
AC   Q9D920; Q8BJB0;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Loss of heterozygosity 12 chromosomal region 1 protein homolog;
GN   Name=Loh12cr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Pancreas, Spleen, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the LOH12CR1 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK007423; BAB25030.1; -; mRNA.
DR   EMBL; AK089648; BAC40938.1; -; mRNA.
DR   EMBL; AK151342; BAE30320.1; -; mRNA.
DR   EMBL; AK169615; BAE41262.1; -; mRNA.
DR   EMBL; BC023059; AAH23059.1; -; mRNA.
DR   IPI; IPI00457620; -.
DR   RefSeq; NP_001163950.1; NM_001170479.1.
DR   RefSeq; NP_080647.2; NM_026371.3.
DR   UniGene; Mm.41892; -.
DR   ProteinModelPortal; Q9D920; -.
DR   PhosphoSite; Q9D920; -.
DR   PRIDE; Q9D920; -.
DR   Ensembl; ENSMUST00000062755; ENSMUSP00000054913; ENSMUSG00000042992.
DR   GeneID; 67774; -.
DR   KEGG; mmu:67774; -.
DR   UCSC; uc009ekn.1; mouse.
DR   CTD; 67774; -.
DR   MGI; MGI:1915024; Loh12cr1.
DR   eggNOG; roNOG15729; -.
DR   GeneTree; ENSGT00390000015016; -.
DR   HOGENOM; HBG447299; -.
DR   HOVERGEN; HBG108081; -.
DR   InParanoid; Q9D920; -.
DR   OMA; PFSMRPD; -.
DR   OrthoDB; EOG4JDH7T; -.
DR   PhylomeDB; Q9D920; -.
DR   NextBio; 325533; -.
DR   ArrayExpress; Q9D920; -.
DR   Bgee; Q9D920; -.
DR   Genevestigator; Q9D920; -.
DR   InterPro; IPR018780; Tumour_suppressor_LOH1CR12.
DR   Pfam; PF10158; LOH1CR12; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein.
FT   CHAIN         1    195       Loss of heterozygosity 12 chromosomal
FT                                region 1 protein homolog.
FT                                /FTId=PRO_0000318597.
FT   MOD_RES      75     75       Phosphoserine (By similarity).
FT   CONFLICT     58     58       E -> K (in Ref. 1; BAC40938).
SQ   SEQUENCE   195 AA;  22120 MW;  F3DF9A7520D35D51 CRC64;
     MGSEQSAEAE SRPGDLNASV TPSPAKHRAK MDDIVVVAQG SQASRNVSND PDVIKLQEIP
     TFQPLLKGLL SGQTSPTNAK LEKLDSQQVL QLCLRYQDHL HQCAEAVAFD QNALVKRIKE
     MDLSVETLFC FMQERQKRYA KYAEQIQKVN EMSAILRRIQ MGIDQTVPLM ERLNSMLPEA
     ERLEPFSMKP ERERH
//
ID   ISCA1_MOUSE             Reviewed;         129 AA.
AC   Q9D924; Q5SZT5;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Iron-sulfur cluster assembly 1 homolog, mitochondrial;
DE   AltName: Full=HESB-like domain-containing protein 2;
DE   AltName: Full=Iron-sulfur assembly protein IscA;
DE   Flags: Precursor;
GN   Name=Isca1; Synonyms=Hbld2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Amnion, Embryo, Kidney, Pancreas, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Involved in the assembly of mitochondrial iron-sulfur
CC       proteins. Probably involved in the binding of an intermediate of
CC       Fe/S cluster assembly (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the hesB/iscA family.
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DR   EMBL; AK007415; BAB25025.1; -; mRNA.
DR   EMBL; AK045175; BAC32248.1; -; mRNA.
DR   EMBL; AK090000; BAC41037.1; -; mRNA.
DR   EMBL; AK153820; BAE32196.1; -; mRNA.
DR   EMBL; AK169028; BAE40820.1; -; mRNA.
DR   EMBL; AL589742; CAI25004.1; -; Genomic_DNA.
DR   EMBL; BC018547; AAH18547.1; -; mRNA.
DR   EMBL; BC085482; AAH85482.1; -; mRNA.
DR   IPI; IPI00720014; -.
DR   RefSeq; NP_081197.1; NM_026921.4.
DR   RefSeq; XP_484225.3; XM_484225.6.
DR   RefSeq; XP_985754.2; XM_980660.3.
DR   UniGene; Mm.390551; -.
DR   UniGene; Mm.7884; -.
DR   ProteinModelPortal; Q9D924; -.
DR   SMR; Q9D924; 19-129.
DR   STRING; Q9D924; -.
DR   PRIDE; Q9D924; -.
DR   Ensembl; ENSMUST00000057115; ENSMUSP00000054858; ENSMUSG00000044792.
DR   GeneID; 432732; -.
DR   GeneID; 69046; -.
DR   KEGG; mmu:432732; -.
DR   KEGG; mmu:69046; -.
DR   UCSC; uc007qvd.1; mouse.
DR   CTD; 432732; -.
DR   CTD; 69046; -.
DR   MGI; MGI:1916296; Isca1.
DR   eggNOG; roNOG16488; -.
DR   GeneTree; ENSGT00490000043385; -.
DR   HOGENOM; HBG730174; -.
DR   HOVERGEN; HBG081809; -.
DR   InParanoid; Q9D924; -.
DR   OMA; GMEYTID; -.
DR   OrthoDB; EOG4GHZQK; -.
DR   PhylomeDB; Q9D924; -.
DR   NextBio; 328458; -.
DR   ArrayExpress; Q9D924; -.
DR   Bgee; Q9D924; -.
DR   Genevestigator; Q9D924; -.
DR   GermOnline; ENSMUSG00000044792; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR   InterPro; IPR000361; FeS_biogenesis.
DR   InterPro; IPR016092; FeS_cluster_insertion.
DR   InterPro; IPR017870; FeS_cluster_insertion_CS.
DR   Gene3D; G3DSA:2.60.300.12; HesB_yadR_yfhF; 1.
DR   PANTHER; PTHR10072; HesB_yadR_yfhF; 1.
DR   Pfam; PF01521; Fe-S_biosyn; 1.
DR   SUPFAM; SSF89360; HesB_yadR_yfhF-like; 1.
DR   TIGRFAMs; TIGR00049; HesB_yadR_yfhF; 1.
DR   PROSITE; PS01152; HESB; 1.
PE   2: Evidence at transcript level;
KW   Iron; Iron-sulfur; Metal-binding; Mitochondrion; Transit peptide.
FT   TRANSIT       1     12       Mitochondrion (Potential).
FT   CHAIN        13    129       Iron-sulfur cluster assembly 1 homolog,
FT                                mitochondrial.
FT                                /FTId=PRO_0000042736.
FT   CONFLICT     11     11       R -> W (in Ref. 2; CAI25004).
SQ   SEQUENCE   129 AA;  14188 MW;  3E2133D641688233 CRC64;
     MSASLVRATV RAVSKRKLQP TRAALTLTPS AVNKIKQLLK DKPEHVGLKV GVRTRGCNGL
     SYSLEYTKTK GDSDEEVIQD GVRVFIEKKA QLTLLGTEMD YVEDKLSSEF VFNNPNIKGT
     CGCGESFHV
//
ID   Q9D927_MOUSE            Unreviewed;       233 AA.
AC   Q9D927;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   30-NOV-2010, entry version 51.
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=1810009N02Rik;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RA   Adachi J., Aizawa K., Akahira S., Akimura T., Arai A., Aono H.,
RA   Arakawa T., Bono H., Carninci P., Fukuda S., Fukunishi Y., Furuno M.,
RA   Hanagaki T., Hara A., Hayatsu N., Hiramoto K., Hiraoka T., Hori F.,
RA   Imotani K., Ishii Y., Itoh M., Izawa M., Kasukawa T., Kato H.,
RA   Kawai J., Kojima Y., Konno H., Kouda M., Koya S., Kurihara C.,
RA   Matsuyama T., Miyazaki A., Nishi K., Nomura K., Numazaki R., Ohno M.,
RA   Okazaki Y., Okido T., Owa C., Saito H., Saito R., Sakai C., Sakai K.,
RA   Sano H., Sasaki D., Shibata K., Shibata Y., Shinagawa A., Shiraki T.,
RA   Sogabe Y., Suzuki H., Tagami M., Tagawa A., Takahashi F., Tanaka T.,
RA   Tejima Y., Toya T., Yamamura T., Yasunishi A., Yoshida K., Yoshino M.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AK007409; BAB25021.1; -; mRNA.
DR   IPI; IPI00111946; -.
DR   RefSeq; NP_081215.1; NM_026939.1.
DR   UniGene; Mm.423020; -.
DR   HSSP; Q02169; 1EX2.
DR   ProteinModelPortal; Q9D927; -.
DR   SMR; Q9D927; 10-210.
DR   PRIDE; Q9D927; -.
DR   GeneID; 69099; -.
DR   KEGG; mmu:69099; -.
DR   MGI; MGI:1916349; 1810009N02Rik.
DR   PhylomeDB; Q9D927; -.
DR   NextBio; 328602; -.
DR   Genevestigator; Q9D927; -.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   HAMAP; MF_00528; Maf; 1; -.
DR   InterPro; IPR003697; Maf.
DR   Pfam; PF02545; Maf; 1.
DR   PIRSF; PIRSF006305; Maf; 1.
DR   TIGRFAMs; TIGR00172; maf; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   233 AA;  25066 MW;  342345E0E7C577DC CRC64;
     MSLTSLALSL RSRRVVLASA SPRRKEILGL TGVALEVVPP RFPETLSKAA WPRPQDYARE
     TATGKAQEVA ARLVQEDPET PTIVIGADTV VAVDGRILEK PKDREDALGD LRSLSGKQHQ
     VITGVAIVTW GGCEGPAQEV TAFHEETSVT FSPLSEELIR EYTDSGEGWD KAGAYAIQAR
     GAMLVQDVAG DVLNAVGFPL NRFCRELARV PPTRTGSEEV TSQTTGIDSK DVK
//
ID   PO5F2_MOUSE             Reviewed;         329 AA.
AC   Q9DAC9; Q8BVS2;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=POU domain, class 5, transcription factor 2;
DE   AltName: Full=Sperm 1 POU domain transcription factor;
DE            Short=SPRM-1;
GN   Name=Pou5f2; Synonyms=Sprm1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=94192665; PubMed=7908264;
RX   DOI=10.1111/j.1432-1033.1994.tb18676.x;
RA   Wey E., Lyons G.E., Schaefer B.W.;
RT   "A human POU domain gene, mPOU, is expressed in developing brain and
RT   specific adult tissues.";
RL   Eur. J. Biochem. 220:753-762(1994).
CC   -!- FUNCTION: Transcription factor that binds preferentially to the
CC       octamer motif (5'-ATGTTAAT-3'). May exert a regulatory function in
CC       meiotic events that are required for terminal differentiation of
CC       male germ cell (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- TISSUE SPECIFICITY: In adult brain, expressed in the olfactory
CC       bulb, becoming specifically concentrated in the mitral cell layer.
CC       Also found in the pyramidal cell layer of the hippocampus, in the
CC       granule cell layer of the cerebellum and in the cortex.
CC   -!- DEVELOPMENTAL STAGE: Low expression levels observed at 12 dpc in
CC       neural tube and brain. On days 15.5 and 16.5, expression levels
CC       increased and became localized specifically to the forebrain, with
CC       highest levels found in the laminar region of the forebrain
CC       cortex. Also expressed in the mitral region of the olfactory bulb.
CC   -!- SIMILARITY: Belongs to the POU transcription factor family. Class-
CC       5 subfamily.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
CC   -!- SIMILARITY: Contains 1 POU-specific domain.
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DR   EMBL; AK005948; BAB24332.1; -; mRNA.
DR   EMBL; AK076753; BAC36466.1; -; mRNA.
DR   IPI; IPI00344731; -.
DR   RefSeq; NP_083591.1; NM_029315.1.
DR   UniGene; Mm.443255; -.
DR   ProteinModelPortal; Q9DAC9; -.
DR   SMR; Q9DAC9; 107-256.
DR   PRIDE; Q9DAC9; -.
DR   GeneID; 75507; -.
DR   KEGG; mmu:75507; -.
DR   CTD; 75507; -.
DR   MGI; MGI:1922757; Pou5f2.
DR   HOVERGEN; HBG057998; -.
DR   Genevestigator; Q9DAC9; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR001356; Homeobox.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR010982; Lambda_DNA-bd.
DR   InterPro; IPR013847; POU.
DR   InterPro; IPR000327; POU_specific.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Pfam; PF00046; Homeobox; 1.
DR   Pfam; PF00157; Pou; 1.
DR   PRINTS; PR00028; POUDOMAIN.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00352; POU; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
DR   SUPFAM; SSF47413; Lambda_like_DNA; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; FALSE_NEG.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00035; POU_1; 1.
DR   PROSITE; PS00465; POU_2; 1.
DR   PROSITE; PS51179; POU_3; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Homeobox; Nucleus; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    329       POU domain, class 5, transcription factor
FT                                2.
FT                                /FTId=PRO_0000100757.
FT   DOMAIN      107    181       POU-specific.
FT   DNA_BIND    199    258       Homeobox.
FT   CONFLICT    292    292       T -> P (in Ref. 1; BAC36466).
SQ   SEQUENCE   329 AA;  36411 MW;  A882639979987F31 CRC64;
     MAGRRSSNVF PLSGNSGGGL EVDTPTWLSS QAATSRLMVR PSMGPGICPG PEVWGVPLGS
     SPYEFRGGIA PYRACEARAW SQSSSEDTCP GPYIALRYMP NLALPEDVSA IQKEMEQLAK
     ELRQKRMTLG YSQADVGFAV GAMFGKVLSQ TTICRFEAQQ LSLANMWKLR PLLKMWLEEV
     DEKNLLGICR MEMILEQARK RRRASRERRI GSNLEKLFLQ CPEPTPQQIS YIAGRLRLQK
     DLVQVWFSNR SQMGSWPTND TSRREDVGAT GSPFPGPPVC FPMAPGLHFD FTHYEGSCLT
     PLYSSTPFPV RGALLSAPTT TLGLPRLSS
//
ID   F135B_MOUSE             Reviewed;        1403 AA.
AC   Q9DAI6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 3.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=Protein FAM135B;
GN   Name=Fam135b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 982-1403.
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 982-1403.
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the FAM135 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI19175.1; Type=Erroneous initiation;
CC       Sequence=BAB24252.2; Type=Erroneous initiation;
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DR   EMBL; AC125528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC157277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC157602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK005816; BAB24252.2; ALT_INIT; mRNA.
DR   EMBL; BC119174; AAI19175.1; ALT_INIT; mRNA.
DR   IPI; IPI00282805; -.
DR   RefSeq; NP_808487.2; NM_177819.3.
DR   UniGene; Mm.126450; -.
DR   ProteinModelPortal; Q9DAI6; -.
DR   PRIDE; Q9DAI6; -.
DR   Ensembl; ENSMUST00000022953; ENSMUSP00000022953; ENSMUSG00000036800.
DR   GeneID; 70363; -.
DR   KEGG; mmu:70363; -.
DR   UCSC; uc007wbh.1; mouse.
DR   CTD; 70363; -.
DR   MGI; MGI:1917613; Fam135b.
DR   GeneTree; ENSGT00390000007885; -.
DR   HOGENOM; HBG444070; -.
DR   HOVERGEN; HBG107866; -.
DR   InParanoid; Q9DAI6; -.
DR   OrthoDB; EOG4TXBR5; -.
DR   ArrayExpress; Q9DAI6; -.
DR   Bgee; Q9DAI6; -.
DR   Genevestigator; Q9DAI6; -.
DR   InterPro; IPR022122; DUF3657.
DR   InterPro; IPR007751; DUF676_hydro-like.
DR   Pfam; PF12394; DUF3657; 2.
DR   Pfam; PF05057; DUF676; 1.
PE   2: Evidence at transcript level;
FT   CHAIN         1   1403       Protein FAM135B.
FT                                /FTId=PRO_0000314172.
SQ   SEQUENCE   1403 AA;  155524 MW;  FD949E39FEDF060B CRC64;
     MSEVQGTVEF SVELHKFYNV DLFQRGYYQI RVTLKVSSRI PHRLSASIVG QSESSSLHSA
     CVHESAVHSR VFQILYRNEE VSINDAMLFR VHLLLDGERV EDALSEVEFQ LKVDLHFTDS
     EQQLRDVTGT PMISSRTLGL HFHPRRGLHH QVPVMFDYFH LSVISVAIHA ALVALQQPLI
     SFTRPGRGSW LGKGGPDTGP EQPTISLENL VFGAGYCKPT SSEGSFYVPS ENCIQHAHKW
     HRDLCLLLLH AYQGLRLYFL VIMRDIPELP TMELEALAVE ETLSQLCSEL QMLNNPEKIA
     EQISKDLAWL ASHLMALWTQ FLDTVTLHSQ VTTYLTQEHH TLRVRRFSEA FFYMEHQKLA
     VLTFQENLIQ THSQLSLDIR NSEYLTSMPP LPAECLDIDG DWNTLPVIFE DRYVDCPVSG
     HNLSVYPNFD VPVTSPAIMN LKGKEKNLIN QNSSSRKDIP LSTTEAPQLG SDEDVTRRPE
     VQENVSTWNP IDVCSESQVY LTIGEFQNRA GIPEDECWTG PRPDAVKDSL TDTDICSRSP
     GPDEGQTPAL TYIDVQSSNK YCPRAELVQG INVQHEHRSS RESYGIVKTV PSKVVAGTSQ
     NNSTSLNQTA ALELRTLGRG VNQDGKPVLL SLKLTPAEPC DPPSTALREA LDTKPSQPDH
     AEEPEDLSAL SGVIKRSASI ISDSGIESEP SSVAWSEARS RALELPSDRD VLHQVVRRHA
     HHRNSLEGGH TESNTSLPSG IQASLSSISS LPFEEEEREL ALNKLTKSVS APQISSPEES
     AEGADTIKNT AGFSEDLDPS SKENSPPRHT SLSYGGSRVQ DVRAGHSLAD IALDSDRPQG
     PGYMDIPNDK GNHPELQEPC CLDGMAETPL HVETKGLNLK IPCTIVLENS KSRSFHRAAG
     ETAKGKPEEL SMSKCVLSNN SISEVRAASH HRVPEISCSP AVEAVNLNST GVQNSSLSVN
     DTMTLNRRHN ASLEAKHEAG TVCPTVTHTI ASQVSRNQEL KTGTSISGSH LNSTEAFTLD
     SLKAVEVVNL SVSCTATCLP FSSVPKETPA RAGLSSKQNP APITHQPLGS FGVVSTYSSK
     LEEEVSERMF SFYQAKEKFK KELKIEGFLY SDLSVLASDI PYFPPEEEEE NLEDGIHLVV
     CVHGLDGNSA DLRLVKTFIE LGLPGGKLDF LMSEKNQTDT FADFDTMTDR LLDEIIQHIQ
     LYNLSISRIS FIGHSLGNII IRSVLTRPRF RYYLNKLHTF LSLSGPHLGT LYNNSTLVST
     GLWLMQKLKK SGSLLQLTFR DNADLRKCFL YQLSQKTGLQ YFKNVVLVAS PQDRYVPFHS
     ARIEMCKTAL KDRHTGPVYA EMINNLLGPL VEAKDCTLIR HNVFHALPNT ANTLIGRAAH
     IAVLDSELFL EKFFLVAGLN YFK
//
ID   GBG12_MOUSE             Reviewed;          72 AA.
AC   Q9DAS9; Q544P3;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12;
DE   Flags: Precursor;
GN   Name=Gng12;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cecum, Colon, Lung, Mammary gland, Placenta, and
RC   Sympathetic ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10 AND SER-26, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC       involved as a modulator or transducer in various transmembrane
CC       signaling systems. The beta and gamma chains are required for the
CC       GTPase activity, for replacement of GDP by GTP, and for G protein-
CC       effector interaction.
CC   -!- SUBUNIT: G proteins are composed of 3 units, alpha, beta and
CC       gamma.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- SIMILARITY: Belongs to the G protein gamma family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK005561; BAB24121.1; -; mRNA.
DR   EMBL; AK033422; BAC28280.1; -; mRNA.
DR   EMBL; AK148765; BAE28660.1; -; mRNA.
DR   EMBL; AK159872; BAE35445.1; -; mRNA.
DR   EMBL; AK162342; BAE36863.1; -; mRNA.
DR   EMBL; AK166035; BAE38536.1; -; mRNA.
DR   EMBL; AK166299; BAE38688.1; -; mRNA.
DR   EMBL; BC040685; AAH40685.1; -; mRNA.
DR   IPI; IPI00227838; -.
DR   RefSeq; NP_001171027.1; NM_001177556.1.
DR   RefSeq; NP_001171028.1; NM_001177557.1.
DR   RefSeq; NP_001171029.1; NM_001177558.1.
DR   RefSeq; NP_001171030.1; NM_001177559.1.
DR   RefSeq; NP_001171031.1; NM_001177560.1.
DR   RefSeq; NP_079554.1; NM_025278.5.
DR   UniGene; Mm.234342; -.
DR   ProteinModelPortal; Q9DAS9; -.
DR   SMR; Q9DAS9; 10-53.
DR   STRING; Q9DAS9; -.
DR   PhosphoSite; Q9DAS9; -.
DR   PRIDE; Q9DAS9; -.
DR   Ensembl; ENSMUST00000043148; ENSMUSP00000046557; ENSMUSG00000036402.
DR   Ensembl; ENSMUST00000114222; ENSMUSP00000109860; ENSMUSG00000036402.
DR   Ensembl; ENSMUST00000114224; ENSMUSP00000109862; ENSMUSG00000036402.
DR   Ensembl; ENSMUST00000114225; ENSMUSP00000109863; ENSMUSG00000036402.
DR   Ensembl; ENSMUST00000114226; ENSMUSP00000109864; ENSMUSG00000036402.
DR   Ensembl; ENSMUST00000114227; ENSMUSP00000109865; ENSMUSG00000036402.
DR   Ensembl; ENSMUST00000114228; ENSMUSP00000109866; ENSMUSG00000036402.
DR   GeneID; 14701; -.
DR   KEGG; mmu:14701; -.
DR   UCSC; uc009cey.1; mouse.
DR   CTD; 14701; -.
DR   MGI; MGI:1336171; Gng12.
DR   eggNOG; roNOG17490; -.
DR   GeneTree; ENSGT00550000074352; -.
DR   HOGENOM; HBG444905; -.
DR   HOVERGEN; HBG014983; -.
DR   InParanoid; Q9DAS9; -.
DR   OMA; DKKTCTI; -.
DR   OrthoDB; EOG4ZGPF1; -.
DR   PhylomeDB; Q9DAS9; -.
DR   NextBio; 286667; -.
DR   ArrayExpress; Q9DAS9; -.
DR   Bgee; Q9DAS9; -.
DR   Genevestigator; Q9DAS9; -.
DR   GermOnline; ENSMUSG00000036402; Mus musculus.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; IEA:InterPro.
DR   InterPro; IPR015898; G-protein_gamma_dom.
DR   InterPro; IPR001770; Gprotein-gamma.
DR   Gene3D; G3DSA:4.10.260.10; G-protein_gamma_dom; 1.
DR   PANTHER; PTHR13809; Gprotein-gamma; 1.
DR   Pfam; PF00631; G-gamma; 1.
DR   PRINTS; PR00321; GPROTEING.
DR   SMART; SM00224; GGL; 1.
DR   SUPFAM; SSF48670; G-protein_gamma-like; 1.
DR   PROSITE; PS50058; G_PROTEIN_GAMMA; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Lipoprotein; Membrane; Methylation;
KW   Phosphoprotein; Prenylation; Transducer.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2     69       Guanine nucleotide-binding protein
FT                                G(I)/G(S)/G(O) subunit gamma-12.
FT                                /FTId=PRO_0000012669.
FT   PROPEP       70     72       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000012670.
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES      10     10       Phosphoserine.
FT   MOD_RES      26     26       Phosphoserine.
FT   MOD_RES      42     42       Phosphotyrosine (By similarity).
FT   MOD_RES      69     69       Cysteine methyl ester (By similarity).
FT   LIPID        69     69       S-geranylgeranyl cysteine (By
FT                                similarity).
SQ   SEQUENCE   72 AA;  7997 MW;  A4D56F3BD697E7B4 CRC64;
     MSSKTASTNS IAQARRTVQQ LRLEASIERI KVSKASADLM SYCEEHARSD PLLMGIPTSE
     NPFKDKKTCI IL
//
ID   ZFY19_MOUSE             Reviewed;         389 AA.
AC   Q9DAZ9; Q8VCV7;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Zinc finger FYVE domain-containing protein 19;
GN   Name=Zfyve19;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-64; GLN-91;
RP   GLY-94; PRO-157; LEU-164 AND ALA-229.
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [9]
RP   STRUCTURE BY NMR OF 1-75 AND 336-389.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the FYVE domain and the B-box domain of the
RT   zinc finger FYVE domain-containing protein 19 from Mus musculus.";
RL   Submitted (JUN-2006) to the PDB data bank.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK005386; BAB23993.1; -; mRNA.
DR   EMBL; BC018420; AAH18420.1; -; mRNA.
DR   IPI; IPI00119998; -.
DR   RefSeq; NP_082330.2; NM_028054.3.
DR   UniGene; Mm.386807; -.
DR   PDB; 1WFK; NMR; -; A=1-75.
DR   PDB; 2D8V; NMR; -; A=336-389.
DR   PDBsum; 1WFK; -.
DR   PDBsum; 2D8V; -.
DR   ProteinModelPortal; Q9DAZ9; -.
DR   SMR; Q9DAZ9; 1-75, 336-389.
DR   PhosphoSite; Q9DAZ9; -.
DR   PRIDE; Q9DAZ9; -.
DR   Ensembl; ENSMUST00000090174; ENSMUSP00000087636; ENSMUSG00000068580.
DR   GeneID; 72008; -.
DR   KEGG; mmu:72008; -.
DR   UCSC; uc008lti.1; mouse.
DR   CTD; 72008; -.
DR   MGI; MGI:1919258; Zfyve19.
DR   GeneTree; ENSGT00390000016108; -.
DR   HOGENOM; HBG282791; -.
DR   HOVERGEN; HBG057281; -.
DR   InParanoid; Q9DAZ9; -.
DR   OrthoDB; EOG4R7VB7; -.
DR   NextBio; 335208; -.
DR   ArrayExpress; Q9DAZ9; -.
DR   Bgee; Q9DAZ9; -.
DR   CleanEx; MM_ZFYVE19; -.
DR   Genevestigator; Q9DAZ9; -.
DR   GermOnline; ENSMUSG00000068580; Mus musculus.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Metal-binding; Phosphoprotein;
KW   Polymorphism; Zinc; Zinc-finger.
FT   CHAIN         1    389       Zinc finger FYVE domain-containing
FT                                protein 19.
FT                                /FTId=PRO_0000098719.
FT   ZN_FING       1     58       FYVE-type.
FT   COILED      226    261       Potential.
FT   COMPBIAS    332    335       Poly-Glu.
FT   COMPBIAS    339    362       Cys-rich.
FT   MOD_RES      69     69       Phosphoserine (By similarity).
FT   MOD_RES     142    142       Phosphothreonine (By similarity).
FT   MOD_RES     280    280       Phosphoserine.
FT   VARIANT      64     64       N -> S (in strain: FVB/N).
FT   VARIANT      91     91       H -> Q (in strain: FVB/N).
FT   VARIANT      94     94       S -> G (in strain: FVB/N).
FT   VARIANT     157    157       T -> P (in strain: FVB/N).
FT   VARIANT     164    164       P -> L (in strain: FVB/N).
FT   VARIANT     229    229       E -> A (in strain: FVB/N).
FT   TURN          6      8
FT   STRAND       14     16
FT   STRAND       18     20
FT   STRAND       22     24
FT   STRAND       27     29
FT   TURN         30     32
FT   STRAND       35     39
FT   TURN         40     43
FT   STRAND       44     49
FT   HELIX        51     59
FT   STRAND       66     68
FT   TURN        340    342
FT   STRAND      348    350
FT   TURN        351    354
FT   STRAND      355    358
FT   HELIX       362    366
FT   TURN        367    369
FT   TURN        372    374
FT   STRAND      383    386
SQ   SEQUENCE   389 AA;  43276 MW;  BF5CFA4F90785A95 CRC64;
     MESRCYGCAV KFTLFKKEYG CKNCGRAFCN GCLSFSALVP RAGNTQQKVC KQCHTILTRG
     SSDNASKWSP PQNYKKRVAA LEAKKKSSTS HSQSLTHKDQ AIAERLARLR QENKPKSVPS
     QAEIEARLAA LKDEVQGPIP STQEMEDRLA ALQGRVTPSH TVRPAHQAPD TRTQAQQTQD
     LLTQLTAEVA IDENCQPRAS ASLQNDLNKG AARSQRTNSQ GQASQSLEEE KYKLLAEAAV
     ELQEENTRQE RILALAKRLA VLKGQDPSRV TLQDYHLPDS DEDEETAIQR VMQQLTEEAA
     LDEASGFNIP EKPAPGSRAQ PCKAEMEGPQ AEEEELPWCC ICNEDATLRC AGCDGDLYCA
     RCFREGHDNF DLKEHQTSPY HPRRPCQEH
//
ID   SNAA_MOUSE              Reviewed;         295 AA.
AC   Q9DB05; Q543I3;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Alpha-soluble NSF attachment protein;
DE            Short=SNAP-alpha;
DE   AltName: Full=N-ethylmaleimide-sensitive factor attachment protein alpha;
GN   Name=Napa; Synonyms=Snapa;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Cerebellum, Epididymis, Spleen, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 247-264 AND 272-282, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Required for vesicular transport between the endoplasmic
CC       reticulum and the Golgi apparatus (By similarity).
CC   -!- SUBUNIT: Interacts with PRKCABP, and disrupts the interaction
CC       between GRIA2 and PRKCABP, leading to the internalization of
CC       GRIA2. Found in a complex with VAMP8. Component of a SNARE-like
CC       complex that contains at least ZW10, USE1L, RINT1, STX18 and
CC       NAPA/SNAP-alpha (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the SNAP family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK005372; BAB23981.1; -; mRNA.
DR   EMBL; AK050623; BAC34348.1; -; mRNA.
DR   EMBL; AK136689; BAE23100.1; -; mRNA.
DR   EMBL; AK171998; BAE42767.1; -; mRNA.
DR   EMBL; BC004804; AAH04804.1; -; mRNA.
DR   IPI; IPI00118930; -.
DR   RefSeq; NP_080174.1; NM_025898.3.
DR   UniGene; Mm.104540; -.
DR   ProteinModelPortal; Q9DB05; -.
DR   SMR; Q9DB05; 8-293.
DR   STRING; Q9DB05; -.
DR   PhosphoSite; Q9DB05; -.
DR   REPRODUCTION-2DPAGE; Q9DB05; -.
DR   PRIDE; Q9DB05; -.
DR   Ensembl; ENSMUST00000006181; ENSMUSP00000006181; ENSMUSG00000006024.
DR   GeneID; 108124; -.
DR   KEGG; mmu:108124; -.
DR   UCSC; uc009fgw.1; mouse.
DR   CTD; 108124; -.
DR   MGI; MGI:104563; Napa.
DR   eggNOG; roNOG11824; -.
DR   GeneTree; ENSGT00390000005826; -.
DR   HOGENOM; HBG397841; -.
DR   HOVERGEN; HBG001325; -.
DR   InParanoid; Q9DB05; -.
DR   OMA; INCLNRA; -.
DR   OrthoDB; EOG428227; -.
DR   PhylomeDB; Q9DB05; -.
DR   NextBio; 360116; -.
DR   ArrayExpress; Q9DB05; -.
DR   Bgee; Q9DB05; -.
DR   Genevestigator; Q9DB05; -.
DR   GermOnline; ENSMUSG00000006024; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:InterPro.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:InterPro.
DR   GO; GO:0019905; F:syntaxin binding; IDA:MGI.
DR   GO; GO:0045176; P:apical protein localization; IMP:MGI.
DR   GO; GO:0007420; P:brain development; IMP:MGI.
DR   GO; GO:0006886; P:intracellular protein transport; IMP:MGI.
DR   GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000744; NSF_attach.
DR   InterPro; IPR011990; TPR-like_helical.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
DR   PANTHER; PTHR13768; NSF_attach; 1.
DR   PRINTS; PR00448; NSFATTACHMNT.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; ER-Golgi transport; Membrane;
KW   Protein transport; Transport.
FT   CHAIN         1    295       Alpha-soluble NSF attachment protein.
FT                                /FTId=PRO_0000219057.
SQ   SEQUENCE   295 AA;  33190 MW;  30D099B598992AA3 CRC64;
     MDNSGKQAEA MALLAEAERK VKNSQSFFSG LFGGSSKIEE ACEIYARAAN MFKMAKNWSA
     AGNAFCQAAQ LHLQLQSKHD AATCFVDAGN AFKKADPQEA INCLMRAIEI YTDMGRFTIA
     AKHHISIAEI YETELVDVEK AIAHYEQSAD YYKGEESNSS ANKCLLKVAG YAAQLEQYQK
     AIDIYEQVGT SAMDSPLLKY SAKDYFFKAA LCHFCIDMLN AKLAVQKYEE LFPAFSDSRE
     CKLMKKLLEA HEEQNVDSYT EAVKEYDSIS RLDQWLTTML LRIKKTIQGD EEDLR
//
ID   RM12_MOUSE              Reviewed;         201 AA.
AC   Q9DB15; B1ATZ3; Q3TKJ3; Q99JS8;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2001, sequence version 2.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=39S ribosomal protein L12, mitochondrial;
DE            Short=L12mt;
DE            Short=MRP-L12;
DE   Flags: Precursor;
GN   Name=Mrpl12; Synonyms=Rpml12;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Liver, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 154-165.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the ribosomal protein L12P family.
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DR   EMBL; AK005328; BAB23955.1; -; mRNA.
DR   EMBL; AK028168; BAC25787.1; -; mRNA.
DR   EMBL; AK134816; BAE22297.1; -; mRNA.
DR   EMBL; AK166969; BAE39152.1; -; mRNA.
DR   EMBL; AK168337; BAE40275.1; -; mRNA.
DR   EMBL; AL669855; CAM27051.1; -; Genomic_DNA.
DR   EMBL; BC005712; AAH05712.1; -; mRNA.
DR   EMBL; BC019565; AAH19565.1; -; mRNA.
DR   IPI; IPI00118963; -.
DR   RefSeq; NP_081480.2; NM_027204.2.
DR   UniGene; Mm.133851; -.
DR   ProteinModelPortal; Q9DB15; -.
DR   SMR; Q9DB15; 65-201.
DR   STRING; Q9DB15; -.
DR   PRIDE; Q9DB15; -.
DR   Ensembl; ENSMUST00000043627; ENSMUSP00000044417; ENSMUSG00000039640.
DR   GeneID; 56282; -.
DR   KEGG; mmu:56282; -.
DR   NMPDR; fig|10090.3.peg.25796; -.
DR   UCSC; uc007mta.1; mouse.
DR   CTD; 56282; -.
DR   MGI; MGI:1926273; Mrpl12.
DR   eggNOG; roNOG16457; -.
DR   GeneTree; ENSGT00390000000190; -.
DR   HOGENOM; HBG746222; -.
DR   HOVERGEN; HBG001832; -.
DR   InParanoid; Q9DB15; -.
DR   OMA; FDAKSKP; -.
DR   OrthoDB; EOG4R5044; -.
DR   PhylomeDB; Q9DB15; -.
DR   NextBio; 312184; -.
DR   ArrayExpress; Q9DB15; -.
DR   Bgee; Q9DB15; -.
DR   CleanEx; MM_MRPL12; -.
DR   Genevestigator; Q9DB15; -.
DR   GermOnline; ENSMUSG00000039640; Mus musculus.
DR   GO; GO:0005762; C:mitochondrial large ribosomal subunit; ISS:UniProtKB.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR015607; Ribosomal_L12_mit.
DR   InterPro; IPR014719; Ribosomal_L7/12_C/ClpS-like.
DR   InterPro; IPR013823; Ribosomal_L7/L12_C.
DR   InterPro; IPR008932; Ribosomal_L7/L12_oligo.
DR   Gene3D; G3DSA:3.30.1390.10; Ribosomal_L7/12_C/ClpS-like; 1.
DR   PANTHER; PTHR11809:SF2; Ribosomal_L12_mit; 1.
DR   Pfam; PF00542; Ribosomal_L12; 1.
DR   ProDom; PD001326; Ribosomal_L7/L12_C; 1.
DR   SUPFAM; SSF48300; Ribosomal_L12/7; 1.
DR   SUPFAM; SSF54736; Ribosomal_L7/12_C/ClpS-like; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Mitochondrion; Ribonucleoprotein;
KW   Ribosomal protein; Transit peptide.
FT   TRANSIT       1     46       Mitochondrion (Potential).
FT   CHAIN        47    201       39S ribosomal protein L12, mitochondrial.
FT                                /FTId=PRO_0000030459.
FT   CONFLICT      8     18       RCLWGPRLGLR -> AACGGHGLDSW (in Ref. 1;
FT                                BAB23955).
SQ   SEQUENCE   201 AA;  21708 MW;  893BEFB4F154076D CRC64;
     MLPVAASRCL WGPRLGLRGA ALRLARQQMP SVCAARQLRS SSHRRSEALA GAPLDNAPKE
     YPPKIQQLVQ DIASLTLLEI SDLNELLKKT LKIQDVGLMP MGGMVPGPVS AAAPASEAAE
     EEDVPKQKER THFTVRLTEA KPVDKVKLIK EIKNYVQGIN LVQAKKLVES LPQEIKANVA
     KAEAEKIKAA LEAVGGTVVL E
//
ID   ATPO_MOUSE              Reviewed;         213 AA.
AC   Q9DB20;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=ATP synthase subunit O, mitochondrial;
DE   AltName: Full=Oligomycin sensitivity conferral protein;
DE            Short=OSCP;
DE   Flags: Precursor;
GN   Name=Atp5o; Synonyms=D12Wsu28e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 27-51; 65-84; 99-158; 163-172 AND 177-188, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60; LYS-70; LYS-158;
RP   LYS-162; LYS-172; LYS-176 AND LYS-192, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
CC       synthase or Complex V) produces ATP from ADP in the presence of a
CC       proton gradient across the membrane which is generated by electron
CC       transport complexes of the respiratory chain. F-type ATPases
CC       consist of two structural domains, F(1) - containing the
CC       extramembraneous catalytic core and F(0) - containing the membrane
CC       proton channel, linked together by a central stalk and a
CC       peripheral stalk. During catalysis, ATP synthesis in the catalytic
CC       domain of F(1) is coupled via a rotary mechanism of the central
CC       stalk subunits to proton translocation. Part of the complex F(0)
CC       domain and the peripheric stalk, which acts as a stator to hold
CC       the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC       relative to the rotary elements.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel. CF(1) has five
CC       subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
CC       has three main subunits: a, b and c.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). Mitochondrion
CC       inner membrane (By similarity).
CC   -!- PTM: Acetylation of Lys-70 and Lys-158 is observed in liver
CC       mitochondria from fasted mice but not from fed mice.
CC   -!- SIMILARITY: Belongs to the ATPase delta chain family.
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CC   -----------------------------------------------------------------------
DR   EMBL; AK005309; BAB23945.1; -; mRNA.
DR   EMBL; BC012241; AAH12241.1; -; mRNA.
DR   IPI; IPI00118986; -.
DR   RefSeq; NP_613063.1; NM_138597.2.
DR   RefSeq; XP_001478145.1; XM_001478095.2.
DR   UniGene; Mm.41; -.
DR   ProteinModelPortal; Q9DB20; -.
DR   SMR; Q9DB20; 24-212.
DR   STRING; Q9DB20; -.
DR   PhosphoSite; Q9DB20; -.
DR   PRIDE; Q9DB20; -.
DR   Ensembl; ENSMUST00000023677; ENSMUSP00000023677; ENSMUSG00000022956.
DR   GeneID; 100047429; -.
DR   GeneID; 28080; -.
DR   KEGG; mmu:100047429; -.
DR   KEGG; mmu:28080; -.
DR   NMPDR; fig|10090.3.peg.1898; -.
DR   UCSC; uc007zys.1; mouse.
DR   CTD; 28080; -.
DR   MGI; MGI:106341; Atp5o.
DR   GeneTree; ENSGT00390000015060; -.
DR   HOGENOM; HBG668108; -.
DR   HOVERGEN; HBG004309; -.
DR   InParanoid; Q9DB20; -.
DR   OMA; SIGDKYV; -.
DR   PhylomeDB; Q9DB20; -.
DR   NextBio; 460864; -.
DR   Bgee; Q9DB20; -.
DR   Genevestigator; Q9DB20; -.
DR   GermOnline; ENSMUSG00000022956; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:InterPro.
DR   GO; GO:0046933; F:hydrogen ion transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR000711; ATPase_F1-cplx_OSCP/dsu.
DR   InterPro; IPR020781; ATPase_F1-cplx_OSCP/dsu_CS.
DR   Gene3D; G3DSA:1.10.520.20; ATPase_F1_OSCP/d; 1.
DR   PANTHER; PTHR11910; ATPase_F1_OSCP/d; 1.
DR   Pfam; PF00213; OSCP; 1.
DR   PRINTS; PR00125; ATPASEDELTA.
DR   SUPFAM; SSF47928; ATPsynt_OSCP; 1.
DR   TIGRFAMs; TIGR01145; ATP_synt_delta; 1.
DR   PROSITE; PS00389; ATPASE_DELTA; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP synthesis; Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Transit peptide; Transport.
FT   TRANSIT       1     23       Mitochondrion (By similarity).
FT   CHAIN        24    213       ATP synthase subunit O, mitochondrial.
FT                                /FTId=PRO_0000002647.
FT   MOD_RES      54     54       N6-acetyllysine (By similarity).
FT   MOD_RES      60     60       N6-acetyllysine.
FT   MOD_RES      70     70       N6-acetyllysine.
FT   MOD_RES     158    158       N6-acetyllysine.
FT   MOD_RES     162    162       N6-acetyllysine.
FT   MOD_RES     172    172       N6-acetyllysine.
FT   MOD_RES     176    176       N6-acetyllysine.
FT   MOD_RES     192    192       N6-acetyllysine.
SQ   SEQUENCE   213 AA;  23364 MW;  1B0DAD4CCFCCB086 CRC64;
     MAAPAASGLS RQVRSFSTSV VRPFAKLVRP PVQVYGIEGR YATALYSAAS KEKKLDQVEK
     ELLRVGQLLK DPKVSLAVLN PYIKRTVKVK SLNDITKREK FSPLTANLMN LLAENGRLGN
     TQGIISAFST IMSVHRGEVP CTVTTASPLD DAVLSELKTV LKSFLSPNQI LKLEIKTDPS
     IMGGMIVRIG EKYVDMSAKS KIQKLSKAMR EML
//
ID   Q9DB24_MOUSE            Unreviewed;       200 AA.
AC   Q9DB24;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   SubName: Full=Putative uncharacterized protein;
DE   SubName: Full=Transcription elongation factor A (SII)-like 6;
GN   Name=Tceal6; ORFNames=RP23-460B8.1-001;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RA   Adachi J., Aizawa K., Akahira S., Akimura T., Arai A., Aono H.,
RA   Arakawa T., Bono H., Carninci P., Fukuda S., Fukunishi Y., Furuno M.,
RA   Hanagaki T., Hara A., Hayatsu N., Hiramoto K., Hiraoka T., Hori F.,
RA   Imotani K., Ishii Y., Itoh M., Izawa M., Kasukawa T., Kato H.,
RA   Kawai J., Kojima Y., Konno H., Kouda M., Koya S., Kurihara C.,
RA   Matsuyama T., Miyazaki A., Nishi K., Nomura K., Numazaki R., Ohno M.,
RA   Okazaki Y., Okido T., Owa C., Saito H., Saito R., Sakai C., Sakai K.,
RA   Sano H., Sasaki D., Shibata K., Shibata Y., Shinagawa A., Shiraki T.,
RA   Sogabe Y., Suzuki H., Tagami M., Tagawa A., Takahashi F., Tanaka T.,
RA   Tejima Y., Toya T., Yamamura T., Yasunishi A., Yoshida K., Yoshino M.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RA   Grafham D.;
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; BC087890; AAH87890.1; -; mRNA.
DR   EMBL; AK005297; BAB23939.1; -; mRNA.
DR   EMBL; AL731676; CAM25049.1; -; Genomic_DNA.
DR   IPI; IPI00480568; -.
DR   RefSeq; NP_079631.2; NM_025355.4.
DR   UniGene; Mm.336239; -.
DR   ProteinModelPortal; Q9DB24; -.
DR   STRING; Q9DB24; -.
DR   PhosphoSite; Q9DB24; -.
DR   PRIDE; Q9DB24; -.
DR   Ensembl; ENSMUST00000033783; ENSMUSP00000033783; ENSMUSG00000031409.
DR   GeneID; 66104; -.
DR   KEGG; mmu:66104; -.
DR   UCSC; uc009uhc.1; mouse.
DR   CTD; 66104; -.
DR   MGI; MGI:1923939; Tceal6.
DR   eggNOG; roNOG17318; -.
DR   GeneTree; ENSGT00510000046867; -.
DR   HOGENOM; HBG127442; -.
DR   HOVERGEN; HBG055896; -.
DR   InParanoid; Q9DB24; -.
DR   OMA; YNENEGK; -.
DR   OrthoDB; EOG4VQ9QH; -.
DR   PhylomeDB; Q9DB24; -.
DR   NextBio; 320634; -.
DR   Bgee; Q9DB24; -.
DR   Genevestigator; Q9DB24; -.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR021156; TF_A-like/BEX-like.
DR   InterPro; IPR010370; TFA.
DR   PANTHER; PTHR14754; TFA; 1.
DR   Pfam; PF04538; BEX; 1.
PE   2: Evidence at transcript level;
KW   Elongation factor; Protein biosynthesis.
SQ   SEQUENCE   200 AA;  22572 MW;  7E7858ED441F4C75 CRC64;
     MEEVRGENEG KLEKEGKPED EVEPEDEEKS DEEEKPDKKA KPAPRQGKPE EEAKPDEQGQ
     DEGKPEKQGK SDGEGKRQGE SKPDSQAKSA SEARAAEKRP AEDYVPRKAK RKTDRGTDDS
     PKNSQEDLQD RHVSSEEMMR ECTDMTRARE ELRKRQKMGG FHWVPRDAQD ALVPRGQRGV
     RGVRGGGGRS QRGLHDIPYL
//
ID   IAH1_MOUSE              Reviewed;         249 AA.
AC   Q9DB29;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Isoamyl acetate-hydrolyzing esterase 1 homolog;
DE            EC=3.1.-.-;
GN   Name=Iah1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Probable lipase (By similarity).
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family. IAH1
CC       subfamily.
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DR   EMBL; AK005287; BAB23934.1; -; mRNA.
DR   EMBL; BC060949; AAH60949.1; -; mRNA.
DR   EMBL; BC087901; AAH87901.1; -; mRNA.
DR   IPI; IPI00119004; -.
DR   RefSeq; NP_080623.2; NM_026347.3.
DR   UniGene; Mm.335830; -.
DR   ProteinModelPortal; Q9DB29; -.
DR   SMR; Q9DB29; 13-236.
DR   STRING; Q9DB29; -.
DR   REPRODUCTION-2DPAGE; IPI00119004; -.
DR   PRIDE; Q9DB29; -.
DR   Ensembl; ENSMUST00000076813; ENSMUSP00000076090; ENSMUSG00000062054.
DR   GeneID; 67732; -.
DR   KEGG; mmu:67732; -.
DR   UCSC; uc007ndt.1; mouse.
DR   CTD; 67732; -.
DR   MGI; MGI:1914982; Iah1.
DR   eggNOG; roNOG05022; -.
DR   GeneTree; ENSGT00390000008069; -.
DR   HOGENOM; HBG618579; -.
DR   HOVERGEN; HBG105140; -.
DR   InParanoid; Q9DB29; -.
DR   OMA; LWTLMQK; -.
DR   OrthoDB; EOG4868D7; -.
DR   PhylomeDB; Q9DB29; -.
DR   NextBio; 325403; -.
DR   ArrayExpress; Q9DB29; -.
DR   Bgee; Q9DB29; -.
DR   Genevestigator; Q9DB29; -.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR013830; Esterase_SGNH_hydro-type.
DR   InterPro; IPR013831; Esterase_SGNH_hydro-type_subgr.
DR   InterPro; IPR001087; Lipase_GDSL.
DR   Gene3D; G3DSA:3.40.50.1110; Esterase_SGNH_hydro-type_subgr; 1.
DR   Pfam; PF00657; Lipase_GDSL; 1.
DR   SUPFAM; SSF52266; Esterase_SGNH_hydro-type; 1.
DR   PROSITE; PS01098; LIPASE_GDSL_SER; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Hydrolase; Lipid degradation.
FT   CHAIN         1    249       Isoamyl acetate-hydrolyzing esterase 1
FT                                homolog.
FT                                /FTId=PRO_0000315724.
FT   ACT_SITE     24     24       Nucleophile (By similarity).
FT   ACT_SITE    197    197       By similarity.
FT   ACT_SITE    200    200       By similarity.
FT   BINDING      56     56       Substrate; via amide nitrogen (By
FT                                similarity).
FT   BINDING      89     89       Substrate (By similarity).
SQ   SEQUENCE   249 AA;  27974 MW;  45E9C8FE068F8423 CRC64;
     MSLCERAASG SALLWPRVLL FGDSITQFSF QQGGWGSLLA DRLVRKCDVL NRGFSGYNTR
     WAKIILPRLI RKGPGMENPV AVTIFFGAND SSLKDENPKQ HVPLDEYSAN LRDMVQYLRS
     VDVPRERVIL ITPPPLCEAA WEKECVLKGC KLNRLNSVVG EYANACLQVA RDCGTDVLDL
     WTLMQKDSQD FSSYLSDGLH LSPMGNEFLF LNLCPLLDKK VSSLPWLLPY WKDVEEAKPE
     LSLLGDGDY
//
ID   GHC2_MOUSE              Reviewed;         320 AA.
AC   Q9DB41; B2RPU3; Q14AI5;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 4.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Mitochondrial glutamate carrier 2;
DE            Short=GC-2;
DE   AltName: Full=Glutamate/H(+) symporter 2;
DE   AltName: Full=Solute carrier family 25 member 18;
GN   Name=Slc25a18; Synonyms=Gc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Involved in the transport of glutamate across the inner
CC       mitochondrial membrane. Glutamate is cotransported with H(+) (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9DB41-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9DB41-2; Sequence=VSP_022262;
CC         Note=Incomplete sequence;
CC   -!- SIMILARITY: Belongs to the mitochondrial carrier family.
CC   -!- SIMILARITY: Contains 3 Solcar repeats.
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DR   EMBL; BC116828; AAI16829.2; -; mRNA.
DR   EMBL; BC137603; AAI37604.1; -; mRNA.
DR   EMBL; AK005250; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00817038; -.
DR   IPI; IPI00875016; -.
DR   RefSeq; NP_001074517.1; NM_001081048.2.
DR   UniGene; Mm.425340; -.
DR   ProteinModelPortal; Q9DB41; -.
DR   SMR; Q9DB41; 7-309.
DR   PRIDE; Q9DB41; -.
DR   Ensembl; ENSMUST00000000102; ENSMUSP00000000102; ENSMUSG00000004902.
DR   Ensembl; ENSMUST00000112682; ENSMUSP00000108302; ENSMUSG00000004902.
DR   GeneID; 71803; -.
DR   KEGG; mmu:71803; -.
DR   UCSC; uc009dnq.1; mouse.
DR   CTD; 71803; -.
DR   MGI; MGI:1919053; Slc25a18.
DR   eggNOG; roNOG14118; -.
DR   GeneTree; ENSGT00530000062944; -.
DR   HOGENOM; HBG735918; -.
DR   HOVERGEN; HBG039469; -.
DR   InParanoid; Q9DB41; -.
DR   OMA; ASTHRRP; -.
DR   OrthoDB; EOG49CQ83; -.
DR   NextBio; 334560; -.
DR   ArrayExpress; Q9DB41; -.
DR   Bgee; Q9DB41; -.
DR   Genevestigator; Q9DB41; -.
DR   GermOnline; ENSMUSG00000004902; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   InterPro; IPR002067; Mit_carrier.
DR   InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR   Pfam; PF00153; Mito_carr; 3.
DR   PRINTS; PR00926; MITOCARRIER.
DR   PROSITE; PS50920; SOLCAR; 3.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Repeat; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    320       Mitochondrial glutamate carrier 2.
FT                                /FTId=PRO_0000090622.
FT   TRANSMEM     17     37       Helical; Name=1; (Potential).
FT   TRANSMEM     66     86       Helical; Name=2; (Potential).
FT   TRANSMEM    110    128       Helical; Name=3; (Potential).
FT   TRANSMEM    190    210       Helical; Name=4; (Potential).
FT   TRANSMEM    230    250       Helical; Name=5; (Potential).
FT   TRANSMEM    293    313       Helical; Name=6; (Potential).
FT   REPEAT       11     97       Solcar 1.
FT   REPEAT      105    215       Solcar 2.
FT   REPEAT      224    313       Solcar 3.
FT   VAR_SEQ       1     17       MIACRMSSQDLSISAKL -> TPSSCRTKI (in
FT                                isoform 2).
FT                                /FTId=VSP_022262.
SQ   SEQUENCE   320 AA;  34166 MW;  1FC0AD760C44E6FE CRC64;
     MIACRMSSQD LSISAKLING GIAGLVGVTC VFPIDLAKTR LQNQQGKDVY RGMTDCLMKT
     ARAEGFLGMY RGAAVNLTLV TPEKAIKLAA NDFLRQLLMQ DGTQRNLKME MLAGCGAGIC
     QVVITCPMEM LKIQLQDAGR LAVCHQASAS ATPTSRPYST GSTSTHRRPS ATLIARELLR
     TQGLSGLYRG LGATLLRDIP FSIIYFPLFA NLNQLGVSEL TGKASFTHSF VAGCTAGSVA
     AVAVTPLDVL KTRIQTLKKG LGEDTYSGVT DCARKLWTQE GPAAFMKGAG CRALVIAPLF
     GIAQGVYFIG IGERILKCFE
//
ID   F122A_MOUSE             Reviewed;         284 AA.
AC   Q9DB52; Q3TA50; Q9D078;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Protein FAM122A;
GN   Name=Fam122a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Cecum, Cerebellum, Embryo, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-267, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-140 AND SER-144,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140 AND SER-144, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; SER-73; SER-140 AND
RP   SER-144, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- SIMILARITY: Belongs to the FAM122 family.
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DR   EMBL; AK005219; BAB23889.1; -; mRNA.
DR   EMBL; AK011741; BAB27811.1; -; mRNA.
DR   EMBL; AK033646; BAC28405.1; -; mRNA.
DR   EMBL; AK077654; BAC36930.1; -; mRNA.
DR   EMBL; AK172089; BAE42820.1; -; mRNA.
DR   EMBL; BC028637; AAH28637.1; -; mRNA.
DR   EMBL; BC083062; AAH83062.1; -; mRNA.
DR   IPI; IPI00154109; -.
DR   RefSeq; NP_080796.1; NM_026520.3.
DR   UniGene; Mm.440181; -.
DR   ProteinModelPortal; Q9DB52; -.
DR   PhosphoSite; Q9DB52; -.
DR   PRIDE; Q9DB52; -.
DR   Ensembl; ENSMUST00000099556; ENSMUSP00000097152; ENSMUSG00000074922.
DR   GeneID; 68034; -.
DR   KEGG; mmu:68034; -.
DR   UCSC; uc008haq.1; mouse.
DR   CTD; 68034; -.
DR   MGI; MGI:1915284; Fam122a.
DR   eggNOG; roNOG17667; -.
DR   GeneTree; ENSGT00390000015476; -.
DR   HOGENOM; HBG714535; -.
DR   HOVERGEN; HBG073694; -.
DR   InParanoid; Q9DB52; -.
DR   OMA; CEMETDY; -.
DR   OrthoDB; EOG4BK552; -.
DR   NextBio; 326258; -.
DR   ArrayExpress; Q9DB52; -.
DR   Bgee; Q9DB52; -.
DR   Genevestigator; Q9DB52; -.
DR   GermOnline; ENSMUSG00000074922; Mus musculus.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    284       Protein FAM122A.
FT                                /FTId=PRO_0000089690.
FT   COMPBIAS     21     28       Poly-Gly.
FT   MOD_RES      32     32       Phosphoserine (By similarity).
FT   MOD_RES      34     34       Phosphoserine (By similarity).
FT   MOD_RES      42     42       Phosphoserine.
FT   MOD_RES      45     45       Phosphoserine (By similarity).
FT   MOD_RES      59     59       Phosphoserine.
FT   MOD_RES      73     73       Phosphoserine.
FT   MOD_RES     140    140       Phosphoserine.
FT   MOD_RES     144    144       Phosphoserine.
FT   MOD_RES     146    146       Phosphothreonine (By similarity).
FT   MOD_RES     264    264       Phosphoserine (By similarity).
FT   MOD_RES     267    267       Phosphoserine.
FT   MOD_RES     273    273       Phosphoserine (By similarity).
FT   CONFLICT     18     20       PAE -> RRR (in Ref. 1; BAB27811).
FT   CONFLICT     37     37       L -> P (in Ref. 1; BAB27811).
SQ   SEQUENCE   284 AA;  30270 MW;  F099612EB932120B CRC64;
     MAQEKMELDL ELPAGASPAE GGGPGGGGLR RSNSAPLIHG LSDSSPVFQA EAPSARRNST
     TFPSRHGLLL PASPVRMHSS RLHQIKQEEG MDLINRETVH EREVQTAMQI SHSWEESFSL
     SDNDVEKSAS PKRIDFIPVS PAPSPTRGIG KQCFSPSLQS FVSSNGLPPS PIPSPTTRFT
     TRRSQSPINC IRPSVLGPLK RKCEMETDYQ PKRFFQGITN MLSSDVAQLS DPGVCVSSDT
     LDGNSSSAGS SCNSPAKVST TTDSPVSPAQ AASPFIPVDE LSSK
//
ID   FUND1_MOUSE             Reviewed;         155 AA.
AC   Q9DB70;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 58.
DE   RecName: Full=FUN14 domain-containing protein 1;
GN   Name=Fundc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the FUN14 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK005163; BAB23854.1; -; mRNA.
DR   EMBL; AK168868; BAE40687.1; -; mRNA.
DR   EMBL; BC012515; AAH12515.1; -; mRNA.
DR   EMBL; BC030487; AAH30487.1; -; mRNA.
DR   IPI; IPI00119124; -.
DR   RefSeq; NP_082334.1; NM_028058.3.
DR   UniGene; Mm.41558; -.
DR   PhosphoSite; Q9DB70; -.
DR   PRIDE; Q9DB70; -.
DR   Ensembl; ENSMUST00000026016; ENSMUSP00000026016; ENSMUSG00000025040.
DR   GeneID; 72018; -.
DR   KEGG; mmu:72018; -.
DR   UCSC; uc009ssf.1; mouse.
DR   CTD; 72018; -.
DR   MGI; MGI:1919268; Fundc1.
DR   GeneTree; ENSGT00390000003926; -.
DR   HOGENOM; HBG279857; -.
DR   HOVERGEN; HBG054805; -.
DR   InParanoid; Q9DB70; -.
DR   OMA; HSGYVQV; -.
DR   OrthoDB; EOG4S4PHM; -.
DR   PhylomeDB; Q9DB70; -.
DR   NextBio; 335232; -.
DR   ArrayExpress; Q9DB70; -.
DR   Bgee; Q9DB70; -.
DR   CleanEx; MM_FUNDC1; -.
DR   Genevestigator; Q9DB70; -.
DR   InterPro; IPR007014; FUN14.
DR   Pfam; PF04930; FUN14; 1.
PE   2: Evidence at transcript level;
KW   Phosphoprotein.
FT   CHAIN         1    155       FUN14 domain-containing protein 1.
FT                                /FTId=PRO_0000271346.
FT   MOD_RES      13     13       Phosphoserine (By similarity).
SQ   SEQUENCE   155 AA;  17159 MW;  8AAA46566714ED80 CRC64;
     MASRNPPPQD YESDDESYEV LDLTEYARRH HWWNRVFGHS SGPMVEKYSV ATQIVMGGVT
     GWCAGFLFQK VGKLAATAVG GGFLLLQVAS HSGYVQIDWK RVEKDVNKAK RQIKKRANKA
     APEINNIIEE ATDFIKQNIV ISSGFVGGFL LGLAS
//
ID   LITFL_MOUSE             Reviewed;         208 AA.
AC   Q9DB75; Q3UD73; Q9CYP1;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=LITAF-like protein;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow, Cerebellum, Lung, Spinal ganglion, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9DB75-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9DB75-2; Sequence=VSP_023632;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the LITAF family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK005157; BAB23848.1; -; mRNA.
DR   EMBL; AK017480; BAB30764.1; -; mRNA.
DR   EMBL; AK031705; BAC27523.1; -; mRNA.
DR   EMBL; AK051560; BAC34673.1; -; mRNA.
DR   EMBL; AK149939; BAE29181.1; -; mRNA.
DR   EMBL; AK150219; BAE29388.1; -; mRNA.
DR   EMBL; AK166141; BAE38594.1; -; mRNA.
DR   EMBL; BC004063; AAH04063.1; -; mRNA.
DR   IPI; IPI00111778; -.
DR   IPI; IPI00830386; -.
DR   RefSeq; NP_079946.2; NM_025670.4.
DR   UniGene; Mm.157648; -.
DR   UniGene; Mm.443028; -.
DR   IntAct; Q9DB75; 1.
DR   Ensembl; ENSMUST00000004173; ENSMUSP00000004173; ENSMUSG00000004071.
DR   Ensembl; ENSMUST00000118703; ENSMUSP00000113889; ENSMUSG00000004071.
DR   GeneID; 66626; -.
DR   KEGG; mmu:66626; -.
DR   UCSC; uc007yaj.1; mouse.
DR   MGI; MGI:1913876; 5730403B10Rik.
DR   eggNOG; roNOG16211; -.
DR   GeneTree; ENSGT00540000071542; -.
DR   HOGENOM; HBG715290; -.
DR   HOVERGEN; HBG006272; -.
DR   InParanoid; Q9DB75; -.
DR   OMA; DIGPPPY; -.
DR   PhylomeDB; Q9DB75; -.
DR   NextBio; 322208; -.
DR   ArrayExpress; Q9DB75; -.
DR   Bgee; Q9DB75; -.
DR   CleanEx; MM_5730403B10RIK; -.
DR   Genevestigator; Q9DB75; -.
DR   InterPro; IPR006629; LITAF.
DR   Pfam; PF10601; zf-LITAF-like; 1.
DR   SMART; SM00714; LITAF; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing.
FT   CHAIN         1    208       LITAF-like protein.
FT                                /FTId=PRO_0000280337.
FT   COMPBIAS      5    108       Pro-rich.
FT   VAR_SEQ      81     97       Missing (in isoform 2).
FT                                /FTId=VSP_023632.
FT   CONFLICT     70     70       H -> R (in Ref. 1; BAE29388).
FT   CONFLICT    180    180       I -> V (in Ref. 1; BAB30764).
SQ   SEQUENCE   208 AA;  21835 MW;  DC1A9A7C17EC0B90 CRC64;
     MSNEPPPPYP GGPTAPLLEE KSGAPLTPGR TSPAVMQPPP GMPLPSADIA PPPYEPPGQP
     VPQPGFVPPH MNADGTYMPA GFYPPPGPHP PMGYYPPGPY PPGPYPGPGG HTATVLVPSG
     AATTVTVLQG EIFEGAPVQT VCPHCQQAIT TKISYEIGLM NFVLGFFCCF MGCDLGCCLI
     PCLINDFKDV THTCPSCKAY ICTYKRLC
//
ID   QCR2_MOUSE              Reviewed;         453 AA.
AC   Q9DB77; Q8BK11; Q9CVK7;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Cytochrome b-c1 complex subunit 2, mitochondrial;
DE   AltName: Full=Complex III subunit 2;
DE   AltName: Full=Core protein II;
DE   AltName: Full=Ubiquinol-cytochrome-c reductase complex core protein 2;
DE   Flags: Precursor;
GN   Name=Uqcrc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Pancreas, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 24-60; 71-85; 117-147; 163-196; 200-241; 301-315;
RP   360-375 AND 436-453, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-159 AND LYS-250, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- FUNCTION: This is a component of the ubiquinol-cytochrome c
CC       reductase complex (complex III or cytochrome b-c1 complex), which
CC       is part of the mitochondrial respiratory chain. The core protein 2
CC       is required for the assembly of the complex (By similarity).
CC   -!- SUBUNIT: The bc1 complex contains 11 subunits: 3 respiratory
CC       subunits (cytochrome b, cytochrome c1 and Rieske/UQCRFS1), 2 core
CC       proteins (UQCRC1/QCR1 and UQCRC2/QCR2) and 6 low-molecular weight
CC       proteins (UQCRH/QCR6, UQCRB/QCR7, UQCRQ/QCR8, UQCR10/QCR9,
CC       UQCR11/QCR10 and a cleavage product of Rieske/UQCRFS1) (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein; Matrix side (By similarity).
CC   -!- PTM: Acetylation of Lys-159 and Lys-250 is observed in liver
CC       mitochondria from fasted mice but not from fed mice.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family. UQCRC2/QCR2
CC       subfamily.
CC   -!- CAUTION: Does not seem to have a protease activity as it lack the
CC       zinc-binding site.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK005151; BAB23845.1; -; mRNA.
DR   EMBL; AK007669; BAB25176.1; -; mRNA.
DR   EMBL; AK077583; BAC36876.1; -; mRNA.
DR   EMBL; AK088103; BAC40146.1; -; mRNA.
DR   EMBL; BC003423; AAH03423.1; -; mRNA.
DR   IPI; IPI00119138; -.
DR   PIR; PC7073; PC7073.
DR   RefSeq; NP_080175.1; NM_025899.2.
DR   UniGene; Mm.334206; -.
DR   ProteinModelPortal; Q9DB77; -.
DR   SMR; Q9DB77; 35-453.
DR   STRING; Q9DB77; -.
DR   PhosphoSite; Q9DB77; -.
DR   PRIDE; Q9DB77; -.
DR   Ensembl; ENSMUST00000033176; ENSMUSP00000033176; ENSMUSG00000030884.
DR   GeneID; 67003; -.
DR   KEGG; mmu:67003; -.
DR   NMPDR; fig|10090.3.peg.17543; -.
DR   UCSC; uc009jms.1; mouse.
DR   CTD; 67003; -.
DR   MGI; MGI:1914253; Uqcrc2.
DR   eggNOG; roNOG06675; -.
DR   GeneTree; ENSGT00550000074666; -.
DR   HOGENOM; HBG446240; -.
DR   HOVERGEN; HBG055236; -.
DR   InParanoid; Q9DB77; -.
DR   OMA; NFTSARM; -.
DR   OrthoDB; EOG4QRH45; -.
DR   PhylomeDB; Q9DB77; -.
DR   NextBio; 323278; -.
DR   ArrayExpress; Q9DB77; -.
DR   Bgee; Q9DB77; -.
DR   CleanEx; MM_UQCRC2; -.
DR   Genevestigator; Q9DB77; -.
DR   GermOnline; ENSMUSG00000030884; Mus musculus.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR011249; Metalloenz_metal-bd.
DR   InterPro; IPR011237; Pept_M16_core.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   Gene3D; G3DSA:3.30.830.10; Pept_M16_core; 2.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; Metalloenz_metal-bd; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Electron transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Respiratory chain;
KW   Transit peptide; Transport.
FT   TRANSIT       1     14       Mitochondrion (By similarity).
FT   CHAIN        15    453       Cytochrome b-c1 complex subunit 2,
FT                                mitochondrial.
FT                                /FTId=PRO_0000026792.
FT   MOD_RES     159    159       N6-acetyllysine.
FT   MOD_RES     250    250       N6-acetyllysine.
FT   CONFLICT     36     36       Q -> L (in Ref. 1; BAB25176).
FT   CONFLICT    319    319       Q -> R (in Ref. 1; BAC36876).
SQ   SEQUENCE   453 AA;  48235 MW;  24A2BDDDA657867E CRC64;
     MKLLSRAGSF SRFYSLKVAP KVKTSAAPGG VPLQPQDLEF TKLPNGLVIA SLENYAPLSR
     IGLFVKAGSR YEDSNNLGTS HLLRLASSLT TKGASSFKIT RGIEAVGGKL SVTATRENMA
     YTVEGIRSDI EILMEFLLNV TTAPEFRRWE VAALRSQLKI DKAVAFQNSQ TRIIENLHDV
     AYKNALANPL YCPDYRMGKI TSEELHYFVQ NHFTSARMAL VGLGVSHSVL KQVAEQFLNM
     RGGLGLAGAK AKYRGGEIRE QNGDNLVHAA IVAESAAIGN AEANAFSVLQ HLLGAGPHIK
     RGNNTTSLLS QSVAKGSHQP FDVSAFNASY SDSGLFGIYT ISQAAAAGEV INAAYNQVKA
     VAQGNLSSAD VQAAKNKLKA GYLMSVETSE GFLSEIGSQA LAAGSYMPPS TVLQQIDSVA
     DADVVKAAKK FVSGKKSMAA SGNLGHTPFL DEL
//
ID   SELO_MOUSE              Reviewed;         667 AA.
AC   Q9DBC0; Q80ZK3;
DT   04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Selenoprotein O;
DE            Short=SelO;
GN   Name=Selo;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 326-667.
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SIMILARITY: Belongs to the UPF0061 (SELO) family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH48849.1; Type=Erroneous termination; Positions=665; Note=Translated as Sec;
CC       Sequence=BAB23774.1; Type=Erroneous termination; Positions=665; Note=Translated as Sec;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK005048; BAB23774.1; ALT_SEQ; mRNA.
DR   EMBL; BC048849; AAH48849.1; ALT_SEQ; mRNA.
DR   IPI; IPI00321577; -.
DR   RefSeq; NP_082181.2; NM_027905.2.
DR   UniGene; Mm.380934; -.
DR   UniGene; Mm.44763; -.
DR   STRING; Q9DBC0; -.
DR   PRIDE; Q9DBC0; -.
DR   Ensembl; ENSMUST00000082439; ENSMUSP00000081020; ENSMUSG00000035757.
DR   GeneID; 223776; -.
DR   KEGG; mmu:223776; -.
DR   MGI; MGI:1919007; 1300018J18Rik.
DR   GeneTree; ENSGT00390000005508; -.
DR   HOGENOM; HBG683993; -.
DR   HOVERGEN; HBG044520; -.
DR   InParanoid; Q9DBC0; -.
DR   OrthoDB; EOG4MCX02; -.
DR   NextBio; 376898; -.
DR   ArrayExpress; Q9DBC0; -.
DR   Bgee; Q9DBC0; -.
DR   CleanEx; MM_1300018J18RIK; -.
DR   Genevestigator; Q9DBC0; -.
DR   GermOnline; ENSMUSG00000035757; Mus musculus.
DR   InterPro; IPR003846; UPF0061.
DR   Pfam; PF02696; UPF0061; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Selenocysteine.
FT   CHAIN         1    667       Selenoprotein O.
FT                                /FTId=PRO_0000121400.
FT   NON_STD     665    665       Selenocysteine (By similarity).
FT   MOD_RES     544    544       Phosphoserine.
FT   CONFLICT    619    619       L -> R (in Ref. 2; AAH48849).
SQ   SEQUENCE   667 AA;  74178 MW;  4D93C1E27B8D9026 CRC64;
     MASVRAAVGA SLAVARTRPR CVGLALPSSA PRSAWAAAME PTPRWLAGLR FDNRALRELP
     VETPPPGPED SLATPRPVPG ACFSRARPAP LRRPRLVALS EPALALLGLE ASEEAEVEAE
     AALFFSGNAL LPGTEPAAHC YCGHQFGQFA GQLGDGAAMY LGEVCTAAGE RWELQLKGAG
     PTPFSRQADG RKVLRSSIRE FLCSEAMFHL GIPTTRAGAC VTSESTVMRD VFYDGNPKYE
     KCTVVLRIAP TFIRFGSFEI FKPPDEHTGR AGPSVGRDDI RVQLLDYVIS SFYPEIQAAH
     TCDTDNIQRN AAFFREVTQR TARMVAEWQC VGFCHGVLNT DNMSIVGLTI DYGPFGFLDR
     YDPDHICNAS DNAGRYTYSK QPQVCKWNLQ KLAEALEPEL PLALAEAILK EEFDTEFQRH
     YLQKMRKKLG LIRVEKEEDG TLVAKLLETM HLTGADFTNT FCVLSSFPAD LSDSAEFLSR
     LTSQCASLEE LRLAFRPQMD PRQLSMMLML AQSNPQLFAL IGTQANVTKE LERVEHQSRL
     EQLSPSDLQR KNRDHWEAWL QEYRDRLDKE KEGVGDTAAW QAERVRVMRA NNPKYVLRNY
     IAQKAIEAAE NGDFSEVRLV LKLLESPYHS EEEATGPEAV ARSTEEQSSY SNRPPLWAAE
     LCVTUSS
//
ID   MTR1_MOUSE              Reviewed;         837 AA.
AC   Q9DBC3; Q3U3G5; Q3U7Y9; Q6A0D5; Q8C7V0;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Cap-specific mRNA (nucleoside-2'-O-)-methyltransferase 1;
DE            EC=2.1.1.57;
DE   AltName: Full=Cap1 2'O-ribose methyltransferase 1;
DE            Short=MTr1;
DE   AltName: Full=FtsJ methyltransferase domain-containing protein 2;
GN   Name=Ftsjd2; Synonyms=Kiaa0082;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Brain cortex, Dendritic cell, Embryonic stem cell, Liver,
RC   Macrophage, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 115-837.
RC   TISSUE=Embryonic tail;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-30, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC       mediates mRNA cap1 2'-O-ribose methylation to the 5'-cap structure
CC       of mRNAs. Methylates the ribose of the first nucleotide of a
CC       m(7)GpppG-capped mRNA to produce m(7)GpppNmp (cap1). Cap1
CC       modification is linked to higher levels of translation (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + m(7)G(5')pppR-RNA =
CC       S-adenosyl-L-homocysteine + m(7)G(5')pppRm-RNA.
CC   -!- SUBUNIT: Interacts with POLR2A (via C-terminus) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. RrmJ
CC       family.
CC   -!- SIMILARITY: Contains 1 G-patch domain.
CC   -!- SIMILARITY: Contains 1 WW domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32161.1; Type=Frameshift; Positions=532;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK005044; BAB23771.1; -; mRNA.
DR   EMBL; AK042060; BAC31146.1; -; mRNA.
DR   EMBL; AK043733; BAC31634.1; -; mRNA.
DR   EMBL; AK049190; BAC33600.1; -; mRNA.
DR   EMBL; AK080379; BAC37899.1; -; mRNA.
DR   EMBL; AK150392; BAE29520.1; -; mRNA.
DR   EMBL; AK151194; BAE30191.1; -; mRNA.
DR   EMBL; AK152276; BAE31091.1; -; mRNA.
DR   EMBL; AK152452; BAE31230.1; -; mRNA.
DR   EMBL; AK152799; BAE31504.1; -; mRNA.
DR   EMBL; AK153021; BAE31655.1; -; mRNA.
DR   EMBL; AK153066; BAE31692.1; -; mRNA.
DR   EMBL; AK154773; BAE32821.1; -; mRNA.
DR   EMBL; BC024691; AAH24691.1; -; mRNA.
DR   EMBL; AK172883; BAD32161.1; ALT_FRAME; Transcribed_RNA.
DR   IPI; IPI00459652; -.
DR   RefSeq; NP_083067.1; NM_028791.5.
DR   UniGene; Mm.475060; -.
DR   ProteinModelPortal; Q9DBC3; -.
DR   PhosphoSite; Q9DBC3; -.
DR   PRIDE; Q9DBC3; -.
DR   Ensembl; ENSMUST00000024816; ENSMUSP00000024816; ENSMUSG00000024019.
DR   GeneID; 74157; -.
DR   KEGG; mmu:74157; -.
DR   UCSC; uc008bth.1; mouse.
DR   CTD; 74157; -.
DR   MGI; MGI:1921407; Ftsjd2.
DR   GeneTree; ENSGT00530000063742; -.
DR   HOGENOM; HBG713770; -.
DR   HOVERGEN; HBG057271; -.
DR   InParanoid; Q9DBC3; -.
DR   OMA; RLSYTGR; -.
DR   NextBio; 339938; -.
DR   ArrayExpress; Q9DBC3; -.
DR   Bgee; Q9DBC3; -.
DR   CleanEx; MM_1300018I05RIK; -.
DR   Genevestigator; Q9DBC3; -.
DR   GermOnline; ENSMUSG00000024019; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004483; F:mRNA (nucleoside-2'-O-)-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006370; P:mRNA capping; ISS:UniProtKB.
DR   InterPro; IPR000467; G_patch.
DR   InterPro; IPR002877; rRNA_MeTrfase_RrmJ/FtsJ.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Pfam; PF01728; FtsJ; 1.
DR   Pfam; PF01585; G-patch; 1.
DR   SMART; SM00443; G_patch; 1.
DR   SMART; SM00456; WW; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; FALSE_NEG.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Methyltransferase; mRNA capping; mRNA processing;
KW   Nucleus; Phosphoprotein; S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1    837       Cap-specific mRNA (nucleoside-2'-O-)-
FT                                methyltransferase 1.
FT                                /FTId=PRO_0000251240.
FT   DOMAIN       86    132       G-patch.
FT   DOMAIN      751    785       WW.
FT   REGION      726    834       Interaction with POLR2A (By similarity).
FT   ACT_SITE    403    403       Proton acceptor (By similarity).
FT   BINDING     280    280       S-adenosyl-L-methionine; via amide
FT                                nitrogen (By similarity).
FT   BINDING     310    310       S-adenosyl-L-methionine (By similarity).
FT   BINDING     363    363       S-adenosyl-L-methionine (By similarity).
FT   MOD_RES      27     27       Phosphoserine.
FT   MOD_RES      30     30       Phosphoserine.
FT   MOD_RES      50     50       Phosphoserine (By similarity).
FT   MOD_RES      52     52       Phosphoserine (By similarity).
FT   MOD_RES      54     54       Phosphoserine (By similarity).
FT   MOD_RES      63     63       Phosphoserine (By similarity).
FT   MOD_RES     107    107       N6-acetyllysine (By similarity).
FT   MOD_RES     223    223       Phosphotyrosine (By similarity).
FT   CONFLICT    151    151       C -> W (in Ref. 1; BAE32821).
FT   CONFLICT    378    378       L -> F (in Ref. 1; BAE31091/BAE31230).
FT   CONFLICT    459    459       L -> I (in Ref. 1; BAE31091/BAE31230).
FT   CONFLICT    500    500       E -> V (in Ref. 1; BAE31091/BAE31230).
FT   CONFLICT    689    689       V -> I (in Ref. 1; BAC33600).
SQ   SEQUENCE   837 AA;  95676 MW;  8DB980D2FFA4F9C7 CRC64;
     MKRRTDPECT APLKKQKRIG ELARHLSSTS DDEPLSSVNH AAKASATSLS GSDSETEGKQ
     PCSDDFKDAF KADSLVEGTS SRYSMYNSVS QRLMAKMGFR EGEGLGKYSQ GRKDIVETSN
     QKGRRGLGLT LQGFDQELNV DWRDEPEPNA CEQVSWFPEC TTEIPDSREM SDWMVVGKRK
     MVIEDETEFC GEELLHSMLK CKSVFDILDG EEMRRARTRA NPYEMIRGVF FLNRAAMKMA
     NMDFVFDRMF TNPLDSSGKP LLKESDIDLL YFADVCAGPG GFSEYVLWRK KWHAKGFGMT
     LKGPNDFKLE DFYSASSELF EPYYGEGGVD GDGDITRPEN INAFRNFVLD NTDRKGVHFV
     MADGGFSVEG QENLQEILSK QLLLCQFLMA LSVVRTGGHF VCKTFDLFTP FSVGLIYLLY
     CCFERVCLFK PITSRPANSE RYVVCKGLKV GIDDVREYLF SVNIKLNQLR NTESDVNLVV
     PLMVIKGDHE FNDYMIRSNE SYCSLQIKAL AKIHAFVQDT TLSEPRQAEI RKECLQLWKI
     PDQARVAPSS SDPKFKFFEL IKDTDINIFS YKPTLLTAKT LEKIRPVLEY RCMVSGSEQK
     FLLGLGKSQI YTWDGRQSDR WVKLDLKTEL PRDTLLCVEI VHELKGEGKA QRKISAIHIL
     DVLVLNGSDV REQHFNQRIQ LAEKFVKAVS KPSRPDMNPI RVKEVYRLEE MEKIFVRLEM
     KLIKGSGGTP KLSYTGRDDR HFVPTGVYIV RTVNEPWTMG FSKSNNRKFF YNKKTQKSVY
     ALPTESIAPF HTCYYSRLFW EWGDGFHMRD SQKPQDPDKL SKEDVLSFIQ SHNPLGP
//
ID   KAP0_MOUSE              Reviewed;         381 AA.
AC   Q9DBC7; Q3UKU7; Q9JHR5; Q9JHR6;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=cAMP-dependent protein kinase type I-alpha regulatory subunit;
GN   Name=Prkar1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Kidney, Liver, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60 AND 259-382.
RX   MEDLINE=20374962; PubMed=10913627; DOI=10.1016/S0014-5793(00)01653-7;
RA   Barradeau S., Imaizumi-Scherrer T., Weiss M.C., Faust D.M.;
RT   "Alternative 5'-exons of the mouse cAMP-dependent protein kinase
RT   subunit RIalpha gene are conserved and expressed in both a ubiquitous
RT   and tissue-restricted fashion.";
RL   FEBS Lett. 476:272-276(2000).
RN   [4]
RP   INTERACTION WITH AKAP4.
RX   PubMed=9852104; DOI=10.1074/jbc.273.51.34384;
RA   Miki K., Eddy E.M.;
RT   "Identification of tethering domains for protein kinase A type Ialpha
RT   regulatory subunits on sperm fibrous sheath protein FSC1.";
RL   J. Biol. Chem. 273:34384-34390(1998).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-83, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-83, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- SUBUNIT: The inactive form of the enzyme is composed of two
CC       regulatory chains and two catalytic chains. Activation by cAMP
CC       produces two active catalytic monomers and a regulatory dimer that
CC       binds four cAMP molecules. PRKAR1A also interacts with RFC2; the
CC       complex may be involved in cell survival. Interacts with RARA; the
CC       interaction occurs in the presence of cAMP or FSH and regulates
CC       RARA transcriptional activity (By similarity). Interacts with
CC       AKAP4.
CC   -!- PTM: The pseudophosphorylation site binds to the substrate-binding
CC       region of the catalytic chain, resulting in the inhibition of its
CC       activity (By similarity).
CC   -!- MISCELLANEOUS: Two types of regulatory chains are found: type I,
CC       which predominates in skeletal muscle, and type II, which
CC       predominates in cardiac muscle (By similarity).
CC   -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC       family.
CC   -!- SIMILARITY: Contains 2 cyclic nucleotide-binding domains.
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DR   EMBL; AK005039; BAB23766.1; -; mRNA.
DR   EMBL; AK027916; BAC25664.1; -; mRNA.
DR   EMBL; AK051068; BAC34516.1; -; mRNA.
DR   EMBL; AK145797; BAE26655.1; -; mRNA.
DR   EMBL; AK145860; BAE26704.1; -; mRNA.
DR   EMBL; AK147188; BAE27748.1; -; mRNA.
DR   EMBL; AK150427; BAE29550.1; -; mRNA.
DR   EMBL; AK151124; BAE30132.1; -; mRNA.
DR   EMBL; AK153227; BAE31820.1; -; mRNA.
DR   EMBL; BC003461; AAH03461.1; -; mRNA.
DR   EMBL; BC005697; AAH05697.1; -; mRNA.
DR   EMBL; AJ278427; CAB94778.1; -; Genomic_DNA.
DR   EMBL; AJ278429; CAB94718.1; -; Genomic_DNA.
DR   IPI; IPI00762049; -.
DR   RefSeq; NP_068680.1; NM_021880.2.
DR   UniGene; Mm.30039; -.
DR   ProteinModelPortal; Q9DBC7; -.
DR   SMR; Q9DBC7; 14-62, 94-378.
DR   IntAct; Q9DBC7; 10.
DR   STRING; Q9DBC7; -.
DR   PhosphoSite; Q9DBC7; -.
DR   REPRODUCTION-2DPAGE; IPI00762049; -.
DR   REPRODUCTION-2DPAGE; Q9DBC7; -.
DR   PRIDE; Q9DBC7; -.
DR   Ensembl; ENSMUST00000020932; ENSMUSP00000020932; ENSMUSG00000020612.
DR   Ensembl; ENSMUST00000049527; ENSMUSP00000056500; ENSMUSG00000020612.
DR   Ensembl; ENSMUST00000106677; ENSMUSP00000102288; ENSMUSG00000020612.
DR   GeneID; 19084; -.
DR   KEGG; mmu:19084; -.
DR   UCSC; uc007mct.1; mouse.
DR   CTD; 19084; -.
DR   MGI; MGI:104878; Prkar1a.
DR   GeneTree; ENSGT00530000062947; -.
DR   HOVERGEN; HBG002025; -.
DR   InParanoid; Q9DBC7; -.
DR   OrthoDB; EOG4JQ3XP; -.
DR   PhylomeDB; Q9DBC7; -.
DR   NextBio; 295622; -.
DR   ArrayExpress; Q9DBC7; -.
DR   Bgee; Q9DBC7; -.
DR   Genevestigator; Q9DBC7; -.
DR   GermOnline; ENSMUSG00000020612; Mus musculus.
DR   GO; GO:0005952; C:cAMP-dependent protein kinase complex; IEA:InterPro.
DR   GO; GO:0005737; C:cytoplasm; TAS:MGI.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0008283; P:cell proliferation; TAS:MGI.
DR   GO; GO:0001707; P:mesoderm formation; IMP:MGI.
DR   GO; GO:0009887; P:organ morphogenesis; TAS:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; TAS:MGI.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR002373; cAMP/cGMP_kin.
DR   InterPro; IPR012198; cAMP_dep_PK_reg_su.
DR   InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR018488; cNMP-bd_CS.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 2.
DR   Pfam; PF00027; cNMP_binding; 2.
DR   Pfam; PF02197; RIIa; 1.
DR   PIRSF; PIRSF000548; PK_regulatory; 1.
DR   PRINTS; PR00103; CAMPKINASE.
DR   SMART; SM00100; cNMP; 2.
DR   SMART; SM00394; RIIa; 1.
DR   SUPFAM; SSF47391; cAMP-dep_prot_kin_reg_I/II_a/b; 1.
DR   SUPFAM; SSF51206; cNMP_binding; 2.
DR   PROSITE; PS00888; CNMP_BINDING_1; 2.
DR   PROSITE; PS00889; CNMP_BINDING_2; 2.
DR   PROSITE; PS50042; CNMP_BINDING_3; 2.
PE   1: Evidence at protein level;
KW   Acetylation; cAMP; cAMP-binding; Disulfide bond; Nucleotide-binding;
KW   Phosphoprotein; Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    381       cAMP-dependent protein kinase type I-
FT                                alpha regulatory subunit.
FT                                /FTId=PRO_0000205378.
FT   NP_BIND     137    254       cAMP 1.
FT   NP_BIND     255    381       cAMP 2.
FT   REGION        2    136       Dimerization and phosphorylation.
FT   MOTIF        96    100       Pseudophosphorylation motif.
FT   BINDING     202    202       cAMP 1.
FT   BINDING     211    211       cAMP 1.
FT   BINDING     326    326       cAMP 2.
FT   BINDING     335    335       cAMP 2.
FT   MOD_RES       2      2       N-acetylalanine (Probable).
FT   MOD_RES      77     77       Phosphoserine.
FT   MOD_RES      83     83       Phosphoserine.
FT   MOD_RES     101    101       Phosphoserine.
FT   DISULFID     18     18       Interchain (with C-39) (By similarity).
FT   DISULFID     39     39       Interchain (with C-18) (By similarity).
SQ   SEQUENCE   381 AA;  43185 MW;  08F164BB4528C63B CRC64;
     MASGSMATSE EERSLRECEL YVQKHNIQAL LKDSIVQLCT TRPERPMAFL REYFERLEKE
     EARQIQCLQK TGIRTDSRED EISPPPPNPV VKGRRRRGAI SAEVYTEEDA ASYVRKVIPK
     DYKTMAALAK AIEKNVLFSH LDDNERSDIF DAMFPVSFIA GETVIQQGDE GDNFYVIDQG
     EMDVYVNNEW ATSVGEGGSF GELALIYGTP RAATVKAKTN VKLWGIDRDS YRRILMGSTL
     RKRKMYEEFL SKVSILESLD KWERLTVADA LEPVQFEDGQ KIVVQGEPGD EFFIILEGTA
     AVLQRRSENE EFVEVGRLGP SDYFGEIALL MNRPRAATVV ARGPLKCVKL DRPRFERVLG
     PCSDILKRNI QQYNSFVSLS V
//
ID   PELP1_MOUSE             Reviewed;        1123 AA.
AC   Q9DBD5; Q5F2E2; Q6PEM0; Q91YM9;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Proline-, glutamic acid- and leucine-rich protein 1;
DE   AltName: Full=Modulator of non-genomic activity of estrogen receptor;
GN   Name=Pelp1; Synonyms=Mnar;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N;
RC   TISSUE=Embryonic brain, Liver, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=21474315; PubMed=11481323; DOI=10.1074/jbc.M103783200;
RA   Vadlamudi R.K., Wang R.-A., Mazumdar A., Kim Y.-S., Shin J., Sahin A.,
RA   Kumar R.;
RT   "Molecular cloning and characterization of PELP1, a novel human
RT   coregulator of estrogen receptor alpha.";
RL   J. Biol. Chem. 276:38272-38279(2001).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-751, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Coactivator of estrogen receptor-mediated transcription
CC       and a corepressor of other nuclear hormone receptors and sequence-
CC       specific transcription factors. Plays a role in estrogen receptor
CC       (ER) genomic activity when present in the nuclear compartment by
CC       activating the ER target genes in a hormonal stimulation dependent
CC       manner. Can facilitate ER non-genomic signaling via SRC and PI3K
CC       interaction in the cytosol. Plays a role in E2-mediated cell cycle
CC       progression by interacting with RB1. May have important functional
CC       implications in ER/growth factor cross-talk. Interacts with
CC       several growth factor signaling components including EGFR and HRS.
CC       Involved in nuclear receptor signaling via its interaction with AR
CC       and NR3C1. May promote tumorigenesis via its interaction with and
CC       modulation of several oncogenes including SRC, PI3K, STAT3 and
CC       EGFR. Plays a role in cancer cell metastasis via its ability to
CC       modulate E2-mediated cytoskeleton changes and cell migration via
CC       its interaction with SRC and PI3K (By similarity).
CC   -!- SUBUNIT: Interacts with HRS, RXRA, SUMO2, HDAC2, RB1 and STAT3.
CC       Interacts with PI3K, SRC and EGFR in cytoplasm. Interacts with
CC       ESR1 and ESR2 and this interaction is enhanced by 17-beta-
CC       estradiol. Interacts with CREBBP, EP300, AR and NR3C1 in a ligand-
CC       dependent manner. Forms two complexes in the presence of 17-beta-
CC       estradiol; one with SRC and ESR1 and the other with LCK and ESR1.
CC       Interacts with histone H1 and H3 with a greater affinity for H1.
CC       Component of some MLL1/MLL complex, at least composed of the core
CC       components MLL, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the
CC       facultative components C17orf49, CHD8, E2F6, HSP70, IN80C,
CC       KIAA1267, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31,
CC       RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7,
CC       TAF9 and TEX10 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity). Note=Also found associated with the plasma membrane
CC       (By similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed with high levels in testis,
CC       ovary, uterus and pituitary gland.
CC   -!- DOMAIN: The Glu-rich region mediates histones interaction (By
CC       similarity).
CC   -!- DOMAIN: The Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs are required for
CC       the association with nuclear receptor ESR1 (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
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DR   EMBL; AK005027; BAB23754.1; -; mRNA.
DR   EMBL; AL596096; CAI51981.1; -; Genomic_DNA.
DR   EMBL; BC016444; AAH16444.1; -; mRNA.
DR   EMBL; BC057987; AAH57987.1; -; mRNA.
DR   EMBL; BC090620; AAH90620.1; -; mRNA.
DR   IPI; IPI00321597; -.
DR   RefSeq; NP_083507.3; NM_029231.4.
DR   UniGene; Mm.340601; -.
DR   ProteinModelPortal; Q9DBD5; -.
DR   STRING; Q9DBD5; -.
DR   PhosphoSite; Q9DBD5; -.
DR   PRIDE; Q9DBD5; -.
DR   Ensembl; ENSMUST00000019065; ENSMUSP00000019065; ENSMUSG00000018921.
DR   GeneID; 75273; -.
DR   KEGG; mmu:75273; -.
DR   NMPDR; fig|10090.3.peg.24558; -.
DR   UCSC; uc007jup.1; mouse.
DR   CTD; 75273; -.
DR   MGI; MGI:1922523; Pelp1.
DR   eggNOG; roNOG07164; -.
DR   GeneTree; ENSGT00570000079050; -.
DR   HOGENOM; HBG446761; -.
DR   HOVERGEN; HBG080634; -.
DR   InParanoid; Q9DBD5; -.
DR   OMA; IPPDETF; -.
DR   OrthoDB; EOG4FJ889; -.
DR   PhylomeDB; Q9DBD5; -.
DR   NextBio; 342600; -.
DR   ArrayExpress; Q9DBD5; -.
DR   Bgee; Q9DBD5; -.
DR   CleanEx; MM_PELP1; -.
DR   Genevestigator; Q9DBD5; -.
DR   GermOnline; ENSMUSG00000018921; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR012583; NUC201.
DR   InterPro; IPR012980; Uncharacterised_NUC202.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 2.
DR   Pfam; PF08167; NUC201; 1.
DR   Pfam; PF08166; NUC202; 2.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Cytoplasm; Nucleus; Phosphoprotein; Repeat;
KW   Repressor; Transcription.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   1123       Proline-, glutamic acid- and leucine-rich
FT                                protein 1.
FT                                /FTId=PRO_0000252137.
FT   MOTIF        33     37       LXXLL motif 1.
FT   MOTIF        69     73       LXXLL motif 2.
FT   MOTIF       111    115       LXXLL motif 3.
FT   MOTIF       155    159       LXXLL motif 4.
FT   MOTIF       177    181       LXXLL motif 5.
FT   MOTIF       264    268       LXXLL motif 6.
FT   MOTIF       271    275       LXXLL motif 7.
FT   MOTIF       365    369       LXXLL motif 8.
FT   MOTIF       460    464       LXXLL motif 9.
FT   MOTIF       580    584       LXXLL motif 10.
FT   MOTIF       585    589       LXXLL motif 11.
FT   COMPBIAS     33    407       Leu-rich.
FT   COMPBIAS    634    876       Pro-rich.
FT   COMPBIAS    893   1094       Glu-rich.
FT   COMPBIAS    974   1121       Pro-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      13     13       Phosphoserine.
FT   MOD_RES     478    478       Phosphoserine (By similarity).
FT   MOD_RES     482    482       Phosphoserine (By similarity).
FT   MOD_RES     749    749       Phosphoserine (By similarity).
FT   MOD_RES     751    751       Phosphothreonine.
FT   MOD_RES    1029   1029       Phosphoserine (By similarity).
FT   MOD_RES    1039   1039       Phosphoserine (By similarity).
FT   MOD_RES    1083   1083       Phosphothreonine (By similarity).
FT   MOD_RES    1098   1098       Phosphothreonine (By similarity).
FT   CONFLICT    566    566       L -> P (in Ref. 3; AAH16444/AAH57987).
FT   CONFLICT    864    864       Q -> L (in Ref. 1; BAB23754).
SQ   SEQUENCE   1123 AA;  118069 MW;  571BF1BD6A705067 CRC64;
     MAAAVLSGAS AGSPAGAPGG PGGLSAVGSG PRLRLLLLES ISGLLQPRTA SPVAPVHPPI
     QWAPHLPGLM CLLRLHGTAG GAQNLSALGA LVNLSNAHLG SIKTRFEGLC LLSLLIGESP
     TELFQQHCVS WLRSIQQVLQ SQDSPSTMEL AVAVLRDLLR HASQLPTLFR DISTNHLPGL
     LTSLLGLRPE CEQSALEGMK ACVTYFPRAC GSLKGKLASF FLSRLDSLNP QLQQLACECY
     SRLPSLGAGF SQGLKHTENW EQELHSLLTS LHSLLGSLFE ETEPAPVQSE GPGIEMLLSH
     SEDGNTHVLL QLRQRFSGLA RCLGLMLSSE FGAPVSVPVQ EILDLICRIL GISSKNINLL
     GDGPLRLLLL PSLHLEALDL LSALILACGS RLLRFGALIS RLLPQVLNAW STGRDTLAPG
     QERPYSTIRT KVYAILELWV QVCGASAGML QGGASGEALL THLLSDISPP ADALKLCSTR
     GSSDGGLQSG KPSAPKKLKL DMGEALAPPS QRKGDRNANS DVCAAALRGL SRTILMCGPL
     IKEETHRRLH DLVLPLVMSV QQGEVLGSSP YNSSCCRLGL YRLLLALLLA PSPRCPPPLA
     CALKAFSLGQ WEDSLEVSSF CSEALVTCAA LTHPRVPPLQ SSGPACPTPA PVPPPEAPSS
     FRAPAFHPPG PMPSIGAVPS TGPLPSAGPI PTVGSMASTG QVPSRPGPPA TANHLGLSVP
     GLVSVPPRLL PGPENHRAGS GEDPVLAPSG TPPPSIPPDE TFGGRVPRPA FVHYDKEEAS
     DVEISLESDS DDSVVIVPEG LPSLPPAPPS GTPPPAAPAG PPTASPPVPA KEDSEELPAT
     PGPPPPPPPP PPPASGPVTL PPPQLVPEGT PGGGGPTAME EDLTVININS SDEEEEEEEE
     EEEEDEDEEE EDFEEEEEDE EEYFEEEEEE EEFEEEFEEE EGELEEEEEE EEEELDEVED
     VEFGSAGEVE EGGPPPPTLP PALPPSDSPK VQPEAEPEPG LLLEVEEPGP EEVPGPETAP
     TLAPEVLPSQ EEGEQEVGSP AAGPPQELVE ESSAPPALLE EGTEGGGDKV PPPPETPAEE
     METEAEVPAP QEKEQDDTAA MLADFIDCPP DDEKPPPATE PDS
//
ID   PGAM1_MOUSE             Reviewed;         254 AA.
AC   Q9DBJ1; Q9D6W0; Q9ERT3;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 106.
DE   RecName: Full=Phosphoglycerate mutase 1;
DE            EC=3.1.3.13;
DE            EC=5.4.2.1;
DE            EC=5.4.2.4;
DE   AltName: Full=BPG-dependent PGAM 1;
DE   AltName: Full=Phosphoglycerate mutase isozyme B;
DE            Short=PGAM-B;
GN   Name=Pgam1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Yu L.;
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 11-39; 47-61; 91-100; 118-138; 163-176; 181-191;
RP   223-240 AND 242-251, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Yang J.W., Zigmond M.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-26, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-26, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Interconversion of 3- and 2-phosphoglycerate with 2,3-
CC       bisphosphoglycerate as the primer of the reaction. Can also
CC       catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13
CC       (phosphatase), but with a reduced activity.
CC   -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate.
CC   -!- CATALYTIC ACTIVITY: 3-phospho-D-glyceroyl phosphate = 2,3-
CC       bisphospho-D-glycerate.
CC   -!- CATALYTIC ACTIVITY: 2,3-bisphospho-D-glycerate + H(2)O = 3-
CC       phospho-D-glycerate + phosphate.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- TISSUE SPECIFICITY: In mammalian tissues there are two types of
CC       phosphoglycerate mutase isozymes: type-M in muscles and type-B in
CC       other tissues.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily.
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DR   EMBL; AF283667; AAG13955.1; -; mRNA.
DR   EMBL; AK004921; BAB23672.1; -; mRNA.
DR   EMBL; AK009905; BAB26576.1; -; mRNA.
DR   EMBL; BC002241; AAH02241.1; -; mRNA.
DR   EMBL; BC005661; AAH05661.1; -; mRNA.
DR   EMBL; BC066844; AAH66844.1; -; mRNA.
DR   EMBL; BC083090; AAH83090.1; -; mRNA.
DR   IPI; IPI00457898; -.
DR   RefSeq; NP_075907.2; NM_023418.2.
DR   UniGene; Mm.391589; -.
DR   UniGene; Mm.480556; -.
DR   ProteinModelPortal; Q9DBJ1; -.
DR   SMR; Q9DBJ1; 3-245.
DR   STRING; Q9DBJ1; -.
DR   PhosphoSite; Q9DBJ1; -.
DR   COMPLUYEAST-2DPAGE; Q9DBJ1; -.
DR   REPRODUCTION-2DPAGE; IPI00457898; -.
DR   REPRODUCTION-2DPAGE; Q9DBJ1; -.
DR   PRIDE; Q9DBJ1; -.
DR   Ensembl; ENSMUST00000011896; ENSMUSP00000011896; ENSMUSG00000011752.
DR   GeneID; 18648; -.
DR   KEGG; mmu:18648; -.
DR   UCSC; uc008hml.1; mouse.
DR   CTD; 18648; -.
DR   MGI; MGI:97552; Pgam1.
DR   GeneTree; ENSGT00390000016700; -.
DR   HOGENOM; HBG658938; -.
DR   HOVERGEN; HBG027528; -.
DR   InParanoid; Q9DBJ1; -.
DR   OMA; TGWKDPD; -.
DR   OrthoDB; EOG4MCX10; -.
DR   PhylomeDB; Q9DBJ1; -.
DR   BRENDA; 3.1.3.13; 244.
DR   BRENDA; 5.4.2.1; 244.
DR   BRENDA; 5.4.2.4; 244.
DR   NextBio; 294652; -.
DR   Bgee; Q9DBJ1; -.
DR   CleanEx; MM_PGAM1; -.
DR   Genevestigator; Q9DBJ1; -.
DR   GermOnline; ENSMUSG00000011752; Mus musculus.
DR   GermOnline; ENSMUSG00000066695; Mus musculus.
DR   GermOnline; ENSMUSG00000069106; Mus musculus.
DR   GO; GO:0004083; F:2,3-bisphospho-D-glycerate 2-phosphohydrolase activity; IEA:EC.
DR   GO; GO:0004082; F:bisphosphoglycerate mutase activity; IEA:EC.
DR   GO; GO:0004619; F:phosphoglycerate mutase activity; IDA:MGI.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR001345; PG/BPGM_mutase_AS.
DR   InterPro; IPR005952; Phosphogly_mut1.
DR   PANTHER; PTHR11931; Phosphogly_mut1; 1.
DR   Pfam; PF00300; PGAM; 1.
DR   SMART; SM00855; PGAM; 1.
DR   TIGRFAMs; TIGR01258; pgm_1; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Glycolysis; Hydrolase;
KW   Isomerase; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    254       Phosphoglycerate mutase 1.
FT                                /FTId=PRO_0000179826.
FT   COMPBIAS    122    131       Pro-rich.
FT   ACT_SITE     11     11       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   ACT_SITE    186    186       By similarity.
FT   SITE         62     62       Interaction with carboxyl group of
FT                                phosphoglycerates (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      14     14       Phosphoserine.
FT   MOD_RES      26     26       Phosphotyrosine.
FT   MOD_RES      31     31       Phosphoserine (By similarity).
FT   MOD_RES      92     92       Phosphotyrosine (By similarity).
FT   MOD_RES     118    118       Phosphoserine.
FT   CONFLICT     42     42       G -> R (in Ref. 1; AAG13955).
FT   CONFLICT     65     65       R -> Q (in Ref. 1; AAG13955).
FT   CONFLICT     85     85       W -> G (in Ref. 2; BAB26576).
FT   CONFLICT    152    152       S -> F (in Ref. 1; AAG13955).
FT   CONFLICT    176    176       K -> I (in Ref. 1; AAG13955).
FT   CONFLICT    195    197       KHL -> MHV (in Ref. 1; AAG13955).
SQ   SEQUENCE   254 AA;  28832 MW;  6DC09A3BEBB22409 CRC64;
     MAAYKLVLIR HGESAWNLEN RFSGWYDADL SPAGHEEAKR GGQALRDAGY EFDICFTSVQ
     KRAIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEA QVKIWRRSYD
     VPPPPMEPDH PFYSNISKDR RYADLTEDQL PSCESLKDTI ARALPFWNEE IVPQIKEGKR
     VLIAAHGNSL RGIVKHLEGL SEEAIMELNL PTGIPIVYEL DKNLKPIKPM QFLGDEETVR
     KAMEAVAAQG KVKK
//
ID   K1191_MOUSE             Reviewed;         303 AA.
AC   Q9DBN4; Q3TJ26; Q3UMA7; Q69ZP2; Q8C1J8; Q9D4T9;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=UPF0498 protein KIAA1191;
GN   Name=Kiaa1191;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Amnion, Head, Liver, Mammary gland, Placenta, Skin, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9DBN4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9DBN4-2; Sequence=VSP_028802, VSP_028803;
CC         Note=Ref.2 (BAC25449) sequence differs from that shown due to a
CC         frameshift in position 38;
CC       Name=3;
CC         IsoId=Q9DBN4-3; Sequence=VSP_028804, VSP_028805;
CC   -!- SIMILARITY: Belongs to the UPF0498 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32404.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK173126; BAD32404.1; ALT_INIT; mRNA.
DR   EMBL; AK004845; BAB23611.1; -; mRNA.
DR   EMBL; AK014792; BAC25449.1; ALT_FRAME; mRNA.
DR   EMBL; AK016176; BAB30137.1; -; mRNA.
DR   EMBL; AK028697; BAC26072.1; -; mRNA.
DR   EMBL; AK145025; BAE26191.1; -; mRNA.
DR   EMBL; AK159945; BAE35501.1; -; mRNA.
DR   EMBL; AK167616; BAE39669.1; -; mRNA.
DR   EMBL; AK169399; BAE41145.1; -; mRNA.
DR   EMBL; BC033445; AAH33445.1; -; mRNA.
DR   EMBL; BC039775; AAH39775.1; -; mRNA.
DR   EMBL; BC043040; AAH43040.1; -; mRNA.
DR   EMBL; BC054417; AAH54417.1; -; mRNA.
DR   IPI; IPI00119921; -.
DR   IPI; IPI00224275; -.
DR   IPI; IPI00869362; -.
DR   RefSeq; NP_598558.1; NM_133797.3.
DR   UniGene; Mm.24593; -.
DR   UniGene; Mm.451378; -.
DR   ProteinModelPortal; Q9DBN4; -.
DR   PhosphoSite; Q9DBN4; -.
DR   PRIDE; Q9DBN4; -.
DR   Ensembl; ENSMUST00000026989; ENSMUSP00000026989; ENSMUSG00000025871.
DR   Ensembl; ENSMUST00000110014; ENSMUSP00000105641; ENSMUSG00000025871.
DR   GeneID; 97820; -.
DR   KEGG; mmu:97820; -.
DR   UCSC; uc007qof.1; mouse.
DR   MGI; MGI:1921162; 4833439L19Rik.
DR   eggNOG; roNOG09579; -.
DR   GeneTree; ENSGT00390000000537; -.
DR   HOGENOM; HBG445313; -.
DR   HOVERGEN; HBG055539; -.
DR   InParanoid; Q9DBN4; -.
DR   OMA; PEVPALE; -.
DR   OrthoDB; EOG4K9BCQ; -.
DR   NextBio; 353088; -.
DR   ArrayExpress; Q9DBN4; -.
DR   Bgee; Q9DBN4; -.
DR   CleanEx; MM_4833439L19RIK; -.
DR   Genevestigator; Q9DBN4; -.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    303       UPF0498 protein KIAA1191.
FT                                /FTId=PRO_0000307731.
FT   MOD_RES     183    183       Phosphoserine.
FT   MOD_RES     235    235       Phosphoserine.
FT   VAR_SEQ       1     70       Missing (in isoform 2).
FT                                /FTId=VSP_028802.
FT   VAR_SEQ      71    112       EEGAASVSSLAVTPSPATDSSDKAPVVKAKATHVIMSSLIT
FT                                K -> MGAFVALSRWLCSVQPSSLLGHLEPRSLFSAGSRAA
FT                                GGGRAE (in isoform 2).
FT                                /FTId=VSP_028803.
FT   VAR_SEQ     152    164       LHKLKLQSGETAK -> PHFPFKTASVIPF (in
FT                                isoform 3).
FT                                /FTId=VSP_028804.
FT   VAR_SEQ     165    303       Missing (in isoform 3).
FT                                /FTId=VSP_028805.
FT   CONFLICT     13     13       P -> H (in Ref. 2; BAE26191).
FT   CONFLICT    127    139       LRDAGYTPHKGLT -> RRDSCITPQWGLS (in Ref.
FT                                2; BAB30137).
FT   CONFLICT    143    143       T -> A (in Ref. 2; BAE39669).
FT   CONFLICT    145    145       Y -> L (in Ref. 2; BAB30137).
SQ   SEQUENCE   303 AA;  32715 MW;  2203ADB0AC7EB153 CRC64;
     MASRQPEVPA LAPSGPLGKM SLPIGMCRRA FSYDDALEDP APMTPPPSDM GSIPWKPVIP
     ERKYQHLDKT EEGAASVSSL AVTPSPATDS SDKAPVVKAK ATHVIMSSLI TKQTQESIQR
     FEQQAGLRDA GYTPHKGLTT EETKYLRVAE ALHKLKLQSG ETAKEEKHPA SAQSTPSSTP
     HASPKQKSRG WFPSGSSTAL PAPNPHTMDP GSGNDRNSAD KWSLFGPRPL QKSDSGFAIQ
     AYKGAPRPSP MEVMRAQATR VGEDPATFKP PKMDVPMVEG KKQPLRTHNL KPRDLNVLTP
     TGF
//
ID   PACE1_MOUSE             Reviewed;         735 AA.
AC   Q9DBQ7; Q3TRA7; Q6NY01; Q8BQC9; Q8BRJ1;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Protein-associating with the carboxyl-terminal domain of ezrin;
DE   AltName: Full=Ezrin-binding protein PACE-1;
DE   AltName: Full=SCY1-like protein 3;
GN   Name=Scyl3; Synonyms=Pace1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex, Embryo, Lung, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: May play a role in regulating cell adhesion/migration
CC       complexes in migrating cells.
CC   -!- SUBUNIT: Interacts with EZR/VIL2 C-terminal domain (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus
CC       (By similarity). Cell projection, lamellipodium (By similarity).
CC       Note=Colocalized with EZR/VIL2, actin and CD44 in lamellipodia (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9DBQ7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9DBQ7-2; Sequence=VSP_037985, VSP_013126;
CC         Note=May be produced at very low levels due to a premature stop
CC         codon in the mRNA, leading to nonsense-mediated mRNA decay. No
CC         experimental confirmation available;
CC       Name=3;
CC         IsoId=Q9DBQ7-3; Sequence=VSP_027369;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
CC   -!- PTM: May be myristoylated; myristoylation may target it to Golgi
CC       compartment (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily.
CC   -!- SIMILARITY: Contains 4 HEAT repeats.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC31777.1; Type=Erroneous translation; Note=Wrong choice of CDS;
CC       Sequence=BC066800; Type=Erroneous termination; Positions=613; Note=Translated as Leu;
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DR   EMBL; AK004809; BAB23580.1; -; mRNA.
DR   EMBL; AK044100; BAC31777.1; ALT_SEQ; mRNA.
DR   EMBL; AK050999; BAC34492.1; -; mRNA.
DR   EMBL; AK162937; BAE37123.1; -; mRNA.
DR   EMBL; BC043085; AAH43085.1; -; mRNA.
DR   EMBL; BC066800; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00120024; -.
DR   IPI; IPI00553378; -.
DR   IPI; IPI00857146; -.
DR   RefSeq; NP_083052.1; NM_028776.4.
DR   UniGene; Mm.389213; -.
DR   ProteinModelPortal; Q9DBQ7; -.
DR   SMR; Q9DBQ7; 334-408.
DR   PhosphoSite; Q9DBQ7; -.
DR   PRIDE; Q9DBQ7; -.
DR   Ensembl; ENSMUST00000027876; ENSMUSP00000027876; ENSMUSG00000026584.
DR   GeneID; 240880; -.
DR   KEGG; mmu:240880; -.
DR   UCSC; uc007dhq.1; mouse.
DR   UCSC; uc007dhr.1; mouse.
DR   CTD; 240880; -.
DR   MGI; MGI:1921385; Scyl3.
DR   eggNOG; roNOG15584; -.
DR   GeneTree; ENSGT00600000084511; -.
DR   HOGENOM; HBG714631; -.
DR   HOVERGEN; HBG053485; -.
DR   InParanoid; Q9DBQ7; -.
DR   OMA; WPDWSEP; -.
DR   OrthoDB; EOG4P2Q1R; -.
DR   PhylomeDB; Q9DBQ7; -.
DR   NextBio; 384781; -.
DR   ArrayExpress; Q9DBQ7; -.
DR   Bgee; Q9DBQ7; -.
DR   CleanEx; MM_SCYL3; -.
DR   Genevestigator; Q9DBQ7; -.
DR   GermOnline; ENSMUSG00000026584; Mus musculus.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell projection; Cytoplasm; Golgi apparatus;
KW   Lipoprotein; Myristate; Phosphoprotein; Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    735       Protein-associating with the carboxyl-
FT                                terminal domain of ezrin.
FT                                /FTId=PRO_0000058168.
FT   DOMAIN        2    245       Protein kinase.
FT   REPEAT      194    249       HEAT 1.
FT   REPEAT      285    323       HEAT 2.
FT   REPEAT      333    370       HEAT 3.
FT   REPEAT      372    409       HEAT 4.
FT   REGION      547    735       Interaction with EZR (By similarity).
FT   MOD_RES     475    475       Phosphoserine.
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
FT   VAR_SEQ      56     99       HLKTLRHPCLLRFLSCTVEADGIHLVTERVQPLEVALETLS
FT                                PAE -> MAFTSSLRECSLWKWPWKPCLLQKSVLESMTYCW
FT                                LLSSFMTEDI (in isoform 2).
FT                                /FTId=VSP_037985.
FT   VAR_SEQ     100    735       Missing (in isoform 2).
FT                                /FTId=VSP_013126.
FT   VAR_SEQ     319    331       Missing (in isoform 3).
FT                                /FTId=VSP_027369.
FT   CONFLICT     93     93       E -> Q (in Ref. 1; BAE37123).
FT   CONFLICT    226    226       L -> Q (in Ref. 2; BC066800).
SQ   SEQUENCE   735 AA;  81333 MW;  13E6652AE93A4424 CRC64;
     MGSENSALKS YTLRESPFTL PSGLAVYPAI LQDGKCASVF VYKRENEDKV NKAAKHLKTL
     RHPCLLRFLS CTVEADGIHL VTERVQPLEV ALETLSPAEV CAGIYDILLA LIFLHDRGHL
     THNNVCLSSV FVSEDGHWKL GGMETVCQVP QATPEFLRNI QSVRDPASIP PEEMSPEFSG
     LPESHGHARD AYAFGALVDS LLPIFNEQVS ADVLSSFLQI LHSALLNPMP ECRPALSTLL
     SHDFFRNDFL EVVNFLKSLT LKSEDEKTEF FKFLLDRVSC LSEELIASRL VPLLLNQLVF
     AEPVAVKSFL PYLLGPKKEN APGETPCLLS PALFQSRVIP VLLRLFEVHE EHVRMVLLSH
     IEAYVEHFTQ EQLKKVILPQ VLLGLRDTSN SIVAITLRSL AVLVSLLGPE VVVGGERTKI
     FKRTAPSFTK TSDLSPEGSP MHVVCSQQSR VSKVLEDPSS NVFPKWLSGN VPSSSRKRIQ
     EECYSSLSQT GDQFSHTIKF PMNGLSDVKN TSEDNGSFPA GSNKPEEWPD WSEPEEPEQQ
     PASIHRWPRE PCDVAESQHT NLTAEEVTWD DGEASFGTEI NSTATASAPV PVTSGGQSTS
     AALVPLTEES KPLQSSPSSK TSHRQHEEVK PPQVSQERPL KAPSGLGLGE EFTIQVKKKP
     VQDPELDWFA DMIPEIKPSG TFLILPELRT EVMVPDKDNV SSLMQFSSKF AATEMTEGEA
     EGWEGEELAW EDNNW
//
ID   XRN2_MOUSE              Reviewed;         951 AA.
AC   Q9DBR1; Q3TI26; Q3TKF2; Q3UZT9; Q61489; Q99KS7;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=5'-3' exoribonuclease 2;
DE            EC=3.1.13.-;
DE   AltName: Full=Protein Dhm1;
GN   Name=Xrn2; Synonyms=Dhm1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   MEDLINE=95192042; PubMed=7885830; DOI=10.1093/nar/23.3.357;
RA   Shobuike T., Sugano S., Yamashita T., Ikeda H.;
RT   "Characterization of cDNA encoding mouse homolog of fission yeast
RT   dhp1+ gene: structural and functional conservation.";
RL   Nucleic Acids Res. 23:357-361(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-417 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Eye, Forelimb, Lung, and Pituitary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6, and Czech II; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499 AND SER-501, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499 AND SER-501, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448; SER-499 AND
RP   SER-501, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499 AND SER-501, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Possesses 5'->3' exoribonuclease activity. May promote
CC       the termination of transcription by RNA polymerase II. During
CC       transcription termination, cleavage at the polyadenylation site
CC       liberates a 5' fragment which is subsequently processed to form
CC       the mature mRNA and a 3' fragment which remains attached to the
CC       elongating polymerase. The processive degradation of this 3'
CC       fragment by this protein may promote termination of transcription
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 5'- to 3'-
CC       direction to yield nucleoside 5'-phosphates.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9DBR1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9DBR1-2; Sequence=VSP_007235;
CC         Note=No experimental confirmation available. May result from the
CC         retention of an intron in the cDNA;
CC   -!- TISSUE SPECIFICITY: Expressed in the spleen, testis, heart, brain,
CC       lung, liver, skeletal muscle, and kidney.
CC   -!- SIMILARITY: Belongs to the 5'-3' exonuclease family. XRN2/RAT1
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 CCHC-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH04028.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; D38517; BAA07524.1; -; mRNA.
DR   EMBL; AK004800; BAB23573.1; -; mRNA.
DR   EMBL; AK031247; BAC27318.1; -; mRNA.
DR   EMBL; AK053643; BAC35458.1; -; mRNA.
DR   EMBL; AK133654; BAE21766.1; -; mRNA.
DR   EMBL; AK167019; BAE39193.1; -; mRNA.
DR   EMBL; AK168037; BAE40020.1; -; mRNA.
DR   EMBL; BC004028; AAH04028.1; ALT_INIT; mRNA.
DR   EMBL; BC054743; AAH54743.1; -; mRNA.
DR   IPI; IPI00120046; -.
DR   IPI; IPI00283057; -.
DR   PIR; I49635; I49635.
DR   RefSeq; NP_036047.2; NM_011917.2.
DR   UniGene; Mm.3065; -.
DR   ProteinModelPortal; Q9DBR1; -.
DR   SMR; Q9DBR1; 1-793.
DR   IntAct; Q9DBR1; 1.
DR   STRING; Q9DBR1; -.
DR   PhosphoSite; Q9DBR1; -.
DR   PRIDE; Q9DBR1; -.
DR   Ensembl; ENSMUST00000028921; ENSMUSP00000028921; ENSMUSG00000027433.
DR   GeneID; 24128; -.
DR   KEGG; mmu:24128; -.
DR   UCSC; uc008msq.1; mouse.
DR   UCSC; uc008msr.1; mouse.
DR   CTD; 24128; -.
DR   MGI; MGI:894687; Xrn2.
DR   GeneTree; ENSGT00600000084422; -.
DR   HOGENOM; HBG592534; -.
DR   HOVERGEN; HBG036677; -.
DR   InParanoid; Q9DBR1; -.
DR   OMA; RKRMKRD; -.
DR   OrthoDB; EOG4M0F0Z; -.
DR   PhylomeDB; Q9DBR1; -.
DR   NextBio; 304163; -.
DR   ArrayExpress; Q9DBR1; -.
DR   Bgee; Q9DBR1; -.
DR   CleanEx; MM_XRN2; -.
DR   Genevestigator; Q9DBR1; -.
DR   GermOnline; ENSMUSG00000027433; Mus musculus.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0004534; F:5'-3' exoribonuclease activity; NAS:UniProtKB.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016049; P:cell growth; IGI:UniProtKB.
DR   GO; GO:0000738; P:DNA catabolic process, exonucleolytic; ISS:UniProtKB.
DR   GO; GO:0006310; P:DNA recombination; NAS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; NAS:UniProtKB.
DR   GO; GO:0007017; P:microtubule-based process; TAS:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0007283; P:spermatogenesis; IEP:UniProtKB.
DR   GO; GO:0006353; P:transcription termination, DNA-dependent; IEA:UniProtKB-KW.
DR   InterPro; IPR017151; 5_3_exoribonuclease_2.
DR   InterPro; IPR004859; Put_53exo.
DR   InterPro; IPR001878; Znf_CCHC.
DR   Pfam; PF03159; XRN_N; 1.
DR   PIRSF; PIRSF037239; Exonuclease_Xrn2; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   PROSITE; PS50158; ZF_CCHC; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Exonuclease; Hydrolase;
KW   Metal-binding; mRNA processing; Nuclease; Nucleus; Phosphoprotein;
KW   Transcription; Transcription regulation; Transcription termination;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    951       5'-3' exoribonuclease 2.
FT                                /FTId=PRO_0000071397.
FT   ZN_FING     262    278       CCHC-type.
FT   MOD_RES     439    439       Phosphothreonine (By similarity).
FT   MOD_RES     448    448       Phosphoserine.
FT   MOD_RES     455    455       Phosphoserine (By similarity).
FT   MOD_RES     471    471       Phosphoserine (By similarity).
FT   MOD_RES     473    473       Phosphoserine (By similarity).
FT   MOD_RES     475    475       Phosphoserine (By similarity).
FT   MOD_RES     499    499       Phosphoserine.
FT   MOD_RES     501    501       Phosphoserine.
FT   MOD_RES     796    796       N6-acetyllysine (By similarity).
FT   VAR_SEQ     931    951       GYPREGRKYPLPPPSGRYSWN -> VISTMWAVEGKQHTAH
FT                                C (in isoform 2).
FT                                /FTId=VSP_007235.
FT   CONFLICT    122    124       SKE -> IKG (in Ref. 1; BAA07524).
FT   CONFLICT    221    221       H -> Q (in Ref. 1; BAA07524).
FT   CONFLICT    306    306       L -> P (in Ref. 2; BAE40020).
FT   CONFLICT    332    332       I -> N (in Ref. 1; BAA07524).
FT   CONFLICT    336    336       V -> E (in Ref. 1; BAA07524).
FT   CONFLICT    440    440       P -> H (in Ref. 2; BAE40020).
FT   CONFLICT    449    449       P -> Q (in Ref. 2; BAE40020).
FT   CONFLICT    493    493       K -> R (in Ref. 1; BAA07524).
FT   CONFLICT    563    563       Y -> L (in Ref. 1; BAA07524).
FT   CONFLICT    712    712       P -> H (in Ref. 2; BAC27318).
FT   CONFLICT    734    734       T -> K (in Ref. 2; BAC27318).
FT   CONFLICT    837    837       P -> L (in Ref. 1; BAA07524).
FT   CONFLICT    866    866       Q -> K (in Ref. 1; BAA07524).
FT   CONFLICT    889    889       P -> H (in Ref. 2; BAC27318).
FT   CONFLICT    923    923       D -> G (in Ref. 2; BAE40020).
FT   CONFLICT    930    930       Q -> QV (in Ref. 2; BAC27318).
SQ   SEQUENCE   951 AA;  108687 MW;  CF57479291DD18B9 CRC64;
     MGVPAFFRWL SRKYPSIIVN CVEEKPKECN GVKIPVDASK PNPNDVEFDN LYLDMNGIIH
     PCTHPEDKPA PKNEDEMMVA IFEYIDRLFN IVRPRRLLYM AIDGVAPRAK MNQQRSRRFR
     ASKEGMEAAV EKQRVREEIL AKGGFLPPEE IKERFDSNCI TPGTEFMDNL AKCLRYYIAD
     RLNNDPGWKN LTVILSDASA PGEGEHKIMD YIRRQRAQPN HDPNTHHCLC GADADLIMLG
     LATHEPNFTI IREEFKPNKP KPCALCNQFG HEVKDCEGLP REKKGKHDEL ADSLPCAEGE
     FIFLRLNVLR EYLERELTMA SLPFPFDVER SIDDWVFMCF FVGNDFLPHL PSLEIREGAI
     DRLVNIYKNV VHKTGGYLTE SGYVNLQRVQ MIMLAVGEVE DSIFKKRKDD EDSFRRRQKE
     KRKRMKRDQP AFTPSGILTP HALGSRNSPG CQVASNPRQA AYEMRMQRNS SPSISPNTSF
     ASDGSPSPLG GIKRKAEDSD SEPEPEDNVR LWEAGWKQRY YKNKFDVDAA DEKFRRKVVQ
     SYVEGLCWVL RYYYQGCASW KWYYPFHYAP FASDFEGIAD MSSEFEKGTK PFKPLEQLMG
     VFPAASGNFL PPTWRKLMSD PDSSIIDFYP EDFAIDLNGK KYAWQGVALL PFVDERRLRA
     ALEEVYPDLT PEENRRNSLG GDVLFVGKLH PLRDFILELY QTGSTEPVDV PPELCHGIQG
     TFSLDEEAIL PDQTVCSPVP MLRDLTQNTA VSINFKDPQF AEDYVFKAAM LPGARKPATV
     LKPGDWEKSS NGRQWKPQLG FNRDRRPVHL DQAAFRTLGH VTPRGSGTSV YTNTALPPAN
     YQGNNYRPLL RGQAQIPKLM SNMRPQDSWR GPPPLFQQHR FERSVGAEPL LPWNRMIQNQ
     NAAFQPNQYQ MLGGPGGYPP RRDDHRGGRQ GYPREGRKYP LPPPSGRYSW N
//
ID   FA13C_MOUSE             Reviewed;         601 AA.
AC   Q9DBR2;
DT   11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 47.
DE   RecName: Full=Protein FAM13C;
GN   Name=Fam13c; Synonyms=Fam13c1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 AND SER-258, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SIMILARITY: Belongs to the FAM13 family.
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DR   EMBL; AK004797; BAB23571.1; -; mRNA.
DR   IPI; IPI00120049; -.
DR   RefSeq; NP_077206.3; NM_024244.4.
DR   UniGene; Mm.477813; -.
DR   PRIDE; Q9DBR2; -.
DR   Ensembl; ENSMUST00000105436; ENSMUSP00000101076; ENSMUSG00000043259.
DR   GeneID; 71721; -.
DR   KEGG; mmu:71721; -.
DR   UCSC; uc007fnx.1; mouse.
DR   CTD; 71721; -.
DR   MGI; MGI:1918971; Fam13c.
DR   GeneTree; ENSGT00440000037511; -.
DR   HOGENOM; HBG282113; -.
DR   HOVERGEN; HBG051530; -.
DR   InParanoid; Q9DBR2; -.
DR   OrthoDB; EOG412M59; -.
DR   NextBio; 334327; -.
DR   ArrayExpress; Q9DBR2; -.
DR   Bgee; Q9DBR2; -.
DR   Genevestigator; Q9DBR2; -.
DR   GermOnline; ENSMUSG00000043259; Mus musculus.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    601       Protein FAM13C.
FT                                /FTId=PRO_0000058923.
FT   MOD_RES     130    130       Phosphoserine.
FT   MOD_RES     258    258       Phosphoserine.
SQ   SEQUENCE   601 AA;  66981 MW;  AB1CADCF04322BDD CRC64;
     MFSCFCFSLQ DNSFGSAAVT ECDEDTVSVH EDEDDCSGLR DEDNKENYPQ VAARLDELAL
     PSHEAQQHVE QTLPVDGVLR TSMGNFKSRK PKSILRAESG RNHGESQETE HVVPSQSECQ
     GRAGTPAHES PQSSIFRCQE TVRLQPRIDQ RATIWPKDAF GTQQDLHENS LLKLQALESG
     LCSAFLTTQE EDGQVHGVKD PAPASTQSAP ADSADPADPM PAHKDAPGDA DGTSEDLQSA
     GTSRLLYHIT DGDNPLLSPR CSIFSQSQRF NLDPESAPSP PSSQQFMMPR SSSRCGSGDG
     KEPQTITQLT KHIQSLKRKI RKFEEKFEQE KKYRPSHGDK TSNPEVLKWM NDLAKGRKQL
     KELKLKLSEE QGSTPKGPRR NLSCEQPPVP RENGKSEAVG PEPGSSGEET SDAVVPEKRE
     QTPPQDDGKG TKQDKNLIKP LYDRCRGIKQ ILPTPSLIPT IQEEEDSDED CPQGSQQPSL
     PDPVSRLPVG DHLIYSETEP VRTLLPDEKK EGKQPALSMS NLHEATMPVL LDHLRETRAD
     KKRLRKALRE FEEQFFKQTG RSPQKEDRMP MADEYCEYKH IKAKLRLLEV LISKQDVAQT
     I
//
ID   MYPT1_MOUSE             Reviewed;        1029 AA.
AC   Q9DBR7; Q05A74; Q8CBV2; Q99NB6;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2009, sequence version 2.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 12A;
DE   AltName: Full=Myosin phosphatase-targeting subunit 1;
DE            Short=Myosin phosphatase target subunit 1;
GN   Name=Ppp1r12a; Synonyms=Mypt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Lung, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-79.
RX   MEDLINE=21240333; PubMed=11342221; DOI=10.1016/S0167-4781(00)00285-2;
RA   Machida H., Ito M., Okamoto R., Shiraki K., Isaka N., Hartshorne D.J.,
RA   Nakano T.;
RT   "Molecular cloning and analysis of the 5'-flanking region of human
RT   MYPT1 gene.";
RL   Biochim. Biophys. Acta 1517:424-429(2001).
RN   [5]
RP   PHOSPHORYLATION, AND INTERACTION WITH ARHA AND CIT.
RX   PubMed=8662509; DOI=10.1126/science.273.5272.245;
RA   Kimura K., Ito M., Amano M., Chihara K., Fukata Y., Nakafuku M.,
RA   Yamamori B., Feng J., Nakano T., Okawa K., Iwamatsu A., Kaibuchi K.;
RT   "Regulation of myosin phosphatase by Rho and Rho-associated kinase
RT   (Rho-kinase).";
RL   Science 273:245-248(1996).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-443; SER-445; SER-870
RP   AND SER-909, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507 AND SER-666, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Regulates myosin phosphatase activity.
CC   -!- SUBUNIT: PP1 comprises a catalytic subunit, PPP1CA, PPP1CB or
CC       PPP1CC, and one or several targeting or regulatory subunits.
CC       PPP1R12A mediates binding to myosin. Binds PPP1R12B, ROCK1 and
CC       IL16 (By similarity). Interacts with ARHA and CIT. Interacts
CC       directly with PRKG1. Non-covalent dimer of 2 dimers; PRKG1-PRKG1
CC       and PPP1R12A-PPP1R12A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=Along
CC       actomyosin filaments and stress fibers (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9DBR7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9DBR7-2; Sequence=VSP_038478;
CC   -!- DOMAIN: Heterotetramerization is mediated by the interaction
CC       between a coiled-coil of PRKG1 and the leucine/isoleucine zipper
CC       of PPP1R12A/MBS, the myosin-binding subunit of the myosin
CC       phosphatase (By similarity).
CC   -!- PTM: Phosphorylated on upon DNA damage, probably by ATM or ATR (By
CC       similarity). Phosphorylated by CIT (Rho-associated kinase).
CC       Phosphorylated cooperatively by ROCK1 and CDC42BP on Thr-694.
CC   -!- PTM: In vitro, phosphorylation of Ser-693 by PKA and PKG appears
CC       to prevent phosphorylation of the inhibitory site Thr-694,
CC       probably mediated by PRKG1 (By similarity).
CC   -!- SIMILARITY: Contains 6 ANK repeats.
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DR   EMBL; AK035230; BAC28990.1; -; mRNA.
DR   EMBL; AK004785; BAB23563.1; -; mRNA.
DR   EMBL; CH466539; EDL21703.1; -; Genomic_DNA.
DR   EMBL; BC125381; AAI25382.1; -; mRNA.
DR   EMBL; BC137630; AAI37631.1; -; mRNA.
DR   EMBL; AB042280; BAB39108.1; -; Genomic_DNA.
DR   IPI; IPI00671847; -.
DR   IPI; IPI00876048; -.
DR   RefSeq; NP_082168.1; NM_027892.2.
DR   UniGene; Mm.422959; -.
DR   UniGene; Mm.480604; -.
DR   ProteinModelPortal; Q9DBR7; -.
DR   SMR; Q9DBR7; 1-291.
DR   DIP; DIP-29982N; -.
DR   STRING; Q9DBR7; -.
DR   PhosphoSite; Q9DBR7; -.
DR   PRIDE; Q9DBR7; -.
DR   Ensembl; ENSMUST00000070663; ENSMUSP00000069257; ENSMUSG00000019907.
DR   Ensembl; ENSMUST00000105279; ENSMUSP00000100915; ENSMUSG00000019907.
DR   GeneID; 17931; -.
DR   KEGG; mmu:17931; -.
DR   UCSC; uc007gzc.1; mouse.
DR   CTD; 17931; -.
DR   MGI; MGI:1309528; Ppp1r12a.
DR   GeneTree; ENSGT00600000084108; -.
DR   HOVERGEN; HBG052561; -.
DR   OMA; ETDKTKP; -.
DR   OrthoDB; EOG4R7V9D; -.
DR   NextBio; 292815; -.
DR   PMAP-CutDB; Q9DBR7; -.
DR   ArrayExpress; Q9DBR7; -.
DR   Bgee; Q9DBR7; -.
DR   Genevestigator; Q9DBR7; -.
DR   GermOnline; ENSMUSG00000019907; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0006470; P:protein dephosphorylation; IMP:MGI.
DR   GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IMP:MGI.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR017401; Pase-1_reg_su_12A/B/C_euk.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 4.
DR   PIRSF; PIRSF038141; PP1_12ABC_vert; 1.
DR   SMART; SM00248; ANK; 6.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
PE   1: Evidence at protein level;
KW   Alternative splicing; ANK repeat; Cytoplasm; Phosphoprotein; Repeat.
FT   CHAIN         1   1029       Protein phosphatase 1 regulatory subunit
FT                                12A.
FT                                /FTId=PRO_0000067026.
FT   REPEAT       39     68       ANK 1.
FT   REPEAT       72    101       ANK 2.
FT   REPEAT      105    134       ANK 3.
FT   REPEAT      138    164       ANK 4.
FT   REPEAT      198    227       ANK 5.
FT   REPEAT      231    260       ANK 6.
FT   COMPBIAS    335    370       Glu/Ser-rich.
FT   COMPBIAS    771    794       Ser-rich.
FT   MOD_RES     299    299       Phosphoserine (By similarity).
FT   MOD_RES     422    422       Phosphoserine (By similarity).
FT   MOD_RES     443    443       Phosphothreonine.
FT   MOD_RES     445    445       Phosphoserine.
FT   MOD_RES     473    473       Phosphoserine (By similarity).
FT   MOD_RES     477    477       Phosphoserine (By similarity).
FT   MOD_RES     507    507       Phosphoserine.
FT   MOD_RES     508    508       Phosphothreonine (By similarity).
FT   MOD_RES     509    509       Phosphoserine (By similarity).
FT   MOD_RES     566    566       Phosphoserine (By similarity).
FT   MOD_RES     569    569       Phosphoserine (By similarity).
FT   MOD_RES     666    666       Phosphoserine.
FT   MOD_RES     690    690       Phosphoserine; by PKA and PKG; in vitro
FT                                (By similarity).
FT   MOD_RES     693    693       Phosphoserine; by PKA and PKG; in vitro
FT                                (By similarity).
FT   MOD_RES     694    694       Phosphothreonine; by ROCK1 and CDC42BP.
FT   MOD_RES     851    851       Phosphoserine; by ROCK1 (By similarity).
FT   MOD_RES     861    861       Phosphoserine (By similarity).
FT   MOD_RES     870    870       Phosphoserine.
FT   MOD_RES     889    889       Phosphotyrosine (By similarity).
FT   MOD_RES     900    900       Phosphotyrosine (By similarity).
FT   MOD_RES     909    909       Phosphoserine.
FT   MOD_RES     910    910       Phosphotyrosine (By similarity).
FT   VAR_SEQ     985   1029       ERRALERRISEMEEELKMLPDLKADNQRLKDENGALIRVIS
FT                                KLSK -> VAGKSQYLLGGTKSSRKKNI (in isoform
FT                                2).
FT                                /FTId=VSP_038478.
SQ   SEQUENCE   1029 AA;  114996 MW;  C466573AC1DFC81F CRC64;
     MKMADAKQKR NEQLKRWIGS ETDLEPPVVK RQKTKVKFDD GAVFLAACSS GDTDEVLKLL
     HRGADINYAN VDGLTALHQA CIDDNVDMVK FLVENGANIN QPDNEGWIPL HAAASCGYLD
     IAEFLIGQGA HVGAVNSEGD TPLDIAEEEA MEELLQNEVN RQGVDIEAAR KEEERVMLRD
     ARQWLNSGHI SDVRHAKSGG TALHVAAAKG YTEVLKLLIQ AGYDVNIKDY DGWTPLHAAA
     HWGKEEACRI LVDNLCDMET VNKVGQTAFD VADEDILGYL EELQKKQTLL HSEKRDKKSP
     LIESTANMEN NQPQKAFKNK ETLIIEPEKN ASRIESLEHE KADEEEEGKK DESSCSSEED
     EEDDSESEAE TDKTKPMASV SNAHTSSTQA APAAVTAPTL SSNQGTPTSP VKKFPISTTK
     ISPKEEERKD ESPASWRLGL RKTGSYGALA EISASKEAQK EKDTAGVMRS ASSPRLSSSL
     DNKEKEKDNK GTRLAYVTPT IPRRLASTSD IEEKENRESS SLRTSSSYTR RKWEDDLKKN
     SSINEGSTYH RSCSFGRRQD DLISCSVPST TSTPTVTSAA GLQRSLPSST STAAKTPPGS
     SSAGTQSSTS NRLWAEDSTE KEKDSAPTAV TIPVAPTVVN AAAPSTTTLT TTTAGTVSEV
     RERRRSYLTP VRDEESESQR KARSRQARQS RRSTQGVTLT DLQEAEKTIG RSRSTRTREQ
     ENEEKEKEEK EKQDKEKQEE KKESEASRED EYKQKYSRTY DETYTRYRPV STSSSSAPSS
     SSLSTLGSTL YASSQLNRPN SLVGITSAYS RGLAKENERE GEKKEEEKEG EDKSQPKSIR
     ERRRPREKRR STGVSFWTQD SDENEQERQS DTEDGSSKRE TQTDSVSRYD SSSTSSSDRY
     DSLLGRSASY SYLEDRKPYS SRLEKDDSTD FKKLYEQILA ENEKLKAQLH DTNMELTDLK
     LQLEKATQRQ ERFADRSQLE MEKRERRALE RRISEMEEEL KMLPDLKADN QRLKDENGAL
     IRVISKLSK
//
ID   TPRGL_MOUSE             Reviewed;         266 AA.
AC   Q9DBS2; B1AX99; Q8BTC6;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Tumor protein p63-regulated gene 1-like protein;
DE   AltName: Full=Mossy fiber terminal-associated vertebrate-specific presynaptic protein;
DE   AltName: Full=Protein FAM79A;
GN   Name=Tprg1l; Synonyms=Fam79a, Mover, Tprgl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH BSN.
RC   TISSUE=Brain;
RX   PubMed=17869247; DOI=10.1016/j.febslet.2007.08.070;
RA   Kremer T., Kempf C., Wittenmayer N., Nawrotzki R., Kuner T.,
RA   Kirsch J., Dresbach T.;
RT   "Mover is a novel vertebrate-specific presynaptic protein with
RT   differential distribution at subsets of CNS synapses.";
RL   FEBS Lett. 581:4727-4733(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, Embryo, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-13, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- SUBUNIT: Interacts with BSN.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle (By similarity). Note=Localized to presynaptic
CC       nerve terminals (By similarity).
CC   -!- SIMILARITY: Belongs to the TPRG1 family.
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DR   EMBL; AK004324; BAC25076.1; -; mRNA.
DR   EMBL; AK004777; BAB23555.1; -; mRNA.
DR   EMBL; AK155413; BAE33252.1; -; mRNA.
DR   EMBL; AL806525; CAM18762.1; -; Genomic_DNA.
DR   EMBL; BX465212; CAM18762.1; JOINED; Genomic_DNA.
DR   EMBL; BX465212; CAM27993.1; -; Genomic_DNA.
DR   EMBL; AL806525; CAM27993.1; JOINED; Genomic_DNA.
DR   EMBL; BC019544; AAH19544.1; -; mRNA.
DR   IPI; IPI00120085; -.
DR   RefSeq; NP_080664.1; NM_026388.2.
DR   UniGene; Mm.288737; -.
DR   ProteinModelPortal; Q9DBS2; -.
DR   IntAct; Q9DBS2; 1.
DR   MINT; MINT-217707; -.
DR   STRING; Q9DBS2; -.
DR   PhosphoSite; Q9DBS2; -.
DR   PRIDE; Q9DBS2; -.
DR   Ensembl; ENSMUST00000030896; ENSMUSP00000030896; ENSMUSG00000029030.
DR   GeneID; 67808; -.
DR   KEGG; mmu:67808; -.
DR   UCSC; uc008wbm.1; mouse.
DR   CTD; 67808; -.
DR   MGI; MGI:1915058; Tprgl.
DR   eggNOG; roNOG11177; -.
DR   GeneTree; ENSGT00390000001652; -.
DR   HOGENOM; HBG447012; -.
DR   HOVERGEN; HBG056028; -.
DR   InParanoid; Q9DBS2; -.
DR   OMA; GEFEFPP; -.
DR   OrthoDB; EOG48GW40; -.
DR   PhylomeDB; Q9DBS2; -.
DR   NextBio; 325607; -.
DR   ArrayExpress; Q9DBS2; -.
DR   Bgee; Q9DBS2; -.
DR   CleanEx; MM_TPRGL; -.
DR   Genevestigator; Q9DBS2; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR   InterPro; IPR022158; hSac2.
DR   Pfam; PF12456; hSac2; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cytoplasmic vesicle; Phosphoprotein; Synapse.
FT   CHAIN         1    266       Tumor protein p63-regulated gene 1-like
FT                                protein.
FT                                /FTId=PRO_0000269187.
FT   MOD_RES      13     13       Phosphothreonine.
FT   MOD_RES      14     14       Phosphoserine (By similarity).
FT   MOD_RES      34     34       Phosphothreonine (By similarity).
SQ   SEQUENCE   266 AA;  29814 MW;  3885516EF3995459 CRC64;
     MLQLRDTVDS AGTSPTAVLA AGEDAGAGRP GAGTPLRQTL WPLNVHDPTR RARVKEYFVF
     RPGTIEQAVE EIRAVVRPVE DGEIQGVWLL TEVDHWNNEK ERLVLVTDQS LLICKYDFIS
     LQCQQVVRVA LSAVDTISCG EFQFPPKSLN KREGFGVRIQ WDKQSRPSFI NRWNPWSTNM
     PYATFIEHPM AGMDEKTASL CHLESFKALL IQAVKKAQKE SPLPGQANTV LVLERPLLIE
     TYVGLMSFIN NEAKLGYSMT RGKIGF
//
ID   KLC4_MOUSE              Reviewed;         619 AA.
AC   Q9DBS5; Q3TCC5;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Kinesin light chain 4;
DE            Short=KLC 4;
DE   AltName: Full=Kinesin-like protein 8;
GN   Name=Klc4; Synonyms=Knsl8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; SER-566 AND
RP   SER-590, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
CC   -!- FUNCTION: Kinesin is a microtubule-associated force-producing
CC       protein that may play a role in organelle transport. The light
CC       chain may function in coupling of cargo to the heavy chain or in
CC       the modulation of its ATPase activity (By similarity).
CC   -!- SUBUNIT: Oligomeric complex composed of two heavy chains and two
CC       light chains (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (Probable).
CC   -!- SIMILARITY: Belongs to the kinesin light chain family.
CC   -!- SIMILARITY: Contains 7 TPR repeats.
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DR   EMBL; AK004774; BAB23552.1; -; mRNA.
DR   EMBL; AK170793; BAE42032.1; -; mRNA.
DR   IPI; IPI00120089; -.
DR   RefSeq; NP_083367.1; NM_029091.2.
DR   UniGene; Mm.279599; -.
DR   ProteinModelPortal; Q9DBS5; -.
DR   SMR; Q9DBS5; 94-602.
DR   DIP; DIP-48704N; -.
DR   PhosphoSite; Q9DBS5; -.
DR   PRIDE; Q9DBS5; -.
DR   Ensembl; ENSMUST00000003642; ENSMUSP00000003642; ENSMUSG00000003546.
DR   GeneID; 74764; -.
DR   KEGG; mmu:74764; -.
DR   UCSC; uc008ctj.1; mouse.
DR   CTD; 74764; -.
DR   MGI; MGI:1922014; Klc4.
DR   eggNOG; roNOG10405; -.
DR   GeneTree; ENSGT00390000006393; -.
DR   HOGENOM; HBG447230; -.
DR   HOVERGEN; HBG006217; -.
DR   InParanoid; Q9DBS5; -.
DR   OMA; MSKSRHR; -.
DR   OrthoDB; EOG4NZTT0; -.
DR   PhylomeDB; Q9DBS5; -.
DR   NextBio; 341588; -.
DR   ArrayExpress; Q9DBS5; -.
DR   Bgee; Q9DBS5; -.
DR   CleanEx; MM_KLC4; -.
DR   Genevestigator; Q9DBS5; -.
DR   GermOnline; ENSMUSG00000003546; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005871; C:kinesin complex; IEA:InterPro.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   InterPro; IPR002151; Kinesin_light.
DR   InterPro; IPR015792; Kinesin_light_repeat.
DR   InterPro; IPR015390; Rabaptin_Rab5-bd.
DR   InterPro; IPR001440; TPR-1.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 2.
DR   Pfam; PF09311; Rab5-bind; 1.
DR   Pfam; PF00515; TPR_1; 3.
DR   PRINTS; PR00381; KINESINLIGHT.
DR   SMART; SM00028; TPR; 5.
DR   PROSITE; PS01160; KINESIN_LIGHT; 3.
DR   PROSITE; PS50005; TPR; 6.
DR   PROSITE; PS50293; TPR_REGION; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW   Motor protein; Phosphoprotein; Repeat; TPR repeat.
FT   CHAIN         1    619       Kinesin light chain 4.
FT                                /FTId=PRO_0000215098.
FT   REPEAT       55     88       TPR 1.
FT   REPEAT      211    244       TPR 2.
FT   REPEAT      253    286       TPR 3.
FT   REPEAT      295    328       TPR 4.
FT   REPEAT      337    370       TPR 5.
FT   REPEAT      379    412       TPR 6.
FT   REPEAT      464    497       TPR 7.
FT   COILED       65    155       Potential.
FT   MOD_RES      74     74       Phosphoserine (By similarity).
FT   MOD_RES      83     83       Phosphoserine (By similarity).
FT   MOD_RES      93     93       Phosphoserine (By similarity).
FT   MOD_RES     100    100       Phosphoserine (By similarity).
FT   MOD_RES     174    174       Phosphoserine.
FT   MOD_RES     391    391       N6-acetyllysine (By similarity).
FT   MOD_RES     460    460       Phosphoserine (By similarity).
FT   MOD_RES     566    566       Phosphoserine.
FT   MOD_RES     590    590       Phosphoserine.
FT   MOD_RES     593    593       Phosphotyrosine (By similarity).
FT   MOD_RES     612    612       Phosphothreonine (By similarity).
SQ   SEQUENCE   619 AA;  68613 MW;  BE2D6B3CD451A7BF CRC64;
     MSGLVLGQRD EPAGHRLSQE EILGSTKVVS QGLEALHSEH QAVLQSLSHT IECLQQGGHE
     EGLVHEKARQ LRRSMENIEL GLSEAQVMLA LASHLSTVES EKQKLRAQVR RLCQENQWLR
     DELAGTQQRL QRSEQAVAQL EEEKKHLEFL RQLRQYDEDG HGMEEKEGEA TKDSLDDLFP
     NEEEEDSGND LSRGQGAAAA QQGGYEIPAR LRTLHNLVIQ YAAQGRYEVA VPLCKQALED
     LERTSGRGHP DVATMLNILA LVYRDQNKYK EAAHLLNDAL SIRESTLGRD HPAVAATLNN
     LAVLYGKRGK YKEAEPLCQR ALEIREKVLG TDHPDVAKQL NNLALLCQNQ GKYEAVERYY
     QRALAIYESQ LGPDNPNVAR TKNNLASCYL KQGKYSEAEA LYKEILTCAH VQEFGSVDDD
     HKPIWMHAEE REEMSRSRPR DSSAPYAEYG GWYKACRVSS PTVNTTLKNL GALYRRQGKL
     EAAETLEECA LRSRKQGTDP ISQTKVAELL GEGDGRKAIQ EGPGDSVKFE GGEDASVAVE
     WSGDGSGTLQ RSGSLGKIRD VLRRSSELLV RKLQGTEPRP SSSSMKRAAS LNYLNQPNAA
     PLQVSRGLSA STVDLSSSS
//
ID   AMPD2_MOUSE             Reviewed;         798 AA.
AC   Q9DBT5; A2AE28; Q91YI2;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=AMP deaminase 2;
DE            EC=3.5.4.6;
DE   AltName: Full=AMP deaminase isoform L;
GN   Name=Ampd2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-64, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-111, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: AMP deaminase plays a critical role in energy metabolism
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: AMP + H(2)O = IMP + NH(3).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway;
CC       IMP from AMP: step 1/1.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the adenosine and AMP deaminases family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH16662.2; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AK004759; BAB23540.1; -; mRNA.
DR   EMBL; AK169980; BAE41495.1; -; mRNA.
DR   EMBL; AL671854; CAM27248.1; -; Genomic_DNA.
DR   EMBL; BC016662; AAH16662.2; ALT_INIT; mRNA.
DR   EMBL; BC049119; AAH49119.1; -; mRNA.
DR   IPI; IPI00406639; -.
DR   RefSeq; NP_083055.1; NM_028779.4.
DR   UniGene; Mm.274335; -.
DR   ProteinModelPortal; Q9DBT5; -.
DR   SMR; Q9DBT5; 137-784.
DR   STRING; Q9DBT5; -.
DR   PhosphoSite; Q9DBT5; -.
DR   PRIDE; Q9DBT5; -.
DR   Ensembl; ENSMUST00000102637; ENSMUSP00000099697; ENSMUSG00000027889.
DR   Ensembl; ENSMUST00000102638; ENSMUSP00000099698; ENSMUSG00000027889.
DR   GeneID; 109674; -.
DR   KEGG; mmu:109674; -.
DR   UCSC; uc008qxz.1; mouse.
DR   CTD; 109674; -.
DR   MGI; MGI:88016; Ampd2.
DR   GeneTree; ENSGT00390000008190; -.
DR   HOGENOM; HBG713563; -.
DR   HOVERGEN; HBG050494; -.
DR   InParanoid; Q9DBT5; -.
DR   OrthoDB; EOG41JZBP; -.
DR   PhylomeDB; Q9DBT5; -.
DR   BRENDA; 3.5.4.6; 244.
DR   NextBio; 362553; -.
DR   ArrayExpress; Q9DBT5; -.
DR   Bgee; Q9DBT5; -.
DR   CleanEx; MM_AMPD2; -.
DR   Genevestigator; Q9DBT5; -.
DR   GermOnline; ENSMUSG00000027889; Mus musculus.
DR   GO; GO:0003876; F:AMP deaminase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006144; P:purine base metabolic process; IEA:InterPro.
DR   GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; IEA:InterPro.
DR   InterPro; IPR006650; A/AMP_deam_AS.
DR   InterPro; IPR001365; A/AMP_deaminase.
DR   InterPro; IPR006329; AMP_deaminase.
DR   InterPro; IPR016297; AMP_deaminase_met.
DR   Pfam; PF00962; A_deaminase; 1.
DR   PIRSF; PIRSF001251; AMP_deaminase_met; 1.
DR   TIGRFAMs; TIGR01429; AMP_deaminase; 1.
DR   PROSITE; PS00485; A_DEAMINASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Hydrolase; Metal-binding; Nucleotide metabolism;
KW   Phosphoprotein; Zinc.
FT   CHAIN         1    798       AMP deaminase 2.
FT                                /FTId=PRO_0000194408.
FT   REGION      409    414       Substrate binding (By similarity).
FT   REGION      685    688       Substrate binding (By similarity).
FT   ACT_SITE    629    629       Proton acceptor (By similarity).
FT   METAL       338    338       Zinc; catalytic (By similarity).
FT   METAL       340    340       Zinc; catalytic (By similarity).
FT   METAL       607    607       Zinc; catalytic (By similarity).
FT   METAL       684    684       Zinc; catalytic (By similarity).
FT   BINDING     340    340       Substrate (By similarity).
FT   BINDING     610    610       Substrate (By similarity).
FT   MOD_RES      19     19       Phosphoserine (By similarity).
FT   MOD_RES      37     37       Phosphoserine (By similarity).
FT   MOD_RES      64     64       Phosphotyrosine.
FT   MOD_RES      70     70       Phosphoserine (By similarity).
FT   MOD_RES      87     87       Phosphoserine.
FT   MOD_RES     109    109       Phosphoserine (By similarity).
FT   MOD_RES     111    111       Phosphoserine.
FT   MOD_RES     414    414       Phosphotyrosine (By similarity).
FT   MOD_RES     420    420       Phosphoserine (By similarity).
FT   MOD_RES     436    436       N6-acetyllysine (By similarity).
SQ   SEQUENCE   798 AA;  92024 MW;  2BC4F37E4006C7D5 CRC64;
     MASEARSGLG ASPLQSARSL PGNAPCLKHF PLDLRTSMDG KCKEIAEELF SRSLAESELR
     SAPYEFPEES PIEQLEERRQ RLERQISQDV KLEPDILLRA KQDFLKTDSD SDLQLYKEQG
     EGQGDRGLWE RDVVLEREFQ RVIISGEEKC GVPFTDLLDA AKSVVRALFI REKYMALSLQ
     SFCPTTRRYL QQLAEKPLET RTYEQSPDTP VSADAPVHPP ALEQHPYEHC EPSAMPGDLG
     LGLRMVRGVV HVYTRRDPDE HCPEVELPYP DLQEFVADVN VLMALIINGP IKSFCYRRLQ
     YLSSKFQMHV LLNEMKELAA QKKVPHRDFY NIRKVDTHIH ASSCMNQKHL LRFIKRAMKR
     HLEEIVHVEQ GREQTLREVF ESMNLTAYDL SVDTLDVHAD RNTFHRFDKF NAKYNPIGES
     VLREIFIKTD NKISGKYFAH IIKEVMADLE ESKYQNAELR LSIYGRSRDE WDKLARWAVN
     HKVHSPNVRW LVQVPRLFDV YRTKGQLANF QEMLENIFLP LFEATVHPAS HPELHLFLEH
     VDGFDSVDDE SKPENHVFNL ESPLPEAWVE EDNPPYAYYL YYTFANMAML NHLRRQRGFH
     TFVLRPHCGE AGPIHHLVSA FMLAENISHG LLLRKAPVLQ YLYYLAQIGI AMSPLSNNSL
     FLSYHRNPLP EYLSRGLMVS LSTDDPLQFH FTKEPLMEEY SIATQVWKLS SCDMCELARN
     SVLMSGFSHK VKSHWLGPNY TKEGPEGNDI RRTNVPDIRV GYRYETLCQE LALITQAVQS
     EMLETIPEEV GIVMSPGP
//
ID   RGC32_MOUSE             Reviewed;         137 AA.
AC   Q9DBX1; Q9D0U0;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Response gene to complement 32 protein;
DE            Short=RGC-32;
GN   Name=Rgc32;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=21634895; PubMed=11687586; DOI=10.1074/jbc.M109354200;
RA   Badea T., Niculescu F., Soane L., Fosbrink M., Sorana H., Rus V.,
RA   Shin M.L., Rus H.;
RT   "RGC-32 increases p34CDC2 kinase activity and entry of aortic smooth
RT   muscle cells into S-phase.";
RL   J. Biol. Chem. 277:502-508(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E.,
RA   Mollenhauer J., Wiemann S., Schick M., Korn B.;
RT   "Cloning of mouse full open reading frames in Gateway(R) system entry
RT   vector (pDONR201).";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Modulates the activity of cell cycle-specific kinases.
CC       Enhances CDK1 activity. May contribute to the regulation of the
CC       cell cycle (By similarity).
CC   -!- SUBUNIT: Interacts with CDK1 and PLK1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Cytoplasm, cytoskeleton, centrosome (By similarity).
CC       Note=Cytoplasmic in unstimulated cells. Nuclear after activation
CC       by complement. Associated with the centrosome during prometaphase
CC       and metaphase (By similarity).
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DR   EMBL; AF276981; AAK69442.1; -; mRNA.
DR   EMBL; AK004451; BAB23310.1; -; mRNA.
DR   EMBL; AK004705; BAB23490.1; -; mRNA.
DR   EMBL; CT010403; CAJ18609.1; -; mRNA.
DR   EMBL; BC049580; AAH49580.1; -; mRNA.
DR   EMBL; BC050935; AAH50935.1; -; mRNA.
DR   IPI; IPI00321859; -.
DR   RefSeq; NP_079703.2; NM_025427.2.
DR   UniGene; Mm.29811; -.
DR   STRING; Q9DBX1; -.
DR   PhosphoSite; Q9DBX1; -.
DR   PRIDE; Q9DBX1; -.
DR   Ensembl; ENSMUST00000022595; ENSMUSP00000022595; ENSMUSG00000022018.
DR   GeneID; 66214; -.
DR   KEGG; mmu:66214; -.
DR   UCSC; uc007ust.1; mouse.
DR   MGI; MGI:1913464; 1190002H23Rik.
DR   eggNOG; roNOG17100; -.
DR   GeneTree; ENSGT00390000011709; -.
DR   HOGENOM; HBG447054; -.
DR   HOVERGEN; HBG060999; -.
DR   InParanoid; Q9DBX1; -.
DR   OrthoDB; EOG4NKBX7; -.
DR   PhylomeDB; Q9DBX1; -.
DR   NextBio; 320993; -.
DR   ArrayExpress; Q9DBX1; -.
DR   Bgee; Q9DBX1; -.
DR   CleanEx; MM_1190002H23RIK; -.
DR   Genevestigator; Q9DBX1; -.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Cell cycle; Cytoplasm; Cytoskeleton; Nucleus; Phosphoprotein.
FT   CHAIN         1    137       Response gene to complement 32 protein.
FT                                /FTId=PRO_0000274702.
FT   COMPBIAS     11     26       Ala-rich.
FT   COMPBIAS     64    108       Ser/Thr-rich.
FT   MOD_RES       9      9       Phosphoserine (By similarity).
FT   MOD_RES      44     44       Phosphoserine (By similarity).
FT   MOD_RES      69     69       Phosphoserine (By similarity).
FT   MOD_RES      71     71       Phosphoserine (By similarity).
FT   MOD_RES      75     75       Phosphoserine (By similarity).
FT   MOD_RES      97     97       Phosphoserine (By similarity).
FT   MOD_RES     111    111       Phosphothreonine; by CDK1 (By
FT                                similarity).
FT   CONFLICT     68     68       V -> I (in Ref. 2; BAB23310).
FT   CONFLICT     70     70       D -> N (in Ref. 2; BAB23310).
SQ   SEQUENCE   137 AA;  14717 MW;  01646F247F8B284A CRC64;
     MKPPSAQSSP AAVAAAAPAM DSAAAADLTD VLCEFDAVLA DFASPFHERH FHYEEHLERM
     KRRSSASVSD SSGFSDSESA DSVYRDSFTF SDEKLNSPTN SSPALLPSAV TPRKAKLGDT
     KELEDFIADL DRTLASM
//
ID   FOXP4_MOUSE             Reviewed;         795 AA.
AC   Q9DBY0; Q80V92; Q8CG10; Q8CIS1;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-FEB-2011, entry version 74.
DE   RecName: Full=Forkhead box protein P4;
DE   AltName: Full=Fork head-related protein-like A;
DE            Short=mFKHLA;
GN   Name=Foxp4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=C57BL/6; TISSUE=Lung;
RX   MEDLINE=22879833; PubMed=14516685; DOI=10.1016/S0925-4773(03)00116-3;
RA   Lu M.M., Li S., Yang H., Morrisey E.E.;
RT   "Foxp4: a novel member of the Foxp subfamily of winged-helix genes co-
RT   expressed with Foxp1 and Foxp2 in pulmonary and gut tissues.";
RL   Mech. Dev. 119:S197-S202(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Daigo Y., Takayama I., Fujino M.A.;
RT   "Isolation and characterization of novel human and mouse genes, which
RT   are expressed in the digestive tract.";
RL   Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=12818433; DOI=10.1016/S0167-4781(03)00074-5;
RA   Teufel A., Wong E.A., Mukhopadhyay M., Malik N., Westphal H.;
RT   "FoxP4, a novel forkhead transcription factor.";
RL   Biochim. Biophys. Acta 1627:147-152(2003).
RN   [6]
RP   FUNCTION, DIMERIZATION, DOMAIN, AND MUTAGENESIS OF GLU-366.
RX   PubMed=14701752; DOI=10.1128/MCB.24.2.809-822.2004;
RA   Li S., Weidenfeld J., Morrisey E.E.;
RT   "Transcriptional and DNA binding activity of the Foxp1/2/4 family is
RT   modulated by heterotypic and homotypic protein interactions.";
RL   Mol. Cell. Biol. 24:809-822(2004).
CC   -!- FUNCTION: Transcriptional repressor that represses lung-specific
CC       expression.
CC   -!- SUBUNIT: Forms homodimers and heterodimers with FOXP1 and FOXP2.
CC       Dimerization is required for DNA-binding.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9DBY0-1; Sequence=Displayed;
CC         Note=No experimental confirmation available;
CC       Name=2;
CC         IsoId=Q9DBY0-2; Sequence=VSP_052130, VSP_052131;
CC       Name=3;
CC         IsoId=Q9DBY0-3; Sequence=VSP_052129, VSP_052130, VSP_052131;
CC   -!- TISSUE SPECIFICITY: Expressed in the adult heart, brain, spleen
CC       lung, liver, kidney and testes.
CC   -!- DEVELOPMENTAL STAGE: Expressed predominantly in the lung and brain
CC       during embryogenesis. Expressed in the lung epithelium and the
CC       mesenchyme immediately adjacent to the epithelium from 10.5 dpc.
CC       At 9.5 dpc, expressed in the foregut endoderm but not in the
CC       heart. At 16.5 and 18.5 dpc, expressed in both the proximal and
CC       distal airway epithelium. Also expressed in the developing gut. In
CC       the hindgut, primarily expressed in epithelial cells of the
CC       intestine and stomach. Expressed in the brain in a dynamic
CC       pattern. At 14.5 dpc, expressed at high levels in the intermediate
CC       zone of the neopallial cortex with lower levels in the surrounding
CC       cells. By 16.5 dpc, no longer expressed in the intermediate zone,
CC       but still present in the surrounding cells of the neopallial
CC       cortex.
CC   -!- DOMAIN: The leucine-zipper is required for dimerization and
CC       transcriptional repression.
CC   -!- SIMILARITY: Contains 1 C2H2-type zinc finger.
CC   -!- SIMILARITY: Contains 1 fork-head DNA-binding domain.
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CC   -----------------------------------------------------------------------
DR   EMBL; AY135029; AAN08624.1; -; mRNA.
DR   EMBL; AB052766; BAC53799.1; -; mRNA.
DR   EMBL; AK004693; BAB23479.1; -; mRNA.
DR   EMBL; BC043702; AAH43702.1; -; mRNA.
DR   EMBL; BC052407; AAH52407.1; -; mRNA.
DR   EMBL; BC057110; AAH57110.1; -; mRNA.
DR   IPI; IPI00762582; -.
DR   IPI; IPI00775924; -.
DR   IPI; IPI00775986; -.
DR   RefSeq; NP_001104294.1; NM_001110824.1.
DR   RefSeq; NP_001104295.1; NM_001110825.1.
DR   RefSeq; NP_083043.2; NM_028767.2.
DR   UniGene; Mm.240062; -.
DR   ProteinModelPortal; Q9DBY0; -.
DR   SMR; Q9DBY0; 458-539.
DR   STRING; Q9DBY0; -.
DR   PhosphoSite; Q9DBY0; -.
DR   PRIDE; Q9DBY0; -.
DR   Ensembl; ENSMUST00000024790; ENSMUSP00000024790; ENSMUSG00000023991.
DR   GeneID; 74123; -.
DR   KEGG; mmu:74123; -.
DR   UCSC; uc008cwl.1; mouse.
DR   UCSC; uc008cwm.1; mouse.
DR   UCSC; uc008cwn.1; mouse.
DR   CTD; 74123; -.
DR   MGI; MGI:1921373; Foxp4.
DR   eggNOG; roNOG15084; -.
DR   GeneTree; ENSGT00560000076806; -.
DR   HOGENOM; HBG402802; -.
DR   HOVERGEN; HBG051657; -.
DR   InParanoid; Q9DBY0; -.
DR   OMA; SLHGGGP; -.
DR   NextBio; 339838; -.
DR   ArrayExpress; Q9DBY0; -.
DR   Bgee; Q9DBY0; -.
DR   CleanEx; MM_FOXP4; -.
DR   Genevestigator; Q9DBY0; -.
DR   GermOnline; ENSMUSG00000023991; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IC:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0016564; F:transcription repressor activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0048617; P:embryonic foregut morphogenesis; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   InterPro; IPR001766; TF_fork_head.
DR   InterPro; IPR018122; TF_fork_head_CS.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   PANTHER; PTHR11829; Fork_box_protein; 1.
DR   Pfam; PF00250; Fork_head; 1.
DR   PRINTS; PR00053; FORKHEAD.
DR   SMART; SM00339; FH; 1.
DR   SMART; SM00355; ZnF_C2H2; 1.
DR   PROSITE; PS00657; FORK_HEAD_1; FALSE_NEG.
DR   PROSITE; PS00658; FORK_HEAD_2; 1.
DR   PROSITE; PS50039; FORK_HEAD_3; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW   Phosphoprotein; Repressor; Transcription; Transcription regulation;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    795       Forkhead box protein P4.
FT                                /FTId=PRO_0000247653.
FT   DOMAIN      354    375       Leucine-zipper.
FT   ZN_FING     312    337       C2H2-type.
FT   DNA_BIND    459    549       Fork-head.
FT   COMPBIAS     71    225       Gln-rich.
FT   COMPBIAS    603    724       Pro-rich.
FT   MOD_RES     365    365       Phosphoserine (By similarity).
FT   VAR_SEQ     388    388       P -> PLNPVPGSSSFSK (in isoform 3).
FT                                /FTId=VSP_052129.
FT   VAR_SEQ     672    672       P -> S (in isoform 2 and isoform 3).
FT                                /FTId=VSP_052130.
FT   VAR_SEQ     673    795       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_052131.
FT   MUTAGEN     366    366       Missing: Loss of dimerization. Almost
FT                                complete loss of DNA-binding. Reduced
FT                                transcriptional repression activity.
FT   CONFLICT    226    226       A -> AA (in Ref. 2; AAN08624 and 4;
FT                                AAH43702/AAH52407).
SQ   SEQUENCE   795 AA;  85981 MW;  860AE60AAD3742CE CRC64;
     MMVESASETI RSAPSGQNGV GSLSAQADGG GGAGTAGTAP AAGRDASGRE AASGGADSNG
     EMSPAELLHF QQQQALQVAR QFLLQQASSL NSPGNNDSKQ SASAVQVPVS VAMMSQQMLT
     PQQMQQILSP PQLQALLQQQ QALMLQQLQE YYKKQQEQLH LQLLTQQQAG KQQPKEALGN
     KQLAFQQQLL QMQQLQQQHL LNLQRQGLVS LQPSQASGPL QALPQAVCPT DLPQLWKGEG
     APGQPAEDSG RQEGLDLAST AVTATSFASP PKVSPPLSHH PLPNGQPTVL TSRRDSSSHE
     ETPSSHPLYG HGECKWPGCE TLCEDLGQFI KHLNTEHALD DRSTAQCRVQ MQVVQQLEIQ
     LAKESERLQA MMAHLHMRPS EPKPFSQPVT VSADPFPDGL VHPPTSAAAP VTPLRPPGLG
     SASLHSGGPA RRRSNDKFCS PISSELAQNH EFYKNADVRP PFTYASLIRQ AILETPDRQL
     TLNEIYNWFT RMFAYFRRNT ATWKNAVRHN LSLHKCFVRV ENVKGAVWTV DEREYQKRRP
     PKMTGSPTLV KNMISGLSYG ALNASYQAAL AESSFPLLSN PGMLNPGSAS SLLPLSQEDL
     GVPGEPLPSN GSSSPPRLSP PQYSHQIQVK EEPAEAEEDR RPGPPLGAPN PSTVGPPEDR
     DLEEDLGGED MPSQPCPLIP GWKPSLLHLS YCVKPKFTVS VGSKTPSSPL PPPPRVQGSY
     SLPPCSYLAY GDMRGQNPAP SPGLLSGVGG GLFRCLHRTK SPSLPGVWIL AAELETMRFH
     RPPMGDPQPK TADWV
//
ID   TRIL_MOUSE              Reviewed;         809 AA.
AC   Q9DBY4; Q80TV0; Q8BKM5;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=TLR4 interactor with leucine rich repeats;
DE   AltName: Full=Leucine-rich repeat-containing protein KIAA0644;
DE   Flags: Precursor;
GN   Name=Tril; Synonyms=Kiaa0644;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Lung, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INDUCTION BY LPS, AND TISSUE SPECIFICITY.
RX   PubMed=19710467; DOI=10.4049/jimmunol.0901518;
RA   Carpenter S., Carlson T., Dellacasagrande J., Garcia A., Gibbons S.,
RA   Hertzog P., Lyons A., Lin L.L., Lynch M., Monie T., Murphy C.,
RA   Seidl K.J., Wells C., Dunne A., O'Neill L.A.;
RT   "TRIL, a functional component of the TLR4 signaling complex, highly
RT   expressed in brain.";
RL   J. Immunol. 183:3989-3995(2009).
CC   -!- FUNCTION: Component of the TLR4 signaling complex. Mediate the
CC       innate immune response to bacterial lipopolysaccharide (LPS)
CC       leading to cytokine secretion (By similarity).
CC   -!- SUBUNIT: Belongs to the lipopolysaccharide (LPS) receptor, a
CC       multi-protein complex containing at least CD14, MD-2 and TLR4.
CC       Interacts with TLR4; this interaction is greatly enhanced by LPS
CC       stimulation (By similarity). Interacts with LPS (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- TISSUE SPECIFICITY: Higly expressed in brain, spinal cord and
CC       lung.
CC   -!- INDUCTION: By bacterial lipopolysaccharides (LPS) (in vivo and in
CC       vitro).
CC   -!- PTM: N-glycolysaled (By similarity).
CC   -!- SIMILARITY: Contains 13 LRR (leucine-rich) repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65620.1; Type=Frameshift; Positions=621;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK122338; BAC65620.1; ALT_FRAME; mRNA.
DR   EMBL; AK004681; BAB23469.1; -; mRNA.
DR   EMBL; AK033401; BAC28270.1; -; mRNA.
DR   EMBL; AK051421; BAC34634.1; -; mRNA.
DR   EMBL; BC043099; AAH43099.1; -; mRNA.
DR   EMBL; BC059224; AAH59224.1; -; mRNA.
DR   IPI; IPI00469248; -.
DR   RefSeq; NP_080093.1; NM_025817.4.
DR   UniGene; Mm.422727; -.
DR   UniGene; Mm.475802; -.
DR   HSSP; Q9BZR6; 1OZN.
DR   ProteinModelPortal; Q9DBY4; -.
DR   SMR; Q9DBY4; 27-412, 586-684.
DR   PRIDE; Q9DBY4; -.
DR   Ensembl; ENSMUST00000127748; ENSMUSP00000116056; ENSMUSG00000043496.
DR   GeneID; 66873; -.
DR   KEGG; mmu:66873; -.
DR   CTD; 66873; -.
DR   MGI; MGI:1914123; 1200009O22Rik.
DR   GeneTree; ENSGT00600000084136; -.
DR   HOVERGEN; HBG066060; -.
DR   OrthoDB; EOG4KWJSW; -.
DR   NextBio; 322893; -.
DR   Bgee; Q9DBY4; -.
DR   Genevestigator; Q9DBY4; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR000372; LRR-contain_N.
DR   Pfam; PF00560; LRR_1; 3.
DR   Pfam; PF01463; LRRCT; 1.
DR   SMART; SM00369; LRR_TYP; 6.
DR   SMART; SM00082; LRRCT; 1.
DR   SMART; SM00013; LRRNT; 1.
DR   PROSITE; PS51450; LRR; 13.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Immunity; Inflammatory response; Innate immunity;
KW   Leucine-rich repeat; Membrane; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     25       Potential.
FT   CHAIN        26    809       TLR4 interactor with leucine rich
FT                                repeats.
FT                                /FTId=PRO_0000349256.
FT   TOPO_DOM     26    694       Extracellular (Potential).
FT   TRANSMEM    695    715       Helical; (Potential).
FT   TOPO_DOM    716    809       Cytoplasmic (Potential).
FT   REPEAT       61     81       LRR 1.
FT   REPEAT       82    105       LRR 2.
FT   REPEAT      107    129       LRR 3.
FT   REPEAT      130    153       LRR 4.
FT   REPEAT      154    177       LRR 5.
FT   REPEAT      179    201       LRR 6.
FT   REPEAT      203    227       LRR 7.
FT   REPEAT      228    251       LRR 8.
FT   REPEAT      252    275       LRR 9.
FT   REPEAT      277    299       LRR 10.
FT   REPEAT      300    323       LRR 11.
FT   REPEAT      325    347       LRR 12.
FT   REPEAT      349    375       LRR 13.
FT   CARBOHYD     73     73       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    411    411       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    587    587       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   809 AA;  88810 MW;  5E86F55B8AE419FA CRC64;
     MEGVGAVRFW LVVCGCLAFP PRAESVCPER CDCQHPQHLL CTNRGLRAVP KTSSLPSPQD
     VLTYSLGGNF ITNITAFDFH RLGQLRRLDL QYNQIRSLHP KTFEKLSRLE ELYLGNNLLQ
     ALVPGTLAPL RKLRILYANG NEIGRLSRGS FEGLESLVKL RLDGNVLGAL PDAVFAPLGN
     LLYLHLESNR IRFLGKNAFS QLGKLRFLNL SANELQPSLR HAATFVPLRS LSTLILSANS
     LQHLGPRVFQ HLPRLGLLSL SGNQLTHLAP EAFWGLEALR ELRLEGNRLN QLPLTLLEPL
     HSLEALDLSG NELSALHPAT FGHQGRLREL SLRDNALSAL SGDIFAASPA LYRLDLDGNG
     WTCDCRLRGL KRWMGNWHSQ GRLLTVFVQC RHPPALRGKY LDYLDDQLLQ NGSCVDPSPS
     PTAGSRQWPL PTSSEEGMTP PAGLSQELPL QPQPQPQQRG RLLPGVAWGG AAKELVGNRS
     ALRLSRRGPG PHQGPSAAAP GSAPQSLDLH EKPGRGRHTR ANLSQTEPTP TSEPASGTPS
     ARDSWQRAAK QRLASEQQES AVQSVSGVGL PPLVSDPCDF NKFILCNLTV EAVSANSASV
     RWAVREHRSP RPQGGARFRL LFDRFGQQPK FQRFVYLPER SDSATLHELR GDTPYLVCVE
     GVLGGRVCPV APRDHCAGLV TLPEAGGRGG VDYQLLTLVL LAVNALLVLL ALAAWGSRWL
     RRKLRARRKG GAPVHVRHMY STRRPLRSMG TGVSADFSGF QSHRPRTTVC ALSEADLIEF
     PCDRFMDSTG GGTSGSLRRE DHLLQRFAD
//
ID   NVL_MOUSE               Reviewed;         855 AA.
AC   Q9DBY8; Q3USC4; Q8BW27; Q8K2B5;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Nuclear valosin-containing protein-like;
DE            Short=NVLp;
DE            Short=Nuclear VCP-like protein;
GN   Name=Nvl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Lung, and Ovary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity).
CC   -!- PTM: Phosphorylated (By similarity).
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK004676; BAB23464.1; -; mRNA.
DR   EMBL; AK054502; BAC35806.1; -; mRNA.
DR   EMBL; AK140509; BAE24409.1; -; mRNA.
DR   EMBL; BC031847; AAH31847.1; -; mRNA.
DR   IPI; IPI00321884; -.
DR   RefSeq; NP_080447.1; NM_026171.1.
DR   UniGene; Mm.263464; -.
DR   ProteinModelPortal; Q9DBY8; -.
DR   SMR; Q9DBY8; 256-854.
DR   PhosphoSite; Q9DBY8; -.
DR   PRIDE; Q9DBY8; -.
DR   Ensembl; ENSMUST00000027797; ENSMUSP00000027797; ENSMUSG00000026516.
DR   GeneID; 67459; -.
DR   KEGG; mmu:67459; -.
DR   UCSC; uc007dxb.1; mouse.
DR   CTD; 67459; -.
DR   MGI; MGI:1914709; Nvl.
DR   eggNOG; roNOG05451; -.
DR   GeneTree; ENSGT00570000079239; -.
DR   HOGENOM; HBG597299; -.
DR   HOVERGEN; HBG001226; -.
DR   InParanoid; Q9DBY8; -.
DR   OMA; LRCDCYT; -.
DR   OrthoDB; EOG4ZPDTN; -.
DR   PhylomeDB; Q9DBY8; -.
DR   NextBio; 324638; -.
DR   ArrayExpress; Q9DBY8; -.
DR   Bgee; Q9DBY8; -.
DR   CleanEx; MM_NVL; -.
DR   Genevestigator; Q9DBY8; -.
DR   GermOnline; ENSMUSG00000026516; Mus musculus.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   Pfam; PF00004; AAA; 2.
DR   SMART; SM00382; AAA; 2.
DR   PROSITE; PS00674; AAA; 2.
PE   2: Evidence at transcript level;
KW   ATP-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Repeat.
FT   CHAIN         1    855       Nuclear valosin-containing protein-like.
FT                                /FTId=PRO_0000084589.
FT   NP_BIND     304    311       ATP (Potential).
FT   NP_BIND     621    628       ATP (Potential).
FT   MOD_RES     133    133       Phosphoserine (By similarity).
FT   MOD_RES     137    137       Phosphothreonine (By similarity).
FT   MOD_RES     158    158       Phosphoserine (By similarity).
FT   MOD_RES     184    184       Phosphoserine (By similarity).
FT   MOD_RES     190    190       Phosphoserine (By similarity).
FT   MOD_RES     210    210       Phosphoserine (By similarity).
FT   CONFLICT    513    513       E -> K (in Ref. 2; AAH31847).
SQ   SEQUENCE   855 AA;  94476 MW;  F69A173AB40E0AE9 CRC64;
     MKPRPGVFVD RKLKQRVIQY LSSNRCGKYV DTGILASDLQ RLYSVDYGRR KRNAFRIQVE
     KVFSIISSEK ELKNLKELED GHLAKRARQD EEDEYTESYS DDDSNMEDYP DPQSANPMNS
     SLLSLYRRGN SESVSTTPKW GQREATTSTP LLTSKTGSVP LKTPARESEG GWFIDKTPGG
     KKESLPLDLS DDQSNSKKQD SEIQILKDSS LLESDKKRKG RAKGKGNKRK TENLQEVDGE
     IEALLQKKAK ARSTELQISN VKFEDVGGND ATLKEVCKML IHMRHPEVYQ HLGVVPPRGV
     LLHGPPGCGK TLLAHAIAGE LDLPILKVAA PEIVSGVSGE SEQKLRELFD QAVSNAPCIV
     FIDEIDAITP KREVASKDME RRIVAQLLTC MDDLNNVAAT ARVLVIGATN RPDSLDPALR
     RAGRFDREVC LGIPDEAARE RILQTLCRKL RLPETFNFCH LAHLTPGFVG ADLMALCREA
     AMCAVNRVLM KQQAQQKKKP EIEGLPSEGD QEERLGAEPT SETQDELQRL LGLLRDQDPL
     SEEQMQGLCI ELNDFIVALA EVQPSAKREG FVTVPNVTWA DIGALEDIRD ELIMAILAPV
     RNPDQFRTLG LGTPAGILLA GPPGCGKTLL AKAVANESGL NFISVKGPEL LNMYVGESER
     AVRQVFQRAK NSAPCVIFFD EVDALCPRRS DRETGASVRV VNQLLTEMDG LETRQQVFIL
     AATNRPDIID PAILRPGRLD KTLFVGLPPP ADRVAILKTI TKNGTKPPLD EDVNLETIAN
     DLRCNCYTGA DLTALVREAS LCALRQEITA QKNGVGAGEL KVSHKHFEDA FKKVKPSISI
     KDQVMYEALQ RSLSQ
//
ID   SYDE1_MOUSE             Reviewed;         737 AA.
AC   Q9DBZ9;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Rho GTPase-activating protein SYDE1;
DE   AltName: Full=Synapse defective protein 1 homolog 1;
DE            Short=Protein syd-1 homolog 1;
GN   Name=Syde1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: GTPase activator for the Rho-type GTPases by converting
CC       them to an inactive GDP-bound state (By similarity).
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK004654; BAB23445.1; -; mRNA.
DR   IPI; IPI00321899; -.
DR   UniGene; Mm.86439; -.
DR   HSSP; Q07960; 1TX4.
DR   ProteinModelPortal; Q9DBZ9; -.
DR   SMR; Q9DBZ9; 396-599.
DR   STRING; Q9DBZ9; -.
DR   PhosphoSite; Q9DBZ9; -.
DR   PRIDE; Q9DBZ9; -.
DR   Ensembl; ENSMUST00000040580; ENSMUSP00000043085; ENSMUSG00000032714.
DR   UCSC; uc007fyb.1; mouse.
DR   MGI; MGI:1918959; Syde1.
DR   eggNOG; roNOG10108; -.
DR   GeneTree; ENSGT00600000084123; -.
DR   HOGENOM; HBG506187; -.
DR   HOVERGEN; HBG053037; -.
DR   InParanoid; Q9DBZ9; -.
DR   OrthoDB; EOG48WC1M; -.
DR   ArrayExpress; Q9DBZ9; -.
DR   Bgee; Q9DBZ9; -.
DR   Genevestigator; Q9DBZ9; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005100; F:Rho GTPase activator activity; ISS:UniProtKB.
DR   GO; GO:0032862; P:activation of Rho GTPase activity; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
PE   2: Evidence at transcript level;
KW   GTPase activation; Phosphoprotein.
FT   CHAIN         1    737       Rho GTPase-activating protein SYDE1.
FT                                /FTId=PRO_0000312159.
FT   DOMAIN      398    604       Rho-GAP.
FT   COMPBIAS     38    162       Pro-rich.
FT   MOD_RES     231    231       Phosphoserine (By similarity).
FT   MOD_RES     235    235       Phosphoserine (By similarity).
FT   MOD_RES     244    244       Phosphoserine (By similarity).
FT   MOD_RES     246    246       Phosphothreonine (By similarity).
FT   MOD_RES     683    683       Phosphoserine (By similarity).
FT   MOD_RES     685    685       Phosphoserine (By similarity).
SQ   SEQUENCE   737 AA;  80496 MW;  929D6191D05339A1 CRC64;
     MAEPLLRKTF SRLRGREKLP RKKSEAKDRG HPAQRSEPKP PEPEPRVLEG SQAGAEVPPS
     PETPRSPTRG AYLQSLEPSS RRWVLGGAKP PEEISLGPRT PSSGEPAGEI WYNPIPEEDP
     RPPAPEPLGS QLASSEPEGP NIQGAAPTSP PTKTSRTKSP GPARRLSMKM KKLPELRRRL
     SLRSTRTGRD RERTAPAGSV ISRYRLDSSV GTPGQASVAG GSRSPRGGYL SDGDSPERPG
     GPPSPTAFRP YEVGPSARTP PAALWGRLSL HLYGLGGLRP SPGATPRDLC CLLQVDGVAR
     ARTGPLRSGP DFLRLDHTFH LELEAARLLR ALVLAWDPGV RRHRPCAQGT VLLPTIFRGC
     QAQQLAVRLE PQGFLYAKLT LSEQQEAPAT AEPRVFGLPL QLLVEREQSP GQVPLIIRKC
     VGQIECRGLR VVGLYRLCGS AAVKKELRDA FEQDSAAVCL SEDVYPDINV ITGILKDYLR
     ELPTPLITQP LYQVVLEAMA QGHPSRASLG PEGTRGLLRC LPDVERATLT LLLDHLRLVS
     SFHTHNRMTP QNXAVCFGPV LLPARQTPSR PRLRSSGPGV TSAVDFKRHI EVLHYLLQSW
     PDTRRPSDTP DGAVAPYLRP KRQPPLHLPL AGPEVVTRPR GRGGPESPPS NRYAGDWSVC
     GGDLLPCGRD FLSGPDYDHV TGSDSEEDDD ETGEPRGTTD FEDEFDAPFN PHLNLKDFDA
     LILDLERELS KQINVCL
//
ID   PXDC2_MOUSE             Reviewed;         530 AA.
AC   Q9DC11; Q6PET5; Q91ZV6;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Plexin domain-containing protein 2;
DE   AltName: Full=Tumor endothelial marker 7-related protein;
DE   Flags: Precursor;
GN   Name=Plxdc2; Synonyms=Tem7r;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX   MEDLINE=21443268; PubMed=11559528;
RA   Carson-Walter E.B., Watkins D.N., Nanda A., Vogelstein B.,
RA   Kinzler K.W., St Croix B.;
RT   "Cell surface tumor endothelial markers are conserved in mice and
RT   humans.";
RL   Cancer Res. 61:6649-6655(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NMRI; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH CTTN.
RX   PubMed=15574754; DOI=10.1158/0008-5472.CAN-04-2716;
RA   Nanda A., Buckhaults P., Seaman S., Agrawal N., Boutin P.,
RA   Shankara S., Nacht M., Teicher B., Stampfl J., Singh S.,
RA   Vogelstein B., Kinzler K.W., St Croix B.;
RT   "Identification of a binding partner for the endothelial cell surface
RT   proteins TEM7 and TEM7R.";
RL   Cancer Res. 64:8507-8511(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May play a role in tumor angiogenesis.
CC   -!- SUBUNIT: Interacts with CTTN.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- TISSUE SPECIFICITY: Expressed in tumor endothelium and in vessels
CC       of some normal tissues, such as the muscle and lung.
CC   -!- SIMILARITY: Belongs to the plexin family.
CC   -!- SIMILARITY: Contains 1 PSI domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF378761; AAL11998.1; -; mRNA.
DR   EMBL; AK004640; BAB23431.1; -; mRNA.
DR   EMBL; AK154921; BAE32927.1; -; mRNA.
DR   EMBL; BC057881; AAH57881.1; -; mRNA.
DR   IPI; IPI00471179; -.
DR   RefSeq; NP_080438.2; NM_026162.5.
DR   UniGene; Mm.313938; -.
DR   UniGene; Mm.394655; -.
DR   ProteinModelPortal; Q9DC11; -.
DR   SMR; Q9DC11; 314-357.
DR   STRING; Q9DC11; -.
DR   PhosphoSite; Q9DC11; -.
DR   PRIDE; Q9DC11; -.
DR   Ensembl; ENSMUST00000028081; ENSMUSP00000028081; ENSMUSG00000026748.
DR   GeneID; 67448; -.
DR   KEGG; mmu:67448; -.
DR   UCSC; uc008ikz.1; mouse.
DR   CTD; 67448; -.
DR   MGI; MGI:1914698; Plxdc2.
DR   eggNOG; roNOG13411; -.
DR   GeneTree; ENSGT00440000033408; -.
DR   HOGENOM; HBG402962; -.
DR   HOVERGEN; HBG079500; -.
DR   InParanoid; Q9DC11; -.
DR   OMA; RIYGPSD; -.
DR   OrthoDB; EOG4CRM04; -.
DR   NextBio; 324598; -.
DR   ArrayExpress; Q9DC11; -.
DR   Bgee; Q9DC11; -.
DR   CleanEx; MM_PLXDC2; -.
DR   Genevestigator; Q9DC11; -.
DR   GermOnline; ENSMUSG00000026748; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR003659; Plexin-like.
DR   InterPro; IPR002165; Plexin_repeat.
DR   Pfam; PF01437; PSI; 1.
DR   SMART; SM00423; PSI; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Membrane; Phosphoprotein; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     30       Potential.
FT   CHAIN        31    530       Plexin domain-containing protein 2.
FT                                /FTId=PRO_0000234575.
FT   TOPO_DOM     31    455       Extracellular (Potential).
FT   TRANSMEM    456    476       Helical; (Potential).
FT   TOPO_DOM    477    530       Cytoplasmic (Potential).
FT   DOMAIN      327    372       PSI.
FT   COMPBIAS    385    428       Thr-rich.
FT   MOD_RES     507    507       Phosphoserine.
FT   CARBOHYD    103    103       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    160    160       N-linked (GlcNAc...) (Potential).
FT   CONFLICT      5      5       R -> W (in Ref. 3; AAH57881).
FT   CONFLICT     26     26       Q -> H (in Ref. 1; AAL11998).
SQ   SEQUENCE   530 AA;  59616 MW;  FB956C020735E36D CRC64;
     MARFRRADLA AAGVMLLCHF LTDRFQFAHG EPGHHTNDWI YEVTNAFPWN EEGVEVDSQA
     YNHRWKRNVD PFKAVDTNRA SMGQASPESK GFTDLLLDDG QDNNTQIEED TDHNYYISRI
     YGPADSASRD LWVNIDQMEK DKVKIHGILS NTHRQAARVN LSFDFPFYGH FLNEVTVATG
     GFIYTGEVVH RMLTATQYIA PLMANFDPSV SRNSTVRYFD NGTALVVQWD HVHLQDNYNL
     GSFTFQATLL MDGRIIFGYK EIPVLVTQIS STNHPVKVGL SDAFVVVHRI QQIPNVRRRT
     IYEYHRVELQ MSKITNISAV EMTPLPTCLQ FNGCGPCVSS QIGFNCSWCS KLQRCSSGFD
     RHRQDWVDSG CPEEVQSKEK MCEKTEPGET SQTTTTSHTT TMQFRVLTTT RRAVTSQMPT
     SLPTEDDTKI ALHLKDSGAS TDDSAAEKKG GTLHAGLIVG ILILVLIIAA AILVTVYMYH
     HPTSAASIFF IERRPSRWPA MKFRRGSGHP AYAEVEPVGE KEGFIVSEQC
//
ID   DCAF6_MOUSE             Reviewed;         876 AA.
AC   Q9DC22; Q8BK50;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=DDB1- and CUL4-associated factor 6;
DE   AltName: Full=IQ motif and WD repeat-containing protein 1;
DE   AltName: Full=Nuclear receptor interaction protein;
DE            Short=NRIP;
GN   Name=Dcaf6; Synonyms=Iqwd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Lung, Ovary, and Uterus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-673, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Ligand-dependent coactivator of nuclear receptors.
CC       Enhance transcriptional activity of the nuclear receptors NR3C1
CC       and AR. May function as a substrate receptor for CUL4-DDB1 E3
CC       ubiquitin-protein ligase complex (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with the nuclear receptors NR3C1 and AR in the
CC       presence of ligand. Interacts with DDB1, CUL4A and CUL4B (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains 1 IQ domain.
CC   -!- SIMILARITY: Contains 7 WD repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK004618; BAB23414.1; -; mRNA.
DR   EMBL; AK077238; BAC36701.1; -; mRNA.
DR   IPI; IPI00120084; -.
DR   RefSeq; NP_083035.1; NM_028759.1.
DR   UniGene; Mm.227605; -.
DR   ProteinModelPortal; Q9DC22; -.
DR   SMR; Q9DC22; 38-285, 718-806.
DR   STRING; Q9DC22; -.
DR   PhosphoSite; Q9DC22; -.
DR   PRIDE; Q9DC22; -.
DR   Ensembl; ENSMUST00000027856; ENSMUSP00000027856; ENSMUSG00000026571.
DR   GeneID; 74106; -.
DR   KEGG; mmu:74106; -.
DR   UCSC; uc007djb.1; mouse.
DR   CTD; 74106; -.
DR   MGI; MGI:1921356; Dcaf6.
DR   eggNOG; roNOG11779; -.
DR   GeneTree; ENSGT00530000062951; -.
DR   HOGENOM; HBG447125; -.
DR   HOVERGEN; HBG054871; -.
DR   InParanoid; Q9DC22; -.
DR   OMA; EKLSPKP; -.
DR   OrthoDB; EOG4KPT96; -.
DR   PhylomeDB; Q9DC22; -.
DR   ArrayExpress; Q9DC22; -.
DR   Bgee; Q9DC22; -.
DR   CleanEx; MM_IQWD1; -.
DR   Genevestigator; Q9DC22; -.
DR   GO; GO:0080008; C:CUL4 RING ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 2.
DR   Pfam; PF00400; WD40; 5.
DR   SMART; SM00015; IQ; 1.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Repeat; Ubl conjugation pathway; WD repeat.
FT   CHAIN         1    876       DDB1- and CUL4-associated factor 6.
FT                                /FTId=PRO_0000304402.
FT   REPEAT       49     88       WD 1.
FT   REPEAT       92    133       WD 2.
FT   REPEAT      139    179       WD 3.
FT   REPEAT      189    229       WD 4.
FT   REPEAT      251    290       WD 5.
FT   DOMAIN      692    721       IQ.
FT   REPEAT      734    772       WD 6.
FT   REPEAT      775    814       WD 7.
FT   MOD_RES     336    336       Phosphoserine (By similarity).
FT   MOD_RES     670    670       Phosphothreonine (By similarity).
FT   MOD_RES     673    673       Phosphoserine.
FT   MOD_RES     863    863       Phosphoserine (By similarity).
FT   MOD_RES     866    866       Phosphoserine (By similarity).
SQ   SEQUENCE   876 AA;  97588 MW;  6F7B1A3F8DFBB407 CRC64;
     MARSGSCPHL LWDVRKRSLG LEDPSRLRSR YLGRREFIQR LKLEATLNVH DGCVNTICWN
     DTGEYILSGS DDTKLVISNP YSRKVLTTIR SGHRANIFSA KFLPCTDDKQ IVSCSGDGVI
     FYTNIEQDAE TNRQCQFTCH YGTTYEIMTV PNDPYTFLSC GEDGTVRWFD TRIKTSCTKE
     DCKDDILINC RRAATSVAIC PPVPYYLAVG CSDSSVRIYD RRMLGTRATG NYAGRGTTGM
     VARFIPSHLS NKSCRVTSLC YSEDGQEILV SYSSDYIYLF DPKDDTAREL KTPSAEERRE
     ELRQPPVKRL RLRGDWSDTG PRARPESERE RDGEQSPNVS LMQRMSDMLS RWFEEASEVA
     QSNRGRGRPR PRGGTNQPDV STLPTVPSSP NLEVCETAMD VDMPAALLQP STSSTDPVQA
     QAATAAIESP RSSSLLSCPD SEPRQSVEAS GHHAHHQSDN SNERLSPKPG TGEPVLSLHY
     STEGTTTSTI KLNFTDEWSS TASSSRGNGS HCKSEGQEEC LVPPSSVQPP EGDSETRAPE
     ELSEKGTLPE NLTQNQIDTA QLDNFPAEPL DSNSGEKNNP SQDSPCGLPE EGTLSETDRE
     TCEQASTESA TRHASTKPEL PSQTEAIEQA STESATRHTS ANPELPSQTE AIAPLAHEDP
     SARDSALQDT DDSDDDPVLI PGARYRTGPG DRRSAVARIQ EFFRRRKERK EMEELDTLNI
     RRPLVKMVYK GHRNSRTMIK EANFWGANFV MSGSDCGHIF IWDRHTAEHL MLLEADNHVV
     NCLQPHPFDP ILASSGIDYD IKIWSPLEES RIFNRKLADE VITRNELMLE ETRNTITVPA
     SFMLRMLASL NHIRADRLEG DRSEGSGQEN ENEDEE
//
ID   KC1D_MOUSE              Reviewed;         415 AA.
AC   Q9DC28; Q3TZK2; Q99KK4;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Casein kinase I isoform delta;
DE            Short=CKI-delta;
DE            Short=CKId;
DE            EC=2.7.11.1;
GN   Name=Csnk1d;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Lung, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH PER1, AND SUBCELLULAR LOCATION.
RX   PubMed=10848614; DOI=10.1128/MCB.20.13.4888-4899.2000;
RA   Vielhaber E., Eide E., Rivers A., Gao Z.-H., Virshup D.M.;
RT   "Nuclear entry of the circadian regulator mPER1 is controlled by
RT   mammalian casein kinase I epsilon.";
RL   Mol. Cell. Biol. 20:4888-4899(2000).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   DISRUPTION PHENOTYPE, INTERACTION WITH PER1 AND PER2, CATALYTIC
RP   ACTIVITY, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=19414593; DOI=10.1128/MCB.00338-09;
RA   Etchegaray J.P., Machida K.K., Noton E., Constance C.M., Dallmann R.,
RA   Di Napoli M.N., DeBruyne J.P., Lambert C.M., Yu E.A., Reppert S.M.,
RA   Weaver D.R.;
RT   "Casein kinase 1 delta regulates the pace of the mammalian circadian
RT   clock.";
RL   Mol. Cell. Biol. 29:3853-3866(2009).
CC   -!- FUNCTION: Casein kinases are operationally defined by their
CC       preferential utilization of acidic proteins such as caseins as
CC       substrates. It can phosphorylate a large number of proteins.
CC       Participates in Wnt signaling. Central component of the circadian
CC       clock. May act as a negative regulator of circadian rhythmicity by
CC       phosphorylating PER1 and PER2. Retains PER1 in the cytoplasm.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Exhibits substrate-dependent heparin activation
CC       (By similarity).
CC   -!- SUBUNIT: Monomer. Component of the circadian core oscillator,
CC       which includes the CRY proteins, CLOCK, or NPAS2, BMAL1 or BMAL2,
CC       CSNK1D and/or CSNK1E, TIMELESS and the PER proteins. Interacts
CC       directly with PER1 and PER2 which may lead to their degradation.
CC       Interacts with DBNDD2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9DC28-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9DC28-2; Sequence=VSP_010254;
CC         Note=Phosphorylated on Ser-401 (By similarity);
CC   -!- PTM: Autophosphorylated on serine and threonine residues (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Lethal. There are fewer embryos than
CC       expected at late stages of gestation; they weigh about 30% less
CC       than control animals, but appear otherwise normal. Mice die
CC       shortly after birth. Tissue-specific disruption increases the
CC       half-life of PER2 protein and alters circadian protein expression
CC       dynamics.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC       protein kinase family. Casein kinase I subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK004606; BAB23405.1; -; mRNA.
DR   EMBL; AK088642; BAC40472.1; -; mRNA.
DR   EMBL; AK152721; BAE31444.1; -; mRNA.
DR   EMBL; AK157812; BAE34206.1; -; mRNA.
DR   EMBL; BC004604; AAH04604.1; -; mRNA.
DR   IPI; IPI00410959; -.
DR   IPI; IPI00761242; -.
DR   PIR; S47616; S47616.
DR   RefSeq; NP_620690.1; NM_139059.2.
DR   UniGene; Mm.216227; -.
DR   ProteinModelPortal; Q9DC28; -.
DR   SMR; Q9DC28; 1-296.
DR   STRING; Q9DC28; -.
DR   PhosphoSite; Q9DC28; -.
DR   PRIDE; Q9DC28; -.
DR   Ensembl; ENSMUST00000018274; ENSMUSP00000018274; ENSMUSG00000025162.
DR   Ensembl; ENSMUST00000070575; ENSMUSP00000070721; ENSMUSG00000025162.
DR   GeneID; 104318; -.
DR   KEGG; mmu:104318; -.
DR   UCSC; uc007mva.1; mouse.
DR   UCSC; uc007mvb.1; mouse.
DR   CTD; 104318; -.
DR   MGI; MGI:1355272; Csnk1d.
DR   GeneTree; ENSGT00560000076651; -.
DR   HOVERGEN; HBG000176; -.
DR   OrthoDB; EOG42V8G9; -.
DR   PhylomeDB; Q9DC28; -.
DR   BRENDA; 2.7.11.1; 244.
DR   Reactome; REACT_24972; Circadian Clock (mouse).
DR   NextBio; 356922; -.
DR   ArrayExpress; Q9DC28; -.
DR   Bgee; Q9DC28; -.
DR   CleanEx; MM_CSNK1D; -.
DR   Genevestigator; Q9DC28; -.
DR   GermOnline; ENSMUSG00000025162; Mus musculus.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:Reactome.
DR   GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Kinase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.
FT   CHAIN         1    415       Casein kinase I isoform delta.
FT                                /FTId=PRO_0000192834.
FT   DOMAIN        9    277       Protein kinase.
FT   NP_BIND      15     23       ATP (By similarity).
FT   REGION      317    342       Autoinhibitory (By similarity).
FT   ACT_SITE    128    128       Proton acceptor (By similarity).
FT   BINDING      38     38       ATP (By similarity).
FT   MOD_RES     328    328       Phosphoserine (By similarity).
FT   MOD_RES     329    329       Phosphothreonine (By similarity).
FT   MOD_RES     331    331       Phosphoserine (By similarity).
FT   MOD_RES     337    337       Phosphothreonine (By similarity).
FT   MOD_RES     344    344       Phosphothreonine (By similarity).
FT   MOD_RES     347    347       Phosphothreonine (By similarity).
FT   MOD_RES     349    349       Phosphothreonine (By similarity).
FT   MOD_RES     350    350       Phosphoserine (By similarity).
FT   MOD_RES     352    352       Phosphothreonine (By similarity).
FT   MOD_RES     355    355       Phosphothreonine (By similarity).
FT   MOD_RES     356    356       Phosphoserine (By similarity).
FT   MOD_RES     361    361       Phosphoserine (By similarity).
FT   MOD_RES     382    382       Phosphoserine.
FT   MOD_RES     383    383       Phosphoserine (By similarity).
FT   MOD_RES     384    384       Phosphoserine (By similarity).
FT   MOD_RES     387    387       Phosphothreonine (By similarity).
FT   MOD_RES     392    392       Phosphothreonine (By similarity).
FT   MOD_RES     393    393       Phosphoserine (By similarity).
FT   MOD_RES     396    396       Phosphoserine (By similarity).
FT   MOD_RES     397    397       Phosphothreonine (By similarity).
FT   MOD_RES     398    398       Phosphoserine (By similarity).
FT   MOD_RES     406    406       Phosphoserine (By similarity).
FT   MOD_RES     407    407       Phosphoserine (By similarity).
FT   MOD_RES     411    411       Phosphoserine (By similarity).
FT   VAR_SEQ     400    415       IPGRVASSGLQSVVHR -> NSIPFEHHGK (in
FT                                isoform 2).
FT                                /FTId=VSP_010254.
FT   CONFLICT    313    313       E -> G (in Ref. 1; BAB23405).
SQ   SEQUENCE   415 AA;  47316 MW;  B97F04AF9EB466D2 CRC64;
     MELRVGNRYR LGRKIGSGSF GDIYLGTDIA AGEEVAIKLE CVKTKHPQLH IESKIYKMMQ
     GGVGIPTIRW CGAEGDYNVM VMELLGPSLE DLFNFCSRKF SLKTVLLLAD QMISRIEYIH
     SKNFIHRDVK PDNFLMGLGK KGNLVYIIDF GLAKKYRDAR THQHIPYREN KNLTGTARYA
     SINTHLGIEQ SRRDDLESLG YVLMYFNLGS LPWQGLKAAT KRQKYERISE KKMSTPIEVL
     CKGYPSEFAT YLNFCRSLRF DDKPDYSYLR QLFRNLFHRQ GFSYDYVFDW NMLKFGASRA
     ADDAERERRD REERLRHSRN PATRGLPSTA SGRLRGTQEV APPTPLTPTS HTANTSPRPV
     SGMERERKVS MRLHRGAPVN VSSSDLTGRQ DTSRMSTSQI PGRVASSGLQ SVVHR
//
ID   GNAI3_MOUSE             Reviewed;         354 AA.
AC   Q9DC51; A2AE36; Q3TGV1; Q61019;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Guanine nucleotide-binding protein G(k) subunit alpha;
DE   AltName: Full=G(i) alpha-3;
GN   Name=Gnai3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart, Kidney, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 36-46; 55-67; 181-192; 198-205 AND 249-257, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 248-322.
RC   STRAIN=CF-1 / Harlan;
RX   MEDLINE=97011591; PubMed=8858601;
RX   DOI=10.1002/(SICI)1098-2795(199607)44:3<315::AID-MRD5>3.3.CO;2-V;
RA   Williams C.J., Schultz R.M., Kopf G.S.;
RT   "G protein gene expression during mouse oocyte growth and maturation,
RT   and preimplantation embryo development.";
RL   Mol. Reprod. Dev. 44:315-323(1996).
RN   [6]
RP   INTERACTION WITH GPSM1.
RX   PubMed=16009138; DOI=10.1016/j.cell.2005.05.009;
RA   Sanada K., Tsai L.-H.;
RT   "G protein betagamma subunits and AGS3 control spindle orientation and
RT   asymmetric cell fate of cerebral cortical progenitors.";
RL   Cell 122:119-131(2005).
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are
CC       involved as modulators or transducers in various transmembrane
CC       signaling systems. G(k) is the stimulatory G protein of receptor-
CC       regulated K(+) channels (By similarity).
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and
CC       gamma. The alpha chain contains the guanine nucleotide binding
CC       site. Interacts with GPSM1.
CC   -!- INTERACTION:
CC       P09405:Ncl; NbExp=2; IntAct=EBI-641852, EBI-641864;
CC   -!- SIMILARITY: Belongs to the G-alpha family. G(i/o/t/z) subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK004566; BAB23377.1; -; mRNA.
DR   EMBL; AK077490; BAC36828.1; -; mRNA.
DR   EMBL; AK133749; BAE21821.1; -; mRNA.
DR   EMBL; AK168578; BAE40447.1; -; mRNA.
DR   EMBL; AK169067; BAE40854.1; -; mRNA.
DR   EMBL; AK169285; BAE41043.1; -; mRNA.
DR   EMBL; AL671854; CAM27256.1; -; Genomic_DNA.
DR   EMBL; BC041107; AAH41107.1; -; mRNA.
DR   EMBL; U38502; AAB01733.1; -; mRNA.
DR   IPI; IPI00338854; -.
DR   RefSeq; NP_034436.1; NM_010306.2.
DR   UniGene; Mm.271703; -.
DR   PDB; 3AB3; X-ray; 2.40 A; A/C=1-28.
DR   PDBsum; 3AB3; -.
DR   ProteinModelPortal; Q9DC51; -.
DR   SMR; Q9DC51; 5-348.
DR   IntAct; Q9DC51; 5.
DR   STRING; Q9DC51; -.
DR   PhosphoSite; Q9DC51; -.
DR   PRIDE; Q9DC51; -.
DR   Ensembl; ENSMUST00000000001; ENSMUSP00000000001; ENSMUSG00000000001.
DR   GeneID; 14679; -.
DR   KEGG; mmu:14679; -.
DR   UCSC; uc008qyd.1; mouse.
DR   CTD; 14679; -.
DR   MGI; MGI:95773; Gnai3.
DR   GeneTree; ENSGT00560000076725; -.
DR   HOGENOM; HBG444960; -.
DR   HOVERGEN; HBG063184; -.
DR   InParanoid; Q9DC51; -.
DR   OMA; RISQTNY; -.
DR   OrthoDB; EOG4WDDC1; -.
DR   PhylomeDB; Q9DC51; -.
DR   NextBio; 286582; -.
DR   ArrayExpress; Q9DC51; -.
DR   Bgee; Q9DC51; -.
DR   Genevestigator; Q9DC51; -.
DR   GermOnline; ENSMUSG00000000001; Mus musculus.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; TAS:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; TAS:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; TAS:MGI.
DR   InterPro; IPR001408; Gprotein_alpha_I.
DR   InterPro; IPR001019; Gprotein_alpha_su.
DR   InterPro; IPR011025; GproteinA_insert.
DR   Gene3D; G3DSA:1.10.400.10; GproteinA_insert; 1.
DR   PANTHER; PTHR10218; Gprotein_alph_bd; 1.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   PRINTS; PR00441; GPROTEINAI.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF47895; Transducn_insert; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; GTP-binding; Lipoprotein;
KW   Myristate; Nucleotide-binding; Palmitate; Phosphoprotein; Transducer.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    354       Guanine nucleotide-binding protein G(k)
FT                                subunit alpha.
FT                                /FTId=PRO_0000203693.
FT   NP_BIND      40     47       GTP (By similarity).
FT   NP_BIND     200    204       GTP (By similarity).
FT   NP_BIND     269    272       GTP (By similarity).
FT   MOD_RES      69     69       Phosphotyrosine (By similarity).
FT   MOD_RES     354    354       Phosphotyrosine (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
FT   LIPID         3      3       S-palmitoyl cysteine (By similarity).
SQ   SEQUENCE   354 AA;  40538 MW;  A03C83CE5488C777 CRC64;
     MGCTLSAEDK AAVERSKMID RNLREDGEKA AKEVKLLLLG AGESGKSTIV KQMKIIHEDG
     YSEDECKQYK VVVYSNTIQS IIAIIRAMGR LKIDFGESAR ADDARQLFVL AGSAEEGVMT
     SELAGVIKRL WRDGGVQACF SRSREYQLND SASYYLNDLD RISQTNYIPT QQDVLRTRVK
     TTGIVETHFT FKELYFKMFD VGGQRSERKK WIHCFEGVTA IIFCVALSDY DLVLAEDEEM
     NRMHESMKLF DSICNNKWFT DTSIILFLNK KDLFEEKIKR SPLTICYPEY TGSNTYEEAA
     AYIQCQFEDL NRRKDTKEVY THFTCATDTK NVQFVFDAVT DVIIKNNLKE CGLY
//
ID   ARP21_MOUSE             Reviewed;         807 AA.
AC   Q9DCB4; A1A561; Q3UUU8; Q7TS83; Q8BLD1; Q8BWM1; Q8C018; Q8C038;
AC   Q8C0Y6; Q91Y59;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 2.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=cAMP-regulated phosphoprotein 21;
DE            Short=ARPP-21;
DE   AltName: Full=Regulator of calmodulin signaling;
DE   AltName: Full=Thymocyte cAMP-regulated phosphoprotein;
GN   Name=Arpp21; Synonyms=Rcs, Tarpp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION,
RP   AND SUBCELLULAR LOCATION.
RC   TISSUE=Thymus;
RX   MEDLINE=21195301; PubMed=11298339;
RX   DOI=10.1002/1521-4141(200104)31:4<1141::AID-IMMU1141>3.0.CO;2-R;
RA   Kisielow J., Nairn A.C., Karjalainen K.;
RT   "TARPP, a novel protein that accompanies TCR gene rearrangement and
RT   thymocyte education.";
RL   Eur. J. Immunol. 31:1141-1149(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4; 6; 7; 8 AND 9),
RP   AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-807 (ISOFORM 5).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain, Corpora quadrigemina, Head, Olfactory bulb, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 10).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 55-61 AND 201-227, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION AT SER-55.
RX   PubMed=10854908; DOI=10.1016/S0028-3908(99)00230-0;
RA   Caporaso G.L., Bibb J.A., Snyder G.L., Valle C., Rakhilin S.,
RA   Fienberg A.A., Hemmings H.C. Jr., Nairn A.C., Greengard P.;
RT   "Drugs of abuse modulate the phosphorylation of ARPP-21, a cyclic AMP-
RT   regulated phosphoprotein enriched in the basal ganglia.";
RL   Neuropharmacology 39:1637-1644(2000).
RN   [6]
RP   METHYLATION AT ARG-650, MUTAGENESIS OF ARG-650, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=15096520; DOI=10.1074/jbc.M402544200;
RA   Kim J., Lee J., Yadav N., Wu Q., Carter C., Richard S., Richie E.,
RA   Bedford M.T.;
RT   "Loss of CARM1 results in hypomethylation of thymocyte cyclic AMP-
RT   regulated phosphoprotein and deregulated early T cell development.";
RL   J. Biol. Chem. 279:25339-25344(2004).
RN   [7]
RP   INTERACTION WITH CALM1, FUNCTION, AND PHOSPHORYLATION AT SER-55.
RX   PubMed=15499021; DOI=10.1126/science.1099961;
RA   Rakhilin S.V., Olson P.A., Nishi A., Starkova N.N., Fienberg A.A.,
RA   Nairn A.C., Surmeier D.J., Greengard P.;
RT   "A network of control mediated by regulator of calcium/calmodulin-
RT   dependent signaling.";
RL   Science 306:698-701(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
CC   -!- FUNCTION: Isoform 2 may act as a competitive inhibitor of
CC       calmodulin-dependent enzymes such as calcineurin in neurons.
CC   -!- SUBUNIT: Interacts with CALM1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=10;
CC       Name=1; Synonyms=TARPP;
CC         IsoId=Q9DCB4-1; Sequence=Displayed;
CC       Name=2; Synonyms=ARPP-21, RCS;
CC         IsoId=Q9DCB4-2; Sequence=VSP_029477, VSP_029478;
CC       Name=3;
CC         IsoId=Q9DCB4-3; Sequence=VSP_029485, VSP_029490;
CC       Name=4;
CC         IsoId=Q9DCB4-4; Sequence=VSP_029485, VSP_029488, VSP_029490;
CC       Name=5;
CC         IsoId=Q9DCB4-5; Sequence=VSP_029485;
CC         Note=No experimental confirmation available;
CC       Name=6;
CC         IsoId=Q9DCB4-6; Sequence=VSP_029479, VSP_029480;
CC         Note=No experimental confirmation available;
CC       Name=7;
CC         IsoId=Q9DCB4-7; Sequence=VSP_029487, VSP_029489;
CC         Note=No experimental confirmation available;
CC       Name=8;
CC         IsoId=Q9DCB4-8; Sequence=VSP_029483, VSP_029484;
CC         Note=No experimental confirmation available;
CC       Name=9;
CC         IsoId=Q9DCB4-9; Sequence=VSP_029479, VSP_029481, VSP_029491,
CC                                  VSP_029492;
CC         Note=No experimental confirmation available;
CC       Name=10;
CC         IsoId=Q9DCB4-10; Sequence=VSP_029482, VSP_029486;
CC         Note=No experimental confirmation available. May be produced at
CC         very low levels due to a premature stop codon in the mRNA,
CC         leading to nonsense-mediated mRNA decay;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is present at high levels in thymus
CC       and low levels in brain. In thymus, isoform 1 is specifically
CC       found in immature thymocytes (at protein level).
CC   -!- INDUCTION: Isoform 1 is down-regulated in thymocytes upon TCR
CC       engagement (at protein level).
CC   -!- PTM: Phosphorylation of isoform 2 at Ser-55 is enhanced upon
CC       dopamine D1 receptor activation and favors interaction with CALM1.
CC   -!- PTM: Isoform 1 is methylated by CARM1 in immature thymocytes
CC       (Probable).
CC   -!- SIMILARITY: Contains 1 R3H domain.
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DR   EMBL; AF324451; AAK48713.1; -; mRNA.
DR   EMBL; AK002950; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK029467; BAC26463.1; -; mRNA.
DR   EMBL; AK032417; BAC27859.1; -; mRNA.
DR   EMBL; AK032543; BAC27918.1; -; mRNA.
DR   EMBL; AK045507; BAC32399.1; -; mRNA.
DR   EMBL; AK050613; BAC34343.1; -; mRNA.
DR   EMBL; AK137974; BAE23526.1; -; mRNA.
DR   EMBL; BC027107; AAH27107.1; -; mRNA.
DR   EMBL; BC053001; AAH53001.1; -; mRNA.
DR   EMBL; BC128376; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00120663; -.
DR   IPI; IPI00129525; -.
DR   IPI; IPI00387538; -.
DR   IPI; IPI00404123; -.
DR   IPI; IPI00660397; -.
DR   IPI; IPI00828684; -.
DR   IPI; IPI00874312; -.
DR   IPI; IPI00875150; -.
DR   IPI; IPI00875278; -.
DR   IPI; IPI00875440; -.
DR   RefSeq; NP_001171086.1; NM_001177615.1.
DR   RefSeq; NP_001171087.1; NM_001177616.1.
DR   RefSeq; NP_001171088.1; NM_001177617.1.
DR   RefSeq; NP_001171089.1; NM_001177618.1.
DR   RefSeq; NP_001171090.1; NM_001177619.1.
DR   RefSeq; NP_001171091.1; NM_001177620.1.
DR   RefSeq; NP_001171094.1; NM_001177623.1.
DR   RefSeq; NP_083031.1; NM_028755.3.
DR   RefSeq; NP_150289.1; NM_033264.2.
DR   UniGene; Mm.297444; -.
DR   ProteinModelPortal; Q9DCB4; -.
DR   SMR; Q9DCB4; 146-256.
DR   STRING; Q9DCB4; -.
DR   PhosphoSite; Q9DCB4; -.
DR   PRIDE; Q9DCB4; -.
DR   Ensembl; ENSMUST00000027590; ENSMUSP00000027590; ENSMUSG00000032503.
DR   Ensembl; ENSMUST00000035085; ENSMUSP00000035085; ENSMUSG00000032503.
DR   Ensembl; ENSMUST00000062476; ENSMUSP00000058161; ENSMUSG00000032503.
DR   Ensembl; ENSMUST00000070218; ENSMUSP00000069264; ENSMUSG00000032503.
DR   Ensembl; ENSMUST00000084898; ENSMUSP00000081960; ENSMUSG00000032503.
DR   Ensembl; ENSMUST00000111872; ENSMUSP00000107503; ENSMUSG00000032503.
DR   GeneID; 74100; -.
DR   KEGG; mmu:74100; -.
DR   UCSC; uc009rwh.1; mouse.
DR   CTD; 74100; -.
DR   MGI; MGI:107562; Arpp21.
DR   eggNOG; roNOG12067; -.
DR   GeneTree; ENSGT00440000038338; -.
DR   HOVERGEN; HBG052192; -.
DR   OMA; DCSQEYT; -.
DR   OrthoDB; EOG4NP735; -.
DR   NextBio; 339769; -.
DR   ArrayExpress; Q9DCB4; -.
DR   Bgee; Q9DCB4; -.
DR   CleanEx; MM_ARPP21; -.
DR   Genevestigator; Q9DCB4; -.
DR   GermOnline; ENSMUSG00000032503; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; TAS:MGI.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0034605; P:cellular response to heat; IDA:MGI.
DR   InterPro; IPR001374; R3H_ss-bd.
DR   Pfam; PF01424; R3H; 1.
DR   SMART; SM00393; R3H; 1.
DR   PROSITE; PS51061; R3H; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW   Direct protein sequencing; Methylation; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    807       cAMP-regulated phosphoprotein 21.
FT                                /FTId=PRO_0000064683.
FT   DOMAIN      163    226       R3H.
FT   COILED       32     57       Potential.
FT   COMPBIAS    335    433       Ser-rich.
FT   COMPBIAS    502    749       Gln-rich.
FT   MOD_RES       2      2       N-acetylserine (By similarity).
FT   MOD_RES      32     32       Phosphoserine (By similarity).
FT   MOD_RES      55     55       Phosphoserine; by PKA.
FT   MOD_RES     278    278       Phosphoserine.
FT   MOD_RES     381    381       Phosphoserine (By similarity).
FT   MOD_RES     557    557       Phosphoserine (By similarity).
FT   MOD_RES     650    650       Omega-N-methylated arginine.
FT   VAR_SEQ      87     88       ES -> TL (in isoform 2).
FT                                /FTId=VSP_029477.
FT   VAR_SEQ      89    807       Missing (in isoform 2).
FT                                /FTId=VSP_029478.
FT   VAR_SEQ     228    228       I -> M (in isoform 6 and isoform 9).
FT                                /FTId=VSP_029479.
FT   VAR_SEQ     229    807       Missing (in isoform 6).
FT                                /FTId=VSP_029480.
FT   VAR_SEQ     229    330       Missing (in isoform 9).
FT                                /FTId=VSP_029481.
FT   VAR_SEQ     229    282       PEQRFCEHLKDEKSEESQKRFILKRDNSSIDKEDNQNRMHP
FT                                FRDDRRSKSIEER -> QFAPRKAYFWTTGLTETAQEELPG
FT                                AGRAAQRLSSGGQTTSGLGAAQIRTVPTAI (in
FT                                isoform 10).
FT                                /FTId=VSP_029482.
FT   VAR_SEQ     229    248       PEQRFCEHLKDEKSEESQKR -> VQDTGWRCKHAHRTGAV
FT                                CTN (in isoform 8).
FT                                /FTId=VSP_029483.
FT   VAR_SEQ     249    807       Missing (in isoform 8).
FT                                /FTId=VSP_029484.
FT   VAR_SEQ     265    297       Missing (in isoform 3, isoform 4 and
FT                                isoform 5).
FT                                /FTId=VSP_029485.
FT   VAR_SEQ     283    807       Missing (in isoform 10).
FT                                /FTId=VSP_029486.
FT   VAR_SEQ     298    371       SVCSQESLFLDNSRLQEDMHICNETYKKRQLFRAHRDSSGR
FT                                TSGSRQSSSETELRWPDHQRAWSSTDSDSSNRN -> VSSC
FT                                FNCLLSMVLPSAERPLVARTEIWQGVQRLGARNELQSRKHK
FT                                CFWERTWFRDALKQSKSLCMCPPGHHLPG (in isoform
FT                                7).
FT                                /FTId=VSP_029487.
FT   VAR_SEQ     310    329       Missing (in isoform 4).
FT                                /FTId=VSP_029488.
FT   VAR_SEQ     372    807       Missing (in isoform 7).
FT                                /FTId=VSP_029489.
FT   VAR_SEQ     543    543       Q -> QSVQSLQPSSQSVQYPAVSFPPQHLLPMSPTQHFPL
FT                                (in isoform 3 and isoform 4).
FT                                /FTId=VSP_029490.
FT   VAR_SEQ     674    703       YQPVLSGQQGFQGMMGVQQSAHSQGVMSSQ -> LMIAPDT
FT                                WPTVPAELALQKVTLLWISEGRW (in isoform 9).
FT                                /FTId=VSP_029491.
FT   VAR_SEQ     704    807       Missing (in isoform 9).
FT                                /FTId=VSP_029492.
FT   MUTAGEN     650    650       R->A: Abolishes methylation, no effect on
FT                                subcellular location.
FT   CONFLICT    263    263       N -> NQ (in Ref. 2; BAC26463).
SQ   SEQUENCE   807 AA;  88567 MW;  99DD32A59954E139 CRC64;
     MSEQGGLTPT ILEEGQTEPE SAPENGILKS ESLDEEEKLE LQRRLAAQNQ ERRKSKSGAG
     KGKLTRSLAV CEESSARSGG ESHQDQESIH LQLSSFPSLQ EEDKSRKDDS EREKEKDKNR
     EKLSERPKIR MLSKDCSQEY TDSTGIDLHG FLINTLKNNS RDRMILLKME QEMIDFIADS
     NNHYKKFPQM SSYQRMLVHR VAAYFGLDHN VDQTGKSVII NKTSSTRIPE QRFCEHLKDE
     KSEESQKRFI LKRDNSSIDK EDNQNRMHPF RDDRRSKSIE EREEEYQRVR ERIFAHDSVC
     SQESLFLDNS RLQEDMHICN ETYKKRQLFR AHRDSSGRTS GSRQSSSETE LRWPDHQRAW
     SSTDSDSSNR NLKPTMTKTA SFGGITVLTR GDSTSSTRSA GKLSKTGSES SSSAGSSGSL
     SRTHPQSTAL TSSVAAGSPG CMAYSENGMG GQVPPSSTSY ILLPLESATG IPPGSILLNP
     HTGQPFVNPD GTPAIYNPPG SQQTLRGTVG GQPQQPPQQQ PSPQPQQQVQ ASQPQMAGPL
     VTQREELAAQ FSQLSMSRQS SGDTPEPPSG TVYPASLLPQ TAQPQSYVIT SAGQQLSTGG
     FSDSGPPISQ QVLQAPPSPQ GFVQQPPPAQ MSVYYYPSGQ YPTSTSQQYR PLASVQYSAQ
     RSQQIPQTTQ QAGYQPVLSG QQGFQGMMGV QQSAHSQGVM SSQQGAPVHG VMVSYPTMSS
     YQVPMTQGSQ AVPQQTYQPP IMLPSQAGQG SLPATGMPVY CNVTPPNPQN NLRLMGPHCP
     SSTVPVMSAS CRTNCGNVSN AGWQVKF
//
ID   TOM20_MOUSE             Reviewed;         145 AA.
AC   Q9DCC8;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Mitochondrial import receptor subunit TOM20 homolog;
DE   AltName: Full=Mitochondrial 20 kDa outer membrane protein;
DE   AltName: Full=Outer mitochondrial membrane receptor Tom20;
GN   Name=Tomm20;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 126-132, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Central component of the receptor complex responsible
CC       for the recognition and translocation of cytosolically synthesized
CC       mitochondrial preproteins. Together with TOM22 functions as the
CC       transit peptide receptor at the surface of the mitochondrion outer
CC       membrane and facilitates the movement of preproteins into the
CC       TOM40 translocation pore (By similarity).
CC   -!- SUBUNIT: Forms part of the preprotein translocase complex of the
CC       outer mitochondrial membrane (TOM complex) which consists of at
CC       least 7 different proteins (TOMM5, TOMM6, TOMM7, TOMM20, TOMM22,
CC       TOMM40 and TOMM70). Interacts with TOM22. Interacts with APEX1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC       membrane protein (Potential).
CC   -!- SIMILARITY: Belongs to the Tom20 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK002902; BAB22444.1; -; mRNA.
DR   EMBL; BC002087; AAH02087.1; -; mRNA.
DR   IPI; IPI00120715; -.
DR   RefSeq; NP_077176.1; NM_024214.1.
DR   UniGene; Mm.380026; -.
DR   UniGene; Mm.6932; -.
DR   ProteinModelPortal; Q9DCC8; -.
DR   SMR; Q9DCC8; 59-126.
DR   STRING; Q9DCC8; -.
DR   PhosphoSite; Q9DCC8; -.
DR   PRIDE; Q9DCC8; -.
DR   Ensembl; ENSMUST00000078812; ENSMUSP00000077864; ENSMUSG00000058779.
DR   GeneID; 67952; -.
DR   KEGG; mmu:67952; -.
DR   UCSC; uc009nza.1; mouse.
DR   CTD; 67952; -.
DR   MGI; MGI:1915202; Tomm20.
DR   GeneTree; ENSGT00390000011698; -.
DR   HOGENOM; HBG444091; -.
DR   HOVERGEN; HBG057315; -.
DR   InParanoid; Q9DCC8; -.
DR   OMA; HKRINAP; -.
DR   OrthoDB; EOG48SGVH; -.
DR   PhylomeDB; Q9DCC8; -.
DR   NextBio; 457301; -.
DR   ArrayExpress; Q9DCC8; -.
DR   Bgee; Q9DCC8; -.
DR   Genevestigator; Q9DCC8; -.
DR   GermOnline; ENSMUSG00000058779; Mus musculus.
DR   GermOnline; ENSMUSG00000060714; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005742; C:mitochondrial outer membrane translocase complex; IEA:InterPro.
DR   GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; ISS:HGNC.
DR   GO; GO:0051082; F:unfolded protein binding; ISS:HGNC.
DR   GO; GO:0006626; P:protein targeting to mitochondrion; ISS:HGNC.
DR   InterPro; IPR002056; MAS20_rcpt-related.
DR   InterPro; IPR022422; MAS20_rcpt_metazoan.
DR   PANTHER; PTHR12430; MAS20_rcpt; 1.
DR   Pfam; PF02064; MAS20; 1.
DR   PIRSF; PIRSF037707; MAS20_rcpt; 1.
DR   PRINTS; PR01989; EUOM20RECPTR.
DR   PRINTS; PR00351; OM20RECEPTOR.
DR   TIGRFAMs; TIGR00985; 3a0801s04tom; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Phosphoprotein; Protein transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    145       Mitochondrial import receptor subunit
FT                                TOM20 homolog.
FT                                /FTId=PRO_0000051539.
FT   TOPO_DOM      1      6       Mitochondrial intermembrane (Potential).
FT   TRANSMEM      7     24       Helical; (Potential).
FT   TOPO_DOM     25    145       Cytoplasmic (Potential).
FT   MOD_RES     135    135       Phosphoserine.
FT   MOD_RES     138    138       Phosphoserine.
SQ   SEQUENCE   145 AA;  16284 MW;  50E3BD25AD5C9B3B CRC64;
     MVGRNSAIAA GVCGALFIGY CIYFDRKRRS DPNFKNRLRE RRKKQKLAKE RAGLSKLPDL
     KDAEAVQKFF LEEIQLGEEL LAQGDYEKGV DHLTNAIAVC GQPQQLLQVL QQTLPPPVFQ
     MLLTKLPTIS QRIVSAQSLA EDDVE
//
ID   PK1IP_MOUSE             Reviewed;         382 AA.
AC   Q9DCE5; Q3UBK7; Q80UT4; Q8C5N6; Q923K2; Q9D3E9;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=p21-activated protein kinase-interacting protein 1;
DE   AltName: Full=PAK1-interacting protein 1;
DE   AltName: Full=Putative PAK inhibitor Skb15;
GN   Name=Pak1ip1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=21286898; PubMed=11389855; DOI=10.1016/S1097-2765(01)00248-9;
RA   Kim H.W., Yang P., Qyang Y., Lai H., Du H., Henkel J.S., Kumar K.,
RA   Bao S., Liu M., Marcus S.;
RT   "Genetic and molecular characterization of Skb15, a highly conserved
RT   inhibitor of the fission yeast PAK, Shk1.";
RL   Mol. Cell 7:1095-1101(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Liu M., Xia C.;
RT   "Mouse homolog of human p21-activated protein kinase-interacting
RT   protein 1 (hPIP1).";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Kidney, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 254-382.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Negatively regulates the PAK1 kinase. PAK1 is a member
CC       of the PAK kinase family, which have been shown to play a positive
CC       role in the regulation of signaling pathways involving MAPK8 and
CC       RELA. PAK1 exists as an inactive homodimer, which is activated by
CC       binding of small GTPases such as CDC42 to an N-terminal regulatory
CC       domain. PAK1IP1 also binds to the N-terminus of PAK1, and inhibits
CC       the specific activation of PAK1 by CDC42 (By similarity).
CC   -!- SUBUNIT: Interacts with PAK1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity).
CC   -!- SIMILARITY: Contains 5 WD repeats.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY030406; AAK51599.1; -; mRNA.
DR   EMBL; AF386076; AAL40652.1; -; mRNA.
DR   EMBL; AK002852; BAB22407.1; -; mRNA.
DR   EMBL; AK077941; BAC37076.1; -; mRNA.
DR   EMBL; AK150747; BAE29818.1; -; mRNA.
DR   EMBL; AK150919; BAE29957.1; -; mRNA.
DR   EMBL; BC051498; AAH51498.1; -; mRNA.
DR   IPI; IPI00120790; -.
DR   RefSeq; NP_080826.2; NM_026550.3.
DR   UniGene; Mm.24789; -.
DR   ProteinModelPortal; Q9DCE5; -.
DR   SMR; Q9DCE5; 2-281.
DR   STRING; Q9DCE5; -.
DR   PhosphoSite; Q9DCE5; -.
DR   PRIDE; Q9DCE5; -.
DR   Ensembl; ENSMUST00000046951; ENSMUSP00000040846; ENSMUSG00000038683.
DR   GeneID; 68083; -.
DR   KEGG; mmu:68083; -.
DR   UCSC; uc007qer.1; mouse.
DR   CTD; 68083; -.
DR   MGI; MGI:1915333; Pak1ip1.
DR   eggNOG; roNOG14133; -.
DR   GeneTree; ENSGT00390000001263; -.
DR   HOGENOM; HBG403002; -.
DR   HOVERGEN; HBG082144; -.
DR   InParanoid; Q9DCE5; -.
DR   OMA; YDMKKKV; -.
DR   OrthoDB; EOG45MN5T; -.
DR   PhylomeDB; Q9DCE5; -.
DR   NextBio; 326384; -.
DR   ArrayExpress; Q9DCE5; -.
DR   Bgee; Q9DCE5; -.
DR   CleanEx; MM_PAK1IP1; -.
DR   Genevestigator; Q9DCE5; -.
DR   GermOnline; ENSMUSG00000038683; Mus musculus.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 4.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   2: Evidence at transcript level;
KW   Nucleus; Repeat; Signal transduction inhibitor; WD repeat.
FT   CHAIN         1    382       p21-activated protein kinase-interacting
FT                                protein 1.
FT                                /FTId=PRO_0000051126.
FT   REPEAT       37     77       WD 1.
FT   REPEAT       80    120       WD 2.
FT   REPEAT      122    160       WD 3.
FT   REPEAT      202    240       WD 4.
FT   REPEAT      243    284       WD 5.
FT   CONFLICT    176    176       G -> R (in Ref. 1; AAK51599).
FT   CONFLICT    382    382       M -> MSLTWQIPDFSSLSECPFDGILHVPVRRKYLLP
FT                                (in Ref. 2 and 3; BAB22407).
SQ   SEQUENCE   382 AA;  42116 MW;  7EA5788A4B7EF2D1 CRC64;
     MELVAGSYEQ VLFGFTVQRG PAKSGHQETW TPVADFTHHS HTASLSVLAS NSRYVVSGSK
     DETIHIYDMK RKVEHGALVH HAGTVTCLKF HGNQHLISGA EDGHICIWDV KRWKCLKTFK
     AHRGHVTFLS IHPSGKLALS VGTDKTLRTW NLIEGRSAFI KNIKENAHIV EWSPSGGKYI
     VVVQNKVDVY RLGTASVSGT ITNGKRISSV TFLSDSVLAV AGDEEVVRIF DCDSLECLCE
     FRAHENRVKD MVSFEVPDHH VLVTASNDGF IKMWTLPQDK KVPPSLLCEA KTGARLTCLT
     VWLDRAANGM ASLPPAAEPC PDQPKTIEKE SGDTVQEETS EPNSEKSDVS GDSKQPTKGN
     SPVTAKKRKM ATMSEKKRKK KM
//
ID   TMM25_MOUSE             Reviewed;         365 AA.
AC   Q9DCF1; Q3TMP3; Q6PAK7;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Transmembrane protein 25;
DE   Flags: Precursor;
GN   Name=Tmem25;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
CC       membrane protein (Potential).
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Secreted (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9DCF1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9DCF1-2; Sequence=VSP_012942;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 Ig-like (immunoglobulin-like) domain.
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DR   EMBL; AK002841; BAB22398.1; -; mRNA.
DR   EMBL; AK165199; BAE38074.1; -; mRNA.
DR   EMBL; AK165827; BAE38398.1; -; mRNA.
DR   EMBL; BC060057; AAH60057.1; -; mRNA.
DR   EMBL; BC060243; AAH60243.1; -; mRNA.
DR   IPI; IPI00120815; -.
DR   IPI; IPI00553522; -.
DR   RefSeq; NP_082141.1; NM_027865.2.
DR   UniGene; Mm.41409; -.
DR   ProteinModelPortal; Q9DCF1; -.
DR   SMR; Q9DCF1; 42-73, 140-221.
DR   STRING; Q9DCF1; -.
DR   PhosphoSite; Q9DCF1; -.
DR   PRIDE; Q9DCF1; -.
DR   Ensembl; ENSMUST00000002100; ENSMUSP00000002100; ENSMUSG00000002032.
DR   Ensembl; ENSMUST00000114705; ENSMUSP00000110353; ENSMUSG00000002032.
DR   GeneID; 71687; -.
DR   KEGG; mmu:71687; -.
DR   UCSC; uc009pem.1; mouse.
DR   CTD; 71687; -.
DR   MGI; MGI:1918937; Tmem25.
DR   eggNOG; roNOG07579; -.
DR   GeneTree; ENSGT00390000003414; -.
DR   HOVERGEN; HBG057137; -.
DR   OrthoDB; EOG4255T6; -.
DR   PhylomeDB; Q9DCF1; -.
DR   NextBio; 334233; -.
DR   ArrayExpress; Q9DCF1; -.
DR   Bgee; Q9DCF1; -.
DR   CleanEx; MM_TMEM25; -.
DR   Genevestigator; Q9DCF1; -.
DR   GermOnline; ENSMUSG00000002032; Mus musculus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR013162; CD80_C2-set.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Pfam; PF08205; C2-set_2; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Secreted; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     26       Potential.
FT   CHAIN        27    365       Transmembrane protein 25.
FT                                /FTId=PRO_0000014985.
FT   TOPO_DOM     27    232       Extracellular (Potential).
FT   TRANSMEM    233    253       Helical; (Potential).
FT   TOPO_DOM    254    365       Cytoplasmic (Potential).
FT   DOMAIN       30    123       Ig-like.
FT   CARBOHYD    106    106       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    162    162       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    192    192       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    205    205       N-linked (GlcNAc...) (Potential).
FT   DISULFID     52    107       By similarity.
FT   VAR_SEQ     280    365       Missing (in isoform 2).
FT                                /FTId=VSP_012942.
FT   CONFLICT    279    279       S -> R (in Ref. 2).
SQ   SEQUENCE   365 AA;  39170 MW;  9BE03C7945A24757 CRC64;
     MELPLSQATL RHTLLLLPAL LSSGQGELAP QIDGQTWAER ALRENEHHAF TCRVAGGSAT
     PRLAWYLDGQ LQEATTSRLL SVGGDAFSGG TSTFTVTAQR SQHELNCSLQ DPGSGRPANA
     SVILNVQFKP EIAQVGAKYQ EAQGPGLLVV LFALVRANPP ANVTWIDQDG PVTVNASDFL
     VLDAQNYPWL TNHTVQLQLR SLAHNLSVVA TNDVGVTSAS LPAPGLLATR IEVPLLGIVV
     AGGLALGTLV GFSTLVACLV CRKEKKTKGP SRRPSLISSD SNNLKLNNVR LPRENMSLPS
     NLQLNDLTPD LRGKATERPM AQHSSRPELL EAEPGGLLTS RGFIRLPMLG YIYRVSSVSS
     DEIWL
//
ID   SSRG_MOUSE              Reviewed;         185 AA.
AC   Q9DCF9; Q8C0Z8;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Translocon-associated protein subunit gamma;
DE            Short=TRAP-gamma;
DE   AltName: Full=Signal sequence receptor subunit gamma;
DE            Short=SSR-gamma;
GN   Name=Ssr3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Head, Kidney, Liver, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: TRAP proteins are part of a complex whose function is to
CC       bind calcium to the ER membrane and thereby regulate the retention
CC       of ER resident proteins (By similarity).
CC   -!- SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and
CC       TRAP-gamma.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9DCF9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9DCF9-2; Sequence=VSP_013474, VSP_013475;
CC   -!- SIMILARITY: Belongs to the TRAP-gamma family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK002818; BAB22381.1; -; mRNA.
DR   EMBL; AK029353; BAC26413.1; -; mRNA.
DR   EMBL; AK076235; BAC36268.1; -; mRNA.
DR   EMBL; AK088555; BAC40420.1; -; mRNA.
DR   EMBL; BC011111; AAH11111.1; -; mRNA.
DR   IPI; IPI00120826; -.
DR   IPI; IPI00458428; -.
DR   RefSeq; NP_080431.1; NM_026155.3.
DR   UniGene; Mm.232728; -.
DR   ProteinModelPortal; Q9DCF9; -.
DR   STRING; Q9DCF9; -.
DR   PhosphoSite; Q9DCF9; -.
DR   PRIDE; Q9DCF9; -.
DR   Ensembl; ENSMUST00000029414; ENSMUSP00000029414; ENSMUSG00000027828.
DR   GeneID; 67437; -.
DR   KEGG; mmu:67437; -.
DR   UCSC; uc008pkn.1; mouse.
DR   UCSC; uc008pko.1; mouse.
DR   CTD; 67437; -.
DR   MGI; MGI:1914687; Ssr3.
DR   GeneTree; ENSGT00390000000970; -.
DR   HOGENOM; HBG716286; -.
DR   HOVERGEN; HBG012424; -.
DR   InParanoid; Q9DCF9; -.
DR   OMA; AVPIWLF; -.
DR   OrthoDB; EOG4Z36FX; -.
DR   PhylomeDB; Q9DCF9; -.
DR   NextBio; 324562; -.
DR   ArrayExpress; Q9DCF9; -.
DR   Bgee; Q9DCF9; -.
DR   CleanEx; MM_SSR3; -.
DR   Genevestigator; Q9DCF9; -.
DR   GermOnline; ENSMUSG00000027828; Mus musculus.
DR   GO; GO:0030176; C:integral to endoplasmic reticulum membrane; IEA:InterPro.
DR   GO; GO:0005784; C:Sec61 translocon complex; IEA:InterPro.
DR   GO; GO:0006613; P:cotranslational protein targeting to membrane; IEA:InterPro.
DR   InterPro; IPR009779; TRAP-gamma.
DR   PANTHER; PTHR13399; TRAP-gamma; 1.
DR   Pfam; PF07074; TRAP-gamma; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    185       Translocon-associated protein subunit
FT                                gamma.
FT                                /FTId=PRO_0000191691.
FT   TOPO_DOM      1     27       Lumenal (Potential).
FT   TRANSMEM     28     48       Helical; (Potential).
FT   TOPO_DOM     49     54       Cytoplasmic (Potential).
FT   TRANSMEM     55     76       Helical; (Potential).
FT   TOPO_DOM     77    135       Lumenal (Potential).
FT   TRANSMEM    136    157       Helical; (Potential).
FT   TOPO_DOM    158    163       Cytoplasmic (Potential).
FT   TRANSMEM    164    184       Helical; (Potential).
FT   MOD_RES      11     11       Phosphoserine (By similarity).
FT   MOD_RES     105    105       Phosphoserine.
FT   VAR_SEQ     165    179       NYILSISASSGLIAL -> YPLESFPINSSLLCF (in
FT                                isoform 2).
FT                                /FTId=VSP_013474.
FT   VAR_SEQ     180    185       Missing (in isoform 2).
FT                                /FTId=VSP_013475.
SQ   SEQUENCE   185 AA;  21064 MW;  18E0A54483E45D6E CRC64;
     MAPKGGSKQQ SEEDLLLQDF SRNLSAKSSA LFFGNAFIVS AIPIWLYWRI WHMDLIQSAV
     LYSVMTLVST YLVAFAYKNV KFVLKHKVAQ KREDAVSKEV TRKLSEADNR KMSRKEKDER
     ILWKKNEVAD YEATTFSIFY NNTLFLVLVI VASFFILKNF NPTVNYILSI SASSGLIALL
     STGSK
//
ID   MENTO_MOUSE             Reviewed;         235 AA.
AC   Q9DCI3; Q3U8Q7; Q99J63; Q9D356;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-NOV-2002, sequence version 2.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=MLN64 N-terminal domain homolog;
DE   AltName: Full=STARD3 N-terminal-like protein;
GN   Name=Stard3nl; Synonyms=Mentho;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NMRI; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-193, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane; Multi-pass membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Contains 1 MENTAL domain.
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DR   EMBL; AK002760; BAB22337.1; -; mRNA.
DR   EMBL; AK152116; BAE30960.1; -; mRNA.
DR   EMBL; BC003334; AAH03334.1; -; mRNA.
DR   IPI; IPI00317163; -.
DR   RefSeq; NP_077232.2; NM_024270.2.
DR   UniGene; Mm.41940; -.
DR   ProteinModelPortal; Q9DCI3; -.
DR   STRING; Q9DCI3; -.
DR   PhosphoSite; Q9DCI3; -.
DR   PRIDE; Q9DCI3; -.
DR   Ensembl; ENSMUST00000039694; ENSMUSP00000037991; ENSMUSG00000003062.
DR   GeneID; 76205; -.
DR   KEGG; mmu:76205; -.
DR   UCSC; uc007ppa.1; mouse.
DR   CTD; 76205; -.
DR   MGI; MGI:1923455; Stard3nl.
DR   GeneTree; ENSGT00530000063139; -.
DR   HOGENOM; HBG716905; -.
DR   HOVERGEN; HBG052455; -.
DR   InParanoid; Q9DCI3; -.
DR   OMA; VQYDYYS; -.
DR   OrthoDB; EOG4D52ZK; -.
DR   NextBio; 344761; -.
DR   ArrayExpress; Q9DCI3; -.
DR   Bgee; Q9DCI3; -.
DR   CleanEx; MM_STARD3NL; -.
DR   Genevestigator; Q9DCI3; -.
DR   GermOnline; ENSMUSG00000003062; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR019498; MENTAL.
DR   Pfam; PF10457; MENTAL; 1.
DR   PROSITE; PS51439; MENTAL; 1.
PE   1: Evidence at protein level;
KW   Endosome; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    235       MLN64 N-terminal domain homolog.
FT                                /FTId=PRO_0000096420.
FT   TOPO_DOM      1     53       Cytoplasmic (Potential).
FT   TRANSMEM     54     74       Helical; (Potential).
FT   TOPO_DOM     75     97       Extracellular (Potential).
FT   TRANSMEM     98    118       Helical; (Potential).
FT   TOPO_DOM    119    122       Cytoplasmic (Potential).
FT   TRANSMEM    123    143       Helical; (Potential).
FT   TOPO_DOM    144    150       Extracellular (Potential).
FT   TRANSMEM    151    171       Helical; (Potential).
FT   TOPO_DOM    172    235       Cytoplasmic (Potential).
FT   DOMAIN       48    218       MENTAL.
FT   MOD_RES      27     27       Phosphoserine.
FT   MOD_RES      39     39       Phosphoserine (By similarity).
FT   MOD_RES     193    193       Phosphoserine.
FT   MOD_RES     210    210       Phosphoserine (By similarity).
FT   MOD_RES     214    214       Phosphoserine (By similarity).
FT   MOD_RES     218    218       Phosphoserine (By similarity).
FT   CONFLICT     32     33       QL -> HS (in Ref. 1; BAB22337).
FT   CONFLICT     52     52       R -> G (in Ref. 2; AAH03334).
SQ   SEQUENCE   235 AA;  26811 MW;  F251725390CB1503 CRC64;
     MNHLPEHMEN TLTGSQSSHA SLRDIHSINP AQLMARIESY EGREKKGISD VRRTFCLFVT
     FDLLFVTLLW IIELNVNGGI ENTLKKEVIH YDYYSSYFDI FLLAVFRFKV LILGYAVCRL
     RHWWAIALTT AVTSAFLLAK VILSKLFSQG AFGYVLPIIS FILAWIETWF LDFKVLPQEA
     EEENRLLLVQ DASERAALIP AGLSDGQFYS PPESEAGSEE EAEEKQESEK PLLEL
//
ID   NPL_MOUSE               Reviewed;         320 AA.
AC   Q9DCJ9;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=N-acetylneuraminate lyase;
DE            Short=NALase;
DE            EC=4.1.3.3;
DE   AltName: Full=N-acetylneuraminate pyruvate-lyase;
DE   AltName: Full=N-acetylneuraminic acid aldolase;
DE   AltName: Full=Sialate lyase;
DE   AltName: Full=Sialate-pyruvate lyase;
DE   AltName: Full=Sialic acid aldolase;
DE   AltName: Full=Sialic acid lyase;
GN   Name=Npl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Catalyzes the cleavage of N-acetylneuraminic acid
CC       (sialic acid) to form pyruvate and N-acetylmannosamine via a
CC       Schiff base intermediate. It prevents sialic acids from being
CC       recycled and returning to the cell surface (By similarity).
CC   -!- CATALYTIC ACTIVITY: N-acetylneuraminate = N-acetyl-D-mannosamine +
CC       pyruvate.
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation;
CC       D-fructose 6-phosphate from N-acetylneuraminate: step 1/5.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the DHDPS family. NanA subfamily.
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DR   EMBL; AK002734; BAB22314.1; -; mRNA.
DR   EMBL; AK088859; BAC40618.1; -; mRNA.
DR   EMBL; BC022734; AAH22734.1; -; mRNA.
DR   IPI; IPI00120989; -.
DR   RefSeq; NP_083025.1; NM_028749.1.
DR   UniGene; Mm.24887; -.
DR   HSSP; P44539; 1F6K.
DR   ProteinModelPortal; Q9DCJ9; -.
DR   SMR; Q9DCJ9; 4-306.
DR   STRING; Q9DCJ9; -.
DR   PRIDE; Q9DCJ9; -.
DR   Ensembl; ENSMUST00000041874; ENSMUSP00000037454; ENSMUSG00000042684.
DR   GeneID; 74091; -.
DR   KEGG; mmu:74091; -.
DR   UCSC; uc007dac.1; mouse.
DR   CTD; 74091; -.
DR   MGI; MGI:1921341; Npl.
DR   eggNOG; roNOG09348; -.
DR   GeneTree; ENSGT00530000063604; -.
DR   HOGENOM; HBG714619; -.
DR   HOVERGEN; HBG082055; -.
DR   InParanoid; Q9DCJ9; -.
DR   OMA; GKNKLDQ; -.
DR   OrthoDB; EOG48PMM2; -.
DR   PhylomeDB; Q9DCJ9; -.
DR   BRENDA; 4.1.3.3; 244.
DR   NextBio; 339741; -.
DR   ArrayExpress; Q9DCJ9; -.
DR   Bgee; Q9DCJ9; -.
DR   CleanEx; MM_NPL; -.
DR   Genevestigator; Q9DCJ9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008747; F:N-acetylneuraminate lyase activity; IEA:EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002220; Dihydrodipicolinate_synth.
DR   Gene3D; G3DSA:3.20.20.70; Aldolase_TIM; 1.
DR   PANTHER; PTHR12128; DHDPS; 1.
DR   Pfam; PF00701; DHDPS; 1.
DR   PRINTS; PR00146; DHPICSNTHASE.
DR   PROSITE; PS00665; DHDPS_1; FALSE_NEG.
DR   PROSITE; PS00666; DHDPS_2; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cytoplasm; Lyase; Schiff base.
FT   CHAIN         1    320       N-acetylneuraminate lyase.
FT                                /FTId=PRO_0000273353.
FT   REGION       51     52       Substrate binding (By similarity).
FT   ACT_SITE    173    173       Schiff-base intermediate with substrate
FT                                (By similarity).
FT   SITE        143    143       Involved in proton transfer during
FT                                cleavage (By similarity).
SQ   SEQUENCE   320 AA;  35130 MW;  9426AD7CC8438468 CRC64;
     MAFPKKKLRG LVAATITPMT ENGEINFPVI GQYVDYLVKE QGVKNIFVNG TTGEGLSLSV
     SERRQVAEEW VNQGRNKLDQ VVIHVGALNV KESQELAQHA AEIGADGIAV IAPFFFKSQN
     KDALISFLRE VAAAAPTLPF YYYHMPSMTG VKIRAEELLD GIQDKIPTFQ GLKFTDTDLL
     DFGQCVDQNH QRQFALLFGV DEQLLSALVM GATGAVGSTY NYLGKKTNQM LEAFEQKDLA
     SALSYQFRIQ RFINYVIKLG FGVSQTKAIM TLVSGIPMGP PRLPLQKATQ EFTAKAEAKL
     KSLDFLSSPS VKEGKPLASA
//
ID   IPP2_MOUSE              Reviewed;         206 AA.
AC   Q9DCL8; Q3UD25; Q8C1A6;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Protein phosphatase inhibitor 2;
DE            Short=IPP-2;
GN   Name=Ppp1r2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow, Eye, Kidney, Olfactory bulb, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-123, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-123, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-123, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-123, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122 AND SER-123, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH R.NORVEGICUS
RP   PPP1CC.
RX   PubMed=17636256; DOI=10.1074/jbc.M703472200;
RA   Hurley T.D., Yang J., Zhang L., Goodwin K.D., Zou Q., Cortese M.,
RA   Dunker A.K., DePaoli-Roach A.A.;
RT   "Structural basis for regulation of protein phosphatase 1 by
RT   inhibitor-2.";
RL   J. Biol. Chem. 282:28874-28883(2007).
CC   -!- FUNCTION: Inhibitor of protein-phosphatase 1 (By similarity).
CC   -!- SUBUNIT: Heterodimer with PP1 (By similarity).
CC   -!- PTM: Phosphorylation on Ser-45 by ATM activates PP1 by
CC       dissociating the PP1-PPP1R2 complex (By similarity).
CC       Phosphorylation on Thr-74 by GSK3 activates PP1 by dissociating
CC       the PP1-PPP1R2 complex (By similarity).
CC   -!- SIMILARITY: Belongs to the protein phosphatase inhibitor 2 family.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK002671; BAB22274.1; -; mRNA.
DR   EMBL; AK028603; BAC26028.1; -; mRNA.
DR   EMBL; AK032462; BAC27882.1; -; mRNA.
DR   EMBL; AK053657; BAC35465.1; -; mRNA.
DR   EMBL; AK150281; BAE29437.1; -; mRNA.
DR   EMBL; BC069885; AAH69885.1; -; mRNA.
DR   EMBL; BC069886; AAH69886.1; -; mRNA.
DR   IPI; IPI00322095; -.
DR   RefSeq; NP_080076.1; NM_025800.3.
DR   UniGene; Mm.194477; -.
DR   UniGene; Mm.291593; -.
DR   PDB; 2O8A; X-ray; 2.61 A; I/J=1-206.
DR   PDB; 2O8G; X-ray; 2.50 A; I/J=1-206.
DR   PDBsum; 2O8A; -.
DR   PDBsum; 2O8G; -.
DR   ProteinModelPortal; Q9DCL8; -.
DR   SMR; Q9DCL8; 130-169.
DR   STRING; Q9DCL8; -.
DR   PRIDE; Q9DCL8; -.
DR   Ensembl; ENSMUST00000060188; ENSMUSP00000060118; ENSMUSG00000047714.
DR   GeneID; 66849; -.
DR   KEGG; mmu:66849; -.
DR   UCSC; uc007yxd.1; mouse.
DR   CTD; 66849; -.
DR   MGI; MGI:1914099; Ppp1r2.
DR   eggNOG; roNOG15540; -.
DR   GeneTree; ENSGT00390000004757; -.
DR   HOVERGEN; HBG006170; -.
DR   InParanoid; Q9DCL8; -.
DR   OMA; KIDEPNT; -.
DR   OrthoDB; EOG4PNXJC; -.
DR   PhylomeDB; Q9DCL8; -.
DR   NextBio; 322815; -.
DR   ArrayExpress; Q9DCL8; -.
DR   Bgee; Q9DCL8; -.
DR   Genevestigator; Q9DCL8; -.
DR   GermOnline; ENSMUSG00000047714; Mus musculus.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IEA:InterPro.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR   InterPro; IPR007062; PPI-2.
DR   Pfam; PF04979; IPP-2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Carbohydrate metabolism;
KW   Glycogen metabolism; Phosphoprotein; Protein phosphatase inhibitor.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    206       Protein phosphatase inhibitor 2.
FT                                /FTId=PRO_0000071482.
FT   REGION       12     17       Required for binding PPP1CC.
FT   REGION       44     56       Required for binding the 'RVXF' binding
FT                                groove of PPP1CC.
FT   REGION      148    151       Required for binding PPP1CC catalytic
FT                                center, displacing metal ions and
FT                                inhibition of PPP1CC catyltic activity.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      20     20       Phosphoserine (By similarity).
FT   MOD_RES      45     45       Phosphoserine; by ATM (By similarity).
FT   MOD_RES      74     74       Phosphothreonine; by GSK3 (By
FT                                similarity).
FT   MOD_RES      88     88       Phosphoserine (By similarity).
FT   MOD_RES     122    122       Phosphoserine.
FT   MOD_RES     123    123       Phosphoserine.
FT   CONFLICT    193    193       S -> C (in Ref. 1; BAC26028).
FT   HELIX        50     55
FT   HELIX       134    148
FT   HELIX       151    154
FT   HELIX       155    166
SQ   SEQUENCE   206 AA;  23119 MW;  0AE35744A51A523D CRC64;
     MAASTASHRP IKGILKNKTS AASPPVVPSA EQPRPIVEEE LSKKSQKWDE MNILATYHPA
     DKDYGLMKID EPNTPYHNMI GDDEDAYSDS EGNEVMTPDI LAKKLAAAEG SEPKYRTREQ
     ESSGEEDNDL SPEEREKKRQ FEMKRKLHYN EGLNIKLARQ LISKDLHDDD EDEEMAETAD
     GDSMNVEESS QGSTTSDHLQ HKSQSS
//
ID   S38A3_MOUSE             Reviewed;         505 AA.
AC   Q9DCP2; Q8BS53; Q9JLL8;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Sodium-coupled neutral amino acid transporter 3;
DE   AltName: Full=N-system amino acid transporter 1;
DE   AltName: Full=Na(+)-coupled neutral amino acid transporter 3;
DE   AltName: Full=Solute carrier family 38 member 3;
DE            Short=mNAT;
DE   AltName: Full=System N amino acid transporter 1;
GN   Name=Slc38a3; Synonyms=Sn1, Snat3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Brain, Kidney, and Liver;
RX   MEDLINE=20202617; PubMed=10716701; DOI=10.1073/pnas.050318197;
RA   Gu S., Roderick H.L., Camacho P., Jiang J.X.;
RT   "Identification and characterization of an amino acid transporter
RT   expressed differentially in liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:3230-3235(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-53, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Sodium-dependent amino acid/proton antiporter. Mediates
CC       electrogenic cotransport of glutamine and sodium ions in exchange
CC       for protons. Also recognizes histidine, asparagine and alanine.
CC       May mediate amino acid transport in either direction under
CC       physiological conditions. May play a role in nitrogen metabolism
CC       and synaptic transmission.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in liver, moderately
CC       expressed in kidney and brain, and barely detectable in heart and
CC       muscle. Within liver, expressed in hepatocytes. Not detected in
CC       testis.
CC   -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF159856; AAF61849.1; -; mRNA.
DR   EMBL; AK002607; BAB22226.1; -; mRNA.
DR   EMBL; AK035155; BAC28963.1; -; mRNA.
DR   EMBL; BC054846; AAH54846.1; -; mRNA.
DR   EMBL; BC055339; AAH55339.1; -; mRNA.
DR   IPI; IPI00322156; -.
DR   RefSeq; NP_001186146.1; NM_001199217.1.
DR   RefSeq; NP_001186147.1; NM_001199218.1.
DR   RefSeq; NP_076294.2; NM_023805.3.
DR   UniGene; Mm.296560; -.
DR   ProteinModelPortal; Q9DCP2; -.
DR   STRING; Q9DCP2; -.
DR   TCDB; 2.A.18.6.2; amino acid/auxin permease (AAAP) family.
DR   PRIDE; Q9DCP2; -.
DR   Ensembl; ENSMUST00000010208; ENSMUSP00000010208; ENSMUSG00000010064.
DR   GeneID; 76257; -.
DR   KEGG; mmu:76257; -.
DR   UCSC; uc009rmn.1; mouse.
DR   CTD; 76257; -.
DR   MGI; MGI:1923507; Slc38a3.
DR   eggNOG; roNOG13316; -.
DR   GeneTree; ENSGT00550000074222; -.
DR   HOGENOM; HBG443748; -.
DR   HOVERGEN; HBG059571; -.
DR   InParanoid; Q9DCP2; -.
DR   OMA; TTGNFSH; -.
DR   OrthoDB; EOG4DR9C7; -.
DR   PhylomeDB; Q9DCP2; -.
DR   NextBio; 344865; -.
DR   ArrayExpress; Q9DCP2; -.
DR   Bgee; Q9DCP2; -.
DR   CleanEx; MM_SLC38A3; -.
DR   Genevestigator; Q9DCP2; -.
DR   GermOnline; ENSMUSG00000010064; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; IDA:MGI.
DR   GO; GO:0015297; F:antiporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0015186; F:L-glutamine transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0005290; F:L-histidine transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR013057; AA_transpt_TM.
DR   Pfam; PF01490; Aa_trans; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Antiport; Cell membrane; Glycoprotein;
KW   Ion transport; Membrane; Phosphoprotein; Sodium; Sodium transport;
KW   Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    505       Sodium-coupled neutral amino acid
FT                                transporter 3.
FT                                /FTId=PRO_0000093829.
FT   TRANSMEM     82    102       Helical; (Potential).
FT   TRANSMEM    105    125       Helical; (Potential).
FT   TRANSMEM    143    163       Helical; (Potential).
FT   TRANSMEM    186    206       Helical; (Potential).
FT   TRANSMEM    212    232       Helical; (Potential).
FT   TRANSMEM    288    308       Helical; (Potential).
FT   TRANSMEM    325    345       Helical; (Potential).
FT   TRANSMEM    367    387       Helical; (Potential).
FT   TRANSMEM    409    429       Helical; (Potential).
FT   TRANSMEM    432    452       Helical; (Potential).
FT   TRANSMEM    472    492       Helical; (Potential).
FT   MOD_RES      51     51       Phosphoserine.
FT   MOD_RES      53     53       Phosphoserine.
FT   CARBOHYD     73     73       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    247    247       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    251    251       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    324    324       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    110    110       S -> N (in Ref. 2; BAC28963).
FT   CONFLICT    130    130       Q -> R (in Ref. 2; BAC28963).
FT   CONFLICT    270    270       T -> A (in Ref. 1; AAF61849).
SQ   SEQUENCE   505 AA;  55592 MW;  368DBB87F1BB248A CRC64;
     MEIPRQTEMV ELVPNGKHLE GLLPVGVPTT DTQRTEDTQH CGEGKGFLQK SPSKEPHFTD
     FEGKTSFGMS VFNLSNAIMG SGILGLAYAM ANTGIILFLF LLTAVALLSS YSIHLLLKSS
     GIVGIRAYEQ LGYRAFGTPG KLAAALAITL QNIGAMSSYL YIIKSELPLV IQTFLNLEKP
     ASVWYMDGNY LVILVSVTII LPLALMRQLG YLGYSSGFSL SCMVFFLIAV IYKKFQVPCP
     LAHNLANATG NFSHMVVAEE KAQLQGEPDT AAEAFCTPSY FTLNSQTAYT IPIMAFAFVC
     HPEVLPIYTE LKDPSKRKMQ HISNLSIAVM YVMYFLAALF GYLTFYDGVE SELLHTYSKV
     DPFDVLILCV RVAVLIAVTL TVPIVLFPVR RAIQQMLFQN QEFSWLRHVL IATGLLTCIN
     LLVIFAPNIL GIFGIIGATS APCLIFIFPA IFYFRIMPTD KEPARSTPKI LALCFAAVGF
     LLMTMSLSFI IIDWVSGTSQ HGGNH
//
ID   CP013_MOUSE             Reviewed;         204 AA.
AC   Q9DCS2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=UPF0585 protein C16orf13 homolog;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SIMILARITY: Belongs to the UPF0585 family.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK002535; BAB22171.1; -; mRNA.
DR   EMBL; AK151352; BAE30328.1; -; mRNA.
DR   EMBL; AK170337; BAE41727.1; -; mRNA.
DR   EMBL; BC069266; AAH69266.1; -; mRNA.
DR   IPI; IPI00121271; -.
DR   RefSeq; NP_080962.1; NM_026686.2.
DR   UniGene; Mm.35098; -.
DR   ProteinModelPortal; Q9DCS2; -.
DR   SMR; Q9DCS2; 14-141.
DR   STRING; Q9DCS2; -.
DR   PRIDE; Q9DCS2; -.
DR   Ensembl; ENSMUST00000026827; ENSMUSP00000026827; ENSMUSG00000025731.
DR   GeneID; 68347; -.
DR   KEGG; mmu:68347; -.
DR   UCSC; uc008bcl.1; mouse.
DR   MGI; MGI:1915597; 0610011F06Rik.
DR   eggNOG; roNOG05443; -.
DR   GeneTree; ENSGT00390000010750; -.
DR   HOGENOM; HBG608100; -.
DR   HOVERGEN; HBG060382; -.
DR   InParanoid; Q9DCS2; -.
DR   OMA; NTLHIMS; -.
DR   OrthoDB; EOG447FV9; -.
DR   PhylomeDB; Q9DCS2; -.
DR   NextBio; 327037; -.
DR   ArrayExpress; Q9DCS2; -.
DR   Bgee; Q9DCS2; -.
DR   Genevestigator; Q9DCS2; -.
DR   InterPro; IPR010342; DUF938.
DR   PANTHER; PTHR20974; DUF938; 1.
DR   Pfam; PF06080; DUF938; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein.
FT   CHAIN         1    204       UPF0585 protein C16orf13 homolog.
FT                                /FTId=PRO_0000337115.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     149    149       Phosphoserine.
SQ   SEQUENCE   204 AA;  22687 MW;  494D8B329AD1EAD0 CRC64;
     MMMAAAAERN KEPILSVLRQ YVDPAQRCVR VLEVASGSGQ HAAHFAQAFP NAEWQPSDVD
     QRCLDSIAAT TRAQGLSNVK APLYLDVTWE WEQWGGIPPR SLDLLLCINM IHISPLNCTE
     GLFRAAGHLL KTKAVLITYG PYAVNGKISP QSNVDFDLTL RCRNPEWGLR DTVLLEELGQ
     ASGLVLERMV DMPANNKCLI FRKE
//
ID   NDUBA_MOUSE             Reviewed;         176 AA.
AC   Q9DCS9; Q3UAE3;
DT   27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 10;
DE   AltName: Full=Complex I-PDSW;
DE            Short=CI-PDSW;
DE   AltName: Full=NADH-ubiquinone oxidoreductase PDSW subunit;
GN   Name=Ndufb10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-49; 71-93; 95-109; 128-134 AND 143-153, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Accessory subunit of the mitochondrial membrane
CC       respiratory chain NADH dehydrogenase (Complex I), that is believed
CC       not to be involved in catalysis. Complex I functions in the
CC       transfer of electrons from NADH to the respiratory chain. The
CC       immediate electron acceptor for the enzyme is believed to be
CC       ubiquinone (By similarity).
CC   -!- SUBUNIT: Complex I is composed of 45 different subunits (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein; Matrix side (By similarity).
CC   -!- SIMILARITY: Belongs to the complex I NDUFB10 subunit family.
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DR   EMBL; AK002517; BAB22156.1; -; mRNA.
DR   EMBL; AK151404; BAE30371.1; -; mRNA.
DR   EMBL; BC031664; AAH31664.1; -; mRNA.
DR   EMBL; BC043013; AAH43013.1; -; mRNA.
DR   IPI; IPI00121288; -.
DR   RefSeq; NP_080960.1; NM_026684.2.
DR   UniGene; Mm.1129; -.
DR   STRING; Q9DCS9; -.
DR   TCDB; 3.D.1.6.1; H+ or Na+-translocating NADH dehydrogenase (NDH) family.
DR   PhosphoSite; Q9DCS9; -.
DR   PRIDE; Q9DCS9; -.
DR   Ensembl; ENSMUST00000045602; ENSMUSP00000043543; ENSMUSG00000040048.
DR   GeneID; 68342; -.
DR   KEGG; mmu:68342; -.
DR   UCSC; uc008ayd.1; mouse.
DR   CTD; 68342; -.
DR   MGI; MGI:1915592; Ndufb10.
DR   eggNOG; roNOG04156; -.
DR   GeneTree; ENSGT00390000006348; -.
DR   HOGENOM; HBG269703; -.
DR   HOVERGEN; HBG003196; -.
DR   InParanoid; Q9DCS9; -.
DR   OMA; KDVYPEP; -.
DR   OrthoDB; EOG4907B6; -.
DR   PhylomeDB; Q9DCS9; -.
DR   NextBio; 327025; -.
DR   ArrayExpress; Q9DCS9; -.
DR   Bgee; Q9DCS9; -.
DR   Genevestigator; Q9DCS9; -.
DR   GermOnline; ENSMUSG00000040048; Mus musculus.
DR   GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR019377; NADH_UbQ_OxRdtase_su10.
DR   Pfam; PF10249; NDUFB10; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW   Respiratory chain; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    176       NADH dehydrogenase [ubiquinone] 1 beta
FT                                subcomplex subunit 10.
FT                                /FTId=PRO_0000118831.
FT   MOD_RES      62     62       Phosphotyrosine (By similarity).
FT   MOD_RES     149    149       Phosphotyrosine (By similarity).
SQ   SEQUENCE   176 AA;  21024 MW;  1A3BA32E0F8551C4 CRC64;
     MPDSWDKDVY PEPPSRTPAP SPQTSLPNPI TYLTKAYDLV VDWPVTLVRE FIERQHAKNR
     TYYYHRQYRR VPDITECKEG DVLCIYEAEM QWRRDFKVDQ EIMNIIQERL KACQQREGEN
     YQQNCAKELE QFTKVTKAYQ DRYLDLGAYY SARKCLAKQK QRMLEERKAA RQEAAA
//
ID   ATP5H_MOUSE             Reviewed;         161 AA.
AC   Q9DCX2; B1ASE1; Q542H1; Q7M0I0; Q91YK9;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=ATP synthase subunit d, mitochondrial;
DE            Short=ATPase subunit d;
GN   Name=Atp5h;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RA   Chen H., Huang C.-H.;
RT   "The mouse ATP synthase subunit D interacts with the C-terminal domain
RT   of Rh type C glycoprotein (Rhcg).";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Kidney, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 10-25; 33-73; 86-111; 124-144 AND 149-161, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   PROTEIN SEQUENCE OF 150-161.
RA   Kato H.;
RT   "Analysis of proteins isolated by two dimensional electrophoresis of
RT   mouse neuroblastoma cells.";
RL   Kawasaki Igakkaishi 22:245-259(1996).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-63; LYS-78; LYS-85; LYS-99;
RP   LYS-117 AND LYS-149, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
CC       synthase or Complex V) produces ATP from ADP in the presence of a
CC       proton gradient across the membrane which is generated by electron
CC       transport complexes of the respiratory chain. F-type ATPases
CC       consist of two structural domains, F(1) - containing the
CC       extramembraneous catalytic core, and F(0) - containing the
CC       membrane proton channel, linked together by a central stalk and a
CC       peripheral stalk. During catalysis, ATP synthesis in the catalytic
CC       domain of F(1) is coupled via a rotary mechanism of the central
CC       stalk subunits to proton translocation. Part of the complex F(0)
CC       domain and the peripheric stalk, which acts as a stator to hold
CC       the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static
CC       relative to the rotary elements.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
CC       core - and CF(0) - the membrane proton channel. CF(0) seems to
CC       have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC   -!- SIMILARITY: Belongs to the ATPase d subunit family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF354051; AAL83962.1; -; mRNA.
DR   EMBL; AK002376; BAB22053.1; -; mRNA.
DR   EMBL; AK088617; BAC40456.1; -; mRNA.
DR   EMBL; AL627096; CAM22613.1; -; Genomic_DNA.
DR   EMBL; BC016547; AAH16547.1; -; mRNA.
DR   EMBL; BC081431; AAH81431.1; -; mRNA.
DR   IPI; IPI00230507; -.
DR   PIR; PN0046; PN0046.
DR   RefSeq; NP_082138.1; NM_027862.1.
DR   UniGene; Mm.371641; -.
DR   ProteinModelPortal; Q9DCX2; -.
DR   SMR; Q9DCX2; 4-124.
DR   STRING; Q9DCX2; -.
DR   PhosphoSite; Q9DCX2; -.
DR   REPRODUCTION-2DPAGE; Q9DCX2; -.
DR   PRIDE; Q9DCX2; -.
DR   Ensembl; ENSMUST00000043931; ENSMUSP00000046256; ENSMUSG00000034566.
DR   Ensembl; ENSMUST00000073791; ENSMUSP00000086072; ENSMUSG00000034566.
DR   Ensembl; ENSMUST00000106537; ENSMUSP00000102147; ENSMUSG00000034566.
DR   GeneID; 71679; -.
DR   KEGG; mmu:71679; -.
DR   UCSC; uc007mhm.1; mouse.
DR   CTD; 71679; -.
DR   MGI; MGI:1918929; Atp5h.
DR   eggNOG; roNOG05500; -.
DR   GeneTree; ENSGT00390000003582; -.
DR   HOGENOM; HBG714348; -.
DR   HOVERGEN; HBG050612; -.
DR   InParanoid; Q9DCX2; -.
DR   OMA; EPVDTQT; -.
DR   OrthoDB; EOG4XWG04; -.
DR   PhylomeDB; Q9DCX2; -.
DR   NextBio; 334211; -.
DR   ArrayExpress; Q9DCX2; -.
DR   Bgee; Q9DCX2; -.
DR   Genevestigator; Q9DCX2; -.
DR   GermOnline; ENSMUSG00000034566; Mus musculus.
DR   GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro.
DR   GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR008689; ATPase_F0-cplx_dsu_mt.
DR   Pfam; PF05873; Mt_ATP-synt_D; 1.
DR   PIRSF; PIRSF005514; ATPase_F0_D_mt; 1.
PE   1: Evidence at protein level;
KW   Acetylation; CF(0); Direct protein sequencing; Hydrogen ion transport;
KW   Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    161       ATP synthase subunit d, mitochondrial.
FT                                /FTId=PRO_0000071674.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      63     63       N6-acetyllysine.
FT   MOD_RES      78     78       N6-acetyllysine.
FT   MOD_RES      85     85       N6-acetyllysine.
FT   MOD_RES      95     95       N6-acetyllysine (By similarity).
FT   MOD_RES      99     99       N6-acetyllysine.
FT   MOD_RES     117    117       N6-acetyllysine.
FT   MOD_RES     149    149       N6-acetyllysine.
FT   CONFLICT     90     90       V -> L (in Ref. 4; AAH16547).
FT   CONFLICT    159    161       ENL -> LMC (in Ref. 6; AA sequence).
SQ   SEQUENCE   161 AA;  18749 MW;  380F3C6671D6DB4D CRC64;
     MAGRKLALKT IDWVSFVEVM PQNQKAIGNA LKSWNETFHA RLASLSEKPP AIDWAYYRAN
     VAKPGLVDDF EKKYNALKIP VPEDKYTALV DQEEKEDVKS CAEFVSGSQL RIQEYEKQLE
     KMRNIIPFDQ MTIDDLNEIF PETKLDKKKY PYWPHQPIEN L
//
ID   APOO_MOUSE              Reviewed;         212 AA.
AC   Q9DCZ4; B1ASQ3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   08-MAR-2011, entry version 55.
DE   RecName: Full=Apolipoprotein O;
DE   AltName: Full=Protein FAM121B;
GN   Name=Apoo; Synonyms=Fam121b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the apolipoprotein O family.
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DR   EMBL; AK002320; BAB22011.1; -; mRNA.
DR   EMBL; AL627302; CAM19210.1; -; Genomic_DNA.
DR   IPI; IPI00121576; -.
DR   RefSeq; NP_001186266.1; NM_001199337.1.
DR   UniGene; Mm.379156; -.
DR   PRIDE; Q9DCZ4; -.
DR   Ensembl; ENSMUST00000113897; ENSMUSP00000109530; ENSMUSG00000079508.
DR   GeneID; 68316; -.
DR   UCSC; uc009ttl.1; mouse.
DR   MGI; MGI:1915566; Apoo.
DR   GeneTree; ENSGT00530000063666; -.
DR   HOGENOM; HBG447237; -.
DR   HOVERGEN; HBG059567; -.
DR   InParanoid; Q9DCZ4; -.
DR   OMA; ISHLRHY; -.
DR   ArrayExpress; Q9DCZ4; -.
DR   Bgee; Q9DCZ4; -.
DR   CleanEx; MM_APOO; -.
DR   Genevestigator; Q9DCZ4; -.
DR   GermOnline; ENSMUSG00000049233; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR019166; Apolipoprotein_O.
DR   Pfam; PF09769; ApoO; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    212       Apolipoprotein O.
FT                                /FTId=PRO_0000254647.
FT   TRANSMEM    122    142       Helical; (Potential).
SQ   SEQUENCE   212 AA;  24137 MW;  6DA22AC79F55D787 CRC64;
     MPFWGCGEDE ARSGRCRVIQ RSVGPASLSL LTFRVYAAPK KDSPHKSYMK IDELSLYSVP
     EGQSKYVEEP RTQLEENISQ LRHHCEPYTS FCQEIYSHTK PKVDHFVQWG VDNYNYLQNA
     PPGFFPRLGV IGFAGFVGLL FARGSKIKKL VYPPFFMGLG ASVYYPQQAI TIAQITGEKL
     YDWGLRGYIV IEDLWKQNFQ KPGNVKNSPG NK
//
ID   DTD1_MOUSE              Reviewed;         209 AA.
AC   Q9DD18; A2ANA2; Q3TY44; Q9CRE8; Q9CYL0; Q9D013; Q9D1G4;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 2.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=D-tyrosyl-tRNA(Tyr) deacylase 1;
DE            EC=3.1.-.-;
GN   Name=Dtd1; Synonyms=Hars2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryo, Embryonic stem cell, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N-3; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 11-25, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Hydrolyzes D-tyrosyl-tRNA(Tyr) into D-tyrosine and free
CC       tRNA(Tyr). Could be a defense mechanism against a harmful effect
CC       of D-tyrosine (Potential).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9DD18-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9DD18-2; Sequence=VSP_026130;
CC   -!- SIMILARITY: Belongs to the DTD family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB30808.1; Type=Frameshift; Positions=199;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK003594; BAB22882.1; -; mRNA.
DR   EMBL; AK010822; BAB27205.1; -; mRNA.
DR   EMBL; AK011917; BAB27914.1; -; mRNA.
DR   EMBL; AK017565; BAB30808.1; ALT_FRAME; mRNA.
DR   EMBL; AK158898; BAE34719.1; -; mRNA.
DR   EMBL; AL844516; CAM22364.1; -; Genomic_DNA.
DR   EMBL; AL808119; CAM22364.1; JOINED; Genomic_DNA.
DR   EMBL; AL808119; CAM26713.1; -; Genomic_DNA.
DR   EMBL; AL844516; CAM26713.1; JOINED; Genomic_DNA.
DR   EMBL; BC026537; AAH26537.1; -; mRNA.
DR   IPI; IPI00133713; -.
DR   IPI; IPI00848595; -.
DR   RefSeq; NP_079590.1; NM_025314.3.
DR   UniGene; Mm.28109; -.
DR   ProteinModelPortal; Q9DD18; -.
DR   SMR; Q9DD18; 1-150.
DR   STRING; Q9DD18; -.
DR   PhosphoSite; Q9DD18; -.
DR   PRIDE; Q9DD18; -.
DR   Ensembl; ENSMUST00000028917; ENSMUSP00000028917; ENSMUSG00000027430.
DR   GeneID; 66044; -.
DR   KEGG; mmu:66044; -.
DR   NMPDR; fig|10090.3.peg.7039; -.
DR   UCSC; uc008mro.1; mouse.
DR   CTD; 66044; -.
DR   MGI; MGI:1913294; Dtd1.
DR   eggNOG; roNOG11724; -.
DR   GeneTree; ENSGT00390000008298; -.
DR   HOVERGEN; HBG039436; -.
DR   InParanoid; Q9DD18; -.
DR   OMA; MKAVIQR; -.
DR   OrthoDB; EOG48WC2Z; -.
DR   PhylomeDB; Q9DD18; -.
DR   NextBio; 320458; -.
DR   ArrayExpress; Q9DD18; -.
DR   Bgee; Q9DD18; -.
DR   Genevestigator; Q9DD18; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0019478; P:D-amino acid catabolic process; IEA:InterPro.
DR   InterPro; IPR023509; DTD-like_dom.
DR   InterPro; IPR003732; DTyrtRNA_deacyls.
DR   Gene3D; G3DSA:3.50.80.10; DTyrtRNA_deacyls; 1.
DR   PANTHER; PTHR10472; DTyrtRNA_deacyls; 1.
DR   Pfam; PF02580; Tyr_Deacylase; 1.
DR   SUPFAM; SSF69500; DTyrtRNA_deacyls; 1.
DR   TIGRFAMs; TIGR00256; DTyrtRNA_deacyls; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm;
KW   Direct protein sequencing; Hydrolase; Phosphoprotein.
FT   CHAIN         1    209       D-tyrosyl-tRNA(Tyr) deacylase 1.
FT                                /FTId=PRO_0000164627.
FT   ACT_SITE     81     81       Nucleophile (By similarity).
FT   MOD_RES      65     65       N6-acetyllysine (By similarity).
FT   MOD_RES     194    194       Phosphoserine (By similarity).
FT   MOD_RES     196    196       Phosphoserine.
FT   MOD_RES     197    197       Phosphoserine (By similarity).
FT   MOD_RES     204    204       Phosphoserine (By similarity).
FT   MOD_RES     205    205       Phosphoserine.
FT   VAR_SEQ     199    209       AEGDVSSEREP -> DRG (in isoform 2).
FT                                /FTId=VSP_026130.
FT   CONFLICT     30     30       L -> F (in Ref. 1; BAB27205).
FT   CONFLICT    102    102       A -> T (in Ref. 1; BAB30808).
FT   CONFLICT    145    145       L -> M (in Ref. 1; BAE34719).
SQ   SEQUENCE   209 AA;  23384 MW;  B6FBB1BB090A060F CRC64;
     MKAVVQRVTR ASVTVGGEQI SAIGRGICVL LGISMEDSQK ELEHMVRKIL NLRVFEDESG
     KHWSKSVMDK EYEVLCVSQF TLQCVLKGNK PDFHLAMPTE QAESFYNSFL EQLRKSYRPE
     LIRDGKFGAY MQVHIQNDGP VTIELESPAP GAASSDPKQL SKLEKQQQRK EKTRAKGPSE
     SSKERNAPRK EDRSASSGAE GDVSSEREP
//
ID   TSC1_MOUSE              Reviewed;        1161 AA.
AC   Q9EP53; A2AHW1; Q3UHF2; Q7TS92; Q80U55; Q924U7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 54.
DE   RecName: Full=Hamartin;
DE   AltName: Full=Tuberous sclerosis 1 protein homolog;
GN   Name=Tsc1; Synonyms=Kiaa0243;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX   MEDLINE=21015414; PubMed=11130985; DOI=10.1007/s003350010203;
RA   Cheadle J.P., Dobbie L., Idziaszczyk S., Hodges A.K., Smith A.J.H.,
RA   Sampson J.R., Young J.M.;
RT   "Genomic organization and comparative analysis of the mouse tuberous
RT   sclerosis 1 (Tsc1) locus.";
RL   Mamm. Genome 11:1135-1138(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=129/Sv;
RX   MEDLINE=21352974; PubMed=11438694; DOI=10.1073/pnas.151033798;
RA   Kobayashi T., Minowa O., Sugitani Y., Takai S., Mitani H.,
RA   Kobayashi E., Noda T., Hino O.;
RT   "A germ-line Tsc1 mutation causes tumor development and embryonic
RT   lethality that are similar, but not identical to, those caused by Tsc2
RT   mutation in mice.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:8762-8767(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 489-1161 (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: In complex with TSC2, inhibits the nutrient-mediated or
CC       growth factor-stimulated phosphorylation of S6K1 and EIF4EBP1 by
CC       negatively regulating mTORC1 signaling (By similarity). Implicated
CC       as a tumor suppressor. Involved in microtubule-mediated protein
CC       transport, but this seems to be due to unregulated mTOR signaling
CC       (By similarity).
CC   -!- SUBUNIT: Interacts with TSC2, leading to stabilize TSC2. In the
CC       absence of TSC2, TSC1 self-aggregates. Interacts with DOCK7 (By
CC       similarity). Interacts with TBC1D7 (By similarity).
CC   -!- INTERACTION:
CC       P62137:Ppp1ca; NbExp=1; IntAct=EBI-1202690, EBI-357187;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane;
CC       Peripheral membrane protein (By similarity). Note=At steady state
CC       found in association with membranes (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9EP53-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9EP53-2; Sequence=VSP_037747;
CC       Name=3;
CC         IsoId=Q9EP53-3; Sequence=VSP_037747, VSP_037748;
CC       Name=4;
CC         IsoId=Q9EP53-4; Sequence=VSP_037747, VSP_037749;
CC   -!- DOMAIN: The putative coiled-coil domain is necessary for
CC       interaction with TSC2 (By similarity).
CC   -!- PTM: Phosphorylation at Ser-502 does not affect interaction with
CC       TSC2. Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
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DR   EMBL; AJ271911; CAC20676.1; -; Genomic_DNA.
DR   EMBL; AJ271912; CAC20677.1; -; mRNA.
DR   EMBL; AK147428; BAE27905.1; -; mRNA.
DR   EMBL; AB047561; BAB60810.1; -; mRNA.
DR   EMBL; AL731851; CAM22294.1; -; Genomic_DNA.
DR   EMBL; AL731851; CAM22295.1; -; Genomic_DNA.
DR   EMBL; AL731851; CAM22296.2; -; Genomic_DNA.
DR   EMBL; CH466542; EDL08392.1; -; Genomic_DNA.
DR   EMBL; BC052399; AAH52399.1; -; mRNA.
DR   EMBL; AK122229; BAC65511.1; -; mRNA.
DR   IPI; IPI00109178; -.
DR   IPI; IPI00754969; -.
DR   IPI; IPI00756571; -.
DR   IPI; IPI00943454; -.
DR   RefSeq; NP_075025.2; NM_022887.3.
DR   UniGene; Mm.224354; -.
DR   ProteinModelPortal; Q9EP53; -.
DR   IntAct; Q9EP53; 1.
DR   STRING; Q9EP53; -.
DR   PRIDE; Q9EP53; -.
DR   Ensembl; ENSMUST00000113869; ENSMUSP00000109500; ENSMUSG00000026812.
DR   GeneID; 64930; -.
DR   KEGG; mmu:64930; -.
DR   UCSC; uc008iyw.1; mouse.
DR   CTD; 64930; -.
DR   MGI; MGI:1929183; Tsc1.
DR   GeneTree; ENSGT00390000014148; -.
DR   HOGENOM; HBG445246; -.
DR   InParanoid; Q9EP53; -.
DR   OMA; GFDSPFY; -.
DR   OrthoDB; EOG4S4PFD; -.
DR   PhylomeDB; Q9EP53; -.
DR   ArrayExpress; Q9EP53; -.
DR   Bgee; Q9EP53; -.
DR   Genevestigator; Q9EP53; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR   GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:MGI.
DR   GO; GO:0030030; P:cell projection organization; IMP:MGI.
DR   GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR   GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR   GO; GO:0001822; P:kidney development; IMP:MGI.
DR   GO; GO:0042552; P:myelination; IMP:MGI.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0045792; P:negative regulation of cell size; IMP:MGI.
DR   GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR   GO; GO:0006813; P:potassium ion transport; IGI:MGI.
DR   GO; GO:0045859; P:regulation of protein kinase activity; IGI:MGI.
DR   GO; GO:0050808; P:synapse organization; IMP:MGI.
DR   InterPro; IPR007483; Hamartin.
DR   PANTHER; PTHR15154; Hamartin; 1.
DR   Pfam; PF04388; Hamartin; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Membrane;
KW   Phosphoprotein; Tumor suppressor.
FT   CHAIN         1   1161       Hamartin.
FT                                /FTId=PRO_0000379922.
FT   COILED      721    849       Potential.
FT   COILED      879    917       Potential.
FT   COILED      967    991       Potential.
FT   COMPBIAS    312    315       Poly-Ser.
FT   COMPBIAS    692    695       Poly-Leu.
FT   COMPBIAS   1035   1040       Poly-Ser.
FT   COMPBIAS   1106   1111       Poly-Ser.
FT   MOD_RES     394    394       Phosphoserine.
FT   MOD_RES     502    502       Phosphoserine (By similarity).
FT   MOD_RES     508    508       Phosphoserine (By similarity).
FT   MOD_RES     595    595       Phosphoserine (By similarity).
FT   MOD_RES    1096   1096       Phosphoserine (By similarity).
FT   VAR_SEQ     381    381       Missing (in isoform 2, isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_037747.
FT   VAR_SEQ     678    682       Missing (in isoform 3).
FT                                /FTId=VSP_037748.
FT   VAR_SEQ    1056   1067       Missing (in isoform 4).
FT                                /FTId=VSP_037749.
SQ   SEQUENCE   1161 AA;  128746 MW;  F80ACF8492007801 CRC64;
     MAQLANIGEL LSMLDSSTLG VRDDVTAIFK ESLNSERGPM LVNTLVDYYL ETNSQPVLHI
     LTTLQEPHDK HLLDKINEYV GKAATRLSIL SLLGHVVRLQ PSWKHKLSQA PLLPSLLKCL
     KMDTDVVVLT TGVLVLITML PMIPQSGKQH LLDFFDIFGR LSSWCLKKPG HVTEVYLVHL
     HASVYALFHR LYGMYPCNFV SFLRSHYSMK ENVETFEEVV KPMMEHVRIH PELVTGSKDH
     ELDPRRWKTL ETHDVVIECA KISLDPTEAS YEDGYSVSHQ LSACFPYRSA DVTTSPYVDT
     QNSYGGSTST PSSSSRLMLF SPPGQLPQSL SSPSTRLLPE PLQASLWSPS AVCGMTTPPT
     SPGNVPADLS HPYSKAFGTT AGGKGTPSGT PATSPPPAPP CPQDDCVHGS AAQASATAPR
     KEERADSSRP YLHRQSNDRG LEDPPGSKGS VTLRNLPDFL GDLASEEDSI EKDKEEAAIS
     KELSEITTAE ADPVVPRGGF DSPFYRDSLS GSQRKTHSAA SGTQGSSVNP EPLHSSLDKH
     GPDTPKQAFT PIDPPSGSAD VSPAGDRDRQ TSLETSILTP SPCKIPPQRG VSFGSGQLPP
     YDHLFEVALP KTACHFVSKK TEELLKKVKG NPEEDCVPST SPMEVLDRLI EQGAGAHSKE
     LSRLSLPSKS VDWTHFGGSP PSDELRTLRD QLLLLHNQLL YERFKRQQHA LRNRRLLRKV
     IRAAALEEHN AAMKDQLKLQ EKDIQMWKVS LQKEQARYSQ LQEQRDTMVT QLHSQIRQLQ
     HDREEFYNQS QELQTKLEDC RNMIAELRVE LKKANNKVCH TELLLSQVSQ KLSNSESVQQ
     QMEFLNRQLL VLGEVNELYL EQLQSKHPDT TKEVEMMKTA YRKELEKNRS HLLQQNQRLD
     ASQRRVLELE SLLAKKDHLL LEQKKYLEDV KSQASGQLLA AESRYEAQRK ITRVLELEIL
     DLYGRLEKDG RLRKLEEDRA EAAEAAEERL DCCSDGCTDS LVGHNEEASG HNGETRTSRP
     GGTRASCGGR VTGGSSSSSS ELSTPEKPPS QRFSSRWEPA LGEPSSSIPT TVGSLPSSKS
     FLGMKARELF RNKSESQCDE DSVTMSSSSL SETLKTELGK DSGTENKTSL SLDAPHPSSP
     NSDNVGQLHI MDYNETHPEH S
//
ID   RAI14_MOUSE             Reviewed;         979 AA.
AC   Q9EP71; Q3URT3; Q6ZPT6;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Ankycorbin;
DE   AltName: Full=Ankyrin repeat and coiled-coil structure-containing protein;
DE   AltName: Full=Novel retinal pigment epithelial cell protein;
DE   AltName: Full=Retinoic acid-induced protein 14;
DE   AltName: Full=p125;
GN   Name=Rai14; Synonyms=Kiaa1334, Norpeg;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND LACK OF INTERACTION TO F-ACTIN.
RC   STRAIN=C57BL/6; TISSUE=Kidney;
RX   MEDLINE=21110708; PubMed=11168586;
RX   DOI=10.1046/j.1365-2443.2000.00381.x;
RA   Peng Y.-F., Mandai K., Sakisaka T., Okabe N., Yamamoto Y.,
RA   Yokoyama S., Mizoguchi A., Shiozaki H., Monden M., Takai Y.;
RT   "Ankycorbin: a novel actin cytoskeleton-associated protein.";
RL   Genes Cells 5:1001-1008(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   MEDLINE=21264742; PubMed=11042181; DOI=10.1074/jbc.M007421200;
RA   Kutty R.K., Kutty G., Samuel W., Duncan T., Bridges C.C.,
RA   El-Sherbeeny A., Nagineni C.N., Smith S.B., Wiggert B.;
RT   "Molecular characterization and developmental expression of NORPEG, a
RT   novel gene induced by retinoic acid.";
RL   J. Biol. Chem. 276:2831-2840(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 88-876.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBUNIT: Doesn't bind directly to F-actin.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex (By similarity).
CC       Cytoplasm, cytoskeleton (By similarity). Note=Associated with the
CC       cortical actin cytoskeleton structures in terminal web and cell-
CC       cell adhesion sites and stress fibers.
CC   -!- TISSUE SPECIFICITY: Highly expressed in seminiferous tubules of
CC       testis. Expressed in ganglion cell layer and in Muller cell fibers
CC       of the retina (at protein level). In small intestine highly
CC       expressed at the apical and lateral borders of absorptive
CC       epithelia. In liver highly expressed along the bile canaliculi.
CC   -!- DEVELOPMENTAL STAGE: At 9.5 days, expression is detected in
CC       branchial arch mesenchyme, forebrain, hindbrain, midbrain, and
CC       neural tube. At 12.5 days, is detected in the hindbrain,
CC       forebrain, lung, genital eminence, spinal ligaments around
CC       vertebrae and ribs, and around the cartilage of ribs and nasal
CC       sinuses. Also detected in frontonasal mass, mandibular arch, optic
CC       sulcus, spinal ganglia and hind limb bud. At 15.5 days, expression
CC       is detected in the ventricular layer of neurons subjacent to the
CC       neocortex, around the nasal sinuses, bronchioles of the lung,
CC       kidney, and around the vertebrae of the tail. Also seen in the
CC       olfactory bulb.
CC   -!- SIMILARITY: Contains 7 ANK repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98143.1; Type=Erroneous initiation;
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DR   EMBL; AF202315; AAG24483.1; -; mRNA.
DR   EMBL; AF274866; AAG25937.1; -; mRNA.
DR   EMBL; AK129333; BAC98143.1; ALT_INIT; mRNA.
DR   EMBL; BC052458; AAH52458.1; -; mRNA.
DR   EMBL; AK141233; BAE24605.1; -; mRNA.
DR   IPI; IPI00453820; -.
DR   RefSeq; NP_001159880.1; NM_001166408.1.
DR   RefSeq; NP_109615.1; NM_030690.3.
DR   UniGene; Mm.212395; -.
DR   ProteinModelPortal; Q9EP71; -.
DR   SMR; Q9EP71; 16-241.
DR   IntAct; Q9EP71; 2.
DR   STRING; Q9EP71; -.
DR   PhosphoSite; Q9EP71; -.
DR   PRIDE; Q9EP71; -.
DR   Ensembl; ENSMUST00000090339; ENSMUSP00000087815; ENSMUSG00000022246.
DR   GeneID; 75646; -.
DR   KEGG; mmu:75646; -.
DR   UCSC; uc007vgl.1; mouse.
DR   CTD; 75646; -.
DR   MGI; MGI:1922896; Rai14.
DR   eggNOG; roNOG08477; -.
DR   GeneTree; ENSGT00530000063369; -.
DR   HOGENOM; HBG445266; -.
DR   HOVERGEN; HBG093886; -.
DR   InParanoid; Q9EP71; -.
DR   OMA; KQMKLGL; -.
DR   OrthoDB; EOG49078F; -.
DR   PhylomeDB; Q9EP71; -.
DR   NextBio; 343616; -.
DR   ArrayExpress; Q9EP71; -.
DR   Bgee; Q9EP71; -.
DR   CleanEx; MM_RAI14; -.
DR   Genevestigator; Q9EP71; -.
DR   GermOnline; ENSMUSG00000022246; Mus musculus.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 5.
DR   SMART; SM00248; ANK; 6.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
PE   1: Evidence at protein level;
KW   ANK repeat; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW   Repeat.
FT   CHAIN         1    979       Ankycorbin.
FT                                /FTId=PRO_0000239631.
FT   REPEAT       18     51       ANK 1.
FT   REPEAT       52     81       ANK 2.
FT   REPEAT       85    114       ANK 3.
FT   REPEAT      118    147       ANK 4.
FT   REPEAT      151    180       ANK 5.
FT   REPEAT      184    213       ANK 6.
FT   REPEAT      217    247       ANK 7.
FT   COILED      349    374       Potential.
FT   COILED      430    943       Potential.
FT   MOD_RES     249    249       Phosphothreonine (By similarity).
FT   MOD_RES     260    260       Phosphoserine (By similarity).
FT   MOD_RES     293    293       Phosphoserine (By similarity).
FT   MOD_RES     318    318       Phosphoserine (By similarity).
FT   MOD_RES     358    358       Phosphoserine (By similarity).
FT   CONFLICT    420    420       P -> L (in Ref. 3; BAC98143).
SQ   SEQUENCE   979 AA;  108852 MW;  B2E8C016D80237C4 CRC64;
     MKSLKAKFRK SDTNEWNKND DRLLQAVENG DAEKVASLLG KKGASATKHD SEGKTAFHLA
     AAKGHVECLK VMVTHGVDVT AQDSSGHSAL HVAAKNGHPE CIRKLLQYKS PAENIDNSGK
     TALHYAAAQG CLQAVQLLCE HKSPINLKDL DGNIPLLVAV QNGHSEACHF LLDHGADVNS
     RDKNGRTALM LACETGSSNT VDALIKKGAD LSLVDSLGHN ALHYSKLSEN AGIQNLLLSK
     ISQDADLKTP TKPKQHDQVS KISSERSGTP KKRKAPPPPI SPTQLSDVSS PRSITSTPLS
     GKESVFFAEA PFKAEISSIQ ENKDRLSDST AGADSLLDIS SEADQQDLLV LLQAKVASLT
     LHNKELQDKL QAKSPKDKEA EADLSFQSFH STQTDLAPSP GKASDIPSSD AKSSPPVEHP
     AGTSTTDNDV IIRQLQDSLH DLQKRLESSE AEKKQLQDEL QSQRTDTLCL NNTEISENGS
     DLSQKLKETQ SKYEEAMKEV LSVQKQMKLG LLSQESADGY SHLREAPADE DIDTLKQDLQ
     KAVEESARNK ERVRELETKL AEKEQAEATK PPAEACEELR SSYCSVIENM NKEKAFLFEK
     YQQAQEEIMK LKDTLKSQMP QEAPDDSGDM KEAMNRMIDE LNKQVSELSQ LYREAQAELE
     DYRKRKSLED AAEYIHKAEH ERLMHVSNLS RAKSEEALSE MKSQYSKVLN ELTQLKQLVD
     AHKENSVSIT EHLQVITTLR TTAKEMEEKI SALTGHLANK EAEVAKLEKQ LAEEKAAVSD
     AMVPKSSYEK LQASLESEVN ALATKLKESV REREKAHSEV AQVRSEVSQA RREKDNIQTL
     LKAKEQEVTA LVQKFQRAQE ELAGMRRCSE TSSKLEEDKD EKINEMTREV LKLKEALNSL
     SQLSYSTSSS KRQSQQLDLL QQQVKQLQNQ LAECKKHHQE VISVYRMHLL YAVQGQMDED
     VQKVLKQILT MCKNQSQKK
//
ID   WDR4_MOUSE              Reviewed;         413 AA.
AC   Q9EP82; Q80V01;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 2.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=tRNA (guanine-N(7)-)-methyltransferase subunit WDR4;
DE   AltName: Full=WD repeat-containing protein 4;
GN   Name=Wdr4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20408888; PubMed=10950928; DOI=10.1006/geno.2000.6258;
RA   Michaud J., Kudoh J., Berry A., Bonne-Tamir B., Lalioti M.D.,
RA   Rossier C., Shibuya K., Kawasaki K., Asakawa S., Minoshima S.,
RA   Shimizu N., Antonarakis S.E., Scott H.S.;
RT   "Isolation and characterization of a human chromosome 21q22.3 gene
RT   (WDR4) and its mouse homologue that code for a WD-repeat protein.";
RL   Genomics 68:71-79(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Required for the formation of N(7)-methylguanine at
CC       position 46 (m7G46) in tRNA. In the complex, it is required to
CC       stabilize and induce conformational change of the catalytic
CC       subunit (By similarity).
CC   -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC   -!- SUBUNIT: Forms a complex with METTL1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the WD repeat TRM82 family.
CC   -!- SIMILARITY: Contains 5 WD repeats.
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DR   EMBL; AJ271893; CAC05585.1; -; mRNA.
DR   EMBL; AJ271892; CAC05584.1; -; mRNA.
DR   EMBL; AK144821; BAE26082.1; -; mRNA.
DR   EMBL; AK152271; BAE31087.1; -; mRNA.
DR   EMBL; AK153161; BAE31771.1; -; mRNA.
DR   EMBL; BC039272; AAH39272.1; -; mRNA.
DR   IPI; IPI00109290; -.
DR   RefSeq; NP_067297.2; NM_021322.2.
DR   UniGene; Mm.143771; -.
DR   ProteinModelPortal; Q9EP82; -.
DR   STRING; Q9EP82; -.
DR   PhosphoSite; Q9EP82; -.
DR   PRIDE; Q9EP82; -.
DR   Ensembl; ENSMUST00000024837; ENSMUSP00000024837; ENSMUSG00000024037.
DR   GeneID; 57773; -.
DR   KEGG; mmu:57773; -.
DR   UCSC; uc008bvc.1; mouse.
DR   CTD; 57773; -.
DR   MGI; MGI:1889002; Wdr4.
DR   eggNOG; roNOG08347; -.
DR   GeneTree; ENSGT00390000012174; -.
DR   HOGENOM; HBG447073; -.
DR   HOVERGEN; HBG022880; -.
DR   InParanoid; Q9EP82; -.
DR   OMA; YIFQLDA; -.
DR   OrthoDB; EOG4G1MGZ; -.
DR   PhylomeDB; Q9EP82; -.
DR   NextBio; 313940; -.
DR   ArrayExpress; Q9EP82; -.
DR   Bgee; Q9EP82; -.
DR   CleanEx; MM_WDR4; -.
DR   Genevestigator; Q9EP82; -.
DR   GermOnline; ENSMUSG00000024037; Mus musculus.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 2.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Nucleus; Phosphoprotein; Repeat; tRNA processing;
KW   WD repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    413       tRNA (guanine-N(7)-)-methyltransferase
FT                                subunit WDR4.
FT                                /FTId=PRO_0000051349.
FT   REPEAT       61    100       WD 1.
FT   REPEAT      102    141       WD 2.
FT   REPEAT      145    185       WD 3.
FT   REPEAT      188    228       WD 4.
FT   REPEAT      289    329       WD 5.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     392    392       Phosphoserine.
FT   MOD_RES     412    412       Phosphoserine (By similarity).
FT   CONFLICT     28     28       T -> A (in Ref. 1; CAC05584/CAC05585).
SQ   SEQUENCE   413 AA;  45756 MW;  8EAFB152CFE2884E CRC64;
     MASSAGLALC AQTLVVRGGS RFLAFSTTGS DDDCVFTYDC STAEKKATPE DKGEDGQPAD
     TGSDSILAST FSKSGRYFAL TDDSKRLILF RTKPWQCLSV RMVVRRCTAL TFTASEDRVL
     VADKSGDVYS FSVLEPDGCG RLELGHLSML LDVAVSPDDQ FVLTADRDEK IRVSWAAAPH
     SIESFCLGHT EFVSRILVVP SHPELLLSSS GDGTLRLWEY RSGRQLQCCD LAGLQEPGEQ
     PGHKGLAASR IAFWGQESYV VLLCECVPVV FVFQLDASRQ QLVFRQRLTF PHRVWDVVFE
     EARGLWVLQD CRDAPLVLWR PVGGEWQAAP DGAVSPRLCS HLRESWAMLE GSVGTDDSFR
     SLYKATFDNM TSYLKKKEER LQQQLKKKRQ RSPFPGSPEQ TKKACPGQSA LSC
//
ID   SENP3_MOUSE             Reviewed;         568 AA.
AC   Q9EP97; Q5F2A5; Q8BRD5; Q8C2H5;
DT   28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Sentrin-specific protease 3;
DE            EC=3.4.22.-;
DE   AltName: Full=SUMO-1-specific protease 3;
DE   AltName: Full=Sentrin/SUMO-specific protease SENP3;
DE   AltName: Full=Smt3-specific isopeptidase 1;
DE            Short=Smt3ip1;
GN   Name=Senp3; Synonyms=Smt3ip, Smt3ip1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND FUNCTION.
RC   TISSUE=T-cell lymphoma;
RX   PubMed=11029585; DOI=10.1046/j.1432-1327.2000.01729.x;
RA   Nishida T., Tanaka H., Yasuda H.;
RT   "A novel mammalian Smt3-specific isopeptidase 1 (SMT3IP1) localized in
RT   the nucleolus at interphase.";
RL   Eur. J. Biochem. 267:6423-6427(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20267842; PubMed=10806345; DOI=10.1016/S0378-1119(00)00139-6;
RA   Yeh E.T.H., Gong L., Kamitani T.;
RT   "Ubiquitin-like proteins: new wines in new bottles.";
RL   Gene 248:1-14(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Embryo, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Deconjugates SUMO2 and SUMO3 from CDCA8. Redox sensor
CC       that, when redistributed into nucleoplasm, can act as an effector
CC       to enhance HIF1A transcriptional activity by desumoylating EP300.
CC       Required for rRNA processing through deconjugation of SUMO2 and
CC       SUMO3 from nucleophosmin, NPM1 (By similarity). Protease that
CC       releases SUMO2 and SUMO3 monomers from sumoylated substrates, but
CC       has only weak activity against SUMO1 conjugates. Deconjugates
CC       SUMO2 from MEF2D, which increases its transcriptional activation
CC       capability.
CC   -!- ENZYME REGULATION: On oxidative stress, SENP3 degradation is
CC       blocked by inhibition of its ubiquitination, which stabilizes it
CC       as it accumulates in the nucleoplasm (By similarity).
CC   -!- SUBUNIT: Binds to SUMO1 and SUMO3 (By similarity). Component of
CC       some MLL1/MLL complex, at least composed of the core components
CC       MLL, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative
CC       components C17orf49, CHD8, E2F6, HSP70, IN80C, KIAA1267, LAS1L,
CC       MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2,
CC       RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9
CC       and TEX10. Interacts with EP300, NPM1 and CDCA8 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm.
CC       Note=Redistributes between the nucleolus and the nucleoplasm in
CC       response to mild oxidative stress (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase C48 family.
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DR   EMBL; AF194031; AAG28418.1; -; mRNA.
DR   EMBL; AY008764; AAG33253.1; -; mRNA.
DR   EMBL; AK045071; BAC32209.1; -; mRNA.
DR   EMBL; AK088608; BAC40451.1; -; mRNA.
DR   EMBL; AL603707; CAI51945.1; -; Genomic_DNA.
DR   EMBL; BC037014; AAH37014.1; -; mRNA.
DR   IPI; IPI00109326; -.
DR   RefSeq; NP_001157043.1; NM_001163571.1.
DR   RefSeq; NP_109627.3; NM_030702.4.
DR   UniGene; Mm.284592; -.
DR   UniGene; Mm.422171; -.
DR   ProteinModelPortal; Q9EP97; -.
DR   SMR; Q9EP97; 325-567.
DR   STRING; Q9EP97; -.
DR   MEROPS; C48.003; -.
DR   PhosphoSite; Q9EP97; -.
DR   PRIDE; Q9EP97; -.
DR   Ensembl; ENSMUST00000005336; ENSMUSP00000005336; ENSMUSG00000005204.
DR   Ensembl; ENSMUST00000066760; ENSMUSP00000066581; ENSMUSG00000005204.
DR   GeneID; 80886; -.
DR   KEGG; mmu:80886; -.
DR   UCSC; uc007jrb.1; mouse.
DR   CTD; 80886; -.
DR   MGI; MGI:2158736; Senp3.
DR   eggNOG; roNOG14537; -.
DR   GeneTree; ENSGT00530000062941; -.
DR   HOGENOM; HBG283939; -.
DR   HOVERGEN; HBG059450; -.
DR   InParanoid; Q9EP97; -.
DR   OMA; RRGLAHP; -.
DR   OrthoDB; EOG4RXXZX; -.
DR   PhylomeDB; Q9EP97; -.
DR   NextBio; 350207; -.
DR   ArrayExpress; Q9EP97; -.
DR   Bgee; Q9EP97; -.
DR   CleanEx; MM_SENP3; -.
DR   Genevestigator; Q9EP97; -.
DR   GermOnline; ENSMUSG00000005204; Mus musculus.
DR   GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004843; F:ubiquitin-specific protease activity; IDA:MGI.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR003653; Peptidase_C48.
DR   Pfam; PF02902; Peptidase_C48; 1.
DR   PROSITE; PS50600; ULP_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Nucleus; Phosphoprotein; Protease; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN         1    568       Sentrin-specific protease 3.
FT                                /FTId=PRO_0000101722.
FT   REGION      380    537       Protease.
FT   MOTIF       119    122       Nuclear localization signal (Potential).
FT   MOTIF       147    153       Nuclear localization signal (Potential).
FT   COMPBIAS     13     66       Pro-rich.
FT   COMPBIAS     70     86       Glu-rich.
FT   ACT_SITE    459    459       By similarity.
FT   ACT_SITE    476    476       By similarity.
FT   ACT_SITE    526    526       By similarity.
FT   MOD_RES      71     71       Phosphoserine (By similarity).
FT   MOD_RES      73     73       Phosphoserine (By similarity).
FT   MOD_RES     163    163       Phosphoserine (By similarity).
FT   MOD_RES     170    170       Phosphothreonine (By similarity).
FT   MOD_RES     175    175       Phosphoserine.
FT   MOD_RES     182    182       Phosphoserine (By similarity).
FT   MOD_RES     206    206       Phosphoserine (By similarity).
FT   MOD_RES     226    226       Phosphoserine (By similarity).
FT   MOD_RES     247    247       Phosphoserine (By similarity).
FT   MOD_RES     301    301       Phosphoserine (By similarity).
FT   MOD_RES     347    347       Phosphothreonine (By similarity).
FT   CONFLICT    229    229       D -> G (in Ref. 3; BAC32209).
FT   CONFLICT    440    440       K -> E (in Ref. 3; BAC40451).
SQ   SEQUENCE   568 AA;  64403 MW;  655F1FAB1AB62EA8 CRC64;
     MKETIQGTGS WGPEPPGPGT TYSNPRRERL RWPLPPKPRL KSGGGFGPDP GSGTTVPTRR
     LPAPRPSFDA SASEEEEEEE EEDEEEVAAW RLPPRWGQLG ASQRSRALRP SHRKTCSQRR
     RRAMRAFQML LYSKSTSLTF HWKLWGRHRG RRRNLAHPKN HLSPQEGGAT PQVPSPCCRF
     DSPRGLPPPR LGLLGALMAE DGMRGSPPVP SGPPMEEDGL RWTPKSPLDP DSGLLSCTLP
     NGFGGLSGPE GERSLAPPDA SILISNVCSI GDHVAQELFQ SSDLGIAEEA DRTGEKAGQH
     SPLREEHVTC VQSILDEFLQ TYGSLIPLST DEVVEKLEDI FQQEFSTPSR KSLVLQLIQS
     YQRMPGNAMV RGFRVSYKRH VLTMDDLGTL YGQNWLNDQV MNMYGDLVMD TVPEKVHFFN
     SFFYDKLRTK GYDGVKRWTK NVDIFNKELL LIPIHLEVHW SLISVDVRRR TITYFDSQRT
     LNRRCPKHIA KYLQAEAVKK DRLDFHQGWK GYFKMNVARQ NNDSDCGAFV LQYCKHLALS
     QPFSFTQQDM PKLRRQIYKE LCHCKLTV
//
ID   AT131_MOUSE             Reviewed;        1200 AA.
AC   Q9EPE9;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Probable cation-transporting ATPase 13A1;
DE            Short=CATP;
DE            EC=3.6.3.-;
GN   Name=Atp13a1; Synonyms=Atp13a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Inoue S., Ohta M.;
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-931, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       (TC 3.A.3) family. Type V subfamily.
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DR   EMBL; AB035381; BAB20095.1; -; mRNA.
DR   IPI; IPI00109891; -.
DR   UniGene; Mm.186066; -.
DR   ProteinModelPortal; Q9EPE9; -.
DR   SMR; Q9EPE9; 833-887.
DR   STRING; Q9EPE9; -.
DR   PhosphoSite; Q9EPE9; -.
DR   PRIDE; Q9EPE9; -.
DR   Ensembl; ENSMUST00000034326; ENSMUSP00000034326; ENSMUSG00000031862.
DR   UCSC; uc009lxr.1; mouse.
DR   MGI; MGI:2180801; Atp13a1.
DR   GeneTree; ENSGT00550000075064; -.
DR   HOGENOM; HBG316596; -.
DR   HOVERGEN; HBG050602; -.
DR   InParanoid; Q9EPE9; -.
DR   PhylomeDB; Q9EPE9; -.
DR   NextBio; 370358; -.
DR   ArrayExpress; Q9EPE9; -.
DR   Bgee; Q9EPE9; -.
DR   CleanEx; MM_ATP13A1; -.
DR   Genevestigator; Q9EPE9; -.
DR   GermOnline; ENSMUSG00000031862; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015662; F:ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   GO; GO:0006812; P:cation transport; IEA:InterPro.
DR   InterPro; IPR023306; ATPase_cation_domN.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR023300; ATPase_P-typ_cyto_domA.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR006544; ATPase_P-typ_unknown-pump-sp.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Gene3D; G3DSA:2.70.150.10; ATPase_P-typ_cyto_domA; 1.
DR   Gene3D; G3DSA:3.40.1110.10; ATPase_P-typ_cyto_domN; 1.
DR   Gene3D; G3DSA:3.40.50.1000; HAD-like_dom; 2.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SUPFAM; SSF81660; ATPase_cation_domN; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR   TIGRFAMs; TIGR01657; P-ATPase-V; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Glycoprotein; Hydrolase; Magnesium; Membrane;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   1200       Probable cation-transporting ATPase 13A1.
FT                                /FTId=PRO_0000046422.
FT   TOPO_DOM      1     63       Cytoplasmic (Potential).
FT   TRANSMEM     64     84       Helical; (Potential).
FT   TOPO_DOM     85     92       Extracellular (Potential).
FT   TRANSMEM     93    113       Helical; (Potential).
FT   TOPO_DOM    114    240       Cytoplasmic (Potential).
FT   TRANSMEM    241    261       Helical; (Potential).
FT   TOPO_DOM    262    440       Extracellular (Potential).
FT   TRANSMEM    441    461       Helical; (Potential).
FT   TOPO_DOM    462    985       Cytoplasmic (Potential).
FT   TRANSMEM    986   1006       Helical; (Potential).
FT   TOPO_DOM   1007   1007       Extracellular (Potential).
FT   TRANSMEM   1008   1028       Helical; (Potential).
FT   TOPO_DOM   1029   1047       Cytoplasmic (Potential).
FT   TRANSMEM   1048   1068       Helical; (Potential).
FT   TOPO_DOM   1069   1092       Extracellular (Potential).
FT   TRANSMEM   1093   1113       Helical; (Potential).
FT   TOPO_DOM   1114   1128       Cytoplasmic (Potential).
FT   TRANSMEM   1129   1149       Helical; (Potential).
FT   TOPO_DOM   1150   1162       Extracellular (Potential).
FT   TRANSMEM   1163   1183       Helical; (Potential).
FT   TOPO_DOM   1184   1200       Cytoplasmic (Potential).
FT   ACT_SITE    530    530       4-aspartylphosphate intermediate (By
FT                                similarity).
FT   METAL       861    861       Magnesium (By similarity).
FT   METAL       865    865       Magnesium (By similarity).
FT   MOD_RES     896    896       Phosphoserine (By similarity).
FT   MOD_RES     931    931       Phosphoserine.
FT   CARBOHYD    284    284       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    417    417       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   1200 AA;  132378 MW;  A69C366D632C6D74 CRC64;
     MAVVGNAVPC GARPGGARDN GSPQPGSRLR PGLAAGPALI ANGDELVAAV WPYRRLALLR
     RLTVLPFAGL LYPAWLGAAA SGCWGWGSSW TQIPEAALLA LATICLAHAL TVLSGHWSVH
     AHCALTCTPE YDPNKVTFVK VVPTPNNGST ELVALHRDKG EDGLEVLSFE FQKIKYSYDA
     LEKKQFLSVA FPVGNAFSYY QSNRGFQEDS EIRAAEKKFG SNKAEMVVPD FSELFKERAT
     APFFVFQVFC VGLWCLDEYW YYSVFTLSML VAFEASLVQQ QMRNMSEIRK MGNKPHMIQV
     YRSRKWRPVA SDDIVPGDIV SIGRSPQENL VPCDVLLLRG RCIVDEAMLT GESVPQMKEP
     IEDLSPDRVL DLQADARLHV IFGGTKVVQH IPPQKATSGL KPVDNGCVAF VLRTGFNTSQ
     GRLLRTILFG VKRVTANNLE TFIFILFLLV FAIAAAAYVW VEGTKDPSRN RYKLFLECTL
     ILTSVVPPEL PIELSLAVNT SLIALAKLYM YCTEPFRIPF AGKVEVCCFD KTGTLTSDSL
     VVRGVAGLRD GKEVTPVSSI PIETHRALAS CHSLMQLDDG TLVGDPLEKA MLTAVDWTLT
     KDEKVFPRSI KTQGLKIHQR FHFASALKRM SVLASYEKLG STDLCYIAAV KGAPETLHSM
     FSQCPPDYHH IHTEISREGA RVLALGYKEL GHLTHQQARE IKREALECSL KFVGFIVVSC
     PLKADSKAVI REIQNASHRV VMITGDNPLT ACHVAQELHF IDKAHTLILH PPSEKGQPCE
     WRSIDSSIVL PLTLGSPKAL ALEHALCLTG DGLAHLQAVD PQQLLCLIPH VQVFARVAPK
     QKEFVITSLK ELGYVTLMCG DGTNDVGALK HADVGVALLA NAPERVVERR RRPRDSPVLS
     NSGPRVSRST KQKSALLSPE EPPASHRDRL SQVLRDLEEE STPIVKLGDA SIAAPFTSKL
     SSIQCICHVI KQGRCTLVTT LQMFKILALN ALILAYSQSV LYLEGVKFSD FQATLQGLLL
     AGCFLFISRS KPLKTLSRER PLPNIFNLYT ILTVMLQFSV HFLSLVYLYR EAQARSPEKQ
     EQFVDLYKEF EPSLVNSTVY IMAMAMQMAT FAINYKGPPF MESLPENKPL VWSLAVSLLA
     IIGLLLGSSP DFNSQFGLVD IPVEFKLVIG QVLALDFCLA LLADRVLQFF LGTPKLRVPS
//
ID   ARFG1_MOUSE             Reviewed;         414 AA.
AC   Q9EPJ9; A8WIR9; A8WIS1; Q3TI52; Q8BMM6; Q8BMQ7;
DT   27-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=ADP-ribosylation factor GTPase-activating protein 1;
DE            Short=ARF GAP 1;
DE   AltName: Full=ADP-ribosylation factor 1 GTPase-activating protein;
DE            Short=ARF1 GAP;
DE   AltName: Full=ARF1-directed GTPase-activating protein;
GN   Name=Arfgap1; Synonyms=Arf1gap;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Venkateswarlu K.;
RT   "Cloning and functional characterisation of mouse ARF1GAP.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Ovary, Pituitary, Placenta, and Uterus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135; SER-342; SER-344
RP   AND SER-347, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: GTPase-activating protein (GAP) for the ADP ribosylation
CC       factor 1 (ARF1). Involved in membrane trafficking and /or vesicle
CC       transport. Promotes hydrolysis of the ARF1-bound GTP and thus, is
CC       required for the dissociation of coat proteins from Golgi-derived
CC       membranes and vesicles, a prerequisite for vesicle's fusion with
CC       target compartment. Probably regulates ARF1-mediated transport via
CC       its interaction with the KDELR proteins and RNP24. Overexpression
CC       induces the redistribution of the entire Golgi complex to the
CC       endoplasmic reticulum, as when ARF1 is deactivated. Its activity
CC       is stimulated by phosphoinosides and inhibited by
CC       phosphatidylcholine (By similarity).
CC   -!- SUBUNIT: Interacts with ARF1. Interacts with the COPI coat
CC       proteins, KDELR1 and RNP24. It is probably a component of the COPI
CC       coat protein complex. The interaction with RNP24 inhibits the GAP
CC       activity (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus
CC       (By similarity). Note=Associates with the Golgi complex (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9EPJ9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9EPJ9-2; Sequence=VSP_011303;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The region downstream of Arf-GAP domain is essential to
CC       GAP activity in vivo. This region may be required for its
CC       targeting to Golgi membranes (By similarity).
CC   -!- SIMILARITY: Contains 1 Arf-GAP domain.
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DR   EMBL; AJ401461; CAC18721.1; -; mRNA.
DR   EMBL; AK030295; BAC26883.1; -; mRNA.
DR   EMBL; AK030520; BAC27002.1; -; mRNA.
DR   EMBL; AK145879; BAE26720.1; -; mRNA.
DR   EMBL; AK168007; BAE39994.1; -; mRNA.
DR   EMBL; BX649560; CAM23227.1; -; Genomic_DNA.
DR   EMBL; BX649560; CAM23229.1; -; Genomic_DNA.
DR   IPI; IPI00387227; -.
DR   IPI; IPI00403723; -.
DR   RefSeq; NP_001171177.1; NM_001177706.1.
DR   RefSeq; NP_001171178.1; NM_001177707.1.
DR   RefSeq; NP_001171179.1; NM_001177708.1.
DR   RefSeq; NP_001171180.1; NM_001177709.1.
DR   RefSeq; NP_665703.2; NM_145760.3.
DR   UniGene; Mm.33765; -.
DR   ProteinModelPortal; Q9EPJ9; -.
DR   SMR; Q9EPJ9; 1-152.
DR   STRING; Q9EPJ9; -.
DR   PhosphoSite; Q9EPJ9; -.
DR   PRIDE; Q9EPJ9; -.
DR   Ensembl; ENSMUST00000029092; ENSMUSP00000029092; ENSMUSG00000027575.
DR   GeneID; 228998; -.
DR   KEGG; mmu:228998; -.
DR   UCSC; uc008okj.1; mouse.
DR   UCSC; uc008okm.1; mouse.
DR   CTD; 228998; -.
DR   MGI; MGI:2183559; Arfgap1.
DR   GeneTree; ENSGT00550000075077; -.
DR   HOGENOM; HBG713165; -.
DR   HOVERGEN; HBG050562; -.
DR   InParanoid; Q9EPJ9; -.
DR   OMA; QASQKFW; -.
DR   OrthoDB; EOG4M65HQ; -.
DR   PhylomeDB; Q9EPJ9; -.
DR   NextBio; 379297; -.
DR   ArrayExpress; Q9EPJ9; -.
DR   Bgee; Q9EPJ9; -.
DR   Genevestigator; Q9EPJ9; -.
DR   GermOnline; ENSMUSG00000027575; Mus musculus.
DR   GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001164; ArfGAP.
DR   Pfam; PF01412; ArfGap; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00105; ArfGap; 1.
DR   SUPFAM; SSF57863; ArfGAP; 1.
DR   PROSITE; PS50115; ARFGAP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; ER-Golgi transport;
KW   Golgi apparatus; GTPase activation; Metal-binding; Phosphoprotein;
KW   Protein transport; Transport; Zinc; Zinc-finger.
FT   CHAIN         1    414       ADP-ribosylation factor GTPase-activating
FT                                protein 1.
FT                                /FTId=PRO_0000074191.
FT   DOMAIN        7    124       Arf-GAP.
FT   ZN_FING      22     45       C4-type.
FT   MOD_RES     135    135       Phosphothreonine.
FT   MOD_RES     189    189       Phosphothreonine (By similarity).
FT   MOD_RES     231    231       N6-acetyllysine (By similarity).
FT   MOD_RES     246    246       Phosphoserine (By similarity).
FT   MOD_RES     342    342       Phosphoserine.
FT   MOD_RES     344    344       Phosphoserine.
FT   MOD_RES     347    347       Phosphoserine.
FT   MOD_RES     360    360       Phosphoserine.
FT   VAR_SEQ     259    280       Missing (in isoform 2).
FT                                /FTId=VSP_011303.
FT   CONFLICT    112    112       R -> K (in Ref. 1; CAC18721).
FT   CONFLICT    188    188       N -> K (in Ref. 1; CAC18721).
SQ   SEQUENCE   414 AA;  45288 MW;  72A3279D185714C0 CRC64;
     MASPRTRKVL KEVRAQDENN VCFECGAFNP QWVSVTYGIW ICLECSGRHR GLGVHLSFVR
     SVTMDKWKDI ELEKMKAGGN AKFREFLETQ DDYEPSWSLQ DKYSSRAAAL FRDKVATLAE
     GKEWSLESSP AQNWTPPQPK TLQFTAHRAS GQPQSAAASG DKAFEDWLND DLGSYQGAQE
     NRYVGFGNTV PPQKREDDFL NNAMSSLYSG WSSFTTGASK FASAAKEGAT KFGSQASQKA
     SELGHSLNEN VLKPAQEKVK EGRIFDDVSS GVSQLASKVQ GVGSKGWRDV TTFFSGKAED
     SSDRPLEGHS YQNSSGDNSQ NSNIDQSFWE TFGSAEPPKA KSPSSDSWTC ADASTGRRSS
     DSWDVWGSGS ASNNKNSNSD GWESWEGASG EGRAKATKKA APSTADEGWD NQNW
//
ID   ACOX3_MOUSE             Reviewed;         700 AA.
AC   Q9EPL9; Q7TPP6; Q80UQ0;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Peroxisomal acyl-coenzyme A oxidase 3;
DE            EC=1.3.3.6;
DE   AltName: Full=Branched-chain acyl-CoA oxidase;
DE            Short=BRCACox;
DE   AltName: Full=Pristanoyl-CoA oxidase;
GN   Name=Acox3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Van Veldhoven P.P., Ghys K.;
RT   "Cloning of the mouse pristanoyl-CoA oxidase.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N, and FVB/N-3; TISSUE=Liver, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Oxidizes the CoA-esters of 2-methyl-branched fatty acids
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + O(2) = trans-2,3-dehydroacyl-CoA +
CC       H(2)O(2).
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- PATHWAY: Lipid metabolism; peroxisomal fatty acid beta-oxidation.
CC   -!- SUBCELLULAR LOCATION: Peroxisome (Potential).
CC   -!- SIMILARITY: Belongs to the acyl-CoA oxidase family.
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DR   EMBL; AJ278430; CAC20692.1; -; mRNA.
DR   EMBL; BC044725; AAH44725.1; -; mRNA.
DR   EMBL; BC055019; AAH55019.1; -; mRNA.
DR   IPI; IPI00318108; -.
DR   RefSeq; NP_109646.2; NM_030721.2.
DR   UniGene; Mm.291503; -.
DR   ProteinModelPortal; Q9EPL9; -.
DR   SMR; Q9EPL9; 20-689.
DR   STRING; Q9EPL9; -.
DR   PhosphoSite; Q9EPL9; -.
DR   PRIDE; Q9EPL9; -.
DR   Ensembl; ENSMUST00000068947; ENSMUSP00000063412; ENSMUSG00000029098.
DR   Ensembl; ENSMUST00000114237; ENSMUSP00000109875; ENSMUSG00000029098.
DR   GeneID; 80911; -.
DR   KEGG; mmu:80911; -.
DR   CTD; 80911; -.
DR   MGI; MGI:1933156; Acox3.
DR   GeneTree; ENSGT00530000062919; -.
DR   HOVERGEN; HBG101107; -.
DR   OrthoDB; EOG4B8JCR; -.
DR   PhylomeDB; Q9EPL9; -.
DR   BRENDA; 1.3.3.6; 244.
DR   NextBio; 350282; -.
DR   ArrayExpress; Q9EPL9; -.
DR   Bgee; Q9EPL9; -.
DR   CleanEx; MM_ACOX3; -.
DR   Genevestigator; Q9EPL9; -.
DR   GermOnline; ENSMUSG00000029098; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005782; C:peroxisomal matrix; TAS:MGI.
DR   GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016402; F:pristanoyl-CoA oxidase activity; TAS:MGI.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; TAS:MGI.
DR   InterPro; IPR006090; Acyl-CoA_Oxase/DH_1.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
DR   InterPro; IPR012258; Acyl-CoA_oxidase.
DR   InterPro; IPR002655; Acyl-CoA_oxidase_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase.
DR   Gene3D; G3DSA:2.40.110.10; Acyl_CoA_DH/ox_M; 1.
DR   Gene3D; G3DSA:1.20.140.10; AcylCoA_DH_1/2_C; 2.
DR   Pfam; PF01756; ACOX; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   PIRSF; PIRSF000168; Acyl-CoA_oxidase; 1.
DR   SUPFAM; SSF56645; AcylCoA_dehyd_NM; 1.
DR   SUPFAM; SSF47203; AcylCoADH_C_like; 2.
PE   2: Evidence at transcript level;
KW   FAD; Fatty acid metabolism; Flavoprotein; Lipid metabolism;
KW   Oxidoreductase; Peroxisome; Phosphoprotein.
FT   CHAIN         1    700       Peroxisomal acyl-coenzyme A oxidase 3.
FT                                /FTId=PRO_0000204686.
FT   MOTIF       698    700       Microbody targeting signal (By
FT                                similarity).
FT   MOD_RES     281    281       Phosphothreonine (By similarity).
FT   CONFLICT    177    178       DP -> ES (in Ref. 1; CAC20692).
FT   CONFLICT    364    364       Y -> H (in Ref. 1; CAC20692).
FT   CONFLICT    408    409       KP -> NR (in Ref. 1; CAC20692).
FT   CONFLICT    555    555       C -> V (in Ref. 1; CAC20692).
FT   CONFLICT    576    576       H -> Y (in Ref. 2; AAH44725).
FT   CONFLICT    593    594       TL -> SV (in Ref. 1; CAC20692).
FT   CONFLICT    607    607       L -> S (in Ref. 1; CAC20692).
FT   CONFLICT    669    669       A -> R (in Ref. 1; CAC20692).
FT   CONFLICT    681    681       A -> R (in Ref. 1; CAC20692).
SQ   SEQUENCE   700 AA;  78404 MW;  85C448E38A4A0C67 CRC64;
     MGSLPEEKDS ALWSDTPKGP LSAYRARASF NSGELLLFWD GQDVIHFKKT IFSTLENDPL
     FARSYGADLP LEKLRELNFL RCKRVFEYGF FKVEELLKNP LKILVLINCL GMYDWSLANK
     CVLHMLVFGT TVFVSGSEKH FKYLEKIYSL EIFGCFALTE LSHGSNTKAM RTTAHYDPDT
     QEFILHSPDF EAAKFWVGNL GKTATHAVVF AQLYMPDGQC HGLHSFLVQI RDTKTLLPMT
     GVMVGDIGKK LGQNGLDNGF AMFNKVRIPR QNLLDRTGNI TSEGTYNSPF KDVRQRLGAS
     LGSLSSGRIS IISMSVVNLK LAVSIAIRFS ATRCQFGPTD KEEIPVLEYP LQQWRILPYL
     AAAYALDHFS KTIFMDLIEV QSARLRGDHS DQQAELGREI HALASAGKPL ASWTAQRGIQ
     ECREACGGHG YLAMNRFGDL RNDNDPNCTY EGDNNVLLQQ TSNYLLSLLE PPLQDGAHFT
     SPLKTVDFLE AYPGILGQKF LGSSKADWMD SAAPLAAYRW LVCYLLQESH RRYCQEKKSR
     GSDFEARNNS QVYGCRPLAL AFMELTVMQR FHEHIHSSGL SPSLRTVLGR LSTLYGLWCL
     SQHMALLYRG GYISGEQTGR AMEDAILTLC EQLKDDAVAL VDVIAPSDFV LNSPIAKADG
     ELYKNLWAAV LQQNGVLERA AWWPEFSANK SVADRLKSQL
//
ID   NBEA_MOUSE              Reviewed;        2936 AA.
AC   Q9EPN1; Q8C931; Q9EPM9; Q9EPN0; Q9WVM9;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Neurobeachin;
DE   AltName: Full=Lysosomal-trafficking regulator 2;
GN   Name=Nbea; Synonyms=Lyst2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), FUNCTION,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Brain;
RX   MEDLINE=20556611; PubMed=11102458;
RA   Wang X., Herberg F.W., Laue M.M., Wullner C., Hu B.,
RA   Petrasch-Parwez E., Kilimann M.W.;
RT   "Neurobeachin: a protein kinase A-anchoring, beige/Chediak-Higashi
RT   protein homolog implicated in neuronal membrane traffic.";
RL   J. Neurosci. 20:8551-8565(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC   TISSUE=Brain;
RX   MEDLINE=22150869; PubMed=12160729; DOI=10.1006/geno.2002.6822;
RA   Dyomin V.G., Chaganti S.R., Dyomina K., Palanisamy N., Murty V.V.V.S.,
RA   Dalla-Favera R., Chaganti R.S.K.;
RT   "BCL8 is a novel, evolutionarily conserved human gene family encoding
RT   proteins with presumptive protein kinase A anchoring function.";
RL   Genomics 80:158-165(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2220-2936.
RA   Tchernev V.T., McMurtrie E.B., Nguyen Q.A., Mishra V.S.,
RA   Barbosa M.D.F.S., McIndoe R., Kingsmore S.F.;
RT   "Identification of LYST2, a brain-specific member of the Chediak-
RT   Higashi syndrome gene family.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1519, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Binds to type II regulatory subunits of protein kinase A
CC       and anchors/targets them to the membrane. May anchor the kinase to
CC       cytoskeletal and/or organelle-associated proteins. May have a role
CC       in membrane trafficking.
CC   -!- SUBUNIT: Interacts with RII subunit of PKA.
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC       Endomembrane system; Peripheral membrane protein. Cell junction,
CC       synapse, postsynaptic cell membrane; Peripheral membrane protein.
CC       Note=Associated with pleomorphic tubulovesicular endomembranes
CC       near the trans sides of Golgi stacks and throughout the cell
CC       bodies and cell processes. Concentrated at the postsynaptic plasma
CC       membrane of a subpopulation of synapses.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9EPN1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9EPN1-2; Sequence=VSP_050540;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q9EPN1-3; Sequence=VSP_050541;
CC       Name=4;
CC         IsoId=Q9EPN1-4; Sequence=VSP_050542;
CC   -!- TISSUE SPECIFICITY: Forebrain, brainstem and cerebellum.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in neonatal brain, levels
CC       decline in adults.
CC   -!- DOMAIN: RII-alpha binding site, predicted to form an amphipathic
CC       helix, could participate in protein-protein interactions with a
CC       complementary surface on the R-subunit dimer.
CC   -!- SIMILARITY: Belongs to the WD repeat neurobeachin family.
CC   -!- SIMILARITY: Contains 1 BEACH domain.
CC   -!- SIMILARITY: Contains 5 WD repeats.
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DR   EMBL; Y18276; CAC18811.1; -; mRNA.
DR   EMBL; Y18276; CAC18812.1; -; mRNA.
DR   EMBL; Y18276; CAC18813.1; -; mRNA.
DR   EMBL; AK043125; BAC31466.1; -; mRNA.
DR   EMBL; AF072372; AAD41634.1; -; mRNA.
DR   IPI; IPI00320831; -.
DR   IPI; IPI00320836; -.
DR   IPI; IPI00421047; -.
DR   IPI; IPI00469204; -.
DR   RefSeq; NP_085098.1; NM_030595.1.
DR   UniGene; Mm.384353; -.
DR   ProteinModelPortal; Q9EPN1; -.
DR   SMR; Q9EPN1; 1923-1949, 2140-2553, 2671-2923.
DR   STRING; Q9EPN1; -.
DR   PhosphoSite; Q9EPN1; -.
DR   PRIDE; Q9EPN1; -.
DR   Ensembl; ENSMUST00000029374; ENSMUSP00000029374; ENSMUSG00000027799.
DR   Ensembl; ENSMUST00000107943; ENSMUSP00000103576; ENSMUSG00000027799.
DR   Ensembl; ENSMUST00000107951; ENSMUSP00000103585; ENSMUSG00000027799.
DR   GeneID; 26422; -.
DR   KEGG; mmu:26422; -.
DR   UCSC; uc008pgt.1; mouse.
DR   CTD; 26422; -.
DR   MGI; MGI:1347075; Nbea.
DR   GeneTree; ENSGT00600000084267; -.
DR   HOGENOM; HBG381680; -.
DR   HOVERGEN; HBG012582; -.
DR   InParanoid; Q9EPN1; -.
DR   OMA; XRKVEIM; -.
DR   OrthoDB; EOG4TXBQZ; -.
DR   NextBio; 304447; -.
DR   ArrayExpress; Q9EPN1; -.
DR   Bgee; Q9EPN1; -.
DR   CleanEx; MM_NBEA; -.
DR   Genevestigator; Q9EPN1; -.
DR   GermOnline; ENSMUSG00000027799; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0012505; C:endomembrane system; IDA:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; NAS:UniProtKB.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR   GO; GO:0051018; F:protein kinase A binding; NAS:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; IDA:MGI.
DR   GO; GO:0006892; P:post-Golgi vesicle-mediated transport; NAS:UniProtKB.
DR   GO; GO:0008104; P:protein localization; IDA:MGI.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000409; Beige_BEACH.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   InterPro; IPR010508; DUF1088.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 3.
DR   Gene3D; G3DSA:1.10.1540.10; Beige_BEACH; 1.
DR   Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 1.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF02138; Beach; 1.
DR   Pfam; PF06469; DUF1088; 1.
DR   Pfam; PF00400; WD40; 2.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF81837; Beige_BEACH; 1.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS50197; BEACH; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Membrane;
KW   Phosphoprotein; Postsynaptic cell membrane; Repeat; Synapse;
KW   WD repeat.
FT   CHAIN         1   2936       Neurobeachin.
FT                                /FTId=PRO_0000051090.
FT   REPEAT     1316   1358       WD 1.
FT   DOMAIN     2264   2553       BEACH.
FT   REPEAT     2708   2751       WD 2.
FT   REPEAT     2768   2808       WD 3.
FT   REPEAT     2850   2889       WD 4.
FT   REPEAT     2892   2931       WD 5.
FT   MOD_RES    1519   1519       Phosphoserine.
FT   VAR_SEQ       1   2197       Missing (in isoform 2).
FT                                /FTId=VSP_050540.
FT   VAR_SEQ    1601   1632       Missing (in isoform 3).
FT                                /FTId=VSP_050541.
FT   VAR_SEQ    2560   2564       Missing (in isoform 4).
FT                                /FTId=VSP_050542.
FT   CONFLICT   2220   2221       FM -> SR (in Ref. 2).
FT   CONFLICT   2332   2332       D -> H (in Ref. 2; AAD41634).
FT   CONFLICT   2337   2337       I -> K (in Ref. 2; AAD41634).
FT   CONFLICT   2375   2375       A -> P (in Ref. 2; AAD41634).
FT   CONFLICT   2431   2431       L -> V (in Ref. 2; AAD41634).
FT   CONFLICT   2532   2532       E -> V (in Ref. 2; AAD41634).
FT   CONFLICT   2539   2539       G -> A (in Ref. 2; AAD41634).
FT   CONFLICT   2554   2554       S -> T (in Ref. 2; AAD41634).
FT   CONFLICT   2561   2561       F -> S (in Ref. 2; AAD41634).
FT   CONFLICT   2802   2802       D -> N (in Ref. 2; AAD41634).
FT   CONFLICT   2805   2805       R -> K (in Ref. 2; AAD41634).
FT   CONFLICT   2920   2936       AFNIDFNRWHYEHQNRY -> LLI (in Ref. 2;
FT                                AAD41634).
SQ   SEQUENCE   2936 AA;  326743 MW;  A6CFD90CA666CEA4 CRC64;
     MASDKPGPGL EPQPVALLAV GAGGGAGGGG AMGEPRGAAG SGPVVLPAGM INPSVPIRNI
     RMKFAVLIGL IQVGEVSNRD IVETVLNLLV GGEFDLEMNF IIQDAESITC MTELLEHCDV
     TCQAEIWSMF TAILRKSVRN LQTSTEVGLI EQVLLKMSAV DDMIADLLVD MLGVLASYSI
     TVKELKLLFS MLRGESGIWP RHAVKLLSVL NQMPQRHGPD TFFNFPGCSA AAIALPPIAK
     WPYQNGFTLN TWFRMDPLNN INVDKDKPYL YCFRTSKGVG YSAHFVGNCL IVTSLKSKGK
     GFQHCVKYDF QPRKWYMISI VHIYNRWRNS EIRCYVNGQL VSYGDMAWHV NTNDSYDKCF
     LGSSETADAN RVFCGQLGAV YVFSEALNPA QIFAVHQLGP GYKSTFKFKS ESDIHLAEHH
     KQVLYDGKLA SSIAFSYNAK ATDAQLCLES SPKENASIFV HSPHALMLQD VKAIVTHSIH
     SAIHSIGGIQ VLFPLFAQLD NRQLNDSQVE TTVCATLLAF LVELLKSSVA MQEQMLGGKG
     FLVIGYLLEK SSRVHITRAV LEQFLSFAKY LDGLSHGAPL LKQLCDHILF NPAIWIHTPA
     KVQLSLYTYL SAEFIGTATI YTTIRRVGTV LQLMHTLKYY YWVINPADSS GIAPKGLDGP
     RPSQKEIISL RAFMLLFLKQ LILKDRGVKE DELQSILNYL LTMHEDENIH DVLQLLVALM
     SEHPASMIPA FDQRNGIRVI YKLLASKSES IWVQALKVLG YFLKHLGHKR KVEIMHTHSL
     FTLLGERLML HTNTVTVTTY NTLYEILTEQ VCTQVVHKPH PEPDSTVKIQ NPMILKVVAT
     LLKNSTPSAE LMEVRRLFLS DMIKLFSNSR ENRRCLLQCS VWQDWMFSLG YINPKSSEEQ
     KITEMVYNIF RILLYHAIKY EWGGWRVWVD TLSIAHSKVT YEAHKEYLAK MYEEYQRQEE
     ENIKKGKKGN VSTISGLSSQ TAGAKGGMEI REIEDLSQSQ SPESETDYPV STDTRDLLMS
     TKVSDDILGS SDRPGSGVHV EVHDLLVDIK AEKVEATEVK LDDMDLSPET LVGGENGALV
     EVESLLDNVY SAAVEKLQNN VHGSVGIIKK NEEKDNGPLI TLADEKEELP NSSTPFLFDK
     IPRQEEKLLP ELSSNHIIPN IQDTQVHLGV SDDLGLLAHM TASVELTCTS SIMEEKDFRI
     HTTSDGVSSV SERELASSTK GLDYAEMTAT TLETESSNSK AVPNVDAGSI ISDTERSDDG
     KESGKEIRKI QTTATTQAVQ GRSSTQQDRD LRVDLGFRGM PMTEEQRRQF SPGPRTTMFR
     IPEFKWSPMH QRLLTDLLFA LETDVHVWRS HSTKSVMDFV NSNENIIFVH NTIHLISQMV
     DNIIIACGGI LPLLSAATSP TGSKTELENI EVTQGMSAET AVTFLSRLMA MVDVLVFASS
     LNFSEIEAEK NMSSGGLMRQ CLRLVCCVAV RNCLECRQRQ RDRGSKSSHG SSKPQEAPHS
     VTAASASKTP LENVPGNLSP IKDPDRLLQD VDINRLRAVV FRDVDDSKQA QFLALAVVYF
     ISVLMVSKYR DILEPQRETA RTGSQPGRNI RQEINSPTST VVVIPSIPHP SLNHGLLAKL
     MPEQSFAHSF YKETPATFPD TVKEKETPTP GEDIQLESSV PHTDSGMGEE QVASILDGAE
     LEPAAGPDAM SELLSTLSSE VKKSQESLTE HPSEMLKPAP SISSISQTKG INVKEILKSL
     VAAPVEIAEC GPEPIPYPDP ALKREAHAIL PMQFHSFDRS VVVPVKKPPP GSLAVTTVGA
     TAAGSGLPTG STSSIFAAPG ATPKSMINTT GAVDSGSSSS SSSSSFVNGA TSKNLPAVQT
     VAPMPEDSAE NMSITAKLER ALEKVAPLLR EIFVDFAPFL SRTLLGSHGQ ELLIEGLVCM
     KSSTSVVELV MLLCSQEWQN SIQKNAGLAF IELINEGRLL CHAMKDHIVR VANEAEFILN
     RQRAEDVHKH AEFESQCAQY AADRREEEKM CDHLISAAKH RDHVTANQLK QKILNILTNK
     HGAWGAVSHS QLHDFWRLDY WEDDLRRRRR FVRNAFGSTH AEALLKSAVE YGTEEDVVKS
     KKAFRSQAIV NQNSETELML EGDDDAVSLL QEKEIDNLAG PVVLSTPAQL IAPVVVAKGT
     LSITTTEIYF EVDEDDAAFK KIDTKVLAYT EGLHGKWMFS EIRAVFSRRY LLQNTALEVF
     MANRTSVMFN FPDQATVKKV VYSLPRVGVG TSYGLPQARR ISLATPRQLY KSSNMTQRWQ
     RREISNFEYL MFLNTIAGRT YNDLNQYPVF PWVLTNYESE ELDLTLPGNF RDLSKPIGAL
     NPKRAVFYAE RYETWEEDQS PPFHYNTHYS TATSALSWLV RIEPFTTFFL NANDGKFDHP
     DRTFSSIARS WRTSQRDTSD VKELIPEFYY LPEMFVNSNG YHLGVREDEV VVNDVDLPPW
     AKKPEDFVRI NRMALESEFV SCQLHQWIDL IFGYKQRGPE AVRALNVFHY LTYEGSVNLD
     SITDPVLREA MEAQIQNFGQ TPSQLLIEPH PPRSSAMHLC FLPQSPLMFK DQMQQDVIMV
     LKFPSNSPVT HVAANTLPHL TIPAVVTVTC SRLFAVNRWH NTVGLRGAPG YSLDQAHHLP
     IEMDPLIANN SGVNKRQITD LVDQSIQINA HCFVVTADNR YILICGFWDK SFRVYSTETG
     KLTQIVFGHW DVVTCLARSE SYIGGDCYIV SGSRDATLLL WYWSGRHHII GDNPNSSDYP
     APRAVLTGHD HEVVCVSVCA ELGLVISGAK EGPCLVHTIT GDLLRALEGP ENCLFPRLIS
     VSSEGHCIIY YERGRFSNFS INGKLLAQME INDSTRAILL SSDGQNLVTG GDNGVVEVWQ
     ACDFKQLYIY PGCDAGIRAM DLSHDQRTLI TGMASGSIVA FNIDFNRWHY EHQNRY
//
ID   TCF20_MOUSE             Reviewed;        1983 AA.
AC   Q9EPQ8; Q60792;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2002, sequence version 2.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Transcription factor 20;
DE            Short=TCF-20;
DE   AltName: Full=Nuclear factor SPBP;
DE   AltName: Full=Stromelysin-1 PDGF-responsive element-binding protein;
DE            Short=SPRE-binding protein;
GN   Name=Tcf20; Synonyms=Spbp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CHARACTERIZATION, AND
RP   ALTERNATIVE SPLICING.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=20568288; PubMed=10995766; DOI=10.1074/jbc.M006978200;
RA   Rekdal C., Sjoettem E., Johansen T.;
RT   "The nuclear factor SPBP contains different functional domains and
RT   stimulates the activity of various transcriptional activators.";
RL   J. Biol. Chem. 275:40288-40300(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 774-1965 (ISOFORM 2).
RC   TISSUE=Fibroblast;
RX   MEDLINE=95280915; PubMed=7760812;
RA   Sanz L., Moscat J., Diaz-Meco M.T.;
RT   "Molecular characterization of a novel transcription factor that
RT   controls stromelysin expression.";
RL   Mol. Cell. Biol. 15:3164-3170(1995).
RN   [3]
RP   INTERACTION WITH JUN.
RX   MEDLINE=96279378; PubMed=8663478; DOI=10.1074/jbc.271.30.18231;
RA   Kirstein M., Sanz L., Moscat J., Diaz-Meco M.T., Saus J.;
RT   "Cross-talk between different enhancer elements during mitogenic
RT   induction of the human stromelysin-1 gene.";
RL   J. Biol. Chem. 271:18231-18236(1996).
RN   [4]
RP   INTERACTION WITH RNF4, TISSUE SPECIFICITY, AND MUTAGENESIS.
RX   MEDLINE=20408957; PubMed=10849425; DOI=10.1074/jbc.M003405200;
RA   Lyngsoe C., Bouteiller G., Damgaard C.K., Ryom D., Sanchez-Munoz S.,
RA   Noerby P.L., Bonven B.J., Joergensen P.;
RT   "Interaction between the transcription factor SPBP and the positive
RT   cofactor RNF4. An interplay between protein binding zinc fingers.";
RL   J. Biol. Chem. 275:26144-26149(2000).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Transcriptional activator that binds to the regulatory
CC       region of MMP3 and thereby controls stromelysin expression. It
CC       stimulates the activity of various transcriptional activators such
CC       as JUN, SP1, PAX6 and ETS1, suggesting a function as a
CC       coactivator.
CC   -!- SUBUNIT: Homodimer (Probable). Interacts with RNF4 and JUN. Binds
CC       to the regulatory region of MMP3.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9EPQ8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9EPQ8-2; Sequence=VSP_003986;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, lung, liver, kidney and
CC       testes.
CC   -!- DEVELOPMENTAL STAGE: Isoform 2 is exclusively expressed at 7-11
CC       days of development. Isoform 1 is found only at low levels in 15-
CC       17 days embryos.
CC   -!- DOMAIN: The atypical PHD domain functions as a negative modulator
CC       of cofactor binding.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 A.T hook DNA-binding domain.
CC   -!- SIMILARITY: Contains 1 PHD-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA86495.1; Type=Frameshift; Positions=Several;
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DR   EMBL; AY007594; AAG28929.1; -; mRNA.
DR   EMBL; U20282; AAA86495.1; ALT_SEQ; mRNA.
DR   IPI; IPI00228557; -.
DR   IPI; IPI00407458; -.
DR   UniGene; Mm.252156; -.
DR   STRING; Q9EPQ8; -.
DR   PhosphoSite; Q9EPQ8; -.
DR   PRIDE; Q9EPQ8; -.
DR   Ensembl; ENSMUST00000048966; ENSMUSP00000048486; ENSMUSG00000041852.
DR   Ensembl; ENSMUST00000066843; ENSMUSP00000064485; ENSMUSG00000041852.
DR   Ensembl; ENSMUST00000109510; ENSMUSP00000105136; ENSMUSG00000041852.
DR   UCSC; uc007wzo.1; mouse.
DR   MGI; MGI:108399; Tcf20.
DR   GeneTree; ENSGT00530000063684; -.
DR   HOVERGEN; HBG079232; -.
DR   InParanoid; Q9EPQ8; -.
DR   OrthoDB; EOG40GCPZ; -.
DR   ArrayExpress; Q9EPQ8; -.
DR   Bgee; Q9EPQ8; -.
DR   CleanEx; MM_TCF20; -.
DR   Genevestigator; Q9EPQ8; -.
DR   GermOnline; ENSMUSG00000041852; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0010843; F:promoter binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0030528; F:transcription regulator activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0010552; P:positive regulation of gene-specific transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR001965; Znf_PHD.
DR   SMART; SM00249; PHD; 1.
DR   PROSITE; PS01359; ZF_PHD_1; FALSE_NEG.
DR   PROSITE; PS50016; ZF_PHD_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW   Phosphoprotein; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1983       Transcription factor 20.
FT                                /FTId=PRO_0000072449.
FT   DOMAIN     1198   1219       Leucine-zipper.
FT   DNA_BIND   1565   1579       A.T hook.
FT   ZN_FING    1911   1962       PHD-type; atypical.
FT   MOTIF      1282   1295       Nuclear localization signal.
FT   MOTIF      1604   1628       Nuclear localization signal.
FT   MOTIF      1812   1819       Nuclear localization signal.
FT   COMPBIAS     62     69       Poly-Ala.
FT   COMPBIAS    173    195       Poly-Gln.
FT   COMPBIAS    249    277       Ser-rich.
FT   COMPBIAS    322    350       Poly-Gln.
FT   COMPBIAS   1585   1592       Poly-Pro.
FT   COMPBIAS   1681   1684       Poly-Glu.
FT   COMPBIAS   1793   1797       Poly-Glu.
FT   MOD_RES      31     31       Phosphoserine (By similarity).
FT   MOD_RES     447    447       Phosphoserine (By similarity).
FT   MOD_RES     458    458       Phosphoserine (By similarity).
FT   MOD_RES     534    534       Phosphoserine (By similarity).
FT   MOD_RES     567    567       Phosphoserine (By similarity).
FT   MOD_RES     588    588       Phosphoserine.
FT   MOD_RES     603    603       Phosphoserine (By similarity).
FT   MOD_RES     612    612       Phosphoserine (By similarity).
FT   MOD_RES     656    656       Phosphoserine (By similarity).
FT   MOD_RES     669    669       Phosphoserine (By similarity).
FT   MOD_RES     900    900       Phosphoserine (By similarity).
FT   MOD_RES    1033   1033       Phosphoserine (By similarity).
FT   MOD_RES    1150   1150       Phosphoserine (By similarity).
FT   MOD_RES    1363   1363       Phosphoserine (By similarity).
FT   MOD_RES    1389   1389       Phosphoserine (By similarity).
FT   MOD_RES    1550   1550       Phosphoserine (By similarity).
FT   MOD_RES    1697   1697       Phosphoserine (By similarity).
FT   MOD_RES    1699   1699       Phosphothreonine (By similarity).
FT   VAR_SEQ    1961   1983       CPLPPLQNKTAKGSLSTEQSERG -> VRLWR (in
FT                                isoform 2).
FT                                /FTId=VSP_003986.
FT   MUTAGEN    1629   1629       A->T: Loss of interaction with RNF4; when
FT                                associated with S-1702; R-1736 and V-
FT                                1737.
FT   MUTAGEN    1702   1702       P->S: Loss of interaction with RNF4; when
FT                                associated with T-1629; R-1736 and V-
FT                                1737.
FT   MUTAGEN    1736   1737       CG->RV: Loss of interaction with RNF4;
FT                                when associated with T-1629 and S-1702.
FT   MUTAGEN    1926   1926       C->A: Reduces the inhibitory effect of
FT                                the atypical PHD domain.
FT   MUTAGEN    1931   1931       C->A: Reduces the inhibitory effect of
FT                                the atypical PHD domain.
FT   MUTAGEN    1936   1936       H->L: Reduces the inhibitory effect of
FT                                the atypical PHD domain.
FT   MUTAGEN    1939   1939       C->A: Reduces the inhibitory effect of
FT                                the atypical PHD domain.
SQ   SEQUENCE   1983 AA;  215284 MW;  E749A9355CB2971B CRC64;
     MQSFREQSSY HGNQQSYPQE VHSSSRIEEF SPRQAQMFQN FGGAGGGSSG TGSSSSGRRG
     TAAAAAAMAS ETSGHQGYQG FRKEAGDFYY MAGNKDTVAA GTPQPPQRRP SGPVQSYGPP
     QGSSFGNQYA SEGHVSQFQA QHSALGGVSH YQQDYTGPFS PGSAQYQQQA SSQQQQQQQQ
     QQQQQQQQQQ QQVQQLRQQL YQSHQPLPQT TGQPASGSSH LQPMQRPSTL PSSAGYQLRV
     GQFGQHYQSS ASSSSSSSFP SPQRFSQSGQ SYDGSYSVNA GSQYEGHNVG SNAQAYGTQS
     NYSYQPQSMK NFEQAKIPPG NQQGQQQQQQ QPQPQQQQPQ QQQQQQQQQQ HPPQRVMQYT
     NAATKIPLQS QVGQYNQPEV PVRSPMQFHQ NFSPISNPSP AASVVQSPSC SSTPSPLMQS
     GENLQCGQGN VPMSSRNRIL QLLPQLSPTP SMMPSPNSHA AGFKGFGLEG VPEKRLTDPG
     LSSLSALSSQ VANLPNTVQH MLLSDALTPQ KKTSKRPSSS SKKADSCTNS EGSSQPEEQL
     KSPMAESLDG GCSSSSEDQG ERVRQLSGQS TSSDTTYKCG ASEKAGSSPT QGAQNEAPRL
     STSPATRDEA ASPGAKDTSL SSEGNTKVNE KTVGVIVSRE AMTGRVEKSG GQDKGSQEDD
     PAASQRPPSN SGVKEISHTS LPQPDPPGGG SKGNKNGDNN SSNHNGEGNG PSSHSAVGPS
     FTGRTEPSKS PGSLRYSYKE SFGSAVPRNV SGYPQYPSGQ EKGDFGSHGE RKGRNEKFPS
     LLQEVLQGYH HHPDRRYPRS AQEHQGMASG LEGTARPNIL VSQTNELASR GLLNKSIGSL
     LENPHWGPWE RKSSSTAPEM KQINLSDYPI PRKFEIEPPS SAHEPGGSLS ERRSVICDIS
     PLRQIVRDPG AHSLGHMGTD ARIGRNERLN PSLSQSVILP GGLVSMETKL KSQGGQIKEE
     DFEQSKSQAS FNKKSGDHCH PTSIKHETYR GNASPGAAAH DSISDYGPQD SRSTPMRRVP
     GRVGSRETMR GRSSSQYHDF AEKLKMSPGR SRGPGGDPHH MNPHMTFSER ANRSSLHAPF
     SPNSESLASA YHTNTRAHAY GDPNTGLNSQ LHYKRQMYQQ QQEEYKDWAS SSAQGVIAAA
     QHRQEGPRKS PRQQQFLDRV RSPLKNDKDG MMYGPPVGTY HDPSTQEAGR CLMSSDGLPA
     QSMELKHSSQ KLQESRWDLS RQTSPAKSSG PPGMSNQKRY GPPHEPDGHG LAESAQSSKP
     SNVMLRLPGQ EDHSSQNPLI MRRRVRSFIS PIPSKRQSQD VKNSNADDKG RLLHPSKEGA
     DKAYNSYSHL SHSQDIKSIP KRDSSKDLPN PDNRNCPAVT LTSPAKTKIL PPRKGRGLKL
     EAIVQKITSP NIRRSASANS AEAGGDTVTL DDILSLKSGP PEGGTVATQE AEMEKRKCEV
     VSDLVSVTNQ ESNVEKPLPG PSEEWRGSGD DKVKTEAHVE TASTGKEPSG TMTSTASQKP
     GGNQGRPDGS LGGAAPLIFP DSKNVAPVGI LAPEANPKAE EKENDTVMIS PKQESFPPKG
     YFPSGKKKGR PIGSVNKQKK QQQQPPPPPQ PPQMPEGSAD GEPKPKKQRQ RRERRKPGAQ
     PRKRKTKQAV PIVEPQEPEI KLKYATQPLD KTDAKNKSFF PYIHVVNKCE LGAVCTIINA
     EEEEQTKLVR SRKGQRSLTP PPSSTESKVL PASSFMLQGP VVTESSVMGH LVCCLCGKWA
     SYRNMGDLFG PFYPQDYAAT LPKNPPPKRS SEMQSKVKVR HKSASNGSKT DTEEEEEQQQ
     QKEQRSLAAH PRFKRRHRSE DCGGGPRSLS RGLPCKKAAT EGSSEKTVSD TKPSVPTTSE
     GGPELELQIP ELPLDSNEFW VHEGCILWAN GIYLVCGRLY GLQEALEIAR EMKCSHCQEA
     GATLGCYNKG CSFRYHYPCA IDADCLLHEE NFSVRCPKHK CPLPPLQNKT AKGSLSTEQS
     ERG
//
ID   S23A2_MOUSE             Reviewed;         648 AA.
AC   Q9EPR4; Q80Y23; Q8C327; Q9JM78;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Solute carrier family 23 member 2;
DE   AltName: Full=Na(+)/L-ascorbic acid transporter 2;
DE   AltName: Full=Sodium-dependent vitamin C transporter 2;
DE            Short=SVCT-2;
DE            Short=mSVCT2;
DE   AltName: Full=Yolk sac permease-like molecule 2;
GN   Name=Slc23a2; Synonyms=Kiaa0238, Svct2, Yspl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=129/SvEv; TISSUE=Brain;
RX   MEDLINE=21082931; PubMed=11214969; DOI=10.1093/dnares/7.6.339;
RA   Gispert S., Dutra A., Lieberman A., Friedlich D., Nussbaum R.L.;
RT   "Cloning and genomic organization of the mouse gene slc23a1 encoding a
RT   vitamin C transporter.";
RL   DNA Res. 7:339-345(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-647 (ISOFORM 1).
RC   TISSUE=Brain;
RA   Fujita I., Hirano J., Tanaka K.;
RT   "Mouse sodium dependent vitamin C transporter 2 (mSVCT2).";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 108-648 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [9]
RP   TISSUE SPECIFICITY, AND DISEASE.
RX   PubMed=17689499; DOI=10.1016/j.bcp.2007.05.024;
RA   Wu X., Iguchi T., Hirano J., Fujita I., Ueda H., Itoh N., Tanaka K.,
RA   Nakanishi T.;
RT   "Upregulation of sodium-dependent vitamin C transporter 2 expression
RT   in adrenals increases norepinephrine production and aggravates
RT   hyperlipidemia in mice with streptozotocin-induced diabetes.";
RL   Biochem. Pharmacol. 74:1020-1028(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-79 AND THR-647, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Sodium/ascorbate cotransporter. Mediates electrogenic
CC       uptake of vitamin C, with a stoichiometry of 2 Na(+) for each
CC       ascorbate (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9EPR4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9EPR4-2; Sequence=VSP_007367, VSP_007368;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in metabolically active and
CC       specialized tissues, including high expression in brain and
CC       adrenals. Detected in a wide range of tissues. Expression in
CC       kidney is almost undetectable.
CC   -!- DISEASE: Note=Elevated expression levels in the adrenals of
CC       diabetic mice.
CC   -!- SIMILARITY: Belongs to the xanthine/uracil permease family.
CC       Nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG02252.1; Type=Erroneous initiation;
CC       Sequence=BAA90751.1; Type=Erroneous initiation;
CC       Sequence=BAC65509.1; Type=Erroneous gene model prediction;
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CC   -----------------------------------------------------------------------
DR   EMBL; AY004874; AAG02252.1; ALT_INIT; mRNA.
DR   EMBL; AK087175; BAC39819.1; -; mRNA.
DR   EMBL; AL831706; CAM26800.1; -; Genomic_DNA.
DR   EMBL; CH466519; EDL28341.1; -; Genomic_DNA.
DR   EMBL; BC050823; AAH50823.1; -; mRNA.
DR   EMBL; AB038145; BAA90751.1; ALT_INIT; mRNA.
DR   EMBL; AK122227; BAC65509.1; ALT_SEQ; Transcribed_RNA.
DR   IPI; IPI00165688; -.
DR   IPI; IPI00261336; -.
DR   RefSeq; NP_061294.2; NM_018824.2.
DR   UniGene; Mm.103581; -.
DR   ProteinModelPortal; Q9EPR4; -.
DR   STRING; Q9EPR4; -.
DR   PhosphoSite; Q9EPR4; -.
DR   PRIDE; Q9EPR4; -.
DR   Ensembl; ENSMUST00000028815; ENSMUSP00000028815; ENSMUSG00000027340.
DR   GeneID; 54338; -.
DR   KEGG; mmu:54338; -.
DR   UCSC; uc008mmi.1; mouse.
DR   UCSC; uc008mmj.1; mouse.
DR   CTD; 54338; -.
DR   MGI; MGI:1859682; Slc23a2.
DR   GeneTree; ENSGT00390000015686; -.
DR   HOVERGEN; HBG056256; -.
DR   InParanoid; Q9EPR4; -.
DR   OMA; MVGKFSA; -.
DR   OrthoDB; EOG4JHCF8; -.
DR   PhylomeDB; Q9EPR4; -.
DR   NextBio; 311116; -.
DR   ArrayExpress; Q9EPR4; -.
DR   Bgee; Q9EPR4; -.
DR   Genevestigator; Q9EPR4; -.
DR   GermOnline; ENSMUSG00000027340; Mus musculus.
DR   GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0008520; F:L-ascorbate:sodium symporter activity; IMP:MGI.
DR   InterPro; IPR006042; Xan_ur_permease.
DR   InterPro; IPR006043; Xant/urac/vitC.
DR   PANTHER; PTHR11119; Xant/urac/vitC; 1.
DR   Pfam; PF00860; Xan_ur_permease; 1.
DR   PROSITE; PS01116; XANTH_URACIL_PERMASE; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Glycoprotein; Ion transport; Membrane;
KW   Phosphoprotein; Sodium; Sodium transport; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1    648       Solute carrier family 23 member 2.
FT                                /FTId=PRO_0000165979.
FT   TRANSMEM    103    123       Helical; (Potential).
FT   TRANSMEM    140    160       Helical; (Potential).
FT   TRANSMEM    162    182       Helical; (Potential).
FT   TRANSMEM    217    237       Helical; (Potential).
FT   TRANSMEM    240    260       Helical; (Potential).
FT   TRANSMEM    264    284       Helical; (Potential).
FT   TRANSMEM    311    331       Helical; (Potential).
FT   TRANSMEM    370    390       Helical; (Potential).
FT   TRANSMEM    460    480       Helical; (Potential).
FT   TRANSMEM    484    504       Helical; (Potential).
FT   TRANSMEM    512    532       Helical; (Potential).
FT   TRANSMEM    546    566       Helical; (Potential).
FT   MOD_RES      78     78       Phosphoserine.
FT   MOD_RES      79     79       Phosphothreonine.
FT   MOD_RES      81     81       Phosphoserine.
FT   MOD_RES     647    647       Phosphothreonine.
FT   CARBOHYD    188    188       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    196    196       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     162    272       LPLFQASAFAFLAPARAILSLDKWKCNTTEITVANGTAELL
FT                                EHIWHPRIQEIQGAIIMSSLIEVVIGLLGLPGALLRYIGPL
FT                                TITPTVALIGLSGFQAAGERAGKHWGIAM -> DYSCQWNG
FT                                RAVGTHLASPNPRDPGGYHHVLTDRSGHWPPWPAWGSAEVY
FT                                WTLDHHTHRGPHWPLWFPGSRRESRKALGHCHAVSVLRELQ
FT                                GWGTIFTTMWDSLVEYLKQSH (in isoform 2).
FT                                /FTId=VSP_007367.
FT   VAR_SEQ     273    648       Missing (in isoform 2).
FT                                /FTId=VSP_007368.
SQ   SEQUENCE   648 AA;  70049 MW;  2590BB11B2A257CB CRC64;
     MMGIGKNTAS KSVEAGGSTE GKYEEEAKHS NFFTLPVVIN GGATSSGEQD NEDTELMAIY
     TTENGIAEKS SLAETLDSTG SLDPQRSDMI YTIEDVPPWY LCIFLGLQHY LTCFSGTIAV
     PFLLADAMCV GDDQWATSQL IGTIFFCVGI TTLLQTTFGC RLPLFQASAF AFLAPARAIL
     SLDKWKCNTT EITVANGTAE LLEHIWHPRI QEIQGAIIMS SLIEVVIGLL GLPGALLRYI
     GPLTITPTVA LIGLSGFQAA GERAGKHWGI AMLTIFLVLL FSQYARNVKF PLPIYKSKKG
     WTAYKFQLFK MFPIILAILV SWLLCFIFTV TDVFPSNSTD YGYYARTDAR KGVLLVAPWF
     KVPYPFQWGM PTVSAAGVIG MLSAVVASII ESIGDYYACA RLSCAPPPPI HAINRGIFVE
     GLSCVLDGIF GTGNGSTSSS PNIGVLGITK VGSRRVIQYG AALMLGLGMV GKFSALFASL
     PDPVLGALFC TLFGMITAVG LSNLQFIDLN SSRNLFVLGF SIFFGLVLPS YLRQNPLVTG
     ITGIDQILNV LLTTAMFVGG CVAFILDNTI PGTPEERGIK KWKKGVSKGS KSLDGMESYN
     LPFGMNIIKK YRCFSYLPIS PTFAGYTWKG FGKSENSRSS DKDSQATV
//
ID   TNR21_MOUSE             Reviewed;         655 AA.
AC   Q9EPU5; Q91W77; Q91XH9;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2002, sequence version 2.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Tumor necrosis factor receptor superfamily member 21;
DE   AltName: Full=Death receptor 6;
DE   AltName: CD_antigen=CD358;
DE   Flags: Precursor;
GN   Name=Tnfrsf21; Synonyms=Dr6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Kidney;
RA   Isogai D., Ichino M., Yoshinari M., Yamaura A., Kurokawa F.,
RA   Minami M.;
RT   "Mouse DR6: mouse homolog of human TNFR-related death receptor-6
RT   (DR6).";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Kidney;
RA   Kim V., Machleidt T., Shi W.-X., Wang X., Cai Z.;
RT   "Murine DR6: murine TNFR-related death receptor-6.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION.
RX   MEDLINE=21571606; PubMed=11714751; DOI=10.1084/jem.194.10.1441;
RA   Zhao H., Yan M., Wang H., Erickson S., Grewal I.S., Dixit V.M.;
RT   "Impaired c-Jun amino terminal kinase activity and T cell
RT   differentiation in death receptor 6-deficient mice.";
RL   J. Exp. Med. 194:1441-1448(2001).
RN   [5]
RP   FUNCTION, INDUCTION, TISSUE SPECIFICITY, AND INTERACTION WITH APP.
RX   PubMed=19225519; DOI=10.1038/nature07767;
RA   Nikolaev A., McLaughlin T., O'Leary D.D.M., Tessier-Lavigne M.;
RT   "APP binds DR6 to trigger axon pruning and neuron death via distinct
RT   caspases.";
RL   Nature 457:981-989(2009).
CC   -!- FUNCTION: May activate NF-kappa-B and promote apoptosis (By
CC       similarity). May activate JNK and be involved in T-cell
CC       differentiation. Required for both normal cell body death and
CC       axonal pruning. Trophic-factor deprivation triggers the cleavage
CC       of surface APP by beta-secretase to release sAPP-beta which is
CC       further cleaved to release an N-terminal fragment of APP (N-APP).
CC       N-APP binds TNFRSF21 triggering caspase activation and
CC       degeneration of both neuronal cell bodies (via caspase-3) and
CC       axons (via caspase-6).
CC   -!- SUBUNIT: Associates with TRADD (By similarity). Interacts with N-
CC       APP.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Probable).
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in adult spleen,
CC       thymus, testis, prostate, ovary, small intestine, colon, brain,
CC       lung and kidney, and in fetal brain, liver and lung. Detected at
CC       lower levels in adult peripheral blood leukocytes, lung, and in
CC       fetal muscle, heart, kidney, small intestine and skin. Detected in
CC       T-cells, B-cells and monocytes. In T-cells expression is highest
CC       in Th0 cells, intermediate in Th2 cells and lower in Th1 cells.
CC       Expressed at low levels in proliferating progenitors in the spinal
CC       cord, but is highly expressed by differentiating neurons within
CC       the spinal cord and adjacent dorsal root ganglia. Expressed by
CC       developing neurons as they differentiate and enter a pro-apoptotic
CC       state. Expressed by both cell bodies and axons.
CC   -!- INDUCTION: Activated by a cleaved N-terminal fragment of APP (N-
CC       APP). Trophic-factor deprivation triggers beta-secretase-dependent
CC       cleavage of APP to release N-APP.
CC   -!- SIMILARITY: Contains 1 death domain.
CC   -!- SIMILARITY: Contains 4 TNFR-Cys repeats.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-25 is the initiator.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF322069; AAG38115.1; -; mRNA.
DR   EMBL; AY043489; AAK74193.1; -; mRNA.
DR   EMBL; BC016420; AAH16420.1; -; mRNA.
DR   IPI; IPI00110366; -.
DR   RefSeq; NP_848704.1; NM_178589.3.
DR   UniGene; Mm.200792; -.
DR   ProteinModelPortal; Q9EPU5; -.
DR   SMR; Q9EPU5; 48-216, 417-499, 569-655.
DR   STRING; Q9EPU5; -.
DR   PhosphoSite; Q9EPU5; -.
DR   PRIDE; Q9EPU5; -.
DR   Ensembl; ENSMUST00000024708; ENSMUSP00000024708; ENSMUSG00000023915.
DR   GeneID; 94185; -.
DR   KEGG; mmu:94185; -.
DR   UCSC; uc008cov.1; mouse.
DR   CTD; 94185; -.
DR   MGI; MGI:2151075; Tnfrsf21.
DR   GeneTree; ENSGT00550000074207; -.
DR   HOGENOM; HBG403016; -.
DR   HOVERGEN; HBG054218; -.
DR   InParanoid; Q9EPU5; -.
DR   OMA; EHCTNTS; -.
DR   OrthoDB; EOG47SSDR; -.
DR   PhylomeDB; Q9EPU5; -.
DR   NextBio; 352147; -.
DR   ArrayExpress; Q9EPU5; -.
DR   Bgee; Q9EPU5; -.
DR   Genevestigator; Q9EPU5; -.
DR   GermOnline; ENSMUSG00000023915; Mus musculus.
DR   GO; GO:0030424; C:axon; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0051402; P:neuron apoptosis; IMP:UniProtKB.
DR   InterPro; IPR000488; Death.
DR   InterPro; IPR011029; DEATH-like.
DR   InterPro; IPR022330; TNFR_21.
DR   InterPro; IPR001368; TNFR_Cys_rich_reg.
DR   Gene3D; G3DSA:1.10.533.10; DEATH_like; 2.
DR   Pfam; PF00531; Death; 1.
DR   PRINTS; PR01971; TNFACTORR21.
DR   SMART; SM00005; DEATH; 1.
DR   SMART; SM00208; TNFR; 4.
DR   SUPFAM; SSF47986; DEATH_like; 1.
DR   PROSITE; PS50017; DEATH_DOMAIN; 1.
DR   PROSITE; PS00652; TNFR_NGFR_1; 1.
DR   PROSITE; PS50050; TNFR_NGFR_2; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Disulfide bond; Glycoprotein; Membrane; Receptor; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     41       Potential.
FT   CHAIN        42    655       Tumor necrosis factor receptor
FT                                superfamily member 21.
FT                                /FTId=PRO_0000034603.
FT   TOPO_DOM     42    349       Extracellular (Potential).
FT   TRANSMEM    350    370       Helical; (Potential).
FT   TOPO_DOM    371    655       Cytoplasmic (Potential).
FT   REPEAT       50     88       TNFR-Cys 1.
FT   REPEAT       90    131       TNFR-Cys 2.
FT   REPEAT      133    167       TNFR-Cys 3.
FT   REPEAT      170    211       TNFR-Cys 4.
FT   DOMAIN      415    498       Death.
FT   CARBOHYD     82     82       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    141    141       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    252    252       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    257    257       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    278    278       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    289    289       N-linked (GlcNAc...) (Potential).
FT   DISULFID     67     80       By similarity.
FT   DISULFID     70     88       By similarity.
FT   DISULFID     91    106       By similarity.
FT   DISULFID    109    123       By similarity.
FT   DISULFID    113    131       By similarity.
FT   DISULFID    133    144       By similarity.
FT   DISULFID    150    168       By similarity.
FT   DISULFID    171    186       By similarity.
FT   DISULFID    192    211       By similarity.
FT   CONFLICT    352    352       W -> L (in Ref. 1; AAG38115).
FT   CONFLICT    523    523       M -> I (in Ref. 3; AAH16420).
SQ   SEQUENCE   655 AA;  71983 MW;  5EC7C51C7C99EFF7 CRC64;
     MGTRASSITA LASCSRTAGQ VGATMVAGSL LLLGFLSTIT AQPEQKTLSL PGTYRHVDRT
     TGQVLTCDKC PAGTYVSEHC TNMSLRVCSS CPAGTFTRHE NGIERCHDCS QPCPWPMIER
     LPCAALTDRE CICPPGMYQS NGTCAPHTVC PVGWGVRKKG TENEDVRCKQ CARGTFSDVP
     SSVMKCKAHT DCLGQNLEVV KPGTKETDNV CGMRLFFSST NPPSSGTVTF SHPEHMESHD
     VPSSTYEPQG MNSTDSNSTA SVRTKVPSGI EEGTVPDNTS STSGKEGTNR TLPNPPQVTH
     QQAPHHRHIL KLLPSSMEAT GEKSSTAIKA PKRGHPRQNA HKHFDINEHL PWMIVLFLLL
     VLVLIVVCSI RKSSRTLKKG PRQDPSAIVE KAGLKKSLTP TQNREKWIYY RNGHGIDILK
     LVAAQVGSQW KDIYQFLCNA SEREVAAFSN GYTADHERAY AALQHWTIRG PEASLAQLIS
     ALRQHRRNDV VEKIRGLMED TTQLETDKLA LPMSPSPLSP SPMPSPNVKL ENSTLLTVEP
     SPLDKNKCFF VDESEPLLRC DSTSSGSSAL SRNGSFITKE KKDTVLRQVR LDPCDLQPIF
     DDMLHILNPE ELRVIEEIPQ AEDKLDRLFE IIGVKSQEAS QTLLDSVYSH LPDLL
//
ID   INP4A_MOUSE             Reviewed;         939 AA.
AC   Q9EPW0; Q8CBJ8;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-FEB-2011, entry version 61.
DE   RecName: Full=Type I inositol-3,4-bisphosphate 4-phosphatase;
DE            EC=3.1.3.66;
DE   AltName: Full=Inositol polyphosphate 4-phosphatase type I;
GN   Name=Inpp4a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC   STRAIN=C57BL/6;
RX   MEDLINE=20558569; PubMed=11087841; DOI=10.1073/pnas.250476397;
RA   Vyas P., Norris F.A., Joseph R., Majerus P.W., Orkin S.H.;
RT   "Inositol polyphosphate 4-phosphatase type I regulates cell growth
RT   downstream of transcription factor GATA-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:13696-13701(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=21378148; PubMed=11485317; DOI=10.1006/bbrc.2001.5331;
RA   Shearn C.T., Walker J., Norris F.A.;
RT   "Identification of a novel spliceoform of inositol polyphosphate 4-
RT   phosphatase type Ialpha expressed in human platelets: structure of
RT   human inositol polyphosphate 4-phosphatase type I gene.";
RL   Biochem. Biophys. Res. Commun. 286:119-125(2001).
CC   -!- FUNCTION: Catalyzes the hydrolysis of the 4-position phosphate of
CC       phosphatidylinositol 3,4-bisphosphate, inositol 1,3,4-
CC       trisphosphate and inositol 1,4-bisphosphate. Involved in the
CC       regulation of megakaryocyte and fibroblast proliferation.
CC       Regulates cell growth downstream of transcription factor GATA-1.
CC   -!- CATALYTIC ACTIVITY: 1-phosphatidyl-myo-inositol 3,4-bisphosphate +
CC       H(2)O = 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate.
CC   -!- PATHWAY: Signal transduction; phosphatidylinositol signaling
CC       pathway.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9EPW0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9EPW0-2; Sequence=VSP_015243, VSP_015244, VSP_015245,
CC                                  VSP_015246;
CC   -!- TISSUE SPECIFICITY: Spleen, skeletal muscle, lung and uterus.
CC   -!- SIMILARITY: Belongs to the inositol-3,4-bisphosphate 4-phosphatase
CC       family.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF317838; AAG40778.1; -; mRNA.
DR   EMBL; AK035867; BAC29220.1; -; mRNA.
DR   IPI; IPI00110426; -.
DR   IPI; IPI00785480; -.
DR   RefSeq; NP_766559.2; NM_172971.2.
DR   UniGene; Mm.5294; -.
DR   ProteinModelPortal; Q9EPW0; -.
DR   SMR; Q9EPW0; 49-147.
DR   STRING; Q9EPW0; -.
DR   PhosphoSite; Q9EPW0; -.
DR   PRIDE; Q9EPW0; -.
DR   Ensembl; ENSMUST00000027287; ENSMUSP00000027287; ENSMUSG00000026113.
DR   Ensembl; ENSMUST00000058307; ENSMUSP00000057233; ENSMUSG00000026113.
DR   GeneID; 269180; -.
DR   KEGG; mmu:269180; -.
DR   CTD; 269180; -.
DR   MGI; MGI:1931123; Inpp4a.
DR   GeneTree; ENSGT00390000002033; -.
DR   HOGENOM; HBG358151; -.
DR   HOVERGEN; HBG081796; -.
DR   InParanoid; Q9EPW0; -.
DR   BRENDA; 3.1.3.66; 244.
DR   ArrayExpress; Q9EPW0; -.
DR   Bgee; Q9EPW0; -.
DR   CleanEx; MM_INPP4A; -.
DR   Genevestigator; Q9EPW0; -.
DR   GermOnline; ENSMUSG00000026113; Mus musculus.
DR   GO; GO:0016316; F:phosphatidylinositol-3,4-bisphosphate 4-phosphatase activity; TAS:MGI.
DR   GO; GO:0034597; F:phosphatidylinositol-4,5-bisphosphate 4-phosphatase activity; IEA:EC.
DR   GO; GO:0006798; P:polyphosphate catabolic process; TAS:MGI.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   PROSITE; PS50004; C2; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Hydrolase; Phosphoprotein.
FT   CHAIN         1    939       Type I inositol-3,4-bisphosphate 4-
FT                                phosphatase.
FT                                /FTId=PRO_0000190233.
FT   DOMAIN       46    137       C2.
FT   MOD_RES     355    355       Phosphotyrosine (By similarity).
FT   MOD_RES     488    488       Phosphoserine (By similarity).
FT   VAR_SEQ       1    265       Missing (in isoform 2).
FT                                /FTId=VSP_015243.
FT   VAR_SEQ     266    272       LLEEDAA -> MCVCFAC (in isoform 2).
FT                                /FTId=VSP_015244.
FT   VAR_SEQ     575    585       Missing (in isoform 2).
FT                                /FTId=VSP_015245.
FT   VAR_SEQ     897    939       EGCRRENTMKNVGSRKYAFNSLQLKAFPKHYRPPEGTYGKV
FT                                ET -> IGTREVVTQKNLSGLVPIRDLRLDPSLLCSIPLLA
FT                                LSPNLLIVWLFLSIAYLVTKLRCK (in isoform 2).
FT                                /FTId=VSP_015246.
FT   CONFLICT    529    529       Q -> E (in Ref. 2; BAC29220).
FT   CONFLICT    553    553       D -> E (in Ref. 2; BAC29220).
FT   CONFLICT    717    717       S -> N (in Ref. 2; BAC29220).
FT   CONFLICT    741    741       V -> F (in Ref. 2; BAC29220).
FT   CONFLICT    744    744       F -> L (in Ref. 2; BAC29220).
FT   CONFLICT    783    783       G -> V (in Ref. 2; BAC29220).
FT   CONFLICT    786    786       G -> V (in Ref. 2; BAC29220).
FT   CONFLICT    792    792       V -> L (in Ref. 2; BAC29220).
SQ   SEQUENCE   939 AA;  105540 MW;  FBF3750836FA8962 CRC64;
     MTAREHSPRH GARARAMQRA STIDVAADMV GLSLAGNIQD PDEPILEFSL ACSELHTPSL
     DRKPNSFVAV SVTTPPQAFW TKHAQTEIIE GTNNPIFLSS IAFFQDSLIN QMTQIKLSVY
     DVKDRSQGTM YLLGSGTFVV KDLLQDRHHR LHLTLRSAES DRVGNITVIG WQMEEKSDQQ
     PPVTRFLDTV NGRMVLPVDE SLTEALGIRS KYAFLRKDSL LKAVFGGAIC RMYRFPTTDG
     NHLRILEQMA ESVLSLHVPR QFVKLLLEED AARVCELEEL GELSPCWESL RRQIVTQYQT
     IILTYQENLT DLHQYKGPSF KASSLKADKK LEFVPTNLHI QRMRVQDDGG SDQNYDVVTI
     GAPAAHCQGF KSGGLRKKLH KFEEAKKHSF EECCTSSSGQ SIIYIPQDIT RAKEIIAQIN
     TLKTQVSYYA ERLSRAAKDR SATGLERTLA ILADKTRQLV TVCDCKLLAN SIHGLNAARP
     DYIASKASPT STEEEQVMLR NDQDTLMARW AGRSSRSSLQ VDWHEEEWQK VWLNVDKSLE
     CIIQRVDKLL QKDRLHGEGC EDAFPCSSTC SSKKDCSPPP EESSPGEWSE ALYPLLTTLT
     DCVAMMSDKA KAAMVFLLMQ DSAPTIASYL SLQYRRDVVF CQTLTALICG FIIKLRNCLH
     DGGFLRQLYT IGLLAQFESL LSTYGEELAM LEDMSLGIMD LRNVTFKVTQ ATSNASSDML
     PVITGNRDGF NVRIPLPGPL VDSFPREIQS GMLLRVQPVL FNVGINEQQT LAERFGDTSL
     QEGINGESLV RVNSYFEQFK EVLPEDCLPR SRSQTCLPEL LRFLGQNVHA RKNKNVDILW
     QAAEVCRRLN GVRFTSCKSA KDRTAMSVTL EQCLILQHEH GMAPQVFTQA LECMRSEGCR
     RENTMKNVGS RKYAFNSLQL KAFPKHYRPP EGTYGKVET
//
ID   CHST1_MOUSE             Reviewed;         411 AA.
AC   Q9EQC0; Q9D0K5;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Carbohydrate sulfotransferase 1;
DE            EC=2.8.2.21;
DE   AltName: Full=Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 1;
DE            Short=GST-1;
DE   AltName: Full=Keratan sulfate Gal-6 sulfotransferase;
DE            Short=KS6ST;
DE            Short=KSGal6ST;
DE            Short=KSST;
GN   Name=Chst1; Synonyms=Gst1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   MEDLINE=21096027; PubMed=11181564; DOI=10.1093/glycob/11.1.75;
RA   Hemmerich S., Lee J.K., Bhakta S., Bistrup A., Ruddle N.R.,
RA   Rosen S.D.;
RT   "Chromosomal localization and genomic organization for the galactose/
RT   N-acetylgalactosamine/N-acetylglucosamine 6-O-sulfotransferase gene
RT   family.";
RL   Glycobiology 11:75-87(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 292-411.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Catalyzes the transfer of sulfate to position 6 of
CC       galactose (Gal) residues of keratan. Has a preference for
CC       sulfating keratan sulfate, but it also transfers sulfate to the
CC       unsulfated polymer. The sulfotransferase activity on sialyl LacNAc
CC       structures is much higher than the corresponding desialylated
CC       substrate, and only internal Gal residues are sulfated. May
CC       function in the sulfation of sialyl N-acetyllactosamine
CC       oligosaccharide chains attached to glycoproteins. Participates in
CC       biosynthesis of selectin ligands. Selectin ligands are present in
CC       high endothelial cells (HEVs) and play a central role in
CC       lymphocyte homing at sites of inflammation (By similarity).
CC   -!- CATALYTIC ACTIVITY: 3'-phosphoadenylyl sulfate + keratan =
CC       adenosine 3',5'-bisphosphate + keratan 6'-sulfate.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type
CC       II membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the sulfotransferase 1 family.
CC       Gal/GlcNAc/GalNAc subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF280087; AAG48245.1; -; mRNA.
DR   EMBL; BC030667; AAH30667.1; -; mRNA.
DR   EMBL; AK011344; BAB27556.2; -; mRNA.
DR   IPI; IPI00111007; -.
DR   RefSeq; NP_076339.1; NM_023850.2.
DR   UniGene; Mm.38021; -.
DR   ProteinModelPortal; Q9EQC0; -.
DR   STRING; Q9EQC0; -.
DR   PhosphoSite; Q9EQC0; -.
DR   PRIDE; Q9EQC0; -.
DR   Ensembl; ENSMUST00000028649; ENSMUSP00000028649; ENSMUSG00000027221.
DR   Ensembl; ENSMUST00000065797; ENSMUSP00000064246; ENSMUSG00000027221.
DR   GeneID; 76969; -.
DR   KEGG; mmu:76969; -.
DR   UCSC; uc008lfk.1; mouse.
DR   CTD; 76969; -.
DR   MGI; MGI:1924219; Chst1.
DR   GeneTree; ENSGT00530000062902; -.
DR   HOGENOM; HBG445813; -.
DR   HOVERGEN; HBG106811; -.
DR   InParanoid; Q9EQC0; -.
DR   OMA; LYHVQYT; -.
DR   OrthoDB; EOG418BNF; -.
DR   BRENDA; 2.8.2.21; 244.
DR   NextBio; 346207; -.
DR   ArrayExpress; Q9EQC0; -.
DR   Bgee; Q9EQC0; -.
DR   Genevestigator; Q9EQC0; -.
DR   GermOnline; ENSMUSG00000027221; Mus musculus.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045130; F:keratan sulfotransferase activity; IEA:EC.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   InterPro; IPR016469; Carbohydrate_sulfotransferase.
DR   InterPro; IPR000863; Sulfotransferase_dom.
DR   Pfam; PF00685; Sulfotransfer_1; 1.
DR   PIRSF; PIRSF005883; Carbohydrate_sulfotransferase; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Glycoprotein; Golgi apparatus;
KW   Inflammatory response; Membrane; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    411       Carbohydrate sulfotransferase 1.
FT                                /FTId=PRO_0000085183.
FT   TOPO_DOM      1      2       Cytoplasmic (Potential).
FT   TRANSMEM      3     23       Helical; Signal-anchor for type II
FT                                membrane protein; (Potential).
FT   TOPO_DOM     24    411       Lumenal (Potential).
FT   NP_BIND      69     75       PAPS (By similarity).
FT   NP_BIND     234    242       PAPS (By similarity).
FT   MOTIF       337    339       Cell attachment site (Potential).
FT   CARBOHYD     56     56       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    145    145       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    189    189       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    334    334       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   411 AA;  46904 MW;  B1AE590EF5B9CBDC CRC64;
     MQCSWKAVLL LALASIAIQY TAIRTFTAKS FHTCPGLTDT GLAERLCEEG PTFSYNLSRK
     THVLILATTR SGSSFVGQLF NQHMDVFYLF EPLYHVQNTL IPRFTQGKSP ADRRVMLGAS
     RDLLRSLYDC DLYFLENYIK PPPVNHTTNR VFRRGASRVL CSRPVCDPPG SSDLILEEGD
     CVRMCGLLNL TLAAEACRER SHVAIKTVRV PEVNDLRALV EDPRLNLKVI QLVRDPRGIL
     ASRSETFRDT YRLWRLWYGT GRKPYNLDVT QLTTVCEDFS SSVSTGLMRP SWLKGKYMLV
     RYEDLARNPM KKTEEIYEFL GIPLDSHVAH WIQNNTRGDP TLGKHKYSTV RNSAATAEKW
     RFRLSYDIVA FAQNACQQVL AQLGYKMANS EEELKNPAIS LVEERDFRPF L
//
ID   DPYL5_MOUSE             Reviewed;         564 AA.
AC   Q9EQF6;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Dihydropyrimidinase-related protein 5;
DE            Short=DRP-5;
DE   AltName: Full=Collapsin response mediator protein 5;
DE            Short=CRMP-5;
GN   Name=Dpysl5; Synonyms=Crmp5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   AND SUBUNIT.
RC   STRAIN=Swiss Webster / NIH; TISSUE=Embryo;
RX   MEDLINE=20545548; PubMed=10956643; DOI=10.1074/jbc.M003277200;
RA   Fukada M., Watakabe I., Yuasa-Kawada J., Kawachi H., Kuroiwa A.,
RA   Matsuda Y., Noda M.;
RT   "Molecular characterization of CRMP5, a novel member of the collapsin
RT   response mediator protein family.";
RL   J. Biol. Chem. 275:37957-37965(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH SEPT4, AND SUBCELLULAR LOCATION.
RX   MEDLINE=22469591; PubMed=12581152;
RX   DOI=10.1046/j.1365-2443.2003.00617.x;
RA   Takahashi S., Inatome R., Yamamura H., Yanagi S.;
RT   "Isolation and expression of a novel mitochondrial septin that
RT   interacts with CRMP/CRAM in the developing neurones.";
RL   Genes Cells 8:81-93(2003).
CC   -!- FUNCTION: May have a function in neuronal differentiation and/or
CC       axon growth.
CC   -!- SUBUNIT: Homotetramer, and heterotetramer with other DPYS-like
CC       proteins. Interacts with DPYSL2, DPYSL3 and DPYSL4. Interacts with
CC       SEPT4 isoform 4.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Note=Translocates
CC       into the mitochondria upon interaction with SEPT4 isoform 4.
CC   -!- TISSUE SPECIFICITY: Detected in brain.
CC   -!- DEVELOPMENTAL STAGE: Detected in whole embryos after 11 days of
CC       development. Detected in embryonic head. Highly expressed in
CC       newborns and up to 7 days after birth. Expression is decreased
CC       after 14 days.
CC   -!- SIMILARITY: Belongs to the DHOase family.
CC       Hydantoinase/dihydropyrimidinase subfamily.
CC   -!- CAUTION: Lacks most of the conserved residues that are essential
CC       for binding the metal cofactor and hence for dihydropyrimidinase
CC       activity. Its enzyme activity is therefore unsure.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF249295; AAG37998.1; -; mRNA.
DR   EMBL; BC065054; AAH65054.1; -; mRNA.
DR   IPI; IPI00624192; -.
DR   RefSeq; NP_075534.1; NM_023047.2.
DR   UniGene; Mm.27732; -.
DR   ProteinModelPortal; Q9EQF6; -.
DR   SMR; Q9EQF6; 8-492.
DR   STRING; Q9EQF6; -.
DR   MEROPS; M38.978; -.
DR   PhosphoSite; Q9EQF6; -.
DR   PRIDE; Q9EQF6; -.
DR   Ensembl; ENSMUST00000088081; ENSMUSP00000085400; ENSMUSG00000029168.
DR   Ensembl; ENSMUST00000114729; ENSMUSP00000110377; ENSMUSG00000029168.
DR   GeneID; 65254; -.
DR   KEGG; mmu:65254; -.
DR   UCSC; uc008wvw.1; mouse.
DR   CTD; 65254; -.
DR   MGI; MGI:1929772; Dpysl5.
DR   GeneTree; ENSGT00550000074371; -.
DR   HOGENOM; HBG724623; -.
DR   HOVERGEN; HBG000806; -.
DR   InParanoid; Q9EQF6; -.
DR   OMA; GITWWAP; -.
DR   OrthoDB; EOG4DNF42; -.
DR   PhylomeDB; Q9EQF6; -.
DR   NextBio; 320340; -.
DR   ArrayExpress; Q9EQF6; -.
DR   Bgee; Q9EQF6; -.
DR   CleanEx; MM_DPYSL5; -.
DR   Genevestigator; Q9EQF6; -.
DR   GermOnline; ENSMUSG00000029168; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IPI:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007411; P:axon guidance; TAS:MGI.
DR   InterPro; IPR006680; Amidohydro_1.
DR   InterPro; IPR011778; D-hydantoinase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Metalo_hydrolase; 2.
DR   TIGRFAMs; TIGR02033; D-hydantoinase; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein.
FT   CHAIN         1    564       Dihydropyrimidinase-related protein 5.
FT                                /FTId=PRO_0000165925.
FT   MOD_RES     509    509       Phosphothreonine (By similarity).
FT   MOD_RES     514    514       Phosphothreonine (By similarity).
FT   MOD_RES     516    516       Phosphothreonine (By similarity).
FT   MOD_RES     534    534       Phosphoserine (By similarity).
SQ   SEQUENCE   564 AA;  61516 MW;  CA93790FC8F9CD98 CRC64;
     MLANSASVRI LIKGGKVVND DCTHEADVYI ESGIIQQVGR ELMIPGGAKV IDATGKLVIP
     GGIDTSTHFH QTFMNATCVD DFYHGTKAAL VGGTTMIIGH VLPDKETSLV EAYEKCRALA
     DPKVCCDYAL HVGITWWAPK VKAEMETLVR EKGVNSFQMF MTYKDLYMLR DSELYQVFHA
     CRDIGAIPRV HAENGELVAE GAKEALDLGI TGPEGIEISH PEELEAEATH RVITIANRTH
     CPIYLVNVSS ISAGDVIAAA KMQGKVVLAE TTNAHATLTG LHYYHQDWSH AAAYVTVPPL
     RLDTNTSTYL MSLLANDTLN IVASDHRPFT TKQKAMGKED FTKIPHGVSG VQDRMSVVWE
     RGVVGGKMDE NRFVAVTSSN AAKILNLYPR KGRIIPGADA DVVVWDPEAT KTISASTQVQ
     GGDFNLYENM RCHGVPLVTI SRGRVVYENG VFMCAEGTGK FCPLRSFPDI VYKKLVQREK
     TLKVRGVDRT PYLGDVAIVV HPGKKEMGTP LADTPTRPVT RHGGMRDLHE SSFSLSGSQI
     DDHVPKRASA RILAPPGGRS SGIW
//
ID   VPS35_MOUSE             Reviewed;         796 AA.
AC   Q9EQH3; Q61123;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Vacuolar protein sorting-associated protein 35;
DE   AltName: Full=Maternal-embryonic 3;
DE   AltName: Full=Vesicle protein sorting 35;
GN   Name=Vps35; Synonyms=Mem3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo, and Embryonic carcinoma;
RX   MEDLINE=96327632; PubMed=8678978; DOI=10.1007/s003359900174;
RA   Hwang S.-Y., Benjamin L.E., Oh B., Rothstein J.L., Ackerman S.L.,
RA   Beddington R.S.P., Solter D., Knowles B.B.;
RT   "Genetic mapping and embryonic expression of a novel, maternally
RT   transcribed gene Mem3.";
RL   Mamm. Genome 7:586-590(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20564209; PubMed=11112353; DOI=10.1006/geno.2000.6380;
RA   Zhang P., Yu L., Gao J., Fu Q., Dai F., Zhao Y., Zheng L., Zhao S.;
RT   "Cloning and characterization of human VPS35 and mouse Vps35 and
RT   mapping of VPS35 to human chromosome 16q13-q21.";
RL   Genomics 70:253-257(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 91-107; 218-226; 297-305; 313-323; 372-382;
RP   404-417 AND 574-582, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   INTERACTION WITH VPS26B.
RX   PubMed=16190980; DOI=10.1111/j.1600-0854.2005.00328.x;
RA   Kerr M.C., Bennetts J.S., Simpson F., Thomas E.C., Flegg C.,
RA   Gleeson P.A., Wicking C., Teasdale R.D.;
RT   "A novel mammalian retromer component, Vps26B.";
RL   Traffic 6:991-1001(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-791, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-791, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Essential component of the retromer complex, a complex
CC       required to retrieve lysosomal enzyme receptors (IGF2R and M6PR)
CC       from endosomes to the trans-Golgi network. Also required to
CC       regulate transcytosis of the polymeric immunoglobulin receptor
CC       (pIgR-pIgA) (By similarity).
CC   -!- SUBUNIT: Component of the retromer complex composed of VPS26
CC       (VPS26A or VPS26B), VPS29, VPS35, SNX1 and SNX2. Interacts
CC       directly with VPS26A and VPS26B. Found in a complex with XPO7,
CC       EIF4A1, ARHGAP1, VPS26A, VPS29, VPS35 and SFN. Interacts with
CC       GOLPH3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane;
CC       Peripheral membrane protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in fat tissue,
CC       testis, brain, kidney, thymus, liver and pancreas, and at lower
CC       levels in heart, intestine and skeletal muscle. Detected in
CC       oocytes, pre-implantation embryos and at E6.5-E12.5.
CC   -!- SIMILARITY: Belongs to the VPS35 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB18153.1; Type=Frameshift; Positions=Several;
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DR   EMBL; U47024; AAB18153.1; ALT_FRAME; mRNA.
DR   EMBL; AF226323; AAG40621.1; -; mRNA.
DR   EMBL; BC005469; AAH05469.1; -; mRNA.
DR   EMBL; BC006637; AAH06637.1; -; mRNA.
DR   IPI; IPI00111181; -.
DR   RefSeq; NP_075373.1; NM_022997.4.
DR   UniGene; Mm.296520; -.
DR   UniGene; Mm.391632; -.
DR   ProteinModelPortal; Q9EQH3; -.
DR   SMR; Q9EQH3; 483-780.
DR   DIP; DIP-32210N; -.
DR   STRING; Q9EQH3; -.
DR   PhosphoSite; Q9EQH3; -.
DR   PRIDE; Q9EQH3; -.
DR   Ensembl; ENSMUST00000034131; ENSMUSP00000034131; ENSMUSG00000031696.
DR   GeneID; 65114; -.
DR   KEGG; mmu:65114; -.
DR   UCSC; uc009mpo.1; mouse.
DR   CTD; 65114; -.
DR   MGI; MGI:1890467; Vps35.
DR   GeneTree; ENSGT00390000007315; -.
DR   HOGENOM; HBG317989; -.
DR   HOVERGEN; HBG054277; -.
DR   InParanoid; Q9EQH3; -.
DR   OMA; ISQEYLM; -.
DR   OrthoDB; EOG4HT8RK; -.
DR   PhylomeDB; Q9EQH3; -.
DR   NextBio; 320313; -.
DR   ArrayExpress; Q9EQH3; -.
DR   Bgee; Q9EQH3; -.
DR   CleanEx; MM_VPS35; -.
DR   Genevestigator; Q9EQH3; -.
DR   GermOnline; ENSMUSG00000031696; Mus musculus.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR005378; VPS35.
DR   PANTHER; PTHR11099; Vps35; 1.
DR   Pfam; PF03635; Vps35; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Membrane; Phosphoprotein;
KW   Protein transport; Transport.
FT   CHAIN         1    796       Vacuolar protein sorting-associated
FT                                protein 35.
FT                                /FTId=PRO_0000065897.
FT   MOD_RES       7      7       Phosphoserine.
FT   MOD_RES     791    791       Phosphotyrosine.
SQ   SEQUENCE   796 AA;  91713 MW;  2ABD338111D641CC CRC64;
     MPTTQQSPQD EQEKLLDEAI QAVKVQSFQM KRCLDKNKLM DALKHASNML GELRTSMLSP
     KSYYELYMAI SDELHYLEVY LTDEFAKGRK VADLYELVQY AGNIIPRLYL LITVGVVYVK
     SFPQSRKDIL KDLVEMCRGV QHPLRGLFLR NYLLQCTRNI LPDEGEPTDE ETTGDISDSM
     DFVLLNFAEM NKLWVRMQHQ GHSRDREKRE RERQELRILV GTNLVRLSQL EGVNVERYKQ
     IVLTGILEQV VNCRDALAQE YLMECIIQVF PDEFHLQTLN PFLRACAELH QNVNVKNIII
     ALIDRLALFA HREDGPGIPA EIKLFDIFSQ QVATVIQSRQ DMPSEDVVSL QVSLINLAMK
     CYPDRVDYVD KVLETTVEIF NKLNLEHIAT SSAVSKELTR LLKIPVDTYN NILTVLKLKH
     FHPLFEYFDY ESRKSMSCYV LSNVLDYNTE IVSQDQVDSI MNLVSTLIQD QPDQPVEDPD
     PEDFADEQSL VGRFIHLLRS DDPDQQYLIL NTARKHFGAG GNQRIRFTLP PLVFAAYQLA
     FRYKENSQMD DKWEKKCQKI FSFAHQTISA LIKAELAELP LRLFLQGALA AGEIGFENHE
     TVAYEFMSQA FSLYEDEISD SKAQLAAITL IIGTFERMKC FSEENHEPLR TQCALAASKL
     LKKPDQGRAV STCAHLFWSG RNTDKNGEEL HGGKRVMECL KKALKIANQC MDPSLQVQLF
     IEILNRYIYF YEKENDAVTI QVLNQLIQKI REDLPNLESS EETEQINKHF HNTLEHLRSR
     RESPESEGPI YEGLIL
//
ID   MAGI3_MOUSE             Reviewed;        1476 AA.
AC   Q9EQJ9; B0V3N7; B0V3N8; Q69ZE1; Q8C0P8;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 2.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3;
DE   AltName: Full=Membrane-associated guanylate kinase inverted 3;
DE            Short=MAGI-3;
GN   Name=Magi3; Synonyms=Kiaa1634;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY,
RP   AND INTERACTION WITH TGFA.
RX   PubMed=15652357; DOI=10.1016/j.yexcr.2004.10.007;
RA   Franklin J.L., Yoshiura K., Dempsey P.J., Bogatcheva G., Jeyakumar L.,
RA   Meise K.S., Pearsall R.S., Threadgill D., Coffey R.J.;
RT   "Identification of MAGI-3 as a transforming growth factor-alpha tail
RT   binding protein.";
RL   Exp. Cell Res. 303:457-470(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 53-1355 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-1476 (ISOFORM 1).
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=14645510; DOI=10.1128/MCB.23.24.8970-8981.2003;
RA   Nguyen M.M., Nguyen M.L., Caruana G., Bernstein A., Lambert P.F.,
RA   Griep A.E.;
RT   "Requirement of PDZ-containing proteins for cell cycle regulation and
RT   differentiation in the mouse lens epithelium.";
RL   Mol. Cell. Biol. 23:8970-8981(2003).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FZD4; FZD7 AND
RP   VANGL2.
RX   PubMed=15195140; DOI=10.1038/sj.onc.1207817;
RA   Yao R., Natsume Y., Noda T.;
RT   "MAGI-3 is involved in the regulation of the JNK signaling pathway as
RT   a scaffold protein for frizzled and Ltap.";
RL   Oncogene 23:6023-6030(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-700 AND SER-702, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-833, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Acts as a scaffolding protein at cell-cell junctions,
CC       thereby regulating various cellular and signaling processes.
CC       Cooperates with PTEN to modulate the kinase activity of AKT1. Its
CC       interaction with PTPRB and tyrosine phosphorylated proteins
CC       suggests that it may link receptor tyrosine phosphatase with its
CC       substrates at the plasma membrane. In polarized epithelial cells,
CC       involved in efficient trafficking of TGFA to the cell surface.
CC       Regulates the ability of LPAR2 to activate ERK and RhoA pathways.
CC       Regulates the JNK signaling cascade via its interaction with FZD4
CC       and VANGL2.
CC   -!- SUBUNIT: Interacts with ADRB1, BAI1, LPAR2/EDG4, GRIN2B, PTEN, and
CC       PTPRB. Interacts with unidentified tyrosine phosphorylated
CC       proteins (By similarity). Interacts with FZD4, FZD7, TGFA and
CC       VANGL2.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC       Cell junction, tight junction. Nucleus (By similarity).
CC       Note=Concentrates in specific sites at the plasma membrane and in
CC       the nucleus. In epithelial cells, it localizes at tight junctions
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9EQJ9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9EQJ9-2; Sequence=VSP_034288, VSP_034289;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Colocalizes with TGFA in
CC       neurons in the cortex and dentate gyrus, as well as in ependymal
CC       cells and some astrocytes (at protein level). Present in lens
CC       epithelium.
CC   -!- SIMILARITY: Belongs to the MAGUK family.
CC   -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC   -!- SIMILARITY: Contains 6 PDZ (DHR) domains.
CC   -!- SIMILARITY: Contains 2 WW domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32503.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA;
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DR   EMBL; AF213258; AAG43836.1; -; mRNA.
DR   EMBL; AC162922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CU210868; CAQ12905.1; -; Genomic_DNA.
DR   EMBL; CU210868; CAQ12906.1; -; Genomic_DNA.
DR   EMBL; AK030083; BAC26773.1; -; mRNA.
DR   EMBL; AK173225; BAD32503.1; ALT_SEQ; Transcribed_RNA.
DR   IPI; IPI00111234; -.
DR   IPI; IPI00880273; -.
DR   RefSeq; NP_598614.1; NM_133853.3.
DR   UniGene; Mm.264849; -.
DR   HSSP; Q86UL8; 1UEQ.
DR   ProteinModelPortal; Q9EQJ9; -.
DR   SMR; Q9EQJ9; 140-195, 292-383, 400-506, 570-1106.
DR   MINT; MINT-1894696; -.
DR   STRING; Q9EQJ9; -.
DR   PRIDE; Q9EQJ9; -.
DR   Ensembl; ENSMUST00000064371; ENSMUSP00000067932; ENSMUSG00000052539.
DR   Ensembl; ENSMUST00000098772; ENSMUSP00000096369; ENSMUSG00000052539.
DR   Ensembl; ENSMUST00000121198; ENSMUSP00000112934; ENSMUSG00000052539.
DR   GeneID; 99470; -.
DR   KEGG; mmu:99470; -.
DR   UCSC; uc008qua.1; mouse.
DR   CTD; 99470; -.
DR   MGI; MGI:1923484; Magi3.
DR   GeneTree; ENSGT00530000063259; -.
DR   HOVERGEN; HBG007091; -.
DR   OrthoDB; EOG41RPTC; -.
DR   ArrayExpress; Q9EQJ9; -.
DR   Bgee; Q9EQJ9; -.
DR   Genevestigator; Q9EQJ9; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF00595; PDZ; 4.
DR   Pfam; PF00397; WW; 2.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 6.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF50156; PDZ; 6.
DR   SUPFAM; SSF51045; WW_Rsp5_WWP; 2.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 6.
DR   PROSITE; PS01159; WW_DOMAIN_1; 2.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell junction; Cell membrane;
KW   Membrane; Nucleotide-binding; Nucleus; Phosphoprotein; Repeat;
KW   Tight junction.
FT   CHAIN         1   1476       Membrane-associated guanylate kinase, WW
FT                                and PDZ domain-containing protein 3.
FT                                /FTId=PRO_0000341408.
FT   DOMAIN       18    108       PDZ 1.
FT   DOMAIN      116    290       Guanylate kinase-like.
FT   DOMAIN      296    329       WW 1.
FT   DOMAIN      342    375       WW 2.
FT   DOMAIN      413    495       PDZ 2.
FT   DOMAIN      581    657       PDZ 3.
FT   DOMAIN      729    811       PDZ 4.
FT   DOMAIN      852    939       PDZ 5.
FT   DOMAIN     1022   1104       PDZ 6.
FT   NP_BIND     123    130       ATP (By similarity).
FT   REGION       18    108       Interaction with ADRB1 and TGFA.
FT   REGION      413    495       Interaction with PTEN (By similarity).
FT   REGION      729    811       Interaction with BAI1 (By similarity).
FT   REGION      852    939       Interaction with LPAR2 and GRIN2B (By
FT                                similarity).
FT   COMPBIAS      6      9       Poly-Lys.
FT   COMPBIAS    240    245       Poly-Glu.
FT   MOD_RES     598    598       Phosphoserine (By similarity).
FT   MOD_RES     700    700       Phosphoserine.
FT   MOD_RES     702    702       Phosphoserine.
FT   MOD_RES     833    833       Phosphoserine.
FT   VAR_SEQ    1112   1126       DWDTNSPSSSNVIYD -> LAPSGLCSYVKPEQH (in
FT                                isoform 2).
FT                                /FTId=VSP_034288.
FT   VAR_SEQ    1127   1476       Missing (in isoform 2).
FT                                /FTId=VSP_034289.
FT   CONFLICT    625    625       I -> N (in Ref. 3; BAC26773).
SQ   SEQUENCE   1476 AA;  161672 MW;  A9F041B5EA4B6F3F CRC64;
     MSKTLKKKKH WLSKVQECAV SWAGPPGDLG AEIRGGAERG EFPYLGRLRD EAGGGGGTCC
     VVSGKAPSPG DVLLEVNGTP VSGLTNRDTL AVIRHFREPI RLKTVKPGKV INKDLRHYLS
     LQFQKGSIDH KLQQVIRDNL YLRTIPCTTR APRDGEVPGV DYNFISVEQF KALEESGALL
     ESGTYDGNFY GTPKPPAEPS PFQPDPVDQV LFDNEFDTES QRKRTTSVSK MERMDSSLPE
     EEEDEDKEAV NGSGSMETRE MHSETSDCWM KTVPSYNQTN SSMDFRNYMM RDENLEPLPK
     NWEMAYTDTG MIYFIDHNTK TTTWLDPRLC KKAKAPEDCE DGELPYGWEK IEDPQYGTYY
     VDHLNQKTQF ENPVEEAKRK KQLGQAEIHS AKTDVERAHF TRDPSQLKGV LVRASLKKST
     MGFGFTIIGG DRPDEFLQVK NVLKDGPAAQ DGKIAPGDVI VDINGNCVLG HTHADVVQMF
     QLVPVNQYVN LTLCRGYPLP DDSEDPVVDI VAATPVINGQ SLTKGETCMN TQDFKLGAMV
     LDQNGKSGQI LASDRLNGPS ESSEQRASLA SSGSSQPELV TIPLIKGPKG FGFAIADSPT
     GQKVKMILDS QWCQGLQKGD IIKEIYHQNV QNLTHLQVVE VLKQFPVGAD VPLLILRGGP
     CSPTKTAKTK TDTKENSGSL ETINEPIPQP MPFPPSIIRS GSPKLDPSEV YLKSKTLYED
     KPPNTKDLDV FLRKQESGFG FRVLGGDGPD QSIYIGAIIP LGAAEKDGRL RAADELMCID
     GIPVKGKSHK QVLDLMTTAA RNGHVLLTVR RKIFYGEKQP EDESHQAFSQ NGSPRLNRAE
     LPTRSAPQEA YDVTLQRKEN EGFGFVILTS KSKPPPGVIP HKIGRVIDGS PADRCGGLKV
     GDHISAVNGQ SIVDLSHDNI VQLIKDAGVT VTLTVVAEEE HHGPPSGTNS ARQSPALQHR
     PMGQAQANHI PGDRIALEGE IGRDVCSSYR HSWSDHKHLA QPDTAVISVV GSRHNQSLGC
     YPVELERGPR GFGFSLRGGK EYNMGLFILR LAEDGPAIKD GRIHVGDQIV EINGEPTQGI
     THTRAIELIQ AGGNKVLLLL RPGTGLIPDH GDWDTNSPSS SNVIYDEQPP PLPSSHSAST
     FEESHVPATE DSLTRVQICE KAEELKDTVQ EKKSTLNGSQ PEMKYQSVHK TMSKKDPPRG
     SGHGEKSRLK GENGVTRRGR SASPKKSVNR HSEEHLEKIP RPLKSDPKEK SRDRSLSPRK
     GESKGRLTIK AGSGQDPYRK DRGRSSSPKK QQKIGGNSLS NTEGKLSEAG SRRAAGHPRD
     STEQLPDGRE KSGVSRKDLK QSQPGKTRTK SPEKKSSKVD ETSLPSKKTS STAGRVVSEK
     EKGKKPTAGE TSRETVEHTQ ISAKQLKQEA QEKTALGNAD DHKGRESEVT DRCRERAGCT
     PQSSSLVKKA PITPGPWRVP RANKVTGTTG MADKQL
//
ID   T22D4_MOUSE             Reviewed;         387 AA.
AC   Q9EQN3;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-FEB-2011, entry version 65.
DE   RecName: Full=TSC22 domain family protein 4;
DE   AltName: Full=TSC22-related-inducible leucine zipper protein 2;
GN   Name=Tsc22d4; Synonyms=Tilz2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ershler M.A., Belyavsky A.V., Visser J.W.M.;
RT   "Identification and characterization of a family of leucine zipper
RT   genes related to TSC22.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcriptional repressor (By similarity).
CC   -!- SUBUNIT: Forms homodimer or heterodimer. Can form an heterodimer
CC       with TSC22D1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- SIMILARITY: Belongs to the TSC-22/Dip/Bun family.
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DR   EMBL; AF201286; AAG41219.1; -; mRNA.
DR   IPI; IPI00111328; -.
DR   UniGene; Mm.286399; -.
DR   ProteinModelPortal; Q9EQN3; -.
DR   SMR; Q9EQN3; 318-371.
DR   STRING; Q9EQN3; -.
DR   PhosphoSite; Q9EQN3; -.
DR   PRIDE; Q9EQN3; -.
DR   Ensembl; ENSMUST00000100539; ENSMUSP00000098107; ENSMUSG00000029723.
DR   MGI; MGI:1926079; Tsc22d4.
DR   GeneTree; ENSGT00530000063062; -.
DR   HOVERGEN; HBG069048; -.
DR   ArrayExpress; Q9EQN3; -.
DR   Bgee; Q9EQN3; -.
DR   CleanEx; MM_TSC22D4; -.
DR   Genevestigator; Q9EQN3; -.
DR   GermOnline; ENSMUSG00000029723; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   GO; GO:0006970; P:response to osmotic stress; IDA:MGI.
DR   InterPro; IPR000580; TSC-22_Dip_Bun.
DR   PANTHER; PTHR12348; TSC-22_Dip_Bun; 1.
DR   Pfam; PF01166; TSC22; 1.
DR   ProDom; PD007152; TSC-22_Dip_Bun; 1.
DR   PROSITE; PS01289; TSC22; 1.
PE   2: Evidence at transcript level;
KW   Nucleus; Phosphoprotein; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    387       TSC22 domain family protein 4.
FT                                /FTId=PRO_0000219375.
FT   DOMAIN      336    357       Leucine-zipper.
FT   MOD_RES      62     62       Phosphoserine (By similarity).
FT   MOD_RES     165    165       Phosphoserine (By similarity).
FT   MOD_RES     219    219       Phosphoserine (By similarity).
FT   MOD_RES     223    223       Phosphothreonine (By similarity).
FT   MOD_RES     227    227       Phosphoserine (By similarity).
FT   MOD_RES     271    271       Phosphoserine (By similarity).
FT   MOD_RES     362    362       Phosphoserine (By similarity).
SQ   SEQUENCE   387 AA;  39988 MW;  C78BB96B5B2DFB90 CRC64;
     MSGGKKKSSF QITSVTTDYE GPGSPGASDS PVPPALAGPP PRLPNGDPNP DPGGRGTPRN
     GSPPPGAPAS RFRVVKLPQG LGEPYRRGRW TCVDVYERDL EPPSFGRLLE GIRGASGGTG
     GRSLDSRLEL ASLGISTPIP QPGLSQGPTS WLRPPPTSPG PQARSFTGGL GQLAGPGKAK
     VETPPLSASP PQQRPPGPGT GDSAQTLPSL RVEVESGGSA AATPPLSRRR DGAVRLRMEL
     VAPAETGKVP PTDSRPNSPA LYFDASLVHK SPDPFGAAAA QSLSLARSML AISGHLDSDD
     DSGSGSLVGI DNKIEQAMDL VKSHLMFAVR EEVEVLKEHI RDLAERNAAL EQENGLLRAL
     ASPEQLAQLP SSGLPRLGPS APNGPSI
//
ID   EHD4_MOUSE              Reviewed;         541 AA.
AC   Q9EQP2;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=EH domain-containing protein 4;
DE   AltName: Full=PAST homolog 2;
DE            Short=mPAST2;
GN   Name=Ehd4; Synonyms=Past2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR;
RA   Plomann M., Behrendt D., Ritter B., Modregger J., Halbach A.,
RA   Paulsson M.;
RT   "MPAST2, a novel murine isoform of the PAST protein family.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION.
RX   PubMed=15930129; DOI=10.1091/mbc.E05-01-0076;
RA   Braun A., Pinyol R., Dahlhaus R., Koch D., Fonarev P., Grant B.D.,
RA   Kessels M.M., Qualmann B.;
RT   "EHD proteins associate with syndapin I and II and such interactions
RT   play a crucial role in endosomal recycling.";
RL   Mol. Biol. Cell 16:3642-3658(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Plays a role in early endosomal transport.
CC   -!- SUBUNIT: Homooligomer, and heterooligomer with EHD1, EHD2 and EHD3
CC       (By similarity).
CC   -!- INTERACTION:
CC       Q9QY17:Pacsin2 (xeno); NbExp=2; IntAct=EBI-491022, EBI-491201;
CC       Q9Z2P6:Snap29 (xeno); NbExp=1; IntAct=EBI-491022, EBI-492883;
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane; Peripheral membrane
CC       protein (By similarity). Recycling endosome membrane; Peripheral
CC       membrane protein (By similarity).
CC   -!- DOMAIN: The EH domain interacts with Asn-Pro-Phe (NPF) motifs of
CC       target proteins (By similarity).
CC   -!- SIMILARITY: Contains 1 EF-hand domain.
CC   -!- SIMILARITY: Contains 1 EH domain.
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DR   EMBL; AF173639; AAG45672.1; -; mRNA.
DR   EMBL; BC007480; AAH07480.1; -; mRNA.
DR   IPI; IPI00318671; -.
DR   RefSeq; NP_598599.2; NM_133838.4.
DR   UniGene; Mm.132226; -.
DR   ProteinModelPortal; Q9EQP2; -.
DR   SMR; Q9EQP2; 22-535.
DR   IntAct; Q9EQP2; 6.
DR   STRING; Q9EQP2; -.
DR   PhosphoSite; Q9EQP2; -.
DR   PRIDE; Q9EQP2; -.
DR   Ensembl; ENSMUST00000028755; ENSMUSP00000028755; ENSMUSG00000027293.
DR   GeneID; 98878; -.
DR   KEGG; mmu:98878; -.
DR   UCSC; uc008lvd.1; mouse.
DR   CTD; 98878; -.
DR   MGI; MGI:1919619; Ehd4.
DR   GeneTree; ENSGT00600000084243; -.
DR   HOVERGEN; HBG018183; -.
DR   InParanoid; Q9EQP2; -.
DR   OMA; KISSLMS; -.
DR   OrthoDB; EOG418BN4; -.
DR   PhylomeDB; Q9EQP2; -.
DR   NextBio; 353697; -.
DR   ArrayExpress; Q9EQP2; -.
DR   Bgee; Q9EQP2; -.
DR   CleanEx; MM_EHD4; -.
DR   Genevestigator; Q9EQP2; -.
DR   GermOnline; ENSMUSG00000027293; Mus musculus.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   InterPro; IPR001401; Dynamin_GTPase.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR000261; EPS15_homology.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   SMART; SM00027; EH; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS50031; EH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Calcium; Endosome; Membrane;
KW   Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1    541       EH domain-containing protein 4.
FT                                /FTId=PRO_0000146115.
FT   DOMAIN      447    535       EH.
FT   DOMAIN      479    514       EF-hand.
FT   NP_BIND      68     75       ATP (By similarity).
FT   CA_BIND     492    503       By similarity.
FT   BINDING     223    223       ATP (By similarity).
FT   BINDING     261    261       ATP (By similarity).
FT   MOD_RES     327    327       N6-acetyllysine (By similarity).
FT   MOD_RES     451    451       Phosphotyrosine (By similarity).
FT   MOD_RES     456    456       Phosphotyrosine (By similarity).
FT   MOD_RES     459    459       Phosphoserine.
FT   MOD_RES     482    482       Phosphoserine (By similarity).
SQ   SEQUENCE   541 AA;  61481 MW;  D34C28F046D740E1 CRC64;
     MFSWMGRQAG GRERSGGMDA VQTVTGGLRS LYQRKVLPLE EAYRFHEFHS PALEDADFEN
     KPMILLVGQY STGKTTFIRY LLEQDFPGMR IGPEPTTDSF IAVMYGETEG STPGNALVVD
     PKKPFRKLSR FGNAFLNRFM CSQLPNQVLK SISIIDSPGI LSGEKQRISR GYDFCQVLQW
     FAERVDRIIL LFDAHKLDIS DEFSEAIKAF RGQDDKIRVV LNKADQVDTQ QLMRVYGALM
     WSLGKVINTP EVLRVYIGSF WAQPLQNTDN RRLFEAEAQD LFRDIQSLPQ KAAVRKLNDL
     IKRARLAKVH AYIISYLKKE MPNMFGKENK KRELIYRLPE IYVQLQREYQ ISAGDFPEVK
     AMQEQLENYD FTKFHSLKPK LIEAVDNMLT NKISSLMGLI SQEEMNMPTQ MVQGGAFDGT
     TEGPFNQGYG EGAKEGADEE EWVVAKDKPV YDELFYTLSP INGKISGVNA KKEMVTSKLP
     NSVLGKIWKL ADCDCDGMLD EEEFALAKHL IKIKLDGYEL PNSLPPHLVP PSHRKSLPKA
     D
//
ID   NCOAT_MOUSE             Reviewed;         916 AA.
AC   Q9EQQ9; Q3ULY7; Q6ZQ71; Q8BK05; Q8BTT2; Q8CFX2; Q9CSJ4; Q9CUR7;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 2.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Bifunctional protein NCOAT;
DE   AltName: Full=Meningioma-expressed antigen 5;
DE   AltName: Full=Nuclear cytoplasmic O-GlcNAcase and acetyltransferase;
DE   Includes:
DE     RecName: Full=Beta-hexosaminidase;
DE              EC=3.2.1.52;
DE     AltName: Full=Beta-N-acetylhexosaminidase;
DE     AltName: Full=Hexosaminidase C;
DE     AltName: Full=N-acetyl-beta-D-glucosaminidase;
DE     AltName: Full=N-acetyl-beta-glucosaminidase;
DE     AltName: Full=O-GlcNAcase;
DE   Includes:
DE     RecName: Full=Histone acetyltransferase;
DE              Short=HAT;
DE              EC=2.3.1.48;
GN   Name=Mgea5; Synonyms=Hexc, Kiaa0679;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Csoka A.B.;
RT   "Mgea5, the murine homolog of a neutral-active cytosolic beta-N-
RT   acetylglucosaminidase, localized on chromosome 19.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-603 (ISOFORM 1), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-77 (ISOFORM 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Head, Mammary gland, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N-3; TISSUE=Kidney, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 109-127, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   PROTEIN SEQUENCE OF 157-167; 775-785 AND 875-886, FUNCTION, SUBUNIT,
RP   DISULFIDE BOND, AND MUTAGENESIS OF ASP-774; CYS-777; PHE-789; CYS-793;
RP   SER-796; ASP-853; ASP-884 AND TYR-891.
RX   PubMed=16356930; DOI=10.1074/jbc.M510485200;
RA   Toleman C.A., Paterson A.J., Kudlow J.E.;
RT   "The histone acetyltransferase NCOAT contains a zinc finger-like motif
RT   involved in substrate recognition.";
RL   J. Biol. Chem. 281:3918-3925(2006).
RN   [7]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=11341771; DOI=10.1006/bbrc.2001.4815;
RA   Comtesse N., Maldener E., Meese E.;
RT   "Identification of a nuclear variant of MGEA5, a cytoplasmic
RT   hyaluronidase and a beta-N-acetylglucosaminidase.";
RL   Biochem. Biophys. Res. Commun. 283:634-640(2001).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY, ACTIVE SITE, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND MUTAGENESIS OF CYS-166; ASP-174; ASP-175; ASP-177 AND
RP   CYS-878.
RX   PubMed=16517082; DOI=10.1016/j.bbagen.2006.01.017;
RA   Toleman C., Paterson A.J., Kudlow J.E.;
RT   "Location and characterization of the O-GlcNAcase active site.";
RL   Biochim. Biophys. Acta 1760:829-839(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Cleaves GlcNAc but not GalNAc from glycopeptides. Can
CC       use p-nitrophenyl-beta-GlcNAc as substrate but not p-nitrophenyl-
CC       beta-GalNAc or p-nitrophenyl-alpha-GlcNAc. Possesses hyaluronidase
CC       activity (By similarity). Acetylates 'Lys-8' of histone H4.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing N-acetyl-
CC       D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + [histone] = CoA + acetyl-
CC       [histone].
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.49 mM for pNP-GLcNAc;
CC       pH dependence:
CC         Optimum pH is 6.5-7;
CC   -!- SUBUNIT: Monomer (By similarity). Binds both acetylated and
CC       unacetylated histone H4 tail but acetylation on 'Lys-8' of histone
CC       H4 abolishes binding.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9EQQ9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9EQQ9-2; Sequence=VSP_020870, VSP_020872;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q9EQQ9-3; Sequence=VSP_020871;
CC         Note=No experimental confirmation available;
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout development from
CC       blastocyst stage to embryonic day 16.5.
CC   -!- PTM: Proteolytically cleaved by caspase-3 (By similarity).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH41109.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
CC       Sequence=BAC97998.1; Type=Erroneous initiation;
CC       Sequence=BAE26311.1; Type=Erroneous initiation;
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DR   EMBL; AF132214; AAG43273.2; -; mRNA.
DR   EMBL; AK129188; BAC97998.1; ALT_INIT; mRNA.
DR   EMBL; BC041109; AAH41109.1; ALT_SEQ; mRNA.
DR   EMBL; BC054821; AAH54821.1; -; mRNA.
DR   EMBL; AK012695; BAB28416.1; -; mRNA.
DR   EMBL; AK014781; BAB29550.1; -; mRNA.
DR   EMBL; AK077613; BAC36900.1; -; mRNA.
DR   EMBL; AK088774; BAC40564.1; -; mRNA.
DR   EMBL; AK145227; BAE26311.1; ALT_INIT; mRNA.
DR   IPI; IPI00406624; -.
DR   IPI; IPI00655175; -.
DR   IPI; IPI00788404; -.
DR   RefSeq; NP_076288.1; NM_023799.3.
DR   UniGene; Mm.393213; -.
DR   UniGene; Mm.440640; -.
DR   UniGene; Mm.480399; -.
DR   ProteinModelPortal; Q9EQQ9; -.
DR   SMR; Q9EQQ9; 46-390.
DR   MINT; MINT-2844950; -.
DR   STRING; Q9EQQ9; -.
DR   CAZy; GH84; Glycoside Hydrolase Family 84.
DR   PhosphoSite; Q9EQQ9; -.
DR   PRIDE; Q9EQQ9; -.
DR   Ensembl; ENSMUST00000026243; ENSMUSP00000026243; ENSMUSG00000025220.
DR   Ensembl; ENSMUST00000070185; ENSMUSP00000065431; ENSMUSG00000025220.
DR   GeneID; 76055; -.
DR   KEGG; mmu:76055; -.
DR   NMPDR; fig|10090.3.peg.5165; -.
DR   UCSC; uc008hrm.1; mouse.
DR   UCSC; uc008hrn.1; mouse.
DR   CTD; 76055; -.
DR   MGI; MGI:1932139; Mgea5.
DR   GeneTree; ENSGT00390000007726; -.
DR   HOVERGEN; HBG053044; -.
DR   InParanoid; Q9EQQ9; -.
DR   OMA; KFEEMCG; -.
DR   OrthoDB; EOG469QT2; -.
DR   BRENDA; 2.3.1.48; 244.
DR   BRENDA; 3.2.1.52; 244.
DR   NextBio; 344519; -.
DR   ArrayExpress; Q9EQQ9; -.
DR   Bgee; Q9EQQ9; -.
DR   CleanEx; MM_MGEA5; -.
DR   Genevestigator; Q9EQQ9; -.
DR   GermOnline; ENSMUSG00000025220; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004563; F:beta-N-acetylhexosaminidase activity; IEA:EC.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IEA:EC.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR011496; Beta-N-acetylglucosaminidase.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Gene3D; G3DSA:3.40.630.30; Acyl_CoA_acyltransferase; 2.
DR   Pfam; PF07555; NAGidase; 1.
DR   SUPFAM; SSF55729; Acyl_CoA_acyltransferase; 1.
DR   SUPFAM; SSF51445; Glyco_hydro_cat; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Alternative splicing; Cytoplasm;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Multifunctional enzyme; Nucleus; Phosphoprotein; Transferase.
FT   CHAIN         1    916       Bifunctional protein NCOAT.
FT                                /FTId=PRO_0000252119.
FT   REGION      583    916       Histone acetyltransferase activity (By
FT                                similarity).
FT   REGION      695    814       Required for histone H4 binding.
FT   ACT_SITE    175    175       Nucleophile; for O-GlcNAcase activity.
FT   ACT_SITE    177    177       Proton donor; for O-GlcNAcase activity.
FT   MOD_RES     364    364       Phosphoserine.
FT   DISULFID    777    793
FT   VAR_SEQ       1    698       Missing (in isoform 2).
FT                                /FTId=VSP_020870.
FT   VAR_SEQ       1      1       M -> MVRPRVWRSSRRVASQNGLRAFGPTDRGRRGAVAGG
FT                                RRM (in isoform 3).
FT                                /FTId=VSP_020871.
FT   VAR_SEQ     699    725       NDLFFQPPPLTPTSKVYTIRPYFPKDE -> MYTTHSCLYS
FT                                FFLTFFLVCCLTRLYFQ (in isoform 2).
FT                                /FTId=VSP_020872.
FT   MUTAGEN     166    166       C->S: No change in substrate affinity but
FT                                60% reduction in O-GlcNAcase activity.
FT   MUTAGEN     174    174       D->N: 2-fold increase in substrate
FT                                affinity and 77% reduction in O-GlcNAcase
FT                                activity. Regains appreciable level of
FT                                catalytic efficiency in the acidic pH
FT                                range. No recovery of activity in the
FT                                presence of sodium azide.
FT   MUTAGEN     175    175       D->A: 3-fold increase in substrate
FT                                affinity and 90% reduction in O-GlcNAcase
FT                                activity. Regains appreciable level of
FT                                catalytic efficiency in the acidic pH
FT                                range. 70% recovery of activity in the
FT                                presence of sodium azide.
FT   MUTAGEN     177    177       D->N: 2-fold decrease in substrate
FT                                affinity and 96% reduction in O-GlcNAcase
FT                                activity. Regains appreciable level of
FT                                catalytic efficiency in the acidic pH
FT                                range. 40% recovery of activity in the
FT                                presence of sodium azide.
FT   MUTAGEN     774    774       D->A: Disrupts ability to bind histone H4
FT                                as well as HAT activity.
FT   MUTAGEN     777    777       C->A: Disrupts ability to bind histone H4
FT                                as well as HAT activity.
FT   MUTAGEN     789    789       F->A: Disrupts ability to bind histone H4
FT                                as well as HAT activity.
FT   MUTAGEN     793    793       C->A: Disrupts ability to bind histone H4
FT                                as well as HAT activity.
FT   MUTAGEN     796    796       S->A: Disrupts ability to bind histone H4
FT                                as well as HAT activity.
FT   MUTAGEN     853    853       D->N: Retains ability to bind histone H4.
FT   MUTAGEN     878    878       C->S: No effect on O-GlcNAcase activity.
FT   MUTAGEN     884    884       D->N: Retains ability to bind histone H4.
FT   MUTAGEN     891    891       Y->F: Retains ability to bind histone H4.
FT   CONFLICT      6      6       S -> T (in Ref. 3; BAE26311).
FT   CONFLICT     52     53       GA -> RT (in Ref. 3; BAE26311).
FT   CONFLICT    742    742       F -> S (in Ref. 2; BAC97998).
SQ   SEQUENCE   916 AA;  103162 MW;  B2FAC6F10E03C5CA CRC64;
     MVQKESQAAL EERESERNAN PAAASGASLE QSVAPAPGED NPSGAGAAAV VGAAGGARRF
     LCGVVEGFYG RPWVMEQRKE LFRRLQKWEL NTYLYAPKDD YKHRMFWREM YSVEEAEQLM
     TLISAAREYE IEFIYAISPG LDITFSNPKE VSTLKRKLDQ VSQFGCRSFA LLFDDIDHNM
     CAADKEVFSS FAHAQVSITN EIYQYLGEPE TFLFCPTEYC GTFCYPNVSQ SPYLRTVGEK
     LLPGIEVLWT GPKVVSKEIP VESIEEVSKI IKRAPVIWDN IHANDYDQKR LFLGPYKGRS
     TELIPRLKGV LTNPNCEFEA NYVAIHTLAT WYKSNMNGVR KDVVMTDSED STVSIQIKLE
     NEGSDEDIET DVLYSPQMAL KLALTEWLQE FGVPHQYSSR QVAHSGAKTS VVDGTPLVAA
     PSLNATTVVT TVYQEPIMSQ GAALSGEPSV LTKEEEKKQP DEEPMDMVVE KQEEAEHKND
     NQILTEIVEA KMAEELRPMD TDKESMAESK SPEMSMQEDC IPDVAPMQTD EQTQKEQFVP
     GPNEKPLYTA EPVTLEDLQL LADLFYLPYE HGPKGAQMLR EFQWLRANSS VVSVNCKGKD
     SEKIEEWRSR AAKFEEMCAL VMGMFTRLSN CANRTILYDM YSYVWDIKSI MSMVKSFVQW
     LGCRSHSSAQ FLIGDQEPWA FRGGLAGEFQ RLLPIDGAND LFFQPPPLTP TSKVYTIRPY
     FPKDEASVYK ICREMYDDGV GFPFQSQPDL IGDKLVGGLL SLSLDYCFVL EDEDGICGYA
     LGTVDVTPFI KKCKISWIPF MQEKYTKPNG DKELSEAEKI MLSFHEEQEV LPETFLANFP
     SLIKMDIHKK VTDPSVAKSM MACLLSSLKA NGSRGAFCEV RPDDKRILEF YSKLGCFEIA
     KMEGFPKDVV ILGRSL
//
ID   KCNH7_MOUSE             Reviewed;        1195 AA.
AC   Q9ER47;
DT   28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Potassium voltage-gated channel subfamily H member 7;
DE   AltName: Full=Ether-a-go-go-related gene potassium channel 3;
DE            Short=ERG-3;
DE            Short=Eag-related protein 3;
DE            Short=Ether-a-go-go-related protein 3;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv11.3;
GN   Name=Kcnh7; Synonyms=Erg3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Arcangeli A.;
RT   "Erg genes expression during development of mouse embryos.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium
CC       channel (By similarity). Channel properties may be modulated by
CC       cAMP and subunit assembly.
CC   -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC       heterotetrameric complex of pore-forming alpha subunits that can
CC       associate with modulating beta subunits. Heteromultimer with
CC       KCNH2/ERG1 and KCNH6/ERG2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position.
CC   -!- SIMILARITY: Belongs to the potassium channel family. H (Eag)
CC       (TC 1.A.1.20) subfamily. Kv11.3/KCNH7 sub-subfamily.
CC   -!- SIMILARITY: Contains 1 cyclic nucleotide-binding domain.
CC   -!- SIMILARITY: Contains 1 PAC (PAS-associated C-terminal) domain.
CC   -!- SIMILARITY: Contains 1 PAS (PER-ARNT-SIM) domain.
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DR   EMBL; AJ291608; CAC14797.1; -; mRNA.
DR   IPI; IPI00274979; -.
DR   UniGene; Mm.242532; -.
DR   ProteinModelPortal; Q9ER47; -.
DR   SMR; Q9ER47; 26-135, 572-667, 670-858.
DR   STRING; Q9ER47; -.
DR   PhosphoSite; Q9ER47; -.
DR   PRIDE; Q9ER47; -.
DR   Ensembl; ENSMUST00000075052; ENSMUSP00000074563; ENSMUSG00000059742.
DR   UCSC; uc008jvq.1; mouse.
DR   MGI; MGI:2159566; Kcnh7.
DR   GeneTree; ENSGT00550000074394; -.
DR   HOGENOM; HBG717083; -.
DR   HOVERGEN; HBG052232; -.
DR   InParanoid; Q9ER47; -.
DR   OrthoDB; EOG4STS3W; -.
DR   ArrayExpress; Q9ER47; -.
DR   Bgee; Q9ER47; -.
DR   Genevestigator; Q9ER47; -.
DR   GermOnline; ENSMUSG00000059742; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR   InterPro; IPR003967; K_chnl_volt-dep_ERG.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   Gene3D; G3DSA:2.60.120.10; RmlC-like_jellyroll; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   PRINTS; PR01463; EAGCHANLFMLY.
DR   PRINTS; PR01470; ERGCHANNEL.
DR   SMART; SM00100; cNMP; 1.
DR   SMART; SM00086; PAC; 1.
DR   SUPFAM; SSF51206; cNMP_binding; 1.
DR   PROSITE; PS00888; CNMP_BINDING_1; FALSE_NEG.
DR   PROSITE; PS00889; CNMP_BINDING_2; FALSE_NEG.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS50113; PAC; FALSE_NEG.
DR   PROSITE; PS50112; PAS; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Ion transport; Ionic channel; Membrane; Phosphoprotein;
KW   Potassium; Potassium channel; Potassium transport; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1   1195       Potassium voltage-gated channel subfamily
FT                                H member 7.
FT                                /FTId=PRO_0000054016.
FT   TOPO_DOM      1    412       Cytoplasmic (Potential).
FT   TRANSMEM    413    433       Helical; Name=Segment S1; (Potential).
FT   TOPO_DOM    434    449       Extracellular (Potential).
FT   TRANSMEM    450    470       Helical; Name=Segment S2; (Potential).
FT   TOPO_DOM    471    494       Cytoplasmic (Potential).
FT   TRANSMEM    495    515       Helical; Name=Segment S3; (Potential).
FT   TOPO_DOM    516    521       Extracellular (Potential).
FT   TRANSMEM    522    542       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TOPO_DOM    543    549       Cytoplasmic (Potential).
FT   TRANSMEM    550    570       Helical; Name=Segment S5; (Potential).
FT   TOPO_DOM    571    614       Extracellular (Potential).
FT   INTRAMEM    615    635       Pore-forming; Name=Segment H5;
FT                                (Potential).
FT   TOPO_DOM    636    641       Extracellular (Potential).
FT   TRANSMEM    642    662       Helical; Name=Segment S6; (Potential).
FT   TOPO_DOM    663   1195       Cytoplasmic (Potential).
FT   DOMAIN       41     70       PAS.
FT   DOMAIN       92    144       PAC.
FT   NP_BIND     745    862       cNMP.
FT   MOTIF       627    632       Selectivity filter (By similarity).
FT   MOD_RES     350    350       Phosphoserine (By similarity).
FT   MOD_RES     353    353       Phosphoserine (By similarity).
FT   CARBOHYD    600    600       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   1195 AA;  135027 MW;  8DCCB9BA0580FFC2 CRC64;
     MPVRRGHVAP QNTFLGTIIR KFEGQNKKFI IANARVQNCA IIYCNDGLCE MTGFSRPDVM
     QKPCTCDFLH GPETKRHDIA QIAQALLGSE ERKVEVTYYH KNGSTFICNT HIIPVKNQEG
     VAMMFIINFE YVTDEENAAT PERVNPILPV KTVNRKLFGF KFPGLRVLTY RKQSLPQEDP
     DVVVIDSSKH SDDSVAMKHF KSPTKESCSP SEADDTKALI QPSQCSPLVN ISGPLDHSSP
     KRQWDRLYPD MLQSSSQLTH SRSRESLCSI RRASSVHDIE GFSVHPKNIF RDRHASEDNG
     RNVKGPFNHI KSSLLGSTSD SNLNKYSTIN KIPQLTLNFS DVKTEKKNTS PPSSDKTIIA
     PKVKERTHNV TEKVTQVLSL GADVLPEYKL QTPRINKFTI LHYSPFKAVW DWLILLLVIY
     TAIFTPYSAA FLLNDREEQK RRECGYSCSP LNVVDLIVDI MFIIDILINF RTTYVNQNEE
     VVSDPAKIAI HYFKGWFLID MVAAIPFDLL VFGSGSDETT TLIGLLKTAR LLRLVRVARK
     LDRYSEYGAA VLMLLMCIFA LIAHWLACIW YAIGNVERPY LTDKIGWLDS LGTQIGKRYN
     DSDSSSGPSI KDKYVTALYF TFSSLTSVGF GNVSPNTNSE KIFSICVMLI GSLMYASIFG
     NVSAIIQRLY SGTARYHMQM LRVKEFIRFH QIPNPLRQRL EEYFQHAWTY TNGIDMNMVL
     KGFPECLQAD ICLHLNQTLL QNCKAFRGAN KGCLRALAMK FKTTHAPPGD TLVHCGDVLT
     ALYFLSRGSI EILKDDIVVA ILGKNDIFGE MVHLYAKPGK SNADVRALTY CDLHKIQRED
     LLEVLDMYPE FSDHFLTNLE LTFNLRHESA KSQSVNDSEG DTGKLRRRRL SFESEGEKDF
     SKENSANDAD DSTDTIRRYQ SSKKHFEERK SRSSSFISSI DDEQKPLFLG TVDSTPRMVK
     ATRLHGEETM PPSPRIHTDK RSHSCRDITD THSWEREPAR AQPEECSPSG LQRAAWGVSE
     TESDLTYGEV EQRLDLLQEQ LNRLESQMTT DIQAILQLLQ KQTTVVPPAY SMVTAGAEYQ
     RPILRLLRTS HPRASIKTDR SFSPSSQCPE FLDLEKSKLQ SKESLSSGRR LNTASEDNLT
     SLLKQDSDAS SELDPRQRKT YLHPIRHPSL PDSSLSTVGI LGLHRHVSDP GLPGK
//
ID   OSBL5_MOUSE             Reviewed;         874 AA.
AC   Q9ER64; Q8R510; Q99NF5;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   11-FEB-2002, sequence version 3.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Oxysterol-binding protein-related protein 5;
DE            Short=ORP-5;
DE            Short=OSBP-related protein 5;
DE   AltName: Full=Oxysterol-binding protein homolog 1;
GN   Name=Osbpl5; Synonyms=Obph1, Osbp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129/Sv;
RX   MEDLINE=20519229; PubMed=11063728; DOI=10.1093/hmg/9.18.2691;
RA   Engemann S., Stroedicke M., Paulsen M., Franck O., Reinhardt R.,
RA   Lane N., Reik W., Walter J.;
RT   "Sequence and functional comparison in the Beckwith-Wiedemann region:
RT   implications for a novel imprinting centre and extended imprinting.";
RL   Hum. Mol. Genet. 9:2691-2706(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Higashimoto K., Soejima H., Yatsuki H., Joh K., Wang Y., Ishino F.,
RA   Ono R., Jinno Y., Iwasaka T., Uchiyama M., Masuko S., Xin Z., Zhu X.,
RA   Katsuki T., Mukai T.;
RT   "Unique imprinted status of mouse Obph1 gene and no imprimted status
RT   of the human homologue in placenta.";
RL   Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SIMILARITY: Belongs to the OSBP family.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC16404.2; Type=Erroneous initiation;
CC       Sequence=CAC27351.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AJ278263; CAC16404.2; ALT_INIT; mRNA.
DR   EMBL; AJ276505; CAC27351.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AB074008; BAB85687.1; -; mRNA.
DR   EMBL; BC079872; AAH79872.1; -; mRNA.
DR   IPI; IPI00624705; -.
DR   RefSeq; NP_001186156.1; NM_001199227.1.
DR   UniGene; Mm.21199; -.
DR   ProteinModelPortal; Q9ER64; -.
DR   SMR; Q9ER64; 125-243.
DR   STRING; Q9ER64; -.
DR   PhosphoSite; Q9ER64; -.
DR   PRIDE; Q9ER64; -.
DR   Ensembl; ENSMUST00000020411; ENSMUSP00000020411; ENSMUSG00000037606.
DR   Ensembl; ENSMUST00000119499; ENSMUSP00000113362; ENSMUSG00000037606.
DR   Ensembl; ENSMUST00000121409; ENSMUSP00000113375; ENSMUSG00000037606.
DR   GeneID; 79196; -.
DR   UCSC; uc009kpw.1; mouse.
DR   MGI; MGI:1930265; Osbpl5.
DR   GeneTree; ENSGT00550000074515; -.
DR   HOGENOM; HBG446335; -.
DR   HOVERGEN; HBG053375; -.
DR   InParanoid; Q9ER64; -.
DR   OrthoDB; EOG45TCMJ; -.
DR   PhylomeDB; Q9ER64; -.
DR   ArrayExpress; Q9ER64; -.
DR   Bgee; Q9ER64; -.
DR   CleanEx; MM_OSBP2; -.
DR   CleanEx; MM_OSBPL5; -.
DR   Genevestigator; Q9ER64; -.
DR   GermOnline; ENSMUSG00000037606; Mus musculus.
DR   GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:0008202; P:steroid metabolic process; IEA:InterPro.
DR   InterPro; IPR000648; Oxysterol-bd.
DR   InterPro; IPR018494; Oxysterol-bd_CS.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   PANTHER; PTHR10972; Oxysterol_bd; 1.
DR   Pfam; PF01237; Oxysterol_BP; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS01013; OSBP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   2: Evidence at transcript level;
KW   Lipid transport; Lipid-binding; Phosphoprotein; Transport.
FT   CHAIN         1    874       Oxysterol-binding protein-related protein
FT                                5.
FT                                /FTId=PRO_0000100374.
FT   DOMAIN      126    243       PH.
FT   MOD_RES     746    746       Phosphoserine (By similarity).
FT   CONFLICT     37     44       ENELGPIT -> MSLVPSPQ (in Ref. 1;
FT                                CAC27351).
FT   CONFLICT    312    312       D -> N (in Ref. 2; BAB85687).
SQ   SEQUENCE   874 AA;  98922 MW;  FBC41FA8E219F5E3 CRC64;
     MKEEAFLRRR FSLCPPASTP QKTDPRKVPR NLLLGCENEL GPITPGRDME SNGPSQPRDE
     EPQTPGSATK VPLAEYRLCN GSDKECTSPT TRVSKKDALK AQKENYRQEK KRATKQLFSA
     LTDPSVVIMA DSLKIRGTLK SWTKLWCVLK PGVLLIYKTP KVGQWVGTVL LHCCELIERP
     SKKDGFCFKL FHPLDQSVWA VKGPKGESVG SITQPLPSSY LIFRAASESD GRCWLDALEL
     ALRCSSLLRL STCKQGRDGE QGSSPDASPS SLYGLPTSAT IPDQDLFPLN GSALENDAFS
     DKSERENAED SDAETQDHSR KTNESGSDLL DSPGGPWRGT TYVEQVQEEL GELDETSQVE
     TVSEENKSLM WVLLRQLRPG MDLSRVVLPT FVLEPRSFLG KLSDYYYHGD LLSRAAAEDD
     PYCRMKLVLR WYLSGFYKKP KGIKKPYNPI LGETFRCRWL HPQTNSHTFY IAEQVSHHPP
     VSAFYVSNRK DGFCMSGSIT AKSKFYGNSL SALLDGKAKL TFLNRKEEYT LTMPYAHCRG
     ILYGTMTMEL GGKVNIECEK NNLQAELDFK LKPFFGSSAN INQISGKIMS GEEVLARLTG
     HWDRDVFIKE ESSGGTELFW TPSEEVRRQR LKRHTVLLEE QSELESERLW QHVTRAIREG
     DQHKATQEKS VLEEAQRQRA REHQQSLTPW KPQLFLLDPL TQEWRYRYED LSPWDPLKDI
     AQYEQDGILH TLQRETMSGQ TTFLGSPDSR HKRPSSDRRL RKASDQPSGH SQVTESSGST
     PESCPDLSDE DFVPGGESPC PRCRREVHRL KMLQEAVLSI QEAQQELHRH LSTMLSSTVR
     AGQAPAPSLL QNPRSWFLLC IFLTCQLFIN YILK
//
ID   TFP11_MOUSE             Reviewed;         838 AA.
AC   Q9ERA6; Q8VD06;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Tuftelin-interacting protein 11;
DE   AltName: Full=Septin and tuftelin-interacting protein 1;
DE            Short=STIP-1;
DE   AltName: Full=Tuftelin-interacting protein 39;
GN   Name=Tfip11; Synonyms=Stip, Tip39;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster; TISSUE=Tooth;
RX   MEDLINE=20515038; PubMed=11063033;
RA   Paine C.T., Paine M.L., Snead M.L.;
RT   "Identification of tuftelin- and amelogenin-interacting proteins using
RT   the yeast two-hybrid system.";
RL   Connect. Tissue Res. 38:257-267(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND INTERACTION
RP   WITH TUFT1.
RC   STRAIN=Swiss Webster; TISSUE=Tooth;
RX   MEDLINE=20357353; PubMed=10806191; DOI=10.1074/jbc.M000118200;
RA   Paine C.T., Paine M.L., Luo W., Okamoto C.T., Lyngstadaas S.P.,
RA   Snead M.L.;
RT   "A tuftelin-interacting protein (TIP39) localizes to the apical
RT   secretory pole of mouse ameloblasts.";
RL   J. Biol. Chem. 275:22284-22292(2000).
RN   [3]
RP   SEQUENCE REVISION.
RA   Paine C.T., Paine M.L., Snead M.L.;
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-99, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-96 AND SER-99,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May play a role in the differentiation of ameloblasts
CC       and odontoblasts or in the forming of the enamel extracellular
CC       matrix. May also be involved in pre-mRNA splicing.
CC   -!- SUBUNIT: Identified in the spliceosome C complex, at least
CC       composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23,
CC       DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1,
CC       GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK,
CC       HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1,
CC       PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B,
CC       PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2,
CC       SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2,
CC       SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2,
CC       SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8 (By
CC       similarity). Interacts with TUFT1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- TISSUE SPECIFICITY: Widely expressed. In tooth it is expressed in
CC       ameloblasts and odontoblasts.
CC   -!- DEVELOPMENTAL STAGE: Expressed as early as E14 and continues into
CC       postnatal development. Within the developing tooth, expression is
CC       localized at the apical region of the ameloblast cells and to the
CC       apical regions of the newly formed enamel matrix.
CC   -!- SIMILARITY: Belongs to the TFP11/STIP family.
CC   -!- SIMILARITY: Contains 1 G-patch domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF290474; AAG10198.2; -; mRNA.
DR   EMBL; BC017682; AAH17682.1; -; mRNA.
DR   IPI; IPI00112101; -.
DR   RefSeq; NP_061253.2; NM_018783.4.
DR   UniGene; Mm.172947; -.
DR   ProteinModelPortal; Q9ERA6; -.
DR   STRING; Q9ERA6; -.
DR   PhosphoSite; Q9ERA6; -.
DR   PRIDE; Q9ERA6; -.
DR   Ensembl; ENSMUST00000031288; ENSMUSP00000031288; ENSMUSG00000029345.
DR   GeneID; 54723; -.
DR   KEGG; mmu:54723; -.
DR   UCSC; uc008ysy.1; mouse.
DR   CTD; 54723; -.
DR   MGI; MGI:1930075; Tfip11.
DR   GeneTree; ENSGT00390000012739; -.
DR   HOGENOM; HBG589450; -.
DR   HOVERGEN; HBG055868; -.
DR   InParanoid; Q9ERA6; -.
DR   OMA; CERRMQP; -.
DR   OrthoDB; EOG4BRWK2; -.
DR   PhylomeDB; Q9ERA6; -.
DR   NextBio; 311578; -.
DR   ArrayExpress; Q9ERA6; -.
DR   Bgee; Q9ERA6; -.
DR   CleanEx; MM_TFIP11; -.
DR   Genevestigator; Q9ERA6; -.
DR   GermOnline; ENSMUSG00000029345; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:MGI.
DR   GO; GO:0005681; C:spliceosomal complex; ISS:UniProtKB.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; NAS:UniProtKB.
DR   GO; GO:0030198; P:extracellular matrix organization; NAS:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR000467; G_patch.
DR   InterPro; IPR022783; GCFC_dom.
DR   InterPro; IPR022159; TIP_N.
DR   Pfam; PF01585; G-patch; 1.
DR   Pfam; PF07842; GCFC; 1.
DR   Pfam; PF12457; TIP_N; 1.
DR   SMART; SM00443; G_patch; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
PE   1: Evidence at protein level;
KW   Biomineralization; Cytoplasm; Direct protein sequencing;
KW   mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Spliceosome.
FT   CHAIN         1    838       Tuftelin-interacting protein 11.
FT                                /FTId=PRO_0000072502.
FT   DOMAIN      150    196       G-patch.
FT   COMPBIAS     15     20       Poly-Asp.
FT   MOD_RES      60     60       Phosphoserine.
FT   MOD_RES      96     96       Phosphoserine.
FT   MOD_RES      99     99       Phosphoserine.
FT   MOD_RES     163    163       Phosphotyrosine (By similarity).
FT   MOD_RES     211    211       Phosphoserine (By similarity).
FT   CONFLICT    393    393       A -> T (in Ref. 4; AAH17682).
SQ   SEQUENCE   838 AA;  96305 MW;  B50842BF12733930 CRC64;
     MSLSHLYRDG EGHLDDDDDD ERENFEITDW DLQNEFNPNR QRHWQTKEEA TYGVWAERDS
     DEERPSFGGK RARDYSAPVN FISAGLKKGA AEEADSEDSD AEEKPVKQED FPKDLGPKKL
     KTGGNFKPSQ KGFSGGTKSF MDFGSWERHT KGIGQKLLQK MGYVPGRGLG KNAQGIINPI
     EAKQRKGKGA VGAYGSERTT QSLQDFPVAD SEEEAEEEFQ KELSQWRKDP SGSKKKPKYS
     YKTVEELKAK GRVSKKLTAP QKELSQVKVI DMTGREQKVY YSYSQISHKH SVPDEGVPLL
     AQLPPTAGKE ARMPGFALPE LEHNLQLLIE RTEQEIIQSD RQLQYERDMV VSLSHELEKT
     AEVLAHEERV ISNLSKVLAL VEECERRMQP HGADPLTLDE CARIFETLQD KYYEEYRLAD
     RADLAVAIVY PLVKDYFKDW HPLEDGSYGT QIISKWKSLL ENDQLLSHSS QDLSSDAFHR
     LMWEVWMPFV RNVVAQWQPR NCEPMVDFLD SWAHIIPVWI LDNILDQLIF PKLQKEVDNW
     NPLTDTVPIH SWIHPWLPLM QARLEPLYSP VRSKLSSALQ KWHPSDASAK LILQPWKEVL
     TPGSWEAFML RNIVPKLGMC LGELVINPHQ QHMDAFYWVM DWEGMISVSS LVGLLEKHFF
     PKWLQVLCSW LSNSPNYEEI TKWYLGWKSM FSDQVLAHPS VKDKFNEALD IMNRAVSSNV
     GAYMQPGARE NIAYLTHTER RKDFQYEAMQ ERREAENMAQ RGIGVAASSV PMNFKDLIET
     KAEEHNIVFM PVIGKRHEGK QLYTFGRIVI YIDRGVVFVQ GEKTWVPTSL QSLIDMAK
//
ID   SNP29_MOUSE             Reviewed;         260 AA.
AC   Q9ERB0; Q3UGN0; Q9DBC5;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Synaptosomal-associated protein 29;
DE            Short=SNAP-29;
DE   AltName: Full=Golgi SNARE of 32 kDa;
DE            Short=Gs32;
DE   AltName: Full=Soluble 29 kDa NSF attachment protein;
DE   AltName: Full=Vesicle-membrane fusion protein SNAP-29;
GN   Name=Snap29;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Bui T.D., Hong W.;
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hypothalamus, Liver, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Involved in multiple membrane trafficking steps (By
CC       similarity).
CC   -!- SUBUNIT: Binds tightly to multiple syntaxins (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane;
CC       Peripheral membrane protein (By similarity). Cell junction,
CC       synapse, synaptosome (By similarity). Note=Appears to be mostly
CC       membrane-bound, probably via interaction with syntaxins, but a
CC       significant portion is cytoplasmic (By similarity).
CC   -!- SIMILARITY: Belongs to the SNAP-25 family.
CC   -!- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY008722; AAG32076.1; -; mRNA.
DR   EMBL; AK005042; BAB23769.1; -; mRNA.
DR   EMBL; AK007065; BAB24850.1; -; mRNA.
DR   EMBL; AK039203; BAC30277.1; -; mRNA.
DR   EMBL; AK147845; BAE28177.1; -; mRNA.
DR   EMBL; BC030066; AAH30066.1; -; mRNA.
DR   IPI; IPI00321581; -.
DR   RefSeq; NP_075837.3; NM_023348.4.
DR   UniGene; Mm.271992; -.
DR   ProteinModelPortal; Q9ERB0; -.
DR   SMR; Q9ERB0; 54-110, 205-257.
DR   STRING; Q9ERB0; -.
DR   PhosphoSite; Q9ERB0; -.
DR   PRIDE; Q9ERB0; -.
DR   Ensembl; ENSMUST00000023449; ENSMUSP00000023449; ENSMUSG00000022765.
DR   GeneID; 67474; -.
DR   KEGG; mmu:67474; -.
DR   UCSC; uc007yku.1; mouse.
DR   CTD; 67474; -.
DR   MGI; MGI:1914724; Snap29.
DR   eggNOG; roNOG15248; -.
DR   GeneTree; ENSGT00510000048053; -.
DR   HOGENOM; HBG278212; -.
DR   HOVERGEN; HBG057045; -.
DR   InParanoid; Q9ERB0; -.
DR   OMA; PWRDARD; -.
DR   OrthoDB; EOG4FFD2R; -.
DR   PhylomeDB; Q9ERB0; -.
DR   NextBio; 324690; -.
DR   ArrayExpress; Q9ERB0; -.
DR   Bgee; Q9ERB0; -.
DR   CleanEx; MM_SNAP29; -.
DR   Genevestigator; Q9ERB0; -.
DR   GermOnline; ENSMUSG00000022765; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR   GO; GO:0019717; C:synaptosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR000928; SNAP-25.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   Pfam; PF00835; SNAP-25; 1.
DR   Pfam; PF05739; SNARE; 1.
DR   SMART; SM00397; t_SNARE; 2.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Coiled coil; Cytoplasm; Membrane; Phosphoprotein;
KW   Protein transport; Synapse; Synaptosome; Transport.
FT   CHAIN         1    260       Synaptosomal-associated protein 29.
FT                                /FTId=PRO_0000213602.
FT   DOMAIN      198    260       t-SNARE coiled-coil homology.
FT   COILED       76    107       Potential.
FT   MOD_RES     212    212       Phosphoserine.
FT   CONFLICT    183    184       SS -> FF (in Ref. 2; BAB23769).
SQ   SEQUENCE   260 AA;  29572 MW;  DD813A78C605576F CRC64;
     MSGYPKSYNP FDDDVEEEDT RPAPWKDVRD LPDGPDAPID RQQYLRQEVL RRAEATAAST
     SRSLSLMYES EKIGVASSEE LVRQRGVLEH TEKMVDKMDQ DLKMSQKHIN SIKSVFGGFI
     NYFKSKPVEP PPEQNGSIVS QPNSRLKEAI NTSKDQENKY QASHPNLRRL QDAELDSVPK
     EPSSTVNTEV YPKNSTLRTY HQKIDSNLDE LSVGLGHLKD IALGMQTEIE EQDDILDRLT
     TKVDKLDVNI KSTEKKVRQL
//
ID   SO1C1_MOUSE             Reviewed;         715 AA.
AC   Q9ERB5; Q8BX54;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Solute carrier organic anion transporter family member 1C1;
DE   AltName: Full=Organic anion transporter 2;
DE            Short=OATP2;
DE   AltName: Full=Organic anion transporter F;
DE            Short=OATP-F;
DE   AltName: Full=Organic anion-transporting polypeptide 14;
DE            Short=OATP-14;
DE   AltName: Full=Solute carrier family 21 member 14;
DE   AltName: Full=Thyroxine transporter;
GN   Name=Slco1c1; Synonyms=Oatp1c1, Oatpf, Slc21a14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Cochlea;
RA   Hampton L.L., Lattig M.C., Battey J.F.;
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=18687783; DOI=10.1210/en.2008-0378;
RA   Roberts L.M., Woodford K., Zhou M., Black D.S., Haggerty J.E.,
RA   Tate E.H., Grindstaff K.K., Mengesha W., Raman C., Zerangue N.;
RT   "Expression of the thyroid hormone transporters monocarboxylate
RT   transporter-8 (SLC16A2) and organic ion transporter-14 (SLCO1C1) at
RT   the blood-brain barrier.";
RL   Endocrinology 149:6251-6261(2008).
CC   -!- FUNCTION: Mediates the Na(+)-independent high affinity transport
CC       of organic anions such as the thyroid hormones thyroxine (T4) and
CC       rT3. Other potential substrates, such as triiodothyronine (T3),
CC       estradiol-17-beta-glucuronide, estrone-3-sulfate and
CC       sulfobromophthalein (BSP) are transported with much lower
CC       efficiency (By similarity). May play a signifiant role in
CC       regulating T4 flux into and out of the brain (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Highly expressed in cerebral microvessels (at
CC       protein level). Highly expressed in cerebral microvessels
CC       throughout the brain and in tanycytes of the third ventricle.
CC   -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60)
CC       family.
CC   -!- SIMILARITY: Contains 1 Kazal-like domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AY007379; AAG09622.1; -; mRNA.
DR   EMBL; AK048926; BAC33495.1; -; mRNA.
DR   IPI; IPI00112146; -.
DR   RefSeq; NP_001171243.1; NM_001177772.1.
DR   RefSeq; NP_067446.1; NM_021471.2.
DR   UniGene; Mm.284495; -.
DR   ProteinModelPortal; Q9ERB5; -.
DR   SMR; Q9ERB5; 482-511.
DR   STRING; Q9ERB5; -.
DR   PhosphoSite; Q9ERB5; -.
DR   PRIDE; Q9ERB5; -.
DR   Ensembl; ENSMUST00000032362; ENSMUSP00000032362; ENSMUSG00000030235.
DR   Ensembl; ENSMUST00000111837; ENSMUSP00000107468; ENSMUSG00000030235.
DR   GeneID; 58807; -.
DR   KEGG; mmu:58807; -.
DR   UCSC; uc009eop.1; mouse.
DR   CTD; 58807; -.
DR   MGI; MGI:1889679; Slco1c1.
DR   GeneTree; ENSGT00560000077029; -.
DR   HOGENOM; HBG717600; -.
DR   HOVERGEN; HBG063896; -.
DR   InParanoid; Q9ERB5; -.
DR   OMA; NLLVITF; -.
DR   OrthoDB; EOG4PC9RQ; -.
DR   PhylomeDB; Q9ERB5; -.
DR   NextBio; 314394; -.
DR   ArrayExpress; Q9ERB5; -.
DR   Bgee; Q9ERB5; -.
DR   Genevestigator; Q9ERB5; -.
DR   GermOnline; ENSMUSG00000030235; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR020846; Major_facilitator_SF.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   InterPro; IPR004156; OA_transporter.
DR   InterPro; IPR002350; Prot_inh_Kazal.
DR   InterPro; IPR011497; Prot_Inh_Kazal_2.
DR   PANTHER; PTHR11388; OA_transporter; 1.
DR   Pfam; PF07648; Kazal_2; 1.
DR   Pfam; PF03137; OATP; 1.
DR   SMART; SM00280; KAZAL; 1.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
DR   TIGRFAMs; TIGR00805; oat; 1.
DR   PROSITE; PS51465; KAZAL_2; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Disulfide bond; Glycoprotein; Ion transport; Membrane;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    715       Solute carrier organic anion transporter
FT                                family member 1C1.
FT                                /FTId=PRO_0000191056.
FT   TOPO_DOM      1     43       Cytoplasmic (Potential).
FT   TRANSMEM     44     63       Helical; Name=1; (Potential).
FT   TOPO_DOM     64     82       Extracellular (Potential).
FT   TRANSMEM     83    103       Helical; Name=2; (Potential).
FT   TOPO_DOM    104    109       Cytoplasmic (Potential).
FT   TRANSMEM    110    134       Helical; Name=3; (Potential).
FT   TOPO_DOM    135    187       Extracellular (Potential).
FT   TRANSMEM    188    216       Helical; Name=4; (Potential).
FT   TOPO_DOM    217    235       Cytoplasmic (Potential).
FT   TRANSMEM    236    256       Helical; Name=5; (Potential).
FT   TOPO_DOM    257    274       Extracellular (Potential).
FT   TRANSMEM    275    299       Helical; Name=6; (Potential).
FT   TOPO_DOM    300    351       Cytoplasmic (Potential).
FT   TRANSMEM    352    373       Helical; Name=7; (Potential).
FT   TOPO_DOM    374    393       Extracellular (Potential).
FT   TRANSMEM    394    417       Helical; Name=8; (Potential).
FT   TOPO_DOM    418    421       Cytoplasmic (Potential).
FT   TRANSMEM    422    445       Helical; Name=9; (Potential).
FT   TOPO_DOM    446    557       Extracellular (Potential).
FT   TRANSMEM    558    580       Helical; Name=10; (Potential).
FT   TOPO_DOM    581    589       Cytoplasmic (Potential).
FT   TRANSMEM    590    615       Helical; Name=11; (Potential).
FT   TOPO_DOM    616    649       Extracellular (Potential).
FT   TRANSMEM    650    667       Helical; Name=12; (Potential).
FT   TOPO_DOM    668    715       Cytoplasmic (Potential).
FT   DOMAIN      473    528       Kazal-like.
FT   COMPBIAS    145    188       Ser-rich.
FT   CARBOHYD    452    452       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    523    523       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    536    536       N-linked (GlcNAc...) (Potential).
FT   DISULFID    479    505       By similarity.
FT   DISULFID    483    494       By similarity.
FT   DISULFID    485    509       By similarity.
FT   CONFLICT    603    603       Missing (in Ref. 2; BAC33495).
SQ   SEQUENCE   715 AA;  78320 MW;  8659472884FAD7FE CRC64;
     MDTSSKENAH LFHKNSAQPA GGPSFTVGYP STEEARPCCG KLKVFLGALS FVYFAKALAE
     GYLKSTVTQI ERRFEIPSSL VGIIDGSFEI GNLLVITFVS YFGAKLHRPK IIGAGCLVMG
     FGTMLIAVPQ FFMEKYSYEK YERYSPSSNV TPSISPCYLE SSSPSPSSIL GKSQNKISHE
     CVGDSSSSMW VYVFLGNLLR GLGETPIQPL GIAYLDDFAS EDNAAFYIGC VQTVAIIGPI
     FGFLLGSLCA KLYVDIGFVN LDHITITPKD PQWVGAWWLG YLIAGFLSLL AAVPFWCLPK
     TLPRSQSREN SGSTSEKSKF IDDPIHYQMA PGDDKMKIME MAKDFLPSLK TLFRNPVYIL
     YLCASTVQFN SLFGMVTYKP KYIEQQYGQS SSKANFVIGL INIPAVALGI FSGGIVMKKF
     RLGICEATKL YLGSSVFGYL LFLSLFALGC ENSSVAGLTV SYQGTKPVSY HERALFSDCN
     SRCKCSDSKW EPMCGDNGIT YVSACLAGCQ SSSRSGKNII FSNCTCVGFA APKSGNWSGM
     MGRCQKDNGC SQMFLYFLVI SVITSYTLSL GGIPGYILLL RCIQPQLKSF ALGIYTLAVR
     VLAGIPAPVY FGVLIDTSCL KWGFKKCGSR GSCRLYDSHA FRHIYLGLTT LLGTVSVFLS
     MAVLFVLKKK YVSKHSSLIT TREKIGMSSS IKKETCAARD RGLQPKYWPG KETRL
//
ID   RGPS2_MOUSE             Reviewed;         590 AA.
AC   Q9ERD6; Q7TPZ6; Q80YA6; Q8BZ37; Q8BZU2; Q9D2Y7;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Ras-specific guanine nucleotide-releasing factor RalGPS2;
DE   AltName: Full=Ral GEF with PH domain and SH3-binding motif 2;
DE   AltName: Full=RalA exchange factor RalGPS2;
GN   Name=Ralgps2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Testis;
RX   PubMed=12485849;
RA   Martegani E., Ceriani M., Tisi R., Berruti G.;
RT   "Cloning and characterization of a new Ral-GEF expressed in mouse
RT   testis.";
RL   Ann. N. Y. Acad. Sci. 973:135-137(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Cecum, Colon, and Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Egg;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   MOTIF.
RX   MEDLINE=20250892; PubMed=10747847; DOI=10.1074/jbc.C000085200;
RA   Rebhun J.F., Chen H., Quilliam L.A.;
RT   "Identification and characterization of a new family of guanine
RT   nucleotide exchange factors for the ras-related GTPase Ral.";
RL   J. Biol. Chem. 275:13406-13410(2000).
RN   [5]
RP   FUNCTION, INTERACTION WITH GRB2 AND PLCG1, SUBCELLULAR LOCATION,
RP   ALTERNATIVE SPLICING, TISSUE SPECIFICITY, DOMAIN, AND MOTIF.
RX   PubMed=17462626; DOI=10.1016/j.yexcr.2007.03.016;
RA   Ceriani M., Scandiuzzi C., Amigoni L., Tisi R., Berruti G.,
RA   Martegani E.;
RT   "Functional analysis of RalGPS2, a murine guanine nucleotide exchange
RT   factor for RalA GTPase.";
RL   Exp. Cell Res. 313:2293-2307(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-308; THR-333 AND
RP   SER-336, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Guanine nucleotide exchange factor for the small GTPase
CC       RALA. May be involved in cytoskeletal organization. May also be
CC       involved in the stimulation of transcription in a Ras-independent
CC       fashion.
CC   -!- SUBUNIT: Interacts with RALA (By similarity). Interacts with the
CC       SH3 domains of GRB2 and PLCG1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Associates
CC       with membranes through the PH domain.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9ERD6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9ERD6-2; Sequence=VSP_031972;
CC       Name=3;
CC         IsoId=Q9ERD6-3; Sequence=VSP_031973;
CC       Name=4;
CC         IsoId=Q9ERD6-4; Sequence=VSP_031974, VSP_031975;
CC   -!- TISSUE SPECIFICITY: Abundant in brain and testis.
CC   -!- DOMAIN: The PH domain m1ediates binding to phosphatidylinositol
CC       4,5-biphosphate.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 Ras-GEF domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF312924; AAG34162.1; -; mRNA.
DR   EMBL; AK018622; BAB31312.1; -; mRNA.
DR   EMBL; AK033549; BAC28351.1; -; mRNA.
DR   EMBL; AK036803; BAC29580.1; -; mRNA.
DR   EMBL; AK169368; BAE41116.1; -; mRNA.
DR   EMBL; BC043132; AAH43132.1; -; mRNA.
DR   EMBL; BC052663; AAH52663.1; -; mRNA.
DR   IPI; IPI00380471; -.
DR   IPI; IPI00403905; -.
DR   IPI; IPI00885611; -.
DR   IPI; IPI00885790; -.
DR   RefSeq; NP_001153437.1; NM_001159965.1.
DR   RefSeq; NP_001153438.1; NM_001159966.1.
DR   RefSeq; NP_001153439.1; NM_001159967.1.
DR   RefSeq; NP_001153440.1; NM_001159968.1.
DR   RefSeq; NP_076373.3; NM_023884.4.
DR   UniGene; Mm.28376; -.
DR   ProteinModelPortal; Q9ERD6; -.
DR   SMR; Q9ERD6; 47-287, 466-579.
DR   STRING; Q9ERD6; -.
DR   PhosphoSite; Q9ERD6; -.
DR   PRIDE; Q9ERD6; -.
DR   Ensembl; ENSMUST00000027886; ENSMUSP00000027886; ENSMUSG00000026594.
DR   Ensembl; ENSMUST00000063199; ENSMUSP00000063872; ENSMUSG00000026594.
DR   GeneID; 78255; -.
DR   KEGG; mmu:78255; -.
DR   UCSC; uc007dcu.1; mouse.
DR   CTD; 78255; -.
DR   MGI; MGI:1925505; Ralgps2.
DR   GeneTree; ENSGT00600000084163; -.
DR   HOGENOM; HBG445143; -.
DR   HOVERGEN; HBG059258; -.
DR   InParanoid; Q9ERD6; -.
DR   OMA; QSNRQQV; -.
DR   OrthoDB; EOG45DWP2; -.
DR   PhylomeDB; Q9ERD6; -.
DR   NextBio; 348555; -.
DR   ArrayExpress; Q9ERD6; -.
DR   Bgee; Q9ERD6; -.
DR   CleanEx; MM_RALGPS2; -.
DR   Genevestigator; Q9ERD6; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001895; RasGRF_CDC25.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.10.840.10; RasGRF_CDC25; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00720; RASGEF; FALSE_NEG.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasm;
KW   Guanine-nucleotide releasing factor; Membrane; Phosphoprotein.
FT   CHAIN         1    590       Ras-specific guanine nucleotide-releasing
FT                                factor RalGPS2.
FT                                /FTId=PRO_0000322601.
FT   DOMAIN       49    287       Ras-GEF.
FT   DOMAIN      464    576       PH.
FT   REGION      466    590       Required for stimulation of nucleotide
FT                                exchange by RALA (By similarity).
FT   MOTIF       331    334       PXXP.
FT   MOD_RES     293    293       Phosphoserine (By similarity).
FT   MOD_RES     296    296       Phosphoserine (By similarity).
FT   MOD_RES     308    308       Phosphoserine.
FT   MOD_RES     333    333       Phosphothreonine.
FT   MOD_RES     336    336       Phosphoserine.
FT   MOD_RES     350    350       Phosphoserine (By similarity).
FT   MOD_RES     429    429       Phosphoserine (By similarity).
FT   VAR_SEQ      20     54       Missing (in isoform 2).
FT                                /FTId=VSP_031972.
FT   VAR_SEQ     423    448       Missing (in isoform 3).
FT                                /FTId=VSP_031973.
FT   VAR_SEQ     552    568       NSYKFQAGSRMNAMLWF -> ERLDRLGSSTADPNSGS
FT                                (in isoform 4).
FT                                /FTId=VSP_031974.
FT   VAR_SEQ     569    590       Missing (in isoform 4).
FT                                /FTId=VSP_031975.
FT   CONFLICT    252    252       I -> M (in Ref. 1; AAG34162).
FT   CONFLICT    298    298       E -> G (in Ref. 3; AAH52663).
FT   CONFLICT    429    429       S -> T (in Ref. 2; BAC28351).
SQ   SEQUENCE   590 AA;  65530 MW;  49EAF1951FDF5DB7 CRC64;
     MDLMNGQASS VTIAATVSEK SSSSESLSEK GSELKKSFDA VVFDVLKVTP EEYAGQITLM
     DVPVFKAIQP DELSSCGWNK KEKYSSAPNA VAFTRRFNHV SFWVVREILH AQTLKIRAEV
     LSHYIKTAKK LYELNNLHAL MAVVSGLQSA PIFRLTKTWA LLSRKDKTTF EKLEYVMSKE
     DNYKRLRDYI SSLKMTPCIP YLGIYLSDLT YIDSAYPSTG SILENEQRSN LMNNILRIIS
     DLQQSCEYDI PILPHVQKYL NSVQYIEELQ KFVEDDNYKL SLKIEPGAST PRSAASREDL
     AGPDIGASPQ GGRKSSAAAA AAAAAEGALL PQTPPSPRNL IPHGHRKCHS LGYNFIHKMN
     TAEFKSATFP NAGPRHLLDD SVMEPHAPSR GQAESSTLSS GISIGSSDGS ELSEETSWPA
     FERNRLYHSL GPVTRVPRNG YRSHTKASSS AESEDLAVHL YPGAVTIQGV LRRKTLLKEG
     KKPTVASWTK YWAALCGTQL FYYAAKSLKA TERKHFKSTS NKNVSVVGWM VMMADDPEHP
     DLFLLTDSEK GNSYKFQAGS RMNAMLWFKH LSAACQSNKQ QVPTNLMTFE
//
ID   TBB3_MOUSE              Reviewed;         450 AA.
AC   Q9ERD7; Q3UF42; Q5I036;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Tubulin beta-3 chain;
GN   Name=Tubb3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wu Y., Li C., Zhao S.;
RT   "Cloning and sequencing of mouse tubulin beta-3 isotype.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Embryo, Spinal ganglion, and Sympathetic ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 63-77; 104-121; 217-251; 253-276; 310-318; 337-350
RP   AND 381-390, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   POLYGLUTAMYLATION.
RX   PubMed=15890843; DOI=10.1126/science.1113010;
RA   Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M.,
RA   Temurak N., van Dijk J., Boucher D., van Dorsselaer A.,
RA   Suryavanshi S., Gaertig J., Edde B.;
RT   "Tubulin polyglutamylase enzymes are members of the TTL domain protein
RT   family.";
RL   Science 308:1758-1762(2005).
RN   [6]
RP   POLYGLYCYLATION.
RX   PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA   Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M.,
RA   Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J.,
RA   Janke C.;
RT   "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT   polyglycylation.";
RL   Cell 137:1076-1087(2009).
RN   [7]
RP   FUNCTION, AND MUTAGENESIS OF ARG-262.
RX   PubMed=20074521; DOI=10.1016/j.cell.2009.12.011;
RA   Tischfield M.A., Baris H.N., Wu C., Rudolph G., Van Maldergem L.,
RA   He W., Chan W.M., Andrews C., Demer J.L., Robertson R.L., Mackey D.A.,
RA   Ruddle J.B., Bird T.D., Gottlob I., Pieh C., Traboulsi E.I.,
RA   Pomeroy S.L., Hunter D.G., Soul J.S., Newlin A., Sabol L.J.,
RA   Doherty E.J., de Uzcategui C.E., de Uzcategui N., Collins M.L.,
RA   Sener E.C., Wabbels B., Hellebrand H., Meitinger T., de Berardinis T.,
RA   Magli A., Schiavi C., Pastore-Trossello M., Koc F., Wong A.M.,
RA   Levin A.V., Geraghty M.T., Descartes M., Flaherty M., Jamieson R.V.,
RA   Moller H.U., Meuthen I., Callen D.F., Kerwin J., Lindsay S.,
RA   Meindl A., Gupta M.L. Jr., Pellman D., Engle E.C.;
RT   "Human TUBB3 mutations perturb microtubule dynamics, kinesin
RT   interactions, and axon guidance.";
RL   Cell 140:74-87(2010).
CC   -!- FUNCTION: Tubulin is the major constituent of microtubules. It
CC       binds two moles of GTP, one at an exchangeable site on the beta
CC       chain and one at a non-exchangeable site on the alpha-chain. TUBB3
CC       plays a critical role in proper axon guidance and mantainance.
CC   -!- SUBUNIT: Dimer of alpha and beta chains.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- DOMAIN: The highly acidic C-terminal region may bind cations such
CC       as calcium.
CC   -!- PTM: Some glutamate residues at the C-terminus are either
CC       polyglutamylated or polyglycylated. These 2 modifications occur
CC       exclusively on glutamate residues and result in either
CC       polyglutamate or polyglycine chains on the gamma-carboxyl group.
CC       Glycylation is mainly limited to tubulin incorporated into
CC       axonemes (cilia and flagella) whereas glutamylation is prevalent
CC       in neuronal cells, centrioles, axonemes, and the mitotic spindle.
CC       Both modifications can coexist on the same protein on adjacent
CC       residues, and lowering polyglycylation levels increases
CC       polyglutamylation, and reciprocally. The precise function of such
CC       modifications is still unclear but they are regulate the assembly
CC       and dynamics of axonemal microtubules.
CC   -!- SIMILARITY: Belongs to the tubulin family.
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DR   EMBL; AF312873; AAG26010.1; -; mRNA.
DR   EMBL; AK012528; BAB28299.1; -; mRNA.
DR   EMBL; AK051298; BAC34596.1; -; mRNA.
DR   EMBL; AK149014; BAE28719.1; -; mRNA.
DR   EMBL; BC031357; AAH31357.1; -; mRNA.
DR   EMBL; BC088749; AAH88749.1; -; mRNA.
DR   IPI; IPI00112251; -.
DR   RefSeq; NP_075768.1; NM_023279.2.
DR   UniGene; Mm.40068; -.
DR   ProteinModelPortal; Q9ERD7; -.
DR   SMR; Q9ERD7; 2-427.
DR   DIP; DIP-48419N; -.
DR   STRING; Q9ERD7; -.
DR   PhosphoSite; Q9ERD7; -.
DR   REPRODUCTION-2DPAGE; IPI00112251; -.
DR   REPRODUCTION-2DPAGE; Q9ERD7; -.
DR   UCD-2DPAGE; Q9ERD7; -.
DR   PRIDE; Q9ERD7; -.
DR   Ensembl; ENSMUST00000071134; ENSMUSP00000071134; ENSMUSG00000062380.
DR   GeneID; 22152; -.
DR   KEGG; mmu:22152; -.
DR   UCSC; uc009nvt.1; mouse.
DR   CTD; 22152; -.
DR   MGI; MGI:107813; Tubb3.
DR   eggNOG; maNOG13588; -.
DR   GeneTree; ENSGT00600000084255; -.
DR   HOGENOM; HBG750007; -.
DR   HOVERGEN; HBG000089; -.
DR   InParanoid; Q9ERD7; -.
DR   OMA; VIDVLTC; -.
DR   OrthoDB; EOG4W6NW0; -.
DR   PhylomeDB; Q9ERD7; -.
DR   NextBio; 302066; -.
DR   ArrayExpress; Q9ERD7; -.
DR   Bgee; Q9ERD7; -.
DR   CleanEx; MM_TUBB3; -.
DR   Genevestigator; Q9ERD7; -.
DR   GermOnline; ENSMUSG00000062380; Mus musculus.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0007411; P:axon guidance; IMP:UniProtKB.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   GO; GO:0051258; P:protein polymerization; IEA:InterPro.
DR   InterPro; IPR013838; Beta-tubulin_BS.
DR   InterPro; IPR002453; Beta_tubulin.
DR   InterPro; IPR008280; Tub_FtsZ_C.
DR   InterPro; IPR000217; Tubulin.
DR   InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR   InterPro; IPR023123; Tubulin_C.
DR   InterPro; IPR017975; Tubulin_CS.
DR   InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR   Gene3D; G3DSA:3.30.1330.20; Tubulin/FtsZ_2-layer-sand-dom; 1.
DR   Gene3D; G3DSA:1.10.287.600; Tubulin_C; 1.
DR   Gene3D; G3DSA:3.40.50.1440; Tubulin_FtsZ; 1.
DR   PANTHER; PTHR11588; Tubulin; 1.
DR   Pfam; PF00091; Tubulin; 1.
DR   Pfam; PF03953; Tubulin_C; 1.
DR   PRINTS; PR01163; BETATUBULIN.
DR   PRINTS; PR01161; TUBULIN.
DR   SMART; SM00864; Tubulin; 1.
DR   SMART; SM00865; Tubulin_C; 1.
DR   SUPFAM; SSF55307; Tub_FtsZ_C; 1.
DR   SUPFAM; SSF52490; Tubulin_FtsZ; 1.
DR   PROSITE; PS00227; TUBULIN; 1.
DR   PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   GTP-binding; Microtubule; Nucleotide-binding.
FT   CHAIN         1    450       Tubulin beta-3 chain.
FT                                /FTId=PRO_0000048251.
FT   NP_BIND     140    146       GTP (Potential).
FT   MOD_RES      58     58       N6-acetyllysine (By similarity).
FT   MUTAGEN     262    262       R->C: Brain from homozygous mice shows
FT                                defects in the guidance of commissural
FT                                axons and nerves, without evidence of
FT                                cortical cells migration defects.
FT   CONFLICT    206    206       A -> S (in Ref. 2; BAE28719).
SQ   SEQUENCE   450 AA;  50419 MW;  4B9D9B7DBA102949 CRC64;
     MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPSGNYVGDS DLQLERISVY YNEASSHKYV
     PRAILVDLEP GTMDSVRSGA FGHLFRPDNF IFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
     RKECENCDCL QGFQLTHSLG GGTGSGMGTL LISKVREEYP DRIMNTFSVV PSPKVSDTVV
     EPYNATLSIH QLVENTDETY CIDNEALYDI CFRTLKLATP TYGDLNHLVS ATMSGVTTSL
     RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTARGSQQ YRALTVPELT QQMFDAKNMM
     AACDPRHGRY LTVATVFRGR MSMKEVDEQM LAIQSKNSSY FVEWIPNNVK VAVCDIPPRG
     LKMSSTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
     EYQQYQDATA EEEGEMYEDD DEESEAQGPK
//
ID   MESD1_MOUSE             Reviewed;         362 AA.
AC   Q9ERE8; Q542D0;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Mesoderm development candidate 1;
GN   Name=Mesdc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=129/SvJ;
RX   MEDLINE=21145589; PubMed=11247670; DOI=10.1006/geno.2000.6466;
RA   Wines M.E., Lee L., Katari M.S., Zhang L., DeRossi C., Shi Y.,
RA   Perkins S., Feldman M., McCombie W.R., Holdener B.C.;
RT   "Identification of mesoderm development (mesd) candidate genes by
RT   comparative mapping and genome sequence analysis.";
RL   Genomics 72:88-98(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Heart, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
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DR   EMBL; AF311213; AAG33620.1; -; Genomic_DNA.
DR   EMBL; AK084510; BAC39204.1; -; mRNA.
DR   EMBL; AK089082; BAC40740.1; -; mRNA.
DR   EMBL; AK162446; BAE36922.1; -; mRNA.
DR   EMBL; BC018326; AAH18326.1; -; mRNA.
DR   IPI; IPI00112306; -.
DR   RefSeq; NP_109630.1; NM_030705.4.
DR   UniGene; Mm.272998; -.
DR   ProteinModelPortal; Q9ERE8; -.
DR   SMR; Q9ERE8; 40-348.
DR   MINT; MINT-3369867; -.
DR   STRING; Q9ERE8; -.
DR   PhosphoSite; Q9ERE8; -.
DR   PRIDE; Q9ERE8; -.
DR   Ensembl; ENSMUST00000094216; ENSMUSP00000091769; ENSMUSG00000070462.
DR   GeneID; 80889; -.
DR   KEGG; mmu:80889; -.
DR   UCSC; uc009idw.1; mouse.
DR   CTD; 80889; -.
DR   MGI; MGI:1891420; Mesdc1.
DR   eggNOG; roNOG04581; -.
DR   GeneTree; ENSGT00550000074542; -.
DR   HOGENOM; HBG446710; -.
DR   HOVERGEN; HBG052459; -.
DR   InParanoid; Q9ERE8; -.
DR   OMA; SVCDHCK; -.
DR   OrthoDB; EOG4X97HK; -.
DR   PhylomeDB; Q9ERE8; -.
DR   NextBio; 350215; -.
DR   ArrayExpress; Q9ERE8; -.
DR   Bgee; Q9ERE8; -.
DR   CleanEx; MM_MESDC1; -.
DR   Genevestigator; Q9ERE8; -.
DR   GermOnline; ENSMUSG00000070462; Mus musculus.
DR   InterPro; IPR015710; Talin-rel.
DR   PANTHER; PTHR19981; Talin; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    362       Mesoderm development candidate 1.
FT                                /FTId=PRO_0000096442.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      10     10       Phosphothreonine.
SQ   SEQUENCE   362 AA;  37786 MW;  EFE9BBFC09BB7CB5 CRC64;
     MASGSAGKPT GEAASPAPGS AVGGASSQPR KRLVSICDHC KGKMQLVADL LLLSSEARPV
     LFEGPASPGA GAESFEQCRD TIIARTKGLS ILTHDVQSQL NMGRFGEAGD SLVELGDLVV
     SLTECSAHAA YLAAVATPGA QPAQPGLVDR YRVTRCRHEV EQGCAVLRAT PLADMTPQLL
     LEVSQGLSRN LKFLTDACAL ASDKSRDRFS REQFKLGVKC MSTSASALLA CVREVKAAPS
     ELARSRCALF SGPLVQAVSA LVGFATEPQF LGRAAAVSTE GKAVQTAILG GAMSVVSACV
     LLTQCLRDLA QHPDGSAKMS DHRERLRNSA CAVSEGCTLL SQALRERSSP RTLPPVNSNS
     VN
//
ID   JIP2_MOUSE              Reviewed;         830 AA.
AC   Q9ERE9; Q9CXI4;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=C-Jun-amino-terminal kinase-interacting protein 2;
DE            Short=JIP-2;
DE            Short=JNK-interacting protein 2;
DE   AltName: Full=Islet-brain-2;
DE            Short=IB-2;
DE   AltName: Full=JNK MAP kinase scaffold protein 2;
DE   AltName: Full=Mitogen-activated protein kinase 8-interacting protein 2;
GN   Name=Mapk8ip2; Synonyms=Ib2, Jip2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH APOER2.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=20400499; PubMed=10827199; DOI=10.1074/jbc.M004119200;
RA   Stockinger W., Brandes C., Fasching D., Hermann M., Gotthardt M.,
RA   Herz J., Schneider W.J., Nimpf J.;
RT   "The reelin receptor ApoER2 recruits JNK-interacting proteins-1 and
RT   -2.";
RL   J. Biol. Chem. 275:25625-25632(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: The JNK-interacting protein (JIP) group of scaffold
CC       proteins selectively mediates JNK signaling by aggregating
CC       specific components of the MAPK cascade to form a functional JNK
CC       signaling module. JIP2 inhibits IL1 beta-induced apoptosis in
CC       insulin-secreting cells (By similarity).
CC   -!- SUBUNIT: Forms homo-or heterooligomeric complexes. Binds specific
CC       components of the JNK signaling pathway namely JNK, MAPKK7 and
CC       MLK2, MLK3 and DLK (By similarity). Also binds the proline-rich
CC       domain-containing splice variant of apolipoprotein E receptor 2
CC       (ApoER2). Binds the TPR motif-containing C-terminal of kinesin
CC       light chain. Binds the cytoplasmic tails of LRP1 and LRP2
CC       (Megalin).
CC   -!- INTERACTION:
CC       P14599:Appl (xeno); NbExp=2; IntAct=EBI-74576, EBI-74135;
CC       Q91ZX7:Lrp1; NbExp=1; IntAct=EBI-74576, EBI-300955;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Accumulates in cell surface
CC       projections (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain. Expressed in all
CC       neurons. Also expressed in testis, primarily in the epididymal
CC       epidermis.
CC   -!- INDUCTION: Upon neuron differentiation.
CC   -!- SIMILARITY: Belongs to the JIP scaffold family.
CC   -!- SIMILARITY: Contains 1 PID domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AK014339; Type=Erroneous termination; Positions=701; Note=Translated as Cys;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF310135; AAG31800.1; -; mRNA.
DR   EMBL; AK014339; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00112307; -.
DR   RefSeq; NP_068740.3; NM_021921.3.
DR   UniGene; Mm.173337; -.
DR   ProteinModelPortal; Q9ERE9; -.
DR   SMR; Q9ERE9; 612-666, 687-820.
DR   IntAct; Q9ERE9; 8.
DR   STRING; Q9ERE9; -.
DR   PhosphoSite; Q9ERE9; -.
DR   PRIDE; Q9ERE9; -.
DR   Ensembl; ENSMUST00000023291; ENSMUSP00000023291; ENSMUSG00000022619.
DR   GeneID; 60597; -.
DR   KEGG; mmu:60597; -.
DR   CTD; 60597; -.
DR   MGI; MGI:1926555; Mapk8ip2.
DR   GeneTree; ENSGT00390000003908; -.
DR   HOGENOM; HBG713638; -.
DR   HOVERGEN; HBG018568; -.
DR   InParanoid; Q9ERE9; -.
DR   OMA; SDPGIEA; -.
DR   OrthoDB; EOG4Q84X6; -.
DR   PhylomeDB; Q9ERE9; -.
DR   ArrayExpress; Q9ERE9; -.
DR   Bgee; Q9ERE9; -.
DR   Genevestigator; Q9ERE9; -.
DR   GermOnline; ENSMUSG00000022619; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IDA:BHF-UCL.
DR   GO; GO:0019894; F:kinesin binding; IPI:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR   GO; GO:0001662; P:behavioral fear response; IMP:BHF-UCL.
DR   GO; GO:0048813; P:dendrite morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0007254; P:JNK cascade; IDA:MGI.
DR   GO; GO:0007617; P:mating behavior; IMP:BHF-UCL.
DR   GO; GO:0046958; P:nonassociative learning; IMP:BHF-UCL.
DR   GO; GO:0060079; P:regulation of excitatory postsynaptic membrane potential; IMP:BHF-UCL.
DR   GO; GO:0046328; P:regulation of JNK cascade; ISS:UniProtKB.
DR   GO; GO:0010469; P:regulation of receptor activity; IMP:BHF-UCL.
DR   GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IMP:BHF-UCL.
DR   GO; GO:0035176; P:social behavior; IMP:BHF-UCL.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00640; PID; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS01179; PID; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; SH3 domain.
FT   CHAIN         1    830       C-Jun-amino-terminal kinase-interacting
FT                                protein 2.
FT                                /FTId=PRO_0000220632.
FT   DOMAIN      610    671       SH3.
FT   DOMAIN      683    819       PID.
FT   REGION      111    278       JNK-binding domain (JBD).
FT   COMPBIAS     30     36       Asp/Glu-rich (acidic).
FT   COMPBIAS     85    104       Asp/Glu-rich (acidic).
FT   COMPBIAS    154    157       Poly-Asn.
FT   COMPBIAS    282    293       Ser-rich.
FT   COMPBIAS    420    437       Pro-rich.
FT   COMPBIAS    472    487       Asp/Glu-rich (acidic).
FT   CONFLICT    216    216       P -> Q (in Ref. 2; AK014339).
SQ   SEQUENCE   830 AA;  89900 MW;  7EC8EAD19A90163C CRC64;
     MADRAEMFSL STFHSLSPPG CRPPQDISLE EFDDEDLSEI TDDCGLGLSY DSDHCEKDSL
     SLGRSEQPHP ICSFQDDFQE FEMIDDNEEE DDEEEEEEEE EEEDGDRQGK AGGGPGSQAL
     AGDSLIPSPS LEESHKLRPT TLHLTTLGAQ DSLNNNNGGF TSAPPSSWQE TVLRSPAQEP
     LKELPAPLLP AEEERHEVQS LARPGCDCEG NQPPEPPASS GGASPSSDPG IEADLRSHSS
     GGHEGRRSSQ ELSSPGSDSE DAGGARLGRM ISSISETELE LSSDGGSSSG RSSHLTNSIE
     EASSPASEPE PEPEPLHEPP RRPAFLPVGQ DDTNSEYESG SESEPDLSED ADSPWLLSNL
     VSRMISEGSS PIRCPGQCLS PAPRLPEEAA SQANSVPQDC QDPEAGPHVE LVDMDTLCGP
     PPPAPAAPRL GPAQPGPCLF LSNPTRDTIT PLWATPGRTA RPGRSCSAAC SEEEEEDEEE
     DEEDEEDAED SVVPPGSRTT GSTAPLDASL VYDAVKYTLV VDEHTQLELV SLRRCAGLGN
     DSEEDSSCEA SEEEAGATLL GSDQVPEDAS PDSPDLTFSK KFLNVFVNST SRSSSTESFG
     LFSCVVNGEE REQTHRAVFR FIPRHPDELE LDVDDPVLVE AEEDDFWFRG FNMRTGERGV
     FPAFYAHAVP GPAKDLLGSK RSPCWVDRFD VQFLGSVEVP CHQGNGILCA AMQKIATARK
     LTVHLRPPAS CDLEISLRGV KLSLSGGGPE FQRCSHFFQM KNISFCGCHP RNSCYFGFIT
     KHPLLSRFAC HVFVSQESMR PVARSVGRAF LEYYQEHLAF ACPTEDIYLE
//
ID   LIMA1_MOUSE             Reviewed;         753 AA.
AC   Q9ERG0; Q9ERG1;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   05-MAR-2002, sequence version 2.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=LIM domain and actin-binding protein 1;
DE   AltName: Full=Epithelial protein lost in neoplasm;
DE            Short=mEPLIN;
GN   Name=Lima1; Synonyms=D15Ertd366e, Eplin;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
RX   MEDLINE=21100452; PubMed=11179679; DOI=10.1016/S0378-1119(00)00540-0;
RA   Maul R.S., Sachi Gerbin C., Chang D.D.;
RT   "Characterization of mouse epithelial protein lost in neoplasm (EPLIN)
RT   and comparison of mammalian and zebrafish EPLIN.";
RL   Gene 262:155-160(2001).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-539, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225; SER-230; SER-367;
RP   SER-485; SER-488 AND SER-615, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225; SER-230; SER-467
RP   AND SER-488, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-735, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Binds to actin monomers and filaments. Increases the
CC       number and size of actin stress fibers and inhibits membrane
CC       ruffling. Inhibits actin filament depolymerization. Bundles actin
CC       filaments, delays filament nucleation and reduces formation of
CC       branched filaments (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
CC       Note=This cytoskeletal protein colocalizes with actin stress
CC       fibers.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage; Named isoforms=2;
CC       Name=Beta;
CC         IsoId=Q9ERG0-1; Sequence=Displayed;
CC       Name=Alpha;
CC         IsoId=Q9ERG0-2; Sequence=VSP_003118;
CC   -!- TISSUE SPECIFICITY: Isoform Alpha is highly expressed in embryos
CC       from day 7-11 and in adult spleen and lung. Isoform Beta
CC       expression is highest in adult kidney, testis, lung and liver,
CC       intermediate in heart, brain, spleen, skeletal muscle and low in
CC       embryos.
CC   -!- DOMAIN: Contains at least 2 actin-binding domains, one on each
CC       side of the LIM domain. Both domains bind actin monomers and
CC       filaments. The C-terminal domain binds filaments more efficiently
CC       than the N-terminus (By similarity).
CC   -!- SIMILARITY: Contains 1 LIM zinc-binding domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF307844; AAG31147.1; -; mRNA.
DR   EMBL; AF307845; AAG31148.1; -; mRNA.
DR   IPI; IPI00112339; -.
DR   IPI; IPI00759925; -.
DR   RefSeq; NP_001107017.1; NM_001113545.1.
DR   UniGene; Mm.33207; -.
DR   ProteinModelPortal; Q9ERG0; -.
DR   SMR; Q9ERG0; 372-455.
DR   DIP; DIP-29634N; -.
DR   DIP; DIP-29637N; -.
DR   STRING; Q9ERG0; -.
DR   PhosphoSite; Q9ERG0; -.
DR   PRIDE; Q9ERG0; -.
DR   Ensembl; ENSMUST00000073691; ENSMUSP00000073371; ENSMUSG00000023022.
DR   Ensembl; ENSMUST00000109024; ENSMUSP00000104652; ENSMUSG00000023022.
DR   GeneID; 65970; -.
DR   KEGG; mmu:65970; -.
DR   CTD; 65970; -.
DR   MGI; MGI:1920992; Lima1.
DR   GeneTree; ENSGT00510000046839; -.
DR   HOGENOM; HBG713294; -.
DR   HOVERGEN; HBG051492; -.
DR   InParanoid; Q9ERG0; -.
DR   OrthoDB; EOG44XJG7; -.
DR   NextBio; 320412; -.
DR   ArrayExpress; Q9ERG0; -.
DR   Bgee; Q9ERG0; -.
DR   CleanEx; MM_LIMA1; -.
DR   Genevestigator; Q9ERG0; -.
DR   GermOnline; ENSMUSG00000023022; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR   GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
DR   GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR   GO; GO:0003785; F:actin monomer binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
DR   GO; GO:0030835; P:negative regulation of actin filament depolymerization; ISS:UniProtKB.
DR   GO; GO:0031529; P:ruffle organization; ISS:UniProtKB.
DR   InterPro; IPR001781; Znf_LIM.
DR   Gene3D; G3DSA:2.10.110.10; Znf_LIM; 1.
DR   Pfam; PF00412; LIM; 1.
DR   SMART; SM00132; LIM; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative promoter usage; Cytoplasm; Cytoskeleton;
KW   LIM domain; Metal-binding; Phosphoprotein; Zinc.
FT   CHAIN         1    753       LIM domain and actin-binding protein 1.
FT                                /FTId=PRO_0000075731.
FT   DOMAIN      386    446       LIM zinc-binding.
FT   MOD_RES      15     15       Phosphoserine (By similarity).
FT   MOD_RES     132    132       Phosphoserine (By similarity).
FT   MOD_RES     225    225       Phosphoserine.
FT   MOD_RES     230    230       Phosphoserine.
FT   MOD_RES     263    263       Phosphoserine (By similarity).
FT   MOD_RES     360    360       Phosphoserine (By similarity).
FT   MOD_RES     366    366       Phosphoserine (By similarity).
FT   MOD_RES     367    367       Phosphoserine.
FT   MOD_RES     371    371       Phosphoserine (By similarity).
FT   MOD_RES     372    372       Phosphoserine (By similarity).
FT   MOD_RES     467    467       Phosphoserine.
FT   MOD_RES     485    485       Phosphoserine.
FT   MOD_RES     488    488       Phosphoserine.
FT   MOD_RES     539    539       Phosphoserine.
FT   MOD_RES     602    602       Phosphoserine (By similarity).
FT   MOD_RES     607    607       Phosphoserine (By similarity).
FT   MOD_RES     615    615       Phosphoserine.
FT   MOD_RES     617    617       Phosphoserine (By similarity).
FT   MOD_RES     620    620       Phosphoserine (By similarity).
FT   MOD_RES     692    692       Phosphoserine (By similarity).
FT   MOD_RES     735    735       Phosphoserine.
FT   MOD_RES     746    746       Phosphotyrosine (By similarity).
FT   VAR_SEQ       1    160       Missing (in isoform Alpha).
FT                                /FTId=VSP_003118.
FT   CONFLICT    216    216       S -> N (in Ref. 1; AAG31148).
FT   CONFLICT    325    325       A -> T (in Ref. 1; AAG31148).
FT   CONFLICT    486    486       P -> S (in Ref. 1; AAG31147).
FT   CONFLICT    499    499       V -> A (in Ref. 1; AAG31147).
FT   CONFLICT    538    538       S -> G (in Ref. 1; AAG31148).
FT   CONFLICT    605    605       T -> A (in Ref. 1; AAG31148).
SQ   SEQUENCE   753 AA;  84090 MW;  9A4692E86DF4A2AF CRC64;
     MESTPFNRRQ WTSLSLRVTA KELSLVNKNK SSAIVEIFSK YQKAAEEANM ERKKNNPESL
     PQHFRRGTLS VLKKKWENPV AGAEFHTDSL PNSSSEGGHT ADYPPAEVTD KPAPGVRADR
     EEHTQPKPRF GSRPEAVIQS RYPRSENSHD FKAQATESQK MENCLGDSRH EAEKPETSEN
     TETSGKIEKY NVPLNRLKMM FEKGEHNQTK SLWTQSRNAG GRRLSENNCS LDDWEIGAGH
     LSSSAFNSEK NESKRNLELP RLSETSIKDR MAKYQAAVSK QSSPASYTNE LKTSESKTHK
     WEQKENVPPG PEACSVHQEG SKVSATENSL VALSVPAEDD TCNSQVKSEA QQPMHPKPLS
     PDARTSSLPE SSPSKTAKKF QAPAKESCVE CQKTVYPMER LLANQQVFHI SCFRCSYCNN
     KLSLGTYASL HGRIYCKPHF NQLFKSKGNY DEGFGHKQHK DLWASKSDNE ETLGRPAQPP
     NAGESPHSPG VEDAPIAKVG VLAASMEAKA SSQREREDKP AETKKLRIAW PPPAELGSSG
     SALEEGIKVS KPKWPPEDDV CKTEAPEDVD LDLKKLRRSS SLKERSRPFT VAASFRTSSI
     KSPKTSSPSL RKGWSESEQS EEFGGGIATM ERKQTENARP SGEKENVGKS RWQGEEVPRS
     KDRSSFELES ENFMENGANI AEDDNHVHAQ QSPLEPEAPG WSGFVDTTAA KEFTTQNQKS
     QDVGFWEGEV VRELSVEEQI KRNRYYDEDE DEE
//
ID   STRN3_MOUSE             Reviewed;         796 AA.
AC   Q9ERG2;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Striatin-3;
DE   AltName: Full=Cell cycle autoantigen SG2NA;
DE   AltName: Full=S/G2 antigen;
GN   Name=Strn3; Synonyms=Gs2na, Sg2na;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Castets F., Rakitina T.;
RT   "Expression analysis of SG2NA isoform.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=20347911; PubMed=10748158; DOI=10.1074/jbc.M909782199;
RA   Castets F., Rakitina T., Gaillard S., Moqrich A., Mattei M.-G.,
RA   Monneron A.;
RT   "Zinedin, SG2NA, and striatin are calmodulin-binding, WD repeat
RT   proteins principally expressed in the brain.";
RL   J. Biol. Chem. 275:19970-19977(2000).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229 AND SER-257, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Binds calmodulin in a calcium dependent manner. May
CC       function as scaffolding or signaling protein (By similarity).
CC   -!- SUBUNIT: Interacts with protein phosphatase 2A (PP2A) (Potential).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Mainly expressed in the brain and muscles but
CC       is also detected at low levels in various tissues such as kidney,
CC       spleen and lung.
CC   -!- SIMILARITY: Belongs to the WD repeat striatin family.
CC   -!- SIMILARITY: Contains 6 WD repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF307777; AAG24454.1; -; mRNA.
DR   IPI; IPI00229990; -.
DR   RefSeq; NP_443205.1; NM_052973.2.
DR   UniGene; Mm.65979; -.
DR   ProteinModelPortal; Q9ERG2; -.
DR   SMR; Q9ERG2; 442-795.
DR   STRING; Q9ERG2; -.
DR   PhosphoSite; Q9ERG2; -.
DR   PRIDE; Q9ERG2; -.
DR   Ensembl; ENSMUST00000013130; ENSMUSP00000013130; ENSMUSG00000020954.
DR   GeneID; 94186; -.
DR   KEGG; mmu:94186; -.
DR   UCSC; uc007nmt.1; mouse.
DR   CTD; 94186; -.
DR   MGI; MGI:2151064; Strn3.
DR   GeneTree; ENSGT00520000055597; -.
DR   HOGENOM; HBG385782; -.
DR   HOVERGEN; HBG007117; -.
DR   InParanoid; Q9ERG2; -.
DR   OMA; NHINRVV; -.
DR   OrthoDB; EOG4TMR1P; -.
DR   NextBio; 352151; -.
DR   ArrayExpress; Q9ERG2; -.
DR   Bgee; Q9ERG2; -.
DR   CleanEx; MM_STRN3; -.
DR   Genevestigator; Q9ERG2; -.
DR   GermOnline; ENSMUSG00000020954; Mus musculus.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR013258; Striatin_N.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF08232; Striatin; 1.
DR   Pfam; PF00400; WD40; 5.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 2.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Calmodulin-binding; Coiled coil; Cytoplasm; Membrane; Phosphoprotein;
KW   Repeat; WD repeat.
FT   CHAIN         1    796       Striatin-3.
FT                                /FTId=PRO_0000051237.
FT   REPEAT      477    516       WD 1.
FT   REPEAT      530    569       WD 2.
FT   REPEAT      583    622       WD 3.
FT   REPEAT      678    717       WD 4.
FT   REPEAT      720    759       WD 5.
FT   REPEAT      766    795       WD 6.
FT   REGION       71     79       Caveolin-binding (Potential).
FT   REGION      166    183       Calmodulin-binding (Potential).
FT   COILED       77    136       Potential.
FT   COMPBIAS      6     13       Poly-Gly.
FT   MOD_RES     229    229       Phosphoserine.
FT   MOD_RES     257    257       Phosphoserine.
SQ   SEQUENCE   796 AA;  87150 MW;  161FAF5DDEBE23DD CRC64;
     MDELAGGGGG GQGMAAPPRP QQGPGGNLSL PPGANGAPGG GGPPAAEAAG PPAGPELSRP
     QQYTIPGILH YIQHEWARFE MERAHWEVER AELQARIAFL QGERKGQENL KKDLVRRIKM
     LEYALKQERA KYHKLKYGTE LNQGDLKMPT FESEETKDVE APPAPQNSQL TWKQGRQLLR
     QYLQEVGYTD TILDVRSQRV RSLLGLSNSE PNGSVEAKNL EQILNGGESP KQKGQEIKRP
     PGDVLETFNF LENADDSDEE ENDMIEGIPE GKDKLRIHKH KIGNEGLAAD LTDDPDTEEA
     LKEFDFLVTA EDGEGAGEAR SSGDGTEWDK DDLSPTAEVW DVDQGLISKL KEQYKKERKG
     KKGVKRVNRT NLCDMITDLG DDELPHIPSG IINQSRSAST RMADHEGARA EEAEPITFPS
     GGGKSFIMGS DDVLLSVLGL GDLADLTVTN DADYSYDLPA NKDAFRKTWN PKYTLRSHFD
     GVRALAFHPV EPVLVTASED HTLKLWNLQK TVPAKKSASL DVEPIYTFRA HIGPVLSLAI
     SSNGEQCFSG GIDATIQWWN MPSPNVDPYD TYESNVLAGT LVAHTDAVWG LAYSGIKNQL
     LSCSADGTIR LWNPQEKLPC VCTYNGDKEH GIPTSVDFIG CDPAHMVTSF NTGSAVIYDL
     ETSQSLVMLS SQVDSGLQSS NHINRVVSHP TLPVTITAHE DRHIKFFDNK TGKMIHSMVA
     HLDAVTSLAV DPNGIYLMSG SHDCSIRLWN LDSKTCVQEI TAHRKKLDES IYDVAFHPSK
     AYIASAGADA LAKVFV
//
ID   HIPK3_MOUSE             Reviewed;        1192 AA.
AC   Q9ERH7; O88906; Q9QZR2;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Homeodomain-interacting protein kinase 3;
DE            EC=2.7.11.1;
DE   AltName: Full=Androgen receptor-interacting nuclear protein kinase;
DE            Short=ANPK;
DE   AltName: Full=Fas-interacting serine/threonine-protein kinase;
DE            Short=FIST;
DE   AltName: Full=Nuclear body-associated kinase 3;
DE            Short=Nbak3;
GN   Name=Hipk3; Synonyms=Fist3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH NKX1-2.
RC   STRAIN=BALB/c;
RX   MEDLINE=98421509; PubMed=9748262; DOI=10.1074/jbc.273.40.25875;
RA   Kim Y.H., Choi C.Y., Lee S.-J., Conti M.A., Kim Y.;
RT   "Homeodomain-interacting protein kinases, a novel family of co-
RT   repressors for homeodomain transcription factors.";
RL   J. Biol. Chem. 273:25875-25879(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH FAS AND DAXX,
RP   IDENTIFICATION IN A COMPLEX WITH FAS AND FADD, TISSUE SPECIFICITY,
RP   SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF LYS-226 AND
RP   ASP-322.
RC   STRAIN=CD-1; TISSUE=Testis;
RX   MEDLINE=20490849; PubMed=11034606; DOI=10.1084/jem.192.8.1165;
RA   Rochat-Steiner V., Becker K., Micheau O., Schneider P., Burns K.,
RA   Tschopp J.;
RT   "FIST/HIPK3: a Fas/FADD-interacting serine/threonine kinase that
RT   induces FADD phosphorylation and inhibits Fas-mediated Jun NH2-
RT   terminal kinase activation.";
RL   J. Exp. Med. 192:1165-1174(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Sather S.L., Johnson N.L., Johnson G.L.;
RT   "Protein kinases associated with PML/CBP nuclear bodies and
RT   filamentous threads regulate transcription and inhibit cell growth.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   INTERACTION WITH AR, AND SUBCELLULAR LOCATION.
RX   MEDLINE=98395052; PubMed=9725910;
RA   Moilanen A.-M., Karvonen U., Poukka H., Jaenne O.A., Palvimo J.J.;
RT   "Activation of androgen receptor function by a novel nuclear protein
RT   kinase.";
RL   Mol. Biol. Cell 9:2527-2543(1998).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-359, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Seems to negatively regulate apoptosis by promoting FADD
CC       phosphorylation. Enhances androgen receptor-mediated
CC       transcription. May act as a transcriptional corepressor for NK
CC       homeodomain transcription factors.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts with UBL1/SUMO-1 (By similarity). Interacts
CC       with and stabilizes ligand-bound androgen receptor (AR). Interacts
CC       with Nkx1-2. Interacts with FAS and DAXX. Probably part of a
CC       complex consisting of HIPK3, FAS and FADD.
CC   -!- INTERACTION:
CC       O35613:Daxx; NbExp=1; IntAct=EBI-524356, EBI-77304;
CC       Q61160:Fadd; NbExp=1; IntAct=EBI-524356, EBI-524415;
CC       P25446:Fas; NbExp=3; IntAct=EBI-524356, EBI-296206;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- TISSUE SPECIFICITY: Heart, skeletal muscle, spleen, testis and
CC       lung.
CC   -!- PTM: Autophosphorylated, but autophosphorylation is not required
CC       for catalytic activity (By similarity).
CC   -!- PTM: May be sumoylated.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. HIPK subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF077660; AAC63012.1; -; mRNA.
DR   EMBL; AF305238; AAG25989.1; -; mRNA.
DR   EMBL; AF170305; AAD52570.1; -; mRNA.
DR   IPI; IPI00754912; -.
DR   PIR; T17089; T17089.
DR   UniGene; Mm.257925; -.
DR   ProteinModelPortal; Q9ERH7; -.
DR   SMR; Q9ERH7; 173-527.
DR   IntAct; Q9ERH7; 5.
DR   STRING; Q9ERH7; -.
DR   PhosphoSite; Q9ERH7; -.
DR   PRIDE; Q9ERH7; -.
DR   Ensembl; ENSMUST00000028600; ENSMUSP00000028600; ENSMUSG00000027177.
DR   Ensembl; ENSMUST00000111124; ENSMUSP00000106753; ENSMUSG00000027177.
DR   MGI; MGI:1314882; Hipk3.
DR   GeneTree; ENSGT00550000074148; -.
DR   HOVERGEN; HBG051908; -.
DR   OrthoDB; EOG4F1X2F; -.
DR   PhylomeDB; Q9ERH7; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 287881; -.
DR   ArrayExpress; Q9ERH7; -.
DR   Bgee; Q9ERH7; -.
DR   CleanEx; MM_HIPK3; -.
DR   Genevestigator; Q9ERH7; -.
DR   GermOnline; ENSMUSG00000027177; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0043508; P:negative regulation of JUN kinase activity; IMP:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:UniProtKB.
DR   GO; GO:0043388; P:positive regulation of DNA binding; ISS:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Serine/threonine-protein kinase;
KW   Transcription; Transcription regulation; Transferase; Ubl conjugation.
FT   CHAIN         1   1192       Homeodomain-interacting protein kinase 3.
FT                                /FTId=PRO_0000085999.
FT   DOMAIN      197    525       Protein kinase.
FT   NP_BIND     203    211       ATP (By similarity).
FT   REGION      767    921       Interaction with AR (By similarity).
FT   REGION      775    868       Interaction with FAS.
FT   REGION      847    857       Interaction with UBL1 (By similarity).
FT   COMPBIAS    887    939       Ser-rich.
FT   ACT_SITE    322    322       Proton acceptor (By similarity).
FT   BINDING     226    226       ATP (By similarity).
FT   MOD_RES     359    359       Phosphotyrosine.
FT   MUTAGEN     226    226       K->S: Impairs catalytic activity.
FT   MUTAGEN     322    322       D->N: Impairs catalytic activity and
FT                                abolishes interaction with DAXX.
FT   CONFLICT     65     65       K -> N (in Ref. 1; AAC63012).
FT   CONFLICT    405    405       Y -> H (in Ref. 1; AAC63012).
FT   CONFLICT    985    985       G -> D (in Ref. 2; AAG25989).
FT   CONFLICT   1084   1084       A -> D (in Ref. 1; AAC63012).
FT   CONFLICT   1186   1186       L -> V (in Ref. 1; AAC63012).
SQ   SEQUENCE   1192 AA;  130123 MW;  FC27FC0BB3C21190 CRC64;
     MASQVLVYPP YVYQTQSSAF CSVKKLKVEP SGCVFQERTY PQIHVNGRNF GNSHPSTKGS
     AFQTKIPFTK PRGHSFSLQA GAIVVKDTAG ATKVLAAQAQ QAGVEAPRAV VWRNRLHFLE
     GPQRCGLKRK SEELENHSGA MQIVDELSIL PAMLQTNMGN PVTVVTATTG SKQNCTSGEG
     DYQLVQHEVL CSMKNTYEVL DFLGRGTFGQ VVKCWKRGTN EIVAIKILKN HPSYARQGQI
     EVSILARLST ENADEYNFVR AYECFQHRNH TCLVFEMLEQ NLYDFLKQNK FSPLPLKVIR
     PVLQQVATAL KKLKSLGLIH ADLKPENIML VDPVRQPYRV KVIDFGSASH VSKTVCSTYL
     QSRYYRAPEI ILGLPFCEAI DMWSLGCVIA ELFLGWPLYP GALEYDQIRY ISQTQGLPGE
     QLLNVGTKST RFFCRETDMS HSGWRLKTLE EHEAETGMKS KEARKYIFNS LDDIVHVNTV
     MDLEGGDLLA EKADRREFVN LLKKMLLIDA DLRITPIETL NHPFVNMKHL LDFPHSNHVK
     SCFHIMDICK SPSSCETNNH SKMSLLRPVA SNGTAALAAN FTKVGTLRSQ ALTTSAHSVV
     HHGIPLQAGT AQFGCGDAFH QTLIICPPAI QGIPAAHGKP TSYSIRVDNT VPLVTQAPAV
     QPLQIRPGVL SQQTWSGRTQ QMLIPAWQQV TPMAPAAATL TSEGMAGSQR LGDWGKMIPH
     SNHYNSVMPP PLLTNQITLS APQPISVGIA HVVWPQPATT KKNKLCQNRS NSLQNTNIPH
     SAFISPKIIS GKEVEEVSCV DTQDNHTSEG EARTCREASV RQDSSVSDKQ RQTIIIADSP
     SPAVSVITIS SDSDDEETSP RPSLRECKGS LDCEACQSTL NIDRMCSLSS PDSTLSTSSS
     GQSSPSPCKR PNSMSDDEQE SGCETVDGSP TSDSSGHDSP FAENSFVEDA HQNTELGTCA
     GPEAKPAVGT AVEPPVGRES GLSVGEHMAN TDSTCQPLRK GQPAPGKLHQ PPALGARQQK
     PAAAFPQQHL NLSQVQHFGT GHQEWNGNFG HRRQQAYIPT SVTSNPFTLS HGSPNHTAVH
     AHLAGSTHLG GQPTLLPYPS SASLSSAAPV AHLLASPCTS RPMLQHPTYN ISHPSGIVHQ
     VPVGINPRLL PSPTIHQTQY KPIFPPHSYI AASPAYTGFP LSPTKLSQYP YM
//
ID   Q9ERN6_MOUSE            Unreviewed;      4967 AA.
AC   Q9ERN6;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   SubName: Full=Cardiac Ca2+ release channel;
GN   Name=Ryr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=99403027; PubMed=10473538; DOI=10.1074/jbc.274.37.25971;
RA   Zhao M., Li P., Li X., Zhang L., Winkfein R.J., Chen S.R.;
RT   "Molecular identification of the ryanodine receptor pore-forming
RT   segment.";
RL   J. Biol. Chem. 274:25971-25974(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Chen S.W.;
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 1-217.
RX   PubMed=19913485; DOI=10.1016/j.str.2009.08.016;
RA   Lobo P.A., Van Petegem F.;
RT   "Crystal structures of the N-terminal domains of cardiac and skeletal
RT   muscle ryanodine receptors: insights into disease mutations.";
RL   Structure 17:1505-1514(2009).
CC   -!- INTERACTION:
CC       Q9JIF7:Copb1; NbExp=2; IntAct=EBI-643628, EBI-643655;
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DR   EMBL; AF295105; AAG34081.1; -; mRNA.
DR   IPI; IPI00338309; -.
DR   RefSeq; NP_076357.2; NM_023868.2.
DR   UniGene; Mm.239871; -.
DR   PDB; 3IM5; X-ray; 2.55 A; A/B=1-217.
DR   PDB; 3IM6; X-ray; 1.70 A; A=1-217.
DR   PDB; 3IM7; X-ray; 2.21 A; A=1-217.
DR   PDBsum; 3IM5; -.
DR   PDBsum; 3IM6; -.
DR   PDBsum; 3IM7; -.
DR   ProteinModelPortal; Q9ERN6; -.
DR   SMR; Q9ERN6; 12-310, 3581-3607.
DR   IntAct; Q9ERN6; 5.
DR   STRING; Q9ERN6; -.
DR   PhosphoSite; Q9ERN6; -.
DR   PRIDE; Q9ERN6; -.
DR   Ensembl; ENSMUST00000021750; ENSMUSP00000021750; ENSMUSG00000021313.
DR   GeneID; 20191; -.
DR   KEGG; mmu:20191; -.
DR   UCSC; uc007pld.1; mouse.
DR   CTD; 20191; -.
DR   MGI; MGI:99685; Ryr2.
DR   GeneTree; ENSGT00600000084483; -.
DR   HOGENOM; HBG315203; -.
DR   HOVERGEN; HBG006699; -.
DR   InParanoid; Q9ERN6; -.
DR   ArrayExpress; Q9ERN6; -.
DR   Bgee; Q9ERN6; -.
DR   Genevestigator; Q9ERN6; -.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; IDA:MGI.
DR   GO; GO:0030018; C:Z disc; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005219; F:ryanodine-sensitive calcium-release channel activity; IDA:MGI.
DR   GO; GO:0031000; P:response to caffeine; IDA:MGI.
DR   InterPro; IPR001870; B302/SPRY.
DR   InterPro; IPR000699; Ca-rel_channel.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR014821; Ins145_P3_rcpt.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003608; MIR.
DR   InterPro; IPR016093; MIR_motif.
DR   InterPro; IPR013662; RIH_assoc-dom.
DR   InterPro; IPR013333; Ryan_recept.
DR   InterPro; IPR003032; Ryanodine_rcpt.
DR   InterPro; IPR015925; Ryanodine_recept-rel.
DR   InterPro; IPR009460; Ryanrecept_TM4-6.
DR   InterPro; IPR018355; SPla/RYanodine_receptor_sg.
DR   InterPro; IPR003877; SPRY_rcpt.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   PANTHER; PTHR13715; Ryanodine_recept-rel; 1.
DR   Pfam; PF08709; Ins145_P3_rec; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02815; MIR; 1.
DR   Pfam; PF08454; RIH_assoc; 1.
DR   Pfam; PF06459; RR_TM4-6; 1.
DR   Pfam; PF01365; RYDR_ITPR; 2.
DR   Pfam; PF02026; RyR; 4.
DR   Pfam; PF00622; SPRY; 3.
DR   PRINTS; PR00795; RYANODINER.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM00472; MIR; 4.
DR   SMART; SM00449; SPRY; 3.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 2.
DR   SUPFAM; SSF82109; MIR; 1.
DR   PROSITE; PS50188; B302_SPRY; 3.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS50919; MIR; 5.
PE   1: Evidence at protein level;
KW   3D-structure; Ion transport; Ionic channel; Membrane; Transmembrane;
KW   Transport.
SQ   SEQUENCE   4967 AA;  564900 MW;  81A27F4DCFF4E4FB CRC64;
     MADAGEGEDE IQFLRTDDEV VLQCTATIHK EQQKLCLAAE GFGNRLCFLE STSNSKNVPP
     DLSICTFVLE QSLSVRALQE MLANTVEKSE GQVDVEKWKF MMKTAQGGGH RTLLYGHAIL
     LRHSYSGMYL CCLSTSRSST DKLAFDVGLQ EDTTGEACWW TIHPASKQRS EGEKVRVGDD
     LILVSVSSER YLHLSYGNSS WHVDAAFQQT LWSVAPISSG SEAAQGYLIG GDVLRLLHGH
     MDECLTVPSG EHGEEQRRTV HYEGGAVSVH ARSLWRLETL RVAWSGSHIR WGQPFRLRHV
     TTGKYLSLME DKNLLLMDKE KADVKSTAFA FRSSKEKLDV GVRKEVDGMG TSEIKYGDSI
     CYIQHVDTGL WLTYQAVDVK SARMGSIQRK AIMHHEGHMD DGLNLSRSQH EESRTARVIR
     STVFLFNRFI RGLDALSKKV KLPTIDLPIE SVSLSLQDLI GYFHPPDEHL EHEDKQNRLR
     ALKNRQNLFQ EEGMINLVLE CIDRLHVYSS AAHFADVAGR EAGESWKSIL NSLYELLAAL
     IRGNRKNCAQ FSGSLDWLIS RLERLEASSG ILEVLHCVLV ESPEALNIIK EGHIKSIISL
     LDKHGRNHKV LDVLCSLCVC HGVAVRSNQH LICDNLLPGR DLLLQTRLVN HVSSMRPNIF
     LGVSEGSAQY KKWYYELMVD HTEPFVTAEA THLRVGWAST EGYSPYPGGG EEWGGNGVGD
     DLFSYGFDGL HLWSGCIART VSSPNQHLLR TDDVISCCLD LSAPSISFRI NGQPVQGMFE
     NFNIDGLFFP VVSFSAGIKV RFLLGGRHGE FKFLPPPGYA ACYEAVLPKE KLKVEHSREY
     KQERTYTRDL LGPTVSLTQA AFTPVPVDTS QIVLPPHLER IRERLAENIH ELWVMNKIEL
     GWQYGPVRDD NKRQHPCLVE FCKLPEQERN YNLQMSLETL KTLLALGCHV GIADEHAEEK
     VKKMKLPKNY QLTSGYKPAP MDLSFIKLTP SQEAMVDKLA ENAHNVWARD RIRQGWTYGI
     QQDVKNRRNP RLVPYTLLDD RTKKSNKDSL REAVRTLLGY GYHLEAPDQD HASRAEVCSG
     TGERFRIFRA EKTYAVKAGR WYFEFEAVTA GDMRVGWSRP GCQPDLELGS DDRAFAFDGF
     KAQRWHQGNE HYGRSWQAGD VVGCMVDMNE HTMMFTLNGE ILLDDSGSEL AFKDFDVGDG
     FIPVCSLGVA QVGRMNFGKD VSTLKYFTIC GLQEGYEPFA VNTNRDITMW LSKRLPQFLQ
     VPSNHEHIEV TRIDGTIDSS PCLKVTQKSF GSQNNNTDIM FYRLSMPIEC AEVFSKSVAG
     GLPGAGFYGP KSDLEDFDVD SDFEVLMKTA HGHLVPDRID KDKETPKPEF NNHKDYAQEK
     PSRLKQRFLL RRTKPDYSTG HSARLTEDVL AGDRDDYEYL MQTSTYYYSV RIFPGQEPAN
     VWVGWITSDF HQYDTGFDLD RVRTVTVTLG DEKGKVHESI KRSNCYMVCA GESMSPGQGR
     NNSNGLEIGC VVDAASGLLT FIANGKELST YYQVEPSTKL FPAVFAQATS PNVFQFELGR
     IKNVMPLSAG LFKSEHKNPV PQCPPRLHVQ FLSHVLWSRM PNQFLKVDVS RISERQGWLV
     QCLDPLQFMS LHIPEENRSV DILELTEQEE LLQFHYHTLR LYSAVCALGN HRVAHALCSH
     VDEPQLLYAI ENKYMPGLLR AGYYDLLIDI HLSSYATARL MMNNEFIVPM TEETKSITLF
     PDENKKHGLP GIGLSTSLRP RMRFSSPSFV SISNDCYQYS PEFPLDILKA KTIQMLTEAV
     KEGSLHARDP VGGTTEFLFV PLIKLFYTLL IMGIFHNEDL KHILQLIEPS VFKEAAVPEE
     EGGTPEKEIS IEDAKLEGEE EAKGGKRPKE GLLQMKLPEP VKLQMCLLLQ YLCDCQVRHR
     IEAIVAFSDD FVAKLQDNQR FRYNEVMQAL NMSAALTARK TKEFRSPPQE QINMLLNFKD
     DKSECPCPEE IRDQLLDFHE DLMTHCGIEL DEDGSLDGSN DLTIRGRLLS LVEKVTYLKK
     KQAEKPVASD SRKCSSLQQL ISETMVRWAQ ESVIEDPELV RAMFVLLHRQ YDGIGGLVRA
     LPKTYTINGV SVEDTINLLA SLGQIRSLLS VRMGKEEEKL MIRGLGDIMN NKVFYQHPNL
     MRALGMHETV MEVMVNVLGG GESKEITFPK MVANCCRFLC YFCRISRQNQ KAMFDHLSYL
     LENSSVGLAS PAMRGSTPLD VAAASVMDNN ELALALREPD LEKVVARYLA GCGLQSCQML
     VSKGYPDIGW NPVEGERYLD FLRFAVFCNG ESVEENANVV VRLLIRRPEC FGPALRGEGG
     NGLLAAMEEA IKIAEDPSRD GPSPTSGSSK TLDIEEEEDD TIHMGNAIMT FYAALIDLLG
     RCAPEMHLIH AGKGEAIRIR SILRSLIPLG DLVGVISIAF QMPTIAKDGK VVEPDMSAGF
     CPDHKAAMVL FLDRVYGIEV QDFLLHLLEV GFLPDLRAAA SLDTAALSAT DMALALNRYL
     CTAVLPLLTR CARLFAGTEH HASLIDSLLH TVYRLSKGCS LTKAQRDSIE VCLLSICGQL
     RPSMMQHLLR RLVFDVPLLN EHAKMPLKLL TNHYERCWKY YCLPGGWGNF GAASEEELHL
     SRKLFWGIFD ALSQKKYEQE LFKLALPCLS AVAGALPPDY MESNYVSMME KQSSMDSEGN
     FNPQPVDTSN ITIPEKLEYF INKYAEHSHD KWSMDKLANG WIYGEIYSDS SKIQPLMKPY
     KLLSEKEKEI YRWPIKESLK TMLAWGWRIE RTREGDSMAL YNRTRRISQT SQVSIDAAHG
     YSPRAIDMSN VTLSRDLHAM AEMMAENYHN IWAKKKKLEL ESKGGGNHPL LVPYDTLTAK
     EKAKDREKAQ DIFKFLQISG YVVSRGFKDL DLDTPSIEKR FAYSFLQQLI RYVDEAHQYI
     LEFDGGSRSK GEHFPYEQEI KFFAKVVLPL IDQYFKNHRL YFLSAASRPL CTGGHASNKE
     KEMVTSLFCK LGVLVRHRIS LFGNDATSIV NCLHILGQTL DARTVMKTGL DSVKSALRAF
     LDNAAEDLEK TMENLKQGQF THTRSQPKGV TQIINYTTVA LLPMLSSLFE HIGQHQFGED
     LILEDVQVSC YRILTSLYAL GTSKSIYVER QRSALGECLA AFAGAFPIAF LETHLDKHNV
     YSIYNTRSSR ERTALSLPAN VEDVCPNIPS LEKLMTEIIE LAESGIRYTQ MPYMMEVVLP
     MLCSYMSRWW EHGPENHPER AEMCCTALNS EHMNTLLGNI LKIIYNNLGI DEGAWMKRLA
     VFSQPIINKV KPQLLKTHFL PLMEKLKKKA AMVVSEEDHL KAEARGDMSE AELLILDEFT
     TLARDLYAFY PLLIRFVDYN RAKWLKEPNP EAEELFRMVA EVFIYWSKSH NFKREEQNFV
     VQNEINNMSF LITDTKSKMS KAAISDQERK KMKRKGDRYS MQTSLIVAAL KRLLPIGLNI
     CAPGDQELIA LAKNRFSLKD TEEEVRDIIR SNIHLQGKLE DPAIRWQMAL YKDFPNRTED
     PSDPERTVER VLGIANVLFH LEQKSKYTGR GYFSLVEHPQ RSKKAVWHKL LSKQRKRAVV
     ACFRMAPLYN LPRHRAVNLF LQGYEKSWIE TEEHYFEDKL IEDLAKPGAE LPEEDEAMKR
     VDPLHQLILL FSRTALTEKC KLEEDFLYMA YADIMAKSCH DEEDDDGEEE VKSFEEKEME
     KQKLLYQQAR LHDRGAAEMV LQTISASKGE TGPMVAATLK LGIAILNGGN STVQQKMLDY
     LKEKKDVGFF QSLAGLMQSC SVLDLNAFER QNKAEGLGMV TEEGSGEKVL QDDEFTCDLF
     RFLQLLCEGH NSDFQNYLRT QTGNNTTVNI IISTVDYLLR VQESISDFYW YYSGKDIIDE
     QGQRNFSKAI QVAKQVFNTL TEYIQGPCTG NQQSLAHSRL WDAVVGFLHV FAHMQMKLSQ
     DSSQIELLKE LMDLQKDMVV MLLSMLEGNV VNGTIGKQMV DMLVESSNNV EMILKFFDMF
     LKLKDLTSSD TFKEYDPDGK GVISKRDFHK AMESHKHYTQ SETEFLLSCA ETDENETLDY
     EEFVKRFHEP AKDIGFNVAV LLTNLSEHMP NDTRLQTFLE LAESVLNYFQ PFLGRIEIMG
     SAKRIERVYF EISESSRTQW EKPQVKESKR QFIFDVVNEG GEKEKMELFV NFCEDTIFEM
     QLAAQISESD LNERLANKEE SEKERPEEQA PRMGFFSLLT IQSALFALRY NVLTLVRMLS
     LKSLKKQMKR MKKMTVKDMV LAFFSSYWSV FVTLLHFVAS VCRGFFRIVS SLLLGGSLVE
     GAKKIKVAEL LANMPDPTQD EVRGDEEEGE RKPLESALPS EDLTDLKELT EESDLLSDIF
     GLDLKREGGQ YKLIPHNPNA GLSDLMTNPV PVPEVQEKFQ EQKAKEEKEE KEETKSEPEK
     AEGEDGEKEE KAKDEKSKQK LRQLHTHRYG EPEVPESAFW KKIIAYQQKL LNYFARNFYN
     MRMLALFVAF AINFILLFYK VSTSSVVEGK ELPTRTSSDT AKVTNSLDSS PHRIIAVHYV
     LEESSGYMEP TLRILAILHT IISFFCIIGY YCLKVPLVIF KREKEVARKL EFDGLYITEQ
     PSEDDIKGQW DRLVINTQSF PNNYWDKFVK RKVMDKYGEF YGRDRISELL GMDKAALDFS
     DAREKKKPKK DSSLSAVLNS IDVKYQMWKL GVVFTDNSFL YLAWYMTMSV LGHYNNFFFA
     AHLLDIAMGF KTLRTILSSV THNGKQLVLT VGLLAVVVYL YTVVAFNFFR KFYNKSEDGD
     TPDMKCDDML TCYMFHMYVG VRAGGGIGDE IEDPAGDEYE IYRIIFDITF FFFVIVILLA
     IIQGLIIDAF GELRDQQEQV KEDMETKCFI CGIGNDYFDT VPHGFETHTL QEHNLANYLF
     FLMYLINKDE TEHTGQESYV WKMYQERCWE FFPAGDCFRK QYEDQLN
//
ID   ZN704_MOUSE             Reviewed;         566 AA.
AC   Q9ERQ3; Q7TQL8; Q8BJW9;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Zinc finger protein 704;
DE   AltName: Full=Glucocorticoid-induced gene 1 protein;
GN   Name=Znf704; Synonyms=Gig1, Zfp704;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RA   Kuscuoglu U., Sen G., Chapman M., Miesfeld R.;
RT   "Glucocorticoid-induced gene-1 (GIG1) is up-regulated in WEHI 7.2
RT   thymoma cells undergoing dexamethasone induced apoptosis.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 301-566.
RC   TISSUE=Pancreas;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 363-566.
RC   STRAIN=C57BL/6J; TISSUE=Muellerian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SIMILARITY: Contains 1 C2H2-type zinc finger.
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DR   EMBL; AF292939; AAG34027.1; -; mRNA.
DR   EMBL; BC052936; AAH52936.1; -; mRNA.
DR   EMBL; AK078492; BAC37306.1; -; mRNA.
DR   IPI; IPI00112602; -.
DR   RefSeq; NP_573481.1; NM_133218.2.
DR   UniGene; Mm.212908; -.
DR   ProteinModelPortal; Q9ERQ3; -.
DR   PhosphoSite; Q9ERQ3; -.
DR   PRIDE; Q9ERQ3; -.
DR   Ensembl; ENSMUST00000041124; ENSMUSP00000041242; ENSMUSG00000040209.
DR   GeneID; 170753; -.
DR   KEGG; mmu:170753; -.
DR   UCSC; uc008opb.1; mouse.
DR   CTD; 170753; -.
DR   MGI; MGI:2180715; Zfp704.
DR   eggNOG; roNOG07170; -.
DR   GeneTree; ENSGT00400000022069; -.
DR   HOGENOM; HBG715639; -.
DR   HOVERGEN; HBG061238; -.
DR   InParanoid; Q9ERQ3; -.
DR   OMA; SAMEGEA; -.
DR   OrthoDB; EOG4R23TV; -.
DR   PhylomeDB; Q9ERQ3; -.
DR   NextBio; 370334; -.
DR   ArrayExpress; Q9ERQ3; -.
DR   Bgee; Q9ERQ3; -.
DR   CleanEx; MM_ZFP704; -.
DR   Genevestigator; Q9ERQ3; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   SMART; SM00355; ZnF_C2H2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Zinc; Zinc-finger.
FT   CHAIN         1    566       Zinc finger protein 704.
FT                                /FTId=PRO_0000288825.
FT   ZN_FING     346    371       C2H2-type.
FT   COMPBIAS     21     58       Pro-rich.
FT   COMPBIAS     84     91       Poly-Arg.
FT   COMPBIAS    248    306       Ser-rich.
SQ   SEQUENCE   566 AA;  61150 MW;  25DCE20EC0180E64 CRC64;
     MQARRLAKRP SLGSRRGGAA PAPAPEAAAL GLPPPGPSPA AAPGSWRPPL PPPRGTGPSR
     AAAASSPVLL LLGEEDEDEE GAGRRRRTRG RVTEKPRGVA EEEDDDEEED EEVVVEVVDG
     DEDDEDAEER FVPLGPGRAL PKGPARGAVK VGSFKREMTF TFQSEDFRRD SSKKPSHHLF
     PLAMEEDVRT ADTKKTSRVL DQEKETRSVC LLEQKRKVVS SNIDVPPARK SSEELDMDKV
     TAAMVLTSLS TSPLVRSPPV RPNEGLSGSW KEGAPSSSSS SGYWSWSAPS DQSNPSTPSP
     PLSADSFKPF RSPAPPDDGI DEADASNLLF DEPIPRKRKN SMKVMFKCLW KSCGKVLNTA
     AGIQKHIRAV HLGRVGESDC SDGEEDFYYT EIKLNTDATA EGLNTVAPVS PSQSLASAPA
     FPIPDSSRTE TPCAKTDTKL VTPLSRSAPT TLYLVHTDHA YQATPPVTIP GSAKFTPNGS
     SFSISWQSPP VTFTGVPVSP PHHPTAGSGE QRQHAHTALS SPPRGTVTLR KPRGEGKKCR
     KVYGMENRDM WCTACRWKKA CQRFID
//
ID   NDEL1_MOUSE             Reviewed;         345 AA.
AC   Q9ERR1; Q9D0Q4; Q9EPT6;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 2.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Nuclear distribution protein nudE-like 1;
DE   AltName: Full=Protein mNudE-like;
DE            Short=Protein Nudel;
DE            Short=mNudE-L;
GN   Name=Ndel1; Synonyms=Nudel;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SELF-ASSOCIATION, INTERACTION
RP   WITH PAFAH1B1 AND DYNEIN, TISSUE SPECIFICITY, AND PHOSPHORYLATION BY
RP   CDK5.
RX   MEDLINE=21094477; PubMed=11163259; DOI=10.1016/S0896-6273(00)00146-X;
RA   Sasaki S., Shionoya A., Ishida M., Gambello M.J., Yingling J.,
RA   Wynshaw-Boris A., Hirotsune S.;
RT   "A LIS1/NUDEL/cytoplasmic dynein heavy chain complex in the developing
RT   and adult nervous system.";
RL   Neuron 28:681-696(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH PAFAH1B1,
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=Swiss Webster / NIH;
RX   PubMed=11231056; DOI=10.1016/S0925-4773(00)00543-8;
RA   Sweeney K.J., Prokscha A., Eichele G.;
RT   "NudE-L, a novel Lis1-interacting protein, belongs to a family of
RT   vertebrate coiled-coil proteins.";
RL   Mech. Dev. 101:21-33(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   INTERACTION WITH PAFAH1B1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND DEVELOPMENTAL STAGE.
RX   MEDLINE=21094478; PubMed=11163260; DOI=10.1016/S0896-6273(00)00147-1;
RA   Niethammer M., Smith D.S., Ayala R., Peng J., Ko J., Lee M.-S.,
RA   Morabito M., Tsai L.-H.;
RT   "NUDEL is a novel cdk5 substrate that associates with LIS1 and
RT   cytoplasmic dynein.";
RL   Neuron 28:697-711(2000).
RN   [7]
RP   FUNCTION, INTERACTION WITH PAFAH1B1 AND YWHAE, SUBCELLULAR LOCATION,
RP   PHOSPHORYLATION BY CDK5, AND MUTAGENESIS OF SER-198; THR-219 AND
RP   SER-231.
RX   PubMed=12796778; DOI=10.1038/ng1169;
RA   Toyo-oka K., Shionoya A., Gambello M.J., Cardoso C., Leventer R.,
RA   Ward H.L., Ayala R., Tsai L.-H., Dobyns W., Ledbetter D.,
RA   Hirotsune S., Wynshaw-Boris A.;
RT   "14-3-3epsilon is important for neuronal migration by binding to
RT   NUDEL: a molecular explanation for Miller-Dieker syndrome.";
RL   Nat. Genet. 34:274-285(2003).
RN   [8]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15147871; DOI=10.1016/j.febslet.2004.04.009;
RA   Yamaguchi N., Takanezawa Y., Koizumi H., Umezu-Goto M., Aoki J.,
RA   Arai H.;
RT   "Expression of NUDEL in manchette and its implication in
RT   spermatogenesis.";
RL   FEBS Lett. 566:71-76(2004).
RN   [9]
RP   INTERACTION WITH DISC1; DYNEIN; TUBULIN GAMMA AND MICROTUBULES,
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-266 AND GLU-267.
RX   PubMed=14962739; DOI=10.1016/j.mcn.2003.09.009;
RA   Brandon N.J., Handford E.J., Schurov I., Rain J.-C., Pelling M.,
RA   Duran-Jimeniz B., Camargo L.M., Oliver K.R., Beher D., Shearman M.S.,
RA   Whiting P.J.;
RT   "Disrupted in Schizophrenia 1 and Nudel form a neurodevelopmentally
RT   regulated protein complex: implications for schizophrenia and other
RT   major neurological disorders.";
RL   Mol. Cell. Neurosci. 25:42-55(2004).
RN   [10]
RP   FUNCTION, INTERACTION WITH NEFH; NEFL AND PAFAH1B1, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=15208636; DOI=10.1038/ncb1139;
RA   Nguyen M.-D., Shu T., Sanada K., Lariviere R.C., Tseng H.-C.,
RA   Park S.K., Julien J.-P., Tsai L.-H.;
RT   "A NUDEL-dependent mechanism of neurofilament assembly regulates the
RT   integrity of CNS neurons.";
RL   Nat. Cell Biol. 6:595-608(2004).
RN   [11]
RP   FUNCTION, INTERACTION WITH DYNEIN, SUBCELLULAR LOCATION, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=15473966; DOI=10.1016/j.neuron.2004.09.030;
RA   Shu T., Ayala R., Nguyen M.-D., Xie Z., Gleeson J.G., Tsai L.-H.;
RT   "Ndel1 operates in a common pathway with LIS1 and cytoplasmic dynein
RT   to regulate cortical neuronal positioning.";
RL   Neuron 44:263-277(2004).
RN   [12]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=15473967; DOI=10.1016/j.neuron.2004.09.023;
RA   Feng Y., Walsh C.A.;
RT   "Mitotic spindle regulation by Nde1 controls cerebral cortical size.";
RL   Neuron 44:279-293(2004).
RN   [13]
RP   FUNCTION, INTERACTION WITH KATNA1 AND KATNB1, SUBCELLULAR LOCATION,
RP   PHOSPHORYLATION BY CDK5, AND MUTAGENESIS OF SER-198; THR-219 AND
RP   SER-231.
RX   PubMed=16203747; DOI=10.1093/hmg/ddi339;
RA   Toyo-Oka K., Sasaki S., Yano Y., Mori D., Kobayashi T.,
RA   Toyoshima Y.Y., Tokuoka S.M., Ishii S., Shimizu T., Muramatsu M.,
RA   Hiraiwa N., Yoshiki A., Wynshaw-Boris A., Hirotsune S.;
RT   "Recruitment of katanin p60 by phosphorylated NDEL1, an LIS1
RT   interacting protein, is essential for mitotic cell division and
RT   neuronal migration.";
RL   Hum. Mol. Genet. 14:3113-3128(2005).
RN   [14]
RP   FUNCTION.
RX   PubMed=16107726; DOI=10.1128/MCB.25.17.7812-7827.2005;
RA   Sasaki S., Mori D., Toyo-oka K., Chen A., Garrett-Beal L.,
RA   Muramatsu M., Miyagawa S., Hiraiwa N., Yoshiki A., Wynshaw-Boris A.,
RA   Hirotsune S.;
RT   "Complete loss of Ndel1 results in neuronal migration defects and
RT   early embryonic lethality.";
RL   Mol. Cell. Biol. 25:7812-7827(2005).
RN   [15]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15797709; DOI=10.1016/j.mcn.2004.11.003;
RA   Brandon N.J., Schurov I., Camargo L.M., Handford E.J.,
RA   Duran-Jimeniz B., Hunt P., Millar J.K., Porteous D.J., Shearman M.S.,
RA   Whiting P.J.;
RT   "Subcellular targeting of DISC1 is dependent on a domain independent
RT   from the Nudel binding site.";
RL   Mol. Cell. Neurosci. 28:613-624(2005).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215 AND THR-219, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Required for organization of the cellular microtubule
CC       array and microtubule anchoring at the centrosome. May regulate
CC       microtubule organization at least in part by targeting the
CC       microtubule severing protein KATNA1 to the centrosome. Also
CC       positively regulates the activity of the minus-end directed
CC       microtubule motor protein dynein. May enhance dynein-mediated
CC       microtubule sliding by targeting dynein to the microtubule plus
CC       ends. Required for several dynein- and microtubule-dependent
CC       processes such as the maintenance of Golgi integrity, the
CC       centripetal motion of secretory vesicles and the coupling of the
CC       nucleus and centrosome. Also required during brain development for
CC       the migration of newly formed neurons from the
CC       ventricular/subventricular zone toward the cortical plate. Plays a
CC       role, together with DISC1, in the regulation of neurite outgrowth.
CC       Required for mitosis in some cell types but appears to be
CC       dispensible for mitosis in cortical neuronal progenitors, which
CC       instead requires NDE1. Facilitates the polymerization of
CC       neurofilaments from the individual subunits NEFH and NEFL.
CC   -!- SUBUNIT: Interacts with dynactin, PCM1 and PCNT. Interacts (via C-
CC       terminus) with CENPF (By similarity). Self-associates. Interacts
CC       with DISC1, dynein, tubulin gamma, KATNA1, KATNB1, microtubules,
CC       PAFAHB1 and YWHAE. Interacts directly with NEFL and indirectly
CC       with NEFH.
CC   -!- INTERACTION:
CC       P63005:Pafah1b1; NbExp=2; IntAct=EBI-646668, EBI-917499;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
CC       cytoskeleton, centrosome. Chromosome, centromere, kinetochore (By
CC       similarity). Cytoplasm, cytoskeleton, spindle. Note=Localizes to
CC       the kinetochore in a CENPF-dependent manner. Colocalizes with
CC       DISC1 in the perinuclear region, including the centrosome (By
CC       similarity). Localizes to the interphase centrosome and the
CC       mitotic spindle. Localizes to the cell body of the motor neurons
CC       and colocalizes with assembled neurofilaments within axonal
CC       processes. Localizes to the microtubules of the manchette in
CC       elongated spermatids. Localizes to the interphase centrosome and
CC       the mitotic spindle.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9ERR1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9ERR1-2; Sequence=VSP_019311;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, liver, lung and testis (at
CC       protein level). Expressed in brain, epididymis, eye, heart,
CC       kidney, large intestine, liver, ovary, pancreas, prostate,
CC       skeletal muscle, smooth muscle, spleen, submaxillary gland,
CC       testis, thymus and thyroid. Within the brain expression is
CC       pronounced in the cortex, hippocampus, olfactory bulb, striatum,
CC       thalamic and hypothalamic structures and in the molecular layer of
CC       the cerebellum. Largely excluded from cortical progenitor cells
CC       which express NDE1.
CC   -!- DEVELOPMENTAL STAGE: Expression in the brain is detectable from
CC       E7, rises at E15 and E17 and peaks at P5. Enriched in the
CC       developing cortex, particularly in neuroblasts of the ventricular
CC       zone and postmitotic migrating cortical plate neurons. Interaction
CC       with DISC1 in the brain is developmentally regulated, peaking at
CC       E17 and decreasing at P16 so as to be undetectable in the adult
CC       brain. Expressed in the testis from P12, when zygotene
CC       spermatocytes first appear, and expression subsequently rises at
CC       P27.
CC   -!- PTM: Phosphorylated by CDK1 and MAPK1 (By similarity).
CC       Phosphorylated in mitosis. Phosphorylated by CDK5. Phosphorylation
CC       by CDK5 promotes interaction with KATNA1 and YWHAE.
CC   -!- SIMILARITY: Belongs to the nudE family.
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DR   EMBL; AF290472; AAG10061.1; -; mRNA.
DR   EMBL; AF323918; AAG42496.1; -; mRNA.
DR   EMBL; AK011168; BAB27443.1; -; mRNA.
DR   EMBL; AL603662; CAI25525.1; -; Genomic_DNA.
DR   EMBL; AL603662; CAI25526.1; -; Genomic_DNA.
DR   EMBL; BC021434; AAH21434.1; -; mRNA.
DR   EMBL; BC046796; AAH46796.1; -; mRNA.
DR   IPI; IPI00318238; -.
DR   IPI; IPI00648601; -.
DR   RefSeq; NP_076157.2; NM_023668.2.
DR   UniGene; Mm.31979; -.
DR   ProteinModelPortal; Q9ERR1; -.
DR   SMR; Q9ERR1; 8-168.
DR   DIP; DIP-29553N; -.
DR   IntAct; Q9ERR1; 4.
DR   MINT; MINT-267613; -.
DR   STRING; Q9ERR1; -.
DR   PhosphoSite; Q9ERR1; -.
DR   PRIDE; Q9ERR1; -.
DR   Ensembl; ENSMUST00000018880; ENSMUSP00000018880; ENSMUSG00000018736.
DR   GeneID; 83431; -.
DR   KEGG; mmu:83431; -.
DR   UCSC; uc007joc.1; mouse.
DR   UCSC; uc007jod.1; mouse.
DR   CTD; 83431; -.
DR   MGI; MGI:1932915; Ndel1.
DR   eggNOG; roNOG08639; -.
DR   GeneTree; ENSGT00390000000111; -.
DR   HOGENOM; HBG505908; -.
DR   HOVERGEN; HBG082010; -.
DR   InParanoid; Q9ERR1; -.
DR   OMA; CISAMNI; -.
DR   OrthoDB; EOG4FFD2B; -.
DR   PhylomeDB; Q9ERR1; -.
DR   NextBio; 350554; -.
DR   ArrayExpress; Q9ERR1; -.
DR   Bgee; Q9ERR1; -.
DR   Genevestigator; Q9ERR1; -.
DR   GermOnline; ENSMUSG00000018736; Mus musculus.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR   GO; GO:0005813; C:centrosome; IDA:MGI.
DR   GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005875; C:microtubule associated complex; IDA:MGI.
DR   GO; GO:0060053; C:neurofilament cytoskeleton; IDA:MGI.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0043014; F:alpha-tubulin binding; IDA:MGI.
DR   GO; GO:0048487; F:beta-tubulin binding; IDA:MGI.
DR   GO; GO:0008017; F:microtubule binding; IDA:MGI.
DR   GO; GO:0032864; P:activation of Cdc42 GTPase activity; IDA:MGI.
DR   GO; GO:0021955; P:central nervous system neuron axonogenesis; IMP:MGI.
DR   GO; GO:0051642; P:centrosome localization; IMP:MGI.
DR   GO; GO:0001833; P:inner cell mass cell proliferation; IMP:MGI.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IGI:MGI.
DR   GO; GO:0060052; P:neurofilament cytoskeleton organization; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IGI:MGI.
DR   GO; GO:0008090; P:retrograde axon cargo transport; IDA:MGI.
DR   GO; GO:0047496; P:vesicle transport along microtubule; IGI:MGI.
DR   InterPro; IPR006964; NUDE_C.
DR   Pfam; PF04880; NUDE_C; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Centromere; Chromosome; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Developmental protein; Differentiation; Kinetochore;
KW   Microtubule; Neurogenesis; Phosphoprotein; Transport.
FT   CHAIN         1    345       Nuclear distribution protein nudE-like 1.
FT                                /FTId=PRO_0000240212.
FT   REGION       56    166       Self-association.
FT   REGION       64    189       Interaction with KATNB1.
FT   REGION      114    133       Required for interaction with PAFAH1B1
FT                                (By similarity).
FT   REGION      175    345       Interaction with CENPF (By similarity).
FT   REGION      189    256       Interaction with YWHAE.
FT   REGION      191    345       Interaction with NEFL.
FT   REGION      195    256       Interaction with KATNA1.
FT   REGION      241    280       Interaction with DISC1 (By similarity).
FT   REGION      256    291       Required for localization to the
FT                                centrosome and interaction with dynein,
FT                                dynactin, tubulin gamma, PCM1 and PCNT1
FT                                (By similarity).
FT   COILED       28    190       Potential.
FT   MOD_RES     194    194       Phosphoserine (By similarity).
FT   MOD_RES     197    197       Phosphoserine (By similarity).
FT   MOD_RES     198    198       Phosphoserine (By similarity).
FT   MOD_RES     215    215       Phosphoserine.
FT   MOD_RES     219    219       Phosphothreonine; by CDK1 and MAPK1 (By
FT                                similarity).
FT   MOD_RES     241    241       Phosphothreonine (By similarity).
FT   MOD_RES     242    242       Phosphoserine; by CDK1 (By similarity).
FT   MOD_RES     245    245       Phosphothreonine; by CDK1 and MAPK1 (By
FT                                similarity).
FT   VAR_SEQ     316    345       Missing (in isoform 2).
FT                                /FTId=VSP_019311.
FT   MUTAGEN     198    198       S->A: Reduces phosphorylation by CDK5 and
FT                                impairs interaction with YWHAE. Impairs
FT                                interaction with KATNA1; when associated
FT                                with A-219 and A-231.
FT   MUTAGEN     219    219       T->A: Reduces phosphorylation by CDK5 and
FT                                impairs interaction with YWHAE. Impairs
FT                                interaction with KATNA1; when associated
FT                                with A-198 and A-231.
FT   MUTAGEN     231    231       S->A: Reduces phosphorylation by CDK5 and
FT                                impairs interaction with YWHAE. Impairs
FT                                interaction with KATNA1; when associated
FT                                with A-198 and A-219.
FT   MUTAGEN     266    266       L->A: Impairs interaction with DISC1.
FT   MUTAGEN     267    267       E->A: Impairs interaction with DISC1.
FT   CONFLICT    302    302       E -> K (in Ref. 1; AAG10061).
SQ   SEQUENCE   345 AA;  38366 MW;  CB3059DFD998E9EC CRC64;
     MDGEDIPDFS SLKEETAYWK ELSLKYKQSF QEARDELVEF QEGSRELEAE LEAQLVQAEQ
     RNRDLQADNQ RLKYEVEALK EKLEHQYAQS YKQVSVLEDD LSQTRAIKEQ LHKYVRELEQ
     ANDDLERAKR ATIVSLEDFE QRLNQAIERN AFLESELDEK ESLLVSVQRL KDEARDLRQE
     LAVRERQQEV TRKSAPSSPT LDCEKMDSAV QASLSLPATP VGKGTENSFP SPKAIPNGFG
     TSPLTPSARI SALNIVGDLL RKVGALESKL AACRNFAKDQ ASRKSYVPGS VNCGVMNSNG
     PECPRSGRAT FFHKGAVNGF DPAPPPPGLG SSRPSSAPGM LPLSV
//
ID   SEP15_MOUSE             Reviewed;         162 AA.
AC   Q9ERR7; Q3TXW1; Q544W8; Q8VE40;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=15 kDa selenoprotein;
DE   Flags: Precursor;
GN   Name=Sep15;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20519655; PubMed=10945981; DOI=10.1074/jbc.M004014200;
RA   Kumaraswamy E., Malykh A., Korotkov K.V., Kozyavkin S., Hu Y.,
RA   Kwon S.Y., Moustafa M.E., Carlson B.A., Berry M.J., Lee B.J.,
RA   Hatfield D.L., Diamond A.M., Gladyshev V.N.;
RT   "Structure-expression relationships of the 15-kDa selenoprotein gene.
RT   Possible role of the protein in cancer etiology.";
RL   J. Biol. Chem. 275:35540-35547(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH UGGT1.
RX   PubMed=11278576; DOI=10.1074/jbc.M009861200;
RA   Korotkov K.V., Kumaraswamy E., Zhou Y., Hatfield D.L., Gladyshev V.N.;
RT   "Association between the 15-kDa selenoprotein and UDP-
RT   glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum
RT   of mammalian cells.";
RL   J. Biol. Chem. 276:15330-15336(2001).
CC   -!- FUNCTION: May be involved in redox reactions associated with the
CC       formation of disulfide bonds. May contribute to the quality
CC       control of protein folding in the endoplasmic reticulum (By
CC       similarity).
CC   -!- SUBUNIT: Forms a tight complex with UGGT1/UGCGL1.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen (By similarity).
CC       Note=The association with UGGT1/UGCGL1 is essential for its
CC       retention in the endoplasmic reticulum (By similarity).
CC   -!- SIMILARITY: Belongs to the selenoprotein M/SEP15 family.
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DR   EMBL; AF288740; AAG31765.1; -; mRNA.
DR   EMBL; AK020419; BAC55255.1; -; mRNA.
DR   EMBL; AK159085; BAE34803.1; -; mRNA.
DR   EMBL; AK159353; BAE35012.1; -; mRNA.
DR   EMBL; BC019792; AAH19792.2; -; mRNA.
DR   IPI; IPI00112641; -.
DR   RefSeq; NP_444332.1; NM_053102.2.
DR   UniGene; Mm.29812; -.
DR   ProteinModelPortal; Q9ERR7; -.
DR   SMR; Q9ERR7; 72-161.
DR   IntAct; Q9ERR7; 1.
DR   STRING; Q9ERR7; -.
DR   PRIDE; Q9ERR7; -.
DR   Ensembl; ENSMUST00000082437; ENSMUSP00000046910; ENSMUSG00000037072.
DR   GeneID; 93684; -.
DR   KEGG; mmu:93684; -.
DR   CTD; 93684; -.
DR   MGI; MGI:1927947; Sep15.
DR   eggNOG; roNOG15764; -.
DR   GeneTree; ENSGT00390000005531; -.
DR   HOGENOM; HBG320363; -.
DR   HOVERGEN; HBG108472; -.
DR   InParanoid; Q9ERR7; -.
DR   OrthoDB; EOG49KFRV; -.
DR   NextBio; 351408; -.
DR   ArrayExpress; Q9ERR7; -.
DR   Bgee; Q9ERR7; -.
DR   CleanEx; MM_SEP15; -.
DR   Genevestigator; Q9ERR7; -.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0008430; F:selenium binding; IDA:UniProtKB.
DR   GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:UniProtKB.
DR   InterPro; IPR014912; Sep15_SelM.
DR   InterPro; IPR012336; Thioredoxin-like_fold.
DR   Pfam; PF08806; Sep15_SelM; 1.
DR   SUPFAM; SSF52833; Thiordxn-like_fd; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Selenocysteine; Signal.
FT   SIGNAL        1     28       Potential.
FT   CHAIN        29    162       15 kDa selenoprotein.
FT                                /FTId=PRO_0000022308.
FT   NON_STD      93     93       Selenocysteine.
FT   CONFLICT     26     26       V -> A (in Ref. 1; AAG31765 and 2;
FT                                BAE35012/BAC55255).
FT   CONFLICT     98     98       F -> L (in Ref. 3; AAH19792).
SQ   SEQUENCE   162 AA;  17806 MW;  6EFF88F68C81903C CRC64;
     MAAGQGGWLR PALGLRLLLA TAFQAVSALG AEFASEACRE LGFSSNLLCS SCDLLGQFNL
     LPLDPVCRGC CQEEAQFETK KLYAGAILEV CGUKLGRFPQ VQAFVRSDKP KLFRGLQIKY
     VRGSDPVLKL LDDNGNIAEE LSILKWNTDS VEEFLSEKLE RI
//
ID   PPR1A_MOUSE             Reviewed;         171 AA.
AC   Q9ERT9;
DT   22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 1A;
DE   AltName: Full=Protein phosphatase inhibitor 1;
DE            Short=I-1;
DE            Short=IPP-1;
GN   Name=Ppp1r1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=20417820; PubMed=10960791; DOI=10.1016/S0925-4773(00)00388-9;
RA   McLaren L., Boyle S., Mason J.O., Bard J.B.L.;
RT   "Expression and genomic characterization of protein phosphatase
RT   inhibitor-1: a novel marker for mesothelium in the mouse.";
RL   Mech. Dev. 96:237-241(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Inhibitor of protein-phosphatase 1. This protein may be
CC       important in hormonal control of glycogen metabolism. Hormones
CC       that elevate intracellular cAMP increase I-1 activity in many
CC       tissues. I-1 activation may impose cAMP control over proteins that
CC       are not directly phosphorylated by PKA. Following a rise in
CC       intracellular calcium, I-1 is inactivated by calcineurin (or
CC       PP2B). Does not inhibit type-2 phosphatases.
CC   -!- SUBUNIT: Interacts with PPP1R15A (By similarity).
CC   -!- PTM: Phosphorylation of Thr-35 is required for activity (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein phosphatase inhibitor 1 family.
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DR   EMBL; AF281676; AAG15192.1; -; mRNA.
DR   EMBL; BC025123; AAH25123.1; -; mRNA.
DR   IPI; IPI00112721; -.
DR   RefSeq; NP_067366.1; NM_021391.3.
DR   UniGene; Mm.143788; -.
DR   ProteinModelPortal; Q9ERT9; -.
DR   STRING; Q9ERT9; -.
DR   PhosphoSite; Q9ERT9; -.
DR   PRIDE; Q9ERT9; -.
DR   Ensembl; ENSMUST00000023133; ENSMUSP00000023133; ENSMUSG00000022490.
DR   GeneID; 58200; -.
DR   KEGG; mmu:58200; -.
DR   UCSC; uc007xyj.1; mouse.
DR   CTD; 58200; -.
DR   MGI; MGI:1889595; Ppp1r1a.
DR   GeneTree; ENSGT00530000063381; -.
DR   HOGENOM; HBG713228; -.
DR   HOVERGEN; HBG096069; -.
DR   InParanoid; Q9ERT9; -.
DR   OMA; LKSTLSM; -.
DR   OrthoDB; EOG4TMR3H; -.
DR   PhylomeDB; Q9ERT9; -.
DR   NextBio; 314177; -.
DR   ArrayExpress; Q9ERT9; -.
DR   Bgee; Q9ERT9; -.
DR   Genevestigator; Q9ERT9; -.
DR   GermOnline; ENSMUSG00000022490; Mus musculus.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR008466; PPI_1DARPP-32.
DR   PANTHER; PTHR15417; PPI_1DARPP-32; 1.
DR   Pfam; PF05395; DARPP-32; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Glycogen metabolism; Phosphoprotein;
KW   Protein phosphatase inhibitor.
FT   CHAIN         1    171       Protein phosphatase 1 regulatory subunit
FT                                1A.
FT                                /FTId=PRO_0000071478.
FT   REGION        9     12       Essential for activity.
FT   REGION       42     54       Essential for activity (Probable).
FT   REGION      143    171       Interaction with PPP1R15A (By
FT                                similarity).
FT   MOD_RES      35     35       Phosphothreonine; by PKA (By similarity).
SQ   SEQUENCE   171 AA;  18718 MW;  F6981C75CA163F8D CRC64;
     MEPDNSPRKI QFTVPLLEPH LDPEAAEQIR RRRPTPATLV LTSDQSSPEI DEDRIPNSLL
     KSTLSMSPRQ RKKMTRTTPT MKELQTMVEH HLGQQKQGEE PEGATESTGN QESCPPGIPD
     TGSASRPDTP GTAQKSAESN PKTQEQCGVE PRTEDSSAHM LPLDSQGASL V
//
ID   RBP2_MOUSE              Reviewed;        3053 AA.
AC   Q9ERU9; Q61992; Q8C9K9;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=E3 SUMO-protein ligase RanBP2;
DE   AltName: Full=Ran-binding protein 2;
DE            Short=RanBP2;
GN   Name=Ranbp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/Ola;
RX   MEDLINE=21251165; PubMed=11353387; DOI=10.1007/s003350010291;
RA   Fauser S., Aslanukov A., Roepman R., Ferreira P.A.;
RT   "Genomic organization, expression, and localization of murine Ran-
RT   binding protein 2 (RanBP2) gene.";
RL   Mamm. Genome 12:406-415(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-222.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 985-2249.
RX   MEDLINE=96187094; PubMed=8603673;
RA   Wilken N., Senecal J.L., Scheer U., Dabauvalle M.C.;
RT   "Localization of the Ran-GTP binding protein RanBP2 at the cytoplasmic
RT   side of the nuclear pore complex.";
RL   Eur. J. Cell Biol. 68:211-219(1995).
RN   [4]
RP   INTERACTION WITH PARK2.
RX   PubMed=16332688; DOI=10.1074/jbc.M504994200;
RA   Um J.W., Min D.S., Rhim H., Kim J., Paik S.R., Chung K.C.;
RT   "Parkin ubiquitinates and promotes the degradation of RanBP2.";
RL   J. Biol. Chem. 281:3595-3603(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2505, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1098; SER-2083;
RP   SER-2088; SER-2113; SER-2117; THR-2130; SER-2134; SER-2576 AND
RP   THR-2578, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2505 AND SER-2729, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-954 AND SER-2729, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-781; SER-788 AND
RP   SER-2505, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: E3 SUMO-protein ligase which facilitates SUMO1 and SUMO2
CC       conjugation by UBE2I. Involved in transport factor (Ran-GTP,
CC       karyopherin)-mediated protein import via the F-G repeat-containing
CC       domain which acts as a docking site for substrates. Could also
CC       have isomerase or chaperone activity and may bind RNA or DNA.
CC       Component of the nuclear export pathway. Specific docking site for
CC       the nuclear export factor exportin-1 (By similarity).
CC   -!- PATHWAY: Protein modification; protein sumoylation.
CC   -!- SUBUNIT: Forms a tight complex with RANBP1 and UBE2I. Interacts
CC       with SUMO1 but not SUMO2. Interacts with sumoylated RANGAP1.
CC       Interacts with CDCA8 (By similarity). Interacts with PARK2.
CC   -!- INTERACTION:
CC       Q9WVS6:Park2; NbExp=1; IntAct=EBI-643756, EBI-973635;
CC       Q01320:Top2a; NbExp=1; IntAct=EBI-643756, EBI-642809;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex (By
CC       similarity). Note=Cytoplasmic filaments (By similarity).
CC   -!- DOMAIN: Contains F-X-F-G repeats.
CC   -!- PTM: Polyubiquitinated by PARK2, which leads to proteasomal
CC       degradation (By similarity).
CC   -!- SIMILARITY: Contains 1 PPIase cyclophilin-type domain.
CC   -!- SIMILARITY: Contains 4 RanBD1 domains.
CC   -!- SIMILARITY: Contains 6 RanBP2-type zinc fingers.
CC   -!- SIMILARITY: Contains 3 TPR repeats.
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DR   EMBL; AF279458; AAG17403.1; -; Genomic_DNA.
DR   EMBL; AK041932; BAC31101.1; -; mRNA.
DR   EMBL; X87337; CAA60778.1; -; mRNA.
DR   IPI; IPI00337844; -.
DR   PIR; S57968; S57968.
DR   UniGene; Mm.401648; -.
DR   UniGene; Mm.431695; -.
DR   ProteinModelPortal; Q9ERU9; -.
DR   SMR; Q9ERU9; 30-119, 1165-1298, 1553-1593, 1619-1652, 1864-1991, 2146-2278, 2468-2530, 2543-2603, 2754-2875, 2892-3053.
DR   IntAct; Q9ERU9; 26.
DR   STRING; Q9ERU9; -.
DR   PhosphoSite; Q9ERU9; -.
DR   PRIDE; Q9ERU9; -.
DR   Ensembl; ENSMUST00000003310; ENSMUSP00000003310; ENSMUSG00000003226.
DR   UCSC; uc007fdd.1; mouse.
DR   MGI; MGI:894323; Ranbp2.
DR   eggNOG; roNOG11346; -.
DR   GeneTree; ENSGT00530000063483; -.
DR   HOGENOM; HBG268317; -.
DR   HOVERGEN; HBG092361; -.
DR   InParanoid; Q9ERU9; -.
DR   OrthoDB; EOG4J3WG2; -.
DR   PhylomeDB; Q9ERU9; -.
DR   ArrayExpress; Q9ERU9; -.
DR   Bgee; Q9ERU9; -.
DR   CleanEx; MM_RANBP2; -.
DR   Genevestigator; Q9ERU9; -.
DR   GermOnline; ENSMUSG00000003226; Mus musculus.
DR   GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0046907; P:intracellular transport; IEA:InterPro.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:UniProtKB-KW.
DR   InterPro; IPR015891; Cyclophilin-like.
DR   InterPro; IPR022011; IR1-M.
DR   InterPro; IPR020892; Pep-Pro_Isoase_cyclophilin_CS.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR002130; PPIase_cyclophilin.
DR   InterPro; IPR000156; RanBP.
DR   InterPro; IPR001440; TPR-1.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 4.
DR   Gene3D; G3DSA:2.40.100.10; PPIase_cyclophilin; 1.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 3.
DR   Pfam; PF12185; IR1-M; 2.
DR   Pfam; PF00160; Pro_isomerase; 1.
DR   Pfam; PF00638; Ran_BP1; 4.
DR   Pfam; PF00515; TPR_1; 1.
DR   Pfam; PF00641; zf-RanBP; 6.
DR   PRINTS; PR00153; CSAPPISMRASE.
DR   SMART; SM00160; RanBD; 4.
DR   SMART; SM00547; ZnF_RBZ; 6.
DR   SUPFAM; SSF50891; CSA_PPIase; 1.
DR   PROSITE; PS00170; CSA_PPIASE_1; 1.
DR   PROSITE; PS50072; CSA_PPIASE_2; 1.
DR   PROSITE; PS50196; RANBD1; 4.
DR   PROSITE; PS50005; TPR; 2.
DR   PROSITE; PS50293; TPR_REGION; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 6.
DR   PROSITE; PS50199; ZF_RANBP2_2; 6.
PE   1: Evidence at protein level;
KW   Acetylation; Isomerase; Isopeptide bond; Metal-binding;
KW   mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW   Protein transport; Repeat; Rotamase; TPR repeat; Translocation;
KW   Transport; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   3053       E3 SUMO-protein ligase RanBP2.
FT                                /FTId=PRO_0000204914.
FT   REPEAT       26     59       TPR 1.
FT   REPEAT       60     93       TPR 2.
FT   REPEAT      583    616       TPR 3.
FT   DOMAIN     1165   1301       RanBD1 1.
FT   DOMAIN     1849   1985       RanBD1 2.
FT   DOMAIN     2146   2282       RanBD1 3.
FT   REPEAT     2470   2522       1.
FT   REPEAT     2546   2596       2.
FT   DOMAIN     2740   2875       RanBD1 4.
FT   DOMAIN     2896   3052       PPIase cyclophilin-type.
FT   ZN_FING    1345   1375       RanBP2-type 1.
FT   ZN_FING    1410   1439       RanBP2-type 2.
FT   ZN_FING    1469   1498       RanBP2-type 3.
FT   ZN_FING    1494   1527       RanBP2-type 4.
FT   ZN_FING    1558   1587       RanBP2-type 5.
FT   ZN_FING    1617   1646       RanBP2-type 6.
FT   REGION     2468   2472       Interaction with sumoylated RANGAP1 (By
FT                                similarity).
FT   REGION     2470   2596       2 X 50 AA approximate repeats.
FT   REGION     2470   2545       Required for E3 SUMO-ligase activity (By
FT                                similarity).
FT   REGION     2470   2522       Interaction with UBE2I (By similarity).
FT   REGION     2523   2596       Interaction with SUMO1 (By similarity).
FT   COMPBIAS   2074   2079       Poly-Ser.
FT   COMPBIAS   2506   2509       Poly-Glu.
FT   COMPBIAS   2638   2641       Poly-Ser.
FT   MOD_RES      21     21       Phosphoserine (By similarity).
FT   MOD_RES     115    115       N6-acetyllysine (By similarity).
FT   MOD_RES     128    128       Phosphoserine (By similarity).
FT   MOD_RES     394    394       Phosphoserine (By similarity).
FT   MOD_RES     779    779       Phosphothreonine (By similarity).
FT   MOD_RES     781    781       Phosphoserine.
FT   MOD_RES     788    788       Phosphoserine.
FT   MOD_RES     796    796       Phosphoserine (By similarity).
FT   MOD_RES     799    799       Phosphothreonine (By similarity).
FT   MOD_RES     947    947       Phosphoserine (By similarity).
FT   MOD_RES     954    954       Phosphoserine.
FT   MOD_RES    1098   1098       Phosphoserine.
FT   MOD_RES    1138   1138       Phosphothreonine (By similarity).
FT   MOD_RES    1154   1154       Phosphoserine (By similarity).
FT   MOD_RES    1394   1394       Phosphothreonine (By similarity).
FT   MOD_RES    1407   1407       Phosphothreonine (By similarity).
FT   MOD_RES    1438   1438       Phosphoserine (By similarity).
FT   MOD_RES    1446   1446       Phosphoserine (By similarity).
FT   MOD_RES    1528   1528       Phosphoserine (By similarity).
FT   MOD_RES    1706   1706       Phosphoserine (By similarity).
FT   MOD_RES    1965   1965       Phosphothreonine (By similarity).
FT   MOD_RES    1990   1990       Phosphothreonine (By similarity).
FT   MOD_RES    2083   2083       Phosphoserine.
FT   MOD_RES    2088   2088       Phosphoserine.
FT   MOD_RES    2107   2107       Phosphoserine (By similarity).
FT   MOD_RES    2113   2113       Phosphoserine.
FT   MOD_RES    2115   2115       Phosphoserine (By similarity).
FT   MOD_RES    2117   2117       Phosphoserine.
FT   MOD_RES    2127   2127       Phosphoserine (By similarity).
FT   MOD_RES    2130   2130       Phosphothreonine.
FT   MOD_RES    2134   2134       Phosphoserine.
FT   MOD_RES    2284   2284       Phosphoserine (By similarity).
FT   MOD_RES    2287   2287       Phosphothreonine (By similarity).
FT   MOD_RES    2291   2291       Phosphoserine (By similarity).
FT   MOD_RES    2342   2342       Phosphothreonine (By similarity).
FT   MOD_RES    2348   2348       Phosphoserine (By similarity).
FT   MOD_RES    2356   2356       Phosphoserine (By similarity).
FT   MOD_RES    2450   2450       Phosphothreonine (By similarity).
FT   MOD_RES    2505   2505       Phosphoserine.
FT   MOD_RES    2576   2576       Phosphoserine.
FT   MOD_RES    2578   2578       Phosphothreonine.
FT   MOD_RES    2639   2639       Phosphoserine (By similarity).
FT   MOD_RES    2640   2640       Phosphoserine (By similarity).
FT   MOD_RES    2729   2729       Phosphoserine.
FT   MOD_RES    3036   3036       Phosphoserine (By similarity).
FT   CROSSLNK   2430   2430       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CONFLICT    213    222       EYLESLQCLD -> VGETYFSTVF (in Ref. 2).
FT   CONFLICT    985   1001       LVAHASRSAESKVIEFG -> IPGSRFKVSRIKGYRIWL
FT                                (in Ref. 3).
FT   CONFLICT   1086   1089       ISGQ -> YLA (in Ref. 3; CAA60778).
FT   CONFLICT   1269   1269       L -> F (in Ref. 3; CAA60778).
FT   CONFLICT   1273   1273       E -> G (in Ref. 3; CAA60778).
FT   CONFLICT   1276   1276       A -> S (in Ref. 3; CAA60778).
FT   CONFLICT   1280   1280       K -> Q (in Ref. 3; CAA60778).
FT   CONFLICT   1293   1293       E -> G (in Ref. 3; CAA60778).
FT   CONFLICT   1297   1297       N -> D (in Ref. 3; CAA60778).
FT   CONFLICT   1861   1861       E -> D (in Ref. 3; CAA60778).
SQ   SEQUENCE   3053 AA;  341091 MW;  685DF8526444D7BE CRC64;
     MRRSKADVER YIASVQGSAP SPREKSMKGF YFAKLYYEAK EYDLAKKYIS TYINVQERDP
     KAHRFLGLLY EVEENIDKAV ECYKRSVELN PTQKDLVLKI AELLCKNDVT DGRAKYWVER
     AAKLFPGSPA IYKLKEQLLD CKGEDGWNKL FDLIQSELYA RPDDIHVNIR LVELYRSNKR
     LKDAVAHCHE ADRNTALRSS LEWNLCVVQT LKEYLESLQC LDSDKSTWRA TNKDLLLAYA
     NLMLLTLSTR DVQEGRELLE SFDSALQSVK SSVGGNDELS ATFLETKGHF YMHVGSLLLK
     MGQQSDIQWR ALSELAALCY LVAFQVPRPK VKLIKGEAGQ NLLETMAHDR LSQSGHMLLN
     LSRGKQDFLK EVVESFANKS GQSALCDALF SSQSSKERSF LGNDDIGNLD GQVPDPDDLA
     RYDTGAVRAH NGSLQHLTWL GLQWNSLSTL PAIRKWLKQL FHHLPQETSR LETNAPESIC
     ILDLEVFLLG VIYTSHLQLK EKCNSHHTSY QPLCLPLPVC RQLCTERQKT WWDAVCTLIH
     RKALPGTSAK LRLLVQREIN SLRGQEKHGL QPALLVHWAQ SLQKTGSSLN SFYDQREYIG
     RSVHYWRKVL PLLKMIRKKN SIPEPIDPLF KHFHSVDIQA SEIGEYEEDA HITFAILDAV
     NGNIEDAMTA FESIKNVVSY WNLALIFHRK AEDIENDALS PEEQEECKNY LRKTRDYLIR
     ILDDSDSNTS VVQKLPVPLE SVKEMLNSVM QELEDYSEGG TLYKNGCWRS ADSELKHSTP
     SPTKYSLSPS KSYKYSPKTP PRWAEDQNSL LKMICQQVEA IKKEMQELKL NSNNSASPHR
     WPAEPYGQDP APDGYQGSQT FHGAPLTVAT TGPSVYYSQS PAYNSQYLLR PAANVTPTKG
     PVYGMNRLPP QQHIYAYSQQ MHTPPVQSSS ACMFSQEMYG PPLRFESPAT GILSPRGDDY
     FNYNVQQTST NPPLPEPGYF TKPPLVAHAS RSAESKVIEF GKSNFVQPMQ GEVIRPPLTT
     PAHTTQPTPF KFNSNFKSND GDFTFSSPQV VAQPPSTAYS NSESLLGLLT SDKPLQGDGY
     SGLKPISGQA SGSRNTFSFG SKNTLTENMG PNQQKNFGFH RSDDMFAFHG PGKSVFTTAA
     SELANKSHET DGGSAHGDEE DDGPHFEPVV PLPDKIEVKT GEEDEEEFFC NRAKLFRFDG
     ESKEWKERGI GNVKILRHKT SGKIRLLMRR EQVLKICANH YISPDMKLTP NAGSDRSFVW
     HALDYADELP KPEQLAIRFK TPEEAALFKC KFEEAQNILK ALGTNTSTAP NHTLRIVKES
     ATQDNKDICK ADGGNLNFEF QIVKKEGPYW NCNSCSFKNA ATAKKCVSCQ NTNPTSNKEL
     LGPPLVENGF APKTGLENAQ DRFATMTANK EGHWDCSVCL VRNEPTVSRC IACQNTKSAS
     SFVQTSFKFG QGDLPKSVDS DFRSVFSKKE GQWECSVCLV RNERSAKKCV ACENPGKQFK
     EWHCSLCSVK NEAHAIKCVA CNNPVTPSLS TAPPSFKFGT SEMSKPFRIG FEGMFAKKEG
     QWDCSLCFVR NEASATHCIA CQYPNKQNQP TSCVSAPASS ETSRSPKSGF EGLFPKKEGE
     WECAVCSVQN ESSSLKCVAC EASKPTHKPH EAPSAFTVGS KSQSNESAGS QVGTEFKSNF
     PEKNFKVGIS EQKFKFGHVD QEKTPSFAFQ GGSNTEFKSI KDGFSFCIPV SADGFKFGIQ
     EKGNQEKKSE KHLENDPSFQ AHDTSGQKNG SGVVFGQTSS TFTFADLAKS TSREGFQFGK
     KDPNFKGFSG AGEKLFSSQS GKVAEKANTS SDLEKDDDAY KTEDSDDIHF EPVVQMPEKV
     ELVTGEEDEK VLYSQRVKLF RFDAEISQWK ERGLGNLKIL KNEVNGKLRM LMRREQVLKV
     CANHWITTTM NLKPLSGSDR AWMWLASDFS DGDAKLEQLA AKFKTPELAE EFKQKFEECQ
     RLLLDIPLQT PHKLVDTGRA AKLIQRAEEM KSGLKDFKTF LTNDQVKVTD EENASSGADA
     PSASDTTAKQ NPDNTGPALE WDNYDLREDA LDDSVSSSSV HASPLASSPV RKNLFRFGES
     TTGFNFSFKS ALSPSKSPAK LNQSGASVGT DEESDVTQEE ERDGQYFEPV VPLPDLVEVS
     SGEENEQVVF SHRAKLYRYD KDVGQWKERG IGDIKILQNY DNKQVRIVMR RDQVLKLCAN
     HRITPDMTLQ TMKGTERVWV WTACDFADGE RKIEHLAVRF KLQDVADSFK KIFDEAKTAQ
     EKDSLITPHV SHLSTPRESP CGKIAIAVLE ETTRERTDLT QGDEVIDTTS EAGETSSTSE
     TTPKAVVSPP KFVFGSESVK SIFSSEKSKP FAFGNSSATG SLFGFSFNAP LKNSNSEMTS
     RVQSGSEGKV KPDKCELPQN SDIKQSSDGK VKNLSAFSKE NSSTSYTFKT PEKAQEKSKP
     EDLPSDNDIL IVYELTPTPE QKALAEKLLL PSTFFCYKNR PGYVSEEEED DEDYEMAVKK
     LNGKLYLDDS EKPLEENLAD NDKECVIVWE KKPTVEERAK ADTLKLPPTF FCGVCSDTDE
     DNGNGEDFQS ELRKVCEAQK SQNEKVTDRV GIEHIGETEV TNPVGCKSEE PDSDTKHSSS
     SPVSGTMDKP VDLSTRKETD MEFPSKGENK PVLFGFGSGT GLSFADLASS NSGDFAFGSK
     DKNFQWANTG AAVFGTQTTS KGGEDEDGSD EDVVHNEDIH FEPIVSLPEV EVKSGEEDEE
     VLFKERAKLY RWDRDVSQWK ERGIGDIKIL WHTMKKYYRI LMRRDQVFKV CANHVITKAM
     ELKPLNVSNN ALVWTASDYA DGEAKVEQLA VRFKTKEMTE SFKKKFEDSQ QNIIKLQNGH
     TSLAAELSKD TNPVVFFDVC ADGEPLGRII MELFSNIVPQ TAENFRALCT GEKGFGFKNS
     IFHRVVPDFI CQGGDITKYN GTGGQSIYGD KFDDENFDLK HTGPGLLSMA NYGQNTNSSQ
     FFITLKKAEH LDFKHVVFGF VKDGMDTVRK IESFGSPKGS VSRRICITEC GQL
//
ID   MKRN2_MOUSE             Reviewed;         416 AA.
AC   Q9ERV1; Q9D0L9;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Probable E3 ubiquitin-protein ligase makorin-2;
DE            EC=6.3.2.-;
GN   Name=Mkrn2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=21481893; PubMed=11597136; DOI=10.1006/geno.2001.6627;
RA   Gray T.A., Azama K., Whitmore K., Min A., Abe S., Nicholls R.D.;
RT   "Phylogenetic conservation of the makorin-2 gene, encoding a multiple
RT   zinc-finger protein, antisense to the raf1 proto-oncogene.";
RL   Genomics 77:119-126(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: E3 ubiquitin ligase catalyzing the covalent attachment
CC       of ubiquitin moieties onto substrate proteins (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SIMILARITY: Contains 4 C3H1-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
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DR   EMBL; AF277171; AAG27596.1; -; mRNA.
DR   EMBL; AK011295; BAB27523.1; -; mRNA.
DR   IPI; IPI00620251; -.
DR   RefSeq; NP_075779.2; NM_023290.2.
DR   UniGene; Mm.101316; -.
DR   ProteinModelPortal; Q9ERV1; -.
DR   SMR; Q9ERV1; 2-61, 164-215, 233-296, 324-350.
DR   STRING; Q9ERV1; -.
DR   PhosphoSite; Q9ERV1; -.
DR   PRIDE; Q9ERV1; -.
DR   Ensembl; ENSMUST00000000449; ENSMUSP00000000449; ENSMUSG00000000439.
DR   GeneID; 67027; -.
DR   KEGG; mmu:67027; -.
DR   CTD; 67027; -.
DR   MGI; MGI:1914277; Mkrn2.
DR   GeneTree; ENSGT00390000014093; -.
DR   HOGENOM; HBG384370; -.
DR   HOVERGEN; HBG066965; -.
DR   InParanoid; Q9ERV1; -.
DR   OrthoDB; EOG4229K2; -.
DR   ArrayExpress; Q9ERV1; -.
DR   Bgee; Q9ERV1; -.
DR   CleanEx; MM_MKRN2; -.
DR   Genevestigator; Q9ERV1; -.
DR   GermOnline; ENSMUSG00000000439; Mus musculus.
DR   GO; GO:0005622; C:intracellular; ISS:UniProtKB.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00356; ZnF_C3H1; 4.
DR   PROSITE; PS50103; ZF_C3H1; 4.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Ligase; Metal-binding; Phosphoprotein; Repeat;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    416       Probable E3 ubiquitin-protein ligase
FT                                makorin-2.
FT                                /FTId=PRO_0000055956.
FT   ZN_FING       2     29       C3H1-type 1.
FT   ZN_FING      31     58       C3H1-type 2.
FT   ZN_FING     165    192       C3H1-type 3.
FT   ZN_FING     238    292       RING-type.
FT   ZN_FING     321    350       C3H1-type 4.
FT   REGION      193    222       Makorin-type Cys-His.
FT   MOD_RES     139    139       Phosphoserine (By similarity).
FT   CONFLICT    181    181       L -> F (in Ref. 2; BAB27523).
SQ   SEQUENCE   416 AA;  46563 MW;  5F268E6B9D9A6C9F CRC64;
     MSTKQVTCRY FMHGVCREGS QCLFSHDLAN SKPSTICKYY QKGYCAYGAR CRYDHTKPPA
     AAGGAVGPAP NPSPSSGLHS PHPSPDIATS VMRTHSNEPG KREKKTLVLR DRNLTGLAED
     KTPPSKVNNP GGCSDPQTSP EMKPHSYLDA IRTGLDDLEA SSSYSNEPQL CPYAAAGECR
     LGDACVYLHG DMCEICRLQV LHPFDPEQRK AHEKMCMSTF EHEMEKAFAF QASQDKVCSI
     CMEVILEKAS ASERRFGILS NCSHTYCLSC IRQWRCAKQF ENPIIKSCPE CRVISEFVIP
     SVYWVEDQNK KNELIEAFKQ GMGKKACKYF EQGKGTCPFG SKCLYRHAYP DGRLAEPEKP
     RKQLSSEGTV RFFNSVRLWD FIENRETRQV PSTDDVDVTE LGDLFMHLSG VESSEP
//
ID   ACM3_MOUSE              Reviewed;         589 AA.
AC   Q9ERZ3; Q64055;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Muscarinic acetylcholine receptor M3;
DE   AltName: Full=Mm3 mAChR;
GN   Name=Chrm3; Synonyms=Chrm-3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Gomeza J., Wess J.;
RT   "Isolation, sequence and functional expression of mouse muscarinic
RT   acetylcholine receptor genes.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 314-439.
RC   TISSUE=Brain;
RX   MEDLINE=95179320; PubMed=7874308;
RX   DOI=10.1111/j.1460-9568.1994.tb00561.x;
RA   Andre C., Dos Santos G., Koulakoff A.;
RT   "Cultured neurons from mouse brain reproduce the muscarinic receptor
RT   profile of their tissue of origin.";
RL   Eur. J. Neurosci. 6:1691-1701(1994).
CC   -!- FUNCTION: The muscarinic acetylcholine receptor mediates various
CC       cellular responses, including inhibition of adenylate cyclase,
CC       breakdown of phosphoinositides and modulation of potassium
CC       channels through the action of G proteins. Primary transducing
CC       effect is Pi turnover.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity). Cell junction, synapse, postsynaptic cell
CC       membrane; Multi-pass membrane protein (By similarity). Basolateral
CC       cell membrane; Multi-pass membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Muscarinic acetylcholine receptor subfamily. CHRM3 sub-subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF264050; AAG14344.1; -; Genomic_DNA.
DR   EMBL; S74908; AAB33576.2; -; mRNA.
DR   IPI; IPI00112941; -.
DR   RefSeq; NP_150372.1; NM_033269.4.
DR   UniGene; Mm.342315; -.
DR   ProteinModelPortal; Q9ERZ3; -.
DR   SMR; Q9ERZ3; 67-565.
DR   STRING; Q9ERZ3; -.
DR   PhosphoSite; Q9ERZ3; -.
DR   PRIDE; Q9ERZ3; -.
DR   Ensembl; ENSMUST00000063093; ENSMUSP00000055579; ENSMUSG00000046159.
DR   GeneID; 12671; -.
DR   KEGG; mmu:12671; -.
DR   UCSC; uc007plb.1; mouse.
DR   CTD; 12671; -.
DR   MGI; MGI:88398; Chrm3.
DR   GeneTree; ENSGT00560000076730; -.
DR   HOGENOM; HBG713567; -.
DR   HOVERGEN; HBG105720; -.
DR   InParanoid; Q9ERZ3; -.
DR   OMA; ECFIQFL; -.
DR   OrthoDB; EOG4NVZK1; -.
DR   PhylomeDB; Q9ERZ3; -.
DR   NextBio; 281910; -.
DR   ArrayExpress; Q9ERZ3; -.
DR   Bgee; Q9ERZ3; -.
DR   CleanEx; MM_CHRM3; -.
DR   Genevestigator; Q9ERZ3; -.
DR   GermOnline; ENSMUSG00000046159; Mus musculus.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005887; C:integral to plasma membrane; TAS:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome.
DR   GO; GO:0007207; P:activation of phospholipase C activity by muscarinic acetylcholine receptor signaling pathway; TAS:MGI.
DR   GO; GO:0007586; P:digestion; IMP:MGI.
DR   GO; GO:0045987; P:positive regulation of smooth muscle contraction; IDA:MGI.
DR   GO; GO:0006939; P:smooth muscle contraction; IMP:MGI.
DR   GO; GO:0007271; P:synaptic transmission, cholinergic; TAS:MGI.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR001183; Musac_M3_rcpt.
DR   InterPro; IPR000995; Musac_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00243; MUSCARINICR.
DR   PRINTS; PR00540; MUSCRINICM3R.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Receptor; Synapse; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    589       Muscarinic acetylcholine receptor M3.
FT                                /FTId=PRO_0000069030.
FT   TOPO_DOM      1     66       Extracellular (By similarity).
FT   TRANSMEM     67     90       Helical; Name=1; (By similarity).
FT   TOPO_DOM     91    103       Cytoplasmic (By similarity).
FT   TRANSMEM    104    124       Helical; Name=2; (By similarity).
FT   TOPO_DOM    125    141       Extracellular (By similarity).
FT   TRANSMEM    142    163       Helical; Name=3; (By similarity).
FT   TOPO_DOM    164    183       Cytoplasmic (By similarity).
FT   TRANSMEM    184    206       Helical; Name=4; (By similarity).
FT   TOPO_DOM    207    228       Extracellular (By similarity).
FT   TRANSMEM    229    251       Helical; Name=5; (By similarity).
FT   TOPO_DOM    252    491       Cytoplasmic (By similarity).
FT   TRANSMEM    492    512       Helical; Name=6; (By similarity).
FT   TOPO_DOM    513    526       Extracellular (By similarity).
FT   TRANSMEM    527    546       Helical; Name=7; (By similarity).
FT   TOPO_DOM    547    589       Cytoplasmic (By similarity).
FT   MOTIF       274    280       Basolateral sorting signal (By
FT                                similarity).
FT   CARBOHYD      6      6       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     15     15       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     41     41       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     48     48       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     52     52       N-linked (GlcNAc...) (Potential).
FT   DISULFID    140    220       By similarity.
SQ   SEQUENCE   589 AA;  66212 MW;  AB782149EBEE7804 CRC64;
     MTLHSNSTTS PLFPNISSSW VHSPSEAGLP LGTVSQLDSY NISQTSGNFS SNDTSSDPLG
     GHTIWQVVFI AFLTGFLALV TIIGNILVIV AFKVNKQLKT VNNYFLLSLA CADLIIGVIS
     MNLFTTYIIM NRWALGNLAC DLWLSIDYVA SNASVMNLLV ISFDRYFSIT RPLTYRAKRT
     TKRAGVMIGL AWVISFVLWA PAILFWQYFV GKRTVPPGEC FIQFLSEPTI TFGTAIAAFY
     MPVTIMTILY WRIYKETEKR TKELAGLQAS GTEAEAENFV HPTGSSRSCS SYELQQQGTK
     RSSRRKYGGC HFWFTTKSWK PSAEQMDQDH SSSDSWNNND AAASLENSAS SDEEDIGSET
     RAIYSIVLKL PGHSTILNST KLPSSDNLQV PDKDLGTMDV ERNAHKLQAQ KSMDDRDNCQ
     KDFSKLPIQL ESAVDTAKTS DTNSSVDKTT AALPLSFKEA TLAKRFALKT RSQITKRKRM
     SLIKEKKAAQ TLSAILLAFI ITWTPYNIMV LVNTFCDSCI PKTYWNLGYW LCYINSTVNP
     VCYALCNKTF RTTFKMLLLC QCDKRKRRKQ QYQQRQSVIF HKRVPEQAL
//
ID   ACM2_MOUSE              Reviewed;         466 AA.
AC   Q9ERZ4;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Muscarinic acetylcholine receptor M2;
GN   Name=Chrm2; Synonyms=Chrm-2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Gomeza J., Wess J.;
RT   "Isolation, sequence and functional expression of mouse muscarinic
RT   acetylcholine receptor genes.";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232 AND SER-234, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: The muscarinic acetylcholine receptor mediates various
CC       cellular responses, including inhibition of adenylate cyclase,
CC       breakdown of phosphoinositides and modulation of potassium
CC       channels through the action of G proteins. Primary transducing
CC       effect is adenylate cyclase inhibition.
CC   -!- SUBUNIT: Interacts with ARRB1 and ARRB2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Cell junction, synapse, postsynaptic cell membrane; Multi-pass
CC       membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       Muscarinic acetylcholine receptor subfamily. CHRM2 sub-subfamily.
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DR   EMBL; AF264049; AAG14343.1; -; Genomic_DNA.
DR   IPI; IPI00112942; -.
DR   UniGene; Mm.448632; -.
DR   ProteinModelPortal; Q9ERZ4; -.
DR   SMR; Q9ERZ4; 22-456.
DR   STRING; Q9ERZ4; -.
DR   PhosphoSite; Q9ERZ4; -.
DR   PRIDE; Q9ERZ4; -.
DR   Ensembl; ENSMUST00000062520; ENSMUSP00000062955; ENSMUSG00000045613.
DR   UCSC; uc009biy.1; mouse.
DR   MGI; MGI:88397; Chrm2.
DR   GeneTree; ENSGT00560000076730; -.
DR   HOGENOM; HBG713567; -.
DR   HOVERGEN; HBG105720; -.
DR   InParanoid; Q9ERZ4; -.
DR   OrthoDB; EOG41JZCC; -.
DR   NextBio; 385914; -.
DR   Bgee; Q9ERZ4; -.
DR   CleanEx; MM_CHRM2; -.
DR   Genevestigator; Q9ERZ4; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004981; F:muscarinic acetylcholine receptor activity; IMP:MGI.
DR   InterPro; IPR000276; 7TM_GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_supfam.
DR   InterPro; IPR001065; Musac_M2_rcpt.
DR   InterPro; IPR000995; Musac_rcpt.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00243; MUSCARINICR.
DR   PRINTS; PR00539; MUSCRINICM2R.
DR   PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Disulfide bond;
KW   G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Receptor; Synapse; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    466       Muscarinic acetylcholine receptor M2.
FT                                /FTId=PRO_0000069022.
FT   TOPO_DOM      1     22       Extracellular (By similarity).
FT   TRANSMEM     23     45       Helical; Name=1; (By similarity).
FT   TOPO_DOM     46     59       Cytoplasmic (By similarity).
FT   TRANSMEM     60     80       Helical; Name=2; (By similarity).
FT   TOPO_DOM     81     97       Extracellular (By similarity).
FT   TRANSMEM     98    119       Helical; Name=3; (By similarity).
FT   TOPO_DOM    120    139       Cytoplasmic (By similarity).
FT   TRANSMEM    140    162       Helical; Name=4; (By similarity).
FT   TOPO_DOM    163    184       Extracellular (By similarity).
FT   TRANSMEM    185    207       Helical; Name=5; (By similarity).
FT   TOPO_DOM    208    388       Cytoplasmic (By similarity).
FT   TRANSMEM    389    409       Helical; Name=6; (By similarity).
FT   TOPO_DOM    410    423       Extracellular (By similarity).
FT   TRANSMEM    424    443       Helical; Name=7; (By similarity).
FT   TOPO_DOM    444    466       Cytoplasmic (By similarity).
FT   MOD_RES     232    232       Phosphoserine.
FT   MOD_RES     234    234       Phosphoserine.
FT   MOD_RES     446    446       Phosphothreonine (Potential).
FT   MOD_RES     450    450       Phosphothreonine (Potential).
FT   MOD_RES     465    465       Phosphothreonine (Potential).
FT   CARBOHYD      2      2       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD      3      3       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD      6      6       N-linked (GlcNAc...) (Potential).
FT   DISULFID     96    176       By similarity.
SQ   SEQUENCE   466 AA;  51515 MW;  CDCF281AD28276F8 CRC64;
     MNNSTNSSNN GLAITSPYKT FEVVFIVLVA GSLSLVTIIG NILVMVSIKV NRHLQTVNNY
     FLFSLACADL IIGVFSMNLY TLYTVIGYWP LGPVVCDLWL ALDYVVSNAS VMNLLIISFD
     RYFCVTKPLT YPVKRTTKMA GMMIAAAWVL SFILWAPAIL FWQFIVGVRT VEDGECYIQF
     FSNAAVTFGT AIAAFYLPVI IMTVLYWHIS RASKSRIKKE KKEPVANQDP VSPSLVQGRI
     VKPNNNNMPG GDGGLEHNKI QNGKALRDGG TENCVQGEEK ESSNDSTSVS AVASNMRDDE
     ITQDENTVST SLGHSKDDNS RQTCIKIVTK TQKGDACTPT STTVELVGSS GQNGDEKQNI
     VARKIVKMTK QPAKKKPPPS REKKVTRTIL AILLAFIITW APYNVMVLIN TFCAPCIPNT
     VWTIGYWLCY INSTINPACY ALCNATFKKT FKHLLMCHYK NIGATR
//
ID   UBE4B_MOUSE             Reviewed;        1173 AA.
AC   Q9ES00; Q9EQE0;
DT   04-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2003, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Ubiquitin conjugation factor E4 B;
DE   AltName: Full=Ubiquitin fusion degradation protein 2;
DE   AltName: Full=Ufd2a;
GN   Name=Ube4b; Synonyms=Ufd2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=C57BL/Ola; TISSUE=Brain;
RX   MEDLINE=20481916; PubMed=11027338; DOI=10.1073/pnas.97.21.11377;
RA   Conforti L., Tarlton A., Mack T.G.A., Mi W., Buckmaster E.A.,
RA   Wagner D., Perry V.H., Coleman M.P.;
RT   "A Ufd2/D4Cole1e chimeric protein and overexpression of Rbp7 in the
RT   slow Wallerian degeneration (WldS) mouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:11377-11382(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=T-cell;
RX   MEDLINE=22392632; PubMed=12504083; DOI=10.1016/S0006-291X(02)02834-6;
RA   Kaneko C., Hatakeyama S., Matsumoto M., Yada M., Nakayama K.,
RA   Nakayama K.;
RT   "Characterization of the mouse gene for the U-box-type ubiquitin
RT   ligase UFD2a.";
RL   Biochem. Biophys. Res. Commun. 300:297-304(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   SUBCELLULAR LOCATION, AND ROLE IN DELAY OF WALLERIAN DEGENERATION.
RX   MEDLINE=21626129; PubMed=11770485; DOI=10.1038/nn770;
RA   Mack T.G.A., Reiner M., Beirowski B., Mi W., Emanuelli M., Wagner D.,
RA   Thomson D., Gillingwater T., Court F., Conforti L., Fernando F.S.,
RA   Tarlton A., Andressen C., Addicks K., Magni G., Ribchester R.R.,
RA   Perry V.H., Coleman M.P.;
RT   "Wallerian degeneration of injured axons and synapses is delayed by a
RT   Ube4b/Nmnat chimeric gene.";
RL   Nat. Neurosci. 4:1199-1206(2001).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-101, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Binds to the ubiquitin moieties of preformed conjugates
CC       and catalyzes ubiquitin chain assembly in conjunction with E1, E2,
CC       and E3 (By similarity).
CC   -!- SUBUNIT: Interacts with VCP.
CC   -!- INTERACTION:
CC       Q01853:Vcp; NbExp=1; IntAct=EBI-80579, EBI-80597;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in neuronal tissues.
CC   -!- PTM: Proteolytically cleaved by caspases during apoptosis. Cleaved
CC       efficiently at Asp-123 by caspase-6 and granzyme B. Cleaved with
CC       approximately 10-fold less efficiency at Asp-109 by caspase-3 and
CC       caspase-7 (By similarity).
CC   -!- MISCELLANEOUS: In strain C57BL/Ola, a 85 kb region on chromosome 4
CC       containing Nmnat1 and Ube4b is triplicated. Ube4b becomes linked
CC       to Nmnat1 and encodes a fusion protein located in the nucleus
CC       which is responsible for the delayed Wallerian degeneration of
CC       injured axons in C57BL/Ola.
CC   -!- SIMILARITY: Belongs to the ubiquitin conjugation factor E4 family.
CC   -!- SIMILARITY: Contains 1 U-box domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF260924; AAG17285.1; ALT_TERM; mRNA.
DR   EMBL; AF260926; AAG17287.1; -; mRNA.
DR   EMBL; AF260927; AAG38492.1; -; Genomic_DNA.
DR   EMBL; AB083274; BAC56586.1; -; Genomic_DNA.
DR   EMBL; AK029914; BAC26672.1; -; mRNA.
DR   IPI; IPI00112597; -.
DR   UniGene; Mm.393991; -.
DR   UniGene; Mm.415260; -.
DR   PDB; 2KR4; NMR; -; A=1092-1173.
DR   PDBsum; 2KR4; -.
DR   ProteinModelPortal; Q9ES00; -.
DR   SMR; Q9ES00; 297-1171.
DR   IntAct; Q9ES00; 1.
DR   STRING; Q9ES00; -.
DR   PhosphoSite; Q9ES00; -.
DR   PRIDE; Q9ES00; -.
DR   Ensembl; ENSMUST00000103212; ENSMUSP00000099501; ENSMUSG00000028960.
DR   MGI; MGI:1927086; Ube4b.
DR   GeneTree; ENSGT00390000009300; -.
DR   HOVERGEN; HBG058129; -.
DR   InParanoid; Q9ES00; -.
DR   OrthoDB; EOG4C87RK; -.
DR   PhylomeDB; Q9ES00; -.
DR   ArrayExpress; Q9ES00; -.
DR   Bgee; Q9ES00; -.
DR   Genevestigator; Q9ES00; -.
DR   GermOnline; ENSMUSG00000028960; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0000151; C:ubiquitin ligase complex; TAS:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IDA:MGI.
DR   GO; GO:0051082; F:unfolded protein binding; NAS:UniProtKB.
DR   GO; GO:0006915; P:apoptosis; ISS:UniProtKB.
DR   GO; GO:0031175; P:neuron projection development; IMP:MGI.
DR   GO; GO:0006457; P:protein folding; NAS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
DR   GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; TAS:UniProtKB.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:MGI.
DR   GO; GO:0009411; P:response to UV; ISS:UniProtKB.
DR   GO; GO:0003222; P:ventricular trabecular myocardium morphogenesis; IMP:MGI.
DR   InterPro; IPR019474; Ub_conjug_fac_E4_core.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF04564; U-box; 1.
DR   Pfam; PF10408; Ufd2P_core; 1.
DR   SMART; SM00504; Ubox; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Phosphoprotein; Ubl conjugation pathway.
FT   CHAIN         1   1173       Ubiquitin conjugation factor E4 B.
FT                                /FTId=PRO_0000194994.
FT   DOMAIN     1102   1164       U-box.
FT   SITE        109    110       Cleavage; by caspase-3 and caspase-7 (By
FT                                similarity).
FT   SITE        123    124       Cleavage; by caspase-6 and granzyme B (By
FT                                similarity).
FT   MOD_RES      22     22       Phosphothreonine (By similarity).
FT   MOD_RES      26     26       Phosphothreonine (By similarity).
FT   MOD_RES      31     31       Phosphoserine.
FT   MOD_RES      84     84       Phosphoserine (By similarity).
FT   MOD_RES      87     87       Phosphoserine (By similarity).
FT   MOD_RES      88     88       Phosphoserine (By similarity).
FT   MOD_RES      90     90       Phosphoserine (By similarity).
FT   MOD_RES      92     92       Phosphoserine (By similarity).
FT   MOD_RES      95     95       Phosphothreonine (By similarity).
FT   MOD_RES     101    101       Phosphoserine.
FT   MOD_RES     105    105       Phosphoserine.
FT   MOD_RES     674    674       Phosphoserine (By similarity).
FT   MOD_RES    1136   1136       Phosphoserine (By similarity).
FT   CONFLICT    298    298       L -> P (in Ref. 1; AAG17287).
FT   CONFLICT    408    408       D -> E (in Ref. 3; BAC26672).
FT   CONFLICT    674    674       S -> T (in Ref. 3; BAC26672).
FT   CONFLICT    697    697       C -> Y (in Ref. 1; AAG17287).
FT   CONFLICT    753    753       E -> K (in Ref. 3; BAC26672).
FT   TURN       1101   1103
FT   TURN       1106   1108
FT   STRAND     1113   1117
FT   STRAND     1123   1125
FT   HELIX      1126   1135
FT   TURN       1140   1142
FT   HELIX      1148   1150
FT   HELIX      1155   1170
SQ   SEQUENCE   1173 AA;  133304 MW;  153853C06372F6CD CRC64;
     MEELSADEIR RRRLARLAGG QTSQPTTPLT SPQRENPPGP PIAASAPGPS QSLGLNVHNM
     TPATSPIGAA GVAHRSQSSE GVSSLSSSPS NSLETQSQSL SRSQSMDIDG VSCEKSMSQV
     DVDSGIENME VDENDRREKR SLSDKEPSSG PEVSEEQALQ LVCKIFRVSW KDRDRDVIFL
     SSLSAQFKQN PKEVFSDFKD LIGQILMEVL MMSTQTRDEN PFASLTATSQ PIATAARSPD
     RNLMLNTGSS SGTSPMFCNM GSFSTSSLSS LGASGGASNW DSYSDHFTIE TCKETDMLNY
     LIECFDRVGI EEKKAPKMCS QPAVSQLLSN IRSQCISHTA LVLQGSLTQP RSLQQPSFLV
     PYMLCRNLPY GFIQELVRTT HQDEEVFKQI FIPILQGLAL AAKECSLDSD YFKYPLMALG
     ELCETKFGKT HPMCNLVASL PLWLPKSLSP GSGRELQRLS YLGAFFSFSV FAEDDAKVVE
     KYFSGPAITL ENTRVVSQSL QHYLELGRQE LFKILHSILL NGETREAALS YMAALVNANM
     KKAQMQADDR LVSTDGFMLN LLWVLQQLST KIKLETVDPT YIFHPRCRIT LPNDETRINA
     TMEDVNERLT ELYGDQPPFS EPKFPTECFF LTLHAHHLSI LPSCRRYIRR LRAIRELNRT
     VEDLKNNESQ WKDSPLATRH REMLKRCKTQ LKKLVRCKAC ADAGLLDESF LRRCLNFYGL
     LIQLMLRILD PAYPDVTLPL NSEVPKVFAA LPEFYVEDVA EFLFFIVQYS PQVLYEPCTQ
     DIVMFLVVML CNQNYIRNPY LVAKLVEVMF MTNPSVQPRT QKFFEMIENH PLSTKLLVPS
     LMKFYTDVEH TGATSEFYDK FTIRYHISTI FKSLWQNIAH HGTFMEEFNS GKQFVRYINM
     LINDTTFLLD ESLESLKRIH EVQEEMKNKE QWDQLPRDQQ QARQSQLAQD ERVSRSYLAL
     ATETVDMFHL LTKQVQKPFL RPELGPRLAA MLNFNLQQLC GPKCRDLKVE NPEKYGFEPK
     KLLDQLTDIY LQLDCARFAK AIADDQRSYS KELFEEVISK MRKAGIKSTI AIEKFKLLAE
     KVEEIVAKNA RAEIDYSDAP DEFRDPLMDT LMTDPVRLPS GTVMDRSIIL RHLLNSPTDP
     FNRQMLTESM LEPVPELKEQ IQAWMREKQS SDH
//
ID   FOXJ2_MOUSE             Reviewed;         565 AA.
AC   Q9ES18;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Forkhead box protein J2;
DE   AltName: Full=Fork head homologous X;
GN   Name=Foxj2; Synonyms=Fhx;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Brain;
RX   PubMed=11025217; DOI=10.1016/S0925-4773(00)00410-X;
RA   Granadino B., Arias-de-la-Fuente C., Perez-Sanchez C., Parraga M.,
RA   Lopez-Fernandez L.A., del Mazo J., Rey-Campos J.;
RT   "Fhx (Foxj2) expression is activated during spermatogenesis and very
RT   early in embryonic development.";
RL   Mech. Dev. 97:157-160(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=16376864; DOI=10.1016/j.brainres.2005.11.022;
RA   Wijchers P.J.E.C., Hoekman M.F.M., Burbach J.P.H., Smidt M.P.;
RT   "Identification of forkhead transcription factors in cortical and
RT   dopaminergic areas of the adult murine brain.";
RL   Brain Res. 1068:23-33(2006).
CC   -!- FUNCTION: Transcriptional activator. Able to bind to two different
CC       type of DNA binding sites.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- TISSUE SPECIFICITY: In embryos, both cell layers of the
CC       blastocyst: the trophectoderm (TE) and the inner cell mass (ICM)
CC       show expression. Expressed in adult brain, heart skeletal muscle,
CC       lung, kidney and gonads. Liver, small intestine, and spleen also
CC       show expression but at lower levels. In the testis, expressed from
CC       pachytene spermatocytes to round spermatids, but not in
CC       spermatogonia. In addition to the germ lineage, also expressed in
CC       Sertoli cells of the testis. In the ovary, only granulosa cells of
CC       the follicles show expression. In the brain, expressed in the
CC       piriform cortex, hippocampus, habenula and in the granula cell
CC       layer in the cerebellum.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Zygotic expression first begins in 8-cell stage embryos, with
CC       expression increasing in blastocysts.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 fork-head DNA-binding domain.
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DR   EMBL; AF253052; AAG30406.1; -; mRNA.
DR   EMBL; BC040395; AAH40395.1; -; mRNA.
DR   IPI; IPI00112644; -.
DR   RefSeq; NP_068699.1; NM_021899.3.
DR   UniGene; Mm.87142; -.
DR   ProteinModelPortal; Q9ES18; -.
DR   SMR; Q9ES18; 66-147.
DR   STRING; Q9ES18; -.
DR   PhosphoSite; Q9ES18; -.
DR   PRIDE; Q9ES18; -.
DR   Ensembl; ENSMUST00000003238; ENSMUSP00000003238; ENSMUSG00000003154.
DR   Ensembl; ENSMUST00000112575; ENSMUSP00000108194; ENSMUSG00000003154.
DR   GeneID; 60611; -.
DR   KEGG; mmu:60611; -.
DR   UCSC; uc009dpr.1; mouse.
DR   CTD; 60611; -.
DR   MGI; MGI:1926805; Foxj2.
DR   GeneTree; ENSGT00560000076806; -.
DR   HOGENOM; HBG713235; -.
DR   HOVERGEN; HBG051648; -.
DR   InParanoid; Q9ES18; -.
DR   OMA; DMPPSNN; -.
DR   OrthoDB; EOG473PR7; -.
DR   PhylomeDB; Q9ES18; -.
DR   NextBio; 315058; -.
DR   ArrayExpress; Q9ES18; -.
DR   Bgee; Q9ES18; -.
DR   CleanEx; MM_FOXJ2; -.
DR   Genevestigator; Q9ES18; -.
DR   GermOnline; ENSMUSG00000003154; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   InterPro; IPR001766; TF_fork_head.
DR   InterPro; IPR018122; TF_fork_head_CS.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   PANTHER; PTHR11829; Fork_box_protein; 1.
DR   Pfam; PF00250; Fork_head; 1.
DR   PRINTS; PR00053; FORKHEAD.
DR   SMART; SM00339; FH; 1.
DR   PROSITE; PS00657; FORK_HEAD_1; FALSE_NEG.
DR   PROSITE; PS00658; FORK_HEAD_2; 1.
DR   PROSITE; PS50039; FORK_HEAD_3; 1.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    565       Forkhead box protein J2.
FT                                /FTId=PRO_0000091854.
FT   DNA_BIND     66    143       Fork-head.
FT   COMPBIAS    266    269       Poly-Ser.
FT   COMPBIAS    290    296       Poly-Gln.
FT   COMPBIAS    306    314       Poly-Gln.
FT   MOD_RES      46     46       Phosphoserine (By similarity).
FT   MOD_RES     161    161       Phosphoserine (By similarity).
FT   MOD_RES     172    172       Phosphoserine (By similarity).
FT   MOD_RES     259    259       Phosphotyrosine (By similarity).
FT   MOD_RES     261    261       Phosphoserine (By similarity).
SQ   SEQUENCE   565 AA;  61570 MW;  9178AFF3F9227AD4 CRC64;
     MASDLESSLT SIDWLPQLTL RATIEKLGSA SQAGPPGGAR KCSPGSPTDP NATLSKDEAA
     VHQDGKPRYS YATLITYAIN SSPAKKMTLS EIYRWICDNF PYYKNAGIGW KNSIRHNLSL
     NKCFRKVPRP RDDPGKGSYW TIDTCPDISR KRRHPPDDDL SQDSPEQEAS KSPRGGVPGS
     GEASLSHEGT PQMSLQSPSS VANYSQGPGS VDGGAVAAGA PGQESTEGAP PLYNTNHDFK
     FSYSEINFQD LSWSFRNLYK SMLERSSSSQ HGFSSLLGDM PPSNNYYVYQ QQQQQQPPPQ
     PQPPPQQPQP QQQQAPTQGP SNVGGAPPLH TPSPDGCTTP GGKQAGAEGY GPPTGMAMHP
     PPLQHGGYHP HQHHPHSHPA QQPPQPQAQS QASINSTGFA FPPDWCSNID SLKESFKMVN
     RLNWSSIEQS QFSELMESLR QAEQRNWTLD QHHIANLCDS LNHFLTQTGH MPQQGGSHRP
     PAPSRITDSC ALTSGKPEPS MNQVNSYGHP QASHLYPGPA PMYPISTQDS AGYNRPAHHM
     VPRPPVPPPG ANEEITDDFD WDLIT
//
ID   ARHG7_MOUSE             Reviewed;         862 AA.
AC   Q9ES28; O08757; Q3UTS5; Q6XPA5; Q6ZQI5; Q8C750; Q91ZZ6; Q9ES27;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   08-FEB-2011, entry version 97.
DE   RecName: Full=Rho guanine nucleotide exchange factor 7;
DE   AltName: Full=Beta-Pix;
DE   AltName: Full=PAK-interacting exchange factor beta;
DE   AltName: Full=p85SPR;
GN   Name=Arhgef7; Synonyms=Kiaa0142, Pak3bp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS G AND H).
RC   STRAIN=ICR; TISSUE=Brain;
RX   PubMed=15120616; DOI=10.1016/j.bbrc.2004.04.039;
RA   Rhee S., Yang S.J., Lee S.J., Park D.;
RT   "betaPix-b(L), a novel isoform of betaPix, is generated by alternative
RT   translation.";
RL   Biochem. Biophys. Res. Commun. 318:415-421(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS D AND F).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 59-862 (ISOFORM B), NUCLEOTIDE SEQUENCE
RP   [MRNA] OF 150-862 (ISOFORM C), AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=20318354; PubMed=10860822; DOI=10.1006/bbrc.2000.2845;
RA   Kim S., Kim T., Lee D., Park S.-H., Kim H., Park D.;
RT   "Molecular cloning of neuronally expressed mouse betaPix isoforms.";
RL   Biochem. Biophys. Res. Commun. 272:721-725(2000).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 63-862 (ISOFORM E), AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=11266127;
RA   Kim T., Park D.;
RT   "Molecular cloning and characterization of a novel mouse betaPix
RT   isoform.";
RL   Mol. Cells 11:89-94(2001).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 126-862 (ISOFORM A).
RC   TISSUE=Thymus;
RX   MEDLINE=97350865; PubMed=9207241; DOI=10.1006/bbrc.1997.6875;
RA   Oh W.K., Yoo J.C., Jo D., Song Y.H., Kim M.G., Park D.;
RT   "Cloning of a SH3 domain-containing proline-rich protein, p85SPR, and
RT   its localization in focal adhesion.";
RL   Biochem. Biophys. Res. Commun. 235:794-798(1997).
RN   [8]
RP   INTERACTION WITH GIT1.
RX   MEDLINE=99357767; PubMed=10428811; DOI=10.1074/jbc.274.32.22393;
RA   Bagrodia S., Bailey D., Lenard Z., Hart M., Guan J.L., Premont R.T.,
RA   Taylor S.J., Cerione R.A.;
RT   "A tyrosine-phosphorylated protein that binds to an important
RT   regulatory region on the cool family of p21-activated kinase-binding
RT   proteins.";
RL   J. Biol. Chem. 274:22393-22400(1999).
RN   [9]
RP   INTERACTION WITH GIT1 AND TGFB1I1.
RX   PubMed=12153727;
RA   Nishiya N., Shirai T., Suzuki W., Nose K.;
RT   "Hic-5 interacts with GIT1 with a different binding mode from
RT   paxillin.";
RL   J. Biochem. 132:279-289(2002).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-673, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-155, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; SER-673 AND
RP   SER-776, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497 AND SER-673, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 164-220.
RX   PubMed=16307729; DOI=10.1016/j.bbrc.2005.10.212;
RA   Li X., Liu X., Sun F., Gao J., Zhou H., Gao G.F., Bartlam M., Rao Z.;
RT   "Crystal structure of the N-terminal SH3 domain of mouse betaPIX, p21-
RT   activated kinase-interacting exchange factor.";
RL   Biochem. Biophys. Res. Commun. 339:407-414(2006).
CC   -!- FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF)
CC       and can induce membrane ruffling. May function as a positive
CC       regulator of apoptosis. May function in cell migration (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with PAK kinases through the SH3 domain.
CC       Interacts with unphosphorylated PAK1. Interacts with ITCH.
CC       Interacts with SCRIB; interaction is direct and may play a role in
CC       regulation of apoptosis (By similarity). Interacts with GIT1 and
CC       TGFB1I1. Interacts with FRMPD4 (via N-terminus) (By similarity).
CC   -!- INTERACTION:
CC       Q9JLQ2:Git2; NbExp=3; IntAct=EBI-642580, EBI-642860;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing, Alternative initiation; Named isoforms=8;
CC       Name=B;
CC         IsoId=Q9ES28-1; Sequence=Displayed;
CC       Name=A;
CC         IsoId=Q9ES28-2; Sequence=VSP_001817;
CC       Name=C;
CC         IsoId=Q9ES28-3; Sequence=VSP_001816;
CC       Name=D;
CC         IsoId=Q9ES28-4; Sequence=VSP_023052, VSP_023053, VSP_001817;
CC       Name=E; Synonyms=d;
CC         IsoId=Q9ES28-5; Sequence=VSP_023055, VSP_023057;
CC       Name=F;
CC         IsoId=Q9ES28-6; Sequence=VSP_023052, VSP_023053, VSP_023054,
CC                                  VSP_023056;
CC       Name=G; Synonyms=b(L);
CC         IsoId=Q9ES28-7; Sequence=VSP_023052, VSP_023053;
CC       Name=H; Synonyms=b;
CC         IsoId=Q9ES28-8; Sequence=VSP_023051;
CC         Note=Produced by alternative initiation at Met-158 of isoform G;
CC   -!- TISSUE SPECIFICITY: Seems to be expressed in the central nervous
CC       system. Isoform B, isoform C and isoform E are expressed with
CC       highest levels in brain and testis.
CC   -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB57691.1; Type=Erroneous initiation;
CC       Sequence=AAG18017.1; Type=Erroneous initiation;
CC       Sequence=AAG18018.1; Type=Erroneous initiation;
CC       Sequence=AAH44838.1; Type=Erroneous initiation;
CC       Sequence=AAK97363.1; Type=Erroneous initiation;
CC       Sequence=BAC35033.1; Type=Erroneous initiation;
CC       Sequence=BAC97874.1; Type=Erroneous initiation;
CC       Sequence=BAE23905.1; Type=Erroneous initiation;
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DR   EMBL; AK129064; BAC97874.1; ALT_INIT; mRNA.
DR   EMBL; AY220301; AAO65479.1; -; mRNA.
DR   EMBL; AK052545; BAC35033.1; ALT_INIT; mRNA.
DR   EMBL; AK139156; BAE23905.1; ALT_INIT; mRNA.
DR   EMBL; BC044838; AAH44838.1; ALT_INIT; mRNA.
DR   EMBL; AF247654; AAG18017.1; ALT_INIT; mRNA.
DR   EMBL; AF247655; AAG18018.1; ALT_INIT; mRNA.
DR   EMBL; AF343877; AAK97363.1; ALT_INIT; mRNA.
DR   EMBL; U96634; AAB57691.1; ALT_INIT; mRNA.
DR   IPI; IPI00230704; -.
DR   IPI; IPI00331212; -.
DR   IPI; IPI00387322; -.
DR   IPI; IPI00655136; -.
DR   IPI; IPI00828241; -.
DR   IPI; IPI00828536; -.
DR   IPI; IPI00828723; -.
DR   IPI; IPI00828966; -.
DR   RefSeq; NP_001106989.1; NM_001113517.1.
DR   RefSeq; NP_001106990.1; NM_001113518.1.
DR   RefSeq; NP_059098.2; NM_017402.4.
DR   UniGene; Mm.244068; -.
DR   PDB; 2ESW; X-ray; 2.01 A; A/B=164-220.
DR   PDBsum; 2ESW; -.
DR   ProteinModelPortal; Q9ES28; -.
DR   SMR; Q9ES28; 5-111, 162-560, 803-862.
DR   IntAct; Q9ES28; 9.
DR   MINT; MINT-1786275; -.
DR   STRING; Q9ES28; -.
DR   PhosphoSite; Q9ES28; -.
DR   PRIDE; Q9ES28; -.
DR   Ensembl; ENSMUST00000110909; ENSMUSP00000106534; ENSMUSG00000031511.
DR   Ensembl; ENSMUST00000110910; ENSMUSP00000106535; ENSMUSG00000031511.
DR   Ensembl; ENSMUST00000110911; ENSMUSP00000106536; ENSMUSG00000031511.
DR   Ensembl; ENSMUST00000110914; ENSMUSP00000106539; ENSMUSG00000031511.
DR   GeneID; 54126; -.
DR   KEGG; mmu:54126; -.
DR   UCSC; uc009kvx.1; mouse.
DR   CTD; 54126; -.
DR   MGI; MGI:1860493; Arhgef7.
DR   eggNOG; roNOG08839; -.
DR   GeneTree; ENSGT00600000084055; -.
DR   HOVERGEN; HBG050569; -.
DR   InParanoid; Q9ES28; -.
DR   OMA; TEAIRCW; -.
DR   NextBio; 310921; -.
DR   ArrayExpress; Q9ES28; -.
DR   Bgee; Q9ES28; -.
DR   CleanEx; MM_ARHGEF7; -.
DR   Genevestigator; Q9ES28; -.
DR   GermOnline; ENSMUSG00000031511; Mus musculus.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0043065; P:positive regulation of apoptosis; ISS:UniProtKB.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00033; CH; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50021; CH; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative initiation; Alternative splicing;
KW   Coiled coil; Guanine-nucleotide releasing factor; Phosphoprotein;
KW   SH3 domain.
FT   CHAIN         1    862       Rho guanine nucleotide exchange factor 7.
FT                                /FTId=PRO_0000080922.
FT   DOMAIN        1    111       CH.
FT   DOMAIN      163    222       SH3.
FT   DOMAIN      250    430       DH.
FT   DOMAIN      452    557       PH.
FT   COILED      804    854       Potential.
FT   MOD_RES     132    132       Phosphoserine.
FT   MOD_RES     155    155       Phosphoserine.
FT   MOD_RES     164    164       Phosphoserine.
FT   MOD_RES     228    228       Phosphoserine (By similarity).
FT   MOD_RES     497    497       Phosphoserine.
FT   MOD_RES     673    673       Phosphoserine.
FT   MOD_RES     776    776       Phosphoserine.
FT   VAR_SEQ       1    157       Missing (in isoform H).
FT                                /FTId=VSP_023051.
FT   VAR_SEQ       1     52       Missing (in isoform D, isoform F and
FT                                isoform G).
FT                                /FTId=VSP_023052.
FT   VAR_SEQ      53     55       IEK -> MLQ (in isoform D, isoform F and
FT                                isoform G).
FT                                /FTId=VSP_023053.
FT   VAR_SEQ     576    650       Missing (in isoform C).
FT                                /FTId=VSP_001816.
FT   VAR_SEQ     712    820       TWQGTDLMHNHVLADDDQSSLDSLGRRSSLSRLEPSDLSED
FT                                SEYDSIWTAHSYRMGSASRSRKESAPQVLLPEEEKIIVEET
FT                                KSNGQTVIEEKSLVDTVYALKDEVQEL -> SECRSSPRVG
FT                                TDYKQLLHGLAALEREVSGA (in isoform F).
FT                                /FTId=VSP_023054.
FT   VAR_SEQ     712    771       TWQGTDLMHNHVLADDDQSSLDSLGRRSSLSRLEPSDLSED
FT                                SEYDSIWTAHSYRMGSASR -> S (in isoform A
FT                                and isoform D).
FT                                /FTId=VSP_001817.
FT   VAR_SEQ     772    824       SRKESAPQVLLPEEEKIIVEETKSNGQTVIEEKSLVDTVYA
FT                                LKDEVQELRQDN -> KSCCSYISHQN (in isoform
FT                                E).
FT                                /FTId=VSP_023055.
FT   VAR_SEQ     821    862       Missing (in isoform F).
FT                                /FTId=VSP_023056.
FT   VAR_SEQ     825    862       Missing (in isoform E).
FT                                /FTId=VSP_023057.
FT   CONFLICT    485    488       NLLL -> KPSV (in Ref. 2; AAO65479, 5;
FT                                AAG18017/AAG18018 and 7; AAB57691).
FT   CONFLICT    492    492       A -> P (in Ref. 2; AAO65479, 5; AAG18017/
FT                                AAG18018 and 7; AAB57691).
FT   CONFLICT    616    616       S -> R (in Ref. 2; AAO65479, 5; AAG18017
FT                                and 7; AAB57691).
FT   CONFLICT    624    625       KT -> PH (in Ref. 7; AAB57691).
FT   CONFLICT    628    628       P -> A (in Ref. 2; AAO65479 and 7;
FT                                AAB57691).
FT   CONFLICT    630    630       S -> G (in Ref. 7; AAB57691).
FT   CONFLICT    633    633       C -> W (in Ref. 2; AAO65479, 5; AAG18017
FT                                and 7; AAB57691).
FT   CONFLICT    635    636       RP -> WT (in Ref. 7; AAB57691).
FT   STRAND      167    172
FT   STRAND      189    195
FT   STRAND      199    205
FT   STRAND      208    213
FT   HELIX       214    216
FT   STRAND      217    219
SQ   SEQUENCE   862 AA;  97056 MW;  46D61B606B8391B4 CRC64;
     MNSAEQTVTW LITLGVLESP KKTISDPEVF LQASLKDGVV LCRLLERLLP GTIEKVYPEP
     RNESECLSNI REFLRACGAS LRLETFDAND LYQGQNFNKV LSSLVTLNKV TADIGLGSDS
     VCARPSSHRI KSFDSLGSQS SHSRTSKLLQ SQYRSLDMTD NTNSQLVVRA KFNFQQTNED
     ELSFSKGDVI HVTRVEEGGW WEGTHNGRTG WFPSNYVREI KPSEKPVSPK SGTLKSPPKG
     FDTTAINKSY YNVVLQNILE TEHEYSKELQ SVLSTYLRPL QTSDKLSSAN TSYLMGNLEE
     ISSFQQVLVQ SLEECTKSPE AQQRVGGCFL SLMPQMRTLY LAYCANHPSA VSVLTEHSED
     LGEFMETKGA SSPGILVLTT GLSKPFMRLD KYPTLLKELE RHMEDYHPDR QDIQKSMTAF
     KNLSAQCQEV RKRKELELQI LTEPIRSWEG DDIKTLGSVT YMSQVTIQCA GSEEKNERYL
     LLFPNLLLML SASPRMSGFI YQGKLPTTGM TITKLEDSEN HRNAFEISGS MIERILVSCT
     SQQDLHEWVE HLQKQTKVTS VSNPTIKPHS VPSHTLPSHP LTPSSKHADS KPVALTPAYH
     TLPHPSHHGT PHTTISWGPL EPPKTPKPWS LSCLRPAPPL RPSAALCYKE DLSKSPKTMK
     KLLPKRKPER KPSDEEFAVR KSTAALEEDA QILKVIEAYC TSAKTRQTLN STWQGTDLMH
     NHVLADDDQS SLDSLGRRSS LSRLEPSDLS EDSEYDSIWT AHSYRMGSAS RSRKESAPQV
     LLPEEEKIIV EETKSNGQTV IEEKSLVDTV YALKDEVQEL RQDNKKMKKS LEEEQRARKD
     LEKLVRKVLK NMNDPAWDET NL
//
ID   UBE3B_MOUSE             Reviewed;        1070 AA.
AC   Q9ES34; Q8K068;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 3.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Ubiquitin-protein ligase E3B;
DE            EC=6.3.2.-;
GN   Name=Ube3b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J;
RX   PubMed=12837265; DOI=10.1016/S0888-7543(03)00111-3;
RA   Gong T.-W.L., Huang L., Warner S.J., Lomax M.I.;
RT   "Characterization of the human UBE3B gene: structure, expression,
RT   evolution, and alternative splicing.";
RL   Genomics 82:143-152(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Eye, Liver, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from
CC       an E2 ubiquitin-conjugating enzyme in the form of a thioester and
CC       then directly transfers the ubiquitin to targeted substrates (By
CC       similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- SIMILARITY: Contains 1 HECT (E6AP-type E3 ubiquitin-protein
CC       ligase) domain.
CC   -!- SIMILARITY: Contains 1 IQ domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH34059.1; Type=Erroneous initiation;
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DR   EMBL; AF244362; AAG16783.3; -; mRNA.
DR   EMBL; BC023956; AAH23956.1; -; mRNA.
DR   EMBL; BC034059; AAH34059.1; ALT_INIT; mRNA.
DR   EMBL; BC096743; AAH96743.1; -; mRNA.
DR   IPI; IPI00112716; -.
DR   RefSeq; NP_473434.2; NM_054093.2.
DR   UniGene; Mm.28792; -.
DR   HSSP; Q9H0M0; 1ND7.
DR   ProteinModelPortal; Q9ES34; -.
DR   SMR; Q9ES34; 639-1063.
DR   PhosphoSite; Q9ES34; -.
DR   PRIDE; Q9ES34; -.
DR   Ensembl; ENSMUST00000074002; ENSMUSP00000073652; ENSMUSG00000029577.
DR   GeneID; 117146; -.
DR   KEGG; mmu:117146; -.
DR   UCSC; uc008yzn.1; mouse.
DR   CTD; 117146; -.
DR   MGI; MGI:1891295; Ube3b.
DR   eggNOG; roNOG11006; -.
DR   GeneTree; ENSGT00550000074668; -.
DR   HOGENOM; HBG315289; -.
DR   HOVERGEN; HBG108644; -.
DR   InParanoid; Q9ES34; -.
DR   OMA; FFTIRKR; -.
DR   OrthoDB; EOG4R501Z; -.
DR   PhylomeDB; Q9ES34; -.
DR   NextBio; 369516; -.
DR   ArrayExpress; Q9ES34; -.
DR   Bgee; Q9ES34; -.
DR   CleanEx; MM_UBE3B; -.
DR   Genevestigator; Q9ES34; -.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0006464; P:protein modification process; IEA:InterPro.
DR   InterPro; IPR000569; HECT.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00612; IQ; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00015; IQ; 1.
DR   SUPFAM; SSF56204; HECT; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS50096; IQ; 1.
PE   2: Evidence at transcript level;
KW   Ligase; Phosphoprotein; Ubl conjugation pathway.
FT   CHAIN         1   1070       Ubiquitin-protein ligase E3B.
FT                                /FTId=PRO_0000281883.
FT   DOMAIN       29     58       IQ.
FT   DOMAIN      704   1070       HECT.
FT   ACT_SITE   1038   1038       Glycyl thioester intermediate (By
FT                                similarity).
FT   MOD_RES     421    421       Phosphoserine (By similarity).
SQ   SEQUENCE   1070 AA;  122762 MW;  AEC9A7F4232A434E CRC64;
     MFTVSQTSRA WFIDRARQAR EERLVQKERE RSAVTIQALV RSFLCRRRLH RDIRKEIDEF
     FSADESGSSK RSALCIFKIA RRLLFICKTT EDSERLEKLC RSILNSMDAE NEPKVWYVSL
     ALSKDLTLLW IKQIKSILWH CCELLGQLKP EILQDSRLIT LYLTMLVTFT DTSTWKILRG
     KGESLRPALN HICANIMGHL NQRGLYSVLQ VLLTRGLARP RPCLSKGMLT AAFSLALRPV
     VAAQFSDNLM RPFIIHVMSV PALVAHLSTV APERLGVLES HDMLRKFIVF LRDRDRCRDA
     CESLEGCHTL CLMGNLLHLG SLSLRLLEEE MDGFVSALTQ MLCYCQKYVA QKKSNLTHWH
     PVLGWFSQPV DYGLNDSMYL ITKQLQFLWA VPLIRILFSD ILSRKLLEHA EPAPVQPQPS
     SPQTVLPVKS LLKRAFQKSA SVRNILRPVG GRRVDSAEVR KVCNICVLYQ TSLTTLTQIR
     LQILTGLTYL DDLLPKLWAF ICELGPHGGL KLFLECLNND TGESKQLLAM LMLFCDCSRH
     LITILDDIEV YEEQISFKLE ELVTISSFLN SFVFKMIWDG IVENAKGETL ELFQSVHGWL
     MVLYERDCRR RFAPEDHWLR RDLKPGVLFQ ELDKDRRRAQ LVLQHIPHVV PHKNRVLLFR
     NMVIKEKEKL GLVETSSASP HVTHITIRRS RMLEDGYEQL RQLSQHAMKG VIRVKFVNDL
     GVDEAGIDQD GVFKEFLEEI IKRVFDPALN LFKTTSGDER LYPSPTSYIH ENYLQLFEFV
     GKMLGKAVYE GIVVDVPFAS FFLSQMLGHH HSVFYSSVDE LPSLDSEFYK NLTSIKRYDG
     DIADLGLTLS YDEDVMGQLV CHELVPGGKT IPVTDENKIS YIHLMAHFRM HTQIKNQTAA
     LISGFRSIIK PEWIRMFSTP ELQRLISGDN AEIDLEDLKK HTVYYGGFHG SHRVIIWLWD
     ILASDFTPEE RAMFLKFVTS CSRPPLLGFA YLKPPFSIRC VEVSDDQDTG DTLGSVLRGF
     FTIRKREPGG RLPTSSTCFN LLKLPNYSKK SVLREKLRYA ISMNTGFELS
//
ID   RTN3_MOUSE              Reviewed;         964 AA.
AC   Q9ES97; Q3UF62; Q544J1; Q68FE4; Q6IM69; Q6R8K6; Q6R8K7; Q6T929;
AC   Q8C6D5; Q8CCU2;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Reticulon-3;
GN   Name=Rtn3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX   PubMed=11990451;
RA   Hamada N., Iwahashi J., Suzuki K., Ogi H., Kashiwagi T., Hara K.,
RA   Toyoda M., Yamada T., Toyoda T.;
RT   "Molecular cloning and characterization of the mouse reticulon 3
RT   cDNA.";
RL   Cell. Mol. Biol. 48:163-172(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND IDENTIFICATION (ISOFORM
RP   4).
RX   MEDLINE=22715887; PubMed=12832288; DOI=10.1096/fj.02-1166hyp;
RA   Oertle T., Klinger M., Stuermer C.A.O., Schwab M.E.;
RT   "A reticular rhapsody: phylogenic evolution and nomenclature of the
RT   RTN/Nogo gene family.";
RL   FASEB J. 17:1238-1247(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF
RP   83-964 (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4 AND 5),
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=FVB/N;
RX   PubMed=15350194; DOI=10.1042/BJ20040458;
RA   Di Scala F., Dupuis L., Gaiddon C., De Tapia M., Jokic N.,
RA   Gonzalez de Aguilar J.-L., Raul J.-S., Ludes B., Loeffler J.-P.;
RT   "Tissue specificity and regulation of the N-terminal diversity of
RT   reticulon 3.";
RL   Biochem. J. 385:125-134(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J;
RX   PubMed=15946766; DOI=10.1016/j.molbrainres.2005.04.020;
RA   Cai Y., Saiyin H., Lin Q., Zhang P., Tang L., Pan X., Yu L.;
RT   "Identification of a new RTN3 transcript, RTN3-A1, and its
RT   distribution in adult mouse brain.";
RL   Brain Res. Mol. Brain Res. 138:236-243(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA   Huang X., Zhou Y., Qiang H., Yuan J., Qiang B.;
RT   "Cloning and expression profile of a novel mouse cDNA encoding a human
RT   RTN3 homolog.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Heart, Hippocampus, Medulla oblongata, Sympathetic ganglion,
RC   Thymus, Tongue, and Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6; TISSUE=Brain, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   PROTEIN SEQUENCE OF 103-110; 153-164 AND 204-214, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230; THR-524; THR-526;
RP   THR-671 AND SER-673, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [10]
RP   INTERACTION WITH ATL1 AND ATL2.
RX   PubMed=19665976; DOI=10.1016/j.cell.2009.05.025;
RA   Hu J., Shibata Y., Zhu P.-P., Voss C., Rismanchi N., Prinz W.A.,
RA   Rapoport T.A., Blackstone C.;
RT   "A class of dynamin-like GTPases involved in the generation of the
RT   tubular ER network.";
RL   Cell 138:549-561(2009).
CC   -!- FUNCTION: May be involved in membrane trafficking in the early
CC       secretory pathway. Inhibits BACE1 activity and amyloid precursor
CC       protein processing. May induce caspase-8 cascade and apoptosis.
CC       May favor BCL2 translocation to the mitochondria upon endoplasmic
CC       reticulum stress (By similarity).
CC   -!- SUBUNIT: Homodimer. Interacts with RTN4. Isoform 3 interacts with
CC       BACE1, BACE2, BCL2 and FADD (By similarity). Interacts with ATL1
CC       and ATL2.
CC   -!- INTERACTION:
CC       Q8BWG8:Arrb1; NbExp=2; IntAct=EBI-643369, EBI-641778;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein. Golgi apparatus membrane; Multi-pass membrane
CC       protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1; Synonyms=A1, A4b, B;
CC         IsoId=Q9ES97-1; Sequence=Displayed;
CC       Name=2; Synonyms=A2, A3b;
CC         IsoId=Q9ES97-2; Sequence=VSP_023763;
CC       Name=3; Synonyms=B1, A1, Rtn3c;
CC         IsoId=Q9ES97-3; Sequence=VSP_023762;
CC       Name=4; Synonyms=B2, A2;
CC         IsoId=Q9ES97-4; Sequence=VSP_023764;
CC       Name=5; Synonyms=A4a;
CC         IsoId=Q9ES97-5; Sequence=VSP_023765;
CC   -!- TISSUE SPECIFICITY: Isoform 1, isoform 3, isoform 4 and isoform 5
CC       are expressed in spinal cord. Isoform 1 is present in brain, where
CC       it is expressed in the neurons of cerebral cortex, hippocampus,
CC       hypothalamus and cerebellum (at protein level).
CC   -!- SIMILARITY: Contains 1 reticulon domain.
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DR   EMBL; AB046114; BAB62070.1; -; mRNA.
DR   EMBL; BK001796; DAA01968.1; -; mRNA.
DR   EMBL; AY164700; AAP47278.1; -; mRNA.
DR   EMBL; AY507126; AAR98631.1; -; mRNA.
DR   EMBL; AY507127; AAR98632.1; -; mRNA.
DR   EMBL; AY427822; AAR08193.1; -; mRNA.
DR   EMBL; AY750849; AAU81931.1; -; mRNA.
DR   EMBL; AF195940; AAG31360.1; -; mRNA.
DR   EMBL; AK032109; BAC27708.1; -; mRNA.
DR   EMBL; AK036892; BAC29625.1; -; mRNA.
DR   EMBL; AK049845; BAC33952.1; -; mRNA.
DR   EMBL; AK075883; BAC36028.1; -; mRNA.
DR   EMBL; AK088670; BAC40493.1; -; mRNA.
DR   EMBL; AK146505; BAE27220.1; -; mRNA.
DR   EMBL; AK148792; BAE28664.1; -; mRNA.
DR   EMBL; AK148947; BAE28699.1; -; mRNA.
DR   EMBL; AK165683; BAE38336.1; -; mRNA.
DR   EMBL; BC014697; AAH14697.1; -; mRNA.
DR   EMBL; BC036717; AAH36717.1; -; mRNA.
DR   EMBL; BC079882; AAH79882.1; -; mRNA.
DR   IPI; IPI00112948; -.
DR   IPI; IPI00470981; -.
DR   IPI; IPI00474993; -.
DR   IPI; IPI00480414; -.
DR   IPI; IPI00750847; -.
DR   RefSeq; NP_001003933.1; NM_001003933.1.
DR   RefSeq; NP_001003934.1; NM_001003934.1.
DR   RefSeq; NP_444306.1; NM_053076.2.
DR   UniGene; Mm.246990; -.
DR   UniGene; Mm.453608; -.
DR   ProteinModelPortal; Q9ES97; -.
DR   SMR; Q9ES97; 826-885.
DR   IntAct; Q9ES97; 13.
DR   STRING; Q9ES97; -.
DR   PhosphoSite; Q9ES97; -.
DR   PRIDE; Q9ES97; -.
DR   Ensembl; ENSMUST00000025667; ENSMUSP00000025667; ENSMUSG00000024758.
DR   Ensembl; ENSMUST00000065304; ENSMUSP00000065810; ENSMUSG00000024758.
DR   Ensembl; ENSMUST00000088169; ENSMUSP00000085494; ENSMUSG00000024758.
DR   Ensembl; ENSMUST00000088171; ENSMUSP00000085496; ENSMUSG00000024758.
DR   GeneID; 20168; -.
DR   KEGG; mmu:20168; -.
DR   UCSC; uc008gle.1; mouse.
DR   CTD; 20168; -.
DR   MGI; MGI:1339970; Rtn3.
DR   eggNOG; roNOG04901; -.
DR   GeneTree; ENSGT00390000009934; -.
DR   HOVERGEN; HBG093922; -.
DR   InParanoid; Q9ES97; -.
DR   OMA; QFSHTTA; -.
DR   OrthoDB; EOG4229M0; -.
DR   NextBio; 297685; -.
DR   ArrayExpress; Q9ES97; -.
DR   Bgee; Q9ES97; -.
DR   CleanEx; MM_RTN3; -.
DR   Genevestigator; Q9ES97; -.
DR   GermOnline; ENSMUSG00000024758; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.
DR   InterPro; IPR003388; Reticulon.
DR   PANTHER; PTHR10994; Reticulon; 1.
DR   Pfam; PF02453; Reticulon; 1.
DR   PROSITE; PS50845; RETICULON; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Apoptosis;
KW   Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport;
KW   Golgi apparatus; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    964       Reticulon-3.
FT                                /FTId=PRO_0000168164.
FT   TRANSMEM    796    816       Helical; (Potential).
FT   TRANSMEM    877    899       Helical; (Potential).
FT   TRANSMEM    904    926       Helical; (Potential).
FT   DOMAIN      776    964       Reticulon.
FT   REGION      919    964       Interaction with FADD (By similarity).
FT   REGION      932    934       Interaction with BACE1 (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      31     31       Phosphoserine (By similarity).
FT   MOD_RES     217    217       Phosphoserine (By similarity).
FT   MOD_RES     230    230       Phosphoserine.
FT   MOD_RES     524    524       Phosphothreonine.
FT   MOD_RES     526    526       Phosphothreonine.
FT   MOD_RES     596    596       Phosphoserine (By similarity).
FT   MOD_RES     597    597       Phosphoserine (By similarity).
FT   MOD_RES     671    671       Phosphothreonine.
FT   MOD_RES     673    673       Phosphoserine.
FT   VAR_SEQ      49    775       Missing (in isoform 3).
FT                                /FTId=VSP_023762.
FT   VAR_SEQ      49     67       Missing (in isoform 2).
FT                                /FTId=VSP_023763.
FT   VAR_SEQ      68    775       Missing (in isoform 4).
FT                                /FTId=VSP_023764.
FT   VAR_SEQ      68    388       Missing (in isoform 5).
FT                                /FTId=VSP_023765.
FT   CONFLICT     17     17       S -> P (in Ref. 3; AAR98631).
FT   CONFLICT    215    215       S -> P (in Ref. 3; AAR98632).
FT   CONFLICT    355    355       E -> G (in Ref. 3; AAR98632).
FT   CONFLICT    899    899       M -> I (in Ref. 6; BAC36028).
FT   CONFLICT    964    964       E -> K (in Ref. 6; BAE28664/BAE28699).
SQ   SEQUENCE   964 AA;  103879 MW;  5170809A696F8F7A CRC64;
     MAESSAATQS PSVSSSSSGA EPSALGGGGG SPGACPALGA KSCGSSCADS FVSSSSSQPV
     SIFSTSQAGL SSLCSDEPPS KSMTSSFLSS SEIHNPDPTT PLGEKSETLG SQFVLAKGKD
     PLVLLDKKKL DSPQGTNKDR VDAPVSLATG IPCSHPSIPD SFPEQPAFLS KEIGPAEEWV
     VKDQEPKNPN KVPDGEDRSA LDFGQSKAEH ICTYSLSPSE LPVASVEKDS PESPFEVIID
     KATFDREFKD LYKENPNDLG GWAAHGDRES PADLLEMNDK LFPLRNKEAG RYPSSVLLGR
     QFSHTTAALE EVSRCVNDMH NFTNEILTWD LDPQAKQQAN KTSCTTESTG LDRSELRSEI
     PVINLKTNPQ QKMPVCSFNG STPITKSTGD WTEAFTEGKP VRDYLSSTKE AGGNGVPGSS
     QLHSELPGSM PEKWVSGSGA ATVEVTLPNL RGAWPNSVMG EVTEVDSSGE SDDTVIEDIT
     EKPDSLPSAA AKTSEREIKE TPSRETVRSE MCENSEQPQA QPETPTQKSL EGEVASQVPN
     TLNEVTPEKL DMTNNPKVCS AAPPSVLNET GFSLTVPASA KLESLLGKYV EDTDGSSPED
     LMAVLTGAEE KGIVDKEEGD VLEAVLEKIA DFKNTLPVEL LHESELSGSE TKNIKSKYSE
     DSRETTGGAP TMSPDLEQEQ LTIRAIKELG ERQAEKVQDE GISSGGKLKQ TFAPQSGPQS
     SSDILEHTDV KTGSDLGIPK NPTIIKNTRI DSISSLTKTE MVNKNVLARL LSDFPVHDLI
     FWRDVKKTGF VFGTTLIMLL SLAAFSVISV VSYLILALLS VTISFRVYKS VIQAVQKSEE
     GHPFKAYLDV DITLSSEAFH NYMNAAMVHV NKALKLIIRL FLVEDLVDSL KLAVFMWLMT
     YVGAVFNGIT LLILAELLVF SVPIVYEKYK TQIDHYVGIA RDQTKSIVEK IQAKLPGIAK
     KKAE
//
ID   AFF4_MOUSE              Reviewed;        1160 AA.
AC   Q9ESC8; B2RST9; Q8C6K4; Q8C6W3; Q8CCH3;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=AF4/FMR2 family member 4;
GN   Name=Aff4; Synonyms=Alf4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=NIH Black Swiss;
RX   MEDLINE=20171376; PubMed=10704283; DOI=10.1006/geno.1999.6100;
RA   Wenderfer S.E., Slack J.P., McCluskey T.S., Monaco J.J.;
RT   "Identification of 40 genes on a 1-Mb contig around the IL-4 cytokine
RT   family gene cluster on mouse chromosome 11.";
RL   Genomics 63:354-373(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, Ovary, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=16024815; DOI=10.1128/MCB.25.15.6834-6845.2005;
RA   Urano A., Endoh M., Wada T., Morikawa Y., Itoh M., Kataoka Y.,
RA   Taki T., Akazawa H., Nakajima H., Komuro I., Yoshida N., Hayashi Y.,
RA   Handa H., Kitamura T., Nosaka T.;
RT   "Infertility with defective spermiogenesis in mice lacking AF5q31, the
RT   target of chromosomal translocation in human infant leukemia.";
RL   Mol. Cell. Biol. 25:6834-6845(2005).
CC   -!- FUNCTION: May play a role in transcriptional regulation.
CC   -!- SUBUNIT: Component of the cyclin-dependent kinase pair
CC       (CDK9/cyclin-T1) complex, also called positive transcription
CC       elongation factor b (P-TEFb) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis by Sertoli cells,
CC       and at low levels in other tissues.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout embryogenesis with
CC       maximum expression at 10.5 and 12.5 dpc.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice are infertile with azoospermia.
CC       Spermatogenesis is arrested at the level of spermiogenesis.
CC   -!- SIMILARITY: Belongs to the AF4 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC28178.1; Type=Frameshift; Positions=921;
CC       Sequence=BAC35763.1; Type=Frameshift; Positions=573, 577;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF190449; AAG17126.1; -; mRNA.
DR   EMBL; AK033163; BAC28178.1; ALT_FRAME; mRNA.
DR   EMBL; AK053034; BAC35244.1; -; mRNA.
DR   EMBL; AK054401; BAC35763.1; ALT_FRAME; mRNA.
DR   EMBL; BC138999; AAI39000.1; -; mRNA.
DR   IPI; IPI00113246; -.
DR   RefSeq; NP_291043.1; NM_033565.2.
DR   UniGene; Mm.395281; -.
DR   ProteinModelPortal; Q9ESC8; -.
DR   STRING; Q9ESC8; -.
DR   PhosphoSite; Q9ESC8; -.
DR   PRIDE; Q9ESC8; -.
DR   Ensembl; ENSMUST00000060945; ENSMUSP00000051479; ENSMUSG00000049470.
DR   GeneID; 93736; -.
DR   KEGG; mmu:93736; -.
DR   UCSC; uc007ivu.1; mouse.
DR   CTD; 93736; -.
DR   MGI; MGI:2136171; Aff4.
DR   eggNOG; roNOG10359; -.
DR   GeneTree; ENSGT00530000063217; -.
DR   HOGENOM; HBG715005; -.
DR   HOVERGEN; HBG004189; -.
DR   InParanoid; Q9ESC8; -.
DR   OMA; TEHLKNS; -.
DR   OrthoDB; EOG4CC40N; -.
DR   PhylomeDB; Q9ESC8; -.
DR   NextBio; 351587; -.
DR   ArrayExpress; Q9ESC8; -.
DR   Bgee; Q9ESC8; -.
DR   CleanEx; MM_AFF4; -.
DR   Genevestigator; Q9ESC8; -.
DR   GermOnline; ENSMUSG00000049470; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0007286; P:spermatid development; IMP:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR007797; TF_AF4/FMR2.
DR   PANTHER; PTHR10528; AF-4; 1.
DR   Pfam; PF05110; AF-4; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Nucleus; Phosphoprotein; Proto-oncogene; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   1160       AF4/FMR2 family member 4.
FT                                /FTId=PRO_0000239394.
FT   COMPBIAS    102    456       Ser-rich.
FT   COMPBIAS    784    896       Ser-rich.
FT   COMPBIAS   1032   1079       Ser-rich.
FT   MOD_RES      31     31       Phosphoserine (By similarity).
FT   MOD_RES      32     32       Phosphoserine (By similarity).
FT   MOD_RES      79     79       N6-acetyllysine (By similarity).
FT   MOD_RES     124    124       Phosphoserine (By similarity).
FT   MOD_RES     173    173       Phosphoserine (By similarity).
FT   MOD_RES     205    205       Phosphoserine (By similarity).
FT   MOD_RES     207    207       Phosphoserine (By similarity).
FT   MOD_RES     217    217       Phosphoserine (By similarity).
FT   MOD_RES     382    382       Phosphoserine (By similarity).
FT   MOD_RES     383    383       Phosphoserine (By similarity).
FT   MOD_RES     384    384       Phosphoserine (By similarity).
FT   MOD_RES     387    387       Phosphoserine (By similarity).
FT   MOD_RES     482    482       Phosphoserine (By similarity).
FT   MOD_RES     486    486       Phosphoserine (By similarity).
FT   MOD_RES     494    494       Phosphoserine (By similarity).
FT   MOD_RES     523    523       Phosphothreonine (By similarity).
FT   MOD_RES     544    544       Phosphoserine (By similarity).
FT   MOD_RES     594    594       Phosphoserine (By similarity).
FT   MOD_RES     612    612       Phosphoserine (By similarity).
FT   MOD_RES     663    663       Phosphotyrosine (By similarity).
FT   MOD_RES     666    666       Phosphoserine (By similarity).
FT   MOD_RES     669    669       Phosphothreonine (By similarity).
FT   MOD_RES     689    689       Phosphoserine (By similarity).
FT   MOD_RES     698    698       Phosphoserine (By similarity).
FT   MOD_RES     701    701       Phosphoserine (By similarity).
FT   MOD_RES     707    707       Phosphotyrosine (By similarity).
FT   MOD_RES     809    809       Phosphoserine (By similarity).
FT   MOD_RES     831    831       Phosphoserine (By similarity).
FT   MOD_RES    1040   1040       Phosphoserine (By similarity).
FT   MOD_RES    1052   1052       Phosphoserine (By similarity).
FT   MOD_RES    1055   1055       Phosphoserine (By similarity).
FT   MOD_RES    1059   1059       Phosphoserine (By similarity).
FT   CONFLICT    932    932       R -> S (in Ref. 2; BAC28178).
FT   CONFLICT    980    980       L -> Q (in Ref. 2; BAC28178).
FT   CONFLICT   1088   1088       Q -> K (in Ref. 2; BAC28178).
SQ   SEQUENCE   1160 AA;  126639 MW;  0C13253EAC9192B3 CRC64;
     MNREDRNVLR MKERERRNQE IQQGEDAFPP SSPLFAEPYK VTSKEDKLSS RIQSMLGNYD
     EMKDYIGDRS IPKLVAIPKP AVPTTTDEKA NPNFFEQRHG GSHQSSKWTP VGPAPSTSQS
     QKRSSALQSG HSSQRSGAGG SGASSSGQRH DRDSYSSSRK KGQHGSEHSK SRSSSPGKPQ
     AVSSLSSSHS RSHGNDHHSK EHQRSKSPRD PDANWDSPSR GPFSSGQHSS QSFPPSLMSK
     SSSMLQKPTA YVRPMDGQES VEPKLSSEHY SSQSHGNSMT ELKPSSKAHL TKLKIPSRPL
     DASVSGDVSC VDEILKEMTH SWPPPLTAIH TPCKTEPSKF PFPTKESQQS NFGPGEQKRY
     STAKTSNGHQ SKSMLKDDLK LSSSEDSDGE QDCDKTMPRS TPGSNSEPSH HNSEGADNSR
     DDSSSHSGSE SSSGSDSESE SSSSDSEANE PSQSASPEPE PPPTNKWQLD NWLNKVNPHK
     VSPASSVDSN IPSSQAYKKE GREQGTASNY TDPGGTKETS SATPGRDSKT IQKGSESGRG
     RQKSPAQSDS TTQRRTVGKK QPKKPEKSAA EEPRGGLKIE SETPVDMAAS MPSSRHKAAT
     KGSRKPNIKK ESKSSPRPTA EKKKYKSASK PSQKSREIIE TDTSSSDSDG SESLPPSSQT
     PKYPESNRTP VKPSSVEEED SFFRQRMFSP MEEKELLSPL SEPDDRYPLI VKIDLNLLTR
     IPGKPYKETE PPKGEKKNVP EKHSREVQKQ ASEKASNKGK RKHKNDDDTR ASESKKPKTE
     DKNSSGHKPS SSRESSKQSS TKEKDLLPSP AGPILSKDSK TEHGSRKRTV SQSSSLKSSG
     TSSKENSGSS SKSSSSSTAK QKKTEGKGPS SSKEAKEKAP NSSSNCPPST PTSESSKPRR
     TKLAFDDRNY SADHYLQEAK KLKHNADALS DRFEKAVYYL DAVVSFIECG NALEKNAQES
     KSPFPMYSDT VELIKYTMKL KNYLAPDATA ADKRLTVLCL RCQSLLYLRL FKLKKENALK
     YSKTLTEHLK NSYSNSQAPS PGLGSKAVGM PSPVSPKLSP GNSGSYSSGG SSASASGSSV
     TIPQKIHQMA ASYVQVTSNF LYATEIWDQA EQLSKEQKEF FAELDKVMGP LIFNASIMTD
     LARYTRQGLH WLRQDAKLIS
//
ID   LRBA_MOUSE              Reviewed;        2856 AA.
AC   Q9ESE1; Q9ESD3; Q9ESD4;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Lipopolysaccharide-responsive and beige-like anchor protein;
DE   AltName: Full=Beige-like protein;
GN   Name=Lrba; Synonyms=Bgl, Lba;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION,
RP   SUBCELLULAR LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   MEDLINE=21154060; PubMed=11254716;
RA   Wang J.-W., Howson J., Haller E., Kerr W.G.;
RT   "Identification of a novel lipopolysaccharide-inducible gene with key
RT   features of both A kinase anchor proteins and chs1/beige proteins.";
RL   J. Immunol. 166:4586-4595(2001).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-904, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1005, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-979, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May be involved in coupling signal transduction and
CC       vesicle trafficking to enable polarized secretion and/or membrane
CC       deposition of immune effector molecules.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein
CC       (Potential). Endoplasmic reticulum. Golgi apparatus, trans-Golgi
CC       network. Lysosome.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=lba-alpha;
CC         IsoId=Q9ESE1-1; Sequence=Displayed;
CC       Name=2; Synonyms=lba-beta;
CC         IsoId=Q9ESE1-2; Sequence=VSP_038229, VSP_038230;
CC       Name=3; Synonyms=lba-gamma;
CC         IsoId=Q9ESE1-3; Sequence=VSP_038227, VSP_038228;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is expressed in the brain, is absent
CC       from the lung and the bone marrow and is less abundant in the
CC       spleen. Isoform 2 is expressed in the spleen, lung, brain and bone
CC       marrow. Isoform 3 is expressed in the brain, is absent from the
CC       bone marrow and is less abundant in the spleen and lung.
CC   -!- INDUCTION: By lipopolysaccharide (LPS).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 BEACH domain.
CC   -!- SIMILARITY: Contains 6 WD repeats.
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DR   EMBL; AF187731; AAG14003.1; -; mRNA.
DR   EMBL; AF188506; AAG15400.1; -; mRNA.
DR   EMBL; AF188507; AAG15401.1; -; mRNA.
DR   IPI; IPI00227851; -.
DR   IPI; IPI00816903; -.
DR   IPI; IPI00816940; -.
DR   RefSeq; NP_001071155.1; NM_001077687.1.
DR   RefSeq; NP_001071156.1; NM_001077688.1.
DR   RefSeq; NP_109620.2; NM_030695.2.
DR   UniGene; Mm.439825; -.
DR   HSSP; P50851; 1T77.
DR   ProteinModelPortal; Q9ESE1; -.
DR   SMR; Q9ESE1; 2069-2482, 2592-2720, 2759-2789.
DR   STRING; Q9ESE1; -.
DR   PhosphoSite; Q9ESE1; -.
DR   PRIDE; Q9ESE1; -.
DR   Ensembl; ENSMUST00000082226; ENSMUSP00000080857; ENSMUSG00000028080.
DR   GeneID; 80877; -.
DR   KEGG; mmu:80877; -.
DR   CTD; 80877; -.
DR   MGI; MGI:1933162; Lrba.
DR   GeneTree; ENSGT00600000084267; -.
DR   OrthoDB; EOG4TXBQZ; -.
DR   ArrayExpress; Q9ESE1; -.
DR   Bgee; Q9ESE1; -.
DR   Genevestigator; Q9ESE1; -.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0016197; P:endosome transport; TAS:MGI.
DR   GO; GO:0007165; P:signal transduction; TAS:MGI.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000409; Beige_BEACH.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   InterPro; IPR010508; DUF1088.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 2.
DR   Gene3D; G3DSA:1.10.1540.10; Beige_BEACH; 1.
DR   Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 1.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF02138; Beach; 1.
DR   Pfam; PF06469; DUF1088; 1.
DR   Pfam; PF00400; WD40; 2.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF81837; Beige_BEACH; 1.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS50197; BEACH; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR   PROSITE; PS50294; WD_REPEATS_REGION; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Endoplasmic reticulum;
KW   Golgi apparatus; Lysosome; Membrane; Phosphoprotein; Repeat;
KW   Transmembrane; Transmembrane helix; WD repeat.
FT   CHAIN         1   2856       Lipopolysaccharide-responsive and beige-
FT                                like anchor protein.
FT                                /FTId=PRO_0000386545.
FT   TRANSMEM   1529   1545       Helical; (Potential).
FT   REPEAT     1298   1340       WD 1.
FT   DOMAIN     2193   2482       BEACH.
FT   REPEAT     2584   2626       WD 2.
FT   REPEAT     2629   2672       WD 3.
FT   REPEAT     2688   2728       WD 4.
FT   REPEAT     2770   2809       WD 5.
FT   REPEAT     2812   2851       WD 6.
FT   COMPBIAS   1994   1998       Poly-Arg.
FT   MOD_RES      10     10       Phosphoserine (By similarity).
FT   MOD_RES     904    904       Phosphotyrosine.
FT   MOD_RES     979    979       Phosphoserine.
FT   MOD_RES    1005   1005       Phosphoserine.
FT   MOD_RES    1670   1670       Phosphothreonine (By similarity).
FT   VAR_SEQ    2569   2579       ACGTGTHRRQV -> GLPLLSLFAIH (in isoform
FT                                3).
FT                                /FTId=VSP_038227.
FT   VAR_SEQ    2580   2856       Missing (in isoform 3).
FT                                /FTId=VSP_038228.
FT   VAR_SEQ    2777   2792       AIQLSRDGQYLLTGGD -> VSAVGSTLFLLLGSSK (in
FT                                isoform 2).
FT                                /FTId=VSP_038229.
FT   VAR_SEQ    2793   2856       Missing (in isoform 2).
FT                                /FTId=VSP_038230.
SQ   SEQUENCE   2856 AA;  317064 MW;  6E7C5DD865384BEA CRC64;
     MASEDNRAPS RPPTGDDGGG GGKEETPTEG GALSLKPGLP IRGIRMKFAV LTGLVEVGEV
     SNRDIVETVF NLLVGGQFDL EMNFIIQEGE SIMCMVELLE KCDVTCQAEV WSMFTAILKK
     SIRNLQVCTE VGLVEKVLGK IEKVDSMIAD LLVDMLGVLA SYNLTVRELK LFFSKLQGDK
     GQWPPHAGKL LSVLKHMPQK YGPDAFFNFP GKSAAAIALP PIARWPYQNG FTFHTWLRMD
     PVNNINVDKD KPYLYCFRTS KGLGYSAHFV GGCLIITSIK SKGKGFQHCV KFDFKPQKWY
     MVTIVHIYNR WKNSELRCYV NGELASYGEI TWFVNTSDTF DKCFLGSSET ADANRVFCGQ
     MTAVYLFSDA LNAAQIFAIY QLGLGYKGTF KFKAESDLFL AEHHKLLLYD GKLSSAIAFM
     YNPRATDAQL CLESSPKDNP SIFVHSPHAL MLQDVKAVLT HSIQSAMHSI GGVQVLFPLF
     AQLDYKQYLS DEVDLTICTT LLAFIMELLK NSIAMQEQML ACKGFLVIGY SLEKSSKSHV
     SRAVLELCLA FSKYLSNLQN GMPLLKQLCD HILLNPAVWI HTPAKVQLML YTYLSTEFIG
     TVNIYNTIRR VGTVLLIMHT LKYYYWAVNP QDRSGITPKG LDGPRPNQKE ILSLRAFLLM
     FIKQLVMKDS GVKEDELQAI LNYLLTMHED DNLMDVLQLL VALMAEHPNS MIPAFDQRNG
     LRVIYKLLAS KSEGIRVQAL KALGYFLKHL APKRKAEVML GHGLFSLLAE RLMLQTNLIT
     MTMYNVLFEI LIEQICTQVI HKQHPDPDST VKIQNPQILK VIATLLRNSP QCPESMEVRR
     AFLSDMIKLF NNSRENRRSL LQCSVWQEWM LSLCYFNPKN SDEQKITEMV YAIFRILLYH
     AVKYEWGGWR VWVDTLSITH SKVTFEIHKE NLANIFREEQ RKGDEETGPC SSSLVPEGTG
     ATRGVDVSVG SQHEDRKDSP ISPHFTRNSD ENSSIGRASS IDSASNTELQ THDMSSDEKK
     VERENQELLD QATVEETATN GAKDDLETSS DAAEPVTINS NSLEPGKDTV TISEVSASIS
     SPSEEDAAEM PELLEKSGVE EKEDDDYVEL KVEGSPTEEA GLPTELQGEG LSVAASGGRE
     EPDMCGHGCE VQVEAPITKI HNDPETTDSE DSRFPTVATA GSLATSSEVP VPQATVQSDS
     HEMLDGGMKA TNLAGETESV SDCADNVSEA PATSEQKITK LDVSSVASDT ERFELKASTS
     TEAPQPQRHG LEISRQQEQT AQGTAPDAVD QQRRDSRSTM FRIPEFKWSQ MHQRLLTDLL
     FSIETDIQMW RSHSTKTVMD FVNSSDNVIF VHNTIHLISQ VMDNMVMACG GILPLLSAAT
     SATHELENIE PTQGLSIEAS VTFLQRLISL VDVLIFASSL GFTEIEAEKN MSSGGILRQC
     LRLVCAVAVR NCLECQQHSQ LKARGDTAKS SKTIHSLIPM GKSAAKSPVD IVTGGISSVR
     DLDRLPARTW TLIGLRAVVF RDIEDSKQAQ FLALAVVYFI SVLMVSKYRD ILEPQDERHS
     QSLKETSSDN GNASLPDAEN TPAEFSSLTL SSVEESLEGT SCTRRRDSGL GEETASGLGS
     GLSVASPAAP LGVSAGPDAI SEVLCTLSLE VNKSQETRID GGNELDRKVT PSVPVSKNVN
     VKDILRSLVN MPADGVTVDP ALLPPACLGA LGDLSVDPPM QFRSFDRSVI IATKKSSVLP
     SALTTSAPSS AVSVVSSVDP THASDTGGES PGSRSPKCKT ALSCKQLAPS HKTPAAHMSI
     TERLEHALEK AAPLLREIFV DFAPFLSRTL LGSHGQELLI EGTSLVCMKS SSSVVELVML
     LCSQEWQNSI QKNAGLAFIE LVNEGRLLSQ TMKDHLVRVA NEAEFILSRQ RAEDIHRHAE
     FESLCAQYSA DKREEEKMCD HLIRAAKYRD HVTATQLIQK IINLLTDKHG AWGSSAVSRP
     REFWRLDYWE DDLRRRRRFV RNPLGSTHPE ATLKTAVEHA ADEDILAKGK QSIKSQALGN
     QNSENEALLE GDDDTLSSVD EKDLENLAGP VSLSTPAQLV APSVVVKGTL SVTSSELYFE
     VDEEDPNFKK IDPKILAYTE GLHGKWLFTE IRSIFSRRYL LQNTALEIFM ANRVAVMFNF
     PDPATVKKVV NYLPRVGVGT SFGLPQTRRI SLATPRQLFK ASNMTQRWQH REISNFEYLM
     FLNTIAGRSY NDLNQYPVFP WVITNYESEE LDLTLPSNFR DLSKPIGALN PKRAAFFAER
     FESWEDDQVP KFHYGTHYST ASFVLAWLLR IEPFTTYFLN LQGGKFDHAD RTFSSVSRAW
     RNSQRDTSDI KELIPEFYYL PEMFVNFNNY NLGVMDDGTV VSDVELPPWA KTSEEFVRIN
     RLALESEFVS CQLHQWIDLI FGYKQQGPEA VRALNVFYYL TYEGAVNLNS ITDPVLREAV
     EAQIRSFGQT PSQLLIEPHP PRGSAMQASP LMFTDQAQQD VIMVLKFPSN SPVTHVAANT
     QPGLAMPAVI TVTANRLFAV NKWHNLPAHQ GAVQDQPYQL PVEIDPLIAC GTGTHRRQVT
     DLLDQSIQVH SQCFVITSDN RYILVCGFWD KSFRVYSTDT GKLIQVVFGH WDVVTCLARS
     ESYIGGNCYI LSGSRDATLL LWYWNGKSSG IGDNPGGETA TPRAILTGHD YEITCAAVCA
     ELGLVLSGSQ EGPCLIHSMN GDLLRTLEGP ENCLKPKLIQ ASREGHCVIF YENGCFCTFS
     VNGKLQATVE TDDHIRAIQL SRDGQYLLTG GDNGVVIVRQ VSDLKQLFAY PGCDAGIRAM
     ALSFDQRCII SGMASGSIVL FYNDFNRWHH EYQTRY
//
ID   SPN90_MOUSE             Reviewed;         714 AA.
AC   Q9ESJ4; Q3UYF3; Q68G72;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=NCK-interacting protein with SH3 domain;
DE   AltName: Full=54 kDa VacA-interacting protein;
DE            Short=VIP54;
DE   AltName: Full=90 kDa N-WASP-interacting protein;
DE   AltName: Full=90 kDa SH3 protein interacting with Nck;
DE   AltName: Full=SH3 adapter protein SPIN90;
DE   AltName: Full=WASP-interacting SH3-domain protein;
DE            Short=WISH;
DE   AltName: Full=Wiskott-Aldrich syndrome protein-binding protein;
DE            Short=N-WASP-binding protein;
GN   Name=Nckipsd; Synonyms=Spin90, Wasbp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND POSSIBLE FUNCTION.
RC   TISSUE=Myoblast;
RX   PubMed=11157975; DOI=10.1083/jcb.152.3.471;
RA   Fukuoka M., Suetsugu S., Miki H., Fukami K., Endo T., Takenawa T.;
RT   "A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding
RT   protein, WISH, induces Arp2/3 complex activation independent of
RT   Cdc42.";
RL   J. Cell Biol. 152:471-482(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 216-646.
RX   MEDLINE=20086819; PubMed=10619843; DOI=10.1093/emboj/19.1.48;
RA   de Bernard M., Moschioni M., Napolitani G., Rappuoli R.,
RA   Montecucco C.;
RT   "The VacA toxin of Helicobacter pylori identifies a new intermediate
RT   filament-interacting protein.";
RL   EMBO J. 19:48-56(2000).
CC   -!- FUNCTION: Has an important role in stress fiber formation induced
CC       by active diaphanous protein homolog 1 (DRF1) (By similarity).
CC       Induces microspike formation, in vivo. In vitro, stimulates N-
CC       WASP-induced ARP2/3 complex activation in the absence of CDC42.
CC       May play an important role in the maintenance of sarcomere and/or
CC       in the assembly of myofibrils into sarcomeres. Implicated in
CC       regulation of actin polymerization and cell adhesion.
CC   -!- SUBUNIT: Associates with the intermediate filaments, vimentin and
CC       desmin (By similarity). Binds the first and third SH3 domains of
CC       NCK (By similarity). Binds the proline-rich domains of N-WASP
CC       through its SH3 domain. Similarly, binds diaphanous protein
CC       homolog 1 (DRF1) (By similarity). Binds the SH3 domains of GRB2
CC       through its proline-rich domains. Interacts with FASLG (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Note=Colocalizes
CC       with DRF1 at membrane ruffles, and with Nck at Z-disks in mature
CC       cardiac myocytes (By similarity).
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; AF130313; AAF36503.2; -; mRNA.
DR   EMBL; AK134725; BAE22259.1; -; mRNA.
DR   EMBL; CH466560; EDL21315.1; -; Genomic_DNA.
DR   EMBL; BC064818; AAH64818.1; -; mRNA.
DR   IPI; IPI00467223; -.
DR   RefSeq; NP_109654.2; NM_030729.4.
DR   UniGene; Mm.192416; -.
DR   ProteinModelPortal; Q9ESJ4; -.
DR   SMR; Q9ESJ4; 1-56.
DR   MINT; MINT-157148; -.
DR   PhosphoSite; Q9ESJ4; -.
DR   PRIDE; Q9ESJ4; -.
DR   Ensembl; ENSMUST00000035218; ENSMUSP00000035218; ENSMUSG00000032598.
DR   GeneID; 80987; -.
DR   KEGG; mmu:80987; -.
DR   UCSC; uc009rqz.1; mouse.
DR   CTD; 80987; -.
DR   MGI; MGI:1931834; Nckipsd.
DR   GeneTree; ENSGT00390000015725; -.
DR   HOGENOM; HBG314401; -.
DR   HOVERGEN; HBG061630; -.
DR   InParanoid; Q9ESJ4; -.
DR   OMA; CQMDRMI; -.
DR   OrthoDB; EOG4GMTWT; -.
DR   PhylomeDB; Q9ESJ4; -.
DR   NextBio; 350330; -.
DR   ArrayExpress; Q9ESJ4; -.
DR   Bgee; Q9ESJ4; -.
DR   CleanEx; MM_NCKIPSD; -.
DR   Genevestigator; Q9ESJ4; -.
DR   GermOnline; ENSMUSG00000032598; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   InterPro; IPR018556; DUF2013.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF09431; DUF2013; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   2: Evidence at transcript level;
KW   Nucleus; Phosphoprotein; SH3 domain; SH3-binding.
FT   CHAIN         1    714       NCK-interacting protein with SH3 domain.
FT                                /FTId=PRO_0000072131.
FT   DOMAIN        1     58       SH3.
FT   MOTIF       168    185       Nuclear localization signal (Potential).
FT   COMPBIAS    200    233       Ser-rich.
FT   COMPBIAS    225    264       Pro-rich.
FT   COMPBIAS    434    479       Leu-rich.
FT   COMPBIAS    526    593       Leu-rich.
FT   MOD_RES     174    174       Phosphothreonine (By similarity).
SQ   SEQUENCE   714 AA;  78572 MW;  2111AB09799F4718 CRC64;
     MYRALYAFRS AEPNAMAFAA GETFLVLERS STHWWLAARA RSGETGYVPP AYLHRLQGME
     QDVLQAIDRA IEAVHNTAMR DGGKYSLEQR GVLQKLIHHR KETLSRRGTS ASSATVMTPS
     TSDHHLDAAV SRQPNGVCRT GFERQHSLPS SEHLGTDGAL YQVPPQPRRA APTTPPPPVK
     RRDREALVIS GSGGRTAIPS GGSSVSSGSS ASSTSMDTLY TGSSPSELGP SCSPTPPPVP
     RRGAHTTVSQ PQPSPSKAPS PEPPTEEVAA ETNSTPDDLE AQDALSPETT EEKAAAETVV
     PRTIGAELME LVRRNTGLSH ELCRVAIGVV VGHIQATVPA SSPIMEQVLL SLVEGKDLST
     ALPSGQVCHD QQRLEVIFAD LARRKDDAQQ RSWALYEDED VIRCYLEELL HILTDADPEV
     CKKMCKRSDF ESVLALVAYY QMEHRASLRL LLLKCFGAMC SLDAAIISTL VSSVLPVELA
     RDMQTDTQDH QKLCYSALVL AMVFSMGEAV PYAHYEHLGT PFAQFLLSIV EDGLPMDTTE
     QLPDLCMNLL LALNLHLTAP EQNVIMAALS RHTNVKIFSE KLLLLLNRGD DPVRIFRHEP
     QPPHSVLKFL QDVFSSSATA AIFYHTDMMA LIDITVRQIA DLSPGDKLRM EYLSLMHAVV
     RSTPYLQHRH RLSDLQATLR RILTEEEASP QCQMDRMIVQ EMYKEFPDLG EVPS
//
ID   RBCC1_MOUSE             Reviewed;        1588 AA.
AC   Q9ESK9; Q3TXX2; Q61384; Q8BRY9; Q9JK14;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 2.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=RB1-inducible coiled-coil protein 1;
DE   AltName: Full=Coiled-coil-forming protein 1;
DE   AltName: Full=LaXp180;
GN   Name=Rb1cc1; Synonyms=Cc1, Kiaa0203;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP   CO-LOCALIZATION WITH RB1, AND FUNCTION.
RC   STRAIN=C57BL/6; TISSUE=Skeletal muscle;
RX   MEDLINE=22090535; PubMed=12095676; DOI=10.1016/S0378-1119(02)00585-1;
RA   Chano T., Ikegawa S., Saito-Ohara F., Inazawa J., Mabuchi A.,
RA   Saeki Y., Okabe H.;
RT   "Isolation, characterization and mapping of the mouse and human RB1CC1
RT   genes.";
RL   Gene 291:29-34(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 589-1304 AND 1374-1588.
RC   STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1081-1222.
RX   MEDLINE=95241452; PubMed=7724523; DOI=10.1073/pnas.92.8.3100;
RA   Maucuer A., Camonis J.H., Sobel A.;
RT   "Stathmin interaction with a putative kinase and coiled-coil-forming
RT   protein domains.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:3100-3104(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1359-1588.
RC   STRAIN=CD-1;
RX   MEDLINE=21128561; PubMed=11207567;
RX   DOI=10.1046/j.1462-5822.2000.00034.x;
RA   Pfeuffer T., Goebel W., Laubinger J., Bachmann M., Kuhn M.;
RT   "LaXp180, a mammalian ActA-binding protein, identified with the yeast
RT   two-hybrid system co-localizes with intracellular Listeria
RT   monocytogenes.";
RL   Cell. Microbiol. 2:101-114(2000).
RN   [5]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=15375585;
RA   Bamba N., Chano T., Taga T., Ohta S., Takeuchi Y., Okabe H.;
RT   "Expression and regulation of RB1CC1 in developing murine and human
RT   tissues.";
RL   Int. J. Mol. Med. 14:583-587(2004).
RN   [6]
RP   FUNCTION.
RX   PubMed=15968549; DOI=10.1007/s00428-004-1183-1;
RA   Watanabe R., Chano T., Inoue H., Isono T., Koiwai O., Okabe H.;
RT   "Rb1cc1 is critical for myoblast differentiation through Rb1
RT   regulation.";
RL   Virchows Arch. 447:643-648(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-665, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [10]
RP   FUNCTION, INTERACTION WITH ULK1 AND ATG13, AND SUBCELLULAR LOCATION.
RX   PubMed=19258318; DOI=10.1074/jbc.M900573200;
RA   Ganley I.G., Lam du H., Wang J., Ding X., Chen S., Jiang X.;
RT   "ULK1.ATG13.FIP200 complex mediates mTOR signaling and is essential
RT   for autophagy.";
RL   J. Biol. Chem. 284:12297-12305(2009).
CC   -!- FUNCTION: Implicated in the regulation of RB1 expression.
CC       Functions as a DNA-binding transcription factor. Is a potent
CC       regulator of the RB1 pathway and a novel mediator that plays a
CC       crucial role in muscular differentiation. Expression is, thus, a
CC       prerequisite for myogenic differentiation. Could be also, a novel
CC       protein inhibitor for PTK2 (By similarity). Involved in autophagy.
CC       Required for autophagosome formation.
CC   -!- SUBUNIT: Part of a complex containing ATG13/KIAA0652, ULK1 and
CC       RB1CC1. This complex associates with ATG101 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol.
CC       Preautophagosomal structure. Note=Under starvation conditions, is
CC       localized to puncate structures primarily representing the
CC       isolation membrane that sequesters a portion of the cytoplasm
CC       resulting in the formation of an autophagosome.
CC   -!- TISSUE SPECIFICITY: Expressed abundantly in heart and testis, and
CC       moderately in kidney, liver and skeletal muscles. Very low
CC       expression levels in lung and spleen. Co-localizes with RB1 in
CC       various tissues.
CC   -!- DEVELOPMENTAL STAGE: Abundantly expressed from an early stage of
CC       the embryo throughout development. Ubiquitously expressed,
CC       especially in the musculoskeletal system, heart and neural
CC       tissues.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC30793.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AB050017; BAB16846.2; -; mRNA.
DR   EMBL; AB070619; BAB85610.1; -; mRNA.
DR   EMBL; AK041038; BAC30793.1; ALT_INIT; mRNA.
DR   EMBL; AK159066; BAE34792.1; -; mRNA.
DR   EMBL; X82318; CAA57761.1; -; mRNA.
DR   EMBL; AJ242720; CAB92238.1; -; mRNA.
DR   IPI; IPI00113372; -.
DR   PIR; I48282; I48282.
DR   RefSeq; NP_033956.2; NM_009826.4.
DR   UniGene; Mm.293811; -.
DR   ProteinModelPortal; Q9ESK9; -.
DR   SMR; Q9ESK9; 1-68.
DR   IntAct; Q9ESK9; 1.
DR   STRING; Q9ESK9; -.
DR   PhosphoSite; Q9ESK9; -.
DR   PRIDE; Q9ESK9; -.
DR   Ensembl; ENSMUST00000027040; ENSMUSP00000027040; ENSMUSG00000025907.
DR   GeneID; 12421; -.
DR   KEGG; mmu:12421; -.
DR   UCSC; uc007afr.1; mouse.
DR   CTD; 12421; -.
DR   MGI; MGI:1341850; Rb1cc1.
DR   eggNOG; roNOG09266; -.
DR   GeneTree; ENSGT00390000015871; -.
DR   HOGENOM; HBG447376; -.
DR   HOVERGEN; HBG091209; -.
DR   InParanoid; Q9ESK9; -.
DR   OrthoDB; EOG47D9F7; -.
DR   NextBio; 281224; -.
DR   ArrayExpress; Q9ESK9; -.
DR   Bgee; Q9ESK9; -.
DR   CleanEx; MM_RB1CC1; -.
DR   Genevestigator; Q9ESK9; -.
DR   GermOnline; ENSMUSG00000025907; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0000407; C:pre-autophagosomal structure; IDA:UniProtKB.
DR   GO; GO:0070969; C:ULK1-ATG13-FIP200 complex; IPI:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0000045; P:autophagic vacuole assembly; IMP:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0007254; P:JNK cascade; IGI:MGI.
DR   GO; GO:0001889; P:liver development; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptosis; IMP:MGI.
DR   GO; GO:0045793; P:positive regulation of cell size; IMP:MGI.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:MGI.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR019460; Autophagy-rel_p11.
DR   Pfam; PF10377; ATG11; 1.
PE   1: Evidence at protein level;
KW   Autophagy; Cell cycle; Coiled coil; Cytoplasm; Nucleus;
KW   Phosphoprotein; Transcription; Transcription regulation;
KW   Tumor suppressor.
FT   CHAIN         1   1588       RB1-inducible coiled-coil protein 1.
FT                                /FTId=PRO_0000097184.
FT   COILED      858   1393       Potential.
FT   COILED     1440   1479       Potential.
FT   MOTIF       565    568       Nuclear localization signal.
FT   COMPBIAS    662    665       Poly-Thr.
FT   MOD_RES     237    237       Phosphoserine.
FT   MOD_RES     243    243       Phosphoserine (By similarity).
FT   MOD_RES     257    257       Phosphoserine (By similarity).
FT   MOD_RES     261    261       Phosphoserine.
FT   MOD_RES     623    623       Phosphoserine (By similarity).
FT   MOD_RES     646    646       Phosphoserine (By similarity).
FT   MOD_RES     649    649       Phosphoserine (By similarity).
FT   MOD_RES     652    652       Phosphoserine (By similarity).
FT   MOD_RES     665    665       Phosphothreonine.
FT   CONFLICT    809    809       T -> S (in Ref. 2; BAC30793).
FT   CONFLICT    981    981       E -> Q (in Ref. 2; BAC30793).
FT   CONFLICT   1222   1222       D -> A (in Ref. 3; CAA57761).
FT   CONFLICT   1450   1451       KQ -> NE (in Ref. 4; CAB92238).
FT   CONFLICT   1537   1539       Missing (in Ref. 4; CAB92238).
SQ   SEQUENCE   1588 AA;  182365 MW;  591B01C0C4B1ADF7 CRC64;
     MKLYVFLVNT GTTLTFDTEL TVQTVADLKH AIQSKYKIAI QHQVLVVNGG ECMAADRRVC
     TYSAGTDTNP IFLFNKEMIL CDRAPAIPKA TFSTENDMEI KVEESLMMPA VFHTVASRTQ
     LAVEMYDVAK KLCSFCEGLV HDEHLQHQGW AAIMANLEDC SNSYQKLLFK FESIYSDYLQ
     SIEDIKLKLT HLGTAVSVMA KIPLLECLTR HSYRECLGRP DSLNEHEGSE KAEMKRSTEL
     VLSPDMPRTT NTSLVTSFHK SMEHVAPDPT GTERGKELRE SCQSTVQQEE ASVDAKDSDL
     PFFNVSLLDW INVQDRPNDV ESLVRKCFDS MSRLDPKIIQ PFMLECHQTI AKLDNQNMKA
     IKGLEDRLYA LDQMIASCSR LVNEQKELAQ GFLANQMRAE NLKDASVLPD LCLSHANQLM
     IMLQNHRKLL DIKQKCTTAK QELANNLHVR LKWCCFVMLH ADQDGEKLQA LLRLVIELLE
     RVRIVEALST VPQMYCLAVV EVVRRKMFIK HYREWAGALV KDGKQLYEAE KSKRESFGKL
     FRKSFLRNRL FKGLDSWPSS FCTQKPRKFD CELPDISLKD LQFLQSFCPS EVQPFLRVPL
     LCDFEPLHQH VLALHNLVKA AQSLDEMSQT ITDLLNEQKV STSQASPQSA ASPRIESTTG
     ITTTTSPKTP PPLTVQDTLC PAVCPLEELS PDSIDAHTFD FETISHPNTE QPVHQASIDL
     DSLAESPESD FMSAVNEFVI EENLSSPNPI SDPQSPEMMV ESLYSSVINA IDSRRMQDTS
     TRGNEGFGDR AALHVQLEKC RAAAQDSHTS IQTIKDDLCH FRTFVQKEQC DLANYLKCTA
     VEIRNIIEKV KCSLEITLKE KHQQELQSLK IEYECKLDAL VKDSEENVNK ILKLKENLVS
     LEEALQNKDN EFTSIKHEKD AIVCVQQEKD QKLLEMEKIM HTQHCEIKEL KQSREMALED
     LKKLHDEKIE SLRAEFQCLE ENHLKELEDT LHIRHTQEFE KVMTDHNMSL EKLKKENQQR
     IDQMLESHAS TIQEKEQQLQ ELKLKVSDLS DMRCKLEVEL ALKEAETDEI KILLEESRTQ
     QKEMLKSLLE QETENLRTEI SKLNQKIHDN NESYQVGLSE LRALMTIEKD QCISELISRH
     EEESNILKAE LDNVTSLHRQ AYEIEKKLKE QIVELQTRLN SELSALEKQK DEKITQQEEK
     YEALIQNLEK DKERLVKNHE QDKEHLIQEL NFEKNKAVQT ALDEFKVERE LVEKELLEKV
     KHLENQIAKT PAFESAREDS SSLVAELQEK LQEEKAKFLE QLEEQEKRKN EEMQNVRTSL
     IAEQQTNFNT VLTREKMRKE NIINDLSDKL KSTMQQQERD KDLIESLSED RARLLEEKKQ
     LEEEVSKLRT SSFLSSAPVA AAPELYGACA PELPGEPERS VMETADEGRL DSAMETSMMS
     VQENMLSEEK QRIMLLERTL QLKEEENKRL NQRLMSQSLS SVSSRHSEKI AIRDFQVGDL
     VLIILDERHD NYVLFTVSPT LYFLHSESLP ALDLKPGEGA SGASRRPWVL GKVMEKEYCQ
     AKKAQNRFKV PLGTKFYRVK AVSWNKKV
//
ID   TRIM2_MOUSE             Reviewed;         744 AA.
AC   Q9ESN6; Q3UHP5; Q8C981;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Tripartite motif-containing protein 2;
DE   AltName: Full=Neural activity-related RING finger protein;
GN   Name=Trim2; Synonyms=Narf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=ICR; TISSUE=Hippocampus;
RX   MEDLINE=21326316; PubMed=11432975;
RX   DOI=10.1046/j.1471-4159.2001.00373.x;
RA   Ohkawa N., Kokura K., Matsu-ura T., Obinata T., Konishi Y.,
RA   Tamura T.-A.;
RT   "Molecular cloning and characterization of neural activity-related
RT   RING finger protein (NARF): a new member of the RBCC family is a
RT   candidate for the partner of myosin V.";
RL   J. Neurochem. 78:75-87(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=21231161; PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA   Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA   Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A.,
RA   Minucci S., Pelicci P.G., Ballabio A.;
RT   "The tripartite motif family identifies cell compartments.";
RL   EMBO J. 20:2140-2151(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone, Cerebellum, Corpora quadrigemina, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May contribute to the alteration of neural cellular
CC       mechanisms.
CC   -!- SUBUNIT: Interacts with myosin V.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in the brain,
CC       especially in the hippocampus.
CC   -!- DOMAIN: The interaction with myosin V is dependent upon its NHL
CC       repeats, which form a beta-propeller (NHL) domain containing six
CC       blades.
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC   -!- SIMILARITY: Contains 1 B box-type zinc finger.
CC   -!- SIMILARITY: Contains 1 filamin repeat.
CC   -!- SIMILARITY: Contains 6 NHL repeats.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
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DR   EMBL; AB043550; BAB17634.1; -; mRNA.
DR   EMBL; AF220017; AAG53471.1; -; mRNA.
DR   EMBL; AK042752; BAC31352.1; -; mRNA.
DR   EMBL; AK045410; BAC32350.1; -; mRNA.
DR   EMBL; AK079415; BAC37640.1; -; mRNA.
DR   EMBL; AK147275; BAE27812.1; -; mRNA.
DR   EMBL; BC058961; AAH58961.1; -; mRNA.
DR   IPI; IPI00113430; -.
DR   RefSeq; NP_109631.1; NM_030706.2.
DR   UniGene; Mm.44876; -.
DR   UniGene; Mm.474162; -.
DR   ProteinModelPortal; Q9ESN6; -.
DR   SMR; Q9ESN6; 19-75, 466-744.
DR   DIP; DIP-46254N; -.
DR   STRING; Q9ESN6; -.
DR   PhosphoSite; Q9ESN6; -.
DR   PRIDE; Q9ESN6; -.
DR   Ensembl; ENSMUST00000054990; ENSMUSP00000049902; ENSMUSG00000027993.
DR   Ensembl; ENSMUST00000065380; ENSMUSP00000069922; ENSMUSG00000027993.
DR   Ensembl; ENSMUST00000107691; ENSMUSP00000103319; ENSMUSG00000027993.
DR   Ensembl; ENSMUST00000107692; ENSMUSP00000103320; ENSMUSG00000027993.
DR   Ensembl; ENSMUST00000107693; ENSMUSP00000103321; ENSMUSG00000027993.
DR   Ensembl; ENSMUST00000107694; ENSMUSP00000103322; ENSMUSG00000027993.
DR   Ensembl; ENSMUST00000107695; ENSMUSP00000103323; ENSMUSG00000027993.
DR   GeneID; 80890; -.
DR   KEGG; mmu:80890; -.
DR   UCSC; uc008ppw.1; mouse.
DR   CTD; 80890; -.
DR   MGI; MGI:1933163; Trim2.
DR   GeneTree; ENSGT00550000074377; -.
DR   HOVERGEN; HBG054843; -.
DR   InParanoid; Q9ESN6; -.
DR   OrthoDB; EOG46T30V; -.
DR   PhylomeDB; Q9ESN6; -.
DR   NextBio; 350219; -.
DR   ArrayExpress; Q9ESN6; -.
DR   Bgee; Q9ESN6; -.
DR   CleanEx; MM_NARF; -.
DR   CleanEx; MM_TRIM2; -.
DR   Genevestigator; Q9ESN6; -.
DR   GermOnline; ENSMUSG00000027993; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR   GO; GO:0017022; F:myosin binding; NAS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR001298; Filamin.
DR   InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR001258; NHL_repeat.
DR   InterPro; IPR013017; NHL_repeat_subgr.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Gene3D; G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00630; Filamin; 1.
DR   Pfam; PF01436; NHL; 6.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00557; IG_FLMN; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF81296; Ig_E-set; 1.
DR   PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR   PROSITE; PS51125; NHL; 6.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Metal-binding; Phosphoprotein; Repeat; Zinc; Zinc-finger.
FT   CHAIN         1    744       Tripartite motif-containing protein 2.
FT                                /FTId=PRO_0000056196.
FT   REPEAT      320    421       Filamin.
FT   REPEAT      473    516       NHL 1.
FT   REPEAT      520    563       NHL 2.
FT   REPEAT      564    605       NHL 3.
FT   REPEAT      609    652       NHL 4.
FT   REPEAT      656    699       NHL 5.
FT   REPEAT      700    743       NHL 6.
FT   ZN_FING      23     64       RING-type.
FT   ZN_FING     113    154       B box-type.
FT   MOD_RES     440    440       Phosphoserine.
SQ   SEQUENCE   744 AA;  81445 MW;  80336DA2EFEE5EFD CRC64;
     MASEGASIPS PVVRQIDKQF LICSICLERY KNPKVLPCLH TFCERCLQNY IPAHSLTLSC
     PVCRQTSILP EKGVAALQNN FFITNLMDVL QRTPGSNGED SSILETVTAV AAGKPLSCPN
     HDGNVMEFYC QSCETAMCRE CTEGEHAEHP TVPLKDVVEQ HKASLQVQLD AVNKRLPEID
     SALQFISEII HQLTNQKASI VDDIHSTFDE LQKTLNVRKS VLLMELEVNY GLKHKVLQSQ
     LDTLLQGQES IKSCSNFTAQ ALNHGTETEV LLVKKQMSEK LNELADQDFP LHPRENDQLD
     FIVETEGLKK SIHNLGTILT TNAVASETVA TGEGLRQTII GQPMSVTITT KDKDGELCKT
     GNAYLTAELS TPDGSVADGE ILDNKNGTYE FLYTVQKEGD FTLSLRLYDQ HIRGSPFKLK
     VIRSADVSPT TEGVKRRVKS PGSGHVKQKA VKRPASMYST GKRKENPIED DLIFRVGTKG
     RNKGEFTNLQ GVAASTSGKI LIADSNNQCV QIFSNDGQFK SRFGIRGRSP GQLQRPTGVA
     VHPSGDIIIA DYDNKWVSIF SNDGKFKTKI GSGKLMGPKG VSVDRNGHII VVDNKACCVF
     IFQPNGKIVT RFGSRGNGDR QFAGPHFAAV NSNNEIIITD FHNHSVKVFN QEGEFMLKFG
     SNGEGNGQFN APTGVAVDSN GNIIVADWGN SRIQVFDGSG SFLSYINTSA DPLYGPQGLA
     LTSDGHVVVA DSGNHCFKVY RYLQ
//
ID   JIP3_MOUSE              Reviewed;        1337 AA.
AC   Q9ESN9; Q5D062; Q99KU7; Q9EQD8; Q9ESN7; Q9ESN8; Q9ESP0; Q9JLH2;
AC   Q9JLH3; Q9R0U7;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=C-Jun-amino-terminal kinase-interacting protein 3;
DE            Short=JIP-3;
DE            Short=JNK-interacting protein 3;
DE   AltName: Full=JNK MAP kinase scaffold protein 3;
DE   AltName: Full=JNK/SAPK-associated protein 1;
DE            Short=JSAP1;
DE   AltName: Full=Mitogen-activated protein kinase 8-interacting protein 3;
DE   AltName: Full=Sunday driver 2;
GN   Name=Mapk8ip3; Synonyms=Jip3, Jsap1, Syd2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A), FUNCTION, PHOSPHORYLATION,
RP   AND INTERACTION WITH MAPK8; MAPK9; MAPK10; MAP2K4 AND MAP3K1.
RC   TISSUE=Brain;
RX   MEDLINE=99455010; PubMed=10523642;
RA   Ito M., Yoshioka K., Akechi M., Yamashita S., Takamatsu N.,
RA   Sugiyama K., Hibi M., Nakabeppu Y., Shiba T., Yamamoto K.;
RT   "JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein
RT   that functions as a scaffold factor in the JNK signaling pathway.";
RL   Mol. Cell. Biol. 19:7539-7548(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1A; 1B; 1C; 1D AND 1E),
RP   AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=20480689; PubMed=11024282; DOI=10.1016/S0378-1119(00)00335-8;
RA   Ito M., Akechi M., Hirose R., Ichimura M., Takamatsu N., Xu P.,
RA   Nakabeppu Y., Tadayoshi S., Yamamoto K., Yoshioka K.;
RT   "Isoforms of JSAP1 scaffold protein generated through alternative
RT   splicing.";
RL   Gene 255:229-234(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE (ISOFORMS 1C AND 3A), FUNCTION, INDUCTION, TISSUE
RP   SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-266; THR-276
RP   AND THR-287, MUTAGENESIS OF ARG-205; PRO-206; THR-207; SER-208;
RP   LEU-209; THR-266; THR-276 AND THR-287, AND INTERACTION WITH MAPK8IP2;
RP   MAPK8; MAPK9; MAPK10; MAP2K7 AND MAP3K11.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Heart;
RX   MEDLINE=20094982; PubMed=10629060;
RX   DOI=10.1128/MCB.20.3.1030-1043.2000;
RA   Kelkar N., Gupta S., Dickens M., Davis R.J.;
RT   "Interaction of a mitogen-activated protein kinase signaling module
RT   with the neuronal protein JIP3.";
RL   Mol. Cell. Biol. 20:1030-1043(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1C), SUBCELLULAR LOCATION, AND
RP   INTERACTION WITH KLC1.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=20560743; PubMed=11106729; DOI=10.1016/S0092-8674(00)00162-8;
RA   Bowman A.B., Kamal A., Ritchings B.W., Philp A.V., McGrail M.,
RA   Gindhart J.G., Goldstein L.S.B.;
RT   "Kinesin-dependent axonal transport is mediated by the Sunday Driver
RT   (SYD) protein.";
RL   Cell 103:583-594(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1B), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1240-1337 (ISOFORM 1C).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   INTERACTION WITH KLC.
RC   TISSUE=Brain;
RX   MEDLINE=21135887; PubMed=11238452; DOI=10.1083/jcb.152.5.959;
RA   Verhey K.J., Meyer D., Deehan R., Blenis J., Schnapp B.J.,
RA   Rapoport T.A., Margolis B.;
RT   "Cargo of kinesin identified as JIP scaffolding proteins and
RT   associated signaling molecules.";
RL   J. Cell Biol. 152:959-970(2001).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: The JNK-interacting protein (JIP) group of scaffold
CC       proteins selectively mediates JNK signaling by aggregating
CC       specific components of the MAPK cascade to form a functional JNK
CC       signaling module. May function as a regulator of vesicle
CC       transport, through interations with the JNK-signaling components
CC       and motor proteins.
CC   -!- SUBUNIT: Forms homo- or heterooligomeric complexes. The central
CC       region of MAPK8IP3 interacts with the C-terminal of MAPK8IP2 but
CC       not MAPK8IP1. Binds specific components of the JNK signaling
CC       pathway namely MAPK8, MAPK9 and MAPK10 to the N-terminal region,
CC       MAP2K4 and MAP2K7 to the central region and MAP3K11 to the C-
CC       terminal region. Binds the TPR motif-containing C-terminal of
CC       kinesin light chain, pre-assembled MAPK8IP1 scaffolding complexes
CC       are then transported as a cargo of kinesin, to the required
CC       subcellular location.
CC   -!- INTERACTION:
CC       O88447:Klc1; NbExp=2; IntAct=EBI-301496, EBI-301550;
CC       O88448:Klc2; NbExp=2; IntAct=EBI-301496, EBI-301558;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus. Cytoplasmic
CC       vesicle. Cell projection, growth cone. Note=Localized in the soma
CC       and growth cones of differentiated neurites and the Golgi and
CC       vesicles of the early secretory compartment of epithelial cells.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1c; Synonyms=3b;
CC         IsoId=Q9ESN9-1; Sequence=Displayed;
CC       Name=1a;
CC         IsoId=Q9ESN9-2; Sequence=VSP_002775, VSP_002777;
CC       Name=1b;
CC         IsoId=Q9ESN9-3; Sequence=VSP_002776, VSP_002777;
CC       Name=1d;
CC         IsoId=Q9ESN9-4; Sequence=VSP_002775;
CC       Name=3a;
CC         IsoId=Q9ESN9-5; Sequence=VSP_002778, VSP_002779;
CC       Name=1e;
CC         IsoId=Q9ESN9-6; Sequence=VSP_002776;
CC   -!- TISSUE SPECIFICITY: Highly expressed throughout many regions of
CC       the brain and at lower levels in the heart, liver, lung, testes
CC       and kidney. All isoforms have been identified in the brain,
CC       isoform 1a is also expressed in the spleen and lung.
CC   -!- INDUCTION: Expressed in neurites 5 days following initiation of
CC       nerve growth factor induced differentiation. NGF withdrawal
CC       results in the down-regulation of MAPK8IP3 protein by caspase-
CC       mediated cleavage.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the JIP scaffold family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG36931.1; Type=Erroneous initiation;
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DR   EMBL; AB005662; BAA85874.1; -; mRNA.
DR   EMBL; AB043124; BAB16675.1; -; mRNA.
DR   EMBL; AB043125; BAB16676.1; -; mRNA.
DR   EMBL; AB043123; BAB16674.1; -; mRNA.
DR   EMBL; AB043129; BAB16685.1; -; Genomic_DNA.
DR   EMBL; AF178637; AAF26843.1; -; mRNA.
DR   EMBL; AF178636; AAF26842.1; -; mRNA.
DR   EMBL; AF262046; AAG36931.1; ALT_INIT; mRNA.
DR   EMBL; BC004003; AAH04003.1; -; mRNA.
DR   EMBL; BC060603; AAH60603.1; -; mRNA.
DR   IPI; IPI00230497; -.
DR   IPI; IPI00230498; -.
DR   IPI; IPI00230499; -.
DR   IPI; IPI00230500; -.
DR   IPI; IPI00230501; -.
DR   IPI; IPI00751423; -.
DR   RefSeq; NP_001156919.1; NM_001163447.1.
DR   RefSeq; NP_001156920.1; NM_001163448.1.
DR   RefSeq; NP_001156921.1; NM_001163449.1.
DR   RefSeq; NP_001156923.1; NM_001163451.1.
DR   RefSeq; NP_038959.2; NM_013931.4.
DR   UniGene; Mm.43081; -.
DR   UniGene; Mm.479986; -.
DR   UniGene; Mm.480937; -.
DR   ProteinModelPortal; Q9ESN9; -.
DR   SMR; Q9ESN9; 417-476, 1066-1115.
DR   IntAct; Q9ESN9; 8.
DR   STRING; Q9ESN9; -.
DR   PhosphoSite; Q9ESN9; -.
DR   PRIDE; Q9ESN9; -.
DR   Ensembl; ENSMUST00000088345; ENSMUSP00000085683; ENSMUSG00000024163.
DR   Ensembl; ENSMUST00000115228; ENSMUSP00000110883; ENSMUSG00000024163.
DR   Ensembl; ENSMUST00000115229; ENSMUSP00000110884; ENSMUSG00000024163.
DR   GeneID; 30957; -.
DR   KEGG; mmu:30957; -.
DR   UCSC; uc008azc.1; mouse.
DR   UCSC; uc008aze.1; mouse.
DR   UCSC; uc008azf.1; mouse.
DR   CTD; 30957; -.
DR   MGI; MGI:1353598; Mapk8ip3.
DR   GeneTree; ENSGT00600000084097; -.
DR   HOVERGEN; HBG024110; -.
DR   OMA; WLYVHSA; -.
DR   NextBio; 307444; -.
DR   ArrayExpress; Q9ESN9; -.
DR   Bgee; Q9ESN9; -.
DR   Genevestigator; Q9ESN9; -.
DR   GermOnline; ENSMUSG00000024163; Mus musculus.
DR   GO; GO:0030673; C:axolemma; IDA:MGI.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR   GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR   GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0005625; C:soluble fraction; IDA:MGI.
DR   GO; GO:0019894; F:kinesin binding; IPI:UniProtKB.
DR   GO; GO:0005078; F:MAP-kinase scaffold activity; IPI:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0007257; P:activation of JUN kinase activity; IDA:MGI.
DR   GO; GO:0007411; P:axon guidance; IMP:MGI.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0048286; P:lung alveolus development; IMP:MGI.
DR   GO; GO:0060425; P:lung morphogenesis; IMP:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0008104; P:protein localization; IMP:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
DR   GO; GO:0007585; P:respiratory gaseous exchange; IMP:MGI.
DR   GO; GO:0016192; P:vesicle-mediated transport; IDA:UniProtKB.
DR   InterPro; IPR019143; JNK/Rab-associated_protein-1_N.
DR   InterPro; IPR011047; Quino_AlcDH-like.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF09744; Jnk-SapK_ap_N; 1.
DR   SUPFAM; SSF50998; Quin_alc_DH_like; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW   Cytoplasmic vesicle; Golgi apparatus; Phosphoprotein.
FT   CHAIN         1   1337       C-Jun-amino-terminal kinase-interacting
FT                                protein 3.
FT                                /FTId=PRO_0000220634.
FT   COILED       58    177       Potential.
FT   COILED      437    555       Potential.
FT   MOD_RES     266    266       Phosphothreonine; by MAPK.
FT   MOD_RES     268    268       Phosphoserine (By similarity).
FT   MOD_RES     276    276       Phosphothreonine; by MAPK.
FT   MOD_RES     287    287       Phosphothreonine; by MAPK.
FT   MOD_RES     366    366       Phosphoserine.
FT   MOD_RES     586    586       Phosphoserine (By similarity).
FT   MOD_RES     677    677       Phosphoserine.
FT   VAR_SEQ     201    201       Missing (in isoform 1a and isoform 1d).
FT                                /FTId=VSP_002775.
FT   VAR_SEQ     201    201       S -> SPRQSWRKS (in isoform 1b and isoform
FT                                1e).
FT                                /FTId=VSP_002776.
FT   VAR_SEQ     219    249       Missing (in isoform 1a and isoform 1b).
FT                                /FTId=VSP_002777.
FT   VAR_SEQ     410    415       Missing (in isoform 3a).
FT                                /FTId=VSP_002778.
FT   VAR_SEQ     505    513       Missing (in isoform 3a).
FT                                /FTId=VSP_002779.
FT   MUTAGEN     205    205       R->G: Results in inhibition of JNK
FT                                binding.
FT   MUTAGEN     206    206       P->G: Results in inhibition of JNK
FT                                binding.
FT   MUTAGEN     207    207       T->G: Results in inhibition of JNK
FT                                binding.
FT   MUTAGEN     208    208       S->G: Results in inhibition of JNK
FT                                binding.
FT   MUTAGEN     209    209       L->G: Results in inhibition of JNK
FT                                binding.
FT   MUTAGEN     266    266       T->A: Results in loss of phosphorylation
FT                                of MAPK8IP3; when associated with A-276
FT                                and A-287. Does not effect binding of
FT                                components of the JNK pathway.
FT   MUTAGEN     276    276       T->A: Results in loss of phosphorylation
FT                                of MAPK8IP3; when associated with A-266
FT                                and A-287. Does not effect binding of
FT                                components of the JNK pathway.
FT   MUTAGEN     287    287       T->A: Results in loss of phosphorylation
FT                                of MAPK8IP3; when associated with A-266
FT                                and A-287. Does not effect binding of
FT                                components of the JNK pathway.
FT   CONFLICT    312    312       K -> R (in Ref. 4; AAG36931).
FT   CONFLICT    376    376       F -> L (in Ref. 3; AAF26843).
FT   CONFLICT    561    561       E -> K (in Ref. 4; AAG36931).
FT   CONFLICT   1272   1272       A -> V (in Ref. 4; AAG36931).
FT   CONFLICT   1322   1322       A -> D (in Ref. 4; AAG36931).
FT   CONFLICT   1325   1325       S -> T (in Ref. 4; AAG36931).
SQ   SEQUENCE   1337 AA;  147561 MW;  D7DEE54C17B74106 CRC64;
     MMEIQMDEGG GVVVYQDDYC SGSVMSERVS GLAGSIYREF ERLIHCYDEE VVKELMPLVV
     NVLENLDSVL SENQEHEVEL ELLREDNEQL LTQYEREKAL RKQAEEKFIE FEDALEQEKK
     ELQIQVEHYE FQTRQLELKA KNYADQISRL EERESEMKKE YNALHQRHTE MIQTYVEHIE
     RSKMQQVGGS GQTESSLPGR SRKERPTSLN VFPLADGMVR AQMGGKLVPA GDHWHLSDLG
     QLQSSSSYQC PNDEMSESGQ SSAAATPSTT GTKSNTPTSS VPSAAVTPLN ESLQPLGDYV
     SVTKNNKQAR EKRNSRNMEV QVTQEMRNVS IGMGSSDEWS DVQDIIDSTP ELDVCPETRL
     ERTGSSPTQG IVNKAFGINT DSLYHELSTA GSEVIGDVDE GADLLGEFSV RDDFFGMGKE
     VGNLLLENSQ LLETKNALNV VKNDLIAKVD QLSGEQEVLK GELEAAKQAK VKLENRIKEL
     EEELKRVKSE AVTARREPRE EVEDVSSYLC TELDKIPMAQ RRRFTRVEMA RVLMERNQYK
     ERLMELQEAV RWTEMIRASR EHPSVQEKKK STIWQFFSRL FSSSSSPPPA KRSYPSVNIH
     YKSPTAAGFS QRRSHALCQI SAGSRPLEFF PDDDCTSSAR REQKREQYRQ VREHVRNDDG
     RLQACGWSLP AKYKQLSPNG GQEDTRMKNV PVPVYCRPLV EKDPSTKLWC AAGVNLSGWK
     PHEEDSSNGP KPVPGRDPLT CDREGEGEPK STHPSPEKKK AKETPEADAT SSRVWILTST
     LTTSKVVIID ANQPGTIVDQ FTVCNAHVLC ISSIPAASDS DYPPGEMFLD SDVNPEDSGA
     DGVLAGITLV GCATRCNVPR SNCSSRGDTP VLDKGQGDVA TTANGKVNPS QSTEEATEAT
     EVPDPGPSES EATTVRPGPL TEHVFTDPAP TPSSSTQPAS ENGSESNGTI VQPQVEPSGE
     LSTTTSSAAP TMWLGAQNGW LYVHSAVANW KKCLHSIKLK DSVLSLVHVK GRVLVALADG
     TLAIFHRGED GQWDLSNYHL MDLGHPHHSI RCMAVVNDRV WCGYKNKVHV IQPKTMQIEK
     SFDAHPRRES QVRQLAWIGD GVWVSIRLDS TLRLYHAHTH QHLQDVDIEP YVSKMLGTGK
     LGFSFVRITA LLIAGNRLWV GTGNGVVISI PLTETVVLHR GQLLGLRANK TSPTSGEGTR
     PGGIIHVYGD DSSDKAASSF IPYCSMAQAQ LCFHGHRDAV KFFVSVPGNV LATLNGSVLD
     SPSEGPGPAA PAADAEGQKL KNALVLSGGE GYIDFRIGDG EDDETEECAG DVNQTKPSLS
     KAERSHIIVW QVSYTPE
//
ID   BRD4_MOUSE              Reviewed;        1400 AA.
AC   Q9ESU6; Q8VHF7; Q8VHF8;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-FEB-2011, entry version 75.
DE   RecName: Full=Bromodomain-containing protein 4;
DE   AltName: Full=Mitotic chromosome-associated protein;
DE            Short=MCAP;
GN   Name=Brd4; Synonyms=Mcap;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP   FUNCTION.
RX   MEDLINE=20396330; PubMed=10938129;
RX   DOI=10.1128/MCB.20.17.6537-6549.2000;
RA   Dey A., Ellenberg J., Farina A., Coleman A.E., Maruyama T.,
RA   Sciortino S., Lippincott-Schwartz J., Ozato K.;
RT   "A bromodomain protein, MCAP, associates with mitotic chromosomes and
RT   affects G(2)-to-M transition.";
RL   Mol. Cell. Biol. 20:6537-6549(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX   MEDLINE=21993140; PubMed=11997514;
RX   DOI=10.1128/MCB.22.11.3794-3802.2002;
RA   Houzelstein D., Bullock S.L., Lynch D.E., Grigorieva E.F.,
RA   Wilson V.A., Beddington R.S.P.;
RT   "Growth and early postimplantation defects in mice deficient for the
RT   bromodomain-containing protein Brd4.";
RL   Mol. Cell. Biol. 22:3794-3802(2002).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-599; SER-602 AND
RP   SER-1048, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 347-460.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Crystal structure of bromodomain-containing protein 4.";
RL   Submitted (AUG-2007) to the PDB data bank.
CC   -!- FUNCTION: Plays a role in a process governing chromosomal dynamics
CC       during mitosis.
CC   -!- SUBUNIT: Associated with chromosomes during mitosis.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Long;
CC         IsoId=Q9ESU6-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short;
CC         IsoId=Q9ESU6-2; Sequence=VSP_010904, VSP_010905;
CC   -!- SIMILARITY: Contains 2 bromo domains.
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DR   EMBL; AF273217; AAG02191.1; -; mRNA.
DR   EMBL; AF461395; AAL67833.1; -; mRNA.
DR   EMBL; AF461396; AAL67834.1; -; mRNA.
DR   IPI; IPI00652110; -.
DR   IPI; IPI00885355; -.
DR   RefSeq; NP_065254.3; NM_020508.3.
DR   RefSeq; NP_932762.2; NM_198094.2.
DR   UniGene; Mm.253518; -.
DR   PDB; 2DWW; X-ray; 1.80 A; A=347-460.
DR   PDB; 2JNS; NMR; -; A=601-683.
DR   PDB; 3JVJ; X-ray; 1.55 A; A=42-168.
DR   PDB; 3JVK; X-ray; 1.80 A; A=42-168.
DR   PDB; 3JVL; X-ray; 1.20 A; A=349-464.
DR   PDB; 3JVM; X-ray; 1.20 A; A=349-464.
DR   PDB; 3MUK; X-ray; 1.75 A; A=42-168.
DR   PDB; 3MUL; X-ray; 1.65 A; A=42-168.
DR   PDB; 3MXF; X-ray; 1.60 A; A=44-168.
DR   PDBsum; 2DWW; -.
DR   PDBsum; 2JNS; -.
DR   PDBsum; 3JVJ; -.
DR   PDBsum; 3JVK; -.
DR   PDBsum; 3JVL; -.
DR   PDBsum; 3JVM; -.
DR   PDBsum; 3MUK; -.
DR   PDBsum; 3MUL; -.
DR   PDBsum; 3MXF; -.
DR   ProteinModelPortal; Q9ESU6; -.
DR   SMR; Q9ESU6; 42-168, 349-460, 606-683.
DR   MINT; MINT-1176459; -.
DR   STRING; Q9ESU6; -.
DR   PhosphoSite; Q9ESU6; -.
DR   PRIDE; Q9ESU6; -.
DR   Ensembl; ENSMUST00000114475; ENSMUSP00000110119; ENSMUSG00000024002.
DR   Ensembl; ENSMUST00000119123; ENSMUSP00000113197; ENSMUSG00000024002.
DR   Ensembl; ENSMUST00000121285; ENSMUSP00000113070; ENSMUSG00000024002.
DR   GeneID; 57261; -.
DR   KEGG; mmu:57261; -.
DR   UCSC; uc008bwa.1; mouse.
DR   UCSC; uc008bwc.1; mouse.
DR   CTD; 57261; -.
DR   MGI; MGI:1888520; Brd4.
DR   GeneTree; ENSGT00550000074306; -.
DR   HOVERGEN; HBG004896; -.
DR   NextBio; 313577; -.
DR   ArrayExpress; Q9ESU6; -.
DR   Bgee; Q9ESU6; -.
DR   CleanEx; MM_BRD4; -.
DR   Genevestigator; Q9ESU6; -.
DR   GermOnline; ENSMUSG00000024002; Mus musculus.
DR   GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR   GO; GO:0000790; C:nuclear chromatin; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007059; P:chromosome segregation; IMP:MGI.
DR   GO; GO:0044154; P:histone H3-K14 acetylation; IMP:MGI.
DR   GO; GO:0043983; P:histone H4-K12 acetylation; IMP:MGI.
DR   GO; GO:0001833; P:inner cell mass cell proliferation; IMP:MGI.
DR   GO; GO:0043388; P:positive regulation of DNA binding; IDA:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IPI:MGI.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   Gene3D; G3DSA:1.20.920.10; Bromodomain; 2.
DR   Pfam; PF00439; Bromodomain; 2.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 2.
DR   SUPFAM; SSF47370; Bromodomain; 2.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Bromodomain; Nucleus;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1   1400       Bromodomain-containing protein 4.
FT                                /FTId=PRO_0000211184.
FT   DOMAIN       75    147       Bromo 1.
FT   DOMAIN      369    441       Bromo 2.
FT   COMPBIAS    206    345       Pro-rich.
FT   COMPBIAS    485    504       Ser-rich.
FT   COMPBIAS    536    595       Lys-rich.
FT   COMPBIAS    693    718       Ser-rich.
FT   COMPBIAS    745   1226       Pro-rich.
FT   COMPBIAS    929   1115       Gln-rich.
FT   COMPBIAS   1319   1362       Gln-rich.
FT   MOD_RES     470    470       Phosphoserine (By similarity).
FT   MOD_RES     471    471       Phosphoserine (By similarity).
FT   MOD_RES     599    599       Phosphothreonine.
FT   MOD_RES     602    602       Phosphoserine.
FT   MOD_RES    1048   1048       Phosphoserine.
FT   MOD_RES    1147   1147       N6-acetyllysine (By similarity).
FT   MOD_RES    1153   1153       Phosphoserine (By similarity).
FT   VAR_SEQ     721    723       EMA -> GPA (in isoform 2).
FT                                /FTId=VSP_010904.
FT   VAR_SEQ     724   1400       Missing (in isoform 2).
FT                                /FTId=VSP_010905.
FT   CONFLICT    188    188       A -> T (in Ref. 2; AAL67834).
FT   CONFLICT    823    823       G -> S (in Ref. 2; AAL67833).
FT   CONFLICT    908    908       V -> A (in Ref. 2; AAL67833).
FT   HELIX       349    365
FT   HELIX       368    370
FT   HELIX       371    374
FT   HELIX       375    377
FT   HELIX       391    394
FT   HELIX       401    409
FT   HELIX       416    433
FT   HELIX       439    457
SQ   SEQUENCE   1400 AA;  155923 MW;  9902BFF7B00ADB59 CRC64;
     MSTESGPGTR LRNLPVMGDG LETSQMSTTQ AQAQPQPANA ASTNPPPPET SNPNKPKRQT
     NQLQYLLRVV LKTLWKHQFA WPFQQPVDAV KLNLPDYYKI IKTPMDMGTI KKRLENNYYW
     NAQECIQDFN TMFTNCYIYN KPGDDIVLMA EALEKLFLQK INELPTEETE IMIVQAKGRG
     RGRKETGAAK PGVSTVPNTT QASTSPQTQT PQQNPPPPVQ ATTHPFPAVT PDLIAQPPVM
     TMVPPQPLQT PSPVPPQPPP PPAPVPQPVQ SHPPIIATTP QPVKTKKGVK RKADTTTPTT
     IDPIHEPPSL APEPKTAKLG PRRESSRPVK PPKKDVPDSQ QHPGPEKSSK ISEQLKCCSG
     ILKEMFAKKH AAYAWPFYKP VDVEALGLHD YCDIIKHPMD MSTIKSKLES REYRDAQEFG
     ADVRLMFSNC YKYNPPDHEV VAMARKLQDV FEMRFAKMPD EPEEPVVTVS SPAVPPPTKV
     VAPPSSSDSS SDSSSDSDSS TDDSEEERAQ RLAELQEQLK AVHEQLAALS QPQQNKPKKK
     EKDKKEKKKE KHKKKEEVEE NKKSKTKELP PKKTKKNNSS NSNVSKKEPV PTKTKPPPTY
     ESEEEDKCKP MSYEEKRQLS LDINKLPGEK LGRVVHIIQS REPSLKNSNP DEIEIDFETL
     KPSTLRELER YVTSCLRKKR KPQAEKVDVI AGSSKMKGFS SSESESTSES SSSDSEDSET
     EMAPKSKKKG HTGRDQKKHH HHHHPQMQPA PAPVPQQPPP PPQQPPPPPP PQQQQQQPPP
     PPPPPSMPQQ TAPAMKSSPP PFITAQVPVL EPQLPGSVFD PIGHFTQPIL HLPQPELPPH
     LPQPPEHSTP PHLNQHAVVS PPALHNALPQ QPSRPSNRAA ALPPKPTRPP AVSPALAQPP
     LLPQPPMVQP PQVLLEDEEP PAPPLTSMQM QLYLQQLQKV QPPTPLLPSV KVQSQPPPPL
     PPPPHPSVQQ QQLQPQPPPP PPPQPQPPPQ QQHQPPPRPV HLPSMPFSAH IQQPPPPPGQ
     QPTHPPPGQQ PPPPQPAKPQ QVIQHHPSPR HHKSDPYSAG HLREAPSPLM IHSPQMPQFQ
     SLTHQSPPQQ NVQPKKQVKG RAEPQPPGPV MGQGQGCPPA SPAAVPMLSQ ELRPPSVVQP
     QPLVVVKEEK IHSPIIRSEP FSTSLRPEPP KHPENIKAPV HLPQRPEMKP VDIGRPVIRP
     PEQSAPPPGA PDKDKQKQEP KTPVAPKKDL KIKNMGSWAS LVQKHPTTPS STAKSSSDSF
     EHFRRAAREK EEREKALKAQ AEHAEKEKER LRQERMRSRE DEDALEQARR AHEEARRRQE
     QQQQQQQQRQ EQQQQQQQAA AVAAASAPQA QSSQPQSMLD QQRELARKRE QERRRREAMA
     ATIDMNFQSD LLSIFEENLF
//
ID   Q9ESU8_MOUSE            Unreviewed;       532 AA.
AC   Q9ESU8;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   08-FEB-2011, entry version 63.
DE   SubName: Full=Neutral amino acid transporter ASCT1;
DE   SubName: Full=Putative uncharacterized protein;
DE   SubName: Full=Solute carrier family 1 (Glutamate/neutral amino acid transporter), member 4;
GN   Name=Slc1a4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Swiss; TISSUE=Kidney;
RX   MEDLINE=20392164; PubMed=10933718;
RX   DOI=10.1128/JVI.74.17.8085-8093.2000;
RA   Marin M., Tailor C.S., Nouri A., Kabat D.;
RT   "Sodium-dependent neutral amino acid transporter type 1 is an
RT   auxiliary receptor for baboon endogenous retrovirus.";
RL   J. Virol. 74:8085-8093(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3;
RC   TISSUE=Mammary tumor. MMTV-LTR/INT3 model. 5 month old mouse. Taken by
RC   biopsy.;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; AF246129; AAG02179.1; -; mRNA.
DR   EMBL; BC043483; AAH43483.1; -; mRNA.
DR   EMBL; AK148075; BAE28327.1; -; mRNA.
DR   IPI; IPI00135130; -.
DR   UniGene; Mm.6379; -.
DR   ProteinModelPortal; Q9ESU8; -.
DR   STRING; Q9ESU8; -.
DR   Ensembl; ENSMUST00000109594; ENSMUSP00000105223; ENSMUSG00000020142.
DR   MGI; MGI:2135601; Slc1a4.
DR   GeneTree; ENSGT00550000074215; -.
DR   HOVERGEN; HBG000080; -.
DR   InParanoid; Q9ESU8; -.
DR   NextBio; 311666; -.
DR   ArrayExpress; Q9ESU8; -.
DR   Bgee; Q9ESU8; -.
DR   Genevestigator; Q9ESU8; -.
DR   GO; GO:0005882; C:intermediate filament; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0017153; F:sodium:dicarboxylate symporter activity; IEA:InterPro.
DR   InterPro; IPR001991; Na-dicarboxylate_symporter.
DR   InterPro; IPR018107; Na-dicarboxylate_symporter_CS.
DR   PANTHER; PTHR11958; Na/diCO_symport; 1.
DR   Pfam; PF00375; SDF; 1.
DR   PRINTS; PR00173; EDTRNSPORT.
DR   PROSITE; PS00713; NA_DICARBOXYL_SYMP_1; 1.
DR   PROSITE; PS00714; NA_DICARBOXYL_SYMP_2; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   532 AA;  56031 MW;  9FA49E43C5DB55D0 CRC64;
     MEKSGETNGY LDGTQAEPAA GPRTPETATG KSQRCASFFR RHALVLLTVS GVLVGAGMGA
     ALRGLQLTRT QITYLAFPGE MLLRMLRMII LPLVVCSLVS GAASLDASSL GRLGGIAVAY
     FGLTTLSASA LAVALAFIIK PGAGAQTLQS SSLGLENSGP PPVSKETVDS FLDLLRNLFP
     SNLVVAAFTT SATDYTVVTH NTSSGNVTKE KIPVVTDVEG MNILGLVLFA LVLGVALKKL
     GPEGEDLIRF FNSFNEATMV LVSWIMWYVP IGIMFLIGSK IVEMKDIVML VTSLGKYIFA
     SMLGHVIHGG IVLPLVYFAF TRKNPFTFLL GLLTPFATAF ATCSSSATLP SMMKCIEENN
     GVDKRISRFI LPIGATVNMD GAAIFQCVAA VFIAQLNNVD LNAGQIFTIL VTATASSVGA
     AGVPAGGVLT IAIILEAIGL PTHDLSLILA VDWIVDRTTT VVNVEGDALG AGILNHLNQK
     VVKKGEQELQ EVKVEAIPNS KSEEETSPLV THQNPAGPVA IAPELESKES VL
//
ID   DDX24_MOUSE             Reviewed;         857 AA.
AC   Q9ESV0; Q61119;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=ATP-dependent RNA helicase DDX24;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 24;
GN   Name=Ddx24;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20396139; PubMed=10936056; DOI=10.1006/geno.2000.6255;
RA   Zhao Y., Yu L., Fu Q., Chen W., Jiang J., Gao J., Zhao S.;
RT   "Cloning and characterization of human DDX24 and mouse Ddx24, two
RT   novel putative DEAD-box proteins, and mapping DDX24 to human
RT   chromosome 14q32.";
RL   Genomics 67:351-355(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 399-857.
RC   STRAIN=BALB/c;
RA   Drysdale B., Howard D.L., Johnson R.J.;
RT   "Identification of a lipopolysaccharide inducible gene in murine
RT   macrophages that putatively encodes an ATP-dependent RNA helicase.";
RL   Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: ATP-dependent RNA helicase (Potential).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX24/MAK5
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
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DR   EMBL; AF214732; AAG02170.1; -; mRNA.
DR   EMBL; U46690; AAB01091.1; -; mRNA.
DR   IPI; IPI00113576; -.
DR   UniGene; Mm.3935; -.
DR   UniGene; Mm.475067; -.
DR   ProteinModelPortal; Q9ESV0; -.
DR   SMR; Q9ESV0; 189-716.
DR   PhosphoSite; Q9ESV0; -.
DR   PRIDE; Q9ESV0; -.
DR   Ensembl; ENSMUST00000044923; ENSMUSP00000040890; ENSMUSG00000041645.
DR   Ensembl; ENSMUST00000110001; ENSMUSP00000105628; ENSMUSG00000041645.
DR   MGI; MGI:1351337; Ddx24.
DR   GeneTree; ENSGT00550000074847; -.
DR   HOGENOM; HBG737336; -.
DR   HOVERGEN; HBG104200; -.
DR   InParanoid; Q9ESV0; -.
DR   OrthoDB; EOG45TCMP; -.
DR   PhylomeDB; Q9ESV0; -.
DR   ArrayExpress; Q9ESV0; -.
DR   Bgee; Q9ESV0; -.
DR   CleanEx; MM_DDX24; -.
DR   Genevestigator; Q9ESV0; -.
DR   GermOnline; ENSMUSG00000041645; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Phosphoprotein;
KW   RNA-binding.
FT   CHAIN         1    857       ATP-dependent RNA helicase DDX24.
FT                                /FTId=PRO_0000055030.
FT   DOMAIN      225    528       Helicase ATP-binding.
FT   DOMAIN      576    723       Helicase C-terminal.
FT   NP_BIND     238    245       ATP (By similarity).
FT   MOTIF       193    221       Q motif.
FT   MOTIF       471    474       DEAD box.
FT   COMPBIAS     81     87       Poly-Glu.
FT   COMPBIAS    755    758       Poly-Ala.
FT   MOD_RES      80     80       Phosphoserine.
FT   MOD_RES      92     92       Phosphoserine (By similarity).
FT   MOD_RES     193    193       Phosphoserine (By similarity).
FT   MOD_RES     288    288       Phosphoserine (By similarity).
FT   MOD_RES     296    296       Phosphoserine (By similarity).
FT   CONFLICT    616    616       T -> N (in Ref. 2; AAB01091).
FT   CONFLICT    710    710       E -> EDIPLFPVHFKKIYKTLQKDE (in Ref. 2).
SQ   SEQUENCE   857 AA;  96471 MW;  2AAE641D008B3227 CRC64;
     MKVKETNSKP KLASRGTFQR KGIKIVGKWK QVTIDPNLFA DGQMDDLVCF EELTDYRLVK
     NPSRLFSSEE TKKRKAQAVS EEEEEEEGQS SSPKKKIKLK KQRDAARAAE GAAAQNEYEV
     KASEPEAQGE VTACSDQKVG GAKSESLAQA APRKKKNKGK KKLDTFQSTS PKLPKKSKKT
     WMAEVHDQKA DVSAWRDLFV PKAVLRALSF LGFSAPTPIQ ALTLAPAIRD KLDILGAAET
     GSGKTLAFAI PMIHSVLQWH KMKAPPIPRS TGMPPREMRF GATAHLGSPC KDRTESGVLP
     EEARIETEAQ PSDSGVQATP ETSASASAQT LLVCDDDAGE GPSSLEEKPV PKQNEDGEEK
     FDAEQAGKLK QELCDQIAIY KVHPRRPLLG LVLTPTRELA IQVRQHIDAV AKFTGINTAI
     LVGGMSTQKQ QRMLNRHPEI VIATPGRLWE LVKEKHPHLS NLRQLRCLVI DEADRMVEKG
     HFAELSQLLE MLNDSQYNPS RQTLVFSATL TLVHQAPARI LHKKHVKKMD KTDKLDLLMQ
     KVGMRGKPKV IDLTRERGTV ETLTETKIHC ETDEKDLYLY YFLMQYPGRS LVFANSISCI
     KRLSGLLKVL DVMPLTLHAC MHQKQRLRNL EQFARLQDCV LLATDVAARG LDIPKVQHVI
     HYQVPRTSEI YIHRSGRTAR AASEGLSLML IGPEDVINFK KIYKTLQKDE DIPLFPVQSK
     YMDVVKERIR LARQIEKAEY RNFQACLHNS WIEQAAAALE IELEEEMYKG GKADQQEERR
     RQKQMKMLKQ ELRHLLSQPL FQENLKTRYP TQSGRPPQPV LASRNIESAL SCLSRQKRRR
     KKPKEPRAPP QPGSSTS
//
ID   AGK_MOUSE               Reviewed;         421 AA.
AC   Q9ESW4; Q9D087;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Acylglycerol kinase, mitochondrial;
DE            EC=2.7.1.107;
DE            EC=2.7.1.94;
DE   AltName: Full=Multiple substrate lipid kinase;
DE            Short=MuLK;
DE            Short=Multi-substrate lipid kinase;
DE   Flags: Precursor;
GN   Name=Agk; Synonyms=Mulk;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND TISSUE SPECIFICITY.
RC   STRAIN=FVB/N; TISSUE=Carcinoma;
RX   PubMed=15252046; DOI=10.1074/jbc.M405932200;
RA   Waggoner D.W., Johnson L.B., Mann P.C., Morris V., Guastella J.,
RA   Bajjalieh S.M.;
RT   "MuLK, a eukaryotic multi-substrate lipid kinase.";
RL   J. Biol. Chem. 279:38228-38235(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=16269826; DOI=10.1194/jlr.M500321-JLR200;
RA   Van Overloop H., Gijsbers S., Van Veldhoven P.P.;
RT   "Further characterization of mammalian ceramide kinase: substrate
RT   delivery and (stereo)specificity, tissue distribution, and subcellular
RT   localization studies.";
RL   J. Lipid Res. 47:268-283(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Liver, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Lipid kinase that can phosphorylate both
CC       monoacylglycerol and diacylglycerol to form lysophosphatidic acid
CC       (LPA) and phosphatidic acid (PA), respectively. Does not
CC       phosphorylate sphingosine. Overexpression increases the formation
CC       and secretion of LPA, resulting in transactivation of EGFR and
CC       activation of the downstream MAPK signaling pathway, leading to
CC       increased cell growth.
CC   -!- CATALYTIC ACTIVITY: ATP + acylglycerol = ADP + acyl-sn-glycerol 3-
CC       phosphate.
CC   -!- CATALYTIC ACTIVITY: ATP + 1,2-diacylglycerol = ADP + 1,2-diacyl-
CC       sn-glycerol 3-phosphate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=45 uM for diacylglycerol;
CC         Vmax=159 nmol/min/mg enzyme with dioeoylglycerol as substrate;
CC   -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9ESW4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9ESW4-2; Sequence=VSP_020927;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- SIMILARITY: Contains 1 DAGKc domain.
CC   -!- CAUTION: Was originally (PubMed:15252046) thought to have ceramide
CC       kinase activity. Such activity is however unlikely in vivo.
CC   -----------------------------------------------------------------------
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DR   EMBL; AY772469; AAV38106.1; -; mRNA.
DR   EMBL; AJ401619; CAC06108.1; -; mRNA.
DR   EMBL; AK011715; BAB27796.1; -; mRNA.
DR   EMBL; AK076224; BAC36260.1; -; mRNA.
DR   EMBL; BC019145; AAH19145.1; -; mRNA.
DR   EMBL; BC093525; AAH93525.1; -; mRNA.
DR   IPI; IPI00113606; -.
DR   IPI; IPI00798555; -.
DR   RefSeq; NP_076027.1; NM_023538.2.
DR   UniGene; Mm.32840; -.
DR   ProteinModelPortal; Q9ESW4; -.
DR   STRING; Q9ESW4; -.
DR   PhosphoSite; Q9ESW4; -.
DR   PRIDE; Q9ESW4; -.
DR   Ensembl; ENSMUST00000031977; ENSMUSP00000031977; ENSMUSG00000029916.
DR   GeneID; 69923; -.
DR   KEGG; mmu:69923; -.
DR   UCSC; uc009bmm.1; mouse.
DR   UCSC; uc009bmn.1; mouse.
DR   CTD; 69923; -.
DR   MGI; MGI:1917173; Agk.
DR   eggNOG; roNOG08304; -.
DR   GeneTree; ENSGT00530000063185; -.
DR   HOGENOM; HBG278744; -.
DR   HOVERGEN; HBG080751; -.
DR   InParanoid; Q9ESW4; -.
DR   OMA; KYWYLGP; -.
DR   OrthoDB; EOG48D0VC; -.
DR   PhylomeDB; Q9ESW4; -.
DR   BRENDA; 2.7.1.107; 244.
DR   BRENDA; 2.7.1.94; 244.
DR   NextBio; 330619; -.
DR   ArrayExpress; Q9ESW4; -.
DR   Bgee; Q9ESW4; -.
DR   CleanEx; MM_AGK; -.
DR   Genevestigator; Q9ESW4; -.
DR   GermOnline; ENSMUSG00000029916; Mus musculus.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0047620; F:acylglycerol kinase activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0001729; F:ceramide kinase activity; IDA:MGI.
DR   GO; GO:0004143; F:diacylglycerol kinase activity; IEA:EC.
DR   GO; GO:0003951; F:NAD+ kinase activity; IEA:InterPro.
DR   GO; GO:0007205; P:activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway; IEA:InterPro.
DR   GO; GO:0046513; P:ceramide biosynthetic process; IDA:MGI.
DR   InterPro; IPR017438; ATP-NAD_kinase_PpnK-typ_a/b.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   Gene3D; G3DSA:3.40.50.10330; ATP-NAD_kinase_PpnK-typ_a/b; 1.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   PROSITE; PS50146; DAGK; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Kinase; Membrane;
KW   Mitochondrion; Nucleotide-binding; Transferase; Transit peptide.
FT   TRANSIT       1     31       Mitochondrion (Potential).
FT   CHAIN        32    421       Acylglycerol kinase, mitochondrial.
FT                                /FTId=PRO_0000252381.
FT   DOMAIN       58    199       DAGKc.
FT   MOD_RES       6      6       N6-acetyllysine (By similarity).
FT   VAR_SEQ     174    421       Missing (in isoform 2).
FT                                /FTId=VSP_020927.
SQ   SEQUENCE   421 AA;  46976 MW;  DBBC48C9EB3206FD CRC64;
     MTAFFKTLRN HWKKTTAGLC LLTWGGHWLY GKHCDNLLRR AACQEAQVFG NQLIPPNAQV
     KKATVFLNPA ACKGKARTLF EKNAAPILHL SGMDVTVVKT DYEGQAKKLL ELMESTDVII
     VAGGDGTLQE VVTGVLRRTD EATFSKIPIG FIPLGQTSSL SHTLFAESGN KVQHITDATL
     AIVKGETVPL DVLQIKGEKE QPVYAMTGLR WGSFRDAGVK VSKYWYLGPL KTKAAHFFST
     LQEWPQTHQA SISYTGPRER PPIEPEETPP RPSLYRRILR RLASFWAQPQ DASSREVSPE
     VWKDVQLSTI ELSITTRNTQ LDLMSKEDFM NICIEPDTVS KGDFIIIGSK KVRDPGLRAA
     GTECLQASHC TLVLPEGTEG SFSIDSEEYE AMPVEVKLLP RKLRFFCDPR KREQMLPSTS
     Q
//
ID   DKC1_MOUSE              Reviewed;         509 AA.
AC   Q9ESX5;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=H/ACA ribonucleoprotein complex subunit 4;
DE            EC=5.4.99.-;
DE   AltName: Full=Dyskerin;
DE   AltName: Full=Nopp140-associated protein of 57 kDa;
DE   AltName: Full=Nucleolar protein NAP57;
DE   AltName: Full=Nucleolar protein family A member 4;
DE   AltName: Full=snoRNP protein DKC1;
GN   Name=Dkc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=129/Ola;
RX   MEDLINE=20366132; PubMed=10903840; DOI=10.1006/geno.2000.6227;
RA   Heiss N.S., Baechner D., Salowsky R., Kolb A., Kioschis P.,
RA   Poustka A.;
RT   "Gene structure and expression of the mouse dyskeratosis congenita
RT   gene, dkc1.";
RL   Genomics 67:153-163(2000).
RN   [2]
RP   FUNCTION.
RX   PubMed=12522253; DOI=10.1126/science.1079447;
RA   Ruggero D., Grisendi S., Piazza F., Rego E., Mari F., Rao P.H.,
RA   Cordon-Cardo C., Pandolfi P.P.;
RT   "Dyskeratosis congenita and cancer in mice deficient in ribosomal RNA
RT   modification.";
RL   Science 299:259-262(2003).
RN   [3]
RP   FUNCTION, AND MUTAGENESIS OF ALA-353 AND GLY-402.
RX   PubMed=15240872; DOI=10.1073/pnas.0402560101;
RA   Mochizuki Y., He J., Kulkarni S., Bessler M., Mason P.J.;
RT   "Mouse dyskerin mutations affect accumulation of telomerase RNA and
RT   small nucleolar RNA, telomerase activity, and ribosomal RNA
RT   processing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:10756-10761(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-453 AND
RP   SER-455, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-453 AND
RP   SER-481, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-453 AND
RP   THR-458, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451; SER-453; SER-455
RP   AND SER-508, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Required for ribosome biogenesis and telomere
CC       maintenance. Probable catalytic subunit of H/ACA small nucleolar
CC       ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes
CC       pseudouridylation of rRNA. This involves the isomerization of
CC       uridine such that the ribose is subsequently attached to C5,
CC       instead of the normal N1. Each rRNA can contain up to 100
CC       pseudouridine ('psi') residues, which may serve to stabilize the
CC       conformation of rRNAs. Also required for correct processing or
CC       intranuclear trafficking of TERC, the RNA component of the
CC       telomerase reverse transcriptase (TERT) holoenzyme.
CC   -!- CATALYTIC ACTIVITY: RNA uridine = RNA pseudouridine.
CC   -!- SUBUNIT: Part of the H/ACA small nucleolar ribonucleoprotein
CC       (H/ACA snoRNP) complex, which contains NHP2/NOLA2, GAR1/NOLA1,
CC       NOP10/NOLA3, and DKC1/NOLA4, which is presumed to be the catalytic
CC       subunit. The complex contains a stable core formed by binding of
CC       one or two NOP10-DKC1 heterodimers to NHP2; GAR1 subsequently
CC       binds to this core via DKC1. The complex binds a box H/ACA small
CC       nucleolar RNA (snoRNA), which may target the specific site of
CC       modification within the RNA substrate. During assembly, the
CC       complex contains NAF1 instead of GAR1/NOLA1. The complex also
CC       interacts with TERC, which contains a 3'-terminal domain related
CC       to the box H/ACA snoRNAs. Specific interactions with snoRNAs or
CC       TERC are mediated by GAR1 and NHP2. Associates with NOLC1/NOPP140.
CC       H/ACA snoRNPs interact with the SMN complex, consisting of SMN1 or
CC       SMN2, SIP1/GEMIN2, DDX20/GEMIN3, and GEMIN4. This is mediated by
CC       interaction between GAR1 and SMN1 or SMN2. The SMN complex may be
CC       required for correct assembly of the H/ACA snoRNP complex.
CC       Component of the telomerase holoenzyme complex at least composed
CC       of TERT, DKC1, WRAP53/TCAB1, NOP10, NHP2, GAR1, TEP1, EST1A, POT1
CC       and a telomerase RNA template component (TERC) (By similarity).
CC       Interacts with SHQ1; this interaction may lead to the
CC       stabilization of DKC1, from the time of its synthesis until its
CC       association with NOP10, NHP2, and NAF1 at the nascent H/ACA RNA
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, Cajal body.
CC       Note=Also localized to Cajal bodies (coiled bodies).
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed, with elevated levels
CC       in Purkinje cells, the olfactory bulb, and Leydig cells of the
CC       testis.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout development,
CC       particularly in developing epithelial tissues.
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase truB family.
CC   -!- SIMILARITY: Contains 1 PUA domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ250973; CAC04528.1; -; Genomic_DNA.
DR   EMBL; AJ250972; CAC04528.1; JOINED; Genomic_DNA.
DR   EMBL; AJ250974; CAC04528.1; JOINED; Genomic_DNA.
DR   EMBL; AJ250975; CAC04528.1; JOINED; Genomic_DNA.
DR   EMBL; AJ250976; CAC04528.1; JOINED; Genomic_DNA.
DR   EMBL; AJ250978; CAC04528.1; JOINED; Genomic_DNA.
DR   EMBL; AJ250980; CAC04528.1; JOINED; Genomic_DNA.
DR   EMBL; AJ250981; CAC04528.1; JOINED; Genomic_DNA.
DR   EMBL; AJ250979; CAC04528.1; JOINED; Genomic_DNA.
DR   EMBL; AJ250977; CAC04528.1; JOINED; Genomic_DNA.
DR   IPI; IPI00113635; -.
DR   UniGene; Mm.291062; -.
DR   ProteinModelPortal; Q9ESX5; -.
DR   SMR; Q9ESX5; 61-379.
DR   STRING; Q9ESX5; -.
DR   PhosphoSite; Q9ESX5; -.
DR   PRIDE; Q9ESX5; -.
DR   Ensembl; ENSMUST00000033776; ENSMUSP00000033776; ENSMUSG00000031403.
DR   MGI; MGI:1861727; Dkc1.
DR   GeneTree; ENSGT00510000047092; -.
DR   HOGENOM; HBG397258; -.
DR   HOVERGEN; HBG081442; -.
DR   InParanoid; Q9ESX5; -.
DR   PhylomeDB; Q9ESX5; -.
DR   ArrayExpress; Q9ESX5; -.
DR   Bgee; Q9ESX5; -.
DR   Genevestigator; Q9ESX5; -.
DR   GermOnline; ENSMUSG00000031403; Mus musculus.
DR   GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; TAS:MGI.
DR   GO; GO:0030529; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro.
DR   GO; GO:0004730; F:pseudouridylate synthase activity; TAS:MGI.
DR   GO; GO:0003723; F:RNA binding; TAS:MGI.
DR   GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR   GO; GO:0000154; P:rRNA modification; TAS:MGI.
DR   InterPro; IPR012960; Dyskerin-like.
DR   InterPro; IPR002501; PsdUridine_synth.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom.
DR   InterPro; IPR004802; Pseudouridine_synthase-related.
DR   InterPro; IPR002478; PUA.
DR   InterPro; IPR015947; PUA-like.
DR   InterPro; IPR004521; Uncharacterised_dom_2.
DR   Pfam; PF08068; DKCLD; 1.
DR   Pfam; PF01472; PUA; 1.
DR   Pfam; PF01509; TruB_N; 1.
DR   SMART; SM00359; PUA; 1.
DR   SUPFAM; SSF55120; PsdUridine_synth_cat_dom; 1.
DR   SUPFAM; SSF88697; PUA-like; 1.
DR   TIGRFAMs; TIGR00425; CBF5; 1.
DR   TIGRFAMs; TIGR00451; unchar_dom_2; 1.
DR   PROSITE; PS50890; PUA; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Isomerase; Nucleus; Phosphoprotein; Ribonucleoprotein;
KW   Ribosome biogenesis; RNA-binding; rRNA processing.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    509       H/ACA ribonucleoprotein complex subunit
FT                                4.
FT                                /FTId=PRO_0000121984.
FT   DOMAIN      297    372       PUA.
FT   REGION        2     21       Nucleolar localization (By similarity).
FT   REGION      446    509       Nuclear and nucleolar localization (By
FT                                similarity).
FT   COMPBIAS     11     17       Poly-Lys.
FT   ACT_SITE    125    125       Nucleophile (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     422    422       Phosphoserine (By similarity).
FT   MOD_RES     451    451       Phosphoserine.
FT   MOD_RES     453    453       Phosphoserine.
FT   MOD_RES     455    455       Phosphoserine.
FT   MOD_RES     458    458       Phosphothreonine.
FT   MOD_RES     481    481       Phosphoserine.
FT   MOD_RES     492    492       Phosphothreonine (By similarity).
FT   MOD_RES     493    493       Phosphothreonine (By similarity).
FT   MOD_RES     508    508       Phosphoserine.
FT   MUTAGEN     353    353       A->V: Destabilization of TERC, impaired
FT                                telomerase function, and reduced rRNA
FT                                pseudouridylation and pre-rRNA
FT                                processing.
FT   MUTAGEN     402    402       G->E: Reduced rRNA pseudouridylation and
FT                                pre-rRNA processing.
SQ   SEQUENCE   509 AA;  57502 MW;  E2522E700D84D301 CRC64;
     MADAEVITFP KKHKKKKDRK PLQEDDVAEI QHAEEFLIKP ESKVAQLDTS QWPLLLKNFD
     KLNVRTAHYT PLPCGSNPLK REIGDYIRTG FINLDKPSNP SSHEVVAWIR RILRVEKTGH
     SGTLDPKVTG CLIVCIERAT RLVKSQQSAG KEYVGIVRLH NAIEGGTQLS RALETLTGAL
     FQRPPLIAAV KRQLRVRTIY ESKMIEYDPE RRLGIFWVSC EAGTYIRTLC VHLCFVLGSG
     CQMQELRRVR SGVMSEKDHM VTMHDVLDAQ WLYDNHKDES YLRRVVYPLE KLLTSHKRLV
     MKDSAVNAIC YGAKIMLPGL LRYEDGIEVN QEIVVITTKG EAICMAIALM TTAVISTCDH
     GIVAKIKRVI MERDTYPRKW GLGPKASQKK MMIKQGLLDK HGKPTDNTPA TWKQDYIDYS
     DSGKNTLVTE AVQAPQLAAE AVNVIKRKRD SESESDETPT VPQLKEKKKK KDKKPKTVLE
     SGGETGDGDN DTTKKKKKKK VKVVEEMSE
//
ID   CLD12_MOUSE             Reviewed;         244 AA.
AC   Q9ET43; Q3TM65; Q8BH13;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2003, sequence version 2.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Claudin-12;
GN   Name=Cldn12;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, Lung, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-237.
RC   STRAIN=ICR;
RA   Kiuchi Y., Morita K., Furuse M., Tsukita S.;
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-228, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Plays a major role in tight junction-specific
CC       obliteration of the intercellular space, through calcium-
CC       independent cell-adhesion activity (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction. Cell
CC       membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the claudin family.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK039672; BAC30414.1; -; mRNA.
DR   EMBL; AK049331; BAC33687.1; -; mRNA.
DR   EMBL; AK132155; BAE21001.1; -; mRNA.
DR   EMBL; AK166110; BAE38577.1; -; mRNA.
DR   EMBL; BC024057; AAH24057.1; -; mRNA.
DR   EMBL; AF247664; AAF98801.1; -; mRNA.
DR   IPI; IPI00282282; -.
DR   RefSeq; NP_001180588.1; NM_001193659.1.
DR   RefSeq; NP_001180589.1; NM_001193660.1.
DR   RefSeq; NP_001180590.1; NM_001193661.1.
DR   RefSeq; NP_075028.1; NM_022890.2.
DR   UniGene; Mm.40132; -.
DR   UniGene; Mm.481743; -.
DR   STRING; Q9ET43; -.
DR   PhosphoSite; Q9ET43; -.
DR   PRIDE; Q9ET43; -.
DR   Ensembl; ENSMUST00000060947; ENSMUSP00000061928; ENSMUSG00000046798.
DR   Ensembl; ENSMUST00000115445; ENSMUSP00000111105; ENSMUSG00000046798.
DR   Ensembl; ENSMUST00000115446; ENSMUSP00000111106; ENSMUSG00000046798.
DR   GeneID; 64945; -.
DR   KEGG; mmu:64945; -.
DR   UCSC; uc008wip.1; mouse.
DR   CTD; 64945; -.
DR   MGI; MGI:1929288; Cldn12.
DR   eggNOG; roNOG13568; -.
DR   GeneTree; ENSGT00400000022250; -.
DR   HOGENOM; HBG716037; -.
DR   HOVERGEN; HBG050986; -.
DR   InParanoid; Q9ET43; -.
DR   OMA; WYCACKS; -.
DR   OrthoDB; EOG4DR9D2; -.
DR   PhylomeDB; Q9ET43; -.
DR   NextBio; 320247; -.
DR   ArrayExpress; Q9ET43; -.
DR   Bgee; Q9ET43; -.
DR   CleanEx; MM_CLDN12; -.
DR   Genevestigator; Q9ET43; -.
DR   GermOnline; ENSMUSG00000046798; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005923; C:tight junction; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0016338; P:calcium-independent cell-cell adhesion; ISS:UniProtKB.
DR   InterPro; IPR013287; Claudin12.
DR   InterPro; IPR017974; Claudin_CS.
DR   PRINTS; PR01872; CLAUDIN12.
DR   PROSITE; PS01346; CLAUDIN; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Membrane; Phosphoprotein;
KW   Tight junction; Transmembrane; Transmembrane helix.
FT   CHAIN         1    244       Claudin-12.
FT                                /FTId=PRO_0000144766.
FT   TOPO_DOM      1     10       Cytoplasmic (Potential).
FT   TRANSMEM     11     31       Helical; (Potential).
FT   TOPO_DOM     32     87       Extracellular (Potential).
FT   TRANSMEM     88    108       Helical; (Potential).
FT   TOPO_DOM    109    135       Cytoplasmic (Potential).
FT   TRANSMEM    136    156       Helical; (Potential).
FT   TOPO_DOM    157    174       Extracellular (Potential).
FT   TRANSMEM    175    195       Helical; (Potential).
FT   TOPO_DOM    196    244       Cytoplasmic (Potential).
FT   MOD_RES     228    228       Phosphoserine.
FT   MOD_RES     231    231       Phosphoserine (By similarity).
SQ   SEQUENCE   244 AA;  26995 MW;  5A49F3BD7C25C87E CRC64;
     MGCRDVHAAT VLSFLCGIAS VAGLFAGTLL PNWRKLRLIT FNRNEKNLTI YTGLWVKCAR
     YDGSSDCLMY DRTWYLSVDQ LDLRVLQFAL PLSIVIAMGA LLLCLIGMCN TAFNSSVPNI
     KLAKCLVNSA GCHLVAGLLF FLAGTVSLSP SIWAIFYNSH LNRKFEPVFT FDYAVFVTIA
     SSGGLFMTAL LLFVWYCACK SLSSPFWQPL YSHAPGMHTY SQPYSSRSRL SAIEIDIPVV
     SHST
//
ID   JPH3_MOUSE              Reviewed;         744 AA.
AC   Q9ET77; Q3ZAS3; Q8BNM7; Q9EQZ2;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Junctophilin-3;
DE            Short=JP-3;
DE   AltName: Full=Junctophilin type 3;
GN   Name=Jph3; Synonyms=Jp3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=129, and C57BL/6J; TISSUE=Brain;
RX   MEDLINE=20403299; PubMed=10949023; DOI=10.1016/S1097-2765(00)00003-4;
RA   Takeshima H., Komazaki S., Nishi M., Iino M., Kangawa K.;
RT   "Junctophilins: a novel family of junctional membrane complex
RT   proteins.";
RL   Mol. Cell 6:11-22(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   MEDLINE=21903756; PubMed=11906164; DOI=10.1006/bbrc.2002.6649;
RA   Nishi M., Hashimoto K., Kuriyama K., Komazaki S., Kano M., Shibata S.,
RA   Takeshima H.;
RT   "Motor discoordination in mutant mice lacking junctophilin type 3.";
RL   Biochem. Biophys. Res. Commun. 292:318-324(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-506, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Contributes to the stabilization of the junctional
CC       membrane complexes, which are common to excitable cells and
CC       mediate cross-talk between cell surface and intracellular ion
CC       channels. Probably acts by anchoring the plasma membrane and
CC       endoplasmic reticulum (By similarity). May play an active role in
CC       certain neurons involved in motor coordination.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC       Endoplasmic reticulum membrane; Single-pass type IV membrane
CC       protein. Note=Localized predominantly on the plasma membrane. The
CC       transmembrane domain is anchored in endoplasmic reticulum
CC       membrane, while the N-terminal part associates with the plasma
CC       membrane.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in brain. Expressed in
CC       certain populations of neurons but not in glial cells. In
CC       cerebellar sections, it is highly expressed in Purkinge cells,
CC       while it is weakly expressed in granular cells.
CC   -!- DOMAIN: The MORN (membrane occupation and recognition nexus)
CC       repeats contribute to the plasma membrane binding, possibly by
CC       interacting with phospholipids (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice are viable and fertile but have defects
CC       in balance/motor coordination tasks.
CC   -!- SIMILARITY: Belongs to the junctophilin family.
CC   -!- SIMILARITY: Contains 8 MORN repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC38666.1; Type=Erroneous termination; Positions=745; Note=Translated as stop;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB024449; BAB12046.1; -; mRNA.
DR   EMBL; AB024450; BAB20320.1; -; Genomic_DNA.
DR   EMBL; AK082880; BAC38666.1; ALT_SEQ; mRNA.
DR   EMBL; BC103682; AAI03683.1; -; mRNA.
DR   EMBL; BC104736; AAI04737.1; -; mRNA.
DR   EMBL; BC105307; AAI05308.1; -; mRNA.
DR   IPI; IPI00113636; -.
DR   RefSeq; NP_065630.1; NM_020605.2.
DR   UniGene; Mm.306870; -.
DR   ProteinModelPortal; Q9ET77; -.
DR   SMR; Q9ET77; 31-145, 282-360.
DR   STRING; Q9ET77; -.
DR   PhosphoSite; Q9ET77; -.
DR   PRIDE; Q9ET77; -.
DR   Ensembl; ENSMUST00000026357; ENSMUSP00000026357; ENSMUSG00000025318.
DR   GeneID; 57340; -.
DR   KEGG; mmu:57340; -.
DR   UCSC; uc009nrz.1; mouse.
DR   CTD; 57340; -.
DR   MGI; MGI:1891497; Jph3.
DR   GeneTree; ENSGT00600000084242; -.
DR   HOGENOM; HBG715737; -.
DR   HOVERGEN; HBG031648; -.
DR   InParanoid; Q9ET77; -.
DR   OMA; NGLEYQR; -.
DR   OrthoDB; EOG4F7NJZ; -.
DR   PhylomeDB; Q9ET77; -.
DR   NextBio; 313702; -.
DR   ArrayExpress; Q9ET77; -.
DR   Bgee; Q9ET77; -.
DR   CleanEx; MM_JPH3; -.
DR   Genevestigator; Q9ET77; -.
DR   GermOnline; ENSMUSG00000025318; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; TAS:MGI.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0040011; P:locomotion; IMP:MGI.
DR   InterPro; IPR017191; Junctophilin.
DR   InterPro; IPR003409; MORN.
DR   Pfam; PF02493; MORN; 8.
DR   PIRSF; PIRSF037387; Junctophilin; 1.
DR   SMART; SM00698; MORN; 7.
PE   1: Evidence at protein level;
KW   Cell membrane; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW   Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN         1    744       Junctophilin-3.
FT                                /FTId=PRO_0000159851.
FT   TOPO_DOM      1    723       Cytoplasmic (Potential).
FT   TRANSMEM    724    744       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   REPEAT       15     37       MORN 1.
FT   REPEAT       39     60       MORN 2.
FT   REPEAT       61     82       MORN 3.
FT   REPEAT       83    105       MORN 4.
FT   REPEAT      107    129       MORN 5.
FT   REPEAT      130    152       MORN 6.
FT   REPEAT      288    310       MORN 7.
FT   REPEAT      311    333       MORN 8.
FT   COMPBIAS      4    143       Gly-rich.
FT   COMPBIAS    366    416       Ala-rich.
FT   MOD_RES     420    420       Phosphoserine.
FT   MOD_RES     506    506       Phosphoserine.
SQ   SEQUENCE   744 AA;  81229 MW;  3D72AED6A6FDA914 CRC64;
     MSSGGRFNFD DGGSYCGGWE DGKAHGHGVC TGPKGQGEYT GSWSHGFEVL GVYTWPSGNT
     YQGTWAQGKR HGIGLESKGK WVYKGEWTHG FKGRYGVREC TGNGAKYEGT WSNGLQDGYG
     TETYSDGGTY QGQWVGGMRQ GYGVRQSVPY GMAAVIRSPL RTSINSLRSE HTNGAALHPD
     ASPAVAGSPA VSRGGFVLVA HSDSEILKSK KKGLFRRSLL SGLKLRKSES KSSLASQRSK
     QSSFRSEAGM STVSSTASDI HSTISLGEAE AELAVIEDDI DATTTETYVG EWKNDKRSGF
     GVSQRSDGLK YEGEWVSNRR HGYGCMTFPD GTKEEGKYKQ NVLVSGKRKN LIPLRASKIR
     EKVDRAVEAA ERAATIAKQK AEIAASRTSH SRAKAEAALT AAQKAQEEAR IARITAKEFS
     PSFQHRENGL EYQRPKHQMS CDDIEVLSTG TPLQQESPEL YRKGTTPSDL TPDDSPLQSF
     PASPTSTPPP APASRTKMAH FSRQVSVDEE RSGDIQMLLE GRGGDYARNS WGEEKAGASR
     GIRSGALRSG QPTEDFRTRG SGHKQPGNPK PRERRTESPT TFSWTSHHRA GNPCSGGPKL
     LEPDEEQLSN YKLEMKPLLR MDACPQDTHP QRRRHSRGAG GDRGFGLQRL RSKSQNKENL
     RPASSAEPTV QKLESLRLGD RPEPRLLRWD LTFSPPQKSL PVALESDEET GDELKSSTGS
     APILVVMVIL LNIGVAILFI NFFI
//
ID   JPH1_MOUSE              Reviewed;         660 AA.
AC   Q9ET80; Q0VB08; Q9EQZ3;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Junctophilin-1;
DE            Short=JP-1;
DE   AltName: Full=Junctophilin type 1;
GN   Name=Jph1; Synonyms=Jp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND CHARACTERIZATION.
RC   STRAIN=129, and C57BL/6J; TISSUE=Skeletal muscle;
RX   MEDLINE=20403299; PubMed=10949023; DOI=10.1016/S1097-2765(00)00003-4;
RA   Takeshima H., Komazaki S., Nishi M., Iino M., Kangawa K.;
RT   "Junctophilins: a novel family of junctional membrane complex
RT   proteins.";
RL   Mol. Cell 6:11-22(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   MEDLINE=21426954; PubMed=11535622; DOI=10.1083/jcb.200105040;
RA   Ito K., Komazaki S., Sasamoto K., Yoshida M., Nishi M., Kitamura K.,
RA   Takeshima H.;
RT   "Deficiency of triad junction and contraction in mutant skeletal
RT   muscle lacking junctophilin type 1.";
RL   J. Cell Biol. 154:1059-1067(2001).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448 AND SER-452, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-448 AND
RP   SER-452, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Contributes to the stabilization of the junctional
CC       membrane complexes, which are common to excitable cells and
CC       mediate cross-talk between cell surface and intracellular ion
CC       channels. Probably acts by anchoring the plasma membrane and
CC       endoplasmic/sarcoplasmic reticulum. Contributes to the
CC       construction of skeletal muscle triad junctions.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC       Endoplasmic reticulum membrane; Single-pass type IV membrane
CC       protein. Sarcoplasmic reticulum membrane; Single-pass type IV
CC       membrane protein. Note=Predominantly on the plasma membrane. The
CC       transmembrane domain is anchored in endoplasmic/sarcoplasmic
CC       reticulum membrane, while the N-terminal part associates with the
CC       plasma membrane. In skeletal muscle cells, it is predominantly
CC       localized at the junction of the A and I bands.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in skeletal muscle.
CC       While it is weakly expressed in embryos and neonates, it is
CC       abundant in young adult muscles.
CC   -!- DOMAIN: The MORN (membrane occupation and recognition nexus)
CC       repeats contribute to the plasma membrane binding, possibly by
CC       interacting with phospholipids (By similarity).
CC   -!- MISCELLANEOUS: JPH1 deficient mice show no milk suckling and die
CC       shortly after birth. In the skeletal muscles, triad junctions are
CC       reduced in number, and sarcoplasmic reticulum is often
CC       structurally abnormal.
CC   -!- SIMILARITY: Belongs to the junctophilin family.
CC   -!- SIMILARITY: Contains 7 MORN repeats.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB024445; BAB12043.1; -; mRNA.
DR   EMBL; AB024446; BAB20319.1; -; Genomic_DNA.
DR   EMBL; BC120839; AAI20840.1; -; mRNA.
DR   EMBL; BC137669; AAI37670.1; -; mRNA.
DR   IPI; IPI00113656; -.
DR   RefSeq; NP_065629.1; NM_020604.1.
DR   UniGene; Mm.143761; -.
DR   UniGene; Mm.443358; -.
DR   ProteinModelPortal; Q9ET80; -.
DR   SMR; Q9ET80; 275-348.
DR   STRING; Q9ET80; -.
DR   PhosphoSite; Q9ET80; -.
DR   PRIDE; Q9ET80; -.
DR   Ensembl; ENSMUST00000038382; ENSMUSP00000039072; ENSMUSG00000042686.
DR   GeneID; 57339; -.
DR   KEGG; mmu:57339; -.
DR   UCSC; uc007aka.1; mouse.
DR   CTD; 57339; -.
DR   MGI; MGI:1891495; Jph1.
DR   GeneTree; ENSGT00600000084242; -.
DR   HOGENOM; HBG715737; -.
DR   HOVERGEN; HBG031648; -.
DR   InParanoid; Q9ET80; -.
DR   OMA; KWSPSKS; -.
DR   OrthoDB; EOG4868C6; -.
DR   PhylomeDB; Q9ET80; -.
DR   NextBio; 313698; -.
DR   ArrayExpress; Q9ET80; -.
DR   Bgee; Q9ET80; -.
DR   CleanEx; MM_JPH1; -.
DR   Genevestigator; Q9ET80; -.
DR   GermOnline; ENSMUSG00000042686; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030018; C:Z disc; IDA:MGI.
DR   GO; GO:0008307; F:structural constituent of muscle; IMP:MGI.
DR   GO; GO:0007517; P:muscle organ development; IMP:MGI.
DR   InterPro; IPR017191; Junctophilin.
DR   InterPro; IPR003409; MORN.
DR   Pfam; PF02493; MORN; 8.
DR   PIRSF; PIRSF037387; Junctophilin; 1.
DR   SMART; SM00698; MORN; 7.
PE   1: Evidence at protein level;
KW   Cell membrane; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW   Repeat; Sarcoplasmic reticulum; Transmembrane; Transmembrane helix.
FT   CHAIN         1    660       Junctophilin-1.
FT                                /FTId=PRO_0000159845.
FT   TOPO_DOM      1    638       Cytoplasmic (Potential).
FT   TRANSMEM    639    659       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   REPEAT       14     36       MORN 1.
FT   REPEAT       38     59       MORN 2.
FT   REPEAT       60     82       MORN 3.
FT   REPEAT      106    128       MORN 4.
FT   REPEAT      129    151       MORN 5.
FT   REPEAT      281    303       MORN 6.
FT   REPEAT      304    326       MORN 7.
FT   COMPBIAS      3    142       Gly-rich.
FT   COMPBIAS    226    258       Ser-rich.
FT   COMPBIAS    359    409       Ala-rich.
FT   MOD_RES     157    157       Phosphoserine (By similarity).
FT   MOD_RES     216    216       Phosphoserine.
FT   MOD_RES     220    220       Phosphoserine (By similarity).
FT   MOD_RES     448    448       Phosphoserine.
FT   MOD_RES     452    452       Phosphoserine.
FT   MOD_RES     460    460       Phosphothreonine (By similarity).
FT   MOD_RES     461    461       Phosphothreonine (By similarity).
FT   MOD_RES     465    465       Phosphoserine (By similarity).
FT   MOD_RES     469    469       Phosphoserine (By similarity).
SQ   SEQUENCE   660 AA;  71905 MW;  CC307C68F1250831 CRC64;
     MTGGRFDFDD GGTYCGGWEE GKAHGHGICT GPKGQGEYSG SWSHGFEVVG VYTWPSGNTY
     QGYWAQGKRH GLGVETKGKW MYRGEWSHGF KGRYGVRQSL CTPARYEGTW SNGLQDGYGV
     ETYGDGGTYQ GQWAGGMRHG YGVRQSVPYG MATVIRSPLR TSLASLRSEQ SNGSVLHEAA
     AAAADSPAGT RGGFVLNFHA DTELGKKKGG LFRRGSLLGS MKLRKSESKS SISSKRSSVR
     SDAAMSRISS SDANSTISFG DVDCDFCPVE DHVDATTTET YMGEWKNDKR NGFGISERSN
     GMKYEGEWAN NKRHGYGCTV FPDGSKEEGK YKNNILVRGI RKQLIPIRNT KTREKVDRAI
     EGAQRAAAMA RTKVEIANSR TAHARAKADA ADQAALAARQ ECDIARAVAR ELSPDFYQPG
     PDYIKQRCQE GGDIKENPEE KVLEKPPSPK ESPHFYRKGT TPPRSPESSP KQSHSPQPSS
     PEPSKKQNPS PGARLSQDKQ SLAEEQVTAF VNKPSMSKAP AKELGASVSK YSGRHHVPNP
     SNGELHSQYH GYYVKLNTPQ HPPEDREDDR GVSQSSSALV PRPSPNKWGP PKSVTKPVAK
     ESKTEPKAKK SELAIPKNPA SNDTCPSLEK EANSGPNSIM IVLVMLLNIG LAILFVHFLT
//
ID   RCAN1_MOUSE             Reviewed;         198 AA.
AC   Q9JHG6; Q91WQ4; Q9JK50; Q9JK51; Q9JKK2; Q9JKK3;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Calcipressin-1;
DE   AltName: Full=Down syndrome critical region protein 1 homolog;
DE   AltName: Full=Myocyte-enriched calcineurin-interacting protein 1;
DE            Short=MCIP1;
DE   AltName: Full=Regulator of calcineurin 1;
GN   Name=Rcan1; Synonyms=Dscr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=20534792; PubMed=11080588; DOI=10.1016/S0378-1119(00)00407-8;
RA   Strippoli P., Petrini M., Lenzi L., Carinci P., Zannotti M.;
RT   "The murine DSCR1-like (Down syndrome candidate region 1) gene family:
RT   conserved synteny with the human orthologous genes.";
RL   Gene 257:223-232(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RX   MEDLINE=20187590; PubMed=10722714; DOI=10.1074/jbc.275.12.8719;
RA   Rothermel B., Vega R.B., Yang J., Wu H., Bassel-Duby R.,
RA   Williams R.S.;
RT   "A protein encoded within the Down syndrome critical region is
RT   enriched in striated muscles and inhibits calcineurin signaling.";
RL   J. Biol. Chem. 275:8719-8725(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND FUNCTION.
RC   TISSUE=Fetal brain;
RX   MEDLINE=21152920; PubMed=11231093; DOI=10.1016/S0925-4773(00)00583-9;
RA   Casas C., Martinez S., Pritchard M.A., Fuentes J.J., Nadal M.,
RA   Guimera J., Arbones M., Florez J., Soriano E., Estivill X.,
RA   Alcantara S.;
RT   "Dscr1, a novel endogenous inhibitor of calcineurin signaling, is
RT   expressed in the primitive ventricle of the heart and during
RT   neurogenesis.";
RL   Mech. Dev. 101:289-292(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C).
RA   Fuentes J.J., Pritchard M.A., Pucharcos C., Estivill X.;
RT   "Down syndrome candidate region 1 (Dscr1), one of three alternatively
RT   spliced exon 1 transcripts.";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic stem cell;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   STRUCTURE BY NMR OF 14-103.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of RRM domain in calcipressin 1.";
RL   Submitted (MAY-2004) to the PDB data bank.
CC   -!- FUNCTION: Inhibits calcineurin-dependent transcriptional responses
CC       by binding to the catalytic domain of calcineurin A. Could play a
CC       role during central nervous system development.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Additional isoforms seem to exist;
CC       Name=A; Synonyms=1;
CC         IsoId=Q9JHG6-1; Sequence=Displayed;
CC       Name=B; Synonyms=4;
CC         IsoId=Q9JHG6-2; Sequence=VSP_001317;
CC       Name=C;
CC         IsoId=Q9JHG6-3; Sequence=VSP_001318;
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart and skeletal muscle.
CC       Also expressed in all other tissues.
CC   -!- SIMILARITY: Belongs to the RCAN family.
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DR   EMBL; AF282255; AAF91461.1; -; mRNA.
DR   EMBL; AF237789; AAF63485.1; -; mRNA.
DR   EMBL; AF237790; AAF63486.1; -; mRNA.
DR   EMBL; AF260717; AAF70343.1; -; mRNA.
DR   EMBL; AF263239; AAF72701.1; -; mRNA.
DR   EMBL; AF263240; AAF72702.1; -; mRNA.
DR   EMBL; AK010696; BAB27128.1; -; mRNA.
DR   EMBL; BC013551; AAH13551.1; -; mRNA.
DR   IPI; IPI00128307; -.
DR   IPI; IPI00319914; -.
DR   IPI; IPI00331535; -.
DR   RefSeq; NP_062339.2; NM_019466.3.
DR   UniGene; Mm.265744; -.
DR   PDB; 1WEY; NMR; -; A=29-103.
DR   PDBsum; 1WEY; -.
DR   ProteinModelPortal; Q9JHG6; -.
DR   SMR; Q9JHG6; 11-103.
DR   IntAct; Q9JHG6; 1.
DR   STRING; Q9JHG6; -.
DR   PhosphoSite; Q9JHG6; -.
DR   PRIDE; Q9JHG6; -.
DR   Ensembl; ENSMUST00000023672; ENSMUSP00000023672; ENSMUSG00000022951.
DR   Ensembl; ENSMUST00000060005; ENSMUSP00000060394; ENSMUSG00000022951.
DR   GeneID; 54720; -.
DR   KEGG; mmu:54720; -.
DR   UCSC; uc007zzd.1; mouse.
DR   CTD; 54720; -.
DR   MGI; MGI:1890564; Rcan1.
DR   GeneTree; ENSGT00400000022053; -.
DR   HOVERGEN; HBG018932; -.
DR   InParanoid; Q9JHG6; -.
DR   OMA; VFSESET; -.
DR   OrthoDB; EOG4RJG2R; -.
DR   ArrayExpress; Q9JHG6; -.
DR   Bgee; Q9JHG6; -.
DR   CleanEx; MM_RCAN1; -.
DR   Genevestigator; Q9JHG6; -.
DR   GermOnline; ENSMUSG00000022951; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0019722; P:calcium-mediated signaling; IEA:InterPro.
DR   GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IDA:MGI.
DR   GO; GO:0048741; P:skeletal muscle fiber development; IDA:MGI.
DR   InterPro; IPR006931; Calcipressin.
DR   PANTHER; PTHR10300; Calcipressin; 1.
DR   Pfam; PF04847; Calcipressin; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing.
FT   CHAIN         1    198       Calcipressin-1.
FT                                /FTId=PRO_0000211415.
FT   VAR_SEQ       1     80       Missing (in isoform C).
FT                                /FTId=VSP_001318.
FT   VAR_SEQ       1     28       MEEVDLQDLPSATIACHLDPRVFVDGLC -> MHFRDFSYN
FT                                FSSLIACVANDDVFSESET (in isoform B).
FT                                /FTId=VSP_001317.
FT   CONFLICT    152    152       T -> P (in Ref. 2; AAF63485/AAF63486).
FT   HELIX        29     37
FT   STRAND       44     48
FT   TURN         49     52
FT   STRAND       53     57
FT   HELIX        63     69
FT   STRAND       74     76
FT   STRAND       82     84
SQ   SEQUENCE   198 AA;  22706 MW;  BA35340AFD6F0582 CRC64;
     MEEVDLQDLP SATIACHLDP RVFVDGLCRA KFESLFRTYD KDTTFQYFKS FKRVRINFSN
     PLSAADARLR LHKTEFLGKE MKLYFAQTLH IGSSHLAPPN PDKQFLISPP ASPPVGWKQV
     EDATPVINYD LLYAISKLGP GEKYELHAAT DTTPSVVVHV CESDQENEEE EEEMERMKRP
     KPKIIQTRRP EYTPIHLS
//
ID   NHRF2_MOUSE             Reviewed;         337 AA.
AC   Q9JHL1; Q3TDR3; Q6P074; Q8BGL9; Q8BW05; Q9DCR6;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   08-FEB-2011, entry version 85.
DE   RecName: Full=Na(+)/H(+) exchange regulatory cofactor NHE-RF2;
DE            Short=NHERF-2;
DE   AltName: Full=NHE3 kinase A regulatory protein E3KARP;
DE   AltName: Full=Octs2;
DE   AltName: Full=SRY-interacting protein 1;
DE            Short=SIP-1;
DE   AltName: Full=Sodium-hydrogen exchanger regulatory factor 2;
DE   AltName: Full=Solute carrier family 9 isoform A3 regulatory factor 2;
DE   AltName: Full=Tyrosine kinase activator protein 1;
DE            Short=TKA-1;
GN   Name=Slc9a3r2; Synonyms=Nherf2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Blood, and Embryo;
RA   Sarker A.H., Akiyama K., Tsutsui K., Seki S.;
RT   "cDNA cloning, genomic structure and sequence analysis of the mouse
RT   mSlc9a3r2/E3karp/Sip-1/Tka-1/Octs2 gene.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Embryonic heart, Kidney, Small intestine, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH PDZK1.
RX   MEDLINE=22894942; PubMed=14531806;
RX   DOI=10.1046/j.1523-1755.2003.00266.x;
RA   Gisler S.M., Pribanic S., Bacic D., Forrer P., Gantenbein A.,
RA   Sabourin L.A., Tsuji A., Zhao Z.-S., Manser E., Biber J., Murer H.;
RT   "PDZK1: I. a major scaffolder in brush borders of proximal tubular
RT   cells.";
RL   Kidney Int. 64:1733-1745(2003).
RN   [5]
RP   INTERACTION WITH SRY.
RX   PubMed=16166090; DOI=10.1074/jbc.M504127200;
RA   Thevenet L., Albrecht K.H., Malki S., Berta P., Boizet-Bonhoure B.,
RA   Poulat F.;
RT   "NHERF2/SIP-1 interacts with mouse SRY via a different mechanism than
RT   human SRY.";
RL   J. Biol. Chem. 280:38625-38630(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 199-226 IN COMPLEX WITH RDX.
RX   PubMed=16615918; DOI=10.1016/j.str.2006.01.015;
RA   Terawaki S., Maesaki R., Hakoshima T.;
RT   "Structural basis for NHERF recognition by ERM proteins.";
RL   Structure 14:777-789(2006).
CC   -!- FUNCTION: Scaffold protein that connects plasma membrane proteins
CC       with members of the ezrin/moesin/radixin family and thereby helps
CC       to link them to the actin cytoskeleton and to regulate their
CC       surface expression. Necessary for cAMP-mediated phosphorylation
CC       and inhibition of SLC9A3. May also act as scaffold protein in the
CC       nucleus (By similarity).
CC   -!- SUBUNIT: Homodimer, and heterodimer with SLC9A3R1. Binds PDZK1.
CC       Interacts with SRY. Binds ADRB2, SLC9A3, P2RY1, P2YR2, RDX and
CC       LPAR2 (By similarity). Interacts with MCC (By similarity). Found
CC       in a complex with EZR, PODXL and SLC9A3R2 (By similarity).
CC       Interacts (via the PDZ domains) with PODXL (via the C-terminal
CC       PDZ-binding motif DTHL); interaction is detected in glomerular
CC       epithelium cells (By similarity).
CC   -!- INTERACTION:
CC       P69744:Trpv5; NbExp=1; IntAct=EBI-538451, EBI-538447;
CC   -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane
CC       protein (By similarity). Nucleus (By similarity). Apical cell
CC       membrane (By similarity). Note=Localizes with EZR and PODXL at the
CC       apical cell membrane of glomerular epithelium cells and the sides
CC       of the food processes. Nuclear, in a punctate pattern (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9JHL1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9JHL1-2; Sequence=VSP_009379, VSP_009380;
CC   -!- SIMILARITY: Contains 2 PDZ (DHR) domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB026489; BAA97568.1; -; mRNA.
DR   EMBL; AB026490; BAA97569.1; -; Genomic_DNA.
DR   EMBL; AK002557; BAB22185.1; -; mRNA.
DR   EMBL; AK039491; BAC30366.1; -; mRNA.
DR   EMBL; AK075813; BAC35980.1; -; mRNA.
DR   EMBL; AK084801; BAC39282.1; -; mRNA.
DR   EMBL; AK170057; BAE41537.1; -; mRNA.
DR   EMBL; BC065778; AAH65778.1; -; mRNA.
DR   IPI; IPI00308063; -.
DR   IPI; IPI00399912; -.
DR   RefSeq; NP_075542.2; NM_023055.2.
DR   RefSeq; NP_075938.2; NM_023449.3.
DR   UniGene; Mm.21587; -.
DR   PDB; 2D11; X-ray; 2.81 A; E/F/G/H=310-337.
DR   PDBsum; 2D11; -.
DR   ProteinModelPortal; Q9JHL1; -.
DR   SMR; Q9JHL1; 9-91, 147-232.
DR   IntAct; Q9JHL1; 1.
DR   MINT; MINT-152409; -.
DR   STRING; Q9JHL1; -.
DR   PhosphoSite; Q9JHL1; -.
DR   PRIDE; Q9JHL1; -.
DR   Ensembl; ENSMUST00000002572; ENSMUSP00000002572; ENSMUSG00000002504.
DR   Ensembl; ENSMUST00000019684; ENSMUSP00000019684; ENSMUSG00000002504.
DR   GeneID; 65962; -.
DR   KEGG; mmu:65962; -.
DR   UCSC; uc008axk.1; mouse.
DR   CTD; 65962; -.
DR   MGI; MGI:1890662; Slc9a3r2.
DR   eggNOG; roNOG14538; -.
DR   GeneTree; ENSGT00530000062999; -.
DR   HOGENOM; HBG714863; -.
DR   HOVERGEN; HBG052616; -.
DR   InParanoid; Q9JHL1; -.
DR   NextBio; 320388; -.
DR   ArrayExpress; Q9JHL1; -.
DR   Bgee; Q9JHL1; -.
DR   Genevestigator; Q9JHL1; -.
DR   GermOnline; ENSMUSG00000002504; Mus musculus.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   InterPro; IPR015098; EBP50_C-term.
DR   InterPro; IPR017300; NaH_exchngr_reg_CF_NHE-RF.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF09007; EBP50_C-term; 1.
DR   Pfam; PF00595; PDZ; 2.
DR   PIRSF; PIRSF037866; EBP50; 1.
DR   ProDom; PD283022; EBP50_C-term; 1.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; PDZ; 2.
DR   PROSITE; PS50106; PDZ; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell membrane; Membrane; Nucleus;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1    337       Na(+)/H(+) exchange regulatory cofactor
FT                                NHE-RF2.
FT                                /FTId=PRO_0000096806.
FT   DOMAIN       11     91       PDZ 1.
FT   DOMAIN      151    231       PDZ 2.
FT   MOD_RES     183    183       Phosphoserine (By similarity).
FT   MOD_RES     254    254       Phosphoserine (By similarity).
FT   MOD_RES     272    272       Phosphoserine.
FT   MOD_RES     275    275       Phosphoserine (By similarity).
FT   VAR_SEQ       1    111       Missing (in isoform 2).
FT                                /FTId=VSP_009379.
FT   VAR_SEQ     112    138       LPPAHNPWEPKPDWACSGSLGSDTGQK -> MARSRTSMLP
FT                                ASAPGAPPVNSQLGLTQ (in isoform 2).
FT                                /FTId=VSP_009380.
FT   CONFLICT      4      4       P -> L (in Ref. 2; BAC30366/BAC35980/
FT                                BAC39282).
FT   CONFLICT    143    143       P -> S (in Ref. 1; BAA97568/BAA97569 and
FT                                2; BAE41537).
FT   CONFLICT    242    242       V -> I (in Ref. 2; BAC30366/BAC35980/
FT                                BAC39282 and 3; AAH65778).
FT   CONFLICT    326    326       D -> A (in Ref. 2; BAB22185).
FT   HELIX       327    336
SQ   SEQUENCE   337 AA;  37403 MW;  A28ED245DE453A5F CRC64;
     MAAPESLRPR LCRLVRGEQG YGFHLHGEKG RRGQFIRRVE PGSPAEAAAL RAGDRLVEVN
     GVNVEGETHH QVVQRIKAVE GQTQLLVVDK ETDEELCRRQ LTCTEEMAHR GLPPAHNPWE
     PKPDWACSGS LGSDTGQKDV NGPPRELRPR LCHLRRGPQG YGFNLHSDKS RPGQYIRSVD
     PGSPASHSGL RAQDRLIEVN GQNVEGLRHA EVVARIKAQE DEARLLVVDP ETDEHFKRLR
     VVPTEEHVEG PLPSPVTNGT SPAQLNGGSV CSSRSDLPGS EKDNEDGSTW KRDPFQESGL
     HLSPTAAEAK EKARATRVNK RAPQMDWNRK REIFSNF
//
ID   PALMD_MOUSE             Reviewed;         551 AA.
AC   Q9JHU2; Q3TAG0; Q91X00; Q9D693;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=Palmdelphin;
GN   Name=Palmd;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   MEDLINE=21564168; PubMed=11707320; DOI=10.1016/S0378-1119(01)00719-3;
RA   Andreu N., Escarceller M., Feather S., Devriendt K., Wolf A.S.,
RA   Estivill X., Sumoy L.;
RT   "PALML, a novel paralemmin-related gene mapping on human chromosome
RT   1p21.";
RL   Gene 278:33-40(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Muscle;
RX   MEDLINE=21371761; PubMed=11478809; DOI=10.1006/bbrc.2001.5329;
RA   Hu B., Copeland N.G., Gilbert D.J., Jenkins N.A., Kilimann M.W.;
RT   "The paralemmin protein family: identification of paralemmin-2, an
RT   isoform differentially spliced to AKAP2/AKAP-KL, and of palmdelphin, a
RT   more distant cytosolic relative.";
RL   Biochem. Biophys. Res. Commun. 285:1369-1376(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   The European IMAGE consortium;
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Skin, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-375 AND
RP   SER-385, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at highest levels in the
CC       heart and lung.
CC   -!- SIMILARITY: Belongs to the paralemmin family.
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DR   EMBL; AF263246; AAK48507.1; -; mRNA.
DR   EMBL; AJ312215; CAC59696.1; -; mRNA.
DR   EMBL; AL391037; CAC01530.1; -; mRNA.
DR   EMBL; AK014531; BAB29414.1; -; mRNA.
DR   EMBL; AK171869; BAE42708.1; -; mRNA.
DR   EMBL; BC010193; AAH10193.1; -; mRNA.
DR   IPI; IPI00314152; -.
DR   RefSeq; NP_075734.3; NM_023245.3.
DR   UniGene; Mm.253736; -.
DR   STRING; Q9JHU2; -.
DR   PhosphoSite; Q9JHU2; -.
DR   PRIDE; Q9JHU2; -.
DR   Ensembl; ENSMUST00000040097; ENSMUSP00000044693; ENSMUSG00000033377.
DR   GeneID; 114301; -.
DR   KEGG; mmu:114301; -.
DR   CTD; 114301; -.
DR   MGI; MGI:2148896; Palmd.
DR   eggNOG; roNOG12348; -.
DR   GeneTree; ENSGT00530000063206; -.
DR   HOGENOM; HBG280401; -.
DR   HOVERGEN; HBG082103; -.
DR   InParanoid; Q9JHU2; -.
DR   OrthoDB; EOG49W2F8; -.
DR   NextBio; 368337; -.
DR   ArrayExpress; Q9JHU2; -.
DR   Bgee; Q9JHU2; -.
DR   CleanEx; MM_PALMD; -.
DR   Genevestigator; Q9JHU2; -.
DR   GermOnline; ENSMUSG00000033377; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:InterPro.
DR   InterPro; IPR004965; Paralemmin.
DR   Pfam; PF03285; Paralemmin; 2.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Phosphoprotein.
FT   CHAIN         1    551       Palmdelphin.
FT                                /FTId=PRO_0000262529.
FT   COILED       12    106       Potential.
FT   MOD_RES     135    135       Phosphoserine (By similarity).
FT   MOD_RES     321    321       Phosphoserine (By similarity).
FT   MOD_RES     370    370       Phosphoserine.
FT   MOD_RES     375    375       Phosphoserine.
FT   MOD_RES     385    385       Phosphoserine.
FT   MOD_RES     515    515       Phosphoserine (By similarity).
FT   CONFLICT     65     65       R -> K (in Ref. 2; CAC59696 and 4;
FT                                BAB29414/BAE42708).
FT   CONFLICT    144    144       P -> H (in Ref. 4; BAB29414).
FT   CONFLICT    395    395       V -> I (in Ref. 4; BAE42708).
FT   CONFLICT    470    470       N -> S (in Ref. 2; CAC59696 and 4;
FT                                BAB29414/BAE42708).
SQ   SEQUENCE   551 AA;  62700 MW;  F4AE52C14BC2582C CRC64;
     MEEAELVKGR LQAITDKRKI QEEISQKRLK IEEEKLKHQH LKKKALREKW LLDGIGSGKE
     HEEMRKQNQQ DQHQTQVLEQ SILRLEKEIQ DLEKAELQIS ANEEAILKKL KSIEKTTEDI
     IRSVKVEKEE NPEESIEDIY ANIPDLPSSY IPSRLRKERN EGPDDEQNRK ALYAMEIKVE
     KDLKTGESVV LSSIPLPSDD FKSTGIKVYE DRQKSVYAVS SNQNTTYNGT DGLAPVEVED
     LLRQASERNS KSPTEYHEPV YANPFCRPVT PQRERVISPG PNFQERIMMK TNGLGNHANE
     SAHNMTDGLS ERRSNGPTHT SPTRPTPQPR SMVQQVEEMV HTQQKRMASP WEESSNRQNE
     HEVSPRMELS PSRASPGKSG PQCSSPTCQE ETEDVRYNIV HSLPSDVDDT EPVTMIFMGY
     QQADDNEEEK KLLTGYDGVI HAELVVIDDE AEDNEGQTER PSYHPVAPYN QVYQPPKPTP
     LPRKRAEVRP YENTNHKSPH KNSISLKEQE ERLGSPARHS PLDVPVAGDG TEDPSLTALR
     IRMAKLGKKV I
//
ID   DYHC1_MOUSE             Reviewed;        4644 AA.
AC   Q9JHU4;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Cytoplasmic dynein 1 heavy chain 1;
DE   AltName: Full=Cytoplasmic dynein heavy chain 1;
DE   AltName: Full=Dynein heavy chain, cytosolic;
GN   Name=Dync1h1; Synonyms=Dhc1, Dnch1, Dnchc1, Dyhc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=FVB;
RA   Sasaki S., Shionoya A., Hirotsune S.;
RT   "Complete cDNA sequence of murine cytoplasmic dynein heavy chain.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-3377, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4216 AND THR-4219, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   VARIANT LOA TYR-580, AND VARIANT CRA1 CYS-1055.
RX   MEDLINE=22616479; PubMed=12730604; DOI=10.1126/science.1083129;
RA   Hafezparast M., Klocke R., Ruhrberg C., Marquardt A., Ahmad-Annuar A.,
RA   Bowen S., Lalli G., Witherden A.S., Hummerich H., Nicholson S.,
RA   Morgan P.J., Oozageer R., Priestley J.V., Averill S., King V.R.,
RA   Ball S., Peters J., Toda T., Yamamoto A., Hiraoka Y., Augustin M.,
RA   Korthaus D., Wattler S., Wabnitz P., Dickneite C., Lampel S.,
RA   Boehme F., Peraus G., Popp A., Rudelius M., Schlegel J., Fuchs H.,
RA   de Angelis M.H., Schiavo G., Shima D.T., Russ A.P., Stumm G.,
RA   Martin J.E., Fisher E.M.C.;
RT   "Mutations in dynein link motor neuron degeneration to defects in
RT   retrograde transport.";
RL   Science 300:808-812(2003).
CC   -!- FUNCTION: Cytoplasmic dynein 1 acts as a motor for the
CC       intracellular retrograde motility of vesicles and organelles along
CC       microtubules. Dynein has ATPase activity; the force-producing
CC       power stroke is thought to occur on release of ADP.
CC   -!- SUBUNIT: Homodimer. The cytoplasmic dynein 1 complex consists of
CC       two catalytic heavy chains (HCs) and a number of non-catalytic
CC       subunits presented by intermediate chains (ICs), light
CC       intermediate chains (LICs) and light chains (LCs); the composition
CC       seems to vary in respect to the IC, LIC and LC composition. The
CC       heavy chain homodimer serves as a scaffold for the probable
CC       homodimeric assembly of the respective non-catalytic subunits. The
CC       ICs and LICs bind directly to the HC dimer and dynein LCs assemble
CC       on the IC dimer. Interacts with DYNC1LI1; DYNC1LI1 and DYNC1LI2
CC       bind mutually exclusive to DYNC1H1. Interacts with DYNC1LI2;
CC       DYNC1LI1 and DYNC1LI2 bind mutually exclusive to DYNC1H1.
CC       Interacts with DYNC1I2 (By similarity).
CC   -!- INTERACTION:
CC       P07141:Csf1; NbExp=1; IntAct=EBI-645061, EBI-777188;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- DOMAIN: Dynein heavy chains probably consist of an N-terminal stem
CC       (which binds cargo and interacts with other dynein components),
CC       and the head or motor domain. The motor contains six tandemly-
CC       linked AAA domains in the head, which form a ring. A stalk-like
CC       structure (formed by two of the coiled coil domains) protrudes
CC       between AAA 4 and AAA 5 and terminates in a microtubule-binding
CC       site. A seventh domain may also contribute to this ring; it is not
CC       clear whether the N-terminus or the C-terminus forms this extra
CC       domain. There are four well-conserved and two non-conserved ATPase
CC       sites, one per AAA domain. Probably only one of these (within AAA
CC       1) actually hydrolyzes ATP, the others may serve a regulatory
CC       function.
CC   -!- DISEASE: Note=Defects in Dync1h1 are the cause of the 'Legs at odd
CC       angles' (LOA) phenotype, an autosomal dominant trait where
CC       affected animals display unusual twisting of the body and
CC       clenching of the hindlimbs when suspended by the tail.
CC       Heterozygotes suffer age-related progressive loss of muscle tone
CC       and locomotor ability without major reduction in life-span while
CC       homozygotes show a more severe phenotype with an inability to move
CC       or feed, and die within 24 hours of birth. LOA mutants display
CC       defects in migration of facial motor neuron cell bodies and
CC       impaired retrograde transport in spinal cord motor neurons.
CC   -!- DISEASE: Note=Defects in Dync1h1 are the cause of the Cramping 1
CC       (Cra1) phenotype, an autosomal dominant trait where affected
CC       animals display unusual twisting of the body and clenching of the
CC       hindlimbs when suspended by the tail. Heterozygotes suffer age-
CC       related progressive loss of muscle tone and locomotor ability
CC       without major reduction in life-span while homozygotes show a more
CC       severe phenotype with an inability to move or feed, and die within
CC       24 hours of birth.
CC   -!- SIMILARITY: Belongs to the dynein heavy chain family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AY004877; AAF91078.1; -; mRNA.
DR   IPI; IPI00119876; -.
DR   UniGene; Mm.181430; -.
DR   PDB; 3ERR; X-ray; 2.27 A; A/B=3260-3427.
DR   PDBsum; 3ERR; -.
DR   ProteinModelPortal; Q9JHU4; -.
DR   SMR; Q9JHU4; 1903-1961, 2213-2241, 2589-2625, 2924-3000, 3227-3435.
DR   IntAct; Q9JHU4; 17.
DR   STRING; Q9JHU4; -.
DR   PhosphoSite; Q9JHU4; -.
DR   PRIDE; Q9JHU4; -.
DR   Ensembl; ENSMUST00000018851; ENSMUSP00000018851; ENSMUSG00000018707.
DR   UCSC; uc007pbo.1; mouse.
DR   MGI; MGI:103147; Dync1h1.
DR   GeneTree; ENSGT00600000084413; -.
DR   HOGENOM; HBG358329; -.
DR   HOVERGEN; HBG096595; -.
DR   InParanoid; Q9JHU4; -.
DR   OrthoDB; EOG4P5K86; -.
DR   PhylomeDB; Q9JHU4; -.
DR   ArrayExpress; Q9JHU4; -.
DR   Bgee; Q9JHU4; -.
DR   CleanEx; MM_DYNC1H1; -.
DR   Genevestigator; Q9JHU4; -.
DR   GermOnline; ENSMUSG00000018707; Mus musculus.
DR   GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0033962; P:cytoplasmic mRNA processing body assembly; IMP:BHF-UCL.
DR   GO; GO:0034063; P:stress granule assembly; IMP:BHF-UCL.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR011704; ATPase_AAA-5.
DR   InterPro; IPR004273; Dynein_heavy.
DR   InterPro; IPR013594; Dynein_heavy_N-1.
DR   InterPro; IPR013602; Dynein_heavy_N-2.
DR   Pfam; PF07728; AAA_5; 2.
DR   Pfam; PF08385; DHC_N1; 1.
DR   Pfam; PF08393; DHC_N2; 1.
DR   Pfam; PF03028; Dynein_heavy; 1.
DR   SMART; SM00382; AAA; 4.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Disease mutation; Dynein; Microtubule; Motor protein;
KW   Nucleotide-binding; Phosphoprotein; Repeat; Transport.
FT   CHAIN         1   4644       Cytoplasmic dynein 1 heavy chain 1.
FT                                /FTId=PRO_0000114628.
FT   NP_BIND    1904   1911       ATP (Potential).
FT   NP_BIND    2222   2229       ATP (Potential).
FT   NP_BIND    2593   2600       ATP (Potential).
FT   NP_BIND    2935   2942       ATP (Potential).
FT   REGION        1   1865       Stem (By similarity).
FT   REGION      446    701       Interaction with DYNC1I2 (By similarity).
FT   REGION      649    800       Interaction with DYNC1LI2 (By
FT                                similarity).
FT   REGION     1866   2097       AAA 1 (By similarity).
FT   REGION     2178   2450       AAA 2 (By similarity).
FT   REGION     2554   2803       AAA 3 (By similarity).
FT   REGION     2897   3166       AAA 4 (By similarity).
FT   REGION     3187   3498       Stalk (By similarity).
FT   REGION     3551   3780       AAA 5 (By similarity).
FT   REGION     4003   4219       AAA 6 (By similarity).
FT   COILED       48     69       Potential.
FT   COILED      179    200       Potential.
FT   COILED      453    476       Potential.
FT   COILED      541    564       Potential.
FT   COILED     1169   1201       Potential.
FT   COILED     1229   1250       Potential.
FT   COILED     1355   1371       Potential.
FT   COILED     3187   3273       Potential.
FT   COILED     3394   3498       Potential.
FT   COILED     3735   3798       Potential.
FT   MOD_RES     369    369       N6-acetyllysine (By similarity).
FT   MOD_RES     392    392       N6-acetyllysine (By similarity).
FT   MOD_RES     752    752       N6-acetyllysine (By similarity).
FT   MOD_RES    1123   1123       N6-acetyllysine (By similarity).
FT   MOD_RES    2408   2408       Phosphoserine (By similarity).
FT   MOD_RES    2759   2759       Phosphoserine (By similarity).
FT   MOD_RES    3377   3377       Phosphotyrosine.
FT   MOD_RES    3478   3478       N6-acetyllysine (By similarity).
FT   MOD_RES    4216   4216       Phosphothreonine.
FT   MOD_RES    4219   4219       Phosphothreonine.
FT   MOD_RES    4281   4281       N6-acetyllysine (By similarity).
FT   MOD_RES    4366   4366       Phosphoserine (By similarity).
FT   VARIANT     580    580       F -> Y (in LOA).
FT   VARIANT    1055   1055       Y -> C (in CRA1).
FT   HELIX      3260   3295
FT   HELIX      3299   3306
FT   HELIX      3313   3325
FT   HELIX      3333   3336
FT   HELIX      3339   3341
FT   HELIX      3345   3351
FT   HELIX      3354   3356
FT   HELIX      3359   3368
FT   TURN       3369   3371
FT   HELIX      3377   3383
FT   HELIX      3390   3427
SQ   SEQUENCE   4644 AA;  532025 MW;  FE5B4E15DD479E1B CRC64;
     MSEPGGGEDG SAGLEVSAVQ NVADVAVLQK HLRKLVPLLL EDGGDAPAAL EAALEEKSAL
     EQMRKFLSDP QVHTVLVERS TLKEDVGDEG EEEKEFISYN INIDIHYGVK SNSLAFIKRA
     PVIDADKPVS SQLRVLTLSE DSPYETLHSF ISNAVAPFFK SYIRESGKAD RDGDKMAPSV
     EKKIAELEMG LLHLQQNIEI PEISLPIHPI ITNVAKQCYE RGEKPKVTDF GDKVEDPTFL
     NQLQSGVNRW IREIQKVTKL DRDPASGTAL QEISFWLNLE RALYRIQEKR ESPEVLLTLD
     ILKHGKRFHA TVSFDTDTGL KQALETVNDY NPLMKDFPLN DLLSATELDK IRQALVAIFT
     HLRKIRNTKY PIQRALRLVE AISRDLSSQL LKVLGTRKLM HVAYEEFEKV MVACFEVFQT
     WDDEYEKLQV LLRDIVKRKR EENLKMVWRI NPAHRKLQAR LDQMRKFRRQ HEQLRAVIVR
     VLRPQVTAVA QQNQGEAPEP QDMKVAEVLF DAADANTIEE VNLAYENVKE VDGLDVSKEG
     TEAWEAAMKR YDERIDRVET RITARLRDQL GTAKNANEMF RIFSRFNALF VRPHIRGAIR
     EYQTQLIQRV KDDIESLHDK FKVQYPQSQA CKMSHVRDLP PVSGSIIWAK QIDRQLTAYM
     KRVEDVLGKG WENHVEGQKL KQDGDSFRMK LNTQEIFDDW ARKVQQRNLG VSGRIFTIES
     ARVRGRTGNV LKLKVNFLPE IITLSKEVRN LKWLGFRVPL AIVNKAHQAN QLYPFAISLI
     ESVRTYERTC EKVEERNTIS LLVAGLKKEV QALIAEGIAL VWESYKLDPY VQRLAETVFN
     FQEKVDDLLI IEEKIDLEVR SLETCMYDHK TFSEILNRVQ KAVDDLNLHS YSNLPIWVNK
     LDMEIERILG VRLQAGLRAW TQVLLGQAED KAEVDMDTDA PQVSHKPGGE PKIKNVVHEL
     RITNQVIYLN PPIEECRYKL YQEMFAWKMV VLSLPRIQSQ RYQVGVHYEL TEEEKFYRNA
     LTRMPDGPVA LEESYSAVMG IVTEVEQYVK VWLQYQCLWD MQAENIYNRL GEDLNKWQAL
     LVQIRKARGT FDNAETKKEF GPVVIDYGKV QSKVNLKYDS WHKEVLSKFG QMLGSNMTEF
     HSQISKSRQE LEQHSVDTAS TSDAVTFITY VQSLKRKIKQ FEKQVELYRN GQRLLEKQRF
     QFPPSWLYID NIEGEWGAFN DIMRRKDSAI QQQVANLQMK IVQEDRAVES RTTDLLTDWE
     KTKPVTGNLR PEEALQALTI YEGKFGRLKD DREKCAKAKE ALELTDTGLL SGSEERVQVA
     LEELQDLKGV WSELSKVWEQ IDQMKEQPWV SVQPRKLRQN LDGLLNQLKN FPARLRQYAS
     YEFVQRLLKG YMKINMLVIE LKSEALKDRH WKQLMKRLHV NWVVSELTLG QIWDVDLQKN
     EAVVKDVLLV AQGEMALEEF LKQIREVWNT YELDLVNYQN KCRLIRGWDD LFNKVKEHIN
     SVSAMKLSPY YKVFEEDALS WEDKLNRIMA LFDVWIDVQR RWVYLEGIFT GSADIKHLLP
     VETQRFQSIS TEFLALMKKV SKSPLVMDVL NIQGVQRSLE RLADLLGKIQ KALGEYLERE
     RSSFPRFYFV GDEDLLEIIG NSKNVAKLQK HFKKMFAGVS SIILNEDNSV VLGISSREGE
     EVMFKTPVSI TEHPKINEWL TLVEKEMRVT LAKLLAESVT EVEIFGKATS IDPNTYITWI
     DKYQAQLVVL SAQIAWSENV ENALSNVGGG GDVGPLQSVL SNVEVTLNVL ADSVLMEQPP
     LRRRKLEHLI TELVHQRDVT RSLIKSKIDN AKSFEWLSQM RFYFDPKQTD VLQQLSIQMA
     NAKFNYGFEY LGVQDKLVQT PLTDRCYLTM TQALEARLGG SPFGPAGTGK TESVKALGHQ
     LGRFVLVFNC DETFDFQAMG RIFVGLCQVG AWGCFDEFNR LEERMLSAVS QQVQCIQEAL
     REHSNPNYDK TSAPITCELL NKQVKVSPDM AIFITMNPGY AGRSNLPDNL KKLFRSLAMT
     KPDRQLIAQV MLYSQGFRTA EVLANKIVPF FKLCDEQLSS QSHYDFGLRA LKSVLVSAGN
     VKRERIQKIK REKEERGEAV DEGEIAENLP EQEILIQSVC ETMVPKLVAE DIPLLFSLLS
     DVFPGVQYHR GEMTALREEL KKVCQEMYLT YGDGEEVGGM WVEKVLQLYQ ITQINHGLMM
     VGPSGSGKSM AWRVLLKALE RLEGVEGVAH IIDPKAISKD HLYGTLDPNT REWTDGLFTH
     VLRKIIDNVR GELQKRQWIV FDGDVDPEWV ENLNSVLDDN KLLTLPNGER LSLPPNVRIM
     FEVQDLKYAT LATVSRCGMV WFSEDVLSTD MILNNFLARL RSIPLDEGED EAQRRRKGKE
     DEGEEAASPM LQIQRDAATI MQPYFTSNGL VTKALEHAFK LEHIMDLTRL RCLGSLFSML
     HQACRNVAQY NANHPDFPMQ IEQLERYIQR YLVYAILWSL SGDSRLKMRA ELGEYIRRIT
     TVPLPTAPNV PIIDYEVSIS GEWSPWQAKV PQIEVETHKV AAPDVVVPTL DTVRHEALLY
     TWLAEHKPLV LCGPPGSGKT MTLFSALRAL PDMEVVGLNF SSATTPELLL KTFDHYCEYR
     RTPNGVVLAP VQLGKWLVLF CDEINLPDMD KYGTQRVISF IRQMVEHGAF YRTSDQTWVK
     LERIQFVGAC NPPTDPGRKP LSHRFLRHVP VVYVDYPGPA SLTQIYGTFN RAMLRLIPSL
     RTYAEPLTAA MVEFYTMSQE RFTQDTQPHY IYSPREMTRW VRGIFEALRP LETLPVEGLI
     RIWAHEALRL FQDRLVEDEE RRWTDENIDM VALKHFPNID KEKAMSRPIL YSNWLSKDYI
     PVDQEELRDY VKARLKVFYE EELDVPLVLF NEVLDHVLRI DRIFRQPQGH LLLIGVSGAG
     KTTLSRFVAW MNGLSVYQIK VHRKYTGEDF DEDLRTVLRR SGCKNEKIAF IMDESNVLDS
     GFLERMNTLL ANGEVPGLFE GDEYATLMTQ CKEGAQKEGL MLDSHEELYK WFTSQVIRNL
     HVVFTMNPSS EGLKDRAATS PALFNRCVLN WFGDWSTEAL YQVGKEFTSK MDLEKPNYIV
     PDYMPVVYDK LPQPPTHREA IVNSCVFVHQ TLHQANARLA KRGGRTMAIT PRHYLDFINH
     YANLFHEKRS ELEEQQMHLN VGLRKIKETV DQVEELRRDL RIKSQELEVK NAAANDKLKK
     MVKDQQEAEK KKVMSQEIQE QLHKQQEVIA DKQMSVKEDL DKVEPAVIEA QNAVKSIKKQ
     HLVEVRSMAN PPAAVKLALE SICLLLGEST TDWKQIRSII MRENFIPTIV NFSAEEISDA
     IREKMKKNYM SNPSYNYEIV NRASLACGPM VKWAIAQLNY ADMLKRVEPL RNELQKLEDD
     AKDNQQKANE VEQMIRDLEA SIARYKEEYA VLISEAQAIK ADLAAVEAKV NRSTALLKSL
     SAERERWEKT SETFKNQMST IAGDCLLSAA FIAYAGYFDQ QMRQNLFTTW SHHLQQANIQ
     FRTDIARTEY LSNADERLRW QASSLPADDL CTENAIMLKR FNRYPLIIDP SGQATEFIMN
     EYKDRKITRT SFLDDAFRKN LESALRFGNP LLVQDVESYD PVLNPVLNRE VRRTGGRVLI
     TLGDQDIDLS PSFVIFLSTR DPTVEFPPDL CSRVTFVNFT VTRSSLQSQC LNEVLKAERP
     DVDEKRSDLL KLQGEFQLRL RQLEKSLLQA LNEVKGRILV DDTIITTLEN LKREAAEVTR
     KVEETDIVMQ EVETVSQQYL PLSTACSSIY FTMESLKQVH FLYQYSLQFF LDIYHNVLYE
     NPNLKGATDH TQRLSVITKD LFQVAFNRVA RGMLHQDHIT FAMLLARIKL KGTVGEPTYD
     AEFQHFLRGK EIVLSAGSTP KIQGLTVEQA EAVVRLSCLP AFKDLIAKVQ ADEQFGIWLD
     SSSPEQTVPY LWSEETPTTP IGQAIHRLLL IQAFRPDRLL AMAHMFVSTN LGESFMSIME
     QPLDLTHIVG TEVKPNTPVL MCSVPGYDAS GHVEDLAAEQ NTQITSIAIG SAEGFNQADK
     AINTAVKSGR WVMLKNVHLA PGWLMQLEKK LHSLQPHACF RLFLTMEINP KVPVNLLRAG
     RIFVFEPPPG VKANMLRTFS SIPVSRICKS PNERARLYFL LAWFHAIIQE RLRYAPLGWS
     KKYEFGESDL RSACDTVDTW LDDTAKGRQN ISPDKIPWSA LKTLMAQSIY GGRVDNEFDQ
     RLLNTFLERL FTTRSFDSEF KLACKVDGHK DIQMPDGIRR EEFVQWVELL PDAQTPSWLG
     LPNNAERVLL TTQGVDMISK MLKMQMLEDE DDLAYAETEK KARTDSTSDG RPAWMRTLHT
     TASNWLHLIP QTLSPLKRTV ENIKDPLFRF FEREVKMGAK LLQDVRQDLA DVVQVCEGKK
     KQTNYLRTLI NELVKGILPR SWSHYTVPAG MTVIQWVSDF SERIKQLQNI SQAAASGGAK
     ELKNIHVCLG GLFVPEAYIT ATRQYVAQAN SWSLEELCLE VNVTASQSAT LDACSFGVTG
     LKLQGATCSN NKLSLSNAIS TVLPLTQLRW VKQTSAEKKA SVVTLPVYLN FTRADLIFTV
     DFEIATKEDP RSFYERGVAV LCTE
//
ID   INO1_MOUSE              Reviewed;         557 AA.
AC   Q9JHU9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Inositol-3-phosphate synthase 1;
DE            Short=IPS 1;
DE            EC=5.5.1.4;
DE   AltName: Full=Myo-inositol-1-phosphate synthase;
DE            Short=MI-1-P synthase;
DE            Short=MIP synthase;
GN   Name=Isyna1; Synonyms=Ino1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=17121280;
RA   Parthasarathy L.K., Seelan R.S., Tobias C., Casanova M.F.,
RA   Parthasarathy R.N.;
RT   "Mammalian inositol 3-phosphate synthase: its role in the biosynthesis
RT   of brain inositol and its clinical use as a psychoactive agent.";
RL   Subcell. Biochem. 39:293-314(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=14613899; DOI=10.1095/biolreprod.103.022731;
RA   Chauvin T.R., Griswold M.D.;
RT   "Characterization of the expression and regulation of genes necessary
RT   for myo-inositol biosynthesis and transport in the seminiferous
RT   epithelium.";
RL   Biol. Reprod. 70:744-751(2004).
CC   -!- FUNCTION: Key enzyme in myo-inositol biosynthesis pathway that
CC       catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol
CC       1-phosphate in a NAD-dependent manner. Rate-limiting enzyme in the
CC       synthesis of all inositol-containing compounds (By similarity).
CC   -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate = 1D-myo-inositol 3-
CC       phosphate.
CC   -!- COFACTOR: NAD (By similarity).
CC   -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-
CC       inositol from D-glucose 6-phosphate: step 1/2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: In testis, it is expressed in Sertoli cells.
CC       Highly expressed in 2 types of germ cells, pachytene spermatocytes
CC       and round spermatids.
CC   -!- SIMILARITY: Belongs to the myo-inositol-1-phosphate synthase
CC       family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF288525; AAF90201.1; -; mRNA.
DR   EMBL; AK005029; BAB23756.1; -; mRNA.
DR   EMBL; AK079323; BAC37607.1; -; mRNA.
DR   EMBL; BC003458; AAH03458.1; -; mRNA.
DR   IPI; IPI00119886; -.
DR   RefSeq; NP_076116.1; NM_023627.1.
DR   UniGene; Mm.29357; -.
DR   HSSP; P11986; 1P1H.
DR   ProteinModelPortal; Q9JHU9; -.
DR   SMR; Q9JHU9; 5-513.
DR   STRING; Q9JHU9; -.
DR   REPRODUCTION-2DPAGE; IPI00119886; -.
DR   REPRODUCTION-2DPAGE; Q9JHU9; -.
DR   PRIDE; Q9JHU9; -.
DR   Ensembl; ENSMUST00000019283; ENSMUSP00000019283; ENSMUSG00000019139.
DR   GeneID; 71780; -.
DR   KEGG; mmu:71780; -.
DR   UCSC; uc009mav.1; mouse.
DR   CTD; 71780; -.
DR   MGI; MGI:1919030; Isyna1.
DR   eggNOG; maNOG17194; -.
DR   GeneTree; ENSGT00390000018395; -.
DR   HOGENOM; HBG316335; -.
DR   HOVERGEN; HBG061200; -.
DR   InParanoid; Q9JHU9; -.
DR   OMA; NPVLYAP; -.
DR   OrthoDB; EOG44F68X; -.
DR   PhylomeDB; Q9JHU9; -.
DR   BRENDA; 5.5.1.4; 244.
DR   NextBio; 334505; -.
DR   ArrayExpress; Q9JHU9; -.
DR   Bgee; Q9JHU9; -.
DR   CleanEx; MM_ISYNA1; -.
DR   Genevestigator; Q9JHU9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0004512; F:inositol-3-phosphate synthase activity; IEA:EC.
DR   GO; GO:0006021; P:inositol biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002587; Myo-inos-1-P_Synthase.
DR   InterPro; IPR013021; Myo-inos-1-P_Synthase_GAPDH.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 2.
DR   PANTHER; PTHR11510; Inos-1-P_synth; 1.
DR   Pfam; PF01658; Inos-1-P_synth; 1.
DR   Pfam; PF07994; NAD_binding_5; 1.
DR   PIRSF; PIRSF015578; Myoinos-ppht_syn; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Inositol biosynthesis; Isomerase; NAD;
KW   Phospholipid biosynthesis.
FT   CHAIN         1    557       Inositol-3-phosphate synthase 1.
FT                                /FTId=PRO_0000324630.
SQ   SEQUENCE   557 AA;  60932 MW;  91166BD2A2C53ADA CRC64;
     MEPAAEILVD SPDVVYSPET IEARYEYRTT RVSREGGVLR VQPRATRFTF RTARQVPRLG
     VMLVGWGGNN GSTLTAAVLA NRLRLTWPTR TGRKEANYYG SLTQAGTVNL GLDENGREVF
     VPFSALLPMV APNDLVFDGW DISSLNLAEA MRRAQVLDCG LQEQLWPHME SLRPRPSVYI
     PEFIAANQTA RADNLIPGTR AQQLEQIRKD IRDFRSSAGL DKVIVLWTAN TERFCEVVPG
     RNDTAENLLH TIQLGLEVSP STLFAVASIL EDCAFLNGSP QNTLVPGALE LASQRHVFVG
     GDDFKSGQTK VKSVLVDFLI GSGLKTMSIV SYNHLGNNDG QNLSAPLQFR SKEVTKSSVV
     DDMVHSNHVL YAPGERPDHC VVIKYVPYVG DSKRALDEYT SELMLGGTNT LVLHNTCEDS
     LLAAPIMLDL VLLTELCQRV SFCTDSDPEP QGFHTVLSLL SFLFKAPLVP PGSPVVNALF
     RQRSCIENIF RACVGLPPQN HMLLEHKMER PGPGIKPGEV VATSPLPCKK EPTPATNGCT
     GDANGHPQAP TPKLSTA
//
ID   STK4_MOUSE              Reviewed;         487 AA.
AC   Q9JI11;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Serine/threonine-protein kinase 4;
DE            EC=2.7.11.1;
DE   AltName: Full=Mammalian STE20-like protein kinase 1;
DE            Short=MST-1;
DE   AltName: Full=STE20-like kinase MST1;
GN   Name=Stk4; Synonyms=Mst1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RX   MEDLINE=21276425; PubMed=11278283; DOI=10.1074/jbc.M005109200;
RA   Lee K.-K., Ohyama T., Yajima N., Tsubuki S., Yonehara S.;
RT   "MST, a physiological caspase substrate, highly sensitizes apoptosis
RT   both upstream and downstream of caspase activation.";
RL   J. Biol. Chem. 276:19276-19285(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-433, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=20080689; DOI=10.1073/pnas.0911427107;
RA   Lu L., Li Y., Kim S.M., Bossuyt W., Liu P., Qiu Q., Wang Y.,
RA   Halder G., Finegold M.J., Lee J.S., Johnson R.L.;
RT   "Hippo signaling is a potent in vivo growth and tumor suppressor
RT   pathway in the mammalian liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:1437-1442(2010).
CC   -!- FUNCTION: Stress-activated, pro-apoptotic kinase which, following
CC       caspase-cleavage, enters the nucleus and induces chromatin
CC       condensation followed by internucleosomal DNA fragmentation. Key
CC       component of the Hippo signaling pathway which plays a pivotal
CC       role in organ size control and tumor suppression by restricting
CC       proliferation and promoting apoptosis. The core of this pathway is
CC       composed of a kinase cascade wherein MST1/MST2, in complex with
CC       its regulatory protein SAV1, phosphorylates and activates LATS1/2
CC       in complex with its regulatory protein MOB1, which in turn
CC       phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ.
CC       Phosphorylation of YAP1 by LATS2 inhibits its translocation into
CC       the nucleus to regulate cellular genes important for cell
CC       proliferation, cell death, and cell migration. MST1/MST2 are
CC       required to repress proliferation of mature hepatocytes, to
CC       prevent activation of facultative adult liver stem cells (oval
CC       cells), and to inhibit tumor formation. Phosphorylates 'Ser-14' of
CC       histone H2B (H2BS14ph) during apoptosis. Phosphorylates FOXO3 upon
CC       oxidative stress, which results in its nuclear translocation and
CC       cell death initiation.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Inhibited by the C-terminal non-catalytic
CC       region. Activated by caspase-cleavage. Full activation also
CC       requires homodimerization and autophosphorylation of Thr-183 (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer; mediated via the coiled-coil region. Interacts
CC       with NORE1, which inhibits autoactivation. Interacts with and
CC       stabilizes SAV1. Interacts with RASSF1, which leads to enzyme
CC       activation. Interacts with FOXO3 (By similarity).
CC   -!- INTERACTION:
CC       Q5EBH1:Rassf5; NbExp=1; IntAct=EBI-1181352, EBI-960530;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=The caspase-cleaved form cycles between nucleus
CC       and cytoplasm (By similarity).
CC   -!- PTM: Autophosphorylated on Thr-183 (By similarity).
CC   -!- PTM: Proteolytically cleaved by caspase during apoptosis (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice show progressive hepatomegaly with a 2-
CC       fold increase in liver mass relative to total body mass at 1 month
CC       of age and a 3-fold increase by 3 months of age.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 SARAH domain.
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DR   EMBL; AF271360; AAF75789.1; -; mRNA.
DR   EMBL; AK028838; BAC26147.1; -; mRNA.
DR   EMBL; BC054521; AAH54521.1; -; mRNA.
DR   IPI; IPI00119772; -.
DR   RefSeq; NP_067395.1; NM_021420.3.
DR   UniGene; Mm.479158; -.
DR   ProteinModelPortal; Q9JI11; -.
DR   SMR; Q9JI11; 16-300, 432-480.
DR   IntAct; Q9JI11; 4.
DR   STRING; Q9JI11; -.
DR   PhosphoSite; Q9JI11; -.
DR   PRIDE; Q9JI11; -.
DR   Ensembl; ENSMUST00000018353; ENSMUSP00000018353; ENSMUSG00000018209.
DR   GeneID; 58231; -.
DR   KEGG; mmu:58231; -.
DR   UCSC; uc008ntt.1; mouse.
DR   CTD; 58231; -.
DR   MGI; MGI:1929004; Stk4.
DR   GeneTree; ENSGT00600000084209; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108518; -.
DR   InParanoid; Q9JI11; -.
DR   OMA; KRRDETM; -.
DR   OrthoDB; EOG4N30P2; -.
DR   PhylomeDB; Q9JI11; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 314257; -.
DR   ArrayExpress; Q9JI11; -.
DR   Bgee; Q9JI11; -.
DR   CleanEx; MM_STK4; -.
DR   Genevestigator; Q9JI11; -.
DR   GermOnline; ENSMUSG00000018209; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0035329; P:hippo signaling cascade; IMP:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR011524; SARAH.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG.
DR   PROSITE; PS50951; SARAH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; ATP-binding; Coiled coil; Cytoplasm; Kinase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    487       Serine/threonine-protein kinase 4.
FT                                /FTId=PRO_0000246627.
FT   DOMAIN       30    281       Protein kinase.
FT   DOMAIN      433    480       SARAH.
FT   NP_BIND      36     44       ATP (By similarity).
FT   COILED      289    311       Potential.
FT   COMPBIAS    373    378       Poly-Glu.
FT   ACT_SITE    149    149       Proton acceptor (By similarity).
FT   BINDING      59     59       ATP (By similarity).
FT   SITE        326    327       Cleavage; by caspase-3 (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES       3      3       Phosphothreonine (By similarity).
FT   MOD_RES      40     40       Phosphoserine (By similarity).
FT   MOD_RES      41     41       Phosphotyrosine (By similarity).
FT   MOD_RES     175    175       Phosphothreonine (By similarity).
FT   MOD_RES     177    177       Phosphothreonine (By similarity).
FT   MOD_RES     183    183       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     265    265       Phosphoserine (By similarity).
FT   MOD_RES     320    320       Phosphoserine.
FT   MOD_RES     327    327       Phosphoserine (By similarity).
FT   MOD_RES     329    329       Phosphothreonine (By similarity).
FT   MOD_RES     340    340       Phosphothreonine (By similarity).
FT   MOD_RES     353    353       Phosphothreonine (By similarity).
FT   MOD_RES     360    360       Phosphothreonine (By similarity).
FT   MOD_RES     367    367       Phosphothreonine (By similarity).
FT   MOD_RES     380    380       Phosphothreonine (By similarity).
FT   MOD_RES     387    387       Phosphothreonine (By similarity).
FT   MOD_RES     394    394       Phosphoserine (By similarity).
FT   MOD_RES     410    410       Phosphoserine (By similarity).
FT   MOD_RES     422    422       Phosphoserine (By similarity).
FT   MOD_RES     433    433       Phosphotyrosine.
FT   MOD_RES     438    438       Phosphoserine (By similarity).
SQ   SEQUENCE   487 AA;  55541 MW;  A21E9519AD209C40 CRC64;
     METVQLRNPP RRQLKKLDED SLTKQPEEVF DVLEKLGEGS YGSVYKAIHK ETGQIVAIKQ
     VPVESDLQEI IKEISIMQQC DSPHVVKYYG SYFKNTDLWI VMEYCGAGSV SDIIRLRNKT
     LTEDEIATIL QSTLKGLEYL HFMRKIHRDI KAGNILLNTE GHAKLADFGV AGQLTDTMAK
     RNTVIGTPFW MAPEVIQEIG YNCVADIWSL GITAIEMAEG KPPYADIHPM RAIFMIPTNP
     PPTFRKPELW SDNFMDFVKQ CLVKSPEQRA TATQLLQHPF VKSAKGVSIL RDLINEAMDV
     KLKRQEAQQR EVDQDDEENS EEDEMDSGTM VRAAGDEMGT VRVASTMSGG ANTMIEHGDT
     LPSQLGTMVI NTEDEEEEGT MKRRDETMQP AKPSFLEYFE QKEKENQINS FGKNVSGSLK
     NSSDWKIPQD GDYEFLKSWT VEDLQKRLLA LDPMMEQEME EIRQKYRSKR QPILDAIEAK
     KRRQQNF
//
ID   NUDT3_MOUSE             Reviewed;         168 AA.
AC   Q9JI46; B2KF68; Q6PG02; Q8BV71;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Diphosphoinositol polyphosphate phosphohydrolase 1;
DE            Short=DIPP-1;
DE            Short=muDIPP1;
DE            EC=3.6.1.52;
DE   AltName: Full=Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 1;
DE            EC=3.6.1.-;
DE   AltName: Full=Nucleoside diphosphate-linked moiety X motif 3;
DE            Short=Nudix motif 3;
GN   Name=Nudt3; Synonyms=Dipp, Dipp1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP   GLU-70.
RC   TISSUE=Heart;
RX   PubMed=15212765; DOI=10.1016/j.cellsig.2004.02.009;
RA   Chu C., Alapat D., Wen X., Timo K., Burstein D., Lisanti M.,
RA   Shears S., Kohtz D.S.;
RT   "Ectopic expression of murine diphosphoinositol polyphosphate
RT   phosphohydrolase 1 attenuates signaling through the ERK1/2 pathway.";
RL   Cell. Signal. 16:1045-1059(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 81-168.
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in
CC       PP-InsP5 (diphosphoinositol pentakisphosphate) and [PP]2-InsP4
CC       (bisdiphosphoinositol tetrakisphosphate), suggesting that it may
CC       play a role in signal transduction. InsP6 (inositol
CC       hexakisphophate) is not a substrate. Also able to catalyze the
CC       hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A
CC       being the preferred substrates. The major reaction products are
CC       ADP and p4a from Ap6A and ADP and ATP from Ap5A. Also able to
CC       hydrolyze 5-phosphoribose 1-diphosphate (By similarity). Acts as a
CC       negative regulator of the ERK1/2 pathway.
CC   -!- CATALYTIC ACTIVITY: Diphospho-myo-inositol polyphosphate + H(2)O =
CC       myo-inositol polyphosphate + phosphate.
CC   -!- COFACTOR: Binds 3 magnesium ions per subunit (By similarity).
CC   -!- ENZYME REGULATION: Inhibited by fluoride and InsP6 (By
CC       similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- TISSUE SPECIFICITY: Present in heart, lung, liver and spleen (at
CC       protein level). Widely expressed.
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. DIPP subfamily.
CC   -!- SIMILARITY: Contains 1 nudix hydrolase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH57331.1; Type=Miscellaneous discrepancy; Note=Chimeric at the C-terminus;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF264064; AAF74761.1; -; mRNA.
DR   EMBL; CT027568; CAQ52215.1; -; Genomic_DNA.
DR   EMBL; BC016534; AAH16534.1; -; mRNA.
DR   EMBL; BC046805; AAH46805.1; -; mRNA.
DR   EMBL; BC057331; AAH57331.1; ALT_SEQ; mRNA.
DR   EMBL; AK079658; BAC37717.1; -; mRNA.
DR   IPI; IPI00119880; -.
DR   RefSeq; NP_062811.1; NM_019837.2.
DR   UniGene; Mm.144699; -.
DR   UniGene; Mm.32556; -.
DR   UniGene; Mm.473041; -.
DR   ProteinModelPortal; Q9JI46; -.
DR   SMR; Q9JI46; 8-142.
DR   STRING; Q9JI46; -.
DR   PhosphoSite; Q9JI46; -.
DR   PRIDE; Q9JI46; -.
DR   Ensembl; ENSMUST00000025050; ENSMUSP00000025050; ENSMUSG00000024213.
DR   Ensembl; ENSMUST00000062397; ENSMUSP00000059061; ENSMUSG00000024213.
DR   GeneID; 56409; -.
DR   KEGG; mmu:56409; -.
DR   UCSC; uc008bpg.1; mouse.
DR   CTD; 56409; -.
DR   MGI; MGI:1928484; Nudt3.
DR   eggNOG; roNOG17195; -.
DR   GeneTree; ENSGT00390000012928; -.
DR   HOGENOM; HBG713158; -.
DR   HOVERGEN; HBG053341; -.
DR   InParanoid; Q9JI46; -.
DR   OMA; GCLANNG; -.
DR   OrthoDB; EOG479F89; -.
DR   PhylomeDB; Q9JI46; -.
DR   BRENDA; 3.6.1.52; 244.
DR   NextBio; 312542; -.
DR   ArrayExpress; Q9JI46; -.
DR   Bgee; Q9JI46; -.
DR   Genevestigator; Q9JI46; -.
DR   GermOnline; ENSMUSG00000024213; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008486; F:diphosphoinositol-polyphosphate diphosphatase activity; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0071544; P:diphosphoinositol polyphosphate catabolic process; ISS:UniProtKB.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR015797; NUDIX_hydrolase_dom-like.
DR   Gene3D; G3DSA:3.90.79.10; NUDIX_hydrolase; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   SUPFAM; SSF55811; NUDIX_hydrolase; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Magnesium; Metal-binding.
FT   CHAIN         1    168       Diphosphoinositol polyphosphate
FT                                phosphohydrolase 1.
FT                                /FTId=PRO_0000057056.
FT   DOMAIN       17    144       Nudix hydrolase.
FT   REGION       18     20       Substrate binding (By similarity).
FT   REGION       89     91       Substrate binding (By similarity).
FT   MOTIF        51     72       Nudix box.
FT   ACT_SITE     69     69       Proton acceptor (By similarity).
FT   METAL        50     50       Magnesium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        66     66       Magnesium 2 (By similarity).
FT   METAL        66     66       Magnesium 3 (By similarity).
FT   METAL        70     70       Magnesium 1 (By similarity).
FT   BINDING      10     10       Substrate (By similarity).
FT   BINDING      41     41       Substrate (By similarity).
FT   MUTAGEN      70     70       E->Q: Loss of enzyme activity, but
FT                                retains ability to regulate the ERK1/2
FT                                pathway.
SQ   SEQUENCE   168 AA;  19030 MW;  E543BE5CBE520910 CRC64;
     MMKLKSNQTR TYDGDGYKKR AACLCFRSES EEEVLLVSSS RHPDRWIVPG GGMEPEEEPS
     VAAVREVCEE AGVKGTLGRL VGIFENQERK HRTYVYVLIV TEVLEDWEDS VNIGRKREWF
     KIEDAIKVLQ CHKPVQASYF ETLRQGYPAN NGTPVVPTTY SSSVSGIR
//
ID   SGPP1_MOUSE             Reviewed;         430 AA.
AC   Q9JI99;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-FEB-2011, entry version 73.
DE   RecName: Full=Sphingosine-1-phosphate phosphatase 1;
DE            Short=SPP;
DE            Short=SPPase1;
DE            Short=mSPP1;
DE            EC=3.1.3.-;
DE   AltName: Full=Sphingosine-1-phosphatase 1;
GN   Name=Sgpp1; Synonyms=Spp1, Spph1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=20345077; PubMed=10859351; DOI=10.1073/pnas.120146897;
RA   Mandala S.M., Thornton R., Galve-Roperh I., Poulton S., Peterson C.,
RA   Olivera A., Bergstrom J., Kurtz M.B., Spiegel S.;
RT   "Molecular cloning and characterization of a lipid phosphohydrolase
RT   that degrades sphingosine-1-phosphate and induces cell death.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:7859-7864(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Thompson D., Pyne S.;
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary cancer;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101 AND THR-103, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Has enzymatic activity against both sphingosine 1-
CC       phosphate (S1P) and dihydro-S1P. Regulates intracellular and
CC       extracellular S1P levels (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in liver and kidney.
CC   -!- SIMILARITY: Belongs to the type 2 lipid phosphate phosphatase
CC       family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF247177; AAF90052.1; -; mRNA.
DR   EMBL; AF415215; AAL07501.1; -; mRNA.
DR   EMBL; BC037592; AAH37592.1; -; mRNA.
DR   IPI; IPI00120052; -.
DR   RefSeq; NP_109675.1; NM_030750.3.
DR   UniGene; Mm.478829; -.
DR   ProteinModelPortal; Q9JI99; -.
DR   STRING; Q9JI99; -.
DR   PhosphoSite; Q9JI99; -.
DR   PRIDE; Q9JI99; -.
DR   Ensembl; ENSMUST00000021450; ENSMUSP00000021450; ENSMUSG00000021054.
DR   GeneID; 81535; -.
DR   KEGG; mmu:81535; -.
DR   NMPDR; fig|10090.3.peg.26697; -.
DR   UCSC; uc007nxk.1; mouse.
DR   CTD; 81535; -.
DR   MGI; MGI:2135760; Sgpp1.
DR   GeneTree; ENSGT00390000017322; -.
DR   HOGENOM; HBG713817; -.
DR   HOVERGEN; HBG079185; -.
DR   InParanoid; Q9JI99; -.
DR   OMA; QCTKDII; -.
DR   PhylomeDB; Q9JI99; -.
DR   NextBio; 350406; -.
DR   ArrayExpress; Q9JI99; -.
DR   Bgee; Q9JI99; -.
DR   CleanEx; MM_SGPP1; -.
DR   CleanEx; MM_SPP1; -.
DR   Genevestigator; Q9JI99; -.
DR   GermOnline; ENSMUSG00000021054; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0042392; F:sphingosine-1-phosphate phosphatase activity; IDA:MGI.
DR   GO; GO:0006915; P:apoptosis; IDA:MGI.
DR   GO; GO:0006668; P:sphinganine-1-phosphate metabolic process; IDA:MGI.
DR   GO; GO:0006670; P:sphingosine metabolic process; IDA:MGI.
DR   InterPro; IPR016118; P_Acid_Pase/Cl_peroxidase_N.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   Gene3D; G3DSA:1.20.144.10; P_Acid_Pase/Cl_peroxidase_N; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   SMART; SM00014; acidPPc; 1.
DR   SUPFAM; SSF48317; AcPase_VanPerase; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Hydrolase; Membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    430       Sphingosine-1-phosphate phosphatase 1.
FT                                /FTId=PRO_0000114478.
FT   TRANSMEM    121    141       Helical; (Potential).
FT   TRANSMEM    152    172       Helical; (Potential).
FT   TRANSMEM    193    213       Helical; (Potential).
FT   TRANSMEM    216    236       Helical; (Potential).
FT   TRANSMEM    246    266       Helical; (Potential).
FT   TRANSMEM    279    299       Helical; (Potential).
FT   TRANSMEM    311    331       Helical; (Potential).
FT   TRANSMEM    348    368       Helical; (Potential).
FT   TRANSMEM    409    429       Helical; (Potential).
FT   MOD_RES     101    101       Phosphoserine.
FT   MOD_RES     103    103       Phosphothreonine.
SQ   SEQUENCE   430 AA;  47744 MW;  503A6D8162C141C7 CRC64;
     MSLGQRLALL ASRLQEPQRV ASFQRLCGVE VPLSSPAADE DAETEVRGAP GEPRRRGRQP
     GAEDSPAKAD CCGAPNGVRN GLAAEPGPTG PRRAGSQRRN SLTGEEGELV KVSNLPLYYL
     FCLGTELGNE LFYILFFPFW IWNLDPFVGR RLVIIWVLVM YLGQCTKDII RWPRPASPPV
     IKLEVFYNSE YSMPSTHAMS GTAIPIAMFL LTYGRWQYPL IYGLILIPCW SSLVCLSRIY
     MGMHSILDVI AGFLYTILIL IIFYPLVDLI DNFNQTYKYA PLIIIGLHLI LGIFSFTLDT
     WSTSRGDTAE ILGSGAGIAC GSHAAYTLGL SLEPSLHMLP LAIPPLTVTL FGKAILRIVL
     GMLLVLFVRD IMKKITIPLA CKLSSIPCHD IRQARQHMEV ELPYRYITYG MVGFSITFLV
     PYVFSFIGIS
//
ID   SPHK2_MOUSE             Reviewed;         617 AA.
AC   Q9JIA7; Q91VA9; Q9DBH6;
DT   24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-MAR-2002, sequence version 2.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Sphingosine kinase 2;
DE            Short=SK 2;
DE            Short=SPK 2;
DE            EC=2.7.1.91;
GN   Name=Sphk2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=20347850; PubMed=10751414; DOI=10.1074/jbc.M002759200;
RA   Liu H., Sugiura M., Nava V.E., Edsall L.C., Kono K., Poulton S.,
RA   Milstien S., Kohama T., Spiegel S.;
RT   "Molecular cloning and functional characterization of a novel
RT   mammalian sphingosine kinase type 2 isoform.";
RL   J. Biol. Chem. 275:19513-19520(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Thompson D., Pyne S.;
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Limb, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Catalyzes the phosphorylation of sphingosine to form
CC       sphingosine 1-phosphate (SPP), a lipid mediator with both intra-
CC       and extracellular functions. Also acts on D-erythro-
CC       dihydrosphingosine, D-erythro-sphingosine and L-threo-
CC       dihydrosphingosine. Binds phosphoinositides (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + sphinganine = ADP + sphinganine 1-
CC       phosphate.
CC   -!- CATALYTIC ACTIVITY: ATP + sphingosine = ADP + sphingosine 1-
CC       phosphate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- INTERACTION:
CC       P06241:FYN (xeno); NbExp=1; IntAct=EBI-985434, EBI-515315;
CC       P39688:Fyn; NbExp=2; IntAct=EBI-985434, EBI-524514;
CC       P07948:LYN (xeno); NbExp=1; IntAct=EBI-985434, EBI-79452;
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane (By similarity).
CC   -!- SIMILARITY: Contains 1 DAGKc domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF245448; AAF74125.1; -; mRNA.
DR   EMBL; AF415214; AAL07500.1; -; mRNA.
DR   EMBL; AK004951; BAB23694.1; -; mRNA.
DR   EMBL; BC006941; AAH06941.1; -; mRNA.
DR   EMBL; BC053737; AAH53737.1; -; mRNA.
DR   IPI; IPI00310333; -.
DR   RefSeq; NP_001166032.1; NM_001172561.1.
DR   RefSeq; NP_064395.2; NM_020011.5.
DR   RefSeq; NP_975009.1; NM_203280.3.
DR   UniGene; Mm.24222; -.
DR   ProteinModelPortal; Q9JIA7; -.
DR   IntAct; Q9JIA7; 5.
DR   STRING; Q9JIA7; -.
DR   PhosphoSite; Q9JIA7; -.
DR   PRIDE; Q9JIA7; -.
DR   Ensembl; ENSMUST00000072836; ENSMUSP00000072615; ENSMUSG00000057342.
DR   Ensembl; ENSMUST00000107737; ENSMUSP00000103366; ENSMUSG00000057342.
DR   Ensembl; ENSMUST00000107738; ENSMUSP00000103367; ENSMUSG00000057342.
DR   GeneID; 56632; -.
DR   KEGG; mmu:56632; -.
DR   UCSC; uc009gwt.1; mouse.
DR   CTD; 56632; -.
DR   MGI; MGI:1861380; Sphk2.
DR   GeneTree; ENSGT00530000063185; -.
DR   HOGENOM; HBG447384; -.
DR   HOVERGEN; HBG054796; -.
DR   InParanoid; Q9JIA7; -.
DR   OMA; AEAMAPP; -.
DR   OrthoDB; EOG4X0MSG; -.
DR   PhylomeDB; Q9JIA7; -.
DR   BRENDA; 2.7.1.91; 244.
DR   NextBio; 313067; -.
DR   ArrayExpress; Q9JIA7; -.
DR   Bgee; Q9JIA7; -.
DR   CleanEx; MM_SPHK2; -.
DR   Genevestigator; Q9JIA7; -.
DR   GermOnline; ENSMUSG00000057342; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005624; C:membrane fraction; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017050; F:D-erythro-sphingosine kinase activity; IDA:MGI.
DR   GO; GO:0004143; F:diacylglycerol kinase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0008481; F:sphinganine kinase activity; NAS:UniProtKB.
DR   GO; GO:0007205; P:activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway; IEA:InterPro.
DR   GO; GO:0006916; P:anti-apoptosis; NAS:UniProtKB.
DR   GO; GO:0001568; P:blood vessel development; IGI:MGI.
DR   GO; GO:0007420; P:brain development; IGI:MGI.
DR   GO; GO:0008283; P:cell proliferation; NAS:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IGI:MGI.
DR   GO; GO:0006669; P:sphinganine-1-phosphate biosynthetic process; NAS:UniProtKB.
DR   GO; GO:0006670; P:sphingosine metabolic process; IMP:MGI.
DR   InterPro; IPR001206; Diacylglycerol_kinase_cat_dom.
DR   Pfam; PF00781; DAGK_cat; 1.
DR   SMART; SM00046; DAGKc; 1.
DR   PROSITE; PS50146; DAGK; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Lysosome; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Transferase.
FT   CHAIN         1    617       Sphingosine kinase 2.
FT                                /FTId=PRO_0000181359.
FT   DOMAIN      143    290       DAGKc.
FT   REGION        1    140       Required for binding to sulfatide and
FT                                phosphoinositides and for membrane
FT                                localization (By similarity).
FT   MOD_RES     364    364       Phosphoserine.
FT   MOD_RES     379    379       Phosphoserine (By similarity).
FT   CONFLICT    252    252       N -> S (in Ref. 1; AAF74125).
FT   CONFLICT    510    510       P -> T (in Ref. 1; AAF74125).
FT   CONFLICT    548    548       L -> F (in Ref. 1; AAF74125).
SQ   SEQUENCE   617 AA;  65618 MW;  40EE2C2C288BE26A CRC64;
     MAPPPLLPVA ASTPILHGEF GSYPANGPRF ALTLTTQALH IQRLRPKPEA RPRDGLVSLD
     EVSGCGTLQS RSPEDTAAYF CIYTYPRGRR GGRRRATRTF RADGATTYEE NRAEAQRWAT
     ALTCLLRGVP LSGDQEITPE LLPRKPRLLI LVNPFGGRGL AWQRCMDHVV PMISEAGLSF
     NLIQTERQNH ARELVQGLSL SEWEGIVTVS GDGLLYEVLN GLLDRPDWED AVRMPIGVLP
     CGSGNALAGA VNHHGGFEQV VGVDLLLNCS LLLCRGGSHP LDLLSVTLAS GSRCFSFLSV
     AWGFLSDVDI HSERFRALGS ARFTLGAVLG LASLHTYRGR LSYLPATTEP ALPIPGHSLP
     RAKSELVLAP APAPAATHSP LHRSVSDLPL PLPQPALVSP GSPEPLPDLS LNGGGPELTG
     DWGGAGDAPL SPDPLLPSSP NALKTAQLSP IAEGPPEMPA SSGFLPPTHS APEASTWGPV
     DHLLPPLGSP LPQDWVTIEG EFVLMLGILP SHLCADLMAA PHARFDDGVV HLCWVRSGIS
     RAALLRILLA MEHGNHFSLG CPHLGYAAAR AFRLEPLTPR GLLTVDGELV EYGPIQAQVH
     PGLATLLTGP AGQKPQA
//
ID   GTR8_MOUSE              Reviewed;         477 AA.
AC   Q9JIF3; Q9JJP4; Q9JJZ0;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Solute carrier family 2, facilitated glucose transporter member 8;
DE   AltName: Full=Glucose transporter type 8;
DE            Short=GLUT-8;
DE   AltName: Full=Glucose transporter type X1;
GN   Name=Slc2a8; Synonyms=Glut8, GlutX1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20138191; PubMed=10671487; DOI=10.1074/jbc.275.7.4607;
RA   Ibberson M.R., Uldry M.A., Thorens B.;
RT   "GLUTX1, a novel mammalian glucose transporter expressed in the
RT   central nervous system and insulin-sensitive tissues.";
RL   J. Biol. Chem. 275:4607-4612(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   MEDLINE=20283667; PubMed=10821868; DOI=10.1074/jbc.275.21.16275;
RA   Doege H., Schuermann A., Bahrenberg G., Brauers A., Joost H.-G.;
RT   "GLUT8, a novel member of the sugar transport facilitator family with
RT   glucose transport activity.";
RL   J. Biol. Chem. 275:16275-16280(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129; TISSUE=Embryonic carcinoma;
RX   MEDLINE=20319023; PubMed=10860996; DOI=10.1073/pnas.97.13.7313;
RA   Carayannopoulos M.O., Chi M.M.-Y., Cui Y., Pingsterhaus J.M.,
RA   McKnight R.A., Mueckler M., Devaskar S.U., Moley K.H.;
RT   "GLUT8 is a glucose transporter responsible for insulin-stimulated
RT   glucose uptake in the blastocyst.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:7313-7318(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Ola; TISSUE=Spleen;
RX   MEDLINE=21547794; PubMed=11689004; DOI=10.1006/bbrc.2001.5866;
RA   Scheepers A., Doege H., Joost H.-G., Schuermann A.;
RT   "Mouse GLUT8: genomic organization and regulation of expression in
RT   3T3-L1 adipocytes by glucose.";
RL   Biochem. Biophys. Res. Commun. 288:969-974(2001).
RN   [5]
RP   INTERACTION WITH AP2B1, AND MUTAGENESIS OF 12-LEU-LEU-13.
RX   PubMed=16723738; DOI=10.1242/jcs.02943;
RA   Schmidt U., Briese S., Leicht K., Schuermann A., Joost H.-G.,
RA   Al-Hasani H.;
RT   "Endocytosis of the glucose transporter GLUT8 is mediated by
RT   interaction of a dileucine motif with the beta2-adaptin subunit of the
RT   AP-2 adaptor complex.";
RL   J. Cell Sci. 119:2321-2331(2006).
CC   -!- FUNCTION: Insulin-regulated facilitative glucose transporter.
CC       Binds cytochalasin B in a glucose-inhibitable manner. Seems to be
CC       a dual-specific sugar transporter as it is inhibitable by
CC       fructose.
CC   -!- SUBUNIT: Interacts with AP2B1.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity). Cytoplasmic vesicle membrane; Multi-pass membrane
CC       protein (By similarity). Note=Principally intracellular. May move
CC       between intracellular vesicles and the plasma membrane. The
CC       dileucine internalization motif is critical for intracellular
CC       sequestration (By similarity). Insulin induces a change in the
CC       intracellular localization and gives rise to insertion in the
CC       plasma membrane.
CC   -!- TISSUE SPECIFICITY: Highest level of expression in placenta and
CC       testis. Highly expressed in adult and pubertal testis, but not
CC       prepubertal testis. Lower levels of expression in brain, liver,
CC       heart, kidney, fat and skeletal muscle.
CC   -!- DEVELOPMENTAL STAGE: High expression in blastocysts.
CC   -!- INDUCTION: Inhibited under glucose deprivation.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC       transporter (TC 2.A.1.1) family. Glucose transporter subfamily.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AJ245936; CAB75719.1; -; mRNA.
DR   EMBL; Y17802; CAB89815.1; -; mRNA.
DR   EMBL; AF232061; AAF78366.1; -; mRNA.
DR   EMBL; AJ413951; CAC88690.1; -; Genomic_DNA.
DR   IPI; IPI00310367; -.
DR   RefSeq; NP_062361.1; NM_019488.4.
DR   UniGene; Mm.305754; -.
DR   ProteinModelPortal; Q9JIF3; -.
DR   SMR; Q9JIF3; 438-470.
DR   MINT; MINT-7035216; -.
DR   STRING; Q9JIF3; -.
DR   TCDB; 2.A.1.1.46; major facilitator superfamily (MFS).
DR   PRIDE; Q9JIF3; -.
DR   Ensembl; ENSMUST00000028129; ENSMUSP00000028129; ENSMUSG00000026791.
DR   GeneID; 56017; -.
DR   KEGG; mmu:56017; -.
DR   CTD; 56017; -.
DR   MGI; MGI:1860103; Slc2a8.
DR   GeneTree; ENSGT00600000084007; -.
DR   HOGENOM; HBG744444; -.
DR   HOVERGEN; HBG104335; -.
DR   InParanoid; Q9JIF3; -.
DR   OrthoDB; EOG41G349; -.
DR   ArrayExpress; Q9JIF3; -.
DR   Bgee; Q9JIF3; -.
DR   Genevestigator; Q9JIF3; -.
DR   GermOnline; ENSMUSG00000026791; Mus musculus.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005887; C:integral to plasma membrane; IDA:MGI.
DR   GO; GO:0005536; F:glucose binding; IDA:MGI.
DR   GO; GO:0005355; F:glucose transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0006006; P:glucose metabolic process; TAS:MGI.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IDA:MGI.
DR   GO; GO:0001666; P:response to hypoxia; IDA:MGI.
DR   InterPro; IPR020846; Major_facilitator_SF.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   InterPro; IPR005828; Sub_transporter.
DR   InterPro; IPR003663; Sugar/inositol_transpt.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   PRINTS; PR00171; SUGRTRNSPORT.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
DR   TIGRFAMs; TIGR00879; SP; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
DR   PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasmic vesicle; Glycoprotein; Membrane;
KW   Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    477       Solute carrier family 2, facilitated
FT                                glucose transporter member 8.
FT                                /FTId=PRO_0000050376.
FT   TOPO_DOM      1     25       Cytoplasmic (Potential).
FT   TRANSMEM     26     46       Helical; Name=1; (Potential).
FT   TOPO_DOM     47     70       Extracellular (Potential).
FT   TRANSMEM     71     91       Helical; Name=2; (Potential).
FT   TOPO_DOM     92     96       Cytoplasmic (Potential).
FT   TRANSMEM     97    117       Helical; Name=3; (Potential).
FT   TOPO_DOM    118    127       Extracellular (Potential).
FT   TRANSMEM    128    148       Helical; Name=4; (Potential).
FT   TOPO_DOM    149    156       Cytoplasmic (Potential).
FT   TRANSMEM    157    177       Helical; Name=5; (Potential).
FT   TOPO_DOM    178    182       Extracellular (Potential).
FT   TRANSMEM    183    203       Helical; Name=6; (Potential).
FT   TOPO_DOM    204    257       Cytoplasmic (Potential).
FT   TRANSMEM    258    278       Helical; Name=7; (Potential).
FT   TOPO_DOM    279    293       Extracellular (Potential).
FT   TRANSMEM    294    314       Helical; Name=8; (Potential).
FT   TOPO_DOM    315    320       Cytoplasmic (Potential).
FT   TRANSMEM    321    341       Helical; Name=9; (Potential).
FT   TOPO_DOM    342    367       Extracellular (Potential).
FT   TRANSMEM    368    388       Helical; Name=10; (Potential).
FT   TOPO_DOM    389    404       Cytoplasmic (Potential).
FT   TRANSMEM    405    425       Helical; Name=11; (Potential).
FT   TOPO_DOM    426    438       Extracellular (Potential).
FT   TRANSMEM    439    459       Helical; Name=12; (Potential).
FT   TOPO_DOM    460    477       Cytoplasmic (Potential).
FT   MOTIF        12     13       Dileucine internalization motif
FT                                (Potential).
FT   CARBOHYD    350    350       N-linked (GlcNAc...) (By similarity).
FT   MUTAGEN      12     13       LL->AA: Abolishes interaction with AP2B1.
FT   CONFLICT     39     39       S -> N (in Ref. 1; CAB75719).
FT   CONFLICT     94     94       S -> A (in Ref. 2 and 4).
FT   CONFLICT    429    429       S -> N (in Ref. 1; CAB75719).
SQ   SEQUENCE   477 AA;  51524 MW;  A3753FB34E452F9A CRC64;
     MSPEDPQETQ PLLRPPEART PRGRRVFLAS FAAALGPLSF GFALGYSSPA IPSLRRTAPP
     ALRLGDNAAS WFGAVVTLGA AAGGILGGWL LDRSGRKLSL LLCTVPFVTG FAVITAARDV
     WMLLGGRLLT GLACGVASLV APVYISEIAY PAVRGLLGSC VQLMVVTGIL LAYVAGWVLE
     WRWLAVLGCV PPTLMLLLMC YMPETPRFLL TQHQYQEAMA ALRFLWGSEE GWEEPPVGAE
     HQGFQLALLR RPGIYKPLII GISLMVFQQL SGVNAIMFYA NSIFEEAKFK DSSLASVTVG
     IIQVLFTAVA ALIMDRAGRR LLLALSGVIM VFSMSAFGTY FKLTQSLPSN SSHVGLVPIA
     AEPVDVQVGL AWLAVGSMCL FIAGFAVGWG PIPWLLMSEI FPLHVKGVAT GICVLTNWFM
     AFLVTKEFSS VMEMLRPYGA FWLTAAFCAL SVLFTLTVVP ETKGRTLEQV TAHFEGR
//
ID   PPR3F_MOUSE             Reviewed;         799 AA.
AC   Q9JIG4; B1AW09; B1AW10; Q3UGL4; Q6PCL6;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 3.
DT   08-MAR-2011, entry version 52.
DE   RecName: Full=Protein phosphatase 1 regulatory subunit 3F;
GN   Name=Ppp1r3f; Synonyms=DXImx48e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 12-799 (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 44-799 (ISOFORM 1).
RC   TISSUE=Thymus;
RX   MEDLINE=20313888; PubMed=10857745; DOI=10.1006/geno.2000.6173;
RA   Means G.D., Toy D.Y., Baum P.R., Derry J.M.J.;
RT   "A transcript map of a 2-Mb BAC contig in the proximal portion of the
RT   mouse X chromosome and regional mapping of the scurfy mutation.";
RL   Genomics 65:213-223(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 393-735 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J; TISSUE=Melanocyte;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9JIG4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9JIG4-2; Sequence=VSP_021363;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 CBM21 (carbohydrate binding type-21)
CC       domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF66954.2; Type=Erroneous initiation;
CC       Sequence=AAH59275.1; Type=Erroneous initiation;
CC       Sequence=CAM14759.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AL731793; CAM14759.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL731793; CAM14760.1; -; Genomic_DNA.
DR   EMBL; BC059275; AAH59275.1; ALT_INIT; mRNA.
DR   EMBL; AF229644; AAF66954.2; ALT_INIT; mRNA.
DR   EMBL; AK147873; BAE28194.1; -; mRNA.
DR   IPI; IPI00120535; -.
DR   IPI; IPI00752434; -.
DR   RefSeq; NP_613071.2; NM_138605.2.
DR   UniGene; Mm.148163; -.
DR   ProteinModelPortal; Q9JIG4; -.
DR   SMR; Q9JIG4; 112-288.
DR   CAZy; CBM21; Carbohydrate-Binding Module Family 21.
DR   Ensembl; ENSMUST00000115742; ENSMUSP00000111407; ENSMUSG00000039556.
DR   GeneID; 54646; -.
DR   KEGG; mmu:54646; -.
DR   NMPDR; fig|10090.3.peg.21149; -.
DR   UCSC; uc009slj.1; mouse.
DR   CTD; 54646; -.
DR   MGI; MGI:1859617; Ppp1r3f.
DR   eggNOG; roNOG10722; -.
DR   GeneTree; ENSGT00390000013859; -.
DR   HOGENOM; HBG283646; -.
DR   OMA; DDNTPAV; -.
DR   NextBio; 311496; -.
DR   ArrayExpress; Q9JIG4; -.
DR   Bgee; Q9JIG4; -.
DR   Genevestigator; Q9JIG4; -.
DR   GermOnline; ENSMUSG00000039556; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR005036; CBM_21.
DR   Pfam; PF03370; CBM_21; 1.
DR   PROSITE; PS51159; CBM21; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    799       Protein phosphatase 1 regulatory subunit
FT                                3F.
FT                                /FTId=PRO_0000257497.
FT   TOPO_DOM      1    772       Extracellular (Potential).
FT   TRANSMEM    773    793       Helical; (Potential).
FT   TOPO_DOM    794    799       Cytoplasmic (Potential).
FT   DOMAIN      127    283       CBM21.
FT   CARBOHYD    279    279       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     377    377       L -> LQ (in isoform 2).
FT                                /FTId=VSP_021363.
FT   CONFLICT    266    266       T -> N (in Ref. 2; AAH59275).
SQ   SEQUENCE   799 AA;  84120 MW;  DF6572A80FECB7BC CRC64;
     MARTAPVEPP LRHPAPPSPA AGEPRASAEA AVAPRRVLFA DEALGLPLAQ LRRYRPWGGP
     GAGKMAAATG QDGGGGGADE EDDGEDGDEG EEEEEAFPDP SPPCPVPAGG GFYLVPTFSL
     PPALGRLERL GRVMVELEAL LPPPGAVPGG SGVWVPGGRP PVVRGLVRVL NRSFEKAVHV
     RASHDGWATF CDHPARYVPR SPPGAGVGGT GAGDPLLDPG LGLGPGQMSA SSPDDGGCTD
     RFAFQLPFAE GASDGARLDF VVRYETPEGT FWANNHGRNY TVLLRIAPAP TPTDAEGLPQ
     QQQLQQLEPQ PECQGPVEAE ARQLKSCMKP VRRRPFEEEP RMRSADDNTL AEHPDVRESL
     GPLLAPTPLR PWPQMTLQVP EVMLTSNPQE EGDIPRSNPP VAFTEVRQAP AIRILPATCG
     LGGPPRDQAS GPDASDRAAG SFLEPTQQQV EAAWESGGGR KAPMVGALTD EPARGLEIVS
     GLDELLGEDT IDQELEQLYL SHLSRLRAVA AAGGGEGTSP THALGILTDR DLILKWPGPE
     RALNSALAEE ITLHYARLGC GVELIKDTED PDDEGEGEDG LSITPSSPEG GSPKESPPEI
     LSGARSVIAT MGDVWVPWAE RSSSRCDSPV VLGTQGQFTE NPEKGMGKDT KSLHLNRVIV
     GMSKSPGEAG TESQMEELPT ERESSWVPSS EKELPLPVQQ EQSPALLGPT GTEVCLSSVA
     KPHVNSQEEE GGSLNLESPK RSPMPAAPAE CACGLAPQLW GPLTQTLGVL AGLVMVPVAL
     NSGVSLLVLV LCLSLAWFS
//
ID   INP5E_MOUSE             Reviewed;         647 AA.
AC   Q9JII1; Q3TCC9;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=72 kDa inositol polyphosphate 5-phosphatase;
DE            EC=3.1.3.36;
DE   AltName: Full=Phosphatidylinositol polyphosphate 5-phosphatase type IV;
DE   AltName: Full=Phosphatidylinositol-4,5-bisphosphate 5-phosphatase;
GN   Name=Inpp5e;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=20379050; PubMed=10806194; DOI=10.1074/jbc.M000874200;
RA   Kong A.M., Speed C.J., O'Malley C.J., Layton M.J., Meehan T.,
RA   Loveland K.L., Cheema S., Ooms L.M., Mitchell C.A.;
RT   "Cloning and characterization of a 72-kDa inositol-polyphosphate 5-
RT   phosphatase localized to the Golgi network.";
RL   J. Biol. Chem. 275:24052-24064(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Aorta, and Vein;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19668215; DOI=10.1038/ng.427;
RA   Jacoby M., Cox J.J., Gayral S., Hampshire D.J., Ayub M., Blockmans M.,
RA   Pernot E., Kisseleva M.V., Compere P., Schiffmann S.N., Gergely F.,
RA   Riley J.H., Perez-Morga D., Woods C.G., Schurmans S.;
RT   "INPP5E mutations cause primary cilium signaling defects, ciliary
RT   instability and ciliopathies in human and mouse.";
RL   Nat. Genet. 41:1027-1031(2009).
CC   -!- FUNCTION: Converts phosphatidylinositol-3,4,5-triphosphate (PtdIns
CC       3,4,5-P3) to PtdIns-P2. Specific for lipid substrates, inactive
CC       towards water soluble inositol phosphates.
CC   -!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-
CC       bisphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 4-phosphate
CC       + phosphate.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme.
CC       Golgi apparatus, Golgi stack membrane; Peripheral membrane
CC       protein; Cytoplasmic side. Note=Peripheral membrane protein
CC       associated with Golgi stacks.
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis, in pachytene and
CC       diplotene spermatocytes, but not in more mature elongating
CC       spermatids. Detected in neurons throughout the brain.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the inositol-1,4,5-trisphosphate 5-
CC       phosphatase type IV family.
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DR   EMBL; AF226683; AAF86957.1; -; mRNA.
DR   EMBL; AK080075; BAC37823.1; -; mRNA.
DR   EMBL; AK154097; BAE32374.1; -; mRNA.
DR   EMBL; AK170786; BAE42028.1; -; mRNA.
DR   EMBL; BC052717; AAH52717.1; -; mRNA.
DR   EMBL; BC080295; AAH80295.1; -; mRNA.
DR   IPI; IPI00120602; -.
DR   RefSeq; NP_149125.1; NM_033134.2.
DR   UniGene; Mm.330070; -.
DR   ProteinModelPortal; Q9JII1; -.
DR   SMR; Q9JII1; 285-626.
DR   STRING; Q9JII1; -.
DR   PhosphoSite; Q9JII1; -.
DR   PRIDE; Q9JII1; -.
DR   Ensembl; ENSMUST00000145701; ENSMUSP00000119485; ENSMUSG00000026925.
DR   GeneID; 64436; -.
DR   KEGG; mmu:64436; -.
DR   UCSC; uc008ivf.1; mouse.
DR   CTD; 64436; -.
DR   MGI; MGI:1927753; Inpp5e.
DR   GeneTree; ENSGT00600000084387; -.
DR   HOGENOM; HBG278327; -.
DR   HOVERGEN; HBG052132; -.
DR   InParanoid; Q9JII1; -.
DR   OMA; SGMISTS; -.
DR   OrthoDB; EOG4CVG6H; -.
DR   PhylomeDB; Q9JII1; -.
DR   BRENDA; 3.1.3.36; 244.
DR   NextBio; 320083; -.
DR   ArrayExpress; Q9JII1; -.
DR   Bgee; Q9JII1; -.
DR   CleanEx; MM_INPP5E; -.
DR   Genevestigator; Q9JII1; -.
DR   GermOnline; ENSMUSG00000026925; Mus musculus.
DR   GO; GO:0035085; C:cilium axoneme; IDA:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IDA:MGI.
DR   GO; GO:0030384; ?:?; IDA:MGI.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   InterPro; IPR000300; IPPc.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   SMART; SM00128; IPPc; 1.
DR   SUPFAM; SSF56219; Exo_endo_phos; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Cilium; Cytoplasm; Cytoskeleton; Golgi apparatus;
KW   Hydrolase; Lipid metabolism; Membrane; Phosphoprotein; Repeat.
FT   CHAIN         1    647       72 kDa inositol polyphosphate 5-
FT                                phosphatase.
FT                                /FTId=PRO_0000209748.
FT   REPEAT       52     55       1.
FT   REPEAT       76     79       2.
FT   REPEAT      240    243       3.
FT   REGION       52    243       3 X 4 AA repeats of P-X-X-P.
FT   COMPBIAS     96    101       Poly-Arg.
FT   MOD_RES     103    103       Phosphoserine (By similarity).
FT   MOD_RES     245    245       Phosphoserine.
SQ   SEQUENCE   647 AA;  71915 MW;  4BBE3A39DB7ECB0E CRC64;
     MPSKSACLRH TEAPGQLEGR MLQGQPPNTE KKLIPTPGFL PASDSQGSET NPMPPFSIPA
     KTSNQNPQTK ANLITPQPPI RPKLERTLSL DDKGWRRRRF RGSQEDLTVQ NGASPCRGSL
     QDSVAQSPAY SRPLPCLSTS LQEIPKSRRA TGSEGGSPSL WSDCLSGMIS TSLDLLHRDA
     ASGGPPSRLA SLHASHTPPA MDLSIASSSL RTANKVDPEH TDYKLRMQTR LVRAHSNLGP
     SRPRSPLAGD DHSIHSARSF SLLAPIRTKD IRSRSYLEGS LLASGALLGA EELARYFPDR
     NMALFVATWN MQGQKELPAS LDEFLLPTEA DYTQDLYVIG IQEGCSDRRE WETRLQETLG
     PQYVLLSSAA HGVLYMSLFI RRDLIWFCSE VEYSTVTTRI VSQIKTKGAL GVSFTFFGTS
     FLFITSHFTS GDGKVAERLL DYSRTIQALA LPRNVPDTNP YRSSAGDVTT RFDEVFWFGD
     FNFRLSGGRV AVEAFLKQKP EVDVLALLQH DQLTREMKKG SIFRGFEEAE IHFLPSYKFD
     IGKDTYDSTS KQRTPSYTDR VLYKSRHKGD ICPMKYSSCP GIKTSDHRPV YGLFQVKVRP
     GRDNIPLAAG KFDRELYLIG IKRRISKEIQ RQEALKSQSS SAVCTVS
//
ID   DDX21_MOUSE             Reviewed;         851 AA.
AC   Q9JIK5; Q9WV45;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   04-MAY-2001, sequence version 2.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Nucleolar RNA helicase 2;
DE            EC=3.6.4.13;
DE   AltName: Full=DEAD box protein 21;
DE   AltName: Full=Gu-alpha;
DE   AltName: Full=Nucleolar RNA helicase Gu;
DE   AltName: Full=Nucleolar RNA helicase II;
DE   AltName: Full=RH II/Gu;
GN   Name=Ddx21;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=129/SvJ;
RX   MEDLINE=20318620; PubMed=10860663; DOI=10.1006/geno.2000.6209;
RA   Valdez B.C., Wang W.;
RT   "Mouse RNA helicase II/Gu: cDNA and genomic sequences, chromosomal
RT   localization, and regulation of expression.";
RL   Genomics 66:184-194(2000).
RN   [2]
RP   SEQUENCE REVISION TO N-TERMINUS.
RA   Valdez B.C.;
RL   Submitted (APR-2001) to UniProtKB.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; SER-244; SER-245
RP   AND THR-247, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118; SER-155 AND
RP   SER-192, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND SER-144, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118; SER-155; THR-247
RP   AND SER-261, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Can unwind double-stranded RNA (helicase) and can fold
CC       or introduce a secondary structure to a single-stranded RNA
CC       (foldase). Functions as cofactor for JUN-activated transcription
CC       (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Component of the B-WICH complex, at least composed of
CC       SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and
CC       DDX21 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus.
CC   -!- TISSUE SPECIFICITY: Highly expressed in liver and testis.
CC       Expressed at lower level in brain, lungs, and skeletal muscle.
CC   -!- DOMAIN: The two enzymatic activities reside in two separate
CC       domains, the helicase in the N-terminus and the foldase in the C-
CC       terminus.
CC   -!- DOMAIN: The 3 X 5 AA repeats seem to be critical for the RNA
CC       folding activity.
CC   -!- DOMAIN: The 3 X 37 AA tandem repeats may be important for nuclear
CC       localization and/or interaction with nucleic acids or other
CC       proteins.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX21/DDX50
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF220365; AAF61690.1; -; Genomic_DNA.
DR   EMBL; AF159131; AAD43959.3; -; mRNA.
DR   IPI; IPI00120691; -.
DR   UniGene; Mm.413275; -.
DR   ProteinModelPortal; Q9JIK5; -.
DR   SMR; Q9JIK5; 258-780.
DR   DIP; DIP-48574N; -.
DR   STRING; Q9JIK5; -.
DR   PhosphoSite; Q9JIK5; -.
DR   PRIDE; Q9JIK5; -.
DR   Ensembl; ENSMUST00000045866; ENSMUSP00000042691; ENSMUSG00000020075.
DR   MGI; MGI:1860494; Ddx21.
DR   GeneTree; ENSGT00580000081323; -.
DR   HOGENOM; HBG737336; -.
DR   HOVERGEN; HBG051331; -.
DR   InParanoid; Q9JIK5; -.
DR   OrthoDB; EOG46143T; -.
DR   ArrayExpress; Q9JIK5; -.
DR   Bgee; Q9JIK5; -.
DR   CleanEx; MM_DDX21; -.
DR   Genevestigator; Q9JIK5; -.
DR   GermOnline; ENSMUSG00000020075; Mus musculus.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR012562; GUCT.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF08152; GUCT; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; FALSE_NEG.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Repeat; RNA-binding.
FT   CHAIN         1    851       Nucleolar RNA helicase 2.
FT                                /FTId=PRO_0000055028.
FT   REPEAT      117    153       1-1.
FT   REPEAT      154    190       1-2.
FT   REPEAT      191    227       1-3.
FT   DOMAIN      289    468       Helicase ATP-binding.
FT   DOMAIN      501    645       Helicase C-terminal.
FT   REPEAT      807    811       2-1.
FT   REPEAT      817    823       2-2.
FT   REPEAT      829    833       2-3.
FT   NP_BIND     302    309       ATP (By similarity).
FT   REGION      117    227       3 X 37 AA tandem repeats.
FT   REGION      807    833       3 X 5 AA repeats.
FT   MOTIF       258    286       Q motif.
FT   MOTIF       411    414       DEVD box.
FT   COMPBIAS     95     98       Poly-Lys.
FT   MOD_RES      13     13       Phosphoserine (By similarity).
FT   MOD_RES     118    118       Phosphoserine.
FT   MOD_RES     144    144       Phosphoserine.
FT   MOD_RES     155    155       Phosphoserine.
FT   MOD_RES     192    192       Phosphoserine.
FT   MOD_RES     236    236       Phosphoserine.
FT   MOD_RES     243    243       Phosphoserine (By similarity).
FT   MOD_RES     244    244       Phosphoserine.
FT   MOD_RES     245    245       Phosphoserine.
FT   MOD_RES     247    247       Phosphothreonine.
FT   MOD_RES     261    261       Phosphoserine.
FT   MOD_RES     387    387       Phosphothreonine (By similarity).
FT   MOD_RES     847    847       N6-acetyllysine (By similarity).
FT   CONFLICT      1     46       Missing (in Ref. 1; AAF61690).
FT   CONFLICT    790    790       Q -> P (in Ref. 1; AAF61690).
SQ   SEQUENCE   851 AA;  93582 MW;  71D7286F4CA1DDD7 CRC64;
     MPGKLRSGAK LGSDGAEESM ETLPKPSEKK TRKEKTKSKT EEATEGMEEA VSSKAKKTNK
     KGPSEDDVDP PKSRKAKKQE EEPQDDTAST SKTSKKKKEP LEKQADSETK EIITEEPSEE
     EADMPKPKKM KKGKEANGDA GEKSPKLKNG LSQPSEEEAD IPKPKKMKKG KEANGDAGEK
     SPKLKNGLSQ PSEEEVDIPK PKKMKKGKEA SGDAGEKSPR LKDGLSQPSE PKSNSSDAPG
     EESSSETEKE IPVEQKEGAF SNFPISEETV KLLKARGVNF LFPIQAKTFH HVYSGKDLIA
     QARTGTGKTF SFAIPLIEKL QGGLQERKRG RAPQVLVLAP TRELANQVSK DFSDITKKLS
     VACFYGGTPY GGQIERMRSG IDILVGTPGR IKDHLQNGKL DLTKLKHVVL DEVDQMLDMG
     FADQVEEILC VAYKKDSEDN PQTLLFSATC PHWVFNVAKK YMKSTYEQVD LIGKKTQKAA
     ITVEHLAIKC HWTERAAVIG DVIRVYSGHQ GRTIIFCETK KDAQELSQNT CIKQDAQSLH
     GDIPQKQREI TLKGFRNGNF GVLVATNVAA RGLDIPEVDL VVQSCPPKDV ESYIHRSGRT
     GRAGRTGVCI CFYQNKEEYQ LAQVEQKAGI KFKRIGVPSA TEIIKASSKD AIRLLDSVPP
     TAISHFKQSA EKLIEEKGAV EALAAALAHI SGATSVDQRS LINSQAGFVT MILRCSIEMP
     NISYAWKELK EQLGESIDAK VKGMVFLKGK LGVCFDVRTE AVTEIQEKWH DSRRWQLTVA
     TEQPELEGPQ DGYRGRMGQR DGSRGAFRGQ RGGSRNFRGQ GQRGGSRNFR GQRPGGGNRG
     QKRSFSKAFG Q
//
ID   S29A1_MOUSE             Reviewed;         460 AA.
AC   Q9JIM1; Q99K84; Q9DBT8; Q9JHF0;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Equilibrative nucleoside transporter 1;
DE   AltName: Full=Equilibrative nitrobenzylmercaptopurine riboside-sensitive nucleoside transporter;
DE            Short=Equilibrative NBMPR-sensitive nucleoside transporter;
DE   AltName: Full=Nucleoside transporter, es-type;
DE   AltName: Full=Solute carrier family 29 member 1;
GN   Name=Slc29a1; Synonyms=Ent1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2), AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=129/SvJ;
RX   PubMed=11027664; DOI=10.1006/bbrc.2000.3665;
RA   Choi D.-S., Handa M., Young H., Gordon A.S., Diamond I., Messing R.O.;
RT   "Genomic organization and expression of the mouse equilibrative,
RT   nitrobenzylthioinosine-sensitive nucleoside transporter 1 (ENT1)
RT   gene.";
RL   Biochem. Biophys. Res. Commun. 277:200-208(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=CD-1; TISSUE=Brain;
RX   MEDLINE=20539821; PubMed=11085929; DOI=10.1042/0264-6021:3520363;
RA   Kiss A., Farah K., Kim J., Garriock R.J., Drysdale T.A., Hammond J.R.;
RT   "Molecular cloning and functional characterization of inhibitor-
RT   sensitive (mENT1) and inhibitor-resistant (mENT2) equilibrative
RT   nucleoside transporters from mouse brain.";
RL   Biochem. J. 352:363-372(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Liver, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-48, AND MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Mediates both influx and efflux of nucleosides across
CC       the membrane (equilibrative transporter). It is sensitive (ES) to
CC       low concentrations of the inhibitor nitrobenzylmercaptopurine
CC       riboside (NBMPR) and is sodium-independent. It has a higher
CC       affinity for adenosine. Resistant to dipyridamole and dilazep
CC       inhibition (anticancer chemotherapeutics drugs).
CC   -!- SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass
CC       membrane protein (By similarity). Apical cell membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Ent1b;
CC         IsoId=Q9JIM1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9JIM1-2; Sequence=VSP_010471;
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart, spleen, lung, liver
CC       and testis. Lower level of expression in brain and kidney.
CC   -!- SIMILARITY: Belongs to the SLC29A transporter family.
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DR   EMBL; AF218255; AAF64035.2; -; Genomic_DNA.
DR   EMBL; AF218255; AAF64036.2; -; Genomic_DNA.
DR   EMBL; AF305501; AAG22828.1; -; mRNA.
DR   EMBL; AF131212; AAF78452.1; -; mRNA.
DR   EMBL; AK004756; BAB23537.1; -; mRNA.
DR   EMBL; AK050089; BAC34063.1; -; mRNA.
DR   EMBL; BC004828; AAH04828.1; -; mRNA.
DR   EMBL; BC006812; AAH06812.1; -; mRNA.
DR   IPI; IPI00120769; -.
DR   IPI; IPI00416751; -.
DR   RefSeq; NP_001186042.1; NM_001199113.1.
DR   RefSeq; NP_001186043.1; NM_001199114.1.
DR   RefSeq; NP_001186044.1; NM_001199115.1.
DR   RefSeq; NP_001186045.1; NM_001199116.1.
DR   RefSeq; NP_075018.1; NM_022880.3.
DR   UniGene; Mm.29744; -.
DR   ProteinModelPortal; Q9JIM1; -.
DR   STRING; Q9JIM1; -.
DR   PhosphoSite; Q9JIM1; -.
DR   PRIDE; Q9JIM1; -.
DR   Ensembl; ENSMUST00000051574; ENSMUSP00000063096; ENSMUSG00000023942.
DR   Ensembl; ENSMUST00000064889; ENSMUSP00000063757; ENSMUSG00000023942.
DR   Ensembl; ENSMUST00000097317; ENSMUSP00000094923; ENSMUSG00000023942.
DR   GeneID; 63959; -.
DR   KEGG; mmu:63959; -.
DR   UCSC; uc008cra.1; mouse.
DR   UCSC; uc008crb.1; mouse.
DR   CTD; 63959; -.
DR   MGI; MGI:1927073; Slc29a1.
DR   GeneTree; ENSGT00390000002232; -.
DR   HOGENOM; HBG714196; -.
DR   HOVERGEN; HBG074626; -.
DR   InParanoid; Q9JIM1; -.
DR   OMA; IKIMLIN; -.
DR   OrthoDB; EOG48PMKH; -.
DR   PhylomeDB; Q9JIM1; -.
DR   ArrayExpress; Q9JIM1; -.
DR   Bgee; Q9JIM1; -.
DR   Genevestigator; Q9JIM1; -.
DR   GermOnline; ENSMUSG00000023942; Mus musculus.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005337; F:nucleoside transmembrane transporter activity; IDA:MGI.
DR   InterPro; IPR002259; DER/eqnu_transpt.
DR   PANTHER; PTHR10332; DER/eqnu_transpt; 1.
DR   Pfam; PF01733; Nucleoside_tran; 1.
DR   PRINTS; PR01130; DERENTRNSPRT.
DR   TIGRFAMs; TIGR00939; 2a57; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW   Phosphoprotein; Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    460       Equilibrative nucleoside transporter 1.
FT                                /FTId=PRO_0000209338.
FT   TOPO_DOM      2     12       Cytoplasmic (Potential).
FT   TRANSMEM     13     29       Helical; (Potential).
FT   TOPO_DOM     30     82       Extracellular (Potential).
FT   TRANSMEM     83    107       Helical; (Potential).
FT   TOPO_DOM    108    111       Cytoplasmic (Potential).
FT   TRANSMEM    112    130       Helical; (Potential).
FT   TOPO_DOM    131    138       Extracellular (Potential).
FT   TRANSMEM    139    157       Helical; (Potential).
FT   TOPO_DOM    158    174       Cytoplasmic (Potential).
FT   TRANSMEM    175    199       Helical; (Potential).
FT   TOPO_DOM    200    206       Extracellular (Potential).
FT   TRANSMEM    207    227       Helical; (Potential).
FT   TOPO_DOM    228    291       Cytoplasmic (Potential).
FT   TRANSMEM    292    311       Helical; (Potential).
FT   TOPO_DOM    312    323       Extracellular (Potential).
FT   TRANSMEM    324    342       Helical; (Potential).
FT   TOPO_DOM    343    359       Cytoplasmic (Potential).
FT   TRANSMEM    360    378       Helical; (Potential).
FT   TOPO_DOM    379    397       Extracellular (Potential).
FT   TRANSMEM    398    417       Helical; (Potential).
FT   TOPO_DOM    418    435       Cytoplasmic (Potential).
FT   TRANSMEM    436    456       Helical; (Potential).
FT   TOPO_DOM    457    460       Extracellular (Potential).
FT   MOD_RES     254    254       Phosphoserine (By similarity).
FT   CARBOHYD     48     48       N-linked (GlcNAc...).
FT   VAR_SEQ     254    256       SKG -> R (in isoform 2).
FT                                /FTId=VSP_010471.
FT   CONFLICT     54     54       D -> G (in Ref. 3; BAB23537).
FT   CONFLICT    138    138       I -> T (in Ref. 4; AAH04828).
FT   CONFLICT    372    372       I -> V (in Ref. 4; AAH04828).
SQ   SEQUENCE   460 AA;  50192 MW;  FE37EEA155F9AB2F CRC64;
     MTTSHQPQDR YKAVWLIFFV LGLGTLLPWN FFMTATKYFT NRLDVSQNVS SDTDQSCEST
     KALADPTVAL PARSSLSAIF NNVMTLCAML PLLVFTCLNS FLHQRISQSV RILGSLLAIL
     LVFLVTAALV KVEMDALIFF VITMIKIVLI NSFGAILQAS LFGLAGVLPA NYTAPIMSGQ
     GLAGFFTSVA MICAIASGSE LSESAFGYFI TACAVVILAI LCYLALPRTE FYRHYLQLNL
     AGPAEQETKL DLISKGEEPK GRREESGVPG PNSPPTNRNQ SIKAILKSIC VPALSVCFIF
     TVTIGLFPAV TAEVESSIAG TSPWKSYFIP VACFLNFNVF DWLGRSLTAV CMWPGQDSRW
     LPVLVASRIV FIPLLMLCNV KARHCGAQRH HFVFKHDAWF IAFMAAFAFS NGYLASLCMC
     FGPKKVKPAE AETAGNIMSF FLCLGLALGA VLSFLLRALV
//
ID   SV2A_MOUSE              Reviewed;         742 AA.
AC   Q9JIS5; Q80TT0; Q8R0R5;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Synaptic vesicle glycoprotein 2A;
DE            Short=Synaptic vesicle protein 2;
DE            Short=Synaptic vesicle protein 2A;
DE   AltName: Full=Calcium regulator SV2A;
GN   Name=Sv2a; Synonyms=Kiaa0736, Sv2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=129/Sv;
RX   MEDLINE=20088300; PubMed=10624962; DOI=10.1016/S0896-6273(00)81046-6;
RA   Janz R., Goda Y., Geppert M., Missler M., Suedhof T.C.;
RT   "SV2A and SV2B function as redundant Ca2+ regulators in
RT   neurotransmitter release.";
RL   Neuron 24:1003-1016(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=10611374; DOI=10.1073/pnas.96.26.15268;
RA   Crowder K.M., Gunther J.M., Jones T.A., Hale B.D., Zhang H.Z.,
RA   Peterson M.R., Scheller R.H., Chavkin C., Bajjalieh S.M.;
RT   "Abnormal neurotransmission in mice lacking synaptic vesicle protein
RT   2A (SV2A).";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:15268-15273(1999).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=11483953; DOI=10.1038/35087000;
RA   Xu T., Bajjalieh S.M.;
RT   "SV2 modulates the size of the readily releasable pool of secretory
RT   vesicles.";
RL   Nat. Cell Biol. 3:691-698(2001).
RN   [8]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=12687700; DOI=10.1002/cne.10636;
RA   Wang M.M., Janz R., Belizaire R., Frishman L.J., Sherry D.M.;
RT   "Differential distribution and developmental expression of synaptic
RT   vesicle protein 2 isoforms in the mouse retina.";
RL   J. Comp. Neurol. 460:106-122(2003).
RN   [9]
RP   FUNCTION.
RX   PubMed=16436618; DOI=10.1523/JNEUROSCI.2699-05.2006;
RA   Custer K.L., Austin N.S., Sullivan J.M., Bajjalieh S.M.;
RT   "Synaptic vesicle protein 2 enhances release probability at quiescent
RT   synapses.";
RL   J. Neurosci. 26:1303-1313(2006).
RN   [10]
RP   FUNCTION AS A BOTA RECEPTOR, AND DISRUPTION PHENOTYPE.
RX   PubMed=16543415; DOI=10.1126/science.1123654;
RA   Dong M., Yeh F., Tepp W.H., Dean C., Johnson E.A., Janz R.,
RA   Chapman E.R.;
RT   "SV2 is the protein receptor for botulinum neurotoxin A.";
RL   Science 312:592-596(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-65; TYR-66 AND TYR-480,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Plays a role in the control of regulated secretion in
CC       neural and endocrine cells, enhancing selectively low-frequency
CC       neurotransmission. Positively regulates vesicle fusion by
CC       maintaining the readily releasable pool of secretory vesicles.
CC   -!- FUNCTION: Receptor for the botulinium neurotoxin type A/BOTA.
CC   -!- SUBUNIT: Interacts with SYT1/synaptotagmin-1 in a calcium-
CC       dependent manner. Binds the adapter protein complex AP-2 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane; Multi-pass membrane protein (By
CC       similarity). Note=Enriched in chromaffin granules, not present in
CC       adrenal microsomes. Associated with both insulin granules and
CC       synaptic-like microvesicles in insulin-secreting cells of the
CC       pancreas (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in conventional synapses and cone
CC       ribbon synapses in the retina (at protein level).
CC   -!- DEVELOPMENTAL STAGE: Expressed during synaptogenesis in the retina
CC       (at protein level).
CC   -!- PTM: Phosphorylation by CK1 of the N-terminal cytoplasmic domain
CC       regulates interaction with SYT1 (By similarity).
CC   -!- PTM: N-glycosylated (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice fail to grow, experience severe
CC       epileptic seizures and die immediately or shortly after birth
CC       probably due to multiple neural and endocrine deficits. Mice
CC       lacking both Sv2a and Sv2b display a similar phenotype.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65642.3; Type=Frameshift; Positions=72;
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DR   EMBL; AF196781; AAF87321.1; -; Genomic_DNA.
DR   EMBL; AF196780; AAF87321.1; JOINED; Genomic_DNA.
DR   EMBL; AK122360; BAC65642.3; ALT_SEQ; Transcribed_RNA.
DR   EMBL; AK028318; BAC25876.1; -; mRNA.
DR   EMBL; BC026494; AAH26494.1; -; mRNA.
DR   EMBL; BC046587; AAH46587.1; -; mRNA.
DR   IPI; IPI00465810; -.
DR   RefSeq; NP_071313.1; NM_022030.3.
DR   UniGene; Mm.480601; -.
DR   ProteinModelPortal; Q9JIS5; -.
DR   STRING; Q9JIS5; -.
DR   PhosphoSite; Q9JIS5; -.
DR   PRIDE; Q9JIS5; -.
DR   Ensembl; ENSMUST00000035371; ENSMUSP00000037576; ENSMUSG00000038486.
DR   GeneID; 64051; -.
DR   KEGG; mmu:64051; -.
DR   UCSC; uc008qmf.1; mouse.
DR   CTD; 64051; -.
DR   MGI; MGI:1927139; Sv2a.
DR   eggNOG; roNOG15218; -.
DR   GeneTree; ENSGT00550000074384; -.
DR   HOGENOM; HBG445732; -.
DR   HOVERGEN; HBG053967; -.
DR   InParanoid; Q9JIS5; -.
DR   OMA; YASRTKV; -.
DR   OrthoDB; EOG4K0QMZ; -.
DR   PhylomeDB; Q9JIS5; -.
DR   NextBio; 319875; -.
DR   ArrayExpress; Q9JIS5; -.
DR   Bgee; Q9JIS5; -.
DR   CleanEx; MM_SV2A; -.
DR   Genevestigator; Q9JIS5; -.
DR   GermOnline; ENSMUSG00000038486; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:MGI.
DR   GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR   GO; GO:0007268; P:synaptic transmission; TAS:MGI.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR020846; Major_facilitator_SF.
DR   InterPro; IPR011701; MFS_1.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   InterPro; IPR005828; Sub_transporter.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   InterPro; IPR022308; SV2_chordata.
DR   Pfam; PF07690; MFS_1; 1.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
DR   TIGRFAMs; TIGR01299; synapt_SV2; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cytoplasmic vesicle; Glycoprotein; Membrane;
KW   Neurotransmitter transport; Phosphoprotein; Receptor; Synapse;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    742       Synaptic vesicle glycoprotein 2A.
FT                                /FTId=PRO_0000239766.
FT   TOPO_DOM      1    169       Cytoplasmic (Potential).
FT   TRANSMEM    170    190       Helical; (Potential).
FT   TOPO_DOM    191    205       Extracellular (Potential).
FT   TRANSMEM    206    226       Helical; (Potential).
FT   TOPO_DOM    227    233       Cytoplasmic (Potential).
FT   TRANSMEM    234    254       Helical; (Potential).
FT   TOPO_DOM    255    262       Extracellular (Potential).
FT   TRANSMEM    263    283       Helical; (Potential).
FT   TOPO_DOM    284    294       Cytoplasmic (Potential).
FT   TRANSMEM    295    315       Helical; (Potential).
FT   TOPO_DOM    316    334       Extracellular (Potential).
FT   TRANSMEM    335    355       Helical; (Potential).
FT   TOPO_DOM    356    447       Cytoplasmic (Potential).
FT   TRANSMEM    448    468       Helical; (Potential).
FT   TOPO_DOM    469    598       Extracellular (Potential).
FT   TRANSMEM    599    619       Helical; (Potential).
FT   TOPO_DOM    620    626       Cytoplasmic (Potential).
FT   TRANSMEM    627    647       Helical; (Potential).
FT   TOPO_DOM    648    651       Extracellular (Potential).
FT   TRANSMEM    652    672       Helical; (Potential).
FT   TOPO_DOM    673    685       Cytoplasmic (Potential).
FT   TRANSMEM    686    708       Helical; (Potential).
FT   TOPO_DOM    709    712       Extracellular (Potential).
FT   TRANSMEM    713    731       Helical; (Potential).
FT   TOPO_DOM    732    742       Cytoplasmic (Potential).
FT   REGION        1     57       Interaction with SYT1 (By similarity).
FT   REGION      543    580       BOTA-binding (By similarity).
FT   MOD_RES      65     65       Phosphotyrosine.
FT   MOD_RES      66     66       Phosphotyrosine.
FT   MOD_RES      80     80       Phosphoserine (By similarity).
FT   MOD_RES      81     81       Phosphoserine (By similarity).
FT   MOD_RES      84     84       Phosphothreonine (By similarity).
FT   MOD_RES     127    127       Phosphoserine.
FT   MOD_RES     480    480       Phosphotyrosine.
FT   CARBOHYD    498    498       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    548    548       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    573    573       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   742 AA;  82647 MW;  1074857FD13ED894 CRC64;
     MEEGFRDRAA FIRGAKDIAK EVKKHAAKKV VKGLDRVQDE YSRRSYSRFE EEDDDDDFPA
     PADGYYRGEG AQDEEEGGAS SDATEGHDED DEIYEGEYQG IPRAESGGKG ERMADGAPLA
     GVRGGLSDGE GPPGGRGEAQ RRKDREELAQ QYETILRECG HGRFQWTLYF VLGLALMADG
     VEVFVVGFVL PSAEKDMCLS DSNKGMLGLI VYLGMMVGAF LWGGLADRLG RRQCLLISLS
     VNSVFAFFSS FVQGYGTFLF CRLLSGVGIG GSIPIVFSYF SEFLAQEKRG EHLSWLCMFW
     MIGGVYAAAM AWAIIPHYGW SFQMGSAYQF HSWRVFVLVC AFPSVFAIGA LTTQPESPRF
     FLENGKHDEA WMVLKQVHDT NMRAKGHPER VFSVTHIKTI HQEDELIEIQ SDTGTWYQRW
     GVRALSLGGQ VWGNFLSCFS PEYRRITLMM MGVWFTMSFS YYGLTVWFPD MIRHLQAVDY
     AARTKVFPGE RVEHVTFNFT LENQIHRGGQ YFNDKFIGLR LKSVSFEDSL FEECYFEDVT
     SSNTFFRNCT FINTVFYNTD LFEYKFVNSR LVNSTFLHNK EGCPLDVTGT GEGAYMVYFV
     SFLGTLAVLP GNIVSALLMD KIGRLRMLAG SSVLSCVSCF FLSFGNSESA MIALLCLFGG
     VSIASWNALD VLTVELYPSD KRTTAFGFLN ALCKLAAVLG ISIFTSFVGI TKAAPILFAS
     AALALGSSLA LKLPETRGQV LQ
//
ID   S12A4_MOUSE             Reviewed;        1085 AA.
AC   Q9JIS8; O55069; Q9ET57;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2002, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Solute carrier family 12 member 4;
DE   AltName: Full=Electroneutral potassium-chloride cotransporter 1;
DE   AltName: Full=Erythroid K-Cl cotransporter 1;
DE            Short=mKCC1;
GN   Name=Slc12a4; Synonyms=Kcc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=DBA; TISSUE=Erythroleukemia;
RX   MEDLINE=98184935; PubMed=9516379; DOI=10.1006/bcmd.1998.0168;
RA   Pellegrino C.M., Rybicki A.C., Musto S., Nagel R.L., Schwartz R.S.;
RT   "Molecular identification and expression of erythroid K:Cl
RT   cotransporter in human and mouse erythroleukemic cells.";
RL   Blood Cells Mol. Dis. 24:31-40(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   STRAIN=CD-1; TISSUE=Brain, and Spleen;
RX   MEDLINE=20035026; PubMed=10564083;
RA   Su W., Shmukler B.E., Chernova M.N., Stuart-Tilley A.K.,
RA   de Franceschi L., Brugnara C., Alper S.L.;
RT   "Mouse K-Cl cotransporter KCC1: cloning, mapping, pathological
RT   expression, and functional regulation.";
RL   Am. J. Physiol. 277:C899-C912(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=20461840; PubMed=11004507; DOI=10.1016/S0167-4781(00)00118-4;
RA   Shmukler B.E., Brugnara C., Alper S.L.;
RT   "Structure and genetic polymorphism of the mouse KCC1 gene.";
RL   Biochim. Biophys. Acta 1492:353-361(2000).
RN   [4]
RP   SUBUNIT.
RX   MEDLINE=21551256; PubMed=11551954; DOI=10.1074/jbc.M107155200;
RA   Casula S., Shmukler B.E., Wilhelm S., Stuart-Tilley A.K., Su W.,
RA   Chernova M.N., Brugnara C., Alper S.L.;
RT   "A dominant negative mutant of the KCC1 K-Cl cotransporter: both N-
RT   and C-terminal cytoplasmic domains are required for K-Cl cotransport
RT   activity.";
RL   J. Biol. Chem. 276:41870-41878(2001).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-967, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND THR-983, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-331, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-331, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Mediates electroneutral potassium-chloride cotransport
CC       when activated by cell swelling. May contribute to cell volume
CC       homeostasis in single cells. May be involved in the regulation of
CC       basolateral Cl(-) exit in NaCl absorbing epithelia.
CC   -!- SUBUNIT: Homomultimer and heteromultimer with other K-Cl
CC       cotransporters.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Detected in embryo, adult heart, erythrocytes,
CC       brain, kidney, stomach, ovary, testis and liver.
CC   -!- DEVELOPMENTAL STAGE: Expression levels remained constant upon
CC       induction of erythroid differentiation of embryonic stem cells.
CC       Not detected in reticulocytes, but present during differentiation
CC       of erythroleukemia cells to erythroblasts.
CC   -!- PTM: N-glycosylated.
CC   -!- MISCELLANEOUS: Activated by N-ethylmaleimide (NEM). Inhibited by
CC       DIOA.
CC   -!- SIMILARITY: Belongs to the SLC12A transporter family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF047339; AAC32816.1; -; mRNA.
DR   EMBL; AF121118; AAF02444.1; -; mRNA.
DR   EMBL; AF191023; AAF91094.1; -; Genomic_DNA.
DR   EMBL; AF190018; AAF91090.1; -; Genomic_DNA.
DR   EMBL; AF190016; AAF91090.1; JOINED; Genomic_DNA.
DR   EMBL; AF190017; AAF91090.1; JOINED; Genomic_DNA.
DR   IPI; IPI00889900; -.
DR   RefSeq; NP_033221.1; NM_009195.2.
DR   UniGene; Mm.292447; -.
DR   UniGene; Mm.396326; -.
DR   ProteinModelPortal; Q9JIS8; -.
DR   STRING; Q9JIS8; -.
DR   PhosphoSite; Q9JIS8; -.
DR   PRIDE; Q9JIS8; -.
DR   Ensembl; ENSMUST00000116429; ENSMUSP00000112130; ENSMUSG00000017765.
DR   GeneID; 20498; -.
DR   KEGG; mmu:20498; -.
DR   UCSC; uc009ner.1; mouse.
DR   CTD; 20498; -.
DR   MGI; MGI:1309465; Slc12a4.
DR   eggNOG; roNOG12599; -.
DR   HOVERGEN; HBG052852; -.
DR   OMA; DTVRCTT; -.
DR   OrthoDB; EOG476JZG; -.
DR   PhylomeDB; Q9JIS8; -.
DR   NextBio; 298659; -.
DR   ArrayExpress; Q9JIS8; -.
DR   Bgee; Q9JIS8; -.
DR   CleanEx; MM_SLC12A4; -.
DR   Genevestigator; Q9JIS8; -.
DR   GermOnline; ENSMUSG00000017765; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015377; F:cation:chloride symporter activity; IEA:InterPro.
DR   GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR   InterPro; IPR004841; AA-permease_dom.
DR   InterPro; IPR000622; K/Cl_cotranspt1.
DR   InterPro; IPR018491; K/Cl_cotranspt_1/3.
DR   InterPro; IPR000076; KCL_cotranspt.
DR   InterPro; IPR004842; Na/K/Cl_cotransptS.
DR   Pfam; PF00324; AA_permease; 2.
DR   Pfam; PF03522; KCl_Cotrans_1; 1.
DR   PRINTS; PR01081; KCLTRNSPORT.
DR   PRINTS; PR01082; KCLTRNSPORT1.
DR   TIGRFAMs; TIGR00930; 2a30; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Ion transport; Membrane; Phosphoprotein; Potassium;
KW   Potassium transport; Symport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1   1085       Solute carrier family 12 member 4.
FT                                /FTId=PRO_0000178031.
FT   TOPO_DOM      1    118       Cytoplasmic (Potential).
FT   TRANSMEM    119    139       Helical; (Potential).
FT   TRANSMEM    149    169       Helical; (Potential).
FT   TOPO_DOM    170    214       Cytoplasmic (Potential).
FT   TRANSMEM    215    235       Helical; (Potential).
FT   TRANSMEM    253    273       Helical; (Potential).
FT   TOPO_DOM    274    275       Cytoplasmic (Potential).
FT   TRANSMEM    276    296       Helical; (Potential).
FT   TRANSMEM    356    376       Helical; (Potential).
FT   TOPO_DOM    377    415       Cytoplasmic (Potential).
FT   TRANSMEM    416    436       Helical; (Potential).
FT   TRANSMEM    453    473       Helical; (Potential).
FT   TOPO_DOM    474    493       Cytoplasmic (Potential).
FT   TRANSMEM    494    514       Helical; (Potential).
FT   TRANSMEM    567    587       Helical; (Potential).
FT   TOPO_DOM    588    627       Cytoplasmic (Potential).
FT   TRANSMEM    628    648       Helical; (Potential).
FT   TRANSMEM    845    865       Helical; (Potential).
FT   TOPO_DOM    866   1085       Cytoplasmic (Potential).
FT   COMPBIAS    160    163       Poly-Cys.
FT   COMPBIAS    969    972       Poly-Glu.
FT   MOD_RES      47     47       Phosphoserine.
FT   MOD_RES     967    967       Phosphoserine.
FT   MOD_RES     983    983       Phosphothreonine.
FT   CARBOHYD    312    312       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    331    331       N-linked (GlcNAc...).
FT   CARBOHYD    347    347       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    439    439       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   1085 AA;  120624 MW;  9094931060972E03 CRC64;
     MPHFTVVPVD GPRRGDYDNL EGLSWVDYGE RAEREDSDGQ GNHRENSPFL CPLDASRGND
     YYDRNLALFE EELDIRPKVS SLLGKLVSYT NLTQGAKEHE EAESGEGGRR RAAKAPSMGT
     LMGVYLPCLQ NIFGVILFLR LTWMVGTAGV LQALLIVLIC CCCTLLTAIS MSAIATNGVV
     PAGGSYFMIS RSLGPEFGGA VGLCFYLGTT FAAAMYILGA IEILLTYIAP PAAIFYPSGT
     HDMSSATLNN MRVYGTIFLT LMTLVVFVGV KYVNKFASLF LACVIISILS IYAGGIKSIF
     DPPVFPVCML GNRTLSRDQF DICAKTVVVD NETVATRLWT FFCHSPNLTA DSCDPYFLLN
     NVTEIPGIPG AAAGVLQENL WSAYLEKGEV VEKHGLPSTD TLGLKESLSL YVVADIATSF
     TVLVGIFFPS VTGIMAGSNR SGDLRDAQKS IPVGTILAIV TTSLVYFSSV ILFGACIEGV
     VLRDKYGDGV SRNLVVGTLA WPSPWVIVVG SFFSTCGAGL QSLTGAPRLL QAIAKDNIIP
     FLRVFGHGKA NGEPTWALLL TALIAELGIL IASLDMVAPI LSMFFLMCYL FVNLACAVQT
     LLRTPNWRPR FKYYHWTLSF LGMSLCLALM FVSSWYYALV AMLIAGMIYK YIEYQGAEKE
     WGDGIRGLSL SAARYALLRL EEGPPHTKNW RPQLLVLLKL DEDLHVKYPR LLTFASQLKA
     GKGLTIVGSV IQGSFLESYG EAQAAEQTIK NMMDIEKVKG FCQVVVASKV REGLAHLIQS
     CGLGGMRHNS VVLGWPYGWR QSEDPRAWKT FIDTVRCTTA AHLALLVPKN IAFYPSNHER
     YLDGHIDVWW IVHDGGMLML LPFLLRQHKV WKKCRMRIFT VAQMDDNSIQ MKKDLAIFLY
     HLRLEAEVEV VEMHNSDISA YTYERTLMME QRSQMLRQMR LTKTERDREA QLVKDRHSAL
     RLESLYSDEE EESVAGADKI QMTWTRDKYM AEPWDPSHAP DNFRELVHIK PDQSNVRRMH
     TAVKLNEVIV TRSHDARLVL LNMPGPPKNS EGDENYMEFL EVLTEGLERV LLVRGGGREV
     ITIYS
//
ID   PKHO1_MOUSE             Reviewed;         408 AA.
AC   Q9JIY0; Q9CXH2;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Pleckstrin homology domain-containing family O member 1;
DE            Short=PH domain-containing family O member 1;
GN   Name=Plekho1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kohchi C., Shige K.;
RT   "Identification of a protein that associates with TNF intracellular
RT   domain.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION.
RX   PubMed=17942896; DOI=10.1158/0008-5472.CAN-07-1050;
RA   Tokuda E., Fujita N., Oh-hara T., Sato S., Kurata A., Katayama R.,
RA   Itoh T., Takenawa T., Miyazono K., Tsuruo T.;
RT   "Casein kinase 2-interacting protein-1, a novel Akt pleckstrin
RT   homology domain-interacting protein, down-regulates PI3K/Akt signaling
RT   and suppresses tumor growth in vivo.";
RL   Cancer Res. 67:9666-9676(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; SER-226 AND
RP   SER-270, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Plays a role in the regulation of the actin cytoskeleton
CC       through its interactions with actin capping protein (CP). May
CC       function to target CK2 to the plasma membrane thereby serving as
CC       an adapter to facilitate the phosphorylation of CP by protein
CC       kinase 2 (CK2). Appears to target ATM to the plasma membrane.
CC       Appears to also inhibit tumor cell growth by inhibiting AKT-
CC       mediated cell-survival. Also implicated in PI3K-regulated muscle
CC       differentiation, the regulation of AP-1 activity (plasma membrane
CC       bound AP-1 regulator that translocates to the nucleus) and the
CC       promotion of apoptosis induced by tumor necrosis factor TNF. When
CC       bound to PKB, it inhibits it probably by decreasing PKB level of
CC       phosphorylation (By similarity).
CC   -!- SUBUNIT: Heterodimer or homodimer. Interacts with CK2 and actin
CC       capping subunits (capping protein CP-alpha and CP-beta). CKIP1 and
CC       CK2 together inhibit the activity of actin capping protein at the
CC       barbed ends of actin filaments. Interacts with ATM, IFP35, JUN,
CC       JUND, NMI and PI3K. Interacts with AKT1, AKT2 and AKT3 (each
CC       isozyme of PKB), PtdIns(3,5)P2, PtdIns(4,5)P2 and PtdIns(3,4,5)P2
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane (By similarity). Nucleus (By
CC       similarity). Cytoplasm (By similarity).
CC   -!- PTM: C-terminal fragments could be released during apoptosis via
CC       caspase-3-dependent cleavage (By similarity).
CC   -!- SIMILARITY: Contains 1 PH domain.
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DR   EMBL; AF168675; AAF89643.1; -; mRNA.
DR   EMBL; AK014374; BAB29306.1; -; mRNA.
DR   EMBL; AK170025; BAE41517.1; -; mRNA.
DR   EMBL; AK170922; BAE42115.1; -; mRNA.
DR   EMBL; BC117003; AAI17004.1; -; mRNA.
DR   EMBL; BC125441; AAI25442.1; -; mRNA.
DR   IPI; IPI00471230; -.
DR   RefSeq; NP_075809.1; NM_023320.2.
DR   UniGene; Mm.458147; -.
DR   HSSP; Q9HB21; 1EAZ.
DR   ProteinModelPortal; Q9JIY0; -.
DR   SMR; Q9JIY0; 20-131.
DR   STRING; Q9JIY0; -.
DR   PhosphoSite; Q9JIY0; -.
DR   PRIDE; Q9JIY0; -.
DR   Ensembl; ENSMUST00000015889; ENSMUSP00000015889; ENSMUSG00000015745.
DR   GeneID; 67220; -.
DR   KEGG; mmu:67220; -.
DR   UCSC; uc008qlx.1; mouse.
DR   CTD; 67220; -.
DR   MGI; MGI:1914470; Plekho1.
DR   eggNOG; roNOG06126; -.
DR   GeneTree; ENSGT00530000063760; -.
DR   HOGENOM; HBG506089; -.
DR   HOVERGEN; HBG108259; -.
DR   InParanoid; Q9JIY0; -.
DR   OMA; RDRAKIQ; -.
DR   PhylomeDB; Q9JIY0; -.
DR   NextBio; 323920; -.
DR   ArrayExpress; Q9JIY0; -.
DR   Bgee; Q9JIY0; -.
DR   Genevestigator; Q9JIY0; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Membrane; Nucleus; Phosphoprotein; Tumor suppressor.
FT   CHAIN         1    408       Pleckstrin homology domain-containing
FT                                family O member 1.
FT                                /FTId=PRO_0000310424.
FT   DOMAIN       20    131       PH.
FT   REGION      132    192       Interaction with capping proteins (CPs)
FT                                (By similarity).
FT   REGION      135    307       Interaction with ATM, CKIP, IFP35 and NMI
FT                                (By similarity).
FT   REGION      307    408       Negative regulator of AP-1 activity (By
FT                                similarity).
FT   BINDING     154    154       Capping protein (By similarity).
FT   BINDING     156    156       Capping protein (By similarity).
FT   SITE        309    310       Cleavage; by caspase-3 (Potential).
FT   SITE        344    345       Cleavage; by caspase-3 (Potential).
FT   MOD_RES     220    220       Phosphoserine.
FT   MOD_RES     226    226       Phosphoserine.
FT   MOD_RES     270    270       Phosphoserine.
FT   CONFLICT    116    116       P -> S (in Ref. 2; BAB29306).
SQ   SEQUENCE   408 AA;  45997 MW;  33C36EC5DC8D4A72 CRC64;
     MKKSGSGKRG PPDGNHQSAA PEKVGWVRKF CGKGIFREIW KNRYVVLKGD QLYVSEKEVK
     DEKNSQEVFD LSDYEKCEEL RKSKSRSKKN HSKFTLARCR QPGTTAPNLI FLAVSPEEKE
     SWINALSSAI TRAKNRILDE VTVEEDSYLA HPTRDRAKIQ HSRRPPTRGH LMAVASTSTS
     DGMLTLDLIQ EEDPSPEEPA SCAESFRVDL DKSVAQLAGS RRRADSDRIQ PSSQRASSLS
     RPWEKPDKGA PYTPQALKKF PSTEKSRCAS LEEILSQRDT APARPLHLQA EESLPPVPAQ
     PGQLSRIQDL VARKLEKTQE LLAEVQGLGD GKRKAKDPPQ SPPDSESEQL LLETERLLGE
     ASSNWSQAKR VLQEVRELRD LYRQMDLQTP DSHLRQTSQH SQYRKSLM
//
ID   KCIP2_MOUSE             Reviewed;         270 AA.
AC   Q9JJ69; Q6DTJ2; Q8K1T8; Q8K1T9; Q8K1U0; Q8VHN4; Q8VHN5; Q8VHN6;
AC   Q9JJ68;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Kv channel-interacting protein 2;
DE            Short=KChIP2;
DE   AltName: Full=A-type potassium channel modulatory protein 2;
DE   AltName: Full=Potassium channel-interacting protein 2;
GN   Name=Kcnip2; Synonyms=Kchip2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND TISSUE SPECIFICITY.
RC   TISSUE=Aorta, Brain, Heart, and Stomach;
RX   MEDLINE=21164705; PubMed=11263977; DOI=10.1006/bbrc.2001.4558;
RA   Ohya S., Morohashi Y., Muraki K., Tomita T., Watanabe M., Iwatsubo T.,
RA   Imaizumi Y.;
RT   "Molecular cloning and expression of the novel splice variants of K(+)
RT   channel-interacting protein 2.";
RL   Biochem. Biophys. Res. Commun. 282:96-102(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, TISSUE
RP   SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=BALB/c;
RX   MEDLINE=21614492; PubMed=11747815; DOI=10.1016/S0092-8674(01)00588-8;
RA   Kuo H.-C., Cheng C.-F., Clark R.B., Lin J.J.C., Lin J.L.C.,
RA   Hoshijima M., Nguyen-Tran V.T.B., Gu Y., Ikeda Y., Chu P.-H.,
RA   Ross J. Jr., Giles W.R., Chien K.R.;
RT   "A defect in the Kv channel-interacting protein 2 (KChIP2) gene leads
RT   to a complete loss of I(to) and confers susceptibility to ventricular
RT   tachycardia.";
RL   Cell 107:801-813(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RA   Xia K.U., Fang H.Y., Zhong X.Y., Xia J.H., Zhang Z.H.;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 19-270 (ISOFORMS 1; 2 AND 3).
RA   Franz O., Soloviev M., Roeper J.;
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   INTERACTION WITH KCND2 AND KCND3.
RX   MEDLINE=21906624; PubMed=11909823;
RX   DOI=10.1161/01.RES.0000012664.05949.E0;
RA   Guo W., Li H., Aimond F., Johns D.C., Rhodes K.J., Trimmer J.S.,
RA   Nerbonne J.M.;
RT   "Role of heteromultimers in the generation of myocardial transient
RT   outward K+ currents.";
RL   Circ. Res. 90:586-593(2002).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=15363885; DOI=10.1016/j.molbrainres.2004.06.024;
RA   Xiong H., Kovacs I., Zhang Z.;
RT   "Differential distribution of KChIPs mRNAs in adult mouse brain.";
RL   Brain Res. Mol. Brain Res. 128:103-111(2004).
CC   -!- FUNCTION: Regulatory subunit of Kv4/D (Shal)-type voltage-gated
CC       rapidly inactivating A-type potassium channels. Probably modulates
CC       channels density, inactivation kinetics and rate of recovery from
CC       inactivation in a calcium-dependent and isoform-specific manner.
CC       In vitro, modulates KCND2/Kv4.2 and KCND3/Kv4.3 currents. Involved
CC       in KCND2 and KCNDV3 trafficking to the cell surface (By
CC       similarity).
CC   -!- SUBUNIT: Component of heteromultimeric potassium channels. The
CC       KCND2-KCNIP2 channel complex contains four KCND2 and four KCNIP2
CC       subunits. Probably part of a complex consisting of KCNIP1, KCNIP2
CC       isoform 3 and KCND2. At least isoform 2 and isoform 3 can self-
CC       associate to form homodimers and homotetramers. Isoform 3
CC       interacts with KCNIP1 in a calcium-dependent manner (By
CC       similarity). Interacts with KCND2. Isoform 1 and isoform 3
CC       interact with KCND3 isoform 1.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=A, KChIP2a, KCHIP2B, KChIP2L;
CC         IsoId=Q9JJ69-1; Sequence=Displayed;
CC       Name=2; Synonyms=B, KChIP2b, KCHIP2C;
CC         IsoId=Q9JJ69-2; Sequence=VSP_015061;
CC       Name=3; Synonyms=KCHIP2A, KChIP2b, KChIP2c, KChIP2S;
CC         IsoId=Q9JJ69-3; Sequence=VSP_015060;
CC       Name=4;
CC         IsoId=Q9JJ69-4; Sequence=VSP_015059;
CC   -!- TISSUE SPECIFICITY: Expressed in brain. Highly expressed in layer
CC       IV of the cerebral cortex and in striatum and hippocampus, but
CC       expressed at low levels in cerebellum. Also expressed in heart.
CC       According to PubMed:11747815 expressed in heart at much higher
CC       levels than in brain.
CC   -!- PTM: Palmitoylated. Palmitoylation enhances association with the
CC       plasma membrane (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice are highly susceptible to the induction
CC       of cardiac arrhythmias and show a loss of I(To) current in heart.
CC   -!- SIMILARITY: Belongs to the recoverin family.
CC   -!- SIMILARITY: Contains 4 EF-hand domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; AB044570; BAA96738.1; -; mRNA.
DR   EMBL; AB044571; BAA96739.1; -; mRNA.
DR   EMBL; AF439339; AAL32044.1; -; mRNA.
DR   EMBL; AF439340; AAL32045.1; -; mRNA.
DR   EMBL; AF439341; AAL32046.1; -; mRNA.
DR   EMBL; AY647241; AAT68467.1; -; mRNA.
DR   EMBL; AJ278535; CAC82023.1; -; mRNA.
DR   EMBL; AJ278536; CAC82024.1; -; mRNA.
DR   EMBL; AJ278537; CAC82026.1; -; mRNA.
DR   IPI; IPI00261304; -.
DR   IPI; IPI00399896; -.
DR   IPI; IPI00402825; -.
DR   IPI; IPI00457555; -.
DR   RefSeq; NP_109641.2; NM_030716.2.
DR   RefSeq; NP_663749.1; NM_145703.1.
DR   RefSeq; NP_663750.1; NM_145704.1.
DR   UniGene; Mm.213204; -.
DR   ProteinModelPortal; Q9JJ69; -.
DR   SMR; Q9JJ69; 27-60, 90-270.
DR   STRING; Q9JJ69; -.
DR   PhosphoSite; Q9JJ69; -.
DR   PRIDE; Q9JJ69; -.
DR   Ensembl; ENSMUST00000026247; ENSMUSP00000026247; ENSMUSG00000025221.
DR   Ensembl; ENSMUST00000079431; ENSMUSP00000078400; ENSMUSG00000025221.
DR   Ensembl; ENSMUST00000086993; ENSMUSP00000084215; ENSMUSG00000025221.
DR   GeneID; 80906; -.
DR   KEGG; mmu:80906; -.
DR   UCSC; uc008hrr.1; mouse.
DR   CTD; 80906; -.
DR   MGI; MGI:2135916; Kcnip2.
DR   GeneTree; ENSGT00560000076973; -.
DR   HOVERGEN; HBG108179; -.
DR   InParanoid; Q9JJ69; -.
DR   OMA; ILRGTTD; -.
DR   OrthoDB; EOG4K6G52; -.
DR   PhylomeDB; Q9JJ69; -.
DR   NextBio; 350258; -.
DR   ArrayExpress; Q9JJ69; -.
DR   Bgee; Q9JJ69; -.
DR   CleanEx; MM_KCNIP2; -.
DR   Genevestigator; Q9JJ69; -.
DR   GermOnline; ENSMUSG00000025221; Mus musculus.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR   InterPro; IPR018248; EF-hand.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR001125; Recoverin.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF00036; efhand; 1.
DR   PRINTS; PR00450; RECOVERIN.
DR   SMART; SM00054; EFh; 3.
DR   PROSITE; PS00018; EF_HAND_1; 3.
DR   PROSITE; PS50222; EF_HAND_2; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell membrane; Ion transport;
KW   Ionic channel; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW   Potassium; Potassium channel; Potassium transport; Repeat; Transport;
KW   Voltage-gated channel.
FT   CHAIN         1    270       Kv channel-interacting protein 2.
FT                                /FTId=PRO_0000073822.
FT   DOMAIN       81    137       EF-hand 1; degenerate.
FT   DOMAIN      140    175       EF-hand 2.
FT   DOMAIN      176    211       EF-hand 3.
FT   DOMAIN      224    259       EF-hand 4.
FT   CA_BIND     189    200       1 (By similarity).
FT   CA_BIND     237    248       2 (By similarity).
FT   REGION      257    270       Interaction with KCND2 (By similarity).
FT   MOD_RES     103    103       Phosphothreonine (By similarity).
FT   MOD_RES     111    111       Phosphotyrosine (By similarity).
FT   LIPID        45     45       S-palmitoyl cysteine (By similarity).
FT   LIPID        46     46       S-palmitoyl cysteine (By similarity).
FT   VAR_SEQ       1     73       MRGQGRKESLSDSRDLDGSYDQLTGHPPGPSKKALKQRFLK
FT                                LLPCCGPQALPSVSETLAAPASLRPHRPRPLD -> MNRCP
FT                                RRCRSPLGQAARSLYQLVTGSLS (in isoform 4).
FT                                /FTId=VSP_015059.
FT   VAR_SEQ      25     74       Missing (in isoform 3).
FT                                /FTId=VSP_015060.
FT   VAR_SEQ      57     75       TLAAPASLRPHRPRPLDPD -> N (in isoform 2).
FT                                /FTId=VSP_015061.
FT   CONFLICT     12     12       D -> E (in Ref. 2; AAL32044/AAL32045/
FT                                AAL32046).
FT   CONFLICT     31     31       S -> T (in Ref. 1; BAA96738).
FT   CONFLICT     50     50       A -> V (in Ref. 1; BAA96738).
FT   CONFLICT     75     75       D -> G (in Ref. 4; CAC82023).
FT   CONFLICT    105    105       R -> K (in Ref. 1; BAA96738/BAA96739).
FT   CONFLICT    143    143       N -> T (in Ref. 1; BAA96738/BAA96739).
FT   CONFLICT    177    177       I -> V (in Ref. 1; BAA96738/BAA96739).
FT   CONFLICT    239    239       N -> S (in Ref. 1; BAA96738/BAA96739).
FT   CONFLICT    248    248       E -> G (in Ref. 4; CAC82024).
FT   CONFLICT    255    255       Q -> K (in Ref. 1; BAA96738/BAA96739).
SQ   SEQUENCE   270 AA;  30946 MW;  DB5AC273B2C0F667 CRC64;
     MRGQGRKESL SDSRDLDGSY DQLTGHPPGP SKKALKQRFL KLLPCCGPQA LPSVSETLAA
     PASLRPHRPR PLDPDSVEDE FELSTVCHRP EGLEQLQEQT KFTRRELQVL YRGFKNECPS
     GIVNEENFKQ IYSQFFPQGD SSNYATFLFN AFDTNHDGSV SFEDFVAGLS VILRGTIDDR
     LNWAFNLYDL NKDGCITKEE MLDIMKSIYD MMGKYTYPAL REEAPREHVE SFFQKMDRNK
     DGVVTIEEFI ESCQQDENIM RSMQLFDNVI
//
ID   RPRM_MOUSE              Reviewed;         109 AA.
AC   Q9JJ72; Q8K1G8;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Protein reprimo;
GN   Name=Rprm;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INDUCTION,
RP   AND GLYCOSYLATION AT ASN-7 AND ASN-18.
RX   PubMed=10930422; DOI=10.1074/jbc.C000235200;
RA   Ohki R., Nemoto J., Murasawa H., Oda E., Inazawa J., Tanaka N.,
RA   Taniguchi T.;
RT   "Reprimo, a new candidate mediator of the p53-mediated cell cycle
RT   arrest at the G2 phase.";
RL   J. Biol. Chem. 275:22627-22630(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, and Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in the regulation of p53-dependent G2
CC       arrest of the cell cycle. Seems to induce cell cycle arrest by
CC       inhibiting CDK1 activity and nuclear translocation of the CDC2
CC       cyclin B1 complex.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Single-pass membrane
CC       protein (Potential).
CC   -!- INDUCTION: By p53/TP53, following X-ray irradiation.
CC   -!- MISCELLANEOUS: 'Reprimo' signifies stop/repress.
CC   -!- SIMILARITY: Belongs to the reprimo family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB043586; BAB01514.1; -; mRNA.
DR   EMBL; AK010465; BAB26960.1; -; mRNA.
DR   EMBL; AK014769; BAB29541.1; -; mRNA.
DR   EMBL; AL844850; CAM18780.1; -; Genomic_DNA.
DR   EMBL; BC030065; AAH30065.1; -; mRNA.
DR   IPI; IPI00462776; -.
DR   RefSeq; NP_075885.1; NM_023396.5.
DR   UniGene; Mm.27086; -.
DR   STRING; Q9JJ72; -.
DR   PRIDE; Q9JJ72; -.
DR   Ensembl; ENSMUST00000100089; ENSMUSP00000097667; ENSMUSG00000075334.
DR   GeneID; 67874; -.
DR   KEGG; mmu:67874; -.
DR   UCSC; uc008jrp.1; mouse.
DR   CTD; 67874; -.
DR   MGI; MGI:1915124; Rprm.
DR   eggNOG; roNOG16773; -.
DR   GeneTree; ENSGT00390000010523; -.
DR   HOGENOM; HBG269721; -.
DR   HOVERGEN; HBG105220; -.
DR   InParanoid; Q9JJ72; -.
DR   OMA; CCNFSSV; -.
DR   OrthoDB; EOG4S7JRH; -.
DR   NextBio; 325801; -.
DR   ArrayExpress; Q9JJ72; -.
DR   Bgee; Q9JJ72; -.
DR   Genevestigator; Q9JJ72; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007050; P:cell cycle arrest; IDA:MGI.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IDA:MGI.
PE   1: Evidence at protein level;
KW   Cytoplasm; Glycoprotein; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN         1    109       Protein reprimo.
FT                                /FTId=PRO_0000312753.
FT   TRANSMEM     56     76       Helical; (Potential).
FT   CARBOHYD      7      7       N-linked (GlcNAc...).
FT   CARBOHYD     18     18       N-linked (GlcNAc...).
FT   CONFLICT     17     17       V -> A (in Ref. 4; AAH30065).
SQ   SEQUENCE   109 AA;  11820 MW;  954F7C6397A84F9E CRC64;
     MNSVLGNQTD VAGLFLVNSS EALERAVRCC TQASVVTDDG FAEGGPDERS LYIMRVVQIA
     VMCVLSLTVV FGIFFLGCNL LIKSEGMINF LVKDRRPSKE VEAVVVGPY
//
ID   GRASP_MOUSE             Reviewed;         392 AA.
AC   Q9JJA9; Q9JKL0;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=General receptor for phosphoinositides 1-associated scaffold protein;
DE            Short=GRP1-associated scaffold protein;
GN   Name=Grasp; ORFNames=MNCb-4428;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH
RP   PSCD3, AND SUBCELLULAR LOCATION.
RX   MEDLINE=20287554; PubMed=10828067; DOI=10.1074/jbc.275.22.16827;
RA   Nevrivy D.J., Peterson V.J., Avram D., Ishmael J.E., Hansen S.G.,
RA   Dowell P., Hruby D.E., Dawson M.I., Leid M.;
RT   "Interaction of GRASP, a protein encoded by a novel retinoic acid-
RT   induced gene, with members of the cytohesin family of guanine
RT   nucleotide exchange factors.";
RL   J. Biol. Chem. 275:16827-16836(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S.,
RA   Hashimoto K.;
RT   "Isolation of full-length cDNA clones from mouse brain cDNA library
RT   made by oligo-capping method.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=21839219; PubMed=11850456;
RA   Kitano J., Kimura K., Yamazaki Y., Soda T., Shigemoto R., Nakajima Y.,
RA   Nakanishi S.;
RT   "Tamalin, a PDZ domain-containing protein, links a protein complex
RT   formation of group 1 metabotropic glutamate receptors and the guanine
RT   nucleotide exchange factor cytohesins.";
RL   J. Neurosci. 22:1280-1289(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Plays a role in intracellular trafficking and
CC       contributes to the macromolecular organization of group 1
CC       metabotropic glutamate receptors (mGluRs) at synapses (By
CC       similarity).
CC   -!- SUBUNIT: Heteromer. Composed of GRASP, PSCD2 and at least one
CC       GRM1. Also interacts with GRM2, GRM3 and GRM5 (By similarity).
CC       Interacts with PSCD3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Primarily
CC       localized to the plasma membrane but also distributed diffusely
CC       throughout the cytoplasm.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain, heart and lung, and
CC       to a lower extent in embryo, kidney and ovary.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF236099; AAF36997.1; -; mRNA.
DR   EMBL; AB041603; BAA95086.1; -; mRNA.
DR   EMBL; BC046307; AAH46307.1; -; mRNA.
DR   IPI; IPI00123131; -.
DR   RefSeq; NP_062391.3; NM_019518.3.
DR   UniGene; Mm.276573; -.
DR   ProteinModelPortal; Q9JJA9; -.
DR   SMR; Q9JJA9; 97-191.
DR   STRING; Q9JJA9; -.
DR   PhosphoSite; Q9JJA9; -.
DR   PRIDE; Q9JJA9; -.
DR   Ensembl; ENSMUST00000000543; ENSMUSP00000000543; ENSMUSG00000000531.
DR   GeneID; 56149; -.
DR   KEGG; mmu:56149; -.
DR   UCSC; uc007xsu.1; mouse.
DR   CTD; 56149; -.
DR   MGI; MGI:1860303; Grasp.
DR   eggNOG; roNOG09044; -.
DR   GeneTree; ENSGT00530000063734; -.
DR   HOGENOM; HBG716198; -.
DR   HOVERGEN; HBG053061; -.
DR   InParanoid; Q9JJA9; -.
DR   OMA; HTCFFGG; -.
DR   OrthoDB; EOG47D9GP; -.
DR   PhylomeDB; Q9JJA9; -.
DR   NextBio; 311928; -.
DR   ArrayExpress; Q9JJA9; -.
DR   Bgee; Q9JJA9; -.
DR   Genevestigator; Q9JJA9; -.
DR   GermOnline; ENSMUSG00000000531; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0007165; P:signal transduction; IPI:MGI.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; Membrane; Phosphoprotein.
FT   CHAIN         1    392       General receptor for phosphoinositides 1-
FT                                associated scaffold protein.
FT                                /FTId=PRO_0000087585.
FT   DOMAIN      100    189       PDZ.
FT   REGION      180    257       Interaction with PSCD3.
FT   COMPBIAS    294    323       Pro-rich.
FT   MOD_RES      93     93       Phosphoserine.
FT   MOD_RES     236    236       Phosphotyrosine (By similarity).
FT   CONFLICT    299    299       P -> L (in Ref. 2; BAA95086).
SQ   SEQUENCE   392 AA;  42337 MW;  52144F07D36B57FE CRC64;
     MTLRRLRKLQ QKEEATAAPD PAGRAPDSEA ARAAPLPSGP PAAAAPPGAP GEELYAALED
     YHPAELYRAL AVSGGTLPRR KGSGFRWKNF TQSPEQQRKV LTLEKGDNQT FGFEIQTYGL
     HHREEQRVEM VTFVCRVHES SPAQLAGLTP GDTIASVNGL NVEGIRHREI VDIIKASGNV
     LRLETLYGTS IRKAELEARL QYLKQTLYEK WGEYRSLMVQ EQRLVHGLVV KDPSIYDTLE
     SVRSCLYGAG LLPGSLPFGP LLAAPGSARG GARRAKGDTD DAVYHTCFFG GAEPQALPPP
     PPPARALGPS SAETPASVLF PAPRSTLSRS ASVRCAGPGG GGGAPGALWT EAREQALCGA
     GLRKTKYRSF RRRLLKFIPG LNRSLEEEES QL
//
ID   RIPL1_MOUSE             Reviewed;         406 AA.
AC   Q9JJC6; Q80WV8;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=RILP-like protein 1;
DE   AltName: Full=Rab-interacting lysosomal-like protein 1;
GN   Name=Rilpl1; ORFNames=MNCb-2440;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S.,
RA   Hashimoto K.;
RT   "Isolation of full-length cDNA clones from mouse brain cDNA library
RT   made by oligo-capping method.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: Neuroprotective protein, which acts by sequestring GAPDH
CC       in the cytosol and prevent the apoptotic function of GAPDH in the
CC       nucleus. Competes with SIAH1 for binding GAPDH. Does not regulate
CC       lysosomal morphology and distribution (By similarity).
CC   -!- SUBUNIT: Interacts (when S-nitrosylated) with GAPDH (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity).
CC   -!- PTM: S-nitrosylation is required for the interaction with GAPDH
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the RILPL family.
CC   -!- SIMILARITY: Contains 1 RILP-like domain.
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DR   EMBL; AB041584; BAA95067.1; -; mRNA.
DR   EMBL; BC051945; AAH51945.1; -; mRNA.
DR   EMBL; BC051946; AAH51946.2; -; mRNA.
DR   EMBL; BC058384; AAH58384.1; -; mRNA.
DR   IPI; IPI00121674; -.
DR   RefSeq; NP_067405.1; NM_021430.2.
DR   UniGene; Mm.480598; -.
DR   ProteinModelPortal; Q9JJC6; -.
DR   SMR; Q9JJC6; 298-337.
DR   PhosphoSite; Q9JJC6; -.
DR   PRIDE; Q9JJC6; -.
DR   Ensembl; ENSMUST00000062153; ENSMUSP00000050014; ENSMUSG00000029392.
DR   GeneID; 75695; -.
DR   KEGG; mmu:75695; -.
DR   UCSC; uc008zpz.1; mouse.
DR   CTD; 75695; -.
DR   MGI; MGI:1922945; Rilpl1.
DR   eggNOG; roNOG16865; -.
DR   GeneTree; ENSGT00530000063269; -.
DR   HOGENOM; HBG713484; -.
DR   HOVERGEN; HBG060448; -.
DR   InParanoid; Q9JJC6; -.
DR   OMA; QWANSHR; -.
DR   OrthoDB; EOG4V9TRB; -.
DR   PhylomeDB; Q9JJC6; -.
DR   NextBio; 343728; -.
DR   ArrayExpress; Q9JJC6; -.
DR   Bgee; Q9JJC6; -.
DR   CleanEx; MM_RILPL1; -.
DR   Genevestigator; Q9JJC6; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0043526; P:neuroprotection; IMP:UniProtKB.
DR   InterPro; IPR019143; JNK/Rab-associated_protein-1_N.
DR   InterPro; IPR021563; RILP.
DR   Pfam; PF09744; Jnk-SapK_ap_N; 1.
DR   Pfam; PF11461; RILP; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Phosphoprotein; S-nitrosylation.
FT   CHAIN         1    406       RILP-like protein 1.
FT                                /FTId=PRO_0000299311.
FT   DOMAIN      290    324       RILP-like.
FT   COILED       76    258       Potential.
FT   MOD_RES      47     47       S-nitrosocysteine (By similarity).
FT   MOD_RES     328    328       Phosphoserine.
SQ   SEQUENCE   406 AA;  47323 MW;  F866CA2025C71E87 CRC64;
     MEEPLGSPPA ALSALEKNVA ELTVMDVYDI ASLVGHEFER VIDQHGCESI ARLMPKVVRV
     LEILEVLVSR HHVAPELDEL RLELDRLRVE RMDRIEKERK HQKELELVED VWRGEAQDLL
     SQIAQLQEEN KQLMTNLNHK DVGFSEEEFQ KQEGMSERER QVMKRLKEVV DKQRDELRAK
     DRELGLKNED VEALQQQQTR LMKINHDLRH RVTVVEAQGK ALIEQKVELE ADLQTKEQEM
     GSLRAELGKL RERLQGEHSQ NGEEEEAEIQ PQPDGEESIS DAEKAALDLK DPNRPRFTLQ
     ELRDVLHERN ELKSKVFLLQ EELAYYKSEE IEEENRIPQP PPITHPRTSP QPESGIKRLF
     SFFSRDKKRL ANTQRPTHIH ESFGQWAITQ RDDGYTEQGQ EALQHL
//
ID   CNBP1_MOUSE             Reviewed;          81 AA.
AC   Q9JJN6;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Beta-catenin-interacting protein 1;
DE   AltName: Full=Inhibitor of beta-catenin and Tcf-4;
GN   Name=Ctnnbip1; Synonyms=Catnbip1, Icat;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND MUTAGENESIS OF
RP   37-GLU--GLU-39.
RC   TISSUE=Embryo;
RX   MEDLINE=20357107; PubMed=10898789;
RA   Tago K., Nakamura T., Nishita M., Hyodo J., Nagai S., Murata Y.,
RA   Adachi S., Ohwada S., Morishita Y., Shibuya H., Akiyama T.;
RT   "Inhibition of Wnt signaling by ICAT, a novel beta-catenin-interacting
RT   protein.";
RL   Genes Dev. 14:1741-1749(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, Head, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Prevents the interaction between CTNNB1 and TCF family
CC       members, and acts as negative regulator of the Wnt signaling
CC       pathway.
CC   -!- SUBUNIT: Binds CTNNB1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart, brain, liver and
CC       skeletal muscle. Detected at low levels in kidney, testis and
CC       lung.
CC   -!- SIMILARITY: Belongs to the CTNNBIP1 family.
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DR   EMBL; AB021261; BAB03457.1; -; mRNA.
DR   EMBL; AK003595; BAB22883.1; -; mRNA.
DR   EMBL; AK009066; BAB26052.1; -; mRNA.
DR   EMBL; AK036181; BAC29336.1; -; mRNA.
DR   EMBL; AK048258; BAC33287.1; -; mRNA.
DR   EMBL; BC038253; AAH38253.1; -; mRNA.
DR   IPI; IPI00122060; -.
DR   RefSeq; NP_001135402.1; NM_001141930.1.
DR   RefSeq; NP_075954.1; NM_023465.4.
DR   UniGene; Mm.299735; -.
DR   UniGene; Mm.474667; -.
DR   ProteinModelPortal; Q9JJN6; -.
DR   SMR; Q9JJN6; 8-53.
DR   MINT; MINT-139054; -.
DR   PRIDE; Q9JJN6; -.
DR   Ensembl; ENSMUST00000030839; ENSMUSP00000030839; ENSMUSG00000028988.
DR   Ensembl; ENSMUST00000105692; ENSMUSP00000101317; ENSMUSG00000028988.
DR   Ensembl; ENSMUST00000116260; ENSMUSP00000111964; ENSMUSG00000028988.
DR   GeneID; 67087; -.
DR   KEGG; mmu:67087; -.
DR   UCSC; uc008vwm.1; mouse.
DR   CTD; 67087; -.
DR   MGI; MGI:1915756; Ctnnbip1.
DR   eggNOG; maNOG21074; -.
DR   GeneTree; ENSGT00510000048990; -.
DR   HOGENOM; HBG268864; -.
DR   HOVERGEN; HBG051037; -.
DR   InParanoid; Q9JJN6; -.
DR   OMA; MNREGAS; -.
DR   OrthoDB; EOG4GB77S; -.
DR   NextBio; 323538; -.
DR   ArrayExpress; Q9JJN6; -.
DR   Bgee; Q9JJN6; -.
DR   CleanEx; MM_CTNNBIP1; -.
DR   Genevestigator; Q9JJN6; -.
DR   GermOnline; ENSMUSG00000028988; Mus musculus.
DR   GO; GO:0005634; C:nucleus; TAS:MGI.
DR   GO; GO:0008013; F:beta-catenin binding; IPI:MGI.
DR   GO; GO:0009952; P:anterior/posterior pattern formation; IMP:MGI.
DR   GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI.
DR   GO; GO:0010553; P:negative regulation of gene-specific transcription from RNA polymerase II promoter; IDA:BHF-UCL.
DR   GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IMP:BHF-UCL.
DR   GO; GO:0043433; P:negative regulation of transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0060633; P:negative regulation of transcription initiation from RNA polymerase II promoter; IDA:BHF-UCL.
DR   GO; GO:0030178; P:negative regulation of Wnt receptor signaling pathway; IDA:MGI.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IPI:MGI.
DR   InterPro; IPR009428; ICAT.
DR   Gene3D; G3DSA:1.10.10.490; ICAT; 1.
DR   Pfam; PF06384; ICAT; 1.
DR   SUPFAM; SSF81730; ICAT; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Wnt signaling pathway.
FT   CHAIN         1     81       Beta-catenin-interacting protein 1.
FT                                /FTId=PRO_0000152883.
FT   MUTAGEN      37     39       EEE->AAA: Abolishes CTNNB1 binding.
SQ   SEQUENCE   81 AA;  9174 MW;  2C58D060B50CE942 CRC64;
     MNREGAPGKS PEEMYIQQKV RVLLMLRKMG SNLTASEEEF LRTYAGVVSS QLSQLPQHSI
     DQGAEDVVMA FSRSETEDRR Q
//
ID   TMM9B_MOUSE             Reviewed;         199 AA.
AC   Q9JJR8;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Transmembrane protein 9B;
DE   Flags: Precursor;
GN   Name=Tmem9b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=21418998; PubMed=11528127;
RA   Amid C., Bahr A., Mujica A., Sampson N., Bikar S.E., Winterpacht A.,
RA   Zabel B., Hankeln T., Schmidt E.R.;
RT   "Comparative genomic sequencing reveals a strikingly similar
RT   architecture of a conserved syntenic region on human chromosome
RT   11p15.3 (including gene ST5) and mouse chromosome 7.";
RL   Cytogenet. Cell Genet. 93:284-290(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Ovary, Pancreas, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the TMEM9 family.
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DR   EMBL; AJ400878; CAB92295.1; -; Genomic_DNA.
DR   EMBL; AK009147; BAB26105.1; -; mRNA.
DR   EMBL; AK007430; BAB25033.1; -; mRNA.
DR   EMBL; AK077253; BAC36710.1; -; mRNA.
DR   EMBL; BC002208; AAH02208.1; -; mRNA.
DR   IPI; IPI00122175; -.
DR   RefSeq; NP_064434.1; NM_020050.1.
DR   UniGene; Mm.240668; -.
DR   ProteinModelPortal; Q9JJR8; -.
DR   PhosphoSite; Q9JJR8; -.
DR   PRIDE; Q9JJR8; -.
DR   Ensembl; ENSMUST00000033333; ENSMUSP00000033333; ENSMUSG00000031021.
DR   GeneID; 56786; -.
DR   KEGG; mmu:56786; -.
DR   UCSC; uc009jec.1; mouse.
DR   CTD; 56786; -.
DR   MGI; MGI:1915254; Tmem9b.
DR   GeneTree; ENSGT00390000000819; -.
DR   HOGENOM; HBG506119; -.
DR   HOVERGEN; HBG050972; -.
DR   InParanoid; Q9JJR8; -.
DR   OMA; DQQPFAN; -.
DR   OrthoDB; EOG45HRZP; -.
DR   PhylomeDB; Q9JJR8; -.
DR   NextBio; 313316; -.
DR   ArrayExpress; Q9JJR8; -.
DR   Bgee; Q9JJR8; -.
DR   CleanEx; MM_TMEM9B; -.
DR   Genevestigator; Q9JJR8; -.
DR   GermOnline; ENSMUSG00000031021; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR008853; TMEM9.
DR   PANTHER; PTHR13064; TMEM9; 1.
DR   Pfam; PF05434; Tmemb_9; 1.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     34       Potential.
FT   CHAIN        35    199       Transmembrane protein 9B.
FT                                /FTId=PRO_0000045787.
FT   TRANSMEM    106    126       Helical; (Potential).
FT   MOD_RES     165    165       Phosphoserine.
SQ   SEQUENCE   199 AA;  22607 MW;  476B6FD1BCECA4E5 CRC64;
     MASLWCGNLL RLGSGLSMSC LALSVLLLAQ LTGAAKNFED VRCKCICPPY KENPGHIYNK
     NISQKDCDCL HVVEPMPVRG PDVEAYCLRC ECKYEERSSV TIKVTIIIYL SILGLLLLYM
     VYLTLVEPIL KRRLFGHSQL LQSDDDVGDH QPFANAHDVL ARSRSRANVL NKVEYAQQRW
     KLQVQEQRKS VFDRHVVLS
//
ID   Q9JJU6_MOUSE            Unreviewed;       373 AA.
AC   Q9JJU6;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   08-FEB-2011, entry version 57.
DE   SubName: Full=B-Raf protein;
DE   Flags: Fragment;
GN   Name=Braf; Synonyms=B-raf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Barnier J.V., Papin C., Eychene A., Lecoq O.;
RT   "The mouse B-raf gene encodes multiple protein isoforms with tissue-
RT   specific expression.";
RL   J. Biochem. 270:23381-23389(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Barnier J.V.;
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AJ276307; CAB81555.1; -; mRNA.
DR   IPI; IPI00668709; -.
DR   UniGene; Mm.245513; -.
DR   UniGene; Mm.480758; -.
DR   HSSP; P04049; 1FAR.
DR   ProteinModelPortal; Q9JJU6; -.
DR   IntAct; Q9JJU6; 1.
DR   STRING; Q9JJU6; -.
DR   Ensembl; ENSMUST00000101497; ENSMUSP00000099036; ENSMUSG00000002413.
DR   UCSC; uc009bmg.1; mouse.
DR   MGI; MGI:88190; Braf.
DR   GeneTree; ENSGT00600000084194; -.
DR   HOVERGEN; HBG001886; -.
DR   ArrayExpress; Q9JJU6; -.
DR   Bgee; Q9JJU6; -.
DR   Genevestigator; Q9JJU6; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005057; F:receptor signaling protein activity; IEA:InterPro.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR003116; Raf-like_ras-bd.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF02196; RBD; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00455; RBD; 1.
DR   PROSITE; PS50898; RBD; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Zinc.
FT   NON_TER       1      1
FT   NON_TER     373    373
SQ   SEQUENCE   373 AA;  41107 MW;  A69DB67E8A8333F8 CRC64;
     KFGGEHNPPS IYLEAYEEYT SKLDALQQRE QQLLESLGNG AYFSVSSSAS MDTVTSSSSS
     SLSVLPSSLS VFQTPTDASR NNPKSPQKPI VRVFLPNKQR TVVPARCGVT VRDSLKKALM
     MRGLIPECCA VYRIQDGEKK PIGWDTDISW LTGEELHVEV LENVPLTTHN FVRKTFFTLA
     FCDFCRKLLF QGFRCQTCGY KFHQRCSTEV PLMCVNYDQL DLLFVSKFFE HHPVPQEEAS
     FPETALPSGS SSAPPSDSTG PQILTSPSPS KSIPIPQPFR PADEDHRNQF GQRDRSSSAP
     NVHINTIEPV NIDDLIRDQG FRGDGGSTTG LSATPPASLP GSLTNVKALQ KSPGPQRERK
     SSSSSSSEDR SRM
//
ID   CCG4_MOUSE              Reviewed;         327 AA.
AC   Q9JJV4;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Voltage-dependent calcium channel gamma-4 subunit;
DE   AltName: Full=Neuronal voltage-gated calcium channel gamma-4 subunit;
GN   Name=Cacng4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=20200313; PubMed=10734232; DOI=10.1016/S0014-5793(00)01306-5;
RA   Klugbauer N., Dai S., Specht V., Lacinova L., Marais E., Bohn G.,
RA   Hofmann F.;
RT   "A family of gamma-like calcium channel subunits.";
RL   FEBS Lett. 470:189-197(2000).
RN   [2]
RP   SUBCELLULAR LOCATION, AND MEMBRANE TOPOLOGY.
RX   PubMed=11389205; DOI=10.1111/j.1469-7793.2001.0467a.x;
RA   Green P.J., Warre R., Hayes P.D., McNaughton N.C., Medhurst A.D.,
RA   Pangalos M., Duckworth D.M., Randall A.D.;
RT   "Kinetic modification of the alpha(1I) subunit-mediated T-type Ca(2+)
RT   channel by a human neuronal Ca(2+) channel gamma subunit.";
RL   J. Physiol. (Lond.) 533:467-478(2001).
CC   -!- FUNCTION: Thought to stabilize the calcium channel in an
CC       inactivated (closed) state (By similarity).
CC   -!- SUBUNIT: The L-type calcium channel is composed of five subunits:
CC       alpha-1, alpha-2/delta, beta and gamma.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG
CC       subfamily.
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DR   EMBL; AJ272045; CAB86386.1; -; mRNA.
DR   IPI; IPI00122299; -.
DR   RefSeq; NP_062304.1; NM_019431.2.
DR   UniGene; Mm.103724; -.
DR   ProteinModelPortal; Q9JJV4; -.
DR   STRING; Q9JJV4; -.
DR   PRIDE; Q9JJV4; -.
DR   Ensembl; ENSMUST00000021066; ENSMUSP00000021066; ENSMUSG00000020723.
DR   GeneID; 54377; -.
DR   KEGG; mmu:54377; -.
DR   UCSC; uc007maz.1; mouse.
DR   CTD; 54377; -.
DR   MGI; MGI:1859167; Cacng4.
DR   GeneTree; ENSGT00550000074547; -.
DR   HOGENOM; HBG564649; -.
DR   HOVERGEN; HBG003682; -.
DR   InParanoid; Q9JJV4; -.
DR   OMA; QEASFLQ; -.
DR   OrthoDB; EOG4GB76R; -.
DR   PhylomeDB; Q9JJV4; -.
DR   NextBio; 311192; -.
DR   ArrayExpress; Q9JJV4; -.
DR   Bgee; Q9JJV4; -.
DR   Genevestigator; Q9JJV4; -.
DR   GermOnline; ENSMUSG00000020723; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005245; F:voltage-gated calcium channel activity; IEA:InterPro.
DR   GO; GO:0019226; P:transmission of nerve impulse; IGI:MGI.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   InterPro; IPR005423; VDCC_g4su.
DR   InterPro; IPR008368; VDCC_gsu.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01792; VDCCGAMMA.
DR   PRINTS; PR01603; VDCCGAMMA4.
PE   1: Evidence at protein level;
KW   Calcium; Calcium channel; Calcium transport; Cell membrane;
KW   Glycoprotein; Ion transport; Ionic channel; Membrane; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    327       Voltage-dependent calcium channel gamma-4
FT                                subunit.
FT                                /FTId=PRO_0000164679.
FT   TOPO_DOM      1      9       Cytoplasmic (Potential).
FT   TRANSMEM     10     30       Helical; (Potential).
FT   TOPO_DOM     31    107       Extracellular (Potential).
FT   TRANSMEM    108    128       Helical; (Potential).
FT   TOPO_DOM    129    136       Cytoplasmic (Potential).
FT   TRANSMEM    137    157       Helical; (Potential).
FT   TOPO_DOM    158    186       Extracellular (Potential).
FT   TRANSMEM    187    207       Helical; (Potential).
FT   TOPO_DOM    208    327       Cytoplasmic (Potential).
FT   CARBOHYD     42     42       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     45     45       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   327 AA;  36535 MW;  6BFB38B546FBCA86 CRC64;
     MVRCDRGLQM LLTTAGAFAA FSLMAIAIGT DYWLYSSAHI CNGTNLTMDD GPPPRRARGD
     LTHSGLWRVC CIEGIYRGHC FRINHFPEDN DYDHDSSEYL LRIVRASSVF PILSTILLLL
     GGLCIGAGRI YSRKNNIVLS AGILFVAAGL SNIIGIIVYI SSNTGDPSDK RDEDKKNHYN
     YGWSFYFGAL SFIVAETVGV LAVNIYIEKN KELRFKTKRE FLKASSSSPY ARMPSYRYRR
     RRSRSSSRST EASPSRDASP VGLKITGAIP MGELSMYTLS REPLKVTTAA SYSPDQDAGF
     LQMHDFFQQD LKEGFHVSML NRRTTPV
//
ID   CCG3_MOUSE              Reviewed;         315 AA.
AC   Q9JJV5;
DT   10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Voltage-dependent calcium channel gamma-3 subunit;
DE   AltName: Full=Neuronal voltage-gated calcium channel gamma-3 subunit;
GN   Name=Cacng3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=20200313; PubMed=10734232; DOI=10.1016/S0014-5793(00)01306-5;
RA   Klugbauer N., Dai S., Specht V., Lacinova L., Marais E., Bohn G.,
RA   Hofmann F.;
RT   "A family of gamma-like calcium channel subunits.";
RL   FEBS Lett. 470:189-197(2000).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Thought to stabilize the calcium channel in an
CC       inactivated (closed) state.
CC   -!- SUBUNIT: The L-type calcium channel is composed of five subunits:
CC       alpha-1, alpha-2/delta, beta and gamma.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. CACNG
CC       subfamily.
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DR   EMBL; AJ272044; CAB86385.1; -; mRNA.
DR   IPI; IPI00122300; -.
DR   UniGene; Mm.444212; -.
DR   ProteinModelPortal; Q9JJV5; -.
DR   STRING; Q9JJV5; -.
DR   PhosphoSite; Q9JJV5; -.
DR   PRIDE; Q9JJV5; -.
DR   Ensembl; ENSMUST00000084615; ENSMUSP00000081664; ENSMUSG00000066189.
DR   UCSC; uc009jov.1; mouse.
DR   MGI; MGI:1859165; Cacng3.
DR   eggNOG; roNOG13115; -.
DR   GeneTree; ENSGT00550000074547; -.
DR   HOGENOM; HBG564649; -.
DR   HOVERGEN; HBG003682; -.
DR   InParanoid; Q9JJV5; -.
DR   OrthoDB; EOG4P5K9M; -.
DR   NextBio; 311188; -.
DR   ArrayExpress; Q9JJV5; -.
DR   Bgee; Q9JJV5; -.
DR   Genevestigator; Q9JJV5; -.
DR   GermOnline; ENSMUSG00000066189; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005262; F:calcium channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   InterPro; IPR008368; VDCC_gsu.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01792; VDCCGAMMA.
PE   1: Evidence at protein level;
KW   Calcium; Calcium channel; Calcium transport; Ion transport;
KW   Ionic channel; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    315       Voltage-dependent calcium channel gamma-3
FT                                subunit.
FT                                /FTId=PRO_0000164676.
FT   TRANSMEM      8     28       Helical; (Potential).
FT   TRANSMEM    104    124       Helical; (Potential).
FT   TRANSMEM    135    155       Helical; (Potential).
FT   TRANSMEM    181    201       Helical; (Potential).
FT   MOD_RES     248    248       Phosphoserine.
SQ   SEQUENCE   315 AA;  35576 MW;  FB4EAC47C494B3AC CRC64;
     MRMCDRGIQM LITTVGAFAA FSLMTIAVGT DYWLYSRGVC RTKSTSDNET SRKNEEVMTH
     FGLWRTCCLE GAFRGVCKKI DHFPEDADYE QDTAEYLLRA VRASSVFPIL SVTLLFFGGL
     CVAASEFHRS RHSVILSAGI FFVSAGLSNI IGIIVYISAN AGDPGQRDSK KSYSYGWSFY
     FGAFSFIIAE IVGVVAVHIY IEKHQQLRAR SHSELLKKST FARLPPYRYR FRRRSSSRST
     EPRSRDLSPI SKGFHTIPST DISMFTLSRD PSKLTMGTLL NSDRDHAFLQ FHNSTPKEFK
     ESLHNNPANR RTTPV
//
ID   NSMA2_MOUSE             Reviewed;         655 AA.
AC   Q9JJY3; Q3UTQ5;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Sphingomyelin phosphodiesterase 3;
DE            EC=3.1.4.12;
DE   AltName: Full=Neutral sphingomyelinase 2;
DE            Short=nSMase-2;
DE            Short=nSMase2;
DE   AltName: Full=Neutral sphingomyelinase II;
GN   Name=Smpd3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=20283922; PubMed=10823942; DOI=10.1073/pnas.97.11.5895;
RA   Hofmann K., Tomiuk S., Wolff G., Stoffel W.;
RT   "Cloning and characterization of the mammalian brain-specific, Mg2+-
RT   dependent neutral sphingomyelinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:5895-5900(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   CATALYTIC ACTIVITY, COFACTOR, AND ENZYME REGULATION.
RX   PubMed=12566438; DOI=10.1074/jbc.M212262200;
RA   Marchesini N., Luberto C., Hannun Y.A.;
RT   "Biochemical properties of mammalian neutral sphingomyelinase 2 and
RT   its role in sphingolipid metabolism.";
RL   J. Biol. Chem. 278:13775-13783(2003).
RN   [5]
RP   FUNCTION.
RX   PubMed=15051724; DOI=10.1074/jbc.M313662200;
RA   Marchesini N., Osta W., Bielawski J., Luberto C., Obeid L.M.,
RA   Hannun Y.A.;
RT   "Role for mammalian neutral sphingomyelinase 2 in confluence-induced
RT   growth arrest of MCF7 cells.";
RL   J. Biol. Chem. 279:25101-25111(2004).
RN   [6]
RP   FUNCTION.
RX   PubMed=15929065; DOI=10.1002/jnr.20549;
RA   Goswami R., Ahmed M., Kilkus J., Han T., Dawson S.A., Dawson G.;
RT   "Differential regulation of ceramide in lipid-rich microdomains
RT   (rafts): antagonistic role of palmitoyl:protein thioesterase and
RT   neutral sphingomyelinase 2.";
RL   J. Neurosci. Res. 81:208-217(2005).
RN   [7]
RP   FUNCTION.
RX   PubMed=16025116; DOI=10.1038/ng1603;
RA   Aubin I., Adams C.P., Opsahl S., Septier D., Bishop C.E., Auge N.,
RA   Salvayre R., Negre-Salvayre A., Goldberg M., Guenet J.-L., Poirier C.;
RT   "A deletion in the gene encoding sphingomyelin phosphodiesterase 3
RT   (Smpd3) results in osteogenesis and dentinogenesis imperfecta in the
RT   mouse.";
RL   Nat. Genet. 37:803-805(2005).
RN   [8]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX   PubMed=15764706; DOI=10.1073/pnas.0406380102;
RA   Stoffel W., Jenke B., Bloeck B., Zumbansen M., Koebke J.;
RT   "Neutral sphingomyelinase 2 (smpd3) in the control of postnatal growth
RT   and development.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:4554-4559(2005).
CC   -!- FUNCTION: Catalyzes the hydrolysis of sphingomyelin to form
CC       ceramide and phosphocholine. Ceramide mediates numerous cellular
CC       functions, such as apoptosis and growth arrest, and is capable of
CC       regulating these 2 cellular events independently. Also hydrolyzes
CC       sphingosylphosphocholine. Regulates the cell cycle by acting as a
CC       growth suppressor in confluent cells. Acts as a regulator of
CC       postnatal development and participates in bone and dentin
CC       mineralization. Overexpression enhances cell death, suggesting
CC       that it may be involved in apoptosis control.
CC   -!- CATALYTIC ACTIVITY: Sphingomyelin + H(2)O = N-acylsphingosine +
CC       choline phosphate.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: Inhibited by nSMase inhibitor GW4869.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Multi-pass
CC       membrane protein. Note=May localize to detergent-resistant
CC       subdomains of Golgi membranes of hypothalamic neurosecretory
CC       neurons.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in brain (at protein
CC       level).
CC   -!- DISRUPTION PHENOTYPE: Defects in smpd3 are the cause of fragilitas
CC       ossium (fro) mutation characterized by severe osteogenesis and
CC       dentinogenesis imperfecta with no detectable collagen defect. Mice
CC       lacking Smpd2 and Smpd3 are completely devoid of neutral SMase
CC       activity but do not developed sphingomyelin storage abnormalities.
CC       Mice lacking Smpd3 develop a form of dwarfism and delayed puberty
CC       as part of a hypothalamus-induced combined pituitary hormone
CC       deficiency (CPHD). Growth retardation is probably due to delayed
CC       ossification of long bones.
CC   -!- SIMILARITY: Belongs to the neutral sphingomyelinase family.
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DR   EMBL; AJ250461; CAB92970.1; -; mRNA.
DR   EMBL; AK019476; BAB31745.1; -; mRNA.
DR   EMBL; AK139226; BAE23925.1; -; mRNA.
DR   EMBL; BC043077; AAH43077.1; -; mRNA.
DR   EMBL; BC046980; AAH46980.1; -; mRNA.
DR   IPI; IPI00122396; -.
DR   RefSeq; NP_067466.1; NM_021491.3.
DR   UniGene; Mm.23298; -.
DR   ProteinModelPortal; Q9JJY3; -.
DR   SMR; Q9JJY3; 353-519.
DR   STRING; Q9JJY3; -.
DR   PRIDE; Q9JJY3; -.
DR   Ensembl; ENSMUST00000067512; ENSMUSP00000069255; ENSMUSG00000031906.
DR   GeneID; 58994; -.
DR   KEGG; mmu:58994; -.
DR   UCSC; uc009nfx.1; mouse.
DR   CTD; 58994; -.
DR   MGI; MGI:1927578; Smpd3.
DR   GeneTree; ENSGT00400000022168; -.
DR   HOGENOM; HBG444551; -.
DR   HOVERGEN; HBG079416; -.
DR   InParanoid; Q9JJY3; -.
DR   OMA; RTASVEY; -.
DR   OrthoDB; EOG4PVNZ9; -.
DR   PhylomeDB; Q9JJY3; -.
DR   NextBio; 314498; -.
DR   ArrayExpress; Q9JJY3; -.
DR   Bgee; Q9JJY3; -.
DR   CleanEx; MM_SMPD3; -.
DR   Genevestigator; Q9JJY3; -.
DR   GermOnline; ENSMUSG00000031906; Mus musculus.
DR   GO; GO:0000137; C:Golgi cis cisterna; IDA:MGI.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004767; F:sphingomyelin phosphodiesterase activity; IDA:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0030072; P:peptide hormone secretion; IMP:MGI.
DR   GO; GO:0006950; P:response to stress; TAS:MGI.
DR   GO; GO:0007165; P:signal transduction; TAS:MGI.
DR   GO; GO:0006684; P:sphingomyelin metabolic process; IDA:MGI.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   SUPFAM; SSF56219; Exo_endo_phos; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Developmental protein; Golgi apparatus; Hydrolase;
KW   Magnesium; Membrane; Metal-binding; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    655       Sphingomyelin phosphodiesterase 3.
FT                                /FTId=PRO_0000075693.
FT   TOPO_DOM      1     10       Lumenal (Potential).
FT   TRANSMEM     11     31       Helical; (Potential).
FT   TOPO_DOM     32     64       Cytoplasmic (Potential).
FT   TRANSMEM     65     85       Helical; (Potential).
FT   TOPO_DOM     86    655       Lumenal (Potential).
FT   ACT_SITE    639    639       Proton acceptor (By similarity).
FT   METAL       362    362       Magnesium (By similarity).
FT   SITE        510    510       Important for substrate recognition (By
FT                                similarity).
SQ   SEQUENCE   655 AA;  71197 MW;  6764769EEAB5A168 CRC64;
     MVLYTTPFPN SCLSALHAVS WALIFPCYWL VDRLLASFIP TTYEKRQRAD DPCCLQLFCT
     VLFTPVYLAL LVAALPFAFL GFIFWSPLQS ARRPYSYSRL EDKNPAGGAA LLSEWKGTGA
     GKSFCFATAN VCLLPDSLAR LNNVFNTQAR AKEIGQRIRN GAARPQIKIY IDSPTNTSIS
     AASFSSLVSP QGGDGSRAVP GSIKRTASVE YKGDGGRHPS DEAANGPASG EQADGSLEDS
     CIVRIGGEEG GRPQEADDPA AGSQARNGAG GTPKGQTPNH NQRDGDSGSL GSPSASRESL
     VKARAGQDSG GSGEPGANSK LLYKTSVVKK AAARRRRHPD EAFDHEVSAF FPANLDFLCL
     QEVFDKRAAA KLKEQLHGYF EYILYDVGVY GCHGCCNFKC LNSGLFFASR YPVMDVAYHC
     YPNGCSFDAL ASKGALFLKV QVGSTPQDQR IVGYIACTHL HAPPEDSAVR CEQLDLLQDW
     LADFRKSTSS TSTANPEELV VFDVICGDLN FDNCSSDDKL EQQHSLFTRY KDPCRLGPGE
     EKPWAIGTLL DTNGLYDEDV CTPDNLQKVL ESEEGRREYL AFPTSKSPGA GQKGRKDLLK
     GNGRRIDYML HAEEGLCPDW KAEVEEFSFI TQLSGLTDHL PVAMRLMVSA GEEEA
//
ID   DDX20_MOUSE             Reviewed;         825 AA.
AC   Q9JJY4; Q9JIK4;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Probable ATP-dependent RNA helicase DDX20;
DE            EC=3.6.4.13;
DE   AltName: Full=Component of gems 3;
DE   AltName: Full=DEAD box protein 20;
DE   AltName: Full=DEAD box protein DP 103;
DE   AltName: Full=Gemin-3;
DE   AltName: Full=Regulator of steroidogenic factor 1;
DE            Short=ROSF-1;
GN   Name=Ddx20; Synonyms=Dp103, Gemin3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH SMN1.
RX   MEDLINE=20231537; PubMed=10767334; DOI=10.1093/hmg/9.7.1093;
RA   Campbell L., Hunter K.M., Mohaghegh P., Tinsley J.M., Brasch M.A.,
RA   Davies K.E.;
RT   "Direct interaction of Smn with dp103, a putative RNA helicase: a role
RT   for Smn in transcription regulation?";
RL   Hum. Mol. Genet. 9:1093-1100(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Testis;
RX   MEDLINE=20581305; PubMed=11145740; DOI=10.1210/me.15.1.69;
RA   Ou Q., Mouillet J.F., Yan X., Dorn C., Crawford P.A., Sadovsky Y.;
RT   "The DEAD box protein DP103 is a regulator of steroidogenic factor-
RT   1.";
RL   Mol. Endocrinol. 15:69-79(2001).
RN   [3]
RP   INTERACTION WITH FOXL2.
RX   PubMed=16153597; DOI=10.1016/j.bbrc.2005.08.184;
RA   Lee K., Pisarska M.D., Ko J.J., Kang Y., Yoon S., Ryou S.M., Cha K.Y.,
RA   Bae J.;
RT   "Transcriptional factor FOXL2 interacts with DP103 and induces
RT   apoptosis.";
RL   Biochem. Biophys. Res. Commun. 336:876-881(2005).
CC   -!- FUNCTION: The SMN complex plays an essential role in spliceosomal
CC       snRNP assembly in the cytoplasm and is required for pre-mRNA
CC       splicing in the nucleus. It may also play a role in the metabolism
CC       of snoRNPs.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Part of the core SMN complex that contains SMN1,
CC       SIP1/GEMIN2, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8
CC       and STRAP/UNRIP. Interacts directly with SMN1 and with several
CC       spliceosomal snRNP core Sm proteins, including SNUPN, SNRPB,
CC       SNRPD2 and SNRPD3. Interacts with PPP4R2 (By similarity).
CC       Interacts with FOXL2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus, gem. Note=Localized in
CC       subnuclear structures next to coiled bodies, called Gemini of
CC       Cajal bodies (Gems).
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
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DR   EMBL; AJ250027; CAB86201.1; -; mRNA.
DR   EMBL; AF220454; AAF76301.1; -; mRNA.
DR   IPI; IPI00122400; -.
DR   UniGene; Mm.272826; -.
DR   ProteinModelPortal; Q9JJY4; -.
DR   SMR; Q9JJY4; 63-441.
DR   IntAct; Q9JJY4; 1.
DR   STRING; Q9JJY4; -.
DR   PhosphoSite; Q9JJY4; -.
DR   PRIDE; Q9JJY4; -.
DR   Ensembl; ENSMUST00000090680; ENSMUSP00000088176; ENSMUSG00000027905.
DR   MGI; MGI:1858415; Ddx20.
DR   GeneTree; ENSGT00580000081513; -.
DR   HOGENOM; HBG446952; -.
DR   HOVERGEN; HBG051330; -.
DR   InParanoid; Q9JJY4; -.
DR   OrthoDB; EOG4SF95N; -.
DR   PhylomeDB; Q9JJY4; -.
DR   ArrayExpress; Q9JJY4; -.
DR   Bgee; Q9JJY4; -.
DR   CleanEx; MM_DDX20; -.
DR   Genevestigator; Q9JJY4; -.
DR   GermOnline; ENSMUSG00000027905; Mus musculus.
DR   GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0017053; C:transcriptional repressor complex; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016564; F:transcription repressor activity; IDA:MGI.
DR   GO; GO:0006917; P:induction of apoptosis; IPI:MGI.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; DNA-binding; Helicase; Hydrolase;
KW   mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Spliceosome.
FT   CHAIN         1    825       Probable ATP-dependent RNA helicase
FT                                DDX20.
FT                                /FTId=PRO_0000055026.
FT   DOMAIN       94    265       Helicase ATP-binding.
FT   DOMAIN      300    449       Helicase C-terminal.
FT   NP_BIND     107    114       ATP (By similarity).
FT   MOTIF        63     91       Q motif.
FT   MOTIF       212    215       DEAD box.
FT   MOD_RES     188    188       Phosphoserine (By similarity).
FT   MOD_RES     501    501       Phosphoserine (By similarity).
FT   MOD_RES     552    552       Phosphothreonine (By similarity).
FT   MOD_RES     650    650       Phosphoserine (By similarity).
FT   MOD_RES     653    653       Phosphoserine (By similarity).
FT   MOD_RES     655    655       Phosphoserine (By similarity).
FT   MOD_RES     657    657       Phosphoserine (By similarity).
FT   MOD_RES     673    673       Phosphoserine (By similarity).
FT   MOD_RES     678    678       Phosphoserine (By similarity).
FT   MOD_RES     679    679       Phosphoserine (By similarity).
FT   MOD_RES     706    706       Phosphothreonine (By similarity).
FT   CONFLICT      5      5       A -> T (in Ref. 2; AAF76301).
FT   CONFLICT      9      9       P -> R (in Ref. 2; AAF76301).
FT   CONFLICT    226    226       H -> Q (in Ref. 2; AAF76301).
FT   CONFLICT    468    468       V -> I (in Ref. 2; AAF76301).
SQ   SEQUENCE   825 AA;  91719 MW;  F6B06E2EA8FA7D2D CRC64;
     MAAAAFEVPA ALTTSESTMA AERAAAPVQA VEPTPASPWT QRTAHDIGGP RTRTGDVVLA
     EPADFESLLL SRPVLEGLRA AGFERPSPVQ LKAIPLGRCG LDLIVQAKSG TGKTCVFSTI
     ALDSLILENY STQILILAPT REIAVQIHSV ITAIGIKMEG LECHVFIGGT PLSQDKTRLK
     KCHIAVGSPG RIKQLIELDY LNPGSIRLFI LDEADKLLEE GSFQEHINWI YSSLPASKQM
     LAVSATYPEV LANALTRYMR DPTFVRLNPS DPSLIGLKQY YQVVNSYPLA HKIFEEKTQH
     LQELFSKVPF NQALVFSNLH SRAQHLADIL SSKGFPTECI SGNMNQNQRL DAMAKLKQFH
     CRVLISTDLT SRGIDAEKVN LVVNLDVPLD WETYMHRIGR AGRFGTLGLT VTYCCRGEEE
     NMMMKIAQKC NINLLPLPDP IPPGLMEECL NWDVEVKAAM HTYSSPTVAT QSPKKQVQKL
     ERAFQSQRTP GNQTPSPRNT SASALSARPK HSKPKLPVKS HSECGVLEKA APPQESGCPA
     QLEEQVKNSV QTSVEDSSSN SQHQAKDSSP GSLPKIPCLS SFKVHQPSTL TFAELVDDYE
     HYIKEGLEKP VEIIRHYTGP EAQTGNPQNG FVRNRVSEDR AQMLVSSSQS GDSESDSDSC
     SSRTSSQSKG NKSYLEGSSD TQLKDTECTP VGGPLSLEQV QNGNDTPTQV EYQEAPETQV
     KARHKEGANQ RSKQSRRNPA RRSSYRVQSE PQEESWYDCH RETTASFSDT YQDYEEYWRA
     YYRAWQEYYA AASHSYYWNA QRHPSWMAAY HMNTVYLQEM MRGNQ
//
ID   UB2J1_MOUSE             Reviewed;         318 AA.
AC   Q9JJZ4; Q9DC92;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 J1;
DE            EC=6.3.2.19;
DE   AltName: Full=Non-canonical ubiquitin-conjugating enzyme 1;
DE            Short=NCUBE-1;
GN   Name=Ube2j1; Synonyms=Ncube1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20175227; PubMed=10708578; DOI=10.1006/bbrc.2000.2302;
RA   Lester D.H., Farquharson C., Russell G.C., Houston B.;
RT   "Identification of a family of non-canonical ubiquitin-conjugating
RT   enzymes structurally related to yeast UBC6.";
RL   Biochem. Biophys. Res. Commun. 269:474-480(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. Seems to function in the selective degradation of
CC       misfolded membrane proteins from the endoplasmic reticulum (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC       diphosphate + protein N-ubiquityllysine.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       type IV membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ245899; CAB83217.1; -; mRNA.
DR   EMBL; AK003050; BAB22532.1; -; mRNA.
DR   EMBL; AK031669; BAC27502.1; -; mRNA.
DR   EMBL; BC024623; AAH24623.1; -; mRNA.
DR   IPI; IPI00321895; -.
DR   RefSeq; NP_062532.2; NM_019586.3.
DR   UniGene; Mm.259095; -.
DR   ProteinModelPortal; Q9JJZ4; -.
DR   SMR; Q9JJZ4; 9-151.
DR   STRING; Q9JJZ4; -.
DR   PhosphoSite; Q9JJZ4; -.
DR   PRIDE; Q9JJZ4; -.
DR   Ensembl; ENSMUST00000029944; ENSMUSP00000029944; ENSMUSG00000028277.
DR   GeneID; 56228; -.
DR   KEGG; mmu:56228; -.
DR   UCSC; uc008sfp.1; mouse.
DR   CTD; 56228; -.
DR   MGI; MGI:1926245; Ube2j1.
DR   GeneTree; ENSGT00530000063379; -.
DR   HOGENOM; HBG379346; -.
DR   HOVERGEN; HBG058959; -.
DR   InParanoid; Q9JJZ4; -.
DR   OMA; CGSTMKD; -.
DR   PhylomeDB; Q9JJZ4; -.
DR   BRENDA; 6.3.2.19; 244.
DR   NextBio; 312128; -.
DR   ArrayExpress; Q9JJZ4; -.
DR   Bgee; Q9JJZ4; -.
DR   CleanEx; MM_UBE2J1; -.
DR   Genevestigator; Q9JJZ4; -.
DR   GermOnline; ENSMUSG00000028277; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:EC.
DR   GO; GO:0043687; P:post-translational protein modification; IEA:InterPro.
DR   GO; GO:0051246; P:regulation of protein metabolic process; IEA:InterPro.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Gene3D; G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SUPFAM; SSF54495; UBQ-conjugat/RWD-like; 1.
DR   PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; FALSE_NEG.
DR   PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Endoplasmic reticulum; Ligase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Transmembrane;
KW   Transmembrane helix; Ubl conjugation pathway.
FT   CHAIN         1    318       Ubiquitin-conjugating enzyme E2 J1.
FT                                /FTId=PRO_0000082595.
FT   TOPO_DOM      1    282       Cytoplasmic (Potential).
FT   TRANSMEM    283    303       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   TOPO_DOM    304    318       Lumenal (Potential).
FT   ACT_SITE     91     91       Glycyl thioester intermediate (By
FT                                similarity).
FT   MOD_RES     266    266       Phosphoserine.
FT   MOD_RES     268    268       Phosphoserine (By similarity).
FT   CONFLICT    286    286       G -> V (in Ref. 1; CAB83217).
FT   CONFLICT    289    289       M -> V (in Ref. 1; CAB83217).
SQ   SEQUENCE   318 AA;  34990 MW;  61A409ADF397EA36 CRC64;
     METRYNLKSP AVKRLMKEAA ELKDPTDHYH AQPLEDNLFE WHFTVRGPPD SDFDGGVYHG
     RIVLPPEYPM KPPSIILLTA NGRFEVGKKI CLSISGHHPE TWQPSWSIRT ALLAIIGFMP
     TKGEGAIGSL DYTPEERRAL AKKSQDFCCE GCGSAMKDVL LPLKSGSGSS QADQEAKELA
     RQISFKAEVN SSGKTIAESD LNQCFSLNDS QDDLPTTFQG ATASTSYGAQ NPSGAPLPQP
     TQPAPKNTSM SPRQRRAQQQ SQRRPSTSPD VLQGQPPRAH HTEHGGSAML IIILTLALAA
     LIFRRIYLAN EYIFDFEL
//
ID   MYOZ1_MOUSE             Reviewed;         296 AA.
AC   Q9JK37; Q8C9L3; Q9D7N4;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Myozenin-1;
DE   AltName: Full=Calsarcin-2;
DE   AltName: Full=Filamin-, actinin- and telethonin-binding protein;
DE   AltName: Full=Protein FATZ;
GN   Name=Myoz1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Diaphragm;
RX   MEDLINE=20576288; PubMed=10984498; DOI=10.1074/jbc.M007493200;
RA   Faulkner G., Pallavicini A., Comelli A., Salamon M., Bortoletto G.,
RA   Ievolella C., Trevisan S., Kojic' S., Dalla Vecchia F., Laveder P.,
RA   Valle G., Lanfranchi G.;
RT   "FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-
RT   disc of skeletal muscle.";
RL   J. Biol. Chem. 275:41234-41242(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PPP3CA, TISSUE
RP   SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=20570531; PubMed=11114196; DOI=10.1073/pnas.260501097;
RA   Frey N., Richardson J.A., Olson E.N.;
RT   "Calsarcins, a novel family of sarcomeric calcineurin-binding
RT   proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:14632-14637(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Myozenins may serve as intracellular binding proteins
CC       involved in linking Z-disk proteins such as alpha-actinin, gamma-
CC       filamin, TCAP/telethonin, LDB3/ZASP and localizing calcineurin
CC       signaling to the sarcomere. Plays an important role in the
CC       modulation of calcineurin signaling. May play a role in
CC       myofibrillogenesis.
CC   -!- SUBUNIT: Interacts with ACTN2, ACTN3, FLNA, FLNB, FLNC, LDB3,
CC       PPP3CA and TCAP. Interacts via its C-terminal region with MYOT.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cell projection,
CC       pseudopodium (By similarity). Note=Localized to the nucleus and
CC       pseudopodia of undifferentiated cells and detected throughout the
CC       myotubes of differentiated cells. Colocalizes with ACTN2, FLNC and
CC       MYOT at the Z-lines of skeletal muscle (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed primarily in skeletal muscle and
CC       specifically enriched in the gastrocnemius, which is composed
CC       predominantly of fast-twitch muscle fibers. Detected at lower
CC       levels in heart.
CC   -!- DEVELOPMENTAL STAGE: At E9.5, expressed at significant levels in
CC       cardiac muscle with lower levels detected in skeletal muscle of
CC       tongue. At E15.5, cardiac expression is down-regulated and only
CC       weakly detected in atria, whereas skeletal muscle expression is
CC       more robust.
CC   -!- SIMILARITY: Belongs to the myozenin family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ005620; CAB76836.1; -; mRNA.
DR   EMBL; AY013298; AAG38941.1; -; mRNA.
DR   EMBL; AK009077; BAB26059.1; -; mRNA.
DR   EMBL; AK041896; BAC31092.1; -; mRNA.
DR   EMBL; BC024660; AAH24660.1; -; mRNA.
DR   IPI; IPI00459945; -.
DR   RefSeq; NP_067483.1; NM_021508.3.
DR   UniGene; Mm.439911; -.
DR   STRING; Q9JK37; -.
DR   PRIDE; Q9JK37; -.
DR   Ensembl; ENSMUST00000090469; ENSMUSP00000087955; ENSMUSG00000068697.
DR   GeneID; 59011; -.
DR   KEGG; mmu:59011; -.
DR   UCSC; uc007skd.1; mouse.
DR   CTD; 59011; -.
DR   MGI; MGI:1929471; Myoz1.
DR   eggNOG; roNOG07931; -.
DR   GeneTree; ENSGT00530000063184; -.
DR   HOGENOM; HBG716323; -.
DR   HOVERGEN; HBG071289; -.
DR   InParanoid; Q9JK37; -.
DR   OMA; DIGIPLD; -.
DR   OrthoDB; EOG4RV2S7; -.
DR   NextBio; 314556; -.
DR   ArrayExpress; Q9JK37; -.
DR   Bgee; Q9JK37; -.
DR   CleanEx; MM_MYOZ1; -.
DR   Genevestigator; Q9JK37; -.
DR   GermOnline; ENSMUSG00000068697; Mus musculus.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0031143; C:pseudopodium; IEA:UniProtKB-SubCell.
DR   InterPro; IPR008438; Calsarcin-bd.
DR   PANTHER; PTHR15941; Calsarcin_bd; 1.
DR   Pfam; PF05556; Calsarcin; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Nucleus.
FT   CHAIN         1    296       Myozenin-1.
FT                                /FTId=PRO_0000111096.
FT   COMPBIAS     95    172       Gly-rich.
FT   CONFLICT    100    100       T -> A (in Ref. 3; BAB26059).
FT   CONFLICT    131    131       Q -> H (in Ref. 3; BAC31092).
SQ   SEQUENCE   296 AA;  31457 MW;  E9D16F4723B1EE83 CRC64;
     MPLSGTPAPN KRRKSSKLIM ELTGGGRESS GLNLGKKISV PRDVMLEELS LLTNRGSKMF
     KLRQMRVEKF IYENHPDVFS DSSMDHFQKF LPTVGGQLET AGQGFSYGKG SSGGQAGSSG
     SAGQYGSDRH QQGSGFGAGG SGGPGGQAGG GGAPGTVGLG EPGSGDQAGG DGKHVTVFKT
     YISPWDRAMG VDPQQKVELG IDLLAYGAKA ELPKYKSFNR TAMPYGGYEK ASKRMTFQMP
     KFDLGPLLSE PLVLYNQNLS NRPSFNRTPI PWLSSGEHVD YNVDVGIPLD GETEEL
//
ID   KCNQ5_MOUSE             Reviewed;         933 AA.
AC   Q9JK45; Q4QXS5; Q8BSF6;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Potassium voltage-gated channel subfamily KQT member 5;
DE   AltName: Full=KQT-like 5;
DE   AltName: Full=Potassium channel subunit alpha KvLQT5;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv7.5;
GN   Name=Kcnq5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, SUBUNIT, AND
RP   MISCELLANEOUS.
RC   TISSUE=Brain;
RX   PubMed=15963599; DOI=10.1016/j.molbrainres.2005.05.007;
RA   Jensen H.S., Callo K., Jespersen T., Jensen B.S., Olesen S.-P.;
RT   "The KCNQ5 potassium channel from mouse: a broadly expressed M-current
RT   like potassium channel modulated by zinc, pH, and volume changes.";
RL   Brain Res. Mol. Brain Res. 139:52-62(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 56-933.
RC   STRAIN=BALB/c; TISSUE=Brain;
RA   Kniazeva M., Han M.;
RT   "A new gene of the voltage-gated potassium channel KCNQ family, KCNQ5,
RT   is a candidate gene for retinal disorders.";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 362-933.
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Probably important in the regulation of neuronal
CC       excitability. Associates with KCNQ3 to form a potassium channel
CC       which contributes to M-type current, a slowly activating and
CC       deactivating potassium conductance which plays a critical role in
CC       determining the subthreshold electrical excitability of neurons.
CC       May contribute, with other potassium channels, to the molecular
CC       diversity of an heterogeneous population of M-channels, varying in
CC       kinetic and pharmacological properties, which underlie this
CC       physiologically important current (By similarity).
CC   -!- SUBUNIT: Heteromultimer with KCNQ3 (By similarity). Forms homomers
CC       when expressed in Xenopus oocytes.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position (By similarity).
CC   -!- MISCELLANEOUS: The activity of this channel is modulated by zinc,
CC       pH and volume changes.
CC   -!- SIMILARITY: Belongs to the potassium channel family. KQT
CC       (TC 1.A.1.15) subfamily. Kv7.5/KCNQ5 sub-subfamily.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AY679158; AAT76442.1; -; mRNA.
DR   EMBL; AF263836; AAF73447.1; -; mRNA.
DR   EMBL; AK033079; BAC28145.1; -; mRNA.
DR   IPI; IPI00122258; -.
DR   RefSeq; NP_076361.1; NM_023872.3.
DR   UniGene; Mm.336519; -.
DR   UniGene; Mm.403737; -.
DR   ProteinModelPortal; Q9JK45; -.
DR   SMR; Q9JK45; 127-378, 599-628.
DR   STRING; Q9JK45; -.
DR   TCDB; 1.A.1.15.5; voltage-gated ion channel (VIC) superfamily.
DR   PhosphoSite; Q9JK45; -.
DR   PRIDE; Q9JK45; -.
DR   Ensembl; ENSMUST00000029667; ENSMUSP00000029667; ENSMUSG00000028033.
DR   GeneID; 226922; -.
DR   KEGG; mmu:226922; -.
DR   UCSC; uc007alq.1; mouse.
DR   CTD; 226922; -.
DR   MGI; MGI:1924937; Kcnq5.
DR   eggNOG; roNOG04562; -.
DR   GeneTree; ENSGT00550000074513; -.
DR   HOVERGEN; HBG059014; -.
DR   NextBio; 378396; -.
DR   ArrayExpress; Q9JK45; -.
DR   Bgee; Q9JK45; -.
DR   Genevestigator; Q9JK45; -.
DR   GermOnline; ENSMUSG00000028033; Mus musculus.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:MGI.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR015574; K_chnl_KQT5.
DR   InterPro; IPR003937; K_chnl_volt-dep_KCNQ.
DR   InterPro; IPR013821; K_chnl_volt-dep_KCNQ_C.
DR   PANTHER; PTHR11537:SF7; K_channel_KQT5; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF03520; KCNQ_channel; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01459; KCNQCHANNEL.
PE   1: Evidence at protein level;
KW   Ion transport; Ionic channel; Membrane; Potassium; Potassium channel;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN         1    933       Potassium voltage-gated channel subfamily
FT                                KQT member 5.
FT                                /FTId=PRO_0000054041.
FT   TRANSMEM    127    147       Helical; Name=Segment S1; (Potential).
FT   TRANSMEM    158    178       Helical; Name=Segment S2; (Potential).
FT   TRANSMEM    202    222       Helical; Name=Segment S3; (Potential).
FT   TRANSMEM    231    253       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TRANSMEM    268    288       Helical; Name=Segment S5; (Potential).
FT   INTRAMEM    300    320       Pore-forming; Name=Segment H5;
FT                                (Potential).
FT   TRANSMEM    327    347       Helical; Name=Segment S6; (Potential).
FT   MOTIF       312    317       Selectivity filter (By similarity).
FT   CONFLICT    636    636       S -> Y (in Ref. 3; BAC28145).
FT   CONFLICT    923    923       D -> G (in Ref. 3; BAC28145).
SQ   SEQUENCE   933 AA;  102258 MW;  92B8C314D7144288 CRC64;
     MPRHHAGGEE GGAAGLWVRS GAAAAAGAGG GRPGSGMKDV ESGRGRVLLN SAAARGDGLL
     LLGTRAAALG GGGGGLRESR RGKQGARMSL LGKPLSYTSS QSCRRNVKYR RVQNYLYNVL
     ERPRGWAFVY HAFVFLLVFG CLILSVFSTI PEHTKLASSC LLILEFVMIV VFGLEFIIRI
     WSAGCCCRYR GWQGRLRFAR KPFCVIDTIV LIASIAVVSA KTQGNIFATS ALRSLRFLQI
     LRMVRMDRRG GTWKLLGSVV YAHSKELITA WYIGFLVLIF SSFLVYLVEK DANKEFSTYA
     DALWWGTITL TTIGYGDKTP LTWLGRLLSA GFALLGISFF ALPAGILGSG FALKVQEQHR
     QKHFEKRRNP AANLIQCVWR SYAADEKSVS IATWKPHLKA LHTCSPTKKE QGEASSSQKL
     SFKERVRMAS PRGQSIKSRQ ASVGDRRSPS TDITAEGSPT KVQKSWSFND RTRFRPSLRL
     KSSQPKPVID ADTALGIDDV YDEKGCQCDV SVEDLTPPLK TVIRAIRIMK FHVAKRKFKE
     TLRPYDVKDV IEQYSAGHLD MLCRIKSLQT RVDQILGKGQ MTSDKKSREK ITAEHETTDD
     PSMLARVVKV EKQVQSIESK LDCLLDIYQQ VLRKGSASAL TLASFQIPPF ECEQTSDYQS
     PVDSKDLSGS AQNSGCLTRS ASANISRGLQ FILTPNEFSA QTFYALSPTM HSQATQVPMS
     QNDGSSVVAT NNIANQISAA PKPAAPTTLQ IPPPLSAIKH LSRPEPLLSN PTGLQESISD
     VTTCLVASKE SVQFAQSNLT KDRSLRKSFD MGGETLLSVR PMVPKDLGKS LSVQNLIRST
     EELNLQFSGS ESSGSRGSQD FYPKWRESKL FITDEEVGAE ETETDTFDGT PPPAGEAAFS
     SDSLRTGRSR SSQNICKTGD STDALSLPHV KLN
//
ID   UCHL3_MOUSE             Reviewed;         230 AA.
AC   Q9JKB1; Q9EQX7;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase isozyme L3;
DE            Short=UCH-L3;
DE            EC=3.4.19.12;
DE   AltName: Full=Ubiquitin thioesterase L3;
GN   Name=Uchl3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=Swiss Webster / NIH;
RX   MEDLINE=20180078; PubMed=10713173;
RX   DOI=10.1128/MCB.20.7.2498-2504.2000;
RA   Kurihara L.J., Semenova E., Levorse J.M., Tilghman S.M.;
RT   "Expression and functional analysis of Uch-L3 during mouse
RT   development.";
RL   Mol. Cell. Biol. 20:2498-2504(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Liver;
RX   MEDLINE=21240090; PubMed=11341770; DOI=10.1006/bbrc.2001.4841;
RA   Osawa Y., Wang Y.-L., Osaka H., Aoki S., Wada K.;
RT   "Cloning, expression, and mapping of a mouse gene, Uchl4, highly
RT   homologous to human and mouse Uchl3.";
RL   Biochem. Biophys. Res. Commun. 283:627-633(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   DEVELOPMENTAL STAGE.
RX   MEDLINE=99008885; PubMed=9790970; DOI=10.1006/bbrc.1998.9532;
RA   Wada H., Kito K., Caskey L.S., Yeh E.T.H., Kamitani T.;
RT   "Cleavage of the C-terminus of NEDD8 by UCH-L3.";
RL   Biochem. Biophys. Res. Commun. 251:688-692(1998).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15884048; DOI=10.1002/hipo.20082;
RA   Wood M.A., Kaplan M.P., Brensinger C.M., Guo W., Abel T.;
RT   "Ubiquitin C-terminal hydrolase L3 (Uchl3) is involved in working
RT   memory.";
RL   Hippocampus 15:610-621(2005).
RN   [6]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=16816367;
RA   Sano Y., Furuta A., Setsuie R., Kikuchi H., Wang Y.L., Sakurai M.,
RA   Kwon J., Noda M., Wada K.;
RT   "Photoreceptor cell apoptosis in the retinal degeneration of Uchl3-
RT   deficient mice.";
RL   Am. J. Pathol. 169:132-141(2006).
RN   [7]
RP   DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=17460351; DOI=10.1538/expanim.56.71;
RA   Kwon J.;
RT   "The new function of two ubiquitin C-terminal hydrolase isozymes as
RT   reciprocal modulators of germ cell apoptosis.";
RL   Exp. Anim. 56:71-77(2007).
RN   [8]
RP   FUNCTION IN ENAC RECYCLING, AND SUBCELLULAR LOCATION.
RX   PubMed=17967898; DOI=10.1074/jbc.M707989200;
RA   Butterworth M.B., Edinger R.S., Ovaa H., Burg D., Johnson J.P.,
RA   Frizzell R.A.;
RT   "The deubiquitinating enzyme UCH-L3 regulates the apical membrane
RT   recycling of the epithelial sodium channel.";
RL   J. Biol. Chem. 282:37885-37893(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [10]
RP   DISRUPTION PHENOTYPE, FUNCTION IN ADIPOGENESIS AND INSULIN SIGNALING,
RP   AND MUTAGENESIS OF CYS-95.
RX   PubMed=19837878; DOI=10.1210/en.2009-0332;
RA   Suzuki M., Setsuie R., Wada K.;
RT   "Ubiquitin carboxyl-terminal hydrolase l3 promotes insulin signaling
RT   and adipogenesis.";
RL   Endocrinology 150:5230-5239(2009).
RN   [11]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=20380862; DOI=10.1016/j.neuint.2010.03.021;
RA   Setsuie R., Suzuki M., Tsuchiya Y., Wada K.;
RT   "Skeletal muscles of Uchl3 knockout mice show polyubiquitinated
RT   protein accumulation and stress responses.";
RL   Neurochem. Int. 56:911-918(2010).
CC   -!- FUNCTION: Deubiquitinating enzyme (DUB) that controls levels of
CC       cellular ubiquitin through processing of ubiquitin precursors and
CC       ubiquitinated proteins. Thiol protease that recognizes and
CC       hydrolyzes a peptide bond at the C-terminal glycine of either
CC       ubiquitin or NEDD8. Has a 10-fold preference for Arg and Lys at
CC       position P3". Deubiquitinates ENAC in apical compartments, thereby
CC       regulating apical membrane recycling. Indirectly increases the
CC       phosphorylation of IGFIR, AKT and FOXO1 and promotes insulin-
CC       signaling and insulin-induced adipogenesis. Required for stress-
CC       response retinal, skeletal muscle and germ cell maintenance. May
CC       be involved in working memory.
CC   -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- ENZYME REGULATION: Inhibited by monoubiquitin and diubiquitin (By
CC       similarity).
CC   -!- SUBUNIT: Preferentially binds diubiquitin; the interaction does
CC       not hydrolyze diubiquitin but, in vitro, inhibits the hydrolyzing
CC       activity on other substrates (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC       brain, liver, heart, thymus, kidney and testis. Highly expressed
CC       in the cauda epididymidis, in meiotic pachytene spermatocytes and
CC       post-meiotic spematids. In the retina, enriched in the
CC       photoreceptor inner segment.
CC   -!- DEVELOPMENTAL STAGE: Expressed at E8.5 in structures required for
CC       skeletal patterning. Highly expressed at E11, and decreases
CC       markedly from E15.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice have no developmental defects, are
CC       fertile, and show normal T-cell differentiation. They have normal
CC       anxiety, locomotor behavior, motor function and synaptic
CC       transmission, but show defects in spatial learning and working
CC       memory. Exhibit stress-related effects with profound apoptosis-
CC       mediated germ cell loss and also, prominent retinal degeneration
CC       with photoreceptor cell apoptosis and mitochondrial oxidative
CC       stress. Mice show reduced capacity for adipocyte differentiation
CC       and impaired insulin responses.
CC   -!- SIMILARITY: Belongs to the peptidase C12 family.
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DR   EMBL; AF247358; AAF64193.1; -; mRNA.
DR   EMBL; AB033370; BAB20094.1; -; mRNA.
DR   EMBL; BC048481; AAH48481.1; -; mRNA.
DR   IPI; IPI00311369; -.
DR   PIR; JC7688; JC7688.
DR   RefSeq; NP_057932.2; NM_016723.2.
DR   UniGene; Mm.275970; -.
DR   ProteinModelPortal; Q9JKB1; -.
DR   SMR; Q9JKB1; 2-230.
DR   STRING; Q9JKB1; -.
DR   MEROPS; C12.003; -.
DR   PhosphoSite; Q9JKB1; -.
DR   REPRODUCTION-2DPAGE; IPI00311369; -.
DR   REPRODUCTION-2DPAGE; Q9JKB1; -.
DR   PRIDE; Q9JKB1; -.
DR   Ensembl; ENSMUST00000002289; ENSMUSP00000002289; ENSMUSG00000022111.
DR   GeneID; 50933; -.
DR   KEGG; mmu:50933; -.
DR   UCSC; uc007uvw.1; mouse.
DR   CTD; 50933; -.
DR   MGI; MGI:1355274; Uchl3.
DR   GeneTree; ENSGT00510000046640; -.
DR   HOGENOM; HBG436319; -.
DR   HOVERGEN; HBG075483; -.
DR   InParanoid; Q9JKB1; -.
DR   OMA; YETFRTE; -.
DR   OrthoDB; EOG4HX51V; -.
DR   PhylomeDB; Q9JKB1; -.
DR   BRENDA; 3.4.19.12; 244.
DR   NextBio; 307977; -.
DR   ArrayExpress; Q9JKB1; -.
DR   Bgee; Q9JKB1; -.
DR   Genevestigator; Q9JKB1; -.
DR   GermOnline; ENSMUSG00000022111; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:InterPro.
DR   GO; GO:0007628; P:adult walking behavior; IGI:MGI.
DR   GO; GO:0032869; P:cellular response to insulin stimulus; IDA:UniProtKB.
DR   GO; GO:0042755; P:eating behavior; IGI:MGI.
DR   GO; GO:0045600; P:positive regulation of fat cell differentiation; IDA:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR001578; Peptidase_C12.
DR   Gene3D; G3DSA:3.40.532.10; Peptidase_C12; 1.
DR   PANTHER; PTHR10589; Peptidase_C12; 1.
DR   Pfam; PF01088; Peptidase_C12; 1.
DR   PRINTS; PR00707; UBCTHYDRLASE.
DR   PROSITE; PS00140; UCH_1; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Phosphoprotein; Protease; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN         1    230       Ubiquitin carboxyl-terminal hydrolase
FT                                isozyme L3.
FT                                /FTId=PRO_0000211062.
FT   REGION        8     13       Interaction with ubiquitin (By
FT                                similarity).
FT   REGION      152    159       Interaction with ubiquitin (By
FT                                similarity).
FT   REGION      219    224       Interaction with ubiquitin (By
FT                                similarity).
FT   ACT_SITE     95     95       Nucleophile (By similarity).
FT   ACT_SITE    169    169       Proton donor (By similarity).
FT   SITE        184    184       Important for enzyme activity (By
FT                                similarity).
FT   MOD_RES      75     75       Phosphoserine (By similarity).
FT   MOD_RES     130    130       Phosphoserine.
FT   MUTAGEN      95     95       C->S: No increase in phosphorylation of
FT                                AKT1, FOXO1 and INSR. No increased
FT                                expression of SLC2A1, FABP4 nor ADIPOQ.
FT                                Impaired formation of large lipid
FT                                droplets.
FT   CONFLICT    205    207       AIE -> VIK (in Ref. 1; AAF64193).
SQ   SEQUENCE   230 AA;  26152 MW;  F147991F3ED69AC3 CRC64;
     MEGQRWLPLE ANPEVTNQFL KQLGLHPNWQ FVDVYGMEPE LLSMVPRPVC AVLLLFPITE
     KYEVFRTEEE EKIKSQGQDV TSSVYFMKQT ISNACGTIGL IHAIANNKDK MHFESGSTLK
     KFLEESVSMS PEERAKFLEN YDAIRVTHET SAHEGQTEAP SIDEKVDLHF IALVHVDGHL
     YELDGRKPFP INHGKTSDET LLEDAIEVCK KFMERDPDEL RFNAIALSAA
//
ID   CEND_MOUSE              Reviewed;         149 AA.
AC   Q9JKC6; Q9DBA0;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Cell cycle exit and neuronal differentiation protein 1;
DE   AltName: Full=BM88 antigen;
GN   Name=Cend1; Synonyms=Bm88;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=21210945; PubMed=11311134;
RA   Gaitanou M., Buanne P., Pappa C., Georgopoulou N., Mamalaki A.,
RA   Tirone F., Matsas R.;
RT   "Cloning, expression and localization of human BM88 shows that it maps
RT   to chromosome 11p15.5, a region implicated in Beckwith-Wiedemann
RT   syndrome and tumorigenesis.";
RL   Biochem. J. 355:715-724(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 43-61 AND 99-114, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Involved in neuroblastoma cell differentiation (By
CC       similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type IV membrane
CC       protein (Potential).
CC   -!- SIMILARITY: Belongs to the CEND1 family.
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DR   EMBL; AF243130; AAF62099.1; -; mRNA.
DR   EMBL; AK005092; BAB23812.1; -; mRNA.
DR   EMBL; AK079045; BAC37512.1; -; mRNA.
DR   EMBL; BC023032; AAH23032.1; -; mRNA.
DR   IPI; IPI00122826; -.
DR   RefSeq; NP_067291.1; NM_021316.4.
DR   UniGene; Mm.87027; -.
DR   ProteinModelPortal; Q9JKC6; -.
DR   STRING; Q9JKC6; -.
DR   PhosphoSite; Q9JKC6; -.
DR   PRIDE; Q9JKC6; -.
DR   Ensembl; ENSMUST00000084436; ENSMUSP00000081476; ENSMUSG00000060240.
DR   GeneID; 57754; -.
DR   KEGG; mmu:57754; -.
DR   UCSC; uc009kkx.1; mouse.
DR   CTD; 57754; -.
DR   MGI; MGI:1929898; Cend1.
DR   eggNOG; roNOG16993; -.
DR   GeneTree; ENSGT00390000012831; -.
DR   HOGENOM; HBG126821; -.
DR   HOVERGEN; HBG081082; -.
DR   InParanoid; Q9JKC6; -.
DR   OMA; NHSNLKP; -.
DR   OrthoDB; EOG41RPWM; -.
DR   PhylomeDB; Q9JKC6; -.
DR   NextBio; 313916; -.
DR   ArrayExpress; Q9JKC6; -.
DR   Bgee; Q9JKC6; -.
DR   CleanEx; MM_CEND1; -.
DR   Genevestigator; Q9JKC6; -.
DR   GermOnline; ENSMUSG00000060240; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR020162; Cend1.
DR   ProDom; PD079544; Cend1; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    149       Cell cycle exit and neuronal
FT                                differentiation protein 1.
FT                                /FTId=PRO_0000064952.
FT   TOPO_DOM      1    124       Cytoplasmic (Potential).
FT   TRANSMEM    125    145       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   TOPO_DOM    146    149       Extracellular (Potential).
FT   CONFLICT    117    117       W -> R (in Ref. 2; BAB23812).
SQ   SEQUENCE   149 AA;  14987 MW;  88B252ED5DD1EE9B CRC64;
     MESRGKSASS PKPDTKVPQA TAEAKATPAA DGKAPLTKPV KKDTQAEKQE QAAAPGPAAT
     KKTPAKADPV LLNNHSNLKP APTVPAAPSS PDATSEPKGP GDGAEEDESN TGGRGPWPCE
     NLTPLLVAGG VAVATIALIL GVAFLARKK
//
ID   PVRL1_MOUSE             Reviewed;         515 AA.
AC   Q9JKF6; Q9ERL5; Q9JI17;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Poliovirus receptor-related protein 1;
DE   AltName: Full=Herpes virus entry mediator C;
DE            Short=Herpesvirus entry mediator C;
DE            Short=HveC;
DE   AltName: Full=Nectin-1;
DE   AltName: CD_antigen=CD111;
DE   Flags: Precursor;
GN   Name=Pvrl1; Synonyms=Hvec, Prr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20243787; PubMed=10781093; DOI=10.1073/pnas.97.9.4867;
RA   Menotti L., Lopez M., Avitabile E., Stefan A., Cocchi F., Adelaide J.,
RA   Lecocq E., Dubreuil P., Campadelli-Fiume G.;
RT   "The murine homolog of human nectin1 delta serves as a species
RT   nonspecific mediator for entry of human and animal alpha herpesviruses
RT   in a pathway independent of detectable binding to gD.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:4867-4872(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20541977; PubMed=11090177;
RX   DOI=10.1128/JVI.74.24.11773-11781.2000;
RA   Shukla D., Dal Canto M.C., Rowe C.L., Spear P.G.;
RT   "Striking similarity of murine nectin-1alpha to human nectin-1alpha
RT   (HveC) in sequence and activity as a glycoprotein D receptor for
RT   alphaherpesvirus entry.";
RL   J. Virol. 74:11773-11781(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster;
RA   Zhan J., Wimmer E.;
RT   "Mouse nectin-1 (mPRR1), a herpesvirus receptor, is expressed in the
RT   floor plate during embryogenesis, suggesting a role in neural
RT   development.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   INTERACTION WITH PVRL3.
RX   MEDLINE=20209403; PubMed=10744716; DOI=10.1074/jbc.275.14.10291;
RA   Satoh-Horikawa K., Nakanishi H., Takahashi K., Miyahara M.,
RA   Nishimura M., Tachibana K., Mizoguchi A., Takai Y.;
RT   "Nectin-3: a new member of immunoglobulin-like cell adhesion molecules
RT   that shows homophilic and heterophilic cell-cell adhesion
RT   activities.";
RL   J. Biol. Chem. 275:10291-10299(2000).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433 AND SER-434, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-200; ASN-202; ASN-274 AND
RP   ASN-286, AND MASS SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-202; ASN-286 AND ASN-332,
RP   AND MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Probably involved in cell adhesion. Receptor for
CC       alphaherpesvirus (HSV-1, HSV-2 and pseudorabies virus) entry into
CC       cells.
CC   -!- SUBUNIT: Can form trans-heterodimers with PVRL3/nectin-3.
CC       Interacts with HSV glycoprotein D (gD).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the nectin family.
CC   -!- SIMILARITY: Contains 2 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC       domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF239762; AAF60333.1; -; mRNA.
DR   EMBL; AF270977; AAF76195.1; -; mRNA.
DR   EMBL; AF297665; AAG22808.1; -; mRNA.
DR   IPI; IPI00311405; -.
DR   UniGene; Mm.335096; -.
DR   ProteinModelPortal; Q9JKF6; -.
DR   SMR; Q9JKF6; 32-339.
DR   MINT; MINT-254710; -.
DR   STRING; Q9JKF6; -.
DR   PhosphoSite; Q9JKF6; -.
DR   PRIDE; Q9JKF6; -.
DR   Ensembl; ENSMUST00000034510; ENSMUSP00000034510; ENSMUSG00000032012.
DR   MGI; MGI:1926483; Pvrl1.
DR   GeneTree; ENSGT00600000084002; -.
DR   HOGENOM; HBG447380; -.
DR   HOVERGEN; HBG100542; -.
DR   InParanoid; Q9JKF6; -.
DR   OrthoDB; EOG4KWJSZ; -.
DR   ArrayExpress; Q9JKF6; -.
DR   Bgee; Q9JKF6; -.
DR   CleanEx; MM_PVRL1; -.
DR   Genevestigator; Q9JKF6; -.
DR   GermOnline; ENSMUSG00000032012; Mus musculus.
DR   GO; GO:0005913; C:cell-cell adherens junction; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:HGNC.
DR   GO; GO:0004872; F:receptor activity; IDA:MGI.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion; IDA:HGNC.
DR   GO; GO:0007156; P:homophilic cell adhesion; IDA:HGNC.
DR   GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
DR   GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR   InterPro; IPR013162; CD80_C2-set.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3.
DR   Pfam; PF08205; C2-set_2; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 2.
DR   PROSITE; PS50835; IG_LIKE; 2.
PE   1: Evidence at protein level;
KW   Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW   Host-virus interaction; Immunoglobulin domain; Membrane;
KW   Phosphoprotein; Receptor; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     30       Potential.
FT   CHAIN        31    515       Poliovirus receptor-related protein 1.
FT                                /FTId=PRO_0000015134.
FT   TOPO_DOM     31    354       Extracellular (Potential).
FT   TRANSMEM    355    375       Helical; (Potential).
FT   TOPO_DOM    376    515       Cytoplasmic (Potential).
FT   DOMAIN       31    141       Ig-like V-type.
FT   DOMAIN      145    243       Ig-like C2-type 1.
FT   DOMAIN      247    334       Ig-like C2-type 2.
FT   COMPBIAS    436    442       Poly-Glu.
FT   COMPBIAS    443    447       Poly-Gly.
FT   MOD_RES     421    421       Phosphoserine.
FT   MOD_RES     433    433       Phosphoserine.
FT   MOD_RES     434    434       Phosphoserine.
FT   MOD_RES     466    466       Phosphotyrosine (By similarity).
FT   CARBOHYD     36     36       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     72     72       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    139    139       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    200    200       N-linked (GlcNAc...).
FT   CARBOHYD    202    202       N-linked (GlcNAc...).
FT   CARBOHYD    274    274       N-linked (GlcNAc...).
FT   CARBOHYD    286    286       N-linked (GlcNAc...).
FT   CARBOHYD    297    297       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    332    332       N-linked (GlcNAc...).
FT   DISULFID     51    124       By similarity.
FT   DISULFID    172    226       By similarity.
FT   DISULFID    269    316       By similarity.
FT   CONFLICT    138    138       L -> P (in Ref. 1; AAF60333).
FT   CONFLICT    165    165       N -> D (in Ref. 1; AAF60333).
FT   CONFLICT    342    342       P -> PP (in Ref. 2; AAF76195).
FT   CONFLICT    428    428       S -> G (in Ref. 3; AAG22808).
SQ   SEQUENCE   515 AA;  57064 MW;  FFF608EB5FFB7A0F CRC64;
     MARMGLAGAA GRWWGLALGL TAFFLPGTHT QVVQVNDSMY GFIGTDVVLH CSFANPLPSV
     KITQVTWQKA SNGSKQNMAI YNPTMGVSVL PPYEKRVEFL RPSFIDGTIR LSGLELEDEG
     MYICEFATFP TGNRESQLNL TVMAKPTNWI EGTRAVLRAR KGQDNKVLVA TCTSANGKPP
     SAVSWETRLK GEAEYQEIRN PNGTVTVISR YRLVPSREAH RQSLACIVNY HLDRFRESLT
     LNVQYEPEVT IEGFDGNWYL QRTDVKLTCK ADANPPATEY HWTTLNGSLP KGVEAQNRTL
     FFRGPITYSL AGTYICEATN PIGTRSGQVE VNITEFPYTP TPEHGRRAGQ MPTAIIGGVA
     GSVLLVLIVV GGIIVALRRR RHTFKGDYST KKHVYGNGYS KAGIPQHHPP MAQNLQYPDD
     SDDEKKASPL GGSSYEEEEE EEGGGGGERK VGGPHPKYDE DAKRPYFTVD EAEARQDGYG
     DRTLGYQYDP EQLDLAENMV SQNDGSFISK KEWYV
//
ID   STX6_MOUSE              Reviewed;         255 AA.
AC   Q9JKK1; Q9D3A1; Q9D729;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Syntaxin-6;
GN   Name=Stx6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Low D.Y.H., Tang B.L., Hong W.;
RT   "Mouse syntaxin 6.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic stem cell, Testis, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Involved in intracellular vesicle trafficking.
CC   -!- SUBUNIT: Binds EEA1. Interacts with VPS45A and GOPC. Interacts
CC       with MARCH2 and MARCH3 (By similarity). Identified in a complex
CC       containing STX6, STX13, VAMP4 and VTI1A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type
CC       IV membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9JKK1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9JKK1-2; Sequence=VSP_016138;
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the syntaxin family.
CC   -!- SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF237814; AAF40221.1; -; mRNA.
DR   EMBL; AK009690; BAB26441.1; -; mRNA.
DR   EMBL; AK019106; BAB31549.1; -; mRNA.
DR   EMBL; AK031673; BAC27505.1; -; mRNA.
DR   EMBL; AK044905; BAC32135.1; -; mRNA.
DR   EMBL; AK049124; BAC33556.1; -; mRNA.
DR   EMBL; BC029205; AAH29205.1; -; mRNA.
DR   IPI; IPI00109506; -.
DR   IPI; IPI00123104; -.
DR   RefSeq; NP_067408.1; NM_021433.3.
DR   UniGene; Mm.465911; -.
DR   UniGene; Mm.66264; -.
DR   ProteinModelPortal; Q9JKK1; -.
DR   SMR; Q9JKK1; 4-109, 170-232.
DR   STRING; Q9JKK1; -.
DR   PhosphoSite; Q9JKK1; -.
DR   PRIDE; Q9JKK1; -.
DR   Ensembl; ENSMUST00000027743; ENSMUSP00000027743; ENSMUSG00000026470.
DR   Ensembl; ENSMUST00000111779; ENSMUSP00000107409; ENSMUSG00000026470.
DR   GeneID; 58244; -.
DR   KEGG; mmu:58244; -.
DR   UCSC; uc007dbb.1; mouse.
DR   CTD; 58244; -.
DR   MGI; MGI:1926235; Stx6.
DR   GeneTree; ENSGT00390000008991; -.
DR   HOVERGEN; HBG007194; -.
DR   OMA; SGGQNWS; -.
DR   OrthoDB; EOG45HRZ9; -.
DR   NextBio; 314297; -.
DR   ArrayExpress; Q9JKK1; -.
DR   Bgee; Q9JKK1; -.
DR   CleanEx; MM_STX6; -.
DR   Genevestigator; Q9JKK1; -.
DR   GermOnline; ENSMUSG00000026470; Mus musculus.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
DR   GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR   GO; GO:0007032; P:endosome organization; IMP:MGI.
DR   GO; GO:0048193; P:Golgi vesicle transport; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   InterPro; IPR015260; Syntaxin-6_N.
DR   InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR   InterPro; IPR010989; t-SNARE.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   Pfam; PF05739; SNARE; 1.
DR   Pfam; PF09177; Syntaxin-6_N; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF47661; t-snare; 1.
DR   PROSITE; PS00914; SYNTAXIN; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Golgi apparatus; Membrane;
KW   Phosphoprotein; Protein transport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    255       Syntaxin-6.
FT                                /FTId=PRO_0000210209.
FT   TOPO_DOM      1    234       Cytoplasmic (Potential).
FT   TRANSMEM    235    255       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   DOMAIN      163    225       t-SNARE coiled-coil homology.
FT   COILED       41     74       Potential.
FT   MOD_RES     129    129       Phosphoserine (By similarity).
FT   MOD_RES     152    152       Phosphoserine (By similarity).
FT   VAR_SEQ     231    255       DRRQWCAIAILFAVLVVVLILFLVL -> GNDVRQVKIQYL
FT                                LFIWRLLPGERKT (in isoform 2).
FT                                /FTId=VSP_016138.
SQ   SEQUENCE   255 AA;  28997 MW;  2CD91C02D23D28DE CRC64;
     MSMEDPFFVV KGEVQKAVNT AQGLFQRWTE LLQGPSAATR EEIDWTTNEL RNNLRSIEWD
     LEDLDETISI VEANPRKFNL DATELSIRKA FITSTRQIVR DMKDQMSASS VQALAERKNR
     QALLGDSSSQ SWNAGVADRY GRLDRELQLA NSHFIEEQQA QQQLIVEQQD EQLELVSGSI
     GVLKNMSQRI GGELEEQAVM LDDFSHELES TQSRLDNVMK KLAKVSHMTS DRRQWCAIAI
     LFAVLVVVLI LFLVL
//
ID   TMOD2_MOUSE             Reviewed;         351 AA.
AC   Q9JKK7; Q3UH50; Q8BGX9; Q9CUK4; Q9JLH9;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Tropomodulin-2;
DE   AltName: Full=Neuronal tropomodulin;
DE            Short=N-Tmod;
GN   Name=Tmod2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Conley C.A., Fowler V.M.;
RT   "Identifying novel tropomodulin isoforms.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20130118; PubMed=10662549; DOI=10.1006/geno.1999.6061;
RA   Cox P.R., Zoghbi H.Y.;
RT   "Sequencing, expression analysis, and mapping of three unique human
RT   tropomodulin genes and their mouse orthologs.";
RL   Genomics 63:97-107(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon, Hippocampus, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 31-51; 82-93 AND 258-279, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
CC   -!- FUNCTION: Blocks the elongation and depolymerization of the actin
CC       filaments at the pointed end. The Tmod/TM complex contributes to
CC       the formation of the short actin protofilament, which in turn
CC       defines the geometry of the membrane skeleton (By similarity).
CC   -!- SUBUNIT: Binds to the N-terminus of tropomyosin and to actin.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9JKK7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9JKK7-2; Sequence=VSP_024896, VSP_024897;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q9JKK7-3; Sequence=VSP_024895;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Neuronal-tissue specific.
CC   -!- SIMILARITY: Belongs to the tropomodulin family.
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DR   EMBL; AF237629; AAF45297.1; -; mRNA.
DR   EMBL; AF177170; AAF31669.1; -; mRNA.
DR   EMBL; AK015719; BAB29946.3; -; mRNA.
DR   EMBL; AK076562; BAC36394.1; -; mRNA.
DR   EMBL; AK079077; BAC37527.1; -; mRNA.
DR   EMBL; AK147581; BAE28007.1; -; mRNA.
DR   EMBL; AK164178; BAE37665.1; -; mRNA.
DR   EMBL; BC061124; AAH61124.1; -; mRNA.
DR   IPI; IPI00402982; -.
DR   IPI; IPI00461085; -.
DR   IPI; IPI00845765; -.
DR   RefSeq; NP_001033799.1; NM_001038710.1.
DR   RefSeq; NP_057920.2; NM_016711.3.
DR   UniGene; Mm.291880; -.
DR   ProteinModelPortal; Q9JKK7; -.
DR   SMR; Q9JKK7; 181-346.
DR   STRING; Q9JKK7; -.
DR   PRIDE; Q9JKK7; -.
DR   Ensembl; ENSMUST00000064433; ENSMUSP00000069956; ENSMUSG00000032186.
DR   Ensembl; ENSMUST00000098552; ENSMUSP00000096152; ENSMUSG00000032186.
DR   GeneID; 50876; -.
DR   KEGG; mmu:50876; -.
DR   CTD; 50876; -.
DR   MGI; MGI:1355335; Tmod2.
DR   eggNOG; roNOG07593; -.
DR   GeneTree; ENSGT00550000074341; -.
DR   HOGENOM; HBG506911; -.
DR   HOVERGEN; HBG056172; -.
DR   InParanoid; Q9JKK7; -.
DR   OMA; VFEEPPN; -.
DR   OrthoDB; EOG4X97HG; -.
DR   PhylomeDB; Q9JKK7; -.
DR   NextBio; 462045; -.
DR   ArrayExpress; Q9JKK7; -.
DR   Bgee; Q9JKK7; -.
DR   CleanEx; MM_TMOD2; -.
DR   Genevestigator; Q9JKK7; -.
DR   GermOnline; ENSMUSG00000032186; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0007611; P:learning or memory; IMP:MGI.
DR   GO; GO:0007270; P:nerve-nerve synaptic transmission; IMP:MGI.
DR   GO; GO:0045745; P:positive regulation of G-protein coupled receptor protein signaling pathway; IMP:MGI.
DR   InterPro; IPR004934; Tropomodulin.
DR   PANTHER; PTHR10901; Tropomodulin; 1.
DR   Pfam; PF03250; Tropomodulin; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing.
FT   CHAIN         1    351       Tropomodulin-2.
FT                                /FTId=PRO_0000186132.
FT   VAR_SEQ       1    191       Missing (in isoform 3).
FT                                /FTId=VSP_024895.
FT   VAR_SEQ     165    240       NVVKGEKAKPVFEEPPNPTNVEASLQQMKANDPSLQEVNLN
FT                                NIKNIPIPTLKEFAKSLETNTHVKKFSLAATRSND -> SK
FT                                LTRALGAWEVPEPAWCMFHQAQCLVSASPSVVTQGTQSYRT
FT                                HIRGTSSSGEKKSIPDKFAQSAQNANKVFCSKG (in
FT                                isoform 2).
FT                                /FTId=VSP_024896.
FT   VAR_SEQ     241    351       Missing (in isoform 2).
FT                                /FTId=VSP_024897.
FT   CONFLICT     26     27       EE -> KR (in Ref. 3; BAB29946).
FT   CONFLICT     42     42       E -> K (in Ref. 3; BAB29946).
FT   CONFLICT    157    157       E -> Q (in Ref. 1; AAF45297).
FT   CONFLICT    263    263       S -> F (in Ref. 2; AAF31669).
SQ   SEQUENCE   351 AA;  39511 MW;  640E9577D4C9CA16 CRC64;
     MALPFQKGLE KYKNIDEDEL LGKLSEEELK QLENVLDDLD PESATLPAGF RQKDQTQKAA
     TGPFDREHLL MYLEKEALEQ KDREDFVPFT GEKKGRVFIP KEKPVETRKE EKVTLDPELE
     EALASASDTE LYDLAAVLGV HNLLNNPKFD EETTNGEGRK GPVRNVVKGE KAKPVFEEPP
     NPTNVEASLQ QMKANDPSLQ EVNLNNIKNI PIPTLKEFAK SLETNTHVKK FSLAATRSND
     PVALAFAEML KVNKTLKSLN VESNFITGTG ILALVEALRE NDTLTEIKID NQRQQLGTAV
     EMEIAQMLEE NSRILKFGYQ FTKQGPRTRV AAAITKNNDL VRKKRVEGDR R
//
ID   NOVA1_MOUSE             Reviewed;         507 AA.
AC   Q9JKN6; Q8C8B9;
DT   04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   08-FEB-2011, entry version 79.
DE   RecName: Full=RNA-binding protein Nova-1;
DE   AltName: Full=Neuro-oncological ventral antigen 1;
DE   AltName: Full=Ventral neuron-specific protein 1;
GN   Name=Nova1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 15-507.
RC   STRAIN=CBA/J; TISSUE=Brain;
RX   MEDLINE=20458856; PubMed=11003693; DOI=10.1007/s003350010167;
RA   Ward-Bailey P.F., Wood B., Johnson K.R., Bronson R.T., Donahue L.R.,
RA   Davisson M.T.;
RT   "Neuromuscular ataxia: a new spontaneous mutation in the mouse.";
RL   Mamm. Genome 11:820-823(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 264-507.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   FUNCTION.
RX   MEDLINE=20182810; PubMed=10719891; DOI=10.1016/S0896-6273(00)80900-9;
RA   Jensen K.B., Dredge B.K., Stefani G., Zhong R., Buckanovich R.J.,
RA   Okano H.J., Yang Y.Y.-L., Darnell R.B.;
RT   "Nova-1 regulates neuron-specific alternative splicing and is
RT   essential for neuronal viability.";
RL   Neuron 25:359-371(2000).
RN   [5]
RP   INTERACTION WITH PTBP2.
RX   MEDLINE=20300904; PubMed=10829067; DOI=10.1073/pnas.110128397;
RA   Polydorides A.D., Okano H.J., Yang Y.Y.L., Stefani G., Darnell R.B.;
RT   "A brain-enriched polypyrimidine tract-binding protein antagonizes the
RT   ability of Nova to regulate neuron-specific alternative splicing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:6350-6355(2000).
RN   [6]
RP   FUNCTION.
RX   MEDLINE=22692957; PubMed=12808107;
RX   DOI=10.1128/MCB.23.13.4687-4700.2003;
RA   Dredge B.K., Darnell R.B.;
RT   "Nova regulates GABA(A) receptor gamma2 alternative splicing via a
RT   distal downstream UCAU-rich intronic splicing enhancer.";
RL   Mol. Cell. Biol. 23:4687-4700(2003).
RN   [7]
RP   FUNCTION, AND PHOSPHORYLATION SER-154.
RX   PubMed=15933722; DOI=10.1038/sj.emboj.7600630;
RA   Dredge B.K., Stefani G., Engelhard C.C., Darnell R.B.;
RT   "Nova autoregulation reveals dual functions in neuronal splicing.";
RL   EMBO J. 24:1608-1620(2005).
CC   -!- FUNCTION: Functions to regulate alternative splicing in neurons by
CC       binding pre-mRNA in a sequence-specific manner to activate exon
CC       inclusion. It binds specifically to the sequence UCAUY. Most
CC       likely acts to activate the inclusion of exon E3A in the glycine
CC       receptor alpha-2 chain and of exon E9 in gamma-aminobutyric-acid
CC       receptor gamma-2 subunit via a distal downstream UCAU-rich
CC       intronic splicing enhancer.
CC   -!- SUBUNIT: Interacts with PTBP2; the interaction is direct.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DISEASE: Note=Defects in Nova1 leads to neuronal death in spinal
CC       and brainstem neurons.
CC   -!- SIMILARITY: Contains 3 KH domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AC108802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC156636; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF232828; AAF35907.1; -; mRNA.
DR   EMBL; AK047565; BAC33088.1; -; mRNA.
DR   IPI; IPI00659424; -.
DR   RefSeq; NP_067336.1; NM_021361.1.
DR   UniGene; Mm.247195; -.
DR   UniGene; Mm.462575; -.
DR   ProteinModelPortal; Q9JKN6; -.
DR   SMR; Q9JKN6; 49-246, 421-492.
DR   STRING; Q9JKN6; -.
DR   PhosphoSite; Q9JKN6; -.
DR   PRIDE; Q9JKN6; -.
DR   Ensembl; ENSMUST00000021438; ENSMUSP00000021438; ENSMUSG00000021047.
DR   GeneID; 664883; -.
DR   KEGG; mmu:664883; -.
DR   UCSC; uc007nmd.1; mouse.
DR   CTD; 664883; -.
DR   MGI; MGI:104297; Nova1.
DR   GeneTree; ENSGT00550000074311; -.
DR   HOGENOM; HBG316865; -.
DR   HOVERGEN; HBG082048; -.
DR   InParanoid; Q9JKN6; -.
DR   OMA; YADINGP; -.
DR   PhylomeDB; Q9JKN6; -.
DR   NextBio; 426120; -.
DR   ArrayExpress; Q9JKN6; -.
DR   Bgee; Q9JKN6; -.
DR   CleanEx; MM_NOVA1; -.
DR   Genevestigator; Q9JKN6; -.
DR   GermOnline; ENSMUSG00000021047; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IC:MGI.
DR   GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR   GO; GO:0000398; P:nuclear mRNA splicing, via spliceosome; IDA:MGI.
DR   InterPro; IPR004087; KH.
DR   InterPro; IPR004088; KH_type_1.
DR   InterPro; IPR018111; KH_type_1_subgr.
DR   Pfam; PF00013; KH_1; 3.
DR   SMART; SM00322; KH; 3.
DR   PROSITE; PS50084; KH_TYPE_1; 3.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Repeat; RNA-binding.
FT   CHAIN         1    507       RNA-binding protein Nova-1.
FT                                /FTId=PRO_0000050117.
FT   DOMAIN       49    116       KH 1.
FT   DOMAIN      171    237       KH 2.
FT   DOMAIN      421    488       KH 3.
FT   MOTIF        27     43       Bipartite nuclear localization signal
FT                                (Potential).
FT   COMPBIAS    273    409       Ala-rich.
FT   MOD_RES     154    154       Phosphoserine.
SQ   SEQUENCE   507 AA;  51756 MW;  EB68F2D777BF8135 CRC64;
     MMAAAPIQQN GTHTGVPIDL DPPDSRKRPL EAPPEAGSTK RTNTGEDGQY FLKVLIPSYA
     AGSIIGKGGQ TIVQLQKETG ATIKLSKSKD FYPGTTERVC LIQGTIEALN AVHGFIAEKI
     REMPQNVAKT EPVSILQPQT TVNPDRIKQT LPSSPTTTKS SPSDPMTTSR ANQVKIIVPN
     STAGLIIGKG GATVKAIMEQ SGAWVQLSQK PDGINLQERV VTVSGEPEQN RKAVELIIQK
     IQEDPQSGSC LNISYANVTG PVANSNPTGS PYANTAEVLP TAAAAAGLLG HANLAGVAAF
     PAVLSGFTGN DLVAITSALN TLASYGYNLN TLGLGLSQAA ATGALAAAAA SANPAAAAAN
     LLATYASEAS ASGSTAGGTA GTFALGSLAA ATAATNGYFG AASPLAASAI LGTEKSTDGS
     KDVVEIAVPE NLVGAILGKG GKTLVEYQEL TGARIQISKK GEFVPGTRNR KVTITGTPAA
     TQAAQYLITQ RITYEQGVRA ANPQKVG
//
ID   HYOU1_MOUSE             Reviewed;         999 AA.
AC   Q9JKR6; Q3TAL1; Q3TZD0; Q3U1U2; Q64139; Q80X75;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Hypoxia up-regulated protein 1;
DE            Short=GRP-170;
DE   AltName: Full=140 kDa Ca(2+)-binding protein;
DE            Short=CBP-140;
DE   Flags: Precursor;
GN   Name=Hyou1; Synonyms=Grp170;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Chen X., Easton D.P., Subjeck J.R.;
RT   "The 170 kDa glucose regulated protein of mouse.";
RL   Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Inner ear, Placenta, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 347-999, AND SUBCELLULAR LOCATION.
RX   MEDLINE=95368740; PubMed=7641295;
RA   Naved A.F., Ozawa M., Yu S., Miyauchi T., Muramatsu H., Muramatsu T.;
RT   "CBP-140, a novel endoplasmic reticulum resident Ca(2+)-binding
RT   protein with a carboxy-terminal NDEL sequence showed partial homology
RT   with 70-kDa heat shock protein (hsp70).";
RL   Cell Struct. Funct. 20:133-141(1995).
RN   [5]
RP   PROTEIN SEQUENCE OF 439-451.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [6]
RP   COMPONENT OF A CHAPERONE COMPLEX.
RX   PubMed=12475965; DOI=10.1091/mbc.E02-05-0311;
RA   Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
RT   "A subset of chaperones and folding enzymes form multiprotein
RT   complexes in endoplasmic reticulum to bind nascent proteins.";
RL   Mol. Biol. Cell 13:4456-4469(2002).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Has a pivotal role in cytoprotective cellular mechanisms
CC       triggered by oxygen deprivation. May play a role as a molecular
CC       chaperone and participate in protein folding (By similarity).
CC   -!- SUBUNIT: Part a large chaperone multiprotein complex comprising
CC       DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1,
CC       UGT1A1 and very small amounts of ERP29, but not, or at very low
CC       levels, CALR nor CANX.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF228709; AAF65544.1; -; mRNA.
DR   EMBL; AK171769; BAE42657.1; -; mRNA.
DR   EMBL; AK145857; BAE26702.1; -; mRNA.
DR   EMBL; AK155721; BAE33401.1; -; mRNA.
DR   EMBL; AK157949; BAE34279.1; -; mRNA.
DR   EMBL; BC050107; AAH50107.1; -; mRNA.
DR   EMBL; S78797; AAB35051.1; -; mRNA.
DR   IPI; IPI00123342; -.
DR   RefSeq; NP_067370.3; NM_021395.4.
DR   UniGene; Mm.116721; -.
DR   ProteinModelPortal; Q9JKR6; -.
DR   SMR; Q9JKR6; 25-555.
DR   STRING; Q9JKR6; -.
DR   PhosphoSite; Q9JKR6; -.
DR   REPRODUCTION-2DPAGE; IPI00123342; -.
DR   REPRODUCTION-2DPAGE; Q3TZD0; -.
DR   REPRODUCTION-2DPAGE; Q64139; -.
DR   REPRODUCTION-2DPAGE; Q9JKR6; -.
DR   PRIDE; Q9JKR6; -.
DR   Ensembl; ENSMUST00000066601; ENSMUSP00000068594; ENSMUSG00000032115.
DR   GeneID; 12282; -.
DR   KEGG; mmu:12282; -.
DR   UCSC; uc009pdf.1; mouse.
DR   CTD; 12282; -.
DR   MGI; MGI:108030; Hyou1.
DR   eggNOG; roNOG12656; -.
DR   GeneTree; ENSGT00390000016919; -.
DR   HOGENOM; HBG379834; -.
DR   HOVERGEN; HBG106402; -.
DR   InParanoid; Q9JKR6; -.
DR   OMA; TVCTIVT; -.
DR   OrthoDB; EOG4R5021; -.
DR   PhylomeDB; Q9JKR6; -.
DR   NextBio; 280746; -.
DR   ArrayExpress; Q9JKR6; -.
DR   Bgee; Q9JKR6; -.
DR   CleanEx; MM_HYOU1; -.
DR   Genevestigator; Q9JKR6; -.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR001023; Hsp70.
DR   InterPro; IPR013126; Hsp_70.
DR   PANTHER; PTHR19375; Hsp70; 1.
DR   Pfam; PF00012; HSP70; 2.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Chaperone; Direct protein sequencing;
KW   Endoplasmic reticulum; Glycoprotein; Nucleotide-binding; Signal;
KW   Stress response.
FT   SIGNAL        1     32       By similarity.
FT   CHAIN        33    999       Hypoxia up-regulated protein 1.
FT                                /FTId=PRO_5000057827.
FT   MOTIF       996    999       Prevents secretion from ER (Potential).
FT   COMPBIAS    603    606       Poly-Glu.
FT   CARBOHYD    155    155       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    222    222       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    515    515       N-linked (GlcNAc...).
FT   CARBOHYD    596    596       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    830    830       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    862    862       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    869    869       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    922    922       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    931    931       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    137    137       Q -> L (in Ref. 3; AAH50107).
FT   CONFLICT    227    227       N -> D (in Ref. 3; AAH50107).
FT   CONFLICT    247    247       T -> A (in Ref. 2; BAE34279).
FT   CONFLICT    290    290       Q -> R (in Ref. 2; BAE42657).
FT   CONFLICT    467    467       R -> G (in Ref. 4; AAB35051).
FT   CONFLICT    540    540       K -> R (in Ref. 3; AAH50107).
FT   CONFLICT    615    615       E -> K (in Ref. 3; AAH50107).
FT   CONFLICT    665    665       Missing (in Ref. 4; AAB35051).
FT   CONFLICT    687    687       P -> L (in Ref. 4; AAB35051).
FT   CONFLICT    710    710       D -> N (in Ref. 4; AAB35051).
FT   CONFLICT    734    734       Q -> R (in Ref. 3; AAH50107).
FT   CONFLICT    744    744       E -> K (in Ref. 3; AAH50107).
FT   CONFLICT    772    772       S -> P (in Ref. 3; AAH50107).
SQ   SEQUENCE   999 AA;  111181 MW;  2951482D1EE2EF36 CRC64;
     MAATVRRQRP RRLLCWALVA VLLADLLALS DTLAVMSVDL GSESMKVAIV KPGVPMEIVL
     NKESRRKTPV TVTLKENERF LGDSAAGMAI KNPKATLRYF QHLLGKQADN PHVALYRSRF
     PEHELIVDPQ RQTVRFQISP QLQFSPEEVL GMVLNYSRSL AEDFAEQPIK DAVITVPAFF
     NQAERRAVLQ AARMAGLKVL QLINDNTATA LSYGVFRRKD INSTAQNVMF YDMGSGSTVC
     TIVTYQTVKT KEAGMQPQLQ IRGVGFDRTL GGLEMELRLR EHLAKLFNEQ RKGQKAKDVR
     ENPRAMAKLL REANRLKTVL SANADHMAQI EGLMDDVDFK AKVTRVEFEE LCADLFDRVP
     GPVQQALQSA EMSLDQIEQV ILVGGATRVP KVQEVLLKAV GKEELGKNIN ADEAAAMGAV
     YQAAALSKAF KVKPFVVRDA VIYPILVEFT REVEEEPGLR SLKHNKRVLF SRMGPYPQRK
     VITFNRYSHD FNFHINYGDL GFLGPEDLRV FGSQNLTTVK LKGVGESFKK YPDYESKGIK
     AHFNLDESGV LSLDRVESVF ETLVEDSPEE ESTLTKLGNT ISSLFGGGTS SDAKENGTDA
     VQEEEESPAE GSKDEPAEQG ELKEEAEPPA EETSQPPPSE PKGDAAREGE KPDEKESGDK
     PEAQKPNEKG QAGPEGAAPA PEEDKKPKPA RKQKMVEEIG VELAVLDLPD LPEDELARSV
     QKLEELTLRD LEKQEREKAA NSLEAFIFET QDKLYQPEYQ EVSTEEQREE ISGKLSATST
     WLEDEGFGAT TVMLKDKLAE LRKLCQGLFF RVEERRKWPE RLSALDNLLN HSSIFLKGAR
     LIPEMDQVFT EVEMTTLEKV INDTWAWKNA TLAEQAKLPA TEKPVLLSKD IEAKMMALDR
     EVQYLLNKAK FTKPRPRPKD KNGTRAEPPL NASAGDQEEK VIPPAGQTEE AKPILEPDKE
     ETGTEPADSE PLELGGPGAG PEQEEQSAGQ KRPSKNDEL
//
ID   HABP4_MOUSE             Reviewed;         411 AA.
AC   Q9JKS5; Q3UNH8; Q9D450;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Intracellular hyaluronan-binding protein 4;
DE            Short=IHABP-4;
DE            Short=IHABP4;
GN   Name=Habp4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=20449071; PubMed=10887182; DOI=10.1074/jbc.M002737200;
RA   Huang L., Grammatikakis N., Yoneda M., Banerjee S.D., Toole B.P.;
RT   "Molecular characterization of a novel intracellular hyaluronan-
RT   binding protein.";
RL   J. Biol. Chem. 275:29829-29839(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: May be involved in nuclear functions such as the
CC       remodeling of chromatin and the regulation of transcription (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with the C-terminus of CHD3. Interacts via its
CC       C-terminal region with GNB2L1. Interacts with p53/TP53 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Transported into the nuclear compartment in
CC       activated leukocytes (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in adult heart, brain, liver,
CC       kidney, testis, and in various embryonic tissues, but not in adult
CC       spleen, lung or skeletal muscle.
CC   -!- PTM: Phosphorylated by phorbol 12-myristate 13-acetate (PMA)-
CC       activated PKC isoforms at Thr-352 and Thr-373 (By similarity).
CC   -!- MISCELLANEOUS: Able to bind hyaluronan. However, its intracellular
CC       localization suggests that this interaction may not be relevant in
CC       vivo.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB30437.1; Type=Miscellaneous discrepancy; Note=Intron retention;
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DR   EMBL; AF227684; AAF36966.1; -; mRNA.
DR   EMBL; AK016800; BAB30437.1; ALT_SEQ; mRNA.
DR   EMBL; AK144206; BAE25769.1; -; mRNA.
DR   IPI; IPI00123374; -.
DR   RefSeq; NP_064370.2; NM_019986.3.
DR   UniGene; Mm.40989; -.
DR   STRING; Q9JKS5; -.
DR   PhosphoSite; Q9JKS5; -.
DR   PRIDE; Q9JKS5; -.
DR   Ensembl; ENSMUST00000021929; ENSMUSP00000021929; ENSMUSG00000021476.
DR   GeneID; 56541; -.
DR   KEGG; mmu:56541; -.
DR   UCSC; uc007qyl.1; mouse.
DR   CTD; 56541; -.
DR   MGI; MGI:1891713; Habp4.
DR   GeneTree; ENSGT00520000055591; -.
DR   HOGENOM; HBG713968; -.
DR   HOVERGEN; HBG056357; -.
DR   InParanoid; Q9JKS5; -.
DR   OrthoDB; EOG4V438Z; -.
DR   NextBio; 312906; -.
DR   ArrayExpress; Q9JKS5; -.
DR   Bgee; Q9JKS5; -.
DR   CleanEx; MM_HABP4; -.
DR   Genevestigator; Q9JKS5; -.
DR   GermOnline; ENSMUSG00000021476; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR006861; HABP4_PAIRBP1-bd.
DR   Pfam; PF04774; HABP4_PAI-RBP1; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Nucleus; Phosphoprotein; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    411       Intracellular hyaluronan-binding protein
FT                                4.
FT                                /FTId=PRO_0000257973.
FT   COILED       42     62       Potential.
FT   COILED      279    301       Potential.
FT   MOD_RES      97     97       Phosphoserine (By similarity).
FT   MOD_RES     108    108       Phosphoserine (By similarity).
FT   MOD_RES     352    352       Phosphothreonine; by PKC (By similarity).
FT   MOD_RES     373    373       Phosphothreonine; by PKC (By similarity).
FT   CONFLICT     64     64       A -> AA (in Ref. 2; BAB30437).
FT   CONFLICT    187    187       P -> L (in Ref. 2; BAE25769).
FT   CONFLICT    194    194       R -> K (in Ref. 1; AAF36966).
FT   CONFLICT    266    266       T -> A (in Ref. 2; BAB30437).
SQ   SEQUENCE   411 AA;  45924 MW;  234C0E38C98990F4 CRC64;
     MKGALGSPVA AAGAAMQETF GCVVANRFHQ LLDDESDPFD ILREAEHRRQ QQLQRKRRDE
     AAAASGAGHR GGRSPAVASG HRPGAGGRRE SQKERKSLAA SGAQQPDSPG GPQPPGQKRT
     PRRGEQQGWN DNRGTDVVLE RAERRSYREY RPYETERQAD LPVEKFTDEK PVDRFDRDRP
     LRGRGGPRGG LRSRGRGGPG NRAFDSFDQR GKRDFERYSS NDKTNRMEDS MGGCGIRPWG
     SGKDTSDTEP PAPMEETSMM EECQGTLDEE SAAKVPELEV EEENQVQEMT LDEWKNLQEQ
     TRPKPEFNIR KPESTVPSKA VVIHKSRYRD DMVKEDYEDE SHVFRKAAND ITSQLEINFG
     NLPRPGRGAR GSTRGGRGRM RRTENYGPRA EVVTQDVAPN PDDPEDFPAL A
//
ID   SC5A3_MOUSE             Reviewed;         718 AA.
AC   Q9JKZ2;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Sodium/myo-inositol cotransporter;
DE            Short=Na(+)/myo-inositol cotransporter;
DE   AltName: Full=Solute carrier family 5 member 3;
GN   Name=Slc5a3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=20237552; PubMed=10773690;
RA   McVeigh K.E., Mallee J.J., Lucente A., Barnoski B.L., Wu S.,
RA   Berry G.T.;
RT   "Murine chromosome 16 telomeric region, homologous with human
RT   chromosome 21q22, contains the osmoregulatory Na(+)/myo-inositol
RT   cotransporter (SLC5A3) gene.";
RL   Cytogenet. Cell Genet. 88:153-158(2000).
CC   -!- FUNCTION: Prevents intracellular accumulation of high
CC       concentrations of myo-inositol (an osmolyte) that result in
CC       impairment of cellular function.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF)
CC       (TC 2.A.21) family.
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DR   EMBL; AF220915; AAF43668.1; -; Genomic_DNA.
DR   IPI; IPI00123644; -.
DR   UniGene; Mm.217354; -.
DR   UniGene; Mm.451146; -.
DR   ProteinModelPortal; Q9JKZ2; -.
DR   SMR; Q9JKZ2; 6-539.
DR   PRIDE; Q9JKZ2; -.
DR   Ensembl; ENSMUST00000113975; ENSMUSP00000109608; ENSMUSG00000089774.
DR   UCSC; uc007zyt.1; mouse.
DR   MGI; MGI:1858226; Slc5a3.
DR   GeneTree; ENSGT00550000074313; -.
DR   HOGENOM; HBG585824; -.
DR   HOVERGEN; HBG052859; -.
DR   InParanoid; Q9JKZ2; -.
DR   OrthoDB; EOG4JQ3X1; -.
DR   PhylomeDB; Q9JKZ2; -.
DR   ArrayExpress; Q9JKZ2; -.
DR   Bgee; Q9JKZ2; -.
DR   Genevestigator; Q9JKZ2; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0006020; P:inositol metabolic process; IMP:MGI.
DR   GO; GO:0015798; P:myo-inositol transport; IMP:MGI.
DR   GO; GO:0007422; P:peripheral nervous system development; IMP:MGI.
DR   GO; GO:0043576; P:regulation of respiratory gaseous exchange; IMP:MGI.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR001734; Na/solute_symporter.
DR   InterPro; IPR018212; Na/solute_symporter_CS.
DR   InterPro; IPR019900; Na/solute_symporter_subgr.
DR   PANTHER; PTHR11819; Na/solut_symport; 1.
DR   Pfam; PF00474; SSF; 1.
DR   TIGRFAMs; TIGR00813; sss; 1.
DR   PROSITE; PS00456; NA_SOLUT_SYMP_1; 1.
DR   PROSITE; PS00457; NA_SOLUT_SYMP_2; 1.
DR   PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Ion transport; Membrane; Sodium; Sodium transport;
KW   Symport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    718       Sodium/myo-inositol cotransporter.
FT                                /FTId=PRO_0000105382.
FT   TOPO_DOM      1      9       Cytoplasmic (Potential).
FT   TRANSMEM     10     29       Helical; (Potential).
FT   TOPO_DOM     30     38       Extracellular (Potential).
FT   TRANSMEM     39     57       Helical; (Potential).
FT   TOPO_DOM     58     86       Cytoplasmic (Potential).
FT   TRANSMEM     87    110       Helical; (Potential).
FT   TOPO_DOM    111    123       Extracellular (Potential).
FT   TRANSMEM    124    144       Helical; (Potential).
FT   TOPO_DOM    145    157       Cytoplasmic (Potential).
FT   TRANSMEM    158    183       Helical; (Potential).
FT   TOPO_DOM    184    186       Extracellular (Potential).
FT   TRANSMEM    187    205       Helical; (Potential).
FT   TOPO_DOM    206    303       Cytoplasmic (Potential).
FT   TRANSMEM    304    324       Helical; (Potential).
FT   TOPO_DOM    325    353       Extracellular (Potential).
FT   TRANSMEM    354    376       Helical; (Potential).
FT   TOPO_DOM    377    406       Cytoplasmic (Potential).
FT   TRANSMEM    407    430       Helical; (Potential).
FT   TOPO_DOM    431    443       Extracellular (Potential).
FT   TRANSMEM    444    462       Helical; (Potential).
FT   TOPO_DOM    463    510       Cytoplasmic (Potential).
FT   TRANSMEM    511    532       Helical; (Potential).
FT   TOPO_DOM    533    695       Extracellular (Potential).
FT   TRANSMEM    696    716       Helical; (Potential).
FT   SITE         24     24       Implicated in sodium coupling (By
FT                                similarity).
FT   SITE        285    285       Implicated in sodium coupling (By
FT                                similarity).
FT   CARBOHYD     32     32       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   718 AA;  79555 MW;  D035CFBECDDA803B CRC64;
     MRAVLEAADI AVVALYFILV MCIGFFAMWK SNRSTVSGYF LAGRSMTWVA IGASLFVSNI
     GSEHFIGLAG SGAASGFAVG AWEFNALLLL QLLGWVFIPI YIRSGVYTMP EYLSKRFGGH
     RIQVYFAALS LLLYIFTKLS VDLYSGALFI QESLGWNLYV SVILLIGMTA LLTVTGGLVA
     VIYTDTLQAL LMIIGALTLM VISMVKIGGF EEVKRRYMLA SPDVASILLK YNLSNTNACM
     VHPKANALKM LRDPTDEDVP WPGFILGQTP ASVWYWCADQ VIVQRVLAAK NIAHAKGSTL
     MAGFLKLLPM FIIVVPGMIS RIVFADEIAC INPEHCMQVC GSRAGCSNIA YPRLVMTLVP
     VGLRGLMMAV MIAALMSDLD SIFNSASTIF TLDVYKLIRK SASSRELMIV GRIFVAFMVV
     ISIAWVPIIV EMQGGQMYLY IQEVADYLTP PVAALFLLAI FWKRCNEQGA FYGGMAGFVL
     GAVRLILAFT YRAPECDQPD NRPGFIKDIH YMYVATALFW ITGLITVIVS LLTPPPTKDQ
     IRTTTFWSKK TLVTKESCSQ KDEPYKMQEK SILQCSENSE VISHTIPNGK SEDSIKGLQP
     EDVNLLVTCR EEGNPVASMG HSEAETPVDA YSNGQAALMG EREREKETEN RSQYWKFIDW
     FCGFKSKSLS KRSLRDLMDE EAVCLQMLEE TPQVKVILNI GLFAVCSLGI FMFVYFSL
//
ID   FMN2_MOUSE              Reviewed;        1578 AA.
AC   Q9JL04; Q505D3;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Formin-2;
GN   Name=Fmn2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=20245324; PubMed=10781961; DOI=10.1016/S0925-4773(00)00276-8;
RA   Leader B., Leder P.;
RT   "Formin-2, a novel formin homology protein of the cappuccino
RT   subfamily, is highly expressed in the developing and adult central
RT   nervous system.";
RL   Mech. Dev. 93:221-231(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-724, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339; SER-493 AND
RP   THR-723, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- TISSUE SPECIFICITY: Expressed almost exclusively in the developing
CC       and mature central nervous system.
CC   -!- DEVELOPMENTAL STAGE: Expression begins at embryonic day 9.5 in the
CC       developing spinal cord and brain structures and continues in
CC       neonatal and adult brain structures including the olfactory bulb,
CC       cortex, thalamus, hypothalamus, hippocampus and cerebellum.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the formin homology family. Cappuccino
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 FH1 (formin homology 1) domain.
CC   -!- SIMILARITY: Contains 1 FH2 (formin homology 2) domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF218940; AAF72883.1; -; mRNA.
DR   EMBL; BC094606; AAH94606.1; -; mRNA.
DR   IPI; IPI00123295; -.
DR   RefSeq; NP_062318.2; NM_019445.2.
DR   UniGene; Mm.330620; -.
DR   ProteinModelPortal; Q9JL04; -.
DR   SMR; Q9JL04; 1138-1542.
DR   STRING; Q9JL04; -.
DR   PhosphoSite; Q9JL04; -.
DR   PRIDE; Q9JL04; -.
DR   Ensembl; ENSMUST00000030039; ENSMUSP00000030039; ENSMUSG00000028354.
DR   GeneID; 54418; -.
DR   KEGG; mmu:54418; -.
DR   UCSC; uc007dtc.1; mouse.
DR   CTD; 54418; -.
DR   MGI; MGI:1859252; Fmn2.
DR   GeneTree; ENSGT00560000076948; -.
DR   HOGENOM; HBG755275; -.
DR   HOVERGEN; HBG107923; -.
DR   InParanoid; Q9JL04; -.
DR   OMA; PSKPPDE; -.
DR   OrthoDB; EOG4M0F16; -.
DR   NextBio; 311284; -.
DR   ArrayExpress; Q9JL04; -.
DR   Bgee; Q9JL04; -.
DR   CleanEx; MM_FMN2; -.
DR   Genevestigator; Q9JL04; -.
DR   GermOnline; ENSMUSG00000028354; Mus musculus.
DR   GO; GO:0015629; C:actin cytoskeleton; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0051295; P:establishment of meiotic spindle localization; IMP:BHF-UCL.
DR   GO; GO:0016344; P:meiotic chromosome movement towards spindle pole; IMP:BHF-UCL.
DR   GO; GO:0007132; P:meiotic metaphase I; IMP:BHF-UCL.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0048477; P:oogenesis; IMP:BHF-UCL.
DR   GO; GO:0040038; P:polar body extrusion after meiotic divisions; IMP:BHF-UCL.
DR   InterPro; IPR003104; Actin-bd_FH2/DRF_autoreg.
DR   InterPro; IPR015425; FH2_actin-bd.
DR   InterPro; IPR001265; Formin.
DR   InterPro; IPR009408; Formin_homology_1.
DR   Pfam; PF06346; Drf_FH1; 2.
DR   Pfam; PF02181; FH2; 1.
DR   PRINTS; PR00828; FORMIN.
DR   SMART; SM00498; FH2; 1.
DR   SUPFAM; SSF101447; FH2_actin_bd; 1.
DR   PROSITE; PS51444; FH2; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Developmental protein; Phosphoprotein; Repeat.
FT   CHAIN         1   1578       Formin-2.
FT                                /FTId=PRO_0000194889.
FT   DOMAIN      735   1124       FH1.
FT   REPEAT      919    929       1.
FT   REPEAT      930    940       2.
FT   REPEAT      941    951       3.
FT   REPEAT      952    962       4.
FT   REPEAT      963    973       5.
FT   REPEAT      974    984       6.
FT   REPEAT      985    995       7.
FT   REPEAT      996   1006       8.
FT   REPEAT     1007   1017       9.
FT   REPEAT     1018   1028       10.
FT   REPEAT     1029   1039       11.
FT   REPEAT     1040   1050       12.
FT   DOMAIN     1139   1554       FH2.
FT   REGION      919   1039       12 X 11 AA tandem repeats of [MV]-G-I-P-
FT                                P-P-P-P-L-P-G.
FT   COILED      643    683       Potential.
FT   COILED     1419   1455       Potential.
FT   COMPBIAS     48     55       Poly-Gly.
FT   COMPBIAS    202    207       Poly-Gln.
FT   COMPBIAS    797    801       Poly-Pro.
FT   COMPBIAS    861    864       Poly-Pro.
FT   COMPBIAS    908    917       Poly-Pro.
FT   COMPBIAS    922    928       Poly-Pro.
FT   COMPBIAS    933    939       Poly-Pro.
FT   COMPBIAS    955    961       Poly-Pro.
FT   COMPBIAS    966    972       Poly-Pro.
FT   COMPBIAS    977    983       Poly-Pro.
FT   COMPBIAS    988    994       Poly-Pro.
FT   COMPBIAS    999   1005       Poly-Pro.
FT   COMPBIAS   1010   1016       Poly-Pro.
FT   COMPBIAS   1021   1027       Poly-Pro.
FT   COMPBIAS   1032   1038       Poly-Pro.
FT   COMPBIAS   1043   1049       Poly-Pro.
FT   COMPBIAS   1054   1057       Poly-Pro.
FT   COMPBIAS   1065   1071       Poly-Pro.
FT   COMPBIAS   1076   1083       Poly-Pro.
FT   COMPBIAS   1088   1091       Poly-Pro.
FT   MOD_RES     339    339       Phosphoserine.
FT   MOD_RES     373    373       Phosphoserine (By similarity).
FT   MOD_RES     377    377       Phosphoserine (By similarity).
FT   MOD_RES     381    381       Phosphoserine (By similarity).
FT   MOD_RES     493    493       Phosphoserine.
FT   MOD_RES     723    723       Phosphothreonine.
FT   MOD_RES     724    724       Phosphoserine.
FT   CONFLICT     33     33       I -> T (in Ref. 2; AAH94606).
FT   CONFLICT    348    348       V -> M (in Ref. 2; AAH94606).
FT   CONFLICT    372    372       V -> A (in Ref. 2; AAH94606).
FT   CONFLICT    430    432       RSS -> PSP (in Ref. 2; AAH94606).
FT   CONFLICT    745    745       L -> P (in Ref. 2; AAH94606).
FT   CONFLICT    936    946       Missing (in Ref. 2; AAH94606).
FT   CONFLICT   1040   1040       V -> M (in Ref. 2; AAH94606).
FT   CONFLICT   1142   1142       L -> P (in Ref. 2; AAH94606).
SQ   SEQUENCE   1578 AA;  167387 MW;  DD0FDC8FC25C47DB CRC64;
     MGNQDGKLKR SAGDASHEGG GAEDAAGPRD AEITKKASGS KKALGKHGKG GGGSGETSKK
     KSKSDSRASV FSNLRIRKNL TKGKGACDSR EDVLDSQALP IGELDSAHSI VTKTPDLSLS
     AEETGLSDTE CADPFEVIHP GASRPAEAGV GIQATAEDLE TAAGAQDGQR TSSGSDTDIY
     SFHSATEQED LLSDIQQAIR LQQQQQQKLL LQDSEEPAAP PTAISPQPGA FLGLDQFLLG
     PRSEAEKDTV QALPVRPDLP ETTKSLVPEH PPSSGSHLTS ETPGYATAPS AVTDSLSSPA
     FTFPEAGPGE GAAGVPVAGT GDTDEECEED AFEDAPRGSP GEEWVPEVEE ASQRLEKEPE
     EGMRESITSA VVSLPGSPAP SPRCFKPYPL ITPCYIKTTT RQLSSPNHSP SQSPNQSPRI
     KKRPDPSVSR SSRTALASAA APAKKHRLEG GLTGGLSRSA DWTEELGVRT PGAGGSVHLL
     GRGATADDSG GGSPVLAAKA PGAPATADGF QNVFTGRTLL EKLFSQQENG PPEEAEKFCS
     RIIAMGLLLP FSDCFREPCN QNAGSSSAPF DQDQLYTWAA VSQPTHSMDY SEGQFPRREP
     SMWPSSKLPE EEPSPKDVDT EPKSSILESP KKCSNGVQQE VFDVKSEGQA TVIQQLEQTI
     EDLRTKIAEL EKQYPALDLE GPRGLSGLEN GLTASADVSL DALVLHGKVA QPPRTLEAKS
     IQTSPTEEGR ILTLPPPKAP PEGLLGSPAA ASGESALLTS PSGPQTKFCS EISLIVSPRR
     ISVQLDAQQI QSASQLPPPP PLLGSDSQGQ PSQPSLHTES ETSHEHSVSS SFGNNCNVPP
     APPLPCTESS SFMPGLGMAI PPPPCLSDIT VPALPSPTAP ALQFSNLQGP EMLPAPPQPP
     PLPGLGVPPP PPAPPLPGMG IPPPPPLPGM GIPPPPPLPG MGISPLPPLP GMGIPPPPPL
     PGVGIPPPPP LPGVGIPPPP PLPGVGIPPP PPLPGVGIPP PPPLPGVGIP PPPPLPGVGI
     PPPPPLPGVG IPPPPPLPGV GIPPPPPLPG SGIPPPPALP GVAIPPPPPL PGMGVPPPAP
     PPPGAGIPPP PLLPGSGPPH SSQVGSSTLP AAPQGCGFLF PPLPTGLFGL GMNQDRVARK
     QLIEPCRPMK PLYWTRIQLH SKRDSSPSLI WEKIEEPSID CHEFEELFSK TAVKERKKPI
     SDTISKTKAK QVVKLLSNKR SQAVGILMSS LHLDMKDIQH AVVNLDNSVV DLETLQALYE
     NRAQSDELEK IEKHSRSSKD KENAKSLDKP EQFLYELSLI PNFSERVFCI LFQSTFSESI
     CSIRRKLELL QKLCETLKNG PGVMQVLGLV LAFGNYMNAG NKTRGQADGF GLDILPKLKD
     VKSSDNSRSL LSYIVSYYLR NFDEDAGKEQ CVFPLAEPQE LFQASQMKFE DFQKDLRKLK
     KDLKACEAEA GKVYQVSSAE HMQPFKENME QFISQAKIDQ ESQEAALTET HKCFLETTAY
     YFMKPKLGEK EVSPNVFFSV WHEFSSDFKD AWKKENKLIL QERVKEAEEV CRQKKGKSLY
     KVKPRHDSGI KAKISMKT
//
ID   FMNL_MOUSE              Reviewed;        1094 AA.
AC   Q9JL26; Q6KAN4; Q9Z2V7;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Formin-like protein 1;
DE   AltName: Full=Formin-related protein;
GN   Name=Fmnl1; Synonyms=Frl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION
RP   WITH RAC1; PFN1 AND PFN2, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   MEDLINE=20414696; PubMed=10958683;
RX   DOI=10.1128/MCB.20.18.6872-6881.2000;
RA   Yayoshi-Yamamoto S., Taniuchi I., Watanabe T.;
RT   "FRL, a novel formin-related protein, binds to Rac and regulates cell
RT   motility and survival of macrophages.";
RL   Mol. Cell. Biol. 20:6872-6881(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 231-1094.
RC   TISSUE=Natural killer cell;
RX   PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of FLJ genes:
RT   the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:127-135(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: May play a role in the control of cell motility and
CC       survival of macrophages.
CC   -!- SUBUNIT: Interacts with RAC1, PFN1 and PFN2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Frlalpha;
CC         IsoId=Q9JL26-1; Sequence=Displayed;
CC       Name=2; Synonyms=Frlbeta;
CC         IsoId=Q9JL26-2; Sequence=VSP_013978, VSP_013979, VSP_013980;
CC   -!- TISSUE SPECIFICITY: Highly expressed in the spleen, lymph node and
CC       bone marrow cells.
CC   -!- SIMILARITY: Belongs to the formin homology family.
CC   -!- SIMILARITY: Contains 1 DAD (diaphanous autoregulatory) domain.
CC   -!- SIMILARITY: Contains 1 FH2 (formin homology 2) domain.
CC   -!- SIMILARITY: Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology
CC       3) domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF006466; AAD01273.1; -; mRNA.
DR   EMBL; AF215666; AAF25953.1; -; mRNA.
DR   EMBL; AK131173; BAD21423.1; -; mRNA.
DR   IPI; IPI00123377; -.
DR   IPI; IPI00131441; -.
DR   PIR; T13963; T13963.
DR   RefSeq; NP_001071166.1; NM_001077698.1.
DR   RefSeq; NP_062653.2; NM_019679.2.
DR   UniGene; Mm.138913; -.
DR   ProteinModelPortal; Q9JL26; -.
DR   SMR; Q9JL26; 35-381, 623-1019.
DR   STRING; Q9JL26; -.
DR   PhosphoSite; Q9JL26; -.
DR   PRIDE; Q9JL26; -.
DR   Ensembl; ENSMUST00000042286; ENSMUSP00000046296; ENSMUSG00000055805.
DR   Ensembl; ENSMUST00000107027; ENSMUSP00000102642; ENSMUSG00000055805.
DR   GeneID; 57778; -.
DR   KEGG; mmu:57778; -.
DR   UCSC; uc007ltu.1; mouse.
DR   UCSC; uc007ltv.1; mouse.
DR   CTD; 57778; -.
DR   MGI; MGI:1888994; Fmnl1.
DR   GeneTree; ENSGT00570000078740; -.
DR   HOGENOM; HBG445684; -.
DR   HOVERGEN; HBG053118; -.
DR   InParanoid; Q9JL26; -.
DR   OMA; PLIYESD; -.
DR   OrthoDB; EOG4R502B; -.
DR   PhylomeDB; Q9JL26; -.
DR   NextBio; 313954; -.
DR   ArrayExpress; Q9JL26; -.
DR   Bgee; Q9JL26; -.
DR   CleanEx; MM_FMNL1; -.
DR   Genevestigator; Q9JL26; -.
DR   GermOnline; ENSMUSG00000055805; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0005522; F:profilin binding; IDA:MGI.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0006929; P:substrate-dependent cell migration; IMP:MGI.
DR   InterPro; IPR003104; Actin-bd_FH2/DRF_autoreg.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR014767; Diaphanous_autoregulatory.
DR   InterPro; IPR010472; Drf_FH3.
DR   InterPro; IPR010473; Drf_GTPase-bd.
DR   InterPro; IPR015425; FH2_actin-bd.
DR   InterPro; IPR014768; GTPase-bd/formin_homology_3.
DR   Pfam; PF06367; Drf_FH3; 1.
DR   Pfam; PF06371; Drf_GBD; 2.
DR   Pfam; PF02181; FH2; 1.
DR   SMART; SM00498; FH2; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF101447; FH2_actin_bd; 1.
DR   PROSITE; PS51231; DAD; 1.
DR   PROSITE; PS51444; FH2; 1.
DR   PROSITE; PS51232; GBD_FH3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Phosphoprotein.
FT   CHAIN         1   1094       Formin-like protein 1.
FT                                /FTId=PRO_0000194891.
FT   DOMAIN       27    464       GBD/FH3.
FT   DOMAIN      627   1018       FH2.
FT   DOMAIN     1049   1082       DAD.
FT   COMPBIAS    532    611       Pro-rich.
FT   MOD_RES     184    184       Phosphoserine.
FT   MOD_RES    1010   1010       Phosphothreonine (By similarity).
FT   MOD_RES    1021   1021       Phosphoserine (By similarity).
FT   VAR_SEQ       1     26       Missing (in isoform 2).
FT                                /FTId=VSP_013978.
FT   VAR_SEQ      27     30       QPMP -> MVGT (in isoform 2).
FT                                /FTId=VSP_013979.
FT   VAR_SEQ    1061   1094       DLRNQPYIRADTGRRSARRRPPGPPLPVTTDLAL -> VLK
FT                                TVPFTARTGKRTSRLLCEASLGEEMTL (in isoform
FT                                2).
FT                                /FTId=VSP_013980.
FT   CONFLICT     64     64       K -> R (in Ref. 1; AAD01273).
FT   CONFLICT     94     94       G -> D (in Ref. 1; AAD01273).
FT   CONFLICT    111    111       K -> R (in Ref. 1; AAD01273).
FT   CONFLICT    117    117       S -> F (in Ref. 1; AAD01273).
FT   CONFLICT    581    581       P -> H (in Ref. 1; AAD01273).
FT   CONFLICT    620    620       D -> N (in Ref. 1; AAD01273).
FT   CONFLICT    981    981       F -> L (in Ref. 1; AAD01273).
SQ   SEQUENCE   1094 AA;  122060 MW;  23A4BF24FB8F7A68 CRC64;
     MGNAAGSAEQ PAGPTASPPK QPAVPKQPMP AAGELEERFT RVLNCMNLPP DKVQLLSQYD
     NEKKWELICD QERFQVKNPP AAYIQKLKSY LDTGGVSRKV ASDWMSNLGF KRRVQESTQV
     LRELETSLRT NHIGWVQEFL NEENRGLDVL LEYLAFAQCS VAYDMESTDS VASGAEKSKP
     LDQSVEDLSK APPSSVPKSR LTIKLTPAHS RKALRNSRIV SQKDDVHVCI MCLRAIMNYQ
     SGFSLVMNHP ACVNEIALSL NNKSPRTKAL VLELLAAVCL VRGGHDIILA AFDNFKEVCG
     EQHRFEKLME YFRHEDSNID FMVACMQFIN IVVHSVENMN FRVFLQYEFT HLGLDLYLER
     LRLTESDKLQ VQIQAYLDNV FDVGTLLEET ETKNAVLEHM EELQEQVATL TERLRDTEND
     SMAKIAELEK QLSQARKELE TLRERFSEST PMGTSRRIPE PEKVPVPTVV RPSALELKVE
     ELEEKGLIRI LRGPGDVVSI EILPGAAATP SGDDAQAPRV STDSPSTAES IPEAASPPPP
     PPPPPPPLPN LQSQQEAPPS APPLAPPLPG CAEPPPAPPL PGDLPPPPPP PPLGTDGPVP
     PPPPPPPGGP PDILGGQGPD IGPGVKAKKP IQTKFRMPLL NWVALKPSQI TGTVFTELND
     EKVLQELDMN DFEEHFKTKS QGPCLDISAL KGKASQKAPT KTILIEANRA KNLAITLRKG
     NLGADRICQA IETYDLQTLS LDFLELLTRF LPTDYERSLI ARFEKEQRPM EELSEEDRFM
     LRFSRIQRLP ERMNTLTFLG NFPDTAQLLM PQLNAIIAAS MSIKSSDKLR QILEIVLAFG
     NYMNSSKRGA AYGFRLQSLD ALLEMKSTDR KQTLLHYLVK VIAEKYPQLT GFHSDLHFLD
     KAGSVSLDSV LGDVRSLQRG LELTQREFVR QDDCLVLKEF LRANSPTMDK LLADSKTAQE
     AYESVVEYFG ENPKTTSPSM FFSLFSRFTK AYKKAEQEVE QWKKEAAADT SGREEPPTPK
     SPPKARRQQM DLISELKRKQ QKEPLIYESD RDGAIEDIIT DLRNQPYIRA DTGRRSARRR
     PPGPPLPVTT DLAL
//
ID   MPP6_MOUSE              Reviewed;         553 AA.
AC   Q9JLB0; Q9JLB1; Q9WV37;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=MAGUK p55 subfamily member 6;
DE   AltName: Full=Dlgh4 protein;
DE   AltName: Full=P55T protein;
DE   AltName: Full=Protein associated with Lin-7 2;
GN   Name=Mpp6; Synonyms=Dlgh4, Pals2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
RX   MEDLINE=20219199; PubMed=10753959; DOI=10.1074/jbc.275.15.11425;
RA   Kamberov E., Makarova O., Roh M., Liu A., Karnak D., Straight S.,
RA   Margolis B.;
RT   "Molecular cloning and characterization of Pals, proteins associated
RT   with mLin-7.";
RL   J. Biol. Chem. 275:11425-11431(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
RA   Lin L., Chishti A.H.;
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INTERACTION WITH CADM1.
RX   PubMed=12826663; DOI=10.1074/jbc.M305387200;
RA   Shingai T., Ikeda W., Kakunaga S., Morimoto K., Takekuni K., Itoh S.,
RA   Satoh K., Takeuchi M., Imai T., Monden M., Takai Y.;
RT   "Implications of nectin-like molecule-
RT   2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 in cell-cell adhesion and
RT   transmembrane protein localization in epithelial cells.";
RL   J. Biol. Chem. 278:35421-35427(2003).
CC   -!- SUBUNIT: Interacts with CADM1. Interacts with the LIN7 proteins.
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Beta;
CC         IsoId=Q9JLB0-1; Sequence=Displayed;
CC       Name=Alpha;
CC         IsoId=Q9JLB0-2; Sequence=VSP_003161;
CC   -!- SIMILARITY: Belongs to the MAGUK family.
CC   -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC   -!- SIMILARITY: Contains 2 L27 domains.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF199009; AAF63790.1; -; mRNA.
DR   EMBL; AF199010; AAF63791.1; -; mRNA.
DR   EMBL; AF161181; AAD45009.1; -; mRNA.
DR   IPI; IPI00124046; -.
DR   IPI; IPI00314316; -.
DR   RefSeq; NP_001158205.1; NM_001164733.1.
DR   RefSeq; NP_001158206.1; NM_001164734.1.
DR   RefSeq; NP_064323.2; NM_019939.2.
DR   UniGene; Mm.41288; -.
DR   UniGene; Mm.463873; -.
DR   UniGene; Mm.478422; -.
DR   ProteinModelPortal; Q9JLB0; -.
DR   SMR; Q9JLB0; 2-550.
DR   STRING; Q9JLB0; -.
DR   PhosphoSite; Q9JLB0; -.
DR   PRIDE; Q9JLB0; -.
DR   Ensembl; ENSMUST00000036225; ENSMUSP00000038772; ENSMUSG00000038388.
DR   Ensembl; ENSMUST00000036236; ENSMUSP00000039314; ENSMUSG00000038388.
DR   GeneID; 56524; -.
DR   KEGG; mmu:56524; -.
DR   UCSC; uc009bwu.1; mouse.
DR   UCSC; uc009bwv.1; mouse.
DR   CTD; 56524; -.
DR   MGI; MGI:1927340; Mpp6.
DR   GeneTree; ENSGT00560000077048; -.
DR   HOGENOM; HBG446173; -.
DR   HOVERGEN; HBG001858; -.
DR   InParanoid; Q9JLB0; -.
DR   OMA; SYRDTII; -.
DR   OrthoDB; EOG4T1HM6; -.
DR   PhylomeDB; Q9JLB0; -.
DR   NextBio; 312858; -.
DR   ArrayExpress; Q9JLB0; -.
DR   Bgee; Q9JLB0; -.
DR   Genevestigator; Q9JLB0; -.
DR   GermOnline; ENSMUSG00000038388; Mus musculus.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR004172; L27.
DR   InterPro; IPR014775; L27_C.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF02828; L27; 2.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00569; L27; 2.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS51022; L27; 2.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Membrane; Phosphoprotein; Repeat; SH3 domain.
FT   CHAIN         1    553       MAGUK p55 subfamily member 6.
FT                                /FTId=PRO_0000094585.
FT   DOMAIN        1     48       L27 1.
FT   DOMAIN       49    107       L27 2.
FT   DOMAIN      129    208       PDZ.
FT   DOMAIN      228    297       SH3.
FT   DOMAIN      351    538       Guanylate kinase-like.
FT   MOD_RES     513    513       Phosphotyrosine (By similarity).
FT   VAR_SEQ     217    230       Missing (in isoform Alpha).
FT                                /FTId=VSP_003161.
FT   CONFLICT    393    394       DE -> EQ (in Ref. 2; AAD45009).
SQ   SEQUENCE   553 AA;  62631 MW;  26F3BE2445ABEDC2 CRC64;
     MQQVLENLTE LPSSTGAEEI DLIFLKGIME NPIVKSLAKA HERLEDSKLE AVSDNNLELV
     NEILEDITPL ISVDENVAEL VGILKEPHFQ SLLEAHDIVA SKCYDSPPSS PEMNIPSLNN
     QLPVDAIRIL GIHKKAGEPL GVTFRVENND LVIARILHGG MIDRQGLLHV GDIIKEVNGH
     EVGNNPKELQ ELLKNISGSV TLKILPSYRD TITPQQSYVN MERHPAHVRQ VFVKCHFDYN
     PFNDNLIPCK EAGLKFSKGE ILQIVNREDP NWWQASHVKE GGSAGLIPSQ FLEEKRKAFV
     RRDWDNSGPF CGTISNKKKK KMMYLTTRNA EFDRHEIQIY EEVAKMPPFQ RKTLVLIGAQ
     GVGRRSLKNR FIVLNPARFG TTVPFTSRKP REDEKDGQAY KFVSRSEMEA DIKAGKYLEH
     GEYEGNLYGT KIDSILEVVQ TGRTCILDVN PQALKVLRTS EFMPYVVFIA APELETLRAM
     HKAVVDAGIT TKLLTDSDLK KTVDESARIQ RAYNHYFDLI IVNDNLDKAF EKLQTAIEKL
     RMEPQWVPIS WVY
//
ID   MPP5_MOUSE              Reviewed;         675 AA.
AC   Q9JLB2;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=MAGUK p55 subfamily member 5;
DE   AltName: Full=Protein associated with Lin-7 1;
GN   Name=Mpp5; Synonyms=Pals1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF GLU-207; LEU-208; LEU-212;
RP   HIS-216; LEU-221; HIS-224; ASP-225 AND VAL-227, TISSUE SPECIFICITY,
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH LIN7C.
RC   TISSUE=Embryo;
RX   MEDLINE=20219199; PubMed=10753959; DOI=10.1074/jbc.275.15.11425;
RA   Kamberov E., Makarova O., Roh M., Liu A., Karnak D., Straight S.,
RA   Margolis B.;
RT   "Molecular cloning and characterization of Pals, proteins associated
RT   with mLin-7.";
RL   J. Biol. Chem. 275:11425-11431(2000).
RN   [2]
RP   INTERACTION WITH INADL, DOMAIN, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP   OF LEU-150 AND VAL-154.
RX   MEDLINE=21924824; PubMed=11927608; DOI=10.1083/jcb.200109010;
RA   Roh M.H., Makarova O., Liu C.-J., Shin K., Lee S., Laurinec S.,
RA   Goyal M., Wiggins R., Margolis B.;
RT   "The Maguk protein, Pals1, functions as an adapter, linking mammalian
RT   homologues of Crumbs and Discs Lost.";
RL   J. Cell Biol. 157:161-172(2002).
RN   [3]
RP   INTERACTION WITH CRB3.
RX   PubMed=12527193; DOI=10.1016/S0378111902010843;
RA   Makarova O., Roh M.H., Liu C.-J., Laurinec S., Margolis B.;
RT   "Mammalian Crumbs3 is a small transmembrane protein linked to protein
RT   associated with Lin-7 (Pals1).";
RL   Gene 302:21-29(2003).
RN   [4]
RP   INTERACTION WITH PARD6B.
RX   MEDLINE=22450976; PubMed=12545177; DOI=10.1038/ncb923;
RA   Hurd T.W., Gao L., Roh M.H., Macara I.G., Margolis B.;
RT   "Direct interaction of two polarity complexes implicated in epithelial
RT   tight junction assembly.";
RL   Nat. Cell Biol. 5:137-142(2003).
RN   [5]
RP   MUTAGENESIS OF HIS-32; ARG-33; GLU-34; ALA-36; VAL-37; ASP-38; CYS-39
RP   AND PRO-40, SUBCELLULAR LOCATION, AND INTERACTION WITH PARD6B.
RX   PubMed=15140881; DOI=10.1074/jbc.M401930200;
RA   Wang Q., Hurd T.W., Margolis B.;
RT   "Tight junction protein Par6 interacts with an evolutionarily
RT   conserved region in the amino terminus of PALS1/stardust.";
RL   J. Biol. Chem. 279:30715-30721(2004).
RN   [6]
RP   INTERACTION WITH MPDZ.
RX   PubMed=15316081; DOI=10.1242/jcs.01301;
RA   van de Pavert S.A., Kantardzhieva A., Malysheva A., Meuleman J.,
RA   Versteeg I., Levelt C., Klooster J., Geiger S., Seeliger M.W.,
RA   Rashbass P., Le Bivic A., Wijnholds J.;
RT   "Crumbs homologue 1 is required for maintenance of photoreceptor cell
RT   polarization and adhesion during light exposure.";
RL   J. Cell Sci. 117:4169-4177(2004).
RN   [7]
RP   INTERACTION WITH SC6A1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP   DOMAIN.
RX   PubMed=15234345; DOI=10.1016/j.mcn.2004.03.006;
RA   McHugh E.M., Zhu W., Milgram S., Mager S.;
RT   "The GABA transporter GAT1 and the MAGUK protein Pals1: interaction,
RT   uptake modulation, and coexpression in the brain.";
RL   Mol. Cell. Neurosci. 26:406-417(2004).
RN   [8]
RP   INTERACTION WITH EZR, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=15677456; DOI=10.1074/jbc.M411941200;
RA   Cao X., Ding X., Guo Z., Zhou R., Wang F., Long F., Wu F., Bi F.,
RA   Wang Q., Fan D., Forte J.G., Teng M., Yao X.;
RT   "PALS1 specifies the localization of Ezrin to the apical membrane of
RT   gastric parietal cells.";
RL   J. Biol. Chem. 280:13584-13592(2005).
RN   [9]
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=15558731; DOI=10.1002/cne.20367;
RA   Stoehr H., Molday L.L., Molday R.S., Weber B.H.F., Biedermann B.,
RA   Reichenbach A., Kraemer F.;
RT   "Membrane-associated guanylate kinase proteins MPP4 and MPP5 associate
RT   with Veli3 at distinct intercellular junctions of the neurosensory
RT   retina.";
RL   J. Comp. Neurol. 481:31-41(2005).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 123-180.
RX   PubMed=15241471; DOI=10.1038/sj.emboj.7600294;
RA   Li Y., Karnak D., Demeler B., Margolis B., Lavie A.;
RT   "Structural basis for L27 domain-mediated assembly of signaling and
RT   cell polarity complexes.";
RL   EMBO J. 23:2723-2733(2004).
RN   [11]
RP   STRUCTURE BY NMR OF 236-335.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the PDZ domain of PALS1 protein.";
RL   Submitted (FEB-2005) to the PDB data bank.
CC   -!- FUNCTION: May play a role in tight junctions biogenesis and in the
CC       establishment of cell polarity in epithelial cells. May modulate
CC       SC6A1/GAT1-mediated GABA uptake by stabilizing the transporter.
CC       Required for localization of EZR to the apical membrane of
CC       parietal cells and may play a role in the dynamic remodeling of
CC       the apical cytoskeleton.
CC   -!- SUBUNIT: Heterodimer with MPP1. Interacts with MPP7. Forms a
CC       complex with CRB1 and MPP4. Component of a complex whose core is
CC       composed of ARHGAP17, AMOT, MPP5/PALS1, INADL/PATJ and PARD3/PAR3
CC       (By similarity). Interacts with CRB3, EZR, INADL, LIN7C, MPDZ,
CC       PARD6B and SC6A1.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC       Endomembrane system; Peripheral membrane protein. Cell junction,
CC       tight junction. Note=Localized to the tight junctions of
CC       epithelial cells and a subset of intracellular vesicles. Localized
CC       to the Purkinje cell body and axon. Localized to apical membrane
CC       domains of the outer limiting membrane junctions in the retina.
CC       Colocalizes with MPP1 in the retina at the outer limiting membrane
CC       (OLM) (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in retina, lung, kidney, and heart.
CC       In the brain, expressed in the dentate gyrus of hippocampus,
CC       striatum and cerebellum (at protein level). Expressed in placenta,
CC       kidney, brain, heart, skeletal muscles, lung, pancreas and liver.
CC   -!- DOMAIN: The L27 domain 1 functions in targeting to the tight
CC       junctions by binding to INADL.
CC   -!- DOMAIN: The PDZ domain binds to the C-terminus of SC6A1.
CC   -!- SIMILARITY: Belongs to the MAGUK family.
CC   -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC   -!- SIMILARITY: Contains 2 L27 domains.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF199008; AAF63789.1; -; mRNA.
DR   IPI; IPI00124051; -.
DR   RefSeq; NP_062525.1; NM_019579.3.
DR   UniGene; Mm.425777; -.
DR   PDB; 1VA8; NMR; -; A=236-335.
DR   PDB; 1VF6; X-ray; 2.10 A; C/D=123-180.
DR   PDBsum; 1VA8; -.
DR   PDBsum; 1VF6; -.
DR   ProteinModelPortal; Q9JLB2; -.
DR   SMR; Q9JLB2; 121-337, 346-412, 480-667.
DR   MINT; MINT-1206544; -.
DR   STRING; Q9JLB2; -.
DR   PhosphoSite; Q9JLB2; -.
DR   PRIDE; Q9JLB2; -.
DR   Ensembl; ENSMUST00000082024; ENSMUSP00000080683; ENSMUSG00000021112.
DR   GeneID; 56217; -.
DR   KEGG; mmu:56217; -.
DR   UCSC; uc007nzh.1; mouse.
DR   CTD; 56217; -.
DR   MGI; MGI:1927339; Mpp5.
DR   eggNOG; roNOG11147; -.
DR   GeneTree; ENSGT00560000077018; -.
DR   HOGENOM; HBG446173; -.
DR   HOVERGEN; HBG001858; -.
DR   InParanoid; Q9JLB2; -.
DR   OMA; PVHQKEG; -.
DR   OrthoDB; EOG4Z36D9; -.
DR   PhylomeDB; Q9JLB2; -.
DR   NextBio; 312080; -.
DR   ArrayExpress; Q9JLB2; -.
DR   Bgee; Q9JLB2; -.
DR   Genevestigator; Q9JLB2; -.
DR   GermOnline; ENSMUSG00000021112; Mus musculus.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR004172; L27.
DR   InterPro; IPR014775; L27_C.
DR   InterPro; IPR015145; L27_N.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF02828; L27; 1.
DR   Pfam; PF09060; L27_N; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00569; L27; 2.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS51022; L27; 2.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell junction; Cell membrane; Membrane; Phosphoprotein;
KW   Repeat; SH3 domain; Tight junction.
FT   CHAIN         1    675       MAGUK p55 subfamily member 5.
FT                                /FTId=PRO_0000094581.
FT   DOMAIN      120    177       L27 1.
FT   DOMAIN      179    235       L27 2.
FT   DOMAIN      256    336       PDZ.
FT   DOMAIN      345    417       SH3.
FT   DOMAIN      479    660       Guanylate kinase-like.
FT   REGION       21    140       Interaction with PARD6B.
FT   REGION      181    243       Interaction with LIN7C.
FT   MOD_RES      25     25       Phosphoserine (By similarity).
FT   MOD_RES      53     53       Phosphoserine (By similarity).
FT   MOD_RES     243    243       Phosphotyrosine (By similarity).
FT   MUTAGEN      32     32       H->A: No effect on interaction with
FT                                PARD6B.
FT   MUTAGEN      33     33       R->A: No effect on interaction with
FT                                PARD6B.
FT   MUTAGEN      34     34       E->A: No effect on interaction with
FT                                PARD6B.
FT   MUTAGEN      36     36       A->G: No effect on interaction with
FT                                PARD6B.
FT   MUTAGEN      37     37       V->G: Prevents interaction with PARD6B.
FT                                Does not affect localization to the tight
FT                                junctions.
FT   MUTAGEN      37     37       V->I: No effect on interaction with
FT                                PARD6B.
FT   MUTAGEN      38     38       D->A: Prevents interaction with PARD6B.
FT   MUTAGEN      38     38       D->E: No effect on interaction with
FT                                PARD6B.
FT   MUTAGEN      39     39       C->A: No effect on interaction with
FT                                PARD6B.
FT   MUTAGEN      40     40       P->A: No effect on interaction with
FT                                PARD6B.
FT   MUTAGEN     150    150       L->G: No effect on PARD6B interaction.
FT                                Prevents interaction with INADL; when
FT                                associated with G-154.
FT   MUTAGEN     154    154       V->G: No effect on PARD6B interaction.
FT                                Prevents interaction with INADL; when
FT                                associated with G-150.
FT   MUTAGEN     207    207       E->Q: No effect on interaction with
FT                                LIN7C.
FT   MUTAGEN     208    208       L->G: Prevents interaction with LIN7C.
FT   MUTAGEN     212    212       L->G: Prevents interaction with LIN7C.
FT   MUTAGEN     216    216       H->N: No effect on interaction with
FT                                LIN7C.
FT   MUTAGEN     221    221       L->G: Partially prevents interaction with
FT                                LIN7C.
FT   MUTAGEN     224    224       H->N: Partially prevents interaction with
FT                                LIN7C.
FT   MUTAGEN     225    225       D->N: Prevents interaction with LIN7C.
FT   MUTAGEN     227    227       V->G: Prevents interaction with LIN7C.
FT   HELIX       123    135
FT   HELIX       141    155
FT   HELIX       157    169
FT   STRAND      247    249
FT   STRAND      255    261
FT   STRAND      269    273
FT   STRAND      275    283
FT   HELIX       288    292
FT   STRAND      300    304
FT   HELIX       314    323
FT   STRAND      326    333
SQ   SEQUENCE   675 AA;  77229 MW;  66670F919F18063B CRC64;
     MTTSYMNGHV TEESDSGIKN LDLASPEEYP KHREMAVDCP GDLGTRMMPV RRSAQLERIR
     QQQEDMRRRR EEEGKKQELD LNSSMRLKKL AQIPPKTGID NPIFDTEEGI VLESPHYAVN
     ILDVEDLFSS LKHIQHTLVD SQSQEDISLL LQLVQNRDFQ NAFKIHNAVT VHMSKASPPF
     PLIANVQDLV QEVQTVLKPV HQKEGQELTA LLNAPHIQAL LLAHDKVAEQ EMQLEPITDE
     RVYESIGHYG GETVKIVRIE KARDIPLGAT VRNEMDSVII SRIVKGGAAE KSGLLHEGDE
     VLEINGIEIR GKDVNEVFDL LSDMHGTLTF VLIPSQQIKP PPAKETVIHV KAHFDYDPSD
     DPYVPCRELG LSFQKGDILH VISQEDPNWW QAYREGDEDN QPLAGLVPGK SFQQQREAMK
     QTIEEDKEPE KSGKLWCAKK NKKKRKKVLY NANKNDDYDN EEILTYEEMS LYHQPANRKR
     PIILIGPQNC GQNELRQRLM NKEKDRFASA VPHTTRNRRD HEVAGRDYHF VSRQAFEADI
     AAGKFIEHGE FEKNLYGTSI DSVRQVINSG KICLLSLRTQ SLKTLRNSDL KPYIIFIAPP
     SQERLRALLA KEGKNPKPEE LREIIEKTRE MEQNNGHYFD TAIVNSDLDK AYQELLRLIN
     KLDTEPQWVP STWLR
//
ID   PVRL3_MOUSE             Reviewed;         549 AA.
AC   Q9JLB9; Q059N7; Q9D006; Q9JLB7; Q9JLB8;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Poliovirus receptor-related protein 3;
DE   AltName: Full=Nectin-3;
DE   AltName: CD_antigen=CD113;
DE   Flags: Precursor;
GN   Name=Pvrl3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), SUBUNIT, TISSUE
RP   SPECIFICITY, AND FUNCTION.
RX   MEDLINE=20209403; PubMed=10744716; DOI=10.1074/jbc.275.14.10291;
RA   Satoh-Horikawa K., Nakanishi H., Takahashi K., Miyahara M.,
RA   Nishimura M., Tachibana K., Mizoguchi A., Takai Y.;
RT   "Nectin-3: a new member of immunoglobulin-like cell adhesion molecules
RT   that shows homophilic and heterophilic cell-cell adhesion
RT   activities.";
RL   J. Biol. Chem. 275:10291-10299(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12121624; DOI=10.1016/S0960-9822(02)00922-3;
RA   Ozaki-Kuroda K., Nakanishi H., Ohta H., Tanaka H., Kurihara H.,
RA   Mueller S., Irie K., Ikeda W., Sakai T., Wimmer E., Nishimune Y.,
RA   Takai Y.;
RT   "Nectin couples cell-cell adhesion and the actin scaffold at
RT   heterotypic testicular junctions.";
RL   Curr. Biol. 12:1145-1150(2002).
RN   [5]
RP   FUNCTION.
RX   PubMed=12558799; DOI=10.1046/j.1365-2443.2003.00616.x;
RA   Honda T., Shimizu K., Kawakatsu T., Yasumi M., Shingai T.,
RA   Fukuhara A., Ozaki-Kuroda K., Irie K., Nakanishi H., Takai Y.;
RT   "Antagonistic and agonistic effects of an extracellular fragment of
RT   nectin on formation of E-cadherin-based cell-cell adhesion.";
RL   Genes Cells 8:51-63(2003).
RN   [6]
RP   INTERACTION WITH IGSF4.
RX   PubMed=12826663; DOI=10.1074/jbc.M305387200;
RA   Shingai T., Ikeda W., Kakunaga S., Morimoto K., Takekuni K., Itoh S.,
RA   Satoh K., Takeuchi M., Imai T., Monden M., Takai Y.;
RT   "Implications of nectin-like molecule-
RT   2/IGSF4/RA175/SgIGSF/TSLC1/SynCAM1 in cell-cell adhesion and
RT   transmembrane protein localization in epithelial cells.";
RL   J. Biol. Chem. 278:35421-35427(2003).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH PVR.
RX   PubMed=16128743; DOI=10.1111/j.1349-7006.2005.00087.x;
RA   Sato T., Irie K., Okamoto R., Ooshio T., Fujita N., Takai Y.;
RT   "Common signaling pathway is used by the trans-interaction of Necl-
RT   5/Tage4/PVR/CD155 and nectin, and of nectin and nectin during the
RT   formation of cell-cell adhesion.";
RL   Cancer Sci. 96:578-589(2005).
RN   [8]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=15728677; DOI=10.1242/dev.01697;
RA   Inagaki M., Irie K., Ishizaki H., Tanaka-Okamoto M., Morimoto K.,
RA   Inoue E., Ohtsuka T., Miyoshi J., Takai Y.;
RT   "Roles of cell-adhesion molecules nectin 1 and nectin 3 in ciliary
RT   body development.";
RL   Development 132:1525-1537(2005).
RN   [9]
RP   INTERACTION WITH IGSF4B.
RX   PubMed=15741237; DOI=10.1242/jcs.01656;
RA   Kakunaga S., Ikeda W., Itoh S., Deguchi-Tawarada M., Ohtsuka T.,
RA   Mizoguchi A., Takai Y.;
RT   "Nectin-like molecule-1/TSLL1/SynCAM3: a neural tissue-specific
RT   immunoglobulin-like cell-cell adhesion molecule localizing at non-
RT   junctional contact sites of presynaptic nerve terminals, axons and
RT   glia cell processes.";
RL   J. Cell Sci. 118:1267-1277(2005).
RN   [10]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=16300961; DOI=10.1016/j.mcn.2005.10.002;
RA   Honda T., Sakisaka T., Yamada T., Kumazawa N., Hoshino T., Kajita M.,
RA   Kayahara T., Ishizaki H., Tanaka-Okamoto M., Mizoguchi A., Manabe T.,
RA   Miyoshi J., Takai Y.;
RT   "Involvement of nectins in the formation of puncta adherentia
RT   junctions and the mossy fiber trajectory in the mouse hippocampus.";
RL   Mol. Cell. Neurosci. 31:315-325(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Plays a role in cell-cell adhesion through heterophilic
CC       trans-interactions with nectins-like or other nectins, such as
CC       trans-interaction with PVRL2/nectin-2 at Sertoli-spermatid
CC       junctions. Trans-interaction with PVR induces activation of CDC42
CC       and RAC small G proteins through common signaling molecules such
CC       as SRC and RAP1. Also involved in the formation of cell-cell
CC       junctions, including adherens junctions and synapses. Induces
CC       endocytosis-mediated down-regulation of PVR from the cell surface,
CC       resulting in reduction of cell movement and proliferation. Plays a
CC       role in the morphology of the ciliary body.
CC   -!- SUBUNIT: Cis- and trans-homodimer. Can form trans-heterodimers
CC       with PVRL1/nectin-1, PVRL2/nectin-2, PVR, IGSF4B/Necl-1 and with
CC       IGSF4. Interacts with MLLT4/afadin. Binds with low affinity to
CC       TIGIT.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Nectin-3 alpha;
CC         IsoId=Q9JLB9-1; Sequence=Displayed;
CC       Name=2; Synonyms=Nectin-3 beta;
CC         IsoId=Q9JLB9-2; Sequence=VSP_017437, VSP_017440;
CC       Name=3; Synonyms=Nectin-3 gamma;
CC         IsoId=Q9JLB9-3; Sequence=VSP_017438, VSP_017439;
CC   -!- TISSUE SPECIFICITY: Ubiquitous with high expression in testes.
CC       Localized in spermatids at Sertoli-spermatid junctions. Expressed
CC       in ovarian granulosa cells, but only faintly expressed after
CC       ovulation.
CC   -!- DISRUPTION PHENOTYPE: Mice show an ocular phenotype,
CC       microphthalmia, accompanied by a separation of the contact between
CC       the pigment and non-pigment cell layers of the ciliary epithelia.
CC       Male mice exhibits infertility, suggesting a role in
CC       spermatogenesis. In the hippocampus, the formation and the number
CC       of adherens junctions at the synapses is impaired, and the
CC       trajectory of mossy fiber is abnormal.
CC   -!- SIMILARITY: Belongs to the nectin family.
CC   -!- SIMILARITY: Contains 2 Ig-like C2-type (immunoglobulin-like)
CC       domains.
CC   -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like)
CC       domain.
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DR   EMBL; AF195833; AAF63685.1; -; mRNA.
DR   EMBL; AF195834; AAF63686.1; -; mRNA.
DR   EMBL; AF195835; AAF63687.1; -; mRNA.
DR   EMBL; AK011949; BAB27933.1; -; mRNA.
DR   EMBL; BC125588; AAI25589.1; -; mRNA.
DR   EMBL; BC132187; AAI32188.1; -; mRNA.
DR   IPI; IPI00130525; -.
DR   IPI; IPI00227826; -.
DR   IPI; IPI00471187; -.
DR   RefSeq; NP_067470.1; NM_021495.3.
DR   RefSeq; NP_067471.1; NM_021496.2.
DR   RefSeq; NP_067472.1; NM_021497.2.
DR   UniGene; Mm.328072; -.
DR   UniGene; Mm.440435; -.
DR   ProteinModelPortal; Q9JLB9; -.
DR   SMR; Q9JLB9; 62-361.
DR   MINT; MINT-254672; -.
DR   STRING; Q9JLB9; -.
DR   PhosphoSite; Q9JLB9; -.
DR   PRIDE; Q9JLB9; -.
DR   Ensembl; ENSMUST00000023334; ENSMUSP00000023334; ENSMUSG00000022656.
DR   Ensembl; ENSMUST00000023335; ENSMUSP00000023335; ENSMUSG00000022656.
DR   Ensembl; ENSMUST00000096052; ENSMUSP00000093757; ENSMUSG00000022656.
DR   GeneID; 58998; -.
DR   KEGG; mmu:58998; -.
DR   UCSC; uc007zji.1; mouse.
DR   UCSC; uc007zjj.1; mouse.
DR   UCSC; uc007zjk.1; mouse.
DR   CTD; 58998; -.
DR   MGI; MGI:1930171; Pvrl3.
DR   GeneTree; ENSGT00600000084002; -.
DR   HOGENOM; HBG447380; -.
DR   HOVERGEN; HBG082234; -.
DR   InParanoid; Q9JLB9; -.
DR   OMA; IDLPPTH; -.
DR   OrthoDB; EOG4X6C8C; -.
DR   PhylomeDB; Q9JLB9; -.
DR   NextBio; 314506; -.
DR   ArrayExpress; Q9JLB9; -.
DR   Bgee; Q9JLB9; -.
DR   CleanEx; MM_PVRL3; -.
DR   Genevestigator; Q9JLB9; -.
DR   GermOnline; ENSMUSG00000022656; Mus musculus.
DR   GO; GO:0043296; C:apical junction complex; IDA:MGI.
DR   GO; GO:0005913; C:cell-cell adherens junction; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:HGNC.
DR   GO; GO:0009566; P:fertilization; IMP:MGI.
DR   GO; GO:0007156; P:homophilic cell adhesion; IDA:HGNC.
DR   GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
DR   GO; GO:0060042; P:retina morphogenesis in camera-type eye; IMP:MGI.
DR   InterPro; IPR013162; CD80_C2-set.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 4.
DR   Pfam; PF08205; C2-set_2; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 1.
DR   PROSITE; PS50835; IG_LIKE; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW   Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     57       Potential.
FT   CHAIN        58    549       Poliovirus receptor-related protein 3.
FT                                /FTId=PRO_0000226373.
FT   TOPO_DOM     58    404       Extracellular (Potential).
FT   TRANSMEM    405    425       Helical; (Potential).
FT   TOPO_DOM    426    549       Cytoplasmic (Potential).
FT   DOMAIN       58    165       Ig-like V-type.
FT   DOMAIN      170    258       Ig-like C2-type 1.
FT   DOMAIN      269    354       Ig-like C2-type 2.
FT   MOD_RES     529    529       Phosphoserine.
FT   CARBOHYD     73     73       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     83     83       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    125    125       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    186    186       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    222    222       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    331    331       N-linked (GlcNAc...) (Potential).
FT   DISULFID     78    148       By similarity.
FT   DISULFID    193    246       By similarity.
FT   DISULFID    291    338       By similarity.
FT   VAR_SEQ     358    510       PPTTTTLQPTVQWHSSPADVQDIATEHKKLPFPLSTLATLK
FT                                DDTIGTIIASVVGGALFLVLVSILAGVFCYRRRRTFRGDYF
FT                                AKNYIPPSDMQKESQIDVLHQDELDSYPDSVKKENKNPVNN
FT                                LIRKDYLEEPEKTQWNNVENLTRFERPMDY -> IPLTQTS
FT                                SIAVAGAVIGAVLALFIITVFVTVLLTPRKKRPSYLDKVID
FT                                LPPTHKPPPVYEERIPSLPQKDLLGQTEHLPLQTQFKEKGA
FT                                GGLQPSNGPISRRFDYEDESTMQEDGTQRMCPLYSQMCHQD
FT                                RSPRQHHPRNPERLYINPREHYV (in isoform 2).
FT                                /FTId=VSP_017437.
FT   VAR_SEQ     358    438       PPTTTTLQPTVQWHSSPADVQDIATEHKKLPFPLSTLATLK
FT                                DDTIGTIIASVVGGALFLVLVSILAGVFCYRRRRTFRGDY
FT                                -> IPLTQTSSIAVAGAVIGAVLALFIITVFVTVLLTPRKK
FT                                RPSYLDKVIDLPPTHKPPPVYEERIPSLPQKDLLGQVRALE
FT                                DT (in isoform 3).
FT                                /FTId=VSP_017438.
FT   VAR_SEQ     439    549       Missing (in isoform 3).
FT                                /FTId=VSP_017439.
FT   VAR_SEQ     511    549       Missing (in isoform 2).
FT                                /FTId=VSP_017440.
FT   CONFLICT    181    181       L -> S (in Ref. 2; BAB27933).
FT   CONFLICT    195    196       AA -> SS (in Ref. 2; BAB27933).
FT   CONFLICT    213    221       MESSTTSFP -> REFSTISFL (in Ref. 2;
FT                                BAB27933).
FT   CONFLICT    232    232       K -> E (in Ref. 2; BAB27933).
SQ   SEQUENCE   549 AA;  60583 MW;  5492C9ABB472F185 CRC64;
     MARTPGPAPL CPGGGKAQLS SAFPPAAGLL LPAPTPPPLL LLLIPLLLFS RLCGALAGSI
     IVEPHVTAVW GKNVSLKCLI EVNETITQIS WEKIHGKSTQ TVAVHHPQYG FSVQGDYQGR
     VLFKNYSLND ATITLHNIGF SDSGKYICKA VTFPLGNAQS STTVTVLVEP TVSLIKGPDS
     LIDGGNETVA AVCVAATGKP VAQIDWEGDL GEMESSTTSF PNETATIVSQ YKLFPTRFAR
     GRRITCVVKH PALEKDIRYS FILDIQYAPE VSVTGYDGNW FVGRKGVNLK CNADANPPPF
     KSVWSRLDGQ WPDGLLASDN TLHFVHPLTV NYSGVYVCKV SNSLGQRSDQ KVIYISDPPT
     TTTLQPTVQW HSSPADVQDI ATEHKKLPFP LSTLATLKDD TIGTIIASVV GGALFLVLVS
     ILAGVFCYRR RRTFRGDYFA KNYIPPSDMQ KESQIDVLHQ DELDSYPDSV KKENKNPVNN
     LIRKDYLEEP EKTQWNNVEN LTRFERPMDY YEDLKMGMKF VSDERYNESE DGLVSHVDGS
     VISRREWYV
//
ID   SACS_MOUSE              Reviewed;        4582 AA.
AC   Q9JLC8; Q3TUF2; Q6A007; Q8BQT3; Q8C764; Q8CAJ4;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   08-FEB-2011, entry version 72.
DE   RecName: Full=Sacsin;
DE   AltName: Full=DnaJ homolog subfamily C member 29;
DE            Short=DNAJC29;
GN   Name=Sacs; Synonyms=Kiaa0730;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=20120709; PubMed=10655055; DOI=10.1038/72769;
RA   Engert J.C., Berube P., Mercier J., Dore C., Lepage P., Ge B.,
RA   Bouchard J.-P., Mathieu J., Melancon S.B., Schalling M., Lander E.S.,
RA   Morgan K., Hudson T.J., Richter A.;
RT   "ARSACS, a spastic ataxia common in northeastern Quebec, is caused by
RT   mutations in a new gene encoding an 11.5-kb ORF.";
RL   Nat. Genet. 24:120-125(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3559-4582.
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1471 (ISOFORM 2),
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-768 (ISOFORM 1), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-178 (ISOFORM 3).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Corpora quadrigemina, Head, Hypothalamus, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4265, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=19208651; DOI=10.1093/hmg/ddp067;
RA   Parfitt D.A., Michael G.J., Vermeulen E.G., Prodromou N.V., Webb T.R.,
RA   Gallo J.M., Cheetham M.E., Nicoll W.S., Blatch G.L., Chapple J.P.;
RT   "The ataxia protein sacsin is a functional co-chaperone that protects
RT   against polyglutamine-expanded ataxin-1.";
RL   Hum. Mol. Genet. 18:1556-1565(2009).
CC   -!- FUNCTION: Co-chaperone which acts as a regulator of the Hsp70
CC       chaperone machinery and may be involved in the processing of other
CC       ataxia-linked proteins (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC       Note=Predominantly cytoplasmic, a small portion is present in the
CC       nucleus and also shows a partial mitochondrial overlap with the
CC       mitochondrial marker Hsp60 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9JLC8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9JLC8-2; Sequence=VSP_022326;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q9JLC8-3; Sequence=VSP_022327;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Brain (at protein level).
CC   -!- DOMAIN: The ubiquitin-like domain mediates interaction with the
CC       proteasome (By similarity).
CC   -!- DOMAIN: The J domain is functional and is able to stimulate E.coli
CC       dnaK ATPase activity (By similarity).
CC   -!- SIMILARITY: Contains 1 HEPN domain.
CC   -!- SIMILARITY: Contains 1 J domain.
CC   -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC32757.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF193557; AAF31263.1; -; Genomic_DNA.
DR   EMBL; AC124555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC138718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK173011; BAD32289.1; -; mRNA.
DR   EMBL; AK038655; BAC30083.1; -; mRNA.
DR   EMBL; AK046501; BAC32757.1; ALT_INIT; mRNA.
DR   EMBL; AK052467; BAC35006.1; -; mRNA.
DR   EMBL; AK160797; BAE36019.1; -; mRNA.
DR   IPI; IPI00124120; -.
DR   IPI; IPI00816906; -.
DR   IPI; IPI00816925; -.
DR   RefSeq; NP_766397.2; NM_172809.3.
DR   UniGene; Mm.440703; -.
DR   UniGene; Mm.446687; -.
DR   ProteinModelPortal; Q9JLC8; -.
DR   SMR; Q9JLC8; 99-209, 4309-4383, 4448-4578.
DR   STRING; Q9JLC8; -.
DR   PhosphoSite; Q9JLC8; -.
DR   PRIDE; Q9JLC8; -.
DR   Ensembl; ENSMUST00000074447; ENSMUSP00000074047; ENSMUSG00000048279.
DR   Ensembl; ENSMUST00000100499; ENSMUSP00000098068; ENSMUSG00000048279.
DR   Ensembl; ENSMUST00000119943; ENSMUSP00000113377; ENSMUSG00000048279.
DR   GeneID; 50720; -.
DR   KEGG; mmu:50720; -.
DR   CTD; 50720; -.
DR   MGI; MGI:1354724; Sacs.
DR   eggNOG; roNOG11070; -.
DR   GeneTree; ENSGT00390000016695; -.
DR   HOGENOM; HBG444260; -.
DR   HOVERGEN; HBG093399; -.
DR   InParanoid; Q9JLC8; -.
DR   NextBio; 307569; -.
DR   ArrayExpress; Q9JLC8; -.
DR   Bgee; Q9JLC8; -.
DR   CleanEx; MM_SACS; -.
DR   Genevestigator; Q9JLC8; -.
DR   GermOnline; ENSMUSG00000048279; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   InterPro; IPR003594; ATPase-like_ATP-bd.
DR   InterPro; IPR001623; DnaJ_N.
DR   InterPro; IPR007842; HEPN.
DR   Gene3D; G3DSA:3.30.565.10; ATP_bd_ATPase; 4.
DR   Gene3D; G3DSA:1.10.287.110; DnaJ_N; 1.
DR   Pfam; PF05168; HEPN; 1.
DR   SMART; SM00748; HEPN; 1.
DR   SUPFAM; SSF55874; ATP_bd_ATPase; 3.
DR   SUPFAM; SSF46565; DnaJ_N; 1.
DR   PROSITE; PS00636; DNAJ_1; FALSE_NEG.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS50910; HEPN; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; FALSE_NEG.
DR   PROSITE; PS50053; UBIQUITIN_2; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Chaperone; Cytoplasm;
KW   Phosphoprotein.
FT   CHAIN         1   4582       Sacsin.
FT                                /FTId=PRO_0000097564.
FT   DOMAIN        7     84       Ubiquitin-like.
FT   DOMAIN     4309   4396       J.
FT   DOMAIN     4454   4570       HEPN.
FT   MOD_RES     945    945       N6-acetyllysine (By similarity).
FT   MOD_RES    4265   4265       Phosphothreonine.
FT   MOD_RES    4266   4266       Phosphoserine (By similarity).
FT   MOD_RES    4336   4336       Phosphotyrosine (By similarity).
FT   VAR_SEQ       1    752       Missing (in isoform 2).
FT                                /FTId=VSP_022326.
FT   VAR_SEQ       1      6       METKFQ -> MGD (in isoform 3).
FT                                /FTId=VSP_022327.
FT   CONFLICT      4      6       KFQ -> EET (in Ref. 4; BAE36019).
FT   CONFLICT     58     58       V -> I (in Ref. 4; BAC35006/BAE36019).
FT   CONFLICT    224    224       P -> H (in Ref. 4; BAC32757).
FT   CONFLICT    731    744       GRPCTQLQLLNPER -> AQQLLWGYSGRITD (in Ref.
FT                                4; BAC32757).
FT   CONFLICT    732    768       RPCTQLQLLNPERFARLIKEVMNTFWPGRELVVQWYP ->
FT                                YVKHDLLTTLERISLAYSGNKNSDSPSRRSPSAVTCK (in
FT                                Ref. 4; BAE36019).
SQ   SEQUENCE   4582 AA;  520685 MW;  2409B6DA64905B48 CRC64;
     METKFQRWVR VTVLRGCVGC RTVAVPATAT GRDLKERIFA ETSFPVAEQR LWRGDREVPD
     WIKIGDLTSK TCHLFVNLQS KGLKGGGRFG QTTPPLVDFL KDILRRYPEG GQILKELIQN
     AEDAGATEVK FLYDETQYGT ETLWSKDMAQ YQGSALYVYN NAVFTPEDWH GIQEIARSRK
     KDDPLKVGRF GIGFNSVYHI TDVPCIFSGD QIGMLDPHQT LFGPHESGQC WNLKDDIKEI
     NELPDQFAPF IGVFGSTKET FTNGSFPGTF FRFPLRLQPS QLSSNLYTKQ KVLELFDSFR
     ADADTVLLFL KSVQAVSLHV READGTEKLV FRVTASENKA LKHERPNSIK ILGTAISNYC
     KKIPSNSVTC VTYHINIVLE DESTKDAQKT SWLVCNSVGG RGISSKLDSL ADELKFVPII
     GLAMPLSGKD EENGAISDFS GKAFCFLPLP PGEESRTGLP VHISGFFGLT DNRRSIKWRE
     LDQWRDPAAL WNEYLIVNVV PKTYATLILD SIKRLETEKS SDFPLSVDTI YKLWPEASKV
     KAHWHPVLGP LFSELFQHAV IYSIGGEWVK LEQVHFSELD GSLESTRSVL NYLQSSGKQI
     AKVPGNLAAA VQLSAASATS SASPVRKVTP AWVRQVLRKC AHLGSAEEKL HLLEFVLSDQ
     AYSELLGLEL LPLQSGAFVP FSSSVSDQDV VYITSEEFPR SLFPGLEARL ILENLKPHLL
     AALKEAAQTR GRPCTQLQLL NPERFARLIK EVMNTFWPGR ELVVQWYPFS EDKRHPSLSW
     LKMVWKNLYI HFSEDLTLFD EMPLIPRTLL NEDQTCVELI RLRIPSVVIL DDETEAQLPE
     FLADIVQKLG GIVLKRLDTS IQHPLVKKYI HSPLPSAILQ IMEKIPLQKL CNQIASLLPT
     HKDALRKFLA SLTDTSEKEK RIIQELTIFK RINHSSDQGI SSYTKLKGCK VLDHTAKLPT
     DLRLSVSVID SSDEATIRLA NMLKIEKLKT TSCLKFVLKD IGNAFYTQEE VTQLMLWILE
     NLSSLKNENS NVLDWLMPLK FIHMSQGHVV AAGDLFDPDI EVLRDLFYNE EEACFPPTIF
     TSPDILHSLR QIGLKNESSL KEKDVVQVAR KIEALQVSSC QNQDVLMKKA KTLLLVLNKN
     QTLLQSSEGK MALKKIKWVP ACKERPPNYP GSLVWKGDLC NLCAPPDMCD AAHAVLVGSS
     LPLVESVHVN LEQALSIFTK PTINAVLKHF KTVVDWYTSK TFSDEDYYQF QHILLEIYGF
     MHDHLSEGKD SFKALKFPWV WTGKNFCPLA QAVIKPTHDL DLQPYLYNVP KTMAKFHQLF
     KACGSIEELT SDHISMVIQK VYLKSDQELS EEESKQNLHL MLNIMRWLYS NQIPASPNTP
     VPIYHSRNPS KLVMKPIHEC CYCDIKVDDL NDLLEDSVEP IILVHEDIPM KTAEWLKVPC
     LSTRLINPEN MGFEQSGQRE PLTVRIKNIL EEYPSVSDIF KELLQNADDA NATECSFMID
     MRRNMDIREN LLDPGMAACH GPALWSFNNS EFSDSDFLNI TRLGESLKRG EVDKVGKFGL
     GFNSVYHITD IPIIMSREFM IMFDPNINHI SKHIKDRSNP GIKINWSKQQ KRLRKFPNQF
     KPFIDVFGCQ LPLAVEAPYS YNGTLFRLSF RTQQEAKVSE VSSTCYNTAD IYSLVDEFSL
     CGHRLIIFTQ SVNSMYLKYL KIEETNPSLA QDTIIIKKKV CPSKALNAPV LSVLKEAAKL
     MKTCSSSNKK LPTDVPKSSC ILQITVEEFH HVFRRIADLQ SPLFRGPDDD PATLFEMAKS
     GQSKKPSDEL PQKTVDCTTW LICTCMDTGE ALKFSLNESG RRLGLVPCGA VGVLLHETQE
     QKWTVKPHIG EVFCYLPLRI KTGLPIHING CFAVTSNRKE IWKTDTKGRW NTTFMRHVIV
     KAYLQALSVL RDLAIGGELT DYTYYAVWPD PDLVHDDFSV ICKGFYEDIA HGKGKELTRV
     FSDGSMWVSM KNVRFLDDSI LQRKDVGSAA FKIFLKYLKK TGSKNLCAVE LPSSVKAGFE
     EAGCKQILLE NTFSEKQFFS EVFFPNIQEI EAELRDPLMN FVLNEKLDEF SGILRVTPCV
     PCSLEGHPLV LPSRLIHPEG RVAKLFDTKD GRFPYGSTQD YLNPIILIKL VQLGMAKDDI
     LWDDMLERAE SVAEINKSDH AAACLRSSIL LSLIDEKLKI KDPRAKDFAA KYQTIPFLPF
     LTKPAGFSLE WKGNSFKPET MFAATDIYTA EYQDIVCLLQ PILNENSHSF RGCGSVSLAV
     KEFLGLLKKP TVDLVINQLK QVAKSVDDGI TLYQENITNA CYKYLHEAVL QNEMAKATII
     EKLKPFCFIL VENVYVESEK VSFHLNFEAA PYLYQLPNKY KNNFRELFES VGVRQSFTVE
     DFALVLESID QERGKKQITE ENFQLCRRII SEGIWSLIRE KRQEFCEKNY GKILLPDTNL
     LLLPAKSLCY NDCPWIKVKD STVKYCHADI PREVAVKLGA IPKRHKALER YASNICFTAL
     GTEFGQKEKL TSRIKSILNA YPSEKEMLKE LLQNADDAKA TEICFVFDPR QHPVDRIFDD
     KWAPLQGPAL CVYNNQPFTE DDVRGIQNLG KGTKEGNPCK TGHYGIGFNS VYHITDCPSF
     ISGNDILGIF DPHARYAPGA TSVSPGRMFR DLDADFRTQF SDVLDLYLGN HFKLDNCTMF
     RFPLRNAEMA QVSEISSVPS SDRMVQNLLD KLRSDGAELL MFLNHMEKIS ICEIDKATGG
     LNVLYSVKGK ITDGDRLKRK QFHASVIDSV TKKRQLKDIP VQQITYTMDT EDSEGNLTTW
     LICNRSGFSS MEKVSKSVIS AHKNQDITLF PRGGVAACIT HNYKKPHRAF CFLPLSLETG
     LPFHVNGHFA LDSARRNLWR DDNGVGVRSD WNNSLMTALI APAYVELLIQ LKKRYFPGSD
     PTLSVLQNTP IHVVKDTLKK FLSFFPVNRL DLQPDLYCLV KALYSCIHED MKRLLPVVRA
     PNIDGSDLHS AVIITWINMS TSNKTRPFFD NLLQDELQHL KNADYNITTR KTVAENVYRL
     KHLLLEIGFN LVYNCDETAN LYHCLVDADI PVSYVTPADV RSFLMTFSSP DTNCHIGKLP
     CRLQQTNLKL FHSLKLLVDY CFKDAEESEF EVEGLPLLIT LDSVLQIFDG KRPKFLTTYH
     ELIPSRKDLF MNTLYLKYSS VLLNCKVAKV FDISSFADLL SSVLPREYKT KNCAKWKDNF
     ASESWLKNAW HFISESVSVT DDQEEPKPAF DVIVDILKDW ALLPGTKFTV STSQLVVPEG
     DVLIPLSLMH IAVFPNAQSD KVFHALMKAG CIQLALNKIC SKDSALVPLL SCHTANIDSP
     ASILKAVHYM VQTSTFRTEK LMENDFEALL MYFNCNLSHL MSQDDIKILK SLPCYKSISG
     RYMSIAKFGT CYVLTKSIPS AEVEKWTQSS SSAFLEEKVH LKELYEVLGC VPVDDLEVYL
     KHLLPKIENL SYDAKLEHLI YLKNRLASIE EPSEIKEQLF EKLESLLIIH DANNRLKQAK
     HFYDRTVRVF EVMLPEKLFI PKEFFKKLEQ VIKPKNQAAF MTSWVEFLRN IGLKYALSQQ
     QLLQFAKEIS VRANTENWSK ETLQSTVDIL LHHIFQERMD LLSGNFLKEL SLIPFLCPER
     APAEYIRFHP QYQEVNGTLP LIKFNGAQVN PKFKQCDVLQ LLWTSCPILP EKATPLSIKE
     QEGSDLAPQE QLEQVLNMLN VNLDPPLDKV INNCRNICNI TTLDEEMVKT RAKVLRSIYE
     FLSAEKREFR FQLRGVAFVM VEDGWKLLKP EEVVINLEYE ADFKPYLYKL PLELGTFHQL
     FKHLGTEDII STKQYVEVLS RIFKSSEGKQ LDPNEMRTVK RVVSGLFKSL QNDSVKVRSD
     LENARDLALY LPSQDGKLVK SSILVFDDAP HYKSRIQGNI GVQMLVDLSQ CYLGKDHGFH
     TKLIMLFPQK LRPRLLSSIL EEQLDEETPK VCQFGALCSL QGRLQLLLSS EQFITGLIRI
     MKHENDNAFL ANEEKAIRLC KALREGLKVS CFEKLQTTLR VKGFNPIPHS RSETFAFLKR
     FGNAVILLYI QHSDSKDINF LLALAMTLKS ATDNLISDTS YLIAMLGCND IYRISEKLDS
     LGVKYDSSEP SKLELPMPGT PIPAEIHYTL LMDPMNVFYP GEYVGYLVDA EGGDIYGSYQ
     PTYTYAIIVQ EVEREDADNT SFLGKIYQID IGYSEYKIVS SLDLYKFSRP DESSQNRDSA
     PTTPTSPTEF LTPGLRSIPP LFSGKESHKS PSTKHHSPRK LKVNALPEIL KEVTSVVEQA
     WKLPESERKK IIRRLYLKWH PDKNPENHDI ANEVFKHLQN EINRLEKQAF LDQNADRASR
     RTFSTSASRF QSDKYSFQRF YTSWNQEATS HKSERQQQSK EKCPPSAGQT YSQRFFVPPT
     FKSVGNPVEA RRWLRQARAN FSAARNDLHK NANEWVCFKC YLSTKLALIA ADYAVRGKSD
     KDVKPTALAQ KIEEYSQQLE GLTNDVHTLE AYGVDSLKTR YPDLLPFPQI PNDRFTSEVA
     MRVMECTACI IIKLENFIQQ KV
//
ID   ZMYM3_MOUSE             Reviewed;        1370 AA.
AC   Q9JLM4; Q80U17;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Zinc finger MYM-type protein 3;
DE   AltName: Full=DXHXS6673E protein;
DE   AltName: Full=Zinc finger protein 261;
GN   Name=Zmym3; Synonyms=Kiaa0385, Zfp261, Znf261;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=20130120; PubMed=10662551; DOI=10.1006/geno.1999.6027;
RA   Scheer M.P., van der Maarel S.M., Kuebart S., Schulz A., Wirth J.,
RA   Schweiger S., Ropers H.-H., Nothwang H.G.;
RT   "DXS6673E encodes a predominantly nuclear protein, and its mouse
RT   ortholog DXHXS6673E is alternatively spliced in a developmental- and
RT   tissue-specific manner.";
RL   Genomics 63:123-132(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
CC   -!- SUBUNIT: May be a component of a BHC histone deacetylase complex
CC       that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST,
CC       PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed in all embryonic stages
CC       and adult tissues.
CC   -!- SIMILARITY: Contains 9 MYM-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65550.3; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF156605; AAF37800.1; -; mRNA.
DR   EMBL; AK122268; BAC65550.3; ALT_INIT; Transcribed_RNA.
DR   IPI; IPI00124492; -.
DR   RefSeq; NP_062805.1; NM_019831.3.
DR   UniGene; Mm.23458; -.
DR   ProteinModelPortal; Q9JLM4; -.
DR   SMR; Q9JLM4; 310-342.
DR   PhosphoSite; Q9JLM4; -.
DR   PRIDE; Q9JLM4; -.
DR   Ensembl; ENSMUST00000063577; ENSMUSP00000068197; ENSMUSG00000031310.
DR   GeneID; 56364; -.
DR   KEGG; mmu:56364; -.
DR   UCSC; uc009txl.1; mouse.
DR   CTD; 56364; -.
DR   MGI; MGI:1927231; Zmym3.
DR   GeneTree; ENSGT00550000074408; -.
DR   HOGENOM; HBG716329; -.
DR   HOVERGEN; HBG057545; -.
DR   InParanoid; Q9JLM4; -.
DR   OMA; VQKRSER; -.
DR   OrthoDB; EOG44MXR5; -.
DR   PhylomeDB; Q9JLM4; -.
DR   NextBio; 312398; -.
DR   ArrayExpress; Q9JLM4; -.
DR   Bgee; Q9JLM4; -.
DR   CleanEx; MM_ZMYM3; -.
DR   Genevestigator; Q9JLM4; -.
DR   GermOnline; ENSMUSG00000031310; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR021893; DUF3504.
DR   InterPro; IPR011017; TRASH.
DR   InterPro; IPR010507; Znf_MYM.
DR   Pfam; PF12012; DUF3504; 1.
DR   Pfam; PF06467; zf-FCS; 10.
DR   SMART; SM00746; TRASH; 10.
PE   2: Evidence at transcript level;
KW   Acetylation; Metal-binding; Nucleus; Phosphoprotein; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1370       Zinc finger MYM-type protein 3.
FT                                /FTId=PRO_0000191379.
FT   ZN_FING     334    368       MYM-type 1.
FT   ZN_FING     380    424       MYM-type 2.
FT   ZN_FING     431    466       MYM-type 3.
FT   ZN_FING     479    513       MYM-type 4.
FT   ZN_FING     523    561       MYM-type 5.
FT   ZN_FING     569    606       MYM-type 6.
FT   ZN_FING     614    648       MYM-type 7.
FT   ZN_FING     655    694       MYM-type 8.
FT   ZN_FING     701    735       MYM-type 9.
FT   MOD_RES     265    265       Phosphoserine (By similarity).
FT   MOD_RES     269    269       Phosphoserine (By similarity).
FT   MOD_RES     647    647       N6-acetyllysine (By similarity).
FT   MOD_RES     818    818       Phosphothreonine (By similarity).
FT   MOD_RES     827    827       Phosphothreonine (By similarity).
FT   CONFLICT    238    239       Missing (in Ref. 2; BAC65550).
FT   CONFLICT    493    495       KNT -> VGP (in Ref. 2; BAC65550).
FT   CONFLICT    719    735       AARCHACKRQGKLLETI -> VRRVNRAERRQQGDELW
FT                                (in Ref. 2; BAC65550).
SQ   SEQUENCE   1370 AA;  152879 MW;  E9270E68366E46F1 CRC64;
     MDPSDFPSPF DPLTLPEKPL AGDLPVDMEF GEDLLESQTA PSRGWAPPGP SPSSGALDLL
     DTPSGLEKDP GGVLDGATEL LGLGGLLYKA PSPPEVDHGP EGTLAWDSGE QTLEPGPGCQ
     TPEVMPPDPG AGASPPSPEG LLEPLAPDSP IILESPHIEE EIPPLATRRR GSPGQEEEHT
     QGQPQSPNAP PSPSVGETLG DGINSSQSKP GVCTPTAHPS LPGDGLTGKE IEKPPERVQK
     RSERVRRAEP PKPEVVDSTE SIPVSDEDSD AMVDDPNDED FVPFRPRRSP RMSLRSSMAQ
     RAGRSSMGTK MSCAHCRTPL QKGQTAYQRK GLPQLFCSSS CLTTYSKKPL GRKTCTFCKK
     EIWNTKDSVV VQTGPGGSFH EFCTSVCLSL YEAQQQRPIP QSGDPADATR CSICQKTGEV
     LHEVSNGSVV HRLCSDSCFS KFRANKGLKT NCCDQCGAYI YARPGGLGPE LLFHDGQQKR
     FCNTTCLGAY KKKNTRVYPC VWCKTLCKNF EMLSHVDRNG KTSLFCSLCC TTSYKVKQAG
     LTGPPRPCSF CRRSLSDPCY YNKVDRTVYQ FCSPSCWTKF QHTSPEGGIH LSCHYCHSLF
     SGKPEVLEWQ DQVFQFCCRD CCEDFKRLRG VVSQCEHCRQ EKLLHEKLRF SGVEKSFCSE
     GCVLLYKQDF TKKLGLCCIT CTYCSQTCQR GVTEQLDGST WDFCSEDCKT KYLLWYCKAA
     RCHACKRQGK LLETIHWRGQ IRHFCNQQCL LRFYSQQNQP NLDTQSGPES LLNSQSSESK
     PQTPSQTKVE NNHTVRTPDE NGNLGKTPVK RATPSVPTPP PPPPPATPRK NKAAMCKPLM
     QNRGVSCKAE MKSKGSQTEE WKPQVIVLPI PVPIFVPVPM HLYCQKVPVP FSMPIPVPVP
     MFLPTTLEST EKIVETIEEL KVKIPSNPLE ADILAMAEMI AEAEELDKAS SDLCDLVSNQ
     SAEGLLEDCD LFGTARDDVL AMAVKMANVL DEPGQDLEAD FPKNPLDINP SVDFLFDCGL
     VGPEDVSTEQ DLPRAMRKGQ KRLMLSESCS RDSLSSQPSC TGLNYSYGVN AWKCWVQSKY
     ANGETSKGDE LRFGPKPMRI KEDILACSAA ELNYGLAQFV REITRPNGER YEPDSIYYLC
     LGIQQYLLEN NRMVNIFTDL YYLTFVQELN KSLSTWQPTL LPNNTVFSRV EEEHLWECKQ
     LGVYSPFVLL NTLMFFNTKF FGLQTAEEHM QLSFTNVVRQ SRKCTTPRGT TKVVSIRYYA
     PVRQRKGRDT GPGKRKREDE TILEQRENRM NPLRCPVKFY EFYLSKCPES LRTRNDVFYL
     QPERSCIAES PLWYSVIPMD RSMLESMLNR ILAVREIYEE LGRPGEEDLD
//
ID   DCLK1_MOUSE             Reviewed;         756 AA.
AC   Q9JLM8; Q6P207;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 106.
DE   RecName: Full=Serine/threonine-protein kinase DCLK1;
DE            EC=2.7.11.1;
DE   AltName: Full=Doublecortin-like and CAM kinase-like 1;
DE   AltName: Full=Doublecortin-like kinase 1;
GN   Name=Dclk1; Synonyms=Dcamkl1, Dclk;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM1).
RC   TISSUE=Brain;
RX   MEDLINE=20004649; PubMed=10533048;
RX   DOI=10.1002/(SICI)1097-4547(19991115)58:4<567::AID-JNR9>3.3.CO;2-K;
RA   Burgess H.A., Martinez S., Reiner O.;
RT   "KIAA0369, doublecortin-like kinase, is expressed during brain
RT   development.";
RL   J. Neurosci. Res. 58:567-575(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305; SER-307; SER-738
RP   AND SER-742, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364 AND SER-392, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-509 AND TYR-536, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; SER-332 AND
RP   THR-336, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-36, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-330; SER-332 AND
RP   SER-337, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Probable kinase that may be involved in a calcium-
CC       signaling pathway controlling neuronal migration in the developing
CC       brain. May also participate in functions of the mature nervous
CC       system (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9JLM8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9JLM8-2; Sequence=VSP_019593, VSP_019594;
CC         Note=Phosphorylated on Ser-352;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. CaMK subfamily.
CC   -!- SIMILARITY: Contains 2 doublecortin domains.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF155819; AAF26673.1; -; mRNA.
DR   EMBL; BC064783; AAH64783.1; -; mRNA.
DR   IPI; IPI00468380; -.
DR   IPI; IPI00761729; -.
DR   RefSeq; NP_064362.1; NM_019978.3.
DR   UniGene; Mm.393242; -.
DR   UniGene; Mm.472264; -.
DR   ProteinModelPortal; Q9JLM8; -.
DR   SMR; Q9JLM8; 54-154, 180-267, 400-685.
DR   STRING; Q9JLM8; -.
DR   PhosphoSite; Q9JLM8; -.
DR   PRIDE; Q9JLM8; -.
DR   Ensembl; ENSMUST00000054237; ENSMUSP00000050034; ENSMUSG00000027797.
DR   Ensembl; ENSMUST00000089805; ENSMUSP00000087238; ENSMUSG00000027797.
DR   GeneID; 13175; -.
DR   KEGG; mmu:13175; -.
DR   UCSC; uc008pgl.1; mouse.
DR   CTD; 13175; -.
DR   MGI; MGI:1330861; Dclk1.
DR   GeneTree; ENSGT00600000084006; -.
DR   HOVERGEN; HBG003790; -.
DR   InParanoid; Q9JLM8; -.
DR   OrthoDB; EOG4H9XK1; -.
DR   PhylomeDB; Q9JLM8; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 283276; -.
DR   PMAP-CutDB; Q9JLM8; -.
DR   ArrayExpress; Q9JLM8; -.
DR   Bgee; Q9JLM8; -.
DR   CleanEx; MM_DCLK1; -.
DR   Genevestigator; Q9JLM8; -.
DR   GermOnline; ENSMUSG00000027797; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0048675; P:axon extension; IGI:MGI.
DR   GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IGI:MGI.
DR   GO; GO:0048813; P:dendrite morphogenesis; IGI:MGI.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IGI:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR003533; Doublecortin_dom.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Gene3D; G3DSA:3.10.20.230; Doublecortin_dom; 2.
DR   Pfam; PF03607; DCX; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00537; DCX; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF89837; Doublecortin_dom; 2.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50309; DC; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Developmental protein;
KW   Differentiation; Kinase; Neurogenesis; Nucleotide-binding;
KW   Phosphoprotein; Repeat; Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    756       Serine/threonine-protein kinase DCLK1.
FT                                /FTId=PRO_0000085920.
FT   DOMAIN       57    143       Doublecortin 1.
FT   DOMAIN      186    269       Doublecortin 2.
FT   DOMAIN      406    663       Protein kinase.
FT   NP_BIND     412    420       ATP (By similarity).
FT   COMPBIAS    298    358       Pro/Ser-rich.
FT   ACT_SITE    527    527       Proton acceptor (By similarity).
FT   BINDING     435    435       ATP (By similarity).
FT   MOD_RES      32     32       Phosphoserine.
FT   MOD_RES      36     36       Phosphoserine.
FT   MOD_RES     305    305       Phosphoserine.
FT   MOD_RES     307    307       Phosphoserine.
FT   MOD_RES     330    330       Phosphoserine.
FT   MOD_RES     332    332       Phosphoserine.
FT   MOD_RES     334    334       Phosphoserine (By similarity).
FT   MOD_RES     336    336       Phosphothreonine.
FT   MOD_RES     337    337       Phosphoserine.
FT   MOD_RES     364    364       Phosphoserine.
FT   MOD_RES     392    392       Phosphoserine.
FT   MOD_RES     509    509       Phosphotyrosine.
FT   MOD_RES     536    536       Phosphotyrosine.
FT   MOD_RES     738    738       Phosphoserine.
FT   MOD_RES     742    742       Phosphoserine.
FT   VAR_SEQ     343    363       KQRISQHGGSSTSLSSTKVCS -> RQRDLYRPLSSDDLDS
FT                                VGDSV (in isoform 2).
FT                                /FTId=VSP_019593.
FT   VAR_SEQ     364    756       Missing (in isoform 2).
FT                                /FTId=VSP_019594.
SQ   SEQUENCE   756 AA;  84153 MW;  3D1DBF18C23129F2 CRC64;
     MSFGRDMELE HFDERDKAQR YSRGSRVNGL PSPTHSAHCS FYRTRTLQTL SSEKKAKKVR
     FYRNGDRYFK GIVYAISPDR FRSFEALLAD LTRTLSDNVN LPQGVRTIYT IDGLKKISSL
     DQLVEGESYV CGSIEPFKKL EYTKNVNPNW SVNVKTTSAS RAVSSLATAK GGPSEVRENK
     DFIRPKLVTI IRSGVKPRKA VRILLNKKTA HSFEQVLTDI TDAIKLDSGV VKRLYTLDGK
     QVMCLQDFFG DDDIFIACGP EKFRYQDDFL LDESECRVVK STSYTKIASA SRRGTTKSPG
     PSRRSKSPAS TSSVNGTPGS QLSTPRSGKS PSPSPTSPGS LRKQRISQHG GSSTSLSSTK
     VCSSMDENDG PGEGDELGRR HSLQRGWRRE ESEEGFQIPA TITERYKVGR TIGDGNFAVV
     KECIERSTAR EYALKIIKKS KCRGKEHMIQ NEVSILRRVK HPNIVLLIEE MDVPTELYLV
     MELVKGGDLF DAITSTSKYT ERDASGMLYN LASAIKYLHS LNIVHRDIKP ENLLVYEHQD
     GSKSLKLGDF GLATIVDGPL YTVCGTPTYV APEIIAETGY GLKVDIWAAG VITYILLCGF
     PPFRGSGDDQ EVLFDQILMG QVDFPSPYWD NVSDSAKELI NMMLLVNVDQ RFSAVQVLEH
     PWVNDDGLPE NEHQLSVAGK IKKHFNTGPK PSSTAAGVSV IATTALDKER QVFRRRRNQD
     VRSRYKAQPA PPELNSESED YSPSSSETVR SPNSPF
//
ID   GRB14_MOUSE             Reviewed;         538 AA.
AC   Q9JLM9; Q3UI77; Q8VDI2; Q9CR03;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=Growth factor receptor-bound protein 14;
DE   AltName: Full=GRB14 adapter protein;
GN   Name=Grb14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20179877; PubMed=10713090; DOI=10.1074/jbc.275.11.7771;
RA   Reilly J.F., Mickey G., Maher P.A.;
RT   "Association of fibroblast growth factor receptor 1 with the adaptor
RT   protein Grb14. Characterization of a new receptor binding partner.";
RL   J. Biol. Chem. 275:7771-7778(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic liver, and Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 332-538.
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Adapter protein which modulates coupling of cell surface
CC       receptor kinases with specific signaling pathways. Binds to, and
CC       suppresses signals from, the activated insulin receptor (INSR).
CC       Markedly decreases insulin-stimulated AKT1 phosphorylation. Potent
CC       inhibitor of insulin-stimulated MAPK3 phosphorylation (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with the cytoplasmic domain of the
CC       autophosphorylated insulin receptor, through the SH2 domain. Binds
CC       to the ankyrin repeat region of TNKS2 via its N-terminus.
CC       Interacts with activated NRAS (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus
CC       membrane; Peripheral membrane protein (By similarity). Endosome
CC       membrane; Peripheral membrane protein (By similarity). Note=Upon
CC       insulin stimulation, translocates to the plasma membrane (By
CC       similarity).
CC   -!- DOMAIN: The PH domain binds relatively non-specifically and with
CC       low affinity to several phosphoinositides, the best binder being
CC       PI(3,4,5)P3 (By similarity).
CC   -!- SIMILARITY: Belongs to the GRB7/10/14 family.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 Ras-associating domain.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
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DR   EMBL; AF155647; AAF43996.1; -; mRNA.
DR   EMBL; AK010849; BAB27221.3; -; mRNA.
DR   EMBL; AK010903; BAB27256.3; -; mRNA.
DR   EMBL; AK147041; BAE27629.1; -; mRNA.
DR   EMBL; BC021820; AAH21820.1; -; mRNA.
DR   IPI; IPI00124500; -.
DR   RefSeq; NP_057928.1; NM_016719.1.
DR   UniGene; Mm.214554; -.
DR   ProteinModelPortal; Q9JLM9; -.
DR   SMR; Q9JLM9; 105-350, 371-535.
DR   STRING; Q9JLM9; -.
DR   PhosphoSite; Q9JLM9; -.
DR   PRIDE; Q9JLM9; -.
DR   Ensembl; ENSMUST00000028252; ENSMUSP00000028252; ENSMUSG00000026888.
DR   GeneID; 50915; -.
DR   KEGG; mmu:50915; -.
DR   UCSC; uc008jvx.1; mouse.
DR   CTD; 50915; -.
DR   MGI; MGI:1355324; Grb14.
DR   GeneTree; ENSGT00550000074537; -.
DR   HOGENOM; HBG358659; -.
DR   HOVERGEN; HBG000468; -.
DR   InParanoid; Q9JLM9; -.
DR   OMA; HLPHIGV; -.
DR   OrthoDB; EOG4N30NN; -.
DR   PhylomeDB; Q9JLM9; -.
DR   NextBio; 307911; -.
DR   ArrayExpress; Q9JLM9; -.
DR   Bgee; Q9JLM9; -.
DR   CleanEx; MM_GRB14; -.
DR   Genevestigator; Q9JLM9; -.
DR   GermOnline; ENSMUSG00000026888; Mus musculus.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005070; F:SH3/SH2 adaptor activity; IPI:MGI.
DR   GO; GO:0007165; P:signal transduction; TAS:MGI.
DR   InterPro; IPR015042; BPS-dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000159; Ras-assoc.
DR   InterPro; IPR000980; SH2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF08947; BPS; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00017; SH2; 1.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00314; RA; 1.
DR   SMART; SM00252; SH2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Endosome; Golgi apparatus; Membrane; Phosphoprotein;
KW   SH2 domain.
FT   CHAIN         1    538       Growth factor receptor-bound protein 14.
FT                                /FTId=PRO_0000150349.
FT   DOMAIN      104    190       Ras-associating.
FT   DOMAIN      232    340       PH.
FT   DOMAIN      437    533       SH2.
FT   MOD_RES     370    370       Phosphoserine.
SQ   SEQUENCE   538 AA;  60573 MW;  04ABD6CEB6ABC6CB CRC64;
     MTTSLQDGQS AAGRAGAQDS PLAVQVCRVA QGKGDAQDPA QVPGLHALSP ASDATLRGAI
     DRRKMKDLDV LEKPPIPNPF PELCCSPLTS VLSAGLFPRA NSRKKQVIKV YSEDETSRAL
     EVPSDITARD VCQLLILKNH YVDDNSWTLF EHLSHIGLER TVEDHELPTE VLSHWGVEED
     NKLYLRKNYA KYEFFKNPMY FFPEHMVSFA AEMNGDRSPT QILQVFLSSS TYPEIHGFLH
     AKEQGKKSWK KAYFFLRRSG LYFSTKGTSK EPRHLQLFSE FSTSHVYMSL AGKKKHGAPT
     PYGFCLKPNK AGGPRDLKML CAEEEQSRTC WVTAIRLLKD GMQLYQNYMH PYQGRSACNS
     QSMSPMRSVS ENSLVAMDFS GEKSRVIDNP TEALSVAVEE GLAWRKKGCL RLGNHGSPSA
     PSQSSAVNMA LHRSQPWFHH RISRDEAQRL IIRQGPVDGV FLVRDSQSNP RTFVLSMSHG
     QKIKHYQIIP VEDDGELFHT LDDGHTKFTD LIQLVEFYQL NRGVLPCKLK HYCARMAV
//
ID   MTOR_MOUSE              Reviewed;        2549 AA.
AC   Q9JLN9; Q2KHT0; Q811J5; Q9CST1;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Serine/threonine-protein kinase mTOR;
DE            EC=2.7.11.1;
DE   AltName: Full=FK506-binding protein 12-rapamycin complex-associated protein 1;
DE   AltName: Full=FKBP12-rapamycin complex-associated protein;
DE   AltName: Full=Mammalian target of rapamycin;
DE            Short=mTOR;
DE   AltName: Full=Mechanistic target of rapamycin;
DE   AltName: Full=Rapamycin target protein 1;
DE            Short=RAPT1;
GN   Name=Mtor; Synonyms=Frap, Frap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c;
RA   Bliskovsky V., Mock B.;
RT   "Positional cloning of mouse plasmacytoma susceptibility gene.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Kidney, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1155-1334.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PROTEIN SEQUENCE OF 1287-1293, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1987-2146, INTERACTION WITH THE
RP   FKBP12-RAPAMYCIN COMPLEX, AND MUTAGENESIS OF SER-2035.
RC   TISSUE=Embryo;
RX   MEDLINE=95108000; PubMed=7809080; DOI=10.1073/pnas.91.26.12574;
RA   Chiu M.I., Katz H., Berlin V.;
RT   "RAPT1, a mammalian homolog of yeast Tor, interacts with the
RT   FKBP12/rapamycin complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:12574-12578(1994).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11930000; DOI=10.1073/pnas.261702698;
RA   Desai B.N., Myers B.R., Schreiber S.L.;
RT   "FKBP12-rapamycin-associated protein associates with mitochondria and
RT   senses osmotic stress via mitochondrial dysfunction.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4319-4324(2002).
RN   [8]
RP   FUNCTION, AND IDENTIFICATION IN TORC2 COMPLEX.
RX   PubMed=15467718; DOI=10.1038/ncb1183;
RA   Jacinto E., Loewith R., Schmidt A., Lin S., Ruegg M.A., Hall A.,
RA   Hall M.N.;
RT   "Mammalian TOR complex 2 controls the actin cytoskeleton and is
RT   rapamycin insensitive.";
RL   Nat. Cell Biol. 6:1122-1128(2004).
RN   [9]
RP   FUNCTION.
RX   PubMed=16221682; DOI=10.1074/jbc.M508361200;
RA   Hresko R.C., Mueckler M.;
RT   "mTOR.RICTOR is the Ser473 kinase for Akt/protein kinase B in 3T3-L1
RT   adipocytes.";
RL   J. Biol. Chem. 280:40406-40416(2005).
RN   [10]
RP   FUNCTION, AND IDENTIFICATION IN TORC2 COMPLEX.
RX   PubMed=16962653; DOI=10.1016/j.cell.2006.08.033;
RA   Jacinto E., Facchinetti V., Liu D., Soto N., Wei S., Jung S.Y.,
RA   Huang Q., Qin J., Su B.;
RT   "SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt
RT   phosphorylation and substrate specificity.";
RL   Cell 127:125-137(2006).
RN   [11]
RP   INTERACTION WITH PPAPDC3.
RX   PubMed=19704009; DOI=10.1128/MCB.00684-09;
RA   Liu G.H., Guan T., Datta K., Coppinger J., Yates J. III, Gerace L.;
RT   "Regulation of myoblast differentiation by the nuclear envelope
RT   protein NET39.";
RL   Mol. Cell. Biol. 29:5800-5812(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2478 AND SER-2481, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2481, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Kinase subunit of both mTORC1 and mTORC2, which
CC       regulates cell growth and survival in response to nutrient and
CC       hormonal signals. mTORC1 is activated in response to growth
CC       factors or amino-acids. Growth factor-stimulated mTORC1 activation
CC       involves AKT1-mediated phosphorylation of TSC1-TSC2, which leads
CC       to the activation of the RHEB GTPase that potently activates the
CC       protein kinase activity of mTORC1. Amino-acid-signaling to mTORC1
CC       requires its relocalization to the lysosomes mediated by the
CC       Ragulator complex and the Rag GTPases. Activated mTORC1 up-
CC       regulates protein synthesis by phosphorylating key regulators of
CC       mRNA translation and ribosome synthesis. mTORC1 phosphorylates
CC       EIF4EBP1 and releases it from inhibiting the elongation initiation
CC       factor 4E (eiF4E). mTORC1 phosphorylates EIF4EBP1 and releases it
CC       from inhibiting the elongation initiation factor 4E (eiF4E).
CC       mTORC1 phosphorylates and activates S6K1 at 'Thr-421', which then
CC       promotes protein synthesis by phosphorylating PDCD4 and targeting
CC       it for degradation. Phosphorylates MAF1 leading to attenuation of
CC       its RNA polymerase III-repressive function. mTORC2 is also
CC       activated by growth factors, but seems to be nutrient-insensitive.
CC       mTORC2 seems to function upstream of Rho GTPases to regulate the
CC       actin cytoskeleton, probably by activating one or more Rho-type
CC       guanine nucleotide exchange factors. mTORC2 promotes the serum-
CC       induced formation of stress-fibers or F-actin. mTORC2 plays a
CC       critical role in AKT1 'Ser-473' phosphorylation, which may
CC       facilitate the phosphorylation of the activation loop of AKT1 on
CC       'Thr-308' by PDK1 which is a prerequisite for full activation.
CC       mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2
CC       also modulates the phosphorylation of PRKCA on 'Ser-657'.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Kinase activity is positively regulated by RHEB
CC       and negatively regulated by DEPTOR (By similarity).
CC   -!- SUBUNIT: Part of the mammalian target of rapamycin complex 1
CC       (mTORC1) which contains MTOR/FRAP1, MLST8, RPTOR and AKT1S1 (By
CC       similarity). mTORC1 binds to and is inhibited by FKBP12-rapamycin.
CC       Part of the mammalian target of rapamycin complex 2 (mTORC2) which
CC       contains MTOR, MLST8, PRR5, RICTOR and MAPKAP1. Contrary to
CC       mTORC1, mTORC2 does not bind to and is not sensitive to FKBP12-
CC       rapamycin. Binds directly to PRR5 and RICTOR within the mTORC2
CC       complex (By similarity). Interacts with UBQLN1 (By similarity).
CC       Interacts with DEPTOR. Interacts with TTI1 and TELO2 (By
CC       similarity). Interacts with PPAPDC3.
CC   -!- INTERACTION:
CC       Q13541:EIF4EBP1 (xeno); NbExp=1; IntAct=EBI-1571628, EBI-74090;
CC       P67999:Rps6kb1 (xeno); NbExp=1; IntAct=EBI-1571628, EBI-2639458;
CC       Q8N122:RPTOR (xeno); NbExp=1; IntAct=EBI-1571628, EBI-1567928;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein; Cytoplasmic side (By similarity). Golgi
CC       apparatus membrane; Peripheral membrane protein; Cytoplasmic side
CC       (By similarity). Mitochondrion outer membrane; Peripheral membrane
CC       protein; Cytoplasmic side. Lysosome (By similarity).
CC       Note=Targeting to lysosomes depends on amino acid availability and
CC       RRAGA and RRAGB (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9JLN9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9JLN9-2; Sequence=VSP_011909, VSP_011910;
CC         Note=No experimental confirmation available;
CC   -!- PTM: Autophosphorylated; when part of mTORC1 or mTORC2 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC   -!- SIMILARITY: Contains 1 FAT domain.
CC   -!- SIMILARITY: Contains 1 FATC domain.
CC   -!- SIMILARITY: Contains 7 HEAT repeats.
CC   -!- SIMILARITY: Contains 1 PI3K/PI4K domain.
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DR   EMBL; AF152838; AAF73196.1; -; mRNA.
DR   EMBL; AL731654; CAM22525.1; -; Genomic_DNA.
DR   EMBL; AL713995; CAM22525.1; JOINED; Genomic_DNA.
DR   EMBL; AL713995; CAM23943.1; -; Genomic_DNA.
DR   EMBL; AL731654; CAM23943.1; JOINED; Genomic_DNA.
DR   EMBL; CU210865; CAQ51622.1; -; Genomic_DNA.
DR   EMBL; BC043920; AAH43920.1; -; mRNA.
DR   EMBL; BC112904; AAI12905.1; -; mRNA.
DR   EMBL; AK012031; BAB27985.2; -; mRNA.
DR   IPI; IPI00268673; -.
DR   IPI; IPI00457494; -.
DR   RefSeq; NP_064393.2; NM_020009.2.
DR   UniGene; Mm.21158; -.
DR   ProteinModelPortal; Q9JLN9; -.
DR   SMR; Q9JLN9; 695-722, 731-779, 818-850, 864-890, 1130-1185, 2019-2112, 2142-2423, 2517-2549.
DR   DIP; DIP-40570N; -.
DR   IntAct; Q9JLN9; 8.
DR   MINT; MINT-1899010; -.
DR   STRING; Q9JLN9; -.
DR   PhosphoSite; Q9JLN9; -.
DR   PRIDE; Q9JLN9; -.
DR   Ensembl; ENSMUST00000103221; ENSMUSP00000099510; ENSMUSG00000028991.
DR   GeneID; 56717; -.
DR   KEGG; mmu:56717; -.
DR   UCSC; uc008vuq.1; mouse.
DR   UCSC; uc008vur.1; mouse.
DR   CTD; 56717; -.
DR   MGI; MGI:1928394; Mtor.
DR   GeneTree; ENSGT00600000084391; -.
DR   HOGENOM; HBG320181; -.
DR   HOVERGEN; HBG005744; -.
DR   InParanoid; Q9JLN9; -.
DR   OrthoDB; EOG41RPT0; -.
DR   PhylomeDB; Q9JLN9; -.
DR   NextBio; 313190; -.
DR   ArrayExpress; Q9JLN9; -.
DR   Bgee; Q9JLN9; -.
DR   Genevestigator; Q9JLN9; -.
DR   GermOnline; ENSMUSG00000028991; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
DR   GO; GO:0007281; P:germ cell development; IDA:MGI.
DR   GO; GO:0045792; P:negative regulation of cell size; IGI:MGI.
DR   GO; GO:0016242; P:negative regulation of macroautophagy; IMP:MGI.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:MGI.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:MGI.
DR   GO; GO:0010592; P:positive regulation of lamellipodium assembly; IDA:MGI.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
DR   GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:MGI.
DR   GO; GO:0045859; P:regulation of protein kinase activity; IGI:MGI.
DR   GO; GO:0032314; P:regulation of Rac GTPase activity; IMP:MGI.
DR   GO; GO:0043200; P:response to amino acid stimulus; IDA:MGI.
DR   GO; GO:0032868; P:response to insulin stimulus; IDA:MGI.
DR   GO; GO:0031529; P:ruffle organization; IDA:MGI.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR003152; FATC.
DR   InterPro; IPR009076; FKBP_rapamycin-assoc_FKBP12-bd.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000403; PI3/4_kinase_cat.
DR   InterPro; IPR018936; PI3/4_kinase_CS.
DR   InterPro; IPR003151; PIK-rel_kinase_FAT.
DR   InterPro; IPR014009; PIK_FAT.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 3.
DR   Gene3D; G3DSA:1.20.120.150; FRAP_FKBP12_bd; 1.
DR   Gene3D; G3DSA:1.10.1070.11; PI3/4_kinase_cat; 3.
DR   Pfam; PF02259; FAT; 1.
DR   Pfam; PF02260; FATC; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF08771; Rapamycin_bind; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 2.
DR   SUPFAM; SSF47212; FRAP_FKBP12_bind; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51189; FAT; 1.
DR   PROSITE; PS51190; FATC; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; FALSE_NEG.
DR   PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding;
KW   Direct protein sequencing; Endoplasmic reticulum; Golgi apparatus;
KW   Kinase; Lysosome; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Nucleotide-binding; Phosphoprotein;
KW   Repeat; Transferase.
FT   CHAIN         1   2549       Serine/threonine-protein kinase mTOR.
FT                                /FTId=PRO_0000088809.
FT   REPEAT       16     53       HEAT 1.
FT   REPEAT      650    688       HEAT 2.
FT   REPEAT      859    897       HEAT 3.
FT   REPEAT      988   1025       HEAT 4.
FT   REPEAT     1069   1106       HEAT 5.
FT   REPEAT     1109   1148       HEAT 6.
FT   REPEAT     1150   1186       HEAT 7.
FT   DOMAIN     1382   1982       FAT.
FT   DOMAIN     2182   2516       PI3K/PI4K.
FT   DOMAIN     2517   2549       FATC.
FT   MOD_RES     567    567       Phosphoserine (By similarity).
FT   MOD_RES     916    916       Phosphoserine (By similarity).
FT   MOD_RES    1162   1162       Phosphothreonine (By similarity).
FT   MOD_RES    1218   1218       N6-acetyllysine (By similarity).
FT   MOD_RES    1261   1261       Phosphoserine (By similarity).
FT   MOD_RES    1829   1829       Phosphothreonine (By similarity).
FT   MOD_RES    1843   1843       Phosphoserine (By similarity).
FT   MOD_RES    1847   1847       Phosphoserine (By similarity).
FT   MOD_RES    1849   1849       Phosphoserine (By similarity).
FT   MOD_RES    1851   1851       Phosphoserine (By similarity).
FT   MOD_RES    1859   1859       Phosphoserine (By similarity).
FT   MOD_RES    1863   1863       Phosphoserine (By similarity).
FT   MOD_RES    2448   2448       Phosphoserine (By similarity).
FT   MOD_RES    2449   2449       Phosphotyrosine (By similarity).
FT   MOD_RES    2478   2478       Phosphoserine.
FT   MOD_RES    2481   2481       Phosphoserine.
FT   VAR_SEQ     236    256       HTFEEAEKGFDETLAKEKGMN -> VRDGSTQPLAKHFGLE
FT                                SCSWP (in isoform 2).
FT                                /FTId=VSP_011909.
FT   VAR_SEQ     257   2549       Missing (in isoform 2).
FT                                /FTId=VSP_011910.
FT   MUTAGEN    2035   2035       S->R: Abolishes interaction with the
FT                                FKBP12-rapamycin complex.
FT   CONFLICT     33     33       N -> K (in Ref. 3; AAH43920).
FT   CONFLICT    628    628       R -> C (in Ref. 1; AAF73196).
SQ   SEQUENCE   2549 AA;  288789 MW;  56302E5171FB6DBD CRC64;
     MLGTGPAVAT ASAATSSNVS VLQQFASGLK SRNEETRAKA AKELQHYVTM ELREMSQEES
     TRFYDQLNHH IFELVSSSDA NERKGGILAI ASLIGVEGGN STRIGRFANY LRNLLPSSDP
     VVMEMASKAI GRLAMAGDTF TAEYVEFEVK RALEWLGADR NEGRRHAAVL VLRELAISVP
     TFFFQQVQPF FDNIFVAVWD PKQAIREGAV AALRACLILT TQREPKEMQK PQWYRHTFEE
     AEKGFDETLA KEKGMNRDDR IHGALLILNE LVRISSMEGE RLREEMEEIT QQQLVHDKYC
     KDLMGFGTKP RHITPFTSFQ AVQPQQPNAL VGLLGYSSPQ GLMGFGTSPS PAKSTLVESR
     CCRDLMEEKF DQVCQWVLKC RSSKNSLIQM TILNLLPRLA AFRPSAFTDT QYLQDTMNHV
     LSCVKKEKER TAAFQALGLL SVAVRSEFKV YLPRVLDIIR AALPPKDFAH KRQKTVQVDA
     TVFTCISMLA RAMGPGIQQD IKELLEPMLA VGLSPALTAV LYDLSRQIPQ LKKDIQDGLL
     KMLSLVLMHK PLRHPGMPKG LAHQLASPGL TTLPEASDVA SITLALRTLG SFEFEGHSLT
     QFVRHCADHF LNSEHKEIRM EAARTCSRLL TPSIHLISGH AHVVSQTAVQ VVADVLSKLL
     VVGITDPDPD IRYCVLASLD ERFDAHLAQA ENLQALFVAL NDQVFEIREL AICTVGRLSS
     MNPAFVMPFL RKMLIQILTE LEHSGIGRIK EQSARMLGHL VSNAPRLIRP YMEPILKALI
     LKLKDPDPDP NPGVINNVLA TIGELAQVSG LEMRKWVDEL FIIIMDMLQD SSLLAKRQVA
     LWTLGQLVAS TGYVVEPYRK YPTLLEVLLN FLKTEQNQGT RREAIRVLGL LGALDPYKHK
     VNIGMIDQSR DASAVSLSES KSSQDSSDYS TSEMLVNMGN LPLDEFYPAV SMVALMRIFR
     DQSLSHHHTM VVQAITFIFK SLGLKCVQFL PQVMPTFLNV IRVCDGAIRE FLFQQLGMLV
     SFVKSHIRPY MDEIVTLMRE FWVMNTSIQS TIILLIEQIV VALGGEFKLY LPQLIPHMLR
     VFMHDNSQGR IVSIKLLAAI QLFGANLDDY LHLLLPPIVK LFDAPEVPLP SRKAALETVD
     RLTESLDFTD YASRIIHPIV RTLDQSPELR STAMDTLSSL VFQLGKKYQI FIPMVNKVLV
     RHRINHQRYD VLICRIVKGY TLADEEEDPL IYQHRMLRSS QGDALASGPV ETGPMKKLHV
     STINLQKAWG AARRVSKDDW LEWLRRLSLE LLKDSSSPSL RSCWALAQAY NPMARDLFNA
     AFVSCWSELN EDQQDELIRS IELALTSQDI AEVTQTLLNL AEFMEHSDKG PLPLRDDNGI
     VLLGERAAKC RAYAKALHYK ELEFQKGPTP AILESLISIN NKLQQPEAAS GVLEYAMKHF
     GELEIQATWY EKLHEWEDAL VAYDKKMDTN KEDPELMLGR MRCLEALGEW GQLHQQCCEK
     WTLVNDETQA KMARMAAAAA WGLGQWDSME EYTCMIPRDT HDGAFYRAVL ALHQDLFSLA
     QQCIDKARDL LDAELTAMAG ESYSRAYGAM VSCHMLSELE EVIQYKLVPE RREIIRQIWW
     ERLQGCQRIV EDWQKILMVR SLVVSPHEDM RTWLKYASLC GKSGRLALAH KTLVLLLGVD
     PSRQLDHPLP TAHPQVTYAY MKNMWKSARK IDAFQHMQHF VQTMQQQAQH AIATEDQQHK
     QELHKLMARC FLKLGEWQLN LQGINESTIP KVLQYYSAAT EHDRSWYKAW HAWAVMNFEA
     VLHYKHQNQA RDEKKKLRHA SGANITNATT AATTAASAAA ATSTEGSNSE SEAESNENSP
     TPSPLQKKVT EDLSKTLLLY TVPAVQGFFR SISLSRGNNL QDTLRVLTLW FDYGHWPDVN
     EALVEGVKAI QIDTWLQVIP QLIARIDTPR PLVGRLIHQL LTDIGRYHPQ ALIYPLTVAS
     KSTTTARHNA ANKILKNMCE HSNTLVQQAM MVSEELIRVA ILWHEMWHEG LEEASRLYFG
     ERNVKGMFEV LEPLHAMMER GPQTLKETSF NQAYGRDLME AQEWCRKYMK SGNVKDLTQA
     WDLYYHVFRR ISKQLPQLTS LELQYVSPKL LMCRDLELAV PGTYDPNQPI IRIQSIAPSL
     QVITSKQRPR KLTLMGSNGH EFVFLLKGHE DLRQDERVMQ LFGLVNTLLA NDPTSLRKNL
     SIQRYAVIPL STNSGLIGWV PHCDTLHALI RDYREKKKIL LNIEHRIMLR MAPDYDHLTL
     MQKVEVFEHA VNNTAGDDLA KLLWLKSPSS EVWFDRRTNY TRSLAVMSMV GYILGLGDRH
     PSNLMLDRLS GKILHIDFGD CFEVAMTREK FPEKIPFRLT RMLTNAMEVT GLDGNYRTTC
     HTVMEVLREH KDSVMAVLEA FVYDPLLNWR LMDTNTKGNK RSRTRTDSYS AGQSVEILDG
     VELGEPAHKK AGTTVPESIH SFIGDGLVKP EALNKKAIQI INRVRDKLTG RDFSHDDTLD
     VPTQVELLIK QATSHENLCQ CYIGWCPFW
//
ID   CD2AP_MOUSE             Reviewed;         637 AA.
AC   Q9JLQ0; O88903; Q8K4Z1; Q8VCI9;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 2.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=CD2-associated protein;
DE   AltName: Full=Mesenchyme-to-epithelium transition protein with SH3 domains 1;
DE            Short=METS-1;
GN   Name=Cd2ap; Synonyms=Mets1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CD2.
RX   MEDLINE=98412662; PubMed=9741631; DOI=10.1016/S0092-8674(00)81608-6;
RA   Dustin M.L., Olszowy M.W., Holdorf A.D., Li J., Bromley S., Desai N.,
RA   Widder P., Rosenberger F., van der Merwe P.A., Allen P.M., Shaw A.S.;
RT   "A novel adaptor protein orchestrates receptor patterning and
RT   cytoskeletal polarity in T-cell contacts.";
RL   Cell 94:667-677(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH PKD2.
RX   MEDLINE=20490726; PubMed=10913159; DOI=10.1074/jbc.M006624200;
RA   Lehtonen S., Ora A., Olkkonen V.M., Geng L., Zerial M., Somlo S.,
RA   Lehtonen E.;
RT   "In vivo interaction of the adapter protein CD2-associated protein
RT   with the type 2 polycystic kidney disease protein, polycystin-2.";
RL   J. Biol. Chem. 275:32888-32893(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Meton I., Le Marchand-Brustel Y., Cormont M.;
RT   "Role of the interaction between CD2AP and c-Cbl.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 394-637.
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NPHS1, AND DISRUPTION
RP   PHENOTYPE.
RX   MEDLINE=99445926; PubMed=10514378; DOI=10.1126/science.286.5438.312;
RA   Shih N.Y., Li J., Karpitskii V., Nguyen A., Dustin M.L., Kanagawa O.,
RA   Miner J.H., Shaw A.S.;
RT   "Congenital nephrotic syndrome in mice lacking CD2-associated
RT   protein.";
RL   Science 286:312-315(1999).
RN   [6]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH NPHS1.
RX   MEDLINE=21590051; PubMed=11733379;
RA   Shih N.Y., Li J., Cotran R., Mundel P., Miner J.H., Shaw A.S.;
RT   "CD2AP localizes to the slit diaphragm and binds to nephrin via a
RT   novel C-terminal domain.";
RL   Am. J. Pathol. 159:2303-2308(2001).
RN   [7]
RP   INTERACTION WITH NPHS1 AND NPHS2.
RX   MEDLINE=21590460; PubMed=11733557;
RA   Schwarz K., Simons M., Reiser J., Saleem M.A., Faul C., Kriz W.,
RA   Shaw A.S., Holzman L.B., Mundel P.;
RT   "Podocin, a raft-associated component of the glomerular slit
RT   diaphragm, interacts with CD2AP and nephrin.";
RL   J. Clin. Invest. 108:1621-1629(2001).
RN   [8]
RP   INTERACTION WITH F-ACTIN.
RX   MEDLINE=22205713; PubMed=12217865; DOI=10.1152/ajprenal.00312.2001;
RA   Lehtonen S., Zhao F., Lehtonen E.;
RT   "CD2-associated protein directly interacts with the actin
RT   cytoskeleton.";
RL   Am. J. Physiol. 283:F734-F743(2002).
RN   [9]
RP   INTERACTION WITH WTIP.
RX   PubMed=14736876; DOI=10.1074/jbc.M314155200;
RA   Srichai M.B., Konieczkowski M., Padiyar A., Konieczkowski D.J.,
RA   Mukherjee A., Hayden P.S., Kamat S., El-Meanawy M.A., Khan S.,
RA   Mundel P., Lee S.B., Bruggeman L.A., Schelling J.R., Sedor J.R.;
RT   "A WT1 co-regulator controls podocyte phenotype by shuttling between
RT   adhesion structures and nucleus.";
RL   J. Biol. Chem. 279:14398-14408(2004).
RN   [10]
RP   INTERACTION WITH DDN.
RX   PubMed=17537921; DOI=10.1073/pnas.0700917104;
RA   Asanuma K., Campbell K.N., Kim K., Faul C., Mundel P.;
RT   "Nuclear relocation of the nephrin and CD2AP-binding protein dendrin
RT   promotes apoptosis of podocytes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10134-10139(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Required for cytokinesis (By similarity). Seems to act
CC       as an adapter protein between membrane proteins and the actin
CC       cytoskeleton. May play a role in receptor clustering and
CC       cytoskeletal polarity in the junction between T-cell and antigen-
CC       presenting cell. May anchor the podocyte slit diaphragm to the
CC       actin cytoskeleton in renal glomerolus.
CC   -!- SUBUNIT: Self-associates. Homodimer (Potential). Interacts (via
CC       SH3 2 domain) with CBL (via phosphorylated C-terminus). Interacts
CC       with BCAR1/p130Cas (via SH3 domain). Interacts with F-actin, PKD2,
CC       NPHS1 and NPHS2. Interacts with WTIP. Interacts with FAM125A and
CC       ARHGAP17. Interacts with ANLN, CD2 and CBLB. Interacts with
CC       PDCD6IP and TSG101 (By similarity). Interacts with DDN;
CC       interaction is direct.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection,
CC       ruffle. Note=During late anaphase and telophase, concentrates in
CC       the vicinity of the midzone microtubules and in the midbody in
CC       late telophase (By similarity). Located at podocyte slit diaphragm
CC       between podocyte foot processes.
CC   -!- DOMAIN: Potential homodimerization is mediated by the coiled coil
CC       domain (By similarity).
CC   -!- PTM: Phosphorylated on tyrosine residues; probably by c-Abl, Fyn
CC       and c-Src (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Death at 6 to 7 weeks of age from renal
CC       failure. Mice show defects in epithelial foot processes,
CC       accompanied by mesangial cell hyperplasia and extracellular matrix
CC       deposition.
CC   -!- SIMILARITY: Contains 3 SH3 domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF077003; AAC36099.1; -; mRNA.
DR   EMBL; AF149092; AAF73150.1; -; mRNA.
DR   EMBL; AJ459109; CAD30510.1; -; mRNA.
DR   EMBL; BC019744; AAH19744.1; -; mRNA.
DR   IPI; IPI00268688; -.
DR   RefSeq; NP_033977.3; NM_009847.3.
DR   UniGene; Mm.218637; -.
DR   PDB; 2JTE; NMR; -; A=270-329.
DR   PDB; 2KRM; NMR; -; A=2-58.
DR   PDB; 2KRN; NMR; -; A=111-166.
DR   PDB; 2KRO; NMR; -; A=270-329.
DR   PDBsum; 2JTE; -.
DR   PDBsum; 2KRM; -.
DR   PDBsum; 2KRN; -.
DR   PDBsum; 2KRO; -.
DR   ProteinModelPortal; Q9JLQ0; -.
DR   SMR; Q9JLQ0; 2-168, 266-329, 475-503.
DR   IntAct; Q9JLQ0; 14.
DR   MINT; MINT-255809; -.
DR   STRING; Q9JLQ0; -.
DR   PhosphoSite; Q9JLQ0; -.
DR   PRIDE; Q9JLQ0; -.
DR   Ensembl; ENSMUST00000024709; ENSMUSP00000024709; ENSMUSG00000061665.
DR   GeneID; 12488; -.
DR   KEGG; mmu:12488; -.
DR   UCSC; uc008cot.1; mouse.
DR   CTD; 12488; -.
DR   MGI; MGI:1330281; Cd2ap.
DR   eggNOG; roNOG12271; -.
DR   GeneTree; ENSGT00530000063594; -.
DR   HOGENOM; HBG445658; -.
DR   HOVERGEN; HBG057824; -.
DR   InParanoid; Q9JLQ0; -.
DR   OrthoDB; EOG4GMTWW; -.
DR   NextBio; 281400; -.
DR   ArrayExpress; Q9JLQ0; -.
DR   Bgee; Q9JLQ0; -.
DR   CleanEx; MM_CD2AP; -.
DR   Genevestigator; Q9JLQ0; -.
DR   GermOnline; ENSMUSG00000061665; Mus musculus.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   InterPro; IPR000108; p67phox.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00018; SH3_1; 2.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR00499; P67PHOX.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 3.
DR   SUPFAM; SSF50044; SH3; 3.
DR   PROSITE; PS50002; SH3; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Cell projection; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Mitosis; Phosphoprotein; Repeat; SH3 domain;
KW   SH3-binding.
FT   CHAIN         1    637       CD2-associated protein.
FT                                /FTId=PRO_0000089436.
FT   DOMAIN        1     59       SH3 1; truncated.
FT   DOMAIN      108    167       SH3 2.
FT   DOMAIN      269    330       SH3 3.
FT   REGION        1    175       Interaction with ANLN and localization to
FT                                the midbody (By similarity).
FT   COILED      578    636       Potential.
FT   MOTIF       336    352       SH3-binding (Potential).
FT   MOTIF       378    397       SH3-binding (Potential).
FT   MOTIF       410    422       SH3-binding (Potential).
FT   COMPBIAS    336    422       Pro-rich.
FT   MOD_RES      88     88       Phosphotyrosine (By similarity).
FT   MOD_RES     224    224       Phosphoserine (By similarity).
FT   MOD_RES     458    458       Phosphoserine.
FT   MOD_RES     510    510       Phosphoserine (By similarity).
FT   CONFLICT     78     78       V -> E (in Ref. 2; AAF73150).
FT   CONFLICT    107    107       Missing (in Ref. 1; AAC36099).
FT   CONFLICT    110    110       K -> Q (in Ref. 1; AAC36099).
FT   CONFLICT    244    244       P -> R (in Ref. 1; AAC36099).
FT   CONFLICT    295    297       IIH -> LS (in Ref. 1; AAC36099).
FT   CONFLICT    392    392       P -> PTAPTKA (in Ref. 1; AAC36099).
FT   CONFLICT    545    545       P -> S (in Ref. 1; AAC36099).
FT   CONFLICT    578    578       K -> R (in Ref. 1; AAC36099).
FT   STRAND      272    278
FT   STRAND      285    287
FT   STRAND      295    298
FT   HELIX       322    324
FT   STRAND      325    329
SQ   SEQUENCE   637 AA;  70432 MW;  24B3702130C2391B CRC64;
     MVDYIVEYDY DAVHDDELTI RVGEIIRNVK KLQEEGWLEG ELNGRRGMFP DNFVKEIKRE
     TEPKDDNLPI KRERQGNVAS LVQRISTYGL PAGGIQPHPQ TKAIKKKTKK RQCKVLFDYS
     PQNEDELELI VGDVIDVIEE VEEGWWSGTL NNKLGLFPSN FVKELESTED GETHNAQEES
     EVPLTGPTSP LPSPGNGSEP APGSVAQPKK IRGIGFGDIF KEGSVKLRTR TSSSETEEKK
     TEKPLILQPL GSRTQNVEVT KPDVDGKIKA KEYCRTLFPY TGTNEDELTF REGEIIHLIS
     KETGEAGWWK GELNGKEGVF PDNFAVQISE LDKDFPKPKK PPPPAKGPAP KPDLSAAEKK
     AFPLKAEEKD EKSLLEQKPS KPAAPQVPPK KPTAPTKASN LLRSPGAVYP KRPEKPVPPP
     PPAAKINGEV SIISSKIDTE PVSKPKLDPE QLPVRPKSVD LDAFVARNSK ETDDVNFDDI
     ASSENLLHLT ANRPKMPGRR LPGRFNGGHS PTQSPEKTLK LPKEDDSGNL KPLEFKKDAS
     YSSKPSLSTP SSASKVNTAA FLTPLELKAK AEADDGKKNS VDELRAQIIE LLCIVDALKK
     DHGKELEKLR KELEEEKAMR SNLEVEIAKL KKAVLLS
//
ID   BAG3_MOUSE              Reviewed;         577 AA.
AC   Q9JLV1; Q9JJC7;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=BAG family molecular chaperone regulator 3;
DE            Short=BAG-3;
DE   AltName: Full=Bcl-2-associated athanogene 3;
DE   AltName: Full=Bcl-2-binding protein Bis;
GN   Name=Bag3; Synonyms=Bis; ORFNames=MNCb-2243;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20065084; PubMed=10597216; DOI=10.1038/sj.onc.1203043;
RA   Lee J.H., Takahashi T., Yasuhara N., Inazawa J., Kamada S.,
RA   Tsujimoto Y.;
RT   "Bis, a Bcl-2-binding protein that synergizes with Bcl-2 in preventing
RT   cell death.";
RL   Oncogene 18:6183-6190(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S.,
RA   Hashimoto K.;
RT   "Isolation of full-length cDNA clones from mouse brain cDNA library
RT   made by oligo-capping method.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [5]
RP   STRUCTURE BY NMR OF 404-503.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the murine BAG domain of Bcl2-associated
RT   athanogene 3.";
RL   Submitted (FEB-2004) to the PDB data bank.
CC   -!- FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by
CC       promoting substrate release. Has anti-apoptotic activity.
CC   -!- SUBUNIT: Binds to the ATPase domain of HSP/HSC70 chaperones. Binds
CC       to Bcl-2 and PLC-gamma (By similarity).
CC   -!- SIMILARITY: Contains 1 BAG domain.
CC   -!- SIMILARITY: Contains 2 WW domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF130471; AAF26840.1; -; mRNA.
DR   EMBL; AB041583; BAA95066.1; -; mRNA.
DR   IPI; IPI00331334; -.
DR   UniGene; Mm.84073; -.
DR   PDB; 1UK5; NMR; -; A=406-503.
DR   PDBsum; 1UK5; -.
DR   ProteinModelPortal; Q9JLV1; -.
DR   SMR; Q9JLV1; 18-57, 401-503.
DR   IntAct; Q9JLV1; 1.
DR   STRING; Q9JLV1; -.
DR   PhosphoSite; Q9JLV1; -.
DR   PRIDE; Q9JLV1; -.
DR   Ensembl; ENSMUST00000033136; ENSMUSP00000033136; ENSMUSG00000030847.
DR   MGI; MGI:1352493; Bag3.
DR   GeneTree; ENSGT00530000063256; -.
DR   HOGENOM; HBG714179; -.
DR   HOVERGEN; HBG003419; -.
DR   InParanoid; Q9JLV1; -.
DR   OrthoDB; EOG4ZW5BW; -.
DR   ArrayExpress; Q9JLV1; -.
DR   Bgee; Q9JLV1; -.
DR   CleanEx; MM_BAG3; -.
DR   Genevestigator; Q9JLV1; -.
DR   GermOnline; ENSMUSG00000030847; Mus musculus.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0006916; P:anti-apoptosis; IDA:MGI.
DR   InterPro; IPR003103; Apoptosis_reg_Bcl-2_prot_BAG.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Pfam; PF02179; BAG; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00264; BAG; 1.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF51045; WW_Rsp5_WWP; 1.
DR   PROSITE; PS51035; BAG; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Apoptosis; Chaperone; Phosphoprotein; Repeat.
FT   CHAIN         1    577       BAG family molecular chaperone regulator
FT                                3.
FT                                /FTId=PRO_0000088869.
FT   DOMAIN       22     56       WW 1.
FT   DOMAIN      126    157       WW 2.
FT   DOMAIN      426    503       BAG.
FT   COMPBIAS    186    193       Poly-Ser.
FT   MOD_RES     136    136       Phosphoserine (By similarity).
FT   MOD_RES     138    138       Phosphoserine (By similarity).
FT   MOD_RES     177    177       Phosphoserine (By similarity).
FT   MOD_RES     179    179       Phosphoserine (By similarity).
FT   MOD_RES     200    200       Phosphoserine (By similarity).
FT   MOD_RES     246    246       Phosphotyrosine (By similarity).
FT   MOD_RES     253    253       Phosphotyrosine (By similarity).
FT   MOD_RES     280    280       Phosphoserine (By similarity).
FT   MOD_RES     281    281       Phosphoserine (By similarity).
FT   MOD_RES     285    285       Phosphoserine (By similarity).
FT   MOD_RES     291    291       Phosphothreonine (By similarity).
FT   MOD_RES     297    297       Phosphoserine.
FT   MOD_RES     382    382       Phosphoserine (By similarity).
FT   MOD_RES     386    386       Phosphoserine (By similarity).
FT   MOD_RES     390    390       Phosphoserine.
FT   CONFLICT     74     74       N -> D (in Ref. 2; BAA95066).
FT   CONFLICT    527    527       P -> Q (in Ref. 2; BAA95066).
FT   CONFLICT    539    539       K -> E (in Ref. 2; BAA95066).
FT   STRAND      417    420
FT   HELIX       425    445
FT   STRAND      451    453
FT   HELIX       454    471
SQ   SEQUENCE   577 AA;  61828 MW;  367528AC914287E1 CRC64;
     MSAATQSPMM QMASGNGASD RDPLPPGWEI KIDPQTGWPF FVDHNSRTTT WNDPRVPPEG
     PKDTASSANG PSRNGSRLLP IREGHPIYPQ LRPGYIPIPV LHEGSENRQP HLFHAYSQPG
     VQRFRTEAAA ATPQRSQSPL RGGMTEAAQT DKQCGQMPAT ATTAAAQPPT AHGPERSQSP
     AASDCSSSSS SASLPSSGRS SLGSHQLPRG YIPIPVIHEQ NITRPAAQPS FHQAQKTHYP
     AQQGEYQPQQ PVYHKIQGDD WEPRPLRAAS PFRSPVRGAS SREGSPARSG TPVHCPSPIR
     VHTVVDRPQP MTHREPPPVT QPENKPESKP GPAGPDLPPG HIPIQVIRRE ADSKPVSQKS
     PPPAEKVEVK VSSAPIPCPS PSPAPSAVPS PPKNVAAEQK AAPSPAPAEP AAPKSGEAET
     PPKHPGVLKV EAILEKVQGL EQAVDSFEGK KTDKKYLMIE EYLTKELLAL DSVDPEGRAD
     VRQARRDGVR KVQTILEKLE QKAIDVPGQV QVYELQPSNL EAEQPLPEIM GAVVADKDKK
     GPENKDPQTE SQQLEAKAAT PPNPSNPADS AGNLVAP
//
ID   CUL3_MOUSE              Reviewed;         768 AA.
AC   Q9JLV5;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Cullin-3;
DE            Short=CUL-3;
GN   Name=Cul3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Levy N., Agulnik A.I., Boettger-Tong H., Bishop C.E.;
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   SUBCELLULAR LOCATION, INTERACTION WITH CYCE, AND TISSUE SPECIFICITY.
RX   MEDLINE=99431971; PubMed=10500095; DOI=10.1101/gad.13.18.2375;
RA   Singer J.D., Gurian-West M., Clurman B., Roberts J.M.;
RT   "Cullin-3 targets cyclin E for ubiquitination and controls S phase in
RT   mammalian cells.";
RL   Genes Dev. 13:2375-2387(1999).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [5]
RP   STRUCTURE BY NMR OF 678-768.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the cullin-3 homologue.";
RL   Submitted (OCT-2003) to the PDB data bank.
CC   -!- FUNCTION: Core component of multiple cullin-RING-based BCR (BTB-
CC       CUL3-RBX1) E3 ubiquitin-protein ligase complexes which mediate the
CC       ubiquitination and subsequent proteasomal degradation of target
CC       proteins. As a scaffold protein may contribute to catalysis
CC       through positioning of the substrate and the ubiquitin-conjugating
CC       enzyme. The E3 ubiquitin-protein ligase activity of the complex is
CC       dependent on the neddylation of the cullin subunit and is
CC       inhibited by the association of the deneddylated cullin subunit
CC       with TIP120A/CAND1 (By similarity). The functional specificity of
CC       the BCR complex depends on the BTB domain-containing protein as
CC       the susbstrate recognition component. BCR(SPOP) is involved in
CC       ubiquitination of BMI1/PCGF4, H2AFY and DAXX, and probably GLI2 or
CC       GLI3. BCR(KLHL9-KLHL13) controls the dynamic behavior of AURKB on
CC       mitotic chromosomes and thereby coordinates faithful mitotic
CC       progression and completion of cytokinesis. Involved in
CC       ubiquitination of cyclin E and of cyclin D1 (in vitro) thus
CC       involved in regulation of G1/S transition (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Forms neddylation-dependent homodimers. Component of
CC       multiple BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes
CC       formed of CUL3, RBX1 and a variable BTB domain-containing protein
CC       acting as both, asapter to cullin and substrate recognition
CC       subunit. The BCR complex may be active as a heterodimeric complex,
CC       in which NEDD8, covalently attached to one CUL3 molecule, binds to
CC       the C-terminus of a second CUL3 molecule. Interacts with RBX1,
CC       RNF7, CYCE and TIP120A/CAND1. Part of the BCR(SPOP) containing
CC       SPOP. Part of the probable BCR(KLHL9-KLHL13) complex with BTB
CC       domain proteins KLHL9 and KLHL13. Part of the BCR(KBTBD10) complex
CC       containing KBTBD10. Part of the BCR(ENC1) complex containing ENC1.
CC       Part of a complex consisting of BMI1/PCGF4, CUL3 and SPOP. Part of
CC       a complex consisting of H2AFY, CUL3 and SPOP. Interacts with
CC       KCTD5, KLHL9, KLHL13, GAN, ZBTB16, KLHL21, KLHL3, KLHL15, KLHL20,
CC       C16orf44, GMCL1L, BTBD1. Part of a complex that contains CUL3,
CC       RBX1 and GAN. Interacts (via BTB domain) with KLHL17; the
CC       interaction regulates surface GRIK2 expression (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Golgi apparatus.
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in
CC       brain, spleen and testis.
CC   -!- PTM: Neddylated. Attachment of NEDD8 is required for the E3
CC       ubiquitin-protein ligase activity of the BCR E3 ligase complex.
CC       Deneddylated via its interaction with the COP9 signalosome (CSN)
CC       complex (By similarity).
CC   -!- MISCELLANEOUS: Null deficient mice are not viable. Extraembryonic
CC       ectoderm shows a greatly increased number of cells in S phase. In
CC       the trophectoderm cells are blocked to entry into S phase.
CC   -!- SIMILARITY: Belongs to the cullin family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF129738; AAF36500.1; -; mRNA.
DR   EMBL; BC027304; AAH27304.1; -; mRNA.
DR   IPI; IPI00467383; -.
DR   RefSeq; NP_057925.1; NM_016716.4.
DR   UniGene; Mm.12665; -.
DR   PDB; 1IUY; NMR; -; A=678-768.
DR   PDBsum; 1IUY; -.
DR   ProteinModelPortal; Q9JLV5; -.
DR   SMR; Q9JLV5; 11-768.
DR   STRING; Q9JLV5; -.
DR   PhosphoSite; Q9JLV5; -.
DR   PRIDE; Q9JLV5; -.
DR   Ensembl; ENSMUST00000004478; ENSMUSP00000004478; ENSMUSG00000004364.
DR   GeneID; 26554; -.
DR   KEGG; mmu:26554; -.
DR   UCSC; uc007brc.1; mouse.
DR   CTD; 26554; -.
DR   MGI; MGI:1347360; Cul3.
DR   GeneTree; ENSGT00550000074299; -.
DR   HOVERGEN; HBG003619; -.
DR   InParanoid; Q9JLV5; -.
DR   OMA; AKLKTEC; -.
DR   OrthoDB; EOG4JWVCW; -.
DR   PhylomeDB; Q9JLV5; -.
DR   NextBio; 304599; -.
DR   ArrayExpress; Q9JLV5; -.
DR   Bgee; Q9JLV5; -.
DR   CleanEx; MM_CUL3; -.
DR   Genevestigator; Q9JLV5; -.
DR   GermOnline; ENSMUSG00000004364; Mus musculus.
DR   GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005827; C:polar microtubule; ISS:UniProtKB.
DR   GO; GO:0030332; F:cyclin binding; IPI:MGI.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:InterPro.
DR   GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR   GO; GO:0071445; P:cellular response to protein stimulus; IDA:MGI.
DR   GO; GO:0000910; P:cytokinesis; ISS:UniProtKB.
DR   GO; GO:0007369; P:gastrulation; IMP:MGI.
DR   GO; GO:0000090; P:mitotic anaphase; ISS:UniProtKB.
DR   GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISS:UniProtKB.
DR   GO; GO:0043149; P:stress fiber assembly; ISS:UniProtKB.
DR   GO; GO:0001831; P:trophectodermal cellular morphogenesis; IMP:MGI.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IDA:MGI.
DR   InterPro; IPR016157; Cullin_CS.
DR   InterPro; IPR016158; Cullin_homology.
DR   InterPro; IPR001373; Cullin_N.
DR   InterPro; IPR019559; Cullin_neddylation_domain.
DR   InterPro; IPR016159; Cullin_repeat-like_dom.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 2.
DR   Pfam; PF00888; Cullin; 1.
DR   Pfam; PF10557; Cullin_Nedd8; 1.
DR   SMART; SM00182; CULLIN; 1.
DR   SMART; SM00884; Cullin_Nedd8; 1.
DR   SUPFAM; SSF75632; Cullin_homology; 1.
DR   SUPFAM; SSF74788; Cullin_repeat-like; 1.
DR   PROSITE; PS01256; CULLIN_1; 1.
DR   PROSITE; PS50069; CULLIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Golgi apparatus; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN         1    768       Cullin-3.
FT                                /FTId=PRO_0000119794.
FT   MOD_RES      58     58       Phosphotyrosine (By similarity).
FT   MOD_RES     450    450       Phosphoserine.
FT   MOD_RES     737    737       Phosphoserine (By similarity).
FT   CROSSLNK    712    712       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in NEDD8) (By
FT                                similarity).
FT   TURN        699    701
FT   HELIX       702    714
FT   STRAND      716    718
FT   HELIX       719    729
FT   HELIX       738    750
FT   STRAND      753    756
FT   STRAND      761    766
SQ   SEQUENCE   768 AA;  88948 MW;  841E20407BD076A3 CRC64;
     MSNLSKGTGS RKDTKMRIRA FPMTMDEKYV NSIWDLLKNA IQEIQRKNNS GLSFEELYRN
     AYTMVLHKHG EKLYTGLREV VTEHLINKVR EDVLNSLNNN FLQTLNQAWN DHQTAMVMIR
     DILMYMDRVY VQQNNVENVY NLGLIIFRDQ VVRYGCIRDH LRQTLLDMIA RERKGEVVDR
     GAIRNACQML MILGLEGRSV YEEDFEAPFL EMSAEFFQME SQKFLAENSA SVYIKKVEAR
     INEEIERVMH CLDKSTEEPI VKVVERELIS KHMKTIVEME NSGLVHMLKN GKTEDLACMY
     KLFSRVPNGL KTMCECMSCY LREQGKALVS EEGEGKNPVD YIQGLLDLKS RFDRFLQESF
     NNDRLFKQTI AGDFEYFLNL NSRSPEYLSL FIDDKLKKGV KGLTEQEVET ILDKAMVLFR
     FMQEKDVFER YYKQHLARRL LTNKSVSDDS EKNMISKLKT ECGCQFTSKL EGMFRDMSIS
     NTTMDEFRQH LQATGVSLGG VDLTVRVLTT GYWPTQSATP KCNIPPAPRH AFEIFRRFYL
     AKHSGRQLTL QHHMGSADLN ATFYGPVKKE DGSEVGVGGA QVTGSNTRKH ILQVSTFQMT
     ILMLFNNREK YTFEEIQQET DIPERELVRA LQSLACGKPT QRVLTKEPKS KEIESGHIFT
     VNDQFTSKLH RVKIQTVAAK QGESDPERKE TRQKVDDDRK HEIEAAIVRI MKSRKKMQHN
     VLVAEVTQQL KARFLPSPVV IKKRIEGLIE REYLARTPED RKVYTYVA
//
ID   NT5C_MOUSE              Reviewed;         200 AA.
AC   Q9JM14;
DT   31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=5'(3')-deoxyribonucleotidase, cytosolic type;
DE            EC=3.1.3.-;
DE   AltName: Full=Cytosolic 5',3'-pyrimidine nucleotidase;
DE   AltName: Full=Deoxy-5'-nucleotidase 1;
DE            Short=dNT-1;
GN   Name=Nt5c; Synonyms=Dnt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20148737; PubMed=10681516; DOI=10.1074/jbc.275.8.5409;
RA   Rampazzo C., Johansson M., Gallinaro L., Ferraro P., Hellman U.,
RA   Karlsson A., Reichard P., Bianchi V.;
RT   "Mammalian 5'(3')-deoxyribonucleotidase, cDNA cloning, and
RT   overexpression of the enzyme in Escherichia coli and mammalian
RT   cells.";
RL   J. Biol. Chem. 275:5409-5415(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   GENE STRUCTURE.
RX   MEDLINE=22220121; PubMed=12234672; DOI=10.1016/S0378-1119(02)00651-0;
RA   Rampazzo C., Kost-Alimova M., Ruzzenente B., Dumanski J.P.,
RA   Bianchi V.;
RT   "Mouse cytosolic and mitochondrial deoxyribonucleotidases: cDNA
RT   cloning of the mitochondrial enzyme, gene structures, chromosomal
RT   mapping and comparison with the human orthologs.";
RL   Gene 294:109-117(2002).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM
RP   IONS; 2'-DEOXYURIDINE 5'-MONOPHOSPHATE AND
RP   2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE, COFACTOR, AND SUBUNIT.
RX   PubMed=17985935; DOI=10.1021/bi7014794;
RA   Wallden K., Rinaldo-Matthis A., Ruzzenente B., Rampazzo C.,
RA   Bianchi V., Nordlund P.;
RT   "Crystal structures of human and murine deoxyribonucleotidases:
RT   insights into recognition of substrates and nucleotide analogues.";
RL   Biochemistry 46:13809-13818(2007).
CC   -!- FUNCTION: Dephosphorylates the 5' and 2'(3')-phosphates of
CC       deoxyribonucleotides, with a preference for dUMP and dTMP,
CC       intermediate activity towards dGMP, and low activity towards dCMP
CC       and dAMP.
CC   -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside
CC       + phosphate.
CC   -!- COFACTOR: Magnesium.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the 5'(3')-deoxyribonucleotidase family.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AF078840; AAF36421.1; -; mRNA.
DR   EMBL; AK007418; BAB25027.1; -; mRNA.
DR   EMBL; BC024368; AAH24368.1; -; mRNA.
DR   EMBL; BK000208; DAA00069.1; -; Genomic_DNA.
DR   IPI; IPI00124639; -.
DR   RefSeq; NP_056622.1; NM_015807.1.
DR   UniGene; Mm.390379; -.
DR   PDB; 2JAO; X-ray; 2.00 A; A=1-200.
DR   PDB; 2JAR; X-ray; 1.94 A; A=1-200.
DR   PDBsum; 2JAO; -.
DR   PDBsum; 2JAR; -.
DR   ProteinModelPortal; Q9JM14; -.
DR   SMR; Q9JM14; 4-199.
DR   STRING; Q9JM14; -.
DR   PhosphoSite; Q9JM14; -.
DR   REPRODUCTION-2DPAGE; IPI00124639; -.
DR   PRIDE; Q9JM14; -.
DR   Ensembl; ENSMUST00000021082; ENSMUSP00000021082; ENSMUSG00000020736.
DR   GeneID; 50773; -.
DR   KEGG; mmu:50773; -.
DR   UCSC; uc007mhu.1; mouse.
DR   CTD; 50773; -.
DR   MGI; MGI:1354954; Nt5c.
DR   GeneTree; ENSGT00390000011596; -.
DR   HOGENOM; HBG353930; -.
DR   HOVERGEN; HBG045599; -.
DR   InParanoid; Q9JM14; -.
DR   OMA; DTIRGQE; -.
DR   OrthoDB; EOG4DNF5C; -.
DR   PhylomeDB; Q9JM14; -.
DR   NextBio; 307701; -.
DR   ArrayExpress; Q9JM14; -.
DR   Bgee; Q9JM14; -.
DR   CleanEx; MM_NT5C; -.
DR   Genevestigator; Q9JM14; -.
DR   GermOnline; ENSMUSG00000020736; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0008253; F:5'-nucleotidase activity; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR010708; 5'(3')-deoxyribonucleotidase.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Gene3D; G3DSA:3.40.50.1000; HAD-like_dom; 1.
DR   Pfam; PF06941; NT5C; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW   Nucleotide metabolism; Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1    200       5'(3')-deoxyribonucleotidase, cytosolic
FT                                type.
FT                                /FTId=PRO_0000164372.
FT   ACT_SITE     12     12       Nucleophile (Probable).
FT   ACT_SITE     14     14       Proton donor (Probable).
FT   METAL        12     12       Magnesium.
FT   METAL        14     14       Magnesium; via carbonyl oxygen.
FT   METAL       147    147       Magnesium.
FT   BINDING      20     20       Substrate.
FT   BINDING      46     46       Substrate.
FT   BINDING      67     67       Substrate.
FT   BINDING     101    101       Substrate.
FT   BINDING     136    136       Substrate.
FT   MOD_RES     184    184       Phosphoserine (By similarity).
FT   STRAND        7     19
FT   HELIX        20     31
FT   STRAND       33     35
FT   STRAND       40     48
FT   HELIX        49     55
FT   HELIX        59     64
FT   STRAND       65     76
FT   HELIX        82     90
FT   STRAND       91    102
FT   STRAND      104    110
FT   HELIX       111    120
FT   STRAND      124    157
FT   STRAND      159    175
FT   STRAND      177    188
FT   HELIX       189    197
SQ   SEQUENCE   200 AA;  23076 MW;  5E5A3AFB0A214082 CRC64;
     MAVKRPVRVL VDMDGVLADF ESGLLQGFRR RFPEEPHVPL EQRRGFLANE QYGALRPDLA
     EKVASVYESP GFFLNLEPIP GALDALREMN DMKDTEVFIC TTPLLKYDHC VGEKYRWVEQ
     NLGPEFVERI ILTRDKTVVM GDLLIDDKDN IQGLEETPSW EHILFTCCHN QHLALPPTRR
     RLLSWSDNWR GIIESKRASL
//
ID   IRK10_MOUSE             Reviewed;         379 AA.
AC   Q9JM63;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=ATP-sensitive inward rectifier potassium channel 10;
DE   AltName: Full=Inward rectifier K(+) channel Kir4.1;
DE   AltName: Full=Potassium channel, inwardly rectifying subfamily J member 10;
GN   Name=Kcnj10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Inanobe A., Takahashi K., Tanemoto M., Fujita A., Kurachi Y.;
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CD-1, and ICR; TISSUE=Brain;
RX   MEDLINE=21100968; PubMed=11169792;
RX   DOI=10.1002/1098-1136(20010101)33:1<57::AID-GLIA1006>3.0.CO;2-0;
RA   Li L., Head V., Timpe L.C.;
RT   "Identification of an inward rectifier potassium channel gene
RT   expressed in mouse cortical astrocytes.";
RL   Glia 33:57-71(2001).
RN   [3]
RP   INTERACTION WITH INADL.
RX   MEDLINE=98313406; PubMed=9647694; DOI=10.1006/mcne.1998.0679;
RA   Kurschner C., Mermelstein P.G., Holden W.T., Surmeier D.J.;
RT   "CIPP, a novel multivalent PDZ domain protein, selectively interacts
RT   with Kir4.0 family members, NMDA receptor subunits, neurexins, and
RT   neuroligins.";
RL   Mol. Cell. Neurosci. 11:161-172(1998).
CC   -!- FUNCTION: May be responsible for potassium buffering action of
CC       glial cells in the brain. Inward rectifier potassium channels are
CC       characterized by a greater tendency to allow potassium to flow
CC       into the cell rather than out of it. Their voltage dependence is
CC       regulated by the concentration of extracellular potassium; as
CC       external potassium is raised, the voltage range of the channel
CC       opening shifts to more positive voltages. The inward rectification
CC       is mainly due to the blockage of outward current by internal
CC       magnesium. Can be blocked by extracellular barium and cesium (By
CC       similarity).
CC   -!- SUBUNIT: Seems to form heterodimer with Kir5.1/KCNJ16 (By
CC       similarity). Interacts with INADL.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the inward rectifier-type potassium channel
CC       (TC 1.A.2.1) family. KCNJ10 subfamily.
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DR   EMBL; AB039879; BAA92432.1; -; mRNA.
DR   EMBL; AF322631; AAG42845.1; -; mRNA.
DR   IPI; IPI00124792; -.
DR   RefSeq; NP_001034573.1; NM_001039484.1.
DR   UniGene; Mm.254563; -.
DR   ProteinModelPortal; Q9JM63; -.
DR   SMR; Q9JM63; 28-352.
DR   STRING; Q9JM63; -.
DR   PRIDE; Q9JM63; -.
DR   Ensembl; ENSMUST00000056136; ENSMUSP00000054356; ENSMUSG00000044708.
DR   GeneID; 16513; -.
DR   KEGG; mmu:16513; -.
DR   UCSC; uc007dqj.1; mouse.
DR   CTD; 16513; -.
DR   MGI; MGI:1194504; Kcnj10.
DR   GeneTree; ENSGT00560000076991; -.
DR   HOVERGEN; HBG006178; -.
DR   InParanoid; Q9JM63; -.
DR   OMA; LGPPANH; -.
DR   OrthoDB; EOG483D4R; -.
DR   PhylomeDB; Q9JM63; -.
DR   NextBio; 289861; -.
DR   ArrayExpress; Q9JM63; -.
DR   Bgee; Q9JM63; -.
DR   Genevestigator; Q9JM63; -.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0005887; C:integral to plasma membrane; IC:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; IMP:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0022010; P:central nervous system myelination; IMP:MGI.
DR   GO; GO:0051935; P:glutamate uptake involved in synaptic transmission; IMP:MGI.
DR   GO; GO:0055075; P:potassium ion homeostasis; IMP:MGI.
DR   GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:MGI.
DR   GO; GO:0060075; P:regulation of resting membrane potential; IMP:MGI.
DR   GO; GO:0007601; P:visual perception; IMP:MGI.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR016449; K_chnl_inward-rec_Kir.
DR   InterPro; IPR001838; K_chnl_inward-rec_Kir-like.
DR   InterPro; IPR003269; K_chnl_inward-rec_Kir1.2.
DR   InterPro; IPR013521; K_chnl_inward-rec_Kir_Cr2.
DR   InterPro; IPR013518; K_chnl_inward-rec_Kir_cyto.
DR   Gene3D; G3DSA:2.60.40.1400; IR_K+channel_cytopl; 1.
DR   PANTHER; PTHR11767; K+channel_IR; 1.
DR   PANTHER; PTHR11767:SF21; KIR12_channel; 1.
DR   Pfam; PF01007; IRK; 1.
DR   PIRSF; PIRSF005465; GIRK_kir; 1.
DR   PRINTS; PR01322; KIR12CHANNEL.
DR   PRINTS; PR01320; KIRCHANNEL.
DR   SUPFAM; SSF81296; Ig_E-set; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Ion transport; Ionic channel; Membrane;
KW   Nucleotide-binding; Potassium; Potassium transport; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    379       ATP-sensitive inward rectifier potassium
FT                                channel 10.
FT                                /FTId=PRO_0000154954.
FT   TOPO_DOM      1     64       Cytoplasmic (By similarity).
FT   TRANSMEM     65     89       Helical; Name=M1; (By similarity).
FT   TOPO_DOM     90    114       Extracellular (By similarity).
FT   INTRAMEM    115    126       Helical; Pore-forming; Name=H5; (By
FT                                similarity).
FT   INTRAMEM    127    133       Pore-forming; (By similarity).
FT   TOPO_DOM    134    142       Extracellular (By similarity).
FT   TRANSMEM    143    164       Helical; Name=M2; (By similarity).
FT   TOPO_DOM    165    379       Cytoplasmic (By similarity).
FT   NP_BIND     210    217       ATP (Potential).
FT   MOTIF       128    133       Selectivity filter (By similarity).
FT   SITE        158    158       Role in the control of polyamine-mediated
FT                                channel gating and in the blocking by
FT                                intracellular magnesium (By similarity).
SQ   SEQUENCE   379 AA;  42432 MW;  7FF08446B7F43453 CRC64;
     MTSVAKVYYS QTTQTESRPL VAPGIRRRRV LTKDGRSNVR MEHIADKRFL YLKDLWTTFI
     DMQWRYKLLL FSATFAGTWF LFGVVWYLVA VAHGDLLELG PPANHTPCVV QVHTLTGAFL
     FSLESQTTIG YGFRYISEEC PLAIVLLIAQ LVLTTILEIF ITGTFLAKIA RPKKRAETIR
     FSQHAVVASH NGKPCLMIRV ANMRKSLLIG CQVTGKLLQT HQTKEGENIR LNQVNVTFQV
     DTASDSPFLI LPLTFYHVVD ETSPLKDLPL RSGEGDFELV LILSGTVEST SATCQVRTSY
     LPEEILWGYE FTPAISLSAS GKYIADFSLF DQVVKVASPS GLRDSTVRYG DPEKLKLEES
     LREQAEKEGS ALSVRISNV
//
ID   SRF_MOUSE               Reviewed;         504 AA.
AC   Q9JM73;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Serum response factor;
DE            Short=SRF;
GN   Name=Srf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Miwa T.;
RT   "Serum response factor.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   INTERACTION WITH SRFBP1, AND SUBUNIT.
RX   PubMed=15492011; DOI=10.1074/jbc.M405945200;
RA   Zhang X., Azhar G., Zhong Y., Wei J.Y.;
RT   "Identification of a novel serum response factor cofactor in cardiac
RT   gene regulation.";
RL   J. Biol. Chem. 279:55626-55632(2004).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=15169892; DOI=10.1128/MCB.24.12.5281-5289.2004;
RA   Parlakian A., Tuil D., Hamard G., Tavernier G., Hentzen D.,
RA   Concordet J.-P., Paulin D., Li Z., Daegelen D.;
RT   "Targeted inactivation of serum response factor in the developing
RT   heart results in myocardial defects and embryonic lethality.";
RL   Mol. Cell. Biol. 24:5281-5289(2004).
RN   [5]
RP   INTERACTION WITH ARID2, AND SUBUNIT.
RX   PubMed=16782067; DOI=10.1016/j.bbrc.2006.05.211;
RA   Zhang X., Azhar G., Zhong Y., Wei J.Y.;
RT   "Zipzap/p200 is a novel zinc finger protein contributing to cardiac
RT   gene regulation.";
RL   Biochem. Biophys. Res. Commun. 346:794-801(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [8]
RP   INTERACTION WITH MKL1 AND SCAI, AND SUBCELLULAR LOCATION.
RX   PubMed=19350017; DOI=10.1038/ncb1862;
RA   Brandt D.T., Baarlink C., Kitzing T.M., Kremmer E., Ivaska J.,
RA   Nollau P., Grosse R.;
RT   "SCAI acts as a suppressor of cancer cell invasion through the
RT   transcriptional control of beta1-integrin.";
RL   Nat. Cell Biol. 11:557-568(2009).
CC   -!- FUNCTION: SRF is a transcription factor that binds to the serum
CC       response element (SRE), a short sequence of dyad symmetry located
CC       300 bp to the 5' of the site of transcription initiation of some
CC       genes (such as FOS) (By similarity). Required for cardiac
CC       differentiation and maturation.
CC   -!- SUBUNIT: Binds DNA as a multimer, probably a dimer. Interacts with
CC       MLLT7/FOXO4, NKX3A and SSRP1 (By similarity). Interacts with ARID2
CC       and SRFBP1. Forms complexes with ARID2, MYOCD, NKX2-5 and SRFBP1.
CC       Forms a nuclear ternary complex with MKL1 and SCAI.
CC   -!- INTERACTION:
CC       Q3U1N2:Srebf2; NbExp=2; IntAct=EBI-493266, EBI-645275;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- PTM: Phosphorylated by PRKDC (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice lacking Srf in cardiac tissue display
CC       lethal cardiac defects between E10.5 and E13.5 characterized by
CC       abnormally thin myocardium, dilated cardiac chambers, poor
CC       trabeculation and a disorganised interventricular septum.
CC   -!- SIMILARITY: Contains 1 MADS-box domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB038376; BAA92314.1; -; Genomic_DNA.
DR   EMBL; BC051950; AAH51950.1; -; mRNA.
DR   IPI; IPI00124827; -.
DR   RefSeq; NP_065239.1; NM_020493.2.
DR   UniGene; Mm.45044; -.
DR   ProteinModelPortal; Q9JM73; -.
DR   SMR; Q9JM73; 131-219.
DR   IntAct; Q9JM73; 5.
DR   STRING; Q9JM73; -.
DR   PhosphoSite; Q9JM73; -.
DR   PRIDE; Q9JM73; -.
DR   Ensembl; ENSMUST00000015749; ENSMUSP00000015749; ENSMUSG00000015605.
DR   GeneID; 20807; -.
DR   KEGG; mmu:20807; -.
DR   UCSC; uc008ctg.1; mouse.
DR   CTD; 20807; -.
DR   MGI; MGI:106658; Srf.
DR   eggNOG; roNOG17183; -.
DR   GeneTree; ENSGT00400000022158; -.
DR   HOGENOM; HBG714175; -.
DR   HOVERGEN; HBG014968; -.
DR   InParanoid; Q9JM73; -.
DR   OMA; QVQEPGG; -.
DR   OrthoDB; EOG48KRCZ; -.
DR   PhylomeDB; Q9JM73; -.
DR   NextBio; 299523; -.
DR   ArrayExpress; Q9JM73; -.
DR   Bgee; Q9JM73; -.
DR   CleanEx; MM_SRF; -.
DR   Genevestigator; Q9JM73; -.
DR   GermOnline; ENSMUSG00000015605; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0010736; F:serum response element binding; IDA:MGI.
DR   GO; GO:0007015; P:actin filament organization; IMP:MGI.
DR   GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; IMP:MGI.
DR   GO; GO:0048589; P:developmental growth; IMP:MGI.
DR   GO; GO:0001947; P:heart looping; IMP:MGI.
DR   GO; GO:0001707; P:mesoderm formation; IMP:MGI.
DR   GO; GO:0046716; P:muscle cell homeostasis; IMP:MGI.
DR   GO; GO:0001569; P:patterning of blood vessels; IMP:MGI.
DR   GO; GO:0051491; P:positive regulation of filopodium assembly; IMP:MGI.
DR   GO; GO:0090009; P:primitive streak formation; IMP:MGI.
DR   GO; GO:0030155; P:regulation of cell adhesion; IMP:MGI.
DR   InterPro; IPR002100; TF_MADSbox.
DR   Pfam; PF00319; SRF-TF; 1.
DR   PRINTS; PR00404; MADSDOMAIN.
DR   SMART; SM00432; MADS; 1.
DR   SUPFAM; SSF55455; TF_MADSbox; 1.
DR   PROSITE; PS00350; MADS_BOX_1; 1.
DR   PROSITE; PS50066; MADS_BOX_2; 1.
PE   1: Evidence at protein level;
KW   Activator; Developmental protein; DNA-binding; Glycoprotein; Nucleus;
KW   Phosphoprotein; Transcription; Transcription regulation.
FT   CHAIN         1    504       Serum response factor.
FT                                /FTId=PRO_0000245225.
FT   DOMAIN      137    197       MADS-box.
FT   DNA_BIND    129    218       By similarity.
FT   REGION      164    218       Involved in dimerization (By similarity).
FT   COMPBIAS     13    138       Gly-rich.
FT   COMPBIAS     76     86       Asp/Glu-rich (acidic).
FT   COMPBIAS    238    254       Asp/Glu-rich (acidic).
FT   MOD_RES      72     72       Phosphotyrosine (By similarity).
FT   MOD_RES      73     73       Phosphoserine (By similarity).
FT   MOD_RES      75     75       Phosphoserine (By similarity).
FT   MOD_RES      79     79       Phosphoserine (By similarity).
FT   MOD_RES      81     81       Phosphoserine (By similarity).
FT   MOD_RES      99     99       Phosphoserine (By similarity).
FT   MOD_RES     220    220       Phosphoserine.
FT   MOD_RES     249    249       Phosphoserine (By similarity).
FT   MOD_RES     431    431       Phosphoserine; by dsDNA kinase (By
FT                                similarity).
FT   MOD_RES     442    442       Phosphoserine; by dsDNA kinase (By
FT                                similarity).
FT   CARBOHYD    273    273       O-linked (GlcNAc) (By similarity).
FT   CARBOHYD    303    303       O-linked (GlcNAc) (By similarity).
FT   CARBOHYD    305    305       O-linked (GlcNAc) (By similarity).
FT   CARBOHYD    312    312       O-linked (GlcNAc) (By similarity).
FT   CARBOHYD    379    379       O-linked (GlcNAc) (By similarity).
SQ   SEQUENCE   504 AA;  51247 MW;  26353F18A2B46F6B CRC64;
     MLPSQAGAAA ALGRGSALGG NLNRTPTGRP GGGGGTRGAN GGRVPGNGAG LGQSRLEREA
     AAAAAPTAGA LYSGSEGDSE SGEEEELGAE RRGLKRSLSE MELGVVVGGP EAAAAAAGGY
     GPVSGAVSGA KPGKKTRGRV KIKMEFIDNK LRRYTTFSKR KTGIMKKAYE LSTLTGTQVL
     LLVASETGHV YTFATRKLQP MITSETGKAL IQTCLNSPDS PPRSDPTTDQ RMSATGFEEP
     DLTYQVSESD SSGETKDTLK PAFTVTNLPG TTSTIQTAPS TSTTMQVSSG PSFPITNYLA
     PVSASVSPSA VSSANGTVLK STGSGPVSSG GLMQLPTSFT LMPGGAVAQQ VPVQAIHVHQ
     APQQASPSRD SSTDLTQTSS SGTVTLPATI MTSSVPTTVG GHMMYPSPHA VMYAPTSGLA
     DGSLTVLNAF SQAPSTMQVS HSQVQEPGGV PQVFLTAPSG TVQIPVSAVQ LHQMAVIGQQ
     AGSSSNLTEL QVVNLDATHS TKSE
//
ID   BORG4_MOUSE             Reviewed;         349 AA.
AC   Q9JM96; Q3TNF3; Q9QZT8;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Cdc42 effector protein 4;
DE   AltName: Full=Binder of Rho GTPases 4;
GN   Name=Cdc42ep4; Synonyms=Borg4, Cep4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Ileal mucosa;
RX   MEDLINE=21036164; PubMed=11185749; DOI=10.1007/s100380070012;
RA   Osada N., Kusuda J., Suzuki Y., Sugano S., Hashimoto K.;
RT   "Sequence analysis, gene expression, and chromosomal assignment of
RT   mouse Borg4 gene and its human orthologue.";
RL   J. Hum. Genet. 45:374-377(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-143, AND INTERACTION WITH RHOQ AND
RP   CDC42.
RX   MEDLINE=99421943; PubMed=10490598;
RA   Joberty G., Perlungher R.R., Macara I.G.;
RT   "The Borgs, a new family of Cdc42 and TC10 GTPase-interacting
RT   proteins.";
RL   Mol. Cell. Biol. 19:6585-6597(1999).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64 AND SER-223, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-107 AND SER-223,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-139 AND SER-154, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Probably involved in the organization of the actin
CC       cytoskeleton. May act downstream of CDC42 to induce actin filament
CC       assembly leading to cell shape changes. Induces pseudopodia
CC       formation, when overexpressed in fibroblasts.
CC   -!- SUBUNIT: Interacts with CDC42 and RHOQ, in a GTP-dependent manner.
CC   -!- SUBCELLULAR LOCATION: Endomembrane system; Peripheral membrane
CC       protein (By similarity). Cytoplasm, cytoskeleton (By similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the BORG/CEP family.
CC   -!- SIMILARITY: Contains 1 CRIB domain.
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DR   EMBL; AB035088; BAA95932.1; -; mRNA.
DR   EMBL; AK075739; BAC35920.1; -; mRNA.
DR   EMBL; AK165318; BAE38136.1; -; mRNA.
DR   EMBL; BC003857; AAH03857.1; -; mRNA.
DR   EMBL; AF165114; AAD47822.1; -; mRNA.
DR   IPI; IPI00124906; -.
DR   RefSeq; NP_001156818.1; NM_001163346.1.
DR   RefSeq; NP_064390.1; NM_020006.2.
DR   UniGene; Mm.293378; -.
DR   ProteinModelPortal; Q9JM96; -.
DR   MINT; MINT-1342086; -.
DR   STRING; Q9JM96; -.
DR   PhosphoSite; Q9JM96; -.
DR   PRIDE; Q9JM96; -.
DR   Ensembl; ENSMUST00000053536; ENSMUSP00000060227; ENSMUSG00000041598.
DR   Ensembl; ENSMUST00000106616; ENSMUSP00000102227; ENSMUSG00000041598.
DR   GeneID; 56699; -.
DR   KEGG; mmu:56699; -.
DR   UCSC; uc007mfb.1; mouse.
DR   CTD; 56699; -.
DR   MGI; MGI:1929760; Cdc42ep4.
DR   GeneTree; ENSGT00530000063054; -.
DR   HOGENOM; HBG714096; -.
DR   HOVERGEN; HBG052803; -.
DR   InParanoid; Q9JM96; -.
DR   OMA; SIMDKEE; -.
DR   OrthoDB; EOG4WWRKP; -.
DR   PhylomeDB; Q9JM96; -.
DR   NextBio; 313139; -.
DR   ArrayExpress; Q9JM96; -.
DR   Bgee; Q9JM96; -.
DR   CleanEx; MM_CDC42EP4; -.
DR   Genevestigator; Q9JM96; -.
DR   GermOnline; ENSMUSG00000041598; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0007266; P:Rho protein signal transduction; IDA:MGI.
DR   InterPro; IPR000095; PAK_box_Rho-bd.
DR   Pfam; PF00786; PBD; 1.
DR   PROSITE; PS50108; CRIB; 1.
PE   1: Evidence at protein level;
KW   Cell shape; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein.
FT   CHAIN         1    349       Cdc42 effector protein 4.
FT                                /FTId=PRO_0000212656.
FT   DOMAIN       27     41       CRIB.
FT   MOD_RES      64     64       Phosphoserine.
FT   MOD_RES     107    107       Phosphoserine.
FT   MOD_RES     136    136       Phosphoserine (By similarity).
FT   MOD_RES     139    139       Phosphoserine.
FT   MOD_RES     140    140       Phosphoserine (By similarity).
FT   MOD_RES     154    154       Phosphoserine.
FT   MOD_RES     165    165       Phosphoserine (By similarity).
FT   MOD_RES     223    223       Phosphoserine.
FT   MOD_RES     285    285       Phosphoserine (By similarity).
FT   MOD_RES     288    288       Phosphoserine (By similarity).
FT   CONFLICT    143    143       K -> R (in Ref. 4; AAD47822).
SQ   SEQUENCE   349 AA;  37869 MW;  7C44125A7083E16B CRC64;
     MPILKQLVSS SVNSKRRSRA DLTAEMISAP LGDFRHTMHV GRAGDAFGDT SFLTSKAREA
     DDESLDEQAS ASKLSLLSRK FRGSKRSQSV TRGDREQRDM LGSLRDSALF VKNAMSLPQL
     NEKEAAEKDS SKLPKSLSSS PVKKADARDG GPKSPHRNGA TGPHSPDPLL DEQAFGDLMD
     LPIMPKVSYG LKHAESILSF HIDLGPSMLG DVLSIMDKDQ WGSEEEEEAG GYRDKEGPSS
     IVQAPPVLEV VPPLGRQESK ASWDQASMLP PHAVEDDGWA VVAPSPSSAR SVGSHTTRDS
     SSLSSYTSGV LEERSPAFRG PDRVAAAPPR QPDKEFCFMD EEEEDEIRV
//
ID   UBP14_MOUSE             Reviewed;         493 AA.
AC   Q9JMA1; Q543U5; Q923F2; Q9D0L0;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 14;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 14;
DE   AltName: Full=Ubiquitin thiolesterase 14;
DE   AltName: Full=Ubiquitin-specific-processing protease 14;
GN   Name=Usp14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Hidaka T., Morishita T.;
RT   "Mouse deubiquitinating enzyme-type TGT.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, Embryo, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION, AND ASSOCIATION WITH THE 26S PROTEASOME.
RX   PubMed=11566882; DOI=10.1093/emboj/20.18.5187;
RA   Borodovsky A., Kessler B.M., Casagrande R., Overkleeft H.S.,
RA   Wilkinson K.D., Ploegh H.L.;
RT   "A novel active site-directed probe specific for deubiquitylating
RT   enzymes reveals proteasome association of USP14.";
RL   EMBO J. 20:5187-5196(2001).
RN   [5]
RP   FUNCTION, AND ASSOCIATION WITH THE 26S PROTEASOME.
RX   PubMed=16190881; DOI=10.1111/j.1471-4159.2005.03409.x;
RA   Anderson C., Crimmins S., Wilson J.A., Korbel G.A., Ploegh H.L.,
RA   Wilson S.M.;
RT   "Loss of Usp14 results in reduced levels of ubiquitin in ataxia
RT   mice.";
RL   J. Neurochem. 95:724-731(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-136; SER-143 AND
RP   SER-222, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   FUNCTION.
RX   PubMed=19726649; DOI=10.1523/JNEUROSCI.2635-09.2009;
RA   Chen P.C., Qin L.N., Li X.M., Walters B.J., Wilson J.A., Mei L.,
RA   Wilson S.M.;
RT   "The proteasome-associated deubiquitinating enzyme Usp14 is essential
RT   for the maintenance of synaptic ubiquitin levels and the development
RT   of neuromuscular junctions.";
RL   J. Neurosci. 29:10909-10919(2009).
RN   [8]
RP   STRUCTURE BY NMR OF 4-86.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the N-terminal ubiquitin-like domain of mouse
RT   ubiquitin specific protease 14 (usp14).";
RL   Submitted (NOV-2004) to the PDB data bank.
CC   -!- FUNCTION: Proteasome-associated deubiquitinase which releases
CC       ubiquitin from the proteasome targeted ubiquitinated proteins.
CC       Ensures the regeneration of ubiquitin at the proteasome. Maintains
CC       the cellular levels of monomeric ubiquitin in cells. Indispensable
CC       for synaptic development and function at neuromuscular junctions
CC       (NMJs). Is a reversibly associated subunit of the proteasome and a
CC       large fraction of proteasome-free protein exists within the cell.
CC       Required for the degradation of the chemokine receptor cxcr4 which
CC       is critical for CXCL12-induced cell chemotaxis. Serves also as a
CC       physiological inhibitor of endoplasmic reticulum-associated
CC       degradation (ERAD) under the non-stressed condition by inhibiting
CC       the degradation of unfolded endoplasmic reticulum proteins via
CC       interaction with ERN1.
CC   -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- SUBUNIT: Homodimer (Potential). Interacts with FANCC, CXCR4 and
CC       ERN1 (By similarity). Associates with the 26S proteasome.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cell membrane;
CC       Peripheral membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. USP14/UBP6
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB034633; BAA93551.1; -; mRNA.
DR   EMBL; AK011322; BAB27544.1; -; mRNA.
DR   EMBL; AK029977; BAC26713.1; -; mRNA.
DR   EMBL; AK045909; BAC32528.1; -; mRNA.
DR   EMBL; BC005571; AAH05571.1; -; mRNA.
DR   IPI; IPI00270877; -.
DR   RefSeq; NP_067497.2; NM_021522.4.
DR   UniGene; Mm.329277; -.
DR   UniGene; Mm.447089; -.
DR   PDB; 1WGG; NMR; -; A=4-85.
DR   PDBsum; 1WGG; -.
DR   ProteinModelPortal; Q9JMA1; -.
DR   SMR; Q9JMA1; 6-86, 98-482.
DR   STRING; Q9JMA1; -.
DR   MEROPS; C19.015; -.
DR   PhosphoSite; Q9JMA1; -.
DR   PRIDE; Q9JMA1; -.
DR   Ensembl; ENSMUST00000092096; ENSMUSP00000089728; ENSMUSG00000047879.
DR   GeneID; 59025; -.
DR   KEGG; mmu:59025; -.
DR   UCSC; uc008ean.1; mouse.
DR   CTD; 59025; -.
DR   MGI; MGI:1928898; Usp14.
DR   GeneTree; ENSGT00390000009615; -.
DR   HOVERGEN; HBG054185; -.
DR   OMA; YGPRRIE; -.
DR   OrthoDB; EOG4JT05C; -.
DR   PhylomeDB; Q9JMA1; -.
DR   BRENDA; 3.1.2.15; 244.
DR   NextBio; 314596; -.
DR   ArrayExpress; Q9JMA1; -.
DR   Bgee; Q9JMA1; -.
DR   CleanEx; MM_USP14; -.
DR   Genevestigator; Q9JMA1; -.
DR   GermOnline; ENSMUSG00000047879; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0005625; C:soluble fraction; IDA:MGI.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IEA:EC.
DR   GO; GO:0007268; P:synaptic transmission; IMP:MGI.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19.
DR   InterPro; IPR000626; Ubiquitin.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019955; Ubiquitin_supergroup.
DR   Pfam; PF00443; UCH; 1.
DR   SMART; SM00213; UBQ; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; 1.
DR   PROSITE; PS50235; UCH_2_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell membrane; Cytoplasm; Hydrolase;
KW   Membrane; Phosphoprotein; Protease; Proteasome; Thiol protease;
KW   Ubl conjugation pathway.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    493       Ubiquitin carboxyl-terminal hydrolase 14.
FT                                /FTId=PRO_0000080637.
FT   DOMAIN        4     80       Ubiquitin-like.
FT   ACT_SITE    114    114       Nucleophile (By similarity).
FT   ACT_SITE    434    434       Proton acceptor (By similarity).
FT   MOD_RES     136    136       Phosphotyrosine.
FT   MOD_RES     143    143       Phosphoserine.
FT   MOD_RES     222    222       Phosphoserine.
FT   MOD_RES     291    291       N6-acetyllysine (By similarity).
FT   MOD_RES     313    313       N6-acetyllysine (By similarity).
FT   MOD_RES     448    448       N6-acetyllysine (By similarity).
FT   CONFLICT    185    185       Q -> R (in Ref. 1; BAA93551).
FT   CONFLICT    310    310       L -> S (in Ref. 1; BAA93551).
FT   CONFLICT    385    385       Q -> E (in Ref. 2; BAB27544).
FT   STRAND        4     10
FT   STRAND       13     24
FT   HELIX        26     36
FT   TURN         41     43
FT   STRAND       68     70
SQ   SEQUENCE   493 AA;  56002 MW;  4E5F5DCB86057FF9 CRC64;
     MPLYSVTVKW GKEKFEGVEL NTDEPPMVFK AQLFALTGVQ PARQKVMVKG GTLKDDDWGN
     IKMKNGMTVL MMGSADALPE EPSAKTVFVE DMTEEQLATA MELPCGLTNL GNTCYMNATV
     QCIRSVPELK DALKRYAGAL RASGEMASAQ YITAALRDLF DSMDKTSSSI PPIILLQFLH
     MAFPQFAEKG EQGQYLQQDA NECWIQMMRV LQQKLEAIED DSGRETDSSS APAVTPSKKK
     SLIDQYFGVE FETTMKCTES EEEEVTKGKE NQLQLSCFIN QEVKYLFTGL KLRLQEEITK
     QSPTLQRNAL YIKSSKISRL PAYLTIQMVR FFYKEKESVN AKVLKDVKFP LMLDVYELCT
     PELQEKMVSF RSKFKDLEDK KVNQQPNAND KNSPPKEIKY EPFSFADDIG SNNCGYYDLQ
     AVLTHQGRSS SSGHYVSWVR RKQDEWIKFD DDKVSIVTPE DILRLSGGGD WHIAYVLLYG
     PRRVEIMEEE SEQ
//
ID   TGT_MOUSE               Reviewed;         403 AA.
AC   Q9JMA2; Q80VS3;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Queuine tRNA-ribosyltransferase;
DE            EC=2.4.2.29;
DE   AltName: Full=Guanine insertion enzyme;
DE   AltName: Full=tRNA-guanine transglycosylase;
GN   Name=Qtrt1; Synonyms=Tgt, Tgut;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 17-403.
RC   TISSUE=Brain;
RA   Morishita T., Hidaka T.;
RT   "Another gene for tRNA-guanine transglycosylase in mammals.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH QTRTD1, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=19414587; DOI=10.1074/jbc.M109.002477;
RA   Boland C., Hayes P., Santa-Maria I., Nishimura S., Kelly V.P.;
RT   "Queuosine formation in eukaryotic tRNA occurs via a mitochondria-
RT   localized heteromeric transglycosylase.";
RL   J. Biol. Chem. 284:18218-18227(2009).
CC   -!- FUNCTION: Interacts with QTRTD1 to form an active queuine tRNA-
CC       ribosyltransferase. This enzyme exchanges queuine for the guanine
CC       at the wobble position of tRNAs with GU(N) anticodons (tRNA-Asp,
CC       -Asn, -His and -Tyr), thereby forming the hypermodified nucleoside
CC       queuosine (Q) (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-
CC       yl)amino)methyl)-7-deazaguanosine).
CC   -!- CATALYTIC ACTIVITY: [tRNA]-guanine + queuine = [tRNA]-queuine +
CC       guanine.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC   -!- SUBUNIT: Interacts with QTRTD1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion. Nucleus.
CC       Note=Weakly associates with mitochondria, possibly via QTRTD1.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver,
CC       ling, skeletal muscle, spleen and testis.
CC   -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB27717.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=BAB27717.1; Type=Frameshift; Positions=6;
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DR   EMBL; AK011586; BAB27717.1; ALT_SEQ; mRNA.
DR   EMBL; BC044811; AAH44811.1; -; mRNA.
DR   EMBL; AB034632; BAA93550.1; -; mRNA.
DR   IPI; IPI00125326; -.
DR   RefSeq; NP_068688.2; NM_021888.2.
DR   UniGene; Mm.436579; -.
DR   ProteinModelPortal; Q9JMA2; -.
DR   SMR; Q9JMA2; 15-381.
DR   STRING; Q9JMA2; -.
DR   PhosphoSite; Q9JMA2; -.
DR   PRIDE; Q9JMA2; -.
DR   Ensembl; ENSMUST00000002902; ENSMUSP00000002902; ENSMUSG00000002825.
DR   GeneID; 60507; -.
DR   KEGG; mmu:60507; -.
DR   UCSC; uc009oli.1; mouse.
DR   CTD; 60507; -.
DR   MGI; MGI:1931441; Qtrt1.
DR   GeneTree; ENSGT00530000063679; -.
DR   HOGENOM; HBG629929; -.
DR   HOVERGEN; HBG101131; -.
DR   InParanoid; Q9JMA2; -.
DR   OMA; RCIAAHK; -.
DR   OrthoDB; EOG4THVT7; -.
DR   BRENDA; 2.4.2.29; 244.
DR   NextBio; 314913; -.
DR   ArrayExpress; Q9JMA2; -.
DR   Bgee; Q9JMA2; -.
DR   CleanEx; MM_QTRT1; -.
DR   Genevestigator; Q9JMA2; -.
DR   GermOnline; ENSMUSG00000002825; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:EC.
DR   GO; GO:0008616; P:queuosine biosynthetic process; IDA:UniProtKB.
DR   InterPro; IPR004803; Queuine_tRNA-ribosylTrfase.
DR   InterPro; IPR002616; tRNA_ribo_trans.
DR   Gene3D; G3DSA:3.20.20.105; tRNA_ribo_trans; 1.
DR   PANTHER; PTHR11962; tRNA_ribo_trans; 1.
DR   Pfam; PF01702; TGT; 1.
DR   SUPFAM; SSF51713; tRNA_ribo_trans; 1.
DR   TIGRFAMs; TIGR00430; Q_tRNA_tgt; 1.
DR   TIGRFAMs; TIGR00449; tgt_general; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Glycosyltransferase; Metal-binding; Mitochondrion; Nucleus;
KW   Queuosine biosynthesis; Transferase; tRNA processing; Zinc.
FT   CHAIN         1    403       Queuine tRNA-ribosyltransferase.
FT                                /FTId=PRO_0000135566.
FT   ACT_SITE    279    279       Nucleophile (By similarity).
FT   METAL       317    317       Zinc (By similarity).
FT   METAL       319    319       Zinc (By similarity).
FT   METAL       322    322       Zinc (By similarity).
FT   METAL       348    348       Zinc (By similarity).
FT   BINDING     106    106       Substrate (By similarity).
SQ   SEQUENCE   403 AA;  44093 MW;  DC514C9E384314AD CRC64;
     MAAVGSPGSL ESAPRIMRLV AECSRSGARA GELRLPHGTV ATPVFMPVGT QATMKGITTE
     QLDSLGCRIC LGNTYHLGLR PGPELIRKAQ GLHGFMNWPH NLLTDSGGFQ MVSLFSLSEV
     TEEGVHFRSP YDGEETLLSP ERSVEIQNAL GSDIIMQLDH VVSSTVTGPL VEEAMHRSVR
     WLDRCIAAHK HPDKQNLFAI IQGGLNADLR TTCLKEMTKR DVPGFAIGGL SGGESKAQFW
     KMVALSTSML PKDKPRYLMG VGYATDLVVC VALGCDMFDC VYPTRTARFG SALVPTGNLQ
     LKKKQYAKDF SPINPECPCP TCQTHSRAFL HALLHSDNTT ALHHLTVHNI AYQLQLLSAV
     RSSILEQRFP DFVRNFMRTM YGDHSLCPAW AVEALASVGI MLT
//
ID   DNJA4_MOUSE             Reviewed;         397 AA.
AC   Q9JMC3; B2RW09; Q543S9; Q9CTD6; Q9CUD4;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=DnaJ homolog subfamily A member 4;
DE   AltName: Full=MmDjA4;
DE   Flags: Precursor;
GN   Name=Dnaja4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CD-1;
RX   MEDLINE=20435298; PubMed=10978524; DOI=10.1016/S0167-4781(00)00136-6;
RA   Hata M., Ohtsuka K.;
RT   "Murine cDNA encoding a novel type I HSP40/DNAJ homolog, mmDjA4.";
RL   Biochim. Biophys. Acta 1493:208-210(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain, Corpora quadrigemina, Embryo, Spinal ganglion, and
RC   Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor (Potential).
CC   -!- TISSUE SPECIFICITY: Specifically expressed in testis and heart.
CC   -!- SIMILARITY: Contains 1 CR-type zinc finger.
CC   -!- SIMILARITY: Contains 1 J domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB30367.2; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AB032401; BAA92775.1; -; mRNA.
DR   EMBL; AK003903; BAB23067.1; -; mRNA.
DR   EMBL; AK016666; BAB30367.2; ALT_INIT; mRNA.
DR   EMBL; AK046476; BAC32747.1; -; mRNA.
DR   EMBL; AK076175; BAC36232.1; -; mRNA.
DR   EMBL; AK141909; BAE24880.1; -; mRNA.
DR   EMBL; BC147484; AAI47485.1; -; mRNA.
DR   EMBL; BC147486; AAI47487.1; -; mRNA.
DR   IPI; IPI00125454; -.
DR   RefSeq; NP_067397.1; NM_021422.4.
DR   UniGene; Mm.28437; -.
DR   ProteinModelPortal; Q9JMC3; -.
DR   SMR; Q9JMC3; 3-68, 102-370.
DR   STRING; Q9JMC3; -.
DR   PhosphoSite; Q9JMC3; -.
DR   REPRODUCTION-2DPAGE; Q9JMC3; -.
DR   PRIDE; Q9JMC3; -.
DR   Ensembl; ENSMUST00000070070; ENSMUSP00000070413; ENSMUSG00000032285.
DR   Ensembl; ENSMUST00000120452; ENSMUSP00000112520; ENSMUSG00000032285.
DR   GeneID; 58233; -.
DR   KEGG; mmu:58233; -.
DR   UCSC; uc009prk.1; mouse.
DR   CTD; 58233; -.
DR   MGI; MGI:1927638; Dnaja4.
DR   eggNOG; roNOG13985; -.
DR   GeneTree; ENSGT00490000043321; -.
DR   HOGENOM; HBG635315; -.
DR   HOVERGEN; HBG066727; -.
DR   InParanoid; Q9JMC3; -.
DR   OMA; VIFPEKH; -.
DR   OrthoDB; EOG4RJG1R; -.
DR   PhylomeDB; Q9JMC3; -.
DR   NextBio; 314261; -.
DR   ArrayExpress; Q9JMC3; -.
DR   Bgee; Q9JMC3; -.
DR   CleanEx; MM_DNAJA4; -.
DR   Genevestigator; Q9JMC3; -.
DR   GermOnline; ENSMUSG00000032285; Mus musculus.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0009408; P:response to heat; IEA:InterPro.
DR   InterPro; IPR012724; DnaJ.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_N.
DR   InterPro; IPR018253; Heat_shock_DnaJ_CS.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR003095; Hsp_DnaJ.
DR   InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR   Gene3D; G3DSA:1.10.287.110; DnaJ_N; 1.
DR   Gene3D; G3DSA:2.10.230.10; HSP_DnaJ_cys-rich; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; DnaJ_N; 1.
DR   SUPFAM; SSF49493; HSP40_DnaJ_pep; 2.
DR   SUPFAM; SSF57938; HSP_DnaJ_cys-rich; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51188; ZF_CR; 1.
PE   2: Evidence at transcript level;
KW   Chaperone; Lipoprotein; Membrane; Metal-binding; Methylation;
KW   Prenylation; Repeat; Zinc; Zinc-finger.
FT   CHAIN         1    394       DnaJ homolog subfamily A member 4.
FT                                /FTId=PRO_0000071015.
FT   PROPEP      395    397       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000396761.
FT   DOMAIN        4     70       J.
FT   REPEAT      135    142       CXXCXGXG motif.
FT   REPEAT      151    158       CXXCXGXG motif.
FT   REPEAT      178    185       CXXCXGXG motif.
FT   REPEAT      194    201       CXXCXGXG motif.
FT   ZN_FING     122    206       CR-type.
FT   COMPBIAS     75     96       Gly-rich.
FT   METAL       135    135       Zinc 1 (By similarity).
FT   METAL       138    138       Zinc 1 (By similarity).
FT   METAL       151    151       Zinc 2 (By similarity).
FT   METAL       154    154       Zinc 2 (By similarity).
FT   METAL       178    178       Zinc 2 (By similarity).
FT   METAL       181    181       Zinc 2 (By similarity).
FT   METAL       194    194       Zinc 1 (By similarity).
FT   METAL       197    197       Zinc 1 (By similarity).
FT   MOD_RES     394    394       Cysteine methyl ester (By similarity).
FT   LIPID       394    394       S-farnesyl cysteine (By similarity).
SQ   SEQUENCE   397 AA;  44902 MW;  EF47E79FADDD9055 CRC64;
     MVKETQYYDI LGVKPSASPE EIKKAYRKLA LKYHPDKNPD EGEKFKLISQ AYEVLSDPKK
     RDIYDQGGEQ AIKEGGSGSP SFSSPMDIFD MFFGGGGRMT RERRGKNVVH QLSVTLEDLY
     NGITKKLALQ KNVICEKCEG IGGKKGSVEK CPLCKGRGMQ VHIQQIGPGM VQQIQTVCIE
     CKGQGERINP KDRCENCSGA KVTREKKIIE VHVEKGMKDG QKILFHGEGD QEPELDPGDV
     IIVLDQKDHS VFQRRGQDLI MKMKIQLSEA LCGFKKTIKT LDDRVLVISS KSGEVIKHGD
     LKCIRNEGMP IYKAPLEKGV MIIQFLVVFP EKQWLSQEKL PQLEALLPPR QKVRITDDMD
     QVELKEFNPN EQSWRQHREA YEEDDEEPRA GVQCQTA
//
ID   AP3B2_MOUSE             Reviewed;        1082 AA.
AC   Q9JME5; B2RTK2; Q3UYP8; Q6QR53; Q8R1E5;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 2.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=AP-3 complex subunit beta-2;
DE   AltName: Full=Adapter-related protein complex 3 subunit beta-2;
DE   AltName: Full=Adaptor protein complex AP-3 subunit beta-2;
DE   AltName: Full=Beta-3B-adaptin;
DE   AltName: Full=Clathrin assembly protein complex 3 beta-2 large chain;
GN   Name=Ap3b2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Seong E., Burmeister M.;
RT   "Ap3b2, a neuron specific subunit of adaptor protein complex 3 (AP-
RT   3).";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-738.
RC   STRAIN=C57BL/6J; TISSUE=Embryonic head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 608-1082.
RC   TISSUE=Brain;
RX   MEDLINE=20145471; PubMed=10679242; DOI=10.1006/bbrc.2000.2170;
RA   Inoue S., Sano H., Ohta M.;
RT   "Growth suppression of Escherichia coli by induction of expression of
RT   mammalian genes with transmembrane or ATPase domains.";
RL   Biochem. Biophys. Res. Commun. 268:553-561(2000).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272 AND SER-282, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Subunit of non-clathrin- and clathrin-associated adaptor
CC       protein complex 3 that plays a role in protein sorting in the
CC       late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP
CC       complexes mediate both the recruitment of clathrin to membranes
CC       and the recognition of sorting signals within the cytosolic tails
CC       of transmembrane cargo molecules. AP-3 appears to be involved in
CC       the sorting of a subset of transmembrane proteins targeted to
CC       lysosomes and lysosome-related organelles (By similarity).
CC   -!- SUBUNIT: Adaptor protein complex 3 (AP-3) is an heterotetramer
CC       composed of two large adaptins (delta-type subunit AP3D1 and beta-
CC       type subunit AP3B1 or AP3B2), a medium adaptin (mu-type subunit
CC       AP3M1 or AP3M2) and a small adaptin (sigma-type subunit APS1 or
CC       AP3S2) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle,
CC       clathrin-coated vesicle membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity). Golgi apparatus (By similarity).
CC       Note=Component of the coat surrounding the cytoplasmic face of
CC       coated vesicles located at the Golgi complex (By similarity).
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
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DR   EMBL; AY528675; AAS18679.1; -; mRNA.
DR   EMBL; BC139378; AAI39379.1; -; mRNA.
DR   EMBL; BC139379; AAI39380.1; -; mRNA.
DR   EMBL; AK134504; BAE22164.1; -; mRNA.
DR   EMBL; AB030202; BAA92765.1; -; mRNA.
DR   IPI; IPI00420426; -.
DR   RefSeq; NP_067467.2; NM_021492.3.
DR   UniGene; Mm.322894; -.
DR   ProteinModelPortal; Q9JME5; -.
DR   SMR; Q9JME5; 30-638.
DR   STRING; Q9JME5; -.
DR   PhosphoSite; Q9JME5; -.
DR   PRIDE; Q9JME5; -.
DR   Ensembl; ENSMUST00000082090; ENSMUSP00000080739; ENSMUSG00000062444.
DR   GeneID; 11775; -.
DR   KEGG; mmu:11775; -.
DR   UCSC; uc009iby.1; mouse.
DR   UCSC; uc009ibz.1; mouse.
DR   CTD; 11775; -.
DR   MGI; MGI:1100869; Ap3b2.
DR   GeneTree; ENSGT00530000063546; -.
DR   HOGENOM; HBG356465; -.
DR   HOVERGEN; HBG050519; -.
DR   InParanoid; Q9JME5; -.
DR   OMA; VVQKVTA; -.
DR   OrthoDB; EOG4VQ9NJ; -.
DR   PhylomeDB; Q9JME5; -.
DR   NextBio; 279567; -.
DR   ArrayExpress; Q9JME5; -.
DR   Bgee; Q9JME5; -.
DR   CleanEx; MM_AP3B2; -.
DR   Genevestigator; Q9JME5; -.
DR   GermOnline; ENSMUSG00000062444; Mus musculus.
DR   GO; GO:0030665; C:clathrin coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030117; C:membrane coat; IEA:InterPro.
DR   GO; GO:0005802; C:trans-Golgi network; TAS:MGI.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0008565; F:protein transporter activity; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR   InterPro; IPR017108; AP3_complex_bsu.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   InterPro; IPR008153; Clathrin_g-adaptin_app.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 2.
DR   Gene3D; G3DSA:2.60.40.1230; Clathrin_g-adaptin_app; 2.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   PIRSF; PIRSF037096; AP3_complex_beta; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Endocytosis; Golgi apparatus; Membrane;
KW   Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1   1082       AP-3 complex subunit beta-2.
FT                                /FTId=PRO_0000193749.
FT   COMPBIAS    646    798       Glu/Ser-rich.
FT   MOD_RES     272    272       Phosphoserine.
FT   MOD_RES     282    282       Phosphoserine.
FT   CONFLICT    734    734       E -> D (in Ref. 4; BAA92765).
SQ   SEQUENCE   1082 AA;  119193 MW;  A2FEB20E83E16A52 CRC64;
     MSAAPAYSED KGGSAGPGEP EYGHDPASGG IFSSDYKRHD DLKEMLDTNK DSLKLEAMKR
     IVAMIARGKN ASDLFPAVVK NVACKNIEVK KLVYVYLVRY AEEQQDLALL SISTFQRGLK
     DPNQLIRASA LRVLSSIRVP IIVPIMMLAI KEAASDMSPY VRKTAAHAIP KLYSLDSDQK
     DQLIEVIEKL LADKTTLVAG SVVMAFEEVC PERIDLIHKN YRKLCNLLID VEEWGQVVII
     SMLTRYARTQ FLSPTQNESL LEENPEKAFY GSEEDEAKGP GSEEAATAAL PARKPYVMDP
     DHRLLLRNTK PLLQSRSAAV VMAVAQLYFH LAPKAEVGVI AKALVRLLRS HSEVQYVVLQ
     NVATMSIKRR GMFEPYLKSF YIRSTDPTQI KILKLEVLTN LANETNIPTV LREFQTYIRS
     MDKDFVAATI QAIGRCATNI GRVRDTCLNG LVQLLSNRDE LVVAESVVVI KKLLQMQPAQ
     HGEIIKHLAK LTDNIQVPMA RASILWLIGE YCEHVPKIAP DVLRKMAKSF TAEEDIVKLQ
     VINLAAKLYL TNSKQTKLLT QYVLSLAKYD QNYDIRDRAR FTRQLIVPSE QGGALSRHAK
     KLFLAPKPAP ILESSFKDRD HFQLGSLSHL LNAKATGYQE LPDWPEEAPD PSVRNVEVPE
     WTKCSNREKR KEKEKPFYSD SEGESGPTES ADSEPESESE SESKSSSGSG SGESSSESDN
     EEEDEEKGGG SESEQSEEED EKKKKTKKKK ASEGHREGSS SEEGSDSSSS SESEVTSESE
     EEQVEPASWR KKTPPGSKSA PVAKEISLLD LEDFTPPSVQ PVSPPMVVST SLAADLEGLT
     LTDSSLVPSL LSPVSSIGRQ ELLHRVAGEG LSVDYAFSRQ PFSGDPHMVS LHIYFSNNSE
     TPIKGLHVGT PKLPAGISIQ EFPEIESLAP GESTTTVMGI NFCDSTQAAN FQLCTQTRQF
     YVSIQPPVGE LMAPVFMSEN EFKKEQGKLT GMNEITEKLT LPDTCRSDHM VVQKVTATAN
     LGRVPCGTSD EYRFAGRTLT SGSLVLLTLD ARAAGAAQLT VNSEKMVIGT MLVKDVIQAL
     TQ
//
ID   TMUB1_MOUSE             Reviewed;         245 AA.
AC   Q9JMG3; Q53AQ3;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Transmembrane and ubiquitin-like domain-containing protein 1;
DE   AltName: Full=Hepatocyte odd protein shuttling protein;
GN   Name=Tmub1; Synonyms=Hops;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=20145471; PubMed=10679242; DOI=10.1006/bbrc.2000.2170;
RA   Inoue S., Sano H., Ohta M.;
RT   "Growth suppression of Escherichia coli by induction of expression of
RT   mammalian genes with transmembrane or ATPase domains.";
RL   Biochem. Biophys. Res. Commun. 268:553-561(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, SUBCELLULAR LOCATION,
RP   INTERACTION WITH EEF1A1, AND FUNCTION.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   PubMed=16014383; DOI=10.1242/jcs.02452;
RA   Della Fazia M.A., Castelli M., Bartoli D., Pieroni S., Pettirossi V.,
RA   Piobbico D., Viola-Magni M., Servillo G.;
RT   "HOPS: a novel cAMP-dependent shuttling protein involved in protein
RT   synthesis regulation.";
RL   J. Cell Sci. 118:3185-3194(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May contribute to the regulation of translation during
CC       cell-cycle progression. May contribute to the regulation of cell
CC       proliferation.
CC   -!- SUBUNIT: Interacts with EEF1A1.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential). Cytoplasm. Nucleus. Note=Actively exported from the
CC       nucleus in dividing cells. Predominantly nuclear during growth
CC       arrest.
CC   -!- INDUCTION: Up-regulated in regenerating liver.
CC   -!- SIMILARITY: Contains 1 ubiquitin-like domain.
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DR   EMBL; AB030183; BAA92747.1; -; mRNA.
DR   EMBL; AY603379; AAU00155.1; -; mRNA.
DR   EMBL; AK008109; BAB25465.1; -; mRNA.
DR   EMBL; BC019547; AAH19547.1; -; mRNA.
DR   IPI; IPI00125641; -.
DR   RefSeq; NP_071863.1; NM_022418.3.
DR   UniGene; Mm.150098; -.
DR   ProteinModelPortal; Q9JMG3; -.
DR   SMR; Q9JMG3; 96-180.
DR   STRING; Q9JMG3; -.
DR   PhosphoSite; Q9JMG3; -.
DR   PRIDE; Q9JMG3; -.
DR   Ensembl; ENSMUST00000030799; ENSMUSP00000030799; ENSMUSG00000028958.
DR   Ensembl; ENSMUST00000115033; ENSMUSP00000110685; ENSMUSG00000028958.
DR   Ensembl; ENSMUST00000115036; ENSMUSP00000110688; ENSMUSG00000028958.
DR   GeneID; 64295; -.
DR   KEGG; mmu:64295; -.
DR   UCSC; uc008wrt.1; mouse.
DR   CTD; 64295; -.
DR   MGI; MGI:1923764; Tmub1.
DR   eggNOG; roNOG10724; -.
DR   GeneTree; ENSGT00390000014069; -.
DR   HOGENOM; HBG717365; -.
DR   HOVERGEN; HBG050920; -.
DR   InParanoid; Q9JMG3; -.
DR   OrthoDB; EOG4KH2W8; -.
DR   PhylomeDB; Q9JMG3; -.
DR   NextBio; 320013; -.
DR   ArrayExpress; Q9JMG3; -.
DR   Bgee; Q9JMG3; -.
DR   Genevestigator; Q9JMG3; -.
DR   GermOnline; ENSMUSG00000028958; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000626; Ubiquitin.
DR   InterPro; IPR019955; Ubiquitin_supergroup.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SMART; SM00213; UBQ; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Membrane; Nucleus; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    245       Transmembrane and ubiquitin-like domain-
FT                                containing protein 1.
FT                                /FTId=PRO_0000114923.
FT   TRANSMEM    194    214       Helical; (Potential).
FT   TRANSMEM    219    239       Helical; (Potential).
FT   DOMAIN      102    175       Ubiquitin-like.
FT   MOTIF        18     27       Nuclear export signal (Potential).
FT   MOD_RES      97     97       Phosphoserine (By similarity).
FT   CONFLICT    233    233       L -> Q (in Ref. 2; AAU00155).
SQ   SEQUENCE   245 AA;  26316 MW;  02C1D1B24C13139D CRC64;
     MALIEGVGDE VTVLFAVLAC LLVLALAWVS THTTESTDPQ PQPPGTTTPA QPSEAMSASD
     SIREEAPGAE SPSLRHRGPS AQPEPDTGVT ASTPPDSPQE PLLLRLKFLN DSEQVARAWP
     QDTIGSLKRT QFPGQEQQVR LIYQGQLLGD DTQTLGSLHL PPNCVLHCHV STRVGPPHPP
     CPPGSEPGPS GLEIGSLLLP LLLLLLLLLW YCQIQYRPFF PLTATLGLAG FTLLLSLLAF
     AMYRP
//
ID   NEUR3_MOUSE             Reviewed;         418 AA.
AC   Q9JMH7;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Sialidase-3;
DE            EC=3.2.1.18;
DE   AltName: Full=Ganglioside sialidase;
DE   AltName: Full=Membrane sialidase;
DE   AltName: Full=N-acetyl-alpha-neuraminidase 3;
GN   Name=Neu3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=20179907; PubMed=10713120; DOI=10.1074/jbc.275.11.8007;
RA   Hasegawa T., Yamaguchi K., Wada T., Takeda A., Itoyama Y., Miyagi T.;
RT   "Molecular cloning of mouse ganglioside sialidase and its increased
RT   expression in Neuro2a cell differentiation.";
RL   J. Biol. Chem. 275:8007-8015(2000).
CC   -!- FUNCTION: Plays a role in modulating the ganglioside content of
CC       the lipid bilayer at the level of membrane-bound sialyl
CC       glycoconjugates (By similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-,
CC       alpha-(2->8)- glycosidic linkages of terminal sialic acid residues
CC       in oligosaccharides, glycoproteins, glycolipids, colominic acid
CC       and synthetic substrates.
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in heart, brain and cerebral cortex.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 33 family.
CC   -!- SIMILARITY: Contains 3 BNR repeats.
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DR   EMBL; AB026842; BAA92868.1; -; mRNA.
DR   IPI; IPI00125683; -.
DR   RefSeq; NP_057929.1; NM_016720.2.
DR   UniGene; Mm.103703; -.
DR   ProteinModelPortal; Q9JMH7; -.
DR   SMR; Q9JMH7; 4-411.
DR   STRING; Q9JMH7; -.
DR   CAZy; GH33; Glycoside Hydrolase Family 33.
DR   PhosphoSite; Q9JMH7; -.
DR   PRIDE; Q9JMH7; -.
DR   Ensembl; ENSMUST00000036331; ENSMUSP00000045222; ENSMUSG00000035239.
DR   GeneID; 50877; -.
DR   KEGG; mmu:50877; -.
DR   NMPDR; fig|10090.3.peg.17025; -.
DR   UCSC; uc009imc.1; mouse.
DR   CTD; 50877; -.
DR   MGI; MGI:1355305; Neu3.
DR   GeneTree; ENSGT00390000011171; -.
DR   HOGENOM; HBG445278; -.
DR   HOVERGEN; HBG052608; -.
DR   InParanoid; Q9JMH7; -.
DR   OMA; VYLFFIC; -.
DR   OrthoDB; EOG4FR0RV; -.
DR   PhylomeDB; Q9JMH7; -.
DR   BRENDA; 3.2.1.18; 244.
DR   NextBio; 307853; -.
DR   ArrayExpress; Q9JMH7; -.
DR   Bgee; Q9JMH7; -.
DR   CleanEx; MM_NEU3; -.
DR   Genevestigator; Q9JMH7; -.
DR   GermOnline; ENSMUSG00000035239; Mus musculus.
DR   GO; GO:0004308; F:exo-alpha-sialidase activity; IEA:EC.
DR   InterPro; IPR011040; Neuraminidase.
DR   Gene3D; G3DSA:2.120.10.10; Neuraminidase; 2.
DR   SUPFAM; SSF50939; Sialidase; 1.
PE   2: Evidence at transcript level;
KW   Glycosidase; Hydrolase; Membrane; Phosphoprotein; Repeat.
FT   CHAIN         1    418       Sialidase-3.
FT                                /FTId=PRO_0000208904.
FT   REPEAT      129    140       BNR 1.
FT   REPEAT      203    214       BNR 2.
FT   REPEAT      254    265       BNR 3.
FT   MOTIF        24     27       FRIP motif.
FT   ACT_SITE     50     50       Proton acceptor (By similarity).
FT   ACT_SITE    369    369       Nucleophile (By similarity).
FT   ACT_SITE    386    386       Potential.
FT   BINDING      25     25       Substrate (By similarity).
FT   BINDING     243    243       Substrate (Potential).
FT   BINDING     339    339       Substrate (By similarity).
FT   MOD_RES     414    414       Phosphoserine (By similarity).
SQ   SEQUENCE   418 AA;  46846 MW;  64853FC963FE7686 CRC64;
     MEEVPPYSLS STLFQQEEQS GVTYRIPALL YLPPTHTFLA FAEKRTSVRD EDAACLVLRR
     GLMKGRSVQW GPQRLLMEAT LPGHRTMNPC PVWEKNTGRV YLFFICVRGH VTERCQIVWG
     KNAARLCFLC SEDAGCSWGE VKDLTEEVIG SEVKRWATFA VGPGHGIQLH SGRLIIPAYA
     YYVSRWFLCF ACSVKPHSLM IYSDDFGVTW HHGKFIEPQV TGECQVAEVA GTAGNPVLYC
     SARTPSRFRA EAFSTDSGGC FQKPTLNPQL HEPRTGCQGS VVSFRPLKMP NTYQDSIGKG
     APATQKCPLL DSPLEVEKGA ETPSATWLLY SHPTSKRKRI NLGIYYNRNP LEVNCWSRPW
     ILNRGPSGYS DLAVVEEQDL VACLFECGEK NEYERIDFCL FSDHEVLSCE DCTSPSSD
//
ID   MY18A_MOUSE             Reviewed;        2050 AA.
AC   Q9JMH9; Q3TBB2; Q3UH48; Q3UV60; Q5SYN8; Q5SYN9; Q5SYP0; Q5SYP1;
AC   Q811D7;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 2.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Myosin-XVIIIa;
DE   AltName: Full=Molecule associated with JAK3 N-terminus;
DE            Short=MAJN;
DE   AltName: Full=Myosin containing a PDZ domain;
GN   Name=Myo18a; Synonyms=Myspdz;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Spleen;
RX   MEDLINE=20200096; PubMed=10733906; DOI=10.1006/bbrc.2000.2377;
RA   Furusawa T., Ikawa S., Yanai N., Obinata M.;
RT   "Isolation of a novel PDZ-containing myosin from hematopoietic
RT   supportive bone marrow stromal cell lines.";
RL   Biochem. Biophys. Res. Commun. 270:67-75(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-873 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Bone, and Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1032-2050 (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH JAK3.
RX   PubMed=10733938; DOI=10.1006/bbrc.2000.2413;
RA   Ji H., Zhai Q., Zhu J., Yan M., Sun L., Liu X., Zheng Z.;
RT   "A novel protein MAJN binds to Jak3 and inhibits apoptosis induced by
RT   IL-2 deprival.";
RL   Biochem. Biophys. Res. Commun. 270:267-271(2000).
RN   [6]
RP   ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), AND DIFFERENTIAL EXPRESSION.
RC   TISSUE=Spleen;
RX   MEDLINE=22646225; PubMed=12761286; DOI=10.1093/jb/mvg053;
RA   Mori K., Furusawa T., Okubo T., Inoue T., Ikawa S., Yanai N.,
RA   Mori K.J., Obinata M.;
RT   "Genome structure and differential expression of two isoforms of a
RT   novel PDZ-containing myosin (MysPDZ) (Myo18A).";
RL   J. Biochem. 133:405-413(2003).
RN   [7]
RP   PHOSPHORYLATION, AND MASS SPECTROMETRY.
RX   PubMed=14969583; DOI=10.1042/BJ20031978;
RA   Cross M., Csar X.F., Wilson N.J., Manes G., Addona T.A., Marks D.C.,
RA   Whitty G.A., Ashman K., Hamilton J.A.;
RT   "A novel 110 kDa form of myosin XVIIIA (MysPDZ) is tyrosine-
RT   phosphorylated after colony-stimulating factor-1 receptor
RT   signalling.";
RL   Biochem. J. 380:243-253(2004).
RN   [8]
RP   HOMODIMER, SUBCELLULAR LOCATION, AND INTERACTION WITH ACTIN.
RX   PubMed=15582604; DOI=10.1016/j.bbrc.2004.11.058;
RA   Mori K., Matsuda K., Furusawa T., Kawata M., Inoue T., Obinata M.;
RT   "Subcellular localization and dynamics of MysPDZ (Myo18A) in live
RT   mammalian cells.";
RL   Biochem. Biophys. Res. Commun. 326:491-498(2005).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1966 AND SER-1970, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340 (ISOFORM 6), AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72; SER-74; SER-83;
RP   SER-102; SER-164; SER-1966; SER-2032; SER-2037 AND SER-2039, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-1966; SER-1970;
RP   SER-2016; SER-2037 AND SER-2039, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1966 AND SER-1970, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: May be involved in the maintenance of the stromal cell
CC       architecture required for cell to cell contact. Isoform 1 may be
CC       related to adherence and/or some other functions of mature
CC       macrophages.
CC   -!- SUBUNIT: Homodimer. Interacts with JAK3 and actin.
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum-Golgi
CC       intermediate compartment. Cytoplasm, cytoskeleton.
CC       Note=Colocalizes with actin.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm. Note=Lacks the PDZ
CC       domain. Diffusely localized in the cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=7;
CC       Name=3;
CC         IsoId=Q9JMH9-3; Sequence=Displayed;
CC       Name=1; Synonyms=Alpha;
CC         IsoId=Q9JMH9-1; Sequence=VSP_023062;
CC       Name=2; Synonyms=Beta;
CC         IsoId=Q9JMH9-2; Sequence=VSP_007873, VSP_007874;
CC       Name=4;
CC         IsoId=Q9JMH9-4; Sequence=VSP_023061, VSP_023062;
CC       Name=5;
CC         IsoId=Q9JMH9-5; Sequence=VSP_007873, VSP_007874, VSP_023062;
CC       Name=6;
CC         IsoId=Q9JMH9-6; Sequence=VSP_023060;
CC         Note=Phosphorylated at position 340;
CC       Name=7;
CC         IsoId=Q9JMH9-7; Sequence=VSP_007873, VSP_023059, VSP_023062;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is expressed ubiquitously. Isoform 2
CC       is specifically expressed in most hematopoietic cells.
CC   -!- PTM: Phosphorylated on tyrosine upon CSF1R activation. Isoform 6
CC       is phosphorylated on Ser-340.
CC   -!- SIMILARITY: Contains 1 IQ domain.
CC   -!- SIMILARITY: Contains 1 myosin head-like domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
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DR   EMBL; AB026497; BAA93660.1; -; mRNA.
DR   EMBL; AK137574; BAE23413.1; -; mRNA.
DR   EMBL; AK147584; BAE28009.1; -; mRNA.
DR   EMBL; AK171342; BAE42402.1; -; mRNA.
DR   EMBL; AL591065; CAI24424.1; -; Genomic_DNA.
DR   EMBL; AL591065; CAI24425.1; -; Genomic_DNA.
DR   EMBL; AL591065; CAI24426.1; -; Genomic_DNA.
DR   EMBL; AL591065; CAI24427.1; -; Genomic_DNA.
DR   EMBL; BC046638; AAH46638.1; -; mRNA.
DR   IPI; IPI00407425; -.
DR   IPI; IPI00619995; -.
DR   IPI; IPI00622556; -.
DR   IPI; IPI00648918; -.
DR   IPI; IPI00649326; -.
DR   IPI; IPI00828545; -.
DR   IPI; IPI00828766; -.
DR   RefSeq; NP_035716.1; NM_011586.2.
DR   UniGene; Mm.341248; -.
DR   UniGene; Mm.476162; -.
DR   ProteinModelPortal; Q9JMH9; -.
DR   SMR; Q9JMH9; 217-309, 341-1271.
DR   IntAct; Q9JMH9; 3.
DR   STRING; Q9JMH9; -.
DR   PhosphoSite; Q9JMH9; -.
DR   PRIDE; Q9JMH9; -.
DR   Ensembl; ENSMUST00000000645; ENSMUSP00000000645; ENSMUSG00000000631.
DR   Ensembl; ENSMUST00000092886; ENSMUSP00000090562; ENSMUSG00000000631.
DR   Ensembl; ENSMUST00000092887; ENSMUSP00000090563; ENSMUSG00000000631.
DR   Ensembl; ENSMUST00000108375; ENSMUSP00000104012; ENSMUSG00000000631.
DR   Ensembl; ENSMUST00000108376; ENSMUSP00000104013; ENSMUSG00000000631.
DR   GeneID; 360013; -.
DR   KEGG; mmu:360013; -.
DR   UCSC; uc007khg.1; mouse.
DR   CTD; 360013; -.
DR   MGI; MGI:2667185; Myo18a.
DR   eggNOG; roNOG15346; -.
DR   GeneTree; ENSGT00580000081235; -.
DR   HOVERGEN; HBG052543; -.
DR   OMA; LFHERTF; -.
DR   PhylomeDB; Q9JMH9; -.
DR   ArrayExpress; Q9JMH9; -.
DR   Bgee; Q9JMH9; -.
DR   CleanEx; MM_MYO18A; -.
DR   Genevestigator; Q9JMH9; -.
DR   GermOnline; ENSMUSG00000000631; Mus musculus.
DR   GO; GO:0005793; C:ER-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003774; F:motor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR002928; Myosin_tail.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF00063; Myosin_head; 2.
DR   Pfam; PF01576; Myosin_tail_1; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00015; IQ; 1.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Motor protein; Myosin; Nucleotide-binding;
KW   Phosphoprotein.
FT   CHAIN         1   2050       Myosin-XVIIIa.
FT                                /FTId=PRO_0000123477.
FT   DOMAIN      220    311       PDZ.
FT   DOMAIN      407   1169       Myosin head-like.
FT   DOMAIN     1184   1213       IQ.
FT   NP_BIND     498    505       ATP (Potential).
FT   COILED     1242   1967       Potential.
FT   MOTIF       114    118       Interaction with actin (By similarity).
FT   MOD_RES      72     72       Phosphoserine.
FT   MOD_RES      74     74       Phosphoserine.
FT   MOD_RES      83     83       Phosphoserine.
FT   MOD_RES     102    102       Phosphoserine.
FT   MOD_RES     140    140       Phosphoserine (By similarity).
FT   MOD_RES     164    164       Phosphoserine.
FT   MOD_RES     234    234       Phosphoserine (By similarity).
FT   MOD_RES    1035   1035       Phosphoserine (By similarity).
FT   MOD_RES    1059   1059       Phosphoserine (By similarity).
FT   MOD_RES    1063   1063       Phosphoserine (By similarity).
FT   MOD_RES    1066   1066       Phosphoserine (By similarity).
FT   MOD_RES    1938   1938       Phosphoserine (By similarity).
FT   MOD_RES    1947   1947       Phosphoserine (By similarity).
FT   MOD_RES    1966   1966       Phosphoserine.
FT   MOD_RES    1970   1970       Phosphoserine.
FT   MOD_RES    1994   1994       Phosphoserine (By similarity).
FT   MOD_RES    1998   1998       Phosphoserine (By similarity).
FT   MOD_RES    2003   2003       Phosphoserine (By similarity).
FT   MOD_RES    2016   2016       Phosphoserine.
FT   MOD_RES    2032   2032       Phosphoserine.
FT   MOD_RES    2037   2037       Phosphoserine.
FT   MOD_RES    2039   2039       Phosphoserine.
FT   MOD_RES    2041   2041       Phosphothreonine (By similarity).
FT   VAR_SEQ       1    331       Missing (in isoform 2, isoform 5 and
FT                                isoform 7).
FT                                /FTId=VSP_007873.
FT   VAR_SEQ     332    333       AD -> ML (in isoform 2 and isoform 5).
FT                                /FTId=VSP_007874.
FT   VAR_SEQ     332    333       AD -> MLLDPEAASPAYSQ (in isoform 7).
FT                                /FTId=VSP_023059.
FT   VAR_SEQ     333    333       D -> DLDPEAASPAYSQ (in isoform 6).
FT                                /FTId=VSP_023060.
FT   VAR_SEQ    1567   1603       Missing (in isoform 4).
FT                                /FTId=VSP_023061.
FT   VAR_SEQ    1948   1962       Missing (in isoform 1, isoform 4, isoform
FT                                5 and isoform 7).
FT                                /FTId=VSP_023062.
FT   CONFLICT    399    399       A -> T (in Ref. 2; BAE28009).
FT   CONFLICT    466    466       R -> Q (in Ref. 2; BAE42402).
FT   CONFLICT    680    683       Missing (in Ref. 2; BAE42402).
FT   CONFLICT    680    680       E -> EPLEEQD (in Ref. 2; BAE28009).
FT   CONFLICT    798    798       G -> D (in Ref. 2; BAE42402).
FT   CONFLICT   1362   1362       D -> N (in Ref. 2; BAE42402).
FT   CONFLICT   1655   1655       K -> R (in Ref. 2; BAE28009).
SQ   SEQUENCE   2050 AA;  232755 MW;  3D82B901F03D73B4 CRC64;
     MFNLMKKDKD KDGGRKEKKE KKEKKERMSA AELRSLEEMS MRRGFFNLNR SSKRESKTRL
     EISNPIPIKV ASGSDLHLTD IDSDSNRGSI ILDSGHLSTA SSSDDLKGEE GSFRGSVLQR
     AAKFGSLAKQ NSQMIVKRFS FSQRSRDESA SETSTPSEHS AAPSPQVEVR TLEGQLMQHP
     GLGIPRPGPR SRVPELVTKR FPADLRLPAL VPPPPPALRE LELQRRPTGD FGFSLRRTTM
     LDRAPEGQAY RRVVHFAEPG AGTKDLALGL VPGDRLVEIN GQNVENKSRD EIVEMIRQSG
     DSVRLKVQPI PELSELSRSW LRTGEGHRRE PADAKTEEQI AAEEAWYETE KVWLVHRDGF
     SLASQLKSEE LSLPEGKARV KLDHDGAILD VDEDDIEKAN APSCDRLEDL ASLVYLNESS
     VLHTLRQRYG ASLLHTYAGP SLLVLSTRGA PAVYSEKVMH MFKGCRREDM APHIYAVAQT
     AYRAMLMSRQ DQSIVLLGSS GSGKTTSFQH LVQYLATIAG TSGTKVFSVE KWQALSTLLE
     AFGNSPTIMN GSATRFSQIL SLDFDQAGQV ASASIQTMLL EKLRVARRPA SEATFNVFYY
     LLACGDATLR TELHLNHLAE NNVFGIVPLS KPEEKQKAAQ QFSKLQAAMK VLAISPEEQK
     TCWLILASIY HLGAAGATKE AAEAGRKQFA RHEWAQKAAY LLGCSLEELS SAIFKHQLKG
     GTLQRSTSFR QGPEESGLGE GTKLSALECL EGMASGLYSE LFTLLISLVN RALKSSQHSL
     CSMMIVDTPG FQNPEWGGSA RGASFEELCH NYAQDRLQRL FHERTFLQEL ERYKEDNIEL
     AFDDLEPVAD DSVAAVDQAS HLVRSLAHAD EARGLLWLLE EEALVPGATE DALLDRLFSY
     YGPQEGDKKG QSPLLRSSKP RHFLLGHSHG TNWVEYNVAG WLNYTKQNPA TQNAPRLLQD
     SQKKIISNLF LGRAGSATVL SGSIAGLEGG SQLALRRATS MRKTFTTGMA AVKKKSLCIQ
     IKLQVDALID TIKRSKMHFV HCFLPVAEGW PGEPRSASSR RVSSSSELDL PPGDPCEAGL
     LQLDVSLLRA QLRGSRLLDA MRMYRQGYPD HMVFSEFRRR FDVLAPHLTK KHGRNYIVVD
     EKRAVEELLE SLDLEKSSCC LGLSRVFFRA GTLARLEEQR DEQTSRHLTL FQAACRGYLA
     RQHFKKRKIQ DLAIRCVQKN IKKNKGVKDW PWWKLFTTVR PLIQVQLSEE QIRNKDEEIQ
     QLRSKLEKVE KERNELRLSS DRLETRISEL TSELTDERNT GESASQLLDA ETAERLRTEK
     EMKELQTQYD ALKKQMEVME MEVMEARLIR AAEINGEVDD DDAGGEWRLK YERAVREVDF
     TKKRLQQELE DKMEVEQQSR RQLERRLGDL QADSDESQRA LQQLKKKCQR LTAELQDTKL
     HLEGQQVRNH ELEKKQRRFD SELSQAHEET QREKLQREKL QREKDMLLAE AFSLKQQMEE
     KDLDIAGFTQ KVVSLEAELQ DISSQESKDE ASLAKVKKQL RDLEAKVKDQ EEELDEQAGS
     IQMLEQAKLR LEMEMERMRQ THSKEMESRD EEVEEARQSC QKKLKQMEVQ LEEEYEDKQK
     ALREKRELES KLSTLSDQVN QRDFESEKRL RKDLKRTKAL LADAQIMLDH LKNNAPSKRE
     IAQLKNQLEE SEFTCAAAVK ARKAMEVEME DLHLQIDDIA KAKTALEEQL SRLQREKNEI
     QNRLEEDQED MNELMKKHKA AVAQASRDMA QMNDLQAQIE ESNKEKQELQ EKLQALQSQV
     EFLEQSMVDK SLVSRQEAKI RELETRLEFE KTQVKRLENL ASRLKETMEK LTEERDQRAA
     AENREKEQNK RLQRQLRDTK EEMSELARKE AEASRKKHEL EMDLESLEAA NQSLQADLKL
     AFKRIGDLQA AIEDEMESDE NEDLINSLQD MVTKYQKKKN KLEGDSDVDS ELEDRVDGVK
     SWLSKNKGPS KAPSDDGSLK SSSPTSHWKP LAPDPSDDEH DPVDSISRPR FSHSYLSDSD
     TEAKLTETSA
//
ID   GRP2_MOUSE              Reviewed;         608 AA.
AC   Q9QUG9; O09004; Q80WC0; Q8BSC8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=RAS guanyl-releasing protein 2;
DE   AltName: Full=Calcium and DAG-regulated guanine nucleotide exchange factor I;
DE            Short=CalDAG-GEFI;
DE   AltName: Full=F25B3.3 kinase-like protein;
GN   Name=Rasgrp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION AS A RAP
RP   ACTIVATOR.
RX   MEDLINE=99007305; PubMed=9789079; DOI=10.1073/pnas.95.22.13278;
RA   Kawasaki H., Springett G.M., Toki S., Canales J.J., Harlan P.,
RA   Blumenstiel J.P., Chen E.J., Bany I.A., Mochizuki N., Ashbacher A.,
RA   Matsuda M., Housman D.E., Graybiel A.M.;
RT   "A Rap guanine nucleotide exchange factor enriched highly in the basal
RT   ganglia.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:13278-13283(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 204-608 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 349-608 (ISOFORM 1).
RX   MEDLINE=98001089; PubMed=9341881; DOI=10.1007/s004390050562;
RA   Kedra D., Seroussi E., Fransson I., Trifunovic J., Clark M.,
RA   Lagercrantz J., Blennow E., Mehlin H., Dumanski J.;
RT   "The germinal centre kinase gene and a novel CDC25-like gene are
RT   located in the vicinity of the PYGM gene on 11q13.";
RL   Hum. Genet. 100:611-619(1997).
RN   [5]
RP   FUNCTION.
RX   PubMed=10777492; DOI=10.1074/jbc.M000981200;
RA   Ohba Y., Mochizuki N., Yamashita S., Chan A.M., Schrader J.W.,
RA   Hattori S., Nagashima K., Matsuda M.;
RT   "Regulatory proteins of R-Ras, TC21/R-Ras2, and M-Ras/R-Ras3.";
RL   J. Biol. Chem. 275:20020-20026(2000).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=10835426; DOI=10.1074/jbc.M003414200;
RA   Yamashita S., Mochizuki N., Ohba Y., Tobiume M., Okada Y., Sawa H.,
RA   Nagashima K., Matsuda M.;
RT   "CalDAG-GEFIII activation of Ras, R-ras, and Rap1.";
RL   J. Biol. Chem. 275:25488-25493(2000).
RN   [7]
RP   FUNCTION AS RAP2 ACTIVATOR.
RX   PubMed=10913189; DOI=10.1128/MCB.20.16.6074-6083.2000;
RA   Ohba Y., Mochizuki N., Matsuo K., Yamashita S., Nakaya M.,
RA   Hashimoto Y., Hamaguchi M., Kurata T., Nagashima K., Matsuda M.;
RT   "Rap2 as a slowly responding molecular switch in the Rap1 signaling
RT   cascade.";
RL   Mol. Cell. Biol. 20:6074-6083(2000).
RN   [8]
RP   FUNCTION.
RX   PubMed=11432821; DOI=10.1093/emboj/20.13.3333;
RA   Ohba Y., Ikuta K., Ogura A., Matsuda J., Mochizuki N., Nagashima K.,
RA   Kurokawa K., Mayer B.J., Maki K., Miyazaki J., Matsuda M.;
RT   "Requirement for C3G-dependent Rap1 activation for cell adhesion and
RT   embryogenesis.";
RL   EMBO J. 20:3333-3341(2001).
RN   [9]
RP   FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=11278453; DOI=10.1074/jbc.M008970200;
RA   Dupuy A.J., Morgan K., von Lintig F.C., Shen H., Acar H., Hasz D.E.,
RA   Jenkins N.A., Copeland N.G., Boss G.R., Largaespada D.A.;
RT   "Activation of the Rap1 guanine nucleotide exchange gene, CalDAG-GEF
RT   I, in BXH-2 murine myeloid leukemia.";
RL   J. Biol. Chem. 276:11804-11811(2001).
RN   [10]
RP   FUNCTION.
RX   PubMed=12239348; DOI=10.1073/pnas.202380099;
RA   Eto K., Murphy R., Kerrigan S.W., Bertoni A., Stuhlmann H., Nakano T.,
RA   Leavitt A.D., Shattil S.J.;
RT   "Megakaryocytes derived from embryonic stem cells implicate CalDAG-
RT   GEFI in integrin signaling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12819-12824(2002).
RN   [11]
RP   FUNCTION IN PLATELETS AGGREGATION, DISRUPTION PHENOTYPE, INTERACTION
RP   WITH RAP1, AND TISSUE SPECIFICITY.
RX   PubMed=15334074; DOI=10.1038/nm1098;
RA   Crittenden J.R., Bergmeier W., Zhang Y., Piffath C.L., Liang Y.,
RA   Wagner D.D., Housman D.E., Graybiel A.M.;
RT   "CalDAG-GEFI integrates signaling for platelet aggregation and
RT   thrombus formation.";
RL   Nat. Med. 10:982-986(2004).
RN   [12]
RP   FUNCTION.
RX   PubMed=16357324; DOI=10.1182/blood-2005-07-3023;
RA   Bernardi B., Guidetti G.F., Campus F., Crittenden J.R., Graybiel A.M.,
RA   Balduini C., Torti M.;
RT   "The small GTPase Rap1b regulates the cross talk between platelet
RT   integrin alpha2beta1 and integrin alphaIIbbeta3.";
RL   Blood 107:2728-2735(2006).
RN   [13]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17492052; DOI=10.1172/JCI30575;
RA   Bergmeier W., Goerge T., Wang H.-W., Crittenden J.R., Baldwin A.C.W.,
RA   Cifuni S.M., Housman D.E., Graybiel A.M., Wagner D.D.;
RT   "Mice lacking the signaling molecule CalDAG-GEFI represent a model for
RT   leukocyte adhesion deficiency type III.";
RL   J. Clin. Invest. 117:1699-1707(2007).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-117, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-117, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Functions as a calcium- and DAG-regulated nucleotide
CC       exchange factor specifically activating Rap through the exchange
CC       of bound GDP for GTP. May also activates other GTPases such as
CC       RRAS, RRAS2, NRAS, KRAS but not HRAS. Functions in aggregation of
CC       platelets and adhesion of T-lymphocytes and neutrophils probably
CC       through inside-out integrin activation. May function in the
CC       muscarinic acetylcholine receptor M1/CHRM1 signaling pathway.
CC   -!- SUBUNIT: Forms a signaling complex with RAP1 and BRAF. Interacts
CC       with F-actin (By similarity). Interacts with RAP1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity). Cell
CC       membrane; Peripheral membrane protein (By similarity). Cell
CC       junction, synapse, synaptosome (By similarity). Cell projection,
CC       ruffle membrane; Peripheral membrane protein (Potential).
CC       Note=Found both in the cytosol and associated with membranes (By
CC       similarity). Enriched at juxtamembrane areas and membrane ruffles
CC       (By similarity). Localizes to the cell bodies and axons of
CC       striatal neurons (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=CalDAG-GEF1a;
CC         IsoId=Q9QUG9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9QUG9-2; Sequence=VSP_030579;
CC         Note=No experimental confirmation available;
CC       Name=3; Synonyms=CalDAG-GEF1b;
CC         IsoId=Q9QUG9-3; Sequence=VSP_030577, VSP_030578;
CC         Note=The corresponding protein is not undetectable;
CC   -!- TISSUE SPECIFICITY: Detected in megakaryocytes, platelet and
CC       neutrophils but not in lymphocytes (at protein level). Isoform 1
CC       and isoform 3 are detected in brain basal glanglia, heart, lung,
CC       spleen, liver and kidney interstitial cells.
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryo with higher expression
CC       between E15 and E17.
CC   -!- DOMAIN: The N-terminal Ras-GEF domain mediates association with F-
CC       actin (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice have a combination of defects in
CC       leukocytes and platelet functions which are reminiscent of the
CC       human leukocyte adhesion deficiency type III syndrome (LAD3). They
CC       display bleeding diathesis due to a defect in platelet aggregation
CC       and are resistant to collagen-induced thrombosis. In parallel,
CC       they also display impaired response to acute inflammation
CC       associated with defects in beta-1 and beta-2 integrin-mediated
CC       adhesion of neutrophils.
CC   -!- SIMILARITY: Belongs to the RASGRP family.
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
CC   -!- SIMILARITY: Contains 1 N-terminal Ras-GEF domain.
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC   -!- SIMILARITY: Contains 1 Ras-GEF domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC28797.1; Type=Erroneous initiation;
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DR   EMBL; AF081193; AAC79697.1; -; mRNA.
DR   EMBL; U78171; AAD12742.1; -; mRNA.
DR   EMBL; BC051474; AAH51474.1; -; mRNA.
DR   EMBL; AK034683; BAC28797.1; ALT_INIT; mRNA.
DR   EMBL; Y12339; CAA73008.1; -; mRNA.
DR   IPI; IPI00622961; -.
DR   IPI; IPI00830445; -.
DR   IPI; IPI00857529; -.
DR   RefSeq; NP_035372.2; NM_011242.2.
DR   UniGene; Mm.77017; -.
DR   HSSP; P28867; 1PTQ.
DR   ProteinModelPortal; Q9QUG9; -.
DR   SMR; Q9QUG9; 153-387, 433-484, 498-548.
DR   STRING; Q9QUG9; -.
DR   PhosphoSite; Q9QUG9; -.
DR   PRIDE; Q9QUG9; -.
DR   Ensembl; ENSMUST00000035716; ENSMUSP00000041135; ENSMUSG00000032946.
DR   Ensembl; ENSMUST00000113476; ENSMUSP00000109104; ENSMUSG00000032946.
DR   GeneID; 19395; -.
DR   KEGG; mmu:19395; -.
DR   UCSC; uc008gip.1; mouse.
DR   CTD; 19395; -.
DR   MGI; MGI:1333849; Rasgrp2.
DR   eggNOG; maNOG07943; -.
DR   GeneTree; ENSGT00510000046358; -.
DR   HOGENOM; HBG403023; -.
DR   HOVERGEN; HBG007513; -.
DR   InParanoid; Q9QUG9; -.
DR   OMA; KMSLLFD; -.
DR   OrthoDB; EOG4TB49W; -.
DR   NextBio; 296505; -.
DR   ArrayExpress; Q9QUG9; -.
DR   Bgee; Q9QUG9; -.
DR   CleanEx; MM_RASGRP2; -.
DR   Genevestigator; Q9QUG9; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR   GO; GO:0019717; C:synaptosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR   InterPro; IPR008937; Ras_GEF.
DR   InterPro; IPR001895; RasGRF_CDC25.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Gene3D; G3DSA:1.10.840.10; RasGRF_CDC25; 1.
DR   PANTHER; PTHR23113; Ras_GEF; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00618; RasGEF_N; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00229; RasGEFN; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS00720; RASGEF; FALSE_NEG.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50212; RASGEF_NTER; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell junction; Cell membrane;
KW   Cell projection; Cytoplasm; Guanine-nucleotide releasing factor;
KW   Membrane; Metal-binding; Phosphoprotein; Repeat; Synapse; Synaptosome;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    608       RAS guanyl-releasing protein 2.
FT                                /FTId=PRO_0000315609.
FT   DOMAIN        4    126       N-terminal Ras-GEF.
FT   DOMAIN      154    387       Ras-GEF.
FT   DOMAIN      426    461       EF-hand 1.
FT   DOMAIN      455    490       EF-hand 2.
FT   CA_BIND     439    450       1 (Potential).
FT   CA_BIND     468    479       2 (Potential).
FT   ZN_FING     498    548       Phorbol-ester/DAG-type.
FT   MOD_RES     116    116       Phosphoserine.
FT   MOD_RES     117    117       Phosphoserine.
FT   VAR_SEQ     125    141       PTYKWKRQVTQRNPVEQ -> CVGAERKGHYACYTICA
FT                                (in isoform 3).
FT                                /FTId=VSP_030577.
FT   VAR_SEQ     142    608       Missing (in isoform 3).
FT                                /FTId=VSP_030578.
FT   VAR_SEQ     472    608       Missing (in isoform 2).
FT                                /FTId=VSP_030579.
FT   CONFLICT      2      2       T -> A (in Ref. 1; AAC79697/AAD12742).
FT   CONFLICT     73     73       M -> V (in Ref. 1; AAC79697/AAD12742).
FT   CONFLICT     83     83       I -> V (in Ref. 1; AAC79697/AAD12742).
FT   CONFLICT     99     99       Q -> P (in Ref. 1; AAC79697/AAD12742).
FT   CONFLICT    233    233       R -> K (in Ref. 1; AAC79697/AAD12742).
FT   CONFLICT    339    339       C -> S (in Ref. 1; AAC79697/AAD12742).
FT   CONFLICT    542    542       E -> D (in Ref. 1; AAC79697/AAD12742).
FT   CONFLICT    598    598       S -> T (in Ref. 1; AAC79697/AAD12742).
SQ   SEQUENCE   608 AA;  69446 MW;  1E6F768EF00B0468 CRC64;
     MTSTLDLDKG CTVEELLRGC IEAFDDSGKV RDPQLVRMFL MMHPWYIPSS QLASKLLHFY
     QQSRKDNSNS LQMKTCHLVR YWISAFPAEF DLNPELAEQI KELKALLDQE GNRRHSSLID
     IESVPTYKWK RQVTQRNPVE QKKRKMSLLF DHLEPMELAE HLTYLEYRSF CKILFQDYHS
     FVTHGCTVDN PVLERFISLF NSVSQWVQLM ILSKPTATQR ALVITHFVHV AERLLQLQNF
     NTLMAVVGGL SHSSISRLKE THSHVSPDTI KLWEGLTELV TATGNYSNYR RRLAACVGFR
     FPILGVHLKD LVALQLALPD WLDPGRTRLN GAKMRQLFCI LEELAMVTSL RPPVQANPDL
     LSLLTVSLDQ YQTEDELYQL SLQREPRSKS SPTSPTSCTP PPRPPVLEEW TSVAKPKLDQ
     ALVAEHIEKM VESVFRNFDV DGDGHISQEE FQIIRGNFPY LSAFGDLDQN QDGCISREEM
     ISYFLRSSSV LGGRMGFVHN FQESNSLRPV ACRHCKALIL GIYKQGLKCR ACGVNCHKQC
     KERLSVECRR RAQSVSLEGS APSPSPTHTH HRAFSFSLPR PGRRSSRPPE IREEEVQSVE
     DGVFDIHL
//
ID   SYGP1_RAT               Reviewed;        1308 AA.
AC   Q9QUH6; O88449; Q9ESK6; Q9ET81; Q9QX02; Q9QX06; Q9QX12;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 2.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Ras GTPase-activating protein SynGAP;
DE   AltName: Full=Neuronal RasGAP;
DE   AltName: Full=Synaptic Ras GTPase-activating protein 1;
DE            Short=Synaptic Ras-GAP 1;
DE   AltName: Full=p135 SynGAP;
GN   Name=Syngap1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF
RP   16-276 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 1264-1290 (ISOFORM
RP   5), AND PROTEIN SEQUENCE OF 32-47; 242-248; 259-272; 300-321; 325-329;
RP   340-354; 419-429; 588-596; 804-815; 923-940; 968-1002; 1086-1102 AND
RP   1276-1286.
RC   STRAIN=Sprague-Dawley;
RX   MEDLINE=98282016; PubMed=9620694; DOI=10.1016/S0896-6273(00)80471-7;
RA   Chen H.-J., Rojas-Soto M., Oguni A., Kennedy M.B.;
RT   "A synaptic Ras-GTPase activating protein (p135 SynGAP) inhibited by
RT   CaM kinase II.";
RL   Neuron 20:895-904(1998).
RN   [2]
RP   ERRATUM.
RA   Oh J.S., Chen H.-J., Rojas-Soto M., Oguni A., Kennedy M.B.;
RL   Neuron 33:151-151(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), AND INTERACTION WITH
RP   DLG3 AND DLG4.
RC   TISSUE=Hippocampus;
RX   MEDLINE=98240917; PubMed=9581761; DOI=10.1016/S0896-6273(00)81008-9;
RA   Kim J.H., Liao D., Lau L.-F., Huganir R.L.;
RT   "SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90
RT   protein family.";
RL   Neuron 20:683-691(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RC   STRAIN=Sprague-Dawley;
RX   MEDLINE=21293034; PubMed=11278737; DOI=10.1074/jbc.M010744200;
RA   Li W., Okano A., Tian Q.B., Nakayama K., Furihata T., Nawa H.,
RA   Suzuki T.;
RT   "Characterization of a novel synGAP isoform, synGAP-beta.";
RL   J. Biol. Chem. 276:21417-21424(2001).
RN   [5]
RP   INTERACTION WITH MPDZ; DLG4; CAMK2A AND CAMK2B, PHOSPHORYLATION, AND
RP   FUNCTION.
RX   PubMed=15312654; DOI=10.1016/j.neuron.2004.08.003;
RA   Krapivinsky G., Medina I., Krapivinsky L., Gapon S., Clapham D.E.;
RT   "SynGAP-MUPP1-CaMKII synaptic complexes regulate p38 MAP kinase
RT   activity and NMDA receptor-dependent synaptic AMPA receptor
RT   potentiation.";
RL   Neuron 43:563-574(2004).
RN   [6]
RP   FUNCTION.
RX   PubMed=15500970; DOI=10.1016/j.neulet.2004.08.044;
RA   Yang S.-N., Huang C.-B., Yang C.-H., Lai M.-C., Chen W.-F.,
RA   Wang C.-L., Wu C.-L., Huang L.-T.;
RT   "Impaired SynGAP expression and long-term spatial learning and memory
RT   in hippocampal CA1 area from rats previously exposed to perinatal
RT   hypoxia-induced insults: beneficial effects of A68930.";
RL   Neurosci. Lett. 371:73-78(2004).
RN   [7]
RP   INTERACTION WITH KLHL17.
RX   PubMed=16054660; DOI=10.1016/j.neuropharm.2005.05.022;
RA   Chen Y., Li M.;
RT   "Interactions between CAP70 and actinfilin are important for integrity
RT   of actin cytoskeleton structures in neurons.";
RL   Neuropharmacology 49:1026-1041(2005).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=16507876; DOI=10.1074/mcp.D500009-MCP200;
RA   Cheng D., Hoogenraad C.C., Rush J., Ramm E., Schlager M.A.,
RA   Duong D.M., Xu P., Wijayawardana S.R., Hanfelt J., Nakagawa T.,
RA   Sheng M., Peng J.;
RT   "Relative and absolute quantification of postsynaptic density proteome
RT   isolated from rat forebrain and cerebellum.";
RL   Mol. Cell. Proteomics 5:1158-1170(2006).
RN   [9]
RP   FUNCTION.
RX   PubMed=16537406; DOI=10.1073/pnas.0600084103;
RA   Rumbaugh G., Adams J.P., Kim J.H., Huganir R.L.;
RT   "SynGAP regulates synaptic strength and mitogen-activated protein
RT   kinases in cultured neurons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:4344-4351(2006).
CC   -!- FUNCTION: Major constituent of the PSD essential for postsynaptic
CC       signaling. Inhibitory regulator of the Ras-cAMP pathway. Member of
CC       the NMDAR signaling complex in excitatory synapses, it may play a
CC       role in NMDAR-dependent control of AMPAR potentiation, AMPAR
CC       membrane trafficking and synaptic plasticity. Regulates AMPAR-
CC       mediated miniature excitatory postsynaptic currents. May be
CC       involved in certain forms of brain injury, leading to long-term
CC       learning and memory deficits.
CC   -!- SUBUNIT: Isoforms containing the PDZ-binding domain associate with
CC       DLG4 and DLG3 to form the PSD protein complex colocalized with
CC       GRIN2B at synapses. Interacts with MPDZ, KLHL17 CAMK2A and CAMK2B.
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein. Cell
CC       junction, synapse. Note=Mostly in excitatory glutamatergic
CC       synapses.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1;
CC         IsoId=Q9QUH6-1; Sequence=Displayed;
CC       Name=2; Synonyms=SynGAP-a;
CC         IsoId=Q9QUH6-2; Sequence=VSP_026378, VSP_007979;
CC       Name=3; Synonyms=SynGAP-b;
CC         IsoId=Q9QUH6-3; Sequence=VSP_007974;
CC       Name=4; Synonyms=SynGAP-c;
CC         IsoId=Q9QUH6-4; Sequence=VSP_007976, VSP_007980;
CC       Name=5; Synonyms=SynGAP-d, SynGAP-beta;
CC         IsoId=Q9QUH6-5; Sequence=VSP_007975, VSP_007977, VSP_007978;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain; predominantly in
CC       the cortex, hippocampus and olfactory bulb. Present in the
CC       postsynaptic density of central excitatory synapses.
CC   -!- DOMAIN: The PDZ-binding domain interacts with all three PDZ
CC       domains of DGL4.
CC   -!- PTM: Phosphorylated by CaM-kinase II. Dephosphorylated upon NMDA
CC       receptor activation or SYNGAP1/MPDZ complex disruption.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 Ras-GAP domain.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-16 is the initiator
CC       methionine.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC08071.1; Type=Erroneous initiation;
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DR   EMBL; AF048976; AAC08071.1; ALT_INIT; mRNA.
DR   EMBL; AF053938; AAC23491.1; -; mRNA.
DR   EMBL; AF055883; AAC23492.1; -; mRNA.
DR   EMBL; AF058789; AAC63510.2; -; mRNA.
DR   EMBL; AF058790; AAC63511.1; -; mRNA.
DR   EMBL; AF050183; AAC40082.2; -; mRNA.
DR   EMBL; AB016962; BAA74972.1; -; mRNA.
DR   IPI; IPI00212566; -.
DR   IPI; IPI00339023; -.
DR   IPI; IPI00339026; -.
DR   IPI; IPI00339027; -.
DR   IPI; IPI00391507; -.
DR   PIR; T13958; T13958.
DR   PIR; T14259; T14259.
DR   PIR; T14270; T14270.
DR   UniGene; Rn.9908; -.
DR   PDB; 3BXJ; X-ray; 3.00 A; A/B=252-734.
DR   PDBsum; 3BXJ; -.
DR   ProteinModelPortal; Q9QUH6; -.
DR   SMR; Q9QUH6; 401-734.
DR   MINT; MINT-1778299; -.
DR   STRING; Q9QUH6; -.
DR   PhosphoSite; Q9QUH6; -.
DR   Ensembl; ENSRNOT00000040859; ENSRNOP00000044041; ENSRNOG00000000483.
DR   RGD; 621090; Syngap1.
DR   eggNOG; roNOG07298; -.
DR   GeneTree; ENSGT00600000084217; -.
DR   HOVERGEN; HBG006492; -.
DR   InParanoid; Q9QUH6; -.
DR   OrthoDB; EOG49ZXNH; -.
DR   NextBio; 622685; -.
DR   ArrayExpress; Q9QUH6; -.
DR   Genevestigator; Q9QUH6; -.
DR   GermOnline; ENSRNOG00000000483; Rattus norvegicus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR021887; DUF3498.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001936; RasGAP.
DR   InterPro; IPR023152; RasGAP_CS.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR023315; SynGAP_C2_N.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Gene3D; G3DSA:1.10.506.10; RasGAP; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF12004; DUF3498; 1.
DR   Pfam; PF00616; RasGAP; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00323; RasGAP; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50004; C2; FALSE_NEG.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell junction;
KW   Direct protein sequencing; GTPase activation; Membrane;
KW   Phosphoprotein; SH3-binding; Synapse.
FT   CHAIN         1   1308       Ras GTPase-activating protein SynGAP.
FT                                /FTId=PRO_0000056655.
FT   DOMAIN      150    251       PH.
FT   DOMAIN      249    347       C2.
FT   DOMAIN      443    635       Ras-GAP.
FT   REGION     1197   1308       Interaction with MPDZ.
FT   MOTIF       785    815       SH3-binding (Potential).
FT   MOTIF      1305   1308       PDZ-binding (Potential).
FT   VAR_SEQ       1    173       Missing (in isoform 4).
FT                                /FTId=VSP_007976.
FT   VAR_SEQ       1    121       MSRSRASIHRGSIPAMSYAPFRDVRGPPMHRTQYVHSPYDR
FT                                PGWNPRFCIISGNQLLMLDEDEIHPLLIRDRRSESSRNKLL
FT                                RRTVSVPVEGRPHGEHEYHLGRSRRKSVPGGKQYSMEAA
FT                                -> MEYF (in isoform 5).
FT                                /FTId=VSP_007975.
FT   VAR_SEQ       1     98       MSRSRASIHRGSIPAMSYAPFRDVRGPPMHRTQYVHSPYDR
FT                                PGWNPRFCIISGNQLLMLDEDEIHPLLIRDRRSESSRNKLL
FT                                RRTVSVPVEGRPHGEH -> MGLRPPTPTPSGGSGSGSLPP
FT                                PSHRQPLRRRCSSCCFPG (in isoform 3).
FT                                /FTId=VSP_007974.
FT   VAR_SEQ       1     15       Missing (in isoform 2).
FT                                /FTId=VSP_026378.
FT   VAR_SEQ    1195   1196       Missing (in isoform 5).
FT                                /FTId=VSP_007977.
FT   VAR_SEQ    1265   1308       RLMLVEEELRRDHPAMAEPLPEPKKRLLDAQRGSFPPWVQQ
FT                                TRV -> SPSLQADAGGGGAAPGPPRHG (in isoform
FT                                5).
FT                                /FTId=VSP_007978.
FT   VAR_SEQ    1296   1308       RGSFPPWVQQTRV -> LLIR (in isoform 2).
FT                                /FTId=VSP_007979.
FT   VAR_SEQ    1296   1308       RGSFPPWVQQTRV -> VERQLPPLGPTNPRVTLAPPWNGL
FT                                APPAPPPPPRLQITENGEFRNTADH (in isoform 4).
FT                                /FTId=VSP_007980.
FT   CONFLICT    308    309       WG -> GY (in Ref. 1; AA sequence).
FT   CONFLICT    316    316       N -> M (in Ref. 1; AA sequence).
FT   CONFLICT    427    429       HYR -> GQK (in Ref. 1; AA sequence).
FT   CONFLICT    937    939       DGP -> ADG (in Ref. 1; AA sequence).
FT   CONFLICT   1002   1002       H -> G (in Ref. 1; AA sequence).
FT   CONFLICT   1088   1088       S -> Q (in Ref. 1; AA sequence).
FT   CONFLICT   1277   1277       H -> L (in Ref. 1; AA sequence).
FT   STRAND      257    262
FT   STRAND      403    408
FT   HELIX       414    417
FT   HELIX       418    425
FT   HELIX       428    438
FT   HELIX       445    457
FT   HELIX       463    475
FT   STRAND      477    481
FT   STRAND      486    488
FT   HELIX       489    500
FT   HELIX       504    507
FT   HELIX       513    519
FT   TURN        528    530
FT   TURN        533    535
FT   HELIX       536    555
FT   HELIX       556    560
FT   HELIX       563    578
FT   HELIX       582    593
FT   TURN        594    597
FT   HELIX       598    603
FT   HELIX       605    607
FT   HELIX       617    634
FT   TURN        642    645
FT   HELIX       650    656
FT   HELIX       660    666
FT   HELIX       688    699
FT   HELIX       700    702
FT   HELIX       705    710
FT   HELIX       714    724
SQ   SEQUENCE   1308 AA;  144722 MW;  CA2536782C8C4DCB CRC64;
     MSRSRASIHR GSIPAMSYAP FRDVRGPPMH RTQYVHSPYD RPGWNPRFCI ISGNQLLMLD
     EDEIHPLLIR DRRSESSRNK LLRRTVSVPV EGRPHGEHEY HLGRSRRKSV PGGKQYSMEA
     APAAPFRPSQ GFLSRRLKSS IKRTKSQPKL DRTSSFRQIL PRFRSADHDR ARLMQSFKES
     HSHESLLSPS SAAEALELNL DEDSIIKPVH SSILGQEFCF EVTTSSGTKC FACRSAAERD
     KWIENLQRAV KPNKDNSRRV DNVLKLWIIE ARELPPKKRY YCELCLDDML YARTTSKPRS
     ASGDTVFWGE HFEFNNLPAV RALRLHLYRD SDKKRKKDKA GYVGLVTVPV ATLAGRHFTE
     QWYPVTLPTG SGGSGGMGSG GGGGSGGGSG GKGKGGCPAV RLKARYQTMS ILPMELYKEF
     AEYVTNHYRM LCAVLEPALN VKGKEEVASA LVHILQSTGK AKDFLSDMAM SEVDRFMERE
     HLIFRENTLA TKAIEEYMRL IGQKYLKDAI GEFIRALYES EENCEVDPIK CTASSLAEHQ
     ANLRMCCELA LCKVVNSHCV FPRELKEVFA SWRLRCAERG REDIADRLIS ASLFLRFLCP
     AIMSPSLFGL MQEYPDEQTS RTLTLIAKVI QNLANFSKFT SKEDFLGFMN EFLELEWGSM
     QQFLYEISNL DTLTNSSSFE GYIDLGRELS TLHALLWEVL PQLSKEALLK LGPLPRLLSD
     ISTALRNPNI QRQPSRQSER ARSQPMVLRG PSAEMQGYMM RDLNSSIDLQ SFMARGLNSS
     MDMARLPSPT KEKPPPPPPG GGKDLFYVSR PPLARSSPAY CTSSSDITEP EQKMLSVNKS
     VSMLDLQGDG PGGRLNSSSV SNLAAVGDLL HSSQASLTAA LGLRPAPAGR LSQGSGSSIT
     AAGMRLSQMG VTTDGVPAQQ LRIPLSFQNP LFHMAADGPG PPAGHGGSSG HGPPSSHHHH
     HHHHHHRGGE PPGDTFAPFH GYSKSEDLST GVPKPPAASI LHSHSYSDEF GPSGTDFTRR
     QLSLQDNLQH MLSPPQITIG PQRPAPSGPG GGSGGGSGGG GGGQPPPLQR GKSQQLTVSA
     AQKPRPSSGN LLQSPEPSYG PARPRQQSLS KEGSIGGSGG SGGGGGGGLK PSITKQHSQT
     PSTLNPTMPA SERTVAWVSN MPHLSADIES AHIEREEYKL KEYSKSMDES RLDRVKEYEE
     EIHSLKERLH MSNRKLEEYE RRLLSQEEQT SKILMQYQAR LEQSEKRLRQ QQVEKDSQIK
     SIIGRLMLVE EELRRDHPAM AEPLPEPKKR LLDAQRGSFP PWVQQTRV
//
ID   ACSL4_MOUSE             Reviewed;         711 AA.
AC   Q9QUJ7; Q9JHT4; Q9R0H3;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=Long-chain-fatty-acid--CoA ligase 4;
DE            EC=6.2.1.3;
DE   AltName: Full=Long-chain acyl-CoA synthetase 4;
DE            Short=LACS 4;
DE            Short=mACS4;
GN   Name=Acsl4; Synonyms=Acs4, Facl4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RX   MEDLINE=20384168; PubMed=10924347; DOI=10.1006/bbrc.2000.3207;
RA   Cho Y.-Y., Kang M.-J., Ogawa S., Yamashita Y., Fujino T.,
RA   Yamamoto T.T.;
RT   "Regulation by adrenocorticotropic hormone and arachidonate of the
RT   expression of acyl-CoA synthetase 4, an arachidonate-preferring enzyme
RT   expressed in steroidogenic tissues.";
RL   Biochem. Biophys. Res. Commun. 274:741-745(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RC   TISSUE=Embryo;
RX   MEDLINE=20291004; PubMed=10828604;
RA   Vitelli F., Meloni I., Fineschi S., Favara F., Tiziana Storlazzi C.,
RA   Rocchi M., Renieri A.;
RT   "Identification and characterization of mouse orthologs of the AMMECR1
RT   and FACL4 genes deleted in AMME syndrome: orthology of Xq22.3 and
RT   MmuXF1-F3.";
RL   Cytogenet. Cell Genet. 88:259-263(2000).
CC   -!- FUNCTION: Activation of long-chain fatty acids for both synthesis
CC       of cellular lipids, and degradation via beta-oxidation.
CC       Preferentially uses arachidonate and eicosapentaenoate as
CC       substrates.
CC   -!- CATALYTIC ACTIVITY: ATP + a long-chain carboxylic acid + CoA = AMP
CC       + diphosphate + an acyl-CoA.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC       type III membrane protein (By similarity). Peroxisome membrane;
CC       Single-pass type III membrane protein (By similarity). Microsome
CC       membrane; Single-pass type III membrane protein (By similarity).
CC       Endoplasmic reticulum membrane; Single-pass type III membrane
CC       protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=Q9QUJ7-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=Q9QUJ7-2; Sequence=VSP_000239;
CC   -!- TISSUE SPECIFICITY: Abundant in steroidogenic tissues, also found
CC       in the kidney, brain and liver.
CC   -!- INDUCTION: Induced by adrenocorticotropic hormone (ACTH) and
CC       suppressed by glucocorticoid.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family.
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DR   EMBL; AB033887; BAA85931.1; -; mRNA.
DR   EMBL; AB033886; BAA85930.1; -; mRNA.
DR   EMBL; AB033885; BAA85929.1; -; mRNA.
DR   EMBL; AJ243502; CAB95965.1; -; mRNA.
DR   IPI; IPI00131701; -.
DR   IPI; IPI00230141; -.
DR   RefSeq; NP_001028772.1; NM_001033600.1.
DR   RefSeq; NP_062350.3; NM_019477.3.
DR   RefSeq; NP_997508.1; NM_207625.2.
DR   UniGene; Mm.391337; -.
DR   ProteinModelPortal; Q9QUJ7; -.
DR   STRING; Q9QUJ7; -.
DR   PhosphoSite; Q9QUJ7; -.
DR   PRIDE; Q9QUJ7; -.
DR   Ensembl; ENSMUST00000033634; ENSMUSP00000033634; ENSMUSG00000031278.
DR   Ensembl; ENSMUST00000112907; ENSMUSP00000108528; ENSMUSG00000031278.
DR   GeneID; 50790; -.
DR   KEGG; mmu:50790; -.
DR   CTD; 50790; -.
DR   MGI; MGI:1354713; Acsl4.
DR   GeneTree; ENSGT00600000084142; -.
DR   HOGENOM; HBG721674; -.
DR   HOVERGEN; HBG106947; -.
DR   InParanoid; Q9QUJ7; -.
DR   OrthoDB; EOG4SN1N5; -.
DR   PhylomeDB; Q9QUJ7; -.
DR   BRENDA; 6.2.1.3; 244.
DR   NextBio; 307771; -.
DR   ArrayExpress; Q9QUJ7; -.
DR   Bgee; Q9QUJ7; -.
DR   CleanEx; MM_ACSL4; -.
DR   Genevestigator; Q9QUJ7; -.
DR   GermOnline; ENSMUSG00000031278; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005792; C:microsome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IEA:EC.
DR   GO; GO:0060136; P:embryonic process involved in female pregnancy; IMP:MGI.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019217; P:regulation of fatty acid metabolic process; TAS:MGI.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   Pfam; PF00501; AMP-binding; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Alternative splicing; ATP-binding; Endoplasmic reticulum;
KW   Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Membrane;
KW   Microsome; Mitochondrion; Mitochondrion outer membrane;
KW   Nucleotide-binding; Peroxisome; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    711       Long-chain-fatty-acid--CoA ligase 4.
FT                                /FTId=PRO_0000193110.
FT   TRANSMEM      8     28       Helical; Signal-anchor for type III
FT                                membrane protein; (Potential).
FT   TOPO_DOM     29    711       Cytoplasmic (Potential).
FT   MOD_RES      89     89       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1     41       Missing (in isoform Short).
FT                                /FTId=VSP_000239.
FT   CONFLICT    288    288       L -> V (in Ref. 2; CAB95965).
FT   CONFLICT    293    293       T -> S (in Ref. 2; CAB95965).
FT   CONFLICT    430    432       DLV -> ALL (in Ref. 2; CAB95965).
FT   CONFLICT    441    441       Y -> S (in Ref. 2; CAB95965).
FT   CONFLICT    458    458       L -> F (in Ref. 2; CAB95965).
FT   CONFLICT    584    584       F -> S (in Ref. 2; CAB95965).
FT   CONFLICT    704    704       V -> I (in Ref. 2; CAB95965).
SQ   SEQUENCE   711 AA;  79223 MW;  A90EAD489B36C1BB CRC64;
     MNLKLNVLTI ILLPVHLLIT IYSALIFIPW YFLTNAKKKN AMAKRIKAKP TSDKPGSPYR
     SVTHFDSLAV IDIPGADTLD KLFDHAVAKF GKKDSLGTRE ILSEENEMQP NGKVFKKLIL
     GNYKWINYLE VNCRVNNFGS GLTALGLKPK NTIAIFCETR AEWMIAAQTC FKYNFPLVTL
     YATLGREAVV HGLNESEASY LITSVELLES KLKAALVDIN CVKHIIYVDN KTINRAEYPE
     GLEIHSMQSV EELGAKPENL SVPPSRPTPS DMAIVMYTSG STGRPKGLMM HHTNLIAGMT
     GQCERIPGLG PKDTYIGYLP LAHVLELTAE ISCFTYGCRI GYSSPLTLSD QSSKIKKGSK
     GDCTVLKPTL MAAVPEIMDR IYKNVMSKVQ EMNYVQKTLF KIGYDYKLEQ IKKGYDAPLC
     NLILFKKVKD LVGGNVRMML YGGAPLSPQT HRFMNVCLCC PIGQGYGLTE SCGAGTVTEV
     TDYTTGRVGA PLICCEIKLK DWQEGGYTVH DKPNPRGEIV IGGQNISMGY FKNEEKTAED
     YCVDENGQRW FCTGDIGEFH PDGCLQIIDR KKDLVKLQAG EYVFLGKVEA ALKNCPLIDN
     ICAFAKSDQS YVISFVVPNQ KKLTLLAQQK GVEGSWVDIC NNPAMEAEIL KEIREAANAM
     KLERFEIPIK VRLSPEPWTP ETGLVTDAFK LKRKELKNHY LKDVERMYGG K
//
ID   PPCE_MOUSE              Reviewed;         710 AA.
AC   Q9QUR6; Q80YS1;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Prolyl endopeptidase;
DE            Short=PE;
DE            EC=3.4.21.26;
DE   AltName: Full=Post-proline cleaving enzyme;
GN   Name=Prep; Synonyms=Pep;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=98207037; PubMed=9538240;
RA   Ishino T., Ohtsuki S., Homma K., Natori S.;
RT   "cDNA cloning of mouse prolyl endopeptidase and its involvement in DNA
RT   synthesis by Swiss 3T3 cells.";
RL   J. Biochem. 123:540-545(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=99377037; PubMed=10446174; DOI=10.1074/jbc.274.34.24047;
RA   Kimura A., Yoshida I., Takagi N., Takahashi T.;
RT   "Structure and localization of the mouse prolyl oligopeptidase gene.";
RL   J. Biol. Chem. 274:24047-24053(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Limb, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Cleaves peptide bonds on the C-terminal side of prolyl
CC       residues within peptides that are up to approximately 30 amino
CC       acids long.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in
CC       oligopeptides.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the peptidase S9A family.
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DR   EMBL; AB007631; BAA88239.1; -; mRNA.
DR   EMBL; AB022053; BAA83071.1; -; Genomic_DNA.
DR   EMBL; BC012869; AAH12869.1; -; mRNA.
DR   EMBL; BC050830; AAH50830.2; -; mRNA.
DR   IPI; IPI00132089; -.
DR   PIR; JW0080; JW0080.
DR   RefSeq; NP_035286.1; NM_011156.2.
DR   UniGene; Mm.37294; -.
DR   ProteinModelPortal; Q9QUR6; -.
DR   SMR; Q9QUR6; 1-709.
DR   STRING; Q9QUR6; -.
DR   MEROPS; S09.001; -.
DR   PhosphoSite; Q9QUR6; -.
DR   PRIDE; Q9QUR6; -.
DR   Ensembl; ENSMUST00000099858; ENSMUSP00000097444; ENSMUSG00000019849.
DR   GeneID; 19072; -.
DR   KEGG; mmu:19072; -.
DR   UCSC; uc007ezx.1; mouse.
DR   CTD; 19072; -.
DR   MGI; MGI:1270863; Prep.
DR   GeneTree; ENSGT00530000063426; -.
DR   HOVERGEN; HBG007251; -.
DR   InParanoid; Q9QUR6; -.
DR   OrthoDB; EOG4548Z1; -.
DR   PhylomeDB; Q9QUR6; -.
DR   BRENDA; 3.4.21.26; 244.
DR   NextBio; 295594; -.
DR   ArrayExpress; Q9QUR6; -.
DR   Bgee; Q9QUR6; -.
DR   CleanEx; MM_PREP; -.
DR   Genevestigator; Q9QUR6; -.
DR   GermOnline; ENSMUSG00000019849; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   InterPro; IPR002471; Pept_S9_AS.
DR   InterPro; IPR023302; Pept_S9A_oligopept_N.
DR   InterPro; IPR001375; Peptidase_S9.
DR   InterPro; IPR002470; Peptidase_S9A.
DR   InterPro; IPR004106; Peptidase_S9A_B_C_N.
DR   Gene3D; G3DSA:2.130.10.120; Pept_S9A_oligopept_N; 1.
DR   PANTHER; PTHR11757; Peptidase_S9A; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   Pfam; PF02897; Peptidase_S9_N; 1.
DR   PRINTS; PR00862; PROLIGOPTASE.
DR   SUPFAM; SSF50993; Peptidase_S9A_N; 1.
DR   PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cytoplasm; Hydrolase; Protease; Serine protease.
FT   CHAIN         1    710       Prolyl endopeptidase.
FT                                /FTId=PRO_0000122402.
FT   ACT_SITE    554    554       Charge relay system (By similarity).
FT   ACT_SITE    641    641       Charge relay system (By similarity).
FT   ACT_SITE    680    680       Charge relay system (By similarity).
FT   MOD_RES     157    157       N6-acetyllysine (By similarity).
SQ   SEQUENCE   710 AA;  80752 MW;  1B010D5D6CA73C0E CRC64;
     MLSFQYPDVY RDETSVQEYH GHKICDPYSW LEDPDSEQTK AFVEAQNKIT VPFLEQCPIR
     GLYKERMTEL YDYPKYSCHF KKGKRYFYFY NTGLQNQRVL YVQDSLEGEA RVFLDPNTLS
     DDGTVALRGY AFSEDGEYFA YGLSASGSDW VTIKFMKVDG AKELPDVLER VKFTCMAWTH
     DGKGMFYNSY PQQDGKSDGT ETSTNLHQKL CYHVLGTDQS EDILCAEFPD EPKWMGGAEL
     SDDGRYVLLS IWEGCDPVNR LWYCDLQQEP NGITGILKWV KLIDNFEGEY DYVTNEGTVF
     TFKTNRNSPN YRLINIDFTD PDESKWKVLV PEHEKDVLEW VACVRSNFLV LCYLHDVKNI
     LQLHDLTTGA LLKTFPLDVG SVVGYSGRKK DSEIFYQFTS FLSPGVIYHC DLTKEELEPM
     VFREVTVKGI DAADYQTIQI FYPSKDGTKI PMFIVHKKGI KLDGSHPAFL YGYGGFNISI
     TPNYSVSRLI FVRHMGGVLA VANIRGGGEY GETWHKGGIL ANKQNCFDDF QCAAEYLIKE
     GYTSPKRLTI NGGSNGGLLV AACANQRPDL FGCVIAQVGV MDMLKFHKFT IGHAWTTDYG
     CSDTKQHFEW LLKYSPLHNV KLPEADDIQY PSMLLLTADH DDRVVPLHSL KFIATLQYIV
     GRSRKQSNPL LIHVDTKAGH GAGKPTAKVI EEVSDMFAFI ARCLNIEWIQ
//
ID   TRIM1_MOUSE             Reviewed;         705 AA.
AC   Q9QUS6;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Probable E3 ubiquitin-protein ligase MID2;
DE            EC=6.3.2.-;
DE   AltName: Full=Midline defect 2;
DE   AltName: Full=Midline-2;
DE   AltName: Full=Tripartite motif-containing protein 1;
GN   Name=Mid2; Synonyms=Fxy2, Trim1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99330546; PubMed=10400986; DOI=10.1093/hmg/8.8.1397;
RA   Buchner G., Montini E., Andolfi G., Quaderi N., Cainarca S.,
RA   Messali S., Bassi M.T., Ballabio A., Meroni G., Franco B.;
RT   "MID2, a homologue of the Opitz syndrome gene MID1: similarities in a
RT   sub-cellular localization and differences in expression during
RT   development.";
RL   Hum. Mol. Genet. 8:1397-1407(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 13-705.
RX   MEDLINE=20112752; PubMed=10644436; DOI=10.1006/geno.1999.6043;
RA   Perry J., Short K.M., Romer J.T., Swift S., Cox T.C., Ashworth A.;
RT   "FXY2/MID2, a gene related to the X-linked Opitz syndrome gene
RT   FXY/MID1, maps to Xq22 and encodes a FNIII domain-containing protein
RT   that associates with microtubules.";
RL   Genomics 62:385-394(1999).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Homodimer or heterodimer with MID1. Interacts with IGBP1
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton.
CC       Note=Microtubule-associated.
CC   -!- TISSUE SPECIFICITY: Low abundance in brain and lung, with even
CC       lower levels in heart, liver, and kidney.
CC   -!- DEVELOPMENTAL STAGE: At E10.5, a very low level is mostly confined
CC       to the central nervous system and the developing heart and kidney,
CC       while at later stages it is present in other organ systems.
CC   -!- DOMAIN: The tripartite motif (RBCC; RING- and B box-type zinc
CC       fingers and coiled coil domains) mediates dimerization (By
CC       similarity).
CC   -!- DOMAIN: Associates with microtubules in a manner that is dependent
CC       on the C-terminal B30.2 domain.
CC   -!- PTM: Phosphorylated on serine and threonine residues (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC   -!- SIMILARITY: Contains 2 B box-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 B30.2/SPRY domain.
CC   -!- SIMILARITY: Contains 1 COS domain.
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-21 is the initiator.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF07340.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=CAB56170.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; Y18881; CAB56170.1; ALT_INIT; mRNA.
DR   EMBL; AF196480; AAF07340.1; ALT_INIT; mRNA.
DR   IPI; IPI00755362; -.
DR   RefSeq; NP_035975.1; NM_011845.2.
DR   UniGene; Mm.131097; -.
DR   ProteinModelPortal; Q9QUS6; -.
DR   SMR; Q9QUS6; 19-104, 107-252, 396-674.
DR   STRING; Q9QUS6; -.
DR   PhosphoSite; Q9QUS6; -.
DR   PRIDE; Q9QUS6; -.
DR   Ensembl; ENSMUST00000112990; ENSMUSP00000108614; ENSMUSG00000000266.
DR   Ensembl; ENSMUST00000112993; ENSMUSP00000108617; ENSMUSG00000000266.
DR   GeneID; 23947; -.
DR   KEGG; mmu:23947; -.
DR   UCSC; uc009uld.1; mouse.
DR   CTD; 23947; -.
DR   MGI; MGI:1344333; Mid2.
DR   eggNOG; roNOG08128; -.
DR   GeneTree; ENSGT00580000081333; -.
DR   HOVERGEN; HBG056432; -.
DR   OrthoDB; EOG44J2HG; -.
DR   PhylomeDB; Q9QUS6; -.
DR   NextBio; 303761; -.
DR   ArrayExpress; Q9QUS6; -.
DR   Bgee; Q9QUS6; -.
DR   CleanEx; MM_MID2; -.
DR   Genevestigator; Q9QUS6; -.
DR   GermOnline; ENSMUSG00000000266; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001870; B302/SPRY.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR003879; Butyrophylin.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR017903; COS_domain.
DR   InterPro; IPR008957; Fibronectin_III_dom.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR018355; SPla/RYanodine_receptor_sg.
DR   InterPro; IPR003877; SPRY_rcpt.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   PRINTS; PR01407; BUTYPHLNCDUF.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 2.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
DR   SUPFAM; SSF49265; FN_III-like; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS51262; COS; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Ligase; Metal-binding;
KW   Microtubule; Phosphoprotein; Repeat; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    705       Probable E3 ubiquitin-protein ligase
FT                                MID2.
FT                                /FTId=PRO_0000056194.
FT   DOMAIN      340    399       COS.
FT   DOMAIN      398    501       Fibronectin type-III.
FT   DOMAIN      486    679       B30.2/SPRY.
FT   ZN_FING      30     80       RING-type.
FT   ZN_FING     137    184       B box-type 1; degenerate.
FT   ZN_FING     190    232       B box-type 2.
FT   COILED      233    301       Potential.
SQ   SEQUENCE   705 AA;  79774 MW;  141D80291912FA6B CRC64;
     MGESPASAVL NASAGLFSLK METLESELTC PICLELFEDP LLLPCAHSLC FSCAHRILVS
     SCSSGESIEP ITAFQCPTCR YVISLNHRGL DGLKRNVTLQ NIIDRFQKAS VSGPNSPSES
     RRERTYRPSS AMSSERIACQ FCEQDPPRDA VKTCITCEVS YCDRCLRATH PNKKPFTSHR
     LVEPVSDTHL RGITCLDHEN EKVNMYCVSD DQLICALCKL VGRHRDHQVA SLNDRFEKLK
     QTLEMNLTNL VKRNSELENQ MAKLIQICQQ VEVNTAMHEA KLMEECDELV EIIQQRKQMI
     AVKIKETKVM KLRKLAQQVA NCRQCLERST VLINQAEHIL KENDQARFLQ SAKNIAERVA
     MATASSQVLI PDINFNDAFE NFALDFSREK KLLEGLDYLT APNPPSIREE LCTASHDTIT
     VHWISDDEFS ISSYELQYTI FTGQANFISL YNSVDSWMIV PNIKQNHYTV HGLQSGTRYI
     FIVKAINQAG SRNSEPTRLK TNSQPFKLDP KMTHKKLKIS NDGLQMEKDE SSLKKSHTPE
     RFSGTGCYGA AGNIFIDSGC HYWEVVMGSS TWYAIGIAYK SAPKNEWIGK NASSWVFSRC
     NSNFVVRHNN KEMLVDVPPQ LKRLGVLLDY DNNMLSFYDP ANSLHLHTFD VTFILPVCPT
     FTIWNKSLMI LSGLPAPDFI DYPERQECNC RPQESPYVSG MKACH
//
ID   FAK2_MOUSE              Reviewed;        1009 AA.
AC   Q9QVP9; B2RQ16;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 110.
DE   RecName: Full=Protein-tyrosine kinase 2-beta;
DE            EC=2.7.10.2;
DE   AltName: Full=Calcium-dependent tyrosine kinase;
DE            Short=CADTK;
DE   AltName: Full=Cell adhesion kinase beta;
DE            Short=CAK-beta;
DE   AltName: Full=Focal adhesion kinase 2;
DE            Short=FADK 2;
DE   AltName: Full=Proline-rich tyrosine kinase 2;
DE   AltName: Full=Related adhesion focal tyrosine kinase;
DE            Short=RAFTK;
GN   Name=Ptk2b; Synonyms=Fak2, Pyk2, Raftk;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=96070905; PubMed=7499242; DOI=10.1074/jbc.270.46.27742;
RA   Avraham S., London R., Fu Y., Ota S., Hiregowdara D., Li J., Jiang S.,
RA   Pasztor L.M., White R.A., Groopman J.E., Avraham H.;
RT   "Identification and characterization of a novel related adhesion focal
RT   tyrosine kinase (RAFTK) from megakaryocytes and brain.";
RL   J. Biol. Chem. 270:27742-27751(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 469-479, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   INTERACTION WITH TGFB1I1.
RX   MEDLINE=98086276; PubMed=9422762; DOI=10.1074/jbc.273.2.1003;
RA   Matsuya M., Sasaki H., Aoto H., Mitaka T., Nagura K., Ohba T.,
RA   Ishino M., Takahashi S., Suzuki R., Sasaki T.;
RT   "Cell adhesion kinase beta forms a complex with a new member, Hic-5,
RT   of proteins localized at focal adhesions.";
RL   J. Biol. Chem. 273:1003-1014(1998).
RN   [5]
RP   INTERACTION WITH PTPNS1.
RX   MEDLINE=99401000; PubMed=10469599; DOI=10.1016/S0960-9822(99)80401-1;
RA   Timms J.F., Swanson K.D., Marie-Cardine A., Raab M., Rudd C.E.,
RA   Schraven B., Neel B.G.;
RT   "SHPS-1 is a scaffold for assembling distinct adhesion-regulated
RT   multi-protein complexes in macrophages.";
RL   Curr. Biol. 9:927-930(1999).
RN   [6]
RP   PHOSPHORYLATION AT TYR-402; TYR-580 AND TYR-881.
RX   MEDLINE=21313779; PubMed=11420674; DOI=10.1038/sj.onc.1204359;
RA   Nakamura K., Yano H., Schaefer E., Sabe H.;
RT   "Different modes and qualities of tyrosine phosphorylation of Fak and
RT   Pyk2 during epithelial-mesenchymal transdifferentiation and cell
RT   migration: analysis of specific phosphorylation events using site-
RT   directed antibodies.";
RL   Oncogene 20:2626-2635(2001).
RN   [7]
RP   PHOSPHORYLATION AT TYR-402, AND INTERACTION WITH NEPHROCYSTIN.
RX   MEDLINE=21396557; PubMed=11493697; DOI=10.1073/pnas.171269898;
RA   Benzing T., Gerke P., Hoepker K., Hildebrandt F., Kim E., Walz G.;
RT   "Nephrocystin interacts with Pyk2, p130(Cas), and tensin and triggers
RT   phosphorylation of Pyk2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9784-9789(2001).
RN   [8]
RP   INTERACTION WITH SH2D3C.
RX   MEDLINE=22476996; PubMed=12486027; DOI=10.1074/jbc.M207942200;
RA   Sakakibara A., Hattori S., Nakamura S., Katagiri T.;
RT   "A novel hematopoietic adaptor protein, Chat-H, positively regulates T
RT   cell receptor-mediated interleukin-2 production by Jurkat cells.";
RL   J. Biol. Chem. 278:6012-6017(2003).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-402; TYR-579 AND
RP   TYR-580, AND MASS SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-440, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Involved in calcium induced regulation of ion channel
CC       and activation of the map kinase signaling pathway. May represent
CC       an important signaling intermediate between neuropeptide activated
CC       receptors or neurotransmitters that increase calcium flux and the
CC       downstream signals that regulate neuronal activity. Interacts with
CC       the SH2 domain of Grb2. May phosphorylate the voltage-gated
CC       potassium channel protein Kv1.2. Its activation is highly
CC       correlated with the stimulation of c-Jun N-terminal kinase
CC       activity. Involved in osmotic stress-dependent SNCA 'Tyr-125'
CC       phosphorylation (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- SUBUNIT: Interacts with ASAP2 and SKAP2 (By similarity). Interacts
CC       with Crk-associated substrate (Cas), PTPNS1, nephrocystin, OPHN1L,
CC       SH2D3C and TGFB1I1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Note=Interaction
CC       with nephrocystin induces the membrane-association of the kinase.
CC   -!- PTM: Phosphorylated on tyrosine residues in response to various
CC       stimuli that elevate the intracellular calcium concentration, as
CC       well as by PKC activation. Recruitment by nephrocystin to cell
CC       matrix adhesions initiates Tyr-402 phosphorylation. In monocytes,
CC       adherence to substrata is required for tyrosine phosphorylation
CC       and kinase activation. Angiotensin II, thapsigargin and L-alpha-
CC       lysophosphatidic acid (LPA) also induce autophosphorylation and
CC       increase kinase activity (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. FAK subfamily.
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; BC137704; AAI37705.1; -; mRNA.
DR   EMBL; BC144849; AAI44850.1; -; mRNA.
DR   IPI; IPI00133132; -.
DR   UniGene; Mm.21613; -.
DR   ProteinModelPortal; Q9QVP9; -.
DR   SMR; Q9QVP9; 39-692, 867-1007.
DR   MINT; MINT-266339; -.
DR   STRING; Q9QVP9; -.
DR   PhosphoSite; Q9QVP9; -.
DR   PRIDE; Q9QVP9; -.
DR   Ensembl; ENSMUST00000022622; ENSMUSP00000022622; ENSMUSG00000059456.
DR   MGI; MGI:104908; Ptk2b.
DR   GeneTree; ENSGT00600000084269; -.
DR   HOGENOM; HBG444482; -.
DR   HOVERGEN; HBG004018; -.
DR   InParanoid; Q9QVP9; -.
DR   BRENDA; 2.7.10.2; 244.
DR   ArrayExpress; Q9QVP9; -.
DR   Bgee; Q9QVP9; -.
DR   CleanEx; MM_PTK2B; -.
DR   Genevestigator; Q9QVP9; -.
DR   GermOnline; ENSMUSG00000059456; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:EC.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0007172; P:signal complex assembly; IEA:InterPro.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR005189; Focal_adhesion_kin_target_dom.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr-Pkinase.
DR   InterPro; IPR020635; Tyr_Pkinase_cat_dom.
DR   InterPro; IPR008266; Tyr_prot_kinase_AS.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF03623; Focal_AT; 1.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   ProDom; PD006413; Focal_adhesion_target_reg; 1.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   SUPFAM; SSF68993; Focal_AT; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00660; FERM_1; FALSE_NEG.
DR   PROSITE; PS00661; FERM_2; FALSE_NEG.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Cytoplasm; Direct protein sequencing;
KW   Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Transferase;
KW   Tyrosine-protein kinase.
FT   CHAIN         1   1009       Protein-tyrosine kinase 2-beta.
FT                                /FTId=PRO_0000088082.
FT   DOMAIN       39    359       FERM.
FT   DOMAIN      425    683       Protein kinase.
FT   NP_BIND     431    439       ATP (By similarity).
FT   REGION      801   1009       Interaction with TGFB1I1 (By similarity).
FT   REGION      868   1009       Focal adhesion targeting (FAT).
FT   COMPBIAS    701    767       Pro-rich.
FT   COMPBIAS    831    869       Pro-rich.
FT   ACT_SITE    549    549       Proton acceptor (By similarity).
FT   BINDING     457    457       ATP (By similarity).
FT   MOD_RES       2      2       Phosphoserine (By similarity).
FT   MOD_RES      15     15       Phosphothreonine (By similarity).
FT   MOD_RES     361    361       Phosphoserine (By similarity).
FT   MOD_RES     375    375       Phosphoserine.
FT   MOD_RES     389    389       Phosphoserine (By similarity).
FT   MOD_RES     392    392       Phosphoserine (By similarity).
FT   MOD_RES     394    394       Phosphoserine (By similarity).
FT   MOD_RES     396    396       Phosphoserine (By similarity).
FT   MOD_RES     399    399       Phosphoserine (By similarity).
FT   MOD_RES     402    402       Phosphotyrosine.
FT   MOD_RES     440    440       Phosphotyrosine.
FT   MOD_RES     559    559       Phosphoserine (By similarity).
FT   MOD_RES     579    579       Phosphotyrosine; by autocatalysis.
FT   MOD_RES     580    580       Phosphotyrosine.
FT   MOD_RES     583    583       Phosphoserine (By similarity).
FT   MOD_RES     722    722       Phosphotyrosine (By similarity).
FT   MOD_RES     746    746       Phosphoserine (By similarity).
FT   MOD_RES     758    758       Phosphoserine (By similarity).
FT   MOD_RES     762    762       Phosphoserine (By similarity).
FT   MOD_RES     765    765       Phosphothreonine (By similarity).
FT   MOD_RES     778    778       Phosphoserine (By similarity).
FT   MOD_RES     834    834       Phosphotyrosine (By similarity).
FT   MOD_RES     839    839       Phosphoserine (By similarity).
FT   MOD_RES     842    842       Phosphothreonine (By similarity).
FT   MOD_RES     849    849       Phosphotyrosine (By similarity).
FT   MOD_RES     866    866       Phosphoserine (By similarity).
FT   MOD_RES     881    881       Phosphotyrosine.
FT   MOD_RES     966    966       Phosphothreonine (By similarity).
SQ   SEQUENCE   1009 AA;  115822 MW;  963959FF56DF9605 CRC64;
     MSGVSEPLSR VKVGTLRRPE GPPEPMVVVP VDVEKEDVRI LKVCFYSNSF NPGKNFKLVK
     CTVQTEIQEI ITSILLSGRI GPNIQLAECY GLRLKHMKSD EIHWLHPQMT VGEVQDKYEC
     LHVEAEWRYD LQIRYLPEDF MESLKEDRTT LLYFYQQLRN DYMQRYASKV SEGMALQLGC
     LELRRFFKDM PHNALDKKSN FELLEKEVGL DLFFPKQMQE NLKPKQFRKM IQQTFQQYAS
     LREEECVMKF FNTLAGFANI DQETYRCELI QGWNITVDLV IGPKGIRQLT SQDTKPTCLA
     EFKQIRSIRC LPLEETQAVL QLGIEGAPQS LSIKTSSLAE AENMADLIDG YCRLQGEHKG
     SLIMHAKKDG EKRNSLPQIP TLNLEARRSH LSESCSIESD IYAEIPDETL RRPGGPQYGV
     AREEVVLNRI LGEGFFGEVY EGVYTNHKGE KINVAVKTCK KDCTQDNKEK FMSEAVIMKN
     LDHPHIVKLI GIIEEEPTWI IMELYPYGEL GHYLERNKNS LKVPTLVLYT LQICKAMAYL
     ESINCVHRDI AVRNILVASP ECVKLGDFGL SRYIEDEDYY KASVTRLPIK WMSPESINFR
     RFTTASDVWM FAVCMWEILS FGKQPFFWLE NKDVIGVLEK GDRLPKPELC PPVLYTLMTR
     CWDYDPSDRP RFTELVCSLS DIYQMEKDIA IEQERNARYR PPKILEPTTF QEPPPKPSRP
     KYRPPPQTNL LAPKLQFQVP EGLCASSPTL TSPMEYPSPV NSLHTPPLHR HNVFKRHSMR
     EEDFIRPSSR EEAQQLWEAE KIKMKQVLER QQKQMVEDSQ WLRREERCLD PMVYMNDKSP
     LTPEKEAGYT EFTGPPQKPP RLGAQSIQPT ANLDRTDDLV YHNVMTLVEA VLELKNKLGQ
     LPPEDYVVVV KNVGLNLRKL IGSVDDLLPS LPASSRTEIE GTQKLLNKDL AELINKMKLA
     QQNAVTSLSE DCKRQMLTAS HTLAVDAKNL LDAVDQAKVV ANLAHPPAE
//
ID   SRCN1_MOUSE             Reviewed;        1250 AA.
AC   Q9QWI6; O70298;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 2.
DT   08-FEB-2011, entry version 77.
DE   RecName: Full=SRC kinase signaling inhibitor 1;
DE   AltName: Full=SNAP-25-interacting protein;
DE            Short=SNIP;
DE   AltName: Full=p130Cas-associated protein;
DE   AltName: Full=p140Cap;
GN   Name=Srcin1; Synonyms=Kiaa1684, P140;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA   Croci L., Bossolasco M., Consalez G.G.;
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 271-1250 (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX   PubMed=14657239; DOI=10.1091/mbc.E03-09-0689;
RA   Di Stefano P., Cabodi S., Erba E.B., Margaria V., Bergatto E.,
RA   Giuffrida M.G., Silengo L., Tarone G., Turco E., Defilippi P.;
RT   "p130Cas-associated protein (p140Cap) as a new tyrosine-phosphorylated
RT   protein involved in cell spreading.";
RL   Mol. Biol. Cell 15:787-800(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1054, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233; SER-411; SER-588;
RP   SER-933; SER-1054 AND SER-1110, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309 AND TYR-464, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293; SER-375; SER-430;
RP   SER-579; SER-670; THR-704 AND SER-1054, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-98 AND SER-1054,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [10]
RP   TISSUE SPECIFICITY.
RX   PubMed=19146815; DOI=10.1016/j.neuron.2008.11.013;
RA   Jaworski J., Kapitein L.C., Gouveia S.M., Dortland B.R., Wulf P.S.,
RA   Grigoriev I., Camera P., Spangler S.A., Di Stefano P., Demmers J.,
RA   Krugers H., Defilippi P., Akhmanova A., Hoogenraad C.C.;
RT   "Dynamic microtubules regulate dendritic spine morphology and synaptic
RT   plasticity.";
RL   Neuron 61:85-100(2009).
CC   -!- FUNCTION: Acts as a negative regulator of SRC by activating CSK
CC       which inhibits SRC activity and downstream signaling, leading to
CC       impaired cell spreading and migration. Regulates dendritic spine
CC       morphology. Involved in calcium-dependent exocytosis. May play a
CC       role in neurotransmitter release or synapse maintenance (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with the N-terminal coiled-coil region of
CC       SNAP25. Interacts with BCAR1/p130Cas and SRC through its C-
CC       terminal domain. Interacts with CSK, CTTN, SORBS3/vinexin, SYP and
CC       MAPRE3/EB3 (By similarity).
CC   -!- INTERACTION:
CC       P56945:BCAR1 (xeno); NbExp=1; IntAct=EBI-775592, EBI-702093;
CC       Q61140:Bcar1; NbExp=1; IntAct=EBI-775592, EBI-77088;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity). Cell projection, axon (By
CC       similarity). Cell projection, dendrite (By similarity). Cell
CC       junction, synapse (By similarity). Cell junction, synapse,
CC       postsynaptic cell membrane, postsynaptic density (By similarity).
CC       Note=Localized to the perinuclear region, lamellopodia, cortical
CC       actin and actin stress fibers but not to focal adhesions. Strongly
CC       expressed in axons and dendrites of the CA1 and CA3 hippocampal
CC       regions and of the dentate gyrus. Detected in both pre- and post-
CC       synapses and in post-synaptic density fractions (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=1a;
CC         IsoId=Q9QWI6-1; Sequence=Displayed;
CC       Name=2; Synonyms=1b;
CC         IsoId=Q9QWI6-2; Sequence=VSP_050631;
CC       Name=3;
CC         IsoId=Q9QWI6-3; Sequence=VSP_050632;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in central nervous
CC       system with high levels detected in cortex, cerebellum, midbrain
CC       and spinal cord (at protein level). Also expressed in testis and
CC       epithelial-rich tissues such as mammary gland, lung and kidney.
CC   -!- PTM: Tyrosine-phosphorylated in response to EGF and to cell
CC       adhesion to integrin ligands (By similarity).
CC   -!- SIMILARITY: Belongs to the SRCIN1 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98232.1; Type=Frameshift; Positions=483, 527;
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DR   EMBL; AF040944; AAC15635.1; -; mRNA.
DR   EMBL; U59873; AAD00087.1; -; mRNA.
DR   EMBL; AK129422; BAC98232.1; ALT_FRAME; mRNA.
DR   IPI; IPI00396743; -.
DR   IPI; IPI00467346; -.
DR   IPI; IPI00828414; -.
DR   PIR; T34101; T34101.
DR   RefSeq; NP_061361.2; NM_018873.2.
DR   UniGene; Mm.342665; -.
DR   ProteinModelPortal; Q9QWI6; -.
DR   IntAct; Q9QWI6; 64.
DR   MINT; MINT-4135063; -.
DR   STRING; Q9QWI6; -.
DR   PhosphoSite; Q9QWI6; -.
DR   PRIDE; Q9QWI6; -.
DR   Ensembl; ENSMUST00000064145; ENSMUSP00000065424; ENSMUSG00000038453.
DR   Ensembl; ENSMUST00000107595; ENSMUSP00000103221; ENSMUSG00000038453.
DR   GeneID; 56013; -.
DR   KEGG; mmu:56013; -.
DR   CTD; 56013; -.
DR   MGI; MGI:1933179; Srcin1.
DR   eggNOG; roNOG12795; -.
DR   GeneTree; ENSGT00390000012399; -.
DR   HOGENOM; HBG505832; -.
DR   HOVERGEN; HBG019587; -.
DR   InParanoid; Q9QWI6; -.
DR   NextBio; 311742; -.
DR   ArrayExpress; Q9QWI6; -.
DR   Bgee; Q9QWI6; -.
DR   Genevestigator; Q9QWI6; -.
DR   GermOnline; ENSMUSG00000038453; Mus musculus.
DR   GO; GO:0030424; C:axon; ISS:UniProtKB.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0007162; P:negative regulation of cell adhesion; IDA:MGI.
DR   GO; GO:0061099; P:negative regulation of protein tyrosine kinase activity; ISS:UniProtKB.
DR   GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISS:UniProtKB.
DR   GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR   GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR   InterPro; IPR022782; AIP3_C.
DR   Pfam; PF03915; AIP3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Exocytosis; Membrane;
KW   Phosphoprotein; Postsynaptic cell membrane; Synapse.
FT   CHAIN         1   1250       SRC kinase signaling inhibitor 1.
FT                                /FTId=PRO_0000072012.
FT   REGION      681    731       Interaction with SNAP25 (By similarity).
FT   COILED      627    654       Potential.
FT   COILED      716    741       Potential.
FT   COILED      783    845       Potential.
FT   COMPBIAS   1023   1081       Pro-rich.
FT   MOD_RES      79     79       Phosphoserine.
FT   MOD_RES      98     98       Phosphoserine.
FT   MOD_RES     208    208       Phosphoserine.
FT   MOD_RES     233    233       Phosphoserine.
FT   MOD_RES     293    293       Phosphoserine.
FT   MOD_RES     309    309       Phosphotyrosine.
FT   MOD_RES     375    375       Phosphoserine.
FT   MOD_RES     411    411       Phosphoserine.
FT   MOD_RES     430    430       Phosphoserine.
FT   MOD_RES     464    464       Phosphotyrosine.
FT   MOD_RES     579    579       Phosphoserine.
FT   MOD_RES     588    588       Phosphoserine.
FT   MOD_RES     670    670       Phosphoserine.
FT   MOD_RES     704    704       Phosphothreonine.
FT   MOD_RES     933    933       Phosphoserine.
FT   MOD_RES     974    974       Phosphoserine.
FT   MOD_RES    1054   1054       Phosphoserine.
FT   MOD_RES    1110   1110       Phosphoserine.
FT   VAR_SEQ       1     41       MQPWQCLRRFALAWWERTAEGRARSPREEVGPRDPGGRGEP
FT                                -> MGNAPSQ (in isoform 2).
FT                                /FTId=VSP_050631.
FT   VAR_SEQ    1207   1250       Missing (in isoform 3).
FT                                /FTId=VSP_050632.
FT   CONFLICT    740    741       NV -> KL (in Ref. 2; BAC98232).
FT   CONFLICT    755    755       P -> R (in Ref. 2; BAC98232).
FT   CONFLICT    759    760       DV -> EL (in Ref. 2; BAC98232).
FT   CONFLICT    821    821       M -> V (in Ref. 2; BAC98232).
FT   CONFLICT    960    960       C -> G (in Ref. 2; BAC98232).
FT   CONFLICT   1121   1122       KL -> NV (in Ref. 1; AAD00087).
SQ   SEQUENCE   1250 AA;  134859 MW;  85F394C9523F78C0 CRC64;
     MQPWQCLRRF ALAWWERTAE GRARSPREEV GPRDPGGRGE PDPERSSPPM LSADDAEYPR
     EYRTLGGGGG GGSGGRRFSN VGLVHTSERR HTVIAAQSLE ALSGLQKADA DRKRDAFMDH
     LKSKYPQHAL ALRGQQDRMR EQVGGWTVDP VCLLSSLCSH LHGDSTPSGA GQPAQQPNYW
     SFKTRSSRHT QGAQPGLADQ AAKLSYASAE SLETMSEAEL PLGFSRMNRF RQSLPLSRSA
     SQTKLRSPGV LFLQFGEETR RVHITHEVSS LDTLHALIAH MFPQKLTMGM LKSPNTAILI
     KDEARNVFYE LEDVRDIQDR SIIKIYRKEP LYAAFPGSHL TNGDLRREMV YASRESSPTR
     RLNNLSPASH LASSSPPPGL PSGLPSGLPS GSPSRSRLSY AGGRPPSYAG SPVHHAAERL
     GGAPTGQGVS PSPSAILERR DVKPDEDLAG KAGGMVLVKG EGLYADPYGL LHEGRLSLAA
     AAETHSHTRA RAACTSGVPC ALSAPTPLPR CSPTWRTRCT RRALAALYGD GYGFRLPPSS
     PQKLADVSAP SGGPPPPHSP YSGPPSRGSP VRQSFRKDSG SSSVFAESPG GKARSTGSAS
     TAGAPPSELF PGPGERSLVG FGPPVPAKDT ETRERMEAME KQIASLTGLV QSALLRGSEP
     ETPSEKVEGS NGAATPSAPV CGSGSKSSGA TPVSGPPPPS ASSTPAGQPT AVSRLQMQLH
     LRGLQNSASD LRGQLQQLRN VQLQNQESVR ALLKPTEADV SMRVSEAARR QEDPLQRQRT
     LVEEERLRYL NDEELITQQL NDLEKSVEKI QRDVAHNHRL MPGPELEEKA LVLKQLGETL
     TELKAHFPGL QSKMRVVLRV EVEAVKFLKE EPQRLDGLLK RCRGVTDTLA QIRRQVDEGM
     WPPPNNLLNQ SPKKVAAETD FSKGLDFEIP PPSPPLNLHE LSGPAEGTPL TPKSTNPTKC
     LDASSKRNTD KAVSVEAAER DWEEKRAALT QYSAKDINRL LEETQAELLK AIPDLDCASK
     THPGPAPTPD HKPPKAPHGQ KAAPRTEPSG RRGSDELTVP RYRTEKPSKS PPPPPPRRSF
     PSSHGLTTTR TGEVVVTSKK DSVFIKKAES EELEVQKPQV KLRRAVSEVV RPASTPPIMA
     SAIKDEDDEE RIIAELESGG SSVPPMKVVT PGASRLKAAQ GPAGSPDKGK HGKQRTEYMR
     IQAQQQATKP SKEVSGPNET SSPGSEKPSG SRTSIPVLTS FGARNSSISF
//
ID   K1C17_MOUSE             Reviewed;         433 AA.
AC   Q9QWL7; A2A4G6; Q61783;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Keratin, type I cytoskeletal 17;
DE   AltName: Full=Cytokeratin-17;
DE            Short=CK-17;
DE   AltName: Full=Keratin-17;
DE            Short=K17;
GN   Name=Krt17; Synonyms=Krt1-17;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, DEVELOPMENTAL
RP   STAGE, AND INDUCTION.
RC   STRAIN=129/SvJ;
RX   MEDLINE=99003303; PubMed=9786956; DOI=10.1083/jcb.143.2.469;
RA   McGowan K.M., Coulombe P.A.;
RT   "Onset of keratin 17 expression coincides with the definition of major
RT   epithelial lineages during skin development.";
RL   J. Cell Biol. 143:469-486(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/10J; TISSUE=Skin;
RX   MEDLINE=99189238; PubMed=10087197; DOI=10.1006/geno.1998.5721;
RA   Sato H., Koide T., Sagai T., Ishiguro S., Tamai M., Saitou N.,
RA   Shiroishi T.;
RT   "The genomic organization of type I keratin genes in mice.";
RL   Genomics 56:303-309(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 95-101; 164-170; 285-297 AND 377-385, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 229-433, TISSUE SPECIFICITY, AND
RP   INDUCTION.
RC   TISSUE=Skin;
RX   MEDLINE=87109202; PubMed=2433272;
RA   Knapp B., Rentrop M., Schweizer J., Winter H.;
RT   "Three cDNA sequences of mouse type I keratins: cellular localization
RT   of the mRNAs in normal and hyperproliferative tissues.";
RL   J. Biol. Chem. 262:938-945(1987).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=10844551; DOI=10.1046/j.1523-1747.2000.00986.x;
RA   McGowan K.M., Coulombe P.A.;
RT   "Keratin 17 expression in the hard epithelial context of the hair and
RT   nail, and its relevance for the pachyonychia congenita phenotype.";
RL   J. Invest. Dermatol. 114:1101-1107(2000).
RN   [8]
RP   FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ARG-94.
RX   PubMed=14714564; DOI=10.1111/j.0906-6705.2003.00099.x;
RA   Fan W., Yoon K.;
RT   "In vivo alteration of the keratin 17 gene in hair follicles by
RT   oligonucleotide-directed gene targeting.";
RL   Exp. Dermatol. 12:832-842(2003).
RN   [9]
RP   FUNCTION, INTERACTION WITH TRADD, AND SUBCELLULAR LOCATION.
RX   PubMed=16702408; DOI=10.1101/gad.1387406;
RA   Tong X., Coulombe P.A.;
RT   "Keratin 17 modulates hair follicle cycling in a TNFalpha-dependent
RT   fashion.";
RL   Genes Dev. 20:1353-1364(2006).
RN   [10]
RP   FUNCTION, INTERACTION WITH SFN, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP   OF THR-9 AND SER-44.
RX   PubMed=16710422; DOI=10.1038/nature04659;
RA   Kim S., Wong P., Coulombe P.A.;
RT   "A keratin cytoskeletal protein regulates protein synthesis and
RT   epithelial cell growth.";
RL   Nature 441:362-365(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: May play a role in the formation and maintenance of
CC       various skin appendages, specifically in determining shape and
CC       orientation of hair. Required for the correct growth of hair
CC       follicles, in particular for the persistence of the anagen
CC       (growth) state. Modulates the function of TNF-alpha in the
CC       specific context of hair cycling. Regulates protein synthesis and
CC       epithelial cell growth through binding to the adapter protein SFN
CC       and by stimulating Akt/mTOR pathway. Involved in tissue repair.
CC       May be a marker of basal cell differentiation in complex epithelia
CC       and therefore indicative of a certain type of epithelial "stem
CC       cells". May act as an autoantigen in the immunopathogenesis of
CC       psoriasis, with certain peptide regions being a major target for
CC       autoreactive T-cells and hence causing their proliferation (By
CC       similarity).
CC   -!- SUBUNIT: Heterodimer of a type I and a type II keratin. KRT17
CC       associates with KRT6 isomers (By similarity). Interacts with TRADD
CC       and SFN.
CC   -!- INTERACTION:
CC       O70456:Sfn; NbExp=2; IntAct=EBI-309015, EBI-1544118;
CC       Q3U0V2:Tradd; NbExp=1; IntAct=EBI-309015, EBI-1544032;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Expressed strongly in outer root sheath and
CC       medulla region of hair follicle and in the early differentiating
CC       epithelial cells (trichocytes) within the hair bulb region. Weak
CC       expression in the matrix cells of hair bulb. Also present in the
CC       sweat gland within the skin, vibrissae follicle, salivary gland,
CC       tooth and thymus.
CC   -!- DEVELOPMENTAL STAGE: Expression first occurs in a subset of
CC       epithelial cells within the single-layered, undifferentiated
CC       ectoderm of embryonic day 10.5 mouse fetuses. In the ensuing 48
CC       hours, K17-expressing cells give rise to placodes, the precursors
CC       of ectoderm-derived appendages (hair, glands, and tooth), and to
CC       periderm.
CC   -!- INDUCTION: Induced in damaged or stressed epidermis and by
CC       interferon-gamma. Up-regulated by LEF1.
CC   -!- MISCELLANEOUS: There are two types of cytoskeletal and
CC       microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to
CC       basic; 56-70 kDa).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AB013608; BAA34229.1; -; mRNA.
DR   EMBL; AL590873; CAM17780.1; -; Genomic_DNA.
DR   EMBL; BC132454; AAI32455.1; -; mRNA.
DR   EMBL; BC132456; AAI32457.1; -; mRNA.
DR   EMBL; M13805; AAA39394.1; -; mRNA.
DR   IPI; IPI00230365; -.
DR   PIR; C26135; C26135.
DR   RefSeq; NP_034793.1; NM_010663.2.
DR   UniGene; Mm.14046; -.
DR   ProteinModelPortal; Q9QWL7; -.
DR   SMR; Q9QWL7; 82-119, 126-232, 248-318, 322-394.
DR   IntAct; Q9QWL7; 7.
DR   STRING; Q9QWL7; -.
DR   PhosphoSite; Q9QWL7; -.
DR   PRIDE; Q9QWL7; -.
DR   Ensembl; ENSMUST00000080893; ENSMUSP00000079699; ENSMUSG00000035557.
DR   GeneID; 16667; -.
DR   KEGG; mmu:16667; -.
DR   UCSC; uc007lks.1; mouse.
DR   CTD; 16667; -.
DR   MGI; MGI:96691; Krt17.
DR   eggNOG; roNOG12467; -.
DR   GeneTree; ENSGT00560000076946; -.
DR   HOGENOM; HBG715391; -.
DR   HOVERGEN; HBG013015; -.
DR   InParanoid; Q9QWL7; -.
DR   OMA; NYSSCYS; -.
DR   OrthoDB; EOG483D4W; -.
DR   PhylomeDB; Q9QWL7; -.
DR   NextBio; 290383; -.
DR   ArrayExpress; Q9QWL7; -.
DR   Bgee; Q9QWL7; -.
DR   CleanEx; MM_KRT17; -.
DR   Genevestigator; Q9QWL7; -.
DR   GermOnline; ENSMUSG00000035557; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0045109; P:intermediate filament organization; IGI:MGI.
DR   GO; GO:0031424; P:keratinization; IGI:MGI.
DR   GO; GO:0002009; P:morphogenesis of an epithelium; IGI:MGI.
DR   GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
DR   GO; GO:0051798; P:positive regulation of hair follicle development; IMP:UniProtKB.
DR   GO; GO:0045727; P:positive regulation of translation; IMP:UniProtKB.
DR   InterPro; IPR016044; F.
DR   InterPro; IPR001664; IF.
DR   InterPro; IPR018039; Intermediate_filament_CS.
DR   InterPro; IPR002957; Keratin_I.
DR   InterPro; IPR009053; Prefoldin.
DR   PANTHER; PTHR23239; IF; 1.
DR   Pfam; PF00038; Filament; 1.
DR   PRINTS; PR01248; TYPE1KERATIN.
DR   SUPFAM; SSF46579; Prefoldin; 1.
DR   PROSITE; PS00226; IF; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Direct protein sequencing;
KW   Intermediate filament; Keratin; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    433       Keratin, type I cytoskeletal 17.
FT                                /FTId=PRO_0000063665.
FT   REGION        2     83       Head.
FT   REGION       84    392       Rod.
FT   REGION       84    120       Coil 1A.
FT   REGION      121    138       Linker 1.
FT   REGION      139    230       Coil 1B.
FT   REGION      231    250       Linker 12.
FT   REGION      251    392       Coil 2.
FT   REGION      393    433       Tail.
FT   MOD_RES      12     12       Phosphoserine (By similarity).
FT   MOD_RES      13     13       Phosphoserine (By similarity).
FT   MOD_RES      32     32       Phosphoserine (By similarity).
FT   MOD_RES      39     39       Phosphoserine (By similarity).
FT   MOD_RES     319    319       Phosphoserine.
FT   MOD_RES     398    398       Phosphotyrosine (By similarity).
FT   MUTAGEN       9      9       T->A: Reduces binding to SNF.
FT   MUTAGEN      44     44       S->A: Reduces binding to SNF.
FT   MUTAGEN      94     94       R->P: Causes twisted hair shafts, broken
FT                                hair follicles at sebaceous gland level
FT                                and occasional rupture of the hair bulb
FT                                or epidermal cyst-like changes.
SQ   SEQUENCE   433 AA;  48162 MW;  279081DF2ECE105D CRC64;
     MTTTIRQFTS SSSIKGSSGL GGGSSRTSCR LSGSLGAGSC RLGSASGLGS ALGSNSYSSC
     YSFGTGSGYG GNFGGVDGLL AGGEKATMQN LNDRLASYLD KVRALEEANT ELEVKIRDWY
     QKQAPGPARD YSAYYHTIED LKNKILVATV DNASILLQID NARLAADDFR TKFETEQALR
     MSVEADINGL RRVLDELTLA RADLEMQIEN LKEELAYLKK NHEEEMNALR GQVGGEINVE
     MDAAPGVDLS RILSEMRDQY EKMAEKNRKD AEDWFFSKTE ELNREVATNS ELVQSGKSEI
     SELRRTMQAL EIELQSQLSM KASLEGSLAE TENRYCVQLS QIQGLIGSVE EQLAQLRCEM
     EQQNQEYKIL LDVKTRLEQE IATYRRLLEG EDAHLTQYKP KEPVTTRQVR TIVEEVQDGK
     VISSREQVHQ TTR
//
ID   MLF1_MOUSE              Reviewed;         267 AA.
AC   Q9QWV4; O70217;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Myeloid leukemia factor 1;
DE   AltName: Full=Hematopoietic lineage switch 7;
DE   AltName: Full=Myelodysplasia-myeloid leukemia factor 1;
GN   Name=Mlf1; Synonyms=Hls7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   MEDLINE=99324296; PubMed=10393836;
RA   Hitzler J.K., Witte D.P., Jenkins N.A., Copeland N.G., Gilbert D.J.,
RA   Naeve C.W., Look A.T., Morris S.W.;
RT   "cDNA cloning, expression pattern, and chromosomal localization of
RT   Mlf1, murine homologue of a gene involved in myelodysplasia and acute
RT   myeloid leukemia.";
RL   Am. J. Pathol. 155:53-59(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Embryo;
RX   MEDLINE=99452763; PubMed=10523300; DOI=10.1093/emboj/18.20.5559;
RA   Williams J.H., Daly L.N., Ingley E., Beaumont J.G., Tilbrook P.A.,
RA   Lalonde J.-P., Stillitano J.P., Klinken S.P.;
RT   "HLS7, a hemopoietic lineage switch gene homologous to the leukemia-
RT   inducing gene MLF1.";
RL   EMBO J. 18:5559-5566(1999).
RN   [3]
RP   INTERACTION WITH NRBP1 AND YWHAZ, SUBCELLULAR LOCATION, AND
RP   PHOSPHORYLATION.
RX   MEDLINE=22287351; PubMed=12176995; DOI=10.1074/jbc.M206041200;
RA   Lim R., Winteringham L.N., Williams J.H., McCulloch R.K., Ingley E.,
RA   Tiao J.Y.-H., Lalonde J.-P., Tsai S., Tilbrook P.A., Sun Y., Wu X.,
RA   Morris S.W., Klinken S.P.;
RT   "MADM, a novel adaptor protein that mediates phosphorylation of the
RT   14-3-3 binding site of myeloid leukemia factor 1.";
RL   J. Biol. Chem. 277:40997-41008(2002).
RN   [4]
RP   FUNCTION.
RX   PubMed=15122318; DOI=10.1038/sj.onc.1207661;
RA   Winteringham L.N., Kobelke S., Williams J.H., Ingley E., Klinken S.P.;
RT   "Myeloid leukemia factor 1 inhibits erythropoietin-induced
RT   differentiation, cell cycle exit and p27Kip1 accumulation.";
RL   Oncogene 23:5105-5109(2004).
RN   [5]
RP   INTERACTION WITH HNRPUL2 AND YWHAZ, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF SER-34 AND SER-149.
RX   PubMed=17008314; DOI=10.1074/jbc.M605401200;
RA   Winteringham L.N., Endersby R., Kobelke S., McCulloch R.K.,
RA   Williams J.H., Stillitano J., Cornwall S.M., Ingley E., Klinken S.P.;
RT   "Myeloid leukemia factor 1 associates with a novel heterogeneous
RT   nuclear ribonucleoprotein U-like molecule.";
RL   J. Biol. Chem. 281:38791-38800(2006).
CC   -!- FUNCTION: Involved in lineage commitment of primary hemopoietic
CC       progenitors by restricting erythroid formation and enhancing
CC       myeloid formation. Interferes with erythropoietin-induced
CC       erythroid terminal differentiation by preventing cells from
CC       exiting the cell cycle through suppression of CDKN1B/p27Kip1
CC       levels. Suppresses RFWD2/COP1 activity via CSN3 which activates
CC       p53 and induces cell cycle arrest. Binds DNA and affects the
CC       expression of a number of genes so may function as a transcription
CC       factor in the nucleus.
CC   -!- SUBUNIT: Interacts with MLF1IP (By similarity). Also interacts
CC       with NRBP1/MADM, YWHAZ/14-3-3-zeta and HNRPUL2/MANP. NRBP1
CC       recruits a serine kinase which phosphorylates both itself and
CC       MLF1. Phosphorylated MLF1 then binds to YWHAZ and is retained in
CC       the cytoplasm. Retained in the nucleus by binding to HNRPUL2.
CC       Binds to COPS3/CSN3 which is required for suppression of RFWD2 and
CC       activation of p53.
CC   -!- INTERACTION:
CC       Q99J45:Nrbp1; NbExp=3; IntAct=EBI-354765, EBI-767484;
CC       P63101:Ywhaz; NbExp=1; IntAct=EBI-354765, EBI-354751;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=In non-
CC       hematopoietic cells, resides primarily in the cytoplasm with some
CC       punctate nuclear localization. Shuttles between the cytoplasm and
CC       nucleus. In hematopoietic cells, located preferentially in the
CC       nucleus.
CC   -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle, heart,
CC       testis. Also found in lung, but not in spleen, thymus, bone
CC       marrow, liver and kidney.
CC   -!- PTM: Phosphorylation is required for binding to YWHAZ.
CC   -!- SIMILARITY: Belongs to the MLF family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF100171; AAD02876.1; -; mRNA.
DR   EMBL; AF009515; AAC17946.1; -; mRNA.
DR   IPI; IPI00475175; -.
DR   RefSeq; NP_034931.2; NM_010801.3.
DR   UniGene; Mm.10414; -.
DR   ProteinModelPortal; Q9QWV4; -.
DR   IntAct; Q9QWV4; 13.
DR   STRING; Q9QWV4; -.
DR   PhosphoSite; Q9QWV4; -.
DR   PRIDE; Q9QWV4; -.
DR   Ensembl; ENSMUST00000077916; ENSMUSP00000077072; ENSMUSG00000048416.
DR   GeneID; 17349; -.
DR   KEGG; mmu:17349; -.
DR   NMPDR; fig|10090.3.peg.8160; -.
DR   UCSC; uc008pll.1; mouse.
DR   CTD; 17349; -.
DR   MGI; MGI:1341819; Mlf1.
DR   eggNOG; roNOG05693; -.
DR   GeneTree; ENSGT00390000005023; -.
DR   HOVERGEN; HBG019060; -.
DR   NextBio; 291942; -.
DR   ArrayExpress; Q9QWV4; -.
DR   Bgee; Q9QWV4; -.
DR   CleanEx; MM_MLF1; -.
DR   Genevestigator; Q9QWV4; -.
DR   GermOnline; ENSMUSG00000048416; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0007050; P:cell cycle arrest; ISS:UniProtKB.
DR   GO; GO:0002318; P:myeloid progenitor cell differentiation; IDA:UniProtKB.
DR   GO; GO:0006350; P:transcription; IDA:UniProtKB.
DR   InterPro; IPR019376; Myeloid_leukemia_factor.
DR   Pfam; PF10248; Mlf1IP; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cytoplasm; Developmental protein; Differentiation;
KW   DNA-binding; Nucleus; Phosphoprotein.
FT   CHAIN         1    267       Myeloid leukemia factor 1.
FT                                /FTId=PRO_0000220753.
FT   REGION       50    125       Interaction with COPS3 (By similarity).
FT   MUTAGEN      34     34       S->A: 70% reduction in binding to YWHAZ
FT                                and increased nuclear localization.
FT   MUTAGEN     149    149       S->A: No effect on binding to YWHAZ.
FT   CONFLICT    172    172       N -> Y (in Ref. 2; AAC17946).
FT   CONFLICT    214    214       N -> H (in Ref. 2; AAC17946).
SQ   SEQUENCE   267 AA;  30432 MW;  0DEF99C708CBE6B8 CRC64;
     MFRMLSSSFE DDPFFADSFL AHRESMRNMM RSFSEPLGRD LLSISDGRGR THNRRERDDG
     EDSLTHADVN PFQTMDRMMA NMRSGIQELQ RNFGQLSMDP NGHSFCSSSV MTYSKVGDEP
     PKVFQASTQT RRAPGGVKET RKAMRDSDSG LERMAVGHHI HDRGHVIRKS KNNKTGDEEV
     NQEFINMNES DAHAFDDEWQ NEVLKYKSIG RSGNTGMRSV GHEHPGSREL KRREKIHRNS
     AIESGRRSNV FVDKLNVKGS PVKITKK
//
ID   HOME2_MOUSE             Reviewed;         354 AA.
AC   Q9QWW1; O89025; Q9Z0E4;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Homer protein homolog 2;
DE            Short=Homer-2;
DE   AltName: Full=Cupidin;
DE   AltName: Full=VASP/Ena-related gene up-regulated during seizure and LTP 2;
DE            Short=Vesl-2;
GN   Name=Homer2; Synonyms=Vesl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Forebrain;
RX   MEDLINE=99023644; PubMed=9808458; DOI=10.1016/S0896-6273(00)80588-7;
RA   Xiao B., Tu J.C., Petralia R.S., Yuan J.P., Doan A., Breder C.D.,
RA   Ruggiero A., Lanahan A.A., Wenthold R.J., Worley P.F.;
RT   "Homer regulates the association of group 1 metabotropic glutamate
RT   receptors with multivalent complexes of homer-related, synaptic
RT   proteins.";
RL   Neuron 21:707-716(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Cerebellum;
RA   Shiraishi Y., Mizutani A., Furuichi T.;
RT   "Cupidin, a gene transiently expressed in developing cerebellar
RT   granule cells.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-192.
RA   Keen J., Inglehearn C.;
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   INTERACTION WITH GRM1; GRM5; DYN3 AND ITPR1, AND TISSUE SPECIFICITY.
RX   MEDLINE=99023645; PubMed=9808459; DOI=10.1016/S0896-6273(00)80589-9;
RA   Tu J.C., Xiao B., Yuan J.P., Lanahan A.A., Leoffert K., Li M.,
RA   Linden D.J., Worley P.F.;
RT   "Homer binds a novel proline-rich motif and links group 1 metabotropic
RT   glutamate receptors with IP3 receptors.";
RL   Neuron 21:717-726(1998).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.24 ANGSTROMS) OF 2-111.
RX   PubMed=11491285; DOI=10.1006/jmbi.2001.4640;
RA   Barzik M., Carl U.D., Schubert W.-D., Frank R., Wehland J.,
RA   Heinz D.W.;
RT   "The N-terminal domain of Homer/Vesl is a new class II EVH1 domain.";
RL   J. Mol. Biol. 309:155-169(2001).
CC   -!- FUNCTION: Postsynaptic density scaffolding protein. Binds and
CC       cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1,
CC       RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with
CC       ER-associated ITPR1 receptors, it aids the coupling of surface
CC       receptors to intracellular calcium release. May also couple GRM1
CC       to PI3 kinase through its interaction with AGAP2. Isoforms can be
CC       differently regulated and may play an important role in
CC       maintaining the plasticity at glutamatergic synapses.
CC   -!- SUBUNIT: Isoform 1 and isoform 2 encode coiled-coil structures
CC       that mediate homo- and heteromultimerization.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell junction, synapse,
CC       postsynaptic cell membrane, postsynaptic density. Cell junction,
CC       synapse. Note=Postsynaptic density of neuronal cells. The
CC       stabilization and clustering of the metabotropic glutamate
CC       receptors appears to be mediated by isoform 1 and isoform 2 at the
CC       cell surface.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=2b;
CC         IsoId=Q9QWW1-1; Sequence=Displayed;
CC       Name=2; Synonyms=2a;
CC         IsoId=Q9QWW1-2; Sequence=VSP_009071;
CC   -!- TISSUE SPECIFICITY: Expressed in olfactory bulb, hippocampus,
CC       thalmus and heart.
CC   -!- SIMILARITY: Belongs to the Homer family.
CC   -!- SIMILARITY: Contains 1 WH1 domain.
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DR   EMBL; AF093259; AAC71023.1; -; mRNA.
DR   EMBL; AF093260; AAC71024.1; -; mRNA.
DR   EMBL; AB017136; BAA37088.1; -; mRNA.
DR   EMBL; AJ012076; CAA09909.1; -; mRNA.
DR   IPI; IPI00134508; -.
DR   IPI; IPI00395070; -.
DR   RefSeq; NP_001157558.1; NM_001164086.1.
DR   RefSeq; NP_001157559.1; NM_001164087.1.
DR   RefSeq; NP_036113.1; NM_011983.2.
DR   UniGene; Mm.228; -.
DR   PDB; 1I7A; X-ray; 2.24 A; A/B/C/D=1-111.
DR   PDBsum; 1I7A; -.
DR   ProteinModelPortal; Q9QWW1; -.
DR   SMR; Q9QWW1; 3-111, 287-352.
DR   STRING; Q9QWW1; -.
DR   PRIDE; Q9QWW1; -.
DR   Ensembl; ENSMUST00000026922; ENSMUSP00000026922; ENSMUSG00000025813.
DR   GeneID; 26557; -.
DR   KEGG; mmu:26557; -.
DR   UCSC; uc009ich.1; mouse.
DR   UCSC; uc009ici.1; mouse.
DR   CTD; 26557; -.
DR   MGI; MGI:1347354; Homer2.
DR   eggNOG; roNOG12514; -.
DR   GeneTree; ENSGT00390000017850; -.
DR   HOGENOM; HBG443677; -.
DR   HOVERGEN; HBG051918; -.
DR   InParanoid; Q9QWW1; -.
DR   OMA; DLHDFRR; -.
DR   OrthoDB; EOG4DFPNT; -.
DR   PhylomeDB; Q9QWW1; -.
DR   NextBio; 304611; -.
DR   ArrayExpress; Q9QWW1; -.
DR   Bgee; Q9QWW1; -.
DR   CleanEx; MM_HOMER2; -.
DR   Genevestigator; Q9QWW1; -.
DR   GermOnline; ENSMUSG00000025813; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IDA:MGI.
DR   GO; GO:0030160; F:GKAP/Homer scaffold activity; IDA:MGI.
DR   GO; GO:0007216; P:metabotropic glutamate receptor signaling pathway; TAS:MGI.
DR   InterPro; IPR000697; EVH1.
DR   InterPro; IPR011993; PH_type.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00568; WH1; 1.
DR   SMART; SM00461; WH1; 1.
DR   PROSITE; PS50229; WH1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW   Coiled coil; Cytoplasm; Membrane; Postsynaptic cell membrane; Synapse.
FT   CHAIN         1    354       Homer protein homolog 2.
FT                                /FTId=PRO_0000191009.
FT   DOMAIN        1    110       WH1.
FT   COILED      160    329       Potential.
FT   VAR_SEQ     130    140       Missing (in isoform 2).
FT                                /FTId=VSP_009071.
FT   CONFLICT    191    192       RE -> VP (in Ref. 3; CAA09909).
FT   STRAND        6     15
FT   STRAND       32     39
FT   TURN         40     43
FT   STRAND       44     51
FT   STRAND       54     61
FT   STRAND       67     79
FT   TURN         80     83
FT   STRAND       84     89
FT   HELIX        93    110
SQ   SEQUENCE   354 AA;  40570 MW;  18AF2F22EA8E1D06 CRC64;
     MGEQPIFTTR AHVFQIDPST KKNWVPASKQ AVTVSYFYDV TRNSYRIISV DGAKVIINST
     ITPNMTFTKT SQKFGQWADS RANTVFGLGF SSELQLTKFA EKFQEVREAA RLARDKSQEK
     TETSSNHSQE SGCETPSSTQ ASSVNGTDDE KASHASPADT HLKSENDKLK IALTQSAANV
     KKWEMELQTL RESNARLTTA LQESAASVEQ WKRQFSICRD ENDRLRSKIE ELEEQCSEIN
     REKEKNTQLK RRIEELESEV RDKEMELKDL RKQSEIIPQL MSECEYVSEK LEAAERDNQN
     LEDKVRSLKT DIEESKYRQR HLKGELKSFL EVLDGKIDDL HDFRRGLSKL GTDN
//
ID   ASAP1_MOUSE             Reviewed;        1147 AA.
AC   Q9QWY8; O08612; Q80TG8; Q80UV6; Q99LV8; Q9Z2B6;
DT   26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1;
DE   AltName: Full=130 kDa phosphatidylinositol 4,5-biphosphate-dependent ARF1 GTPase-activating protein;
DE   AltName: Full=ADP-ribosylation factor-directed GTPase-activating protein 1;
DE            Short=ARF GTPase-activating protein 1;
DE   AltName: Full=Development and differentiation-enhancing factor 1;
DE            Short=DEF-1;
DE            Short=Differentiation-enhancing factor 1;
DE   AltName: Full=PIP2-dependent ARF1 GAP;
GN   Name=Asap1; Synonyms=Ddef1, Kiaa1249, Shag1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), CHARACTERIZATION, AND
RP   MUTAGENESIS OF ARG-811; PRO-910 AND PRO-913.
RC   TISSUE=Brain, and Embryo;
RX   MEDLINE=99038209; PubMed=9819391;
RA   Brown M.T., Andrade J., Radhakrishna H., Donaldson J.G., Cooper J.A.,
RA   Randazzo P.A.;
RT   "ASAP1, a phospholipid-dependent arf GTPase-activating protein that
RT   associates with and is phosphorylated by Src.";
RL   Mol. Cell. Biol. 18:7038-7051(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 57-1147 (ISOFORM 3).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 654-1147 (ISOFORM 1).
RX   MEDLINE=97271433; PubMed=9126384; DOI=10.1006/abio.1997.2040;
RA   Yamabhai M., Kay B.K.;
RT   "Examining the specificity of Src homology 3 domain -- ligand
RT   interactions with alkaline phosphatase fusion proteins.";
RL   Anal. Biochem. 247:143-151(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-1147 (ISOFORM 4), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 722-1147 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=99147067; PubMed=10022919;
RA   King F.J., Hu E., Harris D.F., Sarraf P., Spiegelman B.M.,
RA   Roberts T.M.;
RT   "DEF-1, a novel src SH3 binding protein that promotes adipogenesis in
RT   fibroblastic cell lines.";
RL   Mol. Cell. Biol. 19:2330-2337(1999).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-858, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-732, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   INTERACTION WITH RAB11FIP3.
RX   PubMed=18685082; DOI=10.1091/mbc.E08-03-0290;
RA   Inoue H., Ha V.L., Prekeris R., Randazzo P.A.;
RT   "Arf GTPase-activating protein ASAP1 interacts with Rab11 effector
RT   FIP3 and regulates pericentrosomal localization of transferrin
RT   receptor-positive recycling endosome.";
RL   Mol. Biol. Cell 19:4224-4237(2008).
CC   -!- FUNCTION: May function as a signal transduction protein involved
CC       in the differentiation of fibroblasts into adipocytes and possibly
CC       other cell types (By similarity). Posseses phosphatidylinositol
CC       4,5-biphosphate-dependent GTPase-activating protein activity for
CC       ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity
CC       towards ARF6. May coordinate membrane trafficking with cell growth
CC       or actin cytoskeleton remodeling by binding to both SRC and PIP2.
CC   -!- ENZYME REGULATION: Activity stimulated by phosphatidylinositol
CC       4,5-biphosphate (PIP2).
CC   -!- SUBUNIT: Homodimer. Interacts with SRC and CRK. Interacts with
CC       RAB11FIP3.
CC   -!- INTERACTION:
CC       P84077:ARF1 (xeno); NbExp=1; IntAct=EBI-698498, EBI-447171;
CC       P84080:ARF1 (xeno); NbExp=2; IntAct=EBI-698498, EBI-449051;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane. Note=Predominantly
CC       cytoplasmic. Partially membrane-associated.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=SHAG1a, ASAP1a;
CC         IsoId=Q9QWY8-1; Sequence=Displayed;
CC       Name=2; Synonyms=SHAG1b, ASAP1b;
CC         IsoId=Q9QWY8-2; Sequence=VSP_008368;
CC       Name=3;
CC         IsoId=Q9QWY8-3; Sequence=VSP_008366;
CC       Name=4;
CC         IsoId=Q9QWY8-4; Sequence=VSP_008367;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined but a most
CC       abundant expression was found in the testis, brain, lung and
CC       spleen. A heightened expression was seen in the adipose tissue
CC       from obese (ob) and diabetic (db) animals.
CC   -!- DOMAIN: The PH domain most probably contributes to the
CC       phosphoinositide-dependent regulation of ADP ribosylation factors.
CC   -!- PTM: Phosphorylated on tyrosine residues by SRC.
CC   -!- SIMILARITY: Contains 2 ANK repeats.
CC   -!- SIMILARITY: Contains 1 Arf-GAP domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH02201.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC       Sequence=AAH48818.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF075461; AAC98349.1; -; mRNA.
DR   EMBL; AF075462; AAC98350.1; -; mRNA.
DR   EMBL; AK122477; BAC65759.1; -; mRNA.
DR   EMBL; U92478; AAB82338.1; -; mRNA.
DR   EMBL; BC002201; AAH02201.1; ALT_INIT; mRNA.
DR   EMBL; BC048818; AAH48818.1; ALT_INIT; mRNA.
DR   IPI; IPI00134544; -.
DR   IPI; IPI00349032; -.
DR   IPI; IPI00349033; -.
DR   IPI; IPI00468726; -.
DR   PIR; T42627; T42627.
DR   UniGene; Mm.277236; -.
DR   ProteinModelPortal; Q9QWY8; -.
DR   SMR; Q9QWY8; 341-443, 452-724, 1085-1147.
DR   IntAct; Q9QWY8; 28.
DR   MINT; MINT-266354; -.
DR   STRING; Q9QWY8; -.
DR   PhosphoSite; Q9QWY8; -.
DR   PRIDE; Q9QWY8; -.
DR   Ensembl; ENSMUST00000023008; ENSMUSP00000023008; ENSMUSG00000022377.
DR   Ensembl; ENSMUST00000110114; ENSMUSP00000105741; ENSMUSG00000022377.
DR   Ensembl; ENSMUST00000110115; ENSMUSP00000105742; ENSMUSG00000022377.
DR   UCSC; uc007vzh.1; mouse.
DR   UCSC; uc007vzj.1; mouse.
DR   UCSC; uc007vzl.1; mouse.
DR   MGI; MGI:1342335; Asap1.
DR   GeneTree; ENSGT00600000084109; -.
DR   HOGENOM; HBG444660; -.
DR   HOVERGEN; HBG051327; -.
DR   InParanoid; Q9QWY8; -.
DR   OrthoDB; EOG4PC9RD; -.
DR   PMAP-CutDB; Q9QWY8; -.
DR   ArrayExpress; Q9QWY8; -.
DR   Bgee; Q9QWY8; -.
DR   Genevestigator; Q9QWY8; -.
DR   GermOnline; ENSMUSG00000022377; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008060; F:ARF GTPase activator activity; IEA:InterPro.
DR   GO; GO:0008093; F:cytoskeletal adaptor activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0046847; P:filopodium assembly; IEA:InterPro.
DR   GO; GO:0032312; P:regulation of ARF GTPase activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR001164; ArfGAP.
DR   InterPro; IPR013606; IRSp53/MIM_homology_IMD.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Gene3D; G3DSA:1.20.1270.80; IRSp53/MIM_homology_IMD; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF01412; ArfGap; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00405; REVINTRACTNG.
DR   SMART; SM00248; ANK; 2.
DR   SMART; SM00105; ArfGap; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF57863; ArfGAP; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS50115; ARFGAP; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ANK repeat; Cytoplasm; GTPase activation;
KW   Membrane; Metal-binding; Phosphoprotein; Repeat; SH3 domain; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1147       Arf-GAP with SH3 domain, ANK repeat and
FT                                PH domain-containing protein 1.
FT                                /FTId=PRO_0000074197.
FT   DOMAIN      339    431       PH.
FT   DOMAIN      454    577       Arf-GAP.
FT   REPEAT      615    647       ANK 1.
FT   REPEAT      651    680       ANK 2.
FT   DOMAIN     1085   1147       SH3.
FT   ZN_FING     469    492       C4-type.
FT   COMPBIAS    798   1011       Pro-rich.
FT   MOD_RES     732    732       Phosphoserine.
FT   MOD_RES     854    854       Phosphoserine (By similarity).
FT   MOD_RES     858    858       Phosphoserine.
FT   MOD_RES    1026   1026       Phosphoserine (By similarity).
FT   MOD_RES    1045   1045       Phosphoserine (By similarity).
FT   VAR_SEQ     304    318       Missing (in isoform 4).
FT                                /FTId=VSP_008367.
FT   VAR_SEQ     304    315       Missing (in isoform 3).
FT                                /FTId=VSP_008366.
FT   VAR_SEQ     816    872       Missing (in isoform 2).
FT                                /FTId=VSP_008368.
FT   MUTAGEN     811    811       R->A: Significant reduction in binding to
FT                                SRC and CRK and loss of phosphorylation.
FT                                Loss of binding and phosphorylation; when
FT                                associated with A-910 and A-913.
FT   MUTAGEN     910    910       P->A: Significant reduction in binding to
FT                                SRC and CRK and decrease in
FT                                phosphorylation; when associated with A-
FT                                913. Loss of binding and phosphorylation;
FT                                when associated with A-811 and A-913.
FT   MUTAGEN     913    913       P->A: Significant reduction in binding to
FT                                SRC and CRK and decrease in
FT                                phosphorylation; when associated with A-
FT                                910. Loss of binding and phosphorylation;
FT                                when associated with A-811 and A-910.
FT   CONFLICT    654    654       T -> S (in Ref. 3; AAB82338).
FT   CONFLICT    879    879       S -> L (in Ref. 3; AAB82338 and 4;
FT                                AAH02201/AAH48818).
FT   CONFLICT   1051   1051       R -> I (in Ref. 3; AAB82338).
SQ   SEQUENCE   1147 AA;  127395 MW;  1A08321C491B4609 CRC64;
     MRSSASRLSS FSSRDSLWNR MPDQISVSEF IAETTEDYNS PTTSSFTTRL HNCRNTVTLL
     EEALDQDRTA LQKVKKSVKA IYNSGQDHVQ NEENYAQVLD KFGSNFLSRD NPDLGTAFVK
     FSTLTKELST LLKNLLQGLS HNVIFTLDSL LKGDLKGVKG DLKKPFDKAW KDYETKFTKI
     EKEKREHAKQ HGMIRTEITG AEIAEEMEKE RRLFQLQMCE YLIKVNEIKT KKGVDLLQNL
     IKYYHAQCNF FQDGLKTADK LKQYIEKLAA DLYNIKQTQD EEKKQLTALR DLIKSSLQLD
     PKEVGGLYVA SRANSSRRDS QSRQGGYSMH QLQGNKEYGS EKKGFLLKKS DGIRKVWQRR
     KCAVKNGILT ISHATSNRQP AKLNLLTCQV KPNAEDKKSF DLISHNRTYH FQAEDEQDYI
     AWISVLTNSK EEALTMAFRG EQSTGENSLE DLTKAIIEDV QRLPGNDICC DCGSSEPTWL
     STNLGILTCI ECSGIHREMG VHISRIQSLE LDKLGTSELL LAKNVGNNSF NDIMEANLPS
     PSPKPTPSSD MTVRKEYITA KYVDHRFSRK TCASSSAKLN ELLEAIKSRD LLALIQVYAE
     GVELMEPLLE PGQELGETAL HLAVRTADQT SLHLVDFLVQ NCGNLDKQTS VGNTVLHYCS
     MYGKPECLKL LLRSKPTVDI VNQNGETALD IAKRLKATQC EDLLSQAKSG KFNPHVHVEY
     EWNLRQDEMD ESDDDLDDKP SPIKKERSPR PQSFCHSSSI SPQDKLALPG FSTPRDKQRL
     SYGAFTNQIF ASTSTDLPTS PTSEAPPLPP RNAGKGPTGP PSTLPLGTQT SSGSSTLSKK
     RPPPPPPGHK RTLSDPPSPL PHGPPNKGAI PWGNDVGPSS SSKTANKFEG LSQQASTSSA
     KTALGPRVLP KLPQKVALRK TETSHHLSLD RTNIPPETFQ KSSQLTELPQ KPPLGELPPK
     PVELAPKPQV GELPPKPGEL PPKPQLGDLP PKPQLSDLPP KPQMKDLPPK PQLGDLLAKS
     QAGDVSAKVQ PPSEVTQRSH TGDLSPNVQS RDAIQKQASE DSNDLTPTLP ETPVPLPRKI
     NTGKNKVRRV KTIYDCQADN DDELTFIEGE VIIVTGEEDQ EWWIGHIEGQ PERKGVFPVS
     FVHILSD
//
ID   CYH1_MOUSE              Reviewed;         398 AA.
AC   Q9QX11; O88817;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Cytohesin-1;
DE   AltName: Full=PH, SEC7 and coiled-coil domain-containing protein 1;
DE            Short=CLM1;
DE   AltName: Full=SEC7 homolog A;
DE            Short=mSec7-1;
GN   Name=Cyth1; Synonyms=Pscd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   MEDLINE=98416066; PubMed=9744817; DOI=10.1016/S0014-5793(98)00937-5;
RA   Kim H.-S., Chen Y., Lonai P.;
RT   "Complex regulation of multiple cytohesin-like genes in murine tissues
RT   and cells.";
RL   FEBS Lett. 433:312-316(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=B10D2/NSNJ; TISSUE=Lymph node;
RX   MEDLINE=98435526; PubMed=9745014; DOI=10.1007/s002510050444;
RA   O'Rourke A.M., Escuro G., Feeney A.J.;
RT   "Cloning and sequencing of cDNA encoding mouse cytohesin-1.";
RL   Immunogenetics 48:354-355(1998).
CC   -!- FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF5.
CC       Promotes the activation of ARF through replacement of GDP with
CC       GTP.
CC   -!- SUBUNIT: Interacts with TRIM23 and CYTIP (By similarity).
CC   -!- INTERACTION:
CC       Q9QXJ2:Stat2; NbExp=2; IntAct=EBI-646678, EBI-646643;
CC   -!- SUBCELLULAR LOCATION: Cell membrane (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9QX11-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9QX11-2; Sequence=VSP_006035;
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 SEC7 domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB013464; BAA33428.1; -; mRNA.
DR   EMBL; AF051337; AAC71694.1; -; mRNA.
DR   IPI; IPI00315867; -.
DR   IPI; IPI00752843; -.
DR   RefSeq; NP_001106169.1; NM_001112699.1.
DR   UniGene; Mm.86413; -.
DR   ProteinModelPortal; Q9QX11; -.
DR   SMR; Q9QX11; 58-391.
DR   IntAct; Q9QX11; 2.
DR   STRING; Q9QX11; -.
DR   PhosphoSite; Q9QX11; -.
DR   PRIDE; Q9QX11; -.
DR   Ensembl; ENSMUST00000106305; ENSMUSP00000101912; ENSMUSG00000017132.
DR   GeneID; 19157; -.
DR   KEGG; mmu:19157; -.
DR   CTD; 19157; -.
DR   MGI; MGI:1334257; Cyth1.
DR   eggNOG; roNOG08244; -.
DR   GeneTree; ENSGT00560000076562; -.
DR   HOVERGEN; HBG002647; -.
DR   NextBio; 295810; -.
DR   ArrayExpress; Q9QX11; -.
DR   Bgee; Q9QX11; -.
DR   Genevestigator; Q9QX11; -.
DR   GermOnline; ENSMUSG00000017132; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005086; F:ARF guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000904; Sec7.
DR   InterPro; IPR023394; SEC7_alpha_orthog.
DR   Gene3D; G3DSA:1.10.1000.11; G3DSA:1.10.1000.11; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF01369; Sec7; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00222; Sec7; 1.
DR   SUPFAM; SSF48425; Sec7; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50190; SEC7; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Coiled coil;
KW   Guanine-nucleotide releasing factor; Membrane.
FT   CHAIN         1    398       Cytohesin-1.
FT                                /FTId=PRO_0000120195.
FT   DOMAIN       73    202       SEC7.
FT   DOMAIN      260    377       PH.
FT   COILED       10     67       Potential.
FT   VAR_SEQ     273    273       Missing (in isoform 2).
FT                                /FTId=VSP_006035.
FT   CONFLICT      3      3       E -> D (in Ref. 1; BAA33428).
SQ   SEQUENCE   398 AA;  46288 MW;  098A6528F15300F5 CRC64;
     MEEDDSYVPS DLTAEERQEL ENIRRRKQEL LADIQRLKEE IAEVANEIES LGSTEERKNM
     QRNKQVAMGR KKFNMDPKKG IQFLIENGLL KNTCEDIAQF LYKGEGLNKT AIGDYLGERD
     EFSIQVLHAF VELHEFTDLN LVQALRQFLW SFRLPGEAQK IDRMMEAFAQ RYCQCNTGVF
     QSTDTCYVLS FAIIMLNTSL HNPNVKDKPT VERFIAMNRG INDGGDLPEE LLRNLYESIK
     NEPFKIPEDD GNDLTHTFFN PDREGWLLKL GGGRVKTWKR RWFILTDNCL YYFEYTTDKE
     PRGIIPLENL SIREVEDSKK PNCFELYIPD NKDQVIKACK TEADGRVVEG NHTVYRISAP
     TPEEKEDWIK CIKAAISRDP FYEMLAARKK KVSSTKRH
//
ID   SON_MOUSE               Reviewed;        2404 AA.
AC   Q9QX47; Q9CQ12; Q9CQK6; Q9QXP5;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-FEB-2011, entry version 82.
DE   RecName: Full=Protein SON;
GN   Name=Son;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
RC   STRAIN=129/Sv;
RX   MEDLINE=20408886; PubMed=10950926; DOI=10.1006/geno.2000.6254;
RA   Wynn S.L., Fisher R.A., Pagel C., Price M., Liu Q.Y., Khan I.M.,
RA   Zammit P., Dadrah K., Mazrani W., Kessling A., Lee J.S., Buluwela L.;
RT   "Organization and conservation of the GART/SON/DONSON locus in mouse
RT   and human genomes.";
RL   Genomics 68:57-62(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-116.
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, Small intestine, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1674; SER-1769;
RP   SER-1933; SER-1935 AND SER-1939, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1805; SER-1806;
RP   SER-1809; SER-1933; SER-1935; SER-1939; SER-1987; SER-1989 AND
RP   SER-1991, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1683, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Transcriptional repressor. Binds to the consensus DNA
CC       sequence: 5'-GA[GT]AN[CG][AG]CC-3'. Might protect cells from
CC       apoptosis. Might be involved in pre-mRNA splicing (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9QX47-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9QX47-2; Sequence=VSP_004416, VSP_004417;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- DOMAIN: Contains 8 types of repeats which are distributed in 3
CC       regions.
CC   -!- SIMILARITY: Contains 1 DRBM (double-stranded RNA-binding) domain.
CC   -!- SIMILARITY: Contains 1 G-patch domain.
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DR   EMBL; AF193606; AAF23120.1; -; Genomic_DNA.
DR   EMBL; AF193595; AAF23120.1; JOINED; Genomic_DNA.
DR   EMBL; AF193596; AAF23120.1; JOINED; Genomic_DNA.
DR   EMBL; AF193597; AAF23120.1; JOINED; Genomic_DNA.
DR   EMBL; AF193598; AAF23120.1; JOINED; Genomic_DNA.
DR   EMBL; AF193599; AAF23120.1; JOINED; Genomic_DNA.
DR   EMBL; AF193600; AAF23120.1; JOINED; Genomic_DNA.
DR   EMBL; AF193601; AAF23120.1; JOINED; Genomic_DNA.
DR   EMBL; AF193602; AAF23120.1; JOINED; Genomic_DNA.
DR   EMBL; AF193603; AAF23120.1; JOINED; Genomic_DNA.
DR   EMBL; AF193604; AAF23120.1; JOINED; Genomic_DNA.
DR   EMBL; AF193605; AAF23120.1; JOINED; Genomic_DNA.
DR   EMBL; AF193607; AAF23121.1; -; mRNA.
DR   EMBL; AK019312; BAB31659.1; -; mRNA.
DR   EMBL; AK019081; BAB31536.1; -; mRNA.
DR   EMBL; AK008478; BAB25691.1; -; mRNA.
DR   EMBL; AK008256; BAB25562.1; -; mRNA.
DR   IPI; IPI00134457; -.
DR   IPI; IPI00310168; -.
DR   UniGene; Mm.328698; -.
DR   UniGene; Mm.46401; -.
DR   ProteinModelPortal; Q9QX47; -.
DR   SMR; Q9QX47; 2345-2394.
DR   IntAct; Q9QX47; 4.
DR   STRING; Q9QX47; -.
DR   PhosphoSite; Q9QX47; -.
DR   PRIDE; Q9QX47; -.
DR   Ensembl; ENSMUST00000023683; ENSMUSP00000023683; ENSMUSG00000022961.
DR   UCSC; uc007zxy.1; mouse.
DR   UCSC; uc007zxz.1; mouse.
DR   MGI; MGI:98353; Son.
DR   GeneTree; ENSGT00570000078887; -.
DR   HOVERGEN; HBG023160; -.
DR   ArrayExpress; Q9QX47; -.
DR   Bgee; Q9QX47; -.
DR   CleanEx; MM_SON; -.
DR   Genevestigator; Q9QX47; -.
DR   GermOnline; ENSMUSG00000022961; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0050733; F:RS domain binding; IPI:MGI.
DR   InterPro; IPR001159; Ds-RNA-bd.
DR   InterPro; IPR014720; dsRNA-bd-like.
DR   InterPro; IPR000467; G_patch.
DR   Gene3D; G3DSA:3.30.160.20; dsRNA-bd-like; 1.
DR   Pfam; PF01585; G-patch; 1.
DR   SMART; SM00443; G_patch; 1.
DR   PROSITE; PS50137; DS_RBD; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; DNA-binding; Nucleus;
KW   Phosphoprotein; Repeat; RNA-binding.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   2404       Protein SON.
FT                                /FTId=PRO_0000072038.
FT   REPEAT      961    966       1-1.
FT   REPEAT      969    974       1-2.
FT   REPEAT      976    981       1-3.
FT   REPEAT      985    990       1-4.
FT   REPEAT      993    998       1-5.
FT   REPEAT     1001   1006       1-6.
FT   REPEAT     1010   1015       1-7.
FT   REPEAT     1018   1023       1-8.
FT   REPEAT     1026   1031       1-9.
FT   REPEAT     1035   1040       1-10.
FT   REPEAT     1044   1049       1-11.
FT   REPEAT     1055   1060       1-12.
FT   REPEAT     1066   1071       1-13.
FT   REPEAT     1075   1080       1-14.
FT   REPEAT     1910   1916       2-1.
FT   REPEAT     1919   1937       3-1.
FT   REPEAT     1938   1944       2-2.
FT   REPEAT     1945   1951       2-3.
FT   REPEAT     1952   1958       2-4.
FT   REPEAT     1959   1965       2-5.
FT   REPEAT     1966   1972       2-6.
FT   REPEAT     1973   1979       2-7; approximate.
FT   REPEAT     1980   1990       3-2; approximate.
FT   DOMAIN     2283   2329       G-patch.
FT   DOMAIN     2349   2404       DRBM.
FT   REGION      721    850       13 X 10 AA tandem repeats of L-A-[ST]-
FT                                [NSG]-[TS]-MDSQM.
FT   REGION      867    943       11 X 7 AA tandem repeats of [DR]-P-Y-R-
FT                                [LI][AG][QHP].
FT   REGION      961   1080       14 X 6 AA repeats of [ED]-R-S-M-M-S.
FT   REGION     1101   1133       3 X 11 AA tandem repats of P-P-L-P-P-E-E-
FT                                P-P-[TME]-[MTG].
FT   REGION     1910   1979       7 X 7 AA repeats of P-S-R-R-S-R-[TS].
FT   REGION     1919   1990       2 X 19 AA repeats of P-S-R-R-R-R-S-R-S-V-
FT                                V-R-R-R-S-F-S-I-S.
FT   REGION     1991   2017       3 X tandem repeats of [ST]-P-[VLI]-R-
FT                                [RL]-[RK]-[RF]-S-R.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      16     16       N6-acetyllysine (By similarity).
FT   MOD_RES      94     94       Phosphoserine (By similarity).
FT   MOD_RES     150    150       Phosphoserine (By similarity).
FT   MOD_RES     152    152       Phosphoserine (By similarity).
FT   MOD_RES     284    284       N6-acetyllysine (By similarity).
FT   MOD_RES     343    343       Phosphoserine (By similarity).
FT   MOD_RES     863    863       Phosphoserine (By similarity).
FT   MOD_RES     865    865       Phosphoserine (By similarity).
FT   MOD_RES    1006   1006       Phosphoserine (By similarity).
FT   MOD_RES    1031   1031       Phosphoserine (By similarity).
FT   MOD_RES    1638   1638       Phosphoserine (By similarity).
FT   MOD_RES    1674   1674       Phosphoserine.
FT   MOD_RES    1683   1683       Phosphoserine.
FT   MOD_RES    1751   1751       Phosphoserine (By similarity).
FT   MOD_RES    1754   1754       Phosphoserine (By similarity).
FT   MOD_RES    1767   1767       Phosphoserine (By similarity).
FT   MOD_RES    1768   1768       Phosphoserine (By similarity).
FT   MOD_RES    1769   1769       Phosphoserine.
FT   MOD_RES    1805   1805       Phosphoserine.
FT   MOD_RES    1806   1806       Phosphoserine.
FT   MOD_RES    1809   1809       Phosphoserine.
FT   MOD_RES    1933   1933       Phosphoserine.
FT   MOD_RES    1935   1935       Phosphoserine.
FT   MOD_RES    1939   1939       Phosphoserine.
FT   MOD_RES    1987   1987       Phosphoserine.
FT   MOD_RES    1989   1989       Phosphoserine.
FT   MOD_RES    1991   1991       Phosphoserine.
FT   MOD_RES    2007   2007       Phosphoserine (By similarity).
FT   MOD_RES    2009   2009       Phosphoserine (By similarity).
FT   MOD_RES    2033   2033       N6-acetyllysine (By similarity).
FT   MOD_RES    2107   2107       Phosphoserine (By similarity).
FT   MOD_RES    2141   2141       Phosphothreonine (By similarity).
FT   VAR_SEQ    2086   2086       K -> F (in isoform 2).
FT                                /FTId=VSP_004416.
FT   VAR_SEQ    2087   2404       Missing (in isoform 2).
FT                                /FTId=VSP_004417.
SQ   SEQUENCE   2404 AA;  261431 MW;  648BF28ED3FC01D9 CRC64;
     MAADIEQVFR SFVVSKFREI QQELSSGRSE GQLNGETNPP IEGNQAGDTA ASARSLPNEE
     IVQKIEEVLS GVLDTELRYK PDLKEASRKS RCVSVQTDPT DEVPTKKSKK HKKHKNKKKK
     KKKEKEKKYK RQPEESESKL KSHHDGNLES DSFLKFDSEP SAAALEHPVR AFGLSEASET
     ALVLEPPVVS MEVQESHVLE TLKPATKAAE LSVVSTSVIS EQSEQPMPGM LEPSMTKILD
     SFTAAPVPMS TAALKSPEPV VTMSVEYQKS VLKSLETMPP ETSKTTLVEL PIAKVVEPSE
     TLTIVSETPT EVHPEPSPST MDFPESSTTD VQRLPEQPVE APSEIADSSM TRPQESLELP
     KTTAVELQES TVASALELPG PPATSILELQ GPPVTPVPEL PGPSATPVPE LSGPLSTPVP
     ELPGPPATVV PELPGPSVTP VPQLSQELPG PPAPSMGLEP PQEVPEPPVM AQELSGVPAV
     SAAIELTGQP AVTVAMELTE QPVTTTEFEQ PVAMTTVEHP GHPEVTTATG LLGQPEAAMV
     LELPGQPVAT TALELSGQPS VTGVPELSGL PSATRALELS GQSVATGALE LPGQLMATGA
     LEFSGQSGAA GALELLGQPL ATGVLELPGQ PGAPELPGQP VATVALEISV QSVVTTSELS
     TMTVSQSLEV PSTTALESYN TVAQELPTTL VGETSVTVGV DPLMAQESHM LASNTMETHM
     LASNTMDSQM LASNTMDSQM LASNTMDSQM LASSTMDSQM LASSTMDSQM LATSTMDSQM
     LATSSMDSQM LATSSMDSQM LATSSMDSQM LATSSMESQM LASGAMDSQM LASGTMDAQM
     LASGTMDAQM LASSTQDSAM MGSKSPDPYR LAQDPYRLAQ DPYRLGHDPY RLGHDAYRLG
     QDPYRLGHDP YRLTPDPYRV SPRPYRIAPR SYRIAPRPYR LAPRPLMLAS RRSMMMSYAA
     ERSMMSSYER SMMSYERSMM SPMAERSMMS AYERSMMSAY ERSMMSPMAE RSMMSAYERS
     MMSAYERSMM SPMADRSMMS MGADRSMMSS YSAADRSMMS SYSAADRSMM SSYTDRSMMS
     MAADSYTDSY TDSYTEAYMV PPLPPEEPPT MPPLPPEEPP MTPPLPPEEP PEGPALSTEQ
     SALTADNTWS TEVTLSTGES LSQPEPPVSQ SEISEPMAVP ANYSMSESET SMLASEAVMT
     VPEPAREPES SVTSAPVESA VVAEHEMVPE RPMTYMVSET TMSVEPAVLT SEASVISETS
     ETYDSMRPSG HAISEVTMSL LEPAVTISQP AEDSLELPSM TVPAPSTMTT TESPVVAVTE
     IPPVAVPEPP IMAVPELPTM AVVKTPAVAV PEPLVAAPEP PTMATPELCS LSVSEPPVAV
     SELPALADPE HAITAVSGVS SLEPSVPILE PAVSVLQPVM IVSEPSVPVQ EPTVAVSEPA
     VIVSEHTQIT SPEMAVESSP VIVDSSVMSS QIMKGMNLLG GDENLGPEVG MQETLLHPGE
     EPRDGGHLKS DLYENEYDRN ADLTVNSHLI VKDAEHNTVC ATTVGPVGEA SEEKILPISE
     TKEITELATC AAVSEADIGR SLSSQLALEL DTVGTSKGFE FVTASALISE SKYDVEVSVT
     TQDTEHDMVI STSPSGGSEA DIEGPLPAKD IHLDLPSTNF VCKDVEDSLP IKESAQAVAV
     ALSPKESSED TEVLLPNKEI VPESGYSASI DEINEADLVR PLLPKDMERL TSLRAGIEGP
     LLASEVERDK SAASPVVISI PERASESSSE EKDDYEIFVK VKDTHEKSKK NKNRDKGEKE
     KKRDSSLRSR SKRSKSSEHK SRKRTSESRS RARKRSSKSK SHRSQTRSRS RSRRRRRSSR
     SRSKSRGRRS VSKEKRKRSP KHRSKSRERK RKRSSSRDNR KAARARSRTP SRRSRSHTPS
     RRRRSISVGR RRSFSISPSR RSRTPSRRSR TPSRRSRTPS RRSRTPSRRS RTPSRRRRSR
     SAVRRRSFSI SPVRLRRSRT PLRRRFSRSP IRRKRSRSSE RGRSPKRLTD LDKAQLLEIA
     KANAAAMCAK AGVPLPPNLK PAPPPTIEEK VAKKSGGATI EELTEKCKQI AQSKEDDDVI
     VNKPHVSDEE EEEPPFYHHP FKLSEPKPIF FNLNIAAAKP TPPKSQVTLT KEFPVSSGSQ
     HRKKEADSVY GEWVPVEKNG EESKDDDNVF SSSLPSEPVD ISTAMSERAL AQKRLSENAF
     DLEAMSMLNR AQERIDAWAQ LNSIPGQFTG STGVQVLTQE QLANTGAQAW IKKDQFLRAA
     PVTGGMGAVL MRKMGWREGE GLGKNKEGNK EPILVDFKTD RKGLVAVGER AQKRSGNFSA
     AMKDLSGKHP VSALMEICNK RRWQPPEFLL VHDSGPDHRK HFLFRVLRNG SPYQPNCMFF
     LNRY
//
ID   Q9QXA3_MOUSE            Unreviewed;      4587 AA.
AC   Q9QXA3;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   08-FEB-2011, entry version 75.
DE   SubName: Full=Fat 1 cadherin;
DE   Flags: Fragment;
GN   Name=Fat1; Synonyms=Fath, mfat1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Whole embryo;
RX   MEDLINE=20203461; PubMed=10741417;
RX   DOI=10.1002/(SICI)1097-0177(200003)217:3<233::AID-DVDY1>3.0.CO;2-O;
RA   Cox B.T.M., Hadjantonakis A.K., Collins J., Magee A.I.;
RT   "Cloning and expression throughout mouse development of mfat1, a
RT   homologue of the Drosophila tumour suppressor gene fat.";
RL   Dev. Dyn. 217:233-240(2000).
RN   [2]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [3]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
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DR   EMBL; AJ250768; CAB65271.1; -; mRNA.
DR   IPI; IPI00666346; -.
DR   UniGene; Mm.27365; -.
DR   HSSP; P08709; 1BF9.
DR   ProteinModelPortal; Q9QXA3; -.
DR   DIP; DIP-42865N; -.
DR   MINT; MINT-3370348; -.
DR   STRING; Q9QXA3; -.
DR   PhosphoSite; Q9QXA3; -.
DR   PRIDE; Q9QXA3; -.
DR   Ensembl; ENSMUST00000093529; ENSMUSP00000092968; ENSMUSG00000070047.
DR   UCSC; uc009lok.1; mouse.
DR   MGI; MGI:109168; Fat1.
DR   GeneTree; ENSGT00600000084230; -.
DR   HOVERGEN; HBG005641; -.
DR   ArrayExpress; Q9QXA3; -.
DR   Bgee; Q9QXA3; -.
DR   Genevestigator; Q9QXA3; -.
DR   GO; GO:0030054; C:cell junction; IDA:MGI.
DR   GO; GO:0030175; C:filopodium; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007015; P:actin filament organization; IMP:MGI.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:MGI.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR001881; EGF_Ca-bd.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR012680; Laminin_G_2.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 33.
DR   Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 2.
DR   Pfam; PF00028; Cadherin; 28.
DR   Pfam; PF02210; Laminin_G_2; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 33.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00282; LamG; 1.
DR   SUPFAM; SSF49313; Cadherin; 33.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 1.
DR   PROSITE; PS00232; CADHERIN_1; 17.
DR   PROSITE; PS50268; CADHERIN_2; 33.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell adhesion; EGF-like domain; Membrane; Repeat;
KW   Transmembrane.
FT   NON_TER    4587   4587
SQ   SEQUENCE   4587 AA;  506047 MW;  4D3F23BB05127CB4 CRC64;
     MGRHLTLLLL LLLFLQQFGD SDGSQRLEPT PPIQFTHFQY NVTVHENSAA KTYVGHPRKM
     GIYILDPSWE IRYKIVSGDS ENLFKAEEYV LGDFCFLRIR TKGGNTAILN REVRDHYTLI
     VKAVEKATDA EARAKVRVQV LDTNDLRPLF SPTSYSVSLP ENTAIRTSIA RVSATDADIG
     TNGEFYYSFK DRTDVFAIHP TSGVVVLTGR LDFLETQLYE LEILAADRGM KLYGSSGVSS
     LAKLTVHVEQ ANECAPIITA VTLSPSELDK DPTYAIITVE DCDQGANGEI ASLSIVAGDF
     LQQFKTVRSF PGSKAFKVKA VGAVDWDSHP YGYNLTLQAK DKGTPPQFSP VKVVHIISPQ
     FRAGPVKFEM DVYRAEISEF APPHTPVVLV KAIPSYSHLR YVFKSAPGKP KFGLNHNTGL
     ISILEPIRRQ HTSHFELEVT TSDKRASARV VVKVLGTNSN PPEFTQTSYK ASIDENAPIG
     AAVTRVSAMD PDEGENGYVT YSIANLNHVP FVIDHFTGTV STSENLDYEL MPRVYTLRIR
     ASDWGLPYRR EVEVLATITL NNLNDNTPLF ERINCEGTIP RDLGVGEQIT TVSAIDADEL
     QLFRYQIEAG NELDLFGLNP SSGVLSLKHS LTDGLGAKVS FHSLRITATD GENFATPLYI
     NLTVAASRKP VNLQCEETGV AKMLAEKLLQ ANKLHSQGDV EDIFFDSYSV NTHTPQFGVT
     LPTGIEVKEN LPVGANILFM NATDLDSGFN GKLVYAISGG NDDSCFTIDM ETGVLKVLSP
     LDREVMDKYT LNITVYDLGI PQKAAWRLLD VTVLDANDNA PEFLQESYFV EVSEDKEVNS
     EIIQVEATDK DLGPSGHVTY AILTDTEKFS IDSMTGVVKI IQPLDREVQP VHYLKIEARD
     QATEEPRLFS TVLLKVSLDD VNDNPPRFIP PNYSVKVRED LPEGTIIMWL EAYDPDVGQS
     SQVRYSLLDH GEGHFDVDKL SGAVRIVQQL DFEKKQLYNL TVRAKDKGKP VSLSSTCYVE
     VEVVDVNENL HTPVFSSFVE KGVVKEDVPT GSSVMTVSAH DEDTGRDGEI RYSIRDGSGI
     GVFRIDEETG VIETSDRLDR ESTSHYWLTV YATDQGVVPL SSFIEVYIEV EDVNDNAPQT
     SEPVYYPEIM ENSPKDVSVV QIEAFDPDSS SNDKLTYRIT SGNPQGFFSI HPKTGLITTT
     SRKLDREQQD EHILEVTVTD NGVPPRSTIA RVIVKILDEN DNRPQFLQKF YKIRLPEREK
     ADGDRSASKR EPLYRVIAAD KDEGPNAELS YSIEEGNEHG RFSIEPKTGV VSSKKFSAAG
     EYDILSIKAV DNGRPQKSST TRLHIEWISK PKPSSEPISF EESVFSFTVM ESDPVAHMIG
     VISVEPPGMP LWFDIIGGNY DSHFDVDKGT GTIIVAKPLD AEQKSSYNLT VEATDGTTTI
     LTQVLIKVID TNDHRPQFST SKYEVAVPED TEPEVEILQI SAVDRDEKNK LIYTLQSSID
     PASLKKFRLD PATGALYTAE KLDHEAIHQH VLTVMVRDQD VPVKRNFARI VVNVSDKNDH
     APWFTSPSYD GRVYESAAVG SVVLQVTALD KDKGRNAEVL YSIESGNIGN SFTIDPILGS
     IKTARELDRS HQVDYDLMVK ATDKGDPPMS EMTSVRIAVT VADNASPKFT SKEYSAEISE
     AIRIGSFVGM VSAHSQSSVM YEIRDGNMGD AFNINPHSGS IITQRALDFE TLPMYSLTVQ
     GTNMAGLSTN TTVVVHVRDE NDNPPVFTQA EYSGFISESA SVNSVVLTDR NVPLVIRATD
     ADRESNALLV YQIVEPSVHN YFAIDPTTGA IRTVLSLDYE ETHAFHFTVQ VHDMGTPRLF
     AEYAANVTVH VIDINDCPPV FSKSLYEVSL LLPTYRGVNV ITVNATDADS KAFSQVMYSI
     TEGNIGEKFS MDHKTGTIAI QNTTQLRSRY ELTVRASDGR FTSMASVKIN VKESRESPLK
     FTQDAYSAVV KENSTEARTL AVITAIGNPL NEPLFYRILN PDRRFKISHT SGVLSTTGIP
     FDREQQETFD VVVEVTKEHE PSAVAHVVVK VTVEDQNDNA PVFVNLPYYA VVKVDAEVGH
     VIRYVTAIDR DSGRNGDIHY YLKEHHDHFQ IGPSGDISLK KQFEHDTLNK EYLVTVVAKD
     GGSPAFSAEV LVPITVMNKA MPVFEKAFYS AEIPENIQMH SPVVHIQANS PEGLKVFYSI
     TDGDPFSQFT INFNTGVVNV IAPLDFESHP AYKLSVRATD SLTGAHAEVF VDIIVEDIND
     NPPVFVQPSY STTLSEASVI GTPVLQVRAT DSDSEPNRGI SYQLIGNHSK SHDHFHIDSN
     TGLISLVRAL DYEQSQQHRI FVRAVDGGMP ALSSDVVVTV AVTDLNDNPP LFEQQVYEAR
     ISEHAAHGHF VMCVRACDAD SSDLDKLEYS ILSGNDHKSF IIDRETGIIT LSNLRRHTLK
     PFYSLNVSVS DGVFRSSARV NVTVMGGNLH SPVFHQNEYE VELAENAPLH TLVVQVKASD
     RDSGIYSHVT YHIVNDFAKD RFYVNDRGQI FTLEKLDRET PAEKVISIRL MAKDAGGKVA
     FCTVNVILTD DNDNAPQFRS TKYEVNIGSS AAKGTSVVKV FASDADEGSN ADVTYAIEAD
     SESVKENLEI NKLTGLITTK ESLIGLENEF FTFFVRAVDS GSPPRESVVP VYIKILPPEV
     QLPRFSEPFY TYTISEDTPI GTEIDLIRVE HGGAVLYILV KGNTPESNRD EFFVIDRQNG
     RLKLEKSLDH ETTKWYQFSI LARCTLDDYE VVASIDVSIQ VKDANDNSPV LESSPYEAFI
     VENLPGGSRV IQIRASDLDS GANGQVMYSL DQSQDADIIE SFAINMETGW ITTLKELDHE
     ERASYQIKVV ASDHGEKVQL SSTAIVGVTV TDVNDSPPRF TAEIYKGTVS EDDPPGGVIA
     ILSTTDADTE EINRQVSYFI TGGDALGQFA VENVQSDWRV YVKKPLDREQ KDSYLLTVTA
     TDGTFSSKAR VEVKVLDAND NSPVCEKTSY SDTIPEDALP GKLVMQVSAT DADIRSNAEI
     TYTLFGSGAE KFKLNPDTGE LRTLALLDRE EQAVYNLLVK ATDGGGRSCQ AAIVLTLEDV
     NDNAPEFTAE PYTITVFENT EPGTPLTRVQ ATDADTGLNR KISYSLVESA DGQFSINERS
     GIIQLEKHLD RELQAVYTLT LKAVDQGLPR RLTATGTVVV SVLDINDNPP VFEYREYGAS
     VSEDIVIGTE VLQVYAASRD IEANAEITYA IISGNEHGKF SIDSKTGAIF IIESLDYESS
     HEYYLTVEAT DGGTPSLSDV ATVNINVTDI NDNSPVFSQD TYTTVVSEDA ALEQPVITIM
     ADDADGPSNS HIHYSIIEGN QGSPFTIDPV RGEVKVTKPL DRETISGYTL TVQAADNGNP
     PRVNTTTVNI DVSDVNDNAP LFSRDNYSVI IQENKPVGFS VLKLVVTDKD SSHNGPPFFF
     TIVSGNDENA FEVNQHGVLL TAATIKRKVK DHYFLHVKVA DSGKPQLSSM THIDIRVIEE
     SIHPPAILPL EIFITAFGEE YSGGVIGKIH ATDQDVYDTL MYSLDPHMDG LFSVSSTGGK
     LIAHRKLDIG QYLLNVSVTD GKFTTVADIT VHIQQVTQEM LNHTVAIRFA NLTPEEFVGD
     YWRNFQRALR NILGVRKNDI QIVSLQPSEP HSHLDVLLFV ERSGGTTFST KQLLHKINSS
     VTDVEEIIGV RILEVFQKLC AGLDCPWKFC DEKVSVDENV MSTHSTARLS FVTPRHHRTA
     VCLCKDGTCP PVHHGCEDNP CPAGSECVAD PREEKYSCVC PGGGFGKCPG SSSITFTGNS
     FVKYRLLENE NRLEMKLSMR LRTYSLHAVV MYARGTDYSI PGIVSVQSIQ VNDGQWHAVS
     LEVEGNYAKL VLDEVHTASG TAPGALKTLN LDNYVFFGGH LRQQGTKHGR GAQVASGFRG
     CMDSIYLNGQ ELPLNNKPRA YAHIEEWVDL SHGCLLTATE DCSSSPCQNG GVCNPSPTGG
     YYCKCNALYV GTFCEVSVNP CSSNPCLSGG TFICIDSGVC SCSLGLVLLC SDCQLCSFCQ
     DDPCQIGGTC FDSLDGAVCH CDSGFRGERF QIDIDECAGN PCRNGALCEI TLSFYHCNCS
     QEYRGKHCED ASPNHYVSTP WNIGLAEGIG IIVFIAGIVL LVMVFVLCRK MISRKKKRQA
     EPEDKRLGPT TAFLQRPYFD SKLNKNIYFD IPAQVPVRPI SYTFPSIPSD SRNNLDRNSF
     EGSAIPEHPE FSTFNPESMH GHRKAVAVCS VAPNLPPPPP SNSPSDSDSI QKPSWDFDYD
     AKVVDLDPCL SKKPLEEKPS QPYSARESLS EVQSLSSFQS ESCDDNESLA APDLSKPRGY
     HWDTSDWMPS VPLPDIQEFP NYEAIDEHTP LYSADPNAID TDYYPGGYDI ESDFPPPPEE
     FPAPDELPPL LPEFSDQFES IHPPRDMPAA GSLGFSSRSR QRFNLNQYLP NFYPADMSEP
     QKQGAGENSP CREPYTPYPP GYQRNFEAPT IENMPMSVYA STASCSDVSA CCEVESEVMM
     SDYESGDDGH FEEVTIPPLD SQQHTEV
//
ID   ACSA_MOUSE              Reviewed;         701 AA.
AC   Q9QXG4;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Acetyl-coenzyme A synthetase, cytoplasmic;
DE            EC=6.2.1.1;
DE   AltName: Full=Acetate--CoA ligase;
DE   AltName: Full=Acetyl-CoA synthetase;
DE            Short=ACS;
DE            Short=AceCS;
DE   AltName: Full=Acyl-CoA synthetase short-chain family member 2;
DE   AltName: Full=Acyl-activating enzyme;
GN   Name=Acss2; Synonyms=Acas2, Acecs1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=22045843; PubMed=12049778; DOI=10.1016/S0925-4773(02)00097-7;
RA   Loikkanen I., Haghighi S., Vainio S., Pajunen A.;
RT   "Expression of cytosolic acetyl-CoA synthetase gene is developmentally
RT   regulated.";
RL   Mech. Dev. 115:139-141(2002).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND SER-267, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
CC   -!- FUNCTION: Activates acetate so that it can be used for lipid
CC       synthesis or for energy generation.
CC   -!- CATALYTIC ACTIVITY: ATP + acetate + CoA = AMP + diphosphate +
CC       acetyl-CoA.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family.
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DR   EMBL; AF216873; AAF24510.1; -; mRNA.
DR   IPI; IPI00330302; -.
DR   UniGene; Mm.255026; -.
DR   ProteinModelPortal; Q9QXG4; -.
DR   SMR; Q9QXG4; 45-695.
DR   STRING; Q9QXG4; -.
DR   PhosphoSite; Q9QXG4; -.
DR   PRIDE; Q9QXG4; -.
DR   Ensembl; ENSMUST00000029135; ENSMUSP00000029135; ENSMUSG00000027605.
DR   MGI; MGI:1890410; Acss2.
DR   GeneTree; ENSGT00550000074278; -.
DR   HOVERGEN; HBG014401; -.
DR   OrthoDB; EOG4VHK61; -.
DR   PhylomeDB; Q9QXG4; -.
DR   BRENDA; 6.2.1.1; 244.
DR   ArrayExpress; Q9QXG4; -.
DR   Bgee; Q9QXG4; -.
DR   CleanEx; MM_ACSS2; -.
DR   Genevestigator; Q9QXG4; -.
DR   GermOnline; ENSMUSG00000027605; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0003987; F:acetate-CoA ligase activity; IDA:MGI.
DR   GO; GO:0016208; F:AMP binding; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006085; P:acetyl-CoA biosynthetic process; IDA:MGI.
DR   InterPro; IPR011904; Ac_CoA_lig.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   Pfam; PF00501; AMP-binding; 1.
DR   TIGRFAMs; TIGR02188; Ac_CoA_lig_AcsA; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding;
KW   Phosphoprotein.
FT   CHAIN         1    701       Acetyl-coenzyme A synthetase,
FT                                cytoplasmic.
FT                                /FTId=PRO_0000208424.
FT   MOD_RES      30     30       Phosphoserine.
FT   MOD_RES     263    263       Phosphoserine.
FT   MOD_RES     267    267       Phosphoserine.
FT   MOD_RES     418    418       N6-acetyllysine (By similarity).
SQ   SEQUENCE   701 AA;  78921 MW;  CEA99D719F6FBA77 CRC64;
     MGLPEERRKS GSGSRAREET GAEGRVRGWS PPPEVRRSAH VPSLQRYREL HRRSVEEPRE
     FWGNIAKEFY WKTACPGPFL QYNFDVTKGK IFTEWMKGAT TNICYNVLDR NVHEKKLGDK
     VAFYWEGNEP GETTKITYRE LLVQVCQFSN VLRKQGIQKG DRVAIYMPMI LELVVAMLAC
     ARLGALHSIV FAGFSAESLC ERILDSSCCL LITTDAFYRG EKLVNLKELA DESLEKCREK
     GFPVRCCIVV KHLGRAELGM NDSPSQSPPV KRPCPDVQIC WNEGVDLWWH ELMQQAGDEC
     EPEWCDAEDP LFILYTSGST GKPKGVVHTI GGYMLYVATT FKYVFDFHPE DVFWCTADIG
     WITGHSYVTY GPLANGATSV LFEGIPTYPD EGRLWSIVDK YKVTKFYTAP TAIRMLMKFG
     DDPVTKHSRA SLQVLGTVGE PINPEAWLWY HRVVGSQRCP IVDTFWQTET GGHMLTPLPG
     ATPMKPGSAS FPFFGVALQS LNESGEELEG EAEGYLVFKQ PWPGIMRTVY GNHTRFETTY
     FKKFPGYYVT GDGCRRDQDG YYWITGRIDD MLNVSGHLLS TAEVESALVE HEAVAEAAVV
     GHPHPVKGEC LYCFVTLCDG HTFSPTLTEE LKKQIREKIG PIATPDYIQN APGLLKPRSG
     KIMRRVLRKI AQNDHDLGDT STVADPSVIN HLFSHRCLTT Q
//
ID   APBB1_MOUSE             Reviewed;         710 AA.
AC   Q9QXJ1; O08642; Q3TPU0; Q8BNF4; Q8BSR9;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Amyloid beta A4 precursor protein-binding family B member 1;
DE   AltName: Full=Protein Fe65;
GN   Name=Apbb1; Synonyms=Fe65;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Liakicheva A.V., Ivanova N.B., Belyavsky A.V.;
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 498-674.
RC   TISSUE=Embryo;
RX   MEDLINE=97049965; PubMed=8894693; DOI=10.1093/hmg/5.10.1589;
RA   Bressler S.L., Gray M.D., Sopher B.L., Hu Q., Hearn M.G., Pham D.G.,
RA   Dinulos M.B., Fukuchi K., Sisodia S.S., Miller M.A., Disteche C.M.,
RA   Martin G.M.;
RT   "cDNA cloning and chromosome mapping of the human Fe65 gene:
RT   interaction of the conserved cytoplasmic domains of the human beta-
RT   amyloid precursor protein and its homologues with the mouse Fe65
RT   protein.";
RL   Hum. Mol. Genet. 5:1589-1598(1996).
RN   [4]
RP   INTERACTION WITH APBB1IP AND ENAH, AND MUTAGENESIS OF TRP-280 AND
RP   PRO-283.
RX   MEDLINE=98070482; PubMed=9407065; DOI=10.1074/jbc.272.52.32869;
RA   Ermekova K.S., Zambrano N., Linn H., Minopoli G., Gertler F.,
RA   Russo T., Sudol M.;
RT   "The WW domain of neural protein FE65 interacts with proline-rich
RT   motifs in Mena, the mammalian homolog of Drosophila enabled.";
RL   J. Biol. Chem. 272:32869-32877(1997).
RN   [5]
RP   FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=17121854; DOI=10.1074/jbc.C600276200;
RA   Minopoli G., Stante M., Napolitano F., Telese F., Aloia L.,
RA   De Felice M., Di Lauro R., Pacelli R., Brunetti A., Zambrano N.,
RA   Russo T.;
RT   "Essential roles for Fe65, Alzheimer amyloid precursor-binding
RT   protein, in the cellular response to DNA damage.";
RL   J. Biol. Chem. 282:831-835(2007).
RN   [6]
RP   INTERACTION WITH TSHZ1; TSHZ2 AND TSHZ3.
RX   PubMed=19343227; DOI=10.1371/journal.pone.0005071;
RA   Kajiwara Y., Akram A., Katsel P., Haroutunian V., Schmeidler J.,
RA   Beecham G., Haines J.L., Pericak-Vance M.A., Buxbaum J.D.;
RT   "FE65 binds Teashirt, inhibiting expression of the primate-specific
RT   caspase-4.";
RL   PLoS ONE 4:E5071-E5071(2009).
CC   -!- FUNCTION: Adapter protein that forms a transcriptionally active
CC       complex with the gamma-secretase-derived amyloid precursor protein
CC       (APP) intracellular domain. Plays a central role in the response
CC       to DNA damage by translocating to the nucleus and inducing
CC       apoptosis. May act by specifically recognizing and binding histone
CC       H2AX phosphorylated on 'Tyr-142' (H2AXY142ph) at double-strand
CC       breaks (DSBs), recruiting other pro-apoptosis factors such as
CC       MAPK8/JNK1. Required for histone H4 acetylation at double-strand
CC       breaks (DSBs). Its ability to specifically bind modified histones
CC       and chromatin modifying enzymes such as KAT5/TIP60, probably
CC       explains its trancription activation activity. Function in
CC       association with TSHZ3, SET and HDAC factors as a transcriptional
CC       repressor, that inhibits the expression of CASP4. Associates with
CC       chromatin in a region surrounding the CASP4 transcriptional start
CC       site(s).
CC   -!- SUBUNIT: Interacts with SET. Found in a trimeric complex with
CC       HDAC1 and TSHZ3; the interaction between HDAC1 and APBB1 is
CC       mediated by TSHZ3 (By similarity). Component of a complex, at
CC       least composed of APBB1, RASD1/DEXRAS1 and APP. Interacts (via PID
CC       domain 2) with APP (with the intracellular domain of the beta-
CC       amyloid precursor protein). Interacts (via PID domain 2) with
CC       RASD1/DEXRAS1; impairs the trancription activation activity.
CC       Interacts (via PID domain 1) with KAT5/TIP60. Interacts (via the
CC       WW domain) with histone H2AX (when phosphorylated on 'Tyr-142').
CC       Interacts with MAPK8 (By similarity). Interacts (via the WW
CC       domain) with proline-rich regions of APBB1IP and ENAH. Interacts
CC       (via PID domain 1) with TSHZ3 (via homeobox domain). Interacts
CC       with TSHZ1 and TSHZ2.
CC   -!- INTERACTION:
CC       P12023:App; NbExp=1; IntAct=EBI-81338, EBI-78814;
CC   -!- SUBCELLULAR LOCATION: Cell membrane. Cytoplasm. Nucleus. Cell
CC       projection, growth cone (By similarity). Note=Colocalizes with
CC       TSHZ3 in the nucleus and in axonal growth cone (By similarity). In
CC       normal conditions, it mainly localizes to the cytoplasm, while a
CC       small fraction is tethered to the cell membrane via its
CC       interaction with APP. Following exposure to DNA damaging agents,
CC       it is released from cell membrane and translocates to the nucleus.
CC       Nuclear translocation is under the regulation of APP.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9QXJ1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9QXJ1-2; Sequence=VSP_011659;
CC   -!- PTM: Phosphorylated following nuclear translocation.
CC       Phosphorylation at Tyr-546 enhances the transcription activation
CC       activity and reduces the affinity with RASD1/DEXRAS1 (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: No phenotype in normal conditions. Displays
CC       an increased sensitivity to genotoxic stress and exposur to DNA
CC       damaging agents.
CC   -!- SIMILARITY: Contains 2 PID domains.
CC   -!- SIMILARITY: Contains 1 WW domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF206720; AAF20141.1; -; mRNA.
DR   EMBL; AK030748; BAC27116.1; -; mRNA.
DR   EMBL; AK083830; BAC39033.1; -; mRNA.
DR   EMBL; AK164140; BAE37645.1; -; mRNA.
DR   EMBL; L77865; AAB51603.1; -; mRNA.
DR   IPI; IPI00387261; -.
DR   IPI; IPI00626699; -.
DR   RefSeq; NP_033815.1; NM_009685.2.
DR   UniGene; Mm.38469; -.
DR   ProteinModelPortal; Q9QXJ1; -.
DR   SMR; Q9QXJ1; 241-290, 366-666.
DR   IntAct; Q9QXJ1; 2.
DR   MINT; MINT-142893; -.
DR   STRING; Q9QXJ1; -.
DR   PhosphoSite; Q9QXJ1; -.
DR   PRIDE; Q9QXJ1; -.
DR   Ensembl; ENSMUST00000081165; ENSMUSP00000079932; ENSMUSG00000037032.
DR   GeneID; 11785; -.
DR   KEGG; mmu:11785; -.
DR   UCSC; uc009iyi.1; mouse.
DR   CTD; 11785; -.
DR   MGI; MGI:107765; Apbb1.
DR   eggNOG; roNOG12845; -.
DR   GeneTree; ENSGT00390000000002; -.
DR   HOGENOM; HBG443527; -.
DR   HOVERGEN; HBG050524; -.
DR   InParanoid; Q9QXJ1; -.
DR   OrthoDB; EOG4X3H12; -.
DR   NextBio; 279601; -.
DR   ArrayExpress; Q9QXJ1; -.
DR   Bgee; Q9QXJ1; -.
DR   Genevestigator; Q9QXJ1; -.
DR   GermOnline; ENSMUSG00000037032; Mus musculus.
DR   GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0001540; F:beta-amyloid binding; IPI:UniProtKB.
DR   GO; GO:0035035; F:histone acetyltransferase binding; NAS:UniProtKB.
DR   GO; GO:0008134; F:transcription factor binding; IDA:UniProtKB.
DR   GO; GO:0030048; P:actin filament-based movement; NAS:UniProtKB.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0007411; P:axon guidance; IGI:MGI.
DR   GO; GO:0007050; P:cell cycle arrest; IDA:UniProtKB.
DR   GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
DR   GO; GO:0030198; P:extracellular matrix organization; IGI:MGI.
DR   GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR   GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:MGI.
DR   GO; GO:0045749; P:negative regulation of S phase of mitotic cell cycle; IDA:UniProtKB.
DR   GO; GO:0050760; P:negative regulation of thymidylate synthase biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0001764; P:neuron migration; IGI:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptosis; ISS:UniProtKB.
DR   GO; GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
DR   GO; GO:0050821; P:protein stabilization; NAS:UniProtKB.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Pfam; PF00640; PID; 2.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00462; PTB; 2.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF51045; WW_Rsp5_WWP; 1.
DR   PROSITE; PS01179; PID; 2.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Apoptosis; Cell membrane;
KW   Cell projection; Chromatin regulator; Cytoplasm; DNA damage; Membrane;
KW   Nucleus; Phosphoprotein; Repeat; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    710       Amyloid beta A4 precursor protein-binding
FT                                family B member 1.
FT                                /FTId=PRO_0000076050.
FT   DOMAIN      253    285       WW.
FT   DOMAIN      370    509       PID 1.
FT   DOMAIN      542    699       PID 2.
FT   COMPBIAS    158    171       Glu-rich.
FT   MOD_RES     546    546       Phosphotyrosine (By similarity).
FT   VAR_SEQ     462    463       Missing (in isoform 2).
FT                                /FTId=VSP_011659.
FT   MUTAGEN     280    280       W->F: Abolishes ligand binding; when
FT                                associated with A-283.
FT   MUTAGEN     283    283       P->A: Abolishes ligand binding; when
FT                                associated with F-280.
FT   CONFLICT     92     92       T -> A (in Ref. 1; AAF20141).
FT   CONFLICT    313    313       E -> D (in Ref. 1; AAF20141).
FT   CONFLICT    630    630       A -> S (in Ref. 2; BAC39033).
SQ   SEQUENCE   710 AA;  77468 MW;  9E1A121C5408F979 CRC64;
     MSVPSSLSQS AINANSHGGP ALSFPLPLHA AHNQLLNAKL QATAVVPKDL RSAMGEGSVP
     EPGPANAKWL KEGQNQLRRA ATAHRDQNRN VTLTLAEEAS QEAETAPLGP KGLMHLYSEL
     ELSAHNAANR GLHGSALIIN TQEQGPDEGE EKAAGEAEED DEDEEEEEEE EDLSSPPGLP
     EPLENVEVPS GPQALTDGPR EHSKSASLLF GMRNSAASDE DSSWATLSQG SPSYGSPEDT
     DSFWNPNAFE TDSDLPAGWM RVQDTSGTYY WHIPTGTTQW EPPGRASPSQ GSSPQEESQL
     TWTGFAHQEG FEEGEFWKDE PSEEAPMELG LKDPEEATLS FPAQSLSPEP VPQEEEKLSQ
     RNANPGIKCF AVRSLGWVEM TEEELAPGRS SVAVNNCIRQ LSYHKNNLHD PMAGGWGEGK
     DLLLQLEDET LKLVEPQNQT LLHAQPIVSI RVWGVGRDSG RERDFAYVAR DKLTQMLKCH
     VFRCEAPAKN IATSLHEICS KIMSERRNAR CLVNGLSLDH SKLVDVPFQV EFPAPKNELV
     QKFQVYYLGN VPVAKPVGVD VINGALESVL SSSSREQWTP SHVSVAPATL TILHQQTEAV
     LGECRVRFLS FLAVGRDVHT FAFIMAAGPA SFCCHMFWCE PNAASLSEAV QAACMLRYQK
     CLDARSQTST SCLPAPPAES VARRVGWTVR RGVQSLWGSL KPKRLGSQTP
//
ID   KI21B_MOUSE             Reviewed;        1668 AA.
AC   Q9QXL1; P97424;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 79.
DE   RecName: Full=Kinesin-like protein KIF21B;
DE   AltName: Full=Kinesin-like protein KIF6;
GN   Name=Kif21b; Synonyms=Kif6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=99242603; PubMed=10225949; DOI=10.1083/jcb.145.3.469;
RA   Marszalek J.R., Weiner J.A., Farlow S.J., Chun J., Goldstein L.S.;
RT   "Novel dendritic kinesin sorting identified by different process
RT   targeting of two related kinesins: KIF21A and KIF21B.";
RL   J. Cell Biol. 145:469-479(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 100-173.
RC   TISSUE=Brain cortex;
RA   Honeycutt R.J., McClelland M., Chada K., Welsh J.;
RT   "Identifying differentially regulated genes in mouse brain using
RT   arbitrarily primed PCR.";
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 491-504, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580 AND THR-583, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
CC   -!- FUNCTION: Microtubule-binding motor protein probably involved in
CC       neuronal dendritic transport. In vitro, has a plus-end directed
CC       motor activity.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection,
CC       dendrite. Note=In neurons, localized to axons and dendrites.
CC   -!- TISSUE SPECIFICITY: Expressed in brain and spleen. Expressed at
CC       lower levels in testes.
CC   -!- SIMILARITY: Belongs to the kinesin-like protein family.
CC   -!- SIMILARITY: Contains 1 kinesin-motor domain.
CC   -!- SIMILARITY: Contains 7 WD repeats.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF202893; AAF17084.1; -; mRNA.
DR   EMBL; U71298; AAB39695.1; -; mRNA.
DR   IPI; IPI00135132; -.
DR   RefSeq; NP_001034561.1; NM_001039472.1.
DR   UniGene; Mm.276135; -.
DR   ProteinModelPortal; Q9QXL1; -.
DR   SMR; Q9QXL1; 4-398, 1303-1620.
DR   PhosphoSite; Q9QXL1; -.
DR   PRIDE; Q9QXL1; -.
DR   Ensembl; ENSMUST00000075164; ENSMUSP00000074661; ENSMUSG00000041642.
DR   GeneID; 16565; -.
DR   KEGG; mmu:16565; -.
DR   UCSC; uc007cul.1; mouse.
DR   CTD; 16565; -.
DR   MGI; MGI:109234; Kif21b.
DR   eggNOG; roNOG13842; -.
DR   GeneTree; ENSGT00600000084098; -.
DR   HOGENOM; HBG358343; -.
DR   HOVERGEN; HBG052247; -.
DR   InParanoid; Q9QXL1; -.
DR   PhylomeDB; Q9QXL1; -.
DR   NextBio; 290069; -.
DR   ArrayExpress; Q9QXL1; -.
DR   Bgee; Q9QXL1; -.
DR   Genevestigator; Q9QXL1; -.
DR   GermOnline; ENSMUSG00000041642; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR009053; Prefoldin.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:3.40.850.10; kinesin_motor; 1.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF00400; WD40; 7.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF46579; Prefoldin; 1.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_DOMAIN1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_DOMAIN2; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Microtubule; Motor protein;
KW   Nucleotide-binding; Phosphoprotein; Repeat; WD repeat.
FT   CHAIN         1   1668       Kinesin-like protein KIF21B.
FT                                /FTId=PRO_0000125465.
FT   DOMAIN        5    299       Kinesin-motor.
FT   REPEAT     1308   1345       WD 1.
FT   REPEAT     1348   1386       WD 2.
FT   REPEAT     1412   1450       WD 3.
FT   REPEAT     1453   1495       WD 4.
FT   REPEAT     1504   1541       WD 5.
FT   REPEAT     1545   1584       WD 6.
FT   REPEAT     1587   1624       WD 7.
FT   NP_BIND      87     94       ATP (By similarity).
FT   COILED      372    465       Potential.
FT   COILED      924   1019       Potential.
FT   MOD_RES     580    580       Phosphoserine.
FT   MOD_RES     583    583       Phosphothreonine.
FT   MOD_RES    1239   1239       Phosphothreonine (By similarity).
FT   MOD_RES    1243   1243       Phosphoserine (By similarity).
FT   MOD_RES    1246   1246       Phosphothreonine (By similarity).
SQ   SEQUENCE   1668 AA;  186164 MW;  37145B2D867C9A57 CRC64;
     MAGQGDCCVK VAVRIRPQLS KEKIEGCHIC TSVTPGEPQV LLGKDKAFTY DFVFDLDTWQ
     EQIYSTCVSK LIEGCFEGYN ATVLAYGQTG AGKTYTMGTG FDTVTSEEEQ GIIPRAIAHL
     FRGIDERKRR AQEKGVTGPE FKVSAQFLEL YNEEILDLFD STRDPDARHR RSNIKIHEDA
     NGGIYTTGVT SRLINSQEEL IQCLKQGALS RTTASTQMNV QSSRSHAIFT IHLCQMRVCA
     QPDLVNETVT GLPDGAAPTG TEYETLTAKF HFVDLAGSER LKRTGATGER AKEGISINCG
     LLALGNVISA LGDQSKKVVH VPYRDSKLTR LLQDSLGGNS QTIMIACVSP SDRDFMETLN
     TLKYANRARN IKNKVVVNQD KTSQQISALR AEIARLQMEL MEYKAGKRVI GEDGTEGYSD
     LFRENAMLQK ENGALRLRVK AMQEAIDAIN NRVTQLMSQE ANLLLAKAGD GNEAIGALIQ
     NYIREIEELR TKLLESEAMN ESLRRSLSRA SARNPYSLGA SPAGPAFGGS PATSMEDASE
     VIRKAKQDLE RLKKKEVRQR RKSPEKEAFK KRAKLQAENS EETDENEAEE EEEERDESGC
     EEEEGREDED EDSGSEESLV DSDSDPEEKE VNFQADLADL TCEIEIKQKL IDELENSQRR
     LQTLKHQYEE KLILLQNKIR DTQLERDRVL QNLSTMECYT EEKANKIKAD YEKRLREMNR
     DLQKLQAAQK EHARLLKNQS RYERELKKLQ AEVAEMKKAK VALMKQMREE QQRRRLVETK
     RNREIAQLKK EQRRQEFQIR ALESQKRQQE IVLRRKTQEV SALRRLAKPM SERVAGRVGL
     KPPNMDSGAE VSASTTSSEA ESGARSVSSI VRQWNRKIDH FLGDRPTATV NGGRPARKKF
     QKKGASQSFS KAARLKWQSL ERRIIDIVMQ RMTIVNLEAD MERLIKKREE LFLLQEALRR
     KREHLQAESP EEEKGLQELA EEIEVLAANI DYINDSITDC QATIVQLEET KEELDSTDTS
     VVISSCSLAE ARLLLDNFLK ASIDKGLQVA QKEAQIRLLE GRLRQTDMTG SSQNHLLLDA
     LREKAEAHPE LQALIYNVQH ENGYASTDEE VSEFSEGSFS QSFTMKGSTS HDDFKFKGEP
     KLSAQMKAVS AECLGPPLDS STKNITKSLA SLVEIKEDGV GFSIRDPYYR DKVSRTVSLP
     TRGSTFPRQS RGATDTSPLT RRKSYDRGQP IRSTDMGFTP PSSPPTRPRN DRNVFSRLTS
     NQSQGSALDK SDDSDASLSE VLRGIITPIG GAKGARTAPL QCISMAEGHT KPILCLDATD
     ELLFTGSKDR SCKMWNLVTG QEIAALKGHP NNVVSIKYCS HSGLVFSVSS SYIKVWDIRD
     SAKCIRTLTS SGQVISGDAC IATSTRAITS AQGEHQINQM ALSPSGSMLY VASGNAVRIW
     ELNRFQPIGK LTGHIGPVMC LTVTQTSNQH DLVVTGSKDH YVKMFQLGDC VTGTIGPTHN
     FEPPHYDGIE CLAIQGDILF SGSRDNGIKK WDLDQQELIQ QIPNAHKDWV CALAFVPGRP
     MLLSACRAGF IKVWNVDNFT PIGEIKGHDS PINAICTNSK HIFTASSDCR VKLWNYVPGL
     TPCLPRRVLA IKGRAPPCPD LPPPPLTLPI LPFPVFPPPR SELLLHVT
//
ID   KI21A_MOUSE             Reviewed;        1672 AA.
AC   Q9QXL2; Q6P5H1; Q6ZPJ8; Q8BWZ9; Q8BXF1;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Kinesin-like protein KIF21A;
GN   Name=Kif21a; Synonyms=Kiaa1708;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY,
RP   AND SUBCELLULAR LOCATION.
RX   MEDLINE=99242603; PubMed=10225949; DOI=10.1083/jcb.145.3.469;
RA   Marszalek J.R., Weiner J.A., Farlow S.J., Chun J., Goldstein L.S.;
RT   "Novel dendritic kinesin sorting identified by different process
RT   targeting of two related kinesins: KIF21A and KIF21B.";
RL   J. Cell Biol. 145:469-479(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-551, AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1129-1672 (ISOFORM 4).
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 382-1672 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-80 AND TYR-87, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1660 AND SER-1671, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Microtubule-binding motor protein probably involved in
CC       neuronal axonal transport. In vitro, has a plus-end directed motor
CC       activity.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection,
CC       dendrite. Cell projection, axon. Note=In neurons, localized to
CC       axons and dendrites.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9QXL2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9QXL2-2; Sequence=VSP_010873, VSP_010874, VSP_010875;
CC       Name=3;
CC         IsoId=Q9QXL2-3; Sequence=VSP_010873, VSP_010876;
CC       Name=4;
CC         IsoId=Q9QXL2-4; Sequence=VSP_010877;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in
CC       brain.
CC   -!- SIMILARITY: Belongs to the kinesin-like protein family.
CC   -!- SIMILARITY: Contains 1 kinesin-motor domain.
CC   -!- SIMILARITY: Contains 7 WD repeats.
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DR   EMBL; AF202892; AAF17083.1; -; mRNA.
DR   EMBL; BC060698; AAH60698.1; -; mRNA.
DR   EMBL; BC062896; AAH62896.1; -; mRNA.
DR   EMBL; AK129426; BAC98236.1; -; mRNA.
DR   EMBL; AK049303; BAC33669.1; -; mRNA.
DR   EMBL; AK047350; BAC33031.1; -; mRNA.
DR   IPI; IPI00454081; -.
DR   IPI; IPI00454082; -.
DR   IPI; IPI00454083; -.
DR   IPI; IPI00454084; -.
DR   RefSeq; NP_001102510.1; NM_001109040.1.
DR   RefSeq; NP_001102511.1; NM_001109041.1.
DR   RefSeq; NP_001102512.1; NM_001109042.1.
DR   RefSeq; NP_057914.2; NM_016705.3.
DR   UniGene; Mm.41379; -.
DR   UniGene; Mm.481341; -.
DR   ProteinModelPortal; Q9QXL2; -.
DR   SMR; Q9QXL2; 7-398, 1335-1654.
DR   STRING; Q9QXL2; -.
DR   PhosphoSite; Q9QXL2; -.
DR   PRIDE; Q9QXL2; -.
DR   Ensembl; ENSMUST00000088614; ENSMUSP00000085985; ENSMUSG00000022629.
DR   Ensembl; ENSMUST00000109287; ENSMUSP00000104910; ENSMUSG00000022629.
DR   Ensembl; ENSMUST00000109288; ENSMUSP00000104911; ENSMUSG00000022629.
DR   Ensembl; ENSMUST00000109289; ENSMUSP00000104912; ENSMUSG00000022629.
DR   GeneID; 16564; -.
DR   KEGG; mmu:16564; -.
DR   UCSC; uc007xhs.1; mouse.
DR   UCSC; uc007xht.1; mouse.
DR   UCSC; uc007xhv.1; mouse.
DR   CTD; 16564; -.
DR   MGI; MGI:109188; Kif21a.
DR   GeneTree; ENSGT00600000084098; -.
DR   HOGENOM; HBG358343; -.
DR   HOVERGEN; HBG052247; -.
DR   InParanoid; Q9QXL2; -.
DR   OMA; KTKVRLM; -.
DR   OrthoDB; EOG479F67; -.
DR   NextBio; 290065; -.
DR   ArrayExpress; Q9QXL2; -.
DR   Bgee; Q9QXL2; -.
DR   CleanEx; MM_KIF21A; -.
DR   Genevestigator; Q9QXL2; -.
DR   GermOnline; ENSMUSG00000022629; Mus musculus.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
DR   GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR009053; Prefoldin.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:3.40.850.10; kinesin_motor; 1.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   Pfam; PF00400; WD40; 6.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF46579; Prefoldin; 1.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_DOMAIN1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_DOMAIN2; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell projection; Coiled coil;
KW   Cytoplasm; Cytoskeleton; Microtubule; Motor protein;
KW   Nucleotide-binding; Phosphoprotein; Repeat; WD repeat.
FT   CHAIN         1   1672       Kinesin-like protein KIF21A.
FT                                /FTId=PRO_0000125463.
FT   DOMAIN        1    299       Kinesin-motor.
FT   REPEAT     1343   1380       WD 1.
FT   REPEAT     1383   1421       WD 2.
FT   REPEAT     1447   1485       WD 3.
FT   REPEAT     1488   1530       WD 4.
FT   REPEAT     1539   1576       WD 5.
FT   REPEAT     1580   1619       WD 6.
FT   REPEAT     1622   1659       WD 7.
FT   NP_BIND      88     95       ATP (By similarity).
FT   COILED      365    840       Potential.
FT   COILED      933   1021       Potential.
FT   COILED     1055   1085       Potential.
FT   MOD_RES      80     80       Phosphotyrosine.
FT   MOD_RES      87     87       Phosphotyrosine.
FT   MOD_RES    1225   1225       Phosphoserine (By similarity).
FT   MOD_RES    1227   1227       Phosphoserine (By similarity).
FT   MOD_RES    1231   1231       Phosphoserine (By similarity).
FT   MOD_RES    1241   1241       Phosphoserine (By similarity).
FT   MOD_RES    1273   1273       Phosphoserine (By similarity).
FT   MOD_RES    1276   1276       Phosphoserine (By similarity).
FT   MOD_RES    1660   1660       Phosphoserine.
FT   MOD_RES    1671   1671       Phosphoserine.
FT   VAR_SEQ     558    570       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_010873.
FT   VAR_SEQ    1109   1115       Missing (in isoform 2).
FT                                /FTId=VSP_010874.
FT   VAR_SEQ    1226   1305       ISRQSSLSEKKVPEPSPVTRRKAYEKADKPKAKEHKHSDSG
FT                                ASETSLSPPSSPPSRPRNELNVFNRLTVPQGTPSVQQDK
FT                                -> M (in isoform 2).
FT                                /FTId=VSP_010875.
FT   VAR_SEQ    1227   1318       Missing (in isoform 3).
FT                                /FTId=VSP_010876.
FT   VAR_SEQ    1262   1318       HSDSGASETSLSPPSSPPSRPRNELNVFNRLTVPQGTPSVQ
FT                                QDKSDESDSSLSEVHR -> Q (in isoform 4).
FT                                /FTId=VSP_010877.
FT   CONFLICT   1127   1127       P -> A (in Ref. 1; AAF17083).
FT   CONFLICT   1311   1311       S -> F (in Ref. 1).
FT   CONFLICT   1321   1321       I -> L (in Ref. 1).
SQ   SEQUENCE   1672 AA;  186536 MW;  1B2480E5129105AB CRC64;
     MLGAADESSV RVAVRIRPQL AKEKIEGCHI CTSVTPGEPQ VFLGKDKAFT FDYVFDIDSQ
     QEQIYTQCIE KLIEGCFEGY NATVFAYGQT GAGKTYTMGT GFDVNIMEEE QGIISRAVRH
     LFKSIDEKKT SAIKNGLPPP EFKVNAQFLE LYNEEVLDLF DTTRDIDAKN KKSNIRIHED
     STGGIYTVGV TTRTVNTEPE MMQCLKLGAL SRTTASTQMN VQSSRSHAIF TIHVCQTRVC
     PQTDAENATD NKLISESSPM NEFETLTAKF HFVDLAGSER LKRTGATGER AKEGISINCG
     LLALGNVISA LGDKSKRATH VPYRDSKLTR LLQDSLGGNS QTIMIACVSP SDRDFMETLN
     TLKYANRARN IKNKVMVNQD RASQQINALR SEITRLQMEL MEYKTGKRII DEEGVESIND
     MFHENAMLQT ENNNLRVRIK AMQETVDALR ARITQLVSEQ ANQVLARAGE GNEEISNMIH
     SYIKEIEDLR AKLLESEAVN ENLRKNLTRA TARSPYFSAS SAFSPTILSS DKETIEIIDL
     AKKDLEKLKR KEKKKKKRLQ KLEESGREER SVAGKDDNAD TDQEKKEEKG VSEKENNELD
     VEENQEVSDH EDEEEEEEDE EEEDDIEGEE SSDESDSESD EKANYQADLA NITCEIAIKQ
     KLIDELENSQ KRLQTLKKQY EEKLMMLQHK IRDTQLERDQ VLQNLGSVES YSEEKAKKVK
     CEYEKKLHAM NKELQRLQTA QKEHARLLKN QSQYEKQLKK LQQDVMEMKK TKVRLMKQMK
     EEQEKARLTE SRRNREIAQL KKDQRKRDHQ LRLLEAQKRN QEVVLRRKTE EVTALRRQVR
     PMSDKVAGKV TRKLSSSESP APDTGSSAAS GEADTSRPGT QQKMRIPVAR VQALPTPTTN
     GTRKKYQRKG FTGRVFTSKT ARMKWQLLER RVTDIIMQKM TISNMEADMN RLLRQREELT
     KRREKLSKRR EKIVKESGEG DKSVANIIEE MESLTANIDY INDSIADCQA NIMQMEEAKE
     EGETLDVTAV INACTLTEAR YLLDHFLSMG INKGLQAAQK EAQIKVLEGR LKQTEITSAT
     QNQLLFHMLK EKAELNPELD ALLGHALQDL DGAPPENEED SSEEDGPLHS PGSEGSTLSS
     DLMKLCGEVK PKNKARRRTT TQMELLYADS SEVASDTSAG DASLSGPLAP VAEGQEIGMN
     TETSGTSARD KELLAPSGLP SKIGSISRQS SLSEKKVPEP SPVTRRKAYE KADKPKAKEH
     KHSDSGASET SLSPPSSPPS RPRNELNVFN RLTVPQGTPS VQQDKSDESD SSLSEVHRGI
     INPFPACKGV RASPLQCVHI AEGHTKAVLC VDSTDDLLFT GSKDRTCKVW NLVTGQEIMS
     LGVHPNNVVS VKYCNYTSLV FTVSTSYIKV WDIRESAKCI RTLTSSGQVT LGEACSASTS
     RTVAIPSGES QINQIALNPT GTFLYAASGN AVRMWDLKRF QSTGKLTGHL GPVMCLTVDQ
     ISNGQDLIIT GSKDHYIKMF DVTEGALGTV SPTHNFEPPH YDGIEALAIQ GDNLFSGSRD
     NGIKKWDLAQ KGLLQQVPNA HKDWVCALGL VPGHPVLLSG CRGGILKLWN VDTFVPVGEM
     RGHDSPINAI CVNSTHVFTA ADDRTVRIWK AHNLQDGQLS DTGDLGEDIA SN
//
ID   JMY_MOUSE               Reviewed;         983 AA.
AC   Q9QXM1; Q3UQZ0; Q5BL16; Q6NST0; Q8CBP9; Q8VDZ3;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 57.
DE   RecName: Full=Junction-mediating and -regulatory protein;
GN   Name=Jmy;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
RP   EP300, AND TISSUE SPECIFICITY.
RX   MEDLINE=99446485; PubMed=10518217; DOI=10.1016/S1097-2765(00)80338-X;
RA   Shikama N., Lee C.-W., France S., Delavaine L., Lyon J.,
RA   Krstic-Demonacos M., La Thangue N.B.;
RT   "A novel cofactor for p300 that regulates the p53 response.";
RL   Mol. Cell 4:365-376(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-555 AND 940-983 (ISOFORM
RP   1).
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   FUNCTION, ALTERNATIVE SPLICING (ISOFORM 3), AND INTERACTION WITH TTC5.
RX   PubMed=11511361; DOI=10.1016/S1097-2765(01)00277-5;
RA   Demonacos C., Krstic-Demonacos M., La Thangue N.B.;
RT   "A TPR motif cofactor contributes to p300 activity in the p53
RT   response.";
RL   Mol. Cell 8:71-84(2001).
RN   [5]
RP   UBIQUITINATION, AND INDUCTION.
RX   PubMed=17170761; DOI=10.1038/sj.embor.7400855;
RA   Coutts A.S., Boulahbel H., Graham A., La Thangue N.B.;
RT   "Mdm2 targets the p53 transcription cofactor JMY for degradation.";
RL   EMBO Rep. 8:84-90(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-64 AND SER-75, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-981.
RX   PubMed=19287377; DOI=10.1038/ncb1852;
RA   Zuchero J.B., Coutts A.S., Quinlan M.E., Thangue N.B., Mullins R.D.;
RT   "p53-cofactor JMY is a multifunctional actin nucleation factor.";
RL   Nat. Cell Biol. 11:451-459(2009).
RN   [8]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=19897726; DOI=10.1073/pnas.0906785106;
RA   Coutts A.S., Weston L., La Thangue N.B.;
RT   "A transcription co-factor integrates cell adhesion and motility with
RT   the p53 response.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:19872-19877(2009).
CC   -!- FUNCTION: Acts both as a nuclear p53/TP53-cofactor and a
CC       cytoplasmic regulator of actin dynamics depending on conditions.
CC       In nucleus, acts as a cofactor that increases p53/TP53 response
CC       via its interaction with p300/EP300. Increases p53/TP53-dependent
CC       transcription and apoptosis, suggesting an important role in
CC       p53/TP53 stress response such as DNA damage. In cytoplasm, acts as
CC       a nucleation-promoting factor for both branched and unbranched
CC       actin filaments. Activates the Arp2/3 complex to induce branched
CC       actin filament networks. Also catalyzes actin polymerization in
CC       the absence of Arp2/3, creating unbranched filaments. Contributes
CC       to cell motility by controlling actin dynamics. May promote the
CC       rapid formation of a branched actin network by first nucleating
CC       new mother filaments and then activating Arp2/3 to branch off
CC       these filaments. The p53/TP53-cofactor and actin activator
CC       activities are regulated via its subcellular location.
CC   -!- SUBUNIT: Interacts with p300/EP300, the complex being recruited to
CC       activated p53/TP53. Interacts with TTC5.
CC   -!- INTERACTION:
CC       Q09472:EP300 (xeno); NbExp=6; IntAct=EBI-866001, EBI-447295;
CC       Q00987:MDM2 (xeno); NbExp=1; IntAct=EBI-866001, EBI-389668;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton (By
CC       similarity). Note=Localizes to the nucleus in most cell types. In
CC       primary neutrophils, it colocalizes with actin filaments at the
CC       leading edge and is excluded from the nucleus. Localization
CC       correlates with motility, because it moves from the nucleus to the
CC       cytoplasmic compartment when cells are differentiated from
CC       nonmotile cells into highly motile neutrophil-like cells (By
CC       similarity). Accumulates in nucleus under DNA damage conditions,
CC       increasing p53/TP53 transcription response and reducing its
CC       influence on cell motility.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9QXM1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9QXM1-2; Sequence=VSP_032311, VSP_032312;
CC       Name=3; Synonyms=DeltaP;
CC         IsoId=Q9QXM1-3; Sequence=VSP_032313;
CC         Note=Alters the p53/TP53 response;
CC   -!- TISSUE SPECIFICITY: Widely expressed, except in testis where it is
CC       expressed at low level.
CC   -!- INDUCTION: Accumulates in DNA-damaged cells (at protein level).
CC   -!- PTM: Ubiquitinated by MDM2, leading to its subsequent degradation
CC       by the proteasome. In case of DNA damage, the interaction with
CC       MDM2 is altered, preventing degradation and allowing interaction
CC       with p300/EP300 and its function in p53/TP53 stress response.
CC   -!- SIMILARITY: Belongs to the JMY family.
CC   -!- SIMILARITY: Contains 1 WH2 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH69906.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence;
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DR   EMBL; AF201390; AAF17555.1; -; mRNA.
DR   EMBL; BC020052; AAH20052.1; -; mRNA.
DR   EMBL; BC069906; AAH69906.1; ALT_SEQ; mRNA.
DR   EMBL; BC090835; AAH90835.1; -; mRNA.
DR   EMBL; AK035559; BAC29105.1; -; mRNA.
DR   EMBL; AK141957; BAE24898.1; -; mRNA.
DR   IPI; IPI00135188; -.
DR   IPI; IPI00889204; -.
DR   IPI; IPI00889211; -.
DR   RefSeq; NP_067285.2; NM_021310.2.
DR   UniGene; Mm.390630; -.
DR   ProteinModelPortal; Q9QXM1; -.
DR   IntAct; Q9QXM1; 17.
DR   STRING; Q9QXM1; -.
DR   PhosphoSite; Q9QXM1; -.
DR   PRIDE; Q9QXM1; -.
DR   Ensembl; ENSMUST00000065537; ENSMUSP00000070339; ENSMUSG00000021690.
DR   GeneID; 57748; -.
DR   KEGG; mmu:57748; -.
DR   CTD; 57748; -.
DR   MGI; MGI:1913096; Jmy.
DR   eggNOG; roNOG12060; -.
DR   GeneTree; ENSGT00510000046704; -.
DR   HOGENOM; HBG715540; -.
DR   HOVERGEN; HBG067146; -.
DR   InParanoid; Q9QXM1; -.
DR   OrthoDB; EOG4MW85R; -.
DR   NextBio; 313889; -.
DR   ArrayExpress; Q9QXM1; -.
DR   Bgee; Q9QXM1; -.
DR   CleanEx; MM_JMY; -.
DR   Genevestigator; Q9QXM1; -.
DR   GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR   GO; GO:0070060; P:'de novo' actin filament nucleation; IDA:UniProtKB.
DR   GO; GO:0070358; P:actin polymerization-dependent cell motility; IDA:UniProtKB.
DR   GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; IDA:UniProtKB.
DR   GO; GO:0007050; P:cell cycle arrest; IDA:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006917; P:induction of apoptosis; IDA:MGI.
DR   GO; GO:0051091; P:positive regulation of transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0043620; P:regulation of transcription in response to stress; TAS:UniProtKB.
DR   InterPro; IPR003124; WH2_actin-bd.
DR   SMART; SM00246; WH2; 1.
DR   PROSITE; PS51082; WH2; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Coiled coil; Cytoplasm;
KW   Cytoskeleton; DNA damage; DNA repair; Nucleus; Phosphoprotein;
KW   Ubl conjugation.
FT   CHAIN         1    983       Junction-mediating and -regulatory
FT                                protein.
FT                                /FTId=PRO_0000324612.
FT   DOMAIN      916    933       WH2.
FT   REGION        1    119       Interaction with p300/EP300.
FT   REGION      469    558       Interaction with p300/EP300.
FT   COILED      315    351       Potential.
FT   COILED      480    528       Potential.
FT   COILED      571    612       Potential.
FT   COMPBIAS    762    818       Pro-rich.
FT   MOD_RES      64     64       Phosphothreonine.
FT   MOD_RES      75     75       Phosphoserine.
FT   MOD_RES     108    108       Phosphoserine (By similarity).
FT   MOD_RES     969    969       Phosphoserine (By similarity).
FT   VAR_SEQ     445    446       VY -> FP (in isoform 2).
FT                                /FTId=VSP_032311.
FT   VAR_SEQ     447    983       Missing (in isoform 2).
FT                                /FTId=VSP_032312.
FT   VAR_SEQ     794    812       Missing (in isoform 3).
FT                                /FTId=VSP_032313.
FT   MUTAGEN     981    981       W->A: Decreases the activation of Arp2/3
FT                                wizhout affecting the intinsic nucleation
FT                                activity.
FT   CONFLICT     54     54       Q -> H (in Ref. 3; BAE24898).
FT   CONFLICT     63     63       G -> V (in Ref. 2; AAH20052).
FT   CONFLICT     70     70       S -> R (in Ref. 3; BAE24898).
FT   CONFLICT    153    153       I -> T (in Ref. 2; AAH20052/AAH90835 and
FT                                3; BAE24898).
FT   CONFLICT    159    159       V -> A (in Ref. 2; AAH20052/AAH90835 and
FT                                3; BAE24898).
FT   CONFLICT    189    189       M -> I (in Ref. 2; AAH20052).
FT   CONFLICT    214    214       S -> P (in Ref. 2; AAH20052/AAH90835 and
FT                                3; BAE24898).
FT   CONFLICT    331    331       R -> K (in Ref. 2; AAH20052).
SQ   SEQUENCE   983 AA;  110586 MW;  EC58500CC05B8BAA CRC64;
     MSFALEETLE SDWVAVRPHV FDEREKHKFV FIVAWNEIEG KFAITCHNRT AQRQRSGSRE
     QAGTPASDGS RGPGSPAARG RSEAAASATA ALRSPGPRKS QAWAEGGSPR SARSLKGDPP
     RGPAGRGPES PLRSPARAKA SPLRRSAESR DAIASATPVP PAPPVPPVSS VRVVSASGAV
     SEEIEVLEMV REDEAPQPLP DSEQPPSAAE LESSAEECSW AGLFSFQDLR AVHQQLCSVN
     SQLEPCLPVF PEEPSGMWTV LFGGAPEMTE QEIDALCYQL QVYLGHGLDT CGWKILSQVL
     FTETDDPEEY YESLSELRQK GYEEVLQRAR RRIQELLDKH KTIESMVELL DLYQMEDEAY
     SSLAEATTEL YQYLLQPFRD MRELAMLRRQ QIKISMENDY LGPRRIESLQ KEDADWQRKA
     HMAVLSIQDL TVKYFEITAK AQKAVYDRMR ADQKKFGKAS WAAAAERMEK LQYAVSKETL
     QMMRAKEICL EQKKHALKEE MQSLQGGTEA IARLDQLESD YYDLQLQLYE VQFEILKCEE
     LLLTAQLESI KRLISEKRDE VVYYDTYESM EAMLEKEEMA ASVHAQREEL QKLQQKARQL
     EARRGRVSAK KAYLRNKKEI CIAKHHEKFQ QRFQSEDEYR AHHTIQIKRD KLHDEEERKS
     AWVSQERQRT LDRLRTFKQR YPGQVILKST RLRVAHSRRK STASPVPCEE QCHSLPTVLQ
     GQEKTEVGGG GSQLGPSQTA EPQSLVQLED TSSEQLESTS LPPRAVVSSE LPPPQSAPLL
     TSIDPKPCSV TIDPLPPPLP PTPPPPPPPP PPPPPPLPVA KDNGASTTAE TLEKDALRTE
     GNERSIPKSA SAPAAHLFDS SQLVSARKKL RKTVEGLQRR RVSSPMDEVL ASLKRGSFHL
     KKVEQRTLPP FPDEDDSNNI LAQIRKGVKL KKVQKEVLRE SFTLLPDTDP LTRSIHEALR
     RIKEASPESE DEEEALPCTD WEN
//
ID   SHRM3_MOUSE             Reviewed;        1986 AA.
AC   Q9QXN0; Q3TNX1; Q6ZPP9; Q99L16; Q9QXM9;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Protein Shroom3;
GN   Name=Shroom3; Synonyms=Kiaa1481, Shrm;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), DEVELOPMENTAL STAGE,
RP   SUBCELLULAR LOCATION, INTERACTION WITH F-ACTIN, FUNCTION, AND
RP   DISRUPTION PHENOTYPE.
RX   MEDLINE=20055594; PubMed=10589677; DOI=10.1016/S0092-8674(00)81537-8;
RA   Hildebrand J.D., Soriano P.;
RT   "Shroom, a PDZ domain-containing actin-binding protein, is required
RT   for neural tube morphogenesis in mice.";
RL   Cell 99:485-497(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF 123-145; 257-280; 283-300 AND 1107-1141, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 255-1986 (ISOFORM 3).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1506-1986 (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   FUNCTION.
RX   PubMed=14680628; DOI=10.1016/j.cub.2003.11.054;
RA   Haigo S.L., Hildebrand J.D., Harland R.M., Wallingford J.B.;
RT   "Shroom induces apical constriction and is required for hingepoint
RT   formation during neural tube closure.";
RL   Curr. Biol. 13:2125-2137(2003).
RN   [7]
RP   FUNCTION.
RX   PubMed=16249236; DOI=10.1242/jcs.02626;
RA   Hildebrand J.D.;
RT   "Shroom regulates epithelial cell shape via the apical positioning of
RT   an actomyosin network.";
RL   J. Cell Sci. 118:5191-5203(2005).
RN   [8]
RP   FUNCTION.
RX   PubMed=16684770; DOI=10.1074/jbc.M512463200;
RA   Dietz M.L., Bernaciak T.M., Vendetti F., Kielec J.M., Hildebrand J.D.;
RT   "Differential actin-dependent localization modulates the
RT   evolutionarily conserved activity of Shroom family proteins.";
RL   J. Biol. Chem. 281:20542-20554(2006).
RN   [9]
RP   NOMENCLATURE.
RX   PubMed=16615870; DOI=10.1186/1471-2121-7-18;
RA   Hagens O., Ballabio A., Kalscheuer V., Kraehenbuhl J.-P.,
RA   Schiaffino M.V., Smith P., Staub O., Hildebrand J.D.,
RA   Wallingford J.B.;
RT   "A new standard nomenclature for proteins related to Apx and Shroom.";
RL   BMC Cell Biol. 7:18-18(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439; SER-443; SER-888
RP   AND THR-909, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Controls cell shape changes in the neuroepithelium
CC       during neural tube closure. Induces apical constriction in
CC       epithelial cells by promoting the apical accumulation of F-actin
CC       and myosin II, and probably by bundling stress fibers. Induces
CC       apicobasal cell elongation by redistributing gamma-tubulin and
CC       directing the assembly of robust apicobasal microtubule arrays.
CC   -!- SUBUNIT: Interacts with F-actin.
CC   -!- SUBCELLULAR LOCATION: Cell junction, adherens junction. Cytoplasm,
CC       cytoskeleton. Note=Colocalizes with F-actin in stress fibers and
CC       adherens junctions.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=L,a;
CC         IsoId=Q9QXN0-1; Sequence=Displayed;
CC       Name=2; Synonyms=S,b;
CC         IsoId=Q9QXN0-2; Sequence=VSP_024969;
CC       Name=3;
CC         IsoId=Q9QXN0-3; Sequence=VSP_024970;
CC       Name=4;
CC         IsoId=Q9QXN0-4; Sequence=VSP_024969, VSP_024970;
CC   -!- DEVELOPMENTAL STAGE: At E8.75, strongly expressed in the cranial
CC       neuroepithelium, and also expressed in neural tube, paraxial
CC       mesoderm and gut. At E10.5, expressed in neural tube, forebrain,
CC       somites, ventral body wall, heart and gut. At E14.5, expression is
CC       restricted to skeletal muscle, tips of the digits and forebrain.
CC   -!- DOMAIN: The ASD1 domain mediates F-actin binding.
CC   -!- DOMAIN: The ASD2 domain is required for apical constriction
CC       induction.
CC   -!- DISRUPTION PHENOTYPE: Death at birth due to defects in neural tube
CC       closure causing exencephaly, acrania, facial clefting and spina
CC       bifida.
CC   -!- SIMILARITY: Belongs to the shroom family.
CC   -!- SIMILARITY: Contains 1 ASD1 domain.
CC   -!- SIMILARITY: Contains 1 ASD2 domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF13269.1; Type=Frameshift; Positions=1097, 1124;
CC       Sequence=AAF13270.1; Type=Frameshift; Positions=1097, 1124;
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DR   EMBL; AF199421; AAF13269.1; ALT_FRAME; mRNA.
DR   EMBL; AF199422; AAF13270.1; ALT_FRAME; mRNA.
DR   EMBL; AK147493; BAE27948.1; -; mRNA.
DR   EMBL; AK164918; BAE37966.1; -; mRNA.
DR   EMBL; AK129371; BAC98181.1; -; mRNA.
DR   EMBL; BC003909; AAH03909.1; -; mRNA.
DR   IPI; IPI00135239; -.
DR   IPI; IPI00808498; -.
DR   IPI; IPI00845609; -.
DR   IPI; IPI00845631; -.
DR   RefSeq; NP_001071063.1; NM_001077595.1.
DR   RefSeq; NP_001071064.1; NM_001077596.1.
DR   RefSeq; NP_056571.2; NM_015756.2.
DR   UniGene; Mm.46014; -.
DR   HSSP; Q8R1G6; 1VB7.
DR   ProteinModelPortal; Q9QXN0; -.
DR   SMR; Q9QXN0; 20-107.
DR   STRING; Q9QXN0; -.
DR   PhosphoSite; Q9QXN0; -.
DR   PRIDE; Q9QXN0; -.
DR   Ensembl; ENSMUST00000113051; ENSMUSP00000108674; ENSMUSG00000029381.
DR   Ensembl; ENSMUST00000113054; ENSMUSP00000108677; ENSMUSG00000029381.
DR   Ensembl; ENSMUST00000113055; ENSMUSP00000108678; ENSMUSG00000029381.
DR   GeneID; 27428; -.
DR   KEGG; mmu:27428; -.
DR   CTD; 27428; -.
DR   MGI; MGI:1351655; Shroom3.
DR   eggNOG; roNOG06397; -.
DR   GeneTree; ENSGT00530000063061; -.
DR   HOGENOM; HBG283187; -.
DR   HOVERGEN; HBG108489; -.
DR   InParanoid; Q9QXN0; -.
DR   OrthoDB; EOG44QT03; -.
DR   NextBio; 305484; -.
DR   ArrayExpress; Q9QXN0; -.
DR   Bgee; Q9QXN0; -.
DR   CleanEx; MM_SHROOM3; -.
DR   Genevestigator; Q9QXN0; -.
DR   GO; GO:0005912; C:adherens junction; IDA:MGI.
DR   GO; GO:0043296; C:apical junction complex; IDA:MGI.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; IDA:MGI.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IGI:MGI.
DR   GO; GO:0045176; P:apical protein localization; ISS:HGNC.
DR   GO; GO:0000902; P:cell morphogenesis; ISS:HGNC.
DR   GO; GO:0043482; P:cellular pigment accumulation; ISS:HGNC.
DR   GO; GO:0002066; P:columnar/cuboidal epithelial cell development; IDA:MGI.
DR   GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR   GO; GO:0007389; P:pattern specification process; IMP:MGI.
DR   GO; GO:0008360; P:regulation of cell shape; IDA:MGI.
DR   InterPro; IPR014800; ASD1.
DR   InterPro; IPR014799; ASD2.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF08688; ASD1; 1.
DR   Pfam; PF08687; ASD2; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS51306; ASD1; 1.
DR   PROSITE; PS51307; ASD2; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Cell junction; Cell shape;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW   Direct protein sequencing; Microtubule; Phosphoprotein.
FT   CHAIN         1   1986       Protein Shroom3.
FT                                /FTId=PRO_0000286067.
FT   DOMAIN       24    109       PDZ.
FT   DOMAIN      927   1023       ASD1.
FT   DOMAIN     1659   1947       ASD2.
FT   COILED     1844   1890       Potential.
FT   COMPBIAS    191    268       Ser-rich.
FT   COMPBIAS   1351   1540       Pro-rich.
FT   MOD_RES     439    439       Phosphoserine.
FT   MOD_RES     443    443       Phosphoserine.
FT   MOD_RES     574    574       Phosphothreonine (By similarity).
FT   MOD_RES     580    580       Phosphoserine (By similarity).
FT   MOD_RES     888    888       Phosphoserine.
FT   MOD_RES     909    909       Phosphothreonine.
FT   MOD_RES     912    912       Phosphoserine (By similarity).
FT   MOD_RES    1219   1219       Phosphoserine (By similarity).
FT   VAR_SEQ       1    175       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_024969.
FT   VAR_SEQ    1354   1359       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_024970.
FT   CONFLICT    409    409       Q -> H (in Ref. 1; AAF13270/AAF13269).
FT   CONFLICT    617    617       R -> K (in Ref. 1; AAF13270/AAF13269).
FT   CONFLICT    683    683       Q -> P (in Ref. 4; BAC98181).
FT   CONFLICT    800    800       Y -> N (in Ref. 1; AAF13270/AAF13269).
FT   CONFLICT   1078   1078       S -> N (in Ref. 1; AAF13270/AAF13269).
FT   CONFLICT   1239   1239       R -> K (in Ref. 1; AAF13270/AAF13269).
FT   CONFLICT   1293   1293       P -> H (in Ref. 1; AAF13270/AAF13269).
FT   CONFLICT   1318   1318       A -> S (in Ref. 4; BAC98181).
FT   CONFLICT   1397   1397       P -> L (in Ref. 1; AAF13270/AAF13269).
FT   CONFLICT   1407   1408       GE -> EK (in Ref. 4; BAC98181).
FT   CONFLICT   1419   1419       R -> Q (in Ref. 4; BAC98181).
FT   CONFLICT   1423   1423       P -> L (in Ref. 4; BAC98181).
FT   CONFLICT   1457   1457       R -> L (in Ref. 4; BAC98181).
FT   CONFLICT   1770   1770       N -> Y (in Ref. 1; AAF13270/AAF13269).
FT   CONFLICT   1967   1967       A -> G (in Ref. 2; BAE27948/BAE37966).
SQ   SEQUENCE   1986 AA;  214888 MW;  52C7A4AF6390D547 CRC64;
     MKTPENLEEP SATPNPSRTP TERFVYLEAL LEGGAPWGFT LKGGLERGEP LIISKIEEGG
     KADSVSSGLQ AGDEVIHINE VALSSPRREA VSLVKGSYKT LRLVVRRDVC AAPGHADPGT
     SKSLSSELLT CSPQHRKATW SGGVKLRLKQ RCSEPATRPH SWHTTKFGET QPDVSMMQIS
     QGTMGPPWHQ SYHSSSSTSD LSNYDHAYLR RSPDQCSSQG SMESLEPSGG YPPCHLLSPA
     KSTSSIDQLG HLHNKRDSAY SSFSTSSSIF EYPPPGGSAR ERSGSMDVIS ARGGLLEGMR
     QADIRYVKTV YDTRRGVSSE YEVNPSALLL QGRDAHASAD SQGCAKWHSI PRGKGTPSPS
     WSQQCSGSLE TATDNLPQKA GAPLPPTRSD SYAAFRHRER PSSWSSLDQK RFCRPQTNSS
     GSQKTPFAED QLHTVPERSP ENSPPVKSKH NYTQKAQPGQ PLLPTGIYPV PSPEPHFAQV
     PQPSVSSNGT VYPALVKESG YTAAQGTCNK MATLDENGNQ NEASRPGFAF CQPLEHNSVT
     PVEKRPEPTA KYIYKVHFSS VPENEDSSLK RHITPPHGHS PYPSERKNIH GGSRACSNHH
     SLSSPQAQAL HVGDDRRPSR LSQPWEGDFQ EDHNANLRQK VEREGQGQGL SGNSGRTRSA
     FSSLQNIPES LRRQSNVELG EAQEVHPGGR SKVEDPGRKA GASDIRGYLD RSVSYPRPEG
     KMNAVDSVHS ADSRYEESPA PALPQTSGAS QRRLSSSSSA APQYRKPHCS VLEKVSRIEE
     REQGRHRPLS VGSSAYGPGY RPGRTGPTPS TSSSDLDDPK AGSVHFSEST EHLRNGEQNP
     PNGEAKQEEA SRPQCSHLIR RAPADGRGPP ARGGEPSRPE ARLLRSQSTF QLYSEAEREA
     SWSEDRPGTP ESPLLDAPFS RAYRNSIKDA QSRVLGATSF RRRDLEPGTP ATSRPWRPRP
     ASAHVGMRSP EAAVPSSSPH TPRERHSVTP AAPQAARRGP RRRLTVEQKK RSYSEPEKMN
     EVGVSEEAEP TPCGPPRPAQ PRFSESTVAD RRRIFERDGK ACSTLSLSGP ELKQFQQSAL
     ADYIQRKTGK RPTGAACTPE AGLRERAQSA YLQAGPAAPD GPGLASACSL SSLREPEALP
     RKEHTHPSAA DGPQAPRDRS SSFASGRLVG ERRRWDPQVP RQLLSGANCE PRGVQRMDGA
     PGGPPSWGMV AGKAGKSKSA EDLLERSDTL AVPVHVRSRS SPTSDKKGQD VLLREGSNFG
     FVKDPCCLAG PGPRSLSCSD KGQNELALPL HHPTPCWNGS GCKATVASSA PPESSGAADH
     LKQRRAPGPR PLSAGMHGHF PDARAASLSS PLPSPVPSAS PVPSSYRSQL AMDQQTGQQP
     PSSPASAVTQ PTSPRSPELS SPAYGLGEGM WKRTSLPQRP PPPWVKWAHA VREDGLAEDT
     LAPEFANLKH YRNQPSRPSS CSTSDPDTPG RISLRISESA LQPSPPPRGD YDDEVFMKDL
     HPKVTSSPTF EALPPPPPPS PPSEEPLVNG TDDFPPPPPP QALCEVLLDG EASTEAGSGP
     CRIPRVMVTR EGHVPGAAHS EGSQIMTATP PQTSAKGSEA ESNTPSSASA QPQLNGSPGK
     QLCPSQTRNL TYEPVERTQD LGKKTHAEPQ KTSEDIRTEA LAKEIVHQDK SLADILDPDS
     RMKTTMDLME GLFPGDASVL MDSGAKRKAL DITARRAGCE AKASDHKEAV SVLVNCPAYY
     SVSAAKAELL NKIKDMPEEL QEEEGQEDVN EKKAELIGSL THKLESLQEA KGSLLTDIKL
     NNALGEEVEA LISELCKPNE FDKYKMFIGD LDKVVNLLLS LSGRLARVEN VLRGLGEDAS
     KEERSSLNEK RKVLAGQHED ARELKENLDR RERVVLDILA NYLSAEQLQD YQHFVKMKST
     LLIEQRKLDD KIKLGQEQVR CLLESLPSDF RPKAGAISLP PALTGHATPG GTSVFGGVFP
     TLTSPL
//
ID   PDE7B_MOUSE             Reviewed;         446 AA.
AC   Q9QXQ1; A1L3T2;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=cAMP-specific 3',5'-cyclic phosphodiesterase 7B;
DE            EC=3.1.4.17;
GN   Name=Pde7b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20087273; PubMed=10618442; DOI=10.1073/pnas.97.1.472;
RA   Hetman J.M., Soderling S.H., Glavas N.A., Beavo J.A.;
RT   "Cloning and characterization of PDE7B, a cAMP-specific
RT   phosphodiesterase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:472-476(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RX   MEDLINE=20329226; PubMed=10872825; DOI=10.1006/bbrc.2000.2743;
RA   Gardner C.E., Robas N.M., Cawkill D., Fidock M.D.;
RT   "Cloning and characterisation of the human and mouse PDE7B, a novel
RT   cAMP-specific nucleotide phosphodiesterase.";
RL   Biochem. Biophys. Res. Commun. 272:186-192(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Hydrolyzes the second messenger cAMP, which is a key
CC       regulator of many important physiological processes. May be
CC       involved in the control of cAMP-mediated neural activity and cAMP
CC       metabolism in the brain.
CC   -!- CATALYTIC ACTIVITY: Adenosine 3',5'-cyclic phosphate + H(2)O =
CC       adenosine 5'-phosphate.
CC   -!- COFACTOR: Binds 2 divalent metal cations per subunit. Site 1 may
CC       preferentially bind zinc ions, while site 2 has a preference for
CC       magnesium and/or manganese ions (By similarity).
CC   -!- ENZYME REGULATION: Inhibited by dipyridamole, IBMX and SCH 51866.
CC       Insensitive to zaprinast, rolipram, and milrinone.
CC   -!- PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from
CC       3',5'-cyclic AMP: step 1/1.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain.
CC   -!- DOMAIN: Composed of a C-terminal catalytic domain containing two
CC       putative divalent metal sites and an N-terminal regulatory domain.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase
CC       family. PDE7 subfamily.
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DR   EMBL; AF190639; AAF25195.1; -; mRNA.
DR   EMBL; AJ251859; CAB92530.1; -; mRNA.
DR   EMBL; BC130267; AAI30268.1; -; mRNA.
DR   IPI; IPI00135368; -.
DR   RefSeq; NP_038903.3; NM_013875.5.
DR   UniGene; Mm.425617; -.
DR   ProteinModelPortal; Q9QXQ1; -.
DR   SMR; Q9QXQ1; 100-416.
DR   STRING; Q9QXQ1; -.
DR   PhosphoSite; Q9QXQ1; -.
DR   PRIDE; Q9QXQ1; -.
DR   Ensembl; ENSMUST00000020165; ENSMUSP00000020165; ENSMUSG00000019990.
DR   GeneID; 29863; -.
DR   KEGG; mmu:29863; -.
DR   UCSC; uc007eob.1; mouse.
DR   CTD; 29863; -.
DR   MGI; MGI:1352752; Pde7b.
DR   GeneTree; ENSGT00590000082915; -.
DR   HOGENOM; HBG403038; -.
DR   HOVERGEN; HBG053543; -.
DR   InParanoid; Q9QXQ1; -.
DR   OMA; VHDRHFM; -.
DR   OrthoDB; EOG4JDH6S; -.
DR   PhylomeDB; Q9QXQ1; -.
DR   BRENDA; 3.1.4.17; 244.
DR   NextBio; 307074; -.
DR   ArrayExpress; Q9QXQ1; -.
DR   Bgee; Q9QXQ1; -.
DR   CleanEx; MM_PDE7B; -.
DR   Genevestigator; Q9QXQ1; -.
DR   GermOnline; ENSMUSG00000019990; Mus musculus.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR003607; Metal-dep_PHydrolase_HD_dom.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR023174; PDEase_CS.
DR   Gene3D; G3DSA:1.10.1300.10; PDEase_catalytic_dom; 1.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00471; HDc; 1.
DR   PROSITE; PS00126; PDEASE_I; 1.
PE   2: Evidence at transcript level;
KW   cAMP; Hydrolase; Metal-binding; Phosphoprotein.
FT   CHAIN         1    446       cAMP-specific 3',5'-cyclic
FT                                phosphodiesterase 7B.
FT                                /FTId=PRO_0000198837.
FT   REGION      172    410       Catalytic (By similarity).
FT   ACT_SITE    173    173       Proton donor (By similarity).
FT   METAL       177    177       Divalent metal cation 1 (By similarity).
FT   METAL       213    213       Divalent metal cation 1 (By similarity).
FT   METAL       214    214       Divalent metal cation 1 (By similarity).
FT   METAL       214    214       Divalent metal cation 2 (By similarity).
FT   METAL       323    323       Divalent metal cation 1 (By similarity).
FT   MOD_RES      45     45       Phosphoserine (By similarity).
FT   MOD_RES      74     74       Phosphoserine (By similarity).
SQ   SEQUENCE   446 AA;  51337 MW;  7C052664B693A5A8 CRC64;
     MSCLMVERCG EVLFESPEQS VKCVCMLGDV RLRGQTGVPA ERRGSYPFID FRLLNNTTHS
     GEIGTKKKVK RLLSFQRYFH ASRLLRGIIP QAPLHLLDED YLGQARHMLS KVGTWDFDIF
     LFDRLTNGNS LVTLLCHLFN SHGLIHHFKL DMVTLHRFLV MVQEDYHGHN PYHNAVHAAD
     VTQAMHCYLK EPKLASFLTP LDIMLGLLAA AAHDVDHPGV NQPFLIKTNH HLANLYQNMS
     VLENHHWRST IGMLRESRLL AHLPKEMTQD IEQQLGSLIL ATDINRQNEF LTRLKAHLHN
     KDLRLENVQD RHFMLQIALK CADICNPCRI WEMSKQWSER VCEEFYRQGD LEQKFELEIS
     PLCNQQKDSI PSIQIGFMTY IVEPLFREWA RFTGNSTLSE NMLSHLAHNK AQWKSLLSNQ
     HRRRGSGQDL AGPAPETLEQ TEGATP
//
ID   PLEC_MOUSE              Reviewed;        4691 AA.
AC   Q9QXS1; Q6S384; Q6S389; Q6S394; Q9CS65; Q9QUT2; Q9QXQ8; Q9QXQ9;
AC   Q9QXR0; Q9QXR1; Q9QXR2; Q9QXR3; Q9QXR4; Q9QXR5; Q9QXR6; Q9QXR7;
AC   Q9QXR8; Q9QXR9; Q9QXS0; Q9QXS2; Q9QXS3;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 109.
DE   RecName: Full=Plectin;
DE            Short=PCN;
DE            Short=PLTN;
DE   AltName: Full=Plectin-1;
DE   AltName: Full=Plectin-6;
GN   Name=Plec; Synonyms=Plec1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX   PubMed=14672974; DOI=10.1101/gr.1225204;
RA   Zhang T., Haws P., Wu Q.;
RT   "Multiple variable first exons: a mechanism for cell- and tissue-
RT   specific gene regulation.";
RL   Genome Res. 14:79-89(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-964, ALTERNATIVE SPLICING, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Brain, Embryo, Heart, Kidney, Skeletal muscle, and Testis;
RX   MEDLINE=20025755; PubMed=10556294; DOI=10.1093/hmg/8.13.2461;
RA   Fuchs P., Zoerer M., Rezniczek G.A., Spazierer D., Oehler S.,
RA   Castanon M.J., Hauptmann R., Wiche G.;
RT   "Unusual 5' transcript complexity of plectin isoforms: novel tissue-
RT   specific exons modulate actin binding activity.";
RL   Hum. Mol. Genet. 8:2461-2472(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 181-812.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PROTEIN SEQUENCE OF 629-633, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   INTERACTION WITH NESPRIN-3.
RX   PubMed=16330710; DOI=10.1083/jcb.200506083;
RA   Wilhelmsen K., Litjens S.H.M., Kuikman I., Tshimbalanga N.,
RA   Janssen H., van den Bout I., Raymond K., Sonnenberg A.;
RT   "Nesprin-3, a novel outer nuclear membrane protein, associates with
RT   the cytoskeletal linker protein plectin.";
RL   J. Cell Biol. 171:799-810(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2788; TYR-3040;
RP   TYR-3369; TYR-3797 AND TYR-4622, PHOSPHORYLATION [LARGE SCALE
RP   ANALYSIS] AT TYR-26 (ISOFORM PLEC-1A), AND MASS SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-728; SER-1443 AND
RP   SER-4393, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-823, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17208939; DOI=10.1074/mcp.M600218-MCP200;
RA   Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
RT   "Mitochondrial phosphoproteome revealed by an improved IMAC method and
RT   MS/MS/MS.";
RL   Mol. Cell. Proteomics 6:669-676(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4393; SER-4397; SER-4629
RP   AND SER-4633, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4391 AND SER-4393, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-1729; SER-4393
RP   AND SER-4633, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4396 AND SER-4399, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4389 AND SER-4393, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 181-417, AND INTERACTION
RP   WITH VIM.
RX   PubMed=15128297; DOI=10.1111/j.1432-1033.2004.04095.x;
RA   Sevcik J., Urbanikova L., Kost'an J., Janda L., Wiche G.;
RT   "Actin-binding domain of mouse plectin. Crystal structure and binding
RT   to vimentin.";
RL   Eur. J. Biochem. 271:1873-1884(2004).
CC   -!- FUNCTION: Interlinks intermediate filaments with microtubules and
CC       microfilaments and anchors intermediate filaments to desmosomes or
CC       hemidesmosomes. May be involved not only in the cross-linking and
CC       stabilization of cytoskeletal intermediate filaments network, but
CC       also in the regulation of their dynamics.
CC   -!- SUBUNIT: Homodimer or homotetramer (By similarity). Interacts (via
CC       actin-binding domain) with Nesprin-3. Interacts (via CH 1 domain)
CC       with VIM (via rod region).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=16;
CC       Name=PLEC-1,2A;
CC         IsoId=Q9QXS1-1; Sequence=Displayed;
CC       Name=PLEC-1;
CC         IsoId=Q9QXS1-2; Sequence=VSP_005048;
CC       Name=PLEC-1A;
CC         IsoId=Q9QXS1-3; Sequence=VSP_005036, VSP_005045, VSP_005048;
CC         Note=Phosphorylated on Ser-21 (By similarity). Phosphorylated on
CC         Tyr-26;
CC       Name=PLEC-1B,2A;
CC         IsoId=Q9QXS1-4; Sequence=VSP_005037, VSP_005045;
CC       Name=PLEC-1B;
CC         IsoId=Q9QXS1-5; Sequence=VSP_005037, VSP_005045, VSP_005048;
CC       Name=PLEC-0,1C;
CC         IsoId=Q9QXS1-6; Sequence=VSP_005039, VSP_005047, VSP_005048;
CC       Name=PLEC-0,1C,2A;
CC         IsoId=Q9QXS1-7; Sequence=VSP_005039, VSP_005047;
CC       Name=PLEC-0,1C,2A,3A;
CC         IsoId=Q9QXS1-8; Sequence=VSP_005039, VSP_005047, VSP_005049;
CC       Name=PLEC-1D,2A;
CC         IsoId=Q9QXS1-9; Sequence=VSP_005032, VSP_005041;
CC       Name=PLEC-1D;
CC         IsoId=Q9QXS1-10; Sequence=VSP_005032, VSP_005041, VSP_005048;
CC       Name=PLEC-1E,2A;
CC         IsoId=Q9QXS1-11; Sequence=VSP_005033, VSP_005042;
CC       Name=PLEC-1E;
CC         IsoId=Q9QXS1-12; Sequence=VSP_005033, VSP_005042, VSP_005048;
CC       Name=PLEC-1F;
CC         IsoId=Q9QXS1-13; Sequence=VSP_005034, VSP_005043, VSP_005048;
CC       Name=PLEC-1G;
CC         IsoId=Q9QXS1-14; Sequence=VSP_005038, VSP_005046, VSP_005048;
CC       Name=PLEC-1H;
CC         IsoId=Q9QXS1-15; Sequence=VSP_005040;
CC       Name=PLEC-1I;
CC         IsoId=Q9QXS1-16; Sequence=VSP_005035, VSP_005044;
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in lung, brain, small
CC       intestine, muscle, heart and skin with lower levels found in
CC       kidney, liver, uterus, spleen and salivary gland.
CC   -!- DOMAIN: The N-terminus interacts with actin, the C-terminus with
CC       vimentin, desmin, GFAP, cytokeratins, lamin B; whereas both the N-
CC       and the C-terminus can bind integrin beta-4.
CC   -!- PTM: Phosphorylated by CDK1; regulates dissociation from
CC       intermediate filaments during mitosis. Phosphorylated upon DNA
CC       damage, probably by ATM or ATR (By similarity). Isoform PLEC-1A is
CC       phosphorylated on Ser-21 (By similarity). Isoform PLEC-1A is
CC       phosphorylated on Tyr-26.
CC   -!- SIMILARITY: Belongs to the plakin or cytolinker family.
CC   -!- SIMILARITY: Contains 1 actin-binding domain.
CC   -!- SIMILARITY: Contains 2 CH (calponin-homology) domains.
CC   -!- SIMILARITY: Contains 33 plectin repeats.
CC   -!- SIMILARITY: Contains 4 spectrin repeats.
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DR   EMBL; AY480033; AAR95666.1; -; mRNA.
DR   EMBL; AY480038; AAR95671.1; -; mRNA.
DR   EMBL; AY480043; AAR95676.1; -; mRNA.
DR   EMBL; AF188006; AAF18066.1; -; mRNA.
DR   EMBL; AF188007; AAF18067.1; -; mRNA.
DR   EMBL; AF188008; AAF18068.1; -; mRNA.
DR   EMBL; AF188009; AAF18069.1; -; mRNA.
DR   EMBL; AF188010; AAF18070.1; -; mRNA.
DR   EMBL; AF188011; AAF18071.1; -; mRNA.
DR   EMBL; AF188012; AAF18072.1; -; mRNA.
DR   EMBL; AF188013; AAF18073.1; -; mRNA.
DR   EMBL; AF188014; AAF18074.1; -; mRNA.
DR   EMBL; AF188015; AAF18075.1; -; mRNA.
DR   EMBL; AF188016; AAF18076.1; -; mRNA.
DR   EMBL; AF188017; AAF18077.1; -; mRNA.
DR   EMBL; AF188018; AAF18078.1; -; mRNA.
DR   EMBL; AF188019; AAF18079.1; -; mRNA.
DR   EMBL; AF188020; AAF18080.1; -; mRNA.
DR   EMBL; AF188021; AAF18081.1; -; mRNA.
DR   EMBL; AF188022; AAF18082.1; -; mRNA.
DR   EMBL; AF188023; AAF18083.1; -; mRNA.
DR   EMBL; AK017743; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00229509; -.
DR   IPI; IPI00230061; -.
DR   IPI; IPI00400209; -.
DR   IPI; IPI00400214; -.
DR   IPI; IPI00400215; -.
DR   IPI; IPI00421267; -.
DR   IPI; IPI00421268; -.
DR   IPI; IPI00421271; -.
DR   IPI; IPI00468273; -.
DR   IPI; IPI00625928; -.
DR   PIR; D59404; D59404.
DR   RefSeq; NP_001157012.1; NM_001163540.1.
DR   RefSeq; NP_001157014.1; NM_001163542.1.
DR   RefSeq; NP_001157021.1; NM_001163549.1.
DR   RefSeq; NP_001157675.1; NM_001164203.1.
DR   RefSeq; NP_035247.2; NM_011117.2.
DR   RefSeq; NP_958791.2; NM_201389.2.
DR   RefSeq; NP_958796.2; NM_201394.2.
DR   UniGene; Mm.234912; -.
DR   PDB; 1SH5; X-ray; 2.00 A; A/B=181-417.
DR   PDB; 1SH6; X-ray; 2.00 A; A=181-417.
DR   PDBsum; 1SH5; -.
DR   PDBsum; 1SH6; -.
DR   ProteinModelPortal; Q9QXS1; -.
DR   SMR; Q9QXS1; 181-411, 424-641, 667-857, 2789-3030, 3117-3358, 3448-3688, 3783-4612.
DR   STRING; Q9QXS1; -.
DR   PhosphoSite; Q9QXS1; -.
DR   PRIDE; Q9QXS1; -.
DR   Ensembl; ENSMUST00000023226; ENSMUSP00000023226; ENSMUSG00000022565.
DR   Ensembl; ENSMUST00000054449; ENSMUSP00000057158; ENSMUSG00000022565.
DR   Ensembl; ENSMUST00000071869; ENSMUSP00000071765; ENSMUSG00000022565.
DR   Ensembl; ENSMUST00000072692; ENSMUSP00000072478; ENSMUSG00000022565.
DR   Ensembl; ENSMUST00000073418; ENSMUSP00000073124; ENSMUSG00000022565.
DR   Ensembl; ENSMUST00000074834; ENSMUSP00000074383; ENSMUSG00000022565.
DR   Ensembl; ENSMUST00000076355; ENSMUSP00000075693; ENSMUSG00000022565.
DR   Ensembl; ENSMUST00000076442; ENSMUSP00000075772; ENSMUSG00000022565.
DR   Ensembl; ENSMUST00000080857; ENSMUSP00000079668; ENSMUSG00000022565.
DR   Ensembl; ENSMUST00000089610; ENSMUSP00000087037; ENSMUSG00000022565.
DR   GeneID; 18810; -.
DR   KEGG; mmu:18810; -.
DR   UCSC; uc007wir.1; mouse.
DR   UCSC; uc007wis.1; mouse.
DR   UCSC; uc007wja.1; mouse.
DR   UCSC; uc007wjb.1; mouse.
DR   CTD; 18810; -.
DR   MGI; MGI:1277961; Plec.
DR   GeneTree; ENSGT00550000074288; -.
DR   HOVERGEN; HBG053616; -.
DR   InParanoid; Q9QXS1; -.
DR   OrthoDB; EOG4SN1MR; -.
DR   PhylomeDB; Q9QXS1; -.
DR   NextBio; 295126; -.
DR   ArrayExpress; Q9QXS1; -.
DR   Bgee; Q9QXS1; -.
DR   CleanEx; MM_PLEC1; -.
DR   Genevestigator; Q9QXS1; -.
DR   GermOnline; ENSMUSG00000022565; Mus musculus.
DR   GO; GO:0043292; C:contractile fiber; IDA:MGI.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005626; C:insoluble fraction; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR001101; Plectin_repeat.
DR   InterPro; IPR005326; S10_plectin_N.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 2.
DR   Pfam; PF00307; CH; 2.
DR   Pfam; PF00681; Plectin; 18.
DR   Pfam; PF03501; S10_plectin; 1.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00250; PLEC; 35.
DR   SMART; SM00150; SPEC; 6.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS00019; ACTININ_1; 1.
DR   PROSITE; PS00020; ACTININ_2; 1.
DR   PROSITE; PS50021; CH; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1   4691       Plectin.
FT                                /FTId=PRO_0000078136.
FT   DOMAIN      181    411       Actin-binding.
FT   DOMAIN      185    293       CH 1.
FT   DOMAIN      306    408       CH 2.
FT   REPEAT      653    727       Spectrin 1.
FT   REPEAT      748    832       Spectrin 2.
FT   REPEAT      845    938       Spectrin 3.
FT   REPEAT     1323   1423       Spectrin 4.
FT   REPEAT     2795   2832       Plectin 1.
FT   REPEAT     2833   2870       Plectin 2.
FT   REPEAT     2871   2908       Plectin 3.
FT   REPEAT     2909   2946       Plectin 4.
FT   REPEAT     2947   2984       Plectin 5.
FT   REPEAT     2988   3022       Plectin 6.
FT   REPEAT     3123   3160       Plectin 7.
FT   REPEAT     3161   3198       Plectin 8.
FT   REPEAT     3199   3236       Plectin 9.
FT   REPEAT     3237   3274       Plectin 10.
FT   REPEAT     3275   3312       Plectin 11.
FT   REPEAT     3315   3350       Plectin 12.
FT   REPEAT     3492   3529       Plectin 13.
FT   REPEAT     3530   3567       Plectin 14.
FT   REPEAT     3568   3605       Plectin 15.
FT   REPEAT     3606   3643       Plectin 16.
FT   REPEAT     3647   3681       Plectin 17.
FT   REPEAT     3827   3864       Plectin 18.
FT   REPEAT     3865   3902       Plectin 19.
FT   REPEAT     3903   3940       Plectin 20.
FT   REPEAT     3941   3978       Plectin 21.
FT   REPEAT     3982   4015       Plectin 22.
FT   REPEAT     4070   4107       Plectin 23.
FT   REPEAT     4108   4145       Plectin 24.
FT   REPEAT     4146   4183       Plectin 25.
FT   REPEAT     4184   4221       Plectin 26.
FT   REPEAT     4225   4259       Plectin 27.
FT   REPEAT     4272   4312       Plectin 28.
FT   REPEAT     4415   4452       Plectin 29.
FT   REPEAT     4453   4490       Plectin 30.
FT   REPEAT     4491   4528       Plectin 31.
FT   REPEAT     4529   4566       Plectin 32.
FT   REPEAT     4567   4604       Plectin 33.
FT   REGION        1   1478       Globular 1 (By similarity).
FT   REGION     1479   2762       Central fibrous rod domain (By
FT                                similarity).
FT   REGION     2763   4691       Globular 2 (By similarity).
FT   REGION     4257   4307       Binding to intermediate filaments (By
FT                                similarity).
FT   REGION     4632   4647       4 X 4 AA tandem repeats of G-S-R-X.
FT   COILED     1477   1697       Potential.
FT   COILED     1729   2764       Potential.
FT   MOD_RES     193    193       N6-acetyllysine (By similarity).
FT   MOD_RES     212    212       Phosphoserine.
FT   MOD_RES     728    728       Phosphoserine.
FT   MOD_RES     790    790       Phosphoserine (By similarity).
FT   MOD_RES     823    823       Phosphothreonine.
FT   MOD_RES    1443   1443       Phosphoserine.
FT   MOD_RES    1452   1452       Phosphoserine (By similarity).
FT   MOD_RES    1652   1652       Phosphoserine (By similarity).
FT   MOD_RES    1729   1729       Phosphoserine.
FT   MOD_RES    2524   2524       Phosphoserine (By similarity).
FT   MOD_RES    2788   2788       Phosphotyrosine.
FT   MOD_RES    2821   2821       Phosphothreonine (By similarity).
FT   MOD_RES    2848   2848       N6-acetyllysine (By similarity).
FT   MOD_RES    3040   3040       Phosphotyrosine.
FT   MOD_RES    3098   3098       N6-acetyllysine (By similarity).
FT   MOD_RES    3369   3369       Phosphotyrosine.
FT   MOD_RES    3427   3427       N6-acetyllysine (By similarity).
FT   MOD_RES    3797   3797       Phosphotyrosine.
FT   MOD_RES    4037   4037       Phosphothreonine (By similarity).
FT   MOD_RES    4162   4162       Phosphotyrosine (By similarity).
FT   MOD_RES    4389   4389       Phosphoserine.
FT   MOD_RES    4391   4391       Phosphoserine.
FT   MOD_RES    4392   4392       Phosphoserine (By similarity).
FT   MOD_RES    4393   4393       Phosphoserine.
FT   MOD_RES    4396   4396       Phosphoserine.
FT   MOD_RES    4397   4397       Phosphoserine.
FT   MOD_RES    4398   4398       Phosphoserine (By similarity).
FT   MOD_RES    4399   4399       Phosphoserine.
FT   MOD_RES    4400   4400       Phosphotyrosine (By similarity).
FT   MOD_RES    4403   4403       Phosphoserine (By similarity).
FT   MOD_RES    4409   4409       Phosphothreonine (By similarity).
FT   MOD_RES    4418   4418       Phosphothreonine (By similarity).
FT   MOD_RES    4546   4546       Phosphothreonine; by CDK1 (By
FT                                similarity).
FT   MOD_RES    4618   4618       Phosphotyrosine (By similarity).
FT   MOD_RES    4620   4620       Phosphoserine (By similarity).
FT   MOD_RES    4622   4622       Phosphotyrosine.
FT   MOD_RES    4625   4625       Phosphoserine (By similarity).
FT   MOD_RES    4627   4627       Phosphoserine (By similarity).
FT   MOD_RES    4629   4629       Phosphoserine.
FT   MOD_RES    4633   4633       Phosphoserine.
FT   MOD_RES    4635   4635       Phosphothreonine (By similarity).
FT   MOD_RES    4649   4649       Phosphoserine (By similarity).
FT   MOD_RES    4665   4665       Phosphoserine (By similarity).
FT   MOD_RES    4682   4682       Phosphoserine (By similarity).
FT   VAR_SEQ       1    242       Missing (in isoform PLEC-1H).
FT                                /FTId=VSP_005040.
FT   VAR_SEQ       1     66       MVAGMLMPLDRLRAIYEVLFREGVMVAKKDRRPRSLHPHVP
FT                                GVTNLQVMRAMASLKARGLVRETFA -> MSGEDSEVRPVA
FT                                VAEGSSNGSSGSPSPGDTLPWNLGKTQRSRRSGGGSVGNGS
FT                                VLDPAERAVIRIA (in isoform PLEC-0,1C,
FT                                isoform PLEC-0,1C,2A,3A and isoform PLEC-
FT                                0,1C,2A).
FT                                /FTId=VSP_005039.
FT   VAR_SEQ       1     44       MVAGMLMPLDRLRAIYEVLFREGVMVAKKDRRPRSLHPHVP
FT                                GVT -> MAGTWAAKGVFTSQREVLLERPCWLDGGCEQVRR
FT                                GYLYGQLCCV (in isoform PLEC-1G).
FT                                /FTId=VSP_005038.
FT   VAR_SEQ       1     37       MVAGMLMPLDRLRAIYEVLFREGVMVAKKDRRPRSLH ->
FT                                MSQHRLRVPEPEGLGSKRTSSEDNLYLAVLRASEGKK (in
FT                                isoform PLEC-1A).
FT                                /FTId=VSP_005036.
FT   VAR_SEQ       1     37       MVAGMLMPLDRLRAIYEVLFREGVMVAKKDRRPRSLH ->
FT                                MEPSGSLFPSLVVVGHVVTLAAVWHWRKGHRQAKDEQ (in
FT                                isoform PLEC-1B and isoform PLEC-1B,2A).
FT                                /FTId=VSP_005037.
FT   VAR_SEQ       1     33       MVAGMLMPLDRLRAIYEVLFREGVMVAKKDRRP -> MNET
FT                                VCRRKLSPSGSTNTLSRLRGTSVTCTKTS (in isoform
FT                                PLEC-1I).
FT                                /FTId=VSP_005035.
FT   VAR_SEQ       1     28       MVAGMLMPLDRLRAIYEVLFREGVMVAK -> MAHLLTSGP
FT                                PPDEQDFIQAYEEVREKYK (in isoform PLEC-1F).
FT                                /FTId=VSP_005034.
FT   VAR_SEQ       1     15       MVAGMLMPLDRLRAI -> MDPSRAIQHEISSLK (in
FT                                isoform PLEC-1E and isoform PLEC-1E,2A).
FT                                /FTId=VSP_005033.
FT   VAR_SEQ       1      5       MVAGM -> MKIVP (in isoform PLEC-1D and
FT                                isoform PLEC-1D,2A).
FT                                /FTId=VSP_005032.
FT   VAR_SEQ       6    180       Missing (in isoform PLEC-1D and isoform
FT                                PLEC-1D,2A).
FT                                /FTId=VSP_005041.
FT   VAR_SEQ      16    180       Missing (in isoform PLEC-1E and isoform
FT                                PLEC-1E,2A).
FT                                /FTId=VSP_005042.
FT   VAR_SEQ      29    180       Missing (in isoform PLEC-1F).
FT                                /FTId=VSP_005043.
FT   VAR_SEQ      34    180       Missing (in isoform PLEC-1I).
FT                                /FTId=VSP_005044.
FT   VAR_SEQ      38    180       Missing (in isoform PLEC-1A, isoform
FT                                PLEC-1B and isoform PLEC-1B,2A).
FT                                /FTId=VSP_005045.
FT   VAR_SEQ      45    180       Missing (in isoform PLEC-1G).
FT                                /FTId=VSP_005046.
FT   VAR_SEQ      67    180       Missing (in isoform PLEC-0,1C, isoform
FT                                PLEC-0,1C,2A and isoform PLEC-
FT                                0,1C,2A,3A).
FT                                /FTId=VSP_005047.
FT   VAR_SEQ     202    206       Missing (in isoform PLEC-1, isoform PLEC-
FT                                1A, isoform PLEC-1B, isoform PLEC-1D,
FT                                isoform PLEC-1E, isoform PLEC-1G, isoform
FT                                PLEC-1F and isoform PLEC-0,1C).
FT                                /FTId=VSP_005048.
FT   VAR_SEQ     239    239       E -> ERDVIRSVRLPRE (in isoform PLEC-
FT                                0,1C,2A,3A).
FT                                /FTId=VSP_005049.
FT   HELIX       182    199
FT   HELIX       205    207
FT   TURN        214    220
FT   HELIX       222    232
FT   HELIX       244    260
FT   HELIX       270    274
FT   HELIX       278    292
FT   TURN        293    296
FT   HELIX       308    319
FT   TURN        320    322
FT   HELIX       333    335
FT   HELIX       339    346
FT   TURN        350    352
FT   HELIX       355    360
FT   HELIX       363    378
FT   HELIX       386    389
FT   STRAND      390    393
FT   HELIX       396    409
SQ   SEQUENCE   4691 AA;  534216 MW;  9574A9C80E88DA79 CRC64;
     MVAGMLMPLD RLRAIYEVLF REGVMVAKKD RRPRSLHPHV PGVTNLQVMR AMASLKARGL
     VRETFAWCHF YWYLTNEGID HLRQYLHLPP EIVPASLQRV RRPVAMVIPA RRRSPHVQTM
     QGPLGCPPKR GPLPAEDPAR EERQVYRRKE REEGAPETPV VSATTVGTLA RPGPEPAPAT
     DERDRVQKKT FTKWVNKHLI KHWRAEAQRH ISDLYEDLRD GHNLISLLEV LSGDSLPREK
     GRMRFHKLQN VQIALDYLRH RQVKLVNIRN DDIADGNPKL TLGLIWTIIL HFQISDIQVS
     GQSEDMTAKE KLLLWSQRMV EGYQGLRCDN FTTSWRDGRL FNAIIHRHKP MLIDMNKVYR
     QTNLENLDQA FSVAERDLGV TRLLDPEDVD VPQPDEKSII TYVSSLYDAM PRVPGAQDGV
     RANELQLRWQ EYRELVLLLL QWIRHHTAAF EERKFPSSFE EIEILWCQFL KFKETELPAK
     EADKNRSKVI YQSLEGAVQA GQLKIPPGYH PLDVEKEWGK LHVAILEREK QLRSEFERLE
     CLQRIVSKLQ MEAGLCEEQL NQADALLQSD IRLLASGKVA QRAGEVERDL DKADGMIRLL
     FNDVQTLKDG RHPQGEQMYR RVYRLHERLV AIRTEYNLRL KAGVGAPVTQ VTLQSTQRRP
     ELEDSTLRYL QDLLAWVEEN QRRIDSAEWG VDLPSVEAQL GSHRGMHQSI EEFRAKIERA
     RNDESQLSPA TRGAYRDCLG RLDLQYAKLL NSSKARLRSL ESLHGFVAAA TKELMWLNEK
     EEEEVGFDWS DRNTNMAAKK ESYSALMREL EMKEKKIKEI QNTGDRLLRE DHPARPTVES
     FQAALQTQWS WMLQLCCCIE AHLKENTAYF QFFSDVREAE EQLQKLQETL RRKYSCDRTI
     TVTRLEDLLQ DAQDEKEQLN EYKGHLSGLA KRAKAIVQLK PRNPAHPVRG HVPLIAVCDY
     KQVEVTVHKG DQCQLVGPAQ PSHWKVLSGS SSEAAVPSVC FLVPPPNQEA QEAVARLEAQ
     HQALVTLWHQ LHVDMKSLLA WQSLSRDIQL IRSWSLVTFR TLKPEEQRQA LRNLELHYQA
     FLRDSQDAGG FGPEDRLVAE REYGSCSRHY QQLLQSLEQG EQEESRCQRC ISELKDIRLQ
     LEACETRTVH RLRLPLDKDP ARECAQRIAE QQKAQAEVEG LGKGVARLSA EAEKVLALPE
     PSPAAPTLRS ELELTLGKLE QVRSLSAIYL EKLKTISLVI RSTQGAEEVL KTHEEQLKEA
     QAVPATLQEL EATKASLKKL RAQAEAQQPV FNTLRDELRG AQEVGERLQQ RHGERDVEVE
     RWRERVTQLL ERWQAVLAQT DVRQRELEQL GRQLRYYRES ADPLSAWLQD AKRRQEQIQA
     VPIANCQAAR EQLRQEKALL EEIERHGEKV EECQKFAKQY INAIKDYELQ LITYKAQLEP
     VASPAKKPKV QSGSESVIQE YVDLRTRYSE LTTLTSQYIK FISETLRRME EEERLAEQQR
     AEERERLAEV EAALEKQRQL AEAHAQAKAQ AELEAQELQR RMQEEVARRE EAAVDAQQQK
     RSIQEELQHL RQSSEAEIQA KAQQVEAAER SRMRIEEEIR VVRLQLETTE RQRGGAEGEL
     QALRARAEEA EAQKRQAQEE AERLRRQVQD ESQRKRQAEA ELALRVKAEA EAAREKQRAL
     QALDELRLQA EEAERRLRQA EAERARQVQV ALETAQRSAE VELQSKRASF AEKTAQLERT
     LQEEHVTVAQ LREEAERRAQ QQAEAERARE EAERELERWQ LKANEALRLR LQAEEVAQQK
     SLAQADAEKQ KEEAEREARR RGKAEEQAVR QRELAEQELE KQRQLAEGTA QQRLAAEQEL
     IRLRAETEQG EQQRQLLEEE LARLQHEATA ATQKRQELEA ELAKVRAEME VLLASKARAE
     EESRSTSEKS KQRLEAEAGR FRELAEEAAR LRALAEEAKR QRQLAEEDAA RQRAEAERVL
     TEKLAAISEA TRLKTEAEIA LKEKEAENER LRRLAEDEAF QRRRLEEQAA LHKADIEERL
     AQLRKASESE LERQKGLVED TLRQRRQVEE EIMALKVSFE KAAAGKAELE LELGRIRSNA
     EDTMRSKEQA ELEAARQRQL AAEEEQRRRE AEERVQRSLA AEEEAARQRK VALEEVERLK
     AKVEEARRLR ERAEQESARQ LQLAQEAAQK RLQAEEKAHA FVVQQREEEL QQTLQQEQNM
     LDRLRSEAEA ARRAAEEAEE AREQAEREAA QSRKQVEEAE RLKQSAEEQA QAQAQAQAAA
     EKLRKEAEQE AARRAQAEQA ALKQKQAADA EMEKHKKFAE QTLRQKAQVE QELTTLRLQL
     EETDHQKSIL DEELQRLKAE VTEAARQRSQ VEEELFSVRV QMEELGKLKA RIEAENRALI
     LRDKDNTQRF LEEEAEKMKQ VAEEAARLSV AAQEAARLRQ LAEEDLAQQR ALAEKMLKEK
     MQAVQEATRL KAEAELLQQQ KELAQEQARR LQEDKEQMAQ QLVEETQGFQ RTLEAERQRQ
     LEMSAEAERL KLRMVEMSRA QARAEEDAQR FRKQAEEIGE KLHRTELATQ EKVTLVQTLE
     IQRQQSDHDA ERLREAIAEL EREKEKLKQE AKLLQLKSEE MQTVQQEQIL QETQALQKSF
     LSEKDSLLQR ERFIEQEKAK LEQLFQDEVA KAKQLREEQQ RQQQQMEQEK QELMASMEEA
     RRRQREAEEG VRRKQEELQH LEQQRQQQEK LLAEENQRLR ERLQRLEEEH RAALAHSEIA
     TTQAASTKAL PNGRDAPDGP SVEAEPEYTF EGLRQKVPAQ QLQEAGILSQ EELQRLAQGH
     TTVAELTQRE DVYRYLKGRS SIAGLLLKPT NEKLSVYTAL QRQLLSPGTA LILLEAQAAS
     GFLLDPVRNR RLTVNEAVKE GVVGPELHHK LLSAERAVTG YKDPYTGEQI SLFQAMKKDL
     IVRDHGVRLL EAQIATGGII DPVHSHRVPV DVAYKRGYFD EEMNRILSDP SDDTKGFFDP
     NTHENLTYLQ LLERCVEDPE TGLRLLPLTD KAAKGGELVY TDTEARDVFE KATVSAPFGK
     FQGRTVTIWE IINSEYFTAE QRRDLLQQFR TGHITVEKII KIVITVVEEH ERKGQLCFEG
     LRALVPAAEL LDSGVISHEL YQQLQRGERS VREVAEADSV RQALRGTNVI AGVWLEEAGQ
     KLSIYEALKK DLLQPEVAVA LLEAQAGTGH IIDPATSARL TVDEAVRAGL VGPELHEKLL
     SAEKAVTGYR DPYSGQSVSL FQALKKGLIP REQGLRLLDA QLSTGGIVDP SKSHRVPLDV
     AYARGYLDKE TNRALTSPRD DARVYHDPST QEPVTYSQLQ QRCRSDQLTG LSLLPLSEKA
     VRARQEEVYS ELQARETLEQ AKVEVPVGSF KGRAMTVWEL ISSEYFTEEQ RQELLRQFRT
     GKVTVEKVIK IVITIVEEVE TRRQERLSFS GLRAPVPASE LLDAKILSRA QFDQLKDGKT
     SVKELSEVGS VRTLLQGSGC LAGIYLEDSK EKVTIYEAMR RGLLRPSTAT LLLEAQAATG
     FLVDPVRNQR LYVHEAVKAG VVGPELHEKL LSAEKAVTGY KDPYSGNTIS LFQAMKKGLV
     LRDHAIRLLE AQVATGGIID PVHSHRLPVD VAYQRGYFDE EMNRVLADPS DDTKGFFDPN
     THENLTYLQL LERCVEDPET GLRLLPLKGA EKTEVVETTQ VYTEEETRRA FEETQIDIPG
     GGSHGGSSMS LWEVMQSNMI PEDQRARLMA DFQAGRVTKE RMIIIIIEII EKTEIIRQQN
     LASYDYVRRR LTAEDLYEAR IISLETYNLF REGTKNLREV LEMESAWRYL YGTGAVAGVY
     LPGSRQTLTI YQALKKGLLS AEVARLLLEA QAATGFLLDP VKGERLTVDE AVRKGLVGPE
     LHDRLLSAER AVTGYRDPYT EQTISLFQAM KKELIPAEEA LRLLDAQLAT GGIVDPRLGF
     HLPLEVAYQR GYLNKDTHDQ LSEPSEVRSY VDPSTDERLS YTQLLKRCRR DDPSGQMLLL
     LSDARKLTFR GLRKQITVEE LVRSQVMDEA TALQLQEGLT SIEEVTKNLQ KFLEGTSCIA
     GVFVDATKER LSVYQAMKKG IIRPGTAFEL LEAQAATGYV IDPIKGLKLT VEEAVRMGIV
     GPEFKDKLLS AERAVTGYKD PYSGKLISLF QAMKKGLILK DHGIRLLEAQ IATGGIIDPE
     ESHRLPVEVA YKRGLFDEEM NEILTDPSDD TKGFFDPNTE ENLTYLQLME RCITDPQTGL
     CLLPLKEKKR ERKTSSKSSV RKRRVVIVDP ETGKEMSVYE AYRKGLIDHQ TYLELSEQEC
     EWEEITISSS DGVVKSMIID RRSGRQYDID DAITKNLIDR SALDQYRAGT LSITEFADML
     SGNAGGFRSR SSSVGSSSSY PISSAGPRTQ LASWSDPTEE TGPVAGILDT ETLEKVSITE
     AMHRNLVDNI TGQRLLEAQA CTGGIIDPST GERFPVTEAV NKGLVDKIMV DRINLAQKAF
     CGFEDPRTKT KMSAAQALKK GWLYYEAGQR FLEVQYLTGG LIEPDTPGRV SLDEALQRGT
     VDARTAQKLR DVSAYSKYLT CPKTKLKISY KDALDRSMVE EGTGLRLLEA AAQSSKGYYS
     PYSVSGSGST AGSRTGSRTG SRAGSRRGSF DATGSGFSMT FSSSSYSSSG YGRRYASGPS
     ASLGGPESAV A
//
ID   DREB_MOUSE              Reviewed;         706 AA.
AC   Q9QXS6; A2CG16; Q3V234; Q922X1; Q9QXS5;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   08-FEB-2011, entry version 89.
DE   RecName: Full=Drebrin;
DE   AltName: Full=Developmentally-regulated brain protein;
GN   Name=Dbn1; Synonyms=Drba;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND E2).
RC   STRAIN=129/Sv;
RX   MEDLINE=20100797; PubMed=10633083;
RA   Keon B.H., Jedrzejewski P.T., Paul D.L., Goodenough D.A.;
RT   "Isoform specific expression of the neuronal F-actin binding protein,
RT   drebrin, in specialized cells of stomach and kidney epithelia.";
RL   J. Cell Sci. 113:325-336(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A2).
RC   STRAIN=ICR;
RX   PubMed=11991718; DOI=10.1006/geno.2002.6764;
RA   Jin M., Tanaka S., Sekino Y., Ren Y., Yamazaki H., Kawai-Hirai R.,
RA   Kojima N., Shirao T.;
RT   "A novel, brain-specific mouse drebrin: cDNA cloning, chromosomal
RT   mapping, genomic structure, expression, and functional
RT   characterization.";
RL   Genomics 79:686-692(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E2).
RC   STRAIN=C57BL/6J; TISSUE=Embryonic head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM E2).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-683 (ISOFORM A).
RC   STRAIN=C57BL/6 X CBA;
RA   Shirao T., Kawai-Hirai R.;
RT   "Mouse genome for drebrin.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   PROTEIN SEQUENCE OF 2-10; 43-71; 140-147; 150-165; 178-185; 272-291
RP   AND 376-402, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RA   Bienvenut W.V., Serrels B., Brunton V.G., Frame M.C.;
RL   Submitted (FEB-2008) to UniProtKB.
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390 AND THR-394, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15648052; DOI=10.1002/pmic.200401066;
RA   Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,
RA   Hart G.W., Burlingame A.L.;
RT   "Quantitative analysis of both protein expression and serine /
RT   threonine post-translational modifications through stable isotope
RT   labeling with dithiothreitol.";
RL   Proteomics 5:388-398(2005).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; SER-344 AND
RP   SER-385, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Drebrins might play some role in cell migration,
CC       extension of neuronal processes and plasticity of dendrites,
CC       respectively (By similarity).
CC   -!- SUBUNIT: Binds F-actin (By similarity).
CC   -!- INTERACTION:
CC       P08050:Gja1 (xeno); NbExp=1; IntAct=EBI-445208, EBI-476947;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Additional isoforms seem to exist;
CC       Name=A;
CC         IsoId=Q9QXS6-1; Sequence=Displayed;
CC       Name=A2;
CC         IsoId=Q9QXS6-2; Sequence=VSP_004199, VSP_004200;
CC       Name=E2;
CC         IsoId=Q9QXS6-3; Sequence=VSP_004198;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain. Also present in
CC       stomach and to a lesser degree in kidney, colon, and urinary
CC       bladder. The E2 isoform is specifically expressed in adult
CC       stomach, kidney, and cultured cells.
CC   -!- SIMILARITY: Contains 1 ADF-H domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF187147; AAF25189.1; -; mRNA.
DR   EMBL; AF187148; AAF25190.1; -; mRNA.
DR   EMBL; AB064321; BAB86904.1; -; mRNA.
DR   EMBL; AK132060; BAE20965.1; -; mRNA.
DR   EMBL; CT009762; CAM17636.1; -; Genomic_DNA.
DR   EMBL; BC006714; AAH06714.1; -; mRNA.
DR   EMBL; AB028740; BAB87811.1; -; Genomic_DNA.
DR   IPI; IPI00135475; -.
DR   IPI; IPI00230338; -.
DR   IPI; IPI00331516; -.
DR   RefSeq; NP_001170842.1; NM_001177371.1.
DR   RefSeq; NP_001170843.1; NM_001177372.1.
DR   RefSeq; NP_062787.2; NM_019813.4.
DR   UniGene; Mm.19016; -.
DR   ProteinModelPortal; Q9QXS6; -.
DR   SMR; Q9QXS6; 1-139.
DR   IntAct; Q9QXS6; 5.
DR   STRING; Q9QXS6; -.
DR   PhosphoSite; Q9QXS6; -.
DR   PRIDE; Q9QXS6; -.
DR   Ensembl; ENSMUST00000054646; ENSMUSP00000050477; ENSMUSG00000034675.
DR   Ensembl; ENSMUST00000109925; ENSMUSP00000105551; ENSMUSG00000034675.
DR   GeneID; 56320; -.
DR   KEGG; mmu:56320; -.
DR   UCSC; uc007qrc.1; mouse.
DR   UCSC; uc007qre.1; mouse.
DR   CTD; 56320; -.
DR   MGI; MGI:1931838; Dbn1.
DR   eggNOG; roNOG08105; -.
DR   GeneTree; ENSGT00530000062953; -.
DR   HOGENOM; HBG281945; -.
DR   HOVERGEN; HBG000823; -.
DR   InParanoid; Q9QXS6; -.
DR   OMA; TTQKEGT; -.
DR   ArrayExpress; Q9QXS6; -.
DR   Bgee; Q9QXS6; -.
DR   CleanEx; MM_DBN1; -.
DR   Genevestigator; Q9QXS6; -.
DR   GermOnline; ENSMUSG00000034675; Mus musculus.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005522; F:profilin binding; ISS:UniProtKB.
DR   GO; GO:0007015; P:actin filament organization; IDA:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   InterPro; IPR002108; Actin-bd_cofilin/tropomyosin.
DR   Pfam; PF00241; Cofilin_ADF; 1.
DR   SMART; SM00102; ADF; 1.
DR   PROSITE; PS51263; ADF_H; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Alternative splicing; Cytoplasm;
KW   Developmental protein; Differentiation; Direct protein sequencing;
KW   Neurogenesis; Phosphoprotein.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    706       Drebrin.
FT                                /FTId=PRO_0000080009.
FT   DOMAIN        3    134       ADF-H.
FT   MOD_RES       2      2       N-acetylalanine.
FT   MOD_RES     134    134       Phosphoserine.
FT   MOD_RES     141    141       Phosphoserine (By similarity).
FT   MOD_RES     142    142       Phosphoserine.
FT   MOD_RES     344    344       Phosphoserine.
FT   MOD_RES     379    379       Phosphothreonine (By similarity).
FT   MOD_RES     383    383       Phosphothreonine (By similarity).
FT   MOD_RES     385    385       Phosphoserine.
FT   MOD_RES     387    387       Phosphoserine (By similarity).
FT   MOD_RES     390    390       Phosphoserine.
FT   MOD_RES     391    391       Phosphothreonine (By similarity).
FT   MOD_RES     393    393       Phosphoserine (By similarity).
FT   MOD_RES     394    394       Phosphothreonine.
FT   MOD_RES     658    658       Phosphoserine (By similarity).
FT   MOD_RES     679    679       Phosphotyrosine (By similarity).
FT   VAR_SEQ     322    367       Missing (in isoform E2).
FT                                /FTId=VSP_004198.
FT   VAR_SEQ     368    368       S -> R (in isoform A2).
FT                                /FTId=VSP_004199.
FT   VAR_SEQ     369    706       Missing (in isoform A2).
FT                                /FTId=VSP_004200.
FT   CONFLICT     79     79       K -> T (in Ref. 1; AAF25189/AAF25190 and
FT                                2; BAB86904).
FT   CONFLICT    649    649       Q -> QQ (in Ref. 3; BAE20965).
SQ   SEQUENCE   706 AA;  77287 MW;  39E542D2BB859346 CRC64;
     MAGVSFSGHR LELLAAYEEV IREESAADWA LYTYEDGSDD LKLAASGEGG LQELSGHFEN
     QKVMYGFCSV KDSQAALPKY VLINWVGEDV PDARKCACAS HVAKVAEFFQ GVDVIVNASS
     VEDIDAGAIG QRLSNGLARL SSPVLHRLRL REDENAEPVG TTYQKTDAAV EMKRINREQF
     WEQAKKEEEL RKEEERKKAL DARLRFEQER MEQERQEQEE RERRYREREQ QIEEHRRKQQ
     SLEAEEAKRR LKEQSIFGDQ RDEEEESQMK KSESEVEEAA AIIAQRPDNP REFFRQQERV
     ASASGGSCDA PAPAPFNHRP GRPYCPFIKA SDSGPSSSSS SSSSPPRTPF PYITCHRTPN
     LSSSLPCSHL DSHRRMAPTP IPTRSPSDSS TASTPIAEQI ERALDEVTSS QPPPPPPPPP
     PTQEAQETTP SLDEELSKEA KVTAAPEVWA GCAAEPPQAQ EPPLLQSSPL EDSMCTESPE
     QAALAAPAEP AASVTSVADV HAADTIETTT ATTDTTIANN VTPAAASLID LWPGNGEEAS
     TLQAEPRVPT PPSGAEASLA EVPLLNEAAQ EPLPPVGEGC ANLLNFDELP EPPATFCDPE
     EEVGETLAAS QVLTMPSALE EVDQVLEQEL EPEPHLLTNG ETTQKEGTQA SEGYFSQSQE
     EEFAQSEEPC AKVPPPVFYN KPPEIDITCW DADPVPEEEE GFEGGD
//
ID   CSEN_MOUSE              Reviewed;         256 AA.
AC   Q9QXT8; Q924L0; Q99PH9; Q99PI0; Q99PI2; Q99PI3; Q9JHZ5;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   08-FEB-2011, entry version 87.
DE   RecName: Full=Calsenilin;
DE   AltName: Full=A-type potassium channel modulatory protein 3;
DE   AltName: Full=DRE-antagonist modulator;
DE            Short=DREAM;
DE   AltName: Full=Kv channel-interacting protein 3;
DE            Short=KChIP3;
GN   Name=Kcnip3; Synonyms=Csen, Dream, Kchip3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3), NUCLEOTIDE SEQUENCE
RP   [GENOMIC DNA], TISSUE SPECIFICITY, AND VARIANT SER-14.
RC   STRAIN=129/Ola, and C57BL/6;
RX   MEDLINE=21109365; PubMed=11161465; DOI=10.1006/mcne.2000.0913;
RA   Spreafico F., Barski J.J., Farina C., Meyer M.;
RT   "Mouse DREAM/calsenilin/KChIP3: gene structure, coding potential and
RT   expression.";
RL   Mol. Cell. Neurosci. 17:1-16(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Jo D.G., Kim M., Jung Y.K.;
RT   "Cloning and charaterization of mouse calsenilin/DREAM.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-14.
RC   STRAIN=FVB/NJ; TISSUE=Brain;
RA   Deng L., Reid R.E., Leavitt B., Hayden M.R.;
RT   "Allele of Mus musculus Dream/calsenilin gene.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-14.
RC   STRAIN=BALB/c;
RA   Lee H.G., Choi J.K., Choi E.K., Wasco W., Buxbaum J.D., Beier D.R.,
RA   Kim Y.S.;
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain, Eye, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=20140134; PubMed=10676964; DOI=10.1038/35000592;
RA   An W.F., Bowlby M.R., Betty M., Cao J., Ling H.-P., Mendoza G.,
RA   Hinson J.W., Mattsson K.I., Strassle B.W., Trimmer J.S., Rhodes K.J.;
RT   "Modulation of A-type potassium channels by a family of calcium
RT   sensors.";
RL   Nature 403:553-556(2000).
RN   [7]
RP   INTERACTION WITH KCND3.
RX   MEDLINE=21481767; PubMed=11598014; DOI=10.1093/emboj/20.20.5715;
RA   Liss B., Franz O., Sewing S., Bruns R., Neuhoff H., Roeper J.;
RT   "Tuning pacemaker frequency of individual dopaminergic neurons by
RT   Kv4.3L and KChip3.1 transcription.";
RL   EMBO J. 20:5715-5724(2001).
RN   [8]
RP   FUNCTION.
RX   MEDLINE=21652533; PubMed=11792319; DOI=10.1016/S0092-8674(01)00629-8;
RA   Cheng H.Y., Pitcher G.M., Laviolette S.R., Whishaw I.Q., Tong K.I.,
RA   Kockeritz L.K., Wada T., Joza N.A., Crackower M., Goncalves J.,
RA   Sarosi I., Woodgett J.R., Oliveira-dos-Santos A.J., Ikura M.,
RA   van der Kooy D., Salter M.W., Penninger J.M.;
RT   "DREAM is a critical transcriptional repressor for pain modulation.";
RL   Cell 108:31-43(2002).
RN   [9]
RP   INTERACTION WITH KCND2.
RX   MEDLINE=22338839; PubMed=12451113;
RA   Schrader L.A., Anderson A.E., Mayne A., Pfaffinger P.J., Sweatt J.D.;
RT   "PKA modulation of Kv4.2-encoded A-type potassium channels requires
RT   formation of a supramolecular complex.";
RL   J. Neurosci. 22:10123-10133(2002).
RN   [10]
RP   TISSUE SPECIFICITY.
RX   PubMed=12646414; DOI=10.1152/ajpcell.00416.2002;
RA   Boland L.M., Jiang M., Lee S.Y., Fahrenkrug S.C., Harnett M.T.,
RA   O'Grady S.M.;
RT   "Functional properties of a brain-specific NH2-terminally spliced
RT   modulator of Kv4 channels.";
RL   Am. J. Physiol. 285:C161-C170(2003).
RN   [11]
RP   FUNCTION.
RX   MEDLINE=22896672; PubMed=14534243;
RA   Lilliehook C., Bozdagi O., Yao J., Gomez-Ramirez M., Zaidi N.F.,
RA   Wasco W., Gandy S., Santucci A.C., Haroutunian V., Huntley G.W.,
RA   Buxbaum J.D.;
RT   "Altered Abeta formation and long-term potentiation in a calsenilin
RT   knock-out.";
RL   J. Neurosci. 23:9097-9106(2003).
RN   [12]
RP   TISSUE SPECIFICITY.
RX   PubMed=15363885; DOI=10.1016/j.molbrainres.2004.06.024;
RA   Xiong H., Kovacs I., Zhang Z.;
RT   "Differential distribution of KChIPs mRNAs in adult mouse brain.";
RL   Brain Res. Mol. Brain Res. 128:103-111(2004).
RN   [13]
RP   DNA-BINDING, CALCIUM-BINDING, SUBUNIT, AND MUTAGENESIS OF GLU-186 AND
RP   GLU-234.
RX   PubMed=15746104; DOI=10.1074/jbc.M500338200;
RA   Osawa M., Dace A., Tong K.I., Valiveti A., Ikura M., Ames J.B.;
RT   "Mg2+ and Ca2+ differentially regulate DNA binding and dimerization of
RT   DREAM.";
RL   J. Biol. Chem. 280:18008-18014(2005).
RN   [14]
RP   STRUCTURE BY NMR, SUBUNIT, DNA BINDING, AND CALCIUM BINDING.
RX   PubMed=18201103; DOI=10.1021/bi7017267;
RA   Lusin J.D., Vanarotti M., Li C., Valiveti A., Ames J.B.;
RT   "NMR structure of DREAM: implications for Ca(2+)-dependent DNA binding
RT   and protein dimerization.";
RL   Biochemistry 47:2252-2264(2008).
CC   -!- FUNCTION: Calcium-dependent transcriptional repressor that binds
CC       to the DRE element of genes including PDYN and FOS. Affinity for
CC       DNA is reduced upon binding to calcium and enhanced by binding to
CC       magnesium. Seems to be involved in nociception.
CC   -!- FUNCTION: Regulatory subunit of Kv4/D (Shal)-type voltage-gated
CC       rapidly inactivating A-type potassium channels. Probably modulates
CC       channels density, inactivation kinetics and rate of recovery from
CC       inactivation in a calcium-dependent and isoform-specific manner.
CC       In vitro, modulates KCND2/Kv4.2 and KCND3/Kv4.3 currents. Involved
CC       in KCND2 and probably KCND3 trafficking to the cell surface (By
CC       similarity).
CC   -!- FUNCTION: May play a role in the regulation of PSEN2 proteolytic
CC       processing and apoptosis. Together with PSEN2 involved in
CC       modulation of beta-amyloid formation (By similarity).
CC   -!- SUBUNIT: Binds to DNA as a homomultimer. Dimerization is induced
CC       by binding to calcium. Interacts with the C-terminus of PSEN1 and
CC       PSEN2 and with PSEN2 CTF subunit. Associates with KCN1. Component
CC       of heteromultimeric potassium channels (By similarity). Interacts
CC       with KCND2 and KCND3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Lipid-anchor.
CC       Endoplasmic reticulum. Golgi apparatus. Nucleus (By similarity).
CC       Note=In the presence of PSEN2 associated with the endoplasmic
CC       reticulum and Golgi.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=Calsenilin/KChIP3 T+;
CC         IsoId=Q9QXT8-1; Sequence=Displayed;
CC       Name=2; Synonyms=Calsenilin/KChIP3 T-;
CC         IsoId=Q9QXT8-2; Sequence=VSP_015042;
CC         Note=Lacks EF-hand domains;
CC       Name=3; Synonyms=DREAM T-;
CC         IsoId=Q9QXT8-3; Sequence=VSP_015041;
CC       Name=4; Synonyms=DREAM T+;
CC         IsoId=P0C092-1; Sequence=External;
CC         Note=Lacks EF-hand domains;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain. Isoform 1 or
CC       isoform 4 (T+ forms) are expressed at equal levels with isoform 2
CC       or isoform 3 (T- forms). Primarily detected in the layer V and
CC       deep layer VI of the cerebral cortex, the hippocampus, and the
CC       entire cerebellum. Expressed at low levels in testis. Also
CC       expressed in heart.
CC   -!- PTM: Palmitoylated. Palmitoylation enhances association with the
CC       plasma membrane (By similarity).
CC   -!- PTM: Proteolytically cleaved by caspase-3 (By similarity).
CC   -!- MISCELLANEOUS: Mice deficient for Csen show a significant decrease
CC       of beta-amyloid protein 40 and beta-amyloid-protein 42, and
CC       display markedly reduced responses in models of acute thermal,
CC       mechanical, and visceral pain.
CC   -!- SIMILARITY: Belongs to the recoverin family.
CC   -!- SIMILARITY: Contains 4 EF-hand domains.
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DR   EMBL; AF287732; AAK08175.1; -; mRNA.
DR   EMBL; AF287733; AAK08180.1; -; mRNA.
DR   EMBL; AF287737; AAK08176.1; -; Genomic_DNA.
DR   EMBL; AF287734; AAK08176.1; JOINED; Genomic_DNA.
DR   EMBL; AF287735; AAK08176.1; JOINED; Genomic_DNA.
DR   EMBL; AF287736; AAK08176.1; JOINED; Genomic_DNA.
DR   EMBL; AF287737; AAK08177.1; -; Genomic_DNA.
DR   EMBL; AF287734; AAK08177.1; JOINED; Genomic_DNA.
DR   EMBL; AF287735; AAK08177.1; JOINED; Genomic_DNA.
DR   EMBL; AF287736; AAK08177.1; JOINED; Genomic_DNA.
DR   EMBL; AF287737; AAK08179.1; -; Genomic_DNA.
DR   EMBL; AF287734; AAK08179.1; JOINED; Genomic_DNA.
DR   EMBL; AF287735; AAK08179.1; JOINED; Genomic_DNA.
DR   EMBL; AF287736; AAK08179.1; JOINED; Genomic_DNA.
DR   EMBL; AF184624; AAF14576.1; -; mRNA.
DR   EMBL; AF274050; AAF74784.1; -; mRNA.
DR   EMBL; AF300870; AAG17450.1; -; mRNA.
DR   EMBL; BC026980; AAH26980.1; -; mRNA.
DR   EMBL; BC047139; AAH47139.1; -; mRNA.
DR   EMBL; BC057329; AAH57329.1; -; mRNA.
DR   IPI; IPI00135534; -.
DR   IPI; IPI00474630; -.
DR   IPI; IPI00475040; -.
DR   RefSeq; NP_001104801.1; NM_001111331.1.
DR   RefSeq; NP_062763.2; NM_019789.3.
DR   UniGene; Mm.315292; -.
DR   PDB; 2JUL; NMR; -; A=1-256.
DR   PDBsum; 2JUL; -.
DR   ProteinModelPortal; Q9QXT8; -.
DR   SMR; Q9QXT8; 76-256.
DR   DisProt; DP00291; -.
DR   STRING; Q9QXT8; -.
DR   PhosphoSite; Q9QXT8; -.
DR   PRIDE; Q9QXT8; -.
DR   Ensembl; ENSMUST00000028850; ENSMUSP00000028850; ENSMUSG00000079056.
DR   Ensembl; ENSMUST00000103215; ENSMUSP00000099504; ENSMUSG00000079056.
DR   GeneID; 56461; -.
DR   KEGG; mmu:56461; -.
DR   UCSC; uc008mfm.1; mouse.
DR   UCSC; uc008mfn.1; mouse.
DR   CTD; 56461; -.
DR   MGI; MGI:1929258; Kcnip3.
DR   GeneTree; ENSGT00560000076973; -.
DR   HOVERGEN; HBG108179; -.
DR   PhylomeDB; Q9QXT8; -.
DR   NextBio; 312710; -.
DR   ArrayExpress; Q9QXT8; -.
DR   Bgee; Q9QXT8; -.
DR   CleanEx; MM_KCNIP3; -.
DR   Genevestigator; Q9QXT8; -.
DR   GermOnline; ENSMUSG00000027376; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0048306; F:calcium-dependent protein binding; IPI:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:MGI.
DR   GO; GO:0016566; F:specific transcriptional repressor activity; IMP:MGI.
DR   GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0007610; P:behavior; IMP:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:MGI.
DR   GO; GO:0043523; P:regulation of neuron apoptosis; IDA:MGI.
DR   GO; GO:0048265; P:response to pain; IMP:MGI.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR018248; EF-hand.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR001125; Recoverin.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF00036; efhand; 1.
DR   PRINTS; PR00450; RECOVERIN.
DR   SMART; SM00054; EFh; 3.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Apoptosis; Calcium; Cell membrane;
KW   Cytoplasm; Endoplasmic reticulum; Golgi apparatus; Ion transport;
KW   Ionic channel; Lipoprotein; Membrane; Nucleus; Palmitate;
KW   Polymorphism; Potassium; Potassium channel; Potassium transport;
KW   Repeat; Repressor; Transcription; Transcription regulation; Transport;
KW   Voltage-gated channel.
FT   CHAIN         1    256       Calsenilin.
FT                                /FTId=PRO_0000073815.
FT   DOMAIN       67    123       EF-hand 1; degenerate.
FT   DOMAIN      126    161       EF-hand 2.
FT   DOMAIN      162    197       EF-hand 3.
FT   DOMAIN      210    245       EF-hand 4.
FT   CA_BIND     175    186       1.
FT   CA_BIND     223    234       2.
FT   REGION      243    256       Interaction with KCND2 (By similarity).
FT   LIPID        45     45       S-palmitoyl cysteine (By similarity).
FT   LIPID        46     46       S-palmitoyl cysteine (By similarity).
FT   VAR_SEQ       1     61       MQRTKEAVKASDGNLLGDPGRIPLSKRESIKWQRPRFTRQA
FT                                LMRCCLIKWILSSAAPQGSD -> MRQLPAGPSSLACSGCK
FT                                AGRLVTVPFSSRDAEDQGSREGIGWQPPGRSWAHTTEQEGK
FT                                HQVAKATVHPPGPDALLLNQVDPVQCCPTRL (in
FT                                isoform 3).
FT                                /FTId=VSP_015041.
FT   VAR_SEQ      61    256       DSSDSELELSTVRHQPEGLDQLQAQTKFTKKELQSLYRGFK
FT                                NECPTGLVDEDTFKLIYSQFFPQGDATTYAHFLFNAFDADG
FT                                NGAIHFEDFVVGLSILLRGTVHEKLKWAFNLYDINKDGCIT
FT                                KEEMLAIMKSIYDMMGRHTYPILREDAPLEHVERFFQKMDR
FT                                NQDGVVTIDEFLETCQKDENIMNSMQLFENVI -> AVTVN
FT                                WSYPRCAISQRAWTSYKLRPSSPRRSCSPFTEASRMSVPQA
FT                                WWMKTPSNSFIPSSSLREMPPPMHTSSSMPSMLMGTGPSTL
FT                                RTLWLGSPSCFEGRSMRSSSGPSISMTLTRMVASPRRRCWP
FT                                S (in isoform 2).
FT                                /FTId=VSP_015042.
FT   VARIANT      14     14       N -> S (in strain: 129/Ola, BALB/c and
FT                                FVB/NJ).
FT   MUTAGEN     186    186       E->Q: Abolishes calcium-binding.
FT   MUTAGEN     234    234       E->Q: Abolishes calcium-binding.
FT   CONFLICT    246    246       M -> T (in Ref. 2; AAF14576).
FT   HELIX        78     85
FT   HELIX        90    103
FT   STRAND      107    110
FT   HELIX       111    121
FT   HELIX       128    137
FT   STRAND      144    146
FT   HELIX       149    159
FT   HELIX       163    173
FT   STRAND      177    180
FT   HELIX       184    197
FT   HELIX       211    221
FT   HELIX       232    241
FT   HELIX       245    255
SQ   SEQUENCE   256 AA;  29463 MW;  0F43D5F239D6378C CRC64;
     MQRTKEAVKA SDGNLLGDPG RIPLSKRESI KWQRPRFTRQ ALMRCCLIKW ILSSAAPQGS
     DSSDSELELS TVRHQPEGLD QLQAQTKFTK KELQSLYRGF KNECPTGLVD EDTFKLIYSQ
     FFPQGDATTY AHFLFNAFDA DGNGAIHFED FVVGLSILLR GTVHEKLKWA FNLYDINKDG
     CITKEEMLAI MKSIYDMMGR HTYPILREDA PLEHVERFFQ KMDRNQDGVV TIDEFLETCQ
     KDENIMNSMQ LFENVI
//
ID   PCSK1_MOUSE             Reviewed;         258 AA.
AC   Q9QXV0; Q91W26;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=ProSAAS;
DE   AltName: Full=IA-4;
DE   AltName: Full=Proprotein convertase subtilisin/kexin type 1 inhibitor;
DE            Short=Proprotein convertase 1 inhibitor;
DE   AltName: Full=pro-SAAS;
DE   Contains:
DE     RecName: Full=KEP;
DE   Contains:
DE     RecName: Full=Big SAAS;
DE              Short=b-SAAS;
DE   Contains:
DE     RecName: Full=Little SAAS;
DE              Short=l-SAAS;
DE   Contains:
DE     RecName: Full=Big PEN-LEN;
DE              Short=b-PEN-LEN;
DE     AltName: Full=SAAS CT(1-49);
DE   Contains:
DE     RecName: Full=PEN;
DE   Contains:
DE     RecName: Full=PEN-20;
DE   Contains:
DE     RecName: Full=PEN-19;
DE   Contains:
DE     RecName: Full=Little LEN;
DE              Short=l-LEN;
DE   Contains:
DE     RecName: Full=Big LEN;
DE              Short=b-LEN;
DE     AltName: Full=SAAS CT(25-40);
DE   Flags: Precursor;
GN   Name=Pcsk1n;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PROTEOLYTIC PROCESSING (KEP; BIG
RP   SAAS; LITTLE SAAS; PEN AND LITTLE LEN), TISSUE SPECIFICITY,
RP   SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RX   MEDLINE=20098938; PubMed=10632593;
RA   Fricker L., McKinzie A.A., Sun J., Curran E., Qian Y., Yan L.,
RA   Patterson S.D., Courchesne P.L., Richards B., Levin N., Mzhavia N.,
RA   Devi L.A., Douglass J.;
RT   "Identification and characterization of proSAAS, a granin-like
RT   neuroendocrine peptide precursor that inhibits prohormone
RT   processing.";
RL   J. Neurosci. 20:639-648(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION OF PCSK1-INHIBITING HEXAPEPTIDE.
RX   PubMed=9756897; DOI=10.1074/jbc.273.41.26589;
RA   Apletalina E., Appel J., Lamango N.S., Houghten R.A., Lindberg I.;
RT   "Identification of inhibitors of prohormone convertases 1 and 2 using
RT   a peptide combinatorial library.";
RL   J. Biol. Chem. 273:26589-26595(1998).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=98292390; PubMed=9630436; DOI=10.1159/000054314;
RA   Donadel G., Marinos N., DeSilva M.G., Lu J., Notkins A.L., Lan M.S.;
RT   "Molecular cloning and characterization of a highly basic protein, IA-
RT   4, expressed in pancreatic islets and brain.";
RL   Neuroendocrinology 67:190-196(1998).
RN   [5]
RP   PROTEOLYTIC PROCESSING (LITTLE SAAS; PEN AND BIG LEN).
RX   PubMed=11094058; DOI=10.1074/jbc.M009067200;
RA   Mzhavia N., Berman Y., Che F.-Y., Fricker L.D., Devi L.A.;
RT   "ProSAAS processing in mouse brain and pituitary.";
RL   J. Biol. Chem. 276:6207-6213(2001).
RN   [6]
RP   TISSUE SPECIFICITY, AND PROTEOLYTIC PROCESSING.
RX   PubMed=11259501; DOI=10.1046/j.1471-4159.2001.00165.x;
RA   Sayah M., Fortenberry Y., Cameron A., Lindberg I.;
RT   "Tissue distribution and processing of proSAAS by proprotein
RT   convertases.";
RL   J. Neurochem. 76:1833-1841(2001).
RN   [7]
RP   FUNCTION, PROTEOLYTIC PROCESSING (BIG SAAS; LITTLE SAAS; BIG PEN-LEN;
RP   PEN; PEN-20; PEN-19 AND BIG LEN), AND SUBCELLULAR LOCATION.
RX   PubMed=11742530; DOI=10.1042/0264-6021:3610067;
RA   Mzhavia N., Qian Y., Feng Y., Che F.-Y., Devi L.A., Fricker L.D.;
RT   "Processing of proSAAS in neuroendocrine cell lines.";
RL   Biochem. J. 361:67-76(2002).
RN   [8]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=15018810; DOI=10.1016/S1567-133X(02)00002-9;
RA   Feng Y., Reznik S.E., Fricker L.D.;
RT   "ProSAAS and prohormone convertase 1 are broadly expressed during
RT   mouse development.";
RL   Gene Expr. Patterns 1:135-140(2002).
RN   [9]
RP   FUNCTION, PROTEOLYTIC PROCESSING (BIG PEN-LEN AND BIG LEN), AND
RP   MUTAGENESIS OF 241-LYS-ARG-242.
RX   PubMed=11719503; DOI=10.1074/jbc.M104531200;
RA   Fortenberry Y., Hwang J.R., Apletalina E.V., Lindberg I.;
RT   "Functional characterization of ProSAAS: similarities and differences
RT   with 7B2.";
RL   J. Biol. Chem. 277:5175-5186(2002).
RN   [10]
RP   TISSUE SPECIFICITY (PEN).
RX   PubMed=16631141; DOI=10.1016/j.brainres.2006.02.124;
RA   Chakraborty T.R., Tkalych O., Nanno D., Garcia A.L., Devi L.A.,
RA   Salton S.R.;
RT   "Quantification of VGF- and pro-SAAS-derived peptides in endocrine
RT   tissues and the brain, and their regulation by diet and cold stress.";
RL   Brain Res. 1089:21-32(2006).
CC   -!- FUNCTION: May function in the control of the neuroendocrine
CC       secretory pathway. Proposed be a specific endogenous inhibitor of
CC       PCSK1. ProSAAS and Big PEN-LEN, both containing the C-terminal
CC       inhibitory domain, but not the processed peptides reduce PCSK1
CC       activity in the endoplasmic reticulum and Golgi. It reduces the
CC       activity of the 87 kDa form but not the autocatalytically derived
CC       66 kDa form of PCSK1. Subsequent processing of proSAAS may
CC       eliminate the inhibition. Slows down convertase-mediated
CC       processing of proopiomelanocortin and proenkephalin. May control
CC       the intracellular timing of PCSK1 rather than its total level of
CC       activity. The function of the processed secreted peptides is not
CC       known.
CC   -!- SUBUNIT: Interacts via the C-terminal inhibitory domain with PCSK1
CC       66 kDa form (By similarity).
CC   -!- SUBCELLULAR LOCATION: Secreted. Golgi apparatus, trans-Golgi
CC       network.
CC   -!- TISSUE SPECIFICITY: Expressed in brain (mostly hypothalamus and
CC       pituitary) and gut. Expressed in trigeminal ganglia and
CC       neuroendocrine cell lines. PEN is expressed in pancreas, spinal
CC       cord and brain (most abundant in striatum, hippocampus, pons and
CC       medulla, and cortex) (at protein level).
CC   -!- DEVELOPMENTAL STAGE: Broadly expressed from E9 to E11, with some
CC       enrichment in neural tube-derived tissues. By E15, the expression
CC       is largely restricted to neuroendocrine tissues.
CC   -!- DOMAIN: ProSAAS(1-180) increases secretion of enzymatically
CC       inactive PCSK1.
CC   -!- DOMAIN: The C-terminal inhibitory domain is involved in inhibtion
CC       of PCSK1. It corresponds to the probable processing intermediate
CC       Big PEN-LEN, binds to PCSK1 in vitro and contains the hexapeptide
CC       L-L-R-V-K-R, which, as a synthetic peptide, is sufficient for
CC       PCSK1 inhibition.
CC   -!- PTM: Proteolytically cleaved in the Golgi. Little SAAS, PEN, PEN-
CC       20 and Big LEN are the major processed peptides in proSAAS-
CC       overexpressing AtT-20 pituitary corticotrophic cell line.
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DR   EMBL; AF181560; AAF22641.1; -; mRNA.
DR   EMBL; BC012263; AAH12263.1; -; mRNA.
DR   IPI; IPI00135604; -.
DR   RefSeq; NP_038920.2; NM_013892.3.
DR   UniGene; Mm.4881; -.
DR   ProteinModelPortal; Q9QXV0; -.
DR   STRING; Q9QXV0; -.
DR   MEROPS; I49.001; -.
DR   PRIDE; Q9QXV0; -.
DR   Ensembl; ENSMUST00000041096; ENSMUSP00000040342; ENSMUSG00000039278.
DR   GeneID; 30052; -.
DR   KEGG; mmu:30052; -.
DR   UCSC; uc009snf.1; mouse.
DR   CTD; 30052; -.
DR   MGI; MGI:1353431; Pcsk1n.
DR   eggNOG; roNOG17559; -.
DR   GeneTree; ENSGT00390000013488; -.
DR   HOGENOM; HBG282075; -.
DR   HOVERGEN; HBG080210; -.
DR   InParanoid; Q9QXV0; -.
DR   OMA; VYDDGPT; -.
DR   OrthoDB; EOG4VDQ0S; -.
DR   PhylomeDB; Q9QXV0; -.
DR   NextBio; 307162; -.
DR   ArrayExpress; Q9QXV0; -.
DR   Bgee; Q9QXV0; -.
DR   Genevestigator; Q9QXV0; -.
DR   GermOnline; ENSMUSG00000039278; Mus musculus.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0030141; C:stored secretory granule; IDA:MGI.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:MGI.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:MGI.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0016486; P:peptide hormone processing; IDA:MGI.
DR   GO; GO:0009409; P:response to cold; IDA:MGI.
DR   GO; GO:0002021; P:response to dietary excess; IDA:MGI.
DR   InterPro; IPR010832; ProSAAS.
DR   Pfam; PF07259; ProSAAS; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Golgi apparatus; Neuropeptide;
KW   Secreted; Signal.
FT   SIGNAL        1     33       Potential.
FT   CHAIN        34    258       ProSAAS.
FT                                /FTId=PRO_0000259681.
FT   PEPTIDE      34     59       Big SAAS.
FT                                /FTId=PRO_0000259683.
FT   PEPTIDE      34     40       KEP.
FT                                /FTId=PRO_0000259682.
FT   PEPTIDE      42     59       Little SAAS.
FT                                /FTId=PRO_0000259684.
FT   PEPTIDE     219    258       Big PEN-LEN.
FT                                /FTId=PRO_0000259685.
FT   PEPTIDE     219    240       PEN.
FT                                /FTId=PRO_0000259686.
FT   PEPTIDE     219    238       PEN-20.
FT                                /FTId=PRO_0000259687.
FT   PEPTIDE     219    237       PEN-19.
FT                                /FTId=PRO_0000259688.
FT   PEPTIDE     243    258       Big LEN.
FT                                /FTId=PRO_0000259690.
FT   PEPTIDE     243    252       Little LEN.
FT                                /FTId=PRO_0000259689.
FT   REGION       34    213       ProSAAS(1-180).
FT   REGION      219    258       C-terminal inhibitory domain; interacts
FT                                with PCSK1.
FT   MOTIF       237    242       Sufficient for inhibition of PCSK1.
FT   MUTAGEN     241    242       KR->SS: Abolishes inhibition of PCSK1.
FT   CONFLICT     83     83       L -> Q (in Ref. 1; AAF22641).
SQ   SEQUENCE   258 AA;  27270 MW;  4197C8B077A20A22 CRC64;
     MAGSPLLCGP RAGGVGILVL LLLGLLRLPP TLSARPVKEP RSLSAASAPL VETSTPLRLR
     RAVPRGEAAG AVQELARALA HLLEAERQER ARAEAQEAED QQARVLAQLL RAWGSPRASD
     PPLAPDDDPD APAAQLARAL LRARLDPAAL AAQLVPAPAA APRPRPPVYD DGPTGPDVED
     AGDETPDVDP ELLRYLLGRI LTGSSEPEAA PAPRRLRRSV DQDLGPEVPP ENVLGALLRV
     KRLENPSPQA PARRLLPP
//
ID   LAT2_MOUSE              Reviewed;         531 AA.
AC   Q9QXW9;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Large neutral amino acids transporter small subunit 2;
DE   AltName: Full=L-type amino acid transporter 2;
DE            Short=mLAT2;
DE   AltName: Full=Solute carrier family 7 member 8;
GN   Name=Slc7a8; Synonyms=Lat2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   MEDLINE=20044753; PubMed=10574970; DOI=10.1074/jbc.274.49.34948;
RA   Rossier G., Meier C., Bauch C., Summa V., Sordat B., Verrey F.,
RA   Kuehn L.C.;
RT   "LAT2, a new basolateral 4F2hc/CD98-associated amino acid transporter
RT   of kidney and intestine.";
RL   J. Biol. Chem. 274:34948-34954(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20079165; PubMed=10610726; DOI=10.1006/geno.1999.5978;
RA   Bassi M.T., Sperandeo M.P., Incerti B., Bulfone A., Pepe A.,
RA   Surace E.M., Gattuso C., de Grandi A., Buoninconti A., Riboni M.,
RA   Manzoni M., Andria G., Ballabio A., Borsani G., Sebastio G.;
RT   "SLC7A8, a gene mapping within the lysinuric protein intolerance
RT   critical region, encodes a new member of the glycoprotein-associated
RT   amino acid transporter family.";
RL   Genomics 62:297-303(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Sodium-independent, high-affinity transport of small and
CC       large neutral amino acids such as alanine, serine, threonine,
CC       cysteine, phenylalanine, tyrosine, leucine, arginine and
CC       tryptophan, when associated with SLC3A2/4F2hc. Acts as an amino
CC       acid exchanger. Has higher affinity for L-phenylalanine than LAT1
CC       but lower affinity for glutamine and serine. L-alanine is
CC       transported at physiological concentrations. Plays a role in
CC       basolateral (re)absorption of neutral amino acids. Involved in the
CC       uptake of methylmercury (MeHg) when administered as the L-cysteine
CC       or D,L-homocysteine complexes, and hence plays a role in metal ion
CC       homeostasis and toxicity. Involved in the cellular activity of
CC       small molecular weight nitrosothiols, via the stereoselective
CC       transport of L-nitrosocysteine (L-CNSO) across the transmembrane.
CC       Plays an essential role in the reabsorption of neutral amino acids
CC       from the epithelial cells to the bloodstream in the kidney.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=12.2 uM for L-phenylalanine;
CC         KM=48 uM for L-leucine;
CC         KM=167 uM for L-alanine;
CC         KM=275 uM for L-glutamine;
CC         KM=294 uM for L-histidine;
CC   -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid
CC       transport protein SLC3A2/4F2hc.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Basolateral cell
CC       membrane; Multi-pass membrane protein. Note=Localized to the
CC       cytoplasm when expressed alone (By similarity). When coexpressed
CC       with SLC3A2/4F2hc, is localized to the plasma membrane.
CC       Colocalized with SLC3A2/4F2hc at the basolateral membrane of
CC       kidney cortex proximal tubules and small intestine epithelia of
CC       the villi.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in kidney and small
CC       intestine. Moderately present in placenta, ovary and brain.
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8)
CC       family.
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DR   EMBL; AF171668; AAF20380.1; -; mRNA.
DR   EMBL; Y19022; CAB69072.1; -; mRNA.
DR   EMBL; BC059004; AAH59004.1; -; mRNA.
DR   IPI; IPI00135632; -.
DR   RefSeq; NP_058668.1; NM_016972.2.
DR   UniGene; Mm.276831; -.
DR   ProteinModelPortal; Q9QXW9; -.
DR   STRING; Q9QXW9; -.
DR   PRIDE; Q9QXW9; -.
DR   Ensembl; ENSMUST00000022787; ENSMUSP00000022787; ENSMUSG00000022180.
DR   GeneID; 50934; -.
DR   KEGG; mmu:50934; -.
DR   UCSC; uc007txa.1; mouse.
DR   CTD; 50934; -.
DR   MGI; MGI:1355323; Slc7a8.
DR   eggNOG; roNOG06118; -.
DR   GeneTree; ENSGT00600000084149; -.
DR   HOGENOM; HBG714539; -.
DR   HOVERGEN; HBG000476; -.
DR   InParanoid; Q9QXW9; -.
DR   OMA; VYVFANI; -.
DR   OrthoDB; EOG4V437M; -.
DR   PhylomeDB; Q9QXW9; -.
DR   NextBio; 307981; -.
DR   ArrayExpress; Q9QXW9; -.
DR   Bgee; Q9QXW9; -.
DR   CleanEx; MM_LAT2; -.
DR   Genevestigator; Q9QXW9; -.
DR   GermOnline; ENSMUSG00000022180; Mus musculus.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IDA:MGI.
DR   InterPro; IPR004841; AA-permease_dom.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   InterPro; IPR004760; L_AA_transporter.
DR   PANTHER; PTHR11785; AA/rel_permease1; 1.
DR   Pfam; PF00324; AA_permease; 1.
DR   PIRSF; PIRSF006060; AA_transporter; 1.
DR   TIGRFAMs; TIGR00911; 2A0308; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Cell membrane; Cytoplasm; Disulfide bond;
KW   Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    531       Large neutral amino acids transporter
FT                                small subunit 2.
FT                                /FTId=PRO_0000054274.
FT   TRANSMEM     39     59       Helical; (Potential).
FT   TRANSMEM     71     91       Helical; (Potential).
FT   TRANSMEM    112    132       Helical; (Potential).
FT   TRANSMEM    154    174       Helical; (Potential).
FT   TRANSMEM    188    208       Helical; (Potential).
FT   TRANSMEM    230    250       Helical; (Potential).
FT   TRANSMEM    267    287       Helical; (Potential).
FT   TRANSMEM    309    329       Helical; (Potential).
FT   TRANSMEM    361    381       Helical; (Potential).
FT   TRANSMEM    387    407       Helical; (Potential).
FT   TRANSMEM    421    441       Helical; (Potential).
FT   TRANSMEM    446    466       Helical; (Potential).
SQ   SEQUENCE   531 AA;  57873 MW;  AE9C3B42F3B24F8C CRC64;
     MEKGARQRNN TAKNHPGSDT SPEAEASSGG GGVALKKEIG LVSACGIIVG NIIGSGIFVS
     PKGVLENAGS VGLALIVWIV TGIITAVGAL CYAELGVTIP KSGGDYSYVK DIFGGLAGFL
     RLWIAVLVIY PTNQAVIALT FSNYVLQPLF PTCFPPESGL RLLAAICLLL LTWVNCSSVR
     WATRVQDIFT AGKLLALALI IIMGIVQICK GEFFWLEPKN AFENFQEPDI GLVALAFLQG
     SFAYGGWNFL NYVTEELVDP YKNLPRAIFI SIPLVTFVYV FANIAYVTAM SPQELLASNA
     VAVTFGEKLL GVMAWIMPIS VALSTFGGVN GSLFTSSRLF FAGAREGHLP SVLAMIHVKR
     CTPIPALLFT CLSTLLMLVT SDMYTLINYV GFINYLFYGV TVAGQIVLRW KKPDIPRPIK
     VSLLFPIIYL LFWAFLLIFS LWSEPVVCGI GLAIMLTGVP VYFLGVYWQH KPKCFNDFIK
     SLTLVSQKMC VVVYPQEGNS GAEETTDDLE EQHKPIFKPT PVKDPDSEEQ P
//
ID   EHD3_MOUSE              Reviewed;         535 AA.
AC   Q9QXY6; Q8K590;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=EH domain-containing protein 3;
GN   Name=Ehd3; Synonyms=Ehd2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Galperin E., Tulzinski S., Horowitz M.;
RT   "EHD2 - EH domain containing 2, homolog of the EHD1.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Park S.Y., Lee W.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 33-41; 125-162; 252-268; 270-280 AND 359-370, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   INTERACTION WITH PACSIN1, AND SUBCELLULAR LOCATION.
RX   PubMed=15930129; DOI=10.1091/mbc.E05-01-0076;
RA   Braun A., Pinyol R., Dahlhaus R., Koch D., Fonarev P., Grant B.D.,
RA   Kessels M.M., Qualmann B.;
RT   "EHD proteins associate with syndapin I and II and such interactions
RT   play a crucial role in endosomal recycling.";
RL   Mol. Biol. Cell 16:3642-3658(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Plays a role in endocytic transport (By similarity).
CC   -!- SUBUNIT: Homooligomer, and heterooligomer with EHD1, EHD2 and EHD4
CC       (By similarity). Interacts with PACSIN1.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Endosome membrane; Peripheral membrane protein
CC       (By similarity). Recycling endosome membrane; Peripheral membrane
CC       protein (By similarity).
CC   -!- DOMAIN: The EH domain interacts with Asn-Pro-Phe (NPF) motifs of
CC       target proteins (By similarity).
CC   -!- SIMILARITY: Contains 1 EF-hand domain.
CC   -!- SIMILARITY: Contains 1 EH domain.
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DR   EMBL; AF155883; AAF19020.1; -; mRNA.
DR   EMBL; AF506002; AAM28633.1; -; mRNA.
DR   EMBL; AK141265; BAE24623.1; -; mRNA.
DR   EMBL; BC046596; AAH46596.1; -; mRNA.
DR   IPI; IPI00135677; -.
DR   RefSeq; NP_065603.2; NM_020578.3.
DR   UniGene; Mm.18526; -.
DR   ProteinModelPortal; Q9QXY6; -.
DR   SMR; Q9QXY6; 19-532.
DR   STRING; Q9QXY6; -.
DR   PhosphoSite; Q9QXY6; -.
DR   PRIDE; Q9QXY6; -.
DR   Ensembl; ENSMUST00000024860; ENSMUSP00000024860; ENSMUSG00000024065.
DR   GeneID; 57440; -.
DR   KEGG; mmu:57440; -.
DR   UCSC; uc008dnn.1; mouse.
DR   CTD; 57440; -.
DR   MGI; MGI:1928900; Ehd3.
DR   eggNOG; roNOG08616; -.
DR   GeneTree; ENSGT00600000084243; -.
DR   HOGENOM; HBG317590; -.
DR   HOVERGEN; HBG018183; -.
DR   InParanoid; Q9QXY6; -.
DR   OMA; KVWKLAD; -.
DR   OrthoDB; EOG418BN4; -.
DR   NextBio; 313833; -.
DR   ArrayExpress; Q9QXY6; -.
DR   Bgee; Q9QXY6; -.
DR   CleanEx; MM_EHD2; -.
DR   CleanEx; MM_EHD3; -.
DR   Genevestigator; Q9QXY6; -.
DR   GermOnline; ENSMUSG00000024065; Mus musculus.
DR   GO; GO:0030139; C:endocytic vesicle; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR001401; Dynamin_GTPase.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR000261; EPS15_homology.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   SMART; SM00027; EH; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS50031; EH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Calcium; Cell membrane; Coiled coil;
KW   Direct protein sequencing; Endosome; Membrane; Nucleotide-binding;
KW   Phosphoprotein.
FT   CHAIN         1    535       EH domain-containing protein 3.
FT                                /FTId=PRO_0000146113.
FT   DOMAIN      444    532       EH.
FT   DOMAIN      476    511       EF-hand.
FT   NP_BIND      65     72       ATP (By similarity).
FT   CA_BIND     489    500       By similarity.
FT   COILED      198    227       Potential.
FT   BINDING     220    220       ATP (By similarity).
FT   BINDING     258    258       ATP (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     456    456       Phosphoserine.
FT   CONFLICT    358    358       R -> K (in Ref. 1; AAF19020).
FT   CONFLICT    529    529       S -> Y (in Ref. 1; AAF19020).
SQ   SEQUENCE   535 AA;  60821 MW;  80BF1F3B45CB87DF CRC64;
     MFSWLGNDDR RKKDPEVFQT VSDGLKKLYK TKLLPLEEYY RFHEFHSPAL EDADFDNKPM
     VLLVGQYSTG KTTFIRYLLE QDFPGMRIGP EPTTDSFIAV MQGDVEGIIP GNALVVDPKK
     PFRKLNAFGN AFLNRFVCAQ LPNAVLESIS VIDTPGILSG EKQRISRGYD FAAVLEWFAE
     RVDRIILLFD AHKLDISDEF SEVIKALKNH EDKMRVVLNK ADQIETQQLM RVYGALMWSL
     GKIVNTPEVI RVYIGSFWSH PLLIPDNRKL FEAEEQDLFR DIQSLPRNAA LRKLNDLIKR
     ARLAKVHAYI ISSLKKEMPS VFGKDTKKKE LVNNLAEIYG RIEREHQISP GDFPNLKRMQ
     DQLQAQDFSK FQPLKSKLLE VVDDMLAHDI AQLMVLVRQE ETQRPVQMVK GGAFEGTLQG
     PFGHGYGEGA GEGIDDAEWV VARDKPMYDE IFYTLSPVDG KITGANAKKE MVRSKLPNSV
     LGKIWKLADI DKDGMLDDEE FALANHLIKV KLEGHELPSE LPAHLLPPSK RKVSE
//
ID   ULK2_MOUSE              Reviewed;        1037 AA.
AC   Q9QY01; Q80TV7; Q9WTP4;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Serine/threonine-protein kinase ULK2;
DE            EC=2.7.11.1;
DE   AltName: Full=Serine/threonine-protein kinase Unc51.2;
DE   AltName: Full=Unc-51-like kinase 2;
GN   Name=Ulk2; Synonyms=Kiaa0623;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   MEDLINE=20088285; PubMed=10624947; DOI=10.1016/S0896-6273(00)81031-4;
RA   Tomoda T., Bhatt R.S., Kuroyanagi H., Shirasawa T., Hatten M.E.;
RT   "A mouse serine/threonine kinase homologous to C. elegans UNC51
RT   functions in parallel fiber formation of cerebellar granule neurons.";
RL   Neuron 24:833-846(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND
RP   AUTOPHOSPHORYLATION.
RX   MEDLINE=20027371; PubMed=10557072; DOI=10.1038/sj.onc.1202988;
RA   Yan J., Kuroyanagi H., Tomemori T., Okazaki N., Asato K., Matsuda Y.,
RA   Suzuki Y., Ohshima Y., Mitani S., Masuho Y., Shirasawa T.,
RA   Muramatsu M.;
RT   "Mouse ULK2, a novel member of the UNC-51-like protein kinases: unique
RT   features of functional domains.";
RL   Oncogene 18:5850-5859(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts (via C-terminus) with ATG13/KIAA0652 (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- PTM: Autophosphorylated.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. APG1/unc-51/ULK1 subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65613.2; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF145922; AAF18325.1; -; mRNA.
DR   EMBL; AB019577; BAA77341.1; -; mRNA.
DR   EMBL; AK146620; BAE27309.1; -; mRNA.
DR   EMBL; AK122331; BAC65613.2; ALT_INIT; mRNA.
DR   EMBL; BC046778; AAH46778.1; -; mRNA.
DR   EMBL; BC053029; AAH53029.1; -; mRNA.
DR   IPI; IPI00336256; -.
DR   RefSeq; NP_038909.3; NM_013881.4.
DR   UniGene; Mm.162025; -.
DR   ProteinModelPortal; Q9QY01; -.
DR   SMR; Q9QY01; 3-276.
DR   STRING; Q9QY01; -.
DR   PhosphoSite; Q9QY01; -.
DR   PRIDE; Q9QY01; -.
DR   Ensembl; ENSMUST00000004920; ENSMUSP00000004920; ENSMUSG00000004798.
DR   GeneID; 29869; -.
DR   KEGG; mmu:29869; -.
DR   CTD; 29869; -.
DR   MGI; MGI:1352758; Ulk2.
DR   GeneTree; ENSGT00570000078909; -.
DR   HOGENOM; HBG446996; -.
DR   HOVERGEN; HBG000342; -.
DR   InParanoid; Q9QY01; -.
DR   OMA; LMPSIPR; -.
DR   OrthoDB; EOG4F1X2B; -.
DR   PhylomeDB; Q9QY01; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 307094; -.
DR   ArrayExpress; Q9QY01; -.
DR   Bgee; Q9QY01; -.
DR   CleanEx; MM_ULK2; -.
DR   Genevestigator; Q9QY01; -.
DR   GermOnline; ENSMUSG00000004798; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0048675; P:axon extension; IMP:MGI.
DR   GO; GO:0048671; P:negative regulation of collateral sprouting; IMP:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR022708; Ser/Thr_kinase_C.
DR   InterPro; IPR016237; Ser/Thr_prot_kin_STPK_Ulk-1/2.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF12063; DUF3543; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF000580; Ser/Thr_PK_STPK_ULK-1/2; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1   1037       Serine/threonine-protein kinase ULK2.
FT                                /FTId=PRO_0000086783.
FT   DOMAIN        9    271       Protein kinase.
FT   NP_BIND      15     23       ATP (By similarity).
FT   ACT_SITE    131    131       Proton acceptor (By similarity).
FT   BINDING      39     39       ATP (By similarity).
FT   CONFLICT    998    998       L -> V (in Ref. 2; BAA77341).
SQ   SEQUENCE   1037 AA;  112877 MW;  2E7DC3B0B87E9607 CRC64;
     MEVVGDFEYC KRDLVGHGAF AVVFRGRHRQ KTDWEVAIKS INKKNLSKSQ ILLGKEIKIL
     KELQHENIVA LYDVQELPNS VFLVMEYCNG GDLADYLQAK GTLSEDTIRV FLHQIAAAMR
     ILHSKGIIHR DLKPQNILLS YANRRKSNVS GIRIKIADFG FARYLHSNTM AATLCGSPMY
     MAPEVIMSQH YDAKADLWSI GTVIYQCLVG KPPFQANSPQ DLRMFYEKNR SLMPSIPRET
     SPYLANLLLG LLQRNQKDRM DFEAFFSHPF LEQVPVKKSC PVPVPVYSGP VPGSSCSSSP
     SCRFASPPSL PDMQHIQEEN LSSPPLGPPN YLQVSKDSAS NSSKNSSCDT DDFVLVPHNI
     SSDHSYDMPM GTTARRASNE FFMCGGQCQP TVSPHSETAP IPVPTQVRNY QRIEQNLIST
     ASSGTNPHGS PRSAVVRRSN TSPMGFLRVG SCSPVPGDTV QTGGRRLSTG SSRPYSPSPL
     VGTIPEQFSQ CCCGHPQGHE ARSRHSSGSP VPQTQAPQSL LLGARLQSAP TLTDIYQNKQ
     KLRKQHSDPV CPSHAGAGYS YSPQPSRPGS LGTSPTKHTG SSPRNSDWFF KTPLPTIIGS
     PTKTTAPFKI PKTQASSNLL ALVTRHGPAE SQSKDGNDPR ECSHCLSVQG SERHRSEQQQ
     SKAVFGRSVS TGKLSEQQVK APLGGHQGST DSLNTERPMD VAPAGACGVM LALPAGTAAS
     ARAVLFTVGS PPHSATAPTC THMVLRTRTT SVGSSSSGGS LCSASGRVCV GSPPGPGLGS
     SPPGAEGAPS LRYVPYGASP PSLEGLITFE APELPEETLM EREHTDTLRH LNMMLMFTEC
     VLDLTAVRGG NPELCTSAVS LYQIQESVVV DQISQLSKDW GRVEQLVLYM KAAQLLAASL
     HLAKAQVKSG KLSPSMAVKQ VVKNLNERYK FCITMCKKLT EKLNRFFSDK QRFIDEINSV
     TAEKLIYNCA VEMVQSAALD EMFQQTEDIV YRYHKAALLL EGLSKILQDP TDVENVHKYK
     CSIERRLSAL CCSTATV
//
ID   MYO9B_MOUSE             Reviewed;        2114 AA.
AC   Q9QY06; Q9QY07; Q9QY08; Q9QY09;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 2.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Myosin-IXb;
DE   AltName: Full=Unconventional myosin-9b;
GN   Name=Myo9b; Synonyms=Myr5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING, AND
RP   VARIANTS.
RC   STRAIN=C57BL/6;
RX   MEDLINE=20047919; PubMed=10580159; DOI=10.1016/S0378-1119(99)00459-X;
RA   Grewal P.K., Jones A.-M., Maconochie M., Lemmers R.J.F., Frants R.R.,
RA   Hewitt J.E.;
RT   "Cloning of the murine unconventional myosin gene Myo9b and
RT   identification of alternative splicing.";
RL   Gene 240:389-398(1999).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1319 AND SER-1949, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1175 AND SER-1325, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1175, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1218, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Myosins are actin-based motor molecules with ATPase
CC       activity. Unconventional myosins serve in intracellular movements.
CC       May be involved in the remodeling of the actin cytoskeleton. Binds
CC       actin with high affinity both in the absence and presence of ATP
CC       and its mechanochemical activity is inhibited by calcium ions.
CC       Also acts as a GTPase activating protein on Rho.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex (By similarity).
CC       Cytoplasm, perinuclear region (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity). Note=In undifferentiated cells
CC       colocalizes with F-actin in the cell periphery while in
CC       differentiated cells its localization is cytoplasmic with the
CC       highest levels in the perinuclear region (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9QY06-1; Sequence=Displayed;
CC       Name=2; Synonyms=Q;
CC         IsoId=Q9QY06-2; Sequence=VSP_003363;
CC       Name=3; Synonyms=C;
CC         IsoId=Q9QY06-3; Sequence=VSP_003364, VSP_003365;
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, heart, muscle and
CC       inner ear.
CC   -!- SIMILARITY: Contains 4 IQ domains.
CC   -!- SIMILARITY: Contains 1 myosin head-like domain.
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC   -!- SIMILARITY: Contains 1 Ras-associating domain.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
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DR   EMBL; AF143687; AAF00122.1; -; Genomic_DNA.
DR   EMBL; AF143685; AAF00120.1; -; mRNA.
DR   EMBL; AF143686; AAF00121.1; ALT_FRAME; mRNA.
DR   EMBL; AF143683; AAF00118.1; -; mRNA.
DR   IPI; IPI00135379; -.
DR   IPI; IPI00229766; -.
DR   IPI; IPI00319697; -.
DR   UniGene; Mm.33779; -.
DR   ProteinModelPortal; Q9QY06; -.
DR   SMR; Q9QY06; 16-113, 141-981, 1585-1640, 1648-1842.
DR   STRING; Q9QY06; -.
DR   PhosphoSite; Q9QY06; -.
DR   PRIDE; Q9QY06; -.
DR   Ensembl; ENSMUST00000071935; ENSMUSP00000071827; ENSMUSG00000004677.
DR   Ensembl; ENSMUST00000098648; ENSMUSP00000096245; ENSMUSG00000004677.
DR   UCSC; uc009mck.1; mouse.
DR   MGI; MGI:106624; Myo9b.
DR   GeneTree; ENSGT00600000084203; -.
DR   HOVERGEN; HBG052558; -.
DR   OrthoDB; EOG408N75; -.
DR   PhylomeDB; Q9QY06; -.
DR   ArrayExpress; Q9QY06; -.
DR   Bgee; Q9QY06; -.
DR   CleanEx; MM_MYO9B; -.
DR   Genevestigator; Q9QY06; -.
DR   GermOnline; ENSMUSG00000004677; Mus musculus.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000159; Ras-assoc.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF00612; IQ; 4.
DR   Pfam; PF00063; Myosin_head; 1.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00015; IQ; 4.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00314; RA; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50096; IQ; 3.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding;
KW   Coiled coil; Cytoplasm; Cytoskeleton; GTPase activation;
KW   Metal-binding; Motor protein; Myosin; Nucleotide-binding;
KW   Phosphoprotein; Polymorphism; Repeat; Zinc; Zinc-finger.
FT   CHAIN         1   2114       Myosin-IXb.
FT                                /FTId=PRO_0000123470.
FT   DOMAIN        1    939       Myosin head-like.
FT   DOMAIN       15    114       Ras-associating.
FT   DOMAIN      957    977       IQ 1.
FT   DOMAIN      979   1000       IQ 2.
FT   DOMAIN     1001   1023       IQ 3.
FT   DOMAIN     1024   1053       IQ 4.
FT   DOMAIN     1661   1846       Rho-GAP.
FT   NP_BIND     239    246       ATP (Potential).
FT   ZN_FING    1590   1639       Phorbol-ester/DAG-type.
FT   REGION      844    855       Actin-binding.
FT   REGION      940   1044       Neck or regulatory domain.
FT   REGION     1045   2114       Tail.
FT   COILED     1562   1592       Potential.
FT   COILED     1839   1859       Potential.
FT   COILED     1915   1945       Potential.
FT   MOD_RES     716    716       Phosphoserine (By similarity).
FT   MOD_RES    1175   1175       Phosphoserine.
FT   MOD_RES    1218   1218       Phosphoserine.
FT   MOD_RES    1241   1241       Phosphoserine (By similarity).
FT   MOD_RES    1264   1264       Phosphoserine (By similarity).
FT   MOD_RES    1317   1317       Phosphothreonine (By similarity).
FT   MOD_RES    1319   1319       Phosphothreonine.
FT   MOD_RES    1325   1325       Phosphoserine.
FT   MOD_RES    1371   1371       Phosphoserine (By similarity).
FT   MOD_RES    1949   1949       Phosphoserine.
FT   VAR_SEQ     740    740       R -> RCTGLDFSFERSEELDVNAFEDIMAFYESR (in
FT                                isoform 2).
FT                                /FTId=VSP_003363.
FT   VAR_SEQ    1875   1890       Missing (in isoform 3).
FT                                /FTId=VSP_003364.
FT   VAR_SEQ    1977   2114       GPPAPALPCPISPTLSPLPEAAAPPRGRPTSFVTVRVKTPR
FT                                RTPIMPMANIKLPPGLPLHLTSWAPALQEAVVPVKRREPPA
FT                                RRQDQVHSVYIAPGADLPSQSTLIALDHDTILPGTKRRYSD
FT                                PPTYCLPPSSGQANG -> E (in isoform 3).
FT                                /FTId=VSP_003365.
FT   VARIANT    1243   1243       L -> LEVSPVLPSSSL (only in strain C57BL/
FT                                6; contains an in-frame 33 bp imperfect
FT                                duplication).
FT   VARIANT    2083   2083       A -> P.
SQ   SEQUENCE   2114 AA;  238834 MW;  D774D4B1B2788045 CRC64;
     MSAHEAGSSG RRQQATYHLH IYPQLSSAGS QTSCRVTATK DSTTSDVIQD VVASLHLDGS
     KHYVLVEVKE SGGEEWVLDA SDSPVHRVLL WPRRAQDEHP QEDGYYFLLQ ERNADGSIQY
     LPIQLLAQPT AACRLVERGL LPRPQADFDD LCNLPELTEA NLLQNLKLRF MQQKIYTYAG
     SILVAINPFK FLPIYNPKYV KMYENQQLGK LEPHVFALAD VAYYAMLRKH VNQCIVISGE
     SGSGKTQSTN FLIHCLTALS QKGYASGVER TILGAGPVLE AFGNAKTAHN NNSSRFGKFI
     QVNYLENGIV RGAVVEKYLL EKSRLVSQEK DERNYHVFYY LLLGVSEEER LEFQLKQPQD
     YFYLNQHNLN IEDGEDLKHD FERLQQAMEM VGFLPATKKQ IFSVLSAILY LGNVTYKKRA
     TGRDEGLEVG PPEVLDTLSQ LLKVKRETLV EVLTKRKTVT VNDKLILPYS LSEAITARDS
     MAKSLYSALF DWIVLRINHA LLNKKDMEEA VSCLSIGVLD IFGFEDFERN SFEQFCINYA
     NEQLQYYFTQ HIFKLEQEEY QGEGISWHNI DYTDNVGCIH LISKKPTGLF YLLDEESNFP
     HATSHTLLAK FKQQHEDNKY FLGTPVLEPA FIIQHFAGRV KYQIKDFREK NMDYMRPDIV
     ALLRGSDSSY VRQLIGMDPV AVFRWAVLRA AIRAMAVLRE AGRLRAERAE KAAGISSPAT
     RSHMEELPRG ASTPSEKLYR DLHNQIIKSL KGLPWQGEDP RRLLQSLSLL QKPRTSFLKS
     KGIKQKQIIP KNLLDSKSLR LIISMTLHDR TTKSLLHLHK KKKPPSISAQ FQTSLNKLLE
     ALGKAEPFFI RCIRSNAEKK ELCFDDELVL QQLRYTGMLE TVRIRRSGYS AKYTFQDFTE
     QFQVLLPKDV QPCREAIAAL LEKLQVDRQN YQIGKTKVFL KETERQTLQE KLHGEVLRRI
     LQLQSWFRMV LERKHFVQMK HAALTIQACW RSYRVRRALE RTQAAVYLQA AWRGYLQRQA
     YHHQRHSIIR LQSLCRGHLQ RRSFSQMVSE KQKAEQAREA AGGKLSEGEP GPVAAGEQLS
     EHPVEDPESL GVEAETWMNK SPDGMSPKKE TPSPEMETAA QKTVPAESHE KVSSSREKRE
     SRRQRGLEHV ERQNKHIQSC REESSTHREP SRRASLEIGE SFPEGTKGPR EDGLEAWTET
     TAPSSSKQAQ VVGDPPGSPS PVQRPTTLAL DSRVSPMLPS SSLESPKDKD KDESSTKAQD
     KPESPSGSTQ IQRYQHPDTE RLATAVEIWR GKKLASAVLS QSLDLSEKHR ATGAALTPTE
     ERRISFSTSD ISKLSPVKTS AEIDGDFSSK KPSIHKKKSG DPSAGPDAGL SPGSQGDSKS
     AFKRLFLHKA KDKKPSLEGV EETESNGGQA AQETPARKTL DVPSSQQHRH TTGEKPLKGK
     KNRNRKVGQI TVSEKWRESV FRKITNANEL KFLDEFLLNK VNDLRSQKTP IESLFIEATE
     RFRSNIKTMY SVPNGKIHVG YKDLMENYQI VVSNLAAERG EKDTNLVLNV FQSLLDEFTR
     SYNKTDFERA KSKAQKKKRK QERAVQEHNG HVFASYQVNI PQSCEQCLSY IWLMDKALLC
     SVCKMTCHKK CVHKIQSYCS YTGRRKSELG AEPGHFGVCV DSLTSDKASV PIVLEKLLEH
     VEMHGLYTEG LYRKSGAANR TRELRQALQT DPAAVKLEDF PIHAITGVLK QWLRELPEPL
     MTFAQYGDFL RAVELPEKQE QLSAIYAVLD HLPEANHTSL ERLIFHLVKV ALLEDVNRMS
     PGALAIIFAP CLLRCPDNSD PLTSMKDVLK ITTCVEMLIK EQMRKYKMKM EEINHLEAAE
     SIAFRRLSLL RQNAPWPLKL GFSSPYEGVR IKSPRTPVVQ DLELGALSEE AAGGDEDREK
     EILMERIQSI KEEKEDITYR LPELDPRGSD EENLDSETSA STESLLEERG VRGAVEGPPA
     PALPCPISPT LSPLPEAAAP PRGRPTSFVT VRVKTPRRTP IMPMANIKLP PGLPLHLTSW
     APALQEAVVP VKRREPPARR QDQVHSVYIA PGADLPSQST LIALDHDTIL PGTKRRYSDP
     PTYCLPPSSG QANG
//
ID   PKP3_MOUSE              Reviewed;         797 AA.
AC   Q9QY23; A4QPD8; Q0VGP3; Q3KQL7;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 2.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Plakophilin-3;
GN   Name=Pkp3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=99310799; PubMed=10381383;
RA   Bonne S., van Hengel J., Nollet F., Kools P., van Roy F.;
RT   "Plakophilin-3, a novel armadillo-like protein present in nuclei and
RT   desmosomes of epithelial cells.";
RL   J. Cell Sci. 112:2265-2276(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Colon, and Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May play a role in junctional plaques.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cell junction, desmosome.
CC       Note=Nuclear and associated with desmosomes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9QY23-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9QY23-2; Sequence=VSP_026139;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the beta-catenin family.
CC   -!- SIMILARITY: Contains 8 ARM repeats.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF136719; AAD55892.1; -; mRNA.
DR   EMBL; BC090668; AAH90668.1; -; mRNA.
DR   EMBL; BC106141; AAI06142.1; -; mRNA.
DR   EMBL; BC139775; AAI39776.1; -; mRNA.
DR   IPI; IPI00135464; -.
DR   IPI; IPI00850034; -.
DR   RefSeq; NP_001156396.1; NM_001162924.1.
DR   RefSeq; NP_062736.2; NM_019762.2.
DR   UniGene; Mm.350037; -.
DR   ProteinModelPortal; Q9QY23; -.
DR   SMR; Q9QY23; 319-784.
DR   STRING; Q9QY23; -.
DR   PhosphoSite; Q9QY23; -.
DR   PRIDE; Q9QY23; -.
DR   Ensembl; ENSMUST00000066873; ENSMUSP00000069961; ENSMUSG00000054065.
DR   Ensembl; ENSMUST00000106039; ENSMUSP00000101654; ENSMUSG00000054065.
DR   GeneID; 56460; -.
DR   KEGG; mmu:56460; -.
DR   NMPDR; fig|10090.3.peg.17916; -.
DR   UCSC; uc009kji.1; mouse.
DR   CTD; 56460; -.
DR   MGI; MGI:1891830; Pkp3.
DR   eggNOG; roNOG11208; -.
DR   GeneTree; ENSGT00550000074290; -.
DR   HOVERGEN; HBG106682; -.
DR   OMA; VSEQLEP; -.
DR   OrthoDB; EOG4C5CHV; -.
DR   PhylomeDB; Q9QY23; -.
DR   NextBio; 312706; -.
DR   ArrayExpress; Q9QY23; -.
DR   Bgee; Q9QY23; -.
DR   CleanEx; MM_PKP3; -.
DR   Genevestigator; Q9QY23; -.
DR   GermOnline; ENSMUSG00000054065; Mus musculus.
DR   GO; GO:0030057; C:desmosome; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF00514; Arm; 1.
DR   SMART; SM00185; ARM; 3.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Cell junction; Nucleus;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1    797       Plakophilin-3.
FT                                /FTId=PRO_0000064288.
FT   REPEAT      305    348       ARM 1.
FT   REPEAT      351    390       ARM 2.
FT   REPEAT      393    432       ARM 3.
FT   REPEAT      449    487       ARM 4.
FT   REPEAT      491    536       ARM 5.
FT   REPEAT      596    637       ARM 6.
FT   REPEAT      645    684       ARM 7.
FT   REPEAT      689    730       ARM 8.
FT   MOD_RES      66     66       Phosphoserine.
FT   MOD_RES      84     84       Phosphotyrosine (By similarity).
FT   MOD_RES     115    115       Phosphoserine (By similarity).
FT   MOD_RES     176    176       Phosphotyrosine (By similarity).
FT   MOD_RES     180    180       Phosphoserine (By similarity).
FT   MOD_RES     195    195       Phosphotyrosine (By similarity).
FT   MOD_RES     240    240       Phosphoserine (By similarity).
FT   MOD_RES     313    313       Phosphoserine.
FT   MOD_RES     314    314       Phosphoserine (By similarity).
FT   MOD_RES     390    390       Phosphotyrosine (By similarity).
FT   VAR_SEQ       1     12       MQEGNFLLSALQ -> MEPTAGSRTRMEPRRNCPTAGTSRM
FT                                SQGASGGQTSGK (in isoform 2).
FT                                /FTId=VSP_026139.
FT   CONFLICT    182    182       R -> P (in Ref. 1; AAD55892).
FT   CONFLICT    216    216       E -> K (in Ref. 1; AAD55892).
FT   CONFLICT    459    459       A -> P (in Ref. 1; AAD55892).
SQ   SEQUENCE   797 AA;  87333 MW;  C2ECF73BDE7323B1 CRC64;
     MQEGNFLLSA LQPETGVCSL ALPSDLQLDR RGAEGPEADR LRAARVQEQV RARLLQLGQQ
     SRHNGSAELD GSAESARGMP RGQYHTMQTG FSSRSQGMSG DKTSTFRPIA KPAYSPASWS
     SRSAVDLTCS RRLSSAHNGG SAFGAVGYGG TQPTPPMPTR PVSFHERGGA ASRADYDTLS
     LRSLRLGPGG LDDRYSVVSE QLEPAAASTY RAYAYERQAS SGSSRAGGLD WPEATEGPPS
     RTIRAPAMRT LQRFQSSHRS RGGTGSVSGA GLEPVARAPS VRSLSLSLAD SGHLPDVRGL
     DSYTGHRTLQ RLSSGFDDID LPSAVKYLMA SDPNLQVLGA AYIQHRCYSD AAAKKQARSL
     QAVPRLVKLF NHANQEVQRH ATGAMRNLIY DNVDNKLALV EENGIFELLR TLREQDDELR
     KNVTGILWNL SSSDHLKDRL ARDTLEQLTD LVLSPLSGAG GPPLIQQNAS EAEIFYNATG
     FLRNLSSASQ ATRQKMRECH GLVDALVTYI NHALDVGKCE DKSVENAVCV LRNLSYRLYD
     EMPPSALQRL EGRGRRDMAG APPGEMVGCF TPQSRRLREL PLTADALTFA EVSKDPKGLE
     WLWSPQIVGL YNRLLQRCEL NRHTTEAAAG ALQNITAGDR RWAGVLSRLA LEQERILNPL
     LDRVRTADHN QLRSLTGLIR NLSRNARNKD EMSTKVVSHL IEKLPGSVGE KCPPAEVLVN
     IIAVLNNLVV ASPIAARDLL YFDGLRKLVF IKKKRDSPDS EKSSRAASSL LANLWQYSKL
     HRDFRAKGYR KEDFLGP
//
ID   PDZD4_MOUSE             Reviewed;         772 AA.
AC   Q9QY39; A2AFG4; Q6PHP2;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=PDZ domain-containing protein 4;
DE   AltName: Full=PDZ domain-containing RING finger protein 4-like protein;
GN   Name=Pdzd4; Synonyms=Pdzk4, Pdzrn4l, Xlu;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Platzer M., Brenner V., Reichwald K., Wiehe T., Oksche A.,
RA   Rosenthal A.;
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-772.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex (By similarity).
CC       Note=Mainly localized under the plasma membrane (By similarity).
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH56462.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF133093; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL672094; CAM22462.1; -; Genomic_DNA.
DR   EMBL; BC056462; AAH56462.1; ALT_INIT; mRNA.
DR   IPI; IPI00380160; -.
DR   RefSeq; NP_001025039.1; NM_001029868.1.
DR   UniGene; Mm.103782; -.
DR   ProteinModelPortal; Q9QY39; -.
DR   SMR; Q9QY39; 15-54, 137-232.
DR   STRING; Q9QY39; -.
DR   PhosphoSite; Q9QY39; -.
DR   PRIDE; Q9QY39; -.
DR   Ensembl; ENSMUST00000002080; ENSMUSP00000002080; ENSMUSG00000002006.
DR   GeneID; 245469; -.
DR   KEGG; mmu:245469; -.
DR   UCSC; uc009tmt.1; mouse.
DR   CTD; 245469; -.
DR   MGI; MGI:2443483; Pdzd4.
DR   GeneTree; ENSGT00510000046421; -.
DR   HOGENOM; HBG445469; -.
DR   HOVERGEN; HBG053554; -.
DR   InParanoid; Q9QY39; -.
DR   OMA; RERCMKA; -.
DR   OrthoDB; EOG441Q9Z; -.
DR   PhylomeDB; Q9QY39; -.
DR   NextBio; 386719; -.
DR   ArrayExpress; Q9QY39; -.
DR   Bgee; Q9QY39; -.
DR   CleanEx; MM_PDZD4; -.
DR   Genevestigator; Q9QY39; -.
DR   GermOnline; ENSMUSG00000002006; Mus musculus.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm.
FT   CHAIN         1    772       PDZ domain-containing protein 4.
FT                                /FTId=PRO_0000055922.
FT   DOMAIN      136    221       PDZ.
FT   COILED      394    424       Potential.
SQ   SEQUENCE   772 AA;  86819 MW;  1D5A1BA6A6900713 CRC64;
     MGCNMCVVQK PEEQYKVMLQ VNGKELSKLS QEQTLEALRA SKEPLVIQVL RRSPRLRGDS
     SCHDLQLVDS GTQTDITFEH IMALGKLRPP TPPMGILEPY VLSELPPISH EYYDPAEFME
     GGPQEAERMD ELEYEEVELC KNSHQDKLGL MVCYRTDEEE DLGIYVGEVN PNSIAAKDGR
     IREGDRIIQI NGMDVQNREE AVAILSQEEN TNISLLVARP ESQLAKRWKD SDRDDFLDDF
     GSENEGDLRA RKLKSPPVQQ IGNDEKGAPD GGPGLNNSQD LDSGVGRTDE STRNEESSEH
     DLLGDEPPST TNTPGSLRKF GLQGDALQSR DFHFSMDSLL AEGAGLGGAD LPGLTDEEYE
     RYRELLEIKC HLENGNQLGI FFSRASSGNS ALDVNRNESL GHEMAMLEEE LRHLEFKCRN
     ILRAQKMQQL RERCMKAWLL EEESLYDLAA SEPKKHELSD ISELPEKSDK DSTSAYNTGE
     SCRSTPLLVE PLPESPLKRS GAGNSNLNRT PSGPPVTTHL KGAPSPGSPA KFRSLSRDPE
     VGRRQHTEER VRRSTKTSVT LERVGPEGSP YLSRRHRGQE IEQYHSCVQL APPRTLEDLG
     HGSLSLASGP RVGGVAAAAV EAPRMEWKVK VRSDGTRYVA KRPVRDRLLK ARALKIREER
     SGMTTDDDAV SEMKMGRYWS KEERKQHLIR AREQRKRREF MMQSRLECLR EQQNGDSKPE
     LNIIALSHRK TMKKRNKKIL DNWITIQEML AHGARSADGK RIYNPLLSVT TV
//
ID   TMM59_MOUSE             Reviewed;         323 AA.
AC   Q9QY73; Q3TWB4; Q99LY8; Q9D1P9;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Transmembrane protein 59;
DE   AltName: Full=Thymic dendritic cell-derived factor 1;
DE   Flags: Precursor;
GN   Name=Tmem59; Synonyms=ORF18, Tdcf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Thymus;
RA   Jin C.G., Chen W.F.;
RT   "Isolation and molecular cloning of gene encoding a novel dendritic
RT   cell-derived factor.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N;
RC   TISSUE=Colon, Eye, Kidney, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 316-323, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: Modulates the O-glycosylation and complex N-
CC       glycosylation steps occurring during the Golgi maturation of
CC       several proteins such as APP, BACE1, SEAP or PRNP. Inhibits APP
CC       transport to the cell surface and further shedding (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane (By similarity);
CC       Single-pass type I membrane protein.
CC   -!- PTM: N-glycosylated (By similarity).
CC   -!- SIMILARITY: Belongs to the TMEM59 family.
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DR   EMBL; AF116911; AAF20283.1; -; mRNA.
DR   EMBL; AK003252; BAB22668.2; -; mRNA.
DR   EMBL; AK050162; BAC34103.1; -; mRNA.
DR   EMBL; AK145644; BAE26561.1; -; mRNA.
DR   EMBL; AK159761; BAE35352.1; -; mRNA.
DR   EMBL; AK166772; BAE39008.1; -; mRNA.
DR   EMBL; AK167058; BAE39221.1; -; mRNA.
DR   EMBL; BC002164; AAH02164.1; -; mRNA.
DR   EMBL; BC014732; AAH14732.1; -; mRNA.
DR   EMBL; BC018379; AAH18379.1; -; mRNA.
DR   EMBL; BC045145; AAH45145.1; -; mRNA.
DR   EMBL; BC058273; AAH58273.1; -; mRNA.
DR   IPI; IPI00135648; -.
DR   RefSeq; NP_083841.4; NM_029565.3.
DR   UniGene; Mm.291192; -.
DR   ProteinModelPortal; Q9QY73; -.
DR   STRING; Q9QY73; -.
DR   PRIDE; Q9QY73; -.
DR   Ensembl; ENSMUST00000030361; ENSMUSP00000030361; ENSMUSG00000028618.
DR   GeneID; 56374; -.
DR   KEGG; mmu:56374; -.
DR   UCSC; uc008tzj.1; mouse.
DR   CTD; 56374; -.
DR   MGI; MGI:1929278; Tmem59.
DR   eggNOG; roNOG12942; -.
DR   GeneTree; ENSGT00390000008279; -.
DR   HOGENOM; HBG445912; -.
DR   HOVERGEN; HBG018206; -.
DR   InParanoid; Q9QY73; -.
DR   OMA; YGDLEFM; -.
DR   OrthoDB; EOG4NGGN4; -.
DR   PhylomeDB; Q9QY73; -.
DR   NextBio; 312436; -.
DR   ArrayExpress; Q9QY73; -.
DR   Bgee; Q9QY73; -.
DR   CleanEx; MM_TMEM59; -.
DR   Genevestigator; Q9QY73; -.
DR   GermOnline; ENSMUSG00000028618; Mus musculus.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR022065; Uncharacterised_TMEM59.
DR   Pfam; PF12280; BSMAP; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Golgi apparatus; Membrane;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     35       Potential.
FT   CHAIN        36    323       Transmembrane protein 59.
FT                                /FTId=PRO_0000003004.
FT   TOPO_DOM     36    238       Extracellular (Potential).
FT   TRANSMEM    239    259       Helical; (Potential).
FT   TOPO_DOM    260    323       Cytoplasmic (Potential).
FT   CARBOHYD     90     90       N-linked (GlcNAc...) (Potential).
FT   CONFLICT     48     48       C -> V (in Ref. 1; AAF20283).
FT   CONFLICT    103    103       A -> T (in Ref. 1; AAF20283).
FT   CONFLICT    121    121       L -> W (in Ref. 1; AAF20283).
FT   CONFLICT    139    139       H -> Q (in Ref. 1; AAF20283).
FT   CONFLICT    221    222       YL -> DR (in Ref. 1; AAF20283).
FT   CONFLICT    248    248       L -> F (in Ref. 3; AAH45145).
FT   CONFLICT    264    264       A -> G (in Ref. 1; AAF20283).
FT   CONFLICT    277    300       YGDLEFMNEQKLSRYPAPSLVIVR -> IGHFQFINQQNLT
FT                                TYPPPPLLIVK (in Ref. 1; AAF20283).
SQ   SEQUENCE   323 AA;  36314 MW;  0E9BF6B6E07C7D96 CRC64;
     MAAPKGKLWV QAQLGLPPLL LLTMALAGGS GTAAAEAFDS VLGDTASCHR ACQLTYPLHT
     YPKEEELYAC QRGCRLFSIC QFVDDGLDLN RTKLECESAC TEAYSQPDEQ YACHLGCQDQ
     LPFAELRQEQ LMSLMPRMHL LFPLTLVRSF WSDMMDSAQS FITSSWTFYL QADDGKIVIF
     QSKPEIQYAP QLEQEPTNLR ESSLSKMSYL QMRNSQAHRN YLEEEESDGF LRCLSLNSGW
     ILTTTLVLSV MVLLWICCAA VATAVEQYVP PEKLSIYGDL EFMNEQKLSR YPAPSLVIVR
     SQTEEHEEAG PLPTKVNLAH SEI
//
ID   VAPB_MOUSE              Reviewed;         243 AA.
AC   Q9QY76;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Vesicle-associated membrane protein-associated protein B;
DE            Short=VAMP-B;
DE            Short=VAMP-associated protein B;
DE            Short=VAP-B;
DE   AltName: Full=VAMP-associated protein 33b;
GN   Name=Vapb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Tang B.L., Low D.L.H., Lock M.L., Hong W.;
RT   "Two forms of mammalian VAP33.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in vesicle trafficking.
CC   -!- SUBUNIT: Homodimer, and heterodimer with VAPA. Interacts with
CC       VAMP1 and VAMP2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type IV membrane
CC       protein (By similarity). Endomembrane system; Single-pass type IV
CC       membrane protein (By similarity). Note=Present in the plasma
CC       membrane and in intracellular vesicles (By similarity).
CC   -!- SIMILARITY: Belongs to the VAMP-associated protein (VAP)
CC       (TC 9.B.17) family.
CC   -!- SIMILARITY: Contains 1 MSP domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF115504; AAF23077.1; -; mRNA.
DR   IPI; IPI00135655; -.
DR   UniGene; Mm.260456; -.
DR   ProteinModelPortal; Q9QY76; -.
DR   SMR; Q9QY76; 1-125.
DR   STRING; Q9QY76; -.
DR   PhosphoSite; Q9QY76; -.
DR   PRIDE; Q9QY76; -.
DR   Ensembl; ENSMUST00000067530; ENSMUSP00000064699; ENSMUSG00000054455.
DR   MGI; MGI:1928744; Vapb.
DR   GeneTree; ENSGT00390000006947; -.
DR   HOGENOM; HBG446464; -.
DR   HOVERGEN; HBG028551; -.
DR   InParanoid; Q9QY76; -.
DR   OrthoDB; EOG4DNF5D; -.
DR   PhylomeDB; Q9QY76; -.
DR   ArrayExpress; Q9QY76; -.
DR   Bgee; Q9QY76; -.
DR   Genevestigator; Q9QY76; -.
DR   GermOnline; ENSMUSG00000054455; Mus musculus.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005624; C:membrane fraction; IDA:HGNC.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR000535; Major_sperm.
DR   InterPro; IPR008962; PapD-like.
DR   InterPro; IPR016763; Vesicle-associated_membrane.
DR   Gene3D; G3DSA:2.60.40.360; MSP; 1.
DR   Pfam; PF00635; Motile_Sperm; 1.
DR   PIRSF; PIRSF019693; VAMP-associated; 1.
DR   SUPFAM; SSF49354; PapD-like; 1.
DR   PROSITE; PS50202; MSP; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell membrane; Coiled coil; Membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    243       Vesicle-associated membrane protein-
FT                                associated protein B.
FT                                /FTId=PRO_0000213474.
FT   TOPO_DOM      2    218       Cytoplasmic (Potential).
FT   TRANSMEM    219    239       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   DOMAIN        7    124       MSP.
FT   COILED      161    196       Potential.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       3      3       N6-acetyllysine (By similarity).
FT   MOD_RES     156    156       Phosphoserine (By similarity).
FT   MOD_RES     159    159       Phosphoserine (By similarity).
FT   MOD_RES     206    206       Phosphoserine (By similarity).
SQ   SEQUENCE   243 AA;  26946 MW;  9D88CBC31701C84E CRC64;
     MAKVEQVLSL EPQHELKFRG PFTDVVTTNL KLGNPTDRNV CFKVKTTVPR RYCVRPNSGV
     IDAGASLNVS VMLQPFDYDP NEKSKHKFMV QSMFAPPDTS DMEAVWKEAK PEDLMDSKLR
     CVFELPAENA KPHDVEINKI IPTSASKTEA PAAAKSLTSP LDDTEVKKVM EECRRLQGEV
     QRLREESRQL KEEDGLRVRK AMPSNSPVAA LAATGKEEGL SARLLALVVL FFIVGVIIGK
     IAL
//
ID   PO210_MOUSE             Reviewed;        1886 AA.
AC   Q9QY81; Q3U031; Q69ZW2; Q7TQM1;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 2.
DT   08-FEB-2011, entry version 61.
DE   RecName: Full=Nuclear pore membrane glycoprotein 210;
DE            Short=Nuclear pore protein gp210;
DE   AltName: Full=Nuclear envelope pore membrane protein POM 210;
DE            Short=POM210;
DE   AltName: Full=Nucleoporin Nup210;
DE   AltName: Full=Pore membrane protein of 210 kDa;
DE   Flags: Precursor;
GN   Name=Nup210; Synonyms=Kiaa0906;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=NMRI; TISSUE=Kidney;
RX   MEDLINE=99398513; PubMed=10469352;
RX   DOI=10.1046/j.1523-1755.1999.00618.x;
RA   Olsson M., Ekblom M., Fecker L., Kurkinen M., Ekblom P.;
RT   "cDNA cloning and embryonic expression of mouse nuclear pore membrane
RT   glycoprotein 210 mRNA.";
RL   Kidney Int. 56:827-838(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-1886.
RC   TISSUE=Thymus;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1160.
RC   TISSUE=Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1844, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Nucleoporin essential for nuclear pore assembly and
CC       fusion, nuclear pore spacing, as well as structural integrity.
CC   -!- SUBUNIT: Forms dimers and possibly higher-order oligomers (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex (By
CC       similarity). Nucleus membrane; Single-pass type I membrane protein
CC       (By similarity). Endoplasmic reticulum membrane; Single-pass type
CC       I membrane protein (By similarity).
CC   -!- DEVELOPMENTAL STAGE: Preferential expressed in epithelial cells.
CC       In the kidney, expression was seen in both the epithelium derived
CC       from the ureteric tree and the mesenchyme-derived epithelium. In
CC       other tissues of 13-day-old embryos, expression was also confined
CC       to the epithelium. In nervous tissues, mainly expressed in the
CC       olfactory epithelium and walls of the lateral ventricle. Weak
CC       expression was seen in the heart.
CC   -!- PTM: N-glycosylated, but not all potential glycosylation sites may
CC       be used. Contains high-mannose type oligosaccharides (By
CC       similarity).
CC   -!- PTM: Phosphorylated at Ser-1880 in mitosis specifically; not
CC       phosphorylated in interphase (By similarity).
CC   -!- SIMILARITY: Belongs to the NUP210 family.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF113751; AAF21969.1; -; mRNA.
DR   EMBL; BC052468; AAH52468.1; -; mRNA.
DR   EMBL; AK173056; BAD32334.1; -; mRNA.
DR   EMBL; AK157272; BAE34024.1; -; mRNA.
DR   IPI; IPI00342158; -.
DR   RefSeq; NP_061285.2; NM_018815.2.
DR   UniGene; Mm.28162; -.
DR   ProteinModelPortal; Q9QY81; -.
DR   SMR; Q9QY81; 471-538, 1080-1142, 1324-1355.
DR   STRING; Q9QY81; -.
DR   PhosphoSite; Q9QY81; -.
DR   PRIDE; Q9QY81; -.
DR   Ensembl; ENSMUST00000032179; ENSMUSP00000032179; ENSMUSG00000030091.
DR   GeneID; 54563; -.
DR   KEGG; mmu:54563; -.
DR   UCSC; uc009cxu.1; mouse.
DR   CTD; 54563; -.
DR   MGI; MGI:1859555; Nup210.
DR   eggNOG; roNOG09646; -.
DR   GeneTree; ENSGT00390000009491; -.
DR   HOGENOM; HBG716176; -.
DR   HOVERGEN; HBG082098; -.
DR   InParanoid; Q9QY81; -.
DR   OMA; DSHNALR; -.
DR   NextBio; 311384; -.
DR   ArrayExpress; Q9QY81; -.
DR   Bgee; Q9QY81; -.
DR   CleanEx; MM_NUP210; -.
DR   Genevestigator; Q9QY81; -.
DR   GermOnline; ENSMUSG00000030091; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:UniProtKB-KW.
DR   InterPro; IPR003343; Big_2.
DR   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   Pfam; PF02368; Big_2; 1.
DR   SMART; SM00635; BID_2; 1.
DR   SUPFAM; SSF49373; Invasin_intimin; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycoprotein; Membrane; mRNA transport;
KW   Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW   Signal; Translocation; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL        1     26       By similarity.
FT   CHAIN        27   1886       Nuclear pore membrane glycoprotein 210.
FT                                /FTId=PRO_0000236047.
FT   TOPO_DOM     27   1808       Lumenal (Probable).
FT   TRANSMEM   1809   1829       Helical; (Potential).
FT   TOPO_DOM   1830   1886       Cytoplasmic (Probable).
FT   COMPBIAS    486    492       Poly-Ser.
FT   MOD_RES    1844   1844       Phosphothreonine.
FT   MOD_RES    1873   1873       Phosphoserine (By similarity).
FT   MOD_RES    1876   1876       Phosphoserine (By similarity).
FT   MOD_RES    1880   1880       Phosphoserine (By similarity).
FT   MOD_RES    1885   1885       Phosphoserine (By similarity).
FT   CARBOHYD     44     44       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    337    337       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    405    405       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    484    484       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    681    681       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    801    801       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    926    926       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1039   1039       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1116   1116       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1135   1135       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1362   1362       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1441   1441       N-linked (GlcNAc...) (Potential).
FT   CONFLICT     14     14       L -> V (in Ref. 1; AAF21969).
FT   CONFLICT     37     37       F -> G (in Ref. 1; AAF21969).
FT   CONFLICT    107    108       LR -> VA (in Ref. 1; AAF21969).
FT   CONFLICT    420    420       A -> S (in Ref. 1; AAF21969).
FT   CONFLICT    425    425       L -> F (in Ref. 4; BAE34024).
FT   CONFLICT    512    513       SV -> RE (in Ref. 1; AAF21969).
FT   CONFLICT    517    518       HD -> QH (in Ref. 1; AAF21969).
FT   CONFLICT    597    597       R -> K (in Ref. 1; AAF21969).
FT   CONFLICT    719    762       Missing (in Ref. 2).
FT   CONFLICT    808    808       Q -> E (in Ref. 4; BAE34024).
FT   CONFLICT    812    814       SRP -> FPR (in Ref. 1; AAF21969).
FT   CONFLICT    904    904       I -> V (in Ref. 4; BAE34024).
FT   CONFLICT    969    969       A -> T (in Ref. 4; BAE34024).
FT   CONFLICT    974    975       HV -> QL (in Ref. 1; AAF21969).
FT   CONFLICT   1020   1021       KL -> NW (in Ref. 1; AAF21969).
FT   CONFLICT   1049   1049       V -> C (in Ref. 1; AAF21969).
FT   CONFLICT   1256   1256       V -> L (in Ref. 1; AAF21969).
SQ   SEQUENCE   1886 AA;  204101 MW;  8732FBAA46096862 CRC64;
     MARASLVQPA LWALLLLQVV GPAAAAKLNI PKVLLPFTRA TRVNFTLEAS EGCYRWSSTR
     PEVASIEPLG SSEQQCSQKA VVQARLTQPA RLTSIIFAED ITTGQVLRCD AIVDLIHGIQ
     IVSTTRELYL EDSPLELKIQ ALDSEGNTFS TLAGLVFDWT IVKDTEANGF SDSHNALRIL
     TFLESTYIPP SYISEMEKAA KQGDTILVSG MKTGSSKLKA RIQEAVYKNV RPAEVRLLIL
     ENILLNPAYD VYLLVGTSIH YKVQKIRQGK ITELSMPSDQ YELQLQNSIP DPQGDPARPV
     AILTQDTSRV TAMQMGQSNL VLGHRSIRMQ GASRLPNSTI YVVEAGYLGF TVYPGDRWVL
     ETGHLYAITI EVFDRSSNKV YPSDNIRIEA VLPAEFFEVL SSSQNGSYHH IRAIQSGQTA
     ISATLTSVVD QDGGVHVLQV PVWNQQEVDI HIPITLYPSI LTFPWQPKTG AYQYTIKAHG
     GSGNFSWSSS SSMVATVTVK GVMTTSGDTG LSVIRAHDVQ NPLHFGEMKV YVIEPSSMEF
     APCQVEARVG HTLELPLTIS GFMPGGGSEV VTLSDCSHFD LVVEVENQGV FQPLPGRLPP
     GPEHCSGVKV KADAQGSTTL LVSYTHGHVH LDAKITLAAY LPLKAVDPSS VAVVTLGSSK
     EMLFEGGPRP WVLEPSKFFR NVTSEDTGSI SLSLLGPPAS RNYQQHRVLM TCQALGEQVI
     ALSVGNRPSL SNPFPAVEPT VVKSICAPPS RLTLMPVYAL PQLDLSCPLL QQNKQVVPVS
     SHRNPLLDLG AYDQQGRRFD NFSSLSIQWE SSRPLLASIE LDQPMQLVSQ DDGNGQKKLH
     GLQTVSVHEA SGTTAISATA TGYQQSHLSE ARVKQPHDPL VPVSASIELI LVEDVRVSPE
     EMTIYNHPGV QVELYITEGS GYFFLNTSTQ DIIKVAYQDT RGVALVHPLL PGSSTVMVHD
     LCLAFPAPAK AIIHVSDIQE LYVRVVDKVE IGKAVKAYVR VLDFYKKPFL AKYFTFMDLK
     LQAASQIITL VTLDEALDNY TATFLVHGVA IGQTSLSASV TDKSGQRVSS TPQQIEVFPP
     FRLIPRKVTL IIGAMMQITS EGGPQPQSNI LFSINNESVA AVSSSGLVRG LMVGNGSVLG
     VVQAVDAETG KVIIVSQDLV EVEVLQLQAV RIRAPITRMR TGTQMPVFVT GITSNQSPFS
     FGNAVPGLTF HWSVTKRDVL DLRGRHHEVS IRLPPQYNFA MNVYGRVKGR TGLRVVVKAL
     DPTAGQLHGL GKELSDEIQI QVFEKLRLLN PEIEAEQILM SPNSFIKLQT NRDGAAILSY
     RVLDGPEKAP IVHTDEKGFL VSGSGIGVST LEVIAQEPFG TNQTILVAVK VSPVSYLRIS
     MSPVLHTQHK EALTALPLGM TVTFIVHFHD SSGDIFHAHN SVLNFATNRD DFVQIGKGAT
     NNTCIIRTVS VGLTLLHVWD VEHLGLSDFV PLPVLQAITP ELSGAVVVGD ILCLASVLTS
     LGGVSGTWSS SASHVLYVDP KTGVAIARDA GSVTVYYEIA GQLKTFKEIV VGTPQKIVAR
     RLHSAQTSIQ EATASKVTVS VGDRSSNLLG ECSPAQREAI EALHPESLIS CQLQFKQDVF
     DFPACDVFTV EPGFDAALGQ YLCSVTMRRL TDKQLKHLNM KKTSLAVTAS IPSSYTSVEK
     VGAEVPFSPG LYANQAEILL SNHYTSSEVK VFGAVESLEN LEVKSGSPAV LAFVKEKSFG
     LPSFITYTVG VLDPTAGSQG PLSTALTFSS PATNQAITIP VTVAFVLDRR GPGPYGASLL
     SHFLDSYQVM FFTFFALLAG TAVTIIAYHT VCAPRELASP LALTPRASPQ HSPHYLASSP
     AAFNTLPSGR KASPPSGLWS PAYASH
//
ID   TOM40_MOUSE             Reviewed;         361 AA.
AC   Q9QYA2; Q3TBZ2; Q3TQA1; Q8VI26; Q8VI27; Q9Z2N1;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 3.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Mitochondrial import receptor subunit TOM40 homolog;
DE   AltName: Full=Mitochondrial outer membrane protein of 35 kDa;
DE            Short=MOM35;
DE   AltName: Full=Protein Haymaker;
DE   AltName: Full=Translocase of outer membrane 40 kDa subunit homolog;
GN   Name=Tomm40; Synonyms=Mom35, Tom40;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=21619280; PubMed=11768756; DOI=10.1023/A:1005524815130;
RA   Lee Rivera I., Shore G.C., Schleiff E.;
RT   "Cloning and characterization of a 35-kDa mouse mitochondrial outer
RT   membrane protein MOM35 with high homology to Tom40.";
RL   J. Bioenerg. Biomembr. 32:111-121(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Mastocytoma;
RX   MEDLINE=21610875; PubMed=11745481; DOI=10.1002/ijc.1555;
RA   Das B., Tao S.-Z., Mushnitsky R., Norin A.J.;
RT   "Genetic identity and differential expression of p38.5 (Haymaker) in
RT   human malignant and non-malignant cells.";
RL   Int. J. Cancer 94:800-806(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Yoshiura K., Murray J.C.;
RT   "A transcriptional map in the region of 19q13 derived using direct
RT   sequencing and exon trapping.";
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Corpus striatum, Dendritic cell, Lung, and Macrophage;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 185-195; 316-330 AND 352-361, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: Channel-forming protein essential for import of protein
CC       precursors into mitochondria (By similarity).
CC   -!- SUBUNIT: Forms part of the preprotein translocase complex of the
CC       outer mitochondrial membrane (TOM complex) which consists of at
CC       least 7 different proteins (TOMM5, TOMM6, TOMM7, TOMM20, TOMM22,
CC       TOMM40 and TOMM70). Interacts with mitochondrial targeting
CC       sequences (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the Tom40 family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC82341.1; Type=Frameshift; Positions=34, 43;
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DR   EMBL; AF109918; AAF21906.1; -; mRNA.
DR   EMBL; AF316403; AAL46628.1; -; mRNA.
DR   EMBL; AF316404; AAL46629.1; -; mRNA.
DR   EMBL; AF043249; AAC82341.1; ALT_FRAME; mRNA.
DR   EMBL; AK150019; BAE29244.1; -; mRNA.
DR   EMBL; AK163759; BAE37483.1; -; mRNA.
DR   EMBL; AK164570; BAE37837.1; -; mRNA.
DR   EMBL; AK165173; BAE38058.1; -; mRNA.
DR   EMBL; AK170991; BAE42165.1; -; mRNA.
DR   EMBL; BC100452; AAI00453.1; -; mRNA.
DR   IPI; IPI00474157; -.
DR   RefSeq; NP_001103218.1; NM_001109748.1.
DR   RefSeq; NP_058567.2; NM_016871.2.
DR   UniGene; Mm.416870; -.
DR   UniGene; Mm.440173; -.
DR   ProteinModelPortal; Q9QYA2; -.
DR   PRIDE; Q9QYA2; -.
DR   Ensembl; ENSMUST00000093552; ENSMUSP00000104090; ENSMUSG00000002984.
DR   GeneID; 53333; -.
DR   KEGG; mmu:53333; -.
DR   CTD; 53333; -.
DR   MGI; MGI:1858259; Tomm40.
DR   eggNOG; roNOG10829; -.
DR   GeneTree; ENSGT00390000003308; -.
DR   HOGENOM; HBG446491; -.
DR   HOVERGEN; HBG054707; -.
DR   InParanoid; Q9QYA2; -.
DR   OMA; CGCLPNP; -.
DR   OrthoDB; EOG40K80F; -.
DR   PhylomeDB; Q9QYA2; -.
DR   NextBio; 310161; -.
DR   ArrayExpress; Q9QYA2; -.
DR   Bgee; Q9QYA2; -.
DR   Genevestigator; Q9QYA2; -.
DR   GermOnline; ENSMUSG00000002984; Mus musculus.
DR   GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR   GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR   GO; GO:0008308; F:voltage-gated anion channel activity; IEA:InterPro.
DR   GO; GO:0006626; P:protein targeting to mitochondrion; ISS:UniProtKB.
DR   InterPro; IPR001925; Porin_Euk.
DR   Pfam; PF01459; Porin_3; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Ion transport; Membrane; Mitochondrion;
KW   Mitochondrion outer membrane; Porin; Protein transport; Transmembrane;
KW   Transmembrane beta strand; Transport.
FT   CHAIN         1    361       Mitochondrial import receptor subunit
FT                                TOM40 homolog.
FT                                /FTId=PRO_0000051524.
FT   COMPBIAS     10     39       Pro-rich.
FT   CONFLICT      1     78       MGNVLAASSPPAGPPPPPTPSLVGLPPPPPSPPGFTLPPLG
FT                                GGLGTGSSTGRGSERTPGAAASGAAAASEDGSCGCLP ->
FT                                MMKSGDWVKHWPWFGTDSRGCGQRRCGGLGRWELRMPA
FT                                (in Ref. 1; AAF21906).
FT   CONFLICT     13     14       GP -> R (in Ref. 3; AAC82341).
FT   CONFLICT     70     70       E -> D (in Ref. 4; BAE42165).
FT   CONFLICT    126    126       E -> G (in Ref. 3; AAL46628).
FT   CONFLICT    185    234       Missing (in Ref. 3; AAC82341).
SQ   SEQUENCE   361 AA;  37895 MW;  8415114963EBAB9B CRC64;
     MGNVLAASSP PAGPPPPPTP SLVGLPPPPP SPPGFTLPPL GGGLGTGSST GRGSERTPGA
     AASGAAAASE DGSCGCLPNP GTFEECHRKC KELFPVQMEG VKLTVNKGLS NRFQVTHTVA
     LGTIGESNYH FGVTYVGTKQ LSPTEAFPVL VGDMDNSGSL NAQVIHQLSP GLRSKMAIQT
     QQSKFVNWQV DGEYRGSDFT AAVTLGNPDV LVGSGILVAH YLQSITPCLA LGGELVYHRR
     PGEEGTVMSL AGKYTLNNWL ATVTLGQAGM HATYYHKASD QLQVGVEFEA STRMQDTSAS
     FGYQLDLPKA NFLFKGSVNS NWIVGATLEK KLPPLPLTLS LCAFLNHRKN KFLCGFGLTI
     G
//
ID   ADDG_MOUSE              Reviewed;         706 AA.
AC   Q9QYB5; Q9D2M5; Q9QYB6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Gamma-adducin;
DE   AltName: Full=Adducin-like protein 70;
GN   Name=Add3; Synonyms=Addl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20069066; PubMed=10602987; DOI=10.1007/s003350010004;
RA   Suriyapperuma S.P., Lozovatsky L., Ciciotte S.L., Peters L.L.,
RA   Gilligan D.M.;
RT   "The mouse adducin gene family: alternative splicing and chromosomal
RT   localization.";
RL   Mamm. Genome 11:16-23(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-673 AND SER-681, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402; SER-677 AND
RP   SER-681, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-681, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Membrane-cytoskeleton-associated protein that promotes
CC       the assembly of the spectrin-actin network. Binds to calmodulin.
CC   -!- SUBUNIT: Heterodimer of an alpha and a gamma subunit.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane;
CC       Peripheral membrane protein; Cytoplasmic side.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist;
CC       Name=2; Synonyms=Long;
CC         IsoId=Q9QYB5-1; Sequence=Displayed;
CC       Name=1; Synonyms=Short;
CC         IsoId=Q9QYB5-2; Sequence=VSP_000189;
CC   -!- DOMAIN: Comprised of three regions: a N-terminal protease-
CC       resistant globular head region, a short connecting subdomain, and
CC       a protease-sensitive tail region.
CC   -!- PTM: Sumoylated (By similarity).
CC   -!- SIMILARITY: Belongs to the aldolase class II family. Adducin
CC       subfamily.
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DR   EMBL; AF100425; AAF24975.1; -; mRNA.
DR   EMBL; AF100424; AAF24974.1; -; mRNA.
DR   EMBL; AK019491; BAB31757.1; -; mRNA.
DR   IPI; IPI00387559; -.
DR   IPI; IPI00387580; -.
DR   UniGene; Mm.426080; -.
DR   ProteinModelPortal; Q9QYB5; -.
DR   SMR; Q9QYB5; 124-391.
DR   STRING; Q9QYB5; -.
DR   PhosphoSite; Q9QYB5; -.
DR   PRIDE; Q9QYB5; -.
DR   Ensembl; ENSMUST00000025999; ENSMUSP00000025999; ENSMUSG00000025026.
DR   Ensembl; ENSMUST00000050096; ENSMUSP00000052245; ENSMUSG00000025026.
DR   Ensembl; ENSMUST00000111741; ENSMUSP00000107370; ENSMUSG00000025026.
DR   MGI; MGI:1351615; Add3.
DR   GeneTree; ENSGT00390000016462; -.
DR   HOGENOM; HBG388064; -.
DR   HOVERGEN; HBG004180; -.
DR   InParanoid; Q9QYB5; -.
DR   OrthoDB; EOG4ZKJKS; -.
DR   ArrayExpress; Q9QYB5; -.
DR   Bgee; Q9QYB5; -.
DR   CleanEx; MM_ADD3; -.
DR   Genevestigator; Q9QYB5; -.
DR   GermOnline; ENSMUSG00000025026; Mus musculus.
DR   GO; GO:0005938; C:cell cortex; IDA:MGI.
DR   GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR   GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR   GO; GO:0005856; C:cytoskeleton; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IDA:MGI.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
DR   Gene3D; G3DSA:3.40.225.10; Aldolase_II/adducin_N; 1.
DR   Pfam; PF00596; Aldolase_II; 1.
DR   SUPFAM; SSF53639; Aldolase_II_N; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Calmodulin-binding;
KW   Cell membrane; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein;
KW   Ubl conjugation.
FT   CHAIN         1    706       Gamma-adducin.
FT                                /FTId=PRO_0000218537.
FT   REGION      684    701       Interaction with calmodulin (Potential).
FT   MOD_RES      12     12       Phosphothreonine (By similarity).
FT   MOD_RES      42     42       Phosphoserine (By similarity).
FT   MOD_RES     402    402       Phosphoserine.
FT   MOD_RES     423    423       Phosphoserine (By similarity).
FT   MOD_RES     442    442       Phosphoserine (By similarity).
FT   MOD_RES     673    673       Phosphoserine.
FT   MOD_RES     677    677       Phosphoserine.
FT   MOD_RES     681    681       Phosphoserine.
FT   MOD_RES     683    683       Phosphoserine; by PKC (By similarity).
FT   MOD_RES     693    693       Phosphoserine (By similarity).
FT   VAR_SEQ     578    609       Missing (in isoform 1).
FT                                /FTId=VSP_000189.
FT   CONFLICT     37     37       R -> G (in Ref. 2; BAB31757).
FT   CONFLICT    377    377       S -> T (in Ref. 2; BAB31757).
SQ   SEQUENCE   706 AA;  78763 MW;  4D152CB4457B6618 CRC64;
     MSSDTSPAVV TTPPPPSMPH KERYFDRINE SDPEYLRERN MSPDLRQDFN MMEQRKRVTQ
     ILQSPAFRED LECLIQEQMK KGHNPSGLLA LQQIADYIVT SSFSGFSSPS LSLGMVTPIN
     DLPGADTSSY VKGEKLTRCK LASLYRLADL FGWAHLANTY ISVRISKEQD HIIIIPRGLS
     FSEATASTLV KVNIIGEVVD QGSTDLKIDH TGFSPHAAIY STRPDVKCVI HIHTLATAAV
     SSMKCGILPI SQESLILGDV AYYDYQGSLD EEEERIELQK VLGPSCKVLV LRNHGMVALG
     ETLEEAFHYI FNVQMACEIQ VQAVAGAGGV DNLLVLDLQK YKAFTHGVAM SGGGGVNMAS
     HQKWKVGEIE FEGLMRSLDN LGYRTGYAYR HPLVREKPRH KSDVEIPATV TAFSFEDDSA
     PLSPLKFMAQ RQQREKTRWL NSPNTYMKVN VPEESRNGET SPRTKITWMK AEDSSKVSSG
     TPIKIEDPNQ FVPLNTNPTE VLEKRNKIRE QNRYDLKTAG PQSQLLAGIV VDKPPSTMQF
     DDDDQGPPAP PNPFSHLLEG ELEEYTKTIE RKQQGLDDAE QGSLSDDAAS VSQIQSQTQS
     PQSVPERLEE NHELFSKSFT SMDAPVMIMN GKDEMHDVED ELAQRVSRLT TSTTIENIEI
     TIKSPERTEE VLSPDGSPSK SPSKKKKKFR TPSFLKKNKK KEKVEA
//
ID   ADDB_MOUSE              Reviewed;         725 AA.
AC   Q9QYB8; Q3U0E1; Q80VH9; Q8C1C4; Q9CXE3; Q9JLE4; Q9JLE5; Q9QYB7;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Beta-adducin;
DE   AltName: Full=Add97;
DE   AltName: Full=Erythrocyte adducin subunit beta;
GN   Name=Add2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX   MEDLINE=20069066; PubMed=10602987; DOI=10.1007/s003350010004;
RA   Suriyapperuma S.P., Lozovatsky L., Ciciotte S.L., Peters L.L.,
RA   Gilligan D.M.;
RT   "The mouse adducin gene family: alternative splicing and chromosomal
RT   localization.";
RL   Mamm. Genome 11:16-23(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6;
RX   MEDLINE=20304505; PubMed=10845937;
RA   Muro A.F., Marro M.L., Gajovic S., Porro F., Luzzatto L.,
RA   Baralle F.E.;
RT   "Mild spherocytic hereditary elliptocytosis and altered levels of
RT   alpha- and gamma-adducins in beta-adducin-deficient mice.";
RL   Blood 95:3978-3985(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryonic liver, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Embryonic brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-561 (ISOFORM 2), AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION AT
RP   SER-594 AND SER-602, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-602 AND THR-687, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-532 AND SER-535, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Membrane-cytoskeleton-associated protein that promotes
CC       the assembly of the spectrin-actin network. Binds to calmodulin.
CC       Calmodulin binds preferentially to the beta subunit (By
CC       similarity).
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Cell membrane; Peripheral membrane protein; Cytoplasmic side (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1;
CC         IsoId=Q9QYB8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9QYB8-2; Sequence=VSP_000184, VSP_000185;
CC         Note=Phosphorylated on Thr-561;
CC       Name=3; Synonyms=Delta;
CC         IsoId=Q9QYB8-3; Sequence=VSP_022596;
CC   -!- DOMAIN: Each subunit is comprised of three regions: a NH2-terminal
CC       protease-resistant globular head region, a short connecting
CC       subdomain, and a protease-sensitive tail region.
CC   -!- SIMILARITY: Belongs to the aldolase class II family. Adducin
CC       subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF100422; AAF24972.1; -; mRNA.
DR   EMBL; AF100423; AAF24973.1; -; mRNA.
DR   EMBL; AF189769; AAF29502.1; -; mRNA.
DR   EMBL; AF189770; AAF29503.1; -; mRNA.
DR   EMBL; AK014496; BAB29395.1; -; mRNA.
DR   EMBL; AK028425; BAC25943.1; -; mRNA.
DR   EMBL; AK156954; BAE33913.1; -; mRNA.
DR   EMBL; BC046783; AAH46783.1; -; mRNA.
DR   EMBL; BC053032; AAH53032.1; -; mRNA.
DR   IPI; IPI00311962; -.
DR   IPI; IPI00323122; -.
DR   IPI; IPI00400328; -.
DR   PIR; A60670; A60670.
DR   RefSeq; NP_038486.2; NM_013458.4.
DR   UniGene; Mm.104155; -.
DR   ProteinModelPortal; Q9QYB8; -.
DR   SMR; Q9QYB8; 120-385.
DR   STRING; Q9QYB8; -.
DR   PhosphoSite; Q9QYB8; -.
DR   REPRODUCTION-2DPAGE; Q9QYB8; -.
DR   PRIDE; Q9QYB8; -.
DR   Ensembl; ENSMUST00000032068; ENSMUSP00000032068; ENSMUSG00000030000.
DR   Ensembl; ENSMUST00000032069; ENSMUSP00000032069; ENSMUSG00000030000.
DR   GeneID; 11519; -.
DR   KEGG; mmu:11519; -.
DR   UCSC; uc009crd.1; mouse.
DR   UCSC; uc009cre.1; mouse.
DR   CTD; 11519; -.
DR   MGI; MGI:87919; Add2.
DR   eggNOG; roNOG11939; -.
DR   GeneTree; ENSGT00390000016462; -.
DR   HOVERGEN; HBG004180; -.
DR   InParanoid; Q9QYB8; -.
DR   OMA; NFSMMTP; -.
DR   OrthoDB; EOG4894M8; -.
DR   PhylomeDB; Q9QYB8; -.
DR   NextBio; 278952; -.
DR   ArrayExpress; Q9QYB8; -.
DR   Bgee; Q9QYB8; -.
DR   CleanEx; MM_ADD2; -.
DR   Genevestigator; Q9QYB8; -.
DR   GermOnline; ENSMUSG00000030000; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IDA:MGI.
DR   GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
DR   Gene3D; G3DSA:3.40.225.10; Aldolase_II/adducin_N; 1.
DR   Pfam; PF00596; Aldolase_II; 1.
DR   SUPFAM; SSF53639; Aldolase_II_N; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Alternative splicing; Calmodulin-binding;
KW   Cell membrane; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    725       Beta-adducin.
FT                                /FTId=PRO_0000218534.
FT   REGION      425    444       Interaction with calmodulin (Potential).
FT   REGION      703    720       Interaction with calmodulin (Potential).
FT   MOD_RES       2      2       N-acetylserine.
FT   MOD_RES      55     55       Phosphothreonine (By similarity).
FT   MOD_RES     532    532       Phosphoserine.
FT   MOD_RES     535    535       Phosphoserine.
FT   MOD_RES     561    561       Phosphothreonine.
FT   MOD_RES     594    594       Phosphoserine.
FT   MOD_RES     598    598       Phosphoserine (By similarity).
FT   MOD_RES     602    602       Phosphoserine.
FT   MOD_RES     606    606       Phosphoserine (By similarity).
FT   MOD_RES     687    687       Phosphothreonine.
FT   MOD_RES     692    692       Phosphoserine (By similarity).
FT   MOD_RES     696    696       Phosphoserine (By similarity).
FT   MOD_RES     698    698       Phosphoserine (By similarity).
FT   MOD_RES     702    702       Phosphoserine (By similarity).
FT   MOD_RES     712    712       Phosphoserine (By similarity).
FT   VAR_SEQ     284    531       Missing (in isoform 3).
FT                                /FTId=VSP_022596.
FT   VAR_SEQ     532    562       STESQLMSKGDADTKDESEETVPNPFSQLTD -> VQQRLP
FT                                PTEGEVYQTPGAGQGTPESSGPLTP (in isoform 2).
FT                                /FTId=VSP_000184.
FT   VAR_SEQ     563    725       Missing (in isoform 2).
FT                                /FTId=VSP_000185.
FT   CONFLICT    219    219       R -> T (in Ref. 2; AAF29503).
FT   CONFLICT    469    469       E -> Q (in Ref. 1; AAF24972/AAF24973).
FT   CONFLICT    518    518       Q -> H (in Ref. 3; BAC25943).
FT   CONFLICT    634    634       A -> R (in Ref. 1; AAF24972).
FT   CONFLICT    666    666       G -> V (in Ref. 1; AAF24972).
FT   CONFLICT    675    675       D -> V (in Ref. 2; AAF29502/AAF29503).
SQ   SEQUENCE   725 AA;  80642 MW;  479153AB1BD6C0DA CRC64;
     MSEDTVPEAA SPPPSQGQHY FDRFSEDDPE YLRLRNRAAD LRQDFNLMEQ KKRVTMILQS
     PSFREELEGL IQEQMKKGNN SSNIWALRQI ADFMASTSHA VFPASSMNFS MMTPINDLHT
     ADSLNLAKGE RLMRCKISSV YRLLDLYGWA QLSDTYVTLR VSKEQDHFLI SPKGVSCSEV
     TASSLIKVNI LGEVVEKGSS CFPVDTTGFS LHSAIYAARP DVRCAIHLHT PATAAVSAMK
     CGLLPVSHNA LLVGDMAYYD FNGEMEQEAD RINLQKCLGP TCKILVLRNH GMVALGDTVE
     EAFYKVFHLQ AACEVQVSAL SSAGGTENLI LLEQEKHRPH EVGSVQWAGS TFGPMQKSRL
     GEHEFEALMR MLDNLGYRTG YTYRHPFVQE KTKHKSEVEI PATVTAFVFE EDGVPVPALR
     QHAQKQQKEK TRWLNTPNTY LRVNVADEVQ RNMGSPRPKT TWMKADEVEK SSSGMPIRIE
     NPNQFVPLYT DPQEVLDMRN KIREQNRQDI KSAGPQSQLL ASVIAEKSRS PSTESQLMSK
     GDADTKDESE ETVPNPFSQL TDQELEEYKK EVERKKLEQE QEGEKDIATE KPGSPVKSTP
     ASPVQSPSKA GTKSPAVSPS KTSEDTKKTE VSEANTEPEP VKPEGLVVNG KEEEPSVEEA
     LSKGLGQMTT NADTDGDSYK DKTESVTSGP LSPEGSPSKS PSKKKKKFRT PSFLKKSKKK
     EKVES
//
ID   ADDA_MOUSE              Reviewed;         735 AA.
AC   Q9QYC0; Q9JLE3;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Alpha-adducin;
DE   AltName: Full=Erythrocyte adducin subunit alpha;
GN   Name=Add1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RX   MEDLINE=20069066; PubMed=10602987; DOI=10.1007/s003350010004;
RA   Suriyapperuma S.P., Lozovatsky L., Ciciotte S.L., Peters L.L.,
RA   Gilligan D.M.;
RT   "The mouse adducin gene family: alternative splicing and chromosomal
RT   localization.";
RL   Mamm. Genome 11:16-23(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=20304505; PubMed=10845937;
RA   Muro A.F., Marro M.L., Gajovic S., Porro F., Luzzatto L.,
RA   Baralle F.E.;
RT   "Mild spherocytic hereditary elliptocytosis and altered levels of
RT   alpha- and gamma-adducins in beta-adducin-deficient mice.";
RL   Blood 95:3978-3985(2000).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-610, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-586, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-355; THR-358; SER-586;
RP   THR-610 AND THR-614, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-358; SER-483 AND
RP   THR-610, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Membrane-cytoskeleton-associated protein that promotes
CC       the assembly of the spectrin-actin network. Binds to calmodulin.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit or an alpha
CC       and a gamma subunit. Binds ROCK1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane;
CC       Peripheral membrane protein; Cytoplasmic side.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1;
CC         IsoId=Q9QYC0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9QYC0-2; Sequence=VSP_000177, VSP_000178;
CC   -!- DOMAIN: Each subunit is comprised of three regions: a NH2-terminal
CC       protease-resistant globular head region, a short connecting
CC       subdomain, and a protease-sensitive tail region.
CC   -!- SIMILARITY: Belongs to the aldolase class II family. Adducin
CC       subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF096839; AAF24971.1; -; mRNA.
DR   EMBL; AF189771; AAF29504.1; -; mRNA.
DR   IPI; IPI00136000; -.
DR   IPI; IPI00225322; -.
DR   RefSeq; NP_001019629.2; NM_001024458.3.
DR   RefSeq; NP_001095914.1; NM_001102444.1.
DR   RefSeq; NP_038485.1; NM_013457.3.
DR   UniGene; Mm.289106; -.
DR   ProteinModelPortal; Q9QYC0; -.
DR   SMR; Q9QYC0; 132-397.
DR   STRING; Q9QYC0; -.
DR   PhosphoSite; Q9QYC0; -.
DR   PRIDE; Q9QYC0; -.
DR   Ensembl; ENSMUST00000114338; ENSMUSP00000109977; ENSMUSG00000029106.
DR   Ensembl; ENSMUST00000114340; ENSMUSP00000109979; ENSMUSG00000029106.
DR   GeneID; 11518; -.
DR   KEGG; mmu:11518; -.
DR   NMPDR; fig|10090.3.peg.11472; -.
DR   UCSC; uc008xcp.1; mouse.
DR   UCSC; uc008xcr.1; mouse.
DR   CTD; 11518; -.
DR   MGI; MGI:87918; Add1.
DR   GeneTree; ENSGT00390000016462; -.
DR   HOGENOM; HBG388064; -.
DR   HOVERGEN; HBG004180; -.
DR   InParanoid; Q9QYC0; -.
DR   OMA; KWQIGEQ; -.
DR   OrthoDB; EOG4SQWWG; -.
DR   PhylomeDB; Q9QYC0; -.
DR   NextBio; 278944; -.
DR   ArrayExpress; Q9QYC0; -.
DR   Bgee; Q9QYC0; -.
DR   CleanEx; MM_ADD1; -.
DR   Genevestigator; Q9QYC0; -.
DR   GermOnline; ENSMUSG00000029106; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IDA:MGI.
DR   GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR   GO; GO:0006884; P:cell volume homeostasis; IMP:MGI.
DR   GO; GO:0030218; P:erythrocyte differentiation; IMP:MGI.
DR   GO; GO:0020027; P:hemoglobin metabolic process; IMP:MGI.
DR   GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
DR   Gene3D; G3DSA:3.40.225.10; Aldolase_II/adducin_N; 1.
DR   Pfam; PF00596; Aldolase_II; 1.
DR   SUPFAM; SSF53639; Aldolase_II_N; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Alternative splicing; Calmodulin-binding;
KW   Cell membrane; Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein.
FT   CHAIN         1    735       Alpha-adducin.
FT                                /FTId=PRO_0000218531.
FT   REGION      715    732       Interaction with calmodulin (Potential).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      12     12       Phosphoserine.
FT   MOD_RES      59     59       Phosphoserine; by PKA (By similarity).
FT   MOD_RES     331    331       Phosphothreonine (By similarity).
FT   MOD_RES     334    334       Phosphoserine (By similarity).
FT   MOD_RES     353    353       Phosphoserine (By similarity).
FT   MOD_RES     355    355       Phosphoserine.
FT   MOD_RES     358    358       Phosphothreonine.
FT   MOD_RES     408    408       Phosphoserine; by PKA (By similarity).
FT   MOD_RES     431    431       Phosphoserine (By similarity).
FT   MOD_RES     436    436       Phosphoserine; by PKA (By similarity).
FT   MOD_RES     445    445       Phosphothreonine; by ROCK1 (By
FT                                similarity).
FT   MOD_RES     464    464       Phosphoserine (By similarity).
FT   MOD_RES     465    465       Phosphoserine (By similarity).
FT   MOD_RES     480    480       Phosphothreonine; by ROCK1 (By
FT                                similarity).
FT   MOD_RES     481    481       Phosphoserine; by PKA (By similarity).
FT   MOD_RES     483    483       Phosphoserine.
FT   MOD_RES     586    586       Phosphoserine.
FT   MOD_RES     610    610       Phosphothreonine.
FT   MOD_RES     614    614       Phosphothreonine.
FT   MOD_RES     705    705       Phosphoserine (By similarity).
FT   MOD_RES     708    708       Phosphoserine (By similarity).
FT   MOD_RES     714    714       Phosphoserine; by PKC (By similarity).
FT   MOD_RES     724    724       Phosphoserine; by PKA and PKC (By
FT                                similarity).
FT   VAR_SEQ     621    632       DLPQEPTSRDDS -> AGDGCAKEYLLP (in isoform
FT                                2).
FT                                /FTId=VSP_000177.
FT   VAR_SEQ     633    735       Missing (in isoform 2).
FT                                /FTId=VSP_000178.
FT   CONFLICT    234    234       A -> T (in Ref. 2; AAF29504).
SQ   SEQUENCE   735 AA;  80647 MW;  E6AAA7F6273A33DD CRC64;
     MNGDTRAAVV TSPPPTTAPH KERYFDRVDE NNPEYLRERN MAPDLRQDFN MMEQKKRVSM
     ILQSPAFCEE LESMIQEQFK KGKNPTGLLA LQQIADFMTA SVPNVYPAAP QGGMAALNMS
     LGMVTPVNDL RGSDSIAYDK GEKLLRCKLA AFYRLADLFG WSQLIYNHIT TRVNSEQEHF
     LIVPFGLLYS EVTASSLVKV NLQGDIVDRG STNLGVNQAG FTLHSAVYAA RPDAKCIVHI
     HTPAGAAVSA MKCGLLPISP EALSLGDVAY HDYHGILVDE EEKILIQKNL GPKSKVLILR
     NHGLVSVGES VEEAFYYIHN LVVACEIQVR TLASAGGPDN LVLLDPGKYK AKSRSPGTPA
     GEGSGSPPKW QIGEQEFEAL MRMLDNLGYR TGYPYRYPAL RERSKKYSDV EVPASVTGHS
     FASDGDSGTC SPLRHSFQKQ QREKTRWLHS GRGDDASEEG QNGSSPKSKT KWTKEDGHRT
     STSAVPNLFV PLNTNPKEVQ EMRNKIREQN LQDIKTAGPQ SQVLCGVMMD RSLVQGELVT
     ASKAIIEKEY QPHVIVSTTG PNPFNTLTDR ELEEYRREVE RKQKGSEENL DETREQKEKS
     PPDQSAVPNT PPSTPVKLEE DLPQEPTSRD DSDATTFKPT PPDLSPDEPS EALAFPAVEE
     EAHASPDPTQ PPAEADPEPA SAPTPGAEEV ASPATEEGSP MDPGSDGSPG KSPSKKKKKF
     RTPSFLKKSK KKSDS
//
ID   PCX1_MOUSE              Reviewed;        2344 AA.
AC   Q9QYC1; Q6ZQ41; Q9CUU7;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=Pecanex-like protein 1;
DE   AltName: Full=Pecanex homolog;
GN   Name=Pcnx; Synonyms=Kiaa0805, Pcnxl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 594-2344 (ISOFORM 2).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 880-2344 (ISOFORM 1).
RA   Roux A.-F.;
RT   "Cloning of a mouse homolog of the Drosophila pecanex gene.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1658-2344 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9QYC1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9QYC1-2; Sequence=VSP_022167;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the pecanex family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF21809.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AC124484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC124595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK129221; BAC98031.3; -; mRNA.
DR   EMBL; AF096286; AAF21809.1; ALT_INIT; mRNA.
DR   EMBL; AK014387; BAB29314.1; -; mRNA.
DR   IPI; IPI00420564; -.
DR   IPI; IPI00751279; -.
DR   RefSeq; NP_061284.2; NM_018814.3.
DR   UniGene; Mm.86584; -.
DR   PhosphoSite; Q9QYC1; -.
DR   PRIDE; Q9QYC1; -.
DR   Ensembl; ENSMUST00000021567; ENSMUSP00000021567; ENSMUSG00000021140.
DR   Ensembl; ENSMUST00000095564; ENSMUSP00000093220; ENSMUSG00000021140.
DR   GeneID; 54604; -.
DR   KEGG; mmu:54604; -.
DR   UCSC; uc007ocq.1; mouse.
DR   CTD; 54604; -.
DR   MGI; MGI:1891924; Pcnx.
DR   GeneTree; ENSGT00390000013164; -.
DR   HOGENOM; HBG564661; -.
DR   HOVERGEN; HBG045627; -.
DR   InParanoid; Q9QYC1; -.
DR   OMA; CSGTDRD; -.
DR   OrthoDB; EOG4WSW8Q; -.
DR   PhylomeDB; Q9QYC1; -.
DR   NextBio; 311396; -.
DR   ArrayExpress; Q9QYC1; -.
DR   Bgee; Q9QYC1; -.
DR   CleanEx; MM_PCNX; -.
DR   Genevestigator; Q9QYC1; -.
DR   GermOnline; ENSMUSG00000021140; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR007735; Pecanex.
DR   Pfam; PF05041; Pecanex_C; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   2344       Pecanex-like protein 1.
FT                                /FTId=PRO_0000215794.
FT   TRANSMEM     33     53       Helical; (Potential).
FT   TRANSMEM     57     77       Helical; (Potential).
FT   TRANSMEM   1010   1030       Helical; (Potential).
FT   TRANSMEM   1035   1055       Helical; (Potential).
FT   TRANSMEM   1069   1089       Helical; (Potential).
FT   TRANSMEM   1119   1139       Helical; (Potential).
FT   TRANSMEM   1163   1183       Helical; (Potential).
FT   TRANSMEM   1196   1216       Helical; (Potential).
FT   TRANSMEM   1269   1289       Helical; (Potential).
FT   TRANSMEM   1297   1317       Helical; (Potential).
FT   COMPBIAS    320    417       Ser-rich.
FT   COMPBIAS    573    638       Ser-rich.
FT   COMPBIAS   2106   2202       Ser-rich.
FT   CARBOHYD   1094   1094       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1158   1158       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1582   1582       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1723   1723       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1985   1985       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2075   2075       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2231   2231       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2237   2237       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2263   2263       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     854    945       Missing (in isoform 2).
FT                                /FTId=VSP_022167.
FT   CONFLICT    930    934       Missing (in Ref. 3; AAF21809).
FT   CONFLICT   1220   1220       S -> N (in Ref. 3; AAF21809).
FT   CONFLICT   1457   1457       L -> R (in Ref. 3; AAF21809).
FT   CONFLICT   1806   1806       A -> T (in Ref. 4; BAB29314).
FT   CONFLICT   1874   1874       E -> K (in Ref. 4; BAB29314).
FT   CONFLICT   1899   1899       D -> Y (in Ref. 4; BAB29314).
FT   CONFLICT   2318   2318       K -> N (in Ref. 3; AAF21809).
SQ   SEQUENCE   2344 AA;  258147 MW;  FF3E3C60D57488CB CRC64;
     MGSQTLQILR QGVWAALSGG WYYDPHQATF VNALHLYLWL FLLGLPFTLY MALPSSMIIV
     AVYCPVVAAV FIILKMVNYR LHRALDAGEI VDRSAKEFTD QRAKAEQGNC STRRKDSNGP
     SDPGGGIEMS EFIREATPPV GCSSRNSYAG LDPSNQIGSG SSRLGTAATI KGDTDTAKTS
     DDISLSLGQS SSLCKEGSEE QDLATDRKLF RLVSNDSFIS IQPSLSSCGQ DLPRDFSDKV
     SLPSHSQHHR VDQSLCSACD TEVASLVPLH SHSYRKEHRP RGVPRTSSSA VAFPDASLSG
     LPLYQQQQRR GLDPVTELDS SKPHSGTRES SAGKSCPPAQ SQPAADRRKS SSQPPTKCGK
     SRALNAEKSV DSLRSLSTRS SGSTESYCSG TDRDTNSTLS SYKSEQTSST HIESILSEHE
     ESPKVGDKSA RKRECGADSV EERSHRADDR RTSSDKTAPE GNTPAGPPEA PDAQASEEMA
     DQAAPSSSAS EDANKNPHAN EFTVPGDRPP EQSAESKEEQ SEKPSLATDS RVCKDDGGKQ
     KEGDVRPKSS SLIHRTTSAH KPGRRRTGKK RASSFDSSRH RDYVSFRGVS GTKPHSAVFG
     HDEDSSDQSD LSRAPSIHSA HQFSSDSSSS ATSHSCQSPE GKYGALKTKH GHRDRGTDSD
     HTHRAHPGPE GTTKKRASRR TSSTSSAKTR ARVLSLDSGT VACLNDSNRL LAPDSMKPLT
     TSKSDLEAKE GEVLDELSLL GRASQLETVT RSRNSLPSQV AFPEGEEQDA ATGAAQASEE
     AVAFRRERST FRRQAVRRRH NAGSNPTPPT LLIGSPLSLQ DGQQGQQSTA QVKVQSRPPS
     QAAVLSASAS LLVRKGSVHL EASHDHASAV GGSSLHDELG KFSSTLYETG GCDMSLVNFE
     PAARRASNIC DTDSHVSSST SVRFYPHDML SLPQIRLNRL LTIDTDLLEQ QDIDLSPDLA
     ATYGPTEEAA QKVKHYYRFW VLPQLWIGIN FDRLTLLALF DRNREILENI LAVVLAILVA
     FLGSILLIQG FFRDIWVFQF CLVIASCQYS LLKSVQPDSS SPRHGHNRII AYSRPVYFCL
     CCGLIWLLDY GSRNLTTSKF KLYGVTFTNP LVLLSARDLV IVFTLCFPIV FFIGLLPQVN
     TFVMYLCEQL DIHIFGGNAT TSLLAALYSF LCSIVAVALL YGLCYGALRD SWDGQHVPVL
     FSVFCGLLVA VSYHLSRQSS DPSVLFSLMQ SKIFPKADEK NPEDPLSEVK DPLPEKLSNS
     VSERLQSDLV VCVIIGVLYF AIHVSTVFTA LQPALKYVLY ALVGVVGLVT HYVLPQVRKQ
     LPWHCFSRPL LRTAEHSQYE VRNAATMMWF EKLHVWLLFV EKNIIYPLIV LNELSSSAET
     IASPKKLDTE LGALMITIAG LKLLRSSFSS PTYQYITVIF TVLFFKFDYE AFSETMLLDL
     FFMSILFSKL WELLYKLQFV YTYVAPWQIT WGSAFHAFAQ PFAVPHSAML FVQAIVSAFF
     STPLNPFLGS AIFITSYVRP VKFWERDYNT KRVDHSNTRL ASQLDRNPGS DDNNLNSIFY
     EHLTRSLQHS LCGDLLLGRW GNYSTGDCFI LASDYLNALV HLIEIGNGLV TFQLRGLEFR
     GTYCQQREVE AITEGVEEDE GFCCCEPGHV PHVLSFNAAF GQRWLAWEVV VTKYILEGYS
     ITDNSAASML QVFDLRRVLT TYYVKGIIYY VTTSSKLEEW LANETMQEGL RLCADRNYVD
     VDPTFNPNID EDYDHRLAGI SRESFCVIYL SWIEYCSSRR AKPLDVDKDS SLVTLCYGLC
     VLGRRALGTA SHHMSSNLES FLYGLHALFK GDFRISSVRD EWIFADMELL RKVVVPGIRM
     SIKLHQDHFT SPDEYDDPTV LYEAIVSHEK NLVIAHEGDP AWRSAVLANS PSLLALRHVM
     DDGTNEYKII MLNRRYLSFR VIKVNKECVR GLWAGQQQEL VFLRNRNPER GSIQNAKQAL
     RNMINSSCDQ PIGYPIFVSP LTTSYSDSHD QLKEILGGPI SLGNIRNFIV STWHRLRKGC
     GAGCNSGGNI EDSDTGGGTS CPGNSAVTAS DPHNNVSQGS TGHPGQGAGS GLHPPTTSYP
     PTLGTSHSAH SVQSSLVRQS PARASMASQS SYCYSSRHSS LRMSTTGFVP CRRSSTSQIS
     LRNLPSSIQS RLSMVNQMEA ASQGGMGCVQ HGLPSSSSSS QSIPACKHHT LVAFLGAEGG
     QGSATEAQPG NTSSPANISH ARKGEVIYRV QIVDLSQILE GINVSKRKEL HWPDEGIRLK
     AGRNSWKDWS PQEGMEGHVV HRWVPCSRDP STRSHIDKTV LLVQIDDKYV TIIETGVLEL
     GAEV
//
ID   BC11A_MOUSE             Reviewed;         773 AA.
AC   Q9QYE3; Q80T89; Q8BLC7; Q8BLR4; Q8BWX3; Q921V4; Q9D0V2; Q9JIT4;
AC   Q9JLK8; Q9JLK9;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=B-cell lymphoma/leukemia 11A;
DE            Short=BCL-11A;
DE   AltName: Full=B-cell CLL/lymphoma 11A;
DE   AltName: Full=COUP-TF-interacting protein 1;
DE   AltName: Full=Ecotropic viral integration site 9 protein;
DE            Short=EVI-9;
GN   Name=Bcl11a; Synonyms=Ctip1, Evi9, Kiaa1809;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=BXH/2;
RX   MEDLINE=20221564; PubMed=10757802;
RX   DOI=10.1128/MCB.20.9.3178-3186.2000;
RA   Nakamura T., Yamazaki Y., Saiki Y., Moriyama M., Largaespada D.A.,
RA   Jenkins N.A., Copeland N.G.;
RT   "Evi9 encodes a novel zinc finger protein that physically interacts
RT   with BCL6, a known human B-cell proto-oncogene product.";
RL   Mol. Cell. Biol. 20:3178-3186(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH TFCOUP1;
RP   EAR2 AND ARP1.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=20209406; PubMed=10744719; DOI=10.1074/jbc.275.14.10315;
RA   Avram D., Fields A., Pretty On Top K., Nevrivy D.J., Ishmael J.E.,
RA   Leid M.;
RT   "Isolation of a novel family of C(2)H(2) zinc finger proteins
RT   implicated in transcriptional repression mediated by chicken ovalbumin
RT   upstream promoter transcription factor (COUP-TF) orphan nuclear
RT   receptors.";
RL   J. Biol. Chem. 275:10315-10322(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain, Brain cortex, Corpora quadrigemina, Embryo, and
RC   Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 8).
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   FUNCTION.
RX   PubMed=12717432; DOI=10.1038/ni925;
RA   Liu P., Keller J.R., Ortiz M., Tessarollo L., Rachel R.A.,
RA   Nakamura T., Jenkins N.A., Copeland N.G.;
RT   "Bcl11a is essential for normal lymphoid development.";
RL   Nat. Immunol. 4:525-532(2003).
RN   [7]
RP   SUMOYLATION AT LYS-634, INTERACTION WITH PIAS3, SUBCELLULAR LOCATION,
RP   AND MUTAGENESIS OF LYS-123 AND LYS-637.
RX   PubMed=18681895; DOI=10.1111/j.1365-2443.2008.01216.x;
RA   Kuwata T., Nakamura T.;
RT   "BCL11A is a SUMOylated protein and recruits SUMO-conjugation enzymes
RT   in its nuclear body.";
RL   Genes Cells 13:931-940(2008).
CC   -!- FUNCTION: Functions as a myeloid and B-cell proto-oncogene. May
CC       play important roles in leukemogenesis and hematopoiesis. An
CC       essential factor in lymphopoiesis, is required for B-cell
CC       formation in fetal liver. May function as a modulator of the
CC       transcriptional repression activity of ARP1.
CC   -!- SUBUNIT: Interacts with TFCOUP1, PIAS3, ARP1 and EAR2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Associates with the
CC       nuclear body. Colocalizes with SUMO1 and SENP2 in nuclear
CC       speckles.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC       Name=1; Synonyms=a;
CC         IsoId=Q9QYE3-1; Sequence=Displayed;
CC       Name=2; Synonyms=b;
CC         IsoId=Q9QYE3-10; Sequence=VSP_009557, VSP_009563;
CC       Name=3; Synonyms=c;
CC         IsoId=Q9QYE3-11; Sequence=VSP_009560;
CC       Name=4;
CC         IsoId=Q9QYE3-12; Sequence=VSP_009556, VSP_009564;
CC       Name=5;
CC         IsoId=Q9QYE3-13; Sequence=VSP_009561, VSP_009562;
CC       Name=6;
CC         IsoId=Q9QYE3-14; Sequence=VSP_009558, VSP_009561, VSP_009562;
CC       Name=7;
CC         IsoId=Q9QYE3-15; Sequence=VSP_009559;
CC       Name=8;
CC         IsoId=Q9QYE3-16; Sequence=VSP_009557;
CC   -!- TISSUE SPECIFICITY: Isoforms are expressed in a tissue-specific
CC       fashion. Isoforms 1, isoform 2, and isoform 3 are expressed at
CC       similar levels in testis, kidney and spleen. Isoform 1 is
CC       expressed in the stomach, and isoform 2 is expressed exclusively
CC       in the lung. Overexpression following proviral integration in
CC       hematopoietic cells results in the generation of myeloid leukemia.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed in the developing embryo.
CC   -!- PTM: Sumoylated by SUMO1.
CC   -!- SIMILARITY: Contains 3 C2H2-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF63682.1; Type=Frameshift; Positions=744;
CC       Sequence=BAC65839.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; AF051525; AAF22430.1; -; mRNA.
DR   EMBL; AF169036; AAF65928.1; -; mRNA.
DR   EMBL; AF169037; AAF65929.1; -; mRNA.
DR   EMBL; AF186018; AAF63682.1; ALT_FRAME; mRNA.
DR   EMBL; AK004395; BAB23285.1; -; mRNA.
DR   EMBL; AK043677; BAC31616.1; -; mRNA.
DR   EMBL; AK045556; BAC32416.1; -; mRNA.
DR   EMBL; AK049700; BAC33881.1; -; mRNA.
DR   EMBL; AK122557; BAC65839.1; ALT_INIT; mRNA.
DR   EMBL; BC010585; AAH10585.1; -; mRNA.
DR   EMBL; BC051418; AAH51418.1; -; mRNA.
DR   IPI; IPI00267748; -.
DR   IPI; IPI00272308; -.
DR   IPI; IPI00405328; -.
DR   IPI; IPI00405329; -.
DR   IPI; IPI00405330; -.
DR   IPI; IPI00405331; -.
DR   IPI; IPI00405332; -.
DR   IPI; IPI00405333; -.
DR   PIR; PT0706; PT0706.
DR   RefSeq; NP_001152761.1; NM_001159289.1.
DR   RefSeq; NP_001152762.1; NM_001159290.1.
DR   RefSeq; NP_057916.1; NM_016707.3.
DR   UniGene; Mm.447614; -.
DR   UniGene; Mm.471050; -.
DR   UniGene; Mm.53687; -.
DR   UniGene; Mm.88824; -.
DR   ProteinModelPortal; Q9QYE3; -.
DR   SMR; Q9QYE3; 168-194, 370-458.
DR   STRING; Q9QYE3; -.
DR   PhosphoSite; Q9QYE3; -.
DR   PRIDE; Q9QYE3; -.
DR   Ensembl; ENSMUST00000000881; ENSMUSP00000000881; ENSMUSG00000000861.
DR   Ensembl; ENSMUST00000109512; ENSMUSP00000105138; ENSMUSG00000000861.
DR   GeneID; 14025; -.
DR   KEGG; mmu:14025; -.
DR   UCSC; uc007ifu.1; mouse.
DR   UCSC; uc007ifv.1; mouse.
DR   UCSC; uc007ifw.1; mouse.
DR   CTD; 14025; -.
DR   MGI; MGI:106190; Bcl11a.
DR   GeneTree; ENSGT00530000063542; -.
DR   HOVERGEN; HBG050673; -.
DR   OrthoDB; EOG405S0N; -.
DR   PhylomeDB; Q9QYE3; -.
DR   NextBio; 284944; -.
DR   ArrayExpress; Q9QYE3; -.
DR   Bgee; Q9QYE3; -.
DR   CleanEx; MM_BCL11A; -.
DR   Genevestigator; Q9QYE3; -.
DR   GermOnline; ENSMUSG00000000861; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030183; P:B cell differentiation; IMP:MGI.
DR   GO; GO:0016925; P:protein sumoylation; IMP:UniProtKB.
DR   GO; GO:0030217; P:T cell differentiation; IMP:MGI.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 2.
DR   Pfam; PF00096; zf-C2H2; 1.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Isopeptide bond; Metal-binding;
KW   Nucleus; Phosphoprotein; Repeat; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1    773       B-cell lymphoma/leukemia 11A.
FT                                /FTId=PRO_0000047103.
FT   ZN_FING     170    193       C2H2-type 1.
FT   ZN_FING     377    399       C2H2-type 2.
FT   ZN_FING     405    429       C2H2-type 3.
FT   REGION        1    210       Required for nuclear body formation and
FT                                for SUMO1 recruitment.
FT   COMPBIAS    260    373       Pro-rich.
FT   COMPBIAS    481    509       Glu-rich.
FT   MOD_RES      86     86       Phosphoserine (By similarity).
FT   MOD_RES     205    205       Phosphoserine (By similarity).
FT   MOD_RES     208    208       Phosphothreonine (By similarity).
FT   MOD_RES     332    332       Phosphoserine (By similarity).
FT   MOD_RES     608    608       Phosphoserine (By similarity).
FT   MOD_RES     625    625       Phosphoserine (By similarity).
FT   MOD_RES     630    630       Phosphoserine (By similarity).
FT   MOD_RES     701    701       Phosphothreonine (By similarity).
FT   CROSSLNK    634    634       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO-1).
FT   VAR_SEQ       1    423       Missing (in isoform 4).
FT                                /FTId=VSP_009556.
FT   VAR_SEQ       1    286       Missing (in isoform 2 and isoform 8).
FT                                /FTId=VSP_009557.
FT   VAR_SEQ       1     52       Missing (in isoform 6).
FT                                /FTId=VSP_009558.
FT   VAR_SEQ     131    773       Missing (in isoform 7).
FT                                /FTId=VSP_009559.
FT   VAR_SEQ     212    744       Missing (in isoform 3).
FT                                /FTId=VSP_009560.
FT   VAR_SEQ     212    243       GIPSGLGAECPSQPPLHGIHIADNNPFNLLRI -> LHTPP
FT                                FGVVPRELKMCGSFRMEAQEPLSSEKL (in isoform 5
FT                                and isoform 6).
FT                                /FTId=VSP_009561.
FT   VAR_SEQ     244    773       Missing (in isoform 5 and isoform 6).
FT                                /FTId=VSP_009562.
FT   VAR_SEQ     726    773       Missing (in isoform 2).
FT                                /FTId=VSP_009563.
FT   VAR_SEQ     745    773       PSHTPVRRSTPRAQDVWQFSDGSSRTLKF -> EYCGKVFK
FT                                NCSNLTVHRRSHTGERPYKCELCNYACAQSSKLTRHMKTHG
FT                                QVGKDVYKCEICKMPFSVYSTLEKHMKKWHSDRVLNNDIKT
FT                                E (in isoform 4).
FT                                /FTId=VSP_009564.
FT   MUTAGEN     123    123       K->R: No effect on sumoylation.
FT   MUTAGEN     637    637       K->R: Abolishes sumoylation. No effect on
FT                                nuclear body location.
FT   CONFLICT    104    104       Q -> K (in Ref. 3; BAB23285).
FT   CONFLICT    129    129       D -> G (in Ref. 4; BAC65839).
FT   CONFLICT    211    211       V -> G (in Ref. 1; AAF65929).
FT   CONFLICT    673    673       F -> L (in Ref. 2; AAF63682).
FT   CONFLICT    699    699       F -> L (in Ref. 1; AAF65928).
FT   CONFLICT    743    743       T -> I (in Ref. 2; AAF63682).
FT   CONFLICT    773    773       F -> L (in Ref. 2; AAF63682).
SQ   SEQUENCE   773 AA;  83855 MW;  3BD10B7F14AA9EC4 CRC64;
     MSRRKQGKPQ HLSKREFSPE PLEAILTDDE PDHGPLGAPE GDHDLLTCGQ CQMNFPLGDI
     LIFIEHKRKQ CNGSLCLEKG VDKPPSPSPI EMKKASNPVE VGIQVTPEDD DCLSTSSRGI
     CPKQEHIADK LLHWRGLSSP RSAHGALIPT PGMSAEYAPQ GICKDEPSSY TCTTCKQPFT
     SAWFLLQHAQ NTHGLRIYLE SEHGSPLTPR VGIPSGLGAE CPSQPPLHGI HIADNNPFNL
     LRIPGSVSRE ASGLAEGRFP PTPPLFSPPP RHHLDPHRIE RLGAEEMALA THHPSAFDRV
     LRLNPMAMEP PAMDFSRRLR ELAGNTSSPP LSPGRPSPMQ RLLQPFQPGS KPPFLATPPL
     PPLQSAPPPS QPPVKSKSCE FCGKTFKFQS NLVVHRRSHT GEKPYKCNLC DHACTQASKL
     KRHMKTHMHK SSPMTVKSDD GLSTASSPEP GTSDLVGSAS SALKSVVAKF KSENDPNLIP
     ENGDEEEEED DEEEEEEEEE EEEELTESER VDYGFGLSLE AARHHENSSR GAVVGVGDEG
     RALPDVMQGM VLSSMQHFSE AFHQVLGEKH KRSHLAEAEG HRDTCDEDSV AGESDRIDDG
     TVNGRGCSPG ESASGGLSKK LLLGSPSSLS PFSKRIKLEK EFDLPPAAMP NTENVYSQWL
     AGYAASRQLK DPFLTFGDSR QSPFASSSEH SSENGSLRFS TPPGELDGGI SGRSGTGSGG
     STPHISGPGP GRPSSKEGRR SDTCPSHTPV RRSTPRAQDV WQFSDGSSRT LKF
//
ID   JAG2_MOUSE              Reviewed;        1247 AA.
AC   Q9QYE5; O55139; O70219;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 100.
DE   RecName: Full=Protein jagged-2;
DE            Short=Jagged2;
DE   Flags: Precursor;
GN   Name=Jag2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster / NIH;
RA   Tsai S.;
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 302-819.
RC   TISSUE=Brain;
RX   MEDLINE=98051918; PubMed=9341252; DOI=10.1007/s003359900642;
RA   Lan Y., Jiang R., Shawber C., Weinmaster G., Gridley T.;
RT   "The Jagged2 gene maps to chromosome 12 and is a candidate for the lgl
RT   and sm mutations.";
RL   Mamm. Genome 8:875-876(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 325-759.
RC   TISSUE=Brain;
RX   MEDLINE=98145947; PubMed=9486542; DOI=10.1016/S0925-4773(97)00146-9;
RA   Valsecchi C., Ghezzi C., Ballabio A., Rugarli E.I.;
RT   "JAGGED2: a putative Notch ligand expressed in the apical ectodermal
RT   ridge and in sites of epithelial-mesenchymal interactions.";
RL   Mech. Dev. 69:203-207(1997).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=97459705; PubMed=9315665;
RA   Luo B., Aster J.C., Hasserjian R.P., Kuo F., Sklar J.;
RT   "Isolation and functional analysis of a cDNA for human Jagged2, a gene
RT   encoding a ligand for the Notch1 receptor.";
RL   Mol. Cell. Biol. 17:6057-6067(1997).
CC   -!- FUNCTION: Putative Notch ligand involved in the mediation of Notch
CC       signaling. Plays an essential role during limb, craniofacial and
CC       thymic development. May be involved in myogenesis and in the
CC       development of peripheral and central nervous systems.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Found to be highest in fetal thymus,
CC       epidermis, foregut dorsal root ganglia and inner ear. In 2-weeK-
CC       old mice, abundant in heart, lung, thymus, skeletal muscle, brain
CC       and testis. Expression overlaps partially with Notch1 expression.
CC   -!- DEVELOPMENTAL STAGE: At 13 dpc, found in paravertebral vessels and
CC       dorsal root ganglia. At 14 dpc, in oropharyngeal epithelium,
CC       developing thymus and in the muscles of the tongue. By 15 dpc, in
CC       many tissues.
CC   -!- SIMILARITY: Contains 1 DSL domain.
CC   -!- SIMILARITY: Contains 16 EGF-like domains.
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DR   EMBL; AF038572; AAF16411.1; -; mRNA.
DR   EMBL; AF010137; AAC14010.1; -; mRNA.
DR   EMBL; Y14495; CAA74835.1; -; mRNA.
DR   IPI; IPI00136067; -.
DR   UniGene; Mm.186146; -.
DR   ProteinModelPortal; Q9QYE5; -.
DR   SMR; Q9QYE5; 198-574, 605-865, 936-973.
DR   STRING; Q9QYE5; -.
DR   PRIDE; Q9QYE5; -.
DR   Ensembl; ENSMUST00000075827; ENSMUSP00000075224; ENSMUSG00000002799.
DR   UCSC; uc007pfl.1; mouse.
DR   MGI; MGI:1098270; Jag2.
DR   GeneTree; ENSGT00600000084060; -.
DR   HOGENOM; HBG315533; -.
DR   HOVERGEN; HBG031645; -.
DR   InParanoid; Q9QYE5; -.
DR   OrthoDB; EOG45755R; -.
DR   ArrayExpress; Q9QYE5; -.
DR   Bgee; Q9QYE5; -.
DR   CleanEx; MM_JAG2; -.
DR   Genevestigator; Q9QYE5; -.
DR   GermOnline; ENSMUSG00000002799; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0008083; F:growth factor activity; ISS:UniProtKB.
DR   GO; GO:0009912; P:auditory receptor cell fate commitment; IMP:UniProtKB.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   GO; GO:0001709; P:cell fate determination; NAS:UniProtKB.
DR   GO; GO:0042492; P:gamma-delta T cell differentiation; IMP:UniProtKB.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:MGI.
DR   GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR   GO; GO:0042475; P:odontogenesis of dentine-containing tooth; IMP:MGI.
DR   GO; GO:0042981; P:regulation of apoptosis; IMP:MGI.
DR   GO; GO:0030155; P:regulation of cell adhesion; IMP:MGI.
DR   GO; GO:0042127; P:regulation of cell proliferation; ISS:UniProtKB.
DR   GO; GO:0003016; P:respiratory system process; IMP:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; NAS:UniProtKB.
DR   GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   GO; GO:0045061; P:thymic T cell selection; ISS:UniProtKB.
DR   InterPro; IPR001774; DSL.
DR   InterPro; IPR006209; EGF.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR001881; EGF_Ca-bd.
DR   InterPro; IPR013091; EGF_Ca-bd_2.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR011651; Notch_ligand_N.
DR   InterPro; IPR001007; VWF_C.
DR   Pfam; PF01414; DSL; 1.
DR   Pfam; PF00008; EGF; 9.
DR   Pfam; PF07974; EGF_2; 3.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF07657; MNNL; 1.
DR   SMART; SM00051; DSL; 1.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00179; EGF_CA; 9.
DR   SMART; SM00214; VWC; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 10.
DR   PROSITE; PS51051; DSL; 1.
DR   PROSITE; PS00022; EGF_1; 16.
DR   PROSITE; PS01186; EGF_2; 11.
DR   PROSITE; PS50026; EGF_3; 15.
DR   PROSITE; PS01187; EGF_CA; 7.
PE   2: Evidence at transcript level;
KW   Calcium; Developmental protein; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Membrane; Notch signaling pathway; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL        1     23       Potential.
FT   CHAIN        24   1247       Protein jagged-2.
FT                                /FTId=PRO_0000007630.
FT   TOPO_DOM     24   1082       Extracellular (Potential).
FT   TRANSMEM   1083   1103       Helical; (Potential).
FT   TOPO_DOM   1104   1247       Cytoplasmic (Potential).
FT   DOMAIN      196    240       DSL.
FT   DOMAIN      241    274       EGF-like 1.
FT   DOMAIN      275    305       EGF-like 2.
FT   DOMAIN      307    345       EGF-like 3.
FT   DOMAIN      347    383       EGF-like 4.
FT   DOMAIN      385    421       EGF-like 5; calcium-binding (Potential).
FT   DOMAIN      423    459       EGF-like 6; calcium-binding (Potential).
FT   DOMAIN      461    496       EGF-like 7; calcium-binding (Potential).
FT   DOMAIN      498    534       EGF-like 8.
FT   DOMAIN      536    572       EGF-like 9.
FT   DOMAIN      574    634       EGF-like 10; atypical.
FT   DOMAIN      636    672       EGF-like 11; calcium-binding (Potential).
FT   DOMAIN      674    710       EGF-like 12; calcium-binding (Potential).
FT   DOMAIN      712    748       EGF-like 13.
FT   DOMAIN      751    787       EGF-like 14.
FT   DOMAIN      789    825       EGF-like 15; calcium-binding (Potential).
FT   DOMAIN      827    863       EGF-like 16; calcium-binding (Potential).
FT   CARBOHYD    153    153       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    570    570       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    619    619       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    752    752       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1060   1060       N-linked (GlcNAc...) (Potential).
FT   DISULFID    245    256       By similarity.
FT   DISULFID    249    262       By similarity.
FT   DISULFID    264    273       By similarity.
FT   DISULFID    276    287       By similarity.
FT   DISULFID    282    293       By similarity.
FT   DISULFID    295    304       By similarity.
FT   DISULFID    311    323       By similarity.
FT   DISULFID    317    333       By similarity.
FT   DISULFID    335    344       By similarity.
FT   DISULFID    351    362       By similarity.
FT   DISULFID    356    371       By similarity.
FT   DISULFID    373    382       By similarity.
FT   DISULFID    389    400       By similarity.
FT   DISULFID    394    409       By similarity.
FT   DISULFID    411    420       By similarity.
FT   DISULFID    427    438       By similarity.
FT   DISULFID    432    447       By similarity.
FT   DISULFID    449    458       By similarity.
FT   DISULFID    465    475       By similarity.
FT   DISULFID    469    484       By similarity.
FT   DISULFID    486    495       By similarity.
FT   DISULFID    502    513       By similarity.
FT   DISULFID    507    522       By similarity.
FT   DISULFID    524    533       By similarity.
FT   DISULFID    540    551       By similarity.
FT   DISULFID    545    560       By similarity.
FT   DISULFID    562    571       By similarity.
FT   DISULFID    589    612       Potential.
FT   DISULFID    606    622       Potential.
FT   DISULFID    624    633       By similarity.
FT   DISULFID    640    651       By similarity.
FT   DISULFID    645    660       By similarity.
FT   DISULFID    662    671       By similarity.
FT   DISULFID    678    689       By similarity.
FT   DISULFID    683    698       By similarity.
FT   DISULFID    700    709       By similarity.
FT   DISULFID    716    727       By similarity.
FT   DISULFID    721    736       By similarity.
FT   DISULFID    738    747       By similarity.
FT   DISULFID    755    766       By similarity.
FT   DISULFID    760    775       By similarity.
FT   DISULFID    777    786       By similarity.
FT   DISULFID    793    804       By similarity.
FT   DISULFID    798    813       By similarity.
FT   DISULFID    815    824       By similarity.
FT   DISULFID    831    842       By similarity.
FT   DISULFID    836    851       By similarity.
FT   DISULFID    853    862       By similarity.
FT   CONFLICT    302    302       L -> M (in Ref. 2; AAC14010).
FT   CONFLICT    461    461       N -> T (in Ref. 2; AAC14010).
FT   CONFLICT    469    478       CQHGGTCKDL -> VSAWGHLQGP (in Ref. 2;
FT                                AAC14010).
FT   CONFLICT    492    492       G -> V (in Ref. 2; AAC14010).
FT   CONFLICT    546    546       L -> F (in Ref. 2; AAC14010).
FT   CONFLICT    549    549       A -> V (in Ref. 2; AAC14010).
FT   CONFLICT    735    738       RCAC -> PAR (in Ref. 3; CAA74835).
FT   CONFLICT    809    809       N -> H (in Ref. 2; AAC14010).
FT   CONFLICT    812    812       R -> A (in Ref. 2; AAC14010).
SQ   SEQUENCE   1247 AA;  134727 MW;  1D80C8626FAFAEEC CRC64;
     MRARGWGRLP RRLLLLLVLC VQATRPMGYF ELQLSALRNV NGELLSGACC DGDGRTTRAG
     GCGRDECDTY VRVCLKEYQA KVTPTGPCSY GYGATPVLGG NSFYLPPAGA AGDRARARSR
     TGGHQDPGLV VIPFQFAWPR SFTLIVEAWD WDNDTTPDEE LLIERVSHAG MINPEDRWKS
     LHFSGHVAHL ELQIRVRCDE NYYSATCNKF CRPRNDFFGH YTCDQYGNKA CMDGWMGKEC
     KEAVCKQGCN LLHGGCTVPG ECRCSYGWQG KFCDECVPYP GCVHGSCVEP WHCDCETNWG
     GLLCDKDLNY CGSHHPCVNG GTCINAEPDQ YLCACPDGYL GKNCERAEHA CASNPCANGG
     SCHEVPSGFE CHCPSGWSGP TCALDIDECA SNPCAAGGTC VDQVDGFECI CPEQWVGATC
     QLDANECEGK PCLNAFSCKN LIGGYYCDCL PGWKGINCQI NINDCHGQCQ HGGTCKDLVN
     GYQCVCPRGF GGRHCELEYD KCASSPCRRG GICEDLVDGF RCHCPRGLSG LHCEVDMDLC
     EPSPCLNGAR CYNLEGDYYC ACPEDFGGKN CSVPRDTCPG GACRVIDGCG FEAGSRARGV
     APSGICGPHG HCVSLPGGNF SCICDSGFTG TYCHENIDDC MGQPCRNGGT CIDEVDSFRC
     FCPSGWEGEL CDINPNDCLP DPCHSRGRCY DLVNDFYCAC DDGWKGKTCH SREFQCDAYT
     CSNGGTCYDS GDTFRCACPP GWKGSTCTIA KNSSCVPNPC VNGGTCVGSG DSFSCICRDG
     WEGRTCTHNT NDCNPLPCYN GGICVDGVNW FRCECAPGFA GPDCRINIDE CQSSPCAYGA
     TCVDEINGYR CSCPPGRSGP RCQEVVIFTR PCWSRGMSFP HGSSWMEDCN SCRCLDGHRD
     CSKVWCGWKP CLLSGQPSDP SAQCPPGQQC QEKAVGQCLQ PPCENWGECT AEEPLPPSTP
     CQPRSSHLDN NCARLTLRFN RDQVPQGTTV GAICSGIRAL PATRAAAHDR LLLLLCDRAS
     SGASAVEVAM SFSPARDLPD SSLIQSTAHA IVAAITQRGN SSLLLAVTEV KVETVVMGGS
     STGLLVPVLC SVFSVLWLAC VVICVWWTRK RRKERERSRL PRDESTNNQW APLNPIRNPI
     ERPGGSGLGT GGHKDILYQC KNFTPPPRRA GEALPGPAGH GAGGEDEEDE ELSRGDGDSP
     EAEKFISHKF TKDPSCSLGR PACWAPGPKV DNRAVRSTKD VRRAGRE
//
ID   GOGA5_MOUSE             Reviewed;         729 AA.
AC   Q9QYE6; O88317; Q3TGE7; Q3U6S5; Q3UUF9;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   03-JUL-2003, sequence version 2.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Golgin subfamily A member 5;
DE   AltName: Full=Golgin-84;
DE   AltName: Full=Protein Ret-II;
DE   AltName: Full=Protein Sumiko;
GN   Name=Golga5; Synonyms=Retii;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=B-cell lymphoma;
RA   Ku P.T., You M.J., Cottam M.K., Bose H.R. Jr.;
RT   "Suppression of anti-immunoglobulin-induced apoptosis in B lymphoma
RT   cells by a novel nuclear protein.";
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Snider J., Sano H., Ohta M.;
RT   "Unknown, 5' similar to RET-II mRNA.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Kidney, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Involved in maintaining Golgi structure. Stimulates the
CC       formation of Golgi stacks and ribbons. Involved in intra-Golgi
CC       retrograde transport (By similarity).
CC   -!- SUBUNIT: Homodimer. Interacts with RAB1A that has been activated
CC       by GTP-binding. Interacts with isoform CASP of CUX1 (By
CC       similarity).
CC   -!- INTERACTION:
CC       Q99N72:Mcf2; NbExp=2; IntAct=EBI-644242, EBI-641874;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Single-pass type
CC       IV membrane protein (By similarity). Note=Found throughout the
CC       Golgi (By similarity).
CC   -!- PTM: Highly phosphorylated during mitosis. Phosphorylation is
CC       barely detectable during interphase (By similarity).
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DR   EMBL; AF026274; AAF21628.1; -; mRNA.
DR   EMBL; AB016784; BAA33010.1; -; mRNA.
DR   EMBL; AK138455; BAE23668.1; -; mRNA.
DR   EMBL; AK152533; BAE31289.1; -; mRNA.
DR   EMBL; AK153010; BAE31649.1; -; mRNA.
DR   EMBL; AK168765; BAE40601.1; -; mRNA.
DR   EMBL; BC016883; AAH16883.1; -; mRNA.
DR   EMBL; BC086782; AAH86782.1; -; mRNA.
DR   IPI; IPI00316682; -.
DR   RefSeq; NP_001185933.1; NM_001199004.1.
DR   RefSeq; NP_038775.1; NM_013747.4.
DR   UniGene; Mm.273370; -.
DR   ProteinModelPortal; Q9QYE6; -.
DR   IntAct; Q9QYE6; 3.
DR   STRING; Q9QYE6; -.
DR   PhosphoSite; Q9QYE6; -.
DR   PRIDE; Q9QYE6; -.
DR   Ensembl; ENSMUST00000021609; ENSMUSP00000021609; ENSMUSG00000021192.
DR   GeneID; 27277; -.
DR   KEGG; mmu:27277; -.
DR   UCSC; uc007oug.1; mouse.
DR   CTD; 27277; -.
DR   MGI; MGI:1351475; Golga5.
DR   eggNOG; roNOG14247; -.
DR   GeneTree; ENSGT00390000018470; -.
DR   HOGENOM; HBG282289; -.
DR   HOVERGEN; HBG051755; -.
DR   InParanoid; Q9QYE6; -.
DR   OMA; NRVDQGA; -.
DR   OrthoDB; EOG4894M3; -.
DR   NextBio; 305188; -.
DR   ArrayExpress; Q9QYE6; -.
DR   Bgee; Q9QYE6; -.
DR   CleanEx; MM_GOLGA5; -.
DR   Genevestigator; Q9QYE6; -.
DR   GermOnline; ENSMUSG00000021192; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR   InterPro; IPR019177; Golgin_subfamily_A_member_5.
DR   Pfam; PF09787; Golgin_A5; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Golgi apparatus; Membrane; Methylation; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    729       Golgin subfamily A member 5.
FT                                /FTId=PRO_0000190062.
FT   TOPO_DOM      1    696       Cytoplasmic (Potential).
FT   TRANSMEM    697    717       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   TOPO_DOM    718    729       Lumenal (Potential).
FT   COILED      215    629       Potential.
FT   COMPBIAS    150    223       Ser-rich.
FT   MOD_RES      27     27       Omega-N-methylated arginine (By
FT                                similarity).
FT   MOD_RES      42     42       Phosphotyrosine (By similarity).
FT   MOD_RES      54     54       Phosphotyrosine (By similarity).
FT   MOD_RES      89     89       Omega-N-methylated arginine (By
FT                                similarity).
FT   MOD_RES     116    116       Phosphoserine.
FT   CONFLICT     93     93       D -> N (in Ref. 1; AAF21628).
FT   CONFLICT    145    145       G -> D (in Ref. 1; AAF21628).
FT   CONFLICT    224    224       N -> D (in Ref. 3; BAE31649/BAE31289).
FT   CONFLICT    312    312       V -> M (in Ref. 3; BAE23668).
FT   CONFLICT    417    417       A -> S (in Ref. 1; AAF21628).
FT   CONFLICT    463    463       S -> R (in Ref. 3; BAE40601).
FT   CONFLICT    640    640       S -> P (in Ref. 1; AAF21628).
FT   CONFLICT    669    669       G -> R (in Ref. 3; BAE31649/BAE31289).
SQ   SEQUENCE   729 AA;  82368 MW;  8418BE8E6E4865E1 CRC64;
     MSWFADLAGR AEDLLNRVDQ GAATALRKEN TSNIFYSKNT DYPELQQQNT DSNYQTGQKA
     NYISSAADNI RHQKATILAG TANVKVGSRT VGDATHPTEH ASAPRPSSQF VRRKKSEPDD
     ELLFDFLNSS QKEPTGRVEV KKEKGRAPVS PSSPSGVSSV NTSVTTTKAM GGNAGSQSPG
     VNSSDSVPEV HKEPSEESTA PSATSEEHSS TPSDGSSRSQ ELSNLRLENQ LLRNEVQSLN
     QEMASLLQRS KETQEELNKA RVRVEKWNVD NSKSDRITRE LRAQVDDLTE AVAAKDSQLA
     VLKVRLQEAD QVLSSRTEAL EALRSEKSRI MQDHKEGSSL QNQALQTLQE RLHEADATLK
     REQESYKQMQ SEFAARLNKM EVDRQNLAEA VTLAERKYSE EKKKVDELQQ QVKLHRASLE
     SAKQELVDYK QKATRILQSK EKLINSLKEG SSFEGLESST ASSMELEELR HEKEMQKEEI
     QKLMGQMHQL RSELQDMEAQ QVSEAESARE QLQDLQDQIA KQRTSKQELE TELERMKQEF
     RYMEEDLHRT KNTLQSRIKD REEEIQKLRN QLTNKTLSNS SQSELESRLH QLTETLIQKQ
     TMLESLSTEK NSLVFQLERL EQQVHSASSG PNSGSAINMS GVDSGEGTRL RNVPVLFNDT
     ETNLAGMYGK VRKAASSIDQ FSIRLGIFLR RYPIARVFVI IYMALLHLWV MIVLLTYSPE
     MHHDQPYGK
//
ID   NDRG3_MOUSE             Reviewed;         375 AA.
AC   Q9QYF9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Protein NDRG3;
DE   AltName: Full=Protein Ndr3;
GN   Name=Ndrg3; Synonyms=Ndr3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RX   MEDLINE=20050077; PubMed=10581191; DOI=10.1006/bbrc.1999.1780;
RA   Okuda T., Kondoh H.;
RT   "Identification of new genes ndr2 and ndr3 which are related to
RT   Ndr1/RTP/Drg1 but show distinct tissue specificity and response to N-
RT   myc.";
RL   Biochem. Biophys. Res. Commun. 266:208-215(1999).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331; SER-334 AND
RP   SER-335, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- TISSUE SPECIFICITY: Thymus, nervous system, gut and kidney.
CC   -!- DEVELOPMENTAL STAGE: Its expression is already significant at 9.5
CC       dpc, covering the entire embryo except the heart, and it shows
CC       only a slight increase in later developmental stages.
CC   -!- SIMILARITY: Belongs to the NDRG family.
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DR   EMBL; AB033922; BAA85883.1; -; mRNA.
DR   IPI; IPI00136107; -.
DR   RefSeq; NP_038893.1; NM_013865.2.
DR   UniGene; Mm.279256; -.
DR   ProteinModelPortal; Q9QYF9; -.
DR   SMR; Q9QYF9; 33-312.
DR   STRING; Q9QYF9; -.
DR   PhosphoSite; Q9QYF9; -.
DR   PRIDE; Q9QYF9; -.
DR   Ensembl; ENSMUST00000072298; ENSMUSP00000072144; ENSMUSG00000027634.
DR   GeneID; 29812; -.
DR   KEGG; mmu:29812; -.
DR   UCSC; uc008nof.1; mouse.
DR   CTD; 29812; -.
DR   MGI; MGI:1352499; Ndrg3.
DR   GeneTree; ENSGT00390000001874; -.
DR   HOVERGEN; HBG052591; -.
DR   OrthoDB; EOG4GMTXB; -.
DR   NextBio; 306966; -.
DR   ArrayExpress; Q9QYF9; -.
DR   Bgee; Q9QYF9; -.
DR   CleanEx; MM_NDRG3; -.
DR   Genevestigator; Q9QYF9; -.
DR   GermOnline; ENSMUSG00000027634; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   InterPro; IPR004142; Ndr.
DR   PANTHER; PTHR11034; Ndr; 1.
DR   Pfam; PF03096; Ndr; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein.
FT   CHAIN         1    375       Protein NDRG3.
FT                                /FTId=PRO_0000159578.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     322    322       Phosphothreonine (By similarity).
FT   MOD_RES     331    331       Phosphoserine.
FT   MOD_RES     332    332       Phosphothreonine (By similarity).
FT   MOD_RES     334    334       Phosphoserine.
FT   MOD_RES     335    335       Phosphoserine.
FT   MOD_RES     352    352       Phosphoserine (By similarity).
FT   MOD_RES     361    361       Phosphoserine (By similarity).
FT   MOD_RES     374    374       Phosphoserine (By similarity).
SQ   SEQUENCE   375 AA;  41555 MW;  B33D3CC3E816AEA1 CRC64;
     MDELQDVQLT EIKPLLNDKN GTRNFQDFDC QEHDIETPHG MVHVTIRGLP KGNRPVILTY
     HDIGLNHKSC FNTFFNFEDM QEITQHFAVC HVDAPGQQEA APSFPTGYQY PTMDELAEML
     PPVLTHLSMK SIIGIGVGAG AYILSRFALN HPELVEGLVL INIDPCAKGW IDWAASKLSG
     FTTNIVDIIL AHHFGQEELQ ANLDLIQTYR LHIAQDINQE NLQLFLGSYN GRRDLEIERP
     ILGQNDNRLK TLKCSTLLVV GDNSPAVEAV VECNSRLDPI NTTLLKMADC GGLPQVVQPG
     KLTEAFKYFL QGMGYIPSAS MTRLARSRTH STSSSIGSGE SPFSRSVTSN QSDGTQESCE
     SPDVLDRHQT MEVSC
//
ID   NDRG2_MOUSE             Reviewed;         371 AA.
AC   Q9QYG0; Q3TI48; Q3TY42; Q3U3T5; Q69ZN2; Q8C661;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Protein NDRG2;
DE   AltName: Full=Protein Ndr2;
GN   Name=Ndrg2; Synonyms=Kiaa1248, Ndr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Embryo;
RX   MEDLINE=20050077; PubMed=10581191; DOI=10.1006/bbrc.1999.1780;
RA   Okuda T., Kondoh H.;
RT   "Identification of new genes ndr2 and ndr3 which are related to
RT   Ndr1/RTP/Drg1 but show distinct tissue specificity and response to N-
RT   myc.";
RL   Biochem. Biophys. Res. Commun. 266:208-215(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, DBA/2, and NOD; TISSUE=Head, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 62-84; 155-176 AND 278-287, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 64-371.
RC   TISSUE=Thymus;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [6]
RP   PHOSPHORYLATION AT THR-330; SER-332; THR-348 AND SER-350, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=15461589; DOI=10.1042/BJ20041057;
RA   Murray J.T., Campbell D.G., Morrice N., Auld G.C., Shpiro N.,
RA   Marquez R., Peggie M., Bain J., Bloomberg G.B., Grahammer F., Lang F.,
RA   Wulff P., Kuhl D., Cohen P.;
RT   "Exploitation of KESTREL to identify NDRG family members as
RT   physiological substrates for SGK1 and GSK3.";
RL   Biochem. J. 384:477-488(2004).
RN   [7]
RP   PHOSPHORYLATION AT SER-332 AND THR-348, AND SUBCELLULAR LOCATION.
RX   PubMed=14985363; DOI=10.1074/jbc.M401504200;
RA   Burchfield J.G., Lennard A.J., Narasimhan S., Hughes W.E.,
RA   Wasinger V.C., Corthals G.L., Okuda T., Kondoh H., Biden T.J.,
RA   Schmitz-Peiffer C.;
RT   "Akt mediates insulin-stimulated phosphorylation of Ndrg2: evidence
RT   for cross-talk with protein kinase C theta.";
RL   J. Biol. Chem. 279:18623-18632(2004).
RN   [8]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=15207261; DOI=10.1016/j.nbd.2004.01.003;
RA   Mitchelmore C., Buechmann-Moller S., Rask L., West M.J.,
RA   Troncoso J.C., Jensen N.A.;
RT   "NDRG2: a novel Alzheimer's disease associated protein.";
RL   Neurobiol. Dis. 16:48-58(2004).
RN   [9]
RP   SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=16520977; DOI=10.1007/s00441-005-0137-5;
RA   Hu X.-L., Liu X.-P., Deng Y.-C., Lin S.-X., Wu L., Zhang J.,
RA   Wang L.-F., Wang X.-B., Li X., Shen L., Zhang Y.-Q., Yao L.-B.;
RT   "Expression analysis of the NDRG2 gene in mouse embryonic and adult
RT   tissues.";
RL   Cell Tissue Res. 325:67-76(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332 AND SER-352, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328; THR-330; SER-332;
RP   THR-334; SER-335; SER-338; SER-342; SER-344; THR-348; SER-350;
RP   SER-352; SER-353; SER-355 AND THR-357, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326; SER-328; THR-330;
RP   SER-332; SER-346 AND THR-348, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332 AND SER-338, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May be involved in dendritic cell and neuron
CC       differentiation (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9QYG0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9QYG0-2; Sequence=VSP_019009;
CC   -!- TISSUE SPECIFICITY: Present in brain, heart, liver, skeletal
CC       muscle, kidney, adrenal gland, ovary and uterus (at protein
CC       level).
CC   -!- DEVELOPMENTAL STAGE: Expression is restricted to the developing
CC       heart at the stage of 9.5 dpc, and increases after 11.5 dpc as
CC       development of tissues and organs proceeds. Present in many
CC       developing tissues including heart, brain, lung, liver, gut,
CC       kidney, skeletal muscle, cartilage and epidermis (at protein
CC       level).
CC   -!- SIMILARITY: Belongs to the NDRG family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AB033921; BAA85882.1; -; mRNA.
DR   EMBL; AK076514; BAC36373.1; -; mRNA.
DR   EMBL; AK154597; BAE32700.1; -; mRNA.
DR   EMBL; AK158900; BAE34721.1; -; mRNA.
DR   EMBL; AK168011; BAE39998.1; -; mRNA.
DR   EMBL; BC012963; AAH12963.1; -; mRNA.
DR   EMBL; AK173136; BAD32414.1; -; mRNA.
DR   IPI; IPI00136134; -.
DR   IPI; IPI00759847; -.
DR   RefSeq; NP_001139431.1; NM_001145959.1.
DR   RefSeq; NP_038892.1; NM_013864.2.
DR   UniGene; Mm.26722; -.
DR   PDB; 2QMQ; X-ray; 1.70 A; A=40-313.
DR   PDBsum; 2QMQ; -.
DR   ProteinModelPortal; Q9QYG0; -.
DR   SMR; Q9QYG0; 39-313.
DR   STRING; Q9QYG0; -.
DR   PhosphoSite; Q9QYG0; -.
DR   PRIDE; Q9QYG0; -.
DR   Ensembl; ENSMUST00000004673; ENSMUSP00000004673; ENSMUSG00000004558.
DR   Ensembl; ENSMUST00000111632; ENSMUSP00000107259; ENSMUSG00000004558.
DR   GeneID; 29811; -.
DR   KEGG; mmu:29811; -.
DR   UCSC; uc007tnk.1; mouse.
DR   UCSC; uc007tnl.1; mouse.
DR   CTD; 29811; -.
DR   MGI; MGI:1352498; Ndrg2.
DR   eggNOG; roNOG12450; -.
DR   GeneTree; ENSGT00390000001874; -.
DR   HOGENOM; HBG445737; -.
DR   HOVERGEN; HBG052591; -.
DR   InParanoid; Q9QYG0; -.
DR   OMA; QFGDMQE; -.
DR   OrthoDB; EOG4FBHTF; -.
DR   PhylomeDB; Q9QYG0; -.
DR   NextBio; 306962; -.
DR   ArrayExpress; Q9QYG0; -.
DR   Bgee; Q9QYG0; -.
DR   CleanEx; MM_NDRG2; -.
DR   Genevestigator; Q9QYG0; -.
DR   GermOnline; ENSMUSG00000004558; Mus musculus.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   InterPro; IPR004142; Ndr.
DR   PANTHER; PTHR11034; Ndr; 1.
DR   Pfam; PF03096; Ndr; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW   Developmental protein; Differentiation; Direct protein sequencing;
KW   Neurogenesis; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    371       Protein NDRG2.
FT                                /FTId=PRO_0000159576.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     326    326       Phosphoserine.
FT   MOD_RES     328    328       Phosphoserine.
FT   MOD_RES     330    330       Phosphothreonine; by SGK.
FT   MOD_RES     332    332       Phosphoserine; by PKC/PRKCQ or SGK.
FT   MOD_RES     334    334       Phosphothreonine.
FT   MOD_RES     335    335       Phosphoserine.
FT   MOD_RES     338    338       Phosphoserine.
FT   MOD_RES     342    342       Phosphoserine.
FT   MOD_RES     344    344       Phosphoserine.
FT   MOD_RES     346    346       Phosphoserine.
FT   MOD_RES     348    348       Phosphothreonine; by PKB/AKT1 or SGK.
FT   MOD_RES     350    350       Phosphoserine.
FT   MOD_RES     352    352       Phosphoserine.
FT   MOD_RES     353    353       Phosphoserine.
FT   MOD_RES     355    355       Phosphoserine.
FT   MOD_RES     357    357       Phosphothreonine.
FT   VAR_SEQ      26     39       Missing (in isoform 2).
FT                                /FTId=VSP_019009.
FT   CONFLICT    253    253       L -> P (in Ref. 2; BAE39998).
FT   CONFLICT    347    347       R -> S (in Ref. 2; BAE39998).
FT   STRAND       40     45
FT   STRAND       48     56
FT   STRAND       64     68
FT   HELIX        75     83
FT   HELIX        86     92
FT   STRAND       97    101
FT   TURN        103    105
FT   HELIX       121    126
FT   HELIX       128    135
FT   STRAND      140    145
FT   HELIX       147    158
FT   HELIX       160    162
FT   STRAND      163    170
FT   HELIX       178    188
FT   HELIX       193    201
FT   HELIX       204    208
FT   HELIX       212    222
FT   HELIX       227    238
FT   STRAND      245    247
FT   STRAND      257    262
FT   HELIX       268    277
FT   HELIX       280    282
FT   STRAND      283    288
FT   HELIX       295    298
FT   HELIX       300    311
SQ   SEQUENCE   371 AA;  40789 MW;  A5237C04278197B2 CRC64;
     MAELQEVQIT EEKPLLPGQT PETAKEAELA ARILLDQGQT HSVETPYGSV TFTVYGTPKP
     KRPAIFTYHD VGLNYKSCFQ PLFRFGDMQE IIQNFVRVHV DAPGMEEGAP VFPLGYQYPS
     LDQLADMIPC ILQYLNFSTI IGVGVGAGAY ILSRYALNHP DTVEGLVLIN IDPNAKGWMD
     WAAHKLTGLT SSIPDMILGH LFSQEELSGN SELIQKYRGI IQHAPNLENI ELYWNSYNNR
     RDLNFERGGE TTLKCPVMLV VGDQAPHEDA VVECNSKLDP TQTSFLKMAD SGGQPQLTQP
     GKLTEAFKYF LQGMGYMASS CMTRLSRSRT ASLTSAASID GSRSRSRTLS QSSESGTLPS
     GPPGHTMEVS C
//
ID   DNJA2_MOUSE             Reviewed;         412 AA.
AC   Q9QYJ0;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=DnaJ homolog subfamily A member 2;
DE   AltName: Full=mDj3;
DE   Flags: Precursor;
GN   Name=Dnaja2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=21023480; PubMed=11147971;
RA   Ohtsuka K., Hata M.;
RT   "Mammalian HSP40/DNAJ homologs: cloning of novel cDNAs and a proposal
RT   for their classification and nomenclature.";
RL   Cell Stress Chaperones 5:98-112(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 140-152; 231-255 AND 273-287, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
CC   -!- FUNCTION: Co-chaperone of Hsc70 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor (Potential).
CC   -!- SIMILARITY: Contains 1 CR-type zinc finger.
CC   -!- SIMILARITY: Contains 1 J domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB028853; BAA88301.1; -; mRNA.
DR   EMBL; AK077672; BAC36946.1; -; mRNA.
DR   EMBL; AK083208; BAC38809.1; -; mRNA.
DR   EMBL; BC003420; AAH03420.1; -; mRNA.
DR   IPI; IPI00136251; -.
DR   RefSeq; NP_062768.1; NM_019794.4.
DR   UniGene; Mm.279692; -.
DR   ProteinModelPortal; Q9QYJ0; -.
DR   SMR; Q9QYJ0; 6-70, 110-379.
DR   STRING; Q9QYJ0; -.
DR   PhosphoSite; Q9QYJ0; -.
DR   PRIDE; Q9QYJ0; -.
DR   Ensembl; ENSMUST00000034138; ENSMUSP00000034138; ENSMUSG00000031701.
DR   GeneID; 56445; -.
DR   KEGG; mmu:56445; -.
DR   UCSC; uc009mqa.1; mouse.
DR   CTD; 56445; -.
DR   MGI; MGI:1931882; Dnaja2.
DR   GeneTree; ENSGT00490000043321; -.
DR   HOGENOM; HBG635315; -.
DR   HOVERGEN; HBG066727; -.
DR   InParanoid; Q9QYJ0; -.
DR   OMA; NGQGGKS; -.
DR   OrthoDB; EOG4T783H; -.
DR   PhylomeDB; Q9QYJ0; -.
DR   NextBio; 312650; -.
DR   ArrayExpress; Q9QYJ0; -.
DR   Bgee; Q9QYJ0; -.
DR   CleanEx; MM_DNAJA2; -.
DR   Genevestigator; Q9QYJ0; -.
DR   GermOnline; ENSMUSG00000031701; Mus musculus.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:InterPro.
DR   GO; GO:0009408; P:response to heat; IEA:InterPro.
DR   InterPro; IPR012724; DnaJ.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_N.
DR   InterPro; IPR018253; Heat_shock_DnaJ_CS.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR003095; Hsp_DnaJ.
DR   InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR   Gene3D; G3DSA:1.10.287.110; DnaJ_N; 1.
DR   Gene3D; G3DSA:2.10.230.10; HSP_DnaJ_cys-rich; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; DnaJ_N; 1.
DR   SUPFAM; SSF49493; HSP40_DnaJ_pep; 2.
DR   SUPFAM; SSF57938; HSP_DnaJ_cys-rich; 1.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51188; ZF_CR; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Direct protein sequencing; Lipoprotein; Membrane;
KW   Metal-binding; Methylation; Phosphoprotein; Prenylation; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    409       DnaJ homolog subfamily A member 2.
FT                                /FTId=PRO_0000071012.
FT   PROPEP      410    412       Removed in mature form (By similarity).
FT                                /FTId=PRO_0000396758.
FT   DOMAIN        8     70       J.
FT   REPEAT      143    150       CXXCXGXG motif.
FT   REPEAT      159    166       CXXCXGXG motif.
FT   REPEAT      186    193       CXXCXGXG motif.
FT   REPEAT      202    209       CXXCXGXG motif.
FT   ZN_FING     130    214       CR-type.
FT   METAL       143    143       Zinc 1 (By similarity).
FT   METAL       146    146       Zinc 1 (By similarity).
FT   METAL       159    159       Zinc 2 (By similarity).
FT   METAL       162    162       Zinc 2 (By similarity).
FT   METAL       186    186       Zinc 2 (By similarity).
FT   METAL       189    189       Zinc 2 (By similarity).
FT   METAL       202    202       Zinc 1 (By similarity).
FT   METAL       205    205       Zinc 1 (By similarity).
FT   MOD_RES      78     78       Phosphoserine (By similarity).
FT   MOD_RES     409    409       Cysteine methyl ester (By similarity).
FT   LIPID       409    409       S-farnesyl cysteine (By similarity).
SQ   SEQUENCE   412 AA;  45746 MW;  98130EC0925CB42E CRC64;
     MANVADTKLY DILGVPPGAS ENELKKAYRK LAKEYHPDKN PNAGDKFKEI SFAYEVLSNP
     EKRELYDRYG EQGLREGSGG GGGMDDIFSH IFGGGLFGFM GNQSRSRNGR RRGEDMMHPL
     KVSLEDLYNG KTTKLQLSKN VLCSACSGQG GKSGAVQKCS ACRGRGVRIM IRQLAPGMVQ
     QMQSVCSDCN GEGEVINEKD RCKKCEGKKV IKEVKILEVH VDKGMKHGQR ITFTGEADQA
     PGVEPGDIVL LLQEKEHEVF QRDGNDLHMT YKIGLVEALC GFQFTFKHLD ARQIVVKYPP
     GKVIEPGCVR VVRGEGMPQY RNPFEKGDLY IKFDVQFPEN NWINPDKLSE LEDLLPSRPE
     VPNVIGETEE VELQEFDSTR GSGGGQRREA YNDSSDEESS SHHGPGVQCA HQ
//
ID   RNF11_MOUSE             Reviewed;         154 AA.
AC   Q9QYK7; B1AU36; B1AU37; Q9EQI1;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=RING finger protein 11;
DE   AltName: Full=NEDD4 WW domain-binding protein 2;
DE   AltName: Full=Sid 1669;
GN   Name=Rnf11; Synonyms=N4wbp2, Sid1669;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20135600; PubMed=10673045; DOI=10.1016/S0167-4781(99)00190-6;
RA   Seki N., Hattori A., Hayashi A., Kozuma S., Sasaki M., Suzuki Y.,
RA   Sugano S., Muramatsu M., Saito T.;
RT   "Cloning and expression profile of mouse and human genes, Rnf11/RNF11,
RT   encoding a novel RING-H2 finger protein.";
RL   Biochim. Biophys. Acta 1489:421-427(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], DOMAIN, INTERACTION WITH NEDD4, AND
RP   MUTAGENESIS OF TYR-40.
RX   MEDLINE=20498735; PubMed=11042109; DOI=10.1042/0264-6021:3510557;
RA   Jolliffe C.N., Harvey K.F., Haines B.P., Parasivam G., Kumar S.;
RT   "Identification of multiple proteins expressed in murine embryos as
RT   binding partners for the WW domains of the ubiquitin-protein ligase
RT   Nedd4.";
RL   Biochem. J. 351:557-565(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   INTERACTION WITH TAX1BP1; TNFAIP3 AND RIPK1.
RX   PubMed=19131965; DOI=10.1038/emboj.2008.285;
RA   Shembade N., Parvatiyar K., Harhaj N.S., Harhaj E.W.;
RT   "The ubiquitin-editing enzyme A20 requires RNF11 to downregulate NF-
RT   kappaB signalling.";
RL   EMBO J. 28:513-522(2009).
CC   -!- FUNCTION: Essential component of a ubiquitin-editing protein
CC       complex, comprising also TNFAIP3, ITCH and TAX1BP1, that ensures
CC       the transient nature of inflammatory signaling pathways. Promotes
CC       the association of TNFAIP3 to RIPK1 after TNF stimulation. TNFAIP3
CC       deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and
CC       catalyzes the formation of 'Lys-48'-polyubiquitin chains. This
CC       leads to RIPK1 proteosomal degradation and consequently
CC       termination of the TNF- or LPS-mediated activation of NF-kappa-B.
CC       Recruits STAMBP to the E3 ubiquitin-ligase SMURF2 for
CC       ubiquitination, leading to its degradation by the 26S proteasome.
CC   -!- SUBUNIT: Interacts (when phosphorylated) with 14-3-3. Interacts
CC       with the E3 ubiquitin-ligases NEDD4, ITCH, SMURF2 and WWP1 (By
CC       similarity). Also interacts with the E2 ubiquitin-conjugating
CC       enzymes UBE2D1 and UBE2N, but neither with CDC34, nor with UBE2L3.
CC       Interacts with ZNF350, EPS15 and STAMBP (By similarity). After TNF
CC       stimulation, interacts with TAX1BP1, TNFAIP3 and RIPK1; these
CC       interaction are transient and they are lost after 1 hour of
CC       stimulation with TNF.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly
CC       cytoplasmic, when unphosphorylated, and nuclear, when
CC       phosphorylated by PKB/AKT1 (By similarity).
CC   -!- DOMAIN: The WW-binding motif mediates interaction with NEDD4.
CC   -!- PTM: Ubiquitinated in the presence of SMURF2 and UBE2D1, as well
CC       as WWP1 (By similarity).
CC   -!- PTM: Phosphorylation by PKB/AKT1 may accelerate degradation by the
CC       proteasome (By similarity).
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG44245.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB024427; BAA84682.1; -; mRNA.
DR   EMBL; AF220206; AAG44245.1; ALT_INIT; mRNA.
DR   EMBL; AL669905; CAM13662.1; -; Genomic_DNA.
DR   EMBL; AL669905; CAM13663.1; -; Genomic_DNA.
DR   EMBL; CH466527; EDL30703.1; -; Genomic_DNA.
DR   EMBL; CH466527; EDL30704.1; -; Genomic_DNA.
DR   EMBL; CH466527; EDL30705.1; -; Genomic_DNA.
DR   EMBL; BC010299; AAH10299.1; -; mRNA.
DR   EMBL; BC028255; AAH28255.1; -; mRNA.
DR   IPI; IPI00136284; -.
DR   RefSeq; NP_038904.1; NM_013876.3.
DR   UniGene; Mm.172605; -.
DR   UniGene; Mm.392580; -.
DR   UniGene; Mm.456388; -.
DR   ProteinModelPortal; Q9QYK7; -.
DR   SMR; Q9QYK7; 94-144.
DR   MINT; MINT-147742; -.
DR   STRING; Q9QYK7; -.
DR   PhosphoSite; Q9QYK7; -.
DR   PRIDE; Q9QYK7; -.
DR   Ensembl; ENSMUST00000030284; ENSMUSP00000030284; ENSMUSG00000028557.
DR   Ensembl; ENSMUST00000064167; ENSMUSP00000063798; ENSMUSG00000028557.
DR   GeneID; 29864; -.
DR   KEGG; mmu:29864; -.
DR   UCSC; uc008ucm.1; mouse.
DR   CTD; 29864; -.
DR   MGI; MGI:1352759; Rnf11.
DR   eggNOG; roNOG15621; -.
DR   GeneTree; ENSGT00530000063084; -.
DR   HOGENOM; HBG379842; -.
DR   HOVERGEN; HBG058444; -.
DR   InParanoid; Q9QYK7; -.
DR   OMA; SDRASYG; -.
DR   OrthoDB; EOG41VK45; -.
DR   PhylomeDB; Q9QYK7; -.
DR   NextBio; 307078; -.
DR   ArrayExpress; Q9QYK7; -.
DR   Bgee; Q9QYK7; -.
DR   CleanEx; MM_RNF11; -.
DR   Genevestigator; Q9QYK7; -.
DR   GermOnline; ENSMUSG00000028557; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IPI:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Metal-binding; Nucleus; Phosphoprotein; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    154       RING finger protein 11.
FT                                /FTId=PRO_0000056051.
FT   ZN_FING      99    140       RING-type.
FT   MOTIF        37     40       WW-binding.
FT   MOD_RES     135    135       Phosphothreonine; by PKB/AKT1 (By
FT                                similarity).
FT   MUTAGEN      40     40       Y->A: Abolishes interaction with NEDD4.
SQ   SEQUENCE   154 AA;  17458 MW;  EF192AB0C2D4BF87 CRC64;
     MGNCLKSPTS DDISLLHESQ SDRASFGEGT EPDQEPPPPY QEQVPVPIYH PTPSQTRLAT
     QLTEEEQIRI AQRIGLIQHL PKGVYDPGRD GSEKKIRECV ICMMDFVYGD PIRFLPCMHI
     YHLDCIDDWL MRSFTCPSCM EPVDAALLSS YETN
//
ID   KCC1B_MOUSE             Reviewed;         343 AA.
AC   Q9QYK9; Q80W07;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Calcium/calmodulin-dependent protein kinase type 1B;
DE            EC=2.7.11.17;
DE   AltName: Full=CaM kinase I beta;
DE            Short=CaM kinase IB;
DE            Short=CaM-KI beta;
DE            Short=CaMKI-beta;
DE   AltName: Full=Pregnancy up-regulated non-ubiquitously-expressed CaM kinase homolog;
GN   Name=Pnck;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND DEVELOPMENTAL STAGE.
RX   PubMed=10537072;
RA   Ueda T., Sakagami H., Abe K., Oishi I., Maruo A., Kondo H.,
RA   Terashima T., Ichihashi M., Yamamura H., Minami Y.;
RT   "Distribution and intracellular localization of a mouse homologue of
RT   Ca2+/calmodulin-dependent protein kinase Ibeta2 in the nervous
RT   system.";
RL   J. Neurochem. 73:2119-2129(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   TISSUE=Brain;
RX   MEDLINE=20139438; PubMed=10673339; DOI=10.1006/geno.1999.6091;
RA   Gardner H.P., Rajan J.V., Ha S.I., Copeland N.G., Gilbert D.J.,
RA   Jenkins N.A., Marquis S.T., Chodosh L.A.;
RT   "Cloning, characterization, and chromosomal localization of Pnck, a
RT   Ca2+/calmodulin-pependent protein kinase.";
RL   Genomics 63:279-288(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Brain, and Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Calcium/calmodulin-dependent protein kinase belonging to
CC       a proposed calcium-triggered signaling cascade. In vitro
CC       phosphorylates CREB1 and SYN1/synapsin I. Phosphorylates and
CC       activates CAMK1 (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Activated by Ca(2+)/calmodulin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- TISSUE SPECIFICITY: Expressed at highest levels in adult brain,
CC       and expressed in embryo. In the adult brain detected at high
CC       levels in the anterior olfactory nuclei, piriform cortex, septal
CC       nuclei, bed nuclei of the stria terminalis, hippocampal pyramidal
CC       cells, dentate granule cells, amygdala, hypothalamic nuclei,
CC       parabrachial nucleus, and nucleus of the solitary tract. Expressed
CC       at lower levels in adult ovary and heart and at very low levels in
CC       testis, lung and muscle.
CC   -!- DEVELOPMENTAL STAGE: During embryogenesis detected at E10 and
CC       expression gradually increases thereafter. Expressed mainly in the
CC       nervous system, including brain, spinal cord, trigeminal ganglion,
CC       and retina. Within the CNS detected in the mantle zone, but not in
CC       the ventricular zone. Detected at postnatal day 23 with highest
CC       levels in mesencephalon. Also expressed in developing bone and
CC       gut.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. CaMK subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH51996.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB023027; BAA87926.1; -; mRNA.
DR   EMBL; AF181984; AAF29157.1; -; mRNA.
DR   EMBL; BC051996; AAH51996.1; ALT_INIT; mRNA.
DR   EMBL; BC055891; AAH55891.1; -; mRNA.
DR   IPI; IPI00136288; -.
DR   RefSeq; NP_001186280.1; NM_001199351.1.
DR   RefSeq; NP_001186281.1; NM_001199352.1.
DR   RefSeq; NP_036170.1; NM_012040.3.
DR   UniGene; Mm.89564; -.
DR   ProteinModelPortal; Q9QYK9; -.
DR   SMR; Q9QYK9; 8-294.
DR   STRING; Q9QYK9; -.
DR   PRIDE; Q9QYK9; -.
DR   Ensembl; ENSMUST00000002087; ENSMUSP00000002087; ENSMUSG00000002012.
DR   Ensembl; ENSMUST00000114472; ENSMUSP00000110116; ENSMUSG00000002012.
DR   Ensembl; ENSMUST00000114473; ENSMUSP00000110117; ENSMUSG00000002012.
DR   GeneID; 93843; -.
DR   KEGG; mmu:93843; -.
DR   UCSC; uc009tmc.1; mouse.
DR   CTD; 93843; -.
DR   MGI; MGI:1347357; Pnck.
DR   GeneTree; ENSGT00600000084207; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108055; -.
DR   InParanoid; Q9QYK9; -.
DR   OMA; IYESPTH; -.
DR   OrthoDB; EOG4T4CVW; -.
DR   PhylomeDB; Q9QYK9; -.
DR   BRENDA; 2.7.11.17; 244.
DR   NextBio; 351709; -.
DR   ArrayExpress; Q9QYK9; -.
DR   Bgee; Q9QYK9; -.
DR   Genevestigator; Q9QYK9; -.
DR   GermOnline; ENSMUSG00000002012; Mus musculus.
DR   GO; GO:0005954; C:calcium- and calmodulin-dependent protein kinase complex; TAS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004683; F:calmodulin-dependent protein kinase activity; IEA:EC.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Calcium; Calmodulin-binding; Cytoplasm; Kinase;
KW   Nucleotide-binding; Nucleus; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN         1    343       Calcium/calmodulin-dependent protein
FT                                kinase type 1B.
FT                                /FTId=PRO_0000086080.
FT   DOMAIN       15    270       Protein kinase.
FT   NP_BIND      21     29       ATP (By similarity).
FT   REGION      290    311       Calmodulin-binding (By similarity).
FT   ACT_SITE    136    136       Proton acceptor (By similarity).
FT   BINDING      44     44       ATP (By similarity).
SQ   SEQUENCE   343 AA;  38519 MW;  1B4A28D36E7A936E CRC64;
     MLLLKKQTED ISSVYEIREK LGSGAFSEVM LAQERGSAHL VALKCIPKKA LRGKEALVEN
     EIAVLRRISH PNIVALEDVH ESPSHLYLAM ELVTGGELFD RIMERGSYTE KDASHLVGQV
     LGAVSYLHSL GIVHRDLKPE NLLYATPFED SKIMVSDFGL SKIQAGNMLG TACGTPGYVA
     PELLEQKPYG KAVDVWALGV ISYILLCGYP PFYDESDPEL FSQILRASYE FDSPFWDDIS
     ESAKDFIRHL LERDPQKRFT CQQALQHLWI SGDAAFDRDI LGSVSEQIQK NFARTHWKRA
     FNATSFLRHI RKLGQSPEGE EASRQCMTRH SHPGLGTSQS PKW
//
ID   MAP1A_MOUSE             Reviewed;        2776 AA.
AC   Q9QYR6; A2ARN9; Q3TQM8; Q3TUV8; Q3UHB7; Q9QZH9; Q9QZI0; Q9QZI1;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Microtubule-associated protein 1A;
DE            Short=MAP-1A;
DE   Contains:
DE     RecName: Full=MAP1 light chain LC2;
GN   Name=Map1a; Synonyms=Mtap1, Mtap1a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-224 (ISOFORMS 1 AND 2),
RP   AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=21210968; PubMed=11311937; DOI=10.1016/S0167-4781(01)00173-7;
RA   Nakayama A., Odajima T., Murakami H., Mori N., Takahashi M.;
RT   "Characterization of two promoters that regulate alternative
RT   transcripts in the microtubule-associated protein (MAP) 1A gene.";
RL   Biochim. Biophys. Acta 1518:260-266(2001).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526; SER-527; THR-633;
RP   SER-644 AND SER-667, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   INTERACTION WITH TIAM2.
RX   PubMed=17320046; DOI=10.1016/j.bbrc.2007.02.028;
RA   Takefuji M., Mori K., Morita Y., Arimura N., Nishimura T.,
RA   Nakayama M., Hoshino M., Iwamatsu A., Murohara T., Kaibuchi K.,
RA   Amano M.;
RT   "Rho-kinase modulates the function of STEF, a Rac GEF, through its
RT   phosphorylation.";
RL   Biochem. Biophys. Res. Commun. 355:788-794(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526 AND SER-527, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-177, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-527 AND
RP   THR-633, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527; SER-667; SER-991
RP   AND SER-2082, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526 AND SER-527, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Structural protein involved in the filamentous cross-
CC       bridging between microtubules and other skeletal elements.
CC   -!- SUBUNIT: 3 different light chains, LC1, LC2 and LC3, can associate
CC       with MAP1A and MAP1B proteins. Interacts with guanylate kinase-
CC       like domain of DLG1, DLG2 and DLG4 (By similarity). Interacts with
CC       TIAM2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9QYR6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9QYR6-2; Sequence=VSP_003201;
CC   -!- TISSUE SPECIFICITY: Both isoforms highly expressed in brain, and
CC       to a lesser extent in embryo. Isoform 1 is also expressed at a low
CC       level in other tissues including heart and muscle.
CC   -!- DOMAIN: The basic region containing the repeats may be responsible
CC       for the binding of MAP1A to microtubules.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- PTM: LC2 is generated from MAP1A by proteolytic processing. It is
CC       free to associate with both MAP1A and MAP1B (By similarity).
CC   -!- SIMILARITY: Belongs to the MAP1 family.
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DR   EMBL; AK147474; BAE27940.1; -; mRNA.
DR   EMBL; AK160546; BAE35863.1; -; mRNA.
DR   EMBL; AK163468; BAE37354.1; -; mRNA.
DR   EMBL; AL845466; CAM24218.1; -; Genomic_DNA.
DR   EMBL; AF182211; AAF06164.1; -; Genomic_DNA.
DR   EMBL; AF182208; AAF06164.1; JOINED; Genomic_DNA.
DR   EMBL; AF182209; AAF06164.1; JOINED; Genomic_DNA.
DR   EMBL; AF182211; AAF06163.1; -; Genomic_DNA.
DR   EMBL; AF182213; AAD55790.1; -; mRNA.
DR   EMBL; AF182212; AAD55789.1; -; mRNA.
DR   IPI; IPI00408909; -.
DR   IPI; IPI00676243; -.
DR   RefSeq; NP_001166977.1; NM_001173506.1.
DR   RefSeq; NP_115769.1; NM_032393.2.
DR   UniGene; Mm.36501; -.
DR   ProteinModelPortal; Q9QYR6; -.
DR   SMR; Q9QYR6; 46-105.
DR   MINT; MINT-1203191; -.
DR   STRING; Q9QYR6; -.
DR   PhosphoSite; Q9QYR6; -.
DR   PRIDE; Q9QYR6; -.
DR   Ensembl; ENSMUST00000094639; ENSMUSP00000092223; ENSMUSG00000027254.
DR   Ensembl; ENSMUST00000110639; ENSMUSP00000106269; ENSMUSG00000027254.
DR   GeneID; 17754; -.
DR   KEGG; mmu:17754; -.
DR   UCSC; uc008lyi.1; mouse.
DR   UCSC; uc008lyj.1; mouse.
DR   CTD; 17754; -.
DR   MGI; MGI:1306776; Mtap1a.
DR   eggNOG; roNOG14193; -.
DR   GeneTree; ENSGT00550000074593; -.
DR   HOVERGEN; HBG052408; -.
DR   InParanoid; Q9QYR6; -.
DR   OrthoDB; EOG483D46; -.
DR   ArrayExpress; Q9QYR6; -.
DR   Bgee; Q9QYR6; -.
DR   CleanEx; MM_MTAP1A; -.
DR   Genevestigator; Q9QYR6; -.
DR   GermOnline; ENSMUSG00000027254; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; IDA:MGI.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Cytoskeleton; Microtubule;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1   2776       Microtubule-associated protein 1A.
FT                                /FTId=PRO_0000072753.
FT   CHAIN     ?2466   2776       MAP1 light chain LC2.
FT                                /FTId=PRO_0000269727.
FT   REPEAT      336    338       1.
FT   REPEAT      415    417       2.
FT   REPEAT      420    422       3.
FT   REPEAT      424    426       4.
FT   REPEAT      427    429       5.
FT   REPEAT      431    433       6.
FT   REPEAT      436    438       7.
FT   REPEAT      440    442       8.
FT   REPEAT      444    446       9.
FT   REPEAT      449    451       10.
FT   REPEAT      539    541       11.
FT   REGION      336    541       11 X 3 AA approximate repeats of K-K-
FT                                [DE].
FT   COMPBIAS    338    677       Glu-rich.
FT   COMPBIAS   1748   2303       Pro-rich.
FT   COMPBIAS   2530   2551       Pro-rich.
FT   COMPBIAS   2747   2750       Poly-Gln.
FT   MOD_RES     114    114       Phosphoserine.
FT   MOD_RES     177    177       Phosphotyrosine.
FT   MOD_RES     504    504       Phosphothreonine (By similarity).
FT   MOD_RES     526    526       Phosphoserine.
FT   MOD_RES     527    527       Phosphoserine.
FT   MOD_RES     611    611       Phosphoserine (By similarity).
FT   MOD_RES     633    633       Phosphothreonine.
FT   MOD_RES     644    644       Phosphoserine.
FT   MOD_RES     667    667       Phosphoserine.
FT   MOD_RES     772    772       Phosphotyrosine (By similarity).
FT   MOD_RES     895    895       Phosphoserine (By similarity).
FT   MOD_RES     899    899       Phosphoserine (By similarity).
FT   MOD_RES     991    991       Phosphoserine.
FT   MOD_RES    1008   1008       Phosphoserine (By similarity).
FT   MOD_RES    1062   1062       Phosphoserine (By similarity).
FT   MOD_RES    1147   1147       Phosphoserine (By similarity).
FT   MOD_RES    1205   1205       Phosphoserine (By similarity).
FT   MOD_RES    1310   1310       Phosphoserine (By similarity).
FT   MOD_RES    1313   1313       Phosphoserine (By similarity).
FT   MOD_RES    1634   1634       Phosphoserine (By similarity).
FT   MOD_RES    1648   1648       Phosphoserine (By similarity).
FT   MOD_RES    1747   1747       Phosphoserine (By similarity).
FT   MOD_RES    1762   1762       Phosphoserine (By similarity).
FT   MOD_RES    1768   1768       Phosphoserine (By similarity).
FT   MOD_RES    1772   1772       Phosphoserine (By similarity).
FT   MOD_RES    1789   1789       Phosphoserine (By similarity).
FT   MOD_RES    1990   1990       Phosphoserine (By similarity).
FT   MOD_RES    1993   1993       Phosphoserine (By similarity).
FT   MOD_RES    2082   2082       Phosphoserine.
FT   MOD_RES    2226   2226       Phosphoserine (By similarity).
FT   MOD_RES    2230   2230       Phosphoserine (By similarity).
FT   MOD_RES    2234   2234       Phosphoserine (By similarity).
FT   MOD_RES    2235   2235       Phosphoserine (By similarity).
FT   MOD_RES    2344   2344       Phosphoserine (By similarity).
FT   MOD_RES    2425   2425       Phosphoserine (By similarity).
FT   VAR_SEQ       1      1       M -> METTPELGLQSLGAPPAQNPAEPLCEAGAAVAAARW
FT                                DLRKYSLLIVIGDIGTESQLRAVRAHLEQGILSWNIDLSSF
FT                                DLNQQLRLFITRHLAHFSSEVKGQRTLCHQSETLETIILVN
FT                                PTADSISSEVHHLLSSPSAHKLLILSGQTLEPEGDLILQSG
FT                                TYSYQNFAQVLHKPEIAQLLSNRDPGIQAFLTVSCLGEGDW
FT                                SHLGLSSSQETLHLRLNPEPVLPTM (in isoform 2).
FT                                /FTId=VSP_003201.
FT   CONFLICT    349    349       R -> C (in Ref. 1; BAE27940).
SQ   SEQUENCE   2776 AA;  300140 MW;  62A8CC584CCAB21A CRC64;
     MDGVAEFSEY VSETVDVPSP FDLLEPPTSG GFLKLSKPCC YIFPGGRGDS ALFAVNGFNI
     LVDGGSDRKS CFWKLVRHLD RIDSVLLTHI GADNLPGING LLQRKVAELE EEQSQGSSSY
     SDWVKNLISP ELGVVFFNVP DKLRLPDASR KAKRSIEEAC LTLQHLNRLG IQAEPLYRVV
     SNTIEPLTLF HKMGVGRLDM YVLNPVKDSK EMQFLMQKWA GNSKAKTGIV LANGKEAEIS
     VPYLTSITAL VVWLPANPTE KIVRVLFPGN APQNKILEGL EKLRHLDFLR YPVATQKDLA
     AGAVPANLKP SKIKHRADSK ESLKAAPKTA MSKLAKREEV LEEGAKEARS ELAKELAKSE
     KKAKEPSEKP PEKPSKPERV RTESSEALKA EKRKLIKDKV GKKHLKEKIS KLEEKRDKEK
     KEIKKERKEL KKEEGRKEEK KDAKKDEKRK DTKPELKKFS KPDLKPFTPE VRKTLYKAKA
     PGRLKVDKGR AARGEKELSS EPRTPPAQKG AAPPPAASGH RELALSSPED LTQDFEELKR
     EERGLLAEPR DTELGEKPLP ADASEQGRPS TAIQVTQPPA SVLEQEQVER EKEVVPDFPE
     DKGSKNRAPD SGAEVEREKE TWEERKPREA ELTPENIAAA REESEPEVKE DVIEKAELEE
     MEEVHPSDEE EEETKAESFY QKHMQEALKV IPKGREALGG RELGFQGKAP EKETASFLSS
     LATPAGAAEH VSYIQDETIP GYSETEQTIS DEEIHDEPDE RPAPPRFPTS TYDLSGPEGP
     GPFEASQSAE SAVPASSSKT YGAPETELTY PPNMVAAPLA EEEHVSSATS ITECDKLSSF
     ATSVAEDQSV ASLTAPQTEE TGKSSLLLDT VTSIPSSRTE ATQGLDYVPS AGTISPTSSL
     EEDKGFKSPP CEDFSVTGES EKKGESVGRG LTGEKAVGKE EKNVTTSEKL SSQYAAVFGA
     PGHALHPGEP ALGEVEERCL SPDDSTVKMA SPPPSGPPSA AHTPFHQSPV EEKSEPQDFQ
     EDSWGDTKHA PGVSKEDAEE QTVKPGPEEA MSEEGKVPLS RSPQAQDTLG SLAGGQTGCT
     IQLLPEQDKA VVFETGEAGA ASGAGSLPGE VRTQEPAEPQ KDELLGFTDQ SFSPEDAESL
     SVLSVVSPDT AKQEATPRSP CTPKEQQLHK DLWPMVSPED TQSLSFSEES PSKETSLDIS
     SKQLSPESLG TLQFGELSLG KEEKGPLVKA EDNSCHLAPV SIPEPHTATV SPPTDEAAGE
     AGLTDESPAG NLPGSSFSHS ALSGDRKHSP GEITGPGGHF MTSDSSLTKS PESLSSPAME
     DLAMEWGGKA PGSEDRATEQ KEKELERKSE TLQQKDQILS EKAALVQRDS VMHQKDEALD
     EENKPGGQQD KTSEQKGRDL DKKDTAVELG KGPEPKGKDL YLEDQGLAEK DKALEQRGAA
     LQQTQAPEPR ARAQEHRDLE QKDEHLELRD KTPEEKDKVL VLEDRAPEHI IPQPTQTDRA
     PEHRSKVDKE QKDEASEEKE QVLEQKDWAR EKEGAALDQD NRAAGQKDGT LKEDKTQGQK
     SSFLEDKSTT PKEMTLDQKS PEKAKGVEQQ DGAVPEKTRA LGLEESPEEE GKAREQEEKY
     WKEQDVVQGW RETSPTRGEP VPAWEGKSPE QEVRYWRDRD ITLQQDAYWK ELSCERKVWF
     PHELDGQGAR PRYSEEREST FLDEGPNEQE ITPLQHTPRS PWASDFKDFQ EPLPQKGLEV
     ERWLAESPVG LPPEEEDKLT RSPFEIISPP ASPPEMTGQR VPSAPGQESP VPDTKSTPPT
     RNEPTTPSWL AEIPPWVPKD RPLPPAPLSP APAPPTPAPD PHAPAPFSWG IAEYDSVVAA
     VQEGAAELEG GPYSPLGKDY RKAEGEREGE GGAGAPDSSS FSSKVPEVTE SHTTRDAEQT
     EPEQREPTPY PDERSFQYAD IYEQMMLTGL GPACPTREPP LGASGDWPPH LSTKEEAAGR
     NKSAEKELSS AVSPPNLHSD TPTFSYASLA GPTIPPRQEP EPGPNVEPSF TPPAVPPRAP
     ISLSQDPSPP LNGSTTSCGP DRRTPSPKEA GRSHWDDGTN DSDLEKGARE QPEKETQSPS
     PHHPMPVGHP SLWPETEAHS SLSSDSHLGP VRPSLDFPAS AFGFSSLQPA PPQLPSPAEP
     RSAPCGSLAF SGDRALALVP GTPTRTRHDE YLEVTKAPSL DSSLPQLPSP SSPGAPLLSN
     LPRPASPALS EGSSSEATTP VISSVAERFP PGLEVAEQSS GELGPGNEPA AHSLWDLTPL
     SPAPLASRDL APAPAPAPAP SLPGNLGDGT LSCRPECSGE LTKKPSPFLS HSGDHEANGP
     GETSLNPPGF ATATAEKEEA EALHAWERGS WPEGAERSSR PDTLLSSEQR PGKSSGGPPC
     SLSSEVEAGP QGCATDPRPH CGELSPSFLN PPLPPSTDDS DLSTEEARLA GKGGRRRAGR
     PGATGGPCPM ADETPPTSAS DSGSSQSDSD VPPETEECPS ITAEAALDSD EDGDFLPVDK
     AGGVSGTHHP RPGHDPPPAP LPDPRPPPPR PDVCMADPEG LSSESGRVER LREKVQGRPG
     RKAPGRAKPA SPARRLDIRG KRSPTPGKGP VDRTSRALPR PRSTPSQVTS EEKDGHSPMS
     KGLVNGLKAG STALGSKGSS GPPVYVDLAY IPNHCSGKTA DQDFFRRVRA SYYVVSGNDP
     ANGEPSRAVL DALLEGKAQW GENLQVTLIP THDTEVTREW YQQTHEQQQQ LNVLVLASSS
     TVVMQDESFP ACKIEF
//
ID   GRM3_MOUSE              Reviewed;         879 AA.
AC   Q9QYS2; Q14DJ9;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Metabotropic glutamate receptor 3;
DE            Short=mGluR3;
DE   Flags: Precursor;
GN   Name=Grm3; Synonyms=Gprc1c, Mglur3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=20012997; PubMed=10544282;
RA   Minoshima T., Nakanishi S.;
RT   "Structural organization of the mouse metabotropic glutamate receptor
RT   subtype 3 gene and its regulation by growth factors in cultured
RT   cortical astrocytes.";
RL   J. Biochem. 126:889-896(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Receptor for glutamate. The activity of this receptor is
CC       mediated by a G-protein that inhibits adenylate cyclase activity.
CC   -!- SUBUNIT: Interacts with GRASP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
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DR   EMBL; AF170701; AAF06741.1; -; Genomic_DNA.
DR   EMBL; AF170697; AAF06741.1; JOINED; Genomic_DNA.
DR   EMBL; AF170698; AAF06741.1; JOINED; Genomic_DNA.
DR   EMBL; AF170699; AAF06741.1; JOINED; Genomic_DNA.
DR   EMBL; AF170700; AAF06741.1; JOINED; Genomic_DNA.
DR   EMBL; BC111891; AAI11892.1; -; mRNA.
DR   EMBL; BC113170; AAI13171.1; -; mRNA.
DR   IPI; IPI00136716; -.
DR   PIR; JC7160; JC7160.
DR   RefSeq; NP_862898.1; NM_181850.2.
DR   UniGene; Mm.318966; -.
DR   ProteinModelPortal; Q9QYS2; -.
DR   SMR; Q9QYS2; 28-567.
DR   STRING; Q9QYS2; -.
DR   PhosphoSite; Q9QYS2; -.
DR   PRIDE; Q9QYS2; -.
DR   Ensembl; ENSMUST00000004076; ENSMUSP00000004076; ENSMUSG00000003974.
DR   GeneID; 108069; -.
DR   KEGG; mmu:108069; -.
DR   UCSC; uc008wll.1; mouse.
DR   CTD; 108069; -.
DR   MGI; MGI:1351340; Grm3.
DR   GeneTree; ENSGT00580000081222; -.
DR   HOGENOM; HBG445787; -.
DR   HOVERGEN; HBG107965; -.
DR   InParanoid; Q9QYS2; -.
DR   OMA; LCDAMKI; -.
DR   OrthoDB; EOG49ZXNJ; -.
DR   PhylomeDB; Q9QYS2; -.
DR   NextBio; 359984; -.
DR   ArrayExpress; Q9QYS2; -.
DR   Bgee; Q9QYS2; -.
DR   CleanEx; MM_GRM3; -.
DR   Genevestigator; Q9QYS2; -.
DR   GermOnline; ENSMUSG00000003974; Mus musculus.
DR   GO; GO:0030424; C:axon; IDA:UniProtKB.
DR   GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
DR   GO; GO:0048786; C:presynaptic active zone; NAS:UniProtKB.
DR   GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
DR   GO; GO:0005246; F:calcium channel regulator activity; IDA:MGI.
DR   GO; GO:0001641; F:group II metabotropic glutamate receptor activity; IDA:MGI.
DR   GO; GO:0051930; P:regulation of sensory perception of pain; NAS:UniProtKB.
DR   GO; GO:0019233; P:sensory perception of pain; TAS:UniProtKB.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; TAS:UniProtKB.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR000337; GPCR_3.
DR   InterPro; IPR011500; GPCR_3_9-Cys_dom.
DR   InterPro; IPR017978; GPCR_3_C.
DR   InterPro; IPR017979; GPCR_3_CS.
DR   InterPro; IPR000162; GPCR_3_mtglu_rcpt.
DR   InterPro; IPR001234; GPCR_3_mtglu_rcpt_3.
DR   Pfam; PF00003; 7tm_3; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF07562; NCD3G; 1.
DR   PRINTS; PR00248; GPCRMGR.
DR   PRINTS; PR01053; MTABOTROPC3R.
DR   PRINTS; PR00593; MTABOTROPICR.
DR   PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; 1.
DR   PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; 1.
DR   PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
DR   PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Receptor; Signal; Transducer; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     22       Potential.
FT   CHAIN        23    879       Metabotropic glutamate receptor 3.
FT                                /FTId=PRO_0000012928.
FT   TOPO_DOM     23    576       Extracellular (Potential).
FT   TRANSMEM    577    599       Helical; Name=1; (Potential).
FT   TOPO_DOM    600    613       Cytoplasmic (Potential).
FT   TRANSMEM    614    634       Helical; Name=2; (Potential).
FT   TOPO_DOM    635    645       Extracellular (Potential).
FT   TRANSMEM    646    664       Helical; Name=3; (Potential).
FT   TOPO_DOM    665    688       Cytoplasmic (Potential).
FT   TRANSMEM    689    709       Helical; Name=4; (Potential).
FT   TOPO_DOM    710    734       Extracellular (Potential).
FT   TRANSMEM    735    756       Helical; Name=5; (Potential).
FT   TOPO_DOM    757    769       Cytoplasmic (Potential).
FT   TRANSMEM    770    792       Helical; Name=6; (Potential).
FT   TOPO_DOM    793    802       Extracellular (Potential).
FT   TRANSMEM    803    828       Helical; Name=7; (Potential).
FT   TOPO_DOM    829    879       Cytoplasmic (Potential).
FT   CARBOHYD    209    209       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    292    292       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    414    414       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    439    439       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   879 AA;  99114 MW;  F3A8B26CE96679EF CRC64;
     MKMLTRLQVL MLALFSKGFL VSLGDHNFMR REIKIEGDLV LGGLFPINEK GTGTEECGRI
     NEDRGIQRLE AMLFAIDEIN KDNYLLPGVK LGVHILDTCS RDTYALEQSL EFVRASLTKV
     DEAEYMCPDG SYAIQENIPL LIAGVIGGSY SSVSIQVANL LRLFQIPQIS YASTSAKLSD
     KSRYDYFART VPPDFYQAKA MAEILRYFNW TYVSTVASEG DYGETGIEAF EQEARLRNIC
     IATAEKVGRS NIRKSYDSVI RELLQKPNAR VVVLFMRSDD SRELIAAASR VNASFTWVAS
     DGWGAQESIV KGSEHVAYGA ITLELASHPV RQFDRYFQSL NPYNNHRNPW FRDFWEQKFQ
     CSLQNKRNHR QICDKHLAID SSNYEQESKI MFVVNAVYAM AHALHKMQRT LCPNTTKLCD
     AMKILDGKKL YKDYLLKINF TAPFNPNKGA DSIVKFDTYG DGMGRYNVFN FQHIGGKYSY
     LKVGHWAETL YLDVDSIHWS RNSVPTSQCS DPCAPNEMKN MQPGDVCCWI CIPCEPYEYL
     VDEFTCMDCG PGQWPTADLS GCYNLPEDYI RWEDAWAIGP VTIACLGFMC TCIVITVFIK
     HNNTPLVKAS GRELCYILLF GVSLSYCMTF FFIAKPSPVI CALRRLGLGT SFAICYSALL
     TKTNCIARIF DGVKNGAQRP KFISPSSQVF ICLGLILVQI VMVSVWLILE TPGTRRYTLP
     EKRETVILKC NVKDSSMLIS LTYDVVLVIL CTVYAFKTRK CPENFNEAKF IGFTMYTTCI
     IWLAFLPIFY VTSSDYRVQT TTMCISVSLS GFVVLGCLFA PKVHIVLFQP QKNVVTHRLH
     LNRFSVSGTA TTYSQSSAST YVPTVCNGRE VLDSTTSSL
//
ID   PCLO_MOUSE              Reviewed;        5038 AA.
AC   Q9QYX7; Q8CF91; Q8CF92; Q9QYX6; Q9QZJ0;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 3.
DT   08-FEB-2011, entry version 91.
DE   RecName: Full=Protein piccolo;
DE   AltName: Full=Aczonin;
DE   AltName: Full=Brain-derived HLMN protein;
DE   AltName: Full=Multidomain presynaptic cytomatrix protein;
GN   Name=Pclo; Synonyms=Acz;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
RP   ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND INTERACTION WITH
RP   PROFILIN.
RC   TISSUE=Brain;
RX   MEDLINE=99439764; PubMed=10508862; DOI=10.1083/jcb.147.1.151;
RA   Wang X., Kibschull M., Laue M.M., Lichte B., Petrasch-Parwez E.,
RA   Kilimann M.W.;
RT   "Aczonin, a 550-kd putative scaffolding protein of presynaptic active
RT   zones, shares homology regions with rim and bassoon and binds
RT   profilin.";
RL   J. Cell Biol. 147:151-162(1999).
RN   [2]
RP   SEQUENCE REVISION.
RA   Kilimann M.W.;
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), TISSUE SPECIFICITY, AND
RP   INTERACTION WITH RIMS2.
RX   MEDLINE=22384373; PubMed=12401793; DOI=10.1074/jbc.M210146200;
RA   Fujimoto K., Shibasaki T., Yokoi N., Kashima Y., Matsumoto M.,
RA   Sasaki T., Tajima N., Iwanaga T., Seino S.;
RT   "Piccolo, a Ca2+ sensor in pancreatic beta-cells. Involvement of cAMP-
RT   GEFII.Rim2.Piccolo complex in cAMP-dependent exocytosis.";
RL   J. Biol. Chem. 277:50497-50502(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4502-4682.
RC   TISSUE=Brain;
RA   Huang W., Jin W., Huang C., Chen B., Zhang J., Ju G.;
RT   "Mus musculus brain-derived reactive mRNA.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1409; SER-1545;
RP   THR-1730; SER-1736; SER-1742; SER-1799; SER-3580; SER-3586; THR-3864;
RP   THR-3865; SER-4256; SER-4260; SER-4263 AND SER-4295, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1409; SER-1736;
RP   SER-1742; SER-1799; THR-2968; SER-3328; THR-3346; SER-3580; SER-3586;
RP   SER-3733 AND SER-3922, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-2656 AND SER-2930, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452088; DOI=10.1074/mcp.T500040-MCP200;
RA   Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G.,
RA   Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F.,
RA   Maltby D.A., Schoepfer R., Burlingame A.L.;
RT   "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT   preparations using lectin weak affinity chromatography and mass
RT   spectrometry.";
RL   Mol. Cell. Proteomics 5:923-934(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-3731 AND SER-3733, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-595; SER-718; THR-830;
RP   THR-1090; SER-1310; SER-1311; SER-1370; SER-1409; SER-1414; SER-1427;
RP   SER-1555; SER-1733; SER-1736; SER-1742; SER-1778; TYR-1798; THR-2968;
RP   THR-3483; SER-3515; SER-3580 AND SER-3906, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: May act as a scaffolding protein involved in the
CC       organization of synaptic active zones and in synaptic vesicle
CC       trafficking.
CC   -!- SUBUNIT: Interacts with RABAC1/PRA1, RIMS2 and profilin.
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse. Note=Concentrated at
CC       the presynaptic side of synaptic junctions.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9QYX7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9QYX7-2; Sequence=VSP_003928, VSP_003929;
CC       Name=3; Synonyms=S;
CC         IsoId=Q9QYX7-3; Sequence=VSP_018191, VSP_018192, VSP_003928,
CC                                  VSP_003929;
CC       Name=4; Synonyms=L;
CC         IsoId=Q9QYX7-4; Sequence=VSP_018191, VSP_018192, VSP_018193;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain. Moderately
CC       expresssed in pituitary gland and pancreatic islets. Low levels
CC       found in stomach.
CC   -!- DOMAIN: C2 domain 1 is involved in binding calcium and
CC       phospholipids. Calcium binds with low affinity but with high
CC       specificity and induces a large conformational change.
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
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DR   EMBL; Y19185; CAB60731.2; -; mRNA.
DR   EMBL; Y19186; CAB60732.2; -; mRNA.
DR   EMBL; AB083477; BAC53723.1; -; mRNA.
DR   EMBL; AB083478; BAC53724.1; -; mRNA.
DR   EMBL; AF181269; AAD55786.2; -; mRNA.
DR   IPI; IPI00225140; -.
DR   IPI; IPI00468100; -.
DR   IPI; IPI00752192; -.
DR   IPI; IPI00754054; -.
DR   RefSeq; NP_001104266.1; NM_001110796.1.
DR   RefSeq; NP_036125.4; NM_011995.4.
DR   UniGene; Mm.146275; -.
DR   ProteinModelPortal; Q9QYX7; -.
DR   SMR; Q9QYX7; 4382-4490, 4588-4729, 4905-5014.
DR   STRING; Q9QYX7; -.
DR   PhosphoSite; Q9QYX7; -.
DR   PRIDE; Q9QYX7; -.
DR   Ensembl; ENSMUST00000030691; ENSMUSP00000030691; ENSMUSG00000061601.
DR   Ensembl; ENSMUST00000071768; ENSMUSP00000071676; ENSMUSG00000061601.
DR   GeneID; 26875; -.
DR   KEGG; mmu:26875; -.
DR   UCSC; uc008wmg.1; mouse.
DR   CTD; 26875; -.
DR   MGI; MGI:1349390; Pclo.
DR   eggNOG; roNOG08210; -.
DR   GeneTree; ENSGT00600000084489; -.
DR   HOGENOM; HBG283146; -.
DR   HOVERGEN; HBG031058; -.
DR   InParanoid; Q9QYX7; -.
DR   NextBio; 304679; -.
DR   ArrayExpress; Q9QYX7; -.
DR   Bgee; Q9QYX7; -.
DR   CleanEx; MM_PCLO; -.
DR   Genevestigator; Q9QYX7; -.
DR   GermOnline; ENSMUSG00000061601; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0005544; F:calcium-dependent phospholipid binding; ISS:UniProtKB.
DR   GO; GO:0005522; F:profilin binding; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0019933; P:cAMP-mediated signaling; IDA:MGI.
DR   GO; GO:0007010; P:cytoskeleton organization; IDA:MGI.
DR   GO; GO:0030073; P:insulin secretion; IDA:MGI.
DR   GO; GO:0017157; P:regulation of exocytosis; IDA:MGI.
DR   GO; GO:0016080; P:synaptic vesicle targeting; NAS:UniProtKB.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR008899; Znf_piccolo.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 2.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF05715; zf-piccolo; 2.
DR   SMART; SM00239; C2; 2.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 2.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS50106; PDZ; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Calcium/phospholipid-binding;
KW   Cell junction; Glycoprotein; Metal-binding; Phosphoprotein; Repeat;
KW   Synapse; Zinc; Zinc-finger.
FT   CHAIN         1   5038       Protein piccolo.
FT                                /FTId=PRO_0000058251.
FT   DOMAIN     4394   4488       PDZ.
FT   DOMAIN     4607   4705       C2 1.
FT   DOMAIN     4922   5012       C2 2.
FT   ZN_FING     502    526       C4-type (Potential).
FT   ZN_FING     967    990       C4-type (Potential).
FT   REGION      371    470       10 X 10 AA tandem approximate repeats of
FT                                P-A-K-P-Q-P-Q-Q-P-X.
FT   COMPBIAS   2305   2329       Poly-Pro.
FT   MOD_RES     595    595       Phosphoserine.
FT   MOD_RES     718    718       Phosphoserine.
FT   MOD_RES     830    830       Phosphothreonine.
FT   MOD_RES    1090   1090       Phosphothreonine.
FT   MOD_RES    1310   1310       Phosphoserine.
FT   MOD_RES    1311   1311       Phosphoserine.
FT   MOD_RES    1370   1370       Phosphoserine.
FT   MOD_RES    1409   1409       Phosphoserine.
FT   MOD_RES    1414   1414       Phosphoserine.
FT   MOD_RES    1427   1427       Phosphoserine.
FT   MOD_RES    1545   1545       Phosphoserine.
FT   MOD_RES    1555   1555       Phosphoserine.
FT   MOD_RES    1730   1730       Phosphothreonine.
FT   MOD_RES    1733   1733       Phosphoserine.
FT   MOD_RES    1736   1736       Phosphoserine.
FT   MOD_RES    1742   1742       Phosphoserine.
FT   MOD_RES    1778   1778       Phosphoserine.
FT   MOD_RES    1798   1798       Phosphotyrosine.
FT   MOD_RES    1799   1799       Phosphoserine.
FT   MOD_RES    2953   2953       Phosphoserine (By similarity).
FT   MOD_RES    2968   2968       Phosphothreonine.
FT   MOD_RES    3328   3328       Phosphoserine.
FT   MOD_RES    3346   3346       Phosphothreonine.
FT   MOD_RES    3483   3483       Phosphothreonine.
FT   MOD_RES    3515   3515       Phosphoserine.
FT   MOD_RES    3580   3580       Phosphoserine.
FT   MOD_RES    3586   3586       Phosphoserine.
FT   MOD_RES    3731   3731       Phosphotyrosine.
FT   MOD_RES    3733   3733       Phosphoserine.
FT   MOD_RES    3864   3864       Phosphothreonine.
FT   MOD_RES    3865   3865       Phosphothreonine.
FT   MOD_RES    3906   3906       Phosphoserine.
FT   MOD_RES    3922   3922       Phosphoserine.
FT   MOD_RES    4256   4256       Phosphoserine.
FT   MOD_RES    4260   4260       Phosphoserine.
FT   MOD_RES    4263   4263       Phosphoserine.
FT   MOD_RES    4295   4295       Phosphoserine.
FT   CARBOHYD   2656   2656       O-linked (GlcNAc).
FT   CARBOHYD   2930   2930       O-linked (GlcNAc).
FT   VAR_SEQ     428    428       H -> HPTPAKPQPQQPTPAKPQPQQPTPAKPQPQQ (in
FT                                isoform 3 and isoform 4).
FT                                /FTId=VSP_018191.
FT   VAR_SEQ    2931   2931       T -> TGQYDVAIDPALNCHYGVMHLVSGEQYPCSSFCLHF
FT                                CFLWMVWPYILQYMCIFVSPWFLLLSLPACACMLNIAFLPH
FT                                LIRLTCGFACSPIHCAHQDKRAFTPKQHHSFWNWTITLPCI
FT                                S (in isoform 3 and isoform 4).
FT                                /FTId=VSP_018192.
FT   VAR_SEQ    4640   4648       Missing (in isoform 4).
FT                                /FTId=VSP_018193.
FT   VAR_SEQ    4829   4833       TKPTN -> SKRRK (in isoform 2 and isoform
FT                                3).
FT                                /FTId=VSP_003928.
FT   VAR_SEQ    4834   5038       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_003929.
FT   CONFLICT    156    156       D -> E (in Ref. 1).
FT   CONFLICT    366    366       A -> S (in Ref. 1).
FT   CONFLICT    458    458       Q -> H (in Ref. 1).
FT   CONFLICT    921    921       V -> A (in Ref. 1).
FT   CONFLICT    935    935       P -> H (in Ref. 1).
FT   CONFLICT   1890   1890       Q -> P (in Ref. 1).
FT   CONFLICT   1901   1901       Q -> R (in Ref. 1).
FT   CONFLICT   2305   2316       Missing (in Ref. 3).
FT   CONFLICT   2825   2825       E -> D (in Ref. 1).
FT   CONFLICT   4012   4012       S -> P (in Ref. 1).
FT   CONFLICT   5032   5032       V -> M (in Ref. 3; BAC53723).
SQ   SEQUENCE   5038 AA;  547570 MW;  D1BB352B506F9893 CRC64;
     MGNEASLEGE GLPEGLAAAA GGAGGSGSAL HPGIPAGMEA DLSQLSEEER RQIAAVMSRA
     QGLPKGSVPA AAAESPSMHR KQELDSSQAP QQPGKPPDPG RPPQHGLSKS RTTDTFRSEQ
     KLPGRSPSTI SLKESKSRTD FKEEYKSSMM PGFFSDVNPL SAVSSVVNKF NPFDLISDSE
     AVQEETTKKQ KVAQKDQGKS EGITKPSLQQ PSPKLIPKQQ GPGKEVIPQD IPSKSVSSQQ
     AEKTKPQAPG TAKPSQQSPA QTPAQQAKPV AQQPGPAKAT VQQPGPAKSP AQPAGTGKSP
     AQPPVTAKPP AQQAGLEKTS LQQPGPKSLA QTPGQGKVPP GPAKSPAQQP GTAKLPAQQP
     GPQTAAKVPG PTKTPAQLSG PGKTPAQQPG PTKPSPQQPI PAKPQPQQPV ATKPQPQQPA
     PAKPQPQHPT PAKPQPQQPT PAKPQPQQPT PAKPQPQQPG LGKPSAQQPS KSISQTVTGR
     PLQAPPTSAA QAPAQGLSKT ICPLCNTTEL LLHTPEKANF NTCTECQSTV CSLCGFNPNP
     HLTEIKEWLC LNCQMQRALG GELAAIPSSP QPTPKAASVQ PATASKSPVP SQQASPKKEL
     PSKQDSPKAP ESKKPPPLVK QPTLHGPTPA TAPQPPVAEA LPKPAPPKKP SAALPEQAKA
     PVADVEPKQP KTTETLTDSP SSAAATSKPA ILSSQVQAQA QVTTAPPLKT DSAKTSQSFP
     PTGDTITPLD SKAMPRPASD SKIVSHPGPT SESKDPVQKK EEPKKAQTKV TPKPDTKPVP
     KGSPTPSGTR PTTGQATPQS QQPPKPPEQS RRFSLNLGGI ADAPKSQPTT PQETVTGKLF
     GFGASIFSQA SNLISTAGQQ APHPQTGPAA PSKQAPPPSQ TLAAQGPPKS TGQHPSAPAK
     TTAVKKETKG PAAENLEAKP VQAPTVKKAE KDKKPPPGKV SKPPPTEPEK AVLAQKPDKT
     TKPKPACPLC RTELNVGSQD PPNFNTCTEC KNQVCNLCGF NPTPHLTEIQ EWLCLNCQTQ
     RAISGQLGDM DKMPPASSGP KASPVPAPAE PPPQKTPTAA HAKGKKKETE VKAETEKQIP
     EKETPSIEKT PPAVATDQKL EESEVTKSLV SVLPEKKPSE EEKALPADKK EKKPPAAEAP
     PLEEKKPIPD DQKLPPDAKP SASEGEEKRD LLKAHVQIPE EGPIGKVASL ACEGEQQPDT
     RPEDLPGATP QTLPKDRQKE SRDVTQPQAE GTAKEGRGEP SKDRTEKEED KSDTSSSQQP
     KSPQGLSDTG YSSDGISGSL GEIPSLIPSD EKDLLKGLKK DSFSQESSPS SPSDLAKLES
     TVLSILEAQA STLVGEKAEK KTQPQKVSPE QPQDQQKTQT PSETRDISIS EEEIKESQEK
     KVTSKKDSAQ GFPSRKEHKE NPELVDDLSP RRASYDSVED SSESENSPVA RRKRRTSIGS
     SSSEEYKQED SQGSGEDEDF IRKQIIEMSA DEDASGSEDE EFIRSQLKEI GGVTESQKRE
     ETKGKGKSPA GKHRRLTRKS STSFDDDAGR RHSWHDEDDE TFDESPELKF RETKSQESEE
     LVVAGGGGLR RFKTIELNST VTDKYSAESS QKKTTLYFDE EPELEMESLT DSPEDRSRGE
     GSSSLHASSF TPGTSPTSVS SLDEDSDSSP SHKKGESKQQ RKARHRSHGP LLPTIEDSSE
     EEELREEEEL LKEQEKQREL EQQQRKSSSK KSKKDKDELR AQRRRERPKT PPSNLSPIED
     ASPTEELRQA AEMEELHRSS CSEYSPSIES DPEGFEISPE KIIEVQKVYK LPTAVSLYSP
     TDEQSVMQKE GAQKALKSAE EMYEEMMHKP HKYKAFPAAN ERDEVFEKEP LYGGMLIEDY
     IYESLVEDTY NGSVDGSLLT RQDEQNGFMQ QRGREQKIRL QEQIYDDPMQ KITDLQKEFY
     ELESLHSIVP QEDIVSSSYI IPESHEIVDL GSMVTSTSEE KKLLDADAAY EELMKRQQMQ
     VTDGSSLIQT TMGDDMAEST LDFDRVQDAS LTSSILSGAS LTDSTSSATL SIPDVKITQH
     FSTEEFEDEY VTDYTREIQE IIAHESLILT YSEPSESATS VPPSDTPSLT SSISSVCTTD
     SSSPVTTLDS LTTVYTEPAD VITKFKDSEE ISSTYFPGSV IDYPEDIGVS LDRTITPESR
     TNADQIMISF PGIAPSITES VATKPERPQA DTISTDLPIS EKELIKGKKE TGDGIILEVL
     DAYKDKREES EAELTKISLP ETGLAPTPSS QTKEQPGSPH SVSGEISGQE KPTYRSPSGG
     LPVSTHPSKS HPFFRSSSLD ISAQPPPPPP PPPPPPPPPP PPPPPPLPPA TSPKPPTYPK
     RKLAAAAPVA PTAIVTAHAD AIPTVEATAA RRSNGLPATK ICAAAPPPVP PKPSSIPTGL
     VFTHRPEASK PPIAPKPAVP EIPVTTQKTT DTCPKPTGLP LTSNMSLNLV TSADYKLPSP
     TSPLSPHSNK SSPRYSKSLM ETYVVITLPS EPGTPTDSSA AQAITSWPLG SPPKDLVSLE
     TVFSVVPPMT STEIPSASQP TLYTSGALGT FSVTPAVTAS LFQTVPTSLT QFLPAEASKP
     EVSAVSSAVP SVAPRSVSIP IPPEPLALDR HQYKENGKLP LIGDAIDLRT IPKSEVKVTE
     KCMDLSASAM DVKRQTTANE VYRRQISAVQ PSIINLSAAS SLGTPVTMDS KTVAVVTCTD
     TTIYTTGTES QVGIEHAVTS PLQLTTSKHT ELQYRKPSSQ AFPMIRDEAP INLSLGPSTQ
     AVTLAVTKPV TVPPVGVTNG WTDSTISQGI TDGEVVDLST SKSHRTVVTM DESTSNVVTK
     IIEDEEKPVD LTAGRRAVCC DMVYKLPFGR SCTAQQPATT LPEDRFGYRD DHYQYDRSGP
     YGYRGIGGMK PSMSDTNLAE AGHFFYKSKN AFDYSGGTEA AVDLTSGRVS TGEVMDYSSK
     TTGPYPETRQ VISGVGISTP QYSTARMTPP PGPQYGVGSV LRSSNGVVYS SVATPIPSTF
     AITTQPGSIF STTVRDLSGI HTTDAITSLS ALHQSQPMPR SYFITTGASE TDISVTSIDI
     NASLQTITME TLPAETMDSV PTLTTASEVF SEVVGEESTL LIVPDEDKQQ QQLDLERELL
     ELEKIKQQRF AEELEWERQE IQRFREQEKI MVQKKLEELQ SMKQHLLYQQ EEERQAQFMM
     RQETLAQQQL QLEQIQQLQQ QLHQQLEEQK LRQIYQYNYE PSGTASPQTT TEQAILEGQY
     VATEGSQFWA TEDATTTAST VVAIEIPQSQ GWYTVQSDGV TQYIAPPGIL STVSEIPLTD
     VVVKEEKQPK KRSSGAKVRG QYDEMGESMA DDPRNLKKIV DSGVQTDDEE TADRTYASRR
     RRTKKSVDTS VQTDDEDQDE WDMPSRSRRK ARTGKYGDST AEGDKTKPPS KVSSVAVQTV
     AEISVQTEPL GTIRTPSIRA RVDAKVEIIK HISAPEKTYK GGSLGCQTET DPDTQSPPYM
     GATSPPKDKK RPTPLEIGYS SSHLRADPTV QLAPSPPKSP KVLYSPISPL SPGHALEPAF
     VPYEKPLPDD ISPQKVLHPD MAKVPPASPK TAKMMQRSMS DPKPLSPTAD ESSRAPFQYS
     EGFTAKGSQT TSGTQKKVKR TLPNPPPEEA STGTQSTYST MGTASRRRMC RTNTMARAKI
     LQDIDRELDL VERESAKLRK KQAELDEEEK EIDAKLRYLE MGINRRKEAL LKEREKRERA
     YLQGVAEDRD YMSDSEVSST RPSRVESQHG IERPRTAPQT EFSQFIPPQT QTEAQLVPPT
     SPYTQYQYSS PALPTQAPTP YTQQSHFQQQ TLYHQQVSPY QTQPTFQAVA TMSFTPQAQP
     TPTPQPSYQL PSQMMVIQQK PRQTTLYLEP KITSTYEVIR NQPLMIAPVS TDNTYAVSHL
     GSKYNSLDLR IGLEERSSMA SSPISSISAD SFYADIDHHT SRNYVLIDDI GDITKGTAAL
     SSAFSLHEKD LSKTDRLLRT TETRRSQEVT DFLAPLQTSS RLHSYVKAEE DSMEDPYELK
     LLKHQIKQEF RRGTESLDHL AGLSHYYHAD TSYRHFPKSE KYSISRLTLE KQAAKQLPAA
     ILYQKQSKHK KALIDPKMSK FSPIQESRDL EPDYPTYLSS STSSIGGISS RARLLQDDIT
     FGLRKNITDQ QKFMGSSLGS GLGTLGNTIR SALQDEADKP YSSGSRSRPS SRPSSVYGLD
     LSIKRDSSSS SLRLKAQEAE ALDVSFGHSS SSARTKPTSL PISQSRGRIP IVAQNSEEES
     PLSPVGQPMG MARAAAGPLP PISADTRDQF GSSHSLPEVQ QHMREESRTR GYDRDIAFIM
     DDFQHAMSDS EAYHLRREET DWFDKPRESR LENGHGLDRK LPERLVHSRP LSQHQEQILQ
     MNGKTMHYIF PHARIKITRD SKDHTVSGNG LGIRIVGGKE IPGHSGEIGA YIAKILPGGS
     AEHSGKLIEG MQVLEWNGIP LTSKTYEEVQ SIINQQSGEA EICVRLDLNM LSDSENPQHL
     ELHEPPKVVD KAKSPGVDPK QLAAELQKVS LQQSPLVMSS VVEKGAHAHS GPTSAGSSSV
     PSPGQPGSPS VSKKKHGGSK PTDVSKTASH PITGEIQLQI NYDLGNLIIH ILQARNLVPR
     DNNGYSDPFV KVYLLPGRGQ VMVVQNASVE YKRRTKYVQK SLNPEWNQTV IYKSISMEQL
     MKKTLEVTVW DYDRFSSNDF LGEVLIDLSS TSHLDNTPRW YPLKEQTESI EHGKSHSSQN
     SQQSPKPSVI KSRSHGIFPD PSKDMQVPTI EKSHSSPGSS KSSSEGHLRS HGPSRSQSKT
     SVAQTHLEDA GAAIAAAEAA VQQLRIQPTK PTNHRPAETS VSTGSSGSSV GSGYSVDSEG
     SSCVAGEPNL LPIPRIGKMG QNGQDPVKQP GMGAADTEAK TQVMGEIKLA LKKEMKTDGE
     QLIVEILQCR NITYKFKSPD HLPDLYVKIY VINIATQKKV IKKKTRVCRH DREPSFNETF
     RFSLSPAGHS LQILLFSNGG KFMKKTLIGE ACIWLDKVDL RKRIVNWHKL LVSPTQTH
//
ID   GAB1_MOUSE              Reviewed;         695 AA.
AC   Q9QYY0; Q91VW7;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=GRB2-associated-binding protein 1;
DE   AltName: Full=GRB2-associated binder 1;
DE   AltName: Full=Growth factor receptor bound protein 2-associated protein 1;
GN   Name=Gab1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Sachs M.;
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-504, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Probably involved in EGF and insulin receptor signaling
CC       (By similarity).
CC   -!- SUBUNIT: Interacts with GRB2 and with other SH2-containing
CC       proteins. Interacts with phosphorylated LAT2. Interacts with PTPRJ
CC       (By similarity).
CC   -!- INTERACTION:
CC       Q60631:Grb2; NbExp=1; IntAct=EBI-644784, EBI-1688;
CC       P27986:PIK3R1 (xeno); NbExp=1; IntAct=EBI-644784, EBI-79464;
CC       Q6NZN1:Pprc1; NbExp=2; IntAct=EBI-644784, EBI-644797;
CC   -!- PTM: Phosphorylated on tyrosine residue(s) by the epidermal growth
CC       factor receptor (EGFR) and the insulin receptor (INSR). Tyrosine
CC       phosphorylation of GAB1 mediates interaction with several proteins
CC       that contain SH2 domains (By similarity).
CC   -!- SIMILARITY: Belongs to the GAB family.
CC   -!- SIMILARITY: Contains 1 PH domain.
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DR   EMBL; AJ250669; CAB59832.1; -; mRNA.
DR   EMBL; BC007483; AAH07483.1; -; mRNA.
DR   IPI; IPI00406794; -.
DR   RefSeq; NP_067331.2; NM_021356.2.
DR   UniGene; Mm.277409; -.
DR   ProteinModelPortal; Q9QYY0; -.
DR   SMR; Q9QYY0; 4-119.
DR   IntAct; Q9QYY0; 9.
DR   MINT; MINT-137191; -.
DR   STRING; Q9QYY0; -.
DR   PhosphoSite; Q9QYY0; -.
DR   PRIDE; Q9QYY0; -.
DR   Ensembl; ENSMUST00000034150; ENSMUSP00000034150; ENSMUSG00000031714.
DR   GeneID; 14388; -.
DR   KEGG; mmu:14388; -.
DR   UCSC; uc009mjb.1; mouse.
DR   CTD; 14388; -.
DR   MGI; MGI:108088; Gab1.
DR   GeneTree; ENSGT00510000046662; -.
DR   HOGENOM; HBG716403; -.
DR   HOVERGEN; HBG051685; -.
DR   InParanoid; Q9QYY0; -.
DR   OMA; YLLLINC; -.
DR   OrthoDB; EOG4KSPJ6; -.
DR   PhylomeDB; Q9QYY0; -.
DR   NextBio; 285905; -.
DR   ArrayExpress; Q9QYY0; -.
DR   Bgee; Q9QYY0; -.
DR   Genevestigator; Q9QYY0; -.
DR   GermOnline; ENSMUSG00000031714; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004871; F:signal transducer activity; IDA:MGI.
DR   GO; GO:0007257; P:activation of JUN kinase activity; IMP:MGI.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IMP:MGI.
DR   GO; GO:0008544; P:epidermis development; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IMP:MGI.
DR   GO; GO:0060711; P:labyrinthine layer development; IMP:MGI.
DR   GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:MGI.
DR   GO; GO:0043410; P:positive regulation of MAPKKK cascade; IMP:MGI.
DR   GO; GO:0030334; P:regulation of cell migration; IGI:MGI.
DR   GO; GO:0006979; P:response to oxidative stress; IDA:MGI.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00233; PH; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein.
FT   CHAIN         1    695       GRB2-associated-binding protein 1.
FT                                /FTId=PRO_0000050284.
FT   DOMAIN        5    116       PH.
FT   COMPBIAS    450    541       Pro-rich.
FT   MOD_RES     183    183       Phosphotyrosine (By similarity).
FT   MOD_RES     259    259       Phosphotyrosine (By similarity).
FT   MOD_RES     266    266       Phosphoserine.
FT   MOD_RES     373    373       Phosphotyrosine (By similarity).
FT   MOD_RES     407    407       Phosphotyrosine (By similarity).
FT   MOD_RES     504    504       Phosphothreonine.
FT   MOD_RES     628    628       Phosphotyrosine (By similarity).
FT   MOD_RES     660    660       Phosphotyrosine.
FT   CONFLICT    236    236       F -> L (in Ref. 1; CAB59832).
FT   CONFLICT    351    351       T -> S (in Ref. 1; CAB59832).
FT   CONFLICT    379    379       A -> V (in Ref. 1; CAB59832).
SQ   SEQUENCE   695 AA;  76812 MW;  F0A567896E058C58 CRC64;
     MSGGEVVCSG WLRKSPPEKK LKRYAWKRRW FVLRSGRLTG DPDVLEYYKN DHAKKPIRII
     DLNLCQQVDA GLTFNKKEFE NSYIFDINTI DRIFYLVADS EEDMNKWVRC ICDICGFNPT
     EEDPVKPLTG SSQAPVDSPF AISTAPASSQ MEASSVALPP PYQVISLPPH PDTLGLQDDP
     QDYLLLINCQ SKKPEPNRTL FDSAKPTFSE TDCNDNVPSH QTPASSQSKH GMNGFFQQQM
     MYDCPPSRLT SVSGESSLYN LPRSYSHDVL PKESPSSTEA DGELYTFNTP SGTAGVETQM
     RHVSISYDIP PTPGNTYQIP RTFPESTLGQ SSKLDTIPDI PPPRPPKPHP THDRSPVETC
     GVPRTASDTD SSYCIPPPAG MTPSRSNTIS TVDLNKLRKD ASSQDCYDIP RTFPSDRSSS
     LEGFHSQYKI KSVLTAGGVS GEELDENYVP MNPNSPPRQH SGSFTEPIQE PNYVPMTPGT
     FDFSSFGMQV PPPAHMGFRS SPKTPPRRPV PVADCEPPPV DRNLKPDRKV KPAPLDIKPL
     SEWEELQAPV RSPITRSFAR DSSRFPMSPR PDSVHSTTSS SDSHDSEENY VPMNPNLSGE
     DPNLFASNSL DGGSSPMNKP KGDKQVEYLD LDLDSGKSTP PRKQKSSGSG SSMADERVDY
     VVVDQQKTLA LKSTREAWTD GRQSTESETP TKNVK
//
ID   SPAST_MOUSE             Reviewed;         614 AA.
AC   Q9QYY8; Q6ZPY6; Q80VE0; Q9CVK0;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 3.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Spastin;
DE            EC=3.6.4.3;
GN   Name=Spast; Synonyms=Kiaa1083, Spg4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-614.
RC   STRAIN=C57BL/6J; TISSUE=Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 111-614, AND TISSUE SPECIFICITY.
RX   MEDLINE=20055425; PubMed=10610178; DOI=10.1038/15472;
RA   Hazan J., Fonknechten N., Mavel D., Paternotte C., Samson D.,
RA   Artiguenave F., Davoine C.-S., Cruaud C., Durr A., Wincker P.,
RA   Brottier P., Cattolico L., Barbe V., Burgunder J.-M.,
RA   Prud'homme J.-F., Brice A., Fontaine B., Heilig R., Weissenbach J.;
RT   "Spastin, a new AAA protein, is altered in the most frequent form of
RT   autosomal dominant spastic paraplegia.";
RL   Nat. Genet. 23:296-303(1999).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=16026783; DOI=10.1016/j.yexcr.2005.06.009;
RA   Claudiani P., Riano E., Errico A., Andolfi G., Rugarli E.I.;
RT   "Spastin subcellular localization is regulated through usage of
RT   different translation start sites and active export from the
RT   nucleus.";
RL   Exp. Cell Res. 309:358-369(2005).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=17101632; DOI=10.1093/hmg/ddl431;
RA   Tarrade A., Fassier C., Courageot S., Charvin D., Vitte J., Peris L.,
RA   Thorel A., Mouisel E., Fonknechten N., Roblot N., Seilhean D.,
RA   Dierich A., Hauw J.J., Melki J.;
RT   "A mutation of spastin is responsible for swellings and impairment of
RT   transport in a region of axon characterized by changes in microtubule
RT   composition.";
RL   Hum. Mol. Genet. 15:3544-3558(2006).
RN   [7]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18234839; DOI=10.1091/mbc.E07-09-0878;
RA   Yu W., Qiang L., Solowska J.M., Karabay A., Korulu S., Baas P.W.;
RT   "The microtubule-severing proteins spastin and katanin participate
RT   differently in the formation of axonal branches.";
RL   Mol. Biol. Cell 19:1485-1498(2008).
RN   [8]
RP   INDUCTION.
RX   PubMed=18495362; DOI=10.1016/j.neuroscience.2008.04.025;
RA   Ferrari-Toninelli G., Bonini S.A., Bettinsoli P., Uberti D., Memo M.;
RT   "Microtubule stabilizing effect of notch activation in primary
RT   cortical neurons.";
RL   Neuroscience 154:946-952(2008).
RN   [9]
RP   FUNCTION.
RX   PubMed=19141076; DOI=10.1111/j.1471-4159.2009.05875.x;
RA   Riano E., Martignoni M., Mancuso G., Cartelli D., Crippa F., Toldo I.,
RA   Siciliano G., Di Bella D., Taroni F., Bassi M.T., Cappelletti G.,
RA   Rugarli E.I.;
RT   "Pleiotropic effects of spastin on neurite growth depending on
RT   expression levels.";
RL   J. Neurochem. 108:1277-1288(2009).
CC   -!- FUNCTION: ATP-dependent microtubule severing protein. Microtubule
CC       severing may promote reorganization of cellular microtubule arrays
CC       and the release of microtubules from the centrosome following
CC       nucleation. Required for membrane traffic from the endoplasmic
CC       reticulum (ER) to the Golgi and for completion of the abscission
CC       stage of cytokinesis (By similarity). Required for development of
CC       axonal processes and for axonal branching.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Homohexamer. The homohexamer is stabilized by ATP-
CC       binding. The homohexamer may adopt a ring conformation through
CC       which microtubules pass prior to being severed. Binds to
CC       microtubules at least in part via the alpha-tubulin and beta-
CC       tubulin tails. Interacts (via MIT domain) with CHMP1B; the
CC       interaction is direct. Interacts with ATL1, RTN1, SSNA1 and
CC       ZFYVE27 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein
CC       (Potential). Cytoplasm, cytoskeleton, centrosome (By similarity).
CC       Cytoplasm, cytoskeleton (By similarity). Cytoplasm, perinuclear
CC       region (By similarity). Endoplasmic reticulum (By similarity).
CC       Endosome (By similarity). Nucleus (By similarity). Cytoplasm,
CC       cytoskeleton, spindle (By similarity). Note=Localization to the
CC       centrosome is independent of microtubules. Localizes to the
CC       midbody of dividing cells, and this requires CHMP1B (By
CC       similarity). Evenly distributed along early axons and concentrates
CC       in the growth cone of the axons of late stage 3 neurons.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, heart, liver, lung,
CC       skeletal muscle, spinal cord, spleen and testis.
CC   -!- INDUCTION: Expressed is decreased following activation of the
CC       Notch pathway by JAG1/Jagged1.
CC   -!- DISRUPTION PHENOTYPE: Progressive axonal degeneration
CC       characterized by focal axonal swellings and the accumulation of
CC       organelles and cytoskeletal components, which is suggestive of
CC       impaired axonal transport. Late development of mild motor defects.
CC       Adults are sterile. Primary cortical neurons develop swellings at
CC       the border between stable and dynamic microtubules.
CC   -!- SIMILARITY: Belongs to the AAA ATPase family. Spastin subfamily.
CC   -!- SIMILARITY: Contains 1 MIT domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK129282; BAC98092.1; -; mRNA.
DR   EMBL; BC046286; AAH46286.1; -; mRNA.
DR   EMBL; AK007793; BAB25259.1; -; mRNA.
DR   EMBL; AJ246002; CAB60143.1; -; mRNA.
DR   IPI; IPI00420580; -.
DR   RefSeq; NP_001156342.1; NM_001162870.1.
DR   RefSeq; NP_058658.2; NM_016962.2.
DR   UniGene; Mm.19804; -.
DR   ProteinModelPortal; Q9QYY8; -.
DR   SMR; Q9QYY8; 110-194, 322-606.
DR   STRING; Q9QYY8; -.
DR   PhosphoSite; Q9QYY8; -.
DR   PRIDE; Q9QYY8; -.
DR   Ensembl; ENSMUST00000024869; ENSMUSP00000024869; ENSMUSG00000024068.
DR   GeneID; 50850; -.
DR   KEGG; mmu:50850; -.
DR   UCSC; uc008dnz.1; mouse.
DR   CTD; 50850; -.
DR   MGI; MGI:1858896; Spast.
DR   eggNOG; roNOG11215; -.
DR   GeneTree; ENSGT00570000078874; -.
DR   HOGENOM; HBG724153; -.
DR   HOVERGEN; HBG108502; -.
DR   InParanoid; Q9QYY8; -.
DR   OMA; THKSTPK; -.
DR   OrthoDB; EOG4NZTTF; -.
DR   NextBio; 307827; -.
DR   ArrayExpress; Q9QYY8; -.
DR   Bgee; Q9QYY8; -.
DR   CleanEx; MM_SPAST; -.
DR   Genevestigator; Q9QYY8; -.
DR   GermOnline; ENSMUSG00000024068; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0008568; F:microtubule-severing ATPase activity; ISS:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007109; P:cytokinesis, completion of separation; ISS:UniProtKB.
DR   GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR   GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR   GO; GO:0051013; P:microtubule severing; ISS:UniProtKB.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0034214; P:protein hexamerization; ISS:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR007330; MIT.
DR   InterPro; IPR017179; Spastin.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF04212; MIT; 1.
DR   PIRSF; PIRSF037338; Spastin; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00745; MIT; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW   Developmental protein; Differentiation; Endoplasmic reticulum;
KW   Endosome; Hydrolase; Membrane; Microtubule; Neurogenesis;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    614       Spastin.
FT                                /FTId=PRO_0000084764.
FT   TRANSMEM     55     77       Helical; (Potential).
FT   DOMAIN      114    192       MIT.
FT   NP_BIND     380    387       ATP (Potential).
FT   REGION        1    298       Required for interaction with RTN1 (By
FT                                similarity).
FT   REGION        1    192       Required for midbody localization (By
FT                                similarity).
FT   REGION        1     78       Required for interaction with ATL1 (By
FT                                similarity).
FT   REGION        1     48       Required for nuclear localization (By
FT                                similarity).
FT   REGION       48     85       Required for interaction with SSNA1 and
FT                                microtubules (By similarity).
FT   REGION      110    194       Sufficient for interaction with CHMP1B
FT                                (By similarity).
FT   REGION      111    198       Required for interaction with
FT                                microtubules (By similarity).
FT   REGION      225    326       Sufficient for interaction with
FT                                microtubules (By similarity).
FT   REGION      226    614       Sufficient for microtubule severing (By
FT                                similarity).
FT   REGION      268    326       Required for interaction with
FT                                microtubules and microtubule severing (By
FT                                similarity).
FT   MOTIF         4     11       Nuclear localization signal (By
FT                                similarity).
FT   MOTIF        57     65       Nuclear export signal (By similarity).
FT   MOTIF       307    310       Nuclear localization signal (By
FT                                similarity).
FT   MOD_RES     266    266       Phosphoserine (By similarity).
FT   MOD_RES     301    301       Phosphothreonine (By similarity).
FT   MOD_RES     304    304       Phosphothreonine (By similarity).
FT   CONFLICT    104    104       E -> A (in Ref. 1; BAC98092 and 2;
FT                                AAH46286).
FT   CONFLICT    137    137       Missing (in Ref. 2; AAH46286 and 3;
FT                                BAB25259).
SQ   SEQUENCE   614 AA;  66456 MW;  C0D235031A7E4C8F CRC64;
     MSSPAGRRKK KGSGGASPAP ARPPPPAAVP APAAGPAPAA GSPPKRNPSS FSSPLVVGFA
     LLRLLACHLG LLFAWLCQRF SRALMAAKRS SGTAPAPASP SPPEPGPGGE AESVRVFHKQ
     AFEYISIALR IDEEEKAGQK EQAVEWYKKG IEELEKGIAV IVTGQGEQYE RARRLQAKMM
     TNLVMAKDRL QLLEKLQPVL QFSKSQTDVY NESTNLTCRN GHLQSESGAV PKRKDPLTHA
     SNSLPRSKTV LKSGSAGLSG HHRAPSCSGL SMVSGARPGP GPAATTHKGT PKPNRTNKPS
     TPTTAVRKKK DLKNFRNVDS NLANLIMNEI VDNGTAVKFD DIAGQELAKQ ALQEIVILPS
     LRPELFTGLR APARGLLLFG PPGNGKTMLA KAVAAESNAT FFNISAASLT SKYVGEGEKL
     VRALFAVARE LQPSIIFIDE VDSLLCERRE GEHDASRRLK TEFLIEFDGV QSAGDDRVLV
     MGATNRPQEL DEAVLRRFIK RVYVSLPNEE TRLLLLKNLL CKQGSPLTQK ELAQLARMTD
     GYSGSDLTAL AKDAALGPIR ELKPEQVKNM SASEMRNIRL SDFTESLKKI KRSVSPQTLE
     AYIRWNKDFG DTTV
//
ID   Q9QZ83_MOUSE            Unreviewed;       393 AA.
AC   Q9QZ83;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   SubName: Full=Gamma actin-like protein;
GN   Name=Actg1; Synonyms=Actl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Swiss white;
RX   MEDLINE=96289102; PubMed=8764147;
RA   Lin G., McCormick J.I., Johnstone R.M.;
RT   "Is gamma-actin a regulator of amino acid transport?";
RL   Am. J. Physiol. 270:C1647-C1655(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Swiss white;
RA   Lin G., McCormick J.I., Johnstone R.M.;
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RX   PubMed=17451654; DOI=10.1016/j.bbrc.2007.04.015;
RA   Jeon H.B., Choi E.S., Yoon J.H., Hwang J.H., Chang J.W., Lee E.K.,
RA   Choi H.W., Park Z.-Y., Yoo Y.J.;
RT   "A proteomics approach to identify the ubiquitinated proteins in mouse
RT   heart.";
RL   Biochem. Biophys. Res. Commun. 357:731-736(2007).
CC   -!- FUNCTION: Actins are highly conserved proteins that are involved
CC       in various types of cell motility and are ubiquitously expressed
CC       in all eukaryotic cells (By similarity).
CC   -!- SIMILARITY: Belongs to the actin family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF195094; AAF08293.1; -; mRNA.
DR   IPI; IPI00136929; -.
DR   UniGene; Mm.196173; -.
DR   UniGene; Mm.426706; -.
DR   HSSP; P10983; 1D4X.
DR   ProteinModelPortal; Q9QZ83; -.
DR   SMR; Q9QZ83; 2-368.
DR   IntAct; Q9QZ83; 3.
DR   STRING; Q9QZ83; -.
DR   PhosphoSite; Q9QZ83; -.
DR   PRIDE; Q9QZ83; -.
DR   Ensembl; ENSMUST00000106216; ENSMUSP00000101823; ENSMUSG00000062825.
DR   GeneTree; ENSGT00590000082732; -.
DR   HOGENOM; HBG559892; -.
DR   HOVERGEN; HBG003771; -.
DR   InParanoid; Q9QZ83; -.
DR   PhylomeDB; Q9QZ83; -.
DR   ArrayExpress; Q9QZ83; -.
DR   Bgee; Q9QZ83; -.
DR   Genevestigator; Q9QZ83; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004000; Actin-like.
DR   InterPro; IPR020902; Actin/actin-like_CS.
DR   InterPro; IPR004001; Actin_CS.
DR   PANTHER; PTHR11937; Actin_like; 1.
DR   Pfam; PF00022; Actin; 1.
DR   PRINTS; PR00190; ACTIN.
DR   SMART; SM00268; ACTIN; 1.
DR   PROSITE; PS00406; ACTINS_1; 1.
DR   PROSITE; PS00432; ACTINS_2; 1.
DR   PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Cytoskeleton; Nucleotide-binding.
SQ   SEQUENCE   393 AA;  43601 MW;  F465CE39341F1A5F CRC64;
     MEEEIAALVI DNGSGMCKAN FAGDDAPGPS SLSIVGRPRH QGVMVGIMVG MGQKDSYVGD
     EAQSKRGILT LKYPIEHGIV TNWDDMEKIW HHTFYNELRV APEEHPVLLT EAPLNPKRNR
     EKMTQIMFET FNTPAMYVAI QAVLSLYASG RTTGIVMDSG DGVTHTVPIY EGYALPHAIL
     RLDLAGRDLT DYLMKILTER GYSFTTTAER EIVRDIKEKL CYVALDFEQE MATAASSSSL
     EKSYELPDGQ VITIGNERFR CPEALFQPSF LGMESCGIHE TTFNSIMKCD VDIRKDLYAN
     TVLSGGTTMY PGLADRMQKE ITALAPSTMK IKIIAPPERK YSVWIGGSIL ASLSTFQQMW
     ISKQEYDECQ APPSSTANAS RWTEQVPGIC CMS
//
ID   RGS17_MOUSE             Reviewed;         210 AA.
AC   Q9QZB0; Q543T9;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Regulator of G-protein signaling 17;
DE            Short=RGS17;
DE   AltName: Full=Regulator of Gz-selective protein signaling 2;
GN   Name=Rgs17; Synonyms=Rgsz2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c;
RA   Barker S.A., Ross E.M.;
RT   "RGSZ2, a new member of the Gz-selective GAP family.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Corpora quadrigemina, Olfactory bulb, and
RC   Pituitary;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   INTERACTION WITH OPRM1, GLYCOSYLATION, TISSUE SPECIFICITY, AND
RP   FUNCTION.
RX   PubMed=15827571; DOI=10.1038/sj.npp.1300726;
RA   Garzan J., Rodriguez-Munoz M., Lopez-Fando A., Sanchez-Blazquez P.;
RT   "The RGSZ2 protein exists in a complex with mu-opioid receptors and
RT   regulates the desensitizing capacity of Gz proteins.";
RL   Neuropsychopharmacology 30:1632-1648(2005).
RN   [4]
RP   SUMOYLATION, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=16900103; DOI=10.1038/sj.npp.1301184;
RA   Rodriguez-Munoz M., Bermudez D., Sanchez-Blazquez P., Garzon J.;
RT   "Sumoylated RGS-Rz proteins act as scaffolds for mu-opioid receptors
RT   and G-protein complexes in mouse brain.";
RL   Neuropsychopharmacology 32:842-850(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-137, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: Inhibits signal transduction by increasing the GTPase
CC       activity of G protein alpha subunits thereby driving them into
CC       their inactive GDP-bound form. Binds selectively to G(z)-alpha and
CC       G(alpha)-i2 subunits, accelerates their GTPase activity and
CC       regulates their signaling activities. The G(z)-alpha activity is
CC       inhibited by the phosphorylation and palmitoylation of the G-
CC       protein. Negatively regulates mu-opioid receptor-mediated
CC       activation of the G-proteins.
CC   -!- SUBUNIT: Forms a complex with G(alpha)z/i2 subunits and mu-opioid
CC       receptors; the formation of this complex results in mu-opioid
CC       receptor desensitization. Interacts with OPRM1.
CC   -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor. Nucleus. Cytoplasm.
CC       Note=Shuttles between the cytoplasm/cell membrane and the nucleus.
CC       Anchored to the membrane through palmitoylation (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in the hypothalamus,
CC       periaqueductal gray matter, and pons-medulla. Lower levels in the
CC       thalamus, cortex and spinal cord. Weak expression in the striatum
CC       and cerebellum.
CC   -!- PTM: Fatty acylated. Heavily palmitoylated in the cysteine string
CC       motif (By similarity).
CC   -!- PTM: N- and O-glycosylated in synapsomal membranes.
CC   -!- PTM: Serine phosphorylated in synapsomal membranes.
CC   -!- PTM: Sumoylated by SUMO1 and SUM02 in synaptosomes. The sumoylated
CC       forms act as a scaffold for sequestering mu-opioid receptor-
CC       activated G(alpha) subunits.
CC   -!- SIMILARITY: Contains 1 RGS domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF191555; AAF05758.1; -; mRNA.
DR   EMBL; AK018279; BAB31145.1; -; mRNA.
DR   EMBL; AK030492; BAC26989.1; -; mRNA.
DR   EMBL; AK046009; BAC32571.1; -; mRNA.
DR   EMBL; AK163188; BAE37226.1; -; mRNA.
DR   IPI; IPI00623207; -.
DR   RefSeq; NP_001155294.1; NM_001161822.1.
DR   RefSeq; NP_064342.1; NM_019958.4.
DR   UniGene; Mm.44606; -.
DR   ProteinModelPortal; Q9QZB0; -.
DR   SMR; Q9QZB0; 69-203.
DR   STRING; Q9QZB0; -.
DR   PhosphoSite; Q9QZB0; -.
DR   PRIDE; Q9QZB0; -.
DR   Ensembl; ENSMUST00000019909; ENSMUSP00000019909; ENSMUSG00000019775.
DR   Ensembl; ENSMUST00000064225; ENSMUSP00000065825; ENSMUSG00000019775.
DR   Ensembl; ENSMUST00000117676; ENSMUSP00000113519; ENSMUSG00000019775.
DR   GeneID; 56533; -.
DR   KEGG; mmu:56533; -.
DR   UCSC; uc007egg.1; mouse.
DR   CTD; 56533; -.
DR   MGI; MGI:1927469; Rgs17.
DR   eggNOG; roNOG04999; -.
DR   GeneTree; ENSGT00560000076525; -.
DR   HOVERGEN; HBG013233; -.
DR   InParanoid; Q9QZB0; -.
DR   OrthoDB; EOG418BPC; -.
DR   NextBio; 312890; -.
DR   ArrayExpress; Q9QZB0; -.
DR   Bgee; Q9QZB0; -.
DR   CleanEx; MM_RGS17; -.
DR   Genevestigator; Q9QZB0; -.
DR   GermOnline; ENSMUSG00000019775; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; TAS:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; TAS:MGI.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000342; Regulat_G_prot_signal.
DR   InterPro; IPR016137; Regulat_G_prot_signal_superfam.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48097; Regulat_G_prot_signal_superfam; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Glycoprotein; Lipoprotein; Membrane; Nucleus; Palmitate;
KW   Phosphoprotein; Signal transduction inhibitor; Ubl conjugation.
FT   CHAIN         1    210       Regulator of G-protein signaling 17.
FT                                /FTId=PRO_0000204225.
FT   DOMAIN       84    200       RGS.
FT   COMPBIAS     28     40       Poly-Cys.
FT   MOD_RES     137    137       Phosphotyrosine.
SQ   SEQUENCE   210 AA;  24345 MW;  451B868679E5B9B0 CRC64;
     MRKRQQSQNE GTQAVSQAPG NQRPNNTCCF CWCCCCSCSC LTVRNEERGD SSGRSPHTTK
     MESIQVLEEC QNPTADEVLS WSQNFDKMMK TPAGRNLFRE FLRTEYSEEN LLFWLACEDL
     KKEQNKKAVE EKARMIYEDY ISILSPKEVS LDSRVREVIN RSLLDPSPHM YEDAQLQIYT
     LMHRDSFPRF LNSQIYKAFV ESTTSCTSES
//
ID   RGS20_MOUSE             Reviewed;         239 AA.
AC   Q9QZB1; Q14A97; Q3TY63; Q9CUV8; Q9QZB2;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Regulator of G-protein signaling 20;
DE            Short=RGS20;
DE   AltName: Full=Regulator of G-protein signaling Z1;
GN   Name=Rgs20; Synonyms=Rgsz1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-32.
RC   STRAIN=129/B6, and BALB/c;
RA   Barker S.A., Wang J., Ross E.M.;
RT   "A mouse ortholog of RGSZ1.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, AND GLYCOSYLATION.
RX   PubMed=14997173; DOI=10.1038/sj.npp.1300408;
RA   Garzan J., Rodriguez-Munoz M., Lopez-Fando A., Garcia-Espana A.,
RA   Sanchez-Blazquez P.;
RT   "RGSZ1 and GAIP regulate mu- but not delta-opioid receptors in mouse
RT   CNS: role in tachyphylaxis and acute tolerance.";
RL   Neuropsychopharmacology 29:1091-1104(2004).
RN   [5]
RP   INTERACTION WITH OPRM1, TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=15827571; DOI=10.1038/sj.npp.1300726;
RA   Garzan J., Rodriguez-Munoz M., Lopez-Fando A., Sanchez-Blazquez P.;
RT   "The RGSZ2 protein exists in a complex with mu-opioid receptors and
RT   regulates the desensitizing capacity of Gz proteins.";
RL   Neuropsychopharmacology 30:1632-1648(2005).
RN   [6]
RP   SUMOYLATION, PHOSPHORYLATION, AND FUNCTION.
RX   PubMed=16900103; DOI=10.1038/sj.npp.1301184;
RA   Rodriguez-Munoz M., Bermudez D., Sanchez-Blazquez P., Garzon J.;
RT   "Sumoylated RGS-Rz proteins act as scaffolds for mu-opioid receptors
RT   and G-protein complexes in mouse brain.";
RL   Neuropsychopharmacology 32:842-850(2007).
CC   -!- FUNCTION: Inhibits signal transduction by increasing the GTPase
CC       activity of G protein alpha subunits thereby driving them into
CC       their inactive GDP-bound form. Binds selectively to G(z)-alpha and
CC       G(alpha)-i2 subunits, accelerates their GTPase activity and
CC       regulates their signaling activities. The G(z)-alpha activity is
CC       inhibited by the phosphorylation and palmitoylation of the G-
CC       protein. Negatively regulates mu-opioid receptor-mediated
CC       activation of the G-proteins.
CC   -!- SUBUNIT: Forms a complex with G(alpha)z/i2 subunits and mu-opioid
CC       receptors; the formation of this complex results in mu-opioid
CC       receptor desensitization. Interacts with OPRM1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor. Nucleus. Cytoplasm.
CC       Note=Shuttles between the cytoplasm/cell membrane and the nucleus
CC       Anchored to the membrane through palmitoylation (By similarity).
CC   -!- PTM: Fatty acylated. Heavily palmitoylated in the cysteine string
CC       motif (By similarity).
CC   -!- PTM: N- and O-glycosylated in synapsomal membranes.
CC   -!- PTM: Serine phosphorylated in synapsomal membranes.
CC   -!- PTM: Sumoylated by SUMO1, SUMO2 and SUMO3. Sumoylation increases
CC       binding to the G-proteins, G(alpha)-i2 and G(z), and interaction
CC       with mu-opioid receptors.
CC   -!- SIMILARITY: Contains 1 RGS domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB28987.2; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF191554; AAF05757.1; -; mRNA.
DR   EMBL; AF191552; AAF05756.1; -; mRNA.
DR   EMBL; AK013773; BAB28987.2; ALT_INIT; mRNA.
DR   EMBL; AK158864; BAE34700.1; -; mRNA.
DR   EMBL; BC116925; AAI16926.1; -; mRNA.
DR   EMBL; BC116929; AAI16930.1; -; mRNA.
DR   IPI; IPI00317037; -.
DR   RefSeq; NP_067349.2; NM_021374.4.
DR   UniGene; Mm.103771; -.
DR   ProteinModelPortal; Q9QZB1; -.
DR   SMR; Q9QZB1; 102-229.
DR   STRING; Q9QZB1; -.
DR   PhosphoSite; Q9QZB1; -.
DR   PRIDE; Q9QZB1; -.
DR   Ensembl; ENSMUST00000002533; ENSMUSP00000002533; ENSMUSG00000002459.
DR   GeneID; 58175; -.
DR   KEGG; mmu:58175; -.
DR   UCSC; uc007afk.1; mouse.
DR   CTD; 58175; -.
DR   MGI; MGI:1929866; Rgs20.
DR   GeneTree; ENSGT00560000076525; -.
DR   HOVERGEN; HBG013233; -.
DR   OMA; MRKRQMA; -.
DR   OrthoDB; EOG4VQ9QF; -.
DR   PhylomeDB; Q9QZB1; -.
DR   NextBio; 314115; -.
DR   ArrayExpress; Q9QZB1; -.
DR   Bgee; Q9QZB1; -.
DR   CleanEx; MM_RGS20; -.
DR   Genevestigator; Q9QZB1; -.
DR   GermOnline; ENSMUSG00000002459; Mus musculus.
DR   GO; GO:0005794; C:Golgi apparatus; TAS:MGI.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; TAS:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; TAS:MGI.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000342; Regulat_G_prot_signal.
DR   InterPro; IPR016137; Regulat_G_prot_signal_superfam.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48097; Regulat_G_prot_signal_superfam; 1.
DR   PROSITE; PS50132; RGS; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Glycoprotein; Lipoprotein; Membrane; Nucleus; Palmitate;
KW   Phosphoprotein; Polymorphism; Signal transduction inhibitor;
KW   Ubl conjugation.
FT   CHAIN         1    239       Regulator of G-protein signaling 20.
FT                                /FTId=PRO_0000204234.
FT   DOMAIN      113    229       RGS.
FT   COMPBIAS     59     71       Poly-Cys.
FT   VARIANT      32     32       M -> R (in strain: BALB/c).
SQ   SEQUENCE   239 AA;  26986 MW;  F383923163A44D18 CRC64;
     MRTANGGPRA RASPSASPAD PGLPEGSERT EMRMRQMCGG SETQGPAPSQ QGGRGSNACC
     FCWCCCCTCS CLTVRNQEDQ RPQRASHEIR TDIPACEESP TPTLEEVCAW AQSFDNLMVT
     PAGRNAFREF LRTEFSEENM LFWMACEELK REANKSTIEE KARIIYEDYI SILSPKEVSL
     DSRVREVINR NMVDPSQHIF DDAQLQIYTL MHRDSYPRFM NSTVYKDLLT SLAEKTVEA
//
ID   PLXC1_MOUSE             Reviewed;        1574 AA.
AC   Q9QZC2; Q8CGW1;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Plexin-C1;
DE   AltName: Full=Virus-encoded semaphorin protein receptor;
DE   AltName: CD_antigen=CD232;
DE   Flags: Precursor;
GN   Name=Plxnc1; Synonyms=Vespr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Bradshaw J.D., Comeau M.C., Spriggs M.K.;
RT   "Mouse homolog of human viral-encoded semaphorin protein receptor
RT   (VESPR).";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1205.
RC   STRAIN=129/Sv;
RX   MEDLINE=99026139; PubMed=9806843; DOI=10.1006/geno.1998.5540;
RA   Horvat S., Medrano J.F.;
RT   "A 500-kb YAC and BAC contig encompassing the high-growth deletion in
RT   mouse chromosome 10 and identification of the murine Raidd/Cradd gene
RT   in the candidate region.";
RL   Genomics 54:159-164(1998).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=15967782; DOI=10.1093/intimm/dxh274;
RA   Walzer T., Galibert L., De Smedt T.;
RT   "Dendritic cell function in mice lacking Plexin C1.";
RL   Int. Immunol. 17:943-950(2005).
RN   [4]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=15611227;
RA   Walzer T., Galibert L., Comeau M.R., De Smedt T.;
RT   "Plexin C1 engagement on mouse dendritic cells by viral semaphorin
RT   A39R induces actin cytoskeleton rearrangement and inhibits integrin-
RT   mediated adhesion and chemokine-induced migration.";
RL   J. Immunol. 174:51-59(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-984, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Receptor for SEMA7A, for vaccinia virus semaphorin A39R
CC       and for herpesvirus Sema protein. Binding of semaphorins triggers
CC       cellular responses leading to the rearrangement of the
CC       cytoskeleton and to secretion of IL6 and IL8 (By similarity).
CC   -!- SUBUNIT: Monomer. Homodimer. Interacts with SEMA7A (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- TISSUE SPECIFICITY: Detected on dendritic cells, skin Langerhans
CC       cells and neutrophils (at protein level).
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC   -!- SIMILARITY: Belongs to the plexin family.
CC   -!- SIMILARITY: Contains 1 Sema domain.
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DR   EMBL; AF190578; AAF01334.1; -; mRNA.
DR   EMBL; AE016754; AAN84620.1; -; Genomic_DNA.
DR   IPI; IPI00674255; -.
DR   RefSeq; NP_061267.1; NM_018797.2.
DR   UniGene; Mm.256712; -.
DR   ProteinModelPortal; Q9QZC2; -.
DR   SMR; Q9QZC2; 37-508, 584-621, 662-758, 976-1568.
DR   STRING; Q9QZC2; -.
DR   PhosphoSite; Q9QZC2; -.
DR   PRIDE; Q9QZC2; -.
DR   Ensembl; ENSMUST00000099337; ENSMUSP00000096939; ENSMUSG00000074785.
DR   GeneID; 54712; -.
DR   KEGG; mmu:54712; -.
DR   UCSC; uc007gvz.2; mouse.
DR   CTD; 54712; -.
DR   MGI; MGI:1890127; Plxnc1.
DR   GeneTree; ENSGT00560000076899; -.
DR   HOGENOM; HBG714508; -.
DR   HOVERGEN; HBG082153; -.
DR   InParanoid; Q9QZC2; -.
DR   OMA; ADVCRNI; -.
DR   OrthoDB; EOG4VQ9NM; -.
DR   NextBio; 311556; -.
DR   ArrayExpress; Q9QZC2; -.
DR   Bgee; Q9QZC2; -.
DR   CleanEx; MM_PLXNC1; -.
DR   Genevestigator; Q9QZC2; -.
DR   GermOnline; ENSMUSG00000074785; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:InterPro.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002909; IPT_TIG_rcpt.
DR   InterPro; IPR003659; Plexin-like.
DR   InterPro; IPR016201; Plexin-like_fold.
DR   InterPro; IPR013548; Plexin_cytoplasmic_RasGAP_dom.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR001627; Semaphorin/CD100_Ag.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF08337; Plexin_cytopl; 1.
DR   Pfam; PF01437; PSI; 1.
DR   Pfam; PF01833; TIG; 2.
DR   SMART; SM00429; IPT; 2.
DR   SMART; SM00423; PSI; 2.
DR   SUPFAM; SSF81296; Ig_E-set; 1.
DR   SUPFAM; SSF103575; Plexin-like_fold; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   SUPFAM; SSF101912; Sema; 1.
DR   PROSITE; PS51004; SEMA; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Receptor;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     34       Potential.
FT   CHAIN        35   1574       Plexin-C1.
FT                                /FTId=PRO_0000232750.
FT   TOPO_DOM     35    950       Extracellular (Potential).
FT   TRANSMEM    951    971       Helical; (Potential).
FT   TOPO_DOM    972   1574       Cytoplasmic (Potential).
FT   DOMAIN       35    452       Sema.
FT   MOD_RES     984    984       Phosphoserine.
FT   MOD_RES    1472   1472       Phosphothreonine (By similarity).
FT   CARBOHYD     86     86       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    143    143       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    149    149       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    252    252       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    386    386       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    407    407       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    694    694       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    773    773       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    802    802       N-linked (GlcNAc...) (Potential).
FT   DISULFID     64     87       By similarity.
FT   DISULFID    156    194       By similarity.
FT   DISULFID    283    329       By similarity.
FT   DISULFID    455    472       By similarity.
FT   DISULFID    461    506       By similarity.
FT   DISULFID    464    481       By similarity.
FT   DISULFID    475    487       By similarity.
SQ   SEQUENCE   1574 AA;  176474 MW;  FA8B5E5C6239FFEA CRC64;
     MEVSRRKTPP RPPYPAAPLP LIAYLLALAA PARGADEPVW RSEQAIGAIA ASRADGVFVA
     SGSCLDQLDY SLKNRLSRLY RDQAGNCTEP VSLAPPARPR PGSSFSKLLL PYREGATGLE
     GLLLTGWTFD RGACEVRPLG NLNRSSLRNG TEVVSCHPQG STAGVVYRAS GTDLWYLAVA
     ATYVLPEPET ANRCNPAASD RDTAIALKNT EGRSLATQEL GRLKLRGSAG SLHFVDAFLW
     NGSVYFPYYP YNYTSGAATG WPSMARIAQS TEVLFQGQAA LDCDHGHPEG RRLLLSSSLV
     EAVDIWAGVF SAATGEGQER RSPATTALCL FRMSEIQAHA RSCSWDFQAT EHNCKEGDRP
     ERVQPIASST LIHSDLTSVY GTVVMNRTVL FLGTGDGQLL KVVLGENLTS NCPEVIYEIK
     EETPVFYKLV PHPMKNIYIY LTAGKEVRRI PVANCSKRKS CSECLAAADP HCGWCLPLQR
     CTFQGDCTHA GSFENWLDIS SGPKKCPKIQ ILRSLRERTT VTIVGSISAR HSECVVKNAD
     TGKLLCQGRS QLNWTCACNI PSRPSYNVLV VNATFSFPSW NLSERFNFTN CASLKECPAC
     IRSGCAWCKR DKKCIHPFTP CEPSDYERNQ ELCQVAVEKS PKDSGGGRVK ESKRNRTDGA
     VQVFYIKAIE PQKISTLGKS NVIVTGANFT QASNITMILR GTSTCERDVI RVSHVLNDTH
     MKFSLPSSRK EMKDVCIQFD GGTCSSAGAL SYIALPHCSL IVPATTWISG GQNITIMGRN
     FDVIDNLIIS HELKGNANVN INVSEYCAAT FCRFLAPNLK SSKVRTNVAV KLRVQDTYLD
     CGTLQYLEDP RFTGYRVESE IDTELEVKIQ KENDNFNISK DDIDITLFHG ENKQFNCSFE
     NITRNQDLTT ILCKIKSIKN ANTIASSSKK VRVKLGNLEL YVEQESVPST WYFLIALPIL
     LAIVIVVAVV VTRYKSKELS RKQSQQLELL ESELRKEIRD GFAELQMDKL DVVDSFGTVP
     FLDYKHFALR TFFPESGGFT HIFTEDMHNR DANDKNESLT ALDALICNKS FLVTVIHTLE
     KQKNFSVKDR CLFASFLTIA LQTKLVYLTS ILEVLTRDLM EQCSNMQPKL MLRRTESVVE
     KLLTNWMSVC LSGFLRETVG EPFYLLVTTL NQKINKGPVD VITCKALYTL NEDWLLWQVP
     EFNTVALNVV FEKIPENESA DVCRNISVNV LDCDTIGQAK EKVFQAFLSK NGSPYGLQLN
     EIGLELQVGT RQKELLDIDS SSVILEDGIT KLNTIGHYEI SNGSTIKVFK KIANFTSDVE
     YSDDHCHLIL PDSEAFQVVQ GKRHRGKHKF KVKEMYLTKL LSTKVAIHSV LEKLFRSIWS
     LPNSRAPFAI KYFFDFLDAQ AENKKITDPD VVHIWKTNSL PLRFWVNILK NPQFVFDIKK
     TPHIDSCLSV IAQAFMDAFS LTEQQLGKEA PTNKLLYAKD IPTYKEEVKS YYKAIRDLPP
     LSSLEMEEFL TQESKKHENE FNEEVALTEI YKYIVKYFDE ILNKLERERG LEEAQKQLLH
     VKVLFDEKKK CKWM
//
ID   RAE2_MOUSE              Reviewed;         621 AA.
AC   Q9QZD5; Q0VF88; Q8CH16;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   08-MAR-2011, entry version 65.
DE   RecName: Full=Rab proteins geranylgeranyltransferase component A 2;
DE   AltName: Full=Choroideraemia-like protein;
DE   AltName: Full=Rab escort protein 2;
DE            Short=REP-2;
GN   Name=Chml; Synonyms=Rep2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RA   Gegg M., Tolmachova T., Seabra M.C.;
RT   "Cloning and sequencing of the mouse REP2 gene.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=12242008; DOI=10.1016/S0378-1119(02)00799-0;
RA   Kasper G., Taudien S., Staub E., Mennerich D., Rieder M., Hinzmann B.,
RA   Dahl E., Schwidetzky U., Rosenthal A., Rump A.;
RT   "Different structural organization of the encephalopsin gene in man
RT   and mouse.";
RL   Gene 295:27-32(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Binds unprenylated Rab proteins, presents it to the
CC       catalytic Rab GGTase dimer, and remains bound to it after the
CC       geranylgeranyl transfer reaction. The component A is thought to be
CC       regenerated by transferring its prenylated Rab back to the donor
CC       membrane. Less effective than REP-1 in supporting prenylation of
CC       Rab3 family (By similarity).
CC   -!- SUBUNIT: Monomer. Interacts with Rab and Rab GGTase (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the Rab GDI family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF189156; AAF01059.1; -; Genomic_DNA.
DR   EMBL; AF482427; AAO15718.1; -; Genomic_DNA.
DR   EMBL; BC118932; AAI18933.1; -; mRNA.
DR   IPI; IPI00270187; -.
DR   RefSeq; NP_067325.2; NM_021350.2.
DR   UniGene; Mm.440490; -.
DR   ProteinModelPortal; Q9QZD5; -.
DR   SMR; Q9QZD5; 3-619.
DR   PhosphoSite; Q9QZD5; -.
DR   PRIDE; Q9QZD5; -.
DR   Ensembl; ENSMUST00000104984; ENSMUSP00000100600; ENSMUSG00000078185.
DR   GeneID; 12663; -.
DR   KEGG; mmu:12663; -.
DR   CTD; 12663; -.
DR   MGI; MGI:101913; Chml.
DR   GeneTree; ENSGT00530000063044; -.
DR   HOGENOM; HBG357363; -.
DR   HOVERGEN; HBG004961; -.
DR   InParanoid; Q9QZD5; -.
DR   OrthoDB; EOG441QBB; -.
DR   PhylomeDB; Q9QZD5; -.
DR   Bgee; Q9QZD5; -.
DR   CleanEx; MM_CHML; -.
DR   Genevestigator; Q9QZD5; -.
DR   GO; GO:0005968; C:Rab-protein geranylgeranyltransferase complex; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0004663; F:Rab geranylgeranyltransferase activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR   InterPro; IPR018203; GDP_dissociation_inhibitor.
DR   InterPro; IPR001738; Rab_escort.
DR   InterPro; IPR002005; Rab_GDI_REP.
DR   InterPro; IPR016664; Rab_geranylTrfase_A_euk.
DR   PANTHER; PTHR11787; Rab_GDI_REP; 1.
DR   Pfam; PF00996; GDI; 2.
DR   PIRSF; PIRSF016550; Rab_ger_ger_transf_A_euk; 1.
DR   PRINTS; PR00893; RABESCORT.
DR   PRINTS; PR00891; RABGDIREP.
PE   2: Evidence at transcript level;
KW   GTPase activation.
FT   CHAIN         1    621       Rab proteins geranylgeranyltransferase
FT                                component A 2.
FT                                /FTId=PRO_0000056690.
FT   CONFLICT    351    351       T -> P (in Ref. 1; AAF01059).
FT   CONFLICT    361    361       N -> T (in Ref. 2; AAO15718).
SQ   SEQUENCE   621 AA;  70010 MW;  F198A7489F9D5D6E CRC64;
     MAEKLPTEFD VVIIGTGLPE SILAAACSRS GQRVLHVDSR SYYGGNWASF SFTGLQSWLK
     DYQQNHDSEE GVTATWQDLI HETEEAISLR KKDETIQHTE VFCYASQDVE DSVQDTETLQ
     RSSPLEASAT PADSLDSASL PKERQSAYST SYEVPSRHTE ESDRELSLPS ANVEDSLEKE
     KYCGDKTDMH TVSGEDKGEH KLVVQDSIEQ PKRNRITYSQ MVKESRRFNI DLVSKPLYSQ
     GSLIDLLIKS NVSRYAEFKN VTRILAFWEG KVEQVPCSRA DVFNSKELSM VEKRMLMKFL
     TFCLDYEQHS DEYQDFKQCS FSDYLKTKKL TPNLQHFILH SIAMTSESSC TTLDGLQATK
     NFLQCLGRFG NTPFIFPLYG HGEIPQCFCR MCAVFGGVYC LRHKVQCLVV DKDSGRCKGI
     IDAFGQRISA NYFIVEDSYL PKETCSNVQY KQISRAVLIT DQSILKTDSD QQISILVVPP
     LEPGTTSVRV MELCSSTMTC MKDSYLVHLT CSSSKTARED LEPVVKQLFI PEAEAEAGKD
     ELRKPRLLWA LYFNMRDSSG VSRSSYCGLP SNVYICSGPD WGLGSEHAVK QAETLFQEIF
     PSEEFCPPPP NPEDIIFEAE G
//
ID   EIF3I_MOUSE             Reviewed;         325 AA.
AC   Q9QZD9;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit I;
DE            Short=eIF3i;
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 2;
DE   AltName: Full=TGF-beta receptor-interacting protein 1;
DE            Short=TRIP-1;
DE   AltName: Full=eIF-3-beta;
DE   AltName: Full=eIF3 p36;
GN   Name=Eif3i; Synonyms=Eif3s2, Trip1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Zhou A., Silverman R.H.;
RT   "Mouse TRIP-1 gene isolated from murine L-929 cells.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Joseph P., Fan L., Whong W.-Z., Ong T.-M.;
RT   "Mus musculus TGF-beta receptor interacting protein 1 (TRIP1).";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Embryonic stem cell, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 269-280.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [6]
RP   INTERACTION WITH EIF3B AND EIF4G1.
RX   PubMed=16541103; DOI=10.1038/sj.emboj.7601047;
RA   Harris T.E., Chi A., Shabanowitz J., Hunt D.F., Rhoads R.E.,
RA   Lawrence J.C. Jr.;
RT   "mTOR-dependent stimulation of the association of eIF4G and eIF3 by
RT   insulin.";
RL   EMBO J. 25:1659-1668(2006).
RN   [7]
RP   CHARACTERIZATION OF THE EIF-3 COMPLEX, IDENTIFICATION IN THE EIF-3
RP   COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17581632; DOI=10.1038/sj.emboj.7601765;
RA   Masutani M., Sonenberg N., Yokoyama S., Imataka H.;
RT   "Reconstitution reveals the functional core of mammalian eIF3.";
RL   EMBO J. 26:3373-3383(2007).
CC   -!- FUNCTION: Component of the eukaryotic translation initiation
CC       factor 3 (eIF-3) complex, which is required for several steps in
CC       the initiation of protein synthesis. The eIF-3 complex associates
CC       with the 40S ribosome and facilitates the recruitment of eIF-1,
CC       eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S
CC       preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA
CC       recruitment to the 43S PIC and scanning of the mRNA for AUG
CC       recognition. The eIF-3 complex is also required for disassembly
CC       and recycling of posttermination ribosomal complexes and
CC       subsequently prevents premature joining of the 40S and 60S
CC       ribosomal subunits prior to initiation.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor
CC       3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B,
CC       EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K,
CC       EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable
CC       modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I;
CC       module B is composed of EIF3F, EIF3H, and EIF3M; and module C is
CC       composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module
CC       C binds EIF3B of module A and EIF3H of module B, thereby linking
CC       the three modules. EIF3J is a labile subunit that binds to the
CC       eIF-3 complex via EIF3B. The eIF-3 complex may interact with
CC       RPS6KB1 under conditions of nutrient depletion. Mitogenic
CC       stimulation may lead to binding and activation of a complex
CC       composed of MTOR and RPTOR, leading to phosphorylation and release
CC       of RPS6KB1 and binding of EIF4B to eIF-3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- PTM: Phosphorylated by TGF-beta type II receptor (By similarity).
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit I family.
CC   -!- SIMILARITY: Contains 5 WD repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF188297; AAF01455.1; -; mRNA.
DR   EMBL; AF271072; AAF76199.1; -; mRNA.
DR   EMBL; AK012375; BAB28197.1; -; mRNA.
DR   EMBL; AK002896; BAB22440.1; -; mRNA.
DR   EMBL; AK010781; BAB27177.1; -; mRNA.
DR   EMBL; BC029625; AAH29625.1; -; mRNA.
DR   IPI; IPI00269613; -.
DR   RefSeq; NP_061269.1; NM_018799.2.
DR   UniGene; Mm.250874; -.
DR   ProteinModelPortal; Q9QZD9; -.
DR   SMR; Q9QZD9; 5-316.
DR   MINT; MINT-1869798; -.
DR   STRING; Q9QZD9; -.
DR   PhosphoSite; Q9QZD9; -.
DR   REPRODUCTION-2DPAGE; Q9QZD9; -.
DR   PRIDE; Q9QZD9; -.
DR   Ensembl; ENSMUST00000102593; ENSMUSP00000099653; ENSMUSG00000028798.
DR   GeneID; 54709; -.
DR   KEGG; mmu:54709; -.
DR   NMPDR; fig|10090.3.peg.10442; -.
DR   UCSC; uc008uxm.1; mouse.
DR   CTD; 54709; -.
DR   MGI; MGI:1860763; Eif3i.
DR   GeneTree; ENSGT00530000063490; -.
DR   HOGENOM; HBG525604; -.
DR   HOVERGEN; HBG000900; -.
DR   InParanoid; Q9QZD9; -.
DR   OMA; GHFGPLN; -.
DR   OrthoDB; EOG4HX519; -.
DR   PhylomeDB; Q9QZD9; -.
DR   NextBio; 311544; -.
DR   ArrayExpress; Q9QZD9; -.
DR   Bgee; Q9QZD9; -.
DR   Genevestigator; Q9QZD9; -.
DR   GermOnline; ENSMUSG00000028798; Mus musculus.
DR   GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 4.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Initiation factor;
KW   Isopeptide bond; Phosphoprotein; Protein biosynthesis; Repeat;
KW   Ubl conjugation; WD repeat.
FT   CHAIN         1    325       Eukaryotic translation initiation factor
FT                                3 subunit I.
FT                                /FTId=PRO_0000051037.
FT   REPEAT        8     47       WD 1.
FT   REPEAT       50     91       WD 2.
FT   REPEAT      144    183       WD 3.
FT   REPEAT      186    225       WD 4.
FT   REPEAT      283    324       WD 5.
FT   MOD_RES     264    264       N6-acetyllysine (By similarity).
FT   MOD_RES     308    308       Phosphotyrosine (By similarity).
FT   CROSSLNK    282    282       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
SQ   SEQUENCE   325 AA;  36461 MW;  2B29405772675CC0 CRC64;
     MKPILLQGHE RSITQIKYNR EGDLLFTVAK DPIVNVWYSV NGERLGTYMG HTGAVWCVDA
     DWDTKHVLTG SADNSCRLWD CETGKQLALL KTNSAVRTCG FDFGGNIIMF STDKQMGYQC
     FVSFFDLRDP SQIDSNEPYM KIPCNDSKIT SAVWGPLGEC VIAGHESGEL NQYSAKSGEV
     LVNVKEHSRQ INDIQLSRDM TMFVTASKDN TAKLFDSTTL EHQKTFRTER PVNSAALSPN
     YDHVVLGGGQ EAMDVTTTST RIGKFEARFF HLAFEEEFGR VKGHFGPINS VAFHPDGKSY
     SSGGEDGYVR IHYFDPQYFE FEFEA
//
ID   SERC1_MOUSE             Reviewed;         453 AA.
AC   Q9QZI8; Q3UZ93;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=Serine incorporator 1;
DE   AltName: Full=Axotomy-induced glyco/Golgi protein 2;
DE   AltName: Full=Membrane protein TMS-2;
DE   AltName: Full=Tumor differentially expressed protein 1-like;
DE   AltName: Full=Tumor differentially expressed protein 2;
GN   Name=Serinc1; Synonyms=Aigp2, Tde1l, Tde2, Tms2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20105325; PubMed=10637174;
RA   Grossman T.R., Luque J.M., Nelson N.;
RT   "Identification of a ubiquitous family of membrane proteins and their
RT   expression in mouse brain.";
RL   J. Exp. Biol. 203:447-457(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Li H., Aoki S., Hara Y., Wada K.;
RT   "An axotomy activated gene, mouse AIGP1: genomic organization,
RT   transcriptional regulation and genetic mapping on chromosome 2.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Cerebellum, Hippocampus, Kidney, Pituitary,
RC   Sympathetic ganglion, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Enhances the incorporation of serine into
CC       phosphatidylserine and sphingolipids (By similarity).
CC   -!- SUBUNIT: Interacts with SPTLC1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in the neuronal populations
CC       such as Purkinje cells in the cerebellum, brainstem and spinal
CC       motor neurons, locus coeruleus and raphe nuclei.
CC   -!- SIMILARITY: Belongs to the TDE1 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF181685; AAD54421.1; -; mRNA.
DR   EMBL; AB078030; BAC05512.1; -; Genomic_DNA.
DR   EMBL; AK002847; BAB22403.1; -; mRNA.
DR   EMBL; AK005203; BAB23881.1; -; mRNA.
DR   EMBL; AK088340; BAC40293.1; -; mRNA.
DR   EMBL; AK133668; BAE21775.1; -; mRNA.
DR   EMBL; AK133975; BAE21964.1; -; mRNA.
DR   EMBL; AK135359; BAE22504.1; -; mRNA.
DR   EMBL; AK141574; BAE24743.1; -; mRNA.
DR   EMBL; AK148745; BAE28654.1; -; mRNA.
DR   EMBL; AK159280; BAE34958.1; -; mRNA.
DR   EMBL; AK159436; BAE35082.1; -; mRNA.
DR   EMBL; BC017148; AAH17148.1; -; mRNA.
DR   IPI; IPI00137465; -.
DR   RefSeq; NP_062734.1; NM_019760.3.
DR   UniGene; Mm.29344; -.
DR   ProteinModelPortal; Q9QZI8; -.
DR   PhosphoSite; Q9QZI8; -.
DR   PRIDE; Q9QZI8; -.
DR   Ensembl; ENSMUST00000020027; ENSMUSP00000020027; ENSMUSG00000019877.
DR   GeneID; 56442; -.
DR   KEGG; mmu:56442; -.
DR   UCSC; uc007fcm.1; mouse.
DR   CTD; 56442; -.
DR   MGI; MGI:1926228; Serinc1.
DR   eggNOG; roNOG05819; -.
DR   GeneTree; ENSGT00550000074522; -.
DR   HOGENOM; HBG446824; -.
DR   HOVERGEN; HBG025699; -.
DR   InParanoid; Q9QZI8; -.
DR   OMA; VNCDVLV; -.
DR   OrthoDB; EOG4S4PGF; -.
DR   PhylomeDB; Q9QZI8; -.
DR   NextBio; 312638; -.
DR   ArrayExpress; Q9QZI8; -.
DR   Bgee; Q9QZI8; -.
DR   CleanEx; MM_SERINC1; -.
DR   Genevestigator; Q9QZI8; -.
DR   GermOnline; ENSMUSG00000019877; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:HGNC.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0015194; F:L-serine transmembrane transporter activity; ISS:HGNC.
DR   GO; GO:0006658; P:phosphatidylserine metabolic process; ISS:HGNC.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0051347; P:positive regulation of transferase activity; ISS:HGNC.
DR   GO; GO:0006665; P:sphingolipid metabolic process; ISS:HGNC.
DR   InterPro; IPR005016; TMS_TDE.
DR   PANTHER; PTHR10383; TMS_TDE; 1.
DR   Pfam; PF03348; Serinc; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Lipid metabolism; Membrane;
KW   Phospholipid biosynthesis; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    453       Serine incorporator 1.
FT                                /FTId=PRO_0000218967.
FT   TOPO_DOM      1     88       Extracellular (Potential).
FT   TRANSMEM     89    109       Helical; (Potential).
FT   TOPO_DOM    110    123       Cytoplasmic (Potential).
FT   TRANSMEM    124    144       Helical; (Potential).
FT   TOPO_DOM    145    151       Extracellular (Potential).
FT   TRANSMEM    152    172       Helical; (Potential).
FT   TOPO_DOM    173    197       Cytoplasmic (Potential).
FT   TRANSMEM    198    218       Helical; (Potential).
FT   TOPO_DOM    219    231       Extracellular (Potential).
FT   TRANSMEM    232    252       Helical; (Potential).
FT   TOPO_DOM    253    259       Cytoplasmic (Potential).
FT   TRANSMEM    260    280       Helical; (Potential).
FT   TOPO_DOM    281    309       Extracellular (Potential).
FT   TRANSMEM    310    330       Helical; (Potential).
FT   TOPO_DOM    331    387       Cytoplasmic (Potential).
FT   TRANSMEM    388    408       Helical; (Potential).
FT   TOPO_DOM    409    426       Extracellular (Potential).
FT   TRANSMEM    427    447       Helical; (Potential).
FT   TOPO_DOM    448    453       Cytoplasmic (Potential).
FT   MOD_RES     351    351       Phosphoserine (By similarity).
FT   MOD_RES     352    352       Phosphothreonine (By similarity).
FT   MOD_RES     361    361       Phosphoserine (By similarity).
FT   MOD_RES     364    364       Phosphoserine.
FT   MOD_RES     410    410       Phosphotyrosine (By similarity).
FT   MOD_RES     413    413       Phosphoserine (By similarity).
SQ   SEQUENCE   453 AA;  50509 MW;  0FE8718FA3EA62B7 CRC64;
     MGSVLGLCSV ASWIPCLCGS APCLLCRCCP SGNNSTVTRL IYALFLLVGV CVACVMLIPG
     MEEQLNKIPG FCENEKGVVP CNILVGYKAV YRLCFGLAMF YLLLSLLMIK VKSSSDPRAA
     VHNGFWFFKF ATAVAIIIGA FFIPEGTFTT VWFYVGMAGA FCFILIQLVL LIDFAHSWNE
     SWVEKMEEGN SRCWYAALLS ATALNYLLSL VAVVLFFVYY THPASCAENK AFISVNMLLC
     IGASVMSILP KIQESQPRSG LLQSSVITVY TMYLTWSAMT NEPETNCNPS LLSIIGFNTT
     RPIPKDGQSV QWWHPQGIIG LVLFLLCVFY SSIRTSNNSQ VNKLTLTSDE STLIEDGNGR
     SDGSLDDGDG IHRAVDNERD GVTYSYSFFH FMLFLASLYI MMTLTNWYRY EPSREMKSQW
     TAVWVKISSS WIGLVLYVWT LVAPLVLTNR DFD
//
ID   UBP21_MOUSE             Reviewed;         566 AA.
AC   Q9QZL6; Q9D0R1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-FEB-2011, entry version 84.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 21;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 21;
DE   AltName: Full=Ubiquitin thiolesterase 21;
DE   AltName: Full=Ubiquitin-specific-processing protease 21;
GN   Name=Usp21; Synonyms=Usp23;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20246307; PubMed=10786635; DOI=10.1016/S0167-4781(99)00233-X;
RA   Smith T.S., Southan C.;
RT   "Sequencing, tissue distribution and chromosomal assignment of a novel
RT   ubiquitin-specific protease USP23.";
RL   Biochim. Biophys. Acta 1490:184-188(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-221; HIS-519 AND
RP   ASP-535.
RX   PubMed=18172164; DOI=10.1101/gad.1609708;
RA   Nakagawa T., Kajitani T., Togo S., Masuko N., Ohdan H., Hishikawa Y.,
RA   Koji T., Matsuyama T., Ikura T., Muramatsu M., Ito T.;
RT   "Deubiquitylation of histone H2A activates transcriptional initiation
RT   via trans-histone cross-talk with H3K4 di- and trimethylation.";
RL   Genes Dev. 22:37-49(2008).
CC   -!- FUNCTION: Deubiquitinates histone H2A, a specific tag for
CC       epigenetic transcriptional repression, thereby acting as a
CC       coactivator. Deubiquitination of histone H2A releaves the
CC       repression of di- and trimethylation of histone H3 at 'Lys-4',
CC       resulting in regulation of transcriptional initiation. Regulates
CC       gene expression via histone H2A deubiquitination. Also capable of
CC       removing NEDD8 from NEDD8 conjugates but has no effect on Sentrin-
CC       1 conjugates.
CC   -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. USP21 subfamily.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF177759; AAD54322.1; -; mRNA.
DR   EMBL; AK011148; BAB27431.1; -; mRNA.
DR   EMBL; BC021903; AAH21903.1; -; mRNA.
DR   IPI; IPI00137577; -.
DR   RefSeq; NP_038947.2; NM_013919.4.
DR   UniGene; Mm.27510; -.
DR   ProteinModelPortal; Q9QZL6; -.
DR   SMR; Q9QZL6; 210-559.
DR   STRING; Q9QZL6; -.
DR   MEROPS; C19.034; -.
DR   PhosphoSite; Q9QZL6; -.
DR   PRIDE; Q9QZL6; -.
DR   Ensembl; ENSMUST00000111305; ENSMUSP00000106936; ENSMUSG00000053483.
DR   Ensembl; ENSMUST00000111306; ENSMUSP00000106938; ENSMUSG00000053483.
DR   GeneID; 30941; -.
DR   KEGG; mmu:30941; -.
DR   UCSC; uc007dnt.1; mouse.
DR   CTD; 30941; -.
DR   MGI; MGI:1353665; Usp21.
DR   eggNOG; roNOG10239; -.
DR   GeneTree; ENSGT00600000084018; -.
DR   HOVERGEN; HBG011164; -.
DR   PhylomeDB; Q9QZL6; -.
DR   BRENDA; 3.1.2.15; 244.
DR   NextBio; 307382; -.
DR   ArrayExpress; Q9QZL6; -.
DR   Bgee; Q9QZL6; -.
DR   CleanEx; MM_USP21; -.
DR   Genevestigator; Q9QZL6; -.
DR   GermOnline; ENSMUSG00000053483; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019784; F:NEDD8-specific protease activity; ISS:UniProtKB.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IDA:UniProtKB.
DR   GO; GO:0004843; F:ubiquitin-specific protease activity; ISS:UniProtKB.
DR   GO; GO:0016578; P:histone deubiquitination; IDA:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR018200; Pept_C19ubi-hydrolase_C_CS.
DR   InterPro; IPR001394; Peptidase_C19.
DR   Pfam; PF00443; UCH; 1.
DR   PROSITE; PS00972; UCH_2_1; 1.
DR   PROSITE; PS00973; UCH_2_2; 1.
DR   PROSITE; PS50235; UCH_2_3; 1.
PE   1: Evidence at protein level;
KW   Activator; Chromatin regulator; Hydrolase; Metal-binding; Nucleus;
KW   Protease; Thiol protease; Transcription; Transcription regulation;
KW   Ubl conjugation pathway; Zinc.
FT   CHAIN         1    566       Ubiquitin carboxyl-terminal hydrolase 21.
FT                                /FTId=PRO_0000080649.
FT   ACT_SITE    221    221       Nucleophile.
FT   ACT_SITE    519    519       Proton acceptor (By similarity).
FT   METAL       385    385       Zinc (By similarity).
FT   METAL       388    388       Zinc (By similarity).
FT   METAL       438    438       Zinc (By similarity).
FT   METAL       441    441       Zinc (By similarity).
FT   MUTAGEN     221    221       C->A: Abolishes ability to deubiquitinate
FT                                histone H2A and ability to regulate
FT                                transcription.
FT   MUTAGEN     519    519       H->A: Abolishes ability to deubiquitinate
FT                                histone H2A and ability to regulate
FT                                transcription.
FT   MUTAGEN     535    535       D->N: Abolishes ability to deubiquitinate
FT                                histone H2A and ability to regulate
FT                                transcription.
FT   CONFLICT    220    220       T -> TLPQ (in Ref. 2; BAB27431).
FT   CONFLICT    338    338       R -> C (in Ref. 2; BAB27431).
SQ   SEQUENCE   566 AA;  62673 MW;  F2E1828E9BDB1AFD CRC64;
     MPQASEHRLG RTREPPVNVQ PRVGAKIPFP PRARSKERRN PVPGPNSMLR PLPPRPGPPD
     ERLKKLELGR GRTSGSRPRG PLRADHGVPL PGSPPPAVAL PLPSRTNLAR SKSVSSGDLR
     PMGIALGGHR GAGELGAALS RLALRPEPPT LRRSTSLRRL GGFPGPPTLL SIRTEPPTSH
     GSFHMISARP SEPFYSDDKM AHHTLLLGSG HVGLRNLGNT CFLNAVLQCL SSTRPLRDFC
     LRRDFRQEVP GGGRAQELTE AFADVIGALW HPDSCEAVNP TRFRAVFQKY VPSFSGYSQQ
     DAQEFLKLLM ERLHLEINRR GRRAPPILAS GPVPSPPRRG GGALHEEPEL SDDDRANLMW
     KRYLEREDSK IVDLFVGQLK SCLKCQACGY RSTTFEVFCD LSLPIPKKGF AGGKVSLRDC
     FSLFTKEEEL ESENAPVCDR CRQKTRSTKK LTVQRFPRIL VLHLNRFSTS RGSIKKSSVG
     VDFPLQRLSL GDFASDKAGS PVYQLYALCN HSGSVHYGHY TALCRCQTGW HVYNDSRVSP
     VSENQVASSE GYVLFYQLMQ EPLRCL
//
ID   UBQL2_MOUSE             Reviewed;         638 AA.
AC   Q9QZM0; Q7TSJ8; Q8VDH9;
DT   29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Ubiquilin-2;
DE   AltName: Full=Chap1;
DE   AltName: Full=DSK2 homolog;
DE   AltName: Full=Protein linking IAP with cytoskeleton 2;
DE            Short=PLIC-2;
DE   AltName: Full=Ubiquitin-like product Chap1/Dsk2;
GN   Name=Ubqln2; Synonyms=Plic2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND INTERACTION WITH CD47.
RC   STRAIN=Swiss Webster / NIH; TISSUE=Embryo;
RX   PubMed=10549293; DOI=10.1016/S1097-2765(00)80212-9;
RA   Wu A.-L., Wang J., Zheleznyak A., Brown E.J.;
RT   "Ubiquitin-related proteins regulate interaction of vimentin
RT   intermediate filaments with the plasma membrane.";
RL   Mol. Cell 4:619-625(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Increases the half-life of proteins destined to be
CC       degraded by the proteasome; may modulate proteasome-mediated
CC       protein degradation (By similarity). Links CD47 to vimentin-
CC       containing intermediate filaments of the cytoskeleton.
CC   -!- SUBUNIT: Binds UBE3A and BTRC. Interacts with the 19S proteasome
CC       subunit (By similarity). Binds CD47.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Membrane.
CC       Note=Associated with fibers and membrane-associated.
CC   -!- TISSUE SPECIFICITY: Highly expressed in smooth muscle. Expression
CC       in other tissues is very low.
CC   -!- SIMILARITY: Contains 1 UBA domain.
CC   -!- SIMILARITY: Contains 1 ubiquitin-like domain.
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DR   EMBL; AF177346; AAF01366.1; -; mRNA.
DR   EMBL; BC021824; AAH21824.1; -; mRNA.
DR   EMBL; BC053022; AAH53022.1; -; mRNA.
DR   IPI; IPI00387416; -.
DR   RefSeq; NP_061268.2; NM_018798.2.
DR   UniGene; Mm.430772; -.
DR   ProteinModelPortal; Q9QZM0; -.
DR   SMR; Q9QZM0; 1-103, 587-635.
DR   STRING; Q9QZM0; -.
DR   PhosphoSite; Q9QZM0; -.
DR   PRIDE; Q9QZM0; -.
DR   Ensembl; ENSMUST00000060714; ENSMUSP00000056888; ENSMUSG00000050148.
DR   GeneID; 54609; -.
DR   KEGG; mmu:54609; -.
DR   UCSC; uc009uqw.1; mouse.
DR   CTD; 54609; -.
DR   MGI; MGI:1860283; Ubqln2.
DR   eggNOG; roNOG04362; -.
DR   GeneTree; ENSGT00390000005720; -.
DR   HOGENOM; HBG560425; -.
DR   HOVERGEN; HBG064537; -.
DR   InParanoid; Q9QZM0; -.
DR   OrthoDB; EOG48KRBD; -.
DR   PhylomeDB; Q9QZM0; -.
DR   NextBio; 311408; -.
DR   ArrayExpress; Q9QZM0; -.
DR   Bgee; Q9QZM0; -.
DR   CleanEx; MM_UBQLN2; -.
DR   Genevestigator; Q9QZM0; -.
DR   GermOnline; ENSMUSG00000050148; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR006636; STI1_HS-bd.
DR   InterPro; IPR009060; UBA-like.
DR   InterPro; IPR000449; UBA/transl_elong_EF1B_N.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   InterPro; IPR015496; Ubiquilin.
DR   InterPro; IPR000626; Ubiquitin.
DR   InterPro; IPR019955; Ubiquitin_supergroup.
DR   PANTHER; PTHR10677; Ubiquilin; 1.
DR   Pfam; PF00627; UBA; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SMART; SM00727; STI1; 4.
DR   SMART; SM00165; UBA; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   SUPFAM; SSF46934; UBA_like; 1.
DR   PROSITE; PS50030; UBA; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; FALSE_NEG.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Membrane; Nucleus; Phosphoprotein; Repeat.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    638       Ubiquilin-2.
FT                                /FTId=PRO_0000211012.
FT   DOMAIN       33    107       Ubiquitin-like.
FT   REPEAT      505    507       1.
FT   REPEAT      508    510       2.
FT   REPEAT      511    513       3.
FT   REPEAT      514    516       4.
FT   REPEAT      517    519       5.
FT   REPEAT      520    522       6.
FT   REPEAT      523    525       7.
FT   REPEAT      526    528       8.
FT   REPEAT      529    531       9.
FT   REPEAT      532    533       10.
FT   REPEAT      535    537       11.
FT   DOMAIN      589    635       UBA.
FT   REGION      505    537       11 X 3 AA tandem repeats P-X-X.
FT   COMPBIAS     10     30       Pro-rich.
FT   COMPBIAS    113    152       Thr-rich.
FT   COMPBIAS    336    361       Ser/Thr-rich.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      25     25       Phosphoserine.
FT   CONFLICT    179    179       R -> Q (in Ref. 2; AAH21824/AAH53022).
FT   CONFLICT    362    362       Missing (in Ref. 2; AAH21824).
SQ   SEQUENCE   638 AA;  67379 MW;  D439873D1A1A706B CRC64;
     MAENGESSGP PRPSRGPAAA PGAASPPAEP KIIKVTVKTP KEKEEFAVPE NSTVQQFKEA
     ISKRFKSQTD QLVLIFAGKI LKDQDTLMQH GIHDGLTVHL VIKSQNRPQG QATTQPSTTA
     GTSTTTTTTT TAAAPAATTS SAPRSSSTPT TTNSSSFGLG SLSSLSNLGL NSPNFTELRN
     QMQQQLLASP EMMIQIMENP FVQSMLSNPD LMRQLIMANP QMQQLIQRNP EISHLLNNPD
     IMRQTLEIAR NPAMMQEMMR NQDLALSNLE SIPGGYNALR RMYTDIQEPM LNAAQEQFGG
     NPFATVGSSS TSGEGTQPSR TENRDPLPNP WAPPPTTQTA ATTTTTTTTS SGSGSGSSSS
     STTAGNTMAA ANYVASIFST PGMQSLLQQI TENPQLIQNM LSAPYMRSMM QSLSQNPDMA
     AQMMLSSPLF TSNPQLQEQM RPQLPNFLQQ MQNPETIAAM SNPRAMQALM QIQQGLQTLA
     TEAPGLIPSF APGVGMGVLG TAITPVGPVT PIGPIGPIVP FTPIGPIGPI GPTGPASSPG
     STGTGIPPAT TVSSSAPTET ISPTSESGPN QQFIQQMVQA LTGGSPPQPP NPEVRFQQQL
     EQLNAMGFLN REANLQALIA TGGDINAAIE RLLGSQPS
//
ID   NPAS3_MOUSE             Reviewed;         925 AA.
AC   Q9QZQ0; Q9EQP4;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Neuronal PAS domain-containing protein 3;
DE            Short=Neuronal PAS3;
DE   AltName: Full=Basic-helix-loop-helix-PAS protein MOP6;
DE   AltName: Full=Member of PAS protein 6;
GN   Name=Npas3; Synonyms=Mop6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20005801; PubMed=10534623; DOI=10.1016/S0925-4773(99)00182-3;
RA   Brunskill E.W., Witte D.P., Shreiner A.B., Potter S.S.;
RT   "Characterization of Npas3, a novel basic helix-loop-helix PAS gene
RT   expressed in the developing mouse nervous system.";
RL   Mech. Dev. 88:237-241(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 141-280.
RA   Thomas R.S., Bradfield C.A.;
RT   "Cloning and chromosomal localization of MOP6.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15347806; DOI=10.1073/pnas.0405310101;
RA   Erbel-Sieler C., Dudley C., Zhou Y., Wu X., Estill S.J., Han T.,
RA   Diaz-Arrastia R., Brunskill E.W., Potter S.S., McKnight S.L.;
RT   "Behavioral and regulatory abnormalities in mice deficient in the
RT   NPAS1 and NPAS3 transcription factors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13648-13653(2004).
CC   -!- FUNCTION: May play a broad role in neurogenesis. May control
CC       regulatory pathways relevant to schizophrenia and to psychotic
CC       illness.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another
CC       bHLH protein.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Detected exclusively in adult brain in
CC       inhibitory interneurons.
CC   -!- DEVELOPMENTAL STAGE: Expression detected between 9.5 and 11.5 dpc
CC       in the developing neural tube. Was also expressed throughout the
CC       neuroepithelium of the developing central nervous system between
CC       10. 5 and 12.5 dpc at 14.5 dpc, the expression became restricted
CC       to the neopallial layer of the cortex. At 12.5 dpc, expression was
CC       evident in nonneural tissues such as the developing dermis and
CC       mesenchyme surrounding the otic and nasal placodes. Expression was
CC       also detected in the developing cardiac valves, limb and
CC       developing kidney.
CC   -!- SIMILARITY: Contains 1 basic helix-loop-helix (bHLH) domain.
CC   -!- SIMILARITY: Contains 1 PAC (PAS-associated C-terminal) domain.
CC   -!- SIMILARITY: Contains 2 PAS (PER-ARNT-SIM) domains.
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DR   EMBL; AF173871; AAF14283.1; -; mRNA.
DR   EMBL; AF168769; AAG35181.1; -; mRNA.
DR   IPI; IPI00137835; -.
DR   UniGene; Mm.247044; -.
DR   UniGene; Mm.466545; -.
DR   ProteinModelPortal; Q9QZQ0; -.
DR   SMR; Q9QZQ0; 59-110, 166-216, 333-443.
DR   PhosphoSite; Q9QZQ0; -.
DR   PRIDE; Q9QZQ0; -.
DR   Ensembl; ENSMUST00000021396; ENSMUSP00000021396; ENSMUSG00000021010.
DR   UCSC; uc007nno.1; mouse.
DR   MGI; MGI:1351610; Npas3.
DR   GeneTree; ENSGT00590000082805; -.
DR   HOGENOM; HBG444582; -.
DR   HOVERGEN; HBG052656; -.
DR   InParanoid; Q9QZQ0; -.
DR   OrthoDB; EOG4M0F1J; -.
DR   ArrayExpress; Q9QZQ0; -.
DR   Bgee; Q9QZQ0; -.
DR   CleanEx; MM_NPAS3; -.
DR   Genevestigator; Q9QZQ0; -.
DR   GermOnline; ENSMUSG00000021010; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0030528; F:transcription regulator activity; IEA:InterPro.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0042711; P:maternal behavior; IMP:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   GO; GO:0035176; P:social behavior; IMP:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR011598; HLH_DNA-bd.
DR   InterPro; IPR001092; HLH_DNA-bd_dom.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR013655; PAS_fold_3.
DR   Gene3D; G3DSA:4.10.280.10; HLH_DNA_bd; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   SMART; SM00353; HLH; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF47459; HLH_basic; 1.
DR   PROSITE; PS50888; HLH; 1.
DR   PROSITE; PS50113; PAC; FALSE_NEG.
DR   PROSITE; PS50112; PAS; 2.
PE   2: Evidence at transcript level;
KW   DNA-binding; Nucleus; Repeat; Transcription; Transcription regulation.
FT   CHAIN         1    925       Neuronal PAS domain-containing protein 3.
FT                                /FTId=PRO_0000127409.
FT   DOMAIN       76    112       Helix-loop-helix motif.
FT   DOMAIN      152    222       PAS 1.
FT   DOMAIN      324    394       PAS 2.
FT   DOMAIN      398    441       PAC.
FT   DNA_BIND     59     75       Basic motif.
FT   COMPBIAS    236    244       Poly-Ser.
FT   COMPBIAS    706    709       Poly-Gly.
FT   COMPBIAS    760    771       Poly-Gly.
FT   CONFLICT    141    141       R -> L (in Ref. 2; AAG35181).
FT   CONFLICT    156    156       G -> E (in Ref. 2; AAG35181).
FT   CONFLICT    166    166       F -> L (in Ref. 2; AAG35181).
SQ   SEQUENCE   925 AA;  100458 MW;  B6B07C9B6755B938 CRC64;
     MGRAGAAANG TPQNVQGITS YQQRITAQHP LPNQSECRKI YRYDGIYCES TYQNLQALRK
     EKSRDAARSR RGKENFEFYE LAKLLPLPAA ITSQLDKASI IRLTISYLKM RDFANQGDPP
     WNLRMEGPPP NTSVKGAQRR RSPSALAIEV FEAHLGSHIL QSLDGFVFAL NQEGKFLYIS
     ETVSIYLGLS QVELTGSSVF DYVHPGDHVE MAEQLGMKLP PGRGLLSQGT TEDAASSASS
     SSQSETPEPV ETTSPSLLTT DNTLERSFFI RMKSTLTKRG VHIKSSGYKV IHITGRLRLR
     VPLSHGRTVP SQIMGLVVVA HALPPPTINE VRIDCHMFVT RVNMDLNIIY CENRISDYMD
     LTPVDIVGKR CYHFIHAEDV EGIRHSHLDL LNKGQCVTKY YRWMQKNGGY IWIQSSATIA
     INAKNANEKN IIWVNYLLSN PEYKDTPMDI AQLPHLPEKA SESSETSDSE SDSKDTSGIT
     EDNENSKSDE KGNQSENSED PEPDRKKSGS ACDNDMNCND DGHSSSNPDS RDSDDSFEHS
     DFEHPKAAED GFGALGPMQI KVERYVESEA DLRLQPCESL TSDSAKDSDS ANEAGAQASS
     KHQKRKRRRK RQKGGSASRR RLSSASSPGL DAGLVEPPRL LSSPHSASVL KIKTEIAEPI
     NFDNESSIWN YPPNREISRN ESPYSMTKPP TSEHFPSPQG QGGSIGGGGA LHVAIPDSVL
     TPPGADGTAG RKTQFSGTAP VPSDPLSPPL SASPRDKHPG GGAGSGGGGP GASNSLLYTG
     DLEALQRLQA GNVVLPLVHR VTGTLAATST AAQRVYTTGT IRYAPAEVTL AMQGNLLPNA
     HAVNFVDVNS PGFGLDPKTP MEMLYHHVHR LNMSGPFGGA VSAASLTQMP GGNVFTTAEG
     LFSTLPFPVY SNGIHAAQTL ERKED
//
ID   AFAD_MOUSE              Reviewed;        1820 AA.
AC   Q9QZQ1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 3.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Afadin;
DE   AltName: Full=Protein Af-6;
GN   Name=Mllt4; Synonyms=Af6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-320 (ISOFORM 1), FUNCTION, TISSUE
RP   SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=C57BL/6;
RX   MEDLINE=99408792; PubMed=10477764; DOI=10.1083/jcb.146.5.1117;
RA   Ikeda W., Nakanishi H., Miyoshi J., Mandai K., Ishizaki H., Tanaka M.,
RA   Togawa A., Takahashi K., Nishioka H., Yoshida H., Mizoguchi A.,
RA   Nishikawa S., Takai Y.;
RT   "Afadin: a key molecule essential for structural organization of cell-
RT   cell junctions of polarized epithelia during embryogenesis.";
RL   J. Cell Biol. 146:1117-1132(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-900 (ISOFORM 3).
RC   TISSUE=Leukemia;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   INTERACTION WITH PVRL3.
RX   MEDLINE=20209403; PubMed=10744716; DOI=10.1074/jbc.275.14.10291;
RA   Satoh-Horikawa K., Nakanishi H., Takahashi K., Miyahara M.,
RA   Nishimura M., Tachibana K., Mizoguchi A., Takai Y.;
RT   "Nectin-3: a new member of immunoglobulin-like cell adhesion molecules
RT   that shows homophilic and heterophilic cell-cell adhesion
RT   activities.";
RL   J. Biol. Chem. 275:10291-10299(2000).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107; SER-1182 AND
RP   SER-1275, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1107 AND SER-1182, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [7]
RP   STRUCTURE BY NMR OF 246-487.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the FHA domain and RAS-binding domain in mouse
RT   AF-6 protein.";
RL   Submitted (JUL-2005) to the PDB data bank.
CC   -!- FUNCTION: Belongs to an adhesion system, probably together with
CC       the E-cadherin-catenin system, which plays a role in the
CC       organization of homotypic, interneuronal and heterotypic cell-cell
CC       adherens junctions (AJs). Nectin- and actin-filament-binding
CC       protein that connects nectin to the actin cytoskeleton. May play a
CC       key role in the organization of epithelial structures of the
CC       embryonic ectoderm.
CC   -!- SUBUNIT: Homodimer. Interacts with F-actin, nectin and
CC       PVRL3/nectin-3. Essential for the association of nectin and E-
CC       cadherin. Isoform 2/s-afadin does not interact with F-actin.
CC       Interacts with ZO-1 and occludin, but probably in an indirect
CC       manner. Interacts with RIT1, RIT2, NRXN1 and BCR (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, adherens junction. Note=Not
CC       found at cell-matrix AJs.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=3;
CC         IsoId=Q9QZQ1-3; Sequence=Displayed;
CC       Name=1; Synonyms=l-afadin;
CC         IsoId=Q9QZQ1-2; Sequence=VSP_026731;
CC       Name=2; Synonyms=s-afadin;
CC         IsoId=Q9QZQ1-1; Sequence=Not described;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is expressed only in a restricted
CC       set of epithelial structures during early embryogenesis.
CC   -!- DEVELOPMENTAL STAGE: Highly expressed at restricted set of
CC       epithelial structures and highly concentrated at their junctional
CC       complex regions. At E6.5, localized at the most apical regions of
CC       cell-cell adhesion sites of the entire embryonic ectoderm; not
CC       detected in the extraembryonic regions. At E7.0, expressed in the
CC       primitive streak and the migrating paraxial mesoderm. At E7.5,
CC       highly expressed at the junctional complex regions in the
CC       primitive streak region (neuroepithelium) and the neural
CC       fold/grove region, but hardly detected in other areas of the
CC       ectoderm. By E8.5, highly expressed in the tail bud, somites and
CC       the paraxial mesoderm, concentrated at the junctional complex
CC       regions in neural tube, somites and pericardioperitoneal canal.
CC   -!- DISRUPTION PHENOTYPE: Mice show developmental defects at stages
CC       during and after gastrulation, including disorganization of the
CC       ectoderm, impaired migration of the mesoderm and loss of somites
CC       and other structures derived from both the ectoderm and mesoderm.
CC       Cell-cell adherens juntions and tight junctions are improperly
CC       organized in the ectoderm-derived cells. No redundancy exists in
CC       the function of afadin during gastrulation.
CC   -!- SIMILARITY: Contains 1 dilute domain.
CC   -!- SIMILARITY: Contains 1 FHA domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 2 Ras-associating domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; AC155253; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CAAA01106165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CAAA01134612; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CAAA01201738; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CAAA01218165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF172447; AAD54283.1; -; mRNA.
DR   EMBL; AK016557; -; NOT_ANNOTATED_CDS; mRNA.
DR   IPI; IPI00845596; -.
DR   IPI; IPI00853902; -.
DR   RefSeq; NP_034936.1; NM_010806.1.
DR   UniGene; Mm.472105; -.
DR   PDB; 1WLN; NMR; -; A=381-502.
DR   PDB; 1WXA; NMR; -; A=246-348.
DR   PDBsum; 1WLN; -.
DR   PDBsum; 1WXA; -.
DR   ProteinModelPortal; Q9QZQ1; -.
DR   SMR; Q9QZQ1; 11-138, 249-348, 381-502, 1001-1096.
DR   STRING; Q9QZQ1; -.
DR   PhosphoSite; Q9QZQ1; -.
DR   PRIDE; Q9QZQ1; -.
DR   Ensembl; ENSMUST00000139666; ENSMUSP00000118318; ENSMUSG00000068036.
DR   GeneID; 17356; -.
DR   KEGG; mmu:17356; -.
DR   UCSC; uc008ams.1; mouse.
DR   CTD; 17356; -.
DR   MGI; MGI:1314653; Mllt4.
DR   GeneTree; ENSGT00390000006525; -.
DR   HOVERGEN; HBG050463; -.
DR   InParanoid; Q9QZQ1; -.
DR   NextBio; 291962; -.
DR   ArrayExpress; Q9QZQ1; -.
DR   Bgee; Q9QZQ1; -.
DR   Genevestigator; Q9QZQ1; -.
DR   GermOnline; ENSMUSG00000068036; Mus musculus.
DR   GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR   GO; GO:0005913; C:cell-cell adherens junction; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0050839; F:cell adhesion molecule binding; IPI:BHF-UCL.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR018444; Dil_domain.
DR   InterPro; IPR002710; Dilute.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR000159; Ras-assoc.
DR   InterPro; IPR008984; SMAD_FHA_domain.
DR   Gene3D; G3DSA:2.60.200.20; FHA; 1.
DR   Pfam; PF01843; DIL; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00788; RA; 2.
DR   SMART; SM00240; FHA; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00314; RA; 2.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF49879; SMAD_FHA; 1.
DR   PROSITE; PS51126; DILUTE; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; FALSE_NEG.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50200; RA; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell adhesion; Cell junction;
KW   Coiled coil; Phosphoprotein; Repeat.
FT   CHAIN         1   1820       Afadin.
FT                                /FTId=PRO_0000215919.
FT   DOMAIN       39    133       Ras-associating 1.
FT   DOMAIN      246    348       Ras-associating 2.
FT   DOMAIN      426    492       FHA.
FT   DOMAIN      653    908       Dilute.
FT   DOMAIN     1007   1093       PDZ.
FT   COILED      146    186       Potential.
FT   COILED     1410   1446       Potential.
FT   COILED     1523   1561       Potential.
FT   COILED     1593   1665       Potential.
FT   COMPBIAS    163    175       Glu/Lys-rich.
FT   COMPBIAS   1346   1392       Pro-rich.
FT   COMPBIAS   1676   1706       Pro-rich.
FT   COMPBIAS   1733   1736       Poly-Glu.
FT   MOD_RES      94     94       Phosphotyrosine (By similarity).
FT   MOD_RES     216    216       Phosphoserine (By similarity).
FT   MOD_RES     557    557       Phosphoserine (By similarity).
FT   MOD_RES    1083   1083       Phosphoserine (By similarity).
FT   MOD_RES    1107   1107       Phosphoserine.
FT   MOD_RES    1172   1172       Phosphoserine (By similarity).
FT   MOD_RES    1173   1173       Phosphoserine (By similarity).
FT   MOD_RES    1182   1182       Phosphoserine.
FT   MOD_RES    1201   1201       Phosphoserine (By similarity).
FT   MOD_RES    1230   1230       Phosphotyrosine (By similarity).
FT   MOD_RES    1232   1232       Phosphothreonine (By similarity).
FT   MOD_RES    1275   1275       Phosphoserine.
FT   MOD_RES    1330   1330       Phosphothreonine (By similarity).
FT   MOD_RES    1334   1334       Phosphothreonine (By similarity).
FT   MOD_RES    1510   1510       Phosphoserine (By similarity).
FT   MOD_RES    1694   1694       Phosphoserine (By similarity).
FT   MOD_RES    1696   1696       Phosphoserine (By similarity).
FT   MOD_RES    1719   1719       Phosphoserine (By similarity).
FT   MOD_RES    1795   1795       Phosphoserine (By similarity).
FT   VAR_SEQ     393    407       Missing (in isoform 1).
FT                                /FTId=VSP_026731.
FT   CONFLICT     23     23       N -> Y (in Ref. 2; AAD54283).
FT   CONFLICT    101    101       E -> EE (in Ref. 3; AK016557).
FT   CONFLICT    694    694       N -> D (in Ref. 3; AK016557).
FT   CONFLICT    897    900       DLIE -> PEMR (in Ref. 3; AK016557).
FT   STRAND      249    252
FT   TURN        255    257
FT   STRAND      259    261
FT   STRAND      264    267
FT   HELIX       274    285
FT   STRAND      288    290
FT   TURN        292    294
FT   STRAND      295    301
FT   STRAND      308    311
FT   STRAND      315    317
FT   HELIX       325    330
FT   HELIX       334    336
FT   STRAND      339    345
FT   STRAND      418    420
FT   STRAND      423    427
FT   STRAND      429    431
FT   STRAND      450    457
FT   STRAND      459    464
FT   STRAND      466    468
FT   STRAND      470    474
FT   STRAND      481    483
FT   STRAND      488    491
FT   TURN        492    494
FT   STRAND      495    500
SQ   SEQUENCE   1820 AA;  206499 MW;  9FA4F378D840D8B1 CRC64;
     MSAGGRDEER RKLADIIHHW NANRLDLFEI SQPTEDLEFH GVMRFYFQDK AAGNFATKCI
     RVSSTATTQD VIETLAEKFR PDMRMLSSPK YSLYEVHVSG ERRLDIDEKP LVVQLNWNKD
     DREGRFVLKN ENDAIPAKKA QSNGPEKQEK EGVIQNFKRT LSKKEKKEKK KKEKEALRQA
     SDKEERPSQG DDSENSRLAA EVYKDMPETS FTRTISNPEV VMKRRRQQKL EKRMQEFRSS
     DGRPDSGGTL RIYADSLKPN IPYKTILLST TDTADFAVAE SLEKYGLEKE NPKDYCIARV
     MLPPGAQHSD ERGAKEIILD DDECPLQIFR EWPSDKGILV FQLKRRPPDY IPKKMKKHVE
     GKSLKGKDRA DGSGYGSALP PEKLPYLVEL SPGRRNHFAY YSYHTYEDGS DSRDKPKLYR
     LQLSVTEVGT EKFDDNSIQL FGPGIQPHHC DLTNMDGVVT VTPRSMDAET YVDGQRISET
     TMLQSGMRLQ FGTSHVFKFV DPIQDHVLSK RSVDGGLMVK GPRHKPGAVQ ETTFELGGDV
     HSGTALPASR STTRLDSDRV SSASSTAERG MVKPMIRLDQ EQEYRRRENR TQDATGPELI
     LPASIEFRES SEDSFLSAII NYTNSSTVHF KLSPTYVLYM ACRYVLSSQH RPDISPTERT
     HKAIAVVNKM VSMMEGVIQK QKNIAGALAF WMANASELLN FIKQDRDLSR ITLDAQDVLA
     HLVQMAFKYL VHCLQSELNN YMPAFLDDPE ENSLQRPKID DVLHTLTGAM SLLRRCRVNA
     ALTIQLFSQL FHFINMWLFN RLVTDPDSGL CSHYWGAIIR QQLGHIEAWA EKQGLELAAD
     CHLSRIVQAT TLLTMDKYVP DDIPNINSTC FKLNSLQLQA LLQNYHCAPD EPFIPTDLIE
     NVVAVAENTA DELARSDGRD VQLEEDPDLQ LPFLLPEDGY SCDVVRNIPN GLQEFLDPLC
     QRGFCRLVPH TRSPGTWTIY FEGADYESHL MRENAELAQP LRKEPEIITV TLKKQNGMGL
     SIVAAKGAGQ DKLGIYVKSV VKGGAADVDG RLAAGDQLLS VDGRSLVGLS QERAAELMTR
     TSSVVTLEVA KQGAIYHGLA TLLNQPSPMM QRISDRRGSG KPRPKSEGFE LYNNSAQNGS
     PESPQMPWTE YSEPKKLPGD DRLMKNRADH RSSPNVANQP PSPGGKGPYT SGTAAKITSV
     STGNLCTEEQ SPPPRPEAYP IPTQTYTREY FTFPASKSQD RMAPPQSQWP NYEEKPHVHT
     ESNHSSIAIQ RVTRSQEELR EEKVYQLERH RVEAGMDRKC DSDMWINQSS SVESSTSSQE
     HLNHSSKSVT PASTLTKSGP GRWKTPAAVL PTPVAVSQPI RTDLPPPPPP PPVHYTSEFD
     GIPMDLPLPP PPANQAGPQS AQVAAAEWKK REEHQRWYEK EKARLEEERE RKRREQERKL
     GQMRSQTLNP ASFSPLATQA KPEKPSTLQR PQETVIRELQ PQQQPRTIER KDLQYITISK
     EELSSGDSLS PDPWKRDARE KLEKQQQMHI VDMLSKEIHE LQNKVDRTAE ESDRLRKLML
     EWQFQKRLQE SKQKDEDDDE EEDDDVDTML IMQRLEAERR ARMQDEERRR QQQLEEMRKR
     EAEDRVRQEE DGRHQEEERV KRDAEEKRRQ EEGYYSRLEA ERRRQHEEAA RRLLEPEEPG
     LSRPPLPRDY EPPSLSSAPC APPPPPQRNA SYLKTQVLSP DSLFTAKFVA YDEEEEDYGP
     AGPNSYSGSA GTAVGAYDAP REAREKLTRS QDADLPGSSG APENLTFKER QRLFSQGQDV
     SDKVKASRKL TELENELNTK
//
ID   H2AY_MOUSE              Reviewed;         372 AA.
AC   Q9QZQ8; Q91VZ2; Q9QZQ7;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Core histone macro-H2A.1;
DE            Short=Histone macroH2A1;
DE            Short=mH2A1;
DE   AltName: Full=H2A.y;
DE   AltName: Full=H2A/y;
GN   Name=H2afy;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF
RP   197-229 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   STRAIN=129/SvEvTacfBr;
RX   MEDLINE=99403136; PubMed=10471737; DOI=10.1093/nar/27.18.3685;
RA   Rasmussen T.P., Huang T., Mastrangelo M.-A., Loring J., Panning B.,
RA   Jaenisch R.;
RT   "Messenger RNAs encoding mouse histone macroH2A1 isoforms are
RT   expressed at similar levels in male and female cells and result from
RT   alternative splicing.";
RL   Nucleic Acids Res. 27:3685-3689(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH SPOP.
RC   TISSUE=Brain;
RX   PubMed=12183056; DOI=10.1016/S0167-4889(02)00249-5;
RA   Takahashi I., Kameoka Y., Hashimoto K.;
RT   "MacroH2A1.2 binds the nuclear protein Spop.";
RL   Biochim. Biophys. Acta 1591:63-68(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=9634239; DOI=10.1038/31275;
RA   Costanzi C., Pehrson J.R.;
RT   "Histone macroH2A1 is concentrated in the inactive X chromosome of
RT   female mammals.";
RL   Nature 393:599-601(1998).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=11262398; DOI=10.1074/jbc.M010919200;
RA   Costanzi C., Pehrson J.R.;
RT   "MACROH2A2, a new member of the MACROH2A core histone family.";
RL   J. Biol. Chem. 276:21776-21784(2001).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15564378; DOI=10.1242/cs.01537;
RA   Grigoryev S.A., Nikitina T., Pehrson J.R., Singh P.B., Woodcock C.L.;
RT   "Dynamic relocation of epigenetic chromatin markers reveals an active
RT   role of constitutive heterochromatin in the transition from
RT   proliferation to quiescence.";
RL   J. Cell Sci. 117:6153-6162(2004).
RN   [7]
RP   INTERACTION WITH HDAC1 AND HDAC2, AND FUNCTION.
RX   PubMed=16107708; DOI=10.1128/MCB.25.17.7616-7624.2005;
RA   Chakravarthy S., Gundimella S.K., Caron C., Perche P.-Y.,
RA   Pehrson J.R., Khochbin S., Luger K.;
RT   "Structural characterization of the histone variant macroH2A.";
RL   Mol. Cell. Biol. 25:7616-7624(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Variant histone H2A which replaces conventional H2A in a
CC       subset of nucleosomes where it represses transcription.
CC       Nucleosomes wrap and compact DNA into chromatin, limiting DNA
CC       accessibility to the cellular machineries which require DNA as a
CC       template. Histones thereby play a central role in transcription
CC       regulation, DNA repair, DNA replication and chromosomal stability.
CC       DNA accessibility is regulated via a complex set of post-
CC       translational modifications of histones, also called histone code,
CC       and nucleosome remodeling. Involved in stable X chromosome
CC       inactivation. Inhibits the binding of transcription factors and
CC       interferes with the activity of remodeling SWI/SNF complexes.
CC       Inhibits histone acetylation by EP300 and recruits class I HDACs,
CC       which induces an hypoacetylated state of chromatin. In addition,
CC       isoform 1, but not isoform 2, binds ADP-ribose and O-acetyl-ADP-
CC       ribose, and may be involved in ADP-ribose-mediated chromatin
CC       modulation.
CC   -!- SUBUNIT: The nucleosome is a histone octamer containing two
CC       molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
CC       heterotetramer and two H2A-H2B heterodimers. Interacts with SPOP.
CC       Part of a complex consisting of H2AFY, CUL3 and SPOP. Interacts
CC       with HDAC1 and HDAC2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Enriched in
CC       inactive X chromosome chromatin and in senescence-associated
CC       heterochromatin. In quiescent lymphocytes, associated with
CC       centromeric constitutive heterochromatin.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=2;
CC         IsoId=Q9QZQ8-1; Sequence=Displayed;
CC         Note=Major form;
CC       Name=1;
CC         IsoId=Q9QZQ8-2; Sequence=VSP_017596, VSP_017597;
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed, with high levels in
CC       testis. Present in liver, kidney and adrenal gland (at protein
CC       level). In the liver, present in hepatocytes and at a lesser
CC       extent in cells of the bile ducts. In the kidney, present in
CC       proximal and distal convoluted tubules and in straight proximal
CC       tubules. In the adrenal gland, present in inner cells of the
CC       cortex and medulla.
CC   -!- PTM: Monoubiquitinated at either Lys-116 or Lys-117. May also be
CC       polyubiquitinated. Ubiquitination is mediated by the CUL3/SPOP E3
CC       complex and does not promote proteasomal degradation. Instead, it
CC       is required for enrichment in inactive X chromosome chromatin (By
CC       similarity).
CC   -!- SIMILARITY: Contains 1 histone H2A domain.
CC   -!- SIMILARITY: Contains 1 Macro domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF171080; AAD53745.1; -; mRNA.
DR   EMBL; AF171081; AAD53746.1; -; mRNA.
DR   EMBL; AB071988; BAB68541.1; -; mRNA.
DR   EMBL; BC006955; AAH06955.1; -; mRNA.
DR   IPI; IPI00137852; -.
DR   IPI; IPI00378480; -.
DR   RefSeq; NP_001152985.1; NM_001159513.1.
DR   RefSeq; NP_001152986.1; NM_001159514.1.
DR   RefSeq; NP_001152987.1; NM_001159515.1.
DR   RefSeq; NP_036145.1; NM_012015.2.
DR   UniGene; Mm.283802; -.
DR   UniGene; Mm.478369; -.
DR   ProteinModelPortal; Q9QZQ8; -.
DR   SMR; Q9QZQ8; 10-117, 181-369.
DR   STRING; Q9QZQ8; -.
DR   PhosphoSite; Q9QZQ8; -.
DR   PRIDE; Q9QZQ8; -.
DR   Ensembl; ENSMUST00000016081; ENSMUSP00000016081; ENSMUSG00000015937.
DR   Ensembl; ENSMUST00000045788; ENSMUSP00000038221; ENSMUSG00000015937.
DR   GeneID; 26914; -.
DR   KEGG; mmu:26914; -.
DR   UCSC; uc007qsf.1; mouse.
DR   UCSC; uc007qsg.1; mouse.
DR   CTD; 26914; -.
DR   MGI; MGI:1349392; H2afy.
DR   GeneTree; ENSGT00540000069960; -.
DR   HOGENOM; HBG715905; -.
DR   HOVERGEN; HBG009342; -.
DR   InParanoid; Q9QZQ8; -.
DR   OMA; ANDEELH; -.
DR   OrthoDB; EOG4XH00N; -.
DR   PhylomeDB; Q9QZQ8; -.
DR   NextBio; 304793; -.
DR   ArrayExpress; Q9QZQ8; -.
DR   Bgee; Q9QZQ8; -.
DR   CleanEx; MM_H2AFY; -.
DR   Genevestigator; Q9QZQ8; -.
DR   GermOnline; ENSMUSG00000015937; Mus musculus.
DR   GO; GO:0005813; C:centrosome; TAS:MGI.
DR   GO; GO:0000793; C:condensed chromosome; IDA:MGI.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   InterPro; IPR002589; A1pp.
DR   InterPro; IPR021171; Core_histone_macro-H2A.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR007125; Histone_core_D.
DR   InterPro; IPR002119; Histone_H2A.
DR   Gene3D; G3DSA:1.10.20.10; Histone-fold; 1.
DR   PANTHER; PTHR23430; Histone_H2A; 1.
DR   Pfam; PF00125; Histone; 1.
DR   Pfam; PF01661; Macro; 1.
DR   PIRSF; PIRSF037942; Core_histone_macro-H2A; 1.
DR   PRINTS; PR00620; HISTONEH2A.
DR   SMART; SM00506; A1pp; 1.
DR   SMART; SM00414; H2A; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
DR   PROSITE; PS51154; MACRO; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromatin regulator; Chromosome; DNA-binding;
KW   Isopeptide bond; Methylation; Nucleosome core; Nucleus;
KW   Phosphoprotein; Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    372       Core histone macro-H2A.1.
FT                                /FTId=PRO_0000227904.
FT   DOMAIN        2    117       Histone H2A.
FT   DOMAIN      184    370       Macro.
FT   COMPBIAS    116    161       Lys-rich.
FT   MOD_RES      18     18       N6-methyllysine (By similarity).
FT   MOD_RES     123    123       N6,N6-dimethyllysine (By similarity).
FT   MOD_RES     129    129       Phosphothreonine.
FT   MOD_RES     170    170       Phosphoserine (By similarity).
FT   MOD_RES     173    173       Phosphoserine (By similarity).
FT   MOD_RES     174    174       Phosphothreonine (By similarity).
FT   MOD_RES     178    178       Phosphothreonine (By similarity).
FT   CROSSLNK    116    116       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin);
FT                                alternate (By similarity).
FT   CROSSLNK    117    117       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin);
FT                                alternate (By similarity).
FT   VAR_SEQ     198    217       NLIHSEISNLAGFEVEAIIN -> QVVQADIASIDSDAVVH
FT                                (in isoform 1).
FT                                /FTId=VSP_017596.
FT   VAR_SEQ     221    229       ADIDLKDDL -> TDFYTGGEV (in isoform 1).
FT                                /FTId=VSP_017597.
SQ   SEQUENCE   372 AA;  39735 MW;  076CF76A34FACAA0 CRC64;
     MSSRGGKKKS TKTSRSAKAG VIFPVGRMLR YIKKGHPKYR IGVGAPVYMA AVLEYLTAEI
     LELAGNAARD NKKGRVTPRH ILLAVANDEE LNQLLKGVTI ASGGVLPNIH PELLAKKRGS
     KGKLEAIITP PPAKKAKSPS QKKPVAKKTG GKKGARKSKK KQGEVSKAAS ADSTTEGTPT
     DGFTVLSTKS LFLGQKLNLI HSEISNLAGF EVEAIINPTN ADIDLKDDLG NTLEKKGGKE
     FVEAVLELRK KNGPLEVAGA AISAGHGLPA KFVIHCNSPV WGADKCEELL EKTVKNCLAL
     ADDRKLKSIA FPSIGSGRNG FPKQTAAQLI LKAISSYFVS TMSSSIKTVY FMLFDSESIG
     IYVQEMAKLD AN
//
ID   NUMB_MOUSE              Reviewed;         653 AA.
AC   Q9QZS3; P70422; Q8CIB1; Q9DC57; Q9QZR1; Q9QZS4;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-FEB-2011, entry version 95.
DE   RecName: Full=Protein numb homolog;
DE            Short=m-Nb;
DE            Short=m-Numb;
GN   Name=Numb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RX   MEDLINE=96310876; PubMed=8755477; DOI=10.1016/S0896-6273(00)80279-2;
RA   Zhong W., Feder J.N., Jiang M.-M., Jan L.Y., Jan Y.N.;
RT   "Asymmetric localization of a mammalian numb homolog during mouse
RT   cortical neurogenesis.";
RL   Neuron 17:43-53(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RX   MEDLINE=20020288; PubMed=10551880; DOI=10.1074/jbc.274.46.33097;
RA   Dho S.E., French M.B., Woods S.A., McGlade C.J.;
RT   "Characterization of four mammalian Numb protein isoforms:
RT   Identification of cytoplasmic and membrane-associated variants of the
RT   phosphotyrosine binding domain.";
RL   J. Biol. Chem. 274:33097-33104(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=Czech II; TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH LNX.
RX   MEDLINE=98204916; PubMed=9535908; DOI=10.1074/jbc.273.15.9179;
RA   Dho S.E., Jacob S., Wolting C.D., French M.B., Rohrschneider L.R.,
RA   McGlade C.J.;
RT   "The mammalian numb phosphotyrosine-binding domain. Characterization
RT   of binding specificity and identification of a novel PDZ domain-
RT   containing numb binding protein, LNX.";
RL   J. Biol. Chem. 273:9179-9187(1998).
RN   [6]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX   PubMed=10841580; DOI=10.1073/pnas.97.12.6844;
RA   Zhong W., Jiang M.M., Schonemann M.D., Meneses J.J., Pedersen R.A.,
RA   Jan L.Y., Jan Y.N.;
RT   "Mouse numb is an essential gene involved in cortical neurogenesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:6844-6849(2000).
RN   [7]
RP   UBIQUITINATION BY LNX.
RX   MEDLINE=21642151; PubMed=11782429; DOI=10.1093/emboj/21.1.93;
RA   Nie J., McGill M.A., Dermer M., Dho S.E., Wolting C.D., McGlade C.J.;
RT   "LNX functions as a RING type E3 ubiquitin ligase that targets the
RT   cell fate determinant Numb for ubiquitin-dependent degradation.";
RL   EMBO J. 21:93-102(2002).
RN   [8]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX   PubMed=12410312; DOI=10.1038/nature01124;
RA   Petersen P.H., Zou K., Hwang J.K., Jan Y.N., Zhong W.;
RT   "Progenitor cell maintenance requires numb and numblike during mouse
RT   neurogenesis.";
RL   Nature 419:929-934(2002).
RN   [9]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX   PubMed=15273690; DOI=10.1038/nn1289;
RA   Petersen P.H., Zou K., Krauss S., Zhong W.;
RT   "Continuing role for mouse Numb and Numbl in maintaining progenitor
RT   cells during cortical neurogenesis.";
RL   Nat. Neurosci. 7:803-811(2004).
RN   [10]
RP   FUNCTION, INTERACTION WITH CDH1, DISRUPTION PHENOTYPE, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=17174898; DOI=10.1016/j.cell.2006.10.041;
RA   Kuo C.T., Mirzadeh Z., Soriano-Navarro M., Rasin M., Wang D., Shen J.,
RA   Sestan N., Garcia-Verdugo J., Alvarez-Buylla A., Jan L.Y., Jan Y.N.;
RT   "Postnatal deletion of Numb/Numblike reveals repair and remodeling
RT   capacity in the subventricular neurogenic niche.";
RL   Cell 127:1253-1264(2006).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-633 AND SER-636, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [12]
RP   STRUCTURE BY NMR OF 19-172.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of phosphotyrosine interaction domain of mouse
RT   NUMB protein.";
RL   Submitted (NOV-2004) to the PDB data bank.
CC   -!- FUNCTION: Plays a role in the process of neurogenesis. Required
CC       throughout embryonic neurogenesis to maintain neural progenitor
CC       cells, also called radial glial cells (RGCs), by allowing their
CC       daughter cells to choose progenitor over neuronal cell fate. Not
CC       required for the proliferation of neural progenitor cells before
CC       the onset of neurogenesis. Also involved postnatally in the
CC       subventricular zone (SVZ) neurogenesis by regulating SVZ
CC       neuroblasts survival and ependymal wall integrity. May also
CC       mediate local repair of brain ventricular wall damage.
CC   -!- SUBUNIT: May interact with DUOXA1 (By similarity). Interacts with
CC       CDH1, EPS15, LNX and NOTCH1. Interacts with RALBP1 in a complex
CC       also containing EPN1 and TFAP2A during interphase and mitosis.
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=p72, 72 kDa;
CC         IsoId=Q9QZS3-1; Sequence=Displayed;
CC       Name=2; Synonyms=p66, 66 kDa;
CC         IsoId=Q9QZS3-2; Sequence=VSP_004351;
CC       Name=3; Synonyms=p71, 71 kDa;
CC         IsoId=Q9QZS3-3; Sequence=VSP_004350;
CC       Name=4; Synonyms=p65, 65 kDa;
CC         IsoId=Q9QZS3-4; Sequence=VSP_004350, VSP_004351;
CC   -!- TISSUE SPECIFICITY: Expressed in subventricular zone (SVZ)
CC       neuroprogenitors and ependymal cells.
CC   -!- DEVELOPMENTAL STAGE: Expressed in neural progenitors and neuron
CC       cells throughout the developing nervous system. Expressed in
CC       somites and throughout the neural tube from 8.5 dpc, onward.
CC   -!- PTM: Ubiquitinated; mediated by SIAH1 and leading to its
CC       subsequent proteasomal degradation (By similarity) Isoform 1 and
CC       isoform 2 are ubiquitinated by LNX leading to their subsequent
CC       proteasomal degradation.
CC   -!- DISRUPTION PHENOTYPE: Exhibit severe defects in cranial neuronal
CC       tube closure and die around 11.5 dpc, but neurogenesis
CC       abnormalities are limited. Mice lacking both Numb and Numbl genes
CC       die around 9.5 dpc, with severe defects in somite and vasculature
CC       formation, neuronal tube closure and axial turning. Conditional
CC       mutants, with expression abrogated in neural progenitor cells from
CC       8.5 dpc are viable, fertile and exhibit no obvious phenotypes.
CC       Conditional double-knockout (cdKO) mutants (Numb and Numbl genes),
CC       with expression abrogated in neural progenitor cells from 8.5 dpc
CC       (just before the onset of neurogenesis), display a loss of
CC       neuronal progenitor cells formation and an overexpression of
CC       neurons as neurogenesis progresses; cdKO mutants become necrotic
CC       at 12.5 dpc and die around this stage. Conditional double-knockout
CC       (cdKO) mutants (Numb and Numbl genes), with expression abrogated
CC       in neural progenitor cells from 10.5 dpc (just after the onset of
CC       neurogenesis), display a premature depletion of neural progenitor
CC       cells in the dorsal forebrain ventrical zone of the neocortex and
CC       in the hippocampal CA fields as neurogenesis progresses; cdKO
CC       mutants are viable and fertile, but showed a reduction in the
CC       thickness of the neocortex and the hippocampus and a enlargement
CC       of the lateral ventricles. Tamoxifene-inducible double-knockout
CC       (cdKO) mutants (Numb and Numbl genes), with expression abrogated
CC       postnatally in the subventricular zone (SVZ) neuroprogenitors and
CC       in ependymal cells, display a loss of SVZ neuroblasts and show a
CC       disorganized ependyma lacking both interdigitation junction
CC       between neighboring cells and increasing number of separated
CC       cells.
CC   -!- SIMILARITY: Contains 1 PID domain.
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DR   EMBL; AF169191; AAD47834.1; -; mRNA.
DR   EMBL; AF169192; AAD47835.1; -; mRNA.
DR   EMBL; AF170709; AAD47836.1; -; mRNA.
DR   EMBL; AK004553; BAB23367.1; -; mRNA.
DR   EMBL; BC033459; AAH33459.1; -; mRNA.
DR   EMBL; U70674; AAB09586.1; -; mRNA.
DR   IPI; IPI00137943; -.
DR   IPI; IPI00221542; -.
DR   IPI; IPI00221544; -.
DR   IPI; IPI00221545; -.
DR   RefSeq; NP_001129547.1; NM_001136075.1.
DR   RefSeq; NP_035079.1; NM_010949.1.
DR   UniGene; Mm.4390; -.
DR   PDB; 1WJ1; NMR; -; A=19-172.
DR   PDBsum; 1WJ1; -.
DR   ProteinModelPortal; Q9QZS3; -.
DR   SMR; Q9QZS3; 21-172.
DR   MINT; MINT-237633; -.
DR   STRING; Q9QZS3; -.
DR   PhosphoSite; Q9QZS3; -.
DR   PRIDE; Q9QZS3; -.
DR   Ensembl; ENSMUST00000021647; ENSMUSP00000021647; ENSMUSG00000021224.
DR   Ensembl; ENSMUST00000085215; ENSMUSP00000082311; ENSMUSG00000021224.
DR   Ensembl; ENSMUST00000110298; ENSMUSP00000105927; ENSMUSG00000021224.
DR   GeneID; 18222; -.
DR   KEGG; mmu:18222; -.
DR   UCSC; uc007odu.1; mouse.
DR   UCSC; uc007odv.1; mouse.
DR   UCSC; uc007odw.1; mouse.
DR   UCSC; uc007ody.1; mouse.
DR   CTD; 18222; -.
DR   MGI; MGI:107423; Numb.
DR   eggNOG; roNOG10883; -.
DR   GeneTree; ENSGT00530000062937; -.
DR   HOGENOM; HBG444693; -.
DR   HOVERGEN; HBG006672; -.
DR   InParanoid; Q9QZS3; -.
DR   OMA; VDPFEAQ; -.
DR   PhylomeDB; Q9QZS3; -.
DR   NextBio; 293644; -.
DR   ArrayExpress; Q9QZS3; -.
DR   Bgee; Q9QZS3; -.
DR   CleanEx; MM_NUMB; -.
DR   Genevestigator; Q9QZS3; -.
DR   GermOnline; ENSMUSG00000021224; Mus musculus.
DR   GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0005769; C:early endosome; IDA:MGI.
DR   GO; GO:0019897; C:extrinsic to plasma membrane; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0045294; F:alpha-catenin binding; IPI:MGI.
DR   GO; GO:0008013; F:beta-catenin binding; IPI:MGI.
DR   GO; GO:0045296; F:cadherin binding; IPI:MGI.
DR   GO; GO:0034332; P:adherens junction organization; IGI:MGI.
DR   GO; GO:0007409; P:axonogenesis; IDA:MGI.
DR   GO; GO:0021670; P:lateral ventricle development; IMP:UniProtKB.
DR   GO; GO:0021849; P:neuroblast division in subventricular zone; IMP:UniProtKB.
DR   GO; GO:0050769; P:positive regulation of neurogenesis; IMP:UniProtKB.
DR   InterPro; IPR016698; Numb/numb-like.
DR   InterPro; IPR010449; Numb_domain.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF06311; NumbF; 1.
DR   Pfam; PF00640; PID; 1.
DR   PIRSF; PIRSF017607; Numb/numb-like; 1.
DR   SMART; SM00462; PTB; 1.
DR   PROSITE; PS01179; PID; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Developmental protein; Membrane;
KW   Neurogenesis; Phosphoprotein; Ubl conjugation.
FT   CHAIN         1    653       Protein numb homolog.
FT                                /FTId=PRO_0000058002.
FT   DOMAIN       33    193       PID.
FT   MOD_RES     240    240       Phosphoserine (By similarity).
FT   MOD_RES     241    241       Phosphoserine (By similarity).
FT   MOD_RES     244    244       Phosphoserine (By similarity).
FT   MOD_RES     276    276       Phosphoserine (By similarity).
FT   MOD_RES     295    295       Phosphoserine (By similarity).
FT   MOD_RES     633    633       Phosphothreonine.
FT   MOD_RES     636    636       Phosphoserine.
FT   VAR_SEQ      68     78       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_004350.
FT   VAR_SEQ     367    415       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_004351.
FT   CONFLICT    225    225       V -> A (in Ref. 4; AAH33459).
FT   CONFLICT    362    362       S -> C (in Ref. 3; BAB23367).
FT   HELIX        26     31
FT   TURN         32     35
FT   STRAND       38     48
FT   STRAND       50     52
FT   HELIX        55     79
FT   STRAND       84     91
FT   STRAND       94     98
FT   TURN        100    102
FT   STRAND      105    107
FT   TURN        111    113
FT   STRAND      116    118
FT   STRAND      121    132
FT   STRAND      134    149
FT   HELIX       151    169
SQ   SEQUENCE   653 AA;  70813 MW;  6A2B69AA54B9A928 CRC64;
     MNKLRQSFRR KKDVYVPEAS RPHQWQTDEE GVRTGKCSFP VKYLGHVEVD ESRGMHICED
     AVKRLKAERK FFKGFFGKTG KKAVKAVLWV SADGLRVVDE KTKDLIVDQT IEKVSFCAPD
     RNFDRAFSYI CRDGTTRRWI CHCFMAVKDT GERLSHAVGC AFAACLERKQ KREKECGVTA
     TFDASRTTFT REGSFRVTTA TEQAEREEIM KQLQDAKKAE TDKTVVGPSV APGNTAPSPS
     SPTSPTPDGT ASSEMNNPHA IPRRHAPIEQ LARQGSFRGF PALSQKMSPF KRQLSLRINE
     LPSTMQRKTD FPIKNTVPEV EGEAESISSL CSQITSAFST PSEDPFSSAP MTKPVTLVAP
     QSPVLQANGT DSASHVLTAK PANTALAHVA MPVRETNPWA HVPDAANKEI AAIHPGTEWG
     QSSGAASPGL FQAGHRRTPS EADRWLEEVS KSVRAQQPQV SAAPLQPVLQ PPPPAAIAPP
     APPFQGHAFL TSQPVPVGVV PPLQPAFVPT QSYPVANGMP YPASNVPVVG ITPSQMVANV
     FGTAGHPQTT HPHQSPSLAK QQTFPQYETS SATTSPFFKP PAQHLNGSAA FNGVDNGGLA
     SGNRHAEVPP GTCPVDPFEA QWAALESKSK QRTNPSPTNP FSSDLQKTFE IEL
//
ID   SH2D3_MOUSE             Reviewed;         854 AA.
AC   Q9QZS8; A2AK84; Q9JME1;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=SH2 domain-containing protein 3C;
DE   AltName: Full=Cas/HEF1-associated signal transducer;
DE   AltName: Full=SH2 domain-containing Eph receptor-binding protein 1;
GN   Name=Sh2d3c; Synonyms=Chat, Shep1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   PHOSPHORYLATION.
RX   MEDLINE=20011387; PubMed=10542222; DOI=10.1074/jbc.274.45.31941;
RA   Dodelet V.C., Pazzagli C., Zisch A.H., Hauser C.A., Pasquale E.B.;
RT   "A novel signaling intermediate, SHEP1, directly couples Eph receptors
RT   to R-Ras and Rap1A.";
RL   J. Biol. Chem. 274:31941-31946(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH BCAR1 AND
RP   NEDD9, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   MEDLINE=20158953; PubMed=10692442; DOI=10.1074/jbc.275.9.6404;
RA   Sakakibara A., Hattori S.;
RT   "Chat, a Cas/HEF1-associated adaptor protein that integrates multiple
RT   signaling pathways.";
RL   J. Biol. Chem. 275:6404-6410(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH BCAR1; NEDD9
RP   AND PTK2B, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RC   TISSUE=Spleen;
RX   MEDLINE=22476996; PubMed=12486027; DOI=10.1074/jbc.M207942200;
RA   Sakakibara A., Hattori S., Nakamura S., Katagiri T.;
RT   "A novel hematopoietic adaptor protein, Chat-H, positively regulates T
RT   cell receptor-mediated interleukin-2 production by Jurkat cells.";
RL   J. Biol. Chem. 278:6012-6017(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-273, AND MASS
RP   SPECTROMETRY.
RX   MEDLINE=22426906; PubMed=12522270; DOI=10.1073/pnas.2436191100;
RA   Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,
RA   Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.;
RT   "Profiling of tyrosine phosphorylation pathways in human cells using
RT   mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
RN   [8]
RP   PHOSPHORYLATION AT TYR-273; TYR-278 AND TYR-787, MASS SPECTROMETRY,
RP   AND MUTAGENESIS OF TYR-787.
RX   PubMed=15272013; DOI=10.1074/jbc.M402929200;
RA   Dail M., Kalo M.S., Seddon J.A., Cote J.-F., Vuori K., Pasquale E.B.;
RT   "SHEP1 function in cell migration is impaired by a single amino acid
RT   mutation that disrupts association with the scaffolding protein cas
RT   but not with Ras GTPases.";
RL   J. Biol. Chem. 279:41892-41902(2004).
CC   -!- FUNCTION: Eph receptor-binding protein which may be a positive
CC       regulator of TCR signaling. Binding to BCAR1 is required to induce
CC       membrane ruffling and promote EGF-dependent cell migration.
CC   -!- SUBUNIT: Interacts with PTK2B. Isoform 2 interacts with BCAR1/CAS
CC       and NEDD9/HEF1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC       protein. Note=Associated with the membrane when EGF-stimulated.
CC       Found at ruffling membranes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Chat-H;
CC         IsoId=Q9QZS8-1; Sequence=Displayed;
CC       Name=2; Synonyms=Chat;
CC         IsoId=Q9QZS8-2; Sequence=VSP_017709;
CC   -!- TISSUE SPECIFICITY: Isoform 2 is ubiquitously expressed. Isoform 1
CC       is expressed in hematopoietic cells from spleen, lymph node and
CC       thymus.
CC   -!- SIMILARITY: Contains 1 Ras-GEF domain.
CC   -!- SIMILARITY: Contains 1 SH2 domain.
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DR   EMBL; AF168364; AAF13305.1; -; mRNA.
DR   EMBL; AB030442; BAA90557.1; -; mRNA.
DR   EMBL; AB043953; BAA96361.1; -; mRNA.
DR   EMBL; AK042709; BAC31340.1; -; mRNA.
DR   EMBL; AK155165; BAE33088.1; -; mRNA.
DR   EMBL; AL772271; CAM16622.1; -; Genomic_DNA.
DR   EMBL; BC113203; AAI13204.1; -; mRNA.
DR   IPI; IPI00137970; -.
DR   IPI; IPI00742349; -.
DR   RefSeq; NP_038809.1; NM_013781.2.
DR   UniGene; Mm.9593; -.
DR   ProteinModelPortal; Q9QZS8; -.
DR   SMR; Q9QZS8; 207-318.
DR   MINT; MINT-1503279; -.
DR   STRING; Q9QZS8; -.
DR   PhosphoSite; Q9QZS8; -.
DR   PRIDE; Q9QZS8; -.
DR   Ensembl; ENSMUST00000074248; ENSMUSP00000073866; ENSMUSG00000059013.
DR   Ensembl; ENSMUST00000113242; ENSMUSP00000108868; ENSMUSG00000059013.
DR   GeneID; 27387; -.
DR   KEGG; mmu:27387; -.
DR   UCSC; uc008jgp.1; mouse.
DR   UCSC; uc008jgr.1; mouse.
DR   CTD; 27387; -.
DR   MGI; MGI:1351631; Sh2d3c.
DR   GeneTree; ENSGT00390000008976; -.
DR   HOGENOM; HBG402846; -.
DR   HOVERGEN; HBG053174; -.
DR   InParanoid; Q9QZS8; -.
DR   OMA; RNCALSM; -.
DR   OrthoDB; EOG4WH8K7; -.
DR   PhylomeDB; Q9QZS8; -.
DR   NextBio; 305340; -.
DR   ArrayExpress; Q9QZS8; -.
DR   Bgee; Q9QZS8; -.
DR   CleanEx; MM_CHAT; -.
DR   CleanEx; MM_SH2D3C; -.
DR   Genevestigator; Q9QZS8; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; TAS:MGI.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR001895; RasGRF_CDC25.
DR   InterPro; IPR000980; SH2.
DR   Gene3D; G3DSA:1.10.840.10; RasGRF_CDC25; 1.
DR   Gene3D; G3DSA:3.30.505.10; SH2; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00017; SH2; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00252; SH2; 1.
DR   PROSITE; PS00720; RASGEF; FALSE_NEG.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Membrane; Phosphoprotein; SH2 domain.
FT   CHAIN         1    854       SH2 domain-containing protein 3C.
FT                                /FTId=PRO_0000228834.
FT   DOMAIN      215    314       SH2.
FT   DOMAIN      580    848       Ras-GEF.
FT   MOD_RES     178    178       Phosphotyrosine (By similarity).
FT   MOD_RES     273    273       Phosphotyrosine.
FT   MOD_RES     278    278       Phosphotyrosine.
FT   MOD_RES     787    787       Phosphotyrosine.
FT   VAR_SEQ       1    166       MTEMPKKTGRKFKFFKFKGLGSLSNLPRSFSLRRSSASASI
FT                                RSCPEPDTFEATQDDMVTLPKSPPAYARSSDMYSHMGTMPR
FT                                PNIKKAQKQQAVQKAQEVSRESHLVSRRLPEPPDLEAAKEA
FT                                GEGTEALLEDTAPSAVEVDPMRELEDLTVDTEKEQVPGDVS
FT                                PE -> MTAVGRRCSALEPR (in isoform 2).
FT                                /FTId=VSP_017709.
FT   MUTAGEN     787    787       Y->E: Disrupts binding to BCAR1 and
FT                                inhibits EGF-induced tyrosine
FT                                phosphorylation.
SQ   SEQUENCE   854 AA;  94323 MW;  FA8FC2FDEAE32FF5 CRC64;
     MTEMPKKTGR KFKFFKFKGL GSLSNLPRSF SLRRSSASAS IRSCPEPDTF EATQDDMVTL
     PKSPPAYARS SDMYSHMGTM PRPNIKKAQK QQAVQKAQEV SRESHLVSRR LPEPPDLEAA
     KEAGEGTEAL LEDTAPSAVE VDPMRELEDL TVDTEKEQVP GDVSPERTAA ELEAAGDYVK
     FSKEKYILDS SPEKLHKELE EELKLSSTDL RSHAWYHGRI PREVSETLVQ RNGDFLIRDS
     LTSLGDYVLT CRWHNQALHF KINKVVVKAG ESYTHIRYLF EQESFDHVPA LVRYHVGSRK
     AVSEQSGAII YCPVNRTFPL RYLEASYGLS QGSSKTASPA SPSGSKGSHM KRRSITMTDG
     LTTDKVTRSD GCPNSTSLPH PRDSIRNCAL SMDQIPDLHS PLSPISESPS SPAYSTVTRV
     HAPSATPSTS AQPASPVARR SSEPQLCPGN TPKPPGESDR APHASPSHTL CKASPSPSLS
     SYSDPDSGHY CQLQPPVRGS REQAAGETPR KARGSGERQK ELLENGVSDG EWGKTFTVPV
     VEATSSFNLA TFQSQLIPKE NRPLEVALLR KVKELLSEVD ARTLARHVTK VDCLVARILG
     VTKEMQTLMG VRWGMELLTL PHGRQLRLDL LERFHTMSIM LAVDILGCTG SAEERAALLH
     KTIQLAAELR GTMGNMFSFA AVMGALEMAQ ISRLEQTWMT LRQRHTEGAI LYEKKLKPFL
     KSLNEGKEGP PLSNTTFPHV LPFITLLECD SAPAEGPEPW GSTEHGVEVV LAHLEAARTV
     AHHGGLYHTN AEVKLQGFQA RPELLEVFST EFQMRLLWGS QGANSSQAWR YEKFDKVLTA
     LSHKLEPAIR SSEL
//
ID   SRR_MOUSE               Reviewed;         339 AA.
AC   Q9QZX7; Q401M7; Q5SWE4; Q5SWE5; Q5SWE7; Q8BT19; Q8CD11;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Serine racemase;
DE            EC=4.3.1.17;
DE            EC=4.3.1.18;
DE            EC=5.1.1.18;
DE   AltName: Full=D-serine ammonia-lyase;
DE   AltName: Full=D-serine dehydratase;
DE   AltName: Full=L-serine ammonia-lyase;
DE   AltName: Full=L-serine dehydratase;
GN   Name=Srr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY,
RP   AND COFACTOR.
RC   STRAIN=BALB/c;
RX   MEDLINE=20027561; PubMed=10557334; DOI=10.1073/pnas.96.23.13409;
RA   Wolosker H., Blackshaw S., Snyder S.H.;
RT   "Serine racemase: a glial enzyme synthesizing D-serine to regulate
RT   glutamate-N-methyl-D-aspartate neurotransmission.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:13409-13414(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Brain cortex, Spleen, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-56 (ISOFORMS 1/2/3).
RC   TISSUE=Brain;
RA   Ohba H., Ohnishi T., Yoshikawa T.;
RT   "Multiple splice variants in 5'UTR of mouse serine racemase.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PROTEIN SEQUENCE OF 15-40, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND ENZYME
RP   REGULATION.
RX   PubMed=12515328; DOI=10.1023/A:1021607715824;
RA   Neidle A., Dunlop D.S.;
RT   "Allosteric regulation of mouse brain serine racemase.";
RL   Neurochem. Res. 27:1719-1724(2002).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND ENZYME REGULATION.
RX   PubMed=12393813; DOI=10.1073/pnas.222421299;
RA   De Miranda J., Panizzutti R., Foltyn V.N., Wolosker H.;
RT   "Cofactors of serine racemase that physiologically stimulate the
RT   synthesis of the N-methyl-D-aspartate (NMDA) receptor coagonist D-
RT   serine.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14542-14547(2002).
RN   [9]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=15536068; DOI=10.1074/jbc.M405726200;
RA   Foltyn V.N., Bendikov I., De Miranda J., Panizzutti R., Dumin E.,
RA   Shleper M., Li P., Toney M.D., Kartvelishvily E., Wolosker H.;
RT   "Serine racemase modulates intracellular D-serine levels through an
RT   alpha,beta-elimination activity.";
RL   J. Biol. Chem. 280:1754-1763(2005).
RN   [10]
RP   FUNCTION, S-NITROSYLATION AT CYS-113, ATP-BINDING, AND MUTAGENESIS OF
RP   CYS-113.
RX   PubMed=17293453; DOI=10.1073/pnas.0611620104;
RA   Mustafa A.K., Kumar M., Selvakumar B., Ho G.P., Ehmsen J.T.,
RA   Barrow R.K., Amzel L.M., Snyder S.H.;
RT   "Nitric oxide S-nitrosylates serine racemase, mediating feedback
RT   inhibition of D-serine formation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2950-2955(2007).
CC   -!- FUNCTION: Catalyzes the synthesis of D-serine from L-serine. D-
CC       serine is a key coagonist with glutamate at NMDA receptors. Has
CC       dehydratase activity towards both L-serine and D-serine.
CC   -!- CATALYTIC ACTIVITY: L-serine = D-serine.
CC   -!- CATALYTIC ACTIVITY: L-serine = pyruvate + NH(3).
CC   -!- CATALYTIC ACTIVITY: D-serine = pyruvate + NH(3).
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- ENZYME REGULATION: Allosterically activated by magnesium, and
CC       possibly also other divalent metal cations. Allosterically
CC       activated by ATP, ADP or GTP.
CC   -!- SUBUNIT: Homodimer.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9QZX7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9QZX7-2; Sequence=VSP_025013;
CC       Name=3;
CC         IsoId=Q9QZX7-3; Sequence=VSP_025014;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Detected in brain (at protein level). Brain.
CC   -!- PTM: S-nitrosylated, leading to decrease the enzyme activity.
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI24255.1; Type=Erroneous gene model prediction;
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DR   EMBL; AF148321; AAF08701.1; -; mRNA.
DR   EMBL; AK031687; BAC27514.1; -; mRNA.
DR   EMBL; AK028034; BAC25712.1; -; mRNA.
DR   EMBL; AK043738; BAC31637.1; -; mRNA.
DR   EMBL; AK157122; BAE33968.1; -; mRNA.
DR   EMBL; AK170096; BAE41561.1; -; mRNA.
DR   EMBL; AL604066; CAI24252.1; -; Genomic_DNA.
DR   EMBL; AL604066; CAI24253.1; -; Genomic_DNA.
DR   EMBL; AL604066; CAI24254.1; -; Genomic_DNA.
DR   EMBL; AL604066; CAI24255.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC011164; AAH11164.1; -; mRNA.
DR   EMBL; AB232340; BAE19920.1; -; mRNA.
DR   EMBL; AB232341; BAE19921.1; -; mRNA.
DR   EMBL; AB232342; BAE19922.1; -; mRNA.
DR   EMBL; AB232343; BAE19923.1; -; mRNA.
DR   EMBL; AB235396; BAE44529.1; -; mRNA.
DR   IPI; IPI00138217; -.
DR   IPI; IPI00407158; -.
DR   IPI; IPI00648103; -.
DR   RefSeq; NP_001156783.1; NM_001163311.1.
DR   RefSeq; NP_038789.1; NM_013761.4.
DR   UniGene; Mm.131443; -.
DR   UniGene; Mm.220843; -.
DR   UniGene; Mm.412219; -.
DR   ProteinModelPortal; Q9QZX7; -.
DR   SMR; Q9QZX7; 3-324.
DR   STRING; Q9QZX7; -.
DR   PhosphoSite; Q9QZX7; -.
DR   PRIDE; Q9QZX7; -.
DR   Ensembl; ENSMUST00000065211; ENSMUSP00000067552; ENSMUSG00000001323.
DR   Ensembl; ENSMUST00000071240; ENSMUSP00000071221; ENSMUSG00000001323.
DR   Ensembl; ENSMUST00000092908; ENSMUSP00000090586; ENSMUSG00000001323.
DR   Ensembl; ENSMUST00000108448; ENSMUSP00000104087; ENSMUSG00000001323.
DR   Ensembl; ENSMUST00000121738; ENSMUSP00000113372; ENSMUSG00000001323.
DR   GeneID; 27364; -.
DR   KEGG; mmu:27364; -.
DR   NMPDR; fig|10090.3.peg.24704; -.
DR   UCSC; uc007kcr.1; mouse.
DR   CTD; 27364; -.
DR   MGI; MGI:1351636; Srr.
DR   eggNOG; roNOG13796; -.
DR   GeneTree; ENSGT00550000075026; -.
DR   HOVERGEN; HBG023167; -.
DR   InParanoid; Q9QZX7; -.
DR   OMA; PSNADDC; -.
DR   OrthoDB; EOG4M0F24; -.
DR   PhylomeDB; Q9QZX7; -.
DR   BRENDA; 5.1.1.18; 244.
DR   NextBio; 305244; -.
DR   ArrayExpress; Q9QZX7; -.
DR   Bgee; Q9QZX7; -.
DR   CleanEx; MM_SRR; -.
DR   Genevestigator; Q9QZX7; -.
DR   GermOnline; ENSMUSG00000001323; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR   GO; GO:0016594; F:glycine binding; IDA:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IMP:MGI.
DR   GO; GO:0030378; F:serine racemase activity; IDA:MGI.
DR   GO; GO:0018114; F:threonine racemase activity; IDA:MGI.
DR   GO; GO:0070179; P:D-serine biosynthetic process; IDA:MGI.
DR   GO; GO:0006563; P:L-serine metabolic process; IDA:MGI.
DR   GO; GO:0051289; P:protein homotetramerization; IDA:MGI.
DR   InterPro; IPR001926; PyrdxlP-dep_enz_bsu.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; PyrdxlP-dep_enz_bsu; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; Alternative splicing; ATP-binding;
KW   Direct protein sequencing; Isomerase; Lyase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Pyridoxal phosphate; S-nitrosylation.
FT   CHAIN         1    339       Serine racemase.
FT                                /FTId=PRO_0000185651.
FT   REGION      238    239       Substrate binding (By similarity).
FT   ACT_SITE     56     56       Proton acceptor (By similarity).
FT   ACT_SITE     84     84       Proton acceptor (By similarity).
FT   METAL       210    210       Magnesium (By similarity).
FT   METAL       214    214       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       216    216       Magnesium (By similarity).
FT   BINDING      51     51       ATP (Probable).
FT   BINDING     121    121       ATP (By similarity).
FT   BINDING     135    135       Substrate (By similarity).
FT   MOD_RES      56     56       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
FT   MOD_RES     113    113       S-nitrosocysteine.
FT   VAR_SEQ     174    198       Missing (in isoform 2).
FT                                /FTId=VSP_025013.
FT   VAR_SEQ     183    339       Missing (in isoform 3).
FT                                /FTId=VSP_025014.
FT   MUTAGEN      51     51       K->A: Impairs ATP-binding inducing a 80%
FT                                decrease in enzyme activity.
FT   MUTAGEN     113    113       C->S: Abolishes S-nitrosylation.
FT   CONFLICT    111    111       P -> T (in Ref. 2; BAC25712).
SQ   SEQUENCE   339 AA;  36359 MW;  B9AE9A9336358728 CRC64;
     MCAQYCISFA DVEKAHINIQ DSIHLTPVLT SSILNQIAGR NLFFKCELFQ KTGSFKIRGA
     LNAIRGLIPD TPEEKPKAVV THSSGNHGQA LTYAAKLEGI PAYIVVPQTA PNCKKLAIQA
     YGASIVYCDP SDESREKVTQ RIMQETEGIL VHPNQEPAVI AGQGTIALEV LNQVPLVDAL
     VVPVGGGGMV AGIAITIKAL KPSVKVYAAE PSNADDCYQS KLKGELTPNL HPPETIADGV
     KSSIGLNTWP IIRDLVDDVF TVTEDEIKYA TQLVWGRMKL LIEPTAGVAL AAVLSQHFQT
     VSPEVKNVCI VLSGGNVDLT SLNWVGQAER PAPYQTVSV
//
ID   ZRAB2_MOUSE             Reviewed;         330 AA.
AC   Q9R020; Q3TI29; Q3TLF5; Q3TUB7; Q3UD16;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   08-FEB-2011, entry version 73.
DE   RecName: Full=Zinc finger Ran-binding domain-containing protein 2;
DE   AltName: Full=Zinc finger protein 265;
DE   AltName: Full=Zinc finger, splicing;
GN   Name=Zranb2; Synonyms=Zfp265, Zis, Znf265;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=BALB/c, and C57BL/6J;
RC   TISSUE=Amnion, Brain, Embryo, Embryonic stomach, Erythroblast, and
RC   Macrophage;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-327 (ISOFORM 1).
RC   TISSUE=Kidney;
RX   MEDLINE=20237530; PubMed=10773668;
RA   Adams D.J., van der Weyden L., Kovacic A., Lovicu F.J., Copeland N.G.,
RA   Gilbert D.J., Jenkins N.A., Ioannou P.A., Morris B.J.;
RT   "Chromosome localization and characterization of the mouse and human
RT   zinc finger protein 265 gene.";
RL   Cytogenet. Cell Genet. 88:68-73(2000).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120; SER-153 AND
RP   SER-188, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-114, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153; SER-181; SER-188;
RP   SER-290 AND SER-294, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Splice factor required for alternative splicing of
CC       TRA2B/SFRS10 transcripts. May interfere with constitutive 5'-
CC       splice site selection (By similarity).
CC   -!- SUBUNIT: Interacts with the C-terminal half of SNRNP70, the
CC       Arg/Ser-rich domain of AKAP17A as well as with U2AF1 and CLK1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9R020-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9R020-2; Sequence=VSP_024946;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The RanBP2-type zinc fingers mediate binding to RNA (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the ZRANB2 family.
CC   -!- SIMILARITY: Contains 2 RanBP2-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF04474.1; Type=Frameshift; Positions=263;
CC       Sequence=BAE36054.1; Type=Frameshift; Positions=37;
CC       Sequence=BAE38837.1; Type=Erroneous initiation;
CC       Sequence=BAE39790.1; Type=Frameshift; Positions=240;
CC       Sequence=BAE40017.1; Type=Frameshift; Positions=240;
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DR   EMBL; AK146275; BAE27034.1; -; mRNA.
DR   EMBL; AK150291; BAE29446.1; -; mRNA.
DR   EMBL; AK152536; BAE31292.1; -; mRNA.
DR   EMBL; AK160862; BAE36054.1; ALT_FRAME; mRNA.
DR   EMBL; AK166534; BAE38837.1; ALT_INIT; mRNA.
DR   EMBL; AK167756; BAE39790.1; ALT_FRAME; mRNA.
DR   EMBL; AK167766; BAE39799.1; -; mRNA.
DR   EMBL; AK167862; BAE39880.1; -; mRNA.
DR   EMBL; AK167983; BAE39974.1; -; mRNA.
DR   EMBL; AK168033; BAE40017.1; ALT_FRAME; mRNA.
DR   EMBL; AK168162; BAE40123.1; -; mRNA.
DR   EMBL; AK168613; BAE40479.1; -; mRNA.
DR   EMBL; AK169114; BAE40895.1; -; mRNA.
DR   EMBL; AK169335; BAE41087.1; -; mRNA.
DR   EMBL; BC132547; AAI32548.1; -; mRNA.
DR   EMBL; AF133818; AAF04474.1; ALT_FRAME; mRNA.
DR   IPI; IPI00126804; -.
DR   IPI; IPI00845647; -.
DR   RefSeq; NP_059077.1; NM_017381.2.
DR   UniGene; Mm.259036; -.
DR   ProteinModelPortal; Q9R020; -.
DR   SMR; Q9R020; 1-40, 67-95.
DR   STRING; Q9R020; -.
DR   PhosphoSite; Q9R020; -.
DR   PRIDE; Q9R020; -.
DR   Ensembl; ENSMUST00000106063; ENSMUSP00000101678; ENSMUSG00000028180.
DR   GeneID; 53861; -.
DR   KEGG; mmu:53861; -.
DR   CTD; 53861; -.
DR   MGI; MGI:1858211; Zranb2.
DR   GeneTree; ENSGT00600000084415; -.
DR   HOVERGEN; HBG066285; -.
DR   NextBio; 310705; -.
DR   ArrayExpress; Q9R020; -.
DR   Bgee; Q9R020; -.
DR   CleanEx; MM_ZRANB2; -.
DR   Genevestigator; Q9R020; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR017337; UCP037956_Znf_RanB2.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   Pfam; PF00641; zf-RanBP; 2.
DR   PIRSF; PIRSF037956; UCP037956_ZnF_Ran; 1.
DR   SMART; SM00547; ZnF_RBZ; 2.
DR   PROSITE; PS01358; ZF_RANBP2_1; 2.
DR   PROSITE; PS50199; ZF_RANBP2_2; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Metal-binding; mRNA processing;
KW   mRNA splicing; Nucleus; Phosphoprotein; Repeat; RNA-binding; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    330       Zinc finger Ran-binding domain-containing
FT                                protein 2.
FT                                /FTId=PRO_0000066586.
FT   ZN_FING       9     40       RanBP2-type 1.
FT   ZN_FING      65     94       RanBP2-type 2.
FT   REGION      151    324       Required for nuclear targeting (By
FT                                similarity).
FT   COMPBIAS    198    262       Arg/Ser-rich.
FT   MOD_RES       9      9       Phosphoserine (By similarity).
FT   MOD_RES      54     54       N6-acetyllysine (By similarity).
FT   MOD_RES     114    114       Phosphotyrosine.
FT   MOD_RES     120    120       Phosphoserine.
FT   MOD_RES     153    153       Phosphoserine.
FT   MOD_RES     181    181       Phosphoserine.
FT   MOD_RES     188    188       Phosphoserine.
FT   MOD_RES     193    193       Phosphoserine (By similarity).
FT   MOD_RES     290    290       Phosphoserine.
FT   MOD_RES     294    294       Phosphoserine.
FT   MOD_RES     303    303       Phosphothreonine (By similarity).
FT   MOD_RES     305    305       Phosphoserine (By similarity).
FT   MOD_RES     307    307       Phosphoserine (By similarity).
FT   VAR_SEQ      37     73       Missing (in isoform 2).
FT                                /FTId=VSP_024946.
FT   CONFLICT     86     86       N -> D (in Ref. 3; AAF04474).
FT   CONFLICT    111    111       N -> S (in Ref. 3; AAF04474).
SQ   SEQUENCE   330 AA;  37350 MW;  1FD8F01C7C644F21 CRC64;
     MSTKNFRVSD GDWICPDKKC GNVNFARRTS CNRCGREKTT EAKMMKAGGT EIGKTLAEKS
     RGLFSANDWQ CKTCSNVNWA RRSECNMCNT PKYAKLEERT GYGGGFNERE NVEYIEREES
     DGEYDEFGRK KKKYRGKAVG PASILKEVED KESEGEEEDE DEDLSKYKLD EDEDEDDADL
     SKYNLDASEE EDSNKKKSNR RSRSKSRSSH SRSSSRSSSP SSSRSRSRSR SRSSSSSQSR
     SHSGSREHSR SRGSKSRSSS RSHRGSSSPR KRSYSSSSSS PERDRKRSRS RPSSPAVRKK
     RRTRSRSPER HHRSSSGSTH SGSRSSSKKK
//
ID   XPR1_MUSMC              Reviewed;         691 AA.
AC   Q9R031;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   05-OCT-2010, entry version 41.
DE   RecName: Full=Xenotropic and polytropic retrovirus receptor 1 homolog;
GN   Name=Xpr1;
OS   Mus musculus castaneus (Southeastern Asian house mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   MEDLINE=99445843; PubMed=10516044;
RA   Marin M., Tailor C.S., Nouri A., Kozak S.L., Kabat D.;
RT   "Polymorphisms of the cell surface receptor control mouse
RT   susceptibilities to xenotropic and polytropic leukemia viruses.";
RL   J. Virol. 73:9362-9368(1999).
CC   -!- FUNCTION: May function in G-protein coupled signal transduction
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity).
CC   -!- MISCELLANEOUS: In contrast to the ortholog protein in related Mus
CC       species, does not act as a receptor for xenotropic and polytropic
CC       murine leukemia retroviruses.
CC   -!- SIMILARITY: Belongs to the SYG1 (TC 2.A.94) family.
CC   -!- SIMILARITY: Contains 1 EXS domain.
CC   -!- SIMILARITY: Contains 1 SPX domain.
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DR   EMBL; AF131102; AAF03488.1; -; mRNA.
DR   UniGene; Mm.266215; -.
DR   MGI; MGI:97932; Xpr1.
DR   HOVERGEN; HBG108684; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR004342; EXS_C.
DR   InterPro; IPR004331; SPX_N.
DR   Pfam; PF03124; EXS; 1.
DR   Pfam; PF03105; SPX; 1.
DR   PROSITE; PS51380; EXS; 1.
DR   PROSITE; PS51382; SPX; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Phosphoprotein; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    691       Xenotropic and polytropic retrovirus
FT                                receptor 1 homolog.
FT                                /FTId=PRO_0000315856.
FT   TOPO_DOM      1    236       Cytoplasmic (Potential).
FT   TRANSMEM    237    257       Helical; (Potential).
FT   TOPO_DOM    258    264       Extracellular (Potential).
FT   TRANSMEM    265    285       Helical; (Potential).
FT   TOPO_DOM    286    314       Cytoplasmic (Potential).
FT   TRANSMEM    315    337       Helical; (Potential).
FT   TOPO_DOM    338    340       Extracellular (Potential).
FT   TRANSMEM    341    360       Helical; (Potential).
FT   TOPO_DOM    361    371       Cytoplasmic (Potential).
FT   TRANSMEM    372    392       Helical; (Potential).
FT   TOPO_DOM    393    393       Extracellular (Potential).
FT   TRANSMEM    394    414       Helical; (Potential).
FT   TOPO_DOM    415    475       Cytoplasmic (Potential).
FT   TRANSMEM    476    498       Helical; (Potential).
FT   TOPO_DOM    499    507       Extracellular (Potential).
FT   TRANSMEM    508    528       Helical; (Potential).
FT   TOPO_DOM    529    691       Cytoplasmic (Potential).
FT   DOMAIN        1    177       SPX.
FT   DOMAIN      439    638       EXS.
FT   MOD_RES     661    661       Phosphoserine (By similarity).
FT   MOD_RES     663    663       Phosphoserine (By similarity).
FT   MOD_RES     685    685       Phosphothreonine (By similarity).
SQ   SEQUENCE   691 AA;  81228 MW;  5B9172B85E263CA6 CRC64;
     MKFAEHLSAH ITPEWRKQYI QYEAFKDMLY SAQDQAPSVE VTDEDTVKRY FAKFEEKFFQ
     TCEKELAKIN TFYSEKLAEA QRRFATLQNE LQSSLDVQKE SSAVTALRQR RKPVFHLSHE
     ERVQHRNIKD LKLAFSEFYL SLILLQNYQN LNFTGFRKIL KKHDKILETS RGADWRVIHV
     EVAPFYTCKK INQLISETEA VVTNELEDGD RQKAMKRLRV PPLGAAQPAP AWTIFRVGLF
     CGIFIVLNIT LVFAAVFKLE TDRTVWPLIR IYRGGFLLIE FLFLLGINTY GWRQAGVNHV
     LIFELNPRNN LSHQHLFEIA GFLGILWCLS LLACFFAPIS IIPIYVYPLA LYGFMVFFLI
     NPTKTFYYKS RFWLLKLLFR VFTAPFHKVG FADFWLAGQL NSLSVILMDL EYMICFYSFE
     LKWDESKGLL PNDPQEPEFC HKYSYGVRAI VQCIPAWLRF IQCLRRYRDT RRAFPHLVNA
     GKYSTTFFTV TFAALYSTHK EQNHSDTVVF FYLWVFFCII SSCYTLIWDL KMDWGLFDKN
     AGENTFLREE IVYPQKAYYY CAIIEDVILR FAWIIQISIT AHVGDIIATV FAPLEVFRRF
     VWNFFRLENE HLNNCGEFRA VRDISVAPLN ADDQTLLEQM MDQEDGVRNR QKNRSWKYNQ
     SISLRRPRLA SQSKARDTKV LIEDTDDEAN T
//
ID   AMFR_MOUSE              Reviewed;         643 AA.
AC   Q9R049; Q8K008; Q99LH5;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=E3 ubiquitin-protein ligase AMFR;
DE            EC=6.3.2.-;
DE   AltName: Full=Autocrine motility factor receptor;
DE            Short=AMF receptor;
GN   Name=Amfr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Lung, and Testis;
RX   MEDLINE=99383230; PubMed=10456327; DOI=10.1016/S0014-5793(99)00966-7;
RA   Shimizu K., Tani M., Watanabe H., Nagamachi Y., Niinaka Y.,
RA   Shiroishi T., Ohwada S., Raz A., Yokota J.;
RT   "The autocrine motility factor receptor gene encodes a novel type of
RT   seven transmembrane protein.";
RL   FEBS Lett. 456:295-300(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Colon, and Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   ROLE IN METASTASIS.
RX   MEDLINE=22537118; PubMed=12650607; DOI=10.1023/A:1022594503657;
RA   Onishi Y., Tsukada K., Yokota J., Raz A.;
RT   "Overexpression of autocrine motility factor receptor (AMFR) in NIH3T3
RT   fibroblasts induces cell transformation.";
RL   Clin. Exp. Metastasis 20:51-58(2003).
RN   [4]
RP   INTERACTION WITH NGLY1; PSMC1; SAKS1; RAD23B AND VCP.
RX   PubMed=16709668; DOI=10.1073/pnas.0602747103;
RA   Li G., Zhao G., Zhou X., Schindelin H., Lennarz W.J.;
RT   "The AAA ATPase p97 links peptide N-glycanase to the endoplasmic
RT   reticulum-associated E3 ligase autocrine motility factor receptor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:8348-8353(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-542, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   FUNCTION IN UBIQUITINATION OF MISFOLDED PROTEINS, AND INTERACTION WITH
RP   RNF5.
RX   PubMed=18216283; DOI=10.1091/mbc.E07-06-0601;
RA   Morito D., Hirao K., Oda Y., Hosokawa N., Tokunaga F., Cyr D.M.,
RA   Tanaka K., Iwai K., Nagata K.;
RT   "Gp78 cooperates with RMA1 in endoplasmic reticulum-associated
RT   degradation of CFTRDeltaF508.";
RL   Mol. Biol. Cell 19:1328-1336(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-542, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which can target both itself
CC       and other proteins including CD3D and APOB for proteasomal
CC       degradation. Mediates polyubiquitination of CYP3A4. Specific
CC       receptor for the autocrine motility factor. Mediates tumor
CC       invasion and metastasis. Component of a complex required to couple
CC       deglycosylation and proteasome-mediated degradation of misfolded
CC       proteins in the endoplasmic reticulun that are retrotranslocated
CC       in the cytosol (By similarity). Promotes ubiquitination of
CC       misfolded proteins such as mutant CFTR; proposed to mediate
CC       sequential ubiquitination by recognizing already ubiquitin-
CC       conjugated substrates and to cooperate with E3 ubiquitin-protein
CC       ligase RNF5.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with UBE2G2/UBC7 through a region distinct from
CC       the RING finger. Component of a complex required to couple
CC       retrotranslocation, ubiquitination and deglycosylation composed of
CC       NGLY1, SAKS1, AMFR, VCP and RAD23B. Interacts with RNF5.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9R049-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9R049-2; Sequence=VSP_008224;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in heart, brain, liver, lung,
CC       skeletal muscle, kidney and testis. Not detected in spleen.
CC   -!- DOMAIN: The CUE domain is required for recognition of misfolded
CC       proteins such as mutant CFTR.
CC   -!- SIMILARITY: Contains 1 CUE domain.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF124144; AAD56721.1; -; mRNA.
DR   EMBL; BC003256; AAH03256.1; -; mRNA.
DR   EMBL; BC034538; AAH34538.1; -; mRNA.
DR   EMBL; BC040338; AAH40338.1; -; mRNA.
DR   IPI; IPI00319880; -.
DR   IPI; IPI00351315; -.
DR   RefSeq; NP_035917.2; NM_011787.2.
DR   UniGene; Mm.34641; -.
DR   ProteinModelPortal; Q9R049; -.
DR   SMR; Q9R049; 329-386, 456-502, 574-600.
DR   STRING; Q9R049; -.
DR   PhosphoSite; Q9R049; -.
DR   PRIDE; Q9R049; -.
DR   Ensembl; ENSMUST00000053766; ENSMUSP00000052258; ENSMUSG00000031751.
DR   GeneID; 23802; -.
DR   KEGG; mmu:23802; -.
DR   UCSC; uc009mvn.1; mouse.
DR   CTD; 23802; -.
DR   MGI; MGI:1345634; Amfr.
DR   GeneTree; ENSGT00530000062938; -.
DR   HOGENOM; HBG445825; -.
DR   HOVERGEN; HBG044694; -.
DR   InParanoid; Q9R049; -.
DR   OMA; ARDVAQY; -.
DR   OrthoDB; EOG4DJJW8; -.
DR   BRENDA; 6.3.2.19; 244.
DR   ArrayExpress; Q9R049; -.
DR   Bgee; Q9R049; -.
DR   CleanEx; MM_AMFR; -.
DR   Genevestigator; Q9R049; -.
DR   GermOnline; ENSMUSG00000031751; Mus musculus.
DR   GO; GO:0030176; C:integral to endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030433; P:ER-associated protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR   InterPro; IPR003892; CUE.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF02845; CUE; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00546; CUE; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS51140; CUE; 1.
DR   PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Endoplasmic reticulum; Ligase; Membrane;
KW   Metal-binding; Nucleotide-binding; Phosphoprotein; Receptor;
KW   Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    643       E3 ubiquitin-protein ligase AMFR.
FT                                /FTId=PRO_0000064580.
FT   TRANSMEM     82    102       Helical; (Potential).
FT   TRANSMEM    122    142       Helical; (Potential).
FT   TRANSMEM    186    206       Helical; (Potential).
FT   TRANSMEM    215    235       Helical; (Potential).
FT   TRANSMEM    254    274       Helical; (Potential).
FT   TRANSMEM    276    296       Helical; (Potential).
FT   TRANSMEM    429    449       Helical; (Potential).
FT   DOMAIN      456    498       CUE.
FT   ZN_FING     341    379       RING-type.
FT   MOD_RES     542    542       Phosphoserine.
FT   VAR_SEQ      57     60       Missing (in isoform 2).
FT                                /FTId=VSP_008224.
FT   CONFLICT    412    412       R -> S (in Ref. 1; AAD56721).
SQ   SEQUENCE   643 AA;  73105 MW;  7119277725982F79 CRC64;
     MPLLFLERFP WPSLRTYTGL SGLALLGTIV SAYRALSQPE DGSGEPEPLT APLQPEALAP
     ARLTAGGPRA RDVAQYLLSD SLFVWVLVNT ACCVLMLVAK LIQCIVFGPL RVSERQHLKD
     KFWNFIFYKF IFIFGVLNVQ TVEEVVMWCL WFAGLVFLHL MVQLCKDRFE YLSFSPTTPM
     SSHGRVLSLL IAMLLSCCGL AVVCCVTGYT HGMHTLAFMA AESLLVTVRT AHVILRYVIH
     LWDLNHEGTW EGKGTYVYYT DFVMELALLS LDLMHHIHML LFGNIWLSMA SLVIFMQLRY
     LFHEVQRRIR RHKNYLRVVG NMEARFAVAT PEELAVNNDD CAICWDSMQA ARKLPCGHLF
     HNSCLRSWLE QDTSCPTCRM SLNIADGSRA REDHQGENLD ENLVPVAAAE GRPRLNQHNH
     FFHFDGSRIA SWLPSFSVEV MHTTNILGIT QASNSQLNAM AHQIQEMFPQ VPYHLVLQDL
     QMTRSVEITT DNILEGRIQV PFPTQRSDSL RPALNSPVER PSPDLEEGEA SVQTERVPLD
     LSPRLEETLD FSEVELEPIE VEDFEARGSR FSKSADERQR MLVQRKDDLL QQARKRFLNK
     SSEDDGASER LLPSEGTSSD PVTLRRRMLA AAAERRLQRQ RTT
//
ID   AAKB1_MOUSE             Reviewed;         270 AA.
AC   Q9R078; Q91YN6;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=5'-AMP-activated protein kinase subunit beta-1;
DE            Short=AMPK subunit beta-1;
DE            Short=AMPKb;
GN   Name=Prkab1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CD-1;
RA   Valentijn L.J., Hoff E.I., Baas F.;
RT   "5'-AMP-activated protein kinase subunit beta interacts with the p42
RT   subunit of translation initiation factor eIF3.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: AMPK is responsible for the regulation of fatty acid
CC       synthesis by phosphorylation of acetyl-CoA carboxylase. Also
CC       regulates cholesterol synthesis via phosphorylation and
CC       inactivation of hydroxymethylglutaryl-CoA reductase and hormone-
CC       sensitive lipase. This is a regulatory subunit, may be a positive
CC       regulator of AMPK activity. It may also serve as an adaptor
CC       molecule for the catalytic alpha-subunit (By similarity).
CC   -!- SUBUNIT: Heterotrimer of an alpha catalytic subunit, a beta and a
CC       gamma non-catalytic regulatory subunits. Interacts with FNIP1 and
CC       FNIP2 (By similarity).
CC   -!- SIMILARITY: Belongs to the 5'-AMP-activated protein kinase beta
CC       subunit family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF108215; AAF14222.1; -; mRNA.
DR   EMBL; BC016398; AAH16398.1; -; mRNA.
DR   IPI; IPI00223185; -.
DR   RefSeq; NP_114075.1; NM_031869.2.
DR   UniGene; Mm.458152; -.
DR   ProteinModelPortal; Q9R078; -.
DR   SMR; Q9R078; 77-163, 189-270.
DR   IntAct; Q9R078; 1.
DR   MINT; MINT-4086419; -.
DR   STRING; Q9R078; -.
DR   PhosphoSite; Q9R078; -.
DR   PRIDE; Q9R078; -.
DR   Ensembl; ENSMUST00000031486; ENSMUSP00000031486; ENSMUSG00000029513.
DR   Ensembl; ENSMUST00000111999; ENSMUSP00000107630; ENSMUSG00000029513.
DR   GeneID; 19079; -.
DR   KEGG; mmu:19079; -.
DR   UCSC; uc008zew.1; mouse.
DR   CTD; 19079; -.
DR   MGI; MGI:1336167; Prkab1.
DR   GeneTree; ENSGT00390000001416; -.
DR   HOGENOM; HBG623595; -.
DR   HOVERGEN; HBG050430; -.
DR   InParanoid; Q9R078; -.
DR   OMA; YHQEPYI; -.
DR   OrthoDB; EOG4G1MH4; -.
DR   PhylomeDB; Q9R078; -.
DR   NextBio; 295614; -.
DR   ArrayExpress; Q9R078; -.
DR   Bgee; Q9R078; -.
DR   Genevestigator; Q9R078; -.
DR   GermOnline; ENSMUSG00000029513; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0004679; F:AMP-activated protein kinase activity; TAS:MGI.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0006950; P:response to stress; TAS:MGI.
DR   InterPro; IPR006828; AMP_prot_kin_bsu_interact-dom.
DR   Pfam; PF04739; AMPKBI; 1.
PE   1: Evidence at protein level;
KW   Fatty acid biosynthesis; Lipid synthesis; Lipoprotein; Myristate;
KW   Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    270       5'-AMP-activated protein kinase subunit
FT                                beta-1.
FT                                /FTId=PRO_0000204364.
FT   MOD_RES       4      4       Phosphothreonine (By similarity).
FT   MOD_RES       5      5       Phosphoserine (By similarity).
FT   MOD_RES       6      6       Phosphoserine (By similarity).
FT   MOD_RES      19     19       Phosphothreonine (By similarity).
FT   MOD_RES      24     24       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES      25     25       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES      40     40       Phosphoserine (By similarity).
FT   MOD_RES      96     96       Phosphoserine (By similarity).
FT   MOD_RES     101    101       Phosphoserine (By similarity).
FT   MOD_RES     108    108       Phosphoserine; by autocatalysis.
FT   MOD_RES     148    148       Phosphothreonine (By similarity).
FT   MOD_RES     174    174       Phosphoserine (By similarity).
FT   MOD_RES     177    177       Phosphoserine (By similarity).
FT   MOD_RES     180    180       Phosphoserine (By similarity).
FT   MOD_RES     181    181       Phosphoserine (By similarity).
FT   MOD_RES     182    182       Phosphoserine (By similarity).
FT   MOD_RES     252    252       Phosphoserine (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
SQ   SEQUENCE   270 AA;  30308 MW;  6B520A95A0A844E5 CRC64;
     MGNTSSERAA LERQAGHKTP RRDSSGGAKD GDRPKILMDS PEDADIFHSE EIKAPEKEEF
     LAWQHDLEAN DKAPAQARPT VFRWTGGGKE VYLSGSFNNW SKLPLTRSQN NFVAILDLPE
     GEHQYKFFVD GQWTHDPSEP IVTSQLGTVN NIIQVKKTDF EVFDALMVDS QKCSDVSELS
     SSPPGPYHQE PYMSKPEERF KAPPILPPHL LQVILNKDTG ISCDPALLPE PNHVMLNHLY
     ALSIKDGVMV LSATHRYKKK YVTTLLYKPI
//
ID   PEX14_MOUSE             Reviewed;         376 AA.
AC   Q9R0A0;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Peroxisomal membrane protein PEX14;
DE   AltName: Full=PTS1 receptor-docking protein;
DE   AltName: Full=Peroxin-14;
DE   AltName: Full=Peroxisomal membrane anchor protein PEX14;
GN   Name=Pex14;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Bliskovsky V., Miller M., Mock B.;
RT   "Physical linkage of Pex14 and Cast genes on mouse chromosome 4.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 228-237, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Component of the peroxisomal translocation machinery
CC       with PEX13 and PEX17. Interacts with both the PTS1 and PTS2
CC       receptors. Binds directly to PEX17 (By similarity).
CC   -!- SUBUNIT: Interacts with PEX5 and PEX19 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane; Peripheral membrane
CC       protein; Cytoplasmic side (By similarity).
CC   -!- SIMILARITY: Belongs to the peroxin-14 family.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AF097512; AAF04616.1; -; mRNA.
DR   EMBL; BC028952; AAH28952.1; -; mRNA.
DR   IPI; IPI00127237; -.
DR   RefSeq; NP_062755.1; NM_019781.2.
DR   UniGene; Mm.184172; -.
DR   ProteinModelPortal; Q9R0A0; -.
DR   SMR; Q9R0A0; 25-70.
DR   STRING; Q9R0A0; -.
DR   PhosphoSite; Q9R0A0; -.
DR   PRIDE; Q9R0A0; -.
DR   Ensembl; ENSMUST00000103217; ENSMUSP00000099506; ENSMUSG00000028975.
DR   GeneID; 56273; -.
DR   KEGG; mmu:56273; -.
DR   NMPDR; fig|10090.3.peg.10920; -.
DR   UCSC; uc008vvp.1; mouse.
DR   CTD; 56273; -.
DR   MGI; MGI:1927868; Pex14.
DR   GeneTree; ENSGT00390000015047; -.
DR   HOGENOM; HBG402927; -.
DR   HOVERGEN; HBG053571; -.
DR   InParanoid; Q9R0A0; -.
DR   OMA; SPVKENH; -.
DR   OrthoDB; EOG4BCDNM; -.
DR   PhylomeDB; Q9R0A0; -.
DR   NextBio; 312156; -.
DR   ArrayExpress; Q9R0A0; -.
DR   Bgee; Q9R0A0; -.
DR   CleanEx; MM_PEX14; -.
DR   Genevestigator; Q9R0A0; -.
DR   GermOnline; ENSMUSG00000028975; Mus musculus.
DR   GO; GO:0005778; C:peroxisomal membrane; IDA:MGI.
DR   GO; GO:0055085; P:transmembrane transport; IEA:UniProtKB-KW.
DR   InterPro; IPR016030; AdoCbl_synth_CblAdoTrfase-like.
DR   InterPro; IPR006785; Pex14_N.
DR   Gene3D; G3DSA:1.20.1200.10; AdoCbl_synth_CblAdoTrfase-like; 1.
DR   Pfam; PF04695; Pex14_N; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Membrane; Peroxisome;
KW   Phosphoprotein; Protein transport; Translocation; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    376       Peroxisomal membrane protein PEX14.
FT                                /FTId=PRO_0000058326.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      34     34       N6-acetyllysine (By similarity).
FT   MOD_RES     280    280       Phosphoserine.
FT   MOD_RES     334    334       Phosphoserine.
SQ   SEQUENCE   376 AA;  41208 MW;  F7863CE4B6433580 CRC64;
     MASSEQAEQP NQPSSPPGSE NVVPREPLIA TAVKFLQNSR VRQSPLATRR AFLKKKGLTD
     EEIDLAFQQS GTAADEPSPL GPATPVVPVQ PPHLTPQPYS PRGSRWRDYG ALAIIMAGIA
     FGFHQLYKRY LLPLILGGRE DRKQLERMAA SLSELSGTVA QTVTQVQTTL ASVQELLRQQ
     QQKVQELAHE LATAKATTST NWILESQNIN ELKSEINSLK GLLLNRRQFP PSPSAPKIPS
     WQIPVKSSSP SSPAAVNHHS SSDISPVSNE STSSSPGKDS HSPEGSTATY HLLGPQEEGE
     GVLDVKGQVR MEVQGEEEKR EDKEDEDDED DDVSHVDEED VLGVQREDRR GGDGQINEQV
     EKLRRPEGAS NETERD
//
ID   NEK3_MOUSE              Reviewed;         511 AA.
AC   Q9R0A5; Q9Z0X9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Serine/threonine-protein kinase Nek3;
DE            EC=2.7.11.1;
DE   AltName: Full=Never in mitosis A-related kinase 3;
DE            Short=NimA-related protein kinase 3;
GN   Name=Nek3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99240743; PubMed=10224116; DOI=10.1074/jbc.274.19.13491;
RA   Tanaka K., Nigg E.A.;
RT   "Cloning and characterization of the murine Nek3 protein kinase, a
RT   novel member of the NIMA family of putative cell cycle regulators.";
RL   J. Biol. Chem. 274:13491-13497(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99321807; PubMed=10393247; DOI=10.1016/S0378-1119(99)00165-1;
RA   Chen A., Yanai A., Arama E., Kilfin G., Motro B.;
RT   "NIMA-related kinases: isolation and characterization of murine nek3
RT   and nek4 cDNAs, and chromosomal localization of nek1, nek2 and nek3.";
RL   Gene 234:127-137(1999).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-477, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
CC   -!- FUNCTION: Kinase that may play a role in mitotic regulation.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AF093416; AAD20986.1; -; mRNA.
DR   EMBL; AF099066; AAD16286.1; -; mRNA.
DR   IPI; IPI00127241; -.
DR   UniGene; Mm.478387; -.
DR   ProteinModelPortal; Q9R0A5; -.
DR   SMR; Q9R0A5; 1-258.
DR   STRING; Q9R0A5; -.
DR   PhosphoSite; Q9R0A5; -.
DR   PRIDE; Q9R0A5; -.
DR   Ensembl; ENSMUST00000110730; ENSMUSP00000106358; ENSMUSG00000031478.
DR   MGI; MGI:1344371; Nek3.
DR   GeneTree; ENSGT00600000084179; -.
DR   HOGENOM; HBG444385; -.
DR   HOVERGEN; HBG003063; -.
DR   InParanoid; Q9R0A5; -.
DR   OrthoDB; EOG4DFPN8; -.
DR   PhylomeDB; Q9R0A5; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 303780; -.
DR   ArrayExpress; Q9R0A5; -.
DR   Bgee; Q9R0A5; -.
DR   Genevestigator; Q9R0A5; -.
DR   GermOnline; ENSMUSG00000031478; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell division; Kinase; Magnesium;
KW   Metal-binding; Mitosis; Nucleotide-binding; Phosphoprotein;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    511       Serine/threonine-protein kinase Nek3.
FT                                /FTId=PRO_0000086424.
FT   DOMAIN        4    255       Protein kinase.
FT   NP_BIND      10     18       ATP (By similarity).
FT   ACT_SITE    125    125       Proton acceptor (By similarity).
FT   BINDING      33     33       ATP (By similarity).
FT   MOD_RES     159    159       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     354    354       Phosphoserine (By similarity).
FT   MOD_RES     394    394       Phosphoserine (By similarity).
FT   MOD_RES     477    477       Phosphothreonine.
FT   CONFLICT    239    239       N -> K (in Ref. 2; AAD16286).
FT   CONFLICT    342    343       Missing (in Ref. 2; AAD16286).
SQ   SEQUENCE   511 AA;  57223 MW;  DE6D6C0533C7302F CRC64;
     MDNYTVLRVI GQGSFGRALL VLQESSNQTF AMKEIRLLKS DTQTSRKEAV LLAKMKHPNI
     VAFKESFEAE GYLYIVMEYC DGGDLMQRIK QQKGNLFPED TILNWFIQIC LGVNHIHKRR
     VLHRDIKSKN VFLTHNGKVK LGDFGSARLL SSPMAFACTY VGTPYYVPPE IWENLPYNNK
     SDIWSLGCIL YELCALKHPF QANSWKNLIL KICQGPIHPL PALYSCKLQG LVKQMLKRNP
     SHRPSATTLL CRGSLAPLVP KCLPPQIIRE YGEQILDEIK ISTPKNMKKQ DSNRVGRALG
     EANSAAMQEE ERGRKCSHTE LESTGTTPAG NALGRAARGN PESGNRQEHG SHTSPASPHR
     PRWERHGPSS NVEALEKASI LTSSFTAEDD RGGSVIKYEE NARRQWVREP PEALLSMLKD
     ADLSQAFQTY TIYRPGAEGF LKGPLSEDTA SDSVDGDLDS VMLDPERFEP RLDEEDTDFE
     EDNENPDWVS ELKKHVGYGD GPGGQLLGER A
//
ID   ZEB2_MOUSE              Reviewed;        1215 AA.
AC   Q9R0G7;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Zinc finger E-box-binding homeobox 2;
DE   AltName: Full=Smad-interacting protein 1;
DE   AltName: Full=Zinc finger homeobox protein 1b;
GN   Name=Zeb2; Synonyms=Sip1, Zfhx1b, Zfx1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99329065; PubMed=10400677; DOI=10.1074/jbc.274.29.20489;
RA   Verschueren K., Remacle J.E., Collart C., Kraft H., Baker B.S.,
RA   Tylzanowski P., Nelles L., Wuytens G., Su M.-T., Bodmer R.,
RA   Smith J.C., Huylebroeck D.;
RT   "SIP1, a novel zinc finger/homeodomain repressor, interacts with Smad
RT   proteins and binds to 5'-CACCT sequences in candidate target genes.";
RL   J. Biol. Chem. 274:20489-20498(1999).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-38; SER-778;
RP   SER-780; THR-782; SER-784 AND SER-1167, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Transcriptional inhibitor that binds to DNA sequence 5'-
CC       CACCT-3' in different promoters. Represses transcription of E-
CC       cadherin.
CC   -!- SUBUNIT: Interacts with CBX4 and CTBP1 (By similarity). Binds
CC       activated SMAD1, activated SMAD2 and activated SMAD3; binding with
CC       SMAD4 is not detected.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- PTM: Sumoylation on Lys-391 and Lys-866 is promoted by the E3
CC       SUMO-protein ligase CBX4, and impairs interaction with CTBP1 and
CC       transcription repression activity (By similarity).
CC   -!- SIMILARITY: Belongs to the delta-EF1/ZFH-1 C2H2-type zinc-finger
CC       family.
CC   -!- SIMILARITY: Contains 7 C2H2-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF033116; AAD56590.1; -; mRNA.
DR   IPI; IPI00420464; -.
DR   UniGene; Mm.440702; -.
DR   ProteinModelPortal; Q9R0G7; -.
DR   SMR; Q9R0G7; 206-333, 571-603, 648-705, 957-1075.
DR   STRING; Q9R0G7; -.
DR   PhosphoSite; Q9R0G7; -.
DR   PRIDE; Q9R0G7; -.
DR   Ensembl; ENSMUST00000028229; ENSMUSP00000028229; ENSMUSG00000026872.
DR   Ensembl; ENSMUST00000068415; ENSMUSP00000069685; ENSMUSG00000026872.
DR   Ensembl; ENSMUST00000076836; ENSMUSP00000076111; ENSMUSG00000026872.
DR   MGI; MGI:1344407; Zeb2.
DR   GeneTree; ENSGT00530000063739; -.
DR   HOVERGEN; HBG004697; -.
DR   InParanoid; Q9R0G7; -.
DR   OrthoDB; EOG4KD6K7; -.
DR   ArrayExpress; Q9R0G7; -.
DR   Bgee; Q9R0G7; -.
DR   CleanEx; MM_ZEB2; -.
DR   Genevestigator; Q9R0G7; -.
DR   GermOnline; ENSMUSG00000026872; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0016564; F:transcription repressor activity; NAS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0021846; P:cell proliferation in forebrain; IMP:MGI.
DR   GO; GO:0021766; P:hippocampus development; IMP:MGI.
DR   GO; GO:0001755; P:neural crest cell migration; IMP:MGI.
DR   GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR   GO; GO:0043507; P:positive regulation of JUN kinase activity; IMP:MGI.
DR   GO; GO:0030177; P:positive regulation of Wnt receptor signaling pathway; IMP:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   GO; GO:0001756; P:somitogenesis; IMP:MGI.
DR   InterPro; IPR001356; Homeobox.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 7.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00355; ZnF_C2H2; 8.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; FALSE_NEG.
DR   PROSITE; PS50071; HOMEOBOX_2; FALSE_NEG.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE   1: Evidence at protein level;
KW   Acetylation; DNA-binding; Homeobox; Isopeptide bond; Metal-binding;
KW   Nucleus; Phosphoprotein; Repeat; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN         1   1215       Zinc finger E-box-binding homeobox 2.
FT                                /FTId=PRO_0000047237.
FT   ZN_FING     211    234       C2H2-type 1.
FT   ZN_FING     241    263       C2H2-type 2.
FT   ZN_FING     282    304       C2H2-type 3.
FT   ZN_FING     310    334       C2H2-type 4; atypical.
FT   DNA_BIND    644    703       Homeobox; atypical.
FT   ZN_FING     999   1021       C2H2-type 5.
FT   ZN_FING    1027   1049       C2H2-type 6.
FT   ZN_FING    1055   1076       C2H2-type 7; atypical.
FT   REGION      437    487       SMAD-MH2 binding domain.
FT   COMPBIAS   1084   1215       Glu-rich (acidic).
FT   MOD_RES      36     36       Phosphoserine.
FT   MOD_RES      38     38       Phosphothreonine.
FT   MOD_RES     377    377       N6-acetyllysine (By similarity).
FT   MOD_RES     778    778       Phosphoserine.
FT   MOD_RES     780    780       Phosphoserine.
FT   MOD_RES     782    782       Phosphothreonine.
FT   MOD_RES     784    784       Phosphoserine.
FT   MOD_RES    1167   1167       Phosphoserine.
FT   CROSSLNK    391    391       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   CROSSLNK    866    866       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
SQ   SEQUENCE   1215 AA;  136471 MW;  3EC5AD552E1FB089 CRC64;
     MKQPIMADGP RCKRRKQANP RRKNVVNYDN VVDAGSETDE EDKLHIAEDD SLANPLDQDT
     SPASMPNHES SPHMSQGLLP REEEEEELRE SVVEHSWHSG EILQASVAGP EEMKEDYDAM
     GPEATIQTTI NNGTVKNANC TSDFEEYFAK RKLEERDGHA VSIEEYLQRS DTAIIYPEAP
     EELSRLGTPE ANGQEENDLP PGTPDAFAQL LTCPYCDRGY KRLTSLKEHI KYRHEKNEEN
     FSCPLCSYTF AYRTQLERHM VTHKPGTDQH QMLTQGAGNR KFKCTECGKA FKYKHHLKEH
     LRIHSGEKPY ECPNCKKRFS HSGSYSSHIS SKKCIGLISV NGRMRNNIKT GSSPNSVSSS
     PTNSAITQLR NKLENGKPLS MSEQTGLLKI KTEPLDFNDY KVLMATHGFS GSSPFMNGGL
     GATSPLGVHP SAQSPMQHLG VGMEAPLLGF PTMNSNLSEV QKVLQIVDNT VSRQKMDCKT
     EDISKLKGYH MKDPCSQPEE QGVTSPNIPP VGLPVVSHNG ATKSIIDYTL EKVNEAKACL
     QSLTTDSRRQ ISNIKKEKLR TLIDLVTDDK MIENHSISTP FSCQFCKESF PGPIPLHQHE
     RYLCKMNEEI KAVLQPHENI VPNKAGVFVD NKALLLSSVL SEKGLTSPIN PYKDHMSVLK
     AYYAMNMEPN SDELLKISIA VGLPQEFVKE WFEQRKVYQY SNSRSPSLER TSKPLAPNSN
     PTTKDSLLPR SPVKPMDSIT SPSIAELHNS VTSCDPPLRL TKSSHFTNIK AVDKLDHSRS
     NTPSPLNLSS TSSKNSHSSS YTPNSFSSEE LQAEPLDLSL PKQMREPKGI IATKNKTKAT
     SINLDHNSVS SSSENSDEPL NLTFIKKEFS NSNNLDNKSN NPVFGMNPFS AKPLYTPLPP
     QSAFPPATFM PPVQTSIPGL RPYPGLDQMS FLPHMAYTYP TGAATFADMQ QRRKYQRKQG
     FQGDLLDGAQ DYMSGLDDMT DSDSCLSRKK IKKTESGMYA CDLCDKTFQK SSSLLRHKYE
     HTGKRPHQCQ ICKKAFKHKH HLIEHSRLHS GEKPYQCDKC GKRFSHSGSY SQHMNHRYSY
     CKREAEEREA AEREAREKGH LGPTELLMNR AYLQSITPQG YSDSEERESM PRDGESEKEH
     EKEGEEGYGK LRRRDGDEEE EEEEEESENK SMDTDPETIR DEEETGDHSM DDSSEDGKME
     TKSDHEEDNM EDGMG
//
ID   K2C71_MOUSE             Reviewed;         524 AA.
AC   Q9R0H5; A0JLW9; Q7TPF3; Q9D0X6;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Keratin, type II cytoskeletal 71;
DE   AltName: Full=Cytokeratin-6G;
DE            Short=CK-6G;
DE   AltName: Full=Cytokeratin-71;
DE            Short=CK-71;
DE   AltName: Full=Keratin-6G;
DE            Short=K6G;
DE   AltName: Full=Keratin-71;
DE            Short=K71;
DE   AltName: Full=Type II inner root sheath-specific keratin-K6irs1;
DE            Short=mK6irs;
DE            Short=mK6irs1/Krt2-6g;
DE   AltName: Full=Type-II keratin Kb34;
GN   Name=Krt71; Synonyms=K6irs1, Kb34, Krt2-6g, Krt6g;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Skin;
RX   PubMed=11703281; DOI=10.1046/j.1365-2133.2001.04463.x;
RA   Porter R.M., Corden L.D., Lunny D.P., Smith F.J.D., Lane E.B.,
RA   McLean W.H.I.;
RT   "Keratin K6irs is specific to the inner root sheath of hair follicles
RT   in mice and humans.";
RL   Br. J. Dermatol. 145:558-568(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=C57BL/6NCrj; TISSUE=Skin;
RX   PubMed=11231308; DOI=10.1046/j.1523-1747.2001.01226.x;
RA   Aoki N., Sawada S., Rogers M.A., Schweizer J., Shimomura Y.,
RA   Tsujimoto T., Ito K., Ito M.;
RT   "A novel type II cytokeratin, mK6irs, is expressed in the Huxley and
RT   Henle layers of the mouse inner root sheath.";
RL   J. Invest. Dermatol. 116:359-365(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE
RP   SPECIFICITY, AND MUTAGENESIS OF ASN-140 AND ALA-431.
RC   STRAIN=BALB/cByJ, C3H/HeJ, C57BL/6 X C3H, C57BL/6J, and DBA/2J;
RC   TISSUE=Skin;
RX   MEDLINE=22934800; PubMed=14573483;
RA   Kikkawa Y., Oyama A.H., Ishii R., Miura I., Amano T., Ishii Y.,
RA   Yoshikawa Y., Masuya H., Wakana S., Shiroishi T., Taya C.,
RA   Yonekawa H.;
RT   "A small deletion hotspot in the type II keratin gene mK6irs1/Krt2-6g
RT   on mouse chromosome 15, a candidate for causing the wavy hair of the
RT   caracul (Ca) mutation.";
RL   Genetics 165:721-733(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 381-524.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=14632181; DOI=10.1046/j.1523-1747.2003.12491.x;
RA   Peters T., Sedlmeier R., Buessow H., Runkel F., Lueers G.H.,
RA   Korthaus D., Fuchs H., Hrabe de Angelis M., Stumm G., Russ A.P.,
RA   Porter R.M., Augustin M., Franz T.;
RT   "Alopecia in a novel mouse model RCO3 is caused by mK6irs1
RT   deficiency.";
RL   J. Invest. Dermatol. 121:674-680(2003).
RN   [7]
RP   MUTAGENESIS OF ALA-143 AND ILE-146.
RX   PubMed=17143583; DOI=10.1007/s00335-006-0084-9;
RA   Runkel F., Klaften M., Koch K., Boehnert V., Buessow H., Fuchs H.,
RA   Franz T., Hrabe de Angelis M.;
RT   "Morphologic and molecular characterization of two novel Krt71 (Krt2-
RT   6g) mutations: Krt71rco12 and Krt71rco13.";
RL   Mamm. Genome 17:1172-1182(2006).
CC   -!- FUNCTION: Plays a central role in hair formation. Essential
CC       component of keratin intermediate filaments in the inner root
CC       sheath (IRS) of the hair follicle.
CC   -!- SUBUNIT: Heterodimer of a type I and a type II keratin. Associates
CC       with KRT16 and/or KRT17.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in the inner root
CC       sheath (IRS) of the hair follicle. Present in Henle and the Huxley
CC       layers of the IRS, while expression in the cuticle is unsure (at
CC       protein level).
CC   -!- DEVELOPMENTAL STAGE: Expressed exclusively in the inner root
CC       sheath (IRS) of anagen hair follicles, where expression is
CC       predominantly in the hair cone during anagen III and in the Huxley
CC       and Henle layers of the inner root sheath during anagen VI.
CC   -!- DISRUPTION PHENOTYPE: Mice exhibit defects in hair structure and
CC       progressive alopecia. Missense mutations cause milder phenotypes
CC       such as caracul, characterized by rough and greasy fur, and wavy
CC       hair that is pointed in different directions.
CC   -!- MISCELLANEOUS: There are two types of cytoskeletal and
CC       microfibrillar keratin, I (acidic) and II (neutral to basic) (40-
CC       55 and 56-70 kDa, respectively).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AY033497; AAK55110.1; -; mRNA.
DR   EMBL; AB033744; BAA85657.1; -; mRNA.
DR   EMBL; AB100413; BAC79434.1; -; mRNA.
DR   EMBL; AB100414; BAC79435.1; -; Genomic_DNA.
DR   EMBL; AB100415; BAC79436.1; -; Genomic_DNA.
DR   EMBL; AB100416; BAC79437.1; -; Genomic_DNA.
DR   EMBL; AB100417; BAC79438.1; -; Genomic_DNA.
DR   EMBL; AB100418; BAC79439.1; -; Genomic_DNA.
DR   EMBL; AK004268; BAB23243.2; -; mRNA.
DR   EMBL; BC125346; AAI25347.1; -; mRNA.
DR   EMBL; BC125348; AAI25349.1; -; mRNA.
DR   IPI; IPI00468956; -.
DR   RefSeq; NP_064340.1; NM_019956.1.
DR   UniGene; Mm.358677; -.
DR   ProteinModelPortal; Q9R0H5; -.
DR   SMR; Q9R0H5; 129-166, 174-280, 297-442.
DR   STRING; Q9R0H5; -.
DR   PhosphoSite; Q9R0H5; -.
DR   PRIDE; Q9R0H5; -.
DR   Ensembl; ENSMUST00000023710; ENSMUSP00000023710; ENSMUSG00000051879.
DR   GeneID; 56735; -.
DR   KEGG; mmu:56735; -.
DR   UCSC; uc007xtx.1; mouse.
DR   CTD; 56735; -.
DR   MGI; MGI:1861586; Krt71.
DR   eggNOG; roNOG13479; -.
DR   GeneTree; ENSGT00550000074491; -.
DR   HOGENOM; HBG715391; -.
DR   HOVERGEN; HBG013015; -.
DR   InParanoid; Q9R0H5; -.
DR   OMA; CLFEAEI; -.
DR   OrthoDB; EOG4SQWWS; -.
DR   PhylomeDB; Q9R0H5; -.
DR   NextBio; 313220; -.
DR   ArrayExpress; Q9R0H5; -.
DR   Bgee; Q9R0H5; -.
DR   CleanEx; MM_KRT71; -.
DR   Genevestigator; Q9R0H5; -.
DR   GermOnline; ENSMUSG00000051879; Mus musculus.
DR   GO; GO:0045095; C:keratin filament; IDA:MGI.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0031069; P:hair follicle morphogenesis; IMP:UniProtKB.
DR   InterPro; IPR016044; F.
DR   InterPro; IPR001664; IF.
DR   InterPro; IPR018039; Intermediate_filament_CS.
DR   InterPro; IPR003054; Keratin_II.
DR   PANTHER; PTHR23239; IF; 1.
DR   PANTHER; PTHR23239:SF18; Keratin_II; 1.
DR   Pfam; PF00038; Filament; 1.
DR   PRINTS; PR01276; TYPE2KERATIN.
DR   PROSITE; PS00226; IF; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Intermediate filament; Keratin.
FT   CHAIN         1    524       Keratin, type II cytoskeletal 71.
FT                                /FTId=PRO_0000063738.
FT   REGION        1    130       Head.
FT   REGION      131    440       Rod.
FT   REGION      131    166       Coil 1A.
FT   REGION      167    185       Linker 1.
FT   REGION      186    277       Coil 1B.
FT   REGION      278    301       Linker 12.
FT   REGION      302    440       Coil 2.
FT   REGION      441    524       Tail.
FT   COMPBIAS     10    102       Gly-rich.
FT   SITE        382    382       Stutter.
FT   MUTAGEN     140    140       Missing: In caracul Rinshoken; causes a
FT                                wavy hair phenotype.
FT   MUTAGEN     143    143       A->G: In Rco12; causes a wavy pelage and
FT                                curly vibrissae.
FT   MUTAGEN     146    146       I->F: In Rco13; causes a wavy pelage and
FT                                curly vibrissae.
FT   MUTAGEN     431    431       A->D: In caracul; causes a wavy hair
FT                                phenotype.
SQ   SEQUENCE   524 AA;  57383 MW;  45FF0C44B440A72A CRC64;
     MSRQFTCKSG ASNRGFSGCS AVLSGGSSSS YRAGGKGLSG GFGSRSLYSL GGGRSITLNM
     ASGSGKNGGF GFGRNRASGF AGSIFGSVAL GPVCPAVCPP GGIHQVTVNE SLLAPLNVEL
     DPEIQKVRAQ EREQIKALNN KFASFIDKVR FLEQQNQVLQ TKWELLQQLD LNNCKNNLEP
     ILEGHISNMR KQLETLSGDR VRLDSELRNV RDVVEDYKKK YEEEINRRTA AENEFVLLKK
     DVDAAYANKV ELQAKVDTMD QDIKFFKCLF EAEMAQIQSH ISDMSVILSM DNNRNLDLDS
     IIDEVRAQYE EIALKSKAEA EALYQTKFQE LQLAAGRHGD DLKNTKNEIT ELTRFIQRLR
     SEIENAKKQA SNLETAIADA EQRGDSALKD ARAKLDELEG ALHQAKEELA RMLREYQELM
     SLKLALDMEI ATYRKLLESE ECRMSGEYSS PVSISIISST SGSGGYGFRP STVSGGYVAN
     STSCISGVCS VRGGENRSRG SASDYKDTLT KGSSLSTPSK KGGR
//
ID   AT2B2_MOUSE             Reviewed;        1198 AA.
AC   Q9R0K7; O88863;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   08-MAR-2011, entry version 106.
DE   RecName: Full=Plasma membrane calcium-transporting ATPase 2;
DE            Short=PMCA2;
DE            EC=3.6.3.8;
DE   AltName: Full=Plasma membrane calcium ATPase isoform 2;
DE   AltName: Full=Plasma membrane calcium pump isoform 2;
GN   Name=Atp2b2; Synonyms=Pmca2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT DFW SER-243.
RC   STRAIN=C3H/HeJ;
RX   MEDLINE=98361168; PubMed=9697703; DOI=10.1038/1284;
RA   Street V.A., McKee-Johnson J.W., Fonseca R.C., Tempel B.L.,
RA   Noben-Trauth K.;
RT   "Mutations in a plasma membrane Ca2+-ATPase gene cause deafness in
RT   deafwaddler mice.";
RL   Nat. Genet. 19:390-394(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LYS-412.
RC   STRAIN=BALB/C WMS;
RX   MEDLINE=21982766; PubMed=11985881; DOI=10.1016/S0168-0102(02)00008-1;
RA   Ueno T., Kameyama K., Hirata M., Ogawa M., Hatsuse H., Takagaki Y.,
RA   Ohmura M., Osawa N., Kudo Y.;
RT   "A mouse with a point mutation in plasma membrane Ca2+-ATPase isoform
RT   2 gene showed the reduced Ca2+ influx in cerebellar neurons.";
RL   Neurosci. Res. 42:287-297(2002).
RN   [3]
RP   PROTEIN SEQUENCE OF 16-32; 46-58; 62-77; 80-90; 197-249; 251-270;
RP   305-318; 438-455; 464-477; 489-506; 537-543; 554-561; 570-576;
RP   581-588; 593-601; 626-632; 684-694; 757-767; 785-818; 825-832;
RP   931-938; 976-983; 1104-1116; 1130-1152 AND 1164-1180.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   FUNCTION.
RX   MEDLINE=98334589; PubMed=9668038; DOI=10.1074/jbc.273.30.18693;
RA   Kozel P.J., Friedman R.A., Erway L.C., Yamoah E.N., Liu L.H.,
RA   Riddle T., Duffy J.J., Doetschman T., Miller M.L., Cardell E.L.,
RA   Shull G.E.;
RT   "Balance and hearing deficits in mice with a null mutation in the gene
RT   encoding plasma membrane Ca2+-ATPase isoform 2.";
RL   J. Biol. Chem. 273:18693-18696(1998).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1189 AND THR-1196, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1197, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis
CC       of ATP coupled with the transport of calcium out of the cell.
CC       Plays a role in maintaining balance and hearing.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + Ca(2+)(Cis) = ADP + phosphate +
CC       Ca(2+)(Trans).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Mainly expressed in brain cortex. Found at low
CC       levels in heart, liver, lung and testis during late gestation.
CC       Also found in cochlea (stereocilia and outer wall of hair cells).
CC   -!- DISEASE: Note=Atp2b2 null deficient mice are deaf.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       (TC 3.A.3) family. Type IIB subfamily.
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DR   EMBL; AF053471; AAC61255.1; -; mRNA.
DR   EMBL; AB030737; BAA83104.1; -; mRNA.
DR   EMBL; AB030738; BAA83105.1; -; mRNA.
DR   IPI; IPI00127713; -.
DR   RefSeq; NP_001031761.1; NM_001036684.1.
DR   RefSeq; NP_033853.1; NM_009723.2.
DR   UniGene; Mm.321755; -.
DR   ProteinModelPortal; Q9R0K7; -.
DR   SMR; Q9R0K7; 750-822.
DR   STRING; Q9R0K7; -.
DR   PhosphoSite; Q9R0K7; -.
DR   PRIDE; Q9R0K7; -.
DR   Ensembl; ENSMUST00000089003; ENSMUSP00000086398; ENSMUSG00000030302.
DR   Ensembl; ENSMUST00000101045; ENSMUSP00000098606; ENSMUSG00000030302.
DR   GeneID; 11941; -.
DR   KEGG; mmu:11941; -.
DR   UCSC; uc009dhn.1; mouse.
DR   CTD; 11941; -.
DR   MGI; MGI:105368; Atp2b2.
DR   eggNOG; roNOG14596; -.
DR   GeneTree; ENSGT00510000046331; -.
DR   HOVERGEN; HBG061286; -.
DR   OrthoDB; EOG4K9BBF; -.
DR   PhylomeDB; Q9R0K7; -.
DR   BRENDA; 3.6.3.8; 244.
DR   NextBio; 280043; -.
DR   ArrayExpress; Q9R0K7; -.
DR   Bgee; Q9R0K7; -.
DR   CleanEx; MM_ATP2B2; -.
DR   Genevestigator; Q9R0K7; -.
DR   GermOnline; ENSMUSG00000030302; Mus musculus.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0005929; C:cilium; IDA:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0030899; F:calcium-dependent ATPase activity; IMP:MGI.
DR   GO; GO:0005388; F:calcium-transporting ATPase activity; ISS:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR   GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
DR   GO; GO:0008022; F:protein C-terminus binding; ISS:UniProtKB.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   GO; GO:0060088; P:auditory receptor cell stereocilium organization; IMP:MGI.
DR   GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
DR   GO; GO:0021707; P:cerebellar granule cell differentiation; IMP:MGI.
DR   GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IMP:MGI.
DR   GO; GO:0046068; P:cGMP metabolic process; IMP:MGI.
DR   GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IMP:MGI.
DR   GO; GO:0007595; P:lactation; IMP:MGI.
DR   GO; GO:0040011; P:locomotion; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR   GO; GO:0006996; P:organelle organization; IMP:MGI.
DR   GO; GO:0045299; P:otolith mineralization; IMP:MGI.
DR   GO; GO:0051928; P:positive regulation of calcium ion transport; IMP:MGI.
DR   GO; GO:0008361; P:regulation of cell size; IMP:MGI.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR   GO; GO:0042428; P:serotonin metabolic process; IMP:MGI.
DR   GO; GO:0050808; P:synapse organization; IMP:MGI.
DR   InterPro; IPR022141; ATP_Ca_trans_C.
DR   InterPro; IPR023306; ATPase_cation_domN.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR006408; ATPase_P-typ_Ca-transp_PMCA.
DR   InterPro; IPR006069; ATPase_P-typ_cation-exchng_asu.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023300; ATPase_P-typ_cyto_domA.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Gene3D; G3DSA:2.70.150.10; ATPase_P-typ_cyto_domA; 1.
DR   Gene3D; G3DSA:3.40.1110.10; ATPase_P-typ_cyto_domN; 1.
DR   Gene3D; G3DSA:1.20.1110.10; ATPase_P-typ_TM_dom; 1.
DR   Pfam; PF12424; ATP_Ca_trans_C; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00121; NAKATPASE.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81660; ATPase_cation_domN; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01517; ATPase-IIB_Ca; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 4.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Calcium; Calcium transport; Calmodulin-binding;
KW   Cell membrane; Direct protein sequencing; Disease mutation; Hydrolase;
KW   Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Polymorphism; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1   1198       Plasma membrane calcium-transporting
FT                                ATPase 2.
FT                                /FTId=PRO_0000046215.
FT   TOPO_DOM      1     94       Cytoplasmic (Potential).
FT   TRANSMEM     95    115       Helical; (Potential).
FT   TOPO_DOM    116    152       Extracellular (Potential).
FT   TRANSMEM    153    173       Helical; (Potential).
FT   TOPO_DOM    174    345       Cytoplasmic (Potential).
FT   TRANSMEM    346    365       Helical; (Potential).
FT   TOPO_DOM    366    398       Extracellular (Potential).
FT   TRANSMEM    399    416       Helical; (Potential).
FT   TOPO_DOM    417    830       Cytoplasmic (Potential).
FT   TRANSMEM    831    850       Helical; (Potential).
FT   TOPO_DOM    851    860       Extracellular (Potential).
FT   TRANSMEM    861    881       Helical; (Potential).
FT   TOPO_DOM    882    901       Cytoplasmic (Potential).
FT   TRANSMEM    902    924       Helical; (Potential).
FT   TOPO_DOM    925    942       Extracellular (Potential).
FT   TRANSMEM    943    964       Helical; (Potential).
FT   TOPO_DOM    965    983       Cytoplasmic (Potential).
FT   TRANSMEM    984   1005       Helical; (Potential).
FT   TOPO_DOM   1006   1015       Extracellular (Potential).
FT   TRANSMEM   1016   1037       Helical; (Potential).
FT   TOPO_DOM   1038   1198       Cytoplasmic (Potential).
FT   REGION     1078   1095       Calmodulin-binding subdomain A (By
FT                                similarity).
FT   REGION     1096   1105       Calmodulin-binding subdomain B (By
FT                                similarity).
FT   COMPBIAS    294    297       Poly-Glu.
FT   ACT_SITE    454    454       4-aspartylphosphate intermediate (By
FT                                similarity).
FT   METAL       775    775       Magnesium (By similarity).
FT   METAL       779    779       Magnesium (By similarity).
FT   MOD_RES    1094   1094       Phosphothreonine; by PKC (By similarity).
FT   MOD_RES    1156   1156       Phosphoserine; by PKA (By similarity).
FT   MOD_RES    1186   1186       Phosphoserine (By similarity).
FT   MOD_RES    1189   1189       Phosphoserine.
FT   MOD_RES    1193   1193       Phosphoserine (By similarity).
FT   MOD_RES    1196   1196       Phosphothreonine.
FT   MOD_RES    1197   1197       Phosphoserine.
FT   VARIANT     243    243       G -> S (in dfw).
FT   VARIANT     412    412       E -> K.
SQ   SEQUENCE   1198 AA;  132588 MW;  BAA8CC28620D994B CRC64;
     MGDMTNSDFY SKNQRNESSH GGEFGCTMEE LRSLMELRGT EAVVKIKETY GDTEAICRRL
     KTSPVEGLPG TAPDLEKRKQ IFGQNFIPPK KPKTFLQLVW EALQDVTLII LEIAAIISLG
     LSFYHPPGES NEGCATAQGG AEDEGEAEAG WIEGAAILLS VICVVLVTAF NDWSKEKQFR
     GLQSRIEQEQ KFTVVRAGQV VQIPVAEIVV GDIAQIKYGD LLPADGLFIQ GNDLKIDESS
     LTGESDQVRK SVDKDPMLLS GTHVMEGSGR MVVTAVGVNS QTGIIFTLLG AGGEEEEKKD
     KKAKQQDGAA AMEMQPLKSA EGGDADDKKK ANMHKKEKSV LQGKLTKLAV QIGKAGLVMS
     AITVIILVLY FTVDTFVVNK KPWLTECTPV YVQYFVKFFI IGVTVLVVAV PEGLPLAVTI
     SLAYSVKKMM KDNNLVRHLD ACETMGNATA ICSDKTGTLT TNRMTVVQAY VGDVHYKEIP
     DPSSINAKTL ELLVNAIAIN SAYTTKILPP EKEGALPRQV GNKTECGLLG FVLDLRQDYE
     PVRSQMPEEK LYKVYTFNSV RKSMSTVIKM PDESFRMYSK GASEIVLKKC CKILSGAGEA
     RVFRPRDRDE MVKKVIEPMA CDGLRTICVA YRDFPSSPEP DWDNENDILN ELTCICVVGI
     EDPVRPEVPE AIRKCQRAGI TVRMVTGDNI NTARAIAIKC GIIHPGEDFL CLEGKEFNRR
     IRNEKGEIEQ ERIDKIWPKL RVLARSSPTD KHTLVKGIID STHTEQRQVV AVTGDGTNDG
     PALKKADVGF AMGIAGTDVA KEASDIILTD DNFSSIVKAV MWGRNVYDSI SKFLQFQLTV
     NVVAVIVAFT GACITQDSPL KAVQMLWVNL IMDTFASLAL ATEPPTETLL LRKPYGRNKP
     LISRTMMKNI LGHAVYQLTL IFTLLFVGEK MFQIDSGRNA PLHSPPSEHY TIIFNTFVMM
     QLFNEINARK IHGERNVFDG IFRNPIFCTI VLGTFAIQIV IVQFGGKPFS CSPLQLDQWM
     WCIFIGLGEL VWGQVIATIP TSRLKFLKEA GRLTQKEEIP EEELNEDVEE IDHAERELRR
     GQILWFRGLN RIQTQIRVVK AFRSSLYEGL EKPESRTSIH NFMAHPEFRI EDSQPHIPLI
     DDTDLEEDAA LKQNSSPPSS LNKNNSAIDS GINLTTDTSK SATSSSPGSP IHSLETSL
//
ID   PCM1_MOUSE              Reviewed;        2025 AA.
AC   Q9R0L6; O70287; Q3URH6; Q7TMS7; Q8C9V2; Q91Y27; Q91Y28; Q91Y51;
AC   Q923L0; Q9CRK8; Q9CT57;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 56.
DE   RecName: Full=Pericentriolar material 1 protein;
DE            Short=PCM-1;
DE            Short=mPCM-1;
GN   Name=Pcm1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
RX   MEDLINE=20047083; PubMed=10579718; DOI=10.1083/jcb.147.5.969;
RA   Kubo A., Sasaki H., Yuba-Kubo A., Tsukita S., Shiina N.;
RT   "Centriolar satellites: molecular characterization, ATP-dependent
RT   movement toward centrioles and possible involvement in ciliogenesis.";
RL   J. Cell Biol. 147:969-980(1999).
RN   [2]
RP   ERRATUM.
RA   Kubo A., Sasaki H., Yuba-Kubo A., Tsukita S., Shiina N.;
RL   J. Cell Biol. 147:1585-1585(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-448 (ISOFORM 2).
RC   STRAIN=C57BL/6NCr; TISSUE=Hematopoietic stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-443 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1978-2025 (ISOFORMS 1/2).
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-78 (ISOFORMS 1/2), NUCLEOTIDE SEQUENCE
RP   [MRNA] OF 41-2004 (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 1922-2025
RP   (ISOFORMS 1/2), AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1193-2025.
RC   STRAIN=129S6/SvEvTac, and C57BL/6J; TISSUE=Placenta;
RA   van Geel M., Bolland D.J., Carim Todd L., Frants R.R., Hewitt J.E.,
RA   de Jong P.J.;
RT   "Comparative analysis of an evolutionary chromosomal breakpoint
RT   indicates a recent origin for the human 4q telomere.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1722-1784.
RX   MEDLINE=98345417; PubMed=9680377; DOI=10.1007/s003359900829;
RA   Grewal P.K., Bolland D.J., Todd L.C., Hewitt J.E.;
RT   "High-resolution mapping of mouse chromosome 8 identifies an
RT   evolutionary chromosomal breakpoint.";
RL   Mamm. Genome 9:603-607(1998).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1779-2005 (ISOFORMS 1/2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   MEDLINE=22354683; PubMed=12466851; DOI=10.1038/nature01266;
RA   Okazaki Y., Furuno M., Kasukawa T., Adachi J., Bono H., Kondo S.,
RA   Nikaido I., Osato N., Saito R., Suzuki H., Yamanaka I., Kiyosawa H.,
RA   Yagi K., Tomaru Y., Hasegawa Y., Nogami A., Schonbach C., Gojobori T.,
RA   Baldarelli R., Hill D.P., Bult C., Hume D.A., Quackenbush J.,
RA   Schriml L.M., Kanapin A., Matsuda H., Batalov S., Beisel K.W.,
RA   Blake J.A., Bradt D., Brusic V., Chothia C., Corbani L.E., Cousins S.,
RA   Dalla E., Dragani T.A., Fletcher C.F., Forrest A., Frazer K.S.,
RA   Gaasterland T., Gariboldi M., Gissi C., Godzik A., Gough J.,
RA   Grimmond S., Gustincich S., Hirokawa N., Jackson I.J., Jarvis E.D.,
RA   Kanai A., Kawaji H., Kawasawa Y., Kedzierski R.M., King B.L.,
RA   Konagaya A., Kurochkin I.V., Lee Y., Lenhard B., Lyons P.A.,
RA   Maglott D.R., Maltais L., Marchionni L., McKenzie L., Miki H.,
RA   Nagashima T., Numata K., Okido T., Pavan W.J., Pertea G., Pesole G.,
RA   Petrovsky N., Pillai R., Pontius J.U., Qi D., Ramachandran S.,
RA   Ravasi T., Reed J.C., Reed D.J., Reid J., Ring B.Z., Ringwald M.,
RA   Sandelin A., Schneider C., Semple C.A., Setou M., Shimada K.,
RA   Sultana R., Takenaka Y., Taylor M.S., Teasdale R.D., Tomita M.,
RA   Verardo R., Wagner L., Wahlestedt C., Wang Y., Watanabe Y., Wells C.,
RA   Wilming L.G., Wynshaw-Boris A., Yanagisawa M., Yang I., Yang L.,
RA   Yuan Z., Zavolan M., Zhu Y., Zimmer A., Carninci P., Hayatsu N.,
RA   Hirozane-Kishikawa T., Konno H., Nakamura M., Sakazume N., Sato K.,
RA   Shiraki T., Waki K., Kawai J., Aizawa K., Arakawa T., Fukuda S.,
RA   Hara A., Hashizume W., Imotani K., Ishii Y., Itoh M., Kagawa I.,
RA   Miyazaki A., Sakai K., Sasaki D., Shibata K., Shinagawa A.,
RA   Yasunishi A., Yoshino M., Waterston R., Lander E.S., Rogers J.,
RA   Birney E., Hayashizaki Y.;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=12112146; DOI=10.1002/cm.10043;
RA   Balczon R., Simerly C., Takahashi D., Schatten G.;
RT   "Arrest of cell cycle progression during first interphase in murine
RT   zygotes microinjected with anti-PCM-1 antibodies.";
RL   Cell Motil. Cytoskeleton 52:183-192(2002).
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=22291950; PubMed=12403812; DOI=10.1083/jcb.200204023;
RA   Dammermann A., Merdes A.;
RT   "Assembly of centrosomal proteins and microtubule organization depends
RT   on PCM-1.";
RL   J. Cell Biol. 159:255-266(2002).
RN   [10]
RP   SUBCELLULAR LOCATION.
RX   PubMed=12571289; DOI=10.1242/jcs.00282;
RA   Kubo A., Tsukita S.;
RT   "Non-membranous granular organelle consisting of PCM-1: subcellular
RT   distribution and cell-cycle-dependent assembly/disassembly.";
RL   J. Cell Sci. 116:919-928(2003).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-1766 AND
RP   SER-1769, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [12]
RP   TISSUE SPECIFICITY.
RX   PubMed=15107855; DOI=10.1038/ng1352;
RA   Kim J.C., Badano J.L., Sibold S., Esmail M.A., Hill J., Hoskins B.E.,
RA   Leitch C.C., Venner K., Ansley S.J., Ross A.J., Leroux M.R.,
RA   Katsanis N., Beales P.L.;
RT   "The Bardet-Biedl protein BBS4 targets cargo to the pericentriolar
RT   region and is required for microtubule anchoring and cell cycle
RT   progression.";
RL   Nat. Genet. 36:462-470(2004).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-69; SER-1766;
RP   SER-1769 AND SER-1777, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-864; SER-1287;
RP   SER-1432; SER-1434; SER-1729; SER-1766 AND SER-1769, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65 AND SER-1654, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Required for centrosome assembly and function. Essential
CC       for the correct localization of several centrosomal proteins
CC       probably including CEP250, CETN3, PCNT and NEK2. Required to
CC       anchor microtubules to the centrosome.
CC   -!- SUBUNIT: Self-associates. Interacts with BBS4, BBS8, CETN3, HAP1,
CC       NDE1 and NDEL1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
CC       cytoskeleton, centrosome. Cytoplasmic granule. Note=Localizes to
CC       cytoplasmic granules which are enriched around the centrosome.
CC       This centrosomal enrichment requires microtubules and dynein (By
CC       similarity). The majority of the protein dissociates from the
CC       centrosome during metaphase and subsequently localizes to the
CC       cleavage site in telophase.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9R0L6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9R0L6-2; Sequence=VSP_022612;
CC   -!- TISSUE SPECIFICITY: Expressed in the hippocampus and dentate
CC       gyrus, the columnar epithelial cells of bronchioles, the olfactory
CC       epithelium, the pericardium and the inner segment of the retina.
CC   -!- DEVELOPMENTAL STAGE: Maternally derived during fertilization.
CC       Expressed in the pericardium of the developing embryo and in the
CC       epidermal layer surrounding the digits.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the PCM1 family.
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DR   EMBL; AB029291; BAA87861.1; -; mRNA.
DR   EMBL; BC053728; AAH53728.1; -; mRNA.
DR   EMBL; AK011147; BAB27430.3; -; mRNA.
DR   EMBL; AK040482; BAC30604.1; -; mRNA.
DR   EMBL; AK141516; BAE24712.1; -; mRNA.
DR   EMBL; AY028080; AAK21980.1; -; Genomic_DNA.
DR   EMBL; AF352180; AAK39513.1; -; mRNA.
DR   EMBL; AF369838; AAK39564.1; -; mRNA.
DR   EMBL; AF369839; AAK39565.1; -; mRNA.
DR   EMBL; AF039021; AAC96068.1; -; Genomic_DNA.
DR   EMBL; AK020493; BAB32121.1; -; mRNA.
DR   IPI; IPI00127764; -.
DR   IPI; IPI00828325; -.
DR   RefSeq; NP_076151.2; NM_023662.3.
DR   UniGene; Mm.117896; -.
DR   ProteinModelPortal; Q9R0L6; -.
DR   STRING; Q9R0L6; -.
DR   PhosphoSite; Q9R0L6; -.
DR   PRIDE; Q9R0L6; -.
DR   Ensembl; ENSMUST00000045199; ENSMUSP00000039056; ENSMUSG00000031592.
DR   Ensembl; ENSMUST00000045218; ENSMUSP00000039709; ENSMUSG00000031592.
DR   GeneID; 18536; -.
DR   KEGG; mmu:18536; -.
DR   UCSC; uc009lnr.1; mouse.
DR   UCSC; uc009lns.1; mouse.
DR   CTD; 18536; -.
DR   MGI; MGI:1277958; Pcm1.
DR   eggNOG; roNOG08562; -.
DR   GeneTree; ENSGT00390000006641; -.
DR   HOVERGEN; HBG053890; -.
DR   OrthoDB; EOG4Q84WK; -.
DR   NextBio; 294304; -.
DR   ArrayExpress; Q9R0L6; -.
DR   Bgee; Q9R0L6; -.
DR   CleanEx; MM_PCM1; -.
DR   Genevestigator; Q9R0L6; -.
DR   GO; GO:0034451; C:centriolar satellite; IDA:BHF-UCL.
DR   GO; GO:0000242; C:pericentriolar material; IDA:BHF-UCL.
DR   GO; GO:0005515; F:protein binding; IPI:BHF-UCL.
DR   GO; GO:0022027; P:interkinetic nuclear migration; IMP:BHF-UCL.
DR   GO; GO:0034453; P:microtubule anchoring; IMP:BHF-UCL.
DR   GO; GO:0050768; P:negative regulation of neurogenesis; IMP:BHF-UCL.
DR   GO; GO:0071539; P:protein localization to centrosome; IMP:BHF-UCL.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Phosphoprotein.
FT   CHAIN         1   2025       Pericentriolar material 1 protein.
FT                                /FTId=PRO_0000274038.
FT   COILED      218    301       Potential.
FT   COILED      399    426       Potential.
FT   COILED      492    518       Potential.
FT   COILED      652    772       Potential.
FT   COILED      822    856       Potential.
FT   COILED      985   1017       Potential.
FT   COILED     1061   1086       Potential.
FT   MOD_RES      61     61       Phosphothreonine (By similarity).
FT   MOD_RES      65     65       Phosphoserine.
FT   MOD_RES      68     68       Phosphoserine (By similarity).
FT   MOD_RES      69     69       Phosphoserine.
FT   MOD_RES      93     93       Phosphoserine (By similarity).
FT   MOD_RES     110    110       Phosphoserine (By similarity).
FT   MOD_RES     116    116       Phosphoserine (By similarity).
FT   MOD_RES     119    119       Phosphoserine (By similarity).
FT   MOD_RES     159    159       Phosphoserine (By similarity).
FT   MOD_RES     356    356       Phosphoserine (By similarity).
FT   MOD_RES     372    372       Phosphoserine (By similarity).
FT   MOD_RES     399    399       N6-acetyllysine (By similarity).
FT   MOD_RES     859    859       Phosphoserine (By similarity).
FT   MOD_RES     864    864       Phosphoserine.
FT   MOD_RES     867    867       Phosphoserine (By similarity).
FT   MOD_RES     870    870       Phosphoserine (By similarity).
FT   MOD_RES     875    875       Phosphothreonine (By similarity).
FT   MOD_RES     957    957       Phosphoserine (By similarity).
FT   MOD_RES     988    988       Phosphoserine (By similarity).
FT   MOD_RES    1182   1182       Phosphoserine (By similarity).
FT   MOD_RES    1184   1184       Phosphoserine (By similarity).
FT   MOD_RES    1185   1185       Phosphoserine (By similarity).
FT   MOD_RES    1228   1228       Phosphoserine (By similarity).
FT   MOD_RES    1254   1254       Phosphoserine (By similarity).
FT   MOD_RES    1257   1257       Phosphoserine (By similarity).
FT   MOD_RES    1259   1259       Phosphoserine (By similarity).
FT   MOD_RES    1287   1287       Phosphoserine.
FT   MOD_RES    1370   1370       Phosphoserine (By similarity).
FT   MOD_RES    1432   1432       Phosphoserine.
FT   MOD_RES    1434   1434       Phosphoserine.
FT   MOD_RES    1654   1654       Phosphoserine.
FT   MOD_RES    1695   1695       Phosphoserine (By similarity).
FT   MOD_RES    1729   1729       Phosphoserine.
FT   MOD_RES    1766   1766       Phosphoserine.
FT   MOD_RES    1769   1769       Phosphoserine.
FT   MOD_RES    1777   1777       Phosphoserine.
FT   MOD_RES    1978   1978       Phosphoserine (By similarity).
FT   MOD_RES    2024   2024       Phosphoserine (By similarity).
FT   VAR_SEQ     263    263       R -> RENEEEDVRTVDSAVGSGSVAESTSLNADVQSEASD
FT                                TTAR (in isoform 2).
FT                                /FTId=VSP_022612.
FT   CONFLICT    305    305       A -> T (in Ref. 3; AAH53728).
FT   CONFLICT    408    408       Q -> R (in Ref. 3; AAH53728).
FT   CONFLICT   1216   1216       V -> I (in Ref. 5; AAK39513).
FT   CONFLICT   1329   1329       N -> S (in Ref. 5; AAK39513).
FT   CONFLICT   1819   1819       V -> I (in Ref. 5; AAK39513 and 7;
FT                                BAB32121).
FT   CONFLICT   2018   2025       ETVGAQSI -> GKSYQF (in Ref. 4; BAC30604).
SQ   SEQUENCE   2025 AA;  228833 MW;  728456FD2DAA361F CRC64;
     MATGGGPFEE VMHDQDLPNW SNDSVDDRLN NMEWGGQQKK ANRSSEKNKK KFGVASDKRV
     TNAISPESSP GVGRRRTKIP HTFPHSRYMT QMSVPEQAEL EKLKQRINFS DLDQRSIGSD
     SQGRATAANN KRQLSENRKP FNFLPMQINT NKSKDATASL PKREMTTSAQ CKELFASALS
     NDLLQNCQVS EEDGRGEPAM ESSQIVSRLV QIRDYITKAS SMREDLVEKN ERSANVERLT
     HLIEHLKEQE KSYMKFLQKI LARDPQQEPM EETENLKKQH DLLKRMLQQQ EQLRALQGRQ
     AALLALQHKA EQAIAVMDDS VVTETTGSLS GVSITSELNE ELNDLIQRFH NQLRDSQPPA
     VPDNRRQAES LSLTREISQS RNPSVSEHLP DEKVQLFSKM RVLQEKKQKM DKLLGELHNL
     RDQHLNNSSF VPSTSLQRSG DKRSSTVALS APVGFASAVN GEANSLISSV PCPATSLVSQ
     NESENEGHLN PAEKLQKLNE VQKRLNELRE LVHYYEQTSD MMTDAVNENT KDEETEESEY
     DSEHENSEPV TNIRNPQVAS TWNEVNTNSN TQCGSNNRDG RPVNSNCEIN NRSAANIRAL
     NMPPLDCRYN REGEQRLHVA HGEDEEEEVE EEGVSGASLS SRRSSLVDEA PEDEEFEQKI
     SRLMAAKEKL KQLQDLVAMV QDDDATQVVV PAASNLDDFY AAEEDIKQNS NNARENSNKI
     DTGVNEKTRE KFYEAKLQQQ QRELKQLQEE RKKLIEIQEK IQAVQKACPD LQLSATSISS
     GPTKKYLPAI TSTPTVNEND SSTSKCVIDP EDSSVVDNEL WSDMRRHEML REELRQRRKQ
     LEALMAEHQR RQGLAETSSP VAISLRSDGS ENLCTPQQSR TEKTMATWGG STQCALDEEG
     DEDGYLSEGI VRTDEEEEEE QDASSNDNFP IYPPSMNQNS YNVKETKTRW KSNRPVSADG
     NYRPLAKTRQ QNISMQRQEN LRWVSELSYI EEKEQWQEQI NQLKKQLDFS VNICQTLMQD
     QQTLSCLLQT LLTGPYSVLP SNVASPQVHL IMHQLNQCYT QLTWQQNNVQ RLKQMLTELM
     RQQNQHPEKP RSKERGSSAS HPSSPNLFCP FSFPTQPVNL FNLPGFTNFP SFAPGMNFSP
     LFPSNFGDFS QNVSTPTEQQ QPLAQNPSGK TEYMAFPKPF ESSSSLGAEK QRNQKQPEEE
     AENTKTPWLY DQEGGVEKPF FKTGFTESVE KATNSNRKNQ PDTSRRRRQF DEESLESFSS
     MPDPIDPTTV TKTFKTRKAS AQASLASKDK TPKSKSKKRN STQLKSRVKN IGYESASVSS
     TCEPCKNRNR HSAQTEEPVQ AKLFSRKNHE QLEKIIKYSR SAEISSETGS DFSMFEALRD
     TIYSEVATLI SQNESRPHFL IELFHELQLL NTDYLRQRAL YALQDIVSRH ISESDEREGE
     NVKPVNSGTW VASNSELTPS ESLVTTDDET FEKNFERETH KVSEQNDADN VSVMSVSSNF
     EPFATDDLGN TVIHLDQALA RMREYERMKT ETESHSNMRC TCRVIEDEDG AAAAATVSNS
     EETPIIENHN SPQPISDVSA VPCPRIDTQQ LDRQIKAIMK EVIPFLKEHM DEVCSSQLLT
     SVRRMVLTLT QQNDESKEFV KFFHKQLGSI LQDSLAKFAG RKLKDCGEDL LVEISEVLFN
     ELAFFKLMQD LDNNSIAVKQ RCKRKIEAAG VRQSYAKEAK RILEGDHGSP AGEIDDEDKD
     KDETETVKQT QTSEVYDAKG PKNVRSDVSD QEEDEESERC PVSINLSKAE SQALTNYGSG
     EDENEDEEME DFEESPVDVQ TSLQANTETT EENEHDSQIL QHDLEKTPES TNVPSDQEPT
     SKNDQDSSPV KPCYLNILEN EQQLNSATHK DSLTTTDSSK QPEPLPLPLA ASETLVPRVK
     EVKSAQETPE SSLAGSPDTE SPVLVNDYEA ESGNISQKSD EEDFVKVEDL PLKLTVYSEE
     ELRKKMIEEE QKNHLSGEIC EMQTEELAGN SQILKEPETV GAQSI
//
ID   CELR2_MOUSE             Reviewed;        2920 AA.
AC   Q9R0M0; Q99K26; Q9Z2R4;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2002, sequence version 2.
DT   08-MAR-2011, entry version 111.
DE   RecName: Full=Cadherin EGF LAG seven-pass G-type receptor 2;
DE   AltName: Full=Flamingo homolog;
DE   Flags: Precursor;
GN   Name=Celsr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=99418630; PubMed=10490098; DOI=10.1016/S0092-8674(00)80046-X;
RA   Usui T., Shima Y., Shimada Y., Hirano S., Burgess R.W., Schwarz T.L.,
RA   Takeichi M., Uemura T.;
RT   "Flamingo, a seven-pass transmembrane cadherin, regulates planar cell
RT   polarity under the control of frizzled.";
RL   Cell 98:585-595(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 158-170 AND 205-215, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1913-2796, AND TISSUE SPECIFICITY.
RX   MEDLINE=20253755; PubMed=10790539; DOI=10.1007/s003350010073;
RA   Formstone C.J., Barclay J., Rees M., Little P.F.R.;
RT   "Chromosomal localization of Celsr2 and Celsr3 in the mouse; Celsr3 is
RT   a candidate for the tippy (tip) lethal mutant on chromosome 9.";
RL   Mamm. Genome 11:392-394(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2014-2920 (ISOFORM 2).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   DEVELOPMENTAL STAGE.
RX   MEDLINE=21839555; PubMed=11850187; DOI=10.1016/S0925-4773(01)00623-2;
RA   Tissir F., De-Backer O., Goffinet A.M., Lambert de Rouvroit C.A.;
RT   "Developmental expression profiles of Celsr (Flamingo) genes in the
RT   mouse.";
RL   Mech. Dev. 112:157-160(2002).
CC   -!- FUNCTION: Receptor that may have an important role in cell/cell
CC       signaling during nervous system formation.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9R0M0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9R0M0-2; Sequence=VSP_025765;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in the CNS and in the eye.
CC   -!- DEVELOPMENTAL STAGE: Predominantly expressed in the developing
CC       CNS, the emerging dorsal root ganglia and cranial ganglia. In the
CC       CNS, expression is uniform along the rostrocaudal axis. During
CC       gastrulation, it is expressed within the anterior neural ectoderm.
CC       At E10, expression is strong in the ventricular zones (VZ) in all
CC       sectors of the brain, and lower in the marginal zones (MZ).
CC       Between E12 and E15, expression is prominant in the brain. It is
CC       strong in VZ, lower in MZ, except in telecephalic MZ where it is
CC       predominant. The intensity is higher in all VZ, and lower in
CC       differenciating fields than in VZ, except in the cerebral
CC       hemispheres, and to a lesser extent in the tectum and cerebellum.
CC       A weak expression is also observed in the fetal lungs, kidney and
CC       epithelia. In the newborn and postnatal stages, expression remains
CC       restricted to the VZ as well as in migrating and postmigratory
CC       cells throughout the brain.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains
CC       (By similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       LN-TM7 subfamily.
CC   -!- SIMILARITY: Contains 9 cadherin domains.
CC   -!- SIMILARITY: Contains 7 EGF-like domains.
CC   -!- SIMILARITY: Contains 1 GPS domain.
CC   -!- SIMILARITY: Contains 1 laminin EGF-like domain.
CC   -!- SIMILARITY: Contains 2 laminin G-like domains.
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DR   EMBL; AB028499; BAA84070.1; -; mRNA.
DR   EMBL; AF031573; AAC68837.1; -; mRNA.
DR   EMBL; BC005499; AAH05499.1; -; mRNA.
DR   IPI; IPI00313878; -.
DR   IPI; IPI00850704; -.
DR   UniGene; Mm.39728; -.
DR   ProteinModelPortal; Q9R0M0; -.
DR   SMR; Q9R0M0; 174-1126, 1229-1369, 1577-1612, 1618-1774, 1809-1971.
DR   STRING; Q9R0M0; -.
DR   MEROPS; S63.009; -.
DR   MEROPS; S63.015; -.
DR   PhosphoSite; Q9R0M0; -.
DR   PRIDE; Q9R0M0; -.
DR   Ensembl; ENSMUST00000090558; ENSMUSP00000088046; ENSMUSG00000068740.
DR   UCSC; uc008qyx.1; mouse.
DR   MGI; MGI:1858235; Celsr2.
DR   GeneTree; ENSGT00580000081266; -.
DR   HOGENOM; HBG357942; -.
DR   HOVERGEN; HBG050887; -.
DR   InParanoid; Q9R0M0; -.
DR   OrthoDB; EOG4KKZ23; -.
DR   ArrayExpress; Q9R0M0; -.
DR   Bgee; Q9R0M0; -.
DR   Genevestigator; Q9R0M0; -.
DR   GermOnline; ENSMUSG00000068740; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007156; P:homophilic cell adhesion; IDA:BHF-UCL.
DR   GO; GO:0021999; P:neural plate anterior/posterior regionalization; IDA:BHF-UCL.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:InterPro.
DR   GO; GO:0032583; P:regulation of gene-specific transcription; IDA:BHF-UCL.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IDA:BHF-UCL.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR008985; ConA-like_lec_gl.
DR   InterPro; IPR013320; ConA-like_subgrp.
DR   InterPro; IPR022624; DUF3497.
DR   InterPro; IPR006209; EGF.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR002049; EGF_laminin.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR001879; GPCR_2_extracellular_dom.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR000203; GPS_dom.
DR   InterPro; IPR001791; Laminin_G.
DR   InterPro; IPR012680; Laminin_G_2.
DR   InterPro; IPR001368; TNFR_Cys_rich_reg.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 9.
DR   Gene3D; G3DSA:2.60.120.200; ConA_like_subgrp; 2.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF00028; Cadherin; 8.
DR   Pfam; PF12003; DUF3497; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF01825; GPS; 1.
DR   Pfam; PF00053; Laminin_EGF; 1.
DR   Pfam; PF02210; Laminin_G_2; 2.
DR   PRINTS; PR00205; CADHERIN.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   SMART; SM00112; CA; 9.
DR   SMART; SM00181; EGF; 6.
DR   SMART; SM00180; EGF_Lam; 1.
DR   SMART; SM00303; GPS; 1.
DR   SMART; SM00008; HormR; 1.
DR   SMART; SM00282; LamG; 2.
DR   SMART; SM00208; TNFR; 1.
DR   SUPFAM; SSF49313; Cadherin; 9.
DR   SUPFAM; SSF49899; ConA_like_lec_gl; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00232; CADHERIN_1; 6.
DR   PROSITE; PS50268; CADHERIN_2; 9.
DR   PROSITE; PS00022; EGF_1; 6.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 5.
DR   PROSITE; PS01248; EGF_LAM_1; 1.
DR   PROSITE; PS50027; EGF_LAM_2; 1.
DR   PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; FALSE_NEG.
DR   PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; FALSE_NEG.
DR   PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell membrane; Developmental protein;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   G-protein coupled receptor; Glycoprotein; Hydroxylation;
KW   Laminin EGF-like domain; Membrane; Receptor; Repeat; Signal;
KW   Transducer; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     31       Potential.
FT   CHAIN        32   2920       Cadherin EGF LAG seven-pass G-type
FT                                receptor 2.
FT                                /FTId=PRO_0000012917.
FT   TOPO_DOM     32   2381       Extracellular (Potential).
FT   TRANSMEM   2382   2402       Helical; Name=1; (Potential).
FT   TOPO_DOM   2403   2414       Cytoplasmic (Potential).
FT   TRANSMEM   2415   2434       Helical; Name=2; (Potential).
FT   TOPO_DOM   2435   2439       Extracellular (Potential).
FT   TRANSMEM   2440   2460       Helical; Name=3; (Potential).
FT   TOPO_DOM   2461   2481       Cytoplasmic (Potential).
FT   TRANSMEM   2482   2502       Helical; Name=4; (Potential).
FT   TOPO_DOM   2503   2519       Extracellular (Potential).
FT   TRANSMEM   2520   2540       Helical; Name=5; (Potential).
FT   TOPO_DOM   2541   2564       Cytoplasmic (Potential).
FT   TRANSMEM   2565   2585       Helical; Name=6; (Potential).
FT   TOPO_DOM   2586   2592       Extracellular (Potential).
FT   TRANSMEM   2593   2613       Helical; Name=7; (Potential).
FT   TOPO_DOM   2614   2920       Cytoplasmic (Potential).
FT   DOMAIN      182    289       Cadherin 1.
FT   DOMAIN      290    399       Cadherin 2.
FT   DOMAIN      400    506       Cadherin 3.
FT   DOMAIN      507    611       Cadherin 4.
FT   DOMAIN      612    713       Cadherin 5.
FT   DOMAIN      714    816       Cadherin 6.
FT   DOMAIN      817    922       Cadherin 7.
FT   DOMAIN      923   1024       Cadherin 8.
FT   DOMAIN     1029   1147       Cadherin 9.
FT   DOMAIN     1229   1287       EGF-like 1; atypical.
FT   DOMAIN     1289   1319       EGF-like 2; calcium-binding.
FT   DOMAIN     1329   1367       EGF-like 3; calcium-binding.
FT   DOMAIN     1368   1572       Laminin G-like 1.
FT   DOMAIN     1575   1611       EGF-like 4; calcium-binding.
FT   DOMAIN     1615   1792       Laminin G-like 2.
FT   DOMAIN     1788   1830       EGF-like 5; calcium-binding.
FT   DOMAIN     1831   1868       EGF-like 6; calcium-binding.
FT   DOMAIN     1884   1923       EGF-like 7; calcium-binding.
FT   DOMAIN     1925   1972       Laminin EGF-like.
FT   DOMAIN     2317   2369       GPS.
FT   COMPBIAS   2744   2749       Poly-Glu.
FT   MOD_RES    1592   1592       (3R)-3-hydroxyasparagine (Potential).
FT   CARBOHYD    486    486       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    558    558       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    702    702       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1037   1037       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1077   1077       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1183   1183       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1213   1213       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1502   1502       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1566   1566       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1742   1742       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1828   1828       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1901   1901       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2025   2025       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2044   2044       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2062   2062       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2324   2324       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2346   2346       N-linked (GlcNAc...) (Potential).
FT   DISULFID   1293   1304       By similarity.
FT   DISULFID   1298   1313       By similarity.
FT   DISULFID   1315   1318       By similarity.
FT   DISULFID   1333   1344       By similarity.
FT   DISULFID   1338   1354       By similarity.
FT   DISULFID   1356   1366       By similarity.
FT   DISULFID   1546   1572       By similarity.
FT   DISULFID   1579   1590       By similarity.
FT   DISULFID   1584   1599       By similarity.
FT   DISULFID   1601   1610       By similarity.
FT   DISULFID   1792   1803       By similarity.
FT   DISULFID   1798   1818       By similarity.
FT   DISULFID   1820   1829       By similarity.
FT   DISULFID   1833   1844       By similarity.
FT   DISULFID   1838   1856       By similarity.
FT   DISULFID   1858   1867       By similarity.
FT   DISULFID   1888   1900       By similarity.
FT   DISULFID   1890   1907       By similarity.
FT   DISULFID   1909   1922       By similarity.
FT   DISULFID   1925   1937       By similarity.
FT   DISULFID   1927   1944       By similarity.
FT   DISULFID   1946   1955       By similarity.
FT   DISULFID   1958   1970       By similarity.
FT   VAR_SEQ    2913   2920       Missing (in isoform 2).
FT                                /FTId=VSP_025765.
FT   CONFLICT   2199   2199       V -> L (in Ref. 4; AAH05499).
FT   CONFLICT   2283   2283       A -> V (in Ref. 4; AAH05499).
FT   CONFLICT   2535   2535       S -> R (in Ref. 1; BAA84070).
FT   CONFLICT   2571   2571       L -> R (in Ref. 3; AAC68837).
FT   CONFLICT   2639   2639       Y -> S (in Ref. 4; AAH05499).
FT   CONFLICT   2761   2761       L -> C (in Ref. 1; BAA84070).
FT   CONFLICT   2796   2796       K -> R (in Ref. 3; AAC68837).
FT   CONFLICT   2803   2803       A -> P (in Ref. 4; AAH05499).
FT   CONFLICT   2900   2900       N -> K (in Ref. 4; AAH05499).
SQ   SEQUENCE   2920 AA;  317593 MW;  B412317C916E73A9 CRC64;
     MRTRAASAPL PTPLLPLLLL LLLLPPSPLL GDQVGPCRSL GSGGRSSSGA CAPVGWLCPA
     SASNLWLYTS RCRESGIELT GHLVPHHDGL RVWCPESGAH IPLPPSSEGC PWSCRLLGIG
     GHLSPQGTLT LPEEHPCLKA PRLRCQSCKL AQAPGLRAGE GSPEESLGGR RKRNVNTAPQ
     FQPPSYQATV PENQPAGTSV ASLRAIDPDE GEAGRLEYTM DALFDSRSNH FFSLDPITGV
     VTTAEELDRE TKSTHVFRVT AQDHGMPRRS ALATLTILVT DTNDHDPVFE QQEYKESLRE
     NLEVGYEVLT VRATDGDAPP NANILYRLLE GAGDSPSDAF EIDPRSGVIR TRGPVDREEV
     ESYKLTVEAS DQGRDPGPRS STAIVFLSVE DDNDNAPQFS EKRYVVQVRE DVTPGAPVLR
     VTASDRDKGS NALVHYSIMS GNARGQFYLD AQTGALDVVS PLDYETTKEY TLRIRAQDGG
     RPPLSNVSGL VTVQVLDIND IRPPIFVSTP FQATVLESVP LGYLVLHVQA IDADAGDNAR
     LEYSLAGVGH DFPFTINNGT GWISVAAELD REEVDFYSFG VEARDHGTPA LTASASVSVT
     ILDVNDNNPT FTQPEYTVRL NEDAAVGTSV VTVSAVDRHA HSVITYQITS GNTRNRFSIT
     SQSGGGLVSL ALPLDYKLER QYVLAVTASD GTRQDTAQIV VNVTDANTHR PVFQSSHYTV
     NGNEDRPAGT TVVLISATDE DTGENARITY FMEDSIPQFR IDGDTGAVTT QAELDYEDQV
     SYTLAITARD NGIPQKSDTT YLEILVNDVN DNAPQFLRDS YQGTVYEDVP PFTSVLQILA
     TDRDSGLNGR VFYTFQGGDD GDGDFIVEST SGIVRTLRRL DRENVAQYVL RAYAVDKGMP
     PARTPMEVTV TVLDGNDNPP VFEQDEFDVF VEENSPIGLA VARVTATDPD EGTNAQIMYQ
     IVEGNIPEVF QLDIFSGELT ALVDLDYEDR PEYVLVIQAT SAPLVSRATV HVRLLDRNDN
     PPVLGNFEIL FNNYVTNRSS SFPGGAIGRV PAHDPDISDS LTYSFERGNE LSLVLLNAST
     GELRLSRALD NNRPLEAIMS VLVSDGVHSV TAQCSLRVTI ITDEMLTHSI TLRLEDMSPE
     RFLSPLLGLF IQAVAATLAT PPDHVVVFNV QRDTDAPGGH ILNVSLSVGQ PPGPGGGPPF
     LPSEDLQERL YLNRSLLTAI SAKRVLPFDR QHLLREPCEN YMRCVSVLRF DSSAPFIASS
     SVLFRPIHLV GGLRCRCPPG LTGDYCETEV DLCYSRTCGP HGRCRSREGG YTCLCRGCYT
     GEHCEASTHS GRCTPGVCKN GGTCVNLLVG GIKCDCPSGH FEKPFCQVTT RSFPARPFIT
     FRGLHQRFHF TLALSFATKE RNGLLLYNGR FNEKHDFVAL EVIQEQVQLT FSAGESTTTV
     SPFVPGGVSD GQWHTVQLKY YNKPLLGQTG LPQGPSEQKV AVVSVDGCDT GVALRFGAML
     GNYSCAAQGT QGGSKKSLDL TGPLLLGGVP DLPESFPVRM RHFVGCMKDL QVDSRHIDMA
     DFIANNGTVP GCPTKKIVCD SSICHNGGTC VNQWNTFSCE CPLGFGGKSC AQEMANPQRF
     LGSSLVAWHG LYLPISQPWH LNLMFRTRQA DGVLLQAVTR GRSTITLQLR AGHVRLSMEG
     TGLQASSLHL EPGRANDGDW HHAQLALGAS RGPGHAILSF NYGQQTAEGN LGPRLHGLHL
     SNITVGGVPG PASGVARGFR GCLQGVRVSE TPEGVHSLDP SRGESINVEP GCSLPDPCDS
     NPCPTNSYYS NDWNSYSCSC VLGYYGDNCT NVCDLNPCEH QSVCTRKPNT PHGYICECLP
     NYLGPYCETR IDQPCPRGWW GHPTCGPCNC DVSKGFDPDC NKTSGECHCK EKHYRPPGSP
     TCLLCDCYPT GSLSRVCDPE DGQCPCKPGV IGRQCDRCDN PFAEVTTNGC EVNYDSCPRA
     IEAGIWWPRT RFGLPAAAPC PKGSFGTAVR HCDEHRGWLP PNLFNCTSVT FSELKGFAER
     LQRNESGLDS GRSQRLALLL RNATQHTSGY FGSDVKVAYQ LATRLLAHES AQRGFGLSAT
     QDVHFTENLL RVGSALLDAA NKRHWELIQQ TEGGTAWLLQ HYEAYASALA QNMRHTYLSP
     FTIVTPNIVI SVVRLDKGNF AGTKLPRYEA LRGERPPDVE TTVILPESVF REMPSMVRSA
     GPGEAQETEE LARRQRRHPE LSQGEAVASV IIYHTLAGLL PHNYDPDKRS LRVPKRPVIN
     TPAVSISVHD DEELLPRALD KPVTVQFRLL ETEERTKPIC VFWNHSILVS GTGGWSARGC
     EVVFRNESHV SCQCNHMTSF AVLMDMSRRE NGEILPLKTL TYVALGVTLA ALMLTFLFLT
     LLRALRSNQH GIRRNLTAAL GLAQLVFLLG INQADLPFAC TVIAILLHFL YLCTFSWALL
     EALHLYRALT EVRDVNASPM RFYYMLGWGV PAFITGLAVG LDPEGYGNPD FCWLSVYDTL
     IWSFAGPVAF AVSMSVFLYI LSARASCAAQ RQGFEKKGPV SGLRSSFTVL LLLSATWLLA
     LLSVNSDTLL FHYLFAACNC VQGPFIFLSY VVLSKEVRKA LKFACSRKPS PDPALTTKYT
     LTSSYNCPSP YADGRLYQPY GDSAGSLHSA SRSGKSQPSY IPFLLREEST LNPGQVPPGL
     GDPSGLFLEG QAQQHDPDTD SDSDLSLEDD QSGSYASTHS SDSEEEEEEA AFPGEQGWDS
     LLGPGAERLP LHSTPKDGGP GSGKVPWLGD FGTTTKENSG SGALEERPRE NGDALTREGS
     LGPLPGPSTQ PHKGILKKKC LPTISEKSSL LRLPLEQGTG SSRGSSISEG SRHGPPPRPP
     PRQSLQEQLN GVMPVAMSIN AGTVDEDSSG SEFLFFNFLH
//
ID   SYT11_MOUSE             Reviewed;         430 AA.
AC   Q9R0N3;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Synaptotagmin-11;
DE   AltName: Full=Synaptotagmin XI;
DE            Short=SytXI;
GN   Name=Syt11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Cerebellum;
RX   MEDLINE=20002669; PubMed=10531343; DOI=10.1074/jbc.274.44.31421;
RA   Fukuda M., Kanno E., Mikoshiba K.;
RT   "Conserved N-terminal cysteine motif is essential for homo- and
RT   heterodimer formation of synaptotagmins III, V, VI, and X.";
RL   J. Biol. Chem. 274:31421-31427(1999).
CC   -!- FUNCTION: May be involved in Ca(2+)-dependent exocytosis of
CC       secretory vesicles through Ca(2+) and phospholipid binding to the
CC       C2 domain or may serve as Ca(2+) sensors in the process of
CC       vesicular trafficking and exocytosis (By similarity).
CC   -!- COFACTOR: Binds 3 calcium ions per subunit. The ions are bound to
CC       the C2 domains (By similarity).
CC   -!- SUBUNIT: Homodimer. Can also form heterodimers. Interacts with
CC       PARK2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane; Single-pass membrane protein (By
CC       similarity).
CC   -!- PTM: Ubiquitinated and targeted to the proteasome complex for
CC       degradation (By similarity).
CC   -!- SIMILARITY: Belongs to the synaptotagmin family.
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; AB026808; BAA85780.1; -; mRNA.
DR   IPI; IPI00127865; -.
DR   UniGene; Mm.379376; -.
DR   ProteinModelPortal; Q9R0N3; -.
DR   SMR; Q9R0N3; 156-429.
DR   IntAct; Q9R0N3; 1.
DR   STRING; Q9R0N3; -.
DR   PhosphoSite; Q9R0N3; -.
DR   PRIDE; Q9R0N3; -.
DR   Ensembl; ENSMUST00000090945; ENSMUSP00000088464; ENSMUSG00000068923.
DR   Ensembl; ENSMUST00000107505; ENSMUSP00000103129; ENSMUSG00000068923.
DR   MGI; MGI:1859547; Syt11.
DR   GeneTree; ENSGT00600000084227; -.
DR   HOGENOM; HBG716633; -.
DR   HOVERGEN; HBG005010; -.
DR   InParanoid; Q9R0N3; -.
DR   OrthoDB; EOG4894MK; -.
DR   ArrayExpress; Q9R0N3; -.
DR   Bgee; Q9R0N3; -.
DR   CleanEx; MM_SYT11; -.
DR   Genevestigator; Q9R0N3; -.
DR   GermOnline; ENSMUSG00000068923; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005887; C:integral to plasma membrane; IDA:MGI.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR001565; Synaptotagmin.
DR   Pfam; PF00168; C2; 2.
DR   PRINTS; PR00399; SYNAPTOTAGMN.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 2.
PE   2: Evidence at transcript level;
KW   Calcium; Cell junction; Cytoplasmic vesicle; Membrane; Metal-binding;
KW   Repeat; Synapse; Transmembrane; Transmembrane helix; Ubl conjugation.
FT   CHAIN         1    430       Synaptotagmin-11.
FT                                /FTId=PRO_0000183970.
FT   TOPO_DOM      1     15       Vesicular (Potential).
FT   TRANSMEM     16     36       Helical; (Potential).
FT   TOPO_DOM     37    430       Cytoplasmic (Potential).
FT   DOMAIN      173    261       C2 1.
FT   DOMAIN      303    396       C2 2.
FT   METAL       187    187       Calcium 1 (By similarity).
FT   METAL       187    187       Calcium 2 (By similarity).
FT   METAL       194    194       Calcium 1 (By similarity).
FT   METAL       248    248       Calcium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       249    249       Calcium 1 (By similarity).
FT   METAL       249    249       Calcium 2 (By similarity).
FT   METAL       249    249       Calcium 3 (By similarity).
FT   METAL       252    252       Calcium 3 (By similarity).
FT   METAL       255    255       Calcium 2 (By similarity).
FT   METAL       255    255       Calcium 3 (By similarity).
SQ   SEQUENCE   430 AA;  48359 MW;  25E7CDFC4B4BE036 CRC64;
     MAEITNIRPS FDVSPVAAGL IGASVLVVCV SVTVFVWTCC HQQAEKKHKT PPYKFIHMLK
     GISIYPETLS NKKKIIKVRR DKDGPRRESG RGNLLINAES GLLSHDKDPR GPSPASCMDQ
     LPIKRDYGEE LRSPMTSLTP GESKPTSPSS PEEDVMLGSL TFSVDYNFPK KALVVTIQEA
     HGLPVMDDQT QGSDPYIKMT ILPDKRHRVK TRVLRKTLDP VFDETFTFYG IPYSQLQDLV
     LHFLVLSFDR FSRDDVIGEV MVPLAGVDPS TGKVQLTRDI IKRNIQKCIS RGELQVSLSY
     QPVAQRMTVV VLKARHLPKM DITGLSGNPY VKVNVYYGRK RIAKKKTHVK KCTLNPVFNE
     SFIYDIPTDL LPDISIEFLV IDFDRTTKNE VVGRLILGAH SVTTSGAEHW REVCESPRKP
     IAKWHSLSEY
//
ID   SYT10_MOUSE             Reviewed;         523 AA.
AC   Q9R0N4;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Synaptotagmin-10;
DE   AltName: Full=Synaptotagmin X;
DE            Short=SytX;
GN   Name=Syt10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Cerebellum;
RX   MEDLINE=20002669; PubMed=10531343; DOI=10.1074/jbc.274.44.31421;
RA   Fukuda M., Kanno E., Mikoshiba K.;
RT   "Conserved N-terminal cysteine motif is essential for homo- and
RT   heterodimer formation of synaptotagmins III, V, VI, and X.";
RL   J. Biol. Chem. 274:31421-31427(1999).
CC   -!- FUNCTION: May be involved in Ca(2+)-dependent exocytosis of
CC       secretory vesicles through Ca(2+) and phospholipid binding to the
CC       C2 domain or may serve as Ca(2+) sensors in the process of
CC       vesicular trafficking and exocytosis (By similarity).
CC   -!- COFACTOR: Binds 3 calcium ions per subunit. The ions are bound to
CC       the C2 domains (By similarity).
CC   -!- SUBUNIT: Homodimer. Can also form heterodimers.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane; Single-pass membrane protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the synaptotagmin family.
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB026807; BAA85779.1; -; mRNA.
DR   IPI; IPI00127866; -.
DR   RefSeq; NP_061273.1; NM_018803.2.
DR   UniGene; Mm.261601; -.
DR   ProteinModelPortal; Q9R0N4; -.
DR   SMR; Q9R0N4; 232-500.
DR   PRIDE; Q9R0N4; -.
DR   Ensembl; ENSMUST00000029441; ENSMUSP00000029441; ENSMUSG00000063260.
DR   GeneID; 54526; -.
DR   KEGG; mmu:54526; -.
DR   UCSC; uc007xhi.1; mouse.
DR   CTD; 54526; -.
DR   MGI; MGI:1859546; Syt10.
DR   GeneTree; ENSGT00600000084008; -.
DR   HOGENOM; HBG716633; -.
DR   HOVERGEN; HBG005010; -.
DR   InParanoid; Q9R0N4; -.
DR   OMA; MSFHKED; -.
DR   OrthoDB; EOG4VX251; -.
DR   PhylomeDB; Q9R0N4; -.
DR   NextBio; 311372; -.
DR   ArrayExpress; Q9R0N4; -.
DR   Bgee; Q9R0N4; -.
DR   CleanEx; MM_SYT10; -.
DR   Genevestigator; Q9R0N4; -.
DR   GermOnline; ENSMUSG00000063260; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   InterPro; IPR001565; Synaptotagmin.
DR   Pfam; PF00168; C2; 2.
DR   PRINTS; PR00360; C2DOMAIN.
DR   PRINTS; PR00399; SYNAPTOTAGMN.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 2.
PE   2: Evidence at transcript level;
KW   Calcium; Cell junction; Cytoplasmic vesicle; Membrane; Metal-binding;
KW   Repeat; Synapse; Transmembrane; Transmembrane helix.
FT   CHAIN         1    523       Synaptotagmin-10.
FT                                /FTId=PRO_0000183966.
FT   TOPO_DOM      1     55       Vesicular (Potential).
FT   TRANSMEM     56     76       Helical; (Potential).
FT   TOPO_DOM     77    523       Cytoplasmic (Potential).
FT   DOMAIN      233    334       C2 1.
FT   DOMAIN      365    468       C2 2.
FT   METAL       262    262       Calcium 1 (By similarity).
FT   METAL       262    262       Calcium 2 (By similarity).
FT   METAL       268    268       Calcium 1 (By similarity).
FT   METAL       320    320       Calcium 1 (By similarity).
FT   METAL       320    320       Calcium 2 (By similarity).
FT   METAL       321    321       Calcium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       322    322       Calcium 1 (By similarity).
FT   METAL       322    322       Calcium 2 (By similarity).
FT   METAL       322    322       Calcium 3 (By similarity).
FT   METAL       325    325       Calcium 3 (By similarity).
FT   METAL       328    328       Calcium 2 (By similarity).
FT   METAL       328    328       Calcium 3 (By similarity).
SQ   SEQUENCE   523 AA;  59019 MW;  1F551F4EF75A0A9B CRC64;
     MSFRKEDGVS SLCQKALHII TELCFAGQVE WDKCSGIFPA DRSGQGGGGT DISVSLLAVV
     VSFCGLALLV VSLFVFWKLC WPCWKSKLVA PNLSVLPQSI SSAPTEVFET EEKKEVEENE
     KPAPKAIEPA IKISHTSPDI PAEVQTALKE HLIKHARVQR QTTEPTSSSR HNSFRRHLPR
     QMNVSSVDFS VGTEPILQRG ETRTSIGRIK PELYKQKSVD SEGNRKDDVK TCGKLNFALQ
     YDYENELLVV KIIKALDLPA KDFTGTSDPY VKIYLLPDRK KKFQTRVHRK TLNPLFDELF
     QFPVVYDQLS NRKLHFSIYD FDRFSRHDMI GEVILDNLFE VSDLSREATV WKDIHCATTE
     SIDLGEIMFS LCYLPTAGRM TLTVIKCRNL KAMDITGSSD PYVKVSLMCE GRRLKKRKTT
     TKKNTLNPVY NEAIIFDIPP ENVDQVSLCI AVMDYDRVGH NEVIGVCRTG LDAEGLGRDH
     WNEMLAYHRK PITHWHPLLE LPGRATSFDS QGSCSSPRPP STP
//
ID   SYT5_MOUSE              Reviewed;         386 AA.
AC   Q9R0N5;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=Synaptotagmin-5;
DE   AltName: Full=Synaptotagmin IX;
DE   AltName: Full=Synaptotagmin V;
DE            Short=SytV;
GN   Name=Syt5; Synonyms=Syt9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Cerebellum;
RX   MEDLINE=20002669; PubMed=10531343; DOI=10.1074/jbc.274.44.31421;
RA   Fukuda M., Kanno E., Mikoshiba K.;
RT   "Conserved N-terminal cysteine motif is essential for homo- and
RT   heterodimer formation of synaptotagmins III, V, VI, and X.";
RL   J. Biol. Chem. 274:31421-31427(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 57-61; 240-248; 256-264 AND 269-280, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11751925; DOI=10.1074/jbc.C100588200;
RA   Fukuda M., Kowalchyk J.A., Zhang X., Martin T.F.J., Mikoshiba K.;
RT   "Synaptotagmin IX regulates Ca2+-dependent secretion in PC12 cells.";
RL   J. Biol. Chem. 277:4601-4604(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-278, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: May be involved in Ca(2+)-dependent exocytosis of
CC       secretory vesicles through Ca(2+) and phospholipid binding to the
CC       C2 domain or may serve as Ca(2+) sensors in the process of
CC       vesicular trafficking and exocytosis. Regulates the Ca(2+)-
CC       dependent secretion of norepinephrine in PC12 cells. Required for
CC       export from the endocytic recycling compartment to the cell
CC       surface.
CC   -!- COFACTOR: Binds 3 calcium ions per subunit. The ions are bound to
CC       the C2 domains (By similarity).
CC   -!- SUBUNIT: Homodimer. Can also form heterodimers. Interacts with
CC       both alpha- and beta-tubulin.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane; Single-pass membrane protein. Recycling
CC       endosome membrane; Single-pass membrane protein. Note=In mast
CC       cells, localizes to the endocytic recycling compartment.
CC   -!- SIMILARITY: Belongs to the synaptotagmin family.
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB026806; BAA85778.1; -; mRNA.
DR   EMBL; BC047148; AAH47148.1; -; mRNA.
DR   IPI; IPI00127867; -.
DR   RefSeq; NP_058604.1; NM_016908.2.
DR   UniGene; Mm.358663; -.
DR   ProteinModelPortal; Q9R0N5; -.
DR   SMR; Q9R0N5; 108-375.
DR   STRING; Q9R0N5; -.
DR   PhosphoSite; Q9R0N5; -.
DR   PRIDE; Q9R0N5; -.
DR   Ensembl; ENSMUST00000065957; ENSMUSP00000070322; ENSMUSG00000004961.
DR   GeneID; 53420; -.
DR   KEGG; mmu:53420; -.
DR   UCSC; uc009exy.1; mouse.
DR   CTD; 53420; -.
DR   MGI; MGI:1926368; Syt5.
DR   eggNOG; roNOG12491; -.
DR   GeneTree; ENSGT00600000084008; -.
DR   HOGENOM; HBG716633; -.
DR   HOVERGEN; HBG005010; -.
DR   InParanoid; Q9R0N5; -.
DR   OMA; CCFCLYR; -.
DR   OrthoDB; EOG4JHCFZ; -.
DR   PhylomeDB; Q9R0N5; -.
DR   NextBio; 310253; -.
DR   ArrayExpress; Q9R0N5; -.
DR   Bgee; Q9R0N5; -.
DR   CleanEx; MM_SYT5; -.
DR   CleanEx; MM_SYT9; -.
DR   Genevestigator; Q9R0N5; -.
DR   GermOnline; ENSMUSG00000004961; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0031045; C:dense core granule; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR   GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   InterPro; IPR001565; Synaptotagmin.
DR   Pfam; PF00168; C2; 2.
DR   PRINTS; PR00360; C2DOMAIN.
DR   PRINTS; PR00399; SYNAPTOTAGMN.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 2.
PE   1: Evidence at protein level;
KW   Calcium; Cell junction; Cytoplasmic vesicle;
KW   Direct protein sequencing; Endosome; Membrane; Metal-binding;
KW   Phosphoprotein; Repeat; Synapse; Transmembrane; Transmembrane helix.
FT   CHAIN         1    386       Synaptotagmin-5.
FT                                /FTId=PRO_0000183952.
FT   TOPO_DOM      1     24       Vesicular (Potential).
FT   TRANSMEM     25     45       Helical; (Potential).
FT   TOPO_DOM     46    386       Cytoplasmic (Potential).
FT   DOMAIN      124    211       C2 1.
FT   DOMAIN      253    344       C2 2.
FT   METAL       138    138       Calcium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       139    139       Calcium 1 (By similarity).
FT   METAL       139    139       Calcium 2 (By similarity).
FT   METAL       145    145       Calcium 1 (By similarity).
FT   METAL       197    197       Calcium 1 (By similarity).
FT   METAL       197    197       Calcium 2 (By similarity).
FT   METAL       198    198       Calcium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       199    199       Calcium 1 (By similarity).
FT   METAL       199    199       Calcium 2 (By similarity).
FT   METAL       199    199       Calcium 3 (By similarity).
FT   METAL       202    202       Calcium 3 (By similarity).
FT   METAL       205    205       Calcium 2 (By similarity).
FT   METAL       205    205       Calcium 3 (By similarity).
FT   MOD_RES     278    278       Phosphotyrosine.
SQ   SEQUENCE   386 AA;  43130 MW;  F884902E032082F6 CRC64;
     MFPEPPTLGS PAPKTPPDSS RIRQGAVPAW VLATIVLGSG LLVFSSCFCL YRKRCRRRMG
     KKSQAQAQVH LQEVKELGRS YIDKVQPEIE ELDRSPSMPG QQVSDKHQLG RLQYSLDYDF
     QTGQLLVGIL QAQGLAALDL GGSSDPYVSV YLLPDKRRRH ETKVHRQTLN PHFGETFAFK
     VPYVELGGRV LVMAVYDFDR FSRNDAIGEV RVPMSSVNLG RPVQAWRELQ VAPKEEQEKL
     GDICFSLRYV PTAGKLTVIV LEAKNLKKMD VGGLSDPYVK VHLLQGGKKV RKKKTTIKKN
     TLNPYYNEAF SFEVPCDQVQ KVQVELTVLD YDKLGKNEAI GRVAVGAAVG GAGLRHWADM
     LANPRRPIAQ WHSLRPPDRA RPIPAP
//
ID   SYT9_MOUSE              Reviewed;         491 AA.
AC   Q9R0N9; Q8C280;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=Synaptotagmin-9;
DE   AltName: Full=Synaptotagmin IX;
DE            Short=SytIX;
DE   AltName: Full=Synaptotagmin V;
GN   Name=Syt9; Synonyms=Syt5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR; TISSUE=Cerebellum;
RX   MEDLINE=20002669; PubMed=10531343; DOI=10.1074/jbc.274.44.31421;
RA   Fukuda M., Kanno E., Mikoshiba K.;
RT   "Conserved N-terminal cysteine motif is essential for homo- and
RT   heterodimer formation of synaptotagmins III, V, VI, and X.";
RL   J. Biol. Chem. 274:31421-31427(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-308, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
CC   -!- FUNCTION: May be involved in Ca(2+)-dependent exocytosis of
CC       secretory vesicles through Ca(2+) and phospholipid binding to the
CC       C2 domain or may serve as Ca(2+) sensors in the process of
CC       vesicular trafficking and exocytosis.
CC   -!- COFACTOR: Binds 3 calcium ions per subunit. The ions are bound to
CC       the C2 domains (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle,
CC       synaptic vesicle membrane; Single-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the synaptotagmin family.
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AB026802; BAA85774.1; -; mRNA.
DR   EMBL; AK089115; BAC40759.1; -; mRNA.
DR   IPI; IPI00284835; -.
DR   RefSeq; NP_068689.2; NM_021889.4.
DR   UniGene; Mm.302793; -.
DR   ProteinModelPortal; Q9R0N9; -.
DR   SMR; Q9R0N9; 221-491.
DR   IntAct; Q9R0N9; 1.
DR   STRING; Q9R0N9; -.
DR   PhosphoSite; Q9R0N9; -.
DR   PRIDE; Q9R0N9; -.
DR   Ensembl; ENSMUST00000073459; ENSMUSP00000073164; ENSMUSG00000062542.
DR   GeneID; 60510; -.
DR   KEGG; mmu:60510; -.
DR   CTD; 60510; -.
DR   MGI; MGI:1926373; Syt9.
DR   GeneTree; ENSGT00600000084008; -.
DR   HOGENOM; HBG716633; -.
DR   HOVERGEN; HBG005010; -.
DR   InParanoid; Q9R0N9; -.
DR   OrthoDB; EOG4SF95S; -.
DR   ArrayExpress; Q9R0N9; -.
DR   Bgee; Q9R0N9; -.
DR   CleanEx; MM_SYT5; -.
DR   CleanEx; MM_SYT9; -.
DR   Genevestigator; Q9R0N9; -.
DR   GermOnline; ENSMUSG00000062542; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0031045; C:dense core granule; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0005215; F:transporter activity; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   InterPro; IPR001565; Synaptotagmin.
DR   Pfam; PF00168; C2; 2.
DR   PRINTS; PR00360; C2DOMAIN.
DR   PRINTS; PR00399; SYNAPTOTAGMN.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 2.
PE   1: Evidence at protein level;
KW   Calcium; Cell junction; Cytoplasmic vesicle; Membrane; Metal-binding;
KW   Phosphoprotein; Repeat; Synapse; Transmembrane; Transmembrane helix.
FT   CHAIN         1    491       Synaptotagmin-9.
FT                                /FTId=PRO_0000183963.
FT   TOPO_DOM      1     52       Vesicular (Potential).
FT   TRANSMEM     53     73       Helical; (Potential).
FT   TOPO_DOM     74    491       Cytoplasmic (Potential).
FT   DOMAIN      222    323       C2 1.
FT   DOMAIN      354    457       C2 2.
FT   METAL       251    251       Calcium 1 (By similarity).
FT   METAL       251    251       Calcium 2 (By similarity).
FT   METAL       257    257       Calcium 1 (By similarity).
FT   METAL       309    309       Calcium 1 (By similarity).
FT   METAL       309    309       Calcium 2 (By similarity).
FT   METAL       310    310       Calcium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       311    311       Calcium 1 (By similarity).
FT   METAL       311    311       Calcium 2 (By similarity).
FT   METAL       311    311       Calcium 3 (By similarity).
FT   METAL       314    314       Calcium 3 (By similarity).
FT   METAL       317    317       Calcium 2 (By similarity).
FT   METAL       317    317       Calcium 3 (By similarity).
FT   MOD_RES     308    308       Phosphotyrosine.
FT   CONFLICT    488    488       L -> M (in Ref. 2; BAC40759).
SQ   SEQUENCE   491 AA;  56247 MW;  E08ECFD844D6EE14 CRC64;
     MPGARDALCH QALQLLAELC ARGALEHDSC QDFIYHLRDR ARPRLRDPDI SVSLLTLVVT
     ACGLALFGVS LFVSWKLCWV PWRERGLFSG SKDNNQEPLN YTDTETNEQE NSEDFLDPPT
     PCPDSSMKIS HTSPDIPLST QPGGQENCAH AVRVQRQVTE PTPSARHNSI RRQLNLSNPD
     FNIQQLQRQE QLTGIGRIKP ELYKQRSLDN DDGRRSNSKA CGKLNFILKY DCDLEQLIVK
     IHKAVNLPAK DFSGTSDPYV KIYLLPDRKT KHQTKVHRKT LNPVFDEVFL FPVHYNDLEA
     RKLHFSVYDF DRFSRHDLIG QVVVDHFFDL ADFPRECILW KDIEYVTNDN VDLGELMFSL
     CYLPTAGRLT ITIIKARNLK AMDITGASDP YVKVSLMCDG RRLKKRKTST KRNTLNPVYN
     EAIVFDVPPE SIDQIHLSIA VMDYDRVGHN EVIGVCQVGN EAERLGRDHW SEMLSYPRKP
     IAHWHSLLEK R
//
ID   SMAP_MOUSE              Reviewed;         181 AA.
AC   Q9R0P4;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Small acidic protein;
DE   AltName: Full=Sid 2057;
GN   Name=Smap; Synonyms=Sid2057;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.;
RT   "Mouse small acidic protein sid2057.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2; TISSUE=Embryo, Kidney, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Fetal brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-17, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17 AND SER-145, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- SIMILARITY: Belongs to the SMAP family.
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DR   EMBL; AB025407; BAA84692.1; -; mRNA.
DR   EMBL; AK003415; BAB22777.1; -; mRNA.
DR   EMBL; AK144059; BAE25676.1; -; mRNA.
DR   EMBL; AK167571; BAE39634.1; -; mRNA.
DR   EMBL; AK168206; BAE40166.1; -; mRNA.
DR   EMBL; AK169309; BAE41064.1; -; mRNA.
DR   EMBL; BC072575; AAH72575.1; -; mRNA.
DR   IPI; IPI00127941; -.
DR   RefSeq; NP_062746.1; NM_019772.2.
DR   UniGene; Mm.24231; -.
DR   ProteinModelPortal; Q9R0P4; -.
DR   STRING; Q9R0P4; -.
DR   PhosphoSite; Q9R0P4; -.
DR   PRIDE; Q9R0P4; -.
DR   Ensembl; ENSMUST00000032899; ENSMUSP00000032899; ENSMUSG00000030663.
DR   GeneID; 56372; -.
DR   KEGG; mmu:56372; -.
DR   UCSC; uc009jix.1; mouse.
DR   MGI; MGI:1929274; 1110004F10Rik.
DR   eggNOG; roNOG16389; -.
DR   GeneTree; ENSGT00390000000687; -.
DR   HOGENOM; HBG279999; -.
DR   HOVERGEN; HBG055732; -.
DR   InParanoid; Q9R0P4; -.
DR   OMA; DPESPED; -.
DR   OrthoDB; EOG4BRWN8; -.
DR   PhylomeDB; Q9R0P4; -.
DR   NextBio; 312428; -.
DR   ArrayExpress; Q9R0P4; -.
DR   Bgee; Q9R0P4; -.
DR   CleanEx; MM_1110004F10RIK; -.
DR   Genevestigator; Q9R0P4; -.
DR   GermOnline; ENSMUSG00000030663; Mus musculus.
PE   1: Evidence at protein level;
KW   Acetylation; Phosphoprotein.
FT   CHAIN         1    181       Small acidic protein.
FT                                /FTId=PRO_0000263657.
FT   COMPBIAS    109    137       Asp-rich.
FT   MOD_RES      15     15       Phosphoserine.
FT   MOD_RES      17     17       Phosphoserine.
FT   MOD_RES      25     25       Phosphoserine (By similarity).
FT   MOD_RES      84     84       Phosphotyrosine (By similarity).
FT   MOD_RES     105    105       Phosphoserine (By similarity).
FT   MOD_RES     130    130       Phosphoserine (By similarity).
FT   MOD_RES     134    134       Phosphoserine (By similarity).
FT   MOD_RES     136    136       Phosphoserine (By similarity).
FT   MOD_RES     138    138       Phosphoserine (By similarity).
FT   MOD_RES     140    140       Phosphoserine (By similarity).
FT   MOD_RES     145    145       Phosphoserine.
FT   MOD_RES     172    172       N6-acetyllysine (By similarity).
FT   MOD_RES     177    177       N6-acetyllysine (By similarity).
SQ   SEQUENCE   181 AA;  20046 MW;  1A408EDCBB70DC44 CRC64;
     MSAARESHPH GVKRSASPDD DLGSSNWEAA DLGNEERKQK FLRLMGAGKK EHTGRLVIGD
     HKSTSHFRTG EEDKKINEEL ESQYQQSMDS KLSGRYRRHC GLGFSEVEDH DGEGDVAGDD
     DEDDSPDAES PDDSDSDSES EKEESAEELH AAEHPDDTED PKSKKDAKSN YKMMFVKSSG
     S
//
ID   DEST_MOUSE              Reviewed;         165 AA.
AC   Q9R0P5;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Destrin;
DE   AltName: Full=Actin-depolymerizing factor;
DE            Short=ADF;
DE   AltName: Full=Sid 23;
GN   Name=Dstn; Synonyms=Dsn, Sid23;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.;
RT   "Mouse actin depolymerizing factor sid23.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cecum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF 54-69 AND 133-145, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Actin-depolymerizing protein. Severs actin filaments (F-
CC       actin) and binds to actin monomers (G-actin). Acts in a pH-
CC       independent manner.
CC   -!- PTM: ISGylated (By similarity).
CC   -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC   -!- SIMILARITY: Contains 1 ADF-H domain.
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DR   EMBL; AB025406; BAA84691.1; -; mRNA.
DR   EMBL; AK078898; BAC37447.1; -; mRNA.
DR   IPI; IPI00127942; -.
DR   RefSeq; NP_062745.1; NM_019771.2.
DR   UniGene; Mm.28919; -.
DR   ProteinModelPortal; Q9R0P5; -.
DR   SMR; Q9R0P5; 2-165.
DR   STRING; Q9R0P5; -.
DR   PhosphoSite; Q9R0P5; -.
DR   REPRODUCTION-2DPAGE; IPI00127942; -.
DR   REPRODUCTION-2DPAGE; Q9R0P5; -.
DR   PRIDE; Q9R0P5; -.
DR   Ensembl; ENSMUST00000103172; ENSMUSP00000099461; ENSMUSG00000015932.
DR   GeneID; 56431; -.
DR   KEGG; mmu:56431; -.
DR   UCSC; uc008mqi.1; mouse.
DR   CTD; 56431; -.
DR   MGI; MGI:1929270; Dstn.
DR   GeneTree; ENSGT00440000033289; -.
DR   HOGENOM; HBG628477; -.
DR   HOVERGEN; HBG000381; -.
DR   InParanoid; Q9R0P5; -.
DR   OMA; QMLPEKD; -.
DR   OrthoDB; EOG4FR0SR; -.
DR   PhylomeDB; Q9R0P5; -.
DR   NextBio; 312606; -.
DR   ArrayExpress; Q9R0P5; -.
DR   Bgee; Q9R0P5; -.
DR   CleanEx; MM_DSTN; -.
DR   Genevestigator; Q9R0P5; -.
DR   GermOnline; ENSMUSG00000015932; Mus musculus.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0006928; P:cellular component movement; IMP:MGI.
DR   GO; GO:0000910; P:cytokinesis; IMP:MGI.
DR   GO; GO:0030836; P:positive regulation of actin filament depolymerization; IMP:MGI.
DR   InterPro; IPR002108; Actin-bd_cofilin/tropomyosin.
DR   InterPro; IPR017904; ADF/Cofilin/Destrin.
DR   Pfam; PF00241; Cofilin_ADF; 1.
DR   PRINTS; PR00006; COFILIN.
DR   SMART; SM00102; ADF; 1.
DR   PROSITE; PS51263; ADF_H; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Direct protein sequencing; Phosphoprotein;
KW   Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    165       Destrin.
FT                                /FTId=PRO_0000214919.
FT   DOMAIN        4    153       ADF-H.
FT   MOTIF        30     34       Nuclear localization signal (Potential).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       3      3       Phosphoserine.
FT   MOD_RES      19     19       N6-acetyllysine (By similarity).
FT   MOD_RES     114    114       N6-acetyllysine (By similarity).
SQ   SEQUENCE   165 AA;  18522 MW;  42BD07984C9B3667 CRC64;
     MASGVQVADE VCRIFYDMKV RKCSTPEEIK KRKKAVIFCL SADKKCIVVE EGKEILVGDV
     GATITDPFKH FVGMLPEKDC RYALYDASFE TKESRKEELM FFLWAPEQAP LKSKMIYASS
     KDAIKKKFPG IKHEYQANGP EDLNRTCIAE KLGGSLIVAF EGSPV
//
ID   UCHL1_MOUSE             Reviewed;         223 AA.
AC   Q9R0P9; Q9R122;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase isozyme L1;
DE            Short=UCH-L1;
DE            EC=3.4.19.12;
DE            EC=6.-.-.-;
DE   AltName: Full=Neuron cytoplasmic protein 9.5;
DE   AltName: Full=PGP 9.5;
DE            Short=PGP9.5;
DE   AltName: Full=Ubiquitin thioesterase L1;
GN   Name=Uchl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RC   TISSUE=Brain;
RX   MEDLINE=99400551; PubMed=10471497; DOI=10.1038/12647;
RA   Saigoh K., Wang Y.-L., Suh J.G., Yamanishi T., Sakai Y., Kiyosawa H.,
RA   Harada T., Ichihara N., Wakana S., Kikuchi T., Wada K.;
RT   "Intragenic deletion in the gene encoding ubiquitin carboxy-terminal
RT   hydrolase in gad mice.";
RL   Nat. Genet. 23:47-51(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-10, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Pituitary;
RX   MEDLINE=22448598; PubMed=12559414; DOI=10.1016/S0531-5565(02)00117-1;
RA   Marzban G., Grillari J., Reisinger E., Hemetsberger T., Grabherr R.,
RA   Katinger H.;
RT   "Age-related alterations in the protein expression profile of C57BL/6J
RT   mouse pituitaries.";
RL   Exp. Gerontol. 37:1451-1460(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 20-27; 66-78; 116-123; 136-153 AND 158-199, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [6]
RP   BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-30 AND CYS-90,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, AND DISRUPTION
RP   PHENOTYPE.
RX   MEDLINE=22793835; PubMed=12913066; DOI=10.1093/hmg/ddg211;
RA   Osaka H., Wang Y.-L., Takada K., Takizawa S., Setsuie R., Li H.,
RA   Sato Y., Nishikawa K., Sun Y.-J., Sakurai M., Harada T., Hara Y.,
RA   Kimura I., Chiba S., Namikawa K., Kiyama H., Noda M., Aoki S.,
RA   Wada K.;
RT   "Ubiquitin carboxy-terminal hydrolase L1 binds to and stabilizes
RT   monoubiquitin in neuron.";
RL   Hum. Mol. Genet. 12:1945-1958(2003).
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=14695319;
RA   Harada T., Harada C., Wang Y.-L., Osaka H., Amanai K., Tanaka K.,
RA   Takizawa S., Setsuie R., Sakurai M., Sato Y., Noda M., Wada K.;
RT   "Role of ubiquitin carboxy terminal hydrolase-L1 in neural cell
RT   apoptosis induced by ischemic retinal injury in vivo.";
RL   Am. J. Pathol. 164:59-64(2004).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=15911766; DOI=10.1073/pnas.0503239102;
RA   Lombardino A.J., Li X.-C., Hertel M., Nottebohm F.;
RT   "Replaceable neurons and neurodegenerative disease share depressed
RT   UCHL1 levels.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:8036-8041(2005).
CC   -!- FUNCTION: Ubiquitin-protein hydrolase involved both in the
CC       processing of ubiquitin precursors and of ubiquitinated proteins.
CC       This enzyme is a thiol protease that recognizes and hydrolyzes a
CC       peptide bond at the C-terminal glycine of ubiquitin. Also binds to
CC       free monoubiquitin and may prevent its degradation in lysosomes.
CC       The homodimer may have ATP-independent ubiquitin ligase activity.
CC   -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester,
CC       thioester, amide, peptide and isopeptide bonds formed by the C-
CC       terminal Gly of ubiquitin (a 76-residue protein attached to
CC       proteins as an intracellular targeting signal).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=116 nM for Ub-AMC;
CC   -!- SUBUNIT: Monomer. Homodimer. Interacts with COPS5 and SNCA (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, where it is found in
CC       neurons but not in oligodendrocytes or astrocytes. Found in the
CC       ganglion cell layer and the inner nuclear layer of the retina (at
CC       protein level). Expressed in brain and testis. In the brain,
CC       expression is at its lowest in replaceable neurons of hippocampus
CC       aand olfactory bulb. Highly expressed in senescent pituitary.
CC   -!- PTM: O-glycosylated (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice show sensory ataxia at an early stage,
CC       followed by motor ataxia at a later stage. They have reduced
CC       levels of monoubiquitin in the nervous system, and increased
CC       resistance to retinal ischemia.
CC   -!- MISCELLANEOUS: In contrast to UCHL3, does not hydrolyze a peptide
CC       bond at the C-terminal glycine of NEDD8 (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase C12 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AB025313; BAA84083.1; -; mRNA.
DR   EMBL; AF172334; AAD51029.1; -; mRNA.
DR   EMBL; AK013729; BAB28976.1; -; mRNA.
DR   EMBL; BC039177; AAH39177.1; -; mRNA.
DR   IPI; IPI00313962; -.
DR   RefSeq; NP_035800.2; NM_011670.2.
DR   UniGene; Mm.29807; -.
DR   ProteinModelPortal; Q9R0P9; -.
DR   SMR; Q9R0P9; 1-223.
DR   STRING; Q9R0P9; -.
DR   MEROPS; C12.001; -.
DR   PhosphoSite; Q9R0P9; -.
DR   REPRODUCTION-2DPAGE; IPI00313962; -.
DR   REPRODUCTION-2DPAGE; Q9R0P9; -.
DR   UCD-2DPAGE; Q9R0P9; -.
DR   PRIDE; Q9R0P9; -.
DR   Ensembl; ENSMUST00000031131; ENSMUSP00000031131; ENSMUSG00000029223.
DR   GeneID; 22223; -.
DR   KEGG; mmu:22223; -.
DR   UCSC; uc008xpf.1; mouse.
DR   CTD; 22223; -.
DR   MGI; MGI:103149; Uchl1.
DR   GeneTree; ENSGT00510000046640; -.
DR   HOVERGEN; HBG075483; -.
DR   InParanoid; Q9R0P9; -.
DR   OMA; ICRQFTE; -.
DR   OrthoDB; EOG4RJG2F; -.
DR   PhylomeDB; Q9R0P9; -.
DR   BRENDA; 3.4.19.12; 244.
DR   NextBio; 302243; -.
DR   ArrayExpress; Q9R0P9; -.
DR   Bgee; Q9R0P9; -.
DR   CleanEx; MM_UCHL1; -.
DR   Genevestigator; Q9R0P9; -.
DR   GermOnline; ENSMUSG00000029223; Mus musculus.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008242; F:omega peptidase activity; ISS:UniProtKB.
DR   GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR   GO; GO:0004221; F:ubiquitin thiolesterase activity; IDA:MGI.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0007412; P:axon target recognition; IMP:MGI.
DR   GO; GO:0019896; P:axon transport of mitochondrion; IMP:MGI.
DR   GO; GO:0008283; P:cell proliferation; IMP:MGI.
DR   GO; GO:0042755; P:eating behavior; IGI:MGI.
DR   GO; GO:0050905; P:neuromuscular process; IMP:MGI.
DR   GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR   GO; GO:0006950; P:response to stress; IMP:MGI.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR001578; Peptidase_C12.
DR   Gene3D; G3DSA:3.40.532.10; Peptidase_C12; 1.
DR   PANTHER; PTHR10589; Peptidase_C12; 1.
DR   Pfam; PF01088; Peptidase_C12; 1.
DR   PRINTS; PR00707; UBCTHYDRLASE.
DR   PROSITE; PS00140; UCH_1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Glycoprotein;
KW   Hydrolase; Ligase; Oxidation; Protease; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN         1    223       Ubiquitin carboxyl-terminal hydrolase
FT                                isozyme L1.
FT                                /FTId=PRO_0000211058.
FT   REGION        5     10       Interaction with ubiquitin (By
FT                                similarity).
FT   REGION      151    156       Interaction with ubiquitin (By
FT                                similarity).
FT   REGION      211    216       Interaction with ubiquitin (By
FT                                similarity).
FT   ACT_SITE     90     90       Nucleophile (Probable).
FT   ACT_SITE    161    161       Proton donor (By similarity).
FT   SITE          1      1       Susceptible to oxidation (By similarity).
FT   SITE          6      6       Susceptible to oxidation (By similarity).
FT   SITE         12     12       Susceptible to oxidation (By similarity).
FT   SITE        176    176       Important for enzyme activity (By
FT                                similarity).
FT   SITE        179    179       Susceptible to oxidation (By similarity).
FT   SITE        220    220       Susceptible to oxidation (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MUTAGEN      30     30       D->K: Abolishes enzymatic activity and
FT                                ubiquitin binding.
FT   MUTAGEN      90     90       C->S: Abolishes enzymatic activity, but
FT                                does not affect ubiquitin binding.
FT   CONFLICT    149    149       E -> K (in Ref. 2; AAD51029).
SQ   SEQUENCE   223 AA;  24838 MW;  F1402BF7B0C077EA CRC64;
     MQLKPMEINP EMLNKVLAKL GVAGQWRFAD VLGLEEETLG SVPSPACALL LLFPLTAQHE
     NFRKKQIEEL KGQEVSPKVY FMKQTIGNSC GTIGLIHAVA NNQDKLEFED GSVLKQFLSE
     TEKLSPEDRA KCFEKNEAIQ AAHDSVAQEG QCRVDDKVNF HFILFNNVDG HLYELDGRMP
     FPVNHGASSE DSLLQDAAKV CREFTEREQG EVRFSAVALC KAA
//
ID   TEBP_MOUSE              Reviewed;         160 AA.
AC   Q9R0Q7; Q542V4; Q9D7V0; Q9WV83;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 100.
DE   RecName: Full=Prostaglandin E synthase 3;
DE            EC=5.3.99.3;
DE   AltName: Full=Cytosolic prostaglandin E2 synthase;
DE            Short=cPGES;
DE   AltName: Full=Hsp90 co-chaperone;
DE   AltName: Full=Progesterone receptor complex p23;
DE   AltName: Full=Sid 3177;
DE   AltName: Full=Telomerase-binding protein p23;
GN   Name=Ptges3; Synonyms=Sid3177, Tebp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Kidney;
RX   MEDLINE=22925239; PubMed=14563409; DOI=10.1016/j.bbalip.2003.08.003;
RA   Zhang Y., Schneider A., Rao R., Lu W.J., Fan X., Davis L.,
RA   Breyer R.M., Breyer M.D., Guan Y.;
RT   "Genomic structure and genitourinary expression of mouse cytosolic
RT   prostaglandin E(2) synthase gene.";
RL   Biochim. Biophys. Acta 1634:15-23(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.;
RT   "Mouse p23 uniactive progesterone receptor complexes.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Cheong C., Lee H.-W.;
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and DBA/2; TISSUE=Liver, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 36-48.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [8]
RP   PHOSPHORYLATION AT SER-113.
RX   PubMed=15378723; DOI=10.1002/rcm.1604;
RA   Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R.;
RT   "Phosphoproteome analysis of mouse liver using immobilized metal
RT   affinity purification and linear ion trap mass spectrometry.";
RL   Rapid Commun. Mass Spectrom. 18:2169-2176(2004).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-148 AND
RP   SER-151, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Molecular chaperone that localizes to genomic response
CC       elements in a hormone-dependent manner and disrupts receptor-
CC       mediated transcriptional activation, by promoting disassembly of
CC       transcriptional regulatory complexes (By similarity).
CC   -!- CATALYTIC ACTIVITY: (5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15-
CC       hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-11-alpha,15-
CC       dihydroxy-9-oxoprosta-5,13-dienoate.
CC   -!- PATHWAY: Lipid metabolism; prostaglandin biosynthesis.
CC   -!- SUBUNIT: Binds to the progesterone receptor. Interacts with TERT;
CC       the interaction, together with HSP90A1, is required for correct
CC       assembly and stabilization of the telomerase holoenzyme complex
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in testis, kidney, bladder and
CC       ovary.
CC   -!- SIMILARITY: Belongs to the p23/wos2 family.
CC   -!- SIMILARITY: Contains 1 CS domain.
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DR   EMBL; AY281130; AAP34198.1; -; mRNA.
DR   EMBL; AB024935; BAA84684.1; -; mRNA.
DR   EMBL; AF153479; AAD39543.1; -; mRNA.
DR   EMBL; AK008805; BAB25906.1; -; mRNA.
DR   EMBL; AK075932; BAC36062.1; -; mRNA.
DR   EMBL; AK075987; BAC36099.1; -; mRNA.
DR   EMBL; AK077538; BAC36854.1; -; mRNA.
DR   EMBL; AK168073; BAE40047.1; -; mRNA.
DR   EMBL; AK168210; BAE40169.1; -; mRNA.
DR   EMBL; AK168721; BAE40563.1; -; mRNA.
DR   EMBL; BC003708; AAH03708.1; -; mRNA.
DR   EMBL; BC085264; AAH85264.1; -; mRNA.
DR   IPI; IPI00127989; -.
DR   RefSeq; NP_062740.1; NM_019766.4.
DR   RefSeq; XP_001478909.1; XM_001478859.2.
DR   RefSeq; XP_001480119.1; XM_001480069.2.
DR   UniGene; Mm.22421; -.
DR   UniGene; Mm.305816; -.
DR   ProteinModelPortal; Q9R0Q7; -.
DR   SMR; Q9R0Q7; 1-110.
DR   STRING; Q9R0Q7; -.
DR   PhosphoSite; Q9R0Q7; -.
DR   PRIDE; Q9R0Q7; -.
DR   Ensembl; ENSMUST00000052798; ENSMUSP00000050292; ENSMUSG00000071072.
DR   GeneID; 100043508; -.
DR   GeneID; 100048119; -.
DR   GeneID; 56351; -.
DR   KEGG; mmu:100043508; -.
DR   KEGG; mmu:100048119; -.
DR   KEGG; mmu:56351; -.
DR   UCSC; uc007hld.1; mouse.
DR   CTD; 56351; -.
DR   MGI; MGI:1929282; Ptges3.
DR   GeneTree; ENSGT00510000046493; -.
DR   HOGENOM; HBG749677; -.
DR   HOVERGEN; HBG002143; -.
DR   InParanoid; Q9R0Q7; -.
DR   OMA; YLRKAQP; -.
DR   OrthoDB; EOG48WC3C; -.
DR   PhylomeDB; Q9R0Q7; -.
DR   BRENDA; 5.3.99.3; 244.
DR   NextBio; 456456; -.
DR   ArrayExpress; Q9R0Q7; -.
DR   Bgee; Q9R0Q7; -.
DR   CleanEx; MM_PTGES3; -.
DR   Genevestigator; Q9R0Q7; -.
DR   GermOnline; ENSMUSG00000040078; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0050220; F:prostaglandin-E synthase activity; ISS:UniProtKB.
DR   GO; GO:0051082; F:unfolded protein binding; ISS:UniProtKB.
DR   GO; GO:0001516; P:prostaglandin biosynthetic process; ISS:UniProtKB.
DR   InterPro; IPR007052; CS-like_domain.
DR   InterPro; IPR017447; CS_domain.
DR   InterPro; IPR008978; HSP20-like_chaperone.
DR   Pfam; PF04969; CS; 1.
DR   SUPFAM; SSF49764; HSP20_chap; 1.
DR   PROSITE; PS51203; CS; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing;
KW   Fatty acid biosynthesis; Isomerase; Lipid synthesis; Phosphoprotein;
KW   Prostaglandin biosynthesis.
FT   CHAIN         1    160       Prostaglandin E synthase 3.
FT                                /FTId=PRO_0000218953.
FT   DOMAIN        1     90       CS.
FT   COMPBIAS    108    160       Asp/Glu-rich.
FT   MOD_RES       7      7       N6-acetyllysine (By similarity).
FT   MOD_RES      33     33       N6-acetyllysine (By similarity).
FT   MOD_RES     113    113       Phosphoserine.
FT   MOD_RES     118    118       Phosphoserine (By similarity).
FT   MOD_RES     148    148       Phosphoserine.
FT   MOD_RES     151    151       Phosphoserine.
FT   CONFLICT     87     88       PR -> LG (in Ref. 3; AAD39543).
FT   CONFLICT    108    108       D -> N (in Ref. 1; AAP34198 and 4;
FT                                BAB25906).
SQ   SEQUENCE   160 AA;  18721 MW;  7702CB59D7AFD739 CRC64;
     MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL NEIDLFHCID
     PNDSKHKRTD RSILCCLRKG ESGQSWPRLT KERAKLNWLS VDFNNWKDWE DDSDEDMSNF
     DRFSEMMDHM GGDEDVDLPE VDGADDDSQD SDDEKMPDLE
//
ID   SRS10_MOUSE             Reviewed;         262 AA.
AC   Q9R0U0; B1AV44; B1AV45; O70307; O88468; Q3TGW7; Q8CFZ1; Q9R0T9;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2004, sequence version 2.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Serine/arginine-rich splicing factor 10;
DE   AltName: Full=FUS-interacting serine-arginine-rich protein 1;
DE   AltName: Full=Neural-salient serine/arginine-rich protein;
DE   AltName: Full=Neural-specific SR protein;
DE   AltName: Full=Splicing factor, arginine/serine-rich 13A;
DE   AltName: Full=TLS-associated protein with Ser-Arg repeats;
DE            Short=TASR;
DE            Short=TLS-associated protein with SR repeats;
DE   AltName: Full=TLS-associated serine-arginine protein;
DE            Short=TLS-associated SR protein;
GN   Name=Srsf10; Synonyms=Fusip1, Nssr, Sfrs13a, Srsf13a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX   MEDLINE=98447613; PubMed=9774382; DOI=10.1074/jbc.273.43.27761;
RA   Yang L., Embree L.J., Tsai S., Hickstein D.D.;
RT   "Oncoprotein TLS interacts with serine-arginine proteins involved in
RT   RNA splicing.";
RL   J. Biol. Chem. 273:27761-27764(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RX   MEDLINE=20051033; PubMed=10583508;
RX   DOI=10.1046/j.1365-2443.1999.00286.x;
RA   Komatsu M., Kominami E., Arahata K., Tsukahara T.;
RT   "Cloning and characterization of two neural-salient serine/arginine-
RT   rich (NSSR) proteins involved in the regulation of alternative
RT   splicing in neurones.";
RL   Genes Cells 4:593-606(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=20242028; PubMed=10779324;
RX   DOI=10.1128/MCB.20.10.3345-3354.2000;
RA   Yang L., Embree L.J., Hickstein D.D.;
RT   "TLS-ERG leukemia fusion protein inhibits RNA splicing mediated by
RT   serine-arginine proteins.";
RL   Mol. Cell. Biol. 20:3345-3354(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Amnion, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and FVB/N-3; TISSUE=Brain, and Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, PHOSPHORYLATION
RP   [LARGE SCALE ANALYSIS] AT SER-168 (ISOFORM 3), AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119; SER-121; SER-131;
RP   SER-133; SER-158 AND SER-160, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Splicing factor that in its dephosphorylated form acts
CC       as a general repressor of pre-mRNA splicing. Seems to interfere
CC       with the U1 snRNP 5'-splice recognition of SNRNP70. Required for
CC       splicing repression in M-phase cells and after heat shock (By
CC       similarity). May be involved in regulation of alternative splicing
CC       in neurons, with isoform 1 acting as a positive and isoform 3 as a
CC       negative regulator.
CC   -!- SUBUNIT: The phosphorylated but not the dephosphorylated form
CC       interacts with TRA2B/SFRS10. The dephosphorylated form interacts
CC       with SNRNP70. Isoform 1 and isoform 3 interact with FUS C-terminus
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus speckle.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=TASR-1, NSSR1;
CC         IsoId=Q9R0U0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9R0U0-2; Sequence=VSP_010426;
CC       Name=3; Synonyms=TASR-2, NSSR2;
CC         IsoId=Q9R0U0-3; Sequence=VSP_010427, VSP_010428;
CC         Note=Phosphorylated on Ser-168;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with high levels in brain
CC       and testis.
CC   -!- PTM: Isoform 3 is phosphorylated on Ser-168.
CC   -!- SIMILARITY: Belongs to the splicing factor SR family.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR   EMBL; AF042383; AAC70916.1; -; mRNA.
DR   EMBL; AB015894; BAA35092.1; -; mRNA.
DR   EMBL; AB015895; BAA35093.1; -; mRNA.
DR   EMBL; AF060490; AAC26715.1; -; mRNA.
DR   EMBL; AK014345; BAB29286.1; -; mRNA.
DR   EMBL; AK168524; BAE40403.1; -; mRNA.
DR   EMBL; AK168558; BAE40431.1; -; mRNA.
DR   EMBL; AL672076; CAM15892.1; -; Genomic_DNA.
DR   EMBL; AL672076; CAM15893.1; -; Genomic_DNA.
DR   EMBL; BC037591; AAH37591.1; -; mRNA.
DR   EMBL; BC043060; AAH43060.1; -; mRNA.
DR   EMBL; BC083082; AAH83082.1; -; mRNA.
DR   IPI; IPI00117232; -.
DR   IPI; IPI00314984; -.
DR   IPI; IPI00473196; -.
DR   RefSeq; NP_001073856.1; NM_001080387.1.
DR   RefSeq; NP_034308.1; NM_010178.2.
DR   UniGene; Mm.10229; -.
DR   UniGene; Mm.472035; -.
DR   ProteinModelPortal; Q9R0U0; -.
DR   SMR; Q9R0U0; 4-91.
DR   STRING; Q9R0U0; -.
DR   PhosphoSite; Q9R0U0; -.
DR   PRIDE; Q9R0U0; -.
DR   Ensembl; ENSMUST00000105853; ENSMUSP00000101479; ENSMUSG00000028676.
DR   GeneID; 14105; -.
DR   KEGG; mmu:14105; -.
DR   UCSC; uc008vhd.1; mouse.
DR   CTD; 14105; -.
DR   MGI; MGI:1333805; Srsf10.
DR   eggNOG; roNOG16493; -.
DR   GeneTree; ENSGT00560000076881; -.
DR   HOVERGEN; HBG107480; -.
DR   InParanoid; Q9R0U0; -.
DR   OrthoDB; EOG4HMJBR; -.
DR   NextBio; 285142; -.
DR   ArrayExpress; Q9R0U0; -.
DR   Bgee; Q9R0U0; -.
DR   CleanEx; MM_FUSIP1; -.
DR   Genevestigator; Q9R0U0; -.
DR   GermOnline; ENSMUSG00000028676; Mus musculus.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; NAS:UniProtKB.
DR   GO; GO:0051082; F:unfolded protein binding; NAS:UniProtKB.
DR   GO; GO:0016482; P:cytoplasmic transport; IDA:UniProtKB.
DR   GO; GO:0006406; P:mRNA export from nucleus; NAS:UniProtKB.
DR   GO; GO:0006376; P:mRNA splice site selection; ISS:UniProtKB.
DR   GO; GO:0048025; P:negative regulation of nuclear mRNA splicing, via spliceosome; IDA:UniProtKB.
DR   GO; GO:0045449; P:regulation of transcription; NAS:UniProtKB.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; mRNA processing; mRNA splicing; Nucleus;
KW   Phosphoprotein; RNA-binding.
FT   CHAIN         1    262       Serine/arginine-rich splicing factor 10.
FT                                /FTId=PRO_0000081594.
FT   DOMAIN       10     88       RRM.
FT   COMPBIAS    106    260       Arg/Ser-rich (RS domain).
FT   MOD_RES     110    110       Phosphotyrosine (By similarity).
FT   MOD_RES     119    119       Phosphoserine.
FT   MOD_RES     121    121       Phosphoserine.
FT   MOD_RES     129    129       Phosphoserine (By similarity).
FT   MOD_RES     131    131       Phosphoserine.
FT   MOD_RES     133    133       Phosphoserine.
FT   MOD_RES     156    156       Phosphoserine (By similarity).
FT   MOD_RES     158    158       Phosphoserine.
FT   MOD_RES     160    160       Phosphoserine.
FT   MOD_RES     235    235       Phosphoserine (By similarity).
FT   MOD_RES     251    251       Phosphoserine (By similarity).
FT   MOD_RES     253    253       Phosphoserine (By similarity).
FT   MOD_RES     255    255       Phosphothreonine (By similarity).
FT   MOD_RES     256    256       Phosphoserine (By similarity).
FT   VAR_SEQ     147    147       Missing (in isoform 2).
FT                                /FTId=VSP_010426.
FT   VAR_SEQ     165    183       FKHRNRSFSRSKSNSRSRS -> PNCSWNTQYSSAYYTSRK
FT                                I (in isoform 3).
FT                                /FTId=VSP_010427.
FT   VAR_SEQ     184    262       Missing (in isoform 3).
FT                                /FTId=VSP_010428.
FT   CONFLICT     22     22       R -> Q (in Ref. 6; AAH37591).
FT   CONFLICT    154    154       R -> T (in Ref. 2; BAA35092/BAA35093).
SQ   SEQUENCE   262 AA;  31301 MW;  205F95D36CBBFAB4 CRC64;
     MSRYLRPPNT SLFVRNVADD TRSEDLRREF GRYGPIVDVY VPLDFYTRRP RGFAYVQFED
     VRDAEDALHN LDRKWICGRQ IEIQFAQGDR KTPNQMKAKE GRNVYSSSRY DDYDRYRRSR
     SRSYERRRSR SRSFDYNYRR SYSPRNSRPT GRPRRSRSHS DNDRFKHRNR SFSRSKSNSR
     SRSKSQPKKE MKAKSRSRSA SHTKTRGTSK TDSKTHYKSG SRYEKESRKK EPPRSKSQSR
     SQSRSRSKSR SRSWTSPKSS GH
//
ID   RPGR_MOUSE              Reviewed;        1001 AA.
AC   Q9R0X5; O88408; Q9CU92;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=X-linked retinitis pigmentosa GTPase regulator;
DE            Short=mRpgr;
GN   Name=Rpgr;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND ISOPRENYLATION.
RC   TISSUE=Brain;
RX   MEDLINE=98344060; PubMed=9677393; DOI=10.1074/jbc.273.31.19656;
RA   Yan D., Swain P.K., Breuer D., Tucker R.M., Wu W., Fujita R.,
RA   Rehemtulla A., Burke D., Swaroop A.;
RT   "Biochemical characterization and subcellular localization of the
RT   mouse retinitis pigmentosa GTPase regulator.";
RL   J. Biol. Chem. 273:19656-19663(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   MEDLINE=99330567; PubMed=10401007; DOI=10.1093/hmg/8.8.1571;
RA   Kirschner R., Rosenberg T., Schultz-Heienbrok R., Lenzner S., Feil S.,
RA   Roepman R., Cremers F.P.M., Ropers H.-H., Berger W.;
RT   "RPGR transcription studies in mouse and human tissues reveal a
RT   retina-specific isoform that is disrupted in a patient with X-linked
RT   retinitis pigmentosa.";
RL   Hum. Mol. Genet. 8:1571-1578(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
RP   1).
RC   STRAIN=129/SvEvTacfBr;
RX   MEDLINE=21558421; PubMed=11702207; DOI=10.1007/s004390100572;
RA   Kirschner R., Erturk D., Zeitz C., Sahin S., Ramser J.,
RA   Cremers F.P.M., Ropers H.-H., Berger W.;
RT   "DNA sequence comparison of human and mouse retinitis pigmentosa
RT   GTPase regulator (RPGR) identifies tissue-specific exons and putative
RT   regulatory elements.";
RL   Hum. Genet. 109:271-278(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-845 (ISOFORMS 2/3).
RC   STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   INTERACTION WITH PDE6D.
RX   PubMed=9990021;
RA   Linari M., Ueffing M., Manson F., Wright A., Meitinger T., Becker J.;
RT   "The retinitis pigmentosa GTPase regulator, RPGR, interacts with the
RT   delta subunit of rod cyclic GMP phosphodiesterase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:1315-1320(1999).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=12140192; DOI=10.1093/hmg/11.16.1899;
RA   Mavlyutov T.A., Zhao H., Ferreira P.A.;
RT   "Species-specific subcellular localization of RPGR and RPGRIP
RT   isoforms: implications for the phenotypic variability of congenital
RT   retinopathies among species.";
RL   Hum. Mol. Genet. 11:1899-1907(2002).
CC   -!- FUNCTION: Could be a guanine-nucleotide releasing factor (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with RPGRIP1 (By similarity). Interacts with
CC       PDE6D.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1;
CC         IsoId=Q9R0X5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9R0X5-2; Sequence=VSP_005552;
CC       Name=3;
CC         IsoId=Q9R0X5-3; Sequence=VSP_005552, VSP_005553;
CC       Name=4;
CC         IsoId=Q9R0X5-4; Sequence=VSP_005551, VSP_005552, VSP_005554,
CC                                  VSP_005555;
CC   -!- TISSUE SPECIFICITY: Widely expressed with highest levels in brain
CC       and testis and low levels in eye. Colocalizes with RPGRIP1 in the
CC       photoreceptor connecting cilium, a thin bridge linking the cell
CC       body and the light-sensing outer segment.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout embryonic development
CC       from day 7 of gestation. Also expressed in adult.
CC   -!- PTM: Prenylated.
CC   -!- SIMILARITY: Contains 6 RCC1 repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC40190.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
CC       Sequence=BAB30628.3; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; AF044677; AAC40190.1; ALT_INIT; mRNA.
DR   EMBL; AJ238396; CAB54041.1; -; mRNA.
DR   EMBL; AJ318464; CAC86115.1; -; Genomic_DNA.
DR   EMBL; AK017192; BAB30628.3; ALT_INIT; mRNA.
DR   IPI; IPI00122416; -.
DR   IPI; IPI00128188; -.
DR   IPI; IPI00230648; -.
DR   IPI; IPI00230650; -.
DR   RefSeq; NP_035415.1; NM_011285.2.
DR   UniGene; Mm.247556; -.
DR   ProteinModelPortal; Q9R0X5; -.
DR   SMR; Q9R0X5; 8-366.
DR   DIP; DIP-46319N; -.
DR   STRING; Q9R0X5; -.
DR   PhosphoSite; Q9R0X5; -.
DR   PRIDE; Q9R0X5; -.
DR   Ensembl; ENSMUST00000044598; ENSMUSP00000037358; ENSMUSG00000031174.
DR   Ensembl; ENSMUST00000073392; ENSMUSP00000073106; ENSMUSG00000031174.
DR   Ensembl; ENSMUST00000115536; ENSMUSP00000111198; ENSMUSG00000031174.
DR   GeneID; 19893; -.
DR   KEGG; mmu:19893; -.
DR   UCSC; uc009sqg.1; mouse.
DR   CTD; 19893; -.
DR   MGI; MGI:1344037; Rpgr.
DR   GeneTree; ENSGT00590000082902; -.
DR   HOVERGEN; HBG026899; -.
DR   InParanoid; Q9R0X5; -.
DR   PhylomeDB; Q9R0X5; -.
DR   NextBio; 297416; -.
DR   ArrayExpress; Q9R0X5; -.
DR   Bgee; Q9R0X5; -.
DR   CleanEx; MM_RPGR; -.
DR   Genevestigator; Q9R0X5; -.
DR   GermOnline; ENSMUSG00000031174; Mus musculus.
DR   GO; GO:0005929; C:cilium; IDA:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0042462; P:eye photoreceptor cell development; IMP:MGI.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; ISS:UniProtKB.
DR   InterPro; IPR000408; Reg_chr_condens.
DR   InterPro; IPR009091; Reg_csome_cond/b-lactamase_inh.
DR   Gene3D; G3DSA:2.130.10.30; Reg_csome_cond/b-lactamase_inh; 1.
DR   Pfam; PF00415; RCC1; 6.
DR   PRINTS; PR00633; RCCNDNSATION.
DR   SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR   PROSITE; PS00625; RCC1_1; FALSE_NEG.
DR   PROSITE; PS00626; RCC1_2; 3.
DR   PROSITE; PS50012; RCC1_3; 6.
PE   1: Evidence at protein level;
KW   Alternative splicing; Golgi apparatus;
KW   Guanine-nucleotide releasing factor; Lipoprotein; Methylation;
KW   Phosphoprotein; Prenylation; Repeat; Sensory transduction; Vision.
FT   CHAIN         1    998       X-linked retinitis pigmentosa GTPase
FT                                regulator.
FT                                /FTId=PRO_0000206639.
FT   PROPEP      999   1001       Removed in mature form (Potential).
FT                                /FTId=PRO_0000370845.
FT   REPEAT       54    105       RCC1 1.
FT   REPEAT      106    158       RCC1 2.
FT   REPEAT      159    208       RCC1 3.
FT   REPEAT      209    261       RCC1 4.
FT   REPEAT      262    313       RCC1 5.
FT   REPEAT      314    367       RCC1 6.
FT   COMPBIAS    530    885       Glu-rich.
FT   MOD_RES     544    544       Phosphoserine (By similarity).
FT   MOD_RES     998    998       Cysteine methyl ester (Potential).
FT   LIPID       998    998       S-geranylgeranyl cysteine (Probable).
FT   VAR_SEQ     260    469       Missing (in isoform 4).
FT                                /FTId=VSP_005551.
FT   VAR_SEQ     525    817       Missing (in isoform 2, isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_005552.
FT   VAR_SEQ     904    943       Missing (in isoform 3).
FT                                /FTId=VSP_005553.
FT   VAR_SEQ     904    907       GHMY -> DFLL (in isoform 4).
FT                                /FTId=VSP_005554.
FT   VAR_SEQ     908   1001       Missing (in isoform 4).
FT                                /FTId=VSP_005555.
FT   CONFLICT    226    226       N -> S (in Ref. 3; CAC86115).
FT   CONFLICT    606    606       R -> K (in Ref. 3; CAC86115).
FT   CONFLICT    697    697       N -> S (in Ref. 3; CAC86115).
SQ   SEQUENCE   1001 AA;  111856 MW;  DE145FBFEA0F8759 CRC64;
     MAESESLVPD TGAVFTFGKT KFAENIPSKF WFKNDIPICL SCGDEHTAIV TGNNKLYMFG
     SNNWGQLGLG SKAAIIKPTC IKALKPEKVK LAACGRNHTL VSTDTGGVYA AGGNNEGQLG
     LGDTDDRDTF HQIVFFTPAD TIKQLSAGAN TSAALTEDGK LFMWGDNSEG QIGLEDKSNV
     CIPHEVTVGK PISWISCGYY HSAFVTMDGE LYTFGEPENG KLGLPNELLM NHRSPQRVLG
     IPERVIQVAC GGGHTVVLTE KVVYAFGLGQ FGQLGLGTFL FETSEPKIIE RIKDQKICHI
     SCGENHTALM TELGLLYTFG DGRHGKLGLG MENFTNQFFP TLCSNFLRFA VQLIACGGCH
     MLVFATPRLG TIDEPKFEDV YEPYISTGSF SINDLSPRSS LNRSLSARLR RRERERPPCS
     ASMVGTLPPL EGTSASTSAY FYPSSPPFHL SVNNYPEKSP SESMEPLDSD YFEDKMNKDT
     ETENSSAVDS ENFGETNDIL NMTHMMTTSS NEKLLDFSPI QKQQNQDTFE KVMESTPCTE
     NEDSYEYEEM SKIKEVTVYK QYLAKGIYMI RPAEILEAFS DEEVGNGLDQ VEEPRVFTDG
     KGLQSRQVGK ESDEEIVSEK KTEVMEVADV KKIRESEENS KSDSLFDDLP DKTMNSESED
     NKDIAEERRS SEQNMTFDSE TELVEEPDSY MECERHNEQD SAEELEQPKL VEYSSEEKDE
     KDEKDDDEVE TENLWYDRNC TEQETENVFR ATRFFPKFDL KHDHLSGIPE EQEGPEDSEG
     NVVVEQVVQA QKENLEFEGD RKEAKAEAPS DVITEKEAPQ LSETVKPEEG EMDEEISILN
     VEDTVEEERK EGEKEIVEEG SIPETEGSET IDITDEKLDE VLKEEDSASL LQRALREYNE
     NPKGHMYDRV KSSSSEILGG NDPTSKDIKK AKKISFFNRM SLTGQKLMQN TNDPLPEIKP
     IGDQIALQSD KKDANQNHMG QNLQDSTTPN MEGKSKSCTI L
//
ID   KAD1_MOUSE              Reviewed;         194 AA.
AC   Q9R0Y5; A2AK80; Q542C5; Q9R0Y4;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Adenylate kinase isoenzyme 1;
DE            Short=AK 1;
DE            EC=2.7.4.3;
DE   AltName: Full=ATP-AMP transphosphorylase 1;
DE   AltName: Full=Myokinase;
GN   Name=Ak1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX   MEDLINE=20027374; PubMed=10557075; DOI=10.1038/sj.onc.1202970;
RA   Collavin L., Lazarevic D., Utrera R., Marzinotto S., Monte M.,
RA   Schneider C.;
RT   "wt p53 dependent expression of a membrane-associated isoform of
RT   adenylate kinase.";
RL   Oncogene 18:5879-5888(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=CD-1;
RX   PubMed=16790685; DOI=10.1095/biolreprod.106.053512;
RA   Cao W., Haig-Ladewig L., Gerton G.L., Moss S.B.;
RT   "Adenylate kinases 1 and 2 are part of the accessory structures in the
RT   mouse sperm flagellum.";
RL   Biol. Reprod. 75:492-500(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Adipose tissue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Mammary tumor, and Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 32-44; 64-77; 84-97 AND 150-166, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the reversible transfer of the terminal
CC       phosphate group between ATP and AMP. Small ubiquitous enzyme
CC       involved in energy metabolism and nucleotide synthesis that is
CC       essential for maintenance and cell growth (By similarity). May
CC       provide a mechanism to buffer the adenylate energy charge for
CC       sperm motility.
CC   -!- CATALYTIC ACTIVITY: ATP + AMP = 2 ADP.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Ak1a;
CC         IsoId=Q9R0Y5-1; Sequence=Displayed;
CC       Name=2; Synonyms=Ak1b;
CC         IsoId=Q9R0Y5-2; Sequence=VSP_024843;
CC   -!- DEVELOPMENTAL STAGE: Up-regulated during late spermiogenesis, when
CC       the flagellum is being assembled.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM16612.1; Type=Erroneous gene model prediction;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ010108; CAB52407.1; -; mRNA.
DR   EMBL; AJ010109; CAB52408.1; -; mRNA.
DR   EMBL; DQ486026; ABF46940.1; -; mRNA.
DR   EMBL; AK046613; BAC32808.1; -; mRNA.
DR   EMBL; AK089270; BAC40822.1; -; mRNA.
DR   EMBL; AL772271; CAM16612.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL772271; CAM16613.1; -; Genomic_DNA.
DR   EMBL; AL772271; CAM16614.1; -; Genomic_DNA.
DR   EMBL; BC014802; AAH14802.1; -; mRNA.
DR   EMBL; BC054366; AAH54366.1; -; mRNA.
DR   IPI; IPI00128209; -.
DR   IPI; IPI00750256; -.
DR   RefSeq; NP_001185719.1; NM_001198790.1.
DR   RefSeq; NP_001185720.1; NM_001198791.1.
DR   RefSeq; NP_001185721.1; NM_001198792.1.
DR   RefSeq; NP_067490.1; NM_021515.3.
DR   UniGene; Mm.480325; -.
DR   ProteinModelPortal; Q9R0Y5; -.
DR   SMR; Q9R0Y5; 1-194.
DR   STRING; Q9R0Y5; -.
DR   REPRODUCTION-2DPAGE; IPI00128209; -.
DR   REPRODUCTION-2DPAGE; Q9R0Y5; -.
DR   PRIDE; Q9R0Y5; -.
DR   Ensembl; ENSMUST00000068271; ENSMUSP00000068479; ENSMUSG00000026817.
DR   Ensembl; ENSMUST00000113277; ENSMUSP00000108902; ENSMUSG00000026817.
DR   Ensembl; ENSMUST00000113278; ENSMUSP00000108903; ENSMUSG00000026817.
DR   GeneID; 11636; -.
DR   KEGG; mmu:11636; -.
DR   NMPDR; fig|10090.3.peg.5814; -.
DR   UCSC; uc008jgh.1; mouse.
DR   CTD; 11636; -.
DR   MGI; MGI:87977; Ak1.
DR   eggNOG; roNOG17573; -.
DR   GeneTree; ENSGT00390000016215; -.
DR   HOVERGEN; HBG108060; -.
DR   OMA; IRHIMES; -.
DR   OrthoDB; EOG402WT6; -.
DR   BRENDA; 2.7.4.3; 244.
DR   ArrayExpress; Q9R0Y5; -.
DR   Bgee; Q9R0Y5; -.
DR   CleanEx; MM_AK1; -.
DR   Genevestigator; Q9R0Y5; -.
DR   GermOnline; ENSMUSG00000026817; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0004017; F:adenylate kinase activity; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
DR   GO; GO:0007050; P:cell cycle arrest; IDA:MGI.
DR   InterPro; IPR000850; Adenylate_kin.
DR   InterPro; IPR006267; Adenylate_kin1.
DR   PANTHER; PTHR23359; Adenylate_kin; 1.
DR   Pfam; PF00406; ADK; 1.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   TIGRFAMs; TIGR01360; aden_kin_iso1; 1.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW   Direct protein sequencing; Kinase; Nucleotide-binding; Transferase.
FT   CHAIN         1    194       Adenylate kinase isoenzyme 1.
FT                                /FTId=PRO_0000158911.
FT   NP_BIND      15     23       ATP (By similarity).
FT   NP_BIND      94    101       AMP (By similarity).
FT   BINDING      39     39       AMP (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   VAR_SEQ       1      2       ME -> MGCCVSSEPQEEGGRKTG (in isoform 2).
FT                                /FTId=VSP_024843.
SQ   SEQUENCE   194 AA;  21540 MW;  88E7862522967D14 CRC64;
     MEEKLKKAKI IFVVGGPGSG KGTQCEKIVQ KYGYTHLSTG DLLRAEVSSG SERGKKLSAI
     MEKGELVPLD TVLDMLRDAM LAKVDSSNGF LIDGYPREVK QGEEFEQKIG QPTLLLYVDA
     GAETMTQRLL KRGETSGRVD DNEETIKKRL ETYYNATEPV ISFYDKRGIV RKVNAEGTVD
     TVFSEVCTYL DSLK
//
ID   RHG07_MOUSE             Reviewed;        1092 AA.
AC   Q9R0Z9; Q3TRX3; Q3UH75; Q8R541;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2002, sequence version 2.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Rho GTPase-activating protein 7;
DE   AltName: Full=Deleted in liver cancer 1 protein homolog;
DE            Short=DLC-1;
DE   AltName: Full=Rho-type GTPase-activating protein 7;
DE   AltName: Full=START domain-containing protein 12;
DE            Short=StARD12;
DE   AltName: Full=StAR-related lipid transfer protein 12;
GN   Name=Dlc1; Synonyms=Arhgap7, Stard12;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=129/Sv;
RX   MEDLINE=20169180; PubMed=10702663;
RA   Yuan B.-Z., Keck-Waggoner C.L., Zimonjic D.B., Thorgeirsson S.S.,
RA   Popescu N.C.;
RT   "Assignment and cloning of mouse Arhgap7 to chromosome 8A4-B2, a
RT   conserved syntenic region of human chromosome 8p22-p21.";
RL   Cytogenet. Cell Genet. 87:189-190(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC   STRAIN=129/Sv;
RX   MEDLINE=22030460; PubMed=12034501; DOI=10.1016/S0378-1119(02)00462-6;
RA   Durkin M.E., Yuan B.-Z., Thorgeirsson S.S., Popescu N.C.;
RT   "Gene structure, tissue expression, and linkage mapping of the mouse
RT   DLC-1 gene (Arhgap7).";
RL   Gene 288:119-127(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-1064 (ISOFORM 1).
RC   STRAIN=C57BL/6, and C57BL/6J; TISSUE=Brain, and Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-89, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; SER-89 AND SER-414,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Functions as a GTPase-activating protein specific for
CC       Rho and an activator of PLCD1 in vivo and induces morphological
CC       changes and detachment through cytoskeletal reorganization (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9R0Z9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9R0Z9-2; Sequence=VSP_026144;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Widely expressed with the highest levels in
CC       heart, liver and lung.
CC   -!- SIMILARITY: Contains 1 Rho-GAP domain.
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
CC   -!- SIMILARITY: Contains 1 START domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL87620.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF178078; AAD51760.1; -; mRNA.
DR   EMBL; AF411442; AAL87620.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AF411435; AAL87620.1; JOINED; Genomic_DNA.
DR   EMBL; AF411436; AAL87620.1; JOINED; Genomic_DNA.
DR   EMBL; AF411437; AAL87620.1; JOINED; Genomic_DNA.
DR   EMBL; AF411438; AAL87620.1; JOINED; Genomic_DNA.
DR   EMBL; AF411439; AAL87620.1; JOINED; Genomic_DNA.
DR   EMBL; AF411440; AAL87620.1; JOINED; Genomic_DNA.
DR   EMBL; AF411441; AAL87620.1; JOINED; Genomic_DNA.
DR   EMBL; AK147539; BAE27982.1; -; mRNA.
DR   EMBL; AK162413; BAE36903.1; -; mRNA.
DR   IPI; IPI00314102; -.
DR   IPI; IPI00761452; -.
DR   RefSeq; NP_001181869.1; NM_001194940.1.
DR   RefSeq; NP_001181870.1; NM_001194941.1.
DR   RefSeq; NP_056617.2; NM_015802.3.
DR   UniGene; Mm.210875; -.
DR   ProteinModelPortal; Q9R0Z9; -.
DR   SMR; Q9R0Z9; 1-76, 634-843, 888-1079.
DR   STRING; Q9R0Z9; -.
DR   PhosphoSite; Q9R0Z9; -.
DR   PRIDE; Q9R0Z9; -.
DR   Ensembl; ENSMUST00000033923; ENSMUSP00000033923; ENSMUSG00000031523.
DR   Ensembl; ENSMUST00000098826; ENSMUSP00000096425; ENSMUSG00000031523.
DR   GeneID; 50768; -.
DR   KEGG; mmu:50768; -.
DR   CTD; 50768; -.
DR   MGI; MGI:1354949; Dlc1.
DR   eggNOG; roNOG11056; -.
DR   GeneTree; ENSGT00600000084127; -.
DR   HOVERGEN; HBG055955; -.
DR   OrthoDB; EOG4P2Q1D; -.
DR   NextBio; 307679; -.
DR   ArrayExpress; Q9R0Z9; -.
DR   Bgee; Q9R0Z9; -.
DR   CleanEx; MM_DLC1; -.
DR   Genevestigator; Q9R0Z9; -.
DR   GermOnline; ENSMUSG00000031523; Mus musculus.
DR   GO; GO:0005100; F:Rho GTPase activator activity; NAS:UniProtKB.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IMP:MGI.
DR   GO; GO:0048041; P:focal adhesion assembly; IMP:MGI.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR   GO; GO:0021575; P:hindbrain morphogenesis; IMP:MGI.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
DR   GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR011510; SAM_2.
DR   InterPro; IPR002913; START_lipid-bd.
DR   Gene3D; G3DSA:1.10.555.10; RhoGAP; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   Pfam; PF01852; START; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SMART; SM00234; START; 1.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; FALSE_NEG.
DR   PROSITE; PS50848; START; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; GTPase activation; Phosphoprotein.
FT   CHAIN         1   1092       Rho GTPase-activating protein 7.
FT                                /FTId=PRO_0000056708.
FT   DOMAIN       11     78       SAM.
FT   DOMAIN      642    848       Rho-GAP.
FT   DOMAIN      878   1085       START.
FT   COMPBIAS    306    312       Poly-Ser.
FT   COMPBIAS    432    438       Poly-Ser.
FT   MOD_RES      86     86       Phosphoserine.
FT   MOD_RES      89     89       Phosphoserine.
FT   MOD_RES     306    306       Phosphoserine (By similarity).
FT   MOD_RES     307    307       Phosphoserine (By similarity).
FT   MOD_RES     312    312       Phosphoserine (By similarity).
FT   MOD_RES     314    314       Phosphothreonine (By similarity).
FT   MOD_RES     315    315       Phosphoserine (By similarity).
FT   MOD_RES     319    319       Phosphoserine (By similarity).
FT   MOD_RES     320    320       Phosphothreonine (By similarity).
FT   MOD_RES     414    414       Phosphoserine.
FT   VAR_SEQ       1     13       MCRDEPDTMILTQ -> MGDPEGHVMARPLRGPLRRSFSDH
FT                                IRDSTARALDAIWKNTRERRLAE (in isoform 2).
FT                                /FTId=VSP_026144.
FT   CONFLICT     42     42       V -> I (in Ref. 3; BAE36903/BAE27982).
FT   CONFLICT    120    120       F -> S (in Ref. 3; BAE36903/BAE27982).
FT   CONFLICT    192    192       G -> R (in Ref. 1; AAD51760).
FT   CONFLICT    421    422       HD -> SH (in Ref. 1; AAD51760).
FT   CONFLICT    715    717       KQY -> NRN (in Ref. 1; AAD51760).
FT   CONFLICT    730    735       LSETFL -> FSEPSM (in Ref. 1; AAD51760).
FT   CONFLICT    917    917       D -> E (in Ref. 3; BAE36903/BAE27982).
SQ   SEQUENCE   1092 AA;  123367 MW;  9B5DC3103986A751 CRC64;
     MCRDEPDTMI LTQIEAKEAC DWLRVTGFPQ YAQLYEDLLF PVDIALVKRE HDFLDRDAIE
     ALCRRLNTLN KCAVMKLEIS PHRKRSEDSD EDEPCAISGK WTFQRDSKRW SRLEEFDVFF
     PKQDPIPGSP DNSRLQSATS HESMLTDLSE HQEVASVRSL SSTSSSVPTH AAHSGDATTP
     RTNSVISVCS SGHFVGNDDS FSSLPSPKEL SSFSFSMKGH HEKNTKSKTR SLLKRMESLK
     LKGSHHSKHK APSKLGLIIS APILQEGMDE AKLKQLNCVE ISALNGNHIN VPMVRKRSVS
     NSTQTSSSSS QSETSSAVST PSPVTRTRSL STCNKRVGMY LEGFDPFSQS TLNNVTEQNY
     KNRESYPEDT VFYIPEDHKP GTFPKALSHG SFCPSGNSSV NWRTGSFHGP GHLSLRRENS
     HDSPKELKRR NSSSSLSSRL SIYDNVPGSI LYSSSGELAD LENEDIFPEL DDILYHVKGM
     QRIVNQWSEK FSDEGDSDSA LDSVSPCPSS PKQIHLDVDH DRRTPSDLDS TGNSLNEPEE
     PTDIPERRDS GVGASLTRCN RHRLRWHSFQ SSHRPSLNSV SLQINCQSVA QMNLLQKYSL
     LKLTALLEKY TPSNKHGFSW AVPKFMKRIK VPDYKDRSVF GVPLTVNVQR SGQPLPQSIQ
     QAMRYLRNHC LDQVGLFRKS GVKSRIQALR QMNESAEDNV NYEGQSAYDV ADMLKQYFRD
     LPEPLMTNKL SETFLQIYQY VPKDQRLQAI KAAIMLLPDE NREVLQTLLY FLSDVTAAVK
     ENQMTPTNLA VCLAPSLFHL NTLKRENSSP RVMQRKQSLG KPDQKDLNEN LAATQGLAHM
     IAECKKLFQV PEEMSRCRNS YTEQELKPLT LEALGHLNSD QPADYRHFLQ DCVDGLFKEV
     KEKFKGWVSY PTSEQADLSY KKVSEGPPLR LWRSTIEVPA APEEILKRLL KEQHLWDVDL
     LDSKVIEILD SQTEIYQYVQ NSMAPHPARD YVVLRTWRTN LPRGACALLL TSVDHDRAPV
     AGVRVNVLLS RYLIEPCGSG KSKLTYMCRA DLRGHMPEWY SKSFGHLCAA EVVKIRDSFS
     NQNTESKDTR SR
//
ID   GUAD_MOUSE              Reviewed;         454 AA.
AC   Q9R111;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Guanine deaminase;
DE            Short=Guanase;
DE            Short=Guanine aminase;
DE            EC=3.5.4.3;
DE   AltName: Full=Guanine aminohydrolase;
DE            Short=GAH;
GN   Name=Gda;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Paletzki R.F., Gerfen C.R.;
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC   STRAIN=C57BL/6J; TISSUE=Erythrocyte;
RX   MEDLINE=99175201; PubMed=10075721; DOI=10.1074/jbc.274.12.8175;
RA   Yuan G., Bin J.C., McKay D.J., Snyder F.F.;
RT   "Cloning and characterization of human guanine deaminase. Purification
RT   and partial amino acid sequence of the mouse protein.";
RL   J. Biol. Chem. 274:8175-8180(1999).
CC   -!- FUNCTION: Catalyzes the hydrolytic deamination of guanine,
CC       producing xanthine and ammonia.
CC   -!- CATALYTIC ACTIVITY: Guanine + H(2)O = xanthine + NH(3).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- PATHWAY: Purine metabolism; guanine degradation; xanthine from
CC       guanine: step 1/1.
CC   -!- SUBUNIT: Homodimer.
CC   -!- INTERACTION:
CC       Q62108:Dlg4; NbExp=1; IntAct=EBI-2308876, EBI-300895;
CC   -!- SIMILARITY: Belongs to the ATZ/TRZ family.
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DR   EMBL; AF174583; AAD50297.1; -; mRNA.
DR   IPI; IPI00469987; -.
DR   RefSeq; NP_034396.1; NM_010266.2.
DR   UniGene; Mm.45054; -.
DR   ProteinModelPortal; Q9R111; -.
DR   SMR; Q9R111; 8-451.
DR   IntAct; Q9R111; 4.
DR   STRING; Q9R111; -.
DR   MEROPS; M38.981; -.
DR   REPRODUCTION-2DPAGE; IPI00469987; -.
DR   REPRODUCTION-2DPAGE; Q9R111; -.
DR   PRIDE; Q9R111; -.
DR   Ensembl; ENSMUST00000087600; ENSMUSP00000084882; ENSMUSG00000058624.
DR   GeneID; 14544; -.
DR   KEGG; mmu:14544; -.
DR   UCSC; uc008gyx.1; mouse.
DR   CTD; 14544; -.
DR   MGI; MGI:95678; Gda.
DR   GeneTree; ENSGT00390000017130; -.
DR   HOVERGEN; HBG005930; -.
DR   InParanoid; Q9R111; -.
DR   OMA; CFKPCEI; -.
DR   OrthoDB; EOG4ZKJMM; -.
DR   PhylomeDB; Q9R111; -.
DR   BRENDA; 3.5.4.3; 244.
DR   NextBio; 286216; -.
DR   ArrayExpress; Q9R111; -.
DR   Bgee; Q9R111; -.
DR   CleanEx; MM_GDA; -.
DR   Genevestigator; Q9R111; -.
DR   GermOnline; ENSMUSG00000058624; Mus musculus.
DR   GO; GO:0008892; F:guanine deaminase activity; IEA:EC.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR006680; Amidohydro_1.
DR   InterPro; IPR014311; Guanine_deaminase.
DR   PANTHER; PTHR11271:SF6; Guanine_deaminase; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   TIGRFAMs; TIGR02967; guan_deamin; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Metal-binding; Zinc.
FT   CHAIN         1    454       Guanine deaminase.
FT                                /FTId=PRO_0000122299.
FT   METAL        82     82       Zinc; via tele nitrogen (By similarity).
FT   METAL        84     84       Zinc; via tele nitrogen (By similarity).
FT   METAL       240    240       Zinc; via tele nitrogen (By similarity).
FT   METAL       330    330       Zinc (By similarity).
FT   BINDING      87     87       Substrate (By similarity).
FT   BINDING     213    213       Substrate (By similarity).
FT   BINDING     243    243       Substrate (By similarity).
FT   BINDING     279    279       Substrate (By similarity).
SQ   SEQUENCE   454 AA;  51013 MW;  7711573C8C93D64E CRC64;
     MCAARTPPLA LVFRGTFVHS TWTCPMEVLR DHLLGVSDSG KIVFLEESSQ QEKLAKEWCF
     KPCEIRELSH HEFFMPGLVD THIHAPQYAF AGSNVDLPLL EWLNKYTFPT EQRFRSTDVA
     EEVYTRVVRR TLKNGTTTAC YFGTIHTDSS LILAEITDKF GQRAFVGKVC MDLNDTVPEY
     KETTEESVKE TERFVSEMLQ KNYPRVKPIV TPRFTLSCTE TLMSELGNIA KTHDLYIQSH
     ISENREEIEA VKSLYPSYKN YTDVYDKNNL LTNKTVMAHG CYLSEEELNI FSERGASIAH
     CPNSNLSLSS GLLNVLEVLK HKVKIGLGTD VAGGYSYSML DAIRRAVMVS NVLLINKVNE
     KNLTLKEVFR LATLGGSQAL GLDSEIGNFE VGKEFDALLI NPRASDSPID LFYGDFVGDI
     SEAVIQKFLY LGDDRNIEEV YVGGKQVVPF SSSV
//
ID   SQRD_MOUSE              Reviewed;         450 AA.
AC   Q9R112; Q91XA1; Q9D891;
DT   13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2002, sequence version 2.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=Sulfide:quinone oxidoreductase, mitochondrial;
DE            EC=1.-.-.-;
DE   Flags: Precursor;
GN   Name=Sqrdl;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RA   Huang L., Gitschier J.;
RT   "Positional cloning of the pallid gene in the pallid mutant.";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Catalyzes the oxidation of hydrogen sulfide, with the
CC       help of a quinone (By similarity).
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (Probable).
CC   -!- SIMILARITY: Belongs to the SQRD family.
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DR   EMBL; AF174535; AAD50300.1; -; mRNA.
DR   EMBL; AK008290; BAB25580.1; -; mRNA.
DR   EMBL; BC011153; AAH11153.1; -; mRNA.
DR   IPI; IPI00313998; -.
DR   UniGene; Mm.28986; -.
DR   ProteinModelPortal; Q9R112; -.
DR   SMR; Q9R112; 42-80.
DR   STRING; Q9R112; -.
DR   PhosphoSite; Q9R112; -.
DR   PRIDE; Q9R112; -.
DR   Ensembl; ENSMUST00000005953; ENSMUSP00000005953; ENSMUSG00000005803.
DR   Ensembl; ENSMUST00000110506; ENSMUSP00000106133; ENSMUSG00000005803.
DR   MGI; MGI:1929899; Sqrdl.
DR   GeneTree; ENSGT00390000019406; -.
DR   HOGENOM; HBG296818; -.
DR   HOVERGEN; HBG029110; -.
DR   InParanoid; Q9R112; -.
DR   OrthoDB; EOG40VVPR; -.
DR   NextBio; 314552; -.
DR   ArrayExpress; Q9R112; -.
DR   Bgee; Q9R112; -.
DR   CleanEx; MM_SQRDL; -.
DR   Genevestigator; Q9R112; -.
DR   GermOnline; ENSMUSG00000005803; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR015904; Sulphide_quinone_reductase.
DR   PANTHER; PTHR10632; Sulphide_quinone_reductase; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; FAD; Flavoprotein; Mitochondrion; NADP; Oxidoreductase;
KW   Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    450       Sulfide:quinone oxidoreductase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000022409.
FT   MOD_RES     173    173       N6-acetyllysine (By similarity).
FT   MOD_RES     180    180       N6-acetyllysine (By similarity).
FT   CONFLICT      6      6       T -> A (in Ref. 3; AAH11153).
FT   CONFLICT     99     99       S -> T (in Ref. 2; BAB25580).
FT   CONFLICT    184    184       D -> G (in Ref. 2; BAB25580).
FT   CONFLICT    185    185       F -> L (in Ref. 1; AAD50300).
SQ   SEQUENCE   450 AA;  50340 MW;  08A5003153803D2D CRC64;
     MAPLVTVVSS PRARLFACFL RLGTQQAGPL QLHTGACCTA KNHYEVLVLG GGAGGITMAT
     RMKRRVGAEN VAIVEPSERH FYQPIWTLVG AGAKELSLSV RSTLSVIPSG VQWIQDRVAE
     LNPDENCIRT DSGKEISYRY LIIALGIQLD YEKIKGLPEG FAYPKIGSNY SVKTVEKTWK
     ALQDFKEGNA LFTFPNTPVK CAGAPQKIMY LSEAYFRKTG KRPKANIIFN TALGTIFGVK
     KYADALQEII RERDVSVNYK HNLIEVRPDK QEAVFEILDK PGETHVIPYE MLHVTPPMSA
     PDVLKRSPVA DSAGWVDVDK ETLQHKKYPN VFGIGDCTNL PTSKTAAAVA AQSGILDRTM
     CLIMKNQRPI KKYDGYTSCP LVTGYNRVIL AEFDYTAQPL ETFPFDQSKE RITMYLMKAD
     MMPFLYWNMM LRGYWGGPAF LRKLFHLGMN
//
ID   MTA2_MOUSE              Reviewed;         668 AA.
AC   Q9R190; Q3TVT8;
DT   28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Metastasis-associated protein MTA2;
DE   AltName: Full=Metastasis-associated 1-like 1;
GN   Name=Mta2; Synonyms=Mta1l1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99375308; PubMed=10444591;
RA   Zhang Y., Ng H.-H., Erdjument-Bromage H., Tempst P., Bird A.,
RA   Reinberg D.;
RT   "Analysis of the NuRD subunits reveals a histone deacetylase core
RT   complex and a connection with DNA methylation.";
RL   Genes Dev. 13:1924-1935(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   MEDLINE=21261965; PubMed=11368903; DOI=10.1016/S0378-1119(01)00429-2;
RA   Xia L., Zhang Y.;
RT   "Sp1 and ETS family transcription factors regulate the mouse Mta2 gene
RT   expression.";
RL   Gene 268:77-85(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=129/SvJ; TISSUE=Liver;
RX   MEDLINE=21622604; PubMed=11749719; DOI=10.1089/104454901753340596;
RA   Matsusue K., Takiguchi S., Toh Y., Kono A.;
RT   "Characterization of mouse metastasis-associated gene 2: genomic
RT   structure, nuclear localization signal, and alternative potentials as
RT   transcriptional activator and repressor.";
RL   DNA Cell Biol. 20:603-611(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Amnion, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   INTERACTION WITH HDAC7.
RX   MEDLINE=20442375; PubMed=10984530; DOI=10.1073/pnas.97.19.10330;
RA   Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M.;
RT   "Identification of a nuclear domain with deacetylase activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000).
RN   [7]
RP   INTERACTION WITH MBD3.
RX   MEDLINE=22218071; PubMed=12124384; DOI=10.1074/jbc.M203455200;
RA   Saito M., Ishikawa F.;
RT   "The mCpG-binding domain of human MBD3 does not bind to mCpG but
RT   interacts with NuRD/Mi2 components HDAC1 and MTA2.";
RL   J. Biol. Chem. 277:35434-35439(2002).
CC   -!- FUNCTION: May be involved in the regulation of gene expression as
CC       repressor and activator. The repression might be related to
CC       covalent modification of histone proteins.
CC   -!- SUBUNIT: Component of the nucleosome-remodeling and histone-
CC       deacetylase multiprotein complex (NuRD). Interacts with HDAC7,
CC       p53/TP53, MINT and MBD3 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Contains 1 BAH domain.
CC   -!- SIMILARITY: Contains 1 ELM2 domain.
CC   -!- SIMILARITY: Contains 1 GATA-type zinc finger.
CC   -!- SIMILARITY: Contains 1 SANT domain.
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DR   EMBL; AF159259; AAD51281.1; -; mRNA.
DR   EMBL; AF348083; AAL30174.1; -; Genomic_DNA.
DR   EMBL; AB047977; BAB79231.1; -; Genomic_DNA.
DR   EMBL; AK088158; BAC40180.1; -; mRNA.
DR   EMBL; AK147099; BAE27675.1; -; mRNA.
DR   EMBL; AK159979; BAE35530.1; -; mRNA.
DR   EMBL; BC079847; AAH79847.1; -; mRNA.
DR   IPI; IPI00128230; -.
DR   RefSeq; NP_035972.3; NM_011842.3.
DR   UniGene; Mm.25339; -.
DR   ProteinModelPortal; Q9R190; -.
DR   SMR; Q9R190; 5-142, 265-321.
DR   STRING; Q9R190; -.
DR   PhosphoSite; Q9R190; -.
DR   REPRODUCTION-2DPAGE; IPI00128230; -.
DR   PRIDE; Q9R190; -.
DR   Ensembl; ENSMUST00000096240; ENSMUSP00000093959; ENSMUSG00000071646.
DR   GeneID; 23942; -.
DR   KEGG; mmu:23942; -.
DR   UCSC; uc008gof.1; mouse.
DR   CTD; 23942; -.
DR   MGI; MGI:1346340; Mta2.
DR   eggNOG; roNOG13145; -.
DR   GeneTree; ENSGT00580000081398; -.
DR   HOGENOM; HBG403019; -.
DR   HOVERGEN; HBG002598; -.
DR   InParanoid; Q9R190; -.
DR   OMA; TPTQLEG; -.
DR   OrthoDB; EOG4640BG; -.
DR   PhylomeDB; Q9R190; -.
DR   NextBio; 303749; -.
DR   ArrayExpress; Q9R190; -.
DR   Bgee; Q9R190; -.
DR   CleanEx; MM_MTA2; -.
DR   Genevestigator; Q9R190; -.
DR   GermOnline; ENSMUSG00000071646; Mus musculus.
DR   GO; GO:0016581; C:NuRD complex; IDA:MGI.
DR   GO; GO:0004407; F:histone deacetylase activity; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0016563; F:transcription activator activity; IDA:MGI.
DR   GO; GO:0016564; F:transcription repressor activity; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006338; P:chromatin remodeling; TAS:MGI.
DR   GO; GO:0006323; P:DNA packaging; TAS:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   InterPro; IPR001025; BAH_dom.
DR   InterPro; IPR000949; ELM2_dom.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR001005; SANT_DNA-bd.
DR   InterPro; IPR017884; SANT_eukarya.
DR   InterPro; IPR000679; Znf_GATA.
DR   Pfam; PF01426; BAH; 1.
DR   Pfam; PF01448; ELM2; 1.
DR   Pfam; PF00320; GATA; 1.
DR   SMART; SM00439; BAH; 1.
DR   SMART; SM00717; SANT; 1.
DR   SMART; SM00401; ZnF_GATA; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
DR   PROSITE; PS51038; BAH; 1.
DR   PROSITE; PS51156; ELM2; 1.
DR   PROSITE; PS00344; GATA_ZN_FINGER_1; FALSE_NEG.
DR   PROSITE; PS50114; GATA_ZN_FINGER_2; FALSE_NEG.
DR   PROSITE; PS51293; SANT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Zinc; Zinc-finger.
FT   CHAIN         1    668       Metastasis-associated protein MTA2.
FT                                /FTId=PRO_0000083497.
FT   DOMAIN        1    144       BAH.
FT   DOMAIN      145    256       ELM2.
FT   DOMAIN      263    315       SANT.
FT   ZN_FING     367    394       GATA-type; atypical.
FT   MOD_RES      57     57       Phosphoserine (By similarity).
FT   MOD_RES     152    152       N6-acetyllysine (By similarity).
FT   MOD_RES     433    433       Phosphoserine (By similarity).
FT   MOD_RES     435    435       Phosphoserine (By similarity).
FT   MOD_RES     505    505       Phosphothreonine (By similarity).
FT   MOD_RES     534    534       Phosphothreonine (By similarity).
FT   MOD_RES     540    540       Phosphothreonine (By similarity).
FT   CONFLICT    489    489       N -> I (in Ref. 4; BAC40180).
SQ   SEQUENCE   668 AA;  75030 MW;  88996F779BA6F4D1 CRC64;
     MAANMYRVGD YVYFENSSSN PYLVRRIEEL NKTANGNVEA KVVCLFRRRD ISSSLNSLAD
     SNAREFEEES KQPGVSEQQR HQLKHRELFL SRQFESLPAT HIRGKCSVTL LNETDILNQY
     LDKEDCFFYS LVFDPVQKTL LADQGEIRVG CKFQAEIPDR LAEGESDNRN QQKMEMKVWD
     PDNPLTDRQI DQFLVVARAV GTFARALDCS SSIRQPSLHM SAAAASRDIT LFHAMDTLQR
     NGYDLAKAMS TLVPQGGPVL CRDEMEEWSA SEAMLFEEAL EKYGKDFNDI RQDFLPWKSL
     ASIVQFYYMW KTTDRYIQQK RLKAAEADSK LKQVYIPTYT KPNPNQIISV GSKPGMNGAG
     FQKGLTCESC HTTQSAQWYA WGPPNMQCRL CASCWIYWKK YGGLKTPTQL EGAARGTTEP
     HSRGHLSRPE AQSLSPYTTS ANRAKLLAKN RQTFLLQTTK LTRLARRMCR DLLQPRRAAR
     RPYAPINANA IKAECSIRLP KAAKTPLKIH PLVRLPLATI VKDLVAQAPL KPKTPRGTKT
     PINRNQLTQN RGLGGIMVKR SYETMAGAGV PFSANGRPLA SGIRSSSQPA AKRQKLNPAD
     APNPVVFVAT KDTRALRKAL THLEMRRAAR RPNLPLKVKP TLMTVRPPVP LPASSHPAST
     NEPIVLED
//
ID   CETN2_MOUSE             Reviewed;         172 AA.
AC   Q9R1K9; B1AUQ6; B1AUQ8; Q3UBB4; Q9CWM0;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Centrin-2;
DE   AltName: Full=Caltractin isoform 1;
GN   Name=Cetn2; Synonyms=Calt;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=129/Ola;
RX   PubMed=11250075; DOI=10.1016/S0378-1119(01)00342-0;
RA   Hart P.E., Poynter G.M., Whitehead C.M., Orth J.D., Glantz J.N.,
RA   Busby R.C., Barrett S.L., Salisbury J.L.;
RT   "Characterization of the X-linked murine centrin Cetn2 gene.";
RL   Gene 264:205-213(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=20314869; PubMed=10854409; DOI=10.1101/gr.10.6.758;
RA   Mallon A.-M., Platzer M., Bate R., Gloeckner G., Botcherby M.R.M.,
RA   Nordsiek G., Strivens M.A., Kioschis P., Dangel A., Cunningham D.,
RA   Straw R.N.A., Weston P., Gilbert M., Fernando S., Goodall K.,
RA   Hunter G., Greystrong J.S., Clarke D., Kimberley C., Goerdes M.,
RA   Blechschmidt K., Rump A., Hinzmann B., Mundy C.R., Miller W.,
RA   Poustka A., Herman G.E., Rhodes M., Denny P., Rosenthal A.,
RA   Brown S.D.M.;
RT   "Comparative genome sequence analysis of the Bpa/Str region in mouse
RT   and man.";
RL   Genome Res. 10:758-775(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Corpora quadrigemina, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND THR-26, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Plays a fundamental role in microtubule-organizing
CC       center structure and function. Required for centriole duplication
CC       and correct spindle formation. Has a role in regulating
CC       cytokinesis and genome stability via cooperation with CALM1 and
CC       CEP110 (By similarity).
CC   -!- FUNCTION: Involved in global genome nucleotide excision repair
CC       (GG-NER) by acting as component of the XPC complex. Cooperatively
CC       with Rad23b appears to stabilize Xpc. In vitro, stimulates DNA
CC       binding of the Xpc:Rad23b dimer (By similarity).
CC   -!- FUNCTION: The XPC complex is proposed to represent the first
CC       factor bound at the sites of DNA damage and together with other
CC       core recognition factors, Xpa, RPA and the TFIIH complex, is part
CC       of the pre-incision (or initial recognition) complex. The XPC
CC       complex recognizes a wide spectrum of damaged DNA characterized by
CC       distortions of the DNA helix such as single-stranded loops,
CC       mismatched bubbles or single stranded overhangs. The orientation
CC       of XPC complex binding appears to be crucial for inducing a
CC       productive NER. XPC complex is proposed to recognize and to
CC       interact with unpaired bases on the undamaged DNA strand which is
CC       followed by recruitment of the TFIIH complex and subsequent
CC       scanning for lesions in the opposite strand in a 5'-to-3'
CC       direction by the NER machinery. Cyclobutane pyrimidine dimers
CC       (CPDs) which are formed upon UV-induced DNA damage esacpe
CC       detection by the XPC complex due to a low degree of structural
CC       perurbation. Instead they are detected by the UV-DDB complex which
CC       in turn recruits and cooperates with the XPC complex in the
CC       respective DNA repair (By similarity).
CC   -!- SUBUNIT: Monomer. Homooligomer. Interacts with CEP110, SFI1.
CC       Component of the XPC complex composed of XPC, RAD23B and CETN2 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, centrosome,
CC       centriole. Nucleus (By similarity). Note=Centrosome of S-phase,
CC       interphase and mitotic cells.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed in all adult tissues
CC       tested, with strongest expression in brain, spleen, kidney, small
CC       intestine and ovary. Also expressed in the NIH 3T3 fibroblast cell
CC       line and peripheral blood lymphocytes.
CC   -!- MISCELLANEOUS: Binds two moles of calcium per mole of protein (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the centrin family.
CC   -!- SIMILARITY: Contains 4 EF-hand domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM20357.1; Type=Erroneous gene model prediction;
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DR   EMBL; AF080592; AAD46391.1; -; Genomic_DNA.
DR   EMBL; AL021127; CAB88169.1; -; Genomic_DNA.
DR   EMBL; AK004081; BAB23161.1; -; mRNA.
DR   EMBL; AK010541; BAB27017.1; -; mRNA.
DR   EMBL; AK140156; BAE24259.1; -; mRNA.
DR   EMBL; AK151033; BAE30050.1; -; mRNA.
DR   EMBL; AL671908; CAM20357.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL671908; CAM20359.1; -; Genomic_DNA.
DR   EMBL; CH466624; EDL26558.1; -; Genomic_DNA.
DR   EMBL; BC013545; AAH13545.1; -; mRNA.
DR   IPI; IPI00128741; -.
DR   RefSeq; NP_062278.2; NM_019405.6.
DR   UniGene; Mm.24643; -.
DR   ProteinModelPortal; Q9R1K9; -.
DR   SMR; Q9R1K9; 24-172.
DR   STRING; Q9R1K9; -.
DR   PhosphoSite; Q9R1K9; -.
DR   PRIDE; Q9R1K9; -.
DR   Ensembl; ENSMUST00000114551; ENSMUSP00000110198; ENSMUSG00000031347.
DR   GeneID; 26370; -.
DR   KEGG; mmu:26370; -.
DR   UCSC; uc009tkt.1; mouse.
DR   CTD; 26370; -.
DR   MGI; MGI:1347085; Cetn2.
DR   eggNOG; roNOG15796; -.
DR   GeneTree; ENSGT00590000082945; -.
DR   HOGENOM; HBG746798; -.
DR   HOVERGEN; HBG012180; -.
DR   InParanoid; Q9R1K9; -.
DR   OMA; RDSREEM; -.
DR   OrthoDB; EOG4NZTVG; -.
DR   PhylomeDB; Q9R1K9; -.
DR   NextBio; 304261; -.
DR   ArrayExpress; Q9R1K9; -.
DR   Bgee; Q9R1K9; -.
DR   CleanEx; MM_CETN2; -.
DR   Genevestigator; Q9R1K9; -.
DR   GermOnline; ENSMUSG00000031347; Mus musculus.
DR   GO; GO:0005814; C:centriole; IDA:MGI.
DR   GO; GO:0005932; C:microtubule basal body; IDA:MGI.
DR   GO; GO:0032391; C:photoreceptor connecting cilium; IDA:MGI.
DR   GO; GO:0071942; C:XPC complex; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; TAS:MGI.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IDA:MGI.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0007283; P:spermatogenesis; IEP:BHF-UCL.
DR   InterPro; IPR018248; EF-hand.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   Pfam; PF00036; efhand; 2.
DR   SMART; SM00054; EFh; 4.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 4.
PE   1: Evidence at protein level;
KW   Calcium; Cell cycle; Cell division; Cytoplasm; Cytoskeleton;
KW   DNA damage; DNA repair; Mitosis; Nucleus; Phosphoprotein; Repeat.
FT   CHAIN         1    172       Centrin-2.
FT                                /FTId=PRO_0000073562.
FT   DOMAIN       28     63       EF-hand 1.
FT   DOMAIN       64     99       EF-hand 2.
FT   DOMAIN      101    136       EF-hand 3.
FT   DOMAIN      137    172       EF-hand 4.
FT   CA_BIND     114    125       1 (By similarity).
FT   CA_BIND     150    161       2 (By similarity).
FT   REGION        1     25       Required for self-assembly (By
FT                                similarity).
FT   MOD_RES      20     20       Phosphoserine.
FT   MOD_RES      26     26       Phosphothreonine.
FT   CONFLICT     34     34       R -> P (in Ref. 3; BAB27017).
FT   CONFLICT     76     76       I -> N (in Ref. 3; BAB27017).
SQ   SEQUENCE   172 AA;  19797 MW;  75311C8386861567 CRC64;
     MASNFKKTTM ASSAQRKRMS PKPELTEDQK QEIREAFDLF DADGTGTIDI KELKVAMRAL
     GFEPKKEEIK KMISEIDKEG TGKMNFSDFL TVMTQKMSEK DTKEEILKAF KLFDDDETGK
     ISFKNLKRVA KELGENLTDE ELQEMIDEAD RDGDGEVNEQ EFLRIMKKTS LY
//
ID   MAST1_MOUSE             Reviewed;        1570 AA.
AC   Q9R1L5; Q7TQG9; Q80TN0;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 3.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Microtubule-associated serine/threonine-protein kinase 1;
DE            EC=2.7.11.1;
DE   AltName: Full=Syntrophin-associated serine/threonine-protein kinase;
GN   Name=Mast1; Synonyms=Kiaa0973, Sast;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND INTERACTION WITH SNTB2.
RC   STRAIN=C57BL/10;
RX   MEDLINE=99338326; PubMed=10404183; DOI=10.1038/10165;
RA   Lumeng C., Phelps S., Crawford G.E., Walden P.D., Barald K.,
RA   Chamberlain J.S.;
RT   "Interactions between beta 2-syntrophin and a family of microtubule-
RT   associated serine/threonine kinases.";
RL   Nat. Neurosci. 2:611-617(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-1570.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   SEQUENCE REVISION.
RA   Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Appears to link the dystrophin/utrophin network with
CC       microtubule filaments via the syntrophins. Phosphorylation of DMD
CC       or UTRN may modulate their affinities for associated proteins.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SUBUNIT: Part of a low affinity complex that associates with, but
CC       is distinct from, the post-synaptic density. Interacts with SNTB2.
CC   -!- INTERACTION:
CC       P60484:PTEN (xeno); NbExp=2; IntAct=EBI-491771, EBI-696162;
CC       Q61235:Sntb2; NbExp=3; IntAct=EBI-491771, EBI-295974;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Cytoplasm, cytoskeleton. Note=Colocalizes with
CC       syntrophins at the cell membrane.
CC   -!- TISSUE SPECIFICITY: Expressed in the vascular endothelium and in
CC       proximity to neuronal nuclei throughout the cortex and cerebellum.
CC       Also detected in ependymal cells, the choroid plexus, in
CC       developing spermatid acrosomes and in both the cell bodies and
CC       axonal processes of motor neurons. Observed as punctate clusters
CC       in the processes of interneurons and along the cell body
CC       periphery.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD50548.1; Type=Frameshift; Positions=Several;
CC       Sequence=BAC65693.3; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA;
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DR   EMBL; AF077818; AAD50548.1; ALT_FRAME; mRNA.
DR   EMBL; BC054524; AAH54524.1; -; mRNA.
DR   EMBL; AK122411; BAC65693.3; ALT_SEQ; Transcribed_RNA.
DR   IPI; IPI00408233; -.
DR   RefSeq; NP_064329.2; NM_019945.2.
DR   UniGene; Mm.154614; -.
DR   ProteinModelPortal; Q9R1L5; -.
DR   SMR; Q9R1L5; 185-678, 969-1063.
DR   IntAct; Q9R1L5; 9.
DR   STRING; Q9R1L5; -.
DR   PhosphoSite; Q9R1L5; -.
DR   PRIDE; Q9R1L5; -.
DR   Ensembl; ENSMUST00000109741; ENSMUSP00000105363; ENSMUSG00000053693.
DR   GeneID; 56527; -.
DR   KEGG; mmu:56527; -.
DR   UCSC; uc009mof.1; mouse.
DR   CTD; 56527; -.
DR   MGI; MGI:1861901; Mast1.
DR   GeneTree; ENSGT00530000063286; -.
DR   HOGENOM; HBG445910; -.
DR   HOVERGEN; HBG052414; -.
DR   InParanoid; Q9R1L5; -.
DR   OMA; KREPSTK; -.
DR   OrthoDB; EOG44F68B; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 312870; -.
DR   ArrayExpress; Q9R1L5; -.
DR   Bgee; Q9R1L5; -.
DR   CleanEx; MM_MAST1; -.
DR   Genevestigator; Q9R1L5; -.
DR   GermOnline; ENSMUSG00000053693; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0007010; P:cytoskeleton organization; IDA:UniProtKB.
DR   GO; GO:0007243; P:intracellular protein kinase cascade; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR015022; MA_Ser/thr_Kinase_dom.
DR   InterPro; IPR023142; MAST_pre-PK_dom.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF08926; DUF1908; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Cytoplasm; Cytoskeleton; Kinase;
KW   Magnesium; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1   1570       Microtubule-associated serine/threonine-
FT                                protein kinase 1.
FT                                /FTId=PRO_0000086310.
FT   DOMAIN      375    648       Protein kinase.
FT   DOMAIN      649    720       AGC-kinase C-terminal.
FT   DOMAIN      968   1056       PDZ.
FT   NP_BIND     381    389       ATP (By similarity).
FT   ACT_SITE    498    498       Proton acceptor (By similarity).
FT   BINDING     404    404       ATP (By similarity).
FT   MOD_RES     161    161       Phosphoserine (By similarity).
FT   MOD_RES     163    163       Phosphoserine (By similarity).
FT   CONFLICT    158    158       R -> P (in Ref. 1; AAD50548).
FT   CONFLICT    197    198       LR -> P (in Ref. 1; AAD50548).
FT   CONFLICT    647    647       S -> T (in Ref. 1; AAD50548).
FT   CONFLICT    672    672       D -> E (in Ref. 1; AAD50548).
FT   CONFLICT   1190   1190       H -> L (in Ref. 1; AAD50548).
FT   CONFLICT   1219   1250       SPPPLPGHTVGSSHTTQSFPAKLHSSPPVVRP -> ARRRC
FT                                QATRWAAHIHAELPCQTTYIATCVRR (in Ref. 1;
FT                                AAD50548).
FT   CONFLICT   1454   1454       L -> V (in Ref. 1; AAD50548).
SQ   SEQUENCE   1570 AA;  170997 MW;  A8F9C868CF241486 CRC64;
     MSDSLWTALS NFSMPSFPGG SMFRRTKSCR TSNRKSLILT STSPTLPRPH SPLPGHLGSS
     PLDSPRNFSP NTPAHFSFAS SRRADGRRWS LASLPSSGYG TNTPSSTVSS SCSSQERLHQ
     LPYQPTVDEL HFLSKHFGST ESITDEDGGR RSPAVRPRSR SLSPGRSPSS YDNEIVMMNH
     VYKERFPKAT AQMEEKLRDF ARAYEPDSVL PLADGVLSFI HHQIIELARD CLTKSRDGLI
     TTVYFYELQE NLEKLLQDAY ERSESLEVAF VTQLVKKLLI IISRPARLLE CLEFNPEEFY
     HLLEAAEGHA KEGHLVKTDI PRYIIRQLGL TRDPFPDVVR LEEQDSGGSN TPEQDDTSEG
     RSSTSKAKKP PGESDFDTIK LISNGAYGAV YLVRHRDTRQ RFAMKKINKQ NLILRNQIQQ
     AFVERDILTF AENPFVVGMF CSFETRRHLC MVMEYVEGGD CATLLKNIGA LPVEMARMYF
     AETVLALEYL HNYGIVHRDL KPDNLLITSM GHIKLTDFGL SKMGLMSLTT NLYEGHIEKD
     AREFLDKQVC GTPEYIAPEV ILRQGYGKPV DWWAMGIILY EFLVGCVPFF GDTPEELFGQ
     VISDDILWPE GDEALPTDAQ LLISSLLQTN PLVRLGAGGA FEVKQHSFFR DLDWTGLLRQ
     KAEFIPHLES EDDTSYFDTR SDRYHHVNSY DEDDTTEEEP VEIRQFSSCS PRFSKVYSSM
     EQLSQHEPKT PVSASGASKR DPSAKGPEEK VAGKREGLGG LTLREKTWRG GSPEIKRFSA
     SEASFLEGEA SPPLGARRRF SALLEPSRFT APQEDEDEAR LRRPPRPSSD PPSSLDTRVP
     KEAVQGEGTS TPGEPEATER SHPGDLGPPS KDGDPSGPRA TNDLVLRRAR HQQLSGDLAV
     EKRPSRTGGK VIKSASATAL SVMIPAVDPH GGSPLASPMS PRSLSSNPSS RDSSPSRDYS
     PAVSGLRSPI TIQRSGKKYG FTLRAIRVYM GDSDVYSVHH IVWHVEEGGP AQEAGLCAGD
     LITHVNGEPV HGMVHPEVVE LILKSGNKVA VTTTPFENTS IRIGPARRSS YKAKMARRNK
     RPSAKDGQES KKRSSLFRKI TKQSNLLHTS RSLSSLNRSL SSSDSLPGSP THGLPARSPT
     HSYRSTPDSA YLGASSQSSS PASSTPNSPA SSASHHIRPS TLHGLSPKLH RQYRSARCKS
     AGNIPLSPLA HTPSPTQASP PPLPGHTVGS SHTTQSFPAK LHSSPPVVRP RPKSAEPPRS
     PLLKRVQSAE KLGASLGADK KGALRKHSLE VGHPDFRKDF HGELALHSLA ESDGETPPIE
     GPGATRQVAV RRLGRQESPL SLGADPLLPD GVQRPMASSK EDSAGGTEAC TPPRATTPGS
     RTLERDSGCT RHQSVQTEDG PGGVARALAK AALSPVQEHE TGRRSSSGEA GTPPVPIVVE
     PARPGVKTQA PQPLGTDSKG LKEPVAQMPL MPDAPRGRER WVLEEVEERT TLSGLRSKPA
     SPKLSPDPQT PTLVPTKNVP RSAAPSVPPA SLMVPGTKPE AGLNSRCPAE AVTPAGLTKT
     GAPSPASLGP
//
ID   PSA1_MOUSE              Reviewed;         263 AA.
AC   Q9R1P4;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 93.
DE   RecName: Full=Proteasome subunit alpha type-1;
DE            EC=3.4.25.1;
DE   AltName: Full=Macropain subunit C2;
DE   AltName: Full=Multicatalytic endopeptidase complex subunit C2;
DE   AltName: Full=Proteasome component C2;
DE   AltName: Full=Proteasome nu chain;
GN   Name=Psma1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=B10.A;
RX   MEDLINE=99367391; PubMed=10436176; DOI=10.1007/s002510050562;
RA   Elenich L.A., Nandi D., Kent E.A., McCluskey T.S., Cruz M., Iyer M.N.,
RA   Woodward E.C., Conn C.W., Ochoa A.L., Ginsburg D.B., Monaco J.J.;
RT   "The complete primary structure of mouse 20S proteasomes.";
RL   Immunogenetics 49:835-842(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   TISSUE=Skeletal muscle;
RX   MEDLINE=20334627; PubMed=10873386; DOI=10.1006/geno.2000.6217;
RA   Hopitzan A., Himmelbauer H., Spevak W., Castanon M.J.;
RT   "The mouse Psma1 gene coding for the alpha-type C2 proteasome subunit:
RT   structural and functional analysis, mapping, and colocalization with
RT   Pde3b on mouse chromosome 7.";
RL   Genomics 66:313-323(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N-3; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 63-82 AND 97-107, AND MASS SPECTROMETRY.
RC   TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [5]
RP   FUNCTION, AND INTERACTION WITH LPS.
RX   PubMed=12874245;
RA   Qureshi N., Perera P.-Y., Shen J., Zhang G., Lenschat A., Splitter G.,
RA   Morrison D.C., Vogel S.N.;
RT   "The proteasome as a lipopolysaccharide-binding protein in
RT   macrophages: differential effects of proteasome inhibition on
RT   lipopolysaccharide-induced signaling events.";
RL   J. Immunol. 171:1515-1525(2003).
RN   [6]
RP   INDUCTION.
RX   PubMed=16317774; DOI=10.1002/pmic.200500218;
RA   Cui F., Wang Y., Wang J., Wei K., Hu J., Liu F., Wang H., Zhao X.,
RA   Zhang X., Yang X.;
RT   "The up-regulation of proteasome subunits and lysosomal proteases in
RT   hepatocellular carcinomas of the HBx gene knockin transgenic mice.";
RL   Proteomics 6:498-504(2006).
RN   [7]
RP   INDUCTION BY DITHIOLETHIONE.
RX   PubMed=17521679; DOI=10.1016/j.lfs.2007.04.014;
RA   Kwak M.K., Huang B., Chang H., Kim J.A., Kensler T.W.;
RT   "Tissue specific increase of the catalytic subunits of the 26S
RT   proteasome by indirect antioxidant dithiolethione in mice: enhanced
RT   activity for degradation of abnormal protein.";
RL   Life Sci. 80:2411-2420(2007).
RN   [8]
RP   FUNCTION, AND MASS SPECTROMETRY.
RX   PubMed=19526544; DOI=10.1002/pmic.200800016;
RA   Martinez-Solano L., Reales-Calderon J.A., Nombela C., Molero G.,
RA   Gil C.;
RT   "Proteomics of RAW 264.7 macrophages upon interaction with heat-
RT   inactivated Candida albicans cells unravel an anti-inflammatory
RT   response.";
RL   Proteomics 9:2995-3010(2009).
CC   -!- FUNCTION: The proteasome is a multicatalytic proteinase complex
CC       which is characterized by its ability to cleave peptides with Arg,
CC       Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
CC       slightly basic pH. The proteasome has an ATP-dependent proteolytic
CC       activity. Mediates the lipopolysaccharide-induced signal
CC       macrophage proteasome. Might be involved in the anti-inflammatory
CC       response of macrophages during the interaction with C.albicans
CC       heat-inactivated cells.
CC   -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
CC       specificity.
CC   -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
CC       two 19S regulatory subunits. The 20S proteasome core is composed
CC       of 28 subunits that are arranged in four stacked rings, resulting
CC       in a barrel-shaped structure. The two end rings are each formed by
CC       seven alpha subunits, and the two central rings are each formed by
CC       seven beta subunits. The catalytic chamber with the active sites
CC       is on the inside of the barrel. Interacts with bacterial
CC       lipopolysaccharide (LPS). Interacts with NOTCH3 (By similarity).
CC   -!- INTERACTION:
CC       Q9UM47:NOTCH3 (xeno); NbExp=1; IntAct=EBI-991653, EBI-1236377;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- INDUCTION: Up-regulated in liver tumor tissues. Up-regulated by
CC       the antioxidant dithiolethione (D3T) in liver, lung and colon (at
CC       the protein level).
CC   -!- PTM: C-terminal extension is partially cleaved off by limited
CC       proteolysis leading to a conversion of the proteasome from its
CC       latent into its active form.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family.
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DR   EMBL; AF060088; AAD50533.1; -; mRNA.
DR   EMBL; AJ272019; CAB95966.1; -; mRNA.
DR   EMBL; AJ272272; CAB95969.1; -; Genomic_DNA.
DR   EMBL; BC005762; AAH05762.1; -; mRNA.
DR   IPI; IPI00283862; -.
DR   RefSeq; NP_036095.1; NM_011965.2.
DR   UniGene; Mm.121265; -.
DR   ProteinModelPortal; Q9R1P4; -.
DR   SMR; Q9R1P4; 4-241.
DR   DIP; DIP-35147N; -.
DR   IntAct; Q9R1P4; 19.
DR   STRING; Q9R1P4; -.
DR   MEROPS; T01.976; -.
DR   PhosphoSite; Q9R1P4; -.
DR   COMPLUYEAST-2DPAGE; Q9R1P4; -.
DR   REPRODUCTION-2DPAGE; IPI00283862; -.
DR   REPRODUCTION-2DPAGE; Q9R1P4; -.
DR   PRIDE; Q9R1P4; -.
DR   Ensembl; ENSMUST00000033008; ENSMUSP00000033008; ENSMUSG00000030751.
DR   GeneID; 26440; -.
DR   KEGG; mmu:26440; -.
DR   NMPDR; fig|10090.3.peg.17468; -.
DR   UCSC; uc009jhy.1; mouse.
DR   CTD; 26440; -.
DR   MGI; MGI:1347005; Psma1.
DR   GeneTree; ENSGT00550000074855; -.
DR   HOGENOM; HBG499923; -.
DR   HOVERGEN; HBG105373; -.
DR   InParanoid; Q9R1P4; -.
DR   OMA; RTYLERC; -.
DR   OrthoDB; EOG4S1T7S; -.
DR   PhylomeDB; Q9R1P4; -.
DR   BRENDA; 3.4.25.1; 244.
DR   NextBio; 304517; -.
DR   ArrayExpress; Q9R1P4; -.
DR   Bgee; Q9R1P4; -.
DR   Genevestigator; Q9R1P4; -.
DR   GermOnline; ENSMUSG00000030751; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IEA:InterPro.
DR   GO; GO:0001530; F:lipopolysaccharide binding; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0002862; P:negative regulation of inflammatory response to antigenic stimulus; IMP:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR000426; Proteasome_asu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   Pfam; PF00227; Proteasome; 1.
DR   Pfam; PF10584; Proteasome_A_N; 1.
DR   SMART; SM00948; Proteasome_A_N; 1.
DR   PROSITE; PS00388; PROTEASOME_A_1; 1.
DR   PROSITE; PS51475; PROTEASOME_A_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase;
KW   Immunity; Isopeptide bond; Nucleus; Phosphoprotein; Protease;
KW   Proteasome; Threonine protease; Ubl conjugation.
FT   CHAIN         1    263       Proteasome subunit alpha type-1.
FT                                /FTId=PRO_0000124062.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      14     14       Phosphoserine (By similarity).
FT   CROSSLNK    115    115       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK    208    208       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
SQ   SEQUENCE   263 AA;  29547 MW;  CC791C56AFBA8043 CRC64;
     MFRNQYDNDV TVWSPQGRIH QIEYAMEAVK QGSATVGLKS KTHAVLVALK RAQSELAAHQ
     KKILHVDNHI GISIAGLTAD ARLLCNFMRQ ECLDSRFVFD RPLPVSRLVS LIGSKTQIPT
     QRYGRRPYGV GLLIAGYDDM GPHIFQTCPS ANYFDCRAMS IGARSQSART YLERHMSEFM
     ECNLDELVKH GLRALRETLP AEQDLTTKNV SIGIVGKDLE FTIYDDDDVS PFLDGLEERP
     QRKAQPSQAA EEPAEKADEP MEH
//
ID   TAGL3_MOUSE             Reviewed;         199 AA.
AC   Q9R1Q8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Transgelin-3;
DE   AltName: Full=Neuronal protein NP25;
GN   Name=Tagln3; Synonyms=Np25;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Hayashi A., Hattori A., Okaze H., Kozuma S., Seki N., Saito T.;
RT   "Mouse neuronal protein (NP25).";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 30-49 AND 65-79, AND MASS SPECTROMETRY.
RC   TISSUE=Hippocampus;
RA   Lubec G., Klug S.;
RL   Submitted (MAR-2007) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the calponin family.
CC   -!- SIMILARITY: Contains 1 calponin-like repeat.
CC   -!- SIMILARITY: Contains 1 CH (calponin-homology) domain.
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DR   EMBL; AB031291; BAA83499.1; -; mRNA.
DR   EMBL; BC043027; AAH43027.1; -; mRNA.
DR   EMBL; BC055338; AAH55338.1; -; mRNA.
DR   IPI; IPI00128986; -.
DR   RefSeq; NP_062728.1; NM_019754.3.
DR   UniGene; Mm.24183; -.
DR   ProteinModelPortal; Q9R1Q8; -.
DR   SMR; Q9R1Q8; 25-153.
DR   STRING; Q9R1Q8; -.
DR   PhosphoSite; Q9R1Q8; -.
DR   PRIDE; Q9R1Q8; -.
DR   Ensembl; ENSMUST00000096057; ENSMUSP00000093762; ENSMUSG00000022658.
DR   GeneID; 56370; -.
DR   KEGG; mmu:56370; -.
DR   UCSC; uc007ziw.1; mouse.
DR   CTD; 56370; -.
DR   MGI; MGI:1926784; Tagln3.
DR   GeneTree; ENSGT00550000074447; -.
DR   HOGENOM; HBG396331; -.
DR   HOVERGEN; HBG005186; -.
DR   InParanoid; Q9R1Q8; -.
DR   OMA; ETQMAFK; -.
DR   OrthoDB; EOG4894NG; -.
DR   PhylomeDB; Q9R1Q8; -.
DR   NextBio; 312420; -.
DR   ArrayExpress; Q9R1Q8; -.
DR   Bgee; Q9R1Q8; -.
DR   CleanEx; MM_TAGLN3; -.
DR   Genevestigator; Q9R1Q8; -.
DR   GermOnline; ENSMUSG00000022658; Mus musculus.
DR   GO; GO:0007517; P:muscle organ development; IEA:InterPro.
DR   InterPro; IPR000557; Calponin_repeat.
DR   InterPro; IPR001715; CH-domain.
DR   InterPro; IPR003096; SM22_calponin.
DR   InterPro; IPR001061; Transgelin.
DR   Gene3D; G3DSA:1.10.418.10; Calponin-homology; 1.
DR   Pfam; PF00402; Calponin; 1.
DR   Pfam; PF00307; CH; 1.
DR   PRINTS; PR00888; SM22CALPONIN.
DR   PRINTS; PR00890; TRANSGELIN.
DR   SMART; SM00033; CH; 1.
DR   SUPFAM; SSF47576; Calponin-homology; 1.
DR   PROSITE; PS01052; CALPONIN_1; 1.
DR   PROSITE; PS51122; CALPONIN_2; 1.
DR   PROSITE; PS50021; CH; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Phosphoprotein.
FT   CHAIN         1    199       Transgelin-3.
FT                                /FTId=PRO_0000204789.
FT   DOMAIN       24    136       CH.
FT   REPEAT      174    199       Calponin-like.
FT   MOD_RES     192    192       Phosphotyrosine (By similarity).
SQ   SEQUENCE   199 AA;  22471 MW;  53802F6F94958202 CRC64;
     MANRGPSYGL SREVQEKIEQ KYDADLENKL VDWIILQCAE DIEHPPPGRA HFQKWLMDGT
     VLCKLINSLY PPGQEPIPKI SESKMAFKQM EQISQFLKAA EVYGVRTTDI FQTVDLWEGK
     DMAAVQRTLM ALGSVAVTKD DGCYRGEPSW FHRKAQQNRR GFSEEQLRQG QNVIGLQMGS
     NKGASQAGMT GYGMPRQIM
//
ID   VAS1_MOUSE              Reviewed;         463 AA.
AC   Q9R1Q9;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-FEB-2011, entry version 88.
DE   RecName: Full=V-type proton ATPase subunit S1;
DE            Short=V-ATPase subunit S1;
DE   AltName: Full=Protein C7-1;
DE   AltName: Full=V-ATPase Ac45 subunit;
DE   AltName: Full=V-ATPase S1 accessory protein;
DE   AltName: Full=Vacuolar proton pump subunit S1;
DE   Flags: Precursor;
GN   Name=Atp6ap1; Synonyms=Atp6ip1, Atp6s1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Hayashi A., Hattori A., Okaze H., Kozuma S., Seki N., Saito T.;
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 325-338 AND 454-463, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-332, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-255, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Vacuolar ATPase is responsible for acidifying a variety
CC       of intracellular compartments in eukaryotic cells (By similarity).
CC   -!- SUBUNIT: Composed of at least 10 subunits.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane; Single-pass membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Belongs to the vacuolar ATPase subunit S1 family.
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DR   EMBL; AB031290; BAA83498.1; -; mRNA.
DR   EMBL; BC048241; AAH48241.1; -; mRNA.
DR   IPI; IPI00128989; -.
DR   RefSeq; NP_061264.1; NM_018794.4.
DR   UniGene; Mm.480350; -.
DR   ProteinModelPortal; Q9R1Q9; -.
DR   STRING; Q9R1Q9; -.
DR   PhosphoSite; Q9R1Q9; -.
DR   PRIDE; Q9R1Q9; -.
DR   Ensembl; ENSMUST00000019231; ENSMUSP00000019231; ENSMUSG00000019087.
DR   GeneID; 54411; -.
DR   KEGG; mmu:54411; -.
DR   UCSC; uc009tol.1; mouse.
DR   CTD; 54411; -.
DR   MGI; MGI:109629; Atp6ap1.
DR   GeneTree; ENSGT00530000063584; -.
DR   HOVERGEN; HBG001090; -.
DR   InParanoid; Q9R1Q9; -.
DR   OMA; GEQFSYA; -.
DR   BRENDA; 3.6.3.14; 244.
DR   NextBio; 311280; -.
DR   ArrayExpress; Q9R1Q9; -.
DR   Bgee; Q9R1Q9; -.
DR   Genevestigator; Q9R1Q9; -.
DR   GermOnline; ENSMUSG00000019087; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:hydrogen ion transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR008388; ATPase_V1-cplx_s1su.
DR   PANTHER; PTHR12471; ATPase_V1_S1; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Glycoprotein;
KW   Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW   Phosphoprotein; Signal; Transmembrane; Transmembrane helix; Transport;
KW   Vacuole.
FT   SIGNAL        1     32       Potential.
FT   CHAIN        33    463       V-type proton ATPase subunit S1.
FT                                /FTId=PRO_0000002544.
FT   TRANSMEM    413    433       Helical; (Potential).
FT   MOD_RES     332    332       Phosphotyrosine.
FT   CARBOHYD    164    164       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    255    255       N-linked (GlcNAc...).
FT   CARBOHYD    267    267       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    290    290       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    297    297       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    344    344       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    351    351       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    399    399       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   463 AA;  51008 MW;  AE28D99718BA0AC0 CRC64;
     MMAATVVSRI RTGTGRAPVM WLSLSLVAVA AAVATEQQVP LVLWSSDRNL WAPVADTHEG
     HITSDMQLST YLDPALELGP RNVLLFLQDK LSIEDFTAYG GVFGNKQDSA FSNLENALDL
     APSSLVLPAV DWYAISTLTT YLQEKLGASP LHVDLATLKE LKLNASLPAL LLIRLPYTAS
     SGLMAPREVL TGNDEVIGQV LSTLKSEDVP YTAALTAVRP SRVARDITMV AGGLGRQLLQ
     TQVASPAIHP PVSYNDTAPR ILFWAQNFSV AYKDEWKDLT SLTFGVENLN LTGSFWNDSF
     AMLSLTYEPL FGATVTFKFI LASRFYPVSA RYWFAMERLE IHSNGSVAHF NVSQVTGPSI
     YSFHCEYVSS VSKKGNLLVT NVPSVWQMTL HNFQIQAFNV TGEQFSYASD CAGFFSPGIW
     MGLLTTLFML FIFTYGLHMI LSLKTMDRFD DHKGPTITLT QIV
//
ID   TRIM3_MOUSE             Reviewed;         744 AA.
AC   Q9R1R2; Q3UMU5;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 100.
DE   RecName: Full=Tripartite motif-containing protein 3;
DE   AltName: Full=RING finger protein 22;
DE   AltName: Full=RING finger protein HAC1;
GN   Name=Trim3; Synonyms=Hac1, Rnf22;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Yanai K., Shimamoto Y., Hirota K., Fukamizu A.;
RT   "Cloning of a new co-activator with ring finger motif.";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=21231161; PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA   Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA   Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A.,
RA   Minucci S., Pelicci P.G., Ballabio A.;
RT   "The tripartite motif family identifies cell compartments.";
RL   EMBO J. 20:2140-2151(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Probably involved in vesicular trafficking via its
CC       association with the CART complex. The CART complex is necessary
CC       for efficient transferrin receptor recycling but not for EGFR
CC       degradation (By similarity).
CC   -!- SUBUNIT: Associates with myosin-Vb (MYO5B) and alpha-actinin-4
CC       (ACTN4). Component of the CART complex, at least composed of
CC       ACTN4, HGS/HRS, MYO5B and TRIM3. Interacts with ZFYVE28/LST2 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Early endosome
CC       (By similarity).
CC   -!- DOMAIN: The interaction with MYO5B is dependent upon its NHL
CC       repeats, which form a beta-propeller (NHL) domain containing six
CC       blades (By similarity).
CC   -!- SIMILARITY: Belongs to the TRIM/RBCC family.
CC   -!- SIMILARITY: Contains 1 B box-type zinc finger.
CC   -!- SIMILARITY: Contains 1 filamin repeat.
CC   -!- SIMILARITY: Contains 6 NHL repeats.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB030912; BAA83343.1; -; mRNA.
DR   EMBL; AF220019; AAG53473.1; -; mRNA.
DR   EMBL; AK019165; BAB31580.1; -; mRNA.
DR   EMBL; AK144674; BAE26003.1; -; mRNA.
DR   EMBL; BC034263; AAH34263.1; -; mRNA.
DR   IPI; IPI00129020; -.
DR   RefSeq; NP_061368.1; NM_018880.2.
DR   UniGene; Mm.29290; -.
DR   ProteinModelPortal; Q9R1R2; -.
DR   SMR; Q9R1R2; 18-74, 471-744.
DR   STRING; Q9R1R2; -.
DR   PhosphoSite; Q9R1R2; -.
DR   PRIDE; Q9R1R2; -.
DR   Ensembl; ENSMUST00000057525; ENSMUSP00000053384; ENSMUSG00000036989.
DR   Ensembl; ENSMUST00000106789; ENSMUSP00000102401; ENSMUSG00000036989.
DR   GeneID; 55992; -.
DR   KEGG; mmu:55992; -.
DR   UCSC; uc009iym.1; mouse.
DR   CTD; 55992; -.
DR   MGI; MGI:1860040; Trim3.
DR   GeneTree; ENSGT00550000074377; -.
DR   HOGENOM; HBG403156; -.
DR   HOVERGEN; HBG054843; -.
DR   InParanoid; Q9R1R2; -.
DR   OMA; KAYRYLQ; -.
DR   OrthoDB; EOG46T30V; -.
DR   NextBio; 311722; -.
DR   ArrayExpress; Q9R1R2; -.
DR   Bgee; Q9R1R2; -.
DR   CleanEx; MM_TRIM3; -.
DR   Genevestigator; Q9R1R2; -.
DR   GermOnline; ENSMUSG00000036989; Mus musculus.
DR   GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR003649; Bbox_C.
DR   InterPro; IPR001298; Filamin.
DR   InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR001258; NHL_repeat.
DR   InterPro; IPR013017; NHL_repeat_subgr.
DR   InterPro; IPR000315; Znf_B-box.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Gene3D; G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00630; Filamin; 1.
DR   Pfam; PF01436; NHL; 6.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00502; BBC; 1.
DR   SMART; SM00336; BBOX; 1.
DR   SMART; SM00557; IG_FLMN; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF81296; Ig_E-set; 1.
DR   PROSITE; PS50194; FILAMIN_REPEAT; 1.
DR   PROSITE; PS51125; NHL; 6.
DR   PROSITE; PS50119; ZF_BBOX; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Cytoplasm; Endosome; Metal-binding;
KW   Phosphoprotein; Protein transport; Repeat; Transport; Zinc;
KW   Zinc-finger.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    744       Tripartite motif-containing protein 3.
FT                                /FTId=PRO_0000056198.
FT   REPEAT      317    418       Filamin.
FT   REPEAT      473    516       NHL 1.
FT   REPEAT      520    563       NHL 2.
FT   REPEAT      564    605       NHL 3.
FT   REPEAT      609    652       NHL 4.
FT   REPEAT      656    699       NHL 5.
FT   REPEAT      700    743       NHL 6.
FT   ZN_FING      22     63       RING-type.
FT   ZN_FING     110    151       B box-type.
FT   COILED      153    224       Potential.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       7      7       Phosphoserine.
FT   MOD_RES     437    437       Phosphoserine (By similarity).
FT   MOD_RES     443    443       Phosphoserine (By similarity).
SQ   SEQUENCE   744 AA;  80774 MW;  D9AEF4FA264BA168 CRC64;
     MAKREDSPGP EVQPMDKQFL VCSICLDRYR CPKVLPCLHT FCERCLQNYI PPQSLTLSCP
     VCRQTSILPE QGVSALQNNF FISSLMEAMQ QAPEGAHDPE DPHPLSAVAG RPLSCPNHEG
     KTMEFYCEAC ETAMCGECRA GEHREHGTVL LRDVVEQHKA ALQRQLEAVR GRLPQLSAAI
     ALVGGISQQL QERKAEALAQ ISAAFEDLEQ ALQQRKQALV SDLESICGAK QKVLQTQLDT
     LRQGQEHIGS SCSFAEQALR LGSAPEVLLV RKHMRERLAA LAAQAFPERP HENAQLELVL
     EVDGLRRSVL NLGALLTTSA TAHETVATGE GLRQALVGQP ASLTVTTKDK DGRLVRTGSA
     ELCAEITGPD GVRLAVPVVD HKNGTYELVY TARTEGDLLL SVLLYGQPVR GSPFRVRALR
     PGDLPPSPDD VKRRVKSPGG PGSHVRQKAV RRPSSMYSTG GKRKDNPIED ELVFRVGSRG
     REKGEFTNLQ GVSAASSGRI VVADSNNQCI QVFSNEGQFK FRFGVRGRSP GQLQRPTGVA
     VDTNGDIIVA DYDNRWVSIF SPEGKFKTKI GAGRLMGPKG VAVDRNGHII VVDNKSCCVF
     TFQPNGKLVG RFGGRGATDR HFAGPHFVAV NNKNEIVVTD FHNHSVKVYS ADGEFLFKFG
     SHGEGNGQFN APTGVAVDSN GNIIVADWGN SRIQVFDSSG SFLSYINTSA EPLYGPQGLA
     LTSDGHVVVA DAGNHCFKAY RYLQ
//
ID   SEPT6_MOUSE             Reviewed;         434 AA.
AC   Q9R1T4; A2A3V9; A2A3W0; Q3TRH9; Q3TUA2; Q542H3; Q6A0C4; Q8C2L2;
AC   Q8C848; Q91XH2; Q9CZ94;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Septin-6;
GN   Name=Sept6; Synonyms=Kiaa0128;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM V).
RC   STRAIN=NIH Swiss; TISSUE=Heart;
RA   Kinoshita M.;
RT   "Identification of mouse Septin6 gene and its product.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS II AND V).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Head, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM I).
RC   TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-427.
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 16-111; 164-171; 177-185; 255-273; 281-287;
RP   294-299; 310-337; 388-397 AND 400-420, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=11064363;
RX   DOI=10.1002/1096-9861(20001211)428:2<223::AID-CNE3>3.0.CO;2-M;
RA   Kinoshita A., Noda M., Kinoshita M.;
RT   "Differential localization of septins in the mouse brain.";
RL   J. Comp. Neurol. 428:223-239(2000).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-416, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Filament-forming cytoskeletal GTPase. Required for
CC       normal organization of the actin cytoskeleton. Involved in
CC       cytokinesis.
CC   -!- SUBUNIT: Septins polymerize into heterooligomeric protein
CC       complexes that form filaments, and associate with cellular
CC       membranes, actin filaments and microtubules. GTPase activity is
CC       required for filament formation. Filaments are assembled from
CC       asymmetrical heterotrimers, composed of SEPT2, SEPT6 and SEPT7
CC       that associate head-to-head to form a hexameric unit. Within the
CC       trimer, directly interacts with SEPT2 and SEPT7. Also interacts
CC       with SEPT9 and SEPT12. Interaction with SEPT12 alters filament
CC       structure. Interacts with SOCS7. Interacts with HNRNPA1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, spindle.
CC       Chromosome, centromere, kinetochore (By similarity). Cleavage
CC       furrow (By similarity). Midbody (By similarity). Note=In metaphase
CC       cells, localized within the microtubule spindle. At the metaphase
CC       plate, in close apposition to the kinetochores of the congressed
CC       chromosomes. In cells undergoing cytokinesis, localized to the
CC       midbody, the ingressing cleavage furrow, and the central spindle
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=Additional isoforms seem to exist;
CC       Name=II;
CC         IsoId=Q9R1T4-1; Sequence=Displayed;
CC       Name=I; Synonyms=III;
CC         IsoId=Q9R1T4-2; Sequence=VSP_006055;
CC       Name=V;
CC         IsoId=Q9R1T4-3; Sequence=VSP_006056;
CC   -!- TISSUE SPECIFICITY: Associated with synaptic vesicles in various
CC       brain regions, including glomeruli of the olfactory bulb.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- MISCELLANEOUS: Coordinated expression with SEPT2 and SEPT7 (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the septin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32172.1; Type=Erroneous initiation;
CC       Sequence=CAM19782.1; Type=Erroneous gene model prediction;
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DR   EMBL; AB023622; BAA82838.1; -; mRNA.
DR   EMBL; AK012858; BAB28516.1; -; mRNA.
DR   EMBL; AK048455; BAC33342.1; -; mRNA.
DR   EMBL; AK088406; BAC40335.1; -; mRNA.
DR   EMBL; AK088614; BAC40453.1; -; mRNA.
DR   EMBL; AK160884; BAE36069.1; -; mRNA.
DR   EMBL; AK162755; BAE37050.1; -; mRNA.
DR   EMBL; AL450399; CAM19780.1; -; Genomic_DNA.
DR   EMBL; AL450399; CAM19781.1; -; Genomic_DNA.
DR   EMBL; AL450399; CAM19782.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC010489; AAH10489.1; -; mRNA.
DR   EMBL; AK172894; BAD32172.1; ALT_INIT; mRNA.
DR   IPI; IPI00226602; -.
DR   IPI; IPI00462803; -.
DR   IPI; IPI00473707; -.
DR   RefSeq; NP_001170794.1; NM_001177323.1.
DR   RefSeq; NP_001170795.1; NM_001177324.1.
DR   RefSeq; NP_064326.2; NM_019942.5.
DR   UniGene; Mm.260036; -.
DR   ProteinModelPortal; Q9R1T4; -.
DR   SMR; Q9R1T4; 17-307.
DR   STRING; Q9R1T4; -.
DR   PhosphoSite; Q9R1T4; -.
DR   PRIDE; Q9R1T4; -.
DR   Ensembl; ENSMUST00000060474; ENSMUSP00000062014; ENSMUSG00000050379.
DR   Ensembl; ENSMUST00000115239; ENSMUSP00000110894; ENSMUSG00000050379.
DR   Ensembl; ENSMUST00000115241; ENSMUSP00000110896; ENSMUSG00000050379.
DR   GeneID; 56526; -.
DR   KEGG; mmu:56526; -.
DR   UCSC; uc009sxx.1; mouse.
DR   UCSC; uc009sxz.1; mouse.
DR   UCSC; uc009sya.1; mouse.
DR   CTD; 56526; -.
DR   MGI; MGI:1888939; Sept6.
DR   eggNOG; roNOG13245; -.
DR   GeneTree; ENSGT00590000082767; -.
DR   HOVERGEN; HBG065093; -.
DR   InParanoid; Q9R1T4; -.
DR   OMA; VRRSKQS; -.
DR   OrthoDB; EOG4320Z8; -.
DR   PhylomeDB; Q9R1T4; -.
DR   ArrayExpress; Q9R1T4; -.
DR   Bgee; Q9R1T4; -.
DR   CleanEx; MM_SEPT6; -.
DR   Genevestigator; Q9R1T4; -.
DR   GermOnline; ENSMUSG00000050379; Mus musculus.
DR   GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR   GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0031105; C:septin complex; IEA:InterPro.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   InterPro; IPR000038; Cell_Div_GTP-bd.
DR   InterPro; IPR016491; Septin.
DR   PANTHER; PTHR18884; Cell_Div_GTP_bd; 1.
DR   Pfam; PF00735; Septin; 1.
DR   PIRSF; PIRSF006698; Septin; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell cycle; Cell division;
KW   Centromere; Chromosome; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; GTP-binding; Kinetochore;
KW   Nucleotide-binding; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    434       Septin-6.
FT                                /FTId=PRO_0000173526.
FT   NP_BIND      49     56       GTP (By similarity).
FT   NP_BIND     185    193       GTP (By similarity).
FT   COILED      321    407       Potential.
FT   BINDING     104    104       GTP; via amide nitrogen (By similarity).
FT   BINDING     239    239       GTP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     254    254       GTP (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     196    196       N6-acetyllysine (By similarity).
FT   MOD_RES     367    367       N6-acetyllysine (By similarity).
FT   MOD_RES     408    408       Phosphoserine (By similarity).
FT   MOD_RES     411    411       Phosphoserine (By similarity).
FT   MOD_RES     416    416       Phosphoserine.
FT   MOD_RES     418    418       Phosphothreonine (By similarity).
FT   VAR_SEQ     428    434       Missing (in isoform I).
FT                                /FTId=VSP_006055.
FT   VAR_SEQ     428    434       NPWLCIE -> FF (in isoform V).
FT                                /FTId=VSP_006056.
FT   CONFLICT     10     10       V -> L (in Ref. 2; BAB28516).
FT   CONFLICT     10     10       Missing (in Ref. 2; BAC33342).
FT   CONFLICT     62     62       L -> P (in Ref. 2; BAC40335).
FT   CONFLICT    141    141       H -> Y (in Ref. 1; BAA82838).
FT   CONFLICT    170    170       M -> I (in Ref. 2; BAE36069).
FT   CONFLICT    238    239       VG -> C (in Ref. 2; BAB28516).
FT   CONFLICT    350    350       V -> A (in Ref. 2; BAC40335).
FT   CONFLICT    403    403       A -> R (in Ref. 1; BAA82838).
SQ   SEQUENCE   434 AA;  49620 MW;  33DCD4F44607168A CRC64;
     MAAADIARQV GEDCRTVPLA GHVGFDSLPD QLVNKSVSQG FCFNILCVGE TGLGKSTLMD
     TLFNTKFEGE PATHTQPGVQ LQSNTYDLQE SNVGLKLTIV STVGFGDQIN KEDSYKPIVE
     FIDAQFEAYL QEELKIRRVL HSYHDSRIHV CLYFIAPTGH SLKSLDLVTM KKLDSKVNII
     PVIAKSDAIS KSELAKFKIK ITSELVSNGV QIYQFPTDDE SVSEINGTMN AHLPFAVVGS
     TEEVKIGNKM MRARQYPWGT VQVENEAHCD FVKLREMLIR VNMEDLREQT HARHYELYRR
     CKLEEMGFKD TDPDSKPFSL QETYEAKRNE FLGELQKKEE EMRQMFVQRV KEKEAELKEA
     EKELHEKFDR LKKLHQEEKK KLEDKKKCLD EEMNAFKQRK AAAELLQSQG SQAGGSQTLK
     RDKEKKNNPW LCIE
//
ID   ADA22_MOUSE             Reviewed;         904 AA.
AC   Q9R1V6; Q5TLI8; Q5TLI9; Q5TLJ0; Q5TLJ1; Q5TLJ2; Q5TLJ3; Q5TLJ4;
AC   Q5TLJ5; Q5TLJ6; Q5TLJ7; Q5TLJ8; Q5TLJ9; Q5TLK0; Q5TLK1; Q5TLK2;
AC   Q5TLK3; Q5TLK4; Q5TLK5; Q5TLK6; Q5TLK7; Q5TLK8; Q8BSF2; Q9R1V5;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein 22;
DE            Short=ADAM 22;
DE   Flags: Precursor;
GN   Name=Adam22;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 17 AND 20).
RC   TISSUE=Brain;
RX   MEDLINE=99365303; PubMed=10433968; DOI=10.1016/S0378-1119(99)00253-X;
RA   Sagane K., Yamazaki K., Mizui Y., Tanaka I.;
RT   "Cloning and chromosomal mapping of mouse ADAM11, ADAM22 and ADAM23.";
RL   Gene 236:79-86(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 619-904 (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 709-904 (ISOFORMS 1; 2; 3; 4; 5; 6; 7;
RP   8; 9; 10; 11; 12; 13; 14; 15; 16; 17; 18; 19; 20 AND 21), TISSUE
RP   SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=15876356; DOI=10.1186/1471-2202-6-33;
RA   Sagane K., Hayakawa K., Kai J., Hirohashi T., Takahashi E.,
RA   Miyamoto N., Ino M., Oki T., Yamazaki K., Nagasu T.;
RT   "Ataxia and peripheral nerve hypomyelination in ADAM22-deficient
RT   mice.";
RL   BMC Neurosci. 6:33-33(2005).
RN   [4]
RP   FUNCTION, INTERACTION WITH LGI1, AND MUTAGENESIS OF ASP-509.
RX   PubMed=16990550; DOI=10.1126/science.1129947;
RA   Fukata Y., Adesnik H., Iwanaga T., Bredt D.S., Nicoll R.A., Fukata M.;
RT   "Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate
RT   synaptic transmission.";
RL   Science 313:1792-1795(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832; SER-864 AND
RP   SER-866, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   INTERACTION WITH LIGI1 AND LGI4.
RX   PubMed=18974846;
RA   Sagane K., Ishihama Y., Sugimoto H.;
RT   "LGI1 and LGI4 bind to ADAM22, ADAM23 and ADAM11.";
RL   Int. J. Biol. Sci. 4:387-396(2008).
CC   -!- FUNCTION: Probable ligand for integrin in the brain. This is a non
CC       catalytic metalloprotease-like protein. Involved in regulation of
CC       cell adhesion and spreading and in inhibition of cell
CC       proliferation (By similarity). Neuronal receptor for LGI1.
CC   -!- SUBUNIT: Interacts with LGI1. Can bind to LGI4.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=21;
CC       Name=1; Synonyms=ADAM22-G01, 22g;
CC         IsoId=Q9R1V6-3; Sequence=Displayed;
CC       Name=2; Synonyms=ADAM22-G03, 22g(D27);
CC         IsoId=Q9R1V6-4; Sequence=VSP_018238;
CC       Name=3; Synonyms=ADAM22-G06, 22g(D26D27);
CC         IsoId=Q9R1V6-5; Sequence=VSP_018235;
CC       Name=4; Synonyms=ADAM22=G07, 22g(D26D27)+29.3;
CC         IsoId=Q9R1V6-6; Sequence=VSP_018235, VSP_018245;
CC       Name=5; Synonyms=ADAM22-G08, 22g(D27)+29.3;
CC         IsoId=Q9R1V6-7; Sequence=VSP_018238, VSP_018245;
CC       Name=6; Synonyms=ADAM22-G09, 22g+29.3;
CC         IsoId=Q9R1V6-8; Sequence=VSP_018245;
CC       Name=7; Synonyms=ADAM22-G10, 22g+29.1;
CC         IsoId=Q9R1V6-9; Sequence=VSP_018241;
CC       Name=8; Synonyms=ADAM22-G11, 22g(D27)+29.5+29.7;
CC         IsoId=Q9R1V6-10; Sequence=VSP_018238, VSP_018246;
CC       Name=9; Synonyms=ADAM22-G12, 22g+29.3+29.7;
CC         IsoId=Q9R1V6-11; Sequence=VSP_018247;
CC       Name=10; Synonyms=ADAM22-G17, 22G[27L]+29.3+29.7;
CC         IsoId=Q9R1V6-12; Sequence=VSP_018239, VSP_018242;
CC       Name=11; Synonyms=ADAM22-G18, 22g(D26)[27L];
CC         IsoId=Q9R1V6-13; Sequence=VSP_018236, VSP_018239;
CC       Name=12; Synonyms=ADAM22-G19, 22g[27L]+29.5;
CC         IsoId=Q9R1V6-14; Sequence=VSP_018239, VSP_018243;
CC       Name=13; Synonyms=ADAM22-G20, 22g[27L];
CC         IsoId=Q9R1V6-15; Sequence=VSP_018239;
CC       Name=14; Synonyms=ADAM22-G21, 22g(D26)[27S];
CC         IsoId=Q9R1V6-16; Sequence=VSP_018234;
CC       Name=15; Synonyms=ADAM22-G22, 22g(D27)+29.7;
CC         IsoId=Q9R1V6-17; Sequence=VSP_018238, VSP_018244;
CC       Name=16; Synonyms=ADAM22-G23, 22g(D25D26D27);
CC         IsoId=Q9R1V6-18; Sequence=VSP_018233;
CC       Name=17; Synonyms=ADAM22-A05, Beta;
CC         IsoId=Q9R1V6-2; Sequence=VSP_018238, VSP_018248;
CC       Name=18; Synonyms=ADAM22-A13;
CC         IsoId=Q9R1V6-19; Sequence=VSP_018235, VSP_018248;
CC       Name=19; Synonyms=ADAM22-A15;
CC         IsoId=Q9R1V6-20; Sequence=VSP_018236, VSP_018248;
CC       Name=20; Synonyms=ADAM22-A04, Alpha;
CC         IsoId=Q9R1V6-1; Sequence=VSP_018248;
CC       Name=21; Synonyms=ADAM22-A16;
CC         IsoId=Q9R1V6-21; Sequence=VSP_018237, VSP_018240;
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in the brain.
CC       Strongly expressed in cerebellar granule cells and hippocampus. In
CC       spinal cord, expression is restricted to gray matter.
CC   -!- PTM: The precursor is cleaved by a furin endopeptidase (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice display severe ataxia within one week
CC       after birth and die before weaning, probably due to convulsions.
CC       They display marked hypomyelination of the peripheral nerves.
CC   -!- SIMILARITY: Contains 1 disintegrin domain.
CC   -!- SIMILARITY: Contains 1 EGF-like domain.
CC   -!- SIMILARITY: Contains 1 peptidase M12B domain.
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DR   EMBL; AB009674; BAA83382.1; -; mRNA.
DR   EMBL; AB009674; BAA83383.1; -; mRNA.
DR   EMBL; AK034528; BAC28742.1; -; mRNA.
DR   EMBL; AB179842; BAD72803.1; -; mRNA.
DR   EMBL; AB179843; BAD72804.1; -; mRNA.
DR   EMBL; AB179844; BAD72805.1; -; mRNA.
DR   EMBL; AB179845; BAD72806.1; -; mRNA.
DR   EMBL; AB179846; BAD72807.1; -; mRNA.
DR   EMBL; AB179847; BAD72808.1; -; mRNA.
DR   EMBL; AB179848; BAD72809.1; -; mRNA.
DR   EMBL; AB179849; BAD72810.1; -; mRNA.
DR   EMBL; AB179850; BAD72811.1; -; mRNA.
DR   EMBL; AB179851; BAD72812.1; -; mRNA.
DR   EMBL; AB179852; BAD72813.1; -; mRNA.
DR   EMBL; AB179853; BAD72814.1; -; mRNA.
DR   EMBL; AB179854; BAD72815.1; -; mRNA.
DR   EMBL; AB179855; BAD72816.1; -; mRNA.
DR   EMBL; AB179856; BAD72817.1; -; mRNA.
DR   EMBL; AB179857; BAD72818.1; -; mRNA.
DR   EMBL; AB179858; BAD72819.1; -; mRNA.
DR   EMBL; AB179859; BAD72820.1; -; mRNA.
DR   EMBL; AB179860; BAD72821.1; -; mRNA.
DR   EMBL; AB179861; BAD72822.1; -; mRNA.
DR   EMBL; AB179862; BAD72823.1; -; mRNA.
DR   IPI; IPI00378796; -.
DR   IPI; IPI00379467; -.
DR   IPI; IPI00404650; -.
DR   IPI; IPI00515160; -.
DR   IPI; IPI00515396; -.
DR   IPI; IPI00515509; -.
DR   IPI; IPI00515580; -.
DR   IPI; IPI00515604; -.
DR   IPI; IPI00515681; -.
DR   IPI; IPI00623219; -.
DR   IPI; IPI00627016; -.
DR   IPI; IPI00749834; -.
DR   IPI; IPI00752301; -.
DR   IPI; IPI00752334; -.
DR   IPI; IPI00752342; -.
DR   IPI; IPI00753070; -.
DR   IPI; IPI00753519; -.
DR   IPI; IPI00753532; -.
DR   IPI; IPI00753983; -.
DR   IPI; IPI00754961; -.
DR   IPI; IPI00755165; -.
DR   RefSeq; NP_001007221.1; NM_001007220.2.
DR   RefSeq; NP_001007222.1; NM_001007221.1.
DR   RefSeq; NP_001091695.1; NM_001098225.1.
DR   UniGene; Mm.275895; -.
DR   ProteinModelPortal; Q9R1V6; -.
DR   SMR; Q9R1V6; 231-716.
DR   STRING; Q9R1V6; -.
DR   MEROPS; M12.978; -.
DR   PhosphoSite; Q9R1V6; -.
DR   PRIDE; Q9R1V6; -.
DR   Ensembl; ENSMUST00000046838; ENSMUSP00000049120; ENSMUSG00000040537.
DR   Ensembl; ENSMUST00000078296; ENSMUSP00000077412; ENSMUSG00000040537.
DR   Ensembl; ENSMUST00000088744; ENSMUSP00000086122; ENSMUSG00000040537.
DR   Ensembl; ENSMUST00000088745; ENSMUSP00000086123; ENSMUSG00000040537.
DR   Ensembl; ENSMUST00000088746; ENSMUSP00000086124; ENSMUSG00000040537.
DR   Ensembl; ENSMUST00000088747; ENSMUSP00000086125; ENSMUSG00000040537.
DR   Ensembl; ENSMUST00000088752; ENSMUSP00000086130; ENSMUSG00000040537.
DR   Ensembl; ENSMUST00000088761; ENSMUSP00000086139; ENSMUSG00000040537.
DR   Ensembl; ENSMUST00000088762; ENSMUSP00000086140; ENSMUSG00000040537.
DR   Ensembl; ENSMUST00000102987; ENSMUSP00000100052; ENSMUSG00000040537.
DR   Ensembl; ENSMUST00000115388; ENSMUSP00000111046; ENSMUSG00000040537.
DR   GeneID; 11496; -.
DR   KEGG; mmu:11496; -.
DR   UCSC; uc008wjv.1; mouse.
DR   UCSC; uc008wjy.1; mouse.
DR   UCSC; uc008wjz.1; mouse.
DR   CTD; 11496; -.
DR   MGI; MGI:1340046; Adam22.
DR   GeneTree; ENSGT00590000083076; -.
DR   HOVERGEN; HBG050456; -.
DR   OMA; VHLFSGS; -.
DR   OrthoDB; EOG44J2HD; -.
DR   ArrayExpress; Q9R1V6; -.
DR   Bgee; Q9R1V6; -.
DR   CleanEx; MM_ADAM22; -.
DR   Genevestigator; Q9R1V6; -.
DR   GermOnline; ENSMUSG00000040537; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0004872; F:receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR   GO; GO:0022011; P:myelination in peripheral nervous system; IMP:MGI.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR001762; Blood-coag_inhib_Disintegrin.
DR   InterPro; IPR018358; Disintegrin_CS.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   Gene3D; G3DSA:4.10.70.10; Blood-coag_inhib_Disintegrin; 1.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   PRINTS; PR00289; DISINTEGRIN.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SMART; SM00181; EGF; 1.
DR   SUPFAM; SSF57552; Disintegrin; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS00427; DISINTEGRIN_1; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; FALSE_NEG.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS00142; ZINC_PROTEASE; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cleavage on pair of basic residues;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW   Phosphoprotein; Receptor; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     23       Potential.
FT   PROPEP       24    223       By similarity.
FT                                /FTId=PRO_0000029114.
FT   CHAIN       224    904       Disintegrin and metalloproteinase domain-
FT                                containing protein 22.
FT                                /FTId=PRO_0000029115.
FT   TOPO_DOM     24    734       Extracellular (Potential).
FT   TRANSMEM    735    755       Helical; (Potential).
FT   TOPO_DOM    756    857       Cytoplasmic (Potential).
FT   DOMAIN      237    436       Peptidase M12B.
FT   DOMAIN      442    529       Disintegrin.
FT   DOMAIN      673    710       EGF-like.
FT   COMPBIAS    533    666       Cys-rich.
FT   MOD_RES     832    832       Phosphoserine.
FT   MOD_RES     864    864       Phosphoserine.
FT   MOD_RES     866    866       Phosphoserine.
FT   MOD_RES     867    867       Phosphoserine (By similarity).
FT   MOD_RES     868    868       Phosphoserine (By similarity).
FT   CARBOHYD    163    163       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    517    517       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    632    632       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    673    673       N-linked (GlcNAc...) (Potential).
FT   DISULFID    347    431       By similarity.
FT   DISULFID    390    415       By similarity.
FT   DISULFID    392    399       By similarity.
FT   DISULFID    501    521       By similarity.
FT   DISULFID    677    692       By similarity.
FT   DISULFID    686    698       By similarity.
FT   DISULFID    700    709       By similarity.
FT   VAR_SEQ     730    904       VAGTNIIIGIIAGTILVLALILGITAWGYKNYREQRQLPQG
FT                                DYVKKPGDGDSFYSDFPPGGSTNSASSSKKRSNGLSHSWSE
FT                                RIPDTKHISDICENGRPRSNSWQGNMGGNKKKIRGKRFRPR
FT                                SNSTETLSPAKSPSSSTGSIASSRKYPYPMPPLPDEGKTAG
FT                                RQSARLWETSI -> QMDSLILGVKGFQTQNIFQTSVKMGD
FT                                LAVTPGKVTWEATKRKSEGKDLDLDLTQLRPCHLPSLLLHQ
FT                                LGLLPPAENTRTLCLRFQTRGRQRADRAPGYGRHPF (in
FT                                isoform 16).
FT                                /FTId=VSP_018233.
FT   VAR_SEQ     760    904       NYREQRQLPQGDYVKKPGDGDSFYSDFPPGGSTNSASSSKK
FT                                RSNGLSHSWSERIPDTKHISDICENGRPRSNSWQGNMGGNK
FT                                KKIRGKRFRPRSNSTETLSPAKSPSSSTGSIASSRKYPYPM
FT                                PPLPDEGKTAGRQSARLWETSI -> FPPVPSHIIPLVRTF
FT                                HYFAAGQMDSLILGVKGFQTQNIFQTSVKMGDLAVTPGKVT
FT                                WEATKRKSEGKDLDLDLTQLRPCHLPSLLLHQLGLLPPAEN
FT                                TRTLCLRFQTRGRQRADRAPGYGRHPF (in isoform
FT                                14).
FT                                /FTId=VSP_018234.
FT   VAR_SEQ     760    801       Missing (in isoform 3, isoform 4 and
FT                                isoform 18).
FT                                /FTId=VSP_018235.
FT   VAR_SEQ     760    765       Missing (in isoform 11 and isoform 19).
FT                                /FTId=VSP_018236.
FT   VAR_SEQ     766    846       QLPQGDYVKKPGDGDSFYSDFPPGGSTNSASSSKKRSNGLS
FT                                HSWSERIPDTKHISDICENGRPRSNSWQGNMGGNKKKIRG
FT                                -> FPPVPSHIIPLVRTFHYFAAGQMDSLILGVKGFQTQNI
FT                                FQTSVKMGDLAVTPGKVTWEATKRKSEGKDLDLDLTQLSKL
FT                                YL (in isoform 21).
FT                                /FTId=VSP_018237.
FT   VAR_SEQ     766    801       Missing (in isoform 2, isoform 5, isoform
FT                                8, isoform 15 and isoform 17).
FT                                /FTId=VSP_018238.
FT   VAR_SEQ     802    802       S -> SAFLSHFQISTCSITHYSISQNISLFCSRS (in
FT                                isoform 10, isoform 11, isoform 12 and
FT                                isoform 13).
FT                                /FTId=VSP_018239.
FT   VAR_SEQ     847    904       Missing (in isoform 21).
FT                                /FTId=VSP_018240.
FT   VAR_SEQ     857    904       ETLSPAKSPSSSTGSIASSRKYPYPMPPLPDEGKTAGRQSA
FT                                RLWETSI -> DLGIIT (in isoform 7).
FT                                /FTId=VSP_018241.
FT   VAR_SEQ     857    857       E -> EREPQAPEPGHSLAQTIPSQGISPGGSDSPQTGSLD
FT                                HSSQDGPHQQDR (in isoform 10).
FT                                /FTId=VSP_018242.
FT   VAR_SEQ     857    857       E -> EYLNPWFKRDYNVAKWVEDVNKNTEGPYFR (in
FT                                isoform 12).
FT                                /FTId=VSP_018243.
FT   VAR_SEQ     857    857       E -> DSQDGPHQQDR (in isoform 15).
FT                                /FTId=VSP_018244.
FT   VAR_SEQ     857    857       E -> EREPQAPEPGHSLAQTIPSQGISPGGSDSPQTGSLD
FT                                HR (in isoform 4, isoform 5 and isoform
FT                                6).
FT                                /FTId=VSP_018245.
FT   VAR_SEQ     857    857       E -> EYLNPWFKRDYNVAKWVEDVNKNTEGPYFSSQDSPH
FT                                QQDR (in isoform 8).
FT                                /FTId=VSP_018246.
FT   VAR_SEQ     857    857       E -> EREPQAPEPGHSLAQTIPSQGISPGGSDSPQTGSLD
FT                                HRYLNPWFKRDYNVAKWVEDVNKNTEGPYFR (in
FT                                isoform 9).
FT                                /FTId=VSP_018247.
FT   VAR_SEQ     858    904       Missing (in isoform 17, isoform 18,
FT                                isoform 19 and isoform 20).
FT                                /FTId=VSP_018248.
FT   MUTAGEN     509    509       D->N: Fails to bind to LGI1.
FT   CONFLICT    639    639       K -> R (in Ref. 2; BAC28742).
SQ   SEQUENCE   904 AA;  99715 MW;  0FBBD09398EE0B97 CRC64;
     MQAAAAASFW LLCVLGTCPL ARCGRAGVAS LKGLERGKEN RFLERQSIIP LRLIYRLGGE
     DETQHNQLDT RVRGDPGGPQ LTHVDKASFR VDAFGTSFVL DVLLNHELLS SGYVERQIEH
     GGKVVENKGG EHCYYQGQIR GNPVSFVALS TCHGLHGMFY DGNHTYLIEP EENEKSQESS
     HCHSVYKSRQ FEFPLDDLPS EFQRVNITPP QFILKPRLKR RKRQLLRFPR NVEEETKYIE
     LMIVNDHLMF KKHRLSVVYT NTYAKSVVNM ADVIYKDQLK TRIVLVAMET WAADNKFAIS
     ENPLITLREF MKYRRDFIKE KADAVHLFSG SQFESSRSGA AYIGGICSLL RGGGVNEFGK
     TDLMAVTLAQ SLAHNVGIIS DKRKLASGEC KCEDTWSGCI MGDTGYYLPK KFTQCNVEEY
     HDFLNSGGGA CLFNKPSKLL DPPECGNGFI ETGEECDCGT PAECALEGAE CCKKCTLTQD
     SQCSDGLCCK KCKFQPLGTV CREAVNDCDI REICSGNSSQ CAPNVHKMDG YSCDGTQGIC
     FGGRCKTRDR QCKYIWGQKV TASDRYCYEK LNIEGTEKGN CGKDKDTWTQ CNKRDVLCGY
     LLCTNIGNIP RLGELDGEIT STLVVQQGRT LNCSGAHVKL EEDVDLGYVE DGTPCGPQMM
     CLEHRCLPVA SFNFSTCSSS KAGTVCSGNG VCSNELKCVC NRHWTGADCG THFPHNDDAK
     TGITLSGNGV AGTNIIIGII AGTILVLALI LGITAWGYKN YREQRQLPQG DYVKKPGDGD
     SFYSDFPPGG STNSASSSKK RSNGLSHSWS ERIPDTKHIS DICENGRPRS NSWQGNMGGN
     KKKIRGKRFR PRSNSTETLS PAKSPSSSTG SIASSRKYPY PMPPLPDEGK TAGRQSARLW
     ETSI
//
ID   MRP5_MOUSE              Reviewed;        1436 AA.
AC   Q9R1X5; O88284;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Multidrug resistance-associated protein 5;
DE   AltName: Full=ATP-binding cassette sub-family C member 5;
DE   AltName: Full=Multi-specific organic anion transporter C;
DE            Short=MOAT-C;
DE   AltName: Full=SMRP;
GN   Name=Abcc5; Synonyms=Abcc5a, Mrp5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=20184734; PubMed=10721709; DOI=10.1016/S0378-1119(99)00529-6;
RA   Suzuki T., Sasaki H., Kuh H.J., Agui M., Tatsumi Y., Tanabe S.,
RA   Terada M., Saijo N., Nishio K.;
RT   "Detailed structural analysis on both human MRP5 and mouse mrp5
RT   transcripts.";
RL   Gene 242:167-173(2000).
RN   [2]
RP   PROTEIN SEQUENCE OF 261-266, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1302-1436.
RA   Suzuki T., Kuh H., Nishio K.;
RT   "Moleculer cloning of mouse homologue of SMRP/MRP5.";
RL   Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43; SER-509 AND THR-513,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Acts as a multispecific organic anion pump which can
CC       transport nucleotide analogs (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC
CC       family. Conjugate transporter (TC 3.A.1.208) subfamily.
CC   -!- SIMILARITY: Contains 2 ABC transmembrane type-1 domains.
CC   -!- SIMILARITY: Contains 2 ABC transporter domains.
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DR   EMBL; AB019003; BAA76609.1; -; mRNA.
DR   EMBL; AB012090; BAA32782.1; -; mRNA.
DR   IPI; IPI00129205; -.
DR   UniGene; Mm.20845; -.
DR   ProteinModelPortal; Q9R1X5; -.
DR   SMR; Q9R1X5; 575-784, 842-1429.
DR   STRING; Q9R1X5; -.
DR   PhosphoSite; Q9R1X5; -.
DR   PRIDE; Q9R1X5; -.
DR   Ensembl; ENSMUST00000079158; ENSMUSP00000078158; ENSMUSG00000022822.
DR   MGI; MGI:1351644; Abcc5.
DR   eggNOG; roNOG13030; -.
DR   GeneTree; ENSGT00600000084406; -.
DR   HOGENOM; HBG758042; -.
DR   HOVERGEN; HBG108314; -.
DR   InParanoid; Q9R1X5; -.
DR   OrthoDB; EOG408N77; -.
DR   PhylomeDB; Q9R1X5; -.
DR   ArrayExpress; Q9R1X5; -.
DR   Bgee; Q9R1X5; -.
DR   Genevestigator; Q9R1X5; -.
DR   GermOnline; ENSMUSG00000022822; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR017940; ABC_transporter_type1.
DR   InterPro; IPR001140; ABC_transptr_TM_dom.
DR   InterPro; IPR011527; ABC_transptrTM_dom_typ1.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   Pfam; PF00664; ABC_membrane; 2.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF90123; ABC_TM_1; 2.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Glycoprotein; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN         1   1436       Multidrug resistance-associated protein
FT                                5.
FT                                /FTId=PRO_0000093364.
FT   TRANSMEM    179    199       Helical; (Potential).
FT   TRANSMEM    219    239       Helical; (Potential).
FT   TRANSMEM    296    316       Helical; (Potential).
FT   TRANSMEM    317    337       Helical; (Potential).
FT   TRANSMEM    400    420       Helical; (Potential).
FT   TRANSMEM    426    446       Helical; (Potential).
FT   TRANSMEM    608    628       Helical; (Potential).
FT   TRANSMEM    847    867       Helical; (Potential).
FT   TRANSMEM    916    936       Helical; (Potential).
FT   TRANSMEM    996   1016       Helical; (Potential).
FT   TRANSMEM   1017   1037       Helical; (Potential).
FT   TRANSMEM   1101   1121       Helical; (Potential).
FT   TRANSMEM   1126   1146       Helical; (Potential).
FT   DOMAIN      179    459       ABC transmembrane type-1 1.
FT   DOMAIN      562    783       ABC transporter 1.
FT   DOMAIN      858   1154       ABC transmembrane type-1 2.
FT   DOMAIN     1192   1426       ABC transporter 2.
FT   NP_BIND     595    602       ATP 1 (Potential).
FT   NP_BIND    1226   1233       ATP 2 (Potential).
FT   MOD_RES      43     43       Phosphoserine.
FT   MOD_RES     505    505       Phosphoserine (By similarity).
FT   MOD_RES     509    509       Phosphoserine.
FT   MOD_RES     513    513       Phosphothreonine.
FT   CARBOHYD    494    494       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    636    636       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    684    684       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    889    889       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    896    896       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1043   1043       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1328   1328       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1416   1416       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   1436 AA;  161130 MW;  4E32A6E319B8D23C CRC64;
     MKDIDMGKEY IIPSPGYRSD RDRSAVPGQH RDPEEPRFRR TRSLECQDAL ETAARVEGLS
     LDISVHSHLQ ILDEEHSKGK YHHGLSVLKP FRTTTKHQHP VDNAGLFSYM TFSWLSPLAR
     VVHKKGELLM EDVWPLSKYE SSDVNCRRLE RLWQEELNEV GPDAASLRRV VWIFCRTRLI
     LSIVCLMITQ LAGFSGPAFM VKHLLEYTQA TESNLQCSLL LVLGLLLTEI VRSWSLALTW
     ALNYRTGVRL RGAILTMAFK KILKLKNIKE KSLGELINIC SNDGQRMFEA AAVGSLLAGG
     PVVAILGMIY NVIILGPTGF LGSAVFILFY PAMMFVSRLT AYFRRKRVAA TDDRVQKMNE
     VLTYIKFIKM YAWVKAFSQC VQKIREEERR ILEKAGYFQS ITVGVAPIVV VIASVVTFSV
     HMTLGFHLTA AQAFTVVTVF NSMTFALKVT PFSVKSLSEA SVAVDRFKSL FLMEEVHMIK
     NKPASPHIKI EMKNATLAWD SSHSSIQNSP KLTPKMKKDK RATRGKKEKS RQLQHTEHQA
     VLAEQKGHLL LDSDERPSPE EEEGKQIHTG SLRLQRTLYN IDLEIEEGKL VGICGSVGSG
     KTSLVSAILG QMTLLEGSIA VSGTFAYVAQ QAWILNATLR DNILFGKEFD EERYNSVLNS
     CCLRPDLAIL PNSDLTEIGE RGANLSGGQR QRISLARALY SDRSIYILDD PLSALDAHVG
     NHIFNSAIRK RLKSKTVLFV THQLQYLVDC DEVIFMKEGC ITERGTHEEL MNLNGDYATI
     FNNLLLGETP PVEINSKKEA TGSQKSQDKG PKPGSVKKEK AVKSEEGQLV QVEEKGQGSV
     PWSVYWVYIQ AAGGPLAFLV IMVLFMLNVG STAFSTWWLS YWIKQGSGNS TVYQGNRSFV
     SDSMKDNPFM QYYASIYALS MAVMLILKAI RGVVFVKGTL RASSRLHDEL FRRILRSPMK
     FFDTTPTGRI LNRFSKDMDE VDVRLPFQAE MFIQNVILVF FCVGMIAGVF PWFLVAVGPL
     LILFSLLHIV SRVLIRELKR LDNITQSPFL SHITSSIQGL ATIHAYNKRQ EFLHRYQELL
     DDNQAPFFLF TCAMRWLPVR LDIISIALIT STGLMIVSGM ARSLSAYAGL AISYAVQLIG
     LFQFTVRLAS ETEARFTSVE RINHYIKTLS LEAPARIKNK APPHDWPQEG EVTFENAEMR
     YRENLPLVLK KVSFTIKPKE KIGIVGRTGS GKSSLGMALF RLVELSGGCI KIDGIRISDI
     GLADLRSKLA IIPQEPVLFS GTVRSNLDPF NQYTEDQIWD ALERTHMKEC IAQLPLKLES
     EVMENGDNFS VGERQLLCIA RALLRHCKIL ILDEATAAMD TETDLLIQET IREAFADCTM
     LTIAHRLHTV LGSDRIMVLA QGQVVEFDTP SVLLSNDSSR FYAMFAAAEN KVAVKG
//
ID   PTPS_MOUSE              Reviewed;         144 AA.
AC   Q9R1Z7; Q3UIB6; Q9Z2N2;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-2002, sequence version 2.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=6-pyruvoyl tetrahydrobiopterin synthase;
DE            Short=PTP synthase;
DE            Short=PTPS;
DE            EC=4.2.3.12;
GN   Name=Pts;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Ola;
RX   MEDLINE=99110103; PubMed=9894812;
RA   Turri M.O., Ilg E.C., Thony B., Blau N.;
RT   "Structure, genomic localization and recombinant expression of the
RT   mouse 6-pyruvoyl-tetrahydropterin synthase gene.";
RL   Biol. Chem. 379:1441-1447(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RA   Thony B., Turri M., Blau N.;
RL   Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Involved in the biosynthesis of tetrahydrobiopterin, an
CC       essential cofactor of aromatic amino acid hydroxylases. Catalyzes
CC       the transformation of 7,8-dihydroneopterin triphosphate into 6-
CC       pyruvoyl tetrahydropterin.
CC   -!- CATALYTIC ACTIVITY: 7,8-dihydroneopterin 3'-triphosphate = 6-
CC       pyruvoyl-5,6,7,8-tetrahydropterin + triphosphate.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrobiopterin biosynthesis;
CC       tetrahydrobiopterin from 7,8-dihydroneopterin triphosphate: step
CC       1/3.
CC   -!- SUBUNIT: Homohexamer formed of two homotrimers in a head to head
CC       fashion (By similarity).
CC   -!- PTM: Phosphorylation of Ser-18 is required for maximal enzyme
CC       activity (By similarity).
CC   -!- MISCELLANEOUS: The active site is at the interface between 2
CC       subunits. The proton acceptor Cys is on one subunit, and the
CC       charge relay system is on the other subunit.
CC   -!- SIMILARITY: Belongs to the PTPS family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF061880; AAD15827.1; -; Genomic_DNA.
DR   EMBL; AF061878; AAD15827.1; JOINED; Genomic_DNA.
DR   EMBL; AF061879; AAD15827.1; JOINED; Genomic_DNA.
DR   EMBL; AF043225; AAD02249.1; -; mRNA.
DR   EMBL; AK002614; BAB22231.1; -; mRNA.
DR   EMBL; AK146987; BAE27590.1; -; mRNA.
DR   EMBL; BC029013; AAH29013.1; -; mRNA.
DR   IPI; IPI00154100; -.
DR   RefSeq; NP_035350.1; NM_011220.2.
DR   UniGene; Mm.35856; -.
DR   ProteinModelPortal; Q9R1Z7; -.
DR   SMR; Q9R1Z7; 8-144.
DR   IntAct; Q9R1Z7; 5.
DR   MINT; MINT-217930; -.
DR   STRING; Q9R1Z7; -.
DR   PhosphoSite; Q9R1Z7; -.
DR   PRIDE; Q9R1Z7; -.
DR   Ensembl; ENSMUST00000034570; ENSMUSP00000034570; ENSMUSG00000032067.
DR   GeneID; 19286; -.
DR   KEGG; mmu:19286; -.
DR   NMPDR; fig|10090.3.peg.20157; -.
DR   UCSC; uc009pjp.1; mouse.
DR   CTD; 19286; -.
DR   MGI; MGI:1338783; Pts.
DR   eggNOG; roNOG15848; -.
DR   GeneTree; ENSGT00390000002752; -.
DR   HOGENOM; HBG727155; -.
DR   HOVERGEN; HBG004358; -.
DR   InParanoid; Q9R1Z7; -.
DR   OMA; HKNLDKD; -.
DR   OrthoDB; EOG4V1722; -.
DR   PhylomeDB; Q9R1Z7; -.
DR   BRENDA; 4.2.3.12; 244.
DR   NextBio; 296210; -.
DR   ArrayExpress; Q9R1Z7; -.
DR   Bgee; Q9R1Z7; -.
DR   CleanEx; MM_PTS; -.
DR   Genevestigator; Q9R1Z7; -.
DR   GermOnline; ENSMUSG00000032067; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0003874; F:6-pyruvoyltetrahydropterin synthase activity; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
DR   GO; GO:0006729; P:tetrahydrobiopterin biosynthetic process; IDA:MGI.
DR   InterPro; IPR007116; 6-carboxy/6-PTP_synth.
DR   InterPro; IPR007115; 6-PTP_synth-rel.
DR   InterPro; IPR022470; PTPS_Cys_AS.
DR   InterPro; IPR022469; PTPS_His_AS.
DR   PANTHER; PTHR12589; 6_PTP_synth; 1.
DR   Pfam; PF01242; PTPS; 1.
DR   PIRSF; PIRSF006113; PTP_synth; 1.
DR   TIGRFAMs; TIGR00039; 6PTHBS; 1.
DR   PROSITE; PS00987; PTPS_1; 1.
DR   PROSITE; PS00988; PTPS_2; 1.
PE   2: Evidence at transcript level;
KW   Lyase; Metal-binding; Phosphoprotein;
KW   Tetrahydrobiopterin biosynthesis; Zinc.
FT   CHAIN         1    144       6-pyruvoyl tetrahydrobiopterin synthase.
FT                                /FTId=PRO_0000057915.
FT   ACT_SITE     42     42       Proton acceptor (By similarity).
FT   ACT_SITE     89     89       Charge relay system (By similarity).
FT   ACT_SITE    133    133       Charge relay system (By similarity).
FT   METAL        23     23       Zinc (By similarity).
FT   METAL        48     48       Zinc (By similarity).
FT   METAL        50     50       Zinc (By similarity).
FT   MOD_RES      18     18       Phosphoserine (By similarity).
FT   CONFLICT      6      6       D -> G (in Ref. 1; AAD15827).
SQ   SEQUENCE   144 AA;  16188 MW;  AAB034E27ED7A9E3 CRC64;
     MSAAGDLRRR ARLSRLVSFS ASHRLHSPSL SDEENLRVFG KCNNPNGHGH NYKVVVTVHG
     EIDPVTGMVM NLTDLKEYME EAIMKPLDHK NLDLDVPYFA DAVSTTENVA VYIWESLQKL
     LPVGALYKVK VFETDNNIVV YKGE
//
ID   VINEX_MOUSE             Reviewed;         733 AA.
AC   Q9R1Z8; Q62423;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Vinexin;
DE   AltName: Full=SH3 domain-containing protein SH3P3;
DE   AltName: Full=SH3-containing adapter molecule 1;
DE            Short=SCAM-1;
DE   AltName: Full=Sorbin and SH3 domain-containing protein 3;
GN   Name=Sorbs3; Synonyms=Scam1, Sh3d4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RX   MEDLINE=99102423; PubMed=9885244; DOI=10.1083/jcb.144.1.59;
RA   Kioka N., Sakata S., Kawauchi T., Amachi T., Akiyama S.K., Okazaki K.,
RA   Yaen C., Yamada K.M., Aota S.;
RT   "Vinexin: a novel vinculin-binding protein with multiple SH3 domains
RT   enhances actin cytoskeletal organization.";
RL   J. Cell Biol. 144:59-69(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 559-733.
RC   TISSUE=Embryo;
RX   MEDLINE=98294438; PubMed=9630982; DOI=10.1038/nbt0696-741;
RA   Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.;
RT   "Cloning of ligand targets: systematic isolation of SH3 domain-
RT   containing proteins.";
RL   Nat. Biotechnol. 14:741-744(1996).
RN   [3]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH DLG5.
RX   PubMed=12657639; DOI=10.1074/jbc.M211004200;
RA   Wakabayashi M., Ito T., Mitsushima M., Aizawa S., Ueda K., Amachi T.,
RA   Kioka N.;
RT   "Interaction of lp-dlg/KIAA0583, a membrane-associated guanylate
RT   kinase family protein, with vinexin and beta-catenin at sites of cell-
RT   cell contact.";
RL   J. Biol. Chem. 278:21709-21714(2003).
RN   [4]
RP   INTERACTION WITH SOCS7.
RX   PubMed=15242778; DOI=10.1016/j.yexcr.2004.04.002;
RA   Martens N., Wery M., Wang P., Braet F., Gertler A., Hooghe R.,
RA   Vandenhaute J., Hooghe-Peters E.L.;
RT   "The suppressor of cytokine signaling (SOCS)-7 interacts with the
RT   actin cytoskeleton through vinexin.";
RL   Exp. Cell Res. 298:239-248(2004).
CC   -!- FUNCTION: Promotes up-regulation of actin stress fiber formation.
CC   -!- SUBUNIT: Interacts with vinculin by the first two SH3 domains and
CC       the proline rich region of vinculin. Binds to SOS (guanine
CC       nucleotide exchange factor of RAS and RAC), through its third SH3
CC       domain. The formation of this complex is down-regulated by
CC       phosphorylation of SOS. Interacts with SAFB2, INPPL1/SHIP2 and
CC       SRCIN1 (By similarity). Interacts with DLG5 through its third SH3
CC       domain. Interacts with SOCS7. Interacts with FASLG (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion. Cell
CC       junction. Cell junction. Cytoplasm, cytoskeleton. Note=Localized
CC       at focal adhesion sites, cell-cell junctions and cell-
CC       extracellular matrix junctions.
CC   -!- SIMILARITY: Contains 3 SH3 domains.
CC   -!- SIMILARITY: Contains 1 SoHo domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AF064806; AAD32303.1; -; mRNA.
DR   EMBL; U58889; AAC52642.1; -; mRNA.
DR   IPI; IPI00129264; -.
DR   RefSeq; NP_035496.1; NM_011366.2.
DR   UniGene; Mm.5068; -.
DR   ProteinModelPortal; Q9R1Z8; -.
DR   SMR; Q9R1Z8; 447-589, 677-733.
DR   STRING; Q9R1Z8; -.
DR   PhosphoSite; Q9R1Z8; -.
DR   PRIDE; Q9R1Z8; -.
DR   Ensembl; ENSMUST00000022682; ENSMUSP00000022682; ENSMUSG00000022091.
DR   GeneID; 20410; -.
DR   KEGG; mmu:20410; -.
DR   UCSC; uc007unl.1; mouse.
DR   CTD; 20410; -.
DR   MGI; MGI:700013; Sorbs3.
DR   eggNOG; roNOG04673; -.
DR   GeneTree; ENSGT00550000074287; -.
DR   HOGENOM; HBG446972; -.
DR   HOVERGEN; HBG054842; -.
DR   InParanoid; Q9R1Z8; -.
DR   OMA; ATWTKDS; -.
DR   OrthoDB; EOG457563; -.
DR   PhylomeDB; Q9R1Z8; -.
DR   NextBio; 298392; -.
DR   ArrayExpress; Q9R1Z8; -.
DR   Bgee; Q9R1Z8; -.
DR   CleanEx; MM_SORBS3; -.
DR   Genevestigator; Q9R1Z8; -.
DR   GermOnline; ENSMUSG00000022091; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0008134; F:transcription factor binding; IPI:MGI.
DR   GO; GO:0031589; P:cell-substrate adhesion; IDA:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IGI:MGI.
DR   GO; GO:0043410; P:positive regulation of MAPKKK cascade; IDA:MGI.
DR   InterPro; IPR000108; p67phox.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR003127; Sorb.
DR   Pfam; PF00018; SH3_1; 2.
DR   Pfam; PF07653; SH3_2; 1.
DR   Pfam; PF02208; Sorb; 1.
DR   PRINTS; PR00499; P67PHOX.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 3.
DR   SMART; SM00459; Sorb; 1.
DR   SUPFAM; SSF50044; SH3; 3.
DR   PROSITE; PS50002; SH3; 3.
DR   PROSITE; PS50831; SOHO; 1.
PE   1: Evidence at protein level;
KW   Cell adhesion; Cell junction; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW   Repeat; SH3 domain.
FT   CHAIN         1    733       Vinexin.
FT                                /FTId=PRO_0000065831.
FT   DOMAIN      164    232       SoHo.
FT   DOMAIN      444    503       SH3 1.
FT   DOMAIN      518    579       SH3 2.
FT   DOMAIN      674    733       SH3 3.
FT   REGION      444    579       Binds to vinculin.
FT   REGION      674    733       Binds to SOS (By similarity).
FT   MOD_RES     275    275       Phosphoserine (By similarity).
FT   MOD_RES     412    412       Phosphoserine (By similarity).
FT   MOD_RES     459    459       Phosphoserine (By similarity).
FT   MOD_RES     594    594       Phosphoserine (By similarity).
FT   MOD_RES     624    624       Phosphoserine (By similarity).
SQ   SEQUENCE   733 AA;  82349 MW;  D7716FA1D4F0E3CE CRC64;
     MARILGVGRS SASSLNNKED NESDVALLSP KDPNRVHTKE QLAHPASSNL DPSMQGLPAG
     LSLDDFIPGH LRTHIGSSSR GTRVPVIRNG GSNTLNFQFH DPAPRTVCNG CPPPRRDGSL
     NPDPAWYQTW PGPGSRPSMS PKPPASQHAQ NWSATWTKDS KRQDKRWVKY EGIGPVDESG
     MPIAPRSSVD SPRDWYRRMF QQIHRKMPDL QLDWTLEDPP KVVSARASSA EPRHLGTLQR
     PASRPGTTET SSGRNWNHSE ETSRNTFNYN FRPSSSGLHP PNQVPRHREK VENVWTEDSW
     NQFLHELETG HKPKKPLVDD PVEKPAQPIE VLLERELAKL SAELDKDLRA IETRLPSPKN
     SQAPRRPLEQ PGLEQQPSAR LSSAWRPNSP HAPYFSSSRP LSPHRMADGG GSPFLGRRDF
     VYPSSAREPS ASERGSSPSR KEEKKRKAAR LKFDFQAQSP KELSLQKGDI VYIHKEVDKN
     WLEGEHHGRL GIFPANYVEV LPADEIPKPI KPPTYQVLEY GDAVAQYTFK GDLEVELSFR
     KGERICLIRK VNEHWYEGRI TGTGRQGIFP ASYVQINREP RLRLCDDGPQ LPASPNPTTT
     AHLSSHSHPS SIPVDPTDWG GRTSPRRSAF PFPITLQEPR SQTQSLNTPG PTLSHPRATS
     RPINLGPSSP NTEIHWTPYR AMYQYRPQNE DELELREGDR VDVMQQCDDG WFVGVSRRTQ
     KFGTFPGNYV APV
//
ID   HEBP1_MOUSE             Reviewed;         190 AA.
AC   Q9R257; O88814;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Heme-binding protein 1;
DE   AltName: Full=p22HBP;
GN   Name=Hebp1; Synonyms=Hbp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   MEDLINE=99030414; PubMed=9813049; DOI=10.1074/jbc.273.47.31388;
RA   Taketani S., Adachi Y., Kohno H., Ikehara S., Tokunaga R., Ishii T.;
RT   "Molecular characterizatin of a newly identified heme-binding protein
RT   induced during differentiation of Murine erythroleukemia cells.";
RL   J. Biol. Chem. 273:31388-31394(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20109330; PubMed=10640688; DOI=10.1016/S0169-328X(99)00277-6;
RA   Zylka M.J., Reppert S.M.;
RT   "Discovery of a putative heme-binding protein family (SOUL/HBP) by
RT   two-tissue suppression subtractive hybridization and database
RT   searches.";
RL   Brain Res. Mol. Brain Res. 74:175-181(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   SUBUNIT.
RC   TISSUE=Liver;
RX   MEDLINE=22301044; PubMed=12413491; DOI=10.1016/S0003-9861(02)00471-X;
RA   Jacob Blackmon B., Dailey T.A., Lianchun X., Dailey H.A.;
RT   "Characterization of a human and mouse tetrapyrrole-binding protein.";
RL   Arch. Biochem. Biophys. 407:196-201(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E.,
RA   Mollenhauer J., Wiemann S., Schick M., Korn B.;
RT   "Cloning of mouse full open reading frames in Gateway(R) system entry
RT   vector (pDONR201).";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May act in the binding of free porphyrinogens that may
CC       be present in the cell and thus facilitate removal of these
CC       potentially toxic compound. Binds with a high affinity to one
CC       molecule of heme or porphyrins. It binds metalloporphyrins, free
CC       porphyrins and N-methylprotoporphyrin with similar affinities.
CC   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed. Extremely abundant in
CC       liver.
CC   -!- SIMILARITY: Belongs to the HEBP family.
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DR   EMBL; AB013095; BAA33770.1; -; mRNA.
DR   EMBL; AF117613; AAD32096.1; -; mRNA.
DR   EMBL; CT010262; CAJ18470.1; -; mRNA.
DR   EMBL; BC012654; AAH12654.1; -; mRNA.
DR   IPI; IPI00135085; -.
DR   UniGene; Mm.378937; -.
DR   PDB; 2GOV; NMR; -; A=7-190.
DR   PDB; 2HVA; NMR; -; A=1-190.
DR   PDBsum; 2GOV; -.
DR   PDBsum; 2HVA; -.
DR   ProteinModelPortal; Q9R257; -.
DR   SMR; Q9R257; 1-190.
DR   STRING; Q9R257; -.
DR   PhosphoSite; Q9R257; -.
DR   PRIDE; Q9R257; -.
DR   Ensembl; ENSMUST00000045855; ENSMUSP00000042232; ENSMUSG00000042770.
DR   UCSC; uc009elh.1; mouse.
DR   MGI; MGI:1333880; Hebp1.
DR   eggNOG; roNOG06539; -.
DR   GeneTree; ENSGT00530000063312; -.
DR   HOGENOM; HBG717396; -.
DR   HOVERGEN; HBG053223; -.
DR   InParanoid; Q9R257; -.
DR   OrthoDB; EOG480HXP; -.
DR   ArrayExpress; Q9R257; -.
DR   Bgee; Q9R257; -.
DR   CleanEx; MM_HEBP1; -.
DR   Genevestigator; Q9R257; -.
DR   GermOnline; ENSMUSG00000042770; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0020037; F:heme binding; IDA:MGI.
DR   GO; GO:0042168; P:heme metabolic process; IC:MGI.
DR   InterPro; IPR011256; Reg_factor_effector_bac.
DR   InterPro; IPR006917; SOUL_haem-bd.
DR   PANTHER; PTHR11220; SOUL_heme_bd; 1.
DR   Pfam; PF04832; SOUL; 1.
DR   SUPFAM; SSF55136; Bac_reg_effector; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm.
FT   CHAIN         1    190       Heme-binding protein 1.
FT                                /FTId=PRO_0000116898.
FT   STRAND       19     23
FT   STRAND       27     29
FT   STRAND       31     35
FT   STRAND       40     49
FT   HELIX        51     67
FT   STRAND       82     88
FT   STRAND       94    102
FT   HELIX       106    110
FT   STRAND      117    119
FT   STRAND      121    124
FT   STRAND      129    137
FT   HELIX       141    154
FT   TURN        155    157
FT   STRAND      162    173
FT   STRAND      176    179
FT   STRAND      182    189
SQ   SEQUENCE   190 AA;  21053 MW;  DCCB8DDD8A461009 CRC64;
     MLGMIRNSLF GSVETWPWQV LSTGGKEDVS YEERACEGGK FATVEVTDKP VDEALREAMP
     KIMKYVGGTN DKGVGMGMTV PVSFAVFPNE DGSLQKKLKV WFRIPNQFQG SPPAPSDESV
     KIEEREGITV YSTQFGGYAK EADYVAHATQ LRTTLEGTPA TYQGDVYYCA GYDPPMKPYG
     RRNEVWLVKA
//
ID   STK11_MOUSE             Reviewed;         436 AA.
AC   Q9WTK7; Q3TAE0;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 89.
DE   RecName: Full=Serine/threonine-protein kinase 11;
DE            EC=2.7.11.1;
DE   AltName: Full=Serine/threonine-protein kinase LKB1;
GN   Name=Stk11; Synonyms=Lkb1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DEVELOPMENTAL STAGE.
RX   PubMed=10381580; DOI=10.1016/S0925-4773(99)00050-7;
RA   Luukko K., Ylikorkala A., Tiainen M., Makela T.P.;
RT   "Expression of LKB1 and PTEN tumor suppressor genes during mouse
RT   embryonic development.";
RL   Mech. Dev. 83:187-190(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=129;
RX   MEDLINE=99330555; PubMed=10400995; DOI=10.1093/hmg/8.8.1479;
RA   Smith D.P., Spicer J., Smith A., Swift S., Ashworth A.;
RT   "The mouse Peutz-Jeghers syndrome gene Lkb1 encodes a nuclear protein
RT   kinase.";
RL   Hum. Mol. Genet. 8:1479-1485(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=20115103; PubMed=10642527; DOI=10.1042/0264-6021:3450673;
RA   Collins S.P., Reoma J.L., Gamm D.M., Uhler M.D.;
RT   "LKB1, a novel serine/threonine protein kinase and potential tumour
RT   suppressor, is phosphorylated by cAMP-dependent protein kinase (PKA)
RT   and prenylated in vivo.";
RL   Biochem. J. 345:673-680(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=Swiss Webster / NIH; TISSUE=Embryo;
RX   PubMed=12060709; DOI=10.1073/pnas.122254599;
RA   Jishage K., Nezu J., Kawase Y., Iwata T., Watanabe M., Miyoshi A.,
RA   Ose A., Habu K., Kake T., Kamada N., Ueda O., Kinoshita M.,
RA   Jenne D.E., Shimane M., Suzuki H.;
RT   "Role of Lkb1, the causative gene of Peutz-Jegher's syndrome, in
RT   embryogenesis and polyposis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:8903-8908(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=NOD; TISSUE=Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Essential role in G1 cell cycle arrest. Phosphorylates
CC       and activates members of the AMPK-related subfamily of protein
CC       kinases (By similarity). Tumor suppressor.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium or Manganese (By similarity).
CC   -!- ENZYME REGULATION: Activated by binding of a complex consisting of
CC       CAB39 and STRAD or CAB39 and ALS2CR2 (By similarity).
CC   -!- SUBUNIT: Found in a ternary complex composed of SMAD4, STK11 and
CC       STK11IP. Interacts with SMAD4, STK11IP and WDR6 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Relocates to the
CC       cytoplasm when bound to CAB39 and STRAD or CAB39 and ALS2CR2.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9WTK7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9WTK7-2; Sequence=VSP_052222, VSP_052223;
CC         Note=No experimental confirmation available;
CC   -!- DEVELOPMENTAL STAGE: Ubiquitously expressed 7-11 dpc. Present in
CC       nucleated embryonic blood cells from 9 dpc. Restricted to
CC       gastrointestinal tract, testis and lung from days 15-19 dpc.
CC   -!- DISRUPTION PHENOTYPE: Mice die in utero 8.5 to 9.5 dpc due to
CC       developmental retardation. Heterozygous mice develop multiple
CC       gastric adenomatous polyps.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. LKB1 subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF129870; AAD22100.1; -; mRNA.
DR   EMBL; AF145287; AAD31044.1; -; mRNA.
DR   EMBL; AF145296; AAD55368.1; -; Genomic_DNA.
DR   EMBL; AF145288; AAD55368.1; JOINED; Genomic_DNA.
DR   EMBL; AF145289; AAD55368.1; JOINED; Genomic_DNA.
DR   EMBL; AF145290; AAD55368.1; JOINED; Genomic_DNA.
DR   EMBL; AF145291; AAD55368.1; JOINED; Genomic_DNA.
DR   EMBL; AF145292; AAD55368.1; JOINED; Genomic_DNA.
DR   EMBL; AF145293; AAD55368.1; JOINED; Genomic_DNA.
DR   EMBL; AF145294; AAD55368.1; JOINED; Genomic_DNA.
DR   EMBL; AF145295; AAD55368.1; JOINED; Genomic_DNA.
DR   EMBL; AF151711; AAF21370.1; -; mRNA.
DR   EMBL; AB015801; BAA76749.1; -; mRNA.
DR   EMBL; AK171909; BAE42728.1; -; mRNA.
DR   EMBL; AK172528; BAE43050.1; -; mRNA.
DR   EMBL; AK172385; BAE42977.1; -; mRNA.
DR   EMBL; BC052379; AAH52379.1; -; mRNA.
DR   IPI; IPI00123476; -.
DR   IPI; IPI00652225; -.
DR   RefSeq; NP_035622.1; NM_011492.3.
DR   UniGene; Mm.135645; -.
DR   HSSP; P06782; 2FH9.
DR   ProteinModelPortal; Q9WTK7; -.
DR   SMR; Q9WTK7; 45-342.
DR   STRING; Q9WTK7; -.
DR   PhosphoSite; Q9WTK7; -.
DR   PRIDE; Q9WTK7; -.
DR   Ensembl; ENSMUST00000003152; ENSMUSP00000003152; ENSMUSG00000003068.
DR   Ensembl; ENSMUST00000099495; ENSMUSP00000097094; ENSMUSG00000003068.
DR   GeneID; 20869; -.
DR   KEGG; mmu:20869; -.
DR   UCSC; uc007gbu.1; mouse.
DR   CTD; 20869; -.
DR   MGI; MGI:1341870; Stk11.
DR   eggNOG; roNOG13815; -.
DR   GeneTree; ENSGT00530000063214; -.
DR   HOGENOM; HBG446083; -.
DR   HOVERGEN; HBG054467; -.
DR   InParanoid; Q9WTK7; -.
DR   OMA; DTKDRWR; -.
DR   OrthoDB; EOG49CQ7R; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 299701; -.
DR   ArrayExpress; Q9WTK7; -.
DR   Bgee; Q9WTK7; -.
DR   CleanEx; MM_STK11; -.
DR   Genevestigator; Q9WTK7; -.
DR   GermOnline; ENSMUSG00000003068; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0030275; F:LRR domain binding; IPI:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0060070; P:canonical Wnt receptor signaling pathway; IMP:MGI.
DR   GO; GO:0007050; P:cell cycle arrest; ISS:UniProtKB.
DR   GO; GO:0060770; P:negative regulation of epithelial cell proliferation involved in prostate gland development; IMP:MGI.
DR   GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0051896; P:regulation of protein kinase B signaling cascade; IMP:MGI.
DR   GO; GO:0030111; P:regulation of Wnt receptor signaling pathway; IMP:MGI.
DR   GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell cycle; Cytoplasm; Kinase;
KW   Magnesium; Manganese; Metal-binding; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    436       Serine/threonine-protein kinase 11.
FT                                /FTId=PRO_0000260032.
FT   DOMAIN       49    309       Protein kinase.
FT   NP_BIND      55     63       ATP (By similarity).
FT   ACT_SITE    176    176       Proton acceptor (By similarity).
FT   BINDING      78     78       ATP (By similarity).
FT   MOD_RES      31     31       Phosphoserine.
FT   MOD_RES     336    336       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     366    366       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     431    431       Phosphoserine; by PKA (By similarity).
FT   VAR_SEQ     374    415       QVLEEEVGQNGQSHSLPKAVCVNGTEPQLSSKVKPEGRPGT
FT                                A -> VEEAAEAGLSEDACDTCMWKSQGAGLPGEEPEEGFG
FT                                ALV (in isoform 2).
FT                                /FTId=VSP_052222.
FT   VAR_SEQ     416    436       Missing (in isoform 2).
FT                                /FTId=VSP_052223.
FT   CONFLICT     95     95       V -> L (in Ref. 2; BAE42728).
SQ   SEQUENCE   436 AA;  49267 MW;  CCD9BCF94CF5CC9C CRC64;
     MDVADPEPLG LFSEGELMSV GMDTFIHRID STEVIYQPRR KRAKLIGKYL MGDLLGEGSY
     GKVKEVLDSE TLCRRAVKIL KKKKLRRIPN GEANVKKEIQ LLRRLRHRNV IQLVDVLYNE
     EKQKMYMVME YCVCGMQEML DSVPEKRFPV CQAHGYFRQL IDGLEYLHSQ GIVHKDIKPG
     NLLLTTNGTL KISDLGVAEA LHPFAVDDTC RTSQGSPAFQ PPEIANGLDT FSGFKVDIWS
     AGVTLYNITT GLYPFEGDNI YKLFENIGRG DFTIPCDCGP PLSDLLRGML EYEPAKRFSI
     RQIRQHSWFR KKHPLAEALV PIPPSPDTKD RWRSMTVVPY LEDLHGRAEE EEEEDLFDIE
     DGIIYTQDFT VPGQVLEEEV GQNGQSHSLP KAVCVNGTEP QLSSKVKPEG RPGTANPARK
     VCSSNKIRRL SACKQQ
//
ID   SPY4_MOUSE              Reviewed;         300 AA.
AC   Q9WTP2; Q543R1; Q9QXV7;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Protein sprouty homolog 4;
DE            Short=Spry-4;
GN   Name=Spry4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX   MEDLINE=99264295; PubMed=10330503; DOI=10.1016/S0925-4773(98)00241-X;
RA   de Maximy A.A., Nakatake Y., Moncada S., Itoh N., Thiery J.P.,
RA   Bellusci S.;
RT   "Cloning and expression pattern of a mouse homologue of Drosophila
RT   sprouty in the mouse embryo.";
RL   Mech. Dev. 81:213-216(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99429807; PubMed=10498682;
RA   Minowada G., Jarvis L.A., Chi C.L., Neubueser A., Sun X., Hacohen N.,
RA   Krasnow M.A., Martin G.R.;
RT   "Vertebrate sprouty genes are induced by FGF signaling and can cause
RT   chondrodysplasia when overexpressed.";
RL   Development 126:4465-4475(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, and Skin;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Suppresses the insulin receptor and EGFR-transduced MAPK
CC       signaling pathway, but does not inhibit MAPK activation by a
CC       constitutively active mutant Ras. Probably impairs the formation
CC       of GTP-Ras (By similarity).
CC   -!- SUBUNIT: Interacts with the C-terminus of TESK1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC       protein. Note=Found in the cytoplasm in unstimulated cells but is
CC       translocated to the membrane ruffles in cells stimulated with EGF
CC       (epidermal growth factor).
CC   -!- TISSUE SPECIFICITY: Expressed in the embryo and adult tissues
CC       including heart, brain, lung, kidney, and skeletal muscle.
CC   -!- DEVELOPMENTAL STAGE: At 8 dpc expressed in the lateral plate
CC       mesoderm of the primitive streak. At 9.5 and 10.5 dpc expressed in
CC       the nasal placodes, maxillary and mandibular processes, posterior
CC       part of the hyoid arch and the progress zone of the limb buds and
CC       the presomitic mesoderm. At 11.5 dpc expressed in the dorso-
CC       lateral region of the somites (mostly in the myotome) and in the
CC       otic vesicle. At 11.5 and 12.5 dpc expressed in the distal lung
CC       mesenchyme, with a strong expression in the accessory lobe of the
CC       lung.
CC   -!- INDUCTION: By FGF signaling.
CC   -!- DOMAIN: The Cys-rich domain is responsible for the localization of
CC       the protein to the membrane ruffles.
CC   -!- SIMILARITY: Belongs to the sprouty family.
CC   -!- SIMILARITY: Contains 1 SPR (sprouty) domain.
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DR   EMBL; AB019280; BAA77689.1; -; mRNA.
DR   EMBL; AF176906; AAD56007.1; -; mRNA.
DR   EMBL; AK037180; BAC29739.1; -; mRNA.
DR   EMBL; AK048122; BAC33249.1; -; mRNA.
DR   EMBL; CH466528; EDL10072.1; -; Genomic_DNA.
DR   EMBL; BC050944; AAH50944.1; -; mRNA.
DR   EMBL; BC057005; AAH57005.1; -; mRNA.
DR   IPI; IPI00322677; -.
DR   RefSeq; NP_036028.2; NM_011898.2.
DR   UniGene; Mm.42038; -.
DR   ProteinModelPortal; Q9WTP2; -.
DR   STRING; Q9WTP2; -.
DR   PhosphoSite; Q9WTP2; -.
DR   PRIDE; Q9WTP2; -.
DR   Ensembl; ENSMUST00000025295; ENSMUSP00000025295; ENSMUSG00000024427.
DR   GeneID; 24066; -.
DR   KEGG; mmu:24066; -.
DR   UCSC; uc008esl.1; mouse.
DR   CTD; 24066; -.
DR   MGI; MGI:1345144; Spry4.
DR   GeneTree; ENSGT00390000003535; -.
DR   HOGENOM; HBG444143; -.
DR   HOVERGEN; HBG003544; -.
DR   InParanoid; Q9WTP2; -.
DR   OMA; CYLPATG; -.
DR   OrthoDB; EOG4THVTX; -.
DR   PhylomeDB; Q9WTP2; -.
DR   NextBio; 304037; -.
DR   ArrayExpress; Q9WTP2; -.
DR   Bgee; Q9WTP2; -.
DR   CleanEx; MM_SPRY4; -.
DR   Genevestigator; Q9WTP2; -.
DR   GermOnline; ENSMUSG00000024427; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:MGI.
DR   InterPro; IPR007875; Sprouty.
DR   Pfam; PF05210; Sprouty; 1.
DR   PROSITE; PS51227; SPR; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Developmental protein; Membrane; Phosphoprotein.
FT   CHAIN         1    300       Protein sprouty homolog 4.
FT                                /FTId=PRO_0000076906.
FT   DOMAIN      167    274       SPR.
FT   COMPBIAS     98    108       Poly-Ser.
FT   COMPBIAS    160    284       Cys-rich.
FT   MOD_RES      53     53       Phosphotyrosine (By similarity).
FT   MOD_RES     126    126       Phosphoserine (By similarity).
FT   CONFLICT     10     10       V -> F (in Ref. 2; AAD56007).
SQ   SEQUENCE   300 AA;  32523 MW;  DA963036EFC0E73F CRC64;
     MEPPVPQSSV PVNPSSVMVQ PLLDSRAPHS RLQHPLTILP IDQMKTSHVE NDYIDNPSLA
     PATGPKRPRG GPPELAPTPA RCDQDITHHW ISFSGRPSSV SSSSSTSSDQ RLLDHMAPPP
     VAEQASPRAV RLQPKVVHCK PLDLKGPTAP PELDKHFLLC EACGKCKCKE CASPRTLPSC
     WVCNQECLCS AQTLVNYGTC MCLVQGIFYH CTNEDDEGSC ADHPCSCSGS NCCARWSFMG
     ALSVVLPCLL CYLPATGCVK LAQRGYDRLR RPGCRCKHTN SVICKAASGD TKTSRSDKPF
//
ID   CAD22_MOUSE             Reviewed;         813 AA.
AC   Q9WTP5;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Cadherin-22;
DE   AltName: Full=Pituitary and brain cadherin;
DE            Short=PB-cadherin;
DE   Flags: Precursor;
GN   Name=Cdh22;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=99326347; PubMed=10398531;
RX   DOI=10.1002/(SICI)1097-0177(199907)215:3<206::AID-AJA3>3.3.CO;2-O;
RA   Kitajima K., Koshimizu U., Nakamura T.;
RT   "Expression of a novel type of classic cadherin, PB-cadherin in
RT   developing brain and limb buds.";
RL   Dev. Dyn. 215:206-214(1999).
CC   -!- FUNCTION: Cadherins are calcium dependent cell adhesion proteins.
CC       They preferentially interact with themselves in a homophilic
CC       manner in connecting cells; cadherins may thus contribute to the
CC       sorting of heterogeneous cell types. PB-cadherins may have a role
CC       in the morphological organization of pituitary gland and brain
CC       tissues.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in brain. Abundant in
CC       olfactory bulb, cerebrum, and cerebellum, less in pons, medulla,
CC       and spinal cord. Low expression in heart. No expression in lung,
CC       liver, spleen, kidney, testis, stomach, intestine, colon, and
CC       placenta.
CC   -!- DEVELOPMENTAL STAGE: Expressed at 9.5 dpc onwards. At 10.5 dpc, in
CC       brain (telencephalic vesicles and isthmus), spinal cord and limb
CC       buds (in the zone of polarizing activity). At 14.5 dpc, in
CC       olfactory bulb and cerebellum.
CC   -!- INDUCTION: Down-regulated by thyroid hormone.
CC   -!- SIMILARITY: Contains 5 cadherin domains.
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DR   EMBL; AB019618; BAA34426.1; -; mRNA.
DR   IPI; IPI00123678; -.
DR   UniGene; Mm.151819; -.
DR   ProteinModelPortal; Q9WTP5; -.
DR   SMR; Q9WTP5; 60-604, 727-804.
DR   STRING; Q9WTP5; -.
DR   PhosphoSite; Q9WTP5; -.
DR   PRIDE; Q9WTP5; -.
DR   Ensembl; ENSMUST00000065438; ENSMUSP00000066864; ENSMUSG00000053166.
DR   UCSC; uc008nxc.1; mouse.
DR   MGI; MGI:1341843; Cdh22.
DR   eggNOG; maNOG17836; -.
DR   GeneTree; ENSGT00600000084132; -.
DR   HOGENOM; HBG505775; -.
DR   HOVERGEN; HBG005217; -.
DR   InParanoid; Q9WTP5; -.
DR   OrthoDB; EOG49S65V; -.
DR   ArrayExpress; Q9WTP5; -.
DR   Bgee; Q9WTP5; -.
DR   CleanEx; MM_CDH22; -.
DR   Genevestigator; Q9WTP5; -.
DR   GermOnline; ENSMUSG00000053166; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 5.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF01049; Cadherin_C; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 5.
DR   SUPFAM; SSF49313; Cadherin; 5.
DR   PROSITE; PS00232; CADHERIN_1; 2.
DR   PROSITE; PS50268; CADHERIN_2; 5.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     33       Potential.
FT   CHAIN        34    813       Cadherin-22.
FT                                /FTId=PRO_0000003822.
FT   TOPO_DOM     34    621       Extracellular (Potential).
FT   TRANSMEM    622    642       Helical; (Potential).
FT   TOPO_DOM    643    813       Cytoplasmic (Potential).
FT   DOMAIN       61    165       Cadherin 1.
FT   DOMAIN      166    274       Cadherin 2.
FT   DOMAIN      275    391       Cadherin 3.
FT   DOMAIN      392    495       Cadherin 4.
FT   DOMAIN      496    613       Cadherin 5.
FT   CARBOHYD    159    159       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    463    463       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    609    609       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   813 AA;  88022 MW;  5510F9848D976567 CRC64;
     MRPRPEGALR AGAALSPVLL FLLLLPLLGH LWAASTPAPS SLSPGAQEDN QLGAGRVKRG
     WVWNQFFVVE EYTGTEPLYV GKIHSDSDEG DGTIKYTISG EGAGTIFLID ELTGDIHATE
     RLDREQKTFY TLRAQARDRA TNRLLEPESE FIIKVQDIND SEPRFLHGPY IGSVAELSPT
     GTSVMQVMAS DADDPTYGRS ARLVYSVLDG EHHFTVDPKT GVIRTAVPDL DRESQERYEV
     VIQATDMAGQ LGGLSGSTTV TIVVTDVNDN PPRFPQKMYQ FSIQESAPIG TAVGRVKAED
     SDVGENTDMT YHLREESGSG GDAFKVTTDS DTQEAIIVVQ KHLDFESQQV HTVVLEALNK
     FVDPRFADLG TFRDQAIVRV AVTDVDEPPE FRPPSGLLEV QEDAQVGSLV GVVTARDPDA
     ANRPVRYAID RDSDLEQIFD IDADTGAIVT GKGLDRETAG WHNITVLAME ADNHAQLSRA
     SLRIRILDVN DNPPELATPY EAAVCEDAKP GQLIQTISVV DRDEPQGGHR FYFRLVPEAP
     SNPHFSLLDI EDNTAAVHTQ HVGFNRQEQD VFLLPILVVD SGPPTLSSTG TLTIRICGCD
     SSGTIQSCNT TAFVMAASLS PGALIALLVC VLILVVLALL ILTLRRHHKS HLSSDVDEDM
     RDNVIKYNDE GGGEQDTEAY DMSALRSLYD FGELKGGDPG GGAASPPQAA SSSERHSLPR
     GPSSPEPDFS VFRDFISRKV ALADADLSVP PYDAFQTYAF EGAGSPAASL SSLHSGSTGS
     EQDFAFLRAW GPRFRPLAAL YAGHRGDDEA PAS
//
ID   AKA12_MOUSE             Reviewed;        1684 AA.
AC   Q9WTQ5; Q80SS4; Q810D4; Q8BPK4; Q99MP1;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=A-kinase anchor protein 12;
DE            Short=AKAP-12;
DE   AltName: Full=Germ cell lineage protein gercelin;
DE   AltName: Full=Src-suppressed C kinase substrate;
DE            Short=SSeCKS;
GN   Name=Akap12; Synonyms=Gag12, Ssecks;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   MEDLINE=21322683; PubMed=11429284; DOI=10.1016/S0925-4773(01)00384-7;
RA   Camus A., Mesbah K., Rallu M., Babinet C., Barra J.;
RT   "Gene trap insertion reveals two open reading frames in the mouse
RT   SSeCKS gene: the form predominantly detected in the nervous system is
RT   suppressed by the insertion while the other, specific of the testis,
RT   remains expressed.";
RL   Mech. Dev. 105:79-91(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Testis;
RX   MEDLINE=21657320; PubMed=11799143;
RA   Kitamura H., Okita K., Fujikura D., Mori K., Iwanaga T., Saito M.;
RT   "Induction of Src-suppressed C kinase substrate (SSeCKS) in vascular
RT   endothelial cells by bacterial lipopolysaccharide.";
RL   J. Histochem. Cytochem. 50:245-255(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RA   Nishina Y., Motoda Y.;
RT   "Mouse testicular cell specific gene, GAG12.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RA   Tsuchida J., Tanaka H., Yomogida K., Nozaki M., Maeda N., Matsui Y.,
RA   Nishimune Y.;
RT   "Molecular cloning and characterization of the mouse germ cell lineage
RT   protein cDNA, gercelin, encoding the cytoplasmic AKAP, Gercelin /
RT   SSeCKS and the potential germ cell-specific nuclear antigen, GENA.";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-605 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 139-1684 (ISOFORMS 1/2).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; SER-22 AND SER-584,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631; THR-632; SER-634;
RP   SER-682; SER-683 AND SER-684, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543; SER-598; SER-613;
RP   SER-615; SER-682; SER-683 AND SER-684, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-353, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Anchoring protein that mediates the subcellular
CC       compartmentation of protein kinase A (PKA) and protein kinase C
CC       (PKC) (By similarity).
CC   -!- SUBUNIT: Binds to dimeric RII-alpha regulatory subunit of PKC (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Alpha;
CC         IsoId=Q9WTQ5-1; Sequence=Displayed;
CC       Name=2; Synonyms=Gamma;
CC         IsoId=Q9WTQ5-2; Sequence=VSP_028135;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is predominantly found in the
CC       nervous system. Isoform 3 is testis specific.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Contains 3 AKAP domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC66465.1; Type=Frameshift; Positions=28, 43;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF326228; AAK16150.1; -; mRNA.
DR   EMBL; AF326230; AAK16152.1; -; mRNA.
DR   EMBL; AB020886; BAA76894.1; -; mRNA.
DR   EMBL; AB025278; BAC66465.1; ALT_FRAME; mRNA.
DR   EMBL; AB051563; BAB72161.1; -; mRNA.
DR   EMBL; AB070852; BAB72164.1; -; mRNA.
DR   EMBL; AB070853; BAB72165.1; -; mRNA.
DR   EMBL; AK053844; BAC35553.1; -; mRNA.
DR   EMBL; BC042461; AAH42461.1; -; mRNA.
DR   EMBL; BC043939; AAH43939.1; -; mRNA.
DR   IPI; IPI00123709; -.
DR   IPI; IPI00867770; -.
DR   RefSeq; NP_112462.1; NM_031185.3.
DR   UniGene; Mm.27481; -.
DR   ProteinModelPortal; Q9WTQ5; -.
DR   IntAct; Q9WTQ5; 11.
DR   STRING; Q9WTQ5; -.
DR   PhosphoSite; Q9WTQ5; -.
DR   PRIDE; Q9WTQ5; -.
DR   Ensembl; ENSMUST00000045730; ENSMUSP00000035829; ENSMUSG00000038587.
DR   GeneID; 83397; -.
DR   KEGG; mmu:83397; -.
DR   CTD; 83397; -.
DR   MGI; MGI:1932576; Akap12.
DR   GeneTree; ENSGT00550000074593; -.
DR   HOGENOM; HBG125028; -.
DR   HOVERGEN; HBG050472; -.
DR   InParanoid; Q9WTQ5; -.
DR   OMA; DSDKEMA; -.
DR   OrthoDB; EOG408N80; -.
DR   PhylomeDB; Q9WTQ5; -.
DR   NextBio; 350523; -.
DR   ArrayExpress; Q9WTQ5; -.
DR   Bgee; Q9WTQ5; -.
DR   CleanEx; MM_AKAP12; -.
DR   Genevestigator; Q9WTQ5; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0030159; F:receptor signaling complex scaffold activity; TAS:MGI.
DR   GO; GO:0006605; P:protein targeting; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; TAS:MGI.
DR   InterPro; IPR001573; Pkinase-A_anch_WSK-motif.
DR   InterPro; IPR018459; RII_binding_1.
DR   Pfam; PF10522; RII_binding_1; 1.
DR   Pfam; PF03832; WSK; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Cytoskeleton; Phosphoprotein; Repeat.
FT   CHAIN         1   1684       A-kinase anchor protein 12.
FT                                /FTId=PRO_0000304941.
FT   DOMAIN      590    620       AKAP 1.
FT   DOMAIN      737    767       AKAP 2.
FT   DOMAIN      778    808       AKAP 3.
FT   REGION      253    543       Involved in PKC-binding (By similarity).
FT   REGION     1501   1514       RII-binding (By similarity).
FT   MOD_RES      18     18       Phosphoserine.
FT   MOD_RES      22     22       Phosphoserine.
FT   MOD_RES     270    270       Phosphoserine (By similarity).
FT   MOD_RES     272    272       Phosphothreonine (By similarity).
FT   MOD_RES     273    273       Phosphoserine (By similarity).
FT   MOD_RES     299    299       Phosphoserine (By similarity).
FT   MOD_RES     353    353       Phosphotyrosine.
FT   MOD_RES     467    467       Phosphoserine.
FT   MOD_RES     489    489       Phosphoserine (By similarity).
FT   MOD_RES     540    540       Phosphoserine (By similarity).
FT   MOD_RES     543    543       Phosphoserine.
FT   MOD_RES     551    551       Phosphoserine (By similarity).
FT   MOD_RES     552    552       Phosphoserine (By similarity).
FT   MOD_RES     554    554       Phosphoserine (By similarity).
FT   MOD_RES     555    555       Phosphoserine (By similarity).
FT   MOD_RES     583    583       Phosphothreonine (By similarity).
FT   MOD_RES     584    584       Phosphoserine.
FT   MOD_RES     598    598       Phosphoserine.
FT   MOD_RES     613    613       Phosphoserine.
FT   MOD_RES     615    615       Phosphoserine.
FT   MOD_RES     628    628       Phosphothreonine (By similarity).
FT   MOD_RES     630    630       Phosphoserine (By similarity).
FT   MOD_RES     631    631       Phosphoserine.
FT   MOD_RES     632    632       Phosphothreonine.
FT   MOD_RES     634    634       Phosphoserine.
FT   MOD_RES     637    637       Phosphoserine (By similarity).
FT   MOD_RES     682    682       Phosphoserine.
FT   MOD_RES     683    683       Phosphoserine.
FT   MOD_RES     684    684       Phosphoserine.
FT   MOD_RES    1094   1094       Phosphothreonine (By similarity).
FT   MOD_RES    1351   1351       Phosphoserine (By similarity).
FT   MOD_RES    1355   1355       Phosphoserine (By similarity).
FT   VAR_SEQ       1    105       Missing (in isoform 2).
FT                                /FTId=VSP_028135.
SQ   SEQUENCE   1684 AA;  180695 MW;  E569D55762FCB19E CRC64;
     MGAGSSTEQR SPEQPAESDT PSELELSGHG PAAEASGAAG DPADADPATK LPQKNGQLSA
     VNGVAEQEDV HVQEESQDGQ EEEVTVEDVG QRESEDVKEK DRAKEMAASS TVVEDITKDE
     QEETPEIIEQ IPASESNVEE MAQAAESQAN DVGFKKVFKF VGFKFTVKKD KNEKSDTVQL
     LTVKKDEGEG AEASVGAGDH QEPGVETVGE SASKESELKQ STEKQEGTLK QAQSSTEIPL
     QAESGQGTEE EAAKDGEENR EKEPTKPLES PTSPVSNETT SSFKKFFTHG WAGWRKKTSF
     KKPKEDDLET SEKRKEQEAE KVDEEEGEKT EPAPAEEQEP AEGTDQARLS ADYEKVELPL
     EDQVGDLEAL SEKCAPLATE VFDEKTEAHQ EVVAEVHVST VEKMTKGQGG AEVEGDVVVE
     GSGESLPPEK LAETQEVPQE AEPVEELMKT KEVCVSGGDH TQLTDLSPEE KMLPKHPEGI
     VSEVEMLSSQ ERIKVQGSPL KKLFSSSGLK KLSGKKQKGK RGGGGGDEEP GEYQHIQTES
     PESADEQKGE SSASSPEEPE EIACLEKGPS EAPQEAEAEE GATSDGEKKR EGITPWASFK
     KMVTPKKRVR RPSESDKEEE LDKVKSATLS STESTASGMQ DEVRAVGEEQ RSEEPKRRVD
     TSVSWEALIC VGSSKKRARK ASSSDDEGGP RTLGGDGHRA EEASKDKEAD ALPASTQEQD
     QAHGSSSPEP AGSPSEGEGV STWESFKRLV TPRKKSKSKL EERAEDSGAE QLASEIEPSR
     EESWVSIKKF IPGRRKKRAD GKQEQAAVED SGPGEINEDD PDVPAVVPLS EYDAVEREKL
     EAQRAQENVE LPQLKGAVYV SEELSKTLVH TVSVAVIDGT RAVTSAEERS PSWISASMTE
     PLEHAEGVAT PPVGEVTEKD ITAEATPALA QTLPGGKDAH DDIVTSEVDF TSEAVTAAET
     TEALRAEELT EASGAEETTD MVSAVSQLSD SPDTTEEATP VQEVEGGMLD TEEQERQTQA
     VLQAVADKVK EDSQVPATQT LQRAGPKALE KVEEVEEDSE VLATEKEKDV VPEGPVQEAE
     TEHLAQGSET VQATPESLEV PEVTEDVDRA TTCQVIKHQQ LMEQAVAPES SETLTDSETN
     GSTPLADSDT PNGTQQDETV DSQDSNAIAA VKQSQVTEEE AAAAQTEGPS TPSSFPAQEE
     HREKPGRDVL EPTQALAAGA VPILAKAEVG QEGEAGQFDG EKVKDGQCVK ELEVPVHTGP
     NSQKTADLTR DSEVMEVARC QETESNEEQS ISPEKREMGT DVEKEETETK TEQASEEHEQ
     ETAAPEHEGT HPKPVLTADM PHSERGKALG SLEGSPSLPD QDKADCIEVQ VQSSDTPVTQ
     TTEAVKKVEE TVATSEMDES LECAGAQSLP AEKLSETGGY GTLQHGEDTV PQGPESQAES
     IPIIVTPAPE SILHSDLQRE VSASQKQRSD EDNKPDAGPD AAGKESAARE KILRAEPEIL
     ELESKSNKIV QSVIQTAVDQ FARTETAPET HASDLQNQVP VMQADSQGAQ QMLDKDESDL
     QVSPQDGTLS AVAQEGLAVS DSSEGMSKAS EMITTLAVES ASVKESVEKL PLQCKDEKEH
     AADGPQHQSL AKAEADASGN LTKESPDTNG PKLTEEGDAL KEEMNKAQTE EDDLQEPKGD
     LTES
//
ID   TRPV2_MOUSE             Reviewed;         756 AA.
AC   Q9WTR1; Q99K71;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Transient receptor potential cation channel subfamily V member 2;
DE            Short=TrpV2;
DE   AltName: Full=Growth factor-regulated calcium channel;
DE            Short=GRC;
DE   AltName: Full=Osm-9-like TRP channel 2;
DE            Short=OTRPC2;
GN   Name=Trpv2; Synonyms=Grc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, AND GLYCOSYLATION.
RC   STRAIN=C57BL/6; TISSUE=Spleen;
RX   MEDLINE=20032759; PubMed=10559903; DOI=10.1038/11086;
RA   Kanzaki M., Zhang Y.-Q., Mashima H., Li L., Shibata H., Kojima I.;
RT   "Translocation of a calcium-permeable cation channel induced by
RT   insulin-like growth factor-I.";
RL   Nat. Cell Biol. 1:165-170(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11707512;
RA   Boels K., Glassmeier G., Herrmann D., Riedel I.B., Hampe W.,
RA   Kojima I., Schwarz J.R., Schaller H.C.;
RT   "The neuropeptide head activator induces activation and translocation
RT   of the growth-factor-regulated Ca(2+)-permeable channel GRC.";
RL   J. Cell Sci. 114:3599-3606(2001).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-755, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-47, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Calcium-permeable, non-selective cation channel with an
CC       outward rectification. Seems to be regulated, at least in part, by
CC       IGF-I, PDGF and neuropeptide head activator. May transduce
CC       physical stimuli in mast cells. Activated by temperatures higher
CC       than 52 degrees Celsius; is not activated by vanilloids and acidic
CC       pH.
CC   -!- SUBUNIT: Homotetramer (Probable). Interacts with a cAMP-dependent
CC       protein kinase type II regulatory subunit (PRKAR2A or PRKAR2B) and
CC       ACBD3. Interacts with SLC50A1; the interaction probably occurs
CC       intracellularly and depends on TRPV2 N-glycosylation (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Cytoplasm. Melanosome (By similarity). Note=Translocates from the
CC       cytoplasm to the plasma membrane upon ligand stimulation.
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in spleen, placenta,
CC       skeleton muscle, lung and brain.
CC   -!- PTM: N-glycosylated.
CC   -!- PTM: Phosphorylated by PKA (By similarity).
CC   -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family.
CC       TrpV subfamily. TRPV2 sub-subfamily.
CC   -!- SIMILARITY: Contains 6 ANK repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AB021665; BAA78478.1; -; mRNA.
DR   EMBL; AK089004; BAC40695.1; -; mRNA.
DR   EMBL; AL596181; CAI24670.1; -; Genomic_DNA.
DR   EMBL; BC005415; AAH05415.1; -; mRNA.
DR   IPI; IPI00322698; -.
DR   RefSeq; NP_035836.2; NM_011706.2.
DR   UniGene; Mm.288064; -.
DR   ProteinModelPortal; Q9WTR1; -.
DR   SMR; Q9WTR1; 30-316.
DR   STRING; Q9WTR1; -.
DR   TCDB; 1.A.4.2.4; transient receptor potential Ca2+ channel (TRP-CC) family.
DR   PhosphoSite; Q9WTR1; -.
DR   PRIDE; Q9WTR1; -.
DR   Ensembl; ENSMUST00000018651; ENSMUSP00000018651; ENSMUSG00000018507.
DR   Ensembl; ENSMUST00000102643; ENSMUSP00000099703; ENSMUSG00000018507.
DR   GeneID; 22368; -.
DR   KEGG; mmu:22368; -.
DR   UCSC; uc007jjh.1; mouse.
DR   CTD; 22368; -.
DR   MGI; MGI:1341836; Trpv2.
DR   eggNOG; roNOG05625; -.
DR   GeneTree; ENSGT00550000074425; -.
DR   HOGENOM; HBG446456; -.
DR   HOVERGEN; HBG054085; -.
DR   InParanoid; Q9WTR1; -.
DR   OMA; IQKVILR; -.
DR   OrthoDB; EOG40ZQXF; -.
DR   PhylomeDB; Q9WTR1; -.
DR   NextBio; 302697; -.
DR   ArrayExpress; Q9WTR1; -.
DR   Bgee; Q9WTR1; -.
DR   Genevestigator; Q9WTR1; -.
DR   GermOnline; ENSMUSG00000018507; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005262; F:calcium channel activity; IDA:MGI.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR004729; TRP_channel.
DR   InterPro; IPR008347; TRPV_channel.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 2.
DR   PRINTS; PR01768; TRPVRECEPTOR.
DR   SMART; SM00248; ANK; 4.
DR   SUPFAM; SSF48403; ANK; 1.
DR   TIGRFAMs; TIGR00870; trp; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Calcium; Calcium channel; Calcium transport;
KW   Cell membrane; Cytoplasm; Glycoprotein; Ion transport; Ionic channel;
KW   Membrane; Phosphoprotein; Repeat; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    756       Transient receptor potential cation
FT                                channel subfamily V member 2.
FT                                /FTId=PRO_0000215343.
FT   TOPO_DOM      1    387       Cytoplasmic (Potential).
FT   TRANSMEM    388    408       Helical; (Potential).
FT   TOPO_DOM    409    428       Extracellular (Potential).
FT   TRANSMEM    429    449       Helical; (Potential).
FT   TOPO_DOM    450    455       Cytoplasmic (Potential).
FT   TRANSMEM    456    476       Helical; (Potential).
FT   TOPO_DOM    477    490       Extracellular (Potential).
FT   TRANSMEM    491    511       Helical; (Potential).
FT   TOPO_DOM    512    532       Cytoplasmic (Potential).
FT   TRANSMEM    533    553       Helical; (Potential).
FT   INTRAMEM    568    604       Pore-forming; (Potential).
FT   TRANSMEM    617    637       Helical; (Potential).
FT   TOPO_DOM    638    756       Cytoplasmic (Potential).
FT   REPEAT       68    110       ANK 1.
FT   REPEAT      111    157       ANK 2.
FT   REPEAT      158    203       ANK 3.
FT   REPEAT      204    239       ANK 4.
FT   REPEAT      240    288       ANK 5.
FT   REPEAT      289    315       ANK 6.
FT   REGION        1    385       Required for interaction with SLC50A1 (By
FT                                similarity).
FT   MOD_RES      15     15       Phosphoserine.
FT   MOD_RES      47     47       Phosphoserine.
FT   MOD_RES     520    520       Phosphotyrosine (By similarity).
FT   MOD_RES     521    521       Phosphoserine (By similarity).
FT   MOD_RES     755    755       Phosphoserine.
FT   CARBOHYD    567    567       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    565    565       D -> N (in Ref. 1; BAA78478).
SQ   SEQUENCE   756 AA;  85965 MW;  C0E537AB2C86E1A8 CRC64;
     MTSASNPPAF RLETSDGDEE GSAEVNKGKN EPPPMESPFQ GEDRNFSPQI KVNLNYRKGL
     GPSQQDPNRF DRDRLFSVVS RGVPEELTGL LEYLRRTSKY LTDSAYTEGS TGKTCLMKAV
     LNLQDGVNAC ILPLLQIDRD SGNPQPLVNA QCTDEFYRGH SALHIAIEKR SLWCVKLLVE
     NGANVHIRAC GRFFQKHQGT CFYFGELPLS LAACTKQWDV VTYLLENPHQ PASLEATDSL
     GNTVLHALVM IADNSPENSA LVIHMYDSLL QMGARLCPTV QLEDICNHQG LTPLKLAAKE
     GKIEIFRHIL QREFSGLYQP LSRKFTEWCY GPVRVSLYDL SSVDSWEKNS VLEIIAFHCK
     SPHRHRMVVL EPLNKLLQEK WDRLIPRFFF NFACYLVYMI IFTIVAYHQP SLEQPAIPSS
     KATFGDSMLL LGHILILLGG IYLLLGQLWY FWRRRLFIWI SFMDSYFEIL FLVQALLTVL
     SQVLRFVETE WYLPLLVSSL VLGWLNLLYY TRGFQHTGIY SVMIQKVILR DLLRFLLVYL
     VFLFGFAVAL VSLSREARSP KAPEDSNTTV TEKPTLGQEE EPVPYGGILD ASLELFKFTI
     GMGELAFQEQ LRFRGVVLLL LLAYVLLTYV LLLNMLIALM SETVNSVATD SWSIWKLQKA
     ISVLEMENGY WWCRRKRHRA GRLLKVGTKG DGIPDERWCF RVEEVNWAAW EKTLPTLSED
     PSGAGITGYK KNPTSKPGKN SASEEDHLPL QVLQSH
//
ID   CAD13_MOUSE             Reviewed;         714 AA.
AC   Q9WTR5;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Cadherin-13;
DE   AltName: Full=Heart cadherin;
DE            Short=H-cadherin;
DE   AltName: Full=Truncated cadherin;
DE            Short=T-cad;
DE            Short=T-cadherin;
DE   Flags: Precursor;
GN   Name=Cdh13;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain, and Heart;
RX   MEDLINE=20199866; PubMed=10737605;
RX   DOI=10.1046/j.1471-4159.2000.0741489.x;
RA   Takeuchi T., Misaki A., Liang S.-B., Tachibana A., Hayashi N.,
RA   Sonobe H., Ohtsuki Y.;
RT   "Expression of T-cadherin (CDH13, H-Cadherin) in human brain and its
RT   characteristics as a negative growth regulator of epidermal growth
RT   factor in neuroblastoma cells.";
RL   J. Neurochem. 74:1489-1497(2000).
CC   -!- FUNCTION: Cadherins are calcium dependent cell adhesion proteins.
CC       They preferentially interact with themselves in a homophilic
CC       manner in connecting cells; cadherins may thus contribute to the
CC       sorting of heterogeneous cell types. May act as a negative
CC       regulator of neural cell growth.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor (By
CC       similarity).
CC   -!- SIMILARITY: Contains 5 cadherin domains.
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DR   EMBL; AB022100; BAA76677.1; -; mRNA.
DR   IPI; IPI00123746; -.
DR   UniGene; Mm.334841; -.
DR   PDB; 3K5R; X-ray; 2.00 A; A/B=140-355.
DR   PDB; 3K6F; X-ray; 1.81 A; A/B=140-237.
DR   PDBsum; 3K5R; -.
DR   PDBsum; 3K6F; -.
DR   ProteinModelPortal; Q9WTR5; -.
DR   SMR; Q9WTR5; 20-114, 139-690.
DR   STRING; Q9WTR5; -.
DR   PhosphoSite; Q9WTR5; -.
DR   PRIDE; Q9WTR5; -.
DR   Ensembl; ENSMUST00000117160; ENSMUSP00000113527; ENSMUSG00000031841.
DR   MGI; MGI:99551; Cdh13.
DR   GeneTree; ENSGT00550000074431; -.
DR   HOGENOM; HBG505775; -.
DR   HOVERGEN; HBG106438; -.
DR   InParanoid; Q9WTR5; -.
DR   OrthoDB; EOG498V07; -.
DR   ArrayExpress; Q9WTR5; -.
DR   Bgee; Q9WTR5; -.
DR   CleanEx; MM_CDH13; -.
DR   Genevestigator; Q9WTR5; -.
DR   GermOnline; ENSMUSG00000031841; Mus musculus.
DR   GO; GO:0031225; C:anchored to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0055100; F:adiponectin binding; IDA:BHF-UCL.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:MGI.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR014868; Cadherin_pro.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 5.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF08758; Cadherin_pro; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 5.
DR   SUPFAM; SSF49313; Cadherin; 6.
DR   PROSITE; PS00232; CADHERIN_1; 3.
DR   PROSITE; PS50268; CADHERIN_2; 5.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Cell adhesion; Cell membrane;
KW   Cleavage on pair of basic residues; Glycoprotein; GPI-anchor;
KW   Lipoprotein; Membrane; Repeat; Signal.
FT   SIGNAL        1     22       Potential.
FT   PROPEP       23    138       By similarity.
FT                                /FTId=PRO_0000003796.
FT   CHAIN       139    693       Cadherin-13.
FT                                /FTId=PRO_0000003797.
FT   PROPEP      694    714       Removed in mature form (Potential).
FT                                /FTId=PRO_0000003798.
FT   DOMAIN      143    245       Cadherin 1.
FT   DOMAIN      246    363       Cadherin 2.
FT   DOMAIN      364    477       Cadherin 3.
FT   DOMAIN      478    585       Cadherin 4.
FT   DOMAIN      586    680       Cadherin 5.
FT   LIPID       693    693       GPI-anchor amidated glycine (Potential).
FT   CARBOHYD    382    382       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    489    489       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    500    500       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    530    530       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    598    598       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    638    638       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    671    671       N-linked (GlcNAc...) (Potential).
FT   STRAND      145    148
FT   STRAND      153    155
FT   STRAND      172    176
FT   STRAND      188    190
FT   STRAND      197    199
FT   TURN        205    207
FT   STRAND      209    218
FT   STRAND      224    226
FT   STRAND      228    236
SQ   SEQUENCE   714 AA;  78286 MW;  54383E66B52F9425 CRC64;
     MQPRTPLTLC VLLSQVLLVT SADDLECTPG FQRKVLHIHQ PAEFIEDQPV LNLTFNDCKG
     NEKLHYEVSS PHFKVNSDGT LVALRNITAV GRTLFVHART PHAEDMAELV IVGGKDIQGS
     LQDIFKFART SPVPRQKRSI VVSPILIPEN QRQPFPRDVG KVVDSDRPEG SKFRLTGKGV
     DQDPKGTFRI NENTGSVSVT RTLDRETIAT YQLYVETTDA SGKTLEGPVP LEVIVIDQND
     NRPIFREGPY IGHVMEGSPT GTTVMRMTAF DADDPATDNA LWRYNIRQQT PDKPSPNMFY
     IDPEKGDIVT VVSPALLDRE TLENPKYELI IEAQDMAGLD VGLTGTATAT IVIDDKNDHS
     PKFTKKEFQA RVEEGAVGVI VNLTVEDKDD PTTGAWRAAY TIINGNPGQS FEIHTNPQTN
     EGMLSVVKPL DYEISAFHTL LIKVENEDPL VPDVSYGPSS TATVHITVLD VNEGPVFYPD
     PMMVTKQENI SVGSVLLTVN ATDPDSLQHQ TIRYSIYKDP AGWLSINPIN GTVDTTAVLD
     RESPFVHNSV YTALFLAIDS GNPPATGTGT LLITLEDIND NAPVIYPTVA EVCDDARNLS
     VVILGASDKD LHPNTDPFKF EIHKQTVPDK VWKISKINNT HALVSLLQNL NKANYNLPIM
     VTDSGKPPMT NITDLKVQVC SCKNSKVDCN GAGALHLSLS LLLLFSLLSL LSGL
//
ID   XCT_MOUSE               Reviewed;         502 AA.
AC   Q9WTR6;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Cystine/glutamate transporter;
DE   AltName: Full=Amino acid transport system xc-;
DE   AltName: Full=Solute carrier family 7 member 11;
DE   AltName: Full=xCT;
GN   Name=Slc7a11;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99223452; PubMed=10206947; DOI=10.1074/jbc.274.17.11455;
RA   Sato H., Tamba M., Ishii T., Bannai S.;
RT   "Cloning and expression of a plasma membrane cystine/glutamate
RT   exchange transporter composed of two distinct proteins.";
RL   J. Biol. Chem. 274:11455-11458(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129/SvJ; TISSUE=Liver;
RX   MEDLINE=22323257; PubMed=12235164; DOI=10.1074/jbc.M208704200;
RA   Sasaki H., Sato H., Kuriyama-Matsumura K., Sato K., Maebara K.,
RA   Wang H., Tamba M., Itoh K., Yamamoto M., Bannai S.;
RT   "Electrophile response element-mediated induction of the
RT   cystine/glutamate exchange transporter gene expression.";
RL   J. Biol. Chem. 277:44765-44771(2002).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Sodium-independent, high-affinity exchange of anionic
CC       amino acids with high specificity for anionic form of cystine and
CC       glutamate.
CC   -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid
CC       transport protein SLC3A2/4F2hc.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Probable).
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8)
CC       family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AB022345; BAA77220.1; -; mRNA.
DR   EMBL; AB037661; BAA90522.1; -; Genomic_DNA.
DR   IPI; IPI00123747; -.
DR   RefSeq; NP_036120.1; NM_011990.2.
DR   UniGene; Mm.260988; -.
DR   ProteinModelPortal; Q9WTR6; -.
DR   STRING; Q9WTR6; -.
DR   TCDB; 2.A.3.8.5; amino acid-polyamine-organocation (APC) family.
DR   PhosphoSite; Q9WTR6; -.
DR   PRIDE; Q9WTR6; -.
DR   Ensembl; ENSMUST00000029297; ENSMUSP00000029297; ENSMUSG00000027737.
DR   GeneID; 26570; -.
DR   KEGG; mmu:26570; -.
DR   UCSC; uc008pdi.1; mouse.
DR   CTD; 26570; -.
DR   MGI; MGI:1347355; Slc7a11.
DR   GeneTree; ENSGT00600000084369; -.
DR   HOGENOM; HBG714539; -.
DR   HOVERGEN; HBG000476; -.
DR   InParanoid; Q9WTR6; -.
DR   OMA; VTIFYLA; -.
DR   OrthoDB; EOG4F1X35; -.
DR   PhylomeDB; Q9WTR6; -.
DR   NextBio; 304655; -.
DR   ArrayExpress; Q9WTR6; -.
DR   Bgee; Q9WTR6; -.
DR   Genevestigator; Q9WTR6; -.
DR   GermOnline; ENSMUSG00000027737; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015171; F:amino acid transmembrane transporter activity; IEA:InterPro.
DR   InterPro; IPR004841; AA-permease_dom.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   InterPro; IPR004760; L_AA_transporter.
DR   PANTHER; PTHR11785; AA/rel_permease1; 1.
DR   Pfam; PF00324; AA_permease; 1.
DR   PIRSF; PIRSF006060; AA_transporter; 1.
DR   TIGRFAMs; TIGR00911; 2A0308; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Disulfide bond; Membrane; Phosphoprotein;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    502       Cystine/glutamate transporter.
FT                                /FTId=PRO_0000054280.
FT   TOPO_DOM      1     43       Cytoplasmic (Potential).
FT   TRANSMEM     44     64       Helical; (Potential).
FT   TOPO_DOM     65     74       Extracellular (Potential).
FT   TRANSMEM     75     95       Helical; (Potential).
FT   TOPO_DOM     96    113       Cytoplasmic (Potential).
FT   TRANSMEM    114    134       Helical; (Potential).
FT   TOPO_DOM    135    158       Extracellular (Potential).
FT   TRANSMEM    159    179       Helical; (Potential).
FT   TOPO_DOM    180    189       Cytoplasmic (Potential).
FT   TRANSMEM    190    210       Helical; (Potential).
FT   TOPO_DOM    211    231       Extracellular (Potential).
FT   TRANSMEM    232    252       Helical; (Potential).
FT   TOPO_DOM    253    265       Cytoplasmic (Potential).
FT   TRANSMEM    266    286       Helical; (Potential).
FT   TOPO_DOM    287    317       Extracellular (Potential).
FT   TRANSMEM    318    338       Helical; (Potential).
FT   TOPO_DOM    339    365       Cytoplasmic (Potential).
FT   TRANSMEM    366    386       Helical; (Potential).
FT   TOPO_DOM    387    387       Extracellular (Potential).
FT   TRANSMEM    388    408       Helical; (Potential).
FT   TOPO_DOM    409    422       Cytoplasmic (Potential).
FT   TRANSMEM    423    443       Helical; (Potential).
FT   TOPO_DOM    444    449       Extracellular (Potential).
FT   TRANSMEM    450    470       Helical; (Potential).
FT   TOPO_DOM    471    502       Cytoplasmic (Potential).
FT   MOD_RES      26     26       Phosphoserine.
SQ   SEQUENCE   502 AA;  55456 MW;  A4A185102D83992A CRC64;
     MVRKPVVATI SKGGYLQGNM SGRLPSMGDQ EPPGQEKVVL KKKITLLRGV SIIIGTVIGS
     GIFISPKGIL QNTGSVGMSL VFWSACGVLS LFGALSYAEL GTSIKKSGGH YTYILEVFGP
     LLAFVRVWVE LLVIRPGATA VISLAFGRYI LEPFFIQCEI PELAIKLVTA VGITVVMVLN
     STSVSWSARI QIFLTFCKLT AILIIIVPGV IQLIKGQTHH FKDAFSGRDT SLMGLPLAFY
     YGMYAYAGWF YLNFITEEVD NPEKTIPLAI CISMAIITVG YVLTNVAYFT TISAEELLQS
     SAVAVTFSER LLGKFSLAVP IFVALSCFGS MNGGVFAVSR LFYVASREGH LPEILSMIHV
     HKHTPLPAVI VLHPLTMVML FSGDLYSLLN FLSFARWLFM GLAVAGLIYL RYKRPDMHRP
     FKVPLFIPAL FSFTCLFMVV LSLYSDPFST GVGFLITLTG VPAYYLFIVW DKKPKWFRRL
     SDRITRTLQI ILEVVPEDSK EL
//
ID   TEN1_MOUSE              Reviewed;        2731 AA.
AC   Q9WTS4; Q8CAT1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 63.
DE   RecName: Full=Teneurin-1;
DE            Short=Ten-1;
DE   AltName: Full=Protein Odd Oz/ten-m homolog 1;
DE   AltName: Full=Tenascin-M1;
DE            Short=Ten-m1;
GN   Name=Odz1; Synonyms=Tnm1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   PubMed=10225957; DOI=10.1083/jcb.145.3.563;
RA   Oohashi T., Zhou X.-H., Feng K., Richter B., Moergelin M., Perez M.T.,
RA   Su W.D., Chiquet-Ehrismann R., Rauch U., Faessler R.;
RT   "Mouse ten-m/Odz is a new family of dimeric type II transmembrane
RT   proteins expressed in many tissues.";
RL   J. Cell Biol. 145:563-577(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: May function as a cellular signal transducer.
CC   -!- SUBUNIT: Homodimer; disulfide-linked.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Highly expressed in fetal brain, followed by
CC       kidney, testis and lung.
CC   -!- DOMAIN: EGF-like domains 2 and 5 which have an odd number of
CC       cysteines might enable the formation of intermolecular disulfide
CC       bonds.
CC   -!- DOMAIN: Cytoplasmic proline-rich regions could serve as docking
CC       domains for intracellular SH3-containing proteins.
CC   -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC   -!- SIMILARITY: Contains 8 EGF-like domains.
CC   -!- SIMILARITY: Contains 5 NHL repeats.
CC   -!- SIMILARITY: Contains 1 teneurin N-terminal domain.
CC   -!- SIMILARITY: Contains 23 YD repeats.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB025410; BAA77396.1; -; mRNA.
DR   EMBL; AK037897; BAC29893.1; -; mRNA.
DR   IPI; IPI00720016; -.
DR   RefSeq; NP_035985.2; NM_011855.3.
DR   UniGene; Mm.327698; -.
DR   HSSP; P01135; 1MOX.
DR   ProteinModelPortal; Q9WTS4; -.
DR   SMR; Q9WTS4; 501-833, 1193-1400, 1431-1466, 1499-1527.
DR   STRING; Q9WTS4; -.
DR   PhosphoSite; Q9WTS4; -.
DR   PRIDE; Q9WTS4; -.
DR   Ensembl; ENSMUST00000016294; ENSMUSP00000016294; ENSMUSG00000016150.
DR   Ensembl; ENSMUST00000115059; ENSMUSP00000110711; ENSMUSG00000016150.
DR   GeneID; 23963; -.
DR   KEGG; mmu:23963; -.
DR   UCSC; uc009tbc.1; mouse.
DR   CTD; 23963; -.
DR   MGI; MGI:1345185; Odz1.
DR   GeneTree; ENSGT00580000081247; -.
DR   HOGENOM; HBG444169; -.
DR   HOVERGEN; HBG080306; -.
DR   InParanoid; Q9WTS4; -.
DR   OMA; QVFVLTT; -.
DR   OrthoDB; EOG498TZV; -.
DR   NextBio; 303821; -.
DR   ArrayExpress; Q9WTS4; -.
DR   Bgee; Q9WTS4; -.
DR   CleanEx; MM_ODZ1; -.
DR   Genevestigator; Q9WTS4; -.
DR   GermOnline; ENSMUSG00000016150; Mus musculus.
DR   GO; GO:0005887; C:integral to plasma membrane; IDA:MGI.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR009471; Ten_N.
DR   InterPro; IPR006530; YD.
DR   Gene3D; G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 1.
DR   Pfam; PF07974; EGF_2; 6.
DR   Pfam; PF06484; Ten_N; 2.
DR   SMART; SM00181; EGF; 7.
DR   TIGRFAMs; TIGR01643; YD_repeat_2x; 5.
DR   PROSITE; PS00022; EGF_1; 8.
DR   PROSITE; PS01186; EGF_2; 7.
DR   PROSITE; PS50026; EGF_3; 5.
DR   PROSITE; PS51125; NHL; FALSE_NEG.
DR   PROSITE; PS51361; TENEURIN_N; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW   Phosphoprotein; Repeat; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   2731       Teneurin-1.
FT                                /FTId=PRO_0000259499.
FT   TOPO_DOM      1    324       Cytoplasmic (Potential).
FT   TRANSMEM    325    345       Helical; (Potential).
FT   TOPO_DOM    346   2731       Extracellular (Potential).
FT   DOMAIN        1    318       Teneurin N-terminal.
FT   DOMAIN      527    558       EGF-like 1.
FT   DOMAIN      559    590       EGF-like 2.
FT   DOMAIN      591    623       EGF-like 3.
FT   DOMAIN      624    656       EGF-like 4.
FT   DOMAIN      657    690       EGF-like 5.
FT   DOMAIN      691    720       EGF-like 6.
FT   DOMAIN      721    752       EGF-like 7.
FT   DOMAIN      760    795       EGF-like 8.
FT   REPEAT     1193   1218       NHL 1.
FT   REPEAT     1298   1342       NHL 2.
FT   REPEAT     1357   1408       NHL 3.
FT   REPEAT     1420   1464       NHL 4.
FT   REPEAT     1487   1530       NHL 5.
FT   REPEAT     1540   1559       YD 1.
FT   REPEAT     1576   1596       YD 2.
FT   REPEAT     1614   1638       YD 3.
FT   REPEAT     1639   1660       YD 4.
FT   REPEAT     1661   1681       YD 5.
FT   REPEAT     1851   1870       YD 6.
FT   REPEAT     1871   1891       YD 7.
FT   REPEAT     1892   1910       YD 8.
FT   REPEAT     1911   1931       YD 9.
FT   REPEAT     1939   1955       YD 10.
FT   REPEAT     1956   1975       YD 11.
FT   REPEAT     1976   1995       YD 12.
FT   REPEAT     1998   2018       YD 13.
FT   REPEAT     2021   2041       YD 14.
FT   REPEAT     2091   2111       YD 15.
FT   REPEAT     2119   2139       YD 16.
FT   REPEAT     2159   2179       YD 17.
FT   REPEAT     2180   2200       YD 18.
FT   REPEAT     2202   2222       YD 19.
FT   REPEAT     2234   2254       YD 20.
FT   REPEAT     2256   2276       YD 21.
FT   REPEAT     2302   2319       YD 22.
FT   REPEAT     2320   2343       YD 23.
FT   COMPBIAS    192    200       Poly-Pro.
FT   MOD_RES    2586   2586       Phosphoserine (By similarity).
FT   CARBOHYD    432    432       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    904    904       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1083   1083       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1556   1556       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1573   1573       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1669   1669       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1705   1705       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1743   1743       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1763   1763       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1787   1787       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1848   1848       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2151   2151       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2291   2291       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2608   2608       N-linked (GlcNAc...) (Potential).
FT   DISULFID    531    541       By similarity.
FT   DISULFID    535    546       By similarity.
FT   DISULFID    548    557       By similarity.
FT   DISULFID    566    577       By similarity.
FT   DISULFID    579    588       By similarity.
FT   DISULFID    595    606       By similarity.
FT   DISULFID    600    611       By similarity.
FT   DISULFID    613    622       By similarity.
FT   DISULFID    627    638       By similarity.
FT   DISULFID    632    643       By similarity.
FT   DISULFID    645    654       By similarity.
FT   DISULFID    665    678       By similarity.
FT   DISULFID    680    689       By similarity.
FT   DISULFID    694    704       By similarity.
FT   DISULFID    698    709       By similarity.
FT   DISULFID    711    720       By similarity.
FT   DISULFID    725    735       By similarity.
FT   DISULFID    729    740       By similarity.
FT   DISULFID    742    751       By similarity.
FT   DISULFID    764    774       By similarity.
FT   DISULFID    768    783       By similarity.
FT   DISULFID    785    794       By similarity.
SQ   SEQUENCE   2731 AA;  305795 MW;  9129FA4CFE4A7770 CRC64;
     MEQTDCKPYQ PLSKVKHEMD LAYTSSSDES EDGRKPRQSF NSRETLHEYN QELRRNYNSQ
     SRKRKDVEKS TQEIEFCETP PTLCSGYHTD MHSVSRHGYQ LEMGSDVDTE TEGAASPDHA
     LRMWIRGMKS EHSSCLSSRA NSALSLTDTD HERKSDGENG FKFSPVCCDM EAPADSAQDM
     QSSPHNQFTF RPLPPPPPPP HACTCARKPP PTVDSLQRRS MTTRSQPSPA APAPPTSTQD
     SVHLHNSWVL NSNIPLETRH FLFKHGSGSS AIFSAASQNY PLTSNTVYSP PPRPLPRSTF
     SRPAFTFNKP YRCCNWKCTA LSATAITVTL ALLLAYVIAV HLFGLTWQLQ PVGQIYANGI
     SNGNPGTESM DTTYSPIGGR VSDKSEKKVF QKGRAIDTGE VDIGAQVMQT IPPGLFWRFQ
     ITIHHPIYLK FNISLAKDSL LGIYGRRNIP PTHTQFDFVK LMDGKQLVKQ DSKSSDDIQH
     SPRNLILTSL QETGFIEYMD QGPWYLAFYN DGKKMEQVFV LTTAIEIMDD CSTNCNGNGE
     CISGHCHCFP GFLGPDCARD SCPVLCGGNG EYEKGHCVCR NGWKGPECDV PEEQCIDPTC
     FGHGTCIMGV CICVPGYKGE ICEEEDCLDP MCSSHGICVK GECHCSTGWG GVNCETPLPI
     CQEQCSGHGT FLLDTGVCSC DPKWTGSDCS TELCTMECGS HGVCSRGICQ CEEGWVGPTC
     EERSCHSHCA EHGQCKDGKC ECSPGWEGDH CTIAHYLDAV RDGCPGLCFG NGRCTLDQNG
     WHCVCQVGWS GTGCNIVMEM LCGDNLDNDG DGLTDCVDPD CCQQSNCYVS PLCQGSPDPL
     DLIQQSQPLF SQHTSRLFYD RIKFLIGKDS THVVPQDISF DSRRACVIRG QVVAVDGTPL
     VGVNVSFLHH SDYGFTISRQ DGSFDLVAIG GISVVLIFDR SPFLSEKRTL WLPWNQFIVV
     EKVIMQRIVA DAPSCDISNF ISPNPIVLPS PLTSFGGSCP ERGTIVPELQ VVQEEIPIPS
     SFVRLSYLSS RTPGYKTLLR ILLTHSTIPV GMIKVHLTVS VEGRLTQKWF PAAINLVYTF
     AWNKTDIYGQ KVWGLAEALV SVGYEYEMCP EFILWEQRTV VLQGFEMDAS NLGGWSLNKH
     HIFNPQSGII HKGNGENMFI SQQPPVIATI MGNGHQRSVA CTNCNGPAHN NKLFAPVALA
     SGPDGSVYVG DFNFVRRIFP SGNSVSILEL RNRDTRHSTS PAHKYYLAMD PMSESLYLSD
     TNTRKVYKLK SLVETKDLSK NFEVVAGTGD QCLPFDQSHC GDGGKASEAS LNSPRGITVD
     RHGFIYFVDG TMIRRIDENA VITTVIGSNG LTSTQPLSCD SGMDITQVRL EWPTDLAVNP
     MDNSLYVLDN NIVLQISENR RVRIIAGRPI HCQVPGIDHF LVSKVAIHST LESARAISVS
     HSGLLFIAET DERKVNRIQQ VTTNGEISII AGAPTDCDCK IDPNCDCFSG DGGYAKDAKM
     KAPSSLAVSP DGTLYVADLG NVRIRTISKN QAHLNDMNLY EIASPADQEL YQFTVNGTHL
     HTMNLITRDY VYNFTYNAEG DLGAITSSNG NSVHIRRDAG GMPLWLVVPG GQVYWLTISS
     NGVLKRVSAQ GYNLALMTYP GNTGLLATKS NENGWTTVYE YDPEGHLTNA TFPTGEVSSF
     HSDLEKLTKV ALDTSNRENV LMSTNLTATS TIYILKQENT QSTYRVSPDG SLRVTFASGM
     EINLSSEPHI LAGAVNPTLG KCNISLPGEH NANLIEWRQR KEQNKGNVSA FERRLRAHNR
     NLLSIDFDHM TRTGKIYDDH RKFTLRILYD QTGRPILWSP VSRYNEVNIT YSPSGLVTFI
     QRGTWNEKME YDQSGKIISR TWADGKIWSY TYLEKSVMLL LHSQRRYIFE YDQSDCLLSV
     TMPSMVRHSL QTMLSVGYYR NIYTPPDSST SFIQDYSRDG RLLQTLHLGT GRRVLYKYTK
     QARLSEILYD TTQVTLTYEE SSGVIKTIHL MHDGFICTIR YRQTGPLIGR QIFRFSEEGL
     VNARFDYSYN NFRVTSMQAV INETPLPIDL YRYVDVSGRT EQFGKFSVIN YDLNQVITTT
     VMKHTKIFNA NGQVIEVQYE ILKAIAYWMT IQYDNMGRMV ICDIRVGVDA NITRYFYEYD
     ADGQLQTVSV NDKIQWRYSY DLNGNINLLS HGNSARLTPL RYDLRDRITR LGEIQYKMDE
     DGFLRQRGND IFEYNSNGLL QKAYNKVSGW TVQYYYDGLG RRVASKSSLG QHLQFFYADL
     ANPIRVTHLY NHTSAEITSL YYDLQGHLIA MELSSGEEYY VACDNMGTPL AVFSSRGQVI
     KEILYTPYGD IYHDTYPDFE VIIGFHGGLY DFLTKLVHLG QRDYDVVAGR WTTPNHHIWK
     QLNLLPKPFN LYSFENNYPV GKIQDVAKYT TDIGTWLELF GFQLHNVLPG FPKPELENME
     LTYELLQLQT KTQEWDPGKM ILGIQCELQK QLRNFISLDQ LPMTPQYNEG RCLEGGKQPR
     FAAVPSVFGK GIKFAIKEGI VTADIIGVAN EDSRRLAAIL NNAHYLENLH FTIEGRDTHY
     FIKLGSLEED LVLIGNTGGR RILENGVNVT VSQMTSVLNG RTRRFADIQL QHGALCFNIR
     YGTTVEEEKN HVLEMARQRA VAQAWTQEQR RLQEGEEGTR VWTEGEKQQL LGTGRVQGYD
     GYFVLSVEQY LELSDSANNI HFMRQSEIGR R
//
ID   TEN2_MOUSE              Reviewed;        2764 AA.
AC   Q9WTS5; Q5NBW7; Q5NBW8; Q80TJ0; Q9JLC0; Q9QYZ1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   RecName: Full=Teneurin-2;
DE            Short=Ten-2;
DE   AltName: Full=Protein Odd Oz/ten-m homolog 2;
DE   AltName: Full=Tenascin-M2;
DE            Short=Ten-m2;
GN   Name=Odz2; Synonyms=Kiaa1127, Tnm2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   PubMed=10225957; DOI=10.1083/jcb.145.3.563;
RA   Oohashi T., Zhou X.-H., Feng K., Richter B., Moergelin M., Perez M.T.,
RA   Su W.D., Chiquet-Ehrismann R., Rauch U., Faessler R.;
RT   "Mouse ten-m/Odz is a new family of dimeric type II transmembrane
RT   proteins expressed in many tissues.";
RL   J. Cell Biol. 145:563-577(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 572-799.
RX   PubMed=10588872; DOI=10.1006/dbio.1999.9503;
RA   Rubin B.P., Tucker R.P., Martin D., Chiquet-Ehrismann R.;
RT   "Teneurins: a novel family of neuronal cell surface proteins in
RT   vertebrates, homologous to the Drosophila pair-rule gene product Ten-
RT   m.";
RL   Dev. Biol. 216:195-209(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1835-2764.
RX   PubMed=10625539; DOI=10.1006/dbio.1999.9532;
RA   Ben-Zur T., Feige E., Motro B., Wides R.;
RT   "The mammalian Odz gene family: homologs of a Drosophila pair-rule
RT   gene with expression implying distinct yet overlapping developmental
RT   roles.";
RL   Dev. Biol. 217:107-120(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2512-2764.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
CC   -!- FUNCTION: May function as a cellular signal transducer.
CC   -!- SUBUNIT: Homodimer; disulfide-linked (Probable).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane
CC       protein (Probable).
CC   -!- DOMAIN: EGF-like domains 2 and 5 which have an odd number of
CC       cysteines might enable the formation of intermolecular disulfide
CC       bonds.
CC   -!- DOMAIN: Cytoplasmic proline-rich regions could serve as docking
CC       domains for intracellular SH3-containing proteins.
CC   -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC   -!- SIMILARITY: Contains 8 EGF-like domains.
CC   -!- SIMILARITY: Contains 5 NHL repeats.
CC   -!- SIMILARITY: Contains 1 teneurin N-terminal domain.
CC   -!- SIMILARITY: Contains 23 YD repeats.
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DR   EMBL; AB025411; BAA77397.1; -; mRNA.
DR   EMBL; AL713956; CAI35933.1; -; Genomic_DNA.
DR   EMBL; AL645912; CAI35933.1; JOINED; Genomic_DNA.
DR   EMBL; AL713915; CAI35933.1; JOINED; Genomic_DNA.
DR   EMBL; AL713919; CAI35933.1; JOINED; Genomic_DNA.
DR   EMBL; BX000433; CAI35933.1; JOINED; Genomic_DNA.
DR   EMBL; BX539311; CAI35933.1; JOINED; Genomic_DNA.
DR   EMBL; AL713956; CAI35934.1; -; Genomic_DNA.
DR   EMBL; AL645912; CAI35934.1; JOINED; Genomic_DNA.
DR   EMBL; AL713915; CAI35934.1; JOINED; Genomic_DNA.
DR   EMBL; AL713919; CAI35934.1; JOINED; Genomic_DNA.
DR   EMBL; BX539311; CAI35934.1; JOINED; Genomic_DNA.
DR   EMBL; BX000433; CAI35934.1; JOINED; Genomic_DNA.
DR   EMBL; BX539311; CAI36037.1; -; Genomic_DNA.
DR   EMBL; AL645912; CAI36037.1; JOINED; Genomic_DNA.
DR   EMBL; AL713915; CAI36037.1; JOINED; Genomic_DNA.
DR   EMBL; AL713919; CAI36037.1; JOINED; Genomic_DNA.
DR   EMBL; AL713956; CAI36037.1; JOINED; Genomic_DNA.
DR   EMBL; BX000433; CAI36037.1; JOINED; Genomic_DNA.
DR   EMBL; BX539311; CAI36038.1; -; Genomic_DNA.
DR   EMBL; AL645912; CAI36038.1; JOINED; Genomic_DNA.
DR   EMBL; AL713915; CAI36038.1; JOINED; Genomic_DNA.
DR   EMBL; AL713919; CAI36038.1; JOINED; Genomic_DNA.
DR   EMBL; AL713956; CAI36038.1; JOINED; Genomic_DNA.
DR   EMBL; BX000433; CAI36038.1; JOINED; Genomic_DNA.
DR   EMBL; AL713919; CAI35941.1; -; Genomic_DNA.
DR   EMBL; AL645912; CAI35941.1; JOINED; Genomic_DNA.
DR   EMBL; AL713915; CAI35941.1; JOINED; Genomic_DNA.
DR   EMBL; AL713956; CAI35941.1; JOINED; Genomic_DNA.
DR   EMBL; BX000433; CAI35941.1; JOINED; Genomic_DNA.
DR   EMBL; BX539311; CAI35941.1; JOINED; Genomic_DNA.
DR   EMBL; AL713919; CAI35942.1; -; Genomic_DNA.
DR   EMBL; AL645912; CAI35942.1; JOINED; Genomic_DNA.
DR   EMBL; AL713915; CAI35942.1; JOINED; Genomic_DNA.
DR   EMBL; AL713956; CAI35942.1; JOINED; Genomic_DNA.
DR   EMBL; BX539311; CAI35942.1; JOINED; Genomic_DNA.
DR   EMBL; BX000433; CAI35942.1; JOINED; Genomic_DNA.
DR   EMBL; AL713915; CAI35944.1; -; Genomic_DNA.
DR   EMBL; AL645912; CAI35944.1; JOINED; Genomic_DNA.
DR   EMBL; AL713919; CAI35944.1; JOINED; Genomic_DNA.
DR   EMBL; AL713956; CAI35944.1; JOINED; Genomic_DNA.
DR   EMBL; BX000433; CAI35944.1; JOINED; Genomic_DNA.
DR   EMBL; BX539311; CAI35944.1; JOINED; Genomic_DNA.
DR   EMBL; AL713915; CAI35945.1; -; Genomic_DNA.
DR   EMBL; BX539311; CAI35945.1; JOINED; Genomic_DNA.
DR   EMBL; BX000433; CAI35945.1; JOINED; Genomic_DNA.
DR   EMBL; AL713956; CAI35945.1; JOINED; Genomic_DNA.
DR   EMBL; AL713919; CAI35945.1; JOINED; Genomic_DNA.
DR   EMBL; AL645912; CAI35945.1; JOINED; Genomic_DNA.
DR   EMBL; BX000433; CAI35946.1; -; Genomic_DNA.
DR   EMBL; AL645912; CAI35946.1; JOINED; Genomic_DNA.
DR   EMBL; AL713915; CAI35946.1; JOINED; Genomic_DNA.
DR   EMBL; AL713919; CAI35946.1; JOINED; Genomic_DNA.
DR   EMBL; AL713956; CAI35946.1; JOINED; Genomic_DNA.
DR   EMBL; BX539311; CAI35946.1; JOINED; Genomic_DNA.
DR   EMBL; BX000433; CAI35947.1; -; Genomic_DNA.
DR   EMBL; AL645912; CAI35947.1; JOINED; Genomic_DNA.
DR   EMBL; AL713919; CAI35947.1; JOINED; Genomic_DNA.
DR   EMBL; AL713956; CAI35947.1; JOINED; Genomic_DNA.
DR   EMBL; AL713915; CAI35947.1; JOINED; Genomic_DNA.
DR   EMBL; BX539311; CAI35947.1; JOINED; Genomic_DNA.
DR   EMBL; AL645912; CAI35083.1; -; Genomic_DNA.
DR   EMBL; AL713915; CAI35083.1; JOINED; Genomic_DNA.
DR   EMBL; AL713919; CAI35083.1; JOINED; Genomic_DNA.
DR   EMBL; AL713956; CAI35083.1; JOINED; Genomic_DNA.
DR   EMBL; BX000433; CAI35083.1; JOINED; Genomic_DNA.
DR   EMBL; BX539311; CAI35083.1; JOINED; Genomic_DNA.
DR   EMBL; AL645912; CAI35084.1; -; Genomic_DNA.
DR   EMBL; AL713915; CAI35084.1; JOINED; Genomic_DNA.
DR   EMBL; AL713919; CAI35084.1; JOINED; Genomic_DNA.
DR   EMBL; AL713956; CAI35084.1; JOINED; Genomic_DNA.
DR   EMBL; BX000433; CAI35084.1; JOINED; Genomic_DNA.
DR   EMBL; BX539311; CAI35084.1; JOINED; Genomic_DNA.
DR   EMBL; AJ245710; CAB57282.1; -; mRNA.
DR   EMBL; AF195419; AAF28317.1; -; mRNA.
DR   EMBL; AK122455; BAC65737.1; -; mRNA.
DR   IPI; IPI00123782; -.
DR   RefSeq; NP_035986.3; NM_011856.3.
DR   UniGene; Mm.439889; -.
DR   UniGene; Mm.445432; -.
DR   HSSP; P35555; 1EMN.
DR   ProteinModelPortal; Q9WTS5; -.
DR   SMR; Q9WTS5; 575-869, 1347-1373, 1404-1441, 1463-1563.
DR   PhosphoSite; Q9WTS5; -.
DR   PRIDE; Q9WTS5; -.
DR   Ensembl; ENSMUST00000102801; ENSMUSP00000099865; ENSMUSG00000049336.
DR   Ensembl; ENSMUST00000109310; ENSMUSP00000104933; ENSMUSG00000049336.
DR   GeneID; 23964; -.
DR   KEGG; mmu:23964; -.
DR   UCSC; uc007ilk.1; mouse.
DR   CTD; 23964; -.
DR   MGI; MGI:1345184; Odz2.
DR   eggNOG; roNOG06823; -.
DR   GeneTree; ENSGT00580000081247; -.
DR   HOVERGEN; HBG080306; -.
DR   OrthoDB; EOG4QC14D; -.
DR   ArrayExpress; Q9WTS5; -.
DR   Bgee; Q9WTS5; -.
DR   CleanEx; MM_ODZ2; -.
DR   Genevestigator; Q9WTS5; -.
DR   GermOnline; ENSMUSG00000049336; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR011044; Quino_amine_DH_bsu.
DR   InterPro; IPR022385; Rhs_assc_core.
DR   InterPro; IPR009471; Ten_N.
DR   InterPro; IPR006530; YD.
DR   Gene3D; G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 1.
DR   Pfam; PF07974; EGF_2; 6.
DR   Pfam; PF06484; Ten_N; 1.
DR   SMART; SM00181; EGF; 7.
DR   SUPFAM; SSF50969; Amine_DH_B_like; 1.
DR   SUPFAM; SSF49464; CarboxypepD_reg; 1.
DR   TIGRFAMs; TIGR03696; Rhs_assc_core; 1.
DR   TIGRFAMs; TIGR01643; YD_repeat_2x; 5.
DR   PROSITE; PS00022; EGF_1; 8.
DR   PROSITE; PS01186; EGF_2; 7.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS51125; NHL; FALSE_NEG.
DR   PROSITE; PS51361; TENEURIN_N; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW   Phosphoprotein; Repeat; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   2764       Teneurin-2.
FT                                /FTId=PRO_0000259502.
FT   TOPO_DOM      1    379       Cytoplasmic (Potential).
FT   TRANSMEM    380    400       Helical; (Potential).
FT   TOPO_DOM    401   2764       Extracellular (Potential).
FT   DOMAIN        1    375       Teneurin N-terminal.
FT   DOMAIN      575    603       EGF-like 1.
FT   DOMAIN      598    634       EGF-like 2.
FT   DOMAIN      636    668       EGF-like 3.
FT   DOMAIN      669    701       EGF-like 4.
FT   DOMAIN      702    735       EGF-like 5.
FT   DOMAIN      737    765       EGF-like 6.
FT   DOMAIN      768    796       EGF-like 7.
FT   DOMAIN      798    831       EGF-like 8.
FT   REPEAT     1262   1306       NHL 1.
FT   REPEAT     1332   1376       NHL 2.
FT   REPEAT     1391   1442       NHL 3.
FT   REPEAT     1464   1491       NHL 4.
FT   REPEAT     1520   1563       NHL 5.
FT   REPEAT     1573   1592       YD 1.
FT   REPEAT     1609   1629       YD 2.
FT   REPEAT     1672   1691       YD 3.
FT   REPEAT     1692   1714       YD 4.
FT   REPEAT     1885   1904       YD 5.
FT   REPEAT     1926   1944       YD 6.
FT   REPEAT     1945   1965       YD 7.
FT   REPEAT     1972   1989       YD 8.
FT   REPEAT     1990   2011       YD 9.
FT   REPEAT     2012   2029       YD 10.
FT   REPEAT     2032   2052       YD 11.
FT   REPEAT     2055   2075       YD 12.
FT   REPEAT     2083   2103       YD 13.
FT   REPEAT     2109   2126       YD 14.
FT   REPEAT     2127   2153       YD 15.
FT   REPEAT     2155   2168       YD 16.
FT   REPEAT     2169   2192       YD 17.
FT   REPEAT     2195   2215       YD 18.
FT   REPEAT     2216   2236       YD 19.
FT   REPEAT     2238   2258       YD 20.
FT   REPEAT     2270   2290       YD 21.
FT   REPEAT     2292   2312       YD 22.
FT   REPEAT     2338   2379       YD 23.
FT   COMPBIAS    175    178       Poly-Ser.
FT   COMPBIAS    331    334       Poly-Ser.
FT   MOD_RES     523    523       Phosphoserine (By similarity).
FT   MOD_RES    1140   1140       Phosphotyrosine (By similarity).
FT   CARBOHYD    443    443       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    482    482       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    915    915       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    938    938       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1257   1257       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1606   1606       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1702   1702       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1739   1739       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1763   1763       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1797   1797       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1882   1882       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1983   1983       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2187   2187       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2327   2327       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2638   2638       N-linked (GlcNAc...) (Potential).
FT   DISULFID    576    586       By similarity.
FT   DISULFID    580    591       By similarity.
FT   DISULFID    593    602       By similarity.
FT   DISULFID    611    622       By similarity.
FT   DISULFID    624    633       By similarity.
FT   DISULFID    640    651       By similarity.
FT   DISULFID    645    656       By similarity.
FT   DISULFID    658    667       By similarity.
FT   DISULFID    672    683       By similarity.
FT   DISULFID    677    688       By similarity.
FT   DISULFID    690    699       By similarity.
FT   DISULFID    710    723       By similarity.
FT   DISULFID    725    734       By similarity.
FT   DISULFID    738    748       By similarity.
FT   DISULFID    742    753       By similarity.
FT   DISULFID    755    764       By similarity.
FT   DISULFID    769    779       By similarity.
FT   DISULFID    773    784       By similarity.
FT   DISULFID    786    795       By similarity.
FT   DISULFID    800    810       By similarity.
FT   DISULFID    804    819       By similarity.
FT   DISULFID    821    830       By similarity.
FT   CONFLICT    736    736       V -> VE (in Ref. 2; CAI35934/CAI36038/
FT                                CAI35942/CAI35945/CAI35947/CAI35084 and
FT                                3; CAB57282).
FT   CONFLICT   2369   2369       Y -> F (in Ref. 2; CAI35083/CAI35084/
FT                                CAI35933/CAI35934/CAI35941/CAI35942/
FT                                CAI35944/CAI35945/CAI35946/CAI35947/
FT                                CAI36037/CAI36038 and 4; AAF28317).
FT   CONFLICT   2690   2690       G -> R (in Ref. 2; CAI35083/CAI35084/
FT                                CAI35933/CAI35934/CAI35941/CAI35942/
FT                                CAI35944/CAI35945/CAI35946/CAI35947/
FT                                CAI36037/CAI36038 and 5; BAC65737).
SQ   SEQUENCE   2764 AA;  306468 MW;  73BA3D916D0F0344 CRC64;
     MDVKDRRHRS LTRGRCGKEC RYTSSSLDSE DCRVPTQKSY SSSETLKAYD HDSRMHYGNR
     VTDLVHRESD EFSRQGTNFT LAELGICEPS PHRSGYCSDM GILHQGYSLS TGSDADSDTE
     GGMSPEHAIR LWGRGIKSRR SSGLSSRENS ALTLTDSDNE NKSDDDNGRP IPPTSSSSLL
     PSAQLPSSHN PPPVSCQMPL LDSNTSHQIM DTNPDEEFSP NSYLLRACSG PQQASSSGPP
     NHHSQSTLRP PLPPPHNHTL SHHHSSANSL NRNSLTNRRS QIHAPAPAPN DLATTPESVQ
     LQDSWVLNSN VPLETRHFLF KTSSGSTPLF SSSSPGYPLT SGTVYTPPPR LLPRNTFSRK
     AFKLKKPSKY CSWKCAALSA IAAALLLAIL LAYFIAMHLL GLNWQLQPAD GHTFNNGVRT
     GLPGNDDVAT VPSGGKVPWS LKNSSIDSGE AEVGRRVTQE VPPGVFWRSQ IHISQPQFLK
     FNISLGKDAL FGVYIRRGLP PSHAQYDFME RLDGKEKWSV VESPRERRSI QTLVQNEAVF
     VQYLDVGLWH LAFYNDGKDK EMVSFNTVVL DSVQDCPRNC HGNGECVSGL CHCFPGFLGA
     DCAKAACPVL CSGNGQYSKG TCQCYSGWKG AECDVPMNQC IDPSCGGHGS CIDGNCVCAA
     GYKGEHCEEV DCLDPTCSSH GVCVNGECLC SPGWGGLNCE LARVQCPDQC SGHGTYLPDS
     GLCSCDPNWM GPDCSVVCSV DCGTHGVCIG GACRCEEGWT GAACDQRVCH PRCIEHGTCK
     DGKCECREGW NGEHCTIDGC PDLCNGNGRC TLGQNSWQCV CQTGWRGPGC NVAMETSCAD
     NKDNEGDGLV DCLDPDCCLQ SACQNSLLCR GSRDPLDIIQ QGQTDWPAVK SFYDRIKLLA
     GKDSTHIIPG DNPFNSSLVS LIRGQVVTMD GTPLVGVNVS FVKYPKYGYT ITRQDGTFDL
     IANGGSALTL HFERAPFMSQ ERTVWLPWNS FYAMDTLVMK TEENSIPSCD LSGFVRPDPI
     IISSPLSTFF SASPASNPIV PETQVLHEEI ELPGTNVKLR YLSSRTAGYK SLLKITMTQS
     TVPLNLIRVH LMVAVEGHLF QKSFQASPNL AYTFIWDKTD AYGQRVYGLS DAVVSVGFEY
     ETCPSLILWE KRTALLQGFE LDPSNLGGWS LDKHHTLNVK SGILHKGTGE NQFLTQQPAI
     ITSIMGNGRR RSISCPSCNG LAEGNKLLAP VALAVGIDGS LFVGDFNYIR RIFPSRNVTS
     ILELRNKEFK HSNSPGHKYY LAVDPVTGSL YVSDTNSRRI YRVKSLSGAK DLAGNSEVVA
     GTGEQCLPFD EARCGDGGKA VDATLMSPRG IAVDKNGLMY FVDATMIRKV DQNGIISTLL
     GSNDLTAVRP LSCDSSMDVA QVRLEWPTDL AVNPMDNSLY VLENNVILRI TENHQVSIIA
     GRPMHCQVPG IDYSLSKLAI HSALESASAI AISHTGVLYI TETDEKKINR LRQVTTNGEI
     CLLAGAASDC DCKNDVNCIC YSGDDAYATD AILNSPSSLA VAPDGTIYIA DLGNIRIRAV
     SKNKPVLNAF NQYEAASPGE QELYVFNADG IHQYTVSLVT GEYLYNFTYS ADNDVTELID
     NNGNSLKIRR DSSGMPRHLL MPDNQIITLT VGTNGGLKAV STQNLELGLM TYDGNTGLLA
     TKSDETGWTT FYDYDHEGRL TNVTRPTGVV TSLHREMEKS ITIDIENSNR DDDVTVITNL
     SSVEASYTVV QDQVRNSYQL CNNGTLRVMY ANGMAVSFHS EPHVLAGTIT PTIGRCNISL
     PMENGLNSIE WRLRKEQIKG KVTIFGRKLR VHGRNLLSID YDRNIRTEKI YDDHRKFTLR
     IIYDQVGRPF LWLPSSGLAA VNVSYFFNGR LAGLQRGAMS ERTDIDKQGR IVSRMFADGK
     VWSYSYLDKS MVLLLQSQRQ YIFEYDSSDR LHAVTMPSVA RHSMSTHTSI GYIRNIYNPP
     ESNASVIFDY SDDGRILKTS FLGTGRQVFY KYGKLSKLSE IVYDSTAVTF GYDETTGVLK
     MVNLQSGGFS CTIRYRKVGP LVDKQIYRFS EEGMINARFD YTYHDNSFRI ASIKPVISET
     PLPVDLYRYD EISGKVEHFG KFGVIYYDIN QIITTAVMTL SKHFDTHGRI KEVQYEMFRS
     LMYWMTVQYD SMGRVIKREL KLGPYANTTK YTYDYDGDGQ LQSVAVNDRP TWRYSYDLNG
     NLHLLNPGNS ARLMPLRYDL RDRITRLGDV QYKIDDDGYL CQRGSDIFEY NSKGLLTRAY
     NKASGWSVQY RYDGVGRRAS YKTNLGHHLQ YFYSDLHNPT RITHVYNHSN SEITSLYYDL
     QGHLFAMESS SGEEYYVASD NTGTPLAVYS INGLMIKQLQ YTAYGEIYYD SNPDFQMVIG
     FHGGLYDPLT KLVHFTQRDY DVLAGRWTSP DYTMWRNVGK EPAPFNLYMF KNNNPLSNEL
     DLKNYVTDVK SWLVMFGFQL SNIIPGFPRA KMYFVPPPYE LSESQASENG QLITGVQQTT
     ERHNQAFLAL EGQVITKKLH ASIREKAGHW FATTTPIIGK GIMFAIKEGR VTTGVSSIAS
     EDSRKVASVL NNAYYLDKMH YSIEGKDTHY FVKIGAADGD LVTLGTTIGR KVLESGVNVT
     VSQPTLLVNG RTRRFTNIEF QYSTLLLSIR YGLTPDTLDE EKARVLDQAG QRALGTAWAK
     EQQKARDGRE GSRLWTEGEK QQLLSTGRVQ GYEGYYVLPV EQYPELADSS SNIQFLRQNE
     MGKR
//
ID   TEN3_MOUSE              Reviewed;        2715 AA.
AC   Q9WTS6; Q3UVR9; Q3UX72; Q80TD2; Q8BSL5; Q9CSV2; Q9JLC1;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 67.
DE   RecName: Full=Teneurin-3;
DE            Short=Ten-3;
DE   AltName: Full=Protein Odd Oz/ten-m homolog 3;
DE   AltName: Full=Tenascin-M3;
DE            Short=Ten-m3;
GN   Name=Odz3; Synonyms=Kiaa1455, Tnm3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   PubMed=10225957; DOI=10.1083/jcb.145.3.563;
RA   Oohashi T., Zhou X.-H., Feng K., Richter B., Moergelin M., Perez M.T.,
RA   Su W.D., Chiquet-Ehrismann R., Rauch U., Faessler R.;
RT   "Mouse ten-m/Odz is a new family of dimeric type II transmembrane
RT   proteins expressed in many tissues.";
RL   J. Cell Biol. 145:563-577(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 354-2715 (ISOFORM 2).
RX   PubMed=10625539; DOI=10.1006/dbio.1999.9532;
RA   Ben-Zur T., Feige E., Motro B., Wides R.;
RT   "The mammalian Odz gene family: homologs of a Drosophila pair-rule
RT   gene with expression implying distinct yet overlapping developmental
RT   roles.";
RL   Dev. Biol. 217:107-120(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 871-2715 (ISOFORM 2), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1640-2715 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Egg, Embryo, and Forelimb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 888-2715 (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-380 AND ASN-2140, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
CC   -!- FUNCTION: May function as a cellular signal transducer.
CC   -!- SUBUNIT: Homodimer; disulfide-linked (Probable).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane
CC       protein (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9WTS6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9WTS6-2; Sequence=VSP_021402, VSP_021403;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: EGF-like domains 2 and 5 which have an odd number of
CC       cysteines might enable the formation of intermolecular disulfide
CC       bonds.
CC   -!- DOMAIN: Cytoplasmic proline-rich regions could serve as docking
CC       domains for intracellular SH3-containing proteins.
CC   -!- SIMILARITY: Belongs to the tenascin family. Teneurin subfamily.
CC   -!- SIMILARITY: Contains 8 EGF-like domains.
CC   -!- SIMILARITY: Contains 6 NHL repeats.
CC   -!- SIMILARITY: Contains 1 teneurin N-terminal domain.
CC   -!- SIMILARITY: Contains 23 YD repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE22691.1; Type=Erroneous initiation;
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DR   EMBL; AB025412; BAA77398.1; -; mRNA.
DR   EMBL; AF195418; AAF28316.1; -; mRNA.
DR   EMBL; AK011924; BAB27919.1; -; mRNA.
DR   EMBL; AK031268; BAC27329.1; -; mRNA.
DR   EMBL; AK122513; BAC65795.1; -; mRNA.
DR   EMBL; AK135844; BAE22691.1; ALT_INIT; mRNA.
DR   EMBL; AK136994; BAE23200.1; -; mRNA.
DR   IPI; IPI00123783; -.
DR   IPI; IPI00798466; -.
DR   UniGene; Mm.42191; -.
DR   HSSP; P00750; 1TPG.
DR   ProteinModelPortal; Q9WTS6; -.
DR   SMR; Q9WTS6; 518-821, 1179-1388, 1418-1452, 1484-1514.
DR   PhosphoSite; Q9WTS6; -.
DR   PRIDE; Q9WTS6; -.
DR   Ensembl; ENSMUST00000033965; ENSMUSP00000033965; ENSMUSG00000031561.
DR   UCSC; uc009lrr.1; mouse.
DR   UCSC; uc009lrs.1; mouse.
DR   MGI; MGI:1345183; Odz3.
DR   eggNOG; roNOG06823; -.
DR   GeneTree; ENSGT00580000081247; -.
DR   HOVERGEN; HBG080306; -.
DR   InParanoid; Q9WTS6; -.
DR   OrthoDB; EOG4QC14D; -.
DR   NextBio; 303829; -.
DR   ArrayExpress; Q9WTS6; -.
DR   Bgee; Q9WTS6; -.
DR   CleanEx; MM_ODZ3; -.
DR   Genevestigator; Q9WTS6; -.
DR   GermOnline; ENSMUSG00000031561; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR022385; Rhs_assc_core.
DR   InterPro; IPR009471; Ten_N.
DR   InterPro; IPR006530; YD.
DR   Gene3D; G3DSA:2.120.10.30; 6-blade_b-propeller_TolB-like; 1.
DR   Pfam; PF07974; EGF_2; 5.
DR   Pfam; PF06484; Ten_N; 2.
DR   SMART; SM00181; EGF; 7.
DR   SUPFAM; SSF49464; CarboxypepD_reg; 1.
DR   TIGRFAMs; TIGR03696; Rhs_assc_core; 1.
DR   TIGRFAMs; TIGR01643; YD_repeat_2x; 5.
DR   PROSITE; PS00022; EGF_1; 8.
DR   PROSITE; PS01186; EGF_2; 7.
DR   PROSITE; PS50026; EGF_3; 5.
DR   PROSITE; PS51125; NHL; FALSE_NEG.
DR   PROSITE; PS51361; TENEURIN_N; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; EGF-like domain; Glycoprotein;
KW   Membrane; Repeat; Signal-anchor; Transmembrane; Transmembrane helix.
FT   CHAIN         1   2715       Teneurin-3.
FT                                /FTId=PRO_0000259506.
FT   TOPO_DOM      1    310       Cytoplasmic (Potential).
FT   TRANSMEM    311    331       Helical; (Potential).
FT   TOPO_DOM    332   2715       Extracellular (Potential).
FT   DOMAIN        1    309       Teneurin N-terminal.
FT   DOMAIN      514    545       EGF-like 1.
FT   DOMAIN      546    576       EGF-like 2.
FT   DOMAIN      578    610       EGF-like 3.
FT   DOMAIN      611    642       EGF-like 4.
FT   DOMAIN      644    677       EGF-like 5.
FT   DOMAIN      678    709       EGF-like 6.
FT   DOMAIN      710    739       EGF-like 7.
FT   DOMAIN      740    783       EGF-like 8.
FT   REPEAT     1181   1209       NHL 1.
FT   REPEAT     1216   1260       NHL 2.
FT   REPEAT     1286   1330       NHL 3.
FT   REPEAT     1347   1387       NHL 4.
FT   REPEAT     1418   1445       NHL 5.
FT   REPEAT     1474   1517       NHL 6.
FT   REPEAT     1527   1546       YD 1.
FT   REPEAT     1563   1583       YD 2.
FT   REPEAT     1626   1645       YD 3.
FT   REPEAT     1646   1668       YD 4.
FT   REPEAT     1839   1858       YD 5.
FT   REPEAT     1880   1898       YD 6.
FT   REPEAT     1899   1919       YD 7.
FT   REPEAT     1926   1943       YD 8.
FT   REPEAT     1944   1965       YD 9.
FT   REPEAT     1966   1983       YD 10.
FT   REPEAT     1986   2006       YD 11.
FT   REPEAT     2009   2029       YD 12.
FT   REPEAT     2037   2056       YD 13.
FT   REPEAT     2062   2079       YD 14.
FT   REPEAT     2080   2106       YD 15.
FT   REPEAT     2108   2121       YD 16.
FT   REPEAT     2122   2145       YD 17.
FT   REPEAT     2148   2168       YD 18.
FT   REPEAT     2169   2189       YD 19.
FT   REPEAT     2191   2211       YD 20.
FT   REPEAT     2223   2243       YD 21.
FT   REPEAT     2245   2265       YD 22.
FT   REPEAT     2291   2332       YD 23.
FT   CARBOHYD    345    345       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    380    380       N-linked (GlcNAc...).
FT   CARBOHYD    419    419       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    670    670       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    869    869       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    892    892       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1211   1211       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1543   1543       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1560   1560       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1656   1656       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1693   1693       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1751   1751       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1836   1836       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1937   1937       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2140   2140       N-linked (GlcNAc...).
FT   CARBOHYD   2280   2280       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   2592   2592       N-linked (GlcNAc...) (Potential).
FT   DISULFID    518    528       By similarity.
FT   DISULFID    522    533       By similarity.
FT   DISULFID    535    544       By similarity.
FT   DISULFID    553    564       By similarity.
FT   DISULFID    566    575       By similarity.
FT   DISULFID    582    593       By similarity.
FT   DISULFID    587    598       By similarity.
FT   DISULFID    600    609       By similarity.
FT   DISULFID    614    625       By similarity.
FT   DISULFID    619    630       By similarity.
FT   DISULFID    632    641       By similarity.
FT   DISULFID    652    665       By similarity.
FT   DISULFID    667    676       By similarity.
FT   DISULFID    681    691       By similarity.
FT   DISULFID    685    696       By similarity.
FT   DISULFID    698    707       By similarity.
FT   DISULFID    712    722       By similarity.
FT   DISULFID    716    727       By similarity.
FT   DISULFID    729    738       By similarity.
FT   DISULFID    752    762       By similarity.
FT   DISULFID    756    771       By similarity.
FT   DISULFID    773    782       By similarity.
FT   VAR_SEQ     741    749       Missing (in isoform 2).
FT                                /FTId=VSP_021402.
FT   VAR_SEQ    1219   1225       Missing (in isoform 2).
FT                                /FTId=VSP_021403.
FT   CONFLICT   1632   1637       LLATKS -> AFSHQK (in Ref. 3; BAE22691).
FT   CONFLICT   1640   1640       T -> S (in Ref. 3; BAE23200).
FT   CONFLICT   2332   2332       T -> I (in Ref. 2; AAF28316 and 3;
FT                                BAE23200/BAC65795).
FT   CONFLICT   2482   2482       Missing (in Ref. 3; BAC27329).
FT   CONFLICT   2636   2636       I -> L (in Ref. 3; BAB27919).
SQ   SEQUENCE   2715 AA;  303066 MW;  598F46A77334C2E1 CRC64;
     MDVKERRPYC SLTKSRREKE RRYTNSSADN EECRVPTQKS YSSSETLKAF DHDYSRLLYG
     NRVKDLVHRE ADEYTRQGQN FTLRQLGVCE SATRRGVAFC AEMGLPHRGY SISAGSDADT
     ENEAVMSPEH AMRLWGRGVK SGRSSCLSSR SNSALTLTDT EHENRSDSES EQPSNNPGQP
     TLQPLPPSHK QHPAQHHPSI TSLNRNSLTN RRNQSPAPPA ALPAELQTTP ESVQLQDSWV
     LGSNVPLESR HFLFKTGTGT TPLFSTATPG YTMASGSVYS PPTRPLPRNT LSRSAFKFKK
     SSKYCSWRCT ALCAVGVSVL LAILLSYFIA MHLFGLNWHL QQTENDTFEN GKVNSDTVPT
     NTVSLPSGDN GKLGGFTHEN NTIDSGELDI GRRAIQEVPP GIFWRSQLFI DQPQFLKFNI
     SLQKDALIGV YGRKGLPPSH TQYDFVELLD GSRLIAREQR NLVESERAGR QARSVSLHEA
     GFIQYLDSGI WHLAFYNDGK NPEQVSFNTI VIESVVECPR NCHGNGECVS GTCHCFPGFL
     GPDCSRAACP VLCSGNGQYS KGRCLCFSGW KGTECDVPTT QCIDPQCGGR GICIMGSCAC
     NSGYKGENCE EADCLDPGCS NHGVCIHGEC HCNPGWGGSN CEILKTMCAD QCSGHGTYLQ
     ESGSCTCDPN WTGPDCSNEI CSVDCGSHGV CMGGSCRCEE GWTGPACNQR ACHPRCAEHG
     TCKDGKCECS QGWNGEHCTI AHYLDKIVKE GCPGLCNSNG RCTLDQNGWH CVCQPGWRGA
     GCDVAMETLC TDSKDNEGDG LIDCMDPDCC LQSSCQNQPY CRGLPDPQDI ISQSLQTPSQ
     QAAKSFYDRI SFLIGSDSTH VLPGESPFNK SLASVIRGQV LTADGTPLIG VNVSFLHYSE
     YGYTITRQDG MFDLVANGGA SLTLVFERSP FLTQYHTVWI PWNVFYVMDT LVMKKEENDI
     PSCDLSGFVR PSPIIVSSPL STFFRSSPED SPIIPETQVL HEETTIPGTD LKLSYLSSRA
     AGYKSVLKIT MTQAVIPFNL MKVHLMVAVV GRLFQKWFPA SPNLAYTFIW DKTDAYNQKV
     YGLSEAVVSV GYEYESCLDL TLWEKRTAVL QGYELDASNM GGWTLDKHHV LDVQNGILYK
     GNGENQFISQ QPPVVSSIMG NGRRRSISCP SCNGQADGNK LLAPVALACG IDGSLYVGDF
     NYVRRIFPSG NVTSVLELRN KDFRHSSNPA HRYYLATDPV TGDLYVSDTN TRRIYRPKSL
     TGAKDLTKNA EVVAGTGEQC LPFDEARCGD GGKAVEATLM SPKGMAIDKN GLIYFVDGTM
     IRKVDQNGII STLLGSNDLT SARPLTCDTS MHISQVRLEW PTDLAINPMD NSIYVLDNNV
     VLQITENRQV RIAAGRPMHC QVPGVEYPVG KHAVQTTLES ATAIAVSYSG VLYITETDEK
     KINRIRQVTT DGEISLVAGI PSECDCKNDA NCDCYQSGDG YAKDAKLNAP SSLAASPDGT
     LYIADLGNIR IRAVSKNKPL LNSMNFYEVA SPTDQELYIF DINGTHQYTV SLVTGDYLYN
     FSYSNDNDVT AVTDSNGNTL RIRRDPNRMP VRVVSPDNQV IWLTIGTNGC LKSMTAQGLE
     LVLFTYHGNS GLLATKSDET GWTTFFDYDS EGRLTNVTFP TGVVTNLHGD MDKAITVDIE
     SSSREEDVSI TSNLSSIDSF YTMVQDQLRN SYQIGYDGSL RIFYASGLDS HYQTEPHVLA
     GTANPTVAKR NMTLPGENGQ NLVEWRFRKE QAQGKVNVFG RKLRVNGRNL LSVDFDRTTK
     TEKIYDDHRK FLLRIAYDTS GHPTLWLPSS KLMAVNVTYS STGQIASIQR GTTSEKVDYD
     SQGRIVSRVF ADGKTWSYTY LEKSMVLLLH SQRQYIFEYD MWDRLSAITM PSVARHTMQT
     IRSIGYYRNI YNPPESNASI ITDYNEEGLL LQTAFLGTSR RVLFKYRRQT RLSEILYDST
     RVSFTYDETA GVLKTVNLQS DGFICTIRYR QIGPLIDRQI FRFSEDGMVN ARFDYSYDNS
     FRVTSMQGVI NETPLPIDLY QFDDISGKVE QFGKFGVIYY DINQIISTAV MTYTKHFDAH
     GRIKEIQYEI FRSLMYWITI QYDNMGRVTK REIKIGPFAN TTKYAYEYDV DGQLQTVYLN
     EKIMWRYNYD LNGNLHLLNP SSSARLTPLR YDLRDRITRL GDVQYRLDED GFLRQRGTEI
     FEYSSKGLLT RVYSKGSGWT VIYRYDGLGR RVSSKTSLGQ HLQFFYADLT YPTRITHVYN
     HSSSEITSLY YDLQGHLFAM EISSGDEFYI ASDNTGTPLA VFSSNGLMLK QTQYTAYGEI
     YFDSNVDFQL VIGFHGGLYD PLTKLIHFGE RDYDILAGRW TTPDIEIWKR IGKDPAPFNL
     YMFRNNNPAS KIHDVKDYIT DVNSWLVTFG FHLHNAIPGF PVPKFDLTEP SYELVKSQQW
     EDVPPIFGVQ QQVARQAKAF LSLGKMAEVQ VSRRKAGAEQ SWLWFATVKS LIGKGVMLAV
     SQGRVQTNVL NIANEDCIKV AAVLNNAFYL ENLHFTIEGK DTHYFIKTTT PESDLGTLRL
     TSGRKALENG INVTVSQSTT VVNGRTRRFA DVEMQFGALA LHVRYGMTLD EEKARILEQA
     RQRALARAWA REQQRVRDGE EGARLWTEGE KRQLLSAGKV QGYDGYYVLS VEQYPELADS
     ANNIQFLRQS EIGKR
//
ID   VATG2_MOUSE             Reviewed;         118 AA.
AC   Q9WTT4;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=V-type proton ATPase subunit G 2;
DE            Short=V-ATPase subunit G 2;
DE   AltName: Full=V-ATPase 13 kDa subunit 2;
DE   AltName: Full=Vacuolar proton pump subunit G 2;
GN   Name=Atp6v1g2; Synonyms=Atp6g2, Ng38;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129;
RX   PubMed=14656967; DOI=10.1101/gr.1736803;
RA   Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
RA   Campbell R.D., Hood L.;
RT   "Analysis of the gene-dense major histocompatibility complex class III
RT   region and its comparison to mouse.";
RL   Genome Res. 13:2621-2636(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Catalytic subunit of the peripheral V1 complex of
CC       vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying
CC       a variety of intracellular compartments in eukaryotic cells.
CC   -!- SUBUNIT: V-ATPase is an heteromultimeric enzyme composed of a
CC       peripheral catalytic V1 complex (components A to H) attached to an
CC       integral membrane V0 proton pore complex (components: a, c, c',
CC       c'' and d) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Melanosome (By similarity).
CC   -!- SIMILARITY: Belongs to the V-ATPase G subunit family.
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DR   EMBL; AC007080; AAD30176.1; -; Genomic_DNA.
DR   EMBL; AK011945; BAB27931.1; -; mRNA.
DR   EMBL; BC020190; AAH20190.1; -; mRNA.
DR   EMBL; BC062380; AAH62380.1; -; mRNA.
DR   IPI; IPI00123817; -.
DR   RefSeq; NP_075668.1; NM_023179.3.
DR   UniGene; Mm.396107; -.
DR   STRING; Q9WTT4; -.
DR   PRIDE; Q9WTT4; -.
DR   Ensembl; ENSMUST00000068261; ENSMUSP00000069482; ENSMUSG00000024403.
DR   GeneID; 66237; -.
DR   KEGG; mmu:66237; -.
DR   UCSC; uc008cgy.1; mouse.
DR   CTD; 66237; -.
DR   MGI; MGI:1913487; Atp6v1g2.
DR   GeneTree; ENSGT00390000011172; -.
DR   HOGENOM; HBG621942; -.
DR   HOVERGEN; HBG057827; -.
DR   InParanoid; Q9WTT4; -.
DR   OMA; HPNYRIA; -.
DR   OrthoDB; EOG483D67; -.
DR   PhylomeDB; Q9WTT4; -.
DR   BRENDA; 3.6.3.14; 244.
DR   NextBio; 321055; -.
DR   ArrayExpress; Q9WTT4; -.
DR   Bgee; Q9WTT4; -.
DR   CleanEx; MM_ATP6V1G2; -.
DR   Genevestigator; Q9WTT4; -.
DR   GermOnline; ENSMUSG00000024403; Mus musculus.
DR   GO; GO:0030285; C:integral to synaptic vesicle membrane; IDA:MGI.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IPI:MGI.
DR   GO; GO:0008553; F:hydrogen-exporting ATPase activity, phosphorylative mechanism; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR005124; V-ATPase_G.
DR   PANTHER; PTHR12713; V-ATPase_G; 1.
DR   Pfam; PF03179; V-ATPase_G; 1.
DR   TIGRFAMs; TIGR01147; V_ATP_synt_G; 1.
PE   2: Evidence at transcript level;
KW   Hydrogen ion transport; Ion transport; Transport.
FT   CHAIN         1    118       V-type proton ATPase subunit G 2.
FT                                /FTId=PRO_0000192902.
SQ   SEQUENCE   118 AA;  13651 MW;  32479E10DFF11078 CRC64;
     MASQTQGIQQ LLQAEKRAAE KVADARKRKA RRLKQAKEEA QMEVEQYRRE REQEFQSKQQ
     AAMGSQGNLS AEVEQATRRQ VQGMQSSQQR NRERVLAQLL GMVCEVRPQV HPNYRVTV
//
ID   PHF2_MOUSE              Reviewed;        1096 AA.
AC   Q9WTU0; Q6A023; Q80WA8;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   15-AUG-2003, sequence version 2.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=PHD finger protein 2;
DE   AltName: Full=GRC5;
GN   Name=Phf2; Synonyms=Kiaa0662;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99160472; PubMed=10051327; DOI=10.1007/s003359900989;
RA   Hasenpusch-Theil K., Chadwick B.P., Theil T., Heath S.K.,
RA   Wilkinson D.G., Frischauf A.M.;
RT   "PHF2, a novel PHD finger gene located on human chromosome 9q22.";
RL   Mamm. Genome 10:294-298(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Limb;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 59-1096.
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-677, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-734, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-458 AND SER-459, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   FUNCTION.
RX   PubMed=20129925; DOI=10.1074/jbc.C109.097667;
RA   Wen H., Li J., Song T., Lu M., Kan P.Y., Lee M.G., Sha B., Shi X.;
RT   "Recognition of histone H3K4 trimethylation by the plant homeodomain
RT   of PHF2 modulates histone demethylation.";
RL   J. Biol. Chem. 285:9322-9326(2010).
CC   -!- FUNCTION: Probable regulator of histone methyltransferase
CC       complexes. Recruited to trimethylated 'Lys-4' of histone H3
CC       (H3K4me3) at rDNA promoters and promotes expression of rDNA (By
CC       similarity). Was reported to have histone demethylase activity by
CC       itself and specifically demethylate monomethylated 'Lys-9' of
CC       histone H3 (H3K9me1), an epigenetic repressive mark. However, this
CC       activity is unclear in vivo and requires additional evidence.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity).
CC   -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me2
CC       and H3K4me3 (By similarity).
CC   -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family.
CC       JHDM1D subfamily.
CC   -!- SIMILARITY: Contains 1 JmjC domain.
CC   -!- SIMILARITY: Contains 1 PHD-type zinc finger.
CC   -!- CAUTION: Although highly similar to the histone demethylases
CC       JHDM1D and PHF8, lacks the conserved active His in position 321,
CC       which is replaced by a Tyr. Its activity as histone
CC       methyltransferase reported by a publication is therefore unsure
CC       (PubMed:20129925). May rather act as a regulator of histone
CC       methyltransferase complexes, as in the case of JARID2.
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DR   EMBL; AF043726; AAD21792.1; -; mRNA.
DR   EMBL; BC051633; AAH51633.1; -; mRNA.
DR   EMBL; AK172995; BAD32273.1; -; mRNA.
DR   IPI; IPI00123868; -.
DR   RefSeq; NP_035208.2; NM_011078.3.
DR   UniGene; Mm.480579; -.
DR   ProteinModelPortal; Q9WTU0; -.
DR   SMR; Q9WTU0; 1-444.
DR   PhosphoSite; Q9WTU0; -.
DR   PRIDE; Q9WTU0; -.
DR   Ensembl; ENSMUST00000035540; ENSMUSP00000047308; ENSMUSG00000038025.
DR   GeneID; 18676; -.
DR   KEGG; mmu:18676; -.
DR   UCSC; uc007qin.1; mouse.
DR   CTD; 18676; -.
DR   MGI; MGI:1338034; Phf2.
DR   GeneTree; ENSGT00550000074396; -.
DR   HOGENOM; HBG445752; -.
DR   HOVERGEN; HBG045631; -.
DR   InParanoid; Q9WTU0; -.
DR   OMA; EPPSPIE; -.
DR   OrthoDB; EOG46HG91; -.
DR   PhylomeDB; Q9WTU0; -.
DR   NextBio; 294702; -.
DR   ArrayExpress; Q9WTU0; -.
DR   Bgee; Q9WTU0; -.
DR   CleanEx; MM_PHF2; -.
DR   Genevestigator; Q9WTU0; -.
DR   GermOnline; ENSMUSG00000038025; Mus musculus.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0032454; F:histone demethylase activity (H3-K9 specific); TAS:UniProtKB.
DR   GO; GO:0035064; F:methylated histone residue binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0061188; P:negative regulation of chromatin silencing at rDNA; ISS:UniProtKB.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR013129; TF_JmjC.
DR   InterPro; IPR003347; TF_JmjC_AAH.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Metal-binding; Nucleus; Phosphoprotein;
KW   Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1   1096       PHD finger protein 2.
FT                                /FTId=PRO_0000059291.
FT   DOMAIN      197    353       JmjC.
FT   ZN_FING       5     56       PHD-type.
FT   COMPBIAS    487    606       Lys-rich.
FT   COMPBIAS    959   1021       Ser-rich.
FT   MOD_RES     458    458       Phosphoserine.
FT   MOD_RES     459    459       Phosphoserine.
FT   MOD_RES     536    536       Phosphoserine (By similarity).
FT   MOD_RES     677    677       Phosphoserine.
FT   MOD_RES     734    734       Phosphoserine.
FT   MOD_RES     876    876       Phosphoserine (By similarity).
FT   MOD_RES     893    893       Phosphoserine (By similarity).
FT   CONFLICT    938    938       Q -> L (in Ref. 1; AAD21792).
FT   CONFLICT    955    955       P -> S (in Ref. 3; BAD32273).
SQ   SEQUENCE   1096 AA;  120814 MW;  778B822C007D8860 CRC64;
     MATVPVYCVC RLPYDVTRFM IECDACKDWF HGSCVGVEEE EAPDIDIYHC PNCEKTHGKS
     TLKKKRTWHK HGPGPTPDVK PVQNGSQLFI KELRSRTFPS AEDVVSRVPG SQLTVGYMEE
     HGFTEPILVP KKDGLGLAVP APTFYVSDVE NYVGPERSVD VTDVTKQKDC KMKLKEFVDY
     YYSTNRKRVL NVTNLEFSDT RMSSFVEPPD IVKKLSWVEN YWPDDALLAK PKVTKYCLIC
     VKDSYTDFHI DSGGASAWYH VLKGEKIFYL IRPASANISL YERWRSASNH SEMFFADQVD
     RCYKCTVKQG QTLFIPSGWI YATLTPVDCL AFAGHFLHSL SVEMQMRAYE VERRLKLGSL
     TQFPNFETAC WYMGKHLLEA FKGSHKSGKQ LPPHLVQGAK ILNGAFRSWT KKQALAEHED
     ELPEHFRPSQ LIKDLAKEIR LSENASKTVR PEVNAAASSD EVCDGDREKE EPPSPVETTP
     PRSLLEKVSK KKTSKTVKMP KPSKIPKPPK SPKPPKTLKL KDGSKKKGKK CKESASPTIP
     NLDLLEAHTK EALTKMEPPK KGKTPKSVLS VPNKDTVHTQ NDMERLEIRE QTKSKSEAKW
     KYKNSKPDSL LKMEEEQRLE KSPLAGNKDK FSFSFSNRKL LGSKALRPPS SPGVFGALQS
     FKEDKAKPVR DEYEYVSDDG ELKIDEFPIR RKKSAPKRDL SFLLDKKEAL LMPTSKPKLD
     SAVYKSDDSS DEGSLHIDTD TKPGRNAKVK KESGSSAAGI LDLLQASEEV GALEYNPNSQ
     PPASPSTQEA IQGMLSMANL QASDSCLQTT WGTGQAKGGS LAAHGARKIG GGNKGTGKRL
     LKRTAKNSVD LEDYEEQDHL DACFKDSDYV YPSLESDEDN PVFKSRSKKR KGSDDAPYSP
     TARVGPSVPR QDRPVREGTR VASIETGLAA AAAKLSQQEE QKNRKKKNTK RKPAPNTASP
     SISTSASAST GTTSASTTPA STTPASTTPA STTPASTSTA SSQASQEGSS PEPPPESHSS
     SLADHEYTAA GTFSGSQAGR ASQPMAPGVF LTQRRPSASS PNNTAAKGKR TKKGMATAKQ
     RLGKILKIHR NGKLLL
//
ID   SCN8A_MOUSE             Reviewed;        1978 AA.
AC   Q9WTU3; Q3TYI3; Q60828; Q60858; Q62449;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Sodium channel protein type 8 subunit alpha;
DE   AltName: Full=Sodium channel protein type VIII subunit alpha;
DE   AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.6;
GN   Name=Scn8a; Synonyms=Nbna1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99047535; PubMed=9828131; DOI=10.1006/geno.1998.5550;
RA   Plummer N.W., Galt J., Jones J.M., Burgess D.L., Sprunger L.K.,
RA   Kohrman D.C., Meisler M.H.;
RT   "Exon organization, coding sequence, physical mapping, and polymorphic
RT   intragenic markers for the human neuronal sodium channel gene SCN8A.";
RL   Genomics 54:287-296(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP   DISEASE.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   MEDLINE=95400328; PubMed=7670495; DOI=10.1038/ng0895-461;
RA   Burgess D.L., Kohrman D.C., Galt J., Plummer N.W., Jones J.M.,
RA   Spear B., Meisler M.H.;
RT   "Mutation of a new sodium channel gene, Scn8a, in the mouse mutant
RT   'motor endplate disease'.";
RL   Nat. Genet. 10:461-465(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-804, AND VARIANT LEU-5.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 93-205, AND DISEASE.
RC   STRAIN=129/Sv; TISSUE=Brain;
RX   MEDLINE=96291923; PubMed=8663325; DOI=10.1074/jbc.271.29.17576;
RA   Kohrman D.C., Harris J.B., Meisler M.H.;
RT   "Mutation detection in the med and medJ alleles of the sodium channel
RT   Scn8a. Unusual splicing due to a minor class AT-AC intron.";
RL   J. Biol. Chem. 271:17576-17581(1996).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1411-1686.
RA   Fan Z., Kyle J.W., Makielski J.C.;
RT   "A putative novel Na channel alpha subunit cDNA isolated from mouse
RT   NB2a neuroblastoma cells.";
RL   Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   INTERACTION WITH NEDD4 AND NEDD4L.
RX   PubMed=15123669; DOI=10.1074/jbc.M402820200;
RA   Fotia A.B., Ekberg J., Adams D.J., Cook D.I., Poronnik P., Kumar S.;
RT   "Regulation of neuronal voltage-gated sodium channels by the
RT   ubiquitin-protein ligases Nedd4 and Nedd4-2.";
RL   J. Biol. Chem. 279:28930-28935(2004).
RN   [7]
RP   ALTERNATIVE SPLICING (ISOFORMS 1; 4 AND 5).
RC   TISSUE=Brain, and Fetal brain;
RX   MEDLINE=97442476; PubMed=9295353; DOI=10.1074/jbc.272.38.24008;
RA   Plummer N.W., McBurney M.W., Meisler M.H.;
RT   "Alternative splicing of the sodium channel SCN8A predicts a truncated
RT   two-domain protein in fetal brain and non-neuronal cells.";
RL   J. Biol. Chem. 272:24008-24015(1997).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=19136557; DOI=10.1074/jbc.M801892200;
RA   Carrithers M.D., Chatterjee G., Carrithers L.M., Offoha R.,
RA   Iheagwara U., Rahner C., Graham M., Waxman S.G.;
RT   "Regulation of podosome formation in macrophages by a splice variant
RT   of the sodium channel SCN8A.";
RL   J. Biol. Chem. 284:8114-8126(2009).
RN   [9]
RP   VARIANT MEDJO THR-1317, AND VARIANT LEU-5.
RC   STRAIN=DBA/2WyDi;
RX   MEDLINE=96424513; PubMed=8815882;
RA   Kohrman D.C., Smith M.R., Goldin A.L., Harris J., Meisler M.H.;
RT   "A missense mutation in the sodium channel Scn8a is responsible for
RT   cerebellar ataxia in the mouse mutant jolting.";
RL   J. Neurosci. 16:5993-5999(1996).
RN   [10]
RP   DISEASE.
RX   MEDLINE=21423786; PubMed=11532991; DOI=10.1093/hmg/10.17.1819;
RA   De Repentigny Y., Cote P.D., Pool M., Bernier G., Girard S.,
RA   Vidal S.M., Kothary R.;
RT   "Pathological and genetic analysis of the degenerating muscle (dmu)
RT   mouse: a new allele of Scn8a.";
RL   Hum. Mol. Genet. 10:1819-1827(2001).
CC   -!- FUNCTION: Mediates the voltage-dependent sodium ion permeability
CC       of excitable membranes. Assuming opened or closed conformations in
CC       response to the voltage difference across the membrane, the
CC       protein forms a sodium-selective channel through which Na(+) ions
CC       may pass in accordance with their electrochemical gradient. In
CC       macrophages, isoform 5 may participate in the control of podosome
CC       and invadopodia formation.
CC   -!- SUBUNIT: Interacts with NEDD4 and NEDD4L.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1; Synonyms=18A;
CC         IsoId=Q9WTU3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9WTU3-2; Sequence=VSP_050594;
CC       Name=3;
CC         IsoId=Q9WTU3-3; Sequence=VSP_050595;
CC       Name=4; Synonyms=18N;
CC         IsoId=Q9WTU3-4; Sequence=VSP_050596, VSP_050597;
CC       Name=5;
CC         IsoId=Q9WTU3-5; Sequence=VSP_050598;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, cerebellum and spinal
CC       cord. Isoform 5 may be expressed in non-neuronal tissues, such as
CC       peritoneal macrophages.
CC   -!- DOMAIN: The sequence contains 4 internal repeats, each with 5
CC       hydrophobic segments (S1,S2,S3,S5,S6) and one positively charged
CC       segment (S4). Segments S4 are probably the voltage-sensors and are
CC       characterized by a series of positively charged amino acids at
CC       every third position.
CC   -!- PTM: May be ubiquitinated by NEDD4L; which would promote its
CC       endocytosis (By similarity).
CC   -!- DISEASE: Note=Defects in Scn8a are the cause of motor endplate
CC       disease (med). Med is a recessive neuromuscular disorder that is
CC       characterized by lack of signal transmission at the neuromuscular
CC       junction, excess preterminal arborization and degeneration of
CC       cerebellar Purkinje cells. It produces early onset progressive
CC       paralysis of hind limbs, severe muscle atrophy and juvenile
CC       lethality.
CC   -!- DISEASE: Note=Defects in Scn8a are the cause of the jolting mutant
CC       (medjo), a mild form of motor endplate disease which is
CC       characterized by the absence of spontaneous, regular, simple
CC       discharges from Purkinje cells. After 3 weeks of age, jolting mice
CC       are unsteady and have wide-based gait and a rhythmical tremor of
CC       head and neck induced by attempted movement.
CC   -!- DISEASE: Note=Defects in Scn8a are a cause of degenerating muscle
CC       (dmu). Dmu is an autosomal recessive neuromuscular disorder that
CC       is characterized by skeletal and cardiac muscle degeneration. It
CC       produces early onset progressive loss of mobility of the hind
CC       limbs and subsequent lethality in the first month of life.
CC   -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC       Nav1.6/SCN8A subfamily.
CC   -!- SIMILARITY: Contains 1 IQ domain.
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DR   EMBL; AF049617; AAD20438.1; -; mRNA.
DR   EMBL; U26707; AAC52242.1; -; mRNA.
DR   EMBL; AK158609; BAE34580.1; -; mRNA.
DR   EMBL; U59964; AAC52708.1; -; Genomic_DNA.
DR   EMBL; U59963; AAC52708.1; JOINED; Genomic_DNA.
DR   EMBL; U23158; AAA65599.1; -; mRNA.
DR   IPI; IPI00337974; -.
DR   IPI; IPI00337975; -.
DR   IPI; IPI00337976; -.
DR   IPI; IPI00337977; -.
DR   IPI; IPI00337978; -.
DR   RefSeq; NP_001070967.1; NM_001077499.1.
DR   RefSeq; NP_035453.2; NM_011323.2.
DR   UniGene; Mm.385012; -.
DR   ProteinModelPortal; Q9WTU3; -.
DR   STRING; Q9WTU3; -.
DR   PhosphoSite; Q9WTU3; -.
DR   PRIDE; Q9WTU3; -.
DR   Ensembl; ENSMUST00000082209; ENSMUSP00000080842; ENSMUSG00000023033.
DR   Ensembl; ENSMUST00000108907; ENSMUSP00000104535; ENSMUSG00000023033.
DR   Ensembl; ENSMUST00000108908; ENSMUSP00000104536; ENSMUSG00000023033.
DR   Ensembl; ENSMUST00000108909; ENSMUSP00000104537; ENSMUSG00000023033.
DR   Ensembl; ENSMUST00000108910; ENSMUSP00000104538; ENSMUSG00000023033.
DR   GeneID; 20273; -.
DR   KEGG; mmu:20273; -.
DR   UCSC; uc007xsh.1; mouse.
DR   CTD; 20273; -.
DR   MGI; MGI:103169; Scn8a.
DR   eggNOG; roNOG10225; -.
DR   GeneTree; ENSGT00560000076721; -.
DR   HOVERGEN; HBG053100; -.
DR   OrthoDB; EOG40S0DS; -.
DR   ArrayExpress; Q9WTU3; -.
DR   Bgee; Q9WTU3; -.
DR   CleanEx; MM_SCN8A; -.
DR   Genevestigator; Q9WTU3; -.
DR   GermOnline; ENSMUSG00000023033; Mus musculus.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; IC:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; NAS:UniProtKB.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0007517; P:muscle organ development; IMP:MGI.
DR   GO; GO:0009636; P:response to toxin; IDA:MGI.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR008054; Na_channel_a8su.
DR   InterPro; IPR001696; Na_channel_asu.
DR   InterPro; IPR010526; Na_trans_assoc.
DR   Pfam; PF00520; Ion_trans; 4.
DR   Pfam; PF00612; IQ; 1.
DR   Pfam; PF06512; Na_trans_assoc; 1.
DR   PRINTS; PR00170; NACHANNEL.
DR   PRINTS; PR01667; NACHANNEL8.
DR   SMART; SM00015; IQ; 1.
DR   PROSITE; PS50096; IQ; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Disease mutation; Glycoprotein;
KW   Ion transport; Ionic channel; Membrane; Nucleotide-binding;
KW   Polymorphism; Repeat; Sodium; Sodium channel; Sodium transport;
KW   Transmembrane; Transmembrane helix; Transport; Ubl conjugation;
KW   Voltage-gated channel.
FT   CHAIN         1   1978       Sodium channel protein type 8 subunit
FT                                alpha.
FT                                /FTId=PRO_0000048501.
FT   TRANSMEM    128    151       Helical; Name=S1 of repeat I;
FT                                (Potential).
FT   TRANSMEM    160    179       Helical; Name=S2 of repeat I;
FT                                (Potential).
FT   TRANSMEM    193    211       Helical; Name=S3 of repeat I;
FT                                (Potential).
FT   TRANSMEM    218    237       Helical; Name=S4 of repeat I;
FT                                (Potential).
FT   TRANSMEM    253    277       Helical; Voltage-sensor; Name=S5 of
FT                                repeat I; (Potential).
FT   TRANSMEM    388    413       Helical; Name=S6 of repeat I;
FT                                (Potential).
FT   TRANSMEM    746    770       Helical; Name=S1 of repeat II;
FT                                (Potential).
FT   TRANSMEM    782    805       Helical; Name=S2 of repeat II;
FT                                (Potential).
FT   TRANSMEM    814    833       Helical; Name=S3 of repeat II;
FT                                (Potential).
FT   TRANSMEM    840    860       Helical; Voltage-sensor; Name=S4 of
FT                                repeat II; (Potential).
FT   TRANSMEM    876    896       Helical; Name=S5 of repeat II;
FT                                (Potential).
FT   TRANSMEM    950    975       Helical; Name=S6 of repeat II;
FT                                (Potential).
FT   TRANSMEM   1192   1215       Helical; Name=S1 of repeat III;
FT                                (Potential).
FT   TRANSMEM   1229   1254       Helical; Name=S2 of repeat III;
FT                                (Potential).
FT   TRANSMEM   1261   1282       Helical; Name=S3 of repeat III;
FT                                (Potential).
FT   TRANSMEM   1287   1308       Helical; Voltage-sensor; Name=S4 of
FT                                repeat III; (Potential).
FT   TRANSMEM   1328   1349       Helical; Name=S5 of repeat III;
FT                                (Potential).
FT   TRANSMEM   1436   1462       Helical; Name=S6 of repeat III;
FT                                (Potential).
FT   TRANSMEM   1516   1539       Helical; Name=S1 of repeat IV;
FT                                (Potential).
FT   TRANSMEM   1551   1574       Helical; Name=S2 of repeat IV;
FT                                (Potential).
FT   TRANSMEM   1581   1604       Helical; Name=S3 of repeat IV;
FT                                (Potential).
FT   TRANSMEM   1615   1636       Helical; Voltage-sensor; Name=S4 of
FT                                repeat IV; (Potential).
FT   TRANSMEM   1652   1674       Helical; Name=S5 of repeat IV;
FT                                (Potential).
FT   TRANSMEM   1740   1764       Helical; Name=S6 of repeat IV;
FT                                (Potential).
FT   REPEAT      114    442       I.
FT   REPEAT      733   1005       II.
FT   REPEAT     1178   1493       III.
FT   REPEAT     1502   1799       IV.
FT   DOMAIN     1893   1922       IQ.
FT   NP_BIND     891    898       ATP (Potential).
FT   CARBOHYD    215    215       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    289    289       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    295    295       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    308    308       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    326    326       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    544    544       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    640    640       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    875    875       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1045   1045       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1062   1062       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1089   1089       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1356   1356       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1370   1370       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1381   1381       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1766   1766       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     428    673       Missing (in isoform 2).
FT                                /FTId=VSP_050594.
FT   VAR_SEQ     664    664       E -> EVKIDKAATDS (in isoform 3).
FT                                /FTId=VSP_050595.
FT   VAR_SEQ    1272   1312       Missing (in isoform 5).
FT                                /FTId=VSP_050598.
FT   VAR_SEQ    1273   1280       SLVSLIAN -> PLSLSGLI (in isoform 4).
FT                                /FTId=VSP_050596.
FT   VAR_SEQ    1281   1978       Missing (in isoform 4).
FT                                /FTId=VSP_050597.
FT   VARIANT       5      5       V -> L.
FT   VARIANT    1317   1317       A -> T (in medjo).
FT   CONFLICT    207    207       V -> I (in Ref. 3; BAE34580).
FT   CONFLICT    212    212       D -> N (in Ref. 3; BAE34580).
FT   CONFLICT    554    554       P -> T (in Ref. 3; BAE34580).
FT   CONFLICT    596    596       G -> D (in Ref. 3; BAE34580).
FT   CONFLICT   1498   1498       P -> A (in Ref. 5; AAA65599).
FT   CONFLICT   1504   1504       R -> E (in Ref. 5; AAA65599).
SQ   SEQUENCE   1978 AA;  225141 MW;  9EA4A8E610707220 CRC64;
     MAARVLAPPG PDSFKPFTPE SLANIERRIA ESKLKKPPKA DGSHREDDED SKPKPNSDLE
     AGKSLPFIYG DIPQGLVAVP LEDFDPYYLT QKTFVVLNRG KTLFRFSATP ALYILSPFNL
     IRRIAIKILI HSVFSMIIMC TILTNCVFMT FSNPPEWSKN VEYTFTGIYT FESLVKIIAR
     GFCIDGFTFL RDPWNWLDFS VIMMAYVTEF VDLGNVSALR TFRVLRALKT ISVIPGLKTI
     VGALIQSVKK LSDVMILTVF CLSVFALIGL QLFMGNLRNK CVVWPINFNE SYLENGTRGF
     DWEEYINNKT NFYMVPGMLE PLLCGNSSDA GQCPEGFQCM KAGRNPNYGY TSFDTFSWAF
     LALFRLMTQD YWENLYQLTL RAAGKTYMIF FVLVIFVGSF YLVNLILAVV AMAYEEQNQA
     TLEEAEQKEA EFKAMLEQLK KQQEEAQAAA MATSAGTVSE DAIEEEGEDG VGSPRSSSEL
     SKLSSKSAKE RRNRRKKRKQ KELSEGEEKG DPEKVFKSES EDGMRRKAFR LPDNRIGRKF
     SIMNQSLLSI PGSPFLSRHN SKSSIFSFRG PGRFRDPGSE NEFADDEHST VEESEGRRDS
     LFIPIRARER RSSYSGYSGY SQCSRSSRIF PSLRRSVKRN STVDCNGVVS LIGPGSHIGR
     LLPEATTEVE IKKKGPGSLL VSMEQLASYG RKDRINSIMS VVTNTLVEEL EESQRKCPPC
     WYKFANTFLI WECHPYWIKL KEIVNLIVMD PFVDLAITIC IVLNTLFMAM EHHPMTPQFE
     HVLAVGNLVF TGIFTAEMFL KLIAMDPYYY FQEGWNIFDG FIVSLSLMEL GLADVEGLSV
     LRSFRLLRVF KLAKSWPTLN MLIKIIGNSV GALGNLTLVL AIIVFIFAVV GMQLFGKSYK
     ECVCKISQEC KLPRWHMNDF FHSFLIVFRV LCGEWIETMW DCMEVAGQAM CLIVFMMVMV
     IGNLVVLNLF LALLLSSFSA DNLAATDDDG EMNNLQISVI RIKKGVAWAK VKVHAFMQAH
     FKQREADEVK PLDELYEKKA NCIANHTGVD IHRNGDFQKN GNGTTSGIGS SVEKYIIDED
     HMSFINNPNL TVRVPIAVGE SDFENLNTED VSSESDPEGS KDKLDDTSSS EGSTIDIKPE
     VEEVPVEQPE EYLDPDACFT EGCVQRFKCC QVNIEEGLGK SWWILRKTCF LIVEHNWFET
     FIIFMILLSS GALAFEDIYI EQRKTIRTIL EYADKVFTYI FILEMLLKWT AYGFVKFFTN
     AWCWLDFLIV AVSLVSLIAN ALGYSELGAI KSLRTLRALR PLRALSRFEG MRVVVNALVG
     AIPSIMNVLL VCLIFWLIFS IMGVNLFAGK YHYCFNETSE IRFEIDEVNN KTDCEKLMEG
     NNTEIRWKNV KINFDNVGAG YLALLQVATF KGWMDIMYAA VDSRKPDEQP DYEGNIYMYI
     YFVIFIIFGS FFTLNLFIGV IIDNFNQQKK KFGGQDIFMT EEQKKYYNAM KKLGSKKPQK
     PIPRPLNKIQ GIVFDFVTQQ AFDIVIMMLI CLNMVTMMVE TDTQSKQMEN ILYWINLVFV
     IFFTCECVLK MFALRHYYFT IGWNIFDFVV VILSIVGMFL ADIIEKYFVS PTLFRVIRLA
     RIGRILRLIK GAKGIRTLLF ALMMSLPALF NIGLLLFLVM FIFSIFGMSN FAYVKHEAGI
     DDMFNFETFG NSMICLFQIT TSAGWDGLLL PILNRPPDCS LDKEHPGSGF KGDCGNPSVG
     IFFFVSYIII SFLIVVNMYI AIILENFSVA TEESADPLSE DDFETFYEIW EKFDPDATQF
     IEYCKLADFA DALEHPLRVP KPNTIELIAM DLPMVSGDRI HCLDILFAFT KRVLGDSGEL
     DILRQQMEER FVASNPSKVS YEPITTTLRR KQEEVSAVVL QRAYRGHLAR RGFICRKITS
     NKLENGGTHR EKKESTPSTA SLPSYDSVTK PDKEKQQRAE EGRRERAKRQ KEVRESKC
//
ID   MK09_MOUSE              Reviewed;         423 AA.
AC   Q9WTU6; Q5NCK9; Q5NCL5; Q8C097; Q8VDD2; Q9WTU4; Q9WTU5;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 2.
DT   08-MAR-2011, entry version 114.
DE   RecName: Full=Mitogen-activated protein kinase 9;
DE            Short=MAP kinase 9;
DE            Short=MAPK 9;
DE            EC=2.7.11.24;
DE   AltName: Full=Stress-activated protein kinase JNK2;
DE   AltName: Full=c-Jun N-terminal kinase 2;
GN   Name=Mapk9; Synonyms=Jnk2, Prkm9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1; ALPHA-2; BETA-1 AND
RP   BETA-2), FUNCTION, AND INDUCTION.
RX   MEDLINE=99021480; PubMed=9806643; DOI=10.1016/S1074-7613(00)80640-8;
RA   Yang D.D., Conze D., Whitmarsh A.J., Barrett T., Davis R.J.,
RA   Rincon M., Flavell R.A.;
RT   "Differentiation of CD4+ T cells to Th1 cells requires MAP kinase
RT   JNK2.";
RL   Immunity 9:575-585(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA-1).
RC   TISSUE=Brain;
RX   MEDLINE=99455010; PubMed=10523642;
RA   Ito M., Yoshioka K., Akechi M., Yamashita S., Takamatsu N.,
RA   Sugiyama K., Hibi M., Nakabeppu Y., Shiba T., Yamamoto K.;
RT   "JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein
RT   that functions as a scaffold factor in the JNK signaling pathway.";
RL   Mol. Cell. Biol. 19:7539-7548(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS ALPHA-1; ALPHA-2; BETA-1
RP   AND BETA-2), AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   MEDLINE=20136941; PubMed=10674476;
RA   Casanova E., Callejo A.I., Calvo P., Chinchetru M.A.;
RT   "Analysis of splicing of four mouse JNK/SAPKalpha variants.";
RL   NeuroReport 11:305-309(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-2).
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA-2).
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   FUNCTION, ENZYME REGULATION, AND INDUCTION.
RC   TISSUE=Embryonic stem cell, and T-cell;
RX   MEDLINE=20269361; PubMed=10811224; DOI=10.1038/35011091;
RA   Dong C., Yang D.D., Tournier C., Whitmarsh A.J., Xu J., Davis R.J.,
RA   Flavell R.A.;
RT   "JNK is required for effector T-cell function but not for T-cell
RT   activation.";
RL   Nature 405:91-94(2000).
RN   [8]
RP   SUBUNIT.
RC   TISSUE=Hippocampus;
RX   MEDLINE=21446505; PubMed=11562351; DOI=10.1101/gad.922801;
RA   Whitmarsh A.J., Kuan C.-Y., Kennedy N.J., Kelkar N., Haydar T.F.,
RA   Mordes J.P., Appel M., Rossini A.A., Jones S.N., Flavell R.A.,
RA   Rakic P., Davis R.J.;
RT   "Requirement of the JIP1 scaffold protein for stress-induced JNK
RT   activation.";
RL   Genes Dev. 15:2421-2432(2001).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183 AND TYR-185, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-185, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Responds to activation by environmental stress and pro-
CC       inflammatory cytokines by phosphorylating a number of
CC       transcription factors, primarily components of AP-1 such as c-Jun
CC       and ATF2 and thus regulates AP-1 transcriptional activity. In T-
CC       cells, JNK1 and JNK2 are required for polarized differentiation of
CC       T-helper cells into Th1 cells.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Activated by threonine and tyrosine
CC       phosphorylation by either of two dual specificity kinases, MAP2K4
CC       and MAP2K7. Inhibited by dual specificity phosphatases, such as
CC       DUSP1.
CC   -!- SUBUNIT: Interacts with MECOM. Binds to at least four scaffolding
CC       proteins, MAPK8IP1/JIP-1, MAPK8IP2/JIP-2, MAPK8IP3/JIP-3/JSAP1 and
CC       SPAG9/MAPK8IP4/JIP-4. These proteins also bind other components of
CC       the JNK signaling pathway. Interacts with NFATC4. Interacts with
CC       ATF7; the interaction does not phosphorylate ATF7 but acts as a
CC       docking site for ATF7-associated partners such as JUN (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=Alpha-2;
CC         IsoId=Q9WTU6-1; Sequence=Displayed;
CC       Name=Alpha-1;
CC         IsoId=Q9WTU6-2; Sequence=VSP_004837;
CC       Name=Beta-1;
CC         IsoId=Q9WTU6-3; Sequence=VSP_004836, VSP_004837;
CC       Name=Beta-2;
CC         IsoId=Q9WTU6-4; Sequence=VSP_004836;
CC   -!- TISSUE SPECIFICITY: All four isoforms are widely distributed in
CC       brain. Isoforms alpha-1 and alpha-2 are predominantly expressed in
CC       hippocampus, cerebral cortex, caudate-putamen, amygdala and the
CC       granule layer of the cerebellum. Alpha-1 is more abundant than
CC       alpha-2 in the periaqueductal region and the substantia nigra.
CC   -!- INDUCTION: In T-cells, following T-cell receptor (TCR) activation.
CC       Levels peak 48 hours after TCR and CD-28 costimulation.
CC   -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC       whose phosphorylation activates the MAP kinases.
CC   -!- PTM: Dually phosphorylated on Thr-183 and Tyr-185, which activates
CC       the enzyme.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. MAP kinase subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF052466; AAD22576.1; -; mRNA.
DR   EMBL; AF052467; AAD22577.1; -; mRNA.
DR   EMBL; AF052468; AAD22578.1; -; mRNA.
DR   EMBL; AF052469; AAD22579.1; -; mRNA.
DR   EMBL; AB005664; BAA85876.1; -; mRNA.
DR   EMBL; AJ315339; CAC88132.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AJ315340; CAC88132.1; JOINED; Genomic_DNA.
DR   EMBL; AJ315341; CAC88132.1; JOINED; Genomic_DNA.
DR   EMBL; AJ315342; CAC88132.1; JOINED; Genomic_DNA.
DR   EMBL; AJ315343; CAC88132.1; JOINED; Genomic_DNA.
DR   EMBL; AJ315344; CAC88132.1; JOINED; Genomic_DNA.
DR   EMBL; AJ315345; CAC88132.1; JOINED; Genomic_DNA.
DR   EMBL; AJ315346; CAC88132.1; JOINED; Genomic_DNA.
DR   EMBL; AJ315347; CAC88132.1; JOINED; Genomic_DNA.
DR   EMBL; AJ315348; CAC88132.1; JOINED; Genomic_DNA.
DR   EMBL; AJ315349; CAC88132.1; JOINED; Genomic_DNA.
DR   EMBL; AJ315350; CAC88132.1; JOINED; Genomic_DNA.
DR   EMBL; AK031959; BAC27623.1; -; mRNA.
DR   EMBL; AL606479; CAI23940.1; -; Genomic_DNA.
DR   EMBL; AL606479; CAI23941.1; -; Genomic_DNA.
DR   EMBL; BC028341; AAH28341.1; -; mRNA.
DR   IPI; IPI00123875; -.
DR   IPI; IPI00223339; -.
DR   IPI; IPI00223340; -.
DR   IPI; IPI00223342; -.
DR   RefSeq; NP_001157143.1; NM_001163671.1.
DR   RefSeq; NP_001157144.1; NM_001163672.1.
DR   RefSeq; NP_058657.1; NM_016961.3.
DR   RefSeq; NP_997575.2; NM_207692.2.
DR   UniGene; Mm.68933; -.
DR   ProteinModelPortal; Q9WTU6; -.
DR   SMR; Q9WTU6; 7-363.
DR   IntAct; Q9WTU6; 7.
DR   MINT; MINT-1487632; -.
DR   STRING; Q9WTU6; -.
DR   PhosphoSite; Q9WTU6; -.
DR   PMMA-2DPAGE; Q9WTU6; -.
DR   PRIDE; Q9WTU6; -.
DR   Ensembl; ENSMUST00000020634; ENSMUSP00000020634; ENSMUSG00000020366.
DR   Ensembl; ENSMUST00000043321; ENSMUSP00000042744; ENSMUSG00000020366.
DR   Ensembl; ENSMUST00000109179; ENSMUSP00000104808; ENSMUSG00000020366.
DR   GeneID; 26420; -.
DR   KEGG; mmu:26420; -.
DR   UCSC; uc007irf.1; mouse.
DR   UCSC; uc007irg.1; mouse.
DR   UCSC; uc007irh.1; mouse.
DR   UCSC; uc007iri.1; mouse.
DR   CTD; 26420; -.
DR   MGI; MGI:1346862; Mapk9.
DR   GeneTree; ENSGT00550000074271; -.
DR   HOVERGEN; HBG014652; -.
DR   OMA; NGVVKDQ; -.
DR   OrthoDB; EOG48SGT3; -.
DR   PhylomeDB; Q9WTU6; -.
DR   BRENDA; 2.7.11.24; 244.
DR   NextBio; 304437; -.
DR   ArrayExpress; Q9WTU6; -.
DR   Bgee; Q9WTU6; -.
DR   CleanEx; MM_MAPK9; -.
DR   Genevestigator; Q9WTU6; -.
DR   GermOnline; ENSMUSG00000020366; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004705; F:JUN kinase activity; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0031558; P:induction of apoptosis in response to chemical stimulus; IGI:MGI.
DR   GO; GO:0046686; P:response to cadmium ion; IGI:MGI.
DR   InterPro; IPR008351; JNK_MAPK.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR003527; MAP_kinase_CS.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01772; JNKMAPKINASE.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS01351; MAPK; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    423       Mitogen-activated protein kinase 9.
FT                                /FTId=PRO_0000186274.
FT   DOMAIN       26    321       Protein kinase.
FT   NP_BIND      33     38       ATP (By similarity).
FT   MOTIF       183    185       TXY.
FT   ACT_SITE    151    151       Proton acceptor (By similarity).
FT   BINDING      55     55       ATP (By similarity).
FT   MOD_RES     183    183       Phosphothreonine.
FT   MOD_RES     185    185       Phosphotyrosine.
FT   MOD_RES     403    403       Phosphothreonine (By similarity).
FT   VAR_SEQ     216    230       AEMVLHKVLFPGRDY -> GELVKGCVIFQGTDH (in
FT                                isoform Beta-1 and isoform Beta-2).
FT                                /FTId=VSP_004836.
FT   VAR_SEQ     377    423       DAAVSSKATPSQSSSINDISSMSTEHTLASDTDSSLDASTG
FT                                PLEGCR -> AQMQQ (in isoform Alpha-1 and
FT                                isoform Beta-1).
FT                                /FTId=VSP_004837.
FT   CONFLICT    223    223       V -> C (in Ref. 3).
FT   CONFLICT    237    237       V -> A (in Ref. 3; CAC88132).
FT   CONFLICT    386    386       P -> A (in Ref. 4; BAC27623).
SQ   SEQUENCE   423 AA;  48189 MW;  0E759B486ABCE20D CRC64;
     MSDSKSDGQF YSVQVADSTF TVLKRYQQLK PIGSGAQGIV CAAFDTVLGI NVAVKKLSRP
     FQNQTHAKRA YRELVLLKCV NHKNIISLLN VFTPQKTLEE FQDVYLVMEL MDANLCQVIH
     MELDHERMSY LLYQMLCGIK HLHSAGIIHR DLKPSNIVVK SDCTLKILDF GLARTACTNF
     MMTPYVVTRY YRAPEVILGM GYKENVDIWS VGCIMAEMVL HKVLFPGRDY IDQWNKVIEQ
     LGTPSAEFMK KLQPTVRNYV ENRPKYPGIK FEELFPDWIF PSESERDKIK TSQARDLLSK
     MLVIDPDKRI SVDEALRHPY ITVWYDPAEA EAPPPQIYDA QLEEREHAIE EWKELIYKEV
     MDWEERSKNG VKDQPSDAAV SSKATPSQSS SINDISSMST EHTLASDTDS SLDASTGPLE
     GCR
//
ID   PRKRA_MOUSE             Reviewed;         313 AA.
AC   Q9WTX2; Q9CZB7;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Interferon-inducible double stranded RNA-dependent protein kinase activator A;
DE   AltName: Full=PKR-associated protein X;
DE   AltName: Full=PKR-associating protein X;
DE            Short=RAX;
DE   AltName: Full=Protein activator of the interferon-induced protein kinase;
DE   AltName: Full=Protein kinase, interferon-inducible double stranded RNA-dependent activator;
GN   Name=Prkra; Synonyms=Rax;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH EIF2AK2, TISSUE
RP   SPECIFICITY, AND PHOSPHORYLATION.
RX   MEDLINE=99269074; PubMed=10336432; DOI=10.1074/jbc.274.22.15427;
RA   Ito T., Yang M., May W.S.;
RT   "RAX, a cellular activator for double-stranded RNA-dependent protein
RT   kinase during stress signaling.";
RL   J. Biol. Chem. 274:15427-15432(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Required for siRNA production by DICER1 and for
CC       subsequent siRNA-mediated post-transcriptional gene silencing.
CC       Does not seem to be required for processing of pre-miRNA to miRNA
CC       by DICER1 (By similarity). Activates EIF2AK2/PKR in the absence of
CC       double stranded RNA (dsRNA), leading to phosphorylation of
CC       EIF2S1/EFI2-alpha and inhibition of translation and induction of
CC       apoptosis.
CC   -!- SUBUNIT: Homodimer. Interacts with DICER1, EIF2C2/AGO2 and TARBP2.
CC       Also able to interact with dsRNA (By similarity). Interacts with
CC       EIF2AK2 through its DRBM domains.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Expresssed in brain, heart, kidney, liver,
CC       lung, muscle, spleen and testis.
CC   -!- DOMAIN: Self-association may occur via interactions between DRBM
CC       domains as follows: DRBM 1/DRBM 1, DRBM 1/DRBM 2, DRBM 2/DRBM 2 or
CC       DRBM 3/DRBM3 (By similarity).
CC   -!- PTM: Phosphorylated at Ser-246 in unstressed cells and at Ser-287
CC       in stressed cells. Phosphorylation at Ser-246 appears to be a
CC       prerequisite for subsequent phosphorylation at Ser-287.
CC       Phosphorylation at Ser-246 and Ser-287 are necessary for
CC       activation of EIF2AK2/PKR under conditions of stress (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the PRKRA family.
CC   -!- SIMILARITY: Contains 3 DRBM (double-stranded RNA-binding) domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF083032; AAD33098.1; -; mRNA.
DR   EMBL; AK012798; BAB28477.1; -; mRNA.
DR   EMBL; AK155112; BAE33056.1; -; mRNA.
DR   EMBL; BC011311; AAH11311.1; -; mRNA.
DR   IPI; IPI00471256; -.
DR   RefSeq; NP_036001.1; NM_011871.2.
DR   UniGene; Mm.277250; -.
DR   ProteinModelPortal; Q9WTX2; -.
DR   SMR; Q9WTX2; 28-196, 238-307.
DR   STRING; Q9WTX2; -.
DR   PhosphoSite; Q9WTX2; -.
DR   PRIDE; Q9WTX2; -.
DR   Ensembl; ENSMUST00000002808; ENSMUSP00000002808; ENSMUSG00000002731.
DR   GeneID; 23992; -.
DR   KEGG; mmu:23992; -.
DR   UCSC; uc008kff.1; mouse.
DR   CTD; 23992; -.
DR   MGI; MGI:1344375; Prkra.
DR   GeneTree; ENSGT00530000063014; -.
DR   HOGENOM; HBG447137; -.
DR   HOVERGEN; HBG001700; -.
DR   InParanoid; Q9WTX2; -.
DR   OMA; NTDYIQM; -.
DR   OrthoDB; EOG41RPVB; -.
DR   PhylomeDB; Q9WTX2; -.
DR   NextBio; 303897; -.
DR   ArrayExpress; Q9WTX2; -.
DR   Bgee; Q9WTX2; -.
DR   CleanEx; MM_RAX; -.
DR   Genevestigator; Q9WTX2; -.
DR   GermOnline; ENSMUSG00000002731; Mus musculus.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0006917; P:induction of apoptosis; IDA:MGI.
DR   GO; GO:0042474; P:middle ear morphogenesis; IMP:MGI.
DR   GO; GO:0042473; P:outer ear morphogenesis; IMP:MGI.
DR   GO; GO:0030422; P:production of siRNA involved in RNA interference; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR   GO; GO:0006950; P:response to stress; IDA:MGI.
DR   GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR   InterPro; IPR001159; Ds-RNA-bd.
DR   InterPro; IPR014720; dsRNA-bd-like.
DR   Gene3D; G3DSA:3.30.160.20; dsRNA-bd-like; 2.
DR   Pfam; PF00035; dsrm; 2.
DR   SMART; SM00358; DSRM; 3.
DR   PROSITE; PS50137; DS_RBD; 3.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; Repeat; RNA-binding;
KW   RNA-mediated gene silencing.
FT   CHAIN         1    313       Interferon-inducible double stranded RNA-
FT                                dependent protein kinase activator A.
FT                                /FTId=PRO_0000223610.
FT   DOMAIN       34    101       DRBM 1.
FT   DOMAIN      126    194       DRBM 2.
FT   DOMAIN      240    308       DRBM 3.
FT   REGION        1    103       Sufficient for self-association and
FT                                interaction with TARBP2 (By similarity).
FT   REGION      102    195       Sufficient for self-association and
FT                                interaction with TARBP2 (By similarity).
FT   REGION      195    313       Sufficient for self-association and
FT                                interaction with TARBP2 (By similarity).
FT   MOD_RES      18     18       Phosphoserine.
FT   MOD_RES     246    246       Phosphoserine (By similarity).
FT   MOD_RES     287    287       Phosphoserine (By similarity).
FT   CONFLICT    177    177       K -> N (in Ref. 2; BAB28477).
SQ   SEQUENCE   313 AA;  34371 MW;  6EDF248A55A391D2 CRC64;
     MSHSRHRAEA PPLQREDSGT FSLGKMITAK PGKTPIQVLH EYGMKTKNIP VYECERSDVQ
     VHVPTFTFRV TVGDITCTGE GTSKKLAKHR AAEAAINILK ANASICFAVP DPLMPDPSKQ
     PKNQLNPIGS LQELAIHHGW RLPEYTLSQE GGPAHKREYT TICRLESFME TGKGASKKQA
     KRNAAEKFLA KFSNISPENH ISLTNVVGHS LGCTWHSLRN SPGEKINLLK RSLLSLPNTD
     YIQLLSEIAS EQGFNITYLD IEELSANGQY QCLAELSTSP ITVCHGSGIS CGNAQSDAAH
     NALQYLKIIA ERK
//
ID   MAN1_MOUSE              Reviewed;         921 AA.
AC   Q9WU40; Q0VGU6; Q3USB5;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Inner nuclear membrane protein Man1;
DE   AltName: Full=LEM domain-containing protein 3;
GN   Name=Lemd3; Synonyms=Man1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-331.
RX   MEDLINE=20138223; PubMed=10671519; DOI=10.1074/jbc.275.7.4840;
RA   Lin F., Blake D.L., Callebaut I., Skerjanc I.S., Holmer L.,
RA   McBurney M.W., Paulin-Levasseur M., Worman H.J.;
RT   "MAN1, an inner nuclear membrane protein that shares the LEM domain
RT   with lamina-associated polypeptide 2 and emerin.";
RL   J. Biol. Chem. 275:4840-4847(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 437-921 (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 509-921.
RC   STRAIN=C57BL/6J; TISSUE=Bone;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-260, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Can function as a specific repressor of TGF-beta,
CC       activin, and BMP signaling through its interaction with the R-SMAD
CC       proteins. Antagonizes TGF-beta-induced cell proliferation arrest
CC       (By similarity).
CC   -!- SUBUNIT: Interacts with SMAD1, SMAD2, SMAD3 and SMAD5. Binds to
CC       both phosphorylated and unphosphorylated R-SMADS (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus inner membrane; Multi-pass membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9WU40-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9WU40-2; Sequence=VSP_026782;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 LEM domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BC082610; Type=Frameshift; Positions=840;
CC   -----------------------------------------------------------------------
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DR   EMBL; AC140381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF112300; AAD31594.1; -; mRNA.
DR   EMBL; BC082610; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK140538; BAE24418.1; -; mRNA.
DR   IPI; IPI00123867; -.
DR   IPI; IPI00853982; -.
DR   RefSeq; NP_001074662.2; NM_001081193.2.
DR   UniGene; Mm.339371; -.
DR   ProteinModelPortal; Q9WU40; -.
DR   SMR; Q9WU40; 8-50, 664-884.
DR   STRING; Q9WU40; -.
DR   PhosphoSite; Q9WU40; -.
DR   PRIDE; Q9WU40; -.
DR   Ensembl; ENSMUST00000053671; ENSMUSP00000057191; ENSMUSG00000048661.
DR   Ensembl; ENSMUST00000119944; ENSMUSP00000113103; ENSMUSG00000048661.
DR   GeneID; 380664; -.
DR   KEGG; mmu:380664; -.
DR   CTD; 380664; -.
DR   MGI; MGI:3580376; Lemd3.
DR   eggNOG; roNOG12950; -.
DR   GeneTree; ENSGT00530000063791; -.
DR   HOVERGEN; HBG006319; -.
DR   OrthoDB; EOG4HQDHV; -.
DR   NextBio; 401076; -.
DR   ArrayExpress; Q9WU40; -.
DR   Bgee; Q9WU40; -.
DR   CleanEx; MM_LEMD3; -.
DR   Genevestigator; Q9WU40; -.
DR   GermOnline; ENSMUSG00000048661; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005637; C:nuclear inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   InterPro; IPR018996; Inner-Nucl-membr_MAN1.
DR   InterPro; IPR003887; LEM.
DR   InterPro; IPR011015; LEM-like_dom.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Gene3D; G3DSA:1.10.720.40; LEM; 1.
DR   Pfam; PF03020; LEM; 1.
DR   Pfam; PF09402; MAN1_C; 1.
DR   SMART; SM00540; LEM; 1.
DR   SUPFAM; SSF63451; LEM_like; 1.
DR   PROSITE; PS50954; LEM; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; DNA-binding; Membrane; Nucleus; Phosphoprotein;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    921       Inner nuclear membrane protein Man1.
FT                                /FTId=PRO_0000206150.
FT   TRANSMEM    486    506       Helical; (Potential).
FT   TRANSMEM    637    657       Helical; (Potential).
FT   DOMAIN        7     51       LEM.
FT   DNA_BIND    717    736       By similarity.
FT   REGION      709    921       Interaction with SMAD1, SMAD2, SMAD3 and
FT                                SMAD5 (By similarity).
FT   COMPBIAS     52     62       Poly-Gln.
FT   COMPBIAS     74     79       Poly-Asn.
FT   COMPBIAS    151    157       Poly-Gly.
FT   COMPBIAS    264    272       Poly-Glu.
FT   COMPBIAS    329    332       Poly-Ala.
FT   COMPBIAS    349    357       Poly-Gly.
FT   COMPBIAS    424    429       Poly-Ala.
FT   COMPBIAS    645    650       Poly-Leu.
FT   COMPBIAS    669    672       Poly-Glu.
FT   MOD_RES     136    136       Phosphoserine (By similarity).
FT   MOD_RES     137    137       Phosphoserine (By similarity).
FT   MOD_RES     140    140       Phosphoserine (By similarity).
FT   MOD_RES     260    260       Phosphotyrosine.
FT   MOD_RES     261    261       Phosphoserine (By similarity).
FT   MOD_RES     263    263       Phosphoserine.
FT   MOD_RES     287    287       Phosphoserine (By similarity).
FT   MOD_RES     338    338       Phosphoserine (By similarity).
FT   MOD_RES     387    387       Phosphoserine (By similarity).
FT   MOD_RES     412    412       Phosphoserine (By similarity).
FT   MOD_RES     787    787       Phosphoserine (By similarity).
FT   MOD_RES     921    921       Phosphoserine (By similarity).
FT   VAR_SEQ     575    575       K -> KVHLVFKITAENLCFKTLSDASN (in isoform
FT                                2).
FT                                /FTId=VSP_026782.
FT   CONFLICT    804    804       P -> Q (in Ref. 4; BAE24418).
FT   CONFLICT    861    861       L -> F (in Ref. 4; BAE24418).
SQ   SEQUENCE   921 AA;  100307 MW;  EBFA12FE19D79F3D CRC64;
     MAAATAAAAP QQLSDEELFS QLRRYGLSPG PVTESTRPVY LKKLKKLREE EQQQQQQQQQ
     QQHRAGGRGN KTRNSNNNNT ATAMGGRPGS GDLAYLRSPA GLGRLSASAA ESPVAGGSGG
     AAAVPAAGSK VLLGFSSDES DVEASPREQA GGGGGGGARR DRAALQYRGL RAPPAPPAAG
     EVTGGHPGER RKPHSWWGAR RPAGPEPQPP AAGSDGAAED ADEELADGED RDPEAEEPLW
     ASRAVNGSRL LPYSSCREHY SDSEEEEEEG EEDGDVAPAR QVLKDDSLAR HRPRRSHSKP
     FSALTAKSGG SRQETSVQGG GALAMNDRAA AAGSLDRSRN LEEAAAEPGG GGGGGCGCDP
     VDSIPRYRAG AKKLAPLLSP PSPDGDSTLE SPTGPLLKTN NHIGGGAFGV DSPGLYANSL
     PPGATAAAAP GTLRINHANH TGSNHTYLKT AYGKPKLCEP EEELLQQFKR EEVSPTGSFS
     AHYLSMFLLT AACLFFLILG LTYLGMRGTG VPEDGGLIKN PFDETFGKIQ ESEKNLLMST
     LYKLHDRLAQ IAGDHECGSS SQRMLSVQEA AAYLKNLGPE YEDVFNTSLL WIFKNGKDVG
     IRCVGYGPEE DLTNITDVQF LQSTRPQMPF WCRFRRAFIT VTHRLLLLCL GVVLVCVALR
     YMRYRWTKEE EETRQMYDMV VKIIDVLRSH NEACQETKDL QPYMPLPHVR DSLIQPQDRK
     KMKKVWDRAV DFLAANESRV RTETRRVGGA DFLVWRWIQP SASCDKTLVI PSKVWQGQAF
     HLDRRNSPPN SLTPCLKIRN MFDPVMEIGD HWHLAIQEAI LEKCSDNDGI VHIAVDRNSR
     EGCVYVKCLS PEYAGKAFKA LHGSWFDGKL VTVKYLRLDR YHHRFPQALT CNTPLKPANK
     HMNSLSHLRL RTGLANSQGS S
//
ID   NCOR2_MOUSE             Reviewed;        2472 AA.
AC   Q9WU42; Q9WU43; Q9WUC1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   08-MAR-2011, entry version 102.
DE   RecName: Full=Nuclear receptor corepressor 2;
DE            Short=N-CoR2;
DE   AltName: Full=Silencing mediator of retinoic acid and thyroid hormone receptor;
DE            Short=SMRT;
DE            Short=SMRTe;
DE   AltName: Full=T3 receptor-associating factor;
DE            Short=TRAC;
DE   AltName: Full=Thyroid-, retinoic-acid-receptor-associated corepressor;
GN   Name=Ncor2; Synonyms=Smrt;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
RC   TISSUE=Brain, and Spleen;
RX   MEDLINE=99178941; PubMed=10077563; DOI=10.1073/pnas.96.6.2639;
RA   Ordentlich P., Downes M., Xie W., Genin A., Spinner N.B., Evans R.M.;
RT   "Unique forms of human and mouse nuclear receptor corepressor SMRT.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:2639-2644(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
RC   TISSUE=Embryo;
RX   MEDLINE=99199215; PubMed=10097068; DOI=10.1073/pnas.96.7.3519;
RA   Park E.J., Schroen D.J., Yang M., Li H., Li L., Chen J.D.;
RT   "SMRTe, a silencing mediator for retinoid and thyroid hormone
RT   receptors-extended isoform that is more related to the nuclear
RT   receptor corepressor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:3519-3524(1999).
RN   [3]
RP   INTERACTION WITH C1D.
RX   MEDLINE=98070763; PubMed=9405624; DOI=10.1073/pnas.94.26.14400;
RA   Zamir I., Dawson J., Lavinsky R.M., Glass C.K., Rosenfeld M.G.,
RA   Lazar M.A.;
RT   "Cloning and characterization of a corepressor and potential component
RT   of the nuclear hormone receptor repression complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:14400-14405(1997).
RN   [4]
RP   INTERACTION WITH HDAC7.
RX   MEDLINE=20107033; PubMed=10640276;
RA   Kao H.-Y., Downes M., Ordentlich P., Evans R.M.;
RT   "Isolation of a novel histone deacetylase reveals that class I and
RT   class II deacetylases promote SMRT-mediated repression.";
RL   Genes Dev. 14:55-66(2000).
RN   [5]
RP   INTERACTION WITH CBFA2T3.
RX   PubMed=11533236; DOI=10.1128/MCB.21.19.6470-6483.2001;
RA   Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N.,
RA   Downing J.R., Meyers S., Hiebert S.W.;
RT   "ETO, a target of t(8;21) in acute leukemia, makes distinct contacts
RT   with multiple histone deacetylases and binds mSin3A through its
RT   oligomerization domain.";
RL   Mol. Cell. Biol. 21:6470-6483(2001).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-549; SER-550; SER-938
RP   AND SER-2410, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149; SER-152; SER-863;
RP   THR-1406 AND SER-1749, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH NR4A2.
RX   PubMed=19144721; DOI=10.1242/dev.029769;
RA   Jacobs F.M., van Erp S., van der Linden A.J., von Oerthel L.,
RA   Burbach J.P., Smidt M.P.;
RT   "Pitx3 potentiates Nurr1 in dopamine neuron terminal differentiation
RT   through release of SMRT-mediated repression.";
RL   Development 136:531-540(2009).
CC   -!- FUNCTION: Transcriptional corepressor of NR4A2/NURR1 and acts
CC       through histone deacetylases (HDACs) to keep promoters of
CC       NR4A2/NURR1 target genes in a repressed deacetylated state.
CC       Mediates the transcriptional repression activity of some nuclear
CC       receptors by promoting chromatin condensation, thus preventing
CC       access of the basal transcription.
CC   -!- SUBUNIT: Forms a large corepressor complex that contains SIN3A/B
CC       and histone deacetylases HDAC1 and HDAC2. This complex associates
CC       with the thyroid (TR) and the retinoid acid receptors (RAR) in the
CC       absence of ligand, and may stabilize their interaction with TFIIB.
CC       Interacts directly with RARA in the absence of ligand; the
CC       interaction represses RARA activity. Interacts with HDAC10 and
CC       MINT. Interacts with HDAC7 and ATXN1L. Component of the N-Cor
CC       repressor complex, at least composed of NCOR1, NCOR2, HDAC3,
CC       TBL1X, TBL1R, CORO2A and GPS2 (By similarity). Interacts with
CC       CBFA2T3. Interacts with C1D. Interacts with BCL6; the interaction
CC       is direct (By similarity). Interacts with NR4A2/NURR1 and this
CC       interaction increases in the absence of PITX3.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Alpha;
CC         IsoId=Q9WU42-1; Sequence=Displayed;
CC       Name=Beta;
CC         IsoId=Q9WU42-2; Sequence=VSP_003414;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Also widely expressed in early
CC       embryos.
CC   -!- DOMAIN: The N-terminal region contains repression functions that
CC       are divided into three independent repression domains (RD1, RD2
CC       and RD3). The C-terminal region contains the nuclear receptor-
CC       interacting domains that are divided in two separate interaction
CC       domains (ID1 and ID2).
CC   -!- DOMAIN: The two interaction domains (ID) contain a conserved
CC       sequence referred to as the CORNR box. This motif is required and
CC       sufficient to permit binding to unligated TR and RARS. Sequences
CC       flanking the CORNR box determine nuclear hormone receptor
CC       specificity.
CC   -!- SIMILARITY: Belongs to the N-CoR nuclear receptor corepressors
CC       family.
CC   -!- SIMILARITY: Contains 2 SANT domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF113001; AAD20944.1; -; mRNA.
DR   EMBL; AF113002; AAD20945.1; -; mRNA.
DR   EMBL; AF125671; AAD22972.1; -; mRNA.
DR   IPI; IPI00222492; -.
DR   IPI; IPI00776361; -.
DR   RefSeq; NP_035554.2; NM_011424.2.
DR   UniGene; Mm.278646; -.
DR   ProteinModelPortal; Q9WU42; -.
DR   SMR; Q9WU42; 413-480, 607-667.
DR   MINT; MINT-3154743; -.
DR   STRING; Q9WU42; -.
DR   PhosphoSite; Q9WU42; -.
DR   PRIDE; Q9WU42; -.
DR   Ensembl; ENSMUST00000111400; ENSMUSP00000107031; ENSMUSG00000029478.
DR   Ensembl; ENSMUST00000111401; ENSMUSP00000107032; ENSMUSG00000029478.
DR   GeneID; 20602; -.
DR   KEGG; mmu:20602; -.
DR   CTD; 20602; -.
DR   MGI; MGI:1337080; Ncor2.
DR   GeneTree; ENSGT00550000074554; -.
DR   HOVERGEN; HBG052587; -.
DR   NextBio; 298933; -.
DR   ArrayExpress; Q9WU42; -.
DR   Bgee; Q9WU42; -.
DR   CleanEx; MM_NCOR2; -.
DR   Genevestigator; Q9WU42; -.
DR   GermOnline; ENSMUSG00000029478; Mus musculus.
DR   GO; GO:0000118; C:histone deacetylase complex; IDA:MGI.
DR   GO; GO:0016604; C:nuclear body; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0016566; F:specific transcriptional repressor activity; IMP:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR   GO; GO:0021846; P:cell proliferation in forebrain; IMP:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0003007; P:heart morphogenesis; IGI:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0021537; P:telencephalon development; IMP:MGI.
DR   GO; GO:0050872; P:white fat cell differentiation; IMP:MGI.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR014778; Myb_DNA-bd.
DR   InterPro; IPR001005; SANT_DNA-bd.
DR   InterPro; IPR017884; SANT_eukarya.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Pfam; PF00249; Myb_DNA-binding; 1.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF46689; Homeodomain_like; 2.
DR   PROSITE; PS51293; SANT; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; DNA-binding; Nucleus;
KW   Phosphoprotein; Repeat; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   2472       Nuclear receptor corepressor 2.
FT                                /FTId=PRO_0000055623.
FT   DOMAIN      427    478       SANT 1.
FT   DOMAIN      606    657       SANT 2.
FT   REGION      254    312       Interaction with SIN3A/B (By similarity).
FT   REGION     2086   2090       Required for interaction with RARA in the
FT                                absence of its ligand (By similarity).
FT   COILED      165    207       Potential.
FT   COILED      492    560       Potential.
FT   COILED      658    682       Potential.
FT   MOTIF      2094   2098       CORNR box of ID1.
FT   MOTIF      2296   2300       CORNR box of ID2.
FT   COMPBIAS    494    507       Poly-Gln.
FT   COMPBIAS    775    804       Pro-rich.
FT   COMPBIAS    989    999       Pro-rich.
FT   COMPBIAS   1351   1357       Pro-rich.
FT   COMPBIAS   1615   1619       Poly-Ala.
FT   COMPBIAS   2434   2437       Poly-Pro.
FT   MOD_RES      54     54       Phosphoserine (By similarity).
FT   MOD_RES      67     67       Phosphoserine (By similarity).
FT   MOD_RES     149    149       Phosphoserine.
FT   MOD_RES     152    152       Phosphoserine.
FT   MOD_RES     215    215       Phosphoserine (By similarity).
FT   MOD_RES     549    549       Phosphothreonine.
FT   MOD_RES     550    550       Phosphoserine.
FT   MOD_RES     742    742       Phosphoserine (By similarity).
FT   MOD_RES     743    743       Phosphoserine (By similarity).
FT   MOD_RES     747    747       Phosphoserine (By similarity).
FT   MOD_RES     750    750       Phosphoserine (By similarity).
FT   MOD_RES     863    863       Phosphoserine.
FT   MOD_RES     878    878       N6-acetyllysine (By similarity).
FT   MOD_RES     938    938       Phosphoserine.
FT   MOD_RES     955    955       Phosphoserine (By similarity).
FT   MOD_RES     958    958       N6-acetyllysine (By similarity).
FT   MOD_RES    1181   1181       N6-acetyllysine (By similarity).
FT   MOD_RES    1209   1209       N6-acetyllysine (By similarity).
FT   MOD_RES    1220   1220       Phosphoserine (By similarity).
FT   MOD_RES    1222   1222       Phosphoserine (By similarity).
FT   MOD_RES    1350   1350       Phosphothreonine (By similarity).
FT   MOD_RES    1406   1406       Phosphothreonine.
FT   MOD_RES    1449   1449       Phosphoserine (By similarity).
FT   MOD_RES    1546   1546       Phosphoserine (By similarity).
FT   MOD_RES    1749   1749       Phosphoserine.
FT   MOD_RES    1758   1758       N6-acetyllysine (By similarity).
FT   MOD_RES    1920   1920       N6-acetyllysine (By similarity).
FT   MOD_RES    1929   1929       Phosphoserine (By similarity).
FT   MOD_RES    1963   1963       Phosphoserine (By similarity).
FT   MOD_RES    1983   1983       N6-acetyllysine (By similarity).
FT   MOD_RES    1997   1997       Phosphotyrosine (By similarity).
FT   MOD_RES    2004   2004       Phosphoserine (By similarity).
FT   MOD_RES    2012   2012       Phosphoserine (By similarity).
FT   MOD_RES    2015   2015       Phosphoserine (By similarity).
FT   MOD_RES    2016   2016       Phosphoserine (By similarity).
FT   MOD_RES    2018   2018       Phosphoserine (By similarity).
FT   MOD_RES    2020   2020       Phosphothreonine (By similarity).
FT   MOD_RES    2152   2152       Phosphoserine (By similarity).
FT   MOD_RES    2155   2155       Phosphoserine (By similarity).
FT   MOD_RES    2181   2181       Phosphoserine (By similarity).
FT   MOD_RES    2215   2215       Phosphoserine (By similarity).
FT   MOD_RES    2410   2410       Phosphoserine.
FT   MOD_RES    2469   2469       Phosphoserine (By similarity).
FT   MOD_RES    2471   2471       Phosphoserine (By similarity).
FT   VAR_SEQ      36    254       Missing (in isoform Beta).
FT                                /FTId=VSP_003414.
FT   CONFLICT    176    176       M -> RL (in Ref. 2; AAD22972).
FT   CONFLICT    396    402       PPMLYDA -> RHVVRR (in Ref. 2; AAD22972).
FT   CONFLICT    555    555       D -> H (in Ref. 1; AAD20944).
FT   CONFLICT    756    756       T -> M (in Ref. 1; AAD20944).
FT   CONFLICT    785    785       V -> A (in Ref. 2; AAD22972).
FT   CONFLICT    806    846       HHLPHPRLLWTRMNKKPRLLQLPRQRMPRSRSLRPRRSMWE
FT                                -> PSPAAPPATVDKDEQEAPAAPAPQTEDAKEQKSEAEEI
FT                                DVG (in Ref. 2; AAD22972).
FT   CONFLICT    856    856       E -> K (in Ref. 1; AAD20945).
FT   CONFLICT    859    859       E -> K (in Ref. 1; AAD20945).
FT   CONFLICT    867    867       E -> K (in Ref. 1; AAD20945).
FT   CONFLICT    895    895       E -> K (in Ref. 1; AAD20945).
FT   CONFLICT    916    916       S -> F (in Ref. 1; AAD20944).
FT   CONFLICT    975    975       I -> IQ (in Ref. 1; AAD20944).
FT   CONFLICT   1046   1063       PKLPTEPPRWSSGLPFPI -> QSYRLSPHAGHRLPSH
FT                                (in Ref. 2; AAD22972).
FT   CONFLICT   1073   1080       PHAADPSA -> TRADPL (in Ref. 2; AAD22972).
FT   CONFLICT   1133   1133       Missing (in Ref. 2; AAD22972).
FT   CONFLICT   1149   1149       Missing (in Ref. 2; AAD22972).
FT   CONFLICT   1157   1157       G -> E (in Ref. 2; AAD22972).
FT   CONFLICT   1172   1201       GSATSGSITKGLPSTRAADGPSYRGSITHG -> APPPVEA
FT                                SPRASQYPGCRRPQLQRLYHPR (in Ref. 2;
FT                                AAD22972).
FT   CONFLICT   1696   1696       A -> S (in Ref. 2; AAD22972).
FT   CONFLICT   1855   1857       Missing (in Ref. 2; AAD22972).
FT   CONFLICT   1909   1909       A -> P (in Ref. 2; AAD22972).
FT   CONFLICT   1913   1913       A -> G (in Ref. 2; AAD22972).
FT   CONFLICT   1923   1923       G -> A (in Ref. 2; AAD22972).
FT   CONFLICT   1956   1956       N -> S (in Ref. 2; AAD22972).
FT   CONFLICT   1968   1968       A -> G (in Ref. 2; AAD22972).
FT   CONFLICT   2195   2196       TA -> AV (in Ref. 2; AAD22972).
FT   CONFLICT   2213   2214       LE -> SK (in Ref. 2; AAD22972).
FT   CONFLICT   2224   2224       T -> A (in Ref. 2; AAD22972).
SQ   SEQUENCE   2472 AA;  270859 MW;  2A58F4DF7B79285B CRC64;
     MSGSTQPVAQ TWRAAEPRYP PHGISYPVQI ARSHTDVGLL EYQHHPRDYT SHLSPGSIIQ
     PQRRRPSLLS EFQPGSERSQ ELHLRPESRT FLPELGKPDI EFTESKRPRL ELLPDTLLRP
     SPLLATGQPS GSEDLTKDRS LAGKLEPVSP PSPPHADPEL ELAPSRLSKE ELIQNMDRVD
     REITMVEQQI SKLKKKQQQL EEEAAKPPEP EKPVSPPPIE SKHRSLVQII YDENRKKAEA
     AHRILEGLGP QVELPLYNQP SDTRQYHENI KINQAMRKKL ILYFKRRNHA RKQWEQRFCQ
     RYDQLMEAWE KKVERIENNP RRRAKESKVR EYYEKQFPEI RKQRELQERM QSRVGQRGSG
     LSMSAARSEH EVSEIIDGLS EQENLEKQMR QLAVIPPMLY DADQQRIKFI NMNGLMDDPM
     KVYKDRQVTN MWSEQERDTF REKFMQHPKN FGLIASFLER KTVAECVLYY YLTKKNENYK
     SLVRRSYRRR GKSQQQQQQQ QQQQQQQMAR SSQEEKEEKE KEKEADKEEE KQDAENEKEE
     LSKEKTDDTS GEDNDEKEAV ASKGRKTANS QGRRKGRITR SMANEANHEE TATPQQSSEL
     ASMEMNESSR WTEEEMETAK KGLLEHGRNW SAIARMVGSK TVSQCKNFYF NYKKRQNLDE
     ILQQHKLKME KERNARRKKK KTPAAASEET AFPPAAEDEE MEASGASANE EELAEEAEAS
     QASGNEVPRV GECSGPAAVN NSSDTESVPS PRSEATKDTG PKPTGTEALP AATQPPVPPP
     EEPAVAPAEP SPVPDASGPP SPEPSHHLPH PRLLWTRMNK KPRLLQLPRQ RMPRSRSLRP
     RRSMWEKPEE PEASEEPPES VKSDHKEETE EEPEDKAKGT EAIETVSEAP LKVEEAGSKA
     AVTKGSSSGA TQDSDSSATC SADEVDEPEG GDKGRLLSPR PSLLTPAGDP RASTSPQKPL
     DLKQLKQRAA AIPPIVTKVH EPPREDTVPP KPVPPVPPPT QHLQPEGDVS QQSGGSPRGK
     SRSPVPPAEK EAEKPAFFPA FPTEGPKLPT EPPRWSSGLP FPIPPREVIK TSPHAADPSA
     FSYTPPGHPL PLGLHDSARP VLPRPPISNP PPLISSAKHP GVLERQLGAI SQQGMSVQLR
     VPHSEHAKAP MGPLTMGLPL AVDPKKLGTA LGSATSGSIT KGLPSTRAAD GPSYRGSITH
     GTPADVLYKG TISRIVGEDS PSRLDRARED TLPKGHVIYE GKKGHVLSYE GGMSVSQCSK
     EDGRSSSGPP HETAAPKRTY DMMEGRVGRT VTSASIEGLM GRAIPEQHSP HLKEQHHIRG
     SITQGIPRSY VEAQEDYLRR EAKLLKREGT PPPPPPPRDL TETYKPRPLD PLGPLKLKPT
     HEGVVATVKE AGRSIHEIPR EELRRTPELP LAPRPLKEGS ITQGTPLKYD SGAPSTGTKK
     HDVRSIIGSP GRPFPALHPL DIMADARALE RACYEESLKS RSGTSSGAGG SITRGAPVVV
     PELGKPRQSP LTYEDHGAPF TSHLPRGSPV TTREPTPRLQ EGSLLSSKAS QDRKLTSTPR
     EIAKSPHSTV PEHHPHPISP YEHLLRGVTG VDLYRGHIPL AFDPTSIPRG IPLEAAAAAY
     YLPRHLAPSP TYPHLYPPYL IRGYPDTAAL ENRQTIINDY ITSQQMHHNA ASAMAQRADM
     LRGLSPRESS LALNYAAGPR GIIDLSQVPH LPVLVPPTPG TPATAIDRLA YLPTAPPPFS
     SRHSSSPLSP GGPTHLAKPT ATSSSERERE RERERDKSIL TSTTTVEHAP IWRPGTEQSS
     GAGGSSRPAS HTHQHSPISP RTQDALQQRP SVLHNTSMKG VVTSVEPGTP TVLRWARSTS
     TSSPVRPAAT FPPATHCPLG GTLEGVYPTL MEPVLLPKET SRVARPERAR VDAGHAFLTK
     PPGREPASSP SKSSEPRSLA PPSSSHTAIA RTPAKNLAPH HASPDPPAPT SASDLHREKT
     QSKPFSIQEL ELRSLGYHSG AGYSPDGVEP ISPVSSPSLT HDKGLSKPLE ELEKSHLEGE
     LRHKQPGPMK LSAEAAHLPH LRPLPESQPS SSPLLQTAPG IKGHQRVVTL AQHISEVITQ
     DYTRHHPQQL SGPLPAPLYS FPGASCPVLD LRRPPSDLYL PPPDHGTPAR GSPHSEGGKR
     SPEPSKTSVL GSSEDAIEPV SPPEGMTEPG HARSTAYPLL YRDGEQGEPR MGLESPGNTS
     QPPTFFSKLT ESNSAMVKSK KQEINKKLNT HNRNEPEYNI GQPGTEIFNM PAITGAGLMT
     CRSQAVQEHA STNMGLEAII RKALMGKYDQ WEEPPPLGAN AFNPLNASAS LPAAAMPITT
     ADGRSDHALT SPGGGGKAKV SGRPSSRKAK SPAPGLASGD RPPSVSSVHS EGDCNRRTPL
     TNRVWEDRPS SAGSTPFPYN PLIMRLQAGV MASPPPPGLA AGSGPLAGPH HAWDEEPKPL
     LCSQYETLSD SE
//
ID   ATRN_MOUSE              Reviewed;        1428 AA.
AC   Q9WU60; Q9R263; Q9WU77;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Attractin;
DE   AltName: Full=Protein mahogany;
DE   Flags: Precursor;
GN   Name=Atrn; Synonyms=Mg, Mgca;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99184159; PubMed=10086355; DOI=10.1038/18210;
RA   Nagle D.L., McGrail S.H., Vitale J., Woolf E.A., Dussault B.J. Jr.,
RA   DiRocco L., Holmgren L., Montagno J., Bork P., Huszar D.,
RA   Fairchild-Huntress V., Ge P., Keilty J., Ebeling C., Baldini L.,
RA   Gilchrist J., Burn P., Carlson G.A., Moore K.J.;
RT   "The mahogany protein is a receptor involved in suppression of
RT   obesity.";
RL   Nature 398:148-152(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   MEDLINE=99184160; PubMed=10086356; DOI=10.1038/18217;
RA   Gunn T.M., Miller K.A., He L., Hyman R.W., Davis R.W., Azarani A.,
RA   Schlossman S.F., Duke-Cohan J.S., Barsh G.S.;
RT   "The mouse mahogany locus encodes a transmembrane form of human
RT   attractin.";
RL   Nature 398:152-156(1999).
RN   [3]
RP   FUNCTION.
RX   MEDLINE=20578746; PubMed=11137996; DOI=10.1038/83741;
RA   He L., Gunn T.M., Bouley D.M., Lu X.Y., Watson S.J., Schlossman S.F.,
RA   Duke-Cohan J.S., Barsh G.S.;
RT   "A biochemical function for attractin in agouti-induced pigmentation
RT   and obesity.";
RL   Nat. Genet. 27:40-47(2001).
CC   -!- FUNCTION: Involved in the initial immune cell clustering during
CC       inflammatory response and may regulate chemotactic activity of
CC       chemokines (By similarity). May play a role in melanocortin
CC       signaling pathways that regulate energy homeostasis and hair
CC       color. Low-affinity receptor for agouti. Has a critical role in
CC       normal myelination in the central nervous system (By similarity).
CC   -!- SUBUNIT: Monomer and homotrimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- PTM: Heavily glycosylated (By similarity).
CC   -!- SIMILARITY: Contains 1 C-type lectin domain.
CC   -!- SIMILARITY: Contains 1 CUB domain.
CC   -!- SIMILARITY: Contains 1 EGF-like domain.
CC   -!- SIMILARITY: Contains 6 Kelch repeats.
CC   -!- SIMILARITY: Contains 2 laminin EGF-like domains.
CC   -!- SIMILARITY: Contains 4 PSI domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD20947.1; Type=Frameshift; Positions=1388;
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=Attractin;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_150";
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DR   EMBL; AF116897; AAD20947.1; ALT_FRAME; mRNA.
DR   EMBL; AF119821; AAD25372.1; -; mRNA.
DR   EMBL; AF120318; AAD22476.1; -; Genomic_DNA.
DR   EMBL; AF120317; AAD22476.1; JOINED; Genomic_DNA.
DR   IPI; IPI00224752; -.
DR   RefSeq; NP_033860.2; NM_009730.2.
DR   UniGene; Mm.119936; -.
DR   ProteinModelPortal; Q9WU60; -.
DR   SMR; Q9WU60; 102-319, 326-400, 562-644, 1061-1150.
DR   STRING; Q9WU60; -.
DR   PhosphoSite; Q9WU60; -.
DR   PRIDE; Q9WU60; -.
DR   Ensembl; ENSMUST00000028781; ENSMUSP00000028781; ENSMUSG00000027312.
DR   GeneID; 11990; -.
DR   KEGG; mmu:11990; -.
DR   UCSC; uc008mkc.1; mouse.
DR   CTD; 11990; -.
DR   MGI; MGI:1341628; Atrn.
DR   GeneTree; ENSGT00390000001118; -.
DR   HOGENOM; HBG314862; -.
DR   HOVERGEN; HBG004312; -.
DR   InParanoid; Q9WU60; -.
DR   OrthoDB; EOG4R23SZ; -.
DR   NextBio; 280155; -.
DR   ArrayExpress; Q9WU60; -.
DR   Bgee; Q9WU60; -.
DR   CleanEx; MM_ATRN; -.
DR   Genevestigator; Q9WU60; -.
DR   GermOnline; ENSMUSG00000027312; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004872; F:receptor activity; IPI:MGI.
DR   GO; GO:0005529; F:sugar binding; IEA:UniProtKB-KW.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
DR   InterPro; IPR001304; C-type_lectin.
DR   InterPro; IPR016186; C-type_lectin-like.
DR   InterPro; IPR016187; C-type_lectin_fold.
DR   InterPro; IPR000859; CUB.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR002049; EGF_laminin.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR006652; Kelch_1.
DR   InterPro; IPR003659; Plexin-like.
DR   InterPro; IPR002165; Plexin_repeat.
DR   Gene3D; G3DSA:3.10.100.10; C-type_lectin-like; 1.
DR   Gene3D; G3DSA:2.60.120.290; CUB; 1.
DR   Gene3D; G3DSA:2.120.10.80; Kelch-typ_b-propeller; 1.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF01344; Kelch_1; 1.
DR   Pfam; PF01437; PSI; 3.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00180; EGF_Lam; 1.
DR   SMART; SM00423; PSI; 5.
DR   SUPFAM; SSF56436; C-type_lectin_fold; 1.
DR   SUPFAM; SSF49854; CUB; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS01180; CUB; 1.
DR   PROSITE; PS00022; EGF_1; 3.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01248; EGF_LAM_1; 1.
DR   PROSITE; PS50027; EGF_LAM_2; 3.
PE   2: Evidence at transcript level;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Inflammatory response;
KW   Kelch repeat; Laminin EGF-like domain; Lectin; Membrane; Receptor;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     22       Potential.
FT   PROPEP       23     82       By similarity.
FT                                /FTId=PRO_0000394772.
FT   CHAIN        83   1428       Attractin.
FT                                /FTId=PRO_0000007484.
FT   TOPO_DOM     83   1278       Extracellular (Potential).
FT   TRANSMEM   1279   1299       Helical; (Potential).
FT   TOPO_DOM   1300   1428       Cytoplasmic (Potential).
FT   DOMAIN      100    128       EGF-like.
FT   DOMAIN      131    247       CUB.
FT   REPEAT      351    401       Kelch 1.
FT   REPEAT      402    450       Kelch 2.
FT   REPEAT      460    507       Kelch 3.
FT   REPEAT      512    563       Kelch 4.
FT   REPEAT      565    623       Kelch 5.
FT   REPEAT      624    670       Kelch 6.
FT   DOMAIN      702    747       PSI 1.
FT   DOMAIN      754    793       PSI 2.
FT   DOMAIN      794    918       C-type lectin.
FT   DOMAIN      931    982       PSI 3.
FT   DOMAIN      985   1060       PSI 4.
FT   DOMAIN     1062   1107       Laminin EGF-like 1.
FT   DOMAIN     1108   1156       Laminin EGF-like 2.
FT   CARBOHYD    212    212       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    236    236       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    241    241       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    252    252       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    263    263       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    299    299       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    324    324       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    361    361       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    382    382       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    415    415       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    427    427       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    574    574       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    622    622       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    730    730       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    862    862       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    913    913       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    922    922       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    985    985       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1042   1042       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1053   1053       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1072   1072       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1197   1197       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1205   1205       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1249   1249       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD   1258   1258       N-linked (GlcNAc...) (Potential).
FT   DISULFID    100    110       By similarity.
FT   DISULFID    104    117       By similarity.
FT   DISULFID    119    128       By similarity.
FT   DISULFID    131    157       By similarity.
FT   DISULFID    249    259       By similarity.
FT   DISULFID    253    270       By similarity.
FT   DISULFID    272    281       By similarity.
FT   DISULFID    815    917       By similarity.
FT   DISULFID   1062   1070       By similarity.
FT   DISULFID   1064   1076       By similarity.
FT   DISULFID   1079   1088       By similarity.
FT   DISULFID   1091   1105       By similarity.
FT   DISULFID   1108   1117       By similarity.
FT   DISULFID   1110   1124       By similarity.
FT   DISULFID   1126   1136       By similarity.
FT   DISULFID   1139   1154       By similarity.
FT   CONFLICT      6      6       A -> V (in Ref. 2; AAD25372).
FT   CONFLICT      9      9       A -> S (in Ref. 2; AAD25372).
FT   CONFLICT     20     20       T -> A (in Ref. 2; AAD25372).
FT   CONFLICT    164    169       QPNRIM -> YPNAVL (in Ref. 2; AAD25372).
FT   CONFLICT    255    255       G -> A (in Ref. 2; AAD25372).
FT   CONFLICT    505    505       V -> A (in Ref. 2; AAD25372).
FT   CONFLICT    833    833       F -> L (in Ref. 2; AAD25372).
FT   CONFLICT   1075   1075       I -> V (in Ref. 2; AAD25372).
FT   CONFLICT   1140   1140       E -> K (in Ref. 2; AAD25372).
FT   CONFLICT   1171   1171       E -> G (in Ref. 2; AAD25372).
FT   CONFLICT   1192   1192       L -> F (in Ref. 2; AAD25372).
FT   CONFLICT   1201   1201       N -> K (in Ref. 2; AAD25372).
SQ   SEQUENCE   1428 AA;  158088 MW;  D1EADBF7F53B8911 CRC64;
     MVAVAAAAAT EARLRGSTTT TAAPAGRKGR QHRPCTATGA WRPGPRARLC LPRVLSRALP
     PPPLLPLLFS LLLLPLPREA EAAAVAAAVS GSAAAEAKEC DRPCVNGGRC NPGTGQCVCP
     TGWVGEQCQH CGGRFRLTGS SGFVTDGPGN YKYKTKCTWL IEGQPNRIMR LRFNHFATEC
     SWDHLYVYDG DSIYAPLIAA FSGLIVPERD GNETAPEVTV TSGYALLHFF SDAAYNLTGF
     NITYNFDMCP NNCSGRGECK SSNSSSAVEC ECSENWKGES CDIPHCTDNC GFPHRGICNA
     SDTRGCSCFP HWQGPGCSIP VPANQSFWTR EEYSDLKLPR ASHKAVVNGN IMWVVGGYMF
     NHSDYSMVLA YDLTSREWLP LNHSVNSVVV RYGHSLALHK DKIYMYGGKI DSTGNVTNEL
     RVFHIHNESW VLLTPKAKDQ YAVVGHSAHI VTLASGRVVM LVIFGHCPLY GYISVVQEYD
     LEKNTWSILH TQGALVQGGY GHSSVYDDRT KALYVHGGYK AFSANKYRLA DDLYRYDVDT
     QMWTILKDSR FFRYLHTAVI VSGTMLVFGG NTHNDTSMSH GAKCFSSDFM AYDIACDRWS
     VLPRPELHHD VNRFGHSAVL YNSTMYVFGG FNSLLLSDVL VFTSEQCDAH RSEAACVAAG
     PGIRCLWDTQ SSRCTSWELA TEEQAEKLKS ECFSKRTLDH DRCDQHTDCY SCTANTNDCH
     WCNDHCVPVN HSCTEGQISI AKYESCPKDN PMYYCNKKTS CRSCALDQNC QWEPRNQECI
     ALPENICGNG WHLVGNSCLK ITTAKENYDN AKLSCRNHNA FLASLTSQKK VEFVLKQLRL
     MQSSQSMSKL TLTPWVGLRK INVSYWCWED MSPFTNSLLQ WMPSEPSDAG FCGILSEPST
     RGLKAATCIN PLNGSVCERP ANHSAKQCRT PCALRTACGE CTSSSSECMW CSNMKQCVDS
     NAYVASFPFG QCMEWYTMSS CPPENCSGYC TCSHCLEQPG CGWCTDPSNT GKGKCIEGSY
     KGPVKMPSQA SAGNVYPQPL LNSSMCLEDS RYNWSFIHCP ACQCNGHSKC INQSICEKCE
     DLTTGKHCET CISGFYGDPT NGGKCQPCKC NGHASLCNTN TGKCFCTTKG VKGDECQLCE
     VENRYQGNPL KGTCYYTLLI DYQFTFSLSQ EDDRYYTAIN FVATPDEQNR DLDMFINASK
     NFNLNITWAT SFPAGTQTGE EVPVVSKTNI KEYKDSFSNE KFDFRNHPNI TFFVYVSNFT
     WPIKIQIAFS QHSNFMDLVQ FFVTFFSCFL SLLLVAAVVW KIKQSCWASR RREQLLREMQ
     QMASRPFASV NVALETDEEP PDLIGGSIKT VPKPIALEPC FGNKAAVLSV FVRLPRGLGG
     IPPPGQSGLA VASALVDISQ QMPIVYKEKS GAVRNRKQQP PAQPGTCI
//
ID   K6PP_MOUSE              Reviewed;         784 AA.
AC   Q9WUA3; Q3TNA9; Q3U4P1; Q3U7G4; Q4KUG1; Q543K8; Q8C5I6; Q9JI86;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=6-phosphofructokinase type C;
DE            EC=2.7.1.11;
DE   AltName: Full=Phosphofructo-1-kinase isozyme C;
DE            Short=PFK-C;
DE   AltName: Full=Phosphofructokinase 1;
DE   AltName: Full=Phosphohexokinase;
GN   Name=Pfkp; Synonyms=Pfkc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Ascitic tumor;
RX   PubMed=10814514; DOI=10.1006/bbrc.2000.2681;
RA   Sanchez-Martinez C., Estevez A.M., Aragon J.J.;
RT   "Phosphofructokinase C isozyme from ascites tumor cells: cloning,
RT   expression, and properties.";
RL   Biochem. Biophys. Res. Commun. 271:635-640(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANT
RP   PRO-180.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=11137296; DOI=10.1016/S0378-1119(00)00463-7;
RA   Gunasekera D., Kemp R.G.;
RT   "Genomic organization, 5'flanking region and tissue-specific
RT   expression of mouse phosphofructokinase C gene.";
RL   Gene 260:103-112(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLN-261; MET-292;
RP   ASP-694; PRO-777 AND GLY-782.
RC   STRAIN=LG/J, and SM/J;
RX   PubMed=15919810; DOI=10.2337/diabetes.54.6.1863;
RA   Ehrich T.H., Hrbek T., Kenney-Hunt J.P., Pletscher L.S., Wang B.,
RA   Semenkovich C.F., Cheverud J.M.;
RT   "Fine-mapping gene-by-diet interactions on chromosome 13 in a LG/J x
RT   SM/J murine model of obesity.";
RL   Diabetes 54:1863-1872(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
RP   VARIANTS VAL-104; GLY-145; GLN-261; MET-292; GLU-402; SER-679;
RP   ASP-694; PHE-696; PRO-777 AND GLY-782.
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow, Hippocampus, Kidney, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E.,
RA   Mollenhauer J., Wiemann S., Schick M., Korn B.;
RT   "Cloning of mouse full open reading frames in Gateway(R) system entry
RT   vector (pDONR201).";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N-3; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-650, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
CC   -!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
CC       fructose 1,6-bisphosphate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Allosteric enzyme activated by ADP, AMP, or
CC       fructose bisphosphate and inhibited by ATP or citrate (By
CC       similarity).
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9WUA3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9WUA3-2; Sequence=VSP_016664, VSP_016665;
CC         Note=May be due to intron retention. No experimental
CC         confirmation available;
CC   -!- TISSUE SPECIFICITY: Expression is constant during tumor growth and
CC       markedly decreases when cell proliferation stops.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase family. Two domains
CC       subfamily.
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DR   EMBL; Y19008; CAB64347.1; -; mRNA.
DR   EMBL; AF123533; AAD23571.1; -; mRNA.
DR   EMBL; AF249893; AAF75700.1; -; Genomic_DNA.
DR   EMBL; AF250369; AAF75700.1; JOINED; Genomic_DNA.
DR   EMBL; AF250370; AAF75700.1; JOINED; Genomic_DNA.
DR   EMBL; AF250371; AAF75700.1; JOINED; Genomic_DNA.
DR   EMBL; AF250372; AAF75700.1; JOINED; Genomic_DNA.
DR   EMBL; AF251021; AAF75700.1; JOINED; Genomic_DNA.
DR   EMBL; AY779275; AAX11357.1; -; mRNA.
DR   EMBL; AY779276; AAX11358.1; -; mRNA.
DR   EMBL; AK049841; BAC33949.1; -; mRNA.
DR   EMBL; AK078254; BAC37195.1; -; mRNA.
DR   EMBL; AK152670; BAE31405.1; -; mRNA.
DR   EMBL; AK154125; BAE32390.1; -; mRNA.
DR   EMBL; AK165422; BAE38177.1; -; mRNA.
DR   EMBL; AK165425; BAE38180.1; -; mRNA.
DR   EMBL; AK170624; BAE41918.1; -; mRNA.
DR   EMBL; AK171062; BAE42221.1; -; mRNA.
DR   EMBL; CT010268; CAJ18476.1; -; mRNA.
DR   EMBL; BC006926; AAH06926.1; -; mRNA.
DR   IPI; IPI00124444; -.
DR   IPI; IPI00661241; -.
DR   RefSeq; NP_062677.1; NM_019703.3.
DR   UniGene; Mm.273874; -.
DR   ProteinModelPortal; Q9WUA3; -.
DR   SMR; Q9WUA3; 9-767.
DR   IntAct; Q9WUA3; 3.
DR   STRING; Q9WUA3; -.
DR   PhosphoSite; Q9WUA3; -.
DR   PRIDE; Q9WUA3; -.
DR   Ensembl; ENSMUST00000021614; ENSMUSP00000021614; ENSMUSG00000021196.
DR   GeneID; 56421; -.
DR   KEGG; mmu:56421; -.
DR   NMPDR; fig|10090.3.peg.27322; -.
DR   UCSC; uc007pjz.1; mouse.
DR   UCSC; uc007pkc.1; mouse.
DR   CTD; 56421; -.
DR   MGI; MGI:1891833; Pfkp.
DR   eggNOG; roNOG12278; -.
DR   GeneTree; ENSGT00390000013209; -.
DR   HOVERGEN; HBG000976; -.
DR   InParanoid; Q9WUA3; -.
DR   OMA; KISAKAM; -.
DR   OrthoDB; EOG4NS39Z; -.
DR   PhylomeDB; Q9WUA3; -.
DR   BRENDA; 2.7.1.11; 244.
DR   NextBio; 312572; -.
DR   ArrayExpress; Q9WUA3; -.
DR   Bgee; Q9WUA3; -.
DR   CleanEx; MM_PFKP; -.
DR   Genevestigator; Q9WUA3; -.
DR   GermOnline; ENSMUSG00000021196; Mus musculus.
DR   GO; GO:0005945; C:6-phosphofructokinase complex; IEA:InterPro.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR009161; 6-phosphofructokinase_euk.
DR   InterPro; IPR022953; Phosphofructokinase.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   Pfam; PF00365; PFK; 2.
DR   PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Ppfruckinase; 2.
DR   TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Allosteric enzyme; Alternative splicing; ATP-binding;
KW   Glycolysis; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Repeat; Transferase.
FT   CHAIN         1    784       6-phosphofructokinase type C.
FT                                /FTId=PRO_0000112025.
FT   NP_BIND      43     47       ATP (By similarity).
FT   NP_BIND     201    205       ATP (By similarity).
FT   NP_BIND     218    234       ATP (By similarity).
FT   ACT_SITE    174    174       Proton acceptor (By similarity).
FT   METAL       232    232       Magnesium; via carbonyl oxygen (By
FT                                similarity).
FT   BINDING     209    209       Substrate (By similarity).
FT   BINDING     300    300       Substrate (By similarity).
FT   BINDING     306    306       Substrate (By similarity).
FT   BINDING     309    309       Substrate (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     394    394       N6-acetyllysine (By similarity).
FT   MOD_RES     485    485       N6-acetyllysine (By similarity).
FT   MOD_RES     650    650       Phosphotyrosine.
FT   MOD_RES     687    687       N6-acetyllysine (By similarity).
FT   VAR_SEQ     457    496       IKEIGWADVGGWTGQGGSILGTKRTLPGKYLEKIAEQMHS
FT                                -> VSLPGVLGMLKCYCIWGGHPPLTAPTKSRFLVVGLYQI
FT                                LI (in isoform 2).
FT                                /FTId=VSP_016664.
FT   VAR_SEQ     497    784       Missing (in isoform 2).
FT                                /FTId=VSP_016665.
FT   VARIANT     104    104       E -> V (in strain: NOD).
FT   VARIANT     145    145       E -> G (in strain: C57BL/6J).
FT   VARIANT     180    180       T -> P (in strain: C57BL/6).
FT   VARIANT     261    261       R -> Q (in strain: LG/J and NOD).
FT   VARIANT     292    292       V -> M (in strain: LG/J and NOD).
FT   VARIANT     402    402       D -> E (in strain: C57BL/6J).
FT   VARIANT     679    679       P -> S (in strain: C57BL/6J).
FT   VARIANT     694    694       E -> D (in strain: LG/J and NOD).
FT   VARIANT     696    696       I -> F (in strain: NOD).
FT   VARIANT     777    777       S -> P (in strain: LG/J and NOD).
FT   VARIANT     782    782       E -> G (in strain: LG/J and NOD).
SQ   SEQUENCE   784 AA;  85455 MW;  E9C5AAABF26FCA65 CRC64;
     MSDLDSSSSS AYPKYLEHLS GDGKAIGVLT SGGDAQGMNA AVRAVVRMGI YTGAKVYFIY
     EGYQGLVDGG SNIVEAKWDC VSSILQVGGT IIGSARCKAF RSREGRLKAA CNLARLGITN
     LCVIGGDGSL TGANLFRKEW SGLLEELARN GDIDNDTVQK YSYLNVVGMV GSIDNDFCGT
     DMTIGTDSAL HRIIEVVDAI MTTAQSHQRT FVLEVMGRHC GYLALVSALT CGADWVFLPE
     SPPEEDWEEN MCLKLSENRA RKKRLNIIIV SEGAIDMQNK PITSEKIKEL VVKNLGFDTR
     VTILGHVQRG GTPSAFDRIL ASRMGVEAVI ALLEATPETP ACVVSLRGNQ AVRLPLMECV
     QMTQDVQKAM DERRFKEAVK LRGRRFEGNL NTYKRLAIKL PDEKIVKSNC NVAVINVGAP
     AAGMNAAVRS AVRVGIADGH KMFAIYDGFE GFANGQIKEI GWADVGGWTG QGGSILGTKR
     TLPGKYLEKI AEQMHSHSIN ALLIIGGFEA YLGLLELAAA REKHEAFCVP MVMVPATVSN
     NVPGSDFSIG ADTALNTITD TCDRIKQSAS GTKRRVFIIE TMGGYCGYLA NMGALAAGAD
     AAYIFEEPFD IGDLQSNVVH LTEKMKTSIQ RGLVLRNESC SVNYTTDFIY QLYSEEGKGV
     FDCRKNVLGH MQQGGAPSPF DRNFGTKISA KAMEWISAKL KGSQGTGKKF VSDDSICVLG
     ICKRDLLFQP VAELKKVTDF EHRIPKEQWW LKLRPIMKIL AKYEASYDMS DSGKLESLQH
     HEEL
//
ID   AKT3_MOUSE              Reviewed;         479 AA.
AC   Q9WUA6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 102.
DE   RecName: Full=RAC-gamma serine/threonine-protein kinase;
DE            EC=2.7.11.1;
DE   AltName: Full=Protein kinase Akt-3;
DE   AltName: Full=Protein kinase B gamma;
DE            Short=PKB gamma;
DE   AltName: Full=RAC-PK-gamma;
GN   Name=Akt3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99194749; PubMed=10092583; DOI=10.1074/jbc.274.14.9133;
RA   Brodbeck D., Cron P., Hemmings B.A.;
RT   "A human protein kinase B gamma with regulatory phosphorylation sites
RT   in the activation loop and in the C-terminal hydrophobic domain.";
RL   J. Biol. Chem. 274:9133-9136(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain;
RX   PubMed=11387345; DOI=10.1074/jbc.M104633200;
RA   Brodbeck D., Hill M.M., Hemmings B.A.;
RT   "Two splice variants of PKB gamma have different regulatory capacity
RT   depending on the presence or absence of the regulatory phosphorylation
RT   site Ser-472 in the C-terminal hydrophobic domain.";
RL   J. Biol. Chem. 276:29550-29558(2001).
CC   -!- FUNCTION: IGF-1 leads to the activation of AKT3, which may play a
CC       role in regulating cell survival. Capable of phosphorylating
CC       several known proteins. Truncated isoform 2/PKB gamma 1 without
CC       the second serine phosphorylation site could still be stimulated
CC       but to a lesser extent (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Two specific sites, one in the kinase domain
CC       (Thr-305) and the other in the C-terminal regulatory region (Ser-
CC       472), need to be phosphorylated for its full activation (By
CC       similarity).
CC   -!- SUBUNIT: Interacts (via PH domain) with TCL1A; this enhances AKT3
CC       phosphorylation and activation. Interacts with TRAF6 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC       protein. Note=Membrane-associated after cell stimulation leading
CC       to its translocation.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=PKB gamma;
CC         IsoId=Q9WUA6-1; Sequence=Displayed;
CC       Name=2; Synonyms=PKB gamma 1;
CC         IsoId=Q9WUA6-2; Sequence=VSP_004948;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is expressed in prostate, testis,
CC       uterus and mammary gland and isoform 2 is expressed in prostate,
CC       testis and mammary gland.
CC   -!- DOMAIN: Binding of the PH domain to the phosphatidylinositol 3-
CC       kinase alpha (PI(3)K) results in its targeting to the plasma
CC       membrane.
CC   -!- PTM: Phosphorylation on Thr-305 and Ser-472 is required for full
CC       activity. Phosphorylated upon DNA damage, probably by ATM or ATR
CC       (By similarity).
CC   -!- PTM: Ubiquitinated. When fully phosphorylated and translocated
CC       into the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed
CC       by TTC3, leading to its degradation by the proteasome (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. RAC subfamily.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AF124142; AAD29090.1; -; mRNA.
DR   IPI; IPI00124450; -.
DR   IPI; IPI00228306; -.
DR   RefSeq; NP_035915.3; NM_011785.3.
DR   UniGene; Mm.235194; -.
DR   ProteinModelPortal; Q9WUA6; -.
DR   SMR; Q9WUA6; 2-476.
DR   STRING; Q9WUA6; -.
DR   PhosphoSite; Q9WUA6; -.
DR   PRIDE; Q9WUA6; -.
DR   Ensembl; ENSMUST00000019843; ENSMUSP00000019843; ENSMUSG00000019699.
DR   Ensembl; ENSMUST00000111159; ENSMUSP00000106789; ENSMUSG00000019699.
DR   Ensembl; ENSMUST00000111160; ENSMUSP00000106790; ENSMUSG00000019699.
DR   GeneID; 23797; -.
DR   KEGG; mmu:23797; -.
DR   UCSC; uc007duk.1; mouse.
DR   CTD; 23797; -.
DR   MGI; MGI:1345147; Akt3.
DR   GeneTree; ENSGT00590000082790; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108317; -.
DR   InParanoid; Q9WUA6; -.
DR   OMA; IMSDVTI; -.
DR   OrthoDB; EOG40GCQP; -.
DR   PhylomeDB; Q9WUA6; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 303415; -.
DR   ArrayExpress; Q9WUA6; -.
DR   Bgee; Q9WUA6; -.
DR   CleanEx; MM_AKT3; -.
DR   Genevestigator; Q9WUA6; -.
DR   GermOnline; ENSMUSG00000019699; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cytoplasm; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase;
KW   Transferase; Ubl conjugation.
FT   CHAIN         1    479       RAC-gamma serine/threonine-protein
FT                                kinase.
FT                                /FTId=PRO_0000085612.
FT   DOMAIN        5    107       PH.
FT   DOMAIN      148    405       Protein kinase.
FT   DOMAIN      406    479       AGC-kinase C-terminal.
FT   NP_BIND     154    162       ATP (By similarity).
FT   ACT_SITE    271    271       Proton acceptor (By similarity).
FT   BINDING     177    177       ATP (By similarity).
FT   MOD_RES     120    120       Phosphoserine (By similarity).
FT   MOD_RES     123    123       Phosphoserine (By similarity).
FT   MOD_RES     305    305       Phosphothreonine; by PDPK1 (By
FT                                similarity).
FT   MOD_RES     472    472       Phosphoserine (By similarity).
FT   VAR_SEQ     452    479       YDDDGMDGMDNERRPHFPQFSYSASGRE -> CQQSDCGML
FT                                GNWKKNDNKK (in isoform 2).
FT                                /FTId=VSP_004948.
SQ   SEQUENCE   479 AA;  55714 MW;  F08ACDF75743B8FB CRC64;
     MSDVTIVKEG WVQKRGEYIK NWRPRYFLLK TDGSFIGYKE KPQDVDLPYP LNNFSVAKCQ
     LMKTERPKPN TFIIRCLQWT TVIERTFHVD TPEEREEWTE AIQAVADRLQ RQEEERMNCS
     PTSQIDNIGE EEMDASTTHH KRKTMNDFDY LKLLGKGTFG KVILVREKAS GKYYAMKILK
     KEVIIAKDEV AHTLTESRVL KNTRHPFLTS LKYSFQTKDR LCFVMEYVNG GELFFHLSRE
     RVFSEDRTRF YGAEIVSALD YLHSGKIVYR DLKLENLMLD KDGHIKITDF GLCKEGITDA
     ATMKTFCGTP EYLAPEVLED NDYGRAVDWW GLGVVMYEMM CGRLPFYNQD HEKLFELILM
     EDIKFPRTLS SDAKSLLSGL LIKDPNKRLG GGPDDAKEIM RHSFFSGVNW QDVYDKKLVP
     PFKPQVTSET DTRYFDEEFT AQTITITPPE KYDDDGMDGM DNERRPHFPQ FSYSASGRE
//
ID   UB7I3_MOUSE             Reviewed;         508 AA.
AC   Q9WUB0; A2ANR4; Q3TM86; Q8C2I0;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=RanBP-type and C3HC4-type zinc finger-containing protein 1;
DE            EC=6.3.2.-;
DE   AltName: Full=UbcM4-interacting protein 28;
DE   AltName: Full=Ubiquitin-conjugating enzyme 7-interacting protein 3;
GN   Name=Rbck1; Synonyms=Rbck, Ubce7ip3, Uip28;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Lung, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-508.
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=99358765; PubMed=10431818; DOI=10.1016/S0014-5793(99)00823-6;
RA   Martinez-Noel G., Niedenthal R., Tamura T., Harbers K.;
RT   "A family of structurally related RING finger proteins interacts
RT   specifically with the ubiquitin-conjugating enzyme UbcM4.";
RL   FEBS Lett. 454:257-261(1999).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-328, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-328, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [7]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=19136968; DOI=10.1038/ncb1821;
RA   Tokunaga F., Sakata S., Saeki Y., Satomi Y., Kirisako T., Kamei K.,
RA   Nakagawa T., Kato M., Murata S., Yamaoka S., Yamamoto M., Akira S.,
RA   Takao T., Tanaka K., Iwai K.;
RT   "Involvement of linear polyubiquitylation of NEMO in NF-kappaB
RT   activation.";
RL   Nat. Cell Biol. 11:123-132(2009).
CC   -!- FUNCTION: Acts as an E3 ubiquitin-protein ligase, or as part of an
CC       E3 complex, which accepts ubiquitin from specific E2 ubiquitin-
CC       conjugating enzymes, such as UBE2L3/UBCM4, and then transfers it
CC       to substrates. Functions as an E3 ligase for oxidized IREB2 and
CC       both heme and oxygen are necessary for IREB2 ubiquitination.
CC       Promotes ubiquitination of TAB2 and IRF3 and their degradation by
CC       the proteoasome. Component of the LUBAC complex which conjugates
CC       linear polyubiquitin chains in a head-to-tail manner to
CC       substrates. LUBAC conjugates linear polyubiquitin to IKBKG at
CC       'Lys-278' and 'Lys-302' and is involved in activation of the
CC       canonical NF-kappa-B and the JNK signaling pathways. LUBAC is
CC       proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC)
CC       following polyubiquitination of TNF-RSC components by BIRC2 and/or
CC       BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly
CC       other components contributing to the stability of the complex.
CC       Binds polyubiquitin of different linkage types (By similarity).
CC   -!- SUBUNIT: Forms homodimers in vitro (By similarity). Component of
CC       the LUBAC complex (linear ubiquitin chain assembly complex) which
CC       consists of RBCK1 and RNF31. LUBAC has a MW of approximative 600
CC       kDa suggesting a heteromultimeric assembly of its subunits.
CC       Interacts with beta-I-type (PRKCB1) and zeta-type protein kinase C
CC       (PRKCZ) and with UBE2L3. Isoform 1 and isoform 2 interact with
CC       IREB2 only in iron-rich conditions. Associates with the TNF-R1
CC       signaling complex (TNF-RSC) in a stimulation-dependent manner.
CC       Interacts with TAB2, TAB3, MAP3K7 TRAF6 and RIPK1. Interacts with
CC       IRF3 (By similarity).
CC   -!- PTM: Auto-ubiquitinated. Auto-ubiquitination leads to degradation
CC       by the proteasome (By similarity).
CC   -!- PTM: Phosphorylated. In vitro, phosphorylation inhibits auto-
CC       ubiquitination activity (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Impaired TNF-alpha-mediated NF-kappa-B
CC       activation and enhanced JNK-mediated apoptosis.
CC   -!- SIMILARITY: Contains 1 B box-type zinc finger.
CC   -!- SIMILARITY: Contains 1 RanBP2-type zinc finger.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC   -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD24572.1; Type=Erroneous initiation;
CC       Sequence=AAH34555.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AK088591; BAC40440.1; -; mRNA.
DR   EMBL; AK166075; BAE38556.1; -; mRNA.
DR   EMBL; AL831735; CAM24727.1; -; Genomic_DNA.
DR   EMBL; AL928568; CAM24727.1; JOINED; Genomic_DNA.
DR   EMBL; AL928568; CAM23203.1; -; Genomic_DNA.
DR   EMBL; AL831735; CAM23203.1; JOINED; Genomic_DNA.
DR   EMBL; BC034555; AAH34555.1; ALT_INIT; mRNA.
DR   EMBL; AF124663; AAD24572.1; ALT_INIT; mRNA.
DR   IPI; IPI00322839; -.
DR   RefSeq; NP_001077390.1; NM_001083921.1.
DR   RefSeq; NP_062679.2; NM_019705.3.
DR   UniGene; Mm.182145; -.
DR   ProteinModelPortal; Q9WUB0; -.
DR   SMR; Q9WUB0; 66-131, 192-230, 276-410, 440-484.
DR   STRING; Q9WUB0; -.
DR   PhosphoSite; Q9WUB0; -.
DR   PRIDE; Q9WUB0; -.
DR   Ensembl; ENSMUST00000028964; ENSMUSP00000028964; ENSMUSG00000027466.
DR   Ensembl; ENSMUST00000109847; ENSMUSP00000105473; ENSMUSG00000027466.
DR   GeneID; 24105; -.
DR   KEGG; mmu:24105; -.
DR   UCSC; uc008nfd.1; mouse.
DR   CTD; 24105; -.
DR   MGI; MGI:1344372; Rbck1.
DR   eggNOG; roNOG05898; -.
DR   GeneTree; ENSGT00530000063620; -.
DR   HOGENOM; HBG446806; -.
DR   HOVERGEN; HBG061515; -.
DR   InParanoid; Q9WUB0; -.
DR   OMA; TQDIRLW; -.
DR   OrthoDB; EOG4MW866; -.
DR   NextBio; 304117; -.
DR   ArrayExpress; Q9WUB0; -.
DR   Bgee; Q9WUB0; -.
DR   Genevestigator; Q9WUB0; -.
DR   GermOnline; ENSMUSG00000027466; Mus musculus.
DR   GO; GO:0071797; C:LUBAC complex; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0043065; P:positive regulation of apoptosis; IMP:UniProtKB.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:UniProtKB.
DR   GO; GO:0042346; P:positive regulation of NF-kappaB import into nucleus; IMP:UniProtKB.
DR   InterPro; IPR019955; Ubiquitin_supergroup.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR002867; Znf_C6HC.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF01485; IBR; 2.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   Pfam; PF00641; zf-RanBP; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00547; ZnF_RBZ; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
DR   PROSITE; PS50119; ZF_BBOX; FALSE_NEG.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
DR   PROSITE; PS50199; ZF_RANBP2_2; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Ligase; Metal-binding; Phosphoprotein; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    508       RanBP-type and C3HC4-type zinc finger-
FT                                containing protein 1.
FT                                /FTId=PRO_0000056296.
FT   DOMAIN       55    119       Ubiquitin-like.
FT   ZN_FING     188    220       RanBP2-type.
FT   ZN_FING     280    325       RING-type.
FT   ZN_FING     374    409       B box-type.
FT   REGION        1    268       Interaction with TAB2 (By similarity).
FT   REGION        1    218       Interaction with IRF3 (By similarity).
FT   REGION       69    131       Interaction with RNF31 (By similarity).
FT   COILED      231    259       Potential.
FT   MOD_RES     328    328       Phosphotyrosine.
FT   CONFLICT    322    322       P -> S (in Ref. 1; BAE38556).
FT   CONFLICT    406    406       H -> R (in Ref. 1; BAC40440).
SQ   SEQUENCE   508 AA;  57534 MW;  CBD3B40CD4E55180 CRC64;
     MDEKTKKAEE MALSLARAVA GGDEQAAIKY ATWLAEQRVP LRVQVKPEVS PTQDIRLCVS
     VEDAYMHTVT IWLTVRPDMT VASLKDMVFL DYGFPPSLQQ WVVGQRLARD QETLHSHGIR
     RNGDGAYLYL LSARNTSLNP QELQRQRQLR MLEDLGFKDL TLQSRGPLEP VLPKPRTNQE
     PGQPDAAPES PPVGWQCPGC TFINKPTRPG CEMCCRARPE TYQIPASYQP DEEERARLAG
     EEEALRQYQQ RKQQQQEGNY LQHVQLEQRS LVLNTEPTEC PVCYSVLAPG EAVVLRECLH
     TFCRECLQGT IRNSQEAEVA CPFIDSTYSC PGKLLEREIR ALLSPEDYQR FLDLGVSIAE
     NRSTLSYHCK TPDCRGWCFF EDDVNEFTCP VCTRVNCLLC KAIHEHMNCR EYQDDLALRA
     QNDVAARQTT EMLKVMLQQG EAMHCPQCRI VVQKKDGCDW IRCTVCHTEI CWVTKGPRWG
     PGGPGDTSGG CRCRVNGIPC HPSCQNCH
//
ID   CHIP_MOUSE              Reviewed;         304 AA.
AC   Q9WUD1; Q9DCJ0;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=STIP1 homology and U box-containing protein 1;
DE            EC=6.3.2.-;
DE   AltName: Full=Carboxy terminus of Hsp70-interacting protein;
DE   AltName: Full=E3 ubiquitin-protein ligase CHIP;
GN   Name=Stub1; Synonyms=Chip;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99263023; PubMed=10330192;
RA   Ballinger C.A., Connell P., Wu Y., Hu Z., Thompson L.J., Yin L.-Y.,
RA   Patterson C.;
RT   "Identification of CHIP, a novel tetratricopeptide repeat-containing
RT   protein that interacts with heat shock proteins and negatively
RT   regulates chaperone functions.";
RL   Mol. Cell. Biol. 19:4535-4545(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, Embryo, and Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24 AND SER-26, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 24-304.
RX   PubMed=16307917; DOI=10.1016/j.molcel.2005.09.023;
RA   Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C.,
RA   Pearl L.H.;
RT   "Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3
RT   ubiquitin ligase and a CHIP-Ubc13-Uev1a complex.";
RL   Mol. Cell 20:525-538(2005).
CC   -!- FUNCTION: E3 ubiquitin-protein ligase which targets misfolded
CC       chaperone substrates towards proteasomal degradation.
CC       Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the
CC       activity of several chaperone complexes, including Hsp70, Hsc70
CC       and Hsp90. Mediates transfer of non-canonical short ubiquitin
CC       chains to HSPA8 that have no effect on HSPA8 degradation. Mediates
CC       polyubiquitination of CYP3A4 (By similarity).
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with BAG2, and with the E2 ubiquitin
CC       conjugating enzymes UBE2D1, UBE2D2 and UBE2D3. Interacts with the
CC       C-terminal domains of HSPA8 and HSPA1A. Detected in a ternary
CC       complex containing STUB1, HSPA1A and HSPBP1 (By similarity).
CC       Interacts with MKKS (By similarity). Interacts with DYX1C1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- DOMAIN: The TPR domain is essential for ubiquitination mediated by
CC       UBE2D1 (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- PTM: Auto-ubiquitinated; mediated by UBE2D1 and UBE2D2 (By
CC       similarity).
CC   -!- SIMILARITY: Contains 3 TPR repeats.
CC   -!- SIMILARITY: Contains 1 U-box domain.
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DR   EMBL; AF129086; AAD33401.1; -; mRNA.
DR   EMBL; AK002752; BAB22329.1; -; mRNA.
DR   EMBL; AK004464; BAB23315.1; -; mRNA.
DR   EMBL; AK045776; BAC32489.1; -; mRNA.
DR   EMBL; AK166630; BAE38905.1; -; mRNA.
DR   EMBL; BC027427; AAH27427.1; -; mRNA.
DR   EMBL; BC038939; AAH38939.1; -; mRNA.
DR   IPI; IPI00471361; -.
DR   RefSeq; NP_062693.1; NM_019719.3.
DR   UniGene; Mm.277599; -.
DR   UniGene; Mm.479897; -.
DR   PDB; 2C2L; X-ray; 3.30 A; A/B/C/D=24-304.
DR   PDB; 2C2V; X-ray; 2.90 A; S/T/U/V=227-304.
DR   PDBsum; 2C2L; -.
DR   PDBsum; 2C2V; -.
DR   ProteinModelPortal; Q9WUD1; -.
DR   SMR; Q9WUD1; 24-304.
DR   DIP; DIP-29751N; -.
DR   IntAct; Q9WUD1; 2.
DR   STRING; Q9WUD1; -.
DR   PhosphoSite; Q9WUD1; -.
DR   PRIDE; Q9WUD1; -.
DR   Ensembl; ENSMUST00000044911; ENSMUSP00000040431; ENSMUSG00000039615.
DR   GeneID; 56424; -.
DR   KEGG; mmu:56424; -.
DR   UCSC; uc008bcf.1; mouse.
DR   CTD; 56424; -.
DR   MGI; MGI:1891731; Stub1.
DR   GeneTree; ENSGT00600000084539; -.
DR   HOGENOM; HBG378130; -.
DR   HOVERGEN; HBG053046; -.
DR   InParanoid; Q9WUD1; -.
DR   OMA; LHSYLTR; -.
DR   OrthoDB; EOG4Z36F9; -.
DR   PhylomeDB; Q9WUD1; -.
DR   BRENDA; 6.3.2.19; 244.
DR   NextBio; 312582; -.
DR   ArrayExpress; Q9WUD1; -.
DR   Bgee; Q9WUD1; -.
DR   CleanEx; MM_STUB1; -.
DR   Genevestigator; Q9WUD1; -.
DR   GermOnline; ENSMUSG00000039615; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:HGNC.
DR   GO; GO:0031371; C:ubiquitin conjugating enzyme complex; TAS:HGNC.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0030544; F:Hsp70 protein binding; ISS:HGNC.
DR   GO; GO:0051879; F:Hsp90 protein binding; ISS:BHF-UCL.
DR   GO; GO:0030674; F:protein binding, bridging; TAS:HGNC.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:HGNC.
DR   GO; GO:0046332; F:SMAD binding; ISS:HGNC.
DR   GO; GO:0030911; F:TPR domain binding; ISS:HGNC.
DR   GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; IDA:MGI.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:HGNC.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:HGNC.
DR   GO; GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; ISS:HGNC.
DR   GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR   GO; GO:0006457; P:protein folding; TAS:HGNC.
DR   GO; GO:0051604; P:protein maturation; TAS:HGNC.
DR   GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
DR   GO; GO:0031943; P:regulation of glucocorticoid metabolic process; ISS:HGNC.
DR   GO; GO:0030579; P:ubiquitin-dependent SMAD protein catabolic process; ISS:HGNC.
DR   InterPro; IPR001440; TPR-1.
DR   InterPro; IPR013026; TPR-contain.
DR   InterPro; IPR011990; TPR-like_helical.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:1.25.40.10; TPR-like_helical; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00515; TPR_1; 1.
DR   Pfam; PF04564; U-box; 1.
DR   SMART; SM00028; TPR; 3.
DR   SMART; SM00504; Ubox; 1.
DR   PROSITE; PS50005; TPR; 3.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Isopeptide bond; Ligase; Phosphoprotein;
KW   Repeat; TPR repeat; Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN         1    304       STIP1 homology and U box-containing
FT                                protein 1.
FT                                /FTId=PRO_0000106330.
FT   REPEAT       27     60       TPR 1.
FT   REPEAT       61     94       TPR 2.
FT   REPEAT       96    128       TPR 3.
FT   DOMAIN      227    301       U-box.
FT   COMPBIAS     14     19       Poly-Gly.
FT   MOD_RES      20     20       Phosphoserine.
FT   MOD_RES      24     24       Phosphoserine.
FT   MOD_RES      26     26       Phosphoserine.
FT   MOD_RES     274    274       Phosphoserine (By similarity).
FT   MOD_RES     277    277       Phosphothreonine (By similarity).
FT   CROSSLNK     23     23       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK    222    222       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CROSSLNK    256    256       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CONFLICT     20     20       S -> T (in Ref. 2; BAB22329).
FT   HELIX        27     39
FT   HELIX        43     56
FT   HELIX        61     73
FT   HELIX        77     87
FT   HELIX        95    107
FT   HELIX       111    127
FT   HELIX       135    153
FT   HELIX       161    178
FT   TURN        179    181
FT   HELIX       183    185
FT   TURN        186    188
FT   HELIX       191    194
FT   HELIX       196    218
FT   TURN        235    237
FT   STRAND      242    246
FT   STRAND      252    254
FT   HELIX       257    264
FT   TURN        270    272
FT   HELIX       278    280
FT   HELIX       285    295
SQ   SEQUENCE   304 AA;  34909 MW;  18BD2728908025A8 CRC64;
     MKGKEEKEGG ARLGTGGGGS PDKSPSAQEL KEQGNRLFVG RKYPEAAACY GRAITRNPLV
     AVYYTNRALC YLKMQQPEQA LADCRRALEL DGQSVKAHFF LGQCQLEMES YDEAIANLQR
     AYSLAKEQRL NFGDDIPSAL RIAKKKRWNS IEERRIHQES ELHSYLTRLI AAERERELEE
     CQRNHEGHED DGHIRAQQAC IEAKHDKYMA DMDELFSQVD EKRKKRDIPD YLCGKISFEL
     MREPCITPSG ITYDRKDIEE HLQRVGHFDP VTRSPLTQEQ LIPNLAMKEV IDAFISENGW
     VEDY
//
ID   Q9WUD7_MOUSE            Unreviewed;        38 AA.
AC   Q9WUD7;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1999, sequence version 1.
DT   08-FEB-2011, entry version 36.
DE   SubName: Full=Brain-specific ankyrin-G;
DE   Flags: Fragment;
GN   Name=Ank3; Synonyms=ANK3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RX   MEDLINE=99054755; PubMed=9832557; DOI=10.1083/jcb.143.5.1295;
RA   Zhou D., Lambert S., Malen P.L., Carpenter S., Boland L.M.,
RA   Bennett V.;
RT   "AnkyrinG is required for clustering of voltage-gated Na channels at
RT   axon initial segments and for normal action potential firing.";
RL   J. Cell Biol. 143:1295-1304(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain;
RA   Carpenter S.S.;
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AF130364; AAD29415.1; -; Genomic_DNA.
DR   IPI; IPI00623506; -.
DR   UniGene; Mm.235960; -.
DR   STRING; Q9WUD7; -.
DR   Ensembl; ENSMUST00000092432; ENSMUSP00000090088; ENSMUSG00000069601.
DR   MGI; MGI:88026; Ank3.
DR   GeneTree; ENSGT00600000084024; -.
DR   HOGENOM; HBG444603; -.
DR   InParanoid; Q9WUD7; -.
DR   ArrayExpress; Q9WUD7; -.
DR   Bgee; Q9WUD7; -.
DR   Genevestigator; Q9WUD7; -.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007411; P:axon guidance; IMP:MGI.
DR   GO; GO:0050808; P:synapse organization; IMP:MGI.
PE   2: Evidence at transcript level;
FT   NON_TER      38     38
SQ   SEQUENCE   38 AA;  4645 MW;  B63829B96D2C9788 CRC64;
     MAHAASQLKK NRDLEINAEE ETEKKRKHRK RSRDRKKK
//
ID   C8AP2_MOUSE             Reviewed;        1962 AA.
AC   Q9WUF3; Q9CSW2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 66.
DE   RecName: Full=CASP8-associated protein 2;
DE   AltName: Full=FLICE-associated huge protein;
GN   Name=Casp8ap2; Synonyms=Flash;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN DISC COMPLEX WITH CASP8;
RP   FADD AND FAS, AND TISSUE SPECIFICITY.
RC   TISSUE=T-cell lymphoma;
RX   MEDLINE=99249338; PubMed=10235259; DOI=10.1038/19709;
RA   Imai Y., Kimura T., Murakami A., Yajima N., Sakamaki K., Yonehara S.;
RT   "The CED-4-homologous protein FLASH is involved in Fas-mediated
RT   activation of caspase-8 during apoptosis.";
RL   Nature 398:777-785(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1766-1962.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH TRAF2.
RX   PubMed=11340079; DOI=10.1074/jbc.M102941200;
RA   Choi Y.-H., Kim K.-B., Kim H.-H., Hong G.-S., Kwon Y.-K., Chung C.-W.,
RA   Park Y.-M., Shen Z.-J., Kim B.J., Lee S.-Y., Jung Y.-K.;
RT   "FLASH coordinates NF-kappa B activity via TRAF2.";
RL   J. Biol. Chem. 276:25073-25077(2001).
RN   [4]
RP   FUNCTION.
RX   PubMed=15592525; DOI=10.1038/sj.onc.1208186;
RA   Jun J.-I., Chung C.-W., Lee H.-J., Pyo J.-O., Lee K.N., Kim N.-S.,
RA   Kim Y.S., Yoo H.-S., Lee T.-H., Kim E., Jung Y.-K.;
RT   "Role of FLASH in caspase-8-mediated activation of NF-kappaB:
RT   dominant-negative function of FLASH mutant in NF-kappaB signaling
RT   pathway.";
RL   Oncogene 24:688-696(2005).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17003125; DOI=10.1073/pnas.0604227103;
RA   Barcaroli D., Bongiorno-Borbone L., Terrinoni A., Hofmann T.G.,
RA   Rossi M., Knight R.A., Matera A.G., Melino G., De Laurenzi V.;
RT   "FLASH is required for histone transcription and S-phase
RT   progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:14808-14812(2006).
CC   -!- FUNCTION: Participates in TNF-alpha-induced blockade of
CC       glucocorticoid receptor (GR) transactivation at the nuclear
CC       receptor coactivator level, upstream and independently of NF-
CC       kappa-B. Suppresses both NCOA2- and NCOA3-induced enhancement of
CC       GR transactivation (By similarity). Required for histone gene
CC       transcription and progression through S phase (By similarity).
CC       Required for histone gene transcription and S phase progression
CC       (By similarity). Involved in TNF-alpha-induced activation of NF-
CC       kappa-B via a TRAF2-dependent pathway. Acts as a downstream
CC       mediator for CASP8-induced activation of NF-kappa-B. Required for
CC       the activation of CASP8 in FAS-mediated apoptosis.
CC   -!- SUBUNIT: Interacts with NPAT and SRRT/ARS2 (By similarity). Self-
CC       associates. Component of the death-inducing signaling complex
CC       (DISC) with CASP8, FADD and FAS. Interacts with NCOA2, NCOA3 and
CC       TRAF2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus.
CC       Note=Localizes to discrete nuclear foci.
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart, brain, thymus,
CC       lung, testis and spleen.
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DR   EMBL; AF132726; AAD29045.1; -; mRNA.
DR   EMBL; AK011818; BAB27860.1; -; mRNA.
DR   IPI; IPI00124590; -.
DR   RefSeq; NP_001116450.1; NM_001122978.1.
DR   RefSeq; NP_036127.2; NM_011997.2.
DR   UniGene; Mm.22279; -.
DR   ProteinModelPortal; Q9WUF3; -.
DR   SMR; Q9WUF3; 1883-1959.
DR   IntAct; Q9WUF3; 1.
DR   STRING; Q9WUF3; -.
DR   PhosphoSite; Q9WUF3; -.
DR   PRIDE; Q9WUF3; -.
DR   Ensembl; ENSMUST00000029950; ENSMUSP00000029950; ENSMUSG00000028282.
DR   GeneID; 26885; -.
DR   KEGG; mmu:26885; -.
DR   UCSC; uc008sex.1; mouse.
DR   CTD; 26885; -.
DR   MGI; MGI:1349399; Casp8ap2.
DR   GeneTree; ENSGT00390000005443; -.
DR   HOGENOM; HBG279764; -.
DR   HOVERGEN; HBG080371; -.
DR   InParanoid; Q9WUF3; -.
DR   OrthoDB; EOG4VT5ZV; -.
DR   ArrayExpress; Q9WUF3; -.
DR   Bgee; Q9WUF3; -.
DR   CleanEx; MM_CASP8AP2; -.
DR   Genevestigator; Q9WUF3; -.
DR   GermOnline; ENSMUSG00000028282; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0008656; F:caspase activator activity; IDA:MGI.
DR   GO; GO:0042802; F:identical protein binding; IDA:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR   GO; GO:0006919; P:activation of caspase activity; IDA:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0008625; P:induction of apoptosis via death domain receptors; IDA:MGI.
PE   1: Evidence at protein level;
KW   Activator; Apoptosis; Cell cycle; Cytoplasm; Isopeptide bond; Nucleus;
KW   Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN         1   1962       CASP8-associated protein 2.
FT                                /FTId=PRO_0000076189.
FT   REGION     1688   1962       NCOA2-binding (By similarity).
FT   CROSSLNK     92     92       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CONFLICT   1766   1766       E -> K (in Ref. 2; BAB27860).
SQ   SEQUENCE   1962 AA;  219075 MW;  CD452C4202C12BC2 CRC64;
     MAADDDNGDG TGLFDVCPAS PLKNNDEGSL DIYAGLDSAV SDSTARSCVS FRNCLDLYEE
     ILTEEGTAKE ATYNDLQIEY GKCQQQMKDL MKRFKEIQTQ NLNLKNENQS LKKNISALIK
     TARVEINRKD EEINHLHQRL SEFPHFRNNH KAARTKDSQS TSPHLDDCSK TDHGVKSDVQ
     KDVHPNTAQP NLEKEGKSHS EAQNPLHLST GVEKHCANNV WSRSPYQVGE GNSNEDNRRG
     RSGTRHSQCS RGTDRTQKDL HSSCNDSEPR DKEANSRLQG HPEKHGNSEA RTESKISESK
     SSTGMGYKSE RSASSWEKET SRERPHTRVE SQHDKNLEKQ NERLQNMHRK ELPSQDKTER
     KVDVKFKPAG EEQGHRGRVD RALPPHPKND VKHYGFNKYH PEERRGREDC KRDRGMNSHG
     FQDRRCSSFL SSNRNSKYPH SKEVSVAHQW ENTPFKAERH RTEDRRKRER ENKEESRHVK
     SDKKSPPEHL QRTHKDTKKS TADGKRQTEP KHGKGAVSNS ELSKGTDSKE GATKVESGPN
     EAKGKDLKLS FMEKLNLTLS PAKKQPACQD NPHQITGVPE PSGTCDSRSL ETTGTVACLP
     SGSEHNREET KSELPEPKEA LLATSQLRIS IPENKMKEEK RLLFKSVENT VPCELLACGT
     EISLPAPVEI EQARCLLGSV EVEETCGGAR TAASVVMHVL PEHASEDASQ ELDTKRHDGI
     NACAISEGVK TKVILSPKAA AASESHLAPL VEEPSISLVN CSGDNNPKLE PSLEERPIVE
     TKSCPLESCL PKETFVPSPQ KTELIDHKIE TGESNSVYQD DDNSVLSIDF NNLRPIPDPI
     SPLNSPVRPV CKVVSMESSC AIPLYDSSHK DEFPSNSTLS TFKSQSDLNK ENEKPVPKFD
     KCSEADSCKH LSLDELEEGE IRSDDEESVA QKRLEKSARP RVSAEVQPGK SSPGSRRSTV
     HVHKDNGRTA VKLPRDRLTW SKRSSESRPS NTERKSKTMS ISSLEKILPL ILVPSSLWEV
     MHMLRLLGKH VRKNYMKFKI KFSLTQFHRI IESAILSFTS LIKCLDLSKI CKSVSTLQKS
     LCEVIESNLK QVKKNGIVDR LFEQQQTDMK KKLWKFVDEQ LDYLFEKLKK ILLKFCDSVN
     FENENSEGKL GKKYKERTQH SNCQKKKMDN KEIRREKVLK SENTVNFKSS LGCEKSEEKH
     QDQNKTNASI VKHDVKRTFS TCSDNTKNAE CKEQFLEKSC PSTPRPGKDE GHTEEEAQAA
     QHASAKSERS FEILTEQQAS SLTFNLVSDA QMGEIFKSLL QGSDLLDTSG TEKAEWELKT
     PEKQLLESLK CESAPACATE ELVSEGASLC PKVISDDNWS LLSSEKGPSL SSGLSLPVHP
     DVLDENCMFE VSSNTALGKD NVYSSEKSKP CISSILLEDL AVSLTVPSPL KSDGHLSFLK
     PEVLSTSTPE EVISAHFSED ALLEEEDASE QDIHLALESD NSSSKSSCSS WTSRSVASGF
     QYHPNLPMHA VIMEKSNDHF IVKIRRATPS TSPGLKHGVV AEESLTSLPR TGKEAGVATE
     KEPNLFQSTV LKPVKDLENT DKNIDKSKLT HEEQNSIVQT QVPDIYEFLK DASNKVVHCD
     QVVDDCFKLH QVWEPKVSEN LQELPSMEKI PHSLDNHLPD THIDLTKDSA TETKSLGELM
     EVTVLNVDHL ECSQTNLDQD AEITCSSLQP DTIDAFIDLT HDASSESKNE GSEPVLAVEG
     MGCQVICIDE DTNKEGKMGR ANSPLESIVE ETCIDLTSES PGSCEIKRHN LKSEPPSKLD
     CLELPETLGN GHKKRKNSPG VSHSSQKKQR KDIDLSSEKT QRLSPNSDRN GDAHRKQASK
     KREPAVNETS LSSEASPEVK GSTAVLAASP ASLSAKNVIK KKGEIIVSWT RNDDREILLE
     CQKRMPSLKT FTYLAVKLNK NPNQVSERFQ QLKKLFEKSK CR
//
ID   TM115_MOUSE             Reviewed;         350 AA.
AC   Q9WUH1; Q91VT6;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Transmembrane protein 115;
DE   AltName: Full=Protein PL6 homolog;
GN   Name=Tmem115; Synonyms=Pl6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Ivanov S., Minna J., Lerman M.I.;
RT   "Mouse ortholog of the human gene PL6.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Probable).
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH09099.1; Type=Erroneous initiation;
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DR   EMBL; AF134238; AAD24193.1; -; mRNA.
DR   EMBL; BC009099; AAH09099.1; ALT_INIT; mRNA.
DR   EMBL; BC019473; AAH19473.1; -; mRNA.
DR   IPI; IPI00124661; -.
DR   RefSeq; NP_062678.1; NM_019704.2.
DR   UniGene; Mm.260153; -.
DR   ProteinModelPortal; Q9WUH1; -.
DR   STRING; Q9WUH1; -.
DR   PhosphoSite; Q9WUH1; -.
DR   PRIDE; Q9WUH1; -.
DR   Ensembl; ENSMUST00000010189; ENSMUSP00000010189; ENSMUSG00000010045.
DR   GeneID; 56395; -.
DR   KEGG; mmu:56395; -.
DR   UCSC; uc009rlk.1; mouse.
DR   CTD; 56395; -.
DR   MGI; MGI:1930765; Tmem115.
DR   GeneTree; ENSGT00390000002470; -.
DR   HOGENOM; HBG314498; -.
DR   HOVERGEN; HBG027575; -.
DR   InParanoid; Q9WUH1; -.
DR   OMA; YLFTVRI; -.
DR   OrthoDB; EOG4J1193; -.
DR   PhylomeDB; Q9WUH1; -.
DR   NextBio; 312496; -.
DR   ArrayExpress; Q9WUH1; -.
DR   Bgee; Q9WUH1; -.
DR   CleanEx; MM_TMEM115; -.
DR   Genevestigator; Q9WUH1; -.
DR   GermOnline; ENSMUSG00000010045; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR013861; DUF1751_Mem_euk.
DR   Pfam; PF08551; DUF1751; 1.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    350       Transmembrane protein 115.
FT                                /FTId=PRO_0000058452.
FT   TRANSMEM     12     34       Helical; (Potential).
FT   TRANSMEM     38     60       Helical; (Potential).
FT   TRANSMEM     72     94       Helical; (Potential).
FT   TRANSMEM     98    120       Helical; (Potential).
FT   TRANSMEM    127    149       Helical; (Potential).
FT   TRANSMEM    164    183       Helical; (Potential).
FT   TRANSMEM    190    208       Helical; (Potential).
FT   TRANSMEM    223    245       Helical; (Potential).
FT   MOD_RES     320    320       Phosphoserine.
SQ   SEQUENCE   350 AA;  38099 MW;  9D8B9B164CA2842D CRC64;
     MQRALPGARQ HLGAILASAS VVVKALCAVV LFLYLLSFAV DTGCLAVTPG YLFPPNFWIW
     TLATHGLMEQ HVWDVAISLA TVVVAGRLLE PLWGALELLI FFSVVNVSVG LLGALAYLLT
     YMASFNLVYL FTIRIHGALG FLGGVLVALK QTMGDCVVLR VPQVRVSVVP MLLLALLLLL
     RLATLLQSPA LASYGFGLLS SWVYLRFYQR HSRGRGDMAD HFAFATFFPE ILQPVVGLLA
     NLVHGLLVKV KICQKTVKRY DVGAPSSITI SLPGTDPQDA ERRRQLALKA LNERLKRVED
     QSAWPSMDDD EEEAGAKTDS PLPLEEASTP PGKVTVPESS LITLETAPLL
//
ID   ZN238_MOUSE             Reviewed;         522 AA.
AC   Q9WUK6; Q3UHU9; Q7TMA6; Q80YQ4;
DT   21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Zinc finger protein 238;
DE            Short=Zfp-238;
DE   AltName: Full=58 kDa repressor protein;
DE   AltName: Full=Transcriptional repressor RP58;
GN   Name=Znf238; Synonyms=Rp58, Zfp238;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver, and Thymus;
RX   MEDLINE=20184722; PubMed=10721697; DOI=10.1016/S0378-1119(99)00477-1;
RA   Meng G., Inazawa J., Ishida R., Tokura K., Nakahara K., Aoki K.,
RA   Kasai M.;
RT   "Structural analysis of the gene encoding RP58, a sequence-specific
RT   transrepressor associated with heterochromatin.";
RL   Gene 242:59-64(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=17447250; DOI=10.1002/cne.21350;
RA   Ohtaka-Maruyama C., Miwa A., Kawano H., Kasai M., Okado H.;
RT   "Spatial and temporal expression of RP58, a novel zinc finger
RT   transcriptional repressor, in mouse brain.";
RL   J. Comp. Neurol. 502:1098-1108(2007).
RN   [5]
RP   FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=19409883; DOI=10.1016/j.ydbio.2009.04.030;
RA   Okado H., Ohtaka-Maruyama C., Sugitani Y., Fukuda Y., Ishida R.,
RA   Hirai S., Miwa A., Takahashi A., Aoki K., Mochida K., Suzuki O.,
RA   Honda T., Nakajima K., Ogawa M., Terashima T., Matsuda J., Kawano H.,
RA   Kasai M.;
RT   "The transcriptional repressor RP58 is crucial for cell-division
RT   patterning and neuronal survival in the developing cortex.";
RL   Dev. Biol. 331:140-151(2009).
RN   [6]
RP   FUNCTION.
RX   PubMed=20059953; DOI=10.1016/j.devcel.2009.10.011;
RA   Yokoyama S., Ito Y., Ueno-Kudoh H., Shimizu H., Uchibe K., Albini S.,
RA   Mitsuoka K., Miyaki S., Kiso M., Nagai A., Hikata T., Osada T.,
RA   Fukuda N., Yamashita S., Harada D., Mezzano V., Kasai M., Puri P.L.,
RA   Hayashizaki Y., Okado H., Hashimoto M., Asahara H.;
RT   "A systems approach reveals that the myogenesis genome network is
RT   regulated by the transcriptional repressor RP58.";
RL   Dev. Cell 17:836-848(2009).
CC   -!- FUNCTION: Transcriptional repressor that plays a role in various
CC       developmental processes such as myogenesis and brain development.
CC       Specifically binds the consensus DNA sequence 5'-
CC       [AC]ACATCTG[GT][AC]-3' which contains the E box core, and acts by
CC       recruiting chromatin remodeling multiprotein complexes. Plays a
CC       key role in myogenesis by directly repressing the expression of
CC       ID2 and ID3, 2 inhibitors of skeletal myogenesis. Also involved in
CC       controlling cell division of progenitor cells and regulating the
CC       survival of postmitotic cortical neurons. May also play a role in
CC       the organization of chromosomes in the nucleus.
CC   -!- SUBUNIT: Interacts with DNMT3A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Associates with condensed
CC       chromatin.
CC   -!- DEVELOPMENTAL STAGE: In the developing brain, expression is
CC       detected at embryonic day (E) 10 in the neuroepithelium, and
CC       subsequently in the ventricular zones of the cerebral cortex in
CC       the E12 embryo. Strong expression is observed in the preplate in
CC       the cerebral cortex from this stage onward. High levels of
CC       expression continue to be detected in the cortical plate and
CC       subventricular zone of the neocortex, hippocampus, and parts of
CC       the amygdala, but not in the thalamus or striatum. In the
CC       developing cerebral cortex, it is expressed both in postmitotic
CC       glutamatergic projection neurons and in their progenitor cells,
CC       but not in GABAergic interneurons. Also expressed in the adult
CC       neocortex, hippocampus, parts of the amygdala and granule cells in
CC       the cerebellum.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: Death shortly after birth. Brain of mutant
CC       mice display dysplasia of the neocortex and of the hippocampus,
CC       reduction of the number of mature cortical neurons and defects of
CC       laminar organization. In the cortex, an impaired cell-division
CC       patterning during the late embryonic stage and an enhancement of
CC       apoptosis of the postmitotic neurons are observed.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. ZNF238 subfamily.
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC   -!- SIMILARITY: Contains 4 C2H2-type zinc fingers.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH50909.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF140224; AAD34547.1; -; mRNA.
DR   EMBL; AK147200; BAE27758.1; -; mRNA.
DR   EMBL; BC050909; AAH50909.1; ALT_INIT; mRNA.
DR   EMBL; BC054529; AAH54529.1; -; mRNA.
DR   EMBL; BC054742; AAH54742.1; -; mRNA.
DR   IPI; IPI00466236; -.
DR   RefSeq; NP_001012330.1; NM_001012330.1.
DR   RefSeq; NP_038943.3; NM_013915.3.
DR   UniGene; Mm.480309; -.
DR   ProteinModelPortal; Q9WUK6; -.
DR   SMR; Q9WUK6; 1-118, 342-505.
DR   STRING; Q9WUK6; -.
DR   PhosphoSite; Q9WUK6; -.
DR   PRIDE; Q9WUK6; -.
DR   Ensembl; ENSMUST00000077225; ENSMUSP00000076463; ENSMUSG00000063659.
DR   Ensembl; ENSMUST00000094276; ENSMUSP00000091831; ENSMUSG00000063659.
DR   GeneID; 30928; -.
DR   KEGG; mmu:30928; -.
DR   UCSC; uc007dul.1; mouse.
DR   CTD; 30928; -.
DR   MGI; MGI:1353609; Zfp238.
DR   GeneTree; ENSGT00600000084014; -.
DR   HOVERGEN; HBG059113; -.
DR   InParanoid; Q9WUK6; -.
DR   OrthoDB; EOG47SSDG; -.
DR   NextBio; 307332; -.
DR   ArrayExpress; Q9WUK6; -.
DR   Bgee; Q9WUK6; -.
DR   CleanEx; MM_ZFP238; -.
DR   Genevestigator; Q9WUK6; -.
DR   GermOnline; ENSMUSG00000063659; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0016564; F:transcription repressor activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0010553; P:negative regulation of gene-specific transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IMP:UniProtKB.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR013069; BTB_POZ.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 3.
DR   Pfam; PF00651; BTB; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   2: Evidence at transcript level;
KW   Developmental protein; DNA-binding; Metal-binding; Nucleus;
KW   Phosphoprotein; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    522       Zinc finger protein 238.
FT                                /FTId=PRO_0000047478.
FT   DOMAIN       24     91       BTB.
FT   ZN_FING     370    392       C2H2-type 1.
FT   ZN_FING     410    432       C2H2-type 2.
FT   ZN_FING     438    460       C2H2-type 3.
FT   ZN_FING     466    489       C2H2-type 4.
FT   REGION      310    427       Interaction with DNMT3A (By similarity).
FT   MOD_RES     516    516       Phosphoserine (By similarity).
FT   MOD_RES     517    517       Phosphoserine (By similarity).
FT   CONFLICT     42     42       L -> V (in Ref. 3; AAH54742/AAH54529).
SQ   SEQUENCE   522 AA;  58385 MW;  41E169E690D8B849 CRC64;
     MEFPDHSRHL LQCLSEQRHQ GFLCDCTVLV GDAQFRAHRA VLASCSMYFH LFYKDQLDKR
     DIVHLNSDIV TAPAFALLLE FMYEGKLQFK DLPIEDVLAA ASYLHMYDIV KVCKKKLKEK
     ATTEADSTKK EEDASSCSDK VESLSDGSSH MAGDLPSDED EGEDDKLNIL PSKRDLAAEP
     GNMWMRLPSD SAGIPQAGGE AEPHATAAGK TVASPCSSTE SLSQRSVTSV RDSADVDCVL
     DLSVKSSLSG VENLNSSYFS SQDVLRSNLV QVKVEKEASC DESDVGTNDY DMEHSTVKES
     VSTNNRVQYE PAHLAPLRED SVLRELDRED KASDDEMMTP ESERVQVEGG MENSLLPYVS
     NILSPAGQIF MCPLCNKVFP SPHILQIHLS THFREQDGIR SKPAADVNVP TCSLCGKTFS
     CMYTLKRHER THSGEKPYTC TQCGKSFQYS HNLSRHAVVH TREKPHACKW CERRFTQSGD
     LYRHIRKFHC ELVNSLSVKS EALSLPTVRD WTLEDSSQEL WK
//
ID   ARL3_MOUSE              Reviewed;         182 AA.
AC   Q9WUL7;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=ADP-ribosylation factor-like protein 3;
GN   Name=Arl3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PDE6D, AND MUTAGENESIS OF
RP   THR-31 AND GLN-71.
RX   MEDLINE=99448378; PubMed=10518933; DOI=10.1016/S0014-5793(99)01117-5;
RA   Linari M., Hanzal-Bayer M., Becker J.;
RT   "The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE
RT   delta, interacts with the Arf-like protein Arl3 in a GTP specific
RT   manner.";
RL   FEBS Lett. 458:55-59(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, INTERACTION WITH PDE6D, AND GTP/GDP-BINDING.
RX   PubMed=15979089; DOI=10.1016/j.jmb.2005.05.036;
RA   Hanzal-Bayer M., Linari M., Wittinghofer A.;
RT   "Properties of the interaction of Arf-like protein 2 with PDEdelta.";
RL   J. Mol. Biol. 350:1074-1082(2005).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH GDP AND
RP   MAGNESIUM IONS.
RX   PubMed=11188688; DOI=10.1016/S0969-2126(00)00531-1;
RA   Hillig R.C., Hanzal-Bayer M., Linari M., Becker J., Wittinghofer A.,
RA   Renault L.;
RT   "Structural and biochemical properties show ARL3-GDP as a distinct GTP
RT   binding protein.";
RL   Structure 8:1239-1245(2000).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 17-177 IN COMPLEX WITH HUMAN
RP   RP2 AND GTP, FUNCTION, INTERACTION WITH HUMAN RP2, AND MUTAGENESIS OF
RP   GLN-49; GLN-71; LYS-98; GLU-164 AND ASP-168.
RX   PubMed=18376416; DOI=10.1038/nsmb.1396;
RA   Veltel S., Gasper R., Eisenacher E., Wittinghofer A.;
RT   "The retinitis pigmentosa 2 gene product is a GTPase-activating
RT   protein for Arf-like 3.";
RL   Nat. Struct. Mol. Biol. 15:373-380(2008).
CC   -!- FUNCTION: Small GTP-binding protein which cycles between an
CC       inactive GDP-bound and an active GTP-bound form, and the rate of
CC       cycling is regulated by guanine nucleotide exchange factors (GEF)
CC       and GTPase-activating proteins (GAP). GTP-binding protein that
CC       does not act as an allosteric activator of the cholera toxin
CC       catalytic subunit. Requires assistance from GTPase-activating
CC       proteins (GAPs) like RP2 and PDE6D, in order to cycle between
CC       inactive GDP-bound and active GTP-bound forms. Required for normal
CC       cytokinesis.
CC   -!- SUBUNIT: Found in a complex with ARL3, RP2 and UNC119; RP2 induces
CC       hydrolysis of GTP ARL3 in the complex, leading to the release of
CC       UNC119. Interacts with SYS1 and SCOC. Interacts with ARL2BP; the
CC       GTP-bound form interacts with ARL2BP. Interacts with RP2;
CC       interaction is direct and stimulated with the activated GTP-bound
CC       form of ARL3. Microtubule-associated protein. Does not interact
CC       with TBCC (By similarity). Interacts with RP2 and PDE6D. Interacts
CC       with PDE6D; the interaction occurs specifically with the GTP-bound
CC       form of ARL3.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane; Peripheral
CC       membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton,
CC       spindle. Nucleus. Cytoplasm, cytoskeleton, centrosome (By
CC       similarity). Cytoplasm (By similarity). Cell projection, cilium
CC       (By similarity). Note=Detected predominantly in the photoreceptor
CC       connecting cilium. Centrosome-associated throughout the cell
CC       cycle. Not detected to interphase microtubules (By similarity).
CC       Present on the mitotic spindle.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF143241; AAD33067.1; -; mRNA.
DR   EMBL; BC042941; AAH42941.1; -; mRNA.
DR   IPI; IPI00124787; -.
DR   RefSeq; NP_062692.1; NM_019718.2.
DR   UniGene; Mm.22085; -.
DR   PDB; 1FZQ; X-ray; 1.70 A; A=2-182.
DR   PDB; 3BH6; X-ray; 2.60 A; A=17-177.
DR   PDB; 3BH7; X-ray; 1.90 A; A=17-177.
DR   PDBsum; 1FZQ; -.
DR   PDBsum; 3BH6; -.
DR   PDBsum; 3BH7; -.
DR   ProteinModelPortal; Q9WUL7; -.
DR   SMR; Q9WUL7; 2-177.
DR   DIP; DIP-29025N; -.
DR   STRING; Q9WUL7; -.
DR   REPRODUCTION-2DPAGE; IPI00124787; -.
DR   REPRODUCTION-2DPAGE; Q9WUL7; -.
DR   PRIDE; Q9WUL7; -.
DR   Ensembl; ENSMUST00000026009; ENSMUSP00000026009; ENSMUSG00000025035.
DR   GeneID; 56350; -.
DR   KEGG; mmu:56350; -.
DR   UCSC; uc008htt.1; mouse.
DR   CTD; 56350; -.
DR   MGI; MGI:1929699; Arl3.
DR   GeneTree; ENSGT00600000084074; -.
DR   HOGENOM; HBG745225; -.
DR   HOVERGEN; HBG002073; -.
DR   InParanoid; Q9WUL7; -.
DR   OMA; PTAGFNI; -.
DR   OrthoDB; EOG418BPH; -.
DR   PhylomeDB; Q9WUL7; -.
DR   NextBio; 312350; -.
DR   ArrayExpress; Q9WUL7; -.
DR   Bgee; Q9WUL7; -.
DR   CleanEx; MM_ARL3; -.
DR   Genevestigator; Q9WUL7; -.
DR   GermOnline; ENSMUSG00000025035; Mus musculus.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0032391; C:photoreceptor connecting cilium; ISS:UniProtKB.
DR   GO; GO:0005876; C:spindle microtubule; ISS:UniProtKB.
DR   GO; GO:0019003; F:GDP binding; IDA:UniProtKB.
DR   GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR   GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0000910; P:cytokinesis; ISS:UniProtKB.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR006688; ARF.
DR   InterPro; IPR006689; ARF/SAR.
DR   InterPro; IPR005225; Small_GTP-bd.
DR   PANTHER; PTHR11711; ARF/SAR; 1.
DR   Pfam; PF00025; Arf; 1.
DR   PRINTS; PR00328; SAR1GTPBP.
DR   SMART; SM00177; ARF; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51417; ARF; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Cell projection; Cytoplasm;
KW   Cytoskeleton; Golgi apparatus; GTP-binding; Lipoprotein; Magnesium;
KW   Membrane; Metal-binding; Myristate; Nucleotide-binding; Nucleus;
KW   Phosphoprotein.
FT   INIT_MET      1      1       Removed (Potential).
FT   CHAIN         2    182       ADP-ribosylation factor-like protein 3.
FT                                /FTId=PRO_0000207457.
FT   NP_BIND      24     31       GTP.
FT   NP_BIND      67     71       GTP (By similarity).
FT   NP_BIND     126    129       GTP.
FT   NP_BIND     159    161       GTP.
FT   METAL        31     31       Magnesium.
FT   METAL        48     48       Magnesium.
FT   BINDING      48     48       GTP.
FT   BINDING      70     70       GTP; via amide nitrogen.
FT   MOD_RES      32     32       Phosphothreonine (By similarity).
FT   LIPID         2      2       N-myristoyl glycine (Potential).
FT   MUTAGEN      31     31       T->N: Inihibits interaction with PDE6D.
FT   MUTAGEN      49     49       Q->L: Does not reduce the interaction
FT                                with RP2.
FT   MUTAGEN      71     71       Q->L: Does not inihibit interaction with
FT                                PDE6D.
FT   MUTAGEN      71     71       Q->L: Inhibits RP2-dependent GTP-
FT                                hydrolysis rate.
FT   MUTAGEN      98     98       K->Q: Does not reduce the interaction
FT                                with RP2.
FT   MUTAGEN     164    164       E->A: Reduces the interaction with RP2;
FT                                when associated with A-168.
FT   MUTAGEN     168    168       D->A: Reduces the interaction with RP2;
FT                                when associated with A-164.
FT   HELIX         6      9
FT   STRAND       18     25
FT   HELIX        30     37
FT   STRAND       43     48
FT   STRAND       51     58
FT   STRAND       61     67
FT   HELIX        72     74
FT   HELIX        75     82
FT   STRAND       86     93
FT   HELIX        97     99
FT   HELIX       100    110
FT   HELIX       114    116
FT   STRAND      121    126
FT   HELIX       136    142
FT   HELIX       145    147
FT   STRAND      153    157
FT   TURN        160    162
FT   HELIX       166    175
SQ   SEQUENCE   182 AA;  20487 MW;  16B85B2268ADB9DE CRC64;
     MGLLSILRKL KSAPDQEVRI LLLGLDNAGK TTLLKQLASE DISHITPTQG FNIKSVQSQG
     FKLNVWDIGG QRKIRPYWRS YFENTDILIY VIDSADRKRF EETGQELTEL LEEEKLSCVP
     VLIFANKQDL LTAAPASEIA EGLNLHTIRD RVWQIQSCSA LTGEGVQDGM NWVCKNVNAK
     KK
//
ID   COR1B_MOUSE             Reviewed;         484 AA.
AC   Q9WUM3; Q3UEB1; Q9CVA2;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Coronin-1B;
DE   AltName: Full=Coronin-2;
GN   Name=Coro1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98449467; PubMed=9778037;
RA   Okumura M., Kung C., Wong S., Rodgers M., Thomas M.L.;
RT   "Definition of family of coronin-related proteins conserved between
RT   humans and mice: close genetic linkage between coronin-2 and CD45-
RT   associated protein.";
RL   DNA Cell Biol. 17:779-787(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF 34-46; 135-145 AND 423-456, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   TISSUE SPECIFICITY, AND INTERACTION WITH ACTR2; ARPC1B AND ARPC2.
RX   PubMed=16027158; DOI=10.1074/jbc.M504146200;
RA   Cai L., Holoweckyj N., Schaller M.D., Bear J.E.;
RT   "Phosphorylation of coronin 1B by protein kinase C regulates
RT   interaction with Arp2/3 and cell motility.";
RL   J. Biol. Chem. 280:31913-31923(2005).
CC   -!- FUNCTION: Regulates leading edge dynamics and cell motility in
CC       fibroblasts. May be involved in cytokinesis and signal
CC       transduction (By similarity).
CC   -!- SUBUNIT: Forms homooligomers, but does not form complexes with the
CC       other coronins. Interacts with Arp2/3 complex components,
CC       including ACTR2, ARPC1B and ARPC2. Binds actin (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Note=Localized to the leading edge in fibroblasts, as well as
CC       weakly along actin stress fibers (By similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- PTM: Phosphorylation on Ser-2 regulates the interaction with the
CC       Arp2/3 complex and cell motility in fibroblasts. Phosphorylation
CC       does not seem to affect subcellular location (By similarity).
CC   -!- SIMILARITY: Belongs to the WD repeat coronin family.
CC   -!- SIMILARITY: Contains 5 WD repeats.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF143956; AAD32704.1; -; mRNA.
DR   EMBL; AK008947; BAB25985.1; -; mRNA.
DR   EMBL; AK149639; BAE29000.1; -; mRNA.
DR   IPI; IPI00124819; -.
DR   RefSeq; NP_035908.1; NM_011778.2.
DR   UniGene; Mm.276859; -.
DR   UniGene; Mm.471743; -.
DR   ProteinModelPortal; Q9WUM3; -.
DR   SMR; Q9WUM3; 10-394.
DR   STRING; Q9WUM3; -.
DR   PhosphoSite; Q9WUM3; -.
DR   PRIDE; Q9WUM3; -.
DR   Ensembl; ENSMUST00000008893; ENSMUSP00000008893; ENSMUSG00000024835.
DR   GeneID; 23789; -.
DR   KEGG; mmu:23789; -.
DR   UCSC; uc008fyy.1; mouse.
DR   CTD; 23789; -.
DR   MGI; MGI:1345963; Coro1b.
DR   GeneTree; ENSGT00550000074317; -.
DR   HOGENOM; HBG735393; -.
DR   HOVERGEN; HBG059978; -.
DR   InParanoid; Q9WUM3; -.
DR   OMA; LWDPENL; -.
DR   OrthoDB; EOG4RNB8C; -.
DR   PhylomeDB; Q9WUM3; -.
DR   NextBio; 303387; -.
DR   ArrayExpress; Q9WUM3; -.
DR   Bgee; Q9WUM3; -.
DR   CleanEx; MM_CORO1B; -.
DR   Genevestigator; Q9WUM3; -.
DR   GermOnline; ENSMUSG00000024835; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR015505; Coronin.
DR   InterPro; IPR015048; DUF1899.
DR   InterPro; IPR015049; DUF1900.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   PANTHER; PTHR10856; Coronin; 1.
DR   Pfam; PF08953; DUF1899; 1.
DR   Pfam; PF08954; DUF1900; 1.
DR   Pfam; PF00400; WD40; 3.
DR   SMART; SM00320; WD40; 3.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Phosphoprotein; Repeat; WD repeat.
FT   CHAIN         1    484       Coronin-1B.
FT                                /FTId=PRO_0000050923.
FT   REPEAT       80    120       WD 1.
FT   REPEAT      130    170       WD 2.
FT   REPEAT      174    213       WD 3.
FT   REPEAT      217    260       WD 4.
FT   REPEAT      265    305       WD 5.
FT   COILED      444    482       Potential.
FT   MOD_RES       2      2       Phosphoserine (By similarity).
FT   CONFLICT    393    393       R -> G (in Ref. 2; BAB25985).
SQ   SEQUENCE   484 AA;  53912 MW;  9631CC02E7EAC72F CRC64;
     MSFRKVVRQS KFRHVFGQPV KNDQCYEDIR VSRVTWDSTF CAVNPKFLAV IVEASGGGAF
     MVLPLNKTGR IDKAYPTVCG HTGPVLDIDW CPHNDEVIAS GSEDCTVMVW QIPENGLTSP
     LTEPVVVLEG HTKRVGIITW HPTARNVLLS AGCDNVVLIW NVGTAEELYR LDSLHPDLIY
     NVSWNHNGSL FCSACKDKSV RIIDPRRGTL VAEREKAHEG ARPMRAIFLA DGKVFTTGFS
     RMSERQLALW DPENLEEPMA LQELDSSNGA LLPFYDPDTS VVYVCGKGDS SIRYFEITDE
     PPYIHFLNTF TSKEPQRGMG SMPKRGLEVS KCEIARFYKL HERKCEPIVM TVPRKSDLFQ
     DDLYPDTAGP EAALEAEDWV SGQDANPILI SLREAYVPSK QRDLKVSRRN VLSDSRPASY
     SRSGASTATA VTDVPSGNLA GAGEAGKLEE VMQELRALRM LVKEQGERIS RLEEQLGRME
     NGDT
//
ID   SUCA_MOUSE              Reviewed;         346 AA.
AC   Q9WUM5; Q8C2C3; Q9DBA3; Q9DCI8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 4.
DT   08-MAR-2011, entry version 107.
DE   RecName: Full=Succinyl-CoA ligase [GDP-forming] subunit alpha, mitochondrial;
DE            EC=6.2.1.4;
DE   AltName: Full=Succinyl-CoA synthetase subunit alpha;
DE            Short=SCS-alpha;
DE   Flags: Precursor;
GN   Name=Suclg1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, Kidney, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-346.
RC   TISSUE=Heart;
RA   Tews K.N., Milavetz B.M., Lambeth D.O.;
RT   "Sequence of the alpha subunit of succinyl-CoA synthetase in mouse.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-346.
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 45-53; 58-92; 154-169 AND 279-295, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-280, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Heart;
RX   PubMed=17451654; DOI=10.1016/j.bbrc.2007.04.015;
RA   Jeon H.B., Choi E.S., Yoon J.H., Hwang J.H., Chang J.W., Lee E.K.,
RA   Choi H.W., Park Z.-Y., Yoo Y.J.;
RT   "A proteomics approach to identify the ubiquitinated proteins in mouse
RT   heart.";
RL   Biochem. Biophys. Res. Commun. 357:731-736(2007).
CC   -!- CATALYTIC ACTIVITY: GTP + succinate + CoA = GDP + phosphate +
CC       succinyl-CoA.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity).
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha
CC       subunit family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD33927.2; Type=Erroneous initiation;
CC       Sequence=AAH11087.1; Type=Erroneous initiation;
CC       Sequence=BAB22331.1; Type=Erroneous initiation;
CC       Sequence=BAB23804.1; Type=Erroneous initiation;
CC       Sequence=BAC40634.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK002754; BAB22331.1; ALT_INIT; mRNA.
DR   EMBL; AK005080; BAB23804.1; ALT_INIT; mRNA.
DR   EMBL; AK088888; BAC40634.1; ALT_INIT; mRNA.
DR   EMBL; AF144101; AAD33927.2; ALT_INIT; mRNA.
DR   EMBL; BC011087; AAH11087.1; ALT_INIT; mRNA.
DR   IPI; IPI00406442; -.
DR   RefSeq; NP_063932.2; NM_019879.3.
DR   UniGene; Mm.29845; -.
DR   ProteinModelPortal; Q9WUM5; -.
DR   SMR; Q9WUM5; 42-346.
DR   STRING; Q9WUM5; -.
DR   PhosphoSite; Q9WUM5; -.
DR   PRIDE; Q9WUM5; -.
DR   Ensembl; ENSMUST00000064740; ENSMUSP00000065113; ENSMUSG00000052738.
DR   GeneID; 56451; -.
DR   KEGG; mmu:56451; -.
DR   UCSC; uc009cjm.1; mouse.
DR   CTD; 56451; -.
DR   MGI; MGI:1927234; Suclg1.
DR   eggNOG; roNOG16542; -.
DR   GeneTree; ENSGT00530000063275; -.
DR   HOGENOM; HBG615372; -.
DR   HOVERGEN; HBG000957; -.
DR   InParanoid; Q9WUM5; -.
DR   OrthoDB; EOG4WQ136; -.
DR   BRENDA; 6.2.1.4; 244.
DR   NextBio; 312668; -.
DR   ArrayExpress; Q9WUM5; -.
DR   Bgee; Q9WUM5; -.
DR   CleanEx; MM_SUCLG1; -.
DR   Genevestigator; Q9WUM5; -.
DR   GermOnline; ENSMUSG00000052738; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0003878; F:ATP citrate synthase activity; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004776; F:succinate-CoA ligase (GDP-forming) activity; IEA:EC.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR   InterPro; IPR003781; CoA-bd.
DR   InterPro; IPR005810; CoA_lig_alpha.
DR   InterPro; IPR005811; CoA_ligase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:3.40.50.261; Succinyl-CoA_synth-like; 1.
DR   Pfam; PF02629; CoA_binding; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PIRSF; PIRSF001553; SucCS_alpha; 1.
DR   PRINTS; PR01798; SCOASYNTHASE.
DR   SMART; SM00881; CoA_binding; 1.
DR   SUPFAM; SSF52210; CoA_ligase; 1.
DR   TIGRFAMs; TIGR01019; sucCoAalpha; 1.
DR   PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR   PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; GTP-binding; Isopeptide bond;
KW   Ligase; Mitochondrion; Nucleotide-binding; Phosphoprotein;
KW   Transit peptide; Tricarboxylic acid cycle; Ubl conjugation.
FT   TRANSIT       1     40       Mitochondrion (By similarity).
FT   CHAIN        41    346       Succinyl-CoA ligase [GDP-forming] subunit
FT                                alpha, mitochondrial.
FT                                /FTId=PRO_0000033341.
FT   ACT_SITE    299    299       Tele-phosphohistidine intermediate (By
FT                                similarity).
FT   MOD_RES      54     54       N6-acetyllysine (By similarity).
FT   CROSSLNK    280    280       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT   CONFLICT      6      6       V -> L (in Ref. 2; AAD33927).
FT   CONFLICT    175    175       V -> I (in Ref. 1; BAC40634).
FT   CONFLICT    188    188       G -> A (in Ref. 1; BAB22331).
FT   CONFLICT    201    201       R -> K (in Ref. 2; AAD33927).
FT   CONFLICT    220    220       Q -> H (in Ref. 2; AAD33927).
SQ   SEQUENCE   346 AA;  36155 MW;  1EB7A444DFCE32FA CRC64;
     MTATVVAAAA TATMVSSSSG LAAARLLSRT FLLQQNGIRH GSYTASRKHI YIDKNTKIIC
     QGFTGKQGTF HSQQALEYGT KLVGGTTPGK GGQKHLGLPV FNTVKEAKEK TGATASVIYV
     PPPFAAAAIN EAIDAEIPLV VCITEGIPQQ DMVRVKHRLT RQGTTRLIGP NCPGVINPGE
     CKIGIMPGHI HKKGRIGIVS RSGTLTYEAV HQTTQVGLGQ SLCIGIGGDP FNGTDFIDCL
     EVFLNDPATE GIILIGEIGG HAEENAAAFL KEHNSGPKAK PVVSFIAGIT APPGRRMGHA
     GAIIAGGKGG AKEKISALQS AGVVVSMSPA QLGTTIYKEF EKRKML
//
ID   TNIP1_MOUSE             Reviewed;         647 AA.
AC   Q9WUU8; Q922A9; Q922F7; Q9EPP8; Q9R0X3;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=TNFAIP3-interacting protein 1;
DE   AltName: Full=A20-binding inhibitor of NF-kappa-B activation;
DE            Short=ABIN;
DE   AltName: Full=Nef-associated factor 1;
DE            Short=Naf1;
DE   AltName: Full=Virion-associated nuclear shuttling protein;
DE            Short=VAN;
DE            Short=mVAN;
GN   Name=Tnip1; Synonyms=Abin, Naf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX   MEDLINE=99315915; PubMed=10385526; DOI=10.1083/jcb.145.7.1471;
RA   Heyninck K., De Valck D., Vanden Berghe W., Van Criekinge W.,
RA   Contreras R., Fiers W., Haegeman G., Beyaert R.;
RT   "The zinc finger protein A20 inhibits TNF-induced NF-B-dependent gene
RT   expression by interfering with an RIP- or TRAF2-mediated
RT   transactivation signal and directly binds to a novel NF-B-inhibiting
RT   protein ABIN.";
RL   J. Cell Biol. 145:1471-1482(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 97-647 (ISOFORM 3).
RX   MEDLINE=20541981; PubMed=11090181;
RX   DOI=10.1128/JVI.74.24.11811-11824.2000;
RA   Gupta K., Ott D., Hope T.J., Siliciano R.F., Boeke J.D.;
RT   "A human nuclear shuttling protein that interacts with human
RT   immunodeficiency virus type 1 matrix is packaged into virions.";
RL   J. Virol. 74:11811-11824(2000).
CC   -!- FUNCTION: Increases cell surface CD4(T4) antigen expression (By
CC       similarity). Interacts with zinc finger protein A20/TNFAIP3 and
CC       inhibits TNF-induced NF-kappa-B-dependent gene expression by
CC       interfering with an RIP- or TRAF2-mediated transactivation signal.
CC   -!- SUBUNIT: Interacts with TNFAIP3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Shuttles between the nucleus and cytoplasm in a
CC       CRM1-dependent manner (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=ABINl;
CC         IsoId=Q9WUU8-1; Sequence=Displayed;
CC       Name=2; Synonyms=ABINs;
CC         IsoId=Q9WUU8-2; Sequence=VSP_003914;
CC       Name=3;
CC         IsoId=Q9WUU8-3; Sequence=VSP_003915;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Abundant in heart and skeletal
CC       muscle and expressed at lower levels in thymus, liver, kidney,
CC       brain and intestinal tract.
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DR   EMBL; AJ242777; CAB44239.1; -; mRNA.
DR   EMBL; AJ242778; CAB44240.1; -; mRNA.
DR   EMBL; BC008186; AAH08186.1; -; mRNA.
DR   EMBL; BC008665; AAH08665.1; -; mRNA.
DR   EMBL; AX011241; CAC07546.1; -; Unassigned_DNA.
DR   EMBL; AY012159; AAG42155.2; -; mRNA.
DR   IPI; IPI00228584; -.
DR   IPI; IPI00230531; -.
DR   IPI; IPI00754323; -.
DR   RefSeq; NP_001186205.1; NM_001199276.1.
DR   UniGene; Mm.259671; -.
DR   ProteinModelPortal; Q9WUU8; -.
DR   STRING; Q9WUU8; -.
DR   PhosphoSite; Q9WUU8; -.
DR   PRIDE; Q9WUU8; -.
DR   Ensembl; ENSMUST00000018482; ENSMUSP00000018482; ENSMUSG00000020400.
DR   Ensembl; ENSMUST00000102731; ENSMUSP00000099792; ENSMUSG00000020400.
DR   Ensembl; ENSMUST00000108889; ENSMUSP00000104517; ENSMUSG00000020400.
DR   GeneID; 57783; -.
DR   KEGG; mmu:57783; -.
DR   UCSC; uc007iyl.1; mouse.
DR   UCSC; uc007iym.1; mouse.
DR   UCSC; uc007iyp.1; mouse.
DR   CTD; 57783; -.
DR   MGI; MGI:1926194; Tnip1.
DR   GeneTree; ENSGT00510000046908; -.
DR   HOGENOM; HBG714765; -.
DR   HOVERGEN; HBG019072; -.
DR   InParanoid; Q9WUU8; -.
DR   OrthoDB; EOG4ZS934; -.
DR   NextBio; 313974; -.
DR   ArrayExpress; Q9WUU8; -.
DR   Bgee; Q9WUU8; -.
DR   CleanEx; MM_NAF1; -.
DR   CleanEx; MM_TNIP1; -.
DR   Genevestigator; Q9WUU8; -.
DR   GermOnline; ENSMUSG00000020400; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Nucleus.
FT   CHAIN         1    647       TNFAIP3-interacting protein 1.
FT                                /FTId=PRO_0000096692.
FT   REGION       95    425       Interacts with Nef.
FT   COILED       39     72       Potential.
FT   COILED      209    270       Potential.
FT   COILED      311    551       Potential.
FT   MOTIF       537    543       Nuclear localization signal (Potential).
FT   COMPBIAS    162    165       Poly-Pro.
FT   COMPBIAS    552    647       Pro-rich.
FT   VAR_SEQ       1     53       Missing (in isoform 2).
FT                                /FTId=VSP_003914.
FT   VAR_SEQ     638    647       SADNDCDGPQ -> PADLRLPKV (in isoform 3).
FT                                /FTId=VSP_003915.
FT   CONFLICT     97     98       VQ -> TR (in Ref. 3; AAG42155).
FT   CONFLICT    308    308       A -> V (in Ref. 2; AAH08186).
FT   CONFLICT    533    533       A -> V (in Ref. 2; AAH08186).
SQ   SEQUENCE   647 AA;  73050 MW;  4280879A8C24A16E CRC64;
     MEGRGPYRIY DPGGSTPLGE VSAAFERLVE ENTRLKGKMQ GIKMLGELLE ESQMEASRLR
     QKAEELVKDS ELSPPTSAPS LVSFDDLAEL TGQDTKVQVH PATSTAATTT ATATTGNSME
     KPEPASKSPS NGASSDFEVV PTEEQNSPET GSHPTNMMDL GPPPPEDSNL KLHLQRLETT
     LSVCAEEPDH SQLFTHLGRM ALEFNRLASK VHKNEQRTSI LQTLCEQLRQ ENEALKAKLD
     KGLEQRDLAA ERLREENTEL KKLLMNSSCK EGLCGQPSSP KPEGAGKKGV AGQQQASVMA
     SKVPEAGAFG AAEKKVKLLE QQRMELLEVN KQWDQHFRSM KQQYEQKITE LRQKLVDLQK
     QVTELEAERE QKQRDFDRKL LLAKSKIEME ETDKEQLTAE AKELRQKVRY LQDQLSPLTR
     QREYQEKEIQ RLNKALEEAL SIQASPSSPP AAFGSPEGVG GHLRKQELVT QNELLKQQVK
     IFEEDFQRER SDRERMNEEK EELKKQVEKL QAQVTLTNAQ LKTLKEEEKA KEALKQQKRK
     AKASGERYHM EPHPEHVCGA YPYAYPPMPA MVPHHAYKDW SQIRYPPPPV PMEHPPPHPN
     SRLFHLPEYT WRPPCAGIRN QSSQVMDPPP DRPAEPESAD NDCDGPQ
//
ID   GABR1_MOUSE             Reviewed;         960 AA.
AC   Q9WV18; Q6PGJ2; Q9WU48; Q9WV15; Q9WV16; Q9WV17;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 110.
DE   RecName: Full=Gamma-aminobutyric acid type B receptor subunit 1;
DE            Short=GABA-B receptor 1;
DE            Short=GABA-B-R1;
DE            Short=GABA-BR1;
DE            Short=GABABR1;
DE            Short=Gb1;
DE   Flags: Precursor;
GN   Name=Gabbr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
RX   MEDLINE=20237752; PubMed=10773016;
RA   Sullivan R., Chateauneuf A., Coulombe N., Kolakowski L.F. Jr.,
RA   Johnson M.P., Hebert T.E., Ethier N., Belley M., Metters K.,
RA   Abramovitz M., O'Neill G.P., Ng G.Y.K.;
RT   "Coexpression of full-length gamma-aminobutyric acid(B) (GABA(B))
RT   receptors with truncated receptors and metabotropic glutamate receptor
RT   4 supports the GABA(B) heterodimer as the functional receptor.";
RL   J. Pharmacol. Exp. Ther. 293:460-467(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A AND 1B), AND TISSUE
RP   SPECIFICITY.
RX   PubMed=11306808;
RA   Lamp K., Humeny A., Nikolic Z., Imai K., Adamski J., Schiebel K.,
RA   Becker C.M.;
RT   "The murine GABA(B) receptor 1: cDNA cloning, tissue distribution,
RT   structure of the Gabbr1 gene, and mapping to chromosome 17.";
RL   Cytogenet. Cell Genet. 92:116-121(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1A AND 1B).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   INTERACTION WITH GABBR2.
RX   MEDLINE=99102694; PubMed=9872744; DOI=10.1126/science.283.5398.74;
RA   Kuner R., Koehr G., Gruenewald S., Eisenhardt G., Bach A.,
RA   Kornau H.-C.;
RT   "Role of heteromer formation in GABAB receptor function.";
RL   Science 283:74-77(1999).
RN   [6]
RP   INTERACTION WITH JAKMIP1.
RX   PubMed=14718537; DOI=10.1074/jbc.M311737200;
RA   Couve A., Restituito S., Brandon J.M., Charles K.J., Bawagan H.,
RA   Freeman K.B., Pangalos M.N., Calver A.R., Moss S.J.;
RT   "Marlin-1, a novel RNA-binding protein associates with GABA
RT   receptors.";
RL   J. Biol. Chem. 279:13934-13943(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-929, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-929, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Receptor for GABA. The activity of this receptor is
CC       mediated by G-proteins that inhibit adenylyl cyclase activity,
CC       stimulates phospholipase A2, activates potassium channels,
CC       inactivates voltage-dependent calcium-channels and modulates
CC       inositol phospholipids hydrolysis. Plays a critical role in the
CC       fine-tuning of inhibitory synaptic transmission. Pre-synaptic
CC       GABA-B-R inhibit neurotransmitter release by down-regulating high-
CC       voltage activated calcium channels, whereas postsynaptic GABA-B-R
CC       decrease neuronal excitability by activating a prominent inwardly
CC       rectifying potassium (Kir) conductance that underlies the late
CC       inhibitory postsynaptic potentials. Not only implicated in
CC       synaptic inhibition but also in hippocampal long-term
CC       potentiation, slow wave sleep, muscle relaxation and
CC       antinociception.
CC   -!- COFACTOR: Calcium. Required for high affinity binding to GABA (By
CC       similarity).
CC   -!- SUBUNIT: Heterodimer of GABA-B-R1 and GABA-B-R2. Neither of which
CC       is effective on its own and homodimeric assembly does not seem to
CC       happen. Interacts with the leucine zipper of the C-terminal bZIP
CC       domain of ATF4 via its C-terminal region (By similarity).
CC       Interacts with JAKMIP1.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC       (By similarity). Cell junction, synapse, postsynaptic cell
CC       membrane; Multi-pass membrane protein (By similarity).
CC       Note=Moreover coexpression of GABA-B-R1 and GABA-B-R2 appears to
CC       be a prerequisite for maturation and transport of GABA-B-R1 to the
CC       plasma membrane (By similarity). Colocalizes with ATF4 in
CC       hippocampal neuron dendritic membranes (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1A;
CC         IsoId=Q9WV18-1; Sequence=Displayed;
CC       Name=1B;
CC         IsoId=Q9WV18-2; Sequence=VSP_002041;
CC   -!- TISSUE SPECIFICITY: Expressed in neuronal tissue including cortex,
CC       cerebellum and spinal cord. Not detected in non-neuronal tissues
CC       including heart, liver, spleen and kidney.
CC   -!- DOMAIN: Alpha-helical parts of the C-terminal intracellular region
CC       mediate heterodimeric interaction with GABA-B receptor 2. The
CC       linker region between the transmembrane domain 3 (TM3) and the
CC       transmembrane domain 4 (TM4) probably play a role in the
CC       specificity for G-protein coupling.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family.
CC       GABA-B receptor subfamily.
CC   -!- SIMILARITY: Contains 2 Sushi (CCP/SCR) domains.
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DR   EMBL; AF114168; AAD22194.2; -; mRNA.
DR   EMBL; AF008649; AAG29338.1; -; mRNA.
DR   EMBL; AF120255; AAG29341.1; -; mRNA.
DR   EMBL; AL078630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC054735; AAH54735.1; -; mRNA.
DR   EMBL; BC056990; AAH56990.1; -; mRNA.
DR   IPI; IPI00223325; -.
DR   IPI; IPI00755301; -.
DR   RefSeq; NP_062312.3; NM_019439.3.
DR   UniGene; Mm.32191; -.
DR   ProteinModelPortal; Q9WV18; -.
DR   SMR; Q9WV18; 28-159.
DR   STRING; Q9WV18; -.
DR   PhosphoSite; Q9WV18; -.
DR   PRIDE; Q9WV18; -.
DR   Ensembl; ENSMUST00000025338; ENSMUSP00000025338; ENSMUSG00000024462.
DR   Ensembl; ENSMUST00000113650; ENSMUSP00000109280; ENSMUSG00000024462.
DR   GeneID; 54393; -.
DR   KEGG; mmu:54393; -.
DR   UCSC; uc008cma.1; mouse.
DR   UCSC; uc008cmd.1; mouse.
DR   CTD; 54393; -.
DR   MGI; MGI:1860139; Gabbr1.
DR   GeneTree; ENSGT00530000063129; -.
DR   HOGENOM; HBG315351; -.
DR   HOVERGEN; HBG051688; -.
DR   InParanoid; Q9WV18; -.
DR   OMA; KPHCQVN; -.
DR   OrthoDB; EOG4BG8VH; -.
DR   NextBio; 311240; -.
DR   ArrayExpress; Q9WV18; -.
DR   Bgee; Q9WV18; -.
DR   CleanEx; MM_GABBR1; -.
DR   Genevestigator; Q9WV18; -.
DR   GermOnline; ENSMUSG00000024462; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR016060; Complement_control_module.
DR   InterPro; IPR017978; GPCR_3_C.
DR   InterPro; IPR002455; GPCR_3_GABA_rcpt_B.
DR   InterPro; IPR002456; GPCR_3_GABA_rcpt_B1.
DR   InterPro; IPR000436; Sushi_SCR_CCP.
DR   Gene3D; G3DSA:2.10.70.10; Complement_control_module; 2.
DR   Pfam; PF00003; 7tm_3; 1.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00084; Sushi; 2.
DR   PRINTS; PR01177; GABAB1RECPTR.
DR   PRINTS; PR01176; GABABRECEPTR.
DR   SMART; SM00032; CCP; 2.
DR   SUPFAM; SSF57535; Complement_control_module; 2.
DR   PROSITE; PS00979; G_PROTEIN_RECEP_F3_1; FALSE_NEG.
DR   PROSITE; PS00980; G_PROTEIN_RECEP_F3_2; FALSE_NEG.
DR   PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; FALSE_NEG.
DR   PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
DR   PROSITE; PS50923; SUSHI; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Coiled coil;
KW   Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
KW   Phosphoprotein; Postsynaptic cell membrane; Receptor; Repeat; Signal;
KW   Sushi; Synapse; Transducer; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     16       Potential.
FT   CHAIN        17    960       Gamma-aminobutyric acid type B receptor
FT                                subunit 1.
FT                                /FTId=PRO_0000012950.
FT   TOPO_DOM     17    590       Extracellular (Potential).
FT   TRANSMEM    591    611       Helical; Name=1; (Potential).
FT   TOPO_DOM    612    630       Cytoplasmic (Potential).
FT   TRANSMEM    631    651       Helical; Name=2; (Potential).
FT   TOPO_DOM    652    666       Extracellular (Potential).
FT   TRANSMEM    667    687       Helical; Name=3; (Potential).
FT   TOPO_DOM    688    709       Cytoplasmic (Potential).
FT   TRANSMEM    710    730       Helical; Name=4; (Potential).
FT   TOPO_DOM    731    767       Extracellular (Potential).
FT   TRANSMEM    768    788       Helical; Name=5; (Potential).
FT   TOPO_DOM    789    803       Cytoplasmic (Potential).
FT   TRANSMEM    804    824       Helical; Name=6; (Potential).
FT   TOPO_DOM    825    832       Extracellular (Potential).
FT   TRANSMEM    833    853       Helical; Name=7; (Potential).
FT   TOPO_DOM    854    960       Cytoplasmic (Potential).
FT   DOMAIN       29     95       Sushi 1.
FT   DOMAIN       97    158       Sushi 2.
FT   REGION      887    915       Interaction with ATF4 (By similarity).
FT   COILED      868    924       Potential.
FT   MOD_RES     929    929       Phosphothreonine.
FT   CARBOHYD     23     23       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     83     83       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    408    408       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    439    439       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    481    481       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    501    501       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    513    513       N-linked (GlcNAc...) (Potential).
FT   DISULFID     99    144       By similarity.
FT   DISULFID    130    156       By similarity.
FT   VAR_SEQ       1    163       MLLLLLVPLFLRPLGAGGAQTPNVTSEGCQIIHPPWEGGIR
FT                                YRGLTRDQVKAINFLPVDYEIEYVCRGEREVVGPKVRKCLA
FT                                NGSWTDMDTPSRCVRICSKSYLTLENGKVFLTGGDLPALDG
FT                                ARVDFRCDPDFHLVGSSRSICSQGQWSTPKPHCQVNRTPH
FT                                -> MGPGGPCTPVGWPLPLLLVMAAGVAPVWASHSPHLPRP
FT                                HPRVPPHPS (in isoform 1B).
FT                                /FTId=VSP_002041.
FT   CONFLICT      7      8       VP -> LL (in Ref. 1; AAD22194).
FT   CONFLICT     46     46       T -> I (in Ref. 1; AAD22194).
FT   CONFLICT    618    618       V -> A (in Ref. 1; AAD22194).
FT   CONFLICT    642    642       A -> V (in Ref. 1; AAD22194).
FT   CONFLICT    700    700       W -> R (in Ref. 4; AAH56990).
FT   CONFLICT    721    721       I -> V (in Ref. 1; AAD22194).
FT   CONFLICT    812    812       A -> P (in Ref. 2; AAG29338/AAG29341).
FT   CONFLICT    869    869       A -> T (in Ref. 1; AAD22194).
FT   CONFLICT    921    921       I -> L (in Ref. 1; AAD22194).
SQ   SEQUENCE   960 AA;  108216 MW;  E4B5A9401E23E8B4 CRC64;
     MLLLLLVPLF LRPLGAGGAQ TPNVTSEGCQ IIHPPWEGGI RYRGLTRDQV KAINFLPVDY
     EIEYVCRGER EVVGPKVRKC LANGSWTDMD TPSRCVRICS KSYLTLENGK VFLTGGDLPA
     LDGARVDFRC DPDFHLVGSS RSICSQGQWS TPKPHCQVNR TPHSERRAVY IGALFPMSGG
     WPGGQACQPA VEMALEDVNS RRDILPDYEL KLIHHDSKCD PGQATKYLYE LLYNDPIKII
     LMPGCSSVST LVAEAARMWN LIVLSYGSSS PALSNRQRFP TFFRTHPSAT LHNPTRVKLF
     EKWGWKKIAT IQQTTEVFTS TLDDLEERVK EAGIEITFRQ SFFSDPAVPV KNLKRQDARI
     IVGLFYETEA RKVFCEVYKE RLFGKKYVWF LIGWYADNWF KTYDPSINCT VEEMTEAVEG
     HITTEIVMLN PANTRSISNM TSQEFVEKLT KRLKRHPEET GGFQEAPLAY DAIWALALAL
     NKTSGGGGRS GVRLEDFNYN NQTITDQIYR AMNSSSFEGV SGHVVFDASG SRMAWTLIEQ
     LQGGSYKKIG YYDSTKDDLS WSKTDKWIGG SPPADQTLVI KTFRFLSQKL FISVSVLSSL
     GIVLAVVCLS FNIYNSHVRY IQNSQPNLNN LTAVGCSLAL AAVFPLGLDG YHIGRSQFPF
     VCQARLWLLG LGFSLGYGSM FTKIWWVHTV FTKKEEKKEW RKTLEPWKLY ATVGLLVGMD
     ILTLAIWQIV DPLHRTIETF AKEEPKEDID VSILPQLEHC SSKKMNTWLG IFYGYKGLLL
     LLGIFLAYET KSVSTEKIND HRAVGMAIYN VAVLCLITAP VTMILSSQQD AAFAFASLAI
     VFSSYITLVV LFVPKMRRLI TRGEWQSEAQ DTMKTGSSTN NNEEEKSRLL EKENRELEKI
     IAEKEERVSE LRHQLQSRQQ IRSRRHPPTP PDPSGGLPRG PSEPPDRLSC DGSRVHLLYK
//
ID   NFAT5_MOUSE             Reviewed;        1225 AA.
AC   Q9WV30;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Nuclear factor of activated T-cells 5;
DE            Short=NF-AT5;
DE   AltName: Full=Rel domain-containing transcription factor NFAT5;
DE   AltName: Full=T-cell transcription factor NFAT5;
GN   Name=Nfat5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Lu J., Xu H., Olson E.N.;
RT   "Identification of NFAT5, a new rel-like transcription factor.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays a role in the inducible expression of genes.
CC       Regulates hypertonicity-induced cellular accumulation of osmolytes
CC       (By similarity).
CC   -!- SUBUNIT: Does not bind with Fos and Jun transcription factors. But
CC       might be capable of forming stable dimers with DNA elements (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- SIMILARITY: Contains 1 RHD (Rel-like) domain.
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DR   EMBL; AF162853; AAD44343.1; -; mRNA.
DR   IPI; IPI00283318; -.
DR   UniGene; Mm.390057; -.
DR   ProteinModelPortal; Q9WV30; -.
DR   SMR; Q9WV30; 264-544.
DR   STRING; Q9WV30; -.
DR   PhosphoSite; Q9WV30; -.
DR   PRIDE; Q9WV30; -.
DR   Ensembl; ENSMUST00000075922; ENSMUSP00000075311; ENSMUSG00000003847.
DR   UCSC; uc009nhm.1; mouse.
DR   MGI; MGI:1859333; Nfat5.
DR   GeneTree; ENSGT00550000074562; -.
DR   HOVERGEN; HBG052612; -.
DR   OrthoDB; EOG48GW2P; -.
DR   ArrayExpress; Q9WV30; -.
DR   Bgee; Q9WV30; -.
DR   CleanEx; MM_NFAT5; -.
DR   Genevestigator; Q9WV30; -.
DR   GermOnline; ENSMUSG00000003847; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0001816; P:cytokine production; IDA:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR002909; IPT_TIG_rcpt.
DR   InterPro; IPR008366; NFAT.
DR   InterPro; IPR015646; NFAT5.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd.
DR   InterPro; IPR011539; RHD.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1.
DR   Gene3D; G3DSA:2.60.40.340; RHD; 1.
DR   PANTHER; PTHR12533; NFAT; 1.
DR   PANTHER; PTHR12533:SF1; NFAT5; 1.
DR   Pfam; PF00554; RHD; 1.
DR   PRINTS; PR01789; NUCFACTORATC.
DR   SMART; SM00429; IPT; 1.
DR   SUPFAM; SSF81296; Ig_E-set; 1.
DR   SUPFAM; SSF49417; P53_like_DNA_bnd; 1.
DR   PROSITE; PS01204; REL_1; FALSE_NEG.
DR   PROSITE; PS50254; REL_2; 1.
PE   2: Evidence at transcript level;
KW   Activator; DNA-binding; Nucleus; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   1225       Nuclear factor of activated T-cells 5.
FT                                /FTId=PRO_0000205184.
FT   DOMAIN      264    443       RHD.
FT   DNA_BIND    293    300       By similarity.
FT   COMPBIAS     69    100       Ser-rich.
FT   COMPBIAS    647    653       Poly-Ser.
FT   COMPBIAS    738    741       Poly-Gln.
FT   COMPBIAS    876    885       Poly-Gln.
FT   COMPBIAS    963    968       Poly-Thr.
SQ   SEQUENCE   1225 AA;  132192 MW;  6A91537E7949A527 CRC64;
     MPSDFISLLS ADLDLESPKS LYSRESVYDL LPKELQLPPP RETSVASMSQ TSGGEAGSPP
     PAVVAADASS APSSSSMGGA CSSFTTSSSP TIYSTSVTDS KAMQVESCSS AVGVSNRGVS
     EKQLTGNTVQ QHPSTPKRHT VLYISPPPED LLDNSRMSCQ DEGCGLESEQ SCSMWMEDSP
     SNFSNMSTSS YNDNTEVPRK SRKRNPKQRP GVKRRDCEES NMDIFDADSA KAPHYVLSQL
     TTDNKGNSKA GNGTLDSQKG TGVKKSPMLC GQYPVKSEGK ELKIVVQPET QHRARYLTEG
     SRGSVKDRTQ QGFPTVKLEG HNEPVVLQVF VGNDSGRVKP HGFYQACRVT GRNTTPCKEV
     DIEGTTVIEV GLDPSNNMTL AVDCVGILKL RNADVEARIG IAGSKKKSTR ARLVFRVNIT
     RKDGSTLTLQ TPSSPILCTQ PAGVPEILKK SLHSCSVKGE EEVFLIGKNF LKGTKVIFQE
     NVSDENSWKS EAEIDMELFH QNHLIVKVPP YHDQHITLPV SVGIYVVTNA GRSHDVQPFT
     YTPDPAAGAL NVNVKKEISS PARPCSFEEA MKAMKTTGCN VDKVTILPNA LITPLISSSM
     IKTEDVTPME VTSEKRSSPI FQTTKSIGST QQTLETISNI AGGAPFSSPS SSSHLTPESE
     NQQQLQPKAY NPETLTTIQT QDISQPGTFP AVSAASQLPS SDALLQQATQ FQTREAQSRD
     TIQSDTVVNL SQLTEASQQQ QSPLQEQAQT LQQQIPSNIF PSPSSVSQLQ STIQQLQAGS
     FTGSAAGGRS GSVDLVQQVL EAQQQLSSVL FSTPDGNENV QEQLNADIFQ VSQIQNSVSP
     GMFSSAESAV HTRPDNLLPG RADSVHQQTE NTLSNQQQQQ QQQQQVMESS AAMVMEMQQS
     ICQAAAQIQS ELFPSAASAS GSLQQSPVYQ QPSHMMSALP TNEDMQMQCE LFSSPPAASG
     NETSTTTTPQ VATPGSTMFQ TPSSGDGEET GAQAKQIQNS VFQTMVQMQR SGDSQPQVNL
     FSSTKNIMSV QNNGTQQQGN SLFQQGSEMM SLQSGNFLQQ SSHSQAQLFH PQNPIADAQN
     LSQETQGSIF HSPNPIVHSQ TSTASSEQLQ PSMFHSQNTI AVLQGSSVPQ DQQSPNIFLS
     QSSINNLQTN TVAQEEQISF FAAQNSISPL QSTSNTEQQA AFQQQPPISH IQTPILSQEQ
     AQPSQQGLFQ PQESLHSHIT PDACK
//
ID   ARC_MOUSE               Reviewed;         396 AA.
AC   Q9WV31; Q9ES15;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 64.
DE   RecName: Full=Activity-regulated cytoskeleton-associated protein;
DE   AltName: Full=ARC/ARG3.1;
DE            Short=mArc;
DE   AltName: Full=Activity-regulated gene 3.1 protein homolog;
DE            Short=Arg3.1;
GN   Name=Arc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   MEDLINE=21359664; PubMed=11466419;
RA   Waltereit R., Dammermann B., Wulff P., Scafidi J., Staubli U.,
RA   Kauselmann G., Bundman M., Kuhl D.;
RT   "Arg3.1/Arc mRNA induction by Ca2+ and cAMP requires protein kinase A
RT   and mitogen-activated protein kinase/extracellular regulated kinase
RT   activation.";
RL   J. Neurosci. 21:5484-5493(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6; TISSUE=Forebrain;
RA   Chowdhury S., Lanahan A.A., Worley P.F.;
RT   "The mArc gene, a mouse homolog of rat Arc.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-242.
RC   STRAIN=C57BL/6 X CBA;
RA   Medrano S., Worley P.F., Chowdhury S., Lanahan A., Steward O.,
RA   Scrable H.;
RT   "Characterization of the promoter region of the immediate early gene
RT   Arc.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=12493697; DOI=10.1095/biolreprod.102.004143;
RA   Maier B., Medrano S., Sleight S.B., Visconti P.E., Scrable H.;
RT   "Developmental association of the synaptic activity-regulated protein
RT   arc with the mouse acrosomal organelle and the sperm tail.";
RL   Biol. Reprod. 68:67-76(2003).
RN   [7]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17088210; DOI=10.1016/j.neuron.2006.08.024;
RA   Plath N., Ohana O., Dammermann B., Errington M.L., Schmitz D.,
RA   Gross C., Mao X., Engelsberg A., Mahlke C., Welzl H., Kobalz U.,
RA   Stawrakakis A., Fernandez E., Waltereit R., Bick-Sander A.,
RA   Therstappen E., Cooke S.F., Blanquet V., Wurst W., Salmen B.,
RA   Bosl M.R., Lipp H.P., Grant S.G., Bliss T.V., Wolfer D.P., Kuhl D.;
RT   "Arc/Arg3.1 is essential for the consolidation of synaptic plasticity
RT   and memories.";
RL   Neuron 52:437-444(2006).
RN   [8]
RP   FUNCTION.
RX   PubMed=17088213; DOI=10.1016/j.neuron.2006.08.034;
RA   Shepherd J.D., Rumbaugh G., Wu J., Chowdhury S., Plath N., Kuhl D.,
RA   Huganir R.L., Worley P.F.;
RT   "Arc/Arg3.1 mediates homeostatic synaptic scaling of AMPA Receptors.";
RL   Neuron 52:475-484(2006).
CC   -!- FUNCTION: Required for consolidation of synaptic plasticity as
CC       well as formation of long-term memory. Regulates endocytosis of
CC       AMPA receptors in response to synaptic activity. Required for
CC       homeostatic synaptic scaling of AMPA receptors.
CC   -!- SUBUNIT: Interacts with SH3GL1/endophilin-2, SH3GL3/endophilin-3
CC       and DNM2/DYN2 (By similarity).
CC   -!- INTERACTION:
CC       Q62108:Dlg4; NbExp=1; IntAct=EBI-397779, EBI-300895;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC       Endosome (By similarity). Cytoplasmic vesicle, secretory vesicle,
CC       acrosome. Cell junction, synapse, postsynaptic cell membrane,
CC       postsynaptic density (By similarity). Cell projection, dendrite
CC       (By similarity). Cell projection, dendritic spine (By similarity).
CC       Cell junction, synapse (By similarity). Note=Associated with the
CC       cell cortex of neuronal soma and dendrites. Enriched in
CC       postsynaptic density of dendritic spines (By similarity).
CC       Associated with the sperm tail.
CC   -!- TISSUE SPECIFICITY: Expressed in brain and testis.
CC   -!- DEVELOPMENTAL STAGE: Detectable in brain from postnatal week 1, in
CC       testis from postnatal week 3.
CC   -!- DISRUPTION PHENOTYPE: Mice show deficits in several forms of long-
CC       term memory formation including spatial and fear-related learning,
CC       conditioned taste aversion as well as long-term object
CC       recognition. They show enhanced early-phase but impaired late-
CC       phase long-term potentiation (LTP) as well as impaired long-term
CC       depression (LTD). Neurons lacking Arc show an increase in surface
CC       levels of AMPA receptors.
CC   -!- MISCELLANEOUS: Widely used as activity-dependent neuronal marker
CC       to identify recently activated neurons in behavioral studies.
CC   -!- SIMILARITY: Belongs to the ARC/ARG3.1 family.
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DR   EMBL; AF177701; AAK91587.1; -; Genomic_DNA.
DR   EMBL; AF162777; AAD43586.1; -; mRNA.
DR   EMBL; AK157822; BAE34212.1; -; mRNA.
DR   EMBL; AK170446; BAE41804.1; -; mRNA.
DR   EMBL; BC023127; AAH23127.1; -; mRNA.
DR   EMBL; AF254662; AAG10254.1; -; Genomic_DNA.
DR   IPI; IPI00125140; -.
DR   RefSeq; NP_061260.1; NM_018790.2.
DR   UniGene; Mm.25405; -.
DR   ProteinModelPortal; Q9WV31; -.
DR   IntAct; Q9WV31; 8.
DR   STRING; Q9WV31; -.
DR   PRIDE; Q9WV31; -.
DR   Ensembl; ENSMUST00000023268; ENSMUSP00000023268; ENSMUSG00000022602.
DR   Ensembl; ENSMUST00000110009; ENSMUSP00000105636; ENSMUSG00000022602.
DR   GeneID; 11838; -.
DR   KEGG; mmu:11838; -.
DR   UCSC; uc007wfn.1; mouse.
DR   CTD; 11838; -.
DR   MGI; MGI:88067; Arc.
DR   eggNOG; maNOG11459; -.
DR   GeneTree; ENSGT00390000003914; -.
DR   HOGENOM; HBG269748; -.
DR   HOVERGEN; HBG080862; -.
DR   InParanoid; Q9WV31; -.
DR   OMA; RCQETIA; -.
DR   OrthoDB; EOG49S66B; -.
DR   PhylomeDB; Q9WV31; -.
DR   NextBio; 279775; -.
DR   ArrayExpress; Q9WV31; -.
DR   Bgee; Q9WV31; -.
DR   Genevestigator; Q9WV31; -.
DR   GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003779; F:actin binding; TAS:MGI.
DR   GO; GO:0009952; P:anterior/posterior pattern formation; IMP:MGI.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0007492; P:endoderm development; IMP:MGI.
DR   InterPro; IPR023263; Activity-reg_cytoskelet-assoc.
DR   PRINTS; PR02027; ARCARG31.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW   Cytoplasmic vesicle; Cytoskeleton; Developmental protein; Endocytosis;
KW   Endosome; Membrane; Postsynaptic cell membrane; Synapse.
FT   CHAIN         1    396       Activity-regulated cytoskeleton-
FT                                associated protein.
FT                                /FTId=PRO_0000273286.
FT   REGION       89    100       Binds SH3GL1 or SH3GL3 (By similarity).
FT   REGION      195    214       Required for binding DNM2 (By
FT                                similarity).
FT   COILED       54     78       Potential.
SQ   SEQUENCE   396 AA;  45321 MW;  F4D3505FD477D18A CRC64;
     MELDHMTTGG LHAYPAPRGG PAAKPNVILQ IGKCRAEMLE HVRRTHRHLL TEVSKQVERE
     LKGLHRSVGK LENNLDGYVP TGDSQRWKKS IKACLCRCQE TIANLERWVK REMHVWREVF
     YRLERWADRL ESMGGKYPVG SEPARHTVSV GVGGPEPYCQ EADGYDYTVS PYAITPPPAA
     GELPEQESVE AQQYQSWGPG EDGQPSPGVD TQIFEDPREF LSHLEEYLRQ VGGSEEYWLS
     QIQNHMNGPA KKWWEFKQGS VKNWVEFKKE FLQYSEGTLS REAIQRELEL PQKQGEPLDQ
     FLWRKRDLYQ TLYVDAEEEE IIQYVVGTLQ PKLKRFLRHP LPKTLEQLIQ RGMEVQDGLE
     QAAEPSGTPL PTEDETEALT PALTSESVAS DRTQPE
//
ID   MPP2_MOUSE              Reviewed;         552 AA.
AC   Q9WV34; B1AQF8; Q3T9W1; Q3TT52; Q3URK8;
DT   10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=MAGUK p55 subfamily member 2;
DE   AltName: Full=Discs large homolog 2;
DE   AltName: Full=Protein MPP2;
GN   Name=Mpp2; Synonyms=Dlgh2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Lin L., Chishti A.H.;
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Pituitary, Spinal cord, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 38-46 AND 378-387, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9WV34-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9WV34-2; Sequence=VSP_022952;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the MAGUK family.
CC   -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC   -!- SIMILARITY: Contains 2 L27 domains.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; AF162685; AAD44342.1; -; mRNA.
DR   EMBL; AK141422; BAE24680.1; -; mRNA.
DR   EMBL; AK161577; BAE36473.1; -; mRNA.
DR   EMBL; AK172253; BAE42909.1; -; mRNA.
DR   EMBL; AL591145; CAM23252.1; -; Genomic_DNA.
DR   EMBL; BC053026; AAH53026.1; -; mRNA.
DR   IPI; IPI00125147; -.
DR   IPI; IPI00756238; -.
DR   RefSeq; NP_057904.1; NM_016695.3.
DR   UniGene; Mm.36242; -.
DR   ProteinModelPortal; Q9WV34; -.
DR   SMR; Q9WV34; 5-118, 139-216, 228-549.
DR   PhosphoSite; Q9WV34; -.
DR   PRIDE; Q9WV34; -.
DR   Ensembl; ENSMUST00000017458; ENSMUSP00000017458; ENSMUSG00000017314.
DR   Ensembl; ENSMUST00000100398; ENSMUSP00000097967; ENSMUSG00000017314.
DR   GeneID; 50997; -.
DR   KEGG; mmu:50997; -.
DR   UCSC; uc007lql.1; mouse.
DR   CTD; 50997; -.
DR   MGI; MGI:1858257; Mpp2.
DR   eggNOG; roNOG11339; -.
DR   GeneTree; ENSGT00560000077048; -.
DR   HOVERGEN; HBG001858; -.
DR   OMA; NSETAMQ; -.
DR   OrthoDB; EOG4T1HM6; -.
DR   PhylomeDB; Q9WV34; -.
DR   NextBio; 308004; -.
DR   ArrayExpress; Q9WV34; -.
DR   Bgee; Q9WV34; -.
DR   Genevestigator; Q9WV34; -.
DR   GermOnline; ENSMUSG00000017314; Mus musculus.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR004172; L27.
DR   InterPro; IPR014775; L27_C.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF02828; L27; 2.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00569; L27; 2.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS51022; L27; 2.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing; Phosphoprotein;
KW   Repeat; SH3 domain.
FT   CHAIN         1    552       MAGUK p55 subfamily member 2.
FT                                /FTId=PRO_0000094574.
FT   DOMAIN        8     59       L27 1.
FT   DOMAIN       60    118       L27 2.
FT   DOMAIN      140    219       PDZ.
FT   DOMAIN      225    293       SH3.
FT   DOMAIN      350    537       Guanylate kinase-like.
FT   MOD_RES      42     42       Phosphoserine.
FT   MOD_RES     114    114       Phosphothreonine (By similarity).
FT   MOD_RES     115    115       Phosphotyrosine (By similarity).
FT   MOD_RES     117    117       Phosphothreonine (By similarity).
FT   MOD_RES     121    121       Phosphoserine (By similarity).
FT   MOD_RES     127    127       Phosphothreonine (By similarity).
FT   VAR_SEQ       1     10       MPVAATNSES -> MACSPGSEGSLEGISLGSSEEAELRRE
FT                                (in isoform 2).
FT                                /FTId=VSP_022952.
FT   CONFLICT    215    215       I -> T (in Ref. 2; BAE42909).
SQ   SEQUENCE   552 AA;  61555 MW;  E932CD208309E0FA CRC64;
     MPVAATNSES AMQQVLDNLG SLPNATGAAE LDLIFLRGIM ESPIVRSLAK AHERLEETKL
     EAVRDNNLEL VQEILRDLAE LAEQSSTAAE LARILQEPHF QSLLETHDSV ASKTYETPPP
     SPGLDPTFSN QPVPPDAVRM VGIRKTAGEH LGVTFRVEGG ELVIARILHG GMVAQQGLLH
     VGDIIKEVNG QPVGSDPRAL QELLRSASGS VILKILPSYQ EPHLPRQVFV KCHFDYDPAR
     DSLSPCKEAG LRFNAGDLLQ IVNQDDANWW QACHVEGGSA GLIPSQLLEE KRKAFVKRDL
     ELTPTSGTLC GSLSGKKKKR MMYLTTKNAE FDRHELLIYE EVARMPPFRR KTLVLIGAQG
     VGRRSLKNKL ILWDPDRYGT TVPYTSRRPK DSEREGQGYS FVSRGEMEAD IRAGRYLEHG
     EYEGNLYGTR IDSIRGVVAS GKVCVLDVNP QAVKVLRTAE FVPYVVFIEA PDYETLRAMN
     RAALESGVST KQLTEADLRR TVEESSRIQR GYGHYFDLSL VNSNLERTFR ELQTAMEKLR
     TEPQWVPVSW VY
//
ID   SHAN1_RAT               Reviewed;        2167 AA.
AC   Q9WV48; Q9QZZ8; Q9WU13; Q9WUE8;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 109.
DE   RecName: Full=SH3 and multiple ankyrin repeat domains protein 1;
DE            Short=Shank1;
DE   AltName: Full=GKAP/SAPAP-interacting protein;
DE   AltName: Full=SPANK-1;
DE   AltName: Full=Somatostatin receptor-interacting protein;
DE            Short=SSTR-interacting protein;
DE            Short=SSTRIP;
DE   AltName: Full=Synamon;
GN   Name=Shank1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND INTERACTION WITH
RP   DLGAP1 AND DLG4.
RC   TISSUE=Brain;
RX   MEDLINE=99419021; PubMed=10488079; DOI=10.1074/jbc.274.39.27463;
RA   Yao I., Hata Y., Hirao K., Deguchi M., Ide N., Takeuchi M., Takai Y.;
RT   "Synamon, a novel neuronal protein interacting with synapse-associated
RT   protein 90/postsynaptic density-95-associated protein.";
RL   J. Biol. Chem. 274:27463-27466(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND INTERACTION WITH DLGAP1.
RC   STRAIN=Sprague-Dawley;
RX   MEDLINE=99360650; PubMed=10433268; DOI=10.1016/S0896-6273(00)80809-0;
RA   Naisbitt S., Kim E., Tu J.C., Xiao B., Sala C., Valtschanoff J.,
RA   Weinberg R.J., Worley P.F., Sheng M.;
RT   "Shank, a novel family of postsynaptic density proteins that binds to
RT   the NMDA receptor/PSD-95/GKAP complex and cortactin.";
RL   Neuron 23:569-582(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=20549637; PubMed=10958799; DOI=10.1074/jbc.M006448200;
RA   Tobaben S., Suedhof T.C., Stahl B.;
RT   "The G protein-coupled receptor CL1 interacts directly with proteins
RT   of the Shank family.";
RL   J. Biol. Chem. 275:36204-36210(2000).
RN   [4]
RP   PARTIAL NUCLEOTIDE SEQUENCE (ISOFORMS 1; 2; 3; 4 AND 5), AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Brain;
RX   MEDLINE=99436166; PubMed=10506216; DOI=10.1074/jbc.274.41.29510;
RA   Lim S., Naisbitt S., Yoon J., Hwang J.-I., Suh P.-G., Sheng M.,
RA   Kim E.;
RT   "Characterization of the shank family of synaptic proteins. Multiple
RT   genes, alternative splicing, and differential expression in brain and
RT   development.";
RL   J. Biol. Chem. 274:29510-29518(1999).
RN   [5]
RP   PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM 4).
RC   TISSUE=Brain;
RX   MEDLINE=20020275; PubMed=10551867; DOI=10.1074/jbc.274.46.32997;
RA   Zitzer H., Hoenck H.-H., Baechner D., Richter D., Kreienkamp H.-J.;
RT   "Somatostatin receptor interacting protein defines a novel family of
RT   multidomain proteins present in human and rodent brain.";
RL   J. Biol. Chem. 274:32997-33001(1999).
RN   [6]
RP   INTERACTION WITH HOMER1, AND SUBCELLULAR LOCATION.
RX   MEDLINE=99360651; PubMed=10433269; DOI=10.1016/S0896-6273(00)80810-7;
RA   Tu J.C., Xiao B., Naisbitt S., Yuan J.P., Petralia R.S., Brakeman P.,
RA   Doan A., Aakalu V.K., Lanahan A.A., Sheng M., Worley P.F.;
RT   "Coupling of mGluR/Homer and PSD-95 complexes by the Shank family of
RT   postsynaptic density proteins.";
RL   Neuron 23:583-592(1999).
RN   [7]
RP   INTERACTION WITH SPTAN1.
RX   MEDLINE=21523912; PubMed=11509555; DOI=10.1074/jbc.M102454200;
RA   Bockers T.M., Mameza M.G., Kreutz M.R., Bockmann J., Weise C.,
RA   Buck F., Richter D., Gundelfinger E.D., Kreienkamp H.-J.;
RT   "Synaptic scaffolding proteins in rat brain. Ankyrin repeats of the
RT   multidomain Shank protein family interact with the cytoskeletal
RT   protein alpha-fodrin.";
RL   J. Biol. Chem. 276:40104-40112(2001).
RN   [8]
RP   INTERACTION WITH SHARPIN.
RX   MEDLINE=21109393; PubMed=11178875; DOI=10.1006/mcne.2000.0940;
RA   Lim S., Sala C., Yoon J., Park S., Kuroda S., Sheng M., Kim E.;
RT   "Sharpin, a novel postsynaptic density protein that directly interacts
RT   with the shank family of proteins.";
RL   Mol. Cell. Neurosci. 17:385-397(2001).
RN   [9]
RP   FUNCTION.
RX   MEDLINE=21389514; PubMed=11498055; DOI=10.1016/S0896-6273(01)00339-7;
RA   Sala C., Piech V., Wilson N.R., Passafaro M., Liu G., Sheng M.;
RT   "Regulation of dendritic spine morphology and synaptic function by
RT   Shank and Homer.";
RL   Neuron 31:115-130(2001).
RN   [10]
RP   REVIEW.
RX   MEDLINE=20267867; PubMed=10806096;
RA   Sheng M., Kim E.;
RT   "The Shank family of scaffold proteins.";
RL   J. Cell Sci. 113:1851-1856(2000).
RN   [11]
RP   INTERACTION WITH IGSF9.
RX   PubMed=15340156; DOI=10.1073/pnas.0405371101;
RA   Shi S.-H., Cheng T., Jan L.Y., Jan Y.-N.;
RT   "The immunoglobulin family member dendrite arborization and synapse
RT   maturation 1 (Dasm1) controls excitatory synapse maturation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13346-13351(2004).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 654-762 IN COMPLEX WITH
RP   DLGAP1, AND SUBUNIT.
RX   PubMed=12954649; DOI=10.1074/jbc.M306919200;
RA   Im Y.J., Lee J.H., Park S.H., Park S.J., Rho S.-H., Kang G.B., Kim E.,
RA   Eom S.H.;
RT   "Crystal structure of the Shank PDZ-ligand complex reveals a class I
RT   PDZ interaction and a novel PDZ-PDZ dimerization.";
RL   J. Biol. Chem. 278:48099-48104(2003).
CC   -!- FUNCTION: Seems to be an adapter protein in the postsynaptic
CC       density (PSD) of excitatory synapses that interconnects receptors
CC       of the postsynaptic membrane including NMDA-type and metabotropic
CC       glutamate receptors, and the actin-based cytoskeleton. May play a
CC       role in the structural and functional organization of the
CC       dendritic spine and synaptic junction. Overexpression promotes
CC       maturation of dendritic spines and the enlargement of spine heads
CC       via its ability to recruit Homer to postsynaptic sites, and
CC       enhances presynaptic function.
CC   -!- SUBUNIT: May homomultimerize via its SAM domain. Interacts with
CC       the C-terminus of SSTR2 via the PDZ domain. Interacts with
CC       SHARPIN, SPTAN1, HOMER1 and DLGAP1/GKAP. Part of a complex with
CC       DLG4/PSD-95 and DLGAP1/GKAP. Interacts with BAIAP2 (By
CC       similarity). Interacts with IGSF9.
CC   -!- INTERACTION:
CC       P31016:Dlg4; NbExp=1; IntAct=EBI-80909, EBI-375655;
CC       P97836:Dlgap1; NbExp=3; IntAct=EBI-80909, EBI-80901;
CC       P97879:Grip1; NbExp=1; IntAct=EBI-80909, EBI-936113;
CC       Q9Z214-2:Homer1; NbExp=2; IntAct=EBI-80909, EBI-2338999;
CC       Q9NSC5-1:HOMER3 (xeno); NbExp=1; IntAct=EBI-80909, EBI-748433;
CC       Q9EQL9:Sharpin; NbExp=4; IntAct=EBI-80909, EBI-1394695;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell junction, synapse. Cell
CC       junction, synapse, postsynaptic cell membrane, postsynaptic
CC       density. Note=Postsynaptic density of neuronal cells. Colocalizes
CC       with alpha-latrotoxin receptor 1.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1;
CC         IsoId=Q9WV48-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9WV48-2; Sequence=VSP_006072, VSP_006073;
CC       Name=3;
CC         IsoId=Q9WV48-3; Sequence=VSP_006074;
CC       Name=4; Synonyms=A;
CC         IsoId=Q9WV48-4; Sequence=VSP_006075;
CC       Name=5;
CC         IsoId=Q9WV48-5; Sequence=VSP_006076, VSP_006077;
CC   -!- TISSUE SPECIFICITY: Expressed only in brain (neuropil of cortex,
CC       CA1 region hippocampus and molecular layer of cerebellum).
CC   -!- DEVELOPMENTAL STAGE: Expression increases from low levels at birth
CC       to high levels at 3-4 weeks before dropping slightly in adulthood.
CC       Expressed in the cortex and the molecular layer of the cerebellum
CC       at postnatal day 7. Isoform 2 expression does not change during
CC       development of both cortex and cerebellum. Isoform 4 expression
CC       decreases significantly during development of cortex but not
CC       cerebellum.
CC   -!- SIMILARITY: Belongs to the SHANK family.
CC   -!- SIMILARITY: Contains 7 ANK repeats.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 SAM (sterile alpha motif) domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD29417.1; Type=Erroneous initiation;
CC       Sequence=AAF02498.1; Type=Erroneous initiation;
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DR   EMBL; AF102855; AAD04569.2; -; mRNA.
DR   EMBL; AF131951; AAD29417.1; ALT_INIT; mRNA.
DR   EMBL; AF159046; AAD42975.1; -; mRNA.
DR   EMBL; AF141904; AAF02498.1; ALT_INIT; mRNA.
DR   IPI; IPI00204379; -.
DR   IPI; IPI00231655; -.
DR   IPI; IPI00231656; -.
DR   IPI; IPI00231657; -.
DR   IPI; IPI00231658; -.
DR   RefSeq; NP_113939.2; NM_031751.2.
DR   UniGene; Rn.225968; -.
DR   PDB; 1Q3O; X-ray; 1.80 A; A/B=654-762.
DR   PDB; 1Q3P; X-ray; 2.25 A; A/B=654-762.
DR   PDB; 3L4F; X-ray; 2.80 A; D=653-765.
DR   PDBsum; 1Q3O; -.
DR   PDBsum; 1Q3P; -.
DR   PDBsum; 3L4F; -.
DR   ProteinModelPortal; Q9WV48; -.
DR   SMR; Q9WV48; 192-401, 559-624, 656-759, 2076-2165.
DR   IntAct; Q9WV48; 21.
DR   MINT; MINT-101286; -.
DR   STRING; Q9WV48; -.
DR   PhosphoSite; Q9WV48; -.
DR   Ensembl; ENSRNOT00000026100; ENSRNOP00000026100; ENSRNOG00000019207.
DR   GeneID; 78957; -.
DR   KEGG; rno:78957; -.
DR   UCSC; AF131951; rat.
DR   CTD; 78957; -.
DR   RGD; 621011; Shank1.
DR   eggNOG; maNOG18011; -.
DR   GeneTree; ENSGT00510000046474; -.
DR   HOVERGEN; HBG079186; -.
DR   InParanoid; Q9WV48; -.
DR   OrthoDB; EOG48PMJ9; -.
DR   NextBio; 614372; -.
DR   ArrayExpress; Q9WV48; -.
DR   Genevestigator; Q9WV48; -.
DR   GermOnline; ENSRNOG00000019207; Rattus norvegicus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; NAS:UniProtKB.
DR   GO; GO:0005624; C:membrane fraction; IDA:UniProtKB.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
DR   GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
DR   GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR   GO; GO:0030159; F:receptor signaling complex scaffold activity; IDA:RGD.
DR   GO; GO:0031877; F:somatostatin receptor binding; IPI:UniProtKB.
DR   GO; GO:0007016; P:cytoskeletal anchoring at plasma membrane; NAS:UniProtKB.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM_type.
DR   InterPro; IPR021129; SAM_type1.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR010993; Sterile_alpha_motif_homology.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Gene3D; G3DSA:1.10.150.50; SAM_type; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48403; ANK; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF47769; SAM_homology; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ANK repeat; Cell junction;
KW   Cell membrane; Cytoplasm; Membrane; Phosphoprotein;
KW   Postsynaptic cell membrane; Repeat; SH3 domain; Synapse.
FT   CHAIN         1   2167       SH3 and multiple ankyrin repeat domains
FT                                protein 1.
FT                                /FTId=PRO_0000174672.
FT   REPEAT      195    210       ANK 1.
FT   REPEAT      212    245       ANK 2.
FT   REPEAT      246    278       ANK 3.
FT   REPEAT      279    312       ANK 4.
FT   REPEAT      313    345       ANK 5.
FT   REPEAT      346    378       ANK 6.
FT   REPEAT      379    395       ANK 7.
FT   DOMAIN      554    613       SH3.
FT   DOMAIN      663    757       PDZ.
FT   DOMAIN     2104   2167       SAM.
FT   COMPBIAS    929    932       Poly-Pro.
FT   COMPBIAS   1010   1015       Poly-His.
FT   COMPBIAS   1022   1027       Poly-His.
FT   COMPBIAS   1194   1199       Poly-Gly.
FT   COMPBIAS   1850   1860       Poly-Pro.
FT   MOD_RES     275    275       Phosphotyrosine (By similarity).
FT   VAR_SEQ       1    614       Missing (in isoform 2).
FT                                /FTId=VSP_006072.
FT   VAR_SEQ     615    654       SQEGRQESRSDKAKRLFRHYTVGSYDSFDAPSLIDGIDSG
FT                                -> MALSAVGGGPGGGALPQPPPALSSSWPALGPRRRSVWY
FT                                IY (in isoform 2).
FT                                /FTId=VSP_006073.
FT   VAR_SEQ     646    654       Missing (in isoform 3).
FT                                /FTId=VSP_006074.
FT   VAR_SEQ     797    804       Missing (in isoform 4).
FT                                /FTId=VSP_006075.
FT   VAR_SEQ    1930   1943       LSEDSQTSLLSKPS -> QYRIVVKSSDFGDF (in
FT                                isoform 5).
FT                                /FTId=VSP_006076.
FT   VAR_SEQ    1944   2167       Missing (in isoform 5).
FT                                /FTId=VSP_006077.
FT   CONFLICT   1141   1141       S -> T (in Ref. 1; AAD04569).
FT   CONFLICT   1174   1174       S -> N (in Ref. 2; AAD29417).
FT   CONFLICT   1246   1246       R -> K (in Ref. 1; AAD04569).
FT   CONFLICT   1323   1323       A -> T (in Ref. 1; AAD04569).
FT   CONFLICT   1331   1331       S -> D (in Ref. 1; AAD04569).
FT   CONFLICT   1726   1726       S -> N (in Ref. 2; AAD29417).
FT   STRAND      657    667
FT   STRAND      675    682
FT   STRAND      698    705
FT   HELIX       710    713
FT   STRAND      721    725
FT   HELIX       735    744
FT   TURN        745    747
FT   STRAND      748    757
SQ   SEQUENCE   2167 AA;  226335 MW;  3F478B5A7B18BA86 CRC64;
     MTHSPATSED EERHSASECP EGGSESDSSP DGPGRGPQGT RGRGSGAPGN LASTRGLQGR
     SMSVPDDAHF SMMVFRIGIP DLHQTKCLRF NPDATIWTAK QQVLCALSES LQDVLNYGLF
     QPATSGRDAN FLEEERLLRE YPQSFEKGVP YLEFRYKTRV YKQTNLDEKQ LAKLHTKTGL
     KKFLEYVQLG TSDKVARLLD KGLDPNYHDS DSGETPLTLA AQTEGSVEVI RTLCLGGAHI
     DFRARDGMTA LHKAACARHC LALTALLDLG GSPNYKDRRG LTPLFHTAMV GGDPRCCELL
     LYNRAQLGIA DENGWQEIHQ ACQRGHSQHL EHLLFYGAEP GAQNASGNTA LHICALYNKE
     TCARILLYRG ANKDVKNNNG QTPFQVAVIA GNFELGELIR NHREQDVVPF QESPKYAARR
     RGPPGAGLTV PPALLRANSD TSMALPDWMV FSAPGASSSG TPGPTSGPQG QSQPSAPSTK
     LSSGTLRSAS SPRGARARSP SRGRHPEDAK RQPRGRPSSS GTPRDGPAGG TGGSGGPGGS
     LGSRGRRRKL YSAVPGRSFM AVKSYQAQGE GEISLSKGEK IKVLSIGEGG FWEGQVKGRV
     GWFPSDCLEE VANRSQEGRQ ESRSDKAKRL FRHYTVGSYD SFDAPSLIDG IDSGSDYIIK
     EKTVLLQKKD SEGFGFVLRG AKAQTPIEEF TPTPAFPALQ YLESVDEGGV AWRAGLRMGD
     FLIEVNGQNV VKVGHRQVVN MIRQGGNTLM VKVVMVTRHP DMDEAVHKKA SQQAKRLPPP
     AISLRSKSMT SELEEMVSPW KKKIEYEQQP AAVPSMEKKR TVYQMALNKL DEILAAAQQT
     ISASESPGPG GLASLGKHRP KGFFATESSF DPHHRSQPSY DRPSFLPPGP GLMLRQKSIG
     AAEDDRPYLA PPAMKFSRSL SVPGSEDIPP PPTTSPPEPP YSTPPAPSSS GRLTPSPRGG
     PFNPSSGGPL PASSPSSFDG PSPPDTRGGG REKSLYHSAA LPPAHHHPPH HHHHHAPPPQ
     PHHHHAHPPH PPEMETGGSP DDPPPRLALG PQPSLRGWRG GGPSPTSGAP SPSHHSSSGG
     SSGPTQAPAL RYFQLPPRAA SAAMYVPARS GRGRKGPLVK QTKVEGEPQK GSIPSASSPT
     SPALPRSEPP PAGPSEKNSI PIPTIIIKAP STSSSGRSSQ GSSTEAEPPT QPDGAGGGGS
     SPSPAPATSP VPPSPSPVPT PASPSGPATL DFTSQFGAAL VGAARREGGW QNEARRRSTL
     FLSTDAGDED GGDSGLGPGG PPGPRLRHSK SIDEGMFSAE PYLRLESGGS SGGYGAYAAG
     SRAYGGSGSS SAFTSFLPPR PLVHPLTGKA LDPASPLGLA LAARERALKE SSEGGGTPQP
     PPRPPSPRYD APPPTLHHHS PHSPHSPHAR HEPVLRLWGD PARRELGYRA GLGSQEKALT
     ASPPAARRSL LHRLPPTAPG VGPLLLQLGP EPPTPHPGVS KAWRTAAPEE PERLPLHVRF
     LENCQARPPP AGTRGSSTED GPGVPPPSPR RVLPTSPTSP RGNEENGLPL LVLPPPAPSV
     DVDDGEFLFA EPLPPPLEFS NSFEKPESPL TPGPPHPLPD PPSPATPLPA APPPAVAAAP
     PTLDSTASSL TSYDSEVATL TQGAPAAPGD PPAPGPPAPA APAPPAPQPG PDPPPGTDSG
     IEEVDSRSSS DHPLETISSA STLSSLSAEG GGNTGGVAGG GAGVASGTEL LDTYVAYLDG
     QAFGGSGTPG PPYPPQLMTP SKLRGRALGT SGNLRPGPSG GLRDPVTPTS PTVSVTGAGT
     DGLLALSACP GPSTAGVAGG PVAVEPEVPP VPLPAASSLP RKLLPWEEGP GPPPPPLPGP
     LSQPQASALA TVKASIISEL SSKLQQFGGS STAGGALPWA RGGSGGSTDS HHGGASYIPE
     RTSSLQRQRL SEDSQTSLLS KPSSSIFQNW PKPPLPPLPT GSGVSSSTAA APGATSPSAS
     SASASTRHLQ GVEFEMRPPL LRRAPSPSLL PASDHKVSPA PRPSSLPILP SGPIYPGLFD
     IRSSPTGGAG GSTDPFAPVF VPPHPGISGG LGGALSGASR SLSPTRLLSL PPDKPFGAKP
     LGFWTKFDVA DWLEWLGLSE HRAQFLDHEI DGSHLPALTK EDYVDLGVTR VGHRMNIDRA
     LKFFLER
//
ID   VAPA_MOUSE              Reviewed;         249 AA.
AC   Q9WV55; Q3TJM1; Q9QY77;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 2.
DT   08-MAR-2011, entry version 94.
DE   RecName: Full=Vesicle-associated membrane protein-associated protein A;
DE            Short=VAMP-A;
DE            Short=VAMP-associated protein A;
DE            Short=VAP-A;
DE   AltName: Full=33 kDa VAMP-associated protein;
DE            Short=VAP-33;
GN   Name=Vapa; Synonyms=Vap33;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=20122578; PubMed=10655491; DOI=10.1073/pnas.97.3.1101;
RA   Skehel P.A., Fabian-Fine R., Kandel E.R.;
RT   "Mouse VAP33 is associated with the endoplasmic reticulum and
RT   microtubules.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:1101-1106(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Fetal liver, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-242.
RA   Tang B.L., Low D.L.H., Lock M.L., Hong W.;
RT   "Two forms of mammalian VAP33.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PROTEIN SEQUENCE OF 199-214, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   STRUCTURE BY NMR OF 8-141.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the MSP domain of mouse VAMP-associated protein
RT   A.";
RL   Submitted (NOV-2005) to the PDB data bank.
CC   -!- FUNCTION: May play a role in vesicle trafficking.
CC   -!- SUBUNIT: Homodimer, and heterodimer with VAPB. Interacts with
CC       VAMP1, VAMP2, STX1A, BET1, SEC22C and with the C-terminal domain
CC       of OCLN. Interacts with OSBPL1A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type IV membrane
CC       protein (By similarity). Endomembrane system; Single-pass type IV
CC       membrane protein (By similarity). Note=Present in the plasma
CC       membrane and in intracellular vesicles, together with SNARE
CC       proteins. May also associate with the cytoskeleton. Colocalizes
CC       with OCLN at the tight junction in polarized epithelial cells (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the VAMP-associated protein (VAP)
CC       (TC 9.B.17) family.
CC   -!- SIMILARITY: Contains 1 MSP domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD45320.1; Type=Erroneous initiation;
CC       Sequence=BAB22868.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF157497; AAD45320.1; ALT_INIT; mRNA.
DR   EMBL; AK003576; BAB22868.1; ALT_INIT; mRNA.
DR   EMBL; AK167381; BAE39474.1; -; mRNA.
DR   EMBL; AK168824; BAE40651.1; -; mRNA.
DR   EMBL; AK159582; BAE35202.1; -; mRNA.
DR   EMBL; BC003866; AAH03866.2; -; mRNA.
DR   EMBL; AF115503; AAF23076.1; -; mRNA.
DR   IPI; IPI00125267; -.
DR   RefSeq; NP_038961.2; NM_013933.3.
DR   UniGene; Mm.266767; -.
DR   PDB; 2CRI; NMR; -; A=8-134.
DR   PDBsum; 2CRI; -.
DR   ProteinModelPortal; Q9WV55; -.
DR   SMR; Q9WV55; 8-132.
DR   IntAct; Q9WV55; 4.
DR   STRING; Q9WV55; -.
DR   PhosphoSite; Q9WV55; -.
DR   PRIDE; Q9WV55; -.
DR   Ensembl; ENSMUST00000024897; ENSMUSP00000024897; ENSMUSG00000024091.
DR   GeneID; 30960; -.
DR   KEGG; mmu:30960; -.
DR   UCSC; uc008dgd.1; mouse.
DR   CTD; 30960; -.
DR   MGI; MGI:1353561; Vapa.
DR   eggNOG; roNOG12222; -.
DR   GeneTree; ENSGT00390000006947; -.
DR   HOGENOM; HBG446464; -.
DR   HOVERGEN; HBG028551; -.
DR   InParanoid; Q9WV55; -.
DR   OMA; ENDKLGI; -.
DR   OrthoDB; EOG48D0WH; -.
DR   PhylomeDB; Q9WV55; -.
DR   NextBio; 307452; -.
DR   ArrayExpress; Q9WV55; -.
DR   Bgee; Q9WV55; -.
DR   Genevestigator; Q9WV55; -.
DR   GermOnline; ENSMUSG00000024091; Mus musculus.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   InterPro; IPR000535; Major_sperm.
DR   InterPro; IPR008962; PapD-like.
DR   InterPro; IPR016763; Vesicle-associated_membrane.
DR   Gene3D; G3DSA:2.60.40.360; MSP; 1.
DR   Pfam; PF00635; Motile_Sperm; 1.
DR   PIRSF; PIRSF019693; VAMP-associated; 1.
DR   SUPFAM; SSF49354; PapD-like; 1.
DR   PROSITE; PS50202; MSP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell membrane; Coiled coil;
KW   Direct protein sequencing; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    249       Vesicle-associated membrane protein-
FT                                associated protein A.
FT                                /FTId=PRO_0000213471.
FT   TOPO_DOM      2    228       Cytoplasmic (Potential).
FT   TRANSMEM    229    249       Helical; Anchor for type IV membrane
FT                                protein; (Potential).
FT   DOMAIN       14    131       MSP.
FT   COILED      168    207       Potential.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     125    125       N6-acetyllysine (By similarity).
FT   CONFLICT     10     11       KH -> ND (in Ref. 4; AAF23076).
FT   CONFLICT    154    154       K -> R (in Ref. 4; AAF23076).
FT   STRAND       15     26
FT   STRAND       29     31
FT   STRAND       35     40
FT   STRAND       43     45
FT   STRAND       47     54
FT   STRAND       58     67
FT   STRAND       73     80
FT   STRAND       95    101
FT   HELIX       109    115
FT   TURN        118    120
FT   STRAND      122    131
SQ   SEQUENCE   249 AA;  27855 MW;  FE8F956C1F2C71CA CRC64;
     MASASGAMAK HEQILVLDPP SDLKFKGPFT DVVTTNLKLQ NPSDRKVCFK VKTTAPRRYC
     VRPNSGIIDP GSIVTVSVML QPFDYDPNEK SKHKFMVQTI FAPPNISDME AVWKEAKPDE
     LMDSKLRCVF EMPNENDKLN DMEPSKAVPL NASKQDGPLP KPHSVSLNDT ETRKLMEECK
     RLQGEMMKLS EENRHLRDEG LRLRKVAHSD KPGSTSAVSF RDNVTSPLPS LLVVIAAIFI
     GFFLGKFIL
//
ID   GSK3B_MOUSE             Reviewed;         420 AA.
AC   Q9WV60;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 2.
DT   08-MAR-2011, entry version 113.
DE   RecName: Full=Glycogen synthase kinase-3 beta;
DE            Short=GSK-3 beta;
DE            EC=2.7.11.26;
GN   Name=Gsk3b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RA   Salameh W.A., Guo T.B., Chan K.C., Mitchell A.P.;
RT   "Testicular expression and hormonal control of glycogen synthase
RT   kinase 3, a homologue of yeast RIM11.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II, and FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   INTERACTION WITH ARRB2.
RX   PubMed=16051150; DOI=10.1016/j.cell.2005.05.012;
RA   Beaulieu J.-M., Sotnikova T.D., Marion S., Lefkowitz R.J.,
RA   Gainetdinov R.R., Caron M.G.;
RT   "An Akt/beta-arrestin 2/PP2A signaling complex mediates dopaminergic
RT   neurotransmission and behavior.";
RL   Cell 122:261-273(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, AND MASS
RP   SPECTROMETRY.
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216 AND SER-219, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-216 AND SER-219, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; TYR-216; SER-389
RP   AND THR-395, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-7; TYR-216 AND SER-219,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [11]
RP   INTERACTION WITH DISC1.
RX   PubMed=19303846; DOI=10.1016/j.cell.2008.12.044;
RA   Mao Y., Ge X., Frank C.L., Madison J.M., Koehler A.N., Doud M.K.,
RA   Tassa C., Berry E.M., Soda T., Singh K.K., Biechele T.,
RA   Petryshen T.L., Moon R.T., Haggarty S.J., Tsai L.H.;
RT   "Disrupted in schizophrenia 1 regulates neuronal progenitor
RT   proliferation via modulation of GSK3beta/beta-catenin signaling.";
RL   Cell 136:1017-1031(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Participates in the Wnt signaling pathway. Implicated in
CC       the hormonal control of several regulatory proteins including
CC       glycogen synthase, MYB and the transcription factor JUN.
CC       Phosphorylates JUN at sites proximal to its DNA-binding domain,
CC       thereby reducing its affinity for DNA. May phosphorylate MUC1 and
CC       decrease the interaction of MUC1 with CTNNB1/beta-catenin.
CC       Phosphorylates CTNNB1/beta-catenin. Phosphorylates SNAI1 (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + [tau protein] = ADP + [tau protein]
CC       phosphate.
CC   -!- SUBUNIT: Monomer (By similarity). Interacts with CABYR, MMP2,
CC       MUC1, NIN and PRUNE (By similarity). Interacts with AXIN1; the
CC       interaction mediates hyperphosphorylates of CTNNB1 leading to its
CC       ubiquitination and destruction. Interacts with and phosphorylates
CC       SNAI1. Interacts with DNM1L (via a C-terminal domain) (By
CC       similarity). Interacts with ARRB2 and DISC1.
CC   -!- INTERACTION:
CC       Q811T9:Disc1; NbExp=1; IntAct=EBI-400793, EBI-2298259;
CC       Q9WUA5:Epm2a; NbExp=2; IntAct=EBI-400793, EBI-1040928;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity).
CC   -!- PTM: Phosphorylation on Tyr-216 is necessary for the activity (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. GSK-3 subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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CC   -----------------------------------------------------------------------
DR   EMBL; AF156099; AAD39258.2; -; mRNA.
DR   EMBL; BC006936; AAH06936.1; -; mRNA.
DR   EMBL; BC060743; AAH60743.1; -; mRNA.
DR   IPI; IPI00125319; -.
DR   RefSeq; NP_062801.1; NM_019827.6.
DR   UniGene; Mm.394930; -.
DR   ProteinModelPortal; Q9WV60; -.
DR   SMR; Q9WV60; 23-386.
DR   IntAct; Q9WV60; 7.
DR   STRING; Q9WV60; -.
DR   PhosphoSite; Q9WV60; -.
DR   PRIDE; Q9WV60; -.
DR   Ensembl; ENSMUST00000023507; ENSMUSP00000023507; ENSMUSG00000022812.
DR   GeneID; 56637; -.
DR   KEGG; mmu:56637; -.
DR   UCSC; uc007zen.1; mouse.
DR   CTD; 56637; -.
DR   MGI; MGI:1861437; Gsk3b.
DR   GeneTree; ENSGT00520000055635; -.
DR   HOVERGEN; HBG014652; -.
DR   OrthoDB; EOG4WH8KZ; -.
DR   PhylomeDB; Q9WV60; -.
DR   BRENDA; 2.7.11.26; 244.
DR   NextBio; 313081; -.
DR   PMAP-CutDB; Q9WV60; -.
DR   ArrayExpress; Q9WV60; -.
DR   Bgee; Q9WV60; -.
DR   CleanEx; MM_GSK3B; -.
DR   Genevestigator; Q9WV60; -.
DR   GermOnline; ENSMUSG00000022812; Mus musculus.
DR   GO; GO:0034747; C:Axin-APC-beta-catenin-GSK3B complex; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0043198; C:dendritic shaft; IDA:MGI.
DR   GO; GO:0030426; C:growth cone; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; EXP:Reactome.
DR   GO; GO:0005625; C:soluble fraction; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008013; F:beta-catenin binding; IPI:MGI.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
DR   GO; GO:0050321; F:tau-protein kinase activity; IDA:MGI.
DR   GO; GO:0006916; P:anti-apoptosis; IMP:MGI.
DR   GO; GO:0007409; P:axonogenesis; IGI:MGI.
DR   GO; GO:0044337; P:canonical Wnt receptor signaling pathway involved in positive regulation of apoptosis; IMP:BHF-UCL.
DR   GO; GO:0016477; P:cell migration; IGI:MGI.
DR   GO; GO:0008283; P:cell proliferation; TAS:MGI.
DR   GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB.
DR   GO; GO:0006983; P:ER overload response; IDA:MGI.
DR   GO; GO:0045444; P:fat cell differentiation; IDA:MGI.
DR   GO; GO:0007520; P:myoblast fusion; IDA:MGI.
DR   GO; GO:0009887; P:organ morphogenesis; IMP:MGI.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:MGI.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:MGI.
DR   GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:MGI.
DR   GO; GO:0006611; P:protein export from nucleus; IDA:MGI.
DR   GO; GO:0035372; P:protein localization to microtubule; IGI:MGI.
DR   GO; GO:0000320; P:re-entry into mitotic cell cycle; IDA:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase;
KW   Wnt signaling pathway.
FT   CHAIN         1    420       Glycogen synthase kinase-3 beta.
FT                                /FTId=PRO_0000085981.
FT   DOMAIN       56    340       Protein kinase.
FT   NP_BIND      62     70       ATP (By similarity).
FT   ACT_SITE    181    181       Proton acceptor (By similarity).
FT   BINDING      85     85       ATP (By similarity).
FT   MOD_RES       7      7       Phosphothreonine.
FT   MOD_RES       9      9       Phosphoserine; by PKB/AKT1 (By
FT                                similarity).
FT   MOD_RES      25     25       Phosphoserine (By similarity).
FT   MOD_RES     215    215       Phosphoserine.
FT   MOD_RES     216    216       Phosphotyrosine.
FT   MOD_RES     219    219       Phosphoserine.
FT   MOD_RES     275    275       Phosphothreonine (By similarity).
FT   MOD_RES     277    277       Phosphothreonine (By similarity).
FT   MOD_RES     389    389       Phosphoserine.
FT   MOD_RES     395    395       Phosphothreonine.
FT   MOD_RES     398    398       Phosphoserine (By similarity).
FT   MOD_RES     413    413       Phosphoserine (By similarity).
FT   MOD_RES     415    415       Phosphoserine (By similarity).
FT   MOD_RES     417    417       Phosphoserine (By similarity).
FT   MOD_RES     419    419       Phosphoserine (By similarity).
SQ   SEQUENCE   420 AA;  46710 MW;  200C3FD1B38B4883 CRC64;
     MSGRPRTTSF AESCKPVQQP SAFGSMKVSR DKDGSKVTTV VATPGQGPDR PQEVSYTDTK
     VIGNGSFGVV YQAKLCDSGE LVAIKKVLQD KRFKNRELQI MRKLDHCNIV RLRYFFYSSG
     EKKDEVYLNL VLDYVPETVY RVARHYSRAK QTLPVIYVKL YMYQLFRSLA YIHSFGICHR
     DIKPQNLLLD PDTAVLKLCD FGSAKQLVRG EPNVSYICSR YYRAPELIFG ATDYTSSIDV
     WSAGCVLAEL LLGQPIFPGD SGVDQLVEII KVLGTPTREQ IREMNPNYTE FKFPQIKAHP
     WTKVFRPRTP PEAIALCSRL LEYTPTARLT PLEACAHSFF DELRDPNVKL PNGRDTPALF
     NFTTQELSSN PPLATILIPP HARIQAAASP PANATAASDT NAGDRGQTNN AASASASNST
//
ID   DEMA_MOUSE              Reviewed;         405 AA.
AC   Q9WV69;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-FEB-2011, entry version 74.
DE   RecName: Full=Dematin;
DE   AltName: Full=Erythrocyte membrane protein band 4.9;
GN   Name=Epb49; Synonyms=Epb4.9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Spleen;
RX   MEDLINE=99431674; PubMed=10501976; DOI=10.1007/s003359901153;
RA   Azim A.C., Kim A.C., Lutchman M., Andrabi S., Peters L.L.,
RA   Chishti A.H.;
RT   "cDNA sequence, genomic structure, and expression of the mouse dematin
RT   gene (Epb4.9).";
RL   Mamm. Genome 10:1026-1029(1999).
RN   [2]
RP   INTERACTION WITH RASGRF2.
RX   PubMed=11856323; DOI=10.1046/j.0014-2956.2001.02694.x;
RA   Lutchman M., Kim A.C., Cheng L., Whitehead I.P., Oh S.S., Hanspal M.,
RA   Boukharov A.A., Hanada T., Chishti A.H.;
RT   "Dematin interacts with the Ras-guanine nucleotide exchange factor
RT   Ras-GRF2 and modulates mitogen-activated protein kinase pathways.";
RL   Eur. J. Biochem. 269:638-649(2002).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92 AND SER-226, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87; SER-156; SER-226 AND
RP   SER-372, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-91; SER-289 AND SER-333,
RP   AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-114, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Actin-bundling protein. May function in mitogen-
CC       activated protein kinase pathway (By similarity).
CC   -!- SUBUNIT: Interacts with RASGRF2.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- DOMAIN: Contains at least two actin-binding sites, one in the
CC       headpiece domain and one in the amino-terminal portion.
CC   -!- DOMAIN: Consists of a large core fragment, the amino-terminal
CC       portion, and a small headpiece, the C-terminal portion. The
CC       headpiece can bind but cannot bundle actin filaments.
CC   -!- SIMILARITY: Belongs to the villin/gelsolin family.
CC   -!- SIMILARITY: Contains 1 HP (headpiece) domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF155547; AAD38412.1; -; mRNA.
DR   IPI; IPI00125328; -.
DR   UniGene; Mm.210863; -.
DR   UniGene; Mm.446654; -.
DR   ProteinModelPortal; Q9WV69; -.
DR   SMR; Q9WV69; 341-405.
DR   STRING; Q9WV69; -.
DR   PhosphoSite; Q9WV69; -.
DR   PRIDE; Q9WV69; -.
DR   Ensembl; ENSMUST00000022695; ENSMUSP00000022695; ENSMUSG00000022099.
DR   MGI; MGI:99670; Epb4.9.
DR   GeneTree; ENSGT00570000079028; -.
DR   HOGENOM; HBG443563; -.
DR   HOVERGEN; HBG031499; -.
DR   InParanoid; Q9WV69; -.
DR   OMA; PSYGRTT; -.
DR   ArrayExpress; Q9WV69; -.
DR   Bgee; Q9WV69; -.
DR   CleanEx; MM_EPB4.9; -.
DR   Genevestigator; Q9WV69; -.
DR   GermOnline; ENSMUSG00000022099; Mus musculus.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR   GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR   InterPro; IPR003128; Villin_headpiece.
DR   Gene3D; G3DSA:1.10.950.10; VHP; 1.
DR   Pfam; PF02209; VHP; 1.
DR   SMART; SM00153; VHP; 1.
DR   SUPFAM; SSF47050; VHP; 1.
DR   PROSITE; PS51089; HP; 1.
PE   1: Evidence at protein level;
KW   Actin capping; Actin-binding; Cytoplasm; Phosphoprotein; Repeat.
FT   CHAIN         1    405       Dematin.
FT                                /FTId=PRO_0000218756.
FT   DOMAIN      337    405       HP.
FT   REGION      224    308       Interaction with RASGRF2 (By similarity).
FT   COMPBIAS    216    222       Poly-Glu.
FT   MOD_RES      10     10       Phosphothreonine (By similarity).
FT   MOD_RES      14     14       Phosphoserine (By similarity).
FT   MOD_RES      16     16       Phosphoserine (By similarity).
FT   MOD_RES      22     22       Phosphoserine (By similarity).
FT   MOD_RES      26     26       Phosphoserine (By similarity).
FT   MOD_RES      28     28       Phosphoserine (By similarity).
FT   MOD_RES      87     87       Phosphoserine.
FT   MOD_RES      91     91       Phosphothreonine.
FT   MOD_RES      92     92       Phosphoserine.
FT   MOD_RES      96     96       Phosphoserine (By similarity).
FT   MOD_RES     114    114       Phosphothreonine.
FT   MOD_RES     156    156       Phosphoserine.
FT   MOD_RES     226    226       Phosphoserine.
FT   MOD_RES     289    289       Phosphoserine.
FT   MOD_RES     333    333       Phosphoserine.
FT   MOD_RES     372    372       Phosphoserine.
FT   MOD_RES     403    403       Phosphoserine; by PKA (By similarity).
SQ   SEQUENCE   405 AA;  45468 MW;  AECA552500BDD19A CRC64;
     MERLQKQPLT SPGSVSSSRD SSVPGSPSSI VAKMDNQVLG YKDLAAIPKD KAILDIERPD
     LMIYEPHFTY SLLEHVELPR SRECSLSPKS TSPPPSPEVW AESRTLGIIS QASTPRTTGT
     PRTSLPHFHH PETTRPDSNI YKKPPIYKQR ESVGGSPQSK HLIEDLIIES SKFPAAQPPD
     PNQPAKIETD YWPCPPSLAV VETEWRKRKA SRKGAEEEEE EEDDDSEEEI KAIRERQKEE
     LSKVTSNLGK MILKEEMEKS LPIRRKTRSL PDRTPFHTSL HSGTSKSSSL PSYGRTTLSR
     LQSTEFSPSG SEAGSPGLQN GEGQRGRMDR GNSLPCVLEQ KIYPYEMLVV TNKGRTKLPP
     GVDRMRLERH LSAEDFSRVF AMSPEEFGKL ALWKRNELKK KASLF
//
ID   SNX1_MOUSE              Reviewed;         522 AA.
AC   Q9WV80; Q9EQZ9;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Sorting nexin-1;
GN   Name=Snx1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Thymus;
RA   Takahara K., Omatsu Y., Maeda Y., Shimoyama S., Inaba K.;
RT   "Complete sequence of mouse sorting nexin 1 (Snx1) cDNA.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
RC   STRAIN=C57BL/6;
RX   MEDLINE=21583642; PubMed=11726276;
RA   Nakamura N., Sun-Wada G.H., Yamamoto A., Wada Y., Futai M.;
RT   "Association of mouse sorting nexin 1 with early endosomes.";
RL   J. Biochem. 130:765-771(2001).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=12388759; DOI=10.1091/mbc.E02-03-0145;
RA   Schwarz D.G., Griffin C.T., Schneider E.A., Yee D., Magnuson T.;
RT   "Genetic analysis of sorting nexins 1 and 2 reveals a redundant and
RT   essential function in mice.";
RL   Mol. Biol. Cell 13:3588-3600(2002).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May be involved in several stages of intracellular
CC       trafficking. Plays a role in targeting ligand-activated EGFR to
CC       the lysosomes for degradation after endocytosis from the cell
CC       surface and release from the Golgi. Component of the retromer
CC       complex, a complex required to retrieve lysosomal enzyme receptors
CC       (IGF2R and M6PR) from endosomes to the trans-Golgi network.
CC       Interacts with membranes containing phosphatidylinositol 3-
CC       phosphate (PtdIns(3P)) or phosphatidylinositol 3,5-bisphosphate
CC       (PtdIns(3,5)P2) (By similarity).
CC   -!- SUBUNIT: Self-assembles into a complex of approximately 300 kDa.
CC       Interacts with HGS. Component of the retromer complex composed of
CC       VPS26 (VPS26A or VPS26B), VPS29, VPS35, SNX1 and SNX2. Interacts
CC       with SNX6 (By similarity).
CC   -!- INTERACTION:
CC       O88351:Ikbkb; NbExp=2; IntAct=EBI-646356, EBI-447960;
CC   -!- SUBCELLULAR LOCATION: Endosome membrane; Peripheral membrane
CC       protein; Cytoplasmic side (By similarity). Golgi apparatus, trans-
CC       Golgi network membrane; Peripheral membrane protein; Cytoplasmic
CC       side (By similarity). Early endosome membrane; Peripheral membrane
CC       protein; Cytoplasmic side (By similarity). Note=Enriched on
CC       tubular elements of the early endosome membrane. Binds
CC       preferentially to highly curved membranes enriched in
CC       phosphatidylinositol 3-phosphate (PtdIns(3P)) or
CC       phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) (By
CC       similarity).
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice are born at the
CC       expected Mendelian ratio and are fertile. Mice lacking both Snx1
CC       and Snx2 die during embryonic development, around 9.5 and 11.5
CC       dpc.
CC   -!- MISCELLANEOUS: Binds phosphatidylinositol 3-phosphate (PtdIns-
CC       (3)P) and phosphatidylinositol 3,5-bisphosphate (PtdIns-(3,5)P2)
CC       in liposome-based assays. Can bind PtdIns(3,4,5)P3 in
CC       protein:lipid overlay assays, but not in liposome-based assays (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the sorting nexin family.
CC   -!- SIMILARITY: Contains 1 PX (phox homology) domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF154120; AAD38805.1; -; mRNA.
DR   EMBL; AB019214; BAB20283.1; -; mRNA.
DR   IPI; IPI00622364; -.
DR   RefSeq; NP_062701.2; NM_019727.2.
DR   UniGene; Mm.271891; -.
DR   ProteinModelPortal; Q9WV80; -.
DR   SMR; Q9WV80; 142-269.
DR   IntAct; Q9WV80; 2.
DR   STRING; Q9WV80; -.
DR   PhosphoSite; Q9WV80; -.
DR   PRIDE; Q9WV80; -.
DR   Ensembl; ENSMUST00000034946; ENSMUSP00000034946; ENSMUSG00000032382.
DR   GeneID; 56440; -.
DR   KEGG; mmu:56440; -.
DR   CTD; 56440; -.
DR   MGI; MGI:1928395; Snx1.
DR   GeneTree; ENSGT00550000074512; -.
DR   HOGENOM; HBG445848; -.
DR   HOVERGEN; HBG000618; -.
DR   InParanoid; Q9WV80; -.
DR   OrthoDB; EOG418BNH; -.
DR   PhylomeDB; Q9WV80; -.
DR   NextBio; 312630; -.
DR   ArrayExpress; Q9WV80; -.
DR   Bgee; Q9WV80; -.
DR   CleanEx; MM_SNX1; -.
DR   Genevestigator; Q9WV80; -.
DR   GermOnline; ENSMUSG00000032382; Mus musculus.
DR   GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   InterPro; IPR001683; Phox.
DR   InterPro; IPR005329; Sorting_nexin_N.
DR   InterPro; IPR015404; Vps5_C.
DR   Gene3D; G3DSA:3.30.1520.10; PX; 1.
DR   Pfam; PF00787; PX; 1.
DR   Pfam; PF03700; Sorting_nexin; 1.
DR   Pfam; PF09325; Vps5; 1.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; PX; 1.
DR   PROSITE; PS50195; PX; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Endosome; Golgi apparatus; Lipid-binding; Membrane;
KW   Phosphoprotein; Protein transport; Transport.
FT   CHAIN         1    522       Sorting nexin-1.
FT                                /FTId=PRO_0000213836.
FT   DOMAIN      143    272       PX.
FT   BINDING     186    186       Phosphatidylinositol 3-phosphate (By
FT                                similarity).
FT   BINDING     188    188       Phosphatidylinositol 3-phosphate; via
FT                                amide nitrogen and carbonyl oxygen (By
FT                                similarity).
FT   BINDING     214    214       Phosphatidylinositol 3-phosphate (By
FT                                similarity).
FT   BINDING     238    238       Phosphatidylinositol 3-phosphate (By
FT                                similarity).
FT   MOD_RES      32     32       Phosphoserine (By similarity).
FT   MOD_RES      39     39       Phosphoserine (By similarity).
FT   MOD_RES      41     41       Phosphothreonine (By similarity).
FT   MOD_RES     188    188       Phosphoserine.
FT   MOD_RES     237    237       N6-acetyllysine (By similarity).
FT   CONFLICT     31     31       A -> G (in Ref. 2; BAB20283).
FT   CONFLICT    117    117       S -> P (in Ref. 2; BAB20283).
FT   CONFLICT    124    124       S -> C (in Ref. 2; BAB20283).
FT   CONFLICT    138    138       Missing (in Ref. 2; BAB20283).
FT   CONFLICT    389    389       S -> F (in Ref. 2; BAB20283).
SQ   SEQUENCE   522 AA;  58952 MW;  1EFC06B3EA551311 CRC64;
     MASGGGGCSA SERLPPPFPG MDPESEGAAG ASEPEAGDSD TEGEDIFTGA AAATKPQSPK
     KTTSLFPIKN GSKENGIHED QDQEPQDLFA DATVELSLDS TQNNQKTMPG KTLTSHSPQE
     ATNSPKPQPS YEELEEEEQE DQFDLTVGIT DPEKIGDGMN AYVAYKVTTQ TSLPMFRSRQ
     FAVKRRFSDF LGLYEKLSEK HSQNGFIVPP PPEKSLIGMT KVKVGKEDSS SAEFLEKRRA
     ALERYLQRIV NHPTMLQDPD VREFLEKEEL PRAVGTQALS GAGLLKMFNK ATDAVSKMTI
     KMNESDIWFE EKLQEVECEE QRLRKLHAVV ETLVNHRKEL ALNTALFAKS LAMLGSSEDN
     TALSRALSQL AEVEEKIEQL HQEQANNDSF LLAELLSDYI RLLAIVRAAF DQRMKTWQRW
     QDAQATLQKK RESEARLLWA NKPDKLQQAK DEITEWESRV TQYERDFERI STVVRKEVTR
     FEKEKSKDFK NHVMKYLETL LHSQQQLAKY WEAFLPEAKA IS
//
ID   STXB4_MOUSE             Reviewed;         557 AA.
AC   Q9WV89; Q5SUA6; Q5SUA8; Q5SUA9; Q8CFL1;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=Syntaxin-binding protein 4;
DE   AltName: Full=Syntaxin 4-interacting protein;
DE            Short=STX4-interacting protein;
DE            Short=Synip;
GN   Name=Stxbp4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP   LOCATION, INTERACTION WITH STX4A, AND TISSUE SPECIFICITY.
RX   MEDLINE=99322667; PubMed=10394363; DOI=10.1016/S1097-2765(01)80007-1;
RA   Min J., Okada S., Kanzaki M., Elmendorf J.S., Coker K.J., Ceresa B.P.,
RA   Syu L.-J., Noda Y., Saltiel A.R., Pessin J.E.;
RT   "Synip: a novel insulin-regulated syntaxin 4-binding protein mediating
RT   GLUT4 translocation in adipocytes.";
RL   Mol. Cell 3:751-760(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 368-557 (ISOFORM 4).
RC   STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12855681; DOI=10.1074/jbc.M305114200;
RA   Saito T., Okada S., Yamada E., Ohshima K., Shimizu H., Shimomura K.,
RA   Sato M., Pessin J.E., Mori M.;
RT   "Syntaxin 4 and Synip (syntaxin 4 interacting protein) regulate
RT   insulin secretion in the pancreatic beta HC-9 cell.";
RL   J. Biol. Chem. 278:36718-36725(2003).
RN   [6]
RP   PHOSPHORYLATION AT SER-99, AND MUTAGENESIS OF SER-97 AND SER-99.
RX   PubMed=15753124; DOI=10.1083/jcb.200408182;
RA   Yamada E., Okada S., Saito T., Ohshima K., Sato M., Tsuchiya T.,
RA   Uehara Y., Shimizu H., Mori M.;
RT   "Akt2 phosphorylates Synip to regulate docking and fusion of GLUT4-
RT   containing vesicles.";
RL   J. Cell Biol. 168:921-928(2005).
RN   [7]
RP   STRUCTURE BY NMR OF 12-107.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the PDZ domain of syntaxin binding protein 4.";
RL   Submitted (JUN-2005) to the PDB data bank.
CC   -!- FUNCTION: Plays a role in the translocation of transport vesicles
CC       from the cytoplasm to the plasma membrane. Inhibits the
CC       translocation of SLC2A4 from intracellular vesicles to the plasma
CC       membrane by STX4A binding and preventing the interaction between
CC       STX4A and VAMP2. Stimulation with insulin disrupts the interaction
CC       with STX4A, leading to increased levels of SLC2A4 at the plasma
CC       membrane. May also play a role in the regulation of insulin
CC       release by pancreatic beta cells after stimulation by glucose.
CC   -!- SUBUNIT: Interacts with STX4A.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q9WV89-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9WV89-2; Sequence=VSP_017183;
CC       Name=3;
CC         IsoId=Q9WV89-3; Sequence=VSP_017179, VSP_017180;
CC         Note=Gene prediction based on EST data;
CC       Name=4;
CC         IsoId=Q9WV89-4; Sequence=VSP_017184, VSP_017185;
CC         Note=Gene prediction based on EST data;
CC       Name=5;
CC         IsoId=Q9WV89-5; Sequence=VSP_017181, VSP_017182;
CC         Note=Gene prediction based on EST data;
CC   -!- TISSUE SPECIFICITY: Detected in skeletal muscle, heart, testis,
CC       adipocytes and pancreatic islet cells.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity). Phosphorylated on Ser-99 by PKB/AKT2 after insulin
CC       treatment. Phosphorylation on Ser-99 abolishes the interaction
CC       with STX4A.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
CC   -!- SIMILARITY: Contains 1 WW domain.
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DR   EMBL; AF152924; AAD43533.1; -; mRNA.
DR   EMBL; AL646046; CAI23907.1; -; Genomic_DNA.
DR   EMBL; AL646046; CAI23908.1; -; Genomic_DNA.
DR   EMBL; AL646046; CAI23909.1; -; Genomic_DNA.
DR   EMBL; AL646046; CAI23910.1; -; Genomic_DNA.
DR   EMBL; AL646046; CAI23911.1; -; Genomic_DNA.
DR   EMBL; BC032881; AAH32881.1; -; mRNA.
DR   EMBL; AK138499; BAE23686.1; -; mRNA.
DR   IPI; IPI00125455; -.
DR   IPI; IPI00461639; -.
DR   IPI; IPI00515178; -.
DR   IPI; IPI00648170; -.
DR   IPI; IPI00648897; -.
DR   RefSeq; NP_035635.1; NM_011505.2.
DR   UniGene; Mm.207203; -.
DR   PDB; 1WI4; NMR; -; A=12-107.
DR   PDBsum; 1WI4; -.
DR   ProteinModelPortal; Q9WV89; -.
DR   SMR; Q9WV89; 13-113, 502-534.
DR   STRING; Q9WV89; -.
DR   PhosphoSite; Q9WV89; -.
DR   PRIDE; Q9WV89; -.
DR   Ensembl; ENSMUST00000020858; ENSMUSP00000020858; ENSMUSG00000020546.
DR   Ensembl; ENSMUST00000107873; ENSMUSP00000103505; ENSMUSG00000020546.
DR   GeneID; 20913; -.
DR   KEGG; mmu:20913; -.
DR   UCSC; uc007kwv.1; mouse.
DR   UCSC; uc007kwx.1; mouse.
DR   UCSC; uc007kwy.1; mouse.
DR   CTD; 20913; -.
DR   MGI; MGI:1342296; Stxbp4.
DR   eggNOG; roNOG06804; -.
DR   GeneTree; ENSGT00390000002226; -.
DR   HOGENOM; HBG443872; -.
DR   HOVERGEN; HBG058016; -.
DR   InParanoid; Q9WV89; -.
DR   OMA; DPAFQMI; -.
DR   PhylomeDB; Q9WV89; -.
DR   NextBio; 299809; -.
DR   ArrayExpress; Q9WV89; -.
DR   Bgee; Q9WV89; -.
DR   CleanEx; MM_STXBP4; -.
DR   Genevestigator; Q9WV89; -.
DR   GermOnline; ENSMUSG00000020546; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0015758; P:glucose transport; IDA:MGI.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; IDA:MGI.
DR   GO; GO:0006605; P:protein targeting; IDA:MGI.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00456; WW; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF51045; WW_Rsp5_WWP; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 1.
DR   PROSITE; PS50020; WW_DOMAIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil; Cytoplasm;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1    557       Syntaxin-binding protein 4.
FT                                /FTId=PRO_0000076331.
FT   DOMAIN       19    105       PDZ.
FT   DOMAIN      500    533       WW.
FT   COILED      298    408       Potential.
FT   MOD_RES      10     10       Phosphoserine (By similarity).
FT   MOD_RES      99     99       Phosphoserine; by PKB/AKT2.
FT   MOD_RES     464    464       Phosphoserine (By similarity).
FT   MOD_RES     467    467       Phosphoserine (By similarity).
FT   VAR_SEQ     195    226       DIAPAWTDDDSGPQGKISLNPSVRLKAEKLEM -> AHMER
FT                                KKRHESSGQSKMWHWSCSMMKVEVFIP (in isoform
FT                                3).
FT                                /FTId=VSP_017179.
FT   VAR_SEQ     227    557       Missing (in isoform 3).
FT                                /FTId=VSP_017180.
FT   VAR_SEQ     227    258       ALNYLGIQPTKEQREALREQVQADSKGTVSFG -> VNPLK
FT                                KNHFLHKTAGKNCLVLGEEDIGESLVS (in isoform
FT                                5).
FT                                /FTId=VSP_017181.
FT   VAR_SEQ     259    557       Missing (in isoform 5).
FT                                /FTId=VSP_017182.
FT   VAR_SEQ     502    557       LPYGWEEAYTADGIKYFINHVTQTTSWIHPVMSALNLSCAE
FT                                ESEEDCPRELTDPKS -> KLSLSSSSSPSSSSSFSSSSSC
FT                                NLLNKAEERP (in isoform 2).
FT                                /FTId=VSP_017183.
FT   VAR_SEQ     520    520       N -> K (in isoform 4).
FT                                /FTId=VSP_017184.
FT   VAR_SEQ     521    557       Missing (in isoform 4).
FT                                /FTId=VSP_017185.
FT   MUTAGEN      97     97       S->F: No effect.
FT   MUTAGEN      99     99       S->F: Abolishes phosphorylation by
FT                                PKB/AKT2.
FT   STRAND       20     25
FT   STRAND       33     37
FT   STRAND       39     43
FT   STRAND       45     52
FT   HELIX        57     61
FT   STRAND       69     73
FT   HELIX        83     92
FT   STRAND       96     99
FT   STRAND      101    106
SQ   SEQUENCE   557 AA;  61689 MW;  9211A8B02AF8EC86 CRC64;
     MSDGTASARS SSPLDRDPAF RVITVTKETG LGLKILGGIN RNEGPLVYIH EVIPGGDCYK
     DGRLKPGDQL VSINKESMIG VSFEEAKSII TRAKLRSESP WEIAFIRQKS YCGHPGNICC
     PSPQVSEDCG PQTSTFTLLS SPSETLLPKT SSTPQTQDST FPSCKAIQTK PEHDKTEHSP
     ITSLDNSPAD TSNADIAPAW TDDDSGPQGK ISLNPSVRLK AEKLEMALNY LGIQPTKEQR
     EALREQVQAD SKGTVSFGDF VQVARSLFCL QLDEVNVGVH EIPSILDSQL LPCDSLEADE
     VGKLRQERNA ALEERNVLKE KLLESEKHRK QLIEELQNVK QEAKAVAEET RALRSRIHLA
     EAAQRQAHGM EMDYEEVIRL LEAEVSELKA QLADYSDQNK ESVQDLRKRV TVLDCQLRKS
     EMARKAFKAS TERLLGFIEA IQEVLLDSSA PLSTLSERRA VLASQTSLPL LARNGRSFPA
     TLLLESKELV RSVRAILDMD CLPYGWEEAY TADGIKYFIN HVTQTTSWIH PVMSALNLSC
     AEESEEDCPR ELTDPKS
//
ID   E41L3_MOUSE             Reviewed;         929 AA.
AC   Q9WV92; Q69ZT8; Q9R102;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 96.
DE   RecName: Full=Band 4.1-like protein 3;
DE   AltName: Full=4.1B;
DE   AltName: Full=Differentially expressed in adenocarcinoma of the lung protein 1;
DE            Short=DAL-1;
DE            Short=DAL1P;
DE            Short=mDAL-1;
GN   Name=Epb41l3; Synonyms=Dal1, Epb4.1l3, Kiaa0987;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6).
RC   TISSUE=Brain;
RX   MEDLINE=20119278; PubMed=10652311; DOI=10.1074/jbc.275.5.3247;
RA   Parra M., Gascard P., Walensky L.D., Gimm J.A., Blackshaw S., Chan N.,
RA   Takakuwa Y., Berger T., Lee G., Chasis J.A., Snyder S.H., Mohandas N.,
RA   Conboy J.G.;
RT   "Molecular and functional characterization of protein 4.1B, a novel
RT   member of the protein 4.1 family with high level, focal expression in
RT   brain.";
RL   J. Biol. Chem. 275:3247-3255(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-929 (ISOFORM 7).
RC   STRAIN=BALB/c; TISSUE=Brain;
RA   Azam M., Andrabi S., Lin L., Newsham I., Chishti A.H.;
RT   "Mouse DAL-1 (mDAL-1) cDNA sequence.";
RL   Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 202-929 (ISOFORM 8).
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 719-929 (ISOFORMS 4/5/6/7).
RA   Marra M., Hillier L., Kucaba T., Martin J., Beck C., Wylie T.,
RA   Underwood K., Steptoe M., Theising B., Allen M., Bowers Y., Person B.,
RA   Swaller T., Gibbons M., Pape D., Harvey N., Schurk R., Ritter E.,
RA   Kohn S., Shin T., Jackson Y., Cardenas M., McCann R., Waterston R.,
RA   Wilson R.;
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470; SER-486; THR-495;
RP   SER-543; SER-547 AND SER-804, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-486; THR-495;
RP   SER-543; SER-547; THR-623; SER-626 AND SER-627, AND MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND THR-923, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-451; SER-486;
RP   THR-488; THR-495; THR-542; SER-547; THR-798 AND SER-804, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486; THR-495 AND
RP   SER-543, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-797 AND THR-798, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RA   Lubec G., Kang S.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96; SER-428; SER-451 AND
RP   SER-599, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-486, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Isoform 2 (heart-specific) has the complete spectrin--
CC       actin-binding (SAB) domain and fully interacts with spectrin and
CC       actin.
CC   -!- SUBUNIT: Interacts with CADM1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC         Comment=Experimental confirmation may be lacking for some
CC         isoforms;
CC       Name=1; Synonyms=4.1B-brain;
CC         IsoId=Q9WV92-1; Sequence=Displayed;
CC       Name=2; Synonyms=4.1B-heart;
CC         IsoId=Q9WV92-2; Sequence=VSP_000490, VSP_000489;
CC       Name=3; Synonyms=4.1B-kidney;
CC         IsoId=Q9WV92-3; Sequence=VSP_000490;
CC       Name=4; Synonyms=4.1b-brain;
CC         IsoId=Q9WV92-4; Sequence=VSP_000491;
CC       Name=5; Synonyms=4.1B-heart;
CC         IsoId=Q9WV92-5; Sequence=VSP_000490, VSP_000489, VSP_000491;
CC       Name=6; Synonyms=4.1B-kidney;
CC         IsoId=Q9WV92-6; Sequence=VSP_000490, VSP_000491;
CC       Name=7;
CC         IsoId=Q9WV92-7; Sequence=VSP_000487, VSP_000490, VSP_000488,
CC                                  VSP_000491;
CC         Note=Inferred from the cDNA sequence of Ref.2;
CC       Name=8;
CC         IsoId=Q9WV92-8; Sequence=VSP_000487, VSP_023063, VSP_000491;
CC   -!- TISSUE SPECIFICITY: Highest expression in brain, lower in testis,
CC       adrenal gland, heart and kidney. Also present in muscle and
CC       epithelial cells. Isoform 1 is expressed in brain, isoform 2 is
CC       expressed in heart and isoform 3 is mostly expressed in kidney but
CC       also in heart and brain. Isoform 6 seems to be most abundant in
CC       kidney while isoform 4 and isoform 5 are predominantly expressed
CC       in heart and brain.
CC   -!- MISCELLANEOUS: The complete SAB domain is present only in the
CC       heart-specific isoforms (isoform 2 and isoform 5).
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD51365.1; Type=Erroneous initiation;
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DR   EMBL; AF152247; AAD38048.1; -; mRNA.
DR   EMBL; AF177146; AAD51365.1; ALT_INIT; mRNA.
DR   EMBL; AK173080; BAD32358.1; -; mRNA.
DR   IPI; IPI00125501; -.
DR   IPI; IPI00229294; -.
DR   IPI; IPI00229295; -.
DR   IPI; IPI00229298; -.
DR   IPI; IPI00229299; -.
DR   IPI; IPI00229300; -.
DR   IPI; IPI00406263; -.
DR   IPI; IPI00464296; -.
DR   RefSeq; NP_038841.1; NM_013813.1.
DR   UniGene; Mm.131135; -.
DR   ProteinModelPortal; Q9WV92; -.
DR   SMR; Q9WV92; 114-423.
DR   STRING; Q9WV92; -.
DR   PhosphoSite; Q9WV92; -.
DR   PRIDE; Q9WV92; -.
DR   Ensembl; ENSMUST00000024843; ENSMUSP00000024843; ENSMUSG00000024044.
DR   Ensembl; ENSMUST00000080208; ENSMUSP00000079098; ENSMUSG00000024044.
DR   Ensembl; ENSMUST00000112678; ENSMUSP00000108298; ENSMUSG00000024044.
DR   Ensembl; ENSMUST00000112679; ENSMUSP00000108299; ENSMUSG00000024044.
DR   Ensembl; ENSMUST00000112680; ENSMUSP00000108300; ENSMUSG00000024044.
DR   GeneID; 13823; -.
DR   KEGG; mmu:13823; -.
DR   UCSC; uc008dkp.1; mouse.
DR   UCSC; uc008dkq.1; mouse.
DR   UCSC; uc008dks.2; mouse.
DR   CTD; 13823; -.
DR   MGI; MGI:103008; Epb4.1l3.
DR   eggNOG; roNOG07000; -.
DR   GeneTree; ENSGT00600000084063; -.
DR   HOVERGEN; HBG007777; -.
DR   OrthoDB; EOG4Z8XVQ; -.
DR   NextBio; 284624; -.
DR   ArrayExpress; Q9WV92; -.
DR   Bgee; Q9WV92; -.
DR   CleanEx; MM_EPB4.1L3; -.
DR   Genevestigator; Q9WV92; -.
DR   GermOnline; ENSMUSG00000024044; Mus musculus.
DR   GO; GO:0005911; C:cell-cell junction; ISS:HGNC.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0019898; C:extrinsic to membrane; IEA:InterPro.
DR   GO; GO:0044224; C:juxtaparanode region of axon; IDA:BHF-UCL.
DR   GO; GO:0033270; C:paranode region of axon; IDA:BHF-UCL.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
DR   InterPro; IPR008379; Band_4.1_C.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR021187; Band_41_protein.
DR   InterPro; IPR000798; Ez/rad/moesin.
DR   InterPro; IPR014847; FERM-adjacent.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR007477; SAB.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF05902; 4_1_CTD; 1.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF04382; SAB; 1.
DR   PIRSF; PIRSF002304; Membrane_skeletal_4_1; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Actin-binding; Alternative splicing; Cytoplasm;
KW   Cytoskeleton; Phosphoprotein.
FT   CHAIN         1    929       Band 4.1-like protein 3.
FT                                /FTId=PRO_0000219400.
FT   DOMAIN      118    399       FERM.
FT   REGION      402    528       Hydrophilic.
FT   REGION      559    602       Spectrin--actin-binding.
FT   REGION      777    929       Carboxyl-terminal (CTD).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES       3      3       Phosphothreonine (By similarity).
FT   MOD_RES       5      5       Phosphoserine (By similarity).
FT   MOD_RES       7      7       Phosphoserine (By similarity).
FT   MOD_RES       9      9       Phosphoserine (By similarity).
FT   MOD_RES      11     11       Phosphoserine (By similarity).
FT   MOD_RES      96     96       Phosphoserine.
FT   MOD_RES     413    413       N6-acetyllysine (By similarity).
FT   MOD_RES     428    428       Phosphoserine.
FT   MOD_RES     451    451       Phosphoserine.
FT   MOD_RES     470    470       Phosphoserine.
FT   MOD_RES     486    486       Phosphoserine.
FT   MOD_RES     488    488       Phosphothreonine.
FT   MOD_RES     495    495       Phosphothreonine.
FT   MOD_RES     542    542       Phosphothreonine.
FT   MOD_RES     543    543       Phosphoserine.
FT   MOD_RES     547    547       Phosphoserine.
FT   MOD_RES     599    599       Phosphoserine.
FT   MOD_RES     601    601       Phosphoserine (By similarity).
FT   MOD_RES     623    623       Phosphothreonine.
FT   MOD_RES     626    626       Phosphoserine.
FT   MOD_RES     627    627       Phosphoserine.
FT   MOD_RES     797    797       Phosphoserine.
FT   MOD_RES     798    798       Phosphothreonine.
FT   MOD_RES     804    804       Phosphoserine.
FT   MOD_RES     923    923       Phosphothreonine.
FT   VAR_SEQ     455    472       Missing (in isoform 7 and isoform 8).
FT                                /FTId=VSP_000487.
FT   VAR_SEQ     528    528       K -> KSPPGHGAADSCPPSPPSAHPDPPPPTELRRRCKEK
FT                                ERAEPSSLESEAQGKAYLGDQDVAFSYRQPAGKGTTLFSFS
FT                                LQLPESFPSLLDEDGYLSFPNLSETNLLPQSWQHFLPIRSP
FT                                SLLPCFLFIFFFLLSASFSVPYALTLSFPLALCLCYLEPKA
FT                                ASLSASLDNDPSDSSEEE (in isoform 8).
FT                                /FTId=VSP_023063.
FT   VAR_SEQ     547    558       Missing (in isoform 2, isoform 3, isoform
FT                                5, isoform 6 and isoform 7).
FT                                /FTId=VSP_000490.
FT   VAR_SEQ     559    559       D -> NSLIKRIKGENVYVKHSNLMLED (in isoform
FT                                2 and isoform 5).
FT                                /FTId=VSP_000489.
FT   VAR_SEQ     623    663       Missing (in isoform 7).
FT                                /FTId=VSP_000488.
FT   VAR_SEQ     894    929       ALAQAIKEAKEQHPDMSVTKVVVHKETEITPEDGED -> E
FT                                (in isoform 4, isoform 5, isoform 6,
FT                                isoform 7 and isoform 8).
FT                                /FTId=VSP_000491.
FT   CONFLICT      6     10       GSDSE -> RIRLR (in Ref. 2; AAD51365).
FT   CONFLICT     28     28       Q -> R (in Ref. 2; AAD51365).
FT   CONFLICT    288    288       A -> V (in Ref. 2; AAD51365).
FT   CONFLICT    306    306       V -> G (in Ref. 2; AAD51365).
SQ   SEQUENCE   929 AA;  103338 MW;  F4975FF405DA44AE CRC64;
     MTTESGSDSE SKPDQEAEPQ EAAGPQGQAG AQPGPEPAGG NGSLNGEKQQ PALEQFPEAA
     AHSTPVKREI GDKDRDFAAA AAKQLEYQQF EDDKLSQRSS SSKLSRSPLK IVKRPKSMQC
     KVTLLDGSEY GCDVDKRSRG QVLFDKVCEH LNLLEKDYFG LTYRDAENQK NWLDPAKEIK
     KQIRSGAWHF SFNVKFYPPD PAQLSEDITR YYLCLQLRDD IVSGRLPCSF VTLALLGSYT
     VQSELGDYDP DECGNDYISE FRFAPNHTKE LEDKVIELHK SHRGMTPAEA EMHFLENAKK
     LSMYGVDLHH AKDSEGVEIM LGVCASGLLI YRDRLRINRF AWPKVLKISY KRNNFYIKIR
     PGEFEQFEST IGFKLPNHRA AKRLWKVCVE HHTFFRLLLP EAPPKKFLTL GSKFRYSGRT
     QAQTRRASAL IDRPAPYFER SSSKRYTMSR SLDGASVSEN HEIYMKDSVS AAEVGTGQYA
     TTKGISQTNL ITTVTPEKKA EEERVEEEDR RKKAEEATPV TALRHEGKTD SERTDTAADG
     ETSATESDQE EDAEIKAQDL DKTQDELMKH QTNISELKRT FLETSTETAL TNEWEKRLST
     SPVRLAARQE DAPMIEPLVP EETKQSSGEK LMDGSEILSL LESARKPTEF IGGVSSTTQS
     WVQKLETKTE PVEAEVESTP HPQPLSTEKV LQETILVEER HVMSVHASGD ASHTARDEVD
     AAESTPTDRR HTGKGKEGSS VTEAAKEQRG EEVDQSAPEQ EQPATVSHEE EQASTIRTSE
     GLEQKSHFES STVRVESTSV GSISPGGAKL EISTKEVPVV HTETKTITYE SSQVDPGADL
     EPGVLMSAQT ITSETTSTTT TTHITKTVKG GISETRIEKR IVITGDADID HDQALAQAIK
     EAKEQHPDMS VTKVVVHKET EITPEDGED
//
ID   TIM8A_MOUSE             Reviewed;          97 AA.
AC   Q9WVA2; Q542E5;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit Tim8 A;
DE   AltName: Full=Deafness dystonia protein 1 homolog;
GN   Name=Timm8a1; Synonyms=Ddp1, Tim8a, Timm8a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=20079101; PubMed=10611480; DOI=10.1016/S0014-5793(99)01665-8;
RA   Bauer M.F., Rothbauer U., Muehlenbein N., Smith R.J.H., Gerbitz K.-D.,
RA   Neupert W., Brunner M., Hofmann S.;
RT   "The mitochondrial TIM22 preprotein translocase is highly conserved
RT   throughout the eukaryotic kingdom.";
RL   FEBS Lett. 464:41-47(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Adipocyte;
RX   PubMed=10873677; DOI=10.1006/bbrc.2000.3004;
RA   Nakane T., Inada Y., Ito F., Itoh N., Tazawa S., Chiba S.;
RT   "Cloning and expression of mouse deafness dystonia peptide 1 cDNA.";
RL   Biochem. Biophys. Res. Commun. 273:759-764(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Submandibular gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and Czech II; TISSUE=Mammary gland, and Thymus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=15254020; DOI=10.1093/hmg/ddh217;
RA   Roesch K., Hynds P.J., Varga R., Tranebjaerg L., Koehler C.M.;
RT   "The calcium-binding aspartate/glutamate carriers, citrin and aralar1,
RT   are new substrates for the DDP1/TIMM8a-TIMM13 complex.";
RL   Hum. Mol. Genet. 13:2101-2111(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Mitochondrial intermembrane chaperone that participates
CC       in the import and insertion of some multi-pass transmembrane
CC       proteins into the mitochondrial inner membrane. Also required for
CC       the transfer of beta-barrel precursors from the TOM complex to the
CC       sorting and assembly machinery (SAM complex) of the outer
CC       membrane. Acts as a chaperone-like protein that protects the
CC       hydrophobic precursors from aggregation and guide them through the
CC       mitochondrial intermembrane space. The TIMM8-TIMM13 complex
CC       mediates the import of proteins such as TIMM23, SLC25A12/ARALAR1
CC       and SLC25A13/ARALAR2, while the predominant TIMM9-TIMM10 70 kDa
CC       complex mediates the import of much more proteins (By similarity).
CC   -!- SUBUNIT: Heterohexamer; composed of 3 copies of TIMM8A and 3
CC       copies of TIMM13, named soluble 70 kDa complex. Associates with
CC       the TIM22 complex, whose core is composed of TIMM22 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
CC       membrane protein; Intermembrane side (By similarity).
CC   -!- TISSUE SPECIFICITY: Present at high level in liver and brain, and
CC       at lower level in muscle and heart. In CNS sections, it is
CC       predominantly present in the soma and the dendritic portion of the
CC       Purkinje cells of the cerebellum, but not in the glial cells.
CC       Scattered expression also is also detected in the brain stem,
CC       olfactory bulb, substantia nigra, hippocampus and striatum (at
CC       protein level). Ubiquitously expressed.
CC   -!- DOMAIN: The twin CX3C motif contains 4 conserved Cys residues that
CC       form 2 disulfide bonds in the mitochondrial intermembrane space.
CC       However, during the transit of TIMM8A from cytoplasm into
CC       mitochondrion, the Cys residues probably coordinate zinc, thereby
CC       preventing folding and allowing its transfer across mitochondrial
CC       outer membrane (By similarity).
CC   -!- SIMILARITY: Belongs to the small Tim family.
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DR   EMBL; AF150081; AAD39988.1; -; mRNA.
DR   EMBL; AB031055; BAA90770.1; -; mRNA.
DR   EMBL; AK011402; BAB27594.1; -; mRNA.
DR   EMBL; AK088903; BAC40644.1; -; mRNA.
DR   EMBL; AK090079; BAC41082.1; -; mRNA.
DR   EMBL; AK165573; BAE38265.1; -; mRNA.
DR   EMBL; BC004796; AAH04796.1; -; mRNA.
DR   EMBL; BC094631; AAH94631.1; -; mRNA.
DR   IPI; IPI00125776; -.
DR   PIR; JC7322; JC7322.
DR   RefSeq; NP_038926.1; NM_013898.2.
DR   UniGene; Mm.214504; -.
DR   UniGene; Mm.391835; -.
DR   ProteinModelPortal; Q9WVA2; -.
DR   SMR; Q9WVA2; 28-83.
DR   STRING; Q9WVA2; -.
DR   PhosphoSite; Q9WVA2; -.
DR   PRIDE; Q9WVA2; -.
DR   Ensembl; ENSMUST00000052902; ENSMUSP00000049749; ENSMUSG00000045455.
DR   Ensembl; ENSMUST00000054213; ENSMUSP00000050156; ENSMUSG00000048007.
DR   GeneID; 30058; -.
DR   KEGG; mmu:30058; -.
DR   UCSC; uc009ugd.1; mouse.
DR   CTD; 30058; -.
DR   MGI; MGI:1353433; Timm8a1.
DR   eggNOG; roNOG16537; -.
DR   GeneTree; ENSGT00390000016102; -.
DR   HOGENOM; HBG603145; -.
DR   HOVERGEN; HBG060492; -.
DR   InParanoid; Q9WVA2; -.
DR   OMA; DSRAETC; -.
DR   OrthoDB; EOG408N9N; -.
DR   PhylomeDB; Q9WVA2; -.
DR   NextBio; 446245; -.
DR   ArrayExpress; Q9WVA2; -.
DR   Bgee; Q9WVA2; -.
DR   Genevestigator; Q9WVA2; -.
DR   GermOnline; ENSMUSG00000045455; Mus musculus.
DR   GermOnline; ENSMUSG00000048007; Mus musculus.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042719; C:mitochondrial intermembrane space protein transporter complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045039; P:protein import into mitochondrial inner membrane; IEA:InterPro.
DR   GO; GO:0055085; P:transmembrane transport; IEA:UniProtKB-KW.
DR   InterPro; IPR004217; Tim8/9/10/13_Znf-like.
DR   Pfam; PF02953; zf-Tim10_DDP; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Chaperone; Disulfide bond; Membrane; Metal-binding;
KW   Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW   Protein transport; Translocation; Transport; Zinc.
FT   CHAIN         1     97       Mitochondrial import inner membrane
FT                                translocase subunit Tim8 A.
FT                                /FTId=PRO_0000193585.
FT   MOTIF        43     66       Twin CX3C motif.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      94     94       Phosphoserine.
FT   DISULFID     43     66       By similarity.
FT   DISULFID     47     62       By similarity.
SQ   SEQUENCE   97 AA;  11042 MW;  16C23D7C351BDF00 CRC64;
     MESSTSSSGS ALGAVDPQLQ HFIEVETQKQ RFQQLVHQMT ELCWEKCMDK PGPKLDSRAE
     ACFVNCVERF IDTSQFILNR LEQTQKSKPV FSESLSD
//
ID   BUB3_MOUSE              Reviewed;         326 AA.
AC   Q9WVA3; P97397;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Mitotic checkpoint protein BUB3;
DE   AltName: Full=WD repeat type I transmembrane protein A72.5;
GN   Name=Bub3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RX   MEDLINE=99342046; PubMed=10411903; DOI=10.1073/pnas.96.15.8493;
RA   Martinez-Exposito M.J., Kaplan K.B., Copeland J., Sorger P.K.;
RT   "Retention of the BUB3 checkpoint protein on lagging chromosomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:8493-8498(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X 129/Sv; TISSUE=Bone marrow;
RA   Downs A., Xie X., Yan W., Li J., Palacios R.;
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=19888327; DOI=10.1371/journal.pone.0007701;
RA   Li M., Li S., Yuan J., Wang Z.B., Sun S.C., Schatten H., Sun Q.Y.;
RT   "Bub3 is a spindle assembly checkpoint protein regulating chromosome
RT   segregation during mouse oocyte meiosis.";
RL   PLoS ONE 4:E7701-E7701(2009).
CC   -!- FUNCTION: Has a dual function in spindle-assembly checkpoint
CC       signaling and in promoting the establishment of correct
CC       kinetochore-microtubule (K-MT) attachments. Promotes the formation
CC       of stable end-on bipolar attachments. Necessary for kinetochore
CC       localization of BUB1. The BUB1/BUB3 complex plays a role in the
CC       inhibition of anaphase-promoting complex or cyclosome (APC/C) when
CC       spindle-assembly checkpoint is activated and inhibits the
CC       ubiquitin ligase activity of APC/C by phosphorylating its
CC       activator CDC20. This complex can also phosphorylate MAD1L1 (By
CC       similarity). Regulates chromosome segregation during oocyte
CC       meiosis.
CC   -!- SUBUNIT: Interacts with BUB1 and BUBR1. The BUB1/BUB3 complex
CC       interacts with MAD1L1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Chromosome,
CC       centromere, kinetochore. Note=Starts to localize at kinetochores
CC       in prometaphase I (Pro-MI) stage and maintains the localization
CC       until the metaphase I-anaphase I (MI-AI) transition (By
CC       similarity).
CC   -!- SIMILARITY: Contains 5 WD repeats.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB39606.1; Type=Frameshift; Positions=73, 270, 274;
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DR   EMBL; AF149822; AAD38038.1; -; mRNA.
DR   EMBL; U67327; AAB39606.1; ALT_FRAME; mRNA.
DR   IPI; IPI00626752; -.
DR   UniGene; Mm.441749; -.
DR   UniGene; Mm.927; -.
DR   ProteinModelPortal; Q9WVA3; -.
DR   SMR; Q9WVA3; 5-324.
DR   IntAct; Q9WVA3; 1.
DR   STRING; Q9WVA3; -.
DR   PhosphoSite; Q9WVA3; -.
DR   REPRODUCTION-2DPAGE; Q9WVA3; -.
DR   PRIDE; Q9WVA3; -.
DR   Ensembl; ENSMUST00000084502; ENSMUSP00000081547; ENSMUSG00000066979.
DR   MGI; MGI:1343463; Bub3.
DR   eggNOG; roNOG05653; -.
DR   GeneTree; ENSGT00530000063440; -.
DR   HOGENOM; HBG315851; -.
DR   HOVERGEN; HBG002942; -.
DR   InParanoid; Q9WVA3; -.
DR   OrthoDB; EOG4R7VB2; -.
DR   PhylomeDB; Q9WVA3; -.
DR   ArrayExpress; Q9WVA3; -.
DR   Bgee; Q9WVA3; -.
DR   Genevestigator; Q9WVA3; -.
DR   GermOnline; ENSMUSG00000066979; Mus musculus.
DR   GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007126; P:meiosis; IEA:UniProtKB-KW.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:MGI.
DR   GO; GO:0051983; P:regulation of chromosome segregation; IDA:UniProtKB.
DR   GO; GO:0071173; P:spindle assembly checkpoint; IDA:UniProtKB.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 4.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell cycle; Cell division; Centromere; Chromosome;
KW   Chromosome partition; Isopeptide bond; Kinetochore; Meiosis; Mitosis;
KW   Nucleus; Phosphoprotein; Repeat; Ubl conjugation; WD repeat.
FT   CHAIN         1    326       Mitotic checkpoint protein BUB3.
FT                                /FTId=PRO_0000050892.
FT   REPEAT        5     43       WD 1.
FT   REPEAT       46     83       WD 2.
FT   REPEAT       86    124       WD 3.
FT   REPEAT      128    163       WD 4.
FT   REPEAT      223    262       WD 5.
FT   MOD_RES     179    179       N6-acetyllysine (By similarity).
FT   MOD_RES     211    211       Phosphoserine (By similarity).
FT   CROSSLNK    216    216       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
FT   CONFLICT     62     62       C -> W (in Ref. 2; AAB39606).
FT   CONFLICT    156    156       G -> A (in Ref. 2; AAB39606).
FT   CONFLICT    165    165       W -> R (in Ref. 2; AAB39606).
SQ   SEQUENCE   326 AA;  36985 MW;  F5B80510B82A1342 CRC64;
     MTGSNEFKLN QPPEDGISSV KFSPNTSQFL LVSSWDTSVR LYDVPANSMR LKYQHTGAVL
     DCAFYDPTHA WSGGLDHQLK MHDLNTDQEN LVGTHDAPIR CVEYCPEVNV MVTGSWDQTV
     KLWDPRTPCN AGTFSQPEKV YTLSVSGDRL IVGTAGRRVL VWDLWNMGYV QQRRESSLKY
     QTRCIRAFPN KQGYVLSSIE GRVAVEYLDP SPEVQKKKYA FKCHRLKENN IEQIYPVNAI
     SFHNIHNTFA TGGSDGFVNI WDPFNKKRLC QFHRYPTSIA SLAFSNDGTT LAIASSYMYE
     MDDTEHPEDG IFIRQVTDAE TKPKST
//
ID   CAV2_MOUSE              Reviewed;         162 AA.
AC   Q9WVC3; Q3TYR4;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Caveolin-2;
GN   Name=Cav2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=3T3-L1;
RX   MEDLINE=99303643; PubMed=10373486; DOI=10.1074/jbc.274.26.18721;
RA   Das K., Lewis R.Y., Scherer P.E., Lisanti M.P.;
RT   "The membrane-spanning domains of caveolins-1 and -2 mediate the
RT   formation of caveolin hetero-oligomers. Implications for the assembly
RT   of caveolae membranes in vivo.";
RL   J. Biol. Chem. 274:18721-18728(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Kogo H., Ishiguro K., Kuwaki S., Fujimoto T.;
RT   "Identification of mouse caveolin-2 mRNA variant.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Inner ear, Lung, and Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION AT TYR-19.
RX   MEDLINE=22206546; PubMed=12091389; DOI=10.1074/jbc.M204367200;
RA   Lee H., Park D.S., Wang X.B., Scherer P.E., Schwartz P.E.,
RA   Lisanti M.P.;
RT   "Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-
RT   caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains
RT   associated with lipid rafts/caveolae, but no longer forms a high
RT   molecular mass hetero-oligomer with caveolin-1.";
RL   J. Biol. Chem. 277:34556-34567(2002).
CC   -!- FUNCTION: May act as a scaffolding protein within caveolar
CC       membranes. Interacts directly with G-protein alpha subunits and
CC       can functionally regulate their activity. Acts as an accessory
CC       protein in conjunction with CAV1 in targeting to lipid rafts and
CC       driving caveolae formation. The Ser-36 phosphorylated form has a
CC       role in modulating mitosis in endothelial cells. Positive
CC       regulator of cellular mitogenesis of the MAPK signaling pathway.
CC       Required for the insulin-stimulated nuclear translocation and
CC       activation of MAPK1 and STAT3, and the subsequent regulation of
CC       cell cycle progression (By similarity). May be involved in
CC       synaptic transduction in the retina.
CC   -!- SUBUNIT: Monomer or homodimer. Interacts with CAV1; the
CC       interaction forms a stable heterooligomeric complex that is
CC       required for targeting to lipid rafts and for caveolae formation.
CC       Tyrosine phosphorylated forms do not form heterooligomers with the
CC       Tyr-19-phosphorylated form existing as a monomer or dimer, and the
CC       Tyr-27-form as a monomer only. Interacts (tyrosine phosphorylated
CC       form) with the SH2 domain-containing proteins, RASA1, NCK1 and
CC       SRC. Interacts (tyrosine phosphorylated form) with INSR, the
CC       interaction (Tyr-27-phosphorylated form) is increased on insulin
CC       stimulation. Interacts (Tyr-19 phosphorylated form) with MAPK1
CC       (phosphorylated form); the interaction, promoted by insulin, leads
CC       to nuclear location and MAPK1 activation. Interacts with STAT3;
CC       the interaction is increased on insulin-induced tyrosine
CC       phosphorylation leading to STAT activation (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Golgi apparatus
CC       membrane; Peripheral membrane protein. Cell membrane; Peripheral
CC       membrane protein. Membrane, caveola; Peripheral membrane protein.
CC       Note=Potential hairpin-like structure in the membrane. Membrane
CC       protein of caveolae. Tyr-19-phosphorylated form is enriched at
CC       sites of cell-cell contact and is translocated to the nucleus in
CC       complex with MAPK1 in response to insulin. Tyr-27-phosphorylated
CC       form is located both in the cytoplasm and plasma membrane. CAV1-
CC       mediated Ser-23-phosphorylated form locates to the plasma
CC       membrane. Ser-36-phosphorylated form resides in intracellular
CC       compartments (By similarity).
CC   -!- PTM: Phosphorylated on serine and tyrosine residues. CAV1 promotes
CC       phosphorylation on Ser-23 which then targets the complex to the
CC       plasma membrane, lipid rafts and caveolae. Phosphorylation on Ser-
CC       36 appears to modulate mitosis in endothelial cells.
CC       Phosphorylation on both Tyr-19 and Tyr-27 is required for insulin-
CC       induced 'Ser-727' phosphorylation of STAT3 and its activation.
CC       Phosphorylation on Tyr-19 is required for insulin-induced
CC       phosphorylation of MAPK1 and DNA binding of STAT3. Tyrosine
CC       phosphorylation is induced by both EGF and insulin (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the caveolin family.
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DR   EMBL; AF141322; AAD42349.1; -; mRNA.
DR   EMBL; AB049604; BAB61728.1; -; mRNA.
DR   EMBL; AK004663; BAB23453.1; -; mRNA.
DR   EMBL; AK009913; BAB26582.1; -; mRNA.
DR   EMBL; AK151397; BAE30365.1; -; mRNA.
DR   EMBL; AK158419; BAE34498.1; -; mRNA.
DR   EMBL; BC023095; AAH23095.1; -; mRNA.
DR   IPI; IPI00125832; -.
DR   RefSeq; NP_058596.1; NM_016900.3.
DR   UniGene; Mm.396075; -.
DR   STRING; Q9WVC3; -.
DR   PhosphoSite; Q9WVC3; -.
DR   PRIDE; Q9WVC3; -.
DR   Ensembl; ENSMUST00000000058; ENSMUSP00000000058; ENSMUSG00000000058.
DR   GeneID; 12390; -.
DR   KEGG; mmu:12390; -.
DR   UCSC; uc009azn.1; mouse.
DR   CTD; 12390; -.
DR   MGI; MGI:107571; Cav2.
DR   eggNOG; roNOG17237; -.
DR   GeneTree; ENSGT00390000014924; -.
DR   HOGENOM; HBG443750; -.
DR   HOVERGEN; HBG003422; -.
DR   InParanoid; Q9WVC3; -.
DR   OMA; THSFDKV; -.
DR   OrthoDB; EOG4PRSRW; -.
DR   PhylomeDB; Q9WVC3; -.
DR   NextBio; 281126; -.
DR   ArrayExpress; Q9WVC3; -.
DR   Bgee; Q9WVC3; -.
DR   CleanEx; MM_CAV2; -.
DR   Genevestigator; Q9WVC3; -.
DR   GermOnline; ENSMUSG00000000058; Mus musculus.
DR   GO; GO:0005901; C:caveola; ISS:UniProtKB.
DR   GO; GO:0031234; C:extrinsic to internal side of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0031748; F:D1 dopamine receptor binding; ISS:UniProtKB.
DR   GO; GO:0070836; P:caveola assembly; ISS:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; TAS:MGI.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; IMP:MGI.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR   GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IMP:MGI.
DR   GO; GO:0060161; P:positive regulation of dopamine receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0051259; P:protein oligomerization; IDA:MGI.
DR   GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI.
DR   GO; GO:0048278; P:vesicle docking; ISS:UniProtKB.
DR   GO; GO:0006906; P:vesicle fusion; ISS:UniProtKB.
DR   InterPro; IPR001612; Caveolin.
DR   InterPro; IPR018361; Caveolin_CS.
DR   PANTHER; PTHR10844; Caveolin; 1.
DR   Pfam; PF01146; Caveolin; 1.
DR   PROSITE; PS01210; CAVEOLIN; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cytoplasm; Golgi apparatus; Membrane; Nucleus;
KW   Phosphoprotein.
FT   CHAIN         1    162       Caveolin-2.
FT                                /FTId=PRO_0000144138.
FT   TOPO_DOM      1     86       Cytoplasmic (Potential).
FT   INTRAMEM     87    107       Helical; (Potential).
FT   TOPO_DOM    108    162       Cytoplasmic (Potential).
FT   MOD_RES      19     19       Phosphotyrosine; by SRC.
FT   MOD_RES      20     20       Phosphoserine (By similarity).
FT   MOD_RES      23     23       Phosphoserine (By similarity).
FT   MOD_RES      27     27       Phosphotyrosine; by SRC (By similarity).
FT   MOD_RES      36     36       Phosphoserine (By similarity).
SQ   SEQUENCE   162 AA;  18227 MW;  9E2E272FEC169458 CRC64;
     MGLETEKADV QLFMADDAYS HHSGVDYADP EKYVDSSHDR DPHQLNSHLK LGFEDLIAEP
     ETTHSFDKVW ICSHALFEIS KYVMYKFLTV FLAIPLAFIA GILFATLSCL HIWILMPFVK
     TCLMVLPSVQ TIWKSVTDVV IGPLCTSVGR SFSSVSMQLS HD
//
ID   TUSC2_MOUSE             Reviewed;         110 AA.
AC   Q9WVF8;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 60.
DE   RecName: Full=Tumor suppressor candidate 2;
DE   AltName: Full=Fusion 1 protein;
DE            Short=Fus-1 protein;
DE   AltName: Full=PDGFA-associated protein 2;
GN   Name=Tusc2; Synonyms=Fus1, Lgcc, Pdap2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Duh F.-M., Minna J.D., Lerman M.I.;
RT   "Mouse ortholog of the human Fus1 gene.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- PTM: Myristoylation is required for tumor suppressor activity (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the TUSC2 family.
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DR   EMBL; AF123387; AAD42286.1; -; mRNA.
DR   EMBL; BC048477; AAH48477.1; -; mRNA.
DR   IPI; IPI00125917; -.
DR   RefSeq; NP_062716.1; NM_019742.4.
DR   UniGene; Mm.476802; -.
DR   STRING; Q9WVF8; -.
DR   PhosphoSite; Q9WVF8; -.
DR   PRIDE; Q9WVF8; -.
DR   Ensembl; ENSMUST00000010198; ENSMUSP00000010198; ENSMUSG00000010054.
DR   GeneID; 80385; -.
DR   KEGG; mmu:80385; -.
DR   UCSC; uc009rls.1; mouse.
DR   CTD; 80385; -.
DR   MGI; MGI:1931086; Tusc2.
DR   GeneTree; ENSGT00390000008040; -.
DR   HOGENOM; HBG384386; -.
DR   HOVERGEN; HBG054202; -.
DR   InParanoid; Q9WVF8; -.
DR   OMA; TRRGSMY; -.
DR   OrthoDB; EOG454915; -.
DR   PhylomeDB; Q9WVF8; -.
DR   NextBio; 350029; -.
DR   Bgee; Q9WVF8; -.
DR   CleanEx; MM_TUSC2; -.
DR   Genevestigator; Q9WVF8; -.
DR   GermOnline; ENSMUSG00000010054; Mus musculus.
PE   1: Evidence at protein level;
KW   Lipoprotein; Myristate; Phosphoprotein.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    110       Tumor suppressor candidate 2.
FT                                /FTId=PRO_0000148171.
FT   MOD_RES      50     50       Phosphoserine.
FT   LIPID         2      2       N-myristoyl glycine (By similarity).
SQ   SEQUENCE   110 AA;  12136 MW;  310698A5CB12DC40 CRC64;
     MGASGSKARG LWPFASTPGG GGPEAAGSEQ SLVRSRARAV PPFVFTRRGS MFYDEDGDLA
     HEFYEETIVT KNGQKRAKLR RVHKNLIPQG IVKLDPPRIH VDFPVILYEV
//
ID   Q9WVH4_MOUSE            Unreviewed;       672 AA.
AC   Q9WVH4;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 93.
DE   SubName: Full=Forkhead box O3a;
DE   SubName: Full=Forkhead protein FKHR2;
GN   Name=Foxo3; Synonyms=Fkhr2, Foxo3a; ORFNames=mCG_18802;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=21251166; PubMed=11353388; DOI=10.1007/s003350020002;
RA   Biggs W.H. III, Cavenee W.K., Arden K.C.;
RT   "Identification and characterization of members of the FKHR (FOX O)
RT   subclass of winged-helix transcription factors in the mouse.";
RL   Mamm. Genome 12:416-425(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [11]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Contains 1 fork-head DNA-binding domain.
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DR   EMBL; AF114259; AAD42107.1; -; mRNA.
DR   EMBL; AK047413; BAC33049.1; -; mRNA.
DR   EMBL; CH466540; EDL04998.1; -; Genomic_DNA.
DR   IPI; IPI00125980; -.
DR   RefSeq; NP_062714.1; NM_019740.2.
DR   UniGene; Mm.338613; -.
DR   UniGene; Mm.391700; -.
DR   UniGene; Mm.417859; -.
DR   UniGene; Mm.466459; -.
DR   HSSP; P98177; 1E17.
DR   ProteinModelPortal; Q9WVH4; -.
DR   SMR; Q9WVH4; 157-252.
DR   STRING; Q9WVH4; -.
DR   PhosphoSite; Q9WVH4; -.
DR   PRIDE; Q9WVH4; -.
DR   Ensembl; ENSMUST00000056974; ENSMUSP00000050683; ENSMUSG00000048756.
DR   Ensembl; ENSMUST00000105502; ENSMUSP00000101141; ENSMUSG00000048756.
DR   GeneID; 56484; -.
DR   KEGG; mmu:56484; -.
DR   UCSC; uc007eyl.1; mouse.
DR   CTD; 56484; -.
DR   MGI; MGI:1890081; Foxo3.
DR   GeneTree; ENSGT00390000000589; -.
DR   HOGENOM; HBG714085; -.
DR   HOVERGEN; HBG057789; -.
DR   InParanoid; Q9WVH4; -.
DR   OMA; RSDPMMS; -.
DR   PhylomeDB; Q9WVH4; -.
DR   NextBio; 312750; -.
DR   ArrayExpress; Q9WVH4; -.
DR   Bgee; Q9WVH4; -.
DR   Genevestigator; Q9WVH4; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0016563; F:transcription activator activity; IDA:MGI.
DR   GO; GO:0001547; P:antral ovarian follicle growth; IMP:MGI.
DR   GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IDA:MGI.
DR   GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
DR   GO; GO:0006917; P:induction of apoptosis; IMP:MGI.
DR   GO; GO:0001544; P:initiation of primordial ovarian follicle growth; IMP:MGI.
DR   GO; GO:0001556; P:oocyte maturation; IMP:MGI.
DR   GO; GO:0001542; P:ovulation from ovarian follicle; IMP:MGI.
DR   InterPro; IPR001766; TF_fork_head.
DR   InterPro; IPR018122; TF_fork_head_CS.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   PANTHER; PTHR11829; Fork_box_protein; 1.
DR   Pfam; PF00250; Fork_head; 1.
DR   PRINTS; PR00053; FORKHEAD.
DR   SMART; SM00339; FH; 1.
DR   PROSITE; PS00658; FORK_HEAD_2; 1.
DR   PROSITE; PS50039; FORK_HEAD_3; 1.
PE   2: Evidence at transcript level;
KW   DNA-binding; Nucleus; Transcription; Transcription regulation.
SQ   SEQUENCE   672 AA;  71064 MW;  EC218D9BA0C1DAC5 CRC64;
     MAEAPASPVP LSPLEVELDP EFEPQSRPRS CTWPLQRPEL QASPAKPSGE TAADSMIPEE
     DDDEDDEDGG GRASSAMVIG GGVSSTLGSG LLLEDSAMLL APGGQDLGSG PASAAGALSG
     GTPTQLQPQQ PLPQPQPGAA GGSGQPRKCS SRRNAWGNLS YADLITRAIE SSPDKRLTLS
     QIYEWMVRCV PYFKDKGDSN SSAGWKNSIR HNLSLHSRFM RVQNEGTGKS SWWIINPDGG
     KSGKAPRRRA VSMDNSNKYT KSRGRAAKKK AALQAAPESA DDSPSQLSKW PGSPTSRSSD
     ELDAWTDFRS RTNSNASTVS GRLSPILAST ELDDVQDDDG PLSPMLYSSS ASLSPSVSKP
     CTVELPRLTD MAGTMNLNDG LAENLMDDLL DNIALPPSQP SPPGGLMQRG SSFPYTAKSS
     GLGSPTGSFN STVFGPSSLN SLRQSPMQTI QENRPATFSS VSHYGNQTLQ DLLASDSLSH
     SDVMMTQSDP LMSQASTAVS AQNARRNVML RNDPMMSFAA QPTQGSLVNQ NLLHHQHQTQ
     GALGGSRALS NSVSNMGLSD SSSLGSAKHQ QQSPASQSMQ TLSDSLSGSS LYSASANLPV
     MGHDKFPSDL DLDMFNGSLE CDMESIIRSE LMDADGLDFN FDSLISTQNV VGLNVGNFTG
     AKQASSQSWV PG
//
ID   JIP1_MOUSE              Reviewed;         707 AA.
AC   Q9WVI9; O35145; Q925J8; Q9R1H9; Q9R1Z1; Q9WVI7; Q9WVI8;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   05-DEC-2001, sequence version 2.
DT   08-MAR-2011, entry version 109.
DE   RecName: Full=C-Jun-amino-terminal kinase-interacting protein 1;
DE            Short=JIP-1;
DE            Short=JNK-interacting protein 1;
DE   AltName: Full=Islet-brain-1;
DE            Short=IB-1;
DE   AltName: Full=JNK MAP kinase scaffold protein 1;
DE   AltName: Full=Mitogen-activated protein kinase 8-interacting protein 1;
GN   Name=Mapk8ip1; Synonyms=Ib1, Jip1, Mapk8ip, Prkm8ip;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM JIP-1A), AND POSSIBLE FUNCTION.
RC   TISSUE=Brain;
RX   MEDLINE=97382313; PubMed=9235893; DOI=10.1126/science.277.5326.693;
RA   Dickens M., Rogers J.S., Cavanagh J., Raitano A., Xia Z.,
RA   Halpern J.R., Greenberg M.E., Sawyers C.L., Davis R.J.;
RT   "A cytoplasmic inhibitor of the JNK signal transduction pathway.";
RL   Science 277:693-696(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS JIP-1B; JIP-1C; JIP-1D AND
RP   JIP-1E).
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=99196470; PubMed=10098834;
RX   DOI=10.1046/j.1471-4159.1999.721335.x;
RA   Kim I.-J., Lee K.-W., Park B.Y., Lee J.-K., Park J., Choi I.Y.,
RA   Eom S.-J., Chang T.-S., Kim M.J., Yeom Y.I., Chang S.K., Lee Y.-D.,
RA   Choi E.-J., Han P.-L.;
RT   "Molecular cloning of multiple splicing variants of JIP-1
RT   preferentially expressed in brain.";
RL   J. Neurochem. 72:1335-1343(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM JIP-1B), AND CHARACTERIZATION.
RC   TISSUE=Brain;
RX   MEDLINE=99422004; PubMed=10490659;
RA   Yasuda J., Whitmarsh A.J., Cavanagh J., Sharma M., Davis R.J.;
RT   "The JIP group of mitogen-activated protein kinase scaffold
RT   proteins.";
RL   Mol. Cell. Biol. 19:7245-7254(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM JIP-1B), AND VARIANT ARG-10.
RC   STRAIN=ILS, and ISS;
RX   MEDLINE=21363810; PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM JIP-1B).
RC   TISSUE=Brain;
RX   MEDLINE=22028091; PubMed=11912189; DOI=10.1074/jbc.M108372200;
RA   Taru H., Iijima K., Hase M., Kirino Y., Yagi Y., Suzuki T.;
RT   "Interaction of Alzheimer's beta-amyloid precursor family proteins
RT   with scaffold proteins of the JNK signaling cascade.";
RL   J. Biol. Chem. 277:20070-20078(2002).
RN   [6]
RP   INTERACTION WITH RGNEF, AND SUBCELLULAR LOCATION.
RX   MEDLINE=20044776; PubMed=10574993; DOI=10.1074/jbc.274.49.35113;
RA   Meyer D., Liu A., Margolis B.;
RT   "Interaction of c-Jun amino-terminal kinase interacting protein-1 with
RT   p190 rhoGEF and its localization in differentiated neurons.";
RL   J. Biol. Chem. 274:35113-35118(1999).
RN   [7]
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   MEDLINE=20177638; PubMed=10712642;
RX   DOI=10.1046/j.1460-9568.2000.00945.x;
RA   Pellet J.-B., Haefliger J.-A., Staple J.K., Widmann C., Welker E.,
RA   Hirling H., Bonny C., Nicod P., Catsicas S., Waeber G., Riederer B.M.;
RT   "Spatial, temporal and subcellular localization of islet-brain 1
RT   (IB1), a homologue of JIP-1, in mouse brain.";
RL   Eur. J. Neurosci. 12:621-632(2000).
RN   [8]
RP   INTERACTION WITH LRPS.
RX   MEDLINE=20400498; PubMed=10827173; DOI=10.1074/jbc.M000955200;
RA   Gotthardt M., Trommsdorff M., Nevitt M.F., Shelton J.,
RA   Richardson J.A., Stockinger W., Nimpf J., Herz J.;
RT   "Interactions of the low density lipoprotein receptor gene family with
RT   cytosolic adaptor and scaffold proteins suggest diverse biological
RT   functions in cellular communication and signal transduction.";
RL   J. Biol. Chem. 275:25616-25624(2000).
RN   [9]
RP   INTERACTION WITH KLC1.
RC   TISSUE=Brain;
RX   MEDLINE=21135887; PubMed=11238452; DOI=10.1083/jcb.152.5.959;
RA   Verhey K.J., Meyer D., Deehan R., Blenis J., Schnapp B.J.,
RA   Rapoport T.A., Margolis B.;
RT   "Cargo of kinesin identified as JIP scaffolding proteins and
RT   associated signaling molecules.";
RL   J. Cell Biol. 152:959-970(2001).
RN   [10]
RP   FUNCTION.
RX   MEDLINE=21446505; PubMed=11562351; DOI=10.1101/gad.922801;
RA   Whitmarsh A.J., Kuan C.-Y., Kennedy N.J., Kelkar N., Haydar T.F.,
RA   Mordes J.P., Appel M., Rossini A.A., Jones S.N., Flavell R.A.,
RA   Rakic P., Davis R.J.;
RT   "Requirement of the JIP1 scaffold protein for stress-induced JNK
RT   activation.";
RL   Genes Dev. 15:2421-2432(2001).
CC   -!- FUNCTION: The JNK-interacting protein (JIP) group of scaffold
CC       proteins selectively mediates JNK signaling by aggregating
CC       specific components of the MAPK cascade to form a functional JNK
CC       signaling module. Required for JNK activation in response to
CC       excitotoxic stress. Cytoplasmic MAPK8IP1 causes inhibition of JNK-
CC       regulated activity by retaining JNK in the cytoplasm and thus
CC       inhibiting the JNK phosphorylation of c-Jun. May also participate
CC       in ApoER2-specific reelin signaling. Directly, or indirectly,
CC       regulates GLUT2 gene expression and beta-cell function. Appears to
CC       have a role in cell signaling in mature and developing nerve
CC       terminals. May function as a regulator of vesicle transport,
CC       through interations with the JNK-signaling components and motor
CC       proteins. Functions as an anti-apoptotic protein and whose level
CC       seems to influence the beta-cell death or survival response (By
CC       similarity).
CC   -!- SUBUNIT: Forms homo- or heterooligomeric complexes. Binds specific
CC       components of the JNK signaling pathway namely MAPK8, MAPK9,
CC       MAPK10, MAP2K7, MAP3K10, MAP3K11 and DLK1. Also binds the proline-
CC       rich domain-containing splice variant of apolipoprotein E receptor
CC       2 (ApoER2) (By similarity). Binds the cytoplasmic tails of LRP1
CC       and LRP2 (Megalin). Binds the TPR motif-containing C-terminal of
CC       kinesin light chain, KLC1. Pre-assembled MAPK8IP1 scaffolding
CC       complexes are then transported as a cargo of kinesin, to the
CC       required subcellular location. Interacts with the cytoplasmic
CC       domain of APP (By similarity). Interacts, via the PID domain, with
CC       RGNEF.
CC   -!- INTERACTION:
CC       P12023:App; NbExp=2; IntAct=EBI-74515, EBI-78814;
CC       P14599:Appl (xeno); NbExp=1; IntAct=EBI-74515, EBI-74135;
CC       P92208:bsk (xeno); NbExp=1; IntAct=EBI-74515, EBI-74487;
CC       Q91ZX7:Lrp1; NbExp=1; IntAct=EBI-74515, EBI-300955;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       perinuclear region (By similarity). Nucleus (By similarity).
CC       Note=Accumulates in cell surface projections. Under certain stress
CC       conditions, translocates to the perinuclear region of neurons. In
CC       insulin-secreting cells, detected in both the cytoplasm and
CC       nucleus (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=JIP-1b;
CC         IsoId=Q9WVI9-1; Sequence=Displayed;
CC       Name=JIP-1a; Synonyms=1;
CC         IsoId=Q9WVI9-2; Sequence=VSP_002766;
CC       Name=JIP-1c; Synonyms=2a;
CC         IsoId=Q9WVI9-3; Sequence=VSP_002763;
CC       Name=JIP-1d; Synonyms=2B;
CC         IsoId=Q9WVI9-4; Sequence=VSP_002763, VSP_002765;
CC       Name=JIP-1e; Synonyms=3;
CC         IsoId=Q9WVI9-5; Sequence=VSP_002764;
CC   -!- TISSUE SPECIFICITY: Expressed predominantly in the brain and
CC       insulin-secreting cells. In the brain, high expression found in
CC       the cerebral cortex and hippocampus. Localizes in the synaptic
CC       regions of the olfactory bulb, retina, cerebral and cerebellar
CC       cortex and hippocampus. Also expressed in a restricted number of
CC       axons, including mossy fibers from the hippocampal dentate gyrus,
CC       soma, dendrites and axons of cerebellar Purkinje cells. Also
CC       expressed in kidney, testis and prostate. Low levels in heart,
CC       ovary and small intestine. Isoform JIP-1b is more predominant in
CC       the brain than isoform JIP-1a. Isoform Jip1-a is expressed both in
CC       the brain and kidney, isoform JIP-1c, isoform JIP-1d and isoform
CC       JIP-1e are brain specific.
CC   -!- DEVELOPMENTAL STAGE: Low levels at prenatal stage E15, increased
CC       levels during the first postnatal days, with a plateau at
CC       postnatal day 15.
CC   -!- INDUCTION: Upon neuron differentiation.
CC   -!- PTM: Phosphorylated by MAPK8, MAPK9 and MAPK10. Phosphorylation on
CC       Thr-103 is also necessary for the dissociation and activation of
CC       MAP3K12.
CC   -!- PTM: Ubiquitinated. Two preliminary events are required to prime
CC       for ubiquitination; phosphorylation and an increased in
CC       intracellular calcium concentration. Then, the calcium influx
CC       initiates ubiquitination and degradation by the ubiquitin-
CC       proteasome pathway.
CC   -!- SIMILARITY: Belongs to the JIP scaffold family.
CC   -!- SIMILARITY: Contains 1 PID domain.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF003115; AAB66317.1; -; mRNA.
DR   EMBL; AF109768; AAD38346.1; -; mRNA.
DR   EMBL; AF109769; AAD38347.1; -; mRNA.
DR   EMBL; AF109770; AAD38348.1; -; mRNA.
DR   EMBL; AF109771; AAD38349.1; -; mRNA.
DR   EMBL; AF054611; AAD22580.1; -; mRNA.
DR   EMBL; AF332075; AAK56103.1; -; mRNA.
DR   EMBL; AF332076; AAK56104.1; -; mRNA.
DR   IPI; IPI00230316; -.
DR   IPI; IPI00230317; -.
DR   IPI; IPI00230318; -.
DR   IPI; IPI00321873; -.
DR   IPI; IPI00465532; -.
DR   PIR; T03038; T03038.
DR   RefSeq; NP_035292.2; NM_011162.4.
DR   UniGene; Mm.2720; -.
DR   PDB; 1UKH; X-ray; 2.35 A; B=153-163.
DR   PDB; 1UKI; X-ray; 2.70 A; B=153-163.
DR   PDB; 3O17; X-ray; 3.00 A; F/G=154-163.
DR   PDB; 3O2M; X-ray; 2.70 A; F/G=154-163.
DR   PDBsum; 1UKH; -.
DR   PDBsum; 1UKI; -.
DR   PDBsum; 3O17; -.
DR   PDBsum; 3O2M; -.
DR   ProteinModelPortal; Q9WVI9; -.
DR   SMR; Q9WVI9; 486-697.
DR   IntAct; Q9WVI9; 56.
DR   MINT; MINT-126863; -.
DR   STRING; Q9WVI9; -.
DR   PhosphoSite; Q9WVI9; -.
DR   PRIDE; Q9WVI9; -.
DR   Ensembl; ENSMUST00000050312; ENSMUSP00000050773; ENSMUSG00000027223.
DR   Ensembl; ENSMUST00000111279; ENSMUSP00000106910; ENSMUSG00000027223.
DR   GeneID; 19099; -.
DR   KEGG; mmu:19099; -.
DR   UCSC; uc008kxv.1; mouse.
DR   UCSC; uc008kxw.1; mouse.
DR   UCSC; uc008kxx.1; mouse.
DR   CTD; 19099; -.
DR   MGI; MGI:1309464; Mapk8ip1.
DR   GeneTree; ENSGT00390000003908; -.
DR   HOVERGEN; HBG018568; -.
DR   InParanoid; Q9WVI9; -.
DR   OMA; AEPTSAF; -.
DR   OrthoDB; EOG4BP1BD; -.
DR   PhylomeDB; Q9WVI9; -.
DR   NextBio; 295662; -.
DR   ArrayExpress; Q9WVI9; -.
DR   Bgee; Q9WVI9; -.
DR   Genevestigator; Q9WVI9; -.
DR   GermOnline; ENSMUSG00000027223; Mus musculus.
DR   GO; GO:0044297; C:cell body; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0044302; C:dentate gyrus mossy fiber; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0019894; F:kinesin binding; IPI:UniProtKB.
DR   GO; GO:0005078; F:MAP-kinase scaffold activity; NAS:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006916; P:anti-apoptosis; IDA:MGI.
DR   GO; GO:0007258; P:JUN phosphorylation; IDA:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IDA:MGI.
DR   GO; GO:0016192; P:vesicle-mediated transport; IDA:MGI.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR006020; PTyr_interaction_dom.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00640; PID; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS01179; PID; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Nucleus;
KW   Phosphoprotein; Polymorphism; Repeat; SH3 domain; Ubl conjugation.
FT   CHAIN         1    707       C-Jun-amino-terminal kinase-interacting
FT                                protein 1.
FT                                /FTId=PRO_0000220629.
FT   DOMAIN      484    545       SH3.
FT   DOMAIN      557    696       PID.
FT   REGION      127    281       JNK-binding domain (JBD).
FT   REGION      153    172       Minimal inhibitory domain (MID).
FT   MOTIF       349    356       D-box 1.
FT   MOTIF       360    368       D-box 2.
FT   COMPBIAS     41     47       Asp/Glu-rich (acidic).
FT   COMPBIAS    107    116       Asp/Glu-rich (acidic).
FT   COMPBIAS    355    359       Poly-Pro.
FT   MOD_RES     103    103       Phosphothreonine; by MAPK8, MAPK9 and
FT                                MAPK10 (By similarity).
FT   MOD_RES     201    201       Phosphothreonine; by MAPK8, MAPK9 and
FT                                MAPK10 (By similarity).
FT   VAR_SEQ       1     90       Missing (in isoform JIP-1e).
FT                                /FTId=VSP_002764.
FT   VAR_SEQ       1     33       MAERESGLGGGAASPPAASPFLGLHIASPPNFR -> MQLV
FT                                LKMDSSPDNDSWLEDQWEHW (in isoform JIP-1c
FT                                and isoform JIP-1d).
FT                                /FTId=VSP_002763.
FT   VAR_SEQ      69     93       Missing (in isoform JIP-1d).
FT                                /FTId=VSP_002765.
FT   VAR_SEQ     558    604       Missing (in isoform JIP-1a).
FT                                /FTId=VSP_002766.
FT   VARIANT      10     10       G -> R (in strain: ILS).
FT   CONFLICT    144    145       PG -> A (in Ref. 2; AAD38346/AAD38347/
FT                                AAD38348).
FT   CONFLICT    593    593       R -> RP (in Ref. 2; AAD38346/AAD38347/
FT                                AAD38348).
SQ   SEQUENCE   707 AA;  77282 MW;  274013B12D91049D CRC64;
     MAERESGLGG GAASPPAASP FLGLHIASPP NFRLTHDISL EEFEDEDLSE ITDECGISLQ
     CKDTLSLRPP RAGLLSAGSS GSAGSRLQAE MLQMDLIDAA GDTPGAEDDE EEEDDELAAQ
     RPGVGPPKAE SNQDPAPRSQ GQGPGTGSGD TYRPKRPTTL NLFPQVPRSQ DTLNNNSLGK
     KHSWQDRVSR SSSPLKTGEQ TPPHEHICLS DELPPQGSPV PTQDRGTSTD SPCRRSAATQ
     MAPPSGPPAT APGGRGHSHR DRIHYQADVR LEATEEIYLT PVQRPPDPAE PTSTFMPPTE
     SRMSVSSDPD PAAYSVTAGR PHPSISEEDE GFDCLSSPER AEPPGGGWRG SLGEPPPPPR
     ASLSSDTSAL SYDSVKYTLV VDEHAQLELV SLRPCFGDYS DESDSATVYD NCASASSPYE
     SAIGEEYEEA PQPRPPTCLS EDSTPDEPDV HFSKKFLNVF MSGRSRSSSA ESFGLFSCVI
     NGEEHEQTHR AIFRFVPRHE DELELEVDDP LLVELQAEDY WYEAYNMRTG ARGVFPAYYA
     IEVTKEPEHM AALAKNSDWI DQFRVKFLGS VQVPYHKGND VLCAAMQKIA TTRRLTVHFN
     PPSSCVLEIS VRGVKIGVKA DDALEAKGNK CSHFFQLKNI SFCGYHPKNN KYFGFITKHP
     ADHRFACHVF VSEDSTKALA ESVGRAFQQF YKQFVEYTCP TEDIYLE
//
ID   EHD1_MOUSE              Reviewed;         534 AA.
AC   Q9WVK4;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=EH domain-containing protein 1;
DE   AltName: Full=PAST homolog 1;
DE            Short=mPAST1;
GN   Name=Ehd1; Synonyms=Past1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=ICR;
RX   MEDLINE=99326524; PubMed=10395801; DOI=10.1006/geno.1999.5800;
RA   Mintz L., Galperin E., Pasmanik-Chor M., Tulzinsky S., Bromberg Y.,
RA   Kozak C.A., Joyner A., Fein A., Horowitz M.;
RT   "EHD1 -- an EH-domain-containing protein with a specific expression
RT   pattern.";
RL   Genomics 59:66-76(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RA   Plomann M., Behrendt D., Ritter B., Modregger J., Halback A.,
RA   Paulsson M.;
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF GLY-65 AND
RP   TRP-485, AND INTERACTION WITH PACSIN1 AND PACSIN2.
RX   PubMed=15930129; DOI=10.1091/mbc.E05-01-0076;
RA   Braun A., Pinyol R., Dahlhaus R., Koch D., Fonarev P., Grant B.D.,
RA   Kessels M.M., Qualmann B.;
RT   "EHD proteins associate with syndapin I and II and such interactions
RT   play a crucial role in endosomal recycling.";
RL   Mol. Biol. Cell 16:3642-3658(2005).
CC   -!- FUNCTION: Acts in early endocytic membrane fusion and membrane
CC       trafficking of recycling endosomes.
CC   -!- SUBUNIT: Homodimer, and heterodimer with EHD2, EHD3 and EHD4.
CC       Interacts with ZFYVE20 (By similarity). Interacts with PACSIN1 and
CC       PACSIN2.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Early endosome membrane; Peripheral membrane
CC       protein. Recycling endosome membrane; Peripheral membrane protein
CC       (By similarity).
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis. Also expressed in
CC       kidney, heart, intestine, and brain.
CC   -!- DEVELOPMENTAL STAGE: Expression is already noted at day 9.5 in the
CC       limb buds and pharyngeal arches and at day 10.5 in sclerotomes, at
CC       various elements of the branchial apparatus (mandible and hyoid),
CC       and in the occipital region. At day 15.5 expression peaks in
CC       cartilage, preceding hypertrophy and ossification, and at day 17.5
CC       there is no expression in the bones.
CC   -!- DOMAIN: The EH domain interacts with Asn-Pro-Phe (NPF) motifs of
CC       target proteins.
CC   -!- SIMILARITY: Contains 1 EF-hand domain.
CC   -!- SIMILARITY: Contains 1 EH domain.
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DR   EMBL; AF099186; AAD45423.1; -; mRNA.
DR   EMBL; AF173156; AAF24223.1; -; mRNA.
DR   EMBL; AK012896; BAB28540.1; -; mRNA.
DR   IPI; IPI00126083; -.
DR   RefSeq; NP_034249.1; NM_010119.5.
DR   UniGene; Mm.30169; -.
DR   UniGene; Mm.471458; -.
DR   ProteinModelPortal; Q9WVK4; -.
DR   SMR; Q9WVK4; 19-534.
DR   STRING; Q9WVK4; -.
DR   PhosphoSite; Q9WVK4; -.
DR   PRIDE; Q9WVK4; -.
DR   Ensembl; ENSMUST00000025684; ENSMUSP00000025684; ENSMUSG00000024772.
DR   GeneID; 13660; -.
DR   KEGG; mmu:13660; -.
DR   UCSC; uc008ghz.1; mouse.
DR   CTD; 13660; -.
DR   MGI; MGI:1341878; Ehd1.
DR   GeneTree; ENSGT00600000084243; -.
DR   HOVERGEN; HBG018183; -.
DR   InParanoid; Q9WVK4; -.
DR   OMA; IDELEWV; -.
DR   OrthoDB; EOG418BN4; -.
DR   NextBio; 284400; -.
DR   ArrayExpress; Q9WVK4; -.
DR   Bgee; Q9WVK4; -.
DR   CleanEx; MM_EHD1; -.
DR   Genevestigator; Q9WVK4; -.
DR   GermOnline; ENSMUSG00000024772; Mus musculus.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030139; C:endocytic vesicle; IDA:MGI.
DR   GO; GO:0005811; C:lipid particle; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0031095; C:platelet dense tubular network membrane; IDA:BHF-UCL.
DR   GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0042632; P:cholesterol homeostasis; IMP:BHF-UCL.
DR   GO; GO:0006897; P:endocytosis; IDA:MGI.
DR   GO; GO:0016197; P:endosome transport; IDA:MGI.
DR   GO; GO:0034383; P:low-density lipoprotein particle clearance; IMP:BHF-UCL.
DR   GO; GO:0010886; P:positive regulation of cholesterol storage; IMP:BHF-UCL.
DR   InterPro; IPR001401; Dynamin_GTPase.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR000261; EPS15_homology.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Pfam; PF00350; Dynamin_N; 1.
DR   SMART; SM00027; EH; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS50031; EH; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Calcium; Cell membrane; Coiled coil; Endosome; Membrane;
KW   Nucleotide-binding; Phosphoprotein.
FT   CHAIN         1    534       EH domain-containing protein 1.
FT                                /FTId=PRO_0000146110.
FT   DOMAIN      444    532       EH.
FT   DOMAIN      476    511       EF-hand.
FT   NP_BIND      65     72       ATP (By similarity).
FT   CA_BIND     489    500       By similarity.
FT   COILED      198    227       Potential.
FT   BINDING     220    220       ATP (By similarity).
FT   BINDING     258    258       ATP (By similarity).
FT   MOD_RES     453    453       Phosphotyrosine (By similarity).
FT   MOD_RES     456    456       Phosphoserine (By similarity).
FT   MUTAGEN      65     65       G->R: Abolishes interaction with PACSIN2.
FT   MUTAGEN     485    485       W->A: Abolishes interaction with PACSIN2.
SQ   SEQUENCE   534 AA;  60603 MW;  35502055BC6164F7 CRC64;
     MFSWVSKDAR RKKEPELFQT VAEGLRQLYA QKLLPLEEHY RFHEFHSPAL EDADFDNKPM
     VLLVGQYSTG KTTFIRHLIE QDFPGMRIGP EPTTDSFIAV MHGPTEGVVP GNALVVDPRR
     PFRKLNAFGN AFLNRFMCAQ LPNPVLDSIS IIDTPGILSG EKQRISRGYD FAAVLEWFAE
     RVDRIILLFD AHKLDISDEF SEVIKALKNH EDKIRVVLNK ADQIETQQLM RVYGALMWSL
     GKIINTPEVV RVYIGSFWSH PLLIPDNRKL FEAEEQDLFK DIQSLPRNAA LRKLNDLIKR
     ARLAKVHAYI ISSLKKEMPN VFGKESKKKE LVNNLGEIYQ KIEREHQISS GDFPSLRKMQ
     ELLQTQDFSK FQALKPKLLD TVDDMLANDI ARLMVMVRQE ESLMPSQAVK GGAFDGTMNG
     PFGHGYGEGA GEGIDDVEWV VGKDKPTYDE IFYTLSPVNG KITGANAKKE MVKSKLPNTV
     LGKIWKLADV DKDGLLDDEE FALANHLIKV KLEGHELPAD LPPHLIPPSK RRHE
//
ID   EXTL3_MOUSE             Reviewed;         918 AA.
AC   Q9WVL6;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Exostosin-like 3;
DE            EC=2.4.1.223;
DE   AltName: Full=Glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase;
DE   AltName: Full=Multiple exostosis-like protein 3;
GN   Name=Extl3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Sato T.;
RT   "Molecular cloning of the mouse homolog of EXT1L.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable glycosyltransferase (By similarity).
CC   -!- CATALYTIC ACTIVITY: UDP-N-acetyl-D-glucosamine + beta-D-
CC       glucuronosyl-(1->3)-beta-D-galactosyl-(1->3)-beta-D-galactosyl-
CC       (1->4)-beta-D-xylosyl-proteoglycan = UDP + alpha-N-acetyl-D-
CC       glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-beta-D-galactosyl-
CC       (1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl-proteoglycan.
CC   -!- PATHWAY: Glycan metabolism; heparan sulfate biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       type II membrane protein (By similarity).
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
CC       Note=EXTL3 (Putative GlcNAc Transferase I) [GAG Enzyme];
CC       URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_mou_580";
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DR   EMBL; AF083550; AAD42040.1; -; mRNA.
DR   IPI; IPI00126131; -.
DR   UniGene; Mm.103748; -.
DR   ProteinModelPortal; Q9WVL6; -.
DR   SMR; Q9WVL6; 660-904.
DR   STRING; Q9WVL6; -.
DR   CAZy; GT47; Glycosyltransferase Family 47.
DR   CAZy; GT64; Glycosyltransferase Family 64.
DR   PRIDE; Q9WVL6; -.
DR   Ensembl; ENSMUST00000022550; ENSMUSP00000022550; ENSMUSG00000021978.
DR   Ensembl; ENSMUST00000111165; ENSMUSP00000106795; ENSMUSG00000021978.
DR   MGI; MGI:1860765; Extl3.
DR   GeneTree; ENSGT00550000074496; -.
DR   HOVERGEN; HBG051526; -.
DR   InParanoid; Q9WVL6; -.
DR   OrthoDB; EOG415GCN; -.
DR   BRENDA; 2.4.1.223; 244.
DR   ArrayExpress; Q9WVL6; -.
DR   Bgee; Q9WVL6; -.
DR   CleanEx; MM_EXTL3; -.
DR   Genevestigator; Q9WVL6; -.
DR   GermOnline; ENSMUSG00000021978; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031227; C:intrinsic to endoplasmic reticulum membrane; IEA:InterPro.
DR   GO; GO:0001888; F:glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004263; Exostosin.
DR   InterPro; IPR015338; HexNAc_Trfase_a.
DR   Pfam; PF03016; Exostosin; 1.
DR   Pfam; PF09258; Glyco_transf_64; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Endoplasmic reticulum; Glycoprotein;
KW   Glycosyltransferase; Manganese; Membrane; Metal-binding;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN         1    918       Exostosin-like 3.
FT                                /FTId=PRO_0000149658.
FT   TOPO_DOM      1     30       Cytoplasmic (Potential).
FT   TRANSMEM     31     51       Helical; Signal-anchor for type II
FT                                membrane protein; (Potential).
FT   TOPO_DOM     52    918       Lumenal (Potential).
FT   METAL       745    745       Manganese; catalytic (By similarity).
FT   CARBOHYD    277    277       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    290    290       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    591    591       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    789    789       N-linked (GlcNAc...) (Potential).
FT   DISULFID    830    878       By similarity.
SQ   SEQUENCE   918 AA;  104548 MW;  4EEFEC86E7E6027E CRC64;
     MTGYTMLRNG GVGNGGQTCM LRWSNRIRLT WLSFTLFIIL VFFPLIAHYY LTTLDEADEA
     GKRIFGPRAG SELCEVKHVL DLCRIRESVS EELLQLEAKR QELNSEIAKL NLKIEACKKS
     IENAKQDLLQ LKNVISQTEH SYKELMAQNQ PKLSLPIRLL PEKDDAGLPP PKVTRGCRLH
     NCFDYSRCPL TSGFPVYVYD SDQFAFGSYL DPLVKQAFQA TVRANVYVTE NAAIACLYVV
     LVGEMQEPTV LRPADLEKQL FSLPHWRTDG HNHVIINLSR KSDTQNLLYN VSTGRHVAQS
     TLYAAQYRAG FDLVVSPLVH AMSEPNFMEI PPQVPVKRKY LFTFQGEKIE SLRSSLQEAR
     SFEEEMEGDP PADYDDRIIA TLKAVQDSKL DQVLVEFTCK NQPKPSLPTE WALCGEREDR
     LELLKLSTFA LIITPGDPRL LISSGCATRL FEALEVGAVP VVLGEQVQLP YHDMLQWNEA
     ALVVPKPRVT EVHFLLRSLS DSDLLAMRRQ GRFLWETYFS TADSIFNTVL AMIRTRIQIP
     AAPIREEVAA EIPHRSGKAA GTDPNMADNG DLDLGPVETE PPYASPKYLR NFTLTVTDCY
     RGWNSAPGRF HLFPHTPFDP VLPSEAKFLG SGTGFRPIGG GAGGSGKEFQ AALGGNVQRE
     QFTVVMLTYE REEVLMNSLE RLNGLPYLNK VVVVWNSPKL PSEDLLWPDI GVPIMVVRTE
     KNSLNNRFLP WNEIETEAIL SIDDDAHLRH DEIMFGFWVW REARDRIVGF PGRYHAWDIP
     HQSWLYNSNY SCELSMVLTG AAFFHKYYAY LYSYVMPQAI RDMVDEYINC EDIAMNFLVS
     HITRKPPIKV TSRWTFRCPG CPQALSHDDS HFHERHKCIN FFVKVYGYMP LLYTQFRVDS
     VLFKTRLPHD KTKCFKFI
//
ID   Q9WVM2_MOUSE            Unreviewed;       383 AA.
AC   Q9WVM2;
DT   01-NOV-1999, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 62.
DE   SubName: Full=Dematin 48 kDa subunit;
DE   SubName: Full=Erythrocyte protein band 4.9;
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Epb4.9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=99431674; PubMed=10501976; DOI=10.1007/s003359901153;
RA   Azim A.C., Kim A.C., Lutchman M., Andrabi S., Peters L.L.,
RA   Chishti A.H.;
RT   "cDNA sequence, genomic structure, and expression of the mouse dematin
RT   gene (Epb4.9).";
RL   Mamm. Genome 10:1026-1029(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Spleen;
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K.,
RA   Hori F., Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S.,
RA   Kawai J., Kojima M., Konno H., Murata M., Nakamura M., Ninomiya N.,
RA   Nishiyori H., Nomura K., Ohno M., Sakazume N., Sano H., Sasaki D.,
RA   Shibata K., Shiraki T., Tagami M., Tagami Y., Waki K., Watahiki A.,
RA   Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; AF079846; AAD34233.1; -; mRNA.
DR   EMBL; BC016897; AAH16897.1; -; mRNA.
DR   EMBL; AK165294; BAE38123.1; -; mRNA.
DR   IPI; IPI00620207; -.
DR   RefSeq; NP_038542.1; NM_013514.3.
DR   UniGene; Mm.210863; -.
DR   UniGene; Mm.446654; -.
DR   HSSP; Q08495; 1QZP.
DR   ProteinModelPortal; Q9WVM2; -.
DR   SMR; Q9WVM2; 316-383.
DR   STRING; Q9WVM2; -.
DR   Ensembl; ENSMUST00000022694; ENSMUSP00000022694; ENSMUSG00000022099.
DR   Ensembl; ENSMUST00000110984; ENSMUSP00000106612; ENSMUSG00000022099.
DR   GeneID; 13829; -.
DR   KEGG; mmu:13829; -.
DR   UCSC; uc007uop.1; mouse.
DR   CTD; 13829; -.
DR   MGI; MGI:99670; Epb4.9.
DR   GeneTree; ENSGT00570000079028; -.
DR   HOVERGEN; HBG031499; -.
DR   NextBio; 284636; -.
DR   ArrayExpress; Q9WVM2; -.
DR   Bgee; Q9WVM2; -.
DR   Genevestigator; Q9WVM2; -.
DR   GO; GO:0030863; C:cortical cytoskeleton; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0007010; P:cytoskeleton organization; IEA:InterPro.
DR   InterPro; IPR003128; Villin_headpiece.
DR   Gene3D; G3DSA:1.10.950.10; VHP; 1.
DR   Pfam; PF02209; VHP; 1.
DR   SMART; SM00153; VHP; 1.
DR   SUPFAM; SSF47050; VHP; 1.
DR   PROSITE; PS51089; HP; 1.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   383 AA;  43042 MW;  C8F3299489322DF1 CRC64;
     MERLQKQPLT SPGSVSSSRD SSVPGSPSSI VAKMDNQVLG YKDLAAIPKD KAILDIERPD
     LMIYEPHFTY SLLEHVELPR SRECSLSPKS TSPPPSPEVW AESRTLGIIS QASTPRTTGT
     PRTSLPHFHH PETTRPDSNI YKKPPIYKQR ESVGGSPQSK HLIEDLIIES SKFPAAQPPD
     PNQPAKIETD YWPCPPSLAV VETEWRKRKA SRKGAEEEEE EEDDDSEEEI KAIRERQKEE
     LSKVTSNLGK MILKEEMEKS LPIRRKTRSL PDRTPFHTSL HSGTSKSSSL PSYGRTTLSR
     LQSTEFSPSG SEAGSPGLQI YPYEMLVVTN KGRTKLPPGV DRMRLERHLS AEDFSRVFAM
     SPEEFGKLAL WKRNELKKKA SLF
//
ID   MAGI2_MOUSE             Reviewed;        1275 AA.
AC   Q9WVQ1; Q3UH81; Q6GT88; Q8BYT1; Q8CA85;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2003, sequence version 2.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2;
DE   AltName: Full=Activin receptor-interacting protein 1;
DE            Short=Acvrip1;
DE   AltName: Full=Atrophin-1-interacting protein 1;
DE            Short=AIP-1;
DE   AltName: Full=Membrane-associated guanylate kinase inverted 2;
DE            Short=MAGI-2;
GN   Name=Magi2; Synonyms=Acvrinp1, Aip1, Arip1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH SMAD2;
RP   SMAD3 AND ACVR2A, AND IDENTIFICATION IN A COMPLEX WITH ACVR2A; ACVR1B
RP   AND SMAD3.
RC   STRAIN=ICR; TISSUE=Brain;
RX   MEDLINE=20148748; PubMed=10681527; DOI=10.1074/jbc.275.8.5485;
RA   Shoji H., Tsuchida K., Kishi H., Yamakawa N., Matsuzaki T., Liu Z.,
RA   Nakamura T., Sugino H.;
RT   "Identification and characterization of a PDZ protein that interacts
RT   with activin types II receptors.";
RL   J. Biol. Chem. 275:5485-5492(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH HTR2A.
RX   PubMed=14988405; DOI=10.1074/jbc.M312106200;
RA   Becamel C., Gavarini S., Chanrion B., Alonso G., Galeotti N.,
RA   Dumuis A., Bockaert J., Marin P.;
RT   "The serotonin 5-HT2A and 5-HT2C receptors interact with specific sets
RT   of PDZ proteins.";
RL   J. Biol. Chem. 279:20257-20266(2004).
RN   [5]
RP   INTERACTION WITH HTR4.
RX   PubMed=15466885; DOI=10.1242/jcs.01379;
RA   Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W.,
RA   Marin P., Dumuis A., Bockaert J.;
RT   "New sorting nexin (SNX27) and NHERF specifically interact with the 5-
RT   HT4a receptor splice variant: roles in receptor targeting.";
RL   J. Cell Sci. 117:5367-5379(2004).
RN   [6]
RP   INTERACTION WITH IGSF9.
RX   PubMed=15340156; DOI=10.1073/pnas.0405371101;
RA   Shi S.-H., Cheng T., Jan L.Y., Jan Y.-N.;
RT   "The immunoglobulin family member dendrite arborization and synapse
RT   maturation 1 (Dasm1) controls excitatory synapse maturation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13346-13351(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-361; TYR-365 AND
RP   TYR-826, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1013, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Seems to act as scaffold molecule at synaptic junctions
CC       by assembling neurotransmitter receptors and cell adhesion
CC       proteins. May play a role in regulating activin-mediated signaling
CC       in neuronal cells. Enhances the ability of PTEN to suppress AKT1
CC       activation (By similarity).
CC   -!- SUBUNIT: Interacts via its WW domains with DRPLA (By similarity).
CC       Interacts via its second PDZ domain with PTEN unphosphorylated C-
CC       terminus; this interaction diminishes the degradation rate of PTEN
CC       (By similarity). Interacts through its guanylate kinase domain
CC       with DLGAP1 (By similarity). Interacts through the PDZ domains
CC       with GRIN2A, GRID2 and NLGN1 (By similarity). Interacts with
CC       CTNND2, CTNNB1 and MAGUIN-1 (By similarity). Interacts with
CC       ACVR2A, SMAD2 and SMAD3. Part of a complex consisting of AIP1,
CC       ACVR2A, ACVR1B and SMAD3. May interact with HTR2A. Interacts with
CC       RAPGEF2 (By similarity). Interacts with DDN (By similarity).
CC       Interacts with IGSF9. Interacts with HTR4.
CC   -!- INTERACTION:
CC       Q61483:Dll1; NbExp=1; IntAct=EBI-297151, EBI-297125;
CC   -!- SUBCELLULAR LOCATION: Cell junction, synapse, synaptosome (By
CC       similarity). Cell membrane; Peripheral membrane protein (By
CC       similarity). Note=Membrane-associated in synaptosomes (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=long;
CC         IsoId=Q9WVQ1-1; Sequence=Displayed;
CC       Name=2; Synonyms=short;
CC         IsoId=Q9WVQ1-2; Sequence=VSP_008436;
CC         Note=Major;
CC       Name=3;
CC         IsoId=Q9WVQ1-3; Sequence=VSP_018580, VSP_008437;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q9WVQ1-4; Sequence=VSP_008436, VSP_018581;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Specifically expressed in brain.
CC   -!- SIMILARITY: Belongs to the MAGUK family.
CC   -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC   -!- SIMILARITY: Contains 6 PDZ (DHR) domains.
CC   -!- SIMILARITY: Contains 2 WW domains.
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DR   EMBL; AB029485; BAA82294.1; -; mRNA.
DR   EMBL; AK039336; BAC30321.1; -; mRNA.
DR   EMBL; AK147530; BAE27976.1; -; mRNA.
DR   EMBL; BC059005; AAH59005.1; -; mRNA.
DR   IPI; IPI00378020; -.
DR   IPI; IPI00719895; -.
DR   IPI; IPI00756092; -.
DR   IPI; IPI00849279; -.
DR   RefSeq; NP_001164216.1; NM_001170745.1.
DR   RefSeq; NP_001164217.1; NM_001170746.1.
DR   RefSeq; NP_056638.1; NM_015823.3.
DR   UniGene; Mm.332231; -.
DR   UniGene; Mm.441283; -.
DR   ProteinModelPortal; Q9WVQ1; -.
DR   SMR; Q9WVQ1; 13-98, 133-188, 296-379, 411-521, 593-681, 768-1020, 1133-1228.
DR   IntAct; Q9WVQ1; 2.
DR   MINT; MINT-122116; -.
DR   STRING; Q9WVQ1; -.
DR   PhosphoSite; Q9WVQ1; -.
DR   PRIDE; Q9WVQ1; -.
DR   Ensembl; ENSMUST00000088516; ENSMUSP00000085872; ENSMUSG00000040003.
DR   Ensembl; ENSMUST00000101558; ENSMUSP00000099094; ENSMUSG00000040003.
DR   Ensembl; ENSMUST00000115267; ENSMUSP00000110922; ENSMUSG00000040003.
DR   GeneID; 50791; -.
DR   KEGG; mmu:50791; -.
DR   UCSC; uc008wnv.1; mouse.
DR   UCSC; uc008wnw.1; mouse.
DR   UCSC; uc008wnx.1; mouse.
DR   CTD; 50791; -.
DR   MGI; MGI:1354953; Magi2.
DR   eggNOG; roNOG15000; -.
DR   GeneTree; ENSGT00530000063259; -.
DR   HOGENOM; HBG315069; -.
DR   HOVERGEN; HBG007091; -.
DR   InParanoid; Q9WVQ1; -.
DR   OMA; SDPSHQI; -.
DR   OrthoDB; EOG4WWRHS; -.
DR   NextBio; 307779; -.
DR   ArrayExpress; Q9WVQ1; -.
DR   Bgee; Q9WVQ1; -.
DR   Genevestigator; Q9WVQ1; -.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR   GO; GO:0019717; C:synaptosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004871; F:signal transducer activity; IPI:MGI.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR020590; Guanylate_kinase_CS.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF00595; PDZ; 6.
DR   Pfam; PF00397; WW; 2.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 6.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF50156; PDZ; 6.
DR   SUPFAM; SSF51045; WW_Rsp5_WWP; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 6.
DR   PROSITE; PS01159; WW_DOMAIN_1; 2.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Membrane;
KW   Phosphoprotein; Repeat; Synapse; Synaptosome.
FT   CHAIN         1   1275       Membrane-associated guanylate kinase, WW
FT                                and PDZ domain-containing protein 2.
FT                                /FTId=PRO_0000094587.
FT   DOMAIN       17    101       PDZ 1.
FT   DOMAIN      109    283       Guanylate kinase-like.
FT   DOMAIN      301    334       WW 1.
FT   DOMAIN      347    380       WW 2.
FT   DOMAIN      425    509       PDZ 2.
FT   DOMAIN      604    682       PDZ 3.
FT   DOMAIN      777    859       PDZ 4.
FT   DOMAIN      919   1009       PDZ 5.
FT   DOMAIN     1139   1221       PDZ 6.
FT   REGION      301    380       Interaction with DDN (By similarity).
FT   MOD_RES     361    361       Phosphotyrosine.
FT   MOD_RES     365    365       Phosphotyrosine.
FT   MOD_RES     826    826       Phosphotyrosine.
FT   MOD_RES    1013   1013       Phosphoserine.
FT   VAR_SEQ       1    390       Missing (in isoform 3).
FT                                /FTId=VSP_018580.
FT   VAR_SEQ       1    163       Missing (in isoform 2 and isoform 4).
FT                                /FTId=VSP_008436.
FT   VAR_SEQ     756    770       QQVPPRTSFRMDSSG -> R (in isoform 4).
FT                                /FTId=VSP_018581.
FT   VAR_SEQ    1229   1275       MVPSSLSMCMKSDKHGSPYFYLLGHPKDTTNPTPGVLPLPP
FT                                PQACRK -> AFHSFLHLCSAFSVF (in isoform 3).
FT                                /FTId=VSP_008437.
SQ   SEQUENCE   1275 AA;  140919 MW;  F17DC52517806354 CRC64;
     MSKSLKKKSH WTSKVHESVI GRNPEGQLGF ELKGGAENGQ FPYLGEVKPG KVAYESGSKL
     VSEELLLEVN ETPVAGLTIR DVLAVIKHCK DPLRLKCVKQ GGIVDKDLRH YLNLRFQKGS
     VDHELQQIIR DNLYLRTVPC TTRPHKEGEV PGVDYIFITV EEFMELEKSG ALLESGTYED
     NYYGTPKPPA EPAPLLNVTD QILPGATPSA EGKRKRNKSV TNMEKASIEP PEEEEEERPV
     VNGNGVVITP ESSEHEDKSA GASGETPSQP YPAPVYSQPE ELKDQMDDTK PTKPEENEDS
     DPLPDNWEMA YTEKGEVYFI DHNTKTTSWL DPRLAKKAKP PEECKENELP YGWEKIDDPI
     YGTYYVDHIN RRTQFENPVL EAKRKLQQHN MPHTELGAKP LQAPGFREKP LFTRDASQLK
     GTFLSTTLKK SNMGFGFTII GGDEPDEFLQ VKSVIPDGPA AQDGKMETGD VIVYINEVCV
     LGHTHADVVK LFQSVPIGQS VNLVLCRGYP LPFDPEDPAN SMVPPLAIME RPPPVMVNGR
     HNYETYLEYI SRTSQSVPDI TDRPPHSLHS MPADGQLDGT YPPPVHDDNV SMASSGATQA
     ELMTLTIVKG AQGFGFTIAD SPTGQRVKQI LDIQGCPGLC EGDLIVEINQ QNVQNLSHTE
     VVDILKDCPV GSETSLIIHR GGFFSPWKTP KPMMDRWENQ GSPQTSLSAP AVPQNLPFPP
     ALHRSSFPDS TEAFDPRKPD PYELYEKSRA IYESRQQVPP RTSFRMDSSG PDYKELDVHL
     RRMESGFGFR ILGGDEPGQP ILIGAVIAMG SADRDGRLHP GDELVYVDGI PVAGKTHRYV
     IDLMHHAARN GQVNLTVRRK VLCGGEPCPE NGRSPGSVST HHSSPRSDYA TYSNSNHAAP
     SSNASPPEGF ASHSLQTSDV VIHRKENEGF GFVIISSLNR PESGATITVP HKIGRIIDGS
     PADRCAKLKV GDRILAVNGQ SIINMPHADI VKLIKDAGLS VTLRIIPQEE LNSPTSAPSS
     EKQSPMAQQH SPLAQQSPLA QPSPATPNSP VAQPAPPQPL QLQGHENSYR SEVKARQDVK
     PDIRQPPFTD YRQPPLDYRQ PPGGDYSQPP PLDYRQHSPD TRQYPLSDYR QPQDFDYFTV
     DMEKGAKGFG FSIRGGREYK MDLYVLRLAE DGPAIRNGRM RVGDQIIEIN GESTRDMTHA
     RAIELIKSGG RRVRLLLKRG TGQVPEYGMV PSSLSMCMKS DKHGSPYFYL LGHPKDTTNP
     TPGVLPLPPP QACRK
//
ID   CAH14_MOUSE             Reviewed;         337 AA.
AC   Q9WVT6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Carbonic anhydrase 14;
DE            EC=4.2.1.1;
DE   AltName: Full=Carbonate dehydratase XIV;
DE   AltName: Full=Carbonic anhydrase XIV;
DE            Short=CA-XIV;
DE   Flags: Precursor;
GN   Name=Ca14; Synonyms=Car14, Catm;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   MEDLINE=99269110; PubMed=10336468; DOI=10.1074/jbc.274.22.15701;
RA   Mori K., Ogawa Y., Ebihara K., Tamura N., Tashiro K., Kuwahara T.,
RA   Mukoyama M., Sugawara A., Ozaki S., Tanaka I., Nakao K.;
RT   "Isolation and characterization of CA XIV, a novel membrane-bound
RT   carbonic anhydrase from mouse kidney.";
RL   J. Biol. Chem. 274:15701-15705(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Retina;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 18-278 ALONE AND IN COMPLEX
RP   WITH ACETAZOLAMIDE, DISULFIDE BOND, ZINC-BINDING SITES, ENZYME
RP   REGULATION, AND GLYCOSYLATION AT ASN-213.
RX   PubMed=14660577; DOI=10.1074/jbc.M310809200;
RA   Whittington D.A., Grubb J.H., Waheed A., Shah G.N., Sly W.S.,
RA   Christianson D.W.;
RT   "Expression, assay, and structure of the extracellular domain of
RT   murine carbonic anhydrase XIV: implications for selective inhibition
RT   of membrane-associated isozymes.";
RL   J. Biol. Chem. 279:7223-7228(2004).
CC   -!- FUNCTION: Reversible hydration of carbon dioxide.
CC   -!- CATALYTIC ACTIVITY: H(2)CO(3) = CO(2) + H(2)O.
CC   -!- COFACTOR: Zinc.
CC   -!- ENZYME REGULATION: Inhibited by acetazolamide.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- TISSUE SPECIFICITY: Most abundant in the kidney and heart,
CC       followed by the skeletal muscle, brain, lung and liver.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
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DR   EMBL; AB005450; BAA78709.1; -; mRNA.
DR   EMBL; BC046995; AAH46995.1; -; mRNA.
DR   IPI; IPI00126501; -.
DR   RefSeq; NP_035927.1; NM_011797.2.
DR   UniGene; Mm.306954; -.
DR   PDB; 1RJ5; X-ray; 2.81 A; A/B=18-278.
DR   PDB; 1RJ6; X-ray; 2.90 A; A/B=18-278.
DR   PDBsum; 1RJ5; -.
DR   PDBsum; 1RJ6; -.
DR   ProteinModelPortal; Q9WVT6; -.
DR   SMR; Q9WVT6; 20-278.
DR   STRING; Q9WVT6; -.
DR   PhosphoSite; Q9WVT6; -.
DR   PRIDE; Q9WVT6; -.
DR   Ensembl; ENSMUST00000036181; ENSMUSP00000036983; ENSMUSG00000038526.
DR   GeneID; 23831; -.
DR   KEGG; mmu:23831; -.
DR   UCSC; uc008qls.1; mouse.
DR   CTD; 23831; -.
DR   MGI; MGI:1344341; Car14.
DR   eggNOG; roNOG08385; -.
DR   GeneTree; ENSGT00570000078862; -.
DR   HOGENOM; HBG717384; -.
DR   HOVERGEN; HBG002837; -.
DR   InParanoid; Q9WVT6; -.
DR   OMA; YEGPHGQ; -.
DR   OrthoDB; EOG45MN5P; -.
DR   PhylomeDB; Q9WVT6; -.
DR   BRENDA; 4.2.1.1; 244.
DR   DrugBank; DB00819; Acetazolamide.
DR   NextBio; 303497; -.
DR   ArrayExpress; Q9WVT6; -.
DR   Bgee; Q9WVT6; -.
DR   CleanEx; MM_CAR14; -.
DR   Genevestigator; Q9WVT6; -.
DR   GermOnline; ENSMUSG00000038526; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR001148; Carbonic_anhydrase_a-class_cat.
DR   InterPro; IPR018431; Carbonic_anhydrase_CA14.
DR   Gene3D; G3DSA:3.10.200.10; Euk_COanhd; 1.
DR   PANTHER; PTHR18952:SF20; Carbonic_anhydrase_CA14; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   SUPFAM; SSF51069; Euk_COanhd; 1.
DR   PROSITE; PS00162; ALPHA_CA_1; FALSE_NEG.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Glycoprotein; Lyase; Membrane;
KW   Metal-binding; Signal; Transmembrane; Transmembrane helix; Zinc.
FT   SIGNAL        1     15       Potential.
FT   CHAIN        16    337       Carbonic anhydrase 14.
FT                                /FTId=PRO_0000004252.
FT   TOPO_DOM     16    290       Extracellular (Potential).
FT   TRANSMEM    291    311       Helical; (Potential).
FT   TOPO_DOM    312    337       Cytoplasmic (Potential).
FT   REGION      217    218       Substrate binding (By similarity).
FT   ACT_SITE     84     84       Proton acceptor (By similarity).
FT   ACT_SITE    144    144       By similarity.
FT   METAL       109    109       Zinc; catalytic.
FT   METAL       111    111       Zinc; catalytic.
FT   METAL       135    135       Zinc; catalytic.
FT   CARBOHYD    213    213       N-linked (GlcNAc...).
FT   DISULFID     40    221
FT   STRAND       24     26
FT   TURN         30     32
FT   HELIX        33     36
FT   HELIX        38     41
FT   TURN         52     54
FT   STRAND       65     67
FT   TURN         68     70
FT   STRAND       77     81
FT   STRAND       86     89
FT   STRAND       95    101
FT   STRAND      103    112
FT   STRAND      122    125
FT   STRAND      131    140
FT   TURN        141    143
FT   HELIX       147    150
FT   STRAND      157    166
FT   HELIX       172    178
FT   HELIX       179    184
FT   STRAND      190    193
FT   HELIX       198    201
FT   STRAND      209    214
FT   STRAND      225    232
FT   STRAND      234    236
FT   HELIX       238    245
FT   STRAND      249    255
SQ   SEQUENCE   337 AA;  37505 MW;  32F02F4DB78AC0C9 CRC64;
     MLFFALLLKV TWILAADGGH HWTYEGPHGQ DHWPTSYPEC GGDAQSPINI QTDSVIFDPD
     LPAVQPHGYD QLGTEPLDLH NNGHTVQLSL PPTLHLGGLP RKYTAAQLHL HWGQRGSLEG
     SEHQINSEAT AAELHVVHYD SQSYSSLSEA AQKPQGLAVL GILIEVGETE NPAYDHILSR
     LHEIRYKDQK TSVPPFSVRE LFPQQLEQFF RYNGSLTTPP CYQSVLWTVF NRRAQISMGQ
     LEKLQETLSS TEEDPSEPLV QNYRVPQPLN QRTIFASFIQ AGPLYTTGEM LGLGVGILAG
     CLCLLLAVYF IAQKIRKKRL GNRKSVVFTS ARATTEA
//
ID   NCDN_MOUSE              Reviewed;         729 AA.
AC   Q9Z0E0; Q3TCW4; Q80TW1; Q91YH7; Q9CW81; Q9QUQ0;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Neurochondrin;
DE   AltName: Full=M-Sema F-associating protein of 75 kDa;
DE   AltName: Full=Norbin;
GN   Name=Ncdn; Synonyms=Kiaa0607, Sfap75;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS
RP   1 AND 2).
RC   STRAIN=C57BL/6N;
RX   MEDLINE=99249818; PubMed=10231559; DOI=10.1016/S0167-4889(99)00039-7;
RA   Ishiduka Y., Mochizuki R., Yanai K., Takatsuka M., Nonomura T.,
RA   Niida S., Horiguchi H., Maeda N., Fukamizu A.;
RT   "Induction of hydroxyapatite resorptive activity in bone marrow cell
RT   populations resistant to bafilomycin A1 by a factor with restricted
RT   expression to bone and brain, neurochondrin.";
RL   Biochim. Biophys. Acta 1450:92-98(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 78-729.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [6]
RP   TISSUE SPECIFICITY, AND INTERACTION WITH SEMA4C.
RX   PubMed=11162505; DOI=10.1006/bbrc.2000.4080;
RA   Ohoka Y., Hirotani M., Sugimoto H., Fujioka S., Furuyama T.,
RA   Inagaki S.;
RT   "Semaphorin 4C, a transmembrane semaphorin, associates with a neurite-
RT   outgrowth-related protein, SFAP75.";
RL   Biochem. Biophys. Res. Commun. 280:237-243(2001).
RN   [7]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=11445285; DOI=10.1016/S0304-3940(01)01981-4;
RA   Mani S.T., Kumar R.C., Thakur M.K.;
RT   "Age- and sex-related expression of norbin in the brain cortex of
RT   mice.";
RL   Neurosci. Lett. 308:57-59(2001).
RN   [8]
RP   ERRATUM.
RA   Ohoka Y., Hirotani M., Sugimoto H., Fujioka S., Furuyama T.,
RA   Inagaki S.;
RL   Biochem. Biophys. Res. Commun. 281:266-266(2001).
RN   [9]
RP   DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX   PubMed=14559245; DOI=10.1016/j.bbrc.2003.09.153;
RA   Mochizuki R., Dateki M., Yanai K., Ishizuka Y., Amizuka N.,
RA   Kawashima H., Koga Y., Ozawa H., Fukamizu A.;
RT   "Targeted disruption of the neurochondrin/norbin gene results in
RT   embryonic lethality.";
RL   Biochem. Biophys. Res. Commun. 310:1219-1226(2003).
RN   [10]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15007648; DOI=10.1007/s00427-004-0396-2;
RA   Istvanffy R., Vogt Weisenhorn D.M., Floss T., Wurst W.;
RT   "Expression of neurochondrin in the developing and adult mouse
RT   brain.";
RL   Dev. Genes Evol. 214:206-209(2004).
RN   [11]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15790563; DOI=10.1074/jbc.M414033200;
RA   Dateki M., Horii T., Kasuya Y., Mochizuki R., Nagao Y., Ishida J.,
RA   Sugiyama F., Tanimoto K., Yagami K., Imai H., Fukamizu A.;
RT   "Neurochondrin negatively regulates CaMKII phosphorylation, and
RT   nervous system-specific gene disruption results in epileptic
RT   seizure.";
RL   J. Biol. Chem. 280:20503-20508(2005).
RN   [12]
RP   FUNCTION, AND INTERACTION WITH DIAPH1.
RX   PubMed=18572016; DOI=10.1016/j.bbrc.2008.06.042;
RA   Schwaibold E.M., Brandt D.T.;
RT   "Identification of Neurochondrin as a new interaction partner of the
RT   FH3 domain of the Diaphanous-related formin Dia1.";
RL   Biochem. Biophys. Res. Commun. 373:366-372(2008).
RN   [13]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=20007903; DOI=10.1126/science.1178496;
RA   Wang H., Westin L., Nong Y., Birnbaum S., Bendor J., Brismar H.,
RA   Nestler E., Aperia A., Flajolet M., Greengard P.;
RT   "Norbin is an endogenous regulator of metabotropic glutamate receptor
RT   5 signaling.";
RL   Science 326:1554-1557(2009).
CC   -!- FUNCTION: Probably involved in signal transduction, in the nervous
CC       system, via increasing cell surface localization of GRM5 and
CC       positively regulating its signaling. Required for the spatial
CC       learning process. Acts as a negative regulator of Ca(2+)-
CC       calmodulin-dependent protein kinase 2 (CaMK2) phosphorylation. May
CC       play a role in modulating melanin-concentrating hormone-mediated
CC       functions via its interaction with MCHR1 that interferes with G
CC       protein-coupled signal transduction. May be involved in bone
CC       metabolism. May also be involved in neurite outgrowth.
CC   -!- SUBUNIT: Interacts with MCHR1 and GRM5 (By similarity). Interacts
CC       with SEMA4C and DIAPH1 (via FH3 domain).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell projection,
CC       dendrite. Note=Localizes to somatic regions of neurons (By
CC       similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Neurochondrin-1;
CC         IsoId=Q9Z0E0-1; Sequence=Displayed;
CC       Name=2; Synonyms=Neurochondrin-2;
CC         IsoId=Q9Z0E0-2; Sequence=VSP_032317;
CC   -!- TISSUE SPECIFICITY: Expressed in the neuronal, chondral and bone
CC       tissues. Expressed in dendrites. Enriched in the brain in the
CC       surface layer I-IV. In brains, protein level increases in male but
CC       decreases in female with advancing age (at protein level). In
CC       adult brains, it is highly expressed in the forebrain and
CC       hindbrain. Highly expressed in the hippocampus, piriform cortex,
CC       septum, amygdaloid complex, medial geniculate nucleus, inferior
CC       colliculus, cerebellar nuclei and the nuclei of the Vth, VIIth,
CC       and XIIth cranial nerves. In bone tissues, it is expressed in
CC       osteoblasts and osteocytes.
CC   -!- DEVELOPMENTAL STAGE: In the developing brain, it is first
CC       expressed in the hindbrain and spinal cord at E10.5 followed by
CC       expression in the midbrain at E11.5. By E18 it is also expressed
CC       in the diencephalon and telencephalon, with a strongest expression
CC       in the hindbrain. Highly expressed in the developing olfactory
CC       bulb and in the lateral choroid plexus.
CC   -!- DISRUPTION PHENOTYPE: Death between 3.5 and 6.5 dpc. Heterozygous
CC       mutant do not display gross anatomic abnormalities. They however
CC       show abnormalities in developing cartilage. Nervous system-
CC       specific gene disruption by conditional knockout results in
CC       epileptic seizure. Displays no overt neurite outgrowth phenotype
CC       (PubMed:15790563). Shows a behavioral phenotype associated with a
CC       rodent model of schizophrenia, as observed in alterations in both
CC       sensorimotor gating and psychotomimetic-induced locomotor
CC       activity.
CC   -!- SIMILARITY: Belongs to the neurochondrin family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AB017608; BAA75226.1; -; Genomic_DNA.
DR   EMBL; AB017609; BAA75227.1; -; Genomic_DNA.
DR   EMBL; AB019041; BAA75228.1; -; Genomic_DNA.
DR   EMBL; AB019041; BAA75229.1; -; Genomic_DNA.
DR   EMBL; AK002938; BAB22468.2; -; mRNA.
DR   EMBL; AK154889; BAE32905.1; -; mRNA.
DR   EMBL; AK170502; BAE41841.1; -; mRNA.
DR   EMBL; AL606908; CAM19265.1; -; Genomic_DNA.
DR   EMBL; BC017126; AAH17126.1; -; mRNA.
DR   EMBL; AK122327; BAC65609.1; -; mRNA.
DR   IPI; IPI00331299; -.
DR   IPI; IPI00889265; -.
DR   RefSeq; NP_036116.3; NM_011986.4.
DR   UniGene; Mm.206206; -.
DR   UniGene; Mm.456184; -.
DR   STRING; Q9Z0E0; -.
DR   PRIDE; Q9Z0E0; -.
DR   Ensembl; ENSMUST00000030637; ENSMUSP00000030637; ENSMUSG00000028833.
DR   Ensembl; ENSMUST00000106116; ENSMUSP00000101722; ENSMUSG00000028833.
DR   GeneID; 26562; -.
DR   KEGG; mmu:26562; -.
DR   CTD; 26562; -.
DR   MGI; MGI:1347351; Ncdn.
DR   eggNOG; maNOG11120; -.
DR   GeneTree; ENSGT00390000013601; -.
DR   HOGENOM; HBG714851; -.
DR   HOVERGEN; HBG097452; -.
DR   InParanoid; Q9Z0E0; -.
DR   OMA; PEKQKEP; -.
DR   OrthoDB; EOG4GMTWS; -.
DR   PhylomeDB; Q9Z0E0; -.
DR   NextBio; 304631; -.
DR   ArrayExpress; Q9Z0E0; -.
DR   Bgee; Q9Z0E0; -.
DR   CleanEx; MM_NCDN; -.
DR   Genevestigator; Q9Z0E0; -.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR   GO; GO:0045453; P:bone resorption; IDA:MGI.
DR   InterPro; IPR008709; Neurochondrin.
DR   PANTHER; PTHR13109; Neurochondrin; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell projection; Cytoplasm; Phosphoprotein.
FT   CHAIN         1    729       Neurochondrin.
FT                                /FTId=PRO_0000324618.
FT   MOD_RES      50     50       Phosphoserine (By similarity).
FT   MOD_RES      60     60       Phosphothreonine (By similarity).
FT   VAR_SEQ       1     17       Missing (in isoform 2).
FT                                /FTId=VSP_032317.
FT   CONFLICT    109    109       A -> S (in Ref. 5; AAH17126).
FT   CONFLICT    164    164       G -> D (in Ref. 3; BAE41841).
SQ   SEQUENCE   729 AA;  78895 MW;  F23C439BDE1EDD9C CRC64;
     MSCCDLAAAG QLGKAGIMAS DCEPALNQAE SRNPTLERYL GALREAKNDS EQFAALLLVT
     KAVKAGDIDA KTRRRIFDAV GFTFPNRLLT TKEAPDGCPD HVLRALGVAL LACFCSDPEL
     ASHPQVLNKI PILSTFLTAR GDPDDAARRS MIDDTYQCLT AVAGTPRGPR HLIAGGTVSA
     LCQAYLGHGY GFDQALALLV GLLAAAETQC WKEAEPDLLA VLRGLSEDFQ RAEDASKFEL
     CQLLPLFLPP TTVPPECHRD LQAGLARILG SKLSSWQRNP ALKLAARLAH ACGSDWIPVG
     SSGSKFLALL VNLACVEVRL ALEETGTEVK EDVVTACYAL MELGIQECTR CEQSLLKEPQ
     KVQLVSIMKE AIGAVIHYLL QVGPEKQKEP FVFASVRILG AWLAEETSSL RKEVCQLLPF
     LVRYAKTLYE EAEEASDISQ QVANLAISPT TPGPSWPGDA LRLLLPGWCH LTVEDGPREI
     LIKEGAPSLL CKYFLQQWEL TSPGHDTSVL PDSVEIGLQT CCHIFLNLVV TAPGLIKRDA
     CFTSLMNTLM TSLPSLVQQQ GRLLLAANVA TLGLLMARLL STSPALQGTP ASRGFFAAAI
     LFLSQSHVAR ATPGSDQAVL ALSPDYEGIW ADLQELWFLG MQAFTGCVPL LPWLAPAALR
     SRWPQELLQL LGSVSPNSVK PEMVAAYQGV LVELARANRL CREAMRLQAG EETASHYRMA
     ALEQCLSEP
//
ID   S22A5_MOUSE             Reviewed;         557 AA.
AC   Q9Z0E8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Solute carrier family 22 member 5;
DE   AltName: Full=High-affinity sodium-dependent carnitine cotransporter;
DE   AltName: Full=Organic cation/carnitine transporter 2;
GN   Name=Slc22a5; Synonyms=Octn2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   MEDLINE=99113835; PubMed=9916797; DOI=10.1038/5030;
RA   Nezu J., Tamai I., Oku A., Ohashi R., Yabuuchi H., Hashimoto N.,
RA   Nikaido H., Sai Y., Koizumi A., Shoji Y., Takada G., Matsuishi T.,
RA   Yashino M., Kato H., Ohura T., Tsujimoto G., Hayakawa J., Shimane M.,
RA   Tsuji A.;
RT   "Primary systemic carnitine deficiency is caused by mutations in a
RT   gene encoding sodium ion-dependent carnitine transporter.";
RL   Nat. Genet. 21:91-94(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT JVS ARG-352.
RC   STRAIN=C3H;
RX   MEDLINE=99057546; PubMed=9837751; DOI=10.1006/bbrc.1998.9708;
RA   Lu K., Nishimori H., Nakamura Y., Shima K., Kuwajima M.;
RT   "A missense mutation of mouse OCTN2, a sodium-dependent carnitine
RT   cotransporter, in the juvenile visceral steatosis mouse.";
RL   Biochem. Biophys. Res. Commun. 252:590-594(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX   MEDLINE=99384224; PubMed=10454528;
RA   Wu X., Huang W., Prasad P.D., Seth P., Rajan D.P., Leibach F.H.,
RA   Chen J., Conway S.J., Ganapathy V.;
RT   "Functional characteristics and tissue distribution pattern of organic
RT   cation transporter 2 (OCTN2), an organic cation/carnitine
RT   transporter.";
RL   J. Pharmacol. Exp. Ther. 290:1482-1492(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=20568258; PubMed=11010964; DOI=10.1074/jbc.M005340200;
RA   Tamai I., Ohashi R., Nezu J., Sai Y., Kobayashi D., Oku A.,
RA   Shimane M., Tsuji A.;
RT   "Molecular and functional characterization of organic cation/carnitine
RT   transporter family in mice.";
RL   J. Biol. Chem. 275:40064-40072(2000).
RN   [6]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH PDZK1.
RX   PubMed=15523054; DOI=10.1124/mol.104.002212;
RA   Kato Y., Sai Y., Yoshida K., Watanabe C., Hirata T., Tsuji A.;
RT   "PDZK1 directly regulates the function of organic cation/carnitine
RT   transporter OCTN2.";
RL   Mol. Pharmacol. 67:734-743(2005).
CC   -!- FUNCTION: Sodium-ion dependent, high affinity carnitine
CC       transporter. Involved in the active cellular uptake of carnitine.
CC       Transports one sodium ion with one molecule of carnitine. Also
CC       transports organic cations such as tetraethylammonium (TEA)
CC       without the involvement of sodium. Also relative uptake activity
CC       ratio of carnitine to TEA is 11.3.
CC   -!- SUBUNIT: Interacts with PDZK1.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane; Multi-pass membrane
CC       protein. Note=Colocalizes with PDZK1 on apical membranes of kidney
CC       proximal tubules.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed in kidney, liver
CC       and testis.
CC   -!- DISEASE: Note=Defects in Slc22a5 are the cause of the juvenile
CC       visceral steatosis (JVS) phenotype. JVS is an autosomal recessive
CC       animal model of systemic carnitine deficiency.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Organic
CC       cation transporter family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB015800; BAA36590.1; -; mRNA.
DR   EMBL; AF111425; AAC99787.1; -; mRNA.
DR   EMBL; AF110417; AAD54060.1; -; mRNA.
DR   EMBL; BC031118; AAH31118.1; -; mRNA.
DR   IPI; IPI00129041; -.
DR   RefSeq; NP_035526.1; NM_011396.3.
DR   UniGene; Mm.42253; -.
DR   ProteinModelPortal; Q9Z0E8; -.
DR   STRING; Q9Z0E8; -.
DR   PRIDE; Q9Z0E8; -.
DR   Ensembl; ENSMUST00000019044; ENSMUSP00000019044; ENSMUSG00000018900.
DR   GeneID; 20520; -.
DR   KEGG; mmu:20520; -.
DR   UCSC; uc007ixc.1; mouse.
DR   CTD; 20520; -.
DR   MGI; MGI:1329012; Slc22a5.
DR   GeneTree; ENSGT00600000084173; -.
DR   HOGENOM; HBG713776; -.
DR   HOVERGEN; HBG061545; -.
DR   InParanoid; Q9Z0E8; -.
DR   OMA; FEMFTVL; -.
DR   OrthoDB; EOG4WDDBH; -.
DR   PhylomeDB; Q9Z0E8; -.
DR   NextBio; 298743; -.
DR   ArrayExpress; Q9Z0E8; -.
DR   Bgee; Q9Z0E8; -.
DR   Genevestigator; Q9Z0E8; -.
DR   GermOnline; ENSMUSG00000018900; Mus musculus.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031526; C:brush border membrane; IDA:BHF-UCL.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0015226; F:carnitine transporter activity; IDA:MGI.
DR   GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0007512; P:adult heart development; IMP:MGI.
DR   GO; GO:0009437; P:carnitine metabolic process; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR   GO; GO:0048608; P:reproductive structure development; IMP:MGI.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR020846; Major_facilitator_SF.
DR   InterPro; IPR016196; MFS_general_subst_transpt.
DR   InterPro; IPR004749; Orgcat_transp.
DR   InterPro; IPR005828; Sub_transporter.
DR   InterPro; IPR005829; Sugar_transporter_CS.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   SUPFAM; SSF103473; MFS_gen_substrate_transporter; 1.
DR   TIGRFAMs; TIGR00898; 2A0119; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Disease mutation; Glycoprotein;
KW   Ion transport; Membrane; Nucleotide-binding; Phosphoprotein; Sodium;
KW   Sodium transport; Symport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    557       Solute carrier family 22 member 5.
FT                                /FTId=PRO_0000220501.
FT   TOPO_DOM      1     20       Cytoplasmic (Potential).
FT   TRANSMEM     21     41       Helical; Name=1; (Potential).
FT   TOPO_DOM     42    142       Extracellular (Potential).
FT   TRANSMEM    143    163       Helical; Name=2; (Potential).
FT   TOPO_DOM    164    172       Cytoplasmic (Potential).
FT   TRANSMEM    173    193       Helical; Name=3; (Potential).
FT   TOPO_DOM    194    197       Extracellular (Potential).
FT   TRANSMEM    198    218       Helical; Name=4; (Potential).
FT   TOPO_DOM    219    232       Cytoplasmic (Potential).
FT   TRANSMEM    233    253       Helical; Name=5; (Potential).
FT   TOPO_DOM    254    257       Extracellular (Potential).
FT   TRANSMEM    258    278       Helical; Name=6; (Potential).
FT   TOPO_DOM    279    341       Cytoplasmic (Potential).
FT   TRANSMEM    342    362       Helical; Name=7; (Potential).
FT   TOPO_DOM    363    373       Extracellular (Potential).
FT   TRANSMEM    374    394       Helical; Name=8; (Potential).
FT   TOPO_DOM    395    406       Cytoplasmic (Potential).
FT   TRANSMEM    407    427       Helical; Name=9; (Potential).
FT   TOPO_DOM    428    430       Extracellular (Potential).
FT   TRANSMEM    431    451       Helical; Name=10; (Potential).
FT   TOPO_DOM    452    462       Cytoplasmic (Potential).
FT   TRANSMEM    463    483       Helical; Name=11; (Potential).
FT   TOPO_DOM    484    488       Extracellular (Potential).
FT   TRANSMEM    489    509       Helical; Name=12; (Potential).
FT   TOPO_DOM    510    557       Cytoplasmic (Potential).
FT   NP_BIND     218    225       ATP (Potential).
FT   MOD_RES     486    486       Phosphotyrosine (By similarity).
FT   CARBOHYD     57     57       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     64     64       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     91     91       N-linked (GlcNAc...) (Potential).
FT   VARIANT     352    352       L -> R (in JVS).
SQ   SEQUENCE   557 AA;  62780 MW;  6093F0EE9612B204 CRC64;
     MRDYDEVTAF LGEWGPFQRL IFFLLSASII PNGFNGMSIV FLAGTPEHRC LVPHTVNLSS
     AWRNHSIPLE TKDGRQVPQK CRRYRLATIA NFSELGLEPG RDVDLEQLEQ ESCLDGWEYD
     KDVFLSTIVT EWDLVCKDDW KAPLTTSLFF VGVLMGSFIS GQLSDRFGRK NVLFLTMGMQ
     TGFSFLQVFS VNFEMFTVLF VLVGMGQISN YVAAFVLGTE ILSKSIRIIF ATLGVCIFYA
     FGFMVLPLFA YFIRDWRMLL LALTVPGVLC GALWWFIPES PRWLISQGRI KEAEVIIRKA
     AKINGIVAPS TIFDPSELQD LNSTKPQLHH IYDLIRTRNI RVITIMSIIL WLTISVGYFG
     LSLDTPNLHG DIYVNCFLLA AVEVPAYVLA WLLLQYLPRR YSISAALFLG GSVLLFMQLV
     PSELFYLSTA LVMVGKFGIT SAYSMVYVYT AELYPTVVRN MGVGVSSTAS RLGSILSPYF
     VYLGAYDRFL PYILMGSLTI LTAILTLFFP ESFGVPLPDT IDQMLRVKGI KQWQIQSQTR
     MQKDGEESPT VLKSTAF
//
ID   GIPC1_MOUSE             Reviewed;         333 AA.
AC   Q9Z0G0;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=PDZ domain-containing protein GIPC1;
DE   AltName: Full=GAIP C-terminus-interacting protein;
DE   AltName: Full=RGS-GAIP-interacting protein;
DE   AltName: Full=RGS19-interacting protein 1;
DE   AltName: Full=SemaF cytoplasmic domain-associated protein 1;
DE            Short=SEMCAP-1;
DE   AltName: Full=Synectin;
GN   Name=Gipc1; Synonyms=Gipc, Rgs19ip1, Semcap1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH RGS19.
RX   MEDLINE=98445373; PubMed=9770488; DOI=10.1073/pnas.95.21.12340;
RA   De Vries L., Lou X., Zhao G., Zheng B., Farquhar M.G.;
RT   "GIPC, a PDZ domain containing protein, interacts specifically with
RT   the C-terminus of RGS-GAIP.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:12340-12345(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH SEM4C.
RX   MEDLINE=99253973; PubMed=10318831; DOI=10.1074/jbc.274.20.14137;
RA   Wang L.-H., Kalb R.G., Strittmatter S.M.;
RT   "A PDZ protein regulates the distribution of the transmembrane
RT   semaphorin, M-SemF.";
RL   J. Biol. Chem. 274:14137-14146(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH SDC4.
RX   MEDLINE=20372671; PubMed=10911369;
RX   DOI=10.1002/1097-4652(200009)184:3<373::AID-JCP12>3.0.CO;2-I;
RA   Gao Y., Li M., Chen W., Simons M.;
RT   "Synectin, syndecan-4 cytoplasmic domain binding PDZ protein, inhibits
RT   cell migration.";
RL   J. Cell. Physiol. 184:373-379(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Inhibits endothelial cell migartion (in vitro). May be
CC       involved in G protein-linked signaling (By similarity).
CC   -!- SUBUNIT: Interacts with GLUT1 (C-terminus), ACTN1, KIF1B, MYO6 and
CC       PLEKHG5 (By similarity). Interacts with RGS19 C-terminus.
CC       Interacts with SDC4/syndecan-4 and SEMA4C/semaphorin-4C.
CC   -!- INTERACTION:
CC       Q64151:Sema4c; NbExp=5; IntAct=EBI-300855, EBI-987075;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane;
CC       Peripheral membrane protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- SIMILARITY: Belongs to the GIPC family.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
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DR   EMBL; AF089818; AAC67550.1; -; mRNA.
DR   EMBL; AF104358; AAD12262.1; -; mRNA.
DR   EMBL; AF061263; AAC72311.1; -; mRNA.
DR   EMBL; AK086506; BAC39680.1; -; mRNA.
DR   EMBL; BC003490; AAH03490.1; -; mRNA.
DR   IPI; IPI00129107; -.
DR   RefSeq; NP_061241.1; NM_018771.3.
DR   UniGene; Mm.20945; -.
DR   ProteinModelPortal; Q9Z0G0; -.
DR   SMR; Q9Z0G0; 127-217.
DR   IntAct; Q9Z0G0; 12.
DR   MINT; MINT-91878; -.
DR   STRING; Q9Z0G0; -.
DR   PhosphoSite; Q9Z0G0; -.
DR   PRIDE; Q9Z0G0; -.
DR   Ensembl; ENSMUST00000019577; ENSMUSP00000019577; ENSMUSG00000019433.
DR   GeneID; 67903; -.
DR   KEGG; mmu:67903; -.
DR   UCSC; uc009mkr.1; mouse.
DR   CTD; 67903; -.
DR   MGI; MGI:1926252; Gipc1.
DR   eggNOG; roNOG13185; -.
DR   GeneTree; ENSGT00390000003420; -.
DR   HOGENOM; HBG381653; -.
DR   HOVERGEN; HBG000898; -.
DR   InParanoid; Q9Z0G0; -.
DR   OMA; SFMGIND; -.
DR   OrthoDB; EOG498V1F; -.
DR   PhylomeDB; Q9Z0G0; -.
DR   NextBio; 325906; -.
DR   ArrayExpress; Q9Z0G0; -.
DR   Bgee; Q9Z0G0; -.
DR   CleanEx; MM_GIPC1; -.
DR   Genevestigator; Q9Z0G0; -.
DR   GermOnline; ENSMUSG00000019433; Mus musculus.
DR   GO; GO:0043198; C:dendritic shaft; IDA:MGI.
DR   GO; GO:0043197; C:dendritic spine; IDA:MGI.
DR   GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR   GO; GO:0012506; C:vesicle membrane; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IPI:MGI.
DR   GO; GO:0005096; F:GTPase activator activity; TAS:MGI.
DR   GO; GO:0017022; F:myosin binding; IPI:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
DR   GO; GO:0043542; P:endothelial cell migration; IMP:MGI.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; TAS:MGI.
DR   GO; GO:0014047; P:glutamate secretion; IMP:MGI.
DR   GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
DR   GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
DR   GO; GO:0006605; P:protein targeting; IMP:MGI.
DR   GO; GO:0031647; P:regulation of protein stability; IDA:BHF-UCL.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; IMP:MGI.
DR   GO; GO:0007268; P:synaptic transmission; IMP:MGI.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR017379; UCP038083_PDZ.
DR   Pfam; PF00595; PDZ; 1.
DR   PIRSF; PIRSF038083; UCP038083_GIPC; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Membrane.
FT   CHAIN         1    333       PDZ domain-containing protein GIPC1.
FT                                /FTId=PRO_0000087493.
FT   DOMAIN      133    213       PDZ.
FT   CONFLICT     39     39       A -> G (in Ref. 1; AAC67550).
FT   CONFLICT     53     53       A -> S (in Ref. 1; AAC67550).
FT   CONFLICT    141    141       E -> D (in Ref. 1; AAC67550).
FT   CONFLICT    226    226       A -> S (in Ref. 1; AAC67550).
SQ   SEQUENCE   333 AA;  36129 MW;  52E5ED6092EA9300 CRC64;
     MPLGLGRRKK APPLVENEEA EPSRSGLGVG EPGPLGGSAA GESQMGLPPP PAALRPRLVF
     HTQLAHGSPT GRIEGFTNVK ELYGKIAEAF RLPAAEVMFC TLNTHKVDMD KLLGGQIGLE
     DFIFAHVKGQ RKEVEVFKSE EALGLTITDN GAGYAFIKRI KEGSVIDHIQ LISVGDMIEA
     INGQSLLGCR HYEVARLLKE LPRGRTFTLK LTEPRKAFDM ISQRSAGGHP GSGPQLGTGR
     GTLRLRSRGP ATVEDLPSAF EEKAIEKVDD LLESYMGIRD TELAATMVEL GKDKRNPDEL
     AEALDERLGD FAFPDEFVFD VWGAIGDAKV GRY
//
ID   ZBT22_MOUSE             Reviewed;         638 AA.
AC   Q9Z0G7;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Zinc finger and BTB domain-containing protein 22;
DE   AltName: Full=Protein BING1;
DE   AltName: Full=Zinc finger protein 297;
GN   Name=Zbtb22; Synonyms=Bing1, Zfp297, Znf297;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129/SvJ;
RA   Rowen L., Qin S., Madan A., Loretz C., James R., Dors M., Mix L.,
RA   Hall J., Lasky S., Hood L.;
RT   "Sequence of the mouse major histocompatibility complex class II
RT   region.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Embryo, and Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family.
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC   -!- SIMILARITY: Contains 3 C2H2-type zinc fingers.
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DR   EMBL; AF110520; AAC97972.1; -; Genomic_DNA.
DR   EMBL; AF100956; AAC69892.1; -; Genomic_DNA.
DR   EMBL; BC026964; AAH26964.1; -; mRNA.
DR   EMBL; BC052154; AAH52154.1; -; mRNA.
DR   IPI; IPI00129119; -.
DR   RefSeq; NP_065650.1; NM_020625.3.
DR   UniGene; Mm.154457; -.
DR   ProteinModelPortal; Q9Z0G7; -.
DR   SMR; Q9Z0G7; 32-149, 409-562.
DR   STRING; Q9Z0G7; -.
DR   PRIDE; Q9Z0G7; -.
DR   Ensembl; ENSMUST00000053429; ENSMUSP00000057466; ENSMUSG00000051390.
DR   GeneID; 81630; -.
DR   KEGG; mmu:81630; -.
DR   UCSC; uc008cac.1; mouse.
DR   CTD; 81630; -.
DR   MGI; MGI:1931870; Zbtb22.
DR   GeneTree; ENSGT00580000081322; -.
DR   HOGENOM; HBG716388; -.
DR   HOVERGEN; HBG056510; -.
DR   InParanoid; Q9Z0G7; -.
DR   OMA; YFSPRES; -.
DR   OrthoDB; EOG498V19; -.
DR   PhylomeDB; Q9Z0G7; -.
DR   NextBio; 350418; -.
DR   ArrayExpress; Q9Z0G7; -.
DR   Bgee; Q9Z0G7; -.
DR   Genevestigator; Q9Z0G7; -.
DR   GermOnline; ENSMUSG00000051390; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR013069; BTB_POZ.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 3.
DR   Pfam; PF00651; BTB; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE   2: Evidence at transcript level;
KW   DNA-binding; Metal-binding; Nucleus; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    638       Zinc finger and BTB domain-containing
FT                                protein 22.
FT                                /FTId=PRO_0000047518.
FT   DOMAIN       57    121       BTB.
FT   ZN_FING     483    504       C2H2-type 1; atypical.
FT   ZN_FING     510    532       C2H2-type 2.
FT   ZN_FING     538    559       C2H2-type 3.
SQ   SEQUENCE   638 AA;  66029 MW;  40343A4C6CB5EF6C CRC64;
     MEPSALSPSG ATLPLPLSLA PPPLPLPAAA VVHVSFPEVT SALLESLNQQ RLQGQLCDVS
     IRVQGREFRA HRAVLAASSP YFHDQVLLKG MTSISLPSVM DPGAFETVLA SAYTGRLSMA
     AADIVNFLTV GSVLQMWHIV DKCTELLREG RSAATTTTVT TAAAPSVSVP CASVPSGNGG
     TVAPATVGSV RSHTSSRASE NQSPSSSNYF SPRESTDFSS TSQDAFVASA AGSGNRRDGG
     PVFPAPVVGS AGTTSGKLLL EADELCDDGG DGRGAVAPGA GLRRSNCMPA SAVPQKHWVY
     VKQARNCPAP ASLVHQDPDL EDEEEEEDLV LTCEDDEDEE MGGGSGVPAG GEPEATLSIS
     DVRTLTEPAD KGEEQVNFCE SSNDFGPYEG GGAGAGLDDP GGPTPSSYAL THPPRPLLPL
     DVPGNQILVF PSSSSQAPGQ PPGNTAEHGA VTLGGTSAVG LGIPSGSGGA PGGTGNSDGN
     KIFLCHCGKA FSHKSMRDRH VNMHLNLRPF DCPVCNKKFK MKHHLTEHMK THTGLKPYEC
     SVCAKKFMWR DSFMRHRGHC ERRHRMGVGG VGSGPGPGPG PGTPSGPALQ PKRESSTVGG
     GSGDEANSAT PPSHRRVWSP PSVHKVEMDF SGGGGAAH
//
ID   CLIP2_MOUSE             Reviewed;        1047 AA.
AC   Q9Z0H8; Q7TSI9; Q8CHU1; Q9EP81;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   08-MAR-2011, entry version 81.
DE   RecName: Full=CAP-Gly domain-containing linker protein 2;
DE   AltName: Full=Cytoplasmic linker protein 115;
DE            Short=CLIP-115;
DE   AltName: Full=Cytoplasmic linker protein 2;
GN   Name=Clip2; Synonyms=Cyln2, Kiaa0291;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129;
RX   MEDLINE=99017971; PubMed=9799601; DOI=10.1006/geno.1998.5529;
RA   Hoogenraad C.C., Eussen B.H.J., Langeveld A., van Haperen R.,
RA   Winterberg S., Wouters C.H., Grosveld F., de Zeeuw C.I., Galjart N.;
RT   "The murine CYLN2 gene: genomic organization, chromosome localization,
RT   and comparison to the human gene that is located within the 7q11.23
RT   Williams syndrome critical region.";
RL   Genomics 53:348-358(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/Sv;
RA   Green E.D.;
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   INTERACTION WITH CLASP1 AND CLASP2.
RX   MEDLINE=21185938; PubMed=11290329; DOI=10.1016/S0092-8674(01)00288-4;
RA   Akhmanova A., Hoogenraad C.C., Drabek K., Stepanova T., Dortland B.,
RA   Verkerk T., Vermeulen W., Burgering B.M., de Zeeuw C.I., Grosveld F.,
RA   Galjart N.;
RT   "Clasps are CLIP-115 and -170 associating proteins involved in the
RT   regional regulation of microtubule dynamics in motile fibroblasts.";
RL   Cell 104:923-935(2001).
RN   [5]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   MEDLINE=98087115; PubMed=9427243; DOI=10.1016/S0896-6273(00)80411-0;
RA   de Zeeuw C.I., Hoogenraad C.C., Goedknegt E., Hertzberg E.,
RA   Neubauer A., Grosveld F.G., Galjart N.J.;
RT   "CLIP-115, a novel brain specific cytoplasmic linker protein, mediates
RT   the localisation of dendritic lamellar bodies.";
RL   Neuron 19:1187-1199(1997).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Seems to link microtubules to dendritic lamellar body
CC       (DLB), a membranous organelle predominantly present in bulbous
CC       dendritic appendages of neurons linked by dendrodendritic gap
CC       junctions. May operates in the control of brain-specific organelle
CC       translocations (By similarity).
CC   -!- SUBUNIT: Interacts with CLASP1 and CLASP2.
CC   -!- INTERACTION:
CC       Q80TV8:Clasp1; NbExp=1; IntAct=EBI-775282, EBI-908322;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity). Note=Associated with the
CC       cytoskeleton (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Z0H8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Z0H8-2; Sequence=VSP_015683;
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, and very low levels in
CC       kidneys.
CC   -!- DEVELOPMENTAL STAGE: Expressed at E10.5, expression declines until
CC       birth after which it suddenly increases. Expression gradually
CC       decreases until postnatal day 10, (the day when DLBs start to
CC       occur), then again increases and reaches the levels present in
CC       adult brain.
CC   -!- SIMILARITY: Contains 2 CAP-Gly domains.
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DR   EMBL; AJ228863; CAA13068.1; -; Genomic_DNA.
DR   EMBL; AJ228865; CAA13069.1; -; Genomic_DNA.
DR   EMBL; AJ228868; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228869; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228870; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228872; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228876; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228880; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228867; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228875; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228871; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228873; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228877; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228866; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228879; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228878; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AJ228874; CAA13069.1; JOINED; Genomic_DNA.
DR   EMBL; AF289667; AAF99340.1; -; Genomic_DNA.
DR   EMBL; AF289664; AAF99333.1; -; Genomic_DNA.
DR   EMBL; BC039162; AAH39162.1; -; mRNA.
DR   EMBL; BC053048; AAH53048.1; -; mRNA.
DR   IPI; IPI00408543; -.
DR   IPI; IPI00467854; -.
DR   PIR; T42720; T42720.
DR   RefSeq; NP_001034251.1; NM_001039162.1.
DR   RefSeq; NP_034120.2; NM_009990.2.
DR   UniGene; Mm.255138; -.
DR   ProteinModelPortal; Q9Z0H8; -.
DR   SMR; Q9Z0H8; 1-156, 174-345.
DR   IntAct; Q9Z0H8; 3.
DR   STRING; Q9Z0H8; -.
DR   PhosphoSite; Q9Z0H8; -.
DR   PRIDE; Q9Z0H8; -.
DR   Ensembl; ENSMUST00000036999; ENSMUSP00000037431; ENSMUSG00000063146.
DR   Ensembl; ENSMUST00000100647; ENSMUSP00000098212; ENSMUSG00000063146.
DR   GeneID; 269713; -.
DR   KEGG; mmu:269713; -.
DR   UCSC; uc008zwi.1; mouse.
DR   UCSC; uc008zwj.1; mouse.
DR   CTD; 269713; -.
DR   MGI; MGI:1313136; Clip2.
DR   eggNOG; roNOG05148; -.
DR   GeneTree; ENSGT00550000074375; -.
DR   HOGENOM; HBG715534; -.
DR   HOVERGEN; HBG007123; -.
DR   InParanoid; Q9Z0H8; -.
DR   OMA; WVNGVKP; -.
DR   OrthoDB; EOG4X3H0M; -.
DR   NextBio; 393005; -.
DR   ArrayExpress; Q9Z0H8; -.
DR   Bgee; Q9Z0H8; -.
DR   CleanEx; MM_CLIP2; -.
DR   Genevestigator; Q9Z0H8; -.
DR   GermOnline; ENSMUSG00000063146; Mus musculus.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IDA:MGI.
DR   InterPro; IPR023092; CAP-Gly_CS.
DR   InterPro; IPR000938; CAP-Gly_domain.
DR   Gene3D; G3DSA:2.30.30.190; CAP-Gly_domain; 2.
DR   Pfam; PF01302; CAP_GLY; 2.
DR   SUPFAM; SSF74924; CAP-Gly_domain; 2.
DR   PROSITE; PS00845; CAP_GLY_1; 2.
DR   PROSITE; PS50245; CAP_GLY_2; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Microtubule; Phosphoprotein; Repeat.
FT   CHAIN         1   1047       CAP-Gly domain-containing linker protein
FT                                2.
FT                                /FTId=PRO_0000083516.
FT   DOMAIN      100    142       CAP-Gly 1.
FT   DOMAIN      240    282       CAP-Gly 2.
FT   COILED      355    525       Potential.
FT   COILED      564    637       Potential.
FT   COILED      677   1017       Potential.
FT   COMPBIAS    315    346       Ser-rich.
FT   MOD_RES      50     50       Phosphoserine.
FT   MOD_RES     203    203       Phosphoserine (By similarity).
FT   MOD_RES     205    205       Phosphoserine (By similarity).
FT   MOD_RES     208    208       Phosphoserine (By similarity).
FT   MOD_RES     212    212       Phosphoserine (By similarity).
FT   MOD_RES     353    353       Phosphoserine.
FT   MOD_RES     924    924       Phosphoserine (By similarity).
FT   VAR_SEQ     462    496       Missing (in isoform 2).
FT                                /FTId=VSP_015683.
FT   CONFLICT     25     25       V -> I (in Ref. 3; AAH39162).
FT   CONFLICT     59     59       T -> A (in Ref. 1; CAA13068/CAA13069).
FT   CONFLICT     79     79       D -> H (in Ref. 1; CAA13068/CAA13069).
FT   CONFLICT    127    127       G -> A (in Ref. 1; CAA13068/CAA13069).
FT   CONFLICT    334    335       RP -> PA (in Ref. 1; CAA13068/CAA13069).
FT   CONFLICT    356    356       T -> I (in Ref. 1; CAA13068/CAA13069).
FT   CONFLICT    559    559       R -> D (in Ref. 1; CAA13068/CAA13069).
FT   CONFLICT    713    719       SQHRLEL -> AASAEA (in Ref. 1; CAA13068).
FT   CONFLICT    733    733       A -> V (in Ref. 1; CAA13068/CAA13069).
FT   CONFLICT    856    856       A -> V (in Ref. 1; CAA13068/CAA13069).
FT   CONFLICT   1003   1003       N -> D (in Ref. 3; AAH39162).
SQ   SEQUENCE   1047 AA;  115910 MW;  8F46948122F58872 CRC64;
     MQKPSGLKPP GRGGKHSSPV GRPSVGSASS SVVASTSGSK EGSPLHKQAS GPSSSGAATT
     VSEKPGPKAA EVGDDFLGDF VVGERVWVNG VKPGVVQYLG ETQFAPGQWA GVVLDDPVGK
     NDGAVGGVRY FECPALQGIF TRPSKLTRQP TAEGSGSDTH SVESLTAQNL SLHSGTATPP
     LTGRVIPLRE SVLNSSVKTG NESGSNLSDS GSVKRGDKDL HLGDRVLVGG TKTGVVRYVG
     ETDFAKGEWC GVELDEPLGK NDGAVAGTRY FQCPPKFGLF APIHKVIRIG FPSTSPAKAK
     KTKRMAMGVS ALTHSPSSSS ISSVSSVASS VGGRPSRSGL LTETSSRYAR KISGTTALQE
     ALKEKQQHIE QLLAERDLER AEVAKATSHI CEVEKEIALL KAQHEQYVAE AEEKLQRARL
     LVENVRKEKV DLSNQLEEER RKVEDLQFRV EEESITKGDL ETQTQLEHAR IGELEQSLLL
     EKAQAERLLR ELADNRLTTV AEKSRVLQLE EELSLRRGEI EELQHCLLQS GPPPADHPEA
     AETLRLRERL LSASKEHQRD STLLQDKYEH MLKTYQTEVD KLRAANEKYA QEVADLKAKV
     QQATTENMGL MDNWKSKLDS LASDHQKSLE DLKATLNSGP GAQQKEIGEL KALVEGIKME
     HQLELGNLQA KHDLETAMHG KEKEGLRQKL QEVQEELAGL QQHWREQLEE QASQHRLELQ
     EAQDQCRDAQ LRAQELEGLD VEYRGQAQAI EFLKEQISLA EKKMLDYEML QRAEAQSRQE
     AERLREKLLV AENRLQAAES LCSAQHSHVI ESSDLSEETI RMKETVEGLQ DKLNKRDKEV
     TALTSQMDML RAQVSALENK CKSGEKKIDS LLKEKRRLEA ELEAVSRKTH DASGQLVHIS
     QELLRKERSL NELRVLLLEA NRHSPGPERD LSREVHKAEW RIKEQKLKDD IRGLREKLTG
     LDKEKSLSEQ RRYSLIDPAS PPELLKLQHQ LVSTEDALRD ALNQAQQVER LVEALRGCSD
     RTQTISNSGS ANGIHQPDKA HKQEDKH
//
ID   NOS1_MOUSE              Reviewed;        1429 AA.
AC   Q9Z0J4; Q3UR10; Q64208;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-FEB-2011, entry version 115.
DE   RecName: Full=Nitric oxide synthase, brain;
DE            EC=1.14.13.39;
DE   AltName: Full=Constitutive NOS;
DE   AltName: Full=NC-NOS;
DE   AltName: Full=NOS type I;
DE   AltName: Full=Neuronal NOS;
DE            Short=N-NOS;
DE            Short=nNOS;
DE   AltName: Full=Peptidyl-cysteine S-nitrosylase NOS1;
DE   AltName: Full=bNOS;
GN   Name=Nos1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS N-NOS-1 AND N-NOS-2).
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=93312283; PubMed=7686743; DOI=10.1006/bbrc.1993.1726;
RA   Ogura T., Yokoyama T., Fujisawa H., Kurashima Y., Esumi H.;
RT   "Structural diversity of neuronal oxide synthase mRNA in the nervous
RT   system.";
RL   Biochem. Biophys. Res. Commun. 193:1014-1022(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM NNOS MU).
RC   TISSUE=Skeletal muscle;
RX   MEDLINE=96212184; PubMed=8626668; DOI=10.1074/jbc.271.19.11204;
RA   Silvagno F., Xia H., Bredt D.S.;
RT   "Neuronal nitric-oxide synthase-mu, an alternatively spliced isoform
RT   expressed in differentiated skeletal muscle.";
RL   J. Biol. Chem. 271:11204-11208(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1320-1429.
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   ALTERNATIVE SPLICING (ISOFORMS NNOS BETA; NNOS GAMMA AND NNOS MU).
RX   MEDLINE=97351924; PubMed=9208206;
RA   Brenman J.E., Xia H., Chao D.S., Black S.M., Bredt D.S.;
RT   "Regulation of neuronal nitric oxide synthase through alternative
RT   transcripts.";
RL   Dev. Neurosci. 19:224-231(1997).
RN   [5]
RP   INTERACTION WITH DLG4.
RX   MEDLINE=20090929; PubMed=10623522; DOI=10.1006/jmbi.1999.3350;
RA   Tochio H., Hung F., Li M., Bredt D.S., Zhang M.;
RT   "Solution structure and backbone dynamics of the second PDZ domain of
RT   postsynaptic density-95.";
RL   J. Mol. Biol. 295:225-237(2000).
RN   [6]
RP   INTERACTION WITH RASD1 AND CAPON.
RX   MEDLINE=20537828; PubMed=11086993; DOI=10.1016/S0896-6273(00)00095-7;
RA   Fang M., Jaffrey S.R., Sawa A., Ye K., Luo X., Snyder S.H.;
RT   "Dexras1: a G protein specifically coupled to neuronal nitric oxide
RT   synthase via CAPON.";
RL   Neuron 28:183-193(2000).
RN   [7]
RP   INTERACTION WITH HTR4.
RX   PubMed=15466885; DOI=10.1242/jcs.01379;
RA   Joubert L., Hanson B., Barthet G., Sebben M., Claeysen S., Hong W.,
RA   Marin P., Dumuis A., Bockaert J.;
RT   "New sorting nexin (SNX27) and NHERF specifically interact with the 5-
RT   HT4a receptor splice variant: roles in receptor targeting.";
RL   J. Cell Sci. 117:5367-5379(2004).
RN   [8]
RP   FUNCTION AS NITROSYLASE.
RX   PubMed=17293453; DOI=10.1073/pnas.0611620104;
RA   Mustafa A.K., Kumar M., Selvakumar B., Ho G.P., Ehmsen J.T.,
RA   Barrow R.K., Amzel L.M., Snyder S.H.;
RT   "Nitric oxide S-nitrosylates serine racemase, mediating feedback
RT   inhibition of D-serine formation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2950-2955(2007).
RN   [9]
RP   INTERACTION WITH SLC6A4.
RX   PubMed=17452640; DOI=10.1073/pnas.0610964104;
RA   Chanrion B., Mannoury la Cour C., Bertaso F., Lerner-Natoli M.,
RA   Freissmuth M., Millan M.J., Bockaert J., Marin P.;
RT   "Physical interaction between the serotonin transporter and neuronal
RT   nitric oxide synthase underlies reciprocal modulation of their
RT   activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8119-8124(2007).
CC   -!- FUNCTION: Produces nitric oxide (NO) which is a messenger molecule
CC       with diverse functions throughout the body. In the brain and
CC       peripheral nervous system, NO displays many properties of a
CC       neurotransmitter. Probably has nitrosylase activity and mediates
CC       cysteine S-nitrosylation of cytoplasmic target proteins such SRR.
CC       Isoform NNOS Mu may be an effector enzyme for the dystrophin
CC       complex.
CC   -!- CATALYTIC ACTIVITY: L-arginine + n NADPH + n H(+) + m O(2) =
CC       citrulline + nitric oxide + n NADP(+).
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- COFACTOR: Binds 1 FAD (By similarity).
CC   -!- COFACTOR: Binds 1 FMN (By similarity).
CC   -!- COFACTOR: Tetrahydrobiopterin (BH4). May stabilize the dimeric
CC       form of the enzyme (By similarity).
CC   -!- ENZYME REGULATION: Stimulated by calcium/calmodulin. Inhibited by
CC       n-Nos-inhibiting protein (PIN) which may prevent the dimerization
CC       of the protein. Inhibited by NOSIP (By similarity).
CC   -!- SUBUNIT: Homodimer. Forms a ternary complex with CAPON and SYN1.
CC       Interacts with ZDHHC23. Interacts with NOSIP; which may impair its
CC       synaptic location (By similarity). Interacts with DLG4; the
CC       interaction possibly being prevented by the association between
CC       NOS1 and CAPON. Interacts with HTR4. Forms a ternary complex with
CC       CAPON and RASD1. Interacts with VAC14 (By similarity). Interacts
CC       with SLC6A4.
CC   -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma; Peripheral
CC       membrane protein. Cell projection, dendritic spine (By
CC       similarity). Note=In skeletal muscle, it is localized beneath the
CC       sarcolemma of fast-twitch muscle fiber by associating with the
CC       dystrophin glycoprotein complex. In neurons, enriched in dendritic
CC       spines (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=N-NOS-1;
CC         IsoId=Q9Z0J4-1; Sequence=Displayed;
CC       Name=N-NOS-2;
CC         IsoId=Q9Z0J4-2; Sequence=VSP_003578;
CC       Name=NNOS beta;
CC         IsoId=Q9Z0J4-3; Sequence=VSP_003575, VSP_003576;
CC       Name=NNOS gamma;
CC         IsoId=Q9Z0J4-4; Sequence=VSP_003577;
CC       Name=NNOS Mu; Synonyms=Muscle-specific;
CC         IsoId=Q9Z0J4-5; Sequence=VSP_003579;
CC   -!- TISSUE SPECIFICITY: Widely expressed in the nervous system:
CC       expressed in cerebrum, olfactory bulb, hippocampus, midbrain,
CC       cerebellum, pons, medulla oblongata, and spinal cord. Also found
CC       in skeletal muscle, where it is localized beneath the sarcolemma
CC       of fast twitch muscle fibers, and in spleen, heart, kidney, and
CC       liver. N-NOS-1 and N-NOS-2 are found in all parts of the nervous
CC       system. NNOS beta and gamma occur in a region-specific manner in
CC       the brain and NNOS beta expression is developmentally regulated.
CC       NNOS Mu is only found in mature skeletal and cardiac muscles.
CC   -!- INDUCTION: By cholinergic agonists acting at inositol phosphate-
CC       linked muscarinic receptors in cardiac myocytes.
CC   -!- DOMAIN: The PDZ domain in the N-terminal part of the neuronal
CC       isoform participates in protein-protein interaction, and is
CC       responsible for targeting nNos to synaptic membranes in muscles.
CC       Mediates interaction with VAC14 (By similarity).
CC   -!- PTM: Ubiquitinated; mediated by STUB1/CHIP in the presence of
CC       Hsp70 and Hsp40 (in vitro) (By similarity).
CC   -!- DISEASE: Note=In MDX mice (mouse model of dystrophinopathy) the
CC       dystrophin complex is disrupted and nNOS is displaced from
CC       sarcolemma and accumulates in the cytosol.
CC   -!- SIMILARITY: Belongs to the NOS family.
CC   -!- SIMILARITY: Contains 1 FAD-binding FR-type domain.
CC   -!- SIMILARITY: Contains 1 flavodoxin-like domain.
CC   -!- SIMILARITY: Contains 1 PDZ (DHR) domain.
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DR   EMBL; D14552; BAA03415.1; -; mRNA.
DR   EMBL; S81982; AAB36469.1; -; mRNA.
DR   EMBL; AK141904; BAE24878.1; -; mRNA.
DR   IPI; IPI00129191; -.
DR   IPI; IPI00229026; -.
DR   IPI; IPI00229027; -.
DR   IPI; IPI00229030; -.
DR   IPI; IPI00309243; -.
DR   PIR; JN0609; JN0609.
DR   RefSeq; NP_032738.1; NM_008712.2.
DR   UniGene; Mm.442195; -.
DR   UniGene; Mm.44249; -.
DR   PDB; 2O60; X-ray; 1.55 A; B=725-747.
DR   PDBsum; 2O60; -.
DR   ProteinModelPortal; Q9Z0J4; -.
DR   SMR; Q9Z0J4; 12-126, 298-716, 750-1413.
DR   DIP; DIP-31556N; -.
DR   STRING; Q9Z0J4; -.
DR   PhosphoSite; Q9Z0J4; -.
DR   PRIDE; Q9Z0J4; -.
DR   Ensembl; ENSMUST00000111935; ENSMUSP00000107566; ENSMUSG00000029361.
DR   Ensembl; ENSMUST00000111939; ENSMUSP00000107570; ENSMUSG00000029361.
DR   GeneID; 18125; -.
DR   KEGG; mmu:18125; -.
DR   UCSC; uc008zfy.1; mouse.
DR   CTD; 18125; -.
DR   MGI; MGI:97360; Nos1.
DR   GeneTree; ENSGT00600000084325; -.
DR   HOVERGEN; HBG000159; -.
DR   PhylomeDB; Q9Z0J4; -.
DR   BRENDA; 1.14.13.39; 244.
DR   NextBio; 293344; -.
DR   ArrayExpress; Q9Z0J4; -.
DR   Bgee; Q9Z0J4; -.
DR   CleanEx; MM_NOS1; -.
DR   Genevestigator; Q9Z0J4; -.
DR   GermOnline; ENSMUSG00000029361; Mus musculus.
DR   GO; GO:0005856; C:cytoskeleton; IDA:BHF-UCL.
DR   GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR   GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
DR   GO; GO:0045202; C:synapse; IDA:MGI.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004517; F:nitric-oxide synthase activity; IDA:BHF-UCL.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; IMP:BHF-UCL.
DR   GO; GO:0042738; P:exogenous drug catabolic process; IMP:MGI.
DR   GO; GO:0051926; P:negative regulation of calcium ion transport; IMP:MGI.
DR   GO; GO:0051346; P:negative regulation of hydrolase activity; IMP:MGI.
DR   GO; GO:0043267; P:negative regulation of potassium ion transport; IMP:MGI.
DR   GO; GO:0051612; P:negative regulation of serotonin uptake; IDA:UniProtKB.
DR   GO; GO:0006809; P:nitric oxide biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; IDA:MGI.
DR   GO; GO:0035066; P:positive regulation of histone acetylation; IMP:BHF-UCL.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IMP:BHF-UCL.
DR   GO; GO:0002028; P:regulation of sodium ion transport; IMP:MGI.
DR   GO; GO:0006941; P:striated muscle contraction; IMP:MGI.
DR   InterPro; IPR003097; FAD-binding_1.
DR   InterPro; IPR017927; Fd_Rdtase_FAD-bd.
DR   InterPro; IPR001094; Flavdoxin.
DR   InterPro; IPR008254; Flavodoxin/NO_synth.
DR   InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR   InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_dom3.
DR   InterPro; IPR012144; Nitric-oxide_synthase.
DR   InterPro; IPR004030; NO_synthase_oxygenase_dom.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   Gene3D; G3DSA:1.20.990.10; NADPH_Cyt_P450_Rdtase_dom3; 1.
DR   Gene3D; G3DSA:3.90.340.10; NO_synthase_oxygenase_reg; 1.
DR   Pfam; PF00667; FAD_binding_1; 1.
DR   Pfam; PF00258; Flavodoxin_1; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF02898; NO_synthase; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   PIRSF; PIRSF000333; NOS; 1.
DR   PRINTS; PR00369; FLAVODOXIN.
DR   PRINTS; PR00371; FPNCR.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF56512; NO_synthase_oxygenase_reg; 1.
DR   SUPFAM; SSF50156; PDZ; 1.
DR   SUPFAM; SSF63380; Riboflavin_synthase_like_b-brl; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR   PROSITE; PS60001; NOS; 1.
DR   PROSITE; PS50106; PDZ; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calmodulin-binding; Cell membrane;
KW   Cell projection; FAD; FMN; Heme; Iron; Membrane; Metal-binding; NADP;
KW   Oxidoreductase; Ubl conjugation.
FT   CHAIN         1   1429       Nitric oxide synthase, brain.
FT                                /FTId=PRO_0000170922.
FT   DOMAIN       17     99       PDZ.
FT   DOMAIN      755    935       Flavodoxin-like.
FT   DOMAIN      990   1237       FAD-binding FR-type.
FT   NP_BIND     881    912       FMN (By similarity).
FT   NP_BIND    1027   1038       FAD (By similarity).
FT   NP_BIND    1170   1180       FAD (By similarity).
FT   NP_BIND    1245   1263       NADP (By similarity).
FT   NP_BIND    1343   1358       NADP (By similarity).
FT   REGION        1    200       Interaction with NOSIP (By similarity).
FT   REGION      163    240       PIN (nNOS-inhibiting protein) binding (By
FT                                similarity).
FT   REGION      725    745       Calmodulin-binding (Potential).
FT   REGION      750    769       Tetrahydrobiopterin-binding (By
FT                                similarity).
FT   METAL       415    415       Iron (heme axial ligand) (By similarity).
FT   VAR_SEQ       1    331       Missing (in isoform NNOS gamma).
FT                                /FTId=VSP_003577.
FT   VAR_SEQ       1    230       Missing (in isoform NNOS beta).
FT                                /FTId=VSP_003575.
FT   VAR_SEQ     231    236       TGIQVD -> MRGLGS (in isoform NNOS beta).
FT                                /FTId=VSP_003576.
FT   VAR_SEQ     504    608       Missing (in isoform N-NOS-2).
FT                                /FTId=VSP_003578.
FT   VAR_SEQ     839    839       K -> KYPEPLRFFPRKGPSLSHVDSEAHSLVAARDSQHR
FT                                (in isoform NNOS Mu).
FT                                /FTId=VSP_003579.
FT   CONFLICT   1320   1320       K -> Q (in Ref. 3; BAE24878).
FT   HELIX       731    744
SQ   SEQUENCE   1429 AA;  160472 MW;  3782848D65B41BFC CRC64;
     MEEHTFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG AAEQSGLIQA
     GDIILAVNDR PLVDLSYDSA LEVLRGIASE THVVLILRGP EGFTTHLETT FTGDGTPKTI
     RVTQPLGTPT KAVDLSRQPS ASKDQPLAVD RVPGPSNGPQ HAQGRGQGAG SVSQANGVAI
     DPTMKNTKAN LQDSGEQDEL LKEIEPVLSI LTGGGKAVNR GGPAKAEMKD TGIQVDRDLD
     GKLHKAPPLG GENDRVFNDL WGKGNVPVVL NNPYSENEQS PASGKQSPTK NGSPSRCPRF
     LKVKNWETDV VLTDTLHLKS TLETGCTEQI CMGSIMLPSH HIRKSEDVRT KDQLFPLAKE
     FLDQYYSSIK RFGSKAHMDR LEEVNKEIES TSTYQLKDTE LIYGAKHAWR NASRCVGRIQ
     WSKLQVFDAR DCTTAHGMFN YICNHVKYAT NKGNLRSAIT IFPQRTDGKH DFRVWNSQLI
     RYAGYKQPDG STLGDPANVE FTEICIQQGW KPPRGRFDVL PLLLQANGND PELFQIPPEL
     VLEVPIRHPK FDWFKDLGLK WYGLPAVSNM LLEIGGLEFS ACPFSGWYMG TEIGVRDYCD
     NSRYNILEEV AKKMDLDMRK TSSLWKDQAL VEINIAVLYS FQSDKVTIVD HHSATESFIK
     HMENEYRCRG GCPADWVWIV PPMSGSITPV FHQEMLNYRL TPSFEYQPDP WNTHVWKGTN
     GTPTKRRAIG FKKLAEAVKF SAKLMGQAMA KRVKATILYA TETGKSQAYA KTLCEIFKHA
     FDAKAMSMEE YDIVHLEHEA LVLVVTSTFG NGDPPENGEK FGCALMEMRH PNSVQEERKS
     YKVRFNSVSS YSDSRKSSGD GPDLRDNFES TGPLANVRFS VFGLGSRAYP HFCAFGHAVD
     TLLEELGGER ILKMREGDEL CGQEEAFRTW AKKVFKAACD VFCVGDDVNI EKANNSLISN
     DRSWKRNKFR LTYVAEAPEL TQGLSNVHKK RVSAARLLSR QNLQSPKSSR STIFVRLHTN
     GNQELQYQPG DHLGVFPGNH EDLVNALIER LEDAPPANHV VKVEMLEERN TALGVISNWK
     DESRLPPCTI FQAFKYYLDI TTPPTPLQLQ QFASLATNEK EKQRLLVLSK GLQEYEEWKW
     GKNPTMVEVL EEFPSIQMPA TLLLTQLSLL QPRYYSISSS PDMYPDEVHL TVAIVSYHTR
     DGEGPVHHGV CSSWLNRIQA DDVVPCFVRG APSFHLPRNP QVPCILVGPG TGIAPFRSFW
     QQRQFDIQHK GMNPCPMVLV FGCRQSKIDH IYREETLQAK NKGVFRELYT AYSREPDRPK
     KYVQDVLQEQ LAESVYRALK EQGGHIYVCG DVTMAADVLK AIQRIMTQQG KLSEEDAGVF
     ISRLRDDNRY HEDIFGVTLR TYEVTNRLRS ESIAFIEESK KDTDEVFSS
//
ID   CAD20_MOUSE             Reviewed;         801 AA.
AC   Q9Z0M3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Cadherin-20;
DE   AltName: Full=Cadherin-7;
DE   Flags: Precursor;
GN   Name=Cdh20; Synonyms=Cdh7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Swiss; TISSUE=Eye;
RX   MEDLINE=99365480; PubMed=10433813; DOI=10.1006/mcne.1999.0764;
RA   Faulkner-Jones B.E., Godinho L.N., Reese B.E., Pasquini G.F.,
RA   Ruefli A., Tan S.S.;
RT   "Cloning and expression of mouse cadherin-7, a type-II cadherin
RT   isolated from the developing eye.";
RL   Mol. Cell. Neurosci. 14:1-16(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   STRAIN=BALB/c;
RX   PubMed=15273735; DOI=10.1038/sj.onc.1207675;
RA   Moore R., Champeval D., Denat L., Tan S.S., Faure F.,
RA   Julien-Grille S., Larue L.;
RT   "Involvement of cadherins 7 and 20 in mouse embryogenesis and
RT   melanocyte transformation.";
RL   Oncogene 23:6726-6735(2004).
CC   -!- FUNCTION: Cadherins are calcium dependent cell adhesion proteins.
CC       They preferentially interact with themselves in a homophilic
CC       manner in connecting cells; cadherins may thus contribute to the
CC       sorting of heterogeneous cell types (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in brain. Highest level of
CC       expression in the retina. In embryo it is synthesized by the
CC       forebrain, anterior neural ridge, developing visual system,
CC       primitive external granular layer of the cerebellum and a subset
CC       of neural crest cells likely to develop into melanoblasts.
CC   -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis.
CC   -!- SIMILARITY: Contains 5 cadherin domains.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF007116; AAD01278.1; -; mRNA.
DR   EMBL; AK034475; BAC28721.1; -; mRNA.
DR   EMBL; BC119606; AAI19607.1; -; mRNA.
DR   EMBL; BC119607; AAI19608.1; -; mRNA.
DR   IPI; IPI00129258; -.
DR   RefSeq; NP_035930.1; NM_011800.4.
DR   UniGene; Mm.103640; -.
DR   HSSP; Q7ZYV7; 1ZVN.
DR   ProteinModelPortal; Q9Z0M3; -.
DR   SMR; Q9Z0M3; 60-607, 697-794.
DR   STRING; Q9Z0M3; -.
DR   PhosphoSite; Q9Z0M3; -.
DR   PRIDE; Q9Z0M3; -.
DR   Ensembl; ENSMUST00000062528; ENSMUSP00000052078; ENSMUSG00000050840.
DR   GeneID; 23836; -.
DR   KEGG; mmu:23836; -.
DR   UCSC; uc007cgc.1; mouse.
DR   CTD; 23836; -.
DR   MGI; MGI:1346069; Cdh20.
DR   eggNOG; roNOG13377; -.
DR   GeneTree; ENSGT00590000082742; -.
DR   HOGENOM; HBG505775; -.
DR   HOVERGEN; HBG005217; -.
DR   InParanoid; Q9Z0M3; -.
DR   OMA; LMTARPL; -.
DR   OrthoDB; EOG408N7J; -.
DR   PhylomeDB; Q9Z0M3; -.
DR   NextBio; 303515; -.
DR   ArrayExpress; Q9Z0M3; -.
DR   Bgee; Q9Z0M3; -.
DR   CleanEx; MM_CDH20; -.
DR   CleanEx; MM_CDH7; -.
DR   Genevestigator; Q9Z0M3; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR   Gene3D; G3DSA:2.60.40.60; Cadherin; 5.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF01049; Cadherin_C; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 5.
DR   SUPFAM; SSF49313; Cadherin; 5.
DR   PROSITE; PS00232; CADHERIN_1; 3.
DR   PROSITE; PS50268; CADHERIN_2; 5.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell membrane;
KW   Cleavage on pair of basic residues; Glycoprotein; Membrane; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     34       Potential.
FT   PROPEP       35     59       Potential.
FT                                /FTId=PRO_0000320096.
FT   CHAIN        60    801       Cadherin-20.
FT                                /FTId=PRO_0000320097.
FT   TOPO_DOM     60    619       Extracellular (Potential).
FT   TRANSMEM    620    640       Helical; (Potential).
FT   TOPO_DOM    641    801       Cytoplasmic (Potential).
FT   DOMAIN       61    165       Cadherin 1.
FT   DOMAIN      166    274       Cadherin 2.
FT   DOMAIN      275    389       Cadherin 3.
FT   DOMAIN      390    494       Cadherin 4.
FT   DOMAIN      494    610       Cadherin 5.
FT   CARBOHYD    261    261       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    420    420       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    461    461       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    542    542       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   801 AA;  88998 MW;  AECF5C47A2D6CFBC CRC64;
     MWTTGRMSNA KSWLGLGTSL YFWALMDLTA TVLSSTPMPE VELETLFSGR SQSHQRSKRS
     WVWNQFFVLE EYTGTDPLYV GKLHSDMDRG DGSIKYILSG EGAGIVFTID DTTGDIHAIQ
     RLDREERAQY TLRAQALDRR TGRPMEPESE FIIKIQDIND NEPKFLDGPY IATVPEMSPV
     GTSVIQVTAT DADDPTYGNS ARVVYSILQG QPYFSVDSKT GVIRTALMNM DREAKEYYEV
     IIQAKDMGGQ LGGLAGTTTV NITLSDVNDN PPRFPQKHYQ MSVLESAPIS STVGRVFAKD
     LDEGINAEMK YTIVDGDGAD AFDINTDQNF QVGIITVKKP LSFESKKSYT LKVEGSNPHL
     EMRFLNLGPF QDTTTVHISV EDVDEPPVFE PGFYFVEVPE DVTIGTTIQI ISAKDPDVTN
     NSIRYSIDRG SDPGRFFYVD ITTGALMTAR PLDREEFSWH NITVLAMEMN NPSQVGSVAV
     TIKVLDVNDN APEFPRFYEA FICENAKAGQ LIQTVSAVDQ DDPHNGQHFY YSLAPEAANN
     PNFTVRDNQD NTARILTRRS GFRQQEQSVF YLPILIADSG QPVLSSTGTL TIQVCSCNDD
     GHVMSCSPEA YLLPVSLSRG ALIAILACIF VLLVLVLLIL SMRRHRKQPY IIDDDENIHE
     NIVRYDDEGG GEEDTEAFDI AAMWNPREAQ AGAAPKTRQD MLPEIESLSR YVPQTCAVSS
     TVHSYVLAKL YEADMDLWAP PFDSLQTYMF EGDGSVAGSL SSLQSATSDS EQSFDFLTDW
     GPRFRKLAEL YGASEGPAPL W
//
ID   CD97_MOUSE              Reviewed;         818 AA.
AC   Q9Z0M6; Q923A1; Q9CVI5; Q9JLQ8;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-FEB-2004, sequence version 2.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=CD97 antigen;
DE   AltName: CD_antigen=CD97;
DE   Flags: Precursor;
GN   Name=Cd97;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RX   MEDLINE=20208975; PubMed=10744645; DOI=10.1093/intimm/12.4.439;
RA   Hamann J., van Zventer C., Bijl A., Molenaar C., Tesselaar K.,
RA   van Lier R.A.W.;
RT   "Molecular cloning and characterization of mouse CD97.";
RL   Int. Immunol. 12:439-448(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), INTERACTION WITH DAF,
RP   AND SUBCELLULAR LOCATION.
RC   TISSUE=Testis;
RX   PubMed=10540231; DOI=10.1046/j.1365-2567.1999.00859.x;
RA   Qian Y.-M., Haino M., Kelly K., Song W.-C.;
RT   "Structural characterization of mouse CD97 and study of its specific
RT   interaction with the murine decay-accelerating factor (DAF, CD55).";
RL   Immunology 98:303-311(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 607-818.
RC   STRAIN=C57BL/6J; TISSUE=Small intestine;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   FUNCTION.
RX   PubMed=14707087;
RA   Leemans J.C., te Velde A.A., Florquin S., Bennink R.J., de Bruin K.,
RA   van Lier R.A.W., van der Poll T., Hamann J.;
RT   "The epidermal growth factor-seven transmembrane (EGF-TM7) receptor
RT   CD97 is required for neutrophil migration and host defense.";
RL   J. Immunol. 172:1125-1131(2004).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-299; ASN-395; ASN-407 AND
RP   ASN-461, AND MASS SPECTROMETRY.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
RA   Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
RA   Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-299; ASN-395 AND ASN-407,
RP   AND MASS SPECTROMETRY.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-
RT   linked cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
CC   -!- FUNCTION: Receptor potentially involved in both adhesion and
CC       signaling processes early after leukocyte activation. Plays an
CC       essential role in leukocyte migration.
CC   -!- SUBUNIT: Forms a heterodimer, consisting of a large extracellular
CC       region (alpha subunit) non-covalently linked to a seven-
CC       transmembrane moiety (beta subunit). Interacts with complement
CC       decay-accelerating factor (DAF). The largest isoform (isoform 1)
CC       do not interact with DAF. Interacts also with chondroitin sulfate
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=EGF(1,2,X,3,4);
CC         IsoId=Q9Z0M6-1; Sequence=Displayed;
CC       Name=2; Synonyms=EGF(1,2,4);
CC         IsoId=Q9Z0M6-2; Sequence=VSP_009413;
CC       Name=3; Synonyms=EGF(1,2,3,4);
CC         IsoId=Q9Z0M6-3; Sequence=VSP_009414;
CC   -!- TISSUE SPECIFICITY: Although predominantly expressed by cells of
CC       the immune system is expressed ubiquitously, with particularly
CC       high levels of expression in the lung and the thymus gland. In the
CC       spleen, expression is detected on most myeloid cells and variable
CC       portions of T-cells, B-cells and NK cells. In the bone marrow,
CC       expressed in nearly all myeloid cells, whereas little if any
CC       expression is found on erythroid cells.
CC   -!- INDUCTION: Up-regulated during lymphocyte activation.
CC   -!- DOMAIN: The first two EGF domains mediate the interaction with
CC       DAF. A third tandemly arranged EGF domain is necessary for the
CC       structural integrity of the binding region (By similarity).
CC   -!- DOMAIN: Binding to chondroitin sulfate is mediated by the fourth
CC       EGF domain (By similarity).
CC   -!- PTM: Proteolytically cleaved into 2 subunits, an extracellular
CC       alpha subunit and a seven-transmembrane subunit (By similarity).
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC       LN-TM7 subfamily.
CC   -!- SIMILARITY: Contains 4 EGF-like domains.
CC   -!- SIMILARITY: Contains 1 GPS domain.
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DR   EMBL; Y18365; CAB38246.1; -; mRNA.
DR   EMBL; AF146344; AAF67800.1; -; mRNA.
DR   EMBL; BC006676; AAH06676.1; -; mRNA.
DR   EMBL; AK008101; BAB25461.1; -; mRNA.
DR   IPI; IPI00399798; -.
DR   IPI; IPI00399799; -.
DR   IPI; IPI00399800; -.
DR   RefSeq; NP_001156501.1; NM_001163029.1.
DR   UniGene; Mm.334648; -.
DR   UniGene; Mm.478349; -.
DR   ProteinModelPortal; Q9Z0M6; -.
DR   SMR; Q9Z0M6; 2-255.
DR   STRING; Q9Z0M6; -.
DR   MEROPS; S63.036; -.
DR   PhosphoSite; Q9Z0M6; -.
DR   PRIDE; Q9Z0M6; -.
DR   Ensembl; ENSMUST00000002964; ENSMUSP00000002964; ENSMUSG00000002885.
DR   Ensembl; ENSMUST00000075843; ENSMUSP00000075240; ENSMUSG00000002885.
DR   Ensembl; ENSMUST00000109802; ENSMUSP00000105427; ENSMUSG00000002885.
DR   GeneID; 26364; -.
DR   KEGG; mmu:26364; -.
DR   UCSC; uc009mlc.1; mouse.
DR   CTD; 26364; -.
DR   MGI; MGI:1347095; Cd97.
DR   GeneTree; ENSGT00600000084176; -.
DR   HOGENOM; HBG506068; -.
DR   HOVERGEN; HBG048917; -.
DR   InParanoid; Q9Z0M6; -.
DR   OrthoDB; EOG45X7WF; -.
DR   NextBio; 304231; -.
DR   ArrayExpress; Q9Z0M6; -.
DR   Bgee; Q9Z0M6; -.
DR   CleanEx; MM_CD97; -.
DR   Genevestigator; Q9Z0M6; -.
DR   GermOnline; ENSMUSG00000002885; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; TAS:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004930; F:G-protein coupled receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:InterPro.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR001881; EGF_Ca-bd.
DR   InterPro; IPR013091; EGF_Ca-bd_2.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR017981; GPCR_2-like.
DR   InterPro; IPR003056; GPCR_2_CD97.
DR   InterPro; IPR000832; GPCR_2_secretin-like.
DR   InterPro; IPR000203; GPS_dom.
DR   Pfam; PF00002; 7tm_2; 1.
DR   Pfam; PF07645; EGF_CA; 3.
DR   Pfam; PF01825; GPS; 1.
DR   PRINTS; PR01278; CD97PROTEIN.
DR   PRINTS; PR00249; GPCRSECRETIN.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00179; EGF_CA; 3.
DR   SMART; SM00303; GPS; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 3.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS01187; EGF_CA; 3.
DR   PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; FALSE_NEG.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR   PROSITE; PS50221; GPS; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW   Disulfide bond; EGF-like domain; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Phosphoprotein; Receptor; Repeat; Signal;
KW   Transducer; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     23       Potential.
FT   CHAIN        24    818       CD97 antigen.
FT                                /FTId=PRO_0000012869.
FT   TOPO_DOM     24    533       Extracellular (Potential).
FT   TRANSMEM    534    554       Helical; Name=1; (Potential).
FT   TOPO_DOM    555    562       Cytoplasmic (Potential).
FT   TRANSMEM    563    583       Helical; Name=2; (Potential).
FT   TOPO_DOM    584    602       Extracellular (Potential).
FT   TRANSMEM    603    623       Helical; Name=3; (Potential).
FT   TOPO_DOM    624    637       Cytoplasmic (Potential).
FT   TRANSMEM    638    658       Helical; Name=4; (Potential).
FT   TOPO_DOM    659    679       Extracellular (Potential).
FT   TRANSMEM    680    700       Helical; Name=5; (Potential).
FT   TOPO_DOM    701    723       Cytoplasmic (Potential).
FT   TRANSMEM    724    744       Helical; Name=6; (Potential).
FT   TOPO_DOM    745    752       Extracellular (Potential).
FT   TRANSMEM    753    773       Helical; Name=7; (Potential).
FT   TOPO_DOM    774    818       Cytoplasmic (Potential).
FT   DOMAIN       27     68       EGF-like 1.
FT   DOMAIN       69    119       EGF-like 2; calcium-binding (Potential).
FT   DOMAIN      165    213       EGF-like 3; calcium-binding (Potential).
FT   DOMAIN      214    261       EGF-like 4; calcium-binding (Potential).
FT   DOMAIN      479    524       GPS.
FT   SITE        513    514       Cleavage (By similarity).
FT   MOD_RES     814    814       Phosphoserine (By similarity).
FT   MOD_RES     816    816       Phosphoserine (By similarity).
FT   CARBOHYD     44     44       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    112    112       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    227    227       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    299    299       N-linked (GlcNAc...).
FT   CARBOHYD    395    395       N-linked (GlcNAc...).
FT   CARBOHYD    407    407       N-linked (GlcNAc...).
FT   CARBOHYD    461    461       N-linked (GlcNAc...).
FT   CARBOHYD    502    502       N-linked (GlcNAc...) (Potential).
FT   DISULFID     31     41       By similarity.
FT   DISULFID     35     47       By similarity.
FT   DISULFID     49     67       By similarity.
FT   DISULFID     73     86       By similarity.
FT   DISULFID     80     95       By similarity.
FT   DISULFID     97    118       By similarity.
FT   DISULFID    169    182       By similarity.
FT   DISULFID    176    191       By similarity.
FT   DISULFID    193    212       By similarity.
FT   DISULFID    218    231       By similarity.
FT   DISULFID    225    240       By similarity.
FT   DISULFID    242    260       By similarity.
FT   VAR_SEQ     120    213       Missing (in isoform 2).
FT                                /FTId=VSP_009413.
FT   VAR_SEQ     120    164       Missing (in isoform 3).
FT                                /FTId=VSP_009414.
FT   CONFLICT      3      3       G -> S (in Ref. 1; CAB38246).
FT   CONFLICT     28     28       S -> I (in Ref. 1; CAB38246).
FT   CONFLICT    320    320       Q -> E (in Ref. 3; AAH06676).
FT   CONFLICT    506    506       F -> S (in Ref. 2; AAF67800).
FT   CONFLICT    599    599       M -> V (in Ref. 3; AAH06676).
FT   CONFLICT    726    726       A -> S (in Ref. 3 and 4).
FT   CONFLICT    796    796       F -> I (in Ref. 4; BAB25461).
SQ   SEQUENCE   818 AA;  90413 MW;  E59A292F2CF626C2 CRC64;
     MRGVRCPGLL VVCILLSLSG AGTQKAESKN CAKWCPINSK CVSNRSCVCK PGFSSEKELI
     TNPAESCEDI NECLLPGFSC GDFAMCKNSE GSYTCVCNLG YKLLSGAESF VNESENTCQA
     SVNTGTTPVP SRIHTVTTAP GNLPEQTTTV HQTQMGDSEE RTPKDVNECI SGQNHCHQST
     HCINKLGGYS CICRQGWKPV PGSPNGPVST VCEDVDECSS GQHQCHNSTV CKNTVGSYKC
     HCRPGWKPTS GSLRGPDTIC QEPPFPTWTL LPTAHSQTLL RFSVEVQNLL RDFNPATVNY
     TIQKLIEAVD KLLEDPMETQ TQQVAAQLLS NLEQSLRTLA QFLPKGPFTY TSPSNTELSL
     MVKEQDNKDV TTVHHGQTWM ELDWAVTAGA KISENGSSVA GILSSPNMEK LLGNTPLNLE
     QRRASLEDFY GSPIPSVSLK LLSNINSVFL TNTNTEKLAS NVTFKFDFTS VESIEPRHEL
     ICAFWKAHNG NGYWDTDGCS MNGTGFCHCN HLTSFAILMA QYHVQDPRLE LITKVGLLLS
     LICLLLCILT FLLVKPIQSS RTMVHLHLCI CLFLGSIIFL VGVENEGGEV GLRCRLVAMM
     LHFCFLAAFC WMALEGVELY FLVVRVFQGQ GLSTWQRCLI GYGVPLLIVA ISMAVVKMDG
     YGHATYCWLD FRKQGFLWSF SGPVAFIIFC NAAIFVITVW KLTKKFSEIN PNMKKLRKAR
     VLTITAIAQL LVLGCTWGFG LFLFNPHSTW LSYIFTLLNC LQGLFLYVML CLLNKKVREE
     YWKWACMVTG SKYTEFNSST TGTGTSQTRA LRSSESGM
//
ID   PALM_MOUSE              Reviewed;         383 AA.
AC   Q9Z0P4; Q9Z0P3;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Paralemmin;
DE   Flags: Precursor;
GN   Name=Palm;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND PHOSPHORYLATION.
RC   TISSUE=Brain;
RX   MEDLINE=99030840; PubMed=9813098; DOI=10.1083/jcb.143.3.795;
RA   Kutzleb C., Sanders G., Yamamoto R., Wang X., Lichte B.,
RA   Petrasch-Parwez E., Kilimann M.W.;
RT   "Paralemmin, a prenyl-palmitoyl-anchored phosphoprotein abundant in
RT   neurons and implicated in plasma membrane dynamics and cell process
RT   formation.";
RL   J. Cell Biol. 143:795-813(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 94-109 AND 325-337, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141; THR-145; SER-345;
RP   THR-363 AND SER-365, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141; THR-145; SER-152
RP   AND SER-157, AND MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108; THR-141; THR-145;
RP   SER-157 AND SER-345, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141 AND THR-145, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141 AND THR-145, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May be involved in control of cell shape.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Z0P4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Z0P4-2; Sequence=VSP_003919;
CC   -!- TISSUE SPECIFICITY: Expression is highest in brain, intermediate
CC       in adrenal gland and kidney, and much lower or undetectable in
CC       other tissues. Isoform 1 is the predominant isoform in most
CC       tissues except brain and kidney where isoform 2 predominates.
CC   -!- DEVELOPMENTAL STAGE: In brain, expression is highest in neonates
CC       and declines to approximately 50% in adults. Isoform 2 is the
CC       predominant isoform in neonates with isoform 1 being barely
CC       detectable at this stage. Levels of isoform 1 increase with age,
CC       with the most pronounced increase between postnatal days 10 and
CC       20.
CC   -!- SIMILARITY: Belongs to the paralemmin family.
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DR   EMBL; Y14771; CAB37403.1; -; mRNA.
DR   EMBL; Y14771; CAB37404.1; -; mRNA.
DR   IPI; IPI00129298; -.
DR   IPI; IPI00323809; -.
DR   RefSeq; NP_001155219.1; NM_001161747.1.
DR   RefSeq; NP_075617.3; NM_023128.4.
DR   UniGene; Mm.34650; -.
DR   ProteinModelPortal; Q9Z0P4; -.
DR   STRING; Q9Z0P4; -.
DR   PhosphoSite; Q9Z0P4; -.
DR   PRIDE; Q9Z0P4; -.
DR   Ensembl; ENSMUST00000046945; ENSMUSP00000040596; ENSMUSG00000035863.
DR   Ensembl; ENSMUST00000105379; ENSMUSP00000101018; ENSMUSG00000035863.
DR   GeneID; 18483; -.
DR   KEGG; mmu:18483; -.
DR   UCSC; uc007fzw.1; mouse.
DR   UCSC; uc007fzx.1; mouse.
DR   CTD; 18483; -.
DR   MGI; MGI:1261814; Palm.
DR   GeneTree; ENSGT00530000063206; -.
DR   HOGENOM; HBG712985; -.
DR   HOVERGEN; HBG007431; -.
DR   InParanoid; Q9Z0P4; -.
DR   OrthoDB; EOG4MGS7V; -.
DR   PhylomeDB; Q9Z0P4; -.
DR   ArrayExpress; Q9Z0P4; -.
DR   Bgee; Q9Z0P4; -.
DR   CleanEx; MM_PALM; -.
DR   Genevestigator; Q9Z0P4; -.
DR   GermOnline; ENSMUSG00000035863; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0031750; F:D3 dopamine receptor binding; IPI:MGI.
DR   GO; GO:0007010; P:cytoskeleton organization; IDA:MGI.
DR   GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IDA:MGI.
DR   GO; GO:0030818; P:negative regulation of cAMP biosynthetic process; IDA:MGI.
DR   GO; GO:0008104; P:protein localization; IDA:MGI.
DR   GO; GO:0008360; P:regulation of cell shape; IDA:MGI.
DR   InterPro; IPR004965; Paralemmin.
DR   Pfam; PF03285; Paralemmin; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cell shape; Coiled coil;
KW   Direct protein sequencing; Lipoprotein; Membrane; Methylation;
KW   Palmitate; Phosphoprotein; Prenylation.
FT   CHAIN         1    380       Paralemmin.
FT                                /FTId=PRO_0000058219.
FT   PROPEP      381    383       Removed in mature form (Potential).
FT                                /FTId=PRO_0000396690.
FT   COILED        5    102       Potential.
FT   MOD_RES     108    108       Phosphoserine.
FT   MOD_RES     116    116       Phosphoserine (By similarity).
FT   MOD_RES     124    124       Phosphoserine (By similarity).
FT   MOD_RES     141    141       Phosphothreonine.
FT   MOD_RES     145    145       Phosphothreonine.
FT   MOD_RES     152    152       Phosphoserine.
FT   MOD_RES     153    153       Phosphothreonine (By similarity).
FT   MOD_RES     157    157       Phosphoserine.
FT   MOD_RES     161    161       Phosphoserine (By similarity).
FT   MOD_RES     345    345       Phosphoserine.
FT   MOD_RES     363    363       Phosphothreonine.
FT   MOD_RES     365    365       Phosphoserine.
FT   MOD_RES     380    380       Cysteine methyl ester (Potential).
FT   LIPID       377    377       S-palmitoyl cysteine (Potential).
FT   LIPID       379    379       S-palmitoyl cysteine (Potential).
FT   LIPID       380    380       S-farnesyl cysteine (Potential).
FT   VAR_SEQ     167    210       Missing (in isoform 2).
FT                                /FTId=VSP_003919.
SQ   SEQUENCE   383 AA;  41614 MW;  D63CAF5CFB1A70AB CRC64;
     MEVLATDTAS QQERLQAIAE KRRKQAEIES KRRQLEDDRR QLQYLKSKAL RERWLLEGTP
     SSASEGDEDM RKQMQEDEQK ARGLEESITR LEKEIDVLEF GESAPAASKE NSAAPSPGRP
     QSASPAKEEQ KSETLVNAQQ TPLGTPKENR TSTPVRSPGG STMMKAAMYS VEITVEKDKV
     TGETRVLSST TVLPRDPLPQ GVKVYEDETK VVHAVDGIAE NGIQPLSSSE VDELIHKADE
     VTLSEAGSTA GPAEPRGLAE DVTRTTPSRR EITGVEAQPG EATSGPPGIQ PGQEPPVTMV
     FMGYQNVEDE AETKKVLGLQ DTIKAELVVI EDAATPREPA PLNGSAAELP ATKEENQTGP
     TTTPSDTQDL DMKKPRCRCC SVM
//
ID   ITSN1_MOUSE             Reviewed;        1714 AA.
AC   Q9Z0R4; Q9R143;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 109.
DE   RecName: Full=Intersectin-1;
DE   AltName: Full=EH and SH3 domains protein 1;
GN   Name=Itsn1; Synonyms=Ese1, Itsn;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=99164083; PubMed=10064583; DOI=10.1093/emboj/18.5.1159;
RA   Sengar A.S., Wang W., Bishay J., Cohen S., Egan S.E.;
RT   "The EH and SH3 domain Ese proteins regulate endocytosis by linking to
RT   dynamin and Eps15.";
RL   EMBO J. 18:1159-1171(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 966-1714 (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP   OF 545-599 (ISOFORMS 1 AND 2).
RC   STRAIN=129/Ola; TISSUE=Spleen;
RA   Skripkina I.Y., Tsyba L.O., Anoprienko O.V., Slavov D., Tassone F.,
RA   Rynditch A.V., Gardiner K.;
RT   "Mouse homologues of human chromosome 21 genes.";
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INTERACTION WITH ARHGAP31.
RX   PubMed=11744688; DOI=10.1074/jbc.M105516200;
RA   Jenna S., Hussain N.K., Danek E.I., Triki I., Wasiak S.,
RA   McPherson P.S., Lamarche-Vane N.;
RT   "The activity of the GTPase-activating protein CdGAP is regulated by
RT   the endocytic protein intersectin.";
RL   J. Biol. Chem. 277:6366-6373(2002).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315; SER-335 AND
RP   SER-895, AND MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1130, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-970, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313; SER-318; SER-334;
RP   SER-335; SER-895; SER-897 AND THR-977, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
CC   -!- FUNCTION: Adapter protein that may provide indirect link between
CC       the endocytic membrane traffic and the actin assembly machinery.
CC       May regulate the formation of clathrin-coated vesicles. Inhibits
CC       ARHGAP31 activity toward RAC1.
CC   -!- SUBUNIT: Interacts with dynamin, CDC42, SNAP25 and SNAP23.
CC       Clusters several dynamin in a manner that is regulated by
CC       alternative splicing. Also binds clathrin-associated proteins and
CC       other components of the endocytic machinery, such as SPIN90,
CC       EPS15, EPN1, EPN2 and STON2 (By similarity). Interacts with
CC       ARHGAP31. Interacts with ADAM15 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endomembrane system (By similarity). Cell
CC       junction, synapse, synaptosome (By similarity). Cell projection,
CC       lamellipodium (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC         Comment=Additional isoforms seem to exist;
CC       Name=1; Synonyms=Ese1L;
CC         IsoId=Q9Z0R4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Z0R4-2; Sequence=VSP_004296;
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed at high levels in
CC       brain, heart and skeletal muscle.
CC   -!- DOMAIN: SH3-3, SH3-4 and SH3-5, but not SH3-1 and SH3-2 domains,
CC       bind to dynamin (By similarity). SH3-1 and SH3-4 bind to ARHGAP31.
CC   -!- DOMAIN: The KLERQ domain binds to SNAP-25 and SNAP-23 (By
CC       similarity).
CC   -!- MISCELLANEOUS: Overexpression results in the inhibition of the
CC       transferrin uptake and the blockage of the clathrin-mediated
CC       endocytosis.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
CC   -!- SIMILARITY: Contains 2 EH domains.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 5 SH3 domains.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF132481; AAD19749.1; -; mRNA.
DR   EMBL; AF132478; AAD19746.1; -; mRNA.
DR   EMBL; AF169621; AAD48848.1; -; mRNA.
DR   EMBL; AF356517; AAK40228.1; -; Genomic_DNA.
DR   IPI; IPI00129356; -.
DR   IPI; IPI00222409; -.
DR   RefSeq; NP_001103745.1; NM_001110275.1.
DR   RefSeq; NP_034717.2; NM_010587.2.
DR   UniGene; Mm.40546; -.
DR   PDB; 3HS8; X-ray; 1.90 A; P=840-851.
DR   PDB; 3JV3; X-ray; 2.40 A; A/B=1151-1431.
DR   PDBsum; 3HS8; -.
DR   PDBsum; 3JV3; -.
DR   ProteinModelPortal; Q9Z0R4; -.
DR   SMR; Q9Z0R4; 6-103, 211-303, 739-800, 906-1574, 1588-1711.
DR   IntAct; Q9Z0R4; 3.
DR   MINT; MINT-86500; -.
DR   STRING; Q9Z0R4; -.
DR   PhosphoSite; Q9Z0R4; -.
DR   PRIDE; Q9Z0R4; -.
DR   Ensembl; ENSMUST00000114002; ENSMUSP00000109635; ENSMUSG00000022957.
DR   Ensembl; ENSMUST00000116575; ENSMUSP00000112274; ENSMUSG00000022957.
DR   GeneID; 16443; -.
DR   KEGG; mmu:16443; -.
DR   UCSC; uc007zyi.1; mouse.
DR   UCSC; uc007zyj.1; mouse.
DR   CTD; 16443; -.
DR   MGI; MGI:1338069; Itsn1.
DR   GeneTree; ENSGT00600000084249; -.
DR   HOVERGEN; HBG052159; -.
DR   OrthoDB; EOG46Q6RS; -.
DR   NextBio; 289695; -.
DR   ArrayExpress; Q9Z0R4; -.
DR   Bgee; Q9Z0R4; -.
DR   CleanEx; MM_ITSN1; -.
DR   Genevestigator; Q9Z0R4; -.
DR   GermOnline; ENSMUSG00000022957; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0030139; C:endocytic vesicle; IDA:MGI.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR   GO; GO:0019717; C:synaptosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0019209; F:kinase activator activity; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0043524; P:negative regulation of neuron apoptosis; IMP:MGI.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling cascade; IDA:MGI.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IDA:MGI.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR000261; EPS15_homology.
DR   InterPro; IPR001331; GDS_CDC24_CS.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF00018; SH3_1; 3.
DR   Pfam; PF07653; SH3_2; 2.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM00027; EH; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00326; SH3; 5.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   SUPFAM; SSF50044; SH3; 5.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS00741; DH_1; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS50031; EH; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 5.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Calcium;
KW   Cell junction; Cell projection; Coiled coil; Endocytosis; Membrane;
KW   Phosphoprotein; Repeat; SH3 domain; Synapse; Synaptosome.
FT   CHAIN         1   1714       Intersectin-1.
FT                                /FTId=PRO_0000080958.
FT   DOMAIN       21    109       EH 1.
FT   DOMAIN       53     88       EF-hand 1.
FT   DOMAIN      221    310       EH 2.
FT   DOMAIN      254    289       EF-hand 2.
FT   DOMAIN      738    799       SH3 1.
FT   DOMAIN      906    964       SH3 2.
FT   DOMAIN      995   1053       SH3 3.
FT   DOMAIN     1067   1131       SH3 4.
FT   DOMAIN     1148   1207       SH3 5.
FT   DOMAIN     1230   1416       DH.
FT   DOMAIN     1455   1564       PH.
FT   DOMAIN     1576   1672       C2.
FT   CA_BIND      66     78       1 (Potential).
FT   CA_BIND     267    279       2 (Potential).
FT   REGION      326    702       KLERQ.
FT   COILED      352    662       Potential.
FT   COMPBIAS    321    324       Poly-Ser.
FT   MOD_RES     313    313       Phosphoserine.
FT   MOD_RES     315    315       Phosphoserine.
FT   MOD_RES     318    318       Phosphoserine.
FT   MOD_RES     334    334       Phosphoserine.
FT   MOD_RES     335    335       Phosphoserine.
FT   MOD_RES     494    494       N6-acetyllysine (By similarity).
FT   MOD_RES     558    558       Phosphoserine (By similarity).
FT   MOD_RES     895    895       Phosphoserine.
FT   MOD_RES     897    897       Phosphoserine.
FT   MOD_RES     970    970       Phosphothreonine.
FT   MOD_RES     971    971       Phosphoserine (By similarity).
FT   MOD_RES     977    977       Phosphothreonine.
FT   MOD_RES     979    979       Phosphoserine (By similarity).
FT   MOD_RES    1130   1130       Phosphoserine.
FT   VAR_SEQ    1214   1714       Missing (in isoform 2).
FT                                /FTId=VSP_004296.
SQ   SEQUENCE   1714 AA;  194285 MW;  4D7AF298397860A7 CRC64;
     MAQFPTPFGG SLDVWAITVE ERAKHDQQFL SLKPIAGFIT GDQARNFFFQ SGLPQPVLAQ
     IWALADMNND GRMDQVEFSI AMKLIKLKLQ GYQLPSTLPP VMKQQPVAIS SAPAFGIGGI
     ASMPPLTAVA PVPMGSIPVV GMSPPLVSSV PPAAVPPLAN GAPPVIQPLP AFAHPAATWP
     KSSSFSRSGP GSQLNTKLQK AQSFDVASAP PAAEWAVPQS SRLKYRQLFN SHDKTMSGHL
     TGPQARTILM QSSLPQAQLA SIWNLSDIDQ DGKLTAEEFI LAMHLIDVAM SGQPLPPVLP
     PEYIPPSFRR VRSGSGMSVI SSSSVDQRLP EEPSSEDEQQ PEKKLPVTFE DKKRENFERG
     SVELEKRRQA LLEQQRKEQE RLAQLERAEQ ERKERERQEQ EAKRQLELEK QLEKQRELER
     QREEERRKEI ERREAAKREL ERQRQLEWER NRRQELLNQR NKEQEGTVVL KARRKTLEFE
     LEALNDKKHQ LEGKLQDIRC RLATQRQEIE STNKSRELRI AEITHLQQQL QESQQMLGRL
     IPEKQILSDQ LKQVQQNSLH RDSLLTLKRA LEAKELARQQ LREQLDEVER ETRSKLQEID
     VFNNQLKELR EIHSKQQLQK QRSLEAARLK QKEQERKSLE LEKQKEDAQR RVQERDKQWL
     EHVQQEEQPR PRKPHEEDRL KREDSVRKKE AEERAKPEMQ DKQSRLFHPH QEPAKLATQA
     PWSTTEKGPL TISAQESVKV VYYRALYPFE SRSHDEITIQ PGDIVMVDES QTGEPGWLGG
     ELKGKTGWFP ANYAEKIPEN EVPTPAKPVT DLTSAPAPKL ALRETPAPLP VTSSEPSTTP
     NNWADFSSTW PSSSNEKPET DNWDTWAAQP SLTVPSAGQL RQRSAFTPAT ATGSSPSPVL
     GQGEKVEGLQ AQALYPWRAK KDNHLNFNKS DVITVLEQQD MWWFGEVQGQ KGWFPKSYVK
     LISGPVRKST SIDTGPTESP ASLKRVASPA AKPAIPGEEF IAMYTYESSE QGDLTFQQGD
     VIVVTKKDGD WWTGTVGDKS GVFPSNYVRL KDSEGSGTAG KTGSLGKKPE IAQVIASYAA
     TGPEQLTLAP GQLILIRKKN PGGWWEGELQ ARGKKRQIGW FPANYVKLLS PGTSKITPTE
     LPKTAVQPAV CQVIGMYDYT AQNDDELAFS KGQIINVLNK EDPDWWKGEV SGQVGLFPSN
     YVKLTTDMDP SQQWCSDLHL LDMLTPTERK RQGYIHELIV TEENYVNDLQ LVTEIFQKPL
     TESELLTEKE VAMIFVNWKE LIMCNIKLLK ALRVRKKMSG EKMPVKMIGD ILSAQLPHMQ
     PYIRFCSCQL NGAALIQQKT DEAPDFKEFV KRLAMDPRCK GMPLSSFILK PMQRVTRYPL
     IIKNILENTP ENHPDHSHLK HALEKAEELC SQVNEGVREK ENSDRLEWIQ AHVQCEGLSE
     QLVFNSVTNC LGPRKFLHSG KLYKAKSNKE LYGFLFNDFL LLTQITKPLG SSGTDKVFSP
     KSNLQYKMYK TPIFLNEVLV KLPTDPSGDE PIFHISHIDR VYTLRAESIN ERTAWVQKIK
     AASELYIETE KKKREKAYLV RSQRATGIGR LMVNVVEGIE LKPCRSHGKS NPYCEVTMGS
     QCHITKTIQD TLNPKWNSNC QFFIRDLEQE VLCITVFERD QFSPDDFLGR TEIRVADIKK
     DQGSKGPVTK CLLLHEVPTG EIVVRLDLQL FDEP
//
ID   ITSN2_MOUSE             Reviewed;        1659 AA.
AC   Q9Z0R6; Q8C9C3; Q9Z0R5;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 2.
DT   08-MAR-2011, entry version 104.
DE   RecName: Full=Intersectin-2;
DE   AltName: Full=EH domain and SH3 domain regulator of endocytosis 2;
DE            Short=EH and SH3 domains protein 2;
DE   AltName: Full=SH3 domain-containing protein 1B;
GN   Name=Itsn2; Synonyms=Ese2, Sh3d1B;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-441 (ISOFORM 1/2).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2-1659 (ISOFORMS 1 AND 2).
RX   MEDLINE=99164083; PubMed=10064583; DOI=10.1093/emboj/18.5.1159;
RA   Sengar A.S., Wang W., Bishay J., Cohen S., Egan S.E.;
RT   "The EH and SH3 domain Ese proteins regulate endocytosis by linking to
RT   dynamin and Eps15.";
RL   EMBO J. 18:1159-1171(1999).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-922, AND MASS
RP   SPECTROMETRY.
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-554 AND TYR-922, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-843, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-922, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-843, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Adapter protein that may provide indirect link between
CC       the endocytic membrane traffic and the actin assembly machinery.
CC       May regulate the formation of clathrin-coated vesicles.
CC   -!- SUBUNIT: Belongs to a complex that may contain multimers of ITSN1,
CC       ITSN2 and EPS15, and different partners according to the step in
CC       the endocytic process. Interacts with ADAM15. Interacts with FASLG
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Ese2L, Long;
CC         IsoId=Q9Z0R6-1; Sequence=Displayed;
CC       Name=2; Synonyms=Ese2, Short;
CC         IsoId=Q9Z0R6-2; Sequence=VSP_003896, VSP_003897;
CC   -!- TISSUE SPECIFICITY: Widely expressed in adult tissues.
CC   -!- DEVELOPMENTAL STAGE: Widely distributed throughout the adult
CC       forebrain. Prominent expression was observed in the neocortex, the
CC       piriform cortex, the pyramidal cell layers of hippocampus, the
CC       dentate gyrus, in several nuclei of the thalamus and hypothalamus
CC       and in the amygdala.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
CC   -!- SIMILARITY: Contains 2 EH domains.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 5 SH3 domains.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC31264.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
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DR   EMBL; AK042449; BAC31264.1; ALT_INIT; mRNA.
DR   EMBL; AF132479; AAD19747.1; -; mRNA.
DR   EMBL; AF132480; AAD19748.1; -; mRNA.
DR   IPI; IPI00222827; -.
DR   IPI; IPI00762547; -.
DR   UniGene; Mm.341204; -.
DR   ProteinModelPortal; Q9Z0R6; -.
DR   SMR; Q9Z0R6; 7-104, 238-333, 717-804, 851-1516, 1530-1653.
DR   STRING; Q9Z0R6; -.
DR   PhosphoSite; Q9Z0R6; -.
DR   PRIDE; Q9Z0R6; -.
DR   Ensembl; ENSMUST00000062580; ENSMUSP00000052758; ENSMUSG00000020640.
DR   KEGG; mmu:20403; -.
DR   CTD; 20403; -.
DR   MGI; MGI:1338049; Itsn2.
DR   GeneTree; ENSGT00600000084249; -.
DR   HOGENOM; HBG445076; -.
DR   HOVERGEN; HBG052159; -.
DR   InParanoid; Q9Z0R6; -.
DR   OrthoDB; EOG46Q6RS; -.
DR   NextBio; 298368; -.
DR   ArrayExpress; Q9Z0R6; -.
DR   Bgee; Q9Z0R6; -.
DR   CleanEx; MM_ITSN2; -.
DR   Genevestigator; Q9Z0R6; -.
DR   GermOnline; ENSMUSG00000020640; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002048; EF_hand_Ca-bd.
DR   InterPro; IPR000261; EPS15_homology.
DR   InterPro; IPR000108; p67phox.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF00018; SH3_1; 4.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR00499; P67PHOX.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM00027; EH; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00326; SH3; 5.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF48065; DH-domain; 1.
DR   SUPFAM; SSF50044; SH3; 5.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 2.
DR   PROSITE; PS50031; EH; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 5.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Coiled coil; Cytoplasm; Endocytosis;
KW   Phosphoprotein; Repeat; SH3 domain.
FT   CHAIN         1   1659       Intersectin-2.
FT                                /FTId=PRO_0000080962.
FT   DOMAIN       22    110       EH 1.
FT   DOMAIN       54     89       EF-hand 1.
FT   DOMAIN      245    334       EH 2.
FT   DOMAIN      718    779       SH3 1.
FT   DOMAIN      852    910       SH3 2.
FT   DOMAIN      942   1000       SH3 3.
FT   DOMAIN     1014   1078       SH3 4.
FT   DOMAIN     1088   1147       SH3 5.
FT   DOMAIN     1170   1357       DH.
FT   DOMAIN     1396   1506       PH.
FT   DOMAIN     1518   1614       C2.
FT   CA_BIND      67     79       Potential.
FT   COILED      365    717       Potential.
FT   MOD_RES     211    211       Phosphoserine.
FT   MOD_RES     554    554       Phosphotyrosine.
FT   MOD_RES     813    813       Phosphotyrosine (By similarity).
FT   MOD_RES     836    836       Phosphothreonine (By similarity).
FT   MOD_RES     838    838       Phosphoserine (By similarity).
FT   MOD_RES     843    843       Phosphoserine.
FT   MOD_RES     922    922       Phosphotyrosine.
FT   VAR_SEQ    1188   1198       DDLQLVIEVFQ -> GLQLFEQKTLL (in isoform
FT                                2).
FT                                /FTId=VSP_003896.
FT   VAR_SEQ    1199   1659       Missing (in isoform 2).
FT                                /FTId=VSP_003897.
FT   CONFLICT    452    453       KQ -> NT (in Ref. 2; AAD19748).
FT   CONFLICT   1162   1162       D -> G (in Ref. 2; AAD19748).
SQ   SEQUENCE   1659 AA;  188908 MW;  840F16B3A0DACDD6 CRC64;
     MMAQFPTAMN GGPNMWAITS EERTKHDKQF DNLKPSGGYI TGDQARTFFL QSGLPAPVLA
     EIWALSDLNK DGKMDQQEFS IAMKLIKLKL QGQQLPVVLP PIMKQPPMFS PLISARFGMG
     SMPNLSIHQP LPPVAPIATP LSSATSGTSI PPLMMPAPLV PSVSTSSLPN GTASLIQPLS
     IPYSSSTLPH ASSYSLMMGG FGGASIQKAQ SLIDLGSSSS TSSTASLSGN SPKTGTSEWA
     VPQPSRLKYR QKFNSLDKGM SGYLSGFQAR NALLQSNLSQ TQLATIWTLA DIDGDGQLKA
     EEFILAMHLT DMAKAGQPLP LTLPPELVPP SFRGGKQVDS VNGTLPSYQK TQEEEPQKKL
     PVTFEDKRKA NYERGNMELE KRRQVLMEQQ QREAERKAQK EKEEWERKQR ELQEQEWKKQ
     LELEKRLEKQ RELERQREEE RRKEIERREA AKQELERQRR LEWERLRRQE LLSQKTREQE
     DIVRLSSRKK SLHLELEAVN GKHQQISGRL QDVQIRKQTQ KTELEVLDKQ CDLEIMEIKQ
     LQQELKEYQN KLIYLVPEKQ LLNERIKNMQ LSNTPDSGIS LLHKKSSEKE ELCQRLKEQL
     DALEKETASK LSEMDSFNNQ LKELRESYNT QQLALEQLHK IKRDKLKEIE RKRLEQIQKK
     KLEDEAARKA KQGKENLWRE SIRKEEEEKQ KRLQEEKSQD KTQEEERKAE AKQSETASAL
     VNYRALYPFE ARNHDEMSFS SGDIIQVDEK TVGEPGWLYG SFQGKFGWFP CNYVEKVLSS
     EKALSPKKAL LPPTVSLSAT STSSQPPASV TDYHNVSFSN LTVNTTWQQK SAFTRTVSPG
     SVSPIHGQGQ AVENLKAQAL CSWTAKKENH LNFSKHDVIT VLEQQENWWF GEVHGGRGWF
     PKSYVKLIPG NEVQRGEPEA LYAAVTKKPT STAYPVTSTA YPVGEDYIAL YSYSSVEPGD
     LTFTEGEEIL VTQKDGEWWT GSIGERTGIF PSNYVRPKDQ ENFGNASKSG ASNKKPEIAQ
     VTSAYAASGT EQLSLAPGQL ILILKKNTSG WWQGELQARG KKRQKGWFPA SHVKLLGPSS
     ERTMPTFHAV CQVIAMYDYM ANNEDELNFS KGQLINVMNK DDPDWWQGET NGLTGLFPSN
     YVKMTTDSDP SQQWCADLQA LDTMQPTERK RQGYIHELIQ TEERYMDDDL QLVIEVFQKR
     MAEEGFLTEA DMALIFVNWK ELIMSNTKLL RALRVRKKTG GEKMPVQMIG DILAAELSHM
     QAYIRFCSCQ LNGATLLQQK TDEDTDFKEF LKKLASDPRC KGMPLSSFLL KPMQRITRYP
     LLIRSILENT PQSHVDHSSL KLALERAEEL CSQVNEGVRE KENSDRLEWI QAHVQCEGLA
     EQLIFNSLTN CLGPRKLLHS GKLYKTKSNK ELHAFLFNDF LLLTYLVRQF AAASGHEKLF
     NSKSSAQFRM YKTPIFLNEV LVKLPTDPSG DEPVFHISHI DRVYTLRTDN INERTAWVQK
     IKGASEQYID TEKKKREKAY QARSQKTSGI GRLMVHVIEA TELKACKPNG KSNPYCEVSM
     GSQSYTTRTL QDTLNPKWNF NCQFFIKDLY QDVLCLTMFD RDQFSPDDFL GRTEVPVAKI
     RTEQESKGPT TRRLLLHEVP TGEVWVRFDL QLFEQKTLL
//
ID   BPNT1_MOUSE             Reviewed;         308 AA.
AC   Q9Z0S1; Q3U8Z5; Q91XB9; Q9D7Y0;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=3'(2'),5'-bisphosphate nucleotidase 1;
DE            EC=3.1.3.7;
DE   AltName: Full=Bisphosphate 3'-nucleotidase 1;
DE   AltName: Full=PAP-inositol-1,4-phosphatase;
DE            Short=PIP;
GN   Name=Bpnt1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX   MEDLINE=99240760; PubMed=10224133; DOI=10.1074/jbc.274.19.13619;
RA   Spiegelberg B.D., Xiong J.-P., Smith J.J., Gu R.F., York J.D.;
RT   "Cloning and characterization of a mammalian lithium-sensitive
RT   bisphosphate 3'-nucleotidase inhibited by inositol 1,4-bisphosphate.";
RL   J. Biol. Chem. 274:13619-13628(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Stomach;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS)
CC       to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine
CC       5'- phosphate (PAP) to AMP. Has 1000-fold lower activity towards
CC       inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4-
CC       trisphosphate (Ins(1,3,4)P3), but does not hydrolyze Ins(1)P,
CC       Ins(3,4)P2, Ins(1,3,4,5)P4 or InsP6.
CC   -!- CATALYTIC ACTIVITY: Adenosine 3',5'-bisphosphate + H(2)O =
CC       adenosine 5'-phosphate + phosphate.
CC   -!- COFACTOR: Magnesium.
CC   -!- ENZYME REGULATION: Uncompetitive inhibition by micromolar
CC       concentrations of lithium. Competitive inhibition by inositol 1,4-
CC       bisphosphate.
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase family.
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DR   EMBL; AF125043; AAD17330.1; -; mRNA.
DR   EMBL; AK008714; BAB25850.1; -; mRNA.
DR   EMBL; AK151931; BAE30807.1; -; mRNA.
DR   EMBL; AK152009; BAE30872.1; -; mRNA.
DR   EMBL; BC011036; AAH11036.1; -; mRNA.
DR   IPI; IPI00318545; -.
DR   RefSeq; NP_035924.2; NM_011794.3.
DR   UniGene; Mm.227549; -.
DR   ProteinModelPortal; Q9Z0S1; -.
DR   SMR; Q9Z0S1; 5-308.
DR   STRING; Q9Z0S1; -.
DR   REPRODUCTION-2DPAGE; Q9Z0S1; -.
DR   PRIDE; Q9Z0S1; -.
DR   Ensembl; ENSMUST00000027916; ENSMUSP00000027916; ENSMUSG00000026617.
DR   Ensembl; ENSMUST00000116478; ENSMUSP00000112179; ENSMUSG00000026617.
DR   GeneID; 23827; -.
DR   KEGG; mmu:23827; -.
DR   UCSC; uc007dzc.1; mouse.
DR   CTD; 23827; -.
DR   MGI; MGI:1338800; Bpnt1.
DR   GeneTree; ENSGT00530000063462; -.
DR   HOGENOM; HBG380847; -.
DR   HOVERGEN; HBG050719; -.
DR   InParanoid; Q9Z0S1; -.
DR   OMA; AHAYVFA; -.
DR   OrthoDB; EOG4GXFND; -.
DR   PhylomeDB; Q9Z0S1; -.
DR   BRENDA; 3.1.3.7; 244.
DR   NextBio; 303481; -.
DR   ArrayExpress; Q9Z0S1; -.
DR   Bgee; Q9Z0S1; -.
DR   CleanEx; MM_BPNT1; -.
DR   Genevestigator; Q9Z0S1; -.
DR   GermOnline; ENSMUSG00000026617; Mus musculus.
DR   GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IDA:MGI.
DR   InterPro; IPR020583; Inositol_monoP_metal-BS.
DR   InterPro; IPR000760; Inositol_monophosphatase.
DR   InterPro; IPR020550; Inositol_monophosphatase_CS.
DR   PANTHER; PTHR20854; Inositol_P; 1.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PROSITE; PS00629; IMP_1; 1.
DR   PROSITE; PS00630; IMP_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Hydrolase; Lithium; Magnesium; Metal-binding.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    308       3'(2'),5'-bisphosphate nucleotidase 1.
FT                                /FTId=PRO_0000142528.
FT   REGION      119    122       Substrate binding (By similarity).
FT   REGION      195    198       Substrate binding (By similarity).
FT   METAL        74     74       Magnesium 1 (By similarity).
FT   METAL       117    117       Magnesium 1 (By similarity).
FT   METAL       117    117       Magnesium 2 (By similarity).
FT   METAL       119    119       Magnesium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       120    120       Magnesium 2 (By similarity).
FT   METAL       247    247       Magnesium 2 (By similarity).
FT   BINDING      74     74       Substrate (By similarity).
FT   BINDING     247    247       Substrate (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   CONFLICT    164    164       A -> V (in Ref. 3; AAH11036).
FT   CONFLICT    190    190       H -> R (in Ref. 3; AAH11036).
FT   CONFLICT    276    276       V -> A (in Ref. 1; AAD17330).
SQ   SEQUENCE   308 AA;  33196 MW;  D941FEA4C2E59E9D CRC64;
     MASSHTVLMR LVASAYSIAQ KAGTIVRCVI AEGDLGIVQK TSATDLQTKA DRLVQMSICS
     SLARKFPKLT IIGEEDLPPG EVDQELIEDG QWEEILKQPC PSQYSAIKEE DLVVWVDPLD
     GTKEYTEGLL DNVTVLIGIA YEGKAIAGII NQPYYNYQAG PDAALGRTIW GVLGLGAFGF
     QLKEAPAGKH IITTTRSHSN QLVTDCISAM NPDTVLRVGG AGNKIIQLIE GKASAYVFAS
     PGCKKWDTCA PEVILHAVGG KLTDIHGNAL QYNKEVKHMN SAGVLAALRN YEYYASHVPE
     SVKNALIP
//
ID   CL10A_MOUSE             Reviewed;         231 AA.
AC   Q9Z0S6;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=Claudin-10A;
GN   Name=Cldn10a; Synonyms=Cldn10;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RA   Morita K., Furuse M., Tsukita S.;
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Plays a major role in tight junction-specific
CC       obliteration of the intercellular space, through calcium-
CC       independent cell-adhesion activity (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell junction, tight junction. Cell
CC       membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the claudin family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF124425; AAD17320.1; -; mRNA.
DR   EMBL; BC029019; AAH29019.1; -; mRNA.
DR   IPI; IPI00129394; -.
DR   UniGene; Mm.390755; -.
DR   DIP; DIP-48954N; -.
DR   STRING; Q9Z0S6; -.
DR   TCDB; 1.H.1.8.1; claudin tight junction (Claudin) family.
DR   PhosphoSite; Q9Z0S6; -.
DR   PRIDE; Q9Z0S6; -.
DR   Ensembl; ENSMUST00000100314; ENSMUSP00000097889; ENSMUSG00000022132.
DR   UCSC; uc007uyx.1; mouse.
DR   MGI; MGI:1913101; Cldn10a.
DR   GeneTree; ENSGT00600000084022; -.
DR   HOGENOM; HBG716859; -.
DR   HOVERGEN; HBG000643; -.
DR   InParanoid; Q9Z0S6; -.
DR   OrthoDB; EOG441QCM; -.
DR   NextBio; 314155; -.
DR   ArrayExpress; Q9Z0S6; -.
DR   Bgee; Q9Z0S6; -.
DR   Genevestigator; Q9Z0S6; -.
DR   GermOnline; ENSMUSG00000022132; Mus musculus.
DR   GermOnline; ENSMUSG00000075473; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005923; C:tight junction; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0016338; P:calcium-independent cell-cell adhesion; ISS:UniProtKB.
DR   InterPro; IPR006187; Claudin.
DR   InterPro; IPR003554; Claudin10.
DR   InterPro; IPR017974; Claudin_CS.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   PANTHER; PTHR12002; Claudin; 1.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01077; CLAUDIN.
DR   PRINTS; PR01383; CLAUDIN10.
DR   PROSITE; PS01346; CLAUDIN; 1.
PE   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Membrane; Tight junction; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    231       Claudin-10A.
FT                                /FTId=PRO_0000144758.
FT   TRANSMEM      1     21       Helical; (Potential).
FT   TOPO_DOM     22     80       Extracellular (Potential).
FT   TRANSMEM     81    101       Helical; (Potential).
FT   TOPO_DOM    102    115       Cytoplasmic (Potential).
FT   TRANSMEM    116    136       Helical; (Potential).
FT   TOPO_DOM    137    160       Extracellular (Potential).
FT   TRANSMEM    161    181       Helical; (Potential).
FT   TOPO_DOM    182    231       Cytoplasmic (Potential).
SQ   SEQUENCE   231 AA;  24693 MW;  80A28863A24FAFB5 CRC64;
     MASTALEIVA FVVSISGWVL VSSTLPTDYW KVSTIDGTVI TTATYFANLW KICVTDSTGV
     ANCKEFPSML ALDGYIQACR GLMIAAVSLG FFGSIFALFG MKCTKVGGSD QAKAKIACLA
     GIVFILSGLC SMTGCSLYAN KITTEFFDPL YMEQKYELGA ALFIGWAGAS LCIIGGVIFC
     FSISDNNKTP RMGYTYNGPT SVMSSRTKYQ GGEGDFKTAG PSKQFDKNAY V
//
ID   ZO2_MOUSE               Reviewed;        1167 AA.
AC   Q9Z0U1; Q8K210;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   08-MAR-2011, entry version 108.
DE   RecName: Full=Tight junction protein ZO-2;
DE   AltName: Full=Tight junction protein 2;
DE   AltName: Full=Zona occludens protein 2;
DE   AltName: Full=Zonula occludens protein 2;
GN   Name=Tjp2; Synonyms=Zo2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X CBA;
RX   MEDLINE=99150392; PubMed=10026224; DOI=10.1074/jbc.274.9.5981;
RA   Itoh M., Morita K., Tsukita S.;
RT   "Characterization of ZO-2 as a MAGUK family member associated with
RT   tight as well as adherens junctions with a binding affinity to
RT   occludin and alpha catenin.";
RL   J. Biol. Chem. 274:5981-5986(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=129; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH SAFB.
RX   MEDLINE=22421353; PubMed=12403786; DOI=10.1074/jbc.M206821200;
RA   Traweger A., Fuchs R., Krizbai I.A., Weiger T.M., Bauer H.-C.,
RA   Bauer H.;
RT   "The tight junction protein ZO-2 localizes to the nucleus and
RT   interacts with the heterogeneous nuclear ribonucleoprotein scaffold
RT   attachment factor-B.";
RL   J. Biol. Chem. 278:2692-2700(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107 AND SER-239, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-238, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion
RT   affinity chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-263; SER-265;
RP   SER-267; SER-968 AND SER-988, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-968, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-968 AND TYR-1095, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
RN   [10]
RP   STRUCTURE BY NMR OF 1-106.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of N-terminal PDZ domain from mouse TJP2.";
RL   Submitted (MAY-2005) to the PDB data bank.
CC   -!- FUNCTION: Plays a role in tight junctions and adherens junctions.
CC   -!- SUBUNIT: Homodimer, and heterodimer with ZO1. Interacts with UBN1.
CC       Interacts with SCRIB (By similarity). Interacts with occludin and
CC       SAFB. Interaction with SAFB occurs in the nucleus.
CC   -!- INTERACTION:
CC       Q9PTD7:cgn (xeno); NbExp=1; IntAct=EBI-79579, EBI-79525;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity). Nucleus (By similarity). Cell
CC       junction, tight junction (By similarity). Note=Also nuclear under
CC       environmental stress conditions and in migratory endothelial cells
CC       and subconfluent epithelial cell cultures (By similarity).
CC   -!- SIMILARITY: Belongs to the MAGUK family.
CC   -!- SIMILARITY: Contains 1 guanylate kinase-like domain.
CC   -!- SIMILARITY: Contains 3 PDZ (DHR) domains.
CC   -!- SIMILARITY: Contains 1 SH3 domain.
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DR   EMBL; AF113005; AAD19964.1; -; mRNA.
DR   EMBL; BC034677; AAH34677.1; -; mRNA.
DR   EMBL; BC039924; AAH39924.1; -; mRNA.
DR   IPI; IPI00323349; -.
DR   RefSeq; NP_035727.2; NM_011597.4.
DR   UniGene; Mm.104744; -.
DR   PDB; 2CSJ; NMR; -; A=1-104.
DR   PDBsum; 2CSJ; -.
DR   ProteinModelPortal; Q9Z0U1; -.
DR   SMR; Q9Z0U1; 1-106, 286-364, 488-582, 584-870.
DR   IntAct; Q9Z0U1; 1.
DR   MINT; MINT-113156; -.
DR   STRING; Q9Z0U1; -.
DR   PhosphoSite; Q9Z0U1; -.
DR   PRIDE; Q9Z0U1; -.
DR   Ensembl; ENSMUST00000099558; ENSMUSP00000097154; ENSMUSG00000024812.
DR   GeneID; 21873; -.
DR   KEGG; mmu:21873; -.
DR   UCSC; uc008hal.1; mouse.
DR   CTD; 21873; -.
DR   MGI; MGI:1341872; Tjp2.
DR   eggNOG; roNOG13113; -.
DR   GeneTree; ENSGT00560000077038; -.
DR   HOGENOM; HBG443526; -.
DR   HOVERGEN; HBG017627; -.
DR   InParanoid; Q9Z0U1; -.
DR   OMA; DFEDTDG; -.
DR   OrthoDB; EOG4Q2DDQ; -.
DR   NextBio; 301380; -.
DR   ArrayExpress; Q9Z0U1; -.
DR   Bgee; Q9Z0U1; -.
DR   CleanEx; MM_TJP2; -.
DR   Genevestigator; Q9Z0U1; -.
DR   GermOnline; ENSMUSG00000024812; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005923; C:tight junction; IEA:UniProtKB-SubCell.
DR   InterPro; IPR008144; Guanylate_kin.
DR   InterPro; IPR008145; Guanylate_kin/L-typ_Ca_channel.
DR   InterPro; IPR001478; PDZ/DHR/GLGF.
DR   InterPro; IPR011511; SH3_2.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR005417; ZonOcculdens.
DR   InterPro; IPR005419; ZonOcculS2.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF00595; PDZ; 3.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR01597; ZONOCCLUDNS.
DR   PRINTS; PR01599; ZONOCCLUDNS2.
DR   SMART; SM00072; GuKc; 1.
DR   SMART; SM00228; PDZ; 3.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50156; PDZ; 3.
DR   SUPFAM; SSF50044; SH3; 1.
DR   PROSITE; PS00856; GUANYLATE_KINASE_1; FALSE_NEG.
DR   PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR   PROSITE; PS50106; PDZ; 3.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell junction; Cell membrane; Membrane; Nucleus;
KW   Phosphoprotein; Repeat; SH3 domain; Tight junction.
FT   CHAIN         1   1167       Tight junction protein ZO-2.
FT                                /FTId=PRO_0000094544.
FT   DOMAIN       10     97       PDZ 1.
FT   DOMAIN      287    365       PDZ 2.
FT   DOMAIN      489    570       PDZ 3.
FT   DOMAIN      584    649       SH3.
FT   DOMAIN      660    858       Guanylate kinase-like.
FT   REGION     1165   1167       Interaction with SCRIB (By similarity).
FT   COMPBIAS   1139   1142       Poly-Glu.
FT   MOD_RES     107    107       Phosphoserine.
FT   MOD_RES     145    145       Phosphoserine (By similarity).
FT   MOD_RES     147    147       Phosphoserine (By similarity).
FT   MOD_RES     234    234       Phosphotyrosine (By similarity).
FT   MOD_RES     238    238       Phosphotyrosine.
FT   MOD_RES     239    239       Phosphoserine.
FT   MOD_RES     263    263       Phosphoserine.
FT   MOD_RES     265    265       Phosphoserine.
FT   MOD_RES     267    267       Phosphoserine.
FT   MOD_RES     378    378       Phosphoserine (By similarity).
FT   MOD_RES     380    380       Phosphoserine (By similarity).
FT   MOD_RES     395    395       Phosphoserine (By similarity).
FT   MOD_RES     420    420       Phosphoserine (By similarity).
FT   MOD_RES     421    421       Phosphoserine (By similarity).
FT   MOD_RES     425    425       Phosphothreonine (By similarity).
FT   MOD_RES     435    435       Phosphothreonine (By similarity).
FT   MOD_RES     554    554       Phosphotyrosine (By similarity).
FT   MOD_RES     684    684       Phosphoserine (By similarity).
FT   MOD_RES     902    902       Phosphoserine (By similarity).
FT   MOD_RES     907    907       Phosphothreonine (By similarity).
FT   MOD_RES     915    915       Phosphothreonine (By similarity).
FT   MOD_RES     948    948       Phosphoserine (By similarity).
FT   MOD_RES     960    960       Phosphoserine (By similarity).
FT   MOD_RES     968    968       Phosphoserine.
FT   MOD_RES     988    988       Phosphoserine.
FT   MOD_RES    1044   1044       Phosphoserine (By similarity).
FT   MOD_RES    1095   1095       Phosphotyrosine.
FT   MOD_RES    1136   1136       Phosphoserine (By similarity).
FT   CONFLICT    100    100       Q -> L (in Ref. 1; AAD19964).
FT   CONFLICT    105    107       QGS -> LGC (in Ref. 1; AAD19964).
FT   CONFLICT    111    112       SH -> CL (in Ref. 1; AAD19964).
FT   CONFLICT    156    156       R -> G (in Ref. 1; AAD19964).
FT   CONFLICT    292    292       K -> Q (in Ref. 1; AAD19964).
FT   CONFLICT    378    378       S -> R (in Ref. 1; AAD19964).
FT   CONFLICT    447    447       A -> P (in Ref. 1; AAD19964).
FT   CONFLICT    454    454       S -> T (in Ref. 1; AAD19964).
FT   CONFLICT    470    470       T -> A (in Ref. 1; AAD19964).
FT   CONFLICT    506    506       A -> P (in Ref. 1; AAD19964).
FT   CONFLICT    633    633       E -> D (in Ref. 1; AAD19964).
FT   CONFLICT    649    649       A -> D (in Ref. 1; AAD19964).
FT   CONFLICT    664    664       D -> V (in Ref. 1; AAD19964).
FT   CONFLICT    667    667       R -> W (in Ref. 1; AAD19964).
FT   CONFLICT    670    670       G -> R (in Ref. 1; AAD19964).
FT   CONFLICT    674    674       S -> R (in Ref. 1; AAD19964).
FT   CONFLICT    677    677       V -> D (in Ref. 1; AAD19964).
FT   CONFLICT    680    680       N -> T (in Ref. 1; AAD19964).
FT   CONFLICT    690    691       AA -> RS (in Ref. 1; AAD19964).
FT   CONFLICT    731    731       T -> N (in Ref. 1; AAD19964).
FT   CONFLICT   1035   1035       M -> I (in Ref. 1; AAD19964).
FT   CONFLICT   1038   1038       S -> T (in Ref. 1; AAD19964).
FT   CONFLICT   1069   1069       A -> P (in Ref. 1; AAD19964).
FT   STRAND        4     14
FT   STRAND       17     19
FT   STRAND       23     26
FT   STRAND       42     46
FT   HELIX        52     55
FT   STRAND       61     67
FT   HELIX        75     84
FT   STRAND       87     98
SQ   SEQUENCE   1167 AA;  131280 MW;  C29AF94F423A3A70 CRC64;
     MEEVIWEQYT VTLQKDSKRG FGIAVSGGRD NPHFENGETS IVISDVLPGG PADGLLQEND
     RVVMVNGTPM EDVLHSFAVQ QLRKSGKIAA IVVKRPRKVQ VAPLQGSPPL SHDDRGFEVI
     EEFDGRSFRS GYSERSRHSS HDMLSHSWEG NRERGRPHQR TQSRERERSR GRSLERGLDQ
     EDYGRSRERS RGRSLERGLD RDFVSRDHSR GRSIDRDYDR DYERSYHEAY EPDYGGGYSP
     SYDRRAHPET RYERSRSREH LRSRSPSPES RSRHEHKGQH DPDRPIGVLL TKSKANEEYG
     LRLGSQIFIK EMTRTGLATK DGNLHEGDII LKINGTVTEN MSLTDARKLI EKSRGKLQLV
     VLRDSKQTLI NIPALNDSDS EVEDISEIES NRSFSPEERR QQYSDQDYHS STEKLKERPS
     SREETSGRLS RMGATPTPFK STGDITAAGV TEASREPRYQ EEGPVPQPRT APRVFLRPSP
     EDEAIYGPNT KMVRFKKGDS VGLRLAGGND VGIFVAGIQE GTSAEQEGLQ EGDQILKVNT
     QDFRGLVRED AVLYLLEIPK GETVTILAQS RADVYRDILA CGRGDSFFIR SHFECEKETP
     QSLAFTRGEV FRVVDTLYDG KLGHWLAVRI GNELEKGLIP NKSRAEQMAS VQNAQRENAG
     DRADFWRMRG QRSSGGVKKN LRKSREDLAA AVSVSTKFPA YEKVLLREAG FKRPVVLFGP
     IADIAMERLA TELPDLFQTA KTEPKDAGSE KSSGVVRLNT VRQIIEQDKH ALLDVTPKAV
     DLLNYTQWFP IVIFFNPDSR QGVKTIRQRL SPTSNKSSRK LFDQANKLKK TCSHLFTATI
     NVNSANDGWF GSLKDSIQQQ QNEAVWVSEG KMEGMDDDAE DRMSYLTAMG ADYLSCDSRL
     ISDFEDTDGE GGAYTDNELE EPAEEPLVSS ITRSSEPVQH EENIRKSSPE PRAQMRRAAS
     RDQLRDASPP PAFKPEPPKA RSQNREDSFD YSKSNLPATA GSEIPGGSTK GYPPPIAAKP
     AFGRPILKPS TPVPMPESEE VGESTEEQED APRSVLGRVK IFEKMDHKAK LQRMQELQEA
     QNARIEIAQK HPDIYAVPIK APKPDAGLPP HMSSRPPEPQ KAPSRLYQDT RGSYGSDPEE
     EEYRQQLAAH SKRGYYSQPS RYRDTEL
//
ID   KCND3_MOUSE             Reviewed;         655 AA.
AC   Q9Z0V1; Q8CC44; Q9Z0V0;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Potassium voltage-gated channel subfamily D member 3;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv4.3;
GN   Name=Kcnd3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=Swiss Webster; TISSUE=Heart ventricle;
RA   Tanaka H., Janzen K., Winkfein R.J., Fiset C., Clark R.B., Giles W.R.;
RT   "Cloning and functional characterization of mouse heart K+ channel
RT   alpha subunits, Kv1.5, Kv4.2 and Kv4.3.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   INTERACTION WITH KCNIP3.
RX   MEDLINE=21481767; PubMed=11598014; DOI=10.1093/emboj/20.20.5715;
RA   Liss B., Franz O., Sewing S., Bruns R., Neuhoff H., Roeper J.;
RT   "Tuning pacemaker frequency of individual dopaminergic neurons by
RT   Kv4.3L and KChip3.1 transcription.";
RL   EMBO J. 20:5715-5724(2001).
RN   [4]
RP   INTERACTION WITH KCND2 AND KCNIP2.
RX   MEDLINE=21906624; PubMed=11909823;
RX   DOI=10.1161/01.RES.0000012664.05949.E0;
RA   Guo W., Li H., Aimond F., Johns D.C., Rhodes K.J., Trimmer J.S.,
RA   Nerbonne J.M.;
RT   "Role of heteromultimers in the generation of myocardial transient
RT   outward K+ currents.";
RL   Circ. Res. 90:586-593(2002).
CC   -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated rapidly
CC       inactivating A-type potassium channels. May contribute to I(To)
CC       current in heart and I(Sa) current in neurons. Channel properties
CC       are modulated by interactions with other alpha subunits and with
CC       regulatory subunits.
CC   -!- SUBUNIT: Homotetramer or heterotetramer with KCND1 and/or KCND2.
CC       Associates with the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and
CC       KCNIP4. Interacts with DLG1, KCNE1, KCNE2, SCN1B and KCNAB1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell
CC       membrane, sarcolemma (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Kv4.3L;
CC         IsoId=Q9Z0V1-1; Sequence=Displayed;
CC       Name=2; Synonyms=Kv4.3M;
CC         IsoId=Q9Z0V1-2; Sequence=VSP_008827;
CC       Name=3;
CC         IsoId=Q9Z0V1-3; Sequence=VSP_008828, VSP_008829;
CC         Note=May be due to intron retention. No experimental
CC         confirmation available;
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position.
CC   -!- SIMILARITY: Belongs to the potassium channel family. D (Shal)
CC       (TC 1.A.1.2) subfamily. Kv4.3/KCND3 sub-subfamily.
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DR   EMBL; AF107781; AAD16973.1; -; mRNA.
DR   EMBL; AF107782; AAD16974.1; -; mRNA.
DR   EMBL; AK033962; BAC28529.1; -; mRNA.
DR   IPI; IPI00129489; -.
DR   IPI; IPI00282762; -.
DR   IPI; IPI00387305; -.
DR   RefSeq; NP_001034436.1; NM_001039347.1.
DR   RefSeq; NP_064315.1; NM_019931.1.
DR   UniGene; Mm.44530; -.
DR   ProteinModelPortal; Q9Z0V1; -.
DR   SMR; Q9Z0V1; 6-413.
DR   STRING; Q9Z0V1; -.
DR   PhosphoSite; Q9Z0V1; -.
DR   PRIDE; Q9Z0V1; -.
DR   Ensembl; ENSMUST00000079169; ENSMUSP00000078169; ENSMUSG00000040896.
DR   Ensembl; ENSMUST00000098761; ENSMUSP00000096357; ENSMUSG00000040896.
DR   Ensembl; ENSMUST00000118360; ENSMUSP00000113436; ENSMUSG00000040896.
DR   GeneID; 56543; -.
DR   KEGG; mmu:56543; -.
DR   NMPDR; fig|10090.3.peg.8739; -.
DR   UCSC; uc008qux.1; mouse.
DR   UCSC; uc008quy.1; mouse.
DR   UCSC; uc008quz.1; mouse.
DR   CTD; 56543; -.
DR   MGI; MGI:1928743; Kcnd3.
DR   GeneTree; ENSGT00580000081431; -.
DR   HOGENOM; HBG315067; -.
DR   HOVERGEN; HBG106687; -.
DR   InParanoid; Q9Z0V1; -.
DR   OMA; MGTPEEE; -.
DR   OrthoDB; EOG4HMJ8X; -.
DR   PhylomeDB; Q9Z0V1; -.
DR   NextBio; 312914; -.
DR   ArrayExpress; Q9Z0V1; -.
DR   Bgee; Q9Z0V1; -.
DR   Genevestigator; Q9Z0V1; -.
DR   GermOnline; ENSMUSG00000040896; Mus musculus.
DR   GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003975; K_chnl_volt-dep_Kv4.
DR   InterPro; IPR004056; K_chnl_volt-dep_Kv4.3.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   InterPro; IPR021645; Shal-type.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   Pfam; PF11601; Shal-type; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01518; KV43CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01497; SHALCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Ion transport; Ionic channel;
KW   Membrane; Metal-binding; Phosphoprotein; Potassium; Potassium channel;
KW   Potassium transport; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel; Zinc.
FT   CHAIN         1    655       Potassium voltage-gated channel subfamily
FT                                D member 3.
FT                                /FTId=PRO_0000054069.
FT   TOPO_DOM      1    181       Cytoplasmic (Potential).
FT   TRANSMEM    182    202       Helical; Name=Segment S1; (Potential).
FT   TRANSMEM    222    242       Helical; Name=Segment S2; (Potential).
FT   TOPO_DOM    243    256       Cytoplasmic (Potential).
FT   TRANSMEM    257    277       Helical; Name=Segment S3; (Potential).
FT   TRANSMEM    287    307       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TOPO_DOM    308    320       Cytoplasmic (Potential).
FT   TRANSMEM    321    341       Helical; Name=Segment S5; (Potential).
FT   INTRAMEM    360    380       Pore-forming; Name=Segment H5;
FT                                (Potential).
FT   TRANSMEM    382    402       Helical; Name=Segment S6; (Potential).
FT   TOPO_DOM    403    655       Cytoplasmic (Potential).
FT   REGION        2     20       Interaction with KCNIP2 (By similarity).
FT   MOTIF       367    372       Selectivity filter (By similarity).
FT   METAL       104    104       Zinc (By similarity).
FT   METAL       131    131       Zinc (By similarity).
FT   METAL       132    132       Zinc (By similarity).
FT   MOD_RES     435    435       Phosphothreonine (By similarity).
FT   MOD_RES     441    441       Phosphotyrosine (By similarity).
FT   VAR_SEQ     488    531       GLSYLVDDPLLSVRTSTIKNHEFIDEQMFEQNCMESSMQNY
FT                                PST -> VSSSLLPPPASSLTSQGCTHVIIPRRESSSVPFQ
FT                                SKTIVSLPLG (in isoform 3).
FT                                /FTId=VSP_008828.
FT   VAR_SEQ     488    506       Missing (in isoform 2).
FT                                /FTId=VSP_008827.
FT   VAR_SEQ     532    655       Missing (in isoform 3).
FT                                /FTId=VSP_008829.
SQ   SEQUENCE   655 AA;  73462 MW;  17FCE5AEC2868B33 CRC64;
     MAAGVAAWLP FARAAAIGWM PVANCPMPLA PADKNKRQDE LIVLNVSGRR FQTWRTTLER
     YPDTLLGSTE KEFFFNEDTK EYFFDRDPEV FRCVLNFYRT GKLHYPRYEC ISAYDDELAF
     YGILPEIIGD CCYEEYKDRK RENAERLMDD NDSENNQESM PSLSFRQTMW RAFENPHTST
     LALVFYYVTG FFIAVSVITN VVETVPCGTV PGSKELPCGE RYSVAFFCLD TACVMIFTVE
     YLLRLFAAPS RYRFIRSVMS IIDVVAIMPY YIGLVMTNNE DVSGAFVTLR VFRVFRIFKF
     SRHSQGLRIL GYTLKSCASE LGFLLFSLTM AIIIFATVMF YAEKGSSASK FTSIPASFWY
     TIVTMTTLGY GDMVPKTIAG KIFGSICSLS GVLVIALPVP VIVSNFSRIY HQNQRADKRR
     AQKKARLARI RVAKTGSSNA YLHSKRNGLL NEALELTGTP EEEQMGKTTS LIESQHHHLL
     HCLEKTTGLS YLVDDPLLSV RTSTIKNHEF IDEQMFEQNC MESSMQNYPS TRSPSLSSHS
     GLTTTCCSRR SKKTTHLPNS NLPATRLRSM QELSTLHIQG SEQPSLTTSR SSLNLKADDG
     LRPNCKTSQI TTAIISIPTP PALTPEGESR PPPASPGPNT NIPSITSNVV KVSAL
//
ID   KCND2_MOUSE             Reviewed;         630 AA.
AC   Q9Z0V2; Q8BSK3; Q8CHB7; Q9JJ60;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 102.
DE   RecName: Full=Potassium voltage-gated channel subfamily D member 2;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv4.2;
GN   Name=Kcnd2; Synonyms=Kiaa1044; ORFNames=MNCb-7013;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss Webster; TISSUE=Heart ventricle;
RA   Tanaka H., Janzen K., Winkfein R.J., Fiset C., Clark R.B., Giles W.R.;
RT   "Cloning and functional characterization of mouse heart K+ channel
RT   alpha subunits, Kv1.5, Kv4.2 and Kv4.3.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S.,
RA   Hashimoto K.;
RT   "Isolation of full-length cDNA clones from mouse brain cDNA library
RT   made by oligo-capping method.";
RL   Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22353125; PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
RA   Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   I. The complete nucleotide sequences of 100 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mesonephros, and Olfactory bulb;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PHOSPHORYLATION, AND TISSUE SPECIFICITY.
RX   MEDLINE=20497051; PubMed=11040264;
RA   Varga A.W., Anderson A.E., Adams J.P., Vogel H., Sweatt J.D.;
RT   "Input-specific immunolocalization of differentially phosphorylated
RT   Kv4.2 in the mouse brain.";
RL   Learn. Memory 7:321-332(2000).
RN   [7]
RP   INTERACTION WITH KCNIP3, MUTAGENESIS OF SER-552, AND PHOSPHORYLATION.
RX   MEDLINE=22338839; PubMed=12451113;
RA   Schrader L.A., Anderson A.E., Mayne A., Pfaffinger P.J., Sweatt J.D.;
RT   "PKA modulation of Kv4.2-encoded A-type potassium channels requires
RT   formation of a supramolecular complex.";
RL   J. Neurosci. 22:10123-10133(2002).
RN   [8]
RP   INTERACTION WITH KCND3 AND KCNIP2.
RX   MEDLINE=21906624; PubMed=11909823;
RX   DOI=10.1161/01.RES.0000012664.05949.E0;
RA   Guo W., Li H., Aimond F., Johns D.C., Rhodes K.J., Trimmer J.S.,
RA   Nerbonne J.M.;
RT   "Role of heteromultimers in the generation of myocardial transient
RT   outward K+ currents.";
RL   Circ. Res. 90:586-593(2002).
RN   [9]
RP   INTERACTION WITH KCNIP4.
RX   MEDLINE=21664433; PubMed=11805342; DOI=10.1073/pnas.022509299;
RA   Holmqvist M.H., Cao J., Hernandez-Pineda R., Jacobson M.D.,
RA   Carroll K.I., Sung M.A., Betty M., Ge P., Gilbride K.J., Brown M.E.,
RA   Jurman M.E., Lawson D., Silos-Santiago I., Xie Y., Covarrubias M.,
RA   Rhodes K.J., Distefano P.S., An W.F.;
RT   "Elimination of fast inactivation in Kv4 A-type potassium channels by
RT   an auxiliary subunit domain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:1035-1040(2002).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated rapidly
CC       inactivating A-type potassium channels. May contribute to I(To)
CC       current in heart and I(Sa) current in neurons. Channel properties
CC       are modulated by interactions with other alpha subunits and with
CC       regulatory subunits.
CC   -!- SUBUNIT: Homotetramer or heterotetramer with KCND1 and/or KCND3.
CC       Associates with the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and
CC       KCNIP4. Probably part of a complex consisting of KCNIP1, KCNIP2
CC       isoform 3 and KCND2. The KCND2-KCNIP2 channel complex contains
CC       four KCND2 and four KCNIP2 subunits. Interacts with DPP6, DPP10,
CC       DLG4, NCS1/FREQ, FLNA, FLNC and DLG1 (By similarity).
CC   -!- INTERACTION:
CC       Q99PW8:Kif17; NbExp=2; IntAct=EBI-959779, EBI-959754;
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Detected in brain, especially in hippocampus,
CC       medial habenular nucleus, striatum, amygdala, cortex and
CC       cerebellum.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position.
CC   -!- SIMILARITY: Belongs to the potassium channel family. D (Shal)
CC       (TC 1.A.1.2) subfamily. Kv4.2/KCND2 sub-subfamily.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA97986.1; Type=Frameshift; Positions=520;
CC       Sequence=BAC41464.1; Type=Erroneous initiation;
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DR   EMBL; AF107780; AAD16972.1; -; mRNA.
DR   EMBL; AB045326; BAA97986.1; ALT_FRAME; mRNA.
DR   EMBL; AB093280; BAC41464.1; ALT_INIT; mRNA.
DR   EMBL; AK032268; BAC27787.1; -; mRNA.
DR   EMBL; AK032772; BAC28015.1; -; mRNA.
DR   EMBL; BC079667; AAH79667.1; -; mRNA.
DR   IPI; IPI00129491; -.
DR   RefSeq; NP_062671.1; NM_019697.3.
DR   UniGene; Mm.425316; -.
DR   ProteinModelPortal; Q9Z0V2; -.
DR   SMR; Q9Z0V2; 6-416.
DR   IntAct; Q9Z0V2; 3.
DR   STRING; Q9Z0V2; -.
DR   PhosphoSite; Q9Z0V2; -.
DR   PRIDE; Q9Z0V2; -.
DR   Ensembl; ENSMUST00000081542; ENSMUSP00000080257; ENSMUSG00000060882.
DR   GeneID; 16508; -.
DR   KEGG; mmu:16508; -.
DR   NMPDR; fig|10090.3.peg.12988; -.
DR   UCSC; uc009baq.1; mouse.
DR   CTD; 16508; -.
DR   MGI; MGI:102663; Kcnd2.
DR   eggNOG; roNOG09052; -.
DR   GeneTree; ENSGT00580000081431; -.
DR   HOGENOM; HBG315067; -.
DR   HOVERGEN; HBG106687; -.
DR   InParanoid; Q9Z0V2; -.
DR   OMA; VIGDCCY; -.
DR   OrthoDB; EOG4HMJ8X; -.
DR   PhylomeDB; Q9Z0V2; -.
DR   NextBio; 289839; -.
DR   ArrayExpress; Q9Z0V2; -.
DR   Bgee; Q9Z0V2; -.
DR   Genevestigator; Q9Z0V2; -.
DR   GermOnline; ENSMUSG00000060882; Mus musculus.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR000210; BTB/POZ-like.
DR   InterPro; IPR011333; BTB/POZ_fold.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003975; K_chnl_volt-dep_Kv4.
DR   InterPro; IPR004055; K_chnl_volt-dep_Kv4.2.
DR   InterPro; IPR003131; K_chnl_volt-dep_Kv_tetra.
DR   InterPro; IPR021645; Shal-type.
DR   Gene3D; G3DSA:3.30.710.10; BTB/POZ_fold; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02214; K_tetra; 1.
DR   Pfam; PF11601; Shal-type; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01517; KV42CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01497; SHALCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; BTB/POZ_fold; 1.
PE   1: Evidence at protein level;
KW   Ion transport; Ionic channel; Membrane; Metal-binding; Phosphoprotein;
KW   Potassium; Potassium channel; Potassium transport; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel; Zinc.
FT   CHAIN         1    630       Potassium voltage-gated channel subfamily
FT                                D member 2.
FT                                /FTId=PRO_0000054065.
FT   TOPO_DOM      1    183       Cytoplasmic (Potential).
FT   TRANSMEM    184    204       Helical; Name=Segment S1; (Potential).
FT   TRANSMEM    225    245       Helical; Name=Segment S2; (Potential).
FT   TOPO_DOM    246    259       Cytoplasmic (Potential).
FT   TRANSMEM    260    280       Helical; Name=Segment S3; (Potential).
FT   TRANSMEM    290    310       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TOPO_DOM    311    323       Cytoplasmic (Potential).
FT   TRANSMEM    324    344       Helical; Name=Segment S5; (Potential).
FT   INTRAMEM    363    383       Pore-forming; Name=Segment H5;
FT                                (Potential).
FT   TRANSMEM    385    405       Helical; Name=Segment S6; (Potential).
FT   TOPO_DOM    406    630       Cytoplasmic (Potential).
FT   REGION        2     20       Interaction with KCNIP2 (By similarity).
FT   REGION        7     11       Interaction with KCNIP1 (By similarity).
FT   REGION       71     90       Interaction with KCNIP1 (By similarity).
FT   MOTIF       370    375       Selectivity filter (By similarity).
FT   METAL       105    105       Zinc (By similarity).
FT   METAL       132    132       Zinc (By similarity).
FT   METAL       133    133       Zinc (By similarity).
FT   MOD_RES      38     38       Phosphothreonine.
FT   MOD_RES     548    548       Phosphoserine.
FT   MOD_RES     552    552       Phosphoserine.
FT   MOD_RES     602    602       Phosphothreonine.
FT   MOD_RES     607    607       Phosphothreonine.
FT   MOD_RES     616    616       Phosphoserine.
FT   MUTAGEN     552    552       S->A: Abolishes PKA-mediated modulation
FT                                of channel activity.
FT   CONFLICT     22     22       V -> A (in Ref. 2; BAA97986).
FT   CONFLICT    516    516       S -> R (in Ref. 3; BAC41464).
SQ   SEQUENCE   630 AA;  70577 MW;  7FB94277429E7683 CRC64;
     MAAGVAAWLP FARAAAIGWM PVASGPMPAP PRQERKRTQD ALIVLNVSGT RFQTWQDTLE
     RYPDTLLGSS ERDFFYHPET QQYFFDRDPD IFRHILNFYR TGKLHYPRHE CISAYDEELA
     FFGLIPEIIG DCCYEEYKDR RRENAERLQD DADTDNTGES ALPTMTARQR VWRAFENPHT
     STMALVFYYV TGFFIAVSVI ANVVETVPCG SSPGHIKELP CGERYAVAFF CLDTACVMIF
     TVEYLLRLAA APSRYRFVRS VMSIIDVVAI LPYYIGLVMT DNEDVSGAFV TLRVFRVFRI
     FKFSRHSQGL RILGYTLKSC ASELGFLLFS LTMAIIIFAT VMFYAEKGSS ASKFTSIPAA
     FWYTIVTMTT LGYGDMVPKT IAGKIFGSIC SLSGVLVIAL PVPVIVSNFS RIYHQNQRAD
     KRRAQKKARL ARIRAAKSGS ANAYMQSKRN GLLSNQLQSS EDEPAFISKS GSSFETQHHH
     LLHCLEKTTN HEFVDEQVFE ESCMEVATVN RPSSHSPSLS SQQGVTSTCC SRRHKKTFRI
     PNANVSGSHR GSVQELSTIQ IRCVERTPLS NSRSSLNAKM EECVKLNCEQ PYVTTAIISI
     PTPPVTTPEG DDRPESPEYS GGNIVRVSAL
//
ID   NU160_MOUSE             Reviewed;        1402 AA.
AC   Q9Z0W3; Q3TBI7; Q3TP11; Q3U250; Q6A0A7; Q7TME1; Q9CZD9;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 2.
DT   08-MAR-2011, entry version 76.
DE   RecName: Full=Nuclear pore complex protein Nup160;
DE   AltName: Full=160 kDa nucleoporin;
DE   AltName: Full=Gene trap locus 1-13 protein;
DE            Short=GTL-13;
DE   AltName: Full=Nucleoporin Nup160;
GN   Name=Nup160; Synonyms=Gtl1-13, Kiaa0197;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=129/SvJ;
RA   Van de Putte T., Cozijnsen M., Dewulf N., Tylzanowski P., Lonnoy O.,
RA   Huylebroeck D.;
RT   "Mus musculus mRNA for gtl-13 (gene trap locus-13), similar to human
RT   KIAA0197 gene (D83781), complete cds.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-985 AND 1151-1402 (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, Embryo, and Heart;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 542-1402 (ISOFORM 1).
RC   TISSUE=Natural killer cell;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [5]
RP   IDENTIFICATION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   MEDLINE=21448620; PubMed=11564755; DOI=10.1083/jcb.200101081;
RA   Belgareh N., Rabut G., Bai S.W., van Overbeek M., Beaudouin J.,
RA   Daigle N., Zatsepina O.V., Pasteau F., Labas V., Fromont-Racine M.,
RA   Ellenberg J., Doye V.;
RT   "An evolutionarily conserved NPC subcomplex, which redistributes in
RT   part to kinetochores in mammalian cells.";
RL   J. Cell Biol. 154:1147-1160(2001).
RN   [6]
RP   IDENTIFICATION, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   MEDLINE=21541555; PubMed=11684705; DOI=10.1083/jcb.200108007;
RA   Vasu S., Shah S., Orjalo A., Park M., Fischer W.H., Forbes D.J.;
RT   "Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA
RT   export.";
RL   J. Cell Biol. 155:339-354(2001).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1161, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1123, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
RA   Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT   "Large scale localization of protein phosphorylation by use of
RT   electron capture dissociation mass spectrometry.";
RL   Mol. Cell. Proteomics 8:904-912(2009).
CC   -!- FUNCTION: Involved in poly(A)+ RNA transport.
CC   -!- SUBUNIT: Forms part of the Nup160 subcomplex in the nuclear pore
CC       which is composed of Nup160, Nup133, Nup107 and Nup96. This
CC       complex plays a role in RNA export and in tethering Nup98 and
CC       Nup153 to the nucleus.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Z0W3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Z0W3-2; Sequence=VSP_018500, VSP_018501;
CC         Note=No experimental confirmation available;
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AF104415; AAD17922.2; -; mRNA.
DR   EMBL; AK012715; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AK155492; BAE33292.1; -; mRNA.
DR   EMBL; AK164802; BAE37926.1; -; mRNA.
DR   EMBL; AK171218; BAE42322.1; -; mRNA.
DR   EMBL; BC052450; AAH52450.1; -; mRNA.
DR   EMBL; BC054523; AAH54523.1; -; mRNA.
DR   EMBL; AK172911; BAD32189.1; -; mRNA.
DR   IPI; IPI00129535; -.
DR   IPI; IPI00758290; -.
DR   RefSeq; NP_067487.1; NM_021512.2.
DR   UniGene; Mm.24532; -.
DR   ProteinModelPortal; Q9Z0W3; -.
DR   STRING; Q9Z0W3; -.
DR   PhosphoSite; Q9Z0W3; -.
DR   PRIDE; Q9Z0W3; -.
DR   Ensembl; ENSMUST00000057481; ENSMUSP00000059289; ENSMUSG00000051329.
DR   GeneID; 59015; -.
DR   KEGG; mmu:59015; -.
DR   UCSC; uc008ksw.1; mouse.
DR   UCSC; uc008ksy.1; mouse.
DR   CTD; 59015; -.
DR   MGI; MGI:1926227; Nup160.
DR   GeneTree; ENSGT00390000000972; -.
DR   HOVERGEN; HBG052681; -.
DR   InParanoid; Q9Z0W3; -.
DR   OMA; LERYKVQ; -.
DR   OrthoDB; EOG43TZTN; -.
DR   PhylomeDB; Q9Z0W3; -.
DR   NextBio; 314572; -.
DR   ArrayExpress; Q9Z0W3; -.
DR   Bgee; Q9Z0W3; -.
DR   CleanEx; MM_NUP160; -.
DR   Genevestigator; Q9Z0W3; -.
DR   GermOnline; ENSMUSG00000051329; Mus musculus.
DR   GO; GO:0031080; C:Nup107-160 complex; ISS:UniProtKB.
DR   GO; GO:0005487; F:nucleocytoplasmic transporter activity; IDA:UniProtKB.
DR   GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:UniProtKB-KW.
DR   InterPro; IPR021717; Nup160.
DR   Pfam; PF11715; Nup160; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; mRNA transport; Nuclear pore complex; Nucleus;
KW   Phosphoprotein; Protein transport; Translocation; Transport.
FT   CHAIN         1   1402       Nuclear pore complex protein Nup160.
FT                                /FTId=PRO_0000204852.
FT   MOD_RES    1123   1123       Phosphoserine.
FT   MOD_RES    1161   1161       Phosphothreonine.
FT   VAR_SEQ     836    839       WPSN -> YPFA (in isoform 2).
FT                                /FTId=VSP_018500.
FT   VAR_SEQ     840   1402       Missing (in isoform 2).
FT                                /FTId=VSP_018501.
FT   CONFLICT    562    563       Missing (in Ref. 3; AAH52450/AAH54523).
FT   CONFLICT   1156   1156       A -> T (in Ref. 2).
FT   CONFLICT   1314   1314       E -> G (in Ref. 2; AK012715).
FT   CONFLICT   1368   1368       N -> D (in Ref. 2; AK012715).
SQ   SEQUENCE   1402 AA;  158232 MW;  3BF5D9F057D28772 CRC64;
     MAAAGSLERS FVELSGAERE RPRHFREFTV CDIGTASAAF GTVKYSESAG GFYYVESGKL
     FSITRNRFIH WKTSGDTLEL VEESLDLNLL NNAVRLKFQN YNILPGGVHV SETQNHVIIL
     ILTNQTVHRL ILPHPSRMYR SELVTESQMQ SIFTDIGKVD FRDPCNSQLI PSVPGLSPGS
     TTSAAWLSSD GEALFALPSA SGGIFVLKLP PYDVPGIASV VELKQSSVMQ RLLTGWMPTA
     IRGDHGPSDR ALSLAVHCVE HDAFIFALCQ DHKLRMWSYK DQMCLMVADM LEYVPVNKDL
     RLTAGTGHKL RLAYSPSMGL YLGIYMHAPK RGQFCVFQLV STENNRYSLD HISSLFTSQE
     TLVDFALTST DIWALWHDAE NQTIVKYINF EHNVAGQWNP VFMQPLPEEE IVIRDDQDPR
     EMYLRSLFTP GHFINAALCK ALQIFCRGTE RNLDLSWNEL KKEITLAVEN ELQGSVTEYE
     FSQDEFRTLQ QEFWCKFYAC VLQYQEALSH PLALHLNPVT NMVCLLKKGY LSFLVPSSLV
     DHLYLLPDEH LLTEDETTIS DDADVARDVL CLIKCLRMIG ESVTMDMAVL METSCYNLQS
     PEKAAEHILE DLITIDVENV MEDICSKLQE IRNPVHAIGL LIREMDYETE VEMEKGFDPA
     QPLNVRMNLS QLYGSSTAGY IVCRGVYKIA STRFLICRDL LILQQLLTRL GDAVILGAGQ
     LFQAQQDLLH RTAPLLLSYY LIKWASQCLA TDVPVDTLES NLQHLSVLEL TDSGALMANK
     LVSSPQTIME LFFQEVARKQ IISHLFSQPK APLSQTGLNW PEMITAVTGY LLQLLWPSNP
     GCLFLECLMG NCQYVQLQDY IQLLHPWCQV NVGSCRFMLG RCYLVTGEVQ KALECFCQAA
     SEVGKEEFLD RLIRSEDGEI VSTPKLQYYD KVLRLLDVVG LPELVIQLAT SAITEAGDDW
     KSQATLRTCI FKHHLDLGHN SQAYEALTQI PDSSRQLDCL RQLVVVLCER SQLQDLVEFP
     YVNLHNEVVG IIESRARAVD LMTHNYYELL YAFHIYRHNY RKAGTVMFEY GMRLGREVRT
     LRGLEKQGNC YLAAINCLRL IRPEYAWIVQ PASGAVSDRP GASPKRNHDG ECTAAPTNRQ
     IEILELEDLE KEYSLARIRL TLARHDPSVI AIAGSSSAKE MSALLVQAGL FDTAISLCQT
     FTLPLTPVFE GLAFKCIKLQ FGGEAAQGEA WSWLATNQLS SVITTKESSA TDEAWRLLST
     YLERYKVQNN LYHHCVINKL LSHGVPLPNW LINSYKKVDA AELLRLYLNY DLLEEAVDLV
     SEYVDAVLGK GHQYFGIEFP LSATAPMVWL PYSSIDQLLQ ALGENSANSH NIILSQKILD
     KLEDYQQKVD KATRDLLYRR DL
//
ID   AIFM1_MOUSE             Reviewed;         612 AA.
AC   Q9Z0X1;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 104.
DE   RecName: Full=Apoptosis-inducing factor 1, mitochondrial;
DE            EC=1.-.-.-;
DE   AltName: Full=Programmed cell death protein 8;
DE   Flags: Precursor;
GN   Name=Aifm1; Synonyms=Aif, Pdcd8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, PROTEIN
RP   SEQUENCE OF 322-336, FUNCTION, COFACTOR, MASS SPECTROMETRY, AND
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=99142517; PubMed=9989411; DOI=10.1038/17135;
RA   Susin S.A., Lorenzo H.K., Zamzami N., Marzo I., Snow B.E.,
RA   Brothers G.M., Mangion J., Jacotot E., Costantini P., Loeffler M.,
RA   Larochette N., Goodlett D.R., Aebersold R., Siderovski D.P.,
RA   Penninger J.M., Kroemer G.;
RT   "Molecular characterization of mitochondrial apoptosis-inducing
RT   factor.";
RL   Nature 397:441-446(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 378-386, AND MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-592, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 108-610 IN COMPLEX WITH FAD,
RP   NAD-BINDING, AND MUTAGENESIS OF LYS-176 AND GLU-313.
RX   PubMed=11967568; DOI=10.1038/nsb793;
RA   Mate M.J., Ortiz-Lombardia M., Boitel B., Haouz A., Tello D.,
RA   Susin S.A., Penninger J., Kroemer G., Alzari P.M.;
RT   "The crystal structure of the mouse apoptosis-inducing factor AIF.";
RL   Nat. Struct. Biol. 9:442-446(2002).
CC   -!- FUNCTION: Probable oxidoreductase that has a dual role in
CC       controlling cellular life and death; during apoptosis, it is
CC       translocated from the mitochondria to the nucleus to function as a
CC       proapoptotic factor in a caspase-independent pathway, while in
CC       normal mitochondria, it functions as an antiapoptotic factor via
CC       its oxidoreductase activity. The soluble form (AIFsol) found in
CC       the nucleus induces 'parthanatos' i.e., caspase-independent
CC       fragmentation of chromosomal DNA. Interacts with EIF3G,and thereby
CC       inhibits the EIF3 machinery and protein synthesis,and activates
CC       casapse-7 to amplify apoptosis. Plays a critical role in caspase-
CC       independent, pyknotic cell death in hydrogen peroxide-exposed
CC       cells. Binds to DNA in a sequence-independent manner (By
CC       similarity).
CC   -!- COFACTOR: FAD.
CC   -!- SUBUNIT: Interacts with XIAP. Interacts (via N-terminus) with
CC       EIF3G (via C-terminus) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space.
CC       Mitochondrion inner membrane (By similarity). Cytoplasm (By
CC       similarity). Cytoplasm, perinuclear region (By similarity).
CC       Nucleus. Note=Proteolytic cleavage during or just after
CC       translocation into the mitochondrial intermembrane space (IMS)
CC       results in the formation of an inner-membrane-anchored mature form
CC       (AIFmit). During apoptosis, further proteolytic processing leads
CC       to a mature form, which is confined to the mitochondrial IMS in a
CC       soluble form (AIFsol). AIFsol is released to the cytoplasm in
CC       response to specific death signals, and translocated to the
CC       nucleus, where it induces nuclear apoptosis. Colocalizes with
CC       EIF3G in the nucleus and perinuclear region (By similarity).
CC   -!- PTM: Under normal conditions, a 54-residue N-terminal segment is
CC       first proteolytically removed during or just after translocation
CC       into the mitochondrial intermembrane space (IMS) by the
CC       mitochondrial processing peptidase (MPP) to form the inner-
CC       membrane-anchored mature form (AIFmit). During apoptosis, it is
CC       further proteolytically processed at amino-acid position 101
CC       leading to the generation of the mature form, which is confined to
CC       the mitochondrial IMS in a soluble form (AIFsol). AIFsol is
CC       released to the cytoplasm in response to specific death signals,
CC       and translocated to the nucleus, where it induces nuclear
CC       apoptosis in a caspase-independent manner (By similarity).
CC   -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase family.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF100927; AAD16435.1; -; mRNA.
DR   EMBL; BC003292; AAH03292.1; -; mRNA.
DR   IPI; IPI00129577; -.
DR   RefSeq; NP_036149.1; NM_012019.2.
DR   UniGene; Mm.240434; -.
DR   PDB; 1GV4; X-ray; 2.00 A; A/B=122-610.
DR   PDB; 3GD3; X-ray; 2.95 A; A/B/C/D=78-612.
DR   PDB; 3GD4; X-ray; 2.24 A; A/B=102-612.
DR   PDBsum; 1GV4; -.
DR   PDBsum; 3GD3; -.
DR   PDBsum; 3GD4; -.
DR   ProteinModelPortal; Q9Z0X1; -.
DR   SMR; Q9Z0X1; 121-610.
DR   STRING; Q9Z0X1; -.
DR   PhosphoSite; Q9Z0X1; -.
DR   PRIDE; Q9Z0X1; -.
DR   Ensembl; ENSMUST00000037349; ENSMUSP00000041104; ENSMUSG00000036932.
DR   GeneID; 26926; -.
DR   KEGG; mmu:26926; -.
DR   UCSC; uc009tcg.1; mouse.
DR   CTD; 26926; -.
DR   MGI; MGI:1349419; Aifm1.
DR   GeneTree; ENSGT00530000063416; -.
DR   HOGENOM; HBG644911; -.
DR   HOVERGEN; HBG053538; -.
DR   InParanoid; Q9Z0X1; -.
DR   OMA; KIGDFRT; -.
DR   OrthoDB; EOG40S0FD; -.
DR   PhylomeDB; Q9Z0X1; -.
DR   NextBio; 304817; -.
DR   ArrayExpress; Q9Z0X1; -.
DR   Bgee; Q9Z0X1; -.
DR   Genevestigator; Q9Z0X1; -.
DR   GermOnline; ENSMUSG00000036932; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; ISS:UniProtKB.
DR   GO; GO:0005741; C:mitochondrial outer membrane; TAS:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005625; C:soluble fraction; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; TAS:MGI.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0006919; P:activation of caspase activity; ISS:UniProtKB.
DR   GO; GO:0070059; P:apoptosis in response to endoplasmic reticulum stress; IMP:UniProtKB.
DR   GO; GO:0008637; P:apoptotic mitochondrial changes; TAS:MGI.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0006309; P:DNA fragmentation involved in apoptotic nuclear change; IGI:MGI.
DR   GO; GO:0051402; P:neuron apoptosis; IGI:MGI.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD-bd.
DR   Gene3D; G3DSA:3.30.390.30; Pyr_redox_dim; 1.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   SUPFAM; SSF55424; FAD/NAD-linked_reductase_dimer; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Apoptosis; Cytoplasm;
KW   Direct protein sequencing; DNA-binding; FAD; Flavoprotein; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Nucleus; Oxidoreductase;
KW   Phosphoprotein; Transit peptide.
FT   TRANSIT       1     54       Mitochondrion (By similarity).
FT   PROPEP       55    101       Removed in mature form.
FT                                /FTId=PRO_0000401936.
FT   CHAIN       102    612       Apoptosis-inducing factor 1,
FT                                mitochondrial.
FT                                /FTId=PRO_0000022031.
FT   NP_BIND     137    141       FAD.
FT   NP_BIND     163    164       FAD.
FT   NP_BIND     453    454       FAD.
FT   REGION      133    482       FAD-dependent oxidoreductase.
FT   MOTIF       445    450       Nuclear localization signal (Potential).
FT   BINDING     171    171       FAD.
FT   BINDING     176    176       FAD.
FT   BINDING     232    232       FAD; via amide nitrogen and carbonyl
FT                                oxygen.
FT   BINDING     284    284       FAD.
FT   BINDING     437    437       FAD.
FT   BINDING     482    482       FAD; via carbonyl oxygen.
FT   MOD_RES     267    267       Phosphoserine (By similarity).
FT   MOD_RES     294    294       N6-acetyllysine (By similarity).
FT   MOD_RES     592    592       N6-acetyllysine.
FT   MUTAGEN     176    176       K->A: Increases catalytic efficiency.
FT   MUTAGEN     313    313       E->A: Increases catalytic efficiency 30-
FT                                fold. Increases affinity for NADH 20-
FT                                fold.
FT   STRAND      129    137
FT   HELIX       140    152
FT   STRAND      157    166
FT   HELIX       172    175
FT   HELIX       177    179
FT   HELIX       186    189
FT   STRAND      191    193
FT   STRAND      199    205
FT   HELIX       207    209
FT   HELIX       213    218
FT   STRAND      223    229
FT   STRAND      232    236
FT   TURN        237    240
FT   STRAND      241    244
FT   STRAND      249    257
FT   STRAND      261    263
FT   HELIX       267    270
FT   HELIX       274    277
FT   STRAND      280    282
FT   HELIX       286    296
FT   STRAND      300    305
FT   HELIX       309    325
FT   STRAND      328    332
FT   STRAND      334    337
FT   TURN        338    342
FT   HELIX       345    356
FT   TURN        357    359
FT   STRAND      361    363
FT   STRAND      368    374
FT   STRAND      377    382
FT   STRAND      387    395
FT   STRAND      399    401
FT   HELIX       404    406
FT   TURN        407    410
FT   TURN        415    417
FT   STRAND      419    421
FT   STRAND      426    429
FT   STRAND      432    434
FT   HELIX       436    438
FT   STRAND      439    443
FT   TURN        444    446
FT   STRAND      447    449
FT   HELIX       454    468
FT   STRAND      480    486
FT   STRAND      490    495
FT   STRAND      503    508
FT   HELIX       516    523
FT   HELIX       528    532
FT   HELIX       556    558
FT   STRAND      561    579
FT   HELIX       584    593
FT   HELIX       600    604
FT   HELIX       605    607
SQ   SEQUENCE   612 AA;  66765 MW;  A17EDFD5CF77BB85 CRC64;
     MFRCGGLAGA FKQKLVPLVR TVYVQRPKQR NRLPGNLFQQ WRVPLELQMA RQMASSGSSG
     GKMDNSVLVL IVGLSTIGAG AYAYKTIKED QKRYNERVMG LGLSPEEKQR RAIASATEGG
     SVPQIRAPSH VPFLLIGGGT AAFAAARSIR ARDPGARVLI VSEDPELPYM RPPLSKELWF
     SDDPNVTKTL QFRQWNGKER SIYFQPPSFY VSAQDLPNIE NGGVAVLTGK KVVHLDVRGN
     MVKLNDGSQI TFEKCLIATG GTPRSLSAID RAGAEVKSRT TLFRKIGDFR ALEKISREVK
     SITVIGGGFL GSELACALGR KSQASGIEVI QLFPEKGNMG KILPQYLSNW TMEKVKREGV
     KVMPNAIVQS VGVSGGRLLI KLKDGRKVET DHIVTAVGLE PNVELAKTGG LEIDSDFGGF
     RVNAELQARS NIWVAGDAAC FYDIKLGRRR VEHHDHAVVS GRLAGENMTG AAKPYWHQSM
     FWSDLGPDVG YEAIGLVDSS LPTVGVFAKA TAQDNPKSAT EQSGTGIRSE SETESEASEI
     TIPPSAPAVP QVPVEGEDYG KGVIFYLRDK VVVGIVLWNV FNRMPIARKI IKDGEQHEDL
     NEVAKLFNIH ED
//
ID   HEPH_MOUSE              Reviewed;        1157 AA.
AC   Q9Z0Z4; Q6ZQ65; Q80Y80; Q8C4S2;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Hephaestin;
DE            EC=1.-.-.-;
DE   Flags: Precursor;
GN   Name=Heph; Synonyms=Kiaa0698;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RX   MEDLINE=99140771; PubMed=9988272; DOI=10.1038/5979;
RA   Vulpe C.D., Kuo Y.M., Murphy T.L., Cowley L., Askwith C., Libina N.,
RA   Gitschier J., Anderson G.J.;
RT   "Hephaestin, a ceruloplasmin homologue implicated in intestinal iron
RT   transport, is defective in the sla mouse.";
RL   Nat. Genet. 21:195-199(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryonic tail;
RX   MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-889.
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: May function as a ferroxidase for ferrous (II) to ferric
CC       ion (III) conversion and may be involved in copper transport and
CC       homeostasis. Implicated in iron homeostasis and may mediate iron
CC       efflux associated to ferroportin 1.
CC   -!- COFACTOR: Binds 6 copper ions per monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Z0Z4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Z0Z4-2; Sequence=VSP_011628;
CC   -!- DISEASE: Note=Defects in Heph are a cause of the sex-linked anemia
CC       (sla) that is characterized by moderate to severe microcytic
CC       hypochronic anemia.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC   -!- SIMILARITY: Contains 6 plastocyanin-like domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC98004.1; Type=Erroneous initiation;
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DR   EMBL; AF082567; AAD16035.1; -; mRNA.
DR   EMBL; AK129194; BAC98004.1; ALT_INIT; mRNA.
DR   EMBL; BC048237; AAH48237.1; -; mRNA.
DR   EMBL; BC054442; AAH54442.1; -; mRNA.
DR   EMBL; AK081330; BAC38197.1; -; mRNA.
DR   IPI; IPI00471264; -.
DR   IPI; IPI00471265; -.
DR   RefSeq; NP_001153099.1; NM_001159627.1.
DR   RefSeq; NP_034547.2; NM_010417.2.
DR   RefSeq; NP_851790.1; NM_181273.4.
DR   UniGene; Mm.277092; -.
DR   ProteinModelPortal; Q9Z0Z4; -.
DR   SMR; Q9Z0Z4; 24-1073.
DR   STRING; Q9Z0Z4; -.
DR   PhosphoSite; Q9Z0Z4; -.
DR   PRIDE; Q9Z0Z4; -.
DR   Ensembl; ENSMUST00000033553; ENSMUSP00000033553; ENSMUSG00000031209.
DR   Ensembl; ENSMUST00000113838; ENSMUSP00000109469; ENSMUSG00000031209.
DR   GeneID; 15203; -.
DR   KEGG; mmu:15203; -.
DR   UCSC; uc009tuk.1; mouse.
DR   UCSC; uc009tul.1; mouse.
DR   CTD; 15203; -.
DR   MGI; MGI:1332240; Heph.
DR   GeneTree; ENSGT00550000074552; -.
DR   HOGENOM; HBG357170; -.
DR   HOVERGEN; HBG003674; -.
DR   InParanoid; Q9Z0Z4; -.
DR   OrthoDB; EOG4F4S98; -.
DR   NextBio; 287747; -.
DR   ArrayExpress; Q9Z0Z4; -.
DR   Bgee; Q9Z0Z4; -.
DR   CleanEx; MM_HEPH; -.
DR   Genevestigator; Q9Z0Z4; -.
DR   GermOnline; ENSMUSG00000031209; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0006826; P:iron ion transport; TAS:MGI.
DR   GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
DR   InterPro; IPR011706; Cu-oxidase_2.
DR   InterPro; IPR011707; Cu-oxidase_3.
DR   InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR   InterPro; IPR008972; Cupredoxin.
DR   Gene3D; G3DSA:2.60.40.420; Cupredoxin; 6.
DR   Pfam; PF07731; Cu-oxidase_2; 1.
DR   Pfam; PF07732; Cu-oxidase_3; 3.
DR   SUPFAM; SSF49503; Cupredoxin; 6.
DR   PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3.
DR   PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Copper; Copper transport; Disulfide bond;
KW   Glycoprotein; Ion transport; Iron; Iron transport; Membrane;
KW   Metal-binding; Oxidoreductase; Repeat; Signal; Transmembrane;
KW   Transmembrane helix; Transport.
FT   SIGNAL        1     18       Potential.
FT   CHAIN        19   1157       Hephaestin.
FT                                /FTId=PRO_0000002916.
FT   TOPO_DOM     19   1109       Extracellular (Potential).
FT   TRANSMEM   1110   1130       Helical; (Potential).
FT   TOPO_DOM   1131   1157       Cytoplasmic (Potential).
FT   DOMAIN       24    206       Plastocyanin-like 1.
FT   DOMAIN      218    366       Plastocyanin-like 2.
FT   DOMAIN      379    559       Plastocyanin-like 3.
FT   DOMAIN      569    717       Plastocyanin-like 4.
FT   DOMAIN      730    902       Plastocyanin-like 5.
FT   DOMAIN      910   1086       Plastocyanin-like 6.
FT   METAL       126    126       Copper 1; type 2 (By similarity).
FT   METAL       128    128       Copper 2; type 3 (By similarity).
FT   METAL       186    186       Copper 2; type 3 (By similarity).
FT   METAL       188    188       Copper 3; type 3 (By similarity).
FT   METAL       304    304       Copper 4; type 1 (By similarity).
FT   METAL       347    347       Copper 4; type 1 (By similarity).
FT   METAL       352    352       Copper 4; type 1 (By similarity).
FT   METAL       655    655       Copper 5; type 1 (By similarity).
FT   METAL       698    698       Copper 5; type 1 (By similarity).
FT   METAL       703    703       Copper 5; type 1 (By similarity).
FT   METAL       708    708       Copper 5; type 1 (By similarity).
FT   METAL       999    999       Copper 6; type 1 (By similarity).
FT   METAL      1002   1002       Copper 1; type 2 (By similarity).
FT   METAL      1004   1004       Copper 3; type 3 (By similarity).
FT   METAL      1044   1044       Copper 3; type 3 (By similarity).
FT   METAL      1045   1045       Copper 6; type 1 (By similarity).
FT   METAL      1046   1046       Copper 2; type 3 (By similarity).
FT   METAL      1050   1050       Copper 6; type 1 (By similarity).
FT   METAL      1055   1055       Copper 6; type 1 (By similarity).
FT   CARBOHYD     49     49       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     54     54       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    164    164       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    236    236       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    587    587       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    713    713       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    757    757       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    930    930       N-linked (GlcNAc...) (Potential).
FT   DISULFID    180    206       Potential.
FT   DISULFID    285    366       Potential.
FT   DISULFID    533    559       Potential.
FT   DISULFID    636    717       Potential.
FT   DISULFID    876    902       Potential.
FT   VAR_SEQ    1081   1081       Missing (in isoform 2).
FT                                /FTId=VSP_011628.
FT   CONFLICT    501    542       Missing (in Ref. 4; BAC38197).
FT   CONFLICT    593    593       S -> N (in Ref. 1; AAD16035 and 4;
FT                                BAC38197).
FT   CONFLICT    856    889       VLTYQWNIPERSGPGPSDSACVSWIYYSAVDPIK -> LEH
FT                                LMKRQRLYNPFTLVFWFIPFNILHSWAGQVT (in Ref.
FT                                4; BAC38197).
FT   CONFLICT   1068   1068       F -> Y (in Ref. 1; AAD16035).
SQ   SEQUENCE   1157 AA;  129639 MW;  EF03A3C4DC76C449 CRC64;
     MKAGHLLWAL LLMHSLWSIP TDGAIRNYYL GIQDMQWNYA PKGRNVITNQ TLNNDTVASS
     FLKSGKNRIG SSYKKTVYKE YSDGTYTEEI AKPAWLGFLG PLLQAEVGDV ILIHLKNFAS
     RPYTIHPHGV FYEKDSEGSL YPDGSSGYLK ADDSVPPGGS HVYNWSIPES HAPTEADPAC
     LTWIYHSHVD APRDIATGLI GPLITCKRGT LDGNSPPQRK DVDHNFFLLF SVIDENLSWH
     LDDNIATYCS DPASVDKEDG AFQDSNRMHA INGFVFGNLP ELSMCAQKHV AWHLFGMGNE
     IDVHTAFFHG QMLSIRGHHT DVANIFPATF VTAEMVPQKS GTWLISCEVN SHLRSGMQAF
     YKVDSCSMDP PVDQLTGKVR QYFIQAHEIQ WDYGPIGYDG RTGKSLREPG SGPDKYFQKS
     SSRIGGTYWK VRYEAFQDET FQERVHQEEE THLGILGPVI RAEVGDTIQV VFYNRASQPF
     SIQPHGVFYE KNSEGTVYND GTSHPKVAKS FEKVTYYWTV PPHAGPTAQD PACLTWMYFS
     AADPTRDTNS GLVGPLLVCK AGALGADGKQ KGVDKEFFLL FTVFDENESW YNSANQAAGM
     LDSRLLSEDV EGFQDSNRMH AINGFLFSNL PRLDMCKGDT VAWHLLGLGT ETDVHGVMFE
     GNTVQLQGMR KGAVMLFPHT FVTAIMQPDN PGIFEIYCQA GSHREEGMQA IYNVSQCSSH
     QDSPRQHYQA SRVYYIMAEE IEWDYCPDRS WELEWHNTSE KDSYGHVFLS NKDGLLGSKY
     KKAVFREYTD GTFRIPRPRS GPEEHLGILG PLIRGEVGDI LTVVFKNKAS RPYSIHAHGV
     LESNTGGPQA AEPGEVLTYQ WNIPERSGPG PSDSACVSWI YYSAVDPIKD MYSGLVGPLV
     ICRNGILEPN GGRNDMDREF ALLFLIFDEN QSWYLKENIA TYGPQESSHV NLKDATFLES
     NKMHAINGKL YANLRGLTVY QGERVAWYML AMGQDTDIHT VHFHAESFLY QNGQSYRADV
     VDLFPGTFEV VEMVASNPGT WLMHCHVTDH VHAGMETIFT VLSHEEHFST MTTITKEIGK
     AVILRDIGGD NVKMLGMNIP IKDVEILSSA LIAICVLLLL IALALGGVVW YQHRQRKLRR
     NRRSILDDSF KLLSLKQ
//
ID   ADNP_MOUSE              Reviewed;         828 AA.
AC   Q9Z103;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=Activity-dependent neuroprotector homeobox protein;
DE   AltName: Full=Activity-dependent neuroprotective protein;
GN   Name=Adnp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SYNTHESIS OF 74-81.
RC   TISSUE=Brain;
RX   MEDLINE=99155106; PubMed=10037502;
RX   DOI=10.1046/j.1471-4159.1999.0721283.x;
RA   Bassan M., Zamostiano R., Davidson A., Pinhasov A., Giladi E.,
RA   Perl O., Bassan H., Blat C., Gibney G., Glazner G., Brenneman D.E.,
RA   Gozes I.;
RT   "Complete sequence of a novel protein containing a femtomolar-
RT   activity-dependent neuroprotective peptide.";
RL   J. Neurochem. 72:1283-1293(1999).
CC   -!- FUNCTION: Potential transcription factor. May mediate some of the
CC       neuroprotective peptide VIP-associated effects involving normal
CC       growth and cancer proliferation.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- TISSUE SPECIFICITY: Expressed in the brain, with a higher
CC       expression in cerebellum and hippocampus. Weakly expressed in
CC       lung, kidney and intestine, and expressed at intermediate level in
CC       testis.
CC   -!- INDUCTION: By the neuroprotective peptide VIP.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- MISCELLANEOUS: When isolated from the sequence, the
CC       neuroprotective peptide provides neuroprotection at subfemtomolar
CC       concentrations against toxicity associated with tetrodoxin
CC       (electrical blockade), the beta-amyloid peptide (the Alzheimer
CC       disease neurotoxin), N-methyl-aspartate (excitotoxicity), and the
CC       human immunideficiency virus (HIV) envelope protein.
CC   -!- SIMILARITY: Contains 5 C2H2-type zinc fingers.
CC   -!- SIMILARITY: Contains 1 homeobox DNA-binding domain.
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DR   EMBL; AF068198; AAD19843.1; -; mRNA.
DR   IPI; IPI00672180; -.
DR   UniGene; Mm.201322; -.
DR   ProteinModelPortal; Q9Z103; -.
DR   SMR; Q9Z103; 484-530.
DR   STRING; Q9Z103; -.
DR   PhosphoSite; Q9Z103; -.
DR   PRIDE; Q9Z103; -.
DR   Ensembl; ENSMUST00000057793; ENSMUSP00000056809; ENSMUSG00000051149.
DR   Ensembl; ENSMUST00000088001; ENSMUSP00000085316; ENSMUSG00000051149.
DR   Ensembl; ENSMUST00000109196; ENSMUSP00000104819; ENSMUSG00000051149.
DR   MGI; MGI:1338758; Adnp.
DR   GeneTree; ENSGT00530000063631; -.
DR   HOVERGEN; HBG024319; -.
DR   InParanoid; Q9Z103; -.
DR   OrthoDB; EOG4VHK5N; -.
DR   ArrayExpress; Q9Z103; -.
DR   Bgee; Q9Z103; -.
DR   CleanEx; MM_ADNP; -.
DR   Genevestigator; Q9Z103; -.
DR   GermOnline; ENSMUSG00000051149; Mus musculus.
DR   GO; GO:0005615; C:extracellular space; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IC:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0043524; P:negative regulation of neuron apoptosis; IDA:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR001356; Homeobox.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1.
DR   Gene3D; G3DSA:3.30.160.60; Znf_C2H2/integrase_DNA-bd; 1.
DR   Pfam; PF00046; Homeobox; 1.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   SUPFAM; SSF46689; Homeodomain_like; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; DNA-binding; Homeobox; Metal-binding; Nucleus;
KW   Phosphoprotein; Repeat; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    828       Activity-dependent neuroprotector
FT                                homeobox protein.
FT                                /FTId=PRO_0000048808.
FT   ZN_FING     166    188       C2H2-type 1; atypical.
FT   ZN_FING     208    229       C2H2-type 2.
FT   ZN_FING     231    254       C2H2-type 3.
FT   ZN_FING     341    366       C2H2-type 4; atypical.
FT   ZN_FING     381    405       C2H2-type 5; atypical.
FT   DNA_BIND    473    533       Homeobox.
FT   REGION       74     81       Neuroprotective peptide.
FT   COMPBIAS    599    670       Glu-rich.
FT   MOD_RES     128    128       Phosphoserine (By similarity).
FT   MOD_RES     132    132       Phosphoserine (By similarity).
FT   MOD_RES     428    428       Phosphoserine (By similarity).
FT   MOD_RES     595    595       Phosphoserine (By similarity).
FT   MOD_RES     597    597       Phosphoserine (By similarity).
FT   MOD_RES     679    679       Phosphoserine (By similarity).
FT   MOD_RES     681    681       Phosphoserine (By similarity).
FT   MOD_RES     696    696       Phosphoserine (By similarity).
FT   MOD_RES     708    708       Phosphoserine (By similarity).
FT   MOD_RES     761    761       N6-acetyllysine (By similarity).
FT   MOD_RES     768    768       N6-acetyllysine (By similarity).
SQ   SEQUENCE   828 AA;  92063 MW;  9DFE669C506E8606 CRC64;
     MGLPPRISSL ASGNVRSLPS QQMVNRLSIP KPNLNSTGVN MMSNVHLQQN NYGVKSVGQS
     YGVGQSVRLG LGGNAPVSIP QQSQSVKQLL PSGNGRSFGL GAEQRPPAAA RYSLQTANTS
     LPPGQVKSPS VSQSQASRVL GQSSSKPPPA ATGPPPSNHC ATQKWKICTI CNELFPENVY
     SVHFEKEHKA EKVPAVANYI MKIHNFTSKC LYCNRYLPTD TLLNHMLIHG LSCPYCRSTF
     NDVEKMAAHM RMVHIDEEMG PKTDSTLSFD LTLQQGSHTN IHLLVTTYNL RDAPAESVAY
     HAQNNAPVPP KPQPKVQEKA DVPVKSSPQA AVPYKKDVGK TLCPLCFSIL KGPISDALAH
     HLRERHQVIQ TVHPVEKKLT YKCIHCLGVY TSNMTASTIT LHLVHCRGVG KTQNGQDKTN
     APSRLNQSPG LAPVKRTYEQ MEFPLLKKRK LEEDADSPSC FEEKPEEPVV LALDPKGHED
     DSYEARKSFL TKYFNKQPYP TRREIEKLAA SLWLWKSDIA SHFSNKRKKC VRDCEKYKPG
     VLLGFNMKEL NKVKHEMDFD AEWLFENHDE KDSRVNASKT VDKKHNLGKE DDSFSDSFEH
     LEEESNGSGS PFDPVFEVEP KIPSDNLEEP VPKVIPEGAL ESEKLDQKEE EEEEEEEDGS
     KYETIHLTEE PAKLMHDASD SEVDQDDVVE WKDGASPSES GPGSQQISDF EDNTCEMKPG
     TWSDESSQSE DARSSKPAAK KKATVQDDTE QLKWKNSSYG KVEGFWSKDQ SQWENASENA
     ERLPNPQIEW QNSTIDSEDG EQFDSMTDGV ADPMHGSLTG VKLSSQQA
//
ID   SEM4F_MOUSE             Reviewed;         777 AA.
AC   Q9Z123; Q9R1Y1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 87.
DE   RecName: Full=Semaphorin-4F;
DE   AltName: Full=Semaphorin-W;
DE            Short=Sema W;
DE   Flags: Precursor;
GN   Name=Sema4f; Synonyms=Semaw;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC   STRAIN=129/SvJ, and BALB/c; TISSUE=Brain;
RX   MEDLINE=99162633; PubMed=10051670; DOI=10.1073/pnas.96.5.2491;
RA   Encinas J.A., Kikuchi K., Chedotal A., de Castro F., Goodman C.S.,
RA   Kimura T.;
RT   "Cloning, expression, and genetic mapping of Sema W, a member of the
RT   semaphorin family.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:2491-2496(1999).
CC   -!- FUNCTION: Has growth cone collapse activity against retinal
CC       ganglion-cell axons (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the semaphorin family.
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 1 PSI domain.
CC   -!- SIMILARITY: Contains 1 Sema domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB021291; BAA75630.1; -; mRNA.
DR   EMBL; AB022316; BAA75634.1; -; Genomic_DNA.
DR   IPI; IPI00346653; -.
DR   RefSeq; NP_035480.3; NM_011350.3.
DR   UniGene; Mm.270543; -.
DR   ProteinModelPortal; Q9Z123; -.
DR   SMR; Q9Z123; 45-647.
DR   STRING; Q9Z123; -.
DR   PRIDE; Q9Z123; -.
DR   Ensembl; ENSMUST00000000641; ENSMUSP00000000641; ENSMUSG00000000627.
DR   GeneID; 20355; -.
DR   KEGG; mmu:20355; -.
DR   UCSC; uc009cln.1; mouse.
DR   CTD; 20355; -.
DR   MGI; MGI:1340055; Sema4f.
DR   GeneTree; ENSGT00560000076864; -.
DR   HOGENOM; HBG717343; -.
DR   HOVERGEN; HBG093234; -.
DR   InParanoid; Q9Z123; -.
DR   OrthoDB; EOG4J117K; -.
DR   ArrayExpress; Q9Z123; -.
DR   Bgee; Q9Z123; -.
DR   Genevestigator; Q9Z123; -.
DR   GermOnline; ENSMUSG00000000627; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004872; F:receptor activity; IEA:InterPro.
DR   InterPro; IPR003659; Plexin-like.
DR   InterPro; IPR016201; Plexin-like_fold.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR015512; Seamphorin_4F.
DR   InterPro; IPR001627; Semaphorin/CD100_Ag.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   PANTHER; PTHR11036:SF13; Sema4F; 1.
DR   Pfam; PF01437; PSI; 1.
DR   Pfam; PF01403; Sema; 1.
DR   SMART; SM00423; PSI; 1.
DR   SMART; SM00630; Sema; 1.
DR   SUPFAM; SSF103575; Plexin-like_fold; 1.
DR   SUPFAM; SSF101912; Sema; 1.
DR   PROSITE; PS51004; SEMA; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Neurogenesis; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     40       Potential.
FT   CHAIN        41    777       Semaphorin-4F.
FT                                /FTId=PRO_0000032331.
FT   TOPO_DOM     41    667       Extracellular (Potential).
FT   TRANSMEM    668    688       Helical; (Potential).
FT   TOPO_DOM    689    777       Cytoplasmic (Potential).
FT   DOMAIN       48    516       Sema.
FT   DOMAIN      518    569       PSI.
FT   DOMAIN      586    641       Ig-like C2-type.
FT   CARBOHYD     70     70       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    139    139       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    515    515       N-linked (GlcNAc...) (Potential).
FT   DISULFID    118    128       By similarity.
FT   DISULFID    146    155       By similarity.
FT   DISULFID    279    390       By similarity.
FT   DISULFID    303    349       By similarity.
FT   DISULFID    593    634       By similarity.
FT   VARIANT     490    490       P -> T (in strain: 129/SvJ).
FT   VARIANT     659    659       S -> A (in strain: 129/SvJ).
SQ   SEQUENCE   777 AA;  84502 MW;  B63F853355856924 CRC64;
     MLARAERPRP GPRPPPVSLF PPPSSLLLLL LAMLSAPVCG RVPRSVPRTS LPISEADSYL
     TRFAAPHTYN YSALLVDPAS HTLYVGARDS IFALTLPFSG EKPRRIDWMV PETHRQNCRK
     KGKKEDECHN FIQILAIANA SHLLTCGTFA FDPKCGVIDV SSFQQVERLE SGRGKCPFEP
     AQRSAAVMAG GVLYTATVKN FLGTEPIISR AVGRAEDWIR TETLSSWLNA PAFVAAMVLS
     PAEWGDEDGD DEIFFFFTET SRVLDSYERI KVPRVARVCA GDLGGRKTLQ QRWTTFLKAD
     LLCPGPEHGR ASGVLQDMTE LRPQPGAGTP LFYGIFSSQW EGAAISAVCA FRPQDIRAVL
     NGPFRELKHD CNRGLPVMDN EVPQPRPGEC ITNNMKFQQF GSSLSLPDRV LTFIRDHPLM
     DRPVFPADGR PLLVTTDTAY LRVVAHRVTS LSGKEYDVLY LGTEDGHLHR AVRIGAQLSV
     LEDLALFPEP QPVESMKLYH DWLLVGSHTE VTQVNTSNCG RLQSCSECIL AQDPVCAWSF
     RLDACVAHAG EHRGMVQDIE SADVSSLCPK EPGEHPVVFE VPVATVGHVV LPCSPSSAWA
     SCVWHQPSGV TSLTPRRDGL EVVVTPGAMG AYACECQEGG AARVVAAYSL VWGSQRGPSN
     RAHTVVGAGL VGFFLGVLAA SLTLLLIGRR QQRRRQRELL ARDKVGLDLG APPSGTTSYS
     QDPPSPSPED ERLPLALGKR GSGFGGFPPP FLLDSCPSPA HIRLTGAPLA TCDETSI
//
ID   HNRDL_MOUSE             Reviewed;         301 AA.
AC   Q9Z130; Q9CT01;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Heterogeneous nuclear ribonucleoprotein D-like;
DE            Short=hnRNP D-like;
DE            Short=hnRNP DL;
DE   AltName: Full=JKT41-binding protein;
GN   Name=Hnrpdl; Synonyms=Jktbp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Testis;
RX   MEDLINE=20183688; PubMed=10717477; DOI=10.1016/S0378-1119(00)00032-9;
RA   Akagi T., Kamei D., Tsuchiya N., Nishina Y., Horiguchi H., Matsui M.,
RA   Kamma H., Yamada M.;
RT   "Molecular characterization of a mouse heterogeneous nuclear
RT   ribonucleoprotein D-like protein JKTBP and its tissue-specific
RT   expression.";
RL   Gene 245:267-273(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 1-13, FUNCTION, INTERACTION WITH ZNF148,
RP   SUBCELLULAR LOCATION, AND DNA-BINDING.
RC   TISSUE=Myotube;
RX   PubMed=15190078; DOI=10.1074/jbc.M403160200;
RA   Boopathi E., Lenka N., Prabu S.K., Fang J.-K., Wilkinson F.,
RA   Atchison M., Giallongo A., Avadhani N.G.;
RT   "Regulation of murine cytochrome c oxidase Vb gene expression during
RT   myogenesis: YY-1 and heterogeneous nuclear ribonucleoprotein D-like
RT   protein (JKTBP1) reciprocally regulate transcription activity by
RT   physical interaction with the BERF-1/ZBP-89 factor.";
RL   J. Biol. Chem. 279:35242-35254(2004).
CC   -!- FUNCTION: Acts as a transcriptional regulator. Promotes
CC       transcription repression (By similarity). Promotes transcription
CC       activation in differentiated myotubes. Binds to double- and
CC       single-stranded DNA sequences (By similarity). Binds to the
CC       transcription suppressor CATR sequence of the COX5B promoter.
CC       Binds with high affinity to RNA molecules that contain AU-rich
CC       elements (AREs) found within the 3'-UTR of many proto-oncogenes
CC       and cytokine mRNAs (By similarity). Binds both to nuclear and
CC       cytoplasmic poly(A) mRNAs (By similarity). Binds to poly(G) and
CC       poly(A), but not to poly(U) or poly(C) RNA homopolymers (By
CC       similarity). Binds to the 5'-ACUAGC-3' RNA consensus sequence (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with TNPO1 (By similarity). Interacts with
CC       ZNF148.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Shuttles between
CC       the nucleus and the cytoplasm in a TNPO1-dependent manner (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, myoblast,
CC       myotube, heart, brain, liver, kidney, heart, lung, stomach, small
CC       intestine, large intestine, spleen, and testis (at protein level).
CC       Expressed in brain, skeletal muscle, heart, lung, liver, stomach,
CC       small intestine, large intestine, kidney, spleen and testis.
CC   -!- PTM: Dimethylation of Arg-289 is probably of the asymmetric type
CC       (By similarity).
CC   -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB017020; BAA75479.1; -; mRNA.
DR   EMBL; AK011581; BAB27715.1; -; mRNA.
DR   EMBL; AK172629; BAE43104.1; -; mRNA.
DR   EMBL; BC021374; AAH21374.1; -; mRNA.
DR   IPI; IPI00129417; -.
DR   UniGene; Mm.389579; -.
DR   UniGene; Mm.426680; -.
DR   HSSP; Q14103; 1HD1.
DR   ProteinModelPortal; Q9Z130; -.
DR   SMR; Q9Z130; 26-193.
DR   STRING; Q9Z130; -.
DR   PhosphoSite; Q9Z130; -.
DR   PRIDE; Q9Z130; -.
DR   Ensembl; ENSMUST00000031271; ENSMUSP00000031271; ENSMUSG00000029328.
DR   Ensembl; ENSMUST00000086900; ENSMUSP00000084114; ENSMUSG00000029328.
DR   MGI; MGI:1355299; Hnrpdl.
DR   eggNOG; roNOG10185; -.
DR   GeneTree; ENSGT00560000076532; -.
DR   HOGENOM; HBG756718; -.
DR   HOVERGEN; HBG002295; -.
DR   InParanoid; Q9Z130; -.
DR   PhylomeDB; Q9Z130; -.
DR   ArrayExpress; Q9Z130; -.
DR   Bgee; Q9Z130; -.
DR   CleanEx; MM_HNRPDL; -.
DR   Genevestigator; Q9Z130; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Cytoplasm; Direct protein sequencing;
KW   DNA-binding; Methylation; Nucleus; Phosphoprotein; Repeat; Repressor;
KW   RNA-binding; Transcription; Transcription regulation.
FT   CHAIN         1    301       Heterogeneous nuclear ribonucleoprotein
FT                                D-like.
FT                                /FTId=PRO_0000287240.
FT   DOMAIN       29    111       RRM 1.
FT   DOMAIN      114    193       RRM 2.
FT   REGION      223    301       Necessary for interaction with TNPO1 (By
FT                                similarity).
FT   COMPBIAS    197    202       Poly-Gln.
FT   COMPBIAS    204    292       Gly-rich.
FT   COMPBIAS    234    277       Tyr-rich.
FT   MOD_RES      42     42       N6-methyllysine (By similarity).
FT   MOD_RES      97     97       N6-acetyllysine (By similarity).
FT   MOD_RES     122    122       Phosphoserine (By similarity).
FT   MOD_RES     289    289       Omega-N-methylated arginine (By
FT                                similarity).
SQ   SEQUENCE   301 AA;  33559 MW;  8AB2787FEB73311C CRC64;
     MEDMNEYSNI EEFAEGSKIN ASKNQQDDGK MFIGGLSWDT SKKDLTEYLS RFGEVVDCTI
     KTDPVTGRSR GFGFVLFKDA ASVDKVLELK EHKLDGKLID PKRAKALKGK EPPKKVFVGG
     LSPDTSEEQI KEYFGAFGEI ENIELPMDTK TNERRGFCFI TYTDEEPVKK LLESRYHQIG
     SGKCEIKVAQ PKEVYRQQQQ QQKGGRGAAA GGRGGARGRG RGQGQNWNQG FNNYYDQGYG
     NYNSAYGGDQ NYSGYGGYDY TGYNYGNYGY GQGYADYSGQ QSTYGKASRG GGNHQNNYQP
     Y
//
ID   CPNE6_MOUSE             Reviewed;         557 AA.
AC   Q9Z140;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 73.
DE   RecName: Full=Copine-6;
DE   AltName: Full=Copine VI;
DE   AltName: Full=Neuronal-copine;
DE            Short=N-copine;
GN   Name=Cpne6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=98307387; PubMed=9645480; DOI=10.1016/S0014-5793(98)00497-9;
RA   Nakayama T., Yaoi T., Yasui M., Kuwajima G.;
RT   "N-copine: a novel two C2-domain-containing protein with neuronal
RT   activity-regulated expression.";
RL   FEBS Lett. 428:80-84(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: May function in membrane trafficking. Exhibits calcium-
CC       dependent phospholipid binding properties (By similarity). May
CC       have a role in synaptic plasticity.
CC   -!- SIMILARITY: Belongs to the copine family.
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -!- SIMILARITY: Contains 1 VWFA domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB008893; BAA75898.1; -; mRNA.
DR   EMBL; BC050766; AAH50766.1; -; mRNA.
DR   IPI; IPI00129451; -.
DR   RefSeq; NP_001129529.1; NM_001136057.2.
DR   RefSeq; NP_034077.1; NM_009947.3.
DR   UniGene; Mm.477983; -.
DR   ProteinModelPortal; Q9Z140; -.
DR   SMR; Q9Z140; 16-131, 136-285.
DR   PhosphoSite; Q9Z140; -.
DR   PRIDE; Q9Z140; -.
DR   Ensembl; ENSMUST00000074225; ENSMUSP00000073847; ENSMUSG00000022212.
DR   GeneID; 12891; -.
DR   KEGG; mmu:12891; -.
DR   UCSC; uc007tyr.1; mouse.
DR   CTD; 12891; -.
DR   MGI; MGI:1334445; Cpne6.
DR   GeneTree; ENSGT00550000074189; -.
DR   HOGENOM; HBG464786; -.
DR   HOVERGEN; HBG066841; -.
DR   InParanoid; Q9Z140; -.
DR   OrthoDB; EOG4M3986; -.
DR   NextBio; 282494; -.
DR   ArrayExpress; Q9Z140; -.
DR   Bgee; Q9Z140; -.
DR   CleanEx; MM_CPNE6; -.
DR   Genevestigator; Q9Z140; -.
DR   GermOnline; ENSMUSG00000022212; Mus musculus.
DR   GO; GO:0030424; C:axon; IDA:MGI.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0001786; F:phosphatidylserine binding; IDA:MGI.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR010734; Copine.
DR   InterPro; IPR002035; VWF_A.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF07002; Copine; 1.
DR   SMART; SM00239; C2; 2.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Repeat.
FT   CHAIN         1    557       Copine-6.
FT                                /FTId=PRO_0000144846.
FT   DOMAIN       24    111       C2 1.
FT   DOMAIN      138    243       C2 2.
FT   DOMAIN      306    526       VWFA.
FT   MOD_RES      65     65       Phosphoserine.
SQ   SEQUENCE   557 AA;  61781 MW;  043D6C1487E2ECAC CRC64;
     MSDPEMGWVP EPPAMTLGAS RVELRVSCHG LLDRDTLTKP HPCVLLKLYS DEQWVEVERT
     EVLRSCSSPV FSRVLAIEYF FEEKQPLQFH VFDAEDGATS PSSDTFLGST ECTLGQIVSQ
     TKVTKPLLLK NGKTAGKSTI TIVAEEVSGT NDYVQLTFRA HKLDNKDLFS KSDPFMEIYK
     TNGDQSDQLV WRTEVVKNNL NPSWEPFRLS LHSLCSCDIH RPLKFLVYDY DSSGKHDFIG
     EFTSTFQEMQ EGTANPGQEM QWDCINPKYR DKKKNYKSSG TVVLAQCTVE KVHTFLDYIM
     GGCQISFTVA IDFTASNGDP RSSQSLHCLS PRQPNHYLQA LRTVGGICQD YDSDKRFPAF
     GFGARIPPNF EVSHDFAINF DPENPECEEI SGVIASYRRC LPQIQLYGPT NVAPIINRVA
     EPAQREQSTG QATKYSVLLV LTDGVVSDMA ETRTAIVRAS RLPMSIIIVG VGNADFSDMR
     LLDGDDGPLR CPKGVPAARD IVQFVPFRDF KDAAPSALAK CVLAEVPRQV VEYYASQGIS
     PGAPRPSTPA MTPSPSP
//
ID   TBCD8_MOUSE             Reviewed;        1134 AA.
AC   Q9Z1A9; Q3TRZ8; Q3URH3; Q3UU99; Q6P1G8;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   03-NOV-2009, sequence version 2.
DT   08-MAR-2011, entry version 59.
DE   RecName: Full=TBC1 domain family member 8;
DE   AltName: Full=BUB2-like protein 1;
DE   AltName: Full=Vascular Rab-GAP/TBC-containing protein;
GN   Name=Tbc1d8; Synonyms=Hblp1, Vrp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Epididymis, Hippocampus, and Spinal cord;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Fetal brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 201-1134.
RC   TISSUE=Hematopoietic;
RA   Guimaraes M.J., Bazan J.F.;
RT   "The CHESS protein domain: a novel structural unit that is common
RT   among networks involved in cell signaling, chromatin metabolism and
RT   cell division.";
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May act as a GTPase-activating protein for Rab family
CC       protein(s).
CC   -!- SIMILARITY: Contains 2 GRAM domains.
CC   -!- SIMILARITY: Contains 1 Rab-GAP TBC domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD00658.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC       Sequence=AAH05421.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; AK138630; BAE23728.1; -; mRNA.
DR   EMBL; AK141520; BAE24715.1; -; mRNA.
DR   EMBL; AK162371; BAE36878.1; -; mRNA.
DR   EMBL; CH466536; EDL14558.1; -; Genomic_DNA.
DR   EMBL; BC065081; AAH65081.1; -; mRNA.
DR   EMBL; BC005421; AAH05421.2; ALT_INIT; mRNA.
DR   EMBL; U88873; AAD00658.1; ALT_INIT; mRNA.
DR   IPI; IPI00130023; -.
DR   RefSeq; NP_061245.3; NM_018775.4.
DR   UniGene; Mm.387293; -.
DR   ProteinModelPortal; Q9Z1A9; -.
DR   SMR; Q9Z1A9; 477-787.
DR   STRING; Q9Z1A9; -.
DR   PRIDE; Q9Z1A9; -.
DR   Ensembl; ENSMUST00000054462; ENSMUSP00000049967; ENSMUSG00000003134.
DR   GeneID; 54610; -.
DR   KEGG; mmu:54610; -.
DR   CTD; 54610; -.
DR   MGI; MGI:1927225; Tbc1d8.
DR   GeneTree; ENSGT00580000081243; -.
DR   HOVERGEN; HBG054142; -.
DR   InParanoid; Q9Z1A9; -.
DR   OMA; SCCCWKG; -.
DR   OrthoDB; EOG4S7JP7; -.
DR   ArrayExpress; Q9Z1A9; -.
DR   Bgee; Q9Z1A9; -.
DR   CleanEx; MM_TBC1D8; -.
DR   Genevestigator; Q9Z1A9; -.
DR   GermOnline; ENSMUSG00000003134; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005097; F:Rab GTPase activator activity; IEA:InterPro.
DR   GO; GO:0032313; P:regulation of Rab GTPase activity; IEA:InterPro.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR004182; GRAM.
DR   InterPro; IPR000195; RabGAP/TBC_dom.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   Pfam; PF02893; GRAM; 2.
DR   Pfam; PF00566; TBC; 1.
DR   SMART; SM00568; GRAM; 2.
DR   SMART; SM00164; TBC; 1.
DR   SUPFAM; SSF47923; RabGAP_TBC; 2.
DR   PROSITE; PS50086; TBC_RABGAP; 1.
PE   2: Evidence at transcript level;
KW   GTPase activation; Repeat.
FT   CHAIN         1   1134       TBC1 domain family member 8.
FT                                /FTId=PRO_0000208034.
FT   DOMAIN      145    212       GRAM 1.
FT   DOMAIN      285    353       GRAM 2.
FT   DOMAIN      504    691       Rab-GAP TBC.
FT   CONFLICT    349    349       I -> F (in Ref. 1; BAE36878).
FT   CONFLICT    705    705       A -> D (in Ref. 1; BAE24715).
FT   CONFLICT    824    824       K -> N (in Ref. 1; BAE36878).
SQ   SEQUENCE   1134 AA;  130057 MW;  1F946A2523488158 CRC64;
     MWLKPEEVLL KNALKLWVTQ KSSCYFVLQR RRGHGEGGGR LTGRLVGALD AVLDSSARVA
     PFRILLQVPG SQVYSPIACG ATLEEINRHW DWLEQNLLHT LSVFDNKDDI ASFVKGKVKA
     LIAEETSSRL AEQEEEPEKF REALVKFEAR FNFPEAEKLV TYYSCCCWKG RVPRQGWLYL
     SINHLCFYSF FLGKELKLVI PWVDIQKLER TSNVFLTDTI RITTQNKERD FSTFLNLDEV
     FKIMEQLADV TLRRLLDNEV FDLDPDLQEP SQITKRDLEA RAQNEFFRAF FRLPREEKLH
     AVADCSLWTP FSRCHTAGRI FSSDSYICFA SREDGCCNVV LPLREVVSIE KMEDTSLLPN
     PIIVSIRSKM AFQFIELKDR ENLVEGLLLR LKQVHANHPV HYETSPSDDD MASPVFYSAS
     ICTDKFGDLE MVASQSSEER EEKRPLPHPE PLTAVFQQSG SQSPDSRLSR EQIKISLWND
     HFVEYGRTVC MFRTEKIRKL VAMGIPESLR GRLWLLFSDA VTDLASHPGY YGNLVEQSLG
     RCCLVTEEIE RDLHRSLPEH PAFQNETGIA ALRRVLTAYA HRNPKIGYCQ SMNILTSVLL
     LYAKEEEAFW LLVAVCERML PDYFNHRVIG AQVDQSVFEE LIKEQLPELA EHMSDLSALA
     SISLSWFLTL FLSIMPLESA VHVVDCFFYD GIKAIFQLGL AVLEANAEEL CSSKDDGQAL
     MVLSRFLDHI KNEDSPGPPI GSHHAFFSDD QEPYPVTDIA DLIRDSYEKF GNQSVEQIEH
     LRCKHRIRVL QGHEDTTKQN VLRVVIPEVS ILPEDLEELY DLFKRAHMMS CYWEHHRPMA
     LRHDPSRPYA EQYRIDARQF AHLFQLVSPW TCGVHTEILA ERLFRLLDDN MDQLIEFKAF
     TSCLDIMYNG EMNEKIKLLY RLHIPPALTE NDRDSQSPLK NPLLSTSRPL VLGKPNGDTI
     DYQKQLKQMI KDLAKEKDKM EKELPKMSQR EFIQFCKTLY SMFHEDPEEN DLYQAIATVT
     TLLLQIGEVG QRGSSSGSCS QECEEPQASA PPEQDSVFAE AGKSPQAFPE TEGDWTVSLE
     HILASLLTEQ SLVNFFEKPL NIKSKLENAK LNQYSLKVLE MSHPPQAELK LNDL
//
ID   PLCB1_MOUSE             Reviewed;        1216 AA.
AC   Q9Z1B3; Q62075; Q8K5A5; Q8K5A6; Q9Z0E5; Q9Z2T5;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1;
DE            EC=3.1.4.11;
DE   AltName: Full=PLC-154;
DE   AltName: Full=Phosphoinositide phospholipase C-beta-1;
DE   AltName: Full=Phospholipase C-beta-1;
DE            Short=PLC-beta-1;
GN   Name=Plcb1; Synonyms=Plcb;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RC   STRAIN=Swiss;
RA   Bai J., Wu K., Marks D.L., Machamer C., Pagano R.E.;
RT   "Cloning of PI-specific phospholipase C's from 3T3 cells. Expression
RT   and membrane targeting of a novel phospholipase C-beta-1 isoform.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C).
RC   STRAIN=ILS, and ISS;
RX   MEDLINE=21363810; PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA   Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA   Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT   "High-throughput sequence identification of gene coding variants
RT   within alcohol-related QTLs.";
RL   Mamm. Genome 12:657-663(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 29-145.
RC   STRAIN=C57BL/6;
RX   MEDLINE=98424011; PubMed=9753089;
RX   DOI=10.1046/j.1460-9568.1998.00213.x;
RA   Watanabe M., Nakamura M., Sato K., Kano M., Simon M.I., Inoue Y.;
RT   "Patterns of expression for the mRNA corresponding to the four
RT   isoforms of phospholipase Cbeta in mouse brain.";
RL   Eur. J. Neurosci. 10:2016-2025(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 428-615.
RC   TISSUE=Oocyte;
RX   MEDLINE=96257754; PubMed=8687404;
RA   Dupont G., McGuinness O.M., Johnson M.H., Berridge M.J., Borgese F.;
RT   "Phospholipase C in mouse oocytes: characterization of beta and gamma
RT   isoforms and their possible involvement in sperm-induced Ca2+
RT   spiking.";
RL   Biochem. J. 316:583-591(1996).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333; TYR-334 AND
RP   THR-336, AND MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1197, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: The production of the second messenger molecules
CC       diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is
CC       mediated by activated phosphatidylinositol-specific phospholipase
CC       C enzymes (By similarity).
CC   -!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 4,5-
CC       bisphosphate + H(2)O = 1D-myo-inositol 1,4,5-trisphosphate +
CC       diacylglycerol.
CC   -!- COFACTOR: Calcium (By similarity).
CC   -!- SUBUNIT: Interacts with DGKQ (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=A; Synonyms=C-beta-1a;
CC         IsoId=Q9Z1B3-1; Sequence=Displayed;
CC       Name=B; Synonyms=C-beta-1b;
CC         IsoId=Q9Z1B3-2; Sequence=VSP_008917;
CC       Name=C;
CC         IsoId=Q9Z1B3-3; Sequence=VSP_008918;
CC         Note=No experimental confirmation available;
CC   -!- MISCELLANEOUS: The receptor-mediated activation of PLC-beta-1 is
CC       mediated by two G-protein alpha subunits, alpha-Q and alpha-11.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 PI-PLC X-box domain.
CC   -!- SIMILARITY: Contains 1 PI-PLC Y-box domain.
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DR   EMBL; U85712; AAD00571.1; -; mRNA.
DR   EMBL; U85713; AAD00572.1; -; mRNA.
DR   EMBL; U85714; AAD00573.1; -; mRNA.
DR   EMBL; AF498249; AAM22966.1; -; mRNA.
DR   EMBL; AF498250; AAM22967.1; -; mRNA.
DR   EMBL; AF022801; AAD01749.1; -; mRNA.
DR   EMBL; X95344; CAA64637.1; -; mRNA.
DR   IPI; IPI00130045; -.
DR   IPI; IPI00323250; -.
DR   IPI; IPI00468121; -.
DR   PIR; S68256; S68256.
DR   UniGene; Mm.330607; -.
DR   ProteinModelPortal; Q9Z1B3; -.
DR   SMR; Q9Z1B3; 12-833.
DR   STRING; Q9Z1B3; -.
DR   PhosphoSite; Q9Z1B3; -.
DR   PRIDE; Q9Z1B3; -.
DR   Ensembl; ENSMUST00000110116; ENSMUSP00000105743; ENSMUSG00000051177.
DR   UCSC; uc008mnz.1; mouse.
DR   MGI; MGI:97613; Plcb1.
DR   GeneTree; ENSGT00600000084213; -.
DR   HOGENOM; HBG315986; -.
DR   HOVERGEN; HBG053609; -.
DR   InParanoid; Q9Z1B3; -.
DR   OrthoDB; EOG40S0DW; -.
DR   PhylomeDB; Q9Z1B3; -.
DR   BRENDA; 3.1.4.11; 244.
DR   NextBio; 295080; -.
DR   ArrayExpress; Q9Z1B3; -.
DR   Bgee; Q9Z1B3; -.
DR   CleanEx; MM_PLCB1; -.
DR   Genevestigator; Q9Z1B3; -.
DR   GermOnline; ENSMUSG00000051177; Mus musculus.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; IEA:EC.
DR   GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR015359; Phospholipase_C_EF-hand-like.
DR   InterPro; IPR001711; Phospholipase_C_Pinositol-sp_Y.
DR   InterPro; IPR001192; Pinositol_Phospholipase-C.
DR   InterPro; IPR016280; PLC-beta.
DR   InterPro; IPR014815; PLC-beta_C.
DR   InterPro; IPR009535; PLC-beta_CS.
DR   InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR   InterPro; IPR000909; PLipase_C_PInositol-sp_X_dom.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 1.
DR   Gene3D; G3DSA:3.20.20.190; PLC-like_Pdiesterase_TIM-brl; 2.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF06631; DUF1154; 1.
DR   Pfam; PF09279; efhand_like; 1.
DR   Pfam; PF00388; PI-PLC-X; 1.
DR   Pfam; PF00387; PI-PLC-Y; 1.
DR   Pfam; PF08703; PLC-beta_C; 1.
DR   PIRSF; PIRSF000956; PLC-beta; 1.
DR   PRINTS; PR00390; PHPHLIPASEC.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00148; PLCXc; 1.
DR   SMART; SM00149; PLCYc; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF51695; PLC-like_Pdiesterase_TIM-brl; 1.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR   PROSITE; PS50008; PIPLC_Y_DOMAIN; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Calcium; Hydrolase;
KW   Lipid degradation; Phosphoprotein; Transducer.
FT   CHAIN         1   1216       1-phosphatidylinositol-4,5-bisphosphate
FT                                phosphodiesterase beta-1.
FT                                /FTId=PRO_0000088487.
FT   DOMAIN      316    467       PI-PLC X-box.
FT   DOMAIN      540    656       PI-PLC Y-box.
FT   DOMAIN      663    761       C2.
FT   COMPBIAS    914   1088       Lys-rich.
FT   ACT_SITE    331    331       By similarity.
FT   ACT_SITE    378    378       By similarity.
FT   MOD_RES     333    333       Phosphothreonine.
FT   MOD_RES     334    334       Phosphotyrosine.
FT   MOD_RES     336    336       Phosphothreonine.
FT   MOD_RES     569    569       Phosphoserine (By similarity).
FT   MOD_RES     573    573       Phosphothreonine (By similarity).
FT   MOD_RES     887    887       Phosphoserine; by PKC (By similarity).
FT   MOD_RES     972    972       N6-acetyllysine (By similarity).
FT   MOD_RES     976    976       N6-acetyllysine (By similarity).
FT   MOD_RES    1197   1197       Phosphoserine.
FT   VAR_SEQ    1142   1216       LQTELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSA
FT                                PPSLASDAAKVNLKSPSSEEIERENPGREFDTPL -> GEG
FT                                PSSVLSEGCHEDPSVPPNFTPPNPQALKW (in isoform
FT                                B).
FT                                /FTId=VSP_008917.
FT   VAR_SEQ    1199   1216       Missing (in isoform C).
FT                                /FTId=VSP_008918.
FT   VARIANT      28     28       L -> F (in strain: ILS and ISS).
FT   VARIANT      41     41       T -> I (in strain: C57BL/6, ILS and ISS).
FT   VARIANT      67     67       S -> T (in strain: C57BL/6).
FT   VARIANT      79     79       E -> K (in strain: C57BL/6, ILS and ISS).
FT   VARIANT     112    112       A -> V (in strain: C57BL/6, ILS and ISS).
FT   VARIANT     622    622       M -> V (in strain: ILS and ISS).
FT   VARIANT     714    714       T -> K (in strain: ILS and ISS).
FT   VARIANT     795    795       D -> V (in strain: ILS and ISS).
FT   VARIANT     923    923       H -> Q (in strain: ILS and ISS).
FT   VARIANT     957    957       I -> N (in strain: ILS and ISS).
FT   VARIANT    1084   1084       T -> K (in strain: ILS and ISS).
FT   VARIANT    1197   1197       S -> G (in strain: ILS).
FT   VARIANT    1197   1197       S -> W (in strain: ISS).
FT   VARIANT    1198   1198       P -> S (in strain: ILS and ISS).
FT   CONFLICT    561    561       R -> I (in Ref. 4; CAA64637).
FT   CONFLICT    613    613       L -> I (in Ref. 4).
SQ   SEQUENCE   1216 AA;  138325 MW;  D873078A58CE824D CRC64;
     MAGAQPGVHA LQLKPVCVSD SLKKGTKLVK WDDDSTIVTP TILRTDPQGF FFYWTDQNKE
     TELLDLSLVK DARCGKHAEA PKDPKLRELL DVGNIGHLEQ RMITVVYGPD LANISHLNLV
     AFQEEVAKEW TNEVFSLATN LLAQNMSRDA FLEKAYTKLK LQVTPEGRIP LKNIYRLFSA
     DRKRVETALE ACSLPSSRND SIPQEDFTPD VYRVFLNNLC PRPEIDNIFS EFGAKSKPYL
     TVDQMMDFIN LKQRDPRLNE ILYPPLKQEQ VQVLIEKYEP NSSLAKKGQM SVDGFMRYLS
     GEENGVVSPE KLDLNEDMSQ PLSHYFINSS HNTYLTAGQL AGNSSVEMYR QVLLSGCRCV
     ELDCWKGRTA EEEPVITHGF TMTTEISFKE VIEAIAECAF KTSPFPILLS FENHVDSPKQ
     QAKMAEYCRL IFGDALLMEP LEKYPLESGV PLPSPMDLMY KILVKNKKKS HKSSEGSGKK
     KLSEQASNTY SDSSSVFEPS SPGAGEADTE SDDDDDDDDC KKSSMDEGTA GSEAMATEEM
     SNLVNYIQPV KFESFEISKK RNKSFEMSSF VETKGLEQLT KSPVEFVEYN KMQLSRIYPK
     GTRVDSSNYM PQLFWNAGCQ MMALNFQTVD LAMQINMGMY EYNGKSGYRL KPEFMRRPDK
     HFDPFTEGIV DGIVANTLSV KIISGQFLSD KKVGTYVEVD MFGLPVDTRR KAFTTKTSQG
     NAVNPVWEEE PIVFKKVVLP SLACLRIAAY EEGGKFIGHR ILPVQAIRPG YHYICLRNER
     NQPLTLPAVF VYIEDKDYVP DTYADVIEAL SNPIRYVNLM EQRAKQLAAL TLEDEEEVKK
     EADPGETSSE APSETRTTPA ENGVNHTASL APKPPSQAPH SQPAPGSVKA PAKTEDLIQS
     VLTEVEAQTI EELKQQKSFV KLHKKHYKEM KDLVKRHHKK TTELIKEHTT KYNEIQIDYL
     RRRAALEKSA KKDSKKKSEP SSPDHGSSAI EQDLAALDAE MTQKLIDLKD KQQQQLLNLR
     QEQYYSEKYQ KREHIKLLIQ KLTDVAEECQ NNQLKKLKEI CEKEKKELKK KMDKKRQEKI
     TEATSKDKSQ MEEEKTEMIR SYIQEVVQYI KRLEEAQSKR QEKLVEKHNE IRQQILDEKP
     KLQTELEQEY QDKFKRLPLE ILEFVQEAMK GKISEDSNHG SAPPSLASDA AKVNLKSPSS
     EEIERENPGR EFDTPL
//
ID   EIF3G_MOUSE             Reviewed;         320 AA.
AC   Q9Z1D1; Q9R079;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2002, sequence version 2.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=Eukaryotic translation initiation factor 3 subunit G;
DE            Short=eIF3g;
DE   AltName: Full=Eukaryotic translation initiation factor 3 RNA-binding subunit;
DE            Short=eIF-3 RNA-binding subunit;
DE   AltName: Full=Eukaryotic translation initiation factor 3 subunit 4;
DE   AltName: Full=eIF-3-delta;
DE   AltName: Full=eIF3 p42;
DE   AltName: Full=eIF3 p44;
GN   Name=Eif3g; Synonyms=Eif3p42, Eif3s4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Asano K., Hershey J.W.B., Hinnebusch A.G.;
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CD-1;
RA   Valentijn L.J., Hoff E.I., Baas F.;
RT   "5'-AMP-activated protein kinase subunit beta interacts with the p42
RT   subunit of translation initiation factor eIF3.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-41, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [5]
RP   CHARACTERIZATION OF THE EIF-3 COMPLEX, IDENTIFICATION IN THE EIF-3
RP   COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17581632; DOI=10.1038/sj.emboj.7601765;
RA   Masutani M., Sonenberg N., Yokoyama S., Imataka H.;
RT   "Reconstitution reveals the functional core of mammalian eIF3.";
RL   EMBO J. 26:3373-3383(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Component of the eukaryotic translation initiation
CC       factor 3 (eIF-3) complex, which is required for several steps in
CC       the initiation of protein synthesis. The eIF-3 complex associates
CC       with the 40S ribosome and facilitates the recruitment of eIF-1,
CC       eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S
CC       preinitiation complex (43S PIC). The eIF-3 complex stimulates mRNA
CC       recruitment to the 43S PIC and scanning of the mRNA for AUG
CC       recognition. The eIF-3 complex is also required for disassembly
CC       and recycling of posttermination ribosomal complexes and
CC       subsequently prevents premature joining of the 40S and 60S
CC       ribosomal subunits prior to initiation. This subunit can bind 18S
CC       rRNA.
CC   -!- SUBUNIT: Component of the eukaryotic translation initiation factor
CC       3 (eIF-3) complex, which is composed of 13 subunits: EIF3A, EIF3B,
CC       EIF3C, EIF3D, EIF3E, EIF3F, EIF3G, EIF3H, EIF3I, EIF3J, EIF3K,
CC       EIF3L and EIF3M. The eIF-3 complex appears to include 3 stable
CC       modules: module A is composed of EIF3A, EIF3B, EIF3G and EIF3I;
CC       module B is composed of EIF3F, EIF3H, and EIF3M; and module C is
CC       composed of EIF3C, EIF3D, EIF3E, EIF3K and EIF3L. EIF3C of module
CC       C binds EIF3B of module A and EIF3H of module B, thereby linking
CC       the three modules. EIF3J is a labile subunit that binds to the
CC       eIF-3 complex via EIF3B. The eIF-3 complex may interact with
CC       RPS6KB1 under conditions of nutrient depletion. Mitogenic
CC       stimulation may lead to binding and activation of a complex
CC       composed of MTOR and RPTOR, leading to phosphorylation and release
CC       of RPS6KB1 and binding of EIF4B to eIF-3. Interacts (via C-
CC       terminus) with AIFM1 (via N-terminus) (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). Nucleus (By
CC       similarity). Cytoplasm, perinuclear region (By similarity).
CC       Note=Colocalizes with AIFM1 in the nucleus and perinuclear region
CC       (By similarity).
CC   -!- PTM: Phosphorylated. Phosphorylation is enhanced upon serum
CC       stimulation (By similarity).
CC   -!- SIMILARITY: Belongs to the eIF-3 subunit G family.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR   EMBL; U70733; AAD00176.1; -; mRNA.
DR   EMBL; AF108214; AAF14221.1; -; mRNA.
DR   EMBL; BC008511; AAH08511.1; -; mRNA.
DR   IPI; IPI00622371; -.
DR   RefSeq; NP_058572.2; NM_016876.3.
DR   UniGene; Mm.427309; -.
DR   ProteinModelPortal; Q9Z1D1; -.
DR   SMR; Q9Z1D1; 228-320.
DR   IntAct; Q9Z1D1; 2.
DR   MINT; MINT-1572167; -.
DR   STRING; Q9Z1D1; -.
DR   PhosphoSite; Q9Z1D1; -.
DR   REPRODUCTION-2DPAGE; Q9Z1D1; -.
DR   PRIDE; Q9Z1D1; -.
DR   Ensembl; ENSMUST00000004206; ENSMUSP00000004206; ENSMUSG00000070319.
DR   GeneID; 53356; -.
DR   KEGG; mmu:53356; -.
DR   NMPDR; fig|10090.3.peg.19701; -.
DR   UCSC; uc009ojm.1; mouse.
DR   CTD; 53356; -.
DR   MGI; MGI:1858258; Eif3g.
DR   GeneTree; ENSGT00510000047802; -.
DR   HOGENOM; HBG381036; -.
DR   HOVERGEN; HBG026850; -.
DR   InParanoid; Q9Z1D1; -.
DR   OMA; LILSVEW; -.
DR   OrthoDB; EOG4Z0B62; -.
DR   PhylomeDB; Q9Z1D1; -.
DR   NextBio; 310169; -.
DR   ArrayExpress; Q9Z1D1; -.
DR   Bgee; Q9Z1D1; -.
DR   Genevestigator; Q9Z1D1; -.
DR   GermOnline; ENSMUSG00000070319; Mus musculus.
DR   GO; GO:0005852; C:eukaryotic translation initiation factor 3 complex; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR017334; Transl_init_eIF-3_RNA-bind.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PIRSF; PIRSF037949; Transl_init_eIF-3_RNA-bind; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Initiation factor; Nucleus; Phosphoprotein;
KW   Protein biosynthesis; RNA-binding.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    320       Eukaryotic translation initiation factor
FT                                3 subunit G.
FT                                /FTId=PRO_0000123511.
FT   DOMAIN      239    317       RRM.
FT   MOD_RES      38     38       Phosphothreonine (By similarity).
FT   MOD_RES      41     41       Phosphothreonine.
FT   MOD_RES      42     42       Phosphoserine.
FT   CONFLICT     17     18       EE -> AA (in Ref. 1; AAD00176).
FT   CONFLICT     21     21       E -> Q (in Ref. 1; AAD00176).
FT   CONFLICT     24     24       K -> T (in Ref. 1; AAD00176).
FT   CONFLICT     32     32       K -> T (in Ref. 1; AAD00176).
FT   CONFLICT     60     60       I -> P (in Ref. 1; AAD00176).
FT   CONFLICT     88     88       E -> S (in Ref. 1; AAD00176).
FT   CONFLICT    222    223       AS -> PA (in Ref. 1; AAD00176).
SQ   SEQUENCE   320 AA;  35638 MW;  1B46670351E489AC CRC64;
     MPTGDFDSKP SWADQVEEEG EDDKCVTSEL LKGIPLPTGD TSPEPELLPG DPLPPPKEVI
     NGNIKTVTEY KIEEDGKKFK IVRTFRIETR KASKAVARRK NWKKFGNSEF DPPGPNVATT
     TVSDDVSMTF ITSKEDLNCQ EEEDPMNKLK GQKIVSCRIC KGDHWTTRCP YKDTLGPMQK
     ELAEQLGLST GEKEKLPGEL EPVQAAQSKT GKYVPPSLRD GASRRGESMQ PNRRADDNAT
     IRVTNLSEDT RETDLQELFR PFGSISRIYL AKDKTTGQSK GFAFISFHRR EDAARAIAGV
     SGFGYDHLIL NVEWAKPSTN
//
ID   GYS1_MOUSE              Reviewed;         738 AA.
AC   Q9Z1E4; P54859; Q3TBN4; Q8BQG4; Q8VEB0;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Glycogen [starch] synthase, muscle;
DE            EC=2.4.1.11;
GN   Name=Gys1; Synonyms=Gys, Gys3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Swiss albino; TISSUE=Astrocyte;
RX   MEDLINE=96385248; PubMed=8793107; DOI=10.1016/0169-328X(95)00305-C;
RA   Pellegri G., Rossier C., Magistretti P.J., Martin J.-L.;
RT   "Cloning, localization and induction of mouse brain glycogen
RT   synthase.";
RL   Brain Res. Mol. Brain Res. 38:191-199(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Seldin M.F., Xue Z., Rochelle J.M., DeBry R., Surwit R.;
RT   "Mouse glycogen synthase gene.";
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-641, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-657, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Transfers the glycosyl residue from UDP-Glc to the non-
CC       reducing end of alpha-1,4-glucan (By similarity).
CC   -!- CATALYTIC ACTIVITY: UDP-glucose ((1->4)-alpha-D-glucosyl)(n) = UDP
CC       + ((1->4)-alpha-D-glucosyl)(n+1).
CC   -!- ENZYME REGULATION: Allosteric activation by glucose-6-phosphate.
CC       Phosphorylation reduces the activity towards UDP-glucose. When in
CC       the non-phosphorylated state, glycogen synthase does not require
CC       glucose-6-phosphate as an allosteric activator; when
CC       phosphorylated it does (By similarity).
CC   -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis.
CC   -!- SUBUNIT: Interacts with GYG1 (By similarity).
CC   -!- INTERACTION:
CC       P46976:GYG1 (xeno); NbExp=1; IntAct=EBI-1152696, EBI-740533;
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 3 family.
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DR   EMBL; X94616; CAA64322.1; -; mRNA.
DR   EMBL; U53218; AAD09457.1; -; mRNA.
DR   EMBL; AK050813; BAC34420.1; -; mRNA.
DR   EMBL; AK171148; BAE42275.1; -; mRNA.
DR   EMBL; CH466603; EDL22855.1; -; Genomic_DNA.
DR   EMBL; BC019389; AAH19389.1; -; mRNA.
DR   EMBL; BC131687; AAI31688.1; -; mRNA.
DR   EMBL; BC131688; AAI31689.1; -; mRNA.
DR   EMBL; BC152550; AAI52551.1; -; mRNA.
DR   IPI; IPI00130127; -.
DR   RefSeq; NP_109603.2; NM_030678.3.
DR   UniGene; Mm.275654; -.
DR   ProteinModelPortal; Q9Z1E4; -.
DR   SMR; Q9Z1E4; 22-624.
DR   IntAct; Q9Z1E4; 1.
DR   STRING; Q9Z1E4; -.
DR   CAZy; GT3; Glycosyltransferase Family 3.
DR   PhosphoSite; Q9Z1E4; -.
DR   PRIDE; Q9Z1E4; -.
DR   Ensembl; ENSMUST00000003964; ENSMUSP00000003964; ENSMUSG00000003865.
DR   GeneID; 14936; -.
DR   KEGG; mmu:14936; -.
DR   CTD; 14936; -.
DR   MGI; MGI:101805; Gys1.
DR   eggNOG; roNOG07189; -.
DR   GeneTree; ENSGT00390000018612; -.
DR   HOGENOM; HBG330297; -.
DR   HOVERGEN; HBG001960; -.
DR   InParanoid; Q9Z1E4; -.
DR   OMA; LAQSEEK; -.
DR   OrthoDB; EOG4C2H91; -.
DR   PhylomeDB; Q9Z1E4; -.
DR   BRENDA; 2.4.1.11; 244.
DR   ArrayExpress; Q9Z1E4; -.
DR   Bgee; Q9Z1E4; -.
DR   Genevestigator; Q9Z1E4; -.
DR   GermOnline; ENSMUSG00000003865; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0016234; C:inclusion body; IDA:MGI.
DR   GO; GO:0004373; F:glycogen (starch) synthase activity; IMP:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0005978; P:glycogen biosynthetic process; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   InterPro; IPR008631; Glycogen_synth.
DR   PANTHER; PTHR10176; Glycogen_synth; 1.
DR   Pfam; PF05693; Glycogen_syn; 1.
PE   1: Evidence at protein level;
KW   Allosteric enzyme; Glycogen biosynthesis; Glycosyltransferase;
KW   Phosphoprotein; Transferase.
FT   CHAIN         1    738       Glycogen [starch] synthase, muscle.
FT                                /FTId=PRO_0000194765.
FT   BINDING      39     39       UDP-glucose (By similarity).
FT   MOD_RES       8      8       Phosphoserine; by PKA (By similarity).
FT   MOD_RES      11     11       Phosphoserine (By similarity).
FT   MOD_RES     412    412       Phosphoserine (By similarity).
FT   MOD_RES     641    641       Phosphoserine.
FT   MOD_RES     645    645       Phosphoserine (By similarity).
FT   MOD_RES     649    649       Phosphoserine (By similarity).
FT   MOD_RES     653    653       Phosphoserine (By similarity).
FT   MOD_RES     657    657       Phosphoserine.
FT   MOD_RES     698    698       Phosphoserine (By similarity).
FT   MOD_RES     728    728       Phosphoserine (By similarity).
FT   MOD_RES     730    730       Phosphothreonine (By similarity).
FT   MOD_RES     731    731       Phosphoserine (By similarity).
FT   MOD_RES     732    732       Phosphoserine (By similarity).
FT   CONFLICT      3      3       L -> R (in Ref. 1; CAA64322).
FT   CONFLICT     70     70       E -> V (in Ref. 2; AAD09457).
FT   CONFLICT     80     80       L -> M (in Ref. 3; BAE42275).
FT   CONFLICT    111    112       GP -> D (in Ref. 1; CAA64322).
FT   CONFLICT    120    120       G -> A (in Ref. 2; AAD09457).
FT   CONFLICT    148    148       A -> G (in Ref. 2; AAD09457).
FT   CONFLICT    154    155       FG -> YS (in Ref. 2; AAD09457).
FT   CONFLICT    191    191       C -> S (in Ref. 1; CAA64322).
FT   CONFLICT    208    208       L -> V (in Ref. 2; AAD09457).
FT   CONFLICT    228    228       N -> I (in Ref. 2; AAD09457).
FT   CONFLICT    581    582       QR -> HG (in Ref. 1; CAA64322).
FT   CONFLICT    640    640       A -> V (in Ref. 2; AAD09457).
SQ   SEQUENCE   738 AA;  83927 MW;  D1F9252CA908FF69 CRC64;
     MPLSRSLSVS SLPGLEDWED EFDPENAVLF EVAWEVANKV GGIYTVLQTK AKVTGDEWGD
     NYYLVGPYTE QGVRTQVELL EPPTPELKRT LDSMNSKGCK VYFGRWLIEG GPLVVLLDVG
     ASAWALERWK GELWDTCNIG VPWYDREAND AVLFGFLTTW FLGEFLAQNE EKPYVVAHFH
     EWLAGVGLCL CRARRLPVAT IFTTHATLLG RYLCAGAVDF YNNLENFNVD KEAGERQIYH
     RYCMERAAAH CAHVFTTVSQ ITAIEAQHLL KRKPDIVTPN GLNVKKFSAM HEFQNLHAQS
     KARIQEFVRG HFYGHLDFNL DKTLYFFIAG RYEFSNKGAD VFLEALARLN YLLRVNGSEQ
     TVVAFFIMPA RTNNFNVETL KGQAVRKQLW DTANTVKEKF GRKLYESLLV GSLPDMNKML
     DKEDFTMMKR AIFATQRQSF PPVCTHNMLD DSSDPILTTI RRIGLFNSSA DRVKVIFHPE
     FLSSTSPLLP VDYEEFVRGC HLGVFPSYYE PWGYTPAECT VMGIPSISTN LSGFGCFMEE
     HIADPSAYGI YILDRRFRSL DDSCSQLTSF LYSFCQQSRR QRIIQRNRTE RLSDLLDWKY
     LGRYYMSARH MALAKAFPDH FTYEPHEVDA TQGYRYPRPA SVPPSPSLSR HSSPHQSEDE
     EEPRDGPLGE DSERYDEEEE AAKDRRNIRA PEWPRRASCS SSTGGSKRSN SVDTGPSSSL
     STPTEPLSPT SSLGEERN
//
ID   VATC1_MOUSE             Reviewed;         382 AA.
AC   Q9Z1G3; Q91Z42;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 4.
DT   08-MAR-2011, entry version 85.
DE   RecName: Full=V-type proton ATPase subunit C 1;
DE            Short=V-ATPase subunit C 1;
DE   AltName: Full=Vacuolar proton pump subunit C 1;
GN   Name=Atp6v1c1; Synonyms=Atp6c, Atp6c1, Vatc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=22415104; PubMed=12527205; DOI=10.1016/S0378-1119(02)01099-5;
RA   Sun-Wada G.-H., Yoshimizu T., Imai-Senga Y., Wada Y., Futai M.;
RT   "Diversity of mouse proton-translocating ATPase: presence of multiple
RT   isoforms of the C, d and G subunits.";
RL   Gene 302:147-153(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Howell M.L., Dean G.E.;
RT   "cDNA sequences for mouse vacuolar ATPase subunits.";
RL   Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PROTEIN SEQUENCE OF 38-111; 120-137; 148-155; 200-231; 275-281;
RP   310-326 AND 374-382, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Subunit of the peripheral V1 complex of vacuolar ATPase.
CC       Subunit C is necessary for the assembly of the catalytic sector of
CC       the enzyme and is likely to have a specific function in its
CC       catalytic activity. V-ATPase is responsible for acidifying a
CC       variety of intracellular compartments in eukaryotic cells.
CC   -!- SUBUNIT: V-ATPase is an heteromultimeric enzyme composed of a
CC       peripheral catalytic V1 complex (components A to H) attached to an
CC       integral membrane V0 proton pore complex (components: a, c, c',
CC       c'' and d).
CC   -!- INTERACTION:
CC       P62331:Arf6; NbExp=1; IntAct=EBI-772679, EBI-988682;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Abundant in brain, liver, kidney
CC       and testis.
CC   -!- SIMILARITY: Belongs to the V-ATPase C subunit family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AB088407; BAC57953.1; -; mRNA.
DR   EMBL; U13839; AAC83084.1; -; mRNA.
DR   EMBL; AK075779; BAC35953.1; -; mRNA.
DR   EMBL; AK151237; BAE30229.1; -; mRNA.
DR   EMBL; BC010217; AAH10217.1; -; mRNA.
DR   IPI; IPI00130186; -.
DR   RefSeq; NP_079770.2; NM_025494.3.
DR   UniGene; Mm.276618; -.
DR   ProteinModelPortal; Q9Z1G3; -.
DR   SMR; Q9Z1G3; 2-376.
DR   IntAct; Q9Z1G3; 3.
DR   STRING; Q9Z1G3; -.
DR   PhosphoSite; Q9Z1G3; -.
DR   PRIDE; Q9Z1G3; -.
DR   Ensembl; ENSMUST00000022904; ENSMUSP00000022904; ENSMUSG00000022295.
DR   GeneID; 66335; -.
DR   KEGG; mmu:66335; -.
DR   CTD; 66335; -.
DR   MGI; MGI:1913585; Atp6v1c1.
DR   GeneTree; ENSGT00390000004263; -.
DR   HOGENOM; HBG388608; -.
DR   HOVERGEN; HBG002470; -.
DR   InParanoid; Q9Z1G3; -.
DR   OMA; SEIIGKQ; -.
DR   OrthoDB; EOG46MBJQ; -.
DR   PhylomeDB; Q9Z1G3; -.
DR   BRENDA; 3.6.3.14; 244.
DR   NextBio; 321359; -.
DR   ArrayExpress; Q9Z1G3; -.
DR   Bgee; Q9Z1G3; -.
DR   CleanEx; MM_ATP6V1C1; -.
DR   Genevestigator; Q9Z1G3; -.
DR   GermOnline; ENSMUSG00000022295; Mus musculus.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR   GO; GO:0008553; F:hydrogen-exporting ATPase activity, phosphorylative mechanism; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
DR   InterPro; IPR004907; ATPase_V1-cplx_csu.
DR   PANTHER; PTHR10137; ATPase_V1_c; 1.
DR   Pfam; PF03223; V-ATPase_C; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Direct protein sequencing; Hydrogen ion transport;
KW   Ion transport; Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    382       V-type proton ATPase subunit C 1.
FT                                /FTId=PRO_0000209349.
FT   MOD_RES       2      2       N-acetylthreonine (By similarity).
FT   CONFLICT    267    267       R -> E (in Ref. 2; AAC83084).
SQ   SEQUENCE   382 AA;  43888 MW;  6D1851D8C81DF98F CRC64;
     MTEFWLISAP GEKTCQQTWE KLHAATTKNN NLAVSSKFNI PDLKVGTLDV LVGLSDELAK
     LDAFVEGVVK KVAQYMADVL EDSKDKVQEN LLASGVDLVT YITRFQWDMA KYPIKQSLKN
     ISEIIAKGVT QIDNDLKSRA SAYNNLKGNL QNLERKNAGS LLTRSLAEIV KKDDFVLDSE
     YLVTLLVVVP KLNHNDWIKQ YETLAEMVVP RSSNVLSEDQ DSYLCNVTLF RKAVDDFRHK
     ARENKFIVRD FQYNEEEMKA DKEEMTRLST DKKKQFGPLV RWLKVNFSEA FIAWIHIKAL
     RVFVESVLRY GLPVNFQAML LQPNKKSVKK LREVLHELYK HLDSSAAAII DAPMDIPGLN
     LSQQEYYPYV YYKIDCNLLE FK
//
ID   NEK4_MOUSE              Reviewed;         792 AA.
AC   Q9Z1J2; O35673; Q9R1J1;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Serine/threonine-protein kinase Nek4;
DE            EC=2.7.11.1;
DE   AltName: Full=Never in mitosis A-related kinase 4;
DE            Short=NimA-related protein kinase 4;
DE   AltName: Full=Serine/threonine-protein kinase 2;
GN   Name=Nek4; Synonyms=Stk2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=BALB/c; TISSUE=Spleen;
RX   MEDLINE=20001940; PubMed=10529384; DOI=10.1006/bbrc.1999.1536;
RA   Hayashi K., Igarashi H., Ogawa M., Sakaguchi N.;
RT   "Activity and substrate specificity of the murine STK2
RT   serine/threonine kinase that is structurally related to the mitotic
RT   regulator protein NIMA of Aspergillus nidulans.";
RL   Biochem. Biophys. Res. Commun. 264:449-456(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   MEDLINE=99321807; PubMed=10393247; DOI=10.1016/S0378-1119(99)00165-1;
RA   Chen A., Yanai A., Arama E., Kilfin G., Motro B.;
RT   "NIMA-related kinases: isolation and characterization of murine nek3
RT   and nek4 cDNAs, and chromosomal localization of nek1, nek2 and nek3.";
RL   Gene 234:127-137(1999).
CC   -!- FUNCTION: Seems to act exclusively upon threonine residues.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=mSTK2L;
CC         IsoId=Q9Z1J2-1; Sequence=Displayed;
CC       Name=2; Synonyms=mSTK2S;
CC         IsoId=Q9Z1J2-2; Sequence=VSP_007001;
CC   -!- TISSUE SPECIFICITY: Expressed ubiquitously among various organs
CC       and is up-regulated in the testis.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. NEK Ser/Thr
CC       protein kinase family. NIMA subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AJ223071; CAA11072.1; -; mRNA.
DR   EMBL; Y09234; CAA70436.1; -; mRNA.
DR   EMBL; AF099067; AAD16287.1; -; mRNA.
DR   IPI; IPI00223501; -.
DR   IPI; IPI00309384; -.
DR   PIR; JC7122; JC7122.
DR   RefSeq; NP_035979.1; NM_011849.2.
DR   UniGene; Mm.251494; -.
DR   ProteinModelPortal; Q9Z1J2; -.
DR   SMR; Q9Z1J2; 2-264.
DR   STRING; Q9Z1J2; -.
DR   PhosphoSite; Q9Z1J2; -.
DR   PRIDE; Q9Z1J2; -.
DR   Ensembl; ENSMUST00000050171; ENSMUSP00000057915; ENSMUSG00000021918.
DR   Ensembl; ENSMUST00000112124; ENSMUSP00000107752; ENSMUSG00000021918.
DR   GeneID; 23955; -.
DR   KEGG; mmu:23955; -.
DR   UCSC; uc007swd.1; mouse.
DR   CTD; 23955; -.
DR   MGI; MGI:1344404; Nek4.
DR   eggNOG; roNOG10932; -.
DR   GeneTree; ENSGT00600000084101; -.
DR   HOGENOM; HBG713157; -.
DR   HOVERGEN; HBG031740; -.
DR   InParanoid; Q9Z1J2; -.
DR   OrthoDB; EOG4GXFM4; -.
DR   PhylomeDB; Q9Z1J2; -.
DR   BRENDA; 2.7.11.1; 244.
DR   ArrayExpress; Q9Z1J2; -.
DR   Bgee; Q9Z1J2; -.
DR   Genevestigator; Q9Z1J2; -.
DR   GermOnline; ENSMUSG00000021918; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ATP-binding; Cell cycle; Cell division; Kinase;
KW   Magnesium; Metal-binding; Mitosis; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    792       Serine/threonine-protein kinase Nek4.
FT                                /FTId=PRO_0000086426.
FT   DOMAIN        6    261       Protein kinase.
FT   NP_BIND      12     20       ATP (By similarity).
FT   ACT_SITE    131    131       Proton acceptor (By similarity).
FT   BINDING      35     35       ATP (By similarity).
FT   MOD_RES     165    165       Phosphothreonine; by autocatalysis (By
FT                                similarity).
FT   VAR_SEQ     456    503       Missing (in isoform 2).
FT                                /FTId=VSP_007001.
FT   CONFLICT    499    499       G -> R (in Ref. 2; AAD16287).
SQ   SEQUENCE   792 AA;  88994 MW;  CF9187311C807A1D CRC64;
     MPQAAYCYMR VVGRGSYGEV TLVKHRRDGK QYVIKKLNLR NASSRERRAA EQEAQLLSQL
     KHPNIVTYKE SWEGGDGLLY IVMGFCEGGD LYRKLKEQKG QLLPESQVVE WFVQIAMALQ
     YLHEKHILHR DLKTQNVFLT RTNIIKVGDL GIARVLENHG DMASTLIGTP YYMSPELFSN
     KPYNYKSDVW ALGCCVYEMA TLKHAFNAKD MNSLVYRIIE GKLPPMPKVY STELAELIRT
     MLSRRPEERP SVRSILRQPY IKHHISLFLE ATKAKTSKNN VKNCDSRAKP VAAVVSRKEE
     SNTDVIHYQP RSSEGSALHV MGEDKCLSQE KPVDIGPLRS PASLEGHTGK QDMNNTGESC
     ATISRINIDI LPAERRDSAN AGVVQESQPQ HVDAADEVDS QCSISQEKER LQGNTKSSDQ
     PGNLLPRRSS DGGDGEGSEL VKPLYPSNKD QKPDQDQVTG IIENQDSIHP RSQPHSSMSE
     PSLSRQRRQK KREQTAHSGT KSQFQELPPR LLPSYPGIGK VDIIATQQND GNQGGPVAGC
     VNSSRTSSTA SAKDRPLSAR ERRRLKQSQE EMLPSGPAVQ RTPSAVEPLK PQEEDQPIPA
     QRFSSDCSIT QMNHTLPREK EKRLMHGLSE DELSSSTSST DKSDGDSREG KSHTNEMKDL
     VQLMTQTLRL EAKESCEDLQ VLNPGSEFRL HRKYRDTLVL HGKVAEEVEP HCTELPTGII
     PGSEKIRRIV EVLRADVIQG LGIQLLEQVF DLLGEEDELE REARLQEHMG DKYTTYCVKA
     RQLKFFEENV SF
//
ID   APC2_MOUSE              Reviewed;        2274 AA.
AC   Q9Z1K7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-FEB-2011, entry version 71.
DE   RecName: Full=Adenomatous polyposis coli protein 2;
GN   Name=Apc2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=99147086; PubMed=10021369; DOI=10.1016/S0960-9822(99)80024-4;
RA   van Es J.H., Kirkpatrick C., van de Wetering M., Molenaar M.,
RA   Miles A., Kuipers J., Destree O., Peifer M., Clevers H.;
RT   "Identification of APC2, a homologue of the adenomatous polyposis coli
RT   tumour suppressor.";
RL   Curr. Biol. 9:105-108(1999).
RN   [2]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15018807; DOI=10.1016/S1567-133X(01)00021-7;
RA   Yamanaka H., Hashimoto N., Koyama K., Nakagawa H., Nakamura Y.,
RA   Noguchi K.;
RT   "Expression of Apc2 during mouse development.";
RL   Gene Expr. Patterns 1:107-114(2002).
RN   [3]
RP   INTERACTION WITH PSRC1 AND MAPRE3.
RX   PubMed=17310996; DOI=10.1038/sj.onc.1210304;
RA   Hsieh P.-C., Chang J.-C., Sun W.-T., Hsieh S.-C., Wang M.-C.,
RA   Wang F.-F.;
RT   "p53 downstream target DDA3 is a novel microtubule-associated protein
RT   that interacts with end-binding protein EB3 and activates beta-catenin
RT   pathway.";
RL   Oncogene 26:4928-4940(2007).
CC   -!- FUNCTION: Promotes rapid degradation of CTNNB1 and may function as
CC       a tumor suppressor. May function in Wnt signaling (By similarity).
CC   -!- SUBUNIT: Interacts with APC, CTNNB1, TP53BP2 and possibly with
CC       AXIN2 (By similarity). Interacts with MAPRE3, PSRC1 and probably
CC       MAPRE1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus
CC       membrane; Peripheral membrane protein; Cytoplasmic side (By
CC       similarity). Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity). Cytoplasm, cytoskeleton (By
CC       similarity). Note=Associated with actin filaments and the
CC       microtubule network (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in brain and other neural tissues.
CC   -!- DEVELOPMENTAL STAGE: Strongly expressed in fetal brain but
CC       expression decreases from P12 onward. Expressed in post-mitotic
CC       neurons.
CC   -!- SIMILARITY: Belongs to the adenomatous polyposis coli (APC)
CC       family.
CC   -!- SIMILARITY: Contains 6 ARM repeats.
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DR   EMBL; AJ130783; CAA10207.1; -; Genomic_DNA.
DR   EMBL; AJ130784; CAA10207.1; JOINED; Genomic_DNA.
DR   EMBL; AJ130785; CAA10207.1; JOINED; Genomic_DNA.
DR   EMBL; AJ130786; CAA10207.1; JOINED; Genomic_DNA.
DR   EMBL; AJ130787; CAA10207.1; JOINED; Genomic_DNA.
DR   EMBL; AJ130788; CAA10207.1; JOINED; Genomic_DNA.
DR   EMBL; AJ130789; CAA10207.1; JOINED; Genomic_DNA.
DR   EMBL; AJ130790; CAA10207.1; JOINED; Genomic_DNA.
DR   EMBL; AJ130791; CAA10207.1; JOINED; Genomic_DNA.
DR   EMBL; AJ130792; CAA10207.1; JOINED; Genomic_DNA.
DR   EMBL; AJ130793; CAA10207.1; JOINED; Genomic_DNA.
DR   EMBL; AJ130794; CAA10207.1; JOINED; Genomic_DNA.
DR   EMBL; AJ130795; CAA10207.1; JOINED; Genomic_DNA.
DR   EMBL; AJ130796; CAA10207.1; JOINED; Genomic_DNA.
DR   IPI; IPI00130238; -.
DR   PIR; T30258; T30258.
DR   UniGene; Mm.57247; -.
DR   HSSP; P25054; 1DEB.
DR   ProteinModelPortal; Q9Z1K7; -.
DR   SMR; Q9Z1K7; 6-57, 127-236, 407-693.
DR   STRING; Q9Z1K7; -.
DR   PhosphoSite; Q9Z1K7; -.
DR   PRIDE; Q9Z1K7; -.
DR   Ensembl; ENSMUST00000020349; ENSMUSP00000020349; ENSMUSG00000020135.
DR   UCSC; uc007gcp.1; mouse.
DR   MGI; MGI:1346052; Apc2.
DR   eggNOG; roNOG10901; -.
DR   GeneTree; ENSGT00530000063749; -.
DR   HOVERGEN; HBG104821; -.
DR   ArrayExpress; Q9Z1K7; -.
DR   Bgee; Q9Z1K7; -.
DR   CleanEx; MM_APC2; -.
DR   Genevestigator; Q9Z1K7; -.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0016055; P:Wnt receptor signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR009234; APC_basic.
DR   InterPro; IPR009223; APC_crr.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR009224; SAMP.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 2.
DR   Pfam; PF05956; APC_basic; 1.
DR   Pfam; PF05923; APC_crr; 4.
DR   Pfam; PF00514; Arm; 1.
DR   Pfam; PF05924; SAMP; 2.
DR   SMART; SM00185; ARM; 6.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50176; ARM_REPEAT; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton; Golgi apparatus;
KW   Membrane; Microtubule; Repeat; Wnt signaling pathway.
FT   CHAIN         1   2274       Adenomatous polyposis coli protein 2.
FT                                /FTId=PRO_0000313687.
FT   REPEAT      301    341       ARM 1.
FT   REPEAT      472    511       ARM 2.
FT   REPEAT      515    555       ARM 3.
FT   REPEAT      557    602       ARM 4.
FT   REPEAT      608    647       ARM 5.
FT   REPEAT      650    689       ARM 6.
FT   REPEAT     1049   1068       1.
FT   REPEAT     1140   1159       2.
FT   REPEAT     1250   1269       3.
FT   REPEAT     1375   1394       4.
FT   REPEAT     1546   1565       5.
FT   REGION     1049   1565       5 X 20 AA approximate repeat of F-X-V-E-
FT                                X-T-P-X-C-F-S-R-X-S-S-L-S-S-L-S.
FT   REGION     1049   1565       Interaction with CTNNB1 (By similarity).
FT   REGION     2037   2114       Interaction with MAPRE1 and MAPRE3 (By
FT                                similarity).
FT   COILED        5     59       Potential.
FT   COILED      832    856       Potential.
FT   COMPBIAS   1057   1186       Ser-rich.
FT   COMPBIAS   1829   1922       Pro-rich.
SQ   SEQUENCE   2274 AA;  243139 MW;  75ABDA15D0F707F5 CRC64;
     MTSSMASYEQ LVRQVEALKA ENTHLRQELR DNSSHLSKLE TETSGMKEVL KHLQGKLEQE
     ARVLVSSGQT EVLEQLKALQ TDISSLYNLK FHAPALGPEP AARTPEGSPV HGSGPSKDSF
     GELSRATIRL LEELDQERCF LLSEIEKEEK EKLWYYSQLQ GLSKRLDELP HVDTFSMQMD
     LIRQQLEFEA QHIRSLMEER FGTSDEMVQR AQIRASRLEQ IDKELLEAQD RVQQTEPQAL
     LAVKPVAVEE EQEAEVPTHP EDGTPQPGNS KVEVVFWLLS MLATRDQEDT ARTLLAMSSS
     PESCVAMRRS GCLPLLLQIL HGTEAGSVGR AGIPGAPGAK DARMRANAAL HNIVFSQPDQ
     GLARKEMRVL HVLEQIRAYC ETCWDWLQAR DSGTETPVPI EPQICQATCA VMKLSFDEEY
     RRAMNELGGL QAVAELLQVD YEMHKMTRDP LNLALRRYAG MTLTNLTFGD VANKATLCAR
     RGCMEAIVAQ LGSESEELHQ VVSSILRNLS WRADINSKKV LREVGSMTAL MECVLRASKE
     STLKSVLSAL WNLSAHSTEN KAAICQVDGA LGFLVSTLTY RCQGNSLAVI ESGGGILRNV
     SSLIATREDY RQVLRDHNCL QTLLQHLTSH SLTIVSNACG TLWNLSARSP RDQELLWDLG
     AVGMLRNLVH SKHKMIAMGS AAALRNLLAH RPAKYQAAAM AVSPGTCVPS LYVRKQRALE
     AELDTRHLVH ALGHLEKQSL PEAETTSKKP LPPLRHLDGL VQDYASDSGC FDDDDAPSLA
     AAATTAEPAS PAVMSMFLGG PFLQGQALAR TPPARQGGLE AEKEAGGEAA VAAKAKAKLA
     LAVARIDRLV EDISALHTSS DDSFSLSSGD PGQEAPREGR AQSCSPCRGT EGGRREAGSR
     AHPLLRLKAA HTSLSNDSLN SGSTSDGYCT REHMTPCPLA ALAEHRDDPV RGQTRPRRLD
     LDLPSRAELP ARDTAATDAR VRTIKLSPTY QHVPLLDGAA GAGVRPLVGP GTSPGARKQA
     WIPADSLSKV PEKLVASPLP IASKVLQKLV AQDGPMSLSR CSSLSSLSST GHAVPSQAEN
     LDSDSSLEGL EEAGPGEAEL GRAWRASGST SLPVSIPAPQ RGRSRGLGVE DATPSSSSEN
     CVQETPLVLS RCSSVSSLGS FESRSIASSI PSDPCSGLGS GTVSPSELPD SPGQTMPPSR
     SKTPPAPPGQ PETSQFSLQW ESYVKRFLDI ADCRERCQPP SELDAGSVRF TVEKPDENFS
     CASSLSALAL HELYVQQDVE LRLRPPACPE RAVGGGGHRR RDEAASRLDG PAPAGSRARS
     ATDKELEALR ECLGAAMPAR LRKVASALVP GRRSLPVPVY MLVPAPARGD DSGTDSAEGT
     PVNFSSAASL SDETLQGPSR DKPAGPGDRQ KPTGRAAPAR QTRSHRPKAA GAGKSTEHTR
     GPCRNRAGLE LPLSRPQSAR SNRDSSCQTR TRGDGALQSL CLTTPTEEAV YCFYDSDEEP
     PATAPPPRRA SAIPRALKRE KPAGRKETPS RAAQPATLPV RAQPRLIVDE TPPCYSLTSS
     ASSLSEPEAP EQPANHARGP EQGSKQDSSP SPRAEEELLQ RCISLAMPRR RTQVPGSRRR
     KPRALRSDIR PTEITQKCQE EVAGSDPASD LDSVEWQAIQ EGANSIVTWL HQAAAKASLE
     ASSESDSLLS LVSGVSAGST LQPSKLRKGR KPAAEAGGAW RPEKRGTTST KINGSPRLPN
     GPEKAKGTQK MMAGESTMLR GRTVIYSAGP ASRTQSKGIS GPCTTPKKTG TSGTTQPETV
     TKAPSPEQQR SRSLHRPGKI SELAALRHPP RSATPPARLA KTPSSSSSQT SPASQPLPRR
     SPLATPTGGP LPGPGGSLVP KSPARALLAK QHKTQKSPVR IPFMQRPARR VPPPLARPSP
     EPGSRGRAGA EGTPGARGSR LGLVRMASAR SSGSESSDRS GFRRQLTFIK ESPGLLRRRR
     SELSSADSTA STSQAASPRR GRPALPAVFL CSSRCDELRV SPRQPLAAQR SPQAKPGLAP
     LAPRRTSSES PSRLPVRASP GRPETVKRYA SLPHISVSRR SDSAVSVPTT QANATRRGSD
     GEARPLPRVA PPGTTWRRIK DEDVPHILRS TLPATALPLR VSSPEDSPAG TPQRKTSDAV
     VQTEDVATSK TNSSTSPSLE SRDPPQAPAS GPVAPQGSDV DGPVLTKPPA SAPFPHEGLS
     AVIAGFPTSR HGSPSRAARV PPFNYVPSPM AAATMASDSA VEKAPVSSPA SLLE
//
ID   UAP56_MOUSE             Reviewed;         428 AA.
AC   Q9Z1N5; Q8HW97;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Spliceosome RNA helicase Bat1;
DE            EC=3.6.4.13;
DE   AltName: Full=56 kDa U2AF65-associated protein;
DE   AltName: Full=DEAD box protein UAP56;
DE   AltName: Full=HLA-B-associated transcript 1 protein;
GN   Name=Bat1; Synonyms=Bat1a, Uap56;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/10;
RA   Handel-Fernandez M.E., Vincek V.;
RT   "Sequence analysis of a mouse homolog of the human BAT1 gene (nuclear
RT   RNA helicase of the DEAD box protein family).";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c, and C57BL/10 X DBA/2;
RA   Dolecki K.J., Wong A.M.L., Price P.;
RT   "Characterization of murine Bat1, a putative immunoregulator of
RT   Tnfa.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129;
RX   PubMed=14656967; DOI=10.1101/gr.1736803;
RA   Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
RA   Campbell R.D., Hood L.;
RT   "Analysis of the gene-dense major histocompatibility complex class III
RT   region and its comparison to mouse.";
RL   Genome Res. 13:2621-2636(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Eye, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 145-155, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Component of the THO subcomplex of the TREX complex. The
CC       TREX complex specifically associates with spliced mRNA and not
CC       with unspliced pre-mRNA. It is recruited to spliced mRNAs by a
CC       transcription-independent mechanism. Binds to mRNA upstream of the
CC       exon-junction complex (EJC) and is recruited in a splicing- and
CC       cap-dependent manner to a region near the 5' end of the mRNA where
CC       it functions in mRNA export. The recruitment occurs via an
CC       interaction between THOC4 and the cap-binding protein NCBP1. UAP56
CC       functions as a bridge between THOC4 and the THO complex (By
CC       similarity).
CC   -!- FUNCTION: Splice factor that is required for the first ATP-
CC       dependent step in spliceosome assembly and for the interaction of
CC       U2 snRNP with the branchpoint. Has both RNA-stimulated ATP
CC       binding/hydrolysis activity and ATP-dependent RNA unwinding
CC       activity. Even with the stimulation of RNA, the ATPase activity is
CC       weak. Can only hydrolyze ATP but not other NTPs. The RNA
CC       stimulation of ATPase activity does not have a strong preference
CC       for the sequence and length of the RNA. However, ssRNA stimulates
CC       the ATPase activity much more strongly than dsRNA. The ATPase and
CC       helicase activities are not influenced by U2AF2 and THOC4 (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC   -!- SUBUNIT: Homodimer, and heterodimer with DDX39. Component of the
CC       THO complex, which is composed of THOC1, THOC2, THOC5, THOC6 and
CC       THOC7. Together with THOC3, THOC4 and UAP56, THO forms the
CC       transcription/export (TREX) complex. Component of the spliceosome.
CC       Interacts directly with U2AF2. Interacts directly with THOC4 and
CC       is necessary for THOC4 recruitment to spliced mRNA. Interacts with
CC       RBM8A, RNPS1 and SRRM1. Interacts with FYTTD1/UIF and THOC1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Nucleus speckle (By
CC       similarity).
CC   -!- DOMAIN: The helicase C-terminal domain mediates interaction with
CC       THOC4 (By similarity).
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DECD
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
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DR   EMBL; AF118128; AAD13115.1; -; mRNA.
DR   EMBL; AY255786; AAP91685.1; -; mRNA.
DR   EMBL; AY255787; AAP91686.1; -; mRNA.
DR   EMBL; AC007080; AAD30177.1; -; Genomic_DNA.
DR   EMBL; AK088867; BAC40624.1; -; mRNA.
DR   EMBL; AK051034; BAC34505.1; -; mRNA.
DR   EMBL; BC011067; AAH11067.1; -; mRNA.
DR   EMBL; BC024859; AAH24859.1; -; mRNA.
DR   IPI; IPI00409462; -.
DR   RefSeq; NP_062667.1; NM_019693.3.
DR   UniGene; Mm.439827; -.
DR   ProteinModelPortal; Q9Z1N5; -.
DR   SMR; Q9Z1N5; 46-426.
DR   IntAct; Q9Z1N5; 1.
DR   STRING; Q9Z1N5; -.
DR   PhosphoSite; Q9Z1N5; -.
DR   PRIDE; Q9Z1N5; -.
DR   Ensembl; ENSMUST00000068056; ENSMUSP00000070682; ENSMUSG00000019432.
DR   Ensembl; ENSMUST00000093645; ENSMUSP00000094948; ENSMUSG00000019432.
DR   GeneID; 53817; -.
DR   KEGG; mmu:53817; -.
DR   UCSC; uc008cha.1; mouse.
DR   CTD; 53817; -.
DR   MGI; MGI:99240; Bat1a.
DR   GeneTree; ENSGT00580000081513; -.
DR   HOGENOM; HBG737336; -.
DR   HOVERGEN; HBG107334; -.
DR   InParanoid; Q9Z1N5; -.
DR   OMA; KRFMQDP; -.
DR   OrthoDB; EOG4XSKPX; -.
DR   PhylomeDB; Q9Z1N5; -.
DR   NextBio; 310679; -.
DR   ArrayExpress; Q9Z1N5; -.
DR   Bgee; Q9Z1N5; -.
DR   CleanEx; MM_BAT1A; -.
DR   Genevestigator; Q9Z1N5; -.
DR   GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
DR   InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51195; Q_MOTIF; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Direct protein sequencing; Helicase;
KW   Hydrolase; mRNA processing; mRNA splicing; mRNA transport;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; RNA-binding; Spliceosome;
KW   Transport.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    428       Spliceosome RNA helicase Bat1.
FT                                /FTId=PRO_0000055073.
FT   DOMAIN       76    249       Helicase ATP-binding.
FT   DOMAIN      261    422       Helicase C-terminal.
FT   NP_BIND      89     96       ATP (By similarity).
FT   MOTIF        45     73       Q motif.
FT   MOTIF       196    199       DECD box.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      36     36       N6-acetyllysine (By similarity).
FT   MOD_RES      53     53       N6-acetyllysine (By similarity).
FT   MOD_RES     172    172       Phosphothreonine (By similarity).
FT   MOD_RES     188    188       N6-acetyllysine (By similarity).
SQ   SEQUENCE   428 AA;  49035 MW;  D5AA6B3905FDC968 CRC64;
     MAENDVDNEL LDYEDDEVET AAGADGTEAP AKKDVKGSYV SIHSSGFRDF LLKPELLRAI
     VDCGFEHPSE VQHECIPQAI LGMDVLCQAK SGMGKTAVFV LATLQQLEPV TGQVSVLVMC
     HTRELAFQIS KEYERFSKYM PNVKVAVFFG GLSIKKDEEV LKKNCPHIVV GTPGRILALA
     RNKSLNLKHI KHFILDECDK MLEQLDMRRD VQEIFRMTPH EKQVMMFSAT LSKEIRPVCR
     KFMQDPMEIF VDDETKLTLH GLQQYYVKLK DNEKNRKLFD LLDVLEFNQV VIFVKSVQRC
     IALAQLLVEQ NFPAIAIHRG MPQEERLSRY QQFKDFQRRI LVATNLFGRG MDIERVNIAF
     NYDMPEDSDT YLHRVARAGR FGTKGLAITF VSDENDAKIL NDVQDRFEVN ISELPDEIDI
     SSYIEQTR
//
ID   UN13B_MOUSE             Reviewed;        1602 AA.
AC   Q9Z1N9; A2AG43; B2RXT0; B2RXY6; Q6BCX2;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   08-MAR-2011, entry version 84.
DE   RecName: Full=Protein unc-13 homolog B;
DE   AltName: Full=Munc13-2;
DE            Short=munc13;
GN   Name=Unc13b; Synonyms=Unc13a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
RP   2).
RC   STRAIN=BALB/c;
RX   PubMed=15330860; DOI=10.1111/j.1365-2443.2004.00767.x;
RA   Fukuda M.;
RT   "Alternative splicing in the first alpha-helical region of the Rab-
RT   binding domain of Rim regulates Rab3A binding activity: is Rim a Rab3
RT   effector protein during evolution?";
RL   Genes Cells 9:831-842(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J;
RA   Song Y., Silverman M.;
RT   "Cloning of the mouse renal isoform of munc13s.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION.
RX   PubMed=12070347; DOI=10.1073/pnas.122623799;
RA   Varoqueaux F., Sigler A., Rhee J.-S., Brose N., Enk C., Reim K.,
RA   Rosenmund C.;
RT   "Total arrest of spontaneous and evoked synaptic transmission but
RT   normal synaptogenesis in the absence of Munc13-mediated vesicle
RT   priming.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9037-9042(2002).
CC   -!- FUNCTION: Plays a role in vesicle maturation during exocytosis as
CC       a target of the diacylglycerol second messenger pathway. Is
CC       involved in neurotransmitter release by acting in synaptic vesicle
CC       priming prior to vesicle fusion and participates in the activity-
CC       depending refilling of readily releasable vesicle pool (RRP) (By
CC       similarity). Essential for synaptic vesicle maturation in a subset
CC       of excitatory/glutamatergic but not inhibitory/GABA-mediated
CC       synapses.
CC   -!- SUBUNIT: Interacts with RIMS1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC       protein. Golgi apparatus. Cell junction, synapse (By similarity).
CC       Note=Localized to synapses (By similarity). Translocates to the
CC       Golgi in response to phorbol ester binding.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9Z1N9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Z1N9-2; Sequence=VSP_039197;
CC       Name=3;
CC         IsoId=Q9Z1N9-3; Sequence=VSP_039198;
CC   -!- DOMAIN: The C2 domains are not involved in calcium-dependent
CC       phospholipid binding (By similarity).
CC   -!- SIMILARITY: Belongs to the unc-13 family.
CC   -!- SIMILARITY: Contains 3 C2 domains.
CC   -!- SIMILARITY: Contains 1 MHD1 (MUNC13 homology domain 1) domain.
CC   -!- SIMILARITY: Contains 1 MHD2 (MUNC13 homology domain 2) domain.
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
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DR   EMBL; AB162894; BAD32690.1; -; Genomic_DNA.
DR   EMBL; AF115848; AAD13619.1; -; mRNA.
DR   EMBL; AL672276; CAM14326.1; -; Genomic_DNA.
DR   EMBL; AL732504; CAM14326.1; JOINED; Genomic_DNA.
DR   EMBL; AL772176; CAM14326.1; JOINED; Genomic_DNA.
DR   EMBL; AL732504; CAM16530.1; -; Genomic_DNA.
DR   EMBL; AL672276; CAM16530.1; JOINED; Genomic_DNA.
DR   EMBL; AL772176; CAM16530.1; JOINED; Genomic_DNA.
DR   EMBL; AL772176; CAM22579.1; -; Genomic_DNA.
DR   EMBL; AL672276; CAM22579.1; JOINED; Genomic_DNA.
DR   EMBL; AL732504; CAM22579.1; JOINED; Genomic_DNA.
DR   EMBL; BC157967; AAI57968.1; -; mRNA.
DR   EMBL; BC158025; AAI58026.1; -; mRNA.
DR   IPI; IPI00648554; -.
DR   IPI; IPI00753193; -.
DR   IPI; IPI00875727; -.
DR   RefSeq; NP_001074882.1; NM_001081413.1.
DR   RefSeq; NP_067443.2; NM_021468.2.
DR   UniGene; Mm.128892; -.
DR   ProteinModelPortal; Q9Z1N9; -.
DR   SMR; Q9Z1N9; 2-128, 490-539, 610-742, 1427-1560.
DR   STRING; Q9Z1N9; -.
DR   PhosphoSite; Q9Z1N9; -.
DR   PRIDE; Q9Z1N9; -.
DR   Ensembl; ENSMUST00000079978; ENSMUSP00000078894; ENSMUSG00000028456.
DR   GeneID; 22249; -.
DR   KEGG; mmu:22249; -.
DR   CTD; 22249; -.
DR   MGI; MGI:1342278; Unc13b.
DR   GeneTree; ENSGT00580000081383; -.
DR   HOVERGEN; HBG057340; -.
DR   OrthoDB; EOG4GTKC1; -.
DR   ArrayExpress; Q9Z1N9; -.
DR   Bgee; Q9Z1N9; -.
DR   CleanEx; MM_UNC13A; -.
DR   CleanEx; MM_UNC13B; -.
DR   Genevestigator; Q9Z1N9; -.
DR   GermOnline; ENSMUSG00000028456; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0001566; F:non-kinase phorbol ester receptor activity; TAS:MGI.
DR   GO; GO:0016082; P:synaptic vesicle priming; IMP:MGI.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR020477; C2_region.
DR   InterPro; IPR010439; Ca-dep_secretion_activator.
DR   InterPro; IPR014770; Munc13_1.
DR   InterPro; IPR014772; Munc13_dom-2.
DR   InterPro; IPR019558; Munc13_subgr_dom-2.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00168; C2; 3.
DR   Pfam; PF06292; DUF1041; 1.
DR   Pfam; PF10540; Membr_traf_MHD; 1.
DR   PRINTS; PR00360; C2DOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00239; C2; 3.
DR   SUPFAM; SSF49562; C2_CaLB; 3.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS51258; MHD1; 1.
DR   PROSITE; PS51259; MHD2; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell junction; Coiled coil; Cytoplasm;
KW   Exocytosis; Golgi apparatus; Membrane; Metal-binding; Phosphoprotein;
KW   Repeat; Synapse; Zinc; Zinc-finger.
FT   CHAIN         1   1602       Protein unc-13 homolog B.
FT                                /FTId=PRO_0000188576.
FT   DOMAIN        1     79       C2 1.
FT   DOMAIN      599    705       C2 2.
FT   DOMAIN     1024   1168       MHD1.
FT   DOMAIN     1275   1417       MHD2.
FT   DOMAIN     1437   1542       C2 3.
FT   ZN_FING     489    539       Phorbol-ester/DAG-type.
FT   COILED     1210   1231       Potential.
FT   MOD_RES     617    617       Phosphothreonine (By similarity).
FT   VAR_SEQ     176    188       CHWTYLGWGEHQT -> S (in isoform 2).
FT                                /FTId=VSP_039197.
FT   VAR_SEQ     962    962       Missing (in isoform 3).
FT                                /FTId=VSP_039198.
FT   CONFLICT     31     31       V -> E (in Ref. 2; AAD13619).
FT   CONFLICT    208    208       S -> D (in Ref. 2; AAD13619).
FT   CONFLICT    234    234       L -> W (in Ref. 1; BAD32690 and 2;
FT                                AAD13619).
FT   CONFLICT    262    262       R -> H (in Ref. 2; AAD13619).
FT   CONFLICT    353    353       H -> Y (in Ref. 1; BAD32690 and 2;
FT                                AAD13619).
FT   CONFLICT    512    513       GL -> AV (in Ref. 1; BAD32690 and 2;
FT                                AAD13619).
FT   CONFLICT    579    580       EV -> RI (in Ref. 2; AAD13619).
FT   CONFLICT    804    804       R -> A (in Ref. 2; AAD13619).
FT   CONFLICT    837    837       L -> M (in Ref. 2; AAD13619).
FT   CONFLICT   1073   1073       P -> PG (in Ref. 2; AAD13619).
FT   CONFLICT   1279   1280       PL -> GV (in Ref. 2; AAD13619).
FT   CONFLICT   1280   1280       L -> P (in Ref. 2; AAI58026).
FT   CONFLICT   1418   1418       R -> G (in Ref. 2; AAD13619).
FT   CONFLICT   1492   1492       K -> R (in Ref. 2; AAD13619).
SQ   SEQUENCE   1602 AA;  181813 MW;  FED63BFE566554D2 CRC64;
     MSLLCVRVKR AKFQGSPDKF NTYVTLKVQN VKSTTVAVRG DQPSWEQDFM FEISRLDLGL
     SVEVWNKGLI WDTMVGTVWI ALKTIRQSDE EGPGEWSTLE AETLMKDDEI CGTKNPTPHK
     ILLDTRFELP FDIPEEEARY WTYKLEQINA LADDNEYSSQ EESQRKPLPT AAAQCCHWTY
     LGWGEHQTFE DPDSAVDDRD SDYRSETSNS APPPYHTTTQ PNASVHQFPV PVRLPQQLFL
     QGSSHDSCND SMQSYDLDYP ERRALSPTSS SRYGSSCNVS QGSSLLSELD QYHEQDDDGR
     ERDSIHSSHS YGSLSKDGQA GLGEQEKALE VTCESEKEKT GESKEMRDDA TIHPPSDLVL
     HKDHVLGPQE SLPEETASSP FTQARAHWFR AVTKVRLQLQ EISDDGDPSL PQWLPEGPAG
     GLYGIDSMPD LRRKKPLPLV SDLSLVQSRK AGITSAMATR TSLKDEELKS HVYKKTLQAL
     IYPISCTTPH NFEVWSATTP TYCYECEGLL WGLARQGMRC SECGVKCHEK CQDLLNADCL
     QRAAEKSSKH GAEDRTQNII MAMKDRMKIR ERNKPEIFEV IRDVFTVSKV AHVQQMKTVK
     QSVLDGTSKW SAKITITVVC AQGLQAKDKT GSSDPYVTVQ VGKTKKRTKT IFGNLNPVWE
     EKFHFECHNS SDRIKVRVWD EDDDIKSRVK QRLKRESDDF LGQTIIEVRT LSGEMDVWYN
     LEKRTDKSAV SGAIRLQISV EIKGEEKVAP YHVQYTCLHE NLFHYLTDIQ GSGGVWIPEA
     RGDDAWKVYF DETAQEIVDE FAMRYGIESI YQAMTHFACL SSKYMCPGVP AVMSTLLANI
     NAYYAHTTAS TNVSASDRFA ASNFGKERFV KLLDQLHNSL RIDLSTYRNN FPAGSPERLQ
     DLKSTVDLLT SITFFRMKVQ ELQSPPRASQ VVKDCVKACL NSTYEYIFNN CHDLYSHQYQ
     LQEQPLEEPG PSIRNLDFWP KLITLIVSII EEDKNSYTPV LSQFPQELNV GKVSAEVMWH
     LFAQDMKYAL EEHEKDRLCK SADYMNLHFK VKWLHNEYVR DLPALQGQVP EYPAWFEQFV
     LQWLDENEDV SLEFLRGALE RDKKDGFQQT SEHALFSCSV VDVFTQLNQS FEIIRKLECP
     DPNILAHYMR RFAKTIGKVL MQYADILSKN FPAYCTKERL PCILMNNMQQ LRVQLEKMFE
     AMGGKELDSE AADSLKELQV KLNTVLDELS MVFGNSFQVR IDECVRQMAD ILGQVRGTGN
     ASPNARASVA QDADSVLRPL MDFLDGNLTL FATVCEKTVL KRVLKELWRV VMNTMERVIV
     LPPLTDQTGT QLILTAAKEL SQLSKLKDHM VREETRNLTP KQCAVLDLAL DTIKQYFHAG
     GNGLKKTFLE KSPDLQSLRY ALSLYTQTTD TLIKTFVRSQ TAQGAGVDDP VGEVSIQVDL
     FTHPGTGEHK VTVKVVAAND LKWQTAGMFR PFVEVTMVGP HQSDKKRKFT TKSKSNNWTP
     KYNETFHFLL GNEEGPEAYE LQICVKDYCF AREDRVIGLA VMPLRDVAAK GSCACWCPLG
     RKIHMDETGM TILRILSQRS NDEVAREFVK LKSESRSTEE GS
//
ID   KANK3_MOUSE             Reviewed;         791 AA.
AC   Q9Z1P7;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 75.
DE   RecName: Full=KN motif and ankyrin repeat domain-containing protein 3;
DE   AltName: Full=Ankyrin repeat domain-containing protein 47;
GN   Name=Kank3; Synonyms=Ankrd47, D17Ertd288e, Ng28;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129;
RX   PubMed=14656967; DOI=10.1101/gr.1736803;
RA   Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
RA   Campbell R.D., Hood L.;
RT   "Analysis of the gene-dense major histocompatibility complex class III
RT   region and its comparison to mouse.";
RL   Genome Res. 13:2621-2636(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129/Sv;
RX   PubMed=15112104; DOI=10.1007/s00335-003-2329-1;
RA   Abe K., Yuzuriha M., Sugimoto M., Ko M.S., Brathwaite M.E., Waeltz P.,
RA   Nagaraja R.;
RT   "Gene content of the 750-kb critical region for mouse embryonic
RT   ectoderm lethal tcl-w5.";
RL   Mamm. Genome 15:265-276(2004).
CC   -!- SIMILARITY: Contains 5 ANK repeats.
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DR   EMBL; AK002623; BAB22238.1; -; mRNA.
DR   EMBL; AF110520; AAC97966.1; -; Genomic_DNA.
DR   EMBL; AF528162; AAO17376.1; -; Genomic_DNA.
DR   IPI; IPI00130324; -.
DR   RefSeq; NP_109622.1; NM_030697.2.
DR   UniGene; Mm.196330; -.
DR   ProteinModelPortal; Q9Z1P7; -.
DR   SMR; Q9Z1P7; 606-771.
DR   STRING; Q9Z1P7; -.
DR   PhosphoSite; Q9Z1P7; -.
DR   PRIDE; Q9Z1P7; -.
DR   Ensembl; ENSMUST00000048560; ENSMUSP00000040126; ENSMUSG00000042099.
DR   GeneID; 80880; -.
DR   KEGG; mmu:80880; -.
DR   UCSC; uc008bzq.1; mouse.
DR   CTD; 80880; -.
DR   MGI; MGI:1098615; Kank3.
DR   GeneTree; ENSGT00530000063448; -.
DR   HOGENOM; HBG446458; -.
DR   HOVERGEN; HBG101217; -.
DR   InParanoid; Q9Z1P7; -.
DR   OMA; QLVREQM; -.
DR   OrthoDB; EOG45MN59; -.
DR   PhylomeDB; Q9Z1P7; -.
DR   NextBio; 350191; -.
DR   ArrayExpress; Q9Z1P7; -.
DR   Bgee; Q9Z1P7; -.
DR   CleanEx; MM_KANK3; -.
DR   Genevestigator; Q9Z1P7; -.
DR   GermOnline; ENSMUSG00000042099; Mus musculus.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR020683; Ankyrin_rpt-contain_dom.
DR   InterPro; IPR021939; KN_motif.
DR   Gene3D; G3DSA:1.25.40.20; ANK; 1.
DR   Pfam; PF00023; Ank; 3.
DR   Pfam; PF12075; KN_motif; 1.
DR   SMART; SM00248; ANK; 4.
DR   SUPFAM; SSF48403; ANK; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
PE   2: Evidence at transcript level;
KW   ANK repeat; Coiled coil; Repeat.
FT   CHAIN         1    791       KN motif and ankyrin repeat domain-
FT                                containing protein 3.
FT                                /FTId=PRO_0000244583.
FT   REPEAT      606    636       ANK 1.
FT   REPEAT      640    677       ANK 2.
FT   REPEAT      679    708       ANK 3.
FT   REPEAT      712    742       ANK 4.
FT   REPEAT      746    775       ANK 5.
FT   COILED      180    229       Potential.
FT   COMPBIAS    465    468       Poly-Ser.
FT   COMPBIAS    485    490       Poly-Ser.
SQ   SEQUENCE   791 AA;  84186 MW;  6BB5307AEEDD83E6 CRC64;
     MAKFVLNQNL PDLGGPPLYP GPTGSARSPS SPYSVETPYG FHLDLDFLKY VEEIERGPAS
     RRTPGPPHAR RPRASRTGLA GARSPGAWTS SESLASDDGG ASGALSPGAF PGLSLPPLSP
     RSLSRNPRVE HTLLETSRRL EQAQARERAL SPARAVTRSP RGSGRSSPAP NPALASPGPA
     QLQLVREQMA AALRRLRELE DQARALPELQ EQVRALRAEK ARLLAGRVQP EQEVEIEARP
     DKLAQLRRLT ERLATSDRGV RSRASPRAED PDGLAARRSE GALQVLDPGS RTPDGEPRTR
     ETGTEVVPET REVDAQAVPE TGEAGVEVVP ETVEVDTWVT EELLGLPEAA ERELELLRTS
     LEHQRGVSEL LRGRLRELEE AHEAAVTRPQ SRDVAAQTTL GCTEKTTQTE LPVENQPRPT
     AGDEMAPVGI LKSIMKKKDG IPGAQSSQGP KSLQFVGVLN GEYESSSSED GNSDDEDGVA
     EHPRSSSSGS DDSSGGSDAG TPGPHNDKDA GDCELETHPE LTAGREGRCE LNPRLREACI
     ALNQQLNRPR GVTSRDGNAA RLVAQEWFRV SSQKRSQAES VAGVLRGVKS LGPELLAYVV
     NLADGNGNTA LHYSVSHGNL AISSLLLDTG VCDVNHQNRA GYSALMLAAL TSVGQEEEDM
     AVAQRLFSMG DVNAKASQTG QTALMLAISH GHQDMVAALL ECGADVNVQD ADGATALMCA
     SEYGRLDTVQ LLLAQPGCDL TILDNEGTSA LAIALEAEQD EVAALLHAHL TSNHQGQSST
     GSPTAKECND K
//
ID   ABHGA_MOUSE             Reviewed;         558 AA.
AC   Q9Z1Q2;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 74.
DE   RecName: Full=Abhydrolase domain-containing protein 16A;
DE            EC=3.-.-.-;
DE   AltName: Full=HLA-B-associated transcript 5;
GN   Name=Abhd16a; Synonyms=Bat5, Ng26;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129;
RX   PubMed=14656967; DOI=10.1101/gr.1736803;
RA   Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
RA   Campbell R.D., Hood L.;
RT   "Analysis of the gene-dense major histocompatibility complex class III
RT   region and its comparison to mouse.";
RL   Genome Res. 13:2621-2636(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 418-426, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. ABHD16
CC       family.
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DR   EMBL; AF109905; AAC84159.1; -; Genomic_DNA.
DR   EMBL; BC029114; AAH29114.1; -; mRNA.
DR   IPI; IPI00130339; -.
DR   RefSeq; NP_848707.1; NM_178592.3.
DR   UniGene; Mm.43745; -.
DR   ProteinModelPortal; Q9Z1Q2; -.
DR   SMR; Q9Z1Q2; 251-436.
DR   STRING; Q9Z1Q2; -.
DR   MEROPS; S09.022; -.
DR   PhosphoSite; Q9Z1Q2; -.
DR   PRIDE; Q9Z1Q2; -.
DR   Ensembl; ENSMUST00000007251; ENSMUSP00000007251; ENSMUSG00000007036.
DR   GeneID; 193742; -.
DR   KEGG; mmu:193742; -.
DR   UCSC; uc008cfq.1; mouse.
DR   CTD; 193742; -.
DR   MGI; MGI:99476; Abhd16a.
DR   eggNOG; roNOG11402; -.
DR   GeneTree; ENSGT00390000017119; -.
DR   HOGENOM; HBG444395; -.
DR   HOVERGEN; HBG050666; -.
DR   InParanoid; Q9Z1Q2; -.
DR   OMA; KLLQFRY; -.
DR   OrthoDB; EOG49078Z; -.
DR   PhylomeDB; Q9Z1Q2; -.
DR   NextBio; 371512; -.
DR   ArrayExpress; Q9Z1Q2; -.
DR   Bgee; Q9Z1Q2; -.
DR   CleanEx; MM_BAT5; -.
DR   Genevestigator; Q9Z1Q2; -.
DR   GermOnline; ENSMUSG00000007036; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    558       Abhydrolase domain-containing protein
FT                                16A.
FT                                /FTId=PRO_0000064834.
FT   TRANSMEM     60     80       Helical; (Potential).
FT   TRANSMEM     93    113       Helical; (Potential).
FT   ACT_SITE    355    355       Charge relay system (By similarity).
FT   ACT_SITE    430    430       Charge relay system (By similarity).
FT   ACT_SITE    507    507       Charge relay system (By similarity).
SQ   SEQUENCE   558 AA;  63086 MW;  2DF1890F79E2EE63 CRC64;
     MAKLLSCVLG PRLYKIYRER DTDRAASSVP ETPTAVPAAS SSSWDTYYQP RALEKHADSI
     LALASVFWSI SYYSSPFAFF YLYRKGYLSL SKVVPFSHYA GTLLLLLAGV ACLRGIGRWT
     NPQYRQFITI LEATHRNQSA ENKRQLANYN FDFRSWPVDF HWEEPSSRKG SRGGPSRRGV
     ALLRPEPLHR GTADTFLNRV KKLPCQITSY LVAHTLGRRM LYPGSVYLLQ KALMPVLLQG
     QARLVEECNG RRAKLLACDG NEIDTMFVDR RGTAEPQGQK LVICCEGNAG FYEVGCVSTP
     LEAGYSVLGW NHPGFAGSTG VPFPQNEANA MDVVVQFAIH RLGFQPQDIV IYAWSIGGFT
     ATWAAMSYPD ISAVILDASF DDLVPLALKV MPDSWRALVT RTVRQHLNLN NSEQLCRFQG
     PVLLVRRTKD EIITTTVPED IMSNRGNDLL LKLLQFRYPR VMVEEGLRAV RQWLEASSQL
     EEASIYSRWE VEEDWCVSVL RSYQAEHGPD FPWSVGEDMS ADGRRQLALF LARKHLHNFE
     ATHCTPLPAQ HFQMPWHL
//
ID   BAG6_MOUSE              Reviewed;        1154 AA.
AC   Q9Z1R2; Q8SNA3;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Large proline-rich protein BAG6;
DE   AltName: Full=BAG family molecular chaperone regulator 6;
DE   AltName: Full=BCL2-associated athanogene 6;
DE            Short=BAG-6;
DE            Short=BAG6;
DE   AltName: Full=HLA-B-associated transcript 3;
DE   AltName: Full=Protein Scythe;
GN   Name=Bag6; Synonyms=Bat3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129;
RX   PubMed=14656967; DOI=10.1101/gr.1736803;
RA   Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
RA   Campbell R.D., Hood L.;
RT   "Analysis of the gene-dense major histocompatibility complex class III
RT   region and its comparison to mouse.";
RL   Genome Res. 13:2621-2636(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 318-1154.
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-986 AND SER-995, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=16287848; DOI=10.1128/MCB.25.23.10329-10337.2005;
RA   Desmots F., Russell H.R., Lee Y., Boyd K., McKinnon P.J.;
RT   "The reaper-binding protein scythe modulates apoptosis and
RT   proliferation during mammalian development.";
RL   Mol. Cell. Biol. 25:10329-10337(2005).
RN   [6]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=17403783; DOI=10.1101/gad.1534107;
RA   Sasaki T., Gan E.C., Wakeham A., Kornbluth S., Mak T.W., Okada H.;
RT   "HLA-B-associated transcript 3 (Bat3)/Scythe is essential for p300-
RT   mediated acetylation of p53.";
RL   Genes Dev. 21:848-861(2007).
RN   [7]
RP   FUNCTION, INTERACTION WITH AIFM1, AND SUBCELLULAR LOCATION.
RX   PubMed=18056262; DOI=10.1074/jbc.M706419200;
RA   Desmots F., Russell H.R., Michel D., McKinnon P.J.;
RT   "Scythe regulates apoptosis-inducing factor stability during
RT   endoplasmic reticulum stress-induced apoptosis.";
RL   J. Biol. Chem. 283:3264-3271(2008).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH HSPA2.
RX   PubMed=18678708; DOI=10.1083/jcb.200802113;
RA   Sasaki T., Marcon E., McQuire T., Arai Y., Moens P.B., Okada H.;
RT   "Bat3 deficiency accelerates the degradation of Hsp70-2/HspA2 during
RT   spermatogenesis.";
RL   J. Cell Biol. 182:449-458(2008).
RN   [9]
RP   FUNCTION.
RX   PubMed=20713601; DOI=10.1083/jcb.200908092;
RA   Minami R., Hayakawa A., Kagawa H., Yanagi Y., Yokosawa H.,
RA   Kawahara H.;
RT   "BAG-6 is essential for selective elimination of defective proteasomal
RT   substrates.";
RL   J. Cell Biol. 190:637-650(2010).
CC   -!- FUNCTION: Chaperone that plays a key role in various processes
CC       such as apoptosis, insertion of tail-anchored (TA) membrane
CC       proteins to the endoplasmic reticulum membrane and regulation of
CC       chromatin. Acts in part by regulating stability of proteins and
CC       their degradation by the proteasome. Key component of the
CC       BAG6/BAT3 complex, a cytosolic multiprotein complex involved in
CC       the post-translational delivery of tail-anchored (TA) membrane
CC       proteins to the endoplasmic reticulum. TA membrane proteins, also
CC       named type II transmembrane proteins, contain a single C-terminal
CC       transmembrane region. BAG6/BAT3 acts by facilitating TA membrane
CC       proteins capture by ASNA1/TRC40: it is recruited to ribosomes
CC       synthesizing membrane proteins, interacts with the transmembrane
CC       region of newly released TA proteins and transfers them to
CC       ASNA1/TRC40 for targeting to the endoplasmic reticulum membrane
CC       (By similarity). Participates in endoplasmic reticulum stress-
CC       induced apoptosis via its interaction with AIFM1/AIF by regulating
CC       AIFM1/AIF stability and preventing its degradation. Also required
CC       during spermatogenesis for synaptonemal complex assembly via its
CC       interaction with HSPA2, by inhibiting polyubiquitination and
CC       subsequent proteosomal degradation of HSPA2. Required for
CC       selective ubiquitin-mediated degradation of defective nascent
CC       chain polypeptides by the proteasome. In this context, may play a
CC       role in immuno-proteasomes to generate antigenic peptides via
CC       targeted degradation, thereby playing a role in antigen
CC       presentation in immune response. Also involved in DNA damage-
CC       induced apoptosis: following DNA damage, accumulates in the
CC       nucleus and forms a complex with p300/EP300, enhancing p300/EP300-
CC       mediated p53/TP53 acetylation leading to increase p53/TP53
CC       transcriptional activity. When nuclear, may also act as a
CC       component of some chromatin regulator complex that regulates
CC       histone 3 'Lys-4' dimethylation (H3K4me2).
CC   -!- SUBUNIT: Component of the BAT3 complex, at least composed of
CC       BAG6/BAT3, UBL4A and GET3/TRC35. Interacts with CTCFL and
CC       p300/EP300. Interacts with ricin A chain (By similarity).
CC       Interacts with AIFM1 and HSPA2.
CC   -!- INTERACTION:
CC       O35305:Tnfrsf11a; NbExp=2; IntAct=EBI-644645, EBI-647362;
CC       P70196:Traf6; NbExp=2; IntAct=EBI-644645, EBI-448028;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus (By similarity).
CC       Note=The C-terminal fragment generated by caspase-3 is cytoplasmic
CC       (By similarity).
CC   -!- PTM: Cleavage by caspase-3 releases a C-terminal peptide that
CC       plays a role in ricin-induced apoptosis (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Lethality associated with pronounced
CC       developmental defects in the lung, kidney and brain. Lethality is
CC       either embryonic consecutive to abnormal brain development or
CC       perinatal associated with pronounced developmental defects in the
CC       lung and kidney. These developmental defects were associated with
CC       widespread aberrant apoptosis and proliferation. Lethality can be
CC       partially rescued in an ICR genetic background: mice are slightly
CC       smaller in size than their wild-type counterparts and show
CC       impaired genotoxic stress responses.
CC   -!- SIMILARITY: Contains 1 ubiquitin-like domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF109719; AAC82479.1; -; Genomic_DNA.
DR   EMBL; CR974444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC026647; AAH26647.1; -; mRNA.
DR   IPI; IPI00130381; -.
DR   RefSeq; NP_476512.1; NM_057171.1.
DR   UniGene; Mm.203962; -.
DR   UniGene; Mm.471614; -.
DR   ProteinModelPortal; Q9Z1R2; -.
DR   SMR; Q9Z1R2; 17-101.
DR   IntAct; Q9Z1R2; 10.
DR   STRING; Q9Z1R2; -.
DR   PhosphoSite; Q9Z1R2; -.
DR   PRIDE; Q9Z1R2; -.
DR   Ensembl; ENSMUST00000025250; ENSMUSP00000025250; ENSMUSG00000024392.
DR   GeneID; 224727; -.
DR   KEGG; mmu:224727; -.
DR   UCSC; uc008cgb.1; mouse.
DR   CTD; 224727; -.
DR   MGI; MGI:1919439; Bag6.
DR   GeneTree; ENSGT00390000016199; -.
DR   HOGENOM; HBG444880; -.
DR   HOVERGEN; HBG002193; -.
DR   InParanoid; Q9Z1R2; -.
DR   OMA; PQRENAS; -.
DR   OrthoDB; EOG4255VB; -.
DR   PhylomeDB; Q9Z1R2; -.
DR   NextBio; 377324; -.
DR   ArrayExpress; Q9Z1R2; -.
DR   Bgee; Q9Z1R2; -.
DR   CleanEx; MM_BAT3; -.
DR   Genevestigator; Q9Z1R2; -.
DR   GermOnline; ENSMUSG00000024392; Mus musculus.
DR   GO; GO:0071818; C:BAT3 complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0030544; F:Hsp70 protein binding; IPI:UniProtKB.
DR   GO; GO:0031593; F:polyubiquitin binding; IDA:UniProtKB.
DR   GO; GO:0070628; F:proteasome binding; IDA:UniProtKB.
DR   GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR   GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:UniProtKB.
DR   GO; GO:0070059; P:apoptosis in response to endoplasmic reticulum stress; IMP:UniProtKB.
DR   GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0042771; P:DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis; ISS:UniProtKB.
DR   GO; GO:0009790; P:embryo development; IMP:UniProtKB.
DR   GO; GO:0018393; P:internal peptidyl-lysine acetylation; ISS:UniProtKB.
DR   GO; GO:0001822; P:kidney development; IMP:UniProtKB.
DR   GO; GO:0030324; P:lung development; IMP:UniProtKB.
DR   GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR   GO; GO:0007130; P:synaptonemal complex assembly; IMP:UniProtKB.
DR   GO; GO:0071816; P:tail-anchored membrane protein insertion into ER membrane; ISS:UniProtKB.
DR   GO; GO:0006810; P:transport; IEA:UniProtKB-KW.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR   InterPro; IPR021925; DUF3538.
DR   InterPro; IPR000626; Ubiquitin.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019955; Ubiquitin_supergroup.
DR   Pfam; PF12057; DUF3538; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SMART; SM00213; UBQ; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Apoptosis; Chaperone; Chromatin regulator; Cytoplasm;
KW   Differentiation; Nucleus; Phosphoprotein; Repeat; Spermatogenesis;
KW   Transport.
FT   CHAIN         1   1154       Large proline-rich protein BAG6.
FT                                /FTId=PRO_0000114898.
FT   DOMAIN       17     92       Ubiquitin-like.
FT   REPEAT      237    271       1.
FT   REPEAT      416    444       2.
FT   REPEAT      597    624       3.
FT   REPEAT      630    658       4.
FT   REGION      237    658       4 X 29 AA approximate repeats.
FT   COMPBIAS    196    274       Pro-rich.
FT   COMPBIAS    395    720       Pro-rich.
FT   COMPBIAS    564    610       Ala-rich.
FT   SITE       1023   1024       Cleavage; by caspase-3 (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES     108    108       Phosphothreonine (By similarity).
FT   MOD_RES     986    986       Phosphoserine.
FT   MOD_RES     995    995       Phosphoserine.
FT   MOD_RES    1061   1061       Phosphoserine (By similarity).
FT   MOD_RES    1064   1064       Phosphotyrosine (By similarity).
FT   MOD_RES    1103   1103       Phosphoserine (By similarity).
FT   MOD_RES    1139   1139       Phosphoserine (By similarity).
FT   CONFLICT    528    528       Missing (in Ref. 3; AAH26647).
FT   CONFLICT   1012   1012       P -> S (in Ref. 3; AAH26647).
SQ   SEQUENCE   1154 AA;  121037 MW;  7F3FD14DF5AC1211 CRC64;
     MEPSDSASTA MEEPDSLEVL VKTLDSQTRT FIVGAQMNVK EFKEHIAASV SIPSEKQRLI
     YQGRVLQDDK KLQEYNVGGK VIHLVERAPP QTQLPSGASS GTGSASATHG GAPLPGTRGP
     GASVHDRNAN SYVMVGTFNL PSDGSAVDVH INMEQAPIQS EPRVRLVMAQ HMIRDIQTLL
     SRMECRGGTQ AQASQPPPQT PQTVASETVA LNSQTSEPVE SEAPPREPME SEEMEERPPT
     QTPELAPSGP APAGPAPAGP APAPETNAPN HPSPAEHVEV LQELQRLQRR LQPFLQRYCE
     VLGAAATTDY NNNHEGREED QRLINLVGES LRLLGNTFVA LSDLRCNLAC APPRHLHVVR
     PMSHYTTPMV LQQAAIPIQI NVGTTVTMTG NGARPPPAPG AEAATPGSAQ ATSLPPSSTT
     VDSSTEGAPP PGPAPPPASS HPRVIRISHQ SVEPVVMMHM NIQDSGAQPG GVPSAPTGPL
     GPPGHGQTLG QQVPGFPTAP TRVVIARPTP PQARPSHPGG PPVSGALQGA GLGTNTSLAQ
     MVSGLVGQLL MQPVLVAQGT PGMAQAQAQA QAQAQAQAQA PAPAPAPAPA PATASASAGT
     TNTATTAGPA PGGPAQPPPP QPSAADLQFS QLLGNLLGPA GPGAGGPGMA SPTITVAMPG
     VPAFLQGMTD FLQASQTAPP PPPPPPPPPP APEQQSTPPP GSPSGGTASP GGLGPESLPP
     EFFTSVVQGV LSSLLGSLGA RAGSSESIAA FIQRLSGSSN IFEPGADGAL GFFGALLSLL
     CQNFSMVDVV MLLHGHFQPL QRLQPQLRSF FHQHYLGGQE PTPSNIRMAT HTLITGLEEY
     VRESFSLVQV QPGVDIIRTN LEFLQEQFNS IAAHVLHCTD SGFGARLLEL CNQGLFECLA
     LNLHCLGGQQ MELAAVINGR IRRMSRGVNP SLVSWLTTMM GLRLQVVLEH MPVGPDAILR
     YVRRVGDPPQ TLPEEPMEVQ GAERTSPEPQ RENASPAPGT TAEEAMSRGP PPAPEGGSRD
     EQDGASADAE PWAAAVPPEW VPIIQQDIQS QRKVKPQPPL SDAYLSGMPA KRRKTMQGEG
     PQLLLSEAVS RAAKAAGARP LTSPESLSRD LEAPEVQESY RQQLRSDIQK RLQEDPNYSP
     QRFPNAHRAF ADDP
//
ID   GRP1_MOUSE              Reviewed;         795 AA.
AC   Q9Z1S3; Q3URH0; Q3V401; Q8BQP6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=RAS guanyl-releasing protein 1;
DE   AltName: Full=Calcium and DAG-regulated guanine nucleotide exchange factor II;
DE            Short=CalDAG-GEFII;
DE   AltName: Full=Ras guanyl-releasing protein;
GN   Name=Rasgrp1; Synonyms=Rasgrp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6 X C3H; TISSUE=Brain;
RX   PubMed=10087292; DOI=10.1007/s003359901001;
RA   Bottorff D.A., Ebinu J.O., Stone J.C.;
RT   "RasGRP, a Ras activator: mouse and human cDNA sequences and
RT   chromosomal positions.";
RL   Mamm. Genome 10:358-361(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain, Corpus striatum, and Hippocampus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Fetal brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, MUTAGENESIS OF ARG-271, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=9819387;
RA   Tognon C.E., Kirk H.E., Passmore L.A., Whitehead I.P., Der C.J.,
RA   Kay R.J.;
RT   "Regulation of RasGRP via a phorbol ester-responsive C1 domain.";
RL   Mol. Cell. Biol. 18:6995-7008(1998).
RN   [6]
RP   DISRUPTION PHENOTYPE, FUNCTION IN T-CELL ACTIVATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=11017103; DOI=10.1038/79766;
RA   Dower N.A., Stang S.L., Bottorff D.A., Ebinu J.O., Dickie P.,
RA   Ostergaard H.L., Stone J.C.;
RT   "RasGRP is essential for mouse thymocyte differentiation and TCR
RT   signaling.";
RL   Nat. Immunol. 1:317-321(2000).
RN   [7]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=12433368; DOI=10.1016/S1074-7613(02)00451-X;
RA   Priatel J.J., Teh S.-J., Dower N.A., Stone J.C., Teh H.-S.;
RT   "RasGRP1 transduces low-grade TCR signals which are critical for T
RT   cell development, homeostasis, and differentiation.";
RL   Immunity 17:617-627(2002).
RN   [8]
RP   FUNCTION.
RX   PubMed=12932358; DOI=10.1016/S1074-7613(03)00209-7;
RA   Layer K., Lin G., Nencioni A., Hu W., Schmucker A., Antov A.N., Li X.,
RA   Takamatsu S., Chevassut T., Dower N.A., Stang S.L., Beier D.,
RA   Buhlmann J., Bronson R.T., Elkon K.B., Stone J.C., Van Parijs L.,
RA   Lim B.;
RT   "Autoimmunity as the consequence of a spontaneous mutation in
RT   Rasgrp1.";
RL   Immunity 19:243-255(2003).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY, AND
RP   INDUCTION BY TPA.
RX   PubMed=14532295; DOI=10.1074/jbc.M308240200;
RA   Rambaratsingh R.A., Stone J.C., Blumberg P.M., Lorenzo P.S.;
RT   "RasGRP1 represents a novel non-protein kinase C phorbol ester
RT   signaling pathway in mouse epidermal keratinocytes.";
RL   J. Biol. Chem. 278:52792-52801(2003).
RN   [10]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=12538669;
RA   Norment A.M., Bogatzki L.Y., Klinger M.B., Ojala E.W., Bevan M.J.,
RA   Kay R.J.;
RT   "Transgenic expression of RasGRP1 induces the maturation of double-
RT   negative thymocytes and enhances the production of CD8 single-positive
RT   thymocytes.";
RL   J. Immunol. 170:1141-1149(2003).
RN   [11]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12845332; DOI=10.1038/nature01806;
RA   Bivona T.G., Perez De Castro I., Ahearn I.M., Grana T.M., Chiu V.K.,
RA   Lockyer P.J., Cullen P.J., Pellicer A., Cox A.D., Philips M.R.;
RT   "Phospholipase Cgamma activates Ras on the Golgi apparatus by means of
RT   RasGRP1.";
RL   Nature 424:694-698(2003).
RN   [12]
RP   FUNCTION IN B-CELLS, TISSUE SPECIFICITY, AND MUTAGENESIS OF ARG-271.
RX   PubMed=14970203; DOI=10.1074/jbc.M314273200;
RA   Guilbault B., Kay R.J.;
RT   "RasGRP1 sensitizes an immature B cell line to antigen receptor-
RT   induced apoptosis.";
RL   J. Biol. Chem. 279:19523-19530(2004).
RN   [13]
RP   FUNCTION.
RX   PubMed=16301621;
RA   Coughlin J.J., Stang S.L., Dower N.A., Stone J.C.;
RT   "RasGRP1 and RasGRP3 regulate B cell proliferation by facilitating B
RT   cell receptor-Ras signaling.";
RL   J. Immunol. 175:7179-7184(2005).
RN   [14]
RP   FUNCTION.
RX   PubMed=15829980; DOI=10.1038/sj.onc.1208334;
RA   Klinger M.B., Guilbault B., Goulding R.E., Kay R.J.;
RT   "Deregulated expression of RasGRP1 initiates thymic lymphomagenesis
RT   independently of T-cell receptors.";
RL   Oncogene 24:2695-2704(2005).
RN   [15]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=16849453;
RA   Priatel J.J., Chen X., Dhanji S., Abraham N., Teh H.-S.;
RT   "RasGRP1 transmits prodifferentiation TCR signaling that is crucial
RT   for CD4 T cell development.";
RL   J. Immunol. 177:1470-1480(2006).
RN   [16]
RP   DIACYLGLYCEROL-BINDING, AND SUBCELLULAR LOCATION.
RX   PubMed=17523924; DOI=10.1042/BJ20070294;
RA   Johnson J.E., Goulding R.E., Ding Z., Partovi A., Anthony K.V.,
RA   Beaulieu N., Tazmini G., Cornell R.B., Kay R.J.;
RT   "Differential membrane binding and diacylglycerol recognition by C1
RT   domains of RasGRPs.";
RL   Biochem. J. 406:223-236(2007).
RN   [17]
RP   FUNCTION.
RX   PubMed=17210708; DOI=10.1158/0008-5472.CAN-06-3080;
RA   Oki-Idouchi C.E., Lorenzo P.S.;
RT   "Transgenic overexpression of RasGRP1 in mouse epidermis results in
RT   spontaneous tumors of the skin.";
RL   Cancer Res. 67:276-280(2007).
RN   [18]
RP   FUNCTION IN MAST CELLS ACTIVATION, AND TISSUE SPECIFICITY.
RX   PubMed=17190838; DOI=10.1084/jem.20061598;
RA   Liu Y., Zhu M., Nishida K., Hirano T., Zhang W.;
RT   "An essential role for RasGRP1 in mast cell function and IgE-mediated
RT   allergic response.";
RL   J. Exp. Med. 204:93-103(2007).
RN   [19]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=17675473;
RA   Priatel J.J., Chen X., Zenewicz L.A., Shen H., Harder K.W.,
RA   Horwitz M.S., Teh H.-S.;
RT   "Chronic immunodeficiency in mice lacking RasGRP1 results in CD4 T
RT   cell immune activation and exhaustion.";
RL   J. Immunol. 179:2143-2152(2007).
RN   [20]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17567957; DOI=10.1091/mbc.E06-10-0932;
RA   Beaulieu N., Zahedi B., Goulding R.E., Tazmini G., Anthony K.V.,
RA   Omeis S.L., de Jong D.R., Kay R.J.;
RT   "Regulation of RasGRP1 by B cell antigen receptor requires
RT   cooperativity between three domains controlling translocation to the
RT   plasma membrane.";
RL   Mol. Biol. Cell 18:3156-3168(2007).
CC   -!- FUNCTION: Functions as a diacylglycerol (DAG)-regulated nucleotide
CC       exchange factor specifically activating Ras through the exchange
CC       of bound GDP for GTP. Activates the Erk/MAP kinase cascade.
CC       Couples T-lymphocytes and B-lymphocytes antigen receptors to the
CC       activation of Ras. Hence, regulates T-cells and B-cells
CC       development, homeostasis and differentiation. Functions also in
CC       FcERI-evoked degranulation and cytokine secretion by mast cells,
CC       regulating allergic responses. May also function in other cell
CC       types differentiation. Proto-oncogene which promotes T-cell
CC       lymphomagenesis when its expression is deregulated.
CC   -!- ENZYME REGULATION: Probably regulated by calcium. Regulated by PLC
CC       gamma, DGKA, DGKZ and by F-actin polymerization (By similarity).
CC   -!- SUBUNIT: Forms a signaling complex with DGKZ and HRAS. Interacts
CC       with F-actin. Interacts with SKAP1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol (By similarity). Cell
CC       membrane; Peripheral membrane protein (By similarity). Golgi
CC       apparatus membrane; Peripheral membrane protein. Endoplasmic
CC       reticulum membrane; Peripheral membrane protein (By similarity).
CC       Note=Found both in the cytosol and associated with membranes.
CC       Relocalization to the cell membrane upon activation is F-actin-
CC       dependent (By similarity). Translocates to the Golgi in response
CC       to phorbol ester or nerve growth factor. Localizes to somata and
CC       dendrites but not to axons of hippocampal pyramidal cells (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Detected in spleen and thymus. Expressed by
CC       mature thymocytes and to a lower extent by bone marrow-derived
CC       mast cells (at protein level). Detected in B-cells and
CC       keratinocytes (at protein level).
CC   -!- INDUCTION: Up-regulated at the double-negative to double-positive
CC       transition during thymocyte development. Down-regulated by 12-O-
CC       tetradecanoylphorbol-13-acetate (TPA).
CC   -!- DOMAIN: The phorbol-ester/DAG-type zinc finger is the principal
CC       mediator of the targeting to membranes and is required for
CC       functional activation through DAG-binding.
CC   -!- DISRUPTION PHENOTYPE: Mice fail to mount anaphylactic allergic
CC       reactions and display chronic T-cell immunodeficiencies. Lag
CC       (lymphoproliferation-autoimmunity-glomerulonephritis) mice do not
CC       express Rasgrp1 and display a systemic lupus erythematosus-like
CC       phenotype.
CC   -!- SIMILARITY: Belongs to the RASGRP family.
CC   -!- SIMILARITY: Contains 2 EF-hand domains.
CC   -!- SIMILARITY: Contains 1 N-terminal Ras-GEF domain.
CC   -!- SIMILARITY: Contains 1 phorbol-ester/DAG-type zinc finger.
CC   -!- SIMILARITY: Contains 1 Ras-GEF domain.
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DR   EMBL; AF106070; AAC97348.1; -; mRNA.
DR   EMBL; AK028308; BAE20439.1; -; mRNA.
DR   EMBL; AK047613; BAC33100.1; -; mRNA.
DR   EMBL; AK141524; BAE24718.1; -; mRNA.
DR   EMBL; AL844579; CAM17832.1; -; Genomic_DNA.
DR   EMBL; AL928959; CAM17832.1; JOINED; Genomic_DNA.
DR   EMBL; AL928959; CAM26780.1; -; Genomic_DNA.
DR   EMBL; AL844579; CAM26780.1; JOINED; Genomic_DNA.
DR   EMBL; BC057120; AAH57120.1; -; mRNA.
DR   EMBL; BC057341; AAH57341.1; -; mRNA.
DR   IPI; IPI00130414; -.
DR   RefSeq; NP_035376.1; NM_011246.2.
DR   UniGene; Mm.42150; -.
DR   HSSP; P28867; 1PTQ.
DR   ProteinModelPortal; Q9Z1S3; -.
DR   SMR; Q9Z1S3; 204-436, 473-591.
DR   STRING; Q9Z1S3; -.
DR   PhosphoSite; Q9Z1S3; -.
DR   PRIDE; Q9Z1S3; -.
DR   Ensembl; ENSMUST00000028823; ENSMUSP00000028823; ENSMUSG00000027347.
DR   Ensembl; ENSMUST00000102534; ENSMUSP00000099593; ENSMUSG00000027347.
DR   GeneID; 19419; -.
DR   KEGG; mmu:19419; -.
DR   UCSC; uc008lrl.1; mouse.
DR   CTD; 19419; -.
DR   MGI; MGI:1314635; Rasgrp1.
DR   eggNOG; roNOG05075; -.
DR   GeneTree; ENSGT00510000046358; -.
DR   HOGENOM; HBG403023; -.
DR   HOVERGEN; HBG007513; -.
DR   InParanoid; Q9Z1S3; -.
DR   OMA; EESKDRT; -.
DR   OrthoDB; EOG49ZXNS; -.
DR   NextBio; 296563; -.
DR   ArrayExpress; Q9Z1S3; -.
DR   Bgee; Q9Z1S3; -.
DR   CleanEx; MM_RASGRP1; -.
DR   Genevestigator; Q9Z1S3; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   InterPro; IPR020454; DAG/PE-bd.
DR   InterPro; IPR011992; EF-hand-like_dom.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR018249; EF_HAND_2.
DR   InterPro; IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
DR   InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR   InterPro; IPR008937; Ras_GEF.
DR   InterPro; IPR001895; RasGRF_CDC25.
DR   Gene3D; G3DSA:1.10.238.10; EF-Hand_type; 2.
DR   Gene3D; G3DSA:1.10.840.10; RasGRF_CDC25; 1.
DR   PANTHER; PTHR23113; Ras_GEF; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF00617; RasGEF; 1.
DR   PRINTS; PR00008; DAGPEDOMAIN.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00229; RasGEFN; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 3.
DR   PROSITE; PS00720; RASGEF; FALSE_NEG.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50212; RASGEF_NTER; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   Calcium; Cell membrane; Coiled coil; Cytoplasm; Differentiation;
KW   Endoplasmic reticulum; Golgi apparatus;
KW   Guanine-nucleotide releasing factor; Membrane; Metal-binding;
KW   Phosphoprotein; Proto-oncogene; Repeat; Zinc; Zinc-finger.
FT   CHAIN         1    795       RAS guanyl-releasing protein 1.
FT                                /FTId=PRO_0000316979.
FT   DOMAIN       53    176       N-terminal Ras-GEF.
FT   DOMAIN      205    436       Ras-GEF.
FT   DOMAIN      470    505       EF-hand 1.
FT   DOMAIN      497    532       EF-hand 2.
FT   CA_BIND     483    494       1 (Potential).
FT   CA_BIND     510    521       2 (Potential).
FT   ZN_FING     541    591       Phorbol-ester/DAG-type.
FT   REGION       57    110       Ras exchanger motif region; required for
FT                                transforming activity.
FT   REGION      686    694       Suppress the PT region-mediated
FT                                translocation to plasma membrane.
FT   REGION      717    795       PT region; mediates the BCR-dependent
FT                                translocation to plasma membrane.
FT   COILED      738    779       Potential.
FT   MOD_RES     184    184       Phosphothreonine; by PKC (By similarity).
FT   MOD_RES     694    694       Phosphoserine (By similarity).
FT   MUTAGEN     271    271       R->E: Loss of function and transforming
FT                                activity.
FT   CONFLICT    171    171       T -> R (in Ref. 2; BAE24718).
FT   CONFLICT    472    472       Q -> K (in Ref. 2; BAE20439).
FT   CONFLICT    485    485       D -> E (in Ref. 2; BAE20439).
FT   CONFLICT    501    501       S -> T (in Ref. 2; BAE20439).
FT   CONFLICT    520    520       D -> H (in Ref. 2; BAE20439).
FT   CONFLICT    768    768       K -> R (in Ref. 2; BAC33100).
SQ   SEQUENCE   795 AA;  90304 MW;  E2096D985DFB79A0 CRC64;
     MGTLGKAREA PRKPCHGSRA GPKARLEAKS TNSPLPAQPS LAQITQFRMM VSLGHLAKGA
     SLDDLIDSCI QSFDADGNLC RNNQLLQVML TMHRIIISSA ELLQKVMNLY KDALEKNSPG
     VCLKICYFVR YWITEFWIMF KMDASLTSTM EEFQDLVKAN GEETHCHLID TTQINSRDWS
     RKLTQRIKSN TSKKRKVSLL FDHLEPEELS EHLTYLEFKS FRRISFSDYQ NYLVNSCVKE
     NPTMERSIAL CNGISQWVQL MVLSRPTPQL RAEVFIKFIH VAQKLHQLQN FNTLMAVIGG
     LCHSSISRLK ETSSHVPHEI NKVLGEMTEL LSSCRNYDNY RRAYGECTHF KIPILGVHLK
     DLISLYEAMP DYLEDGKVNV QKLLALYNHI NELVQLQEMA PPLDANKDLV HLLTLSLDLY
     YTEDEIYELS YAREPRNHRA PPLTPSKPPV VVDWASGVSP KPDPKTISKH VQRMVDSVFK
     NYDLDQDGYI SQEEFEKIAA SFPFSFCVMD KDREGLISRD EITAYFMRAS SIYSKLGLGF
     PHNFQETTYL KPTFCDNCAG FLWGVIKQGY RCKDCGMNCH KQCKDLVVFE CKKRIKSPAI
     STENISSVVP MSTLCPLGTK DLLHAPEEGS FIFQNGEIVD HSEESKDRTI MLLGVSSQKI
     SVRLKRTVAH KSTQTESFPW VGGETTPGHF VLSSPRKSAQ GALYVHSPAS PCPSPALVRK
     RAFVKWENKE SLIKPKPELH LRLRTYQELE QEINTLKADN DALKIQLKYA QKKIESLQLG
     KSNHVLAQMD HGDSA
//
ID   FYV1_MOUSE              Reviewed;        2097 AA.
AC   Q9Z1T6; Q3TNE4; Q3UTT6; Q69ZU1; Q9CU94;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   08-MAR-2011, entry version 97.
DE   RecName: Full=1-phosphatidylinositol-3-phosphate 5-kinase;
DE            Short=Phosphatidylinositol-3-phosphate 5-kinase;
DE            EC=2.7.1.150;
DE   AltName: Full=FYVE finger-containing phosphoinositide kinase;
DE   AltName: Full=PIKfyve;
DE   AltName: Full=Phosphatidylinositol-3-phosphate 5-kinase type III;
DE            Short=PIPkin-III;
DE            Short=Type III PIP kinase;
DE   AltName: Full=p235;
GN   Name=Pikfyve; Synonyms=Kiaa0981, Pip5k3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND CHARACTERIZATION.
RC   TISSUE=Adipose tissue;
RX   MEDLINE=99078000; PubMed=9858586;
RA   Shisheva A., Sbrissa D., Ikonomov O.;
RT   "Cloning, characterization, and expression of a novel Zn2+-binding
RT   FYVE finger-containing phosphoinositide kinase in insulin-sensitive
RT   cells.";
RL   Mol. Cell. Biol. 19:623-634(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Pancreatic islet;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Ovary, Spleen, and Uterus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   CATALYTIC ACTIVITY.
RX   PubMed=10567352; DOI=10.1074/jbc.274.48.33905;
RA   McEwen R.K., Dove S.K., Cooke F.T., Painter G.F., Holmes A.B.,
RA   Shisheva A., Ohya Y., Parker P.J., Michell R.H.;
RT   "Complementation analysis in PtdInsP kinase-deficient yeast mutants
RT   demonstrates that Schizosaccharomyces pombe and murine Fab1p
RT   homologues are phosphatidylinositol 3-phosphate 5-kinases.";
RL   J. Biol. Chem. 274:33905-33912(1999).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=17956977; DOI=10.1073/pnas.0702275104;
RA   Zhang Y., Zolov S.N., Chow C.Y., Slutsky S.G., Richardson S.C.,
RA   Piper R.C., Yang B., Nau J.J., Westrick R.J., Morrison S.J.,
RA   Meisler M.H., Weisman L.S.;
RT   "Loss of Vac14, a regulator of the signaling lipid
RT   phosphatidylinositol 3,5-bisphosphate, results in neurodegeneration in
RT   mice.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:17518-17523(2007).
RN   [7]
RP   IDENTIFICATION IN THE PI(3,5)P2 REGULATORY COMPLEX, FUNCTION, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=19037259; DOI=10.1038/emboj.2008.248;
RA   Jin N., Chow C.Y., Liu L., Zolov S.N., Bronson R., Davisson M.,
RA   Petersen J.L., Zhang Y., Park S., Duex J.E., Goldowitz D.,
RA   Meisler M.H., Weisman L.S.;
RT   "VAC14 nucleates a protein complex essential for the acute
RT   interconversion of PI3P and PI(3,5)P(2) in yeast and mouse.";
RL   EMBO J. 27:3221-3234(2008).
CC   -!- FUNCTION: The PI(3,5)P2 regulatory complex regulates both the
CC       synthesis and turnover of phosphatidylinositol-3,5-bisphosphate
CC       (PtdIns(3,5)P2). Catalyzes the phosphorylation of
CC       phosphatidylinositol-3-phosphate on the fifth hydroxyl of the myo-
CC       inositol ring, to form phosphatidylinositol-3,5-bisphosphate.
CC       Required for endocytic-vacuolar pathway and nuclear migration. The
CC       product of the reaction it catalyzes functions as an important
CC       regulator of vacuole homeostasis perhaps by controlling membrane
CC       flux to and/or from the vacuole.
CC   -!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 3-
CC       phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate.
CC   -!- SUBUNIT: Component of the PI(3,5)P2 regulatory complex/PAS
CC       complex, at least composed of PIKFYVE, FIG4 and VAC14. VAC14
CC       nucleates the assembly of the complex and serves as a scaffold.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane; Peripheral
CC       membrane protein. Endosome membrane (By similarity).
CC       Note=Associated with vesicle structures. Displays a peripheral
CC       vesicular punctate pattern. Mainly associated with membranes of
CC       the late endocytic pathway (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=p235S;
CC         IsoId=Q9Z1T6-2; Sequence=Displayed;
CC       Name=2; Synonyms=p235L;
CC         IsoId=Q9Z1T6-1; Sequence=VSP_034953, VSP_034954;
CC       Name=3;
CC         IsoId=Q9Z1T6-3; Sequence=VSP_034955, VSP_034956;
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Contains 1 DEP domain.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 1 PIPK domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD10191.1; Type=Frameshift; Positions=Several;
CC       Sequence=BAB30626.3; Type=Erroneous initiation;
CC       Sequence=BAD32355.1; Type=Erroneous initiation;
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DR   EMBL; AF102777; AAD10191.1; ALT_FRAME; mRNA.
DR   EMBL; AK173077; BAD32355.1; ALT_INIT; mRNA.
DR   EMBL; AK017186; BAB30626.3; ALT_INIT; mRNA.
DR   EMBL; AK139116; BAE23894.1; -; mRNA.
DR   EMBL; AK165350; BAE38145.1; -; mRNA.
DR   IPI; IPI00130449; -.
DR   IPI; IPI00230618; -.
DR   IPI; IPI00874822; -.
DR   PIR; T18290; T18290.
DR   RefSeq; NP_035216.2; NM_011086.2.
DR   UniGene; Mm.38370; -.
DR   ProteinModelPortal; Q9Z1T6; -.
DR   SMR; Q9Z1T6; 147-218, 352-425, 630-866, 1818-2083.
DR   STRING; Q9Z1T6; -.
DR   PhosphoSite; Q9Z1T6; -.
DR   SWISS-2DPAGE; Q9Z1T6; -.
DR   PRIDE; Q9Z1T6; -.
DR   Ensembl; ENSMUST00000097707; ENSMUSP00000095314; ENSMUSG00000025949.
DR   Ensembl; ENSMUST00000114042; ENSMUSP00000109676; ENSMUSG00000025949.
DR   GeneID; 18711; -.
DR   KEGG; mmu:18711; -.
DR   CTD; 18711; -.
DR   MGI; MGI:1335106; Pikfyve.
DR   eggNOG; roNOG08866; -.
DR   GeneTree; ENSGT00580000081507; -.
DR   HOVERGEN; HBG005775; -.
DR   OrthoDB; EOG45755P; -.
DR   BRENDA; 2.7.1.68; 244.
DR   NextBio; 294793; -.
DR   Bgee; Q9Z1T6; -.
DR   Genevestigator; Q9Z1T6; -.
DR   GermOnline; ENSMUSG00000025949; Mus musculus.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR   GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase activity; IEA:EC.
DR   GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0044267; P:cellular protein metabolic process; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:InterPro.
DR   InterPro; IPR002423; Cpn60/TCP-1.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR002498; PInositol-4-P-5-kinase_core.
DR   InterPro; IPR016034; PInositol-4P-5-kinase_core_sub.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00118; Cpn60_TCP1; 1.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF01504; PIP5K; 1.
DR   SMART; SM00049; DEP; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00330; PIPKc; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS50186; DEP; 1.
DR   PROSITE; PS51455; PIPK; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Cytoplasmic vesicle;
KW   Endosome; Kinase; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Transferase; Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2   2097       1-phosphatidylinositol-3-phosphate 5-
FT                                kinase.
FT                                /FTId=PRO_0000185453.
FT   DOMAIN      365    440       DEP.
FT   DOMAIN     1757   2083       PIPK.
FT   ZN_FING     158    218       FYVE-type.
FT   REGION     1841   2097       Catalytic (By similarity).
FT   COMPBIAS   1222   1225       Poly-Ser.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES       8      8       Phosphoserine (By similarity).
FT   MOD_RES      20     20       Phosphoserine (By similarity).
FT   MOD_RES      34     34       Phosphothreonine (By similarity).
FT   MOD_RES      46     46       Phosphotyrosine (By similarity).
FT   MOD_RES      73     73       Phosphoserine (By similarity).
FT   MOD_RES      76     76       Phosphoserine (By similarity).
FT   MOD_RES      88     88       Phosphoserine (By similarity).
FT   MOD_RES     219    219       Phosphoserine (By similarity).
FT   MOD_RES     223    223       Phosphoserine (By similarity).
FT   MOD_RES     299    299       Phosphoserine (By similarity).
FT   MOD_RES     307    307       Phosphoserine.
FT   MOD_RES     318    318       Phosphoserine (By similarity).
FT   MOD_RES     323    323       Phosphoserine (By similarity).
FT   MOD_RES     329    329       Phosphoserine (By similarity).
FT   MOD_RES     352    352       Phosphoserine (By similarity).
FT   MOD_RES     449    449       Phosphoserine (By similarity).
FT   MOD_RES     452    452       Phosphoserine (By similarity).
FT   MOD_RES     454    454       Phosphoserine (By similarity).
FT   MOD_RES     457    457       Phosphoserine (By similarity).
FT   MOD_RES     475    475       Phosphoserine (By similarity).
FT   MOD_RES     477    477       Phosphothreonine (By similarity).
FT   MOD_RES     491    491       Phosphoserine (By similarity).
FT   MOD_RES     493    493       Phosphoserine (By similarity).
FT   MOD_RES    1154   1154       Phosphotyrosine (By similarity).
FT   MOD_RES    1525   1525       Phosphoserine (By similarity).
FT   MOD_RES    1543   1543       Phosphoserine (By similarity).
FT   MOD_RES    1548   1548       Phosphoserine (By similarity).
FT   MOD_RES    1713   1713       Phosphoserine (By similarity).
FT   MOD_RES    1753   1753       Phosphoserine (By similarity).
FT   MOD_RES    1771   1771       Phosphotyrosine (By similarity).
FT   VAR_SEQ     107    107       L -> LENTLPHPQEST (in isoform 2).
FT                                /FTId=VSP_034953.
FT   VAR_SEQ     490    545       Missing (in isoform 2).
FT                                /FTId=VSP_034954.
FT   VAR_SEQ     490    497       NSASPSKR -> SKFGFLML (in isoform 3).
FT                                /FTId=VSP_034955.
FT   VAR_SEQ     498   2097       Missing (in isoform 3).
FT                                /FTId=VSP_034956.
FT   CONFLICT    546    546       E -> K (in Ref. 1; AAD10191).
FT   CONFLICT    944    944       Q -> K (in Ref. 1; AAD10191).
FT   CONFLICT    994    995       QP -> HR (in Ref. 1; AAD10191).
FT   CONFLICT   1107   1107       R -> T (in Ref. 3; BAB30626).
FT   CONFLICT   1141   1141       L -> V (in Ref. 1; AAD10191).
FT   CONFLICT   1264   1264       S -> Y (in Ref. 1; AAD10191).
FT   CONFLICT   1996   1996       V -> E (in Ref. 1; AAD10191).
SQ   SEQUENCE   2097 AA;  236877 MW;  191A26607FD4A372 CRC64;
     MATDDKSSPT LDSANDLPRS PASPSHLTHF KPLTPDQDEP PFKSAYSSFV NLFRFNKERG
     EGGQGEQQSP SSSWASPQIP SRTQSVRSPV PYKKQLNEEL HRRSSVLDSR RKAEPACGGH
     DPRTAVQLRS LSTVLKRLKE IMEGKSQDSD LKQYWMPDSQ CKECYDCSEK FTTFRRRHHC
     RLCGQIFCSR CCNQEIPGKF MGYTGDLRAC TYCRKIALSY AHSTDSNSIG EDLNALSDST
     CSVSILDPSE PRTPVGSRKA SRNIFLEDDL AWQSLIHPDS SNSALSTRLV SVQEDAGKSP
     ARNRSASITN LSLDRSGSPM VPSYETSVSP QANRNYIRTE TTEDERKILL DSAQLKDLWK
     KICHHTSGME FQDHRYWLRT HPNCIVGKEL VNWLIRNGHI ATRAQAIAIG QAMVDGRWLD
     CVSHHDQLFR DEYALYRPLQ STEFSETPSP DSDSVNSVEG HSEPSWFKDI KFDDSDTEQI
     AEEGDDNLAN SASPSKRTSV SSFQSTVDSD SAASISLNVE LDNVNFHIKK PSKYPHVPPH
     PADQKEYLVS DTGGQQLSIS DAFIKESLFN RRVEEKSKEL PFTPLGWHHN NLELLREENE
     EKQAMERLLS ANHNHMMALL QQLLQNESLS SSWRDIIVSL VCQVVQTVRP DVKHQDDDMD
     IRQFVHIKKI PGGKKFDSVV VNGFVCTKNI AHKKMNSCIK NPKILLLKCS IEYLYREETK
     FTCIDPIVLQ EREFLKNYVQ RIVDVRPTLV LVEKTVSRIA QDMLLEHGIT LVINVKSQVL
     ERISRMTQGD LVVSMDQLLT KPHLGTCHKF YMQIFQLPNE QTKTLMFFEG CPQHLGCTIK
     LRGGSDYELA RVKEILIFMI CVAYHSQLEI SFLMDEFAMP PTLMQSPSFH LLTEGRGEEG
     ASQEQVSGSS LPQDPECPRE ALSSEDSTLL ESRTVLEKGE LDNQSIPQAV ASLKHQDYTT
     PTCPAGIPCA LFALVPESLL PLHMDQQDAV GNEQPETSQQ TDEQQDPKSQ MKAFRDPLQD
     DTGMYVTEEV TSSEDQRKTY ALTFKQELKD VILCISPVIT FREPFLLTEK GMRCSTRDYF
     PEQIYWSPLL NKEVKEMESR RKKQLLRDLS GLQGMNGSVQ AKSIQVLPSH ELVSTRIAEH
     LGDSQTLGRM LADYRARGGR IQSKHLDPFV HSKDASCTSG GKSGNKTESD EERGLIPSDV
     IWPTKVDCLN PANHQRLCVL FSSSSAQSSN APSACVSPWI VTMEFYGKND LTLGIFLERY
     CFRSSYQCPS MFCDTPMVHH IRRFVHGQGC VQIILKELDS PVPGYQHTIL TYSWCRICKQ
     VTPVVALSNE SWSMSFAKYL ELRFYGHQYT RRANAEPCGH SIHHDYHQYF SYNQMVASFS
     YSPIRLLEVC VPLPKIFIKR QAPLKVSLLQ DLKDFFQKVS QVYLAVDERL ASLKTDTFSK
     TREEKMEDIF AQKEMEEGEF KNWTEKMQAR LMSSSVDTPQ QLQSIFESLI AKKQSLCEVL
     QAWNSRLQDL FQQEKGRKRP SVPPSPGRLR QGEESKINAM DTSPRNISPG LHNGEKEDRF
     LTTLSSQSST SSTHLQLPTP PEALAEQVVG GPTDLDSASG SEDVFDGHLL GSTDSQVKEK
     STMKAIFANL LPGNSYNPIP FPFDPDKHYL MYEHERVPIA VCEKEPSSII AFALSCKEYR
     NALEELSKAT LRNSAEEGLP ANSALDNRPK SSSPIRLPEI SGGQTNRTVE AEPQPTKKAS
     GMLSFFRGTA GKSPDLSSQK RETLRGADSA YYQVGQAGKE GLESQGLEPQ DEVDGGDTQK
     KQLTNPHVEL QFSDANAKFY CRLYYAGEFH KMREVILGSS EEEFIRSLSH SSPWQARGGK
     SGAAFYATED DRFILKQMPR LEVQSFLDFA PHYFNYITNA VQQKRPTALA KILGVYRIGY
     KNSQNNTEKK LDLLVMENLF YGRKMAQVFD LKGSLRNRNV KTDTGKESCD VVLLDENLLK
     MVRDNPLYIR SHSKSVLRTS IHSDAHFLSS HLIIDYSLLV GRDDTSNELV VGIIDYIRTF
     TWDKKLEMVV KSTGILGGQG KMPTVVSPEL YRTRFCEAMD KYFLMVPDHW TGLDLNC
//
ID   AT12A_MOUSE             Reviewed;        1035 AA.
AC   Q9Z1W8; Q8VHY2;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 2.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Potassium-transporting ATPase alpha chain 2;
DE            EC=3.6.3.10;
DE   AltName: Full=Non-gastric H(+)/K(+) ATPase subunit alpha;
DE   AltName: Full=Proton pump;
GN   Name=Atp12a; Synonyms=Atp1al1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   MEDLINE=21585875; PubMed=11729223;
RA   Zhang W., Kuncewicz T., Higham S.C., Kone B.C.;
RT   "Structure, promoter analysis, and chromosomal localization of the
RT   murine H(+)/K(+)-ATPase alpha 2 subunit gene.";
RL   J. Am. Soc. Nephrol. 12:2554-2564(2001).
RN   [2]
RP   PROTEIN SEQUENCE OF 488-498; 624-636; 710-718 AND 755-785, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 868-981, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Skin;
RX   MEDLINE=99087400; PubMed=9872395; DOI=10.1016/S0014-5793(98)01483-5;
RA   Pestov N.B., Romanova L.G., Korneenko T.V., Egorov M.V., Kostina M.B.,
RA   Sverdlov V.E., Askari A., Shakhparonov M.I., Modyanov N.N.;
RT   "Ouabain-sensitive H,K-ATPase: tissue-specific expression of the
RT   mammalian genes encoding the catalytic alpha subunit.";
RL   FEBS Lett. 440:320-324(1998).
CC   -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the
CC       exchange of H(+) and K(+) ions across the plasma membrane.
CC       Responsible for potassium absorption in various tissues.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) + K(+)(Out) = ADP +
CC       phosphate + H(+)(Out) + K(+)(In).
CC   -!- SUBUNIT: Composed of two subunits: alpha (catalytic) and beta.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Found in skin, kidney and distal colon.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       (TC 3.A.3) family. Type IIC subfamily.
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DR   EMBL; AF350499; AAL68709.1; -; Genomic_DNA.
DR   EMBL; AF100169; AAD03421.1; -; mRNA.
DR   IPI; IPI00268145; -.
DR   UniGene; Mm.273271; -.
DR   ProteinModelPortal; Q9Z1W8; -.
DR   SMR; Q9Z1W8; 45-1035.
DR   STRING; Q9Z1W8; -.
DR   PhosphoSite; Q9Z1W8; -.
DR   PRIDE; Q9Z1W8; -.
DR   Ensembl; ENSMUST00000007340; ENSMUSP00000007340; ENSMUSG00000022229.
DR   MGI; MGI:1926943; Atp12a.
DR   GeneTree; ENSGT00560000076866; -.
DR   HOGENOM; HBG456486; -.
DR   HOVERGEN; HBG004298; -.
DR   InParanoid; Q9Z1W8; -.
DR   OrthoDB; EOG41C6VF; -.
DR   BRENDA; 3.6.3.10; 244.
DR   ArrayExpress; Q9Z1W8; -.
DR   Bgee; Q9Z1W8; -.
DR   Genevestigator; Q9Z1W8; -.
DR   GermOnline; ENSMUSG00000022229; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008900; F:hydrogen:potassium-exchanging ATPase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro.
DR   GO; GO:0055075; P:potassium ion homeostasis; IMP:MGI.
DR   InterPro; IPR023306; ATPase_cation_domN.
DR   InterPro; IPR008250; ATPase_P-typ_ATPase-assoc-dom.
DR   InterPro; IPR005775; ATPase_P-typ_cation-ex_asu_euk.
DR   InterPro; IPR006069; ATPase_P-typ_cation-exchng_asu.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR   InterPro; IPR023300; ATPase_P-typ_cyto_domA.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_domN.
DR   InterPro; IPR001757; ATPase_P-typ_ion-transptr.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom.
DR   InterPro; IPR005834; Dehalogen-like_hydro.
DR   InterPro; IPR023214; HAD-like_dom.
DR   Gene3D; G3DSA:2.70.150.10; ATPase_P-typ_cyto_domA; 1.
DR   Gene3D; G3DSA:3.40.1110.10; ATPase_P-typ_cyto_domN; 1.
DR   Gene3D; G3DSA:1.20.1110.10; ATPase_P-typ_TM_dom; 2.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00121; NAKATPASE.
DR   SMART; SM00831; Cation_ATPase_N; 1.
DR   SUPFAM; SSF81660; ATPase_cation_domN; 1.
DR   SUPFAM; SSF56784; HAD-like_dom; 1.
DR   TIGRFAMs; TIGR01106; ATPase-IIC_X-K; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 4.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Direct protein sequencing; Hydrogen ion transport;
KW   Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Potassium; Potassium transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1   1035       Potassium-transporting ATPase alpha chain
FT                                2.
FT                                /FTId=PRO_0000046261.
FT   TOPO_DOM      1     99       Cytoplasmic (Potential).
FT   TRANSMEM    100    120       Helical; (Potential).
FT   TOPO_DOM    121    142       Lumenal (Potential).
FT   TRANSMEM    143    163       Helical; (Potential).
FT   TOPO_DOM    164    299       Cytoplasmic (Potential).
FT   TRANSMEM    300    319       Helical; (Potential).
FT   TOPO_DOM    320    331       Lumenal (Potential).
FT   TRANSMEM    332    349       Helical; (Potential).
FT   TOPO_DOM    350    783       Cytoplasmic (Potential).
FT   TRANSMEM    784    803       Helical; (Potential).
FT   TOPO_DOM    804    813       Lumenal (Potential).
FT   TRANSMEM    814    834       Helical; (Potential).
FT   TOPO_DOM    835    854       Cytoplasmic (Potential).
FT   TRANSMEM    855    877       Helical; (Potential).
FT   TOPO_DOM    878    929       Lumenal (Potential).
FT   TRANSMEM    930    949       Helical; (Potential).
FT   TOPO_DOM    950    963       Cytoplasmic (Potential).
FT   TRANSMEM    964    982       Helical; (Potential).
FT   TOPO_DOM    983    997       Lumenal (Potential).
FT   TRANSMEM    998   1018       Helical; (Potential).
FT   TOPO_DOM   1019   1035       Cytoplasmic (Potential).
FT   ACT_SITE    387    387       4-aspartylphosphate intermediate (By
FT                                similarity).
FT   METAL       728    728       Magnesium (By similarity).
FT   METAL       732    732       Magnesium (By similarity).
FT   MOD_RES     954    954       Phosphoserine; by PKA (By similarity).
FT   CONFLICT    975    975       I -> M (in Ref. 3; AAD03421).
FT   CONFLICT    981    981       S -> F (in Ref. 3; AAD03421).
SQ   SEQUENCE   1035 AA;  114726 MW;  6FF6E26F52BE1EC4 CRC64;
     MRRKTEIYSV ELNGTKDVEL ADQKDDKKFK GGKNKDSEPN KSQEEELKKE LDLDDHRLSN
     TDLEQKYGTN IIQGLSSIRA AELLARDGPN ALTPPKQTPE IIKFLKQMVG GFSILLWIGA
     ALCWIAYVIQ YVSSTASLDN VYLGAILVLV VILTGIFAYY QEAKSTNIMA SFSKMIPQQA
     LVIRDAEKKI IPAEQLVVGD VVEIKGGDQI PADIRLVFSQ GCKVDNSSLT GESEPQARST
     EFTHENPLET KNIGFYSTTC LEGTATGIVI NTGDRTIIGR IASLASGVGS EKTPIAIEIE
     HFVHIVAAVA VSVGVIFFIT AVCMKYYVLD AIIFLISIIV ANVPEGLLAT VTVTLSLTAK
     RMAKKNCLVK NLEAVETLGS TSIICSDKTG TLTQNRMTVA HLWFDNQIFV ADTSENQTKQ
     AFDQSSGTWA SLSKIITLCN RAEFRPGQES VPIMKRVVVG DASKTALLKF SEVILGDVMD
     IRKRNHKVAE IPFNSTNKFQ LSIHETEDPN DKRFLMVMKG APERILEKCS TIMINGQEQP
     LDKSSADAFH TAYMELGGLG ERVLGFCHLY LPADKFPQSY TFDVDSINFP TSNLCFVGLL
     SMIDPPRSTV PDAVSKCRSA GIKVIMVTGD HPITAKAIAK SVGIISANNE TVEDIAKRRN
     IAVEQVNKRE AKAAVVTGME LKDMTPEQLD ELLINYQEIV FARTSPQQKL IIVEGCQRQD
     AVVAVTGDGV NDSPALKKAD IGIAMGIAGS DAAKNAADMV LLDDNFASIV TGVEEGRLIF
     DNLKKTIAYT LTKNIAELCP FLIYIVAGLP LPIGTITILF IDLGTDIIPS IALAYEKAES
     DIMNRKPRHK KKDRLVNKQL AIYSYLHIGL MQALGGFLVY FTVYAQQGFW PTSLINLRVS
     WETDDINDLE DSYGQEWTRY QRKYLEWTGS TAFFVAIMVQ QIADLIIRKT RRNSIFQQGL
     FRNKVIWVGI ISQIIVALVL SYGLGSVTAL SFTMLRAQYW FVAVPHAILI WVYDEMRKLF
     IRLYPGSWWD KNMYY
//
ID   STK39_MOUSE             Reviewed;         556 AA.
AC   Q9Z1W9; Q80W13;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=STE20/SPS1-related proline-alanine-rich protein kinase;
DE            Short=Ste-20-related kinase;
DE            EC=2.7.11.1;
DE   AltName: Full=Serine/threonine-protein kinase 39;
GN   Name=Stk39; Synonyms=Spak;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=20438689; PubMed=10980603; DOI=10.1038/sj.onc.1203784;
RA   Johnston A.M., Naselli G., Gonez L.J., Martin R.M., Harrison L.C.,
RA   de Aizpurua H.J.;
RT   "SPAK, a STE20/SPS1-related kinase that activates the p38 pathway.";
RL   Oncogene 19:4290-4297(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
CC   -!- FUNCTION: May act as a mediator of stress-activated signals.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- INTERACTION:
CC       P47811:Mapk14; NbExp=1; IntAct=EBI-444764, EBI-298727;
CC       P55012:Slc12a2; NbExp=2; IntAct=EBI-444764, EBI-621078;
CC       Q924N4-1:Slc12a6; NbExp=3; IntAct=EBI-444764, EBI-620992;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable). Nucleus (Probable).
CC       Note=Nucleus when caspase-cleaved (Probable).
CC   -!- DOMAIN: PAPA box (proline-alanine repeats) may target the kinase
CC       to a specific subcellular location by facilitating interaction
CC       with intracellular proteins such as actin or actin-like proteins.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. STE20 subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   -----------------------------------------------------------------------
DR   EMBL; AF099988; AAC72237.1; -; mRNA.
DR   EMBL; BC051964; AAH51964.2; -; mRNA.
DR   EMBL; BC064443; AAH64443.1; -; mRNA.
DR   IPI; IPI00622783; -.
DR   RefSeq; NP_058562.1; NM_016866.2.
DR   UniGene; Mm.198414; -.
DR   ProteinModelPortal; Q9Z1W9; -.
DR   SMR; Q9Z1W9; 65-353, 459-556.
DR   DIP; DIP-31911N; -.
DR   IntAct; Q9Z1W9; 17.
DR   STRING; Q9Z1W9; -.
DR   PhosphoSite; Q9Z1W9; -.
DR   PRIDE; Q9Z1W9; -.
DR   Ensembl; ENSMUST00000102715; ENSMUSP00000099776; ENSMUSG00000027030.
DR   GeneID; 53416; -.
DR   KEGG; mmu:53416; -.
DR   UCSC; uc008jxo.1; mouse.
DR   CTD; 53416; -.
DR   MGI; MGI:1858416; Stk39.
DR   GeneTree; ENSGT00580000081442; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG108518; -.
DR   InParanoid; Q9Z1W9; -.
DR   OMA; SVHDSQG; -.
DR   OrthoDB; EOG4KH2VM; -.
DR   PhylomeDB; Q9Z1W9; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 310237; -.
DR   ArrayExpress; Q9Z1W9; -.
DR   Bgee; Q9Z1W9; -.
DR   Genevestigator; Q9Z1W9; -.
DR   GermOnline; ENSMUSG00000027030; Mus musculus.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Serine/threonine-protein kinase; Transferase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    556       STE20/SPS1-related proline-alanine-rich
FT                                protein kinase.
FT                                /FTId=PRO_0000086723.
FT   DOMAIN       75    349       Protein kinase.
FT   NP_BIND      81     89       ATP (By similarity).
FT   MOTIF       372    378       Nuclear localization signal (Potential).
FT   MOTIF       399    403       Caspase cleavage related site.
FT   COMPBIAS     17     65       Ala/Pro-rich.
FT   COMPBIAS     22     31       Poly-Ala.
FT   ACT_SITE    204    204       Proton acceptor (By similarity).
FT   BINDING     104    104       ATP (By similarity).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES     361    361       N6-acetyllysine (By similarity).
FT   MOD_RES     366    366       Phosphothreonine (By similarity).
FT   MOD_RES     382    382       Phosphoserine (By similarity).
FT   MOD_RES     383    383       Phosphoserine (By similarity).
FT   MOD_RES     397    397       Phosphoserine.
SQ   SEQUENCE   556 AA;  60320 MW;  66085A90554311D8 CRC64;
     MAEPSGSPVH VQLSQQAAPV TAAAATAPAA ATSAPAPAPA PAPAASAAPA PAPAAAPAPA
     PAAQAVGWPI CRDAYELQEV IGSGATAVVQ AALCKPRQER VAIKRINLEK CQTSMDELLK
     EIQAMSQCSH PNVVTYYTSF VVKDELWLVM KLLSGGSMLD IIKYIVNRGE HKNGVLEEAI
     IATILKEVLE GLDYLHRNGQ IHRDLKAGNI LLGEDGSVQI ADFGVSAFLA TGGDVTRNKV
     RKTFVGTPCW MAPEVMEQVR GYDFKADMWS FGITAIELAT GAAPYHKYPP MKVLMLTLQN
     DPPTLETGVE DKEMMKKYGK SFRKLLSLCL QKDPSKRPTA AELLKCKFFQ KAKNREYLIE
     KLLTRTPDIA QRAKKVRRVP GSSGHLHKTE DGDWEWSDDE MDEKSEEGKA AASQEKSRRV
     KEENSEISVN AGGIPEQIQS LSVHDSQAQP NANEDYREGP CAVNLVLRLR NSRKELNDIR
     FEFTPGRDTA DGVSQELFSA GLVDGHDVVI VAANLQKIVD DPKALKTLTF KLASGCDGSE
     IPDEVKLIGF AQLSVS
//
ID   PTSS2_MOUSE             Reviewed;         473 AA.
AC   Q9Z1X2; Q8BHL2; Q8CCI8; Q8CCY7; Q922A1; Q9CY68;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2004, sequence version 2.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Phosphatidylserine synthase 2;
DE            Short=PSS-2;
DE            Short=PtdSer synthase 2;
DE            EC=2.7.8.-;
DE   AltName: Full=Serine-exchange enzyme II;
GN   Name=Ptdss2; Synonyms=Pss2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=99362394; PubMed=10432300; DOI=10.1042/0264-6021:3420057;
RA   Stone S.J., Vance J.E.;
RT   "Cloning and expression of murine liver phosphatidylserine synthase
RT   (PSS)-2: differential regulation of phospholipid metabolism by PSS1
RT   and PSS2.";
RL   Biochem. J. 342:57-64(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Cerebellum, Corpus striatum, Embryo, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Mammary tumor, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Catalyzes a base-exchange reaction in which the polar
CC       head group of phosphatidylethanolamine is replaced by L-serine.
CC   -!- ENZYME REGULATION: Inhibited by excess phosphatidylserine, but not
CC       by phosphatidylcholine or phosphatidylethanolamine (By
CC       similarity).
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylserine biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Z1X2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Z1X2-2; Sequence=VSP_010637, VSP_010638;
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis. Detected at lower
CC       levels in kidney and heart.
CC   -!- SIMILARITY: Belongs to the phosphatidyl serine synthase family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF099053; AAC98383.1; -; mRNA.
DR   EMBL; AK021249; BAB32347.1; -; mRNA.
DR   EMBL; AK031906; BAC27599.1; -; mRNA.
DR   EMBL; AK032686; BAC27987.1; -; mRNA.
DR   EMBL; AK036368; BAC29399.1; -; mRNA.
DR   EMBL; AK081275; BAC38180.1; -; mRNA.
DR   EMBL; BC009013; AAH09013.1; -; mRNA.
DR   EMBL; BC053517; AAH53517.1; -; mRNA.
DR   IPI; IPI00308294; -.
DR   IPI; IPI00420158; -.
DR   RefSeq; NP_038810.2; NM_013782.4.
DR   UniGene; Mm.293591; -.
DR   STRING; Q9Z1X2; -.
DR   PhosphoSite; Q9Z1X2; -.
DR   PRIDE; Q9Z1X2; -.
DR   Ensembl; ENSMUST00000026568; ENSMUSP00000026568; ENSMUSG00000025495.
DR   GeneID; 27388; -.
DR   KEGG; mmu:27388; -.
DR   UCSC; uc009kjp.1; mouse.
DR   UCSC; uc009kjq.1; mouse.
DR   CTD; 27388; -.
DR   MGI; MGI:1351664; Ptdss2.
DR   eggNOG; roNOG13661; -.
DR   GeneTree; ENSGT00530000063576; -.
DR   HOGENOM; HBG557778; -.
DR   HOVERGEN; HBG053766; -.
DR   InParanoid; Q9Z1X2; -.
DR   OMA; QTVQDGR; -.
DR   OrthoDB; EOG42RD78; -.
DR   PhylomeDB; Q9Z1X2; -.
DR   NextBio; 305344; -.
DR   ArrayExpress; Q9Z1X2; -.
DR   Bgee; Q9Z1X2; -.
DR   CleanEx; MM_PTDSS2; -.
DR   Genevestigator; Q9Z1X2; -.
DR   GermOnline; ENSMUSG00000025495; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; IDA:MGI.
DR   GO; GO:0003882; F:CDP-diacylglycerol-serine O-phosphatidyltransferase activity; IMP:MGI.
DR   GO; GO:0006659; P:phosphatidylserine biosynthetic process; IMP:MGI.
DR   InterPro; IPR004277; PSS.
DR   PANTHER; PTHR12615; PSS; 1.
DR   Pfam; PF03034; PSS; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Glycoprotein; Membrane;
KW   Phospholipid biosynthesis; Phosphoprotein; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    473       Phosphatidylserine synthase 2.
FT                                /FTId=PRO_0000056833.
FT   TOPO_DOM      1     40       Cytoplasmic (Potential).
FT   TRANSMEM     41     61       Helical; (Potential).
FT   TOPO_DOM     62     74       Extracellular (Potential).
FT   TRANSMEM     75     95       Helical; (Potential).
FT   TOPO_DOM     96    104       Cytoplasmic (Potential).
FT   TRANSMEM    105    125       Helical; (Potential).
FT   TOPO_DOM    126    291       Extracellular (Potential).
FT   TRANSMEM    292    312       Helical; (Potential).
FT   TOPO_DOM    313    313       Cytoplasmic (Potential).
FT   TRANSMEM    314    334       Helical; (Potential).
FT   TOPO_DOM    335    354       Extracellular (Potential).
FT   TRANSMEM    355    375       Helical; (Potential).
FT   TOPO_DOM    376    381       Cytoplasmic (Potential).
FT   TRANSMEM    382    402       Helical; (Potential).
FT   TOPO_DOM    403    473       Extracellular (Potential).
FT   MOD_RES      16     16       Phosphoserine (By similarity).
FT   CARBOHYD    159    159       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    215    215       N-linked (GlcNAc...) (Potential).
FT   VAR_SEQ     264    303       GKMKRIAFQFTPYSWVRFEWKPASSLHRWLAVCGIILVFL
FT                                -> YILGVIEGNHRALGPQGQGLATWEGGKQNIRVVESDC
FT                                (in isoform 2).
FT                                /FTId=VSP_010637.
FT   VAR_SEQ     304    473       Missing (in isoform 2).
FT                                /FTId=VSP_010638.
FT   CONFLICT      4      4       G -> A (in Ref. 1; AAC98383).
FT   CONFLICT     11     11       G -> A (in Ref. 2; BAC27599).
FT   CONFLICT    469    469       T -> A (in Ref. 1; AAC98383).
SQ   SEQUENCE   473 AA;  55021 MW;  09ECB04E5B906F63 CRC64;
     MRRGERRVAG GSGSESPLLK GRRSTESEVY DDGTNTFFWR AHTLTVLFIL TCALGYVTLL
     EETPQDTAYN TKRGIVASIL VFLCFGVTQA KDGPFSRPHP AYWRFWLCVS VVYELFLIFI
     LFQTVQDGRQ FLKYVDPRLG VPLPERDYGG NCLIYDADNK TDPFHNIWDK LDGFVPAHFI
     GWYLKTLMIR DWWMCMIISV MFEFLEYSLE HQLPNFSECW WDHWIMDVLV CNGLGIYCGM
     KTLEWLSLKT YKWQGLWNIP TYKGKMKRIA FQFTPYSWVR FEWKPASSLH RWLAVCGIIL
     VFLLAELNTF YLKFVLWMPP EHYLVLLRLV FFVNVGGVAM REIYDFMDEL KPHRKLGQQA
     WLVAAITVTE LLIVVKYDPH TLTLSLPFYI SQCWTLGSIL VLTWTVWRFF LRDITMRYKE
     TRRQKQQSHQ ARAVNNRDGH PGPDDDLLGT GTAEEEGTTN DGVTAEEGTS AAS
//
ID   ILF3_MOUSE              Reviewed;         898 AA.
AC   Q9Z1X4; Q80VD5; Q812A1; Q8BP80; Q8C2H8; Q8K588;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 2.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=Interleukin enhancer-binding factor 3;
GN   Name=Ilf3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX   MEDLINE=94327652; PubMed=7519613;
RA   Kao P.N., Chen L., Brock G., Ng J., Kenny J., Smith A.J., Corthesy B.;
RT   "Cloning and expression of cyclosporin A- and FK506-sensitive nuclear
RT   factor of activated T-cells: NF45 and NF90.";
RL   J. Biol. Chem. 269:20691-20699(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND CHARACTERIZATION.
RC   TISSUE=Testis;
RX   MEDLINE=99269911; PubMed=10337617; DOI=10.1007/s003359901022;
RA   Buaas F.W., Lee K., Edelhoff S., Disteche C., Braun R.E.;
RT   "Cloning and characterization of the mouse interleukin enhancer
RT   binding factor 3 (Ilf3) homolog in a screen for RNA binding
RT   proteins.";
RL   Mamm. Genome 10:451-456(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RA   Gasmi L., Viranaicken W., Denoulet P., Larcher J.-C.;
RT   "Alternative splicing generates two mRNA transcripts of mouse
RT   interleukin enhancer binding factor 3 (Ilf3).";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-516 (ISOFORM 2), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 549-898.
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Head, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N-3; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   PROTEIN SEQUENCE OF 163-176; 421-434; 614-628 AND 853-867.
RX   PubMed=15364895; DOI=10.1096/fj.04-1763fje;
RA   Larcher J.-C., Gasmi L., Viranaicken W., Edde B., Bernard R.,
RA   Ginzburg I., Denoulet P.;
RT   "Ilf3 and NF90 associate with the axonal targeting element of Tau
RT   mRNA.";
RL   FASEB J. 18:1761-1763(2004).
CC   -!- FUNCTION: May facilitate double-stranded RNA-regulated gene
CC       expression at the level of post-transcription. Can act as a
CC       translation inhibitory protein which binds to coding sequences of
CC       acid beta-glucosidase (GCase) and other mRNAs and functions at the
CC       initiation phase of GCase mRNA translation, probably by inhibiting
CC       its binding to polysomes. Can regulate protein arginine N-
CC       methyltransferase 1 activity. Can promote the formation of stable
CC       DNA-dependent protein kinase holoenzyme complexes on DNA (By
CC       similarity).
CC   -!- SUBUNIT: Identified in a mRNP complex, at least composed of DHX9,
CC       DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1,
CC       STAU2, SYNCRIP and YBX1. Identified in a mRNP granule complex, at
CC       least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1,
CC       HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1,
CC       ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3,
CC       RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated
CC       mRNAs. Interacts with FUS and SMN proteins and with PRMT1. Forms a
CC       complex with ILF2. Can also bind to PRKDC/XRCC7: this may
CC       stabilize the interaction of PRKDC/XRCC7 and the heterodimeric
CC       complex of XRCC6/KU70 and XRCC5/KU80. Forms a heteromeric complex
CC       with ZNF346 and ILF3. Found in a nuclear export complex with XPO5,
CC       ILF3, Ran and double-stranded RNA or double-stranded minihelix VA1
CC       RNA. Found in a nuclear export complex with XPO5, RAN, ILF3,
CC       ZNF346 and double-stranded RNA. Interacts with XPO5 and ZNF346.
CC       Forms a complex with ILF2, YLPM1, KHDRBS1, RBMX, NCOA5 and PPP1CA
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus (By similarity).
CC       Cytoplasm (By similarity). Note=Localized in cytoplasmic mRNP
CC       granules containing untranslated mRNAs.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9Z1X4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Z1X4-2; Sequence=VSP_013406, VSP_013407, VSP_013408;
CC       Name=3;
CC         IsoId=Q9Z1X4-3; Sequence=VSP_013406;
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Expressed at high levels in the
CC       thymus, testis, ovary and at lower levelss in the spleen.
CC   -!- PTM: Phosphorylated by RNA-dependent protein kinase (EIF2AK2) (By
CC       similarity).
CC   -!- PTM: Methylated by protein arginine N-methyltransferase 1 (By
CC       similarity).
CC   -!- SIMILARITY: Contains 2 DRBM (double-stranded RNA-binding) domains.
CC   -!- SIMILARITY: Contains 1 DZF domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC71052.1; Type=Frameshift; Positions=73, 87;
CC       Sequence=BAC36863.1; Type=Frameshift; Positions=491;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF506968; AAM34210.1; -; Genomic_DNA.
DR   EMBL; AF098967; AAC71052.1; ALT_FRAME; mRNA.
DR   EMBL; AF497751; AAO23054.1; -; mRNA.
DR   EMBL; AF497752; AAO23055.1; -; mRNA.
DR   EMBL; AK048096; BAC33239.1; -; mRNA.
DR   EMBL; AK077560; BAC36863.1; ALT_FRAME; mRNA.
DR   EMBL; AK088604; BAC40448.1; -; mRNA.
DR   EMBL; BC047272; AAH47272.1; -; mRNA.
DR   IPI; IPI00130591; -.
DR   IPI; IPI00403996; -.
DR   IPI; IPI00555078; -.
DR   RefSeq; NP_001036172.1; NM_001042707.1.
DR   RefSeq; NP_001036173.1; NM_001042708.1.
DR   RefSeq; NP_034691.2; NM_010561.2.
DR   UniGene; Mm.440026; -.
DR   ProteinModelPortal; Q9Z1X4; -.
DR   SMR; Q9Z1X4; 403-470, 525-589.
DR   STRING; Q9Z1X4; -.
DR   PhosphoSite; Q9Z1X4; -.
DR   PRIDE; Q9Z1X4; -.
DR   Ensembl; ENSMUST00000067646; ENSMUSP00000065770; ENSMUSG00000032178.
DR   Ensembl; ENSMUST00000115413; ENSMUSP00000111073; ENSMUSG00000032178.
DR   GeneID; 16201; -.
DR   KEGG; mmu:16201; -.
DR   UCSC; uc009olb.1; mouse.
DR   UCSC; uc009old.1; mouse.
DR   UCSC; uc009ole.1; mouse.
DR   CTD; 16201; -.
DR   MGI; MGI:1339973; Ilf3.
DR   GeneTree; ENSGT00550000074528; -.
DR   HOGENOM; HBG402838; -.
DR   HOVERGEN; HBG069915; -.
DR   InParanoid; Q9Z1X4; -.
DR   OMA; GRNADHS; -.
DR   OrthoDB; EOG46WZ80; -.
DR   NextBio; 289137; -.
DR   ArrayExpress; Q9Z1X4; -.
DR   Bgee; Q9Z1X4; -.
DR   CleanEx; MM_ILF3; -.
DR   Genevestigator; Q9Z1X4; -.
DR   GermOnline; ENSMUSG00000032178; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030529; C:ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; TAS:MGI.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR001159; Ds-RNA-bd.
DR   InterPro; IPR014720; dsRNA-bd-like.
DR   InterPro; IPR006561; DZF.
DR   Gene3D; G3DSA:3.30.160.20; dsRNA-bd-like; 2.
DR   Pfam; PF00035; dsrm; 2.
DR   Pfam; PF07528; DZF; 1.
DR   SMART; SM00358; DSRM; 2.
DR   SMART; SM00572; DZF; 1.
DR   PROSITE; PS50137; DS_RBD; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm;
KW   Direct protein sequencing; DNA-binding; Methylation; Nucleus;
KW   Phosphoprotein; Repeat; RNA-binding; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    898       Interleukin enhancer-binding factor 3.
FT                                /FTId=PRO_0000126071.
FT   DOMAIN       94    342       DZF.
FT   DOMAIN      398    467       DRBM 1.
FT   DOMAIN      524    590       DRBM 2.
FT   REGION      609    898       Interaction with PRMT1 (By similarity).
FT   MOTIF       371    389       Bipartite nuclear localization signal
FT                                (Potential).
FT   COMPBIAS    385    389       Poly-Lys.
FT   COMPBIAS    634    637       Poly-Pro.
FT   COMPBIAS    640    659       Arg/Gly-rich.
FT   COMPBIAS    701    710       Poly-Gly.
FT   COMPBIAS    796    800       Poly-Gly.
FT   MOD_RES      81     81       N6-acetyllysine (By similarity).
FT   MOD_RES     100    100       N6-acetyllysine (By similarity).
FT   MOD_RES     190    190       Phosphoserine (By similarity).
FT   MOD_RES     368    368       Phosphothreonine (By similarity).
FT   MOD_RES     382    382       Phosphoserine (By similarity).
FT   MOD_RES     384    384       Phosphoserine (By similarity).
FT   MOD_RES     460    460       N6-acetyllysine (By similarity).
FT   MOD_RES     482    482       Phosphoserine (By similarity).
FT   MOD_RES     579    579       Phosphotyrosine (By similarity).
FT   MOD_RES     592    592       Phosphothreonine (By similarity).
FT   MOD_RES     609    609       Omega-N-methylated arginine (By
FT                                similarity).
FT   MOD_RES     794    794       Phosphoserine (By similarity).
FT   MOD_RES     812    812       Phosphoserine (By similarity).
FT   MOD_RES     814    814       Phosphoserine (By similarity).
FT   MOD_RES     864    864       Phosphoserine (By similarity).
FT   VAR_SEQ       1      1       M -> MALYHHHFITRRRR (in isoform 2 and
FT                                isoform 3).
FT                                /FTId=VSP_013406.
FT   VAR_SEQ     689    703       QFYSNGGHSGNAGGG -> DFFTDCYGYHDFGAS (in
FT                                isoform 2).
FT                                /FTId=VSP_013407.
FT   VAR_SEQ     704    898       Missing (in isoform 2).
FT                                /FTId=VSP_013408.
FT   CONFLICT    796    796       G -> C (in Ref. 2; AAC71052).
SQ   SEQUENCE   898 AA;  96021 MW;  171B31100D1181F7 CRC64;
     MRPMRIFVND DRHVMAKHSS VYPTQEELEA VQNMVSHTER ALKAVSDWID EQEKGNSELS
     EAENMDTPPD DESKEGAGEQ KAEHMTRTLR GVMRVGLVAK GLLLKGDLDL ELVLLCKEKP
     TTALLDKVAD NLAIQLTTVT EDKYEILQSV DDAAIVIKNT KEPPLSLTIH LTSPVVREEM
     EKVLAGETLS VNDPPDVLDR QKCLAALASL RHAKWFQARA NGLKSCVIVI RVLRDLCTRV
     PTWGPLRGWP LELLCEKSIG TANRPMGAGE ALRRVLECLA SGIVMPDGSG IYDPCEKEAT
     DAIGHLDRQQ REDITQSAQH ALRLAAFGQL HKVLGMDPLP SKMPKKPKNE NPVDYTVQIP
     PSTTYAITPM KRPMEEDGEE KSPSKKKKKI QKKEEKADPP QAMNALMRLN QLKPGLQYKL
     ISQTGPVHAP IFTMSVEVDG SNFEASGPSK KTAKLHVAVK VLQDMGLPTG AEGRDSSKGE
     DSAEESDGKP AIVAPPPVVE AVSNPSSVFP SDATTEQGPI LTKHGKNPVM ELNEKRRGLK
     YELISETGGS HDKRFVMEVE VDGQKFQGAG SNKKVAKAYA ALAALEKLFP DTPLALEANK
     KKRTPVPVRG GPKFAAKPHN PGFGMGGPMH NEVPPPPNIR GRGRGGNIRG RGRGRGFGGA
     NHGGGYMNAG AGYGSYGYSS NSATAGYSQF YSNGGHSGNA GGGGSGGGGG SSSYSSYYQG
     DSYNSPVPPK HAGKKPLHGG QQKASYSSGY QSHQGQQQPY NQSQYSSYGT PQGKQKGYGH
     GQGSYSSYSN SYNSPGGGGG SDYSYDSKFN YSGSGGRSGG NSYGSSGSSS YNTGSHGGYG
     TGSGGSSSYQ GKQGGYSSQS NYSSPGSSQS YSGPASSYQS SQGGYSRNTE HSMNYQYR
//
ID   STRAP_MOUSE             Reviewed;         350 AA.
AC   Q9Z1Z2; Q8BP89; Q8C6F6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Serine-threonine kinase receptor-associated protein;
DE   AltName: Full=UNR-interacting protein;
GN   Name=Strap; Synonyms=Unrip;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99074230; PubMed=9856985; DOI=10.1074/jbc.273.52.34671;
RA   Datta P.K., Chytil A., Gorska A.E., Moses H.L.;
RT   "Identification of STRAP, a novel WD domain protein in transforming
RT   growth factor-beta signaling.";
RL   J. Biol. Chem. 273:34671-34674(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, Pancreas, and Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-342, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Mast cell;
RX   PubMed=17947660;
RA   Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA   Kawakami T., Salomon A.R.;
RT   "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT   signaling.";
RL   J. Immunol. 179:5864-5876(2007).
CC   -!- FUNCTION: The SMN complex plays an essential role in spliceosomal
CC       snRNP assembly in the cytoplasm and is required for pre-mRNA
CC       splicing in the nucleus. STRAP may play a role in the cellular
CC       distribution of the SMN complex.
CC   -!- SUBUNIT: Part of the core SMN complex that contains SMN1,
CC       SIP1/GEMIN2, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8
CC       and STRAP/UNRIP. Binds directly to GEMIN6 and GEMIN7. Associates
CC       with the complex in the cytoplasm but not in the nucleus. Also
CC       interacts with CSDE1/UNR and MAWBP (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=Localized predominantly in the cytoplasm but
CC       also found in the nucleus (By similarity).
CC   -!- SIMILARITY: Belongs to the WD repeat STRAP family.
CC   -!- SIMILARITY: Contains 7 WD repeats.
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DR   EMBL; AF096285; AAC98300.1; -; mRNA.
DR   EMBL; AK075804; BAC35972.1; -; mRNA.
DR   EMBL; AK077504; BAC36834.1; -; mRNA.
DR   EMBL; AK145971; BAE26796.1; -; mRNA.
DR   EMBL; AK152283; BAE31097.1; -; mRNA.
DR   IPI; IPI00918973; -.
DR   RefSeq; NP_035629.2; NM_011499.3.
DR   UniGene; Mm.22584; -.
DR   ProteinModelPortal; Q9Z1Z2; -.
DR   SMR; Q9Z1Z2; 8-303.
DR   STRING; Q9Z1Z2; -.
DR   PhosphoSite; Q9Z1Z2; -.
DR   REPRODUCTION-2DPAGE; IPI00130670; -.
DR   REPRODUCTION-2DPAGE; Q9Z1Z2; -.
DR   PRIDE; Q9Z1Z2; -.
DR   Ensembl; ENSMUST00000064910; ENSMUSP00000068267; ENSMUSG00000030224.
DR   GeneID; 20901; -.
DR   KEGG; mmu:20901; -.
DR   UCSC; uc009enf.1; mouse.
DR   CTD; 20901; -.
DR   MGI; MGI:1329037; Strap.
DR   eggNOG; roNOG12701; -.
DR   GeneTree; ENSGT00530000063490; -.
DR   HOVERGEN; HBG055228; -.
DR   OrthoDB; EOG4CRM0M; -.
DR   PhylomeDB; Q9Z1Z2; -.
DR   NextBio; 299765; -.
DR   ArrayExpress; Q9Z1Z2; -.
DR   Bgee; Q9Z1Z2; -.
DR   Genevestigator; Q9Z1Z2; -.
DR   GermOnline; ENSMUSG00000030224; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0005102; F:receptor binding; IDA:MGI.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:MGI.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR011046; WD40_repeat-like_dom.
DR   InterPro; IPR019782; WD40_repeat_2.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR017986; WD40_repeat_dom.
DR   InterPro; IPR019781; WD40_repeat_sg.
DR   Gene3D; G3DSA:2.130.10.10; WD40/YVTN_repeat-like; 1.
DR   Pfam; PF00400; WD40; 6.
DR   PRINTS; PR00320; GPROTEINBRPT.
DR   SMART; SM00320; WD40; 7.
DR   SUPFAM; SSF50978; WD40_like; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 4.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Repeat; Spliceosome; WD repeat.
FT   CHAIN         1    350       Serine-threonine kinase receptor-
FT                                associated protein.
FT                                /FTId=PRO_0000051231.
FT   REPEAT       12     56       WD 1.
FT   REPEAT       57     96       WD 2.
FT   REPEAT       98    137       WD 3.
FT   REPEAT      141    179       WD 4.
FT   REPEAT      180    212       WD 5.
FT   REPEAT      221    262       WD 6.
FT   REPEAT      263    302       WD 7.
FT   MOD_RES     335    335       Phosphoserine (By similarity).
FT   MOD_RES     338    338       Phosphoserine (By similarity).
FT   MOD_RES     342    342       Phosphotyrosine.
FT   CONFLICT    288    288       T -> P (in Ref. 2; BAC36834).
FT   CONFLICT    330    330       L -> LA (in Ref. 1; AAC98300).
SQ   SEQUENCE   350 AA;  38442 MW;  99A71583618B1514 CRC64;
     MAMRQTPLTC SGHTRPVVDL AFSGITPYGY FLISACKDGK PMLRQGDTGD WIGTFLGHKG
     AVWGATLNKD ATKAATAAAD FTAKVWDAVS GDELMTLAHK HIVKTVDFTQ DSNYLLTGGQ
     DKLLRIYDLN KPEAEPKEIS GHTSGIKKAL WCSDDKQILS ADDKTVRLWD HATMTEVKSL
     NFNMSVSSME YIPEGEILVI TYGRSIAFHS AVSLEPIKSF EAPATINSAS LHPEKEFLVA
     GGEDFKLYKY DYNSGEELES YKGHFGPIHC VRFSPDGELY ASGSEDGTLR LWQTVVGKTY
     GLWKCVLPEE DSGELAKPKI GFPETAEEEL EEIASENSDS IYSSTPEVKA
//
ID   HNRPC_MOUSE             Reviewed;         313 AA.
AC   Q9Z204; Q3TLB5; Q501Q3; Q8C2G5; Q99KE2; Q9CQT3; Q9CY83;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 104.
DE   RecName: Full=Heterogeneous nuclear ribonucleoproteins C1/C2;
DE            Short=hnRNP C1/C2;
GN   Name=Hnrnpc; Synonyms=Hnrpc;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM C2).
RX   MEDLINE=20266297; PubMed=10805751;
RX   DOI=10.1128/MCB.20.11.4094-4105.2000;
RA   Williamson D.J., Banik-Maiti S., DeGregori J., Ruley H.E.;
RT   "hnRNP C is required for postimplantation mouse development but is
RT   dispensable for cell viability.";
RL   Mol. Cell. Biol. 20:4094-4105(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C1; C2; 3 AND 5).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Colon, Embryo, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C1 AND 4).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 51-61.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=B-cell lymphoma;
RX   PubMed=14729942; DOI=10.1074/mcp.D300003-MCP200;
RA   Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
RT   "Identification of phosphoproteins and their phosphorylation sites in
RT   the WEHI-231 B lymphoma cell line.";
RL   Mol. Cell. Proteomics 3:279-286(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241 AND SER-249, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241 AND SER-268, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
CC   -!- FUNCTION: Binds pre-mRNA and nucleates the assembly of 40S hnRNP
CC       particles. Single HNRNPC tetramers bind 230-240 nucleotides.
CC       Trimers of HNRNPC tetramers bind 700 nucleotides. May play a role
CC       in the early steps of spliceosome assembly and pre-mRNA splicing.
CC       Interacts with poly-U tracts in the 3'-UTR or 5'-UTR of mRNA and
CC       modulates the stability and the level of translation of bound mRNA
CC       molecules (By similarity).
CC   -!- SUBUNIT: Tetramer composed of 3 copies of isoform C1 and 1 copy of
CC       isoform C2. Assembly of 3 tetramers with bound pre-mRNA gives rise
CC       to a 19S complex that interacts with HNRNPA2B1 tetramers.
CC       Component of the 40S hnRNP particle. Identified in the spliceosome
CC       C complex, at least composed of AQR, ASCC3L1, C19orf29, CDC40,
CC       CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38,
CC       DHX8, EFTUD2, FRG1, GPATC1, HNRNPA1, HNRNPA2B1, HNRPA3, HNRNPC,
CC       HNRPF, HNRPH1, HNRPK, HNRPM, HNRNPR, HNRNPU, KIAA1160, KIAA1604,
CC       LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3,
CC       PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX,
CC       SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2,
CC       SNRPA1, SNRPB, SNRPB2, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF,
CC       SNRPG, SNW1, SRRM1, SRRM2, SYF2, SYNCRIP, TFIP11, THOC4, U2AF1,
CC       WDR57, XAB2 and ZCCHC8. Interacts with IGF2BP1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Note=Component of
CC       ribonucleosomes (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=C2;
CC         IsoId=Q9Z204-1; Sequence=Displayed;
CC       Name=C1;
CC         IsoId=Q9Z204-2; Sequence=VSP_005832;
CC       Name=3;
CC         IsoId=Q9Z204-3; Sequence=VSP_005832, VSP_005833;
CC       Name=4;
CC         IsoId=Q9Z204-4; Sequence=VSP_005832, VSP_019227;
CC       Name=5;
CC         IsoId=Q9Z204-5; Sequence=VSP_005833;
CC   -!- PTM: Phosphorylated on Ser-268 and Ser-306 in resting cells (By
CC       similarity).
CC   -!- PTM: Sumoylated. Sumoylation reduces affinity for mRNA (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the RRM HNRPC family. RALY subfamily.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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DR   EMBL; AF095257; AAD03717.1; -; mRNA.
DR   EMBL; AF095258; AAD19892.1; -; Genomic_DNA.
DR   EMBL; AK011336; BAB27553.1; -; mRNA.
DR   EMBL; AK012633; BAB28370.1; -; mRNA.
DR   EMBL; AK019958; BAB31934.1; -; mRNA.
DR   EMBL; AK088245; BAC40233.1; -; mRNA.
DR   EMBL; AK088678; BAC40499.1; -; mRNA.
DR   EMBL; AK089061; BAC40728.1; -; mRNA.
DR   EMBL; AK166590; BAE38877.1; -; mRNA.
DR   EMBL; AK168802; BAE40632.1; -; mRNA.
DR   EMBL; BC004706; AAH04706.1; -; mRNA.
DR   EMBL; BC095922; AAH95922.1; -; mRNA.
DR   IPI; IPI00223443; -.
DR   IPI; IPI00223444; -.
DR   IPI; IPI00759870; -.
DR   IPI; IPI00759886; -.
DR   IPI; IPI00874321; -.
DR   RefSeq; NP_001164452.1; NM_001170981.1.
DR   RefSeq; NP_001164453.1; NM_001170982.1.
DR   RefSeq; NP_001164454.1; NM_001170983.1.
DR   RefSeq; NP_001164455.1; NM_001170984.1.
DR   RefSeq; NP_058580.1; NM_016884.3.
DR   UniGene; Mm.427321; -.
DR   UniGene; Mm.473169; -.
DR   ProteinModelPortal; Q9Z204; -.
DR   SMR; Q9Z204; 2-92, 194-221.
DR   STRING; Q9Z204; -.
DR   PhosphoSite; Q9Z204; -.
DR   PRIDE; Q9Z204; -.
DR   Ensembl; ENSMUST00000111610; ENSMUSP00000107237; ENSMUSG00000060373.
DR   GeneID; 15381; -.
DR   KEGG; mmu:15381; -.
DR   UCSC; uc007tob.1; mouse.
DR   UCSC; uc007toc.1; mouse.
DR   UCSC; uc007tod.1; mouse.
DR   UCSC; uc007toe.1; mouse.
DR   UCSC; uc007tof.1; mouse.
DR   CTD; 15381; -.
DR   MGI; MGI:107795; Hnrnpc.
DR   eggNOG; roNOG13664; -.
DR   GeneTree; ENSGT00390000006718; -.
DR   HOVERGEN; HBG002302; -.
DR   NextBio; 288046; -.
DR   ArrayExpress; Q9Z204; -.
DR   Bgee; Q9Z204; -.
DR   CleanEx; MM_HNRNPC; -.
DR   Genevestigator; Q9Z204; -.
DR   GermOnline; ENSMUSG00000060373; Mus musculus.
DR   GO; GO:0045120; C:pronucleus; IDA:MGI.
DR   GO; GO:0005681; C:spliceosomal complex; ISS:HGNC.
DR   GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR017347; hnRNP_C_Raly.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   PIRSF; PIRSF037992; hnRNP-C_Raly; 1.
DR   SMART; SM00360; RRM; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Direct protein sequencing;
KW   Isopeptide bond; mRNA processing; mRNA splicing; Nucleus;
KW   Phosphoprotein; Ribonucleoprotein; RNA-binding; Spliceosome;
KW   Ubl conjugation.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    313       Heterogeneous nuclear ribonucleoproteins
FT                                C1/C2.
FT                                /FTId=PRO_0000081845.
FT   DOMAIN       16     87       RRM.
FT   MOTIF       155    161       Nuclear localization signal (Potential).
FT   COMPBIAS    181    303       Asp/Glu-rich (acidic).
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      39     39       N6-acetyllysine (By similarity).
FT   MOD_RES     107    107       Phosphoserine (By similarity).
FT   MOD_RES     113    113       Phosphoserine (By similarity).
FT   MOD_RES     115    115       Phosphoserine (By similarity).
FT   MOD_RES     120    120       Phosphoserine (By similarity).
FT   MOD_RES     121    121       Phosphoserine (By similarity).
FT   MOD_RES     138    138       Phosphoserine (By similarity).
FT   MOD_RES     162    162       Phosphoserine (By similarity).
FT   MOD_RES     170    170       N6-acetyllysine (By similarity).
FT   MOD_RES     217    217       N6-acetyllysine (By similarity).
FT   MOD_RES     232    232       Phosphoserine.
FT   MOD_RES     241    241       Phosphoserine.
FT   MOD_RES     246    246       Phosphoserine (By similarity).
FT   MOD_RES     247    247       Phosphoserine (By similarity).
FT   MOD_RES     249    249       Phosphoserine.
FT   MOD_RES     268    268       Phosphoserine.
FT   MOD_RES     306    306       Phosphoserine (By similarity).
FT   MOD_RES     313    313       Phosphoserine (By similarity).
FT   CROSSLNK    258    258       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   VAR_SEQ     108    120       Missing (in isoform C1, isoform 3 and
FT                                isoform 4).
FT                                /FTId=VSP_005832.
FT   VAR_SEQ     227    234       Missing (in isoform 4).
FT                                /FTId=VSP_019227.
FT   VAR_SEQ     227    233       Missing (in isoform 3 and isoform 5).
FT                                /FTId=VSP_005833.
FT   CONFLICT     46     46       C -> R (in Ref. 3; AAH04706).
SQ   SEQUENCE   313 AA;  34385 MW;  4AB834051E3E301B CRC64;
     MASNVTNKTD PRSMNSRVFI GNLNTLVVKK SDVEAIFSKY GKIVGCSVHK GFAFVQYVNE
     RNARAAVAGE DGRMIAGQVL DINLAAEPKV NRGKAGVKRS AAEMYGSVPE HPSPSPLLSS
     SFDLDYDFQR DYYDRMYSYP ARVPPPPPIA RAVVPSKRQR VSGNTSRRGK SGFNSKSGQR
     GSSSKSGKLK GDDLQAIKKE LTQIKQKVDS LLESLEKIEK EQSKQADLSF SSPVEMKNEK
     SEEEQSSASV KKDETNVKME SEAGADDSAE EGDLLDDDDN EDRGDDQLEL KDDEKEPEEG
     EDDRDSANGE DDS
//
ID   PX11B_MOUSE             Reviewed;         259 AA.
AC   Q9Z210; Q8C4G1; Q9D090;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Peroxisomal membrane protein 11B;
DE   AltName: Full=Peroxin-11B;
DE   AltName: Full=Peroxisomal biogenesis factor 11B;
DE   AltName: Full=Protein PEX11 homolog beta;
DE            Short=PEX11-beta;
GN   Name=Pex11b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99009071; PubMed=9792670; DOI=10.1074/jbc.273.45.29607;
RA   Schrader M., Reuber B.E., Morrell J.C., Jimenez-Sanchez G., Obie C.,
RA   Stroh T.A., Valle D., Schroer T.A., Gould S.J.;
RT   "Expression of PEX11beta mediates peroxisome proliferation in the
RT   absence of extracellular stimuli.";
RL   J. Biol. Chem. 273:29607-29614(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N, and NMRI; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION.
RX   PubMed=11839773; DOI=10.1083/jcb.200112028;
RA   Li X., Gould S.J.;
RT   "PEX11 promotes peroxisome division independently of peroxisome
RT   metabolism.";
RL   J. Cell Biol. 156:643-651(2002).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12024045; DOI=10.1128/MCB.22.12.4358-4365.2002;
RA   Li X., Baumgart E., Morrell J.C., Jimenez-Sanchez G., Valle D.,
RA   Gould S.J.;
RT   "PEX11 beta deficiency is lethal and impairs neuronal migration but
RT   does not abrogate peroxisome function.";
RL   Mol. Cell. Biol. 22:4358-4365(2002).
CC   -!- FUNCTION: Involved in peroxisomal proliferation. May regulate
CC       peroxisomes division by recruiting the dynamin-related GTPase
CC       DNM1L to the peroxisomal membrane (By similarity).
CC   -!- SUBUNIT: Interacts with PEX19 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane; Single-pass membrane
CC       protein (By similarity).
CC   -!- DISRUPTION PHENOTYPE: Mice have a marked decrease in peroxisome
CC       abundance. They share several phenotypes with Zellweger syndrome
CC       mouse models, including neuronal migration defects, hypotonia, a
CC       developmental delay, and neonatal lethality but no detectable
CC       defect in peroxisomal protein import and only mild defects in
CC       peroxisomal metabolic function.
CC   -!- SIMILARITY: Belongs to the peroxin-11 family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF093671; AAC78661.1; -; mRNA.
DR   EMBL; AK011709; BAB27791.1; -; mRNA.
DR   EMBL; AK082279; BAC38453.1; -; mRNA.
DR   EMBL; BC013812; AAH13812.1; -; mRNA.
DR   EMBL; BC054414; AAH54414.1; -; mRNA.
DR   IPI; IPI00459086; -.
DR   RefSeq; NP_001155859.1; NM_001162387.1.
DR   RefSeq; NP_035199.3; NM_011069.3.
DR   UniGene; Mm.20901; -.
DR   STRING; Q9Z210; -.
DR   PhosphoSite; Q9Z210; -.
DR   PRIDE; Q9Z210; -.
DR   Ensembl; ENSMUST00000048766; ENSMUSP00000037962; ENSMUSG00000028102.
DR   Ensembl; ENSMUST00000118557; ENSMUSP00000113365; ENSMUSG00000028102.
DR   GeneID; 18632; -.
DR   KEGG; mmu:18632; -.
DR   UCSC; uc008qnm.1; mouse.
DR   CTD; 18632; -.
DR   MGI; MGI:1338882; Pex11b.
DR   eggNOG; roNOG04684; -.
DR   GeneTree; ENSGT00390000014273; -.
DR   HOGENOM; HBG283401; -.
DR   HOVERGEN; HBG053771; -.
DR   InParanoid; Q9Z210; -.
DR   OMA; LGHALQK; -.
DR   PhylomeDB; Q9Z210; -.
DR   NextBio; 294596; -.
DR   ArrayExpress; Q9Z210; -.
DR   Bgee; Q9Z210; -.
DR   CleanEx; MM_PEX11B; -.
DR   Genevestigator; Q9Z210; -.
DR   GermOnline; ENSMUSG00000074396; Mus musculus.
DR   GO; GO:0005779; C:integral to peroxisomal membrane; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0016559; P:peroxisome fission; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR   InterPro; IPR008733; PEX11.
DR   PANTHER; PTHR12652; PEX11; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Membrane; Peroxisome; Peroxisome biogenesis;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    259       Peroxisomal membrane protein 11B.
FT                                /FTId=PRO_0000105968.
FT   TRANSMEM    234    254       Helical; (Potential).
FT   REGION      211    259       Interaction with PEX19 and peroxisome
FT                                targeting (By similarity).
FT   MOD_RES      43     43       N6-acetyllysine (By similarity).
FT   CONFLICT    119    119       W -> R (in Ref. 2; BAC38453).
FT   CONFLICT    217    217       D -> N (in Ref. 2; BAB27791).
FT   CONFLICT    227    227       L -> F (in Ref. 2; BAB27791).
SQ   SEQUENCE   259 AA;  28710 MW;  C0E1BF979E325EB2 CRC64;
     MDAWVRFSAQ SQARERLCRA AQYACSLLGH ALQRHGASPE LQKQIRQLEG HLSLGRKLLR
     LGNSTDALES AKRAVHLSDV VLRFCITVSH LNRALYFACD NVLWAGKSGL APRVDQEKWA
     QRSFRYYLFS LIMNLSRDAY EIRLLMEQET SAYSRRMKVS GVGVSGGVET VGPGGPGTPG
     GSLPQLALKF RLRILLLARV LRGHPPLLLD VLRNACDLFI PLDKLGLWRC GPGIVGLCGL
     ISSILSILTL ICPWLRLKP
//
ID   PLM_MOUSE               Reviewed;          92 AA.
AC   Q9Z239;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Phospholemman;
DE   AltName: Full=FXYD domain-containing ion transport regulator 1;
DE   Flags: Precursor;
GN   Name=Fxyd1; Synonyms=Plm;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=129/SvJ;
RX   MEDLINE=21303265; PubMed=11410367; DOI=10.1016/S0378-1119(01)00497-8;
RA   Bogaev R.C., Jia L.G., Kobayashi Y.M., Palmer C.J., Mounsey J.P.,
RA   Moorman J.R., Jones L.R., Tucker A.L.;
RT   "Gene structure and expression of phospholemman in mouse.";
RL   Gene 271:69-79(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-79 AND SER-83, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Induces a hyperpolarization-activated chloride current
CC       when expressed in Xenopus oocytes. May have a functional role in
CC       muscle contraction (By similarity).
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- PTM: Major plasma membrane substrate for cAMP-dependent protein
CC       kinase (PK-A) and protein kinase C (PK-C) in several different
CC       tissues. Phosphorylated in response to insulin and adrenergic
CC       stimulation (By similarity).
CC   -!- SIMILARITY: Belongs to the FXYD family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF091390; AAD11781.1; -; Genomic_DNA.
DR   EMBL; AF089734; AAD41683.1; -; mRNA.
DR   EMBL; AK002585; BAB22208.1; -; mRNA.
DR   EMBL; BC024671; AAH24671.1; -; mRNA.
DR   IPI; IPI00130455; -.
DR   RefSeq; NP_062376.2; NM_019503.4.
DR   RefSeq; NP_443717.1; NM_052991.4.
DR   RefSeq; NP_443718.1; NM_052992.3.
DR   RefSeq; NP_919302.1; NM_194321.2.
DR   UniGene; Mm.1491; -.
DR   ProteinModelPortal; Q9Z239; -.
DR   SMR; Q9Z239; 21-92.
DR   STRING; Q9Z239; -.
DR   PhosphoSite; Q9Z239; -.
DR   PRIDE; Q9Z239; -.
DR   Ensembl; ENSMUST00000039909; ENSMUSP00000048460; ENSMUSG00000036570.
DR   Ensembl; ENSMUST00000071697; ENSMUSP00000071617; ENSMUSG00000036570.
DR   Ensembl; ENSMUST00000108110; ENSMUSP00000103745; ENSMUSG00000036570.
DR   GeneID; 56188; -.
DR   KEGG; mmu:56188; -.
DR   UCSC; uc009ghu.1; mouse.
DR   CTD; 56188; -.
DR   MGI; MGI:1889273; Fxyd1.
DR   eggNOG; maNOG21518; -.
DR   GeneTree; ENSGT00530000063932; -.
DR   HOGENOM; HBG444253; -.
DR   HOVERGEN; HBG008212; -.
DR   InParanoid; Q9Z239; -.
DR   OMA; RKCRCKF; -.
DR   OrthoDB; EOG4PG62F; -.
DR   PhylomeDB; Q9Z239; -.
DR   NextBio; 311978; -.
DR   ArrayExpress; Q9Z239; -.
DR   Bgee; Q9Z239; -.
DR   CleanEx; MM_FXYD1; -.
DR   Genevestigator; Q9Z239; -.
DR   GermOnline; ENSMUSG00000036570; Mus musculus.
DR   GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005254; F:chloride channel activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000272; Ion-transport_regulator_FXYD.
DR   Pfam; PF02038; ATP1G1_PLM_MAT8; 1.
DR   PROSITE; PS01310; FXYD; 1.
PE   1: Evidence at protein level;
KW   Chloride; Chloride channel; Ion transport; Ionic channel; Membrane;
KW   Phosphoprotein; Signal; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL        1     20       By similarity.
FT   CHAIN        21     92       Phospholemman.
FT                                /FTId=PRO_0000010360.
FT   TOPO_DOM     21     35       Extracellular (Potential).
FT   TRANSMEM     36     56       Helical; (Potential).
FT   TOPO_DOM     57     92       Cytoplasmic (Potential).
FT   MOD_RES      79     79       Phosphothreonine.
FT   MOD_RES      83     83       Phosphoserine; by PKA and PKC (By
FT                                similarity).
FT   MOD_RES      88     88       Phosphoserine; by PKA (By similarity).
SQ   SEQUENCE   92 AA;  10323 MW;  0BDB1DC83417F3AD CRC64;
     MASPGHILAL CVCLLSMASA EAPQEPDPFT YDYHTLRIGG LTIAGILFIL GILIILSKRC
     RCKFNQQQRT GEPDEEEGTF RSSIRRLSSR RR
//
ID   SNAPN_MOUSE             Reviewed;         136 AA.
AC   Q9Z266; Q3U8V4; Q922V7;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 77.
DE   RecName: Full=SNARE-associated protein Snapin;
DE   AltName: Full=Synaptosomal-associated protein 25-binding protein;
DE            Short=SNAP-associated protein;
GN   Name=Snapin; Synonyms=Snap25bp, Snapap;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH SNAP25.
RC   TISSUE=Brain;
RX   MEDLINE=99211098; PubMed=10195194; DOI=10.1038/5673;
RA   Ilardi J.M., Mochida S., Sheng Z.-H.;
RT   "Snapin: a SNARE-associated protein implicated in synaptic
RT   transmission.";
RL   Nat. Neurosci. 2:119-124(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Bone marrow, Forelimb, Head, Liver, Pancreas, and Retina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Limb, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH SNAP23
RP   AND STX4A.
RX   PubMed=12877659; DOI=10.1042/BJ20030427;
RA   Buxton P., Zhang X.-M., Walsh B., Sriratana A., Schenberg I.,
RA   Manickam E., Rowe T.;
RT   "Identification and characterization of Snapin as a ubiquitously
RT   expressed SNARE-binding protein that interacts with SNAP23 in non-
RT   neuronal cells.";
RL   Biochem. J. 375:433-440(2003).
RN   [5]
RP   PHOSPHORYLATION, INTERACTION WITH SNAP25, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF SER-42; SER-50 AND THR-63.
RX   PubMed=11283605; DOI=10.1038/35070000;
RA   Chheda M.G., Ashery U., Thakur P., Rettig J., Sheng Z.-H.;
RT   "Phosphorylation of Snapin by PKA modulates its interaction with the
RT   SNARE complex.";
RL   Nat. Cell Biol. 3:331-338(2001).
RN   [6]
RP   REVIEW ON PHOSPHORYLATION.
RX   PubMed=12887314; DOI=10.1042/BST0310824;
RA   Evans G.J., Morgan A.;
RT   "Regulation of the exocytotic machinery by cAMP-dependent protein
RT   kinase: implications for presynaptic plasticity.";
RL   Biochem. Soc. Trans. 31:824-827(2003).
CC   -!- FUNCTION: May modulate a step between vesicle priming, fusion and
CC       calcium-dependent neurotransmitter release through its ability to
CC       potentiate the interaction of synaptotagmin with the SNAREs and
CC       the plasma-membrane-associated protein SNAP25. Its phosphorylation
CC       state influences exocytotic protein interactions and may regulate
CC       synaptic vesicle exocytosis. May also have a role in the
CC       mechanisms of SNARE-mediated membrane fusion in non-neuronal
CC       cells.
CC   -!- SUBUNIT: Associates with the SNARE complex. Interacts with RGS7
CC       (By similarity). Interacts with SNAP23, SNAP25 and STX4A but not
CC       with STX1A, VAMP2 and SYT1. Phosphorylation increases its
CC       interaction with SNAP25. Component of the biogenesis of lysosome-
CC       related organelles (BLOC-1) complex which is required for normal
CC       biogenesis of specialized organelles of the endosomal-lysosomal
CC       system. Interacts with CEP110 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC       protein; Cytoplasmic side. Cytoplasmic vesicle membrane;
CC       Peripheral membrane protein; Cytoplasmic side. Cytoplasmic
CC       vesicle, secretory vesicle, synaptic vesicle membrane; Peripheral
CC       membrane protein; Cytoplasmic side. Cell junction, synapse,
CC       synaptosome. Note=According to PubMed:12877659 it is may be
CC       cytoplasmic and peripheral membrane bound. According to
CC       PubMed:11283605 it is anchored to the vesicular membrane through
CC       an N-terminal signal anchor.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Z266-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Z266-2; Sequence=VSP_009165, VSP_009166;
CC   -!- TISSUE SPECIFICITY: Strongly expressed in heart, brain, testis,
CC       kidney and liver; low expression in spleen, lung and skeletal
CC       muscle.
CC   -!- PTM: Phosphorylated.
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DR   EMBL; AF086838; AAD11418.1; -; mRNA.
DR   EMBL; AK007458; BAB25049.1; -; mRNA.
DR   EMBL; AK048007; BAC33212.1; -; mRNA.
DR   EMBL; AK050151; BAC34095.1; -; mRNA.
DR   EMBL; AK077840; BAC37029.1; -; mRNA.
DR   EMBL; AK080718; BAC37991.1; -; mRNA.
DR   EMBL; AK152057; BAE30913.1; -; mRNA.
DR   EMBL; BC006744; AAH06744.1; -; mRNA.
DR   EMBL; BC048691; AAH48691.1; -; mRNA.
DR   IPI; IPI00130554; -.
DR   IPI; IPI00400077; -.
DR   RefSeq; NP_598615.1; NM_133854.3.
DR   UniGene; Mm.331182; -.
DR   MINT; MINT-3389684; -.
DR   STRING; Q9Z266; -.
DR   PhosphoSite; Q9Z266; -.
DR   PRIDE; Q9Z266; -.
DR   Ensembl; ENSMUST00000149884; ENSMUSP00000122090; ENSMUSG00000001018.
DR   GeneID; 20615; -.
DR   KEGG; mmu:20615; -.
DR   UCSC; uc008qck.1; mouse.
DR   CTD; 20615; -.
DR   MGI; MGI:1333745; Snapin.
DR   GeneTree; ENSGT00390000008274; -.
DR   HOGENOM; HBG717464; -.
DR   HOVERGEN; HBG056744; -.
DR   InParanoid; Q9Z266; -.
DR   OMA; CRINEHQ; -.
DR   OrthoDB; EOG4X6C9S; -.
DR   PhylomeDB; Q9Z266; -.
DR   NextBio; 298987; -.
DR   ArrayExpress; Q9Z266; -.
DR   Bgee; Q9Z266; -.
DR   CleanEx; MM_SNAPIN; -.
DR   Genevestigator; Q9Z266; -.
DR   GermOnline; ENSMUSG00000001018; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019717; C:synaptosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   InterPro; IPR017246; Snapin.
DR   PIRSF; PIRSF037631; Snapin; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell junction; Coiled coil;
KW   Cytoplasm; Cytoplasmic vesicle; Exocytosis; Membrane; Phosphoprotein;
KW   Synapse; Synaptosome.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    136       SNARE-associated protein Snapin.
FT                                /FTId=PRO_0000097557.
FT   COILED       37    126       Potential.
FT   MOD_RES       2      2       N-acetylalanine (By similarity).
FT   MOD_RES      14     14       Phosphothreonine (By similarity).
FT   MOD_RES      50     50       Phosphoserine; by PKA; in vitro.
FT   MOD_RES     129    129       Phosphotyrosine (By similarity).
FT   MOD_RES     133    133       Phosphoserine (By similarity).
FT   VAR_SEQ       1     54       Missing (in isoform 2).
FT                                /FTId=VSP_009165.
FT   VAR_SEQ      55     63       REQIDNLAT -> MLVAHFLFP (in isoform 2).
FT                                /FTId=VSP_009166.
FT   MUTAGEN      42     42       S->A: No effect.
FT   MUTAGEN      50     50       S->A: Inhibition of phosphorylation.
FT   MUTAGEN      50     50       S->D: 3.5-fold increase in SNAP25
FT                                binding.
FT   MUTAGEN      63     63       T->A: No effect.
SQ   SEQUENCE   136 AA;  14904 MW;  C81AC2ABCDCA21FA CRC64;
     MAAAGSAAVS GAGTPVAGPT GRDLFAEGLL EFLRPAVQQL DSHVHAVRES QVELREQIDN
     LATELCRINE DQKVALDLDP YVKKLLNARR RVVLVNNILQ NAQERLRRLN HSVAKETARR
     RAMLDSGVYP PGSPSK
//
ID   RASL1_MOUSE             Reviewed;         799 AA.
AC   Q9Z268;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 72.
DE   RecName: Full=RasGAP-activating-like protein 1;
GN   Name=Rasal1; Synonyms=Rasal;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98426153; PubMed=9751798; DOI=10.1016/S0378-1119(98)00394-1;
RA   Allen M., Chu S., Brill S., Stotler C., Buckler A.;
RT   "Restricted tissue expression pattern of a novel human rasGAP-related
RT   gene and its murine ortholog.";
RL   Gene 218:17-25(1998).
CC   -!- FUNCTION: Probable inhibitory regulator of the Ras-cyclic AMP
CC       pathway.
CC   -!- SIMILARITY: Contains 1 Btk-type zinc finger.
CC   -!- SIMILARITY: Contains 2 C2 domains.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 Ras-GAP domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF086714; AAD09007.1; -; mRNA.
DR   IPI; IPI00130555; -.
DR   UniGene; Mm.41209; -.
DR   ProteinModelPortal; Q9Z268; -.
DR   SMR; Q9Z268; 2-238, 261-554, 564-707.
DR   STRING; Q9Z268; -.
DR   PhosphoSite; Q9Z268; -.
DR   PRIDE; Q9Z268; -.
DR   Ensembl; ENSMUST00000031606; ENSMUSP00000031606; ENSMUSG00000029602.
DR   MGI; MGI:1330842; Rasal1.
DR   GeneTree; ENSGT00600000084336; -.
DR   HOGENOM; HBG446496; -.
DR   HOVERGEN; HBG106587; -.
DR   InParanoid; Q9Z268; -.
DR   OrthoDB; EOG4MSCXK; -.
DR   ArrayExpress; Q9Z268; -.
DR   Bgee; Q9Z268; -.
DR   CleanEx; MM_RASAL1; -.
DR   Genevestigator; Q9Z268; -.
DR   GermOnline; ENSMUSG00000029602; Mus musculus.
DR   GO; GO:0005622; C:intracellular; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001936; RasGAP.
DR   InterPro; IPR023152; RasGAP_CS.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR001562; Znf_Btk_motif.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:1.10.506.10; RasGAP; 1.
DR   Pfam; PF00779; BTK; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00616; RasGAP; 1.
DR   SMART; SM00107; BTK; 1.
DR   SMART; SM00239; C2; 2.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00323; RasGAP; 1.
DR   SUPFAM; SSF49562; C2_CaLB; 2.
DR   SUPFAM; SSF48350; Rho_GAP; 1.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR   PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR   PROSITE; PS51113; ZF_BTK; 1.
PE   2: Evidence at transcript level;
KW   GTPase activation; Metal-binding; Repeat; Zinc; Zinc-finger.
FT   CHAIN         1    799       RasGAP-activating-like protein 1.
FT                                /FTId=PRO_0000056646.
FT   DOMAIN        1     88       C2 1.
FT   DOMAIN      135    216       C2 2.
FT   DOMAIN      300    510       Ras-GAP.
FT   DOMAIN      565    672       PH.
FT   ZN_FING     674    710       Btk-type.
FT   COMPBIAS    498    501       Poly-Leu.
SQ   SEQUENCE   799 AA;  89429 MW;  E42F54B677F52269 CRC64;
     MAKSGSLSIR VVEGRALPAK DVSGSSDPYC LVKVDDQVVA RTATIWRSLS PFWGEEYTVH
     LPLDFHHLAF YVLDEDTVGH DDIIGKISLS KEAITADPRG IDSWINLSRV DPDAEVQGEV
     CLDVKLLEDA RGRCLRCHVR QARDLAPRDI SGTSDPFARV FWGNHSLETS TIKKTRFPHW
     DEVLELREAP GTTSPLRVEL WDWDMVGKND FLGMVEFTPQ TLQQKPPNGW FRLLPFPRAE
     DSGGSLGALR LKVRLTEDRV LPSQYYQPLM ELLLESVQGP AEEDTTSPLA LLEELASGDC
     RQDLATKLVK LFLGRGLAGP FLDYLTRREV ARTNDPNTLF RSNSLASKSM EQFMKLVGMR
     YLHEVLRPVI SRVFEEKKYM ELDPCKMDLN RSRRISFKGT PTEEQVRETS LGLLTGYLGS
     VVDAIVSSTG RCPLALRLAF KQLQRCVEKR FSGIEHQDVK YLAISGFLFL RFFAPAILTP
     KLFDLRDQHA DPQTSRSLLL LAKAVQSIGN LGQQLGQGKE QWLAPLHPFL LQSISRVRDF
     LDQLVDVDED EEAGGPACAL VQPSTIVREG FLLKRKEEPG GLATRFAFKK RYFRLSGRDL
     SYSKTPEWQV HTSIPLSCIR AVEHVDEGAF QLPHVMQVVT QDGAGTSHTT YLQCKNVNDF
     NQWLSALRKA SAPNPGKLVA CHPGAFRSGR WTCCLQAERS AAGCSRTHSA ITLGDWSDPL
     DPDAEAQAVY RQLLLGRDQL RLKLLEDSSL DTEVDPGRDS SATDGPCAEV LAQQRAATTH
     LLQVLEDLEQ AHEEFQKRG
//
ID   BAZ1B_MOUSE             Reviewed;        1479 AA.
AC   Q9Z277; B9EJ99; Q3URP5; Q3USR7; Q3UVM2; Q8CAU9; Q9CU68;
DT   30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 2.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Tyrosine-protein kinase BAZ1B;
DE            EC=2.7.10.2;
DE   AltName: Full=Bromodomain adjacent to zinc finger domain protein 1B;
DE   AltName: Full=Williams syndrome transcription factor homolog;
DE   AltName: Full=Williams-Beuren syndrome chromosomal region 9 protein homolog;
GN   Name=Baz1b; Synonyms=Wbscr9, Wstf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99077764; PubMed=9858827;
RA   Peoples R.J., Cisco M.J., Kaplan P., Francke U.;
RT   "Identification of the WBSCR9 gene, encoding a novel transcriptional
RT   regulator, in the Williams-Beuren syndrome deletion at 7q11.23.";
RL   Cytogenet. Cell Genet. 82:238-246(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-810 AND 823-1799 (ISOFORM
RP   1), AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-786 (ISOFORM 2).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Corpora quadrigemina, Thymus, and Urinary bladder;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=12837248; DOI=10.1016/S0092-8674(03)00436-7;
RA   Kitagawa H., Fujiki R., Yoshimura K., Mezaki Y., Uematsu Y.,
RA   Matsui D., Ogawa S., Unno K., Okubo M., Tokita A., Nakagawa T.,
RA   Ito T., Ishimi Y., Nagasawa H., Matsumoto T., Yanagisawa J., Kato S.;
RT   "The chromatin-remodeling complex WINAC targets a nuclear receptor to
RT   promoters and is impaired in Williams syndrome.";
RL   Cell 113:905-917(2003).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH MYO1C.
RX   PubMed=16514417; DOI=10.1038/sj.embor.7400657;
RA   Percipalle P., Fomproix N., Cavellan E., Voit R., Reimer G.,
RA   Krueger T., Thyberg J., Scheer U., Grummt I.,
RA   Oestlund Farrants A.-K.O.;
RT   "The chromatin remodelling complex WSTF-SNF2h interacts with nuclear
RT   myosin 1 and has a role in RNA polymerase I transcription.";
RL   EMBO Rep. 7:525-530(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161; SER-1464; SER-1466
RP   AND SER-1468, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1338, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-1338 AND
RP   SER-1464, AND MASS SPECTROMETRY.
RC   TISSUE=Macrophage;
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH SMARCA5.
RX   PubMed=19092802; DOI=10.1038/nature07668;
RA   Xiao A., Li H., Shechter D., Ahn S.H., Fabrizio L.A.,
RA   Erdjument-Bromage H., Ishibe-Murakami S., Wang B., Tempst P.,
RA   Hofmann K., Patel D.J., Elledge S.J., Allis C.D.;
RT   "WSTF regulates the H2A.X DNA damage response via a novel tyrosine
RT   kinase activity.";
RL   Nature 457:57-62(2009).
CC   -!- FUNCTION: Atypical tyrosine-protein kinase that plays a central
CC       role in chromatin remodeling and acts as a transcription
CC       regulator. Involved in DNA damage response by phosphorylating
CC       'Tyr-142' of histone H2AX (H2AXY142ph). H2AXY142ph plays a central
CC       role in DNA repair and acts as a mark that distinguishes between
CC       apoptotic and repair responses to genotoxic stress. Essential
CC       component of the WICH complex, a chromatin remodeling complex that
CC       mobilizes nucleosomes and reconfigures irregular chromatin to a
CC       regular nucleosomal array structure. The WICH complex regulates
CC       the transcription of various genes, has a role in RNA polymerase I
CC       and RNA polymerase III transcription, mediates the histone H2AX
CC       phosphorylation at 'Tyr-142', and is involved in the maintenance
CC       of chromatin structures during DNA replication processes. In the
CC       complex, it mediates the recruitment of the WICH complex to
CC       replication foci during DNA replication. Also involved in vitamin
CC       D-coupled transcription regulation via its association with the
CC       WINAC complex, a chromatin-remodeling complex recruited by vitamin
CC       D receptor (VDR), which is required for the ligand-bound VDR-
CC       mediated transrepression of the CYP27B1 gene. In the WINAC
CC       complex, plays an essential role by targeting the complex to
CC       acetylated histones, an essential step for VDR-promoter
CC       association (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate.
CC   -!- COFACTOR: Manganese (By similarity).
CC   -!- SUBUNIT: Interacts with MYO1C (By similarity). Interacts with
CC       CDT1. Interacts with SMARCA5/SNF2H; the interaction is direct and
CC       forms the WICH complex. Component of the B-WICH complex, at least
CC       composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6,
CC       MYBBP1A and DDX21. Component of the WINAC complex, at least
CC       composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1,
CC       SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B.
CC       Interacts with VDR; in a ligand-dependent manner. Interacts with
CC       PCNA; the interaction is direct (By similarity).
CC   -!- INTERACTION:
CC       Q91ZW3:Smarca5; NbExp=1; IntAct=EBI-927576, EBI-927547;
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Note=Accumulates in
CC       pericentromeric heterochromatin during replication. Targeted to
CC       replication foci throughout S phase via its association with PCNA
CC       (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Z277-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Z277-2; Sequence=VSP_037470;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues examined including
CC       heart, brain, spleen, lung, skeletal muscle, kidney and testis.
CC   -!- DEVELOPMENTAL STAGE: Expressed as early as day 7 and in equal
CC       amounts during gestation.
CC   -!- DOMAIN: The N-terminal part, including the WAC domain and the C
CC       motif, mediates the tyrosine-protein kinase activity (By
CC       similarity).
CC   -!- DOMAIN: The bromo domain mediates the specific interaction with
CC       acetylated histones (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the WAL family. BAZ1B subfamily.
CC   -!- SIMILARITY: Contains 1 bromo domain.
CC   -!- SIMILARITY: Contains 1 DDT domain.
CC   -!- SIMILARITY: Contains 1 PHD-type zinc finger.
CC   -!- SIMILARITY: Contains 1 WAC domain.
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DR   EMBL; AF084480; AAD08676.1; -; mRNA.
DR   EMBL; CH466529; EDL19376.1; -; Genomic_DNA.
DR   EMBL; BC141399; AAI41400.1; -; mRNA.
DR   EMBL; AK017894; BAB30992.1; -; mRNA.
DR   EMBL; AK037737; BAC29862.1; -; mRNA.
DR   EMBL; AK137139; BAE23247.1; -; mRNA.
DR   EMBL; AK140172; BAE24264.1; -; mRNA.
DR   EMBL; AK141305; BAE24643.1; -; mRNA.
DR   IPI; IPI00923656; -.
DR   IPI; IPI00930843; -.
DR   PIR; T17401; T17401.
DR   RefSeq; NP_035844.2; NM_011714.2.
DR   UniGene; Mm.40331; -.
DR   ProteinModelPortal; Q9Z277; -.
DR   SMR; Q9Z277; 1182-1441.
DR   DIP; DIP-36072N; -.
DR   IntAct; Q9Z277; 2.
DR   STRING; Q9Z277; -.
DR   PhosphoSite; Q9Z277; -.
DR   PRIDE; Q9Z277; -.
DR   Ensembl; ENSMUST00000002825; ENSMUSP00000002825; ENSMUSG00000002748.
DR   GeneID; 22385; -.
DR   KEGG; mmu:22385; -.
DR   UCSC; uc008zxz.1; mouse.
DR   CTD; 22385; -.
DR   MGI; MGI:1353499; Baz1b.
DR   GeneTree; ENSGT00530000063031; -.
DR   HOVERGEN; HBG050668; -.
DR   InParanoid; Q9Z277; -.
DR   OMA; CLHPQGI; -.
DR   OrthoDB; EOG4MKNFK; -.
DR   PhylomeDB; Q9Z277; -.
DR   NextBio; 302753; -.
DR   ArrayExpress; Q9Z277; -.
DR   Bgee; Q9Z277; -.
DR   CleanEx; MM_BAZ1B; -.
DR   Genevestigator; Q9Z277; -.
DR   GermOnline; ENSMUSG00000002748; Mus musculus.
DR   GO; GO:0005721; C:centromeric heterochromatin; IDA:MGI.
DR   GO; GO:0000793; C:condensed chromosome; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0070577; F:histone acetyl-lysine binding; ISS:UniProtKB.
DR   GO; GO:0035173; F:histone kinase activity; ISS:UniProtKB.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:EC.
DR   GO; GO:0071884; F:vitamin D receptor activator activity; IMP:BHF-UCL.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0048096; P:chromatin-mediated maintenance of transcription; IMP:BHF-UCL.
DR   GO; GO:0006302; P:double-strand break repair; IMP:BHF-UCL.
DR   GO; GO:0003007; P:heart morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR018500; DDT_dom_subgr.
DR   InterPro; IPR018501; DDT_dom_superfamily.
DR   InterPro; IPR013136; WSTF_Acf1_Cbp146.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Gene3D; G3DSA:1.20.920.10; Bromodomain; 1.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF10537; WAC_Acf1_DNA_bd; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SMART; SM00571; DDT; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF47370; Bromodomain; 1.
DR   SUPFAM; SSF57903; FYVE_PHD_ZnF; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS50827; DDT; 1.
DR   PROSITE; PS51136; WAC; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Bromodomain;
KW   Coiled coil; DNA damage; Kinase; Metal-binding; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Transcription; Transcription regulation;
KW   Transferase; Tyrosine-protein kinase; Zinc; Zinc-finger.
FT   CHAIN         1   1479       Tyrosine-protein kinase BAZ1B.
FT                                /FTId=PRO_0000211171.
FT   DOMAIN       20    126       WAC.
FT   DOMAIN      605    669       DDT.
FT   DOMAIN     1352   1422       Bromo.
FT   ZN_FING    1184   1234       PHD-type.
FT   REGION        1    345       Mediates the tyrosine-protein kinase
FT                                activity (By similarity).
FT   COILED      537    587       Potential.
FT   COILED      774    809       Potential.
FT   COILED      854    890       Potential.
FT   COILED     1257   1284       Potential.
FT   MOTIF       207    213       C motif.
FT   COMPBIAS    306    579       Lys-rich.
FT   MOD_RES     161    161       Phosphoserine.
FT   MOD_RES     167    167       Phosphoserine (By similarity).
FT   MOD_RES     189    189       Phosphoserine (By similarity).
FT   MOD_RES     283    283       Phosphoserine.
FT   MOD_RES     330    330       Phosphoserine (By similarity).
FT   MOD_RES     345    345       Phosphoserine (By similarity).
FT   MOD_RES     361    361       Phosphoserine (By similarity).
FT   MOD_RES     374    374       Phosphoserine (By similarity).
FT   MOD_RES     427    427       N6-acetyllysine (By similarity).
FT   MOD_RES     706    706       Phosphoserine (By similarity).
FT   MOD_RES     709    709       Phosphoserine (By similarity).
FT   MOD_RES     717    717       Phosphoserine (By similarity).
FT   MOD_RES    1147   1147       Phosphoserine (By similarity).
FT   MOD_RES    1315   1315       Phosphoserine (By similarity).
FT   MOD_RES    1338   1338       Phosphoserine.
FT   MOD_RES    1464   1464       Phosphoserine.
FT   MOD_RES    1466   1466       Phosphoserine.
FT   MOD_RES    1468   1468       Phosphoserine.
FT   VAR_SEQ       1    298       Missing (in isoform 2).
FT                                /FTId=VSP_037470.
FT   CONFLICT    957    957       S -> R (in Ref. 1; AAD08676).
FT   CONFLICT   1017   1017       L -> F (in Ref. 1; AAD08676).
FT   CONFLICT   1031   1034       SIYL -> CNYM (in Ref. 1; AAD08676).
SQ   SEQUENCE   1479 AA;  170651 MW;  6EFBF3913EA93AF0 CRC64;
     MAPLLGRKPF PLVKPLPGEE PLFTIPHTQE AFRTREEYEA RLERYSERIW TCKSTGSSQL
     THKEAWEEEQ EVAELLKEEF PNWYEKLVLE MVHHNTASLE KLVDSAWLEI MTKYAVGEEC
     DFEVGKEKML KVKIVKIHPL EKVDEEAVEK KSDGACDSPS SDKENSSQMA QDLQKKETVV
     KEDEGRRESI NDRARRSPRK LPTSLKKGER KWAPPKFLPH KYDVKLQNED KIISNVPADS
     LIRTERPPNK EILRYFIRHN ALRAGTGENA PWVVEDELVK KYSLPSKFSD FLLDPYKYMT
     LNPSTKRRNT GSPDRKPSKK PKRDSSSLSS PLNPKLWCHV HLEKSLNGPP LKVKNSKNSK
     SPEEHLEGVM KIMSPNNNKL HSFHIPKKGP AAKKPGKHSD KPLKAKGRGK GILNGQKSTG
     NSKSPSKCVK TPKTKMKQMT LLDMAKGTQK MTRTPRSSGG VPRSSGKPHK HLPPAALHLI
     AYYKENKDKE DKKSALSCVI SKTARLLSNE DRARLPEELR ALVQKRYELL EHKKRWASMS
     EEQRKEYLKK KRQELKERLR EKAKERRERE MLERLEKQKR FEDQELGGRN LPAFRLVDTP
     EGLPNTLFGD VALVVEFLSC YSGLLLPDAQ YPITAVSLME ALSADKGGFL YLNRVLVILL
     QTLLQDEIAE DYGELGMKLS EIPLTLHSVS ELVRLCLRRC DVQEDSEGSE TDDNKDSTPF
     EDNEVQDEFL EKLETSEFFE LTSEEKLRIL TALCHRILMT YSVQDHMETR QQVSAELWKE
     RLAVLKEEND KKRAEKQKRK EMEARNKENG KEENVLGKVD RKKEIVKIEQ QVEVEADDMI
     SAVKSRRLLS MQAKRKREIQ ERETKVRLER EAEEERMRKH KAAAEKAFQE GIAKAKLVLR
     RTPIGTDRNH NRYWLFSNEV PGLFIEKGWV HNSIDYRFKH HRKDHSNLPD DDYCPRSKKA
     NLGKNASVNA HHGPALEAVE TTVPKQGQNL WFLCDSQKEL DELLSCLHPQ GIRESQLKER
     LEKRYQEITH SIYLARKPNL GLKSCDGNQE LLNFLRSDLI EVATRLQKGG LGYMEGTSEF
     EARVISLEKL KDFGECVIAL QASVIKKFLQ GFMAPKQKKR KLQSEDSTKS EEVDEEKKMV
     EEAKVASALE KWKTAIREAQ TFSRMHVLLG MLDACIKWDM SAENARCKVC RKKGEDDKLI
     LCDECNKAFH LFCLRPALYE VPDGEWQCPA CQPPTARRNS RGRNYTEEST SEGSEGDESG
     EEEEEEEEEE EEEEDYEVAG LRLRPRKTIR GKQSVIPAAR PGRPPGKKSH PARRSRPKDD
     PEVDDLVLQT KRISRRQSLE LQKCEDILHK LVKYRFSWPF REPVTRDEAE DYYDVIEHPM
     DFQTIQNKCS CGNYRSVQEF LTDMKQVFAN AELYNCRGSH VLSCMEKTEQ CLLALLQKHL
     PGHPYVRRKR RKFPDRLADD EGDSDSESVG QSRGRRQKK
//
ID   PLD1_MOUSE              Reviewed;        1074 AA.
AC   Q9Z280; O35911;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-FEB-2011, entry version 93.
DE   RecName: Full=Phospholipase D1;
DE            Short=PLD 1;
DE            Short=mPLD1;
DE            EC=3.1.4.4;
DE   AltName: Full=Choline phosphatase 1;
DE   AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D1;
GN   Name=Pld1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PLD1A AND PLD1B).
RC   STRAIN=129; TISSUE=Embryonic brain, and Neonatal brain;
RX   MEDLINE=97439716; PubMed=9307024;
RA   Colley W.C., Altshuller Y.M., Sue-Ling C.K., Copeland N.G.,
RA   Gilbert D.J., Jenkins N.A., Branch K.D., Tsirka S.E., Bollag R.J.,
RA   Bollag W.B., Frohman M.A.;
RT   "Cloning and expression analysis of murine phospholipase D1.";
RL   Biochem. J. 326:745-753(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM PLD1A).
RC   STRAIN=129;
RX   MEDLINE=99033000; PubMed=9813240; DOI=10.1016/S0378-1119(98)00465-X;
RA   Redina O.E., Frohman M.A.;
RT   "Genomic analysis of murine phospholipase D1 and comparison to
RT   phospholipase D2 reveals an unusual difference in gene size.";
RL   Gene 222:53-60(1998).
RN   [3]
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=97199446; PubMed=9395408; DOI=10.1016/S0960-9822(97)70090-3;
RA   Colley W.C., Sung T.-C., Roll R., Jenco J.M., Hammond S.M.,
RA   Altshuller Y.M., Bar-Sagi D., Morris A.J., Frohman M.A.;
RT   "Phospholipase D2, a distinct phospholipase D isoform with novel
RT   regulatory properties that provokes cytoskeletal reorganization.";
RL   Curr. Biol. 7:191-201(1997).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Implicated as a critical step in numerous cellular
CC       pathways, including signal transduction, membrane trafficking, and
CC       the regulation of mitosis. May be involved in the regulation of
CC       perinuclear intravesicular membrane traffic.
CC   -!- CATALYTIC ACTIVITY: A phosphatidylcholine + H(2)O = choline + a
CC       phosphatidate.
CC   -!- ENZYME REGULATION: Stimulated by phosphatidylinositol 4,5-
CC       bisphosphate and phosphatidylinositol 3,4,5-trisphosphate,
CC       activated by the phosphokinase C-alpha, by the ADP-ribosylation
CC       factor-1 (ARF-1), and to a lesser extent by GTP-binding proteins:
CC       RHO A, RAC-1 and CDC42.
CC   -!- SUBUNIT: Interacts with PIP5K1A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Endoplasmic
CC       reticulum membrane; Lipid-anchor; Cytoplasmic side (Potential).
CC       Golgi apparatus membrane; Lipid-anchor; Cytoplasmic side
CC       (Potential). Late endosome membrane; Lipid-anchor; Cytoplasmic
CC       side (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=PLD1A;
CC         IsoId=Q9Z280-1; Sequence=Displayed;
CC       Name=PLD1B;
CC         IsoId=Q9Z280-2; Sequence=VSP_005023;
CC   -!- TISSUE SPECIFICITY: Expressed in kidney, lung, and at a much lower
CC       levels, in brain, liver, heart, testis and spleen.
CC   -!- DEVELOPMENTAL STAGE: Expressed most strikingly in selected
CC       ventricular cells lining the spinal cord and brain. The level of
CC       expression decreases dramatically as the cells differentiate into
CC       neurons and migrate to the outer layer of the spinal cord and
CC       brain. Expression is observed during development in a restricted
CC       region of the nasal neuroepithelium.
CC   -!- DISEASE: Note=Defects in Pld1 may result in coa which is
CC       associated with coat color dilution and white spotting. It is also
CC       associated with platelet-storage pool deficiency characterized by
CC       decreased levels in serotonin and dense granules.
CC   -!- SIMILARITY: Belongs to the phospholipase D family.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 2 PLD phosphodiesterase domains.
CC   -!- SIMILARITY: Contains 1 PX (phox homology) domain.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U87868; AAB81245.1; -; mRNA.
DR   EMBL; AF083497; AAC84041.1; -; Genomic_DNA.
DR   EMBL; AF083475; AAC84041.1; JOINED; Genomic_DNA.
DR   EMBL; AF083476; AAC84041.1; JOINED; Genomic_DNA.
DR   EMBL; AF083478; AAC84041.1; JOINED; Genomic_DNA.
DR   EMBL; AF083479; AAC84041.1; JOINED; Genomic_DNA.
DR   EMBL; AF083480; AAC84041.1; JOINED; Genomic_DNA.
DR   EMBL; AF083481; AAC84041.1; JOINED; Genomic_DNA.
DR   EMBL; AF083483; AAC84041.1; JOINED; Genomic_DNA.
DR   EMBL; AF083484; AAC84041.1; JOINED; Genomic_DNA.
DR   EMBL; AF083485; AAC84041.1; JOINED; Genomic_DNA.
DR   EMBL; AF083486; AAC84041.1; JOINED; Genomic_DNA.
DR   EMBL; AF083488; AAC84041.1; JOINED; Genomic_DNA.
DR   EMBL; AF083489; AAC84041.1; JOINED; Genomic_DNA.
DR   EMBL; AF083490; AAC84041.1; JOINED; Genomic_DNA.
DR   EMBL; AF083492; AAC84041.1; JOINED; Genomic_DNA.
DR   EMBL; AF083494; AAC84041.1; JOINED; Genomic_DNA.
DR   EMBL; AF083495; AAC84041.1; JOINED; Genomic_DNA.
DR   EMBL; AF083496; AAC84041.1; JOINED; Genomic_DNA.
DR   IPI; IPI00130629; -.
DR   IPI; IPI00229888; -.
DR   PIR; T17203; T17203.
DR   PIR; T42093; T42093.
DR   UniGene; Mm.212039; -.
DR   ProteinModelPortal; Q9Z280; -.
DR   STRING; Q9Z280; -.
DR   PhosphoSite; Q9Z280; -.
DR   PRIDE; Q9Z280; -.
DR   Ensembl; ENSMUST00000067776; ENSMUSP00000066634; ENSMUSG00000027695.
DR   MGI; MGI:109585; Pld1.
DR   eggNOG; roNOG09371; -.
DR   GeneTree; ENSGT00390000008356; -.
DR   HOGENOM; HBG590223; -.
DR   HOVERGEN; HBG006650; -.
DR   InParanoid; Q9Z280; -.
DR   BRENDA; 3.1.4.4; 244.
DR   ArrayExpress; Q9Z280; -.
DR   Bgee; Q9Z280; -.
DR   CleanEx; MM_PLD1; -.
DR   Genevestigator; Q9Z280; -.
DR   GermOnline; ENSMUSG00000027695; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070290; F:NAPE-specific phospholipase D activity; IEA:EC.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0004630; F:phospholipase D activity; IEA:EC.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:MGI.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR015679; Phospholipase_D.
DR   InterPro; IPR001683; Phox.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   InterPro; IPR016555; PLipase_D_euk.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Gene3D; G3DSA:3.30.1520.10; PX; 1.
DR   PANTHER; PTHR18896; Phospholipase_D; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00614; PLDc; 1.
DR   Pfam; PF00787; PX; 1.
DR   PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00155; PLDc; 2.
DR   SMART; SM00312; PX; 1.
DR   SUPFAM; SSF64268; PX; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50035; PLD; 2.
DR   PROSITE; PS50195; PX; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Endoplasmic reticulum; Endosome;
KW   Golgi apparatus; Hydrolase; Lipid degradation; Lipoprotein; Membrane;
KW   Palmitate; Phosphoprotein; Repeat.
FT   CHAIN         1   1074       Phospholipase D1.
FT                                /FTId=PRO_0000218803.
FT   DOMAIN       81    212       PX.
FT   DOMAIN      219    328       PH.
FT   DOMAIN      459    486       PLD phosphodiesterase 1.
FT   DOMAIN      891    918       PLD phosphodiesterase 2.
FT   REGION      463    928       Catalytic.
FT   MOD_RES     538    538       Phosphoserine.
FT   MOD_RES     629    629       Phosphoserine.
FT   LIPID       240    240       S-palmitoyl cysteine (By similarity).
FT   LIPID       241    241       S-palmitoyl cysteine (By similarity).
FT   VAR_SEQ     585    623       SYFSHCRSHQNLIHGLKPHLKLFHPSSESEQGLTRHSTD
FT                                -> N (in isoform PLD1B).
FT                                /FTId=VSP_005023.
FT   CONFLICT     71     74       NIQT -> QHPD (in Ref. 1; AAB81245).
FT   CONFLICT    574    574       A -> V (in Ref. 1; AAB81245).
FT   CONFLICT    675    675       R -> G (in Ref. 1; AAB81245).
FT   CONFLICT    781    781       N -> I (in Ref. 1; AAB81245).
FT   CONFLICT    876    876       C -> V (in Ref. 1; AAB81245).
FT   CONFLICT    990    990       T -> A (in Ref. 1; AAB81245).
FT   CONFLICT   1071   1073       EVW -> SLT (in Ref. 1).
SQ   SEQUENCE   1074 AA;  123969 MW;  E11260982A217280 CRC64;
     MSLKSETRVN TSTLQKIAAD MSNLIENLDT RELHFEGEEV EYDASPGDPK AQEGCIPFSS
     IYNTQGFKEP NIQTYLSGCP IKAQVLEVER FTSTSRVPSI NLYTIELTHG EFTWQVKRKF
     KHFQEFHREL LKYKAFIRIP IPTKRHTFRR QNVKEEPREM PSLPRSSENA IQEEQFFGRR
     KQLEDYLTKI LKMPMYRNYH ATTEFLDVSQ LSFIHDLGPK GLEGMIMKRS GGHRIPGVNC
     CGHGRACYRW SKRWLIVKDS FLLYMKPDSG AIAFVLLVDK EFRVKVGRKE TETKYGLRID
     NLSRTLILKC NSYRHARWWG GAIEEFIRKH GADFLKDHRF GSYAALHENT LAKWYVNAKG
     YFEDIANAME EASEEIFITD WWLSPEIFLK RPVVEGNRWR LDCILKRKAQ QGVRIFIMLY
     KEVELALGIN SEYSKRTLMR LHPNIKVMRH PDHVSSSVYL WAHHEKLVII DQSVAFVGGI
     DLAYGRWDDN EHRLTDVGSV KRVTSGLSLG SLTAASVESM ESLSLKDKHE FHKKEPISKI
     VDETDMKLKG IGKSRKFSKF SLYRQLHRHH LHNADSISSI DSTSSYFSHC RSHQNLIHGL
     KPHLKLFHPS SESEQGLTRH STDTGSIRSV QTGVGELHGE TRFWHGKDYC NFVFKDWVQL
     DKPFADFIDR YSTPRMPWHD IGSVVHGKAA RDVARHFIQR WNFTKIMKPK YRSLSYPFLL
     PKSQATAHEL RYQVPGAVPA KVQLLRSAAD WSAGIKHHEE SIHAAYIHVI ENSKHYIYIE
     NQFFISCADD KVVFNKVGDR IAQRILKAHR EGQRYRVYIV IPLLPGFEGD ISTGGGNALQ
     AIMHFNYRTM CRGESSILEQ LKPELGNKWI NYISFCGLRT HAELEGNLVT ELIYVHSKLL
     IADDNTVIIG SANINDRSML GKRDSEMAVI VQDTETVPSV MDGKEYQAGR FARDLRLECF
     RLVLGYLSDP SEDLQDPVSD KFFKEIWVST AARNATIYDK VFRCLPNDEV HNLIQLRDFI
     NKPILAKEDA LRAEEELRKI RGFLVQFPLY FLSEENLLPS VGTKEAIVPM EVWT
//
ID   PDPK1_MOUSE             Reviewed;         559 AA.
AC   Q9Z2A0; A6H6U3; Q9R1D8; Q9R215;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   18-OCT-2001, sequence version 2.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=3-phosphoinositide-dependent protein kinase 1;
DE            Short=mPDK1;
DE            EC=2.7.11.1;
GN   Name=Pdpk1; Synonyms=Pdk1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=99175193; PubMed=10075713; DOI=10.1074/jbc.274.12.8117;
RA   Dong L.Q., Zhang R.-B., Langlais P., He H., Clark M., Zhu L., Liu F.;
RT   "Primary structure, tissue distribution, and expression of mouse
RT   phosphoinositide-dependent protein kinase-1, a protein kinase that
RT   phosphorylates and activates protein kinase C zeta.";
RL   J. Biol. Chem. 274:8117-8122(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RA   Park J., Hemmings B.A.;
RT   "Mouse phosphoinositide-dependent protein kinase 1 (mPDK1).";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RA   Xu P., Taylor S.;
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Phosphorylates and activates not only PKB/AKT, but also
CC       PKA, PKC-zeta, RPS6KA1 and RPS6KB1. May play a general role in
CC       signaling processes and in development. Could also play a role in
CC       sex differentiation processes.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SUBUNIT: Interacts with NPRL2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC       protein. Note=Membrane-associated after cell stimulation leading
CC       to its translocation. Tyrosine phosphorylation seems to occur only
CC       at the plasma membrane.
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart, brain, liver and
CC       testis, also expressed in embryonic cells.
CC   -!- PTM: Phosphorylated on tyrosine and serine/threonine.
CC       Phosphorylation on Ser-244 in the activation loop is required for
CC       full activity. PDK1 itself can autophosphorylate Ser-244, leading
CC       to its own activation (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. PDK1 subfamily.
CC   -!- SIMILARITY: Contains 1 PH domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
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DR   EMBL; AF086625; AAC67544.1; -; mRNA.
DR   EMBL; AF126294; AAD38505.1; -; mRNA.
DR   EMBL; AF079535; AAC96115.1; -; mRNA.
DR   EMBL; BC146001; AAI46002.1; -; mRNA.
DR   EMBL; BC146003; AAI46004.1; -; mRNA.
DR   IPI; IPI00323609; -.
DR   RefSeq; NP_035192.2; NM_011062.4.
DR   UniGene; Mm.10504; -.
DR   ProteinModelPortal; Q9Z2A0; -.
DR   SMR; Q9Z2A0; 78-552.
DR   IntAct; Q9Z2A0; 20.
DR   STRING; Q9Z2A0; -.
DR   PhosphoSite; Q9Z2A0; -.
DR   PRIDE; Q9Z2A0; -.
DR   Ensembl; ENSMUST00000102927; ENSMUSP00000099991; ENSMUSG00000024122.
DR   GeneID; 18607; -.
DR   KEGG; mmu:18607; -.
DR   UCSC; uc008aui.1; mouse.
DR   CTD; 18607; -.
DR   MGI; MGI:1338068; Pdpk1.
DR   GeneTree; ENSGT00550000074819; -.
DR   HOGENOM; HBG755340; -.
DR   HOVERGEN; HBG098357; -.
DR   InParanoid; Q9Z2A0; -.
DR   OMA; HLQTPPK; -.
DR   OrthoDB; EOG4ZPDVM; -.
DR   PhylomeDB; Q9Z2A0; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 294526; -.
DR   ArrayExpress; Q9Z2A0; -.
DR   Bgee; Q9Z2A0; -.
DR   CleanEx; MM_PDK1; -.
DR   CleanEx; MM_PDPK1; -.
DR   Genevestigator; Q9Z2A0; -.
DR   GermOnline; ENSMUSG00000024122; Mus musculus.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:MGI.
DR   GO; GO:0004676; F:3-phosphoinositide-dependent protein kinase activity; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0006972; P:hyperosmotic response; IDA:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; TAS:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN         1    559       3-phosphoinositide-dependent protein
FT                                kinase 1.
FT                                /FTId=PRO_0000086501.
FT   DOMAIN       85    345       Protein kinase.
FT   DOMAIN      462    553       PH.
FT   NP_BIND      91     99       ATP (By similarity).
FT   COMPBIAS    392    401       Poly-Ser.
FT   ACT_SITE    208    208       Proton acceptor (By similarity).
FT   BINDING     114    114       ATP (By similarity).
FT   MOD_RES       9      9       Phosphotyrosine (By similarity).
FT   MOD_RES      25     25       Phosphoserine (By similarity).
FT   MOD_RES     244    244       Phosphoserine; by autocatalysis (By
FT                                similarity).
FT   MOD_RES     248    248       Phosphothreonine (By similarity).
FT   MOD_RES     307    307       N6-acetyllysine (By similarity).
FT   MOD_RES     376    376       Phosphotyrosine (By similarity).
FT   MOD_RES     379    379       Phosphotyrosine (By similarity).
FT   MOD_RES     396    396       Phosphoserine (By similarity).
FT   MOD_RES     399    399       Phosphoserine (By similarity).
FT   MOD_RES     406    406       Phosphoserine (By similarity).
FT   MOD_RES     413    413       Phosphoserine (By similarity).
FT   CONFLICT     84     84       D -> N (in Ref. 1; AAC67544).
FT   CONFLICT    248    248       T -> P (in Ref. 3; AAC96115).
FT   CONFLICT    285    285       F -> S (in Ref. 3; AAC96115).
FT   CONFLICT    546    546       W -> R (in Ref. 3; AAC96115).
SQ   SEQUENCE   559 AA;  63759 MW;  F2A617A27460FAC9 CRC64;
     MARTTSQLYD AVPIQSSVVL CSCPSPSMVR SQTEPGSSPG IPSGVSRQGS TMDGTTAEAR
     PSTNPLQQHP AQLPPQPRKK RPEDFKFGKI LGEGSFSTVV LARELATSRE YAIKILEKRH
     IIKENKVPYV TRERDVMSRL DHPFFVKLYF TFQDDEKLYF GLSYAKNGEL LKYIRKIGSF
     DETCTRFYTA EIVSALEYLH GKGIIHRDLK PENILLNEDM HIQITDFGTA KVLSPESKQA
     RANSFVGTAQ YVSPELLTEK SACKSSDLWA LGCIIYQLVA GLPPFRAGNE YLIFQKIIKL
     EYHFPEKFFP KARDLVEKLL VLDATKRLGC EEMEGYGPLK AHPFFETITW ENLHQQTPPK
     LTAYLPAMSE DDEDCYGNYD NLLSQFGFMQ VSSSSSSHSL STVETSLPQR SGSNIEQYIH
     DLDTNSFELD LQFSEDEKRL LLEKQAGGNP WHQFVENNLI LKMGPVDKRK GLFARRRQLL
     LTEGPHLYYV DPVNKVLKGE IPWSQELRPE AKNFKTFFVH TPNRTYYLMD PSGNAHKWCR
     KIQEVWRQQY QSNPDAAVQ
//
ID   DGAT1_MOUSE             Reviewed;         498 AA.
AC   Q9Z2A7; Q9D7Q5;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 82.
DE   RecName: Full=Diacylglycerol O-acyltransferase 1;
DE            EC=2.3.1.20;
DE   AltName: Full=Diglyceride acyltransferase;
GN   Name=Dgat1; Synonyms=Dgat;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=99007259; PubMed=9789033; DOI=10.1073/pnas.95.22.13018;
RA   Cases S., Smith S.J., Zheng Y.-W., Myers H.M., Lear S.R., Sande E.,
RA   Novak S., Collins C., Welch C.B., Lusis A.J., Erickson S.K.,
RA   Farese R.V. Jr.;
RT   "Identification of a gene encoding an acyl CoA:diacylglycerol
RT   acyltransferase, a key enzyme in triacylglycerol synthesis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:13018-13023(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=11959864; DOI=10.1074/jbc.M202013200;
RA   Buhman K.K., Smith S.J., Stone S.J., Repa J.J., Wong J.S.,
RA   Knapp F.F.R. Jr., Burri B.J., Hamilton R.L., Abumrad N.A.,
RA   Farese R.V. Jr.;
RT   "DGAT1 is not essential for intestinal triacylglycerol absorption or
RT   chylomicron synthesis.";
RL   J. Biol. Chem. 277:25474-25479(2002).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   MUTAGENESIS OF HIS-426, SUBUNIT, CATALYTIC ACTIVITY, SUBCELLULAR
RP   LOCATION, MEMBRANE TOPOLOGY, AND FUNCTION.
RX   PubMed=20876538; DOI=10.1074/jbc.M110.163691;
RA   McFie P.J., Stone S.L., Banman S.L., Stone S.J.;
RT   "Acyl CoA:Diacylglycerol acyltransferase-1 (DGAT1): topological
RT   orientation, identification of a putative active site histidine and
RT   the role of the N-terminus in dimer/tetramer formation.";
RL   J. Biol. Chem. 285:37377-37387(2010).
CC   -!- FUNCTION: Catalyzes the terminal and only committed step in
CC       triacylglycerol synthesis by using diacylglycerol and fatty acyl
CC       CoA as substrates. In contrast to DGAT2 it is not essential for
CC       survival. May be involved in VLDL (very low density lipoprotein)
CC       assembly.
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + 1,2-diacylglycerol = CoA +
CC       triacylglycerol.
CC   -!- PATHWAY: Lipid metabolism; glycerolipid metabolism.
CC   -!- SUBUNIT: Homodimer or homotetramer.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
CC   -!- DISRUPTION PHENOTYPE: Mice live well but display reduced
CC       postabsorptive chylomicronemia and accumulate neutral-lipid
CC       droplets in the cytoplasm of enterocytes when chronically fed a
CC       high fat diet.
CC   -!- SIMILARITY: Belongs to the membrane-bound acyltransferase family.
CC       Sterol o-acyltransferase subfamily.
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DR   EMBL; AF078752; AAC72917.1; -; mRNA.
DR   EMBL; AK008995; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC003717; AAH03717.1; -; mRNA.
DR   IPI; IPI00130963; -.
DR   RefSeq; NP_034176.1; NM_010046.2.
DR   UniGene; Mm.22633; -.
DR   STRING; Q9Z2A7; -.
DR   PhosphoSite; Q9Z2A7; -.
DR   PRIDE; Q9Z2A7; -.
DR   Ensembl; ENSMUST00000023214; ENSMUSP00000023214; ENSMUSG00000022555.
DR   GeneID; 13350; -.
DR   KEGG; mmu:13350; -.
DR   NMPDR; fig|10090.3.peg.30145; -.
DR   UCSC; uc007wkn.1; mouse.
DR   CTD; 13350; -.
DR   MGI; MGI:1333825; Dgat1.
DR   GeneTree; ENSGT00530000063122; -.
DR   HOGENOM; HBG326701; -.
DR   HOVERGEN; HBG051341; -.
DR   InParanoid; Q9Z2A7; -.
DR   OMA; GRFFQGN; -.
DR   OrthoDB; EOG4VT5X5; -.
DR   PhylomeDB; Q9Z2A7; -.
DR   BRENDA; 2.3.1.20; 244.
DR   NextBio; 283676; -.
DR   ArrayExpress; Q9Z2A7; -.
DR   Bgee; Q9Z2A7; -.
DR   CleanEx; MM_DGAT1; -.
DR   Genevestigator; Q9Z2A7; -.
DR   GermOnline; ENSMUSG00000022555; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003846; F:2-acylglycerol O-acyltransferase activity; IDA:MGI.
DR   GO; GO:0004144; F:diacylglycerol O-acyltransferase activity; IEA:EC.
DR   InterPro; IPR004299; MBOAT_fam.
DR   Pfam; PF03062; MBOAT; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN         1    498       Diacylglycerol O-acyltransferase 1.
FT                                /FTId=PRO_0000207655.
FT   TOPO_DOM      1     96       Cytoplasmic (Potential).
FT   TRANSMEM     97    118       Helical; (Potential).
FT   TOPO_DOM    119    230       Lumenal (Potential).
FT   TRANSMEM    231    240       Helical; (Potential).
FT   TOPO_DOM    241    241       Cytoplasmic (Potential).
FT   TRANSMEM    242    250       Helical; (Potential).
FT   TOPO_DOM    251    498       Lumenal (Potential).
FT   REGION        1    100       Involved in homomerization.
FT   ACT_SITE    426    426       Probable.
FT   MOD_RES      20     20       Phosphoserine.
FT   MUTAGEN     426    426       H->A: Impairs the ability to synthesize
FT                                triacylglycerols, as well as retinyl and
FT                                wax esters, in an in vitro
FT                                acyltransferase assay.
SQ   SEQUENCE   498 AA;  56790 MW;  E7B0DD6DDCF1EC2B CRC64;
     MGDRGGAGSS RRRRTGSRVS VQGGSGPKVE EDEVRDAAVS PDLGAGGDAP APAPAPAHTR
     DKDGRTSVGD GYWDLRCHRL QDSLFSSDSG FSNYRGILNW CVVMLILSNA RLFLENLIKY
     GILVDPIQVV SLFLKDPYSW PAPCVIIASN IFVVAAFQIE KRLAVGALTE QMGLLLHVVN
     LATIICFPAA VALLVESITP VGSVFALASY SIMFLKLYSY RDVNLWCRQR RVKAKAVSTG
     KKVSGAAAQQ AVSYPDNLTY RDLYYFIFAP TLCYELNFPR SPRIRKRFLL RRVLEMLFFT
     QLQVGLIQQW MVPTIQNSMK PFKDMDYSRI IERLLKLAVP NHLIWLIFFY WFFHSCLNAV
     AELLQFGDRE FYRDWWNAES VTYFWQNWNI PVHKWCIRHF YKPMLRHGSS KWVARTGVFL
     TSAFFHEYLV SVPLRMFRLW AFTAMMAQVP LAWIVGRFFQ GNYGNAAVWV TLIIGQPVAV
     LMYVHDYYVL NYDAPVGV
//
ID   E2AK3_MOUSE             Reviewed;        1114 AA.
AC   Q9Z2B5; Q9CTK8; Q9CWT5;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 102.
DE   RecName: Full=Eukaryotic translation initiation factor 2-alpha kinase 3;
DE            EC=2.7.11.1;
DE   AltName: Full=PRKR-like endoplasmic reticulum kinase;
DE   AltName: Full=Pancreatic eIF2-alpha kinase;
DE   Flags: Precursor;
GN   Name=Eif2ak3; Synonyms=Pek, Perk;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF LYS-618.
RC   STRAIN=NIH Swiss; TISSUE=Fibroblast;
RX   MEDLINE=99127894; PubMed=9930704; DOI=10.1038/16729;
RA   Harding H.P., Zhang Y., Ron D.;
RT   "Protein translation and folding are coupled by an endoplasmic-
RT   reticulum-resident kinase.";
RL   Nature 397:271-274(1999).
RN   [2]
RP   ERRATUM.
RA   Harding H.P., Zhang Y., Ron D.;
RL   Nature 398:90-90(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-152 AND 769-1114.
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   SUBUNIT.
RX   MEDLINE=20313073; PubMed=10854322; DOI=10.1038/35014014;
RA   Bertolotti A., Zhang Y., Hendershot L.M., Harding H.P., Ron D.;
RT   "Dynamic interaction of BiP and ER stress transducers in the unfolded-
RT   protein response.";
RL   Nat. Cell Biol. 2:326-332(2000).
RN   [5]
RP   FUNCTION.
RX   MEDLINE=20524051; PubMed=11035797; DOI=10.1073/pnas.220247197;
RA   Brewer J.W., Diehl J.A.;
RT   "PERK mediates cell-cycle exit during the mammalian unfolded protein
RT   response.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12625-12630(2000).
RN   [6]
RP   INTERACTION WITH DNAJC3.
RX   PubMed=12446838; DOI=10.1073/pnas.252341799;
RA   Yan W., Frank C.L., Korth M.J., Sopher B.L., Novoa I., Ron D.,
RA   Katze M.G.;
RT   "Control of PERK eIF2alpha kinase activity by the endoplasmic
RT   reticulum stress-induced molecular chaperone P58IPK.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:15920-15925(2002).
CC   -!- FUNCTION: Phosphorylates the alpha subunit of eukaryotic
CC       translation-initiation factor 2 (EIF2), leading to its
CC       inactivation and thus to a rapid reduction of translational
CC       initiation and repression of global protein synthesis. Serves as a
CC       critical effector of unfolded protein response (UPR)-induced G1
CC       growth arrest due to the loss of cyclin D1.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Perturbation in protein folding in the
CC       endoplasmic reticulum (ER) promotes reversible dissociation from
CC       HSPA5/BIP and oligomerization, resulting in
CC       transautophosphorylation and kinase activity induction.
CC   -!- SUBUNIT: Forms dimers with HSPA5/BIP in resting cells.
CC       Oligomerizes in ER-stressed cells. Interacts with DNAJC3.
CC   -!- INTERACTION:
CC       P05198:EIF2S1 (xeno); NbExp=4; IntAct=EBI-1226344, EBI-1056162;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC       type I membrane protein.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- INDUCTION: By ER stress.
CC   -!- DOMAIN: The lumenal domain senses perturbations in protein folding
CC       in the ER, probably through reversible interaction with HSPA5/BIP.
CC   -!- PTM: Autophosphorylated.
CC   -!- PTM: N-glycosylated.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. GCN2 subfamily.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF076681; AAD03337.1; -; mRNA.
DR   EMBL; AK010397; BAB26908.1; -; mRNA.
DR   EMBL; AK003226; BAB22655.1; -; mRNA.
DR   IPI; IPI00131000; -.
DR   PIR; T14351; T14351.
DR   UniGene; Mm.247167; -.
DR   ProteinModelPortal; Q9Z2B5; -.
DR   SMR; Q9Z2B5; 100-130, 303-333, 582-1078.
DR   IntAct; Q9Z2B5; 4.
DR   STRING; Q9Z2B5; -.
DR   PhosphoSite; Q9Z2B5; -.
DR   PRIDE; Q9Z2B5; -.
DR   Ensembl; ENSMUST00000034093; ENSMUSP00000034093; ENSMUSG00000031668.
DR   MGI; MGI:1341830; Eif2ak3.
DR   GeneTree; ENSGT00530000062984; -.
DR   HOGENOM; HBG356284; -.
DR   HOVERGEN; HBG051431; -.
DR   InParanoid; Q9Z2B5; -.
DR   OrthoDB; EOG4R23T6; -.
DR   BRENDA; 2.7.11.1; 244.
DR   ArrayExpress; Q9Z2B5; -.
DR   Bgee; Q9Z2B5; -.
DR   Genevestigator; Q9Z2B5; -.
DR   GermOnline; ENSMUSG00000031668; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004694; F:eukaryotic translation initiation factor 2alpha kinase activity; ISS:UniProtKB.
DR   GO; GO:0006919; P:activation of caspase activity; IMP:MGI.
DR   GO; GO:0030282; P:bone mineralization; IMP:MGI.
DR   GO; GO:0019722; P:calcium-mediated signaling; IMP:MGI.
DR   GO; GO:0002063; P:chondrocyte development; IMP:MGI.
DR   GO; GO:0031018; P:endocrine pancreas development; ISS:UniProtKB.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; IMP:MGI.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISS:UniProtKB.
DR   GO; GO:0006983; P:ER overload response; ISS:UniProtKB.
DR   GO; GO:0045444; P:fat cell differentiation; IDA:MGI.
DR   GO; GO:0030073; P:insulin secretion; IMP:MGI.
DR   GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; IMP:MGI.
DR   GO; GO:0007595; P:lactation; IMP:MGI.
DR   GO; GO:0031642; P:negative regulation of myelination; IMP:MGI.
DR   GO; GO:0032092; P:positive regulation of protein binding; IMP:MGI.
DR   GO; GO:0009967; P:positive regulation of signal transduction; IDA:MGI.
DR   GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR   GO; GO:0019217; P:regulation of fatty acid metabolic process; IMP:MGI.
DR   GO; GO:0032933; P:SREBP-mediated signaling pathway; IDA:MGI.
DR   GO; GO:0006412; P:translation; IDA:MGI.
DR   GO; GO:0006926; P:virus-infected cell apoptosis; IMP:MGI.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR011047; Quino_AlcDH-like.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   Gene3D; G3DSA:2.140.10.10; Quinoprotein_alc_DH-like; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50998; Quin_alc_DH_like; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; FALSE_NEG.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Endoplasmic reticulum; Glycoprotein; Kinase; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase;
KW   Signal; Stress response; Transferase; Translation regulation;
KW   Transmembrane; Transmembrane helix; Unfolded protein response.
FT   SIGNAL        1     28       Potential.
FT   CHAIN        29   1114       Eukaryotic translation initiation factor
FT                                2-alpha kinase 3.
FT                                /FTId=PRO_0000024323.
FT   TOPO_DOM     29    510       Lumenal (Potential).
FT   TRANSMEM    511    531       Helical; (Potential).
FT   TOPO_DOM    532   1114       Cytoplasmic (Potential).
FT   DOMAIN      589   1075       Protein kinase.
FT   NP_BIND     595    603       ATP (By similarity).
FT   COMPBIAS     48     51       Poly-Ala.
FT   COMPBIAS    224    229       Poly-Glu.
FT   ACT_SITE    935    935       Proton acceptor (By similarity).
FT   BINDING     618    618       ATP.
FT   MOD_RES     711    711       Phosphoserine (By similarity).
FT   CARBOHYD    254    254       N-linked (GlcNAc...).
FT   MUTAGEN     618    618       K->A: Loss of activity and
FT                                autophosphorylation.
FT   CONFLICT    143    152       VFGNKMIIPS -> GTHKTSSKEC (in Ref. 3;
FT                                BAB26908).
FT   CONFLICT    826    826       Missing (in Ref. 3; BAB22655).
SQ   SEQUENCE   1114 AA;  124682 MW;  65A47D6C0DD2E046 CRC64;
     MERATRPGPR ALLLLLFLLL GCAAGISAVA PARSLLAPAS ETVFGLGAAA APTSAARVPA
     VATAEVTVED AEALPAAAGE PESRATEPDD DVELRPRGRS LVIISTLDGR IAALDAENDG
     KKQWDLDVGS GSLVSSSLSK PEVFGNKMII PSLDGDLFQW DRDRESMEAV PFTVESLLES
     SYKFGDDVVL VGGKSLITYG LSAYSGKLRY ICSALGCRRW DSDEMEEEED ILLLQRTQKT
     VRAVGPRSGS EKWNFSVGHF ELRYIPDMET RAGFIESTFK PGGNKEDSKI ISDVEEQEAT
     MLDTVIKVSV ADWKVMAFSR KGGRLEWEYQ FCTPIASAWL VRDGKVIPIS LFDDTSYTAS
     EEALGDEEDI VEAARGATEN SVYLGMYRGQ LYLQSSVRVS EKFPTSPKAL ESVNGENAII
     PLPTIKWKPL IHSPSRTPVL VGSDEFDKCL SNDKYSHEEY SNGALSILQY PYDNGYYLPY
     YKRERNKRST QITVRFLDSP HYSKNIRKKD PILLLHWWKE IFGTILLCIV ATTFIVRRLF
     HPQPHRQRKE SETQCQTESK YDSVSADVSD NSWNDMKYSG YVSRYLTDFE PIQCMGRGGF
     GVVFEAKNKV DDCNYAIKRI RLPNRELARE KVMREVKALA KLEHPGIVRY FNAWLETPPE
     KWQEEMDEIW LKDESTDWPL SSPSPMDAPS VKIRRMDPFS TKEQIEVIAP SPERSRSFSV
     GISCGQTSSS ESQFSPLEFS GTDCGDNSDS ADAAYNLQDS CLTDCEDVED GTVDGNDEGH
     SFELCPSEAS PYTRSREGTS SSIVFEDSGC GNASSKEEPR GNRLHDGNHY VNKLTDLKCS
     SSRSSSEATT LSTSPTRPTT LSLDFTKNTV GQLQPSSPKV YLYIQMQLCR KENLKDWMNR
     RCSLEDREHG VCLHIFLQIA EAVEFLHSKG LMHRDLKPSN IFFTMDDVVK VGDFGLVTAM
     DQDEEEQTVL TPMPAYATHT GQVGTKLYMS PEQIHGNNYS HKVDIFSLGL ILFELLYPFS
     TQMERVRILT DVRNLKFPLL FTQKYPQEHM MVQDMLSPSP TERPEATDII ENAIFENLEF
     PGKTVLRQRS RSMSSSGTKH SRQPSCSYSP LPGN
//
ID   KS6A4_MOUSE             Reviewed;         773 AA.
AC   Q9Z2B9; Q91X18;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Ribosomal protein S6 kinase alpha-4;
DE            Short=S6K-alpha-4;
DE            EC=2.7.11.1;
DE   AltName: Full=90 kDa ribosomal protein S6 kinase 4;
DE   AltName: Full=Nuclear mitogen- and stress-activated protein kinase 2;
DE   AltName: Full=RSK-like protein kinase;
DE            Short=RLSK;
GN   Name=Rps6ka4; Synonyms=Msk2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98353467; PubMed=9687510; DOI=10.1093/emboj/17.15.4426;
RA   Deak M., Clifton A.D., Lucocq J.M., Alessi D.R.;
RT   "Mitogen- and stress-activated protein kinase-1 (MSK1) is directly
RT   activated by MAPK and SAPK2/p38, and may mediate activation of CREB.";
RL   EMBO J. 17:4426-4441(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
RX   PubMed=16517600; DOI=10.1074/jbc.M513333200;
RA   Duncan E.A., Anest V., Cogswell P., Baldwin A.S.;
RT   "The kinases MSK1 and MSK2 are required for epidermal growth factor-
RT   induced, but not tumor necrosis factor-induced, histone H3 Ser10
RT   phosphorylation.";
RL   J. Biol. Chem. 281:12521-12525(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343 AND SER-347, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-745, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Serine/threonine kinase that may play a role in
CC       mediating the growth-factor and stress induced activation of the
CC       transcription factor CREB. Essential role in the control of RELA
CC       transcriptional activity in response to TNF (By similarity).
CC       Mediates the mitogen- and stress-induced phosphorylation of high
CC       mobility group protein 14 (HMG-14) (By similarity). Phosphorylates
CC       'Ser-10' of histone H3 in response to mitogenics, stress stimuli
CC       and epidemal growth-factor (EGF) and result in the transcriptional
CC       activation of several immediate early genes, including proto-
CC       oncogenes FOS and JUN.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- ENZYME REGULATION: Appears to be activated by multiple
CC       phosphorylations on threonine and serine residues. ERK1/2 and p38
CC       kinases may play a role in this process (By similarity).
CC   -!- SUBUNIT: Forms a complex with either ERK1 or ERK2 in quiescent
CC       cells which transiently dissociates following mitogenic
CC       stimulation. Also associates with MAPK14/p38-alpha. Activated
CC       RPS6KA4 associates with and phosphorylates the NF-kappa-B p65
CC       subunit RELA (By similarity).
CC   -!- INTERACTION:
CC       P63085:Mapk1; NbExp=2; IntAct=EBI-412887, EBI-397697;
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity).
CC   -!- MISCELLANEOUS: Enzyme activity requires the presence of both
CC       kinase domains (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. S6 kinase subfamily.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC   -!- SIMILARITY: Contains 2 protein kinase domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF074714; AAC67394.1; -; mRNA.
DR   EMBL; BC012964; AAH12964.1; -; mRNA.
DR   IPI; IPI00131006; -.
DR   RefSeq; NP_064308.1; NM_019924.1.
DR   UniGene; Mm.20914; -.
DR   ProteinModelPortal; Q9Z2B9; -.
DR   SMR; Q9Z2B9; 12-364, 400-716.
DR   IntAct; Q9Z2B9; 3.
DR   STRING; Q9Z2B9; -.
DR   PhosphoSite; Q9Z2B9; -.
DR   PRIDE; Q9Z2B9; -.
DR   Ensembl; ENSMUST00000025903; ENSMUSP00000025903; ENSMUSG00000024952.
DR   GeneID; 56613; -.
DR   KEGG; mmu:56613; -.
DR   UCSC; uc008gja.1; mouse.
DR   CTD; 56613; -.
DR   MGI; MGI:1930076; Rps6ka4.
DR   GeneTree; ENSGT00600000084335; -.
DR   HOGENOM; HBG315633; -.
DR   HOVERGEN; HBG108317; -.
DR   InParanoid; Q9Z2B9; -.
DR   OrthoDB; EOG4VMFDS; -.
DR   PhylomeDB; Q9Z2B9; -.
DR   BRENDA; 2.7.11.1; 244.
DR   NextBio; 313035; -.
DR   ArrayExpress; Q9Z2B9; -.
DR   Bgee; Q9Z2B9; -.
DR   CleanEx; MM_RPS6KA4; -.
DR   Genevestigator; Q9Z2B9; -.
DR   GermOnline; ENSMUSG00000024952; Mus musculus.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0048273; F:mitogen-activated protein kinase p38 binding; ISS:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0007243; P:intracellular protein kinase cascade; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; ISS:UniProtKB.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR016239; Ribosomal_S6_kinase_II.
DR   InterPro; IPR017442; Se/Thr_prot_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_prot_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 2.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   PIRSF; PIRSF000606; Ribsml_S6_kin_2; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF56112; Kinase_like; 2.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Repeat; Serine/threonine-protein kinase; Transferase.
FT   CHAIN         1    773       Ribosomal protein S6 kinase alpha-4.
FT                                /FTId=PRO_0000086206.
FT   DOMAIN       33    301       Protein kinase 1.
FT   DOMAIN      302    371       AGC-kinase C-terminal.
FT   DOMAIN      417    674       Protein kinase 2.
FT   NP_BIND      39     47       ATP (By similarity).
FT   NP_BIND     417    425       ATP (By similarity).
FT   ACT_SITE    161    161       Proton acceptor (By similarity).
FT   ACT_SITE    530    530       Proton acceptor (By similarity).
FT   BINDING      65     65       ATP (By similarity).
FT   BINDING     440    440       ATP (By similarity).
FT   MOD_RES     196    196       Phosphoserine (By similarity).
FT   MOD_RES     342    342       Phosphotyrosine (By similarity).
FT   MOD_RES     343    343       Phosphoserine.
FT   MOD_RES     347    347       Phosphoserine.
FT   MOD_RES     360    360       Phosphoserine (By similarity).
FT   MOD_RES     542    542       Phosphothreonine (By similarity).
FT   MOD_RES     568    568       Phosphothreonine (By similarity).
FT   MOD_RES     634    634       Phosphoserine (By similarity).
FT   MOD_RES     678    678       Phosphoserine (By similarity).
FT   MOD_RES     681    681       Phosphoserine (By similarity).
FT   MOD_RES     682    682       Phosphoserine (By similarity).
FT   MOD_RES     687    687       Phosphothreonine (By similarity).
FT   MOD_RES     737    737       Phosphoserine (By similarity).
FT   MOD_RES     745    745       Phosphoserine.
FT   CONFLICT    307    307       W -> V (in Ref. 2; AAH12964).
FT   CONFLICT    343    343       S -> P (in Ref. 2; AAH12964).
SQ   SEQUENCE   773 AA;  85739 MW;  4B3F9D00114957C4 CRC64;
     MGDEDEDEGC AVELQITEAN LTGHEEKVSV ENFALLKVLG TGAYGKVFLV RKTGGHDAGK
     LYAMKVLRKA ALVQRAKTQE HTRTERSVLE LVRQAPFLVT LHYAFQTDAK LHLILDYVSG
     GEMFTHLYQR QYFKEAEVRV YGGEIVLALE HLHKLGIIYR DLKLENVLLD SEGHIVLTDF
     GLSKEFLTEE KERTFSFCGT IEYMAPEIIR SKAGHGKAVD WWSLGILLFE LLTGASPFTL
     EGERNTQAEV SRRILKCSPP FPLRIGPVAQ DLLQRLLCKD PKKRLGAGPQ GAQEVKSHPF
     FQGLDWWALA ARKIPAPFRP QIRSELDVGN FAEEFTRLEP VYSPAGSPPP GDPRIFQGYS
     FVAPSILFDH NNAVMADVLQ APGAGYRPGR AAVARSAMMQ DSPFFQQYEL DLREPALGQG
     SFSVCRRCRQ RQSGQEFAVK ILSRRLEENT QREVAALRLC QSHPNVVNLH EVLHDQLHTY
     LVLELLRGGE LLEHIRKKRL FSESEASQIL RSLVSAVSFM HEEAGVVHRD LKPENILYAD
     DTPGAPVKII DFGFARLRPQ SPAEPMQTPC FTLQYAAPEL LAQQGYDESC DLWSLGVILY
     MMLSGQVPFQ GASGQGGQSQ AAEIMCKIRE GRFSLDGEAW QGVSEEAKEL VRGLLTVDPA
     KRLKLEGLRS SSWLQDGSAR SSPPLRTPDV LESSGPAVRS GLNATFMAFN RGKREGFFLK
     SVENAPLAKR RKQKLRSAAA SRRGSPVPAS SGRLPASAAK GTTRRANGPL SPS
//
ID   MTMR1_MOUSE             Reviewed;         669 AA.
AC   Q9Z2C4;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Myotubularin-related protein 1;
DE            EC=3.1.3.-;
GN   Name=Mtmr1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=98409499; PubMed=9736772; DOI=10.1093/hmg/7.11.1703;
RA   Laporte J., Blondeau F., Buj-Bello A., Tentler D., Kretz C., Dahl N.,
RA   Mandel J.-L.;
RT   "Characterization of the myotubularin dual specificity phosphatase
RT   gene family from yeast to human.";
RL   Hum. Mol. Genet. 7:1703-1712(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Wiehe T., Zhao W., Herman G.E., Rosenthal A., Platzer M.;
RT   "Comparative sequence analysis of the mouse Mtm locus and the
RT   corresponding region of human Xq28.";
RL   Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Lipid phosphatase that acts on phosphatidylinositol 3-
CC       phosphate and phosphatidylinositol (3,5)-bisphosphate (By
CC       similarity).
CC   -!- SUBUNIT: Interacts with MTMR12 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC       Cytoplasmic side (By similarity).
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class myotubularin subfamily.
CC   -!- SIMILARITY: Contains 1 GRAM domain.
CC   -!- SIMILARITY: Contains 1 myotubularin phosphatase domain.
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DR   EMBL; AF073997; AAC77822.1; -; mRNA.
DR   EMBL; AF125314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC056376; AAH56376.1; -; mRNA.
DR   EMBL; BC057337; AAH57337.1; -; mRNA.
DR   IPI; IPI00875081; -.
DR   RefSeq; NP_058681.1; NM_016985.2.
DR   UniGene; Mm.219672; -.
DR   ProteinModelPortal; Q9Z2C4; -.
DR   SMR; Q9Z2C4; 99-610.
DR   STRING; Q9Z2C4; -.
DR   PhosphoSite; Q9Z2C4; -.
DR   PRIDE; Q9Z2C4; -.
DR   Ensembl; ENSMUST00000015358; ENSMUSP00000015358; ENSMUSG00000015214.
DR   GeneID; 53332; -.
DR   KEGG; mmu:53332; -.
DR   UCSC; uc009tjt.1; mouse.
DR   CTD; 53332; -.
DR   MGI; MGI:1858271; Mtmr1.
DR   GeneTree; ENSGT00580000081198; -.
DR   HOVERGEN; HBG000220; -.
DR   PhylomeDB; Q9Z2C4; -.
DR   NextBio; 310157; -.
DR   ArrayExpress; Q9Z2C4; -.
DR   Bgee; Q9Z2C4; -.
DR   CleanEx; MM_MTMR1; -.
DR   Genevestigator; Q9Z2C4; -.
DR   GermOnline; ENSMUSG00000015214; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IDA:MGI.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR   InterPro; IPR004182; GRAM.
DR   InterPro; IPR010569; Myotub-related.
DR   InterPro; IPR017906; Myotubularin_phosphatase_dom.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   Pfam; PF02893; GRAM; 1.
DR   Pfam; PF06602; Myotub-related; 1.
DR   SMART; SM00568; GRAM; 1.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cell membrane; Hydrolase; Membrane; Phosphoprotein.
FT   CHAIN         1    669       Myotubularin-related protein 1.
FT                                /FTId=PRO_0000094933.
FT   DOMAIN       94    165       GRAM.
FT   DOMAIN      230    605       Myotubularin phosphatase.
FT   REGION      355    358       Substrate binding (By similarity).
FT   REGION      380    381       Substrate binding (By similarity).
FT   REGION      442    448       Substrate binding (By similarity).
FT   ACT_SITE    442    442       Phosphocysteine intermediate (By
FT                                similarity).
FT   BINDING     488    488       Substrate (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      47     47       Phosphoserine.
SQ   SEQUENCE   669 AA;  75313 MW;  1856792245F2D800 CRC64;
     MDRPVAAAAA ASAASCEGAG GPGPGPGASW RPSRVAGGAS ASSRHPSIET LDSPTGSHVE
     WCKQLIAATI SSQISGSVTS ENVSRDYKAL RDGNKLAQME EAPLFPGESI KAIVKDVIYI
     CPFMGAVSGT LTVTDFKMYF KNVERDPHFV LDVPLGVISR VEKIGAQSHG DNSCGIEIVC
     KDMRNLRLAY KQEEQRKLGI FENLNKHAFP LSNGQVLFAF NYKEKFPVNG WKVYDPVSEY
     KRQGLPNESW KISKINSNYE FCDTYPAIIV VPTSVKDDDL SKVAAFRAKG RVPVLSWIHP
     ESQATITRCS QPLVGPNDKR CKEDEKYLQT IMDANAQSHK LTIFDARQNS VADTNKAKGG
     GYENESAYPN AELIFLEIHN IHVMRESLRK LKEIVYPSID ESHWLSNVDG THWLEYIRVL
     LAGAVRIADK IESGKTSVVI HCSDGWDRTS QLTSLAMLML DSYYRTIKGF EALIEKEWIS
     FGHRFALRVG HGDDNHADAD RSPIFLQFID CVWQMTRQFP SAFEFNELFL ITILDHLYSC
     LFGTFLCNCE QQRIKEDVYT NTISLWSYIN SQLDEFSNPF FVNYENHVLY PVASMSHLEL
     WVNYYVRWNP RMRPQMPIHQ NLKELLAIKA ELQKRVEDLQ REMATRTISS SSERGSSPTH
     SATPVHTSV
//
ID   MTMR7_MOUSE             Reviewed;         660 AA.
AC   Q9Z2C9; Q8C4J6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2003, sequence version 2.
DT   08-MAR-2011, entry version 83.
DE   RecName: Full=Myotubularin-related protein 7;
DE            EC=3.1.3.-;
GN   Name=Mtmr7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 291-602.
RX   MEDLINE=98409499; PubMed=9736772; DOI=10.1093/hmg/7.11.1703;
RA   Laporte J., Blondeau F., Buj-Bello A., Tentler D., Kretz C., Dahl N.,
RA   Mandel J.-L.;
RT   "Characterization of the myotubularin dual specificity phosphatase
RT   gene family from yeast to human.";
RL   Hum. Mol. Genet. 7:1703-1712(1998).
CC   -!- FUNCTION: Phosphatase that acts on lipids with a phosphoinositol
CC       headgroup (By similarity).
CC   -!- SUBUNIT: Interacts with MTMR6, MTMR8 and MTMR9 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class myotubularin subfamily.
CC   -!- SIMILARITY: Contains 1 myotubularin phosphatase domain.
CC   -----------------------------------------------------------------------
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DR   EMBL; AK081973; BAC38383.1; -; mRNA.
DR   EMBL; AF073882; AAC80004.1; -; mRNA.
DR   IPI; IPI00131035; -.
DR   RefSeq; NP_001035789.1; NM_001040699.1.
DR   UniGene; Mm.480344; -.
DR   ProteinModelPortal; Q9Z2C9; -.
DR   SMR; Q9Z2C9; 6-509.
DR   STRING; Q9Z2C9; -.
DR   PRIDE; Q9Z2C9; -.
DR   Ensembl; ENSMUST00000048890; ENSMUSP00000043367; ENSMUSG00000039431.
DR   GeneID; 54384; -.
DR   KEGG; mmu:54384; -.
DR   UCSC; uc009lmz.1; mouse.
DR   CTD; 54384; -.
DR   MGI; MGI:1891693; Mtmr7.
DR   eggNOG; roNOG10456; -.
DR   GeneTree; ENSGT00580000081198; -.
DR   HOGENOM; HBG444628; -.
DR   HOVERGEN; HBG000220; -.
DR   InParanoid; Q9Z2C9; -.
DR   OMA; IANTPQD; -.
DR   OrthoDB; EOG4WH8K8; -.
DR   PhylomeDB; Q9Z2C9; -.
DR   NextBio; 311216; -.
DR   ArrayExpress; Q9Z2C9; -.
DR   Bgee; Q9Z2C9; -.
DR   CleanEx; MM_MTMR7; -.
DR   Genevestigator; Q9Z2C9; -.
DR   GermOnline; ENSMUSG00000039431; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0004437; F:inositol or phosphatidylinositol phosphatase activity; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR   InterPro; IPR010569; Myotub-related.
DR   InterPro; IPR017906; Myotubularin_phosphatase_dom.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   Pfam; PF06602; Myotub-related; 1.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase.
FT   CHAIN         1    660       Myotubularin-related protein 7.
FT                                /FTId=PRO_0000094941.
FT   DOMAIN      126    504       Myotubularin phosphatase.
FT   REGION      250    253       Substrate binding (By similarity).
FT   REGION      275    276       Substrate binding (By similarity).
FT   REGION      338    344       Substrate binding (By similarity).
FT   ACT_SITE    338    338       Phosphocysteine intermediate (By
FT                                similarity).
FT   BINDING     384    384       Substrate (By similarity).
FT   CONFLICT    579    602       PQDYSGNSKSFPSRSPSQGDEDSA -> LRITVGTASPSHP
FT                                GARPRVMKILL (in Ref. 2).
SQ   SEQUENCE   660 AA;  75608 MW;  57CA1A447192A52B CRC64;
     MEHIRTPKVE NVRLVDRVSC KKAALGTLYL TATHVIFVEN APDTRKETWI LHSQISTIEK
     QATTATGCPL LIRCKNFQIV QLVIPQERDC HDVYISLIRL ARPVKYEELY CFSFNPKLDK
     EEREQGWLLV DLSEEYKRMG LPDNYWQLSD VNRDYRVCDS YPTELYVPRS ATAHIIVGSS
     KFRSRRRFPA LSYYCKDSHA SICRSSQPLS GFSARCLEDE QMLQAIRKAN PGSDFIYVVD
     TRPKLNAMAN RAAGKGYENE DNYSNIKFQF IGIENIHVMR NSLQKMLEVC ELKSPSMSDF
     LWGLENSGWL RHIKAIMDAG IFIAKAVSEE GASVLVHCSD GWDRTAQVCS VASLLLDPYY
     RTLKGFMVLI EKDWISFGHK FNHRYGNLDG DPKEISPVID QFIECVWQLT EQFPCAFEFN
     ERFLTHIQHH VYSCQFGNFL CNSQKERREL KIQERTYSLW SNLWKNRADY LNPLFRADHS
     QTQGSLHLPT APCNFTYKFW NGMYNRFEKG LQPRQSVTDY LMAVKEESQQ LEEELESLEE
     RLEKIQKVHL HGTKVKSKQS EPSKHSGFST SDHSTANTPQ DYSGNSKSFP SRSPSQGDED
     SALILTQDNL KSSDPDLSVN SDQESGVEDL SCRSPSGGEH APSEDSGKDR DSDEAVFLTA
//
ID   MTMR2_MOUSE             Reviewed;         643 AA.
AC   Q9Z2D1; Q8VHA7;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2003, sequence version 2.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Myotubularin-related protein 2;
DE            EC=3.1.3.-;
GN   Name=Mtmr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Bolino A., Marigo V., Loader J., Romio L., Leoni A., Di Duca M.,
RA   Cinti R., Feltri M.L., Wrabetz L., Ravazzolo R., Monaco A.P.;
RT   "Molecular characterization and expression analysis of Mtmr2, mouse
RT   homolog of MTMR2, the myotubularin-related 2 gene, mutated in CMT4B.";
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-225.
RX   MEDLINE=98409499; PubMed=9736772; DOI=10.1093/hmg/7.11.1703;
RA   Laporte J., Blondeau F., Buj-Bello A., Tentler D., Kretz C., Dahl N.,
RA   Mandel J.-L.;
RT   "Characterization of the myotubularin dual specificity phosphatase
RT   gene family from yeast to human.";
RL   Hum. Mol. Genet. 7:1703-1712(1998).
RN   [3]
RP   FUNCTION, MUTAGENESIS OF GLY-103, AND TISSUE SPECIFICITY.
RX   PubMed=12045210; DOI=10.1093/hmg/11.13.1569;
RA   Berger P., Bonneick S., Willi S., Wymann M., Suter U.;
RT   "Loss of phosphatase activity in myotubularin-related protein 2 is
RT   associated with Charcot-Marie-Tooth disease type 4B1.";
RL   Hum. Mol. Genet. 11:1569-1579(2002).
RN   [4]
RP   SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-103 AND CYS-417, AND SUBUNIT.
RX   PubMed=14530412; DOI=10.1073/pnas.2132732100;
RA   Berger P., Schaffitzel C., Berger I., Ban N., Suter U.;
RT   "Membrane association of myotubularin-related protein 2 is mediated by
RT   a pleckstrin homology-GRAM domain and a coiled-coil dimerization
RT   module.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:12177-12182(2003).
CC   -!- FUNCTION: Phosphatase that acts on lipids with a phosphoinositol
CC       headgroup. Has phosphatase activity towards phosphatidylinositol-
CC       3-phosphate and phosphatidylinositol-3,5-bisphosphate. Binds
CC       phosphatidylinositol-4-phosphate, hosphatidylinositol-5-phosphate,
CC       phosphatidylinositol-3,5-bisphosphate and phosphatidylinositol-
CC       3,4,5-trisphosphate.
CC   -!- ENZYME REGULATION: interaction with SBF1 increases phosphatase
CC       activity (By similarity).
CC   -!- SUBUNIT: Homooligomer and heterooligomer. Interacts with SBF1 and
CC       SBF2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
CC       protein. Note=Partly associated with membranes.
CC   -!- TISSUE SPECIFICITY: Detected in fetal forebrain, dorsal root
CC       ganglia, trigeminal ganglia, kidney, adrenal gland and lung.
CC       Detected in adult dorsal root ganglia, neurons of the central
CC       nervous system, motor neurons, cell soma and neurites of sensory
CC       neurons, olfactory bulb, cerebellum and hippocampus.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Non-receptor class myotubularin subfamily.
CC   -!- SIMILARITY: Contains 1 GRAM domain.
CC   -!- SIMILARITY: Contains 1 myotubularin phosphatase domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC80002.1; Type=Erroneous initiation;
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DR   EMBL; AY055832; AAL14198.1; -; mRNA.
DR   EMBL; AF073880; AAC80002.1; ALT_INIT; mRNA.
DR   IPI; IPI00128196; -.
DR   RefSeq; NP_076347.3; NM_023858.3.
DR   UniGene; Mm.210405; -.
DR   ProteinModelPortal; Q9Z2D1; -.
DR   SMR; Q9Z2D1; 73-585.
DR   STRING; Q9Z2D1; -.
DR   PhosphoSite; Q9Z2D1; -.
DR   PRIDE; Q9Z2D1; -.
DR   Ensembl; ENSMUST00000034396; ENSMUSP00000034396; ENSMUSG00000031918.
DR   Ensembl; ENSMUST00000115652; ENSMUSP00000111316; ENSMUSG00000031918.
DR   GeneID; 77116; -.
DR   KEGG; mmu:77116; -.
DR   UCSC; uc009ody.1; mouse.
DR   CTD; 77116; -.
DR   MGI; MGI:1924366; Mtmr2.
DR   GeneTree; ENSGT00580000081198; -.
DR   HOGENOM; HBG444628; -.
DR   HOVERGEN; HBG000220; -.
DR   InParanoid; Q9Z2D1; -.
DR   OrthoDB; EOG4GMTWP; -.
DR   PhylomeDB; Q9Z2D1; -.
DR   NextBio; 346504; -.
DR   ArrayExpress; Q9Z2D1; -.
DR   Bgee; Q9Z2D1; -.
DR   CleanEx; MM_MTMR2; -.
DR   Genevestigator; Q9Z2D1; -.
DR   GermOnline; ENSMUSG00000031918; Mus musculus.
DR   GO; GO:0005774; C:vacuolar membrane; IDA:MGI.
DR   GO; GO:0004437; F:inositol or phosphatidylinositol phosphatase activity; IDA:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:MGI.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
DR   GO; GO:0051262; P:protein tetramerization; IPI:MGI.
DR   InterPro; IPR004182; GRAM.
DR   InterPro; IPR010569; Myotub-related.
DR   InterPro; IPR017906; Myotubularin_phosphatase_dom.
DR   InterPro; IPR000387; Tyr/Dual-specificity_Pase.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   Pfam; PF02893; GRAM; 1.
DR   Pfam; PF06602; Myotub-related; 1.
DR   SMART; SM00568; GRAM; 1.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Membrane; Phosphoprotein.
FT   CHAIN         1    643       Myotubularin-related protein 2.
FT                                /FTId=PRO_0000094935.
FT   DOMAIN       68    139       GRAM.
FT   DOMAIN      205    580       Myotubularin phosphatase.
FT   COMPBIAS      4     53       Ser-rich.
FT   ACT_SITE    417    417       Phosphocysteine intermediate.
FT   MOD_RES      58     58       Phosphoserine (By similarity).
FT   MUTAGEN     103    103       G->E: Severely impaired intraction with
FT                                membranes and strongly reduced catalytic
FT                                activity.
FT   MUTAGEN     417    417       C->A: Loss of activity.
SQ   SEQUENCE   643 AA;  73256 MW;  E577B41175C2792F CRC64;
     MEKSSSCESL GAQLPAARLP SEDSLSSAST SHSENSVHTK SASAISSDSI STSADNFSPD
     LRVLREANKL AEMEEPALLP GENIKDMAKD VTYICPFTGA VRGTLTVTSY RLYFKSMERD
     PPFVLDASLG VISRVEKIGG ASSRGENSYG LETVCKDIRN LRFAHKPEGR TRRSIFENLM
     KYAFPVSNGL PLFAFEYKEV FPENGWKLYD PLLEYRRQGI PNESWRITKI NERYELCDTY
     PALLVVPANI PDEELKRVAS FRSRGRIPVL SWIHPESQAT VTRCSQPMVG VSGKRSKEDE
     KYLQAIMDSN AQSHKIFIFD ARPSVNAVAN KAKGGGYESE DAYQNAELVF LDIHNIHVMR
     ESLRKLKEIV YPTIEETHWL SNLESTHWLE HIKLILAGAL RIADKVESGK TSVVVHCSDG
     WDRTAQLTSL AMLMLDGYYR TIRGFEVLVE KEWLSFGHRF QLRVGHGDKN HADADRXPVF
     LQFIDCVWQM TRQFPTAFEF NEYFLITILD HLYSCLFGTF LCNSEQQRGK ENLPKKTVSL
     WSYINSQLED FTNPLYGSYS NHVLYPVASM RHLELWVGYY IRWNPRMKPQ EPIHSRYKEL
     LAKRAELQRK VEELQREISN RSTSSSERAS SPAQCVTPVQ TVV
//
ID   MECP2_MOUSE             Reviewed;         484 AA.
AC   Q9Z2D6; B1AUZ2; B1AUZ3; Q3TYG1;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 106.
DE   RecName: Full=Methyl-CpG-binding protein 2;
DE            Short=MeCp-2 protein;
DE            Short=MeCp2;
GN   Name=Mecp2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ISOFORM A).
RC   STRAIN=C57BL/6;
RX   MEDLINE=98449942; PubMed=9774669;
RA   Hendrich B., Bird A.;
RT   "Identification and characterization of a family of mammalian methyl-
RT   CpG binding proteins.";
RL   Mol. Cell. Biol. 18:6538-6547(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ISOFORM A).
RX   MEDLINE=99299240; PubMed=10369871; DOI=10.1093/hmg/8.7.1253;
RA   Coy J.F., Sedlacek Z., Baechner D., Delius H., Poustka A.;
RT   "A complex pattern of evolutionary conservation and alternative
RT   polyadenylation within the long 3'-untranslated region of the methyl-
RT   CpG-binding protein 2 gene (MeCP2) suggests a regulatory role in gene
RT   expression.";
RL   Hum. Mol. Genet. 8:1253-1262(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE (ISOFORM A).
RA   Reichwald K., Thiessen J., Wiehe T., Kioschis P., Straetling W.H.,
RA   Rosenthal A., Platzer M.;
RT   "Comparative analysis of the methyl CpG binding protein 2 locus in man
RT   and mouse reveals new untranslated sequences.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   INTERACTION WITH FNBP3.
RX   MEDLINE=97315177; PubMed=9171351; DOI=10.1093/emboj/16.9.2376;
RA   Bedford M.T., Chan D.C., Leder P.;
RT   "FBP WW domains and the Abl SH3 domain bind to a specific class of
RT   proline-rich ligands.";
RL   EMBO J. 16:2376-2383(1997).
RN   [8]
RP   IDENTIFICATION (ISOFORM B), AND SUBCELLULAR LOCATION.
RX   PubMed=15034150; DOI=10.1093/nar/gkh349;
RA   Kriaucionis S., Bird A.;
RT   "The major form of MeCP2 has a novel N-terminus generated by
RT   alternative splicing.";
RL   Nucleic Acids Res. 32:1818-1823(2004).
RN   [9]
RP   PHOSPHORYLATION AT SER-421.
RX   PubMed=17046689; DOI=10.1016/j.neuron.2006.09.037;
RA   Zhou Z., Hong E.J., Cohen S., Zhao W.-N., Ho H.H., Schmidt L.,
RA   Chen W.G., Lin Y., Savner E., Griffith E.C., Hu L., Steen J.A.J.,
RA   Weitz C.J., Greenberg M.E.;
RT   "Brain-specific phosphorylation of MeCP2 regulates activity-dependent
RT   Bdnf transcription, dendritic growth, and spine maturation.";
RL   Neuron 52:255-269(2006).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Chromosomal protein that binds to methylated DNA. It can
CC       bind specifically to a single methyl-CpG pair. It is not
CC       influenced by sequences flanking the methyl-CpGs. Mediates
CC       transcriptional repression through interaction with histone
CC       deacetylase and the corepressor SIN3A (By similarity).
CC   -!- SUBUNIT: Interacts with CDKL5 (By similarity). Interacts with
CC       FNBP3.
CC   -!- INTERACTION:
CC       O35846:Smarca2; NbExp=1; IntAct=EBI-1188816, EBI-371564;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Colocalized with methyl-CpG in
CC       the genome.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A; Synonyms=Beta;
CC         IsoId=Q9Z2D6-1; Sequence=Displayed;
CC       Name=B; Synonyms=Alpha;
CC         IsoId=Q9Z2D6-2; Sequence=VSP_022949;
CC         Note=Ten times higher expression levels than isoform A in brain
CC         (at protein level);
CC   -!- PTM: Phosphorylated on Ser-421 by CaMK2 in brain upon synaptic
CC       activity, which attenuates its repressor activity and seems to
CC       regulate dendritic growth and spine maturation. Does not seem to
CC       be phosphorylated on Ser-421 in other tissues.
CC   -!- SIMILARITY: Contains 2 A.T hook DNA-binding domains.
CC   -!- SIMILARITY: Contains 1 MBD (methyl-CpG-binding) domain.
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DR   EMBL; AF072251; AAC68880.1; -; mRNA.
DR   EMBL; AJ132922; CAB46495.1; -; mRNA.
DR   EMBL; AF121351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AF158181; AAF33024.1; -; mRNA.
DR   EMBL; AK158664; BAE34602.1; -; mRNA.
DR   EMBL; AL672002; CAM18741.1; -; Genomic_DNA.
DR   EMBL; AL672002; CAM18742.1; -; Genomic_DNA.
DR   EMBL; BC027153; AAH27153.1; -; mRNA.
DR   IPI; IPI00131063; -.
DR   IPI; IPI00775806; -.
DR   RefSeq; NP_001075448.1; NM_001081979.1.
DR   RefSeq; NP_034918.1; NM_010788.3.
DR   UniGene; Mm.131408; -.
DR   UniGene; Mm.414303; -.
DR   ProteinModelPortal; Q9Z2D6; -.
DR   SMR; Q9Z2D6; 71-195.
DR   IntAct; Q9Z2D6; 4.
DR   MINT; MINT-225556; -.
DR   STRING; Q9Z2D6; -.
DR   PhosphoSite; Q9Z2D6; -.
DR   PRIDE; Q9Z2D6; -.
DR   Ensembl; ENSMUST00000033770; ENSMUSP00000033770; ENSMUSG00000031393.
DR   Ensembl; ENSMUST00000100750; ENSMUSP00000098314; ENSMUSG00000031393.
DR   GeneID; 17257; -.
DR   KEGG; mmu:17257; -.
DR   UCSC; uc009tnt.1; mouse.
DR   CTD; 17257; -.
DR   MGI; MGI:99918; Mecp2.
DR   eggNOG; roNOG14533; -.
DR   GeneTree; ENSGT00530000063687; -.
DR   HOVERGEN; HBG052445; -.
DR   OMA; HHHHSEP; -.
DR   PhylomeDB; Q9Z2D6; -.
DR   NextBio; 291736; -.
DR   ArrayExpress; Q9Z2D6; -.
DR   Bgee; Q9Z2D6; -.
DR   CleanEx; MM_MECP2; -.
DR   Genevestigator; Q9Z2D6; -.
DR   GermOnline; ENSMUSG00000031393; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0010385; F:double-stranded methylated DNA binding; IDA:MGI.
DR   GO; GO:0008327; F:methyl-CpG binding; IDA:MGI.
DR   GO; GO:0003729; F:mRNA binding; IDA:MGI.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IDA:MGI.
DR   GO; GO:0035197; F:siRNA binding; IDA:MGI.
DR   GO; GO:0008134; F:transcription factor binding; IPI:MGI.
DR   GO; GO:0016564; F:transcription repressor activity; IDA:MGI.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR   GO; GO:0001662; P:behavioral fear response; IMP:MGI.
DR   GO; GO:0032048; P:cardiolipin metabolic process; IMP:MGI.
DR   GO; GO:0050432; P:catecholamine secretion; IMP:MGI.
DR   GO; GO:0021549; P:cerebellum development; IMP:MGI.
DR   GO; GO:0006342; P:chromatin silencing; IMP:MGI.
DR   GO; GO:0016358; P:dendrite development; IMP:MGI.
DR   GO; GO:0009790; P:embryo development; IMP:MGI.
DR   GO; GO:0008211; P:glucocorticoid metabolic process; IMP:MGI.
DR   GO; GO:0006541; P:glutamine metabolic process; IMP:MGI.
DR   GO; GO:0016573; P:histone acetylation; IMP:MGI.
DR   GO; GO:0016571; P:histone methylation; IMP:MGI.
DR   GO; GO:0006020; P:inositol metabolic process; IMP:MGI.
DR   GO; GO:0007616; P:long-term memory; IMP:MGI.
DR   GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
DR   GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IMP:MGI.
DR   GO; GO:0035067; P:negative regulation of histone acetylation; IMP:MGI.
DR   GO; GO:0031061; P:negative regulation of histone methylation; IMP:MGI.
DR   GO; GO:0043524; P:negative regulation of neuron apoptosis; IMP:MGI.
DR   GO; GO:0001976; P:neurological system process involved in regulation of systemic arterial blood pressure; IMP:MGI.
DR   GO; GO:0042551; P:neuron maturation; IMP:MGI.
DR   GO; GO:0009405; P:pathogenesis; IMP:MGI.
DR   GO; GO:0046470; P:phosphatidylcholine metabolic process; IMP:MGI.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
DR   GO; GO:0051965; P:positive regulation of synaptogenesis; IMP:MGI.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0019230; P:proprioception; IMP:MGI.
DR   GO; GO:0008104; P:protein localization; IMP:MGI.
DR   GO; GO:0060079; P:regulation of excitatory postsynaptic membrane potential; IMP:MGI.
DR   GO; GO:0006349; P:regulation of gene expression by genetic imprinting; IMP:MGI.
DR   GO; GO:0002087; P:regulation of respiratory gaseous exchange by neurological system process; IMP:MGI.
DR   GO; GO:0007585; P:respiratory gaseous exchange; IMP:MGI.
DR   GO; GO:0001666; P:response to hypoxia; IMP:MGI.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:MGI.
DR   GO; GO:0035176; P:social behavior; IMP:MGI.
DR   GO; GO:0001964; P:startle response; IMP:MGI.
DR   GO; GO:0007416; P:synapse assembly; IMP:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   GO; GO:0021591; P:ventricular system development; IMP:MGI.
DR   GO; GO:0008542; P:visual learning; IMP:MGI.
DR   InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR   InterPro; IPR016177; DNA-bd_integrase-typ.
DR   InterPro; IPR017353; Me_CpG-bd_MeCP2.
DR   InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR   Gene3D; G3DSA:3.30.890.10; Methyl_CpG_DNA-bd; 1.
DR   Pfam; PF01429; MBD; 1.
DR   PIRSF; PIRSF038006; Methyl_CpG_bd_MeCP2; 1.
DR   SMART; SM00384; AT_hook; 2.
DR   SMART; SM00391; MBD; 1.
DR   SUPFAM; SSF54171; DNA-binding_integrase-type; 1.
DR   PROSITE; PS50982; MBD; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; DNA-binding; Nucleus;
KW   Phosphoprotein; Repeat; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    484       Methyl-CpG-binding protein 2.
FT                                /FTId=PRO_0000096347.
FT   DOMAIN       90    162       MBD.
FT   DNA_BIND    185    197       A.T hook 1.
FT   DNA_BIND    265    277       A.T hook 2.
FT   COMPBIAS    366    372       His-rich.
FT   COMPBIAS    379    403       Pro-rich.
FT   MOD_RES      80     80       Phosphoserine.
FT   MOD_RES     116    116       Phosphoserine (By similarity).
FT   MOD_RES     229    229       Phosphoserine (By similarity).
FT   MOD_RES     421    421       Phosphoserine; by CaMK2.
FT   MOD_RES     424    424       Phosphoserine (By similarity).
FT   MOD_RES     447    447       N6-acetyllysine (By similarity).
FT   VAR_SEQ       1      9       MVAGMLGLR -> MAAAAATAAAAAAPSGGGGGGEEERL
FT                                (in isoform B).
FT                                /FTId=VSP_022949.
FT   CONFLICT    328    328       L -> P (in Ref. 4; BAE34602).
SQ   SEQUENCE   484 AA;  52307 MW;  62FD228F0118A49F CRC64;
     MVAGMLGLRE EKSEDQDLQG LRDKPLKFKK AKKDKKEDKE GKHEPLQPSA HHSAEPAEAG
     KAETSESSGS APAVPEASAS PKQRRSIIRD RGPMYDDPTL PEGWTRKLKQ RKSGRSAGKY
     DVYLINPQGK AFRSKVELIA YFEKVGDTSL DPNDFDFTVT GRGSPSRREQ KPPKKPKSPK
     APGTGRGRGR PKGSGTGRPK AAASEGVQVK RVLEKSPGKL VVKMPFQASP GGKGEGGGAT
     TSAQVMVIKR PGRKRKAEAD PQAIPKKRGR KPGSVVAAAA AEAKKKAVKE SSIRSVHETV
     LPIKKRKTRE TVSIEVKEVV KPLLVSTLGE KSGKGLKTCK SPGRKSKESS PKGRSSSASS
     PPKKEHHHHH HHSESTKAPM PLLPSPPPPE PESSEDPISP PEPQDLSSSI CKEEKMPRGG
     SLESDGCPKE PAKTQPMVAT TTTVAEKYKH RGEGERKDIV SSSMPRPNRE EPVDSRTPVT
     ERVS
//
ID   MBD3_MOUSE              Reviewed;         285 AA.
AC   Q9Z2D8; Q792D3; Q8CFJ1;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 78.
DE   RecName: Full=Methyl-CpG-binding domain protein 3;
DE   AltName: Full=Methyl-CpG-binding protein MBD3;
GN   Name=Mbd3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=98449942; PubMed=9774669;
RA   Hendrich B., Bird A.;
RT   "Identification and characterization of a family of mammalian methyl-
RT   CpG binding proteins.";
RL   Mol. Cell. Biol. 18:6538-6547(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=129;
RX   MEDLINE=99373255; PubMed=10441743; DOI=10.1007/s003359901112;
RA   Hendrich B., Abbott C., McQueen H., Chambers D., Cross S.H., Bird A.;
RT   "Genomic structure and chromosomal mapping of the murine and human
RT   mbd1, mbd2, mbd3, and mbd4 genes.";
RL   Mamm. Genome 10:906-912(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=14610093; DOI=10.1074/jbc.M309393200;
RA   Ghoshal K., Majumder S., Datta J., Motiwala T., Bai S., Sharma S.M.,
RA   Frankel W., Jacob S.T.;
RT   "Role of human ribosomal RNA (rRNA) promoter methylation and of
RT   methyl-CpG-binding protein MBD2 in the suppression of rRNA gene
RT   expression.";
RL   J. Biol. Chem. 279:6783-6793(2004).
CC   -!- FUNCTION: Does not bind DNA by itself. Recruits histone
CC       deacetylases and DNA methyltransferases. Acts as transcriptional
CC       repressor and plays a role in gene silencing.
CC   -!- SUBUNIT: Heterodimer with MBD2. Part of the NuRD and the MeCP1
CC       complex. Binds HDAC1, MTA2, DNMT1, p66-alpha and p66-beta (By
CC       similarity).
CC   -!- INTERACTION:
CC       P14404:Mecom; NbExp=1; IntAct=EBI-1994548, EBI-1994523;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Nuclear, in discrete foci.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Z2D8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Z2D8-2; Sequence=VSP_011082;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain, heart, kidney,
CC       liver, lung, skeletal muscle, spleen and testis. Detected at lower
CC       levels in embryonic stem cells.
CC   -!- SIMILARITY: Contains 1 MBD (methyl-CpG-binding) domain.
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DR   EMBL; AF072248; AAC68877.1; -; mRNA.
DR   EMBL; AF120995; AAD48909.1; -; Genomic_DNA.
DR   EMBL; BC038264; AAH38264.1; -; mRNA.
DR   IPI; IPI00131067; -.
DR   IPI; IPI00466458; -.
DR   RefSeq; NP_038623.1; NM_013595.2.
DR   UniGene; Mm.7142; -.
DR   ProteinModelPortal; Q9Z2D8; -.
DR   SMR; Q9Z2D8; 1-72.
DR   IntAct; Q9Z2D8; 20.
DR   STRING; Q9Z2D8; -.
DR   PhosphoSite; Q9Z2D8; -.
DR   PRIDE; Q9Z2D8; -.
DR   Ensembl; ENSMUST00000092295; ENSMUSP00000089948; ENSMUSG00000035478.
DR   GeneID; 17192; -.
DR   KEGG; mmu:17192; -.
DR   UCSC; uc007gda.1; mouse.
DR   UCSC; uc007gdb.1; mouse.
DR   CTD; 17192; -.
DR   MGI; MGI:1333812; Mbd3.
DR   eggNOG; roNOG12118; -.
DR   GeneTree; ENSGT00410000025376; -.
DR   HOGENOM; HBG315648; -.
DR   HOVERGEN; HBG052417; -.
DR   InParanoid; Q9Z2D8; -.
DR   OMA; RQRMRYD; -.
DR   OrthoDB; EOG4GF3FS; -.
DR   NextBio; 291538; -.
DR   ArrayExpress; Q9Z2D8; -.
DR   Bgee; Q9Z2D8; -.
DR   CleanEx; MM_MBD3; -.
DR   Genevestigator; Q9Z2D8; -.
DR   GermOnline; ENSMUSG00000035478; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR   GO; GO:0016581; C:NuRD complex; IPI:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0016573; P:histone acetylation; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0006346; P:methylation-dependent chromatin silencing; IDA:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0009888; P:tissue development; IMP:MGI.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR016177; DNA-bd_integrase-typ.
DR   InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR   Gene3D; G3DSA:3.30.890.10; Methyl_CpG_DNA-bd; 1.
DR   Pfam; PF01429; MBD; 1.
DR   SMART; SM00391; MBD; 1.
DR   SUPFAM; SSF54171; DNA-binding_integrase-type; 1.
DR   PROSITE; PS50982; MBD; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Coiled coil; Nucleus;
KW   Phosphoprotein; Transcription; Transcription regulation.
FT   CHAIN         1    285       Methyl-CpG-binding domain protein 3.
FT                                /FTId=PRO_0000096263.
FT   DOMAIN        1     69       MBD.
FT   COILED      221    279       Potential.
FT   COMPBIAS    229    283       Glu-rich.
FT   MOD_RES       4      4       N6-acetyllysine (By similarity).
FT   MOD_RES      56     56       Phosphoserine (By similarity).
FT   MOD_RES     109    109       N6-acetyllysine (By similarity).
FT   MOD_RES     141    141       N6-acetyllysine (By similarity).
FT   MOD_RES     144    144       Phosphoserine (By similarity).
FT   VAR_SEQ       5     36       Missing (in isoform 2).
FT                                /FTId=VSP_011082.
SQ   SEQUENCE   285 AA;  32168 MW;  E4E57BD48463643F CRC64;
     MERKRWECPA LPQGWEREEV PRRSGLSAGH RDVFYYSPSG KKFRSKPQLA RYLGGSMDLS
     TFDFRTGKML MNKMNKSRQR VRYDSSNQVK GKPDLNTALP VRQTASIFKQ PVTKITNHPS
     NKVKSDPQKA VDQPRQLFWE KKLSGLSAFD IAEELVRTMD LPKGLQGVGP GCTDETLLSA
     IASALHTSTL PITGQLSAAV EKNPGVWLNT AQPLCKAFMV TDDDIRKQEE LVQQVRKRLE
     EALMADMLAH VEELARDGEA PLDKACAEEE EEEEEEEEEP EPERV
//
ID   Q9Z2E4_MOUSE            Unreviewed;       159 AA.
AC   Q9Z2E4;
DT   01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 69.
DE   SubName: Full=G substrate;
DE   SubName: Full=G-substrate;
DE   SubName: Full=Putative uncharacterized protein;
GN   Name=Gsbs; ORFNames=mCG_124606;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=99121086; PubMed=9920894; DOI=10.1074/jbc.274.6.3485;
RA   Hall K.U., Collins S.P., Gamm D.M., Massa E., Depaoli-Roach A.A.,
RA   Uhler M.D.;
RT   "Phosphorylation-dependent inhibition of protein phosphatase-1 by G-
RT   substrate: a Purkinje cell substrate of the cyclic GMP-dependent
RT   protein kinase.";
RL   J. Biol. Chem. 274:3485-3495(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RX   MEDLINE=22036378; PubMed=12040188; DOI=10.1126/science.1069193;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Miklos G.L., Wides R.,
RA   Halpern A., Li P.W., Sutton G.G., Nadeau J., Salzberg S.L., Holt R.A.,
RA   Kodira C.D., Lu F., Chen L., Deng Z., Evangelista C.C., Gan W.,
RA   Heiman T.J., Li J., Li Z., Merkulov G.V., Milshina N.V., Naik A.K.,
RA   Qi R., Shue B.C., Wang A., Wang J., Wang X., Yan X., Ye J.,
RA   Yooseph S., Zhao Q., Zheng L., Zhu S.C., Biddick K., Bolanos R.,
RA   Delcher A.L., Dew I.M., Fasulo D., Flanigan M.J., Huson D.H.,
RA   Kravitz S.A., Miller J.R., Mobarry C.M., Reinert K., Remington K.A.,
RA   Zhang Q., Zheng X.H., Nusskern D.R., Lai Z., Lei Y., Zhong W., Yao A.,
RA   Guan P., Ji R.R., Gu Z., Wang Z.Y., Zhong F., Xiao C., Chiang C.C.,
RA   Yandell M., Wortman J.R., Amanatides P.G., Hladun S.L., Pratts E.C.,
RA   Johnson J.E., Dodson K.L., Woodford K.J., Evans C.A., Gropman B.,
RA   Rusch D.B., Venter E., Wang M., Smith T.J., Houck J.T., Tompkins D.E.,
RA   Haynes C., Jacob D., Chin S.H., Allen D.R., Dahlke C.E., Sanders R.,
RA   Li K., Liu X., Levitsky A.A., Majoros W.H., Chen Q., Xia A.C.,
RA   Lopez J.R., Donnelly M.T., Newman M.H., Glodek A., Kraft C.L.,
RA   Nodell M., Ali F., An H.J., Baldwin-Pitts D., Beeson K.Y., Cai S.,
RA   Carnes M., Carver A., Caulk P.M., Center A., Chen Y.H., Cheng M.L.,
RA   Coyne M.D., Crowder M., Danaher S., Davenport L.B., Desilets R.,
RA   Dietz S.M., Doup L., Dullaghan P., Ferriera S., Fosler C.R.,
RA   Gire H.C., Gluecksmann A., Gocayne J.D., Gray J., Hart B., Haynes J.,
RA   Hoover J., Howland T., Ibegwam C., Jalali M., Johns D., Kline L.,
RA   Ma D.S., MacCawley S., Magoon A., Mann F., May D., McIntosh T.C.,
RA   Mehta S., Moy L., Moy M.C., Murphy B.J., Murphy S.D., Nelson K.A.,
RA   Nuri Z., Parker K.A., Prudhomme A.C., Puri V.N., Qureshi H.,
RA   Raley J.C., Reardon M.S., Regier M.A., Rogers Y.H., Romblad D.L.,
RA   Schutz J., Scott J.L., Scott R., Sitter C.D., Smallwood M.,
RA   Sprague A.C., Stewart E., Strong R.V., Suh E., Sylvester K.,
RA   Thomas R., Tint N.N., Tsonis C., Wang G., Wang G., Williams M.S.,
RA   Williams S.M., Windsor S.M., Wolfe K., Wu M.M., Zaveri J.,
RA   Chaturvedi K., Gabrielian A.E., Ke Z., Sun J., Subramanian G.,
RA   Venter J.C., Pfannkoch C.M., Barnstead M., Stephenson L.D.;
RT   "A comparison of whole-genome shotgun-derived mouse chromosome 16 and
RT   the human genome.";
RL   Science 296:1661-1671(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [6]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group
RG   Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [8]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group
RG   (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [9]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the
RG   FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [10]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to
RT   prepare full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [11]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M.,
RA   Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A.,
RA   Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K.,
RA   Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M.,
RA   Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J.,
RA   Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format
RT   sequencing pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [12]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W.,
RA   Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T.,
RA   Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T.,
RA   Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S.,
RA   Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M.,
RA   Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y.,
RA   Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H.,
RA   Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M.,
RA   Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T.,
RA   Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [13]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6;
RX   MEDLINE=22202111; PubMed=12213562; DOI=10.1016/S0531-5565(02)00066-9;
RA   Iida R., Yasuda T., Tsubota E., Takatsuka H., Masuyama M., Matsuki T.,
RA   Kishi K.;
RT   "Five age-dependently expressed genes in mouse brain revealed by the
RT   fluorescence differential display-PCR technique.";
RL   Exp. Gerontol. 37:1121-1126(2002).
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DR   EMBL; AF071562; AAD12589.1; -; mRNA.
DR   EMBL; BC026822; AAH26822.1; -; mRNA.
DR   EMBL; AF500906; AAM21706.1; -; mRNA.
DR   EMBL; AK078335; BAC37224.1; -; mRNA.
DR   EMBL; CH466597; EDK98736.1; -; Genomic_DNA.
DR   IPI; IPI00131092; -.
DR   RefSeq; NP_035283.1; NM_011153.3.
DR   UniGene; Mm.42096; -.
DR   ProteinModelPortal; Q9Z2E4; -.
DR   STRING; Q9Z2E4; -.
DR   PhosphoSite; Q9Z2E4; -.
DR   PRIDE; Q9Z2E4; -.
DR   Ensembl; ENSMUST00000052827; ENSMUSP00000059708; ENSMUSG00000002930.
DR   GeneID; 19051; -.
DR   KEGG; mmu:19051; -.
DR   UCSC; uc009cay.1; mouse.
DR   CTD; 19051; -.
DR   MGI; MGI:1333876; Gsbs.
DR   eggNOG; roNOG16222; -.
DR   GeneTree; ENSGT00390000005586; -.
DR   HOGENOM; HBG269035; -.
DR   HOVERGEN; HBG005927; -.
DR   InParanoid; Q9Z2E4; -.
DR   OMA; KMSPALH; -.
DR   OrthoDB; EOG4WWRKQ; -.
DR   PhylomeDB; Q9Z2E4; -.
DR   NextBio; 295521; -.
DR   ArrayExpress; Q9Z2E4; -.
DR   Bgee; Q9Z2E4; -.
DR   Genevestigator; Q9Z2E4; -.
DR   GO; GO:0005829; C:cytosol; TAS:MGI.
DR   GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IDA:MGI.
PE   2: Evidence at transcript level;
SQ   SEQUENCE   159 AA;  17815 MW;  18B5ECA9E925856C CRC64;
     MSTEMMTTEP VPPLELSDDI LGKLDPQCSP SDDLSDQFIK DCDLKKKPRK GKNVQATLNV
     ESDQKKPRRK DTPAVHIPPF IPGVISEHLI KRYDVQERIP KAKSGPALHN SDMEQKRPRR
     KDTPALHMPP FVAGLTLLRD ESAGVILEDE EMDGDKLAI
//
ID   BSCL2_MOUSE             Reviewed;         383 AA.
AC   Q9Z2E9; Q3TY41; Q3U1S5; Q810B0; Q9JJC2; Q9JMF1;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 2.
DT   08-MAR-2011, entry version 62.
DE   RecName: Full=Seipin;
DE   AltName: Full=Bernardinelli-Seip congenital lipodystrophy type 2 protein homolog;
GN   Name=Bscl2; Synonyms=Gng3lg; ORFNames=MNCb-2630;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=99009337; PubMed=9790771; DOI=10.1006/geno.1998.5508;
RA   Downes G.B., Copeland N.G., Jenkins N.A., Gautam N.;
RT   "Structure and mapping of the G protein gamma3 subunit gene and a
RT   divergently transcribed novel gene, Gng3lg.";
RL   Genomics 53:220-230(1998).
RN   [2]
RP   SEQUENCE REVISION TO N-TERMINUS.
RA   Downes G.B., Gautam N.;
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=20145471; PubMed=10679242; DOI=10.1006/bbrc.2000.2170;
RA   Inoue S., Sano H., Ohta M.;
RT   "Growth suppression of Escherichia coli by induction of expression of
RT   mammalian genes with transmembrane or ATPase domains.";
RL   Biochem. Biophys. Res. Commun. 268:553-561(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RA   Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S.,
RA   Hashimoto K.;
RT   "Isolation of full-length cDNA clones from mouse brain cDNA library
RT   made by oligo-capping method.";
RL   Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Bone marrow macrophage, Dendritic cell, and Visual cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain, and Olfactory epithelium;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Highest expression in brain and testis.
CC   -!- SIMILARITY: Belongs to the seipin family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH61689.1; Type=Erroneous initiation;
CC       Sequence=BAA95071.1; Type=Erroneous initiation;
CC       Sequence=BAE34722.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF069954; AAC77923.2; -; mRNA.
DR   EMBL; AB030196; BAA92759.1; -; mRNA.
DR   EMBL; AB041588; BAA95071.1; ALT_INIT; mRNA.
DR   EMBL; AK151606; BAE30545.1; -; mRNA.
DR   EMBL; AK155753; BAE33418.1; -; mRNA.
DR   EMBL; AK158901; BAE34722.1; ALT_INIT; mRNA.
DR   EMBL; AK170183; BAE41621.1; -; mRNA.
DR   EMBL; BC043023; AAH43023.2; -; mRNA.
DR   EMBL; BC061689; AAH61689.1; ALT_INIT; mRNA.
DR   IPI; IPI00914720; -.
DR   RefSeq; NP_001129536.1; NM_001136064.2.
DR   RefSeq; NP_032170.3; NM_008144.4.
DR   UniGene; Mm.345134; -.
DR   UniGene; Mm.480870; -.
DR   ProteinModelPortal; Q9Z2E9; -.
DR   PRIDE; Q9Z2E9; -.
DR   Ensembl; ENSMUST00000086058; ENSMUSP00000083224; ENSMUSG00000071657.
DR   GeneID; 14705; -.
DR   KEGG; mmu:14705; -.
DR   UCSC; uc008gnj.1; mouse.
DR   CTD; 14705; -.
DR   MGI; MGI:1298392; Bscl2.
DR   eggNOG; maNOG18822; -.
DR   GeneTree; ENSGT00390000011639; -.
DR   HOGENOM; HBG505354; -.
DR   HOVERGEN; HBG050736; -.
DR   InParanoid; Q9Z2E9; -.
DR   OMA; LPAMVND; -.
DR   OrthoDB; EOG40CHHQ; -.
DR   NextBio; 286683; -.
DR   ArrayExpress; Q9Z2E9; -.
DR   Bgee; Q9Z2E9; -.
DR   Genevestigator; Q9Z2E9; -.
DR   GermOnline; ENSMUSG00000071657; Mus musculus.
DR   GO; GO:0030176; C:integral to endoplasmic reticulum membrane; ISS:UniProtKB.
DR   InterPro; IPR009617; Adipose-reg_protein_Seipin.
DR   Pfam; PF06775; Seipin; 1.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Glycoprotein; Membrane; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1    383       Seipin.
FT                                /FTId=PRO_0000191680.
FT   TOPO_DOM      1     27       Cytoplasmic (Potential).
FT   TRANSMEM     28     48       Helical; (Potential).
FT   TOPO_DOM     49    242       Lumenal (Potential).
FT   TRANSMEM    243    263       Helical; (Potential).
FT   TOPO_DOM    264    383       Cytoplasmic (Potential).
FT   CARBOHYD     88     88       N-linked (GlcNAc...) (By similarity).
FT   CARBOHYD    242    242       N-linked (GlcNAc...) (Potential).
FT   CONFLICT    341    341       A -> V (in Ref. 3; BAA92759).
SQ   SEQUENCE   383 AA;  43105 MW;  AB185C29BC67634E CRC64;
     MVNDPPVPAL LWAQEVGHVL AGRARRLMLQ FGVLFCTILL LLWVSVFLYG SFYYSYMPTV
     SHLSPVHFHY RTDCDSSTAS LCSFPVANVS LAKSGRDRVL MYGQPYRVTL ELELPESPVN
     QDLGMFLVTV SCYTRGGRII STSSRSVMLH YRSQLLQVLD TLLFSSLLLF GFAEQKQLLE
     VELYSDYREN SYVPTTGAII EIHSKRIQMY GAYLRIHAHF TGLRYLLYNF PMTCAFVGVA
     SNFTFLSVIV LFSYMQWVWG AVWPRHRFSL QVNIRQRDNS HHGAPRRISR HQPGQESTQQ
     SDVTEDGESP EDPSGTEGQL SEEEKPEKRP LNGEEEQEPE ASDGSWEDAA LLTEANPPTS
     ASASALAPET LGSLRQRPTC SSS
//
ID   BNI3L_MOUSE             Reviewed;         218 AA.
AC   Q9Z2F7; Q545J6;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-FEB-2011, entry version 86.
DE   RecName: Full=BCL2/adenovirus E1B 19 kDa protein-interacting protein 3-like;
DE   AltName: Full=NIP3-like protein X;
DE            Short=NIP3L;
GN   Name=Bnip3l; Synonyms=Nix;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RX   MEDLINE=99084982; PubMed=9867803; DOI=10.1074/jbc.274.1.7;
RA   Chen G., Cizeau J., Vande Velde C., Park J.H., Bozek G., Bolton J.,
RA   Shi L., Dubik D., Greenberg A.;
RT   "Nix and Nip3 form a subfamily of pro-apoptotic mitochondrial
RT   proteins.";
RL   J. Biol. Chem. 274:7-10(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Cecum, Egg, Hippocampus, Lung, and Pancreas;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61; SER-62; SER-116 AND
RP   SER-119, AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-117 AND
RP   SER-119, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Induces apoptosis. Interacts with viral and cellular
CC       anti-apoptosis proteins. Can overcome the suppressors BCL-2 and
CC       BCL-XL, although high levels of BCL-XL expression will inhibit
CC       apoptosis. May function as a tumor suppressor. Inhibits apoptosis
CC       induced by BNIP3 (By similarity).
CC   -!- SUBUNIT: Self-associates. Interacts with BNIP3 and STEAP3 (By
CC       similarity).
CC   -!- INTERACTION:
CC       Q69ZI1:Sh3rf1; NbExp=2; IntAct=EBI-1774669, EBI-957380;
CC   -!- SUBCELLULAR LOCATION: Nucleus envelope (By similarity).
CC       Endoplasmic reticulum (By similarity). Mitochondrion. Membrane;
CC       Single-pass membrane protein (Potential).
CC   -!- PTM: Undergoes progressive proteolysis to an 11 kDa C-terminal
CC       fragment, which is blocked by the proteasome inhibitor
CC       lactacystin.
CC   -!- SIMILARITY: Belongs to the NIP3 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF067395; AAD03588.1; -; mRNA.
DR   EMBL; AK004667; BAB23456.1; -; mRNA.
DR   EMBL; AK007920; BAB25351.1; -; mRNA.
DR   EMBL; AK013467; BAB28869.1; -; mRNA.
DR   EMBL; AK018668; BAB31334.1; -; mRNA.
DR   EMBL; AK139950; BAE24194.1; -; mRNA.
DR   EMBL; AK155040; BAE33007.1; -; mRNA.
DR   EMBL; BC085237; AAH85237.1; -; mRNA.
DR   IPI; IPI00131125; -.
DR   RefSeq; NP_033891.1; NM_009761.3.
DR   UniGene; Mm.29820; -.
DR   UniGene; Mm.347081; -.
DR   ProteinModelPortal; Q9Z2F7; -.
DR   SMR; Q9Z2F7; 169-212.
DR   IntAct; Q9Z2F7; 4.
DR   STRING; Q9Z2F7; -.
DR   PhosphoSite; Q9Z2F7; -.
DR   PRIDE; Q9Z2F7; -.
DR   Ensembl; ENSMUST00000022634; ENSMUSP00000022634; ENSMUSG00000022051.
DR   GeneID; 12177; -.
DR   KEGG; mmu:12177; -.
DR   UCSC; uc007uks.1; mouse.
DR   CTD; 12177; -.
DR   MGI; MGI:1332659; Bnip3l.
DR   GeneTree; ENSGT00390000013415; -.
DR   HOGENOM; HBG443927; -.
DR   HOVERGEN; HBG050707; -.
DR   InParanoid; Q9Z2F7; -.
DR   OMA; LFISHVL; -.
DR   PhylomeDB; Q9Z2F7; -.
DR   NextBio; 280561; -.
DR   ArrayExpress; Q9Z2F7; -.
DR   Bgee; Q9Z2F7; -.
DR   CleanEx; MM_BNIP3L; -.
DR   Genevestigator; Q9Z2F7; -.
DR   GermOnline; ENSMUSG00000022051; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005740; C:mitochondrial envelope; IEA:InterPro.
DR   GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR   GO; GO:0006917; P:induction of apoptosis; ISS:UniProtKB.
DR   GO; GO:0008634; P:negative regulation of survival gene product expression; ISS:UniProtKB.
DR   InterPro; IPR010548; BNIP3.
DR   Pfam; PF06553; BNIP3; 1.
PE   1: Evidence at protein level;
KW   Apoptosis; Endoplasmic reticulum; Membrane; Mitochondrion; Nucleus;
KW   Phosphoprotein; Transmembrane; Transmembrane helix.
FT   CHAIN         1    218       BCL2/adenovirus E1B 19 kDa protein-
FT                                interacting protein 3-like.
FT                                /FTId=PRO_0000064958.
FT   TRANSMEM    187    207       Helical; (Potential).
FT   MOD_RES      61     61       Phosphoserine.
FT   MOD_RES      62     62       Phosphoserine.
FT   MOD_RES     116    116       Phosphoserine.
FT   MOD_RES     117    117       Phosphoserine.
FT   MOD_RES     119    119       Phosphoserine.
SQ   SEQUENCE   218 AA;  23766 MW;  EAA839DEFDDE50D7 CRC64;
     MSHLVEPPPP LHNNNNNCEE GEQPLPPPAG LNSSWVELPM NSSNGNENGN GKNGGLEHVP
     SSSSIHNGDM EKILLDAQHE SGQSSSRGSS HCDSPSPQED GQIMFDVEMH TSRDHSSQSE
     EEVVEGEKEV EALKKSADWV SDWSSRPENI PPKEFHFRHP KRAASLSMRK SGAMKKGGIF
     SAEFLKVFIP SLFLSHVLAL GLGIYIGKRL STPSASTY
//
ID   RGS6_MOUSE              Reviewed;         472 AA.
AC   Q9Z2H2; Q08AT5; Q8BGI8;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   31-AUG-2004, sequence version 2.
DT   08-MAR-2011, entry version 80.
DE   RecName: Full=Regulator of G-protein signaling 6;
DE            Short=RGS6;
GN   Name=Rgs6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head, and Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 64-472.
RA   He W., Wensel T.G.;
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   INTERACTION WITH RGS7BP.
RX   PubMed=15632198; DOI=10.1074/jbc.C400596200;
RA   Martemyanov K.A., Yoo P.J., Skiba N.P., Arshavsky V.Y.;
RT   "R7BP, a novel neuronal protein interacting with RGS proteins of the
RT   R7 family.";
RL   J. Biol. Chem. 280:5133-5136(2005).
RN   [5]
RP   INTERACTION WITH RGS7BP.
RX   PubMed=15897264; DOI=10.1083/jcb.200502007;
RA   Drenan R.M., Doupnik C.A., Boyle M.P., Muglia L.J., Huettner J.E.,
RA   Linder M.E., Blumer K.J.;
RT   "Palmitoylation regulates plasma membrane-nuclear shuttling of R7BP, a
RT   novel membrane anchor for the RGS7 family.";
RL   J. Cell Biol. 169:623-633(2005).
CC   -!- FUNCTION: Inhibits signal transduction by increasing the GTPase
CC       activity of G protein alpha subunits thereby driving them into
CC       their inactive GDP-bound form. Activity on G(o)-alpha is
CC       specifically enhanced by the RGS6/Gbeta5 dimer (By similarity).
CC   -!- SUBUNIT: Heterodimer with Gbeta5 (By similarity). Interacts with
CC       RGS7BP, leading to regulate the subcellular location of the
CC       heterodimer formed with Gbeta5.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane;
CC       Peripheral membrane protein (By similarity).
CC   -!- SIMILARITY: Contains 1 DEP domain.
CC   -!- SIMILARITY: Contains 1 G protein gamma domain.
CC   -!- SIMILARITY: Contains 1 RGS domain.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK052527; BAC35026.1; -; mRNA.
DR   EMBL; AK053087; BAC35262.1; -; mRNA.
DR   EMBL; BC125029; AAI25030.1; -; mRNA.
DR   EMBL; BC125030; AAI25031.1; -; mRNA.
DR   EMBL; AF061933; AAC70011.1; -; mRNA.
DR   IPI; IPI00265467; -.
DR   RefSeq; NP_056627.1; NM_015812.3.
DR   UniGene; Mm.153013; -.
DR   ProteinModelPortal; Q9Z2H2; -.
DR   SMR; Q9Z2H2; 19-456.
DR   STRING; Q9Z2H2; -.
DR   PRIDE; Q9Z2H2; -.
DR   Ensembl; ENSMUST00000021642; ENSMUSP00000021642; ENSMUSG00000021219.
DR   GeneID; 50779; -.
DR   KEGG; mmu:50779; -.
DR   UCSC; uc007oda.1; mouse.
DR   CTD; 50779; -.
DR   MGI; MGI:1354730; Rgs6.
DR   GeneTree; ENSGT00560000076525; -.
DR   HOGENOM; HBG385421; -.
DR   HOVERGEN; HBG007404; -.
DR   InParanoid; Q9Z2H2; -.
DR   OMA; KPESEQG; -.
DR   OrthoDB; EOG41ZF9K; -.
DR   NextBio; 307721; -.
DR   ArrayExpress; Q9Z2H2; -.
DR   Bgee; Q9Z2H2; -.
DR   CleanEx; MM_RGS6; -.
DR   Genevestigator; Q9Z2H2; -.
DR   GermOnline; ENSMUSG00000021219; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IEA:InterPro.
DR   GO; GO:0005096; F:GTPase activator activity; TAS:MGI.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0007186; P:G-protein coupled receptor protein signaling pathway; TAS:MGI.
DR   GO; GO:0009968; P:negative regulation of signal transduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000591; DEP_dom.
DR   InterPro; IPR015898; G-protein_gamma_dom.
DR   InterPro; IPR000342; Regulat_G_prot_signal.
DR   InterPro; IPR016137; Regulat_G_prot_signal_superfam.
DR   InterPro; IPR011991; WHTH_trsnscrt_rep_DNA-bd.
DR   Gene3D; G3DSA:4.10.260.10; G-protein_gamma_dom; 1.
DR   Gene3D; G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
DR   Pfam; PF00610; DEP; 1.
DR   Pfam; PF00631; G-gamma; 1.
DR   Pfam; PF00615; RGS; 1.
DR   PRINTS; PR01301; RGSPROTEIN.
DR   SMART; SM00049; DEP; 1.
DR   SMART; SM00224; GGL; 1.
DR   SMART; SM00315; RGS; 1.
DR   SUPFAM; SSF48670; G-protein_gamma-like; 1.
DR   SUPFAM; SSF48097; Regulat_G_prot_signal_superfam; 1.
DR   PROSITE; PS50186; DEP; 1.
DR   PROSITE; PS50058; G_PROTEIN_GAMMA; FALSE_NEG.
DR   PROSITE; PS50132; RGS; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Membrane; Signal transduction inhibitor.
FT   CHAIN         1    472       Regulator of G-protein signaling 6.
FT                                /FTId=PRO_0000204193.
FT   DOMAIN       40    115       DEP.
FT   DOMAIN      261    330       G protein gamma.
FT   DOMAIN      336    451       RGS.
SQ   SEQUENCE   472 AA;  54531 MW;  94EB9AD49764196C CRC64;
     MAQGSGDQRA VGIADPEESS PNMIVYCKIE DIITKMQDDK TGGVPIRTVK SFLSKIPSVV
     TGTDIVQWLM KNLSIEDPVE AIHLGSLIAA QGYIFPISDH VLTMKDDGTF YRFQAPYFWP
     SNCWEPENTD YAIYLCKRTM QNKARLELAD YEAENLARLQ RAFARKWEFI FMQAEAQVKI
     DRKKDKTERK ILDSQERAFW DVHRPVPGCV NTTEMDIRKC RRLKNPQKVK KSVYGVTDET
     QSQSPVHIPS QPIRKTTKDD IRKQITFLNA QIDRHCLKMS KVAESLIAYT EQYVEYDPFI
     TPAEPSNPWI SDDITLWDIE MSKEPSQQRV KRWGFSFDEI LKDQVGRDQF LRFLESEFSS
     ENLRFWLSVQ DLKKQPLQDV AKRVEEIWQE FLAPGAPSAI NLDSHSYEIT SQNVKDGGRY
     TFEDAQEHIY KLMKSDSYAR FLRSNAYQDL LLAKKKGKSL AGKRLTGLMQ SS
//
ID   E41L1_MOUSE             Reviewed;         879 AA.
AC   Q9Z2H5; Q3U3L1; Q3UHP7; Q80U34; Q8K204;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Band 4.1-like protein 1;
DE   AltName: Full=Neuronal protein 4.1;
DE            Short=4.1N;
GN   Name=Epb41l1; Synonyms=Epb4, Epb4.1l1, Kiaa0338;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=99343811; PubMed=10414974;
RA   Walensky L.D., Blackshaw S., Liao D., Watkins C.C., Weier H.-U.G.,
RA   Parra M., Huganir R.L., Conboy J.G., Mohandas N., Snyder S.H.;
RT   "A novel neuron-enriched homolog of the erythrocyte membrane
RT   cytoskeletal protein 4.1.";
RL   J. Neurosci. 19:6457-6467(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   STRAIN=C57BL/6J, and NOD;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-685, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; THR-475; SER-546;
RP   THR-550; SER-648 AND SER-650, AND MASS SPECTROMETRY.
RC   TISSUE=Forebrain;
RX   PubMed=15572359; DOI=10.1074/jbc.M411220200;
RA   Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,
RA   Blackstock W.P., Choudhary J.S., Grant S.G.;
RT   "Proteomic analysis of in vivo phosphorylated synaptic proteins.";
RL   J. Biol. Chem. 280:5972-5982(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546; THR-550 AND
RP   SER-648, AND MASS SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
RA   Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-865; SER-868 AND
RP   SER-879, AND MASS SPECTROMETRY.
RC   TISSUE=Teratocarcinoma;
RX   PubMed=17622165; DOI=10.1021/pr070122r;
RA   Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT   "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT   cells.";
RL   J. Proteome Res. 6:3174-3186(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-343, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378; SER-650; SER-677
RP   AND THR-685, AND MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430; SER-510 AND
RP   SER-639, AND MASS SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: May function to confer stability and plasticity to
CC       neuronal membrane via multiple interactions, including the
CC       spectrin-actin-based cytoskeleton, integral membrane channels and
CC       membrane-associated guanylate kinases.
CC   -!- SUBUNIT: Interacts with AGAP2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9Z2H5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Z2H5-2; Sequence=VSP_023964;
CC       Name=3;
CC         IsoId=Q9Z2H5-3; Sequence=VSP_023964, VSP_023965;
CC   -!- TISSUE SPECIFICITY: Highest expression in brain, also present in
CC       kidney, olfactory epithelium, retina, sensory ganglia,
CC       gastrointestinal tract (only enteric neurons) and lung.
CC   -!- SIMILARITY: Contains 1 FERM domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC65533.1; Type=Erroneous initiation;
CC   -----------------------------------------------------------------------
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DR   EMBL; AF061283; AAC68583.1; -; mRNA.
DR   EMBL; AK122251; BAC65533.1; ALT_INIT; mRNA.
DR   EMBL; AK147272; BAE27810.1; -; mRNA.
DR   EMBL; AK154704; BAE32774.1; -; mRNA.
DR   EMBL; BC034751; AAH34751.1; -; mRNA.
DR   IPI; IPI00465812; -.
DR   IPI; IPI00830613; -.
DR   IPI; IPI00831205; -.
DR   RefSeq; NP_001003815.1; NM_001003815.2.
DR   RefSeq; NP_001006665.1; NM_001006664.2.
DR   RefSeq; NP_038538.1; NM_013510.3.
DR   UniGene; Mm.20852; -.
DR   ProteinModelPortal; Q9Z2H5; -.
DR   SMR; Q9Z2H5; 93-402.
DR   STRING; Q9Z2H5; -.
DR   PhosphoSite; Q9Z2H5; -.
DR   PRIDE; Q9Z2H5; -.
DR   Ensembl; ENSMUST00000029155; ENSMUSP00000029155; ENSMUSG00000027624.
DR   Ensembl; ENSMUST00000088565; ENSMUSP00000085926; ENSMUSG00000027624.
DR   Ensembl; ENSMUST00000103135; ENSMUSP00000099424; ENSMUSG00000027624.
DR   Ensembl; ENSMUST00000103136; ENSMUSP00000099425; ENSMUSG00000027624.
DR   Ensembl; ENSMUST00000103137; ENSMUSP00000099426; ENSMUSG00000027624.
DR   Ensembl; ENSMUST00000109571; ENSMUSP00000105199; ENSMUSG00000027624.
DR   Ensembl; ENSMUST00000109576; ENSMUSP00000105204; ENSMUSG00000027624.
DR   Ensembl; ENSMUST00000109577; ENSMUSP00000105205; ENSMUSG00000027624.
DR   GeneID; 13821; -.
DR   KEGG; mmu:13821; -.
DR   UCSC; uc008nni.1; mouse.
DR   CTD; 13821; -.
DR   MGI; MGI:103010; Epb4.1l1.
DR   GeneTree; ENSGT00600000084063; -.
DR   HOGENOM; HBG715532; -.
DR   HOVERGEN; HBG007777; -.
DR   OrthoDB; EOG4J9MZ6; -.
DR   NextBio; 284612; -.
DR   ArrayExpress; Q9Z2H5; -.
DR   Bgee; Q9Z2H5; -.
DR   CleanEx; MM_EPB4.1L1; -.
DR   Genevestigator; Q9Z2H5; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0019898; C:extrinsic to membrane; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
DR   InterPro; IPR008379; Band_4.1_C.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR019750; Band_41_fam.
DR   InterPro; IPR021187; Band_41_protein.
DR   InterPro; IPR000798; Ez/rad/moesin.
DR   InterPro; IPR014847; FERM-adjacent.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR007477; SAB.
DR   Gene3D; G3DSA:1.20.80.10; ACBP; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF05902; 4_1_CTD; 1.
DR   Pfam; PF08736; FA; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF04382; SAB; 1.
DR   PIRSF; PIRSF002304; Membrane_skeletal_4_1; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SUPFAM; SSF47031; FERM_3-hlx; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW   Phosphoprotein.
FT   CHAIN         1    879       Band 4.1-like protein 1.
FT                                /FTId=PRO_0000219396.
FT   DOMAIN       97    378       FERM.
FT   REGION      381    482       Hydrophilic.
FT   REGION      483    541       Spectrin--actin-binding.
FT   REGION      743    879       Carboxyl-terminal (CTD).
FT   MOD_RES      75     75       Phosphoserine (By similarity).
FT   MOD_RES      79     79       Phosphothreonine (By similarity).
FT   MOD_RES     343    343       Phosphotyrosine.
FT   MOD_RES     378    378       Phosphoserine.
FT   MOD_RES     430    430       Phosphoserine.
FT   MOD_RES     437    437       Phosphoserine (By similarity).
FT   MOD_RES     441    441       Phosphoserine (By similarity).
FT   MOD_RES     466    466       Phosphoserine.
FT   MOD_RES     475    475       Phosphothreonine.
FT   MOD_RES     510    510       Phosphoserine.
FT   MOD_RES     540    540       Phosphoserine (By similarity).
FT   MOD_RES     541    541       Phosphoserine (By similarity).
FT   MOD_RES     544    544       Phosphoserine (By similarity).
FT   MOD_RES     546    546       Phosphoserine.
FT   MOD_RES     550    550       Phosphothreonine.
FT   MOD_RES     564    564       Phosphoserine (By similarity).
FT   MOD_RES     578    578       Phosphoserine (By similarity).
FT   MOD_RES     639    639       Phosphoserine.
FT   MOD_RES     648    648       Phosphoserine.
FT   MOD_RES     650    650       Phosphoserine.
FT   MOD_RES     677    677       Phosphoserine.
FT   MOD_RES     685    685       Phosphothreonine.
FT   MOD_RES     721    721       Phosphoserine (By similarity).
FT   MOD_RES     725    725       Phosphoserine (By similarity).
FT   MOD_RES     726    726       Phosphothreonine (By similarity).
FT   MOD_RES     782    782       Phosphoserine (By similarity).
FT   MOD_RES     865    865       Phosphothreonine.
FT   MOD_RES     868    868       Phosphoserine.
FT   MOD_RES     879    879       Phosphoserine.
FT   VAR_SEQ     484    495       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_023964.
FT   VAR_SEQ     556    691       Missing (in isoform 3).
FT                                /FTId=VSP_023965.
FT   CONFLICT     26     26       A -> T (in Ref. 2; BAC65533).
FT   CONFLICT    142    142       F -> Y (in Ref. 1; AAC68583 and 3;
FT                                BAE27810/BAE32774).
FT   CONFLICT    434    434       Missing (in Ref. 3; BAE27810).
FT   CONFLICT    451    451       E -> D (in Ref. 1; AAC68583 and 3;
FT                                BAE27810/BAE32774).
FT   CONFLICT    580    580       M -> T (in Ref. 1; AAC68583).
FT   CONFLICT    659    659       Q -> R (in Ref. 1; AAC68583).
FT   CONFLICT    708    708       K -> R (in Ref. 3; BAE27810).
SQ   SEQUENCE   879 AA;  98315 MW;  E5C91175FA33D067 CRC64;
     MTTETGPDSE VKKAQEETPQ QPEAAAAVTT PVTPAGHSHP ETNSNEKHLT QQDTRPAEQS
     LDMDDKDYSE ADGLSERTTP SKAQKSPQKI AKKFKSAICR VTLLDASEYE CEVEKHGRGQ
     VLFDLVCEHL NLLEKDYFGL TFCDADSQKN WLDPSKEIKK QIRSSPWNFA FTVKFYPPDP
     AQLTEDITRY YLCLQLRADI ITGRLPCSFV THALLGSYAV QAELGDYDAE EHVGNYVSEL
     RFAPNQTREL EERIMELHKT YRGMTPGEAE IHFLENAKKL SMYGVDLHHA KDSEGIDIML
     GVCANGLLIY RDRLRINRFA WPKILKISYK RSNFYIKIRP GEYEQFESTI GFKLPNHRSA
     KRLWKVCIEH HTFFRLVSPE PPPKGFLVMG SKFRYSGRTQ AQTRQASALI DRPAPFFERS
     SSKRYTMSRS LDGAEFSRPA SVSENHDAGP EGDKREDDAE SGGRRSEAEE GEVRTPTKIK
     ELKPEQETTP RHKQEFLDKP EDVLLKHQAS INELKRTLKE PNSKLIHRDR DWDRERRLPS
     SPASPSPKGT PEKASERAGL REGSEEKVKP PRPRAPESDM GDEDQDQERD AVFLKDNHLA
     IERKCSSITV SSTSSLEAEV DFTVIGDYHG GAFEDFSRSL PELDRDKSDS ETEGLVFAQD
     LKGPSSQEDE SGGLEDSPDR GACSTPEMPQ FESVKAETMT VSSLAIRKKI EPEAMLQSRV
     SAADSTQVDG GTPMVKDFMT TPPCITTETI STTMENSLKS GKGAAAMIPG PQTVATEIRS
     LSPIIGKDVL TSTYGATAET LSTSTTTHVT KTVKGGFSET RIEKRIIITG DEDVDQDQAL
     ALAIKEAKLQ HPDMLVTKAV VYRETDPSPE ERDKKPQES
//
ID   SUCB1_MOUSE             Reviewed;         463 AA.
AC   Q9Z2I9; Q3TVH1; Q8BGS6;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2004, sequence version 2.
DT   08-MAR-2011, entry version 102.
DE   RecName: Full=Succinyl-CoA ligase [ADP-forming] subunit beta, mitochondrial;
DE            EC=6.2.1.5;
DE   AltName: Full=ATP-specific succinyl-CoA synthetase subunit beta;
DE   AltName: Full=Succinyl-CoA synthetase beta-A chain;
DE            Short=SCS-betaA;
DE   Flags: Precursor;
GN   Name=Sucla2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, Head, Testis, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 38-463.
RC   TISSUE=Heart;
RX   MEDLINE=98438536; PubMed=9765291; DOI=10.1074/jbc.273.42.27580;
RA   Johnson J.D., Mehus J.G., Tews K., Milavetz B.I., Lambeth D.O.;
RT   "Genetic evidence for the expression of ATP- and GTP-specific
RT   succinyl-CoA synthetases in multicellular eucaryotes.";
RL   J. Biol. Chem. 273:27580-27586(1998).
RN   [4]
RP   PROTEIN SEQUENCE OF 121-129; 206-215; 337-362 AND 443-451, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- CATALYTIC ACTIVITY: ATP + succinate + CoA = ADP + phosphate +
CC       succinyl-CoA.
CC   -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
CC       succinate from succinyl-CoA (ligase route): step 1/1.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta
CC       subunit family.
CC   -!- SIMILARITY: Contains 1 ATP-grasp domain.
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DR   EMBL; AK081965; BAC38380.1; -; mRNA.
DR   EMBL; AK088801; BAC40580.1; -; mRNA.
DR   EMBL; AK132762; BAE21343.1; -; mRNA.
DR   EMBL; AK160130; BAE35647.1; -; mRNA.
DR   EMBL; AK160652; BAE35942.1; -; mRNA.
DR   EMBL; BC056353; AAH56353.1; -; mRNA.
DR   EMBL; BC057605; AAH57605.1; -; mRNA.
DR   EMBL; AF058955; AAC64398.1; -; mRNA.
DR   IPI; IPI00261627; -.
DR   RefSeq; NP_035636.1; NM_011506.3.
DR   UniGene; Mm.38951; -.
DR   ProteinModelPortal; Q9Z2I9; -.
DR   SMR; Q9Z2I9; 53-444.
DR   STRING; Q9Z2I9; -.
DR   PhosphoSite; Q9Z2I9; -.
DR   REPRODUCTION-2DPAGE; IPI00261627; -.
DR   REPRODUCTION-2DPAGE; Q9Z2I9; -.
DR   UCD-2DPAGE; Q9Z2I9; -.
DR   PRIDE; Q9Z2I9; -.
DR   Ensembl; ENSMUST00000022706; ENSMUSP00000022706; ENSMUSG00000022110.
DR   GeneID; 20916; -.
DR   KEGG; mmu:20916; -.
DR   NMPDR; fig|10090.3.peg.29396; -.
DR   UCSC; uc007upx.1; mouse.
DR   CTD; 20916; -.
DR   MGI; MGI:1306775; Sucla2.
DR   GeneTree; ENSGT00390000010170; -.
DR   HOVERGEN; HBG055555; -.
DR   InParanoid; Q9Z2I9; -.
DR   OMA; KKELYVS; -.
DR   OrthoDB; EOG4RBQJQ; -.
DR   PhylomeDB; Q9Z2I9; -.
DR   BRENDA; 6.2.1.5; 244.
DR   NextBio; 299817; -.
DR   ArrayExpress; Q9Z2I9; -.
DR   Bgee; Q9Z2I9; -.
DR   Genevestigator; Q9Z2I9; -.
DR   GermOnline; ENSMUSG00000022110; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:EC.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR013816; ATP_grasp_subdomain_2.
DR   InterPro; IPR005811; CoA_ligase.
DR   InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR   InterPro; IPR005809; Succ_CoA_synthase_bsu.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   Gene3D; G3DSA:3.30.1490.20; ATP_grasp_subdomain_1; 1.
DR   Gene3D; G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1.
DR   Gene3D; G3DSA:3.40.50.261; Succinyl-CoA_synth-like; 1.
DR   PANTHER; PTHR11815; CoA_lig_beta; 1.
DR   Pfam; PF08442; ATP-grasp_2; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   SUPFAM; SSF52210; CoA_ligase; 1.
DR   TIGRFAMs; TIGR01016; sucCoAbeta; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Direct protein sequencing; Ligase;
KW   Mitochondrion; Nucleotide-binding; Phosphoprotein; Transit peptide;
KW   Tricarboxylic acid cycle.
FT   TRANSIT       1     52       Mitochondrion (By similarity).
FT   CHAIN        53    463       Succinyl-CoA ligase [ADP-forming] subunit
FT                                beta, mitochondrial.
FT                                /FTId=PRO_0000033353.
FT   DOMAIN       61    288       ATP-grasp.
FT   MOD_RES      78     78       N6-acetyllysine (By similarity).
FT   MOD_RES      84     84       Phosphotyrosine (By similarity).
FT   MOD_RES     143    143       N6-acetyllysine (By similarity).
FT   MOD_RES     279    279       Phosphoserine.
SQ   SEQUENCE   463 AA;  50114 MW;  74CE8E962BC0BB27 CRC64;
     MAASMFYGRQ LAAAALRSHR PQTTLRAAAQ VLGNSGLFNK HGLQVQQQQQ RTLSLHEYLS
     MELLQEAGVS VPKGFVAKSS DEAYAIAKKL GSKDVVIKAQ VLAGGRGKGT FTSGLKGGVK
     IVFSPEEAKA VSSQMIGQKL ITKQTGEKGR ICNQVLVCER KYPRREYYFA ITMERSFQGP
     VLIGSAQGGV NIEDVAAENP EAIVKEPIDI VEGIKKEQAV TLAQKMGFPS NIVDSAAENM
     IKLYNLFLKY DATMVEINPM VEDSDGKVLC MDAKINFDSN SAYRQKKIFD LQDWSQEDER
     DKEAANADIN YIGLDGSIGC LVNGAGLAMA TMDIIKLHGG TPANFLDVGG GATVQQVTEA
     FKLITSDKKV QAILVNIFGG IMRCDVIAQG IVMAVKDLEI RIPVVVRLQG TRVDDAKALI
     ADSGLKILAC DDLDEAAKMV VKLSEIVTLA KEAHVDVKFQ LPI
//
ID   K1C16_MOUSE             Reviewed;         469 AA.
AC   Q9Z2K1;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 70.
DE   RecName: Full=Keratin, type I cytoskeletal 16;
DE   AltName: Full=Cytokeratin-16;
DE            Short=CK-16;
DE   AltName: Full=Keratin-16;
DE            Short=K16;
GN   Name=Krt16; Synonyms=Krt1-16;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RX   MEDLINE=99042000; PubMed=9822705; DOI=10.1074/jbc.273.48.32265;
RA   Porter R.M., Hutcheson A.M., Rugg E.L., Quinlan R.A., Lane E.B.;
RT   "cDNA cloning, expression, and assembly characteristics of mouse
RT   keratin 16.";
RL   J. Biol. Chem. 273:32265-32272(1998).
RN   [2]
RP   INTERACTION WITH TRADD.
RX   PubMed=16702408; DOI=10.1101/gad.1387406;
RA   Tong X., Coulombe P.A.;
RT   "Keratin 17 modulates hair follicle cycling in a TNFalpha-dependent
RT   fashion.";
RL   Genes Dev. 20:1353-1364(2006).
CC   -!- SUBUNIT: Heterodimer of a type I and a type II keratin. KRT16
CC       associates with KRT6 isomers. Interacts with TCHP (By similarity).
CC       Interacts with TRADD.
CC   -!- INTERACTION:
CC       Q3U0V2:Tradd; NbExp=1; IntAct=EBI-1544045, EBI-1544032;
CC   -!- MISCELLANEOUS: There are two types of cytoskeletal and
CC       microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to
CC       basic; 56-70 kDa).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
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DR   EMBL; AF053235; AAC79424.1; -; mRNA.
DR   IPI; IPI00874585; -.
DR   RefSeq; NP_032496.1; NM_008470.1.
DR   UniGene; Mm.422799; -.
DR   ProteinModelPortal; Q9Z2K1; -.
DR   SMR; Q9Z2K1; 111-147, 158-261, 277-347, 351-423.
DR   IntAct; Q9Z2K1; 1.
DR   STRING; Q9Z2K1; -.
DR   PhosphoSite; Q9Z2K1; -.
DR   PRIDE; Q9Z2K1; -.
DR   Ensembl; ENSMUST00000007280; ENSMUSP00000007280; ENSMUSG00000053797.
DR   GeneID; 16666; -.
DR   KEGG; mmu:16666; -.
DR   UCSC; uc007lkq.1; mouse.
DR   CTD; 16666; -.
DR   MGI; MGI:96690; Krt16.
DR   GeneTree; ENSGT00560000076946; -.
DR   HOVERGEN; HBG013015; -.
DR   OrthoDB; EOG483D4W; -.
DR   NextBio; 290379; -.
DR   ArrayExpress; Q9Z2K1; -.
DR   Bgee; Q9Z2K1; -.
DR   CleanEx; MM_KRT16; -.
DR   Genevestigator; Q9Z2K1; -.
DR   GermOnline; ENSMUSG00000053797; Mus musculus.
DR   GO; GO:0005882; C:intermediate filament; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; IDA:MGI.
DR   GO; GO:0045104; P:intermediate filament cytoskeleton organization; IDA:MGI.
DR   InterPro; IPR016044; F.
DR   InterPro; IPR001664; IF.
DR   InterPro; IPR018039; Intermediate_filament_CS.
DR   InterPro; IPR002957; Keratin_I.
DR   PANTHER; PTHR23239; IF; 1.
DR   Pfam; PF00038; Filament; 1.
DR   PRINTS; PR01248; TYPE1KERATIN.
DR   PROSITE; PS00226; IF; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Intermediate filament; Keratin.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    469       Keratin, type I cytoskeletal 16.
FT                                /FTId=PRO_0000063663.
FT   REGION        2    112       Head.
FT   REGION      113    420       Rod.
FT   REGION      113    148       Coil 1A.
FT   REGION      149    166       Linker 1.
FT   REGION      167    258       Coil 1B.
FT   REGION      259    281       Linker 12.
FT   REGION      282    420       Coil 2.
FT   REGION      421    469       Tail.
SQ   SEQUENCE   469 AA;  51606 MW;  13B8028CF28B64D5 CRC64;
     MATCSRQFTS SSSMKGSCGI GGGSSRMSSI LAGGSCRAPS TCGGMSVTSS RFSSGGVCGI
     GGGYGGSFSS SSFGGGLGSG FGGRFDGFGG GFGAGLGGGL GGGIGDGLLV GSEKVTMQNL
     NDRLATYLDK VRALEEANRD LEVKIRDWYQ RQRPTEIKDY SPYFKTIEDL KSKIIIATQE
     NAQFTLQIDN ARLAADDFRT KYENELFLRQ SVEGDINGLR KVLDELTLSR ADLEMQIENL
     REELAFLKKN HEEEMLALRG QTGGDVNVEM DAAPGVDLSR ILNEMRDQYE QMAEKNRRDV
     EAWFLRKTEE LNKEVASNSD LIQSNRSEVA ELRRVFQGLE IELQSQLSMK ASLENSLEET
     KGRYCMQLSQ IQGLISSVEE QLAQLRCEME QQSQEYNILL DVKTRLEQEI ATYRRLLDGE
     NIHSSSQHSS GQSYSSREVF SSSSRQPRSI LKEQGSTSFS QSQSQSSRD
//
ID   UBL3_MOUSE              Reviewed;         117 AA.
AC   Q9Z2M6; A4FTW0; Q3UKM1;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Ubiquitin-like protein 3;
DE   AltName: Full=Membrane-anchored ubiquitin-fold protein;
DE            Short=MUB;
DE            Short=MmMUB;
DE   AltName: Full=Protein HCG-1;
DE   Flags: Precursor;
GN   Name=Ubl3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99307157; PubMed=10375635; DOI=10.1016/S0378-1119(99)00138-9;
RA   Chadwick B.P., Kidd T., Sgouros J., Ish-Horowicz D., Frischauf A.-M.;
RT   "Cloning, mapping and expression of UBL3, a novel ubiquitin-like
RT   gene.";
RL   Gene 233:189-195(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   IDENTIFICATION, AND NOMENCLATURE.
RX   PubMed=16831869; DOI=10.1074/jbc.M602283200;
RA   Downes B.P., Saracco S.A., Lee S.S., Crowell D.N., Vierstra R.D.;
RT   "MUBS: a family of ubiquitin-fold proteins that are plasma membrane-
RT   anchored by prenylation.";
RL   J. Biol. Chem. 281:27145-27157(2006).
RN   [5]
RP   STRUCTURE BY NMR OF 1-103.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of mouse ubiquitin-like 3 protein.";
RL   Submitted (NOV-2004) to the PDB data bank.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor (By similarity).
CC   -!- SIMILARITY: Contains 1 ubiquitin-like domain.
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CC   -----------------------------------------------------------------------
DR   EMBL; AF044222; AAD02324.1; -; mRNA.
DR   EMBL; AK145952; BAE26780.1; -; mRNA.
DR   EMBL; BC024507; AAH24507.1; -; mRNA.
DR   EMBL; BC025595; AAH25595.1; -; mRNA.
DR   EMBL; BC043729; AAH43729.1; -; mRNA.
DR   IPI; IPI00131227; -.
DR   RefSeq; NP_036038.1; NM_011908.2.
DR   UniGene; Mm.21846; -.
DR   PDB; 1WGH; NMR; -; A=1-103.
DR   PDBsum; 1WGH; -.
DR   ProteinModelPortal; Q9Z2M6; -.
DR   SMR; Q9Z2M6; 2-117.
DR   STRING; Q9Z2M6; -.
DR   PRIDE; Q9Z2M6; -.
DR   Ensembl; ENSMUST00000079324; ENSMUSP00000078303; ENSMUSG00000001687.
DR   GeneID; 24109; -.
DR   KEGG; mmu:24109; -.
DR   UCSC; uc009aou.1; mouse.
DR   CTD; 24109; -.
DR   MGI; MGI:1344373; Ubl3.
DR   GeneTree; ENSGT00390000004952; -.
DR   HOGENOM; HBG382950; -.
DR   HOVERGEN; HBG054980; -.
DR   InParanoid; Q9Z2M6; -.
DR   OMA; KTHEFEF; -.
DR   OrthoDB; EOG483D61; -.
DR   NextBio; 304127; -.
DR   ArrayExpress; Q9Z2M6; -.
DR   Bgee; Q9Z2M6; -.
DR   CleanEx; MM_UBL3; -.
DR   Genevestigator; Q9Z2M6; -.
DR   GermOnline; ENSMUSG00000001687; Mus musculus.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR017000; M-anchored_Ub-fold_HCG-1.
DR   InterPro; IPR019955; Ubiquitin_supergroup.
DR   PIRSF; PIRSF032572; MUB; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; FALSE_NEG.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Lipoprotein; Membrane; Methylation;
KW   Prenylation.
FT   CHAIN         1    114       Ubiquitin-like protein 3.
FT                                /FTId=PRO_0000114863.
FT   PROPEP      115    117       Removed in mature form (Probable).
FT                                /FTId=PRO_0000248184.
FT   DOMAIN       10     88       Ubiquitin-like.
FT   MOD_RES     114    114       Cysteine methyl ester (Probable).
FT   LIPID       114    114       S-geranylgeranyl cysteine (Probable).
FT   STRAND        7     15
FT   STRAND       17     19
FT   STRAND       21     26
FT   HELIX        32     41
FT   STRAND       42     44
FT   TURN         55     57
FT   STRAND       58     62
FT   STRAND       65     67
FT   TURN         73     77
FT   STRAND       83     90
FT   STRAND       95     97
SQ   SEQUENCE   117 AA;  13180 MW;  2EB3A5102AD06F2D CRC64;
     MSSHVPADMI NLRLILVSGK TKEFLFSPND SASDIAKHVY DNWPMDWEEE QVSSPNILRL
     IYQGRFLHGN VTLGALKLPF GKTTVMHLVA RETLPEPNSQ GQRNREKTGE SNCCVIL
//
ID   SEPT5_MOUSE             Reviewed;         369 AA.
AC   Q9Z2Q6; B2RUC5; Q3UYG4; Q6PB74;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 2.
DT   08-MAR-2011, entry version 88.
DE   RecName: Full=Septin-5;
DE   AltName: Full=Cell division control-related protein 1;
DE            Short=CDCrel-1;
DE   AltName: Full=Peanut-like protein 1;
GN   Name=Sept5; Synonyms=Pnutl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 23-369.
RC   STRAIN=C57BL/6; TISSUE=Brain, Cartilage, and Skin;
RA   Botta A., Lindsay E.A., Jurecic V., Zieger B., Ware J., Baldini A.;
RT   "CDCREL-1, a septin deleted in DiGeorge Syndrome, is expressed in the
RT   developing brain and cartilage primordia in mouse embryogenesis.";
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   PROTEIN SEQUENCE OF 23-36; 58-71; 82-90; 182-190; 240-256; 264-282 AND
RP   297-308, AND MASS SPECTROMETRY.
RC   STRAIN=C57BL/6; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   INTERACTION WITH PARK2, AND UBIQUITIN-MEDIATED DEGRADATION.
RX   MEDLINE=20542129; PubMed=11078524; DOI=10.1073/pnas.240347797;
RA   Zhang Y., Gao J., Chung K.K.K., Huang H., Dawson V.L., Dawson T.M.;
RT   "Parkin functions as an E2-dependent ubiquitin-protein ligase and
RT   promotes the degradation of the synaptic vesicle-associated protein,
RT   CDCrel-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:13354-13359(2000).
RN   [6]
RP   INTERACTION WITH SEPT2 AND SEPT7, LACK OF INTERACTION WITH SEPT4,
RP   DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=11739749; DOI=10.1128/MCB.22.1.378-387.2002;
RA   Peng X.-R., Jia Z., Zhang Y., Ware J., Trimble W.S.;
RT   "The septin CDCrel-1 is dispensable for normal development and
RT   neurotransmitter release.";
RL   Mol. Cell. Biol. 22:378-387(2002).
RN   [7]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=11880646; DOI=10.1073/pnas.052715199;
RA   Dent J., Kato K., Peng X.-R., Martinez C., Cattaneo M., Poujol C.,
RA   Nurden P., Nurden A., Trimble W.S., Ware J.;
RT   "A prototypic platelet septin and its participation in secretion.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:3064-3069(2002).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND THR-336, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Filament-forming cytoskeletal GTPase (By similarity).
CC       Involved in cytokinesis (Potential). May play a role in platelet
CC       secretion.
CC   -!- SUBUNIT: Septins polymerize into heterooligomeric protein
CC       complexes that form filaments, and can associate with cellular
CC       membranes, actin filaments and microtubules. GTPase activity is
CC       required for filament formation (By similarity). Interacts with
CC       SEPT2 and SEPT5. Interaction with SEPT4 not detected. In
CC       platelets, associated with a complex containing STX4 (By
CC       similarity). Interacts with PARK2. This interaction leads to SEPT5
CC       ubiquitination and degradation.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity).
CC   -!- DEVELOPMENTAL STAGE: Detected at 17 dpc in the brain. Expression
CC       increases during postnatal life and reaches a plateau at
CC       approximately P10 (at protein level).
CC   -!- DISRUPTION PHENOTYPE: Mice have a normal life-span and show no
CC       apparent abnormalities, including synaptic properties and
CC       hippocampal neuron growth. In platelets, hyperresponsive
CC       degranulation phenotype.
CC   -!- SIMILARITY: Belongs to the septin family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK134700; BAE22248.1; -; mRNA.
DR   EMBL; BC059848; AAH59848.1; -; mRNA.
DR   EMBL; BC141073; AAI41074.1; -; mRNA.
DR   EMBL; BC145331; AAI45332.1; -; mRNA.
DR   EMBL; AF033350; AAC83974.1; -; mRNA.
DR   IPI; IPI00923056; -.
DR   RefSeq; NP_998779.2; NM_213614.2.
DR   UniGene; Mm.20365; -.
DR   ProteinModelPortal; Q9Z2Q6; -.
DR   SMR; Q9Z2Q6; 41-309.
DR   STRING; Q9Z2Q6; -.
DR   PhosphoSite; Q9Z2Q6; -.
DR   Ensembl; ENSMUST00000096987; ENSMUSP00000094750; ENSMUSG00000072214.
DR   GeneID; 18951; -.
DR   KEGG; mmu:18951; -.
DR   UCSC; uc007yoj.1; mouse.
DR   CTD; 18951; -.
DR   MGI; MGI:1195461; Sept5.
DR   eggNOG; roNOG11340; -.
DR   GeneTree; ENSGT00590000082878; -.
DR   HOVERGEN; HBG065093; -.
DR   InParanoid; Q9Z2Q6; -.
DR   OrthoDB; EOG447FTF; -.
DR   PhylomeDB; Q9Z2Q6; -.
DR   NextBio; 295300; -.
DR   ArrayExpress; Q9Z2Q6; -.
DR   Bgee; Q9Z2Q6; -.
DR   CleanEx; MM_SEPT5; -.
DR   Genevestigator; Q9Z2Q6; -.
DR   GermOnline; ENSMUSG00000072214; Mus musculus.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0031105; C:septin complex; IEA:InterPro.
DR   GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR   GO; GO:0019717; C:synaptosome; IDA:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0017157; P:regulation of exocytosis; ISS:UniProtKB.
DR   InterPro; IPR000038; Cell_Div_GTP-bd.
DR   InterPro; IPR016491; Septin.
DR   PANTHER; PTHR18884; Cell_Div_GTP_bd; 1.
DR   Pfam; PF00735; Septin; 1.
DR   PIRSF; PIRSF006698; Septin; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; GTP-binding; Nucleotide-binding;
KW   Phosphoprotein.
FT   CHAIN         1    369       Septin-5.
FT                                /FTId=PRO_0000173523.
FT   NP_BIND      51     58       GTP (By similarity).
FT   NP_BIND     190    198       GTP (By similarity).
FT   COILED      338    369       Potential.
FT   BINDING      85     85       GTP (By similarity).
FT   BINDING     111    111       GTP; via amide nitrogen (By similarity).
FT   BINDING     248    248       GTP; via amide nitrogen and carbonyl
FT                                oxygen (By similarity).
FT   BINDING     263    263       GTP (By similarity).
FT   MOD_RES     225    225       Phosphoserine.
FT   MOD_RES     327    327       Phosphoserine.
FT   MOD_RES     336    336       Phosphothreonine.
SQ   SEQUENCE   369 AA;  42748 MW;  D58468DBA9ADE626 CRC64;
     MSTGLRYKSK LATPEDKQDI DKQYVGFATL PNQVHRKSVK KGFDFTLMVA GESGLGKSTL
     VHSLFLTDLY KDRKLLSAEE RINQTVEILK HTVDIEEKGV KLKLTIVDTP GFGDAVNNSE
     CWKPITDYVD QQFEQYFRDE SGLNRKNIQD NRVHCCLYFI SPFGHGLRPV DVGFMKALHE
     KVNIVPLIAK ADCLVPSEIR KLKDRIREEI DKFGIHVYQF PECDSDEDED FKQQDRELKE
     SAPFAVIGSN TVVEAKGQRV RGRLYPWGIV EVENQAHCDF VKLRNMLIRT HMHDLKDVTC
     DVHYENYRAH CIQQMTSKLT QDSRMESPIP ILPLPTPDAE TEKLIRMKDE ELRRMQEMLQ
     KMKQQMQDQ
//
ID   U119A_MOUSE             Reviewed;         240 AA.
AC   Q9Z2R6;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 61.
DE   RecName: Full=Protein unc-119 homolog A;
DE   AltName: Full=Retinal protein 4;
DE            Short=mRG4;
GN   Name=Unc119; Synonyms=Unc119h;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   MEDLINE=98432431; PubMed=9761287;
RA   Swanson D.A., Chang J.T., Campochiaro P.A., Zack D.J., Valle D.;
RT   "Mammalian orthologs of C. elegans unc-119 highly expressed in
RT   photoreceptors.";
RL   Invest. Ophthalmol. Vis. Sci. 39:2085-2094(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   INTERACTION WITH CABP4, AND TISSUE SPECIFICITY.
RX   PubMed=18296658; DOI=10.1167/iovs.07-1166;
RA   Haeseleer F.;
RT   "Interaction and colocalization of CaBP4 and Unc119 (MRG4) in
RT   photoreceptors.";
RL   Invest. Ophthalmol. Vis. Sci. 49:2366-2375(2008).
CC   -!- FUNCTION: May play a role in the mechanism of photoreceptor
CC       neurotransmitter release through the synaptic vesicle cycle.
CC   -!- SUBUNIT: Interacts with CABP4; in the absence of calcium.
CC       Interacts with ARL2. Found in a complex with ARL3, RP2 and UNC119;
CC       RP2 induces hydrolysis of GTP ARL3 in the complex, leading to the
CC       release of UNC119 (By similarity).
CC   -!- TISSUE SPECIFICITY: Retinal-specific. Localized in photoreceptor
CC       synapses in the outer plexiform layer of the retina.
CC   -!- SIMILARITY: Belongs to the PDE6D/unc-119 family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF030169; AAD01893.1; -; mRNA.
DR   EMBL; BC001990; AAH01990.1; -; mRNA.
DR   IPI; IPI00131315; -.
DR   RefSeq; NP_035806.1; NM_011676.2.
DR   UniGene; Mm.284811; -.
DR   ProteinModelPortal; Q9Z2R6; -.
DR   SMR; Q9Z2R6; 57-239.
DR   STRING; Q9Z2R6; -.
DR   PhosphoSite; Q9Z2R6; -.
DR   PRIDE; Q9Z2R6; -.
DR   Ensembl; ENSMUST00000002127; ENSMUSP00000002127; ENSMUSG00000002058.
DR   GeneID; 22248; -.
DR   KEGG; mmu:22248; -.
DR   UCSC; uc007kjb.1; mouse.
DR   CTD; 22248; -.
DR   MGI; MGI:1328357; Unc119.
DR   GeneTree; ENSGT00390000014595; -.
DR   HOVERGEN; HBG108625; -.
DR   OrthoDB; EOG441QCD; -.
DR   NextBio; 302323; -.
DR   ArrayExpress; Q9Z2R6; -.
DR   Bgee; Q9Z2R6; -.
DR   CleanEx; MM_UNC119; -.
DR   Genevestigator; Q9Z2R6; -.
DR   GermOnline; ENSMUSG00000002058; Mus musculus.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   InterPro; IPR008015; GMP_PDE_delta.
DR   InterPro; IPR014756; Ig_E-set.
DR   Gene3D; G3DSA:2.70.50.40; GMP_PDE_delta; 1.
DR   Pfam; PF05351; GMP_PDE_delta; 1.
DR   SUPFAM; SSF81296; Ig_E-set; 1.
PE   1: Evidence at protein level;
KW   Phosphoprotein; Sensory transduction; Vision.
FT   CHAIN         1    240       Protein unc-119 homolog A.
FT                                /FTId=PRO_0000221213.
FT   MOD_RES      37     37       Phosphoserine.
SQ   SEQUENCE   240 AA;  27010 MW;  9EDF51191F0F5203 CRC64;
     MKVKKGGGGT GSGAEPVPGA SNRSAEPTRE PGAEAESGSE SEPEPGPGPR LGPLQGKQPI
     GPEDVLGLQR ITGDYLCSPE ENIYKIDFVR FKIRDMDSGT VLFEIKKPPV SERLPINRRD
     LDPNAGRFVR YQFTPAFLRL RQVGATVEFT VGDKPVNNFR MIERHYFRNQ LLKSFDFHFG
     FCIPSSKNTC EHIYDFPPLS EELISEMIRH PYETQSDSFY FVDDRLVMHN KADYSYSGTP
//
ID   T22D3_MOUSE             Reviewed;         137 AA.
AC   Q9Z2S7; B1AVF3; Q3UNI6; Q8K160; Q9EQN0; Q9EQN1; Q9EQN2;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   08-MAR-2011, entry version 90.
DE   RecName: Full=TSC22 domain family protein 3;
DE   AltName: Full=Glucocorticoid-induced leucine zipper protein;
DE   AltName: Full=TSC22-related-inducible leucine zipper 3;
DE            Short=Tilz3;
GN   Name=Tsc22d3; Synonyms=Dsip1, Dsipi, Gilz;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND INDUCTION.
RC   STRAIN=C3H/HeN; TISSUE=Thymus;
RX   MEDLINE=98090090; PubMed=9430225; DOI=10.1016/S1074-7613(00)80398-2;
RA   D'Adamio F., Zollo O., Moraca R., Ayroldi E., Bruscoli S., Bartoli A.,
RA   Cannarile L., Migliorati G., Riccardi C.;
RT   "A new dexamethasone-induced gene of the leucine zipper family
RT   protects T lymphocytes from TCR/CD3-activated cell death.";
RL   Immunity 7:803-812(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RA   Ershler M.A., Belyavsky A.V., Visser J.W.M.;
RT   "Identification and characterization of a family of leucine zipper
RT   genes related to TSC22.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=BALB/c, and C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; TISSUE=Liver;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=21361175; PubMed=11468175; DOI=10.1182/blood.V98.3.743;
RA   Ayroldi E., Migliorati G., Bruscoli S., Marchetti C., Zollo O.,
RA   Cannarile L., D'Adamio F., Riccardi C.;
RT   "Modulation of T-cell activation by the glucocorticoid-induced leucine
RT   zipper factor via inhibition of nuclear factor kappa B.";
RL   Blood 98:743-753(2001).
RN   [7]
RP   HOMODIMERIZATION, AND INTERACTION WITH JUN AND FOS.
RX   MEDLINE=21369994; PubMed=11397794; DOI=10.1074/jbc.M101522200;
RA   Mittelstadt P.R., Ashwell J.D.;
RT   "Inhibition of AP-1 by the glucocorticoid-inducible protein GILZ.";
RL   J. Biol. Chem. 276:29603-29610(2001).
RN   [8]
RP   TISSUE SPECIFICITY, AND INDUCTION.
RX   MEDLINE=22397464; PubMed=12393603; DOI=10.1182/blood-2002-02-0538;
RA   Berrebi D., Bruscoli S., Cohen N., Foussat A., Migliorati G.,
RA   Bouchet-Delbos L., Maillot M.-C., Portier A., Couderc J., Galanaud P.,
RA   Peuchmaur M., Riccardi C., Emilie D.;
RT   "Synthesis of glucocorticoid-induced leucine zipper (GILZ) by
RT   macrophages: an anti-inflammatory and immunosuppressive mechanism
RT   shared by glucocorticoids and IL-10.";
RL   Blood 101:729-738(2003).
RN   [9]
RP   INDUCTION.
RX   PubMed=15031210; DOI=10.1182/blood-2003-12-4295;
RA   Asselin-Labat M.-L., David M., Biola-Vidamment A., Lecoeuche D.,
RA   Zennaro M.-C., Bertoglio J., Pallardy M.;
RT   "GILZ, a new target for the transcription factor FoxO3, protects T
RT   lymphocytes from interleukin-2 withdrawal-induced apoptosis.";
RL   Blood 104:215-223(2004).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37 AND SER-40 (ISOFORM
RP   3), AND MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
CC   -!- FUNCTION: Protects T-cells from IL2 deprivation-induced apoptosis
CC       through the inhibition of FOXO3A transcriptional activity that
CC       leads to the down-regulation of the pro-apoptotic factor BCL2L11.
CC       In macrophages, plays a role in the anti-inflammatory and
CC       immunosuppressive effects of glucocorticoids and IL10. In T-cells,
CC       inhibits anti-CD3-induced NFKB1 nuclear translocation. In vitro,
CC       suppresses AP1 and NFKB1 DNA-binding activities (By similarity).
CC   -!- SUBUNIT: Can form homodimers, however it is likely to function as
CC       a monomer. Interacts with AP1 and NFKB1 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Tilz3b;
CC         IsoId=Q9Z2S7-1; Sequence=Displayed;
CC       Name=2; Synonyms=Tilz3a;
CC         IsoId=Q9Z2S7-2; Sequence=VSP_012690;
CC       Name=3; Synonyms=Tilz3c;
CC         IsoId=Q9Z2S7-3; Sequence=VSP_012691;
CC         Note=Phosphorylated on Ser-37 and Ser-40;
CC   -!- TISSUE SPECIFICITY: Constitutively expressed in lung, intestine,
CC       kidney and liver, most probably by resident cells from the
CC       macrophage lineage. Expression inversely correlates with T-cell
CC       activation, being higher in resting cells and lower in cells
CC       activated by TCR/CD3 triggering.
CC   -!- INDUCTION: By glucocorticoids in lymphoid cells and upon IL4,
CC       IL10, IL13 or glucocorticoid treatment in monocyte/macrophage
CC       cells. Transiently induced by IL2 deprivation in T-cells (By
CC       similarity).
CC   -!- DOMAIN: The leucine-zipper is involved in homodimerization.
CC   -!- PTM: Isoform 3 is phosphorylated on Ser-30 and Ser-40.
CC   -!- SIMILARITY: Belongs to the TSC-22/Dip/Bun family.
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DR   EMBL; AF024519; AAD01789.1; -; mRNA.
DR   EMBL; AF201287; AAG41220.1; -; mRNA.
DR   EMBL; AF201288; AAG41221.1; -; mRNA.
DR   EMBL; AF201289; AAG41222.1; -; mRNA.
DR   EMBL; AK083389; BAC38897.1; -; mRNA.
DR   EMBL; AK144196; BAE25761.1; -; mRNA.
DR   EMBL; AL683809; CAM24436.1; -; Genomic_DNA.
DR   EMBL; BC028813; AAH28813.1; -; mRNA.
DR   IPI; IPI00265379; -.
DR   IPI; IPI00331467; -.
DR   IPI; IPI00551119; -.
DR   RefSeq; NP_001070832.1; NM_001077364.1.
DR   RefSeq; NP_034416.3; NM_010286.3.
DR   UniGene; Mm.480311; -.
DR   ProteinModelPortal; Q9Z2S7; -.
DR   SMR; Q9Z2S7; 58-114.
DR   STRING; Q9Z2S7; -.
DR   PhosphoSite; Q9Z2S7; -.
DR   REPRODUCTION-2DPAGE; IPI00265379; -.
DR   PRIDE; Q9Z2S7; -.
DR   Ensembl; ENSMUST00000055738; ENSMUSP00000062589; ENSMUSG00000031431.
DR   Ensembl; ENSMUST00000112996; ENSMUSP00000108620; ENSMUSG00000031431.
DR   GeneID; 14605; -.
DR   KEGG; mmu:14605; -.
DR   UCSC; uc009ukz.1; mouse.
DR   UCSC; uc009ula.1; mouse.
DR   UCSC; uc009ulb.1; mouse.
DR   CTD; 14605; -.
DR   MGI; MGI:1196284; Tsc22d3.
DR   eggNOG; roNOG17552; -.
DR   GeneTree; ENSGT00530000063062; -.
DR   HOVERGEN; HBG075918; -.
DR   OMA; STEMFAK; -.
DR   OrthoDB; EOG4X3H2T; -.
DR   NextBio; 286388; -.
DR   ArrayExpress; Q9Z2S7; -.
DR   Bgee; Q9Z2S7; -.
DR   CleanEx; MM_TSC22D3; -.
DR   Genevestigator; Q9Z2S7; -.
DR   GermOnline; ENSMUSG00000031431; Mus musculus.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006916; P:anti-apoptosis; IDA:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   GO; GO:0006970; P:response to osmotic stress; IDA:MGI.
DR   InterPro; IPR000580; TSC-22_Dip_Bun.
DR   PANTHER; PTHR12348; TSC-22_Dip_Bun; 1.
DR   Pfam; PF01166; TSC22; 1.
DR   ProDom; PD007152; TSC-22_Dip_Bun; 1.
DR   PROSITE; PS01289; TSC22; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein.
FT   CHAIN         1    137       TSC22 domain family protein 3.
FT                                /FTId=PRO_0000219371.
FT   DOMAIN       76     97       Leucine-zipper.
FT   REGION        1     60       AP1-binding.
FT   VAR_SEQ       1     57       Missing (in isoform 2).
FT                                /FTId=VSP_012690.
FT   VAR_SEQ       1     40       MNTEMYQTPMEVAVYQLHNFSISFFSSLLGGDVVSVKLDN
FT                                -> MAQPKTECRSPVGLDCCNCCLDLANRCELQKEKSGESP
FT                                GSPFVSNFRQLQEKLVFENLNTDKLNNIMRQDSMEPVVRDP
FT                                CYLINEGICNRNIDQTMLSILLFFH (in isoform 3).
FT                                /FTId=VSP_012691.
FT   CONFLICT     22     22       I -> T (in Ref. 1; AAD01789).
FT   CONFLICT     33     33       V -> L (in Ref. 2; AAG41221).
SQ   SEQUENCE   137 AA;  15177 MW;  A11D7B69037F111E CRC64;
     MNTEMYQTPM EVAVYQLHNF SISFFSSLLG GDVVSVKLDN SASGASVVAL DNKIEQAMDL
     VKNHLMYAVR EEVEVLKEQI RELLEKNSQL ERENTLLKTL ASPEQLEKFQ SRLSPEEPAP
     EAPETPETPE APGGSAV
//
ID   PSA5_MOUSE              Reviewed;         241 AA.
AC   Q9Z2U1;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 99.
DE   RecName: Full=Proteasome subunit alpha type-5;
DE            EC=3.4.25.1;
DE   AltName: Full=Macropain zeta chain;
DE   AltName: Full=Multicatalytic endopeptidase complex zeta chain;
DE   AltName: Full=Proteasome zeta chain;
GN   Name=Psma5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=B10.A;
RX   MEDLINE=99367391; PubMed=10436176; DOI=10.1007/s002510050562;
RA   Elenich L.A., Nandi D., Kent E.A., McCluskey T.S., Cruz M., Iyer M.N.,
RA   Woodward E.C., Conn C.W., Ochoa A.L., Ginsburg D.B., Monaco J.J.;
RT   "The complete primary structure of mouse 20S proteasomes.";
RL   Immunogenetics 49:835-842(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6, and FVB/N; TISSUE=Brain, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 21-32.
RC   TISSUE=Brain;
RA   Lubec G., Yang J.W., Zigmond M.;
RL   Submitted (JUL-2007) to UniProtKB.
CC   -!- FUNCTION: The proteasome is a multicatalytic proteinase complex
CC       which is characterized by its ability to cleave peptides with Arg,
CC       Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
CC       slightly basic pH. The proteasome has an ATP-dependent proteolytic
CC       activity.
CC   -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad
CC       specificity.
CC   -!- SUBUNIT: The 26S proteasome consists of a 20S proteasome core and
CC       two 19S regulatory subunits. The 20S proteasome core is composed
CC       of 28 subunits that are arranged in four stacked rings, resulting
CC       in a barrel-shaped structure. The two end rings are each formed by
CC       seven alpha subunits, and the two central rings are each formed by
CC       seven beta subunits. The catalytic chamber with the active sites
CC       is on the inside of the barrel. PSMA5 interacts directly with the
CC       PSMG1-PSMG2 heterodimer which promotes 20S proteasome assembly (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- SIMILARITY: Belongs to the peptidase T1A family.
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DR   EMBL; AF019661; AAC69149.1; -; mRNA.
DR   EMBL; BC010709; AAH10709.1; -; mRNA.
DR   EMBL; BC083342; AAH83342.1; -; mRNA.
DR   IPI; IPI00131407; -.
DR   RefSeq; NP_036097.1; NM_011967.3.
DR   UniGene; Mm.208883; -.
DR   ProteinModelPortal; Q9Z2U1; -.
DR   SMR; Q9Z2U1; 8-241.
DR   STRING; Q9Z2U1; -.
DR   MEROPS; T01.975; -.
DR   PhosphoSite; Q9Z2U1; -.
DR   REPRODUCTION-2DPAGE; Q9Z2U1; -.
DR   PRIDE; Q9Z2U1; -.
DR   Ensembl; ENSMUST00000090569; ENSMUSP00000088057; ENSMUSG00000068749.
DR   GeneID; 26442; -.
DR   KEGG; mmu:26442; -.
DR   UCSC; uc008qyq.1; mouse.
DR   CTD; 26442; -.
DR   MGI; MGI:1347009; Psma5.
DR   GeneTree; ENSGT00550000074958; -.
DR   HOGENOM; HBG499923; -.
DR   HOVERGEN; HBG003005; -.
DR   InParanoid; Q9Z2U1; -.
DR   OMA; VEYSLEA; -.
DR   OrthoDB; EOG4R503K; -.
DR   PhylomeDB; Q9Z2U1; -.
DR   BRENDA; 3.4.25.1; 244.
DR   NextBio; 304525; -.
DR   Bgee; Q9Z2U1; -.
DR   Genevestigator; Q9Z2U1; -.
DR   GermOnline; ENSMUSG00000068749; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IEA:InterPro.
DR   GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   InterPro; IPR000426; Proteasome_asu_CS.
DR   InterPro; IPR001353; Proteasome_sua/b.
DR   Pfam; PF00227; Proteasome; 1.
DR   Pfam; PF10584; Proteasome_A_N; 1.
DR   SMART; SM00948; Proteasome_A_N; 1.
DR   PROSITE; PS00388; PROTEASOME_A_1; 1.
DR   PROSITE; PS51475; PROTEASOME_A_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase; Nucleus;
KW   Phosphoprotein; Protease; Proteasome; Threonine protease.
FT   CHAIN         1    241       Proteasome subunit alpha type-5.
FT                                /FTId=PRO_0000124118.
FT   MOD_RES       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      16     16       Phosphoserine (By similarity).
FT   MOD_RES      55     55       Phosphothreonine (By similarity).
FT   MOD_RES      56     56       Phosphoserine (By similarity).
SQ   SEQUENCE   241 AA;  26411 MW;  5610CDA00469120A CRC64;
     MFLTRSEYDR GVNTFSPEGR LFQVEYAIEA IKLGSTAIGI QTSEGVCLAV EKRITSPLME
     PSSIEKIVEI DAHIGCAMSG LIADAKTLID KARVETQNHW FTYNETMTVE SVTQAVSNLA
     LQFGEEDADP GAMSRPFGVA LLFGGVDEKG PQLFHMDPSG TFVQCDARAI GSASEGAQSS
     LQEVYHKSMT LKEAIKSSLI ILKQVMEEKL NATNIELATV QPGQNFHMFT KEELEEVIKD
     I
//
ID   HDAC6_MOUSE             Reviewed;        1149 AA.
AC   Q9Z2V5;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 2.
DT   08-MAR-2011, entry version 86.
DE   RecName: Full=Histone deacetylase 6;
DE            Short=HD6;
DE            EC=3.5.1.98;
DE   AltName: Full=Histone deacetylase mHDA2;
GN   Name=Hdac6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Fetus;
RX   MEDLINE=99107904; PubMed=9891014; DOI=10.1074/jbc.274.4.2440;
RA   Verdel A., Khochbin S.;
RT   "Identification of a new family of higher eukaryotic histone
RT   deacetylases. Coordinate expression of differentiation-dependent
RT   chromatin modifiers.";
RL   J. Biol. Chem. 274:2440-2445(1999).
RN   [2]
RP   INTERACTION WITH CBFA2T3.
RX   PubMed=11533236; DOI=10.1128/MCB.21.19.6470-6483.2001;
RA   Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N.,
RA   Downing J.R., Meyers S., Hiebert S.W.;
RT   "ETO, a target of t(8;21) in acute leukemia, makes distinct contacts
RT   with multiple histone deacetylases and binds mSin3A through its
RT   oligomerization domain.";
RL   Mol. Cell. Biol. 21:6470-6483(2001).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
RN   [4]
RP   FUNCTION, INTERACTION WITH CYLD AND MICROTUBULES, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=19893491; DOI=10.1038/emboj.2009.317;
RA   Wickstrom S.A., Masoumi K.C., Khochbin S., Fassler R., Massoumi R.;
RT   "CYLD negatively regulates cell-cycle progression by inactivating
RT   HDAC6 and increasing the levels of acetylated tubulin.";
RL   EMBO J. 29:131-144(2010).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on
CC       the N-terminal part of the core histones (H2A, H2B, H3 and H4).
CC       Histone deacetylation gives a tag for epigenetic repression and
CC       plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events. Histone deacetylases act via
CC       the formation of large multiprotein complexes (By similarity).
CC       Plays a central role in microtubule-dependent cell motility via
CC       deacetylation of tubulin.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC   -!- COFACTOR: Binds 3 zinc ions per subunit (By similarity).
CC   -!- SUBUNIT: Interacts with HDAC11 and SIRT2. Interacts with F-actin
CC       F-actin. Interacts with BBIP10. Under proteasome impairment
CC       conditions, interacts with UBD via its histone deacetylase 1 and
CC       UBP-type zinc-finger regions. Interacts with CYLD. Interacts with
CC       CBFA2T3.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=It is mainly
CC       cytoplasmic, where it is associated with microtubules.
CC   -!- TISSUE SPECIFICITY: Detected in keratinocytes (at protein level).
CC   -!- PTM: Ubiquitinated. Its polyubiquitination however does not lead
CC       to its degradation (By similarity).
CC   -!- PTM: Sumoylated in vitro (By similarity).
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 UBP-type zinc finger.
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DR   EMBL; AF006603; AAD09835.2; -; mRNA.
DR   IPI; IPI00323705; -.
DR   PIR; T13964; T13964.
DR   RefSeq; NP_034543.3; NM_010413.3.
DR   UniGene; Mm.29854; -.
DR   ProteinModelPortal; Q9Z2V5; -.
DR   SMR; Q9Z2V5; 84-438, 479-834, 1042-1149.
DR   MINT; MINT-220628; -.
DR   STRING; Q9Z2V5; -.
DR   PRIDE; Q9Z2V5; -.
DR   Ensembl; ENSMUST00000115642; ENSMUSP00000111306; ENSMUSG00000031161.
DR   GeneID; 15185; -.
DR   KEGG; mmu:15185; -.
DR   UCSC; uc009sni.1; mouse.
DR   CTD; 15185; -.
DR   MGI; MGI:1333752; Hdac6.
DR   GeneTree; ENSGT00530000062809; -.
DR   HOVERGEN; HBG051894; -.
DR   OrthoDB; EOG40P464; -.
DR   NextBio; 287707; -.
DR   ArrayExpress; Q9Z2V5; -.
DR   Bgee; Q9Z2V5; -.
DR   CleanEx; MM_HDAC6; -.
DR   Genevestigator; Q9Z2V5; -.
DR   GermOnline; ENSMUSG00000031161; Mus musculus.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IDA:MGI.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0048487; F:beta-tubulin binding; IDA:MGI.
DR   GO; GO:0004407; F:histone deacetylase activity; IDA:MGI.
DR   GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR   GO; GO:0042903; F:tubulin deacetylase activity; IDA:UniProtKB.
DR   GO; GO:0043130; F:ubiquitin binding; IDA:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0070842; P:aggresome assembly; IGI:MGI.
DR   GO; GO:0071218; P:cellular response to misfolded protein; IMP:MGI.
DR   GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
DR   GO; GO:0070846; P:Hsp90 deacetylation; IMP:MGI.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IDA:MGI.
DR   GO; GO:0043241; P:protein complex disassembly; IGI:MGI.
DR   GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
DR   GO; GO:0045449; P:regulation of transcription; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   GO; GO:0090042; P:tubulin deacetylation; IDA:UniProtKB.
DR   GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:MGI.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   Gene3D; G3DSA:3.40.800.20; His_deacetylse; 2.
DR   Gene3D; G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
DR   PANTHER; PTHR10625; His_deacetylse; 1.
DR   Pfam; PF00850; Hist_deacetyl; 2.
DR   Pfam; PF02148; zf-UBP; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Chromatin regulator; Cytoplasm; Hydrolase;
KW   Metal-binding; Nucleus; Phosphoprotein; Repeat; Repressor;
KW   Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1149       Histone deacetylase 6.
FT                                /FTId=PRO_0000114704.
FT   ZN_FING    1065   1126       UBP-type.
FT   REGION       87    403       Histone deacetylase 1.
FT   REGION      481    799       Histone deacetylase 2.
FT   REGION     1088   1090       Ubiquitin binding (By similarity).
FT   REGION     1116   1123       Ubiquitin binding (By similarity).
FT   COMPBIAS    455    460       Poly-Glu.
FT   ACT_SITE    215    215       1 (By similarity).
FT   ACT_SITE    610    610       2 (By similarity).
FT   METAL      1047   1047       Zinc 1 (By similarity).
FT   METAL      1049   1049       Zinc 1 (By similarity).
FT   METAL      1067   1067       Zinc 3 (By similarity).
FT   METAL      1070   1070       Zinc 3 (By similarity).
FT   METAL      1079   1079       Zinc 2 (By similarity).
FT   METAL      1082   1082       Zinc 2 (By similarity).
FT   METAL      1087   1087       Zinc 3 (By similarity).
FT   METAL      1094   1094       Zinc 3 (By similarity).
FT   METAL      1098   1098       Zinc 2 (By similarity).
FT   METAL      1104   1104       Zinc 2 (By similarity).
FT   METAL      1117   1117       Zinc 1 (By similarity).
FT   METAL      1120   1120       Zinc 1 (By similarity).
FT   MOD_RES      15     15       Phosphoserine.
FT   MOD_RES      21     21       Phosphoserine (By similarity).
FT   MOD_RES      29     29       Phosphothreonine (By similarity).
SQ   SEQUENCE   1149 AA;  125704 MW;  2B98CDB228CE0D1D CRC64;
     MTSTGQDSST RQRKSRHNPQ SPLQESSATL KRGGKKCAVP HSSPNLAEVK KKGKMKKLSQ
     PAEEDLVVGL QGLDLNPETR VPVGTGLVFD EQLNDFHCLW DDSFPESPER LHAIREQLIL
     EGLLGRCVSF QAWFAEKEEL MLVHSLEYID LMETTQYMNE GELRVLAETY DSVYLHPNSY
     SCACLATGSV LRLVDALMGA EIRNGMAVIR PPGHHAQHNL MDGYCMFNHL AVAARYAQKK
     HRIQRVLIVD WDVHHGQGTQ FIFDQDPSVL YFSIHRYEHG RFWPHLKASN WSTIGFGQGQ
     GYTINVPWNQ TGMRDADYIA AFLHILLPVA SEFQPQLVLV AAGFDALHGD PKGEMAATPA
     GFAHLTHLLM GLAGGKLILS LEGGYNLRAL AKGISASLHT LLGDPCPMLE SCVVPCASAQ
     ISIYCTLEAL EPFWEVLERS VETQEEDEVE EAVLEEEEEE GGWEATALPM DTWPLLQNRT
     GLVYDEKMMS HCNLWDNHHP ETPQRILRIM CHLEEVGLAA RCLILPARPA LGSELLTCHS
     AEYVEHLRTT EKMKTRDLHR EGANFDSIYI CPSTFACAKL ATGAACRLVE AVLSGEVLNG
     IAVVRPPGHH AEPNAACGFC FFNSVAVAAR HAQIIAGRAL RILIVDWDVH HGNGTQHIFE
     DDPSVLYVSL HRYDRGTFFP MGDEGASSQV GRDAGIGFTV NVPWNGPRMG DADYLAAWHR
     LVLPIAYEFN PELVLISAGF DAAQGDPLGG CQVTPEGYAH LTHLLMGLAG GRIILILEGG
     YNLASISESM AACTHSLLGD PPPQLTLLRP PQSGALVSIS EVIQVHRKYW RSLRLSKMED
     KEECSSSRLV VKKLPPTASP VSAKEMTTPK GKVPEESVRK TIAALPGKES TLGQAKSKMA
     KAVLAQGQSS EQAAKGTTLD LATSKETVGG ATTDLWASAA APENFPNQTT SVEALGETEP
     TPPASHTNKQ TTGASPLQGV TAQQSLQLGV LSTLELSREA EEAHDSEEGL LGEAAGGQDM
     NSLMLTQGFG DFNTQDVFYA VTPLSWCPHL MAVCPIPAAG LDVSQPCKTC GTVQENWVCL
     TCYQVYCSRY VNAHMVCHHE ASEHPLVLSC VDLSTWCYVC QAYVHQDDLQ DVKNAAHQNK
     FGEDMPHSH
//
ID   HDAC5_MOUSE             Reviewed;        1113 AA.
AC   Q9Z2V6; Q9JL73;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 2.
DT   08-MAR-2011, entry version 92.
DE   RecName: Full=Histone deacetylase 5;
DE            Short=HD5;
DE            EC=3.5.1.98;
DE   AltName: Full=Histone deacetylase mHDA1;
GN   Name=Hdac5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Fetus;
RX   MEDLINE=99107904; PubMed=9891014; DOI=10.1074/jbc.274.4.2440;
RA   Verdel A., Khochbin S.;
RT   "Identification of a new family of higher eukaryotic histone
RT   deacetylases. Coordinate expression of differentiation-dependent
RT   chromatin modifiers.";
RL   J. Biol. Chem. 274:2440-2445(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH NCOR2.
RC   STRAIN=C57BL/6;
RX   MEDLINE=20107033; PubMed=10640276;
RA   Kao H.-Y., Downes M., Ordentlich P., Evans R.M.;
RT   "Isolation of a novel histone deacetylase reveals that class I and
RT   class II deacetylases promote SMRT-mediated repression.";
RL   Genes Dev. 14:55-66(2000).
RN   [3]
RP   INTERACTION WITH HDAC7, NUCLEAR EXPORT, AND MUTAGENESIS OF HIS-824 AND
RP   HIS-884.
RX   MEDLINE=20442375; PubMed=10984530; DOI=10.1073/pnas.97.19.10330;
RA   Downes M., Ordentlich P., Kao H.-Y., Alvarez J.G.A., Evans R.M.;
RT   "Identification of a nuclear domain with deacetylase activity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:10330-10335(2000).
RN   [4]
RP   INTERACTION WITH CTBP1 AND HDAC9.
RX   PubMed=11022042; DOI=10.1074/jbc.M007364200;
RA   Zhang C.L., McKinsey T.A., Lu J.R., Olson E.N.;
RT   "Association of COOH-terminal-binding protein (CtBP) and MEF2-
RT   interacting transcription repressor (MITR) contributes to
RT   transcriptional repression of the MEF2 transcription factor.";
RL   J. Biol. Chem. 276:35-39(2001).
RN   [5]
RP   INTERACTION WITH PHB2.
RX   PubMed=15140878; DOI=10.1074/jbc.M312300200;
RA   Kurtev V., Margueron R., Kroboth K., Ogris E., Cavailles V.,
RA   Seiser C.;
RT   "Transcriptional regulation by the repressor of estrogen receptor
RT   activity via recruitment of histone deacetylases.";
RL   J. Biol. Chem. 279:24834-24843(2004).
RN   [6]
RP   INTERACTION WITH NRIP1.
RX   PubMed=15060175; DOI=10.1093/nar/gkh524;
RA   Castet A., Boulahtouf A., Versini G., Bonnet S., Augereau P.,
RA   Vignon F., Khochbin S., Jalaguier S., Cavailles V.;
RT   "Multiple domains of the receptor-interacting protein 140 contribute
RT   to transcription inhibition.";
RL   Nucleic Acids Res. 32:1957-1966(2004).
RN   [7]
RP   INTERACTION WITH AHRR.
RX   PubMed=17949687; DOI=10.1016/j.bbrc.2007.09.131;
RA   Oshima M., Mimura J., Yamamoto M., Fujii-Kuriyama Y.;
RT   "Molecular mechanism of transcriptional repression of AhR repressor
RT   involving ANKRA2, HDAC4, and HDAC5.";
RL   Biochem. Biophys. Res. Commun. 364:276-282(2007).
CC   -!- FUNCTION: Responsible for the deacetylation of lysine residues on
CC       the N-terminal part of the core histones (H2A, H2B, H3 and H4).
CC       Histone deacetylation gives a tag for epigenetic repression and
CC       plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events. Histone deacetylases act via
CC       the formation of large multiprotein complexes. Involved in muscle
CC       maturation by repressing transcription of myocyte enhancer MEF2C.
CC       During muscle differentiation, it shuttles into the cytoplasm,
CC       allowing the expression of myocyte enhancer factors (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC   -!- SUBUNIT: Interacts with BAHD1 and KDM5B (By similarity). Interacts
CC       with BCOR, HDAC7, HDAC9, CTBP1, MEF2C, NCOR2, NRIP1, PHB2, AHRR,
CC       and a 14-3-3 chaperone protein.
CC   -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By
CC       similarity). Note=Shuttles between the nucleus and the cytoplasm.
CC       In muscle cells, it shuttles into the cytoplasm during myocyte
CC       differentiation. The export to cytoplasm depends on the
CC       interaction with a 14-3-3 chaperone protein and is due to its
CC       phosphorylation at Ser-250 and Ser-488 by CaMK (By similarity).
CC   -!- DOMAIN: The nuclear export sequence mediates the shuttling between
CC       the nucleus and the cytoplasm.
CC   -!- PTM: Phosphorylated by CaMK at Ser-250 and Ser-488. The
CC       phosphorylation is required for the export to the cytoplasm.
CC       Phosphorylated by the PKC kinases PKN1 and PKN2, impairing nuclear
CC       import (By similarity).
CC   -!- PTM: Ubiquitinated. Polyubiquitination however does not lead to
CC       its degradation (By similarity).
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF006602; AAD09834.2; -; mRNA.
DR   EMBL; AF207748; AAF31418.1; -; mRNA.
DR   IPI; IPI00816951; -.
DR   UniGene; Mm.22665; -.
DR   ProteinModelPortal; Q9Z2V6; -.
DR   SMR; Q9Z2V6; 68-132, 672-1072.
DR   DIP; DIP-40855N; -.
DR   IntAct; Q9Z2V6; 1.
DR   STRING; Q9Z2V6; -.
DR   PhosphoSite; Q9Z2V6; -.
DR   PRIDE; Q9Z2V6; -.
DR   Ensembl; ENSMUST00000107152; ENSMUSP00000102770; ENSMUSG00000008855.
DR   MGI; MGI:1333784; Hdac5.
DR   GeneTree; ENSGT00530000062809; -.
DR   HOVERGEN; HBG057100; -.
DR   OrthoDB; EOG4DR9BQ; -.
DR   ArrayExpress; Q9Z2V6; -.
DR   Bgee; Q9Z2V6; -.
DR   CleanEx; MM_HDAC5; -.
DR   Genevestigator; Q9Z2V6; -.
DR   GermOnline; ENSMUSG00000008855; Mus musculus.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0000118; C:histone deacetylase complex; TAS:UniProtKB.
DR   GO; GO:0016604; C:nuclear body; IDA:MGI.
DR   GO; GO:0004407; F:histone deacetylase activity; TAS:UniProtKB.
DR   GO; GO:0016566; F:specific transcriptional repressor activity; TAS:UniProtKB.
DR   GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR   GO; GO:0008134; F:transcription factor binding; TAS:UniProtKB.
DR   GO; GO:0030183; P:B cell differentiation; TAS:UniProtKB.
DR   GO; GO:0016568; P:chromatin modification; TAS:UniProtKB.
DR   GO; GO:0007507; P:heart development; IGI:MGI.
DR   GO; GO:0006954; P:inflammatory response; TAS:UniProtKB.
DR   GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:MGI.
DR   GO; GO:0045843; P:negative regulation of striated muscle tissue development; TAS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
DR   GO; GO:0007399; P:nervous system development; TAS:UniProtKB.
DR   GO; GO:0002076; P:osteoblast development; IMP:MGI.
DR   GO; GO:0048742; P:regulation of skeletal muscle fiber development; IGI:MGI.
DR   GO; GO:0042220; P:response to cocaine; IDA:MGI.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR017320; Histone_deAcase_II_euk.
DR   Gene3D; G3DSA:3.40.800.20; His_deacetylse; 1.
DR   PANTHER; PTHR10625; His_deacetylse; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037911; HDAC_II_euk; 1.
DR   PRINTS; PR01270; HDASUPER.
PE   1: Evidence at protein level;
KW   Acetylation; Chromatin regulator; Cytoplasm; Hydrolase; Nucleus;
KW   Phosphoprotein; Repressor; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN         1   1113       Histone deacetylase 5.
FT                                /FTId=PRO_0000114702.
FT   REGION      675   1019       Histone deacetylase.
FT   MOTIF      1072   1113       Nuclear export signal (By similarity).
FT   COMPBIAS     47     52       Poly-Gly.
FT   COMPBIAS     85     92       Poly-Gln.
FT   COMPBIAS    577    588       Poly-Glu.
FT   ACT_SITE    824    824       By similarity.
FT   MOD_RES     250    250       Phosphoserine; by CaMK (By similarity).
FT   MOD_RES     283    283       Phosphothreonine; by PKC (By similarity).
FT   MOD_RES     488    488       Phosphoserine; by CaMK (By similarity).
FT   MOD_RES     523    523       N6-acetyllysine (By similarity).
FT   MOD_RES     650    650       Phosphoserine (By similarity).
FT   MUTAGEN     824    824       H->A: Abolishes deacetylase activity.
FT   MUTAGEN     884    884       H->F: Disrupts the dot-like nuclear
FT                                pattern.
FT   CONFLICT      7      7       S -> SA (in Ref. 2; AAF31418).
FT   CONFLICT     18     18       G -> E (in Ref. 2; AAF31418).
SQ   SEQUENCE   1113 AA;  120942 MW;  63071AF45B87815A CRC64;
     MNSPNESDGM SGREPSLGIL PRTPLHSIPV AVEVKPVLPG AMPSSMGGGG GGSPSPVELR
     GALAGPMDPA LREQQLQQEL LVLKQQQQLQ KQLLFAEFQK QHDHLTRQHE VQLQKHLKQQ
     QEMLAAKRQQ ELEQQRQREQ QRQEELEKQR LEQQLLILRN KEKSKESAIA STEVKLRLQE
     FLLSKSKEPT PGGLNHSLPQ HPKCWGAHHA SLDQSSPPQS GPPGTPPSYK LPLLGPYDSR
     DDFPLRKTAS EPNLKVRSRL KQKVAERRSS PLLRRKDGTV ISTFKKRAVE ITGTGPGVSS
     VCNSAPGSGP SSPNSSHSTI AENGFTGSVP NIPTEMIPQH RALPLDSSPN QFSLYTSPSL
     PNISLGLQAT VTVTNSHLTA SPKLSTQQEA ERQALQSLRQ GGTLTGKFMS TSSIPGCLLG
     VALEGDTSPH GHASLLQHVC SWTGRQQSTL IAVPLHGQSP LVTGERVATS MRTVGKLPRH
     RPLSRTQSSP LPQSPQALQQ LVMQQQHQQF LEKQKQQQMQ LGKILTKTGE LSRQPTTHPE
     ETEEELTEQQ EALLGEGALT IPREGSTESE STQEDLEEEE EEEEEEEEDC IQVKDEDGES
     GPDEGPDLEE SSAGYKKLFA DAQQLQPLQV YQAPLSLATV PHQALGRTQS SPAAPGSMKS
     PTDQPTVVKH LFTTGVVYDT FMLKHQCMCG NTHVHPEHAG RIQSIWSRLQ ETGLLGKCER
     IRGRKATLDE IQTVHSEYHT LLYGTSPLNR QKLDSKKLLG PISQKMYAML PCGGIGVDSD
     TVWNEMHSSS AVRMAVGCLV ELAFKVAAGE LKNGFAIIRP PGHHAEESTA MGFCFFNSVA
     ITAKLLQQKL SVGKVLIVDW DIHHGNGTQQ AFYNDPSVLY ISLHRYDNGN FFPGSGAPEE
     VGGGPGVGYN VNVAWTGGVD PPIGDVEYLT AFRTVVMPIA QEFSPDVVLV SAGFDAVEGH
     LSPLGGYSVT ARCFGHLTRQ LMTLAGGRVV LALEGGHDLT AICDASEACV SALLSVELQP
     LDEAVLQQKP SVNAVATLEK VIEIQSKHWS CVQRFAAGLG CSLREAQTGE KEEAETVSAM
     ALLSVGAEQA QAVATQEHSP RPAEEPMEQE PAL
//
ID   DNPEP_MOUSE             Reviewed;         473 AA.
AC   Q9Z2W0;
DT   24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 71.
DE   RecName: Full=Aspartyl aminopeptidase;
DE            EC=3.4.11.21;
GN   Name=Dnpep;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98298097; PubMed=9632644; DOI=10.1074/jbc.273.26.15961;
RA   Wilk S., Wilk E., Magnusson R.P.;
RT   "Purification, characterization, and cloning of a cytosolic aspartyl
RT   aminopeptidase.";
RL   J. Biol. Chem. 273:15961-15970(1998).
CC   -!- FUNCTION: Likely to play an important role in intracellular
CC       protein and peptide metabolism.
CC   -!- CATALYTIC ACTIVITY: Release of an N-terminal aspartate or
CC       glutamate from a peptide, with a preference for aspartate.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Homooctamer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC   -----------------------------------------------------------------------
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DR   EMBL; AF005051; AAD01212.1; -; mRNA.
DR   IPI; IPI00331394; -.
DR   UniGene; Mm.24680; -.
DR   ProteinModelPortal; Q9Z2W0; -.
DR   SMR; Q9Z2W0; 5-470.
DR   STRING; Q9Z2W0; -.
DR   MEROPS; M18.002; -.
DR   PhosphoSite; Q9Z2W0; -.
DR   REPRODUCTION-2DPAGE; Q9Z2W0; -.
DR   PRIDE; Q9Z2W0; -.
DR   Ensembl; ENSMUST00000066668; ENSMUSP00000070821; ENSMUSG00000026209.
DR   Ensembl; ENSMUST00000113605; ENSMUSP00000109235; ENSMUSG00000026209.
DR   MGI; MGI:1278328; Dnpep.
DR   GeneTree; ENSGT00390000003164; -.
DR   HOVERGEN; HBG051386; -.
DR   InParanoid; Q9Z2W0; -.
DR   OrthoDB; EOG4N8R4J; -.
DR   PhylomeDB; Q9Z2W0; -.
DR   BRENDA; 3.4.11.21; 244.
DR   ArrayExpress; Q9Z2W0; -.
DR   Bgee; Q9Z2W0; -.
DR   CleanEx; MM_DNPEP; -.
DR   Genevestigator; Q9Z2W0; -.
DR   GermOnline; ENSMUSG00000026209; Mus musculus.
DR   GO; GO:0005773; C:vacuole; IEA:InterPro.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   Gene3D; G3DSA:2.30.250.10; G3DSA:2.30.250.10; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   2: Evidence at transcript level;
KW   Acetylation; Aminopeptidase; Cytoplasm; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Zinc.
FT   CHAIN         1    473       Aspartyl aminopeptidase.
FT                                /FTId=PRO_0000173452.
FT   METAL        92     92       Zinc (Potential).
FT   METAL       168    168       Zinc (Potential).
FT   METAL       438    438       Zinc (Potential).
FT   MOD_RES      21     21       N6-acetyllysine (By similarity).
SQ   SEQUENCE   473 AA;  52167 MW;  FDD6BE8FE26EEDBF CRC64;
     MAMNGRARKE AIQATARELL KFVNRSPSPF HVVAECRSRL LQAGFRELKE TEGWDIVPEN
     NYFLTRNSSS IIAFAVGGQY VPGNGFSLIG AHTDSPCLRV KRKSRRSQVG YHQVGVETYG
     GGIWSTWFDR DLTLAGRVII KCPTSGRLEQ RLVHIERPIL RIPHLAIHLQ RNINENFGPN
     TEIHLVPILA TAVQEELEKG TPEPGPLGAT DERHHSVLMS LLCTHLGLSP DSIMEMELCL
     ADTQPAVLGG AYEEFIFAPR LDNLHSCFCA LQALIDSCAS PASLARDPHV RMVTLYDNEE
     VGSESAQGAQ SLLTELILRR ISASPQRLTA FEEAIPKSFM ISADMAHAVH PNYSDKHEEN
     HRPSFHKGPV IKVNSKQRYA SNAVSESMIR EVAGQVGVPL QDLMVRNDSP CGTTIGPILA
     SRLGLRVLDL GSPQLAMHSI RETACTTGVL QTLTLFKGFF ELFPSVSRNL LVD
//
ID   GRIA4_MOUSE             Reviewed;         902 AA.
AC   Q9Z2W8;
DT   11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 91.
DE   RecName: Full=Glutamate receptor 4;
DE            Short=GluR-4;
DE            Short=GluR4;
DE   AltName: Full=AMPA-selective glutamate receptor 4;
DE   AltName: Full=GluR-D;
DE   AltName: Full=Glutamate receptor ionotropic, AMPA 4;
DE            Short=GluA4;
DE   Flags: Precursor;
GN   Name=Gria4; Synonyms=Glur4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6;
RA   Sakimura K., Ikeno K.;
RT   "Mouse glutamate receptor channel alpha4 subunit.";
RL   Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PALMITOYLATION AT CYS-837.
RX   PubMed=16129400; DOI=10.1016/j.neuron.2005.06.035;
RA   Hayashi T., Rumbaugh G., Huganir R.L.;
RT   "Differential regulation of AMPA receptor subunit trafficking by
RT   palmitoylation of two distinct sites.";
RL   Neuron 47:709-723(2005).
CC   -!- FUNCTION: Ionotropic glutamate receptor. L-glutamate acts as an
CC       excitatory neurotransmitter at many synapses in the central
CC       nervous system. Binding of the excitatory neurotransmitter L-
CC       glutamate induces a conformation change, leading to the opening of
CC       the cation channel, and thereby converts the chemical signal to an
CC       electrical impulse. The receptor then desensitizes rapidly and
CC       enters a transient inactive state, characterized by the presence
CC       of bound agonist (By similarity).
CC   -!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate
CC       receptor subunits. Tetramers may be formed by the dimerization of
CC       dimers. Interacts with EPB41L1 via its C-terminus (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Cell junction, synapse, postsynaptic cell membrane; Multi-pass
CC       membrane protein.
CC   -!- PTM: Palmitoylated. Depalmitoylated upon glutamate stimulation.
CC       Cys-611 palmitoylation leads to Golgi retention and decreased cell
CC       surface expression. In contrast, Cys-837 palmitoylation does not
CC       affect cell surface expression but regulates stimulation-dependent
CC       endocytosis (By similarity).
CC   -!- MISCELLANEOUS: The postsynaptic actions of Glu are mediated by a
CC       variety of receptors that are named according to their selective
CC       agonists. This receptor binds AMPA (quisqualate) > glutamate >
CC       kainate.
CC   -!- SIMILARITY: Belongs to the glutamate-gated ion channel
CC       (TC 1.A.10.1) family. GRIA4 subfamily.
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DR   EMBL; AB022913; BAA74538.1; -; mRNA.
DR   IPI; IPI00131471; -.
DR   RefSeq; NP_001106651.1; NM_001113180.1.
DR   RefSeq; NP_062665.3; NM_019691.4.
DR   UniGene; Mm.209263; -.
DR   UniGene; Mm.477102; -.
DR   ProteinModelPortal; Q9Z2W8; -.
DR   SMR; Q9Z2W8; 25-839.
DR   STRING; Q9Z2W8; -.
DR   PhosphoSite; Q9Z2W8; -.
DR   PRIDE; Q9Z2W8; -.
DR   Ensembl; ENSMUST00000027020; ENSMUSP00000027020; ENSMUSG00000025892.
DR   GeneID; 14802; -.
DR   KEGG; mmu:14802; -.
DR   UCSC; uc009obo.1; mouse.
DR   CTD; 14802; -.
DR   MGI; MGI:95811; Gria4.
DR   GeneTree; ENSGT00590000082809; -.
DR   HOGENOM; HBG381523; -.
DR   HOVERGEN; HBG051839; -.
DR   InParanoid; Q9Z2W8; -.
DR   OrthoDB; EOG4DBTD0; -.
DR   ArrayExpress; Q9Z2W8; -.
DR   Bgee; Q9Z2W8; -.
DR   CleanEx; MM_GRIA4; -.
DR   Genevestigator; Q9Z2W8; -.
DR   GermOnline; ENSMUSG00000025892; Mus musculus.
DR   GO; GO:0032281; C:alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid selective glutamate receptor complex; IDA:MGI.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005234; F:extracellular-glutamate-gated ion channel activity; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR019594; Glu_rcpt_Glu/Gly-bd.
DR   InterPro; IPR001320; Iontro_glu_rcpt.
DR   InterPro; IPR001508; NMDA_rcpt.
DR   Pfam; PF01094; ANF_receptor; 1.
DR   Pfam; PF00060; Lig_chan; 1.
DR   Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR   PRINTS; PR00177; NMDARECEPTOR.
DR   SMART; SM00918; Lig_chan-Glu_bd; 1.
DR   SMART; SM00079; PBPe; 1.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Glycoprotein; Ion transport;
KW   Ionic channel; Ligand-gated ion channel; Lipoprotein; Membrane;
KW   Palmitate; Postsynaptic cell membrane; Receptor; Signal; Synapse;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21    902       Glutamate receptor 4.
FT                                /FTId=PRO_0000011539.
FT   TOPO_DOM     21    544       Extracellular (Potential).
FT   TRANSMEM    545    565       Helical; (Potential).
FT   TOPO_DOM    566    625       Cytoplasmic (Potential).
FT   TRANSMEM    626    646       Helical; (Potential).
FT   TOPO_DOM    647    813       Extracellular (Potential).
FT   TRANSMEM    814    834       Helical; (Potential).
FT   TOPO_DOM    835    902       Cytoplasmic (Potential).
FT   REGION      500    502       Glutamate binding (By similarity).
FT   REGION      676    677       Glutamate binding (By similarity).
FT   BINDING     507    507       Glutamate (By similarity).
FT   BINDING     727    727       Glutamate (By similarity).
FT   LIPID       611    611       S-palmitoyl cysteine (By similarity).
FT   LIPID       837    837       S-palmitoyl cysteine.
FT   CARBOHYD     56     56       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    258    258       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    371    371       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    407    407       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    414    414       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   902 AA;  100632 MW;  55E3D0866AD0EC81 CRC64;
     MRIICRQIVL LFSGFWGLAM GAFPSSVQIG GLFIRNTDQE YTAFRLAIFL HNTSPNASEA
     PFNLVPHVDN IETANSFAVT NAFCSQYSRG VFAIFGLYDK RSVHTLTSFC SALHISLITP
     SFPTEGESQF VLQLRPSLRG ALLSLLDHYE WNCFVFLYDT DRGYSILQAI MEKAGQNGWH
     VSAICVENFN DVSYRQLLEE LDRRQEKKFV IDCEIERLQN ILEQIVSVGK HVKGYHYIIA
     NLGFKDISLE RFIHGGANVT GFQLVDFNTP MVTKLMDRWK KLDQREYPGS ETPPKYTSAL
     TYDGVLVMAE TFRSLRRQKI DISRRGNAGD CLANPAAPWG QGIDMERTLK QVRIQGLTGN
     VQFDHYGRRV NYTMDVFELK STGPRKVGYW NDMDKLVLIQ DAPTLGNDTA AIENRTVVVT
     TIMESPYVMY KKNHEMFEGN DKYEGYCVDL ASEIAKHIGI KYKIAIVPDG KYGARDADTK
     IWNGMVGELV YGKAEIAIAP LTITLVREEV IDFSKPFMSL GISIMIKKPQ KSKPGVFSFL
     DPLAYEIWMC IVFAYIGVSV VLFLVSRFSP YEWHTEEPED GKEGPSDQPP NEFGIFNSLW
     FSLGAFMQQG CDISPRSLSG RIVGGVWWFG TLIIISSYTA NLAAFLTVER MVSPIESAED
     LAKQTEIAYG TLDSGSTKEF FRRSKIAVYE KMWTYMRSAE PSVFTRTTAE GVARVRKSKG
     KFAFLLESTM NEYIEQRKPC DTMKVGGNLD SKGYGVATPK GSSLGNAVNL AVLKLNEQGL
     LDKLKNKWWY DKGECGSGGG DSKDKTSALS LSNVAGVFYI LVGGLGLAML VALIEFCYKS
     RAEAKRMKLT FSEAIRNKAR LSITGSVGEN GRVLTPDCPK AVHTGTAIRQ SSGLAVIASD
     LP
//
ID   HNRPF_MOUSE             Reviewed;         415 AA.
AC   Q9Z2X1; Q5FWK2; Q8BVU8; Q8K2U9; Q8R0E7;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   08-MAR-2011, entry version 101.
DE   RecName: Full=Heterogeneous nuclear ribonucleoprotein F;
DE            Short=hnRNP F;
DE   Contains:
DE     RecName: Full=Heterogeneous nuclear ribonucleoprotein F, N-terminally processed;
GN   Name=Hnrnpf; Synonyms=Hnrpf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Head;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6, Czech II, and FVB/N;
RC   TISSUE=Eye, Fetal brain, Mammary gland, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   STRUCTURE BY NMR OF 1-105.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the RNA binding domain in heterogeneous nuclear
RT   ribonucleoprotein F homolog.";
RL   Submitted (JUN-2006) to the PDB data bank.
CC   -!- FUNCTION: Component of the heterogeneous nuclear ribonucleoprotein
CC       (hnRNP) complexes which provide the substrate for the processing
CC       events that pre-mRNAs undergo before becoming functional,
CC       translatable mRNAs in the cytoplasm. Plays a role in the
CC       regulation of alternative splicing events. Binds G-rich sequences
CC       in pre-mRNAs and keeps target RNA in an unfolded state (By
CC       similarity).
CC   -!- SUBUNIT: Identified in the spliceosome C complex, at least
CC       composed of AQR, ASCC3L1, C19orf29, CDC40, CDC5L, CRNKL1, DDX23,
CC       DDX41, DDX48, DDX5, DGCR14, DHX35, DHX38, DHX8, EFTUD2, FRG1,
CC       GPATC1, HNRPA1, HNRPA2B1, HNRPA3, HNRPC, HNRNPF, HNRPH1, HNRPK,
CC       HNRPM, HNRPR, HNRPU, KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1,
CC       PABPC1, PLRG1, PNN, PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B,
CC       PRPF6, PRPF8, RALY, RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2,
CC       SF3A3, SF3B1, SF3B2, SF3B3, SFRS1, SKIV2L2, SNRPA1, SNRPB, SNRPB2,
CC       SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2,
CC       SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, WDR57, XAB2 and ZCCHC8.
CC       Interacts with TBP and TXNL4/DIM1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Z2X1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Z2X1-2; Sequence=VSP_021004;
CC   -!- DOMAIN: The N-terminal RRM domains are responsible for recognizing
CC       the G-tract of BCL-X RNA (By similarity).
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By
CC       similarity).
CC   -!- PTM: Sumoylated (By similarity).
CC   -!- SIMILARITY: Contains 3 RRM (RNA recognition motif) domains.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH27003.1; Type=Erroneous initiation;
CC       Sequence=AAH29764.1; Type=Erroneous initiation;
CC       Sequence=BAC36361.1; Type=Erroneous termination; Positions=416; Note=Translated as stop;
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DR   EMBL; AK076478; BAC36361.1; ALT_SEQ; mRNA.
DR   EMBL; BC018185; AAH18185.1; -; mRNA.
DR   EMBL; BC025481; AAH25481.1; -; mRNA.
DR   EMBL; BC027003; AAH27003.1; ALT_INIT; mRNA.
DR   EMBL; BC029163; AAH29163.1; -; mRNA.
DR   EMBL; BC029764; AAH29764.1; ALT_INIT; mRNA.
DR   EMBL; BC033483; AAH33483.1; -; mRNA.
DR   EMBL; BC089313; AAH89313.1; -; mRNA.
DR   IPI; IPI00226073; -.
DR   IPI; IPI00798511; -.
DR   RefSeq; NP_001159899.1; NM_001166427.1.
DR   RefSeq; NP_001159900.1; NM_001166428.1.
DR   RefSeq; NP_001159901.1; NM_001166429.1.
DR   RefSeq; NP_001159902.1; NM_001166430.1.
DR   RefSeq; NP_001159903.1; NM_001166431.1.
DR   RefSeq; NP_001159904.1; NM_001166432.1.
DR   RefSeq; NP_598595.1; NM_133834.2.
DR   UniGene; Mm.422979; -.
DR   UniGene; Mm.426508; -.
DR   UniGene; Mm.437031; -.
DR   UniGene; Mm.475176; -.
DR   UniGene; Mm.476420; -.
DR   UniGene; Mm.479505; -.
DR   PDB; 2DB1; NMR; -; A=1-105.
DR   PDBsum; 2DB1; -.
DR   ProteinModelPortal; Q9Z2X1; -.
DR   SMR; Q9Z2X1; 1-194, 287-367.
DR   STRING; Q9Z2X1; -.
DR   PhosphoSite; Q9Z2X1; -.
DR   REPRODUCTION-2DPAGE; Q9Z2X1; -.
DR   PRIDE; Q9Z2X1; -.
DR   Ensembl; ENSMUST00000035493; ENSMUSP00000045048; ENSMUSG00000042079.
DR   GeneID; 98758; -.
DR   KEGG; mmu:98758; -.
DR   UCSC; uc009dle.1; mouse.
DR   CTD; 98758; -.
DR   MGI; MGI:2138741; Hnrnpf.
DR   eggNOG; roNOG06834; -.
DR   GeneTree; ENSGT00550000074195; -.
DR   HOGENOM; HBG447282; -.
DR   HOVERGEN; HBG055557; -.
DR   InParanoid; Q9Z2X1; -.
DR   OMA; SADTAND; -.
DR   OrthoDB; EOG4CRM03; -.
DR   PhylomeDB; Q9Z2X1; -.
DR   NextBio; 353639; -.
DR   Bgee; Q9Z2X1; -.
DR   Genevestigator; Q9Z2X1; -.
DR   GermOnline; ENSMUSG00000042079; Mus musculus.
DR   GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003727; F:single-stranded RNA binding; ISS:UniProtKB.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR012996; Znf_CHHC.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 3.
DR   Pfam; PF00076; RRM_1; 2.
DR   Pfam; PF08080; zf-RNPHF; 1.
DR   SMART; SM00360; RRM; 3.
DR   PROSITE; PS50102; RRM; 3.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Isopeptide bond;
KW   mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Repeat;
KW   Ribonucleoprotein; RNA-binding; Spliceosome; Ubl conjugation.
FT   CHAIN         1    415       Heterogeneous nuclear ribonucleoprotein
FT                                F.
FT                                /FTId=PRO_0000367116.
FT   INIT_MET      1      1       Removed; alternate (By similarity).
FT   CHAIN         2    415       Heterogeneous nuclear ribonucleoprotein
FT                                F, N-terminally processed.
FT                                /FTId=PRO_0000253053.
FT   DOMAIN       11     90       RRM 1.
FT   DOMAIN      111    188       RRM 2.
FT   DOMAIN      289    366       RRM 3.
FT   REGION       81     86       Interaction with RNA (By similarity).
FT   REGION      179    184       Interaction with RNA (By similarity).
FT   REGION      355    360       Interaction with RNA (By similarity).
FT   SITE         16     16       Interaction with RNA (By similarity).
FT   SITE         20     20       Interaction with RNA (By similarity).
FT   SITE         52     52       Interaction with RNA (By similarity).
FT   SITE         75     75       Interaction with RNA (By similarity).
FT   SITE        116    116       Interaction with RNA (By similarity).
FT   SITE        120    120       Interaction with RNA (By similarity).
FT   SITE        150    150       Interaction with RNA (By similarity).
FT   SITE        173    173       Interaction with RNA (By similarity).
FT   SITE        294    294       Interaction with RNA (By similarity).
FT   SITE        298    298       Interaction with RNA (By similarity).
FT   SITE        326    326       Interaction with RNA (By similarity).
FT   SITE        349    349       Interaction with RNA (By similarity).
FT   MOD_RES       1      1       N-acetylmethionine; in Heterogeneous
FT                                nuclear ribonucleoprotein F; alternate
FT                                (By similarity).
FT   MOD_RES       2      2       N-acetylmethionine; in Heterogeneous
FT                                nuclear ribonucleoprotein F, N-terminally
FT                                processed (By similarity).
FT   MOD_RES      87     87       N6-acetyllysine (By similarity).
FT   MOD_RES     104    104       Phosphoserine (By similarity).
FT   MOD_RES     161    161       Phosphoserine (By similarity).
FT   MOD_RES     187    187       Phosphoserine (By similarity).
FT   MOD_RES     224    224       N6-acetyllysine (By similarity).
FT   MOD_RES     246    246       Phosphotyrosine (By similarity).
FT   MOD_RES     310    310       Phosphoserine (By similarity).
FT   CROSSLNK     72     72       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO) (By
FT                                similarity).
FT   VAR_SEQ       1     22       MMLGPEGGEGYVVKLRGLPWSC -> MW (in isoform
FT                                2).
FT                                /FTId=VSP_021004.
FT   CONFLICT    272    272       Y -> C (in Ref. 2; AAH27003).
FT   STRAND        3      5
FT   STRAND       12     17
FT   HELIX        24     30
FT   TURN         31     33
FT   HELIX        39     42
FT   STRAND       43     47
FT   STRAND       49     51
FT   STRAND       53     63
FT   HELIX        64     70
FT   HELIX        71     73
FT   STRAND       76     78
FT   STRAND       81     88
FT   HELIX        90     98
SQ   SEQUENCE   415 AA;  45730 MW;  31E1C9C90A8E051F CRC64;
     MMLGPEGGEG YVVKLRGLPW SCSIEDVQNF LSDCTIHDGV AGVHFIYTRE GRQSGEAFVE
     LESEDDVKLA LKKDRESMGH RYIEVFKSHR TEMDWVLKHS GPNSADSAND GFVRLRGLPF
     GCTKEEIVQF FSGLEIVPNG ITLPVDPEGK ITGEAFVQFA SQELAEKALG KHKERIGHRY
     IEVFKSSQEE VRSYSDPPLK FMSVQRPGPY DRPGTARRYI GIVKQAGLDR MRSGAYSAGY
     GGYEEYSGLS DGYGFTTDLF GRDLSYCLSG MYDHRYGDSE FTVQSTTGHC VHMRGLPYKA
     TENDIYNFFS PLNPVRVHIE IGPDGRVTGE ADVEFATHEE AVAAMSKDRA NMQHRYIELF
     LNSTTGASNG AYSSQVMQGM GVSAAQATYS GLESQSVSGC YGAGYSGQNS MGGYD
//
ID   HOME1_MOUSE             Reviewed;         366 AA.
AC   Q9Z2Y3; Q8K3E1; Q8K4M8; Q9Z0E9; Q9Z216;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2003, sequence version 2.
DT   08-FEB-2011, entry version 92.
DE   RecName: Full=Homer protein homolog 1;
DE            Short=Homer-1;
DE   AltName: Full=VASP/Ena-related gene up-regulated during seizure and LTP 1;
DE            Short=Vesl-1;
GN   Name=Homer1; Synonyms=Vesl1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 5).
RC   STRAIN=C57BL/6J; TISSUE=Forebrain;
RX   MEDLINE=99023644; PubMed=9808458; DOI=10.1016/S0896-6273(00)80588-7;
RA   Xiao B., Tu J.C., Petralia R.S., Yuan J.P., Doan A., Breder C.D.,
RA   Ruggiero A., Lanahan A.A., Wenthold R.J., Worley P.F.;
RT   "Homer regulates the association of group 1 metabotropic glutamate
RT   receptors with multivalent complexes of homer-related, synaptic
RT   proteins.";
RL   Neuron 21:707-716(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   STRAIN=BALB/c; TISSUE=Heart;
RX   MEDLINE=22165472; PubMed=12176012; DOI=10.1016/S0006-291X(02)00899-9;
RA   Saito H., Kimura M., Inanobe A., Ohe T., Kurachi Y.;
RT   "An N-terminal sequence specific for a novel Homer1 isoform controls
RT   trafficking of group I metabotropic glutamate receptor in mammalian
RT   cells.";
RL   Biochem. Biophys. Res. Commun. 296:523-529(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5).
RC   STRAIN=C57BL/6N; TISSUE=Brain cortex;
RA   Inokuchi K., Hayashi F.;
RT   "Mouse Vesl family of EVH-protein that interacts with group I
RT   mGluRs.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC   STRAIN=129/SvJ; TISSUE=Hippocampus;
RA   Hayashi F., Hirai K., Inokuchi K.;
RT   "Genomic structure of mouse vesl-1 gene.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   INTERACTION WITH GRM1; GRM5; DYN3 AND ITPR1.
RX   MEDLINE=99023645; PubMed=9808459; DOI=10.1016/S0896-6273(00)80589-9;
RA   Tu J.C., Xiao B., Yuan J.P., Lanahan A.A., Leoffert K., Li M.,
RA   Linden D.J., Worley P.F.;
RT   "Homer binds a novel proline-rich motif and links group 1 metabotropic
RT   glutamate receptors with IP3 receptors.";
RL   Neuron 21:717-726(1998).
RN   [6]
RP   REVIEW.
RX   PubMed=10851183; DOI=10.1016/S0959-4388(00)00087-8;
RA   Xiao B., Tu J.C., Worley P.F.;
RT   "Homer: a link between neural activity and glutamate receptor
RT   function.";
RL   Curr. Opin. Neurobiol. 10:370-374(2000).
RN   [7]
RP   TISSUE SPECIFICITY, AND INTERACTION WITH ITPR1.
RX   PubMed=12379179; DOI=10.1016/S0143416002001549;
RA   Salanova M., Priori G., Barone V., Intravaia E., Flucher B.,
RA   Ciruela F., McIlhinney R.A.J., Parys J.B., Mikoshiba K.,
RA   Sorrentino V.;
RT   "Homer proteins and InsP(3) receptors co-localise in the longitudinal
RT   sarcoplasmic reticulum of skeletal muscle fibres.";
RL   Cell Calcium 32:193-200(2002).
RN   [8]
RP   INTERACTION WITH IFT57.
RX   PubMed=17107665; DOI=10.1016/j.bbrc.2006.10.167;
RA   Sakamoto K., Yoshida S., Ikegami K., Minakami R., Kato A., Udo H.,
RA   Sugiyama H.;
RT   "Homer1c interacts with Hippi and protects striatal neurons from
RT   apoptosis.";
RL   Biochem. Biophys. Res. Commun. 352:1-5(2007).
CC   -!- FUNCTION: Postsynaptic density scaffolding protein. Binds and
CC       cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1,
CC       RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with
CC       ER-associated ITPR1 receptors, it aids the coupling of surface
CC       receptors to intracellular calcium release. May also couple GRM1
CC       to PI3 kinase through its interaction with AGAP2. Isoform 1
CC       regulates the trafficking and surface expression of GRM5.
CC       Differentially regulates the functions of the calcium activated
CC       channel ryanodine receptors RYR1 and RYR2. Isoform 1 decreases the
CC       activity of RYR2, and increases the activity of RYR1, whereas
CC       isoform 5 counteracts the effects by competing for binding sites.
CC       Isoform 3 regulates the trafficking and surface expression of
CC       GRM5. Isoform 5 acts as a natural dominant negative, in dynamic
CC       competition with constitutively expressed isoform 1, isoform 2 and
CC       isoform 3 to regulate synaptic metabotropic glutamate function.
CC       Isoform 5, may be involved in the structural changes that occur at
CC       synapses during long-lasting neuronal plasticity and development
CC       (By similarity).
CC   -!- SUBUNIT: Interacts with OPHN1 (By similarity). Isoform 1, isoform
CC       2 and isoform 3 encode a coiled-coil structure that mediates homo-
CC       and heteromultimerization. Interacts with IFT57.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell junction, synapse,
CC       postsynaptic cell membrane, postsynaptic density. Cell junction,
CC       synapse. Note=Postsynaptic density of neuronal cells. Isoform 1
CC       inhibits surface expression of GRM5 causing it to be retained in
CC       the endoplasmic reticulum. The N-terminal of isoform 2 may
CC       facilitate trafficking of the complex with GRM5 from the
CC       endoplasmic reticulum (ER) to the plasma membrane (PM).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1; Synonyms=Vesl-1L;
CC         IsoId=Q9Z2Y3-1; Sequence=Displayed;
CC       Name=2; Synonyms=1d;
CC         IsoId=Q9Z2Y3-2; Sequence=VSP_009060, VSP_009061;
CC       Name=3; Synonyms=1b;
CC         IsoId=Q9Z2Y3-3; Sequence=VSP_009061;
CC       Name=4; Synonyms=Vesl-1M;
CC         IsoId=Q9Z2Y3-4; Sequence=VSP_009063, VSP_009065;
CC       Name=5; Synonyms=Vesl-1S;
CC         IsoId=Q9Z2Y3-5; Sequence=VSP_009062, VSP_009064;
CC   -!- TISSUE SPECIFICITY: Isoform 1, isoform 3 and isoform 5 are
CC       expressed in skeletal muscle at the level of the Z line, in heart,
CC       forebrain and cerebellum. Isoform 2, is a minor isoform and is
CC       expressed in cardiac and skeletal muscle. Isoform 5 is expressed
CC       in the postsynaptic region of neurons.
CC   -!- DOMAIN: The WH1 domain interacts with the PPXXF motif in GRM1,
CC       GRM5, RYR1, RYR2, ITPR1, SHANK 1 and SHANK3.
CC   -!- SIMILARITY: Belongs to the Homer family.
CC   -!- SIMILARITY: Contains 1 WH1 domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF093257; AAC71021.1; -; mRNA.
DR   EMBL; AF093258; AAC71022.1; -; mRNA.
DR   EMBL; AY137385; AAM95461.1; -; mRNA.
DR   EMBL; AB019478; BAA34353.1; -; mRNA.
DR   EMBL; AB019479; BAA34354.1; -; mRNA.
DR   EMBL; AB089435; BAC07257.1; -; mRNA.
DR   IPI; IPI00170191; -.
DR   IPI; IPI00172234; -.
DR   IPI; IPI00282945; -.
DR   IPI; IPI00323731; -.
DR   IPI; IPI00395134; -.
DR   RefSeq; NP_036112.1; NM_011982.2.
DR   RefSeq; NP_671705.2; NM_147176.2.
DR   RefSeq; NP_687036.1; NM_152134.2.
DR   UniGene; Mm.37533; -.
DR   ProteinModelPortal; Q9Z2Y3; -.
DR   SMR; Q9Z2Y3; 1-143, 302-364.
DR   MINT; MINT-3370083; -.
DR   STRING; Q9Z2Y3; -.
DR   TCDB; 8.A.29.1.1; Homer1 family of excitation-contraction coupling proteins.
DR   PhosphoSite; Q9Z2Y3; -.
DR   PRIDE; Q9Z2Y3; -.
DR   Ensembl; ENSMUST00000079086; ENSMUSP00000078093; ENSMUSG00000007617.
DR   Ensembl; ENSMUST00000080127; ENSMUSP00000079026; ENSMUSG00000007617.
DR   Ensembl; ENSMUST00000102752; ENSMUSP00000099813; ENSMUSG00000007617.
DR   GeneID; 26556; -.
DR   KEGG; mmu:26556; -.
DR   UCSC; uc007rlb.1; mouse.
DR   UCSC; uc007rlc.1; mouse.
DR   UCSC; uc007rld.1; mouse.
DR   UCSC; uc007rle.1; mouse.
DR   CTD; 26556; -.
DR   MGI; MGI:1347345; Homer1.
DR   GeneTree; ENSGT00390000017850; -.
DR   HOVERGEN; HBG051918; -.
DR   OMA; TSTPSQX; -.
DR   NextBio; 304603; -.
DR   ArrayExpress; Q9Z2Y3; -.
DR   Bgee; Q9Z2Y3; -.
DR   CleanEx; MM_HOMER1; -.
DR   Genevestigator; Q9Z2Y3; -.
DR   GermOnline; ENSMUSG00000007617; Mus musculus.
DR   GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR   GO; GO:0043034; C:costamere; IDA:MGI.
DR   GO; GO:0005624; C:membrane fraction; IDA:MGI.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030018; C:Z disc; IDA:MGI.
DR   GO; GO:0005515; F:protein binding; IPI:MGI.
DR   GO; GO:0007216; P:metabotropic glutamate receptor signaling pathway; TAS:MGI.
DR   GO; GO:0032236; P:positive regulation of calcium ion transport via store-operated calcium channel activity; IMP:MGI.
DR   GO; GO:0003009; P:skeletal muscle contraction; IMP:MGI.
DR   GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI.
DR   InterPro; IPR000697; EVH1.
DR   InterPro; IPR010356; Haemolysin_E.
DR   InterPro; IPR011993; PH_type.
DR   Gene3D; G3DSA:1.20.1170.10; Haemolysin_E; 1.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 1.
DR   Pfam; PF00568; WH1; 1.
DR   SMART; SM00461; WH1; 1.
DR   PROSITE; PS50229; WH1; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Coiled coil;
KW   Cytoplasm; Membrane; Postsynaptic cell membrane; Synapse.
FT   CHAIN         1    366       Homer protein homolog 1.
FT                                /FTId=PRO_0000191006.
FT   DOMAIN        1    110       WH1.
FT   COILED      193    364       Potential.
FT   VAR_SEQ       1      2       MG -> MLIHHHNRRALCKGSPTT (in isoform 2).
FT                                /FTId=VSP_009060.
FT   VAR_SEQ     176    187       Missing (in isoform 2 and isoform 3).
FT                                /FTId=VSP_009061.
FT   VAR_SEQ     176    186       SAGDRTQALSH -> RYTFNSAIMIK (in isoform
FT                                5).
FT                                /FTId=VSP_009062.
FT   VAR_SEQ     177    203       AGDRTQALSHASSAISKHWEAELATLK -> SSRWIFFPYC
FT                                EDSQLSLLESSSGLGYF (in isoform 4).
FT                                /FTId=VSP_009063.
FT   VAR_SEQ     187    366       Missing (in isoform 5).
FT                                /FTId=VSP_009064.
FT   VAR_SEQ     204    366       Missing (in isoform 4).
FT                                /FTId=VSP_009065.
FT   CONFLICT    193    193       K -> N (in Ref. 3; BAA34354).
FT   CONFLICT    197    197       A -> V (in Ref. 3; BAA34354).
FT   CONFLICT    205    205       N -> T (in Ref. 3; BAA34354).
SQ   SEQUENCE   366 AA;  41413 MW;  6A4CBCE5B8A91A3F CRC64;
     MGEQPIFSTR AHVFQIDPNT KKNWVPTSKH AVTVSYFYDS TRNVYRIISL DGSKAIINST
     ITPNMTFTKT SQKFGQWADS RANTVYGLGF SSEHHLSKFA EKFQEFKEAA RLAKEKSQEK
     MELTSTPSQE SAGGDLQSPL TPESINGTDD ERTPDVTQNS EPRAEPTQNA LPFPHSAGDR
     TQALSHASSA ISKHWEAELA TLKGNNAKLT AALLESTANV KQWKQQLAAY QEEAERLHKR
     VTELECVSSQ ANAVHSHKTE LNQTVQELEE TLKVKEEEIE RLKQEIDNAR ELQEQRDSLT
     QKLQEVEIRN KDLEGQLSDL EQRLEKSQNE QEAFRSNLKT LLEILDGKIF ELTELRDNLA
     KLLECS
//
ID   K1C27_MOUSE             Reviewed;         448 AA.
AC   Q9Z320;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 68.
DE   RecName: Full=Keratin, type I cytoskeletal 27;
DE   AltName: Full=Cytokeratin-27;
DE            Short=CK-27;
DE   AltName: Full=Keratin complex-1, acidic, gene C29;
DE   AltName: Full=Keratin-27;
DE            Short=K27;
DE   AltName: Full=Type I inner root sheath-specific keratin-K25irs3;
GN   Name=Krt27; Synonyms=c29, Krt1-c29;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/10J; TISSUE=Skin;
RX   MEDLINE=99189238; PubMed=10087197; DOI=10.1006/geno.1998.5721;
RA   Sato H., Koide T., Sagai T., Ishiguro S., Tamai M., Saitou N.,
RA   Shiroishi T.;
RT   "The genomic organization of type I keratin genes in mice.";
RL   Genomics 56:303-309(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF
RP   315-LYS--SER-388.
RC   STRAIN=C57BL/6J; TISSUE=Skin;
RX   PubMed=17920809; DOI=10.1016/j.ygeno.2007.07.013;
RA   Tanaka S., Miura I., Yoshiki A., Kato Y., Yokoyama H., Shinogi A.,
RA   Masuya H., Wakana S., Tamura M., Shiroishi T.;
RT   "Mutations in the helix termination motif of mouse type I IRS keratin
RT   genes impair the assembly of keratin intermediate filament.";
RL   Genomics 90:703-711(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=14996088; DOI=10.1111/j.1365-2133.2004.05720.x;
RA   Porter R.M., Gandhi M., Wilson N.J., Wood P., McLean W.H.I.,
RA   Lane E.B.;
RT   "Functional analysis of keratin components in the mouse hair follicle
RT   inner root sheath.";
RL   Br. J. Dermatol. 150:195-204(2004).
CC   -!- FUNCTION: Essential for the proper assembly of type I and type II
CC       keratin protein complexes and formation of keratin intermediate
CC       filaments in the inner root sheath (irs).
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC       Interacts with KRT6A to form filaments.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Expressed in skin. Expressed in the Henle
CC       layer and cuticle of the irs in hair follicle bulb. In the hair
CC       follicle, expression was observed in all layers of the irs but was
CC       stronger in the Henle layer and cuticle than the Huxley layer
CC       until the Henle layer differentiated (at protein level).
CC   -!- MISCELLANEOUS: There are two types of cytoskeletal and
CC       microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to
CC       basic; 56-70 kDa).
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB013607; BAA34228.1; -; mRNA.
DR   EMBL; AL590991; CAM18787.1; -; Genomic_DNA.
DR   IPI; IPI00131336; -.
DR   RefSeq; NP_034796.1; NM_010666.1.
DR   UniGene; Mm.440476; -.
DR   HSSP; P08670; 1GK7.
DR   ProteinModelPortal; Q9Z320; -.
DR   SMR; Q9Z320; 72-109, 125-226, 242-384.
DR   IntAct; Q9Z320; 1.
DR   STRING; Q9Z320; -.
DR   PhosphoSite; Q9Z320; -.
DR   PRIDE; Q9Z320; -.
DR   Ensembl; ENSMUST00000017732; ENSMUSP00000017732; ENSMUSG00000017588.
DR   GeneID; 16675; -.
DR   KEGG; mmu:16675; -.
DR   UCSC; uc007lip.1; mouse.
DR   CTD; 16675; -.
DR   MGI; MGI:1339999; Krt27.
DR   eggNOG; roNOG09726; -.
DR   GeneTree; ENSGT00560000077101; -.
DR   HOGENOM; HBG715391; -.
DR   HOVERGEN; HBG013015; -.
DR   InParanoid; Q9Z320; -.
DR   OMA; HQSVDAD; -.
DR   OrthoDB; EOG4RNB8M; -.
DR   PhylomeDB; Q9Z320; -.
DR   NextBio; 290413; -.
DR   ArrayExpress; Q9Z320; -.
DR   Bgee; Q9Z320; -.
DR   CleanEx; MM_KRT27; -.
DR   Genevestigator; Q9Z320; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
DR   InterPro; IPR016044; F.
DR   InterPro; IPR001664; IF.
DR   InterPro; IPR002957; Keratin_I.
DR   PANTHER; PTHR23239; IF; 1.
DR   Pfam; PF00038; Filament; 1.
DR   PRINTS; PR01248; TYPE1KERATIN.
DR   PROSITE; PS00226; IF; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Intermediate filament; Keratin.
FT   CHAIN         1    448       Keratin, type I cytoskeletal 27.
FT                                /FTId=PRO_0000312702.
FT   REGION        1     73       Head.
FT   REGION       74    385       Rod.
FT   REGION       74    109       Coil 1A.
FT   REGION      110    131       Linker 1.
FT   REGION      132    223       Coil 1B.
FT   REGION      224    246       Linker 12.
FT   REGION      247    385       Coil 2.
FT   REGION      386    448       Tail.
FT   COMPBIAS     21     60       Gly-rich.
FT   MUTAGEN     315    388       Missing: In Rex wavy coat; mice exhibit
FT                                curly hair and vibrissae. The diameter of
FT                                the hair shaft is irregular due to
FT                                morphological abnormalities in all three
FT                                layers of the irs.
SQ   SEQUENCE   448 AA;  49105 MW;  14CAF4EAC0828AEA CRC64;
     MSVRFSSASR RLGSVRLSSA GAALGAGNAC GVPGIGSGFS CAFGGSSLAG GLGMGGASCG
     AFTANEHGLL SGNEKVTMQN LNDRLASYLE NVQALEEANA DLEQKIKDWY EKFGPGSCRG
     LDHDYSRYFP IIDDLRTQII SATAHNANII LQNDNARLTA DDFRMKYENE LALHQSVDAD
     INGLRRVLDE LTLCRTDLEV QLETLSEELA YLKKNHEEEM QALQCAAGGN VNVEMNAAPG
     VDLTVLLNNM RAEYEALAEQ NRRDAEAWFQ EKSASLQQQI SDDAGATTSA RNELTEMKRT
     LQTLEIELQS LLAMKHSLEC SLTETEGNYC TQLAQIQAQI SALEEQLHQV RTETEGQKLE
     YEQLLNVKAH LEKEIETYCR LIDGDEGSCV KAKGQGRPGN QTKDSPKTAI VKTVVEELDP
     RGKVLSSRVH TLEEKSTKVN KTEQRIPS
//
ID   ITPR2_MOUSE             Reviewed;        2701 AA.
AC   Q9Z329; P70226; Q5DWM3; Q5DWM5; Q61744; Q8R3B0;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 3.
DT   08-MAR-2011, entry version 95.
DE   RecName: Full=Inositol 1,4,5-trisphosphate receptor type 2;
DE   AltName: Full=IP3 receptor isoform 2;
DE            Short=IP3R 2;
DE            Short=InsP3R2;
DE   AltName: Full=Inositol 1,4,5-trisphosphate type V receptor;
DE   AltName: Full=Type 2 inositol 1,4,5-trisphosphate receptor;
DE            Short=Type 2 InsP3 receptor;
GN   Name=Itpr2; Synonyms=Itpr5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, TISSUE
RP   SPECIFICITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-507 AND
RP   ARG-510.
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=15632133; DOI=10.1074/jbc.M413824200;
RA   Iwai M., Tateishi Y., Hattori M., Mizutani A., Nakamura T.,
RA   Futatsugi A., Inoue T., Furuichi T., Michikawa T., Mikoshiba K.;
RT   "Molecular cloning of mouse type 2 and type 3 inositol 1,4,5-
RT   trisphosphate receptors and identification of a novel type 2 receptor
RT   splice variant.";
RL   J. Biol. Chem. 280:10305-10317(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Heart;
RX   MEDLINE=98399819; PubMed=9729462;
RA   Futatsugi A., Kuwajima G., Mikoshiba K.;
RT   "Muscle-specific mRNA isoform encodes a protein composed mainly of the
RT   N-terminal 175 residues of type 2 Ins(1,4,5)P3 receptor.";
RL   Biochem. J. 334:559-563(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1290-2701.
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2238-2646 (ISOFORM 1).
RC   STRAIN=C3H; TISSUE=Embryo;
RX   MEDLINE=97218118; PubMed=9065779;
RA   De Smedt H., Missiaen L., Parys J.B., Henning R.H., Sienaert I.,
RA   Vanlingen S., Gijsens A., Himpens B., Casteels R.;
RT   "Isoform diversity of the inositol trisphosphate receptor in cell
RT   types of mouse origin.";
RL   Biochem. J. 322:575-583(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1693-2701 (ISOFORM 1).
RC   STRAIN=C3H; TISSUE=Embryo;
RX   MEDLINE=94342363; PubMed=8063813;
RA   De Smedt H., Missiaen L., Parys J.B., Bootman M.D., Mertens L.,
RA   Van Den Bosch L., Casteels R.;
RT   "Determination of relative amounts of inositol trisphosphate receptor
RT   mRNA isoforms by ratio polymerase chain reaction.";
RL   J. Biol. Chem. 269:21691-21698(1994).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1709, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Melanoma;
RX   PubMed=19367708; DOI=10.1021/pr800599n;
RA   Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,
RA   Faessler R., Mann M.;
RT   "Solid tumor proteome and phosphoproteome analysis by high resolution
RT   mass spectrometry.";
RL   J. Proteome Res. 7:5314-5326(2008).
CC   -!- FUNCTION: Receptor for inositol 1,4,5-trisphosphate, a second
CC       messenger that mediates the release of intracellular calcium.
CC       Isoform 3 has neither inositol 1,4,5-trisphosphate binding
CC       activity nor calcium releasing activity.
CC   -!- SUBUNIT: Homotetramer (By similarity). Interacts with CABP1 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=Long;
CC         IsoId=Q9Z329-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short, TIPR;
CC         IsoId=Q9Z329-2; Sequence=VSP_002701, VSP_002702;
CC       Name=3; Synonyms=Itpr2v;
CC         IsoId=Q9Z329-3; Sequence=VSP_016026;
CC   -!- TISSUE SPECIFICITY: Isoforms 1 and 3 are widely expressed. Isoform
CC       2 is found in skeletal muscle and heart.
CC   -!- DOMAIN: The receptor contains a calcium channel in its C-terminal
CC       extremity. Its large N-terminal cytoplasmic region has the ligand-
CC       binding site in the N-terminus and modulatory sites in the middle
CC       portion immediately upstream of the channel region.
CC   -!- PTM: Phosphorylated on tyrosine residues (By similarity).
CC   -!- SIMILARITY: Belongs to the InsP3 receptor family.
CC   -!- SIMILARITY: Contains 5 MIR domains.
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DR   EMBL; AB182288; BAD90682.1; -; mRNA.
DR   EMBL; AB182290; BAD90684.1; -; mRNA.
DR   EMBL; AB012393; BAA33960.1; -; mRNA.
DR   EMBL; BC025805; AAH25805.1; -; mRNA.
DR   EMBL; Z71173; CAA94861.1; -; mRNA.
DR   EMBL; Z33908; CAA83957.1; -; mRNA.
DR   IPI; IPI00222043; -.
DR   IPI; IPI00556814; -.
DR   IPI; IPI00896029; -.
DR   PIR; I48607; I48607.
DR   RefSeq; NP_034716.1; NM_010586.1.
DR   RefSeq; NP_064307.2; NM_019923.3.
DR   UniGene; Mm.393003; -.
DR   UniGene; Mm.7800; -.
DR   ProteinModelPortal; Q9Z329; -.
DR   SMR; Q9Z329; 5-602.
DR   STRING; Q9Z329; -.
DR   PhosphoSite; Q9Z329; -.
DR   PRIDE; Q9Z329; -.
DR   Ensembl; ENSMUST00000053273; ENSMUSP00000049584; ENSMUSG00000030287.
DR   Ensembl; ENSMUST00000079573; ENSMUSP00000078526; ENSMUSG00000030287.
DR   Ensembl; ENSMUST00000111674; ENSMUSP00000107303; ENSMUSG00000030287.
DR   GeneID; 16439; -.
DR   KEGG; mmu:16439; -.
DR   UCSC; uc009erw.1; mouse.
DR   UCSC; uc009erx.1; mouse.
DR   CTD; 16439; -.
DR   MGI; MGI:99418; Itpr2.
DR   GeneTree; ENSGT00600000084357; -.
DR   HOGENOM; HBG315164; -.
DR   HOVERGEN; HBG052158; -.
DR   InParanoid; Q9Z329; -.
DR   OrthoDB; EOG4GQQ42; -.
DR   NextBio; 289685; -.
DR   ArrayExpress; Q9Z329; -.
DR   Bgee; Q9Z329; -.
DR   CleanEx; MM_ITPR2; -.
DR   Genevestigator; Q9Z329; -.
DR   GermOnline; ENSMUSG00000030287; Mus musculus.
DR   GO; GO:0005938; C:cell cortex; IDA:MGI.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005792; C:microsome; IDA:MGI.
DR   GO; GO:0005220; F:inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IEA:InterPro.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IDA:MGI.
DR   InterPro; IPR000699; Ca-rel_channel.
DR   InterPro; IPR014821; Ins145_P3_rcpt.
DR   InterPro; IPR000493; InsP3_rcpt-bd.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003608; MIR.
DR   InterPro; IPR016093; MIR_motif.
DR   InterPro; IPR013662; RIH_assoc-dom.
DR   InterPro; IPR015925; Ryanodine_recept-rel.
DR   PANTHER; PTHR13715; Ryanodine_recept-rel; 1.
DR   Pfam; PF08709; Ins145_P3_rec; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF02815; MIR; 1.
DR   Pfam; PF08454; RIH_assoc; 1.
DR   Pfam; PF01365; RYDR_ITPR; 2.
DR   PRINTS; PR00779; INSP3RECEPTR.
DR   SMART; SM00472; MIR; 4.
DR   SUPFAM; SSF82109; MIR; 2.
DR   PROSITE; PS50919; MIR; 5.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Calcium; Calcium channel;
KW   Calcium transport; Endoplasmic reticulum; Ion transport;
KW   Ionic channel; Ligand-gated ion channel; Membrane; Phosphoprotein;
KW   Receptor; Repeat; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1   2701       Inositol 1,4,5-trisphosphate receptor
FT                                type 2.
FT                                /FTId=PRO_0000153925.
FT   TOPO_DOM      1   2227       Cytoplasmic (Potential).
FT   TRANSMEM   2228   2248       Helical; (Potential).
FT   TOPO_DOM   2249   2260       Extracellular (Potential).
FT   TRANSMEM   2261   2281       Helical; (Potential).
FT   TOPO_DOM   2282   2307       Cytoplasmic (Potential).
FT   TRANSMEM   2308   2328       Helical; (Potential).
FT   TOPO_DOM   2329   2351       Extracellular (Potential).
FT   TRANSMEM   2352   2372       Helical; (Potential).
FT   TOPO_DOM   2373   2394       Cytoplasmic (Potential).
FT   TRANSMEM   2395   2415       Helical; (Potential).
FT   TOPO_DOM   2416   2520       Extracellular (Potential).
FT   TRANSMEM   2521   2541       Helical; (Potential).
FT   TOPO_DOM   2542   2701       Cytoplasmic (Potential).
FT   DOMAIN      112    166       MIR 1.
FT   DOMAIN      173    223       MIR 2.
FT   DOMAIN      231    287       MIR 3.
FT   DOMAIN      294    372       MIR 4.
FT   DOMAIN      378    434       MIR 5.
FT   MOD_RES     608    608       N6-acetyllysine (By similarity).
FT   MOD_RES    1160   1160       Phosphoserine (By similarity).
FT   MOD_RES    1709   1709       Phosphoserine.
FT   MOD_RES    2607   2607       Phosphotyrosine (Potential).
FT   VAR_SEQ     175    175       N -> NDMGAVI (in isoform 2).
FT                                /FTId=VSP_002701.
FT   VAR_SEQ     176   1281       Missing (in isoform 2).
FT                                /FTId=VSP_002702.
FT   VAR_SEQ     176    208       Missing (in isoform 3).
FT                                /FTId=VSP_016026.
FT   MUTAGEN     507    507       K->A: Loss of binding activity.
FT   MUTAGEN     510    510       R->A: Loss of binding activity.
FT   CONFLICT   1710   1710       I -> V (in Ref. 3; AAH25805).
FT   CONFLICT   1729   1729       S -> G (in Ref. 3; AAH25805).
FT   CONFLICT   1738   1738       K -> T (in Ref. 3; AAH25805).
FT   CONFLICT   2196   2196       F -> L (in Ref. 5).
FT   CONFLICT   2223   2223       S -> P (in Ref. 3; AAH25805).
FT   CONFLICT   2265   2265       A -> V (in Ref. 1).
SQ   SEQUENCE   2701 AA;  307447 MW;  BC7FFF87E6872E61 CRC64;
     MSDKMSSFLY IGDIVSLYAE GSVNGFISTL GLVDDRCVVH PEAGDLANPP KKFRDCLFKV
     CPMNRYSAQK QYWKAKQAKQ GNHTEAALLK KLQHAAELEQ KQNESENRKL LGEIVKYSNV
     IQLLHIKSNK YLTVNKRLPA LLEKNAMRVS LDAAGNEGSW FYIHPFWKLR SEGDNIVVGD
     KVVLMPVNAG QPLHASNVEL LDNPGCKEVN AVNCNTSWKI TLFMKFSSYR EDVLKGGDVV
     RLFHAEQEKF LTCDDYEKKQ HIFLRTTLRQ SATSATSSKA LWEIEVVHHD PCRGGAGQWN
     SLFRFKHLAT GNYLAAELNP DYRDAQNEGK NVKDGEIPTP KKKRQAGEKI MYTLVSVPHG
     NDIASLFELD ATTLQRADCL VPRNSYVRLR HLCTNTWVTS TTIPIDTEEE RPVMLKIGTC
     QTKEDKEAFA IVCVPLSEVR DLDFANDANK VLATTVKKLE NGSITQNERR FVTKLLEDLI
     FFVADVTNNG QDVLDVVITK PNRERQKLMR EQNILAQVFG ILKAPFKEKA GEGSMLRLED
     LGDQRYAPYK YVLRLCYRVL RHSQQDYRKN QEYIAKNFCV MQSQIGYDIL AEDTITALLH
     NNRKLLEKHI TAKEIETFVS LLRRNREPRF LDYLSDLCVS NSTAIPVTQE LICKFMLSPG
     NADILIQTKL VSMQVENPME SSILPDDIDD EEVWLYWIDS NKEPHGKAIR HLAQEAREGT
     KADLEVLTYY RYQLNLFARM CLDRQYLAIN QISTQLSVDL ILRCVSDESL PFDLRASFCR
     LMLHMHVDRD PQESVVPVRY ARLWTEIPTK ITIHEYDSIT DSSRNDMKRK FALTMEFVEE
     YLKEVVNQPF PFGDKEKNKL TFEVVHLARN LIYFGFYSFS ELLRLTRTLL AILDIVQAPM
     SSYFERLSKF QDGSNNVMRT IHGVGEMMTQ MVLSRGSIFP VSVPDAQPIV HPSKQASPGE
     QEDVTVMDTK LKVIEILQFI LSVRLDYRIS YMLSIYKKEF GDNNDNGDPS ASGTPDTLLP
     SALVPDIDEI AAQAETMFAG RKEKTPVQLD DEGGRTFLRV LIHLIMHDYA PLLSGALQLL
     FKHFSQRAEV LQAFKQVQLL VSNQDVDNYK QIKADLDQLR LTVEKSELWV EKSGSYENGD
     VGEGQAKGGE EANEESNLLS PVQDGAKTPQ IDSNKGNNYR IVKEILIRLS KLCVQNKKCR
     NQHQRLLKNM GAHSVVLDLL QIPYEKTDEK MNEVMDLAHT FLQNFCRGNP QNQVLLHKHL
     NLFLTPGLLE AETMRHIFMN NYHLCNEISE RVVQHFVHCI ETHGRHVEYL RFLQTIVKAD
     GKYVKKCQDM VMTELINGGE DVLIFYNDRA SFPILLNMMC SERARGDESG PLAYHITLVE
     LLAACTEGKN VYTEIKCNSL LPLDDIVRVV THDDCIPEVK IAYVNFVNHC YVDTEVEMKE
     IYTSNHIWKL FENFLVDMAR VCNTTTDRKH ADTFLERCVT ESVMNIVSGF FNSPFSDNST
     SLQTHQPVFI QLLQSAFRIY NCTWPNPAQK ASVESCIRAL AEVAKNRGIA IPVDLDSQVN
     TLFMKNHSST VQRAAMGWRL SARSGPRFKE ALGGPAWDYR NIIEKLQDVV ASLEQQFSPM
     MQAEFSVLVD VLYSPELLFP EGSDARIRCG AFMSKLINHT KKLMEKEEKL CIKILQTLRE
     MLEKKDSFME EGSTLRRILL NRYFKGDHSI SVNGPLSGAY AKTAQVGGSF SGQDSDKKGI
     SMSDIQCLLD KEGASELVID VIVNTKNDRI FSEGILLGIA LLEGGNTQTQ YSFYQQLHEQ
     KKSEKFFKVL YDRMKAAQKE IRSTVTVNTI DLGSKKREED SDVMALGPRM RVRDSSLHLR
     EGMKGQLTEA SSATSKAYCV YRREMDPEID TMCPGQEAGS AEEKSAEEVT MSPAITIMRP
     ILRFLQLLCE NHNRELQNFL RNQNNKTNYN LVCETLQFLD CICGSTTGGL GLLGLYINER
     NVALVNQTLE SLTEYCQGPC HENQTCIATH ESNGIDIIIA LILNDINPLG KYRMDLVLQL
     KNNASKLLLA IMESRHDSEN AERILFNMRP RELVDVMKNA YNQGLECDHG DEEGGDDGVS
     PKDVGHNIYI LAHQLARHNK LLQQMLKPGS DPEEGDEALK YYANHTAQIE IVRHDRTMEQ
     IVFPVPNICE FLTRESKYRV FNTTERDEQG SKVNDFFQQT EDLYNEMKWQ KKIRNNPALF
     WFSRHISLWG SISFNLAVFI NLAVALFYPF GDDGDEGTLS PMFSALLWVA VAICTSMLFF
     FSKPVGIRPF LVSVMLRSIY TIGLGPTLIL LGAANLCNKI VFLVSFVGNR GTFTRGYRAV
     ILDMAFLYHV AYVLVCMLGL FVHEFFYSFL LFDLVYREET LLNVIKSVTR NGRSIILTAV
     LALILVYLFS IIGFLFLKDD FTMEVDRLKN RTPVTGNHGV PTMTLSSMME TCQKENCSPT
     IPSSNTAGEE GEDGIERTCD TLLMCIVTVL NQGLRNGGGV GDVLRRPSKD EPLFAARVVY
     DLLFFFIVII IVLNLIFGVI IDTFADLRSE KQKKEEILKT TCFICGLERD KFDNKTVSFE
     EHIKSEHNMW HYLYFIVLVK VKDPTEYTGP ESYVAQMITE KNLDWFPRMR AMSLVSNEGD
     SEQNEIRNLQ EKLESTMSLV KQLSGQLAEL KEQMTEQRKN KQRLGFLGSN TPHVNHHMPP
     H
//
ID   KCNQ2_MOUSE             Reviewed;         759 AA.
AC   Q9Z351; Q3UTI0; Q8R498; Q9QWN9; Q9Z342; Q9Z343; Q9Z344; Q9Z345;
AC   Q9Z346; Q9Z347; Q9Z348; Q9Z349; Q9Z350;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   08-MAR-2011, entry version 98.
DE   RecName: Full=Potassium voltage-gated channel subfamily KQT member 2;
DE   AltName: Full=KQT-like 2;
DE   AltName: Full=Potassium channel subunit alpha KvLQT2;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv7.2;
GN   Name=Kcnq2; Synonyms=Kqt2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9; 10 AND
RP   11).
RC   TISSUE=Brain;
RX   MEDLINE=98330948; PubMed=9666519;
RA   Nakamura M., Watanabe H., Kubo Y., Yokoyama M., Matsumoto T.,
RA   Sasai H., Nishi Y.;
RT   "KQT2, a new putative potassium channel family produced by alternative
RT   splicing. Isolation, genomic structure, and alternative splicing of
RT   the putative potassium channels.";
RL   Recept. Channels 5:255-271(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 12).
RC   STRAIN=BALB/c;
RX   PubMed=12223552;
RA   Wen H., Levitan I.B.;
RT   "Calmodulin is an auxiliary subunit of KCNQ2/3 potassium channels.";
RL   J. Neurosci. 22:7991-8001(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 58-759 (ISOFORM 13).
RC   STRAIN=C57BL/6J; TISSUE=Brain cortex;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   ROLE IN NEURAL HYPEREXCITABILITY.
RX   MEDLINE=20312851; PubMed=10854243;
RX   DOI=10.1046/j.1471-4159.2000.0750028.x;
RA   Watanabe H., Nagata E., Kosakai A., Nakamura M., Yokoyama M.,
RA   Tanaka K., Sasai H.;
RT   "Disruption of the epilepsy KCNQ2 gene results in neural
RT   hyperexcitability.";
RL   J. Neurochem. 75:28-33(2000).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438 AND SER-440, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Brain cortex;
RX   PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
RA   Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA   Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
RA   Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
RT   "Qualitative and quantitative analyses of protein phosphorylation in
RT   naive and stimulated mouse synaptosomal preparations.";
RL   Mol. Cell. Proteomics 6:283-293(2007).
CC   -!- FUNCTION: Probably important in the regulation of neuronal
CC       excitability. Associates with KCNQ3 to form a potassium channel
CC       with essentially identical properties to the channel underlying
CC       the native M-current, a slowly activating and deactivating
CC       potassium conductance which plays a critical role in determining
CC       the subthreshold electrical excitability of neurons as well as the
CC       responsiveness to synaptic inputs.
CC   -!- SUBUNIT: Heteromultimer with KCNQ3.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=13;
CC       Name=1; Synonyms=MKQT2.1;
CC         IsoId=Q9Z351-1; Sequence=Displayed;
CC       Name=2; Synonyms=MKQT2.2;
CC         IsoId=Q9Z351-2; Sequence=VSP_001001;
CC       Name=3; Synonyms=MKQT2.3;
CC         IsoId=Q9Z351-3; Sequence=VSP_001000;
CC       Name=4; Synonyms=MKQT2.4;
CC         IsoId=Q9Z351-4; Sequence=VSP_001002;
CC       Name=5; Synonyms=MKQT2.5;
CC         IsoId=Q9Z351-5; Sequence=VSP_001003, VSP_001004;
CC       Name=6; Synonyms=MKQT2.6;
CC         IsoId=Q9Z351-6; Sequence=VSP_001005, VSP_001006;
CC       Name=7; Synonyms=MKQT2.7;
CC         IsoId=Q9Z351-7; Sequence=VSP_000997, VSP_000998, VSP_000999;
CC       Name=8; Synonyms=MKQT2.8;
CC         IsoId=Q9Z351-8; Sequence=VSP_000998, VSP_000999;
CC       Name=9; Synonyms=MKQT2.9;
CC         IsoId=Q9Z351-9; Sequence=VSP_000993, VSP_000994;
CC       Name=10; Synonyms=MKQT2.10;
CC         IsoId=Q9Z351-10; Sequence=VSP_000995, VSP_000996;
CC       Name=11; Synonyms=MKQT2.11;
CC         IsoId=Q9Z351-11; Sequence=VSP_000991, VSP_000992;
CC       Name=12;
CC         IsoId=Q9Z351-12; Sequence=VSP_000997, VSP_012365, VSP_001002,
CC                                   VSP_012366;
CC       Name=13;
CC         IsoId=Q9Z351-13; Sequence=VSP_000997, VSP_022637, VSP_012366;
CC   -!- TISSUE SPECIFICITY: Exclusively expressed in the brain. Expressed
CC       in every neuron-containing regions of the central nervous system
CC       examined, such as the cerebellum, cerebral cortex, occipital pole,
CC       substantia nigra, amygdala, caudate nucleus, hippocampus and
CC       thalamus. Also detected in the cochlea.
CC   -!- DEVELOPMENTAL STAGE: Detected at day 11, 15 and 17 of the
CC       embryonic development. Expression increases by a factor of 2.5 at
CC       1 week after birth. Then the expression level remains stable until
CC       the adult stage. The mRNAs for shorter forms (isoforms 9, 10 and
CC       11) are specifically expressed in an embryo on the 11th day after
CC       gestation.
CC   -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC       characterized by a series of positively charged amino acids at
CC       every third position (By similarity).
CC   -!- SIMILARITY: Belongs to the potassium channel family. KQT
CC       (TC 1.A.1.15) subfamily. Kv7.2/KCNQ2 sub-subfamily.
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DR   EMBL; AB000494; BAA37156.1; -; mRNA.
DR   EMBL; AB000495; BAA37157.1; -; mRNA.
DR   EMBL; AB000496; BAA37158.1; -; mRNA.
DR   EMBL; AB000497; BAA37159.1; -; mRNA.
DR   EMBL; AB000498; BAA37160.1; -; mRNA.
DR   EMBL; AB000499; BAA37161.1; -; mRNA.
DR   EMBL; AB000500; BAA37162.1; -; mRNA.
DR   EMBL; AB000501; BAA37163.1; -; mRNA.
DR   EMBL; AB000502; BAA37164.1; -; mRNA.
DR   EMBL; AB000503; BAA37165.1; -; mRNA.
DR   EMBL; AB000504; BAA37166.1; -; mRNA.
DR   EMBL; AF490773; AAM09696.1; -; mRNA.
DR   EMBL; AK139411; BAE24000.1; -; mRNA.
DR   IPI; IPI00227840; -.
DR   IPI; IPI00229672; -.
DR   IPI; IPI00229673; -.
DR   IPI; IPI00229676; -.
DR   IPI; IPI00229677; -.
DR   IPI; IPI00229678; -.
DR   IPI; IPI00229679; -.
DR   IPI; IPI00230658; -.
DR   IPI; IPI00230659; -.
DR   IPI; IPI00463003; -.
DR   IPI; IPI00474530; -.
DR   IPI; IPI00751435; -.
DR   IPI; IPI00922989; -.
DR   RefSeq; NP_001003824.1; NM_001003824.1.
DR   RefSeq; NP_001003825.1; NM_001003825.2.
DR   RefSeq; NP_001006669.1; NM_001006668.1.
DR   RefSeq; NP_001006670.1; NM_001006669.1.
DR   RefSeq; NP_001006675.1; NM_001006674.1.
DR   RefSeq; NP_001006676.1; NM_001006675.1.
DR   RefSeq; NP_001006677.1; NM_001006676.1.
DR   RefSeq; NP_001006678.1; NM_001006677.1.
DR   RefSeq; NP_001006679.1; NM_001006678.1.
DR   RefSeq; NP_001006680.1; NM_001006679.1.
DR   RefSeq; NP_001006681.1; NM_001006680.1.
DR   RefSeq; NP_034741.2; NM_010611.2.
DR   UniGene; Mm.40615; -.
DR   UniGene; Mm.440175; -.
DR   ProteinModelPortal; Q9Z351; -.
DR   SMR; Q9Z351; 93-343, 624-653.
DR   STRING; Q9Z351; -.
DR   PhosphoSite; Q9Z351; -.
DR   PRIDE; Q9Z351; -.
DR   Ensembl; ENSMUST00000016491; ENSMUSP00000016491; ENSMUSG00000016346.
DR   Ensembl; ENSMUST00000049792; ENSMUSP00000052453; ENSMUSG00000016346.
DR   Ensembl; ENSMUST00000072952; ENSMUSP00000072721; ENSMUSG00000089863.
DR   Ensembl; ENSMUST00000080022; ENSMUSP00000078934; ENSMUSG00000089747.
DR   Ensembl; ENSMUST00000081528; ENSMUSP00000080243; ENSMUSG00000016346.
DR   Ensembl; ENSMUST00000103047; ENSMUSP00000099336; ENSMUSG00000016346.
DR   Ensembl; ENSMUST00000103048; ENSMUSP00000099337; ENSMUSG00000016346.
DR   Ensembl; ENSMUST00000103049; ENSMUSP00000099338; ENSMUSG00000016346.
DR   GeneID; 16536; -.
DR   KEGG; mmu:16536; -.
DR   UCSC; uc008okr.1; mouse.
DR   UCSC; uc008oks.1; mouse.
DR   UCSC; uc008okt.1; mouse.
DR   UCSC; uc008oku.1; mouse.
DR   UCSC; uc008okv.1; mouse.
DR   UCSC; uc008okz.1; mouse.
DR   UCSC; uc008olb.1; mouse.
DR   UCSC; uc008olc.1; mouse.
DR   UCSC; uc008old.1; mouse.
DR   UCSC; uc008ole.1; mouse.
DR   UCSC; uc008olf.1; mouse.
DR   UCSC; uc008olg.1; mouse.
DR   CTD; 16536; -.
DR   MGI; MGI:1309503; Kcnq2.
DR   eggNOG; maNOG05901; -.
DR   GeneTree; ENSGT00550000074513; -.
DR   HOVERGEN; HBG059014; -.
DR   OrthoDB; EOG41VK29; -.
DR   NextBio; 289965; -.
DR   ArrayExpress; Q9Z351; -.
DR   Bgee; Q9Z351; -.
DR   Genevestigator; Q9Z351; -.
DR   GermOnline; ENSMUSG00000016346; Mus musculus.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   InterPro; IPR005821; Ion_trans.
DR   InterPro; IPR003091; K_chnl.
DR   InterPro; IPR003937; K_chnl_volt-dep_KCNQ.
DR   InterPro; IPR003947; K_chnl_volt-dep_KCNQ2.
DR   InterPro; IPR013821; K_chnl_volt-dep_KCNQ_C.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF03520; KCNQ_channel; 2.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01461; KCNQ2CHANNEL.
DR   PRINTS; PR01459; KCNQCHANNEL.
PE   1: Evidence at protein level;
KW   Alternative splicing; Ion transport; Ionic channel; Membrane;
KW   Phosphoprotein; Potassium; Potassium channel; Potassium transport;
KW   Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1    759       Potassium voltage-gated channel subfamily
FT                                KQT member 2.
FT                                /FTId=PRO_0000054031.
FT   TRANSMEM     92    112       Helical; Name=Segment S1; (Potential).
FT   TOPO_DOM    113    122       Extracellular (Potential).
FT   TRANSMEM    123    143       Helical; Name=Segment S2; (Potential).
FT   TOPO_DOM    144    166       Cytoplasmic (Potential).
FT   TRANSMEM    167    187       Helical; Name=Segment S3; (Potential).
FT   TOPO_DOM    188    197       Extracellular (Potential).
FT   TRANSMEM    198    221       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TOPO_DOM    222    231       Cytoplasmic (Potential).
FT   TRANSMEM    232    252       Helical; Name=Segment S5; (Potential).
FT   TOPO_DOM    253    264       Extracellular (Potential).
FT   INTRAMEM    265    285       Pore-forming; Name=Segment H5;
FT                                (Potential).
FT   TOPO_DOM    286    291       Extracellular (Potential).
FT   TRANSMEM    292    312       Helical; Name=Segment S6; (Potential).
FT   TOPO_DOM    313    759       Cytoplasmic (Potential).
FT   MOTIF       277    282       Selectivity filter (By similarity).
FT   MOD_RES      52     52       Phosphoserine; by PKA (By similarity).
FT   MOD_RES     438    438       Phosphoserine.
FT   MOD_RES     440    440       Phosphoserine.
FT   VAR_SEQ     310    338       GILGSGFALKVQEQHRPKHFEKRRNPAAG -> VSPAHLPT
FT                                LEMLGVLEAPHKAWPWPTCEL (in isoform 11).
FT                                /FTId=VSP_000991.
FT   VAR_SEQ     339    759       Missing (in isoform 11).
FT                                /FTId=VSP_000992.
FT   VAR_SEQ     342    349       SAWRFYAT -> GQVRCAGH (in isoform 9).
FT                                /FTId=VSP_000993.
FT   VAR_SEQ     342    347       SAWRFY -> VSLSPC (in isoform 10).
FT                                /FTId=VSP_000995.
FT   VAR_SEQ     348    759       Missing (in isoform 10).
FT                                /FTId=VSP_000996.
FT   VAR_SEQ     350    759       Missing (in isoform 9).
FT                                /FTId=VSP_000994.
FT   VAR_SEQ     372    372       Y -> YSSQTQTYGAS (in isoform 7, isoform
FT                                12 and isoform 13).
FT                                /FTId=VSP_000997.
FT   VAR_SEQ     406    463       SQKVSLKDRVFSSPRGMAAKGKGSPQAQTVRRSPSADQSLD
FT                                DSPSKVPKSWSFGDRSR -> RSVPPASSRPGVCCTHLALL
FT                                SLCIHHVSWGRATMGPCVCFYVQQVTVCPGTPRVTSQL
FT                                (in isoform 7 and isoform 8).
FT                                /FTId=VSP_000998.
FT   VAR_SEQ     406    406       S -> SKGRPCRGCLCGCCPGHSS (in isoform 12).
FT                                /FTId=VSP_012365.
FT   VAR_SEQ     407    418       Missing (in isoform 3).
FT                                /FTId=VSP_001000.
FT   VAR_SEQ     464    759       Missing (in isoform 7 and isoform 8).
FT                                /FTId=VSP_000999.
FT   VAR_SEQ     562    623       IDMIVGPPPPSTPRDKKYPTKGPTAPSRESPQYSPRVDHIV
FT                                GRGPTITDKDRTKGPAETELP -> QEPLPVQSGHEQGPPG
FT                                QNQAWHKGHQGLGDRCAEQGQYQLWRSLPTLLASCCFLLCF
FT                                HTVCF (in isoform 6).
FT                                /FTId=VSP_001005.
FT   VAR_SEQ     562    597       Missing (in isoform 4 and isoform 12).
FT                                /FTId=VSP_001002.
FT   VAR_SEQ     562    596       IDMIVGPPPPSTPRDKKYPTKGPTAPSRESPQYSP -> QE
FT                                PLPVQSGHEQGPPGQNQAWHKGHQGLGD (in isoform
FT                                2).
FT                                /FTId=VSP_001001.
FT   VAR_SEQ     562    570       IDMIVGPPP -> SCDWRGVLA (in isoform 5).
FT                                /FTId=VSP_001003.
FT   VAR_SEQ     571    759       Missing (in isoform 5).
FT                                /FTId=VSP_001004.
FT   VAR_SEQ     571    606       Missing (in isoform 13).
FT                                /FTId=VSP_022637.
FT   VAR_SEQ     624    759       Missing (in isoform 6).
FT                                /FTId=VSP_001006.
FT   VAR_SEQ     747    759       LRLERSAGMMSCH -> RIPPPPAHERSLSAYGGGNRASTE
FT                                FLRLEGTPACRPSEAALRDSDTSISIPSVDHEELERSFSGF
FT                                SISQSKENLDALGSCYAAVAPCAKVRPYIAEGESDTDSDLC
FT                                TPCGPPPRSATGEGPFGDVAWAGPRK (in isoform 12
FT                                and isoform 13).
FT                                /FTId=VSP_012366.
FT   CONFLICT    125    125       A -> P (in Ref. 1; BAA37161).
FT   CONFLICT    326    326       P -> Q (in Ref. 1; BAA37160/BAA37165 and
FT                                2; AAM09696).
FT   CONFLICT    600    600       H -> Q (in Ref. 2; AAM09696).
SQ   SEQUENCE   759 AA;  84450 MW;  C1D12DBFF3979D3F CRC64;
     MVQKSRNGGV YPGTSGEKKL KVGFVGLDPG APDSTRDGAL LIAGSEAPKR GSVLSKPRTG
     GAGAGKPPKR NAFYRKLQNF LYNVLERPRG WAFIYHAYVF LLVFSCLVLS VFSTIKEYEK
     SSEGALYILE IVTIVVFGVE YFVRIWAAGC CCRYRGWRGR LKFARKPFCV IDIMVLIASI
     AVLAAGSQGN VFATSALRSL RFLQILRMIR MDRRGGTWKL LGSVVYAHSK ELVTAWYIGF
     LCLILASFLV YLAEKGENDH FDTYADALWW GLITLTTIGY GDKYPQTWNG RLLAATFTLI
     GVSFFALPAG ILGSGFALKV QEQHRPKHFE KRRNPAAGLI QSAWRFYATN LSRTDLHSTW
     QYYERTVTVP MYRLIPPLNQ LELLRNLKSK SGLTFRKEPQ PEPSPSQKVS LKDRVFSSPR
     GMAAKGKGSP QAQTVRRSPS ADQSLDDSPS KVPKSWSFGD RSRTRQAFRI KGAASRQNSE
     EASLPGEDIV EDNKSCNCEF VTEDLTPGLK VSIRAVCVMR FLVSKRKFKE SLRPYDVMDV
     IEQYSAGHLD MLSRIKSLQS RIDMIVGPPP PSTPRDKKYP TKGPTAPSRE SPQYSPRVDH
     IVGRGPTITD KDRTKGPAET ELPEDPSMMG RLGKVEKQVL SMEKKLDFLV SIYTQRMGIP
     PAETEAYFGA KEPEPAPPYH SPEDSRDHAD KHGCIIKIVR STSSTGQRNY AAPPAIPPAQ
     CPPSTSWQQS HQRHGTSPVG DHGSLVLRLE RSAGMMSCH
//
